data_8ZTK
# 
_entry.id   8ZTK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8ZTK         pdb_00008ztk 10.2210/pdb8ztk/pdb 
WWPDB D_1300047441 ?            ?                   
EMDB  EMD-60465    ?            ?                   
# 
_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       2025-03-12 
_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                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZTK 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'AtALMT9 with LMNG (cis2 class)' 
_pdbx_database_related.db_id          EMD-60465 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sangholee@skku.edu 
_pdbx_contact_author.name_first         Sangho 
_pdbx_contact_author.name_last          Lee 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7492-1043 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lee, Y.' 1 0000-0002-7492-1043 
'Lee, S.' 2 0000-0003-3886-4579 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1817 
_citation.page_last                 1817 
_citation.title                     
'Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-56940-5 
_citation.pdbx_database_id_PubMed   39979303 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, Y.'          1  0000-0002-7492-1043 
primary 'Demes-Causse, E.' 2  ?                   
primary 'Yoo, J.'          3  0009-0001-0008-8378 
primary 'Jang, S.Y.'       4  0000-0002-1529-2427 
primary 'Jung, S.'         5  0009-0000-1471-6876 
primary 'Jaslan, J.'       6  0000-0002-1620-912X 
primary 'Hwang, G.S.'      7  0000-0002-1600-1556 
primary 'Yoo, J.'          8  ?                   
primary 'De Angeli, A.'    9  0000-0003-3072-7932 
primary 'Lee, S.'          10 0000-0003-3886-4579 
# 
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 'Aluminum-activated malate transporter 9'                         67121.008 2 ? ? ? ? 
2 non-polymer syn '2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE' 648.891   2 ? ? ? ? 
3 water       nat water                                                             18.015    3 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        AtALMT9 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAAKQGSFRHGILEKRERLLSNNGFSDFRFTDIESNDLLENENCGRRTRLCCCCSCGNLSEKISGVYDDAKDVARKAWEM
GVSDPRKIVFSAKIGLALTIVALLIFYQEPNPDLSRYSVWAILTVVVVFEFTIGATLSKGFNRALGTLSAGGLALGMAEL
STLFGDWEEIFCTLSIFCIGFLATFMKLYPSMKAYEYGFRVFLLTYCYILISGFRTGQFIEVAISRFLLIALGAGVSLGV
NMFIYPIWAGEDLHNLVVKNFMNVATSLEGCVNGYLRCLEYERIPSKILTYQASEDPVYKGYRSAVESTSQEESLMSFAI
WEPPHGPYKSFNYPWKNYVKLSGALKHCAFTVMALHGCILSEIQAPEERRQVFRQELQRVGVEGAKLLRELGEKVKKMEK
LGPVDLLFEVHLAAEELQHKIDKKSYLLVNSECWEIGNRATKESEPQELLSLEDSDPPENHAPPIYAFKSLSEAVLEIPP
SWGEKNHREALNHRPTFSKQVSWPARLVLPPHLETTNGASPLVETTKTYESASALSLATFASLLIEFVARLQNVVDAFKE
LSQKANFKEPEIVTTGTDVEFSGERVGLGQKIRRCFGM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAAKQGSFRHGILEKRERLLSNNGFSDFRFTDIESNDLLENENCGRRTRLCCCCSCGNLSEKISGVYDDAKDVARKAWEM
GVSDPRKIVFSAKIGLALTIVALLIFYQEPNPDLSRYSVWAILTVVVVFEFTIGATLSKGFNRALGTLSAGGLALGMAEL
STLFGDWEEIFCTLSIFCIGFLATFMKLYPSMKAYEYGFRVFLLTYCYILISGFRTGQFIEVAISRFLLIALGAGVSLGV
NMFIYPIWAGEDLHNLVVKNFMNVATSLEGCVNGYLRCLEYERIPSKILTYQASEDPVYKGYRSAVESTSQEESLMSFAI
WEPPHGPYKSFNYPWKNYVKLSGALKHCAFTVMALHGCILSEIQAPEERRQVFRQELQRVGVEGAKLLRELGEKVKKMEK
LGPVDLLFEVHLAAEELQHKIDKKSYLLVNSECWEIGNRATKESEPQELLSLEDSDPPENHAPPIYAFKSLSEAVLEIPP
SWGEKNHREALNHRPTFSKQVSWPARLVLPPHLETTNGASPLVETTKTYESASALSLATFASLLIEFVARLQNVVDAFKE
LSQKANFKEPEIVTTGTDVEFSGERVGLGQKIRRCFGM
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE' LPP 
3 water                                                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   ALA n 
1 4   LYS n 
1 5   GLN n 
1 6   GLY n 
1 7   SER n 
1 8   PHE n 
1 9   ARG n 
1 10  HIS n 
1 11  GLY n 
1 12  ILE n 
1 13  LEU n 
1 14  GLU n 
1 15  LYS n 
1 16  ARG n 
1 17  GLU n 
1 18  ARG n 
1 19  LEU n 
1 20  LEU n 
1 21  SER n 
1 22  ASN n 
1 23  ASN n 
1 24  GLY n 
1 25  PHE n 
1 26  SER n 
1 27  ASP n 
1 28  PHE n 
1 29  ARG n 
1 30  PHE n 
1 31  THR n 
1 32  ASP n 
1 33  ILE n 
1 34  GLU n 
1 35  SER n 
1 36  ASN n 
1 37  ASP n 
1 38  LEU n 
1 39  LEU n 
1 40  GLU n 
1 41  ASN n 
1 42  GLU n 
1 43  ASN n 
1 44  CYS n 
1 45  GLY n 
1 46  ARG n 
1 47  ARG n 
1 48  THR n 
1 49  ARG n 
1 50  LEU n 
1 51  CYS n 
1 52  CYS n 
1 53  CYS n 
1 54  CYS n 
1 55  SER n 
1 56  CYS n 
1 57  GLY n 
1 58  ASN n 
1 59  LEU n 
1 60  SER n 
1 61  GLU n 
1 62  LYS n 
1 63  ILE n 
1 64  SER n 
1 65  GLY n 
1 66  VAL n 
1 67  TYR n 
1 68  ASP n 
1 69  ASP n 
1 70  ALA n 
1 71  LYS n 
1 72  ASP n 
1 73  VAL n 
1 74  ALA n 
1 75  ARG n 
1 76  LYS n 
1 77  ALA n 
1 78  TRP n 
1 79  GLU n 
1 80  MET n 
1 81  GLY n 
1 82  VAL n 
1 83  SER n 
1 84  ASP n 
1 85  PRO n 
1 86  ARG n 
1 87  LYS n 
1 88  ILE n 
1 89  VAL n 
1 90  PHE n 
1 91  SER n 
1 92  ALA n 
1 93  LYS n 
1 94  ILE n 
1 95  GLY n 
1 96  LEU n 
1 97  ALA n 
1 98  LEU n 
1 99  THR n 
1 100 ILE n 
1 101 VAL n 
1 102 ALA n 
1 103 LEU n 
1 104 LEU n 
1 105 ILE n 
1 106 PHE n 
1 107 TYR n 
1 108 GLN n 
1 109 GLU n 
1 110 PRO n 
1 111 ASN n 
1 112 PRO n 
1 113 ASP n 
1 114 LEU n 
1 115 SER n 
1 116 ARG n 
1 117 TYR n 
1 118 SER n 
1 119 VAL n 
1 120 TRP n 
1 121 ALA n 
1 122 ILE n 
1 123 LEU n 
1 124 THR n 
1 125 VAL n 
1 126 VAL n 
1 127 VAL n 
1 128 VAL n 
1 129 PHE n 
1 130 GLU n 
1 131 PHE n 
1 132 THR n 
1 133 ILE n 
1 134 GLY n 
1 135 ALA n 
1 136 THR n 
1 137 LEU n 
1 138 SER n 
1 139 LYS n 
1 140 GLY n 
1 141 PHE n 
1 142 ASN n 
1 143 ARG n 
1 144 ALA n 
1 145 LEU n 
1 146 GLY n 
1 147 THR n 
1 148 LEU n 
1 149 SER n 
1 150 ALA n 
1 151 GLY n 
1 152 GLY n 
1 153 LEU n 
1 154 ALA n 
1 155 LEU n 
1 156 GLY n 
1 157 MET n 
1 158 ALA n 
1 159 GLU n 
1 160 LEU n 
1 161 SER n 
1 162 THR n 
1 163 LEU n 
1 164 PHE n 
1 165 GLY n 
1 166 ASP n 
1 167 TRP n 
1 168 GLU n 
1 169 GLU n 
1 170 ILE n 
1 171 PHE n 
1 172 CYS n 
1 173 THR n 
1 174 LEU n 
1 175 SER n 
1 176 ILE n 
1 177 PHE n 
1 178 CYS n 
1 179 ILE n 
1 180 GLY n 
1 181 PHE n 
1 182 LEU n 
1 183 ALA n 
1 184 THR n 
1 185 PHE n 
1 186 MET n 
1 187 LYS n 
1 188 LEU n 
1 189 TYR n 
1 190 PRO n 
1 191 SER n 
1 192 MET n 
1 193 LYS n 
1 194 ALA n 
1 195 TYR n 
1 196 GLU n 
1 197 TYR n 
1 198 GLY n 
1 199 PHE n 
1 200 ARG n 
1 201 VAL n 
1 202 PHE n 
1 203 LEU n 
1 204 LEU n 
1 205 THR n 
1 206 TYR n 
1 207 CYS n 
1 208 TYR n 
1 209 ILE n 
1 210 LEU n 
1 211 ILE n 
1 212 SER n 
1 213 GLY n 
1 214 PHE n 
1 215 ARG n 
1 216 THR n 
1 217 GLY n 
1 218 GLN n 
1 219 PHE n 
1 220 ILE n 
1 221 GLU n 
1 222 VAL n 
1 223 ALA n 
1 224 ILE n 
1 225 SER n 
1 226 ARG n 
1 227 PHE n 
1 228 LEU n 
1 229 LEU n 
1 230 ILE n 
1 231 ALA n 
1 232 LEU n 
1 233 GLY n 
1 234 ALA n 
1 235 GLY n 
1 236 VAL n 
1 237 SER n 
1 238 LEU n 
1 239 GLY n 
1 240 VAL n 
1 241 ASN n 
1 242 MET n 
1 243 PHE n 
1 244 ILE n 
1 245 TYR n 
1 246 PRO n 
1 247 ILE n 
1 248 TRP n 
1 249 ALA n 
1 250 GLY n 
1 251 GLU n 
1 252 ASP n 
1 253 LEU n 
1 254 HIS n 
1 255 ASN n 
1 256 LEU n 
1 257 VAL n 
1 258 VAL n 
1 259 LYS n 
1 260 ASN n 
1 261 PHE n 
1 262 MET n 
1 263 ASN n 
1 264 VAL n 
1 265 ALA n 
1 266 THR n 
1 267 SER n 
1 268 LEU n 
1 269 GLU n 
1 270 GLY n 
1 271 CYS n 
1 272 VAL n 
1 273 ASN n 
1 274 GLY n 
1 275 TYR n 
1 276 LEU n 
1 277 ARG n 
1 278 CYS n 
1 279 LEU n 
1 280 GLU n 
1 281 TYR n 
1 282 GLU n 
1 283 ARG n 
1 284 ILE n 
1 285 PRO n 
1 286 SER n 
1 287 LYS n 
1 288 ILE n 
1 289 LEU n 
1 290 THR n 
1 291 TYR n 
1 292 GLN n 
1 293 ALA n 
1 294 SER n 
1 295 GLU n 
1 296 ASP n 
1 297 PRO n 
1 298 VAL n 
1 299 TYR n 
1 300 LYS n 
1 301 GLY n 
1 302 TYR n 
1 303 ARG n 
1 304 SER n 
1 305 ALA n 
1 306 VAL n 
1 307 GLU n 
1 308 SER n 
1 309 THR n 
1 310 SER n 
1 311 GLN n 
1 312 GLU n 
1 313 GLU n 
1 314 SER n 
1 315 LEU n 
1 316 MET n 
1 317 SER n 
1 318 PHE n 
1 319 ALA n 
1 320 ILE n 
1 321 TRP n 
1 322 GLU n 
1 323 PRO n 
1 324 PRO n 
1 325 HIS n 
1 326 GLY n 
1 327 PRO n 
1 328 TYR n 
1 329 LYS n 
1 330 SER n 
1 331 PHE n 
1 332 ASN n 
1 333 TYR n 
1 334 PRO n 
1 335 TRP n 
1 336 LYS n 
1 337 ASN n 
1 338 TYR n 
1 339 VAL n 
1 340 LYS n 
1 341 LEU n 
1 342 SER n 
1 343 GLY n 
1 344 ALA n 
1 345 LEU n 
1 346 LYS n 
1 347 HIS n 
1 348 CYS n 
1 349 ALA n 
1 350 PHE n 
1 351 THR n 
1 352 VAL n 
1 353 MET n 
1 354 ALA n 
1 355 LEU n 
1 356 HIS n 
1 357 GLY n 
1 358 CYS n 
1 359 ILE n 
1 360 LEU n 
1 361 SER n 
1 362 GLU n 
1 363 ILE n 
1 364 GLN n 
1 365 ALA n 
1 366 PRO n 
1 367 GLU n 
1 368 GLU n 
1 369 ARG n 
1 370 ARG n 
1 371 GLN n 
1 372 VAL n 
1 373 PHE n 
1 374 ARG n 
1 375 GLN n 
1 376 GLU n 
1 377 LEU n 
1 378 GLN n 
1 379 ARG n 
1 380 VAL n 
1 381 GLY n 
1 382 VAL n 
1 383 GLU n 
1 384 GLY n 
1 385 ALA n 
1 386 LYS n 
1 387 LEU n 
1 388 LEU n 
1 389 ARG n 
1 390 GLU n 
1 391 LEU n 
1 392 GLY n 
1 393 GLU n 
1 394 LYS n 
1 395 VAL n 
1 396 LYS n 
1 397 LYS n 
1 398 MET n 
1 399 GLU n 
1 400 LYS n 
1 401 LEU n 
1 402 GLY n 
1 403 PRO n 
1 404 VAL n 
1 405 ASP n 
1 406 LEU n 
1 407 LEU n 
1 408 PHE n 
1 409 GLU n 
1 410 VAL n 
1 411 HIS n 
1 412 LEU n 
1 413 ALA n 
1 414 ALA n 
1 415 GLU n 
1 416 GLU n 
1 417 LEU n 
1 418 GLN n 
1 419 HIS n 
1 420 LYS n 
1 421 ILE n 
1 422 ASP n 
1 423 LYS n 
1 424 LYS n 
1 425 SER n 
1 426 TYR n 
1 427 LEU n 
1 428 LEU n 
1 429 VAL n 
1 430 ASN n 
1 431 SER n 
1 432 GLU n 
1 433 CYS n 
1 434 TRP n 
1 435 GLU n 
1 436 ILE n 
1 437 GLY n 
1 438 ASN n 
1 439 ARG n 
1 440 ALA n 
1 441 THR n 
1 442 LYS n 
1 443 GLU n 
1 444 SER n 
1 445 GLU n 
1 446 PRO n 
1 447 GLN n 
1 448 GLU n 
1 449 LEU n 
1 450 LEU n 
1 451 SER n 
1 452 LEU n 
1 453 GLU n 
1 454 ASP n 
1 455 SER n 
1 456 ASP n 
1 457 PRO n 
1 458 PRO n 
1 459 GLU n 
1 460 ASN n 
1 461 HIS n 
1 462 ALA n 
1 463 PRO n 
1 464 PRO n 
1 465 ILE n 
1 466 TYR n 
1 467 ALA n 
1 468 PHE n 
1 469 LYS n 
1 470 SER n 
1 471 LEU n 
1 472 SER n 
1 473 GLU n 
1 474 ALA n 
1 475 VAL n 
1 476 LEU n 
1 477 GLU n 
1 478 ILE n 
1 479 PRO n 
1 480 PRO n 
1 481 SER n 
1 482 TRP n 
1 483 GLY n 
1 484 GLU n 
1 485 LYS n 
1 486 ASN n 
1 487 HIS n 
1 488 ARG n 
1 489 GLU n 
1 490 ALA n 
1 491 LEU n 
1 492 ASN n 
1 493 HIS n 
1 494 ARG n 
1 495 PRO n 
1 496 THR n 
1 497 PHE n 
1 498 SER n 
1 499 LYS n 
1 500 GLN n 
1 501 VAL n 
1 502 SER n 
1 503 TRP n 
1 504 PRO n 
1 505 ALA n 
1 506 ARG n 
1 507 LEU n 
1 508 VAL n 
1 509 LEU n 
1 510 PRO n 
1 511 PRO n 
1 512 HIS n 
1 513 LEU n 
1 514 GLU n 
1 515 THR n 
1 516 THR n 
1 517 ASN n 
1 518 GLY n 
1 519 ALA n 
1 520 SER n 
1 521 PRO n 
1 522 LEU n 
1 523 VAL n 
1 524 GLU n 
1 525 THR n 
1 526 THR n 
1 527 LYS n 
1 528 THR n 
1 529 TYR n 
1 530 GLU n 
1 531 SER n 
1 532 ALA n 
1 533 SER n 
1 534 ALA n 
1 535 LEU n 
1 536 SER n 
1 537 LEU n 
1 538 ALA n 
1 539 THR n 
1 540 PHE n 
1 541 ALA n 
1 542 SER n 
1 543 LEU n 
1 544 LEU n 
1 545 ILE n 
1 546 GLU n 
1 547 PHE n 
1 548 VAL n 
1 549 ALA n 
1 550 ARG n 
1 551 LEU n 
1 552 GLN n 
1 553 ASN n 
1 554 VAL n 
1 555 VAL n 
1 556 ASP n 
1 557 ALA n 
1 558 PHE n 
1 559 LYS n 
1 560 GLU n 
1 561 LEU n 
1 562 SER n 
1 563 GLN n 
1 564 LYS n 
1 565 ALA n 
1 566 ASN n 
1 567 PHE n 
1 568 LYS n 
1 569 GLU n 
1 570 PRO n 
1 571 GLU n 
1 572 ILE n 
1 573 VAL n 
1 574 THR n 
1 575 THR n 
1 576 GLY n 
1 577 THR n 
1 578 ASP n 
1 579 VAL n 
1 580 GLU n 
1 581 PHE n 
1 582 SER n 
1 583 GLY n 
1 584 GLU n 
1 585 ARG n 
1 586 VAL n 
1 587 GLY n 
1 588 LEU n 
1 589 GLY n 
1 590 GLN n 
1 591 LYS n 
1 592 ILE n 
1 593 ARG n 
1 594 ARG n 
1 595 CYS n 
1 596 PHE n 
1 597 GLY n 
1 598 MET n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   598 
_entity_src_gen.gene_src_common_name               'thale cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ALMT9, At3g18440, MYF24.16' 
_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      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            Sf9 
_entity_src_gen.pdbx_host_org_atcc                 CRL-1711 
_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          Bacmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                   ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LPP non-polymer         . '2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE' 
;1,2-DIPALMITOYL-SN-GLYCERO-3-PHOSPHATE; L-B,G-DIPALMITOYL-A-PHOSPHATIDIC ACID DISODIUM SALT; 3-SN-PHOSPHATIDIC ACID; 1,2-DIPALMITOYLDISODIUM SALT
;
'C35 H69 O8 P'   648.891 
LYS 'L-peptide linking' y LYSINE                                                            ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                        ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                        ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                          ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                            ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   PHE 8   8   ?   ?   ?   A . n 
A 1 9   ARG 9   9   ?   ?   ?   A . n 
A 1 10  HIS 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  ?   ?   ?   A . n 
A 1 12  ILE 12  12  ?   ?   ?   A . n 
A 1 13  LEU 13  13  ?   ?   ?   A . n 
A 1 14  GLU 14  14  ?   ?   ?   A . n 
A 1 15  LYS 15  15  ?   ?   ?   A . n 
A 1 16  ARG 16  16  ?   ?   ?   A . n 
A 1 17  GLU 17  17  ?   ?   ?   A . n 
A 1 18  ARG 18  18  ?   ?   ?   A . n 
A 1 19  LEU 19  19  ?   ?   ?   A . n 
A 1 20  LEU 20  20  ?   ?   ?   A . n 
A 1 21  SER 21  21  ?   ?   ?   A . n 
A 1 22  ASN 22  22  ?   ?   ?   A . n 
A 1 23  ASN 23  23  ?   ?   ?   A . n 
A 1 24  GLY 24  24  ?   ?   ?   A . n 
A 1 25  PHE 25  25  ?   ?   ?   A . n 
A 1 26  SER 26  26  ?   ?   ?   A . n 
A 1 27  ASP 27  27  ?   ?   ?   A . n 
A 1 28  PHE 28  28  ?   ?   ?   A . n 
A 1 29  ARG 29  29  ?   ?   ?   A . n 
A 1 30  PHE 30  30  ?   ?   ?   A . n 
A 1 31  THR 31  31  ?   ?   ?   A . n 
A 1 32  ASP 32  32  ?   ?   ?   A . n 
A 1 33  ILE 33  33  ?   ?   ?   A . n 
A 1 34  GLU 34  34  ?   ?   ?   A . n 
A 1 35  SER 35  35  ?   ?   ?   A . n 
A 1 36  ASN 36  36  ?   ?   ?   A . n 
A 1 37  ASP 37  37  ?   ?   ?   A . n 
A 1 38  LEU 38  38  ?   ?   ?   A . n 
A 1 39  LEU 39  39  ?   ?   ?   A . n 
A 1 40  GLU 40  40  ?   ?   ?   A . n 
A 1 41  ASN 41  41  ?   ?   ?   A . n 
A 1 42  GLU 42  42  ?   ?   ?   A . n 
A 1 43  ASN 43  43  ?   ?   ?   A . n 
A 1 44  CYS 44  44  ?   ?   ?   A . n 
A 1 45  GLY 45  45  ?   ?   ?   A . n 
A 1 46  ARG 46  46  ?   ?   ?   A . n 
A 1 47  ARG 47  47  ?   ?   ?   A . n 
A 1 48  THR 48  48  ?   ?   ?   A . n 
A 1 49  ARG 49  49  ?   ?   ?   A . n 
A 1 50  LEU 50  50  ?   ?   ?   A . n 
A 1 51  CYS 51  51  ?   ?   ?   A . n 
A 1 52  CYS 52  52  ?   ?   ?   A . n 
A 1 53  CYS 53  53  ?   ?   ?   A . n 
A 1 54  CYS 54  54  ?   ?   ?   A . n 
A 1 55  SER 55  55  ?   ?   ?   A . n 
A 1 56  CYS 56  56  ?   ?   ?   A . n 
A 1 57  GLY 57  57  ?   ?   ?   A . n 
A 1 58  ASN 58  58  ?   ?   ?   A . n 
A 1 59  LEU 59  59  ?   ?   ?   A . n 
A 1 60  SER 60  60  ?   ?   ?   A . n 
A 1 61  GLU 61  61  ?   ?   ?   A . n 
A 1 62  LYS 62  62  ?   ?   ?   A . n 
A 1 63  ILE 63  63  ?   ?   ?   A . n 
A 1 64  SER 64  64  ?   ?   ?   A . n 
A 1 65  GLY 65  65  ?   ?   ?   A . n 
A 1 66  VAL 66  66  ?   ?   ?   A . n 
A 1 67  TYR 67  67  ?   ?   ?   A . n 
A 1 68  ASP 68  68  ?   ?   ?   A . n 
A 1 69  ASP 69  69  ?   ?   ?   A . n 
A 1 70  ALA 70  70  ?   ?   ?   A . n 
A 1 71  LYS 71  71  ?   ?   ?   A . n 
A 1 72  ASP 72  72  ?   ?   ?   A . n 
A 1 73  VAL 73  73  ?   ?   ?   A . n 
A 1 74  ALA 74  74  ?   ?   ?   A . n 
A 1 75  ARG 75  75  ?   ?   ?   A . n 
A 1 76  LYS 76  76  ?   ?   ?   A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  MET 80  80  80  MET MET A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 GLN 108 108 108 GLN GLN A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 TRP 120 120 120 TRP TRP A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 TRP 167 167 167 TRP TRP A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 CYS 172 172 172 CYS CYS A . n 
A 1 173 THR 173 173 173 THR THR A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 TYR 189 189 189 TYR TYR A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 CYS 207 207 207 CYS CYS A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 ASN 241 241 241 ASN ASN A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 TRP 248 248 248 TRP TRP A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 GLY 250 250 250 GLY GLY A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 HIS 254 254 254 HIS HIS A . n 
A 1 255 ASN 255 255 255 ASN ASN A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 CYS 271 271 271 CYS CYS A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 CYS 278 278 278 CYS CYS A . n 
A 1 279 LEU 279 279 ?   ?   ?   A . n 
A 1 280 GLU 280 280 ?   ?   ?   A . n 
A 1 281 TYR 281 281 ?   ?   ?   A . n 
A 1 282 GLU 282 282 ?   ?   ?   A . n 
A 1 283 ARG 283 283 ?   ?   ?   A . n 
A 1 284 ILE 284 284 ?   ?   ?   A . n 
A 1 285 PRO 285 285 ?   ?   ?   A . n 
A 1 286 SER 286 286 ?   ?   ?   A . n 
A 1 287 LYS 287 287 ?   ?   ?   A . n 
A 1 288 ILE 288 288 ?   ?   ?   A . n 
A 1 289 LEU 289 289 ?   ?   ?   A . n 
A 1 290 THR 290 290 ?   ?   ?   A . n 
A 1 291 TYR 291 291 ?   ?   ?   A . n 
A 1 292 GLN 292 292 ?   ?   ?   A . n 
A 1 293 ALA 293 293 ?   ?   ?   A . n 
A 1 294 SER 294 294 ?   ?   ?   A . n 
A 1 295 GLU 295 295 ?   ?   ?   A . n 
A 1 296 ASP 296 296 ?   ?   ?   A . n 
A 1 297 PRO 297 297 ?   ?   ?   A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 LYS 300 300 300 LYS LYS A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 GLN 311 311 311 GLN GLN A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 SER 314 314 314 SER SER A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 MET 316 316 316 MET MET A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 PRO 323 323 323 PRO PRO A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 HIS 325 325 325 HIS HIS A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 TYR 328 328 328 TYR TYR A . n 
A 1 329 LYS 329 329 329 LYS LYS A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 TYR 333 333 333 TYR TYR A . n 
A 1 334 PRO 334 334 334 PRO PRO A . n 
A 1 335 TRP 335 335 335 TRP TRP A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 TYR 338 338 338 TYR TYR A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 LYS 340 340 340 LYS LYS A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 HIS 347 347 347 HIS HIS A . n 
A 1 348 CYS 348 348 348 CYS CYS A . n 
A 1 349 ALA 349 349 349 ALA ALA A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 MET 353 353 353 MET MET A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 LEU 355 355 355 LEU LEU A . n 
A 1 356 HIS 356 356 356 HIS HIS A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 CYS 358 358 358 CYS CYS A . n 
A 1 359 ILE 359 359 359 ILE ILE A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 SER 361 361 361 SER SER A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 GLN 364 364 364 GLN GLN A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 ARG 370 370 370 ARG ARG A . n 
A 1 371 GLN 371 371 371 GLN GLN A . n 
A 1 372 VAL 372 372 372 VAL VAL A . n 
A 1 373 PHE 373 373 373 PHE PHE A . n 
A 1 374 ARG 374 374 374 ARG ARG A . n 
A 1 375 GLN 375 375 375 GLN GLN A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 GLN 378 378 378 GLN GLN A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 GLY 381 381 381 GLY GLY A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 LYS 386 386 386 LYS LYS A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 ARG 389 389 389 ARG ARG A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 LYS 397 397 397 LYS LYS A . n 
A 1 398 MET 398 398 398 MET MET A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 PHE 408 408 408 PHE PHE A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 VAL 410 410 410 VAL VAL A . n 
A 1 411 HIS 411 411 411 HIS HIS A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 ALA 414 414 414 ALA ALA A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 GLU 416 416 416 GLU GLU A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 GLN 418 418 418 GLN GLN A . n 
A 1 419 HIS 419 419 419 HIS HIS A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 ILE 421 421 421 ILE ILE A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 LYS 424 424 424 LYS LYS A . n 
A 1 425 SER 425 425 425 SER SER A . n 
A 1 426 TYR 426 426 426 TYR TYR A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 VAL 429 429 429 VAL VAL A . n 
A 1 430 ASN 430 430 430 ASN ASN A . n 
A 1 431 SER 431 431 431 SER SER A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 CYS 433 433 433 CYS CYS A . n 
A 1 434 TRP 434 434 434 TRP TRP A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 ILE 436 436 ?   ?   ?   A . n 
A 1 437 GLY 437 437 ?   ?   ?   A . n 
A 1 438 ASN 438 438 ?   ?   ?   A . n 
A 1 439 ARG 439 439 ?   ?   ?   A . n 
A 1 440 ALA 440 440 ?   ?   ?   A . n 
A 1 441 THR 441 441 ?   ?   ?   A . n 
A 1 442 LYS 442 442 ?   ?   ?   A . n 
A 1 443 GLU 443 443 ?   ?   ?   A . n 
A 1 444 SER 444 444 ?   ?   ?   A . n 
A 1 445 GLU 445 445 ?   ?   ?   A . n 
A 1 446 PRO 446 446 ?   ?   ?   A . n 
A 1 447 GLN 447 447 ?   ?   ?   A . n 
A 1 448 GLU 448 448 ?   ?   ?   A . n 
A 1 449 LEU 449 449 ?   ?   ?   A . n 
A 1 450 LEU 450 450 ?   ?   ?   A . n 
A 1 451 SER 451 451 ?   ?   ?   A . n 
A 1 452 LEU 452 452 ?   ?   ?   A . n 
A 1 453 GLU 453 453 ?   ?   ?   A . n 
A 1 454 ASP 454 454 ?   ?   ?   A . n 
A 1 455 SER 455 455 ?   ?   ?   A . n 
A 1 456 ASP 456 456 ?   ?   ?   A . n 
A 1 457 PRO 457 457 ?   ?   ?   A . n 
A 1 458 PRO 458 458 ?   ?   ?   A . n 
A 1 459 GLU 459 459 ?   ?   ?   A . n 
A 1 460 ASN 460 460 ?   ?   ?   A . n 
A 1 461 HIS 461 461 ?   ?   ?   A . n 
A 1 462 ALA 462 462 ?   ?   ?   A . n 
A 1 463 PRO 463 463 ?   ?   ?   A . n 
A 1 464 PRO 464 464 ?   ?   ?   A . n 
A 1 465 ILE 465 465 ?   ?   ?   A . n 
A 1 466 TYR 466 466 ?   ?   ?   A . n 
A 1 467 ALA 467 467 ?   ?   ?   A . n 
A 1 468 PHE 468 468 ?   ?   ?   A . n 
A 1 469 LYS 469 469 ?   ?   ?   A . n 
A 1 470 SER 470 470 ?   ?   ?   A . n 
A 1 471 LEU 471 471 ?   ?   ?   A . n 
A 1 472 SER 472 472 ?   ?   ?   A . n 
A 1 473 GLU 473 473 ?   ?   ?   A . n 
A 1 474 ALA 474 474 ?   ?   ?   A . n 
A 1 475 VAL 475 475 ?   ?   ?   A . n 
A 1 476 LEU 476 476 ?   ?   ?   A . n 
A 1 477 GLU 477 477 ?   ?   ?   A . n 
A 1 478 ILE 478 478 ?   ?   ?   A . n 
A 1 479 PRO 479 479 ?   ?   ?   A . n 
A 1 480 PRO 480 480 ?   ?   ?   A . n 
A 1 481 SER 481 481 ?   ?   ?   A . n 
A 1 482 TRP 482 482 ?   ?   ?   A . n 
A 1 483 GLY 483 483 ?   ?   ?   A . n 
A 1 484 GLU 484 484 ?   ?   ?   A . n 
A 1 485 LYS 485 485 ?   ?   ?   A . n 
A 1 486 ASN 486 486 ?   ?   ?   A . n 
A 1 487 HIS 487 487 ?   ?   ?   A . n 
A 1 488 ARG 488 488 ?   ?   ?   A . n 
A 1 489 GLU 489 489 ?   ?   ?   A . n 
A 1 490 ALA 490 490 ?   ?   ?   A . n 
A 1 491 LEU 491 491 ?   ?   ?   A . n 
A 1 492 ASN 492 492 ?   ?   ?   A . n 
A 1 493 HIS 493 493 ?   ?   ?   A . n 
A 1 494 ARG 494 494 ?   ?   ?   A . n 
A 1 495 PRO 495 495 ?   ?   ?   A . n 
A 1 496 THR 496 496 ?   ?   ?   A . n 
A 1 497 PHE 497 497 ?   ?   ?   A . n 
A 1 498 SER 498 498 ?   ?   ?   A . n 
A 1 499 LYS 499 499 ?   ?   ?   A . n 
A 1 500 GLN 500 500 ?   ?   ?   A . n 
A 1 501 VAL 501 501 ?   ?   ?   A . n 
A 1 502 SER 502 502 ?   ?   ?   A . n 
A 1 503 TRP 503 503 ?   ?   ?   A . n 
A 1 504 PRO 504 504 ?   ?   ?   A . n 
A 1 505 ALA 505 505 ?   ?   ?   A . n 
A 1 506 ARG 506 506 ?   ?   ?   A . n 
A 1 507 LEU 507 507 ?   ?   ?   A . n 
A 1 508 VAL 508 508 ?   ?   ?   A . n 
A 1 509 LEU 509 509 ?   ?   ?   A . n 
A 1 510 PRO 510 510 ?   ?   ?   A . n 
A 1 511 PRO 511 511 ?   ?   ?   A . n 
A 1 512 HIS 512 512 ?   ?   ?   A . n 
A 1 513 LEU 513 513 ?   ?   ?   A . n 
A 1 514 GLU 514 514 ?   ?   ?   A . n 
A 1 515 THR 515 515 ?   ?   ?   A . n 
A 1 516 THR 516 516 ?   ?   ?   A . n 
A 1 517 ASN 517 517 ?   ?   ?   A . n 
A 1 518 GLY 518 518 ?   ?   ?   A . n 
A 1 519 ALA 519 519 ?   ?   ?   A . n 
A 1 520 SER 520 520 ?   ?   ?   A . n 
A 1 521 PRO 521 521 ?   ?   ?   A . n 
A 1 522 LEU 522 522 ?   ?   ?   A . n 
A 1 523 VAL 523 523 ?   ?   ?   A . n 
A 1 524 GLU 524 524 ?   ?   ?   A . n 
A 1 525 THR 525 525 ?   ?   ?   A . n 
A 1 526 THR 526 526 ?   ?   ?   A . n 
A 1 527 LYS 527 527 527 LYS LYS A . n 
A 1 528 THR 528 528 528 THR THR A . n 
A 1 529 TYR 529 529 529 TYR TYR A . n 
A 1 530 GLU 530 530 530 GLU GLU A . n 
A 1 531 SER 531 531 531 SER SER A . n 
A 1 532 ALA 532 532 532 ALA ALA A . n 
A 1 533 SER 533 533 533 SER SER A . n 
A 1 534 ALA 534 534 534 ALA ALA A . n 
A 1 535 LEU 535 535 535 LEU LEU A . n 
A 1 536 SER 536 536 536 SER SER A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 ALA 538 538 538 ALA ALA A . n 
A 1 539 THR 539 539 539 THR THR A . n 
A 1 540 PHE 540 540 540 PHE PHE A . n 
A 1 541 ALA 541 541 541 ALA ALA A . n 
A 1 542 SER 542 542 542 SER SER A . n 
A 1 543 LEU 543 543 543 LEU LEU A . n 
A 1 544 LEU 544 544 544 LEU LEU A . n 
A 1 545 ILE 545 545 545 ILE ILE A . n 
A 1 546 GLU 546 546 546 GLU GLU A . n 
A 1 547 PHE 547 547 547 PHE PHE A . n 
A 1 548 VAL 548 548 548 VAL VAL A . n 
A 1 549 ALA 549 549 549 ALA ALA A . n 
A 1 550 ARG 550 550 550 ARG ARG A . n 
A 1 551 LEU 551 551 551 LEU LEU A . n 
A 1 552 GLN 552 552 552 GLN GLN A . n 
A 1 553 ASN 553 553 553 ASN ASN A . n 
A 1 554 VAL 554 554 554 VAL VAL A . n 
A 1 555 VAL 555 555 555 VAL VAL A . n 
A 1 556 ASP 556 556 556 ASP ASP A . n 
A 1 557 ALA 557 557 557 ALA ALA A . n 
A 1 558 PHE 558 558 558 PHE PHE A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 GLU 560 560 560 GLU GLU A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 SER 562 562 562 SER SER A . n 
A 1 563 GLN 563 563 563 GLN GLN A . n 
A 1 564 LYS 564 564 564 LYS LYS A . n 
A 1 565 ALA 565 565 565 ALA ALA A . n 
A 1 566 ASN 566 566 566 ASN ASN A . n 
A 1 567 PHE 567 567 567 PHE PHE A . n 
A 1 568 LYS 568 568 568 LYS LYS A . n 
A 1 569 GLU 569 569 569 GLU GLU A . n 
A 1 570 PRO 570 570 570 PRO PRO A . n 
A 1 571 GLU 571 571 571 GLU GLU A . n 
A 1 572 ILE 572 572 ?   ?   ?   A . n 
A 1 573 VAL 573 573 ?   ?   ?   A . n 
A 1 574 THR 574 574 ?   ?   ?   A . n 
A 1 575 THR 575 575 ?   ?   ?   A . n 
A 1 576 GLY 576 576 ?   ?   ?   A . n 
A 1 577 THR 577 577 ?   ?   ?   A . n 
A 1 578 ASP 578 578 ?   ?   ?   A . n 
A 1 579 VAL 579 579 ?   ?   ?   A . n 
A 1 580 GLU 580 580 ?   ?   ?   A . n 
A 1 581 PHE 581 581 ?   ?   ?   A . n 
A 1 582 SER 582 582 ?   ?   ?   A . n 
A 1 583 GLY 583 583 ?   ?   ?   A . n 
A 1 584 GLU 584 584 ?   ?   ?   A . n 
A 1 585 ARG 585 585 ?   ?   ?   A . n 
A 1 586 VAL 586 586 ?   ?   ?   A . n 
A 1 587 GLY 587 587 ?   ?   ?   A . n 
A 1 588 LEU 588 588 ?   ?   ?   A . n 
A 1 589 GLY 589 589 ?   ?   ?   A . n 
A 1 590 GLN 590 590 ?   ?   ?   A . n 
A 1 591 LYS 591 591 ?   ?   ?   A . n 
A 1 592 ILE 592 592 ?   ?   ?   A . n 
A 1 593 ARG 593 593 ?   ?   ?   A . n 
A 1 594 ARG 594 594 ?   ?   ?   A . n 
A 1 595 CYS 595 595 ?   ?   ?   A . n 
A 1 596 PHE 596 596 ?   ?   ?   A . n 
A 1 597 GLY 597 597 ?   ?   ?   A . n 
A 1 598 MET 598 598 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   ALA 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   SER 7   7   ?   ?   ?   B . n 
B 1 8   PHE 8   8   ?   ?   ?   B . n 
B 1 9   ARG 9   9   ?   ?   ?   B . n 
B 1 10  HIS 10  10  ?   ?   ?   B . n 
B 1 11  GLY 11  11  ?   ?   ?   B . n 
B 1 12  ILE 12  12  ?   ?   ?   B . n 
B 1 13  LEU 13  13  ?   ?   ?   B . n 
B 1 14  GLU 14  14  ?   ?   ?   B . n 
B 1 15  LYS 15  15  ?   ?   ?   B . n 
B 1 16  ARG 16  16  ?   ?   ?   B . n 
B 1 17  GLU 17  17  ?   ?   ?   B . n 
B 1 18  ARG 18  18  ?   ?   ?   B . n 
B 1 19  LEU 19  19  ?   ?   ?   B . n 
B 1 20  LEU 20  20  ?   ?   ?   B . n 
B 1 21  SER 21  21  ?   ?   ?   B . n 
B 1 22  ASN 22  22  ?   ?   ?   B . n 
B 1 23  ASN 23  23  ?   ?   ?   B . n 
B 1 24  GLY 24  24  ?   ?   ?   B . n 
B 1 25  PHE 25  25  ?   ?   ?   B . n 
B 1 26  SER 26  26  ?   ?   ?   B . n 
B 1 27  ASP 27  27  ?   ?   ?   B . n 
B 1 28  PHE 28  28  ?   ?   ?   B . n 
B 1 29  ARG 29  29  ?   ?   ?   B . n 
B 1 30  PHE 30  30  ?   ?   ?   B . n 
B 1 31  THR 31  31  ?   ?   ?   B . n 
B 1 32  ASP 32  32  ?   ?   ?   B . n 
B 1 33  ILE 33  33  ?   ?   ?   B . n 
B 1 34  GLU 34  34  ?   ?   ?   B . n 
B 1 35  SER 35  35  ?   ?   ?   B . n 
B 1 36  ASN 36  36  ?   ?   ?   B . n 
B 1 37  ASP 37  37  ?   ?   ?   B . n 
B 1 38  LEU 38  38  ?   ?   ?   B . n 
B 1 39  LEU 39  39  ?   ?   ?   B . n 
B 1 40  GLU 40  40  ?   ?   ?   B . n 
B 1 41  ASN 41  41  ?   ?   ?   B . n 
B 1 42  GLU 42  42  ?   ?   ?   B . n 
B 1 43  ASN 43  43  ?   ?   ?   B . n 
B 1 44  CYS 44  44  ?   ?   ?   B . n 
B 1 45  GLY 45  45  ?   ?   ?   B . n 
B 1 46  ARG 46  46  ?   ?   ?   B . n 
B 1 47  ARG 47  47  ?   ?   ?   B . n 
B 1 48  THR 48  48  ?   ?   ?   B . n 
B 1 49  ARG 49  49  ?   ?   ?   B . n 
B 1 50  LEU 50  50  ?   ?   ?   B . n 
B 1 51  CYS 51  51  ?   ?   ?   B . n 
B 1 52  CYS 52  52  ?   ?   ?   B . n 
B 1 53  CYS 53  53  ?   ?   ?   B . n 
B 1 54  CYS 54  54  ?   ?   ?   B . n 
B 1 55  SER 55  55  ?   ?   ?   B . n 
B 1 56  CYS 56  56  ?   ?   ?   B . n 
B 1 57  GLY 57  57  ?   ?   ?   B . n 
B 1 58  ASN 58  58  ?   ?   ?   B . n 
B 1 59  LEU 59  59  ?   ?   ?   B . n 
B 1 60  SER 60  60  ?   ?   ?   B . n 
B 1 61  GLU 61  61  ?   ?   ?   B . n 
B 1 62  LYS 62  62  ?   ?   ?   B . n 
B 1 63  ILE 63  63  ?   ?   ?   B . n 
B 1 64  SER 64  64  ?   ?   ?   B . n 
B 1 65  GLY 65  65  ?   ?   ?   B . n 
B 1 66  VAL 66  66  ?   ?   ?   B . n 
B 1 67  TYR 67  67  ?   ?   ?   B . n 
B 1 68  ASP 68  68  ?   ?   ?   B . n 
B 1 69  ASP 69  69  ?   ?   ?   B . n 
B 1 70  ALA 70  70  ?   ?   ?   B . n 
B 1 71  LYS 71  71  ?   ?   ?   B . n 
B 1 72  ASP 72  72  ?   ?   ?   B . n 
B 1 73  VAL 73  73  ?   ?   ?   B . n 
B 1 74  ALA 74  74  ?   ?   ?   B . n 
B 1 75  ARG 75  75  ?   ?   ?   B . n 
B 1 76  LYS 76  76  ?   ?   ?   B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  TRP 78  78  78  TRP TRP B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  MET 80  80  80  MET MET B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  ILE 88  88  88  ILE ILE B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  PHE 90  90  90  PHE PHE B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  LEU 96  96  96  LEU LEU B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 PHE 106 106 106 PHE PHE B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 GLN 108 108 108 GLN GLN B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 PRO 110 110 110 PRO PRO B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 PRO 112 112 112 PRO PRO B . n 
B 1 113 ASP 113 113 113 ASP ASP B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 TRP 120 120 120 TRP TRP B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 ILE 133 133 133 ILE ILE B . n 
B 1 134 GLY 134 134 134 GLY GLY B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 THR 136 136 136 THR THR B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 SER 138 138 138 SER SER B . n 
B 1 139 LYS 139 139 139 LYS LYS B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 PHE 141 141 141 PHE PHE B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 MET 157 157 157 MET MET B . n 
B 1 158 ALA 158 158 158 ALA ALA B . n 
B 1 159 GLU 159 159 159 GLU GLU B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 SER 161 161 161 SER SER B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 LEU 163 163 163 LEU LEU B . n 
B 1 164 PHE 164 164 164 PHE PHE B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 ASP 166 166 166 ASP ASP B . n 
B 1 167 TRP 167 167 167 TRP TRP B . n 
B 1 168 GLU 168 168 168 GLU GLU B . n 
B 1 169 GLU 169 169 169 GLU GLU B . n 
B 1 170 ILE 170 170 170 ILE ILE B . n 
B 1 171 PHE 171 171 171 PHE PHE B . n 
B 1 172 CYS 172 172 172 CYS CYS B . n 
B 1 173 THR 173 173 173 THR THR B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 ILE 176 176 176 ILE ILE B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 CYS 178 178 178 CYS CYS B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 THR 184 184 184 THR THR B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 MET 186 186 186 MET MET B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 TYR 189 189 189 TYR TYR B . n 
B 1 190 PRO 190 190 190 PRO PRO B . n 
B 1 191 SER 191 191 191 SER SER B . n 
B 1 192 MET 192 192 192 MET MET B . n 
B 1 193 LYS 193 193 193 LYS LYS B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 TYR 195 195 195 TYR TYR B . n 
B 1 196 GLU 196 196 196 GLU GLU B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 PHE 199 199 199 PHE PHE B . n 
B 1 200 ARG 200 200 200 ARG ARG B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 PHE 202 202 202 PHE PHE B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 TYR 206 206 206 TYR TYR B . n 
B 1 207 CYS 207 207 207 CYS CYS B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 SER 212 212 212 SER SER B . n 
B 1 213 GLY 213 213 213 GLY GLY B . n 
B 1 214 PHE 214 214 214 PHE PHE B . n 
B 1 215 ARG 215 215 215 ARG ARG B . n 
B 1 216 THR 216 216 216 THR THR B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 GLN 218 218 218 GLN GLN B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 VAL 222 222 222 VAL VAL B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ILE 224 224 224 ILE ILE B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 PHE 227 227 227 PHE PHE B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 ILE 230 230 230 ILE ILE B . n 
B 1 231 ALA 231 231 231 ALA ALA B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 GLY 233 233 233 GLY GLY B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 GLY 235 235 235 GLY GLY B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 SER 237 237 237 SER SER B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 VAL 240 240 240 VAL VAL B . n 
B 1 241 ASN 241 241 241 ASN ASN B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 TYR 245 245 245 TYR TYR B . n 
B 1 246 PRO 246 246 246 PRO PRO B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 TRP 248 248 248 TRP TRP B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 GLY 250 250 250 GLY GLY B . n 
B 1 251 GLU 251 251 251 GLU GLU B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 HIS 254 254 254 HIS HIS B . n 
B 1 255 ASN 255 255 255 ASN ASN B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 VAL 258 258 258 VAL VAL B . n 
B 1 259 LYS 259 259 259 LYS LYS B . n 
B 1 260 ASN 260 260 260 ASN ASN B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 MET 262 262 262 MET MET B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 VAL 264 264 264 VAL VAL B . n 
B 1 265 ALA 265 265 265 ALA ALA B . n 
B 1 266 THR 266 266 266 THR THR B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 CYS 271 271 271 CYS CYS B . n 
B 1 272 VAL 272 272 272 VAL VAL B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 GLY 274 274 274 GLY GLY B . n 
B 1 275 TYR 275 275 275 TYR TYR B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 ARG 277 277 277 ARG ARG B . n 
B 1 278 CYS 278 278 278 CYS CYS B . n 
B 1 279 LEU 279 279 ?   ?   ?   B . n 
B 1 280 GLU 280 280 ?   ?   ?   B . n 
B 1 281 TYR 281 281 ?   ?   ?   B . n 
B 1 282 GLU 282 282 ?   ?   ?   B . n 
B 1 283 ARG 283 283 ?   ?   ?   B . n 
B 1 284 ILE 284 284 ?   ?   ?   B . n 
B 1 285 PRO 285 285 ?   ?   ?   B . n 
B 1 286 SER 286 286 ?   ?   ?   B . n 
B 1 287 LYS 287 287 ?   ?   ?   B . n 
B 1 288 ILE 288 288 ?   ?   ?   B . n 
B 1 289 LEU 289 289 ?   ?   ?   B . n 
B 1 290 THR 290 290 ?   ?   ?   B . n 
B 1 291 TYR 291 291 ?   ?   ?   B . n 
B 1 292 GLN 292 292 ?   ?   ?   B . n 
B 1 293 ALA 293 293 ?   ?   ?   B . n 
B 1 294 SER 294 294 ?   ?   ?   B . n 
B 1 295 GLU 295 295 ?   ?   ?   B . n 
B 1 296 ASP 296 296 ?   ?   ?   B . n 
B 1 297 PRO 297 297 ?   ?   ?   B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 LYS 300 300 300 LYS LYS B . n 
B 1 301 GLY 301 301 301 GLY GLY B . n 
B 1 302 TYR 302 302 302 TYR TYR B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 VAL 306 306 306 VAL VAL B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 SER 308 308 308 SER SER B . n 
B 1 309 THR 309 309 309 THR THR B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 GLN 311 311 311 GLN GLN B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 GLU 313 313 313 GLU GLU B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 LEU 315 315 315 LEU LEU B . n 
B 1 316 MET 316 316 316 MET MET B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 PHE 318 318 318 PHE PHE B . n 
B 1 319 ALA 319 319 319 ALA ALA B . n 
B 1 320 ILE 320 320 320 ILE ILE B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 GLU 322 322 322 GLU GLU B . n 
B 1 323 PRO 323 323 323 PRO PRO B . n 
B 1 324 PRO 324 324 324 PRO PRO B . n 
B 1 325 HIS 325 325 325 HIS HIS B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 PRO 327 327 327 PRO PRO B . n 
B 1 328 TYR 328 328 328 TYR TYR B . n 
B 1 329 LYS 329 329 329 LYS LYS B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 PHE 331 331 331 PHE PHE B . n 
B 1 332 ASN 332 332 332 ASN ASN B . n 
B 1 333 TYR 333 333 333 TYR TYR B . n 
B 1 334 PRO 334 334 334 PRO PRO B . n 
B 1 335 TRP 335 335 335 TRP TRP B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ASN 337 337 337 ASN ASN B . n 
B 1 338 TYR 338 338 338 TYR TYR B . n 
B 1 339 VAL 339 339 339 VAL VAL B . n 
B 1 340 LYS 340 340 340 LYS LYS B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 SER 342 342 342 SER SER B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 ALA 344 344 344 ALA ALA B . n 
B 1 345 LEU 345 345 345 LEU LEU B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 HIS 347 347 347 HIS HIS B . n 
B 1 348 CYS 348 348 348 CYS CYS B . n 
B 1 349 ALA 349 349 349 ALA ALA B . n 
B 1 350 PHE 350 350 350 PHE PHE B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 VAL 352 352 352 VAL VAL B . n 
B 1 353 MET 353 353 353 MET MET B . n 
B 1 354 ALA 354 354 354 ALA ALA B . n 
B 1 355 LEU 355 355 355 LEU LEU B . n 
B 1 356 HIS 356 356 356 HIS HIS B . n 
B 1 357 GLY 357 357 357 GLY GLY B . n 
B 1 358 CYS 358 358 358 CYS CYS B . n 
B 1 359 ILE 359 359 359 ILE ILE B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 SER 361 361 361 SER SER B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 ILE 363 363 363 ILE ILE B . n 
B 1 364 GLN 364 364 364 GLN GLN B . n 
B 1 365 ALA 365 365 365 ALA ALA B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 GLU 367 367 367 GLU GLU B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ARG 369 369 369 ARG ARG B . n 
B 1 370 ARG 370 370 370 ARG ARG B . n 
B 1 371 GLN 371 371 371 GLN GLN B . n 
B 1 372 VAL 372 372 372 VAL VAL B . n 
B 1 373 PHE 373 373 373 PHE PHE B . n 
B 1 374 ARG 374 374 374 ARG ARG B . n 
B 1 375 GLN 375 375 375 GLN GLN B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 LEU 377 377 377 LEU LEU B . n 
B 1 378 GLN 378 378 378 GLN GLN B . n 
B 1 379 ARG 379 379 379 ARG ARG B . n 
B 1 380 VAL 380 380 380 VAL VAL B . n 
B 1 381 GLY 381 381 381 GLY GLY B . n 
B 1 382 VAL 382 382 382 VAL VAL B . n 
B 1 383 GLU 383 383 383 GLU GLU B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 ALA 385 385 385 ALA ALA B . n 
B 1 386 LYS 386 386 386 LYS LYS B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 LEU 388 388 388 LEU LEU B . n 
B 1 389 ARG 389 389 389 ARG ARG B . n 
B 1 390 GLU 390 390 390 GLU GLU B . n 
B 1 391 LEU 391 391 391 LEU LEU B . n 
B 1 392 GLY 392 392 392 GLY GLY B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 LYS 394 394 394 LYS LYS B . n 
B 1 395 VAL 395 395 395 VAL VAL B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 LYS 397 397 397 LYS LYS B . n 
B 1 398 MET 398 398 398 MET MET B . n 
B 1 399 GLU 399 399 399 GLU GLU B . n 
B 1 400 LYS 400 400 400 LYS LYS B . n 
B 1 401 LEU 401 401 401 LEU LEU B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 PRO 403 403 403 PRO PRO B . n 
B 1 404 VAL 404 404 404 VAL VAL B . n 
B 1 405 ASP 405 405 405 ASP ASP B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 PHE 408 408 408 PHE PHE B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 VAL 410 410 410 VAL VAL B . n 
B 1 411 HIS 411 411 411 HIS HIS B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 ALA 413 413 413 ALA ALA B . n 
B 1 414 ALA 414 414 414 ALA ALA B . n 
B 1 415 GLU 415 415 415 GLU GLU B . n 
B 1 416 GLU 416 416 416 GLU GLU B . n 
B 1 417 LEU 417 417 417 LEU LEU B . n 
B 1 418 GLN 418 418 418 GLN GLN B . n 
B 1 419 HIS 419 419 419 HIS HIS B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 ILE 421 421 421 ILE ILE B . n 
B 1 422 ASP 422 422 422 ASP ASP B . n 
B 1 423 LYS 423 423 423 LYS LYS B . n 
B 1 424 LYS 424 424 424 LYS LYS B . n 
B 1 425 SER 425 425 425 SER SER B . n 
B 1 426 TYR 426 426 426 TYR TYR B . n 
B 1 427 LEU 427 427 427 LEU LEU B . n 
B 1 428 LEU 428 428 428 LEU LEU B . n 
B 1 429 VAL 429 429 429 VAL VAL B . n 
B 1 430 ASN 430 430 430 ASN ASN B . n 
B 1 431 SER 431 431 431 SER SER B . n 
B 1 432 GLU 432 432 432 GLU GLU B . n 
B 1 433 CYS 433 433 433 CYS CYS B . n 
B 1 434 TRP 434 434 434 TRP TRP B . n 
B 1 435 GLU 435 435 435 GLU GLU B . n 
B 1 436 ILE 436 436 ?   ?   ?   B . n 
B 1 437 GLY 437 437 ?   ?   ?   B . n 
B 1 438 ASN 438 438 ?   ?   ?   B . n 
B 1 439 ARG 439 439 ?   ?   ?   B . n 
B 1 440 ALA 440 440 ?   ?   ?   B . n 
B 1 441 THR 441 441 ?   ?   ?   B . n 
B 1 442 LYS 442 442 ?   ?   ?   B . n 
B 1 443 GLU 443 443 ?   ?   ?   B . n 
B 1 444 SER 444 444 ?   ?   ?   B . n 
B 1 445 GLU 445 445 ?   ?   ?   B . n 
B 1 446 PRO 446 446 ?   ?   ?   B . n 
B 1 447 GLN 447 447 ?   ?   ?   B . n 
B 1 448 GLU 448 448 ?   ?   ?   B . n 
B 1 449 LEU 449 449 ?   ?   ?   B . n 
B 1 450 LEU 450 450 ?   ?   ?   B . n 
B 1 451 SER 451 451 ?   ?   ?   B . n 
B 1 452 LEU 452 452 ?   ?   ?   B . n 
B 1 453 GLU 453 453 ?   ?   ?   B . n 
B 1 454 ASP 454 454 ?   ?   ?   B . n 
B 1 455 SER 455 455 ?   ?   ?   B . n 
B 1 456 ASP 456 456 ?   ?   ?   B . n 
B 1 457 PRO 457 457 ?   ?   ?   B . n 
B 1 458 PRO 458 458 ?   ?   ?   B . n 
B 1 459 GLU 459 459 ?   ?   ?   B . n 
B 1 460 ASN 460 460 ?   ?   ?   B . n 
B 1 461 HIS 461 461 ?   ?   ?   B . n 
B 1 462 ALA 462 462 ?   ?   ?   B . n 
B 1 463 PRO 463 463 ?   ?   ?   B . n 
B 1 464 PRO 464 464 ?   ?   ?   B . n 
B 1 465 ILE 465 465 ?   ?   ?   B . n 
B 1 466 TYR 466 466 ?   ?   ?   B . n 
B 1 467 ALA 467 467 ?   ?   ?   B . n 
B 1 468 PHE 468 468 ?   ?   ?   B . n 
B 1 469 LYS 469 469 ?   ?   ?   B . n 
B 1 470 SER 470 470 ?   ?   ?   B . n 
B 1 471 LEU 471 471 ?   ?   ?   B . n 
B 1 472 SER 472 472 ?   ?   ?   B . n 
B 1 473 GLU 473 473 ?   ?   ?   B . n 
B 1 474 ALA 474 474 ?   ?   ?   B . n 
B 1 475 VAL 475 475 ?   ?   ?   B . n 
B 1 476 LEU 476 476 ?   ?   ?   B . n 
B 1 477 GLU 477 477 ?   ?   ?   B . n 
B 1 478 ILE 478 478 ?   ?   ?   B . n 
B 1 479 PRO 479 479 ?   ?   ?   B . n 
B 1 480 PRO 480 480 ?   ?   ?   B . n 
B 1 481 SER 481 481 ?   ?   ?   B . n 
B 1 482 TRP 482 482 ?   ?   ?   B . n 
B 1 483 GLY 483 483 ?   ?   ?   B . n 
B 1 484 GLU 484 484 ?   ?   ?   B . n 
B 1 485 LYS 485 485 ?   ?   ?   B . n 
B 1 486 ASN 486 486 ?   ?   ?   B . n 
B 1 487 HIS 487 487 ?   ?   ?   B . n 
B 1 488 ARG 488 488 ?   ?   ?   B . n 
B 1 489 GLU 489 489 ?   ?   ?   B . n 
B 1 490 ALA 490 490 ?   ?   ?   B . n 
B 1 491 LEU 491 491 ?   ?   ?   B . n 
B 1 492 ASN 492 492 ?   ?   ?   B . n 
B 1 493 HIS 493 493 ?   ?   ?   B . n 
B 1 494 ARG 494 494 ?   ?   ?   B . n 
B 1 495 PRO 495 495 ?   ?   ?   B . n 
B 1 496 THR 496 496 ?   ?   ?   B . n 
B 1 497 PHE 497 497 ?   ?   ?   B . n 
B 1 498 SER 498 498 ?   ?   ?   B . n 
B 1 499 LYS 499 499 ?   ?   ?   B . n 
B 1 500 GLN 500 500 ?   ?   ?   B . n 
B 1 501 VAL 501 501 ?   ?   ?   B . n 
B 1 502 SER 502 502 ?   ?   ?   B . n 
B 1 503 TRP 503 503 ?   ?   ?   B . n 
B 1 504 PRO 504 504 ?   ?   ?   B . n 
B 1 505 ALA 505 505 ?   ?   ?   B . n 
B 1 506 ARG 506 506 ?   ?   ?   B . n 
B 1 507 LEU 507 507 ?   ?   ?   B . n 
B 1 508 VAL 508 508 ?   ?   ?   B . n 
B 1 509 LEU 509 509 ?   ?   ?   B . n 
B 1 510 PRO 510 510 ?   ?   ?   B . n 
B 1 511 PRO 511 511 ?   ?   ?   B . n 
B 1 512 HIS 512 512 ?   ?   ?   B . n 
B 1 513 LEU 513 513 ?   ?   ?   B . n 
B 1 514 GLU 514 514 ?   ?   ?   B . n 
B 1 515 THR 515 515 ?   ?   ?   B . n 
B 1 516 THR 516 516 ?   ?   ?   B . n 
B 1 517 ASN 517 517 ?   ?   ?   B . n 
B 1 518 GLY 518 518 ?   ?   ?   B . n 
B 1 519 ALA 519 519 ?   ?   ?   B . n 
B 1 520 SER 520 520 ?   ?   ?   B . n 
B 1 521 PRO 521 521 ?   ?   ?   B . n 
B 1 522 LEU 522 522 ?   ?   ?   B . n 
B 1 523 VAL 523 523 ?   ?   ?   B . n 
B 1 524 GLU 524 524 ?   ?   ?   B . n 
B 1 525 THR 525 525 ?   ?   ?   B . n 
B 1 526 THR 526 526 ?   ?   ?   B . n 
B 1 527 LYS 527 527 527 LYS LYS B . n 
B 1 528 THR 528 528 528 THR THR B . n 
B 1 529 TYR 529 529 529 TYR TYR B . n 
B 1 530 GLU 530 530 530 GLU GLU B . n 
B 1 531 SER 531 531 531 SER SER B . n 
B 1 532 ALA 532 532 532 ALA ALA B . n 
B 1 533 SER 533 533 533 SER SER B . n 
B 1 534 ALA 534 534 534 ALA ALA B . n 
B 1 535 LEU 535 535 535 LEU LEU B . n 
B 1 536 SER 536 536 536 SER SER B . n 
B 1 537 LEU 537 537 537 LEU LEU B . n 
B 1 538 ALA 538 538 538 ALA ALA B . n 
B 1 539 THR 539 539 539 THR THR B . n 
B 1 540 PHE 540 540 540 PHE PHE B . n 
B 1 541 ALA 541 541 541 ALA ALA B . n 
B 1 542 SER 542 542 542 SER SER B . n 
B 1 543 LEU 543 543 543 LEU LEU B . n 
B 1 544 LEU 544 544 544 LEU LEU B . n 
B 1 545 ILE 545 545 545 ILE ILE B . n 
B 1 546 GLU 546 546 546 GLU GLU B . n 
B 1 547 PHE 547 547 547 PHE PHE B . n 
B 1 548 VAL 548 548 548 VAL VAL B . n 
B 1 549 ALA 549 549 549 ALA ALA B . n 
B 1 550 ARG 550 550 550 ARG ARG B . n 
B 1 551 LEU 551 551 551 LEU LEU B . n 
B 1 552 GLN 552 552 552 GLN GLN B . n 
B 1 553 ASN 553 553 553 ASN ASN B . n 
B 1 554 VAL 554 554 554 VAL VAL B . n 
B 1 555 VAL 555 555 555 VAL VAL B . n 
B 1 556 ASP 556 556 556 ASP ASP B . n 
B 1 557 ALA 557 557 557 ALA ALA B . n 
B 1 558 PHE 558 558 558 PHE PHE B . n 
B 1 559 LYS 559 559 559 LYS LYS B . n 
B 1 560 GLU 560 560 560 GLU GLU B . n 
B 1 561 LEU 561 561 561 LEU LEU B . n 
B 1 562 SER 562 562 562 SER SER B . n 
B 1 563 GLN 563 563 563 GLN GLN B . n 
B 1 564 LYS 564 564 564 LYS LYS B . n 
B 1 565 ALA 565 565 565 ALA ALA B . n 
B 1 566 ASN 566 566 566 ASN ASN B . n 
B 1 567 PHE 567 567 567 PHE PHE B . n 
B 1 568 LYS 568 568 568 LYS LYS B . n 
B 1 569 GLU 569 569 569 GLU GLU B . n 
B 1 570 PRO 570 570 570 PRO PRO B . n 
B 1 571 GLU 571 571 571 GLU GLU B . n 
B 1 572 ILE 572 572 ?   ?   ?   B . n 
B 1 573 VAL 573 573 ?   ?   ?   B . n 
B 1 574 THR 574 574 ?   ?   ?   B . n 
B 1 575 THR 575 575 ?   ?   ?   B . n 
B 1 576 GLY 576 576 ?   ?   ?   B . n 
B 1 577 THR 577 577 ?   ?   ?   B . n 
B 1 578 ASP 578 578 ?   ?   ?   B . n 
B 1 579 VAL 579 579 ?   ?   ?   B . n 
B 1 580 GLU 580 580 ?   ?   ?   B . n 
B 1 581 PHE 581 581 ?   ?   ?   B . n 
B 1 582 SER 582 582 ?   ?   ?   B . n 
B 1 583 GLY 583 583 ?   ?   ?   B . n 
B 1 584 GLU 584 584 ?   ?   ?   B . n 
B 1 585 ARG 585 585 ?   ?   ?   B . n 
B 1 586 VAL 586 586 ?   ?   ?   B . n 
B 1 587 GLY 587 587 ?   ?   ?   B . n 
B 1 588 LEU 588 588 ?   ?   ?   B . n 
B 1 589 GLY 589 589 ?   ?   ?   B . n 
B 1 590 GLN 590 590 ?   ?   ?   B . n 
B 1 591 LYS 591 591 ?   ?   ?   B . n 
B 1 592 ILE 592 592 ?   ?   ?   B . n 
B 1 593 ARG 593 593 ?   ?   ?   B . n 
B 1 594 ARG 594 594 ?   ?   ?   B . n 
B 1 595 CYS 595 595 ?   ?   ?   B . n 
B 1 596 PHE 596 596 ?   ?   ?   B . n 
B 1 597 GLY 597 597 ?   ?   ?   B . n 
B 1 598 MET 598 598 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        LPP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   LPP 
_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        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 LPP 1 601 601 LPP LPP A . 
D 2 LPP 1 601 602 LPP LPP B . 
E 3 HOH 1 701 2   HOH HOH A . 
E 3 HOH 2 702 1   HOH HOH A . 
F 3 HOH 1 701 3   HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 79  ? CG  ? A GLU 79  CG  
2  1 Y 1 A GLU 79  ? CD  ? A GLU 79  CD  
3  1 Y 1 A GLU 79  ? OE1 ? A GLU 79  OE1 
4  1 Y 1 A GLU 79  ? OE2 ? A GLU 79  OE2 
5  1 Y 1 A LYS 300 ? CG  ? A LYS 300 CG  
6  1 Y 1 A LYS 300 ? CD  ? A LYS 300 CD  
7  1 Y 1 A LYS 300 ? CE  ? A LYS 300 CE  
8  1 Y 1 A LYS 300 ? NZ  ? A LYS 300 NZ  
9  1 Y 1 A GLU 307 ? CG  ? A GLU 307 CG  
10 1 Y 1 A GLU 307 ? CD  ? A GLU 307 CD  
11 1 Y 1 A GLU 307 ? OE1 ? A GLU 307 OE1 
12 1 Y 1 A GLU 307 ? OE2 ? A GLU 307 OE2 
13 1 Y 1 A GLU 571 ? CG  ? A GLU 571 CG  
14 1 Y 1 A GLU 571 ? CD  ? A GLU 571 CD  
15 1 Y 1 A GLU 571 ? OE1 ? A GLU 571 OE1 
16 1 Y 1 A GLU 571 ? OE2 ? A GLU 571 OE2 
17 1 Y 1 B GLU 79  ? CG  ? B GLU 79  CG  
18 1 Y 1 B GLU 79  ? CD  ? B GLU 79  CD  
19 1 Y 1 B GLU 79  ? OE1 ? B GLU 79  OE1 
20 1 Y 1 B GLU 79  ? OE2 ? B GLU 79  OE2 
21 1 Y 1 B LYS 300 ? CG  ? B LYS 300 CG  
22 1 Y 1 B LYS 300 ? CD  ? B LYS 300 CD  
23 1 Y 1 B LYS 300 ? CE  ? B LYS 300 CE  
24 1 Y 1 B LYS 300 ? NZ  ? B LYS 300 NZ  
25 1 Y 1 B GLU 307 ? CG  ? B GLU 307 CG  
26 1 Y 1 B GLU 307 ? CD  ? B GLU 307 CD  
27 1 Y 1 B GLU 307 ? OE1 ? B GLU 307 OE1 
28 1 Y 1 B GLU 307 ? OE2 ? B GLU 307 OE2 
29 1 Y 1 B GLU 571 ? CG  ? B GLU 571 CG  
30 1 Y 1 B GLU 571 ? CD  ? B GLU 571 CD  
31 1 Y 1 B GLU 571 ? OE1 ? B GLU 571 OE1 
32 1 Y 1 B GLU 571 ? OE2 ? B GLU 571 OE2 
# 
_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                     8ZTK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZTK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZTK 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_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                                 8ZTK 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_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                            . 
_refine.ls_d_res_low                             ? 
_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                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_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                    ? 
_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                          ? 
_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               NONE 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_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                    ? 
# 
_struct.entry_id                     8ZTK 
_struct.title                        'AtALMT9 with LMNG (cis2 class)' 
_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        8ZTK 
_struct_keywords.text            'Plant, Stomata, Vacuole, ALMT, Ion channel, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ALMT9_ARATH 
_struct_ref.pdbx_db_accession          Q9LS46 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAAKQGSFRHGILEKRERLLSNNGFSDFRFTDIESNDLLENENCGRRTRLCCCCSCGNLSEKISGVYDDAKDVARKAWEM
GVSDPRKIVFSAKIGLALTIVALLIFYQEPNPDLSRYSVWAILTVVVVFEFTIGATLSKGFNRALGTLSAGGLALGMAEL
STLFGDWEEIFCTLSIFCIGFLATFMKLYPSMKAYEYGFRVFLLTYCYILISGFRTGQFIEVAISRFLLIALGAGVSLGV
NMFIYPIWAGEDLHNLVVKNFMNVATSLEGCVNGYLRCLEYERIPSKILTYQASEDPVYKGYRSAVESTSQEESLMSFAI
WEPPHGPYKSFNYPWKNYVKLSGALKHCAFTVMALHGCILSEIQAPEERRQVFRQELQRVGVEGAKLLRELGEKVKKMEK
LGPVDLLFEVHLAAEELQHKIDKKSYLLVNSECWEIGNRATKESEPQELLSLEDSDPPENHAPPIYAFKSLSEAVLEIPP
SWGEKNHREALNHRPTFSKQVSWPARLVLPPHLETTNGASPLVETTKTYESASALSLATFASLLIEFVARLQNVVDAFKE
LSQKANFKEPEIVTTGTDVEFSGERVGLGQKIRRCFGM
;
_struct_ref.pdbx_align_begin           1 
# 
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 8ZTK A 1 ? 598 ? Q9LS46 1 ? 598 ? 1 598 
2 1 8ZTK B 1 ? 598 ? Q9LS46 1 ? 598 ? 1 598 
# 
_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 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 77  ? ASP A 84  ? ALA A 77  ASP A 84  1 ? 8  
HELX_P HELX_P2  AA2 ASP A 84  ? TYR A 107 ? ASP A 84  TYR A 107 1 ? 24 
HELX_P HELX_P3  AA3 ASN A 111 ? ARG A 116 ? ASN A 111 ARG A 116 1 ? 6  
HELX_P HELX_P4  AA4 SER A 118 ? VAL A 128 ? SER A 118 VAL A 128 1 ? 11 
HELX_P HELX_P5  AA5 THR A 132 ? GLY A 165 ? THR A 132 GLY A 165 1 ? 34 
HELX_P HELX_P6  AA6 TRP A 167 ? MET A 186 ? TRP A 167 MET A 186 1 ? 20 
HELX_P HELX_P7  AA7 TYR A 189 ? LYS A 193 ? TYR A 189 LYS A 193 5 ? 5  
HELX_P HELX_P8  AA8 TYR A 195 ? ILE A 209 ? TYR A 195 ILE A 209 1 ? 15 
HELX_P HELX_P9  AA9 GLY A 217 ? PHE A 243 ? GLY A 217 PHE A 243 1 ? 27 
HELX_P HELX_P10 AB1 TRP A 248 ? ARG A 277 ? TRP A 248 ARG A 277 1 ? 30 
HELX_P HELX_P11 AB2 TYR A 299 ? GLU A 307 ? TYR A 299 GLU A 307 1 ? 9  
HELX_P HELX_P12 AB3 SER A 308 ? ALA A 319 ? SER A 308 ALA A 319 1 ? 12 
HELX_P HELX_P13 AB4 TRP A 335 ? CYS A 358 ? TRP A 335 CYS A 358 1 ? 24 
HELX_P HELX_P14 AB5 ILE A 359 ? SER A 361 ? ILE A 359 SER A 361 5 ? 3  
HELX_P HELX_P15 AB6 PRO A 366 ? GLN A 371 ? PRO A 366 GLN A 371 1 ? 6  
HELX_P HELX_P16 AB7 PHE A 373 ? MET A 398 ? PHE A 373 MET A 398 1 ? 26 
HELX_P HELX_P17 AB8 LEU A 407 ? LYS A 424 ? LEU A 407 LYS A 424 1 ? 18 
HELX_P HELX_P18 AB9 SER A 425 ? LEU A 428 ? SER A 425 LEU A 428 5 ? 4  
HELX_P HELX_P19 AC1 THR A 528 ? ARG A 550 ? THR A 528 ARG A 550 1 ? 23 
HELX_P HELX_P20 AC2 LEU A 551 ? ALA A 565 ? LEU A 551 ALA A 565 1 ? 15 
HELX_P HELX_P21 AC3 TRP B 78  ? ASP B 84  ? TRP B 78  ASP B 84  1 ? 7  
HELX_P HELX_P22 AC4 ASP B 84  ? TYR B 107 ? ASP B 84  TYR B 107 1 ? 24 
HELX_P HELX_P23 AC5 ASN B 111 ? ARG B 116 ? ASN B 111 ARG B 116 1 ? 6  
HELX_P HELX_P24 AC6 SER B 118 ? VAL B 128 ? SER B 118 VAL B 128 1 ? 11 
HELX_P HELX_P25 AC7 THR B 132 ? GLY B 165 ? THR B 132 GLY B 165 1 ? 34 
HELX_P HELX_P26 AC8 TRP B 167 ? MET B 186 ? TRP B 167 MET B 186 1 ? 20 
HELX_P HELX_P27 AC9 TYR B 189 ? LYS B 193 ? TYR B 189 LYS B 193 5 ? 5  
HELX_P HELX_P28 AD1 TYR B 195 ? ILE B 209 ? TYR B 195 ILE B 209 1 ? 15 
HELX_P HELX_P29 AD2 GLY B 217 ? PHE B 243 ? GLY B 217 PHE B 243 1 ? 27 
HELX_P HELX_P30 AD3 TRP B 248 ? ARG B 277 ? TRP B 248 ARG B 277 1 ? 30 
HELX_P HELX_P31 AD4 TYR B 299 ? GLU B 307 ? TYR B 299 GLU B 307 1 ? 9  
HELX_P HELX_P32 AD5 SER B 308 ? ILE B 320 ? SER B 308 ILE B 320 1 ? 13 
HELX_P HELX_P33 AD6 TRP B 335 ? CYS B 358 ? TRP B 335 CYS B 358 1 ? 24 
HELX_P HELX_P34 AD7 ILE B 359 ? SER B 361 ? ILE B 359 SER B 361 5 ? 3  
HELX_P HELX_P35 AD8 PRO B 366 ? GLN B 371 ? PRO B 366 GLN B 371 1 ? 6  
HELX_P HELX_P36 AD9 PHE B 373 ? MET B 398 ? PHE B 373 MET B 398 1 ? 26 
HELX_P HELX_P37 AE1 LEU B 407 ? LYS B 424 ? LEU B 407 LYS B 424 1 ? 18 
HELX_P HELX_P38 AE2 SER B 425 ? LEU B 428 ? SER B 425 LEU B 428 5 ? 4  
HELX_P HELX_P39 AE3 THR B 528 ? ARG B 550 ? THR B 528 ARG B 550 1 ? 23 
HELX_P HELX_P40 AE4 LEU B 551 ? ALA B 565 ? LEU B 551 ALA B 565 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   8ZTK 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 104 ? ? -68.81  3.78  
2  1 MET A 192 ? ? -104.59 40.09 
3  1 TYR A 195 ? ? -95.52  50.02 
4  1 GLU A 307 ? ? -107.17 62.58 
5  1 SER A 308 ? ? -144.51 -4.14 
6  1 PRO A 334 ? ? -67.28  77.63 
7  1 LEU B 104 ? ? -68.79  3.72  
8  1 MET B 192 ? ? -104.56 40.13 
9  1 TYR B 195 ? ? -95.47  49.96 
10 1 GLU B 307 ? ? -107.19 62.68 
11 1 SER B 308 ? ? -144.54 -4.14 
12 1 PRO B 334 ? ? -67.28  77.63 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8ZTK 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    8ZTK 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   'FOURIER SPACE' 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.78 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               76531 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          2 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.6 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'AtALMT9 with LMNG' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8ZTK 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             700 
_em_imaging.nominal_defocus_max             1900 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            70 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Au-flat 1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8ZTK 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277.15 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8ZTK 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              8ZTK 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ALA 2   ? A ALA 2   
3   1 Y 1 A ALA 3   ? A ALA 3   
4   1 Y 1 A LYS 4   ? A LYS 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A GLY 6   ? A GLY 6   
7   1 Y 1 A SER 7   ? A SER 7   
8   1 Y 1 A PHE 8   ? A PHE 8   
9   1 Y 1 A ARG 9   ? A ARG 9   
10  1 Y 1 A HIS 10  ? A HIS 10  
11  1 Y 1 A GLY 11  ? A GLY 11  
12  1 Y 1 A ILE 12  ? A ILE 12  
13  1 Y 1 A LEU 13  ? A LEU 13  
14  1 Y 1 A GLU 14  ? A GLU 14  
15  1 Y 1 A LYS 15  ? A LYS 15  
16  1 Y 1 A ARG 16  ? A ARG 16  
17  1 Y 1 A GLU 17  ? A GLU 17  
18  1 Y 1 A ARG 18  ? A ARG 18  
19  1 Y 1 A LEU 19  ? A LEU 19  
20  1 Y 1 A LEU 20  ? A LEU 20  
21  1 Y 1 A SER 21  ? A SER 21  
22  1 Y 1 A ASN 22  ? A ASN 22  
23  1 Y 1 A ASN 23  ? A ASN 23  
24  1 Y 1 A GLY 24  ? A GLY 24  
25  1 Y 1 A PHE 25  ? A PHE 25  
26  1 Y 1 A SER 26  ? A SER 26  
27  1 Y 1 A ASP 27  ? A ASP 27  
28  1 Y 1 A PHE 28  ? A PHE 28  
29  1 Y 1 A ARG 29  ? A ARG 29  
30  1 Y 1 A PHE 30  ? A PHE 30  
31  1 Y 1 A THR 31  ? A THR 31  
32  1 Y 1 A ASP 32  ? A ASP 32  
33  1 Y 1 A ILE 33  ? A ILE 33  
34  1 Y 1 A GLU 34  ? A GLU 34  
35  1 Y 1 A SER 35  ? A SER 35  
36  1 Y 1 A ASN 36  ? A ASN 36  
37  1 Y 1 A ASP 37  ? A ASP 37  
38  1 Y 1 A LEU 38  ? A LEU 38  
39  1 Y 1 A LEU 39  ? A LEU 39  
40  1 Y 1 A GLU 40  ? A GLU 40  
41  1 Y 1 A ASN 41  ? A ASN 41  
42  1 Y 1 A GLU 42  ? A GLU 42  
43  1 Y 1 A ASN 43  ? A ASN 43  
44  1 Y 1 A CYS 44  ? A CYS 44  
45  1 Y 1 A GLY 45  ? A GLY 45  
46  1 Y 1 A ARG 46  ? A ARG 46  
47  1 Y 1 A ARG 47  ? A ARG 47  
48  1 Y 1 A THR 48  ? A THR 48  
49  1 Y 1 A ARG 49  ? A ARG 49  
50  1 Y 1 A LEU 50  ? A LEU 50  
51  1 Y 1 A CYS 51  ? A CYS 51  
52  1 Y 1 A CYS 52  ? A CYS 52  
53  1 Y 1 A CYS 53  ? A CYS 53  
54  1 Y 1 A CYS 54  ? A CYS 54  
55  1 Y 1 A SER 55  ? A SER 55  
56  1 Y 1 A CYS 56  ? A CYS 56  
57  1 Y 1 A GLY 57  ? A GLY 57  
58  1 Y 1 A ASN 58  ? A ASN 58  
59  1 Y 1 A LEU 59  ? A LEU 59  
60  1 Y 1 A SER 60  ? A SER 60  
61  1 Y 1 A GLU 61  ? A GLU 61  
62  1 Y 1 A LYS 62  ? A LYS 62  
63  1 Y 1 A ILE 63  ? A ILE 63  
64  1 Y 1 A SER 64  ? A SER 64  
65  1 Y 1 A GLY 65  ? A GLY 65  
66  1 Y 1 A VAL 66  ? A VAL 66  
67  1 Y 1 A TYR 67  ? A TYR 67  
68  1 Y 1 A ASP 68  ? A ASP 68  
69  1 Y 1 A ASP 69  ? A ASP 69  
70  1 Y 1 A ALA 70  ? A ALA 70  
71  1 Y 1 A LYS 71  ? A LYS 71  
72  1 Y 1 A ASP 72  ? A ASP 72  
73  1 Y 1 A VAL 73  ? A VAL 73  
74  1 Y 1 A ALA 74  ? A ALA 74  
75  1 Y 1 A ARG 75  ? A ARG 75  
76  1 Y 1 A LYS 76  ? A LYS 76  
77  1 Y 1 A LEU 279 ? A LEU 279 
78  1 Y 1 A GLU 280 ? A GLU 280 
79  1 Y 1 A TYR 281 ? A TYR 281 
80  1 Y 1 A GLU 282 ? A GLU 282 
81  1 Y 1 A ARG 283 ? A ARG 283 
82  1 Y 1 A ILE 284 ? A ILE 284 
83  1 Y 1 A PRO 285 ? A PRO 285 
84  1 Y 1 A SER 286 ? A SER 286 
85  1 Y 1 A LYS 287 ? A LYS 287 
86  1 Y 1 A ILE 288 ? A ILE 288 
87  1 Y 1 A LEU 289 ? A LEU 289 
88  1 Y 1 A THR 290 ? A THR 290 
89  1 Y 1 A TYR 291 ? A TYR 291 
90  1 Y 1 A GLN 292 ? A GLN 292 
91  1 Y 1 A ALA 293 ? A ALA 293 
92  1 Y 1 A SER 294 ? A SER 294 
93  1 Y 1 A GLU 295 ? A GLU 295 
94  1 Y 1 A ASP 296 ? A ASP 296 
95  1 Y 1 A PRO 297 ? A PRO 297 
96  1 Y 1 A ILE 436 ? A ILE 436 
97  1 Y 1 A GLY 437 ? A GLY 437 
98  1 Y 1 A ASN 438 ? A ASN 438 
99  1 Y 1 A ARG 439 ? A ARG 439 
100 1 Y 1 A ALA 440 ? A ALA 440 
101 1 Y 1 A THR 441 ? A THR 441 
102 1 Y 1 A LYS 442 ? A LYS 442 
103 1 Y 1 A GLU 443 ? A GLU 443 
104 1 Y 1 A SER 444 ? A SER 444 
105 1 Y 1 A GLU 445 ? A GLU 445 
106 1 Y 1 A PRO 446 ? A PRO 446 
107 1 Y 1 A GLN 447 ? A GLN 447 
108 1 Y 1 A GLU 448 ? A GLU 448 
109 1 Y 1 A LEU 449 ? A LEU 449 
110 1 Y 1 A LEU 450 ? A LEU 450 
111 1 Y 1 A SER 451 ? A SER 451 
112 1 Y 1 A LEU 452 ? A LEU 452 
113 1 Y 1 A GLU 453 ? A GLU 453 
114 1 Y 1 A ASP 454 ? A ASP 454 
115 1 Y 1 A SER 455 ? A SER 455 
116 1 Y 1 A ASP 456 ? A ASP 456 
117 1 Y 1 A PRO 457 ? A PRO 457 
118 1 Y 1 A PRO 458 ? A PRO 458 
119 1 Y 1 A GLU 459 ? A GLU 459 
120 1 Y 1 A ASN 460 ? A ASN 460 
121 1 Y 1 A HIS 461 ? A HIS 461 
122 1 Y 1 A ALA 462 ? A ALA 462 
123 1 Y 1 A PRO 463 ? A PRO 463 
124 1 Y 1 A PRO 464 ? A PRO 464 
125 1 Y 1 A ILE 465 ? A ILE 465 
126 1 Y 1 A TYR 466 ? A TYR 466 
127 1 Y 1 A ALA 467 ? A ALA 467 
128 1 Y 1 A PHE 468 ? A PHE 468 
129 1 Y 1 A LYS 469 ? A LYS 469 
130 1 Y 1 A SER 470 ? A SER 470 
131 1 Y 1 A LEU 471 ? A LEU 471 
132 1 Y 1 A SER 472 ? A SER 472 
133 1 Y 1 A GLU 473 ? A GLU 473 
134 1 Y 1 A ALA 474 ? A ALA 474 
135 1 Y 1 A VAL 475 ? A VAL 475 
136 1 Y 1 A LEU 476 ? A LEU 476 
137 1 Y 1 A GLU 477 ? A GLU 477 
138 1 Y 1 A ILE 478 ? A ILE 478 
139 1 Y 1 A PRO 479 ? A PRO 479 
140 1 Y 1 A PRO 480 ? A PRO 480 
141 1 Y 1 A SER 481 ? A SER 481 
142 1 Y 1 A TRP 482 ? A TRP 482 
143 1 Y 1 A GLY 483 ? A GLY 483 
144 1 Y 1 A GLU 484 ? A GLU 484 
145 1 Y 1 A LYS 485 ? A LYS 485 
146 1 Y 1 A ASN 486 ? A ASN 486 
147 1 Y 1 A HIS 487 ? A HIS 487 
148 1 Y 1 A ARG 488 ? A ARG 488 
149 1 Y 1 A GLU 489 ? A GLU 489 
150 1 Y 1 A ALA 490 ? A ALA 490 
151 1 Y 1 A LEU 491 ? A LEU 491 
152 1 Y 1 A ASN 492 ? A ASN 492 
153 1 Y 1 A HIS 493 ? A HIS 493 
154 1 Y 1 A ARG 494 ? A ARG 494 
155 1 Y 1 A PRO 495 ? A PRO 495 
156 1 Y 1 A THR 496 ? A THR 496 
157 1 Y 1 A PHE 497 ? A PHE 497 
158 1 Y 1 A SER 498 ? A SER 498 
159 1 Y 1 A LYS 499 ? A LYS 499 
160 1 Y 1 A GLN 500 ? A GLN 500 
161 1 Y 1 A VAL 501 ? A VAL 501 
162 1 Y 1 A SER 502 ? A SER 502 
163 1 Y 1 A TRP 503 ? A TRP 503 
164 1 Y 1 A PRO 504 ? A PRO 504 
165 1 Y 1 A ALA 505 ? A ALA 505 
166 1 Y 1 A ARG 506 ? A ARG 506 
167 1 Y 1 A LEU 507 ? A LEU 507 
168 1 Y 1 A VAL 508 ? A VAL 508 
169 1 Y 1 A LEU 509 ? A LEU 509 
170 1 Y 1 A PRO 510 ? A PRO 510 
171 1 Y 1 A PRO 511 ? A PRO 511 
172 1 Y 1 A HIS 512 ? A HIS 512 
173 1 Y 1 A LEU 513 ? A LEU 513 
174 1 Y 1 A GLU 514 ? A GLU 514 
175 1 Y 1 A THR 515 ? A THR 515 
176 1 Y 1 A THR 516 ? A THR 516 
177 1 Y 1 A ASN 517 ? A ASN 517 
178 1 Y 1 A GLY 518 ? A GLY 518 
179 1 Y 1 A ALA 519 ? A ALA 519 
180 1 Y 1 A SER 520 ? A SER 520 
181 1 Y 1 A PRO 521 ? A PRO 521 
182 1 Y 1 A LEU 522 ? A LEU 522 
183 1 Y 1 A VAL 523 ? A VAL 523 
184 1 Y 1 A GLU 524 ? A GLU 524 
185 1 Y 1 A THR 525 ? A THR 525 
186 1 Y 1 A THR 526 ? A THR 526 
187 1 Y 1 A ILE 572 ? A ILE 572 
188 1 Y 1 A VAL 573 ? A VAL 573 
189 1 Y 1 A THR 574 ? A THR 574 
190 1 Y 1 A THR 575 ? A THR 575 
191 1 Y 1 A GLY 576 ? A GLY 576 
192 1 Y 1 A THR 577 ? A THR 577 
193 1 Y 1 A ASP 578 ? A ASP 578 
194 1 Y 1 A VAL 579 ? A VAL 579 
195 1 Y 1 A GLU 580 ? A GLU 580 
196 1 Y 1 A PHE 581 ? A PHE 581 
197 1 Y 1 A SER 582 ? A SER 582 
198 1 Y 1 A GLY 583 ? A GLY 583 
199 1 Y 1 A GLU 584 ? A GLU 584 
200 1 Y 1 A ARG 585 ? A ARG 585 
201 1 Y 1 A VAL 586 ? A VAL 586 
202 1 Y 1 A GLY 587 ? A GLY 587 
203 1 Y 1 A LEU 588 ? A LEU 588 
204 1 Y 1 A GLY 589 ? A GLY 589 
205 1 Y 1 A GLN 590 ? A GLN 590 
206 1 Y 1 A LYS 591 ? A LYS 591 
207 1 Y 1 A ILE 592 ? A ILE 592 
208 1 Y 1 A ARG 593 ? A ARG 593 
209 1 Y 1 A ARG 594 ? A ARG 594 
210 1 Y 1 A CYS 595 ? A CYS 595 
211 1 Y 1 A PHE 596 ? A PHE 596 
212 1 Y 1 A GLY 597 ? A GLY 597 
213 1 Y 1 A MET 598 ? A MET 598 
214 1 Y 1 B MET 1   ? B MET 1   
215 1 Y 1 B ALA 2   ? B ALA 2   
216 1 Y 1 B ALA 3   ? B ALA 3   
217 1 Y 1 B LYS 4   ? B LYS 4   
218 1 Y 1 B GLN 5   ? B GLN 5   
219 1 Y 1 B GLY 6   ? B GLY 6   
220 1 Y 1 B SER 7   ? B SER 7   
221 1 Y 1 B PHE 8   ? B PHE 8   
222 1 Y 1 B ARG 9   ? B ARG 9   
223 1 Y 1 B HIS 10  ? B HIS 10  
224 1 Y 1 B GLY 11  ? B GLY 11  
225 1 Y 1 B ILE 12  ? B ILE 12  
226 1 Y 1 B LEU 13  ? B LEU 13  
227 1 Y 1 B GLU 14  ? B GLU 14  
228 1 Y 1 B LYS 15  ? B LYS 15  
229 1 Y 1 B ARG 16  ? B ARG 16  
230 1 Y 1 B GLU 17  ? B GLU 17  
231 1 Y 1 B ARG 18  ? B ARG 18  
232 1 Y 1 B LEU 19  ? B LEU 19  
233 1 Y 1 B LEU 20  ? B LEU 20  
234 1 Y 1 B SER 21  ? B SER 21  
235 1 Y 1 B ASN 22  ? B ASN 22  
236 1 Y 1 B ASN 23  ? B ASN 23  
237 1 Y 1 B GLY 24  ? B GLY 24  
238 1 Y 1 B PHE 25  ? B PHE 25  
239 1 Y 1 B SER 26  ? B SER 26  
240 1 Y 1 B ASP 27  ? B ASP 27  
241 1 Y 1 B PHE 28  ? B PHE 28  
242 1 Y 1 B ARG 29  ? B ARG 29  
243 1 Y 1 B PHE 30  ? B PHE 30  
244 1 Y 1 B THR 31  ? B THR 31  
245 1 Y 1 B ASP 32  ? B ASP 32  
246 1 Y 1 B ILE 33  ? B ILE 33  
247 1 Y 1 B GLU 34  ? B GLU 34  
248 1 Y 1 B SER 35  ? B SER 35  
249 1 Y 1 B ASN 36  ? B ASN 36  
250 1 Y 1 B ASP 37  ? B ASP 37  
251 1 Y 1 B LEU 38  ? B LEU 38  
252 1 Y 1 B LEU 39  ? B LEU 39  
253 1 Y 1 B GLU 40  ? B GLU 40  
254 1 Y 1 B ASN 41  ? B ASN 41  
255 1 Y 1 B GLU 42  ? B GLU 42  
256 1 Y 1 B ASN 43  ? B ASN 43  
257 1 Y 1 B CYS 44  ? B CYS 44  
258 1 Y 1 B GLY 45  ? B GLY 45  
259 1 Y 1 B ARG 46  ? B ARG 46  
260 1 Y 1 B ARG 47  ? B ARG 47  
261 1 Y 1 B THR 48  ? B THR 48  
262 1 Y 1 B ARG 49  ? B ARG 49  
263 1 Y 1 B LEU 50  ? B LEU 50  
264 1 Y 1 B CYS 51  ? B CYS 51  
265 1 Y 1 B CYS 52  ? B CYS 52  
266 1 Y 1 B CYS 53  ? B CYS 53  
267 1 Y 1 B CYS 54  ? B CYS 54  
268 1 Y 1 B SER 55  ? B SER 55  
269 1 Y 1 B CYS 56  ? B CYS 56  
270 1 Y 1 B GLY 57  ? B GLY 57  
271 1 Y 1 B ASN 58  ? B ASN 58  
272 1 Y 1 B LEU 59  ? B LEU 59  
273 1 Y 1 B SER 60  ? B SER 60  
274 1 Y 1 B GLU 61  ? B GLU 61  
275 1 Y 1 B LYS 62  ? B LYS 62  
276 1 Y 1 B ILE 63  ? B ILE 63  
277 1 Y 1 B SER 64  ? B SER 64  
278 1 Y 1 B GLY 65  ? B GLY 65  
279 1 Y 1 B VAL 66  ? B VAL 66  
280 1 Y 1 B TYR 67  ? B TYR 67  
281 1 Y 1 B ASP 68  ? B ASP 68  
282 1 Y 1 B ASP 69  ? B ASP 69  
283 1 Y 1 B ALA 70  ? B ALA 70  
284 1 Y 1 B LYS 71  ? B LYS 71  
285 1 Y 1 B ASP 72  ? B ASP 72  
286 1 Y 1 B VAL 73  ? B VAL 73  
287 1 Y 1 B ALA 74  ? B ALA 74  
288 1 Y 1 B ARG 75  ? B ARG 75  
289 1 Y 1 B LYS 76  ? B LYS 76  
290 1 Y 1 B LEU 279 ? B LEU 279 
291 1 Y 1 B GLU 280 ? B GLU 280 
292 1 Y 1 B TYR 281 ? B TYR 281 
293 1 Y 1 B GLU 282 ? B GLU 282 
294 1 Y 1 B ARG 283 ? B ARG 283 
295 1 Y 1 B ILE 284 ? B ILE 284 
296 1 Y 1 B PRO 285 ? B PRO 285 
297 1 Y 1 B SER 286 ? B SER 286 
298 1 Y 1 B LYS 287 ? B LYS 287 
299 1 Y 1 B ILE 288 ? B ILE 288 
300 1 Y 1 B LEU 289 ? B LEU 289 
301 1 Y 1 B THR 290 ? B THR 290 
302 1 Y 1 B TYR 291 ? B TYR 291 
303 1 Y 1 B GLN 292 ? B GLN 292 
304 1 Y 1 B ALA 293 ? B ALA 293 
305 1 Y 1 B SER 294 ? B SER 294 
306 1 Y 1 B GLU 295 ? B GLU 295 
307 1 Y 1 B ASP 296 ? B ASP 296 
308 1 Y 1 B PRO 297 ? B PRO 297 
309 1 Y 1 B ILE 436 ? B ILE 436 
310 1 Y 1 B GLY 437 ? B GLY 437 
311 1 Y 1 B ASN 438 ? B ASN 438 
312 1 Y 1 B ARG 439 ? B ARG 439 
313 1 Y 1 B ALA 440 ? B ALA 440 
314 1 Y 1 B THR 441 ? B THR 441 
315 1 Y 1 B LYS 442 ? B LYS 442 
316 1 Y 1 B GLU 443 ? B GLU 443 
317 1 Y 1 B SER 444 ? B SER 444 
318 1 Y 1 B GLU 445 ? B GLU 445 
319 1 Y 1 B PRO 446 ? B PRO 446 
320 1 Y 1 B GLN 447 ? B GLN 447 
321 1 Y 1 B GLU 448 ? B GLU 448 
322 1 Y 1 B LEU 449 ? B LEU 449 
323 1 Y 1 B LEU 450 ? B LEU 450 
324 1 Y 1 B SER 451 ? B SER 451 
325 1 Y 1 B LEU 452 ? B LEU 452 
326 1 Y 1 B GLU 453 ? B GLU 453 
327 1 Y 1 B ASP 454 ? B ASP 454 
328 1 Y 1 B SER 455 ? B SER 455 
329 1 Y 1 B ASP 456 ? B ASP 456 
330 1 Y 1 B PRO 457 ? B PRO 457 
331 1 Y 1 B PRO 458 ? B PRO 458 
332 1 Y 1 B GLU 459 ? B GLU 459 
333 1 Y 1 B ASN 460 ? B ASN 460 
334 1 Y 1 B HIS 461 ? B HIS 461 
335 1 Y 1 B ALA 462 ? B ALA 462 
336 1 Y 1 B PRO 463 ? B PRO 463 
337 1 Y 1 B PRO 464 ? B PRO 464 
338 1 Y 1 B ILE 465 ? B ILE 465 
339 1 Y 1 B TYR 466 ? B TYR 466 
340 1 Y 1 B ALA 467 ? B ALA 467 
341 1 Y 1 B PHE 468 ? B PHE 468 
342 1 Y 1 B LYS 469 ? B LYS 469 
343 1 Y 1 B SER 470 ? B SER 470 
344 1 Y 1 B LEU 471 ? B LEU 471 
345 1 Y 1 B SER 472 ? B SER 472 
346 1 Y 1 B GLU 473 ? B GLU 473 
347 1 Y 1 B ALA 474 ? B ALA 474 
348 1 Y 1 B VAL 475 ? B VAL 475 
349 1 Y 1 B LEU 476 ? B LEU 476 
350 1 Y 1 B GLU 477 ? B GLU 477 
351 1 Y 1 B ILE 478 ? B ILE 478 
352 1 Y 1 B PRO 479 ? B PRO 479 
353 1 Y 1 B PRO 480 ? B PRO 480 
354 1 Y 1 B SER 481 ? B SER 481 
355 1 Y 1 B TRP 482 ? B TRP 482 
356 1 Y 1 B GLY 483 ? B GLY 483 
357 1 Y 1 B GLU 484 ? B GLU 484 
358 1 Y 1 B LYS 485 ? B LYS 485 
359 1 Y 1 B ASN 486 ? B ASN 486 
360 1 Y 1 B HIS 487 ? B HIS 487 
361 1 Y 1 B ARG 488 ? B ARG 488 
362 1 Y 1 B GLU 489 ? B GLU 489 
363 1 Y 1 B ALA 490 ? B ALA 490 
364 1 Y 1 B LEU 491 ? B LEU 491 
365 1 Y 1 B ASN 492 ? B ASN 492 
366 1 Y 1 B HIS 493 ? B HIS 493 
367 1 Y 1 B ARG 494 ? B ARG 494 
368 1 Y 1 B PRO 495 ? B PRO 495 
369 1 Y 1 B THR 496 ? B THR 496 
370 1 Y 1 B PHE 497 ? B PHE 497 
371 1 Y 1 B SER 498 ? B SER 498 
372 1 Y 1 B LYS 499 ? B LYS 499 
373 1 Y 1 B GLN 500 ? B GLN 500 
374 1 Y 1 B VAL 501 ? B VAL 501 
375 1 Y 1 B SER 502 ? B SER 502 
376 1 Y 1 B TRP 503 ? B TRP 503 
377 1 Y 1 B PRO 504 ? B PRO 504 
378 1 Y 1 B ALA 505 ? B ALA 505 
379 1 Y 1 B ARG 506 ? B ARG 506 
380 1 Y 1 B LEU 507 ? B LEU 507 
381 1 Y 1 B VAL 508 ? B VAL 508 
382 1 Y 1 B LEU 509 ? B LEU 509 
383 1 Y 1 B PRO 510 ? B PRO 510 
384 1 Y 1 B PRO 511 ? B PRO 511 
385 1 Y 1 B HIS 512 ? B HIS 512 
386 1 Y 1 B LEU 513 ? B LEU 513 
387 1 Y 1 B GLU 514 ? B GLU 514 
388 1 Y 1 B THR 515 ? B THR 515 
389 1 Y 1 B THR 516 ? B THR 516 
390 1 Y 1 B ASN 517 ? B ASN 517 
391 1 Y 1 B GLY 518 ? B GLY 518 
392 1 Y 1 B ALA 519 ? B ALA 519 
393 1 Y 1 B SER 520 ? B SER 520 
394 1 Y 1 B PRO 521 ? B PRO 521 
395 1 Y 1 B LEU 522 ? B LEU 522 
396 1 Y 1 B VAL 523 ? B VAL 523 
397 1 Y 1 B GLU 524 ? B GLU 524 
398 1 Y 1 B THR 525 ? B THR 525 
399 1 Y 1 B THR 526 ? B THR 526 
400 1 Y 1 B ILE 572 ? B ILE 572 
401 1 Y 1 B VAL 573 ? B VAL 573 
402 1 Y 1 B THR 574 ? B THR 574 
403 1 Y 1 B THR 575 ? B THR 575 
404 1 Y 1 B GLY 576 ? B GLY 576 
405 1 Y 1 B THR 577 ? B THR 577 
406 1 Y 1 B ASP 578 ? B ASP 578 
407 1 Y 1 B VAL 579 ? B VAL 579 
408 1 Y 1 B GLU 580 ? B GLU 580 
409 1 Y 1 B PHE 581 ? B PHE 581 
410 1 Y 1 B SER 582 ? B SER 582 
411 1 Y 1 B GLY 583 ? B GLY 583 
412 1 Y 1 B GLU 584 ? B GLU 584 
413 1 Y 1 B ARG 585 ? B ARG 585 
414 1 Y 1 B VAL 586 ? B VAL 586 
415 1 Y 1 B GLY 587 ? B GLY 587 
416 1 Y 1 B LEU 588 ? B LEU 588 
417 1 Y 1 B GLY 589 ? B GLY 589 
418 1 Y 1 B GLN 590 ? B GLN 590 
419 1 Y 1 B LYS 591 ? B LYS 591 
420 1 Y 1 B ILE 592 ? B ILE 592 
421 1 Y 1 B ARG 593 ? B ARG 593 
422 1 Y 1 B ARG 594 ? B ARG 594 
423 1 Y 1 B CYS 595 ? B CYS 595 
424 1 Y 1 B PHE 596 ? B PHE 596 
425 1 Y 1 B GLY 597 ? B GLY 597 
426 1 Y 1 B MET 598 ? B MET 598 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LPP P1   P N N 205 
LPP O2   O N N 206 
LPP O3   O N N 207 
LPP O4   O N N 208 
LPP O5   O N N 209 
LPP C6   C N N 210 
LPP C7   C N R 211 
LPP C8   C N N 212 
LPP O9   O N N 213 
LPP O27  O N N 214 
LPP C11  C N N 215 
LPP O10  O N N 216 
LPP C12  C N N 217 
LPP C13  C N N 218 
LPP C14  C N N 219 
LPP C15  C N N 220 
LPP C16  C N N 221 
LPP C17  C N N 222 
LPP C18  C N N 223 
LPP C19  C N N 224 
LPP C20  C N N 225 
LPP C21  C N N 226 
LPP C22  C N N 227 
LPP C23  C N N 228 
LPP C24  C N N 229 
LPP C25  C N N 230 
LPP C26  C N N 231 
LPP C29  C N N 232 
LPP O28  O N N 233 
LPP C30  C N N 234 
LPP C31  C N N 235 
LPP C32  C N N 236 
LPP C33  C N N 237 
LPP C34  C N N 238 
LPP C35  C N N 239 
LPP C36  C N N 240 
LPP C37  C N N 241 
LPP C38  C N N 242 
LPP C39  C N N 243 
LPP C40  C N N 244 
LPP C41  C N N 245 
LPP C42  C N N 246 
LPP C43  C N N 247 
LPP C44  C N N 248 
LPP HO2  H N N 249 
LPP HO4  H N N 250 
LPP HC61 H N N 251 
LPP HC62 H N N 252 
LPP HC7  H N N 253 
LPP HC81 H N N 254 
LPP HC82 H N N 255 
LPP H121 H N N 256 
LPP H122 H N N 257 
LPP H131 H N N 258 
LPP H132 H N N 259 
LPP H141 H N N 260 
LPP H142 H N N 261 
LPP H151 H N N 262 
LPP H152 H N N 263 
LPP H161 H N N 264 
LPP H162 H N N 265 
LPP H171 H N N 266 
LPP H172 H N N 267 
LPP H181 H N N 268 
LPP H182 H N N 269 
LPP H191 H N N 270 
LPP H192 H N N 271 
LPP H201 H N N 272 
LPP H202 H N N 273 
LPP H211 H N N 274 
LPP H212 H N N 275 
LPP H221 H N N 276 
LPP H222 H N N 277 
LPP H231 H N N 278 
LPP H232 H N N 279 
LPP H241 H N N 280 
LPP H242 H N N 281 
LPP H251 H N N 282 
LPP H252 H N N 283 
LPP H261 H N N 284 
LPP H262 H N N 285 
LPP H263 H N N 286 
LPP H301 H N N 287 
LPP H302 H N N 288 
LPP H311 H N N 289 
LPP H312 H N N 290 
LPP H321 H N N 291 
LPP H322 H N N 292 
LPP H331 H N N 293 
LPP H332 H N N 294 
LPP H341 H N N 295 
LPP H342 H N N 296 
LPP H351 H N N 297 
LPP H352 H N N 298 
LPP H361 H N N 299 
LPP H362 H N N 300 
LPP H371 H N N 301 
LPP H372 H N N 302 
LPP H381 H N N 303 
LPP H382 H N N 304 
LPP H391 H N N 305 
LPP H392 H N N 306 
LPP H401 H N N 307 
LPP H402 H N N 308 
LPP H411 H N N 309 
LPP H412 H N N 310 
LPP H421 H N N 311 
LPP H422 H N N 312 
LPP H431 H N N 313 
LPP H432 H N N 314 
LPP H441 H N N 315 
LPP H442 H N N 316 
LPP H443 H N N 317 
LYS N    N N N 318 
LYS CA   C N S 319 
LYS C    C N N 320 
LYS O    O N N 321 
LYS CB   C N N 322 
LYS CG   C N N 323 
LYS CD   C N N 324 
LYS CE   C N N 325 
LYS NZ   N N N 326 
LYS OXT  O N N 327 
LYS H    H N N 328 
LYS H2   H N N 329 
LYS HA   H N N 330 
LYS HB2  H N N 331 
LYS HB3  H N N 332 
LYS HG2  H N N 333 
LYS HG3  H N N 334 
LYS HD2  H N N 335 
LYS HD3  H N N 336 
LYS HE2  H N N 337 
LYS HE3  H N N 338 
LYS HZ1  H N N 339 
LYS HZ2  H N N 340 
LYS HZ3  H N N 341 
LYS HXT  H N N 342 
MET N    N N N 343 
MET CA   C N S 344 
MET C    C N N 345 
MET O    O N N 346 
MET CB   C N N 347 
MET CG   C N N 348 
MET SD   S N N 349 
MET CE   C N N 350 
MET OXT  O N N 351 
MET H    H N N 352 
MET H2   H N N 353 
MET HA   H N N 354 
MET HB2  H N N 355 
MET HB3  H N N 356 
MET HG2  H N N 357 
MET HG3  H N N 358 
MET HE1  H N N 359 
MET HE2  H N N 360 
MET HE3  H N N 361 
MET HXT  H N N 362 
PHE N    N N N 363 
PHE CA   C N S 364 
PHE C    C N N 365 
PHE O    O N N 366 
PHE CB   C N N 367 
PHE CG   C Y N 368 
PHE CD1  C Y N 369 
PHE CD2  C Y N 370 
PHE CE1  C Y N 371 
PHE CE2  C Y N 372 
PHE CZ   C Y N 373 
PHE OXT  O N N 374 
PHE H    H N N 375 
PHE H2   H N N 376 
PHE HA   H N N 377 
PHE HB2  H N N 378 
PHE HB3  H N N 379 
PHE HD1  H N N 380 
PHE HD2  H N N 381 
PHE HE1  H N N 382 
PHE HE2  H N N 383 
PHE HZ   H N N 384 
PHE HXT  H N N 385 
PRO N    N N N 386 
PRO CA   C N S 387 
PRO C    C N N 388 
PRO O    O N N 389 
PRO CB   C N N 390 
PRO CG   C N N 391 
PRO CD   C N N 392 
PRO OXT  O N N 393 
PRO H    H N N 394 
PRO HA   H N N 395 
PRO HB2  H N N 396 
PRO HB3  H N N 397 
PRO HG2  H N N 398 
PRO HG3  H N N 399 
PRO HD2  H N N 400 
PRO HD3  H N N 401 
PRO HXT  H N N 402 
SER N    N N N 403 
SER CA   C N S 404 
SER C    C N N 405 
SER O    O N N 406 
SER CB   C N N 407 
SER OG   O N N 408 
SER OXT  O N N 409 
SER H    H N N 410 
SER H2   H N N 411 
SER HA   H N N 412 
SER HB2  H N N 413 
SER HB3  H N N 414 
SER HG   H N N 415 
SER HXT  H N N 416 
THR N    N N N 417 
THR CA   C N S 418 
THR C    C N N 419 
THR O    O N N 420 
THR CB   C N R 421 
THR OG1  O N N 422 
THR CG2  C N N 423 
THR OXT  O N N 424 
THR H    H N N 425 
THR H2   H N N 426 
THR HA   H N N 427 
THR HB   H N N 428 
THR HG1  H N N 429 
THR HG21 H N N 430 
THR HG22 H N N 431 
THR HG23 H N N 432 
THR HXT  H N N 433 
TRP N    N N N 434 
TRP CA   C N S 435 
TRP C    C N N 436 
TRP O    O N N 437 
TRP CB   C N N 438 
TRP CG   C Y N 439 
TRP CD1  C Y N 440 
TRP CD2  C Y N 441 
TRP NE1  N Y N 442 
TRP CE2  C Y N 443 
TRP CE3  C Y N 444 
TRP CZ2  C Y N 445 
TRP CZ3  C Y N 446 
TRP CH2  C Y N 447 
TRP OXT  O N N 448 
TRP H    H N N 449 
TRP H2   H N N 450 
TRP HA   H N N 451 
TRP HB2  H N N 452 
TRP HB3  H N N 453 
TRP HD1  H N N 454 
TRP HE1  H N N 455 
TRP HE3  H N N 456 
TRP HZ2  H N N 457 
TRP HZ3  H N N 458 
TRP HH2  H N N 459 
TRP HXT  H N N 460 
TYR N    N N N 461 
TYR CA   C N S 462 
TYR C    C N N 463 
TYR O    O N N 464 
TYR CB   C N N 465 
TYR CG   C Y N 466 
TYR CD1  C Y N 467 
TYR CD2  C Y N 468 
TYR CE1  C Y N 469 
TYR CE2  C Y N 470 
TYR CZ   C Y N 471 
TYR OH   O N N 472 
TYR OXT  O N N 473 
TYR H    H N N 474 
TYR H2   H N N 475 
TYR HA   H N N 476 
TYR HB2  H N N 477 
TYR HB3  H N N 478 
TYR HD1  H N N 479 
TYR HD2  H N N 480 
TYR HE1  H N N 481 
TYR HE2  H N N 482 
TYR HH   H N N 483 
TYR HXT  H N N 484 
VAL N    N N N 485 
VAL CA   C N S 486 
VAL C    C N N 487 
VAL O    O N N 488 
VAL CB   C N N 489 
VAL CG1  C N N 490 
VAL CG2  C N N 491 
VAL OXT  O N N 492 
VAL H    H N N 493 
VAL H2   H N N 494 
VAL HA   H N N 495 
VAL HB   H N N 496 
VAL HG11 H N N 497 
VAL HG12 H N N 498 
VAL HG13 H N N 499 
VAL HG21 H N N 500 
VAL HG22 H N N 501 
VAL HG23 H N N 502 
VAL HXT  H N N 503 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LPP P1  O2   sing N N 194 
LPP P1  O3   doub N N 195 
LPP P1  O4   sing N N 196 
LPP P1  O5   sing N N 197 
LPP O2  HO2  sing N N 198 
LPP O4  HO4  sing N N 199 
LPP O5  C6   sing N N 200 
LPP C6  C7   sing N N 201 
LPP C6  HC61 sing N N 202 
LPP C6  HC62 sing N N 203 
LPP C7  C8   sing N N 204 
LPP C7  O9   sing N N 205 
LPP C7  HC7  sing N N 206 
LPP C8  O27  sing N N 207 
LPP C8  HC81 sing N N 208 
LPP C8  HC82 sing N N 209 
LPP O9  C11  sing N N 210 
LPP O27 C29  sing N N 211 
LPP C11 O10  doub N N 212 
LPP C11 C12  sing N N 213 
LPP C12 C13  sing N N 214 
LPP C12 H121 sing N N 215 
LPP C12 H122 sing N N 216 
LPP C13 C14  sing N N 217 
LPP C13 H131 sing N N 218 
LPP C13 H132 sing N N 219 
LPP C14 C15  sing N N 220 
LPP C14 H141 sing N N 221 
LPP C14 H142 sing N N 222 
LPP C15 C16  sing N N 223 
LPP C15 H151 sing N N 224 
LPP C15 H152 sing N N 225 
LPP C16 C17  sing N N 226 
LPP C16 H161 sing N N 227 
LPP C16 H162 sing N N 228 
LPP C17 C18  sing N N 229 
LPP C17 H171 sing N N 230 
LPP C17 H172 sing N N 231 
LPP C18 C19  sing N N 232 
LPP C18 H181 sing N N 233 
LPP C18 H182 sing N N 234 
LPP C19 C20  sing N N 235 
LPP C19 H191 sing N N 236 
LPP C19 H192 sing N N 237 
LPP C20 C21  sing N N 238 
LPP C20 H201 sing N N 239 
LPP C20 H202 sing N N 240 
LPP C21 C22  sing N N 241 
LPP C21 H211 sing N N 242 
LPP C21 H212 sing N N 243 
LPP C22 C23  sing N N 244 
LPP C22 H221 sing N N 245 
LPP C22 H222 sing N N 246 
LPP C23 C24  sing N N 247 
LPP C23 H231 sing N N 248 
LPP C23 H232 sing N N 249 
LPP C24 C25  sing N N 250 
LPP C24 H241 sing N N 251 
LPP C24 H242 sing N N 252 
LPP C25 C26  sing N N 253 
LPP C25 H251 sing N N 254 
LPP C25 H252 sing N N 255 
LPP C26 H261 sing N N 256 
LPP C26 H262 sing N N 257 
LPP C26 H263 sing N N 258 
LPP C29 O28  doub N N 259 
LPP C29 C30  sing N N 260 
LPP C30 C31  sing N N 261 
LPP C30 H301 sing N N 262 
LPP C30 H302 sing N N 263 
LPP C31 C32  sing N N 264 
LPP C31 H311 sing N N 265 
LPP C31 H312 sing N N 266 
LPP C32 C33  sing N N 267 
LPP C32 H321 sing N N 268 
LPP C32 H322 sing N N 269 
LPP C33 C34  sing N N 270 
LPP C33 H331 sing N N 271 
LPP C33 H332 sing N N 272 
LPP C34 C35  sing N N 273 
LPP C34 H341 sing N N 274 
LPP C34 H342 sing N N 275 
LPP C35 C36  sing N N 276 
LPP C35 H351 sing N N 277 
LPP C35 H352 sing N N 278 
LPP C36 C37  sing N N 279 
LPP C36 H361 sing N N 280 
LPP C36 H362 sing N N 281 
LPP C37 C38  sing N N 282 
LPP C37 H371 sing N N 283 
LPP C37 H372 sing N N 284 
LPP C38 C39  sing N N 285 
LPP C38 H381 sing N N 286 
LPP C38 H382 sing N N 287 
LPP C39 C40  sing N N 288 
LPP C39 H391 sing N N 289 
LPP C39 H392 sing N N 290 
LPP C40 C41  sing N N 291 
LPP C40 H401 sing N N 292 
LPP C40 H402 sing N N 293 
LPP C41 C42  sing N N 294 
LPP C41 H411 sing N N 295 
LPP C41 H412 sing N N 296 
LPP C42 C43  sing N N 297 
LPP C42 H421 sing N N 298 
LPP C42 H422 sing N N 299 
LPP C43 C44  sing N N 300 
LPP C43 H431 sing N N 301 
LPP C43 H432 sing N N 302 
LPP C44 H441 sing N N 303 
LPP C44 H442 sing N N 304 
LPP C44 H443 sing N N 305 
LYS N   CA   sing N N 306 
LYS N   H    sing N N 307 
LYS N   H2   sing N N 308 
LYS CA  C    sing N N 309 
LYS CA  CB   sing N N 310 
LYS CA  HA   sing N N 311 
LYS C   O    doub N N 312 
LYS C   OXT  sing N N 313 
LYS CB  CG   sing N N 314 
LYS CB  HB2  sing N N 315 
LYS CB  HB3  sing N N 316 
LYS CG  CD   sing N N 317 
LYS CG  HG2  sing N N 318 
LYS CG  HG3  sing N N 319 
LYS CD  CE   sing N N 320 
LYS CD  HD2  sing N N 321 
LYS CD  HD3  sing N N 322 
LYS CE  NZ   sing N N 323 
LYS CE  HE2  sing N N 324 
LYS CE  HE3  sing N N 325 
LYS NZ  HZ1  sing N N 326 
LYS NZ  HZ2  sing N N 327 
LYS NZ  HZ3  sing N N 328 
LYS OXT HXT  sing N N 329 
MET N   CA   sing N N 330 
MET N   H    sing N N 331 
MET N   H2   sing N N 332 
MET CA  C    sing N N 333 
MET CA  CB   sing N N 334 
MET CA  HA   sing N N 335 
MET C   O    doub N N 336 
MET C   OXT  sing N N 337 
MET CB  CG   sing N N 338 
MET CB  HB2  sing N N 339 
MET CB  HB3  sing N N 340 
MET CG  SD   sing N N 341 
MET CG  HG2  sing N N 342 
MET CG  HG3  sing N N 343 
MET SD  CE   sing N N 344 
MET CE  HE1  sing N N 345 
MET CE  HE2  sing N N 346 
MET CE  HE3  sing N N 347 
MET OXT HXT  sing N N 348 
PHE N   CA   sing N N 349 
PHE N   H    sing N N 350 
PHE N   H2   sing N N 351 
PHE CA  C    sing N N 352 
PHE CA  CB   sing N N 353 
PHE CA  HA   sing N N 354 
PHE C   O    doub N N 355 
PHE C   OXT  sing N N 356 
PHE CB  CG   sing N N 357 
PHE CB  HB2  sing N N 358 
PHE CB  HB3  sing N N 359 
PHE CG  CD1  doub Y N 360 
PHE CG  CD2  sing Y N 361 
PHE CD1 CE1  sing Y N 362 
PHE CD1 HD1  sing N N 363 
PHE CD2 CE2  doub Y N 364 
PHE CD2 HD2  sing N N 365 
PHE CE1 CZ   doub Y N 366 
PHE CE1 HE1  sing N N 367 
PHE CE2 CZ   sing Y N 368 
PHE CE2 HE2  sing N N 369 
PHE CZ  HZ   sing N N 370 
PHE OXT HXT  sing N N 371 
PRO N   CA   sing N N 372 
PRO N   CD   sing N N 373 
PRO N   H    sing N N 374 
PRO CA  C    sing N N 375 
PRO CA  CB   sing N N 376 
PRO CA  HA   sing N N 377 
PRO C   O    doub N N 378 
PRO C   OXT  sing N N 379 
PRO CB  CG   sing N N 380 
PRO CB  HB2  sing N N 381 
PRO CB  HB3  sing N N 382 
PRO CG  CD   sing N N 383 
PRO CG  HG2  sing N N 384 
PRO CG  HG3  sing N N 385 
PRO CD  HD2  sing N N 386 
PRO CD  HD3  sing N N 387 
PRO OXT HXT  sing N N 388 
SER N   CA   sing N N 389 
SER N   H    sing N N 390 
SER N   H2   sing N N 391 
SER CA  C    sing N N 392 
SER CA  CB   sing N N 393 
SER CA  HA   sing N N 394 
SER C   O    doub N N 395 
SER C   OXT  sing N N 396 
SER CB  OG   sing N N 397 
SER CB  HB2  sing N N 398 
SER CB  HB3  sing N N 399 
SER OG  HG   sing N N 400 
SER OXT HXT  sing N N 401 
THR N   CA   sing N N 402 
THR N   H    sing N N 403 
THR N   H2   sing N N 404 
THR CA  C    sing N N 405 
THR CA  CB   sing N N 406 
THR CA  HA   sing N N 407 
THR C   O    doub N N 408 
THR C   OXT  sing N N 409 
THR CB  OG1  sing N N 410 
THR CB  CG2  sing N N 411 
THR CB  HB   sing N N 412 
THR OG1 HG1  sing N N 413 
THR CG2 HG21 sing N N 414 
THR CG2 HG22 sing N N 415 
THR CG2 HG23 sing N N 416 
THR OXT HXT  sing N N 417 
TRP N   CA   sing N N 418 
TRP N   H    sing N N 419 
TRP N   H2   sing N N 420 
TRP CA  C    sing N N 421 
TRP CA  CB   sing N N 422 
TRP CA  HA   sing N N 423 
TRP C   O    doub N N 424 
TRP C   OXT  sing N N 425 
TRP CB  CG   sing N N 426 
TRP CB  HB2  sing N N 427 
TRP CB  HB3  sing N N 428 
TRP CG  CD1  doub Y N 429 
TRP CG  CD2  sing Y N 430 
TRP CD1 NE1  sing Y N 431 
TRP CD1 HD1  sing N N 432 
TRP CD2 CE2  doub Y N 433 
TRP CD2 CE3  sing Y N 434 
TRP NE1 CE2  sing Y N 435 
TRP NE1 HE1  sing N N 436 
TRP CE2 CZ2  sing Y N 437 
TRP CE3 CZ3  doub Y N 438 
TRP CE3 HE3  sing N N 439 
TRP CZ2 CH2  doub Y N 440 
TRP CZ2 HZ2  sing N N 441 
TRP CZ3 CH2  sing Y N 442 
TRP CZ3 HZ3  sing N N 443 
TRP CH2 HH2  sing N N 444 
TRP OXT HXT  sing N N 445 
TYR N   CA   sing N N 446 
TYR N   H    sing N N 447 
TYR N   H2   sing N N 448 
TYR CA  C    sing N N 449 
TYR CA  CB   sing N N 450 
TYR CA  HA   sing N N 451 
TYR C   O    doub N N 452 
TYR C   OXT  sing N N 453 
TYR CB  CG   sing N N 454 
TYR CB  HB2  sing N N 455 
TYR CB  HB3  sing N N 456 
TYR CG  CD1  doub Y N 457 
TYR CG  CD2  sing Y N 458 
TYR CD1 CE1  sing Y N 459 
TYR CD1 HD1  sing N N 460 
TYR CD2 CE2  doub Y N 461 
TYR CD2 HD2  sing N N 462 
TYR CE1 CZ   doub Y N 463 
TYR CE1 HE1  sing N N 464 
TYR CE2 CZ   sing Y N 465 
TYR CE2 HE2  sing N N 466 
TYR CZ  OH   sing N N 467 
TYR OH  HH   sing N N 468 
TYR OXT HXT  sing N N 469 
VAL N   CA   sing N N 470 
VAL N   H    sing N N 471 
VAL N   H2   sing N N 472 
VAL CA  C    sing N N 473 
VAL CA  CB   sing N N 474 
VAL CA  HA   sing N N 475 
VAL C   O    doub N N 476 
VAL C   OXT  sing N N 477 
VAL CB  CG1  sing N N 478 
VAL CB  CG2  sing N N 479 
VAL CB  HB   sing N N 480 
VAL CG1 HG11 sing N N 481 
VAL CG1 HG12 sing N N 482 
VAL CG1 HG13 sing N N 483 
VAL CG2 HG21 sing N N 484 
VAL CG2 HG22 sing N N 485 
VAL CG2 HG23 sing N N 486 
VAL OXT HXT  sing N N 487 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-07 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8ZTK 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'AtALMT9 with LMNG (cis2 class)' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20    mM        C8H18N2O4S 1 HEPES             
1 150   mM        NaCl       2 'Sodium chloride' 
1 1     mM        C9H15O6P   3 TCEP              
1 0.005 '% (w/v)' C47H88O22  4 LMNG              
1 10    mM        C4H6O5     5 Malate            
# 
_em_ctf_correction.details                  'Patch CTF estimation' 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.13 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   1 
_em_entity_assembly_naturalsource.ncbi_tax_id          3702 
_em_entity_assembly_naturalsource.organism             'Arabidopsis thaliana' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   1 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               Sf9 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    18 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   2895997 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? Topaz     0.2.5a  
'IMAGE ACQUISITION'             ? 2  ? ? 1 ?         ?       
MASKING                         ? 3  ? ? ? ?         ?       
'CTF CORRECTION'                ? 4  1 ? ? cryoSPARC 4.4     
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ?       
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ?       
'MODEL FITTING'                 ? 7  ? 1 ? Coot      0.9.8.1 
OTHER                           ? 8  ? ? ? ?         ?       
'MODEL REFINEMENT'              ? 9  ? 1 ? PHENIX    1.20.1  
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? cryoSPARC 4.4     
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC 4.4     
CLASSIFICATION                  ? 12 1 ? ? cryoSPARC 4.4     
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC 4.4     
'VOLUME SELECTION'              ? 14 1 1 1 ?         ?       
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ?       
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ?       
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ?       
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ?       
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?         ?       
# 
_em_specimen.concentration           1.9 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' 2022R1A2C100988211 1 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' RS-2023-00223552   2 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' 2021M3A9I4022936   3 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZTK 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
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    . ALA A 1 77  ? 118.45300 131.06800 105.60600 1.000 89.22736  ? 77  ALA A N    1 
ATOM   2    C CA   . ALA A 1 77  ? 117.95100 131.55200 106.88600 1.000 89.17083  ? 77  ALA A CA   1 
ATOM   3    C C    . ALA A 1 77  ? 117.06200 132.77300 106.69000 1.000 89.57596  ? 77  ALA A C    1 
ATOM   4    O O    . ALA A 1 77  ? 115.85600 132.64700 106.46800 1.000 89.70769  ? 77  ALA A O    1 
ATOM   5    C CB   . ALA A 1 77  ? 119.10600 131.87900 107.82000 1.000 88.60630  ? 77  ALA A CB   1 
ATOM   6    N N    . TRP A 1 78  ? 117.66900 133.95700 106.78900 1.000 92.19718  ? 78  TRP A N    1 
ATOM   7    C CA   . TRP A 1 78  ? 116.91700 135.19300 106.60000 1.000 91.44025  ? 78  TRP A CA   1 
ATOM   8    C C    . TRP A 1 78  ? 116.20200 135.20400 105.25500 1.000 91.51102  ? 78  TRP A C    1 
ATOM   9    O O    . TRP A 1 78  ? 115.06700 135.68400 105.15300 1.000 91.73927  ? 78  TRP A O    1 
ATOM   10   C CB   . TRP A 1 78  ? 117.85000 136.39800 106.72800 1.000 90.57064  ? 78  TRP A CB   1 
ATOM   11   C CG   . TRP A 1 78  ? 117.13300 137.71400 106.77800 1.000 92.10952  ? 78  TRP A CG   1 
ATOM   12   C CD1  . TRP A 1 78  ? 116.51900 138.35500 105.74100 1.000 92.04451  ? 78  TRP A CD1  1 
ATOM   13   C CD2  . TRP A 1 78  ? 116.95100 138.54900 107.92800 1.000 92.88491  ? 78  TRP A CD2  1 
ATOM   14   N NE1  . TRP A 1 78  ? 115.96900 139.53700 106.17400 1.000 91.44474  ? 78  TRP A NE1  1 
ATOM   15   C CE2  . TRP A 1 78  ? 116.22000 139.67900 107.51300 1.000 92.28321  ? 78  TRP A CE2  1 
ATOM   16   C CE3  . TRP A 1 78  ? 117.33700 138.45000 109.26900 1.000 91.84986  ? 78  TRP A CE3  1 
ATOM   17   C CZ2  . TRP A 1 78  ? 115.86700 140.70300 108.38900 1.000 91.57975  ? 78  TRP A CZ2  1 
ATOM   18   C CZ3  . TRP A 1 78  ? 116.98500 139.46800 110.13700 1.000 91.27826  ? 78  TRP A CZ3  1 
ATOM   19   C CH2  . TRP A 1 78  ? 116.25800 140.58000 109.69400 1.000 91.03899  ? 78  TRP A CH2  1 
ATOM   20   N N    . GLU A 1 79  ? 116.85600 134.69900 104.20700 1.000 84.03528  ? 79  GLU A N    1 
ATOM   21   C CA   . GLU A 1 79  ? 116.23800 134.68500 102.88500 1.000 84.39057  ? 79  GLU A CA   1 
ATOM   22   C C    . GLU A 1 79  ? 114.97300 133.83500 102.88100 1.000 85.51039  ? 79  GLU A C    1 
ATOM   23   O O    . GLU A 1 79  ? 113.92200 134.26300 102.38900 1.000 84.64217  ? 79  GLU A O    1 
ATOM   24   C CB   . GLU A 1 79  ? 117.23700 134.17500 101.84600 1.000 84.07161  ? 79  GLU A CB   1 
ATOM   25   N N    . MET A 1 80  ? 115.05700 132.61900 103.42700 1.000 81.90927  ? 80  MET A N    1 
ATOM   26   C CA   . MET A 1 80  ? 113.88600 131.75200 103.45800 1.000 81.45992  ? 80  MET A CA   1 
ATOM   27   C C    . MET A 1 80  ? 112.79300 132.33000 104.34600 1.000 81.19300  ? 80  MET A C    1 
ATOM   28   O O    . MET A 1 80  ? 111.60400 132.13700 104.06900 1.000 80.52438  ? 80  MET A O    1 
ATOM   29   C CB   . MET A 1 80  ? 114.27500 130.35100 103.93100 1.000 80.41374  ? 80  MET A CB   1 
ATOM   30   C CG   . MET A 1 80  ? 113.16200 129.32200 103.79700 1.000 81.86117  ? 80  MET A CG   1 
ATOM   31   S SD   . MET A 1 80  ? 113.41100 127.85100 104.81200 1.000 81.95594  ? 80  MET A SD   1 
ATOM   32   C CE   . MET A 1 80  ? 114.15200 128.56400 106.27800 1.000 80.89271  ? 80  MET A CE   1 
ATOM   33   N N    . GLY A 1 81  ? 113.17300 133.03300 105.41300 1.000 80.46843  ? 81  GLY A N    1 
ATOM   34   C CA   . GLY A 1 81  ? 112.17200 133.64800 106.27000 1.000 80.62971  ? 81  GLY A CA   1 
ATOM   35   C C    . GLY A 1 81  ? 111.44100 134.78300 105.57900 1.000 80.72829  ? 81  GLY A C    1 
ATOM   36   O O    . GLY A 1 81  ? 110.21300 134.88400 105.65300 1.000 81.64517  ? 81  GLY A O    1 
ATOM   37   N N    . VAL A 1 82  ? 112.18500 135.65400 104.89500 1.000 84.18762  ? 82  VAL A N    1 
ATOM   38   C CA   . VAL A 1 82  ? 111.55600 136.76300 104.18500 1.000 85.02107  ? 82  VAL A CA   1 
ATOM   39   C C    . VAL A 1 82  ? 110.68900 136.24100 103.04700 1.000 84.45754  ? 82  VAL A C    1 
ATOM   40   O O    . VAL A 1 82  ? 109.60000 136.76600 102.78700 1.000 84.78357  ? 82  VAL A O    1 
ATOM   41   C CB   . VAL A 1 82  ? 112.61600 137.75800 103.67700 1.000 85.30321  ? 82  VAL A CB   1 
ATOM   42   C CG1  . VAL A 1 82  ? 113.09500 138.65000 104.81300 1.000 83.94045  ? 82  VAL A CG1  1 
ATOM   43   C CG2  . VAL A 1 82  ? 113.77700 137.02600 103.02900 1.000 84.14829  ? 82  VAL A CG2  1 
ATOM   44   N N    . SER A 1 83  ? 111.15500 135.20300 102.34800 1.000 81.86963  ? 83  SER A N    1 
ATOM   45   C CA   . SER A 1 83  ? 110.34500 134.62100 101.28300 1.000 82.32484  ? 83  SER A CA   1 
ATOM   46   C C    . SER A 1 83  ? 109.15500 133.85600 101.84900 1.000 83.87501  ? 83  SER A C    1 
ATOM   47   O O    . SER A 1 83  ? 108.04600 133.93300 101.30700 1.000 83.85996  ? 83  SER A O    1 
ATOM   48   C CB   . SER A 1 83  ? 111.20300 133.71000 100.40500 1.000 81.90239  ? 83  SER A CB   1 
ATOM   49   O OG   . SER A 1 83  ? 112.10500 132.94800 101.18700 1.000 83.96311  ? 83  SER A OG   1 
ATOM   50   N N    . ASP A 1 84  ? 109.36200 133.11500 102.93500 1.000 71.64456  ? 84  ASP A N    1 
ATOM   51   C CA   . ASP A 1 84  ? 108.31300 132.29600 103.54200 1.000 68.88320  ? 84  ASP A CA   1 
ATOM   52   C C    . ASP A 1 84  ? 108.01700 132.78400 104.95200 1.000 70.05886  ? 84  ASP A C    1 
ATOM   53   O O    . ASP A 1 84  ? 108.71600 132.39700 105.90600 1.000 72.12691  ? 84  ASP A O    1 
ATOM   54   C CB   . ASP A 1 84  ? 108.72000 130.82400 103.55900 1.000 68.15387  ? 84  ASP A CB   1 
ATOM   55   C CG   . ASP A 1 84  ? 107.60900 129.90800 103.09000 1.000 70.63413  ? 84  ASP A CG   1 
ATOM   56   O OD1  . ASP A 1 84  ? 106.46700 130.38900 102.93100 1.000 69.68389  ? 84  ASP A OD1  1 
ATOM   57   O OD2  . ASP A 1 84  ? 107.87700 128.70700 102.87700 1.000 72.46718  ? 84  ASP A OD2  1 
ATOM   58   N N    . PRO A 1 85  ? 107.00000 133.63100 105.14200 1.000 59.73305  ? 85  PRO A N    1 
ATOM   59   C CA   . PRO A 1 85  ? 106.64300 134.07100 106.49800 1.000 58.99996  ? 85  PRO A CA   1 
ATOM   60   C C    . PRO A 1 85  ? 105.84600 133.05100 107.29700 1.000 57.16049  ? 85  PRO A C    1 
ATOM   61   O O    . PRO A 1 85  ? 105.66400 133.24700 108.50600 1.000 58.31959  ? 85  PRO A O    1 
ATOM   62   C CB   . PRO A 1 85  ? 105.81300 135.33600 106.24200 1.000 58.18096  ? 85  PRO A CB   1 
ATOM   63   C CG   . PRO A 1 85  ? 105.20700 135.11500 104.89900 1.000 58.40498  ? 85  PRO A CG   1 
ATOM   64   C CD   . PRO A 1 85  ? 106.18900 134.29200 104.10500 1.000 58.65351  ? 85  PRO A CD   1 
ATOM   65   N N    . ARG A 1 86  ? 105.36500 131.97900 106.66500 1.000 44.06070  ? 86  ARG A N    1 
ATOM   66   C CA   . ARG A 1 86  ? 104.62200 130.94800 107.38600 1.000 45.75554  ? 86  ARG A CA   1 
ATOM   67   C C    . ARG A 1 86  ? 105.51900 130.17300 108.34600 1.000 48.04964  ? 86  ARG A C    1 
ATOM   68   O O    . ARG A 1 86  ? 105.10000 129.82800 109.45800 1.000 51.29441  ? 86  ARG A O    1 
ATOM   69   C CB   . ARG A 1 86  ? 103.96100 129.99800 106.38900 1.000 41.93617  ? 86  ARG A CB   1 
ATOM   70   C CG   . ARG A 1 86  ? 102.97400 130.67900 105.45700 1.000 45.95758  ? 86  ARG A CG   1 
ATOM   71   C CD   . ARG A 1 86  ? 101.86400 129.73600 105.02800 1.000 45.91391  ? 86  ARG A CD   1 
ATOM   72   N NE   . ARG A 1 86  ? 102.37800 128.41900 104.67200 1.000 46.13737  ? 86  ARG A NE   1 
ATOM   73   C CZ   . ARG A 1 86  ? 101.74200 127.55300 103.89600 1.000 48.34603  ? 86  ARG A CZ   1 
ATOM   74   N NH1  . ARG A 1 86  ? 100.55700 127.83100 103.37600 1.000 45.14298  ? 86  ARG A NH1  1 
ATOM   75   N NH2  . ARG A 1 86  ? 102.30900 126.37900 103.63200 1.000 46.52641  ? 86  ARG A NH2  1 
ATOM   76   N N    . LYS A 1 87  ? 106.75200 129.88300 107.92800 1.000 37.49628  ? 87  LYS A N    1 
ATOM   77   C CA   . LYS A 1 87  ? 107.68200 129.15700 108.78700 1.000 37.61416  ? 87  LYS A CA   1 
ATOM   78   C C    . LYS A 1 87  ? 107.95600 129.91500 110.08300 1.000 39.08757  ? 87  LYS A C    1 
ATOM   79   O O    . LYS A 1 87  ? 108.03100 129.31100 111.16300 1.000 43.40121  ? 87  LYS A O    1 
ATOM   80   C CB   . LYS A 1 87  ? 108.97700 128.90400 108.01900 1.000 39.48832  ? 87  LYS A CB   1 
ATOM   81   C CG   . LYS A 1 87  ? 108.80300 127.95900 106.83900 1.000 38.53363  ? 87  LYS A CG   1 
ATOM   82   C CD   . LYS A 1 87  ? 110.02400 127.09000 106.60700 1.000 40.92187  ? 87  LYS A CD   1 
ATOM   83   C CE   . LYS A 1 87  ? 109.68600 125.91800 105.69900 1.000 41.44210  ? 87  LYS A CE   1 
ATOM   84   N NZ   . LYS A 1 87  ? 110.84100 125.51100 104.85200 1.000 40.03618  ? 87  LYS A NZ   1 
ATOM   85   N N    . ILE A 1 88  ? 108.06800 131.24200 110.00400 1.000 29.92286  ? 88  ILE A N    1 
ATOM   86   C CA   . ILE A 1 88  ? 108.32000 132.03300 111.20400 1.000 35.25792  ? 88  ILE A CA   1 
ATOM   87   C C    . ILE A 1 88  ? 107.11200 131.99300 112.13000 1.000 41.37006  ? 88  ILE A C    1 
ATOM   88   O O    . ILE A 1 88  ? 107.25300 131.93100 113.35900 1.000 44.83616  ? 88  ILE A O    1 
ATOM   89   C CB   . ILE A 1 88  ? 108.68600 133.47800 110.81900 1.000 37.57821  ? 88  ILE A CB   1 
ATOM   90   C CG1  . ILE A 1 88  ? 110.02100 133.51400 110.07600 1.000 39.12962  ? 88  ILE A CG1  1 
ATOM   91   C CG2  . ILE A 1 88  ? 108.73800 134.36400 112.05300 1.000 41.25687  ? 88  ILE A CG2  1 
ATOM   92   C CD1  . ILE A 1 88  ? 110.32100 134.84800 109.43900 1.000 39.71460  ? 88  ILE A CD1  1 
ATOM   93   N N    . VAL A 1 89  ? 105.90900 131.97800 111.55700 1.000 30.84080  ? 89  VAL A N    1 
ATOM   94   C CA   . VAL A 1 89  ? 104.70200 131.89800 112.37100 1.000 30.33165  ? 89  VAL A CA   1 
ATOM   95   C C    . VAL A 1 89  ? 104.63800 130.55700 113.08900 1.000 25.32533  ? 89  VAL A C    1 
ATOM   96   O O    . VAL A 1 89  ? 104.34800 130.49200 114.28800 1.000 36.49157  ? 89  VAL A O    1 
ATOM   97   C CB   . VAL A 1 89  ? 103.45300 132.13800 111.50400 1.000 30.73403  ? 89  VAL A CB   1 
ATOM   98   C CG1  . VAL A 1 89  ? 102.19100 131.86200 112.30400 1.000 34.60443  ? 89  VAL A CG1  1 
ATOM   99   C CG2  . VAL A 1 89  ? 103.44800 133.55900 110.96700 1.000 30.58758  ? 89  VAL A CG2  1 
ATOM   100  N N    . PHE A 1 90  ? 104.88600 129.46700 112.36200 1.000 7.18300   ? 90  PHE A N    1 
ATOM   101  C CA   . PHE A 1 90  ? 104.88000 128.14500 112.98200 1.000 18.16835  ? 90  PHE A CA   1 
ATOM   102  C C    . PHE A 1 90  ? 105.90300 128.05300 114.11300 1.000 22.04295  ? 90  PHE A C    1 
ATOM   103  O O    . PHE A 1 90  ? 105.60400 127.52900 115.20000 1.000 21.00630  ? 90  PHE A O    1 
ATOM   104  C CB   . PHE A 1 90  ? 105.14900 127.08600 111.91000 1.000 13.78237  ? 90  PHE A CB   1 
ATOM   105  C CG   . PHE A 1 90  ? 105.15200 125.67600 112.42400 1.000 19.42379  ? 90  PHE A CG   1 
ATOM   106  C CD1  . PHE A 1 90  ? 104.00000 125.11000 112.94100 1.000 18.09191  ? 90  PHE A CD1  1 
ATOM   107  C CD2  . PHE A 1 90  ? 106.30300 124.90800 112.36800 1.000 19.50489  ? 90  PHE A CD2  1 
ATOM   108  C CE1  . PHE A 1 90  ? 104.00100 123.81000 113.40500 1.000 18.39769  ? 90  PHE A CE1  1 
ATOM   109  C CE2  . PHE A 1 90  ? 106.30900 123.60800 112.83000 1.000 14.67981  ? 90  PHE A CE2  1 
ATOM   110  C CZ   . PHE A 1 90  ? 105.15700 123.05900 113.34900 1.000 17.97552  ? 90  PHE A CZ   1 
ATOM   111  N N    . SER A 1 91  ? 107.11100 128.58200 113.88800 1.000 19.62102  ? 91  SER A N    1 
ATOM   112  C CA   . SER A 1 91  ? 108.14700 128.48800 114.91100 1.000 13.82566  ? 91  SER A CA   1 
ATOM   113  C C    . SER A 1 91  ? 107.83100 129.35100 116.12700 1.000 18.13136  ? 91  SER A C    1 
ATOM   114  O O    . SER A 1 91  ? 108.09400 128.93600 117.26700 1.000 17.82850  ? 91  SER A O    1 
ATOM   115  C CB   . SER A 1 91  ? 109.49600 128.87800 114.31400 1.000 14.72701  ? 91  SER A CB   1 
ATOM   116  O OG   . SER A 1 91  ? 109.67500 128.27400 113.04600 1.000 16.07200  ? 91  SER A OG   1 
ATOM   117  N N    . ALA A 1 92  ? 107.17300 130.49600 115.93000 1.000 15.35155  ? 92  ALA A N    1 
ATOM   118  C CA   . ALA A 1 92  ? 106.80300 131.29400 117.08800 1.000 11.68088  ? 92  ALA A CA   1 
ATOM   119  C C    . ALA A 1 92  ? 105.57200 130.73700 117.78300 1.000 19.26200  ? 92  ALA A C    1 
ATOM   120  O O    . ALA A 1 92  ? 105.40700 130.94900 118.98800 1.000 27.51864  ? 92  ALA A O    1 
ATOM   121  C CB   . ALA A 1 92  ? 106.55800 132.74600 116.67700 1.000 15.78845  ? 92  ALA A CB   1 
ATOM   122  N N    . LYS A 1 93  ? 104.77500 129.93400 117.07900 1.000 13.37251  ? 93  LYS A N    1 
ATOM   123  C CA   . LYS A 1 93  ? 103.64300 129.28000 117.71900 1.000 14.32645  ? 93  LYS A CA   1 
ATOM   124  C C    . LYS A 1 93  ? 104.13200 128.17600 118.64200 1.000 18.99830  ? 93  LYS A C    1 
ATOM   125  O O    . LYS A 1 93  ? 103.64200 128.02700 119.77100 1.000 22.53803  ? 93  LYS A O    1 
ATOM   126  C CB   . LYS A 1 93  ? 102.70200 128.71300 116.65700 1.000 17.20072  ? 93  LYS A CB   1 
ATOM   127  C CG   . LYS A 1 93  ? 101.63800 129.67600 116.17700 1.000 19.48019  ? 93  LYS A CG   1 
ATOM   128  C CD   . LYS A 1 93  ? 100.39900 128.92800 115.72200 1.000 22.66517  ? 93  LYS A CD   1 
ATOM   129  C CE   . LYS A 1 93  ? 100.61400 128.28800 114.36300 1.000 16.47929  ? 93  LYS A CE   1 
ATOM   130  N NZ   . LYS A 1 93  ? 99.33400  127.84200 113.75500 1.000 14.94005  ? 93  LYS A NZ   1 
ATOM   131  N N    . ILE A 1 94  ? 105.13800 127.42300 118.19400 1.000 10.49266  ? 94  ILE A N    1 
ATOM   132  C CA   . ILE A 1 94  ? 105.69300 126.38500 119.05600 1.000 13.04809  ? 94  ILE A CA   1 
ATOM   133  C C    . ILE A 1 94  ? 106.43200 127.01200 120.23400 1.000 14.82386  ? 94  ILE A C    1 
ATOM   134  O O    . ILE A 1 94  ? 106.34300 126.52600 121.37200 1.000 23.42726  ? 94  ILE A O    1 
ATOM   135  C CB   . ILE A 1 94  ? 106.59900 125.44100 118.24600 1.000 18.25413  ? 94  ILE A CB   1 
ATOM   136  C CG1  . ILE A 1 94  ? 105.75300 124.59300 117.29600 1.000 15.53143  ? 94  ILE A CG1  1 
ATOM   137  C CG2  . ILE A 1 94  ? 107.41900 124.55900 119.17500 1.000 17.33059  ? 94  ILE A CG2  1 
ATOM   138  C CD1  . ILE A 1 94  ? 106.50200 123.44900 116.67000 1.000 18.39502  ? 94  ILE A CD1  1 
ATOM   139  N N    . GLY A 1 95  ? 107.15500 128.11000 119.99300 1.000 13.54988  ? 95  GLY A N    1 
ATOM   140  C CA   . GLY A 1 95  ? 107.78700 128.80500 121.10300 1.000 7.13510   ? 95  GLY A CA   1 
ATOM   141  C C    . GLY A 1 95  ? 106.78600 129.29700 122.13300 1.000 12.25368  ? 95  GLY A C    1 
ATOM   142  O O    . GLY A 1 95  ? 107.01300 129.18000 123.34200 1.000 16.62312  ? 95  GLY A O    1 
ATOM   143  N N    . LEU A 1 96  ? 105.64600 129.82200 121.67300 1.000 22.17324  ? 96  LEU A N    1 
ATOM   144  C CA   . LEU A 1 96  ? 104.63000 130.30300 122.60400 1.000 20.37829  ? 96  LEU A CA   1 
ATOM   145  C C    . LEU A 1 96  ? 104.01400 129.15600 123.39400 1.000 22.16613  ? 96  LEU A C    1 
ATOM   146  O O    . LEU A 1 96  ? 103.76800 129.28500 124.60100 1.000 28.67002  ? 96  LEU A O    1 
ATOM   147  C CB   . LEU A 1 96  ? 103.55000 131.07400 121.84600 1.000 15.56612  ? 96  LEU A CB   1 
ATOM   148  C CG   . LEU A 1 96  ? 102.44000 131.70900 122.68500 1.000 20.91134  ? 96  LEU A CG   1 
ATOM   149  C CD1  . LEU A 1 96  ? 102.96100 132.92000 123.44000 1.000 22.52434  ? 96  LEU A CD1  1 
ATOM   150  C CD2  . LEU A 1 96  ? 101.25800 132.08700 121.80800 1.000 21.83967  ? 96  LEU A CD2  1 
ATOM   151  N N    . ALA A 1 97  ? 103.77100 128.01700 122.74000 1.000 23.43380  ? 97  ALA A N    1 
ATOM   152  C CA   . ALA A 1 97  ? 103.19300 126.88600 123.46000 1.000 17.67696  ? 97  ALA A CA   1 
ATOM   153  C C    . ALA A 1 97  ? 104.14800 126.38100 124.53500 1.000 14.35761  ? 97  ALA A C    1 
ATOM   154  O O    . ALA A 1 97  ? 103.72800 126.07400 125.66300 1.000 23.42792  ? 97  ALA A O    1 
ATOM   155  C CB   . ALA A 1 97  ? 102.83800 125.76500 122.48400 1.000 17.52439  ? 97  ALA A CB   1 
ATOM   156  N N    . LEU A 1 98  ? 105.44400 126.32300 124.21900 1.000 15.55962  ? 98  LEU A N    1 
ATOM   157  C CA   . LEU A 1 98  ? 106.40500 125.88500 125.22600 1.000 15.14566  ? 98  LEU A CA   1 
ATOM   158  C C    . LEU A 1 98  ? 106.49500 126.88600 126.37000 1.000 19.69423  ? 98  LEU A C    1 
ATOM   159  O O    . LEU A 1 98  ? 106.56400 126.49100 127.54100 1.000 24.56266  ? 98  LEU A O    1 
ATOM   160  C CB   . LEU A 1 98  ? 107.78000 125.67000 124.59400 1.000 16.53980  ? 98  LEU A CB   1 
ATOM   161  C CG   . LEU A 1 98  ? 107.99500 124.39300 123.78000 1.000 16.26763  ? 98  LEU A CG   1 
ATOM   162  C CD1  . LEU A 1 98  ? 109.37800 124.39700 123.14900 1.000 18.61775  ? 98  LEU A CD1  1 
ATOM   163  C CD2  . LEU A 1 98  ? 107.80100 123.16000 124.64400 1.000 14.47019  ? 98  LEU A CD2  1 
ATOM   164  N N    . THR A 1 99  ? 106.46100 128.18700 126.06300 1.000 24.32349  ? 99  THR A N    1 
ATOM   165  C CA   . THR A 1 99  ? 106.56100 129.17300 127.13200 1.000 17.83628  ? 99  THR A CA   1 
ATOM   166  C C    . THR A 1 99  ? 105.30700 129.21100 127.99400 1.000 26.32673  ? 99  THR A C    1 
ATOM   167  O O    . THR A 1 99  ? 105.39400 129.52800 129.18500 1.000 28.25134  ? 99  THR A O    1 
ATOM   168  C CB   . THR A 1 99  ? 106.83100 130.55800 126.54200 1.000 22.39025  ? 99  THR A CB   1 
ATOM   169  O OG1  . THR A 1 99  ? 108.21700 130.67300 126.20000 1.000 29.17118  ? 99  THR A OG1  1 
ATOM   170  C CG2  . THR A 1 99  ? 106.47400 131.64400 127.54100 1.000 26.60356  ? 99  THR A CG2  1 
ATOM   171  N N    . ILE A 1 100 ? 104.17200 128.75700 127.46600 1.000 25.78249  ? 100 ILE A N    1 
ATOM   172  C CA   . ILE A 1 100 ? 102.96000 128.70400 128.27600 1.000 23.15772  ? 100 ILE A CA   1 
ATOM   173  C C    . ILE A 1 100 ? 102.98500 127.48800 129.19000 1.000 26.45616  ? 100 ILE A C    1 
ATOM   174  O O    . ILE A 1 100 ? 102.63900 127.57600 130.37700 1.000 31.35439  ? 100 ILE A O    1 
ATOM   175  C CB   . ILE A 1 100 ? 101.70700 128.71500 127.38100 1.000 27.63519  ? 100 ILE A CB   1 
ATOM   176  C CG1  . ILE A 1 100 ? 101.64800 130.00100 126.55700 1.000 28.25004  ? 100 ILE A CG1  1 
ATOM   177  C CG2  . ILE A 1 100 ? 100.45000 128.55900 128.22200 1.000 25.14787  ? 100 ILE A CG2  1 
ATOM   178  C CD1  . ILE A 1 100 ? 100.38300 130.14400 125.74500 1.000 27.96192  ? 100 ILE A CD1  1 
ATOM   179  N N    . VAL A 1 101 ? 103.35000 126.32500 128.64500 1.000 26.67859  ? 101 VAL A N    1 
ATOM   180  C CA   . VAL A 1 101 ? 103.52000 125.15600 129.50500 1.000 26.41264  ? 101 VAL A CA   1 
ATOM   181  C C    . VAL A 1 101 ? 104.53300 125.44600 130.61000 1.000 26.65306  ? 101 VAL A C    1 
ATOM   182  O O    . VAL A 1 101 ? 104.36900 125.00300 131.75200 1.000 24.96724  ? 101 VAL A O    1 
ATOM   183  C CB   . VAL A 1 101 ? 103.92200 123.92300 128.67400 1.000 31.02370  ? 101 VAL A CB   1 
ATOM   184  C CG1  . VAL A 1 101 ? 104.41500 122.81500 129.58500 1.000 27.99743  ? 101 VAL A CG1  1 
ATOM   185  C CG2  . VAL A 1 101 ? 102.74300 123.43800 127.85200 1.000 28.38786  ? 101 VAL A CG2  1 
ATOM   186  N N    . ALA A 1 102 ? 105.59300 126.19900 130.29300 1.000 32.99735  ? 102 ALA A N    1 
ATOM   187  C CA   . ALA A 1 102 ? 106.56900 126.56600 131.31800 1.000 29.31745  ? 102 ALA A CA   1 
ATOM   188  C C    . ALA A 1 102 ? 105.96800 127.49400 132.36900 1.000 34.60383  ? 102 ALA A C    1 
ATOM   189  O O    . ALA A 1 102 ? 106.19100 127.30400 133.57300 1.000 36.94052  ? 102 ALA A O    1 
ATOM   190  C CB   . ALA A 1 102 ? 107.79200 127.21100 130.66900 1.000 29.77773  ? 102 ALA A CB   1 
ATOM   191  N N    . LEU A 1 103 ? 105.21200 128.51000 131.93800 1.000 45.11386  ? 103 LEU A N    1 
ATOM   192  C CA   . LEU A 1 103 ? 104.61200 129.43000 132.89900 1.000 40.74058  ? 103 LEU A CA   1 
ATOM   193  C C    . LEU A 1 103 ? 103.67000 128.70200 133.84700 1.000 41.64089  ? 103 LEU A C    1 
ATOM   194  O O    . LEU A 1 103 ? 103.67600 128.95900 135.05600 1.000 42.69454  ? 103 LEU A O    1 
ATOM   195  C CB   . LEU A 1 103 ? 103.87100 130.55400 132.17400 1.000 42.79033  ? 103 LEU A CB   1 
ATOM   196  C CG   . LEU A 1 103 ? 104.71800 131.70900 131.63900 1.000 46.07546  ? 103 LEU A CG   1 
ATOM   197  C CD1  . LEU A 1 103 ? 103.85200 132.69200 130.87000 1.000 43.36188  ? 103 LEU A CD1  1 
ATOM   198  C CD2  . LEU A 1 103 ? 105.43900 132.40700 132.78000 1.000 41.29192  ? 103 LEU A CD2  1 
ATOM   199  N N    . LEU A 1 104 ? 102.85200 127.78800 133.32200 1.000 44.50859  ? 104 LEU A N    1 
ATOM   200  C CA   . LEU A 1 104 ? 101.90600 127.10200 134.19800 1.000 43.80181  ? 104 LEU A CA   1 
ATOM   201  C C    . LEU A 1 104 ? 102.57700 126.15500 135.18700 1.000 44.84747  ? 104 LEU A C    1 
ATOM   202  O O    . LEU A 1 104 ? 101.86600 125.46900 135.93000 1.000 47.47406  ? 104 LEU A O    1 
ATOM   203  C CB   . LEU A 1 104 ? 100.87900 126.32500 133.37200 1.000 41.82618  ? 104 LEU A CB   1 
ATOM   204  C CG   . LEU A 1 104 ? 100.10000 127.10300 132.31300 1.000 45.77091  ? 104 LEU A CG   1 
ATOM   205  C CD1  . LEU A 1 104 ? 99.64800  126.17600 131.19800 1.000 45.26039  ? 104 LEU A CD1  1 
ATOM   206  C CD2  . LEU A 1 104 ? 98.91000  127.80600 132.94500 1.000 44.86157  ? 104 LEU A CD2  1 
ATOM   207  N N    . ILE A 1 105 ? 103.90800 126.09500 135.22200 1.000 44.57574  ? 105 ILE A N    1 
ATOM   208  C CA   . ILE A 1 105 ? 104.61900 125.19500 136.12400 1.000 44.56866  ? 105 ILE A CA   1 
ATOM   209  C C    . ILE A 1 105 ? 105.55100 125.99800 137.02200 1.000 45.47496  ? 105 ILE A C    1 
ATOM   210  O O    . ILE A 1 105 ? 105.83900 125.59500 138.15400 1.000 45.34425  ? 105 ILE A O    1 
ATOM   211  C CB   . ILE A 1 105 ? 105.39500 124.11300 135.35000 1.000 43.26343  ? 105 ILE A CB   1 
ATOM   212  C CG1  . ILE A 1 105 ? 104.42700 123.17000 134.63400 1.000 43.13770  ? 105 ILE A CG1  1 
ATOM   213  C CG2  . ILE A 1 105 ? 106.31200 123.34100 136.28400 1.000 41.06984  ? 105 ILE A CG2  1 
ATOM   214  C CD1  . ILE A 1 105 ? 105.09600 122.24200 133.64700 1.000 44.78640  ? 105 ILE A CD1  1 
ATOM   215  N N    . PHE A 1 106 ? 106.02800 127.14300 136.52500 1.000 55.20610  ? 106 PHE A N    1 
ATOM   216  C CA   . PHE A 1 106 ? 106.89900 127.98600 137.33900 1.000 52.20401  ? 106 PHE A CA   1 
ATOM   217  C C    . PHE A 1 106 ? 106.14900 128.74500 138.42800 1.000 53.57515  ? 106 PHE A C    1 
ATOM   218  O O    . PHE A 1 106 ? 106.78200 129.21200 139.38000 1.000 56.71315  ? 106 PHE A O    1 
ATOM   219  C CB   . PHE A 1 106 ? 107.66100 128.97700 136.45900 1.000 52.57446  ? 106 PHE A CB   1 
ATOM   220  C CG   . PHE A 1 106 ? 108.92000 128.41600 135.86600 1.000 53.98626  ? 106 PHE A CG   1 
ATOM   221  C CD1  . PHE A 1 106 ? 109.24000 127.07900 136.02700 1.000 54.93011  ? 106 PHE A CD1  1 
ATOM   222  C CD2  . PHE A 1 106 ? 109.78900 129.22800 135.15900 1.000 53.66391  ? 106 PHE A CD2  1 
ATOM   223  C CE1  . PHE A 1 106 ? 110.39900 126.56100 135.48700 1.000 55.30042  ? 106 PHE A CE1  1 
ATOM   224  C CE2  . PHE A 1 106 ? 110.95000 128.71500 134.61600 1.000 55.35612  ? 106 PHE A CE2  1 
ATOM   225  C CZ   . PHE A 1 106 ? 111.25600 127.38000 134.78000 1.000 54.88681  ? 106 PHE A CZ   1 
ATOM   226  N N    . TYR A 1 107 ? 104.83100 128.88200 138.31700 1.000 65.57193  ? 107 TYR A N    1 
ATOM   227  C CA   . TYR A 1 107 ? 104.05900 129.68200 139.26000 1.000 65.17120  ? 107 TYR A CA   1 
ATOM   228  C C    . TYR A 1 107 ? 103.38100 128.85500 140.34400 1.000 67.27570  ? 107 TYR A C    1 
ATOM   229  O O    . TYR A 1 107 ? 102.65800 129.42000 141.17000 1.000 67.42916  ? 107 TYR A O    1 
ATOM   230  C CB   . TYR A 1 107 ? 103.01900 130.52300 138.51500 1.000 64.69231  ? 107 TYR A CB   1 
ATOM   231  C CG   . TYR A 1 107 ? 103.62300 131.69900 137.78400 1.000 66.19645  ? 107 TYR A CG   1 
ATOM   232  C CD1  . TYR A 1 107 ? 104.82000 132.26000 138.20900 1.000 64.99312  ? 107 TYR A CD1  1 
ATOM   233  C CD2  . TYR A 1 107 ? 102.99600 132.25500 136.67600 1.000 66.70692  ? 107 TYR A CD2  1 
ATOM   234  C CE1  . TYR A 1 107 ? 105.38000 133.33700 137.54900 1.000 64.79412  ? 107 TYR A CE1  1 
ATOM   235  C CE2  . TYR A 1 107 ? 103.54800 133.33300 136.01000 1.000 68.57655  ? 107 TYR A CE2  1 
ATOM   236  C CZ   . TYR A 1 107 ? 104.74100 133.87000 136.45100 1.000 68.88884  ? 107 TYR A CZ   1 
ATOM   237  O OH   . TYR A 1 107 ? 105.29500 134.94200 135.79100 1.000 69.08949  ? 107 TYR A OH   1 
ATOM   238  N N    . GLN A 1 108 ? 103.59100 127.54400 140.36600 1.000 73.89474  ? 108 GLN A N    1 
ATOM   239  C CA   . GLN A 1 108 ? 103.09000 126.71200 141.44800 1.000 72.97001  ? 108 GLN A CA   1 
ATOM   240  C C    . GLN A 1 108 ? 104.11400 126.65700 142.57400 1.000 73.03435  ? 108 GLN A C    1 
ATOM   241  O O    . GLN A 1 108 ? 105.32100 126.77100 142.34600 1.000 72.57744  ? 108 GLN A O    1 
ATOM   242  C CB   . GLN A 1 108 ? 102.78000 125.29800 140.95500 1.000 72.86043  ? 108 GLN A CB   1 
ATOM   243  C CG   . GLN A 1 108 ? 101.96100 125.25200 139.68000 1.000 73.36459  ? 108 GLN A CG   1 
ATOM   244  C CD   . GLN A 1 108 ? 100.60700 125.91000 139.83800 1.000 73.27154  ? 108 GLN A CD   1 
ATOM   245  O OE1  . GLN A 1 108 ? 100.45800 127.11100 139.61700 1.000 72.94595  ? 108 GLN A OE1  1 
ATOM   246  N NE2  . GLN A 1 108 ? 99.60900  125.12400 140.22400 1.000 73.09364  ? 108 GLN A NE2  1 
ATOM   247  N N    . GLU A 1 109 ? 103.61700 126.49900 143.79600 1.000 86.89412  ? 109 GLU A N    1 
ATOM   248  C CA   . GLU A 1 109 ? 104.48100 126.52000 144.96500 1.000 86.48161  ? 109 GLU A CA   1 
ATOM   249  C C    . GLU A 1 109 ? 105.64900 125.55400 144.76800 1.000 86.87224  ? 109 GLU A C    1 
ATOM   250  O O    . GLU A 1 109 ? 105.43700 124.41800 144.32000 1.000 86.88697  ? 109 GLU A O    1 
ATOM   251  C CB   . GLU A 1 109 ? 103.69000 126.14600 146.22000 1.000 85.55194  ? 109 GLU A CB   1 
ATOM   252  C CG   . GLU A 1 109 ? 104.44000 126.36700 147.52500 1.000 85.33148  ? 109 GLU A CG   1 
ATOM   253  C CD   . GLU A 1 109 ? 105.35800 125.21300 147.87700 1.000 86.70962  ? 109 GLU A CD   1 
ATOM   254  O OE1  . GLU A 1 109 ? 105.02500 124.06000 147.53000 1.000 87.42775  ? 109 GLU A OE1  1 
ATOM   255  O OE2  . GLU A 1 109 ? 106.41200 125.45800 148.49900 1.000 85.37977  ? 109 GLU A OE2  1 
ATOM   256  N N    . PRO A 1 110 ? 106.88300 125.96200 145.07900 1.000 86.88756  ? 110 PRO A N    1 
ATOM   257  C CA   . PRO A 1 110 ? 108.03600 125.08100 144.84700 1.000 86.41871  ? 110 PRO A CA   1 
ATOM   258  C C    . PRO A 1 110 ? 107.86600 123.71900 145.49900 1.000 85.72464  ? 110 PRO A C    1 
ATOM   259  O O    . PRO A 1 110 ? 107.66300 123.62700 146.71300 1.000 84.98529  ? 110 PRO A O    1 
ATOM   260  C CB   . PRO A 1 110 ? 109.20900 125.85700 145.46600 1.000 86.09576  ? 110 PRO A CB   1 
ATOM   261  C CG   . PRO A 1 110 ? 108.58400 126.96000 146.27900 1.000 86.86596  ? 110 PRO A CG   1 
ATOM   262  C CD   . PRO A 1 110 ? 107.28500 127.26900 145.61800 1.000 85.37845  ? 110 PRO A CD   1 
ATOM   263  N N    . ASN A 1 111 ? 107.94700 122.65400 144.70200 1.000 76.10771  ? 111 ASN A N    1 
ATOM   264  C CA   . ASN A 1 111 ? 107.81300 121.30100 145.21000 1.000 74.91679  ? 111 ASN A CA   1 
ATOM   265  C C    . ASN A 1 111 ? 108.86500 120.40900 144.56500 1.000 76.94642  ? 111 ASN A C    1 
ATOM   266  O O    . ASN A 1 111 ? 109.12100 120.52400 143.35700 1.000 77.91697  ? 111 ASN A O    1 
ATOM   267  C CB   . ASN A 1 111 ? 106.41500 120.73100 144.93900 1.000 74.91131  ? 111 ASN A CB   1 
ATOM   268  C CG   . ASN A 1 111 ? 106.23600 119.33600 145.50200 1.000 76.62661  ? 111 ASN A CG   1 
ATOM   269  O OD1  . ASN A 1 111 ? 106.08200 118.36900 144.75700 1.000 76.09176  ? 111 ASN A OD1  1 
ATOM   270  N ND2  . ASN A 1 111 ? 106.25800 119.22500 146.82500 1.000 76.72436  ? 111 ASN A ND2  1 
ATOM   271  N N    . PRO A 1 112 ? 109.49200 119.52100 145.34000 1.000 74.11974  ? 112 PRO A N    1 
ATOM   272  C CA   . PRO A 1 112 ? 110.45300 118.58700 144.73100 1.000 74.10641  ? 112 PRO A CA   1 
ATOM   273  C C    . PRO A 1 112 ? 109.79300 117.52900 143.86700 1.000 72.22121  ? 112 PRO A C    1 
ATOM   274  O O    . PRO A 1 112 ? 110.35300 117.14400 142.83200 1.000 71.57123  ? 112 PRO A O    1 
ATOM   275  C CB   . PRO A 1 112 ? 111.15800 117.97400 145.94900 1.000 73.84900  ? 112 PRO A CB   1 
ATOM   276  C CG   . PRO A 1 112 ? 110.16200 118.10500 147.05700 1.000 72.77057  ? 112 PRO A CG   1 
ATOM   277  C CD   . PRO A 1 112 ? 109.46000 119.40600 146.80700 1.000 73.03794  ? 112 PRO A CD   1 
ATOM   278  N N    . ASP A 1 113 ? 108.61600 117.04400 144.26200 1.000 66.83525  ? 113 ASP A N    1 
ATOM   279  C CA   . ASP A 1 113 ? 107.95000 115.96600 143.54200 1.000 67.65839  ? 113 ASP A CA   1 
ATOM   280  C C    . ASP A 1 113 ? 107.13900 116.44500 142.34500 1.000 69.37486  ? 113 ASP A C    1 
ATOM   281  O O    . ASP A 1 113 ? 106.67900 115.60800 141.56000 1.000 69.30584  ? 113 ASP A O    1 
ATOM   282  C CB   . ASP A 1 113 ? 107.03900 115.18800 144.49400 1.000 68.05036  ? 113 ASP A CB   1 
ATOM   283  C CG   . ASP A 1 113 ? 106.78800 113.76700 144.03100 1.000 70.52231  ? 113 ASP A CG   1 
ATOM   284  O OD1  . ASP A 1 113 ? 107.76800 113.06300 143.71100 1.000 70.75961  ? 113 ASP A OD1  1 
ATOM   285  O OD2  . ASP A 1 113 ? 105.61000 113.35400 143.98700 1.000 70.97214  ? 113 ASP A OD2  1 
ATOM   286  N N    . LEU A 1 114 ? 106.94500 117.75300 142.18200 1.000 66.77815  ? 114 LEU A N    1 
ATOM   287  C CA   . LEU A 1 114 ? 106.25200 118.25900 141.00400 1.000 65.21006  ? 114 LEU A CA   1 
ATOM   288  C C    . LEU A 1 114 ? 107.19200 118.44800 139.81900 1.000 66.06313  ? 114 LEU A C    1 
ATOM   289  O O    . LEU A 1 114 ? 106.81300 118.16900 138.67700 1.000 66.16987  ? 114 LEU A O    1 
ATOM   290  C CB   . LEU A 1 114 ? 105.55200 119.58200 141.32800 1.000 64.46538  ? 114 LEU A CB   1 
ATOM   291  C CG   . LEU A 1 114 ? 104.92300 120.31600 140.14200 1.000 65.54236  ? 114 LEU A CG   1 
ATOM   292  C CD1  . LEU A 1 114 ? 103.92800 119.42000 139.42100 1.000 65.40883  ? 114 LEU A CD1  1 
ATOM   293  C CD2  . LEU A 1 114 ? 104.25500 121.60500 140.59500 1.000 64.14921  ? 114 LEU A CD2  1 
ATOM   294  N N    . SER A 1 115 ? 108.41400 118.92100 140.07200 1.000 60.20629  ? 115 SER A N    1 
ATOM   295  C CA   . SER A 1 115 ? 109.35800 119.16200 138.98600 1.000 59.60245  ? 115 SER A CA   1 
ATOM   296  C C    . SER A 1 115 ? 109.70400 117.88000 138.24100 1.000 62.18128  ? 115 SER A C    1 
ATOM   297  O O    . SER A 1 115 ? 110.00500 117.92100 137.04300 1.000 63.21450  ? 115 SER A O    1 
ATOM   298  C CB   . SER A 1 115 ? 110.62700 119.81600 139.53100 1.000 61.84205  ? 115 SER A CB   1 
ATOM   299  O OG   . SER A 1 115 ? 110.32900 120.69800 140.59800 1.000 63.44550  ? 115 SER A OG   1 
ATOM   300  N N    . ARG A 1 116 ? 109.67100 116.73700 138.92800 1.000 57.39369  ? 116 ARG A N    1 
ATOM   301  C CA   . ARG A 1 116 ? 110.06100 115.47900 138.29800 1.000 54.96053  ? 116 ARG A CA   1 
ATOM   302  C C    . ARG A 1 116 ? 109.07300 115.05300 137.21800 1.000 55.69446  ? 116 ARG A C    1 
ATOM   303  O O    . ARG A 1 116 ? 109.47400 114.48300 136.19700 1.000 60.82459  ? 116 ARG A O    1 
ATOM   304  C CB   . ARG A 1 116 ? 110.20200 114.38600 139.35700 1.000 55.27307  ? 116 ARG A CB   1 
ATOM   305  C CG   . ARG A 1 116 ? 111.28800 113.37300 139.04700 1.000 56.31388  ? 116 ARG A CG   1 
ATOM   306  C CD   . ARG A 1 116 ? 111.39000 112.31200 140.12700 1.000 54.78735  ? 116 ARG A CD   1 
ATOM   307  N NE   . ARG A 1 116 ? 111.39400 110.96700 139.56500 1.000 55.09574  ? 116 ARG A NE   1 
ATOM   308  C CZ   . ARG A 1 116 ? 111.52500 109.85700 140.27700 1.000 57.87447  ? 116 ARG A CZ   1 
ATOM   309  N NH1  . ARG A 1 116 ? 111.66600 109.89100 141.59200 1.000 58.15561  ? 116 ARG A NH1  1 
ATOM   310  N NH2  . ARG A 1 116 ? 111.51400 108.68200 139.65400 1.000 58.18889  ? 116 ARG A NH2  1 
ATOM   311  N N    . TYR A 1 117 ? 107.78200 115.31900 137.41600 1.000 49.59609  ? 117 TYR A N    1 
ATOM   312  C CA   . TYR A 1 117 ? 106.77700 114.97500 136.41700 1.000 51.33082  ? 117 TYR A CA   1 
ATOM   313  C C    . TYR A 1 117 ? 106.71500 115.95700 135.25400 1.000 53.83916  ? 117 TYR A C    1 
ATOM   314  O O    . TYR A 1 117 ? 106.12500 115.62400 134.22100 1.000 58.68967  ? 117 TYR A O    1 
ATOM   315  C CB   . TYR A 1 117 ? 105.38800 114.90700 137.06000 1.000 52.07789  ? 117 TYR A CB   1 
ATOM   316  C CG   . TYR A 1 117 ? 105.19500 113.80500 138.07600 1.000 54.50344  ? 117 TYR A CG   1 
ATOM   317  C CD1  . TYR A 1 117 ? 105.86100 113.82800 139.29200 1.000 56.01475  ? 117 TYR A CD1  1 
ATOM   318  C CD2  . TYR A 1 117 ? 104.33100 112.74900 137.82400 1.000 55.22235  ? 117 TYR A CD2  1 
ATOM   319  C CE1  . TYR A 1 117 ? 105.68000 112.82500 140.22500 1.000 54.88692  ? 117 TYR A CE1  1 
ATOM   320  C CE2  . TYR A 1 117 ? 104.14400 111.74200 138.74900 1.000 54.74369  ? 117 TYR A CE2  1 
ATOM   321  C CZ   . TYR A 1 117 ? 104.82100 111.78500 139.94800 1.000 55.74968  ? 117 TYR A CZ   1 
ATOM   322  O OH   . TYR A 1 117 ? 104.63800 110.78400 140.87200 1.000 56.03441  ? 117 TYR A OH   1 
ATOM   323  N N    . SER A 1 118 ? 107.31900 117.13900 135.38400 1.000 43.36191  ? 118 SER A N    1 
ATOM   324  C CA   . SER A 1 118 ? 107.14700 118.18200 134.37700 1.000 43.06723  ? 118 SER A CA   1 
ATOM   325  C C    . SER A 1 118 ? 107.57300 117.73600 132.98100 1.000 41.87251  ? 118 SER A C    1 
ATOM   326  O O    . SER A 1 118 ? 107.04500 118.24600 131.98700 1.000 45.55290  ? 118 SER A O    1 
ATOM   327  C CB   . SER A 1 118 ? 107.92400 119.43100 134.79100 1.000 44.08379  ? 118 SER A CB   1 
ATOM   328  O OG   . SER A 1 118 ? 109.18000 119.49200 134.14100 1.000 46.28633  ? 118 SER A OG   1 
ATOM   329  N N    . VAL A 1 119 ? 108.51800 116.79900 132.87600 1.000 34.07478  ? 119 VAL A N    1 
ATOM   330  C CA   . VAL A 1 119 ? 109.05400 116.42100 131.57000 1.000 33.66699  ? 119 VAL A CA   1 
ATOM   331  C C    . VAL A 1 119 ? 107.98900 115.88000 130.62000 1.000 34.43869  ? 119 VAL A C    1 
ATOM   332  O O    . VAL A 1 119 ? 108.14700 115.97200 129.39200 1.000 38.32235  ? 119 VAL A O    1 
ATOM   333  C CB   . VAL A 1 119 ? 110.19600 115.39900 131.75800 1.000 33.91415  ? 119 VAL A CB   1 
ATOM   334  C CG1  . VAL A 1 119 ? 109.63600 113.99800 131.93200 1.000 36.60463  ? 119 VAL A CG1  1 
ATOM   335  C CG2  . VAL A 1 119 ? 111.15700 115.45300 130.58300 1.000 34.90264  ? 119 VAL A CG2  1 
ATOM   336  N N    . TRP A 1 120 ? 106.87800 115.36100 131.14900 1.000 24.89546  ? 120 TRP A N    1 
ATOM   337  C CA   . TRP A 1 120 ? 105.89000 114.72900 130.28200 1.000 28.80105  ? 120 TRP A CA   1 
ATOM   338  C C    . TRP A 1 120 ? 105.07200 115.75000 129.50400 1.000 33.67537  ? 120 TRP A C    1 
ATOM   339  O O    . TRP A 1 120 ? 104.70300 115.49600 128.34900 1.000 37.25342  ? 120 TRP A O    1 
ATOM   340  C CB   . TRP A 1 120 ? 104.97100 113.83100 131.11100 1.000 30.41428  ? 120 TRP A CB   1 
ATOM   341  C CG   . TRP A 1 120 ? 105.69100 112.68700 131.76100 1.000 31.78064  ? 120 TRP A CG   1 
ATOM   342  C CD1  . TRP A 1 120 ? 106.22300 112.66000 133.01700 1.000 34.11991  ? 120 TRP A CD1  1 
ATOM   343  C CD2  . TRP A 1 120 ? 105.96700 111.40600 131.18200 1.000 35.92667  ? 120 TRP A CD2  1 
ATOM   344  N NE1  . TRP A 1 120 ? 106.80800 111.44200 133.25700 1.000 29.34938  ? 120 TRP A NE1  1 
ATOM   345  C CE2  . TRP A 1 120 ? 106.66500 110.65400 132.14600 1.000 32.47969  ? 120 TRP A CE2  1 
ATOM   346  C CE3  . TRP A 1 120 ? 105.68900 110.82200 129.94300 1.000 37.57177  ? 120 TRP A CE3  1 
ATOM   347  C CZ2  . TRP A 1 120 ? 107.08800 109.34900 131.91100 1.000 30.06834  ? 120 TRP A CZ2  1 
ATOM   348  C CZ3  . TRP A 1 120 ? 106.11100 109.52600 129.71200 1.000 36.02925  ? 120 TRP A CZ3  1 
ATOM   349  C CH2  . TRP A 1 120 ? 106.80100 108.80400 130.69100 1.000 33.27444  ? 120 TRP A CH2  1 
ATOM   350  N N    . ALA A 1 121 ? 104.83900 116.92900 130.08100 1.000 27.40873  ? 121 ALA A N    1 
ATOM   351  C CA   . ALA A 1 121 ? 104.11500 117.96200 129.35100 1.000 24.99245  ? 121 ALA A CA   1 
ATOM   352  C C    . ALA A 1 121 ? 104.97600 118.53300 128.23500 1.000 27.76619  ? 121 ALA A C    1 
ATOM   353  O O    . ALA A 1 121 ? 104.48000 118.80900 127.13600 1.000 32.78541  ? 121 ALA A O    1 
ATOM   354  C CB   . ALA A 1 121 ? 103.66200 119.06300 130.30800 1.000 25.97689  ? 121 ALA A CB   1 
ATOM   355  N N    . ILE A 1 122 ? 106.27800 118.68400 128.48700 1.000 18.66757  ? 122 ILE A N    1 
ATOM   356  C CA   . ILE A 1 122 ? 107.18700 119.14100 127.44400 1.000 22.58328  ? 122 ILE A CA   1 
ATOM   357  C C    . ILE A 1 122 ? 107.24300 118.12300 126.31500 1.000 24.92749  ? 122 ILE A C    1 
ATOM   358  O O    . ILE A 1 122 ? 107.22100 118.48200 125.12900 1.000 28.49155  ? 122 ILE A O    1 
ATOM   359  C CB   . ILE A 1 122 ? 108.58400 119.40700 128.03500 1.000 24.46816  ? 122 ILE A CB   1 
ATOM   360  C CG1  . ILE A 1 122 ? 108.54100 120.60100 128.99100 1.000 29.38939  ? 122 ILE A CG1  1 
ATOM   361  C CG2  . ILE A 1 122 ? 109.60100 119.63500 126.92800 1.000 23.44247  ? 122 ILE A CG2  1 
ATOM   362  C CD1  . ILE A 1 122 ? 107.54300 121.66700 128.59400 1.000 30.93233  ? 122 ILE A CD1  1 
ATOM   363  N N    . LEU A 1 123 ? 107.28500 116.83300 126.66000 1.000 21.51145  ? 123 LEU A N    1 
ATOM   364  C CA   . LEU A 1 123 ? 107.34200 115.81500 125.61600 1.000 18.35357  ? 123 LEU A CA   1 
ATOM   365  C C    . LEU A 1 123 ? 106.06600 115.80900 124.78000 1.000 22.58342  ? 123 LEU A C    1 
ATOM   366  O O    . LEU A 1 123 ? 106.12400 115.72900 123.54600 1.000 23.40041  ? 123 LEU A O    1 
ATOM   367  C CB   . LEU A 1 123 ? 107.58800 114.44300 126.24100 1.000 20.46267  ? 123 LEU A CB   1 
ATOM   368  C CG   . LEU A 1 123 ? 107.90300 113.29200 125.28500 1.000 29.17363  ? 123 LEU A CG   1 
ATOM   369  C CD1  . LEU A 1 123 ? 109.37900 113.28300 124.92100 1.000 28.65494  ? 123 LEU A CD1  1 
ATOM   370  C CD2  . LEU A 1 123 ? 107.49200 111.96600 125.90000 1.000 26.55133  ? 123 LEU A CD2  1 
ATOM   371  N N    . THR A 1 124 ? 104.90400 115.91000 125.43000 1.000 24.27174  ? 124 THR A N    1 
ATOM   372  C CA   . THR A 1 124 ? 103.64900 115.96300 124.68500 1.000 22.89355  ? 124 THR A CA   1 
ATOM   373  C C    . THR A 1 124 ? 103.59900 117.18100 123.76800 1.000 23.62775  ? 124 THR A C    1 
ATOM   374  O O    . THR A 1 124 ? 103.24000 117.07100 122.58700 1.000 22.20462  ? 124 THR A O    1 
ATOM   375  C CB   . THR A 1 124 ? 102.46600 115.97400 125.65300 1.000 24.72674  ? 124 THR A CB   1 
ATOM   376  O OG1  . THR A 1 124 ? 102.67300 114.98800 126.67100 1.000 33.28135  ? 124 THR A OG1  1 
ATOM   377  C CG2  . THR A 1 124 ? 101.17400 115.66700 124.91600 1.000 22.62698  ? 124 THR A CG2  1 
ATOM   378  N N    . VAL A 1 125 ? 103.95300 118.35700 124.29600 1.000 27.23436  ? 125 VAL A N    1 
ATOM   379  C CA   . VAL A 1 125 ? 103.93900 119.57400 123.48800 1.000 22.76957  ? 125 VAL A CA   1 
ATOM   380  C C    . VAL A 1 125 ? 104.88600 119.46700 122.30200 1.000 24.57802  ? 125 VAL A C    1 
ATOM   381  O O    . VAL A 1 125 ? 104.61500 120.02400 121.23200 1.000 25.71984  ? 125 VAL A O    1 
ATOM   382  C CB   . VAL A 1 125 ? 104.27300 120.79900 124.36000 1.000 20.53567  ? 125 VAL A CB   1 
ATOM   383  C CG1  . VAL A 1 125 ? 104.19600 122.06800 123.53400 1.000 21.48945  ? 125 VAL A CG1  1 
ATOM   384  C CG2  . VAL A 1 125 ? 103.32200 120.88100 125.53700 1.000 26.14581  ? 125 VAL A CG2  1 
ATOM   385  N N    . VAL A 1 126 ? 106.00800 118.75800 122.46000 1.000 24.27797  ? 126 VAL A N    1 
ATOM   386  C CA   . VAL A 1 126 ? 106.97200 118.65900 121.36700 1.000 22.86579  ? 126 VAL A CA   1 
ATOM   387  C C    . VAL A 1 126 ? 106.66800 117.50800 120.41700 1.000 25.20675  ? 126 VAL A C    1 
ATOM   388  O O    . VAL A 1 126 ? 107.27200 117.43400 119.33600 1.000 28.17462  ? 126 VAL A O    1 
ATOM   389  C CB   . VAL A 1 126 ? 108.40300 118.52500 121.92900 1.000 24.21194  ? 126 VAL A CB   1 
ATOM   390  C CG1  . VAL A 1 126 ? 109.39600 118.18600 120.83000 1.000 23.22647  ? 126 VAL A CG1  1 
ATOM   391  C CG2  . VAL A 1 126 ? 108.81300 119.80400 122.63600 1.000 22.68347  ? 126 VAL A CG2  1 
ATOM   392  N N    . VAL A 1 127 ? 105.72600 116.63000 120.76000 1.000 29.92206  ? 127 VAL A N    1 
ATOM   393  C CA   . VAL A 1 127 ? 105.40500 115.50100 119.90300 1.000 25.41056  ? 127 VAL A CA   1 
ATOM   394  C C    . VAL A 1 127 ? 104.08300 115.67000 119.15400 1.000 27.63600  ? 127 VAL A C    1 
ATOM   395  O O    . VAL A 1 127 ? 103.96100 115.16900 118.03100 1.000 27.05503  ? 127 VAL A O    1 
ATOM   396  C CB   . VAL A 1 127 ? 105.40400 114.18900 120.71600 1.000 26.93583  ? 127 VAL A CB   1 
ATOM   397  C CG1  . VAL A 1 127 ? 104.65400 113.10000 119.97100 1.000 21.27187  ? 127 VAL A CG1  1 
ATOM   398  C CG2  . VAL A 1 127 ? 106.82600 113.74800 121.01200 1.000 27.72501  ? 127 VAL A CG2  1 
ATOM   399  N N    . VAL A 1 128 ? 103.08900 116.35700 119.72900 1.000 22.13971  ? 128 VAL A N    1 
ATOM   400  C CA   . VAL A 1 128 ? 101.76700 116.41600 119.10300 1.000 19.11442  ? 128 VAL A CA   1 
ATOM   401  C C    . VAL A 1 128 ? 101.57900 117.61000 118.17100 1.000 22.67268  ? 128 VAL A C    1 
ATOM   402  O O    . VAL A 1 128 ? 100.50600 117.74300 117.56800 1.000 22.70099  ? 128 VAL A O    1 
ATOM   403  C CB   . VAL A 1 128 ? 100.64700 116.42600 120.16400 1.000 24.84181  ? 128 VAL A CB   1 
ATOM   404  C CG1  . VAL A 1 128 ? 100.75600 115.20700 121.06000 1.000 22.32622  ? 128 VAL A CG1  1 
ATOM   405  C CG2  . VAL A 1 128 ? 100.69400 117.70700 120.97900 1.000 21.98431  ? 128 VAL A CG2  1 
ATOM   406  N N    . PHE A 1 129 ? 102.57900 118.47600 118.02200 1.000 24.59546  ? 129 PHE A N    1 
ATOM   407  C CA   . PHE A 1 129 ? 102.43900 119.70200 117.23700 1.000 24.61913  ? 129 PHE A CA   1 
ATOM   408  C C    . PHE A 1 129 ? 102.80400 119.42100 115.78000 1.000 23.28768  ? 129 PHE A C    1 
ATOM   409  O O    . PHE A 1 129 ? 103.96700 119.14600 115.46800 1.000 24.51894  ? 129 PHE A O    1 
ATOM   410  C CB   . PHE A 1 129 ? 103.32200 120.80200 117.82100 1.000 22.68726  ? 129 PHE A CB   1 
ATOM   411  C CG   . PHE A 1 129 ? 102.67200 122.15800 117.85400 1.000 24.63469  ? 129 PHE A CG   1 
ATOM   412  C CD1  . PHE A 1 129 ? 102.43600 122.85900 116.68500 1.000 23.68962  ? 129 PHE A CD1  1 
ATOM   413  C CD2  . PHE A 1 129 ? 102.31400 122.73700 119.05900 1.000 17.22661  ? 129 PHE A CD2  1 
ATOM   414  C CE1  . PHE A 1 129 ? 101.84700 124.10900 116.71800 1.000 20.27562  ? 129 PHE A CE1  1 
ATOM   415  C CE2  . PHE A 1 129 ? 101.72500 123.98500 119.09700 1.000 17.75776  ? 129 PHE A CE2  1 
ATOM   416  C CZ   . PHE A 1 129 ? 101.49200 124.67100 117.92600 1.000 16.48671  ? 129 PHE A CZ   1 
ATOM   417  N N    . GLU A 1 130 ? 101.81700 119.49700 114.88900 1.000 18.23213  ? 130 GLU A N    1 
ATOM   418  C CA   . GLU A 1 130 ? 102.02200 119.28600 113.46100 1.000 22.99874  ? 130 GLU A CA   1 
ATOM   419  C C    . GLU A 1 130 ? 101.82100 120.58200 112.67900 1.000 22.57332  ? 130 GLU A C    1 
ATOM   420  O O    . GLU A 1 130 ? 101.39900 121.60900 113.21600 1.000 22.71416  ? 130 GLU A O    1 
ATOM   421  C CB   . GLU A 1 130 ? 101.08400 118.19500 112.93100 1.000 18.45247  ? 130 GLU A CB   1 
ATOM   422  C CG   . GLU A 1 130 ? 101.04400 116.94500 113.79000 1.000 21.85178  ? 130 GLU A CG   1 
ATOM   423  C CD   . GLU A 1 130 ? 102.12700 115.95300 113.42600 1.000 23.42246  ? 130 GLU A CD   1 
ATOM   424  O OE1  . GLU A 1 130 ? 102.69600 116.06800 112.32100 1.000 23.06783  ? 130 GLU A OE1  1 
ATOM   425  O OE2  . GLU A 1 130 ? 102.41100 115.05700 114.24700 1.000 32.56479  ? 130 GLU A OE2  1 
ATOM   426  N N    . PHE A 1 131 ? 102.13100 120.51000 111.38100 1.000 16.85359  ? 131 PHE A N    1 
ATOM   427  C CA   . PHE A 1 131 ? 102.06600 121.67700 110.50500 1.000 13.48027  ? 131 PHE A CA   1 
ATOM   428  C C    . PHE A 1 131 ? 100.63900 122.05600 110.11900 1.000 9.98569   ? 131 PHE A C    1 
ATOM   429  O O    . PHE A 1 131 ? 100.35500 123.24100 109.92000 1.000 10.19664  ? 131 PHE A O    1 
ATOM   430  C CB   . PHE A 1 131 ? 102.89600 121.42300 109.24500 1.000 14.70973  ? 131 PHE A CB   1 
ATOM   431  C CG   . PHE A 1 131 ? 103.22300 122.66700 108.47000 1.000 15.93343  ? 131 PHE A CG   1 
ATOM   432  C CD1  . PHE A 1 131 ? 103.98600 123.67200 109.03500 1.000 17.66336  ? 131 PHE A CD1  1 
ATOM   433  C CD2  . PHE A 1 131 ? 102.77300 122.82500 107.17100 1.000 18.94591  ? 131 PHE A CD2  1 
ATOM   434  C CE1  . PHE A 1 131 ? 104.28700 124.81600 108.32200 1.000 20.46976  ? 131 PHE A CE1  1 
ATOM   435  C CE2  . PHE A 1 131 ? 103.07100 123.96500 106.45400 1.000 19.81053  ? 131 PHE A CE2  1 
ATOM   436  C CZ   . PHE A 1 131 ? 103.82900 124.96200 107.03000 1.000 20.80484  ? 131 PHE A CZ   1 
ATOM   437  N N    . THR A 1 132 ? 99.74000  121.08200 109.99900 1.000 16.44559  ? 132 THR A N    1 
ATOM   438  C CA   . THR A 1 132 ? 98.36300  121.32300 109.59500 1.000 4.65722   ? 132 THR A CA   1 
ATOM   439  C C    . THR A 1 132 ? 97.41200  120.83700 110.68300 1.000 8.54957   ? 132 THR A C    1 
ATOM   440  O O    . THR A 1 132 ? 97.78700  120.05600 111.56100 1.000 19.78273  ? 132 THR A O    1 
ATOM   441  C CB   . THR A 1 132 ? 98.04000  120.64000 108.25700 1.000 9.66879   ? 132 THR A CB   1 
ATOM   442  O OG1  . THR A 1 132 ? 98.57100  119.31000 108.25200 1.000 22.18087  ? 132 THR A OG1  1 
ATOM   443  C CG2  . THR A 1 132 ? 98.64300  121.41900 107.10300 1.000 7.49995   ? 132 THR A CG2  1 
ATOM   444  N N    . ILE A 1 133 ? 96.17000  121.32100 110.62300 1.000 10.13542  ? 133 ILE A N    1 
ATOM   445  C CA   . ILE A 1 133 ? 95.16900  120.93300 111.61400 1.000 13.83271  ? 133 ILE A CA   1 
ATOM   446  C C    . ILE A 1 133 ? 94.66200  119.51500 111.36900 1.000 17.51031  ? 133 ILE A C    1 
ATOM   447  O O    . ILE A 1 133 ? 94.43400  118.75000 112.31800 1.000 20.29675  ? 133 ILE A O    1 
ATOM   448  C CB   . ILE A 1 133 ? 94.01300  121.95000 111.61600 1.000 16.34911  ? 133 ILE A CB   1 
ATOM   449  C CG1  . ILE A 1 133 ? 94.49800  123.31000 112.11700 1.000 15.49669  ? 133 ILE A CG1  1 
ATOM   450  C CG2  . ILE A 1 133 ? 92.85500  121.44600 112.45900 1.000 18.17428  ? 133 ILE A CG2  1 
ATOM   451  C CD1  . ILE A 1 133 ? 93.93100  124.47200 111.34800 1.000 16.24915  ? 133 ILE A CD1  1 
ATOM   452  N N    . GLY A 1 134 ? 94.50800  119.12500 110.10200 1.000 6.57662   ? 134 GLY A N    1 
ATOM   453  C CA   . GLY A 1 134 ? 94.05100  117.77500 109.81500 1.000 6.32727   ? 134 GLY A CA   1 
ATOM   454  C C    . GLY A 1 134 ? 95.07400  116.71900 110.17900 1.000 16.23080  ? 134 GLY A C    1 
ATOM   455  O O    . GLY A 1 134 ? 94.72000  115.64400 110.67600 1.000 23.92850  ? 134 GLY A O    1 
ATOM   456  N N    . ALA A 1 135 ? 96.34800  117.03100 110.01200 1.000 6.45955   ? 135 ALA A N    1 
ATOM   457  C CA   . ALA A 1 135 ? 97.38300  116.09600 110.41400 1.000 2.17710   ? 135 ALA A CA   1 
ATOM   458  C C    . ALA A 1 135 ? 97.46700  115.95700 111.90000 1.000 13.15544  ? 135 ALA A C    1 
ATOM   459  O O    . ALA A 1 135 ? 97.67700  114.86800 112.39400 1.000 25.18038  ? 135 ALA A O    1 
ATOM   460  C CB   . ALA A 1 135 ? 98.70000  116.52700 109.90100 1.000 2.34451   ? 135 ALA A CB   1 
ATOM   461  N N    . THR A 1 136 ? 97.31100  117.04500 112.62500 1.000 7.94461   ? 136 THR A N    1 
ATOM   462  C CA   . THR A 1 136 ? 97.29600  116.98300 114.08000 1.000 7.33585   ? 136 THR A CA   1 
ATOM   463  C C    . THR A 1 136 ? 96.12100  116.15400 114.58200 1.000 16.09105  ? 136 THR A C    1 
ATOM   464  O O    . THR A 1 136 ? 96.29100  115.28800 115.44900 1.000 19.71146  ? 136 THR A O    1 
ATOM   465  C CB   . THR A 1 136 ? 97.23700  118.39700 114.66100 1.000 11.71917  ? 136 THR A CB   1 
ATOM   466  O OG1  . THR A 1 136 ? 98.36800  119.15000 114.21000 1.000 15.64043  ? 136 THR A OG1  1 
ATOM   467  C CG2  . THR A 1 136 ? 97.23700  118.35800 116.17900 1.000 15.15361  ? 136 THR A CG2  1 
ATOM   468  N N    . LEU A 1 137 ? 94.93300  116.35700 114.00500 1.000 7.59133   ? 137 LEU A N    1 
ATOM   469  C CA   . LEU A 1 137 ? 93.76500  115.61900 114.47900 1.000 3.49843   ? 137 LEU A CA   1 
ATOM   470  C C    . LEU A 1 137 ? 93.86700  114.13200 114.15300 1.000 13.00621  ? 137 LEU A C    1 
ATOM   471  O O    . LEU A 1 137 ? 93.58200  113.28100 115.00900 1.000 20.18585  ? 137 LEU A O    1 
ATOM   472  C CB   . LEU A 1 137 ? 92.49500  116.21100 113.86900 1.000 9.31500   ? 137 LEU A CB   1 
ATOM   473  C CG   . LEU A 1 137 ? 92.04700  117.59000 114.35700 1.000 13.72831  ? 137 LEU A CG   1 
ATOM   474  C CD1  . LEU A 1 137 ? 90.88600  118.09800 113.52100 1.000 7.94630   ? 137 LEU A CD1  1 
ATOM   475  C CD2  . LEU A 1 137 ? 91.67300  117.55400 115.82800 1.000 10.61176  ? 137 LEU A CD2  1 
ATOM   476  N N    . SER A 1 138 ? 94.32800  113.79400 112.94600 1.000 16.06649  ? 138 SER A N    1 
ATOM   477  C CA   . SER A 1 138 ? 94.42300  112.38600 112.57300 1.000 9.56626   ? 138 SER A CA   1 
ATOM   478  C C    . SER A 1 138 ? 95.48300  111.66000 113.39400 1.000 15.60923  ? 138 SER A C    1 
ATOM   479  O O    . SER A 1 138 ? 95.24800  110.54200 113.87900 1.000 22.17878  ? 138 SER A O    1 
ATOM   480  C CB   . SER A 1 138 ? 94.71400  112.26600 111.07800 1.000 12.16965  ? 138 SER A CB   1 
ATOM   481  O OG   . SER A 1 138 ? 96.09700  112.08500 110.83900 1.000 26.78965  ? 138 SER A OG   1 
ATOM   482  N N    . LYS A 1 139 ? 96.64300  112.28900 113.59600 1.000 4.88020   ? 139 LYS A N    1 
ATOM   483  C CA   . LYS A 1 139 ? 97.68800  111.63000 114.36600 1.000 1.61744   ? 139 LYS A CA   1 
ATOM   484  C C    . LYS A 1 139 ? 97.32700  111.53900 115.84100 1.000 12.78310  ? 139 LYS A C    1 
ATOM   485  O O    . LYS A 1 139 ? 97.68500  110.55400 116.49800 1.000 29.73012  ? 139 LYS A O    1 
ATOM   486  C CB   . LYS A 1 139 ? 99.01300  112.36000 114.16300 1.000 14.97507  ? 139 LYS A CB   1 
ATOM   487  C CG   . LYS A 1 139 ? 99.33200  112.59600 112.69600 1.000 13.49658  ? 139 LYS A CG   1 
ATOM   488  C CD   . LYS A 1 139 ? 100.79600 112.37400 112.38400 1.000 14.09871  ? 139 LYS A CD   1 
ATOM   489  C CE   . LYS A 1 139 ? 101.08200 112.65200 110.91900 1.000 16.24492  ? 139 LYS A CE   1 
ATOM   490  N NZ   . LYS A 1 139 ? 102.34500 113.41200 110.72600 1.000 19.27222  ? 139 LYS A NZ   1 
ATOM   491  N N    . GLY A 1 140 ? 96.59700  112.51900 116.38000 1.000 12.67504  ? 140 GLY A N    1 
ATOM   492  C CA   . GLY A 1 140 ? 96.15100  112.39900 117.75600 1.000 9.11961   ? 140 GLY A CA   1 
ATOM   493  C C    . GLY A 1 140 ? 95.14800  111.27700 117.93100 1.000 12.97646  ? 140 GLY A C    1 
ATOM   494  O O    . GLY A 1 140 ? 95.20500  110.52500 118.91000 1.000 27.24456  ? 140 GLY A O    1 
ATOM   495  N N    . PHE A 1 141 ? 94.24500  111.11500 116.96000 1.000 9.80737   ? 141 PHE A N    1 
ATOM   496  C CA   . PHE A 1 141 ? 93.30800  109.99700 117.00800 1.000 15.73460  ? 141 PHE A CA   1 
ATOM   497  C C    . PHE A 1 141 ? 94.04800  108.66300 116.99500 1.000 15.14809  ? 141 PHE A C    1 
ATOM   498  O O    . PHE A 1 141 ? 93.74800  107.75800 117.79000 1.000 25.45352  ? 141 PHE A O    1 
ATOM   499  C CB   . PHE A 1 141 ? 92.33800  110.09200 115.83000 1.000 16.73333  ? 141 PHE A CB   1 
ATOM   500  C CG   . PHE A 1 141 ? 91.19800  109.11900 115.89700 1.000 14.45580  ? 141 PHE A CG   1 
ATOM   501  C CD1  . PHE A 1 141 ? 90.11500  109.35600 116.72300 1.000 19.43179  ? 141 PHE A CD1  1 
ATOM   502  C CD2  . PHE A 1 141 ? 91.20500  107.97300 115.12400 1.000 15.19701  ? 141 PHE A CD2  1 
ATOM   503  C CE1  . PHE A 1 141 ? 89.06400  108.46500 116.78300 1.000 21.91437  ? 141 PHE A CE1  1 
ATOM   504  C CE2  . PHE A 1 141 ? 90.15900  107.07900 115.17900 1.000 16.91907  ? 141 PHE A CE2  1 
ATOM   505  C CZ   . PHE A 1 141 ? 89.08700  107.32500 116.00900 1.000 23.56715  ? 141 PHE A CZ   1 
ATOM   506  N N    . ASN A 1 142 ? 95.03200  108.52700 116.10300 1.000 13.06891  ? 142 ASN A N    1 
ATOM   507  C CA   . ASN A 1 142 ? 95.76700  107.26700 116.02300 1.000 17.05897  ? 142 ASN A CA   1 
ATOM   508  C C    . ASN A 1 142 ? 96.55000  106.98500 117.30200 1.000 23.51935  ? 142 ASN A C    1 
ATOM   509  O O    . ASN A 1 142 ? 96.55000  105.85200 117.80300 1.000 21.40974  ? 142 ASN A O    1 
ATOM   510  C CB   . ASN A 1 142 ? 96.70600  107.28000 114.81800 1.000 19.21111  ? 142 ASN A CB   1 
ATOM   511  C CG   . ASN A 1 142 ? 95.96400  107.27300 113.49800 1.000 28.00148  ? 142 ASN A CG   1 
ATOM   512  O OD1  . ASN A 1 142 ? 94.74200  107.13300 113.46000 1.000 28.13410  ? 142 ASN A OD1  1 
ATOM   513  N ND2  . ASN A 1 142 ? 96.70300  107.42300 112.40500 1.000 24.30484  ? 142 ASN A ND2  1 
ATOM   514  N N    . ARG A 1 143 ? 97.22900  108.00000 117.84700 1.000 26.48404  ? 143 ARG A N    1 
ATOM   515  C CA   . ARG A 1 143 ? 97.98000  107.79800 119.08200 1.000 18.64119  ? 143 ARG A CA   1 
ATOM   516  C C    . ARG A 1 143 ? 97.07300  107.47200 120.26200 1.000 21.61942  ? 143 ARG A C    1 
ATOM   517  O O    . ARG A 1 143 ? 97.46100  106.68900 121.14300 1.000 33.75770  ? 143 ARG A O    1 
ATOM   518  C CB   . ARG A 1 143 ? 98.81600  109.04000 119.38300 1.000 16.76355  ? 143 ARG A CB   1 
ATOM   519  C CG   . ARG A 1 143 ? 100.02100 109.20200 118.47500 1.000 19.26493  ? 143 ARG A CG   1 
ATOM   520  C CD   . ARG A 1 143 ? 100.86600 110.39100 118.88700 1.000 20.13844  ? 143 ARG A CD   1 
ATOM   521  N NE   . ARG A 1 143 ? 101.05900 111.32400 117.78400 1.000 24.26330  ? 143 ARG A NE   1 
ATOM   522  C CZ   . ARG A 1 143 ? 102.19400 111.46700 117.11300 1.000 28.22374  ? 143 ARG A CZ   1 
ATOM   523  N NH1  . ARG A 1 143 ? 103.26700 110.75200 117.41100 1.000 24.99761  ? 143 ARG A NH1  1 
ATOM   524  N NH2  . ARG A 1 143 ? 102.25300 112.34700 116.11800 1.000 23.66072  ? 143 ARG A NH2  1 
ATOM   525  N N    . ALA A 1 144 ? 95.83300  107.96800 120.25600 1.000 21.19383  ? 144 ALA A N    1 
ATOM   526  C CA   . ALA A 1 144 ? 94.94300  107.62900 121.35900 1.000 19.01969  ? 144 ALA A CA   1 
ATOM   527  C C    . ALA A 1 144 ? 94.39400  106.21800 121.22500 1.000 23.01332  ? 144 ALA A C    1 
ATOM   528  O O    . ALA A 1 144 ? 94.28500  105.50200 122.23200 1.000 25.72669  ? 144 ALA A O    1 
ATOM   529  C CB   . ALA A 1 144 ? 93.79600  108.63600 121.44300 1.000 18.53719  ? 144 ALA A CB   1 
ATOM   530  N N    . LEU A 1 145 ? 94.15200  105.75900 119.99500 1.000 26.24834  ? 145 LEU A N    1 
ATOM   531  C CA   . LEU A 1 145 ? 93.72200  104.37300 119.84300 1.000 24.83021  ? 145 LEU A CA   1 
ATOM   532  C C    . LEU A 1 145 ? 94.84900  103.42200 120.21500 1.000 27.25160  ? 145 LEU A C    1 
ATOM   533  O O    . LEU A 1 145 ? 94.61600  102.39400 120.86400 1.000 31.78393  ? 145 LEU A O    1 
ATOM   534  C CB   . LEU A 1 145 ? 93.24900  104.10000 118.41600 1.000 22.55917  ? 145 LEU A CB   1 
ATOM   535  C CG   . LEU A 1 145 ? 92.25400  105.06500 117.77900 1.000 31.07996  ? 145 LEU A CG   1 
ATOM   536  C CD1  . LEU A 1 145 ? 91.88600  104.57900 116.38800 1.000 29.28965  ? 145 LEU A CD1  1 
ATOM   537  C CD2  . LEU A 1 145 ? 91.01700  105.19900 118.65000 1.000 26.61549  ? 145 LEU A CD2  1 
ATOM   538  N N    . GLY A 1 146 ? 96.08000  103.76300 119.84300 1.000 26.17102  ? 146 GLY A N    1 
ATOM   539  C CA   . GLY A 1 146 ? 97.21600  102.96100 120.24000 1.000 23.84210  ? 146 GLY A CA   1 
ATOM   540  C C    . GLY A 1 146 ? 97.34400  102.84300 121.74600 1.000 30.01000  ? 146 GLY A C    1 
ATOM   541  O O    . GLY A 1 146 ? 97.38300  101.73100 122.28900 1.000 27.20465  ? 146 GLY A O    1 
ATOM   542  N N    . THR A 1 147 ? 97.44300  103.99000 122.42900 1.000 30.82036  ? 147 THR A N    1 
ATOM   543  C CA   . THR A 1 147 ? 97.60900  103.97400 123.88000 1.000 25.08839  ? 147 THR A CA   1 
ATOM   544  C C    . THR A 1 147 ? 96.47000  103.25100 124.59200 1.000 28.48931  ? 147 THR A C    1 
ATOM   545  O O    . THR A 1 147 ? 96.71200  102.53000 125.57400 1.000 37.67204  ? 147 THR A O    1 
ATOM   546  C CB   . THR A 1 147 ? 97.72700  105.40400 124.40900 1.000 26.59309  ? 147 THR A CB   1 
ATOM   547  O OG1  . THR A 1 147 ? 99.01700  105.93500 124.08300 1.000 33.38556  ? 147 THR A OG1  1 
ATOM   548  C CG2  . THR A 1 147 ? 97.54100  105.43000 125.91500 1.000 26.16271  ? 147 THR A CG2  1 
ATOM   549  N N    . LEU A 1 148 ? 95.24000  103.33900 124.07200 1.000 28.54606  ? 148 LEU A N    1 
ATOM   550  C CA   . LEU A 1 148 ? 94.15800  102.66200 124.77500 1.000 30.34183  ? 148 LEU A CA   1 
ATOM   551  C C    . LEU A 1 148 ? 94.12000  101.16600 124.49400 1.000 30.79454  ? 148 LEU A C    1 
ATOM   552  O O    . LEU A 1 148 ? 93.85200  100.38300 125.41400 1.000 34.81595  ? 148 LEU A O    1 
ATOM   553  C CB   . LEU A 1 148 ? 92.81600  103.29900 124.41100 1.000 36.59068  ? 148 LEU A CB   1 
ATOM   554  C CG   . LEU A 1 148 ? 92.21100  104.21700 125.47700 1.000 35.97715  ? 148 LEU A CG   1 
ATOM   555  C CD1  . LEU A 1 148 ? 93.18300  105.32500 125.85000 1.000 33.08660  ? 148 LEU A CD1  1 
ATOM   556  C CD2  . LEU A 1 148 ? 90.89700  104.80700 124.99900 1.000 33.63732  ? 148 LEU A CD2  1 
ATOM   557  N N    . SER A 1 149 ? 94.46800  100.73100 123.28100 1.000 29.79123  ? 149 SER A N    1 
ATOM   558  C CA   . SER A 1 149 ? 94.51800  99.29300  123.05000 1.000 30.10774  ? 149 SER A CA   1 
ATOM   559  C C    . SER A 1 149 ? 95.67900  98.66800  123.80800 1.000 34.54195  ? 149 SER A C    1 
ATOM   560  O O    . SER A 1 149 ? 95.58400  97.51600  124.25800 1.000 35.23847  ? 149 SER A O    1 
ATOM   561  C CB   . SER A 1 149 ? 94.63100  98.99600  121.55600 1.000 30.83936  ? 149 SER A CB   1 
ATOM   562  O OG   . SER A 1 149 ? 93.46800  99.41600  120.86600 1.000 36.85063  ? 149 SER A OG   1 
ATOM   563  N N    . ALA A 1 150 ? 96.75100  99.43400  124.02500 1.000 36.11719  ? 150 ALA A N    1 
ATOM   564  C CA   . ALA A 1 150 ? 97.87000  98.91100  124.79600 1.000 29.51003  ? 150 ALA A CA   1 
ATOM   565  C C    . ALA A 1 150 ? 97.48600  98.75500  126.26100 1.000 31.89680  ? 150 ALA A C    1 
ATOM   566  O O    . ALA A 1 150 ? 97.67700  97.68300  126.85000 1.000 32.94482  ? 150 ALA A O    1 
ATOM   567  C CB   . ALA A 1 150 ? 99.08600  99.82500  124.64700 1.000 29.29865  ? 150 ALA A CB   1 
ATOM   568  N N    . GLY A 1 151 ? 96.95600  99.81900  126.87600 1.000 35.60175  ? 151 GLY A N    1 
ATOM   569  C CA   . GLY A 1 151 ? 96.52600  99.68600  128.25800 1.000 32.60192  ? 151 GLY A CA   1 
ATOM   570  C C    . GLY A 1 151 ? 95.44000  98.64500  128.45200 1.000 31.19615  ? 151 GLY A C    1 
ATOM   571  O O    . GLY A 1 151 ? 95.39500  97.98800  129.50300 1.000 33.99499  ? 151 GLY A O    1 
ATOM   572  N N    . GLY A 1 152 ? 94.66900  98.36500  127.40400 1.000 40.25482  ? 152 GLY A N    1 
ATOM   573  C CA   . GLY A 1 152 ? 93.63100  97.36200  127.48800 1.000 41.27781  ? 152 GLY A CA   1 
ATOM   574  C C    . GLY A 1 152 ? 94.18300  95.95600  127.46000 1.000 43.66636  ? 152 GLY A C    1 
ATOM   575  O O    . GLY A 1 152 ? 93.81700  95.14000  128.30700 1.000 43.66537  ? 152 GLY A O    1 
ATOM   576  N N    . LEU A 1 153 ? 95.05600  95.64800  126.49900 1.000 45.84438  ? 153 LEU A N    1 
ATOM   577  C CA   . LEU A 1 153 ? 95.68600  94.33100  126.51000 1.000 40.33641  ? 153 LEU A CA   1 
ATOM   578  C C    . LEU A 1 153 ? 96.49000  94.11800  127.79000 1.000 41.52729  ? 153 LEU A C    1 
ATOM   579  O O    . LEU A 1 153 ? 96.49800  93.01500  128.35400 1.000 41.16574  ? 153 LEU A O    1 
ATOM   580  C CB   . LEU A 1 153 ? 96.57400  94.16200  125.27800 1.000 42.61403  ? 153 LEU A CB   1 
ATOM   581  C CG   . LEU A 1 153 ? 96.84000  92.72300  124.83600 1.000 44.40426  ? 153 LEU A CG   1 
ATOM   582  C CD1  . LEU A 1 153 ? 95.53400  92.00300  124.54100 1.000 43.81261  ? 153 LEU A CD1  1 
ATOM   583  C CD2  . LEU A 1 153 ? 97.75400  92.69900  123.62200 1.000 45.18768  ? 153 LEU A CD2  1 
ATOM   584  N N    . ALA A 1 154 ? 97.15700  95.16500  128.27900 1.000 46.34081  ? 154 ALA A N    1 
ATOM   585  C CA   . ALA A 1 154 ? 97.93800  95.02100  129.50300 1.000 42.86004  ? 154 ALA A CA   1 
ATOM   586  C C    . ALA A 1 154 ? 97.04900  94.63900  130.68000 1.000 45.95680  ? 154 ALA A C    1 
ATOM   587  O O    . ALA A 1 154 ? 97.36900  93.71500  131.44400 1.000 47.78580  ? 154 ALA A O    1 
ATOM   588  C CB   . ALA A 1 154 ? 98.69800  96.31400  129.79400 1.000 43.89160  ? 154 ALA A CB   1 
ATOM   589  N N    . LEU A 1 155 ? 95.93400  95.35900  130.86400 1.000 56.95046  ? 155 LEU A N    1 
ATOM   590  C CA   . LEU A 1 155 ? 95.03300  95.00400  131.95300 1.000 54.26518  ? 155 LEU A CA   1 
ATOM   591  C C    . LEU A 1 155 ? 94.32400  93.67700  131.71000 1.000 52.08334  ? 155 LEU A C    1 
ATOM   592  O O    . LEU A 1 155 ? 93.91100  93.02600  132.67500 1.000 51.76844  ? 155 LEU A O    1 
ATOM   593  C CB   . LEU A 1 155 ? 94.00600  96.11500  132.17300 1.000 53.99589  ? 155 LEU A CB   1 
ATOM   594  C CG   . LEU A 1 155 ? 94.39400  97.17200  133.20900 1.000 53.27098  ? 155 LEU A CG   1 
ATOM   595  C CD1  . LEU A 1 155 ? 93.15700  97.82700  133.80100 1.000 53.93793  ? 155 LEU A CD1  1 
ATOM   596  C CD2  . LEU A 1 155 ? 95.25800  96.56100  134.30100 1.000 52.18954  ? 155 LEU A CD2  1 
ATOM   597  N N    . GLY A 1 156 ? 94.18000  93.25800  130.45400 1.000 61.89012  ? 156 GLY A N    1 
ATOM   598  C CA   . GLY A 1 156 ? 93.57400  91.98300  130.14100 1.000 62.52732  ? 156 GLY A CA   1 
ATOM   599  C C    . GLY A 1 156 ? 94.53700  90.82400  130.12500 1.000 63.84795  ? 156 GLY A C    1 
ATOM   600  O O    . GLY A 1 156 ? 94.14800  89.69700  129.80200 1.000 61.70701  ? 156 GLY A O    1 
ATOM   601  N N    . MET A 1 157 ? 95.79200  91.07600  130.47000 1.000 71.61439  ? 157 MET A N    1 
ATOM   602  C CA   . MET A 1 157 ? 96.81500  90.03900  130.51800 1.000 70.24117  ? 157 MET A CA   1 
ATOM   603  C C    . MET A 1 157 ? 97.43300  89.88600  131.89800 1.000 69.66121  ? 157 MET A C    1 
ATOM   604  O O    . MET A 1 157 ? 97.75000  88.76200  132.30700 1.000 67.14590  ? 157 MET A O    1 
ATOM   605  C CB   . MET A 1 157 ? 97.92000  90.33000  129.49200 1.000 68.81767  ? 157 MET A CB   1 
ATOM   606  C CG   . MET A 1 157 ? 98.93500  89.21000  129.33900 1.000 67.76482  ? 157 MET A CG   1 
ATOM   607  S SD   . MET A 1 157 ? 98.56700  88.10800  127.96000 1.000 73.98392  ? 157 MET A SD   1 
ATOM   608  C CE   . MET A 1 157 ? 97.89300  89.26200  126.77000 1.000 70.78132  ? 157 MET A CE   1 
ATOM   609  N N    . ALA A 1 158 ? 97.62900  90.98400  132.63300 1.000 76.37552  ? 158 ALA A N    1 
ATOM   610  C CA   . ALA A 1 158 ? 98.19100  90.83800  133.97200 1.000 74.77176  ? 158 ALA A CA   1 
ATOM   611  C C    . ALA A 1 158 ? 97.28800  89.98800  134.86000 1.000 77.15497  ? 158 ALA A C    1 
ATOM   612  O O    . ALA A 1 158 ? 97.77200  89.31100  135.78100 1.000 76.82912  ? 158 ALA A O    1 
ATOM   613  C CB   . ALA A 1 158 ? 98.42400  92.21000  134.60300 1.000 73.59657  ? 158 ALA A CB   1 
ATOM   614  N N    . GLU A 1 159 ? 95.98200  89.96900  134.57300 1.000 87.05279  ? 159 GLU A N    1 
ATOM   615  C CA   . GLU A 1 159 ? 95.07900  89.11500  135.33600 1.000 83.99324  ? 159 GLU A CA   1 
ATOM   616  C C    . GLU A 1 159 ? 95.38200  87.64700  135.07600 1.000 84.71762  ? 159 GLU A C    1 
ATOM   617  O O    . GLU A 1 159 ? 95.48200  86.84900  136.01500 1.000 85.87518  ? 159 GLU A O    1 
ATOM   618  C CB   . GLU A 1 159 ? 93.62600  89.43900  134.99000 1.000 85.47395  ? 159 GLU A CB   1 
ATOM   619  C CG   . GLU A 1 159 ? 92.66700  89.32700  136.16600 1.000 85.39864  ? 159 GLU A CG   1 
ATOM   620  C CD   . GLU A 1 159 ? 92.79900  90.48100  137.14000 1.000 86.30485  ? 159 GLU A CD   1 
ATOM   621  O OE1  . GLU A 1 159 ? 93.86400  90.60000  137.78200 1.000 85.58520  ? 159 GLU A OE1  1 
ATOM   622  O OE2  . GLU A 1 159 ? 91.83800  91.26800  137.26500 1.000 86.27310  ? 159 GLU A OE2  1 
ATOM   623  N N    . LEU A 1 160 ? 95.52600  87.26500  133.80200 1.000 83.35370  ? 160 LEU A N    1 
ATOM   624  C CA   . LEU A 1 160 ? 95.94400  85.89800  133.51900 1.000 82.80253  ? 160 LEU A CA   1 
ATOM   625  C C    . LEU A 1 160 ? 97.27400  85.61000  134.19300 1.000 83.43184  ? 160 LEU A C    1 
ATOM   626  O O    . LEU A 1 160 ? 97.54100  84.47100  134.59400 1.000 82.93616  ? 160 LEU A O    1 
ATOM   627  C CB   . LEU A 1 160 ? 96.04400  85.66700  132.01200 1.000 82.98714  ? 160 LEU A CB   1 
ATOM   628  C CG   . LEU A 1 160 ? 94.88500  84.90600  131.36800 1.000 82.83463  ? 160 LEU A CG   1 
ATOM   629  C CD1  . LEU A 1 160 ? 94.98900  84.95100  129.85300 1.000 84.40190  ? 160 LEU A CD1  1 
ATOM   630  C CD2  . LEU A 1 160 ? 94.85800  83.47000  131.86300 1.000 83.18745  ? 160 LEU A CD2  1 
ATOM   631  N N    . SER A 1 161 ? 98.11700  86.63700  134.32200 1.000 86.95588  ? 161 SER A N    1 
ATOM   632  C CA   . SER A 1 161 ? 99.42000  86.45100  134.94900 1.000 85.84747  ? 161 SER A CA   1 
ATOM   633  C C    . SER A 1 161 ? 99.25200  86.01500  136.39800 1.000 85.45528  ? 161 SER A C    1 
ATOM   634  O O    . SER A 1 161 ? 99.88300  85.05300  136.85100 1.000 87.17704  ? 161 SER A O    1 
ATOM   635  C CB   . SER A 1 161 ? 100.23900 87.73900  134.86200 1.000 85.91241  ? 161 SER A CB   1 
ATOM   636  O OG   . SER A 1 161 ? 101.49100 87.59200  135.50800 1.000 84.31983  ? 161 SER A OG   1 
ATOM   637  N N    . THR A 1 162 ? 98.40200  86.72800  137.14200 1.000 92.51178  ? 162 THR A N    1 
ATOM   638  C CA   . THR A 1 162 ? 98.22800  86.43900  138.56500 1.000 93.80835  ? 162 THR A CA   1 
ATOM   639  C C    . THR A 1 162 ? 97.84800  84.98100  138.79900 1.000 93.23941  ? 162 THR A C    1 
ATOM   640  O O    . THR A 1 162 ? 98.27200  84.37000  139.78700 1.000 92.59561  ? 162 THR A O    1 
ATOM   641  C CB   . THR A 1 162 ? 97.16600  87.35900  139.16300 1.000 93.87380  ? 162 THR A CB   1 
ATOM   642  O OG1  . THR A 1 162 ? 95.86300  86.84500  138.85900 1.000 93.98806  ? 162 THR A OG1  1 
ATOM   643  C CG2  . THR A 1 162 ? 97.29300  88.74900  138.57900 1.000 93.67979  ? 162 THR A CG2  1 
ATOM   644  N N    . LEU A 1 163 ? 97.04400  84.40800  137.89900 1.000 92.70434  ? 163 LEU A N    1 
ATOM   645  C CA   . LEU A 1 163 ? 96.61600  83.01900  138.04300 1.000 92.62244  ? 163 LEU A CA   1 
ATOM   646  C C    . LEU A 1 163 ? 97.79300  82.05400  138.09600 1.000 94.28971  ? 163 LEU A C    1 
ATOM   647  O O    . LEU A 1 163 ? 97.72500  81.03400  138.79200 1.000 93.67927  ? 163 LEU A O    1 
ATOM   648  C CB   . LEU A 1 163 ? 95.67700  82.64200  136.89700 1.000 92.35923  ? 163 LEU A CB   1 
ATOM   649  C CG   . LEU A 1 163 ? 94.98500  81.28100  136.99200 1.000 92.74338  ? 163 LEU A CG   1 
ATOM   650  C CD1  . LEU A 1 163 ? 93.60200  81.33700  136.36400 1.000 93.77102  ? 163 LEU A CD1  1 
ATOM   651  C CD2  . LEU A 1 163 ? 95.83000  80.19900  136.33500 1.000 92.26366  ? 163 LEU A CD2  1 
ATOM   652  N N    . PHE A 1 164 ? 98.87400  82.34700  137.37100 1.000 97.16330  ? 164 PHE A N    1 
ATOM   653  C CA   . PHE A 1 164 ? 99.99800  81.41700  137.31500 1.000 96.35766  ? 164 PHE A CA   1 
ATOM   654  C C    . PHE A 1 164 ? 100.56500 81.13400  138.70100 1.000 95.49946  ? 164 PHE A C    1 
ATOM   655  O O    . PHE A 1 164 ? 100.86600 79.98000  139.03000 1.000 94.61023  ? 164 PHE A O    1 
ATOM   656  C CB   . PHE A 1 164 ? 101.08200 81.95900  136.38500 1.000 94.79717  ? 164 PHE A CB   1 
ATOM   657  C CG   . PHE A 1 164 ? 100.86700 81.60400  134.94200 1.000 94.08836  ? 164 PHE A CG   1 
ATOM   658  C CD1  . PHE A 1 164 ? 99.62100  81.75400  134.35800 1.000 94.14275  ? 164 PHE A CD1  1 
ATOM   659  C CD2  . PHE A 1 164 ? 101.90700 81.11200  134.17300 1.000 95.66406  ? 164 PHE A CD2  1 
ATOM   660  C CE1  . PHE A 1 164 ? 99.41700  81.42500  133.03200 1.000 95.30486  ? 164 PHE A CE1  1 
ATOM   661  C CE2  . PHE A 1 164 ? 101.71000 80.78100  132.84600 1.000 96.91652  ? 164 PHE A CE2  1 
ATOM   662  C CZ   . PHE A 1 164 ? 100.46300 80.93800  132.27500 1.000 96.01665  ? 164 PHE A CZ   1 
ATOM   663  N N    . GLY A 1 165 ? 100.71800 82.15900  139.52600 1.000 97.45038  ? 165 GLY A N    1 
ATOM   664  C CA   . GLY A 1 165 ? 101.22100 81.97800  140.87800 1.000 98.16425  ? 165 GLY A CA   1 
ATOM   665  C C    . GLY A 1 165 ? 102.69900 82.33000  140.98600 1.000 98.27116  ? 165 GLY A C    1 
ATOM   666  O O    . GLY A 1 165 ? 103.11400 83.42000  140.59800 1.000 98.57922  ? 165 GLY A O    1 
ATOM   667  N N    . ASP A 1 166 ? 103.48900 81.39700  141.52200 1.000 100.22868 ? 166 ASP A N    1 
ATOM   668  C CA   . ASP A 1 166 ? 104.91000 81.65800  141.73500 1.000 100.35260 ? 166 ASP A CA   1 
ATOM   669  C C    . ASP A 1 166 ? 105.60900 82.01200  140.42800 1.000 100.58444 ? 166 ASP A C    1 
ATOM   670  O O    . ASP A 1 166 ? 106.36200 82.99000  140.36000 1.000 99.65622  ? 166 ASP A O    1 
ATOM   671  C CB   . ASP A 1 166 ? 105.57000 80.44400  142.39000 1.000 100.28855 ? 166 ASP A CB   1 
ATOM   672  C CG   . ASP A 1 166 ? 105.04700 79.13100  141.84300 1.000 100.29502 ? 166 ASP A CG   1 
ATOM   673  O OD1  . ASP A 1 166 ? 104.47200 79.13400  140.73400 1.000 99.92170  ? 166 ASP A OD1  1 
ATOM   674  O OD2  . ASP A 1 166 ? 105.21100 78.09500  142.52100 1.000 100.48208 ? 166 ASP A OD2  1 
ATOM   675  N N    . TRP A 1 167 ? 105.37700 81.22700  139.37500 1.000 100.77755 ? 167 TRP A N    1 
ATOM   676  C CA   . TRP A 1 167 ? 106.00500 81.48500  138.08000 1.000 100.09695 ? 167 TRP A CA   1 
ATOM   677  C C    . TRP A 1 167 ? 105.26900 82.61900  137.36100 1.000 100.85853 ? 167 TRP A C    1 
ATOM   678  O O    . TRP A 1 167 ? 104.72000 82.46600  136.27100 1.000 101.31431 ? 167 TRP A O    1 
ATOM   679  C CB   . TRP A 1 167 ? 106.03800 80.21900  137.23100 1.000 99.46086  ? 167 TRP A CB   1 
ATOM   680  C CG   . TRP A 1 167 ? 106.36500 78.96100  137.98600 1.000 100.40863 ? 167 TRP A CG   1 
ATOM   681  C CD1  . TRP A 1 167 ? 107.10500 78.85400  139.12900 1.000 100.50616 ? 167 TRP A CD1  1 
ATOM   682  C CD2  . TRP A 1 167 ? 105.97300 77.62800  137.63700 1.000 101.02226 ? 167 TRP A CD2  1 
ATOM   683  N NE1  . TRP A 1 167 ? 107.18900 77.53900  139.51600 1.000 100.93986 ? 167 TRP A NE1  1 
ATOM   684  C CE2  . TRP A 1 167 ? 106.50400 76.76600  138.61700 1.000 100.92982 ? 167 TRP A CE2  1 
ATOM   685  C CE3  . TRP A 1 167 ? 105.22100 77.08000  136.59300 1.000 100.37761 ? 167 TRP A CE3  1 
ATOM   686  C CZ2  . TRP A 1 167 ? 106.30700 75.38700  138.58300 1.000 100.46455 ? 167 TRP A CZ2  1 
ATOM   687  C CZ3  . TRP A 1 167 ? 105.02700 75.71100  136.56100 1.000 100.11740 ? 167 TRP A CZ3  1 
ATOM   688  C CH2  . TRP A 1 167 ? 105.56800 74.88000  137.55000 1.000 100.51642 ? 167 TRP A CH2  1 
ATOM   689  N N    . GLU A 1 168 ? 105.27000 83.78300  138.01100 1.000 93.74115  ? 168 GLU A N    1 
ATOM   690  C CA   . GLU A 1 168 ? 104.60300 84.97100  137.49300 1.000 94.10624  ? 168 GLU A CA   1 
ATOM   691  C C    . GLU A 1 168 ? 105.51200 85.78200  136.57600 1.000 94.22043  ? 168 GLU A C    1 
ATOM   692  O O    . GLU A 1 168 ? 105.09200 86.20200  135.49300 1.000 94.06330  ? 168 GLU A O    1 
ATOM   693  C CB   . GLU A 1 168 ? 104.11100 85.83900  138.65500 1.000 93.69990  ? 168 GLU A CB   1 
ATOM   694  C CG   . GLU A 1 168 ? 102.60000 85.99000  138.72300 1.000 94.32690  ? 168 GLU A CG   1 
ATOM   695  C CD   . GLU A 1 168 ? 102.13100 86.55700  140.04800 1.000 94.35212  ? 168 GLU A CD   1 
ATOM   696  O OE1  . GLU A 1 168 ? 102.53100 87.69000  140.38700 1.000 93.78192  ? 168 GLU A OE1  1 
ATOM   697  O OE2  . GLU A 1 168 ? 101.36000 85.86900  140.75100 1.000 94.67690  ? 168 GLU A OE2  1 
ATOM   698  N N    . GLU A 1 169 ? 106.75900 86.00600  136.99700 1.000 87.29171  ? 169 GLU A N    1 
ATOM   699  C CA   . GLU A 1 169 ? 107.68700 86.79100  136.18900 1.000 86.64145  ? 169 GLU A CA   1 
ATOM   700  C C    . GLU A 1 169 ? 107.96400 86.12000  134.85000 1.000 86.81237  ? 169 GLU A C    1 
ATOM   701  O O    . GLU A 1 169 ? 108.12400 86.79900  133.82800 1.000 88.10150  ? 169 GLU A O    1 
ATOM   702  C CB   . GLU A 1 169 ? 108.99000 87.01200  136.95700 1.000 85.52956  ? 169 GLU A CB   1 
ATOM   703  C CG   . GLU A 1 169 ? 108.79800 87.59300  138.34800 1.000 86.96612  ? 169 GLU A CG   1 
ATOM   704  C CD   . GLU A 1 169 ? 108.00000 88.88100  138.33700 1.000 88.15192  ? 169 GLU A CD   1 
ATOM   705  O OE1  . GLU A 1 169 ? 106.75400 88.80900  138.36100 1.000 87.01591  ? 169 GLU A OE1  1 
ATOM   706  O OE2  . GLU A 1 169 ? 108.61900 89.96500  138.30700 1.000 89.00773  ? 169 GLU A OE2  1 
ATOM   707  N N    . ILE A 1 170 ? 108.03900 84.78800  134.83600 1.000 78.10044  ? 170 ILE A N    1 
ATOM   708  C CA   . ILE A 1 170 ? 108.29400 84.07500  133.58800 1.000 78.68486  ? 170 ILE A CA   1 
ATOM   709  C C    . ILE A 1 170 ? 107.18000 84.33800  132.58300 1.000 79.53269  ? 170 ILE A C    1 
ATOM   710  O O    . ILE A 1 170 ? 107.43800 84.55500  131.39300 1.000 80.92157  ? 170 ILE A O    1 
ATOM   711  C CB   . ILE A 1 170 ? 108.46800 82.57000  133.86100 1.000 78.41317  ? 170 ILE A CB   1 
ATOM   712  C CG1  . ILE A 1 170 ? 109.54500 82.34400  134.92300 1.000 78.12289  ? 170 ILE A CG1  1 
ATOM   713  C CG2  . ILE A 1 170 ? 108.81500 81.83200  132.57800 1.000 78.66198  ? 170 ILE A CG2  1 
ATOM   714  C CD1  . ILE A 1 170 ? 110.75900 83.22900  134.75600 1.000 77.88278  ? 170 ILE A CD1  1 
ATOM   715  N N    . PHE A 1 171 ? 105.92700 84.34500  133.04400 1.000 79.48271  ? 171 PHE A N    1 
ATOM   716  C CA   . PHE A 1 171 ? 104.81200 84.62500  132.14300 1.000 79.72517  ? 171 PHE A CA   1 
ATOM   717  C C    . PHE A 1 171 ? 104.93000 86.02200  131.54300 1.000 79.39257  ? 171 PHE A C    1 
ATOM   718  O O    . PHE A 1 171 ? 104.72900 86.21100  130.33600 1.000 80.52518  ? 171 PHE A O    1 
ATOM   719  C CB   . PHE A 1 171 ? 103.48600 84.46300  132.88600 1.000 78.50982  ? 171 PHE A CB   1 
ATOM   720  C CG   . PHE A 1 171 ? 102.27700 84.63600  132.01400 1.000 80.26571  ? 171 PHE A CG   1 
ATOM   721  C CD1  . PHE A 1 171 ? 102.26400 84.14400  130.72000 1.000 80.46246  ? 171 PHE A CD1  1 
ATOM   722  C CD2  . PHE A 1 171 ? 101.15400 85.29100  132.48600 1.000 79.67841  ? 171 PHE A CD2  1 
ATOM   723  C CE1  . PHE A 1 171 ? 101.15300 84.30200  129.91400 1.000 79.98217  ? 171 PHE A CE1  1 
ATOM   724  C CE2  . PHE A 1 171 ? 100.04000 85.45200  131.68600 1.000 80.24896  ? 171 PHE A CE2  1 
ATOM   725  C CZ   . PHE A 1 171 ? 100.04000 84.95700  130.39800 1.000 80.31421  ? 171 PHE A CZ   1 
ATOM   726  N N    . CYS A 1 172 ? 105.25400 87.01400  132.37200 1.000 64.63698  ? 172 CYS A N    1 
ATOM   727  C CA   . CYS A 1 172 ? 105.37800 88.38000  131.87700 1.000 66.47983  ? 172 CYS A CA   1 
ATOM   728  C C    . CYS A 1 172 ? 106.49600 88.48000  130.84700 1.000 70.12346  ? 172 CYS A C    1 
ATOM   729  O O    . CYS A 1 172 ? 106.32000 89.07000  129.77200 1.000 72.09153  ? 172 CYS A O    1 
ATOM   730  C CB   . CYS A 1 172 ? 105.62700 89.33600  133.04400 1.000 66.97003  ? 172 CYS A CB   1 
ATOM   731  S SG   . CYS A 1 172 ? 104.12800 89.96300  133.83400 1.000 74.37942  ? 172 CYS A SG   1 
ATOM   732  N N    . THR A 1 173 ? 107.67900 87.96300  131.19200 1.000 61.61106  ? 173 THR A N    1 
ATOM   733  C CA   . THR A 1 173 ? 108.80400 88.01700  130.26700 1.000 57.69781  ? 173 THR A CA   1 
ATOM   734  C C    . THR A 1 173 ? 108.51600 87.24300  128.98700 1.000 58.16765  ? 173 THR A C    1 
ATOM   735  O O    . THR A 1 173 ? 109.08800 87.55300  127.93600 1.000 62.28910  ? 173 THR A O    1 
ATOM   736  C CB   . THR A 1 173 ? 110.06500 87.47700  130.94200 1.000 58.77013  ? 173 THR A CB   1 
ATOM   737  O OG1  . THR A 1 173 ? 110.05900 87.84200  132.32800 1.000 60.12368  ? 173 THR A OG1  1 
ATOM   738  C CG2  . THR A 1 173 ? 111.31000 88.04800  130.28200 1.000 60.97977  ? 173 THR A CG2  1 
ATOM   739  N N    . LEU A 1 174 ? 107.63600 86.24000  129.04600 1.000 49.38749  ? 174 LEU A N    1 
ATOM   740  C CA   . LEU A 1 174 ? 107.30400 85.47100  127.85500 1.000 51.74170  ? 174 LEU A CA   1 
ATOM   741  C C    . LEU A 1 174 ? 106.21000 86.12200  127.02700 1.000 56.11585  ? 174 LEU A C    1 
ATOM   742  O O    . LEU A 1 174 ? 106.05200 85.78200  125.84900 1.000 57.42478  ? 174 LEU A O    1 
ATOM   743  C CB   . LEU A 1 174 ? 106.87100 84.05300  128.24000 1.000 53.50941  ? 174 LEU A CB   1 
ATOM   744  C CG   . LEU A 1 174 ? 107.88200 82.93900  127.96700 1.000 56.52656  ? 174 LEU A CG   1 
ATOM   745  C CD1  . LEU A 1 174 ? 108.08400 82.75700  126.47100 1.000 55.32686  ? 174 LEU A CD1  1 
ATOM   746  C CD2  . LEU A 1 174 ? 109.20200 83.22900  128.66300 1.000 55.45933  ? 174 LEU A CD2  1 
ATOM   747  N N    . SER A 1 175 ? 105.45600 87.04600  127.61700 1.000 47.66313  ? 175 SER A N    1 
ATOM   748  C CA   . SER A 1 175 ? 104.44800 87.79000  126.87300 1.000 46.10301  ? 175 SER A CA   1 
ATOM   749  C C    . SER A 1 175 ? 105.03100 89.03800  126.22800 1.000 45.00348  ? 175 SER A C    1 
ATOM   750  O O    . SER A 1 175 ? 104.60100 89.42900  125.13200 1.000 45.09266  ? 175 SER A O    1 
ATOM   751  C CB   . SER A 1 175 ? 103.29000 88.18100  127.79300 1.000 45.24201  ? 175 SER A CB   1 
ATOM   752  O OG   . SER A 1 175 ? 103.77100 88.74600  128.99900 1.000 45.21501  ? 175 SER A OG   1 
ATOM   753  N N    . ILE A 1 176 ? 106.01000 89.66100  126.88900 1.000 35.52042  ? 176 ILE A N    1 
ATOM   754  C CA   . ILE A 1 176 ? 106.67900 90.82100  126.31000 1.000 35.41164  ? 176 ILE A CA   1 
ATOM   755  C C    . ILE A 1 176 ? 107.40100 90.45100  125.02300 1.000 35.73654  ? 176 ILE A C    1 
ATOM   756  O O    . ILE A 1 176 ? 107.42400 91.23700  124.06900 1.000 34.33468  ? 176 ILE A O    1 
ATOM   757  C CB   . ILE A 1 176 ? 107.64600 91.44700  127.33400 1.000 33.39318  ? 176 ILE A CB   1 
ATOM   758  C CG1  . ILE A 1 176 ? 106.88400 91.89000  128.58500 1.000 39.71440  ? 176 ILE A CG1  1 
ATOM   759  C CG2  . ILE A 1 176 ? 108.40600 92.60600  126.71300 1.000 35.28997  ? 176 ILE A CG2  1 
ATOM   760  C CD1  . ILE A 1 176 ? 107.61500 92.92400  129.41100 1.000 38.02357  ? 176 ILE A CD1  1 
ATOM   761  N N    . PHE A 1 177 ? 107.94600 89.23400  124.94500 1.000 34.52640  ? 177 PHE A N    1 
ATOM   762  C CA   . PHE A 1 177 ? 108.62800 88.81200  123.72500 1.000 29.67351  ? 177 PHE A CA   1 
ATOM   763  C C    . PHE A 1 177 ? 107.65100 88.67900  122.56400 1.000 31.11191  ? 177 PHE A C    1 
ATOM   764  O O    . PHE A 1 177 ? 107.93300 89.13900  121.45100 1.000 31.75322  ? 177 PHE A O    1 
ATOM   765  C CB   . PHE A 1 177 ? 109.35900 87.48900  123.97000 1.000 31.68885  ? 177 PHE A CB   1 
ATOM   766  C CG   . PHE A 1 177 ? 110.05000 86.93400  122.75200 1.000 34.34189  ? 177 PHE A CG   1 
ATOM   767  C CD1  . PHE A 1 177 ? 109.34500 86.21100  121.80300 1.000 33.54425  ? 177 PHE A CD1  1 
ATOM   768  C CD2  . PHE A 1 177 ? 111.40600 87.12900  122.56200 1.000 34.53913  ? 177 PHE A CD2  1 
ATOM   769  C CE1  . PHE A 1 177 ? 109.97600 85.70400  120.68700 1.000 29.87993  ? 177 PHE A CE1  1 
ATOM   770  C CE2  . PHE A 1 177 ? 112.04200 86.62200  121.44600 1.000 34.97381  ? 177 PHE A CE2  1 
ATOM   771  C CZ   . PHE A 1 177 ? 111.32600 85.90800  120.50800 1.000 33.07291  ? 177 PHE A CZ   1 
ATOM   772  N N    . CYS A 1 178 ? 106.48400 88.08200  122.80900 1.000 37.71497  ? 178 CYS A N    1 
ATOM   773  C CA   . CYS A 1 178 ? 105.52600 87.88300  121.72800 1.000 35.23044  ? 178 CYS A CA   1 
ATOM   774  C C    . CYS A 1 178 ? 104.88800 89.19600  121.30200 1.000 33.92106  ? 178 CYS A C    1 
ATOM   775  O O    . CYS A 1 178 ? 104.63800 89.40600  120.10700 1.000 37.64232  ? 178 CYS A O    1 
ATOM   776  C CB   . CYS A 1 178 ? 104.45200 86.88400  122.15400 1.000 36.26489  ? 178 CYS A CB   1 
ATOM   777  S SG   . CYS A 1 178 ? 105.09400 85.41000  122.97600 1.000 48.75637  ? 178 CYS A SG   1 
ATOM   778  N N    . ILE A 1 179 ? 104.67800 90.11900  122.24400 1.000 29.23134  ? 179 ILE A N    1 
ATOM   779  C CA   . ILE A 1 179 ? 104.13300 91.41400  121.85700 1.000 26.92567  ? 179 ILE A CA   1 
ATOM   780  C C    . ILE A 1 179 ? 105.16900 92.21800  121.08300 1.000 29.56377  ? 179 ILE A C    1 
ATOM   781  O O    . ILE A 1 179 ? 104.84000 92.88200  120.09400 1.000 35.64315  ? 179 ILE A O    1 
ATOM   782  C CB   . ILE A 1 179 ? 103.62800 92.17700  123.09400 1.000 32.69570  ? 179 ILE A CB   1 
ATOM   783  C CG1  . ILE A 1 179 ? 102.59000 91.33900  123.84200 1.000 34.35668  ? 179 ILE A CG1  1 
ATOM   784  C CG2  . ILE A 1 179 ? 103.04100 93.51700  122.68700 1.000 31.17900  ? 179 ILE A CG2  1 
ATOM   785  C CD1  . ILE A 1 179 ? 101.34700 91.04200  123.02900 1.000 32.05798  ? 179 ILE A CD1  1 
ATOM   786  N N    . GLY A 1 180 ? 106.44100 92.13700  121.48200 1.000 20.43357  ? 180 GLY A N    1 
ATOM   787  C CA   . GLY A 1 180 ? 107.47500 92.81500  120.72100 1.000 17.04668  ? 180 GLY A CA   1 
ATOM   788  C C    . GLY A 1 180 ? 107.60200 92.25900  119.31800 1.000 23.25954  ? 180 GLY A C    1 
ATOM   789  O O    . GLY A 1 180 ? 107.72800 93.01300  118.34700 1.000 28.06478  ? 180 GLY A O    1 
ATOM   790  N N    . PHE A 1 181 ? 107.48500 90.93600  119.18100 1.000 27.99306  ? 181 PHE A N    1 
ATOM   791  C CA   . PHE A 1 181 ? 107.60700 90.33500  117.86000 1.000 23.62383  ? 181 PHE A CA   1 
ATOM   792  C C    . PHE A 1 181 ? 106.43900 90.73500  116.97100 1.000 28.54687  ? 181 PHE A C    1 
ATOM   793  O O    . PHE A 1 181 ? 106.64100 91.10900  115.81000 1.000 32.22826  ? 181 PHE A O    1 
ATOM   794  C CB   . PHE A 1 181 ? 107.70200 88.81200  117.97100 1.000 23.84546  ? 181 PHE A CB   1 
ATOM   795  C CG   . PHE A 1 181 ? 107.72200 88.10800  116.64100 1.000 32.11921  ? 181 PHE A CG   1 
ATOM   796  C CD1  . PHE A 1 181 ? 106.54100 87.79200  115.98700 1.000 32.43284  ? 181 PHE A CD1  1 
ATOM   797  C CD2  . PHE A 1 181 ? 108.92100 87.77100  116.04000 1.000 31.83202  ? 181 PHE A CD2  1 
ATOM   798  C CE1  . PHE A 1 181 ? 106.55900 87.15400  114.76300 1.000 30.90543  ? 181 PHE A CE1  1 
ATOM   799  C CE2  . PHE A 1 181 ? 108.94400 87.13100  114.81600 1.000 29.84823  ? 181 PHE A CE2  1 
ATOM   800  C CZ   . PHE A 1 181 ? 107.76200 86.82200  114.17800 1.000 29.72880  ? 181 PHE A CZ   1 
ATOM   801  N N    . LEU A 1 182 ? 105.21200 90.69500  117.49700 1.000 26.24413  ? 182 LEU A N    1 
ATOM   802  C CA   . LEU A 1 182 ? 104.07800 91.00400  116.63300 1.000 25.92264  ? 182 LEU A CA   1 
ATOM   803  C C    . LEU A 1 182 ? 104.01900 92.49100  116.30800 1.000 28.80102  ? 182 LEU A C    1 
ATOM   804  O O    . LEU A 1 182 ? 103.67700 92.86300  115.17500 1.000 31.67274  ? 182 LEU A O    1 
ATOM   805  C CB   . LEU A 1 182 ? 102.77300 90.54700  117.28500 1.000 28.82442  ? 182 LEU A CB   1 
ATOM   806  C CG   . LEU A 1 182 ? 102.58300 89.03700  117.44500 1.000 28.76053  ? 182 LEU A CG   1 
ATOM   807  C CD1  . LEU A 1 182 ? 101.59700 88.73100  118.56100 1.000 27.12611  ? 182 LEU A CD1  1 
ATOM   808  C CD2  . LEU A 1 182 ? 102.12700 88.41200  116.13700 1.000 31.52697  ? 182 LEU A CD2  1 
ATOM   809  N N    . ALA A 1 183 ? 104.44000 93.35100  117.24300 1.000 28.96578  ? 183 ALA A N    1 
ATOM   810  C CA   . ALA A 1 183 ? 104.39800 94.78500  117.00300 1.000 22.30059  ? 183 ALA A CA   1 
ATOM   811  C C    . ALA A 1 183 ? 105.56500 95.25400  116.15200 1.000 32.04509  ? 183 ALA A C    1 
ATOM   812  O O    . ALA A 1 183 ? 105.51700 96.36700  115.61800 1.000 33.52012  ? 183 ALA A O    1 
ATOM   813  C CB   . ALA A 1 183 ? 104.38200 95.54500  118.33000 1.000 24.57756  ? 183 ALA A CB   1 
ATOM   814  N N    . THR A 1 184 ? 106.60600 94.43300  116.00900 1.000 31.63598  ? 184 THR A N    1 
ATOM   815  C CA   . THR A 1 184 ? 107.67800 94.76800  115.08800 1.000 25.96782  ? 184 THR A CA   1 
ATOM   816  C C    . THR A 1 184 ? 107.45900 94.13900  113.72300 1.000 28.41568  ? 184 THR A C    1 
ATOM   817  O O    . THR A 1 184 ? 108.00700 94.63300  112.73100 1.000 32.01088  ? 184 THR A O    1 
ATOM   818  C CB   . THR A 1 184 ? 109.02900 94.31800  115.64900 1.000 31.03509  ? 184 THR A CB   1 
ATOM   819  O OG1  . THR A 1 184 ? 109.14800 94.74600  117.01200 1.000 35.05352  ? 184 THR A OG1  1 
ATOM   820  C CG2  . THR A 1 184 ? 110.16700 94.91300  114.83800 1.000 26.86406  ? 184 THR A CG2  1 
ATOM   821  N N    . PHE A 1 185 ? 106.66500 93.06800  113.65200 1.000 32.42909  ? 185 PHE A N    1 
ATOM   822  C CA   . PHE A 1 185 ? 106.38500 92.40700  112.38800 1.000 30.52051  ? 185 PHE A CA   1 
ATOM   823  C C    . PHE A 1 185 ? 105.18900 93.00400  111.66300 1.000 34.90239  ? 185 PHE A C    1 
ATOM   824  O O    . PHE A 1 185 ? 105.08200 92.84500  110.44200 1.000 33.77048  ? 185 PHE A O    1 
ATOM   825  C CB   . PHE A 1 185 ? 106.14600 90.91100  112.60600 1.000 30.79124  ? 185 PHE A CB   1 
ATOM   826  C CG   . PHE A 1 185 ? 106.10900 90.11600  111.33400 1.000 32.32066  ? 185 PHE A CG   1 
ATOM   827  C CD1  . PHE A 1 185 ? 107.28100 89.72600  110.71200 1.000 32.16984  ? 185 PHE A CD1  1 
ATOM   828  C CD2  . PHE A 1 185 ? 104.90200 89.76600  110.75700 1.000 32.70066  ? 185 PHE A CD2  1 
ATOM   829  C CE1  . PHE A 1 185 ? 107.24900 88.99800  109.54100 1.000 31.55143  ? 185 PHE A CE1  1 
ATOM   830  C CE2  . PHE A 1 185 ? 104.86500 89.03900  109.58600 1.000 34.30705  ? 185 PHE A CE2  1 
ATOM   831  C CZ   . PHE A 1 185 ? 106.03900 88.65400  108.97700 1.000 33.04503  ? 185 PHE A CZ   1 
ATOM   832  N N    . MET A 1 186 ? 104.29200 93.68800  112.37500 1.000 43.64415  ? 186 MET A N    1 
ATOM   833  C CA   . MET A 1 186 ? 103.13000 94.27200  111.72100 1.000 36.38316  ? 186 MET A CA   1 
ATOM   834  C C    . MET A 1 186 ? 103.36800 95.70900  111.28000 1.000 36.10980  ? 186 MET A C    1 
ATOM   835  O O    . MET A 1 186 ? 102.53600 96.26500  110.55500 1.000 39.17725  ? 186 MET A O    1 
ATOM   836  C CB   . MET A 1 186 ? 101.91300 94.21500  112.64900 1.000 33.47416  ? 186 MET A CB   1 
ATOM   837  C CG   . MET A 1 186 ? 101.00000 93.02700  112.39900 1.000 36.72844  ? 186 MET A CG   1 
ATOM   838  S SD   . MET A 1 186 ? 99.41700  93.18400  113.24500 1.000 52.80192  ? 186 MET A SD   1 
ATOM   839  C CE   . MET A 1 186 ? 99.37000  91.64800  114.16300 1.000 41.69993  ? 186 MET A CE   1 
ATOM   840  N N    . LYS A 1 187 ? 104.47600 96.31500  111.69700 1.000 37.20248  ? 187 LYS A N    1 
ATOM   841  C CA   . LYS A 1 187 ? 104.86600 97.64600  111.25500 1.000 38.11926  ? 187 LYS A CA   1 
ATOM   842  C C    . LYS A 1 187 ? 105.66500 97.62500  109.95600 1.000 35.40883  ? 187 LYS A C    1 
ATOM   843  O O    . LYS A 1 187 ? 105.93500 98.69100  109.39300 1.000 34.90473  ? 187 LYS A O    1 
ATOM   844  C CB   . LYS A 1 187 ? 105.67500 98.34200  112.35900 1.000 36.31299  ? 187 LYS A CB   1 
ATOM   845  C CG   . LYS A 1 187 ? 106.33600 99.64300  111.94400 1.000 36.72690  ? 187 LYS A CG   1 
ATOM   846  C CD   . LYS A 1 187 ? 107.67900 99.83300  112.62900 1.000 38.83871  ? 187 LYS A CD   1 
ATOM   847  C CE   . LYS A 1 187 ? 108.49600 98.55300  112.62300 1.000 41.60934  ? 187 LYS A CE   1 
ATOM   848  N NZ   . LYS A 1 187 ? 109.56000 98.57700  113.66200 1.000 41.61301  ? 187 LYS A NZ   1 
ATOM   849  N N    . LEU A 1 188 ? 106.02600 96.44300  109.46000 1.000 37.28013  ? 188 LEU A N    1 
ATOM   850  C CA   . LEU A 1 188 ? 106.86000 96.29200  108.27600 1.000 38.60466  ? 188 LEU A CA   1 
ATOM   851  C C    . LEU A 1 188 ? 106.06600 95.89000  107.04000 1.000 38.09734  ? 188 LEU A C    1 
ATOM   852  O O    . LEU A 1 188 ? 106.66200 95.47900  106.04000 1.000 38.85488  ? 188 LEU A O    1 
ATOM   853  C CB   . LEU A 1 188 ? 107.96700 95.26700  108.53300 1.000 38.14708  ? 188 LEU A CB   1 
ATOM   854  C CG   . LEU A 1 188 ? 108.91800 95.52900  109.70000 1.000 36.90455  ? 188 LEU A CG   1 
ATOM   855  C CD1  . LEU A 1 188 ? 109.63700 94.25000  110.09300 1.000 35.67966  ? 188 LEU A CD1  1 
ATOM   856  C CD2  . LEU A 1 188 ? 109.91600 96.61600  109.34100 1.000 36.97846  ? 188 LEU A CD2  1 
ATOM   857  N N    . TYR A 1 189 ? 104.74900 95.99400  107.08500 1.000 50.78299  ? 189 TYR A N    1 
ATOM   858  C CA   . TYR A 1 189 ? 103.93000 95.64300  105.93100 1.000 47.22982  ? 189 TYR A CA   1 
ATOM   859  C C    . TYR A 1 189 ? 103.78900 96.85000  105.01200 1.000 51.32038  ? 189 TYR A C    1 
ATOM   860  O O    . TYR A 1 189 ? 103.51900 97.95600  105.49300 1.000 53.70691  ? 189 TYR A O    1 
ATOM   861  C CB   . TYR A 1 189 ? 102.55500 95.17000  106.38000 1.000 46.99081  ? 189 TYR A CB   1 
ATOM   862  C CG   . TYR A 1 189 ? 102.01700 93.99500  105.60000 1.000 52.08490  ? 189 TYR A CG   1 
ATOM   863  C CD1  . TYR A 1 189 ? 101.71200 94.11000  104.25100 1.000 52.18397  ? 189 TYR A CD1  1 
ATOM   864  C CD2  . TYR A 1 189 ? 101.81800 92.76500  106.21300 1.000 52.38770  ? 189 TYR A CD2  1 
ATOM   865  C CE1  . TYR A 1 189 ? 101.22100 93.03600  103.53500 1.000 52.59130  ? 189 TYR A CE1  1 
ATOM   866  C CE2  . TYR A 1 189 ? 101.32700 91.68600  105.50600 1.000 52.70713  ? 189 TYR A CE2  1 
ATOM   867  C CZ   . TYR A 1 189 ? 101.03000 91.82600  104.16700 1.000 54.96048  ? 189 TYR A CZ   1 
ATOM   868  O OH   . TYR A 1 189 ? 100.54200 90.75300  103.45800 1.000 54.12512  ? 189 TYR A OH   1 
ATOM   869  N N    . PRO A 1 190 ? 103.96100 96.68100  103.69800 1.000 51.13791  ? 190 PRO A N    1 
ATOM   870  C CA   . PRO A 1 190 ? 103.95600 97.85200  102.80500 1.000 49.67372  ? 190 PRO A CA   1 
ATOM   871  C C    . PRO A 1 190 ? 102.69200 98.68700  102.89300 1.000 48.14393  ? 190 PRO A C    1 
ATOM   872  O O    . PRO A 1 190 ? 102.74500 99.89700  102.64000 1.000 47.83043  ? 190 PRO A O    1 
ATOM   873  C CB   . PRO A 1 190 ? 104.12500 97.22500  101.41400 1.000 51.51212  ? 190 PRO A CB   1 
ATOM   874  C CG   . PRO A 1 190 ? 104.82300 95.93200  101.67300 1.000 51.07633  ? 190 PRO A CG   1 
ATOM   875  C CD   . PRO A 1 190 ? 104.26500 95.43600  102.97300 1.000 51.01740  ? 190 PRO A CD   1 
ATOM   876  N N    . SER A 1 191 ? 101.55500 98.08300  103.24000 1.000 50.17734  ? 191 SER A N    1 
ATOM   877  C CA   . SER A 1 191 ? 100.32600 98.85500  103.37600 1.000 49.48375  ? 191 SER A CA   1 
ATOM   878  C C    . SER A 1 191 ? 100.30000 99.64900  104.67500 1.000 50.38336  ? 191 SER A C    1 
ATOM   879  O O    . SER A 1 191 ? 99.63200  100.68600 104.75100 1.000 51.63400  ? 191 SER A O    1 
ATOM   880  C CB   . SER A 1 191 ? 99.11000  97.93100  103.29700 1.000 50.59002  ? 191 SER A CB   1 
ATOM   881  O OG   . SER A 1 191 ? 99.09000  97.01600  104.37700 1.000 52.43304  ? 191 SER A OG   1 
ATOM   882  N N    . MET A 1 192 ? 101.01400 99.18200  105.69700 1.000 49.70630  ? 192 MET A N    1 
ATOM   883  C CA   . MET A 1 192 ? 101.06500 99.82600  107.00700 1.000 47.89585  ? 192 MET A CA   1 
ATOM   884  C C    . MET A 1 192 ? 102.37700 100.56800 107.22500 1.000 49.24719  ? 192 MET A C    1 
ATOM   885  O O    . MET A 1 192 ? 102.94000 100.53700 108.32200 1.000 51.69417  ? 192 MET A O    1 
ATOM   886  C CB   . MET A 1 192 ? 100.84300 98.79600  108.11000 1.000 46.88910  ? 192 MET A CB   1 
ATOM   887  C CG   . MET A 1 192 ? 99.53300  98.95900  108.86000 1.000 48.79241  ? 192 MET A CG   1 
ATOM   888  S SD   . MET A 1 192 ? 98.16300  98.08900  108.07800 1.000 56.52163  ? 192 MET A SD   1 
ATOM   889  C CE   . MET A 1 192 ? 98.54700  96.39700  108.51900 1.000 50.42669  ? 192 MET A CE   1 
ATOM   890  N N    . LYS A 1 193 ? 102.88700 101.24800 106.19800 1.000 48.47383  ? 193 LYS A N    1 
ATOM   891  C CA   . LYS A 1 193 ? 104.17200 101.93000 106.27400 1.000 49.43550  ? 193 LYS A CA   1 
ATOM   892  C C    . LYS A 1 193 ? 104.02300 103.42900 106.49700 1.000 48.98954  ? 193 LYS A C    1 
ATOM   893  O O    . LYS A 1 193 ? 104.98100 104.18100 106.28600 1.000 50.09160  ? 193 LYS A O    1 
ATOM   894  C CB   . LYS A 1 193 ? 104.99100 101.66700 105.01000 1.000 49.57637  ? 193 LYS A CB   1 
ATOM   895  C CG   . LYS A 1 193 ? 105.14800 100.20000 104.65900 1.000 48.94711  ? 193 LYS A CG   1 
ATOM   896  C CD   . LYS A 1 193 ? 106.16400 99.52500  105.56400 1.000 48.30006  ? 193 LYS A CD   1 
ATOM   897  C CE   . LYS A 1 193 ? 106.83200 98.35200  104.86400 1.000 50.56699  ? 193 LYS A CE   1 
ATOM   898  N NZ   . LYS A 1 193 ? 108.18500 98.06800  105.41500 1.000 50.51444  ? 193 LYS A NZ   1 
ATOM   899  N N    . ALA A 1 194 ? 102.84400 103.87800 106.91300 1.000 50.12199  ? 194 ALA A N    1 
ATOM   900  C CA   . ALA A 1 194 ? 102.62200 105.26400 107.30200 1.000 50.28060  ? 194 ALA A CA   1 
ATOM   901  C C    . ALA A 1 194 ? 102.36300 105.43200 108.78900 1.000 50.49956  ? 194 ALA A C    1 
ATOM   902  O O    . ALA A 1 194 ? 102.81400 106.41300 109.38200 1.000 57.38732  ? 194 ALA A O    1 
ATOM   903  C CB   . ALA A 1 194 ? 101.44500 105.85400 106.51700 1.000 49.49626  ? 194 ALA A CB   1 
ATOM   904  N N    . TYR A 1 195 ? 101.64900 104.49500 109.40300 1.000 43.41588  ? 195 TYR A N    1 
ATOM   905  C CA   . TYR A 1 195 ? 101.23000 104.59400 110.80200 1.000 43.59879  ? 195 TYR A CA   1 
ATOM   906  C C    . TYR A 1 195 ? 102.18600 103.87300 111.74500 1.000 42.94515  ? 195 TYR A C    1 
ATOM   907  O O    . TYR A 1 195 ? 101.76400 103.07900 112.58300 1.000 46.69835  ? 195 TYR A O    1 
ATOM   908  C CB   . TYR A 1 195 ? 99.80600  104.06900 110.96000 1.000 40.82513  ? 195 TYR A CB   1 
ATOM   909  C CG   . TYR A 1 195 ? 98.90600  104.33300 109.76900 1.000 46.05191  ? 195 TYR A CG   1 
ATOM   910  C CD1  . TYR A 1 195 ? 98.99800  105.51900 109.04800 1.000 47.28160  ? 195 TYR A CD1  1 
ATOM   911  C CD2  . TYR A 1 195 ? 97.97100  103.39200 109.36100 1.000 45.23627  ? 195 TYR A CD2  1 
ATOM   912  C CE1  . TYR A 1 195 ? 98.18500  105.76100 107.96100 1.000 45.97953  ? 195 TYR A CE1  1 
ATOM   913  C CE2  . TYR A 1 195 ? 97.15200  103.62600 108.27200 1.000 47.13425  ? 195 TYR A CE2  1 
ATOM   914  C CZ   . TYR A 1 195 ? 97.26400  104.81200 107.57700 1.000 48.19035  ? 195 TYR A CZ   1 
ATOM   915  O OH   . TYR A 1 195 ? 96.45200  105.05300 106.49300 1.000 48.44806  ? 195 TYR A OH   1 
ATOM   916  N N    . GLU A 1 196 ? 103.49000 104.13700 111.62800 1.000 38.01513  ? 196 GLU A N    1 
ATOM   917  C CA   . GLU A 1 196 ? 104.44500 103.54000 112.55500 1.000 41.44573  ? 196 GLU A CA   1 
ATOM   918  C C    . GLU A 1 196 ? 104.32600 104.13500 113.95100 1.000 42.51731  ? 196 GLU A C    1 
ATOM   919  O O    . GLU A 1 196 ? 104.75000 103.50300 114.93000 1.000 44.39129  ? 196 GLU A O    1 
ATOM   920  C CB   . GLU A 1 196 ? 105.87100 103.72300 112.03400 1.000 39.14209  ? 196 GLU A CB   1 
ATOM   921  C CG   . GLU A 1 196 ? 106.28200 102.71900 110.97500 1.000 43.40995  ? 196 GLU A CG   1 
ATOM   922  C CD   . GLU A 1 196 ? 105.74600 103.06600 109.60300 1.000 47.17475  ? 196 GLU A CD   1 
ATOM   923  O OE1  . GLU A 1 196 ? 105.53500 102.13700 108.79600 1.000 45.48121  ? 196 GLU A OE1  1 
ATOM   924  O OE2  . GLU A 1 196 ? 105.53400 104.26600 109.33200 1.000 47.10204  ? 196 GLU A OE2  1 
ATOM   925  N N    . TYR A 1 197 ? 103.70700 105.30700 114.06600 1.000 29.43533  ? 197 TYR A N    1 
ATOM   926  C CA   . TYR A 1 197 ? 103.58000 106.00800 115.33300 1.000 30.11448  ? 197 TYR A CA   1 
ATOM   927  C C    . TYR A 1 197 ? 102.37300 105.54800 116.13400 1.000 32.85263  ? 197 TYR A C    1 
ATOM   928  O O    . TYR A 1 197 ? 102.22600 105.95600 117.29000 1.000 40.11605  ? 197 TYR A O    1 
ATOM   929  C CB   . TYR A 1 197 ? 103.48800 107.51900 115.08900 1.000 31.34328  ? 197 TYR A CB   1 
ATOM   930  C CG   . TYR A 1 197 ? 102.30900 107.91900 114.23200 1.000 30.54054  ? 197 TYR A CG   1 
ATOM   931  C CD1  . TYR A 1 197 ? 102.34200 107.75300 112.85300 1.000 27.56248  ? 197 TYR A CD1  1 
ATOM   932  C CD2  . TYR A 1 197 ? 101.15800 108.44500 114.80000 1.000 26.69576  ? 197 TYR A CD2  1 
ATOM   933  C CE1  . TYR A 1 197 ? 101.26600 108.10600 112.06600 1.000 28.45732  ? 197 TYR A CE1  1 
ATOM   934  C CE2  . TYR A 1 197 ? 100.07800 108.80100 114.01900 1.000 28.83403  ? 197 TYR A CE2  1 
ATOM   935  C CZ   . TYR A 1 197 ? 100.13800 108.62900 112.65300 1.000 30.59062  ? 197 TYR A CZ   1 
ATOM   936  O OH   . TYR A 1 197 ? 99.06600  108.98300 111.86800 1.000 35.54530  ? 197 TYR A OH   1 
ATOM   937  N N    . GLY A 1 198 ? 101.51000 104.72100 115.55300 1.000 24.98109  ? 198 GLY A N    1 
ATOM   938  C CA   . GLY A 1 198 ? 100.42900 104.12500 116.30800 1.000 25.54214  ? 198 GLY A CA   1 
ATOM   939  C C    . GLY A 1 198 ? 100.86000 102.78000 116.84900 1.000 29.18606  ? 198 GLY A C    1 
ATOM   940  O O    . GLY A 1 198 ? 100.24300 102.24100 117.77200 1.000 37.88667  ? 198 GLY A O    1 
ATOM   941  N N    . PHE A 1 199 ? 101.92800 102.22800 116.27100 1.000 26.62720  ? 199 PHE A N    1 
ATOM   942  C CA   . PHE A 1 199 ? 102.51100 100.97400 116.73100 1.000 23.69277  ? 199 PHE A CA   1 
ATOM   943  C C    . PHE A 1 199 ? 103.59600 101.20200 117.77700 1.000 25.52377  ? 199 PHE A C    1 
ATOM   944  O O    . PHE A 1 199 ? 103.70700 100.43100 118.74100 1.000 30.69676  ? 199 PHE A O    1 
ATOM   945  C CB   . PHE A 1 199 ? 103.09100 100.19900 115.54500 1.000 24.93715  ? 199 PHE A CB   1 
ATOM   946  C CG   . PHE A 1 199 ? 102.05900 99.48100  114.72500 1.000 26.88586  ? 199 PHE A CG   1 
ATOM   947  C CD1  . PHE A 1 199 ? 101.37300 98.39700  115.24300 1.000 30.73172  ? 199 PHE A CD1  1 
ATOM   948  C CD2  . PHE A 1 199 ? 101.77700 99.89000  113.43400 1.000 28.18869  ? 199 PHE A CD2  1 
ATOM   949  C CE1  . PHE A 1 199 ? 100.42400 97.73700  114.48900 1.000 28.38406  ? 199 PHE A CE1  1 
ATOM   950  C CE2  . PHE A 1 199 ? 100.82900 99.23400  112.67700 1.000 25.89799  ? 199 PHE A CE2  1 
ATOM   951  C CZ   . PHE A 1 199 ? 100.15200 98.15600  113.20400 1.000 24.88882  ? 199 PHE A CZ   1 
ATOM   952  N N    . ARG A 1 200 ? 104.38400 102.26900 117.61700 1.000 25.92923  ? 200 ARG A N    1 
ATOM   953  C CA   . ARG A 1 200 ? 105.41700 102.55900 118.60500 1.000 24.57323  ? 200 ARG A CA   1 
ATOM   954  C C    . ARG A 1 200 ? 104.80400 102.90400 119.95800 1.000 30.88542  ? 200 ARG A C    1 
ATOM   955  O O    . ARG A 1 200 ? 105.30200 102.46300 121.00200 1.000 35.04100  ? 200 ARG A O    1 
ATOM   956  C CB   . ARG A 1 200 ? 106.31000 103.69400 118.10600 1.000 27.69602  ? 200 ARG A CB   1 
ATOM   957  C CG   . ARG A 1 200 ? 107.05700 104.42700 119.20200 1.000 32.58800  ? 200 ARG A CG   1 
ATOM   958  C CD   . ARG A 1 200 ? 108.34700 105.03100 118.67600 1.000 30.95583  ? 200 ARG A CD   1 
ATOM   959  N NE   . ARG A 1 200 ? 108.96000 104.19800 117.64900 1.000 35.43661  ? 200 ARG A NE   1 
ATOM   960  C CZ   . ARG A 1 200 ? 109.63100 104.66800 116.60600 1.000 36.74145  ? 200 ARG A CZ   1 
ATOM   961  N NH1  . ARG A 1 200 ? 109.80300 105.96700 116.42300 1.000 34.29623  ? 200 ARG A NH1  1 
ATOM   962  N NH2  . ARG A 1 200 ? 110.14500 103.81300 115.72600 1.000 35.06805  ? 200 ARG A NH2  1 
ATOM   963  N N    . VAL A 1 201 ? 103.70100 103.65600 119.95900 1.000 25.77554  ? 201 VAL A N    1 
ATOM   964  C CA   . VAL A 1 201 ? 103.05700 104.01200 121.21900 1.000 29.07047  ? 201 VAL A CA   1 
ATOM   965  C C    . VAL A 1 201 ? 102.42000 102.78200 121.85000 1.000 23.70566  ? 201 VAL A C    1 
ATOM   966  O O    . VAL A 1 201 ? 102.44600 102.61200 123.07400 1.000 27.60354  ? 201 VAL A O    1 
ATOM   967  C CB   . VAL A 1 201 ? 102.02600 105.13600 121.00600 1.000 24.84974  ? 201 VAL A CB   1 
ATOM   968  C CG1  . VAL A 1 201 ? 102.71500 106.48800 120.96000 1.000 27.43005  ? 201 VAL A CG1  1 
ATOM   969  C CG2  . VAL A 1 201 ? 101.22300 104.89400 119.74200 1.000 28.45412  ? 201 VAL A CG2  1 
ATOM   970  N N    . PHE A 1 202 ? 101.86900 101.89000 121.02500 1.000 15.99799  ? 202 PHE A N    1 
ATOM   971  C CA   . PHE A 1 202 ? 101.29800 100.65300 121.54500 1.000 24.47119  ? 202 PHE A CA   1 
ATOM   972  C C    . PHE A 1 202 ? 102.36300 99.82700  122.25400 1.000 27.89594  ? 202 PHE A C    1 
ATOM   973  O O    . PHE A 1 202 ? 102.15600 99.35400  123.37900 1.000 30.52375  ? 202 PHE A O    1 
ATOM   974  C CB   . PHE A 1 202 ? 100.65600 99.86400  120.39900 1.000 24.99106  ? 202 PHE A CB   1 
ATOM   975  C CG   . PHE A 1 202 ? 100.06400 98.54300  120.81100 1.000 21.64546  ? 202 PHE A CG   1 
ATOM   976  C CD1  . PHE A 1 202 ? 100.87100 97.44700  121.06500 1.000 28.17659  ? 202 PHE A CD1  1 
ATOM   977  C CD2  . PHE A 1 202 ? 98.69400  98.39400  120.92900 1.000 27.31800  ? 202 PHE A CD2  1 
ATOM   978  C CE1  . PHE A 1 202 ? 100.32500 96.23400  121.43800 1.000 27.59939  ? 202 PHE A CE1  1 
ATOM   979  C CE2  . PHE A 1 202 ? 98.14200  97.18300  121.30200 1.000 30.49985  ? 202 PHE A CE2  1 
ATOM   980  C CZ   . PHE A 1 202 ? 98.95900  96.10300  121.55600 1.000 25.90832  ? 202 PHE A CZ   1 
ATOM   981  N N    . LEU A 1 203 ? 103.51800 99.64700  121.60800 1.000 28.99708  ? 203 LEU A N    1 
ATOM   982  C CA   . LEU A 1 203 ? 104.57800 98.84600  122.21300 1.000 24.58387  ? 203 LEU A CA   1 
ATOM   983  C C    . LEU A 1 203 ? 105.09100 99.49900  123.49300 1.000 26.21160  ? 203 LEU A C    1 
ATOM   984  O O    . LEU A 1 203 ? 105.23100 98.83700  124.53300 1.000 29.70413  ? 203 LEU A O    1 
ATOM   985  C CB   . LEU A 1 203 ? 105.71700 98.64500  121.21400 1.000 27.13955  ? 203 LEU A CB   1 
ATOM   986  C CG   . LEU A 1 203 ? 106.65900 97.46500  121.46700 1.000 28.43100  ? 203 LEU A CG   1 
ATOM   987  C CD1  . LEU A 1 203 ? 105.87600 96.22600  121.86400 1.000 28.27376  ? 203 LEU A CD1  1 
ATOM   988  C CD2  . LEU A 1 203 ? 107.51700 97.18900  120.24500 1.000 23.80932  ? 203 LEU A CD2  1 
ATOM   989  N N    . LEU A 1 204 ? 105.34200 100.81200 123.44500 1.000 28.61937  ? 204 LEU A N    1 
ATOM   990  C CA   . LEU A 1 204 ? 105.85500 101.50300 124.62200 1.000 24.29545  ? 204 LEU A CA   1 
ATOM   991  C C    . LEU A 1 204 ? 104.87100 101.42300 125.78100 1.000 27.30247  ? 204 LEU A C    1 
ATOM   992  O O    . LEU A 1 204 ? 105.28100 101.31600 126.94200 1.000 34.15736  ? 204 LEU A O    1 
ATOM   993  C CB   . LEU A 1 204 ? 106.16800 102.95900 124.28300 1.000 24.70353  ? 204 LEU A CB   1 
ATOM   994  C CG   . LEU A 1 204 ? 107.45100 103.19300 123.48600 1.000 29.95046  ? 204 LEU A CG   1 
ATOM   995  C CD1  . LEU A 1 204 ? 107.45900 104.58700 122.88100 1.000 33.62609  ? 204 LEU A CD1  1 
ATOM   996  C CD2  . LEU A 1 204 ? 108.67500 102.97400 124.35700 1.000 31.46913  ? 204 LEU A CD2  1 
ATOM   997  N N    . THR A 1 205 ? 103.56900 101.47600 125.49400 1.000 29.32757  ? 205 THR A N    1 
ATOM   998  C CA   . THR A 1 205 ? 102.59300 101.45400 126.57500 1.000 30.91092  ? 205 THR A CA   1 
ATOM   999  C C    . THR A 1 205 ? 102.48800 100.05400 127.16300 1.000 30.63017  ? 205 THR A C    1 
ATOM   1000 O O    . THR A 1 205 ? 102.48500 99.88100  128.38700 1.000 31.77268  ? 205 THR A O    1 
ATOM   1001 C CB   . THR A 1 205 ? 101.23200 101.93700 126.07200 1.000 27.48899  ? 205 THR A CB   1 
ATOM   1002 O OG1  . THR A 1 205 ? 101.34300 103.28900 125.61200 1.000 28.25024  ? 205 THR A OG1  1 
ATOM   1003 C CG2  . THR A 1 205 ? 100.20100 101.87600 127.18500 1.000 28.77496  ? 205 THR A CG2  1 
ATOM   1004 N N    . TYR A 1 206 ? 102.38900 99.03800  126.30100 1.000 36.40481  ? 206 TYR A N    1 
ATOM   1005 C CA   . TYR A 1 206 ? 102.24300 97.67500  126.79700 1.000 30.42735  ? 206 TYR A CA   1 
ATOM   1006 C C    . TYR A 1 206 ? 103.43700 97.27500  127.65100 1.000 36.58099  ? 206 TYR A C    1 
ATOM   1007 O O    . TYR A 1 206 ? 103.27900 96.62300  128.69000 1.000 37.64120  ? 206 TYR A O    1 
ATOM   1008 C CB   . TYR A 1 206 ? 102.06500 96.69600  125.63900 1.000 30.43833  ? 206 TYR A CB   1 
ATOM   1009 C CG   . TYR A 1 206 ? 101.92100 95.26000  126.09200 1.000 39.37444  ? 206 TYR A CG   1 
ATOM   1010 C CD1  . TYR A 1 206 ? 100.67100 94.72400  126.37000 1.000 34.48327  ? 206 TYR A CD1  1 
ATOM   1011 C CD2  . TYR A 1 206 ? 103.03300 94.44100  126.24700 1.000 38.84828  ? 206 TYR A CD2  1 
ATOM   1012 C CE1  . TYR A 1 206 ? 100.53200 93.41500  126.78600 1.000 37.51548  ? 206 TYR A CE1  1 
ATOM   1013 C CE2  . TYR A 1 206 ? 102.90300 93.13100  126.66400 1.000 33.05989  ? 206 TYR A CE2  1 
ATOM   1014 C CZ   . TYR A 1 206 ? 101.65000 92.62300  126.93200 1.000 37.18781  ? 206 TYR A CZ   1 
ATOM   1015 O OH   . TYR A 1 206 ? 101.51200 91.32000  127.34600 1.000 37.03492  ? 206 TYR A OH   1 
ATOM   1016 N N    . CYS A 1 207 ? 104.64500 97.65600  127.22700 1.000 42.23603  ? 207 CYS A N    1 
ATOM   1017 C CA   . CYS A 1 207 ? 105.84700 97.26700  127.96300 1.000 33.79606  ? 207 CYS A CA   1 
ATOM   1018 C C    . CYS A 1 207 ? 105.97800 98.01100  129.28900 1.000 34.70096  ? 207 CYS A C    1 
ATOM   1019 O O    . CYS A 1 207 ? 106.44700 97.44000  130.27900 1.000 40.89166  ? 207 CYS A O    1 
ATOM   1020 C CB   . CYS A 1 207 ? 107.08600 97.49100  127.09700 1.000 33.46014  ? 207 CYS A CB   1 
ATOM   1021 S SG   . CYS A 1 207 ? 107.30800 96.26100  125.79500 1.000 45.33052  ? 207 CYS A SG   1 
ATOM   1022 N N    . TYR A 1 208 ? 105.57000 99.27900  129.33200 1.000 36.15691  ? 208 TYR A N    1 
ATOM   1023 C CA   . TYR A 1 208 ? 105.65700 100.07600 130.55200 1.000 33.30175  ? 208 TYR A CA   1 
ATOM   1024 C C    . TYR A 1 208 ? 104.68200 99.65100  131.64700 1.000 37.15352  ? 208 TYR A C    1 
ATOM   1025 O O    . TYR A 1 208 ? 104.87600 100.04900 132.80000 1.000 38.37765  ? 208 TYR A O    1 
ATOM   1026 C CB   . TYR A 1 208 ? 105.45200 101.56200 130.21000 1.000 35.28785  ? 208 TYR A CB   1 
ATOM   1027 C CG   . TYR A 1 208 ? 104.89300 102.42600 131.33000 1.000 38.07997  ? 208 TYR A CG   1 
ATOM   1028 C CD1  . TYR A 1 208 ? 103.55400 102.35200 131.70600 1.000 37.63943  ? 208 TYR A CD1  1 
ATOM   1029 C CD2  . TYR A 1 208 ? 105.71400 103.30200 132.02500 1.000 39.51124  ? 208 TYR A CD2  1 
ATOM   1030 C CE1  . TYR A 1 208 ? 103.05500 103.12700 132.73300 1.000 34.89811  ? 208 TYR A CE1  1 
ATOM   1031 C CE2  . TYR A 1 208 ? 105.22100 104.08300 133.05000 1.000 36.49134  ? 208 TYR A CE2  1 
ATOM   1032 C CZ   . TYR A 1 208 ? 103.89200 103.99200 133.39900 1.000 33.95685  ? 208 TYR A CZ   1 
ATOM   1033 O OH   . TYR A 1 208 ? 103.39700 104.76900 134.42100 1.000 36.40274  ? 208 TYR A OH   1 
ATOM   1034 N N    . ILE A 1 209 ? 103.67000 98.83400  131.35100 1.000 40.42840  ? 209 ILE A N    1 
ATOM   1035 C CA   . ILE A 1 209 ? 102.67900 98.49400  132.36700 1.000 39.45267  ? 209 ILE A CA   1 
ATOM   1036 C C    . ILE A 1 209 ? 102.87600 97.09600  132.94200 1.000 42.02061  ? 209 ILE A C    1 
ATOM   1037 O O    . ILE A 1 209 ? 102.14800 96.70600  133.86600 1.000 38.98518  ? 209 ILE A O    1 
ATOM   1038 C CB   . ILE A 1 209 ? 101.25500 98.66900  131.79400 1.000 41.37799  ? 209 ILE A CB   1 
ATOM   1039 C CG1  . ILE A 1 209 ? 100.62900 99.96700  132.30900 1.000 38.52095  ? 209 ILE A CG1  1 
ATOM   1040 C CG2  . ILE A 1 209 ? 100.36800 97.47600  132.10600 1.000 39.79414  ? 209 ILE A CG2  1 
ATOM   1041 C CD1  . ILE A 1 209 ? 99.37800  100.37600 131.56800 1.000 38.14564  ? 209 ILE A CD1  1 
ATOM   1042 N N    . LEU A 1 210 ? 103.87800 96.35400  132.47300 1.000 43.23293  ? 210 LEU A N    1 
ATOM   1043 C CA   . LEU A 1 210 ? 104.15200 95.02100  132.98700 1.000 36.05829  ? 210 LEU A CA   1 
ATOM   1044 C C    . LEU A 1 210 ? 105.47100 94.93300  133.73900 1.000 40.01427  ? 210 LEU A C    1 
ATOM   1045 O O    . LEU A 1 210 ? 105.71300 93.92700  134.41300 1.000 44.62201  ? 210 LEU A O    1 
ATOM   1046 C CB   . LEU A 1 210 ? 104.15600 93.98700  131.85200 1.000 33.08092  ? 210 LEU A CB   1 
ATOM   1047 C CG   . LEU A 1 210 ? 102.84100 93.73700  131.11800 1.000 41.32223  ? 210 LEU A CG   1 
ATOM   1048 C CD1  . LEU A 1 210 ? 103.07100 92.80200  129.94500 1.000 43.79588  ? 210 LEU A CD1  1 
ATOM   1049 C CD2  . LEU A 1 210 ? 101.80100 93.16600  132.06500 1.000 39.01104  ? 210 LEU A CD2  1 
ATOM   1050 N N    . ILE A 1 211 ? 106.32300 95.95200  133.64700 1.000 40.13562  ? 211 ILE A N    1 
ATOM   1051 C CA   . ILE A 1 211 ? 107.60700 95.95200  134.33600 1.000 41.62037  ? 211 ILE A CA   1 
ATOM   1052 C C    . ILE A 1 211 ? 107.70300 97.15500  135.26500 1.000 43.64530  ? 211 ILE A C    1 
ATOM   1053 O O    . ILE A 1 211 ? 108.80400 97.62200  135.57700 1.000 48.48287  ? 211 ILE A O    1 
ATOM   1054 C CB   . ILE A 1 211 ? 108.77500 95.93600  133.33400 1.000 41.41007  ? 211 ILE A CB   1 
ATOM   1055 C CG1  . ILE A 1 211 ? 108.98200 97.32100  132.72400 1.000 40.24045  ? 211 ILE A CG1  1 
ATOM   1056 C CG2  . ILE A 1 211 ? 108.52300 94.91300  132.23800 1.000 42.14147  ? 211 ILE A CG2  1 
ATOM   1057 C CD1  . ILE A 1 211 ? 110.33800 97.49900  132.08500 1.000 42.70973  ? 211 ILE A CD1  1 
ATOM   1058 N N    . SER A 1 212 ? 106.55700 97.66800  135.71600 1.000 45.89521  ? 212 SER A N    1 
ATOM   1059 C CA   . SER A 1 212 ? 106.53600 98.85800  136.55800 1.000 45.02235  ? 212 SER A CA   1 
ATOM   1060 C C    . SER A 1 212 ? 105.84000 98.62900  137.89500 1.000 46.74858  ? 212 SER A C    1 
ATOM   1061 O O    . SER A 1 212 ? 105.59000 99.59700  138.62300 1.000 49.44423  ? 212 SER A O    1 
ATOM   1062 C CB   . SER A 1 212 ? 105.86500 100.01800 135.81500 1.000 45.40211  ? 212 SER A CB   1 
ATOM   1063 O OG   . SER A 1 212 ? 106.39600 101.26600 136.22300 1.000 47.21523  ? 212 SER A OG   1 
ATOM   1064 N N    . GLY A 1 213 ? 105.52000 97.38400  138.23800 1.000 63.92872  ? 213 GLY A N    1 
ATOM   1065 C CA   . GLY A 1 213 ? 104.92400 97.08500  139.52600 1.000 63.37756  ? 213 GLY A CA   1 
ATOM   1066 C C    . GLY A 1 213 ? 103.41600 97.21000  139.54800 1.000 64.12277  ? 213 GLY A C    1 
ATOM   1067 O O    . GLY A 1 213 ? 102.86300 97.93100  140.38300 1.000 66.14570  ? 213 GLY A O    1 
ATOM   1068 N N    . PHE A 1 214 ? 102.73400 96.51500  138.63600 1.000 75.44227  ? 214 PHE A N    1 
ATOM   1069 C CA   . PHE A 1 214 ? 101.28300 96.62900  138.55400 1.000 74.54045  ? 214 PHE A CA   1 
ATOM   1070 C C    . PHE A 1 214 ? 100.59000 96.26200  139.86200 1.000 75.79287  ? 214 PHE A C    1 
ATOM   1071 O O    . PHE A 1 214 ? 99.46300  96.71000  140.09900 1.000 76.27849  ? 214 PHE A O    1 
ATOM   1072 C CB   . PHE A 1 214 ? 100.76100 95.75700  137.41000 1.000 72.71320  ? 214 PHE A CB   1 
ATOM   1073 C CG   . PHE A 1 214 ? 99.26600  95.63900  137.36800 1.000 75.00669  ? 214 PHE A CG   1 
ATOM   1074 C CD1  . PHE A 1 214 ? 98.47200  96.76800  137.26000 1.000 74.92334  ? 214 PHE A CD1  1 
ATOM   1075 C CD2  . PHE A 1 214 ? 98.65400  94.39900  137.42200 1.000 76.86294  ? 214 PHE A CD2  1 
ATOM   1076 C CE1  . PHE A 1 214 ? 97.09500  96.66400  137.21800 1.000 76.18271  ? 214 PHE A CE1  1 
ATOM   1077 C CE2  . PHE A 1 214 ? 97.27700  94.28800  137.37800 1.000 77.13781  ? 214 PHE A CE2  1 
ATOM   1078 C CZ   . PHE A 1 214 ? 96.49700  95.42200  137.27500 1.000 75.13570  ? 214 PHE A CZ   1 
ATOM   1079 N N    . ARG A 1 215 ? 101.23200 95.46600  140.71600 1.000 80.96273  ? 215 ARG A N    1 
ATOM   1080 C CA   . ARG A 1 215 ? 100.63200 94.99000  141.95700 1.000 80.64928  ? 215 ARG A CA   1 
ATOM   1081 C C    . ARG A 1 215 ? 101.00400 95.82200  143.17900 1.000 79.62035  ? 215 ARG A C    1 
ATOM   1082 O O    . ARG A 1 215 ? 100.65500 95.43900  144.30000 1.000 80.87146  ? 215 ARG A O    1 
ATOM   1083 C CB   . ARG A 1 215 ? 100.99300 93.52200  142.18600 1.000 80.35806  ? 215 ARG A CB   1 
ATOM   1084 C CG   . ARG A 1 215 ? 100.26600 92.59700  141.23700 1.000 79.68817  ? 215 ARG A CG   1 
ATOM   1085 C CD   . ARG A 1 215 ? 98.95400  92.15900  141.86400 1.000 80.34394  ? 215 ARG A CD   1 
ATOM   1086 N NE   . ARG A 1 215 ? 97.82200  92.92800  141.35900 1.000 81.38723  ? 215 ARG A NE   1 
ATOM   1087 C CZ   . ARG A 1 215 ? 97.00300  92.52200  140.40000 1.000 80.92343  ? 215 ARG A CZ   1 
ATOM   1088 N NH1  . ARG A 1 215 ? 97.15800  91.35000  139.80900 1.000 80.02711  ? 215 ARG A NH1  1 
ATOM   1089 N NH2  . ARG A 1 215 ? 95.99900  93.31000  140.02800 1.000 80.42380  ? 215 ARG A NH2  1 
ATOM   1090 N N    . THR A 1 216 ? 101.69700 96.94000  143.00100 1.000 75.42500  ? 216 THR A N    1 
ATOM   1091 C CA   . THR A 1 216 ? 101.99800 97.81900  144.12100 1.000 75.53021  ? 216 THR A CA   1 
ATOM   1092 C C    . THR A 1 216 ? 100.85800 98.82900  144.27300 1.000 77.96432  ? 216 THR A C    1 
ATOM   1093 O O    . THR A 1 216 ? 99.76800  98.63900  143.72500 1.000 77.55739  ? 216 THR A O    1 
ATOM   1094 C CB   . THR A 1 216 ? 103.35900 98.49000  143.91400 1.000 76.20241  ? 216 THR A CB   1 
ATOM   1095 O OG1  . THR A 1 216 ? 103.72400 99.20600  145.10000 1.000 77.65834  ? 216 THR A OG1  1 
ATOM   1096 C CG2  . THR A 1 216 ? 103.29900 99.46300  142.74900 1.000 76.62146  ? 216 THR A CG2  1 
ATOM   1097 N N    . GLY A 1 217 ? 101.08900 99.90800  145.01600 1.000 76.07608  ? 217 GLY A N    1 
ATOM   1098 C CA   . GLY A 1 217 ? 100.08400 100.94200 145.16500 1.000 74.92056  ? 217 GLY A CA   1 
ATOM   1099 C C    . GLY A 1 217 ? 100.53400 102.26900 144.59100 1.000 74.91306  ? 217 GLY A C    1 
ATOM   1100 O O    . GLY A 1 217 ? 99.71700  103.05600 144.10400 1.000 76.43261  ? 217 GLY A O    1 
ATOM   1101 N N    . GLN A 1 218 ? 101.84200 102.52600 144.64700 1.000 72.94517  ? 218 GLN A N    1 
ATOM   1102 C CA   . GLN A 1 218 ? 102.39500 103.73500 144.04900 1.000 75.10600  ? 218 GLN A CA   1 
ATOM   1103 C C    . GLN A 1 218 ? 102.22100 103.76100 142.53500 1.000 74.39546  ? 218 GLN A C    1 
ATOM   1104 O O    . GLN A 1 218 ? 102.34700 104.82800 141.92400 1.000 74.80085  ? 218 GLN A O    1 
ATOM   1105 C CB   . GLN A 1 218 ? 103.87400 103.85700 144.42500 1.000 73.72677  ? 218 GLN A CB   1 
ATOM   1106 C CG   . GLN A 1 218 ? 104.62600 104.96600 143.71400 1.000 74.70236  ? 218 GLN A CG   1 
ATOM   1107 C CD   . GLN A 1 218 ? 105.50500 104.44100 142.59700 1.000 76.17613  ? 218 GLN A CD   1 
ATOM   1108 O OE1  . GLN A 1 218 ? 105.15400 103.47800 141.91500 1.000 75.64862  ? 218 GLN A OE1  1 
ATOM   1109 N NE2  . GLN A 1 218 ? 106.66100 105.06800 142.41000 1.000 75.38987  ? 218 GLN A NE2  1 
ATOM   1110 N N    . PHE A 1 219 ? 101.93500 102.61200 141.92200 1.000 66.39385  ? 219 PHE A N    1 
ATOM   1111 C CA   . PHE A 1 219 ? 101.79700 102.54000 140.47000 1.000 67.75623  ? 219 PHE A CA   1 
ATOM   1112 C C    . PHE A 1 219 ? 100.67000 103.43800 139.96600 1.000 68.43178  ? 219 PHE A C    1 
ATOM   1113 O O    . PHE A 1 219 ? 100.87000 104.26100 139.06100 1.000 70.18576  ? 219 PHE A O    1 
ATOM   1114 C CB   . PHE A 1 219 ? 101.56700 101.08600 140.05400 1.000 65.29353  ? 219 PHE A CB   1 
ATOM   1115 C CG   . PHE A 1 219 ? 101.07800 100.92000 138.64400 1.000 66.49780  ? 219 PHE A CG   1 
ATOM   1116 C CD1  . PHE A 1 219 ? 101.91700 101.16700 137.57100 1.000 66.26522  ? 219 PHE A CD1  1 
ATOM   1117 C CD2  . PHE A 1 219 ? 99.78300  100.49900 138.39200 1.000 65.06790  ? 219 PHE A CD2  1 
ATOM   1118 C CE1  . PHE A 1 219 ? 101.46900 101.00800 136.27400 1.000 66.65635  ? 219 PHE A CE1  1 
ATOM   1119 C CE2  . PHE A 1 219 ? 99.33100  100.33900 137.09800 1.000 64.68067  ? 219 PHE A CE2  1 
ATOM   1120 C CZ   . PHE A 1 219 ? 100.17500 100.59400 136.03800 1.000 65.09744  ? 219 PHE A CZ   1 
ATOM   1121 N N    . ILE A 1 220 ? 99.47500  103.29200 140.54300 1.000 63.11941  ? 220 ILE A N    1 
ATOM   1122 C CA   . ILE A 1 220 ? 98.31300  104.03000 140.05000 1.000 62.24616  ? 220 ILE A CA   1 
ATOM   1123 C C    . ILE A 1 220 ? 98.51600  105.53100 140.20200 1.000 62.37979  ? 220 ILE A C    1 
ATOM   1124 O O    . ILE A 1 220 ? 98.12500  106.31400 139.32900 1.000 65.75869  ? 220 ILE A O    1 
ATOM   1125 C CB   . ILE A 1 220 ? 97.03900  103.55800 140.77500 1.000 62.83077  ? 220 ILE A CB   1 
ATOM   1126 C CG1  . ILE A 1 220 ? 96.72600  102.10600 140.41300 1.000 64.64431  ? 220 ILE A CG1  1 
ATOM   1127 C CG2  . ILE A 1 220 ? 95.86800  104.46400 140.43500 1.000 63.42161  ? 220 ILE A CG2  1 
ATOM   1128 C CD1  . ILE A 1 220 ? 95.65100  101.48200 141.27600 1.000 64.98027  ? 220 ILE A CD1  1 
ATOM   1129 N N    . GLU A 1 221 ? 99.12900  105.95800 141.30500 1.000 60.48446  ? 221 GLU A N    1 
ATOM   1130 C CA   . GLU A 1 221 ? 99.34400  107.38500 141.53000 1.000 61.07984  ? 221 GLU A CA   1 
ATOM   1131 C C    . GLU A 1 221 ? 100.23100 107.98400 140.44300 1.000 62.71377  ? 221 GLU A C    1 
ATOM   1132 O O    . GLU A 1 221 ? 99.90200  109.02300 139.84900 1.000 65.85200  ? 221 GLU A O    1 
ATOM   1133 C CB   . GLU A 1 221 ? 99.95100  107.59900 142.91800 1.000 62.66366  ? 221 GLU A CB   1 
ATOM   1134 C CG   . GLU A 1 221 ? 99.59700  108.92800 143.56300 1.000 64.93184  ? 221 GLU A CG   1 
ATOM   1135 C CD   . GLU A 1 221 ? 100.73000 109.48800 144.39900 1.000 65.84675  ? 221 GLU A CD   1 
ATOM   1136 O OE1  . GLU A 1 221 ? 101.68300 108.73500 144.68900 1.000 64.77691  ? 221 GLU A OE1  1 
ATOM   1137 O OE2  . GLU A 1 221 ? 100.66500 110.67900 144.76900 1.000 65.37450  ? 221 GLU A OE2  1 
ATOM   1138 N N    . VAL A 1 222 ? 101.36400 107.33400 140.16800 1.000 53.30225  ? 222 VAL A N    1 
ATOM   1139 C CA   . VAL A 1 222 ? 102.28400 107.83400 139.15200 1.000 55.26095  ? 222 VAL A CA   1 
ATOM   1140 C C    . VAL A 1 222 ? 101.62100 107.81300 137.78300 1.000 55.02095  ? 222 VAL A C    1 
ATOM   1141 O O    . VAL A 1 222 ? 101.76700 108.75500 136.99100 1.000 58.59632  ? 222 VAL A O    1 
ATOM   1142 C CB   . VAL A 1 222 ? 103.58400 107.01000 139.16500 1.000 55.84253  ? 222 VAL A CB   1 
ATOM   1143 C CG1  . VAL A 1 222 ? 104.60500 107.61000 138.21400 1.000 56.55844  ? 222 VAL A CG1  1 
ATOM   1144 C CG2  . VAL A 1 222 ? 104.14200 106.92000 140.57700 1.000 54.14428  ? 222 VAL A CG2  1 
ATOM   1145 N N    . ALA A 1 223 ? 100.85800 106.75600 137.49100 1.000 47.41634  ? 223 ALA A N    1 
ATOM   1146 C CA   . ALA A 1 223 ? 100.19100 106.68500 136.19700 1.000 51.33094  ? 223 ALA A CA   1 
ATOM   1147 C C    . ALA A 1 223 ? 99.19600  107.82700 136.04000 1.000 55.62322  ? 223 ALA A C    1 
ATOM   1148 O O    . ALA A 1 223 ? 99.11700  108.45600 134.97500 1.000 56.40152  ? 223 ALA A O    1 
ATOM   1149 C CB   . ALA A 1 223 ? 99.49800  105.33300 136.03500 1.000 46.86069  ? 223 ALA A CB   1 
ATOM   1150 N N    . ILE A 1 224 ? 98.44600  108.12900 137.10100 1.000 50.46146  ? 224 ILE A N    1 
ATOM   1151 C CA   . ILE A 1 224 ? 97.43700  109.17800 137.02100 1.000 48.28657  ? 224 ILE A CA   1 
ATOM   1152 C C    . ILE A 1 224 ? 98.10300  110.52800 136.80400 1.000 51.98760  ? 224 ILE A C    1 
ATOM   1153 O O    . ILE A 1 224 ? 97.66500  111.32600 135.96600 1.000 54.99542  ? 224 ILE A O    1 
ATOM   1154 C CB   . ILE A 1 224 ? 96.55400  109.17800 138.28100 1.000 48.23232  ? 224 ILE A CB   1 
ATOM   1155 C CG1  . ILE A 1 224 ? 95.89400  107.81200 138.47500 1.000 50.19713  ? 224 ILE A CG1  1 
ATOM   1156 C CG2  . ILE A 1 224 ? 95.50200  110.27100 138.19500 1.000 52.11157  ? 224 ILE A CG2  1 
ATOM   1157 C CD1  . ILE A 1 224 ? 95.02500  107.38400 137.31300 1.000 50.91468  ? 224 ILE A CD1  1 
ATOM   1158 N N    . SER A 1 225 ? 99.16700  110.81200 137.55900 1.000 43.90579  ? 225 SER A N    1 
ATOM   1159 C CA   . SER A 1 225 ? 99.80100  112.12100 137.42500 1.000 47.07974  ? 225 SER A CA   1 
ATOM   1160 C C    . SER A 1 225 ? 100.44500 112.28500 136.05100 1.000 50.24342  ? 225 SER A C    1 
ATOM   1161 O O    . SER A 1 225 ? 100.38500 113.37000 135.44800 1.000 52.41551  ? 225 SER A O    1 
ATOM   1162 C CB   . SER A 1 225 ? 100.83700 112.31400 138.53200 1.000 44.50971  ? 225 SER A CB   1 
ATOM   1163 O OG   . SER A 1 225 ? 100.21900 112.35000 139.80500 1.000 48.61594  ? 225 SER A OG   1 
ATOM   1164 N N    . ARG A 1 226 ? 101.01400 111.20200 135.51100 1.000 42.38365  ? 226 ARG A N    1 
ATOM   1165 C CA   . ARG A 1 226 ? 101.61400 111.27800 134.18500 1.000 42.35645  ? 226 ARG A CA   1 
ATOM   1166 C C    . ARG A 1 226 ? 100.55400 111.49900 133.11200 1.000 40.41139  ? 226 ARG A C    1 
ATOM   1167 O O    . ARG A 1 226 ? 100.74000 112.32400 132.20500 1.000 41.51759  ? 226 ARG A O    1 
ATOM   1168 C CB   . ARG A 1 226 ? 102.41900 110.00700 133.91500 1.000 42.64839  ? 226 ARG A CB   1 
ATOM   1169 C CG   . ARG A 1 226 ? 103.72100 109.94400 134.70600 1.000 38.28612  ? 226 ARG A CG   1 
ATOM   1170 C CD   . ARG A 1 226 ? 104.38600 108.57900 134.62400 1.000 38.33256  ? 226 ARG A CD   1 
ATOM   1171 N NE   . ARG A 1 226 ? 105.77800 108.63100 135.05700 1.000 44.62530  ? 226 ARG A NE   1 
ATOM   1172 C CZ   . ARG A 1 226 ? 106.57600 107.57500 135.15500 1.000 44.82633  ? 226 ARG A CZ   1 
ATOM   1173 N NH1  . ARG A 1 226 ? 106.15200 106.35900 134.85700 1.000 41.89597  ? 226 ARG A NH1  1 
ATOM   1174 N NH2  . ARG A 1 226 ? 107.83000 107.74500 135.56400 1.000 40.49576  ? 226 ARG A NH2  1 
ATOM   1175 N N    . PHE A 1 227 ? 99.42100  110.79600 133.21000 1.000 37.94560  ? 227 PHE A N    1 
ATOM   1176 C CA   . PHE A 1 227 ? 98.35400  111.01900 132.24200 1.000 42.05569  ? 227 PHE A CA   1 
ATOM   1177 C C    . PHE A 1 227 ? 97.77900  112.42500 132.35800 1.000 44.60340  ? 227 PHE A C    1 
ATOM   1178 O O    . PHE A 1 227 ? 97.40200  113.02600 131.34400 1.000 47.56043  ? 227 PHE A O    1 
ATOM   1179 C CB   . PHE A 1 227 ? 97.25100  109.97900 132.42400 1.000 41.53676  ? 227 PHE A CB   1 
ATOM   1180 C CG   . PHE A 1 227 ? 96.15700  110.07500 131.40100 1.000 44.86189  ? 227 PHE A CG   1 
ATOM   1181 C CD1  . PHE A 1 227 ? 96.34900  109.60100 130.11500 1.000 44.01500  ? 227 PHE A CD1  1 
ATOM   1182 C CD2  . PHE A 1 227 ? 94.93700  110.64300 131.72500 1.000 45.69986  ? 227 PHE A CD2  1 
ATOM   1183 C CE1  . PHE A 1 227 ? 95.34400  109.69000 129.17200 1.000 45.47008  ? 227 PHE A CE1  1 
ATOM   1184 C CE2  . PHE A 1 227 ? 93.92800  110.73400 130.78700 1.000 44.37513  ? 227 PHE A CE2  1 
ATOM   1185 C CZ   . PHE A 1 227 ? 94.13100  110.25700 129.50900 1.000 44.40420  ? 227 PHE A CZ   1 
ATOM   1186 N N    . LEU A 1 228 ? 97.72800  112.97400 133.57200 1.000 39.95810  ? 228 LEU A N    1 
ATOM   1187 C CA   . LEU A 1 228 ? 97.23900  114.33800 133.74300 1.000 40.86798  ? 228 LEU A CA   1 
ATOM   1188 C C    . LEU A 1 228 ? 98.14300  115.33100 133.02400 1.000 41.53677  ? 228 LEU A C    1 
ATOM   1189 O O    . LEU A 1 228 ? 97.66800  116.21000 132.29000 1.000 46.32498  ? 228 LEU A O    1 
ATOM   1190 C CB   . LEU A 1 228 ? 97.14100  114.67600 135.23100 1.000 42.32708  ? 228 LEU A CB   1 
ATOM   1191 C CG   . LEU A 1 228 ? 95.91800  114.14000 135.97900 1.000 43.55967  ? 228 LEU A CG   1 
ATOM   1192 C CD1  . LEU A 1 228 ? 96.10700  114.27400 137.48100 1.000 41.32137  ? 228 LEU A CD1  1 
ATOM   1193 C CD2  . LEU A 1 228 ? 94.65600  114.85800 135.53000 1.000 41.37901  ? 228 LEU A CD2  1 
ATOM   1194 N N    . LEU A 1 229 ? 99.45800  115.19900 133.21700 1.000 36.66762  ? 229 LEU A N    1 
ATOM   1195 C CA   . LEU A 1 229 ? 100.37100 116.11800 132.54500 1.000 39.48885  ? 229 LEU A CA   1 
ATOM   1196 C C    . LEU A 1 229 ? 100.32200 115.94800 131.02900 1.000 39.69952  ? 229 LEU A C    1 
ATOM   1197 O O    . LEU A 1 229 ? 100.40700 116.93300 130.28000 1.000 44.46694  ? 229 LEU A O    1 
ATOM   1198 C CB   . LEU A 1 229 ? 101.79200 115.92600 133.07100 1.000 38.91116  ? 229 LEU A CB   1 
ATOM   1199 C CG   . LEU A 1 229 ? 102.18100 116.93900 134.15100 1.000 41.88077  ? 229 LEU A CG   1 
ATOM   1200 C CD1  . LEU A 1 229 ? 101.40900 116.67900 135.43500 1.000 40.42646  ? 229 LEU A CD1  1 
ATOM   1201 C CD2  . LEU A 1 229 ? 103.67200 116.92800 134.40800 1.000 39.74176  ? 229 LEU A CD2  1 
ATOM   1202 N N    . ILE A 1 230 ? 100.13800 114.71300 130.55300 1.000 29.19915  ? 230 ILE A N    1 
ATOM   1203 C CA   . ILE A 1 230 ? 100.06700 114.50200 129.11000 1.000 27.10346  ? 230 ILE A CA   1 
ATOM   1204 C C    . ILE A 1 230 ? 98.81200  115.14700 128.53200 1.000 30.96173  ? 230 ILE A C    1 
ATOM   1205 O O    . ILE A 1 230 ? 98.85000  115.76900 127.45900 1.000 38.12412  ? 230 ILE A O    1 
ATOM   1206 C CB   . ILE A 1 230 ? 100.12800 112.99800 128.78700 1.000 28.30354  ? 230 ILE A CB   1 
ATOM   1207 C CG1  . ILE A 1 230 ? 101.49300 112.42200 129.16700 1.000 32.88775  ? 230 ILE A CG1  1 
ATOM   1208 C CG2  . ILE A 1 230 ? 99.82700  112.75100 127.32000 1.000 27.76347  ? 230 ILE A CG2  1 
ATOM   1209 C CD1  . ILE A 1 230 ? 101.54900 110.91300 129.13000 1.000 34.50344  ? 230 ILE A CD1  1 
ATOM   1210 N N    . ALA A 1 231 ? 97.68900  115.04900 129.24800 1.000 32.32706  ? 231 ALA A N    1 
ATOM   1211 C CA   . ALA A 1 231 ? 96.47000  115.67900 128.75500 1.000 33.36220  ? 231 ALA A CA   1 
ATOM   1212 C C    . ALA A 1 231 ? 96.57900  117.19600 128.77800 1.000 32.42679  ? 231 ALA A C    1 
ATOM   1213 O O    . ALA A 1 231 ? 96.08800  117.86700 127.85900 1.000 30.67682  ? 231 ALA A O    1 
ATOM   1214 C CB   . ALA A 1 231 ? 95.26800  115.21800 129.57800 1.000 33.06482  ? 231 ALA A CB   1 
ATOM   1215 N N    . LEU A 1 232 ? 97.26400  117.75200 129.78000 1.000 25.37107  ? 232 LEU A N    1 
ATOM   1216 C CA   . LEU A 1 232 ? 97.44000  119.20000 129.81100 1.000 27.06554  ? 232 LEU A CA   1 
ATOM   1217 C C    . LEU A 1 232 ? 98.27700  119.66700 128.62700 1.000 30.09054  ? 232 LEU A C    1 
ATOM   1218 O O    . LEU A 1 232 ? 97.93800  120.65700 127.95900 1.000 34.08708  ? 232 LEU A O    1 
ATOM   1219 C CB   . LEU A 1 232 ? 98.08900  119.61800 131.13000 1.000 28.14101  ? 232 LEU A CB   1 
ATOM   1220 C CG   . LEU A 1 232 ? 98.57600  121.06400 131.24200 1.000 32.82429  ? 232 LEU A CG   1 
ATOM   1221 C CD1  . LEU A 1 232 ? 98.32500  121.61500 132.63700 1.000 34.63449  ? 232 LEU A CD1  1 
ATOM   1222 C CD2  . LEU A 1 232 ? 100.05400 121.15700 130.89100 1.000 28.70958  ? 232 LEU A CD2  1 
ATOM   1223 N N    . GLY A 1 233 ? 99.35800  118.94300 128.33000 1.000 25.79260  ? 233 GLY A N    1 
ATOM   1224 C CA   . GLY A 1 233 ? 100.21000 119.34600 127.22400 1.000 22.63422  ? 233 GLY A CA   1 
ATOM   1225 C C    . GLY A 1 233 ? 99.50600  119.23700 125.88600 1.000 26.51331  ? 233 GLY A C    1 
ATOM   1226 O O    . GLY A 1 233 ? 99.64100  120.11900 125.02700 1.000 27.82238  ? 233 GLY A O    1 
ATOM   1227 N N    . ALA A 1 234 ? 98.70400  118.18300 125.70300 1.000 21.12417  ? 234 ALA A N    1 
ATOM   1228 C CA   . ALA A 1 234 ? 97.99400  118.04100 124.43700 1.000 18.46757  ? 234 ALA A CA   1 
ATOM   1229 C C    . ALA A 1 234 ? 96.91600  119.10700 124.28200 1.000 25.29709  ? 234 ALA A C    1 
ATOM   1230 O O    . ALA A 1 234 ? 96.71900  119.64000 123.18300 1.000 25.83963  ? 234 ALA A O    1 
ATOM   1231 C CB   . ALA A 1 234 ? 97.38700  116.64300 124.32900 1.000 20.01589  ? 234 ALA A CB   1 
ATOM   1232 N N    . GLY A 1 235 ? 96.23000  119.46100 125.37300 1.000 26.33929  ? 235 GLY A N    1 
ATOM   1233 C CA   . GLY A 1 235 ? 95.23000  120.51100 125.27800 1.000 16.62309  ? 235 GLY A CA   1 
ATOM   1234 C C    . GLY A 1 235 ? 95.83600  121.85700 124.93500 1.000 21.74771  ? 235 GLY A C    1 
ATOM   1235 O O    . GLY A 1 235 ? 95.30700  122.59700 124.09500 1.000 24.06941  ? 235 GLY A O    1 
ATOM   1236 N N    . VAL A 1 236 ? 96.98100  122.17600 125.54500 1.000 23.57421  ? 236 VAL A N    1 
ATOM   1237 C CA   . VAL A 1 236 ? 97.63900  123.44400 125.24200 1.000 22.12206  ? 236 VAL A CA   1 
ATOM   1238 C C    . VAL A 1 236 ? 98.08600  123.47500 123.78700 1.000 24.68192  ? 236 VAL A C    1 
ATOM   1239 O O    . VAL A 1 236 ? 97.86900  124.46400 123.07200 1.000 21.56836  ? 236 VAL A O    1 
ATOM   1240 C CB   . VAL A 1 236 ? 98.82000  123.68200 126.19900 1.000 18.19202  ? 236 VAL A CB   1 
ATOM   1241 C CG1  . VAL A 1 236 ? 99.40100  125.06900 125.98400 1.000 18.70159  ? 236 VAL A CG1  1 
ATOM   1242 C CG2  . VAL A 1 236 ? 98.37600  123.51100 127.63800 1.000 24.41405  ? 236 VAL A CG2  1 
ATOM   1243 N N    . SER A 1 237 ? 98.73700  122.40100 123.32900 1.000 22.39164  ? 237 SER A N    1 
ATOM   1244 C CA   . SER A 1 237 ? 99.17900  122.36000 121.93800 1.000 20.74577  ? 237 SER A CA   1 
ATOM   1245 C C    . SER A 1 237 ? 98.01100  122.51800 120.97200 1.000 19.64860  ? 237 SER A C    1 
ATOM   1246 O O    . SER A 1 237 ? 98.09100  123.29300 120.01000 1.000 15.33066  ? 237 SER A O    1 
ATOM   1247 C CB   . SER A 1 237 ? 99.92400  121.05500 121.66200 1.000 20.57156  ? 237 SER A CB   1 
ATOM   1248 O OG   . SER A 1 237 ? 101.05200 120.92500 122.50700 1.000 31.90050  ? 237 SER A OG   1 
ATOM   1249 N N    . LEU A 1 238 ? 96.89600  121.83100 121.23400 1.000 27.85927  ? 238 LEU A N    1 
ATOM   1250 C CA   . LEU A 1 238 ? 95.78200  121.89500 120.29600 1.000 24.33170  ? 238 LEU A CA   1 
ATOM   1251 C C    . LEU A 1 238 ? 95.11600  123.26400 120.28500 1.000 27.06375  ? 238 LEU A C    1 
ATOM   1252 O O    . LEU A 1 238 ? 94.72200  123.74400 119.21400 1.000 29.38013  ? 238 LEU A O    1 
ATOM   1253 C CB   . LEU A 1 238 ? 94.75800  120.80900 120.62600 1.000 26.74403  ? 238 LEU A CB   1 
ATOM   1254 C CG   . LEU A 1 238 ? 93.62500  120.62500 119.61500 1.000 29.31246  ? 238 LEU A CG   1 
ATOM   1255 C CD1  . LEU A 1 238 ? 94.05000  119.68200 118.50300 1.000 29.62812  ? 238 LEU A CD1  1 
ATOM   1256 C CD2  . LEU A 1 238 ? 92.36600  120.11800 120.29800 1.000 28.11273  ? 238 LEU A CD2  1 
ATOM   1257 N N    . GLY A 1 239 ? 95.05300  123.95000 121.42800 1.000 23.92470  ? 239 GLY A N    1 
ATOM   1258 C CA   . GLY A 1 239 ? 94.46000  125.27700 121.41600 1.000 17.90368  ? 239 GLY A CA   1 
ATOM   1259 C C    . GLY A 1 239 ? 95.35700  126.31800 120.77200 1.000 19.98658  ? 239 GLY A C    1 
ATOM   1260 O O    . GLY A 1 239 ? 94.89000  127.14600 119.97600 1.000 21.42103  ? 239 GLY A O    1 
ATOM   1261 N N    . VAL A 1 240 ? 96.67000  126.22700 121.02000 1.000 23.25405  ? 240 VAL A N    1 
ATOM   1262 C CA   . VAL A 1 240 ? 97.60700  127.17300 120.41400 1.000 18.34460  ? 240 VAL A CA   1 
ATOM   1263 C C    . VAL A 1 240 ? 97.89300  126.84000 118.96300 1.000 24.65837  ? 240 VAL A C    1 
ATOM   1264 O O    . VAL A 1 240 ? 98.56300  127.62100 118.27500 1.000 27.49701  ? 240 VAL A O    1 
ATOM   1265 C CB   . VAL A 1 240 ? 98.93100  127.23000 121.19900 1.000 21.13142  ? 240 VAL A CB   1 
ATOM   1266 C CG1  . VAL A 1 240 ? 99.85200  128.29000 120.61800 1.000 18.77126  ? 240 VAL A CG1  1 
ATOM   1267 C CG2  . VAL A 1 240 ? 98.66400  127.50900 122.66600 1.000 22.67689  ? 240 VAL A CG2  1 
ATOM   1268 N N    . ASN A 1 241 ? 97.38900  125.71200 118.47100 1.000 17.78931  ? 241 ASN A N    1 
ATOM   1269 C CA   . ASN A 1 241 ? 97.52100  125.38000 117.06200 1.000 9.84678   ? 241 ASN A CA   1 
ATOM   1270 C C    . ASN A 1 241 ? 96.25700  125.68300 116.28100 1.000 22.85592  ? 241 ASN A C    1 
ATOM   1271 O O    . ASN A 1 241 ? 96.34100  126.05900 115.10800 1.000 24.29171  ? 241 ASN A O    1 
ATOM   1272 C CB   . ASN A 1 241 ? 97.87500  123.90000 116.88400 1.000 13.38154  ? 241 ASN A CB   1 
ATOM   1273 C CG   . ASN A 1 241 ? 98.66400  123.64000 115.61800 1.000 17.50068  ? 241 ASN A CG   1 
ATOM   1274 O OD1  . ASN A 1 241 ? 99.16000  124.56700 114.98200 1.000 24.86358  ? 241 ASN A OD1  1 
ATOM   1275 N ND2  . ASN A 1 241 ? 98.77300  122.37400 115.23700 1.000 17.96132  ? 241 ASN A ND2  1 
ATOM   1276 N N    . MET A 1 242 ? 95.08800  125.54500 116.90600 1.000 35.91418  ? 242 MET A N    1 
ATOM   1277 C CA   . MET A 1 242 ? 93.83800  125.77100 116.20200 1.000 22.07550  ? 242 MET A CA   1 
ATOM   1278 C C    . MET A 1 242 ? 93.34400  127.20900 116.27800 1.000 24.69407  ? 242 MET A C    1 
ATOM   1279 O O    . MET A 1 242 ? 92.59400  127.62800 115.39100 1.000 25.47518  ? 242 MET A O    1 
ATOM   1280 C CB   . MET A 1 242 ? 92.75000  124.84100 116.74500 1.000 21.06432  ? 242 MET A CB   1 
ATOM   1281 C CG   . MET A 1 242 ? 91.75700  124.37900 115.69600 1.000 30.72671  ? 242 MET A CG   1 
ATOM   1282 S SD   . MET A 1 242 ? 91.24600  122.66700 115.92000 1.000 49.49659  ? 242 MET A SD   1 
ATOM   1283 C CE   . MET A 1 242 ? 89.72500  122.64600 114.97500 1.000 29.06027  ? 242 MET A CE   1 
ATOM   1284 N N    . PHE A 1 243 ? 93.73600  127.98400 117.29300 1.000 23.76972  ? 243 PHE A N    1 
ATOM   1285 C CA   . PHE A 1 243 ? 93.16200  129.31500 117.44900 1.000 15.07768  ? 243 PHE A CA   1 
ATOM   1286 C C    . PHE A 1 243 ? 94.08100  130.46700 117.05700 1.000 15.80256  ? 243 PHE A C    1 
ATOM   1287 O O    . PHE A 1 243 ? 93.65200  131.62300 117.13600 1.000 20.80845  ? 243 PHE A O    1 
ATOM   1288 C CB   . PHE A 1 243 ? 92.67100  129.50300 118.88800 1.000 19.45719  ? 243 PHE A CB   1 
ATOM   1289 C CG   . PHE A 1 243 ? 91.52100  128.60800 119.24500 1.000 26.04396  ? 243 PHE A CG   1 
ATOM   1290 C CD1  . PHE A 1 243 ? 90.37500  128.59700 118.46800 1.000 18.45430  ? 243 PHE A CD1  1 
ATOM   1291 C CD2  . PHE A 1 243 ? 91.58800  127.76900 120.34200 1.000 29.30909  ? 243 PHE A CD2  1 
ATOM   1292 C CE1  . PHE A 1 243 ? 89.31700  127.77300 118.78100 1.000 18.36304  ? 243 PHE A CE1  1 
ATOM   1293 C CE2  . PHE A 1 243 ? 90.53100  126.94200 120.66100 1.000 24.48135  ? 243 PHE A CE2  1 
ATOM   1294 C CZ   . PHE A 1 243 ? 89.39400  126.94400 119.87900 1.000 20.74456  ? 243 PHE A CZ   1 
ATOM   1295 N N    . ILE A 1 244 ? 95.31600  130.20700 116.63600 1.000 18.29713  ? 244 ILE A N    1 
ATOM   1296 C CA   . ILE A 1 244 ? 96.22500  131.26600 116.20000 1.000 17.32487  ? 244 ILE A CA   1 
ATOM   1297 C C    . ILE A 1 244 ? 96.76000  130.94700 114.80700 1.000 20.57241  ? 244 ILE A C    1 
ATOM   1298 O O    . ILE A 1 244 ? 97.57800  130.03400 114.64700 1.000 29.71266  ? 244 ILE A O    1 
ATOM   1299 C CB   . ILE A 1 244 ? 97.38100  131.47800 117.18700 1.000 23.24338  ? 244 ILE A CB   1 
ATOM   1300 C CG1  . ILE A 1 244 ? 96.86200  132.09100 118.48900 1.000 17.33787  ? 244 ILE A CG1  1 
ATOM   1301 C CG2  . ILE A 1 244 ? 98.45300  132.36300 116.57400 1.000 20.57101  ? 244 ILE A CG2  1 
ATOM   1302 C CD1  . ILE A 1 244 ? 97.07800  131.22700 119.70500 1.000 19.52692  ? 244 ILE A CD1  1 
ATOM   1303 N N    . TYR A 1 245 ? 96.30500  131.70000 113.80800 1.000 16.40448  ? 245 TYR A N    1 
ATOM   1304 C CA   . TYR A 1 245 ? 96.75500  131.56200 112.42700 1.000 19.04678  ? 245 TYR A CA   1 
ATOM   1305 C C    . TYR A 1 245 ? 96.78900  130.11800 111.91800 1.000 24.50533  ? 245 TYR A C    1 
ATOM   1306 O O    . TYR A 1 245 ? 97.84800  129.61700 111.52700 1.000 24.02866  ? 245 TYR A O    1 
ATOM   1307 C CB   . TYR A 1 245 ? 98.11600  132.22000 112.25100 1.000 21.21366  ? 245 TYR A CB   1 
ATOM   1308 C CG   . TYR A 1 245 ? 98.07800  133.72900 112.32200 1.000 23.20319  ? 245 TYR A CG   1 
ATOM   1309 C CD1  . TYR A 1 245 ? 97.44700  134.47300 111.33400 1.000 22.88520  ? 245 TYR A CD1  1 
ATOM   1310 C CD2  . TYR A 1 245 ? 98.67100  134.41100 113.37500 1.000 23.97799  ? 245 TYR A CD2  1 
ATOM   1311 C CE1  . TYR A 1 245 ? 97.40700  135.85200 111.39400 1.000 24.44513  ? 245 TYR A CE1  1 
ATOM   1312 C CE2  . TYR A 1 245 ? 98.63700  135.79000 113.44300 1.000 22.37978  ? 245 TYR A CE2  1 
ATOM   1313 C CZ   . TYR A 1 245 ? 98.00300  136.50500 112.45000 1.000 28.67997  ? 245 TYR A CZ   1 
ATOM   1314 O OH   . TYR A 1 245 ? 97.96600  137.87800 112.51200 1.000 32.59893  ? 245 TYR A OH   1 
ATOM   1315 N N    . PRO A 1 246 ? 95.65100  129.42700 111.90700 1.000 15.52844  ? 246 PRO A N    1 
ATOM   1316 C CA   . PRO A 1 246 ? 95.64200  128.03200 111.44900 1.000 12.71508  ? 246 PRO A CA   1 
ATOM   1317 C C    . PRO A 1 246 ? 96.07600  127.90800 109.99400 1.000 16.40871  ? 246 PRO A C    1 
ATOM   1318 O O    . PRO A 1 246 ? 95.79000  128.77200 109.16400 1.000 22.73808  ? 246 PRO A O    1 
ATOM   1319 C CB   . PRO A 1 246 ? 94.17900  127.61300 111.63200 1.000 12.43627  ? 246 PRO A CB   1 
ATOM   1320 C CG   . PRO A 1 246 ? 93.41600  128.89900 111.66200 1.000 11.66043  ? 246 PRO A CG   1 
ATOM   1321 C CD   . PRO A 1 246 ? 94.31800  129.86900 112.34400 1.000 12.71381  ? 246 PRO A CD   1 
ATOM   1322 N N    . ILE A 1 247 ? 96.78000  126.81800 109.69300 1.000 12.28919  ? 247 ILE A N    1 
ATOM   1323 C CA   . ILE A 1 247 ? 97.16400  126.45900 108.33100 1.000 5.42928   ? 247 ILE A CA   1 
ATOM   1324 C C    . ILE A 1 247 ? 96.30900  125.27900 107.88800 1.000 7.24927   ? 247 ILE A C    1 
ATOM   1325 O O    . ILE A 1 247 ? 96.20000  124.28000 108.60800 1.000 11.19773  ? 247 ILE A O    1 
ATOM   1326 C CB   . ILE A 1 247 ? 98.66300  126.12600 108.23600 1.000 12.12595  ? 247 ILE A CB   1 
ATOM   1327 C CG1  . ILE A 1 247 ? 99.49000  127.41100 108.15400 1.000 15.98255  ? 247 ILE A CG1  1 
ATOM   1328 C CG2  . ILE A 1 247 ? 98.94100  125.23900 107.03500 1.000 8.74145   ? 247 ILE A CG2  1 
ATOM   1329 C CD1  . ILE A 1 247 ? 100.88000 127.28300 108.72700 1.000 16.46964  ? 247 ILE A CD1  1 
ATOM   1330 N N    . TRP A 1 248 ? 95.70000  125.39600 106.71000 1.000 15.58071  ? 248 TRP A N    1 
ATOM   1331 C CA   . TRP A 1 248 ? 94.79900  124.38200 106.17700 1.000 7.14183   ? 248 TRP A CA   1 
ATOM   1332 C C    . TRP A 1 248 ? 95.46200  123.64000 105.02100 1.000 6.82267   ? 248 TRP A C    1 
ATOM   1333 O O    . TRP A 1 248 ? 96.21600  124.23300 104.24600 1.000 16.73399  ? 248 TRP A O    1 
ATOM   1334 C CB   . TRP A 1 248 ? 93.49300  125.02400 105.70500 1.000 10.07317  ? 248 TRP A CB   1 
ATOM   1335 C CG   . TRP A 1 248 ? 92.87100  125.94600 106.71500 1.000 9.99881   ? 248 TRP A CG   1 
ATOM   1336 C CD1  . TRP A 1 248 ? 93.02500  127.29900 106.78700 1.000 9.29812   ? 248 TRP A CD1  1 
ATOM   1337 C CD2  . TRP A 1 248 ? 91.99700  125.58600 107.79200 1.000 17.52639  ? 248 TRP A CD2  1 
ATOM   1338 N NE1  . TRP A 1 248 ? 92.30300  127.80500 107.83800 1.000 10.95937  ? 248 TRP A NE1  1 
ATOM   1339 C CE2  . TRP A 1 248 ? 91.66300  126.77400 108.47200 1.000 13.77354  ? 248 TRP A CE2  1 
ATOM   1340 C CE3  . TRP A 1 248 ? 91.46400  124.37700 108.24700 1.000 15.06084  ? 248 TRP A CE3  1 
ATOM   1341 C CZ2  . TRP A 1 248 ? 90.82100  126.78700 109.58100 1.000 5.62286   ? 248 TRP A CZ2  1 
ATOM   1342 C CZ3  . TRP A 1 248 ? 90.63000  124.39300 109.34700 1.000 12.14564  ? 248 TRP A CZ3  1 
ATOM   1343 C CH2  . TRP A 1 248 ? 90.31600  125.59000 110.00100 1.000 9.55003   ? 248 TRP A CH2  1 
ATOM   1344 N N    . ALA A 1 249 ? 95.17700  122.33800 104.90800 1.000 14.92791  ? 249 ALA A N    1 
ATOM   1345 C CA   . ALA A 1 249 ? 95.74000  121.51600 103.83900 1.000 15.21679  ? 249 ALA A CA   1 
ATOM   1346 C C    . ALA A 1 249 ? 94.98500  121.63700 102.51800 1.000 19.86400  ? 249 ALA A C    1 
ATOM   1347 O O    . ALA A 1 249 ? 95.56500  121.37000 101.45200 1.000 27.95553  ? 249 ALA A O    1 
ATOM   1348 C CB   . ALA A 1 249 ? 95.77500  120.05000 104.27300 1.000 10.88381  ? 249 ALA A CB   1 
ATOM   1349 N N    . GLY A 1 250 ? 93.73200  122.09600 102.55100 1.000 15.34515  ? 250 GLY A N    1 
ATOM   1350 C CA   . GLY A 1 250 ? 92.99300  122.25200 101.31400 1.000 10.10676  ? 250 GLY A CA   1 
ATOM   1351 C C    . GLY A 1 250 ? 93.46200  123.44600 100.51600 1.000 16.00508  ? 250 GLY A C    1 
ATOM   1352 O O    . GLY A 1 250 ? 93.45400  123.41300 99.28100  1.000 33.31035  ? 250 GLY A O    1 
ATOM   1353 N N    . GLU A 1 251 ? 93.96800  124.47300 101.19800 1.000 13.15499  ? 251 GLU A N    1 
ATOM   1354 C CA   . GLU A 1 251 ? 94.52900  125.60000 100.47400 1.000 19.03392  ? 251 GLU A CA   1 
ATOM   1355 C C    . GLU A 1 251 ? 95.87700  125.23900 99.87500  1.000 17.94244  ? 251 GLU A C    1 
ATOM   1356 O O    . GLU A 1 251 ? 96.23200  125.76000 98.81200  1.000 28.37762  ? 251 GLU A O    1 
ATOM   1357 C CB   . GLU A 1 251 ? 94.67800  126.79900 101.41100 1.000 23.71930  ? 251 GLU A CB   1 
ATOM   1358 C CG   . GLU A 1 251 ? 93.36600  127.42000 101.84900 1.000 18.80965  ? 251 GLU A CG   1 
ATOM   1359 C CD   . GLU A 1 251 ? 93.49600  128.90000 102.14300 1.000 29.48317  ? 251 GLU A CD   1 
ATOM   1360 O OE1  . GLU A 1 251 ? 94.12200  129.61500 101.33300 1.000 29.00666  ? 251 GLU A OE1  1 
ATOM   1361 O OE2  . GLU A 1 251 ? 92.97400  129.34900 103.18600 1.000 33.12662  ? 251 GLU A OE2  1 
ATOM   1362 N N    . ASP A 1 252 ? 96.56500  124.25500 100.45800 1.000 13.55876  ? 252 ASP A N    1 
ATOM   1363 C CA   . ASP A 1 252 ? 97.83600  123.81400 99.90100  1.000 23.48590  ? 252 ASP A CA   1 
ATOM   1364 C C    . ASP A 1 252 ? 97.61100  122.95000 98.67100  1.000 23.25744  ? 252 ASP A C    1 
ATOM   1365 O O    . ASP A 1 252 ? 98.33500  123.08300 97.67800  1.000 30.52413  ? 252 ASP A O    1 
ATOM   1366 C CB   . ASP A 1 252 ? 98.63600  123.04600 100.95300 1.000 19.56721  ? 252 ASP A CB   1 
ATOM   1367 C CG   . ASP A 1 252 ? 98.84700  123.84400 102.22000 1.000 26.58897  ? 252 ASP A CG   1 
ATOM   1368 O OD1  . ASP A 1 252 ? 98.00500  124.71300 102.52100 1.000 28.84490  ? 252 ASP A OD1  1 
ATOM   1369 O OD2  . ASP A 1 252 ? 99.85500  123.60100 102.91600 1.000 30.27633  ? 252 ASP A OD2  1 
ATOM   1370 N N    . LEU A 1 253 ? 96.57300  122.11200 98.68900  1.000 12.57949  ? 253 LEU A N    1 
ATOM   1371 C CA   . LEU A 1 253 ? 96.24700  121.35400 97.48400  1.000 16.52749  ? 253 LEU A CA   1 
ATOM   1372 C C    . LEU A 1 253 ? 95.77300  122.28400 96.36800  1.000 14.52787  ? 253 LEU A C    1 
ATOM   1373 O O    . LEU A 1 253 ? 96.21100  122.16700 95.20700  1.000 13.72843  ? 253 LEU A O    1 
ATOM   1374 C CB   . LEU A 1 253 ? 95.18300  120.30600 97.81200  1.000 16.61625  ? 253 LEU A CB   1 
ATOM   1375 C CG   . LEU A 1 253 ? 94.87200  119.23100 96.77200  1.000 22.10536  ? 253 LEU A CG   1 
ATOM   1376 C CD1  . LEU A 1 253 ? 96.10200  118.38800 96.49600  1.000 13.94025  ? 253 LEU A CD1  1 
ATOM   1377 C CD2  . LEU A 1 253 ? 93.71500  118.36400 97.24000  1.000 10.29760  ? 253 LEU A CD2  1 
ATOM   1378 N N    . HIS A 1 254 ? 94.89700  123.23300 96.71700  1.000 10.46514  ? 254 HIS A N    1 
ATOM   1379 C CA   . HIS A 1 254 ? 94.40500  124.20500 95.75000  1.000 5.78491   ? 254 HIS A CA   1 
ATOM   1380 C C    . HIS A 1 254 ? 95.55400  124.97000 95.10300  1.000 14.29352  ? 254 HIS A C    1 
ATOM   1381 O O    . HIS A 1 254 ? 95.56100  125.17500 93.88500  1.000 17.57396  ? 254 HIS A O    1 
ATOM   1382 C CB   . HIS A 1 254 ? 93.42900  125.15600 96.44700  1.000 4.36192   ? 254 HIS A CB   1 
ATOM   1383 C CG   . HIS A 1 254 ? 92.77400  126.14400 95.53300  1.000 17.76984  ? 254 HIS A CG   1 
ATOM   1384 N ND1  . HIS A 1 254 ? 91.47200  126.00700 95.10500  1.000 18.49989  ? 254 HIS A ND1  1 
ATOM   1385 C CD2  . HIS A 1 254 ? 93.23100  127.29400 94.98400  1.000 21.29151  ? 254 HIS A CD2  1 
ATOM   1386 C CE1  . HIS A 1 254 ? 91.15900  127.02300 94.32100  1.000 18.62816  ? 254 HIS A CE1  1 
ATOM   1387 N NE2  . HIS A 1 254 ? 92.20900  127.81800 94.23100  1.000 19.94195  ? 254 HIS A NE2  1 
ATOM   1388 N N    . ASN A 1 255 ? 96.53700  125.40300 95.90000  1.000 11.36641  ? 255 ASN A N    1 
ATOM   1389 C CA   . ASN A 1 255 ? 97.63700  126.18200 95.34200  1.000 10.76379  ? 255 ASN A CA   1 
ATOM   1390 C C    . ASN A 1 255 ? 98.62000  125.31500 94.55800  1.000 16.85147  ? 255 ASN A C    1 
ATOM   1391 O O    . ASN A 1 255 ? 99.20500  125.77800 93.56400  1.000 23.34055  ? 255 ASN A O    1 
ATOM   1392 C CB   . ASN A 1 255 ? 98.36800  126.91000 96.47000  1.000 14.78471  ? 255 ASN A CB   1 
ATOM   1393 C CG   . ASN A 1 255 ? 97.64200  128.16000 96.92600  1.000 19.76918  ? 255 ASN A CG   1 
ATOM   1394 O OD1  . ASN A 1 255 ? 96.60700  128.52900 96.37400  1.000 26.49760  ? 255 ASN A OD1  1 
ATOM   1395 N ND2  . ASN A 1 255 ? 98.17900  128.81300 97.94800  1.000 21.28348  ? 255 ASN A ND2  1 
ATOM   1396 N N    . LEU A 1 256 ? 98.78300  124.05100 94.96100  1.000 11.66014  ? 256 LEU A N    1 
ATOM   1397 C CA   . LEU A 1 256 ? 99.69500  123.15700 94.25800  1.000 16.97652  ? 256 LEU A CA   1 
ATOM   1398 C C    . LEU A 1 256 ? 99.20700  122.86600 92.84500  1.000 13.66838  ? 256 LEU A C    1 
ATOM   1399 O O    . LEU A 1 256 ? 100.01300 122.77600 91.90700  1.000 20.56402  ? 256 LEU A O    1 
ATOM   1400 C CB   . LEU A 1 256 ? 99.86200  121.86300 95.05500  1.000 11.12911  ? 256 LEU A CB   1 
ATOM   1401 C CG   . LEU A 1 256 ? 100.74800 120.76300 94.47100  1.000 18.86417  ? 256 LEU A CG   1 
ATOM   1402 C CD1  . LEU A 1 256 ? 102.19200 121.22400 94.38500  1.000 16.88942  ? 256 LEU A CD1  1 
ATOM   1403 C CD2  . LEU A 1 256 ? 100.63700 119.49700 95.30100  1.000 16.40525  ? 256 LEU A CD2  1 
ATOM   1404 N N    . VAL A 1 257 ? 97.89000  122.73700 92.66500  1.000 6.91259   ? 257 VAL A N    1 
ATOM   1405 C CA   . VAL A 1 257 ? 97.38700  122.46400 91.31800  1.000 14.06168  ? 257 VAL A CA   1 
ATOM   1406 C C    . VAL A 1 257 ? 97.71000  123.62300 90.37300  1.000 14.55633  ? 257 VAL A C    1 
ATOM   1407 O O    . VAL A 1 257 ? 98.16700  123.41700 89.23500  1.000 21.33958  ? 257 VAL A O    1 
ATOM   1408 C CB   . VAL A 1 257 ? 95.87400  122.17300 91.36700  1.000 12.85244  ? 257 VAL A CB   1 
ATOM   1409 C CG1  . VAL A 1 257 ? 95.28200  122.17300 89.96700  1.000 9.56470   ? 257 VAL A CG1  1 
ATOM   1410 C CG2  . VAL A 1 257 ? 95.61200  120.84600 92.06000  1.000 5.75810   ? 257 VAL A CG2  1 
ATOM   1411 N N    . VAL A 1 258 ? 97.52400  124.85800 90.84200  1.000 7.53043   ? 258 VAL A N    1 
ATOM   1412 C CA   . VAL A 1 258 ? 97.80900  126.02700 90.01400  1.000 10.28140  ? 258 VAL A CA   1 
ATOM   1413 C C    . VAL A 1 258 ? 99.30000  126.12600 89.71300  1.000 12.90923  ? 258 VAL A C    1 
ATOM   1414 O O    . VAL A 1 258 ? 99.70600  126.47000 88.59000  1.000 19.04043  ? 258 VAL A O    1 
ATOM   1415 C CB   . VAL A 1 258 ? 97.28400  127.30000 90.70300  1.000 18.70877  ? 258 VAL A CB   1 
ATOM   1416 C CG1  . VAL A 1 258 ? 97.63000  128.53500 89.88700  1.000 16.58619  ? 258 VAL A CG1  1 
ATOM   1417 C CG2  . VAL A 1 258 ? 95.78300  127.20100 90.93300  1.000 10.25803  ? 258 VAL A CG2  1 
ATOM   1418 N N    . LYS A 1 259 ? 100.14300 125.81300 90.70100  1.000 13.82826  ? 259 LYS A N    1 
ATOM   1419 C CA   . LYS A 1 259 ? 101.58000 125.88300 90.46100  1.000 15.88802  ? 259 LYS A CA   1 
ATOM   1420 C C    . LYS A 1 259 ? 102.01400 124.86500 89.41100  1.000 18.19982  ? 259 LYS A C    1 
ATOM   1421 O O    . LYS A 1 259 ? 102.85200 125.16800 88.54900  1.000 23.53690  ? 259 LYS A O    1 
ATOM   1422 C CB   . LYS A 1 259 ? 102.33700 125.67100 91.77100  1.000 17.88995  ? 259 LYS A CB   1 
ATOM   1423 C CG   . LYS A 1 259 ? 103.71400 126.31000 91.80400  1.000 24.28619  ? 259 LYS A CG   1 
ATOM   1424 C CD   . LYS A 1 259 ? 104.59800 125.65400 92.84800  1.000 22.21362  ? 259 LYS A CD   1 
ATOM   1425 C CE   . LYS A 1 259 ? 104.87400 124.20000 92.50800  1.000 25.95468  ? 259 LYS A CE   1 
ATOM   1426 N NZ   . LYS A 1 259 ? 106.32000 123.87100 92.64100  1.000 29.96725  ? 259 LYS A NZ   1 
ATOM   1427 N N    . ASN A 1 260 ? 101.42700 123.66500 89.43800  1.000 14.12987  ? 260 ASN A N    1 
ATOM   1428 C CA   . ASN A 1 260 ? 101.79300 122.66700 88.43600  1.000 15.65896  ? 260 ASN A CA   1 
ATOM   1429 C C    . ASN A 1 260 ? 101.31800 123.08300 87.04800  1.000 15.21790  ? 260 ASN A C    1 
ATOM   1430 O O    . ASN A 1 260 ? 102.02100 122.86400 86.04500  1.000 9.39462   ? 260 ASN A O    1 
ATOM   1431 C CB   . ASN A 1 260 ? 101.21500 121.30500 88.81600  1.000 18.34697  ? 260 ASN A CB   1 
ATOM   1432 C CG   . ASN A 1 260 ? 101.94500 120.66500 89.98100  1.000 22.26358  ? 260 ASN A CG   1 
ATOM   1433 O OD1  . ASN A 1 260 ? 103.05800 121.06000 90.32200  1.000 28.98503  ? 260 ASN A OD1  1 
ATOM   1434 N ND2  . ASN A 1 260 ? 101.31900 119.67000 90.59500  1.000 17.23916  ? 260 ASN A ND2  1 
ATOM   1435 N N    . PHE A 1 261 ? 100.15000 123.73000 86.97500  1.000 19.23847  ? 261 PHE A N    1 
ATOM   1436 C CA   . PHE A 1 261 ? 99.66400  124.19700 85.68000  1.000 13.12472  ? 261 PHE A CA   1 
ATOM   1437 C C    . PHE A 1 261 ? 100.59400 125.24900 85.08900  1.000 18.43682  ? 261 PHE A C    1 
ATOM   1438 O O    . PHE A 1 261 ? 100.85000 125.25100 83.87900  1.000 17.71367  ? 261 PHE A O    1 
ATOM   1439 C CB   . PHE A 1 261 ? 98.24600  124.75000 85.80900  1.000 12.69966  ? 261 PHE A CB   1 
ATOM   1440 C CG   . PHE A 1 261 ? 97.18400  123.82000 85.29800  1.000 13.66086  ? 261 PHE A CG   1 
ATOM   1441 C CD1  . PHE A 1 261 ? 96.95100  123.69800 83.94000  1.000 18.96326  ? 261 PHE A CD1  1 
ATOM   1442 C CD2  . PHE A 1 261 ? 96.41600  123.07400 86.17400  1.000 17.78417  ? 261 PHE A CD2  1 
ATOM   1443 C CE1  . PHE A 1 261 ? 95.97600  122.84500 83.46400  1.000 19.11504  ? 261 PHE A CE1  1 
ATOM   1444 C CE2  . PHE A 1 261 ? 95.43800  122.22000 85.70400  1.000 21.98318  ? 261 PHE A CE2  1 
ATOM   1445 C CZ   . PHE A 1 261 ? 95.21800  122.10600 84.34700  1.000 22.26182  ? 261 PHE A CZ   1 
ATOM   1446 N N    . MET A 1 262 ? 101.10300 126.15900 85.92200  1.000 23.73629  ? 262 MET A N    1 
ATOM   1447 C CA   . MET A 1 262 ? 102.06400 127.14400 85.42200  1.000 20.10932  ? 262 MET A CA   1 
ATOM   1448 C C    . MET A 1 262 ? 103.37700 126.49000 84.98500  1.000 16.54888  ? 262 MET A C    1 
ATOM   1449 O O    . MET A 1 262 ? 103.94400 126.83800 83.93200  1.000 17.02417  ? 262 MET A O    1 
ATOM   1450 C CB   . MET A 1 262 ? 102.32800 128.20600 86.48900  1.000 14.70593  ? 262 MET A CB   1 
ATOM   1451 C CG   . MET A 1 262 ? 101.08100 128.90700 86.99600  1.000 16.21446  ? 262 MET A CG   1 
ATOM   1452 S SD   . MET A 1 262 ? 100.37000 130.01000 85.76000  1.000 35.48815  ? 262 MET A SD   1 
ATOM   1453 C CE   . MET A 1 262 ? 98.64300  129.55600 85.84400  1.000 23.62349  ? 262 MET A CE   1 
ATOM   1454 N N    . ASN A 1 263 ? 103.87100 125.53500 85.77800  1.000 19.74506  ? 263 ASN A N    1 
ATOM   1455 C CA   . ASN A 1 263 ? 105.17700 124.94800 85.49400  1.000 20.45108  ? 263 ASN A CA   1 
ATOM   1456 C C    . ASN A 1 263 ? 105.18100 124.15100 84.19500  1.000 19.60704  ? 263 ASN A C    1 
ATOM   1457 O O    . ASN A 1 263 ? 106.18000 124.16200 83.46300  1.000 16.93713  ? 263 ASN A O    1 
ATOM   1458 C CB   . ASN A 1 263 ? 105.61600 124.06200 86.65900  1.000 13.80923  ? 263 ASN A CB   1 
ATOM   1459 C CG   . ASN A 1 263 ? 106.06600 124.86100 87.86200  1.000 23.39363  ? 263 ASN A CG   1 
ATOM   1460 O OD1  . ASN A 1 263 ? 106.20800 126.08000 87.79400  1.000 27.81199  ? 263 ASN A OD1  1 
ATOM   1461 N ND2  . ASN A 1 263 ? 106.29400 124.17500 88.97400  1.000 23.96233  ? 263 ASN A ND2  1 
ATOM   1462 N N    . VAL A 1 264 ? 104.08400 123.45900 83.87800  1.000 20.69907  ? 264 VAL A N    1 
ATOM   1463 C CA   . VAL A 1 264 ? 104.08900 122.68200 82.63800  1.000 17.46088  ? 264 VAL A CA   1 
ATOM   1464 C C    . VAL A 1 264 ? 104.16000 123.59400 81.41200  1.000 13.93422  ? 264 VAL A C    1 
ATOM   1465 O O    . VAL A 1 264 ? 104.85500 123.28700 80.43200  1.000 17.70965  ? 264 VAL A O    1 
ATOM   1466 C CB   . VAL A 1 264 ? 102.86400 121.75200 82.58700  1.000 20.12155  ? 264 VAL A CB   1 
ATOM   1467 C CG1  . VAL A 1 264 ? 102.83600 120.98600 81.27600  1.000 19.65318  ? 264 VAL A CG1  1 
ATOM   1468 C CG2  . VAL A 1 264 ? 102.89100 120.79200 83.76100  1.000 17.54561  ? 264 VAL A CG2  1 
ATOM   1469 N N    . ALA A 1 265 ? 103.48400 124.74400 81.45700  1.000 11.95791  ? 265 ALA A N    1 
ATOM   1470 C CA   . ALA A 1 265 ? 103.56100 125.68200 80.34000  1.000 11.85752  ? 265 ALA A CA   1 
ATOM   1471 C C    . ALA A 1 265 ? 104.95700 126.27500 80.20900  1.000 17.70753  ? 265 ALA A C    1 
ATOM   1472 O O    . ALA A 1 265 ? 105.48200 126.42700 79.09100  1.000 14.59878  ? 265 ALA A O    1 
ATOM   1473 C CB   . ALA A 1 265 ? 102.52200 126.78900 80.51200  1.000 7.72922   ? 265 ALA A CB   1 
ATOM   1474 N N    . THR A 1 266 ? 105.59700 126.57300 81.34400  1.000 19.12513  ? 266 THR A N    1 
ATOM   1475 C CA   . THR A 1 266 ? 106.95600 127.10000 81.26600  1.000 21.03837  ? 266 THR A CA   1 
ATOM   1476 C C    . THR A 1 266 ? 107.90400 126.07000 80.66300  1.000 23.33693  ? 266 THR A C    1 
ATOM   1477 O O    . THR A 1 266 ? 108.75400 126.40800 79.82700  1.000 22.88165  ? 266 THR A O    1 
ATOM   1478 C CB   . THR A 1 266 ? 107.44000 127.52900 82.65000  1.000 20.94367  ? 266 THR A CB   1 
ATOM   1479 O OG1  . THR A 1 266 ? 106.66400 128.64300 83.10600  1.000 29.10129  ? 266 THR A OG1  1 
ATOM   1480 C CG2  . THR A 1 266 ? 108.90300 127.93400 82.59800  1.000 19.01134  ? 266 THR A CG2  1 
ATOM   1481 N N    . SER A 1 267 ? 107.74700 124.79900 81.04400  1.000 21.45431  ? 267 SER A N    1 
ATOM   1482 C CA   . SER A 1 267 ? 108.60600 123.75800 80.48800  1.000 12.38639  ? 267 SER A CA   1 
ATOM   1483 C C    . SER A 1 267 ? 108.37900 123.58000 78.99100  1.000 17.51591  ? 267 SER A C    1 
ATOM   1484 O O    . SER A 1 267 ? 109.33700 123.38800 78.23500  1.000 14.36841  ? 267 SER A O    1 
ATOM   1485 C CB   . SER A 1 267 ? 108.37800 122.43800 81.21900  1.000 20.31939  ? 267 SER A CB   1 
ATOM   1486 O OG   . SER A 1 267 ? 108.91500 122.48500 82.52600  1.000 28.89529  ? 267 SER A OG   1 
ATOM   1487 N N    . LEU A 1 268 ? 107.12400 123.64100 78.53700  1.000 16.88868  ? 268 LEU A N    1 
ATOM   1488 C CA   . LEU A 1 268 ? 106.87400 123.46600 77.10800  1.000 18.27328  ? 268 LEU A CA   1 
ATOM   1489 C C    . LEU A 1 268 ? 107.51200 124.58500 76.29300  1.000 24.85762  ? 268 LEU A C    1 
ATOM   1490 O O    . LEU A 1 268 ? 108.15500 124.33300 75.25700  1.000 21.49435  ? 268 LEU A O    1 
ATOM   1491 C CB   . LEU A 1 268 ? 105.37200 123.39900 76.83600  1.000 20.11570  ? 268 LEU A CB   1 
ATOM   1492 C CG   . LEU A 1 268 ? 104.99000 123.23500 75.36200  1.000 25.03417  ? 268 LEU A CG   1 
ATOM   1493 C CD1  . LEU A 1 268 ? 105.12900 121.78700 74.92000  1.000 21.41069  ? 268 LEU A CD1  1 
ATOM   1494 C CD2  . LEU A 1 268 ? 103.58400 123.74800 75.10300  1.000 19.75063  ? 268 LEU A CD2  1 
ATOM   1495 N N    . GLU A 1 269 ? 107.36500 125.83200 76.75300  1.000 36.55998  ? 269 GLU A N    1 
ATOM   1496 C CA   . GLU A 1 269 ? 107.97900 126.93100 76.01500  1.000 30.19926  ? 269 GLU A CA   1 
ATOM   1497 C C    . GLU A 1 269 ? 109.49900 126.82400 76.02900  1.000 30.82306  ? 269 GLU A C    1 
ATOM   1498 O O    . GLU A 1 269 ? 110.15400 127.03400 74.99500  1.000 27.35356  ? 269 GLU A O    1 
ATOM   1499 C CB   . GLU A 1 269 ? 107.52700 128.27200 76.59100  1.000 32.74001  ? 269 GLU A CB   1 
ATOM   1500 C CG   . GLU A 1 269 ? 107.49200 129.40000 75.57400  1.000 34.53066  ? 269 GLU A CG   1 
ATOM   1501 C CD   . GLU A 1 269 ? 106.32400 129.28700 74.61400  1.000 41.14193  ? 269 GLU A CD   1 
ATOM   1502 O OE1  . GLU A 1 269 ? 105.73000 128.19200 74.52400  1.000 37.19414  ? 269 GLU A OE1  1 
ATOM   1503 O OE2  . GLU A 1 269 ? 106.00100 130.29400 73.94900  1.000 37.78317  ? 269 GLU A OE2  1 
ATOM   1504 N N    . GLY A 1 270 ? 110.07700 126.45000 77.17400  1.000 32.60522  ? 270 GLY A N    1 
ATOM   1505 C CA   . GLY A 1 270 ? 111.51800 126.28700 77.23300  1.000 30.85772  ? 270 GLY A CA   1 
ATOM   1506 C C    . GLY A 1 270 ? 112.02300 125.18500 76.32300  1.000 31.88594  ? 270 GLY A C    1 
ATOM   1507 O O    . GLY A 1 270 ? 113.08300 125.31400 75.70800  1.000 34.71746  ? 270 GLY A O    1 
ATOM   1508 N N    . CYS A 1 271 ? 111.24900 124.10700 76.18200  1.000 34.13386  ? 271 CYS A N    1 
ATOM   1509 C CA   . CYS A 1 271 ? 111.68100 123.00700 75.32600  1.000 29.36328  ? 271 CYS A CA   1 
ATOM   1510 C C    . CYS A 1 271 ? 111.66600 123.41400 73.86000  1.000 28.78236  ? 271 CYS A C    1 
ATOM   1511 O O    . CYS A 1 271 ? 112.62800 123.15500 73.12400  1.000 22.62942  ? 271 CYS A O    1 
ATOM   1512 C CB   . CYS A 1 271 ? 110.79700 121.77900 75.54800  1.000 30.09199  ? 271 CYS A CB   1 
ATOM   1513 S SG   . CYS A 1 271 ? 111.10900 120.89600 77.08600  1.000 50.13955  ? 271 CYS A SG   1 
ATOM   1514 N N    . VAL A 1 272 ? 110.58400 124.05500 73.41000  1.000 37.42405  ? 272 VAL A N    1 
ATOM   1515 C CA   . VAL A 1 272 ? 110.54500 124.44400 72.00100  1.000 34.02798  ? 272 VAL A CA   1 
ATOM   1516 C C    . VAL A 1 272 ? 111.64000 125.46200 71.69700  1.000 36.48978  ? 272 VAL A C    1 
ATOM   1517 O O    . VAL A 1 272 ? 112.32800 125.37400 70.66500  1.000 33.88576  ? 272 VAL A O    1 
ATOM   1518 C CB   . VAL A 1 272 ? 109.15200 124.97600 71.62000  1.000 35.66788  ? 272 VAL A CB   1 
ATOM   1519 C CG1  . VAL A 1 272 ? 109.17500 125.53700 70.20800  1.000 32.47395  ? 272 VAL A CG1  1 
ATOM   1520 C CG2  . VAL A 1 272 ? 108.11800 123.87100 71.73100  1.000 37.37668  ? 272 VAL A CG2  1 
ATOM   1521 N N    . ASN A 1 273 ? 111.87200 126.40500 72.61800  1.000 40.19048  ? 273 ASN A N    1 
ATOM   1522 C CA   . ASN A 1 273 ? 112.91300 127.39900 72.37200  1.000 37.28016  ? 273 ASN A CA   1 
ATOM   1523 C C    . ASN A 1 273 ? 114.29500 126.75900 72.35000  1.000 36.69578  ? 273 ASN A C    1 
ATOM   1524 O O    . ASN A 1 273 ? 115.10700 127.05900 71.46700  1.000 36.67939  ? 273 ASN A O    1 
ATOM   1525 C CB   . ASN A 1 273 ? 112.85000 128.50800 73.42200  1.000 37.01434  ? 273 ASN A CB   1 
ATOM   1526 C CG   . ASN A 1 273 ? 111.69800 129.46500 73.18900  1.000 40.69079  ? 273 ASN A CG   1 
ATOM   1527 O OD1  . ASN A 1 273 ? 111.20900 129.60400 72.06900  1.000 41.25729  ? 273 ASN A OD1  1 
ATOM   1528 N ND2  . ASN A 1 273 ? 111.26200 130.13400 74.25000  1.000 41.51478  ? 273 ASN A ND2  1 
ATOM   1529 N N    . GLY A 1 274 ? 114.58300 125.87400 73.30600  1.000 41.55239  ? 274 GLY A N    1 
ATOM   1530 C CA   . GLY A 1 274 ? 115.87300 125.20900 73.31200  1.000 35.70297  ? 274 GLY A CA   1 
ATOM   1531 C C    . GLY A 1 274 ? 116.11600 124.38000 72.06700  1.000 34.96928  ? 274 GLY A C    1 
ATOM   1532 O O    . GLY A 1 274 ? 117.22700 124.36000 71.53300  1.000 38.85519  ? 274 GLY A O    1 
ATOM   1533 N N    . TYR A 1 275 ? 115.08500 123.68000 71.58300  1.000 30.71940  ? 275 TYR A N    1 
ATOM   1534 C CA   . TYR A 1 275 ? 115.28000 122.90200 70.36400  1.000 27.56126  ? 275 TYR A CA   1 
ATOM   1535 C C    . TYR A 1 275 ? 115.51300 123.79600 69.15500  1.000 31.35565  ? 275 TYR A C    1 
ATOM   1536 O O    . TYR A 1 275 ? 116.27100 123.42300 68.25300  1.000 29.91233  ? 275 TYR A O    1 
ATOM   1537 C CB   . TYR A 1 275 ? 114.09600 121.97700 70.09900  1.000 33.16132  ? 275 TYR A CB   1 
ATOM   1538 C CG   . TYR A 1 275 ? 114.34100 121.06100 68.92000  1.000 30.97547  ? 275 TYR A CG   1 
ATOM   1539 C CD1  . TYR A 1 275 ? 115.15600 119.94300 69.04400  1.000 31.63396  ? 275 TYR A CD1  1 
ATOM   1540 C CD2  . TYR A 1 275 ? 113.78200 121.32700 67.67800  1.000 29.66842  ? 275 TYR A CD2  1 
ATOM   1541 C CE1  . TYR A 1 275 ? 115.39200 119.10800 67.97200  1.000 27.41046  ? 275 TYR A CE1  1 
ATOM   1542 C CE2  . TYR A 1 275 ? 114.01400 120.49700 66.60000  1.000 28.57793  ? 275 TYR A CE2  1 
ATOM   1543 C CZ   . TYR A 1 275 ? 114.81900 119.38900 66.75200  1.000 29.62612  ? 275 TYR A CZ   1 
ATOM   1544 O OH   . TYR A 1 275 ? 115.04900 118.55900 65.68000  1.000 28.05496  ? 275 TYR A OH   1 
ATOM   1545 N N    . LEU A 1 276 ? 114.88900 124.97300 69.10900  1.000 48.45767  ? 276 LEU A N    1 
ATOM   1546 C CA   . LEU A 1 276 ? 115.04400 125.84100 67.94800  1.000 44.99308  ? 276 LEU A CA   1 
ATOM   1547 C C    . LEU A 1 276 ? 116.14000 126.88200 68.12600  1.000 44.91451  ? 276 LEU A C    1 
ATOM   1548 O O    . LEU A 1 276 ? 116.39200 127.66000 67.20100  1.000 47.80548  ? 276 LEU A O    1 
ATOM   1549 C CB   . LEU A 1 276 ? 113.72100 126.53900 67.61200  1.000 47.82750  ? 276 LEU A CB   1 
ATOM   1550 C CG   . LEU A 1 276 ? 112.67200 125.68900 66.89300  1.000 45.49527  ? 276 LEU A CG   1 
ATOM   1551 C CD1  . LEU A 1 276 ? 111.32300 126.38400 66.90100  1.000 45.12645  ? 276 LEU A CD1  1 
ATOM   1552 C CD2  . LEU A 1 276 ? 113.11400 125.38600 65.47000  1.000 42.64764  ? 276 LEU A CD2  1 
ATOM   1553 N N    . ARG A 1 277 ? 116.80600 126.90600 69.27700  1.000 56.24963  ? 277 ARG A N    1 
ATOM   1554 C CA   . ARG A 1 277 ? 117.85100 127.88800 69.54100  1.000 55.32071  ? 277 ARG A CA   1 
ATOM   1555 C C    . ARG A 1 277 ? 119.14700 127.45400 68.86600  1.000 54.20125  ? 277 ARG A C    1 
ATOM   1556 O O    . ARG A 1 277 ? 119.73000 126.42700 69.23000  1.000 55.41140  ? 277 ARG A O    1 
ATOM   1557 C CB   . ARG A 1 277 ? 118.05800 128.04400 71.04600  1.000 57.49516  ? 277 ARG A CB   1 
ATOM   1558 C CG   . ARG A 1 277 ? 119.46800 128.44500 71.44200  1.000 57.08307  ? 277 ARG A CG   1 
ATOM   1559 C CD   . ARG A 1 277 ? 119.52900 128.86300 72.90200  1.000 57.84174  ? 277 ARG A CD   1 
ATOM   1560 N NE   . ARG A 1 277 ? 118.29700 129.50800 73.33800  1.000 58.38296  ? 277 ARG A NE   1 
ATOM   1561 C CZ   . ARG A 1 277 ? 117.59300 129.13600 74.39900  1.000 58.49415  ? 277 ARG A CZ   1 
ATOM   1562 N NH1  . ARG A 1 277 ? 117.97400 128.12500 75.16200  1.000 57.95373  ? 277 ARG A NH1  1 
ATOM   1563 N NH2  . ARG A 1 277 ? 116.47900 129.79600 74.70200  1.000 57.22262  ? 277 ARG A NH2  1 
ATOM   1564 N N    . CYS A 1 278 ? 119.59700 128.23700 67.89100  1.000 68.75041  ? 278 CYS A N    1 
ATOM   1565 C CA   . CYS A 1 278 ? 120.81900 127.93100 67.15400  1.000 70.00715  ? 278 CYS A CA   1 
ATOM   1566 C C    . CYS A 1 278 ? 122.01100 127.76600 68.09200  1.000 69.87105  ? 278 CYS A C    1 
ATOM   1567 O O    . CYS A 1 278 ? 123.16300 127.87000 67.67000  1.000 69.37292  ? 278 CYS A O    1 
ATOM   1568 C CB   . CYS A 1 278 ? 121.11000 129.02300 66.12300  1.000 69.31705  ? 278 CYS A CB   1 
ATOM   1569 S SG   . CYS A 1 278 ? 120.61600 130.68500 66.63500  1.000 77.59981  ? 278 CYS A SG   1 
ATOM   1570 N N    . VAL A 1 298 ? 114.22100 123.71300 82.38700  1.000 49.69891  ? 298 VAL A N    1 
ATOM   1571 C CA   . VAL A 1 298 ? 113.07300 122.97300 81.88000  1.000 48.24860  ? 298 VAL A CA   1 
ATOM   1572 C C    . VAL A 1 298 ? 112.79000 121.76800 82.76800  1.000 44.65860  ? 298 VAL A C    1 
ATOM   1573 O O    . VAL A 1 298 ? 111.67000 121.26000 82.80900  1.000 47.85582  ? 298 VAL A O    1 
ATOM   1574 C CB   . VAL A 1 298 ? 113.30100 122.53700 80.42100  1.000 46.67250  ? 298 VAL A CB   1 
ATOM   1575 C CG1  . VAL A 1 298 ? 112.30400 121.46300 80.02400  1.000 44.15912  ? 298 VAL A CG1  1 
ATOM   1576 C CG2  . VAL A 1 298 ? 113.20200 123.73400 79.49000  1.000 45.17894  ? 298 VAL A CG2  1 
ATOM   1577 N N    . TYR A 1 299 ? 113.82000 121.32000 83.48700  1.000 47.18092  ? 299 TYR A N    1 
ATOM   1578 C CA   . TYR A 1 299 ? 113.69500 120.11500 84.30000  1.000 50.11438  ? 299 TYR A CA   1 
ATOM   1579 C C    . TYR A 1 299 ? 112.62100 120.27400 85.37000  1.000 48.85580  ? 299 TYR A C    1 
ATOM   1580 O O    . TYR A 1 299 ? 111.73300 119.42300 85.51100  1.000 47.24763  ? 299 TYR A O    1 
ATOM   1581 C CB   . TYR A 1 299 ? 115.04300 119.78200 84.94100  1.000 48.90045  ? 299 TYR A CB   1 
ATOM   1582 C CG   . TYR A 1 299 ? 115.24900 118.31200 85.22500  1.000 50.68609  ? 299 TYR A CG   1 
ATOM   1583 C CD1  . TYR A 1 299 ? 115.03000 117.35600 84.24400  1.000 48.96947  ? 299 TYR A CD1  1 
ATOM   1584 C CD2  . TYR A 1 299 ? 115.65800 117.88000 86.48000  1.000 49.57116  ? 299 TYR A CD2  1 
ATOM   1585 C CE1  . TYR A 1 299 ? 115.21800 116.01200 84.50100  1.000 50.62344  ? 299 TYR A CE1  1 
ATOM   1586 C CE2  . TYR A 1 299 ? 115.84700 116.53800 86.74700  1.000 48.94550  ? 299 TYR A CE2  1 
ATOM   1587 C CZ   . TYR A 1 299 ? 115.62500 115.60900 85.75400  1.000 51.65386  ? 299 TYR A CZ   1 
ATOM   1588 O OH   . TYR A 1 299 ? 115.81100 114.27000 86.01500  1.000 49.76555  ? 299 TYR A OH   1 
ATOM   1589 N N    . LYS A 1 300 ? 112.68100 121.37300 86.12600  1.000 48.03845  ? 300 LYS A N    1 
ATOM   1590 C CA   . LYS A 1 300 ? 111.80100 121.53700 87.27700  1.000 50.66818  ? 300 LYS A CA   1 
ATOM   1591 C C    . LYS A 1 300 ? 110.33200 121.59700 86.88300  1.000 49.89987  ? 300 LYS A C    1 
ATOM   1592 O O    . LYS A 1 300 ? 109.48200 121.05300 87.59700  1.000 46.42737  ? 300 LYS A O    1 
ATOM   1593 C CB   . LYS A 1 300 ? 112.18900 122.79600 88.05400  1.000 47.01352  ? 300 LYS A CB   1 
ATOM   1594 N N    . GLY A 1 301 ? 110.01500 122.18700 85.73300  1.000 38.77792  ? 301 GLY A N    1 
ATOM   1595 C CA   . GLY A 1 301 ? 108.62900 122.28400 85.32100  1.000 40.52290  ? 301 GLY A CA   1 
ATOM   1596 C C    . GLY A 1 301 ? 107.92800 120.94500 85.23700  1.000 39.72667  ? 301 GLY A C    1 
ATOM   1597 O O    . GLY A 1 301 ? 106.94900 120.71600 85.95300  1.000 43.23780  ? 301 GLY A O    1 
ATOM   1598 N N    . TYR A 1 302 ? 108.40400 120.05100 84.37300  1.000 37.56518  ? 302 TYR A N    1 
ATOM   1599 C CA   . TYR A 1 302 ? 107.75000 118.75600 84.24200  1.000 41.23625  ? 302 TYR A CA   1 
ATOM   1600 C C    . TYR A 1 302 ? 108.09300 117.82000 85.39500  1.000 38.99824  ? 302 TYR A C    1 
ATOM   1601 O O    . TYR A 1 302 ? 107.31900 116.89700 85.67900  1.000 41.64723  ? 302 TYR A O    1 
ATOM   1602 C CB   . TYR A 1 302 ? 108.08500 118.12400 82.88200  1.000 37.97997  ? 302 TYR A CB   1 
ATOM   1603 C CG   . TYR A 1 302 ? 109.47900 117.55900 82.72400  1.000 37.65888  ? 302 TYR A CG   1 
ATOM   1604 C CD1  . TYR A 1 302 ? 109.83400 116.34700 83.30100  1.000 38.60670  ? 302 TYR A CD1  1 
ATOM   1605 C CD2  . TYR A 1 302 ? 110.43500 118.22800 81.97100  1.000 36.98493  ? 302 TYR A CD2  1 
ATOM   1606 C CE1  . TYR A 1 302 ? 111.10300 115.82800 83.14800  1.000 38.84611  ? 302 TYR A CE1  1 
ATOM   1607 C CE2  . TYR A 1 302 ? 111.70500 117.71600 81.81200  1.000 37.06719  ? 302 TYR A CE2  1 
ATOM   1608 C CZ   . TYR A 1 302 ? 112.03400 116.51600 82.40200  1.000 40.12550  ? 302 TYR A CZ   1 
ATOM   1609 O OH   . TYR A 1 302 ? 113.29900 116.00000 82.24500  1.000 42.45268  ? 302 TYR A OH   1 
ATOM   1610 N N    . ARG A 1 303 ? 109.21300 118.05500 86.08600  1.000 45.70663  ? 303 ARG A N    1 
ATOM   1611 C CA   . ARG A 1 303 ? 109.59300 117.17800 87.18800  1.000 45.15785  ? 303 ARG A CA   1 
ATOM   1612 C C    . ARG A 1 303 ? 108.68700 117.38200 88.39600  1.000 48.34920  ? 303 ARG A C    1 
ATOM   1613 O O    . ARG A 1 303 ? 108.33100 116.41600 89.07900  1.000 46.39089  ? 303 ARG A O    1 
ATOM   1614 C CB   . ARG A 1 303 ? 111.05400 117.41900 87.56800  1.000 46.55275  ? 303 ARG A CB   1 
ATOM   1615 C CG   . ARG A 1 303 ? 112.05600 116.61500 86.75500  1.000 47.66112  ? 303 ARG A CG   1 
ATOM   1616 C CD   . ARG A 1 303 ? 112.63700 115.47400 87.57300  1.000 49.79921  ? 303 ARG A CD   1 
ATOM   1617 N NE   . ARG A 1 303 ? 111.88300 114.23800 87.40200  1.000 51.16969  ? 303 ARG A NE   1 
ATOM   1618 C CZ   . ARG A 1 303 ? 112.10500 113.35200 86.44100  1.000 48.26034  ? 303 ARG A CZ   1 
ATOM   1619 N NH1  . ARG A 1 303 ? 113.05700 113.53400 85.54000  1.000 45.28679  ? 303 ARG A NH1  1 
ATOM   1620 N NH2  . ARG A 1 303 ? 111.35400 112.25700 86.38100  1.000 48.51824  ? 303 ARG A NH2  1 
ATOM   1621 N N    . SER A 1 304 ? 108.30300 118.63100 88.67900  1.000 45.61101  ? 304 SER A N    1 
ATOM   1622 C CA   . SER A 1 304 ? 107.41300 118.88500 89.80500  1.000 44.39499  ? 304 SER A CA   1 
ATOM   1623 C C    . SER A 1 304 ? 106.06000 118.22200 89.59000  1.000 45.15560  ? 304 SER A C    1 
ATOM   1624 O O    . SER A 1 304 ? 105.45700 117.69700 90.53400  1.000 43.82966  ? 304 SER A O    1 
ATOM   1625 C CB   . SER A 1 304 ? 107.24600 120.39000 90.01300  1.000 46.60641  ? 304 SER A CB   1 
ATOM   1626 O OG   . SER A 1 304 ? 108.50200 121.04500 90.02500  1.000 48.76357  ? 304 SER A OG   1 
ATOM   1627 N N    . ALA A 1 305 ? 105.56500 118.23900 88.35200  1.000 38.96848  ? 305 ALA A N    1 
ATOM   1628 C CA   . ALA A 1 305 ? 104.30300 117.57600 88.04600  1.000 36.88136  ? 305 ALA A CA   1 
ATOM   1629 C C    . ALA A 1 305 ? 104.43800 116.06100 88.12900  1.000 34.83330  ? 305 ALA A C    1 
ATOM   1630 O O    . ALA A 1 305 ? 103.61700 115.39100 88.76500  1.000 41.08392  ? 305 ALA A O    1 
ATOM   1631 C CB   . ALA A 1 305 ? 103.81000 118.00000 86.66300  1.000 36.99656  ? 305 ALA A CB   1 
ATOM   1632 N N    . VAL A 1 306 ? 105.46900 115.49900 87.49400  1.000 35.75954  ? 306 VAL A N    1 
ATOM   1633 C CA   . VAL A 1 306 ? 105.61200 114.04500 87.47800  1.000 38.00953  ? 306 VAL A CA   1 
ATOM   1634 C C    . VAL A 1 306 ? 105.79200 113.49600 88.89000  1.000 40.22238  ? 306 VAL A C    1 
ATOM   1635 O O    . VAL A 1 306 ? 105.30000 112.40900 89.21400  1.000 43.11273  ? 306 VAL A O    1 
ATOM   1636 C CB   . VAL A 1 306 ? 106.77700 113.63300 86.56000  1.000 37.88502  ? 306 VAL A CB   1 
ATOM   1637 C CG1  . VAL A 1 306 ? 106.99700 112.13100 86.62800  1.000 38.45205  ? 306 VAL A CG1  1 
ATOM   1638 C CG2  . VAL A 1 306 ? 106.50500 114.07000 85.12900  1.000 39.91233  ? 306 VAL A CG2  1 
ATOM   1639 N N    . GLU A 1 307 ? 106.49800 114.23000 89.74900  1.000 46.42328  ? 307 GLU A N    1 
ATOM   1640 C CA   . GLU A 1 307 ? 106.80200 113.73500 91.08800  1.000 44.17851  ? 307 GLU A CA   1 
ATOM   1641 C C    . GLU A 1 307 ? 105.99600 114.43600 92.17600  1.000 44.91158  ? 307 GLU A C    1 
ATOM   1642 O O    . GLU A 1 307 ? 106.57600 115.09500 93.04400  1.000 48.17283  ? 307 GLU A O    1 
ATOM   1643 C CB   . GLU A 1 307 ? 108.29800 113.88300 91.37400  1.000 44.57672  ? 307 GLU A CB   1 
ATOM   1644 N N    . SER A 1 308 ? 104.66900 114.30900 92.15000  1.000 42.70906  ? 308 SER A N    1 
ATOM   1645 C CA   . SER A 1 308 ? 103.86300 114.98200 93.16200  1.000 44.50949  ? 308 SER A CA   1 
ATOM   1646 C C    . SER A 1 308 ? 102.62700 114.21200 93.61000  1.000 44.27003  ? 308 SER A C    1 
ATOM   1647 O O    . SER A 1 308 ? 101.93800 114.68700 94.51600  1.000 47.04647  ? 308 SER A O    1 
ATOM   1648 C CB   . SER A 1 308 ? 103.44400 116.36900 92.64500  1.000 45.21176  ? 308 SER A CB   1 
ATOM   1649 O OG   . SER A 1 308 ? 102.67700 117.06500 93.61200  1.000 46.87092  ? 308 SER A OG   1 
ATOM   1650 N N    . THR A 1 309 ? 102.31300 113.05700 93.02000  1.000 42.00588  ? 309 THR A N    1 
ATOM   1651 C CA   . THR A 1 309 ? 101.08900 112.34900 93.39100  1.000 43.51515  ? 309 THR A CA   1 
ATOM   1652 C C    . THR A 1 309 ? 101.04900 112.01800 94.88000  1.000 42.40480  ? 309 THR A C    1 
ATOM   1653 O O    . THR A 1 309 ? 99.98500  112.08300 95.50900  1.000 44.44124  ? 309 THR A O    1 
ATOM   1654 C CB   . THR A 1 309 ? 100.95400 111.07300 92.56000  1.000 45.73400  ? 309 THR A CB   1 
ATOM   1655 O OG1  . THR A 1 309 ? 100.87900 111.41200 91.17100  1.000 45.46619  ? 309 THR A OG1  1 
ATOM   1656 C CG2  . THR A 1 309 ? 99.69900  110.31300 92.95800  1.000 44.81820  ? 309 THR A CG2  1 
ATOM   1657 N N    . SER A 1 310 ? 102.19800 111.67300 95.46500  1.000 38.40822  ? 310 SER A N    1 
ATOM   1658 C CA   . SER A 1 310 ? 102.23400 111.35700 96.89000  1.000 43.76933  ? 310 SER A CA   1 
ATOM   1659 C C    . SER A 1 310 ? 101.81600 112.55600 97.73200  1.000 42.15773  ? 310 SER A C    1 
ATOM   1660 O O    . SER A 1 310 ? 101.02100 112.42700 98.67200  1.000 40.50891  ? 310 SER A O    1 
ATOM   1661 C CB   . SER A 1 310 ? 103.63300 110.88200 97.28300  1.000 43.71592  ? 310 SER A CB   1 
ATOM   1662 O OG   . SER A 1 310 ? 104.62600 111.75300 96.77100  1.000 47.04686  ? 310 SER A OG   1 
ATOM   1663 N N    . GLN A 1 311 ? 102.34800 113.73700 97.40800  1.000 40.22530  ? 311 GLN A N    1 
ATOM   1664 C CA   . GLN A 1 311 ? 101.96400 114.94300 98.13200  1.000 40.25559  ? 311 GLN A CA   1 
ATOM   1665 C C    . GLN A 1 311 ? 100.47800 115.22800 97.96800  1.000 36.63802  ? 311 GLN A C    1 
ATOM   1666 O O    . GLN A 1 311 ? 99.79700  115.59700 98.93300  1.000 41.21626  ? 311 GLN A O    1 
ATOM   1667 C CB   . GLN A 1 311 ? 102.80200 116.12700 97.65200  1.000 36.80814  ? 311 GLN A CB   1 
ATOM   1668 C CG   . GLN A 1 311 ? 102.80400 117.31500 98.59800  1.000 41.24513  ? 311 GLN A CG   1 
ATOM   1669 C CD   . GLN A 1 311 ? 103.40400 118.55500 97.96900  1.000 43.18370  ? 311 GLN A CD   1 
ATOM   1670 O OE1  . GLN A 1 311 ? 104.10000 118.47700 96.95800  1.000 44.31312  ? 311 GLN A OE1  1 
ATOM   1671 N NE2  . GLN A 1 311 ? 103.13900 119.71100 98.56700  1.000 41.94512  ? 311 GLN A NE2  1 
ATOM   1672 N N    . GLU A 1 312 ? 99.95900  115.07400 96.74800  1.000 27.43447  ? 312 GLU A N    1 
ATOM   1673 C CA   . GLU A 1 312 ? 98.55100  115.36200 96.50400  1.000 32.15807  ? 312 GLU A CA   1 
ATOM   1674 C C    . GLU A 1 312 ? 97.65400  114.43300 97.31100  1.000 37.31854  ? 312 GLU A C    1 
ATOM   1675 O O    . GLU A 1 312 ? 96.65500  114.87300 97.89400  1.000 38.37406  ? 312 GLU A O    1 
ATOM   1676 C CB   . GLU A 1 312 ? 98.24400  115.23500 95.01200  1.000 33.85044  ? 312 GLU A CB   1 
ATOM   1677 C CG   . GLU A 1 312 ? 98.52700  116.48700 94.20300  1.000 37.43432  ? 312 GLU A CG   1 
ATOM   1678 C CD   . GLU A 1 312 ? 99.48300  116.22700 93.05600  1.000 40.25694  ? 312 GLU A CD   1 
ATOM   1679 O OE1  . GLU A 1 312 ? 99.41400  115.12900 92.46600  1.000 41.28735  ? 312 GLU A OE1  1 
ATOM   1680 O OE2  . GLU A 1 312 ? 100.30500 117.11400 92.74500  1.000 41.27600  ? 312 GLU A OE2  1 
ATOM   1681 N N    . GLU A 1 313 ? 98.03400  113.15800 97.42600  1.000 37.68370  ? 313 GLU A N    1 
ATOM   1682 C CA   . GLU A 1 313 ? 97.19900  112.22500 98.17300  1.000 29.16906  ? 313 GLU A CA   1 
ATOM   1683 C C    . GLU A 1 313 ? 97.34200  112.41000 99.67700  1.000 30.34316  ? 313 GLU A C    1 
ATOM   1684 O O    . GLU A 1 313 ? 96.36200  112.24400 100.41100 1.000 39.17465  ? 313 GLU A O    1 
ATOM   1685 C CB   . GLU A 1 313 ? 97.53800  110.78500 97.78800  1.000 32.70813  ? 313 GLU A CB   1 
ATOM   1686 C CG   . GLU A 1 313 ? 97.71100  110.56800 96.29800  1.000 34.73236  ? 313 GLU A CG   1 
ATOM   1687 C CD   . GLU A 1 313 ? 96.56300  109.79500 95.68400  1.000 40.15085  ? 313 GLU A CD   1 
ATOM   1688 O OE1  . GLU A 1 313 ? 95.45900  109.80400 96.26700  1.000 38.79252  ? 313 GLU A OE1  1 
ATOM   1689 O OE2  . GLU A 1 313 ? 96.76700  109.17500 94.62000  1.000 41.66627  ? 313 GLU A OE2  1 
ATOM   1690 N N    . SER A 1 314 ? 98.52300  112.80500 100.15400 1.000 18.92412  ? 314 SER A N    1 
ATOM   1691 C CA   . SER A 1 314 ? 98.66300  113.11300 101.57300 1.000 18.56696  ? 314 SER A CA   1 
ATOM   1692 C C    . SER A 1 314 ? 97.81200  114.32200 101.94700 1.000 21.29167  ? 314 SER A C    1 
ATOM   1693 O O    . SER A 1 314 ? 97.07700  114.30300 102.94600 1.000 19.49276  ? 314 SER A O    1 
ATOM   1694 C CB   . SER A 1 314 ? 100.13400 113.35500 101.91000 1.000 18.22132  ? 314 SER A CB   1 
ATOM   1695 O OG   . SER A 1 314 ? 100.37900 113.17000 103.29200 1.000 30.42654  ? 314 SER A OG   1 
ATOM   1696 N N    . LEU A 1 315 ? 97.87900  115.38100 101.13300 1.000 15.94235  ? 315 LEU A N    1 
ATOM   1697 C CA   . LEU A 1 315 ? 97.08600  116.56900 101.41200 1.000 9.84539   ? 315 LEU A CA   1 
ATOM   1698 C C    . LEU A 1 315 ? 95.59800  116.28100 101.28200 1.000 16.67953  ? 315 LEU A C    1 
ATOM   1699 O O    . LEU A 1 315 ? 94.78700  116.90300 101.97700 1.000 22.34624  ? 315 LEU A O    1 
ATOM   1700 C CB   . LEU A 1 315 ? 97.49100  117.70400 100.47200 1.000 15.57913  ? 315 LEU A CB   1 
ATOM   1701 C CG   . LEU A 1 315 ? 98.83400  118.37600 100.75900 1.000 15.99341  ? 315 LEU A CG   1 
ATOM   1702 C CD1  . LEU A 1 315 ? 99.25900  119.23900 99.58600  1.000 12.36522  ? 315 LEU A CD1  1 
ATOM   1703 C CD2  . LEU A 1 315 ? 98.76300  119.19600 102.03400 1.000 21.94334  ? 315 LEU A CD2  1 
ATOM   1704 N N    . MET A 1 316 ? 95.22000  115.34100 100.40900 1.000 15.72408  ? 316 MET A N    1 
ATOM   1705 C CA   . MET A 1 316 ? 93.81800  114.95200 100.32300 1.000 14.18444  ? 316 MET A CA   1 
ATOM   1706 C C    . MET A 1 316 ? 93.38800  114.14100 101.53700 1.000 21.27556  ? 316 MET A C    1 
ATOM   1707 O O    . MET A 1 316 ? 92.21700  114.19000 101.93100 1.000 21.86772  ? 316 MET A O    1 
ATOM   1708 C CB   . MET A 1 316 ? 93.56800  114.14500 99.04900  1.000 14.44296  ? 316 MET A CB   1 
ATOM   1709 C CG   . MET A 1 316 ? 92.21100  114.40200 98.41600  1.000 22.95857  ? 316 MET A CG   1 
ATOM   1710 S SD   . MET A 1 316 ? 91.02100  113.10000 98.76100  1.000 32.90532  ? 316 MET A SD   1 
ATOM   1711 C CE   . MET A 1 316 ? 91.52300  111.86700 97.56800  1.000 21.32180  ? 316 MET A CE   1 
ATOM   1712 N N    . SER A 1 317 ? 94.31900  113.48700 102.21800 1.000 18.63554  ? 317 SER A N    1 
ATOM   1713 C CA   . SER A 1 317 ? 93.97500  112.66100 103.37900 1.000 14.59969  ? 317 SER A CA   1 
ATOM   1714 C C    . SER A 1 317 ? 93.76700  113.45000 104.67700 1.000 19.65426  ? 317 SER A C    1 
ATOM   1715 O O    . SER A 1 317 ? 93.29600  112.90100 105.66300 1.000 23.83740  ? 317 SER A O    1 
ATOM   1716 C CB   . SER A 1 317 ? 95.04600  111.59700 103.60100 1.000 15.88141  ? 317 SER A CB   1 
ATOM   1717 O OG   . SER A 1 317 ? 96.26900  112.18000 104.00700 1.000 19.91389  ? 317 SER A OG   1 
ATOM   1718 N N    . PHE A 1 318 ? 94.11600  114.72800 104.68400 1.000 15.56384  ? 318 PHE A N    1 
ATOM   1719 C CA   . PHE A 1 318 ? 93.96900  115.55100 105.87700 1.000 4.59546   ? 318 PHE A CA   1 
ATOM   1720 C C    . PHE A 1 318 ? 92.91500  116.64000 105.71300 1.000 11.26286  ? 318 PHE A C    1 
ATOM   1721 O O    . PHE A 1 318 ? 92.27800  117.02500 106.68300 1.000 13.23568  ? 318 PHE A O    1 
ATOM   1722 C CB   . PHE A 1 318 ? 95.30300  116.20200 106.21100 1.000 5.34696   ? 318 PHE A CB   1 
ATOM   1723 C CG   . PHE A 1 318 ? 96.38500  115.23600 106.56300 1.000 8.07040   ? 318 PHE A CG   1 
ATOM   1724 C CD1  . PHE A 1 318 ? 96.15000  114.20700 107.45500 1.000 18.17090  ? 318 PHE A CD1  1 
ATOM   1725 C CD2  . PHE A 1 318 ? 97.64900  115.37600 106.02500 1.000 9.38874   ? 318 PHE A CD2  1 
ATOM   1726 C CE1  . PHE A 1 318 ? 97.15300  113.32000 107.78800 1.000 12.45594  ? 318 PHE A CE1  1 
ATOM   1727 C CE2  . PHE A 1 318 ? 98.65700  114.49300 106.35200 1.000 8.24465   ? 318 PHE A CE2  1 
ATOM   1728 C CZ   . PHE A 1 318 ? 98.40900  113.46400 107.23600 1.000 8.75983   ? 318 PHE A CZ   1 
ATOM   1729 N N    . ALA A 1 319 ? 92.75300  117.14700 104.49400 1.000 11.10245  ? 319 ALA A N    1 
ATOM   1730 C CA   . ALA A 1 319 ? 91.78300  118.19800 104.21000 1.000 7.28761   ? 319 ALA A CA   1 
ATOM   1731 C C    . ALA A 1 319 ? 90.40200  117.73900 104.55200 1.000 14.75862  ? 319 ALA A C    1 
ATOM   1732 O O    . ALA A 1 319 ? 89.47200  118.53400 104.64300 1.000 20.52019  ? 319 ALA A O    1 
ATOM   1733 C CB   . ALA A 1 319 ? 91.85500  118.56500 102.74800 1.000 1.51427   ? 319 ALA A CB   1 
ATOM   1734 N N    . ILE A 1 320 ? 90.25400  116.45000 104.73500 1.000 9.94492   ? 320 ILE A N    1 
ATOM   1735 C CA   . ILE A 1 320 ? 88.95700  115.86500 105.08000 1.000 12.01733  ? 320 ILE A CA   1 
ATOM   1736 C C    . ILE A 1 320 ? 88.58400  116.00300 106.55800 1.000 18.45285  ? 320 ILE A C    1 
ATOM   1737 O O    . ILE A 1 320 ? 87.43900  116.32000 106.86600 1.000 27.59889  ? 320 ILE A O    1 
ATOM   1738 C CB   . ILE A 1 320 ? 88.90200  114.41300 104.57900 1.000 15.10250  ? 320 ILE A CB   1 
ATOM   1739 C CG1  . ILE A 1 320 ? 90.01200  113.59100 105.22500 1.000 19.48355  ? 320 ILE A CG1  1 
ATOM   1740 C CG2  . ILE A 1 320 ? 89.03100  114.37200 103.06600 1.000 15.62693  ? 320 ILE A CG2  1 
ATOM   1741 C CD1  . ILE A 1 320 ? 90.04700  112.15000 104.77200 1.000 15.58263  ? 320 ILE A CD1  1 
ATOM   1742 N N    . TRP A 1 321 ? 89.51200  115.74600 107.47100 1.000 7.99107   ? 321 TRP A N    1 
ATOM   1743 C CA   . TRP A 1 321 ? 89.24500  115.94400 108.88500 1.000 7.93072   ? 321 TRP A CA   1 
ATOM   1744 C C    . TRP A 1 321 ? 88.90800  117.36500 109.25000 1.000 9.83804   ? 321 TRP A C    1 
ATOM   1745 O O    . TRP A 1 321 ? 88.34300  117.61200 110.30600 1.000 10.01999  ? 321 TRP A O    1 
ATOM   1746 C CB   . TRP A 1 321 ? 90.45100  115.52400 109.70800 1.000 16.37428  ? 321 TRP A CB   1 
ATOM   1747 C CG   . TRP A 1 321 ? 90.76100  114.07100 109.70100 1.000 20.24254  ? 321 TRP A CG   1 
ATOM   1748 C CD1  . TRP A 1 321 ? 91.25700  113.34200 108.66400 1.000 12.61261  ? 321 TRP A CD1  1 
ATOM   1749 C CD2  . TRP A 1 321 ? 90.63100  113.16700 110.80300 1.000 15.81615  ? 321 TRP A CD2  1 
ATOM   1750 N NE1  . TRP A 1 321 ? 91.42700  112.03500 109.04400 1.000 14.17306  ? 321 TRP A NE1  1 
ATOM   1751 C CE2  . TRP A 1 321 ? 91.05000  111.90200 110.35500 1.000 16.57901  ? 321 TRP A CE2  1 
ATOM   1752 C CE3  . TRP A 1 321 ? 90.19200  113.30400 112.12300 1.000 11.12900  ? 321 TRP A CE3  1 
ATOM   1753 C CZ2  . TRP A 1 321 ? 91.04500  110.78000 111.17900 1.000 14.93233  ? 321 TRP A CZ2  1 
ATOM   1754 C CZ3  . TRP A 1 321 ? 90.18700  112.18900 112.93900 1.000 9.35127   ? 321 TRP A CZ3  1 
ATOM   1755 C CH2  . TRP A 1 321 ? 90.60900  110.94400 112.46500 1.000 11.30816  ? 321 TRP A CH2  1 
ATOM   1756 N N    . GLU A 1 322 ? 89.25200  118.31100 108.38600 1.000 16.90321  ? 322 GLU A N    1 
ATOM   1757 C CA   . GLU A 1 322 ? 89.04300  119.72500 108.68100 1.000 12.19156  ? 322 GLU A CA   1 
ATOM   1758 C C    . GLU A 1 322 ? 87.60100  120.17500 108.46800 1.000 15.33082  ? 322 GLU A C    1 
ATOM   1759 O O    . GLU A 1 322 ? 86.91300  119.65900 107.59600 1.000 21.44935  ? 322 GLU A O    1 
ATOM   1760 C CB   . GLU A 1 322 ? 90.00300  120.55100 107.83200 1.000 13.20943  ? 322 GLU A CB   1 
ATOM   1761 C CG   . GLU A 1 322 ? 91.46700  120.23700 108.09200 1.000 13.64836  ? 322 GLU A CG   1 
ATOM   1762 C CD   . GLU A 1 322 ? 92.39800  120.92900 107.11700 1.000 11.91383  ? 322 GLU A CD   1 
ATOM   1763 O OE1  . GLU A 1 322 ? 91.94900  121.26900 106.00500 1.000 20.69925  ? 322 GLU A OE1  1 
ATOM   1764 O OE2  . GLU A 1 322 ? 93.58100  121.12400 107.45700 1.000 11.12849  ? 322 GLU A OE2  1 
ATOM   1765 N N    . PRO A 1 323 ? 87.13000  121.13000 109.28600 1.000 22.52550  ? 323 PRO A N    1 
ATOM   1766 C CA   . PRO A 1 323 ? 85.75100  121.61600 109.16700 1.000 24.20305  ? 323 PRO A CA   1 
ATOM   1767 C C    . PRO A 1 323 ? 85.62000  122.66100 108.07300 1.000 22.94476  ? 323 PRO A C    1 
ATOM   1768 O O    . PRO A 1 323 ? 86.62500  123.20500 107.59300 1.000 25.44140  ? 323 PRO A O    1 
ATOM   1769 C CB   . PRO A 1 323 ? 85.47600  122.21900 110.55100 1.000 22.02608  ? 323 PRO A CB   1 
ATOM   1770 C CG   . PRO A 1 323 ? 86.81800  122.66600 111.01200 1.000 20.39563  ? 323 PRO A CG   1 
ATOM   1771 C CD   . PRO A 1 323 ? 87.78300  121.62700 110.50900 1.000 21.12723  ? 323 PRO A CD   1 
ATOM   1772 N N    . PRO A 1 324 ? 84.39200  122.96600 107.65300 1.000 28.95990  ? 324 PRO A N    1 
ATOM   1773 C CA   . PRO A 1 324 ? 84.19000  123.97600 106.60600 1.000 29.31983  ? 324 PRO A CA   1 
ATOM   1774 C C    . PRO A 1 324 ? 84.74000  125.33700 107.00700 1.000 28.84004  ? 324 PRO A C    1 
ATOM   1775 O O    . PRO A 1 324 ? 84.68600  125.73200 108.17300 1.000 28.86264  ? 324 PRO A O    1 
ATOM   1776 C CB   . PRO A 1 324 ? 82.66700  124.01500 106.44800 1.000 27.20262  ? 324 PRO A CB   1 
ATOM   1777 C CG   . PRO A 1 324 ? 82.21900  122.66300 106.88200 1.000 29.08826  ? 324 PRO A CG   1 
ATOM   1778 C CD   . PRO A 1 324 ? 83.13500  122.29100 108.01500 1.000 27.05094  ? 324 PRO A CD   1 
ATOM   1779 N N    . HIS A 1 325 ? 85.27500  126.05800 106.02200 1.000 26.35803  ? 325 HIS A N    1 
ATOM   1780 C CA   . HIS A 1 325 ? 85.87600  127.36100 106.26900 1.000 23.63935  ? 325 HIS A CA   1 
ATOM   1781 C C    . HIS A 1 325 ? 86.07400  128.08600 104.94500 1.000 21.82855  ? 325 HIS A C    1 
ATOM   1782 O O    . HIS A 1 325 ? 86.52300  127.48800 103.96600 1.000 22.73780  ? 325 HIS A O    1 
ATOM   1783 C CB   . HIS A 1 325 ? 87.22300  127.22600 106.99300 1.000 13.57767  ? 325 HIS A CB   1 
ATOM   1784 C CG   . HIS A 1 325 ? 88.28000  126.55200 106.17600 1.000 21.48421  ? 325 HIS A CG   1 
ATOM   1785 N ND1  . HIS A 1 325 ? 89.28100  127.24800 105.53400 1.000 25.15836  ? 325 HIS A ND1  1 
ATOM   1786 C CD2  . HIS A 1 325 ? 88.49000  125.24500 105.89100 1.000 22.62660  ? 325 HIS A CD2  1 
ATOM   1787 C CE1  . HIS A 1 325 ? 90.06200  126.40000 104.89000 1.000 20.71545  ? 325 HIS A CE1  1 
ATOM   1788 N NE2  . HIS A 1 325 ? 89.60300  125.17800 105.09000 1.000 19.69859  ? 325 HIS A NE2  1 
ATOM   1789 N N    . GLY A 1 326 ? 85.73200  129.37300 104.93100 1.000 29.36572  ? 326 GLY A N    1 
ATOM   1790 C CA   . GLY A 1 326 ? 85.94800  130.22900 103.78900 1.000 27.86945  ? 326 GLY A CA   1 
ATOM   1791 C C    . GLY A 1 326 ? 85.18100  129.83500 102.54300 1.000 36.55516  ? 326 GLY A C    1 
ATOM   1792 O O    . GLY A 1 326 ? 83.96000  129.65400 102.56300 1.000 38.32470  ? 326 GLY A O    1 
ATOM   1793 N N    . PRO A 1 327 ? 85.89600  129.69900 101.42100 1.000 35.82499  ? 327 PRO A N    1 
ATOM   1794 C CA   . PRO A 1 327 ? 85.22800  129.34000 100.16000 1.000 30.07588  ? 327 PRO A CA   1 
ATOM   1795 C C    . PRO A 1 327 ? 84.69700  127.91900 100.12500 1.000 29.91044  ? 327 PRO A C    1 
ATOM   1796 O O    . PRO A 1 327 ? 83.81000  127.63000 99.31300  1.000 35.16782  ? 327 PRO A O    1 
ATOM   1797 C CB   . PRO A 1 327 ? 86.33000  129.54000 99.11100  1.000 29.12760  ? 327 PRO A CB   1 
ATOM   1798 C CG   . PRO A 1 327 ? 87.30700  130.47200 99.75800  1.000 29.11711  ? 327 PRO A CG   1 
ATOM   1799 C CD   . PRO A 1 327 ? 87.29800  130.09000 101.20400 1.000 31.39579  ? 327 PRO A CD   1 
ATOM   1800 N N    . TYR A 1 328 ? 85.20600  127.02700 100.96700 1.000 22.14790  ? 328 TYR A N    1 
ATOM   1801 C CA   . TYR A 1 328 ? 84.78800  125.62800 100.99000 1.000 23.29682  ? 328 TYR A CA   1 
ATOM   1802 C C    . TYR A 1 328 ? 83.81000  125.46500 102.14800 1.000 24.92409  ? 328 TYR A C    1 
ATOM   1803 O O    . TYR A 1 328 ? 84.21700  125.28000 103.29800 1.000 32.41970  ? 328 TYR A O    1 
ATOM   1804 C CB   . TYR A 1 328 ? 86.00200  124.71700 101.13000 1.000 21.23776  ? 328 TYR A CB   1 
ATOM   1805 C CG   . TYR A 1 328 ? 87.26100  125.32200 100.55100 1.000 23.87705  ? 328 TYR A CG   1 
ATOM   1806 C CD1  . TYR A 1 328 ? 87.50500  125.29700 99.18400  1.000 28.48163  ? 328 TYR A CD1  1 
ATOM   1807 C CD2  . TYR A 1 328 ? 88.19800  125.93700 101.36900 1.000 26.39821  ? 328 TYR A CD2  1 
ATOM   1808 C CE1  . TYR A 1 328 ? 88.65200  125.85700 98.65200  1.000 25.88131  ? 328 TYR A CE1  1 
ATOM   1809 C CE2  . TYR A 1 328 ? 89.34600  126.49900 100.84700 1.000 24.22777  ? 328 TYR A CE2  1 
ATOM   1810 C CZ   . TYR A 1 328 ? 89.56900  126.45500 99.48900  1.000 24.94278  ? 328 TYR A CZ   1 
ATOM   1811 O OH   . TYR A 1 328 ? 90.71200  127.01400 98.96900  1.000 24.19604  ? 328 TYR A OH   1 
ATOM   1812 N N    . LYS A 1 329 ? 82.51300  125.52700 101.84100 1.000 36.50914  ? 329 LYS A N    1 
ATOM   1813 C CA   . LYS A 1 329 ? 81.48300  125.56700 102.86800 1.000 40.95948  ? 329 LYS A CA   1 
ATOM   1814 C C    . LYS A 1 329 ? 80.64300  124.30200 102.97400 1.000 42.55807  ? 329 LYS A C    1 
ATOM   1815 O O    . LYS A 1 329 ? 79.95300  124.13000 103.98300 1.000 45.07536  ? 329 LYS A O    1 
ATOM   1816 C CB   . LYS A 1 329 ? 80.54500  126.75900 102.63100 1.000 41.63512  ? 329 LYS A CB   1 
ATOM   1817 C CG   . LYS A 1 329 ? 80.05900  126.88800 101.19700 1.000 43.00855  ? 329 LYS A CG   1 
ATOM   1818 C CD   . LYS A 1 329 ? 79.90400  128.34700 100.80300 1.000 41.89658  ? 329 LYS A CD   1 
ATOM   1819 C CE   . LYS A 1 329 ? 81.24200  129.06700 100.82300 1.000 41.88499  ? 329 LYS A CE   1 
ATOM   1820 N NZ   . LYS A 1 329 ? 81.08400  130.53900 100.66700 1.000 44.74817  ? 329 LYS A NZ   1 
ATOM   1821 N N    . SER A 1 330 ? 80.67300  123.42400 101.97700 1.000 43.70907  ? 330 SER A N    1 
ATOM   1822 C CA   . SER A 1 330 ? 79.92800  122.18200 102.09700 1.000 43.48365  ? 330 SER A CA   1 
ATOM   1823 C C    . SER A 1 330 ? 80.68100  121.19600 102.98700 1.000 43.81876  ? 330 SER A C    1 
ATOM   1824 O O    . SER A 1 330 ? 81.90000  121.27500 103.15800 1.000 46.83797  ? 330 SER A O    1 
ATOM   1825 C CB   . SER A 1 330 ? 79.67500  121.56800 100.72000 1.000 46.35931  ? 330 SER A CB   1 
ATOM   1826 O OG   . SER A 1 330 ? 80.89200  121.23800 100.07500 1.000 49.66550  ? 330 SER A OG   1 
ATOM   1827 N N    . PHE A 1 331 ? 79.93000  120.25400 103.56000 1.000 53.43591  ? 331 PHE A N    1 
ATOM   1828 C CA   . PHE A 1 331 ? 80.52800  119.30600 104.49600 1.000 55.17196  ? 331 PHE A CA   1 
ATOM   1829 C C    . PHE A 1 331 ? 81.44900  118.32600 103.77900 1.000 58.86909  ? 331 PHE A C    1 
ATOM   1830 O O    . PHE A 1 331 ? 82.57200  118.07200 104.22900 1.000 60.07168  ? 331 PHE A O    1 
ATOM   1831 C CB   . PHE A 1 331 ? 79.43300  118.56300 105.26200 1.000 54.87359  ? 331 PHE A CB   1 
ATOM   1832 C CG   . PHE A 1 331 ? 78.61400  119.44700 106.16000 1.000 58.24014  ? 331 PHE A CG   1 
ATOM   1833 C CD1  . PHE A 1 331 ? 79.04700  120.72200 106.48100 1.000 58.50316  ? 331 PHE A CD1  1 
ATOM   1834 C CD2  . PHE A 1 331 ? 77.41200  119.00200 106.68300 1.000 58.85392  ? 331 PHE A CD2  1 
ATOM   1835 C CE1  . PHE A 1 331 ? 78.29700  121.53700 107.30600 1.000 57.23293  ? 331 PHE A CE1  1 
ATOM   1836 C CE2  . PHE A 1 331 ? 76.65700  119.81300 107.50900 1.000 57.51071  ? 331 PHE A CE2  1 
ATOM   1837 C CZ   . PHE A 1 331 ? 77.10100  121.08200 107.82000 1.000 55.99907  ? 331 PHE A CZ   1 
ATOM   1838 N N    . ASN A 1 332 ? 80.99100  117.76400 102.66400 1.000 46.37510  ? 332 ASN A N    1 
ATOM   1839 C CA   . ASN A 1 332 ? 81.79900  116.86800 101.83800 1.000 44.23030  ? 332 ASN A CA   1 
ATOM   1840 C C    . ASN A 1 332 ? 82.27800  117.64400 100.61700 1.000 46.46027  ? 332 ASN A C    1 
ATOM   1841 O O    . ASN A 1 332 ? 81.53000  117.83200 99.65500  1.000 48.32220  ? 332 ASN A O    1 
ATOM   1842 C CB   . ASN A 1 332 ? 80.99900  115.63200 101.43900 1.000 45.14984  ? 332 ASN A CB   1 
ATOM   1843 C CG   . ASN A 1 332 ? 80.60000  114.78800 102.63200 1.000 50.48723  ? 332 ASN A CG   1 
ATOM   1844 O OD1  . ASN A 1 332 ? 81.38100  113.97100 103.11800 1.000 51.17220  ? 332 ASN A OD1  1 
ATOM   1845 N ND2  . ASN A 1 332 ? 79.37700  114.98200 103.11200 1.000 50.42982  ? 332 ASN A ND2  1 
ATOM   1846 N N    . TYR A 1 333 ? 83.52500  118.09600 100.65600 1.000 28.05719  ? 333 TYR A N    1 
ATOM   1847 C CA   . TYR A 1 333 ? 84.04200  118.84500 99.51600  1.000 29.13078  ? 333 TYR A CA   1 
ATOM   1848 C C    . TYR A 1 333 ? 84.72700  117.89800 98.53600  1.000 32.78325  ? 333 TYR A C    1 
ATOM   1849 O O    . TYR A 1 333 ? 85.55600  117.08000 98.95300  1.000 29.34443  ? 333 TYR A O    1 
ATOM   1850 C CB   . TYR A 1 333 ? 85.01600  119.92100 99.97100  1.000 24.44306  ? 333 TYR A CB   1 
ATOM   1851 C CG   . TYR A 1 333 ? 85.13500  121.07800 99.00500  1.000 23.25070  ? 333 TYR A CG   1 
ATOM   1852 C CD1  . TYR A 1 333 ? 84.08700  121.97200 98.83500  1.000 22.92304  ? 333 TYR A CD1  1 
ATOM   1853 C CD2  . TYR A 1 333 ? 86.29400  121.27900 98.26800  1.000 20.18687  ? 333 TYR A CD2  1 
ATOM   1854 C CE1  . TYR A 1 333 ? 84.18500  123.02900 97.95500  1.000 20.94662  ? 333 TYR A CE1  1 
ATOM   1855 C CE2  . TYR A 1 333 ? 86.40300  122.33600 97.38700  1.000 23.28040  ? 333 TYR A CE2  1 
ATOM   1856 C CZ   . TYR A 1 333 ? 85.34500  123.20800 97.23400  1.000 24.42748  ? 333 TYR A CZ   1 
ATOM   1857 O OH   . TYR A 1 333 ? 85.44700  124.26300 96.35800  1.000 28.06455  ? 333 TYR A OH   1 
ATOM   1858 N N    . PRO A 1 334 ? 84.41200  117.98000 97.24100  1.000 25.72230  ? 334 PRO A N    1 
ATOM   1859 C CA   . PRO A 1 334 ? 85.01500  117.06000 96.26500  1.000 16.11111  ? 334 PRO A CA   1 
ATOM   1860 C C    . PRO A 1 334 ? 86.51000  117.26900 96.07300  1.000 18.55970  ? 334 PRO A C    1 
ATOM   1861 O O    . PRO A 1 334 ? 86.93600  117.86800 95.08200  1.000 28.94146  ? 334 PRO A O    1 
ATOM   1862 C CB   . PRO A 1 334 ? 84.24000  117.36600 94.97700  1.000 22.97097  ? 334 PRO A CB   1 
ATOM   1863 C CG   . PRO A 1 334 ? 83.71600  118.75100 95.17400  1.000 20.43450  ? 334 PRO A CG   1 
ATOM   1864 C CD   . PRO A 1 334 ? 83.38600  118.83800 96.62700  1.000 16.62283  ? 334 PRO A CD   1 
ATOM   1865 N N    . TRP A 1 335 ? 87.31400  116.78000 97.01800  1.000 11.06162  ? 335 TRP A N    1 
ATOM   1866 C CA   . TRP A 1 335 ? 88.76400  116.91100 96.93400  1.000 12.28711  ? 335 TRP A CA   1 
ATOM   1867 C C    . TRP A 1 335 ? 89.39600  115.93100 95.95200  1.000 21.95115  ? 335 TRP A C    1 
ATOM   1868 O O    . TRP A 1 335 ? 90.54600  116.13400 95.55000  1.000 25.66510  ? 335 TRP A O    1 
ATOM   1869 C CB   . TRP A 1 335 ? 89.38800  116.70900 98.31900  1.000 15.93346  ? 335 TRP A CB   1 
ATOM   1870 C CG   . TRP A 1 335 ? 89.10800  117.82000 99.29300  1.000 19.51476  ? 335 TRP A CG   1 
ATOM   1871 C CD1  . TRP A 1 335 ? 88.42700  117.72200 100.47100 1.000 20.77668  ? 335 TRP A CD1  1 
ATOM   1872 C CD2  . TRP A 1 335 ? 89.51200  119.19100 99.17800  1.000 21.02756  ? 335 TRP A CD2  1 
ATOM   1873 N NE1  . TRP A 1 335 ? 88.37500  118.94400 101.09300 1.000 17.36101  ? 335 TRP A NE1  1 
ATOM   1874 C CE2  . TRP A 1 335 ? 89.03500  119.86300 100.32100 1.000 17.60239  ? 335 TRP A CE2  1 
ATOM   1875 C CE3  . TRP A 1 335 ? 90.22800  119.91500 98.22000  1.000 22.69372  ? 335 TRP A CE3  1 
ATOM   1876 C CZ2  . TRP A 1 335 ? 89.25000  121.22300 100.53100 1.000 19.39343  ? 335 TRP A CZ2  1 
ATOM   1877 C CZ3  . TRP A 1 335 ? 90.44100  121.26500 98.43100  1.000 15.43811  ? 335 TRP A CZ3  1 
ATOM   1878 C CH2  . TRP A 1 335 ? 89.95300  121.90400 99.57600  1.000 17.60694  ? 335 TRP A CH2  1 
ATOM   1879 N N    . LYS A 1 336 ? 88.67700  114.87500 95.56400  1.000 25.43868  ? 336 LYS A N    1 
ATOM   1880 C CA   . LYS A 1 336 ? 89.21000  113.88700 94.62800  1.000 23.07566  ? 336 LYS A CA   1 
ATOM   1881 C C    . LYS A 1 336 ? 89.28100  114.40300 93.19200  1.000 23.97963  ? 336 LYS A C    1 
ATOM   1882 O O    . LYS A 1 336 ? 90.13200  113.94800 92.41200  1.000 25.54853  ? 336 LYS A O    1 
ATOM   1883 C CB   . LYS A 1 336 ? 88.35900  112.62100 94.69400  1.000 25.68604  ? 336 LYS A CB   1 
ATOM   1884 C CG   . LYS A 1 336 ? 86.91300  112.84600 94.29100  1.000 24.84974  ? 336 LYS A CG   1 
ATOM   1885 C CD   . LYS A 1 336 ? 86.10000  111.56900 94.37100  1.000 29.09466  ? 336 LYS A CD   1 
ATOM   1886 C CE   . LYS A 1 336 ? 84.65800  111.82000 93.96200  1.000 31.74234  ? 336 LYS A CE   1 
ATOM   1887 N NZ   . LYS A 1 336 ? 83.96200  112.73600 94.90800  1.000 31.28001  ? 336 LYS A NZ   1 
ATOM   1888 N N    . ASN A 1 337 ? 88.42000  115.35300 92.81800  1.000 18.30861  ? 337 ASN A N    1 
ATOM   1889 C CA   . ASN A 1 337 ? 88.46600  115.86800 91.45500  1.000 21.82431  ? 337 ASN A CA   1 
ATOM   1890 C C    . ASN A 1 337 ? 89.72100  116.69000 91.20300  1.000 27.02735  ? 337 ASN A C    1 
ATOM   1891 O O    . ASN A 1 337 ? 90.17900  116.78000 90.05300  1.000 36.99335  ? 337 ASN A O    1 
ATOM   1892 C CB   . ASN A 1 337 ? 87.21900  116.70800 91.18100  1.000 23.15330  ? 337 ASN A CB   1 
ATOM   1893 C CG   . ASN A 1 337 ? 86.00300  115.86000 90.86500  1.000 26.57525  ? 337 ASN A CG   1 
ATOM   1894 O OD1  . ASN A 1 337 ? 85.76900  114.83400 91.50000  1.000 27.20997  ? 337 ASN A OD1  1 
ATOM   1895 N ND2  . ASN A 1 337 ? 85.22200  116.28600 89.88200  1.000 25.14988  ? 337 ASN A ND2  1 
ATOM   1896 N N    . TYR A 1 338 ? 90.36100  117.17200 92.26800  1.000 17.85308  ? 338 TYR A N    1 
ATOM   1897 C CA   . TYR A 1 338 ? 91.62000  117.88700 92.11300  1.000 15.67223  ? 338 TYR A CA   1 
ATOM   1898 C C    . TYR A 1 338 ? 92.73300  116.91300 91.75900  1.000 16.61317  ? 338 TYR A C    1 
ATOM   1899 O O    . TYR A 1 338 ? 93.58300  117.20400 90.90700  1.000 22.48177  ? 338 TYR A O    1 
ATOM   1900 C CB   . TYR A 1 338 ? 91.94700  118.62600 93.41200  1.000 17.61013  ? 338 TYR A CB   1 
ATOM   1901 C CG   . TYR A 1 338 ? 91.23600  119.95000 93.58300  1.000 21.30304  ? 338 TYR A CG   1 
ATOM   1902 C CD1  . TYR A 1 338 ? 89.95600  120.00100 94.11900  1.000 14.67117  ? 338 TYR A CD1  1 
ATOM   1903 C CD2  . TYR A 1 338 ? 91.84400  121.14600 93.23000  1.000 19.50516  ? 338 TYR A CD2  1 
ATOM   1904 C CE1  . TYR A 1 338 ? 89.29700  121.19900 94.28800  1.000 12.77431  ? 338 TYR A CE1  1 
ATOM   1905 C CE2  . TYR A 1 338 ? 91.18900  122.35400 93.39500  1.000 13.19981  ? 338 TYR A CE2  1 
ATOM   1906 C CZ   . TYR A 1 338 ? 89.91600  122.37300 93.92500  1.000 18.82421  ? 338 TYR A CZ   1 
ATOM   1907 O OH   . TYR A 1 338 ? 89.25700  123.56800 94.09400  1.000 19.48800  ? 338 TYR A OH   1 
ATOM   1908 N N    . VAL A 1 339 ? 92.69300  115.71600 92.34800  1.000 12.20334  ? 339 VAL A N    1 
ATOM   1909 C CA   . VAL A 1 339 ? 93.67300  114.69000 92.01900  1.000 17.16484  ? 339 VAL A CA   1 
ATOM   1910 C C    . VAL A 1 339 ? 93.40500  114.12500 90.63200  1.000 13.43083  ? 339 VAL A C    1 
ATOM   1911 O O    . VAL A 1 339 ? 94.34200  113.76700 89.90800  1.000 25.87286  ? 339 VAL A O    1 
ATOM   1912 C CB   . VAL A 1 339 ? 93.66000  113.58600 93.09300  1.000 19.33345  ? 339 VAL A CB   1 
ATOM   1913 C CG1  . VAL A 1 339 ? 94.93100  112.75700 93.02300  1.000 19.43797  ? 339 VAL A CG1  1 
ATOM   1914 C CG2  . VAL A 1 339 ? 93.48900  114.19300 94.47500  1.000 16.74112  ? 339 VAL A CG2  1 
ATOM   1915 N N    . LYS A 1 340 ? 92.13800  114.07700 90.21300  1.000 6.25554   ? 340 LYS A N    1 
ATOM   1916 C CA   . LYS A 1 340 ? 91.84600  113.58900 88.86800  1.000 12.02383  ? 340 LYS A CA   1 
ATOM   1917 C C    . LYS A 1 340 ? 92.35900  114.56200 87.80800  1.000 15.78935  ? 340 LYS A C    1 
ATOM   1918 O O    . LYS A 1 340 ? 92.92700  114.14600 86.78200  1.000 22.35236  ? 340 LYS A O    1 
ATOM   1919 C CB   . LYS A 1 340 ? 90.34100  113.36800 88.72000  1.000 10.31390  ? 340 LYS A CB   1 
ATOM   1920 C CG   . LYS A 1 340 ? 89.95400  112.06500 88.04700  1.000 19.20182  ? 340 LYS A CG   1 
ATOM   1921 C CD   . LYS A 1 340 ? 88.54700  112.13800 87.48100  1.000 17.61016  ? 340 LYS A CD   1 
ATOM   1922 C CE   . LYS A 1 340 ? 88.47000  113.09100 86.30300  1.000 21.59263  ? 340 LYS A CE   1 
ATOM   1923 N NZ   . LYS A 1 340 ? 89.20400  112.56300 85.12100  1.000 20.88615  ? 340 LYS A NZ   1 
ATOM   1924 N N    . LEU A 1 341 ? 92.26300  115.86500 88.08600  1.000 7.04982   ? 341 LEU A N    1 
ATOM   1925 C CA   . LEU A 1 341 ? 92.80500  116.83000 87.13700  1.000 10.64934  ? 341 LEU A CA   1 
ATOM   1926 C C    . LEU A 1 341 ? 94.33200  116.83400 87.16300  1.000 10.54832  ? 341 LEU A C    1 
ATOM   1927 O O    . LEU A 1 341 ? 94.97200  116.97200 86.10900  1.000 12.48603  ? 341 LEU A O    1 
ATOM   1928 C CB   . LEU A 1 341 ? 92.24300  118.22000 87.43800  1.000 13.56320  ? 341 LEU A CB   1 
ATOM   1929 C CG   . LEU A 1 341 ? 92.62900  119.38300 86.52400  1.000 15.68282  ? 341 LEU A CG   1 
ATOM   1930 C CD1  . LEU A 1 341 ? 92.09000  119.16200 85.12200  1.000 7.49901   ? 341 LEU A CD1  1 
ATOM   1931 C CD2  . LEU A 1 341 ? 92.11200  120.69100 87.09300  1.000 11.67765  ? 341 LEU A CD2  1 
ATOM   1932 N N    . SER A 1 342 ? 94.93500  116.62900 88.33900  1.000 10.82118  ? 342 SER A N    1 
ATOM   1933 C CA   . SER A 1 342 ? 96.39000  116.52600 88.39000  1.000 16.02136  ? 342 SER A CA   1 
ATOM   1934 C C    . SER A 1 342 ? 96.89300  115.29500 87.64400  1.000 17.61746  ? 342 SER A C    1 
ATOM   1935 O O    . SER A 1 342 ? 97.97200  115.33400 87.03900  1.000 18.47760  ? 342 SER A O    1 
ATOM   1936 C CB   . SER A 1 342 ? 96.86600  116.49500 89.84200  1.000 13.43049  ? 342 SER A CB   1 
ATOM   1937 O OG   . SER A 1 342 ? 96.58200  117.71600 90.49700  1.000 19.16408  ? 342 SER A OG   1 
ATOM   1938 N N    . GLY A 1 343 ? 96.11200  114.21300 87.62400  1.000 8.37995   ? 343 GLY A N    1 
ATOM   1939 C CA   . GLY A 1 343 ? 96.54100  113.03700 86.88500  1.000 4.49821   ? 343 GLY A CA   1 
ATOM   1940 C C    . GLY A 1 343 ? 96.42900  113.23100 85.38600  1.000 12.07134  ? 343 GLY A C    1 
ATOM   1941 O O    . GLY A 1 343 ? 97.30400  112.79700 84.62300  1.000 18.30846  ? 343 GLY A O    1 
ATOM   1942 N N    . ALA A 1 344 ? 95.37500  113.92200 84.94000  1.000 7.66704   ? 344 ALA A N    1 
ATOM   1943 C CA   . ALA A 1 344 ? 95.30200  114.24800 83.51900  1.000 5.30481   ? 344 ALA A CA   1 
ATOM   1944 C C    . ALA A 1 344 ? 96.47000  115.14200 83.10700  1.000 13.51786  ? 344 ALA A C    1 
ATOM   1945 O O    . ALA A 1 344 ? 97.05600  114.97200 82.02400  1.000 15.19423  ? 344 ALA A O    1 
ATOM   1946 C CB   . ALA A 1 344 ? 93.96600  114.91700 83.19800  1.000 5.17140   ? 344 ALA A CB   1 
ATOM   1947 N N    . LEU A 1 345 ? 96.88300  116.04900 83.99800  1.000 15.87899  ? 345 LEU A N    1 
ATOM   1948 C CA   . LEU A 1 345 ? 98.00900  116.91100 83.65500  1.000 12.42712  ? 345 LEU A CA   1 
ATOM   1949 C C    . LEU A 1 345 ? 99.33700  116.15900 83.67900  1.000 14.36263  ? 345 LEU A C    1 
ATOM   1950 O O    . LEU A 1 345 ? 100.24300 116.49200 82.90800  1.000 18.38941  ? 345 LEU A O    1 
ATOM   1951 C CB   . LEU A 1 345 ? 98.05900  118.10800 84.60300  1.000 14.44979  ? 345 LEU A CB   1 
ATOM   1952 C CG   . LEU A 1 345 ? 99.00400  119.24800 84.22000  1.000 12.76909  ? 345 LEU A CG   1 
ATOM   1953 C CD1  . LEU A 1 345 ? 98.47900  120.00900 83.01500  1.000 16.16472  ? 345 LEU A CD1  1 
ATOM   1954 C CD2  . LEU A 1 345 ? 99.20500  120.18200 85.39700  1.000 15.52444  ? 345 LEU A CD2  1 
ATOM   1955 N N    . LYS A 1 346 ? 99.47400  115.13400 84.52300  1.000 13.67843  ? 346 LYS A N    1 
ATOM   1956 C CA   . LYS A 1 346 ? 100.70500 114.34500 84.49300  1.000 10.85057  ? 346 LYS A CA   1 
ATOM   1957 C C    . LYS A 1 346 ? 100.79600 113.53200 83.20500  1.000 13.68277  ? 346 LYS A C    1 
ATOM   1958 O O    . LYS A 1 346 ? 101.87800 113.40500 82.59800  1.000 9.96151   ? 346 LYS A O    1 
ATOM   1959 C CB   . LYS A 1 346 ? 100.75900 113.42500 85.71100  1.000 12.69341  ? 346 LYS A CB   1 
ATOM   1960 C CG   . LYS A 1 346 ? 101.28200 114.09200 86.96400  1.000 22.92705  ? 346 LYS A CG   1 
ATOM   1961 C CD   . LYS A 1 346 ? 101.25600 113.13900 88.14600  1.000 27.41235  ? 346 LYS A CD   1 
ATOM   1962 C CE   . LYS A 1 346 ? 101.23000 113.89800 89.46300  1.000 24.29809  ? 346 LYS A CE   1 
ATOM   1963 N NZ   . LYS A 1 346 ? 101.24700 115.37200 89.25600  1.000 17.10008  ? 346 LYS A NZ   1 
ATOM   1964 N N    . HIS A 1 347 ? 99.65200  113.01400 82.74800  1.000 14.20353  ? 347 HIS A N    1 
ATOM   1965 C CA   . HIS A 1 347 ? 99.64000  112.30700 81.47500  1.000 12.90017  ? 347 HIS A CA   1 
ATOM   1966 C C    . HIS A 1 347 ? 100.03500 113.23900 80.34200  1.000 14.94184  ? 347 HIS A C    1 
ATOM   1967 O O    . HIS A 1 347 ? 100.72700 112.83100 79.40300  1.000 7.74371   ? 347 HIS A O    1 
ATOM   1968 C CB   . HIS A 1 347 ? 98.26700  111.69700 81.20600  1.000 10.86460  ? 347 HIS A CB   1 
ATOM   1969 C CG   . HIS A 1 347 ? 98.28600  110.61700 80.16900  1.000 15.92133  ? 347 HIS A CG   1 
ATOM   1970 N ND1  . HIS A 1 347 ? 97.53000  110.67700 79.01800  1.000 16.28347  ? 347 HIS A ND1  1 
ATOM   1971 C CD2  . HIS A 1 347 ? 98.97900  109.45500 80.10300  1.000 18.26437  ? 347 HIS A CD2  1 
ATOM   1972 C CE1  . HIS A 1 347 ? 97.75300  109.59700 78.29100  1.000 17.97707  ? 347 HIS A CE1  1 
ATOM   1973 N NE2  . HIS A 1 347 ? 98.62700  108.84000 78.92700  1.000 18.19893  ? 347 HIS A NE2  1 
ATOM   1974 N N    . CYS A 1 348 ? 99.60300  114.50000 80.41100  1.000 18.88377  ? 348 CYS A N    1 
ATOM   1975 C CA   . CYS A 1 348 ? 100.03700 115.45000 79.39100  1.000 17.09208  ? 348 CYS A CA   1 
ATOM   1976 C C    . CYS A 1 348 ? 101.52200 115.80600 79.51900  1.000 21.64384  ? 348 CYS A C    1 
ATOM   1977 O O    . CYS A 1 348 ? 102.19000 116.02000 78.50200  1.000 19.96901  ? 348 CYS A O    1 
ATOM   1978 C CB   . CYS A 1 348 ? 99.17300  116.70900 79.45700  1.000 19.74897  ? 348 CYS A CB   1 
ATOM   1979 S SG   . CYS A 1 348 ? 99.53300  117.94200 78.19600  1.000 34.25793  ? 348 CYS A SG   1 
ATOM   1980 N N    . ALA A 1 349 ? 102.05600 115.86700 80.74300  1.000 22.97273  ? 349 ALA A N    1 
ATOM   1981 C CA   . ALA A 1 349 ? 103.45700 116.23300 80.96300  1.000 14.35406  ? 349 ALA A CA   1 
ATOM   1982 C C    . ALA A 1 349 ? 104.45500 115.13700 80.59700  1.000 22.66072  ? 349 ALA A C    1 
ATOM   1983 O O    . ALA A 1 349 ? 105.65600 115.42700 80.46300  1.000 26.71166  ? 349 ALA A O    1 
ATOM   1984 C CB   . ALA A 1 349 ? 103.66700 116.63800 82.42300  1.000 12.74395  ? 349 ALA A CB   1 
ATOM   1985 N N    . PHE A 1 350 ? 104.00500 113.89900 80.38900  1.000 21.22786  ? 350 PHE A N    1 
ATOM   1986 C CA   . PHE A 1 350 ? 104.98300 112.88800 79.97700  1.000 13.49673  ? 350 PHE A CA   1 
ATOM   1987 C C    . PHE A 1 350 ? 105.50600 113.13200 78.55800  1.000 19.42649  ? 350 PHE A C    1 
ATOM   1988 O O    . PHE A 1 350 ? 106.69300 112.89100 78.28200  1.000 18.75950  ? 350 PHE A O    1 
ATOM   1989 C CB   . PHE A 1 350 ? 104.37900 111.48700 80.07200  1.000 20.31409  ? 350 PHE A CB   1 
ATOM   1990 C CG   . PHE A 1 350 ? 104.35500 110.92600 81.46400  1.000 20.57535  ? 350 PHE A CG   1 
ATOM   1991 C CD1  . PHE A 1 350 ? 105.44600 111.06900 82.30200  1.000 22.60889  ? 350 PHE A CD1  1 
ATOM   1992 C CD2  . PHE A 1 350 ? 103.24500 110.24400 81.93200  1.000 21.44844  ? 350 PHE A CD2  1 
ATOM   1993 C CE1  . PHE A 1 350 ? 105.42900 110.55100 83.58100  1.000 21.46119  ? 350 PHE A CE1  1 
ATOM   1994 C CE2  . PHE A 1 350 ? 103.22200 109.72400 83.21100  1.000 18.77148  ? 350 PHE A CE2  1 
ATOM   1995 C CZ   . PHE A 1 350 ? 104.31600 109.87700 84.03500  1.000 15.19219  ? 350 PHE A CZ   1 
ATOM   1996 N N    . THR A 1 351 ? 104.66900 113.65200 77.65700  1.000 12.01864  ? 351 THR A N    1 
ATOM   1997 C CA   . THR A 1 351 ? 105.17400 113.99100 76.33100  1.000 10.72172  ? 351 THR A CA   1 
ATOM   1998 C C    . THR A 1 351 ? 106.16000 115.15100 76.39100  1.000 10.09253  ? 351 THR A C    1 
ATOM   1999 O O    . THR A 1 351 ? 107.09400 115.21600 75.58200  1.000 13.55571  ? 351 THR A O    1 
ATOM   2000 C CB   . THR A 1 351 ? 104.01700 114.32600 75.38900  1.000 16.64652  ? 351 THR A CB   1 
ATOM   2001 O OG1  . THR A 1 351 ? 102.92000 113.44100 75.64400  1.000 19.18781  ? 351 THR A OG1  1 
ATOM   2002 C CG2  . THR A 1 351 ? 104.45100 114.17200 73.94000  1.000 14.18102  ? 351 THR A CG2  1 
ATOM   2003 N N    . VAL A 1 352 ? 105.99700 116.05400 77.36000  1.000 19.50265  ? 352 VAL A N    1 
ATOM   2004 C CA   . VAL A 1 352 ? 106.95100 117.14700 77.49700  1.000 20.37578  ? 352 VAL A CA   1 
ATOM   2005 C C    . VAL A 1 352 ? 108.27500 116.61800 78.02000  1.000 13.62233  ? 352 VAL A C    1 
ATOM   2006 O O    . VAL A 1 352 ? 109.34800 117.09100 77.61900  1.000 18.57877  ? 352 VAL A O    1 
ATOM   2007 C CB   . VAL A 1 352 ? 106.38100 118.25100 78.40800  1.000 20.93709  ? 352 VAL A CB   1 
ATOM   2008 C CG1  . VAL A 1 352 ? 107.28200 119.47500 78.38600  1.000 14.33855  ? 352 VAL A CG1  1 
ATOM   2009 C CG2  . VAL A 1 352 ? 104.97000 118.61500 77.97900  1.000 18.17598  ? 352 VAL A CG2  1 
ATOM   2010 N N    . MET A 1 353 ? 108.23200 115.60900 78.89300  1.000 20.10701  ? 353 MET A N    1 
ATOM   2011 C CA   . MET A 1 353 ? 109.48500 114.98500 79.30900  1.000 16.23675  ? 353 MET A CA   1 
ATOM   2012 C C    . MET A 1 353 ? 110.16800 114.27000 78.14700  1.000 20.24079  ? 353 MET A C    1 
ATOM   2013 O O    . MET A 1 353 ? 111.40200 114.29000 78.04300  1.000 20.74618  ? 353 MET A O    1 
ATOM   2014 C CB   . MET A 1 353 ? 109.23400 114.00600 80.45300  1.000 16.22671  ? 353 MET A CB   1 
ATOM   2015 C CG   . MET A 1 353 ? 110.38900 113.05400 80.71300  1.000 20.66170  ? 353 MET A CG   1 
ATOM   2016 S SD   . MET A 1 353 ? 110.39500 112.39800 82.38900  1.000 46.73237  ? 353 MET A SD   1 
ATOM   2017 C CE   . MET A 1 353 ? 108.82900 111.53200 82.41700  1.000 28.52355  ? 353 MET A CE   1 
ATOM   2018 N N    . ALA A 1 354 ? 109.39200 113.70700 77.21800  1.000 23.62192  ? 354 ALA A N    1 
ATOM   2019 C CA   . ALA A 1 354 ? 110.03000 113.05400 76.07600  1.000 10.66562  ? 354 ALA A CA   1 
ATOM   2020 C C    . ALA A 1 354 ? 110.55800 114.06500 75.06200  1.000 18.05592  ? 354 ALA A C    1 
ATOM   2021 O O    . ALA A 1 354 ? 111.57700 113.81300 74.40000  1.000 15.31253  ? 354 ALA A O    1 
ATOM   2022 C CB   . ALA A 1 354 ? 109.05100 112.09300 75.40200  1.000 12.60741  ? 354 ALA A CB   1 
ATOM   2023 N N    . LEU A 1 355 ? 109.95800 115.25400 75.00300  1.000 19.49426  ? 355 LEU A N    1 
ATOM   2024 C CA   . LEU A 1 355 ? 110.50600 116.28000 74.12600  1.000 15.37854  ? 355 LEU A CA   1 
ATOM   2025 C C    . LEU A 1 355 ? 111.76000 116.89400 74.72600  1.000 16.54433  ? 355 LEU A C    1 
ATOM   2026 O O    . LEU A 1 355 ? 112.66200 117.30000 73.98500  1.000 12.28383  ? 355 LEU A O    1 
ATOM   2027 C CB   . LEU A 1 355 ? 109.46800 117.36800 73.84700  1.000 19.14932  ? 355 LEU A CB   1 
ATOM   2028 C CG   . LEU A 1 355 ? 108.34400 117.01000 72.87600  1.000 22.16508  ? 355 LEU A CG   1 
ATOM   2029 C CD1  . LEU A 1 355 ? 107.13500 117.90100 73.10200  1.000 18.13174  ? 355 LEU A CD1  1 
ATOM   2030 C CD2  . LEU A 1 355 ? 108.83400 117.11800 71.44100  1.000 14.50300  ? 355 LEU A CD2  1 
ATOM   2031 N N    . HIS A 1 356 ? 111.83700 116.97300 76.05600  1.000 28.56432  ? 356 HIS A N    1 
ATOM   2032 C CA   . HIS A 1 356 ? 113.09300 117.37600 76.67700  1.000 23.79819  ? 356 HIS A CA   1 
ATOM   2033 C C    . HIS A 1 356 ? 114.17400 116.33100 76.43800  1.000 25.38451  ? 356 HIS A C    1 
ATOM   2034 O O    . HIS A 1 356 ? 115.33900 116.67500 76.20900  1.000 28.94312  ? 356 HIS A O    1 
ATOM   2035 C CB   . HIS A 1 356 ? 112.90800 117.60500 78.17400  1.000 27.43403  ? 356 HIS A CB   1 
ATOM   2036 C CG   . HIS A 1 356 ? 114.16200 118.03000 78.87400  1.000 31.46406  ? 356 HIS A CG   1 
ATOM   2037 N ND1  . HIS A 1 356 ? 114.45300 117.66300 80.17000  1.000 32.02478  ? 356 HIS A ND1  1 
ATOM   2038 C CD2  . HIS A 1 356 ? 115.20800 118.77900 78.45200  1.000 30.93283  ? 356 HIS A CD2  1 
ATOM   2039 C CE1  . HIS A 1 356 ? 115.62100 118.17300 80.51800  1.000 31.75957  ? 356 HIS A CE1  1 
ATOM   2040 N NE2  . HIS A 1 356 ? 116.10000 118.85500 79.49400  1.000 26.90099  ? 356 HIS A NE2  1 
ATOM   2041 N N    . GLY A 1 357 ? 113.80700 115.04800 76.48200  1.000 22.81635  ? 357 GLY A N    1 
ATOM   2042 C CA   . GLY A 1 357 ? 114.77300 114.00400 76.18800  1.000 17.75673  ? 357 GLY A CA   1 
ATOM   2043 C C    . GLY A 1 357 ? 115.26400 114.01200 74.75400  1.000 21.88328  ? 357 GLY A C    1 
ATOM   2044 O O    . GLY A 1 357 ? 116.38900 113.58400 74.48000  1.000 21.49023  ? 357 GLY A O    1 
ATOM   2045 N N    . CYS A 1 358 ? 114.43900 114.49300 73.82000  1.000 37.71563  ? 358 CYS A N    1 
ATOM   2046 C CA   . CYS A 1 358 ? 114.88900 114.59200 72.43200  1.000 25.66887  ? 358 CYS A CA   1 
ATOM   2047 C C    . CYS A 1 358 ? 116.05000 115.56700 72.24800  1.000 24.62119  ? 358 CYS A C    1 
ATOM   2048 O O    . CYS A 1 358 ? 116.77800 115.46300 71.25600  1.000 27.34968  ? 358 CYS A O    1 
ATOM   2049 C CB   . CYS A 1 358 ? 113.73500 115.01100 71.51900  1.000 27.12428  ? 358 CYS A CB   1 
ATOM   2050 S SG   . CYS A 1 358 ? 112.68000 113.66100 70.95400  1.000 41.99595  ? 358 CYS A SG   1 
ATOM   2051 N N    . ILE A 1 359 ? 116.23800 116.51300 73.17000  1.000 30.64312  ? 359 ILE A N    1 
ATOM   2052 C CA   . ILE A 1 359 ? 117.32500 117.48200 73.04900  1.000 29.34115  ? 359 ILE A CA   1 
ATOM   2053 C C    . ILE A 1 359 ? 118.65600 116.96200 73.58600  1.000 30.60544  ? 359 ILE A C    1 
ATOM   2054 O O    . ILE A 1 359 ? 119.70500 117.54600 73.28600  1.000 27.12120  ? 359 ILE A O    1 
ATOM   2055 C CB   . ILE A 1 359 ? 116.95700 118.80000 73.75200  1.000 31.87022  ? 359 ILE A CB   1 
ATOM   2056 C CG1  . ILE A 1 359 ? 115.70000 119.40600 73.12600  1.000 29.55976  ? 359 ILE A CG1  1 
ATOM   2057 C CG2  . ILE A 1 359 ? 118.10900 119.79000 73.69200  1.000 29.28310  ? 359 ILE A CG2  1 
ATOM   2058 C CD1  . ILE A 1 359 ? 115.14200 120.58000 73.89900  1.000 25.24436  ? 359 ILE A CD1  1 
ATOM   2059 N N    . LEU A 1 360 ? 118.65100 115.87700 74.35900  1.000 35.35812  ? 360 LEU A N    1 
ATOM   2060 C CA   . LEU A 1 360 ? 119.85800 115.33100 74.96800  1.000 29.45036  ? 360 LEU A CA   1 
ATOM   2061 C C    . LEU A 1 360 ? 120.25900 113.99600 74.34700  1.000 28.43134  ? 360 LEU A C    1 
ATOM   2062 O O    . LEU A 1 360 ? 120.86100 113.15100 75.01400  1.000 32.87168  ? 360 LEU A O    1 
ATOM   2063 C CB   . LEU A 1 360 ? 119.66700 115.17000 76.47600  1.000 30.27951  ? 360 LEU A CB   1 
ATOM   2064 C CG   . LEU A 1 360 ? 119.34800 116.41800 77.29900  1.000 30.07347  ? 360 LEU A CG   1 
ATOM   2065 C CD1  . LEU A 1 360 ? 118.91900 116.02700 78.70300  1.000 26.44732  ? 360 LEU A CD1  1 
ATOM   2066 C CD2  . LEU A 1 360 ? 120.54400 117.35100 77.34300  1.000 29.70976  ? 360 LEU A CD2  1 
ATOM   2067 N N    . SER A 1 361 ? 119.94100 113.79800 73.07400  1.000 34.12732  ? 361 SER A N    1 
ATOM   2068 C CA   . SER A 1 361 ? 120.22400 112.54500 72.39300  1.000 35.74344  ? 361 SER A CA   1 
ATOM   2069 C C    . SER A 1 361 ? 121.56500 112.59800 71.66900  1.000 34.86749  ? 361 SER A C    1 
ATOM   2070 O O    . SER A 1 361 ? 122.08600 113.66700 71.34300  1.000 36.94547  ? 361 SER A O    1 
ATOM   2071 C CB   . SER A 1 361 ? 119.11100 112.21900 71.39800  1.000 36.83459  ? 361 SER A CB   1 
ATOM   2072 O OG   . SER A 1 361 ? 117.89800 111.92300 72.06700  1.000 38.20552  ? 361 SER A OG   1 
ATOM   2073 N N    . GLU A 1 362 ? 122.12400 111.41000 71.42300  1.000 42.04669  ? 362 GLU A N    1 
ATOM   2074 C CA   . GLU A 1 362 ? 123.42200 111.31600 70.76100  1.000 39.98437  ? 362 GLU A CA   1 
ATOM   2075 C C    . GLU A 1 362 ? 123.32100 111.61200 69.27000  1.000 42.73541  ? 362 GLU A C    1 
ATOM   2076 O O    . GLU A 1 362 ? 124.24600 112.18900 68.68900  1.000 44.15720  ? 362 GLU A O    1 
ATOM   2077 C CB   . GLU A 1 362 ? 124.01800 109.92300 70.97700  1.000 39.53215  ? 362 GLU A CB   1 
ATOM   2078 C CG   . GLU A 1 362 ? 123.98400 109.44300 72.41800  1.000 40.74402  ? 362 GLU A CG   1 
ATOM   2079 C CD   . GLU A 1 362 ? 125.33300 109.53300 73.09100  1.000 44.08649  ? 362 GLU A CD   1 
ATOM   2080 O OE1  . GLU A 1 362 ? 126.35900 109.42400 72.39000  1.000 47.43648  ? 362 GLU A OE1  1 
ATOM   2081 O OE2  . GLU A 1 362 ? 125.36900 109.71800 74.32300  1.000 45.00804  ? 362 GLU A OE2  1 
ATOM   2082 N N    . ILE A 1 363 ? 122.21700 111.22500 68.64100  1.000 43.64858  ? 363 ILE A N    1 
ATOM   2083 C CA   . ILE A 1 363 ? 121.96500 111.49200 67.23000  1.000 41.91788  ? 363 ILE A CA   1 
ATOM   2084 C C    . ILE A 1 363 ? 121.13500 112.76300 67.11500  1.000 42.18082  ? 363 ILE A C    1 
ATOM   2085 O O    . ILE A 1 363 ? 120.04600 112.85700 67.69400  1.000 42.62246  ? 363 ILE A O    1 
ATOM   2086 C CB   . ILE A 1 363 ? 121.26000 110.30600 66.55400  1.000 41.92600  ? 363 ILE A CB   1 
ATOM   2087 C CG1  . ILE A 1 363 ? 122.10500 109.03600 66.68900  1.000 41.31773  ? 363 ILE A CG1  1 
ATOM   2088 C CG2  . ILE A 1 363 ? 120.98600 110.61300 65.09200  1.000 40.07528  ? 363 ILE A CG2  1 
ATOM   2089 C CD1  . ILE A 1 363 ? 121.39300 107.89600 67.38000  1.000 40.72612  ? 363 ILE A CD1  1 
ATOM   2090 N N    . GLN A 1 364 ? 121.65000 113.74100 66.37400  1.000 46.22900  ? 364 GLN A N    1 
ATOM   2091 C CA   . GLN A 1 364 ? 120.98200 115.02000 66.18300  1.000 42.64755  ? 364 GLN A CA   1 
ATOM   2092 C C    . GLN A 1 364 ? 120.95200 115.35600 64.69900  1.000 42.67761  ? 364 GLN A C    1 
ATOM   2093 O O    . GLN A 1 364 ? 121.73500 114.82900 63.90500  1.000 45.32429  ? 364 GLN A O    1 
ATOM   2094 C CB   . GLN A 1 364 ? 121.67800 116.14300 66.96500  1.000 40.28342  ? 364 GLN A CB   1 
ATOM   2095 C CG   . GLN A 1 364 ? 122.11600 115.74500 68.36400  1.000 44.37614  ? 364 GLN A CG   1 
ATOM   2096 C CD   . GLN A 1 364 ? 121.37000 116.49800 69.44600  1.000 44.43954  ? 364 GLN A CD   1 
ATOM   2097 O OE1  . GLN A 1 364 ? 120.43500 117.24600 69.16600  1.000 47.27089  ? 364 GLN A OE1  1 
ATOM   2098 N NE2  . GLN A 1 364 ? 121.78300 116.30400 70.69200  1.000 43.53424  ? 364 GLN A NE2  1 
ATOM   2099 N N    . ALA A 1 365 ? 120.02500 116.25600 64.32700  1.000 46.32249  ? 365 ALA A N    1 
ATOM   2100 C CA   . ALA A 1 365 ? 119.82600 116.59500 62.92600  1.000 44.93869  ? 365 ALA A CA   1 
ATOM   2101 C C    . ALA A 1 365 ? 120.63900 117.82400 62.52700  1.000 47.81091  ? 365 ALA A C    1 
ATOM   2102 O O    . ALA A 1 365 ? 120.97600 118.65800 63.37300  1.000 46.83426  ? 365 ALA A O    1 
ATOM   2103 C CB   . ALA A 1 365 ? 118.34900 116.85100 62.64600  1.000 42.92240  ? 365 ALA A CB   1 
ATOM   2104 N N    . PRO A 1 366 ? 120.96600 117.93800 61.24000  1.000 53.66914  ? 366 PRO A N    1 
ATOM   2105 C CA   . PRO A 1 366 ? 121.68000 119.12800 60.76000  1.000 52.57688  ? 366 PRO A CA   1 
ATOM   2106 C C    . PRO A 1 366 ? 120.90700 120.40300 61.06700  1.000 53.57772  ? 366 PRO A C    1 
ATOM   2107 O O    . PRO A 1 366 ? 119.68400 120.46000 60.93100  1.000 55.00598  ? 366 PRO A O    1 
ATOM   2108 C CB   . PRO A 1 366 ? 121.79900 118.88900 59.24900  1.000 50.44693  ? 366 PRO A CB   1 
ATOM   2109 C CG   . PRO A 1 366 ? 120.85100 117.76500 58.94200  1.000 51.17427  ? 366 PRO A CG   1 
ATOM   2110 C CD   . PRO A 1 366 ? 120.78300 116.93900 60.17800  1.000 50.99121  ? 366 PRO A CD   1 
ATOM   2111 N N    . GLU A 1 367 ? 121.64300 121.43500 61.48500  1.000 53.41041  ? 367 GLU A N    1 
ATOM   2112 C CA   . GLU A 1 367 ? 121.00700 122.68000 61.90500  1.000 54.61458  ? 367 GLU A CA   1 
ATOM   2113 C C    . GLU A 1 367 ? 120.27700 123.35900 60.75200  1.000 55.74612  ? 367 GLU A C    1 
ATOM   2114 O O    . GLU A 1 367 ? 119.20700 123.94700 60.94800  1.000 52.72198  ? 367 GLU A O    1 
ATOM   2115 C CB   . GLU A 1 367 ? 122.04900 123.62400 62.50100  1.000 54.49179  ? 367 GLU A CB   1 
ATOM   2116 C CG   . GLU A 1 367 ? 121.50800 124.99900 62.85300  1.000 54.79401  ? 367 GLU A CG   1 
ATOM   2117 C CD   . GLU A 1 367 ? 122.56300 125.90500 63.45500  1.000 57.27556  ? 367 GLU A CD   1 
ATOM   2118 O OE1  . GLU A 1 367 ? 123.65800 125.40600 63.78800  1.000 58.42989  ? 367 GLU A OE1  1 
ATOM   2119 O OE2  . GLU A 1 367 ? 122.29900 127.11800 63.59200  1.000 56.27320  ? 367 GLU A OE2  1 
ATOM   2120 N N    . GLU A 1 368 ? 120.83800 123.29400 59.54300  1.000 57.38403  ? 368 GLU A N    1 
ATOM   2121 C CA   . GLU A 1 368 ? 120.22500 123.97300 58.40700  1.000 55.46447  ? 368 GLU A CA   1 
ATOM   2122 C C    . GLU A 1 368 ? 118.86600 123.39300 58.03800  1.000 55.87440  ? 368 GLU A C    1 
ATOM   2123 O O    . GLU A 1 368 ? 118.06000 124.09300 57.41500  1.000 56.63660  ? 368 GLU A O    1 
ATOM   2124 C CB   . GLU A 1 368 ? 121.16000 123.91900 57.19800  1.000 55.21212  ? 368 GLU A CB   1 
ATOM   2125 C CG   . GLU A 1 368 ? 121.11200 122.60800 56.43400  1.000 56.43382  ? 368 GLU A CG   1 
ATOM   2126 C CD   . GLU A 1 368 ? 122.09500 121.58700 56.96900  1.000 57.43553  ? 368 GLU A CD   1 
ATOM   2127 O OE1  . GLU A 1 368 ? 122.98000 121.97200 57.76000  1.000 56.32211  ? 368 GLU A OE1  1 
ATOM   2128 O OE2  . GLU A 1 368 ? 121.98000 120.40000 56.59900  1.000 57.29071  ? 368 GLU A OE2  1 
ATOM   2129 N N    . ARG A 1 369 ? 118.59200 122.14000 58.39800  1.000 52.59679  ? 369 ARG A N    1 
ATOM   2130 C CA   . ARG A 1 369 ? 117.31500 121.51700 58.07400  1.000 52.45631  ? 369 ARG A CA   1 
ATOM   2131 C C    . ARG A 1 369 ? 116.23800 121.77800 59.11800  1.000 52.32538  ? 369 ARG A C    1 
ATOM   2132 O O    . ARG A 1 369 ? 115.05000 121.61700 58.81400  1.000 50.87039  ? 369 ARG A O    1 
ATOM   2133 C CB   . ARG A 1 369 ? 117.49400 120.00800 57.88500  1.000 50.64415  ? 369 ARG A CB   1 
ATOM   2134 C CG   . ARG A 1 369 ? 118.40800 119.65000 56.72800  1.000 50.84186  ? 369 ARG A CG   1 
ATOM   2135 C CD   . ARG A 1 369 ? 118.06500 118.29400 56.13800  1.000 51.92070  ? 369 ARG A CD   1 
ATOM   2136 N NE   . ARG A 1 369 ? 119.26200 117.53700 55.79500  1.000 54.45188  ? 369 ARG A NE   1 
ATOM   2137 C CZ   . ARG A 1 369 ? 119.25900 116.37200 55.16300  1.000 54.24588  ? 369 ARG A CZ   1 
ATOM   2138 N NH1  . ARG A 1 369 ? 118.13000 115.79200 54.78900  1.000 51.79117  ? 369 ARG A NH1  1 
ATOM   2139 N NH2  . ARG A 1 369 ? 120.41700 115.77300 54.90000  1.000 52.74336  ? 369 ARG A NH2  1 
ATOM   2140 N N    . ARG A 1 370 ? 116.61800 122.17300 60.33400  1.000 41.11900  ? 370 ARG A N    1 
ATOM   2141 C CA   . ARG A 1 370 ? 115.65000 122.47600 61.38000  1.000 41.98581  ? 370 ARG A CA   1 
ATOM   2142 C C    . ARG A 1 370 ? 115.02100 123.85400 61.23000  1.000 44.20552  ? 370 ARG A C    1 
ATOM   2143 O O    . ARG A 1 370 ? 114.04000 124.14500 61.92200  1.000 45.48406  ? 370 ARG A O    1 
ATOM   2144 C CB   . ARG A 1 370 ? 116.30700 122.36600 62.76000  1.000 42.30581  ? 370 ARG A CB   1 
ATOM   2145 C CG   . ARG A 1 370 ? 116.58200 120.94000 63.20900  1.000 41.43061  ? 370 ARG A CG   1 
ATOM   2146 C CD   . ARG A 1 370 ? 117.94500 120.81500 63.86900  1.000 39.30071  ? 370 ARG A CD   1 
ATOM   2147 N NE   . ARG A 1 370 ? 117.94000 121.32100 65.23600  1.000 42.76327  ? 370 ARG A NE   1 
ATOM   2148 C CZ   . ARG A 1 370 ? 118.47800 120.69000 66.27000  1.000 40.70302  ? 370 ARG A CZ   1 
ATOM   2149 N NH1  . ARG A 1 370 ? 119.07700 119.51900 66.13000  1.000 36.89191  ? 370 ARG A NH1  1 
ATOM   2150 N NH2  . ARG A 1 370 ? 118.41500 121.24800 67.47500  1.000 38.11834  ? 370 ARG A NH2  1 
ATOM   2151 N N    . GLN A 1 371 ? 115.55200 124.70200 60.35300  1.000 49.39764  ? 371 GLN A N    1 
ATOM   2152 C CA   . GLN A 1 371 ? 115.05900 126.06200 60.18400  1.000 48.21801  ? 371 GLN A CA   1 
ATOM   2153 C C    . GLN A 1 371 ? 113.95700 126.17300 59.13800  1.000 49.83770  ? 371 GLN A C    1 
ATOM   2154 O O    . GLN A 1 371 ? 113.51300 127.28700 58.84300  1.000 52.34268  ? 371 GLN A O    1 
ATOM   2155 C CB   . GLN A 1 371 ? 116.21500 126.99600 59.81100  1.000 47.00528  ? 371 GLN A CB   1 
ATOM   2156 C CG   . GLN A 1 371 ? 117.31600 127.06500 60.85500  1.000 49.31186  ? 371 GLN A CG   1 
ATOM   2157 C CD   . GLN A 1 371 ? 116.80900 127.51600 62.21000  1.000 51.82769  ? 371 GLN A CD   1 
ATOM   2158 O OE1  . GLN A 1 371 ? 115.84000 128.26800 62.30300  1.000 53.40315  ? 371 GLN A OE1  1 
ATOM   2159 N NE2  . GLN A 1 371 ? 117.46400 127.05700 63.27000  1.000 49.92059  ? 371 GLN A NE2  1 
ATOM   2160 N N    . VAL A 1 372 ? 113.50900 125.05300 58.57100  1.000 47.79607  ? 372 VAL A N    1 
ATOM   2161 C CA   . VAL A 1 372 ? 112.42100 125.07800 57.59900  1.000 47.35998  ? 372 VAL A CA   1 
ATOM   2162 C C    . VAL A 1 372 ? 111.03900 125.01800 58.24400  1.000 47.87998  ? 372 VAL A C    1 
ATOM   2163 O O    . VAL A 1 372 ? 110.05300 125.42200 57.61200  1.000 50.57939  ? 372 VAL A O    1 
ATOM   2164 C CB   . VAL A 1 372 ? 112.58000 123.92100 56.59500  1.000 45.95645  ? 372 VAL A CB   1 
ATOM   2165 C CG1  . VAL A 1 372 ? 111.34300 123.78800 55.72400  1.000 48.23448  ? 372 VAL A CG1  1 
ATOM   2166 C CG2  . VAL A 1 372 ? 113.81800 124.12900 55.73900  1.000 45.72394  ? 372 VAL A CG2  1 
ATOM   2167 N N    . PHE A 1 373 ? 110.93700 124.53500 59.48500  1.000 44.54049  ? 373 PHE A N    1 
ATOM   2168 C CA   . PHE A 1 373 ? 109.65900 124.37000 60.17000  1.000 46.37582  ? 373 PHE A CA   1 
ATOM   2169 C C    . PHE A 1 373 ? 109.54600 125.25000 61.41300  1.000 49.15032  ? 373 PHE A C    1 
ATOM   2170 O O    . PHE A 1 373 ? 108.67200 125.01700 62.25400  1.000 52.15730  ? 373 PHE A O    1 
ATOM   2171 C CB   . PHE A 1 373 ? 109.44800 122.90200 60.55000  1.000 49.44336  ? 373 PHE A CB   1 
ATOM   2172 C CG   . PHE A 1 373 ? 109.78700 121.93300 59.45200  1.000 48.98864  ? 373 PHE A CG   1 
ATOM   2173 C CD1  . PHE A 1 373 ? 111.08000 121.45800 59.30500  1.000 47.20414  ? 373 PHE A CD1  1 
ATOM   2174 C CD2  . PHE A 1 373 ? 108.81300 121.48900 58.57300  1.000 48.15319  ? 373 PHE A CD2  1 
ATOM   2175 C CE1  . PHE A 1 373 ? 111.39700 120.56400 58.29900  1.000 45.61972  ? 373 PHE A CE1  1 
ATOM   2176 C CE2  . PHE A 1 373 ? 109.12400 120.59500 57.56600  1.000 46.80448  ? 373 PHE A CE2  1 
ATOM   2177 C CZ   . PHE A 1 373 ? 110.41800 120.13200 57.43000  1.000 47.11615  ? 373 PHE A CZ   1 
ATOM   2178 N N    . ARG A 1 374 ? 110.41300 126.25400 61.54800  1.000 47.93416  ? 374 ARG A N    1 
ATOM   2179 C CA   . ARG A 1 374 ? 110.47100 127.04400 62.77600  1.000 50.29743  ? 374 ARG A CA   1 
ATOM   2180 C C    . ARG A 1 374 ? 109.13400 127.70600 63.10900  1.000 53.93208  ? 374 ARG A C    1 
ATOM   2181 O O    . ARG A 1 374 ? 108.67900 127.66000 64.25800  1.000 53.85497  ? 374 ARG A O    1 
ATOM   2182 C CB   . ARG A 1 374 ? 111.57600 128.09400 62.65500  1.000 48.10447  ? 374 ARG A CB   1 
ATOM   2183 C CG   . ARG A 1 374 ? 111.60900 129.10300 63.78800  1.000 51.66500  ? 374 ARG A CG   1 
ATOM   2184 C CD   . ARG A 1 374 ? 112.54900 130.25300 63.46900  1.000 53.17357  ? 374 ARG A CD   1 
ATOM   2185 N NE   . ARG A 1 374 ? 113.90300 130.00200 63.94600  1.000 54.17833  ? 374 ARG A NE   1 
ATOM   2186 C CZ   . ARG A 1 374 ? 114.42200 130.53300 65.04400  1.000 52.88564  ? 374 ARG A CZ   1 
ATOM   2187 N NH1  . ARG A 1 374 ? 113.72300 131.35600 65.81000  1.000 51.74204  ? 374 ARG A NH1  1 
ATOM   2188 N NH2  . ARG A 1 374 ? 115.67200 130.23300 65.38300  1.000 50.08226  ? 374 ARG A NH2  1 
ATOM   2189 N N    . GLN A 1 375 ? 108.49100 128.33100 62.12000  1.000 48.37997  ? 375 GLN A N    1 
ATOM   2190 C CA   . GLN A 1 375 ? 107.25400 129.06400 62.38900  1.000 48.10057  ? 375 GLN A CA   1 
ATOM   2191 C C    . GLN A 1 375 ? 106.14100 128.13800 62.87200  1.000 49.66608  ? 375 GLN A C    1 
ATOM   2192 O O    . GLN A 1 375 ? 105.46200 128.42200 63.87100  1.000 54.88097  ? 375 GLN A O    1 
ATOM   2193 C CB   . GLN A 1 375 ? 106.81400 129.81500 61.13100  1.000 50.71862  ? 375 GLN A CB   1 
ATOM   2194 C CG   . GLN A 1 375 ? 107.91900 130.61000 60.45500  1.000 51.85593  ? 375 GLN A CG   1 
ATOM   2195 C CD   . GLN A 1 375 ? 108.47600 131.70900 61.33700  1.000 53.27834  ? 375 GLN A CD   1 
ATOM   2196 O OE1  . GLN A 1 375 ? 109.69100 131.84800 61.48400  1.000 52.50473  ? 375 GLN A OE1  1 
ATOM   2197 N NE2  . GLN A 1 375 ? 107.58900 132.50000 61.92800  1.000 54.46282  ? 375 GLN A NE2  1 
ATOM   2198 N N    . GLU A 1 376 ? 105.94500 127.01900 62.17300  1.000 45.41246  ? 376 GLU A N    1 
ATOM   2199 C CA   . GLU A 1 376 ? 104.89700 126.08000 62.55400  1.000 48.05829  ? 376 GLU A CA   1 
ATOM   2200 C C    . GLU A 1 376 ? 105.17700 125.47000 63.91900  1.000 47.52888  ? 376 GLU A C    1 
ATOM   2201 O O    . GLU A 1 376 ? 104.25100 125.23800 64.70600  1.000 50.75063  ? 376 GLU A O    1 
ATOM   2202 C CB   . GLU A 1 376 ? 104.75300 124.98700 61.49300  1.000 49.17861  ? 376 GLU A CB   1 
ATOM   2203 C CG   . GLU A 1 376 ? 104.33900 125.48100 60.11000  1.000 48.01776  ? 376 GLU A CG   1 
ATOM   2204 C CD   . GLU A 1 376 ? 105.41200 126.30200 59.42000  1.000 53.22998  ? 376 GLU A CD   1 
ATOM   2205 O OE1  . GLU A 1 376 ? 106.35100 126.75400 60.10600  1.000 53.86148  ? 376 GLU A OE1  1 
ATOM   2206 O OE2  . GLU A 1 376 ? 105.31500 126.49900 58.19100  1.000 53.24145  ? 376 GLU A OE2  1 
ATOM   2207 N N    . LEU A 1 377 ? 106.44700 125.19800 64.21700  1.000 32.19531  ? 377 LEU A N    1 
ATOM   2208 C CA   . LEU A 1 377 ? 106.79100 124.63700 65.51800  1.000 37.06826  ? 377 LEU A CA   1 
ATOM   2209 C C    . LEU A 1 377 ? 106.55100 125.64400 66.63800  1.000 43.40208  ? 377 LEU A C    1 
ATOM   2210 O O    . LEU A 1 377 ? 106.10900 125.27000 67.73000  1.000 47.59263  ? 377 LEU A O    1 
ATOM   2211 C CB   . LEU A 1 377 ? 108.24700 124.17200 65.51300  1.000 40.85455  ? 377 LEU A CB   1 
ATOM   2212 C CG   . LEU A 1 377 ? 108.55400 122.92300 64.68200  1.000 43.50667  ? 377 LEU A CG   1 
ATOM   2213 C CD1  . LEU A 1 377 ? 110.05300 122.76200 64.48400  1.000 37.65120  ? 377 LEU A CD1  1 
ATOM   2214 C CD2  . LEU A 1 377 ? 107.95600 121.67900 65.31900  1.000 41.37524  ? 377 LEU A CD2  1 
ATOM   2215 N N    . GLN A 1 378 ? 106.83800 126.92500 66.38900  1.000 42.85283  ? 378 GLN A N    1 
ATOM   2216 C CA   . GLN A 1 378 ? 106.68000 127.93300 67.43400  1.000 40.59252  ? 378 GLN A CA   1 
ATOM   2217 C C    . GLN A 1 378 ? 105.21700 128.28400 67.68000  1.000 42.37361  ? 378 GLN A C    1 
ATOM   2218 O O    . GLN A 1 378 ? 104.84200 128.63200 68.81100  1.000 50.22228  ? 378 GLN A O    1 
ATOM   2219 C CB   . GLN A 1 378 ? 107.46700 129.18900 67.06400  1.000 43.52395  ? 378 GLN A CB   1 
ATOM   2220 C CG   . GLN A 1 378 ? 108.97400 129.00800 67.10100  1.000 45.91947  ? 378 GLN A CG   1 
ATOM   2221 C CD   . GLN A 1 378 ? 109.72000 130.32700 67.08800  1.000 48.05178  ? 378 GLN A CD   1 
ATOM   2222 O OE1  . GLN A 1 378 ? 109.49800 131.17100 66.22000  1.000 50.05176  ? 378 GLN A OE1  1 
ATOM   2223 N NE2  . GLN A 1 378 ? 110.61400 130.50900 68.05300  1.000 48.70479  ? 378 GLN A NE2  1 
ATOM   2224 N N    . ARG A 1 379 ? 104.37000 128.16800 66.65300  1.000 31.33076  ? 379 ARG A N    1 
ATOM   2225 C CA   . ARG A 1 379 ? 102.95700 128.48100 66.85100  1.000 30.69967  ? 379 ARG A CA   1 
ATOM   2226 C C    . ARG A 1 379 ? 102.29700 127.49600 67.81000  1.000 36.67245  ? 379 ARG A C    1 
ATOM   2227 O O    . ARG A 1 379 ? 101.50300 127.89500 68.67500  1.000 42.39191  ? 379 ARG A O    1 
ATOM   2228 C CB   . ARG A 1 379 ? 102.23200 128.48900 65.50600  1.000 32.56895  ? 379 ARG A CB   1 
ATOM   2229 C CG   . ARG A 1 379 ? 102.02600 129.87200 64.91600  1.000 35.06609  ? 379 ARG A CG   1 
ATOM   2230 C CD   . ARG A 1 379 ? 100.58600 130.33000 65.06800  1.000 39.65938  ? 379 ARG A CD   1 
ATOM   2231 N NE   . ARG A 1 379 ? 99.72100  129.74900 64.04900  1.000 41.04509  ? 379 ARG A NE   1 
ATOM   2232 C CZ   . ARG A 1 379 ? 98.40200  129.65400 64.14900  1.000 41.35569  ? 379 ARG A CZ   1 
ATOM   2233 N NH1  . ARG A 1 379 ? 97.75700  130.09300 65.21700  1.000 39.45711  ? 379 ARG A NH1  1 
ATOM   2234 N NH2  . ARG A 1 379 ? 97.71400  129.10300 63.15300  1.000 40.38880  ? 379 ARG A NH2  1 
ATOM   2235 N N    . VAL A 1 380 ? 102.62500 126.20900 67.68300  1.000 31.45523  ? 380 VAL A N    1 
ATOM   2236 C CA   . VAL A 1 380 ? 102.04100 125.20000 68.56200  1.000 34.12789  ? 380 VAL A CA   1 
ATOM   2237 C C    . VAL A 1 380 ? 102.44400 125.45500 70.00800  1.000 32.69274  ? 380 VAL A C    1 
ATOM   2238 O O    . VAL A 1 380 ? 101.62300 125.34300 70.92800  1.000 33.06247  ? 380 VAL A O    1 
ATOM   2239 C CB   . VAL A 1 380 ? 102.45200 123.79000 68.10000  1.000 31.16510  ? 380 VAL A CB   1 
ATOM   2240 C CG1  . VAL A 1 380 ? 102.11100 122.75900 69.16300  1.000 32.81162  ? 380 VAL A CG1  1 
ATOM   2241 C CG2  . VAL A 1 380 ? 101.78200 123.44900 66.78000  1.000 30.76230  ? 380 VAL A CG2  1 
ATOM   2242 N N    . GLY A 1 381 ? 103.70200 125.83500 70.22800  1.000 23.67836  ? 381 GLY A N    1 
ATOM   2243 C CA   . GLY A 1 381 ? 104.14700 126.12500 71.58100  1.000 29.48751  ? 381 GLY A CA   1 
ATOM   2244 C C    . GLY A 1 381 ? 103.44100 127.33000 72.17100  1.000 33.02129  ? 381 GLY A C    1 
ATOM   2245 O O    . GLY A 1 381 ? 102.99200 127.30200 73.32400  1.000 33.26979  ? 381 GLY A O    1 
ATOM   2246 N N    . VAL A 1 382 ? 103.32800 128.40500 71.38900  1.000 27.41277  ? 382 VAL A N    1 
ATOM   2247 C CA   . VAL A 1 382 ? 102.65700 129.60100 71.89100  1.000 23.85060  ? 382 VAL A CA   1 
ATOM   2248 C C    . VAL A 1 382 ? 101.21200 129.28700 72.26300  1.000 29.05727  ? 382 VAL A C    1 
ATOM   2249 O O    . VAL A 1 382 ? 100.73300 129.66900 73.34300  1.000 35.17648  ? 382 VAL A O    1 
ATOM   2250 C CB   . VAL A 1 382 ? 102.74200 130.73300 70.85000  1.000 28.63073  ? 382 VAL A CB   1 
ATOM   2251 C CG1  . VAL A 1 382 ? 101.94200 131.94200 71.30700  1.000 29.52515  ? 382 VAL A CG1  1 
ATOM   2252 C CG2  . VAL A 1 382 ? 104.19100 131.11300 70.59600  1.000 28.68666  ? 382 VAL A CG2  1 
ATOM   2253 N N    . GLU A 1 383 ? 100.50600 128.54800 71.40200  1.000 27.50381  ? 383 GLU A N    1 
ATOM   2254 C CA   . GLU A 1 383 ? 99.10000  128.26600 71.67400  1.000 21.79274  ? 383 GLU A CA   1 
ATOM   2255 C C    . GLU A 1 383 ? 98.92700  127.32000 72.85800  1.000 24.61302  ? 383 GLU A C    1 
ATOM   2256 O O    . GLU A 1 383 ? 98.00900  127.49700 73.67300  1.000 25.47146  ? 383 GLU A O    1 
ATOM   2257 C CB   . GLU A 1 383 ? 98.43400  127.69300 70.42400  1.000 24.09360  ? 383 GLU A CB   1 
ATOM   2258 C CG   . GLU A 1 383 ? 98.26100  128.70100 69.30200  1.000 23.51216  ? 383 GLU A CG   1 
ATOM   2259 C CD   . GLU A 1 383 ? 97.44400  129.90500 69.72200  1.000 34.18667  ? 383 GLU A CD   1 
ATOM   2260 O OE1  . GLU A 1 383 ? 96.35400  129.71400 70.30100  1.000 37.65194  ? 383 GLU A OE1  1 
ATOM   2261 O OE2  . GLU A 1 383 ? 97.89000  131.04500 69.47800  1.000 35.10579  ? 383 GLU A OE2  1 
ATOM   2262 N N    . GLY A 1 384 ? 99.82600  126.34400 73.01100  1.000 15.35256  ? 384 GLY A N    1 
ATOM   2263 C CA   . GLY A 1 384 ? 99.71700  125.44400 74.14600  1.000 16.56538  ? 384 GLY A CA   1 
ATOM   2264 C C    . GLY A 1 384 ? 99.99400  126.14100 75.46200  1.000 21.03019  ? 384 GLY A C    1 
ATOM   2265 O O    . GLY A 1 384 ? 99.31100  125.89400 76.46500  1.000 23.25504  ? 384 GLY A O    1 
ATOM   2266 N N    . ALA A 1 385 ? 100.97100 127.05000 75.47400  1.000 19.86114  ? 385 ALA A N    1 
ATOM   2267 C CA   . ALA A 1 385 ? 101.25700 127.77500 76.70500  1.000 21.19292  ? 385 ALA A CA   1 
ATOM   2268 C C    . ALA A 1 385 ? 100.10800 128.70900 77.06000  1.000 23.06808  ? 385 ALA A C    1 
ATOM   2269 O O    . ALA A 1 385 ? 99.73000  128.82100 78.23500  1.000 22.31300  ? 385 ALA A O    1 
ATOM   2270 C CB   . ALA A 1 385 ? 102.56600 128.55000 76.56800  1.000 19.23177  ? 385 ALA A CB   1 
ATOM   2271 N N    . LYS A 1 386 ? 99.50600  129.35100 76.05400  1.000 21.84004  ? 386 LYS A N    1 
ATOM   2272 C CA   . LYS A 1 386 ? 98.36000  130.21100 76.32800  1.000 20.42891  ? 386 LYS A CA   1 
ATOM   2273 C C    . LYS A 1 386 ? 97.19700  129.41400 76.90700  1.000 21.28103  ? 386 LYS A C    1 
ATOM   2274 O O    . LYS A 1 386 ? 96.55000  129.85000 77.87100  1.000 25.44733  ? 386 LYS A O    1 
ATOM   2275 C CB   . LYS A 1 386 ? 97.93000  130.93200 75.05100  1.000 22.84957  ? 386 LYS A CB   1 
ATOM   2276 C CG   . LYS A 1 386 ? 97.76100  132.43000 75.21000  1.000 25.00442  ? 386 LYS A CG   1 
ATOM   2277 C CD   . LYS A 1 386 ? 97.47100  133.09300 73.87600  1.000 28.31975  ? 386 LYS A CD   1 
ATOM   2278 C CE   . LYS A 1 386 ? 98.70800  133.12500 72.99600  1.000 29.74475  ? 386 LYS A CE   1 
ATOM   2279 N NZ   . LYS A 1 386 ? 99.87800  133.70800 73.70800  1.000 28.20667  ? 386 LYS A NZ   1 
ATOM   2280 N N    . LEU A 1 387 ? 96.93500  128.22500 76.35700  1.000 16.82897  ? 387 LEU A N    1 
ATOM   2281 C CA   . LEU A 1 387 ? 95.82500  127.42400 76.86300  1.000 18.53706  ? 387 LEU A CA   1 
ATOM   2282 C C    . LEU A 1 387 ? 96.08100  126.94400 78.28900  1.000 18.44695  ? 387 LEU A C    1 
ATOM   2283 O O    . LEU A 1 387 ? 95.18100  127.00100 79.14100  1.000 18.13655  ? 387 LEU A O    1 
ATOM   2284 C CB   . LEU A 1 387 ? 95.57700  126.23600 75.93600  1.000 25.26601  ? 387 LEU A CB   1 
ATOM   2285 C CG   . LEU A 1 387 ? 94.48900  125.24900 76.36100  1.000 24.57702  ? 387 LEU A CG   1 
ATOM   2286 C CD1  . LEU A 1 387 ? 93.12700  125.92000 76.40500  1.000 23.74075  ? 387 LEU A CD1  1 
ATOM   2287 C CD2  . LEU A 1 387 ? 94.47400  124.05500 75.43400  1.000 19.29838  ? 387 LEU A CD2  1 
ATOM   2288 N N    . LEU A 1 388 ? 97.30400  126.49000 78.58300  1.000 17.62778  ? 388 LEU A N    1 
ATOM   2289 C CA   . LEU A 1 388 ? 97.57200  126.02300 79.93900  1.000 16.02076  ? 388 LEU A CA   1 
ATOM   2290 C C    . LEU A 1 388 ? 97.53100  127.16500 80.94700  1.000 19.11604  ? 388 LEU A C    1 
ATOM   2291 O O    . LEU A 1 388 ? 97.06200  126.97700 82.08000  1.000 21.63122  ? 388 LEU A O    1 
ATOM   2292 C CB   . LEU A 1 388 ? 98.92400  125.31100 79.99800  1.000 16.76718  ? 388 LEU A CB   1 
ATOM   2293 C CG   . LEU A 1 388 ? 99.02600  123.96100 79.28500  1.000 18.54998  ? 388 LEU A CG   1 
ATOM   2294 C CD1  . LEU A 1 388 ? 100.46100 123.47100 79.25800  1.000 8.78495   ? 388 LEU A CD1  1 
ATOM   2295 C CD2  . LEU A 1 388 ? 98.12100  122.93200 79.94100  1.000 14.78712  ? 388 LEU A CD2  1 
ATOM   2296 N N    . ARG A 1 389 ? 97.92100  128.37400 80.53700  1.000 24.96465  ? 389 ARG A N    1 
ATOM   2297 C CA   . ARG A 1 389 ? 97.87500  129.48400 81.47900  1.000 19.10705  ? 389 ARG A CA   1 
ATOM   2298 C C    . ARG A 1 389 ? 96.45100  129.97100 81.69700  1.000 22.38554  ? 389 ARG A C    1 
ATOM   2299 O O    . ARG A 1 389 ? 96.10300  130.38400 82.81100  1.000 24.58129  ? 389 ARG A O    1 
ATOM   2300 C CB   . ARG A 1 389 ? 98.77200  130.62100 80.98900  1.000 23.30796  ? 389 ARG A CB   1 
ATOM   2301 C CG   . ARG A 1 389 ? 100.21100 130.49000 81.45500  1.000 19.94310  ? 389 ARG A CG   1 
ATOM   2302 C CD   . ARG A 1 389 ? 101.13800 131.42700 80.70600  1.000 19.99019  ? 389 ARG A CD   1 
ATOM   2303 N NE   . ARG A 1 389 ? 102.53300 131.17900 81.05100  1.000 30.03926  ? 389 ARG A NE   1 
ATOM   2304 C CZ   . ARG A 1 389 ? 103.52600 131.12900 80.17400  1.000 27.03899  ? 389 ARG A CZ   1 
ATOM   2305 N NH1  . ARG A 1 389 ? 103.31700 131.31700 78.88200  1.000 23.62755  ? 389 ARG A NH1  1 
ATOM   2306 N NH2  . ARG A 1 389 ? 104.75900 130.88100 80.60500  1.000 22.37370  ? 389 ARG A NH2  1 
ATOM   2307 N N    . GLU A 1 390 ? 95.59300  129.86200 80.67900  1.000 23.87349  ? 390 GLU A N    1 
ATOM   2308 C CA   . GLU A 1 390 ? 94.20600  130.25300 80.88700  1.000 21.31031  ? 390 GLU A CA   1 
ATOM   2309 C C    . GLU A 1 390 ? 93.47300  129.23100 81.74500  1.000 22.72280  ? 390 GLU A C    1 
ATOM   2310 O O    . GLU A 1 390 ? 92.62000  129.60400 82.56200  1.000 22.22621  ? 390 GLU A O    1 
ATOM   2311 C CB   . GLU A 1 390 ? 93.50000  130.43200 79.54400  1.000 21.68099  ? 390 GLU A CB   1 
ATOM   2312 C CG   . GLU A 1 390 ? 91.98700  130.36200 79.62600  1.000 24.66780  ? 390 GLU A CG   1 
ATOM   2313 C CD   . GLU A 1 390 ? 91.34600  131.73300 79.65800  1.000 33.75844  ? 390 GLU A CD   1 
ATOM   2314 O OE1  . GLU A 1 390 ? 92.08800  132.73600 79.68600  1.000 33.45252  ? 390 GLU A OE1  1 
ATOM   2315 O OE2  . GLU A 1 390 ? 90.10000  131.80800 79.65500  1.000 35.39448  ? 390 GLU A OE2  1 
ATOM   2316 N N    . LEU A 1 391 ? 93.84200  127.95100 81.63700  1.000 27.78732  ? 391 LEU A N    1 
ATOM   2317 C CA   . LEU A 1 391 ? 93.23400  126.96100 82.52200  1.000 20.56180  ? 391 LEU A CA   1 
ATOM   2318 C C    . LEU A 1 391 ? 93.71100  127.14000 83.95800  1.000 18.76361  ? 391 LEU A C    1 
ATOM   2319 O O    . LEU A 1 391 ? 92.92600  126.98300 84.90300  1.000 22.61116  ? 391 LEU A O    1 
ATOM   2320 C CB   . LEU A 1 391 ? 93.53800  125.54700 82.02800  1.000 23.50466  ? 391 LEU A CB   1 
ATOM   2321 C CG   . LEU A 1 391 ? 92.75700  125.05900 80.80700  1.000 26.94147  ? 391 LEU A CG   1 
ATOM   2322 C CD1  . LEU A 1 391 ? 93.08000  123.60400 80.51800  1.000 24.15023  ? 391 LEU A CD1  1 
ATOM   2323 C CD2  . LEU A 1 391 ? 91.26300  125.24700 81.01600  1.000 20.66818  ? 391 LEU A CD2  1 
ATOM   2324 N N    . GLY A 1 392 ? 94.97400  127.52700 84.14600  1.000 19.71332  ? 392 GLY A N    1 
ATOM   2325 C CA   . GLY A 1 392 ? 95.44000  127.79900 85.49600  1.000 25.52631  ? 392 GLY A CA   1 
ATOM   2326 C C    . GLY A 1 392 ? 94.76100  129.01000 86.11000  1.000 26.84452  ? 392 GLY A C    1 
ATOM   2327 O O    . GLY A 1 392 ? 94.38400  128.99500 87.28900  1.000 20.42940  ? 392 GLY A O    1 
ATOM   2328 N N    . GLU A 1 393 ? 94.55700  130.06200 85.31000  1.000 29.47648  ? 393 GLU A N    1 
ATOM   2329 C CA   . GLU A 1 393 ? 93.86900  131.24200 85.82300  1.000 20.92091  ? 393 GLU A CA   1 
ATOM   2330 C C    . GLU A 1 393 ? 92.40600  130.95400 86.13200  1.000 26.84684  ? 393 GLU A C    1 
ATOM   2331 O O    . GLU A 1 393 ? 91.85900  131.51500 87.08800  1.000 25.31379  ? 393 GLU A O    1 
ATOM   2332 C CB   . GLU A 1 393 ? 93.98100  132.39500 84.82900  1.000 25.49288  ? 393 GLU A CB   1 
ATOM   2333 C CG   . GLU A 1 393 ? 95.40400  132.85700 84.57400  1.000 31.63272  ? 393 GLU A CG   1 
ATOM   2334 C CD   . GLU A 1 393 ? 95.90200  133.82000 85.63300  1.000 38.09275  ? 393 GLU A CD   1 
ATOM   2335 O OE1  . GLU A 1 393 ? 95.06900  134.53400 86.22900  1.000 35.93838  ? 393 GLU A OE1  1 
ATOM   2336 O OE2  . GLU A 1 393 ? 97.12800  133.86300 85.86800  1.000 38.17661  ? 393 GLU A OE2  1 
ATOM   2337 N N    . LYS A 1 394 ? 91.75500  130.08600 85.35200  1.000 31.64062  ? 394 LYS A N    1 
ATOM   2338 C CA   . LYS A 1 394 ? 90.36600  129.76000 85.66300  1.000 26.10906  ? 394 LYS A CA   1 
ATOM   2339 C C    . LYS A 1 394 ? 90.25400  128.85100 86.87900  1.000 25.06904  ? 394 LYS A C    1 
ATOM   2340 O O    . LYS A 1 394 ? 89.26400  128.92700 87.61400  1.000 21.24317  ? 394 LYS A O    1 
ATOM   2341 C CB   . LYS A 1 394 ? 89.67900  129.11700 84.45900  1.000 23.18407  ? 394 LYS A CB   1 
ATOM   2342 C CG   . LYS A 1 394 ? 88.68400  130.03300 83.77200  1.000 23.28899  ? 394 LYS A CG   1 
ATOM   2343 C CD   . LYS A 1 394 ? 88.69600  129.85500 82.27000  1.000 28.20048  ? 394 LYS A CD   1 
ATOM   2344 C CE   . LYS A 1 394 ? 88.03100  131.03400 81.58100  1.000 30.89745  ? 394 LYS A CE   1 
ATOM   2345 N NZ   . LYS A 1 394 ? 86.64700  131.25900 82.08400  1.000 27.99795  ? 394 LYS A NZ   1 
ATOM   2346 N N    . VAL A 1 395 ? 91.24700  127.99200 87.11600  1.000 20.80242  ? 395 VAL A N    1 
ATOM   2347 C CA   . VAL A 1 395 ? 91.20700  127.16000 88.31500  1.000 20.16697  ? 395 VAL A CA   1 
ATOM   2348 C C    . VAL A 1 395 ? 91.45000  128.00200 89.56200  1.000 24.29455  ? 395 VAL A C    1 
ATOM   2349 O O    . VAL A 1 395 ? 90.81000  127.79400 90.59900  1.000 20.65491  ? 395 VAL A O    1 
ATOM   2350 C CB   . VAL A 1 395 ? 92.21800  126.00400 88.20800  1.000 20.21112  ? 395 VAL A CB   1 
ATOM   2351 C CG1  . VAL A 1 395 ? 92.34200  125.28800 89.54200  1.000 12.50551  ? 395 VAL A CG1  1 
ATOM   2352 C CG2  . VAL A 1 395 ? 91.79700  125.03100 87.12200  1.000 27.68749  ? 395 VAL A CG2  1 
ATOM   2353 N N    . LYS A 1 396 ? 92.37200  128.96500 89.48800  1.000 27.33599  ? 396 LYS A N    1 
ATOM   2354 C CA   . LYS A 1 396 ? 92.67800  129.77100 90.66900  1.000 17.17820  ? 396 LYS A CA   1 
ATOM   2355 C C    . LYS A 1 396 ? 91.48900  130.62400 91.10500  1.000 25.90674  ? 396 LYS A C    1 
ATOM   2356 O O    . LYS A 1 396 ? 91.16900  130.69000 92.29700  1.000 24.33382  ? 396 LYS A O    1 
ATOM   2357 C CB   . LYS A 1 396 ? 93.89800  130.65300 90.40700  1.000 23.58443  ? 396 LYS A CB   1 
ATOM   2358 C CG   . LYS A 1 396 ? 94.27300  131.52800 91.59100  1.000 24.32740  ? 396 LYS A CG   1 
ATOM   2359 C CD   . LYS A 1 396 ? 94.99200  132.79000 91.15400  1.000 22.13462  ? 396 LYS A CD   1 
ATOM   2360 C CE   . LYS A 1 396 ? 96.39800  132.48500 90.67800  1.000 31.77910  ? 396 LYS A CE   1 
ATOM   2361 N NZ   . LYS A 1 396 ? 97.42300  132.99800 91.62700  1.000 30.80054  ? 396 LYS A NZ   1 
ATOM   2362 N N    . LYS A 1 397 ? 90.82200  131.28800 90.15900  1.000 33.42833  ? 397 LYS A N    1 
ATOM   2363 C CA   . LYS A 1 397 ? 89.67600  132.13100 90.48800  1.000 28.59111  ? 397 LYS A CA   1 
ATOM   2364 C C    . LYS A 1 397 ? 88.39000  131.35700 90.75200  1.000 30.87851  ? 397 LYS A C    1 
ATOM   2365 O O    . LYS A 1 397 ? 87.40900  131.96600 91.18900  1.000 29.93613  ? 397 LYS A O    1 
ATOM   2366 C CB   . LYS A 1 397 ? 89.41800  133.14100 89.36700  1.000 25.68812  ? 397 LYS A CB   1 
ATOM   2367 C CG   . LYS A 1 397 ? 90.42500  134.27200 89.29100  1.000 31.58205  ? 397 LYS A CG   1 
ATOM   2368 C CD   . LYS A 1 397 ? 90.10600  135.20200 88.13100  1.000 31.41745  ? 397 LYS A CD   1 
ATOM   2369 C CE   . LYS A 1 397 ? 90.09900  134.45500 86.80700  1.000 32.28665  ? 397 LYS A CE   1 
ATOM   2370 N NZ   . LYS A 1 397 ? 91.24300  134.84500 85.93700  1.000 35.58038  ? 397 LYS A NZ   1 
ATOM   2371 N N    . MET A 1 398 ? 88.36200  130.04800 90.51100  1.000 38.43143  ? 398 MET A N    1 
ATOM   2372 C CA   . MET A 1 398 ? 87.14900  129.25000 90.68100  1.000 32.19275  ? 398 MET A CA   1 
ATOM   2373 C C    . MET A 1 398 ? 86.02300  129.79000 89.79600  1.000 35.86399  ? 398 MET A C    1 
ATOM   2374 O O    . MET A 1 398 ? 84.98300  130.25300 90.26900  1.000 39.34008  ? 398 MET A O    1 
ATOM   2375 C CB   . MET A 1 398 ? 86.72400  129.21400 92.15300  1.000 22.85535  ? 398 MET A CB   1 
ATOM   2376 C CG   . MET A 1 398 ? 87.57200  128.30900 93.02800  1.000 33.63628  ? 398 MET A CG   1 
ATOM   2377 S SD   . MET A 1 398 ? 87.53300  128.78900 94.76600  1.000 42.79940  ? 398 MET A SD   1 
ATOM   2378 C CE   . MET A 1 398 ? 86.44100  127.54400 95.44200  1.000 33.03843  ? 398 MET A CE   1 
ATOM   2379 N N    . GLU A 1 399 ? 86.25300  129.71600 88.48700  1.000 40.77010  ? 399 GLU A N    1 
ATOM   2380 C CA   . GLU A 1 399 ? 85.32600  130.23200 87.49200  1.000 35.47258  ? 399 GLU A CA   1 
ATOM   2381 C C    . GLU A 1 399 ? 85.10200  129.19300 86.40200  1.000 37.63100  ? 399 GLU A C    1 
ATOM   2382 O O    . GLU A 1 399 ? 85.99100  128.39600 86.08900  1.000 43.21349  ? 399 GLU A O    1 
ATOM   2383 C CB   . GLU A 1 399 ? 85.84700  131.53900 86.87900  1.000 35.47127  ? 399 GLU A CB   1 
ATOM   2384 C CG   . GLU A 1 399 ? 84.89100  132.20300 85.90600  1.000 40.32146  ? 399 GLU A CG   1 
ATOM   2385 C CD   . GLU A 1 399 ? 85.34200  133.59500 85.51100  1.000 45.98472  ? 399 GLU A CD   1 
ATOM   2386 O OE1  . GLU A 1 399 ? 86.40100  133.71800 84.86000  1.000 47.40277  ? 399 GLU A OE1  1 
ATOM   2387 O OE2  . GLU A 1 399 ? 84.63800  134.56800 85.85300  1.000 45.95395  ? 399 GLU A OE2  1 
ATOM   2388 N N    . LYS A 1 400 ? 83.90200  129.20500 85.82900  1.000 34.47459  ? 400 LYS A N    1 
ATOM   2389 C CA   . LYS A 1 400 ? 83.54500  128.26900 84.77500  1.000 37.73005  ? 400 LYS A CA   1 
ATOM   2390 C C    . LYS A 1 400 ? 84.05000  128.75900 83.41800  1.000 34.11814  ? 400 LYS A C    1 
ATOM   2391 O O    . LYS A 1 400 ? 84.52600  129.88700 83.26600  1.000 35.00691  ? 400 LYS A O    1 
ATOM   2392 C CB   . LYS A 1 400 ? 82.03200  128.06500 84.73000  1.000 36.16164  ? 400 LYS A CB   1 
ATOM   2393 C CG   . LYS A 1 400 ? 81.48100  127.19800 85.84600  1.000 34.89810  ? 400 LYS A CG   1 
ATOM   2394 C CD   . LYS A 1 400 ? 79.98600  126.98200 85.67800  1.000 36.05072  ? 400 LYS A CD   1 
ATOM   2395 C CE   . LYS A 1 400 ? 79.59300  125.55000 86.00000  1.000 36.25438  ? 400 LYS A CE   1 
ATOM   2396 N NZ   . LYS A 1 400 ? 78.93900  125.44000 87.33300  1.000 37.51209  ? 400 LYS A NZ   1 
ATOM   2397 N N    . LEU A 1 401 ? 83.94200  127.88600 82.42000  1.000 37.58463  ? 401 LEU A N    1 
ATOM   2398 C CA   . LEU A 1 401 ? 84.36400  128.19500 81.06200  1.000 40.30366  ? 401 LEU A CA   1 
ATOM   2399 C C    . LEU A 1 401 ? 83.24400  128.90300 80.30900  1.000 38.71612  ? 401 LEU A C    1 
ATOM   2400 O O    . LEU A 1 401 ? 82.05900  128.63600 80.52200  1.000 38.64592  ? 401 LEU A O    1 
ATOM   2401 C CB   . LEU A 1 401 ? 84.77300  126.92600 80.31200  1.000 39.90881  ? 401 LEU A CB   1 
ATOM   2402 C CG   . LEU A 1 401 ? 85.95000  126.13000 80.87600  1.000 40.52954  ? 401 LEU A CG   1 
ATOM   2403 C CD1  . LEU A 1 401 ? 86.27700  124.94900 79.97500  1.000 36.15148  ? 401 LEU A CD1  1 
ATOM   2404 C CD2  . LEU A 1 401 ? 87.16600  127.02100 81.06100  1.000 39.80326  ? 401 LEU A CD2  1 
ATOM   2405 N N    . GLY A 1 402 ? 83.63300  129.81300 79.42000  1.000 52.26595  ? 402 GLY A N    1 
ATOM   2406 C CA   . GLY A 1 402 ? 82.67600  130.59400 78.67400  1.000 52.15748  ? 402 GLY A CA   1 
ATOM   2407 C C    . GLY A 1 402 ? 82.08100  129.86200 77.48800  1.000 54.72975  ? 402 GLY A C    1 
ATOM   2408 O O    . GLY A 1 402 ? 82.15600  128.63400 77.37500  1.000 56.84704  ? 402 GLY A O    1 
ATOM   2409 N N    . PRO A 1 403 ? 81.47000  130.61700 76.57400  1.000 66.61359  ? 403 PRO A N    1 
ATOM   2410 C CA   . PRO A 1 403 ? 80.79300  130.00200 75.42300  1.000 65.82312  ? 403 PRO A CA   1 
ATOM   2411 C C    . PRO A 1 403 ? 81.72300  129.49300 74.33000  1.000 65.68089  ? 403 PRO A C    1 
ATOM   2412 O O    . PRO A 1 403 ? 81.44800  128.45600 73.71700  1.000 66.68403  ? 403 PRO A O    1 
ATOM   2413 C CB   . PRO A 1 403 ? 79.90300  131.13800 74.90400  1.000 64.76305  ? 403 PRO A CB   1 
ATOM   2414 C CG   . PRO A 1 403 ? 80.63400  132.37700 75.28400  1.000 65.39526  ? 403 PRO A CG   1 
ATOM   2415 C CD   . PRO A 1 403 ? 81.31000  132.08200 76.59700  1.000 65.79059  ? 403 PRO A CD   1 
ATOM   2416 N N    . VAL A 1 404 ? 82.82000  130.20300 74.07200  1.000 62.02794  ? 404 VAL A N    1 
ATOM   2417 C CA   . VAL A 1 404 ? 83.70600  129.86500 72.96200  1.000 62.45946  ? 404 VAL A CA   1 
ATOM   2418 C C    . VAL A 1 404 ? 84.49500  128.59500 73.25200  1.000 64.49745  ? 404 VAL A C    1 
ATOM   2419 O O    . VAL A 1 404 ? 84.50200  128.09400 74.38100  1.000 64.86083  ? 404 VAL A O    1 
ATOM   2420 C CB   . VAL A 1 404 ? 84.65800  131.03300 72.64600  1.000 62.96353  ? 404 VAL A CB   1 
ATOM   2421 C CG1  . VAL A 1 404 ? 83.87100  132.24300 72.17000  1.000 63.50868  ? 404 VAL A CG1  1 
ATOM   2422 C CG2  . VAL A 1 404 ? 85.49500  131.38000 73.86700  1.000 62.58570  ? 404 VAL A CG2  1 
ATOM   2423 N N    . ASP A 1 405 ? 85.16400  128.07100 72.22600  1.000 49.63441  ? 405 ASP A N    1 
ATOM   2424 C CA   . ASP A 1 405 ? 85.96000  126.85400 72.32400  1.000 49.41584  ? 405 ASP A CA   1 
ATOM   2425 C C    . ASP A 1 405 ? 87.42500  127.21800 72.52300  1.000 50.03924  ? 405 ASP A C    1 
ATOM   2426 O O    . ASP A 1 405 ? 87.96400  128.06200 71.80000  1.000 52.18357  ? 405 ASP A O    1 
ATOM   2427 C CB   . ASP A 1 405 ? 85.79000  125.99200 71.07300  1.000 48.80802  ? 405 ASP A CB   1 
ATOM   2428 C CG   . ASP A 1 405 ? 86.51200  124.66300 71.17700  1.000 50.02213  ? 405 ASP A CG   1 
ATOM   2429 O OD1  . ASP A 1 405 ? 86.87800  124.27100 72.30500  1.000 53.63034  ? 405 ASP A OD1  1 
ATOM   2430 O OD2  . ASP A 1 405 ? 86.71000  124.00800 70.13300  1.000 48.84035  ? 405 ASP A OD2  1 
ATOM   2431 N N    . LEU A 1 406 ? 88.06300  126.57900 73.50200  1.000 39.90302  ? 406 LEU A N    1 
ATOM   2432 C CA   . LEU A 1 406 ? 89.44000  126.88600 73.86700  1.000 41.73814  ? 406 LEU A CA   1 
ATOM   2433 C C    . LEU A 1 406 ? 90.48200  126.11400 73.06600  1.000 43.45777  ? 406 LEU A C    1 
ATOM   2434 O O    . LEU A 1 406 ? 91.67600  126.39800 73.20800  1.000 43.19179  ? 406 LEU A O    1 
ATOM   2435 C CB   . LEU A 1 406 ? 89.65700  126.61000 75.35900  1.000 42.98451  ? 406 LEU A CB   1 
ATOM   2436 C CG   . LEU A 1 406 ? 89.18800  127.67800 76.34900  1.000 44.31592  ? 406 LEU A CG   1 
ATOM   2437 C CD1  . LEU A 1 406 ? 90.00000  127.60700 77.63100  1.000 41.67112  ? 406 LEU A CD1  1 
ATOM   2438 C CD2  . LEU A 1 406 ? 89.27500  129.06300 75.73100  1.000 44.42851  ? 406 LEU A CD2  1 
ATOM   2439 N N    . LEU A 1 407 ? 90.07900  125.15600 72.22900  1.000 35.21777  ? 407 LEU A N    1 
ATOM   2440 C CA   . LEU A 1 407 ? 91.02900  124.32700 71.49400  1.000 32.24732  ? 407 LEU A CA   1 
ATOM   2441 C C    . LEU A 1 407 ? 90.94300  124.53300 69.98400  1.000 30.33869  ? 407 LEU A C    1 
ATOM   2442 O O    . LEU A 1 407 ? 91.19300  123.60400 69.21500  1.000 38.84484  ? 407 LEU A O    1 
ATOM   2443 C CB   . LEU A 1 407 ? 90.81500  122.85200 71.83300  1.000 34.71732  ? 407 LEU A CB   1 
ATOM   2444 C CG   . LEU A 1 407 ? 91.12800  122.38800 73.25600  1.000 31.39310  ? 407 LEU A CG   1 
ATOM   2445 C CD1  . LEU A 1 407 ? 90.65900  120.96000 73.46700  1.000 28.19226  ? 407 LEU A CD1  1 
ATOM   2446 C CD2  . LEU A 1 407 ? 92.61100  122.50000 73.53200  1.000 28.25337  ? 407 LEU A CD2  1 
ATOM   2447 N N    . PHE A 1 408 ? 90.59300  125.73800 69.53800  1.000 33.02082  ? 408 PHE A N    1 
ATOM   2448 C CA   . PHE A 1 408 ? 90.46800  125.99400 68.10700  1.000 33.47465  ? 408 PHE A CA   1 
ATOM   2449 C C    . PHE A 1 408 ? 91.78400  126.43800 67.47000  1.000 38.54529  ? 408 PHE A C    1 
ATOM   2450 O O    . PHE A 1 408 ? 92.18500  125.91400 66.42100  1.000 40.70685  ? 408 PHE A O    1 
ATOM   2451 C CB   . PHE A 1 408 ? 89.37900  127.04700 67.87200  1.000 36.88843  ? 408 PHE A CB   1 
ATOM   2452 C CG   . PHE A 1 408 ? 89.16000  127.39000 66.42600  1.000 38.08470  ? 408 PHE A CG   1 
ATOM   2453 C CD1  . PHE A 1 408 ? 89.91000  128.37700 65.80900  1.000 36.19680  ? 408 PHE A CD1  1 
ATOM   2454 C CD2  . PHE A 1 408 ? 88.19700  126.72800 65.68400  1.000 38.30372  ? 408 PHE A CD2  1 
ATOM   2455 C CE1  . PHE A 1 408 ? 89.70800  128.69100 64.48100  1.000 38.87363  ? 408 PHE A CE1  1 
ATOM   2456 C CE2  . PHE A 1 408 ? 87.99100  127.03900 64.35600  1.000 38.43210  ? 408 PHE A CE2  1 
ATOM   2457 C CZ   . PHE A 1 408 ? 88.74700  128.02200 63.75400  1.000 37.90627  ? 408 PHE A CZ   1 
ATOM   2458 N N    . GLU A 1 409 ? 92.48900  127.36700 68.12000  1.000 38.16921  ? 409 GLU A N    1 
ATOM   2459 C CA   . GLU A 1 409 ? 93.74700  127.86200 67.57100  1.000 37.93699  ? 409 GLU A CA   1 
ATOM   2460 C C    . GLU A 1 409 ? 94.83900  126.80000 67.60500  1.000 39.75284  ? 409 GLU A C    1 
ATOM   2461 O O    . GLU A 1 409 ? 95.62300  126.68400 66.65700  1.000 42.85845  ? 409 GLU A O    1 
ATOM   2462 C CB   . GLU A 1 409 ? 94.19200  129.10900 68.33500  1.000 34.12221  ? 409 GLU A CB   1 
ATOM   2463 C CG   . GLU A 1 409 ? 93.35400  130.34400 68.05000  1.000 38.84083  ? 409 GLU A CG   1 
ATOM   2464 C CD   . GLU A 1 409 ? 93.19500  130.61700 66.56800  1.000 44.93551  ? 409 GLU A CD   1 
ATOM   2465 O OE1  . GLU A 1 409 ? 94.20100  130.96000 65.91200  1.000 46.16186  ? 409 GLU A OE1  1 
ATOM   2466 O OE2  . GLU A 1 409 ? 92.06100  130.49000 66.05800  1.000 41.18714  ? 409 GLU A OE2  1 
ATOM   2467 N N    . VAL A 1 410 ? 94.89800  126.00300 68.67300  1.000 28.78313  ? 410 VAL A N    1 
ATOM   2468 C CA   . VAL A 1 410 ? 95.92800  124.97200 68.75300  1.000 31.49245  ? 410 VAL A CA   1 
ATOM   2469 C C    . VAL A 1 410 ? 95.68200  123.89300 67.70400  1.000 28.61548  ? 410 VAL A C    1 
ATOM   2470 O O    . VAL A 1 410 ? 96.62300  123.38700 67.07800  1.000 29.38905  ? 410 VAL A O    1 
ATOM   2471 C CB   . VAL A 1 410 ? 95.99400  124.39200 70.17900  1.000 27.03587  ? 410 VAL A CB   1 
ATOM   2472 C CG1  . VAL A 1 410 ? 94.68800  123.70300 70.54400  1.000 28.39416  ? 410 VAL A CG1  1 
ATOM   2473 C CG2  . VAL A 1 410 ? 97.17200  123.44300 70.31800  1.000 32.29883  ? 410 VAL A CG2  1 
ATOM   2474 N N    . HIS A 1 411 ? 94.41600  123.53700 67.47800  1.000 23.71559  ? 411 HIS A N    1 
ATOM   2475 C CA   . HIS A 1 411 ? 94.10300  122.55000 66.45100  1.000 27.80965  ? 411 HIS A CA   1 
ATOM   2476 C C    . HIS A 1 411 ? 94.44700  123.07500 65.06200  1.000 32.00634  ? 411 HIS A C    1 
ATOM   2477 O O    . HIS A 1 411 ? 95.01700  122.34600 64.23700  1.000 34.90449  ? 411 HIS A O    1 
ATOM   2478 C CB   . HIS A 1 411 ? 92.62700  122.16300 66.52900  1.000 24.34193  ? 411 HIS A CB   1 
ATOM   2479 C CG   . HIS A 1 411 ? 92.29000  121.29700 67.70200  1.000 29.95755  ? 411 HIS A CG   1 
ATOM   2480 N ND1  . HIS A 1 411 ? 91.01000  120.85400 67.95700  1.000 28.15277  ? 411 HIS A ND1  1 
ATOM   2481 C CD2  . HIS A 1 411 ? 93.06500  120.79500 68.69300  1.000 29.12045  ? 411 HIS A CD2  1 
ATOM   2482 C CE1  . HIS A 1 411 ? 91.01100  120.11500 69.05100  1.000 27.95340  ? 411 HIS A CE1  1 
ATOM   2483 N NE2  . HIS A 1 411 ? 92.24600  120.06300 69.51800  1.000 24.87017  ? 411 HIS A NE2  1 
ATOM   2484 N N    . LEU A 1 412 ? 94.13100  124.34500 64.79000  1.000 38.34733  ? 412 LEU A N    1 
ATOM   2485 C CA   . LEU A 1 412 ? 94.49800  124.91800 63.49900  1.000 38.77812  ? 412 LEU A CA   1 
ATOM   2486 C C    . LEU A 1 412 ? 96.01300  124.94200 63.32300  1.000 41.74390  ? 412 LEU A C    1 
ATOM   2487 O O    . LEU A 1 412 ? 96.52800  124.64500 62.23500  1.000 44.39822  ? 412 LEU A O    1 
ATOM   2488 C CB   . LEU A 1 412 ? 93.91200  126.32500 63.37200  1.000 39.67402  ? 412 LEU A CB   1 
ATOM   2489 C CG   . LEU A 1 412 ? 93.99800  127.00200 62.00500  1.000 41.03345  ? 412 LEU A CG   1 
ATOM   2490 C CD1  . LEU A 1 412 ? 92.78800  126.64500 61.15800  1.000 39.74377  ? 412 LEU A CD1  1 
ATOM   2491 C CD2  . LEU A 1 412 ? 94.11400  128.50800 62.16600  1.000 39.93669  ? 412 LEU A CD2  1 
ATOM   2492 N N    . ALA A 1 413 ? 96.74400  125.27400 64.39000  1.000 34.81878  ? 413 ALA A N    1 
ATOM   2493 C CA   . ALA A 1 413 ? 98.20100  125.29600 64.31700  1.000 34.86775  ? 413 ALA A CA   1 
ATOM   2494 C C    . ALA A 1 413 ? 98.75800  123.91200 64.01500  1.000 37.35793  ? 413 ALA A C    1 
ATOM   2495 O O    . ALA A 1 413 ? 99.67200  123.76600 63.19300  1.000 40.22453  ? 413 ALA A O    1 
ATOM   2496 C CB   . ALA A 1 413 ? 98.78400  125.83800 65.62200  1.000 27.50400  ? 413 ALA A CB   1 
ATOM   2497 N N    . ALA A 1 414 ? 98.21200  122.87600 64.65600  1.000 32.95132  ? 414 ALA A N    1 
ATOM   2498 C CA   . ALA A 1 414 ? 98.74400  121.53700 64.42800  1.000 31.43338  ? 414 ALA A CA   1 
ATOM   2499 C C    . ALA A 1 414 ? 98.38000  121.02500 63.04100  1.000 34.40637  ? 414 ALA A C    1 
ATOM   2500 O O    . ALA A 1 414 ? 99.15900  120.28000 62.43000  1.000 33.52107  ? 414 ALA A O    1 
ATOM   2501 C CB   . ALA A 1 414 ? 98.23600  120.57700 65.50200  1.000 30.27509  ? 414 ALA A CB   1 
ATOM   2502 N N    . GLU A 1 415 ? 97.24300  121.46200 62.49500  1.000 41.62355  ? 415 GLU A N    1 
ATOM   2503 C CA   . GLU A 1 415 ? 96.90100  121.04400 61.14000  1.000 39.66939  ? 415 GLU A CA   1 
ATOM   2504 C C    . GLU A 1 415 ? 97.79600  121.74000 60.12100  1.000 40.06310  ? 415 GLU A C    1 
ATOM   2505 O O    . GLU A 1 415 ? 98.20600  121.13200 59.12200  1.000 40.77416  ? 415 GLU A O    1 
ATOM   2506 C CB   . GLU A 1 415 ? 95.42700  121.33000 60.85500  1.000 37.59230  ? 415 GLU A CB   1 
ATOM   2507 C CG   . GLU A 1 415 ? 94.48200  120.24500 61.34700  1.000 39.62954  ? 415 GLU A CG   1 
ATOM   2508 C CD   . GLU A 1 415 ? 93.24700  120.80900 62.02100  1.000 47.48368  ? 415 GLU A CD   1 
ATOM   2509 O OE1  . GLU A 1 415 ? 92.88100  121.96500 61.72500  1.000 47.24503  ? 415 GLU A OE1  1 
ATOM   2510 O OE2  . GLU A 1 415 ? 92.64100  120.09600 62.84700  1.000 46.25186  ? 415 GLU A OE2  1 
ATOM   2511 N N    . GLU A 1 416 ? 98.14900  123.00100 60.38200  1.000 36.79230  ? 416 GLU A N    1 
ATOM   2512 C CA   . GLU A 1 416 ? 99.09900  123.68000 59.50900  1.000 36.96986  ? 416 GLU A CA   1 
ATOM   2513 C C    . GLU A 1 416 ? 100.47300 123.02600 59.58900  1.000 41.26416  ? 416 GLU A C    1 
ATOM   2514 O O    . GLU A 1 416 ? 101.16800 122.89700 58.57400  1.000 44.42020  ? 416 GLU A O    1 
ATOM   2515 C CB   . GLU A 1 416 ? 99.18300  125.16100 59.87200  1.000 38.33408  ? 416 GLU A CB   1 
ATOM   2516 C CG   . GLU A 1 416 ? 97.85600  125.89200 59.78100  1.000 43.86532  ? 416 GLU A CG   1 
ATOM   2517 C CD   . GLU A 1 416 ? 97.98600  127.36900 60.08300  1.000 47.76762  ? 416 GLU A CD   1 
ATOM   2518 O OE1  . GLU A 1 416 ? 99.10000  127.80900 60.43900  1.000 50.17945  ? 416 GLU A OE1  1 
ATOM   2519 O OE2  . GLU A 1 416 ? 96.97400  128.09200 59.96400  1.000 43.16280  ? 416 GLU A OE2  1 
ATOM   2520 N N    . LEU A 1 417 ? 100.88200 122.61600 60.79100  1.000 38.19818  ? 417 LEU A N    1 
ATOM   2521 C CA   . LEU A 1 417 ? 102.14000 121.89000 60.94300  1.000 32.50364  ? 417 LEU A CA   1 
ATOM   2522 C C    . LEU A 1 417 ? 102.14000 120.61000 60.11400  1.000 31.55491  ? 417 LEU A C    1 
ATOM   2523 O O    . LEU A 1 417 ? 103.11400 120.30900 59.41200  1.000 30.81519  ? 417 LEU A O    1 
ATOM   2524 C CB   . LEU A 1 417 ? 102.39200 121.57500 62.41700  1.000 33.43820  ? 417 LEU A CB   1 
ATOM   2525 C CG   . LEU A 1 417 ? 103.72300 120.89200 62.74300  1.000 34.51889  ? 417 LEU A CG   1 
ATOM   2526 C CD1  . LEU A 1 417 ? 104.89400 121.66800 62.16300  1.000 35.06452  ? 417 LEU A CD1  1 
ATOM   2527 C CD2  . LEU A 1 417 ? 103.88300 120.71900 64.24200  1.000 33.34475  ? 417 LEU A CD2  1 
ATOM   2528 N N    . GLN A 1 418 ? 101.06500 119.82300 60.21000  1.000 38.67199  ? 418 GLN A N    1 
ATOM   2529 C CA   . GLN A 1 418 ? 100.98800 118.59100 59.42900  1.000 39.57958  ? 418 GLN A CA   1 
ATOM   2530 C C    . GLN A 1 418 ? 101.04000 118.87000 57.93000  1.000 43.83237  ? 418 GLN A C    1 
ATOM   2531 O O    . GLN A 1 418 ? 101.72000 118.15700 57.18100  1.000 42.35266  ? 418 GLN A O    1 
ATOM   2532 C CB   . GLN A 1 418 ? 99.71600  117.82300 59.78700  1.000 40.29026  ? 418 GLN A CB   1 
ATOM   2533 C CG   . GLN A 1 418 ? 99.67100  116.40300 59.24600  1.000 41.96679  ? 418 GLN A CG   1 
ATOM   2534 C CD   . GLN A 1 418 ? 100.89000 115.59000 59.63400  1.000 48.31188  ? 418 GLN A CD   1 
ATOM   2535 O OE1  . GLN A 1 418 ? 101.53000 114.96600 58.78800  1.000 46.67278  ? 418 GLN A OE1  1 
ATOM   2536 N NE2  . GLN A 1 418 ? 101.21800 115.59400 60.92100  1.000 44.38310  ? 418 GLN A NE2  1 
ATOM   2537 N N    . HIS A 1 419 ? 100.33300 119.90700 57.46900  1.000 50.20517  ? 419 HIS A N    1 
ATOM   2538 C CA   . HIS A 1 419 ? 100.39900 120.26000 56.05200  1.000 48.50078  ? 419 HIS A CA   1 
ATOM   2539 C C    . HIS A 1 419 ? 101.81900 120.62600 55.63400  1.000 49.08099  ? 419 HIS A C    1 
ATOM   2540 O O    . HIS A 1 419 ? 102.30000 120.19000 54.57800  1.000 46.71129  ? 419 HIS A O    1 
ATOM   2541 C CB   . HIS A 1 419 ? 99.44100  121.41100 55.74500  1.000 47.02194  ? 419 HIS A CB   1 
ATOM   2542 C CG   . HIS A 1 419 ? 97.99700  121.01700 55.76000  1.000 50.57562  ? 419 HIS A CG   1 
ATOM   2543 N ND1  . HIS A 1 419 ? 96.97500  121.94200 55.77700  1.000 50.05365  ? 419 HIS A ND1  1 
ATOM   2544 C CD2  . HIS A 1 419 ? 97.40400  119.80100 55.75400  1.000 51.76762  ? 419 HIS A CD2  1 
ATOM   2545 C CE1  . HIS A 1 419 ? 95.81400  121.31100 55.78300  1.000 49.40196  ? 419 HIS A CE1  1 
ATOM   2546 N NE2  . HIS A 1 419 ? 96.04600  120.01100 55.77000  1.000 51.31677  ? 419 HIS A NE2  1 
ATOM   2547 N N    . LYS A 1 420 ? 102.51200 121.41600 56.45700  1.000 46.39642  ? 420 LYS A N    1 
ATOM   2548 C CA   . LYS A 1 420 ? 103.88000 121.79700 56.12000  1.000 46.36501  ? 420 LYS A CA   1 
ATOM   2549 C C    . LYS A 1 420 ? 104.78700 120.57700 56.05900  1.000 49.67950  ? 420 LYS A C    1 
ATOM   2550 O O    . LYS A 1 420 ? 105.63600 120.47000 55.16600  1.000 51.65174  ? 420 LYS A O    1 
ATOM   2551 C CB   . LYS A 1 420 ? 104.41000 122.81400 57.13000  1.000 49.70053  ? 420 LYS A CB   1 
ATOM   2552 C CG   . LYS A 1 420 ? 105.82700 123.27600 56.84600  1.000 49.10969  ? 420 LYS A CG   1 
ATOM   2553 C CD   . LYS A 1 420 ? 105.91700 123.97800 55.50200  1.000 48.29791  ? 420 LYS A CD   1 
ATOM   2554 C CE   . LYS A 1 420 ? 107.14900 124.86400 55.42300  1.000 51.58060  ? 420 LYS A CE   1 
ATOM   2555 N NZ   . LYS A 1 420 ? 106.82600 126.21500 54.88900  1.000 51.95264  ? 420 LYS A NZ   1 
ATOM   2556 N N    . ILE A 1 421 ? 104.62800 119.64600 57.00100  1.000 47.23114  ? 421 ILE A N    1 
ATOM   2557 C CA   . ILE A 1 421 ? 105.47100 118.45400 56.99300  1.000 45.15776  ? 421 ILE A CA   1 
ATOM   2558 C C    . ILE A 1 421 ? 105.19900 117.63200 55.74100  1.000 41.27834  ? 421 ILE A C    1 
ATOM   2559 O O    . ILE A 1 421 ? 106.12100 117.08100 55.12700  1.000 41.54880  ? 421 ILE A O    1 
ATOM   2560 C CB   . ILE A 1 421 ? 105.25700 117.62400 58.27300  1.000 44.70083  ? 421 ILE A CB   1 
ATOM   2561 C CG1  . ILE A 1 421 ? 105.62400 118.44000 59.51200  1.000 42.13369  ? 421 ILE A CG1  1 
ATOM   2562 C CG2  . ILE A 1 421 ? 106.07600 116.34500 58.22200  1.000 41.71870  ? 421 ILE A CG2  1 
ATOM   2563 C CD1  . ILE A 1 421 ? 105.22700 117.77800 60.81200  1.000 42.82896  ? 421 ILE A CD1  1 
ATOM   2564 N N    . ASP A 1 422 ? 103.92900 117.53900 55.34100  1.000 52.09039  ? 422 ASP A N    1 
ATOM   2565 C CA   . ASP A 1 422 ? 103.58600 116.78900 54.13600  1.000 53.05811  ? 422 ASP A CA   1 
ATOM   2566 C C    . ASP A 1 422 ? 104.17400 117.43500 52.88700  1.000 52.57647  ? 422 ASP A C    1 
ATOM   2567 O O    . ASP A 1 422 ? 104.57100 116.73500 51.94800  1.000 47.55701  ? 422 ASP A O    1 
ATOM   2568 C CB   . ASP A 1 422 ? 102.06900 116.66500 54.01000  1.000 51.92662  ? 422 ASP A CB   1 
ATOM   2569 C CG   . ASP A 1 422 ? 101.54200 115.36500 54.58000  1.000 55.05142  ? 422 ASP A CG   1 
ATOM   2570 O OD1  . ASP A 1 422 ? 102.31600 114.65600 55.25600  1.000 56.74384  ? 422 ASP A OD1  1 
ATOM   2571 O OD2  . ASP A 1 422 ? 100.35500 115.05200 54.35200  1.000 55.62659  ? 422 ASP A OD2  1 
ATOM   2572 N N    . LYS A 1 423 ? 104.24000 118.76900 52.85300  1.000 58.41696  ? 423 LYS A N    1 
ATOM   2573 C CA   . LYS A 1 423 ? 104.79000 119.44500 51.67900  1.000 56.19687  ? 423 LYS A CA   1 
ATOM   2574 C C    . LYS A 1 423 ? 106.29100 119.20900 51.52700  1.000 56.59232  ? 423 LYS A C    1 
ATOM   2575 O O    . LYS A 1 423 ? 106.79200 119.10200 50.40200  1.000 55.35502  ? 423 LYS A O    1 
ATOM   2576 C CB   . LYS A 1 423 ? 104.49200 120.94300 51.74600  1.000 55.72548  ? 423 LYS A CB   1 
ATOM   2577 C CG   . LYS A 1 423 ? 103.34200 121.38800 50.85700  1.000 54.52287  ? 423 LYS A CG   1 
ATOM   2578 C CD   . LYS A 1 423 ? 102.12700 120.48800 51.01000  1.000 57.98587  ? 423 LYS A CD   1 
ATOM   2579 C CE   . LYS A 1 423 ? 101.10500 121.09300 51.95800  1.000 59.01910  ? 423 LYS A CE   1 
ATOM   2580 N NZ   . LYS A 1 423 ? 99.96100  120.17000 52.20100  1.000 58.61287  ? 423 LYS A NZ   1 
ATOM   2581 N N    . LYS A 1 424 ? 107.02500 119.12500 52.63500  1.000 61.17667  ? 424 LYS A N    1 
ATOM   2582 C CA   . LYS A 1 424 ? 108.47800 118.98900 52.57200  1.000 57.62744  ? 424 LYS A CA   1 
ATOM   2583 C C    . LYS A 1 424 ? 108.98500 117.75400 53.30700  1.000 56.92449  ? 424 LYS A C    1 
ATOM   2584 O O    . LYS A 1 424 ? 109.81900 117.86700 54.21200  1.000 61.09350  ? 424 LYS A O    1 
ATOM   2585 C CB   . LYS A 1 424 ? 109.15200 120.24200 53.13300  1.000 56.70605  ? 424 LYS A CB   1 
ATOM   2586 C CG   . LYS A 1 424 ? 109.50000 121.27700 52.07900  1.000 59.06233  ? 424 LYS A CG   1 
ATOM   2587 C CD   . LYS A 1 424 ? 109.11200 122.67600 52.52000  1.000 58.70365  ? 424 LYS A CD   1 
ATOM   2588 C CE   . LYS A 1 424 ? 108.80800 123.56100 51.32400  1.000 58.72533  ? 424 LYS A CE   1 
ATOM   2589 N NZ   . LYS A 1 424 ? 109.94200 123.59400 50.35900  1.000 58.85907  ? 424 LYS A NZ   1 
ATOM   2590 N N    . SER A 1 425 ? 108.50000 116.57500 52.92800  1.000 57.33994  ? 425 SER A N    1 
ATOM   2591 C CA   . SER A 1 425 ? 108.88100 115.33700 53.59500  1.000 58.40811  ? 425 SER A CA   1 
ATOM   2592 C C    . SER A 1 425 ? 110.04600 114.62300 52.92200  1.000 59.54638  ? 425 SER A C    1 
ATOM   2593 O O    . SER A 1 425 ? 110.46000 113.56400 53.40200  1.000 60.10075  ? 425 SER A O    1 
ATOM   2594 C CB   . SER A 1 425 ? 107.68000 114.38800 53.67200  1.000 56.84713  ? 425 SER A CB   1 
ATOM   2595 O OG   . SER A 1 425 ? 107.13500 114.14800 52.38700  1.000 57.36223  ? 425 SER A OG   1 
ATOM   2596 N N    . TYR A 1 426 ? 110.58700 115.16700 51.83200  1.000 60.57768  ? 426 TYR A N    1 
ATOM   2597 C CA   . TYR A 1 426 ? 111.72400 114.53900 51.17000  1.000 59.80916  ? 426 TYR A CA   1 
ATOM   2598 C C    . TYR A 1 426 ? 113.04200 114.82500 51.87700  1.000 60.22069  ? 426 TYR A C    1 
ATOM   2599 O O    . TYR A 1 426 ? 114.08800 114.34800 51.42500  1.000 60.67205  ? 426 TYR A O    1 
ATOM   2600 C CB   . TYR A 1 426 ? 111.80700 114.99000 49.70700  1.000 58.47847  ? 426 TYR A CB   1 
ATOM   2601 C CG   . TYR A 1 426 ? 111.92800 116.48400 49.50800  1.000 57.16667  ? 426 TYR A CG   1 
ATOM   2602 C CD1  . TYR A 1 426 ? 113.12300 117.14500 49.76200  1.000 57.65851  ? 426 TYR A CD1  1 
ATOM   2603 C CD2  . TYR A 1 426 ? 110.85700 117.22900 49.03900  1.000 58.72334  ? 426 TYR A CD2  1 
ATOM   2604 C CE1  . TYR A 1 426 ? 113.24100 118.50600 49.57400  1.000 59.58101  ? 426 TYR A CE1  1 
ATOM   2605 C CE2  . TYR A 1 426 ? 110.96500 118.59200 48.84900  1.000 58.56642  ? 426 TYR A CE2  1 
ATOM   2606 C CZ   . TYR A 1 426 ? 112.16000 119.22500 49.11700  1.000 59.29319  ? 426 TYR A CZ   1 
ATOM   2607 O OH   . TYR A 1 426 ? 112.27500 120.58200 48.92900  1.000 62.38750  ? 426 TYR A OH   1 
ATOM   2608 N N    . LEU A 1 427 ? 113.01500 115.59000 52.96500  1.000 57.05884  ? 427 LEU A N    1 
ATOM   2609 C CA   . LEU A 1 427 ? 114.20300 115.92800 53.73500  1.000 54.73331  ? 427 LEU A CA   1 
ATOM   2610 C C    . LEU A 1 427 ? 114.44800 114.96900 54.89100  1.000 56.55930  ? 427 LEU A C    1 
ATOM   2611 O O    . LEU A 1 427 ? 115.44000 115.12600 55.61000  1.000 56.48712  ? 427 LEU A O    1 
ATOM   2612 C CB   . LEU A 1 427 ? 114.09400 117.35800 54.27500  1.000 55.44999  ? 427 LEU A CB   1 
ATOM   2613 C CG   . LEU A 1 427 ? 113.89300 118.47400 53.25100  1.000 55.36579  ? 427 LEU A CG   1 
ATOM   2614 C CD1  . LEU A 1 427 ? 113.68400 119.80700 53.95200  1.000 55.18013  ? 427 LEU A CD1  1 
ATOM   2615 C CD2  . LEU A 1 427 ? 115.07900 118.54500 52.30500  1.000 56.30753  ? 427 LEU A CD2  1 
ATOM   2616 N N    . LEU A 1 428 ? 113.57000 113.98400 55.08800  1.000 53.57435  ? 428 LEU A N    1 
ATOM   2617 C CA   . LEU A 1 428 ? 113.68800 113.04900 56.19600  1.000 52.01138  ? 428 LEU A CA   1 
ATOM   2618 C C    . LEU A 1 428 ? 114.04300 111.63400 55.76800  1.000 52.26967  ? 428 LEU A C    1 
ATOM   2619 O O    . LEU A 1 428 ? 114.50100 110.85200 56.60800  1.000 54.16942  ? 428 LEU A O    1 
ATOM   2620 C CB   . LEU A 1 428 ? 112.37800 113.00900 56.99800  1.000 55.04685  ? 428 LEU A CB   1 
ATOM   2621 C CG   . LEU A 1 428 ? 111.71600 114.35800 57.28900  1.000 54.72937  ? 428 LEU A CG   1 
ATOM   2622 C CD1  . LEU A 1 428 ? 110.27000 114.16500 57.71400  1.000 52.46345  ? 428 LEU A CD1  1 
ATOM   2623 C CD2  . LEU A 1 428 ? 112.49100 115.13000 58.34400  1.000 53.27497  ? 428 LEU A CD2  1 
ATOM   2624 N N    . VAL A 1 429 ? 113.85300 111.28700 54.49700  1.000 66.20146  ? 429 VAL A N    1 
ATOM   2625 C CA   . VAL A 1 429 ? 114.11900 109.95200 53.99000  1.000 66.85176  ? 429 VAL A CA   1 
ATOM   2626 C C    . VAL A 1 429 ? 115.07600 110.05900 52.80600  1.000 66.80284  ? 429 VAL A C    1 
ATOM   2627 O O    . VAL A 1 429 ? 115.46900 111.14900 52.39400  1.000 65.46953  ? 429 VAL A O    1 
ATOM   2628 C CB   . VAL A 1 429 ? 112.82700 109.21100 53.58900  1.000 67.26800  ? 429 VAL A CB   1 
ATOM   2629 C CG1  . VAL A 1 429 ? 111.88100 109.11300 54.77700  1.000 66.69889  ? 429 VAL A CG1  1 
ATOM   2630 C CG2  . VAL A 1 429 ? 112.15700 109.91100 52.41700  1.000 66.24178  ? 429 VAL A CG2  1 
ATOM   2631 N N    . ASN A 1 430 ? 115.45100 108.90100 52.26500  1.000 84.97545  ? 430 ASN A N    1 
ATOM   2632 C CA   . ASN A 1 430 ? 116.32700 108.80900 51.10000  1.000 84.13896  ? 430 ASN A CA   1 
ATOM   2633 C C    . ASN A 1 430 ? 115.58300 108.07300 49.99400  1.000 84.67094  ? 430 ASN A C    1 
ATOM   2634 O O    . ASN A 1 430 ? 115.35200 106.86300 50.09500  1.000 85.41619  ? 430 ASN A O    1 
ATOM   2635 C CB   . ASN A 1 430 ? 117.63300 108.09700 51.45200  1.000 84.39344  ? 430 ASN A CB   1 
ATOM   2636 C CG   . ASN A 1 430 ? 118.58700 108.98200 52.22900  1.000 85.06036  ? 430 ASN A CG   1 
ATOM   2637 O OD1  . ASN A 1 430 ? 118.58200 108.98800 53.46000  1.000 84.77145  ? 430 ASN A OD1  1 
ATOM   2638 N ND2  . ASN A 1 430 ? 119.41200 109.73600 51.51300  1.000 85.05899  ? 430 ASN A ND2  1 
ATOM   2639 N N    . SER A 1 431 ? 115.20900 108.80100 48.94100  1.000 91.19326  ? 431 SER A N    1 
ATOM   2640 C CA   . SER A 1 431 ? 114.44000 108.21000 47.85400  1.000 91.66450  ? 431 SER A CA   1 
ATOM   2641 C C    . SER A 1 431 ? 115.29600 107.38500 46.90200  1.000 92.34031  ? 431 SER A C    1 
ATOM   2642 O O    . SER A 1 431 ? 114.75500 106.54100 46.17900  1.000 94.09670  ? 431 SER A O    1 
ATOM   2643 C CB   . SER A 1 431 ? 113.71100 109.30400 47.07100  1.000 91.29700  ? 431 SER A CB   1 
ATOM   2644 O OG   . SER A 1 431 ? 114.56300 110.41100 46.83000  1.000 92.05452  ? 431 SER A OG   1 
ATOM   2645 N N    . GLU A 1 432 ? 116.61200 107.61000 46.87900  1.000 93.19879  ? 432 GLU A N    1 
ATOM   2646 C CA   . GLU A 1 432 ? 117.47200 106.86500 45.96500  1.000 93.23932  ? 432 GLU A CA   1 
ATOM   2647 C C    . GLU A 1 432 ? 117.42100 105.36900 46.24700  1.000 93.15890  ? 432 GLU A C    1 
ATOM   2648 O O    . GLU A 1 432 ? 117.44700 104.55300 45.31800  1.000 92.99490  ? 432 GLU A O    1 
ATOM   2649 C CB   . GLU A 1 432 ? 118.90900 107.37800 46.05800  1.000 93.46625  ? 432 GLU A CB   1 
ATOM   2650 C CG   . GLU A 1 432 ? 119.29300 107.91500 47.42500  1.000 93.40953  ? 432 GLU A CG   1 
ATOM   2651 C CD   . GLU A 1 432 ? 119.23100 109.42700 47.49400  1.000 94.51095  ? 432 GLU A CD   1 
ATOM   2652 O OE1  . GLU A 1 432 ? 118.16700 109.99600 47.17000  1.000 93.88229  ? 432 GLU A OE1  1 
ATOM   2653 O OE2  . GLU A 1 432 ? 120.24700 110.04900 47.87100  1.000 95.57517  ? 432 GLU A OE2  1 
ATOM   2654 N N    . CYS A 1 433 ? 117.34800 104.98700 47.52100  1.000 92.60848  ? 433 CYS A N    1 
ATOM   2655 C CA   . CYS A 1 433 ? 117.37300 103.58200 47.90400  1.000 92.81933  ? 433 CYS A CA   1 
ATOM   2656 C C    . CYS A 1 433 ? 116.01400 102.90300 47.79700  1.000 92.54757  ? 433 CYS A C    1 
ATOM   2657 O O    . CYS A 1 433 ? 115.92900 101.69200 48.02800  1.000 92.12804  ? 433 CYS A O    1 
ATOM   2658 C CB   . CYS A 1 433 ? 117.90300 103.44000 49.33300  1.000 91.87254  ? 433 CYS A CB   1 
ATOM   2659 S SG   . CYS A 1 433 ? 119.62600 103.94400 49.54500  1.000 95.83257  ? 433 CYS A SG   1 
ATOM   2660 N N    . TRP A 1 434 ? 114.95800 103.64300 47.46300  1.000 90.07657  ? 434 TRP A N    1 
ATOM   2661 C CA   . TRP A 1 434 ? 113.62200 103.06300 47.41800  1.000 90.22113  ? 434 TRP A CA   1 
ATOM   2662 C C    . TRP A 1 434 ? 113.58700 101.85800 46.48700  1.000 91.27664  ? 434 TRP A C    1 
ATOM   2663 O O    . TRP A 1 434 ? 114.06500 101.92000 45.35000  1.000 91.12739  ? 434 TRP A O    1 
ATOM   2664 C CB   . TRP A 1 434 ? 112.60400 104.11000 46.96700  1.000 88.93134  ? 434 TRP A CB   1 
ATOM   2665 C CG   . TRP A 1 434 ? 111.98100 104.85500 48.10300  1.000 89.57516  ? 434 TRP A CG   1 
ATOM   2666 C CD1  . TRP A 1 434 ? 112.07700 104.55500 49.43000  1.000 89.60083  ? 434 TRP A CD1  1 
ATOM   2667 C CD2  . TRP A 1 434 ? 111.14800 106.01700 48.01400  1.000 90.99528  ? 434 TRP A CD2  1 
ATOM   2668 N NE1  . TRP A 1 434 ? 111.36500 105.46400 50.17300  1.000 89.52322  ? 434 TRP A NE1  1 
ATOM   2669 C CE2  . TRP A 1 434 ? 110.78400 106.37100 49.32700  1.000 90.48146  ? 434 TRP A CE2  1 
ATOM   2670 C CE3  . TRP A 1 434 ? 110.67800 106.79400 46.95100  1.000 90.12058  ? 434 TRP A CE3  1 
ATOM   2671 C CZ2  . TRP A 1 434 ? 109.97300 107.46800 49.60700  1.000 90.21002  ? 434 TRP A CZ2  1 
ATOM   2672 C CZ3  . TRP A 1 434 ? 109.87300 107.88200 47.23000  1.000 90.23248  ? 434 TRP A CZ3  1 
ATOM   2673 C CH2  . TRP A 1 434 ? 109.52900 108.20800 48.54700  1.000 90.56343  ? 434 TRP A CH2  1 
ATOM   2674 N N    . GLU A 1 435 ? 113.01800 100.76000 46.97300  1.000 94.21306  ? 435 GLU A N    1 
ATOM   2675 C CA   . GLU A 1 435 ? 112.91000 99.53900  46.18300  1.000 93.57263  ? 435 GLU A CA   1 
ATOM   2676 C C    . GLU A 1 435 ? 111.50200 98.95900  46.26500  1.000 93.62846  ? 435 GLU A C    1 
ATOM   2677 O O    . GLU A 1 435 ? 111.05700 98.52800  47.32800  1.000 93.27726  ? 435 GLU A O    1 
ATOM   2678 C CB   . GLU A 1 435 ? 113.93300 98.50300  46.65100  1.000 93.99481  ? 435 GLU A CB   1 
ATOM   2679 C CG   . GLU A 1 435 ? 113.85300 98.17500  48.13300  1.000 94.38678  ? 435 GLU A CG   1 
ATOM   2680 C CD   . GLU A 1 435 ? 114.33600 96.77300  48.44600  1.000 94.60307  ? 435 GLU A CD   1 
ATOM   2681 O OE1  . GLU A 1 435 ? 115.55000 96.51700  48.30800  1.000 93.99071  ? 435 GLU A OE1  1 
ATOM   2682 O OE2  . GLU A 1 435 ? 113.50100 95.92700  48.83000  1.000 94.51171  ? 435 GLU A OE2  1 
ATOM   2683 N N    . LYS A 1 527 ? 125.01200 106.19600 54.64200  1.000 79.92251  ? 527 LYS A N    1 
ATOM   2684 C CA   . LYS A 1 527 ? 125.53300 106.13800 56.00200  1.000 80.03869  ? 527 LYS A CA   1 
ATOM   2685 C C    . LYS A 1 527 ? 124.39500 105.98300 57.00600  1.000 80.17452  ? 527 LYS A C    1 
ATOM   2686 O O    . LYS A 1 527 ? 123.31100 106.53400 56.81900  1.000 79.81808  ? 527 LYS A O    1 
ATOM   2687 C CB   . LYS A 1 527 ? 126.35300 107.39000 56.31800  1.000 79.97715  ? 527 LYS A CB   1 
ATOM   2688 C CG   . LYS A 1 527 ? 126.98400 107.38900 57.70100  1.000 79.43980  ? 527 LYS A CG   1 
ATOM   2689 C CD   . LYS A 1 527 ? 127.87700 106.17400 57.89700  1.000 79.27952  ? 527 LYS A CD   1 
ATOM   2690 C CE   . LYS A 1 527 ? 127.71400 105.58200 59.28700  1.000 79.33280  ? 527 LYS A CE   1 
ATOM   2691 N NZ   . LYS A 1 527 ? 128.04300 106.56900 60.35200  1.000 79.32516  ? 527 LYS A NZ   1 
ATOM   2692 N N    . THR A 1 528 ? 124.64800 105.22100 58.07200  1.000 76.79857  ? 528 THR A N    1 
ATOM   2693 C CA   . THR A 1 528 ? 123.64000 105.03500 59.11100  1.000 77.13061  ? 528 THR A CA   1 
ATOM   2694 C C    . THR A 1 528 ? 123.39500 106.32800 59.88000  1.000 76.55320  ? 528 THR A C    1 
ATOM   2695 O O    . THR A 1 528 ? 122.24300 106.70600 60.13300  1.000 77.95915  ? 528 THR A O    1 
ATOM   2696 C CB   . THR A 1 528 ? 124.06800 103.91700 60.06200  1.000 76.25203  ? 528 THR A CB   1 
ATOM   2697 O OG1  . THR A 1 528 ? 124.09300 102.67000 59.35700  1.000 75.76102  ? 528 THR A OG1  1 
ATOM   2698 C CG2  . THR A 1 528 ? 123.10100 103.81300 61.23300  1.000 75.85908  ? 528 THR A CG2  1 
ATOM   2699 N N    . TYR A 1 529 ? 124.47000 107.02400 60.26000  1.000 67.59407  ? 529 TYR A N    1 
ATOM   2700 C CA   . TYR A 1 529 ? 124.31600 108.23500 61.05900  1.000 68.96774  ? 529 TYR A CA   1 
ATOM   2701 C C    . TYR A 1 529 ? 123.53000 109.29900 60.30500  1.000 70.79830  ? 529 TYR A C    1 
ATOM   2702 O O    . TYR A 1 529 ? 122.67200 109.97100 60.88600  1.000 71.18249  ? 529 TYR A O    1 
ATOM   2703 C CB   . TYR A 1 529 ? 125.68400 108.77400 61.47700  1.000 68.33499  ? 529 TYR A CB   1 
ATOM   2704 C CG   . TYR A 1 529 ? 125.59700 109.91700 62.46200  1.000 70.35993  ? 529 TYR A CG   1 
ATOM   2705 C CD1  . TYR A 1 529 ? 125.16800 109.70200 63.76500  1.000 69.49568  ? 529 TYR A CD1  1 
ATOM   2706 C CD2  . TYR A 1 529 ? 125.93100 111.21200 62.08900  1.000 70.42518  ? 529 TYR A CD2  1 
ATOM   2707 C CE1  . TYR A 1 529 ? 125.08100 110.74200 64.67000  1.000 69.29925  ? 529 TYR A CE1  1 
ATOM   2708 C CE2  . TYR A 1 529 ? 125.84600 112.25900 62.98700  1.000 70.68427  ? 529 TYR A CE2  1 
ATOM   2709 C CZ   . TYR A 1 529 ? 125.42000 112.01800 64.27700  1.000 69.83639  ? 529 TYR A CZ   1 
ATOM   2710 O OH   . TYR A 1 529 ? 125.33300 113.05500 65.17600  1.000 67.82132  ? 529 TYR A OH   1 
ATOM   2711 N N    . GLU A 1 530 ? 123.83200 109.49100 59.02000  1.000 69.14463  ? 530 GLU A N    1 
ATOM   2712 C CA   . GLU A 1 530 ? 123.12100 110.49200 58.23000  1.000 68.61942  ? 530 GLU A CA   1 
ATOM   2713 C C    . GLU A 1 530 ? 121.62200 110.20600 58.20500  1.000 70.40255  ? 530 GLU A C    1 
ATOM   2714 O O    . GLU A 1 530 ? 120.79700 111.10300 58.43000  1.000 71.22430  ? 530 GLU A O    1 
ATOM   2715 C CB   . GLU A 1 530 ? 123.69100 110.53400 56.81300  1.000 68.41428  ? 530 GLU A CB   1 
ATOM   2716 C CG   . GLU A 1 530 ? 123.40100 111.82000 56.05900  1.000 70.28274  ? 530 GLU A CG   1 
ATOM   2717 C CD   . GLU A 1 530 ? 123.63700 111.68500 54.56800  1.000 71.58283  ? 530 GLU A CD   1 
ATOM   2718 O OE1  . GLU A 1 530 ? 124.39600 110.77800 54.16400  1.000 71.14783  ? 530 GLU A OE1  1 
ATOM   2719 O OE2  . GLU A 1 530 ? 123.06200 112.48300 53.79800  1.000 71.50077  ? 530 GLU A OE2  1 
ATOM   2720 N N    . SER A 1 531 ? 121.25200 108.95300 57.93200  1.000 59.97366  ? 531 SER A N    1 
ATOM   2721 C CA   . SER A 1 531 ? 119.83900 108.60100 57.86000  1.000 61.94423  ? 531 SER A CA   1 
ATOM   2722 C C    . SER A 1 531 ? 119.15900 108.76100 59.21300  1.000 61.42678  ? 531 SER A C    1 
ATOM   2723 O O    . SER A 1 531 ? 118.01900 109.23700 59.28600  1.000 64.30419  ? 531 SER A O    1 
ATOM   2724 C CB   . SER A 1 531 ? 119.68200 107.17000 57.34600  1.000 64.08656  ? 531 SER A CB   1 
ATOM   2725 O OG   . SER A 1 531 ? 120.14000 107.05600 56.01000  1.000 64.29690  ? 531 SER A OG   1 
ATOM   2726 N N    . ALA A 1 532 ? 119.84000 108.38700 60.29900  1.000 50.23485  ? 532 ALA A N    1 
ATOM   2727 C CA   . ALA A 1 532 ? 119.22500 108.54000 61.61400  1.000 51.67405  ? 532 ALA A CA   1 
ATOM   2728 C C    . ALA A 1 532 ? 119.06700 110.01200 61.97400  1.000 53.59398  ? 532 ALA A C    1 
ATOM   2729 O O    . ALA A 1 532 ? 118.05900 110.41200 62.57200  1.000 55.06987  ? 532 ALA A O    1 
ATOM   2730 C CB   . ALA A 1 532 ? 120.05400 107.80800 62.66900  1.000 51.52661  ? 532 ALA A CB   1 
ATOM   2731 N N    . SER A 1 533 ? 120.03100 110.84300 61.57400  1.000 48.58012  ? 533 SER A N    1 
ATOM   2732 C CA   . SER A 1 533 ? 119.93900 112.26700 61.86500  1.000 48.47599  ? 533 SER A CA   1 
ATOM   2733 C C    . SER A 1 533 ? 118.79900 112.89900 61.08400  1.000 50.18915  ? 533 SER A C    1 
ATOM   2734 O O    . SER A 1 533 ? 118.12400 113.80700 61.58200  1.000 52.12670  ? 533 SER A O    1 
ATOM   2735 C CB   . SER A 1 533 ? 121.26400 112.95600 61.54200  1.000 50.04203  ? 533 SER A CB   1 
ATOM   2736 O OG   . SER A 1 533 ? 122.35500 112.25200 62.10700  1.000 50.29349  ? 533 SER A OG   1 
ATOM   2737 N N    . ALA A 1 534 ? 118.56800 112.42900 59.85700  1.000 46.46545  ? 534 ALA A N    1 
ATOM   2738 C CA   . ALA A 1 534 ? 117.44000 112.94300 59.09000  1.000 46.34734  ? 534 ALA A CA   1 
ATOM   2739 C C    . ALA A 1 534 ? 116.11500 112.47600 59.68100  1.000 48.47606  ? 534 ALA A C    1 
ATOM   2740 O O    . ALA A 1 534 ? 115.14700 113.24300 59.73200  1.000 48.82845  ? 534 ALA A O    1 
ATOM   2741 C CB   . ALA A 1 534 ? 117.56000 112.51700 57.62800  1.000 46.38022  ? 534 ALA A CB   1 
ATOM   2742 N N    . LEU A 1 535 ? 116.05200 111.22300 60.13700  1.000 38.58422  ? 535 LEU A N    1 
ATOM   2743 C CA   . LEU A 1 535 ? 114.83700 110.68400 60.73600  1.000 37.81872  ? 535 LEU A CA   1 
ATOM   2744 C C    . LEU A 1 535 ? 114.58300 111.18700 62.15400  1.000 37.70522  ? 535 LEU A C    1 
ATOM   2745 O O    . LEU A 1 535 ? 113.52100 110.89400 62.71300  1.000 39.71709  ? 535 LEU A O    1 
ATOM   2746 C CB   . LEU A 1 535 ? 114.89300 109.15400 60.74000  1.000 37.91801  ? 535 LEU A CB   1 
ATOM   2747 C CG   . LEU A 1 535 ? 113.55500 108.41900 60.64500  1.000 39.01752  ? 535 LEU A CG   1 
ATOM   2748 C CD1  . LEU A 1 535 ? 113.03400 108.43000 59.21700  1.000 38.32739  ? 535 LEU A CD1  1 
ATOM   2749 C CD2  . LEU A 1 535 ? 113.68800 106.99400 61.15700  1.000 38.81980  ? 535 LEU A CD2  1 
ATOM   2750 N N    . SER A 1 536 ? 115.52300 111.92400 62.74700  1.000 29.41767  ? 536 SER A N    1 
ATOM   2751 C CA   . SER A 1 536 ? 115.33300 112.41800 64.11000  1.000 29.62311  ? 536 SER A CA   1 
ATOM   2752 C C    . SER A 1 536 ? 114.35100 113.58700 64.21200  1.000 33.82026  ? 536 SER A C    1 
ATOM   2753 O O    . SER A 1 536 ? 113.73200 113.76900 65.26600  1.000 35.68999  ? 536 SER A O    1 
ATOM   2754 C CB   . SER A 1 536 ? 116.68200 112.83200 64.69900  1.000 29.10694  ? 536 SER A CB   1 
ATOM   2755 O OG   . SER A 1 536 ? 117.37300 111.71300 65.22400  1.000 28.44636  ? 536 SER A OG   1 
ATOM   2756 N N    . LEU A 1 537 ? 114.19900 114.39400 63.15700  1.000 27.86608  ? 537 LEU A N    1 
ATOM   2757 C CA   . LEU A 1 537 ? 113.26800 115.52400 63.20300  1.000 26.40169  ? 537 LEU A CA   1 
ATOM   2758 C C    . LEU A 1 537 ? 111.81300 115.06300 63.26700  1.000 28.35688  ? 537 LEU A C    1 
ATOM   2759 O O    . LEU A 1 537 ? 110.98000 115.67700 63.95800  1.000 29.43098  ? 537 LEU A O    1 
ATOM   2760 C CB   . LEU A 1 537 ? 113.49500 116.42400 61.98800  1.000 28.17539  ? 537 LEU A CB   1 
ATOM   2761 C CG   . LEU A 1 537 ? 112.86300 117.81800 61.99100  1.000 31.77909  ? 537 LEU A CG   1 
ATOM   2762 C CD1  . LEU A 1 537 ? 113.89600 118.87200 61.63700  1.000 27.37449  ? 537 LEU A CD1  1 
ATOM   2763 C CD2  . LEU A 1 537 ? 111.68900 117.87800 61.02800  1.000 30.19975  ? 537 LEU A CD2  1 
ATOM   2764 N N    . ALA A 1 538 ? 111.48400 114.00300 62.52600  1.000 22.71651  ? 538 ALA A N    1 
ATOM   2765 C CA   . ALA A 1 538 ? 110.12200 113.48600 62.53400  1.000 25.38109  ? 538 ALA A CA   1 
ATOM   2766 C C    . ALA A 1 538 ? 109.68600 113.07000 63.93000  1.000 22.53490  ? 538 ALA A C    1 
ATOM   2767 O O    . ALA A 1 538 ? 108.50100 113.16900 64.26000  1.000 24.21330  ? 538 ALA A O    1 
ATOM   2768 C CB   . ALA A 1 538 ? 110.00600 112.30900 61.56600  1.000 24.43628  ? 538 ALA A CB   1 
ATOM   2769 N N    . THR A 1 539 ? 110.62300 112.62600 64.77100  1.000 11.97137  ? 539 THR A N    1 
ATOM   2770 C CA   . THR A 1 539 ? 110.26400 112.25200 66.13500  1.000 19.89452  ? 539 THR A CA   1 
ATOM   2771 C C    . THR A 1 539 ? 109.81500 113.46500 66.94200  1.000 20.59241  ? 539 THR A C    1 
ATOM   2772 O O    . THR A 1 539 ? 108.80100 113.40900 67.64800  1.000 22.57479  ? 539 THR A O    1 
ATOM   2773 C CB   . THR A 1 539 ? 111.44800 111.56300 66.81400  1.000 24.66072  ? 539 THR A CB   1 
ATOM   2774 O OG1  . THR A 1 539 ? 111.74300 110.33800 66.13300  1.000 24.95421  ? 539 THR A OG1  1 
ATOM   2775 C CG2  . THR A 1 539 ? 111.13200 111.26300 68.27000  1.000 20.85999  ? 539 THR A CG2  1 
ATOM   2776 N N    . PHE A 1 540 ? 110.55200 114.57300 66.83900  1.000 14.60004  ? 540 PHE A N    1 
ATOM   2777 C CA   . PHE A 1 540 ? 110.15400 115.80400 67.51400  1.000 19.14844  ? 540 PHE A CA   1 
ATOM   2778 C C    . PHE A 1 540 ? 108.78200 116.27200 67.03900  1.000 18.47649  ? 540 PHE A C    1 
ATOM   2779 O O    . PHE A 1 540 ? 107.91800 116.63700 67.85300  1.000 16.76756  ? 540 PHE A O    1 
ATOM   2780 C CB   . PHE A 1 540 ? 111.21600 116.88100 67.27200  1.000 15.47053  ? 540 PHE A CB   1 
ATOM   2781 C CG   . PHE A 1 540 ? 111.15800 118.03200 68.23600  1.000 17.19479  ? 540 PHE A CG   1 
ATOM   2782 C CD1  . PHE A 1 540 ? 110.33900 119.12100 67.99200  1.000 18.55695  ? 540 PHE A CD1  1 
ATOM   2783 C CD2  . PHE A 1 540 ? 111.93200 118.02900 69.38500  1.000 18.23276  ? 540 PHE A CD2  1 
ATOM   2784 C CE1  . PHE A 1 540 ? 110.28700 120.18000 68.87900  1.000 18.24770  ? 540 PHE A CE1  1 
ATOM   2785 C CE2  . PHE A 1 540 ? 111.88400 119.08400 70.27500  1.000 14.84430  ? 540 PHE A CE2  1 
ATOM   2786 C CZ   . PHE A 1 540 ? 111.06100 120.16100 70.02200  1.000 15.15004  ? 540 PHE A CZ   1 
ATOM   2787 N N    . ALA A 1 541 ? 108.54900 116.23400 65.72400  1.000 17.74679  ? 541 ALA A N    1 
ATOM   2788 C CA   . ALA A 1 541 ? 107.25300 116.67600 65.20800  1.000 13.39127  ? 541 ALA A CA   1 
ATOM   2789 C C    . ALA A 1 541 ? 106.11200 115.76900 65.66900  1.000 21.22627  ? 541 ALA A C    1 
ATOM   2790 O O    . ALA A 1 541 ? 105.04500 116.25500 66.07800  1.000 24.39362  ? 541 ALA A O    1 
ATOM   2791 C CB   . ALA A 1 541 ? 107.29700 116.75000 63.68300  1.000 18.11478  ? 541 ALA A CB   1 
ATOM   2792 N N    . SER A 1 542 ? 106.32100 114.45000 65.63700  1.000 12.64703  ? 542 SER A N    1 
ATOM   2793 C CA   . SER A 1 542 ? 105.28000 113.52800 66.07600  1.000 14.99493  ? 542 SER A CA   1 
ATOM   2794 C C    . SER A 1 542 ? 104.99500 113.66700 67.56300  1.000 14.72119  ? 542 SER A C    1 
ATOM   2795 O O    . SER A 1 542 ? 103.83900 113.54400 67.98800  1.000 20.34184  ? 542 SER A O    1 
ATOM   2796 C CB   . SER A 1 542 ? 105.68200 112.09000 65.74600  1.000 18.32510  ? 542 SER A CB   1 
ATOM   2797 O OG   . SER A 1 542 ? 105.48300 111.80600 64.37400  1.000 26.65352  ? 542 SER A OG   1 
ATOM   2798 N N    . LEU A 1 543 ? 106.01900 113.96500 68.36500  1.000 8.55155   ? 543 LEU A N    1 
ATOM   2799 C CA   . LEU A 1 543 ? 105.79300 114.12300 69.79500  1.000 10.98307  ? 543 LEU A CA   1 
ATOM   2800 C C    . LEU A 1 543 ? 105.02400 115.40400 70.08200  1.000 14.55146  ? 543 LEU A C    1 
ATOM   2801 O O    . LEU A 1 543 ? 104.15700 115.43300 70.96500  1.000 15.51281  ? 543 LEU A O    1 
ATOM   2802 C CB   . LEU A 1 543 ? 107.12900 114.11200 70.53600  1.000 18.02688  ? 543 LEU A CB   1 
ATOM   2803 C CG   . LEU A 1 543 ? 107.84300 112.76100 70.60400  1.000 17.39069  ? 543 LEU A CG   1 
ATOM   2804 C CD1  . LEU A 1 543 ? 109.15400 112.88000 71.35800  1.000 12.68447  ? 543 LEU A CD1  1 
ATOM   2805 C CD2  . LEU A 1 543 ? 106.94900 111.70400 71.23400  1.000 18.31113  ? 543 LEU A CD2  1 
ATOM   2806 N N    . LEU A 1 544 ? 105.29600 116.46500 69.31900  1.000 22.81182  ? 544 LEU A N    1 
ATOM   2807 C CA   . LEU A 1 544 ? 104.51700 117.68800 69.48200  1.000 17.50159  ? 544 LEU A CA   1 
ATOM   2808 C C    . LEU A 1 544 ? 103.05300 117.46900 69.10400  1.000 18.12217  ? 544 LEU A C    1 
ATOM   2809 O O    . LEU A 1 544 ? 102.14100 117.96000 69.78800  1.000 20.78960  ? 544 LEU A O    1 
ATOM   2810 C CB   . LEU A 1 544 ? 105.12800 118.80800 68.64000  1.000 15.04850  ? 544 LEU A CB   1 
ATOM   2811 C CG   . LEU A 1 544 ? 105.17700 120.20100 69.26700  1.000 19.32932  ? 544 LEU A CG   1 
ATOM   2812 C CD1  . LEU A 1 544 ? 105.78300 120.14300 70.65700  1.000 15.99505  ? 544 LEU A CD1  1 
ATOM   2813 C CD2  . LEU A 1 544 ? 105.95900 121.15200 68.37800  1.000 16.71347  ? 544 LEU A CD2  1 
ATOM   2814 N N    . ILE A 1 545 ? 102.80400 116.69200 68.04700  1.000 12.33442  ? 545 ILE A N    1 
ATOM   2815 C CA   . ILE A 1 545 ? 101.41700 116.43800 67.66200  1.000 9.53006   ? 545 ILE A CA   1 
ATOM   2816 C C    . ILE A 1 545 ? 100.70800 115.56500 68.69700  1.000 13.78663  ? 545 ILE A C    1 
ATOM   2817 O O    . ILE A 1 545 ? 99.52000  115.76600 68.98600  1.000 14.29320  ? 545 ILE A O    1 
ATOM   2818 C CB   . ILE A 1 545 ? 101.35600 115.82000 66.25400  1.000 14.81864  ? 545 ILE A CB   1 
ATOM   2819 C CG1  . ILE A 1 545 ? 101.50900 116.91100 65.19200  1.000 12.80774  ? 545 ILE A CG1  1 
ATOM   2820 C CG2  . ILE A 1 545 ? 100.04800 115.07100 66.05200  1.000 12.37161  ? 545 ILE A CG2  1 
ATOM   2821 C CD1  . ILE A 1 545 ? 102.12900 116.43200 63.90300  1.000 20.34003  ? 545 ILE A CD1  1 
ATOM   2822 N N    . GLU A 1 546 ? 101.41900 114.60600 69.29700  1.000 15.02084  ? 546 GLU A N    1 
ATOM   2823 C CA   . GLU A 1 546 ? 100.80400 113.81500 70.36300  1.000 12.68767  ? 546 GLU A CA   1 
ATOM   2824 C C    . GLU A 1 546 ? 100.49300 114.67900 71.58500  1.000 11.42769  ? 546 GLU A C    1 
ATOM   2825 O O    . GLU A 1 546 ? 99.44000  114.51900 72.22700  1.000 15.26119  ? 546 GLU A O    1 
ATOM   2826 C CB   . GLU A 1 546 ? 101.72400 112.65300 70.73900  1.000 16.64075  ? 546 GLU A CB   1 
ATOM   2827 C CG   . GLU A 1 546 ? 101.21200 111.76900 71.86700  1.000 20.44540  ? 546 GLU A CG   1 
ATOM   2828 C CD   . GLU A 1 546 ? 99.95600  111.00800 71.49200  1.000 23.17468  ? 546 GLU A CD   1 
ATOM   2829 O OE1  . GLU A 1 546 ? 99.80900  110.64800 70.30700  1.000 17.76496  ? 546 GLU A OE1  1 
ATOM   2830 O OE2  . GLU A 1 546 ? 99.11900  110.76200 72.38500  1.000 25.14020  ? 546 GLU A OE2  1 
ATOM   2831 N N    . PHE A 1 547 ? 101.37700 115.63200 71.89400  1.000 9.89143   ? 547 PHE A N    1 
ATOM   2832 C CA   . PHE A 1 547 ? 101.10700 116.53000 73.00900  1.000 9.45810   ? 547 PHE A CA   1 
ATOM   2833 C C    . PHE A 1 547 ? 99.86400  117.36200 72.74100  1.000 14.04360  ? 547 PHE A C    1 
ATOM   2834 O O    . PHE A 1 547 ? 99.07400  117.62600 73.65400  1.000 8.14022   ? 547 PHE A O    1 
ATOM   2835 C CB   . PHE A 1 547 ? 102.30500 117.44400 73.26200  1.000 12.98701  ? 547 PHE A CB   1 
ATOM   2836 C CG   . PHE A 1 547 ? 101.99400 118.60500 74.16300  1.000 10.67217  ? 547 PHE A CG   1 
ATOM   2837 C CD1  . PHE A 1 547 ? 102.04100 118.46400 75.53700  1.000 11.00990  ? 547 PHE A CD1  1 
ATOM   2838 C CD2  . PHE A 1 547 ? 101.63000 119.83200 73.63300  1.000 8.66850   ? 547 PHE A CD2  1 
ATOM   2839 C CE1  . PHE A 1 547 ? 101.74800 119.52800 76.36500  1.000 8.03099   ? 547 PHE A CE1  1 
ATOM   2840 C CE2  . PHE A 1 547 ? 101.33200 120.89700 74.45600  1.000 14.89852  ? 547 PHE A CE2  1 
ATOM   2841 C CZ   . PHE A 1 547 ? 101.39100 120.74400 75.82400  1.000 14.96930  ? 547 PHE A CZ   1 
ATOM   2842 N N    . VAL A 1 548 ? 99.66200  117.77100 71.48800  1.000 19.52759  ? 548 VAL A N    1 
ATOM   2843 C CA   . VAL A 1 548 ? 98.47800  118.57600 71.21200  1.000 9.70512   ? 548 VAL A CA   1 
ATOM   2844 C C    . VAL A 1 548 ? 97.22600  117.70600 71.20000  1.000 11.87334  ? 548 VAL A C    1 
ATOM   2845 O O    . VAL A 1 548 ? 96.12500  118.19300 71.47700  1.000 19.79980  ? 548 VAL A O    1 
ATOM   2846 C CB   . VAL A 1 548 ? 98.63300  119.34400 69.89000  1.000 12.68665  ? 548 VAL A CB   1 
ATOM   2847 C CG1  . VAL A 1 548 ? 97.38400  120.16100 69.61000  1.000 10.50247  ? 548 VAL A CG1  1 
ATOM   2848 C CG2  . VAL A 1 548 ? 99.85400  120.24200 69.94100  1.000 13.81629  ? 548 VAL A CG2  1 
ATOM   2849 N N    . ALA A 1 549 ? 97.36700  116.41800 70.88500  1.000 18.82693  ? 549 ALA A N    1 
ATOM   2850 C CA   . ALA A 1 549 ? 96.22800  115.50600 70.91000  1.000 9.23266   ? 549 ALA A CA   1 
ATOM   2851 C C    . ALA A 1 549 ? 95.82700  115.06400 72.31400  1.000 14.28101  ? 549 ALA A C    1 
ATOM   2852 O O    . ALA A 1 549 ? 94.72700  114.52900 72.48400  1.000 19.34361  ? 549 ALA A O    1 
ATOM   2853 C CB   . ALA A 1 549 ? 96.52300  114.27300 70.05600  1.000 11.66447  ? 549 ALA A CB   1 
ATOM   2854 N N    . ARG A 1 550 ? 96.68000  115.26600 73.31900  1.000 17.51972  ? 550 ARG A N    1 
ATOM   2855 C CA   . ARG A 1 550 ? 96.35500  114.82600 74.67900  1.000 8.35198   ? 550 ARG A CA   1 
ATOM   2856 C C    . ARG A 1 550 ? 95.67400  115.87800 75.57200  1.000 13.96178  ? 550 ARG A C    1 
ATOM   2857 O O    . ARG A 1 550 ? 95.52600  115.63000 76.77200  1.000 15.93893  ? 550 ARG A O    1 
ATOM   2858 C CB   . ARG A 1 550 ? 97.61500  114.32200 75.39000  1.000 14.05435  ? 550 ARG A CB   1 
ATOM   2859 C CG   . ARG A 1 550 ? 98.13800  112.99000 74.89100  1.000 16.37002  ? 550 ARG A CG   1 
ATOM   2860 C CD   . ARG A 1 550 ? 99.30900  112.51800 75.73800  1.000 14.07475  ? 550 ARG A CD   1 
ATOM   2861 N NE   . ARG A 1 550 ? 99.89000  111.28000 75.23300  1.000 16.37880  ? 550 ARG A NE   1 
ATOM   2862 C CZ   . ARG A 1 550 ? 100.79000 110.55300 75.88300  1.000 14.11934  ? 550 ARG A CZ   1 
ATOM   2863 N NH1  . ARG A 1 550 ? 101.24400 110.91600 77.07000  1.000 14.27131  ? 550 ARG A NH1  1 
ATOM   2864 N NH2  . ARG A 1 550 ? 101.24400 109.43500 75.32600  1.000 12.88902  ? 550 ARG A NH2  1 
ATOM   2865 N N    . LEU A 1 551 ? 95.25300  117.03100 75.04200  1.000 17.78727  ? 551 LEU A N    1 
ATOM   2866 C CA   . LEU A 1 551 ? 94.68800  118.08800 75.88700  1.000 11.69493  ? 551 LEU A CA   1 
ATOM   2867 C C    . LEU A 1 551 ? 93.17000  118.01700 76.08100  1.000 13.08365  ? 551 LEU A C    1 
ATOM   2868 O O    . LEU A 1 551 ? 92.63900  118.65200 77.01200  1.000 21.42959  ? 551 LEU A O    1 
ATOM   2869 C CB   . LEU A 1 551 ? 95.05200  119.45600 75.30100  1.000 12.35845  ? 551 LEU A CB   1 
ATOM   2870 C CG   . LEU A 1 551 ? 96.52700  119.85900 75.38900  1.000 15.05240  ? 551 LEU A CG   1 
ATOM   2871 C CD1  . LEU A 1 551 ? 96.80400  121.08900 74.53500  1.000 5.98406   ? 551 LEU A CD1  1 
ATOM   2872 C CD2  . LEU A 1 551 ? 96.94000  120.10300 76.83100  1.000 4.45965   ? 551 LEU A CD2  1 
ATOM   2873 N N    . GLN A 1 552 ? 92.45900  117.25200 75.24900  1.000 17.46631  ? 552 GLN A N    1 
ATOM   2874 C CA   . GLN A 1 552 ? 91.00900  117.16100 75.39000  1.000 18.44496  ? 552 GLN A CA   1 
ATOM   2875 C C    . GLN A 1 552 ? 90.60000  116.49000 76.69700  1.000 19.56514  ? 552 GLN A C    1 
ATOM   2876 O O    . GLN A 1 552 ? 89.59300  116.87700 77.30300  1.000 17.32263  ? 552 GLN A O    1 
ATOM   2877 C CB   . GLN A 1 552 ? 90.42400  116.40600 74.19500  1.000 18.00197  ? 552 GLN A CB   1 
ATOM   2878 C CG   . GLN A 1 552 ? 88.91900  116.21500 74.23800  1.000 18.56280  ? 552 GLN A CG   1 
ATOM   2879 C CD   . GLN A 1 552 ? 88.16300  117.51000 74.02100  1.000 25.01589  ? 552 GLN A CD   1 
ATOM   2880 O OE1  . GLN A 1 552 ? 88.18600  118.07900 72.93100  1.000 23.66633  ? 552 GLN A OE1  1 
ATOM   2881 N NE2  . GLN A 1 552 ? 87.48700  117.98400 75.06100  1.000 23.24622  ? 552 GLN A NE2  1 
ATOM   2882 N N    . ASN A 1 553 ? 91.37700  115.51000 77.16600  1.000 16.33569  ? 553 ASN A N    1 
ATOM   2883 C CA   . ASN A 1 553 ? 91.05500  114.86900 78.43500  1.000 15.37427  ? 553 ASN A CA   1 
ATOM   2884 C C    . ASN A 1 553 ? 91.25100  115.81700 79.61000  1.000 17.92997  ? 553 ASN A C    1 
ATOM   2885 O O    . ASN A 1 553 ? 90.50500  115.74700 80.59600  1.000 27.18823  ? 553 ASN A O    1 
ATOM   2886 C CB   . ASN A 1 553 ? 91.90900  113.61400 78.61400  1.000 21.55483  ? 553 ASN A CB   1 
ATOM   2887 C CG   . ASN A 1 553 ? 91.28100  112.60900 79.55500  1.000 29.89727  ? 553 ASN A CG   1 
ATOM   2888 O OD1  . ASN A 1 553 ? 91.79800  112.35100 80.64100  1.000 29.02898  ? 553 ASN A OD1  1 
ATOM   2889 N ND2  . ASN A 1 553 ? 90.15900  112.03200 79.14000  1.000 32.50832  ? 553 ASN A ND2  1 
ATOM   2890 N N    . VAL A 1 554 ? 92.19800  116.75000 79.50300  1.000 9.83277   ? 554 VAL A N    1 
ATOM   2891 C CA   . VAL A 1 554 ? 92.39100  117.71400 80.57900  1.000 17.77360  ? 554 VAL A CA   1 
ATOM   2892 C C    . VAL A 1 554 ? 91.25200  118.72100 80.58600  1.000 15.63304  ? 554 VAL A C    1 
ATOM   2893 O O    . VAL A 1 554 ? 90.76400  119.12500 81.65100  1.000 16.12396  ? 554 VAL A O    1 
ATOM   2894 C CB   . VAL A 1 554 ? 93.76000  118.40800 80.44200  1.000 20.68003  ? 554 VAL A CB   1 
ATOM   2895 C CG1  . VAL A 1 554 ? 93.91300  119.49800 81.49200  1.000 19.05009  ? 554 VAL A CG1  1 
ATOM   2896 C CG2  . VAL A 1 554 ? 94.88900  117.39800 80.54500  1.000 15.93727  ? 554 VAL A CG2  1 
ATOM   2897 N N    . VAL A 1 555 ? 90.77100  119.10400 79.40100  1.000 21.80479  ? 555 VAL A N    1 
ATOM   2898 C CA   . VAL A 1 555 ? 89.62300  120.01000 79.38600  1.000 19.28492  ? 555 VAL A CA   1 
ATOM   2899 C C    . VAL A 1 555 ? 88.37200  119.30800 79.91500  1.000 18.32011  ? 555 VAL A C    1 
ATOM   2900 O O    . VAL A 1 555 ? 87.54600  119.92400 80.60900  1.000 25.19160  ? 555 VAL A O    1 
ATOM   2901 C CB   . VAL A 1 555 ? 89.40300  120.57100 77.97000  1.000 19.85205  ? 555 VAL A CB   1 
ATOM   2902 C CG1  . VAL A 1 555 ? 88.03500  121.22300 77.86400  1.000 18.60787  ? 555 VAL A CG1  1 
ATOM   2903 C CG2  . VAL A 1 555 ? 90.49900  121.56300 77.62200  1.000 12.97045  ? 555 VAL A CG2  1 
ATOM   2904 N N    . ASP A 1 556 ? 88.24200  118.00200 79.66600  1.000 18.25493  ? 556 ASP A N    1 
ATOM   2905 C CA   . ASP A 1 556 ? 87.10300  117.26100 80.20300  1.000 15.80464  ? 556 ASP A CA   1 
ATOM   2906 C C    . ASP A 1 556 ? 87.16900  117.16000 81.72300  1.000 21.98715  ? 556 ASP A C    1 
ATOM   2907 O O    . ASP A 1 556 ? 86.15400  117.34300 82.41300  1.000 24.71158  ? 556 ASP A O    1 
ATOM   2908 C CB   . ASP A 1 556 ? 87.04300  115.86700 79.57900  1.000 17.80703  ? 556 ASP A CB   1 
ATOM   2909 C CG   . ASP A 1 556 ? 86.50000  115.88400 78.16400  1.000 29.30737  ? 556 ASP A CG   1 
ATOM   2910 O OD1  . ASP A 1 556 ? 85.91200  116.90900 77.76000  1.000 28.05741  ? 556 ASP A OD1  1 
ATOM   2911 O OD2  . ASP A 1 556 ? 86.66100  114.87000 77.45400  1.000 32.77589  ? 556 ASP A OD2  1 
ATOM   2912 N N    . ALA A 1 557 ? 88.35600  116.88000 82.26900  1.000 22.21456  ? 557 ALA A N    1 
ATOM   2913 C CA   . ALA A 1 557 ? 88.47500  116.81200 83.72000  1.000 20.58469  ? 557 ALA A CA   1 
ATOM   2914 C C    . ALA A 1 557 ? 88.23200  118.17200 84.36100  1.000 24.41062  ? 557 ALA A C    1 
ATOM   2915 O O    . ALA A 1 557 ? 87.65100  118.24900 85.45400  1.000 24.03159  ? 557 ALA A O    1 
ATOM   2916 C CB   . ALA A 1 557 ? 89.85000  116.27400 84.11300  1.000 13.89260  ? 557 ALA A CB   1 
ATOM   2917 N N    . PHE A 1 558 ? 88.62100  119.25900 83.68700  1.000 26.11025  ? 558 PHE A N    1 
ATOM   2918 C CA   . PHE A 1 558 ? 88.32900  120.56800 84.25600  1.000 21.53645  ? 558 PHE A CA   1 
ATOM   2919 C C    . PHE A 1 558 ? 86.83200  120.83600 84.25700  1.000 23.13863  ? 558 PHE A C    1 
ATOM   2920 O O    . PHE A 1 558 ? 86.30700  121.43200 85.20300  1.000 26.10056  ? 558 PHE A O    1 
ATOM   2921 C CB   . PHE A 1 558 ? 89.05600  121.68200 83.50600  1.000 22.93048  ? 558 PHE A CB   1 
ATOM   2922 C CG   . PHE A 1 558 ? 88.65200  123.05900 83.95800  1.000 27.91942  ? 558 PHE A CG   1 
ATOM   2923 C CD1  . PHE A 1 558 ? 89.30300  123.67200 85.01500  1.000 25.35719  ? 558 PHE A CD1  1 
ATOM   2924 C CD2  . PHE A 1 558 ? 87.60400  123.72800 83.34700  1.000 25.22353  ? 558 PHE A CD2  1 
ATOM   2925 C CE1  . PHE A 1 558 ? 88.92500  124.92900 85.44400  1.000 21.01508  ? 558 PHE A CE1  1 
ATOM   2926 C CE2  . PHE A 1 558 ? 87.22400  124.98500 83.77300  1.000 25.22407  ? 558 PHE A CE2  1 
ATOM   2927 C CZ   . PHE A 1 558 ? 87.88500  125.58500 84.82200  1.000 22.00718  ? 558 PHE A CZ   1 
ATOM   2928 N N    . LYS A 1 559 ? 86.12600  120.42700 83.19900  1.000 29.76396  ? 559 LYS A N    1 
ATOM   2929 C CA   . LYS A 1 559 ? 84.67900  120.62200 83.19900  1.000 25.29306  ? 559 LYS A CA   1 
ATOM   2930 C C    . LYS A 1 559 ? 84.02400  119.82700 84.32100  1.000 26.92296  ? 559 LYS A C    1 
ATOM   2931 O O    . LYS A 1 559 ? 83.11300  120.32100 85.00200  1.000 31.37327  ? 559 LYS A O    1 
ATOM   2932 C CB   . LYS A 1 559 ? 84.08600  120.22400 81.84800  1.000 24.62161  ? 559 LYS A CB   1 
ATOM   2933 C CG   . LYS A 1 559 ? 84.31500  121.23400 80.74100  1.000 28.28836  ? 559 LYS A CG   1 
ATOM   2934 C CD   . LYS A 1 559 ? 83.36500  120.99000 79.58300  1.000 29.06748  ? 559 LYS A CD   1 
ATOM   2935 C CE   . LYS A 1 559 ? 84.06000  121.18100 78.24800  1.000 30.34701  ? 559 LYS A CE   1 
ATOM   2936 N NZ   . LYS A 1 559 ? 84.09700  122.61500 77.85000  1.000 34.51899  ? 559 LYS A NZ   1 
ATOM   2937 N N    . GLU A 1 560 ? 84.51300  118.61000 84.56800  1.000 31.75148  ? 560 GLU A N    1 
ATOM   2938 C CA   . GLU A 1 560 ? 83.94700  117.80800 85.65000  1.000 26.32122  ? 560 GLU A CA   1 
ATOM   2939 C C    . GLU A 1 560 ? 84.19100  118.45300 87.01000  1.000 30.02195  ? 560 GLU A C    1 
ATOM   2940 O O    . GLU A 1 560 ? 83.29600  118.46300 87.86900  1.000 30.21380  ? 560 GLU A O    1 
ATOM   2941 C CB   . GLU A 1 560 ? 84.52400  116.39400 85.61000  1.000 25.93599  ? 560 GLU A CB   1 
ATOM   2942 C CG   . GLU A 1 560 ? 83.53200  115.31500 86.00300  1.000 30.51665  ? 560 GLU A CG   1 
ATOM   2943 C CD   . GLU A 1 560 ? 84.17500  114.18600 86.77900  1.000 40.11181  ? 560 GLU A CD   1 
ATOM   2944 O OE1  . GLU A 1 560 ? 85.31500  113.80300 86.43900  1.000 33.97937  ? 560 GLU A OE1  1 
ATOM   2945 O OE2  . GLU A 1 560 ? 83.54200  113.68100 87.73000  1.000 36.35088  ? 560 GLU A OE2  1 
ATOM   2946 N N    . LEU A 1 561 ? 85.38000  119.02700 87.21700  1.000 24.85163  ? 561 LEU A N    1 
ATOM   2947 C CA   . LEU A 1 561 ? 85.64100  119.68500 88.49500  1.000 18.90858  ? 561 LEU A CA   1 
ATOM   2948 C C    . LEU A 1 561 ? 84.83100  120.96800 88.63800  1.000 23.04198  ? 561 LEU A C    1 
ATOM   2949 O O    . LEU A 1 561 ? 84.32800  121.27000 89.72600  1.000 19.98032  ? 561 LEU A O    1 
ATOM   2950 C CB   . LEU A 1 561 ? 87.13200  119.98300 88.64600  1.000 23.05890  ? 561 LEU A CB   1 
ATOM   2951 C CG   . LEU A 1 561 ? 87.51500  120.85300 89.84800  1.000 17.48411  ? 561 LEU A CG   1 
ATOM   2952 C CD1  . LEU A 1 561 ? 87.31300  120.10500 91.15100  1.000 20.03115  ? 561 LEU A CD1  1 
ATOM   2953 C CD2  . LEU A 1 561 ? 88.94600  121.35100 89.72900  1.000 19.11574  ? 561 LEU A CD2  1 
ATOM   2954 N N    . SER A 1 562 ? 84.68300  121.73300 87.55400  1.000 31.14679  ? 562 SER A N    1 
ATOM   2955 C CA   . SER A 1 562 ? 83.89500  122.95600 87.62600  1.000 28.25912  ? 562 SER A CA   1 
ATOM   2956 C C    . SER A 1 562 ? 82.41300  122.66200 87.79400  1.000 26.59051  ? 562 SER A C    1 
ATOM   2957 O O    . SER A 1 562 ? 81.65300  123.55800 88.17300  1.000 30.58418  ? 562 SER A O    1 
ATOM   2958 C CB   . SER A 1 562 ? 84.11500  123.81100 86.38000  1.000 23.61226  ? 562 SER A CB   1 
ATOM   2959 O OG   . SER A 1 562 ? 83.13900  123.52900 85.39500  1.000 28.27624  ? 562 SER A OG   1 
ATOM   2960 N N    . GLN A 1 563 ? 81.99100  121.42700 87.52700  1.000 35.37723  ? 563 GLN A N    1 
ATOM   2961 C CA   . GLN A 1 563 ? 80.59100  121.07300 87.71400  1.000 32.90840  ? 563 GLN A CA   1 
ATOM   2962 C C    . GLN A 1 563 ? 80.31800  120.51100 89.10300  1.000 37.22139  ? 563 GLN A C    1 
ATOM   2963 O O    . GLN A 1 563 ? 79.30300  120.85500 89.71700  1.000 36.08943  ? 563 GLN A O    1 
ATOM   2964 C CB   . GLN A 1 563 ? 80.15100  120.06500 86.65100  1.000 33.43116  ? 563 GLN A CB   1 
ATOM   2965 C CG   . GLN A 1 563 ? 78.65900  120.07500 86.37700  1.000 36.58258  ? 563 GLN A CG   1 
ATOM   2966 C CD   . GLN A 1 563 ? 78.20400  121.35000 85.69800  1.000 41.77671  ? 563 GLN A CD   1 
ATOM   2967 O OE1  . GLN A 1 563 ? 78.99700  122.05000 85.07000  1.000 38.90417  ? 563 GLN A OE1  1 
ATOM   2968 N NE2  . GLN A 1 563 ? 76.91800  121.66000 85.82200  1.000 40.87957  ? 563 GLN A NE2  1 
ATOM   2969 N N    . LYS A 1 564 ? 81.20000  119.65000 89.61700  1.000 37.66474  ? 564 LYS A N    1 
ATOM   2970 C CA   . LYS A 1 564 ? 80.96100  119.07400 90.93700  1.000 32.20678  ? 564 LYS A CA   1 
ATOM   2971 C C    . LYS A 1 564 ? 81.22900  120.04300 92.08500  1.000 34.96843  ? 564 LYS A C    1 
ATOM   2972 O O    . LYS A 1 564 ? 80.65500  119.86600 93.16400  1.000 37.22082  ? 564 LYS A O    1 
ATOM   2973 C CB   . LYS A 1 564 ? 81.80200  117.81000 91.13000  1.000 31.72744  ? 564 LYS A CB   1 
ATOM   2974 C CG   . LYS A 1 564 ? 81.13000  116.55500 90.60700  1.000 32.22528  ? 564 LYS A CG   1 
ATOM   2975 C CD   . LYS A 1 564 ? 81.69600  115.30600 91.25700  1.000 34.16100  ? 564 LYS A CD   1 
ATOM   2976 C CE   . LYS A 1 564 ? 81.11600  114.05500 90.61900  1.000 36.21523  ? 564 LYS A CE   1 
ATOM   2977 N NZ   . LYS A 1 564 ? 80.84800  114.23800 89.16700  1.000 36.46933  ? 564 LYS A NZ   1 
ATOM   2978 N N    . ALA A 1 565 ? 82.06900  121.05800 91.88700  1.000 38.21163  ? 565 ALA A N    1 
ATOM   2979 C CA   . ALA A 1 565 ? 82.43000  121.98900 92.95000  1.000 31.50669  ? 565 ALA A CA   1 
ATOM   2980 C C    . ALA A 1 565 ? 81.59400  123.26300 92.93700  1.000 32.81773  ? 565 ALA A C    1 
ATOM   2981 O O    . ALA A 1 565 ? 81.86400  124.17700 93.72300  1.000 32.70801  ? 565 ALA A O    1 
ATOM   2982 C CB   . ALA A 1 565 ? 83.91600  122.33900 92.86500  1.000 28.67644  ? 565 ALA A CB   1 
ATOM   2983 N N    . ASN A 1 566 ? 80.59000  123.34400 92.06400  1.000 37.20159  ? 566 ASN A N    1 
ATOM   2984 C CA   . ASN A 1 566 ? 79.67900  124.48900 92.00100  1.000 33.78698  ? 566 ASN A CA   1 
ATOM   2985 C C    . ASN A 1 566 ? 80.42700  125.80400 91.77100  1.000 34.69554  ? 566 ASN A C    1 
ATOM   2986 O O    . ASN A 1 566 ? 80.24300  126.78700 92.49300  1.000 34.66621  ? 566 ASN A O    1 
ATOM   2987 C CB   . ASN A 1 566 ? 78.81700  124.56200 93.26400  1.000 32.21878  ? 566 ASN A CB   1 
ATOM   2988 C CG   . ASN A 1 566 ? 77.54500  125.36000 93.05600  1.000 40.40767  ? 566 ASN A CG   1 
ATOM   2989 O OD1  . ASN A 1 566 ? 77.37600  126.44000 93.62000  1.000 40.19430  ? 566 ASN A OD1  1 
ATOM   2990 N ND2  . ASN A 1 566 ? 76.63500  124.82200 92.25200  1.000 40.33684  ? 566 ASN A ND2  1 
ATOM   2991 N N    . PHE A 1 567 ? 81.27700  125.81800 90.74900  1.000 30.21667  ? 567 PHE A N    1 
ATOM   2992 C CA   . PHE A 1 567 ? 81.96100  127.04400 90.37100  1.000 28.41702  ? 567 PHE A CA   1 
ATOM   2993 C C    . PHE A 1 567 ? 80.95900  128.07600 89.85500  1.000 35.86650  ? 567 PHE A C    1 
ATOM   2994 O O    . PHE A 1 567 ? 79.84100  127.74800 89.44800  1.000 37.78375  ? 567 PHE A O    1 
ATOM   2995 C CB   . PHE A 1 567 ? 83.02800  126.76000 89.31500  1.000 28.64873  ? 567 PHE A CB   1 
ATOM   2996 C CG   . PHE A 1 567 ? 84.30500  126.20000 89.87800  1.000 30.80680  ? 567 PHE A CG   1 
ATOM   2997 C CD1  . PHE A 1 567 ? 84.37600  125.78100 91.19600  1.000 33.53547  ? 567 PHE A CD1  1 
ATOM   2998 C CD2  . PHE A 1 567 ? 85.43700  126.09700 89.08900  1.000 30.35592  ? 567 PHE A CD2  1 
ATOM   2999 C CE1  . PHE A 1 567 ? 85.54900  125.26800 91.71300  1.000 32.91152  ? 567 PHE A CE1  1 
ATOM   3000 C CE2  . PHE A 1 567 ? 86.61300  125.58500 89.59900  1.000 28.73943  ? 567 PHE A CE2  1 
ATOM   3001 C CZ   . PHE A 1 567 ? 86.67000  125.17000 90.91400  1.000 28.03342  ? 567 PHE A CZ   1 
ATOM   3002 N N    . LYS A 1 568 ? 81.37200  129.33900 89.87800  1.000 41.38913  ? 568 LYS A N    1 
ATOM   3003 C CA   . LYS A 1 568 ? 80.49900  130.43900 89.49700  1.000 40.25970  ? 568 LYS A CA   1 
ATOM   3004 C C    . LYS A 1 568 ? 80.55800  130.70300 87.99700  1.000 42.22107  ? 568 LYS A C    1 
ATOM   3005 O O    . LYS A 1 568 ? 81.55800  130.42300 87.33200  1.000 45.75200  ? 568 LYS A O    1 
ATOM   3006 C CB   . LYS A 1 568 ? 80.87300  131.71100 90.25700  1.000 42.08562  ? 568 LYS A CB   1 
ATOM   3007 C CG   . LYS A 1 568 ? 81.95800  132.52800 89.58500  1.000 41.51460  ? 568 LYS A CG   1 
ATOM   3008 C CD   . LYS A 1 568 ? 82.13200  133.87200 90.26700  1.000 42.62680  ? 568 LYS A CD   1 
ATOM   3009 C CE   . LYS A 1 568 ? 83.59200  134.28700 90.30100  1.000 45.64653  ? 568 LYS A CE   1 
ATOM   3010 N NZ   . LYS A 1 568 ? 83.91100  135.08100 91.51800  1.000 46.70435  ? 568 LYS A NZ   1 
ATOM   3011 N N    . GLU A 1 569 ? 79.46900  131.26000 87.47400  1.000 49.38068  ? 569 GLU A N    1 
ATOM   3012 C CA   . GLU A 1 569 ? 79.39600  131.58300 86.05600  1.000 50.07136  ? 569 GLU A CA   1 
ATOM   3013 C C    . GLU A 1 569 ? 80.39200  132.68700 85.70800  1.000 51.58217  ? 569 GLU A C    1 
ATOM   3014 O O    . GLU A 1 569 ? 80.53000  133.66000 86.45700  1.000 50.27426  ? 569 GLU A O    1 
ATOM   3015 C CB   . GLU A 1 569 ? 77.98200  132.01900 85.67700  1.000 50.97632  ? 569 GLU A CB   1 
ATOM   3016 C CG   . GLU A 1 569 ? 76.98600  130.87800 85.57700  1.000 52.68198  ? 569 GLU A CG   1 
ATOM   3017 C CD   . GLU A 1 569 ? 77.28600  129.94300 84.42100  1.000 55.03450  ? 569 GLU A CD   1 
ATOM   3018 O OE1  . GLU A 1 569 ? 77.78800  130.42200 83.38200  1.000 53.65819  ? 569 GLU A OE1  1 
ATOM   3019 O OE2  . GLU A 1 569 ? 77.02200  128.72900 84.55100  1.000 55.88566  ? 569 GLU A OE2  1 
ATOM   3020 N N    . PRO A 1 570 ? 81.10000  132.56600 84.58600  1.000 56.01319  ? 570 PRO A N    1 
ATOM   3021 C CA   . PRO A 1 570 ? 82.11000  133.57100 84.23500  1.000 52.07411  ? 570 PRO A CA   1 
ATOM   3022 C C    . PRO A 1 570 ? 81.51500  134.97200 84.20900  1.000 53.95563  ? 570 PRO A C    1 
ATOM   3023 O O    . PRO A 1 570 ? 80.39100  135.18100 83.74700  1.000 53.33363  ? 570 PRO A O    1 
ATOM   3024 C CB   . PRO A 1 570 ? 82.57800  133.13300 82.84300  1.000 50.03353  ? 570 PRO A CB   1 
ATOM   3025 C CG   . PRO A 1 570 ? 82.23400  131.69100 82.75400  1.000 51.94280  ? 570 PRO A CG   1 
ATOM   3026 C CD   . PRO A 1 570 ? 81.00300  131.49400 83.58200  1.000 53.59182  ? 570 PRO A CD   1 
ATOM   3027 N N    . GLU A 1 571 ? 82.28100  135.92900 84.72900  1.000 58.76575  ? 571 GLU A N    1 
ATOM   3028 C CA   . GLU A 1 571 ? 81.85900  137.32600 84.84300  1.000 57.48202  ? 571 GLU A CA   1 
ATOM   3029 C C    . GLU A 1 571 ? 80.96500  137.77900 83.69100  1.000 55.26626  ? 571 GLU A C    1 
ATOM   3030 O O    . GLU A 1 571 ? 81.45000  138.26500 82.67000  1.000 56.07119  ? 571 GLU A O    1 
ATOM   3031 C CB   . GLU A 1 571 ? 83.08500  138.23900 84.93000  1.000 55.83298  ? 571 GLU A CB   1 
ATOM   3032 N N    . ALA B 1 77  ? 101.19400 88.58000  105.60200 1.000 93.00478  ? 77  ALA B N    1 
ATOM   3033 C CA   . ALA B 1 77  ? 101.69500 88.09700  106.88300 1.000 93.06757  ? 77  ALA B CA   1 
ATOM   3034 C C    . ALA B 1 77  ? 102.58500 86.87600  106.68800 1.000 93.71052  ? 77  ALA B C    1 
ATOM   3035 O O    . ALA B 1 77  ? 103.79100 87.00200  106.46600 1.000 93.87069  ? 77  ALA B O    1 
ATOM   3036 C CB   . ALA B 1 77  ? 100.54000 87.77000  107.81700 1.000 92.78019  ? 77  ALA B CB   1 
ATOM   3037 N N    . TRP B 1 78  ? 101.97800 85.69100  106.78600 1.000 96.03086  ? 78  TRP B N    1 
ATOM   3038 C CA   . TRP B 1 78  ? 102.73000 84.45600  106.59800 1.000 95.24673  ? 78  TRP B CA   1 
ATOM   3039 C C    . TRP B 1 78  ? 103.44600 84.44400  105.25400 1.000 95.23908  ? 78  TRP B C    1 
ATOM   3040 O O    . TRP B 1 78  ? 104.58000 83.96500  105.15200 1.000 95.46944  ? 78  TRP B O    1 
ATOM   3041 C CB   . TRP B 1 78  ? 101.79800 83.25100  106.72600 1.000 94.35123  ? 78  TRP B CB   1 
ATOM   3042 C CG   . TRP B 1 78  ? 102.51500 81.93500  106.77700 1.000 95.93502  ? 78  TRP B CG   1 
ATOM   3043 C CD1  . TRP B 1 78  ? 103.12900 81.29400  105.74100 1.000 95.75711  ? 78  TRP B CD1  1 
ATOM   3044 C CD2  . TRP B 1 78  ? 102.69600 81.10100  107.92800 1.000 96.68919  ? 78  TRP B CD2  1 
ATOM   3045 N NE1  . TRP B 1 78  ? 103.67900 80.11200  106.17400 1.000 95.14187  ? 78  TRP B NE1  1 
ATOM   3046 C CE2  . TRP B 1 78  ? 103.42800 79.97000  107.51300 1.000 96.32482  ? 78  TRP B CE2  1 
ATOM   3047 C CE3  . TRP B 1 78  ? 102.31000 81.20000  109.26800 1.000 95.42411  ? 78  TRP B CE3  1 
ATOM   3048 C CZ2  . TRP B 1 78  ? 103.78100 78.94600  108.39000 1.000 95.47678  ? 78  TRP B CZ2  1 
ATOM   3049 C CZ3  . TRP B 1 78  ? 102.66200 80.18200  110.13700 1.000 95.00477  ? 78  TRP B CZ3  1 
ATOM   3050 C CH2  . TRP B 1 78  ? 103.38900 79.07100  109.69400 1.000 94.79536  ? 78  TRP B CH2  1 
ATOM   3051 N N    . GLU B 1 79  ? 102.79200 84.95000  104.20600 1.000 87.49280  ? 79  GLU B N    1 
ATOM   3052 C CA   . GLU B 1 79  ? 103.41000 84.96200  102.88300 1.000 87.84573  ? 79  GLU B CA   1 
ATOM   3053 C C    . GLU B 1 79  ? 104.67500 85.81300  102.87900 1.000 88.70726  ? 79  GLU B C    1 
ATOM   3054 O O    . GLU B 1 79  ? 105.72600 85.38500  102.38700 1.000 88.04116  ? 79  GLU B O    1 
ATOM   3055 C CB   . GLU B 1 79  ? 102.41200 85.47200  101.84400 1.000 87.44155  ? 79  GLU B CB   1 
ATOM   3056 N N    . MET B 1 80  ? 104.59100 87.02900  103.42500 1.000 84.73376  ? 80  MET B N    1 
ATOM   3057 C CA   . MET B 1 80  ? 105.76200 87.89600  103.45700 1.000 84.66529  ? 80  MET B CA   1 
ATOM   3058 C C    . MET B 1 80  ? 106.85400 87.31800  104.34500 1.000 84.37737  ? 80  MET B C    1 
ATOM   3059 O O    . MET B 1 80  ? 108.04400 87.51000  104.06900 1.000 83.69866  ? 80  MET B O    1 
ATOM   3060 C CB   . MET B 1 80  ? 105.37200 89.29700  103.93000 1.000 83.35303  ? 80  MET B CB   1 
ATOM   3061 C CG   . MET B 1 80  ? 106.48500 90.32600  103.79600 1.000 84.82064  ? 80  MET B CG   1 
ATOM   3062 S SD   . MET B 1 80  ? 106.23600 91.79700  104.81100 1.000 85.09868  ? 80  MET B SD   1 
ATOM   3063 C CE   . MET B 1 80  ? 105.49500 91.08300  106.27700 1.000 83.92225  ? 80  MET B CE   1 
ATOM   3064 N N    . GLY B 1 81  ? 106.47400 86.61500  105.41300 1.000 82.69346  ? 81  GLY B N    1 
ATOM   3065 C CA   . GLY B 1 81  ? 107.47500 86.00100  106.26900 1.000 83.26640  ? 81  GLY B CA   1 
ATOM   3066 C C    . GLY B 1 81  ? 108.20700 84.86600  105.57900 1.000 83.35231  ? 81  GLY B C    1 
ATOM   3067 O O    . GLY B 1 81  ? 109.43400 84.76400  105.65400 1.000 83.68613  ? 81  GLY B O    1 
ATOM   3068 N N    . VAL B 1 82  ? 107.46200 83.99400  104.89400 1.000 87.25736  ? 82  VAL B N    1 
ATOM   3069 C CA   . VAL B 1 82  ? 108.09200 82.88600  104.18400 1.000 88.17021  ? 82  VAL B CA   1 
ATOM   3070 C C    . VAL B 1 82  ? 108.95900 83.40800  103.04700 1.000 87.29936  ? 82  VAL B C    1 
ATOM   3071 O O    . VAL B 1 82  ? 110.04800 82.88200  102.78700 1.000 87.44477  ? 82  VAL B O    1 
ATOM   3072 C CB   . VAL B 1 82  ? 107.03200 81.89000  103.67700 1.000 88.28928  ? 82  VAL B CB   1 
ATOM   3073 C CG1  . VAL B 1 82  ? 106.55200 80.99800  104.81200 1.000 86.77033  ? 82  VAL B CG1  1 
ATOM   3074 C CG2  . VAL B 1 82  ? 105.87100 82.62300  103.02800 1.000 87.19257  ? 82  VAL B CG2  1 
ATOM   3075 N N    . SER B 1 83  ? 108.49400 84.44600  102.34800 1.000 84.88083  ? 83  SER B N    1 
ATOM   3076 C CA   . SER B 1 83  ? 109.30400 85.02700  101.28300 1.000 85.29342  ? 83  SER B CA   1 
ATOM   3077 C C    . SER B 1 83  ? 110.49400 85.79200  101.84900 1.000 86.72984  ? 83  SER B C    1 
ATOM   3078 O O    . SER B 1 83  ? 111.60200 85.71500  101.30700 1.000 86.10210  ? 83  SER B O    1 
ATOM   3079 C CB   . SER B 1 83  ? 108.44600 85.93800  100.40500 1.000 84.46774  ? 83  SER B CB   1 
ATOM   3080 O OG   . SER B 1 83  ? 107.54300 86.70100  101.18600 1.000 86.57269  ? 83  SER B OG   1 
ATOM   3081 N N    . ASP B 1 84  ? 110.28600 86.53300  102.93500 1.000 73.61332  ? 84  ASP B N    1 
ATOM   3082 C CA   . ASP B 1 84  ? 111.33600 87.35300  103.54200 1.000 70.85337  ? 84  ASP B CA   1 
ATOM   3083 C C    . ASP B 1 84  ? 111.63100 86.86400  104.95200 1.000 71.40586  ? 84  ASP B C    1 
ATOM   3084 O O    . ASP B 1 84  ? 110.93200 87.25100  105.90600 1.000 73.13074  ? 84  ASP B O    1 
ATOM   3085 C CB   . ASP B 1 84  ? 110.92900 88.82400  103.55900 1.000 69.92043  ? 84  ASP B CB   1 
ATOM   3086 C CG   . ASP B 1 84  ? 112.04000 89.74000  103.08900 1.000 72.71956  ? 84  ASP B CG   1 
ATOM   3087 O OD1  . ASP B 1 84  ? 113.18200 89.25900  102.93100 1.000 71.28375  ? 84  ASP B OD1  1 
ATOM   3088 O OD2  . ASP B 1 84  ? 111.77200 90.94100  102.87600 1.000 74.22173  ? 84  ASP B OD2  1 
ATOM   3089 N N    . PRO B 1 85  ? 112.64800 86.01800  105.14200 1.000 60.76594  ? 85  PRO B N    1 
ATOM   3090 C CA   . PRO B 1 85  ? 113.00500 85.57700  106.49800 1.000 60.33119  ? 85  PRO B CA   1 
ATOM   3091 C C    . PRO B 1 85  ? 113.80300 86.59700  107.29700 1.000 57.84274  ? 85  PRO B C    1 
ATOM   3092 O O    . PRO B 1 85  ? 113.98400 86.40100  108.50600 1.000 58.40909  ? 85  PRO B O    1 
ATOM   3093 C CB   . PRO B 1 85  ? 113.83400 84.31200  106.24300 1.000 58.91850  ? 85  PRO B CB   1 
ATOM   3094 C CG   . PRO B 1 85  ? 114.44100 84.53300  104.90000 1.000 58.95381  ? 85  PRO B CG   1 
ATOM   3095 C CD   . PRO B 1 85  ? 113.45900 85.35500  104.10500 1.000 59.45841  ? 85  PRO B CD   1 
ATOM   3096 N N    . ARG B 1 86  ? 114.28400 87.66900  106.66500 1.000 45.17412  ? 86  ARG B N    1 
ATOM   3097 C CA   . ARG B 1 86  ? 115.02600 88.70000  107.38600 1.000 47.30604  ? 86  ARG B CA   1 
ATOM   3098 C C    . ARG B 1 86  ? 114.12900 89.47500  108.34600 1.000 48.57426  ? 86  ARG B C    1 
ATOM   3099 O O    . ARG B 1 86  ? 114.54800 89.82000  109.45800 1.000 50.89105  ? 86  ARG B O    1 
ATOM   3100 C CB   . ARG B 1 86  ? 115.68700 89.65000  106.38900 1.000 43.95533  ? 86  ARG B CB   1 
ATOM   3101 C CG   . ARG B 1 86  ? 116.67400 88.97000  105.45700 1.000 46.41348  ? 86  ARG B CG   1 
ATOM   3102 C CD   . ARG B 1 86  ? 117.78400 89.91300  105.02800 1.000 46.82286  ? 86  ARG B CD   1 
ATOM   3103 N NE   . ARG B 1 86  ? 117.27000 91.22900  104.67200 1.000 48.32247  ? 86  ARG B NE   1 
ATOM   3104 C CZ   . ARG B 1 86  ? 117.90600 92.09600  103.89500 1.000 49.61525  ? 86  ARG B CZ   1 
ATOM   3105 N NH1  . ARG B 1 86  ? 119.09000 91.81800  103.37600 1.000 46.02597  ? 86  ARG B NH1  1 
ATOM   3106 N NH2  . ARG B 1 86  ? 117.33900 93.26900  103.63200 1.000 46.78012  ? 86  ARG B NH2  1 
ATOM   3107 N N    . LYS B 1 87  ? 112.89600 89.76500  107.92800 1.000 38.79194  ? 87  LYS B N    1 
ATOM   3108 C CA   . LYS B 1 87  ? 111.96600 90.49100  108.78700 1.000 38.51725  ? 87  LYS B CA   1 
ATOM   3109 C C    . LYS B 1 87  ? 111.69200 89.73300  110.08300 1.000 39.68955  ? 87  LYS B C    1 
ATOM   3110 O O    . LYS B 1 87  ? 111.61700 90.33700  111.16300 1.000 44.18057  ? 87  LYS B O    1 
ATOM   3111 C CB   . LYS B 1 87  ? 110.67100 90.74400  108.01900 1.000 39.74496  ? 87  LYS B CB   1 
ATOM   3112 C CG   . LYS B 1 87  ? 110.84500 91.68900  106.83900 1.000 38.93723  ? 87  LYS B CG   1 
ATOM   3113 C CD   . LYS B 1 87  ? 109.62400 92.55800  106.60600 1.000 41.70772  ? 87  LYS B CD   1 
ATOM   3114 C CE   . LYS B 1 87  ? 109.96100 93.73000  105.69900 1.000 41.99063  ? 87  LYS B CE   1 
ATOM   3115 N NZ   . LYS B 1 87  ? 108.80700 94.13700  104.85200 1.000 40.99791  ? 87  LYS B NZ   1 
ATOM   3116 N N    . ILE B 1 88  ? 111.58000 88.40600  110.00400 1.000 30.81696  ? 88  ILE B N    1 
ATOM   3117 C CA   . ILE B 1 88  ? 111.32800 87.61500  111.20300 1.000 35.43900  ? 88  ILE B CA   1 
ATOM   3118 C C    . ILE B 1 88  ? 112.53600 87.65500  112.12900 1.000 41.26922  ? 88  ILE B C    1 
ATOM   3119 O O    . ILE B 1 88  ? 112.39500 87.71700  113.35800 1.000 44.66905  ? 88  ILE B O    1 
ATOM   3120 C CB   . ILE B 1 88  ? 110.96200 86.17000  110.81900 1.000 37.95366  ? 88  ILE B CB   1 
ATOM   3121 C CG1  . ILE B 1 88  ? 109.62700 86.13400  110.07600 1.000 39.61330  ? 88  ILE B CG1  1 
ATOM   3122 C CG2  . ILE B 1 88  ? 110.91100 85.28400  112.05300 1.000 41.48157  ? 88  ILE B CG2  1 
ATOM   3123 C CD1  . ILE B 1 88  ? 109.32700 84.79900  109.43900 1.000 39.68044  ? 88  ILE B CD1  1 
ATOM   3124 N N    . VAL B 1 89  ? 113.73900 87.67000  111.55700 1.000 31.23568  ? 89  VAL B N    1 
ATOM   3125 C CA   . VAL B 1 89  ? 114.94600 87.75000  112.37100 1.000 30.27811  ? 89  VAL B CA   1 
ATOM   3126 C C    . VAL B 1 89  ? 115.01000 89.09100  113.08900 1.000 26.29486  ? 89  VAL B C    1 
ATOM   3127 O O    . VAL B 1 89  ? 115.30000 89.15600  114.28700 1.000 37.79351  ? 89  VAL B O    1 
ATOM   3128 C CB   . VAL B 1 89  ? 116.19500 87.51000  111.50400 1.000 30.48123  ? 89  VAL B CB   1 
ATOM   3129 C CG1  . VAL B 1 89  ? 117.45700 87.78600  112.30400 1.000 35.05254  ? 89  VAL B CG1  1 
ATOM   3130 C CG2  . VAL B 1 89  ? 116.20000 86.08900  110.96700 1.000 30.73052  ? 89  VAL B CG2  1 
ATOM   3131 N N    . PHE B 1 90  ? 114.76200 90.18100  112.36200 1.000 7.83417   ? 90  PHE B N    1 
ATOM   3132 C CA   . PHE B 1 90  ? 114.76800 91.50300  112.98200 1.000 17.71538  ? 90  PHE B CA   1 
ATOM   3133 C C    . PHE B 1 90  ? 113.74500 91.59500  114.11300 1.000 22.59332  ? 90  PHE B C    1 
ATOM   3134 O O    . PHE B 1 90  ? 114.04400 92.11900  115.20000 1.000 23.71597  ? 90  PHE B O    1 
ATOM   3135 C CB   . PHE B 1 90  ? 114.49900 92.56200  111.91000 1.000 14.28680  ? 90  PHE B CB   1 
ATOM   3136 C CG   . PHE B 1 90  ? 114.49600 93.97200  112.42400 1.000 20.04191  ? 90  PHE B CG   1 
ATOM   3137 C CD1  . PHE B 1 90  ? 115.64800 94.53800  112.94100 1.000 18.14331  ? 90  PHE B CD1  1 
ATOM   3138 C CD2  . PHE B 1 90  ? 113.34500 94.74000  112.36800 1.000 19.52388  ? 90  PHE B CD2  1 
ATOM   3139 C CE1  . PHE B 1 90  ? 115.64700 95.83800  113.40500 1.000 18.55927  ? 90  PHE B CE1  1 
ATOM   3140 C CE2  . PHE B 1 90  ? 113.33900 96.04000  112.83000 1.000 13.69917  ? 90  PHE B CE2  1 
ATOM   3141 C CZ   . PHE B 1 90  ? 114.49100 96.58900  113.34900 1.000 18.84103  ? 90  PHE B CZ   1 
ATOM   3142 N N    . SER B 1 91  ? 112.53700 91.06600  113.88700 1.000 19.81373  ? 91  SER B N    1 
ATOM   3143 C CA   . SER B 1 91  ? 111.50100 91.16000  114.91100 1.000 14.75542  ? 91  SER B CA   1 
ATOM   3144 C C    . SER B 1 91  ? 111.81700 90.29700  116.12700 1.000 20.56934  ? 91  SER B C    1 
ATOM   3145 O O    . SER B 1 91  ? 111.55400 90.71200  117.26600 1.000 20.04345  ? 91  SER B O    1 
ATOM   3146 C CB   . SER B 1 91  ? 110.15200 90.77000  114.31400 1.000 15.11772  ? 91  SER B CB   1 
ATOM   3147 O OG   . SER B 1 91  ? 109.97300 91.37400  113.04600 1.000 16.52997  ? 91  SER B OG   1 
ATOM   3148 N N    . ALA B 1 92  ? 112.47500 89.15200  115.92900 1.000 16.29111  ? 92  ALA B N    1 
ATOM   3149 C CA   . ALA B 1 92  ? 112.84500 88.35400  117.08800 1.000 11.37254  ? 92  ALA B CA   1 
ATOM   3150 C C    . ALA B 1 92  ? 114.07600 88.91100  117.78200 1.000 20.51660  ? 92  ALA B C    1 
ATOM   3151 O O    . ALA B 1 92  ? 114.24100 88.69900  118.98800 1.000 27.33362  ? 92  ALA B O    1 
ATOM   3152 C CB   . ALA B 1 92  ? 113.09000 86.90200  116.67700 1.000 15.40954  ? 92  ALA B CB   1 
ATOM   3153 N N    . LYS B 1 93  ? 114.87300 89.71400  117.07900 1.000 14.61205  ? 93  LYS B N    1 
ATOM   3154 C CA   . LYS B 1 93  ? 116.00500 90.36800  117.71900 1.000 14.28240  ? 93  LYS B CA   1 
ATOM   3155 C C    . LYS B 1 93  ? 115.51600 91.47200  118.64200 1.000 19.13741  ? 93  LYS B C    1 
ATOM   3156 O O    . LYS B 1 93  ? 116.00600 91.62100  119.77100 1.000 23.62246  ? 93  LYS B O    1 
ATOM   3157 C CB   . LYS B 1 93  ? 116.94500 90.93500  116.65700 1.000 17.97674  ? 93  LYS B CB   1 
ATOM   3158 C CG   . LYS B 1 93  ? 118.01000 89.97200  116.17700 1.000 19.08758  ? 93  LYS B CG   1 
ATOM   3159 C CD   . LYS B 1 93  ? 119.24900 90.72000  115.72200 1.000 22.56569  ? 93  LYS B CD   1 
ATOM   3160 C CE   . LYS B 1 93  ? 119.03400 91.36000  114.36200 1.000 16.58372  ? 93  LYS B CE   1 
ATOM   3161 N NZ   . LYS B 1 93  ? 120.31400 91.80600  113.75500 1.000 15.29398  ? 93  LYS B NZ   1 
ATOM   3162 N N    . ILE B 1 94  ? 114.51000 92.22500  118.19400 1.000 10.74302  ? 94  ILE B N    1 
ATOM   3163 C CA   . ILE B 1 94  ? 113.95500 93.26300  119.05600 1.000 14.13252  ? 94  ILE B CA   1 
ATOM   3164 C C    . ILE B 1 94  ? 113.21600 92.63600  120.23400 1.000 16.23744  ? 94  ILE B C    1 
ATOM   3165 O O    . ILE B 1 94  ? 113.30500 93.12200  121.37200 1.000 24.73781  ? 94  ILE B O    1 
ATOM   3166 C CB   . ILE B 1 94  ? 113.04900 94.20700  118.24600 1.000 19.13891  ? 94  ILE B CB   1 
ATOM   3167 C CG1  . ILE B 1 94  ? 113.89500 95.05500  117.29600 1.000 15.57303  ? 94  ILE B CG1  1 
ATOM   3168 C CG2  . ILE B 1 94  ? 112.22900 95.08900  119.17500 1.000 16.91219  ? 94  ILE B CG2  1 
ATOM   3169 C CD1  . ILE B 1 94  ? 113.14600 96.20000  116.67000 1.000 16.92905  ? 94  ILE B CD1  1 
ATOM   3170 N N    . GLY B 1 95  ? 112.49300 91.53800  119.99300 1.000 14.78712  ? 95  GLY B N    1 
ATOM   3171 C CA   . GLY B 1 95  ? 111.86100 90.84300  121.10300 1.000 7.33027   ? 95  GLY B CA   1 
ATOM   3172 C C    . GLY B 1 95  ? 112.86200 90.35100  122.13300 1.000 13.08743  ? 95  GLY B C    1 
ATOM   3173 O O    . GLY B 1 95  ? 112.63500 90.46800  123.34200 1.000 19.32590  ? 95  GLY B O    1 
ATOM   3174 N N    . LEU B 1 96  ? 114.00200 89.82600  121.67300 1.000 23.30814  ? 96  LEU B N    1 
ATOM   3175 C CA   . LEU B 1 96  ? 115.01800 89.34500  122.60400 1.000 19.88329  ? 96  LEU B CA   1 
ATOM   3176 C C    . LEU B 1 96  ? 115.63400 90.49200  123.39400 1.000 22.42300  ? 96  LEU B C    1 
ATOM   3177 O O    . LEU B 1 96  ? 115.88000 90.36200  124.60000 1.000 30.08136  ? 96  LEU B O    1 
ATOM   3178 C CB   . LEU B 1 96  ? 116.09800 88.57400  121.84600 1.000 18.16564  ? 96  LEU B CB   1 
ATOM   3179 C CG   . LEU B 1 96  ? 117.20800 87.93900  122.68500 1.000 23.73077  ? 96  LEU B CG   1 
ATOM   3180 C CD1  . LEU B 1 96  ? 116.68700 86.72800  123.44000 1.000 22.49990  ? 96  LEU B CD1  1 
ATOM   3181 C CD2  . LEU B 1 96  ? 118.39000 87.56100  121.80800 1.000 22.02310  ? 96  LEU B CD2  1 
ATOM   3182 N N    . ALA B 1 97  ? 115.87700 91.63100  122.74000 1.000 23.53474  ? 97  ALA B N    1 
ATOM   3183 C CA   . ALA B 1 97  ? 116.45500 92.76200  123.46000 1.000 19.30302  ? 97  ALA B CA   1 
ATOM   3184 C C    . ALA B 1 97  ? 115.50000 93.26700  124.53500 1.000 15.46151  ? 97  ALA B C    1 
ATOM   3185 O O    . ALA B 1 97  ? 115.92000 93.57300  125.66300 1.000 23.44465  ? 97  ALA B O    1 
ATOM   3186 C CB   . ALA B 1 97  ? 116.81000 93.88200  122.48400 1.000 19.14943  ? 97  ALA B CB   1 
ATOM   3187 N N    . LEU B 1 98  ? 114.20400 93.32500  124.21800 1.000 18.16018  ? 98  LEU B N    1 
ATOM   3188 C CA   . LEU B 1 98  ? 113.24300 93.76300  125.22500 1.000 15.27807  ? 98  LEU B CA   1 
ATOM   3189 C C    . LEU B 1 98  ? 113.15300 92.76200  126.37000 1.000 20.05663  ? 98  LEU B C    1 
ATOM   3190 O O    . LEU B 1 98  ? 113.08400 93.15700  127.54100 1.000 25.44216  ? 98  LEU B O    1 
ATOM   3191 C CB   . LEU B 1 98  ? 111.86800 93.97800  124.59400 1.000 17.73109  ? 98  LEU B CB   1 
ATOM   3192 C CG   . LEU B 1 98  ? 111.65300 95.25500  123.78000 1.000 19.17964  ? 98  LEU B CG   1 
ATOM   3193 C CD1  . LEU B 1 98  ? 110.27000 95.25100  123.14900 1.000 18.81368  ? 98  LEU B CD1  1 
ATOM   3194 C CD2  . LEU B 1 98  ? 111.84700 96.48800  124.64400 1.000 16.06679  ? 98  LEU B CD2  1 
ATOM   3195 N N    . THR B 1 99  ? 113.18700 91.46100  126.06300 1.000 25.07441  ? 99  THR B N    1 
ATOM   3196 C CA   . THR B 1 99  ? 113.08700 90.47500  127.13100 1.000 20.73064  ? 99  THR B CA   1 
ATOM   3197 C C    . THR B 1 99  ? 114.34100 90.43700  127.99300 1.000 28.43004  ? 99  THR B C    1 
ATOM   3198 O O    . THR B 1 99  ? 114.25300 90.11900  129.18500 1.000 30.20466  ? 99  THR B O    1 
ATOM   3199 C CB   . THR B 1 99  ? 112.81700 89.09000  126.54200 1.000 24.55289  ? 99  THR B CB   1 
ATOM   3200 O OG1  . THR B 1 99  ? 111.43100 88.97500  126.19900 1.000 28.74856  ? 99  THR B OG1  1 
ATOM   3201 C CG2  . THR B 1 99  ? 113.17400 88.00400  127.54100 1.000 27.59216  ? 99  THR B CG2  1 
ATOM   3202 N N    . ILE B 1 100 ? 115.47600 90.89100  127.46600 1.000 27.37783  ? 100 ILE B N    1 
ATOM   3203 C CA   . ILE B 1 100 ? 116.68800 90.94300  128.27600 1.000 24.16579  ? 100 ILE B CA   1 
ATOM   3204 C C    . ILE B 1 100 ? 116.66300 92.15900  129.19000 1.000 28.92164  ? 100 ILE B C    1 
ATOM   3205 O O    . ILE B 1 100 ? 117.00800 92.07200  130.37600 1.000 33.39852  ? 100 ILE B O    1 
ATOM   3206 C CB   . ILE B 1 100 ? 117.94100 90.93300  127.38100 1.000 29.01988  ? 100 ILE B CB   1 
ATOM   3207 C CG1  . ILE B 1 100 ? 118.00000 89.64600  126.55700 1.000 30.33003  ? 100 ILE B CG1  1 
ATOM   3208 C CG2  . ILE B 1 100 ? 119.19800 91.08800  128.22200 1.000 26.39270  ? 100 ILE B CG2  1 
ATOM   3209 C CD1  . ILE B 1 100 ? 119.26500 89.50400  125.74500 1.000 29.86528  ? 100 ILE B CD1  1 
ATOM   3210 N N    . VAL B 1 101 ? 116.29800 93.32300  128.64500 1.000 30.50529  ? 101 VAL B N    1 
ATOM   3211 C CA   . VAL B 1 101 ? 116.12800 94.49200  129.50500 1.000 28.06795  ? 101 VAL B CA   1 
ATOM   3212 C C    . VAL B 1 101 ? 115.11500 94.20200  130.61000 1.000 29.30379  ? 101 VAL B C    1 
ATOM   3213 O O    . VAL B 1 101 ? 115.27900 94.64500  131.75200 1.000 28.46721  ? 101 VAL B O    1 
ATOM   3214 C CB   . VAL B 1 101 ? 115.72600 95.72500  128.67400 1.000 31.81890  ? 101 VAL B CB   1 
ATOM   3215 C CG1  . VAL B 1 101 ? 115.23300 96.83300  129.58500 1.000 29.65892  ? 101 VAL B CG1  1 
ATOM   3216 C CG2  . VAL B 1 101 ? 116.90500 96.21000  127.85200 1.000 30.33150  ? 101 VAL B CG2  1 
ATOM   3217 N N    . ALA B 1 102 ? 114.05500 93.44900  130.29300 1.000 35.12485  ? 102 ALA B N    1 
ATOM   3218 C CA   . ALA B 1 102 ? 113.07900 93.08200  131.31700 1.000 31.60927  ? 102 ALA B CA   1 
ATOM   3219 C C    . ALA B 1 102 ? 113.68000 92.15400  132.36900 1.000 36.77033  ? 102 ALA B C    1 
ATOM   3220 O O    . ALA B 1 102 ? 113.45700 92.34300  133.57300 1.000 39.01879  ? 102 ALA B O    1 
ATOM   3221 C CB   . ALA B 1 102 ? 111.85600 92.43700  130.66900 1.000 32.37008  ? 102 ALA B CB   1 
ATOM   3222 N N    . LEU B 1 103 ? 114.43600 91.13800  131.93800 1.000 48.38661  ? 103 LEU B N    1 
ATOM   3223 C CA   . LEU B 1 103 ? 115.03600 90.21800  132.89900 1.000 43.98748  ? 103 LEU B CA   1 
ATOM   3224 C C    . LEU B 1 103 ? 115.97800 90.94600  133.84700 1.000 45.21354  ? 103 LEU B C    1 
ATOM   3225 O O    . LEU B 1 103 ? 115.97200 90.68900  135.05600 1.000 44.79812  ? 103 LEU B O    1 
ATOM   3226 C CB   . LEU B 1 103 ? 115.77700 89.09400  132.17400 1.000 46.09286  ? 103 LEU B CB   1 
ATOM   3227 C CG   . LEU B 1 103 ? 114.93000 87.93900  131.63900 1.000 49.58230  ? 103 LEU B CG   1 
ATOM   3228 C CD1  . LEU B 1 103 ? 115.79600 86.95600  130.87000 1.000 46.37776  ? 103 LEU B CD1  1 
ATOM   3229 C CD2  . LEU B 1 103 ? 114.20900 87.24100  132.77900 1.000 44.28882  ? 103 LEU B CD2  1 
ATOM   3230 N N    . LEU B 1 104 ? 116.79600 91.86000  133.32200 1.000 47.06716  ? 104 LEU B N    1 
ATOM   3231 C CA   . LEU B 1 104 ? 117.74200 92.54600  134.19800 1.000 45.81083  ? 104 LEU B CA   1 
ATOM   3232 C C    . LEU B 1 104 ? 117.07100 93.49300  135.18800 1.000 47.10216  ? 104 LEU B C    1 
ATOM   3233 O O    . LEU B 1 104 ? 117.78200 94.17800  135.93000 1.000 48.81434  ? 104 LEU B O    1 
ATOM   3234 C CB   . LEU B 1 104 ? 118.76900 93.32300  133.37300 1.000 44.07389  ? 104 LEU B CB   1 
ATOM   3235 C CG   . LEU B 1 104 ? 119.54800 92.54500  132.31300 1.000 48.31218  ? 104 LEU B CG   1 
ATOM   3236 C CD1  . LEU B 1 104 ? 120.00000 93.47200  131.19800 1.000 47.42452  ? 104 LEU B CD1  1 
ATOM   3237 C CD2  . LEU B 1 104 ? 120.73800 91.84200  132.94500 1.000 47.01328  ? 104 LEU B CD2  1 
ATOM   3238 N N    . ILE B 1 105 ? 115.74000 93.55300  135.22200 1.000 48.25885  ? 105 ILE B N    1 
ATOM   3239 C CA   . ILE B 1 105 ? 115.02800 94.45300  136.12400 1.000 47.79064  ? 105 ILE B CA   1 
ATOM   3240 C C    . ILE B 1 105 ? 114.09700 93.64900  137.02100 1.000 48.19823  ? 105 ILE B C    1 
ATOM   3241 O O    . ILE B 1 105 ? 113.80800 94.05200  138.15400 1.000 47.22336  ? 105 ILE B O    1 
ATOM   3242 C CB   . ILE B 1 105 ? 114.25300 95.53500  135.35000 1.000 46.95382  ? 105 ILE B CB   1 
ATOM   3243 C CG1  . ILE B 1 105 ? 115.22100 96.47800  134.63400 1.000 46.40053  ? 105 ILE B CG1  1 
ATOM   3244 C CG2  . ILE B 1 105 ? 113.33600 96.30600  136.28400 1.000 44.80888  ? 105 ILE B CG2  1 
ATOM   3245 C CD1  . ILE B 1 105 ? 114.55200 97.40500  133.64700 1.000 47.57445  ? 105 ILE B CD1  1 
ATOM   3246 N N    . PHE B 1 106 ? 113.61900 92.50500  136.52500 1.000 59.72748  ? 106 PHE B N    1 
ATOM   3247 C CA   . PHE B 1 106 ? 112.74900 91.66200  137.33900 1.000 56.74488  ? 106 PHE B CA   1 
ATOM   3248 C C    . PHE B 1 106 ? 113.49800 90.90300  138.42700 1.000 57.45971  ? 106 PHE B C    1 
ATOM   3249 O O    . PHE B 1 106 ? 112.86600 90.43500  139.38000 1.000 59.86733  ? 106 PHE B O    1 
ATOM   3250 C CB   . PHE B 1 106 ? 111.98700 90.67100  136.45900 1.000 56.79629  ? 106 PHE B CB   1 
ATOM   3251 C CG   . PHE B 1 106 ? 110.72800 91.23200  135.86600 1.000 58.00704  ? 106 PHE B CG   1 
ATOM   3252 C CD1  . PHE B 1 106 ? 110.40700 92.56900  136.02700 1.000 59.05859  ? 106 PHE B CD1  1 
ATOM   3253 C CD2  . PHE B 1 106 ? 109.85900 90.42000  135.15800 1.000 57.57951  ? 106 PHE B CD2  1 
ATOM   3254 C CE1  . PHE B 1 106 ? 109.24800 93.08700  135.48700 1.000 59.96681  ? 106 PHE B CE1  1 
ATOM   3255 C CE2  . PHE B 1 106 ? 108.69700 90.93300  134.61600 1.000 59.04892  ? 106 PHE B CE2  1 
ATOM   3256 C CZ   . PHE B 1 106 ? 108.39200 92.26700  134.78000 1.000 58.76244  ? 106 PHE B CZ   1 
ATOM   3257 N N    . TYR B 1 107 ? 114.81700 90.76600  138.31700 1.000 69.99102  ? 107 TYR B N    1 
ATOM   3258 C CA   . TYR B 1 107 ? 115.58800 89.96600  139.26000 1.000 69.79289  ? 107 TYR B CA   1 
ATOM   3259 C C    . TYR B 1 107 ? 116.26600 90.79200  140.34400 1.000 71.62392  ? 107 TYR B C    1 
ATOM   3260 O O    . TYR B 1 107 ? 116.98900 90.22700  141.17000 1.000 71.27189  ? 107 TYR B O    1 
ATOM   3261 C CB   . TYR B 1 107 ? 116.62900 89.12500  138.51500 1.000 69.02300  ? 107 TYR B CB   1 
ATOM   3262 C CG   . TYR B 1 107 ? 116.02500 87.94800  137.78300 1.000 70.76776  ? 107 TYR B CG   1 
ATOM   3263 C CD1  . TYR B 1 107 ? 114.82700 87.38700  138.20800 1.000 69.19220  ? 107 TYR B CD1  1 
ATOM   3264 C CD2  . TYR B 1 107 ? 116.65200 87.39300  136.67600 1.000 71.25678  ? 107 TYR B CD2  1 
ATOM   3265 C CE1  . TYR B 1 107 ? 114.26700 86.31100  137.54900 1.000 69.35498  ? 107 TYR B CE1  1 
ATOM   3266 C CE2  . TYR B 1 107 ? 116.09900 86.31500  136.00900 1.000 72.53081  ? 107 TYR B CE2  1 
ATOM   3267 C CZ   . TYR B 1 107 ? 114.90700 85.77800  136.45000 1.000 73.17930  ? 107 TYR B CZ   1 
ATOM   3268 O OH   . TYR B 1 107 ? 114.35200 84.70500  135.79100 1.000 73.35839  ? 107 TYR B OH   1 
ATOM   3269 N N    . GLN B 1 108 ? 116.05600 92.10400  140.36500 1.000 77.46731  ? 108 GLN B N    1 
ATOM   3270 C CA   . GLN B 1 108 ? 116.55700 92.93600  141.44800 1.000 76.53721  ? 108 GLN B CA   1 
ATOM   3271 C C    . GLN B 1 108 ? 115.53300 92.99000  142.57400 1.000 76.58562  ? 108 GLN B C    1 
ATOM   3272 O O    . GLN B 1 108 ? 114.32600 92.87700  142.34600 1.000 75.69905  ? 108 GLN B O    1 
ATOM   3273 C CB   . GLN B 1 108 ? 116.86700 94.35000  140.95500 1.000 76.16786  ? 108 GLN B CB   1 
ATOM   3274 C CG   . GLN B 1 108 ? 117.68600 94.39600  139.68000 1.000 76.78140  ? 108 GLN B CG   1 
ATOM   3275 C CD   . GLN B 1 108 ? 119.04000 93.73800  139.83800 1.000 76.93502  ? 108 GLN B CD   1 
ATOM   3276 O OE1  . GLN B 1 108 ? 119.18900 92.53600  139.61700 1.000 76.62238  ? 108 GLN B OE1  1 
ATOM   3277 N NE2  . GLN B 1 108 ? 120.03800 94.52400  140.22400 1.000 76.29207  ? 108 GLN B NE2  1 
ATOM   3278 N N    . GLU B 1 109 ? 116.03000 93.14900  143.79600 1.000 91.17184  ? 109 GLU B N    1 
ATOM   3279 C CA   . GLU B 1 109 ? 115.16600 93.12800  144.96500 1.000 90.87347  ? 109 GLU B CA   1 
ATOM   3280 C C    . GLU B 1 109 ? 113.99800 94.09300  144.76800 1.000 91.48848  ? 109 GLU B C    1 
ATOM   3281 O O    . GLU B 1 109 ? 114.21000 95.22900  144.32100 1.000 91.18529  ? 109 GLU B O    1 
ATOM   3282 C CB   . GLU B 1 109 ? 115.95700 93.50100  146.22000 1.000 89.96459  ? 109 GLU B CB   1 
ATOM   3283 C CG   . GLU B 1 109 ? 115.20700 93.28000  147.52500 1.000 89.72139  ? 109 GLU B CG   1 
ATOM   3284 C CD   . GLU B 1 109 ? 114.28800 94.43400  147.87600 1.000 90.73043  ? 109 GLU B CD   1 
ATOM   3285 O OE1  . GLU B 1 109 ? 114.62100 95.58700  147.52900 1.000 91.05977  ? 109 GLU B OE1  1 
ATOM   3286 O OE2  . GLU B 1 109 ? 113.23400 94.18800  148.49900 1.000 89.66144  ? 109 GLU B OE2  1 
ATOM   3287 N N    . PRO B 1 110 ? 112.76400 93.68400  145.07900 1.000 92.05134  ? 110 PRO B N    1 
ATOM   3288 C CA   . PRO B 1 110 ? 111.61100 94.56500  144.84700 1.000 91.17106  ? 110 PRO B CA   1 
ATOM   3289 C C    . PRO B 1 110 ? 111.78000 95.92700  145.49900 1.000 90.61895  ? 110 PRO B C    1 
ATOM   3290 O O    . PRO B 1 110 ? 111.98300 96.01900  146.71400 1.000 89.56650  ? 110 PRO B O    1 
ATOM   3291 C CB   . PRO B 1 110 ? 110.43800 93.78900  145.46600 1.000 90.67966  ? 110 PRO B CB   1 
ATOM   3292 C CG   . PRO B 1 110 ? 111.06300 92.68600  146.27800 1.000 91.46828  ? 110 PRO B CG   1 
ATOM   3293 C CD   . PRO B 1 110 ? 112.36200 92.37700  145.61800 1.000 90.21902  ? 110 PRO B CD   1 
ATOM   3294 N N    . ASN B 1 111 ? 111.69900 96.99300  144.70200 1.000 81.00431  ? 111 ASN B N    1 
ATOM   3295 C CA   . ASN B 1 111 ? 111.83300 98.34600  145.21000 1.000 79.72655  ? 111 ASN B CA   1 
ATOM   3296 C C    . ASN B 1 111 ? 110.78100 99.23700  144.56500 1.000 81.54305  ? 111 ASN B C    1 
ATOM   3297 O O    . ASN B 1 111 ? 110.52500 99.12300  143.35700 1.000 82.38115  ? 111 ASN B O    1 
ATOM   3298 C CB   . ASN B 1 111 ? 113.23200 98.91500  144.93900 1.000 79.95454  ? 111 ASN B CB   1 
ATOM   3299 C CG   . ASN B 1 111 ? 113.41100 100.31000 145.50200 1.000 80.97029  ? 111 ASN B CG   1 
ATOM   3300 O OD1  . ASN B 1 111 ? 113.56500 101.27800 144.75700 1.000 80.92443  ? 111 ASN B OD1  1 
ATOM   3301 N ND2  . ASN B 1 111 ? 113.38900 100.42200 146.82500 1.000 80.83111  ? 111 ASN B ND2  1 
ATOM   3302 N N    . PRO B 1 112 ? 110.15400 100.12500 145.34100 1.000 78.50444  ? 112 PRO B N    1 
ATOM   3303 C CA   . PRO B 1 112 ? 109.19400 101.05900 144.73200 1.000 78.74829  ? 112 PRO B CA   1 
ATOM   3304 C C    . PRO B 1 112 ? 109.85400 102.11800 143.86700 1.000 76.54425  ? 112 PRO B C    1 
ATOM   3305 O O    . PRO B 1 112 ? 109.29500 102.50200 142.83300 1.000 75.61311  ? 112 PRO B O    1 
ATOM   3306 C CB   . PRO B 1 112 ? 108.48900 101.67400 145.95000 1.000 78.27504  ? 112 PRO B CB   1 
ATOM   3307 C CG   . PRO B 1 112 ? 109.48500 101.54200 147.05700 1.000 77.08671  ? 112 PRO B CG   1 
ATOM   3308 C CD   . PRO B 1 112 ? 110.18600 100.24000 146.80800 1.000 77.66444  ? 112 PRO B CD   1 
ATOM   3309 N N    . ASP B 1 113 ? 111.03200 102.60300 144.26200 1.000 70.79707  ? 113 ASP B N    1 
ATOM   3310 C CA   . ASP B 1 113 ? 111.69700 103.68000 143.54200 1.000 71.98221  ? 113 ASP B CA   1 
ATOM   3311 C C    . ASP B 1 113 ? 112.50800 103.20200 142.34500 1.000 73.30965  ? 113 ASP B C    1 
ATOM   3312 O O    . ASP B 1 113 ? 112.96800 104.03900 141.56100 1.000 73.09295  ? 113 ASP B O    1 
ATOM   3313 C CB   . ASP B 1 113 ? 112.60800 104.45800 144.49500 1.000 72.19549  ? 113 ASP B CB   1 
ATOM   3314 C CG   . ASP B 1 113 ? 112.86000 105.88000 144.03100 1.000 74.43017  ? 113 ASP B CG   1 
ATOM   3315 O OD1  . ASP B 1 113 ? 111.87900 106.58400 143.71000 1.000 74.81901  ? 113 ASP B OD1  1 
ATOM   3316 O OD2  . ASP B 1 113 ? 114.03800 106.29300 143.98800 1.000 74.33304  ? 113 ASP B OD2  1 
ATOM   3317 N N    . LEU B 1 114 ? 112.70300 101.89400 142.18300 1.000 70.14279  ? 114 LEU B N    1 
ATOM   3318 C CA   . LEU B 1 114 ? 113.39600 101.38700 141.00400 1.000 68.76437  ? 114 LEU B CA   1 
ATOM   3319 C C    . LEU B 1 114 ? 112.45600 101.19800 139.82000 1.000 69.43252  ? 114 LEU B C    1 
ATOM   3320 O O    . LEU B 1 114 ? 112.83500 101.47700 138.67800 1.000 69.25322  ? 114 LEU B O    1 
ATOM   3321 C CB   . LEU B 1 114 ? 114.09600 100.06500 141.32900 1.000 68.53051  ? 114 LEU B CB   1 
ATOM   3322 C CG   . LEU B 1 114 ? 114.72500 99.33000  140.14300 1.000 69.56303  ? 114 LEU B CG   1 
ATOM   3323 C CD1  . LEU B 1 114 ? 115.72000 100.22700 139.42200 1.000 68.89128  ? 114 LEU B CD1  1 
ATOM   3324 C CD2  . LEU B 1 114 ? 115.39300 98.04200  140.59700 1.000 67.70258  ? 114 LEU B CD2  1 
ATOM   3325 N N    . SER B 1 115 ? 111.23400 100.72500 140.07300 1.000 63.61052  ? 115 SER B N    1 
ATOM   3326 C CA   . SER B 1 115 ? 110.29000 100.48400 138.98700 1.000 63.07486  ? 115 SER B CA   1 
ATOM   3327 C C    . SER B 1 115 ? 109.94400 101.76500 138.24100 1.000 65.06467  ? 115 SER B C    1 
ATOM   3328 O O    . SER B 1 115 ? 109.64200 101.72400 137.04300 1.000 66.47134  ? 115 SER B O    1 
ATOM   3329 C CB   . SER B 1 115 ? 109.02100 99.82900  139.53200 1.000 64.52134  ? 115 SER B CB   1 
ATOM   3330 O OG   . SER B 1 115 ? 109.31900 98.94800  140.60000 1.000 66.95559  ? 115 SER B OG   1 
ATOM   3331 N N    . ARG B 1 116 ? 109.97700 102.90900 138.92800 1.000 60.50397  ? 116 ARG B N    1 
ATOM   3332 C CA   . ARG B 1 116 ? 109.58600 104.16600 138.29800 1.000 58.08631  ? 116 ARG B CA   1 
ATOM   3333 C C    . ARG B 1 116 ? 110.57400 104.59100 137.21700 1.000 58.85231  ? 116 ARG B C    1 
ATOM   3334 O O    . ARG B 1 116 ? 110.17200 105.15900 136.19500 1.000 63.49747  ? 116 ARG B O    1 
ATOM   3335 C CB   . ARG B 1 116 ? 109.44500 105.25900 139.35600 1.000 59.35024  ? 116 ARG B CB   1 
ATOM   3336 C CG   . ARG B 1 116 ? 108.35900 106.27300 139.04600 1.000 59.84266  ? 116 ARG B CG   1 
ATOM   3337 C CD   . ARG B 1 116 ? 108.25800 107.33500 140.12500 1.000 58.77510  ? 116 ARG B CD   1 
ATOM   3338 N NE   . ARG B 1 116 ? 108.25300 108.67900 139.56200 1.000 59.80091  ? 116 ARG B NE   1 
ATOM   3339 C CZ   . ARG B 1 116 ? 108.12200 109.79000 140.27400 1.000 60.98703  ? 116 ARG B CZ   1 
ATOM   3340 N NH1  . ARG B 1 116 ? 107.98300 109.75600 141.58900 1.000 60.79573  ? 116 ARG B NH1  1 
ATOM   3341 N NH2  . ARG B 1 116 ? 108.13300 110.96400 139.65000 1.000 61.10129  ? 116 ARG B NH2  1 
ATOM   3342 N N    . TYR B 1 117 ? 111.86500 104.32700 137.41600 1.000 51.90491  ? 117 TYR B N    1 
ATOM   3343 C CA   . TYR B 1 117 ? 112.87000 104.67200 136.41700 1.000 52.90902  ? 117 TYR B CA   1 
ATOM   3344 C C    . TYR B 1 117 ? 112.93300 103.68900 135.25500 1.000 55.80849  ? 117 TYR B C    1 
ATOM   3345 O O    . TYR B 1 117 ? 113.52200 104.02100 134.22200 1.000 60.34383  ? 117 TYR B O    1 
ATOM   3346 C CB   . TYR B 1 117 ? 114.25900 104.74100 137.06000 1.000 53.55378  ? 117 TYR B CB   1 
ATOM   3347 C CG   . TYR B 1 117 ? 114.45100 105.84400 138.07500 1.000 55.90541  ? 117 TYR B CG   1 
ATOM   3348 C CD1  . TYR B 1 117 ? 113.78600 105.82000 139.29200 1.000 58.01331  ? 117 TYR B CD1  1 
ATOM   3349 C CD2  . TYR B 1 117 ? 115.31600 106.90000 137.82300 1.000 56.85726  ? 117 TYR B CD2  1 
ATOM   3350 C CE1  . TYR B 1 117 ? 113.96600 106.82400 140.22400 1.000 57.02470  ? 117 TYR B CE1  1 
ATOM   3351 C CE2  . TYR B 1 117 ? 115.50200 107.90700 138.74900 1.000 56.68321  ? 117 TYR B CE2  1 
ATOM   3352 C CZ   . TYR B 1 117 ? 114.82500 107.86400 139.94700 1.000 57.60098  ? 117 TYR B CZ   1 
ATOM   3353 O OH   . TYR B 1 117 ? 115.00800 108.86600 140.87100 1.000 57.20247  ? 117 TYR B OH   1 
ATOM   3354 N N    . SER B 1 118 ? 112.33100 102.50600 135.38600 1.000 45.98001  ? 118 SER B N    1 
ATOM   3355 C CA   . SER B 1 118 ? 112.50400 101.46300 134.38000 1.000 44.51342  ? 118 SER B CA   1 
ATOM   3356 C C    . SER B 1 118 ? 112.07800 101.90600 132.98300 1.000 43.47935  ? 118 SER B C    1 
ATOM   3357 O O    . SER B 1 118 ? 112.60700 101.39700 131.99000 1.000 46.51634  ? 118 SER B O    1 
ATOM   3358 C CB   . SER B 1 118 ? 111.72800 100.21200 134.79500 1.000 45.07261  ? 118 SER B CB   1 
ATOM   3359 O OG   . SER B 1 118 ? 110.47200 100.15000 134.14500 1.000 47.96190  ? 118 SER B OG   1 
ATOM   3360 N N    . VAL B 1 119 ? 111.13100 102.84300 132.87900 1.000 34.96905  ? 119 VAL B N    1 
ATOM   3361 C CA   . VAL B 1 119 ? 110.59400 103.22000 131.57300 1.000 35.04500  ? 119 VAL B CA   1 
ATOM   3362 C C    . VAL B 1 119 ? 111.65900 103.76300 130.62200 1.000 35.79376  ? 119 VAL B C    1 
ATOM   3363 O O    . VAL B 1 119 ? 111.50100 103.67100 129.39500 1.000 39.83318  ? 119 VAL B O    1 
ATOM   3364 C CB   . VAL B 1 119 ? 109.45100 104.24000 131.76000 1.000 35.86288  ? 119 VAL B CB   1 
ATOM   3365 C CG1  . VAL B 1 119 ? 110.00900 105.64200 131.93500 1.000 37.55201  ? 119 VAL B CG1  1 
ATOM   3366 C CG2  . VAL B 1 119 ? 108.49000 104.18600 130.58500 1.000 35.58358  ? 119 VAL B CG2  1 
ATOM   3367 N N    . TRP B 1 120 ? 112.76900 104.28200 131.15100 1.000 26.92991  ? 120 TRP B N    1 
ATOM   3368 C CA   . TRP B 1 120 ? 113.75600 104.91600 130.28500 1.000 29.97800  ? 120 TRP B CA   1 
ATOM   3369 C C    . TRP B 1 120 ? 114.57400 103.89600 129.50500 1.000 35.64252  ? 120 TRP B C    1 
ATOM   3370 O O    . TRP B 1 120 ? 114.94200 104.15300 128.35100 1.000 38.44397  ? 120 TRP B O    1 
ATOM   3371 C CB   . TRP B 1 120 ? 114.67500 105.81300 131.11500 1.000 31.00527  ? 120 TRP B CB   1 
ATOM   3372 C CG   . TRP B 1 120 ? 113.95100 106.95300 131.76800 1.000 33.57022  ? 120 TRP B CG   1 
ATOM   3373 C CD1  . TRP B 1 120 ? 113.42000 106.97400 133.02500 1.000 34.56439  ? 120 TRP B CD1  1 
ATOM   3374 C CD2  . TRP B 1 120 ? 113.66200 108.23100 131.19000 1.000 37.40291  ? 120 TRP B CD2  1 
ATOM   3375 N NE1  . TRP B 1 120 ? 112.82700 108.18700 133.26800 1.000 29.57103  ? 120 TRP B NE1  1 
ATOM   3376 C CE2  . TRP B 1 120 ? 112.96100 108.97700 132.15700 1.000 33.62484  ? 120 TRP B CE2  1 
ATOM   3377 C CE3  . TRP B 1 120 ? 113.93100 108.81800 129.95000 1.000 38.82937  ? 120 TRP B CE3  1 
ATOM   3378 C CZ2  . TRP B 1 120 ? 112.52800 110.27900 131.92300 1.000 31.47791  ? 120 TRP B CZ2  1 
ATOM   3379 C CZ3  . TRP B 1 120 ? 113.49900 110.11000 129.72100 1.000 37.39249  ? 120 TRP B CZ3  1 
ATOM   3380 C CH2  . TRP B 1 120 ? 112.80600 110.82600 130.70300 1.000 33.26838  ? 120 TRP B CH2  1 
ATOM   3381 N N    . ALA B 1 121 ? 114.80900 102.71700 130.08100 1.000 28.41791  ? 121 ALA B N    1 
ATOM   3382 C CA   . ALA B 1 121 ? 115.53300 101.68500 129.35100 1.000 24.22668  ? 121 ALA B CA   1 
ATOM   3383 C C    . ALA B 1 121 ? 114.67200 101.11400 128.23400 1.000 27.71706  ? 121 ALA B C    1 
ATOM   3384 O O    . ALA B 1 121 ? 115.16800 100.83900 127.13600 1.000 33.50016  ? 121 ALA B O    1 
ATOM   3385 C CB   . ALA B 1 121 ? 115.98600 100.58300 130.30700 1.000 25.94522  ? 121 ALA B CB   1 
ATOM   3386 N N    . ILE B 1 122 ? 113.37000 100.96400 128.48700 1.000 18.28674  ? 122 ILE B N    1 
ATOM   3387 C CA   . ILE B 1 122 ? 112.46100 100.50700 127.44400 1.000 21.88250  ? 122 ILE B CA   1 
ATOM   3388 C C    . ILE B 1 122 ? 112.40500 101.52500 126.31500 1.000 25.04382  ? 122 ILE B C    1 
ATOM   3389 O O    . ILE B 1 122 ? 112.42700 101.16700 125.12900 1.000 29.42510  ? 122 ILE B O    1 
ATOM   3390 C CB   . ILE B 1 122 ? 111.06400 100.24000 128.03500 1.000 24.19926  ? 122 ILE B CB   1 
ATOM   3391 C CG1  . ILE B 1 122 ? 111.10700 99.04600  128.99000 1.000 29.11594  ? 122 ILE B CG1  1 
ATOM   3392 C CG2  . ILE B 1 122 ? 110.04700 100.01300 126.92800 1.000 23.49440  ? 122 ILE B CG2  1 
ATOM   3393 C CD1  . ILE B 1 122 ? 112.10500 97.98000  128.59300 1.000 30.32626  ? 122 ILE B CD1  1 
ATOM   3394 N N    . LEU B 1 123 ? 112.36200 102.81500 126.66000 1.000 21.90951  ? 123 LEU B N    1 
ATOM   3395 C CA   . LEU B 1 123 ? 112.30600 103.83300 125.61700 1.000 17.76129  ? 123 LEU B CA   1 
ATOM   3396 C C    . LEU B 1 123 ? 113.58200 103.83900 124.78100 1.000 21.36381  ? 123 LEU B C    1 
ATOM   3397 O O    . LEU B 1 123 ? 113.52300 103.91900 123.54600 1.000 23.13855  ? 123 LEU B O    1 
ATOM   3398 C CB   . LEU B 1 123 ? 112.05900 105.20500 126.24100 1.000 19.92951  ? 123 LEU B CB   1 
ATOM   3399 C CG   . LEU B 1 123 ? 111.74500 106.35500 125.28300 1.000 29.62005  ? 123 LEU B CG   1 
ATOM   3400 C CD1  . LEU B 1 123 ? 110.26900 106.36300 124.91800 1.000 27.98313  ? 123 LEU B CD1  1 
ATOM   3401 C CD2  . LEU B 1 123 ? 112.15700 107.68300 125.89300 1.000 26.20740  ? 123 LEU B CD2  1 
ATOM   3402 N N    . THR B 1 124 ? 114.74400 103.73800 125.43000 1.000 23.98990  ? 124 THR B N    1 
ATOM   3403 C CA   . THR B 1 124 ? 115.99900 103.68500 124.68600 1.000 22.59738  ? 124 THR B CA   1 
ATOM   3404 C C    . THR B 1 124 ? 116.04900 102.46700 123.76800 1.000 24.65347  ? 124 THR B C    1 
ATOM   3405 O O    . THR B 1 124 ? 116.40800 102.57700 122.58800 1.000 22.71507  ? 124 THR B O    1 
ATOM   3406 C CB   . THR B 1 124 ? 117.18100 103.67400 125.65400 1.000 24.71634  ? 124 THR B CB   1 
ATOM   3407 O OG1  . THR B 1 124 ? 116.97400 104.66100 126.67100 1.000 34.27966  ? 124 THR B OG1  1 
ATOM   3408 C CG2  . THR B 1 124 ? 118.47300 103.98200 124.91600 1.000 21.98876  ? 124 THR B CG2  1 
ATOM   3409 N N    . VAL B 1 125 ? 115.69400 101.29100 124.29600 1.000 28.51201  ? 125 VAL B N    1 
ATOM   3410 C CA   . VAL B 1 125 ? 115.70900 100.07400 123.48800 1.000 23.69505  ? 125 VAL B CA   1 
ATOM   3411 C C    . VAL B 1 125 ? 114.76100 100.18100 122.30200 1.000 24.72347  ? 125 VAL B C    1 
ATOM   3412 O O    . VAL B 1 125 ? 115.03300 99.62500  121.23200 1.000 27.63900  ? 125 VAL B O    1 
ATOM   3413 C CB   . VAL B 1 125 ? 115.37500 98.84900  124.36000 1.000 20.83887  ? 125 VAL B CB   1 
ATOM   3414 C CG1  . VAL B 1 125 ? 115.45100 97.58000  123.53400 1.000 21.27539  ? 125 VAL B CG1  1 
ATOM   3415 C CG2  . VAL B 1 125 ? 116.32500 98.76700  125.53600 1.000 26.47158  ? 125 VAL B CG2  1 
ATOM   3416 N N    . VAL B 1 126 ? 113.64000 100.89100 122.46000 1.000 24.10303  ? 126 VAL B N    1 
ATOM   3417 C CA   . VAL B 1 126 ? 112.67600 100.99000 121.36600 1.000 21.97416  ? 126 VAL B CA   1 
ATOM   3418 C C    . VAL B 1 126 ? 112.98000 102.14000 120.41700 1.000 24.79497  ? 126 VAL B C    1 
ATOM   3419 O O    . VAL B 1 126 ? 112.37600 102.21500 119.33600 1.000 28.48642  ? 126 VAL B O    1 
ATOM   3420 C CB   . VAL B 1 126 ? 111.24500 101.12400 121.92900 1.000 25.42072  ? 126 VAL B CB   1 
ATOM   3421 C CG1  . VAL B 1 126 ? 110.25200 101.46200 120.83000 1.000 22.79121  ? 126 VAL B CG1  1 
ATOM   3422 C CG2  . VAL B 1 126 ? 110.83500 99.84500  122.63600 1.000 22.26269  ? 126 VAL B CG2  1 
ATOM   3423 N N    . VAL B 1 127 ? 113.92200 103.01800 120.76000 1.000 31.06257  ? 127 VAL B N    1 
ATOM   3424 C CA   . VAL B 1 127 ? 114.24300 104.14700 119.90400 1.000 25.45660  ? 127 VAL B CA   1 
ATOM   3425 C C    . VAL B 1 127 ? 115.56500 103.97900 119.15500 1.000 27.08884  ? 127 VAL B C    1 
ATOM   3426 O O    . VAL B 1 127 ? 115.68700 104.47900 118.03100 1.000 26.52146  ? 127 VAL B O    1 
ATOM   3427 C CB   . VAL B 1 127 ? 114.24500 105.45900 120.71600 1.000 27.38856  ? 127 VAL B CB   1 
ATOM   3428 C CG1  . VAL B 1 127 ? 114.99500 106.54800 119.97100 1.000 20.65961  ? 127 VAL B CG1  1 
ATOM   3429 C CG2  . VAL B 1 127 ? 112.82200 105.90000 121.01200 1.000 27.25759  ? 127 VAL B CG2  1 
ATOM   3430 N N    . VAL B 1 128 ? 116.55900 103.29100 119.72900 1.000 22.95713  ? 128 VAL B N    1 
ATOM   3431 C CA   . VAL B 1 128 ? 117.88100 103.23200 119.10300 1.000 19.50750  ? 128 VAL B CA   1 
ATOM   3432 C C    . VAL B 1 128 ? 118.06900 102.03800 118.17100 1.000 23.44530  ? 128 VAL B C    1 
ATOM   3433 O O    . VAL B 1 128 ? 119.14200 101.90500 117.56800 1.000 24.24187  ? 128 VAL B O    1 
ATOM   3434 C CB   . VAL B 1 128 ? 119.00100 103.22200 120.16400 1.000 26.04691  ? 128 VAL B CB   1 
ATOM   3435 C CG1  . VAL B 1 128 ? 118.89100 104.44100 121.06100 1.000 22.20957  ? 128 VAL B CG1  1 
ATOM   3436 C CG2  . VAL B 1 128 ? 118.95400 101.94100 120.97900 1.000 22.30781  ? 128 VAL B CG2  1 
ATOM   3437 N N    . PHE B 1 129 ? 117.06900 101.17200 118.02200 1.000 24.42050  ? 129 PHE B N    1 
ATOM   3438 C CA   . PHE B 1 129 ? 117.20900 99.94600  117.23700 1.000 25.58193  ? 129 PHE B CA   1 
ATOM   3439 C C    . PHE B 1 129 ? 116.84400 100.22700 115.78100 1.000 24.55871  ? 129 PHE B C    1 
ATOM   3440 O O    . PHE B 1 129 ? 115.68100 100.50200 115.46800 1.000 23.67102  ? 129 PHE B O    1 
ATOM   3441 C CB   . PHE B 1 129 ? 116.32600 98.84600  117.82100 1.000 22.18575  ? 129 PHE B CB   1 
ATOM   3442 C CG   . PHE B 1 129 ? 116.97500 97.49000  117.85400 1.000 25.78048  ? 129 PHE B CG   1 
ATOM   3443 C CD1  . PHE B 1 129 ? 117.21200 96.78900  116.68500 1.000 23.74385  ? 129 PHE B CD1  1 
ATOM   3444 C CD2  . PHE B 1 129 ? 117.33400 96.91100  119.05900 1.000 17.10618  ? 129 PHE B CD2  1 
ATOM   3445 C CE1  . PHE B 1 129 ? 117.80100 95.53900  116.71800 1.000 18.90166  ? 129 PHE B CE1  1 
ATOM   3446 C CE2  . PHE B 1 129 ? 117.92300 95.66300  119.09700 1.000 17.94902  ? 129 PHE B CE2  1 
ATOM   3447 C CZ   . PHE B 1 129 ? 118.15600 94.97700  117.92600 1.000 16.06124  ? 129 PHE B CZ   1 
ATOM   3448 N N    . GLU B 1 130 ? 117.83100 100.15100 114.88900 1.000 17.63963  ? 130 GLU B N    1 
ATOM   3449 C CA   . GLU B 1 130 ? 117.62600 100.36200 113.46100 1.000 21.17506  ? 130 GLU B CA   1 
ATOM   3450 C C    . GLU B 1 130 ? 117.82700 99.06600  112.67900 1.000 23.10827  ? 130 GLU B C    1 
ATOM   3451 O O    . GLU B 1 130 ? 118.24900 98.03900  113.21600 1.000 24.36187  ? 130 GLU B O    1 
ATOM   3452 C CB   . GLU B 1 130 ? 118.56300 101.45300 112.93100 1.000 17.43990  ? 130 GLU B CB   1 
ATOM   3453 C CG   . GLU B 1 130 ? 118.60400 102.70300 113.79000 1.000 23.58703  ? 130 GLU B CG   1 
ATOM   3454 C CD   . GLU B 1 130 ? 117.52100 103.69500 113.42600 1.000 24.93615  ? 130 GLU B CD   1 
ATOM   3455 O OE1  . GLU B 1 130 ? 116.95100 103.58000 112.32100 1.000 24.29791  ? 130 GLU B OE1  1 
ATOM   3456 O OE2  . GLU B 1 130 ? 117.23600 104.59100 114.24700 1.000 30.86489  ? 130 GLU B OE2  1 
ATOM   3457 N N    . PHE B 1 131 ? 117.51700 99.13800  111.38100 1.000 19.23283  ? 131 PHE B N    1 
ATOM   3458 C CA   . PHE B 1 131 ? 117.58200 97.97100  110.50500 1.000 15.48971  ? 131 PHE B CA   1 
ATOM   3459 C C    . PHE B 1 131 ? 119.00900 97.59300  110.11900 1.000 9.62739   ? 131 PHE B C    1 
ATOM   3460 O O    . PHE B 1 131 ? 119.29300 96.40700  109.92000 1.000 9.52178   ? 131 PHE B O    1 
ATOM   3461 C CB   . PHE B 1 131 ? 116.75100 98.22500  109.24500 1.000 14.99009  ? 131 PHE B CB   1 
ATOM   3462 C CG   . PHE B 1 131 ? 116.42500 96.98100  108.47000 1.000 17.15455  ? 131 PHE B CG   1 
ATOM   3463 C CD1  . PHE B 1 131 ? 115.66200 95.97500  109.03500 1.000 18.16587  ? 131 PHE B CD1  1 
ATOM   3464 C CD2  . PHE B 1 131 ? 116.87400 96.82300  107.17100 1.000 19.89482  ? 131 PHE B CD2  1 
ATOM   3465 C CE1  . PHE B 1 131 ? 115.36100 94.83200  108.32300 1.000 21.13621  ? 131 PHE B CE1  1 
ATOM   3466 C CE2  . PHE B 1 131 ? 116.57700 95.68200  106.45400 1.000 20.45128  ? 131 PHE B CE2  1 
ATOM   3467 C CZ   . PHE B 1 131 ? 115.81900 94.68600  107.03100 1.000 22.41020  ? 131 PHE B CZ   1 
ATOM   3468 N N    . THR B 1 132 ? 119.90700 98.56600  109.99900 1.000 15.51067  ? 132 THR B N    1 
ATOM   3469 C CA   . THR B 1 132 ? 121.28500 98.32500  109.59500 1.000 6.01388   ? 132 THR B CA   1 
ATOM   3470 C C    . THR B 1 132 ? 122.23600 98.81200  110.68200 1.000 10.76729  ? 132 THR B C    1 
ATOM   3471 O O    . THR B 1 132 ? 121.86100 99.59300  111.56000 1.000 17.76849  ? 132 THR B O    1 
ATOM   3472 C CB   . THR B 1 132 ? 121.60800 99.01000  108.25700 1.000 10.98617  ? 132 THR B CB   1 
ATOM   3473 O OG1  . THR B 1 132 ? 121.07600 100.34000 108.25200 1.000 23.21171  ? 132 THR B OG1  1 
ATOM   3474 C CG2  . THR B 1 132 ? 121.00400 98.23100  107.10300 1.000 7.32576   ? 132 THR B CG2  1 
ATOM   3475 N N    . ILE B 1 133 ? 123.47800 98.32700  110.62300 1.000 11.02719  ? 133 ILE B N    1 
ATOM   3476 C CA   . ILE B 1 133 ? 124.47900 98.71500  111.61400 1.000 13.46769  ? 133 ILE B CA   1 
ATOM   3477 C C    . ILE B 1 133 ? 124.98600 100.13400 111.36900 1.000 18.28545  ? 133 ILE B C    1 
ATOM   3478 O O    . ILE B 1 133 ? 125.21300 100.89900 112.31800 1.000 23.08732  ? 133 ILE B O    1 
ATOM   3479 C CB   . ILE B 1 133 ? 125.63500 97.69800  111.61600 1.000 16.78298  ? 133 ILE B CB   1 
ATOM   3480 C CG1  . ILE B 1 133 ? 125.14900 96.33900  112.11700 1.000 15.26510  ? 133 ILE B CG1  1 
ATOM   3481 C CG2  . ILE B 1 133 ? 126.79300 98.20200  112.45900 1.000 18.06810  ? 133 ILE B CG2  1 
ATOM   3482 C CD1  . ILE B 1 133 ? 125.71600 95.17700  111.34800 1.000 14.99937  ? 133 ILE B CD1  1 
ATOM   3483 N N    . GLY B 1 134 ? 125.14000 100.52400 110.10200 1.000 7.09188   ? 134 GLY B N    1 
ATOM   3484 C CA   . GLY B 1 134 ? 125.59600 101.87400 109.81500 1.000 6.56553   ? 134 GLY B CA   1 
ATOM   3485 C C    . GLY B 1 134 ? 124.57400 102.93000 110.18000 1.000 16.71076  ? 134 GLY B C    1 
ATOM   3486 O O    . GLY B 1 134 ? 124.92800 104.00500 110.67600 1.000 25.60870  ? 134 GLY B O    1 
ATOM   3487 N N    . ALA B 1 135 ? 123.30200 102.60300 109.99500 1.000 5.81132   ? 135 ALA B N    1 
ATOM   3488 C CA   . ALA B 1 135 ? 122.24300 103.51600 110.38300 1.000 1.22704   ? 135 ALA B CA   1 
ATOM   3489 C C    . ALA B 1 135 ? 122.24900 103.69700 111.88300 1.000 13.55340  ? 135 ALA B C    1 
ATOM   3490 O O    . ALA B 1 135 ? 122.20000 104.81600 112.36900 1.000 24.33825  ? 135 ALA B O    1 
ATOM   3491 C CB   . ALA B 1 135 ? 120.90800 102.99000 109.92200 1.000 1.03211   ? 135 ALA B CB   1 
ATOM   3492 N N    . THR B 1 136 ? 122.33700 102.60300 112.62500 1.000 8.24897   ? 136 THR B N    1 
ATOM   3493 C CA   . THR B 1 136 ? 122.35200 102.66500 114.08000 1.000 7.17887   ? 136 THR B CA   1 
ATOM   3494 C C    . THR B 1 136 ? 123.52600 103.49500 114.58200 1.000 16.94125  ? 136 THR B C    1 
ATOM   3495 O O    . THR B 1 136 ? 123.35600 104.36000 115.44900 1.000 18.03899  ? 136 THR B O    1 
ATOM   3496 C CB   . THR B 1 136 ? 122.41200 101.25100 114.66100 1.000 12.52396  ? 136 THR B CB   1 
ATOM   3497 O OG1  . THR B 1 136 ? 121.28100 100.49700 114.21000 1.000 17.51878  ? 136 THR B OG1  1 
ATOM   3498 C CG2  . THR B 1 136 ? 122.41200 101.28900 116.17900 1.000 16.31616  ? 136 THR B CG2  1 
ATOM   3499 N N    . LEU B 1 137 ? 124.71500 103.29200 114.00500 1.000 8.30808   ? 137 LEU B N    1 
ATOM   3500 C CA   . LEU B 1 137 ? 125.88200 104.03000 114.47900 1.000 3.50289   ? 137 LEU B CA   1 
ATOM   3501 C C    . LEU B 1 137 ? 125.78100 105.51700 114.15300 1.000 13.12472  ? 137 LEU B C    1 
ATOM   3502 O O    . LEU B 1 137 ? 126.06600 106.36800 115.01000 1.000 21.30809  ? 137 LEU B O    1 
ATOM   3503 C CB   . LEU B 1 137 ? 127.15300 103.43800 113.87000 1.000 8.09824   ? 137 LEU B CB   1 
ATOM   3504 C CG   . LEU B 1 137 ? 127.60100 102.05900 114.35800 1.000 13.22288  ? 137 LEU B CG   1 
ATOM   3505 C CD1  . LEU B 1 137 ? 128.76200 101.55100 113.52200 1.000 7.41733   ? 137 LEU B CD1  1 
ATOM   3506 C CD2  . LEU B 1 137 ? 127.97500 102.09500 115.82900 1.000 11.63632  ? 137 LEU B CD2  1 
ATOM   3507 N N    . SER B 1 138 ? 125.32000 105.85500 112.94600 1.000 13.92073  ? 138 SER B N    1 
ATOM   3508 C CA   . SER B 1 138 ? 125.22400 107.26300 112.57300 1.000 10.44828  ? 138 SER B CA   1 
ATOM   3509 C C    . SER B 1 138 ? 124.16500 107.98900 113.39500 1.000 17.26030  ? 138 SER B C    1 
ATOM   3510 O O    . SER B 1 138 ? 124.39900 109.10700 113.88100 1.000 23.78775  ? 138 SER B O    1 
ATOM   3511 C CB   . SER B 1 138 ? 124.93300 107.38300 111.07800 1.000 12.00804  ? 138 SER B CB   1 
ATOM   3512 O OG   . SER B 1 138 ? 123.55000 107.56500 110.83900 1.000 25.50773  ? 138 SER B OG   1 
ATOM   3513 N N    . LYS B 1 139 ? 123.00400 107.36000 113.59700 1.000 5.34789   ? 139 LYS B N    1 
ATOM   3514 C CA   . LYS B 1 139 ? 121.95900 108.01800 114.36700 1.000 2.11287   ? 139 LYS B CA   1 
ATOM   3515 C C    . LYS B 1 139 ? 122.32000 108.10900 115.84300 1.000 13.72239  ? 139 LYS B C    1 
ATOM   3516 O O    . LYS B 1 139 ? 121.96300 109.09400 116.50000 1.000 29.86357  ? 139 LYS B O    1 
ATOM   3517 C CB   . LYS B 1 139 ? 120.63400 107.28800 114.16500 1.000 15.63681  ? 139 LYS B CB   1 
ATOM   3518 C CG   . LYS B 1 139 ? 120.31600 107.05100 112.69700 1.000 13.78559  ? 139 LYS B CG   1 
ATOM   3519 C CD   . LYS B 1 139 ? 118.85200 107.27300 112.38500 1.000 14.05693  ? 139 LYS B CD   1 
ATOM   3520 C CE   . LYS B 1 139 ? 118.56600 106.99600 110.92000 1.000 15.93621  ? 139 LYS B CE   1 
ATOM   3521 N NZ   . LYS B 1 139 ? 117.30300 106.23500 110.72700 1.000 19.06567  ? 139 LYS B NZ   1 
ATOM   3522 N N    . GLY B 1 140 ? 123.05000 107.12900 116.38100 1.000 14.54383  ? 140 GLY B N    1 
ATOM   3523 C CA   . GLY B 1 140 ? 123.49700 107.24900 117.75700 1.000 10.30724  ? 140 GLY B CA   1 
ATOM   3524 C C    . GLY B 1 140 ? 124.50000 108.37100 117.93200 1.000 13.05526  ? 140 GLY B C    1 
ATOM   3525 O O    . GLY B 1 140 ? 124.44400 109.12300 118.91100 1.000 28.60532  ? 140 GLY B O    1 
ATOM   3526 N N    . PHE B 1 141 ? 125.40300 108.53300 116.96100 1.000 8.31144   ? 141 PHE B N    1 
ATOM   3527 C CA   . PHE B 1 141 ? 126.34000 109.65100 117.00900 1.000 15.33720  ? 141 PHE B CA   1 
ATOM   3528 C C    . PHE B 1 141 ? 125.60000 110.98500 116.99700 1.000 14.24732  ? 141 PHE B C    1 
ATOM   3529 O O    . PHE B 1 141 ? 125.90000 111.89000 117.79200 1.000 26.46879  ? 141 PHE B O    1 
ATOM   3530 C CB   . PHE B 1 141 ? 127.31000 109.55600 115.83100 1.000 18.16339  ? 141 PHE B CB   1 
ATOM   3531 C CG   . PHE B 1 141 ? 128.44900 110.53000 115.89700 1.000 15.87964  ? 141 PHE B CG   1 
ATOM   3532 C CD1  . PHE B 1 141 ? 129.53300 110.29200 116.72300 1.000 20.45720  ? 141 PHE B CD1  1 
ATOM   3533 C CD2  . PHE B 1 141 ? 128.44200 111.67600 115.12500 1.000 15.19106  ? 141 PHE B CD2  1 
ATOM   3534 C CE1  . PHE B 1 141 ? 130.58300 111.18300 116.78200 1.000 22.54797  ? 141 PHE B CE1  1 
ATOM   3535 C CE2  . PHE B 1 141 ? 129.48800 112.57000 115.18000 1.000 17.02190  ? 141 PHE B CE2  1 
ATOM   3536 C CZ   . PHE B 1 141 ? 130.56100 112.32300 116.01000 1.000 24.90887  ? 141 PHE B CZ   1 
ATOM   3537 N N    . ASN B 1 142 ? 124.61500 111.12200 116.10500 1.000 13.94820  ? 142 ASN B N    1 
ATOM   3538 C CA   . ASN B 1 142 ? 123.88100 112.38100 116.02600 1.000 19.12161  ? 142 ASN B CA   1 
ATOM   3539 C C    . ASN B 1 142 ? 123.09700 112.66200 117.30600 1.000 24.65779  ? 142 ASN B C    1 
ATOM   3540 O O    . ASN B 1 142 ? 123.09800 113.79600 117.80600 1.000 21.54407  ? 142 ASN B O    1 
ATOM   3541 C CB   . ASN B 1 142 ? 122.94100 112.36900 114.82100 1.000 21.73258  ? 142 ASN B CB   1 
ATOM   3542 C CG   . ASN B 1 142 ? 123.68200 112.37700 113.50100 1.000 28.98330  ? 142 ASN B CG   1 
ATOM   3543 O OD1  . ASN B 1 142 ? 124.90400 112.51700 113.46200 1.000 29.30585  ? 142 ASN B OD1  1 
ATOM   3544 N ND2  . ASN B 1 142 ? 122.94300 112.22700 112.40800 1.000 23.48520  ? 142 ASN B ND2  1 
ATOM   3545 N N    . ARG B 1 143 ? 122.42000 111.64700 117.85000 1.000 26.57165  ? 143 ARG B N    1 
ATOM   3546 C CA   . ARG B 1 143 ? 121.66900 111.84900 119.08500 1.000 18.85329  ? 143 ARG B CA   1 
ATOM   3547 C C    . ARG B 1 143 ? 122.57500 112.17500 120.26600 1.000 22.33890  ? 143 ARG B C    1 
ATOM   3548 O O    . ARG B 1 143 ? 122.18800 112.95700 121.14700 1.000 34.20210  ? 143 ARG B O    1 
ATOM   3549 C CB   . ARG B 1 143 ? 120.83300 110.60700 119.38600 1.000 17.40718  ? 143 ARG B CB   1 
ATOM   3550 C CG   . ARG B 1 143 ? 119.62800 110.44600 118.47800 1.000 19.28973  ? 143 ARG B CG   1 
ATOM   3551 C CD   . ARG B 1 143 ? 118.78300 109.25600 118.88800 1.000 19.16813  ? 143 ARG B CD   1 
ATOM   3552 N NE   . ARG B 1 143 ? 118.58900 108.32400 117.78500 1.000 25.05117  ? 143 ARG B NE   1 
ATOM   3553 C CZ   . ARG B 1 143 ? 117.45500 108.18200 117.11400 1.000 28.42844  ? 143 ARG B CZ   1 
ATOM   3554 N NH1  . ARG B 1 143 ? 116.38200 108.89500 117.41200 1.000 23.92482  ? 143 ARG B NH1  1 
ATOM   3555 N NH2  . ARG B 1 143 ? 117.39500 107.30200 116.11800 1.000 24.23690  ? 143 ARG B NH2  1 
ATOM   3556 N N    . ALA B 1 144 ? 123.81600 111.67800 120.25900 1.000 21.34729  ? 144 ALA B N    1 
ATOM   3557 C CA   . ALA B 1 144 ? 124.70600 112.01700 121.36200 1.000 19.60034  ? 144 ALA B CA   1 
ATOM   3558 C C    . ALA B 1 144 ? 125.25400 113.42900 121.22800 1.000 23.59841  ? 144 ALA B C    1 
ATOM   3559 O O    . ALA B 1 144 ? 125.36400 114.14400 122.23500 1.000 27.08538  ? 144 ALA B O    1 
ATOM   3560 C CB   . ALA B 1 144 ? 125.85400 111.01100 121.44400 1.000 17.87659  ? 144 ALA B CB   1 
ATOM   3561 N N    . LEU B 1 145 ? 125.49600 113.88800 119.99800 1.000 25.24625  ? 145 LEU B N    1 
ATOM   3562 C CA   . LEU B 1 145 ? 125.92500 115.27400 119.84500 1.000 25.21974  ? 145 LEU B CA   1 
ATOM   3563 C C    . LEU B 1 145 ? 124.79800 116.22500 120.21900 1.000 27.21629  ? 145 LEU B C    1 
ATOM   3564 O O    . LEU B 1 145 ? 125.03200 117.25300 120.86700 1.000 31.68820  ? 145 LEU B O    1 
ATOM   3565 C CB   . LEU B 1 145 ? 126.39600 115.54700 118.41800 1.000 23.47539  ? 145 LEU B CB   1 
ATOM   3566 C CG   . LEU B 1 145 ? 127.39100 114.58300 117.78100 1.000 32.01941  ? 145 LEU B CG   1 
ATOM   3567 C CD1  . LEU B 1 145 ? 127.75800 115.07000 116.38900 1.000 28.55487  ? 145 LEU B CD1  1 
ATOM   3568 C CD2  . LEU B 1 145 ? 128.62900 114.45000 118.65100 1.000 25.42217  ? 145 LEU B CD2  1 
ATOM   3569 N N    . GLY B 1 146 ? 123.56700 115.88300 119.84800 1.000 27.48150  ? 146 GLY B N    1 
ATOM   3570 C CA   . GLY B 1 146 ? 122.43000 116.68400 120.24700 1.000 23.71075  ? 146 GLY B CA   1 
ATOM   3571 C C    . GLY B 1 146 ? 122.30400 116.80200 121.75300 1.000 30.41651  ? 146 GLY B C    1 
ATOM   3572 O O    . GLY B 1 146 ? 122.26400 117.91400 122.29500 1.000 28.50344  ? 146 GLY B O    1 
ATOM   3573 N N    . THR B 1 147 ? 122.20600 115.65500 122.43600 1.000 32.12663  ? 147 THR B N    1 
ATOM   3574 C CA   . THR B 1 147 ? 122.04200 115.67100 123.88800 1.000 26.43048  ? 147 THR B CA   1 
ATOM   3575 C C    . THR B 1 147 ? 123.18100 116.39500 124.59800 1.000 28.50449  ? 147 THR B C    1 
ATOM   3576 O O    . THR B 1 147 ? 122.94000 117.11700 125.58000 1.000 37.11695  ? 147 THR B O    1 
ATOM   3577 C CB   . THR B 1 147 ? 121.92600 114.24200 124.41800 1.000 26.77207  ? 147 THR B CB   1 
ATOM   3578 O OG1  . THR B 1 147 ? 120.63700 113.70900 124.09400 1.000 33.17536  ? 147 THR B OG1  1 
ATOM   3579 C CG2  . THR B 1 147 ? 122.11400 114.21700 125.92400 1.000 26.92511  ? 147 THR B CG2  1 
ATOM   3580 N N    . LEU B 1 148 ? 124.41000 116.30800 124.07600 1.000 28.66752  ? 148 LEU B N    1 
ATOM   3581 C CA   . LEU B 1 148 ? 125.49300 116.98700 124.77800 1.000 31.04851  ? 148 LEU B CA   1 
ATOM   3582 C C    . LEU B 1 148 ? 125.52900 118.48200 124.49600 1.000 31.62860  ? 148 LEU B C    1 
ATOM   3583 O O    . LEU B 1 148 ? 125.79700 119.26600 125.41600 1.000 35.91421  ? 148 LEU B O    1 
ATOM   3584 C CB   . LEU B 1 148 ? 126.83400 116.34900 124.41300 1.000 37.37205  ? 148 LEU B CB   1 
ATOM   3585 C CG   . LEU B 1 148 ? 127.41700 115.40000 125.46300 1.000 36.69135  ? 148 LEU B CG   1 
ATOM   3586 C CD1  . LEU B 1 148 ? 126.43200 114.29100 125.79300 1.000 33.46476  ? 148 LEU B CD1  1 
ATOM   3587 C CD2  . LEU B 1 148 ? 128.73100 114.80900 124.98600 1.000 34.18501  ? 148 LEU B CD2  1 
ATOM   3588 N N    . SER B 1 149 ? 125.18000 118.91700 123.28400 1.000 30.80859  ? 149 SER B N    1 
ATOM   3589 C CA   . SER B 1 149 ? 125.12800 120.35500 123.05200 1.000 30.71820  ? 149 SER B CA   1 
ATOM   3590 C C    . SER B 1 149 ? 123.96800 120.98000 123.81000 1.000 34.93259  ? 149 SER B C    1 
ATOM   3591 O O    . SER B 1 149 ? 124.06200 122.13200 124.25900 1.000 35.48941  ? 149 SER B O    1 
ATOM   3592 C CB   . SER B 1 149 ? 125.01500 120.65100 121.55800 1.000 31.31237  ? 149 SER B CB   1 
ATOM   3593 O OG   . SER B 1 149 ? 126.17800 120.23200 120.86800 1.000 36.82035  ? 149 SER B OG   1 
ATOM   3594 N N    . ALA B 1 150 ? 122.89700 120.21300 124.02800 1.000 36.78591  ? 150 ALA B N    1 
ATOM   3595 C CA   . ALA B 1 150 ? 121.77700 120.73500 124.80000 1.000 30.19205  ? 150 ALA B CA   1 
ATOM   3596 C C    . ALA B 1 150 ? 122.16100 120.89200 126.26400 1.000 32.58649  ? 150 ALA B C    1 
ATOM   3597 O O    . ALA B 1 150 ? 121.97000 121.96500 126.85200 1.000 34.01414  ? 150 ALA B O    1 
ATOM   3598 C CB   . ALA B 1 150 ? 120.56200 119.82100 124.65100 1.000 29.98808  ? 150 ALA B CB   1 
ATOM   3599 N N    . GLY B 1 151 ? 122.69200 119.82900 126.87900 1.000 37.07882  ? 151 GLY B N    1 
ATOM   3600 C CA   . GLY B 1 151 ? 123.12300 119.96300 128.26100 1.000 33.39808  ? 151 GLY B CA   1 
ATOM   3601 C C    . GLY B 1 151 ? 124.20800 121.00300 128.45400 1.000 33.07094  ? 151 GLY B C    1 
ATOM   3602 O O    . GLY B 1 151 ? 124.25400 121.66100 129.50600 1.000 34.73050  ? 151 GLY B O    1 
ATOM   3603 N N    . GLY B 1 152 ? 124.97900 121.28300 127.40600 1.000 41.81661  ? 152 GLY B N    1 
ATOM   3604 C CA   . GLY B 1 152 ? 126.01600 122.28700 127.48900 1.000 42.71720  ? 152 GLY B CA   1 
ATOM   3605 C C    . GLY B 1 152 ? 125.46400 123.69200 127.46100 1.000 44.97532  ? 152 GLY B C    1 
ATOM   3606 O O    . GLY B 1 152 ? 125.83000 124.50900 128.30800 1.000 44.99841  ? 152 GLY B O    1 
ATOM   3607 N N    . LEU B 1 153 ? 124.59100 124.00100 126.50000 1.000 47.59039  ? 153 LEU B N    1 
ATOM   3608 C CA   . LEU B 1 153 ? 123.96100 125.31700 126.51000 1.000 42.39765  ? 153 LEU B CA   1 
ATOM   3609 C C    . LEU B 1 153 ? 123.15800 125.53100 127.79100 1.000 44.11825  ? 153 LEU B C    1 
ATOM   3610 O O    . LEU B 1 153 ? 123.14900 126.63400 128.35500 1.000 43.15860  ? 153 LEU B O    1 
ATOM   3611 C CB   . LEU B 1 153 ? 123.07200 125.48600 125.27800 1.000 43.87876  ? 153 LEU B CB   1 
ATOM   3612 C CG   . LEU B 1 153 ? 122.80700 126.92500 124.83600 1.000 46.06032  ? 153 LEU B CG   1 
ATOM   3613 C CD1  . LEU B 1 153 ? 124.11300 127.64500 124.54000 1.000 45.23407  ? 153 LEU B CD1  1 
ATOM   3614 C CD2  . LEU B 1 153 ? 121.89300 126.94900 123.62300 1.000 46.90673  ? 153 LEU B CD2  1 
ATOM   3615 N N    . ALA B 1 154 ? 122.49000 124.48400 128.28000 1.000 48.89643  ? 154 ALA B N    1 
ATOM   3616 C CA   . ALA B 1 154 ? 121.70900 124.62800 129.50400 1.000 44.87549  ? 154 ALA B CA   1 
ATOM   3617 C C    . ALA B 1 154 ? 122.59900 125.01000 130.68100 1.000 47.97965  ? 154 ALA B C    1 
ATOM   3618 O O    . ALA B 1 154 ? 122.27800 125.93400 131.44500 1.000 49.41975  ? 154 ALA B O    1 
ATOM   3619 C CB   . ALA B 1 154 ? 120.94900 123.33500 129.79500 1.000 46.23076  ? 154 ALA B CB   1 
ATOM   3620 N N    . LEU B 1 155 ? 123.71300 124.29000 130.86500 1.000 59.42912  ? 155 LEU B N    1 
ATOM   3621 C CA   . LEU B 1 155 ? 124.61400 124.64500 131.95400 1.000 56.35587  ? 155 LEU B CA   1 
ATOM   3622 C C    . LEU B 1 155 ? 125.32400 125.97200 131.71100 1.000 54.42057  ? 155 LEU B C    1 
ATOM   3623 O O    . LEU B 1 155 ? 125.73600 126.62300 132.67600 1.000 53.71265  ? 155 LEU B O    1 
ATOM   3624 C CB   . LEU B 1 155 ? 125.64200 123.53400 132.17400 1.000 56.11322  ? 155 LEU B CB   1 
ATOM   3625 C CG   . LEU B 1 155 ? 125.25400 122.47700 133.21000 1.000 55.85454  ? 155 LEU B CG   1 
ATOM   3626 C CD1  . LEU B 1 155 ? 126.49100 121.82200 133.80200 1.000 55.19300  ? 155 LEU B CD1  1 
ATOM   3627 C CD2  . LEU B 1 155 ? 124.38900 123.08700 134.30200 1.000 54.88927  ? 155 LEU B CD2  1 
ATOM   3628 N N    . GLY B 1 156 ? 125.46800 126.39100 130.45500 1.000 65.55156  ? 156 GLY B N    1 
ATOM   3629 C CA   . GLY B 1 156 ? 126.07300 127.66600 130.14200 1.000 65.68397  ? 156 GLY B CA   1 
ATOM   3630 C C    . GLY B 1 156 ? 125.11100 128.82500 130.12600 1.000 66.59149  ? 156 GLY B C    1 
ATOM   3631 O O    . GLY B 1 156 ? 125.49900 129.95200 129.80200 1.000 63.89833  ? 156 GLY B O    1 
ATOM   3632 N N    . MET B 1 157 ? 123.85600 128.57300 130.47000 1.000 74.45593  ? 157 MET B N    1 
ATOM   3633 C CA   . MET B 1 157 ? 122.83200 129.61000 130.51900 1.000 72.72650  ? 157 MET B CA   1 
ATOM   3634 C C    . MET B 1 157 ? 122.21400 129.76200 131.89800 1.000 71.60082  ? 157 MET B C    1 
ATOM   3635 O O    . MET B 1 157 ? 121.89700 130.88700 132.30700 1.000 69.74827  ? 157 MET B O    1 
ATOM   3636 C CB   . MET B 1 157 ? 121.72700 129.31800 129.49200 1.000 71.49347  ? 157 MET B CB   1 
ATOM   3637 C CG   . MET B 1 157 ? 120.71200 130.43900 129.33900 1.000 70.37590  ? 157 MET B CG   1 
ATOM   3638 S SD   . MET B 1 157 ? 121.08100 131.54100 127.96000 1.000 76.24509  ? 157 MET B SD   1 
ATOM   3639 C CE   . MET B 1 157 ? 121.75500 130.38600 126.77000 1.000 72.84196  ? 157 MET B CE   1 
ATOM   3640 N N    . ALA B 1 158 ? 122.01800 128.66500 132.63300 1.000 79.17689  ? 158 ALA B N    1 
ATOM   3641 C CA   . ALA B 1 158 ? 121.45500 128.81100 133.97300 1.000 77.72899  ? 158 ALA B CA   1 
ATOM   3642 C C    . ALA B 1 158 ? 122.35900 129.66100 134.86000 1.000 80.10546  ? 158 ALA B C    1 
ATOM   3643 O O    . ALA B 1 158 ? 121.87500 130.33800 135.78100 1.000 79.56447  ? 158 ALA B O    1 
ATOM   3644 C CB   . ALA B 1 158 ? 121.22300 127.43800 134.60300 1.000 76.40765  ? 158 ALA B CB   1 
ATOM   3645 N N    . GLU B 1 159 ? 123.66500 129.67900 134.57400 1.000 89.53419  ? 159 GLU B N    1 
ATOM   3646 C CA   . GLU B 1 159 ? 124.56800 130.53300 135.33700 1.000 86.97171  ? 159 GLU B CA   1 
ATOM   3647 C C    . GLU B 1 159 ? 124.26500 132.00100 135.07600 1.000 87.38254  ? 159 GLU B C    1 
ATOM   3648 O O    . GLU B 1 159 ? 124.16500 132.79800 136.01600 1.000 88.39404  ? 159 GLU B O    1 
ATOM   3649 C CB   . GLU B 1 159 ? 126.02100 130.20900 134.99000 1.000 87.95258  ? 159 GLU B CB   1 
ATOM   3650 C CG   . GLU B 1 159 ? 126.98000 130.32000 136.16600 1.000 88.14263  ? 159 GLU B CG   1 
ATOM   3651 C CD   . GLU B 1 159 ? 126.84800 129.16600 137.14000 1.000 88.83023  ? 159 GLU B CD   1 
ATOM   3652 O OE1  . GLU B 1 159 ? 125.78300 129.04600 137.78100 1.000 87.85967  ? 159 GLU B OE1  1 
ATOM   3653 O OE2  . GLU B 1 159 ? 127.81000 128.38000 137.26500 1.000 88.35129  ? 159 GLU B OE2  1 
ATOM   3654 N N    . LEU B 1 160 ? 124.12100 132.38400 133.80300 1.000 86.10530  ? 160 LEU B N    1 
ATOM   3655 C CA   . LEU B 1 160 ? 123.70300 133.75000 133.52000 1.000 85.88368  ? 160 LEU B CA   1 
ATOM   3656 C C    . LEU B 1 160 ? 122.37300 134.03800 134.19400 1.000 86.35817  ? 160 LEU B C    1 
ATOM   3657 O O    . LEU B 1 160 ? 122.10600 135.17600 134.59600 1.000 85.49585  ? 160 LEU B O    1 
ATOM   3658 C CB   . LEU B 1 160 ? 123.60300 133.98100 132.01300 1.000 86.01180  ? 160 LEU B CB   1 
ATOM   3659 C CG   . LEU B 1 160 ? 124.76200 134.74300 131.36900 1.000 86.06188  ? 160 LEU B CG   1 
ATOM   3660 C CD1  . LEU B 1 160 ? 124.65800 134.69800 129.85400 1.000 87.48111  ? 160 LEU B CD1  1 
ATOM   3661 C CD2  . LEU B 1 160 ? 124.78900 136.17800 131.86400 1.000 85.78677  ? 160 LEU B CD2  1 
ATOM   3662 N N    . SER B 1 161 ? 121.53000 133.01100 134.32300 1.000 90.11210  ? 161 SER B N    1 
ATOM   3663 C CA   . SER B 1 161 ? 120.22600 133.19700 134.95000 1.000 89.11899  ? 161 SER B CA   1 
ATOM   3664 C C    . SER B 1 161 ? 120.39400 133.63300 136.39800 1.000 88.49843  ? 161 SER B C    1 
ATOM   3665 O O    . SER B 1 161 ? 119.76400 134.59500 136.85200 1.000 90.25961  ? 161 SER B O    1 
ATOM   3666 C CB   . SER B 1 161 ? 119.40800 131.90900 134.86200 1.000 88.79084  ? 161 SER B CB   1 
ATOM   3667 O OG   . SER B 1 161 ? 118.15600 132.05700 135.50800 1.000 87.10666  ? 161 SER B OG   1 
ATOM   3668 N N    . THR B 1 162 ? 121.24400 132.92000 137.14300 1.000 96.12085  ? 162 THR B N    1 
ATOM   3669 C CA   . THR B 1 162 ? 121.41800 133.20900 138.56500 1.000 97.45070  ? 162 THR B CA   1 
ATOM   3670 C C    . THR B 1 162 ? 121.79900 134.66700 138.79900 1.000 96.86783  ? 162 THR B C    1 
ATOM   3671 O O    . THR B 1 162 ? 121.37500 135.27800 139.78700 1.000 96.00150  ? 162 THR B O    1 
ATOM   3672 C CB   . THR B 1 162 ? 122.48100 132.28900 139.16300 1.000 97.31281  ? 162 THR B CB   1 
ATOM   3673 O OG1  . THR B 1 162 ? 123.78300 132.80300 138.86000 1.000 97.45652  ? 162 THR B OG1  1 
ATOM   3674 C CG2  . THR B 1 162 ? 122.35400 130.89900 138.57900 1.000 97.19467  ? 162 THR B CG2  1 
ATOM   3675 N N    . LEU B 1 163 ? 122.60200 135.24000 137.90000 1.000 96.75905  ? 163 LEU B N    1 
ATOM   3676 C CA   . LEU B 1 163 ? 123.03000 136.62900 138.04400 1.000 96.59725  ? 163 LEU B CA   1 
ATOM   3677 C C    . LEU B 1 163 ? 121.85300 137.59400 138.09600 1.000 98.19164  ? 163 LEU B C    1 
ATOM   3678 O O    . LEU B 1 163 ? 121.92100 138.61400 138.79200 1.000 97.52084  ? 163 LEU B O    1 
ATOM   3679 C CB   . LEU B 1 163 ? 123.97000 137.00600 136.89700 1.000 96.51984  ? 163 LEU B CB   1 
ATOM   3680 C CG   . LEU B 1 163 ? 124.66100 138.36700 136.99200 1.000 96.89345  ? 163 LEU B CG   1 
ATOM   3681 C CD1  . LEU B 1 163 ? 126.04400 138.31100 136.36400 1.000 97.47663  ? 163 LEU B CD1  1 
ATOM   3682 C CD2  . LEU B 1 163 ? 123.81600 139.44900 136.33500 1.000 95.94854  ? 163 LEU B CD2  1 
ATOM   3683 N N    . PHE B 1 164 ? 120.77200 137.30000 137.37100 1.000 101.27307 ? 164 PHE B N    1 
ATOM   3684 C CA   . PHE B 1 164 ? 119.64800 138.23100 137.31500 1.000 100.17582 ? 164 PHE B CA   1 
ATOM   3685 C C    . PHE B 1 164 ? 119.08100 138.51400 138.70100 1.000 99.44833  ? 164 PHE B C    1 
ATOM   3686 O O    . PHE B 1 164 ? 118.78100 139.66700 139.03000 1.000 98.43251  ? 164 PHE B O    1 
ATOM   3687 C CB   . PHE B 1 164 ? 118.56400 137.68900 136.38500 1.000 98.57502  ? 164 PHE B CB   1 
ATOM   3688 C CG   . PHE B 1 164 ? 118.77900 138.04300 134.94300 1.000 98.32393  ? 164 PHE B CG   1 
ATOM   3689 C CD1  . PHE B 1 164 ? 120.02500 137.89300 134.35800 1.000 98.28579  ? 164 PHE B CD1  1 
ATOM   3690 C CD2  . PHE B 1 164 ? 117.73900 138.53500 134.17300 1.000 99.80487  ? 164 PHE B CD2  1 
ATOM   3691 C CE1  . PHE B 1 164 ? 120.22900 138.22200 133.03200 1.000 99.22640  ? 164 PHE B CE1  1 
ATOM   3692 C CE2  . PHE B 1 164 ? 117.93600 138.86500 132.84600 1.000 100.81579 ? 164 PHE B CE2  1 
ATOM   3693 C CZ   . PHE B 1 164 ? 119.18300 138.70800 132.27500 1.000 99.85713  ? 164 PHE B CZ   1 
ATOM   3694 N N    . GLY B 1 165 ? 118.92800 137.48900 139.52600 1.000 100.94779 ? 165 GLY B N    1 
ATOM   3695 C CA   . GLY B 1 165 ? 118.42500 137.66900 140.87800 1.000 101.39551 ? 165 GLY B CA   1 
ATOM   3696 C C    . GLY B 1 165 ? 116.94700 137.31800 140.98600 1.000 101.50078 ? 165 GLY B C    1 
ATOM   3697 O O    . GLY B 1 165 ? 116.53200 136.22700 140.59800 1.000 101.85251 ? 165 GLY B O    1 
ATOM   3698 N N    . ASP B 1 166 ? 116.15700 138.25100 141.52200 1.000 103.99227 ? 166 ASP B N    1 
ATOM   3699 C CA   . ASP B 1 166 ? 114.73600 137.99000 141.73500 1.000 104.22138 ? 166 ASP B CA   1 
ATOM   3700 C C    . ASP B 1 166 ? 114.03700 137.63600 140.42800 1.000 104.31338 ? 166 ASP B C    1 
ATOM   3701 O O    . ASP B 1 166 ? 113.28400 136.65700 140.36000 1.000 103.21722 ? 166 ASP B O    1 
ATOM   3702 C CB   . ASP B 1 166 ? 114.07500 139.20300 142.39000 1.000 104.12383 ? 166 ASP B CB   1 
ATOM   3703 C CG   . ASP B 1 166 ? 114.59900 140.51700 141.84300 1.000 103.97674 ? 166 ASP B CG   1 
ATOM   3704 O OD1  . ASP B 1 166 ? 115.17400 140.51400 140.73400 1.000 103.35322 ? 166 ASP B OD1  1 
ATOM   3705 O OD2  . ASP B 1 166 ? 114.43500 141.55200 142.52200 1.000 103.97350 ? 166 ASP B OD2  1 
ATOM   3706 N N    . TRP B 1 167 ? 114.26900 138.42000 139.37500 1.000 104.31050 ? 167 TRP B N    1 
ATOM   3707 C CA   . TRP B 1 167 ? 113.64100 138.16300 138.07900 1.000 103.70213 ? 167 TRP B CA   1 
ATOM   3708 C C    . TRP B 1 167 ? 114.37700 137.02800 137.36100 1.000 104.53821 ? 167 TRP B C    1 
ATOM   3709 O O    . TRP B 1 167 ? 114.92600 137.18100 136.27100 1.000 104.93997 ? 167 TRP B O    1 
ATOM   3710 C CB   . TRP B 1 167 ? 113.60800 139.42900 137.23100 1.000 102.97736 ? 167 TRP B CB   1 
ATOM   3711 C CG   . TRP B 1 167 ? 113.28000 140.68600 137.98500 1.000 104.06504 ? 167 TRP B CG   1 
ATOM   3712 C CD1  . TRP B 1 167 ? 112.54000 140.79300 139.12900 1.000 104.17392 ? 167 TRP B CD1  1 
ATOM   3713 C CD2  . TRP B 1 167 ? 113.67100 142.02000 137.63600 1.000 104.76689 ? 167 TRP B CD2  1 
ATOM   3714 N NE1  . TRP B 1 167 ? 112.45500 142.10800 139.51600 1.000 104.64365 ? 167 TRP B NE1  1 
ATOM   3715 C CE2  . TRP B 1 167 ? 113.14000 142.88100 138.61600 1.000 104.64659 ? 167 TRP B CE2  1 
ATOM   3716 C CE3  . TRP B 1 167 ? 114.42300 142.56800 136.59200 1.000 103.91307 ? 167 TRP B CE3  1 
ATOM   3717 C CZ2  . TRP B 1 167 ? 113.33600 144.26000 138.58300 1.000 103.94100 ? 167 TRP B CZ2  1 
ATOM   3718 C CZ3  . TRP B 1 167 ? 114.61600 143.93700 136.56100 1.000 103.62139 ? 167 TRP B CZ3  1 
ATOM   3719 C CH2  . TRP B 1 167 ? 114.07500 144.76700 137.54900 1.000 103.92944 ? 167 TRP B CH2  1 
ATOM   3720 N N    . GLU B 1 168 ? 114.37600 135.86500 138.01100 1.000 96.81004  ? 168 GLU B N    1 
ATOM   3721 C CA   . GLU B 1 168 ? 115.04300 134.67700 137.49300 1.000 96.99264  ? 168 GLU B CA   1 
ATOM   3722 C C    . GLU B 1 168 ? 114.13400 133.86600 136.57600 1.000 97.27821  ? 168 GLU B C    1 
ATOM   3723 O O    . GLU B 1 168 ? 114.55400 133.44500 135.49300 1.000 97.18178  ? 168 GLU B O    1 
ATOM   3724 C CB   . GLU B 1 168 ? 115.53500 133.80800 138.65500 1.000 96.68157  ? 168 GLU B CB   1 
ATOM   3725 C CG   . GLU B 1 168 ? 117.04600 133.65800 138.72300 1.000 97.28032  ? 168 GLU B CG   1 
ATOM   3726 C CD   . GLU B 1 168 ? 117.51600 133.09100 140.04900 1.000 97.30096  ? 168 GLU B CD   1 
ATOM   3727 O OE1  . GLU B 1 168 ? 117.11600 131.95700 140.38700 1.000 96.70137  ? 168 GLU B OE1  1 
ATOM   3728 O OE2  . GLU B 1 168 ? 118.28600 133.77800 140.75100 1.000 97.40561  ? 168 GLU B OE2  1 
ATOM   3729 N N    . GLU B 1 169 ? 112.88800 133.64100 136.99600 1.000 90.13412  ? 169 GLU B N    1 
ATOM   3730 C CA   . GLU B 1 169 ? 111.95900 132.85600 136.18900 1.000 89.57116  ? 169 GLU B CA   1 
ATOM   3731 C C    . GLU B 1 169 ? 111.68300 133.52700 134.84900 1.000 89.49739  ? 169 GLU B C    1 
ATOM   3732 O O    . GLU B 1 169 ? 111.52300 132.84800 133.82800 1.000 90.74525  ? 169 GLU B O    1 
ATOM   3733 C CB   . GLU B 1 169 ? 110.65600 132.63600 136.95700 1.000 88.48358  ? 169 GLU B CB   1 
ATOM   3734 C CG   . GLU B 1 169 ? 110.84800 132.05400 138.34800 1.000 89.80660  ? 169 GLU B CG   1 
ATOM   3735 C CD   . GLU B 1 169 ? 111.64600 130.76600 138.33700 1.000 90.75143  ? 169 GLU B CD   1 
ATOM   3736 O OE1  . GLU B 1 169 ? 112.89300 130.83800 138.36100 1.000 89.51733  ? 169 GLU B OE1  1 
ATOM   3737 O OE2  . GLU B 1 169 ? 111.02700 129.68200 138.30700 1.000 91.25715  ? 169 GLU B OE2  1 
ATOM   3738 N N    . ILE B 1 170 ? 111.60800 134.85900 134.83600 1.000 80.40901  ? 170 ILE B N    1 
ATOM   3739 C CA   . ILE B 1 170 ? 111.35300 135.57200 133.58800 1.000 81.00308  ? 170 ILE B CA   1 
ATOM   3740 C C    . ILE B 1 170 ? 112.46700 135.31000 132.58300 1.000 81.86520  ? 170 ILE B C    1 
ATOM   3741 O O    . ILE B 1 170 ? 112.20900 135.09200 131.39300 1.000 82.97467  ? 170 ILE B O    1 
ATOM   3742 C CB   . ILE B 1 170 ? 111.17900 137.07700 133.86100 1.000 80.42543  ? 170 ILE B CB   1 
ATOM   3743 C CG1  . ILE B 1 170 ? 110.10100 137.30300 134.92300 1.000 80.32887  ? 170 ILE B CG1  1 
ATOM   3744 C CG2  . ILE B 1 170 ? 110.83200 137.81500 132.57800 1.000 80.61093  ? 170 ILE B CG2  1 
ATOM   3745 C CD1  . ILE B 1 170 ? 108.88700 136.41800 134.75600 1.000 80.02040  ? 170 ILE B CD1  1 
ATOM   3746 N N    . PHE B 1 171 ? 113.72000 135.30300 133.04400 1.000 81.64874  ? 171 PHE B N    1 
ATOM   3747 C CA   . PHE B 1 171 ? 114.83500 135.02300 132.14300 1.000 81.90635  ? 171 PHE B CA   1 
ATOM   3748 C C    . PHE B 1 171 ? 114.71700 133.62600 131.54300 1.000 81.50171  ? 171 PHE B C    1 
ATOM   3749 O O    . PHE B 1 171 ? 114.91900 133.43600 130.33700 1.000 82.82841  ? 171 PHE B O    1 
ATOM   3750 C CB   . PHE B 1 171 ? 116.16100 135.18500 132.88600 1.000 81.00055  ? 171 PHE B CB   1 
ATOM   3751 C CG   . PHE B 1 171 ? 117.37000 135.01200 132.01400 1.000 82.92185  ? 171 PHE B CG   1 
ATOM   3752 C CD1  . PHE B 1 171 ? 117.38300 135.50400 130.72000 1.000 83.10348  ? 171 PHE B CD1  1 
ATOM   3753 C CD2  . PHE B 1 171 ? 118.49300 134.35700 132.48700 1.000 82.36980  ? 171 PHE B CD2  1 
ATOM   3754 C CE1  . PHE B 1 171 ? 118.49400 135.34600 129.91400 1.000 82.34498  ? 171 PHE B CE1  1 
ATOM   3755 C CE2  . PHE B 1 171 ? 119.60700 134.19600 131.68600 1.000 82.79594  ? 171 PHE B CE2  1 
ATOM   3756 C CZ   . PHE B 1 171 ? 119.60700 134.69100 130.39800 1.000 82.63673  ? 171 PHE B CZ   1 
ATOM   3757 N N    . CYS B 1 172 ? 114.39300 132.63300 132.37200 1.000 66.62253  ? 172 CYS B N    1 
ATOM   3758 C CA   . CYS B 1 172 ? 114.26900 131.26800 131.87700 1.000 68.40843  ? 172 CYS B CA   1 
ATOM   3759 C C    . CYS B 1 172 ? 113.15100 131.16800 130.84700 1.000 71.79106  ? 172 CYS B C    1 
ATOM   3760 O O    . CYS B 1 172 ? 113.32800 130.57800 129.77200 1.000 74.45695  ? 172 CYS B O    1 
ATOM   3761 C CB   . CYS B 1 172 ? 114.02000 130.31200 133.04400 1.000 69.03558  ? 172 CYS B CB   1 
ATOM   3762 S SG   . CYS B 1 172 ? 115.51900 129.68400 133.83400 1.000 75.79598  ? 172 CYS B SG   1 
ATOM   3763 N N    . THR B 1 173 ? 111.96800 131.68400 131.19200 1.000 63.90289  ? 173 THR B N    1 
ATOM   3764 C CA   . THR B 1 173 ? 110.84300 131.63100 130.26700 1.000 60.26661  ? 173 THR B CA   1 
ATOM   3765 C C    . THR B 1 173 ? 111.13100 132.40500 128.98600 1.000 60.31345  ? 173 THR B C    1 
ATOM   3766 O O    . THR B 1 173 ? 110.56000 132.09500 127.93500 1.000 64.39682  ? 173 THR B O    1 
ATOM   3767 C CB   . THR B 1 173 ? 109.58200 132.17100 130.94200 1.000 61.15226  ? 173 THR B CB   1 
ATOM   3768 O OG1  . THR B 1 173 ? 109.58800 131.80500 132.32700 1.000 62.23091  ? 173 THR B OG1  1 
ATOM   3769 C CG2  . THR B 1 173 ? 108.33800 131.59900 130.28200 1.000 62.88606  ? 173 THR B CG2  1 
ATOM   3770 N N    . LEU B 1 174 ? 112.01200 133.40700 129.04600 1.000 51.06823  ? 174 LEU B N    1 
ATOM   3771 C CA   . LEU B 1 174 ? 112.34300 134.17700 127.85500 1.000 54.10756  ? 174 LEU B CA   1 
ATOM   3772 C C    . LEU B 1 174 ? 113.43800 133.52500 127.02700 1.000 58.27015  ? 174 LEU B C    1 
ATOM   3773 O O    . LEU B 1 174 ? 113.59500 133.86600 125.84900 1.000 59.24974  ? 174 LEU B O    1 
ATOM   3774 C CB   . LEU B 1 174 ? 112.77700 135.59500 128.24000 1.000 55.90728  ? 174 LEU B CB   1 
ATOM   3775 C CG   . LEU B 1 174 ? 111.76600 136.70900 127.96700 1.000 58.89696  ? 174 LEU B CG   1 
ATOM   3776 C CD1  . LEU B 1 174 ? 111.56300 136.89000 126.47100 1.000 57.04469  ? 174 LEU B CD1  1 
ATOM   3777 C CD2  . LEU B 1 174 ? 110.44500 136.41800 128.66300 1.000 57.77547  ? 174 LEU B CD2  1 
ATOM   3778 N N    . SER B 1 175 ? 114.19200 132.60200 127.61700 1.000 48.84794  ? 175 SER B N    1 
ATOM   3779 C CA   . SER B 1 175 ? 115.19900 131.85800 126.87300 1.000 46.96539  ? 175 SER B CA   1 
ATOM   3780 C C    . SER B 1 175 ? 114.61700 130.61000 126.22800 1.000 46.49158  ? 175 SER B C    1 
ATOM   3781 O O    . SER B 1 175 ? 115.04600 130.21900 125.13200 1.000 47.21122  ? 175 SER B O    1 
ATOM   3782 C CB   . SER B 1 175 ? 116.35800 131.46700 127.79300 1.000 47.02934  ? 175 SER B CB   1 
ATOM   3783 O OG   . SER B 1 175 ? 115.87600 130.90200 128.99900 1.000 47.17827  ? 175 SER B OG   1 
ATOM   3784 N N    . ILE B 1 176 ? 113.63800 129.98700 126.88900 1.000 36.49270  ? 176 ILE B N    1 
ATOM   3785 C CA   . ILE B 1 176 ? 112.96800 128.82600 126.31000 1.000 35.99064  ? 176 ILE B CA   1 
ATOM   3786 C C    . ILE B 1 176 ? 112.24600 129.19700 125.02300 1.000 36.79343  ? 176 ILE B C    1 
ATOM   3787 O O    . ILE B 1 176 ? 112.22400 128.41100 124.06900 1.000 34.51218  ? 176 ILE B O    1 
ATOM   3788 C CB   . ILE B 1 176 ? 112.00200 128.20100 127.33400 1.000 34.92309  ? 176 ILE B CB   1 
ATOM   3789 C CG1  . ILE B 1 176 ? 112.76300 127.75700 128.58500 1.000 41.09828  ? 176 ILE B CG1  1 
ATOM   3790 C CG2  . ILE B 1 176 ? 111.24200 127.04200 126.71300 1.000 37.15066  ? 176 ILE B CG2  1 
ATOM   3791 C CD1  . ILE B 1 176 ? 112.03200 126.72300 129.41100 1.000 39.10689  ? 176 ILE B CD1  1 
ATOM   3792 N N    . PHE B 1 177 ? 111.70100 130.41400 124.94500 1.000 35.64826  ? 177 PHE B N    1 
ATOM   3793 C CA   . PHE B 1 177 ? 111.02000 130.83600 123.72500 1.000 31.19372  ? 177 PHE B CA   1 
ATOM   3794 C C    . PHE B 1 177 ? 111.99700 130.96900 122.56400 1.000 33.09330  ? 177 PHE B C    1 
ATOM   3795 O O    . PHE B 1 177 ? 111.71500 130.50900 121.45000 1.000 33.71279  ? 177 PHE B O    1 
ATOM   3796 C CB   . PHE B 1 177 ? 110.28900 132.15900 123.97000 1.000 33.17413  ? 177 PHE B CB   1 
ATOM   3797 C CG   . PHE B 1 177 ? 109.59800 132.71400 122.75200 1.000 35.63200  ? 177 PHE B CG   1 
ATOM   3798 C CD1  . PHE B 1 177 ? 110.30200 133.43700 121.80300 1.000 34.37946  ? 177 PHE B CD1  1 
ATOM   3799 C CD2  . PHE B 1 177 ? 108.24200 132.51900 122.56100 1.000 36.43597  ? 177 PHE B CD2  1 
ATOM   3800 C CE1  . PHE B 1 177 ? 109.67200 133.94400 120.68700 1.000 31.37462  ? 177 PHE B CE1  1 
ATOM   3801 C CE2  . PHE B 1 177 ? 107.60600 133.02600 121.44600 1.000 36.34565  ? 177 PHE B CE2  1 
ATOM   3802 C CZ   . PHE B 1 177 ? 108.32200 133.74000 120.50800 1.000 34.06657  ? 177 PHE B CZ   1 
ATOM   3803 N N    . CYS B 1 178 ? 113.16400 131.56600 122.80900 1.000 38.32193  ? 178 CYS B N    1 
ATOM   3804 C CA   . CYS B 1 178 ? 114.12200 131.76400 121.72800 1.000 35.75019  ? 178 CYS B CA   1 
ATOM   3805 C C    . CYS B 1 178 ? 114.76000 130.45100 121.30200 1.000 34.42039  ? 178 CYS B C    1 
ATOM   3806 O O    . CYS B 1 178 ? 115.00900 130.24200 120.10700 1.000 37.91358  ? 178 CYS B O    1 
ATOM   3807 C CB   . CYS B 1 178 ? 115.19600 132.76400 122.15400 1.000 37.06022  ? 178 CYS B CB   1 
ATOM   3808 S SG   . CYS B 1 178 ? 114.55400 134.23800 122.97600 1.000 49.93540  ? 178 CYS B SG   1 
ATOM   3809 N N    . ILE B 1 179 ? 114.97000 129.52900 122.24400 1.000 30.43623  ? 179 ILE B N    1 
ATOM   3810 C CA   . ILE B 1 179 ? 115.51400 128.23300 121.85700 1.000 26.85948  ? 179 ILE B CA   1 
ATOM   3811 C C    . ILE B 1 179 ? 114.47800 127.43000 121.08300 1.000 29.81348  ? 179 ILE B C    1 
ATOM   3812 O O    . ILE B 1 179 ? 114.80800 126.76600 120.09400 1.000 37.16966  ? 179 ILE B O    1 
ATOM   3813 C CB   . ILE B 1 179 ? 116.02000 127.47100 123.09400 1.000 33.13772  ? 179 ILE B CB   1 
ATOM   3814 C CG1  . ILE B 1 179 ? 117.05800 128.30900 123.84200 1.000 35.10520  ? 179 ILE B CG1  1 
ATOM   3815 C CG2  . ILE B 1 179 ? 116.60700 126.13100 122.68700 1.000 31.86842  ? 179 ILE B CG2  1 
ATOM   3816 C CD1  . ILE B 1 179 ? 118.30100 128.60500 123.03000 1.000 33.24493  ? 179 ILE B CD1  1 
ATOM   3817 N N    . GLY B 1 180 ? 113.20600 127.51100 121.48200 1.000 21.74327  ? 180 GLY B N    1 
ATOM   3818 C CA   . GLY B 1 180 ? 112.17300 126.83300 120.72100 1.000 18.54391  ? 180 GLY B CA   1 
ATOM   3819 C C    . GLY B 1 180 ? 112.04600 127.38800 119.31800 1.000 24.43311  ? 180 GLY B C    1 
ATOM   3820 O O    . GLY B 1 180 ? 111.92000 126.63500 118.34700 1.000 28.77627  ? 180 GLY B O    1 
ATOM   3821 N N    . PHE B 1 181 ? 112.16300 128.71200 119.18000 1.000 29.58764  ? 181 PHE B N    1 
ATOM   3822 C CA   . PHE B 1 181 ? 112.04100 129.31300 117.85900 1.000 25.65155  ? 181 PHE B CA   1 
ATOM   3823 C C    . PHE B 1 181 ? 113.20900 128.91300 116.97100 1.000 29.65437  ? 181 PHE B C    1 
ATOM   3824 O O    . PHE B 1 181 ? 113.00700 128.53900 115.80900 1.000 32.72817  ? 181 PHE B O    1 
ATOM   3825 C CB   . PHE B 1 181 ? 111.94600 130.83500 117.97100 1.000 24.27173  ? 181 PHE B CB   1 
ATOM   3826 C CG   . PHE B 1 181 ? 111.92600 131.54000 116.64100 1.000 31.94089  ? 181 PHE B CG   1 
ATOM   3827 C CD1  . PHE B 1 181 ? 113.10700 131.85600 115.98700 1.000 33.38238  ? 181 PHE B CD1  1 
ATOM   3828 C CD2  . PHE B 1 181 ? 110.72700 131.87700 116.04000 1.000 32.99409  ? 181 PHE B CD2  1 
ATOM   3829 C CE1  . PHE B 1 181 ? 113.08900 132.49400 114.76300 1.000 32.13947  ? 181 PHE B CE1  1 
ATOM   3830 C CE2  . PHE B 1 181 ? 110.70300 132.51700 114.81600 1.000 30.92289  ? 181 PHE B CE2  1 
ATOM   3831 C CZ   . PHE B 1 181 ? 111.88600 132.82600 114.17800 1.000 29.98252  ? 181 PHE B CZ   1 
ATOM   3832 N N    . LEU B 1 182 ? 114.43600 128.95300 117.49700 1.000 27.64846  ? 182 LEU B N    1 
ATOM   3833 C CA   . LEU B 1 182 ? 115.57000 128.64400 116.63300 1.000 27.87310  ? 182 LEU B CA   1 
ATOM   3834 C C    . LEU B 1 182 ? 115.62900 127.15700 116.30800 1.000 30.51036  ? 182 LEU B C    1 
ATOM   3835 O O    . LEU B 1 182 ? 115.97000 126.78500 115.17500 1.000 32.60297  ? 182 LEU B O    1 
ATOM   3836 C CB   . LEU B 1 182 ? 116.87400 129.10100 117.28500 1.000 30.87088  ? 182 LEU B CB   1 
ATOM   3837 C CG   . LEU B 1 182 ? 117.06500 130.61100 117.44500 1.000 30.33225  ? 182 LEU B CG   1 
ATOM   3838 C CD1  . LEU B 1 182 ? 118.05100 130.91600 118.56100 1.000 28.35971  ? 182 LEU B CD1  1 
ATOM   3839 C CD2  . LEU B 1 182 ? 117.52100 131.23600 116.13700 1.000 32.83799  ? 182 LEU B CD2  1 
ATOM   3840 N N    . ALA B 1 183 ? 115.20800 126.29700 117.24300 1.000 31.07785  ? 183 ALA B N    1 
ATOM   3841 C CA   . ALA B 1 183 ? 115.25000 124.86300 117.00300 1.000 24.61563  ? 183 ALA B CA   1 
ATOM   3842 C C    . ALA B 1 183 ? 114.08400 124.39400 116.15200 1.000 33.43773  ? 183 ALA B C    1 
ATOM   3843 O O    . ALA B 1 183 ? 114.13100 123.28100 115.61800 1.000 34.94157  ? 183 ALA B O    1 
ATOM   3844 C CB   . ALA B 1 183 ? 115.26600 124.10300 118.33000 1.000 25.99729  ? 183 ALA B CB   1 
ATOM   3845 N N    . THR B 1 184 ? 113.04200 125.21500 116.00900 1.000 33.92961  ? 184 THR B N    1 
ATOM   3846 C CA   . THR B 1 184 ? 111.97100 124.88000 115.08800 1.000 28.86904  ? 184 THR B CA   1 
ATOM   3847 C C    . THR B 1 184 ? 112.18900 125.50900 113.72300 1.000 29.81544  ? 184 THR B C    1 
ATOM   3848 O O    . THR B 1 184 ? 111.64100 125.01500 112.73100 1.000 33.43200  ? 184 THR B O    1 
ATOM   3849 C CB   . THR B 1 184 ? 110.61900 125.33000 115.65000 1.000 33.05360  ? 184 THR B CB   1 
ATOM   3850 O OG1  . THR B 1 184 ? 110.50100 124.90200 117.01200 1.000 35.65606  ? 184 THR B OG1  1 
ATOM   3851 C CG2  . THR B 1 184 ? 109.48100 124.73500 114.83800 1.000 28.17994  ? 184 THR B CG2  1 
ATOM   3852 N N    . PHE B 1 185 ? 112.98300 126.58000 113.65200 1.000 33.90897  ? 185 PHE B N    1 
ATOM   3853 C CA   . PHE B 1 185 ? 113.26200 127.24100 112.38700 1.000 32.01454  ? 185 PHE B CA   1 
ATOM   3854 C C    . PHE B 1 185 ? 114.45900 126.64400 111.66300 1.000 36.22766  ? 185 PHE B C    1 
ATOM   3855 O O    . PHE B 1 185 ? 114.56500 126.80300 110.44200 1.000 34.35685  ? 185 PHE B O    1 
ATOM   3856 C CB   . PHE B 1 185 ? 113.50200 128.73700 112.60600 1.000 32.46323  ? 185 PHE B CB   1 
ATOM   3857 C CG   . PHE B 1 185 ? 113.53800 129.53200 111.33400 1.000 34.36535  ? 185 PHE B CG   1 
ATOM   3858 C CD1  . PHE B 1 185 ? 112.36700 129.92300 110.71200 1.000 34.29508  ? 185 PHE B CD1  1 
ATOM   3859 C CD2  . PHE B 1 185 ? 114.74600 129.88100 110.75600 1.000 34.13195  ? 185 PHE B CD2  1 
ATOM   3860 C CE1  . PHE B 1 185 ? 112.39900 130.65100 109.54100 1.000 33.08529  ? 185 PHE B CE1  1 
ATOM   3861 C CE2  . PHE B 1 185 ? 114.78300 130.60900 109.58500 1.000 35.55655  ? 185 PHE B CE2  1 
ATOM   3862 C CZ   . PHE B 1 185 ? 113.60800 130.99400 108.97700 1.000 33.85739  ? 185 PHE B CZ   1 
ATOM   3863 N N    . MET B 1 186 ? 115.35600 125.95900 112.37500 1.000 45.83067  ? 186 MET B N    1 
ATOM   3864 C CA   . MET B 1 186 ? 116.51800 125.37600 111.72000 1.000 39.03366  ? 186 MET B CA   1 
ATOM   3865 C C    . MET B 1 186 ? 116.28000 123.93900 111.28000 1.000 37.49133  ? 186 MET B C    1 
ATOM   3866 O O    . MET B 1 186 ? 117.11100 123.38300 110.55500 1.000 39.49740  ? 186 MET B O    1 
ATOM   3867 C CB   . MET B 1 186 ? 117.73500 125.43300 112.64800 1.000 35.78555  ? 186 MET B CB   1 
ATOM   3868 C CG   . MET B 1 186 ? 118.64800 126.62100 112.39800 1.000 38.60295  ? 186 MET B CG   1 
ATOM   3869 S SD   . MET B 1 186 ? 120.23100 126.46400 113.24400 1.000 52.87047  ? 186 MET B SD   1 
ATOM   3870 C CE   . MET B 1 186 ? 120.27800 128.00000 114.16300 1.000 42.35282  ? 186 MET B CE   1 
ATOM   3871 N N    . LYS B 1 187 ? 115.17200 123.33300 111.69700 1.000 39.11213  ? 187 LYS B N    1 
ATOM   3872 C CA   . LYS B 1 187 ? 114.78100 122.00200 111.25500 1.000 40.69296  ? 187 LYS B CA   1 
ATOM   3873 C C    . LYS B 1 187 ? 113.98300 122.02300 109.95600 1.000 39.00134  ? 187 LYS B C    1 
ATOM   3874 O O    . LYS B 1 187 ? 113.71300 120.95700 109.39300 1.000 37.54340  ? 187 LYS B O    1 
ATOM   3875 C CB   . LYS B 1 187 ? 113.97300 121.30600 112.35900 1.000 38.98485  ? 187 LYS B CB   1 
ATOM   3876 C CG   . LYS B 1 187 ? 113.31200 120.00500 111.94400 1.000 38.56691  ? 187 LYS B CG   1 
ATOM   3877 C CD   . LYS B 1 187 ? 111.96900 119.81500 112.62900 1.000 41.49230  ? 187 LYS B CD   1 
ATOM   3878 C CE   . LYS B 1 187 ? 111.15200 121.09500 112.62300 1.000 44.38291  ? 187 LYS B CE   1 
ATOM   3879 N NZ   . LYS B 1 187 ? 110.08800 121.07100 113.66200 1.000 42.72435  ? 187 LYS B NZ   1 
ATOM   3880 N N    . LEU B 1 188 ? 113.62200 123.20500 109.46000 1.000 40.45105  ? 188 LEU B N    1 
ATOM   3881 C CA   . LEU B 1 188 ? 112.78700 123.35500 108.27500 1.000 40.64269  ? 188 LEU B CA   1 
ATOM   3882 C C    . LEU B 1 188 ? 113.58100 123.75800 107.04000 1.000 40.56448  ? 188 LEU B C    1 
ATOM   3883 O O    . LEU B 1 188 ? 112.98500 124.16800 106.04000 1.000 40.57441  ? 188 LEU B O    1 
ATOM   3884 C CB   . LEU B 1 188 ? 111.68100 124.38000 108.53300 1.000 40.02710  ? 188 LEU B CB   1 
ATOM   3885 C CG   . LEU B 1 188 ? 110.72900 124.11800 109.70000 1.000 39.89267  ? 188 LEU B CG   1 
ATOM   3886 C CD1  . LEU B 1 188 ? 110.01000 125.39800 110.09300 1.000 38.19104  ? 188 LEU B CD1  1 
ATOM   3887 C CD2  . LEU B 1 188 ? 109.73200 123.03200 109.34100 1.000 39.03470  ? 188 LEU B CD2  1 
ATOM   3888 N N    . TYR B 1 189 ? 114.89800 123.65400 107.08400 1.000 54.36960  ? 189 TYR B N    1 
ATOM   3889 C CA   . TYR B 1 189 ? 115.71800 124.00500 105.93100 1.000 50.34993  ? 189 TYR B CA   1 
ATOM   3890 C C    . TYR B 1 189 ? 115.85800 122.79800 105.01200 1.000 54.11632  ? 189 TYR B C    1 
ATOM   3891 O O    . TYR B 1 189 ? 116.12900 121.69200 105.49300 1.000 55.84440  ? 189 TYR B O    1 
ATOM   3892 C CB   . TYR B 1 189 ? 117.09300 124.47800 106.38000 1.000 50.49777  ? 189 TYR B CB   1 
ATOM   3893 C CG   . TYR B 1 189 ? 117.63100 125.65300 105.60000 1.000 55.23737  ? 189 TYR B CG   1 
ATOM   3894 C CD1  . TYR B 1 189 ? 117.93600 125.53800 104.25100 1.000 55.60613  ? 189 TYR B CD1  1 
ATOM   3895 C CD2  . TYR B 1 189 ? 117.83000 126.88300 106.21300 1.000 55.04873  ? 189 TYR B CD2  1 
ATOM   3896 C CE1  . TYR B 1 189 ? 118.42700 126.61200 103.53400 1.000 55.31467  ? 189 TYR B CE1  1 
ATOM   3897 C CE2  . TYR B 1 189 ? 118.32000 127.96200 105.50500 1.000 55.69045  ? 189 TYR B CE2  1 
ATOM   3898 C CZ   . TYR B 1 189 ? 118.61700 127.82200 104.16700 1.000 57.78245  ? 189 TYR B CZ   1 
ATOM   3899 O OH   . TYR B 1 189 ? 119.10500 128.89500 103.45700 1.000 56.67019  ? 189 TYR B OH   1 
ATOM   3900 N N    . PRO B 1 190 ? 115.68600 122.96700 103.69700 1.000 54.55237  ? 190 PRO B N    1 
ATOM   3901 C CA   . PRO B 1 190 ? 115.69100 121.79600 102.80400 1.000 52.19126  ? 190 PRO B CA   1 
ATOM   3902 C C    . PRO B 1 190 ? 116.95600 120.96100 102.89300 1.000 50.84142  ? 190 PRO B C    1 
ATOM   3903 O O    . PRO B 1 190 ? 116.90300 119.75100 102.64000 1.000 50.25725  ? 190 PRO B O    1 
ATOM   3904 C CB   . PRO B 1 190 ? 115.52200 122.42200 101.41400 1.000 53.38591  ? 190 PRO B CB   1 
ATOM   3905 C CG   . PRO B 1 190 ? 114.82400 123.71500 101.67300 1.000 53.45422  ? 190 PRO B CG   1 
ATOM   3906 C CD   . PRO B 1 190 ? 115.38200 124.21200 102.97300 1.000 54.14316  ? 190 PRO B CD   1 
ATOM   3907 N N    . SER B 1 191 ? 118.09300 121.56500 103.24000 1.000 53.81497  ? 191 SER B N    1 
ATOM   3908 C CA   . SER B 1 191 ? 119.32200 120.79400 103.37600 1.000 53.24919  ? 191 SER B CA   1 
ATOM   3909 C C    . SER B 1 191 ? 119.34700 119.99900 104.67400 1.000 53.42251  ? 191 SER B C    1 
ATOM   3910 O O    . SER B 1 191 ? 120.01500 118.96100 104.75000 1.000 53.60886  ? 191 SER B O    1 
ATOM   3911 C CB   . SER B 1 191 ? 120.53800 121.71800 103.29700 1.000 53.72333  ? 191 SER B CB   1 
ATOM   3912 O OG   . SER B 1 191 ? 120.55700 122.63200 104.37900 1.000 54.79115  ? 191 SER B OG   1 
ATOM   3913 N N    . MET B 1 192 ? 118.63400 120.46600 105.69700 1.000 53.76311  ? 192 MET B N    1 
ATOM   3914 C CA   . MET B 1 192 ? 118.58300 119.82100 107.00700 1.000 51.75687  ? 192 MET B CA   1 
ATOM   3915 C C    . MET B 1 192 ? 117.27100 119.08000 107.22500 1.000 52.31517  ? 192 MET B C    1 
ATOM   3916 O O    . MET B 1 192 ? 116.70800 119.11100 108.32200 1.000 53.58338  ? 192 MET B O    1 
ATOM   3917 C CB   . MET B 1 192 ? 118.80500 120.85100 108.11000 1.000 50.27764  ? 192 MET B CB   1 
ATOM   3918 C CG   . MET B 1 192 ? 120.11500 120.68800 108.86000 1.000 51.19247  ? 192 MET B CG   1 
ATOM   3919 S SD   . MET B 1 192 ? 121.48500 121.55800 108.07800 1.000 58.40428  ? 192 MET B SD   1 
ATOM   3920 C CE   . MET B 1 192 ? 121.10200 123.25000 108.51900 1.000 53.71462  ? 192 MET B CE   1 
ATOM   3921 N N    . LYS B 1 193 ? 116.76000 118.40000 106.19800 1.000 50.88494  ? 193 LYS B N    1 
ATOM   3922 C CA   . LYS B 1 193 ? 115.47600 117.71800 106.27400 1.000 52.39551  ? 193 LYS B CA   1 
ATOM   3923 C C    . LYS B 1 193 ? 115.62400 116.21900 106.49700 1.000 51.61418  ? 193 LYS B C    1 
ATOM   3924 O O    . LYS B 1 193 ? 114.66600 115.46800 106.28600 1.000 52.55296  ? 193 LYS B O    1 
ATOM   3925 C CB   . LYS B 1 193 ? 114.65700 117.98100 105.01000 1.000 52.04265  ? 193 LYS B CB   1 
ATOM   3926 C CG   . LYS B 1 193 ? 114.50000 119.44800 104.65900 1.000 51.06587  ? 193 LYS B CG   1 
ATOM   3927 C CD   . LYS B 1 193 ? 113.48400 120.12400 105.56400 1.000 50.63601  ? 193 LYS B CD   1 
ATOM   3928 C CE   . LYS B 1 193 ? 112.81600 121.29600 104.86400 1.000 53.71957  ? 193 LYS B CE   1 
ATOM   3929 N NZ   . LYS B 1 193 ? 111.46300 121.58000 105.41600 1.000 52.75857  ? 193 LYS B NZ   1 
ATOM   3930 N N    . ALA B 1 194 ? 116.80400 115.77000 106.91200 1.000 54.23118  ? 194 ALA B N    1 
ATOM   3931 C CA   . ALA B 1 194 ? 117.02500 114.38400 107.30200 1.000 54.16944  ? 194 ALA B CA   1 
ATOM   3932 C C    . ALA B 1 194 ? 117.28400 114.21600 108.78900 1.000 54.22307  ? 194 ALA B C    1 
ATOM   3933 O O    . ALA B 1 194 ? 116.83300 113.23500 109.38200 1.000 60.92409  ? 194 ALA B O    1 
ATOM   3934 C CB   . ALA B 1 194 ? 118.20200 113.79300 106.51700 1.000 53.27342  ? 194 ALA B CB   1 
ATOM   3935 N N    . TYR B 1 195 ? 117.99900 115.15200 109.40200 1.000 47.26523  ? 195 TYR B N    1 
ATOM   3936 C CA   . TYR B 1 195 ? 118.41800 115.05300 110.80100 1.000 47.36365  ? 195 TYR B CA   1 
ATOM   3937 C C    . TYR B 1 195 ? 117.46200 115.77500 111.74500 1.000 46.35158  ? 195 TYR B C    1 
ATOM   3938 O O    . TYR B 1 195 ? 117.88400 116.56900 112.58200 1.000 49.64977  ? 195 TYR B O    1 
ATOM   3939 C CB   . TYR B 1 195 ? 119.84200 115.57800 110.95900 1.000 43.92007  ? 195 TYR B CB   1 
ATOM   3940 C CG   . TYR B 1 195 ? 120.74100 115.31500 109.76800 1.000 49.30819  ? 195 TYR B CG   1 
ATOM   3941 C CD1  . TYR B 1 195 ? 120.64900 114.12800 109.04700 1.000 51.17972  ? 195 TYR B CD1  1 
ATOM   3942 C CD2  . TYR B 1 195 ? 121.67700 116.25500 109.35900 1.000 48.59970  ? 195 TYR B CD2  1 
ATOM   3943 C CE1  . TYR B 1 195 ? 121.46200 113.88600 107.96000 1.000 49.31912  ? 195 TYR B CE1  1 
ATOM   3944 C CE2  . TYR B 1 195 ? 122.49600 116.02000 108.27100 1.000 51.05490  ? 195 TYR B CE2  1 
ATOM   3945 C CZ   . TYR B 1 195 ? 122.38300 114.83500 107.57600 1.000 51.42068  ? 195 TYR B CZ   1 
ATOM   3946 O OH   . TYR B 1 195 ? 123.19500 114.59400 106.49200 1.000 50.49439  ? 195 TYR B OH   1 
ATOM   3947 N N    . GLU B 1 196 ? 116.15800 115.51200 111.62700 1.000 41.24078  ? 196 GLU B N    1 
ATOM   3948 C CA   . GLU B 1 196 ? 115.20300 116.10900 112.55400 1.000 43.75314  ? 196 GLU B CA   1 
ATOM   3949 C C    . GLU B 1 196 ? 115.32200 115.51400 113.95100 1.000 44.99910  ? 196 GLU B C    1 
ATOM   3950 O O    . GLU B 1 196 ? 114.89800 116.14500 114.93000 1.000 46.80975  ? 196 GLU B O    1 
ATOM   3951 C CB   . GLU B 1 196 ? 113.77700 115.92600 112.03300 1.000 41.28062  ? 196 GLU B CB   1 
ATOM   3952 C CG   . GLU B 1 196 ? 113.36500 116.93000 110.97400 1.000 46.01350  ? 196 GLU B CG   1 
ATOM   3953 C CD   . GLU B 1 196 ? 113.90200 116.58300 109.60200 1.000 50.06187  ? 196 GLU B CD   1 
ATOM   3954 O OE1  . GLU B 1 196 ? 114.11100 117.51100 108.79500 1.000 48.50398  ? 196 GLU B OE1  1 
ATOM   3955 O OE2  . GLU B 1 196 ? 114.11400 115.38200 109.33100 1.000 50.24977  ? 196 GLU B OE2  1 
ATOM   3956 N N    . TYR B 1 197 ? 115.94000 114.34100 114.06600 1.000 31.44949  ? 197 TYR B N    1 
ATOM   3957 C CA   . TYR B 1 197 ? 116.06800 113.64100 115.33200 1.000 31.74994  ? 197 TYR B CA   1 
ATOM   3958 C C    . TYR B 1 197 ? 117.27400 114.10100 116.13400 1.000 34.50369  ? 197 TYR B C    1 
ATOM   3959 O O    . TYR B 1 197 ? 117.42100 113.69200 117.29000 1.000 40.36193  ? 197 TYR B O    1 
ATOM   3960 C CB   . TYR B 1 197 ? 116.15900 112.12900 115.08900 1.000 32.90905  ? 197 TYR B CB   1 
ATOM   3961 C CG   . TYR B 1 197 ? 117.33800 111.72900 114.23200 1.000 32.59693  ? 197 TYR B CG   1 
ATOM   3962 C CD1  . TYR B 1 197 ? 117.30600 111.89500 112.85400 1.000 30.43074  ? 197 TYR B CD1  1 
ATOM   3963 C CD2  . TYR B 1 197 ? 118.48900 111.20300 114.80000 1.000 27.80532  ? 197 TYR B CD2  1 
ATOM   3964 C CE1  . TYR B 1 197 ? 118.38100 111.54200 112.06600 1.000 30.04274  ? 197 TYR B CE1  1 
ATOM   3965 C CE2  . TYR B 1 197 ? 119.56900 110.84700 114.02000 1.000 30.84931  ? 197 TYR B CE2  1 
ATOM   3966 C CZ   . TYR B 1 197 ? 119.50900 111.01900 112.65400 1.000 33.26114  ? 197 TYR B CZ   1 
ATOM   3967 O OH   . TYR B 1 197 ? 120.58100 110.66400 111.86900 1.000 36.92582  ? 197 TYR B OH   1 
ATOM   3968 N N    . GLY B 1 198 ? 118.13800 114.92700 115.55200 1.000 26.38410  ? 198 GLY B N    1 
ATOM   3969 C CA   . GLY B 1 198 ? 119.21900 115.52300 116.30700 1.000 26.50201  ? 198 GLY B CA   1 
ATOM   3970 C C    . GLY B 1 198 ? 118.78800 116.86900 116.84900 1.000 31.19652  ? 198 GLY B C    1 
ATOM   3971 O O    . GLY B 1 198 ? 119.40500 117.40700 117.77200 1.000 39.88810  ? 198 GLY B O    1 
ATOM   3972 N N    . PHE B 1 199 ? 117.72100 117.42100 116.27000 1.000 28.86961  ? 199 PHE B N    1 
ATOM   3973 C CA   . PHE B 1 199 ? 117.13800 118.67500 116.73000 1.000 25.31143  ? 199 PHE B CA   1 
ATOM   3974 C C    . PHE B 1 199 ? 116.05300 118.44800 117.77600 1.000 26.71875  ? 199 PHE B C    1 
ATOM   3975 O O    . PHE B 1 199 ? 115.94200 119.21900 118.74000 1.000 31.35409  ? 199 PHE B O    1 
ATOM   3976 C CB   . PHE B 1 199 ? 116.55900 119.45000 115.54400 1.000 27.09553  ? 199 PHE B CB   1 
ATOM   3977 C CG   . PHE B 1 199 ? 117.59100 120.16800 114.72400 1.000 29.14034  ? 199 PHE B CG   1 
ATOM   3978 C CD1  . PHE B 1 199 ? 118.27800 121.25200 115.24200 1.000 32.33999  ? 199 PHE B CD1  1 
ATOM   3979 C CD2  . PHE B 1 199 ? 117.87300 119.75900 113.43300 1.000 29.79944  ? 199 PHE B CD2  1 
ATOM   3980 C CE1  . PHE B 1 199 ? 119.22700 121.91100 114.48800 1.000 30.34363  ? 199 PHE B CE1  1 
ATOM   3981 C CE2  . PHE B 1 199 ? 118.82200 120.41400 112.67600 1.000 28.46853  ? 199 PHE B CE2  1 
ATOM   3982 C CZ   . PHE B 1 199 ? 119.49900 121.49200 113.20300 1.000 27.94724  ? 199 PHE B CZ   1 
ATOM   3983 N N    . ARG B 1 200 ? 115.26400 117.38200 117.61500 1.000 27.92003  ? 200 ARG B N    1 
ATOM   3984 C CA   . ARG B 1 200 ? 114.23100 117.09200 118.60300 1.000 26.23824  ? 200 ARG B CA   1 
ATOM   3985 C C    . ARG B 1 200 ? 114.84300 116.74600 119.95600 1.000 33.25727  ? 200 ARG B C    1 
ATOM   3986 O O    . ARG B 1 200 ? 114.34500 117.18700 121.00000 1.000 35.25488  ? 200 ARG B O    1 
ATOM   3987 C CB   . ARG B 1 200 ? 113.33700 115.95800 118.10400 1.000 28.09058  ? 200 ARG B CB   1 
ATOM   3988 C CG   . ARG B 1 200 ? 112.59000 115.22600 119.20000 1.000 33.32062  ? 200 ARG B CG   1 
ATOM   3989 C CD   . ARG B 1 200 ? 111.29900 114.62400 118.67300 1.000 32.30783  ? 200 ARG B CD   1 
ATOM   3990 N NE   . ARG B 1 200 ? 110.68600 115.45800 117.64600 1.000 37.31063  ? 200 ARG B NE   1 
ATOM   3991 C CZ   . ARG B 1 200 ? 110.01600 114.98900 116.60300 1.000 37.89155  ? 200 ARG B CZ   1 
ATOM   3992 N NH1  . ARG B 1 200 ? 109.84200 113.69000 116.42000 1.000 36.64472  ? 200 ARG B NH1  1 
ATOM   3993 N NH2  . ARG B 1 200 ? 109.50300 115.84400 115.72300 1.000 35.56601  ? 200 ARG B NH2  1 
ATOM   3994 N N    . VAL B 1 201 ? 115.94600 115.99400 119.95800 1.000 28.44395  ? 201 VAL B N    1 
ATOM   3995 C CA   . VAL B 1 201 ? 116.59000 115.63800 121.21800 1.000 30.34110  ? 201 VAL B CA   1 
ATOM   3996 C C    . VAL B 1 201 ? 117.22700 116.86700 121.84900 1.000 24.17712  ? 201 VAL B C    1 
ATOM   3997 O O    . VAL B 1 201 ? 117.20000 117.03700 123.07300 1.000 28.64143  ? 201 VAL B O    1 
ATOM   3998 C CB   . VAL B 1 201 ? 117.62000 114.51300 121.00500 1.000 25.22254  ? 201 VAL B CB   1 
ATOM   3999 C CG1  . VAL B 1 201 ? 116.93000 113.16100 120.95800 1.000 28.24387  ? 201 VAL B CG1  1 
ATOM   4000 C CG2  . VAL B 1 201 ? 118.42400 114.75500 119.74100 1.000 28.15259  ? 201 VAL B CG2  1 
ATOM   4001 N N    . PHE B 1 202 ? 117.77800 117.75900 121.02500 1.000 17.89390  ? 202 PHE B N    1 
ATOM   4002 C CA   . PHE B 1 202 ? 118.35000 118.99600 121.54400 1.000 25.18019  ? 202 PHE B CA   1 
ATOM   4003 C C    . PHE B 1 202 ? 117.28500 119.82200 122.25300 1.000 29.19385  ? 202 PHE B C    1 
ATOM   4004 O O    . PHE B 1 202 ? 117.49200 120.29500 123.37800 1.000 31.04569  ? 202 PHE B O    1 
ATOM   4005 C CB   . PHE B 1 202 ? 118.99200 119.78400 120.39900 1.000 25.23050  ? 202 PHE B CB   1 
ATOM   4006 C CG   . PHE B 1 202 ? 119.58500 121.10600 120.81000 1.000 23.02998  ? 202 PHE B CG   1 
ATOM   4007 C CD1  . PHE B 1 202 ? 118.77800 122.20100 121.06400 1.000 29.96647  ? 202 PHE B CD1  1 
ATOM   4008 C CD2  . PHE B 1 202 ? 120.95500 121.25400 120.92900 1.000 27.94220  ? 202 PHE B CD2  1 
ATOM   4009 C CE1  . PHE B 1 202 ? 119.32500 123.41400 121.43800 1.000 29.03280  ? 202 PHE B CE1  1 
ATOM   4010 C CE2  . PHE B 1 202 ? 121.50700 122.46400 121.30200 1.000 32.02978  ? 202 PHE B CE2  1 
ATOM   4011 C CZ   . PHE B 1 202 ? 120.69000 123.54500 121.55700 1.000 26.81965  ? 202 PHE B CZ   1 
ATOM   4012 N N    . LEU B 1 203 ? 116.13000 120.00300 121.60700 1.000 30.70690  ? 203 LEU B N    1 
ATOM   4013 C CA   . LEU B 1 203 ? 115.07000 120.80300 122.21200 1.000 25.55240  ? 203 LEU B CA   1 
ATOM   4014 C C    . LEU B 1 203 ? 114.55700 120.15100 123.49100 1.000 26.74731  ? 203 LEU B C    1 
ATOM   4015 O O    . LEU B 1 203 ? 114.41600 120.81200 124.53200 1.000 30.78102  ? 203 LEU B O    1 
ATOM   4016 C CB   . LEU B 1 203 ? 113.93100 121.00500 121.21200 1.000 28.11967  ? 203 LEU B CB   1 
ATOM   4017 C CG   . LEU B 1 203 ? 112.99000 122.18500 121.46500 1.000 29.64426  ? 203 LEU B CG   1 
ATOM   4018 C CD1  . LEU B 1 203 ? 113.77300 123.42400 121.86300 1.000 29.68850  ? 203 LEU B CD1  1 
ATOM   4019 C CD2  . LEU B 1 203 ? 112.13200 122.46100 120.24400 1.000 24.78681  ? 203 LEU B CD2  1 
ATOM   4020 N N    . LEU B 1 204 ? 114.30600 118.83800 123.44400 1.000 30.74362  ? 204 LEU B N    1 
ATOM   4021 C CA   . LEU B 1 204 ? 113.79300 118.14600 124.62100 1.000 25.05812  ? 204 LEU B CA   1 
ATOM   4022 C C    . LEU B 1 204 ? 114.77600 118.22700 125.78000 1.000 28.91661  ? 204 LEU B C    1 
ATOM   4023 O O    . LEU B 1 204 ? 114.36600 118.33400 126.94100 1.000 34.90041  ? 204 LEU B O    1 
ATOM   4024 C CB   . LEU B 1 204 ? 113.48000 116.69000 124.28200 1.000 24.70826  ? 204 LEU B CB   1 
ATOM   4025 C CG   . LEU B 1 204 ? 112.19800 116.45400 123.48500 1.000 31.21579  ? 204 LEU B CG   1 
ATOM   4026 C CD1  . LEU B 1 204 ? 112.19100 115.06000 122.88100 1.000 35.44468  ? 204 LEU B CD1  1 
ATOM   4027 C CD2  . LEU B 1 204 ? 110.97300 116.67200 124.35500 1.000 31.68750  ? 204 LEU B CD2  1 
ATOM   4028 N N    . THR B 1 205 ? 116.07800 118.17400 125.49300 1.000 31.45853  ? 205 THR B N    1 
ATOM   4029 C CA   . THR B 1 205 ? 117.05300 118.19600 126.57400 1.000 31.16144  ? 205 THR B CA   1 
ATOM   4030 C C    . THR B 1 205 ? 117.15900 119.59600 127.16200 1.000 30.76769  ? 205 THR B C    1 
ATOM   4031 O O    . THR B 1 205 ? 117.16200 119.76900 128.38500 1.000 32.13706  ? 205 THR B O    1 
ATOM   4032 C CB   . THR B 1 205 ? 118.41500 117.71300 126.07100 1.000 28.96259  ? 205 THR B CB   1 
ATOM   4033 O OG1  . THR B 1 205 ? 118.30300 116.36000 125.61200 1.000 29.85397  ? 205 THR B OG1  1 
ATOM   4034 C CG2  . THR B 1 205 ? 119.44600 117.77400 127.18500 1.000 29.98255  ? 205 THR B CG2  1 
ATOM   4035 N N    . TYR B 1 206 ? 117.25800 120.61100 126.30000 1.000 37.24273  ? 206 TYR B N    1 
ATOM   4036 C CA   . TYR B 1 206 ? 117.40500 121.97500 126.79600 1.000 31.19734  ? 206 TYR B CA   1 
ATOM   4037 C C    . TYR B 1 206 ? 116.21000 122.37500 127.65000 1.000 37.65820  ? 206 TYR B C    1 
ATOM   4038 O O    . TYR B 1 206 ? 116.36800 123.02700 128.68900 1.000 38.50559  ? 206 TYR B O    1 
ATOM   4039 C CB   . TYR B 1 206 ? 117.58300 122.95400 125.63800 1.000 31.47224  ? 206 TYR B CB   1 
ATOM   4040 C CG   . TYR B 1 206 ? 117.72700 124.39000 126.09100 1.000 40.39863  ? 206 TYR B CG   1 
ATOM   4041 C CD1  . TYR B 1 206 ? 118.97600 124.92600 126.37000 1.000 35.89535  ? 206 TYR B CD1  1 
ATOM   4042 C CD2  . TYR B 1 206 ? 116.61400 125.20800 126.24600 1.000 40.23361  ? 206 TYR B CD2  1 
ATOM   4043 C CE1  . TYR B 1 206 ? 119.11400 126.23600 126.78600 1.000 38.49423  ? 206 TYR B CE1  1 
ATOM   4044 C CE2  . TYR B 1 206 ? 116.74300 126.51800 126.66300 1.000 34.86810  ? 206 TYR B CE2  1 
ATOM   4045 C CZ   . TYR B 1 206 ? 117.99600 127.02700 126.93100 1.000 38.25643  ? 206 TYR B CZ   1 
ATOM   4046 O OH   . TYR B 1 206 ? 118.13400 128.33000 127.34600 1.000 37.78052  ? 206 TYR B OH   1 
ATOM   4047 N N    . CYS B 1 207 ? 115.00200 121.99400 127.22500 1.000 43.90327  ? 207 CYS B N    1 
ATOM   4048 C CA   . CYS B 1 207 ? 113.80100 122.38400 127.96100 1.000 34.85545  ? 207 CYS B CA   1 
ATOM   4049 C C    . CYS B 1 207 ? 113.67000 121.63900 129.28600 1.000 36.04413  ? 207 CYS B C    1 
ATOM   4050 O O    . CYS B 1 207 ? 113.20100 122.20900 130.27800 1.000 42.10942  ? 207 CYS B O    1 
ATOM   4051 C CB   . CYS B 1 207 ? 112.56200 122.15900 127.09600 1.000 34.80987  ? 207 CYS B CB   1 
ATOM   4052 S SG   . CYS B 1 207 ? 112.34000 123.39000 125.79300 1.000 45.98825  ? 207 CYS B SG   1 
ATOM   4053 N N    . TYR B 1 208 ? 114.07800 120.37100 129.32900 1.000 37.89568  ? 208 TYR B N    1 
ATOM   4054 C CA   . TYR B 1 208 ? 113.99300 119.57200 130.54800 1.000 35.11735  ? 208 TYR B CA   1 
ATOM   4055 C C    . TYR B 1 208 ? 114.96800 119.99500 131.64300 1.000 37.98242  ? 208 TYR B C    1 
ATOM   4056 O O    . TYR B 1 208 ? 114.77400 119.59500 132.79500 1.000 39.11152  ? 208 TYR B O    1 
ATOM   4057 C CB   . TYR B 1 208 ? 114.19800 118.08700 130.20200 1.000 36.84301  ? 208 TYR B CB   1 
ATOM   4058 C CG   . TYR B 1 208 ? 114.75800 117.22000 131.31900 1.000 40.18887  ? 208 TYR B CG   1 
ATOM   4059 C CD1  . TYR B 1 208 ? 116.09800 117.29500 131.69200 1.000 40.39261  ? 208 TYR B CD1  1 
ATOM   4060 C CD2  . TYR B 1 208 ? 113.93900 116.34300 132.01400 1.000 41.00015  ? 208 TYR B CD2  1 
ATOM   4061 C CE1  . TYR B 1 208 ? 116.60000 116.51700 132.71500 1.000 36.73394  ? 208 TYR B CE1  1 
ATOM   4062 C CE2  . TYR B 1 208 ? 114.43500 115.56000 133.03600 1.000 38.51314  ? 208 TYR B CE2  1 
ATOM   4063 C CZ   . TYR B 1 208 ? 115.76500 115.65000 133.38200 1.000 35.42197  ? 208 TYR B CZ   1 
ATOM   4064 O OH   . TYR B 1 208 ? 116.26200 114.87200 134.40000 1.000 37.36840  ? 208 TYR B OH   1 
ATOM   4065 N N    . ILE B 1 209 ? 115.98000 120.81400 131.34800 1.000 42.22034  ? 209 ILE B N    1 
ATOM   4066 C CA   . ILE B 1 209 ? 116.97000 121.15300 132.36500 1.000 41.70355  ? 209 ILE B CA   1 
ATOM   4067 C C    . ILE B 1 209 ? 116.77300 122.55000 132.94100 1.000 43.44587  ? 209 ILE B C    1 
ATOM   4068 O O    . ILE B 1 209 ? 117.50100 122.94000 133.86500 1.000 40.48244  ? 209 ILE B O    1 
ATOM   4069 C CB   . ILE B 1 209 ? 118.39400 120.97900 131.79200 1.000 44.47056  ? 209 ILE B CB   1 
ATOM   4070 C CG1  . ILE B 1 209 ? 119.02000 119.68000 132.30600 1.000 41.26062  ? 209 ILE B CG1  1 
ATOM   4071 C CG2  . ILE B 1 209 ? 119.28100 122.17100 132.10500 1.000 41.84527  ? 209 ILE B CG2  1 
ATOM   4072 C CD1  . ILE B 1 209 ? 120.27200 119.27200 131.56500 1.000 40.51065  ? 209 ILE B CD1  1 
ATOM   4073 N N    . LEU B 1 210 ? 115.77100 123.29200 132.47200 1.000 45.27930  ? 210 LEU B N    1 
ATOM   4074 C CA   . LEU B 1 210 ? 115.49500 124.62500 132.98700 1.000 39.06057  ? 210 LEU B CA   1 
ATOM   4075 C C    . LEU B 1 210 ? 114.17700 124.71200 133.73900 1.000 42.41754  ? 210 LEU B C    1 
ATOM   4076 O O    . LEU B 1 210 ? 113.93500 125.71900 134.41300 1.000 45.82995  ? 210 LEU B O    1 
ATOM   4077 C CB   . LEU B 1 210 ? 115.49100 125.66000 131.85200 1.000 36.09259  ? 210 LEU B CB   1 
ATOM   4078 C CG   . LEU B 1 210 ? 116.80600 125.91000 131.11800 1.000 43.82680  ? 210 LEU B CG   1 
ATOM   4079 C CD1  . LEU B 1 210 ? 116.57600 126.84700 129.94600 1.000 46.33634  ? 210 LEU B CD1  1 
ATOM   4080 C CD2  . LEU B 1 210 ? 117.84600 126.48200 132.06600 1.000 41.05523  ? 210 LEU B CD2  1 
ATOM   4081 N N    . ILE B 1 211 ? 113.32500 123.69400 133.64600 1.000 44.43188  ? 211 ILE B N    1 
ATOM   4082 C CA   . ILE B 1 211 ? 112.04100 123.69400 134.33600 1.000 45.68052  ? 211 ILE B CA   1 
ATOM   4083 C C    . ILE B 1 211 ? 111.94500 122.49100 135.26500 1.000 47.27249  ? 211 ILE B C    1 
ATOM   4084 O O    . ILE B 1 211 ? 110.84400 122.02400 135.57600 1.000 51.09165  ? 211 ILE B O    1 
ATOM   4085 C CB   . ILE B 1 211 ? 110.87300 123.71000 133.33300 1.000 45.85743  ? 211 ILE B CB   1 
ATOM   4086 C CG1  . ILE B 1 211 ? 110.66500 122.32500 132.72300 1.000 44.91613  ? 211 ILE B CG1  1 
ATOM   4087 C CG2  . ILE B 1 211 ? 111.12500 124.73300 132.23800 1.000 45.46292  ? 211 ILE B CG2  1 
ATOM   4088 C CD1  . ILE B 1 211 ? 109.31000 122.14700 132.08500 1.000 46.16036  ? 211 ILE B CD1  1 
ATOM   4089 N N    . SER B 1 212 ? 113.09000 121.97700 135.71500 1.000 49.88901  ? 212 SER B N    1 
ATOM   4090 C CA   . SER B 1 212 ? 113.11200 120.78800 136.55800 1.000 49.97987  ? 212 SER B CA   1 
ATOM   4091 C C    . SER B 1 212 ? 113.80700 121.01700 137.89400 1.000 51.35341  ? 212 SER B C    1 
ATOM   4092 O O    . SER B 1 212 ? 114.05700 120.04900 138.62300 1.000 53.53262  ? 212 SER B O    1 
ATOM   4093 C CB   . SER B 1 212 ? 113.78200 119.62800 135.81500 1.000 49.98245  ? 212 SER B CB   1 
ATOM   4094 O OG   . SER B 1 212 ? 113.25200 118.37900 136.22300 1.000 49.73215  ? 212 SER B OG   1 
ATOM   4095 N N    . GLY B 1 213 ? 114.12700 122.26200 138.23700 1.000 68.44929  ? 213 GLY B N    1 
ATOM   4096 C CA   . GLY B 1 213 ? 114.72300 122.56200 139.52500 1.000 67.94629  ? 213 GLY B CA   1 
ATOM   4097 C C    . GLY B 1 213 ? 116.23100 122.43700 139.54700 1.000 68.86180  ? 213 GLY B C    1 
ATOM   4098 O O    . GLY B 1 213 ? 116.78400 121.71600 140.38200 1.000 71.15313  ? 213 GLY B O    1 
ATOM   4099 N N    . PHE B 1 214 ? 116.91300 123.13200 138.63600 1.000 78.33675  ? 214 PHE B N    1 
ATOM   4100 C CA   . PHE B 1 214 ? 118.36400 123.01800 138.55400 1.000 78.14023  ? 214 PHE B CA   1 
ATOM   4101 C C    . PHE B 1 214 ? 119.05700 123.38600 139.86200 1.000 79.59197  ? 214 PHE B C    1 
ATOM   4102 O O    . PHE B 1 214 ? 120.18400 122.93700 140.09900 1.000 79.48184  ? 214 PHE B O    1 
ATOM   4103 C CB   . PHE B 1 214 ? 118.88600 123.89000 137.41000 1.000 76.26043  ? 214 PHE B CB   1 
ATOM   4104 C CG   . PHE B 1 214 ? 120.38100 124.00900 137.36800 1.000 78.59779  ? 214 PHE B CG   1 
ATOM   4105 C CD1  . PHE B 1 214 ? 121.17500 122.88000 137.26100 1.000 78.85240  ? 214 PHE B CD1  1 
ATOM   4106 C CD2  . PHE B 1 214 ? 120.99300 125.24900 137.42200 1.000 80.33155  ? 214 PHE B CD2  1 
ATOM   4107 C CE1  . PHE B 1 214 ? 122.55200 122.98400 137.21800 1.000 79.61784  ? 214 PHE B CE1  1 
ATOM   4108 C CE2  . PHE B 1 214 ? 122.37000 125.36000 137.37800 1.000 80.65814  ? 214 PHE B CE2  1 
ATOM   4109 C CZ   . PHE B 1 214 ? 123.15000 124.22600 137.27600 1.000 78.55351  ? 214 PHE B CZ   1 
ATOM   4110 N N    . ARG B 1 215 ? 118.41400 124.18200 140.71600 1.000 86.06722  ? 215 ARG B N    1 
ATOM   4111 C CA   . ARG B 1 215 ? 119.01400 124.65700 141.95600 1.000 85.63475  ? 215 ARG B CA   1 
ATOM   4112 C C    . ARG B 1 215 ? 118.64200 123.82500 143.17900 1.000 84.42061  ? 215 ARG B C    1 
ATOM   4113 O O    . ARG B 1 215 ? 118.99100 124.20900 144.29900 1.000 85.01813  ? 215 ARG B O    1 
ATOM   4114 C CB   . ARG B 1 215 ? 118.65300 126.12500 142.18600 1.000 84.89208  ? 215 ARG B CB   1 
ATOM   4115 C CG   . ARG B 1 215 ? 119.38000 127.05100 141.23700 1.000 84.16485  ? 215 ARG B CG   1 
ATOM   4116 C CD   . ARG B 1 215 ? 120.69200 127.48900 141.86400 1.000 85.10511  ? 215 ARG B CD   1 
ATOM   4117 N NE   . ARG B 1 215 ? 121.82400 126.72100 141.35900 1.000 85.99982  ? 215 ARG B NE   1 
ATOM   4118 C CZ   . ARG B 1 215 ? 122.64300 127.12600 140.40000 1.000 85.34655  ? 215 ARG B CZ   1 
ATOM   4119 N NH1  . ARG B 1 215 ? 122.48700 128.29800 139.80900 1.000 84.55581  ? 215 ARG B NH1  1 
ATOM   4120 N NH2  . ARG B 1 215 ? 123.64700 126.33800 140.02800 1.000 85.08063  ? 215 ARG B NH2  1 
ATOM   4121 N N    . THR B 1 216 ? 117.95000 122.70800 143.00000 1.000 79.37666  ? 216 THR B N    1 
ATOM   4122 C CA   . THR B 1 216 ? 117.64800 121.82800 144.12000 1.000 79.28750  ? 216 THR B CA   1 
ATOM   4123 C C    . THR B 1 216 ? 118.78900 120.81900 144.27300 1.000 81.64241  ? 216 THR B C    1 
ATOM   4124 O O    . THR B 1 216 ? 119.87800 121.00900 143.72600 1.000 81.17346  ? 216 THR B O    1 
ATOM   4125 C CB   . THR B 1 216 ? 116.28700 121.15700 143.91300 1.000 79.80652  ? 216 THR B CB   1 
ATOM   4126 O OG1  . THR B 1 216 ? 115.92200 120.44200 145.09900 1.000 80.80432  ? 216 THR B OG1  1 
ATOM   4127 C CG2  . THR B 1 216 ? 116.34800 120.18400 142.74800 1.000 80.29194  ? 216 THR B CG2  1 
ATOM   4128 N N    . GLY B 1 217 ? 118.55700 119.74000 145.01600 1.000 78.94409  ? 217 GLY B N    1 
ATOM   4129 C CA   . GLY B 1 217 ? 119.56200 118.70600 145.16500 1.000 77.59521  ? 217 GLY B CA   1 
ATOM   4130 C C    . GLY B 1 217 ? 119.11300 117.37900 144.59100 1.000 77.59355  ? 217 GLY B C    1 
ATOM   4131 O O    . GLY B 1 217 ? 119.93000 116.59200 144.10500 1.000 79.16212  ? 217 GLY B O    1 
ATOM   4132 N N    . GLN B 1 218 ? 117.80500 117.12100 144.64700 1.000 74.69271  ? 218 GLN B N    1 
ATOM   4133 C CA   . GLN B 1 218 ? 117.25200 115.91200 144.04900 1.000 76.81123  ? 218 GLN B CA   1 
ATOM   4134 C C    . GLN B 1 218 ? 117.42700 115.88600 142.53500 1.000 76.48047  ? 218 GLN B C    1 
ATOM   4135 O O    . GLN B 1 218 ? 117.30000 114.81900 141.92400 1.000 76.57640  ? 218 GLN B O    1 
ATOM   4136 C CB   . GLN B 1 218 ? 115.77300 115.78900 144.42500 1.000 75.54991  ? 218 GLN B CB   1 
ATOM   4137 C CG   . GLN B 1 218 ? 115.02200 114.68000 143.71400 1.000 76.75159  ? 218 GLN B CG   1 
ATOM   4138 C CD   . GLN B 1 218 ? 114.14200 115.20500 142.59700 1.000 78.06309  ? 218 GLN B CD   1 
ATOM   4139 O OE1  . GLN B 1 218 ? 114.49300 116.16800 141.91500 1.000 77.25666  ? 218 GLN B OE1  1 
ATOM   4140 N NE2  . GLN B 1 218 ? 112.98700 114.57800 142.41000 1.000 77.45613  ? 218 GLN B NE2  1 
ATOM   4141 N N    . PHE B 1 219 ? 117.71300 117.03600 141.92200 1.000 67.88913  ? 219 PHE B N    1 
ATOM   4142 C CA   . PHE B 1 219 ? 117.85000 117.10700 140.47000 1.000 69.03648  ? 219 PHE B CA   1 
ATOM   4143 C C    . PHE B 1 219 ? 118.97700 116.20900 139.96600 1.000 70.14632  ? 219 PHE B C    1 
ATOM   4144 O O    . PHE B 1 219 ? 118.77800 115.38600 139.06100 1.000 71.42063  ? 219 PHE B O    1 
ATOM   4145 C CB   . PHE B 1 219 ? 118.08100 118.56100 140.05400 1.000 66.85997  ? 219 PHE B CB   1 
ATOM   4146 C CG   . PHE B 1 219 ? 118.57000 118.72700 138.64400 1.000 68.30925  ? 219 PHE B CG   1 
ATOM   4147 C CD1  . PHE B 1 219 ? 117.73100 118.48100 137.57100 1.000 67.31476  ? 219 PHE B CD1  1 
ATOM   4148 C CD2  . PHE B 1 219 ? 119.86500 119.14700 138.39300 1.000 66.92761  ? 219 PHE B CD2  1 
ATOM   4149 C CE1  . PHE B 1 219 ? 118.17900 118.63900 136.27400 1.000 68.04331  ? 219 PHE B CE1  1 
ATOM   4150 C CE2  . PHE B 1 219 ? 120.31700 119.30800 137.09900 1.000 66.11965  ? 219 PHE B CE2  1 
ATOM   4151 C CZ   . PHE B 1 219 ? 119.47300 119.05300 136.03800 1.000 66.60030  ? 219 PHE B CZ   1 
ATOM   4152 N N    . ILE B 1 220 ? 120.17300 116.35400 140.54300 1.000 65.00086  ? 220 ILE B N    1 
ATOM   4153 C CA   . ILE B 1 220 ? 121.33400 115.61700 140.05100 1.000 63.73841  ? 220 ILE B CA   1 
ATOM   4154 C C    . ILE B 1 220 ? 121.13200 114.11600 140.20300 1.000 63.71955  ? 220 ILE B C    1 
ATOM   4155 O O    . ILE B 1 220 ? 121.52200 113.33300 139.33000 1.000 67.46717  ? 220 ILE B O    1 
ATOM   4156 C CB   . ILE B 1 220 ? 122.60800 116.08900 140.77500 1.000 64.49380  ? 220 ILE B CB   1 
ATOM   4157 C CG1  . ILE B 1 220 ? 122.92100 117.54100 140.41400 1.000 65.91074  ? 220 ILE B CG1  1 
ATOM   4158 C CG2  . ILE B 1 220 ? 123.78000 115.18300 140.43600 1.000 65.17942  ? 220 ILE B CG2  1 
ATOM   4159 C CD1  . ILE B 1 220 ? 123.99600 118.16500 141.27700 1.000 66.01685  ? 220 ILE B CD1  1 
ATOM   4160 N N    . GLU B 1 221 ? 120.51800 113.68900 141.30600 1.000 61.91136  ? 221 GLU B N    1 
ATOM   4161 C CA   . GLU B 1 221 ? 120.30300 112.26200 141.53100 1.000 62.29814  ? 221 GLU B CA   1 
ATOM   4162 C C    . GLU B 1 221 ? 119.41700 111.66300 140.44400 1.000 64.56690  ? 221 GLU B C    1 
ATOM   4163 O O    . GLU B 1 221 ? 119.74500 110.62300 139.85000 1.000 67.61556  ? 221 GLU B O    1 
ATOM   4164 C CB   . GLU B 1 221 ? 119.69500 112.04800 142.91800 1.000 64.51026  ? 221 GLU B CB   1 
ATOM   4165 C CG   . GLU B 1 221 ? 120.04900 110.71900 143.56300 1.000 66.34015  ? 221 GLU B CG   1 
ATOM   4166 C CD   . GLU B 1 221 ? 118.91600 110.15900 144.39900 1.000 67.49071  ? 221 GLU B CD   1 
ATOM   4167 O OE1  . GLU B 1 221 ? 117.96300 110.91200 144.69000 1.000 66.26148  ? 221 GLU B OE1  1 
ATOM   4168 O OE2  . GLU B 1 221 ? 118.98100 108.96900 144.77000 1.000 66.48323  ? 221 GLU B OE2  1 
ATOM   4169 N N    . VAL B 1 222 ? 118.28300 112.31300 140.16900 1.000 54.67001  ? 222 VAL B N    1 
ATOM   4170 C CA   . VAL B 1 222 ? 117.36400 111.81300 139.15300 1.000 56.22746  ? 222 VAL B CA   1 
ATOM   4171 C C    . VAL B 1 222 ? 118.02700 111.83300 137.78300 1.000 55.88931  ? 222 VAL B C    1 
ATOM   4172 O O    . VAL B 1 222 ? 117.88100 110.89200 136.99100 1.000 59.60087  ? 222 VAL B O    1 
ATOM   4173 C CB   . VAL B 1 222 ? 116.06300 112.63700 139.16400 1.000 57.02959  ? 222 VAL B CB   1 
ATOM   4174 C CG1  . VAL B 1 222 ? 115.04200 112.03700 138.21300 1.000 57.85253  ? 222 VAL B CG1  1 
ATOM   4175 C CG2  . VAL B 1 222 ? 115.50600 112.72800 140.57600 1.000 55.62999  ? 222 VAL B CG2  1 
ATOM   4176 N N    . ALA B 1 223 ? 118.79000 112.89100 137.49100 1.000 48.25361  ? 223 ALA B N    1 
ATOM   4177 C CA   . ALA B 1 223 ? 119.45800 112.96200 136.19700 1.000 52.16866  ? 223 ALA B CA   1 
ATOM   4178 C C    . ALA B 1 223 ? 120.45300 111.82000 136.04100 1.000 56.26031  ? 223 ALA B C    1 
ATOM   4179 O O    . ALA B 1 223 ? 120.53100 111.19100 134.97600 1.000 57.81378  ? 223 ALA B O    1 
ATOM   4180 C CB   . ALA B 1 223 ? 120.15100 114.31400 136.03600 1.000 47.54855  ? 223 ALA B CB   1 
ATOM   4181 N N    . ILE B 1 224 ? 121.20200 111.51700 137.10200 1.000 50.79562  ? 224 ILE B N    1 
ATOM   4182 C CA   . ILE B 1 224 ? 122.21000 110.46800 137.02300 1.000 48.57873  ? 224 ILE B CA   1 
ATOM   4183 C C    . ILE B 1 224 ? 121.54500 109.11800 136.80500 1.000 52.43092  ? 224 ILE B C    1 
ATOM   4184 O O    . ILE B 1 224 ? 121.98300 108.32000 135.96800 1.000 56.20984  ? 224 ILE B O    1 
ATOM   4185 C CB   . ILE B 1 224 ? 123.09400 110.46800 138.28300 1.000 48.84839  ? 224 ILE B CB   1 
ATOM   4186 C CG1  . ILE B 1 224 ? 123.75300 111.83400 138.47700 1.000 50.76987  ? 224 ILE B CG1  1 
ATOM   4187 C CG2  . ILE B 1 224 ? 124.14600 109.37500 138.19700 1.000 52.62204  ? 224 ILE B CG2  1 
ATOM   4188 C CD1  . ILE B 1 224 ? 124.62200 112.26300 137.31500 1.000 50.56392  ? 224 ILE B CD1  1 
ATOM   4189 N N    . SER B 1 225 ? 120.48000 108.83400 137.56000 1.000 43.90931  ? 225 SER B N    1 
ATOM   4190 C CA   . SER B 1 225 ? 119.84600 107.52600 137.42600 1.000 47.15083  ? 225 SER B CA   1 
ATOM   4191 C C    . SER B 1 225 ? 119.20300 107.36200 136.05200 1.000 50.37827  ? 225 SER B C    1 
ATOM   4192 O O    . SER B 1 225 ? 119.26300 106.27600 135.44900 1.000 52.21352  ? 225 SER B O    1 
ATOM   4193 C CB   . SER B 1 225 ? 118.81000 107.33300 138.53200 1.000 44.65764  ? 225 SER B CB   1 
ATOM   4194 O OG   . SER B 1 225 ? 119.42700 107.29700 139.80600 1.000 47.57890  ? 225 SER B OG   1 
ATOM   4195 N N    . ARG B 1 226 ? 118.63400 108.44500 135.51200 1.000 43.70377  ? 226 ARG B N    1 
ATOM   4196 C CA   . ARG B 1 226 ? 118.03500 108.36900 134.18500 1.000 43.17683  ? 226 ARG B CA   1 
ATOM   4197 C C    . ARG B 1 226 ? 119.09500 108.14700 133.11300 1.000 40.53877  ? 226 ARG B C    1 
ATOM   4198 O O    . ARG B 1 226 ? 118.90800 107.32300 132.20600 1.000 41.53842  ? 226 ARG B O    1 
ATOM   4199 C CB   . ARG B 1 226 ? 117.23000 109.64100 133.91500 1.000 43.21073  ? 226 ARG B CB   1 
ATOM   4200 C CG   . ARG B 1 226 ? 115.92800 109.70500 134.70600 1.000 39.37225  ? 226 ARG B CG   1 
ATOM   4201 C CD   . ARG B 1 226 ? 115.26400 111.07000 134.62400 1.000 39.59728  ? 226 ARG B CD   1 
ATOM   4202 N NE   . ARG B 1 226 ? 113.87200 111.01900 135.05600 1.000 44.55067  ? 226 ARG B NE   1 
ATOM   4203 C CZ   . ARG B 1 226 ? 113.07500 112.07500 135.15400 1.000 45.15430  ? 226 ARG B CZ   1 
ATOM   4204 N NH1  . ARG B 1 226 ? 113.49900 113.29200 134.85700 1.000 43.21579  ? 226 ARG B NH1  1 
ATOM   4205 N NH2  . ARG B 1 226 ? 111.82100 111.90700 135.56400 1.000 40.99005  ? 226 ARG B NH2  1 
ATOM   4206 N N    . PHE B 1 227 ? 120.22700 108.85000 133.21100 1.000 37.90899  ? 227 PHE B N    1 
ATOM   4207 C CA   . PHE B 1 227 ? 121.29500 108.62600 132.24400 1.000 42.78551  ? 227 PHE B CA   1 
ATOM   4208 C C    . PHE B 1 227 ? 121.86900 107.22100 132.36000 1.000 45.35633  ? 227 PHE B C    1 
ATOM   4209 O O    . PHE B 1 227 ? 122.24700 106.61900 131.34600 1.000 47.69194  ? 227 PHE B O    1 
ATOM   4210 C CB   . PHE B 1 227 ? 122.39900 109.66500 132.42600 1.000 41.87598  ? 227 PHE B CB   1 
ATOM   4211 C CG   . PHE B 1 227 ? 123.49400 109.56900 131.40500 1.000 44.74209  ? 227 PHE B CG   1 
ATOM   4212 C CD1  . PHE B 1 227 ? 123.30200 110.04300 130.11800 1.000 44.04279  ? 227 PHE B CD1  1 
ATOM   4213 C CD2  . PHE B 1 227 ? 124.71300 109.00000 131.72900 1.000 45.78541  ? 227 PHE B CD2  1 
ATOM   4214 C CE1  . PHE B 1 227 ? 124.30800 109.95500 129.17600 1.000 46.22934  ? 227 PHE B CE1  1 
ATOM   4215 C CE2  . PHE B 1 227 ? 125.72300 108.90900 130.79100 1.000 43.82134  ? 227 PHE B CE2  1 
ATOM   4216 C CZ   . PHE B 1 227 ? 125.52000 109.38700 129.51400 1.000 44.00867  ? 227 PHE B CZ   1 
ATOM   4217 N N    . LEU B 1 228 ? 121.92000 106.67100 133.57400 1.000 39.45159  ? 228 LEU B N    1 
ATOM   4218 C CA   . LEU B 1 228 ? 122.40800 105.30700 133.74500 1.000 40.27154  ? 228 LEU B CA   1 
ATOM   4219 C C    . LEU B 1 228 ? 121.50400 104.31500 133.02600 1.000 42.02993  ? 228 LEU B C    1 
ATOM   4220 O O    . LEU B 1 228 ? 121.97900 103.43500 132.29200 1.000 46.72939  ? 228 LEU B O    1 
ATOM   4221 C CB   . LEU B 1 228 ? 122.50600 104.96900 135.23300 1.000 41.76152  ? 228 LEU B CB   1 
ATOM   4222 C CG   . LEU B 1 228 ? 123.72800 105.50400 135.98100 1.000 43.96456  ? 228 LEU B CG   1 
ATOM   4223 C CD1  . LEU B 1 228 ? 123.53800 105.37100 137.48400 1.000 41.17710  ? 228 LEU B CD1  1 
ATOM   4224 C CD2  . LEU B 1 228 ? 124.99000 104.78600 135.53300 1.000 40.53715  ? 228 LEU B CD2  1 
ATOM   4225 N N    . LEU B 1 229 ? 120.19000 104.44700 133.21800 1.000 37.29060  ? 229 LEU B N    1 
ATOM   4226 C CA   . LEU B 1 229 ? 119.27600 103.52800 132.54600 1.000 39.59091  ? 229 LEU B CA   1 
ATOM   4227 C C    . LEU B 1 229 ? 119.32600 103.69900 131.02900 1.000 39.58938  ? 229 LEU B C    1 
ATOM   4228 O O    . LEU B 1 229 ? 119.24100 102.71400 130.28000 1.000 45.21016  ? 229 LEU B O    1 
ATOM   4229 C CB   . LEU B 1 229 ? 117.85500 103.72000 133.07100 1.000 38.17956  ? 229 LEU B CB   1 
ATOM   4230 C CG   . LEU B 1 229 ? 117.46600 102.70700 134.15000 1.000 42.29665  ? 229 LEU B CG   1 
ATOM   4231 C CD1  . LEU B 1 229 ? 118.23800 102.96700 135.43400 1.000 40.21762  ? 229 LEU B CD1  1 
ATOM   4232 C CD2  . LEU B 1 229 ? 115.97500 102.71800 134.40700 1.000 39.71345  ? 229 LEU B CD2  1 
ATOM   4233 N N    . ILE B 1 230 ? 119.51000 104.93400 130.55400 1.000 28.77085  ? 230 ILE B N    1 
ATOM   4234 C CA   . ILE B 1 230 ? 119.58200 105.14500 129.11000 1.000 26.48192  ? 230 ILE B CA   1 
ATOM   4235 C C    . ILE B 1 230 ? 120.83700 104.50000 128.53300 1.000 30.74174  ? 230 ILE B C    1 
ATOM   4236 O O    . ILE B 1 230 ? 120.79900 103.87800 127.46000 1.000 39.30955  ? 230 ILE B O    1 
ATOM   4237 C CB   . ILE B 1 230 ? 119.52100 106.64900 128.78800 1.000 29.02795  ? 230 ILE B CB   1 
ATOM   4238 C CG1  . ILE B 1 230 ? 118.15700 107.22600 129.16800 1.000 33.92565  ? 230 ILE B CG1  1 
ATOM   4239 C CG2  . ILE B 1 230 ? 119.82300 106.89600 127.32100 1.000 27.26491  ? 230 ILE B CG2  1 
ATOM   4240 C CD1  . ILE B 1 230 ? 118.10100 108.73500 129.13100 1.000 33.41982  ? 230 ILE B CD1  1 
ATOM   4241 N N    . ALA B 1 231 ? 121.96000 104.59700 129.24900 1.000 32.19402  ? 231 ALA B N    1 
ATOM   4242 C CA   . ALA B 1 231 ? 123.17800 103.96700 128.75600 1.000 34.45513  ? 231 ALA B CA   1 
ATOM   4243 C C    . ALA B 1 231 ? 123.06900 102.45000 128.77900 1.000 32.90562  ? 231 ALA B C    1 
ATOM   4244 O O    . ALA B 1 231 ? 123.55900 101.77900 127.86000 1.000 30.26072  ? 231 ALA B O    1 
ATOM   4245 C CB   . ALA B 1 231 ? 124.38100 104.42600 129.58000 1.000 33.16162  ? 231 ALA B CB   1 
ATOM   4246 N N    . LEU B 1 232 ? 122.38300 101.89500 129.78100 1.000 24.47915  ? 232 LEU B N    1 
ATOM   4247 C CA   . LEU B 1 232 ? 122.20800 100.44600 129.81100 1.000 26.85723  ? 232 LEU B CA   1 
ATOM   4248 C C    . LEU B 1 232 ? 121.37000 99.97900  128.62700 1.000 30.60827  ? 232 LEU B C    1 
ATOM   4249 O O    . LEU B 1 232 ? 121.71100 98.99000  127.95900 1.000 35.19002  ? 232 LEU B O    1 
ATOM   4250 C CB   . LEU B 1 232 ? 121.56000 100.02700 131.13000 1.000 27.36556  ? 232 LEU B CB   1 
ATOM   4251 C CG   . LEU B 1 232 ? 121.07300 98.58100  131.24100 1.000 32.58745  ? 232 LEU B CG   1 
ATOM   4252 C CD1  . LEU B 1 232 ? 121.32600 98.02800  132.63400 1.000 33.77843  ? 232 LEU B CD1  1 
ATOM   4253 C CD2  . LEU B 1 232 ? 119.59500 98.48800  130.89100 1.000 27.67551  ? 232 LEU B CD2  1 
ATOM   4254 N N    . GLY B 1 233 ? 120.28800 100.70300 128.32900 1.000 25.11950  ? 233 GLY B N    1 
ATOM   4255 C CA   . GLY B 1 233 ? 119.43700 100.30000 127.22400 1.000 21.55188  ? 233 GLY B CA   1 
ATOM   4256 C C    . GLY B 1 233 ? 120.14100 100.40900 125.88600 1.000 25.70995  ? 233 GLY B C    1 
ATOM   4257 O O    . GLY B 1 233 ? 120.00600 99.52800  125.02700 1.000 28.92229  ? 233 GLY B O    1 
ATOM   4258 N N    . ALA B 1 234 ? 120.94200 101.46300 125.70300 1.000 21.17741  ? 234 ALA B N    1 
ATOM   4259 C CA   . ALA B 1 234 ? 121.65300 101.60600 124.43700 1.000 20.15752  ? 234 ALA B CA   1 
ATOM   4260 C C    . ALA B 1 234 ? 122.73100 100.54000 124.28200 1.000 25.53243  ? 234 ALA B C    1 
ATOM   4261 O O    . ALA B 1 234 ? 122.92800 100.00700 123.18300 1.000 25.20051  ? 234 ALA B O    1 
ATOM   4262 C CB   . ALA B 1 234 ? 122.26000 103.00400 124.32900 1.000 20.94298  ? 234 ALA B CB   1 
ATOM   4263 N N    . GLY B 1 235 ? 123.41700 100.18600 125.37300 1.000 27.61626  ? 235 GLY B N    1 
ATOM   4264 C CA   . GLY B 1 235 ? 124.41800 99.13700  125.27800 1.000 17.88768  ? 235 GLY B CA   1 
ATOM   4265 C C    . GLY B 1 235 ? 123.81100 97.79000  124.93500 1.000 21.98135  ? 235 GLY B C    1 
ATOM   4266 O O    . GLY B 1 235 ? 124.34000 97.05100  124.09400 1.000 24.87758  ? 235 GLY B O    1 
ATOM   4267 N N    . VAL B 1 236 ? 122.66600 97.47100  125.54500 1.000 24.08791  ? 236 VAL B N    1 
ATOM   4268 C CA   . VAL B 1 236 ? 122.00900 96.20300  125.24200 1.000 22.80499  ? 236 VAL B CA   1 
ATOM   4269 C C    . VAL B 1 236 ? 121.56200 96.17200  123.78600 1.000 25.43776  ? 236 VAL B C    1 
ATOM   4270 O O    . VAL B 1 236 ? 121.77900 95.18300  123.07200 1.000 21.02703  ? 236 VAL B O    1 
ATOM   4271 C CB   . VAL B 1 236 ? 120.82800 95.96400  126.19900 1.000 18.86729  ? 236 VAL B CB   1 
ATOM   4272 C CG1  . VAL B 1 236 ? 120.24700 94.57800  125.98300 1.000 19.43544  ? 236 VAL B CG1  1 
ATOM   4273 C CG2  . VAL B 1 236 ? 121.27200 96.13600  127.63800 1.000 23.87002  ? 236 VAL B CG2  1 
ATOM   4274 N N    . SER B 1 237 ? 120.91100 97.24600  123.32800 1.000 22.22894  ? 237 SER B N    1 
ATOM   4275 C CA   . SER B 1 237 ? 120.46900 97.28700  121.93800 1.000 19.82296  ? 237 SER B CA   1 
ATOM   4276 C C    . SER B 1 237 ? 121.63700 97.12900  120.97200 1.000 20.52264  ? 237 SER B C    1 
ATOM   4277 O O    . SER B 1 237 ? 121.55700 96.35400  120.00900 1.000 16.25510  ? 237 SER B O    1 
ATOM   4278 C CB   . SER B 1 237 ? 119.72300 98.59200  121.66200 1.000 19.85923  ? 237 SER B CB   1 
ATOM   4279 O OG   . SER B 1 237 ? 118.59600 98.72200  122.50700 1.000 32.78432  ? 237 SER B OG   1 
ATOM   4280 N N    . LEU B 1 238 ? 122.75200 97.81700  121.23400 1.000 28.19260  ? 238 LEU B N    1 
ATOM   4281 C CA   . LEU B 1 238 ? 123.86600 97.75300  120.29600 1.000 23.53966  ? 238 LEU B CA   1 
ATOM   4282 C C    . LEU B 1 238 ? 124.53200 96.38400  120.28500 1.000 25.94252  ? 238 LEU B C    1 
ATOM   4283 O O    . LEU B 1 238 ? 124.92600 95.90300  119.21400 1.000 28.81209  ? 238 LEU B O    1 
ATOM   4284 C CB   . LEU B 1 238 ? 124.89000 98.83900  120.62600 1.000 25.82884  ? 238 LEU B CB   1 
ATOM   4285 C CG   . LEU B 1 238 ? 126.02300 99.02300  119.61500 1.000 30.16237  ? 238 LEU B CG   1 
ATOM   4286 C CD1  . LEU B 1 238 ? 125.59700 99.96500  118.50300 1.000 29.30802  ? 238 LEU B CD1  1 
ATOM   4287 C CD2  . LEU B 1 238 ? 127.28200 99.53100  120.29800 1.000 26.96059  ? 238 LEU B CD2  1 
ATOM   4288 N N    . GLY B 1 239 ? 124.59400 95.69800  121.42800 1.000 23.56134  ? 239 GLY B N    1 
ATOM   4289 C CA   . GLY B 1 239 ? 125.18800 94.37000  121.41600 1.000 17.65902  ? 239 GLY B CA   1 
ATOM   4290 C C    . GLY B 1 239 ? 124.29100 93.33000  120.77200 1.000 20.59870  ? 239 GLY B C    1 
ATOM   4291 O O    . GLY B 1 239 ? 124.75800 92.50100  119.97600 1.000 23.04170  ? 239 GLY B O    1 
ATOM   4292 N N    . VAL B 1 240 ? 122.97800 93.42000  121.02000 1.000 23.64398  ? 240 VAL B N    1 
ATOM   4293 C CA   . VAL B 1 240 ? 122.04100 92.47500  120.41400 1.000 18.93792  ? 240 VAL B CA   1 
ATOM   4294 C C    . VAL B 1 240 ? 121.75500 92.80800  118.96200 1.000 24.93691  ? 240 VAL B C    1 
ATOM   4295 O O    . VAL B 1 240 ? 121.08500 92.02700  118.27500 1.000 27.90902  ? 240 VAL B O    1 
ATOM   4296 C CB   . VAL B 1 240 ? 120.71700 92.41800  121.19900 1.000 21.31651  ? 240 VAL B CB   1 
ATOM   4297 C CG1  . VAL B 1 240 ? 119.79600 91.35800  120.61700 1.000 18.34623  ? 240 VAL B CG1  1 
ATOM   4298 C CG2  . VAL B 1 240 ? 120.98400 92.13900  122.66600 1.000 22.97924  ? 240 VAL B CG2  1 
ATOM   4299 N N    . ASN B 1 241 ? 122.25900 93.93600  118.47100 1.000 17.73754  ? 241 ASN B N    1 
ATOM   4300 C CA   . ASN B 1 241 ? 122.12700 94.26800  117.06200 1.000 10.94908  ? 241 ASN B CA   1 
ATOM   4301 C C    . ASN B 1 241 ? 123.39200 93.96500  116.28100 1.000 23.73918  ? 241 ASN B C    1 
ATOM   4302 O O    . ASN B 1 241 ? 123.30700 93.58900  115.10800 1.000 23.71203  ? 241 ASN B O    1 
ATOM   4303 C CB   . ASN B 1 241 ? 121.77200 95.74800  116.88400 1.000 12.90819  ? 241 ASN B CB   1 
ATOM   4304 C CG   . ASN B 1 241 ? 120.98400 96.00700  115.61700 1.000 16.87939  ? 241 ASN B CG   1 
ATOM   4305 O OD1  . ASN B 1 241 ? 120.48800 95.08000  114.98200 1.000 25.94680  ? 241 ASN B OD1  1 
ATOM   4306 N ND2  . ASN B 1 241 ? 120.87400 97.27300  115.23700 1.000 15.92844  ? 241 ASN B ND2  1 
ATOM   4307 N N    . MET B 1 242 ? 124.56000 94.10300  116.90600 1.000 36.29898  ? 242 MET B N    1 
ATOM   4308 C CA   . MET B 1 242 ? 125.81100 93.87700  116.20200 1.000 22.70408  ? 242 MET B CA   1 
ATOM   4309 C C    . MET B 1 242 ? 126.30400 92.43900  116.27800 1.000 25.08046  ? 242 MET B C    1 
ATOM   4310 O O    . MET B 1 242 ? 127.05500 92.02000  115.39100 1.000 25.20744  ? 242 MET B O    1 
ATOM   4311 C CB   . MET B 1 242 ? 126.89800 94.80700  116.74500 1.000 22.21408  ? 242 MET B CB   1 
ATOM   4312 C CG   . MET B 1 242 ? 127.89100 95.26800  115.69600 1.000 30.88309  ? 242 MET B CG   1 
ATOM   4313 S SD   . MET B 1 242 ? 128.40300 96.98100  115.92000 1.000 49.13234  ? 242 MET B SD   1 
ATOM   4314 C CE   . MET B 1 242 ? 129.92300 97.00100  114.97500 1.000 27.45022  ? 242 MET B CE   1 
ATOM   4315 N N    . PHE B 1 243 ? 125.91200 91.66400  117.29300 1.000 23.34041  ? 243 PHE B N    1 
ATOM   4316 C CA   . PHE B 1 243 ? 126.48600 90.33300  117.44900 1.000 15.63929  ? 243 PHE B CA   1 
ATOM   4317 C C    . PHE B 1 243 ? 125.56700 89.18100  117.05700 1.000 16.46961  ? 243 PHE B C    1 
ATOM   4318 O O    . PHE B 1 243 ? 125.99500 88.02500  117.13600 1.000 21.93338  ? 243 PHE B O    1 
ATOM   4319 C CB   . PHE B 1 243 ? 126.97700 90.14400  118.88800 1.000 20.09901  ? 243 PHE B CB   1 
ATOM   4320 C CG   . PHE B 1 243 ? 128.12700 91.04000  119.24500 1.000 26.81262  ? 243 PHE B CG   1 
ATOM   4321 C CD1  . PHE B 1 243 ? 129.27300 91.05000  118.46800 1.000 19.05678  ? 243 PHE B CD1  1 
ATOM   4322 C CD2  . PHE B 1 243 ? 128.06000 91.87900  120.34300 1.000 29.79951  ? 243 PHE B CD2  1 
ATOM   4323 C CE1  . PHE B 1 243 ? 130.33100 91.87400  118.78200 1.000 19.06327  ? 243 PHE B CE1  1 
ATOM   4324 C CE2  . PHE B 1 243 ? 129.11700 92.70600  120.66100 1.000 25.33988  ? 243 PHE B CE2  1 
ATOM   4325 C CZ   . PHE B 1 243 ? 130.25400 92.70300  119.87900 1.000 21.12152  ? 243 PHE B CZ   1 
ATOM   4326 N N    . ILE B 1 244 ? 124.33200 89.44100  116.63600 1.000 19.16125  ? 244 ILE B N    1 
ATOM   4327 C CA   . ILE B 1 244 ? 123.42300 88.38100  116.20000 1.000 16.64017  ? 244 ILE B CA   1 
ATOM   4328 C C    . ILE B 1 244 ? 122.88800 88.70100  114.80700 1.000 20.42488  ? 244 ILE B C    1 
ATOM   4329 O O    . ILE B 1 244 ? 122.07000 89.61400  114.64600 1.000 30.24975  ? 244 ILE B O    1 
ATOM   4330 C CB   . ILE B 1 244 ? 122.26700 88.17000  117.18700 1.000 23.49818  ? 244 ILE B CB   1 
ATOM   4331 C CG1  . ILE B 1 244 ? 122.78700 87.55700  118.48900 1.000 17.86861  ? 244 ILE B CG1  1 
ATOM   4332 C CG2  . ILE B 1 244 ? 121.19600 87.28500  116.57400 1.000 19.22726  ? 244 ILE B CG2  1 
ATOM   4333 C CD1  . ILE B 1 244 ? 122.57100 88.42200  119.70500 1.000 19.55577  ? 244 ILE B CD1  1 
ATOM   4334 N N    . TYR B 1 245 ? 123.34300 87.94800  113.80800 1.000 16.18903  ? 245 TYR B N    1 
ATOM   4335 C CA   . TYR B 1 245 ? 122.89300 88.08600  112.42700 1.000 19.86109  ? 245 TYR B CA   1 
ATOM   4336 C C    . TYR B 1 245 ? 122.86000 89.53000  111.91800 1.000 25.41170  ? 245 TYR B C    1 
ATOM   4337 O O    . TYR B 1 245 ? 121.80000 90.03100  111.52700 1.000 24.55706  ? 245 TYR B O    1 
ATOM   4338 C CB   . TYR B 1 245 ? 121.53200 87.42800  112.25000 1.000 22.12151  ? 245 TYR B CB   1 
ATOM   4339 C CG   . TYR B 1 245 ? 121.57000 85.91800  112.32200 1.000 22.73778  ? 245 TYR B CG   1 
ATOM   4340 C CD1  . TYR B 1 245 ? 122.20100 85.17500  111.33500 1.000 23.54866  ? 245 TYR B CD1  1 
ATOM   4341 C CD2  . TYR B 1 245 ? 120.97600 85.23700  113.37400 1.000 23.02233  ? 245 TYR B CD2  1 
ATOM   4342 C CE1  . TYR B 1 245 ? 122.24200 83.79600  111.39400 1.000 25.74347  ? 245 TYR B CE1  1 
ATOM   4343 C CE2  . TYR B 1 245 ? 121.01100 83.85800  113.44300 1.000 22.61530  ? 245 TYR B CE2  1 
ATOM   4344 C CZ   . TYR B 1 245 ? 121.64500 83.14300  112.45000 1.000 30.06073  ? 245 TYR B CZ   1 
ATOM   4345 O OH   . TYR B 1 245 ? 121.68200 81.76900  112.51200 1.000 31.93026  ? 245 TYR B OH   1 
ATOM   4346 N N    . PRO B 1 246 ? 123.99700 90.22100  111.90700 1.000 16.55586  ? 246 PRO B N    1 
ATOM   4347 C CA   . PRO B 1 246 ? 124.00600 91.61600  111.44900 1.000 13.90938  ? 246 PRO B CA   1 
ATOM   4348 C C    . PRO B 1 246 ? 123.57200 91.74000  109.99400 1.000 16.24463  ? 246 PRO B C    1 
ATOM   4349 O O    . PRO B 1 246 ? 123.85800 90.87600  109.16400 1.000 20.58883  ? 246 PRO B O    1 
ATOM   4350 C CB   . PRO B 1 246 ? 125.46900 92.03500  111.63200 1.000 13.32294  ? 246 PRO B CB   1 
ATOM   4351 C CG   . PRO B 1 246 ? 126.23200 90.74900  111.66300 1.000 12.06178  ? 246 PRO B CG   1 
ATOM   4352 C CD   . PRO B 1 246 ? 125.33000 89.77900  112.34500 1.000 13.07315  ? 246 PRO B CD   1 
ATOM   4353 N N    . ILE B 1 247 ? 122.86800 92.83000  109.69300 1.000 13.12346  ? 247 ILE B N    1 
ATOM   4354 C CA   . ILE B 1 247 ? 122.48400 93.18900  108.33100 1.000 6.26800   ? 247 ILE B CA   1 
ATOM   4355 C C    . ILE B 1 247 ? 123.33900 94.36900  107.88800 1.000 8.36329   ? 247 ILE B C    1 
ATOM   4356 O O    . ILE B 1 247 ? 123.44800 95.36800  108.60800 1.000 11.87787  ? 247 ILE B O    1 
ATOM   4357 C CB   . ILE B 1 247 ? 120.98500 93.52200  108.23600 1.000 12.75060  ? 247 ILE B CB   1 
ATOM   4358 C CG1  . ILE B 1 247 ? 120.15900 92.23700  108.15400 1.000 16.42098  ? 247 ILE B CG1  1 
ATOM   4359 C CG2  . ILE B 1 247 ? 120.70700 94.40900  107.03500 1.000 7.91933   ? 247 ILE B CG2  1 
ATOM   4360 C CD1  . ILE B 1 247 ? 118.76800 92.36500  108.72700 1.000 15.72238  ? 247 ILE B CD1  1 
ATOM   4361 N N    . TRP B 1 248 ? 123.94800 94.25200  106.71000 1.000 16.96493  ? 248 TRP B N    1 
ATOM   4362 C CA   . TRP B 1 248 ? 124.84900 95.26600  106.17700 1.000 6.85244   ? 248 TRP B CA   1 
ATOM   4363 C C    . TRP B 1 248 ? 124.18600 96.00800  105.02200 1.000 7.77090   ? 248 TRP B C    1 
ATOM   4364 O O    . TRP B 1 248 ? 123.43300 95.41400  104.24600 1.000 18.61216  ? 248 TRP B O    1 
ATOM   4365 C CB   . TRP B 1 248 ? 126.15500 94.62400  105.70500 1.000 9.72648   ? 248 TRP B CB   1 
ATOM   4366 C CG   . TRP B 1 248 ? 126.77700 93.70100  106.71500 1.000 10.52092  ? 248 TRP B CG   1 
ATOM   4367 C CD1  . TRP B 1 248 ? 126.62300 92.34800  106.78700 1.000 9.05951   ? 248 TRP B CD1  1 
ATOM   4368 C CD2  . TRP B 1 248 ? 127.65100 94.06100  107.79200 1.000 17.49892  ? 248 TRP B CD2  1 
ATOM   4369 N NE1  . TRP B 1 248 ? 127.34500 91.84200  107.83800 1.000 10.96184  ? 248 TRP B NE1  1 
ATOM   4370 C CE2  . TRP B 1 248 ? 127.98500 92.87300  108.47200 1.000 14.35024  ? 248 TRP B CE2  1 
ATOM   4371 C CE3  . TRP B 1 248 ? 128.18500 95.27000  108.24700 1.000 14.63572  ? 248 TRP B CE3  1 
ATOM   4372 C CZ2  . TRP B 1 248 ? 128.82700 92.86000  109.58100 1.000 6.05238   ? 248 TRP B CZ2  1 
ATOM   4373 C CZ3  . TRP B 1 248 ? 129.01900 95.25400  109.34700 1.000 11.60049  ? 248 TRP B CZ3  1 
ATOM   4374 C CH2  . TRP B 1 248 ? 129.33300 94.05800  110.00100 1.000 8.74030   ? 248 TRP B CH2  1 
ATOM   4375 N N    . ALA B 1 249 ? 124.47100 97.30900  104.90800 1.000 14.91053  ? 249 ALA B N    1 
ATOM   4376 C CA   . ALA B 1 249 ? 123.90800 98.13100  103.83900 1.000 15.71130  ? 249 ALA B CA   1 
ATOM   4377 C C    . ALA B 1 249 ? 124.66400 98.01100  102.51900 1.000 19.86544  ? 249 ALA B C    1 
ATOM   4378 O O    . ALA B 1 249 ? 124.08300 98.27800  101.45200 1.000 27.10956  ? 249 ALA B O    1 
ATOM   4379 C CB   . ALA B 1 249 ? 123.87400 99.59700  104.27300 1.000 10.82439  ? 249 ALA B CB   1 
ATOM   4380 N N    . GLY B 1 250 ? 125.91600 97.55100  102.55100 1.000 15.59072  ? 250 GLY B N    1 
ATOM   4381 C CA   . GLY B 1 250 ? 126.65500 97.39600  101.31400 1.000 12.02587  ? 250 GLY B CA   1 
ATOM   4382 C C    . GLY B 1 250 ? 126.18600 96.20200  100.51600 1.000 16.42471  ? 250 GLY B C    1 
ATOM   4383 O O    . GLY B 1 250 ? 126.19400 96.23400  99.28100  1.000 33.80308  ? 250 GLY B O    1 
ATOM   4384 N N    . GLU B 1 251 ? 125.68000 95.17500  101.19800 1.000 12.66307  ? 251 GLU B N    1 
ATOM   4385 C CA   . GLU B 1 251 ? 125.11900 94.04700  100.47400 1.000 18.48906  ? 251 GLU B CA   1 
ATOM   4386 C C    . GLU B 1 251 ? 123.77100 94.40900  99.87500  1.000 18.20243  ? 251 GLU B C    1 
ATOM   4387 O O    . GLU B 1 251 ? 123.41600 93.88800  98.81200  1.000 29.52479  ? 251 GLU B O    1 
ATOM   4388 C CB   . GLU B 1 251 ? 124.97000 92.84900  101.41100 1.000 24.80394  ? 251 GLU B CB   1 
ATOM   4389 C CG   . GLU B 1 251 ? 126.28200 92.22800  101.84900 1.000 19.82932  ? 251 GLU B CG   1 
ATOM   4390 C CD   . GLU B 1 251 ? 126.15200 90.74700  102.14300 1.000 30.41290  ? 251 GLU B CD   1 
ATOM   4391 O OE1  . GLU B 1 251 ? 125.52600 90.03200  101.33300 1.000 28.66861  ? 251 GLU B OE1  1 
ATOM   4392 O OE2  . GLU B 1 251 ? 126.67400 90.29900  103.18500 1.000 33.01445  ? 251 GLU B OE2  1 
ATOM   4393 N N    . ASP B 1 252 ? 123.08300 95.39300  100.45800 1.000 14.08400  ? 252 ASP B N    1 
ATOM   4394 C CA   . ASP B 1 252 ? 121.81200 95.83400  99.90100  1.000 23.83269  ? 252 ASP B CA   1 
ATOM   4395 C C    . ASP B 1 252 ? 122.03700 96.69700  98.67100  1.000 23.01918  ? 252 ASP B C    1 
ATOM   4396 O O    . ASP B 1 252 ? 121.31300 96.56500  97.67800  1.000 30.32779  ? 252 ASP B O    1 
ATOM   4397 C CB   . ASP B 1 252 ? 121.01200 96.60200  100.95300 1.000 20.88143  ? 252 ASP B CB   1 
ATOM   4398 C CG   . ASP B 1 252 ? 120.80100 95.80400  102.22000 1.000 26.86917  ? 252 ASP B CG   1 
ATOM   4399 O OD1  . ASP B 1 252 ? 121.64400 94.93500  102.52100 1.000 28.25069  ? 252 ASP B OD1  1 
ATOM   4400 O OD2  . ASP B 1 252 ? 119.79300 96.04700  102.91600 1.000 31.90041  ? 252 ASP B OD2  1 
ATOM   4401 N N    . LEU B 1 253 ? 123.07500 97.53500  98.68900  1.000 12.31356  ? 253 LEU B N    1 
ATOM   4402 C CA   . LEU B 1 253 ? 123.40100 98.29400  97.48400  1.000 17.37795  ? 253 LEU B CA   1 
ATOM   4403 C C    . LEU B 1 253 ? 123.87500 97.36400  96.36800  1.000 14.67454  ? 253 LEU B C    1 
ATOM   4404 O O    . LEU B 1 253 ? 123.43700 97.48100  95.20700  1.000 14.38321  ? 253 LEU B O    1 
ATOM   4405 C CB   . LEU B 1 253 ? 124.46600 99.34100  97.81200  1.000 17.96237  ? 253 LEU B CB   1 
ATOM   4406 C CG   . LEU B 1 253 ? 124.77600 100.41700 96.77200  1.000 23.51261  ? 253 LEU B CG   1 
ATOM   4407 C CD1  . LEU B 1 253 ? 123.54600 101.25900 96.49700  1.000 13.44999  ? 253 LEU B CD1  1 
ATOM   4408 C CD2  . LEU B 1 253 ? 125.93300 101.28400 97.24000  1.000 9.43741   ? 253 LEU B CD2  1 
ATOM   4409 N N    . HIS B 1 254 ? 124.75100 96.41500  96.71700  1.000 12.04402  ? 254 HIS B N    1 
ATOM   4410 C CA   . HIS B 1 254 ? 125.24300 95.44200  95.75000  1.000 5.08884   ? 254 HIS B CA   1 
ATOM   4411 C C    . HIS B 1 254 ? 124.09400 94.67800  95.10300  1.000 14.77379  ? 254 HIS B C    1 
ATOM   4412 O O    . HIS B 1 254 ? 124.08700 94.47300  93.88500  1.000 17.82471  ? 254 HIS B O    1 
ATOM   4413 C CB   . HIS B 1 254 ? 126.21900 94.49200  96.44700  1.000 3.34833   ? 254 HIS B CB   1 
ATOM   4414 C CG   . HIS B 1 254 ? 126.87300 93.50400  95.53300  1.000 17.83927  ? 254 HIS B CG   1 
ATOM   4415 N ND1  . HIS B 1 254 ? 128.17600 93.64100  95.10500  1.000 18.01131  ? 254 HIS B ND1  1 
ATOM   4416 C CD2  . HIS B 1 254 ? 126.41600 92.35400  94.98300  1.000 22.64216  ? 254 HIS B CD2  1 
ATOM   4417 C CE1  . HIS B 1 254 ? 128.48900 92.62500  94.32100  1.000 19.05695  ? 254 HIS B CE1  1 
ATOM   4418 N NE2  . HIS B 1 254 ? 127.43900 91.83000  94.23100  1.000 20.47829  ? 254 HIS B NE2  1 
ATOM   4419 N N    . ASN B 1 255 ? 123.11100 94.24500  95.90000  1.000 11.49177  ? 255 ASN B N    1 
ATOM   4420 C CA   . ASN B 1 255 ? 122.01000 93.46600  95.34200  1.000 11.52080  ? 255 ASN B CA   1 
ATOM   4421 C C    . ASN B 1 255 ? 121.02800 94.33300  94.55800  1.000 17.96416  ? 255 ASN B C    1 
ATOM   4422 O O    . ASN B 1 255 ? 120.44300 93.87100  93.56400  1.000 22.64020  ? 255 ASN B O    1 
ATOM   4423 C CB   . ASN B 1 255 ? 121.28000 92.73800  96.47000  1.000 15.30945  ? 255 ASN B CB   1 
ATOM   4424 C CG   . ASN B 1 255 ? 122.00600 91.48900  96.92600  1.000 20.78249  ? 255 ASN B CG   1 
ATOM   4425 O OD1  . ASN B 1 255 ? 123.04100 91.11900  96.37400  1.000 24.88457  ? 255 ASN B OD1  1 
ATOM   4426 N ND2  . ASN B 1 255 ? 121.47000 90.83600  97.94800  1.000 20.94473  ? 255 ASN B ND2  1 
ATOM   4427 N N    . LEU B 1 256 ? 120.86500 95.59800  94.96100  1.000 12.24399  ? 256 LEU B N    1 
ATOM   4428 C CA   . LEU B 1 256 ? 119.95300 96.49100  94.25800  1.000 17.87085  ? 256 LEU B CA   1 
ATOM   4429 C C    . LEU B 1 256 ? 120.44100 96.78300  92.84600  1.000 14.06732  ? 256 LEU B C    1 
ATOM   4430 O O    . LEU B 1 256 ? 119.63500 96.87200  91.90700  1.000 20.53085  ? 256 LEU B O    1 
ATOM   4431 C CB   . LEU B 1 256 ? 119.78600 97.78500  95.05500  1.000 8.90225   ? 256 LEU B CB   1 
ATOM   4432 C CG   . LEU B 1 256 ? 118.90000 98.88500  94.47100  1.000 17.95336  ? 256 LEU B CG   1 
ATOM   4433 C CD1  . LEU B 1 256 ? 117.45600 98.42400  94.38600  1.000 15.43090  ? 256 LEU B CD1  1 
ATOM   4434 C CD2  . LEU B 1 256 ? 119.01200 100.15100 95.30100  1.000 16.99533  ? 256 LEU B CD2  1 
ATOM   4435 N N    . VAL B 1 257 ? 121.75800 96.91200  92.66500  1.000 6.13443   ? 257 VAL B N    1 
ATOM   4436 C CA   . VAL B 1 257 ? 122.26200 97.18500  91.31800  1.000 11.53556  ? 257 VAL B CA   1 
ATOM   4437 C C    . VAL B 1 257 ? 121.93800 96.02500  90.37300  1.000 15.57277  ? 257 VAL B C    1 
ATOM   4438 O O    . VAL B 1 257 ? 121.48100 96.23100  89.23600  1.000 21.59565  ? 257 VAL B O    1 
ATOM   4439 C CB   . VAL B 1 257 ? 123.77400 97.47500  91.36700  1.000 12.48836  ? 257 VAL B CB   1 
ATOM   4440 C CG1  . VAL B 1 257 ? 124.36600 97.47500  89.96700  1.000 10.62014  ? 257 VAL B CG1  1 
ATOM   4441 C CG2  . VAL B 1 257 ? 124.03700 98.80200  92.06000  1.000 5.62478   ? 257 VAL B CG2  1 
ATOM   4442 N N    . VAL B 1 258 ? 122.12300 94.79000  90.84300  1.000 9.45592   ? 258 VAL B N    1 
ATOM   4443 C CA   . VAL B 1 258 ? 121.83900 93.62200  90.01400  1.000 9.02294   ? 258 VAL B CA   1 
ATOM   4444 C C    . VAL B 1 258 ? 120.34800 93.52200  89.71300  1.000 12.89923  ? 258 VAL B C    1 
ATOM   4445 O O    . VAL B 1 258 ? 119.94200 93.17800  88.59000  1.000 19.61275  ? 258 VAL B O    1 
ATOM   4446 C CB   . VAL B 1 258 ? 122.36500 92.34900  90.70300  1.000 18.91056  ? 258 VAL B CB   1 
ATOM   4447 C CG1  . VAL B 1 258 ? 122.01800 91.11300  89.88700  1.000 16.55998  ? 258 VAL B CG1  1 
ATOM   4448 C CG2  . VAL B 1 258 ? 123.86500 92.44700  90.93300  1.000 10.57853  ? 258 VAL B CG2  1 
ATOM   4449 N N    . LYS B 1 259 ? 119.50500 93.83500  90.70100  1.000 15.79242  ? 259 LYS B N    1 
ATOM   4450 C CA   . LYS B 1 259 ? 118.06800 93.76500  90.46100  1.000 17.17548  ? 259 LYS B CA   1 
ATOM   4451 C C    . LYS B 1 259 ? 117.63400 94.78300  89.41100  1.000 17.99573  ? 259 LYS B C    1 
ATOM   4452 O O    . LYS B 1 259 ? 116.79600 94.48000  88.54900  1.000 24.76385  ? 259 LYS B O    1 
ATOM   4453 C CB   . LYS B 1 259 ? 117.31100 93.97700  91.77100  1.000 17.35332  ? 259 LYS B CB   1 
ATOM   4454 C CG   . LYS B 1 259 ? 115.93500 93.33700  91.80400  1.000 23.32680  ? 259 LYS B CG   1 
ATOM   4455 C CD   . LYS B 1 259 ? 115.05000 93.99200  92.84800  1.000 22.21382  ? 259 LYS B CD   1 
ATOM   4456 C CE   . LYS B 1 259 ? 114.77400 95.44600  92.50900  1.000 25.60402  ? 259 LYS B CE   1 
ATOM   4457 N NZ   . LYS B 1 259 ? 113.32800 95.77500  92.64400  1.000 29.06870  ? 259 LYS B NZ   1 
ATOM   4458 N N    . ASN B 1 260 ? 118.22000 95.98300  89.43800  1.000 13.60616  ? 260 ASN B N    1 
ATOM   4459 C CA   . ASN B 1 260 ? 117.85500 96.98100  88.43600  1.000 15.85158  ? 260 ASN B CA   1 
ATOM   4460 C C    . ASN B 1 260 ? 118.33000 96.56500  87.04800  1.000 15.35351  ? 260 ASN B C    1 
ATOM   4461 O O    . ASN B 1 260 ? 117.62700 96.78400  86.04500  1.000 7.64442   ? 260 ASN B O    1 
ATOM   4462 C CB   . ASN B 1 260 ? 118.43300 98.34300  88.81600  1.000 17.78512  ? 260 ASN B CB   1 
ATOM   4463 C CG   . ASN B 1 260 ? 117.70300 98.98300  89.98000  1.000 21.62772  ? 260 ASN B CG   1 
ATOM   4464 O OD1  . ASN B 1 260 ? 116.59000 98.58800  90.32200  1.000 28.65291  ? 260 ASN B OD1  1 
ATOM   4465 N ND2  . ASN B 1 260 ? 118.32900 99.97800  90.59500  1.000 16.49442  ? 260 ASN B ND2  1 
ATOM   4466 N N    . PHE B 1 261 ? 119.49800 95.91800  86.97500  1.000 19.68858  ? 261 PHE B N    1 
ATOM   4467 C CA   . PHE B 1 261 ? 119.98400 95.45100  85.68000  1.000 12.30750  ? 261 PHE B CA   1 
ATOM   4468 C C    . PHE B 1 261 ? 119.05400 94.39900  85.08900  1.000 17.47619  ? 261 PHE B C    1 
ATOM   4469 O O    . PHE B 1 261 ? 118.79800 94.39700  83.87900  1.000 19.62979  ? 261 PHE B O    1 
ATOM   4470 C CB   . PHE B 1 261 ? 121.40200 94.89800  85.80900  1.000 14.94769  ? 261 PHE B CB   1 
ATOM   4471 C CG   . PHE B 1 261 ? 122.46400 95.82800  85.29800  1.000 15.65339  ? 261 PHE B CG   1 
ATOM   4472 C CD1  . PHE B 1 261 ? 122.69700 95.95000  83.94000  1.000 20.11657  ? 261 PHE B CD1  1 
ATOM   4473 C CD2  . PHE B 1 261 ? 123.23200 96.57400  86.17400  1.000 16.85171  ? 261 PHE B CD2  1 
ATOM   4474 C CE1  . PHE B 1 261 ? 123.67300 96.80200  83.46400  1.000 18.86716  ? 261 PHE B CE1  1 
ATOM   4475 C CE2  . PHE B 1 261 ? 124.21000 97.42800  85.70400  1.000 21.82969  ? 261 PHE B CE2  1 
ATOM   4476 C CZ   . PHE B 1 261 ? 124.43000 97.54100  84.34700  1.000 22.28901  ? 261 PHE B CZ   1 
ATOM   4477 N N    . MET B 1 262 ? 118.54600 93.48800  85.92200  1.000 23.53147  ? 262 MET B N    1 
ATOM   4478 C CA   . MET B 1 262 ? 117.58400 92.50400  85.42100  1.000 19.50719  ? 262 MET B CA   1 
ATOM   4479 C C    . MET B 1 262 ? 116.27100 93.15800  84.98500  1.000 16.53475  ? 262 MET B C    1 
ATOM   4480 O O    . MET B 1 262 ? 115.70400 92.81000  83.93200  1.000 16.80143  ? 262 MET B O    1 
ATOM   4481 C CB   . MET B 1 262 ? 117.32000 91.44200  86.48800  1.000 14.18049  ? 262 MET B CB   1 
ATOM   4482 C CG   . MET B 1 262 ? 118.56700 90.74100  86.99600  1.000 16.13298  ? 262 MET B CG   1 
ATOM   4483 S SD   . MET B 1 262 ? 119.27800 89.63700  85.75900  1.000 35.52289  ? 262 MET B SD   1 
ATOM   4484 C CE   . MET B 1 262 ? 121.00500 90.09100  85.84400  1.000 23.08953  ? 262 MET B CE   1 
ATOM   4485 N N    . ASN B 1 263 ? 115.77700 94.11200  85.77800  1.000 21.57242  ? 263 ASN B N    1 
ATOM   4486 C CA   . ASN B 1 263 ? 114.47100 94.69900  85.49500  1.000 20.54571  ? 263 ASN B CA   1 
ATOM   4487 C C    . ASN B 1 263 ? 114.46600 95.49600  84.19500  1.000 19.12430  ? 263 ASN B C    1 
ATOM   4488 O O    . ASN B 1 263 ? 113.46800 95.48500  83.46300  1.000 16.03196  ? 263 ASN B O    1 
ATOM   4489 C CB   . ASN B 1 263 ? 114.03200 95.58600  86.65900  1.000 14.21686  ? 263 ASN B CB   1 
ATOM   4490 C CG   . ASN B 1 263 ? 113.58400 94.78700  87.86300  1.000 23.59241  ? 263 ASN B CG   1 
ATOM   4491 O OD1  . ASN B 1 263 ? 113.44100 93.56700  87.79500  1.000 27.12703  ? 263 ASN B OD1  1 
ATOM   4492 N ND2  . ASN B 1 263 ? 113.35700 95.47300  88.97500  1.000 26.23775  ? 263 ASN B ND2  1 
ATOM   4493 N N    . VAL B 1 264 ? 115.56400 96.18800  83.87800  1.000 20.04953  ? 264 VAL B N    1 
ATOM   4494 C CA   . VAL B 1 264 ? 115.55900 96.96500  82.63900  1.000 16.70319  ? 264 VAL B CA   1 
ATOM   4495 C C    . VAL B 1 264 ? 115.48800 96.05400  81.41300  1.000 14.27748  ? 264 VAL B C    1 
ATOM   4496 O O    . VAL B 1 264 ? 114.79200 96.36100  80.43300  1.000 18.12406  ? 264 VAL B O    1 
ATOM   4497 C CB   . VAL B 1 264 ? 116.78300 97.89500  82.58700  1.000 20.54961  ? 264 VAL B CB   1 
ATOM   4498 C CG1  . VAL B 1 264 ? 116.81100 98.66200  81.27600  1.000 19.51505  ? 264 VAL B CG1  1 
ATOM   4499 C CG2  . VAL B 1 264 ? 116.75700 98.85600  83.76100  1.000 18.32488  ? 264 VAL B CG2  1 
ATOM   4500 N N    . ALA B 1 265 ? 116.16400 94.90400  81.45700  1.000 12.15700  ? 265 ALA B N    1 
ATOM   4501 C CA   . ALA B 1 265 ? 116.08700 93.96500  80.34000  1.000 12.19666  ? 265 ALA B CA   1 
ATOM   4502 C C    . ALA B 1 265 ? 114.69000 93.37300  80.20900  1.000 17.15887  ? 265 ALA B C    1 
ATOM   4503 O O    . ALA B 1 265 ? 114.16600 93.22100  79.09100  1.000 14.40851  ? 265 ALA B O    1 
ATOM   4504 C CB   . ALA B 1 265 ? 117.12500 92.85800  80.51200  1.000 7.85377   ? 265 ALA B CB   1 
ATOM   4505 N N    . THR B 1 266 ? 114.05100 93.07500  81.34400  1.000 19.53888  ? 266 THR B N    1 
ATOM   4506 C CA   . THR B 1 266 ? 112.69200 92.54800  81.26600  1.000 22.47337  ? 266 THR B CA   1 
ATOM   4507 C C    . THR B 1 266 ? 111.74400 93.57800  80.66300  1.000 23.94386  ? 266 THR B C    1 
ATOM   4508 O O    . THR B 1 266 ? 110.89300 93.24000  79.82700  1.000 22.67952  ? 266 THR B O    1 
ATOM   4509 C CB   . THR B 1 266 ? 112.20800 92.11900  82.65100  1.000 21.92092  ? 266 THR B CB   1 
ATOM   4510 O OG1  . THR B 1 266 ? 112.98500 91.00500  83.10700  1.000 27.12833  ? 266 THR B OG1  1 
ATOM   4511 C CG2  . THR B 1 266 ? 110.74500 91.71300  82.59800  1.000 19.30239  ? 266 THR B CG2  1 
ATOM   4512 N N    . SER B 1 267 ? 111.90100 94.84900  81.04400  1.000 21.88704  ? 267 SER B N    1 
ATOM   4513 C CA   . SER B 1 267 ? 111.04200 95.89000  80.48800  1.000 12.38559  ? 267 SER B CA   1 
ATOM   4514 C C    . SER B 1 267 ? 111.26900 96.06800  78.99100  1.000 18.11330  ? 267 SER B C    1 
ATOM   4515 O O    . SER B 1 267 ? 110.31000 96.26000  78.23600  1.000 15.29588  ? 267 SER B O    1 
ATOM   4516 C CB   . SER B 1 267 ? 111.27000 97.21000  81.22000  1.000 20.63704  ? 267 SER B CB   1 
ATOM   4517 O OG   . SER B 1 267 ? 110.73300 97.16400  82.52600  1.000 29.87205  ? 267 SER B OG   1 
ATOM   4518 N N    . LEU B 1 268 ? 112.52400 96.00800  78.53800  1.000 18.36973  ? 268 LEU B N    1 
ATOM   4519 C CA   . LEU B 1 268 ? 112.77400 96.18300  77.10900  1.000 18.09251  ? 268 LEU B CA   1 
ATOM   4520 C C    . LEU B 1 268 ? 112.13600 95.06300  76.29300  1.000 25.14525  ? 268 LEU B C    1 
ATOM   4521 O O    . LEU B 1 268 ? 111.49200 95.31600  75.25700  1.000 21.76927  ? 268 LEU B O    1 
ATOM   4522 C CB   . LEU B 1 268 ? 114.27600 96.25000  76.83600  1.000 18.84268  ? 268 LEU B CB   1 
ATOM   4523 C CG   . LEU B 1 268 ? 114.65700 96.41400  75.36200  1.000 24.67909  ? 268 LEU B CG   1 
ATOM   4524 C CD1  . LEU B 1 268 ? 114.51800 97.86200  74.92000  1.000 21.84920  ? 268 LEU B CD1  1 
ATOM   4525 C CD2  . LEU B 1 268 ? 116.06300 95.90100  75.10300  1.000 19.23750  ? 268 LEU B CD2  1 
ATOM   4526 N N    . GLU B 1 269 ? 112.28300 93.81700  76.75300  1.000 37.81728  ? 269 GLU B N    1 
ATOM   4527 C CA   . GLU B 1 269 ? 111.66900 92.71800  76.01500  1.000 29.71187  ? 269 GLU B CA   1 
ATOM   4528 C C    . GLU B 1 269 ? 110.14800 92.82400  76.02900  1.000 31.41148  ? 269 GLU B C    1 
ATOM   4529 O O    . GLU B 1 269 ? 109.49300 92.61400  74.99600  1.000 28.22584  ? 269 GLU B O    1 
ATOM   4530 C CB   . GLU B 1 269 ? 112.12100 91.37700  76.59100  1.000 32.77038  ? 269 GLU B CB   1 
ATOM   4531 C CG   . GLU B 1 269 ? 112.15700 90.24900  75.57400  1.000 35.00614  ? 269 GLU B CG   1 
ATOM   4532 C CD   . GLU B 1 269 ? 113.32400 90.36200  74.61400  1.000 41.38920  ? 269 GLU B CD   1 
ATOM   4533 O OE1  . GLU B 1 269 ? 113.91700 91.45800  74.52300  1.000 37.94250  ? 269 GLU B OE1  1 
ATOM   4534 O OE2  . GLU B 1 269 ? 113.64700 89.35600  73.94800  1.000 37.51240  ? 269 GLU B OE2  1 
ATOM   4535 N N    . GLY B 1 270 ? 109.57100 93.19800  77.17400  1.000 33.83882  ? 270 GLY B N    1 
ATOM   4536 C CA   . GLY B 1 270 ? 108.12900 93.36200  77.23300  1.000 31.07941  ? 270 GLY B CA   1 
ATOM   4537 C C    . GLY B 1 270 ? 107.62500 94.46400  76.32300  1.000 32.44723  ? 270 GLY B C    1 
ATOM   4538 O O    . GLY B 1 270 ? 106.56500 94.33400  75.70900  1.000 34.95191  ? 270 GLY B O    1 
ATOM   4539 N N    . CYS B 1 271 ? 108.39900 95.54100  76.18200  1.000 33.31690  ? 271 CYS B N    1 
ATOM   4540 C CA   . CYS B 1 271 ? 107.96700 96.64100  75.32600  1.000 28.09330  ? 271 CYS B CA   1 
ATOM   4541 C C    . CYS B 1 271 ? 107.98200 96.23400  73.86000  1.000 27.06917  ? 271 CYS B C    1 
ATOM   4542 O O    . CYS B 1 271 ? 107.02000 96.49300  73.12500  1.000 23.22249  ? 271 CYS B O    1 
ATOM   4543 C CB   . CYS B 1 271 ? 108.85100 97.86900  75.54800  1.000 28.92559  ? 271 CYS B CB   1 
ATOM   4544 S SG   . CYS B 1 271 ? 108.53900 98.75200  77.08600  1.000 49.19843  ? 271 CYS B SG   1 
ATOM   4545 N N    . VAL B 1 272 ? 109.06300 95.59300  73.41000  1.000 37.70989  ? 272 VAL B N    1 
ATOM   4546 C CA   . VAL B 1 272 ? 109.10300 95.20400  72.00100  1.000 35.11040  ? 272 VAL B CA   1 
ATOM   4547 C C    . VAL B 1 272 ? 108.00800 94.18500  71.69700  1.000 36.98590  ? 272 VAL B C    1 
ATOM   4548 O O    . VAL B 1 272 ? 107.32100 94.27400  70.66500  1.000 33.20772  ? 272 VAL B O    1 
ATOM   4549 C CB   . VAL B 1 272 ? 110.49600 94.67300  71.61900  1.000 35.88068  ? 272 VAL B CB   1 
ATOM   4550 C CG1  . VAL B 1 272 ? 110.47300 94.11200  70.20800  1.000 32.58322  ? 272 VAL B CG1  1 
ATOM   4551 C CG2  . VAL B 1 272 ? 111.52900 95.77900  71.73000  1.000 36.89065  ? 272 VAL B CG2  1 
ATOM   4552 N N    . ASN B 1 273 ? 107.77600 93.24300  72.61800  1.000 40.41318  ? 273 ASN B N    1 
ATOM   4553 C CA   . ASN B 1 273 ? 106.73500 92.24900  72.37200  1.000 38.61847  ? 273 ASN B CA   1 
ATOM   4554 C C    . ASN B 1 273 ? 105.35300 92.88900  72.35000  1.000 38.63416  ? 273 ASN B C    1 
ATOM   4555 O O    . ASN B 1 273 ? 104.54200 92.58900  71.46700  1.000 37.11695  ? 273 ASN B O    1 
ATOM   4556 C CB   . ASN B 1 273 ? 106.79800 91.14000  73.42200  1.000 38.39606  ? 273 ASN B CB   1 
ATOM   4557 C CG   . ASN B 1 273 ? 107.95000 90.18300  73.19000  1.000 41.12050  ? 273 ASN B CG   1 
ATOM   4558 O OD1  . ASN B 1 273 ? 108.44000 90.04400  72.06900  1.000 40.91168  ? 273 ASN B OD1  1 
ATOM   4559 N ND2  . ASN B 1 273 ? 108.38600 89.51400  74.25000  1.000 41.35141  ? 273 ASN B ND2  1 
ATOM   4560 N N    . GLY B 1 274 ? 105.06500 93.77400  73.30600  1.000 42.62568  ? 274 GLY B N    1 
ATOM   4561 C CA   . GLY B 1 274 ? 103.77500 94.43900  73.31200  1.000 36.47884  ? 274 GLY B CA   1 
ATOM   4562 C C    . GLY B 1 274 ? 103.53200 95.26800  72.06700  1.000 35.78005  ? 274 GLY B C    1 
ATOM   4563 O O    . GLY B 1 274 ? 102.42100 95.28700  71.53300  1.000 37.92893  ? 274 GLY B O    1 
ATOM   4564 N N    . TYR B 1 275 ? 104.56300 95.96800  71.58300  1.000 30.01736  ? 275 TYR B N    1 
ATOM   4565 C CA   . TYR B 1 275 ? 104.36900 96.74500  70.36400  1.000 27.08174  ? 275 TYR B CA   1 
ATOM   4566 C C    . TYR B 1 275 ? 104.13500 95.85200  69.15500  1.000 32.36504  ? 275 TYR B C    1 
ATOM   4567 O O    . TYR B 1 275 ? 103.37700 96.22500  68.25300  1.000 30.11143  ? 275 TYR B O    1 
ATOM   4568 C CB   . TYR B 1 275 ? 105.55200 97.67100  70.09900  1.000 33.52625  ? 275 TYR B CB   1 
ATOM   4569 C CG   . TYR B 1 275 ? 105.30700 98.58700  68.92000  1.000 31.53542  ? 275 TYR B CG   1 
ATOM   4570 C CD1  . TYR B 1 275 ? 104.49200 99.70400  69.04400  1.000 32.40444  ? 275 TYR B CD1  1 
ATOM   4571 C CD2  . TYR B 1 275 ? 105.86600 98.32100  67.67800  1.000 30.23441  ? 275 TYR B CD2  1 
ATOM   4572 C CE1  . TYR B 1 275 ? 104.25600 100.54000 67.97200  1.000 27.71869  ? 275 TYR B CE1  1 
ATOM   4573 C CE2  . TYR B 1 275 ? 105.63400 99.15100  66.59900  1.000 28.98697  ? 275 TYR B CE2  1 
ATOM   4574 C CZ   . TYR B 1 275 ? 104.82900 100.25800 66.75200  1.000 30.16859  ? 275 TYR B CZ   1 
ATOM   4575 O OH   . TYR B 1 275 ? 104.59900 101.08900 65.68000  1.000 28.10913  ? 275 TYR B OH   1 
ATOM   4576 N N    . LEU B 1 276 ? 104.76000 94.67500  69.10900  1.000 49.57943  ? 276 LEU B N    1 
ATOM   4577 C CA   . LEU B 1 276 ? 104.60500 93.80700  67.94800  1.000 45.58207  ? 276 LEU B CA   1 
ATOM   4578 C C    . LEU B 1 276 ? 103.50800 92.76600  68.12500  1.000 44.73990  ? 276 LEU B C    1 
ATOM   4579 O O    . LEU B 1 276 ? 103.25600 91.98800  67.20000  1.000 47.84310  ? 276 LEU B O    1 
ATOM   4580 C CB   . LEU B 1 276 ? 105.92700 93.10900  67.61200  1.000 48.15252  ? 276 LEU B CB   1 
ATOM   4581 C CG   . LEU B 1 276 ? 106.97600 93.95900  66.89300  1.000 45.64427  ? 276 LEU B CG   1 
ATOM   4582 C CD1  . LEU B 1 276 ? 108.32500 93.26400  66.90100  1.000 45.14192  ? 276 LEU B CD1  1 
ATOM   4583 C CD2  . LEU B 1 276 ? 106.53400 94.26200  65.47000  1.000 42.31250  ? 276 LEU B CD2  1 
ATOM   4584 N N    . ARG B 1 277 ? 102.84200 92.74100  69.27700  1.000 57.84114  ? 277 ARG B N    1 
ATOM   4585 C CA   . ARG B 1 277 ? 101.79700 91.76000  69.54100  1.000 56.83647  ? 277 ARG B CA   1 
ATOM   4586 C C    . ARG B 1 277 ? 100.50100 92.19400  68.86600  1.000 55.68258  ? 277 ARG B C    1 
ATOM   4587 O O    . ARG B 1 277 ? 99.91900  93.22100  69.22900  1.000 57.10241  ? 277 ARG B O    1 
ATOM   4588 C CB   . ARG B 1 277 ? 101.59100 91.60300  71.04500  1.000 58.96140  ? 277 ARG B CB   1 
ATOM   4589 C CG   . ARG B 1 277 ? 100.18000 91.20300  71.44100  1.000 57.76146  ? 277 ARG B CG   1 
ATOM   4590 C CD   . ARG B 1 277 ? 100.11900 90.78500  72.90100  1.000 58.72412  ? 277 ARG B CD   1 
ATOM   4591 N NE   . ARG B 1 277 ? 101.35100 90.13900  73.33700  1.000 60.06667  ? 277 ARG B NE   1 
ATOM   4592 C CZ   . ARG B 1 277 ? 102.05500 90.51100  74.39800  1.000 59.77236  ? 277 ARG B CZ   1 
ATOM   4593 N NH1  . ARG B 1 277 ? 101.67400 91.52200  75.16100  1.000 59.18666  ? 277 ARG B NH1  1 
ATOM   4594 N NH2  . ARG B 1 277 ? 103.16900 89.85000  74.70200  1.000 58.34533  ? 277 ARG B NH2  1 
ATOM   4595 N N    . CYS B 1 278 ? 100.05000 91.41100  67.89100  1.000 70.78457  ? 278 CYS B N    1 
ATOM   4596 C CA   . CYS B 1 278 ? 98.82900  91.71800  67.15400  1.000 72.49885  ? 278 CYS B CA   1 
ATOM   4597 C C    . CYS B 1 278 ? 97.63700  91.88300  68.09100  1.000 71.84478  ? 278 CYS B C    1 
ATOM   4598 O O    . CYS B 1 278 ? 96.48500  91.77800  67.67000  1.000 70.70445  ? 278 CYS B O    1 
ATOM   4599 C CB   . CYS B 1 278 ? 98.53700  90.62500  66.12400  1.000 71.79178  ? 278 CYS B CB   1 
ATOM   4600 S SG   . CYS B 1 278 ? 99.03100  88.96300  66.63600  1.000 78.49631  ? 278 CYS B SG   1 
ATOM   4601 N N    . VAL B 1 298 ? 105.42900 95.93800  82.38800  1.000 49.77040  ? 298 VAL B N    1 
ATOM   4602 C CA   . VAL B 1 298 ? 106.57800 96.67700  81.88200  1.000 48.57057  ? 298 VAL B CA   1 
ATOM   4603 C C    . VAL B 1 298 ? 106.86100 97.88200  82.76900  1.000 44.95511  ? 298 VAL B C    1 
ATOM   4604 O O    . VAL B 1 298 ? 107.98100 98.39000  82.81000  1.000 48.45845  ? 298 VAL B O    1 
ATOM   4605 C CB   . VAL B 1 298 ? 106.35000 97.11400  80.42200  1.000 47.76938  ? 298 VAL B CB   1 
ATOM   4606 C CG1  . VAL B 1 298 ? 107.34600 98.18800  80.02500  1.000 45.62071  ? 298 VAL B CG1  1 
ATOM   4607 C CG2  . VAL B 1 298 ? 106.44900 95.91600  79.49100  1.000 46.07237  ? 298 VAL B CG2  1 
ATOM   4608 N N    . TYR B 1 299 ? 105.83100 98.33000  83.48800  1.000 48.32724  ? 299 TYR B N    1 
ATOM   4609 C CA   . TYR B 1 299 ? 105.95600 99.53500  84.30200  1.000 51.30549  ? 299 TYR B CA   1 
ATOM   4610 C C    . TYR B 1 299 ? 107.03000 99.37600  85.37200  1.000 49.90589  ? 299 TYR B C    1 
ATOM   4611 O O    . TYR B 1 299 ? 107.91800 100.22700 85.51300  1.000 48.62386  ? 299 TYR B O    1 
ATOM   4612 C CB   . TYR B 1 299 ? 104.60800 99.86800  84.94200  1.000 50.45760  ? 299 TYR B CB   1 
ATOM   4613 C CG   . TYR B 1 299 ? 104.40200 101.33800 85.22700  1.000 52.37293  ? 299 TYR B CG   1 
ATOM   4614 C CD1  . TYR B 1 299 ? 104.62000 102.29400 84.24500  1.000 50.25847  ? 299 TYR B CD1  1 
ATOM   4615 C CD2  . TYR B 1 299 ? 103.99200 101.77000 86.48100  1.000 51.07561  ? 299 TYR B CD2  1 
ATOM   4616 C CE1  . TYR B 1 299 ? 104.43200 103.63800 84.50300  1.000 51.78628  ? 299 TYR B CE1  1 
ATOM   4617 C CE2  . TYR B 1 299 ? 103.80300 103.11100 86.74900  1.000 50.13388  ? 299 TYR B CE2  1 
ATOM   4618 C CZ   . TYR B 1 299 ? 104.02400 104.04100 85.75600  1.000 52.83567  ? 299 TYR B CZ   1 
ATOM   4619 O OH   . TYR B 1 299 ? 103.83800 105.37900 86.01700  1.000 51.01642  ? 299 TYR B OH   1 
ATOM   4620 N N    . LYS B 1 300 ? 106.97000 98.27700  86.12700  1.000 48.78592  ? 300 LYS B N    1 
ATOM   4621 C CA   . LYS B 1 300 ? 107.85000 98.11200  87.27900  1.000 51.72437  ? 300 LYS B CA   1 
ATOM   4622 C C    . LYS B 1 300 ? 109.31900 98.05200  86.88400  1.000 51.65008  ? 300 LYS B C    1 
ATOM   4623 O O    . LYS B 1 300 ? 110.16800 98.59600  87.59800  1.000 48.36031  ? 300 LYS B O    1 
ATOM   4624 C CB   . LYS B 1 300 ? 107.46100 96.85300  88.05500  1.000 47.98546  ? 300 LYS B CB   1 
ATOM   4625 N N    . GLY B 1 301 ? 109.63500 97.46300  85.73400  1.000 39.97874  ? 301 GLY B N    1 
ATOM   4626 C CA   . GLY B 1 301 ? 111.02100 97.36600  85.32200  1.000 40.72477  ? 301 GLY B CA   1 
ATOM   4627 C C    . GLY B 1 301 ? 111.72300 98.70400  85.23900  1.000 39.57617  ? 301 GLY B C    1 
ATOM   4628 O O    . GLY B 1 301 ? 112.70200 98.93300  85.95500  1.000 44.24747  ? 301 GLY B O    1 
ATOM   4629 N N    . TYR B 1 302 ? 111.24700 99.59900  84.37600  1.000 38.28062  ? 302 TYR B N    1 
ATOM   4630 C CA   . TYR B 1 302 ? 111.90000 100.89400 84.24500  1.000 42.04146  ? 302 TYR B CA   1 
ATOM   4631 C C    . TYR B 1 302 ? 111.55800 101.82900 85.39900  1.000 40.55120  ? 302 TYR B C    1 
ATOM   4632 O O    . TYR B 1 302 ? 112.33300 102.75200 85.68400  1.000 43.40621  ? 302 TYR B O    1 
ATOM   4633 C CB   . TYR B 1 302 ? 111.56600 101.52600 82.88600  1.000 38.25591  ? 302 TYR B CB   1 
ATOM   4634 C CG   . TYR B 1 302 ? 110.17100 102.09200 82.72800  1.000 39.68131  ? 302 TYR B CG   1 
ATOM   4635 C CD1  . TYR B 1 302 ? 109.81600 103.30400 83.30500  1.000 39.10634  ? 302 TYR B CD1  1 
ATOM   4636 C CD2  . TYR B 1 302 ? 109.21600 101.42200 81.97400  1.000 38.45010  ? 302 TYR B CD2  1 
ATOM   4637 C CE1  . TYR B 1 302 ? 108.54700 103.82200 83.15100  1.000 39.42699  ? 302 TYR B CE1  1 
ATOM   4638 C CE2  . TYR B 1 302 ? 107.94600 101.93400 81.81400  1.000 37.91502  ? 302 TYR B CE2  1 
ATOM   4639 C CZ   . TYR B 1 302 ? 107.61600 103.13400 82.40500  1.000 41.29996  ? 302 TYR B CZ   1 
ATOM   4640 O OH   . TYR B 1 302 ? 106.35200 103.65000 82.24700  1.000 43.77966  ? 302 TYR B OH   1 
ATOM   4641 N N    . ARG B 1 303 ? 110.43800 101.59400 86.09100  1.000 46.30766  ? 303 ARG B N    1 
ATOM   4642 C CA   . ARG B 1 303 ? 110.05900 102.47100 87.19300  1.000 45.85379  ? 303 ARG B CA   1 
ATOM   4643 C C    . ARG B 1 303 ? 110.96600 102.26500 88.40000  1.000 49.40412  ? 303 ARG B C    1 
ATOM   4644 O O    . ARG B 1 303 ? 111.32400 103.23100 89.08400  1.000 47.09212  ? 303 ARG B O    1 
ATOM   4645 C CB   . ARG B 1 303 ? 108.59900 102.23000 87.57300  1.000 47.91881  ? 303 ARG B CB   1 
ATOM   4646 C CG   . ARG B 1 303 ? 107.59700 103.03400 86.76200  1.000 48.55482  ? 303 ARG B CG   1 
ATOM   4647 C CD   . ARG B 1 303 ? 107.01600 104.17600 87.58000  1.000 50.59787  ? 303 ARG B CD   1 
ATOM   4648 N NE   . ARG B 1 303 ? 107.76900 105.41200 87.40800  1.000 51.58873  ? 303 ARG B NE   1 
ATOM   4649 C CZ   . ARG B 1 303 ? 107.54700 106.29700 86.44700  1.000 48.71938  ? 303 ARG B CZ   1 
ATOM   4650 N NH1  . ARG B 1 303 ? 106.59500 106.11500 85.54700  1.000 45.40362  ? 303 ARG B NH1  1 
ATOM   4651 N NH2  . ARG B 1 303 ? 108.29900 107.39300 86.38700  1.000 48.85679  ? 303 ARG B NH2  1 
ATOM   4652 N N    . SER B 1 304 ? 111.34900 101.01700 88.68100  1.000 45.88853  ? 304 SER B N    1 
ATOM   4653 C CA   . SER B 1 304 ? 112.24100 100.76000 89.80600  1.000 44.14245  ? 304 SER B CA   1 
ATOM   4654 C C    . SER B 1 304 ? 113.59400 101.42100 89.59100  1.000 44.70401  ? 304 SER B C    1 
ATOM   4655 O O    . SER B 1 304 ? 114.19900 101.94400 90.53500  1.000 42.35850  ? 304 SER B O    1 
ATOM   4656 C CB   . SER B 1 304 ? 112.40500 99.25400  90.01200  1.000 46.81746  ? 304 SER B CB   1 
ATOM   4657 O OG   . SER B 1 304 ? 111.14800 98.60100  90.02500  1.000 49.02662  ? 304 SER B OG   1 
ATOM   4658 N N    . ALA B 1 305 ? 114.08700 101.40500 88.35200  1.000 40.04357  ? 305 ALA B N    1 
ATOM   4659 C CA   . ALA B 1 305 ? 115.35000 102.06600 88.04500  1.000 37.06302  ? 305 ALA B CA   1 
ATOM   4660 C C    . ALA B 1 305 ? 115.21800 103.58200 88.13100  1.000 35.12511  ? 305 ALA B C    1 
ATOM   4661 O O    . ALA B 1 305 ? 116.04300 104.25000 88.76500  1.000 41.38864  ? 305 ALA B O    1 
ATOM   4662 C CB   . ALA B 1 305 ? 115.83900 101.64400 86.65900  1.000 35.87621  ? 305 ALA B CB   1 
ATOM   4663 N N    . VAL B 1 306 ? 114.18600 104.14700 87.50000  1.000 35.04635  ? 306 VAL B N    1 
ATOM   4664 C CA   . VAL B 1 306 ? 114.04700 105.60200 87.48700  1.000 37.52640  ? 306 VAL B CA   1 
ATOM   4665 C C    . VAL B 1 306 ? 113.87300 106.14800 88.90000  1.000 40.18452  ? 306 VAL B C    1 
ATOM   4666 O O    . VAL B 1 306 ? 114.36800 107.23400 89.22400  1.000 42.96418  ? 306 VAL B O    1 
ATOM   4667 C CB   . VAL B 1 306 ? 112.87800 106.01800 86.57400  1.000 37.60918  ? 306 VAL B CB   1 
ATOM   4668 C CG1  . VAL B 1 306 ? 112.66200 107.51900 86.64500  1.000 38.02980  ? 306 VAL B CG1  1 
ATOM   4669 C CG2  . VAL B 1 306 ? 113.14400 105.58200 85.14100  1.000 39.41367  ? 306 VAL B CG2  1 
ATOM   4670 N N    . GLU B 1 307 ? 113.16900 105.41400 89.76100  1.000 46.68409  ? 307 GLU B N    1 
ATOM   4671 C CA   . GLU B 1 307 ? 112.86900 105.90700 91.10100  1.000 43.81726  ? 307 GLU B CA   1 
ATOM   4672 C C    . GLU B 1 307 ? 113.67700 105.20400 92.18800  1.000 45.28514  ? 307 GLU B C    1 
ATOM   4673 O O    . GLU B 1 307 ? 113.09700 104.54500 93.05700  1.000 48.13469  ? 307 GLU B O    1 
ATOM   4674 C CB   . GLU B 1 307 ? 111.37400 105.76000 91.39200  1.000 44.48749  ? 307 GLU B CB   1 
ATOM   4675 N N    . SER B 1 308 ? 115.00400 105.33100 92.16200  1.000 43.61989  ? 308 SER B N    1 
ATOM   4676 C CA   . SER B 1 308 ? 115.80900 104.65600 93.17300  1.000 45.24146  ? 308 SER B CA   1 
ATOM   4677 C C    . SER B 1 308 ? 117.04500 105.42400 93.62200  1.000 45.06214  ? 308 SER B C    1 
ATOM   4678 O O    . SER B 1 308 ? 117.73200 104.94800 94.53000  1.000 48.12031  ? 308 SER B O    1 
ATOM   4679 C CB   . SER B 1 308 ? 116.22700 103.26900 92.65500  1.000 45.12441  ? 308 SER B CB   1 
ATOM   4680 O OG   . SER B 1 308 ? 116.99300 102.57100 93.62000  1.000 46.92117  ? 308 SER B OG   1 
ATOM   4681 N N    . THR B 1 309 ? 117.36200 106.58000 93.03500  1.000 41.58270  ? 309 THR B N    1 
ATOM   4682 C CA   . THR B 1 309 ? 118.58500 107.28600 93.40700  1.000 44.12073  ? 309 THR B CA   1 
ATOM   4683 C C    . THR B 1 309 ? 118.62300 107.61600 94.89700  1.000 43.51265  ? 309 THR B C    1 
ATOM   4684 O O    . THR B 1 309 ? 119.68600 107.55200 95.52800  1.000 44.60797  ? 309 THR B O    1 
ATOM   4685 C CB   . THR B 1 309 ? 118.72500 108.56200 92.57800  1.000 45.44103  ? 309 THR B CB   1 
ATOM   4686 O OG1  . THR B 1 309 ? 118.80300 108.22400 91.18800  1.000 44.74166  ? 309 THR B OG1  1 
ATOM   4687 C CG2  . THR B 1 309 ? 119.98000 109.31900 92.98000  1.000 45.19916  ? 309 THR B CG2  1 
ATOM   4688 N N    . SER B 1 310 ? 117.47300 107.96000 95.48000  1.000 39.85291  ? 310 SER B N    1 
ATOM   4689 C CA   . SER B 1 310 ? 117.43300 108.27500 96.90500  1.000 44.55027  ? 310 SER B CA   1 
ATOM   4690 C C    . SER B 1 310 ? 117.85100 107.07700 97.74700  1.000 43.90696  ? 310 SER B C    1 
ATOM   4691 O O    . SER B 1 310 ? 118.64200 107.20800 98.69000  1.000 41.50019  ? 310 SER B O    1 
ATOM   4692 C CB   . SER B 1 310 ? 116.03300 108.74900 97.29500  1.000 44.45068  ? 310 SER B CB   1 
ATOM   4693 O OG   . SER B 1 310 ? 115.04000 107.87900 96.78100  1.000 47.33321  ? 310 SER B OG   1 
ATOM   4694 N N    . GLN B 1 311 ? 117.32400 105.89500 97.42200  1.000 41.71973  ? 311 GLN B N    1 
ATOM   4695 C CA   . GLN B 1 311 ? 117.70900 104.69100 98.14800  1.000 41.43144  ? 311 GLN B CA   1 
ATOM   4696 C C    . GLN B 1 311 ? 119.19700 104.40800 97.99000  1.000 37.38991  ? 311 GLN B C    1 
ATOM   4697 O O    . GLN B 1 311 ? 119.87700 104.04500 98.95900  1.000 41.38752  ? 311 GLN B O    1 
ATOM   4698 C CB   . GLN B 1 311 ? 116.87300 103.50500 97.66800  1.000 38.54132  ? 311 GLN B CB   1 
ATOM   4699 C CG   . GLN B 1 311 ? 116.87100 102.31900 98.61600  1.000 43.04958  ? 311 GLN B CG   1 
ATOM   4700 C CD   . GLN B 1 311 ? 116.27300 101.07700 97.98900  1.000 45.21943  ? 311 GLN B CD   1 
ATOM   4701 O OE1  . GLN B 1 311 ? 115.57600 101.15200 96.97700  1.000 45.83704  ? 311 GLN B OE1  1 
ATOM   4702 N NE2  . GLN B 1 311 ? 116.54000 99.92300  98.59000  1.000 42.50177  ? 311 GLN B NE2  1 
ATOM   4703 N N    . GLU B 1 312 ? 119.72000 104.56000 96.77000  1.000 27.73352  ? 312 GLU B N    1 
ATOM   4704 C CA   . GLU B 1 312 ? 121.13000 104.27500 96.53400  1.000 33.03707  ? 312 GLU B CA   1 
ATOM   4705 C C    . GLU B 1 312 ? 122.02000 105.20800 97.34300  1.000 38.21325  ? 312 GLU B C    1 
ATOM   4706 O O    . GLU B 1 312 ? 123.01700 104.77300 97.93400  1.000 38.58291  ? 312 GLU B O    1 
ATOM   4707 C CB   . GLU B 1 312 ? 121.44800 104.40200 95.04400  1.000 34.54458  ? 312 GLU B CB   1 
ATOM   4708 C CG   . GLU B 1 312 ? 121.14600 103.16100 94.22400  1.000 37.86681  ? 312 GLU B CG   1 
ATOM   4709 C CD   . GLU B 1 312 ? 120.18100 103.44000 93.08800  1.000 40.94005  ? 312 GLU B CD   1 
ATOM   4710 O OE1  . GLU B 1 312 ? 120.26700 104.53400 92.49200  1.000 41.75319  ? 312 GLU B OE1  1 
ATOM   4711 O OE2  . GLU B 1 312 ? 119.33600 102.57000 92.78900  1.000 42.16552  ? 312 GLU B OE2  1 
ATOM   4712 N N    . GLU B 1 313 ? 121.63400 106.48100 97.45200  1.000 39.35367  ? 313 GLU B N    1 
ATOM   4713 C CA   . GLU B 1 313 ? 122.45900 107.42200 98.20100  1.000 28.89735  ? 313 GLU B CA   1 
ATOM   4714 C C    . GLU B 1 313 ? 122.31000 107.24100 99.70400  1.000 30.17486  ? 313 GLU B C    1 
ATOM   4715 O O    . GLU B 1 313 ? 123.28500 107.42100 100.44100 1.000 39.81614  ? 313 GLU B O    1 
ATOM   4716 C CB   . GLU B 1 313 ? 122.11300 108.85900 97.80800  1.000 33.65015  ? 313 GLU B CB   1 
ATOM   4717 C CG   . GLU B 1 313 ? 121.96800 109.07200 96.31300  1.000 36.46271  ? 313 GLU B CG   1 
ATOM   4718 C CD   . GLU B 1 313 ? 123.12700 109.84500 95.72100  1.000 40.86779  ? 313 GLU B CD   1 
ATOM   4719 O OE1  . GLU B 1 313 ? 122.95000 110.45300 94.64500  1.000 41.23561  ? 313 GLU B OE1  1 
ATOM   4720 O OE2  . GLU B 1 313 ? 124.21600 109.84400 96.33200  1.000 39.47405  ? 313 GLU B OE2  1 
ATOM   4721 N N    . SER B 1 314 ? 121.13000 106.83900 100.17700 1.000 20.55152  ? 314 SER B N    1 
ATOM   4722 C CA   . SER B 1 314 ? 120.98400 106.53400 101.59600 1.000 18.54504  ? 314 SER B CA   1 
ATOM   4723 C C    . SER B 1 314 ? 121.84200 105.33300 101.97900 1.000 20.57250  ? 314 SER B C    1 
ATOM   4724 O O    . SER B 1 314 ? 122.55300 105.35200 102.99500 1.000 19.83317  ? 314 SER B O    1 
ATOM   4725 C CB   . SER B 1 314 ? 119.51300 106.28300 101.92700 1.000 16.76263  ? 314 SER B CB   1 
ATOM   4726 O OG   . SER B 1 314 ? 119.26100 106.47000 103.30800 1.000 29.13341  ? 314 SER B OG   1 
ATOM   4727 N N    . LEU B 1 315 ? 121.79000 104.27100 101.17000 1.000 16.52291  ? 315 LEU B N    1 
ATOM   4728 C CA   . LEU B 1 315 ? 122.59800 103.09600 101.46800 1.000 9.48696   ? 315 LEU B CA   1 
ATOM   4729 C C    . LEU B 1 315 ? 124.08500 103.40100 101.34300 1.000 17.20471  ? 315 LEU B C    1 
ATOM   4730 O O    . LEU B 1 315 ? 124.89700 102.83200 102.08400 1.000 22.46099  ? 315 LEU B O    1 
ATOM   4731 C CB   . LEU B 1 315 ? 122.20800 101.94600 100.54100 1.000 14.19133  ? 315 LEU B CB   1 
ATOM   4732 C CG   . LEU B 1 315 ? 120.87000 101.26900 100.83900 1.000 16.26421  ? 315 LEU B CG   1 
ATOM   4733 C CD1  . LEU B 1 315 ? 120.44700 100.38600 99.67900  1.000 10.93386  ? 315 LEU B CD1  1 
ATOM   4734 C CD2  . LEU B 1 315 ? 120.94400 100.47100 102.12800 1.000 22.21913  ? 315 LEU B CD2  1 
ATOM   4735 N N    . MET B 1 316 ? 124.45700 104.33200 100.45600 1.000 15.27253  ? 316 MET B N    1 
ATOM   4736 C CA   . MET B 1 316 ? 125.85600 104.72800 100.37100 1.000 13.58211  ? 316 MET B CA   1 
ATOM   4737 C C    . MET B 1 316 ? 126.27700 105.55500 101.57600 1.000 22.25464  ? 316 MET B C    1 
ATOM   4738 O O    . MET B 1 316 ? 127.44700 105.51700 101.97400 1.000 22.91867  ? 316 MET B O    1 
ATOM   4739 C CB   . MET B 1 316 ? 126.10400 105.52300 99.09000  1.000 12.94090  ? 316 MET B CB   1 
ATOM   4740 C CG   . MET B 1 316 ? 127.47700 105.29800 98.48100  1.000 22.29134  ? 316 MET B CG   1 
ATOM   4741 S SD   . MET B 1 316 ? 128.60000 106.67900 98.74900  1.000 32.71972  ? 316 MET B SD   1 
ATOM   4742 C CE   . MET B 1 316 ? 128.01500 107.82900 97.51000  1.000 22.52256  ? 316 MET B CE   1 
ATOM   4743 N N    . SER B 1 317 ? 125.33900 106.21500 102.24200 1.000 19.50635  ? 317 SER B N    1 
ATOM   4744 C CA   . SER B 1 317 ? 125.66700 107.01100 103.42700 1.000 12.33516  ? 317 SER B CA   1 
ATOM   4745 C C    . SER B 1 317 ? 125.87800 106.18100 104.69700 1.000 19.50741  ? 317 SER B C    1 
ATOM   4746 O O    . SER B 1 317 ? 126.43900 106.67100 105.66700 1.000 24.50477  ? 317 SER B O    1 
ATOM   4747 C CB   . SER B 1 317 ? 124.58200 108.05500 103.67300 1.000 14.90985  ? 317 SER B CB   1 
ATOM   4748 O OG   . SER B 1 317 ? 123.36200 107.44800 104.05200 1.000 19.73149  ? 317 SER B OG   1 
ATOM   4749 N N    . PHE B 1 318 ? 125.43300 104.93300 104.69800 1.000 14.60586  ? 318 PHE B N    1 
ATOM   4750 C CA   . PHE B 1 318 ? 125.57700 104.07600 105.86800 1.000 3.77065   ? 318 PHE B CA   1 
ATOM   4751 C C    . PHE B 1 318 ? 126.68500 103.03600 105.70300 1.000 10.13053  ? 318 PHE B C    1 
ATOM   4752 O O    . PHE B 1 318 ? 127.41900 102.77100 106.64500 1.000 10.11783  ? 318 PHE B O    1 
ATOM   4753 C CB   . PHE B 1 318 ? 124.25600 103.38000 106.16000 1.000 6.22805   ? 318 PHE B CB   1 
ATOM   4754 C CG   . PHE B 1 318 ? 123.13700 104.31100 106.49400 1.000 8.81383   ? 318 PHE B CG   1 
ATOM   4755 C CD1  . PHE B 1 318 ? 123.33200 105.36100 107.37100 1.000 14.26873  ? 318 PHE B CD1  1 
ATOM   4756 C CD2  . PHE B 1 318 ? 121.88100 104.11900 105.95200 1.000 9.19413   ? 318 PHE B CD2  1 
ATOM   4757 C CE1  . PHE B 1 318 ? 122.29700 106.21700 107.68700 1.000 11.85470  ? 318 PHE B CE1  1 
ATOM   4758 C CE2  . PHE B 1 318 ? 120.84000 104.97000 106.26400 1.000 7.18845   ? 318 PHE B CE2  1 
ATOM   4759 C CZ   . PHE B 1 318 ? 121.04800 106.02100 107.13300 1.000 7.90553   ? 318 PHE B CZ   1 
ATOM   4760 N N    . ALA B 1 319 ? 126.82000 102.47400 104.50400 1.000 12.85111  ? 319 ALA B N    1 
ATOM   4761 C CA   . ALA B 1 319 ? 127.83600 101.45800 104.21900 1.000 7.11683   ? 319 ALA B CA   1 
ATOM   4762 C C    . ALA B 1 319 ? 129.15600 101.89700 104.78400 1.000 16.97756  ? 319 ALA B C    1 
ATOM   4763 O O    . ALA B 1 319 ? 129.93600 101.08700 105.27200 1.000 26.94888  ? 319 ALA B O    1 
ATOM   4764 C CB   . ALA B 1 319 ? 127.79000 101.10600 102.74900 1.000 0.09888   ? 319 ALA B CB   1 
ATOM   4765 N N    . ILE B 1 320 ? 129.37800 103.18200 104.82800 1.000 10.42481  ? 320 ILE B N    1 
ATOM   4766 C CA   . ILE B 1 320 ? 130.69700 103.77500 105.07800 1.000 11.33082  ? 320 ILE B CA   1 
ATOM   4767 C C    . ILE B 1 320 ? 131.01100 103.60100 106.56700 1.000 18.92753  ? 320 ILE B C    1 
ATOM   4768 O O    . ILE B 1 320 ? 132.15400 103.32400 106.91400 1.000 26.68278  ? 320 ILE B O    1 
ATOM   4769 C CB   . ILE B 1 320 ? 130.78700 105.22600 104.57400 1.000 13.94373  ? 320 ILE B CB   1 
ATOM   4770 C CG1  . ILE B 1 320 ? 129.75600 106.09900 105.28400 1.000 18.45224  ? 320 ILE B CG1  1 
ATOM   4771 C CG2  . ILE B 1 320 ? 130.58000 105.27600 103.07000 1.000 14.96893  ? 320 ILE B CG2  1 
ATOM   4772 C CD1  . ILE B 1 320 ? 129.74100 107.53300 104.80800 1.000 16.46535  ? 320 ILE B CD1  1 
ATOM   4773 N N    . TRP B 1 321 ? 130.14100 103.93400 107.46900 1.000 8.60744   ? 321 TRP B N    1 
ATOM   4774 C CA   . TRP B 1 321 ? 130.38600 103.70800 108.88300 1.000 6.50951   ? 321 TRP B CA   1 
ATOM   4775 C C    . TRP B 1 321 ? 130.91700 102.31700 109.10400 1.000 9.09857   ? 321 TRP B C    1 
ATOM   4776 O O    . TRP B 1 321 ? 131.80400 102.11900 109.92200 1.000 12.92421  ? 321 TRP B O    1 
ATOM   4777 C CB   . TRP B 1 321 ? 129.17700 104.12800 109.70200 1.000 17.46036  ? 321 TRP B CB   1 
ATOM   4778 C CG   . TRP B 1 321 ? 128.87200 105.58300 109.69800 1.000 20.13240  ? 321 TRP B CG   1 
ATOM   4779 C CD1  . TRP B 1 321 ? 128.37800 106.31600 108.66300 1.000 11.78148  ? 321 TRP B CD1  1 
ATOM   4780 C CD2  . TRP B 1 321 ? 129.00700 106.48400 110.80100 1.000 15.76768  ? 321 TRP B CD2  1 
ATOM   4781 N NE1  . TRP B 1 321 ? 128.21400 107.62300 109.04600 1.000 13.66876  ? 321 TRP B NE1  1 
ATOM   4782 C CE2  . TRP B 1 321 ? 128.59200 107.75200 110.35700 1.000 17.33750  ? 321 TRP B CE2  1 
ATOM   4783 C CE3  . TRP B 1 321 ? 129.44700 106.34200 112.12000 1.000 9.55357   ? 321 TRP B CE3  1 
ATOM   4784 C CZ2  . TRP B 1 321 ? 128.60400 108.87200 111.18400 1.000 15.40604  ? 321 TRP B CZ2  1 
ATOM   4785 C CZ3  . TRP B 1 321 ? 129.45900 107.45500 112.93800 1.000 10.52915  ? 321 TRP B CZ3  1 
ATOM   4786 C CH2  . TRP B 1 321 ? 129.04000 108.70200 112.46800 1.000 12.03434  ? 321 TRP B CH2  1 
ATOM   4787 N N    . GLU B 1 322 ? 130.38100 101.34200 108.38100 1.000 14.81168  ? 322 GLU B N    1 
ATOM   4788 C CA   . GLU B 1 322 ? 130.59100 99.92800  108.67500 1.000 11.66867  ? 322 GLU B CA   1 
ATOM   4789 C C    . GLU B 1 322 ? 132.03200 99.47900  108.45700 1.000 15.40145  ? 322 GLU B C    1 
ATOM   4790 O O    . GLU B 1 322 ? 132.72000 100.00100 107.58800 1.000 19.40776  ? 322 GLU B O    1 
ATOM   4791 C CB   . GLU B 1 322 ? 129.63000 99.09800  107.83100 1.000 10.90339  ? 322 GLU B CB   1 
ATOM   4792 C CG   . GLU B 1 322 ? 128.16700 99.42900  108.07300 1.000 12.97153  ? 322 GLU B CG   1 
ATOM   4793 C CD   . GLU B 1 322 ? 127.23800 98.71700  107.11100 1.000 11.77278  ? 322 GLU B CD   1 
ATOM   4794 O OE1  . GLU B 1 322 ? 127.68700 98.36600  106.00300 1.000 20.44345  ? 322 GLU B OE1  1 
ATOM   4795 O OE2  . GLU B 1 322 ? 126.05900 98.51600  107.45800 1.000 11.87332  ? 322 GLU B OE2  1 
ATOM   4796 N N    . PRO B 1 323 ? 132.50200 98.51800  109.26700 1.000 23.72860  ? 323 PRO B N    1 
ATOM   4797 C CA   . PRO B 1 323 ? 133.88300 98.03600  109.14900 1.000 25.53909  ? 323 PRO B CA   1 
ATOM   4798 C C    . PRO B 1 323 ? 134.01600 96.98700  108.06000 1.000 24.13981  ? 323 PRO B C    1 
ATOM   4799 O O    . PRO B 1 323 ? 133.01200 96.43700  107.58300 1.000 24.15363  ? 323 PRO B O    1 
ATOM   4800 C CB   . PRO B 1 323 ? 134.15900 97.44000  110.53600 1.000 21.34393  ? 323 PRO B CB   1 
ATOM   4801 C CG   . PRO B 1 323 ? 132.82000 96.99100  111.00000 1.000 18.80444  ? 323 PRO B CG   1 
ATOM   4802 C CD   . PRO B 1 323 ? 131.85100 98.02400  110.49300 1.000 21.16997  ? 323 PRO B CD   1 
ATOM   4803 N N    . PRO B 1 324 ? 135.24400 96.68200  107.64200 1.000 29.46158  ? 324 PRO B N    1 
ATOM   4804 C CA   . PRO B 1 324 ? 135.44800 95.66900  106.59700 1.000 29.52436  ? 324 PRO B CA   1 
ATOM   4805 C C    . PRO B 1 324 ? 134.90100 94.30800  107.00300 1.000 30.16496  ? 324 PRO B C    1 
ATOM   4806 O O    . PRO B 1 324 ? 134.95600 93.91700  108.17100 1.000 29.47487  ? 324 PRO B O    1 
ATOM   4807 C CB   . PRO B 1 324 ? 136.97200 95.63200  106.44000 1.000 26.36454  ? 324 PRO B CB   1 
ATOM   4808 C CG   . PRO B 1 324 ? 137.41700 96.98700  106.86900 1.000 28.99250  ? 324 PRO B CG   1 
ATOM   4809 C CD   . PRO B 1 324 ? 136.50000 97.36100  108.00000 1.000 25.53849  ? 324 PRO B CD   1 
ATOM   4810 N N    . HIS B 1 325 ? 134.36700 93.58400  106.02000 1.000 27.08995  ? 325 HIS B N    1 
ATOM   4811 C CA   . HIS B 1 325 ? 133.76800 92.28000  106.26800 1.000 23.38310  ? 325 HIS B CA   1 
ATOM   4812 C C    . HIS B 1 325 ? 133.57200 91.55500  104.94500 1.000 23.42008  ? 325 HIS B C    1 
ATOM   4813 O O    . HIS B 1 325 ? 133.12200 92.15200  103.96500 1.000 24.67689  ? 325 HIS B O    1 
ATOM   4814 C CB   . HIS B 1 325 ? 132.42100 92.41500  106.99300 1.000 14.07107  ? 325 HIS B CB   1 
ATOM   4815 C CG   . HIS B 1 325 ? 131.36300 93.08700  106.17500 1.000 21.61806  ? 325 HIS B CG   1 
ATOM   4816 N ND1  . HIS B 1 325 ? 130.36200 92.38800  105.53400 1.000 24.42947  ? 325 HIS B ND1  1 
ATOM   4817 C CD2  . HIS B 1 325 ? 131.15300 94.39300  105.88700 1.000 22.56486  ? 325 HIS B CD2  1 
ATOM   4818 C CE1  . HIS B 1 325 ? 129.58100 93.23500  104.88900 1.000 21.17248  ? 325 HIS B CE1  1 
ATOM   4819 N NE2  . HIS B 1 325 ? 130.03800 94.45800  105.08700 1.000 19.39074  ? 325 HIS B NE2  1 
ATOM   4820 N N    . GLY B 1 326 ? 133.91500 90.26900  104.93100 1.000 30.73722  ? 326 GLY B N    1 
ATOM   4821 C CA   . GLY B 1 326 ? 133.70100 89.41300  103.78700 1.000 28.93500  ? 326 GLY B CA   1 
ATOM   4822 C C    . GLY B 1 326 ? 134.46800 89.81000  102.54200 1.000 37.13117  ? 326 GLY B C    1 
ATOM   4823 O O    . GLY B 1 326 ? 135.68900 89.99100  102.56300 1.000 39.39059  ? 326 GLY B O    1 
ATOM   4824 N N    . PRO B 1 327 ? 133.75300 89.94600  101.42000 1.000 36.44549  ? 327 PRO B N    1 
ATOM   4825 C CA   . PRO B 1 327 ? 134.42200 90.30700  100.15900 1.000 30.54590  ? 327 PRO B CA   1 
ATOM   4826 C C    . PRO B 1 327 ? 134.95200 91.72800  100.12600 1.000 31.26058  ? 327 PRO B C    1 
ATOM   4827 O O    . PRO B 1 327 ? 135.83800 92.01900  99.31300  1.000 35.82498  ? 327 PRO B O    1 
ATOM   4828 C CB   . PRO B 1 327 ? 133.32100 90.10500  99.10900  1.000 28.96240  ? 327 PRO B CB   1 
ATOM   4829 C CG   . PRO B 1 327 ? 132.34500 89.17200  99.75500  1.000 28.84425  ? 327 PRO B CG   1 
ATOM   4830 C CD   . PRO B 1 327 ? 132.35200 89.55300  101.20200 1.000 31.60953  ? 327 PRO B CD   1 
ATOM   4831 N N    . TYR B 1 328 ? 134.44200 92.62000  100.96800 1.000 23.45361  ? 328 TYR B N    1 
ATOM   4832 C CA   . TYR B 1 328 ? 134.86000 94.01900  100.99200 1.000 23.77367  ? 328 TYR B CA   1 
ATOM   4833 C C    . TYR B 1 328 ? 135.83700 94.18200  102.14900 1.000 27.17347  ? 328 TYR B C    1 
ATOM   4834 O O    . TYR B 1 328 ? 135.43100 94.36600  103.29900 1.000 34.73371  ? 328 TYR B O    1 
ATOM   4835 C CB   . TYR B 1 328 ? 133.64500 94.92900  101.13200 1.000 20.91277  ? 328 TYR B CB   1 
ATOM   4836 C CG   . TYR B 1 328 ? 132.38600 94.32400  100.55200 1.000 24.30396  ? 328 TYR B CG   1 
ATOM   4837 C CD1  . TYR B 1 328 ? 132.14200 94.35000  99.18600  1.000 29.37286  ? 328 TYR B CD1  1 
ATOM   4838 C CD2  . TYR B 1 328 ? 131.44900 93.70900  101.37100 1.000 26.82701  ? 328 TYR B CD2  1 
ATOM   4839 C CE1  . TYR B 1 328 ? 130.99600 93.79000  98.65400  1.000 25.89417  ? 328 TYR B CE1  1 
ATOM   4840 C CE2  . TYR B 1 328 ? 130.30200 93.14800  100.84900 1.000 25.26950  ? 328 TYR B CE2  1 
ATOM   4841 C CZ   . TYR B 1 328 ? 130.07900 93.19100  99.49000  1.000 25.58500  ? 328 TYR B CZ   1 
ATOM   4842 O OH   . TYR B 1 328 ? 128.93500 92.63300  98.97000  1.000 23.73405  ? 328 TYR B OH   1 
ATOM   4843 N N    . LYS B 1 329 ? 137.13500 94.12000  101.84200 1.000 38.66815  ? 329 LYS B N    1 
ATOM   4844 C CA   . LYS B 1 329 ? 138.16600 94.08100  102.86900 1.000 41.83301  ? 329 LYS B CA   1 
ATOM   4845 C C    . LYS B 1 329 ? 139.00500 95.34500  102.97400 1.000 43.51984  ? 329 LYS B C    1 
ATOM   4846 O O    . LYS B 1 329 ? 139.69600 95.51800  103.98200 1.000 45.83883  ? 329 LYS B O    1 
ATOM   4847 C CB   . LYS B 1 329 ? 139.10300 92.88800  102.63000 1.000 42.78828  ? 329 LYS B CB   1 
ATOM   4848 C CG   . LYS B 1 329 ? 139.58900 92.76000  101.19600 1.000 44.10414  ? 329 LYS B CG   1 
ATOM   4849 C CD   . LYS B 1 329 ? 139.74400 91.30100  100.80100 1.000 43.27521  ? 329 LYS B CD   1 
ATOM   4850 C CE   . LYS B 1 329 ? 138.40700 90.58100  100.82300 1.000 42.89493  ? 329 LYS B CE   1 
ATOM   4851 N NZ   . LYS B 1 329 ? 138.56500 89.10900  100.66700 1.000 44.84559  ? 329 LYS B NZ   1 
ATOM   4852 N N    . SER B 1 330 ? 138.97400 96.22400  101.97700 1.000 45.21617  ? 330 SER B N    1 
ATOM   4853 C CA   . SER B 1 330 ? 139.71900 97.46600  102.09800 1.000 45.26086  ? 330 SER B CA   1 
ATOM   4854 C C    . SER B 1 330 ? 138.96700 98.45200  102.98700 1.000 45.95903  ? 330 SER B C    1 
ATOM   4855 O O    . SER B 1 330 ? 137.74700 98.37200  103.15800 1.000 48.11821  ? 330 SER B O    1 
ATOM   4856 C CB   . SER B 1 330 ? 139.97200 98.08000  100.72100 1.000 47.05151  ? 330 SER B CB   1 
ATOM   4857 O OG   . SER B 1 330 ? 138.75500 98.40900  100.07500 1.000 51.57742  ? 330 SER B OG   1 
ATOM   4858 N N    . PHE B 1 331 ? 139.71700 99.39400  103.56000 1.000 54.89490  ? 331 PHE B N    1 
ATOM   4859 C CA   . PHE B 1 331 ? 139.11900 100.34200 104.49600 1.000 56.75955  ? 331 PHE B CA   1 
ATOM   4860 C C    . PHE B 1 331 ? 138.19800 101.32200 103.78000 1.000 60.07470  ? 331 PHE B C    1 
ATOM   4861 O O    . PHE B 1 331 ? 137.07500 101.57600 104.22900 1.000 60.99281  ? 331 PHE B O    1 
ATOM   4862 C CB   . PHE B 1 331 ? 140.21400 101.08500 105.26200 1.000 56.57652  ? 331 PHE B CB   1 
ATOM   4863 C CG   . PHE B 1 331 ? 141.03300 100.20200 106.16000 1.000 59.39720  ? 331 PHE B CG   1 
ATOM   4864 C CD1  . PHE B 1 331 ? 140.60000 98.92600  106.48200 1.000 59.74640  ? 331 PHE B CD1  1 
ATOM   4865 C CD2  . PHE B 1 331 ? 142.23500 100.64600 106.68300 1.000 60.40516  ? 331 PHE B CD2  1 
ATOM   4866 C CE1  . PHE B 1 331 ? 141.35000 98.11100  107.30700 1.000 58.82165  ? 331 PHE B CE1  1 
ATOM   4867 C CE2  . PHE B 1 331 ? 142.99000 99.83500  107.50900 1.000 58.96361  ? 331 PHE B CE2  1 
ATOM   4868 C CZ   . PHE B 1 331 ? 142.54600 98.56600  107.82100 1.000 57.39344  ? 331 PHE B CZ   1 
ATOM   4869 N N    . ASN B 1 332 ? 138.65700 101.88400 102.66400 1.000 48.20047  ? 332 ASN B N    1 
ATOM   4870 C CA   . ASN B 1 332 ? 137.84900 102.78000 101.83800 1.000 46.64389  ? 332 ASN B CA   1 
ATOM   4871 C C    . ASN B 1 332 ? 137.36900 102.00400 100.61700 1.000 47.72265  ? 332 ASN B C    1 
ATOM   4872 O O    . ASN B 1 332 ? 138.11800 101.81600 99.65500  1.000 49.21025  ? 332 ASN B O    1 
ATOM   4873 C CB   . ASN B 1 332 ? 138.64900 104.01500 101.43900 1.000 47.84489  ? 332 ASN B CB   1 
ATOM   4874 C CG   . ASN B 1 332 ? 139.04800 104.86000 102.63200 1.000 51.77663  ? 332 ASN B CG   1 
ATOM   4875 O OD1  . ASN B 1 332 ? 138.26600 105.67700 103.11800 1.000 51.94722  ? 332 ASN B OD1  1 
ATOM   4876 N ND2  . ASN B 1 332 ? 140.27000 104.66600 103.11200 1.000 51.97874  ? 332 ASN B ND2  1 
ATOM   4877 N N    . TYR B 1 333 ? 136.12200 101.55200 100.65600 1.000 28.72863  ? 333 TYR B N    1 
ATOM   4878 C CA   . TYR B 1 333 ? 135.60600 100.80300 99.51600  1.000 31.04278  ? 333 TYR B CA   1 
ATOM   4879 C C    . TYR B 1 333 ? 134.92100 101.75000 98.53600  1.000 34.86377  ? 333 TYR B C    1 
ATOM   4880 O O    . TYR B 1 333 ? 134.09200 102.56800 98.95200  1.000 29.72043  ? 333 TYR B O    1 
ATOM   4881 C CB   . TYR B 1 333 ? 134.63100 99.72600  99.97100  1.000 25.76966  ? 333 TYR B CB   1 
ATOM   4882 C CG   . TYR B 1 333 ? 134.51300 98.57000  99.00500  1.000 25.54672  ? 333 TYR B CG   1 
ATOM   4883 C CD1  . TYR B 1 333 ? 135.56100 97.67600  98.83500  1.000 24.19705  ? 333 TYR B CD1  1 
ATOM   4884 C CD2  . TYR B 1 333 ? 133.35400 98.36800  98.26800  1.000 21.77407  ? 333 TYR B CD2  1 
ATOM   4885 C CE1  . TYR B 1 333 ? 135.46200 96.61900  97.95500  1.000 21.39176  ? 333 TYR B CE1  1 
ATOM   4886 C CE2  . TYR B 1 333 ? 133.24500 97.31200  97.38700  1.000 24.67876  ? 333 TYR B CE2  1 
ATOM   4887 C CZ   . TYR B 1 333 ? 134.30300 96.44000  97.23400  1.000 24.74665  ? 333 TYR B CZ   1 
ATOM   4888 O OH   . TYR B 1 333 ? 134.20100 95.38500  96.35800  1.000 27.57737  ? 333 TYR B OH   1 
ATOM   4889 N N    . PRO B 1 334 ? 135.23600 101.66800 97.24100  1.000 28.10792  ? 334 PRO B N    1 
ATOM   4890 C CA   . PRO B 1 334 ? 134.63300 102.58800 96.26500  1.000 16.98869  ? 334 PRO B CA   1 
ATOM   4891 C C    . PRO B 1 334 ? 133.13800 102.37900 96.07300  1.000 19.82538  ? 334 PRO B C    1 
ATOM   4892 O O    . PRO B 1 334 ? 132.71200 101.78000 95.08200  1.000 29.56746  ? 334 PRO B O    1 
ATOM   4893 C CB   . PRO B 1 334 ? 135.40800 102.28200 94.97700  1.000 25.65498  ? 334 PRO B CB   1 
ATOM   4894 C CG   . PRO B 1 334 ? 135.93200 100.89700 95.17400  1.000 21.44875  ? 334 PRO B CG   1 
ATOM   4895 C CD   . PRO B 1 334 ? 136.26200 100.81000 96.62700  1.000 17.98165  ? 334 PRO B CD   1 
ATOM   4896 N N    . TRP B 1 335 ? 132.33400 102.86800 97.01800  1.000 12.89092  ? 335 TRP B N    1 
ATOM   4897 C CA   . TRP B 1 335 ? 130.88400 102.73700 96.93400  1.000 12.89996  ? 335 TRP B CA   1 
ATOM   4898 C C    . TRP B 1 335 ? 130.25200 103.71700 95.95200  1.000 21.95011  ? 335 TRP B C    1 
ATOM   4899 O O    . TRP B 1 335 ? 129.10200 103.51400 95.55000  1.000 27.33633  ? 335 TRP B O    1 
ATOM   4900 C CB   . TRP B 1 335 ? 130.26000 102.93900 98.31900  1.000 17.19224  ? 335 TRP B CB   1 
ATOM   4901 C CG   . TRP B 1 335 ? 130.54000 101.82800 99.29300  1.000 20.43411  ? 335 TRP B CG   1 
ATOM   4902 C CD1  . TRP B 1 335 ? 131.22100 101.92600 100.47100 1.000 21.19447  ? 335 TRP B CD1  1 
ATOM   4903 C CD2  . TRP B 1 335 ? 130.13500 100.45700 99.17800  1.000 22.26311  ? 335 TRP B CD2  1 
ATOM   4904 N NE1  . TRP B 1 335 ? 131.27300 100.70400 101.09200 1.000 20.67507  ? 335 TRP B NE1  1 
ATOM   4905 C CE2  . TRP B 1 335 ? 130.61300 99.78500  100.32100 1.000 19.38679  ? 335 TRP B CE2  1 
ATOM   4906 C CE3  . TRP B 1 335 ? 129.41900 99.73300  98.22000  1.000 23.79036  ? 335 TRP B CE3  1 
ATOM   4907 C CZ2  . TRP B 1 335 ? 130.39800 98.42500  100.53000 1.000 21.11867  ? 335 TRP B CZ2  1 
ATOM   4908 C CZ3  . TRP B 1 335 ? 129.20700 98.38300  98.43000  1.000 17.02917  ? 335 TRP B CZ3  1 
ATOM   4909 C CH2  . TRP B 1 335 ? 129.69400 97.74400  99.57600  1.000 18.41446  ? 335 TRP B CH2  1 
ATOM   4910 N N    . LYS B 1 336 ? 130.97100 104.77300 95.56400  1.000 25.26304  ? 336 LYS B N    1 
ATOM   4911 C CA   . LYS B 1 336 ? 130.43800 105.76100 94.62800  1.000 24.59603  ? 336 LYS B CA   1 
ATOM   4912 C C    . LYS B 1 336 ? 130.36700 105.24500 93.19100  1.000 24.30739  ? 336 LYS B C    1 
ATOM   4913 O O    . LYS B 1 336 ? 129.51600 105.70000 92.41200  1.000 26.49801  ? 336 LYS B O    1 
ATOM   4914 C CB   . LYS B 1 336 ? 131.28900 107.02700 94.69400  1.000 27.43728  ? 336 LYS B CB   1 
ATOM   4915 C CG   . LYS B 1 336 ? 132.73500 106.80200 94.29100  1.000 25.75133  ? 336 LYS B CG   1 
ATOM   4916 C CD   . LYS B 1 336 ? 133.54800 108.07900 94.37100  1.000 29.12489  ? 336 LYS B CD   1 
ATOM   4917 C CE   . LYS B 1 336 ? 134.99000 107.82800 93.96200  1.000 32.58276  ? 336 LYS B CE   1 
ATOM   4918 N NZ   . LYS B 1 336 ? 135.68600 106.91200 94.90900  1.000 32.37940  ? 336 LYS B NZ   1 
ATOM   4919 N N    . ASN B 1 337 ? 131.22800 104.29500 92.81800  1.000 16.77711  ? 337 ASN B N    1 
ATOM   4920 C CA   . ASN B 1 337 ? 131.18200 103.78000 91.45500  1.000 22.75738  ? 337 ASN B CA   1 
ATOM   4921 C C    . ASN B 1 337 ? 129.92600 102.95800 91.20300  1.000 27.41256  ? 337 ASN B C    1 
ATOM   4922 O O    . ASN B 1 337 ? 129.46900 102.86800 90.05300  1.000 36.88861  ? 337 ASN B O    1 
ATOM   4923 C CB   . ASN B 1 337 ? 132.42900 102.94000 91.18100  1.000 25.46278  ? 337 ASN B CB   1 
ATOM   4924 C CG   . ASN B 1 337 ? 133.64500 103.78800 90.86500  1.000 28.38328  ? 337 ASN B CG   1 
ATOM   4925 O OD1  . ASN B 1 337 ? 133.87900 104.81400 91.50000  1.000 27.73099  ? 337 ASN B OD1  1 
ATOM   4926 N ND2  . ASN B 1 337 ? 134.42600 103.36200 89.88200  1.000 25.26220  ? 337 ASN B ND2  1 
ATOM   4927 N N    . TYR B 1 338 ? 129.28700 102.47600 92.26800  1.000 19.09488  ? 338 TYR B N    1 
ATOM   4928 C CA   . TYR B 1 338 ? 128.02800 101.76100 92.11300  1.000 15.60263  ? 338 TYR B CA   1 
ATOM   4929 C C    . TYR B 1 338 ? 126.91500 102.73500 91.75900  1.000 17.19187  ? 338 TYR B C    1 
ATOM   4930 O O    . TYR B 1 338 ? 126.06500 102.44400 90.90700  1.000 24.69631  ? 338 TYR B O    1 
ATOM   4931 C CB   . TYR B 1 338 ? 127.70100 101.02200 93.41100  1.000 17.39030  ? 338 TYR B CB   1 
ATOM   4932 C CG   . TYR B 1 338 ? 128.41200 99.69800  93.58200  1.000 21.37315  ? 338 TYR B CG   1 
ATOM   4933 C CD1  . TYR B 1 338 ? 129.69200 99.64700  94.11900  1.000 15.64659  ? 338 TYR B CD1  1 
ATOM   4934 C CD2  . TYR B 1 338 ? 127.80400 98.50200  93.22900  1.000 19.06433  ? 338 TYR B CD2  1 
ATOM   4935 C CE1  . TYR B 1 338 ? 130.35100 98.44900  94.28800  1.000 13.49111  ? 338 TYR B CE1  1 
ATOM   4936 C CE2  . TYR B 1 338 ? 128.45800 97.29400  93.39500  1.000 15.18710  ? 338 TYR B CE2  1 
ATOM   4937 C CZ   . TYR B 1 338 ? 129.73200 97.27500  93.92500  1.000 20.49956  ? 338 TYR B CZ   1 
ATOM   4938 O OH   . TYR B 1 338 ? 130.39100 96.08000  94.09400  1.000 19.55603  ? 338 TYR B OH   1 
ATOM   4939 N N    . VAL B 1 339 ? 126.95500 103.93200 92.34800  1.000 12.15584  ? 339 VAL B N    1 
ATOM   4940 C CA   . VAL B 1 339 ? 125.97500 104.95800 92.01900  1.000 17.84244  ? 339 VAL B CA   1 
ATOM   4941 C C    . VAL B 1 339 ? 126.24300 105.52300 90.63200  1.000 15.33499  ? 339 VAL B C    1 
ATOM   4942 O O    . VAL B 1 339 ? 125.30500 105.88100 89.90800  1.000 26.79258  ? 339 VAL B O    1 
ATOM   4943 C CB   . VAL B 1 339 ? 125.98800 106.06200 93.09300  1.000 18.58716  ? 339 VAL B CB   1 
ATOM   4944 C CG1  . VAL B 1 339 ? 124.71700 106.89100 93.02300  1.000 20.69337  ? 339 VAL B CG1  1 
ATOM   4945 C CG2  . VAL B 1 339 ? 126.15900 105.45600 94.47500  1.000 16.31281  ? 339 VAL B CG2  1 
ATOM   4946 N N    . LYS B 1 340 ? 127.51000 105.57100 90.21300  1.000 7.89985   ? 340 LYS B N    1 
ATOM   4947 C CA   . LYS B 1 340 ? 127.80100 106.05900 88.86700  1.000 11.60764  ? 340 LYS B CA   1 
ATOM   4948 C C    . LYS B 1 340 ? 127.28900 105.08600 87.80800  1.000 15.04319  ? 340 LYS B C    1 
ATOM   4949 O O    . LYS B 1 340 ? 126.72100 105.50200 86.78200  1.000 23.33524  ? 340 LYS B O    1 
ATOM   4950 C CB   . LYS B 1 340 ? 129.30600 106.28000 88.71900  1.000 9.91475   ? 340 LYS B CB   1 
ATOM   4951 C CG   . LYS B 1 340 ? 129.69400 107.58300 88.04700  1.000 19.27717  ? 340 LYS B CG   1 
ATOM   4952 C CD   . LYS B 1 340 ? 131.10100 107.50900 87.48100  1.000 17.00111  ? 340 LYS B CD   1 
ATOM   4953 C CE   . LYS B 1 340 ? 131.17800 106.55700 86.30300  1.000 21.85796  ? 340 LYS B CE   1 
ATOM   4954 N NZ   . LYS B 1 340 ? 130.44400 107.08500 85.12100  1.000 18.88404  ? 340 LYS B NZ   1 
ATOM   4955 N N    . LEU B 1 341 ? 127.38500 103.78300 88.08600  1.000 7.44302   ? 341 LEU B N    1 
ATOM   4956 C CA   . LEU B 1 341 ? 126.84300 102.81800 87.13700  1.000 12.31370  ? 341 LEU B CA   1 
ATOM   4957 C C    . LEU B 1 341 ? 125.31600 102.81400 87.16300  1.000 11.23936  ? 341 LEU B C    1 
ATOM   4958 O O    . LEU B 1 341 ? 124.67600 102.67600 86.10900  1.000 14.53984  ? 341 LEU B O    1 
ATOM   4959 C CB   . LEU B 1 341 ? 127.40500 101.42800 87.43800  1.000 14.37909  ? 341 LEU B CB   1 
ATOM   4960 C CG   . LEU B 1 341 ? 127.01900 100.26500 86.52400  1.000 15.03884  ? 341 LEU B CG   1 
ATOM   4961 C CD1  . LEU B 1 341 ? 127.55800 100.48600 85.12200  1.000 7.78482   ? 341 LEU B CD1  1 
ATOM   4962 C CD2  . LEU B 1 341 ? 127.53600 98.95700  87.09300  1.000 9.86707   ? 341 LEU B CD2  1 
ATOM   4963 N N    . SER B 1 342 ? 124.71300 103.01900 88.33800  1.000 9.41405   ? 342 SER B N    1 
ATOM   4964 C CA   . SER B 1 342 ? 123.25800 103.12300 88.39000  1.000 15.11929  ? 342 SER B CA   1 
ATOM   4965 C C    . SER B 1 342 ? 122.75500 104.35300 87.64300  1.000 16.96924  ? 342 SER B C    1 
ATOM   4966 O O    . SER B 1 342 ? 121.67600 104.31400 87.03800  1.000 20.64529  ? 342 SER B O    1 
ATOM   4967 C CB   . SER B 1 342 ? 122.78200 103.15300 89.84200  1.000 12.89816  ? 342 SER B CB   1 
ATOM   4968 O OG   . SER B 1 342 ? 123.06500 101.93200 90.49700  1.000 18.92053  ? 342 SER B OG   1 
ATOM   4969 N N    . GLY B 1 343 ? 123.53600 105.43500 87.62400  1.000 8.91590   ? 343 GLY B N    1 
ATOM   4970 C CA   . GLY B 1 343 ? 123.10700 106.61100 86.88500  1.000 3.19667   ? 343 GLY B CA   1 
ATOM   4971 C C    . GLY B 1 343 ? 123.21900 106.41700 85.38500  1.000 11.98689  ? 343 GLY B C    1 
ATOM   4972 O O    . GLY B 1 343 ? 122.34400 106.85100 84.62200  1.000 18.03075  ? 343 GLY B O    1 
ATOM   4973 N N    . ALA B 1 344 ? 124.27300 105.72600 84.94000  1.000 7.10358   ? 344 ALA B N    1 
ATOM   4974 C CA   . ALA B 1 344 ? 124.34600 105.40000 83.51800  1.000 4.29257   ? 344 ALA B CA   1 
ATOM   4975 C C    . ALA B 1 344 ? 123.17800 104.50600 83.10700  1.000 13.70988  ? 344 ALA B C    1 
ATOM   4976 O O    . ALA B 1 344 ? 122.59200 104.67600 82.02300  1.000 16.25426  ? 344 ALA B O    1 
ATOM   4977 C CB   . ALA B 1 344 ? 125.68200 104.73100 83.19800  1.000 5.85565   ? 344 ALA B CB   1 
ATOM   4978 N N    . LEU B 1 345 ? 122.76400 103.59900 83.99700  1.000 14.43947  ? 345 LEU B N    1 
ATOM   4979 C CA   . LEU B 1 345 ? 121.63800 102.73700 83.65400  1.000 13.28452  ? 345 LEU B CA   1 
ATOM   4980 C C    . LEU B 1 345 ? 120.31100 103.48900 83.67800  1.000 14.06925  ? 345 LEU B C    1 
ATOM   4981 O O    . LEU B 1 345 ? 119.40500 103.15600 82.90800  1.000 18.94961  ? 345 LEU B O    1 
ATOM   4982 C CB   . LEU B 1 345 ? 121.58900 101.54000 84.60300  1.000 13.93823  ? 345 LEU B CB   1 
ATOM   4983 C CG   . LEU B 1 345 ? 120.64400 100.40000 84.22000  1.000 12.99053  ? 345 LEU B CG   1 
ATOM   4984 C CD1  . LEU B 1 345 ? 121.16900 99.63900  83.01500  1.000 15.38615  ? 345 LEU B CD1  1 
ATOM   4985 C CD2  . LEU B 1 345 ? 120.44300 99.46600  85.39700  1.000 14.05407  ? 345 LEU B CD2  1 
ATOM   4986 N N    . LYS B 1 346 ? 120.17400 104.51400 84.52300  1.000 11.61200  ? 346 LYS B N    1 
ATOM   4987 C CA   . LYS B 1 346 ? 118.94300 105.30300 84.49300  1.000 11.26007  ? 346 LYS B CA   1 
ATOM   4988 C C    . LYS B 1 346 ? 118.85200 106.11600 83.20500  1.000 13.84944  ? 346 LYS B C    1 
ATOM   4989 O O    . LYS B 1 346 ? 117.76900 106.24300 82.59800  1.000 10.32045  ? 346 LYS B O    1 
ATOM   4990 C CB   . LYS B 1 346 ? 118.88900 106.22300 85.71000  1.000 12.49640  ? 346 LYS B CB   1 
ATOM   4991 C CG   . LYS B 1 346 ? 118.36600 105.55700 86.96500  1.000 23.04990  ? 346 LYS B CG   1 
ATOM   4992 C CD   . LYS B 1 346 ? 118.39300 106.51100 88.14500  1.000 26.79125  ? 346 LYS B CD   1 
ATOM   4993 C CE   . LYS B 1 346 ? 118.41900 105.75200 89.46300  1.000 24.26514  ? 346 LYS B CE   1 
ATOM   4994 N NZ   . LYS B 1 346 ? 118.40200 104.27800 89.25700  1.000 17.98618  ? 346 LYS B NZ   1 
ATOM   4995 N N    . HIS B 1 347 ? 119.99500 106.63400 82.74800  1.000 16.67850  ? 347 HIS B N    1 
ATOM   4996 C CA   . HIS B 1 347 ? 120.00700 107.34100 81.47500  1.000 12.87851  ? 347 HIS B CA   1 
ATOM   4997 C C    . HIS B 1 347 ? 119.61300 106.40900 80.34100  1.000 13.75791  ? 347 HIS B C    1 
ATOM   4998 O O    . HIS B 1 347 ? 118.92000 106.81700 79.40200  1.000 9.11757   ? 347 HIS B O    1 
ATOM   4999 C CB   . HIS B 1 347 ? 121.38100 107.95100 81.20600  1.000 10.55076  ? 347 HIS B CB   1 
ATOM   5000 C CG   . HIS B 1 347 ? 121.36200 109.03100 80.16900  1.000 16.78837  ? 347 HIS B CG   1 
ATOM   5001 N ND1  . HIS B 1 347 ? 122.11800 108.97100 79.01800  1.000 15.66608  ? 347 HIS B ND1  1 
ATOM   5002 C CD2  . HIS B 1 347 ? 120.66900 110.19200 80.10300  1.000 19.15188  ? 347 HIS B CD2  1 
ATOM   5003 C CE1  . HIS B 1 347 ? 121.89500 110.05000 78.29100  1.000 17.25775  ? 347 HIS B CE1  1 
ATOM   5004 N NE2  . HIS B 1 347 ? 121.02100 110.80800 78.92700  1.000 17.60928  ? 347 HIS B NE2  1 
ATOM   5005 N N    . CYS B 1 348 ? 120.04400 105.14800 80.41100  1.000 17.16884  ? 348 CYS B N    1 
ATOM   5006 C CA   . CYS B 1 348 ? 119.61000 104.19800 79.39000  1.000 16.83462  ? 348 CYS B CA   1 
ATOM   5007 C C    . CYS B 1 348 ? 118.12600 103.84200 79.51800  1.000 22.42956  ? 348 CYS B C    1 
ATOM   5008 O O    . CYS B 1 348 ? 117.45700 103.62700 78.50100  1.000 20.56730  ? 348 CYS B O    1 
ATOM   5009 C CB   . CYS B 1 348 ? 120.47400 102.93900 79.45700  1.000 20.45376  ? 348 CYS B CB   1 
ATOM   5010 S SG   . CYS B 1 348 ? 120.11500 101.70600 78.19600  1.000 34.61401  ? 348 CYS B SG   1 
ATOM   5011 N N    . ALA B 1 349 ? 117.59100 103.78000 80.74300  1.000 24.41544  ? 349 ALA B N    1 
ATOM   5012 C CA   . ALA B 1 349 ? 116.19000 103.41500 80.96300  1.000 14.14762  ? 349 ALA B CA   1 
ATOM   5013 C C    . ALA B 1 349 ? 115.19200 104.51100 80.59600  1.000 21.63335  ? 349 ALA B C    1 
ATOM   5014 O O    . ALA B 1 349 ? 113.99100 104.22100 80.46200  1.000 25.78181  ? 349 ALA B O    1 
ATOM   5015 C CB   . ALA B 1 349 ? 115.98000 103.01000 82.42300  1.000 12.56030  ? 349 ALA B CB   1 
ATOM   5016 N N    . PHE B 1 350 ? 115.64200 105.74900 80.38900  1.000 19.62636  ? 350 PHE B N    1 
ATOM   5017 C CA   . PHE B 1 350 ? 114.66400 106.76000 79.97700  1.000 14.19253  ? 350 PHE B CA   1 
ATOM   5018 C C    . PHE B 1 350 ? 114.14100 106.51600 78.55800  1.000 20.82073  ? 350 PHE B C    1 
ATOM   5019 O O    . PHE B 1 350 ? 112.95400 106.75700 78.28200  1.000 17.43213  ? 350 PHE B O    1 
ATOM   5020 C CB   . PHE B 1 350 ? 115.26900 108.16100 80.07200  1.000 20.18504  ? 350 PHE B CB   1 
ATOM   5021 C CG   . PHE B 1 350 ? 115.29300 108.72100 81.46400  1.000 20.93718  ? 350 PHE B CG   1 
ATOM   5022 C CD1  . PHE B 1 350 ? 114.20100 108.57900 82.30200  1.000 21.81771  ? 350 PHE B CD1  1 
ATOM   5023 C CD2  . PHE B 1 350 ? 116.40300 109.40300 81.93100  1.000 22.31559  ? 350 PHE B CD2  1 
ATOM   5024 C CE1  . PHE B 1 350 ? 114.22000 109.09700 83.58100  1.000 18.87165  ? 350 PHE B CE1  1 
ATOM   5025 C CE2  . PHE B 1 350 ? 116.42600 109.92300 83.21000  1.000 19.99010  ? 350 PHE B CE2  1 
ATOM   5026 C CZ   . PHE B 1 350 ? 115.33200 109.77000 84.03500  1.000 14.40955  ? 350 PHE B CZ   1 
ATOM   5027 N N    . THR B 1 351 ? 114.97700 105.99600 77.65700  1.000 12.76015  ? 351 THR B N    1 
ATOM   5028 C CA   . THR B 1 351 ? 114.47200 105.65800 76.33000  1.000 10.47784  ? 351 THR B CA   1 
ATOM   5029 C C    . THR B 1 351 ? 113.48500 104.49800 76.39000  1.000 11.21932  ? 351 THR B C    1 
ATOM   5030 O O    . THR B 1 351 ? 112.55100 104.43400 75.58200  1.000 13.58804  ? 351 THR B O    1 
ATOM   5031 C CB   . THR B 1 351 ? 115.62800 105.32300 75.38800  1.000 17.64482  ? 351 THR B CB   1 
ATOM   5032 O OG1  . THR B 1 351 ? 116.72600 106.20700 75.64300  1.000 20.20526  ? 351 THR B OG1  1 
ATOM   5033 C CG2  . THR B 1 351 ? 115.19400 105.47700 73.93900  1.000 14.15622  ? 351 THR B CG2  1 
ATOM   5034 N N    . VAL B 1 352 ? 113.64800 103.59500 77.35900  1.000 20.61153  ? 352 VAL B N    1 
ATOM   5035 C CA   . VAL B 1 352 ? 112.69400 102.50200 77.49600  1.000 21.52013  ? 352 VAL B CA   1 
ATOM   5036 C C    . VAL B 1 352 ? 111.37000 103.03200 78.02000  1.000 12.73831  ? 352 VAL B C    1 
ATOM   5037 O O    . VAL B 1 352 ? 110.29700 102.56000 77.61900  1.000 19.29307  ? 352 VAL B O    1 
ATOM   5038 C CB   . VAL B 1 352 ? 113.26300 101.39800 78.40600  1.000 21.59294  ? 352 VAL B CB   1 
ATOM   5039 C CG1  . VAL B 1 352 ? 112.36200 100.17400 78.38500  1.000 14.08459  ? 352 VAL B CG1  1 
ATOM   5040 C CG2  . VAL B 1 352 ? 114.67500 101.03400 77.97700  1.000 18.79062  ? 352 VAL B CG2  1 
ATOM   5041 N N    . MET B 1 353 ? 111.41500 104.04100 78.89300  1.000 21.03727  ? 353 MET B N    1 
ATOM   5042 C CA   . MET B 1 353 ? 110.16200 104.66400 79.31000  1.000 17.11075  ? 353 MET B CA   1 
ATOM   5043 C C    . MET B 1 353 ? 109.47800 105.38000 78.14800  1.000 21.83654  ? 353 MET B C    1 
ATOM   5044 O O    . MET B 1 353 ? 108.24400 105.36100 78.04600  1.000 19.96215  ? 353 MET B O    1 
ATOM   5045 C CB   . MET B 1 353 ? 110.41300 105.64300 80.45400  1.000 17.91687  ? 353 MET B CB   1 
ATOM   5046 C CG   . MET B 1 353 ? 109.25900 106.59500 80.71500  1.000 23.05826  ? 353 MET B CG   1 
ATOM   5047 S SD   . MET B 1 353 ? 109.25300 107.25100 82.39100  1.000 47.63659  ? 353 MET B SD   1 
ATOM   5048 C CE   . MET B 1 353 ? 110.82000 108.11600 82.41900  1.000 29.03477  ? 353 MET B CE   1 
ATOM   5049 N N    . ALA B 1 354 ? 110.25400 105.94300 77.21900  1.000 26.31889  ? 354 ALA B N    1 
ATOM   5050 C CA   . ALA B 1 354 ? 109.61600 106.59700 76.07800  1.000 11.54794  ? 354 ALA B CA   1 
ATOM   5051 C C    . ALA B 1 354 ? 109.08600 105.58600 75.06400  1.000 17.69841  ? 354 ALA B C    1 
ATOM   5052 O O    . ALA B 1 354 ? 108.06700 105.84000 74.40300  1.000 16.08767  ? 354 ALA B O    1 
ATOM   5053 C CB   . ALA B 1 354 ? 110.59500 107.55800 75.40400  1.000 13.17158  ? 354 ALA B CB   1 
ATOM   5054 N N    . LEU B 1 355 ? 109.68600 104.39700 75.00400  1.000 19.55582  ? 355 LEU B N    1 
ATOM   5055 C CA   . LEU B 1 355 ? 109.13600 103.37200 74.12700  1.000 15.62579  ? 355 LEU B CA   1 
ATOM   5056 C C    . LEU B 1 355 ? 107.88300 102.75800 74.72700  1.000 15.94650  ? 355 LEU B C    1 
ATOM   5057 O O    . LEU B 1 355 ? 106.98100 102.35300 73.98700  1.000 14.17557  ? 355 LEU B O    1 
ATOM   5058 C CB   . LEU B 1 355 ? 110.17400 102.28400 73.84600  1.000 20.06832  ? 355 LEU B CB   1 
ATOM   5059 C CG   . LEU B 1 355 ? 111.29800 102.64200 72.87500  1.000 22.45965  ? 355 LEU B CG   1 
ATOM   5060 C CD1  . LEU B 1 355 ? 112.50600 101.75100 73.09900  1.000 17.35888  ? 355 LEU B CD1  1 
ATOM   5061 C CD2  . LEU B 1 355 ? 110.80600 102.53500 71.44000  1.000 15.54130  ? 355 LEU B CD2  1 
ATOM   5062 N N    . HIS B 1 356 ? 107.80700 102.67800 76.05700  1.000 27.79890  ? 356 HIS B N    1 
ATOM   5063 C CA   . HIS B 1 356 ? 106.55100 102.27500 76.67800  1.000 23.03960  ? 356 HIS B CA   1 
ATOM   5064 C C    . HIS B 1 356 ? 105.47000 103.32100 76.44100  1.000 26.17801  ? 356 HIS B C    1 
ATOM   5065 O O    . HIS B 1 356 ? 104.30400 102.97700 76.21300  1.000 31.00336  ? 356 HIS B O    1 
ATOM   5066 C CB   . HIS B 1 356 ? 106.73800 102.04400 78.17600  1.000 27.65661  ? 356 HIS B CB   1 
ATOM   5067 C CG   . HIS B 1 356 ? 105.48400 101.61900 78.87600  1.000 31.11578  ? 356 HIS B CG   1 
ATOM   5068 N ND1  . HIS B 1 356 ? 105.19500 101.98400 80.17300  1.000 31.68261  ? 356 HIS B ND1  1 
ATOM   5069 C CD2  . HIS B 1 356 ? 104.43700 100.87000 78.45500  1.000 30.07844  ? 356 HIS B CD2  1 
ATOM   5070 C CE1  . HIS B 1 356 ? 104.02700 101.47500 80.52200  1.000 31.40677  ? 356 HIS B CE1  1 
ATOM   5071 N NE2  . HIS B 1 356 ? 103.54700 100.79400 79.49700  1.000 27.78084  ? 356 HIS B NE2  1 
ATOM   5072 N N    . GLY B 1 357 ? 105.83800 104.60400 76.48700  1.000 23.89140  ? 357 GLY B N    1 
ATOM   5073 C CA   . GLY B 1 357 ? 104.87100 105.64800 76.19400  1.000 17.11051  ? 357 GLY B CA   1 
ATOM   5074 C C    . GLY B 1 357 ? 104.37900 105.64200 74.76000  1.000 22.65995  ? 357 GLY B C    1 
ATOM   5075 O O    . GLY B 1 357 ? 103.25400 106.07100 74.48800  1.000 22.29213  ? 357 GLY B O    1 
ATOM   5076 N N    . CYS B 1 358 ? 105.20300 105.16200 73.82600  1.000 37.77422  ? 358 CYS B N    1 
ATOM   5077 C CA   . CYS B 1 358 ? 104.75300 105.06500 72.43700  1.000 26.04701  ? 358 CYS B CA   1 
ATOM   5078 C C    . CYS B 1 358 ? 103.59200 104.09000 72.25100  1.000 24.41973  ? 358 CYS B C    1 
ATOM   5079 O O    . CYS B 1 358 ? 102.86400 104.19700 71.25900  1.000 26.64921  ? 358 CYS B O    1 
ATOM   5080 C CB   . CYS B 1 358 ? 105.90700 104.64700 71.52400  1.000 26.98511  ? 358 CYS B CB   1 
ATOM   5081 S SG   . CYS B 1 358 ? 106.96300 105.99500 70.96000  1.000 40.77393  ? 358 CYS B SG   1 
ATOM   5082 N N    . ILE B 1 359 ? 103.40300 103.14300 73.17200  1.000 30.47623  ? 359 ILE B N    1 
ATOM   5083 C CA   . ILE B 1 359 ? 102.31500 102.17400 73.04800  1.000 29.49723  ? 359 ILE B CA   1 
ATOM   5084 C C    . ILE B 1 359 ? 100.98200 102.69000 73.58300  1.000 30.93180  ? 359 ILE B C    1 
ATOM   5085 O O    . ILE B 1 359 ? 99.93600  102.10200 73.27900  1.000 27.85052  ? 359 ILE B O    1 
ATOM   5086 C CB   . ILE B 1 359 ? 102.68500 100.85700 73.75100  1.000 32.90500  ? 359 ILE B CB   1 
ATOM   5087 C CG1  . ILE B 1 359 ? 103.94400 100.25000 73.12700  1.000 30.65503  ? 359 ILE B CG1  1 
ATOM   5088 C CG2  . ILE B 1 359 ? 101.53500 99.86500  73.69200  1.000 29.00813  ? 359 ILE B CG2  1 
ATOM   5089 C CD1  . ILE B 1 359 ? 104.50200 99.07700  73.90100  1.000 24.65854  ? 359 ILE B CD1  1 
ATOM   5090 N N    . LEU B 1 360 ? 100.97900 103.77300 74.35800  1.000 35.23253  ? 360 LEU B N    1 
ATOM   5091 C CA   . LEU B 1 360 ? 99.76500  104.31000 74.96200  1.000 28.99626  ? 360 LEU B CA   1 
ATOM   5092 C C    . LEU B 1 360 ? 99.35700  105.64200 74.34100  1.000 27.97031  ? 360 LEU B C    1 
ATOM   5093 O O    . LEU B 1 360 ? 98.74500  106.48100 75.00600  1.000 31.62711  ? 360 LEU B O    1 
ATOM   5094 C CB   . LEU B 1 360 ? 99.94800  104.47200 76.47100  1.000 31.05338  ? 360 LEU B CB   1 
ATOM   5095 C CG   . LEU B 1 360 ? 100.26100 103.22200 77.29400  1.000 31.45724  ? 360 LEU B CG   1 
ATOM   5096 C CD1  . LEU B 1 360 ? 100.74600 103.61100 78.68100  1.000 26.57721  ? 360 LEU B CD1  1 
ATOM   5097 C CD2  . LEU B 1 360 ? 99.04300  102.31900 77.38100  1.000 29.28808  ? 360 LEU B CD2  1 
ATOM   5098 N N    . SER B 1 361 ? 99.67900  105.84400 73.07000  1.000 36.08698  ? 361 SER B N    1 
ATOM   5099 C CA   . SER B 1 361 ? 99.39000  107.09600 72.39000  1.000 36.31911  ? 361 SER B CA   1 
ATOM   5100 C C    . SER B 1 361 ? 98.05300  107.03500 71.66000  1.000 35.87352  ? 361 SER B C    1 
ATOM   5101 O O    . SER B 1 361 ? 97.54000  105.96300 71.32900  1.000 39.17620  ? 361 SER B O    1 
ATOM   5102 C CB   . SER B 1 361 ? 100.50500 107.43500 71.40200  1.000 37.95657  ? 361 SER B CB   1 
ATOM   5103 O OG   . SER B 1 361 ? 101.71100 107.74100 72.07900  1.000 39.16568  ? 361 SER B OG   1 
ATOM   5104 N N    . GLU B 1 362 ? 97.48700  108.21900 71.41300  1.000 44.67225  ? 362 GLU B N    1 
ATOM   5105 C CA   . GLU B 1 362 ? 96.19200  108.30700 70.74600  1.000 43.22785  ? 362 GLU B CA   1 
ATOM   5106 C C    . GLU B 1 362 ? 96.30200  108.01400 69.25600  1.000 45.73772  ? 362 GLU B C    1 
ATOM   5107 O O    . GLU B 1 362 ? 95.38000  107.43500 68.67000  1.000 46.78121  ? 362 GLU B O    1 
ATOM   5108 C CB   . GLU B 1 362 ? 95.58700  109.69400 70.96000  1.000 43.47238  ? 362 GLU B CB   1 
ATOM   5109 C CG   . GLU B 1 362 ? 95.57400  110.15000 72.40700  1.000 44.22232  ? 362 GLU B CG   1 
ATOM   5110 C CD   . GLU B 1 362 ? 94.20200  110.05700 73.03500  1.000 47.22914  ? 362 GLU B CD   1 
ATOM   5111 O OE1  . GLU B 1 362 ? 94.11400  110.12200 74.27900  1.000 46.22181  ? 362 GLU B OE1  1 
ATOM   5112 O OE2  . GLU B 1 362 ? 93.21100  109.91800 72.28900  1.000 50.76399  ? 362 GLU B OE2  1 
ATOM   5113 N N    . ILE B 1 363 ? 97.40700  108.40700 68.63100  1.000 46.15804  ? 363 ILE B N    1 
ATOM   5114 C CA   . ILE B 1 363 ? 97.66600  108.14200 67.22100  1.000 44.23490  ? 363 ILE B CA   1 
ATOM   5115 C C    . ILE B 1 363 ? 98.50200  106.87500 67.10800  1.000 44.84481  ? 363 ILE B C    1 
ATOM   5116 O O    . ILE B 1 363 ? 99.58900  106.78400 67.69100  1.000 44.73265  ? 363 ILE B O    1 
ATOM   5117 C CB   . ILE B 1 363 ? 98.36900  109.33200 66.54900  1.000 44.31668  ? 363 ILE B CB   1 
ATOM   5118 C CG1  . ILE B 1 363 ? 97.51800  110.59600 66.68100  1.000 43.71455  ? 363 ILE B CG1  1 
ATOM   5119 C CG2  . ILE B 1 363 ? 98.65200  109.02700 65.08900  1.000 42.60402  ? 363 ILE B CG2  1 
ATOM   5120 C CD1  . ILE B 1 363 ? 98.21900  111.74000 67.37500  1.000 42.41431  ? 363 ILE B CD1  1 
ATOM   5121 N N    . GLN B 1 364 ? 97.99300  105.89500 66.36400  1.000 48.38995  ? 364 GLN B N    1 
ATOM   5122 C CA   . GLN B 1 364 ? 98.66600  104.61900 66.17400  1.000 44.33409  ? 364 GLN B CA   1 
ATOM   5123 C C    . GLN B 1 364 ? 98.70200  104.28300 64.68900  1.000 44.85343  ? 364 GLN B C    1 
ATOM   5124 O O    . GLN B 1 364 ? 97.92000  104.80800 63.89300  1.000 48.05713  ? 364 GLN B O    1 
ATOM   5125 C CB   . GLN B 1 364 ? 97.97100  103.49400 66.95300  1.000 42.83039  ? 364 GLN B CB   1 
ATOM   5126 C CG   . GLN B 1 364 ? 97.53100  103.89100 68.35100  1.000 46.50152  ? 364 GLN B CG   1 
ATOM   5127 C CD   . GLN B 1 364 ? 98.27600  103.14100 69.43600  1.000 46.69882  ? 364 GLN B CD   1 
ATOM   5128 O OE1  . GLN B 1 364 ? 99.21400  102.39600 69.15900  1.000 49.22785  ? 364 GLN B OE1  1 
ATOM   5129 N NE2  . GLN B 1 364 ? 97.86100  103.33600 70.68100  1.000 45.08697  ? 364 GLN B NE2  1 
ATOM   5130 N N    . ALA B 1 365 ? 99.63100  103.38700 64.32100  1.000 47.25985  ? 365 ALA B N    1 
ATOM   5131 C CA   . ALA B 1 365 ? 99.83000  103.05300 62.92000  1.000 46.48803  ? 365 ALA B CA   1 
ATOM   5132 C C    . ALA B 1 365 ? 99.01700  101.82500 62.52000  1.000 49.04156  ? 365 ALA B C    1 
ATOM   5133 O O    . ALA B 1 365 ? 98.68200  100.98900 63.36500  1.000 47.71794  ? 365 ALA B O    1 
ATOM   5134 C CB   . ALA B 1 365 ? 101.30700 102.79900 62.63800  1.000 44.13791  ? 365 ALA B CB   1 
ATOM   5135 N N    . PRO B 1 366 ? 98.68900  101.71100 61.23300  1.000 54.82413  ? 366 PRO B N    1 
ATOM   5136 C CA   . PRO B 1 366 ? 97.97300  100.52100 60.75500  1.000 54.16828  ? 366 PRO B CA   1 
ATOM   5137 C C    . PRO B 1 366 ? 98.74500  99.24600  61.06200  1.000 55.10745  ? 366 PRO B C    1 
ATOM   5138 O O    . PRO B 1 366 ? 99.96900  99.18800  60.92500  1.000 57.11523  ? 366 PRO B O    1 
ATOM   5139 C CB   . PRO B 1 366 ? 97.85200  100.75900 59.24400  1.000 51.94825  ? 366 PRO B CB   1 
ATOM   5140 C CG   . PRO B 1 366 ? 98.80000  101.88200 58.93500  1.000 53.13667  ? 366 PRO B CG   1 
ATOM   5141 C CD   . PRO B 1 366 ? 98.87100  102.70900 60.17000  1.000 52.43251  ? 366 PRO B CD   1 
ATOM   5142 N N    . GLU B 1 367 ? 98.00900  98.21400  61.48100  1.000 56.29793  ? 367 GLU B N    1 
ATOM   5143 C CA   . GLU B 1 367 ? 98.64400  96.97000  61.90200  1.000 57.93704  ? 367 GLU B CA   1 
ATOM   5144 C C    . GLU B 1 367 ? 99.37300  96.28900  60.74900  1.000 59.21190  ? 367 GLU B C    1 
ATOM   5145 O O    . GLU B 1 367 ? 100.44300 95.70100  60.94400  1.000 56.46363  ? 367 GLU B O    1 
ATOM   5146 C CB   . GLU B 1 367 ? 97.60100  96.02600  62.49900  1.000 57.55842  ? 367 GLU B CB   1 
ATOM   5147 C CG   . GLU B 1 367 ? 98.14100  94.65100  62.85200  1.000 58.18822  ? 367 GLU B CG   1 
ATOM   5148 C CD   . GLU B 1 367 ? 97.08500  93.74600  63.45500  1.000 60.51999  ? 367 GLU B CD   1 
ATOM   5149 O OE1  . GLU B 1 367 ? 95.99100  94.24700  63.78900  1.000 61.24995  ? 367 GLU B OE1  1 
ATOM   5150 O OE2  . GLU B 1 367 ? 97.34900  92.53300  63.59300  1.000 59.11968  ? 367 GLU B OE2  1 
ATOM   5151 N N    . GLU B 1 368 ? 98.81100  96.35400  59.54100  1.000 59.16077  ? 368 GLU B N    1 
ATOM   5152 C CA   . GLU B 1 368 ? 99.42400  95.67500  58.40500  1.000 57.25639  ? 368 GLU B CA   1 
ATOM   5153 C C    . GLU B 1 368 ? 100.78300 96.25400  58.03500  1.000 57.93603  ? 368 GLU B C    1 
ATOM   5154 O O    . GLU B 1 368 ? 101.58900 95.55400  57.41300  1.000 58.18180  ? 368 GLU B O    1 
ATOM   5155 C CB   . GLU B 1 368 ? 98.49000  95.72900  57.19500  1.000 57.32744  ? 368 GLU B CB   1 
ATOM   5156 C CG   . GLU B 1 368 ? 98.53800  97.03900  56.43100  1.000 58.37817  ? 368 GLU B CG   1 
ATOM   5157 C CD   . GLU B 1 368 ? 97.55500  98.06000  56.96600  1.000 59.03335  ? 368 GLU B CD   1 
ATOM   5158 O OE1  . GLU B 1 368 ? 96.66900  97.67500  57.75800  1.000 58.23335  ? 368 GLU B OE1  1 
ATOM   5159 O OE2  . GLU B 1 368 ? 97.67000  99.24700  56.59800  1.000 58.38540  ? 368 GLU B OE2  1 
ATOM   5160 N N    . ARG B 1 369 ? 101.05700 97.50700  58.39600  1.000 54.31098  ? 369 ARG B N    1 
ATOM   5161 C CA   . ARG B 1 369 ? 102.33400 98.13000  58.07200  1.000 53.53081  ? 369 ARG B CA   1 
ATOM   5162 C C    . ARG B 1 369 ? 103.41100 97.87000  59.11600  1.000 53.46282  ? 369 ARG B C    1 
ATOM   5163 O O    . ARG B 1 369 ? 104.59900 98.03000  58.81200  1.000 52.15013  ? 369 ARG B O    1 
ATOM   5164 C CB   . ARG B 1 369 ? 102.15500 99.63900  57.88300  1.000 51.20628  ? 369 ARG B CB   1 
ATOM   5165 C CG   . ARG B 1 369 ? 101.24200 99.99800  56.72600  1.000 51.94243  ? 369 ARG B CG   1 
ATOM   5166 C CD   . ARG B 1 369 ? 101.58400 101.35400 56.13600  1.000 52.90926  ? 369 ARG B CD   1 
ATOM   5167 N NE   . ARG B 1 369 ? 100.38600 102.11000 55.79300  1.000 56.04793  ? 369 ARG B NE   1 
ATOM   5168 C CZ   . ARG B 1 369 ? 100.39000 103.27600 55.16200  1.000 55.53200  ? 369 ARG B CZ   1 
ATOM   5169 N NH1  . ARG B 1 369 ? 101.51800 103.85600 54.78800  1.000 52.86223  ? 369 ARG B NH1  1 
ATOM   5170 N NH2  . ARG B 1 369 ? 99.23200  103.87500 54.90000  1.000 53.37579  ? 369 ARG B NH2  1 
ATOM   5171 N N    . ARG B 1 370 ? 103.03100 97.47500  60.33100  1.000 42.34319  ? 370 ARG B N    1 
ATOM   5172 C CA   . ARG B 1 370 ? 103.99800 97.17200  61.37800  1.000 43.26166  ? 370 ARG B CA   1 
ATOM   5173 C C    . ARG B 1 370 ? 104.62700 95.79400  61.22800  1.000 44.72604  ? 370 ARG B C    1 
ATOM   5174 O O    . ARG B 1 370 ? 105.60800 95.50300  61.92000  1.000 46.32778  ? 370 ARG B O    1 
ATOM   5175 C CB   . ARG B 1 370 ? 103.34100 97.28200  62.75700  1.000 43.84749  ? 370 ARG B CB   1 
ATOM   5176 C CG   . ARG B 1 370 ? 103.06700 98.70800  63.20600  1.000 42.64274  ? 370 ARG B CG   1 
ATOM   5177 C CD   . ARG B 1 370 ? 101.70300 98.83300  63.86600  1.000 40.13917  ? 370 ARG B CD   1 
ATOM   5178 N NE   . ARG B 1 370 ? 101.70800 98.32700  65.23300  1.000 43.03681  ? 370 ARG B NE   1 
ATOM   5179 C CZ   . ARG B 1 370 ? 101.17000 98.95800  66.26800  1.000 42.13069  ? 370 ARG B CZ   1 
ATOM   5180 N NH1  . ARG B 1 370 ? 100.57100 100.12900 66.12800  1.000 38.37072  ? 370 ARG B NH1  1 
ATOM   5181 N NH2  . ARG B 1 370 ? 101.23300 98.39900  67.47300  1.000 39.05958  ? 370 ARG B NH2  1 
ATOM   5182 N N    . GLN B 1 371 ? 104.09700 94.94600  60.35100  1.000 50.64951  ? 371 GLN B N    1 
ATOM   5183 C CA   . GLN B 1 371 ? 104.59000 93.58600  60.18300  1.000 50.00448  ? 371 GLN B CA   1 
ATOM   5184 C C    . GLN B 1 371 ? 105.69200 93.47500  59.13700  1.000 50.98489  ? 371 GLN B C    1 
ATOM   5185 O O    . GLN B 1 371 ? 106.13500 92.36000  58.84200  1.000 52.87963  ? 371 GLN B O    1 
ATOM   5186 C CB   . GLN B 1 371 ? 103.43400 92.65200  59.81000  1.000 48.27977  ? 371 GLN B CB   1 
ATOM   5187 C CG   . GLN B 1 371 ? 102.33200 92.58300  60.85300  1.000 50.18188  ? 371 GLN B CG   1 
ATOM   5188 C CD   . GLN B 1 371 ? 102.83800 92.13200  62.20800  1.000 52.91774  ? 371 GLN B CD   1 
ATOM   5189 O OE1  . GLN B 1 371 ? 103.80800 91.38000  62.30200  1.000 54.29058  ? 371 GLN B OE1  1 
ATOM   5190 N NE2  . GLN B 1 371 ? 102.18300 92.59100  63.26800  1.000 51.24853  ? 371 GLN B NE2  1 
ATOM   5191 N N    . VAL B 1 372 ? 106.14000 94.59400  58.57000  1.000 48.06925  ? 372 VAL B N    1 
ATOM   5192 C CA   . VAL B 1 372 ? 107.22800 94.56900  57.59800  1.000 48.20420  ? 372 VAL B CA   1 
ATOM   5193 C C    . VAL B 1 372 ? 108.61000 94.63000  58.24400  1.000 48.64815  ? 372 VAL B C    1 
ATOM   5194 O O    . VAL B 1 372 ? 109.59600 94.22500  57.61200  1.000 50.68092  ? 372 VAL B O    1 
ATOM   5195 C CB   . VAL B 1 372 ? 107.06900 95.72600  56.59400  1.000 46.09167  ? 372 VAL B CB   1 
ATOM   5196 C CG1  . VAL B 1 372 ? 108.30600 95.86000  55.72300  1.000 48.36680  ? 372 VAL B CG1  1 
ATOM   5197 C CG2  . VAL B 1 372 ? 105.83100 95.51800  55.73800  1.000 45.72227  ? 372 VAL B CG2  1 
ATOM   5198 N N    . PHE B 1 373 ? 108.71100 95.11300  59.48500  1.000 45.67438  ? 373 PHE B N    1 
ATOM   5199 C CA   . PHE B 1 373 ? 109.98900 95.27800  60.17000  1.000 47.38709  ? 373 PHE B CA   1 
ATOM   5200 C C    . PHE B 1 373 ? 110.10200 94.39800  61.41300  1.000 50.21855  ? 373 PHE B C    1 
ATOM   5201 O O    . PHE B 1 373 ? 110.97600 94.63100  62.25400  1.000 53.05789  ? 373 PHE B O    1 
ATOM   5202 C CB   . PHE B 1 373 ? 110.19900 96.74600  60.55000  1.000 49.15538  ? 373 PHE B CB   1 
ATOM   5203 C CG   . PHE B 1 373 ? 109.86100 97.71500  59.45100  1.000 49.16617  ? 373 PHE B CG   1 
ATOM   5204 C CD1  . PHE B 1 373 ? 108.56800 98.19000  59.30400  1.000 48.35525  ? 373 PHE B CD1  1 
ATOM   5205 C CD2  . PHE B 1 373 ? 110.83400 98.15900  58.57300  1.000 48.49390  ? 373 PHE B CD2  1 
ATOM   5206 C CE1  . PHE B 1 373 ? 108.25100 99.08400  58.29900  1.000 46.56274  ? 373 PHE B CE1  1 
ATOM   5207 C CE2  . PHE B 1 373 ? 110.52400 99.05400  57.56600  1.000 47.39784  ? 373 PHE B CE2  1 
ATOM   5208 C CZ   . PHE B 1 373 ? 109.23000 99.51600  57.43000  1.000 47.29055  ? 373 PHE B CZ   1 
ATOM   5209 N N    . ARG B 1 374 ? 109.23500 93.39400  61.54800  1.000 48.66163  ? 374 ARG B N    1 
ATOM   5210 C CA   . ARG B 1 374 ? 109.17700 92.60400  62.77600  1.000 50.83657  ? 374 ARG B CA   1 
ATOM   5211 C C    . ARG B 1 374 ? 110.51400 91.94200  63.10900  1.000 55.05231  ? 374 ARG B C    1 
ATOM   5212 O O    . ARG B 1 374 ? 110.96900 91.98800  64.25700  1.000 55.06530  ? 374 ARG B O    1 
ATOM   5213 C CB   . ARG B 1 374 ? 108.07200 91.55400  62.65500  1.000 49.00932  ? 374 ARG B CB   1 
ATOM   5214 C CG   . ARG B 1 374 ? 108.03900 90.54500  63.78700  1.000 52.43548  ? 374 ARG B CG   1 
ATOM   5215 C CD   . ARG B 1 374 ? 107.09900 89.39400  63.46800  1.000 53.80717  ? 374 ARG B CD   1 
ATOM   5216 N NE   . ARG B 1 374 ? 105.74500 89.64600  63.94600  1.000 54.65737  ? 374 ARG B NE   1 
ATOM   5217 C CZ   . ARG B 1 374 ? 105.22700 89.11400  65.04400  1.000 53.53568  ? 374 ARG B CZ   1 
ATOM   5218 N NH1  . ARG B 1 374 ? 105.92500 88.29200  65.81000  1.000 51.28271  ? 374 ARG B NH1  1 
ATOM   5219 N NH2  . ARG B 1 374 ? 103.97700 89.41500  65.38400  1.000 50.27632  ? 374 ARG B NH2  1 
ATOM   5220 N N    . GLN B 1 375 ? 111.15700 91.31700  62.12000  1.000 50.16506  ? 375 GLN B N    1 
ATOM   5221 C CA   . GLN B 1 375 ? 112.39400 90.58400  62.38900  1.000 49.87083  ? 375 GLN B CA   1 
ATOM   5222 C C    . GLN B 1 375 ? 113.50700 91.51000  62.87200  1.000 51.17595  ? 375 GLN B C    1 
ATOM   5223 O O    . GLN B 1 375 ? 114.18600 91.22600  63.87100  1.000 56.81027  ? 375 GLN B O    1 
ATOM   5224 C CB   . GLN B 1 375 ? 112.83400 89.83300  61.13100  1.000 52.46388  ? 375 GLN B CB   1 
ATOM   5225 C CG   . GLN B 1 375 ? 111.72900 89.03800  60.45500  1.000 53.30197  ? 375 GLN B CG   1 
ATOM   5226 C CD   . GLN B 1 375 ? 111.17200 87.93900  61.33700  1.000 54.79705  ? 375 GLN B CD   1 
ATOM   5227 O OE1  . GLN B 1 375 ? 109.95700 87.80000  61.48300  1.000 54.29250  ? 375 GLN B OE1  1 
ATOM   5228 N NE2  . GLN B 1 375 ? 112.05900 87.14800  61.92800  1.000 55.36701  ? 375 GLN B NE2  1 
ATOM   5229 N N    . GLU B 1 376 ? 113.70300 92.62900  62.17300  1.000 46.60320  ? 376 GLU B N    1 
ATOM   5230 C CA   . GLU B 1 376 ? 114.75100 93.56800  62.55400  1.000 49.15923  ? 376 GLU B CA   1 
ATOM   5231 C C    . GLU B 1 376 ? 114.47100 94.17800  63.91900  1.000 48.91410  ? 376 GLU B C    1 
ATOM   5232 O O    . GLU B 1 376 ? 115.39600 94.41000  64.70600  1.000 51.61606  ? 376 GLU B O    1 
ATOM   5233 C CB   . GLU B 1 376 ? 114.89500 94.66100  61.49300  1.000 50.18125  ? 376 GLU B CB   1 
ATOM   5234 C CG   . GLU B 1 376 ? 115.30900 94.16700  60.11000  1.000 49.44809  ? 376 GLU B CG   1 
ATOM   5235 C CD   . GLU B 1 376 ? 114.23600 93.34600  59.42000  1.000 54.67930  ? 376 GLU B CD   1 
ATOM   5236 O OE1  . GLU B 1 376 ? 113.29700 92.89400  60.10600  1.000 56.17922  ? 376 GLU B OE1  1 
ATOM   5237 O OE2  . GLU B 1 376 ? 114.33300 93.14900  58.19100  1.000 54.47184  ? 376 GLU B OE2  1 
ATOM   5238 N N    . LEU B 1 377 ? 113.20100 94.45000  64.21700  1.000 34.13367  ? 377 LEU B N    1 
ATOM   5239 C CA   . LEU B 1 377 ? 112.85700 95.01100  65.51800  1.000 38.55324  ? 377 LEU B CA   1 
ATOM   5240 C C    . LEU B 1 377 ? 113.09700 94.00400  66.63800  1.000 44.34932  ? 377 LEU B C    1 
ATOM   5241 O O    . LEU B 1 377 ? 113.53900 94.37800  67.73000  1.000 48.07520  ? 377 LEU B O    1 
ATOM   5242 C CB   . LEU B 1 377 ? 111.40100 95.47600  65.51300  1.000 42.31365  ? 377 LEU B CB   1 
ATOM   5243 C CG   . LEU B 1 377 ? 111.09400 96.72500  64.68200  1.000 44.81634  ? 377 LEU B CG   1 
ATOM   5244 C CD1  . LEU B 1 377 ? 109.59500 96.88600  64.48400  1.000 39.01115  ? 377 LEU B CD1  1 
ATOM   5245 C CD2  . LEU B 1 377 ? 111.69200 97.96900  65.31900  1.000 42.97234  ? 377 LEU B CD2  1 
ATOM   5246 N N    . GLN B 1 378 ? 112.81000 92.72300  66.38900  1.000 43.97119  ? 378 GLN B N    1 
ATOM   5247 C CA   . GLN B 1 378 ? 112.96800 91.71500  67.43400  1.000 40.99688  ? 378 GLN B CA   1 
ATOM   5248 C C    . GLN B 1 378 ? 114.43100 91.36400  67.68000  1.000 43.30952  ? 378 GLN B C    1 
ATOM   5249 O O    . GLN B 1 378 ? 114.80600 91.01600  68.81100  1.000 51.59882  ? 378 GLN B O    1 
ATOM   5250 C CB   . GLN B 1 378 ? 112.18100 90.45900  67.06400  1.000 43.26208  ? 378 GLN B CB   1 
ATOM   5251 C CG   . GLN B 1 378 ? 110.67400 90.64000  67.10100  1.000 47.20067  ? 378 GLN B CG   1 
ATOM   5252 C CD   . GLN B 1 378 ? 109.92800 89.32100  67.08800  1.000 49.47308  ? 378 GLN B CD   1 
ATOM   5253 O OE1  . GLN B 1 378 ? 110.15000 88.47700  66.22000  1.000 51.40885  ? 378 GLN B OE1  1 
ATOM   5254 N NE2  . GLN B 1 378 ? 109.03400 89.13900  68.05300  1.000 48.94997  ? 378 GLN B NE2  1 
ATOM   5255 N N    . ARG B 1 379 ? 115.27800 91.48000  66.65300  1.000 32.83021  ? 379 ARG B N    1 
ATOM   5256 C CA   . ARG B 1 379 ? 116.69100 91.16700  66.85100  1.000 31.65886  ? 379 ARG B CA   1 
ATOM   5257 C C    . ARG B 1 379 ? 117.35100 92.15200  67.81000  1.000 37.49780  ? 379 ARG B C    1 
ATOM   5258 O O    . ARG B 1 379 ? 118.14400 91.75300  68.67500  1.000 43.93312  ? 379 ARG B O    1 
ATOM   5259 C CB   . ARG B 1 379 ? 117.41600 91.15900  65.50600  1.000 34.95522  ? 379 ARG B CB   1 
ATOM   5260 C CG   . ARG B 1 379 ? 117.62200 89.77600  64.91600  1.000 36.84705  ? 379 ARG B CG   1 
ATOM   5261 C CD   . ARG B 1 379 ? 119.06200 89.31800  65.06800  1.000 41.29613  ? 379 ARG B CD   1 
ATOM   5262 N NE   . ARG B 1 379 ? 119.92700 89.89900  64.04900  1.000 42.88120  ? 379 ARG B NE   1 
ATOM   5263 C CZ   . ARG B 1 379 ? 121.24600 89.99400  64.14900  1.000 42.26849  ? 379 ARG B CZ   1 
ATOM   5264 N NH1  . ARG B 1 379 ? 121.89100 89.55500  65.21700  1.000 40.95680  ? 379 ARG B NH1  1 
ATOM   5265 N NH2  . ARG B 1 379 ? 121.93400 90.54500  63.15300  1.000 40.77983  ? 379 ARG B NH2  1 
ATOM   5266 N N    . VAL B 1 380 ? 117.02300 93.43900  67.68300  1.000 33.57188  ? 380 VAL B N    1 
ATOM   5267 C CA   . VAL B 1 380 ? 117.60700 94.44800  68.56200  1.000 36.10274  ? 380 VAL B CA   1 
ATOM   5268 C C    . VAL B 1 380 ? 117.20400 94.19300  70.00800  1.000 35.27692  ? 380 VAL B C    1 
ATOM   5269 O O    . VAL B 1 380 ? 118.02500 94.30500  70.92700  1.000 35.96263  ? 380 VAL B O    1 
ATOM   5270 C CB   . VAL B 1 380 ? 117.19600 95.85800  68.10000  1.000 32.67996  ? 380 VAL B CB   1 
ATOM   5271 C CG1  . VAL B 1 380 ? 117.53700 96.88900  69.16300  1.000 34.73289  ? 380 VAL B CG1  1 
ATOM   5272 C CG2  . VAL B 1 380 ? 117.86600 96.19900  66.78000  1.000 32.35931  ? 380 VAL B CG2  1 
ATOM   5273 N N    . GLY B 1 381 ? 115.94600 93.81300  70.22800  1.000 25.67671  ? 381 GLY B N    1 
ATOM   5274 C CA   . GLY B 1 381 ? 115.50100 93.52300  71.58100  1.000 31.53890  ? 381 GLY B CA   1 
ATOM   5275 C C    . GLY B 1 381 ? 116.20700 92.31800  72.17100  1.000 33.85546  ? 381 GLY B C    1 
ATOM   5276 O O    . GLY B 1 381 ? 116.65600 92.34600  73.32400  1.000 35.19477  ? 381 GLY B O    1 
ATOM   5277 N N    . VAL B 1 382 ? 116.32000 91.24300  71.38900  1.000 28.57671  ? 382 VAL B N    1 
ATOM   5278 C CA   . VAL B 1 382 ? 116.99100 90.04700  71.89100  1.000 26.38660  ? 382 VAL B CA   1 
ATOM   5279 C C    . VAL B 1 382 ? 118.43600 90.36100  72.26300  1.000 30.51274  ? 382 VAL B C    1 
ATOM   5280 O O    . VAL B 1 382 ? 118.91500 89.97900  73.34300  1.000 36.03180  ? 382 VAL B O    1 
ATOM   5281 C CB   . VAL B 1 382 ? 116.90600 88.91500  70.85000  1.000 30.71483  ? 382 VAL B CB   1 
ATOM   5282 C CG1  . VAL B 1 382 ? 117.70600 87.70600  71.30700  1.000 30.47097  ? 382 VAL B CG1  1 
ATOM   5283 C CG2  . VAL B 1 382 ? 115.45700 88.53500  70.59600  1.000 30.31060  ? 382 VAL B CG2  1 
ATOM   5284 N N    . GLU B 1 383 ? 119.14200 91.10000  71.40200  1.000 28.72286  ? 383 GLU B N    1 
ATOM   5285 C CA   . GLU B 1 383 ? 120.54800 91.38200  71.67400  1.000 23.92394  ? 383 GLU B CA   1 
ATOM   5286 C C    . GLU B 1 383 ? 120.72100 92.32800  72.85800  1.000 26.60951  ? 383 GLU B C    1 
ATOM   5287 O O    . GLU B 1 383 ? 121.63900 92.15100  73.67300  1.000 26.20942  ? 383 GLU B O    1 
ATOM   5288 C CB   . GLU B 1 383 ? 121.21400 91.95500  70.42400  1.000 25.07689  ? 383 GLU B CB   1 
ATOM   5289 C CG   . GLU B 1 383 ? 121.38700 90.94700  69.30200  1.000 25.00138  ? 383 GLU B CG   1 
ATOM   5290 C CD   . GLU B 1 383 ? 122.20400 89.74200  69.72200  1.000 35.40297  ? 383 GLU B CD   1 
ATOM   5291 O OE1  . GLU B 1 383 ? 123.29400 89.93400  70.30100  1.000 40.14591  ? 383 GLU B OE1  1 
ATOM   5292 O OE2  . GLU B 1 383 ? 121.75700 88.60300  69.47800  1.000 34.73301  ? 383 GLU B OE2  1 
ATOM   5293 N N    . GLY B 1 384 ? 119.82200 93.30400  73.01100  1.000 17.03610  ? 384 GLY B N    1 
ATOM   5294 C CA   . GLY B 1 384 ? 119.93100 94.20400  74.14600  1.000 17.24054  ? 384 GLY B CA   1 
ATOM   5295 C C    . GLY B 1 384 ? 119.65400 93.50700  75.46200  1.000 21.82503  ? 384 GLY B C    1 
ATOM   5296 O O    . GLY B 1 384 ? 120.33700 93.75400  76.46400  1.000 22.38914  ? 384 GLY B O    1 
ATOM   5297 N N    . ALA B 1 385 ? 118.67700 92.59800  75.47400  1.000 20.19092  ? 385 ALA B N    1 
ATOM   5298 C CA   . ALA B 1 385 ? 118.39100 91.87300  76.70500  1.000 22.56257  ? 385 ALA B CA   1 
ATOM   5299 C C    . ALA B 1 385 ? 119.54000 90.93900  77.06000  1.000 24.34498  ? 385 ALA B C    1 
ATOM   5300 O O    . ALA B 1 385 ? 119.91800 90.82700  78.23500  1.000 22.69371  ? 385 ALA B O    1 
ATOM   5301 C CB   . ALA B 1 385 ? 117.08200 91.09800  76.56800  1.000 19.53600  ? 385 ALA B CB   1 
ATOM   5302 N N    . LYS B 1 386 ? 120.14200 90.29700  76.05400  1.000 22.67536  ? 386 LYS B N    1 
ATOM   5303 C CA   . LYS B 1 386 ? 121.28800 89.43700  76.32800  1.000 21.74678  ? 386 LYS B CA   1 
ATOM   5304 C C    . LYS B 1 386 ? 122.45100 90.23400  76.90700  1.000 23.06251  ? 386 LYS B C    1 
ATOM   5305 O O    . LYS B 1 386 ? 123.09800 89.79800  77.87100  1.000 26.52853  ? 386 LYS B O    1 
ATOM   5306 C CB   . LYS B 1 386 ? 121.71800 88.71600  75.05100  1.000 23.61673  ? 386 LYS B CB   1 
ATOM   5307 C CG   . LYS B 1 386 ? 121.88700 87.21800  75.21000  1.000 26.02122  ? 386 LYS B CG   1 
ATOM   5308 C CD   . LYS B 1 386 ? 122.17700 86.55500  73.87600  1.000 28.05667  ? 386 LYS B CD   1 
ATOM   5309 C CE   . LYS B 1 386 ? 120.94000 86.52300  72.99600  1.000 31.48230  ? 386 LYS B CE   1 
ATOM   5310 N NZ   . LYS B 1 386 ? 119.77000 85.94000  73.70800  1.000 29.67891  ? 386 LYS B NZ   1 
ATOM   5311 N N    . LEU B 1 387 ? 122.71300 91.42300  76.35700  1.000 19.10271  ? 387 LEU B N    1 
ATOM   5312 C CA   . LEU B 1 387 ? 123.82300 92.22400  76.86300  1.000 19.34611  ? 387 LEU B CA   1 
ATOM   5313 C C    . LEU B 1 387 ? 123.56700 92.70400  78.28900  1.000 20.02324  ? 387 LEU B C    1 
ATOM   5314 O O    . LEU B 1 387 ? 124.46700 92.64700  79.14100  1.000 18.76634  ? 387 LEU B O    1 
ATOM   5315 C CB   . LEU B 1 387 ? 124.07100 93.41200  75.93600  1.000 25.08006  ? 387 LEU B CB   1 
ATOM   5316 C CG   . LEU B 1 387 ? 125.15900 94.39900  76.36100  1.000 24.82043  ? 387 LEU B CG   1 
ATOM   5317 C CD1  . LEU B 1 387 ? 126.52100 93.72800  76.40500  1.000 25.04744  ? 387 LEU B CD1  1 
ATOM   5318 C CD2  . LEU B 1 387 ? 125.17400 95.59300  75.43300  1.000 19.41131  ? 387 LEU B CD2  1 
ATOM   5319 N N    . LEU B 1 388 ? 122.34400 93.15800  78.58200  1.000 18.91537  ? 388 LEU B N    1 
ATOM   5320 C CA   . LEU B 1 388 ? 122.07600 93.62500  79.93900  1.000 15.75007  ? 388 LEU B CA   1 
ATOM   5321 C C    . LEU B 1 388 ? 122.11700 92.48300  80.94700  1.000 19.49214  ? 388 LEU B C    1 
ATOM   5322 O O    . LEU B 1 388 ? 122.58600 92.67100  82.08000  1.000 22.99844  ? 388 LEU B O    1 
ATOM   5323 C CB   . LEU B 1 388 ? 120.72400 94.33700  79.99800  1.000 17.17531  ? 388 LEU B CB   1 
ATOM   5324 C CG   . LEU B 1 388 ? 120.62200 95.68700  79.28500  1.000 18.72786  ? 388 LEU B CG   1 
ATOM   5325 C CD1  . LEU B 1 388 ? 119.18700 96.17700  79.25800  1.000 8.23104   ? 388 LEU B CD1  1 
ATOM   5326 C CD2  . LEU B 1 388 ? 121.52700 96.71600  79.94100  1.000 15.85881  ? 388 LEU B CD2  1 
ATOM   5327 N N    . ARG B 1 389 ? 121.72700 91.27400  80.53700  1.000 25.86471  ? 389 ARG B N    1 
ATOM   5328 C CA   . ARG B 1 389 ? 121.77300 90.16400  81.47900  1.000 21.13967  ? 389 ARG B CA   1 
ATOM   5329 C C    . ARG B 1 389 ? 123.19700 89.67700  81.69600  1.000 24.52384  ? 389 ARG B C    1 
ATOM   5330 O O    . ARG B 1 389 ? 123.54500 89.26400  82.81100  1.000 25.79192  ? 389 ARG B O    1 
ATOM   5331 C CB   . ARG B 1 389 ? 120.87600 89.02700  80.98900  1.000 24.04091  ? 389 ARG B CB   1 
ATOM   5332 C CG   . ARG B 1 389 ? 119.43700 89.15800  81.45500  1.000 21.36226  ? 389 ARG B CG   1 
ATOM   5333 C CD   . ARG B 1 389 ? 118.51000 88.22200  80.70600  1.000 21.66980  ? 389 ARG B CD   1 
ATOM   5334 N NE   . ARG B 1 389 ? 117.11500 88.46900  81.05100  1.000 29.66284  ? 389 ARG B NE   1 
ATOM   5335 C CZ   . ARG B 1 389 ? 116.12200 88.51900  80.17400  1.000 27.37943  ? 389 ARG B CZ   1 
ATOM   5336 N NH1  . ARG B 1 389 ? 116.33100 88.33100  78.88200  1.000 24.14482  ? 389 ARG B NH1  1 
ATOM   5337 N NH2  . ARG B 1 389 ? 114.88900 88.76700  80.60500  1.000 22.25354  ? 389 ARG B NH2  1 
ATOM   5338 N N    . GLU B 1 390 ? 124.05400 89.78600  80.67900  1.000 27.47852  ? 390 GLU B N    1 
ATOM   5339 C CA   . GLU B 1 390 ? 125.44200 89.39500  80.88700  1.000 23.14897  ? 390 GLU B CA   1 
ATOM   5340 C C    . GLU B 1 390 ? 126.17500 90.41700  81.74500  1.000 24.09266  ? 390 GLU B C    1 
ATOM   5341 O O    . GLU B 1 390 ? 127.02800 90.04400  82.56200  1.000 23.30435  ? 390 GLU B O    1 
ATOM   5342 C CB   . GLU B 1 390 ? 126.14800 89.21600  79.54400  1.000 21.84873  ? 390 GLU B CB   1 
ATOM   5343 C CG   . GLU B 1 390 ? 127.66100 89.28600  79.62600  1.000 26.16134  ? 390 GLU B CG   1 
ATOM   5344 C CD   . GLU B 1 390 ? 128.30200 87.91500  79.65800  1.000 34.97796  ? 390 GLU B CD   1 
ATOM   5345 O OE1  . GLU B 1 390 ? 127.56000 86.91200  79.68600  1.000 32.81025  ? 390 GLU B OE1  1 
ATOM   5346 O OE2  . GLU B 1 390 ? 129.54800 87.84000  79.65500  1.000 36.08063  ? 390 GLU B OE2  1 
ATOM   5347 N N    . LEU B 1 391 ? 125.80600 91.69700  81.63700  1.000 28.42637  ? 391 LEU B N    1 
ATOM   5348 C CA   . LEU B 1 391 ? 126.41400 92.68700  82.52200  1.000 19.22488  ? 391 LEU B CA   1 
ATOM   5349 C C    . LEU B 1 391 ? 125.93700 92.50800  83.95800  1.000 18.11825  ? 391 LEU B C    1 
ATOM   5350 O O    . LEU B 1 391 ? 126.72200 92.66500  84.90300  1.000 24.19052  ? 391 LEU B O    1 
ATOM   5351 C CB   . LEU B 1 391 ? 126.11000 94.10100  82.02800  1.000 23.32624  ? 391 LEU B CB   1 
ATOM   5352 C CG   . LEU B 1 391 ? 126.89100 94.58900  80.80700  1.000 27.39455  ? 391 LEU B CG   1 
ATOM   5353 C CD1  . LEU B 1 391 ? 126.56800 96.04400  80.51800  1.000 24.39479  ? 391 LEU B CD1  1 
ATOM   5354 C CD2  . LEU B 1 391 ? 128.38500 94.40100  81.01600  1.000 22.25316  ? 391 LEU B CD2  1 
ATOM   5355 N N    . GLY B 1 392 ? 124.67400 92.12100  84.14600  1.000 20.29061  ? 392 GLY B N    1 
ATOM   5356 C CA   . GLY B 1 392 ? 124.20800 91.84900  85.49600  1.000 27.14552  ? 392 GLY B CA   1 
ATOM   5357 C C    . GLY B 1 392 ? 124.88700 90.63800  86.11000  1.000 27.28654  ? 392 GLY B C    1 
ATOM   5358 O O    . GLY B 1 392 ? 125.26400 90.65300  87.28900  1.000 20.46823  ? 392 GLY B O    1 
ATOM   5359 N N    . GLU B 1 393 ? 125.09100 89.58600  85.31000  1.000 30.32288  ? 393 GLU B N    1 
ATOM   5360 C CA   . GLU B 1 393 ? 125.77900 88.40600  85.82300  1.000 21.15149  ? 393 GLU B CA   1 
ATOM   5361 C C    . GLU B 1 393 ? 127.24200 88.69400  86.13200  1.000 27.62112  ? 393 GLU B C    1 
ATOM   5362 O O    . GLU B 1 393 ? 127.78900 88.13300  87.08800  1.000 25.81103  ? 393 GLU B O    1 
ATOM   5363 C CB   . GLU B 1 393 ? 125.66700 87.25300  84.82800  1.000 25.31398  ? 393 GLU B CB   1 
ATOM   5364 C CG   . GLU B 1 393 ? 124.24300 86.79100  84.57400  1.000 32.50423  ? 393 GLU B CG   1 
ATOM   5365 C CD   . GLU B 1 393 ? 123.74600 85.82800  85.63300  1.000 38.07111  ? 393 GLU B CD   1 
ATOM   5366 O OE1  . GLU B 1 393 ? 124.57900 85.11400  86.22900  1.000 35.71197  ? 393 GLU B OE1  1 
ATOM   5367 O OE2  . GLU B 1 393 ? 122.52000 85.78500  85.86800  1.000 36.83458  ? 393 GLU B OE2  1 
ATOM   5368 N N    . LYS B 1 394 ? 127.89300 89.56200  85.35200  1.000 33.94666  ? 394 LYS B N    1 
ATOM   5369 C CA   . LYS B 1 394 ? 129.28200 89.88800  85.66300  1.000 26.55128  ? 394 LYS B CA   1 
ATOM   5370 C C    . LYS B 1 394 ? 129.39400 90.79700  86.87900  1.000 26.32296  ? 394 LYS B C    1 
ATOM   5371 O O    . LYS B 1 394 ? 130.38400 90.72100  87.61400  1.000 22.22862  ? 394 LYS B O    1 
ATOM   5372 C CB   . LYS B 1 394 ? 129.96900 90.53100  84.45900  1.000 23.94297  ? 394 LYS B CB   1 
ATOM   5373 C CG   . LYS B 1 394 ? 130.96400 89.61500  83.77200  1.000 25.41013  ? 394 LYS B CG   1 
ATOM   5374 C CD   . LYS B 1 394 ? 130.95200 89.79300  82.27000  1.000 29.48283  ? 394 LYS B CD   1 
ATOM   5375 C CE   . LYS B 1 394 ? 131.61700 88.61400  81.58100  1.000 32.99135  ? 394 LYS B CE   1 
ATOM   5376 N NZ   . LYS B 1 394 ? 133.00100 88.38900  82.08400  1.000 28.21642  ? 394 LYS B NZ   1 
ATOM   5377 N N    . VAL B 1 395 ? 128.40100 91.65600  87.11600  1.000 23.23891  ? 395 VAL B N    1 
ATOM   5378 C CA   . VAL B 1 395 ? 128.44100 92.48800  88.31500  1.000 20.42160  ? 395 VAL B CA   1 
ATOM   5379 C C    . VAL B 1 395 ? 128.19800 91.64600  89.56200  1.000 25.94460  ? 395 VAL B C    1 
ATOM   5380 O O    . VAL B 1 395 ? 128.83800 91.85400  90.59900  1.000 22.31129  ? 395 VAL B O    1 
ATOM   5381 C CB   . VAL B 1 395 ? 127.43000 93.64400  88.20800  1.000 21.75946  ? 395 VAL B CB   1 
ATOM   5382 C CG1  . VAL B 1 395 ? 127.30600 94.36000  89.54200  1.000 14.57779  ? 395 VAL B CG1  1 
ATOM   5383 C CG2  . VAL B 1 395 ? 127.85100 94.61800  87.12300  1.000 27.97925  ? 395 VAL B CG2  1 
ATOM   5384 N N    . LYS B 1 396 ? 127.27600 90.68300  89.48800  1.000 28.55674  ? 396 LYS B N    1 
ATOM   5385 C CA   . LYS B 1 396 ? 126.97000 89.87700  90.66900  1.000 18.22729  ? 396 LYS B CA   1 
ATOM   5386 C C    . LYS B 1 396 ? 128.15900 89.02400  91.10500  1.000 27.41993  ? 396 LYS B C    1 
ATOM   5387 O O    . LYS B 1 396 ? 128.47900 88.95800  92.29700  1.000 26.03774  ? 396 LYS B O    1 
ATOM   5388 C CB   . LYS B 1 396 ? 125.75000 88.99500  90.40700  1.000 24.72759  ? 396 LYS B CB   1 
ATOM   5389 C CG   . LYS B 1 396 ? 125.37500 88.12000  91.59100  1.000 25.64550  ? 396 LYS B CG   1 
ATOM   5390 C CD   . LYS B 1 396 ? 124.65600 86.85800  91.15400  1.000 23.58621  ? 396 LYS B CD   1 
ATOM   5391 C CE   . LYS B 1 396 ? 123.25000 87.16300  90.67800  1.000 32.19183  ? 396 LYS B CE   1 
ATOM   5392 N NZ   . LYS B 1 396 ? 122.22500 86.65000  91.62700  1.000 30.47038  ? 396 LYS B NZ   1 
ATOM   5393 N N    . LYS B 1 397 ? 128.82600 88.36000  90.15900  1.000 34.71022  ? 397 LYS B N    1 
ATOM   5394 C CA   . LYS B 1 397 ? 129.97200 87.51700  90.48800  1.000 30.26961  ? 397 LYS B CA   1 
ATOM   5395 C C    . LYS B 1 397 ? 131.25800 88.29100  90.75200  1.000 32.61999  ? 397 LYS B C    1 
ATOM   5396 O O    . LYS B 1 397 ? 132.23900 87.68200  91.18900  1.000 31.30569  ? 397 LYS B O    1 
ATOM   5397 C CB   . LYS B 1 397 ? 130.23000 86.50700  89.36700  1.000 27.28850  ? 397 LYS B CB   1 
ATOM   5398 C CG   . LYS B 1 397 ? 129.22300 85.37600  89.29100  1.000 33.20990  ? 397 LYS B CG   1 
ATOM   5399 C CD   . LYS B 1 397 ? 129.54200 84.44600  88.13100  1.000 33.07010  ? 397 LYS B CD   1 
ATOM   5400 C CE   . LYS B 1 397 ? 129.54900 85.19300  86.80700  1.000 34.31253  ? 397 LYS B CE   1 
ATOM   5401 N NZ   . LYS B 1 397 ? 128.40500 84.80300  85.93700  1.000 37.94324  ? 397 LYS B NZ   1 
ATOM   5402 N N    . MET B 1 398 ? 131.28600 89.60000  90.51100  1.000 41.95794  ? 398 MET B N    1 
ATOM   5403 C CA   . MET B 1 398 ? 132.49900 90.39800  90.68100  1.000 35.49643  ? 398 MET B CA   1 
ATOM   5404 C C    . MET B 1 398 ? 133.62500 89.85800  89.79600  1.000 38.52161  ? 398 MET B C    1 
ATOM   5405 O O    . MET B 1 398 ? 134.66400 89.39500  90.26900  1.000 41.76476  ? 398 MET B O    1 
ATOM   5406 C CB   . MET B 1 398 ? 132.92400 90.43400  92.15300  1.000 25.24420  ? 398 MET B CB   1 
ATOM   5407 C CG   . MET B 1 398 ? 132.07600 91.33900  93.02800  1.000 35.75308  ? 398 MET B CG   1 
ATOM   5408 S SD   . MET B 1 398 ? 132.11500 90.85900  94.76500  1.000 42.95627  ? 398 MET B SD   1 
ATOM   5409 C CE   . MET B 1 398 ? 133.20700 92.10400  95.44200  1.000 36.88333  ? 398 MET B CE   1 
ATOM   5410 N N    . GLU B 1 399 ? 133.39500 89.93200  88.48700  1.000 44.25348  ? 399 GLU B N    1 
ATOM   5411 C CA   . GLU B 1 399 ? 134.32200 89.41600  87.49100  1.000 39.60639  ? 399 GLU B CA   1 
ATOM   5412 C C    . GLU B 1 399 ? 134.54500 90.45500  86.40100  1.000 41.84045  ? 399 GLU B C    1 
ATOM   5413 O O    . GLU B 1 399 ? 133.65700 91.25100  86.08800  1.000 45.76147  ? 399 GLU B O    1 
ATOM   5414 C CB   . GLU B 1 399 ? 133.80100 88.10900  86.87900  1.000 38.61523  ? 399 GLU B CB   1 
ATOM   5415 C CG   . GLU B 1 399 ? 134.75700 87.44500  85.90500  1.000 43.26032  ? 399 GLU B CG   1 
ATOM   5416 C CD   . GLU B 1 399 ? 134.30600 86.05300  85.51100  1.000 48.54825  ? 399 GLU B CD   1 
ATOM   5417 O OE1  . GLU B 1 399 ? 133.24700 85.92900  84.86000  1.000 50.70259  ? 399 GLU B OE1  1 
ATOM   5418 O OE2  . GLU B 1 399 ? 135.01000 85.08000  85.85300  1.000 48.49747  ? 399 GLU B OE2  1 
ATOM   5419 N N    . LYS B 1 400 ? 135.74600 90.44300  85.82900  1.000 38.03084  ? 400 LYS B N    1 
ATOM   5420 C CA   . LYS B 1 400 ? 136.10300 91.37900  84.77500  1.000 40.30174  ? 400 LYS B CA   1 
ATOM   5421 C C    . LYS B 1 400 ? 135.59800 90.88900  83.41800  1.000 36.52436  ? 400 LYS B C    1 
ATOM   5422 O O    . LYS B 1 400 ? 135.12200 89.76100  83.26600  1.000 37.73346  ? 400 LYS B O    1 
ATOM   5423 C CB   . LYS B 1 400 ? 137.61600 91.58300  84.73000  1.000 39.92057  ? 400 LYS B CB   1 
ATOM   5424 C CG   . LYS B 1 400 ? 138.16700 92.45000  85.84600  1.000 36.72637  ? 400 LYS B CG   1 
ATOM   5425 C CD   . LYS B 1 400 ? 139.66200 92.66600  85.67800  1.000 38.64466  ? 400 LYS B CD   1 
ATOM   5426 C CE   . LYS B 1 400 ? 140.05500 94.09800  86.00000  1.000 39.30200  ? 400 LYS B CE   1 
ATOM   5427 N NZ   . LYS B 1 400 ? 140.70900 94.20800  87.33300  1.000 40.28158  ? 400 LYS B NZ   1 
ATOM   5428 N N    . LEU B 1 401 ? 135.70600 91.76200  82.42000  1.000 39.22343  ? 401 LEU B N    1 
ATOM   5429 C CA   . LEU B 1 401 ? 135.28400 91.45300  81.06200  1.000 42.02282  ? 401 LEU B CA   1 
ATOM   5430 C C    . LEU B 1 401 ? 136.40400 90.74500  80.30900  1.000 41.16986  ? 401 LEU B C    1 
ATOM   5431 O O    . LEU B 1 401 ? 137.58900 91.01200  80.52200  1.000 40.86516  ? 401 LEU B O    1 
ATOM   5432 C CB   . LEU B 1 401 ? 134.87500 92.72200  80.31200  1.000 41.12608  ? 401 LEU B CB   1 
ATOM   5433 C CG   . LEU B 1 401 ? 133.69800 93.51800  80.87600  1.000 43.33962  ? 401 LEU B CG   1 
ATOM   5434 C CD1  . LEU B 1 401 ? 133.37100 94.69900  79.97500  1.000 38.68886  ? 401 LEU B CD1  1 
ATOM   5435 C CD2  . LEU B 1 401 ? 132.48200 92.62700  81.06100  1.000 42.45497  ? 401 LEU B CD2  1 
ATOM   5436 N N    . GLY B 1 402 ? 136.01500 89.83500  79.42000  1.000 54.24695  ? 402 GLY B N    1 
ATOM   5437 C CA   . GLY B 1 402 ? 136.97200 89.05400  78.67400  1.000 53.87519  ? 402 GLY B CA   1 
ATOM   5438 C C    . GLY B 1 402 ? 137.56700 89.78600  77.48800  1.000 56.61254  ? 402 GLY B C    1 
ATOM   5439 O O    . GLY B 1 402 ? 137.49200 91.01400  77.37600  1.000 58.46020  ? 402 GLY B O    1 
ATOM   5440 N N    . PRO B 1 403 ? 138.17900 89.03100  76.57400  1.000 67.79867  ? 403 PRO B N    1 
ATOM   5441 C CA   . PRO B 1 403 ? 138.85500 89.64600  75.42300  1.000 67.14608  ? 403 PRO B CA   1 
ATOM   5442 C C    . PRO B 1 403 ? 137.92600 90.15600  74.33000  1.000 67.11724  ? 403 PRO B C    1 
ATOM   5443 O O    . PRO B 1 403 ? 138.20100 91.19200  73.71700  1.000 67.59651  ? 403 PRO B O    1 
ATOM   5444 C CB   . PRO B 1 403 ? 139.74500 88.51100  74.90400  1.000 66.12758  ? 403 PRO B CB   1 
ATOM   5445 C CG   . PRO B 1 403 ? 139.01400 87.27100  75.28400  1.000 66.80731  ? 403 PRO B CG   1 
ATOM   5446 C CD   . PRO B 1 403 ? 138.33900 87.56600  76.59700  1.000 67.34829  ? 403 PRO B CD   1 
ATOM   5447 N N    . VAL B 1 404 ? 136.82800 89.44600  74.07200  1.000 62.91816  ? 404 VAL B N    1 
ATOM   5448 C CA   . VAL B 1 404 ? 135.94300 89.78300  72.96200  1.000 62.92439  ? 404 VAL B CA   1 
ATOM   5449 C C    . VAL B 1 404 ? 135.15300 91.05400  73.25200  1.000 65.49317  ? 404 VAL B C    1 
ATOM   5450 O O    . VAL B 1 404 ? 135.14600 91.55400  74.38100  1.000 65.33649  ? 404 VAL B O    1 
ATOM   5451 C CB   . VAL B 1 404 ? 134.99100 88.61500  72.64600  1.000 63.52848  ? 404 VAL B CB   1 
ATOM   5452 C CG1  . VAL B 1 404 ? 135.77800 87.40500  72.17000  1.000 64.45781  ? 404 VAL B CG1  1 
ATOM   5453 C CG2  . VAL B 1 404 ? 134.15400 88.26800  73.86700  1.000 63.07856  ? 404 VAL B CG2  1 
ATOM   5454 N N    . ASP B 1 405 ? 134.48500 91.57800  72.22500  1.000 51.06032  ? 405 ASP B N    1 
ATOM   5455 C CA   . ASP B 1 405 ? 133.68900 92.79400  72.32400  1.000 51.22184  ? 405 ASP B CA   1 
ATOM   5456 C C    . ASP B 1 405 ? 132.22300 92.43100  72.52300  1.000 51.74429  ? 405 ASP B C    1 
ATOM   5457 O O    . ASP B 1 405 ? 131.68500 91.58700  71.80000  1.000 53.02357  ? 405 ASP B O    1 
ATOM   5458 C CB   . ASP B 1 405 ? 133.85900 93.65700  71.07300  1.000 50.76228  ? 405 ASP B CB   1 
ATOM   5459 C CG   . ASP B 1 405 ? 133.13700 94.98600  71.17700  1.000 51.69349  ? 405 ASP B CG   1 
ATOM   5460 O OD1  . ASP B 1 405 ? 132.77100 95.37800  72.30500  1.000 53.45637  ? 405 ASP B OD1  1 
ATOM   5461 O OD2  . ASP B 1 405 ? 132.93900 95.64100  70.13300  1.000 49.20531  ? 405 ASP B OD2  1 
ATOM   5462 N N    . LEU B 1 406 ? 131.58500 93.06900  73.50200  1.000 40.38839  ? 406 LEU B N    1 
ATOM   5463 C CA   . LEU B 1 406 ? 130.20900 92.76200  73.86700  1.000 42.28541  ? 406 LEU B CA   1 
ATOM   5464 C C    . LEU B 1 406 ? 129.16600 93.53400  73.06600  1.000 44.61908  ? 406 LEU B C    1 
ATOM   5465 O O    . LEU B 1 406 ? 127.97200 93.25000  73.20800  1.000 43.98416  ? 406 LEU B O    1 
ATOM   5466 C CB   . LEU B 1 406 ? 129.99200 93.03700  75.35900  1.000 43.22779  ? 406 LEU B CB   1 
ATOM   5467 C CG   . LEU B 1 406 ? 130.46100 91.96900  76.34800  1.000 44.87724  ? 406 LEU B CG   1 
ATOM   5468 C CD1  . LEU B 1 406 ? 129.64800 92.03900  77.63000  1.000 43.56246  ? 406 LEU B CD1  1 
ATOM   5469 C CD2  . LEU B 1 406 ? 130.37400 90.58400  75.72900  1.000 44.43245  ? 406 LEU B CD2  1 
ATOM   5470 N N    . LEU B 1 407 ? 129.56900 94.49200  72.22900  1.000 37.39232  ? 407 LEU B N    1 
ATOM   5471 C CA   . LEU B 1 407 ? 128.61900 95.32100  71.49400  1.000 32.80869  ? 407 LEU B CA   1 
ATOM   5472 C C    . LEU B 1 407 ? 128.70500 95.11500  69.98400  1.000 30.03525  ? 407 LEU B C    1 
ATOM   5473 O O    . LEU B 1 407 ? 128.45500 96.04400  69.21600  1.000 39.00957  ? 407 LEU B O    1 
ATOM   5474 C CB   . LEU B 1 407 ? 128.83400 96.79600  71.83300  1.000 34.61116  ? 407 LEU B CB   1 
ATOM   5475 C CG   . LEU B 1 407 ? 128.52100 97.26000  73.25600  1.000 32.95550  ? 407 LEU B CG   1 
ATOM   5476 C CD1  . LEU B 1 407 ? 128.99000 98.68800  73.46700  1.000 29.08166  ? 407 LEU B CD1  1 
ATOM   5477 C CD2  . LEU B 1 407 ? 127.03800 97.14800  73.53200  1.000 30.13279  ? 407 LEU B CD2  1 
ATOM   5478 N N    . PHE B 1 408 ? 129.05500 93.91000  69.53800  1.000 33.78942  ? 408 PHE B N    1 
ATOM   5479 C CA   . PHE B 1 408 ? 129.18000 93.65500  68.10700  1.000 35.80340  ? 408 PHE B CA   1 
ATOM   5480 C C    . PHE B 1 408 ? 127.86400 93.21000  67.47000  1.000 40.71150  ? 408 PHE B C    1 
ATOM   5481 O O    . PHE B 1 408 ? 127.46300 93.73300  66.42100  1.000 42.15437  ? 408 PHE B O    1 
ATOM   5482 C CB   . PHE B 1 408 ? 130.27000 92.60200  67.87200  1.000 38.21736  ? 408 PHE B CB   1 
ATOM   5483 C CG   . PHE B 1 408 ? 130.48800 92.26000  66.42500  1.000 39.42923  ? 408 PHE B CG   1 
ATOM   5484 C CD1  . PHE B 1 408 ? 129.73900 91.27200  65.80900  1.000 38.04919  ? 408 PHE B CD1  1 
ATOM   5485 C CD2  . PHE B 1 408 ? 131.45000 92.92300  65.68300  1.000 39.57684  ? 408 PHE B CD2  1 
ATOM   5486 C CE1  . PHE B 1 408 ? 129.94000 90.95700  64.48100  1.000 39.98271  ? 408 PHE B CE1  1 
ATOM   5487 C CE2  . PHE B 1 408 ? 131.65600 92.61100  64.35400  1.000 39.85588  ? 408 PHE B CE2  1 
ATOM   5488 C CZ   . PHE B 1 408 ? 130.90000 91.62800  63.75300  1.000 39.42703  ? 408 PHE B CZ   1 
ATOM   5489 N N    . GLU B 1 409 ? 127.15900 92.28100  68.12000  1.000 39.14220  ? 409 GLU B N    1 
ATOM   5490 C CA   . GLU B 1 409 ? 125.90100 91.78600  67.57200  1.000 38.85631  ? 409 GLU B CA   1 
ATOM   5491 C C    . GLU B 1 409 ? 124.80900 92.84800  67.60500  1.000 41.10285  ? 409 GLU B C    1 
ATOM   5492 O O    . GLU B 1 409 ? 124.02500 92.96400  66.65700  1.000 44.34638  ? 409 GLU B O    1 
ATOM   5493 C CB   . GLU B 1 409 ? 125.45600 90.53900  68.33500  1.000 36.72323  ? 409 GLU B CB   1 
ATOM   5494 C CG   . GLU B 1 409 ? 126.29400 89.30400  68.05100  1.000 41.45036  ? 409 GLU B CG   1 
ATOM   5495 C CD   . GLU B 1 409 ? 126.45300 89.03100  66.56900  1.000 47.08150  ? 409 GLU B CD   1 
ATOM   5496 O OE1  . GLU B 1 409 ? 125.44700 88.68700  65.91300  1.000 46.86132  ? 409 GLU B OE1  1 
ATOM   5497 O OE2  . GLU B 1 409 ? 127.58700 89.15800  66.05900  1.000 42.08285  ? 409 GLU B OE2  1 
ATOM   5498 N N    . VAL B 1 410 ? 124.75000 93.64500  68.67300  1.000 30.64667  ? 410 VAL B N    1 
ATOM   5499 C CA   . VAL B 1 410 ? 123.72000 94.67600  68.75300  1.000 33.97359  ? 410 VAL B CA   1 
ATOM   5500 C C    . VAL B 1 410 ? 123.96600 95.75500  67.70400  1.000 30.29334  ? 410 VAL B C    1 
ATOM   5501 O O    . VAL B 1 410 ? 123.02500 96.26100  67.07800  1.000 30.60959  ? 410 VAL B O    1 
ATOM   5502 C CB   . VAL B 1 410 ? 123.65500 95.25700  70.17900  1.000 29.03453  ? 410 VAL B CB   1 
ATOM   5503 C CG1  . VAL B 1 410 ? 124.96000 95.94500  70.54300  1.000 29.47198  ? 410 VAL B CG1  1 
ATOM   5504 C CG2  . VAL B 1 410 ? 122.47700 96.20500  70.31800  1.000 33.93207  ? 410 VAL B CG2  1 
ATOM   5505 N N    . HIS B 1 411 ? 125.23300 96.11100  67.47800  1.000 25.55479  ? 411 HIS B N    1 
ATOM   5506 C CA   . HIS B 1 411 ? 125.54500 97.09800  66.45100  1.000 29.05454  ? 411 HIS B CA   1 
ATOM   5507 C C    . HIS B 1 411 ? 125.20100 96.57300  65.06200  1.000 32.32639  ? 411 HIS B C    1 
ATOM   5508 O O    . HIS B 1 411 ? 124.63100 97.30100  64.23700  1.000 34.79220  ? 411 HIS B O    1 
ATOM   5509 C CB   . HIS B 1 411 ? 127.02100 97.48500  66.52900  1.000 25.78520  ? 411 HIS B CB   1 
ATOM   5510 C CG   . HIS B 1 411 ? 127.35800 98.35100  67.70200  1.000 31.19986  ? 411 HIS B CG   1 
ATOM   5511 N ND1  . HIS B 1 411 ? 128.63800 98.79300  67.95600  1.000 29.68202  ? 411 HIS B ND1  1 
ATOM   5512 C CD2  . HIS B 1 411 ? 126.58300 98.85300  68.69200  1.000 29.24834  ? 411 HIS B CD2  1 
ATOM   5513 C CE1  . HIS B 1 411 ? 128.63700 99.53300  69.05100  1.000 29.66888  ? 411 HIS B CE1  1 
ATOM   5514 N NE2  . HIS B 1 411 ? 127.40300 99.58500  69.51700  1.000 25.97060  ? 411 HIS B NE2  1 
ATOM   5515 N N    . LEU B 1 412 ? 125.51700 95.30300  64.79000  1.000 38.30919  ? 412 LEU B N    1 
ATOM   5516 C CA   . LEU B 1 412 ? 125.15000 94.72900  63.49900  1.000 39.11405  ? 412 LEU B CA   1 
ATOM   5517 C C    . LEU B 1 412 ? 123.63500 94.70600  63.32300  1.000 43.04965  ? 412 LEU B C    1 
ATOM   5518 O O    . LEU B 1 412 ? 123.12000 95.00300  62.23500  1.000 44.83679  ? 412 LEU B O    1 
ATOM   5519 C CB   . LEU B 1 412 ? 125.73500 93.32300  63.37200  1.000 40.92371  ? 412 LEU B CB   1 
ATOM   5520 C CG   . LEU B 1 412 ? 125.65000 92.64600  62.00500  1.000 42.47608  ? 412 LEU B CG   1 
ATOM   5521 C CD1  . LEU B 1 412 ? 126.85900 93.00300  61.15800  1.000 39.91770  ? 412 LEU B CD1  1 
ATOM   5522 C CD2  . LEU B 1 412 ? 125.53400 91.14000  62.16600  1.000 39.92047  ? 412 LEU B CD2  1 
ATOM   5523 N N    . ALA B 1 413 ? 122.90400 94.37400  64.39000  1.000 37.39892  ? 413 ALA B N    1 
ATOM   5524 C CA   . ALA B 1 413 ? 121.44700 94.35200  64.31700  1.000 36.10365  ? 413 ALA B CA   1 
ATOM   5525 C C    . ALA B 1 413 ? 120.89000 95.73600  64.01500  1.000 38.84709  ? 413 ALA B C    1 
ATOM   5526 O O    . ALA B 1 413 ? 119.97600 95.88100  63.19300  1.000 41.19094  ? 413 ALA B O    1 
ATOM   5527 C CB   . ALA B 1 413 ? 120.86400 93.81000  65.62200  1.000 28.32329  ? 413 ALA B CB   1 
ATOM   5528 N N    . ALA B 1 414 ? 121.43600 96.77200  64.65600  1.000 34.42299  ? 414 ALA B N    1 
ATOM   5529 C CA   . ALA B 1 414 ? 120.90400 98.11000  64.42800  1.000 32.46605  ? 414 ALA B CA   1 
ATOM   5530 C C    . ALA B 1 414 ? 121.26800 98.62300  63.04100  1.000 34.79181  ? 414 ALA B C    1 
ATOM   5531 O O    . ALA B 1 414 ? 120.48900 99.36800  62.43000  1.000 33.41347  ? 414 ALA B O    1 
ATOM   5532 C CB   . ALA B 1 414 ? 121.41300 99.07100  65.50200  1.000 30.22580  ? 414 ALA B CB   1 
ATOM   5533 N N    . GLU B 1 415 ? 122.40500 98.18600  62.49500  1.000 41.75779  ? 415 GLU B N    1 
ATOM   5534 C CA   . GLU B 1 415 ? 122.74700 98.60300  61.13900  1.000 39.92685  ? 415 GLU B CA   1 
ATOM   5535 C C    . GLU B 1 415 ? 121.85200 97.90800  60.12100  1.000 41.38755  ? 415 GLU B C    1 
ATOM   5536 O O    . GLU B 1 415 ? 121.44200 98.51600  59.12200  1.000 41.08139  ? 415 GLU B O    1 
ATOM   5537 C CB   . GLU B 1 415 ? 124.22100 98.31800  60.85500  1.000 38.55066  ? 415 GLU B CB   1 
ATOM   5538 C CG   . GLU B 1 415 ? 125.16600 99.40200  61.34700  1.000 41.05997  ? 415 GLU B CG   1 
ATOM   5539 C CD   . GLU B 1 415 ? 126.40100 98.83900  62.02000  1.000 48.55906  ? 415 GLU B CD   1 
ATOM   5540 O OE1  . GLU B 1 415 ? 126.76700 97.68300  61.72500  1.000 47.84676  ? 415 GLU B OE1  1 
ATOM   5541 O OE2  . GLU B 1 415 ? 127.00700 99.55200  62.84600  1.000 46.59489  ? 415 GLU B OE2  1 
ATOM   5542 N N    . GLU B 1 416 ? 121.49900 96.64700  60.38200  1.000 39.33865  ? 416 GLU B N    1 
ATOM   5543 C CA   . GLU B 1 416 ? 120.54900 95.96700  59.50800  1.000 38.28041  ? 416 GLU B CA   1 
ATOM   5544 C C    . GLU B 1 416 ? 119.17500 96.62200  59.58900  1.000 41.92819  ? 416 GLU B C    1 
ATOM   5545 O O    . GLU B 1 416 ? 118.48000 96.75100  58.57400  1.000 45.92895  ? 416 GLU B O    1 
ATOM   5546 C CB   . GLU B 1 416 ? 120.46500 94.48700  59.87200  1.000 39.70258  ? 416 GLU B CB   1 
ATOM   5547 C CG   . GLU B 1 416 ? 121.79200 93.75600  59.78100  1.000 44.17166  ? 416 GLU B CG   1 
ATOM   5548 C CD   . GLU B 1 416 ? 121.66200 92.27900  60.08300  1.000 48.45819  ? 416 GLU B CD   1 
ATOM   5549 O OE1  . GLU B 1 416 ? 120.54800 91.83900  60.43900  1.000 50.76301  ? 416 GLU B OE1  1 
ATOM   5550 O OE2  . GLU B 1 416 ? 122.67400 91.55600  59.96400  1.000 43.96814  ? 416 GLU B OE2  1 
ATOM   5551 N N    . LEU B 1 417 ? 118.76600 97.03200  60.79100  1.000 38.39231  ? 417 LEU B N    1 
ATOM   5552 C CA   . LEU B 1 417 ? 117.50800 97.75800  60.94300  1.000 34.34029  ? 417 LEU B CA   1 
ATOM   5553 C C    . LEU B 1 417 ? 117.50800 99.03800  60.11400  1.000 33.49802  ? 417 LEU B C    1 
ATOM   5554 O O    . LEU B 1 417 ? 116.53400 99.33800  59.41200  1.000 32.74372  ? 417 LEU B O    1 
ATOM   5555 C CB   . LEU B 1 417 ? 117.25600 98.07300  62.41700  1.000 35.29783  ? 417 LEU B CB   1 
ATOM   5556 C CG   . LEU B 1 417 ? 115.92500 98.75600  62.74300  1.000 35.73833  ? 417 LEU B CG   1 
ATOM   5557 C CD1  . LEU B 1 417 ? 114.75400 97.98000  62.16300  1.000 36.51933  ? 417 LEU B CD1  1 
ATOM   5558 C CD2  . LEU B 1 417 ? 115.76500 98.92800  64.24200  1.000 34.77032  ? 417 LEU B CD2  1 
ATOM   5559 N N    . GLN B 1 418 ? 118.58300 99.82500  60.21000  1.000 40.95872  ? 418 GLN B N    1 
ATOM   5560 C CA   . GLN B 1 418 ? 118.66000 101.05700 59.42900  1.000 41.23497  ? 418 GLN B CA   1 
ATOM   5561 C C    . GLN B 1 418 ? 118.60800 100.77800 57.92900  1.000 44.27040  ? 418 GLN B C    1 
ATOM   5562 O O    . GLN B 1 418 ? 117.92800 101.49100 57.18100  1.000 43.95757  ? 418 GLN B O    1 
ATOM   5563 C CB   . GLN B 1 418 ? 119.93200 101.82500 59.78700  1.000 42.09556  ? 418 GLN B CB   1 
ATOM   5564 C CG   . GLN B 1 418 ? 119.97700 103.24500 59.24600  1.000 43.67705  ? 418 GLN B CG   1 
ATOM   5565 C CD   . GLN B 1 418 ? 118.75800 104.05800 59.63400  1.000 49.99943  ? 418 GLN B CD   1 
ATOM   5566 O OE1  . GLN B 1 418 ? 118.11800 104.68100 58.78800  1.000 47.23512  ? 418 GLN B OE1  1 
ATOM   5567 N NE2  . GLN B 1 418 ? 118.43000 104.05400 60.92100  1.000 46.26978  ? 418 GLN B NE2  1 
ATOM   5568 N N    . HIS B 1 419 ? 119.31500 99.74100  57.46900  1.000 51.74964  ? 419 HIS B N    1 
ATOM   5569 C CA   . HIS B 1 419 ? 119.24900 99.38800  56.05200  1.000 50.35199  ? 419 HIS B CA   1 
ATOM   5570 C C    . HIS B 1 419 ? 117.82900 99.02200  55.63400  1.000 50.95040  ? 419 HIS B C    1 
ATOM   5571 O O    . HIS B 1 419 ? 117.34800 99.45800  54.57800  1.000 48.64211  ? 419 HIS B O    1 
ATOM   5572 C CB   . HIS B 1 419 ? 120.20700 98.23700  55.74500  1.000 48.95434  ? 419 HIS B CB   1 
ATOM   5573 C CG   . HIS B 1 419 ? 121.65100 98.63000  55.76000  1.000 52.74103  ? 419 HIS B CG   1 
ATOM   5574 N ND1  . HIS B 1 419 ? 122.67300 97.70600  55.77700  1.000 51.64542  ? 419 HIS B ND1  1 
ATOM   5575 C CD2  . HIS B 1 419 ? 122.24400 99.84700  55.75400  1.000 53.52396  ? 419 HIS B CD2  1 
ATOM   5576 C CE1  . HIS B 1 419 ? 123.83400 98.33700  55.78300  1.000 51.59898  ? 419 HIS B CE1  1 
ATOM   5577 N NE2  . HIS B 1 419 ? 123.60200 99.63700  55.77000  1.000 53.50662  ? 419 HIS B NE2  1 
ATOM   5578 N N    . LYS B 1 420 ? 117.13600 98.23200  56.45700  1.000 47.16462  ? 420 LYS B N    1 
ATOM   5579 C CA   . LYS B 1 420 ? 115.76800 97.85100  56.12000  1.000 47.55545  ? 420 LYS B CA   1 
ATOM   5580 C C    . LYS B 1 420 ? 114.86100 99.07100  56.05900  1.000 51.34061  ? 420 LYS B C    1 
ATOM   5581 O O    . LYS B 1 420 ? 114.01200 99.17800  55.16600  1.000 53.54204  ? 420 LYS B O    1 
ATOM   5582 C CB   . LYS B 1 420 ? 115.23800 96.83400  57.13000  1.000 50.56370  ? 420 LYS B CB   1 
ATOM   5583 C CG   . LYS B 1 420 ? 113.82100 96.37200  56.84600  1.000 50.35661  ? 420 LYS B CG   1 
ATOM   5584 C CD   . LYS B 1 420 ? 113.73100 95.67000  55.50200  1.000 49.84748  ? 420 LYS B CD   1 
ATOM   5585 C CE   . LYS B 1 420 ? 112.49900 94.78400  55.42300  1.000 52.91772  ? 420 LYS B CE   1 
ATOM   5586 N NZ   . LYS B 1 420 ? 112.82200 93.43300  54.88900  1.000 51.47602  ? 420 LYS B NZ   1 
ATOM   5587 N N    . ILE B 1 421 ? 115.02000 100.00200 57.00100  1.000 48.79090  ? 421 ILE B N    1 
ATOM   5588 C CA   . ILE B 1 421 ? 114.17700 101.19400 56.99300  1.000 46.34593  ? 421 ILE B CA   1 
ATOM   5589 C C    . ILE B 1 421 ? 114.44900 102.01600 55.74100  1.000 41.91712  ? 421 ILE B C    1 
ATOM   5590 O O    . ILE B 1 421 ? 113.52700 102.56700 55.12700  1.000 41.99086  ? 421 ILE B O    1 
ATOM   5591 C CB   . ILE B 1 421 ? 114.39100 102.02400 58.27300  1.000 46.75491  ? 421 ILE B CB   1 
ATOM   5592 C CG1  . ILE B 1 421 ? 114.02400 101.20800 59.51200  1.000 44.44965  ? 421 ILE B CG1  1 
ATOM   5593 C CG2  . ILE B 1 421 ? 113.57200 103.30300 58.22200  1.000 43.05374  ? 421 ILE B CG2  1 
ATOM   5594 C CD1  . ILE B 1 421 ? 114.42100 101.87000 60.81200  1.000 44.28533  ? 421 ILE B CD1  1 
ATOM   5595 N N    . ASP B 1 422 ? 115.71900 102.10900 55.34100  1.000 54.56665  ? 422 ASP B N    1 
ATOM   5596 C CA   . ASP B 1 422 ? 116.06200 102.85900 54.13600  1.000 55.58660  ? 422 ASP B CA   1 
ATOM   5597 C C    . ASP B 1 422 ? 115.47400 102.21200 52.88700  1.000 54.83807  ? 422 ASP B C    1 
ATOM   5598 O O    . ASP B 1 422 ? 115.07700 102.91300 51.94800  1.000 49.49765  ? 422 ASP B O    1 
ATOM   5599 C CB   . ASP B 1 422 ? 117.57900 102.98300 54.01000  1.000 54.21221  ? 422 ASP B CB   1 
ATOM   5600 C CG   . ASP B 1 422 ? 118.10600 104.28300 54.57900  1.000 57.36406  ? 422 ASP B CG   1 
ATOM   5601 O OD1  . ASP B 1 422 ? 117.33200 104.99200 55.25600  1.000 59.68541  ? 422 ASP B OD1  1 
ATOM   5602 O OD2  . ASP B 1 422 ? 119.29300 104.59600 54.35200  1.000 56.95795  ? 422 ASP B OD2  1 
ATOM   5603 N N    . LYS B 1 423 ? 115.40800 100.87900 52.85300  1.000 59.85130  ? 423 LYS B N    1 
ATOM   5604 C CA   . LYS B 1 423 ? 114.85800 100.20300 51.67900  1.000 57.70014  ? 423 LYS B CA   1 
ATOM   5605 C C    . LYS B 1 423 ? 113.35700 100.43900 51.52700  1.000 57.75037  ? 423 LYS B C    1 
ATOM   5606 O O    . LYS B 1 423 ? 112.85600 100.54600 50.40200  1.000 56.67454  ? 423 LYS B O    1 
ATOM   5607 C CB   . LYS B 1 423 ? 115.15600 98.70500  51.74600  1.000 57.06597  ? 423 LYS B CB   1 
ATOM   5608 C CG   . LYS B 1 423 ? 116.30600 98.26000  50.85700  1.000 56.08526  ? 423 LYS B CG   1 
ATOM   5609 C CD   . LYS B 1 423 ? 117.52100 99.16000  51.01000  1.000 59.40389  ? 423 LYS B CD   1 
ATOM   5610 C CE   . LYS B 1 423 ? 118.54300 98.55500  51.95800  1.000 60.27152  ? 423 LYS B CE   1 
ATOM   5611 N NZ   . LYS B 1 423 ? 119.68700 99.47800  52.20100  1.000 59.36292  ? 423 LYS B NZ   1 
ATOM   5612 N N    . LYS B 1 424 ? 112.62300 100.52300 52.63500  1.000 61.30192  ? 424 LYS B N    1 
ATOM   5613 C CA   . LYS B 1 424 ? 111.17000 100.65900 52.57200  1.000 58.29649  ? 424 LYS B CA   1 
ATOM   5614 C C    . LYS B 1 424 ? 110.66300 101.89300 53.30800  1.000 57.73324  ? 424 LYS B C    1 
ATOM   5615 O O    . LYS B 1 424 ? 109.82900 101.78100 54.21200  1.000 61.66101  ? 424 LYS B O    1 
ATOM   5616 C CB   . LYS B 1 424 ? 110.49600 99.40500  53.13300  1.000 57.89945  ? 424 LYS B CB   1 
ATOM   5617 C CG   . LYS B 1 424 ? 110.14800 98.37100  52.07900  1.000 59.79564  ? 424 LYS B CG   1 
ATOM   5618 C CD   . LYS B 1 424 ? 110.53600 96.97200  52.52000  1.000 59.17875  ? 424 LYS B CD   1 
ATOM   5619 C CE   . LYS B 1 424 ? 110.84000 96.08700  51.32300  1.000 59.22678  ? 424 LYS B CE   1 
ATOM   5620 N NZ   . LYS B 1 424 ? 109.70600 96.05400  50.35900  1.000 59.31051  ? 424 LYS B NZ   1 
ATOM   5621 N N    . SER B 1 425 ? 111.14800 103.07300 52.92800  1.000 58.18321  ? 425 SER B N    1 
ATOM   5622 C CA   . SER B 1 425 ? 110.76700 104.31100 53.59500  1.000 59.22308  ? 425 SER B CA   1 
ATOM   5623 C C    . SER B 1 425 ? 109.60200 105.02400 52.92200  1.000 60.72727  ? 425 SER B C    1 
ATOM   5624 O O    . SER B 1 425 ? 109.18800 106.08400 53.40200  1.000 61.47400  ? 425 SER B O    1 
ATOM   5625 C CB   . SER B 1 425 ? 111.96800 105.26000 53.67200  1.000 57.62691  ? 425 SER B CB   1 
ATOM   5626 O OG   . SER B 1 425 ? 112.51300 105.50000 52.38700  1.000 58.06536  ? 425 SER B OG   1 
ATOM   5627 N N    . TYR B 1 426 ? 109.06100 104.48100 51.83200  1.000 61.91469  ? 426 TYR B N    1 
ATOM   5628 C CA   . TYR B 1 426 ? 107.92400 105.10800 51.17100  1.000 61.20391  ? 426 TYR B CA   1 
ATOM   5629 C C    . TYR B 1 426 ? 106.60600 104.82200 51.87700  1.000 62.03186  ? 426 TYR B C    1 
ATOM   5630 O O    . TYR B 1 426 ? 105.56000 105.30000 51.42500  1.000 62.26888  ? 426 TYR B O    1 
ATOM   5631 C CB   . TYR B 1 426 ? 107.84100 104.65800 49.70700  1.000 60.14503  ? 426 TYR B CB   1 
ATOM   5632 C CG   . TYR B 1 426 ? 107.72000 103.16400 49.50800  1.000 59.47387  ? 426 TYR B CG   1 
ATOM   5633 C CD1  . TYR B 1 426 ? 106.52500 102.50300 49.76200  1.000 59.33123  ? 426 TYR B CD1  1 
ATOM   5634 C CD2  . TYR B 1 426 ? 108.79100 102.41900 49.04000  1.000 60.18452  ? 426 TYR B CD2  1 
ATOM   5635 C CE1  . TYR B 1 426 ? 106.40700 101.14200 49.57400  1.000 60.96683  ? 426 TYR B CE1  1 
ATOM   5636 C CE2  . TYR B 1 426 ? 108.68300 101.05600 48.84900  1.000 60.25882  ? 426 TYR B CE2  1 
ATOM   5637 C CZ   . TYR B 1 426 ? 107.48800 100.42300 49.11700  1.000 61.23498  ? 426 TYR B CZ   1 
ATOM   5638 O OH   . TYR B 1 426 ? 107.37300 99.06500  48.92900  1.000 63.54836  ? 426 TYR B OH   1 
ATOM   5639 N N    . LEU B 1 427 ? 106.63300 104.05800 52.96500  1.000 58.83186  ? 427 LEU B N    1 
ATOM   5640 C CA   . LEU B 1 427 ? 105.44500 103.72000 53.73500  1.000 56.47852  ? 427 LEU B CA   1 
ATOM   5641 C C    . LEU B 1 427 ? 105.20000 104.67900 54.89100  1.000 58.12862  ? 427 LEU B C    1 
ATOM   5642 O O    . LEU B 1 427 ? 104.20800 104.52200 55.61000  1.000 58.06476  ? 427 LEU B O    1 
ATOM   5643 C CB   . LEU B 1 427 ? 105.55400 102.29000 54.27500  1.000 57.26508  ? 427 LEU B CB   1 
ATOM   5644 C CG   . LEU B 1 427 ? 105.75500 101.17400 53.25100  1.000 57.26375  ? 427 LEU B CG   1 
ATOM   5645 C CD1  . LEU B 1 427 ? 105.96400 99.84100  53.95200  1.000 56.62163  ? 427 LEU B CD1  1 
ATOM   5646 C CD2  . LEU B 1 427 ? 104.56900 101.10300 52.30500  1.000 57.40935  ? 427 LEU B CD2  1 
ATOM   5647 N N    . LEU B 1 428 ? 106.07800 105.66400 55.08800  1.000 54.38162  ? 428 LEU B N    1 
ATOM   5648 C CA   . LEU B 1 428 ? 105.96000 106.59900 56.19600  1.000 52.84701  ? 428 LEU B CA   1 
ATOM   5649 C C    . LEU B 1 428 ? 105.60400 108.01400 55.76800  1.000 53.55473  ? 428 LEU B C    1 
ATOM   5650 O O    . LEU B 1 428 ? 105.14600 108.79600 56.60800  1.000 54.78006  ? 428 LEU B O    1 
ATOM   5651 C CB   . LEU B 1 428 ? 107.27000 106.64100 56.99700  1.000 56.09049  ? 428 LEU B CB   1 
ATOM   5652 C CG   . LEU B 1 428 ? 107.93300 105.29200 57.28900  1.000 56.13049  ? 428 LEU B CG   1 
ATOM   5653 C CD1  . LEU B 1 428 ? 109.38000 105.48500 57.71300  1.000 53.95478  ? 428 LEU B CD1  1 
ATOM   5654 C CD2  . LEU B 1 428 ? 107.15900 104.51900 58.34400  1.000 54.30104  ? 428 LEU B CD2  1 
ATOM   5655 N N    . VAL B 1 429 ? 105.79400 108.36100 54.49700  1.000 70.15886  ? 429 VAL B N    1 
ATOM   5656 C CA   . VAL B 1 429 ? 105.52800 109.69600 53.99000  1.000 70.40200  ? 429 VAL B CA   1 
ATOM   5657 C C    . VAL B 1 429 ? 104.57200 109.58900 52.80600  1.000 69.51288  ? 429 VAL B C    1 
ATOM   5658 O O    . VAL B 1 429 ? 104.17900 108.49900 52.39400  1.000 67.88549  ? 429 VAL B O    1 
ATOM   5659 C CB   . VAL B 1 429 ? 106.82100 110.43700 53.58900  1.000 70.31718  ? 429 VAL B CB   1 
ATOM   5660 C CG1  . VAL B 1 429 ? 107.76700 110.53400 54.77700  1.000 69.56998  ? 429 VAL B CG1  1 
ATOM   5661 C CG2  . VAL B 1 429 ? 107.49000 109.73700 52.41700  1.000 68.47138  ? 429 VAL B CG2  1 
ATOM   5662 N N    . ASN B 1 430 ? 104.19600 110.74700 52.26500  1.000 89.88044  ? 430 ASN B N    1 
ATOM   5663 C CA   . ASN B 1 430 ? 103.32000 110.83900 51.10000  1.000 89.28419  ? 430 ASN B CA   1 
ATOM   5664 C C    . ASN B 1 430 ? 104.06400 111.57500 49.99400  1.000 89.23786  ? 430 ASN B C    1 
ATOM   5665 O O    . ASN B 1 430 ? 104.29600 112.78500 50.09500  1.000 89.99569  ? 430 ASN B O    1 
ATOM   5666 C CB   . ASN B 1 430 ? 102.01500 111.55100 51.45200  1.000 89.43061  ? 430 ASN B CB   1 
ATOM   5667 C CG   . ASN B 1 430 ? 101.06100 110.66700 52.23000  1.000 89.85074  ? 430 ASN B CG   1 
ATOM   5668 O OD1  . ASN B 1 430 ? 101.06600 110.66100 53.46100  1.000 89.36160  ? 430 ASN B OD1  1 
ATOM   5669 N ND2  . ASN B 1 430 ? 100.23600 109.91200 51.51300  1.000 89.75262  ? 430 ASN B ND2  1 
ATOM   5670 N N    . SER B 1 431 ? 104.43900 110.84700 48.94100  1.000 96.96271  ? 431 SER B N    1 
ATOM   5671 C CA   . SER B 1 431 ? 105.20800 111.43800 47.85400  1.000 97.51942  ? 431 SER B CA   1 
ATOM   5672 C C    . SER B 1 431 ? 104.35200 112.26200 46.90100  1.000 98.27396  ? 431 SER B C    1 
ATOM   5673 O O    . SER B 1 431 ? 104.89200 113.10700 46.17900  1.000 99.58084  ? 431 SER B O    1 
ATOM   5674 C CB   . SER B 1 431 ? 105.93600 110.34400 47.07000  1.000 97.02939  ? 431 SER B CB   1 
ATOM   5675 O OG   . SER B 1 431 ? 105.08500 109.23700 46.83000  1.000 97.76609  ? 431 SER B OG   1 
ATOM   5676 N N    . GLU B 1 432 ? 103.03600 112.03800 46.87900  1.000 99.96764  ? 432 GLU B N    1 
ATOM   5677 C CA   . GLU B 1 432 ? 102.17600 112.78300 45.96500  1.000 99.56028  ? 432 GLU B CA   1 
ATOM   5678 C C    . GLU B 1 432 ? 102.22700 114.27900 46.24700  1.000 99.51879  ? 432 GLU B C    1 
ATOM   5679 O O    . GLU B 1 432 ? 102.20100 115.09400 45.31800  1.000 99.16163  ? 432 GLU B O    1 
ATOM   5680 C CB   . GLU B 1 432 ? 100.73900 112.27000 46.05800  1.000 99.66809  ? 432 GLU B CB   1 
ATOM   5681 C CG   . GLU B 1 432 ? 100.35500 111.73200 47.42500  1.000 99.99339  ? 432 GLU B CG   1 
ATOM   5682 C CD   . GLU B 1 432 ? 100.41700 110.21900 47.49300  1.000 100.94137 ? 432 GLU B CD   1 
ATOM   5683 O OE1  . GLU B 1 432 ? 101.48100 109.65200 47.16900  1.000 100.27571 ? 432 GLU B OE1  1 
ATOM   5684 O OE2  . GLU B 1 432 ? 99.40200  109.59800 47.87000  1.000 101.68819 ? 432 GLU B OE2  1 
ATOM   5685 N N    . CYS B 1 433 ? 102.30000 114.66000 47.52100  1.000 99.39076  ? 433 CYS B N    1 
ATOM   5686 C CA   . CYS B 1 433 ? 102.27400 116.06600 47.90400  1.000 99.42768  ? 433 CYS B CA   1 
ATOM   5687 C C    . CYS B 1 433 ? 103.63400 116.74500 47.79600  1.000 99.09863  ? 433 CYS B C    1 
ATOM   5688 O O    . CYS B 1 433 ? 103.71900 117.95600 48.02800  1.000 98.65585  ? 433 CYS B O    1 
ATOM   5689 C CB   . CYS B 1 433 ? 101.74400 116.20800 49.33300  1.000 98.64802  ? 433 CYS B CB   1 
ATOM   5690 S SG   . CYS B 1 433 ? 100.02200 115.70400 49.54500  1.000 101.28205 ? 433 CYS B SG   1 
ATOM   5691 N N    . TRP B 1 434 ? 104.68900 116.00500 47.46300  1.000 96.21979  ? 434 TRP B N    1 
ATOM   5692 C CA   . TRP B 1 434 ? 106.02600 116.58500 47.41800  1.000 96.29522  ? 434 TRP B CA   1 
ATOM   5693 C C    . TRP B 1 434 ? 106.06000 117.79000 46.48600  1.000 97.24906  ? 434 TRP B C    1 
ATOM   5694 O O    . TRP B 1 434 ? 105.58200 117.72800 45.35000  1.000 96.89474  ? 434 TRP B O    1 
ATOM   5695 C CB   . TRP B 1 434 ? 107.04300 115.53800 46.96700  1.000 95.01900  ? 434 TRP B CB   1 
ATOM   5696 C CG   . TRP B 1 434 ? 107.66700 114.79300 48.10300  1.000 95.76045  ? 434 TRP B CG   1 
ATOM   5697 C CD1  . TRP B 1 434 ? 107.57100 115.09300 49.42900  1.000 95.55487  ? 434 TRP B CD1  1 
ATOM   5698 C CD2  . TRP B 1 434 ? 108.49900 113.63100 48.01300  1.000 97.08600  ? 434 TRP B CD2  1 
ATOM   5699 N NE1  . TRP B 1 434 ? 108.28200 114.18400 50.17300  1.000 95.24961  ? 434 TRP B NE1  1 
ATOM   5700 C CE2  . TRP B 1 434 ? 108.86400 113.27700 49.32700  1.000 96.18869  ? 434 TRP B CE2  1 
ATOM   5701 C CE3  . TRP B 1 434 ? 108.96900 112.85400 46.95000  1.000 96.31452  ? 434 TRP B CE3  1 
ATOM   5702 C CZ2  . TRP B 1 434 ? 109.67500 112.18100 49.60600  1.000 96.12470  ? 434 TRP B CZ2  1 
ATOM   5703 C CZ3  . TRP B 1 434 ? 109.77400 111.76600 47.23000  1.000 95.92743  ? 434 TRP B CZ3  1 
ATOM   5704 C CH2  . TRP B 1 434 ? 110.11900 111.44000 48.54700  1.000 96.05220  ? 434 TRP B CH2  1 
ATOM   5705 N N    . GLU B 1 435 ? 106.63000 118.88800 46.97300  1.000 101.95974 ? 435 GLU B N    1 
ATOM   5706 C CA   . GLU B 1 435 ? 106.73800 120.10900 46.18300  1.000 101.27337 ? 435 GLU B CA   1 
ATOM   5707 C C    . GLU B 1 435 ? 108.14600 120.68900 46.26400  1.000 101.24296 ? 435 GLU B C    1 
ATOM   5708 O O    . GLU B 1 435 ? 108.59000 121.12000 47.32800  1.000 100.54098 ? 435 GLU B O    1 
ATOM   5709 C CB   . GLU B 1 435 ? 105.71500 121.14500 46.65100  1.000 101.76522 ? 435 GLU B CB   1 
ATOM   5710 C CG   . GLU B 1 435 ? 105.79400 121.47300 48.13200  1.000 102.14223 ? 435 GLU B CG   1 
ATOM   5711 C CD   . GLU B 1 435 ? 105.31100 122.87500 48.44500  1.000 102.13584 ? 435 GLU B CD   1 
ATOM   5712 O OE1  . GLU B 1 435 ? 104.09700 123.13100 48.30700  1.000 101.35878 ? 435 GLU B OE1  1 
ATOM   5713 O OE2  . GLU B 1 435 ? 106.14600 123.72100 48.82900  1.000 101.90222 ? 435 GLU B OE2  1 
ATOM   5714 N N    . LYS B 1 527 ? 94.63700  113.45100 54.64100  1.000 80.91224  ? 527 LYS B N    1 
ATOM   5715 C CA   . LYS B 1 527 ? 94.11500  113.50900 56.00200  1.000 81.43554  ? 527 LYS B CA   1 
ATOM   5716 C C    . LYS B 1 527 ? 95.25400  113.66500 57.00500  1.000 81.49774  ? 527 LYS B C    1 
ATOM   5717 O O    . LYS B 1 527 ? 96.33800  113.11300 56.81900  1.000 80.91974  ? 527 LYS B O    1 
ATOM   5718 C CB   . LYS B 1 527 ? 93.29500  112.25800 56.31800  1.000 81.39817  ? 527 LYS B CB   1 
ATOM   5719 C CG   . LYS B 1 527 ? 92.66400  112.25800 57.70100  1.000 80.59952  ? 527 LYS B CG   1 
ATOM   5720 C CD   . LYS B 1 527 ? 91.77100  113.47300 57.89600  1.000 80.33800  ? 527 LYS B CD   1 
ATOM   5721 C CE   . LYS B 1 527 ? 91.93400  114.06600 59.28600  1.000 80.80649  ? 527 LYS B CE   1 
ATOM   5722 N NZ   . LYS B 1 527 ? 91.60500  113.07900 60.35100  1.000 80.67914  ? 527 LYS B NZ   1 
ATOM   5723 N N    . THR B 1 528 ? 95.00000  114.42600 58.07100  1.000 77.78230  ? 528 THR B N    1 
ATOM   5724 C CA   . THR B 1 528 ? 96.00800  114.61200 59.11000  1.000 78.19156  ? 528 THR B CA   1 
ATOM   5725 C C    . THR B 1 528 ? 96.25300  113.31900 59.88000  1.000 77.83907  ? 528 THR B C    1 
ATOM   5726 O O    . THR B 1 528 ? 97.40500  112.94200 60.13200  1.000 79.02716  ? 528 THR B O    1 
ATOM   5727 C CB   . THR B 1 528 ? 95.58000  115.73000 60.06200  1.000 77.50905  ? 528 THR B CB   1 
ATOM   5728 O OG1  . THR B 1 528 ? 95.55500  116.97800 59.35700  1.000 76.64072  ? 528 THR B OG1  1 
ATOM   5729 C CG2  . THR B 1 528 ? 96.54700  115.83400 61.23300  1.000 76.84825  ? 528 THR B CG2  1 
ATOM   5730 N N    . TYR B 1 529 ? 95.17800  112.62400 60.25900  1.000 69.44143  ? 529 TYR B N    1 
ATOM   5731 C CA   . TYR B 1 529 ? 95.33100  111.41300 61.05900  1.000 70.15518  ? 529 TYR B CA   1 
ATOM   5732 C C    . TYR B 1 529 ? 96.11800  110.34900 60.30500  1.000 71.58908  ? 529 TYR B C    1 
ATOM   5733 O O    . TYR B 1 529 ? 96.97600  109.67700 60.88600  1.000 72.57857  ? 529 TYR B O    1 
ATOM   5734 C CB   . TYR B 1 529 ? 93.96400  110.87400 61.47600  1.000 69.40845  ? 529 TYR B CB   1 
ATOM   5735 C CG   . TYR B 1 529 ? 94.05100  109.73100 62.46200  1.000 71.71519  ? 529 TYR B CG   1 
ATOM   5736 C CD1  . TYR B 1 529 ? 94.48000  109.94600 63.76500  1.000 70.44333  ? 529 TYR B CD1  1 
ATOM   5737 C CD2  . TYR B 1 529 ? 93.71700  108.43600 62.08800  1.000 71.93758  ? 529 TYR B CD2  1 
ATOM   5738 C CE1  . TYR B 1 529 ? 94.56700  108.90600 64.67000  1.000 70.46107  ? 529 TYR B CE1  1 
ATOM   5739 C CE2  . TYR B 1 529 ? 93.80200  107.38900 62.98700  1.000 71.97488  ? 529 TYR B CE2  1 
ATOM   5740 C CZ   . TYR B 1 529 ? 94.22800  107.63000 64.27700  1.000 71.04439  ? 529 TYR B CZ   1 
ATOM   5741 O OH   . TYR B 1 529 ? 94.31400  106.59300 65.17600  1.000 68.58081  ? 529 TYR B OH   1 
ATOM   5742 N N    . GLU B 1 530 ? 95.81600  110.15700 59.02000  1.000 70.98729  ? 530 GLU B N    1 
ATOM   5743 C CA   . GLU B 1 530 ? 96.52700  109.15600 58.23000  1.000 70.77201  ? 530 GLU B CA   1 
ATOM   5744 C C    . GLU B 1 530 ? 98.02600  109.44100 58.20500  1.000 72.42911  ? 530 GLU B C    1 
ATOM   5745 O O    . GLU B 1 530 ? 98.85100  108.54400 58.43000  1.000 72.59220  ? 530 GLU B O    1 
ATOM   5746 C CB   . GLU B 1 530 ? 95.95700  109.11300 56.81200  1.000 70.55310  ? 530 GLU B CB   1 
ATOM   5747 C CG   . GLU B 1 530 ? 96.24700  107.82700 56.05900  1.000 71.81334  ? 530 GLU B CG   1 
ATOM   5748 C CD   . GLU B 1 530 ? 96.01100  107.96300 54.56800  1.000 73.10402  ? 530 GLU B CD   1 
ATOM   5749 O OE1  . GLU B 1 530 ? 95.25200  108.86900 54.16400  1.000 73.23237  ? 530 GLU B OE1  1 
ATOM   5750 O OE2  . GLU B 1 530 ? 96.58600  107.16400 53.79900  1.000 72.82001  ? 530 GLU B OE2  1 
ATOM   5751 N N    . SER B 1 531 ? 98.39600  110.69500 57.93100  1.000 61.61834  ? 531 SER B N    1 
ATOM   5752 C CA   . SER B 1 531 ? 99.80900  111.04700 57.86000  1.000 63.37677  ? 531 SER B CA   1 
ATOM   5753 C C    . SER B 1 531 ? 100.48900 110.88600 59.21300  1.000 62.66345  ? 531 SER B C    1 
ATOM   5754 O O    . SER B 1 531 ? 101.62900 110.41100 59.28600  1.000 65.23478  ? 531 SER B O    1 
ATOM   5755 C CB   . SER B 1 531 ? 99.96600  112.47700 57.34500  1.000 64.94334  ? 531 SER B CB   1 
ATOM   5756 O OG   . SER B 1 531 ? 99.50800  112.59200 56.01000  1.000 64.98516  ? 531 SER B OG   1 
ATOM   5757 N N    . ALA B 1 532 ? 99.80800  111.26100 60.29900  1.000 51.10019  ? 532 ALA B N    1 
ATOM   5758 C CA   . ALA B 1 532 ? 100.42300 111.10800 61.61400  1.000 52.57413  ? 532 ALA B CA   1 
ATOM   5759 C C    . ALA B 1 532 ? 100.58100 109.63600 61.97400  1.000 54.24892  ? 532 ALA B C    1 
ATOM   5760 O O    . ALA B 1 532 ? 101.58900 109.23600 62.57200  1.000 55.17312  ? 532 ALA B O    1 
ATOM   5761 C CB   . ALA B 1 532 ? 99.59400  111.84000 62.66800  1.000 52.18885  ? 532 ALA B CB   1 
ATOM   5762 N N    . SER B 1 533 ? 99.61700  108.80500 61.57400  1.000 49.29026  ? 533 SER B N    1 
ATOM   5763 C CA   . SER B 1 533 ? 99.70900  107.38100 61.86500  1.000 49.19496  ? 533 SER B CA   1 
ATOM   5764 C C    . SER B 1 533 ? 100.84900 106.74900 61.08400  1.000 51.63614  ? 533 SER B C    1 
ATOM   5765 O O    . SER B 1 533 ? 101.52400 105.84100 61.58200  1.000 53.30765  ? 533 SER B O    1 
ATOM   5766 C CB   . SER B 1 533 ? 98.38400  106.69100 61.54300  1.000 50.72407  ? 533 SER B CB   1 
ATOM   5767 O OG   . SER B 1 533 ? 97.29300  107.39600 62.10700  1.000 49.76372  ? 533 SER B OG   1 
ATOM   5768 N N    . ALA B 1 534 ? 101.08000 107.21900 59.85700  1.000 48.33482  ? 534 ALA B N    1 
ATOM   5769 C CA   . ALA B 1 534 ? 102.20800 106.70400 59.09000  1.000 47.02654  ? 534 ALA B CA   1 
ATOM   5770 C C    . ALA B 1 534 ? 103.53300 107.17200 59.68100  1.000 49.10023  ? 534 ALA B C    1 
ATOM   5771 O O    . ALA B 1 534 ? 104.50100 106.40500 59.73300  1.000 49.59378  ? 534 ALA B O    1 
ATOM   5772 C CB   . ALA B 1 534 ? 102.08800 107.13000 57.62800  1.000 47.25870  ? 534 ALA B CB   1 
ATOM   5773 N N    . LEU B 1 535 ? 103.59600 108.42400 60.13700  1.000 40.18054  ? 535 LEU B N    1 
ATOM   5774 C CA   . LEU B 1 535 ? 104.81100 108.96400 60.73600  1.000 39.70829  ? 535 LEU B CA   1 
ATOM   5775 C C    . LEU B 1 535 ? 105.06600 108.46100 62.15400  1.000 38.87294  ? 535 LEU B C    1 
ATOM   5776 O O    . LEU B 1 535 ? 106.12800 108.75400 62.71300  1.000 40.23525  ? 535 LEU B O    1 
ATOM   5777 C CB   . LEU B 1 535 ? 104.75600 110.49400 60.74000  1.000 38.74114  ? 535 LEU B CB   1 
ATOM   5778 C CG   . LEU B 1 535 ? 106.09400 111.22900 60.64500  1.000 39.79218  ? 535 LEU B CG   1 
ATOM   5779 C CD1  . LEU B 1 535 ? 106.61500 111.21700 59.21700  1.000 38.75569  ? 535 LEU B CD1  1 
ATOM   5780 C CD2  . LEU B 1 535 ? 105.96100 112.65400 61.15600  1.000 39.14889  ? 535 LEU B CD2  1 
ATOM   5781 N N    . SER B 1 536 ? 104.12500 107.72400 62.74700  1.000 29.50102  ? 536 SER B N    1 
ATOM   5782 C CA   . SER B 1 536 ? 104.31500 107.23000 64.11000  1.000 30.69508  ? 536 SER B CA   1 
ATOM   5783 C C    . SER B 1 536 ? 105.29700 106.06100 64.21200  1.000 35.66331  ? 536 SER B C    1 
ATOM   5784 O O    . SER B 1 536 ? 105.91500 105.87900 65.26600  1.000 35.90159  ? 536 SER B O    1 
ATOM   5785 C CB   . SER B 1 536 ? 102.96600 106.81700 64.69900  1.000 30.25257  ? 536 SER B CB   1 
ATOM   5786 O OG   . SER B 1 536 ? 102.27600 107.93500 65.22400  1.000 28.80655  ? 536 SER B OG   1 
ATOM   5787 N N    . LEU B 1 537 ? 105.44800 105.25400 63.15800  1.000 29.27676  ? 537 LEU B N    1 
ATOM   5788 C CA   . LEU B 1 537 ? 106.38000 104.12400 63.20300  1.000 27.22704  ? 537 LEU B CA   1 
ATOM   5789 C C    . LEU B 1 537 ? 107.83500 104.58500 63.26700  1.000 28.10127  ? 537 LEU B C    1 
ATOM   5790 O O    . LEU B 1 537 ? 108.66800 103.97100 63.95800  1.000 30.22662  ? 537 LEU B O    1 
ATOM   5791 C CB   . LEU B 1 537 ? 106.15300 103.22300 61.98800  1.000 28.65393  ? 537 LEU B CB   1 
ATOM   5792 C CG   . LEU B 1 537 ? 106.78500 101.83000 61.99200  1.000 32.68188  ? 537 LEU B CG   1 
ATOM   5793 C CD1  . LEU B 1 537 ? 105.75100 100.77600 61.63700  1.000 27.69683  ? 537 LEU B CD1  1 
ATOM   5794 C CD2  . LEU B 1 537 ? 107.95900 101.77000 61.02800  1.000 31.21644  ? 537 LEU B CD2  1 
ATOM   5795 N N    . ALA B 1 538 ? 108.16400 105.64500 62.52600  1.000 23.70843  ? 538 ALA B N    1 
ATOM   5796 C CA   . ALA B 1 538 ? 109.52500 106.16200 62.53400  1.000 26.84457  ? 538 ALA B CA   1 
ATOM   5797 C C    . ALA B 1 538 ? 109.96100 106.57800 63.93000  1.000 24.45785  ? 538 ALA B C    1 
ATOM   5798 O O    . ALA B 1 538 ? 111.14600 106.47900 64.26000  1.000 25.85387  ? 538 ALA B O    1 
ATOM   5799 C CB   . ALA B 1 538 ? 109.64200 107.34000 61.56600  1.000 24.94144  ? 538 ALA B CB   1 
ATOM   5800 N N    . THR B 1 539 ? 109.02500 107.02200 64.77100  1.000 12.34277  ? 539 THR B N    1 
ATOM   5801 C CA   . THR B 1 539 ? 109.38300 107.39600 66.13600  1.000 18.58888  ? 539 THR B CA   1 
ATOM   5802 C C    . THR B 1 539 ? 109.83200 106.18300 66.94200  1.000 21.42126  ? 539 THR B C    1 
ATOM   5803 O O    . THR B 1 539 ? 110.84700 106.23900 67.64800  1.000 24.48110  ? 539 THR B O    1 
ATOM   5804 C CB   . THR B 1 539 ? 108.20000 108.08500 66.81500  1.000 25.71266  ? 539 THR B CB   1 
ATOM   5805 O OG1  . THR B 1 539 ? 107.90500 109.31000 66.13400  1.000 24.74032  ? 539 THR B OG1  1 
ATOM   5806 C CG2  . THR B 1 539 ? 108.51600 108.38500 68.27000  1.000 22.33636  ? 539 THR B CG2  1 
ATOM   5807 N N    . PHE B 1 540 ? 109.09600 105.07500 66.84000  1.000 16.49950  ? 540 PHE B N    1 
ATOM   5808 C CA   . PHE B 1 540 ? 109.49400 103.84400 67.51400  1.000 18.24475  ? 540 PHE B CA   1 
ATOM   5809 C C    . PHE B 1 540 ? 110.86600 103.37500 67.03900  1.000 18.72618  ? 540 PHE B C    1 
ATOM   5810 O O    . PHE B 1 540 ? 111.73000 103.01100 67.85300  1.000 19.01832  ? 540 PHE B O    1 
ATOM   5811 C CB   . PHE B 1 540 ? 108.43100 102.76800 67.27200  1.000 15.03982  ? 540 PHE B CB   1 
ATOM   5812 C CG   . PHE B 1 540 ? 108.49000 101.61500 68.23600  1.000 17.55157  ? 540 PHE B CG   1 
ATOM   5813 C CD1  . PHE B 1 540 ? 109.30900 100.52700 67.99100  1.000 19.37116  ? 540 PHE B CD1  1 
ATOM   5814 C CD2  . PHE B 1 540 ? 107.71700 101.61900 69.38500  1.000 17.30792  ? 540 PHE B CD2  1 
ATOM   5815 C CE1  . PHE B 1 540 ? 109.36100 99.46800  68.87800  1.000 18.68618  ? 540 PHE B CE1  1 
ATOM   5816 C CE2  . PHE B 1 540 ? 107.76500 100.56300 70.27400  1.000 15.79899  ? 540 PHE B CE2  1 
ATOM   5817 C CZ   . PHE B 1 540 ? 108.58800 99.48700  70.02100  1.000 15.29703  ? 540 PHE B CZ   1 
ATOM   5818 N N    . ALA B 1 541 ? 111.09900 103.41400 65.72400  1.000 19.07362  ? 541 ALA B N    1 
ATOM   5819 C CA   . ALA B 1 541 ? 112.39500 102.97200 65.20800  1.000 15.01681  ? 541 ALA B CA   1 
ATOM   5820 C C    . ALA B 1 541 ? 113.53600 103.88000 65.66900  1.000 20.50304  ? 541 ALA B C    1 
ATOM   5821 O O    . ALA B 1 541 ? 114.60200 103.39300 66.07800  1.000 24.01802  ? 541 ALA B O    1 
ATOM   5822 C CB   . ALA B 1 541 ? 112.35000 102.89800 63.68300  1.000 17.92673  ? 541 ALA B CB   1 
ATOM   5823 N N    . SER B 1 542 ? 113.32600 105.19800 65.63700  1.000 12.10871  ? 542 SER B N    1 
ATOM   5824 C CA   . SER B 1 542 ? 114.36700 106.12100 66.07600  1.000 15.99546  ? 542 SER B CA   1 
ATOM   5825 C C    . SER B 1 542 ? 114.65300 105.98100 67.56300  1.000 15.48966  ? 542 SER B C    1 
ATOM   5826 O O    . SER B 1 542 ? 115.80900 106.10400 67.98700  1.000 21.54169  ? 542 SER B O    1 
ATOM   5827 C CB   . SER B 1 542 ? 113.96600 107.55800 65.74600  1.000 18.19940  ? 542 SER B CB   1 
ATOM   5828 O OG   . SER B 1 542 ? 114.16400 107.84200 64.37400  1.000 24.35987  ? 542 SER B OG   1 
ATOM   5829 N N    . LEU B 1 543 ? 113.62900 105.68300 68.36500  1.000 9.71849   ? 543 LEU B N    1 
ATOM   5830 C CA   . LEU B 1 543 ? 113.85500 105.52600 69.79500  1.000 11.36918  ? 543 LEU B CA   1 
ATOM   5831 C C    . LEU B 1 543 ? 114.62400 104.24400 70.08200  1.000 14.40751  ? 543 LEU B C    1 
ATOM   5832 O O    . LEU B 1 543 ? 115.49100 104.21500 70.96500  1.000 15.80814  ? 543 LEU B O    1 
ATOM   5833 C CB   . LEU B 1 543 ? 112.51900 105.53600 70.53600  1.000 17.99154  ? 543 LEU B CB   1 
ATOM   5834 C CG   . LEU B 1 543 ? 111.80500 106.88700 70.60400  1.000 18.22727  ? 543 LEU B CG   1 
ATOM   5835 C CD1  . LEU B 1 543 ? 110.49400 106.76800 71.35900  1.000 13.56013  ? 543 LEU B CD1  1 
ATOM   5836 C CD2  . LEU B 1 543 ? 112.69900 107.94400 71.23400  1.000 17.83087  ? 543 LEU B CD2  1 
ATOM   5837 N N    . LEU B 1 544 ? 114.35100 103.18300 69.31900  1.000 22.74568  ? 544 LEU B N    1 
ATOM   5838 C CA   . LEU B 1 544 ? 115.13100 101.96000 69.48200  1.000 16.56713  ? 544 LEU B CA   1 
ATOM   5839 C C    . LEU B 1 544 ? 116.59400 102.17900 69.10400  1.000 17.96379  ? 544 LEU B C    1 
ATOM   5840 O O    . LEU B 1 544 ? 117.50700 101.68800 69.78800  1.000 21.53551  ? 544 LEU B O    1 
ATOM   5841 C CB   . LEU B 1 544 ? 114.51900 100.84000 68.64000  1.000 15.35897  ? 544 LEU B CB   1 
ATOM   5842 C CG   . LEU B 1 544 ? 114.47100 99.44700  69.26700  1.000 18.86325  ? 544 LEU B CG   1 
ATOM   5843 C CD1  . LEU B 1 544 ? 113.86500 99.50600  70.65800  1.000 17.06384  ? 544 LEU B CD1  1 
ATOM   5844 C CD2  . LEU B 1 544 ? 113.68800 98.49700  68.37900  1.000 16.55385  ? 544 LEU B CD2  1 
ATOM   5845 N N    . ILE B 1 545 ? 116.84400 102.95600 68.04700  1.000 13.81919  ? 545 ILE B N    1 
ATOM   5846 C CA   . ILE B 1 545 ? 118.23100 103.21000 67.66200  1.000 9.29875   ? 545 ILE B CA   1 
ATOM   5847 C C    . ILE B 1 545 ? 118.94000 104.08300 68.69700  1.000 15.11212  ? 545 ILE B C    1 
ATOM   5848 O O    . ILE B 1 545 ? 120.12700 103.88200 68.98600  1.000 16.26569  ? 545 ILE B O    1 
ATOM   5849 C CB   . ILE B 1 545 ? 118.29200 103.82800 66.25300  1.000 16.25359  ? 545 ILE B CB   1 
ATOM   5850 C CG1  . ILE B 1 545 ? 118.14000 102.73600 65.19200  1.000 12.28874  ? 545 ILE B CG1  1 
ATOM   5851 C CG2  . ILE B 1 545 ? 119.59900 104.57800 66.05200  1.000 14.32779  ? 545 ILE B CG2  1 
ATOM   5852 C CD1  . ILE B 1 545 ? 117.52000 103.21500 63.90300  1.000 20.88300  ? 545 ILE B CD1  1 
ATOM   5853 N N    . GLU B 1 546 ? 118.22900 105.04200 69.29600  1.000 15.63970  ? 546 GLU B N    1 
ATOM   5854 C CA   . GLU B 1 546 ? 118.84400 105.83300 70.36300  1.000 13.47639  ? 546 GLU B CA   1 
ATOM   5855 C C    . GLU B 1 546 ? 119.15500 104.96900 71.58500  1.000 10.55611  ? 546 GLU B C    1 
ATOM   5856 O O    . GLU B 1 546 ? 120.20800 105.12900 72.22700  1.000 16.75137  ? 546 GLU B O    1 
ATOM   5857 C CB   . GLU B 1 546 ? 117.92400 106.99500 70.73900  1.000 17.90756  ? 546 GLU B CB   1 
ATOM   5858 C CG   . GLU B 1 546 ? 118.43600 107.87900 71.86700  1.000 21.53054  ? 546 GLU B CG   1 
ATOM   5859 C CD   . GLU B 1 546 ? 119.69200 108.64000 71.49200  1.000 23.59784  ? 546 GLU B CD   1 
ATOM   5860 O OE1  . GLU B 1 546 ? 119.83900 109.00000 70.30600  1.000 17.74057  ? 546 GLU B OE1  1 
ATOM   5861 O OE2  . GLU B 1 546 ? 120.52900 108.88600 72.38400  1.000 25.75352  ? 546 GLU B OE2  1 
ATOM   5862 N N    . PHE B 1 547 ? 118.27100 104.01600 71.89400  1.000 9.89442   ? 547 PHE B N    1 
ATOM   5863 C CA   . PHE B 1 547 ? 118.54100 103.11800 73.00900  1.000 10.12891  ? 547 PHE B CA   1 
ATOM   5864 C C    . PHE B 1 547 ? 119.78400 102.28600 72.74100  1.000 13.83003  ? 547 PHE B C    1 
ATOM   5865 O O    . PHE B 1 547 ? 120.57400 102.02200 73.65400  1.000 10.39992  ? 547 PHE B O    1 
ATOM   5866 C CB   . PHE B 1 547 ? 117.34300 102.20400 73.26200  1.000 12.92736  ? 547 PHE B CB   1 
ATOM   5867 C CG   . PHE B 1 547 ? 117.65400 101.04300 74.16300  1.000 10.39890  ? 547 PHE B CG   1 
ATOM   5868 C CD1  . PHE B 1 547 ? 117.60700 101.18400 75.53700  1.000 11.50103  ? 547 PHE B CD1  1 
ATOM   5869 C CD2  . PHE B 1 547 ? 118.01800 99.81600  73.63300  1.000 10.95396  ? 547 PHE B CD2  1 
ATOM   5870 C CE1  . PHE B 1 547 ? 117.90000 100.12000 76.36500  1.000 7.85705   ? 547 PHE B CE1  1 
ATOM   5871 C CE2  . PHE B 1 547 ? 118.31600 98.75200  74.45600  1.000 14.21148  ? 547 PHE B CE2  1 
ATOM   5872 C CZ   . PHE B 1 547 ? 118.25700 98.90400  75.82400  1.000 15.17988  ? 547 PHE B CZ   1 
ATOM   5873 N N    . VAL B 1 548 ? 119.98500 101.87700 71.48800  1.000 18.94269  ? 548 VAL B N    1 
ATOM   5874 C CA   . VAL B 1 548 ? 121.17000 101.07200 71.21200  1.000 9.74284   ? 548 VAL B CA   1 
ATOM   5875 C C    . VAL B 1 548 ? 122.42200 101.94200 71.20000  1.000 12.23459  ? 548 VAL B C    1 
ATOM   5876 O O    . VAL B 1 548 ? 123.52300 101.45500 71.47700  1.000 17.57699  ? 548 VAL B O    1 
ATOM   5877 C CB   . VAL B 1 548 ? 121.01500 100.30400 69.89000  1.000 13.14216  ? 548 VAL B CB   1 
ATOM   5878 C CG1  . VAL B 1 548 ? 122.26400 99.48700  69.61000  1.000 12.17490  ? 548 VAL B CG1  1 
ATOM   5879 C CG2  . VAL B 1 548 ? 119.79400 99.40600  69.94100  1.000 14.64650  ? 548 VAL B CG2  1 
ATOM   5880 N N    . ALA B 1 549 ? 122.28100 103.23100 70.88500  1.000 21.34391  ? 549 ALA B N    1 
ATOM   5881 C CA   . ALA B 1 549 ? 123.42000 104.14200 70.91000  1.000 11.72067  ? 549 ALA B CA   1 
ATOM   5882 C C    . ALA B 1 549 ? 123.82000 104.58400 72.31400  1.000 15.30676  ? 549 ALA B C    1 
ATOM   5883 O O    . ALA B 1 549 ? 124.92100 105.11900 72.48400  1.000 18.13656  ? 549 ALA B O    1 
ATOM   5884 C CB   . ALA B 1 549 ? 123.12500 105.37600 70.05600  1.000 10.82155  ? 549 ALA B CB   1 
ATOM   5885 N N    . ARG B 1 550 ? 122.96800 104.38200 73.31900  1.000 18.92991  ? 550 ARG B N    1 
ATOM   5886 C CA   . ARG B 1 550 ? 123.29300 104.82200 74.67900  1.000 9.43915   ? 550 ARG B CA   1 
ATOM   5887 C C    . ARG B 1 550 ? 123.97400 103.77000 75.57200  1.000 16.02819  ? 550 ARG B C    1 
ATOM   5888 O O    . ARG B 1 550 ? 124.12200 104.01800 76.77200  1.000 14.96419  ? 550 ARG B O    1 
ATOM   5889 C CB   . ARG B 1 550 ? 122.03300 105.32600 75.39000  1.000 15.31405  ? 550 ARG B CB   1 
ATOM   5890 C CG   . ARG B 1 550 ? 121.51000 106.65800 74.89100  1.000 16.53461  ? 550 ARG B CG   1 
ATOM   5891 C CD   . ARG B 1 550 ? 120.33900 107.13000 75.73800  1.000 14.88255  ? 550 ARG B CD   1 
ATOM   5892 N NE   . ARG B 1 550 ? 119.75800 108.36800 75.23300  1.000 17.24944  ? 550 ARG B NE   1 
ATOM   5893 C CZ   . ARG B 1 550 ? 118.85800 109.09500 75.88300  1.000 15.18574  ? 550 ARG B CZ   1 
ATOM   5894 N NH1  . ARG B 1 550 ? 118.40400 108.73200 77.07000  1.000 14.49654  ? 550 ARG B NH1  1 
ATOM   5895 N NH2  . ARG B 1 550 ? 118.40400 110.21400 75.32600  1.000 12.88237  ? 550 ARG B NH2  1 
ATOM   5896 N N    . LEU B 1 551 ? 124.39500 102.61700 75.04200  1.000 17.03889  ? 551 LEU B N    1 
ATOM   5897 C CA   . LEU B 1 551 ? 124.96000 101.56000 75.88700  1.000 11.94261  ? 551 LEU B CA   1 
ATOM   5898 C C    . LEU B 1 551 ? 126.47800 101.63100 76.08000  1.000 15.42108  ? 551 LEU B C    1 
ATOM   5899 O O    . LEU B 1 551 ? 127.00900 100.99600 77.01200  1.000 24.00645  ? 551 LEU B O    1 
ATOM   5900 C CB   . LEU B 1 551 ? 124.59600 100.19200 75.30100  1.000 13.66626  ? 551 LEU B CB   1 
ATOM   5901 C CG   . LEU B 1 551 ? 123.12100 99.78900  75.38900  1.000 17.14064  ? 551 LEU B CG   1 
ATOM   5902 C CD1  . LEU B 1 551 ? 122.84400 98.55900  74.53500  1.000 6.88406   ? 551 LEU B CD1  1 
ATOM   5903 C CD2  . LEU B 1 551 ? 122.70800 99.54500  76.83000  1.000 5.92454   ? 551 LEU B CD2  1 
ATOM   5904 N N    . GLN B 1 552 ? 127.18900 102.39600 75.24900  1.000 19.12507  ? 552 GLN B N    1 
ATOM   5905 C CA   . GLN B 1 552 ? 128.63900 102.48700 75.39000  1.000 19.26404  ? 552 GLN B CA   1 
ATOM   5906 C C    . GLN B 1 552 ? 129.04800 103.15800 76.69700  1.000 20.87400  ? 552 GLN B C    1 
ATOM   5907 O O    . GLN B 1 552 ? 130.05500 102.77100 77.30300  1.000 20.17744  ? 552 GLN B O    1 
ATOM   5908 C CB   . GLN B 1 552 ? 129.22400 103.24100 74.19500  1.000 18.24425  ? 552 GLN B CB   1 
ATOM   5909 C CG   . GLN B 1 552 ? 130.72900 103.43300 74.23800  1.000 20.06276  ? 552 GLN B CG   1 
ATOM   5910 C CD   . GLN B 1 552 ? 131.48500 102.13800 74.02100  1.000 27.47562  ? 552 GLN B CD   1 
ATOM   5911 O OE1  . GLN B 1 552 ? 131.46200 101.57000 72.93000  1.000 24.95683  ? 552 GLN B OE1  1 
ATOM   5912 N NE2  . GLN B 1 552 ? 132.16100 101.66400 75.06100  1.000 23.46774  ? 552 GLN B NE2  1 
ATOM   5913 N N    . ASN B 1 553 ? 128.27100 104.13800 77.16500  1.000 16.59788  ? 553 ASN B N    1 
ATOM   5914 C CA   . ASN B 1 553 ? 128.59300 104.77900 78.43500  1.000 15.65055  ? 553 ASN B CA   1 
ATOM   5915 C C    . ASN B 1 553 ? 128.39700 103.83100 79.61000  1.000 19.75460  ? 553 ASN B C    1 
ATOM   5916 O O    . ASN B 1 553 ? 129.14300 103.90100 80.59600  1.000 29.67976  ? 553 ASN B O    1 
ATOM   5917 C CB   . ASN B 1 553 ? 127.73900 106.03400 78.61400  1.000 22.80369  ? 553 ASN B CB   1 
ATOM   5918 C CG   . ASN B 1 553 ? 128.36700 107.03900 79.55500  1.000 31.08753  ? 553 ASN B CG   1 
ATOM   5919 O OD1  . ASN B 1 553 ? 127.85000 107.29700 80.64100  1.000 29.54548  ? 553 ASN B OD1  1 
ATOM   5920 N ND2  . ASN B 1 553 ? 129.48900 107.61600 79.14000  1.000 33.49906  ? 553 ASN B ND2  1 
ATOM   5921 N N    . VAL B 1 554 ? 127.45000 102.89800 79.50300  1.000 12.04260  ? 554 VAL B N    1 
ATOM   5922 C CA   . VAL B 1 554 ? 127.25700 101.93400 80.57900  1.000 19.28919  ? 554 VAL B CA   1 
ATOM   5923 C C    . VAL B 1 554 ? 128.39600 100.92700 80.58600  1.000 17.35694  ? 554 VAL B C    1 
ATOM   5924 O O    . VAL B 1 554 ? 128.88400 100.52300 81.65100  1.000 18.33602  ? 554 VAL B O    1 
ATOM   5925 C CB   . VAL B 1 554 ? 125.88800 101.24000 80.44200  1.000 21.01253  ? 554 VAL B CB   1 
ATOM   5926 C CG1  . VAL B 1 554 ? 125.73500 100.15000 81.49200  1.000 18.86760  ? 554 VAL B CG1  1 
ATOM   5927 C CG2  . VAL B 1 554 ? 124.75900 102.25000 80.54400  1.000 16.55803  ? 554 VAL B CG2  1 
ATOM   5928 N N    . VAL B 1 555 ? 128.87700 100.54400 79.40100  1.000 21.71263  ? 555 VAL B N    1 
ATOM   5929 C CA   . VAL B 1 555 ? 130.02500 99.63800  79.38600  1.000 19.41334  ? 555 VAL B CA   1 
ATOM   5930 C C    . VAL B 1 555 ? 131.27600 100.34000 79.91400  1.000 19.06845  ? 555 VAL B C    1 
ATOM   5931 O O    . VAL B 1 555 ? 132.10200 99.72300  80.60900  1.000 25.72311  ? 555 VAL B O    1 
ATOM   5932 C CB   . VAL B 1 555 ? 130.24500 99.07700  77.97000  1.000 20.97926  ? 555 VAL B CB   1 
ATOM   5933 C CG1  . VAL B 1 555 ? 131.61300 98.42500  77.86300  1.000 19.77443  ? 555 VAL B CG1  1 
ATOM   5934 C CG2  . VAL B 1 555 ? 129.14900 98.08400  77.62200  1.000 14.03548  ? 555 VAL B CG2  1 
ATOM   5935 N N    . ASP B 1 556 ? 131.40600 101.64600 79.66600  1.000 19.89661  ? 556 ASP B N    1 
ATOM   5936 C CA   . ASP B 1 556 ? 132.54500 102.38700 80.20300  1.000 17.03684  ? 556 ASP B CA   1 
ATOM   5937 C C    . ASP B 1 556 ? 132.47900 102.48800 81.72300  1.000 23.83315  ? 556 ASP B C    1 
ATOM   5938 O O    . ASP B 1 556 ? 133.49400 102.30500 82.41300  1.000 25.89339  ? 556 ASP B O    1 
ATOM   5939 C CB   . ASP B 1 556 ? 132.60500 103.78100 79.57800  1.000 17.96325  ? 556 ASP B CB   1 
ATOM   5940 C CG   . ASP B 1 556 ? 133.14800 103.76400 78.16400  1.000 30.64021  ? 556 ASP B CG   1 
ATOM   5941 O OD1  . ASP B 1 556 ? 133.73600 102.73900 77.76000  1.000 30.31477  ? 556 ASP B OD1  1 
ATOM   5942 O OD2  . ASP B 1 556 ? 132.98700 104.77800 77.45400  1.000 32.99736  ? 556 ASP B OD2  1 
ATOM   5943 N N    . ALA B 1 557 ? 131.29200 102.76800 82.26800  1.000 22.17780  ? 557 ALA B N    1 
ATOM   5944 C CA   . ALA B 1 557 ? 131.17300 102.83600 83.72000  1.000 20.96387  ? 557 ALA B CA   1 
ATOM   5945 C C    . ALA B 1 557 ? 131.41600 101.47600 84.36100  1.000 25.41550  ? 557 ALA B C    1 
ATOM   5946 O O    . ALA B 1 557 ? 131.99800 101.39900 85.45300  1.000 25.38303  ? 557 ALA B O    1 
ATOM   5947 C CB   . ALA B 1 557 ? 129.79800 103.37400 84.11300  1.000 15.06581  ? 557 ALA B CB   1 
ATOM   5948 N N    . PHE B 1 558 ? 131.02800 100.38900 83.68700  1.000 26.80664  ? 558 PHE B N    1 
ATOM   5949 C CA   . PHE B 1 558 ? 131.31900 99.08000  84.25600  1.000 22.31371  ? 558 PHE B CA   1 
ATOM   5950 C C    . PHE B 1 558 ? 132.81600 98.81200  84.25700  1.000 22.63454  ? 558 PHE B C    1 
ATOM   5951 O O    . PHE B 1 558 ? 133.34100 98.21600  85.20200  1.000 26.33527  ? 558 PHE B O    1 
ATOM   5952 C CB   . PHE B 1 558 ? 130.59200 97.96600  83.50600  1.000 24.34952  ? 558 PHE B CB   1 
ATOM   5953 C CG   . PHE B 1 558 ? 130.99600 96.58900  83.95800  1.000 29.43902  ? 558 PHE B CG   1 
ATOM   5954 C CD1  . PHE B 1 558 ? 130.34600 95.97600  85.01500  1.000 26.36028  ? 558 PHE B CD1  1 
ATOM   5955 C CD2  . PHE B 1 558 ? 132.04300 95.92000  83.34600  1.000 27.26319  ? 558 PHE B CD2  1 
ATOM   5956 C CE1  . PHE B 1 558 ? 130.72300 94.71900  85.44400  1.000 22.04072  ? 558 PHE B CE1  1 
ATOM   5957 C CE2  . PHE B 1 558 ? 132.42400 94.66300  83.77200  1.000 25.31818  ? 558 PHE B CE2  1 
ATOM   5958 C CZ   . PHE B 1 558 ? 131.76300 94.06300  84.82200  1.000 23.14575  ? 558 PHE B CZ   1 
ATOM   5959 N N    . LYS B 1 559 ? 133.52200 99.22000  83.19900  1.000 31.06024  ? 559 LYS B N    1 
ATOM   5960 C CA   . LYS B 1 559 ? 134.96900 99.02600  83.19800  1.000 25.82165  ? 559 LYS B CA   1 
ATOM   5961 C C    . LYS B 1 559 ? 135.62400 99.82100  84.32100  1.000 27.90377  ? 559 LYS B C    1 
ATOM   5962 O O    . LYS B 1 559 ? 136.53500 99.32700  85.00200  1.000 32.70182  ? 559 LYS B O    1 
ATOM   5963 C CB   . LYS B 1 559 ? 135.56200 99.42400  81.84800  1.000 25.24588  ? 559 LYS B CB   1 
ATOM   5964 C CG   . LYS B 1 559 ? 135.33300 98.41500  80.74100  1.000 29.19996  ? 559 LYS B CG   1 
ATOM   5965 C CD   . LYS B 1 559 ? 136.28300 98.65900  79.58300  1.000 29.80950  ? 559 LYS B CD   1 
ATOM   5966 C CE   . LYS B 1 559 ? 135.58800 98.46900  78.24700  1.000 30.78845  ? 559 LYS B CE   1 
ATOM   5967 N NZ   . LYS B 1 559 ? 135.55000 97.03500  77.85000  1.000 34.98747  ? 559 LYS B NZ   1 
ATOM   5968 N N    . GLU B 1 560 ? 135.13500 101.03800 84.56800  1.000 32.91791  ? 560 GLU B N    1 
ATOM   5969 C CA   . GLU B 1 560 ? 135.70100 101.84000 85.64900  1.000 26.79035  ? 560 GLU B CA   1 
ATOM   5970 C C    . GLU B 1 560 ? 135.45700 101.19600 87.01000  1.000 31.08969  ? 560 GLU B C    1 
ATOM   5971 O O    . GLU B 1 560 ? 136.35100 101.18500 87.86900  1.000 30.83013  ? 560 GLU B O    1 
ATOM   5972 C CB   . GLU B 1 560 ? 135.12500 103.25400 85.61000  1.000 26.39619  ? 560 GLU B CB   1 
ATOM   5973 C CG   . GLU B 1 560 ? 136.11600 104.33300 86.00300  1.000 32.12257  ? 560 GLU B CG   1 
ATOM   5974 C CD   . GLU B 1 560 ? 135.47300 105.46300 86.77900  1.000 40.26644  ? 560 GLU B CD   1 
ATOM   5975 O OE1  . GLU B 1 560 ? 134.33300 105.84500 86.43900  1.000 33.83940  ? 560 GLU B OE1  1 
ATOM   5976 O OE2  . GLU B 1 560 ? 136.10700 105.96700 87.73000  1.000 35.58105  ? 560 GLU B OE2  1 
ATOM   5977 N N    . LEU B 1 561 ? 134.26800 100.62100 87.21700  1.000 25.58417  ? 561 LEU B N    1 
ATOM   5978 C CA   . LEU B 1 561 ? 134.00700 99.96300  88.49500  1.000 19.36801  ? 561 LEU B CA   1 
ATOM   5979 C C    . LEU B 1 561 ? 134.81700 98.68000  88.63800  1.000 23.01389  ? 561 LEU B C    1 
ATOM   5980 O O    . LEU B 1 561 ? 135.32000 98.37800  89.72600  1.000 19.87783  ? 561 LEU B O    1 
ATOM   5981 C CB   . LEU B 1 561 ? 132.51600 99.66500  88.64600  1.000 25.02703  ? 561 LEU B CB   1 
ATOM   5982 C CG   . LEU B 1 561 ? 132.13300 98.79500  89.84700  1.000 17.97252  ? 561 LEU B CG   1 
ATOM   5983 C CD1  . LEU B 1 561 ? 132.33500 99.54400  91.15100  1.000 20.94176  ? 561 LEU B CD1  1 
ATOM   5984 C CD2  . LEU B 1 561 ? 130.70100 98.29700  89.72900  1.000 19.31955  ? 561 LEU B CD2  1 
ATOM   5985 N N    . SER B 1 562 ? 134.96500 97.91500  87.55400  1.000 31.95053  ? 562 SER B N    1 
ATOM   5986 C CA   . SER B 1 562 ? 135.75400 96.69200  87.62600  1.000 29.18725  ? 562 SER B CA   1 
ATOM   5987 C C    . SER B 1 562 ? 137.23500 96.98700  87.79400  1.000 27.20155  ? 562 SER B C    1 
ATOM   5988 O O    . SER B 1 562 ? 137.99500 96.09000  88.17300  1.000 31.97859  ? 562 SER B O    1 
ATOM   5989 C CB   . SER B 1 562 ? 135.53300 95.83600  86.38000  1.000 26.76247  ? 562 SER B CB   1 
ATOM   5990 O OG   . SER B 1 562 ? 136.51000 96.11800  85.39500  1.000 29.48488  ? 562 SER B OG   1 
ATOM   5991 N N    . GLN B 1 563 ? 137.65700 98.22200  87.52700  1.000 37.34129  ? 563 GLN B N    1 
ATOM   5992 C CA   . GLN B 1 563 ? 139.05700 98.57500  87.71400  1.000 34.01795  ? 563 GLN B CA   1 
ATOM   5993 C C    . GLN B 1 563 ? 139.32900 99.13800  89.10300  1.000 38.65063  ? 563 GLN B C    1 
ATOM   5994 O O    . GLN B 1 563 ? 140.34500 98.79400  89.71700  1.000 37.51636  ? 563 GLN B O    1 
ATOM   5995 C CB   . GLN B 1 563 ? 139.49700 99.58400  86.65000  1.000 34.70141  ? 563 GLN B CB   1 
ATOM   5996 C CG   . GLN B 1 563 ? 140.98900 99.57300  86.37700  1.000 38.23707  ? 563 GLN B CG   1 
ATOM   5997 C CD   . GLN B 1 563 ? 141.44400 98.29900  85.69800  1.000 43.67890  ? 563 GLN B CD   1 
ATOM   5998 O OE1  . GLN B 1 563 ? 140.65100 97.59800  85.07000  1.000 39.61842  ? 563 GLN B OE1  1 
ATOM   5999 N NE2  . GLN B 1 563 ? 142.73000 97.98900  85.82200  1.000 41.93615  ? 563 GLN B NE2  1 
ATOM   6000 N N    . LYS B 1 564 ? 138.44800 99.99900  89.61700  1.000 39.83240  ? 564 LYS B N    1 
ATOM   6001 C CA   . LYS B 1 564 ? 138.68700 100.57500 90.93700  1.000 33.41713  ? 564 LYS B CA   1 
ATOM   6002 C C    . LYS B 1 564 ? 138.41900 99.60600  92.08400  1.000 37.21157  ? 564 LYS B C    1 
ATOM   6003 O O    . LYS B 1 564 ? 138.99300 99.78300  93.16400  1.000 39.59822  ? 564 LYS B O    1 
ATOM   6004 C CB   . LYS B 1 564 ? 137.84600 101.83900 91.13000  1.000 33.04169  ? 564 LYS B CB   1 
ATOM   6005 C CG   . LYS B 1 564 ? 138.51700 103.09400 90.60700  1.000 33.27755  ? 564 LYS B CG   1 
ATOM   6006 C CD   . LYS B 1 564 ? 137.95200 104.34300 91.25600  1.000 36.50944  ? 564 LYS B CD   1 
ATOM   6007 C CE   . LYS B 1 564 ? 138.53200 105.59400 90.61900  1.000 37.12881  ? 564 LYS B CE   1 
ATOM   6008 N NZ   . LYS B 1 564 ? 138.79900 105.41100 89.16600  1.000 36.86529  ? 564 LYS B NZ   1 
ATOM   6009 N N    . ALA B 1 565 ? 137.57900 98.59000  91.88700  1.000 39.78645  ? 565 ALA B N    1 
ATOM   6010 C CA   . ALA B 1 565 ? 137.21900 97.66000  92.95000  1.000 33.13707  ? 565 ALA B CA   1 
ATOM   6011 C C    . ALA B 1 565 ? 138.05500 96.38600  92.93700  1.000 34.91686  ? 565 ALA B C    1 
ATOM   6012 O O    . ALA B 1 565 ? 137.78400 95.47200  93.72300  1.000 35.35697  ? 565 ALA B O    1 
ATOM   6013 C CB   . ALA B 1 565 ? 135.73200 97.30900  92.86500  1.000 30.27980  ? 565 ALA B CB   1 
ATOM   6014 N N    . ASN B 1 566 ? 139.05800 96.30400  92.06400  1.000 40.00449  ? 566 ASN B N    1 
ATOM   6015 C CA   . ASN B 1 566 ? 139.96900 95.16000  92.00100  1.000 37.13002  ? 566 ASN B CA   1 
ATOM   6016 C C    . ASN B 1 566 ? 139.22100 93.84500  91.77100  1.000 38.72412  ? 566 ASN B C    1 
ATOM   6017 O O    . ASN B 1 566 ? 139.40500 92.86300  92.49300  1.000 37.46499  ? 566 ASN B O    1 
ATOM   6018 C CB   . ASN B 1 566 ? 140.83100 95.08700  93.26400  1.000 35.62457  ? 566 ASN B CB   1 
ATOM   6019 C CG   . ASN B 1 566 ? 142.10300 94.28900  93.05500  1.000 43.77459  ? 566 ASN B CG   1 
ATOM   6020 O OD1  . ASN B 1 566 ? 142.27300 93.20900  93.61900  1.000 42.17787  ? 566 ASN B OD1  1 
ATOM   6021 N ND2  . ASN B 1 566 ? 143.01300 94.82700  92.25200  1.000 42.41444  ? 566 ASN B ND2  1 
ATOM   6022 N N    . PHE B 1 567 ? 138.37100 93.83100  90.74900  1.000 33.96599  ? 567 PHE B N    1 
ATOM   6023 C CA   . PHE B 1 567 ? 137.68700 92.60400  90.37000  1.000 30.72778  ? 567 PHE B CA   1 
ATOM   6024 C C    . PHE B 1 567 ? 138.68900 91.57300  89.85500  1.000 37.87065  ? 567 PHE B C    1 
ATOM   6025 O O    . PHE B 1 567 ? 139.80700 91.90100  89.44700  1.000 39.87722  ? 567 PHE B O    1 
ATOM   6026 C CB   . PHE B 1 567 ? 136.62000 92.88900  89.31500  1.000 31.68982  ? 567 PHE B CB   1 
ATOM   6027 C CG   . PHE B 1 567 ? 135.34300 93.44900  89.87700  1.000 33.63600  ? 567 PHE B CG   1 
ATOM   6028 C CD1  . PHE B 1 567 ? 135.27300 93.86700  91.19600  1.000 36.91430  ? 567 PHE B CD1  1 
ATOM   6029 C CD2  . PHE B 1 567 ? 134.21100 93.55100  89.08900  1.000 32.80204  ? 567 PHE B CD2  1 
ATOM   6030 C CE1  . PHE B 1 567 ? 134.09900 94.38000  91.71300  1.000 34.94747  ? 567 PHE B CE1  1 
ATOM   6031 C CE2  . PHE B 1 567 ? 133.03500 94.06200  89.59900  1.000 31.17677  ? 567 PHE B CE2  1 
ATOM   6032 C CZ   . PHE B 1 567 ? 132.97800 94.47700  90.91400  1.000 29.88707  ? 567 PHE B CZ   1 
ATOM   6033 N N    . LYS B 1 568 ? 138.27600 90.31000  89.87800  1.000 45.47815  ? 568 LYS B N    1 
ATOM   6034 C CA   . LYS B 1 568 ? 139.14900 89.21000  89.49700  1.000 44.15849  ? 568 LYS B CA   1 
ATOM   6035 C C    . LYS B 1 568 ? 139.09000 88.94600  87.99700  1.000 45.96164  ? 568 LYS B C    1 
ATOM   6036 O O    . LYS B 1 568 ? 138.09000 89.22600  87.33200  1.000 48.89812  ? 568 LYS B O    1 
ATOM   6037 C CB   . LYS B 1 568 ? 138.77500 87.93800  90.25600  1.000 46.03193  ? 568 LYS B CB   1 
ATOM   6038 C CG   . LYS B 1 568 ? 137.69000 87.12000  89.58500  1.000 45.70071  ? 568 LYS B CG   1 
ATOM   6039 C CD   . LYS B 1 568 ? 137.51700 85.77700  90.26700  1.000 46.84345  ? 568 LYS B CD   1 
ATOM   6040 C CE   . LYS B 1 568 ? 136.05700 85.36100  90.30000  1.000 49.11691  ? 568 LYS B CE   1 
ATOM   6041 N NZ   . LYS B 1 568 ? 135.73700 84.56800  91.51800  1.000 49.35086  ? 568 LYS B NZ   1 
ATOM   6042 N N    . GLU B 1 569 ? 140.17900 88.38900  87.47400  1.000 54.37437  ? 569 GLU B N    1 
ATOM   6043 C CA   . GLU B 1 569 ? 140.25200 88.06600  86.05600  1.000 54.91466  ? 569 GLU B CA   1 
ATOM   6044 C C    . GLU B 1 569 ? 139.25600 86.96100  85.70800  1.000 56.28089  ? 569 GLU B C    1 
ATOM   6045 O O    . GLU B 1 569 ? 139.11800 85.98900  86.45700  1.000 54.61821  ? 569 GLU B O    1 
ATOM   6046 C CB   . GLU B 1 569 ? 141.66600 87.63000  85.67600  1.000 55.43953  ? 569 GLU B CB   1 
ATOM   6047 C CG   . GLU B 1 569 ? 142.66300 88.77100  85.57600  1.000 57.32390  ? 569 GLU B CG   1 
ATOM   6048 C CD   . GLU B 1 569 ? 142.36200 89.70600  84.42100  1.000 59.16015  ? 569 GLU B CD   1 
ATOM   6049 O OE1  . GLU B 1 569 ? 141.86000 89.22700  83.38200  1.000 57.97168  ? 569 GLU B OE1  1 
ATOM   6050 O OE2  . GLU B 1 569 ? 142.62600 90.91900  84.55100  1.000 60.04798  ? 569 GLU B OE2  1 
ATOM   6051 N N    . PRO B 1 570 ? 138.54800 87.08300  84.58600  1.000 59.98371  ? 570 PRO B N    1 
ATOM   6052 C CA   . PRO B 1 570 ? 137.53900 86.07800  84.23500  1.000 56.16898  ? 570 PRO B CA   1 
ATOM   6053 C C    . PRO B 1 570 ? 138.13300 84.67700  84.20900  1.000 58.48376  ? 570 PRO B C    1 
ATOM   6054 O O    . PRO B 1 570 ? 139.25700 84.46800  83.74700  1.000 57.73613  ? 570 PRO B O    1 
ATOM   6055 C CB   . PRO B 1 570 ? 137.07000 86.51500  82.84300  1.000 53.84629  ? 570 PRO B CB   1 
ATOM   6056 C CG   . PRO B 1 570 ? 137.41400 87.95700  82.75300  1.000 55.49927  ? 570 PRO B CG   1 
ATOM   6057 C CD   . PRO B 1 570 ? 138.64500 88.15500  83.58200  1.000 57.09535  ? 570 PRO B CD   1 
ATOM   6058 N N    . GLU B 1 571 ? 137.36700 83.71900  84.72900  1.000 64.05868  ? 571 GLU B N    1 
ATOM   6059 C CA   . GLU B 1 571 ? 137.78900 82.32200  84.84300  1.000 62.70990  ? 571 GLU B CA   1 
ATOM   6060 C C    . GLU B 1 571 ? 138.68300 81.87000  83.69100  1.000 60.53290  ? 571 GLU B C    1 
ATOM   6061 O O    . GLU B 1 571 ? 138.19800 81.38300  82.67000  1.000 60.50080  ? 571 GLU B O    1 
ATOM   6062 C CB   . GLU B 1 571 ? 136.56400 81.41000  84.93000  1.000 60.98168  ? 571 GLU B CB   1 
HETATM 6063 P P1   . LPP C 2 .   ? 107.47400 108.98000 118.90500 1.000 55.49029  ? 601 LPP A P1   1 
HETATM 6064 O O2   . LPP C 2 .   ? 108.41000 107.94300 118.33400 1.000 42.56485  ? 601 LPP A O2   1 
HETATM 6065 O O3   . LPP C 2 .   ? 107.96700 110.35700 118.53500 1.000 42.55368  ? 601 LPP A O3   1 
HETATM 6066 O O4   . LPP C 2 .   ? 106.08600 108.77500 118.34100 1.000 39.71448  ? 601 LPP A O4   1 
HETATM 6067 O O5   . LPP C 2 .   ? 107.42800 108.83300 120.56100 1.000 40.21926  ? 601 LPP A O5   1 
HETATM 6068 C C6   . LPP C 2 .   ? 106.20000 108.53400 121.17400 1.000 36.52349  ? 601 LPP A C6   1 
HETATM 6069 C C7   . LPP C 2 .   ? 106.38000 108.52200 122.68600 1.000 38.44242  ? 601 LPP A C7   1 
HETATM 6070 C C8   . LPP C 2 .   ? 105.98100 109.90800 123.26100 1.000 43.14342  ? 601 LPP A C8   1 
HETATM 6071 O O9   . LPP C 2 .   ? 105.58700 107.50800 123.23200 1.000 40.36988  ? 601 LPP A O9   1 
HETATM 6072 O O27  . LPP C 2 .   ? 104.56700 110.00900 123.42300 1.000 40.42589  ? 601 LPP A O27  1 
HETATM 6073 C C11  . LPP C 2 .   ? 105.32700 107.63700 124.61600 1.000 41.86827  ? 601 LPP A C11  1 
HETATM 6074 O O10  . LPP C 2 .   ? 106.22700 107.72600 125.39200 1.000 41.00926  ? 601 LPP A O10  1 
HETATM 6075 C C12  . LPP C 2 .   ? 103.85500 107.67500 125.10800 1.000 39.25288  ? 601 LPP A C12  1 
HETATM 6076 C C13  . LPP C 2 .   ? 103.54200 106.41000 125.96200 1.000 39.21192  ? 601 LPP A C13  1 
HETATM 6077 C C14  . LPP C 2 .   ? 102.69400 106.83200 127.19600 1.000 40.54125  ? 601 LPP A C14  1 
HETATM 6078 C C15  . LPP C 2 .   ? 103.61400 107.50500 128.26600 1.000 37.86678  ? 601 LPP A C15  1 
HETATM 6079 C C16  . LPP C 2 .   ? 104.09400 106.44200 129.31500 1.000 37.45289  ? 601 LPP A C16  1 
HETATM 6080 C C17  . LPP C 2 .   ? 103.15300 106.43800 130.55600 1.000 41.29047  ? 601 LPP A C17  1 
HETATM 6081 C C18  . LPP C 2 .   ? 101.92100 105.50800 130.31900 1.000 40.56621  ? 601 LPP A C18  1 
HETATM 6082 C C19  . LPP C 2 .   ? 100.66500 106.36100 130.00000 1.000 37.63857  ? 601 LPP A C19  1 
HETATM 6083 C C20  . LPP C 2 .   ? 99.88900  106.69400 131.30800 1.000 38.58282  ? 601 LPP A C20  1 
HETATM 6084 C C21  . LPP C 2 .   ? 98.35400  106.71000 131.02500 1.000 41.21272  ? 601 LPP A C21  1 
HETATM 6085 C C22  . LPP C 2 .   ? 97.82800  105.25200 130.80200 1.000 40.50897  ? 601 LPP A C22  1 
HETATM 6086 C C23  . LPP C 2 .   ? 97.07300  105.17900 129.42300 1.000 37.72390  ? 601 LPP A C23  1 
HETATM 6087 C C24  . LPP C 2 .   ? 96.47000  103.74600 129.21600 1.000 37.29893  ? 601 LPP A C24  1 
HETATM 6088 C C25  . LPP C 2 .   ? 95.24000  103.55200 130.16000 1.000 39.13368  ? 601 LPP A C25  1 
HETATM 6089 C C26  . LPP C 2 .   ? 94.38000  102.35600 129.67800 1.000 35.89288  ? 601 LPP A C26  1 
HETATM 6090 C C29  . LPP C 2 .   ? 104.15600 111.15300 124.17300 1.000 38.53807  ? 601 LPP A C29  1 
HETATM 6091 O O28  . LPP C 2 .   ? 104.56500 111.32100 125.28500 1.000 40.58978  ? 601 LPP A O28  1 
HETATM 6092 C C30  . LPP C 2 .   ? 103.16600 112.17900 123.54900 1.000 39.66680  ? 601 LPP A C30  1 
HETATM 6093 C C31  . LPP C 2 .   ? 102.06500 111.43300 122.75900 1.000 38.16627  ? 601 LPP A C31  1 
HETATM 6094 C C32  . LPP C 2 .   ? 101.24600 110.54500 123.71100 1.000 37.20611  ? 601 LPP A C32  1 
HETATM 6095 C C33  . LPP C 2 .   ? 100.15100 109.80600 122.91500 1.000 40.97566  ? 601 LPP A C33  1 
HETATM 6096 C C34  . LPP C 2 .   ? 98.75100  110.21800 123.42400 1.000 39.39416  ? 601 LPP A C34  1 
HETATM 6097 C C35  . LPP C 2 .   ? 98.44100  111.68000 122.99100 1.000 36.42949  ? 601 LPP A C35  1 
HETATM 6098 C C36  . LPP C 2 .   ? 97.06700  111.77900 122.26200 1.000 37.90303  ? 601 LPP A C36  1 
HETATM 6099 C C37  . LPP C 2 .   ? 96.18700  112.87400 122.94900 1.000 39.96543  ? 601 LPP A C37  1 
HETATM 6100 C C38  . LPP C 2 .   ? 94.98600  113.23500 122.01000 1.000 40.43302  ? 601 LPP A C38  1 
HETATM 6101 C C39  . LPP C 2 .   ? 93.64400  113.09700 122.79700 1.000 42.39011  ? 601 LPP A C39  1 
HETATM 6102 C C40  . LPP C 2 .   ? 92.45000  113.16700 121.80300 1.000 42.01648  ? 601 LPP A C40  1 
HETATM 6103 C C41  . LPP C 2 .   ? 91.36800  112.14300 122.21400 1.000 42.60953  ? 601 LPP A C41  1 
HETATM 6104 C C42  . LPP C 2 .   ? 90.30600  112.04400 121.09900 1.000 40.66195  ? 601 LPP A C42  1 
HETATM 6105 C C43  . LPP C 2 .   ? 89.39500  110.84300 121.36200 1.000 39.91296  ? 601 LPP A C43  1 
HETATM 6106 C C44  . LPP C 2 .   ? 87.97200  111.18300 120.92400 1.000 39.01002  ? 601 LPP A C44  1 
HETATM 6107 H HC61 . LPP C 2 .   ? 105.46800 109.28500 120.90200 1.000 37.07595  ? 601 LPP A HC61 1 
HETATM 6108 H HC62 . LPP C 2 .   ? 105.86000 107.56200 120.84300 1.000 37.40328  ? 601 LPP A HC62 1 
HETATM 6109 H HC7  . LPP C 2 .   ? 107.42300 108.32500 122.92000 1.000 37.32612  ? 601 LPP A HC7  1 
HETATM 6110 H HC81 . LPP C 2 .   ? 106.46400 110.05000 124.22400 1.000 37.56245  ? 601 LPP A HC81 1 
HETATM 6111 H HC82 . LPP C 2 .   ? 106.31700 110.68500 122.57800 1.000 38.70878  ? 601 LPP A HC82 1 
HETATM 6112 H H121 . LPP C 2 .   ? 103.19200 107.70100 124.25200 1.000 37.71816  ? 601 LPP A H121 1 
HETATM 6113 H H122 . LPP C 2 .   ? 103.69900 108.56600 125.70900 1.000 37.43939  ? 601 LPP A H122 1 
HETATM 6114 H H131 . LPP C 2 .   ? 102.98200 105.69100 125.36100 1.000 37.58345  ? 601 LPP A H131 1 
HETATM 6115 H H132 . LPP C 2 .   ? 104.46900 105.96000 126.29600 1.000 37.74740  ? 601 LPP A H132 1 
HETATM 6116 H H141 . LPP C 2 .   ? 102.21800 105.95600 127.61900 1.000 37.37599  ? 601 LPP A H141 1 
HETATM 6117 H H142 . LPP C 2 .   ? 101.93300 107.53700 126.88300 1.000 38.35022  ? 601 LPP A H142 1 
HETATM 6118 H H151 . LPP C 2 .   ? 104.48300 107.93500 127.77400 1.000 37.37531  ? 601 LPP A H151 1 
HETATM 6119 H H152 . LPP C 2 .   ? 103.06100 108.29500 128.76900 1.000 37.69008  ? 601 LPP A H152 1 
HETATM 6120 H H161 . LPP C 2 .   ? 105.10700 106.69400 129.63800 1.000 37.19117  ? 601 LPP A H161 1 
HETATM 6121 H H162 . LPP C 2 .   ? 104.10200 105.46200 128.85700 1.000 37.49859  ? 601 LPP A H162 1 
HETATM 6122 H H171 . LPP C 2 .   ? 103.71100 106.07100 131.42200 1.000 38.05630  ? 601 LPP A H171 1 
HETATM 6123 H H172 . LPP C 2 .   ? 102.81200 107.44200 130.75900 1.000 37.56043  ? 601 LPP A H172 1 
HETATM 6124 H H181 . LPP C 2 .   ? 101.74200 104.91900 131.21300 1.000 37.87609  ? 601 LPP A H181 1 
HETATM 6125 H H182 . LPP C 2 .   ? 102.11800 104.83800 129.49500 1.000 37.46628  ? 601 LPP A H182 1 
HETATM 6126 H H191 . LPP C 2 .   ? 100.02500 105.81100 129.33500 1.000 37.20273  ? 601 LPP A H191 1 
HETATM 6127 H H192 . LPP C 2 .   ? 100.96900 107.28600 129.51700 1.000 37.46984  ? 601 LPP A H192 1 
HETATM 6128 H H201 . LPP C 2 .   ? 100.19800 107.67400 131.66800 1.000 37.76242  ? 601 LPP A H201 1 
HETATM 6129 H H202 . LPP C 2 .   ? 100.09900 105.95600 132.06300 1.000 37.17715  ? 601 LPP A H202 1 
HETATM 6130 H H211 . LPP C 2 .   ? 97.83700  107.15300 131.87400 1.000 38.03979  ? 601 LPP A H211 1 
HETATM 6131 H H212 . LPP C 2 .   ? 98.16000  107.29900 130.14300 1.000 37.87850  ? 601 LPP A H212 1 
HETATM 6132 H H221 . LPP C 2 .   ? 97.14700  104.98700 131.60500 1.000 37.94885  ? 601 LPP A H221 1 
HETATM 6133 H H222 . LPP C 2 .   ? 98.65800  104.56600 130.79500 1.000 37.54247  ? 601 LPP A H222 1 
HETATM 6134 H H231 . LPP C 2 .   ? 97.76600  105.39200 128.62900 1.000 37.64503  ? 601 LPP A H231 1 
HETATM 6135 H H232 . LPP C 2 .   ? 96.27500  105.91200 129.41000 1.000 37.37591  ? 601 LPP A H232 1 
HETATM 6136 H H241 . LPP C 2 .   ? 97.22200  103.00100 129.44500 1.000 37.61448  ? 601 LPP A H241 1 
HETATM 6137 H H242 . LPP C 2 .   ? 96.16000  103.63800 128.18800 1.000 37.74016  ? 601 LPP A H242 1 
HETATM 6138 H H251 . LPP C 2 .   ? 94.63600  104.45300 130.15300 1.000 37.83931  ? 601 LPP A H251 1 
HETATM 6139 H H252 . LPP C 2 .   ? 95.58800  103.35900 131.17300 1.000 37.83562  ? 601 LPP A H252 1 
HETATM 6140 H H261 . LPP C 2 .   ? 94.63100  102.11200 128.64700 1.000 37.91073  ? 601 LPP A H261 1 
HETATM 6141 H H262 . LPP C 2 .   ? 94.57600  101.49100 130.31300 1.000 37.25154  ? 601 LPP A H262 1 
HETATM 6142 H H263 . LPP C 2 .   ? 93.32600  102.61900 129.74100 1.000 36.93876  ? 601 LPP A H263 1 
HETATM 6143 H H301 . LPP C 2 .   ? 102.70800 112.76600 124.34100 1.000 37.81040  ? 601 LPP A H301 1 
HETATM 6144 H H302 . LPP C 2 .   ? 103.71000 112.84300 122.87400 1.000 37.83747  ? 601 LPP A H302 1 
HETATM 6145 H H311 . LPP C 2 .   ? 101.41200 112.15900 122.28500 1.000 37.79481  ? 601 LPP A H311 1 
HETATM 6146 H H312 . LPP C 2 .   ? 102.52700 110.81100 121.99600 1.000 37.51570  ? 601 LPP A H312 1 
HETATM 6147 H H321 . LPP C 2 .   ? 100.78300 111.16700 124.47600 1.000 37.95048  ? 601 LPP A H321 1 
HETATM 6148 H H322 . LPP C 2 .   ? 101.89300 109.81400 124.18300 1.000 37.04125  ? 601 LPP A H322 1 
HETATM 6149 H H331 . LPP C 2 .   ? 100.24100 110.05500 121.86300 1.000 37.82872  ? 601 LPP A H331 1 
HETATM 6150 H H332 . LPP C 2 .   ? 100.27700 108.73700 123.04200 1.000 38.37877  ? 601 LPP A H332 1 
HETATM 6151 H H341 . LPP C 2 .   ? 98.01900  109.54000 123.01500 1.000 37.83942  ? 601 LPP A H341 1 
HETATM 6152 H H342 . LPP C 2 .   ? 98.73000  110.15400 124.50400 1.000 37.27405  ? 601 LPP A H342 1 
HETATM 6153 H H351 . LPP C 2 .   ? 99.21900  112.02800 122.32100 1.000 37.06597  ? 601 LPP A H351 1 
HETATM 6154 H H352 . LPP C 2 .   ? 98.42100  112.31300 123.87200 1.000 37.59887  ? 601 LPP A H352 1 
HETATM 6155 H H361 . LPP C 2 .   ? 96.54700  110.83400 122.30300 1.000 37.65043  ? 601 LPP A H361 1 
HETATM 6156 H H362 . LPP C 2 .   ? 97.23300  112.05100 121.22700 1.000 37.21053  ? 601 LPP A H362 1 
HETATM 6157 H H371 . LPP C 2 .   ? 96.78300  113.75800 123.12500 1.000 38.06234  ? 601 LPP A H371 1 
HETATM 6158 H H372 . LPP C 2 .   ? 95.81100  112.49700 123.89300 1.000 37.79615  ? 601 LPP A H372 1 
HETATM 6159 H H381 . LPP C 2 .   ? 94.97900  112.56100 121.16200 1.000 37.82737  ? 601 LPP A H381 1 
HETATM 6160 H H382 . LPP C 2 .   ? 95.09700  114.26400 121.65600 1.000 37.39938  ? 601 LPP A H382 1 
HETATM 6161 H H391 . LPP C 2 .   ? 93.56300  113.90500 123.51700 1.000 37.80991  ? 601 LPP A H391 1 
HETATM 6162 H H392 . LPP C 2 .   ? 93.62600  112.14600 123.31900 1.000 37.67530  ? 601 LPP A H392 1 
HETATM 6163 H H401 . LPP C 2 .   ? 92.79700  112.94100 120.80200 1.000 37.72704  ? 601 LPP A H401 1 
HETATM 6164 H H402 . LPP C 2 .   ? 92.02600  114.16500 121.82000 1.000 37.69895  ? 601 LPP A H402 1 
HETATM 6165 H H411 . LPP C 2 .   ? 91.82400  111.17300 122.36100 1.000 37.82136  ? 601 LPP A H411 1 
HETATM 6166 H H412 . LPP C 2 .   ? 90.89600  112.46500 123.13500 1.000 38.00202  ? 601 LPP A H412 1 
HETATM 6167 H H421 . LPP C 2 .   ? 89.71200  112.95200 121.08300 1.000 37.56560  ? 601 LPP A H421 1 
HETATM 6168 H H422 . LPP C 2 .   ? 90.80200  111.91900 120.13600 1.000 37.71874  ? 601 LPP A H422 1 
HETATM 6169 H H431 . LPP C 2 .   ? 89.40200  110.60800 122.42600 1.000 37.59135  ? 601 LPP A H431 1 
HETATM 6170 H H432 . LPP C 2 .   ? 89.75000  109.99300 120.80300 1.000 37.77240  ? 601 LPP A H432 1 
HETATM 6171 H H441 . LPP C 2 .   ? 87.56900  111.95600 121.57100 1.000 37.67453  ? 601 LPP A H441 1 
HETATM 6172 H H442 . LPP C 2 .   ? 87.98400  111.54000 119.89700 1.000 37.87667  ? 601 LPP A H442 1 
HETATM 6173 H H443 . LPP C 2 .   ? 87.35300  110.29700 120.99100 1.000 37.48347  ? 601 LPP A H443 1 
HETATM 6174 P P1   . LPP D 2 .   ? 112.17000 110.67000 119.07700 1.000 57.55878  ? 601 LPP B P1   1 
HETATM 6175 O O2   . LPP D 2 .   ? 111.20900 111.71200 118.56100 1.000 43.07051  ? 601 LPP B O2   1 
HETATM 6176 O O3   . LPP D 2 .   ? 111.66700 109.29800 118.70200 1.000 42.45632  ? 601 LPP B O3   1 
HETATM 6177 O O4   . LPP D 2 .   ? 113.53400 110.89000 118.46200 1.000 40.88276  ? 601 LPP B O4   1 
HETATM 6178 O O5   . LPP D 2 .   ? 112.27900 110.78900 120.73300 1.000 41.30308  ? 601 LPP B O5   1 
HETATM 6179 C C6   . LPP D 2 .   ? 113.48200 111.24400 121.29700 1.000 36.51230  ? 601 LPP B C6   1 
HETATM 6180 C C7   . LPP D 2 .   ? 113.37700 111.19300 122.81700 1.000 39.34928  ? 601 LPP B C7   1 
HETATM 6181 C C8   . LPP D 2 .   ? 113.78400 109.78200 123.31400 1.000 44.03033  ? 601 LPP B C8   1 
HETATM 6182 O O9   . LPP D 2 .   ? 114.21600 112.16400 123.37100 1.000 42.13419  ? 601 LPP B O9   1 
HETATM 6183 O O27  . LPP D 2 .   ? 115.20200 109.68900 123.44900 1.000 41.43907  ? 601 LPP B O27  1 
HETATM 6184 C C11  . LPP D 2 .   ? 114.44300 112.01400 124.76000 1.000 42.82302  ? 601 LPP B C11  1 
HETATM 6185 O O10  . LPP D 2 .   ? 113.52100 111.92000 125.51000 1.000 41.24137  ? 601 LPP B O10  1 
HETATM 6186 C C12  . LPP D 2 .   ? 115.90000 111.96100 125.29500 1.000 39.38864  ? 601 LPP B C12  1 
HETATM 6187 C C13  . LPP D 2 .   ? 116.28900 113.34000 125.91000 1.000 40.19170  ? 601 LPP B C13  1 
HETATM 6188 C C14  . LPP D 2 .   ? 116.67600 113.16000 127.40700 1.000 38.50619  ? 601 LPP B C14  1 
HETATM 6189 C C15  . LPP D 2 .   ? 115.44700 112.62400 128.21100 1.000 35.75100  ? 601 LPP B C15  1 
HETATM 6190 C C16  . LPP D 2 .   ? 115.41700 113.27400 129.63500 1.000 39.52949  ? 601 LPP B C16  1 
HETATM 6191 C C17  . LPP D 2 .   ? 116.68900 112.86000 130.43300 1.000 41.48130  ? 601 LPP B C17  1 
HETATM 6192 C C18  . LPP D 2 .   ? 117.69600 114.04900 130.54600 1.000 40.77403  ? 601 LPP B C18  1 
HETATM 6193 C C19  . LPP D 2 .   ? 119.10200 113.63300 130.04100 1.000 37.86269  ? 601 LPP B C19  1 
HETATM 6194 C C20  . LPP D 2 .   ? 119.90800 113.01500 131.21700 1.000 38.57660  ? 601 LPP B C20  1 
HETATM 6195 C C21  . LPP D 2 .   ? 121.41300 112.88200 130.82300 1.000 42.05692  ? 601 LPP B C21  1 
HETATM 6196 C C22  . LPP D 2 .   ? 122.08400 114.29700 130.76600 1.000 41.95351  ? 601 LPP B C22  1 
HETATM 6197 C C23  . LPP D 2 .   ? 122.55100 114.59900 129.29300 1.000 38.26244  ? 601 LPP B C23  1 
HETATM 6198 C C24  . LPP D 2 .   ? 123.17900 116.03500 129.21400 1.000 38.10087  ? 601 LPP B C24  1 
HETATM 6199 C C25  . LPP D 2 .   ? 124.49600 116.08600 130.05300 1.000 39.96189  ? 601 LPP B C25  1 
HETATM 6200 C C26  . LPP D 2 .   ? 125.32900 117.32700 129.64700 1.000 36.76185  ? 601 LPP B C26  1 
HETATM 6201 C C29  . LPP D 2 .   ? 115.63600 108.54100 124.17900 1.000 39.42402  ? 601 LPP B C29  1 
HETATM 6202 O O28  . LPP D 2 .   ? 115.25500 108.36300 125.29900 1.000 40.56874  ? 601 LPP B O28  1 
HETATM 6203 C C30  . LPP D 2 .   ? 116.61300 107.52200 123.52500 1.000 40.72633  ? 601 LPP B C30  1 
HETATM 6204 C C31  . LPP D 2 .   ? 117.76800 108.27400 122.82300 1.000 38.17390  ? 601 LPP B C31  1 
HETATM 6205 C C32  . LPP D 2 .   ? 118.63200 108.99900 123.86800 1.000 38.90834  ? 601 LPP B C32  1 
HETATM 6206 C C33  . LPP D 2 .   ? 119.78900 109.74500 123.16900 1.000 41.21966  ? 601 LPP B C33  1 
HETATM 6207 C C34  . LPP D 2 .   ? 121.12200 108.98200 123.35800 1.000 39.34964  ? 601 LPP B C34  1 
HETATM 6208 C C35  . LPP D 2 .   ? 121.16800 107.73200 122.43600 1.000 36.87436  ? 601 LPP B C35  1 
HETATM 6209 C C36  . LPP D 2 .   ? 122.56600 107.62200 121.76300 1.000 39.05186  ? 601 LPP B C36  1 
HETATM 6210 C C37  . LPP D 2 .   ? 123.64300 107.20700 122.81900 1.000 39.66895  ? 601 LPP B C37  1 
HETATM 6211 C C38  . LPP D 2 .   ? 124.80200 106.44700 122.09000 1.000 41.33471  ? 601 LPP B C38  1 
HETATM 6212 C C39  . LPP D 2 .   ? 126.01300 106.26600 123.06000 1.000 42.90287  ? 601 LPP B C39  1 
HETATM 6213 C C40  . LPP D 2 .   ? 127.34100 106.39000 122.26000 1.000 42.01189  ? 601 LPP B C40  1 
HETATM 6214 C C41  . LPP D 2 .   ? 127.86000 107.84300 122.34900 1.000 42.14095  ? 601 LPP B C41  1 
HETATM 6215 C C42  . LPP D 2 .   ? 128.91500 108.10100 121.25000 1.000 42.23433  ? 601 LPP B C42  1 
HETATM 6216 C C43  . LPP D 2 .   ? 130.31900 108.05400 121.85900 1.000 39.86108  ? 601 LPP B C43  1 
HETATM 6217 C C44  . LPP D 2 .   ? 131.33800 108.51100 120.81800 1.000 38.80088  ? 601 LPP B C44  1 
HETATM 6218 H HC61 . LPP D 2 .   ? 114.29700 110.61100 120.97000 1.000 37.49488  ? 601 LPP B HC61 1 
HETATM 6219 H HC62 . LPP D 2 .   ? 113.66600 112.26200 120.98200 1.000 38.14318  ? 601 LPP B HC62 1 
HETATM 6220 H HC7  . LPP D 2 .   ? 112.35000 111.39500 123.11100 1.000 38.13044  ? 601 LPP B HC7  1 
HETATM 6221 H HC81 . LPP D 2 .   ? 113.31900 109.59800 124.27900 1.000 38.35842  ? 601 LPP B HC81 1 
HETATM 6222 H HC82 . LPP D 2 .   ? 113.44100 109.03600 122.60100 1.000 39.39178  ? 601 LPP B HC82 1 
HETATM 6223 H H121 . LPP D 2 .   ? 116.57200 111.73600 124.47500 1.000 38.20016  ? 601 LPP B H121 1 
HETATM 6224 H H122 . LPP D 2 .   ? 115.98300 111.18400 126.04700 1.000 38.28197  ? 601 LPP B H122 1 
HETATM 6225 H H131 . LPP D 2 .   ? 117.13800 113.75500 125.36300 1.000 38.52638  ? 601 LPP B H131 1 
HETATM 6226 H H132 . LPP D 2 .   ? 115.44700 114.01700 125.83400 1.000 38.66781  ? 601 LPP B H132 1 
HETATM 6227 H H141 . LPP D 2 .   ? 116.98400 114.11700 127.81600 1.000 37.65507  ? 601 LPP B H141 1 
HETATM 6228 H H142 . LPP D 2 .   ? 117.49300 112.45500 127.48500 1.000 38.95162  ? 601 LPP B H142 1 
HETATM 6229 H H151 . LPP D 2 .   ? 114.53100 112.87500 127.68000 1.000 37.79255  ? 601 LPP B H151 1 
HETATM 6230 H H152 . LPP D 2 .   ? 115.52300 111.54300 128.30800 1.000 37.90864  ? 601 LPP B H152 1 
HETATM 6231 H H161 . LPP D 2 .   ? 114.53200 112.92300 130.17000 1.000 38.33200  ? 601 LPP B H161 1 
HETATM 6232 H H162 . LPP D 2 .   ? 115.36600 114.35100 129.53800 1.000 38.55164  ? 601 LPP B H162 1 
HETATM 6233 H H171 . LPP D 2 .   ? 116.39100 112.55100 131.43900 1.000 38.53059  ? 601 LPP B H171 1 
HETATM 6234 H H172 . LPP D 2 .   ? 117.16200 112.02700 129.93600 1.000 38.46206  ? 601 LPP B H172 1 
HETATM 6235 H H181 . LPP D 2 .   ? 117.77000 114.34800 131.58700 1.000 38.58231  ? 601 LPP B H181 1 
HETATM 6236 H H182 . LPP D 2 .   ? 117.35000 114.88900 129.96100 1.000 38.47432  ? 601 LPP B H182 1 
HETATM 6237 H H191 . LPP D 2 .   ? 119.61500 114.50200 129.67200 1.000 38.04147  ? 601 LPP B H191 1 
HETATM 6238 H H192 . LPP D 2 .   ? 119.01000 112.90500 129.23900 1.000 38.15510  ? 601 LPP B H192 1 
HETATM 6239 H H201 . LPP D 2 .   ? 119.50900 112.03000 131.45000 1.000 38.36497  ? 601 LPP B H201 1 
HETATM 6240 H H202 . LPP D 2 .   ? 119.82300 113.64800 132.08500 1.000 37.93711  ? 601 LPP B H202 1 
HETATM 6241 H H211 . LPP D 2 .   ? 121.92600 112.27100 131.56300 1.000 38.57974  ? 601 LPP B H211 1 
HETATM 6242 H H212 . LPP D 2 .   ? 121.48900 112.41200 129.85600 1.000 38.80149  ? 601 LPP B H212 1 
HETATM 6243 H H221 . LPP D 2 .   ? 122.94300 114.31200 131.43100 1.000 38.57051  ? 601 LPP B H221 1 
HETATM 6244 H H222 . LPP D 2 .   ? 121.37600 115.04500 131.07900 1.000 38.37746  ? 601 LPP B H222 1 
HETATM 6245 H H231 . LPP D 2 .   ? 121.70500 114.54300 128.63300 1.000 38.31994  ? 601 LPP B H231 1 
HETATM 6246 H H232 . LPP D 2 .   ? 123.29100 113.86500 128.99300 1.000 38.12751  ? 601 LPP B H232 1 
HETATM 6247 H H241 . LPP D 2 .   ? 122.47400 116.75700 129.60700 1.000 38.31780  ? 601 LPP B H241 1 
HETATM 6248 H H242 . LPP D 2 .   ? 123.39700 116.27100 128.18500 1.000 38.51112  ? 601 LPP B H242 1 
HETATM 6249 H H251 . LPP D 2 .   ? 125.07500 115.18800 129.86900 1.000 38.58830  ? 601 LPP B H251 1 
HETATM 6250 H H252 . LPP D 2 .   ? 124.25000 116.14800 131.11200 1.000 38.48839  ? 601 LPP B H252 1 
HETATM 6251 H H261 . LPP D 2 .   ? 126.36900 117.17600 129.93300 1.000 37.51619  ? 601 LPP B H261 1 
HETATM 6252 H H262 . LPP D 2 .   ? 125.26800 117.47200 128.56700 1.000 38.66595  ? 601 LPP B H262 1 
HETATM 6253 H H263 . LPP D 2 .   ? 124.93800 118.20800 130.15300 1.000 38.14953  ? 601 LPP B H263 1 
HETATM 6254 H H301 . LPP D 2 .   ? 117.02100 106.87000 124.29300 1.000 38.66752  ? 601 LPP B H301 1 
HETATM 6255 H H302 . LPP D 2 .   ? 116.07200 106.92200 122.79000 1.000 38.59364  ? 601 LPP B H302 1 
HETATM 6256 H H311 . LPP D 2 .   ? 118.37400 107.55900 122.27900 1.000 38.41977  ? 601 LPP B H311 1 
HETATM 6257 H H312 . LPP D 2 .   ? 117.35500 109.00200 122.12700 1.000 37.93574  ? 601 LPP B H312 1 
HETATM 6258 H H321 . LPP D 2 .   ? 119.03600 108.27000 124.56800 1.000 38.71456  ? 601 LPP B H321 1 
HETATM 6259 H H322 . LPP D 2 .   ? 118.02400 109.71700 124.40900 1.000 38.04982  ? 601 LPP B H322 1 
HETATM 6260 H H331 . LPP D 2 .   ? 119.57100 109.83500 122.11000 1.000 38.62930  ? 601 LPP B H331 1 
HETATM 6261 H H332 . LPP D 2 .   ? 119.88300 110.73600 123.59800 1.000 38.87943  ? 601 LPP B H332 1 
HETATM 6262 H H341 . LPP D 2 .   ? 121.94200 109.63800 123.11300 1.000 38.50904  ? 601 LPP B H341 1 
HETATM 6263 H H342 . LPP D 2 .   ? 121.21500 108.66900 124.39000 1.000 38.29355  ? 601 LPP B H342 1 
HETATM 6264 H H351 . LPP D 2 .   ? 120.41600 107.82300 121.66200 1.000 38.52295  ? 601 LPP B H351 1 
HETATM 6265 H H352 . LPP D 2 .   ? 120.97700 106.84100 123.02500 1.000 37.83038  ? 601 LPP B H352 1 
HETATM 6266 H H361 . LPP D 2 .   ? 122.83500 108.57600 121.33100 1.000 38.78150  ? 601 LPP B H361 1 
HETATM 6267 H H362 . LPP D 2 .   ? 122.52700 106.87400 120.98100 1.000 37.89564  ? 601 LPP B H362 1 
HETATM 6268 H H371 . LPP D 2 .   ? 123.19600 106.56000 123.55900 1.000 38.58576  ? 601 LPP B H371 1 
HETATM 6269 H H372 . LPP D 2 .   ? 124.03600 108.09500 123.30200 1.000 37.92652  ? 601 LPP B H372 1 
HETATM 6270 H H381 . LPP D 2 .   ? 125.11400 107.01900 121.22400 1.000 38.76642  ? 601 LPP B H381 1 
HETATM 6271 H H382 . LPP D 2 .   ? 124.44600 105.46500 121.76700 1.000 38.12382  ? 601 LPP B H382 1 
HETATM 6272 H H391 . LPP D 2 .   ? 125.96100 105.28700 123.52500 1.000 38.67015  ? 601 LPP B H391 1 
HETATM 6273 H H392 . LPP D 2 .   ? 125.98200 107.03200 123.82800 1.000 38.41330  ? 601 LPP B H392 1 
HETATM 6274 H H401 . LPP D 2 .   ? 127.16300 106.12600 121.22400 1.000 38.32176  ? 601 LPP B H401 1 
HETATM 6275 H H402 . LPP D 2 .   ? 128.08000 105.71700 122.68100 1.000 38.56835  ? 601 LPP B H402 1 
HETATM 6276 H H411 . LPP D 2 .   ? 127.03200 108.52600 122.21700 1.000 38.54181  ? 601 LPP B H411 1 
HETATM 6277 H H412 . LPP D 2 .   ? 128.30700 108.00500 123.32300 1.000 38.67223  ? 601 LPP B H412 1 
HETATM 6278 H H421 . LPP D 2 .   ? 128.83400 107.34400 120.47700 1.000 38.40360  ? 601 LPP B H421 1 
HETATM 6279 H H422 . LPP D 2 .   ? 128.74600 109.08400 120.81200 1.000 38.62732  ? 601 LPP B H422 1 
HETATM 6280 H H431 . LPP D 2 .   ? 130.54700 107.03400 122.16900 1.000 37.99078  ? 601 LPP B H431 1 
HETATM 6281 H H432 . LPP D 2 .   ? 130.36400 108.70800 122.71500 1.000 38.41038  ? 601 LPP B H432 1 
HETATM 6282 H H441 . LPP D 2 .   ? 131.07300 108.10100 119.84800 1.000 38.49040  ? 601 LPP B H441 1 
HETATM 6283 H H442 . LPP D 2 .   ? 131.34000 109.59600 120.76400 1.000 38.12179  ? 601 LPP B H442 1 
HETATM 6284 H H443 . LPP D 2 .   ? 132.32300 108.16100 121.10000 1.000 38.24013  ? 601 LPP B H443 1 
HETATM 6285 O O    . HOH E 3 .   ? 112.09700 108.76900 137.28000 1.000 42.39565  ? 701 HOH A O    1 
HETATM 6286 O O    . HOH E 3 .   ? 109.81000 109.82400 132.92900 1.000 32.79652  ? 702 HOH A O    1 
HETATM 6287 O O    . HOH F 3 .   ? 107.55000 110.87800 137.28000 1.000 48.28192  ? 701 HOH B O    1 
# 
