data_8ZTH
# 
_entry.id   8ZTH 
# 
_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   8ZTH         pdb_00008zth 10.2210/pdb8zth/pdb 
WWPDB D_1300047436 ?            ?                   
EMDB  EMD-60462    ?            ?                   
# 
_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                        8ZTH 
_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 (narrow class)' 
_pdbx_database_related.db_id          EMD-60462 
_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 DECANE                                    142.282   1 ? ? ? ? 
3 non-polymer syn 'PALMITIC ACID'                           256.424   1 ? ? ? ? 
4 non-polymer syn N-OCTANE                                  114.229   1 ? ? ? ? 
5 water       nat water                                     18.015    4 ? ? ? ? 
# 
_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 DECANE          D10 
3 'PALMITIC ACID' PLM 
4 N-OCTANE        OCT 
5 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 
D10 non-polymer         . DECANE          ? 'C10 H22'        142.282 
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 
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 
OCT non-polymer         . N-OCTANE        ? 'C8 H18'         114.229 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PLM non-polymer         . 'PALMITIC ACID' ? 'C16 H32 O2'     256.424 
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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 OCT ? ? OCT ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PLM ? ? PLM ? ? 'SUBJECT OF INVESTIGATION' ? 
3 D10 ? ? D10 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 D10 1 601 604 D10 D10 A . 
D 3 PLM 1 602 605 PLM PLM A . 
E 4 OCT 1 601 601 OCT OCT B . 
F 5 HOH 1 701 1   HOH HOH A . 
G 5 HOH 1 701 2   HOH HOH B . 
G 5 HOH 2 702 3   HOH HOH B . 
G 5 HOH 3 703 4   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 ASP 166 ? CG  ? A ASP 166 CG  
6  1 Y 1 A ASP 166 ? OD1 ? A ASP 166 OD1 
7  1 Y 1 A ASP 166 ? OD2 ? A ASP 166 OD2 
8  1 Y 1 A LYS 300 ? CG  ? A LYS 300 CG  
9  1 Y 1 A LYS 300 ? CD  ? A LYS 300 CD  
10 1 Y 1 A LYS 300 ? CE  ? A LYS 300 CE  
11 1 Y 1 A LYS 300 ? NZ  ? A LYS 300 NZ  
12 1 Y 1 A GLU 307 ? CG  ? A GLU 307 CG  
13 1 Y 1 A GLU 307 ? CD  ? A GLU 307 CD  
14 1 Y 1 A GLU 307 ? OE1 ? A GLU 307 OE1 
15 1 Y 1 A GLU 307 ? OE2 ? A GLU 307 OE2 
16 1 Y 1 A GLU 571 ? CG  ? A GLU 571 CG  
17 1 Y 1 A GLU 571 ? CD  ? A GLU 571 CD  
18 1 Y 1 A GLU 571 ? OE1 ? A GLU 571 OE1 
19 1 Y 1 A GLU 571 ? OE2 ? A GLU 571 OE2 
20 1 Y 1 B GLU 79  ? CG  ? B GLU 79  CG  
21 1 Y 1 B GLU 79  ? CD  ? B GLU 79  CD  
22 1 Y 1 B GLU 79  ? OE1 ? B GLU 79  OE1 
23 1 Y 1 B GLU 79  ? OE2 ? B GLU 79  OE2 
24 1 Y 1 B ASP 166 ? CG  ? B ASP 166 CG  
25 1 Y 1 B ASP 166 ? OD1 ? B ASP 166 OD1 
26 1 Y 1 B ASP 166 ? OD2 ? B ASP 166 OD2 
27 1 Y 1 B LYS 300 ? CG  ? B LYS 300 CG  
28 1 Y 1 B LYS 300 ? CD  ? B LYS 300 CD  
29 1 Y 1 B LYS 300 ? CE  ? B LYS 300 CE  
30 1 Y 1 B LYS 300 ? NZ  ? B LYS 300 NZ  
31 1 Y 1 B GLU 307 ? CG  ? B GLU 307 CG  
32 1 Y 1 B GLU 307 ? CD  ? B GLU 307 CD  
33 1 Y 1 B GLU 307 ? OE1 ? B GLU 307 OE1 
34 1 Y 1 B GLU 307 ? OE2 ? B GLU 307 OE2 
35 1 Y 1 B GLU 571 ? CG  ? B GLU 571 CG  
36 1 Y 1 B GLU 571 ? CD  ? B GLU 571 CD  
37 1 Y 1 B GLU 571 ? OE1 ? B GLU 571 OE1 
38 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                     8ZTH 
_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                         8ZTH 
_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                   8ZTH 
_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                                 8ZTH 
_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                     8ZTH 
_struct.title                        'AtALMT9 with LMNG (narrow 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        8ZTH 
_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 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_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 8ZTH A 1 ? 598 ? Q9LS46 1 ? 598 ? 1 598 
2 1 8ZTH 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,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 77  ? ASP A 84  ? ALA A 77  ASP A 84  1 ? 8  
HELX_P HELX_P2  AA2 ARG A 86  ? GLN A 108 ? ARG A 86  GLN A 108 1 ? 23 
HELX_P HELX_P3  AA3 PRO A 112 ? TYR A 117 ? PRO A 112 TYR A 117 1 ? 6  
HELX_P HELX_P4  AA4 SER A 118 ? PHE A 129 ? SER A 118 PHE A 129 1 ? 12 
HELX_P HELX_P5  AA5 THR A 132 ? SER A 161 ? THR A 132 SER A 161 1 ? 30 
HELX_P HELX_P6  AA6 ILE A 170 ? TYR A 189 ? ILE A 170 TYR A 189 1 ? 20 
HELX_P HELX_P7  AA7 MET A 192 ? ALA A 194 ? MET A 192 ALA A 194 5 ? 3  
HELX_P HELX_P8  AA8 TYR A 195 ? SER A 212 ? TYR A 195 SER A 212 1 ? 18 
HELX_P HELX_P9  AA9 PHE A 227 ? ILE A 244 ? PHE A 227 ILE A 244 1 ? 18 
HELX_P HELX_P10 AB1 TRP A 248 ? LEU A 276 ? TRP A 248 LEU A 276 1 ? 29 
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 ? ILE A 320 ? SER A 308 ILE A 320 1 ? 13 
HELX_P HELX_P13 AB4 TRP A 335 ? LEU A 360 ? TRP A 335 LEU A 360 1 ? 26 
HELX_P HELX_P14 AB5 PRO A 366 ? GLN A 371 ? PRO A 366 GLN A 371 1 ? 6  
HELX_P HELX_P15 AB6 PHE A 373 ? LYS A 397 ? PHE A 373 LYS A 397 1 ? 25 
HELX_P HELX_P16 AB7 LEU A 407 ? LYS A 424 ? LEU A 407 LYS A 424 1 ? 18 
HELX_P HELX_P17 AB8 SER A 425 ? LEU A 428 ? SER A 425 LEU A 428 5 ? 4  
HELX_P HELX_P18 AB9 THR A 528 ? ARG A 550 ? THR A 528 ARG A 550 1 ? 23 
HELX_P HELX_P19 AC1 ARG A 550 ? ALA A 565 ? ARG A 550 ALA A 565 1 ? 16 
HELX_P HELX_P20 AC2 TRP B 78  ? ASP B 84  ? TRP B 78  ASP B 84  1 ? 7  
HELX_P HELX_P21 AC3 PRO B 85  ? TYR B 107 ? PRO B 85  TYR B 107 1 ? 23 
HELX_P HELX_P22 AC4 PRO B 112 ? TYR B 117 ? PRO B 112 TYR B 117 5 ? 6  
HELX_P HELX_P23 AC5 SER B 118 ? VAL B 128 ? SER B 118 VAL B 128 1 ? 11 
HELX_P HELX_P24 AC6 THR B 132 ? THR B 162 ? THR B 132 THR B 162 1 ? 31 
HELX_P HELX_P25 AC7 THR B 173 ? LEU B 188 ? THR B 173 LEU B 188 1 ? 16 
HELX_P HELX_P26 AC8 TYR B 195 ? GLY B 213 ? TYR B 195 GLY B 213 1 ? 19 
HELX_P HELX_P27 AC9 PHE B 219 ? ILE B 244 ? PHE B 219 ILE B 244 1 ? 26 
HELX_P HELX_P28 AD1 TRP B 248 ? ARG B 277 ? TRP B 248 ARG B 277 1 ? 30 
HELX_P HELX_P29 AD2 TYR B 299 ? GLU B 307 ? TYR B 299 GLU B 307 1 ? 9  
HELX_P HELX_P30 AD3 SER B 308 ? ILE B 320 ? SER B 308 ILE B 320 1 ? 13 
HELX_P HELX_P31 AD4 TRP B 335 ? LEU B 360 ? TRP B 335 LEU B 360 1 ? 26 
HELX_P HELX_P32 AD5 PRO B 366 ? GLN B 371 ? PRO B 366 GLN B 371 1 ? 6  
HELX_P HELX_P33 AD6 PHE B 373 ? LYS B 397 ? PHE B 373 LYS B 397 1 ? 25 
HELX_P HELX_P34 AD7 LEU B 407 ? LYS B 424 ? LEU B 407 LYS B 424 1 ? 18 
HELX_P HELX_P35 AD8 SER B 425 ? LEU B 428 ? SER B 425 LEU B 428 5 ? 4  
HELX_P HELX_P36 AD9 THR B 528 ? ARG B 550 ? THR B 528 ARG B 550 1 ? 23 
HELX_P HELX_P37 AE1 ARG B 550 ? ALA B 565 ? ARG B 550 ALA B 565 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   8ZTH 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PRO A 85  ? ? -68.82  1.43   
2  1 ASP A 166 ? ? 67.29   -68.59 
3  1 TRP A 167 ? ? -84.47  49.66  
4  1 TYR A 195 ? ? -105.29 40.83  
5  1 TYR A 245 ? ? 53.00   70.84  
6  1 ASP B 166 ? ? 72.66   -29.38 
7  1 GLU B 169 ? ? 76.82   -4.84  
8  1 MET B 192 ? ? -90.91  51.06  
9  1 TYR B 245 ? ? 48.96   71.09  
10 1 PRO B 334 ? ? -69.68  69.22  
11 1 LEU B 360 ? ? -99.06  34.56  
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8ZTH 
_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                    8ZTH 
_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                  2.63 
_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               168036 
_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                        8ZTH 
_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              8ZTH 
_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                8ZTH 
_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              8ZTH 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A 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  
D10 C1   C N N 88  
D10 C2   C N N 89  
D10 C3   C N N 90  
D10 C4   C N N 91  
D10 C5   C N N 92  
D10 C6   C N N 93  
D10 C7   C N N 94  
D10 C8   C N N 95  
D10 C9   C N N 96  
D10 C10  C N N 97  
D10 H11  H N N 98  
D10 H12  H N N 99  
D10 H13  H N N 100 
D10 H21  H N N 101 
D10 H22  H N N 102 
D10 H31  H N N 103 
D10 H32  H N N 104 
D10 H41  H N N 105 
D10 H42  H N N 106 
D10 H51  H N N 107 
D10 H52  H N N 108 
D10 H61  H N N 109 
D10 H62  H N N 110 
D10 H71  H N N 111 
D10 H72  H N N 112 
D10 H81  H N N 113 
D10 H82  H N N 114 
D10 H91  H N N 115 
D10 H92  H N N 116 
D10 H101 H N N 117 
D10 H102 H N N 118 
D10 H103 H N N 119 
GLN N    N N N 120 
GLN CA   C N S 121 
GLN C    C N N 122 
GLN O    O N N 123 
GLN CB   C N N 124 
GLN CG   C N N 125 
GLN CD   C N N 126 
GLN OE1  O N N 127 
GLN NE2  N N N 128 
GLN OXT  O N N 129 
GLN H    H N N 130 
GLN H2   H N N 131 
GLN HA   H N N 132 
GLN HB2  H N N 133 
GLN HB3  H N N 134 
GLN HG2  H N N 135 
GLN HG3  H N N 136 
GLN HE21 H N N 137 
GLN HE22 H N N 138 
GLN HXT  H N N 139 
GLU N    N N N 140 
GLU CA   C N S 141 
GLU C    C N N 142 
GLU O    O N N 143 
GLU CB   C N N 144 
GLU CG   C N N 145 
GLU CD   C N N 146 
GLU OE1  O N N 147 
GLU OE2  O N N 148 
GLU OXT  O N N 149 
GLU H    H N N 150 
GLU H2   H N N 151 
GLU HA   H N N 152 
GLU HB2  H N N 153 
GLU HB3  H N N 154 
GLU HG2  H N N 155 
GLU HG3  H N N 156 
GLU HE2  H N N 157 
GLU HXT  H N N 158 
GLY N    N N N 159 
GLY CA   C N N 160 
GLY C    C N N 161 
GLY O    O N N 162 
GLY OXT  O N N 163 
GLY H    H N N 164 
GLY H2   H N N 165 
GLY HA2  H N N 166 
GLY HA3  H N N 167 
GLY HXT  H N N 168 
HIS N    N N N 169 
HIS CA   C N S 170 
HIS C    C N N 171 
HIS O    O N N 172 
HIS CB   C N N 173 
HIS CG   C Y N 174 
HIS ND1  N Y N 175 
HIS CD2  C Y N 176 
HIS CE1  C Y N 177 
HIS NE2  N Y N 178 
HIS OXT  O N N 179 
HIS H    H N N 180 
HIS H2   H N N 181 
HIS HA   H N N 182 
HIS HB2  H N N 183 
HIS HB3  H N N 184 
HIS HD1  H N N 185 
HIS HD2  H N N 186 
HIS HE1  H N N 187 
HIS HE2  H N N 188 
HIS HXT  H N N 189 
HOH O    O N N 190 
HOH H1   H N N 191 
HOH H2   H N N 192 
ILE N    N N N 193 
ILE CA   C N S 194 
ILE C    C N N 195 
ILE O    O N N 196 
ILE CB   C N S 197 
ILE CG1  C N N 198 
ILE CG2  C N N 199 
ILE CD1  C N N 200 
ILE OXT  O N N 201 
ILE H    H N N 202 
ILE H2   H N N 203 
ILE HA   H N N 204 
ILE HB   H N N 205 
ILE HG12 H N N 206 
ILE HG13 H N N 207 
ILE HG21 H N N 208 
ILE HG22 H N N 209 
ILE HG23 H N N 210 
ILE HD11 H N N 211 
ILE HD12 H N N 212 
ILE HD13 H N N 213 
ILE HXT  H N N 214 
LEU N    N N N 215 
LEU CA   C N S 216 
LEU C    C N N 217 
LEU O    O N N 218 
LEU CB   C N N 219 
LEU CG   C N N 220 
LEU CD1  C N N 221 
LEU CD2  C N N 222 
LEU OXT  O N N 223 
LEU H    H N N 224 
LEU H2   H N N 225 
LEU HA   H N N 226 
LEU HB2  H N N 227 
LEU HB3  H N N 228 
LEU HG   H N N 229 
LEU HD11 H N N 230 
LEU HD12 H N N 231 
LEU HD13 H N N 232 
LEU HD21 H N N 233 
LEU HD22 H N N 234 
LEU HD23 H N N 235 
LEU HXT  H N N 236 
LYS N    N N N 237 
LYS CA   C N S 238 
LYS C    C N N 239 
LYS O    O N N 240 
LYS CB   C N N 241 
LYS CG   C N N 242 
LYS CD   C N N 243 
LYS CE   C N N 244 
LYS NZ   N N N 245 
LYS OXT  O N N 246 
LYS H    H N N 247 
LYS H2   H N N 248 
LYS HA   H N N 249 
LYS HB2  H N N 250 
LYS HB3  H N N 251 
LYS HG2  H N N 252 
LYS HG3  H N N 253 
LYS HD2  H N N 254 
LYS HD3  H N N 255 
LYS HE2  H N N 256 
LYS HE3  H N N 257 
LYS HZ1  H N N 258 
LYS HZ2  H N N 259 
LYS HZ3  H N N 260 
LYS HXT  H N N 261 
MET N    N N N 262 
MET CA   C N S 263 
MET C    C N N 264 
MET O    O N N 265 
MET CB   C N N 266 
MET CG   C N N 267 
MET SD   S N N 268 
MET CE   C N N 269 
MET OXT  O N N 270 
MET H    H N N 271 
MET H2   H N N 272 
MET HA   H N N 273 
MET HB2  H N N 274 
MET HB3  H N N 275 
MET HG2  H N N 276 
MET HG3  H N N 277 
MET HE1  H N N 278 
MET HE2  H N N 279 
MET HE3  H N N 280 
MET HXT  H N N 281 
OCT C1   C N N 282 
OCT C2   C N N 283 
OCT C3   C N N 284 
OCT C4   C N N 285 
OCT C5   C N N 286 
OCT C6   C N N 287 
OCT C7   C N N 288 
OCT C8   C N N 289 
OCT H11  H N N 290 
OCT H12  H N N 291 
OCT H13  H N N 292 
OCT H21  H N N 293 
OCT H22  H N N 294 
OCT H31  H N N 295 
OCT H32  H N N 296 
OCT H41  H N N 297 
OCT H42  H N N 298 
OCT H51  H N N 299 
OCT H52  H N N 300 
OCT H61  H N N 301 
OCT H62  H N N 302 
OCT H71  H N N 303 
OCT H72  H N N 304 
OCT H81  H N N 305 
OCT H82  H N N 306 
OCT H83  H N N 307 
PHE N    N N N 308 
PHE CA   C N S 309 
PHE C    C N N 310 
PHE O    O N N 311 
PHE CB   C N N 312 
PHE CG   C Y N 313 
PHE CD1  C Y N 314 
PHE CD2  C Y N 315 
PHE CE1  C Y N 316 
PHE CE2  C Y N 317 
PHE CZ   C Y N 318 
PHE OXT  O N N 319 
PHE H    H N N 320 
PHE H2   H N N 321 
PHE HA   H N N 322 
PHE HB2  H N N 323 
PHE HB3  H N N 324 
PHE HD1  H N N 325 
PHE HD2  H N N 326 
PHE HE1  H N N 327 
PHE HE2  H N N 328 
PHE HZ   H N N 329 
PHE HXT  H N N 330 
PLM C1   C N N 331 
PLM O1   O N N 332 
PLM O2   O N N 333 
PLM C2   C N N 334 
PLM C3   C N N 335 
PLM C4   C N N 336 
PLM C5   C N N 337 
PLM C6   C N N 338 
PLM C7   C N N 339 
PLM C8   C N N 340 
PLM C9   C N N 341 
PLM CA   C N N 342 
PLM CB   C N N 343 
PLM CC   C N N 344 
PLM CD   C N N 345 
PLM CE   C N N 346 
PLM CF   C N N 347 
PLM CG   C N N 348 
PLM H    H N N 349 
PLM H21  H N N 350 
PLM H22  H N N 351 
PLM H31  H N N 352 
PLM H32  H N N 353 
PLM H41  H N N 354 
PLM H42  H N N 355 
PLM H51  H N N 356 
PLM H52  H N N 357 
PLM H61  H N N 358 
PLM H62  H N N 359 
PLM H71  H N N 360 
PLM H72  H N N 361 
PLM H81  H N N 362 
PLM H82  H N N 363 
PLM H91  H N N 364 
PLM H92  H N N 365 
PLM HA1  H N N 366 
PLM HA2  H N N 367 
PLM HB1  H N N 368 
PLM HB2  H N N 369 
PLM HC1  H N N 370 
PLM HC2  H N N 371 
PLM HD1  H N N 372 
PLM HD2  H N N 373 
PLM HE1  H N N 374 
PLM HE2  H N N 375 
PLM HF1  H N N 376 
PLM HF2  H N N 377 
PLM HG1  H N N 378 
PLM HG2  H N N 379 
PLM HG3  H N N 380 
PRO N    N N N 381 
PRO CA   C N S 382 
PRO C    C N N 383 
PRO O    O N N 384 
PRO CB   C N N 385 
PRO CG   C N N 386 
PRO CD   C N N 387 
PRO OXT  O N N 388 
PRO H    H N N 389 
PRO HA   H N N 390 
PRO HB2  H N N 391 
PRO HB3  H N N 392 
PRO HG2  H N N 393 
PRO HG3  H N N 394 
PRO HD2  H N N 395 
PRO HD3  H N N 396 
PRO HXT  H N N 397 
SER N    N N N 398 
SER CA   C N S 399 
SER C    C N N 400 
SER O    O N N 401 
SER CB   C N N 402 
SER OG   O N N 403 
SER OXT  O N N 404 
SER H    H N N 405 
SER H2   H N N 406 
SER HA   H N N 407 
SER HB2  H N N 408 
SER HB3  H N N 409 
SER HG   H N N 410 
SER HXT  H N N 411 
THR N    N N N 412 
THR CA   C N S 413 
THR C    C N N 414 
THR O    O N N 415 
THR CB   C N R 416 
THR OG1  O N N 417 
THR CG2  C N N 418 
THR OXT  O N N 419 
THR H    H N N 420 
THR H2   H N N 421 
THR HA   H N N 422 
THR HB   H N N 423 
THR HG1  H N N 424 
THR HG21 H N N 425 
THR HG22 H N N 426 
THR HG23 H N N 427 
THR HXT  H N N 428 
TRP N    N N N 429 
TRP CA   C N S 430 
TRP C    C N N 431 
TRP O    O N N 432 
TRP CB   C N N 433 
TRP CG   C Y N 434 
TRP CD1  C Y N 435 
TRP CD2  C Y N 436 
TRP NE1  N Y N 437 
TRP CE2  C Y N 438 
TRP CE3  C Y N 439 
TRP CZ2  C Y N 440 
TRP CZ3  C Y N 441 
TRP CH2  C Y N 442 
TRP OXT  O N N 443 
TRP H    H N N 444 
TRP H2   H N N 445 
TRP HA   H N N 446 
TRP HB2  H N N 447 
TRP HB3  H N N 448 
TRP HD1  H N N 449 
TRP HE1  H N N 450 
TRP HE3  H N N 451 
TRP HZ2  H N N 452 
TRP HZ3  H N N 453 
TRP HH2  H N N 454 
TRP HXT  H N N 455 
TYR N    N N N 456 
TYR CA   C N S 457 
TYR C    C N N 458 
TYR O    O N N 459 
TYR CB   C N N 460 
TYR CG   C Y N 461 
TYR CD1  C Y N 462 
TYR CD2  C Y N 463 
TYR CE1  C Y N 464 
TYR CE2  C Y N 465 
TYR CZ   C Y N 466 
TYR OH   O N N 467 
TYR OXT  O N N 468 
TYR H    H N N 469 
TYR H2   H N N 470 
TYR HA   H N N 471 
TYR HB2  H N N 472 
TYR HB3  H N N 473 
TYR HD1  H N N 474 
TYR HD2  H N N 475 
TYR HE1  H N N 476 
TYR HE2  H N N 477 
TYR HH   H N N 478 
TYR HXT  H N N 479 
VAL N    N N N 480 
VAL CA   C N S 481 
VAL C    C N N 482 
VAL O    O N N 483 
VAL CB   C N N 484 
VAL CG1  C N N 485 
VAL CG2  C N N 486 
VAL OXT  O N N 487 
VAL H    H N N 488 
VAL H2   H N N 489 
VAL HA   H N N 490 
VAL HB   H N N 491 
VAL HG11 H N N 492 
VAL HG12 H N N 493 
VAL HG13 H N N 494 
VAL HG21 H N N 495 
VAL HG22 H N N 496 
VAL HG23 H N N 497 
VAL HXT  H N N 498 
# 
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  
D10 C1  C2   sing N N 83  
D10 C1  H11  sing N N 84  
D10 C1  H12  sing N N 85  
D10 C1  H13  sing N N 86  
D10 C2  C3   sing N N 87  
D10 C2  H21  sing N N 88  
D10 C2  H22  sing N N 89  
D10 C3  C4   sing N N 90  
D10 C3  H31  sing N N 91  
D10 C3  H32  sing N N 92  
D10 C4  C5   sing N N 93  
D10 C4  H41  sing N N 94  
D10 C4  H42  sing N N 95  
D10 C5  C6   sing N N 96  
D10 C5  H51  sing N N 97  
D10 C5  H52  sing N N 98  
D10 C6  C7   sing N N 99  
D10 C6  H61  sing N N 100 
D10 C6  H62  sing N N 101 
D10 C7  C8   sing N N 102 
D10 C7  H71  sing N N 103 
D10 C7  H72  sing N N 104 
D10 C8  C9   sing N N 105 
D10 C8  H81  sing N N 106 
D10 C8  H82  sing N N 107 
D10 C9  C10  sing N N 108 
D10 C9  H91  sing N N 109 
D10 C9  H92  sing N N 110 
D10 C10 H101 sing N N 111 
D10 C10 H102 sing N N 112 
D10 C10 H103 sing N N 113 
GLN N   CA   sing N N 114 
GLN N   H    sing N N 115 
GLN N   H2   sing N N 116 
GLN CA  C    sing N N 117 
GLN CA  CB   sing N N 118 
GLN CA  HA   sing N N 119 
GLN C   O    doub N N 120 
GLN C   OXT  sing N N 121 
GLN CB  CG   sing N N 122 
GLN CB  HB2  sing N N 123 
GLN CB  HB3  sing N N 124 
GLN CG  CD   sing N N 125 
GLN CG  HG2  sing N N 126 
GLN CG  HG3  sing N N 127 
GLN CD  OE1  doub N N 128 
GLN CD  NE2  sing N N 129 
GLN NE2 HE21 sing N N 130 
GLN NE2 HE22 sing N N 131 
GLN OXT HXT  sing N N 132 
GLU N   CA   sing N N 133 
GLU N   H    sing N N 134 
GLU N   H2   sing N N 135 
GLU CA  C    sing N N 136 
GLU CA  CB   sing N N 137 
GLU CA  HA   sing N N 138 
GLU C   O    doub N N 139 
GLU C   OXT  sing N N 140 
GLU CB  CG   sing N N 141 
GLU CB  HB2  sing N N 142 
GLU CB  HB3  sing N N 143 
GLU CG  CD   sing N N 144 
GLU CG  HG2  sing N N 145 
GLU CG  HG3  sing N N 146 
GLU CD  OE1  doub N N 147 
GLU CD  OE2  sing N N 148 
GLU OE2 HE2  sing N N 149 
GLU OXT HXT  sing N N 150 
GLY N   CA   sing N N 151 
GLY N   H    sing N N 152 
GLY N   H2   sing N N 153 
GLY CA  C    sing N N 154 
GLY CA  HA2  sing N N 155 
GLY CA  HA3  sing N N 156 
GLY C   O    doub N N 157 
GLY C   OXT  sing N N 158 
GLY OXT HXT  sing N N 159 
HIS N   CA   sing N N 160 
HIS N   H    sing N N 161 
HIS N   H2   sing N N 162 
HIS CA  C    sing N N 163 
HIS CA  CB   sing N N 164 
HIS CA  HA   sing N N 165 
HIS C   O    doub N N 166 
HIS C   OXT  sing N N 167 
HIS CB  CG   sing N N 168 
HIS CB  HB2  sing N N 169 
HIS CB  HB3  sing N N 170 
HIS CG  ND1  sing Y N 171 
HIS CG  CD2  doub Y N 172 
HIS ND1 CE1  doub Y N 173 
HIS ND1 HD1  sing N N 174 
HIS CD2 NE2  sing Y N 175 
HIS CD2 HD2  sing N N 176 
HIS CE1 NE2  sing Y N 177 
HIS CE1 HE1  sing N N 178 
HIS NE2 HE2  sing N N 179 
HIS OXT HXT  sing N N 180 
HOH O   H1   sing N N 181 
HOH O   H2   sing N N 182 
ILE N   CA   sing N N 183 
ILE N   H    sing N N 184 
ILE N   H2   sing N N 185 
ILE CA  C    sing N N 186 
ILE CA  CB   sing N N 187 
ILE CA  HA   sing N N 188 
ILE C   O    doub N N 189 
ILE C   OXT  sing N N 190 
ILE CB  CG1  sing N N 191 
ILE CB  CG2  sing N N 192 
ILE CB  HB   sing N N 193 
ILE CG1 CD1  sing N N 194 
ILE CG1 HG12 sing N N 195 
ILE CG1 HG13 sing N N 196 
ILE CG2 HG21 sing N N 197 
ILE CG2 HG22 sing N N 198 
ILE CG2 HG23 sing N N 199 
ILE CD1 HD11 sing N N 200 
ILE CD1 HD12 sing N N 201 
ILE CD1 HD13 sing N N 202 
ILE OXT HXT  sing N N 203 
LEU N   CA   sing N N 204 
LEU N   H    sing N N 205 
LEU N   H2   sing N N 206 
LEU CA  C    sing N N 207 
LEU CA  CB   sing N N 208 
LEU CA  HA   sing N N 209 
LEU C   O    doub N N 210 
LEU C   OXT  sing N N 211 
LEU CB  CG   sing N N 212 
LEU CB  HB2  sing N N 213 
LEU CB  HB3  sing N N 214 
LEU CG  CD1  sing N N 215 
LEU CG  CD2  sing N N 216 
LEU CG  HG   sing N N 217 
LEU CD1 HD11 sing N N 218 
LEU CD1 HD12 sing N N 219 
LEU CD1 HD13 sing N N 220 
LEU CD2 HD21 sing N N 221 
LEU CD2 HD22 sing N N 222 
LEU CD2 HD23 sing N N 223 
LEU OXT HXT  sing N N 224 
LYS N   CA   sing N N 225 
LYS N   H    sing N N 226 
LYS N   H2   sing N N 227 
LYS CA  C    sing N N 228 
LYS CA  CB   sing N N 229 
LYS CA  HA   sing N N 230 
LYS C   O    doub N N 231 
LYS C   OXT  sing N N 232 
LYS CB  CG   sing N N 233 
LYS CB  HB2  sing N N 234 
LYS CB  HB3  sing N N 235 
LYS CG  CD   sing N N 236 
LYS CG  HG2  sing N N 237 
LYS CG  HG3  sing N N 238 
LYS CD  CE   sing N N 239 
LYS CD  HD2  sing N N 240 
LYS CD  HD3  sing N N 241 
LYS CE  NZ   sing N N 242 
LYS CE  HE2  sing N N 243 
LYS CE  HE3  sing N N 244 
LYS NZ  HZ1  sing N N 245 
LYS NZ  HZ2  sing N N 246 
LYS NZ  HZ3  sing N N 247 
LYS OXT HXT  sing N N 248 
MET N   CA   sing N N 249 
MET N   H    sing N N 250 
MET N   H2   sing N N 251 
MET CA  C    sing N N 252 
MET CA  CB   sing N N 253 
MET CA  HA   sing N N 254 
MET C   O    doub N N 255 
MET C   OXT  sing N N 256 
MET CB  CG   sing N N 257 
MET CB  HB2  sing N N 258 
MET CB  HB3  sing N N 259 
MET CG  SD   sing N N 260 
MET CG  HG2  sing N N 261 
MET CG  HG3  sing N N 262 
MET SD  CE   sing N N 263 
MET CE  HE1  sing N N 264 
MET CE  HE2  sing N N 265 
MET CE  HE3  sing N N 266 
MET OXT HXT  sing N N 267 
OCT C1  C2   sing N N 268 
OCT C1  H11  sing N N 269 
OCT C1  H12  sing N N 270 
OCT C1  H13  sing N N 271 
OCT C2  C3   sing N N 272 
OCT C2  H21  sing N N 273 
OCT C2  H22  sing N N 274 
OCT C3  C4   sing N N 275 
OCT C3  H31  sing N N 276 
OCT C3  H32  sing N N 277 
OCT C4  C5   sing N N 278 
OCT C4  H41  sing N N 279 
OCT C4  H42  sing N N 280 
OCT C5  C6   sing N N 281 
OCT C5  H51  sing N N 282 
OCT C5  H52  sing N N 283 
OCT C6  C7   sing N N 284 
OCT C6  H61  sing N N 285 
OCT C6  H62  sing N N 286 
OCT C7  C8   sing N N 287 
OCT C7  H71  sing N N 288 
OCT C7  H72  sing N N 289 
OCT C8  H81  sing N N 290 
OCT C8  H82  sing N N 291 
OCT C8  H83  sing N N 292 
PHE N   CA   sing N N 293 
PHE N   H    sing N N 294 
PHE N   H2   sing N N 295 
PHE CA  C    sing N N 296 
PHE CA  CB   sing N N 297 
PHE CA  HA   sing N N 298 
PHE C   O    doub N N 299 
PHE C   OXT  sing N N 300 
PHE CB  CG   sing N N 301 
PHE CB  HB2  sing N N 302 
PHE CB  HB3  sing N N 303 
PHE CG  CD1  doub Y N 304 
PHE CG  CD2  sing Y N 305 
PHE CD1 CE1  sing Y N 306 
PHE CD1 HD1  sing N N 307 
PHE CD2 CE2  doub Y N 308 
PHE CD2 HD2  sing N N 309 
PHE CE1 CZ   doub Y N 310 
PHE CE1 HE1  sing N N 311 
PHE CE2 CZ   sing Y N 312 
PHE CE2 HE2  sing N N 313 
PHE CZ  HZ   sing N N 314 
PHE OXT HXT  sing N N 315 
PLM C1  O1   sing N N 316 
PLM C1  O2   doub N N 317 
PLM C1  C2   sing N N 318 
PLM O1  H    sing N N 319 
PLM C2  C3   sing N N 320 
PLM C2  H21  sing N N 321 
PLM C2  H22  sing N N 322 
PLM C3  C4   sing N N 323 
PLM C3  H31  sing N N 324 
PLM C3  H32  sing N N 325 
PLM C4  C5   sing N N 326 
PLM C4  H41  sing N N 327 
PLM C4  H42  sing N N 328 
PLM C5  C6   sing N N 329 
PLM C5  H51  sing N N 330 
PLM C5  H52  sing N N 331 
PLM C6  C7   sing N N 332 
PLM C6  H61  sing N N 333 
PLM C6  H62  sing N N 334 
PLM C7  C8   sing N N 335 
PLM C7  H71  sing N N 336 
PLM C7  H72  sing N N 337 
PLM C8  C9   sing N N 338 
PLM C8  H81  sing N N 339 
PLM C8  H82  sing N N 340 
PLM C9  CA   sing N N 341 
PLM C9  H91  sing N N 342 
PLM C9  H92  sing N N 343 
PLM CA  CB   sing N N 344 
PLM CA  HA1  sing N N 345 
PLM CA  HA2  sing N N 346 
PLM CB  CC   sing N N 347 
PLM CB  HB1  sing N N 348 
PLM CB  HB2  sing N N 349 
PLM CC  CD   sing N N 350 
PLM CC  HC1  sing N N 351 
PLM CC  HC2  sing N N 352 
PLM CD  CE   sing N N 353 
PLM CD  HD1  sing N N 354 
PLM CD  HD2  sing N N 355 
PLM CE  CF   sing N N 356 
PLM CE  HE1  sing N N 357 
PLM CE  HE2  sing N N 358 
PLM CF  CG   sing N N 359 
PLM CF  HF1  sing N N 360 
PLM CF  HF2  sing N N 361 
PLM CG  HG1  sing N N 362 
PLM CG  HG2  sing N N 363 
PLM CG  HG3  sing N N 364 
PRO N   CA   sing N N 365 
PRO N   CD   sing N N 366 
PRO N   H    sing N N 367 
PRO CA  C    sing N N 368 
PRO CA  CB   sing N N 369 
PRO CA  HA   sing N N 370 
PRO C   O    doub N N 371 
PRO C   OXT  sing N N 372 
PRO CB  CG   sing N N 373 
PRO CB  HB2  sing N N 374 
PRO CB  HB3  sing N N 375 
PRO CG  CD   sing N N 376 
PRO CG  HG2  sing N N 377 
PRO CG  HG3  sing N N 378 
PRO CD  HD2  sing N N 379 
PRO CD  HD3  sing N N 380 
PRO OXT HXT  sing N N 381 
SER N   CA   sing N N 382 
SER N   H    sing N N 383 
SER N   H2   sing N N 384 
SER CA  C    sing N N 385 
SER CA  CB   sing N N 386 
SER CA  HA   sing N N 387 
SER C   O    doub N N 388 
SER C   OXT  sing N N 389 
SER CB  OG   sing N N 390 
SER CB  HB2  sing N N 391 
SER CB  HB3  sing N N 392 
SER OG  HG   sing N N 393 
SER OXT HXT  sing N N 394 
THR N   CA   sing N N 395 
THR N   H    sing N N 396 
THR N   H2   sing N N 397 
THR CA  C    sing N N 398 
THR CA  CB   sing N N 399 
THR CA  HA   sing N N 400 
THR C   O    doub N N 401 
THR C   OXT  sing N N 402 
THR CB  OG1  sing N N 403 
THR CB  CG2  sing N N 404 
THR CB  HB   sing N N 405 
THR OG1 HG1  sing N N 406 
THR CG2 HG21 sing N N 407 
THR CG2 HG22 sing N N 408 
THR CG2 HG23 sing N N 409 
THR OXT HXT  sing N N 410 
TRP N   CA   sing N N 411 
TRP N   H    sing N N 412 
TRP N   H2   sing N N 413 
TRP CA  C    sing N N 414 
TRP CA  CB   sing N N 415 
TRP CA  HA   sing N N 416 
TRP C   O    doub N N 417 
TRP C   OXT  sing N N 418 
TRP CB  CG   sing N N 419 
TRP CB  HB2  sing N N 420 
TRP CB  HB3  sing N N 421 
TRP CG  CD1  doub Y N 422 
TRP CG  CD2  sing Y N 423 
TRP CD1 NE1  sing Y N 424 
TRP CD1 HD1  sing N N 425 
TRP CD2 CE2  doub Y N 426 
TRP CD2 CE3  sing Y N 427 
TRP NE1 CE2  sing Y N 428 
TRP NE1 HE1  sing N N 429 
TRP CE2 CZ2  sing Y N 430 
TRP CE3 CZ3  doub Y N 431 
TRP CE3 HE3  sing N N 432 
TRP CZ2 CH2  doub Y N 433 
TRP CZ2 HZ2  sing N N 434 
TRP CZ3 CH2  sing Y N 435 
TRP CZ3 HZ3  sing N N 436 
TRP CH2 HH2  sing N N 437 
TRP OXT HXT  sing N N 438 
TYR N   CA   sing N N 439 
TYR N   H    sing N N 440 
TYR N   H2   sing N N 441 
TYR CA  C    sing N N 442 
TYR CA  CB   sing N N 443 
TYR CA  HA   sing N N 444 
TYR C   O    doub N N 445 
TYR C   OXT  sing N N 446 
TYR CB  CG   sing N N 447 
TYR CB  HB2  sing N N 448 
TYR CB  HB3  sing N N 449 
TYR CG  CD1  doub Y N 450 
TYR CG  CD2  sing Y N 451 
TYR CD1 CE1  sing Y N 452 
TYR CD1 HD1  sing N N 453 
TYR CD2 CE2  doub Y N 454 
TYR CD2 HD2  sing N N 455 
TYR CE1 CZ   doub Y N 456 
TYR CE1 HE1  sing N N 457 
TYR CE2 CZ   sing Y N 458 
TYR CE2 HE2  sing N N 459 
TYR CZ  OH   sing N N 460 
TYR OH  HH   sing N N 461 
TYR OXT HXT  sing N N 462 
VAL N   CA   sing N N 463 
VAL N   H    sing N N 464 
VAL N   H2   sing N N 465 
VAL CA  C    sing N N 466 
VAL CA  CB   sing N N 467 
VAL CA  HA   sing N N 468 
VAL C   O    doub N N 469 
VAL C   OXT  sing N N 470 
VAL CB  CG1  sing N N 471 
VAL CB  CG2  sing N N 472 
VAL CB  HB   sing N N 473 
VAL CG1 HG11 sing N N 474 
VAL CG1 HG12 sing N N 475 
VAL CG1 HG13 sing N N 476 
VAL CG2 HG21 sing N N 477 
VAL CG2 HG22 sing N N 478 
VAL CG2 HG23 sing N N 479 
VAL OXT HXT  sing N N 480 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-07 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8ZTH 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'AtALMT9 with LMNG (narrow 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  ? ? ? ?         ?       
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? cryoSPARC 4.4     
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? cryoSPARC 4.4     
CLASSIFICATION             ? 11 1 ? ? cryoSPARC 4.4     
RECONSTRUCTION             ? 12 1 ? ? cryoSPARC 4.4     
'MODEL REFINEMENT'         ? 13 ? 1 ? PHENIX    1.20.1  
# 
_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                    8ZTH 
_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 
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  ? 100.08600 88.06800  106.78200 1.000 91.20217  ? 77  ALA A N    1 
ATOM   2    C CA   . ALA A 1 77  ? 101.43700 88.48700  107.13600 1.000 90.43127  ? 77  ALA A CA   1 
ATOM   3    C C    . ALA A 1 77  ? 102.41600 87.32700  107.04600 1.000 90.93322  ? 77  ALA A C    1 
ATOM   4    O O    . ALA A 1 77  ? 103.60400 87.51900  106.76000 1.000 91.66595  ? 77  ALA A O    1 
ATOM   5    C CB   . ALA A 1 77  ? 101.44900 89.08200  108.53100 1.000 91.54883  ? 77  ALA A CB   1 
ATOM   6    N N    . TRP A 1 78  ? 101.89900 86.11300  107.25600 1.000 95.27411  ? 78  TRP A N    1 
ATOM   7    C CA   . TRP A 1 78  ? 102.74000 84.92900  107.14200 1.000 94.95008  ? 78  TRP A CA   1 
ATOM   8    C C    . TRP A 1 78  ? 103.41100 84.90500  105.77600 1.000 95.95357  ? 78  TRP A C    1 
ATOM   9    O O    . TRP A 1 78  ? 104.59200 84.54800  105.65600 1.000 95.01627  ? 78  TRP A O    1 
ATOM   10   C CB   . TRP A 1 78  ? 101.90000 83.66800  107.40700 1.000 95.26071  ? 78  TRP A CB   1 
ATOM   11   C CG   . TRP A 1 78  ? 102.45400 82.33600  106.92300 1.000 96.39016  ? 78  TRP A CG   1 
ATOM   12   C CD1  . TRP A 1 78  ? 102.55400 81.89200  105.63300 1.000 95.95499  ? 78  TRP A CD1  1 
ATOM   13   C CD2  . TRP A 1 78  ? 102.97300 81.28000  107.74800 1.000 96.41845  ? 78  TRP A CD2  1 
ATOM   14   N NE1  . TRP A 1 78  ? 103.10400 80.63100  105.60800 1.000 95.47126  ? 78  TRP A NE1  1 
ATOM   15   C CE2  . TRP A 1 78  ? 103.37100 80.23400  106.89200 1.000 96.15895  ? 78  TRP A CE2  1 
ATOM   16   C CE3  . TRP A 1 78  ? 103.14100 81.12100  109.12800 1.000 96.00493  ? 78  TRP A CE3  1 
ATOM   17   C CZ2  . TRP A 1 78  ? 103.92700 79.04600  107.37100 1.000 96.09333  ? 78  TRP A CZ2  1 
ATOM   18   C CZ3  . TRP A 1 78  ? 103.69400 79.94200  109.60000 1.000 96.84773  ? 78  TRP A CZ3  1 
ATOM   19   C CH2  . TRP A 1 78  ? 104.08000 78.92100  108.72400 1.000 96.67852  ? 78  TRP A CH2  1 
ATOM   20   N N    . GLU A 1 79  ? 102.66100 85.25100  104.72300 1.000 91.93559  ? 79  GLU A N    1 
ATOM   21   C CA   . GLU A 1 79  ? 103.25700 85.26600  103.39300 1.000 90.16097  ? 79  GLU A CA   1 
ATOM   22   C C    . GLU A 1 79  ? 104.41100 86.25900  103.31700 1.000 90.15802  ? 79  GLU A C    1 
ATOM   23   O O    . GLU A 1 79  ? 105.45900 85.94600  102.74100 1.000 90.45687  ? 79  GLU A O    1 
ATOM   24   C CB   . GLU A 1 79  ? 102.19000 85.59800  102.34800 1.000 88.94761  ? 79  GLU A CB   1 
ATOM   25   N N    . MET A 1 80  ? 104.23500 87.47700  103.85500 1.000 84.69637  ? 80  MET A N    1 
ATOM   26   C CA   . MET A 1 80  ? 105.36000 88.41200  103.84400 1.000 84.35957  ? 80  MET A CA   1 
ATOM   27   C C    . MET A 1 80  ? 106.54400 87.84700  104.61100 1.000 84.04012  ? 80  MET A C    1 
ATOM   28   O O    . MET A 1 80  ? 107.69600 88.16600  104.30400 1.000 82.45286  ? 80  MET A O    1 
ATOM   29   C CB   . MET A 1 80  ? 104.98400 89.77500  104.42600 1.000 83.81750  ? 80  MET A CB   1 
ATOM   30   C CG   . MET A 1 80  ? 105.85200 90.90500  103.85900 1.000 84.00961  ? 80  MET A CG   1 
ATOM   31   S SD   . MET A 1 80  ? 105.54700 92.54800  104.53000 1.000 86.56079  ? 80  MET A SD   1 
ATOM   32   C CE   . MET A 1 80  ? 106.39000 92.42900  106.10500 1.000 83.11563  ? 80  MET A CE   1 
ATOM   33   N N    . GLY A 1 81  ? 106.27200 87.01200  105.61300 1.000 80.13761  ? 81  GLY A N    1 
ATOM   34   C CA   . GLY A 1 81  ? 107.35200 86.38800  106.35200 1.000 78.92209  ? 81  GLY A CA   1 
ATOM   35   C C    . GLY A 1 81  ? 108.11300 85.39100  105.50300 1.000 79.90054  ? 81  GLY A C    1 
ATOM   36   O O    . GLY A 1 81  ? 109.34400 85.30900  105.56600 1.000 80.63285  ? 81  GLY A O    1 
ATOM   37   N N    . VAL A 1 82  ? 107.38700 84.62500  104.69100 1.000 83.38587  ? 82  VAL A N    1 
ATOM   38   C CA   . VAL A 1 82  ? 108.03500 83.63900  103.83300 1.000 83.70673  ? 82  VAL A CA   1 
ATOM   39   C C    . VAL A 1 82  ? 108.76100 84.30100  102.66800 1.000 81.80022  ? 82  VAL A C    1 
ATOM   40   O O    . VAL A 1 82  ? 109.80900 83.81400  102.22700 1.000 82.16829  ? 82  VAL A O    1 
ATOM   41   C CB   . VAL A 1 82  ? 107.01500 82.60400  103.32300 1.000 84.38443  ? 82  VAL A CB   1 
ATOM   42   C CG1  . VAL A 1 82  ? 107.67700 81.66000  102.33700 1.000 83.72580  ? 82  VAL A CG1  1 
ATOM   43   C CG2  . VAL A 1 82  ? 106.40800 81.82700  104.47500 1.000 82.72315  ? 82  VAL A CG2  1 
ATOM   44   N N    . SER A 1 83  ? 108.23300 85.41000  102.14800 1.000 80.33703  ? 83  SER A N    1 
ATOM   45   C CA   . SER A 1 83  ? 108.91400 86.10300  101.05600 1.000 81.88277  ? 83  SER A CA   1 
ATOM   46   C C    . SER A 1 83  ? 110.22200 86.74300  101.51000 1.000 83.76414  ? 83  SER A C    1 
ATOM   47   O O    . SER A 1 83  ? 111.19600 86.77700  100.74900 1.000 82.99264  ? 83  SER A O    1 
ATOM   48   C CB   . SER A 1 83  ? 107.99000 87.15800  100.45000 1.000 81.49196  ? 83  SER A CB   1 
ATOM   49   O OG   . SER A 1 83  ? 107.78600 88.23300  101.34900 1.000 83.65084  ? 83  SER A OG   1 
ATOM   50   N N    . ASP A 1 84  ? 110.26800 87.26400  102.73500 1.000 74.96742  ? 84  ASP A N    1 
ATOM   51   C CA   . ASP A 1 84  ? 111.48200 87.88100  103.27000 1.000 70.01263  ? 84  ASP A CA   1 
ATOM   52   C C    . ASP A 1 84  ? 111.68500 87.46000  104.71700 1.000 69.18860  ? 84  ASP A C    1 
ATOM   53   O O    . ASP A 1 84  ? 111.17300 88.10200  105.64200 1.000 70.92919  ? 84  ASP A O    1 
ATOM   54   C CB   . ASP A 1 84  ? 111.42100 89.40500  103.15500 1.000 69.93019  ? 84  ASP A CB   1 
ATOM   55   C CG   . ASP A 1 84  ? 112.75200 90.01500  102.76200 1.000 76.54640  ? 84  ASP A CG   1 
ATOM   56   O OD1  . ASP A 1 84  ? 113.73700 89.26000  102.61500 1.000 74.31234  ? 84  ASP A OD1  1 
ATOM   57   O OD2  . ASP A 1 84  ? 112.81400 91.25300  102.60200 1.000 75.90010  ? 84  ASP A OD2  1 
ATOM   58   N N    . PRO A 1 85  ? 112.42700 86.37400  104.95600 1.000 60.74950  ? 85  PRO A N    1 
ATOM   59   C CA   . PRO A 1 85  ? 112.70200 85.97900  106.34500 1.000 59.83291  ? 85  PRO A CA   1 
ATOM   60   C C    . PRO A 1 85  ? 113.62000 86.94500  107.07000 1.000 58.79070  ? 85  PRO A C    1 
ATOM   61   O O    . PRO A 1 85  ? 113.94600 86.70800  108.23900 1.000 58.32544  ? 85  PRO A O    1 
ATOM   62   C CB   . PRO A 1 85  ? 113.37800 84.61100  106.19600 1.000 60.64945  ? 85  PRO A CB   1 
ATOM   63   C CG   . PRO A 1 85  ? 112.93300 84.08500  104.88900 1.000 61.43941  ? 85  PRO A CG   1 
ATOM   64   C CD   . PRO A 1 85  ? 112.55400 85.24900  104.01400 1.000 61.98592  ? 85  PRO A CD   1 
ATOM   65   N N    . ARG A 1 86  ? 114.04200 88.02600  106.40900 1.000 54.01913  ? 86  ARG A N    1 
ATOM   66   C CA   . ARG A 1 86  ? 114.87200 89.04000  107.04000 1.000 51.96599  ? 86  ARG A CA   1 
ATOM   67   C C    . ARG A 1 86  ? 114.07000 89.90300  108.00000 1.000 54.38224  ? 86  ARG A C    1 
ATOM   68   O O    . ARG A 1 86  ? 114.64800 90.51200  108.90600 1.000 57.64473  ? 86  ARG A O    1 
ATOM   69   C CB   . ARG A 1 86  ? 115.52200 89.91600  105.96800 1.000 50.74478  ? 86  ARG A CB   1 
ATOM   70   C CG   . ARG A 1 86  ? 116.96000 89.55400  105.65000 1.000 54.60728  ? 86  ARG A CG   1 
ATOM   71   C CD   . ARG A 1 86  ? 117.42400 90.22600  104.37000 1.000 55.06201  ? 86  ARG A CD   1 
ATOM   72   N NE   . ARG A 1 86  ? 116.84500 91.55300  104.20200 1.000 55.50303  ? 86  ARG A NE   1 
ATOM   73   C CZ   . ARG A 1 86  ? 117.51100 92.61100  103.76100 1.000 56.01528  ? 86  ARG A CZ   1 
ATOM   74   N NH1  . ARG A 1 86  ? 118.79000 92.53400  103.43000 1.000 55.11799  ? 86  ARG A NH1  1 
ATOM   75   N NH2  . ARG A 1 86  ? 116.87900 93.77500  103.64700 1.000 53.68852  ? 86  ARG A NH2  1 
ATOM   76   N N    . LYS A 1 87  ? 112.75300 89.96500  107.81300 1.000 46.52698  ? 87  LYS A N    1 
ATOM   77   C CA   . LYS A 1 87  ? 111.86100 90.75700  108.64400 1.000 41.69648  ? 87  LYS A CA   1 
ATOM   78   C C    . LYS A 1 87  ? 111.38200 90.01500  109.88200 1.000 39.33035  ? 87  LYS A C    1 
ATOM   79   O O    . LYS A 1 87  ? 110.79000 90.63900  110.76700 1.000 48.00219  ? 87  LYS A O    1 
ATOM   80   C CB   . LYS A 1 87  ? 110.65300 91.20300  107.81700 1.000 43.12966  ? 87  LYS A CB   1 
ATOM   81   C CG   . LYS A 1 87  ? 110.92100 92.41900  106.95400 1.000 46.87407  ? 87  LYS A CG   1 
ATOM   82   C CD   . LYS A 1 87  ? 109.83500 92.59800  105.91000 1.000 48.40489  ? 87  LYS A CD   1 
ATOM   83   C CE   . LYS A 1 87  ? 109.50500 94.06100  105.69100 1.000 46.34493  ? 87  LYS A CE   1 
ATOM   84   N NZ   . LYS A 1 87  ? 108.48300 94.23000  104.62300 1.000 48.20566  ? 87  LYS A NZ   1 
ATOM   85   N N    . ILE A 1 88  ? 111.61500 88.70200  109.96300 1.000 37.17167  ? 88  ILE A N    1 
ATOM   86   C CA   . ILE A 1 88  ? 111.22300 87.93500  111.14100 1.000 37.57826  ? 88  ILE A CA   1 
ATOM   87   C C    . ILE A 1 88  ? 112.33600 87.84500  112.17300 1.000 40.80313  ? 88  ILE A C    1 
ATOM   88   O O    . ILE A 1 88  ? 112.07000 87.47200  113.32500 1.000 48.80992  ? 88  ILE A O    1 
ATOM   89   C CB   . ILE A 1 88  ? 110.77100 86.51400  110.74800 1.000 40.99768  ? 88  ILE A CB   1 
ATOM   90   C CG1  . ILE A 1 88  ? 109.80500 86.56800  109.56500 1.000 41.07073  ? 88  ILE A CG1  1 
ATOM   91   C CG2  . ILE A 1 88  ? 110.12200 85.81200  111.92700 1.000 42.11824  ? 88  ILE A CG2  1 
ATOM   92   C CD1  . ILE A 1 88  ? 109.34300 85.20800  109.09900 1.000 43.43323  ? 88  ILE A CD1  1 
ATOM   93   N N    . VAL A 1 89  ? 113.57100 88.17600  111.80400 1.000 37.37953  ? 89  VAL A N    1 
ATOM   94   C CA   . VAL A 1 89  ? 114.66100 88.18400  112.77100 1.000 34.18052  ? 89  VAL A CA   1 
ATOM   95   C C    . VAL A 1 89  ? 114.80700 89.55000  113.43700 1.000 35.97843  ? 89  VAL A C    1 
ATOM   96   O O    . VAL A 1 89  ? 115.20300 89.62900  114.60300 1.000 41.09627  ? 89  VAL A O    1 
ATOM   97   C CB   . VAL A 1 89  ? 115.97400 87.75300  112.09600 1.000 36.16506  ? 89  VAL A CB   1 
ATOM   98   C CG1  . VAL A 1 89  ? 117.10600 87.70700  113.10900 1.000 38.09561  ? 89  VAL A CG1  1 
ATOM   99   C CG2  . VAL A 1 89  ? 115.80500 86.40000  111.42400 1.000 31.12601  ? 89  VAL A CG2  1 
ATOM   100  N N    . PHE A 1 90  ? 114.45800 90.62700  112.73000 1.000 23.72529  ? 90  PHE A N    1 
ATOM   101  C CA   . PHE A 1 90  ? 114.50100 91.95900  113.32600 1.000 26.80118  ? 90  PHE A CA   1 
ATOM   102  C C    . PHE A 1 90  ? 113.52500 92.06800  114.49300 1.000 28.09570  ? 90  PHE A C    1 
ATOM   103  O O    . PHE A 1 90  ? 113.85800 92.62200  115.55300 1.000 30.66248  ? 90  PHE A O    1 
ATOM   104  C CB   . PHE A 1 90  ? 114.18500 92.99700  112.24600 1.000 21.89107  ? 90  PHE A CB   1 
ATOM   105  C CG   . PHE A 1 90  ? 114.47800 94.41300  112.64600 1.000 24.47621  ? 90  PHE A CG   1 
ATOM   106  C CD1  . PHE A 1 90  ? 115.76500 94.80500  112.96100 1.000 23.77623  ? 90  PHE A CD1  1 
ATOM   107  C CD2  . PHE A 1 90  ? 113.46800 95.35600  112.68600 1.000 22.91058  ? 90  PHE A CD2  1 
ATOM   108  C CE1  . PHE A 1 90  ? 116.03500 96.10800  113.32200 1.000 25.15539  ? 90  PHE A CE1  1 
ATOM   109  C CE2  . PHE A 1 90  ? 113.73300 96.65900  113.04700 1.000 22.57284  ? 90  PHE A CE2  1 
ATOM   110  C CZ   . PHE A 1 90  ? 115.01700 97.03500  113.36500 1.000 21.15583  ? 90  PHE A CZ   1 
ATOM   111  N N    . SER A 1 91  ? 112.32300 91.51100  114.32800 1.000 21.78569  ? 91  SER A N    1 
ATOM   112  C CA   . SER A 1 91  ? 111.31000 91.58800  115.37400 1.000 20.12513  ? 91  SER A CA   1 
ATOM   113  C C    . SER A 1 91  ? 111.71600 90.77200  116.59300 1.000 21.85487  ? 91  SER A C    1 
ATOM   114  O O    . SER A 1 91  ? 111.53600 91.21400  117.73700 1.000 28.22252  ? 91  SER A O    1 
ATOM   115  C CB   . SER A 1 91  ? 109.97100 91.10500  114.82200 1.000 20.58229  ? 91  SER A CB   1 
ATOM   116  O OG   . SER A 1 91  ? 109.63300 91.80500  113.63800 1.000 18.48470  ? 91  SER A OG   1 
ATOM   117  N N    . ALA A 1 92  ? 112.32000 89.60400  116.37000 1.000 18.78383  ? 92  ALA A N    1 
ATOM   118  C CA   . ALA A 1 92  ? 112.74500 88.78100  117.49300 1.000 16.48728  ? 92  ALA A CA   1 
ATOM   119  C C    . ALA A 1 92  ? 113.97100 89.36600  118.17400 1.000 20.44069  ? 92  ALA A C    1 
ATOM   120  O O    . ALA A 1 92  ? 114.14300 89.19700  119.38400 1.000 32.44897  ? 92  ALA A O    1 
ATOM   121  C CB   . ALA A 1 92  ? 113.02300 87.35400  117.02200 1.000 13.19552  ? 92  ALA A CB   1 
ATOM   122  N N    . LYS A 1 93  ? 114.78700 90.12500  117.44000 1.000 16.05989  ? 93  LYS A N    1 
ATOM   123  C CA   . LYS A 1 93  ? 115.93800 90.76400  118.06500 1.000 19.53094  ? 93  LYS A CA   1 
ATOM   124  C C    . LYS A 1 93  ? 115.50200 91.94000  118.92900 1.000 20.52432  ? 93  LYS A C    1 
ATOM   125  O O    . LYS A 1 93  ? 116.04000 92.14900  120.02600 1.000 30.66158  ? 93  LYS A O    1 
ATOM   126  C CB   . LYS A 1 93  ? 116.92500 91.21400  116.99000 1.000 26.16103  ? 93  LYS A CB   1 
ATOM   127  C CG   . LYS A 1 93  ? 117.78800 90.09300  116.44100 1.000 24.22171  ? 93  LYS A CG   1 
ATOM   128  C CD   . LYS A 1 93  ? 119.11400 90.61400  115.92200 1.000 23.85743  ? 93  LYS A CD   1 
ATOM   129  C CE   . LYS A 1 93  ? 118.97000 91.19800  114.53200 1.000 19.11850  ? 93  LYS A CE   1 
ATOM   130  N NZ   . LYS A 1 93  ? 120.18900 91.93500  114.11400 1.000 23.88758  ? 93  LYS A NZ   1 
ATOM   131  N N    . ILE A 1 94  ? 114.49400 92.68800  118.47900 1.000 15.65319  ? 94  ILE A N    1 
ATOM   132  C CA   . ILE A 1 94  ? 113.95400 93.75100  119.32300 1.000 14.80925  ? 94  ILE A CA   1 
ATOM   133  C C    . ILE A 1 94  ? 113.28500 93.16400  120.56200 1.000 24.98312  ? 94  ILE A C    1 
ATOM   134  O O    . ILE A 1 94  ? 113.45800 93.67500  121.68000 1.000 30.76820  ? 94  ILE A O    1 
ATOM   135  C CB   . ILE A 1 94  ? 112.99000 94.64100  118.51900 1.000 19.49158  ? 94  ILE A CB   1 
ATOM   136  C CG1  . ILE A 1 94  ? 113.75800 95.43200  117.46100 1.000 18.88830  ? 94  ILE A CG1  1 
ATOM   137  C CG2  . ILE A 1 94  ? 112.22800 95.57600  119.44100 1.000 21.99045  ? 94  ILE A CG2  1 
ATOM   138  C CD1  . ILE A 1 94  ? 112.87700 96.14500  116.47800 1.000 24.68762  ? 94  ILE A CD1  1 
ATOM   139  N N    . GLY A 1 95  ? 112.53600 92.07000  120.39800 1.000 11.95597  ? 95  GLY A N    1 
ATOM   140  C CA   . GLY A 1 95  ? 111.93600 91.43100  121.55700 1.000 3.99899   ? 95  GLY A CA   1 
ATOM   141  C C    . GLY A 1 95  ? 112.97000 90.92200  122.54400 1.000 14.63641  ? 95  GLY A C    1 
ATOM   142  O O    . GLY A 1 95  ? 112.79600 91.04400  123.76100 1.000 23.52513  ? 95  GLY A O    1 
ATOM   143  N N    . LEU A 1 96  ? 114.08100 90.38200  122.03500 1.000 19.92895  ? 96  LEU A N    1 
ATOM   144  C CA   . LEU A 1 96  ? 115.12300 89.86500  122.91500 1.000 17.26238  ? 96  LEU A CA   1 
ATOM   145  C C    . LEU A 1 96  ? 115.83200 90.98900  123.66200 1.000 18.06751  ? 96  LEU A C    1 
ATOM   146  O O    . LEU A 1 96  ? 116.13200 90.85600  124.85500 1.000 25.67788  ? 96  LEU A O    1 
ATOM   147  C CB   . LEU A 1 96  ? 116.12000 89.03800  122.10400 1.000 16.54374  ? 96  LEU A CB   1 
ATOM   148  C CG   . LEU A 1 96  ? 117.42700 88.62300  122.77900 1.000 21.63766  ? 96  LEU A CG   1 
ATOM   149  C CD1  . LEU A 1 96  ? 117.19100 87.51900  123.79500 1.000 18.84497  ? 96  LEU A CD1  1 
ATOM   150  C CD2  . LEU A 1 96  ? 118.43600 88.18600  121.73500 1.000 15.56426  ? 96  LEU A CD2  1 
ATOM   151  N N    . ALA A 1 97  ? 116.09600 92.11200  122.98900 1.000 14.37421  ? 97  ALA A N    1 
ATOM   152  C CA   . ALA A 1 97  ? 116.72000 93.23300  123.68700 1.000 25.76616  ? 97  ALA A CA   1 
ATOM   153  C C    . ALA A 1 97  ? 115.79700 93.79200  124.76400 1.000 26.46302  ? 97  ALA A C    1 
ATOM   154  O O    . ALA A 1 97  ? 116.24500 94.12000  125.87500 1.000 26.15881  ? 97  ALA A O    1 
ATOM   155  C CB   . ALA A 1 97  ? 117.10900 94.32500  122.69200 1.000 12.03528  ? 97  ALA A CB   1 
ATOM   156  N N    . LEU A 1 98  ? 114.49700 93.87900  124.46600 1.000 16.90588  ? 98  LEU A N    1 
ATOM   157  C CA   . LEU A 1 98  ? 113.55800 94.38400  125.46000 1.000 15.57127  ? 98  LEU A CA   1 
ATOM   158  C C    . LEU A 1 98  ? 113.47000 93.44300  126.65700 1.000 16.32086  ? 98  LEU A C    1 
ATOM   159  O O    . LEU A 1 98  ? 113.40400 93.89200  127.80800 1.000 26.04669  ? 98  LEU A O    1 
ATOM   160  C CB   . LEU A 1 98  ? 112.18800 94.58400  124.81800 1.000 18.85047  ? 98  LEU A CB   1 
ATOM   161  C CG   . LEU A 1 98  ? 111.84200 96.02000  124.42100 1.000 19.51624  ? 98  LEU A CG   1 
ATOM   162  C CD1  . LEU A 1 98  ? 110.46100 96.08200  123.79300 1.000 19.07545  ? 98  LEU A CD1  1 
ATOM   163  C CD2  . LEU A 1 98  ? 111.94400 96.95400  125.61300 1.000 19.44434  ? 98  LEU A CD2  1 
ATOM   164  N N    . THR A 1 99  ? 113.51500 92.13100  126.40800 1.000 18.81611  ? 99  THR A N    1 
ATOM   165  C CA   . THR A 1 99  ? 113.47900 91.17500  127.51000 1.000 17.33999  ? 99  THR A CA   1 
ATOM   166  C C    . THR A 1 99  ? 114.75600 91.21800  128.34200 1.000 27.03797  ? 99  THR A C    1 
ATOM   167  O O    . THR A 1 99  ? 114.70200 91.04800  129.56600 1.000 25.07670  ? 99  THR A O    1 
ATOM   168  C CB   . THR A 1 99  ? 113.25100 89.76400  126.97200 1.000 18.57477  ? 99  THR A CB   1 
ATOM   169  O OG1  . THR A 1 99  ? 111.98400 89.70600  126.30600 1.000 23.90392  ? 99  THR A OG1  1 
ATOM   170  C CG2  . THR A 1 99  ? 113.27000 88.75300  128.10200 1.000 25.42341  ? 99  THR A CG2  1 
ATOM   171  N N    . ILE A 1 100 ? 115.90600 91.47200  127.71300 1.000 28.65568  ? 100 ILE A N    1 
ATOM   172  C CA   . ILE A 1 100 ? 117.14400 91.56700  128.48000 1.000 22.03132  ? 100 ILE A CA   1 
ATOM   173  C C    . ILE A 1 100 ? 117.12600 92.80400  129.36900 1.000 29.21545  ? 100 ILE A C    1 
ATOM   174  O O    . ILE A 1 100 ? 117.55500 92.75900  130.53000 1.000 38.48319  ? 100 ILE A O    1 
ATOM   175  C CB   . ILE A 1 100 ? 118.36500 91.56100  127.54300 1.000 24.86500  ? 100 ILE A CB   1 
ATOM   176  C CG1  . ILE A 1 100 ? 118.55000 90.18100  126.91400 1.000 27.14413  ? 100 ILE A CG1  1 
ATOM   177  C CG2  . ILE A 1 100 ? 119.61700 91.97200  128.29700 1.000 29.97737  ? 100 ILE A CG2  1 
ATOM   178  C CD1  . ILE A 1 100 ? 119.56300 90.15600  125.79800 1.000 25.49557  ? 100 ILE A CD1  1 
ATOM   179  N N    . VAL A 1 101 ? 116.61000 93.92200  128.85300 1.000 29.76120  ? 101 VAL A N    1 
ATOM   180  C CA   . VAL A 1 101 ? 116.51100 95.12000  129.68500 1.000 24.99190  ? 101 VAL A CA   1 
ATOM   181  C C    . VAL A 1 101 ? 115.54900 94.88200  130.84400 1.000 23.86714  ? 101 VAL A C    1 
ATOM   182  O O    . VAL A 1 101 ? 115.82000 95.26800  131.99200 1.000 30.66680  ? 101 VAL A O    1 
ATOM   183  C CB   . VAL A 1 101 ? 116.08900 96.33300  128.83600 1.000 28.72647  ? 101 VAL A CB   1 
ATOM   184  C CG1  . VAL A 1 101 ? 115.84100 97.53700  129.72300 1.000 27.87398  ? 101 VAL A CG1  1 
ATOM   185  C CG2  . VAL A 1 101 ? 117.15700 96.65200  127.80800 1.000 27.12805  ? 101 VAL A CG2  1 
ATOM   186  N N    . ALA A 1 102 ? 114.41500 94.23400  130.56500 1.000 33.55854  ? 102 ALA A N    1 
ATOM   187  C CA   . ALA A 1 102 ? 113.46300 93.91900  131.62500 1.000 31.98370  ? 102 ALA A CA   1 
ATOM   188  C C    . ALA A 1 102 ? 114.10400 93.06300  132.71100 1.000 36.17855  ? 102 ALA A C    1 
ATOM   189  O O    . ALA A 1 102 ? 113.91500 93.31700  133.90400 1.000 35.81445  ? 102 ALA A O    1 
ATOM   190  C CB   . ALA A 1 102 ? 112.23700 93.22000  131.03900 1.000 27.09932  ? 102 ALA A CB   1 
ATOM   191  N N    . LEU A 1 103 ? 114.85500 92.02800  132.31800 1.000 39.66946  ? 103 LEU A N    1 
ATOM   192  C CA   . LEU A 1 103 ? 115.48100 91.16400  133.31700 1.000 31.91273  ? 103 LEU A CA   1 
ATOM   193  C C    . LEU A 1 103 ? 116.53400 91.91200  134.12600 1.000 38.39019  ? 103 LEU A C    1 
ATOM   194  O O    . LEU A 1 103 ? 116.63100 91.72800  135.34700 1.000 45.22425  ? 103 LEU A O    1 
ATOM   195  C CB   . LEU A 1 103 ? 116.10100 89.93700  132.65200 1.000 32.90045  ? 103 LEU A CB   1 
ATOM   196  C CG   . LEU A 1 103 ? 115.15400 88.84800  132.15100 1.000 38.62038  ? 103 LEU A CG   1 
ATOM   197  C CD1  . LEU A 1 103 ? 115.77800 88.09300  130.99200 1.000 37.32380  ? 103 LEU A CD1  1 
ATOM   198  C CD2  . LEU A 1 103 ? 114.79900 87.89900  133.28100 1.000 35.86989  ? 103 LEU A CD2  1 
ATOM   199  N N    . LEU A 1 104 ? 117.31500 92.77900  133.47500 1.000 39.40458  ? 104 LEU A N    1 
ATOM   200  C CA   . LEU A 1 104 ? 118.32300 93.53200  134.21600 1.000 36.39347  ? 104 LEU A CA   1 
ATOM   201  C C    . LEU A 1 104 ? 117.67700 94.45400  135.23900 1.000 41.10730  ? 104 LEU A C    1 
ATOM   202  O O    . LEU A 1 104 ? 118.19500 94.62000  136.34800 1.000 45.11015  ? 104 LEU A O    1 
ATOM   203  C CB   . LEU A 1 104 ? 119.20900 94.33200  133.26200 1.000 38.00919  ? 104 LEU A CB   1 
ATOM   204  C CG   . LEU A 1 104 ? 120.20600 93.53200  132.42800 1.000 43.74206  ? 104 LEU A CG   1 
ATOM   205  C CD1  . LEU A 1 104 ? 120.99500 94.45500  131.51800 1.000 38.84177  ? 104 LEU A CD1  1 
ATOM   206  C CD2  . LEU A 1 104 ? 121.13700 92.75200  133.33900 1.000 43.32999  ? 104 LEU A CD2  1 
ATOM   207  N N    . ILE A 1 105 ? 116.54400 95.06400  134.88900 1.000 47.17401  ? 105 ILE A N    1 
ATOM   208  C CA   . ILE A 1 105 ? 115.88700 95.95100  135.84500 1.000 43.39087  ? 105 ILE A CA   1 
ATOM   209  C C    . ILE A 1 105 ? 115.22600 95.14700  136.96100 1.000 49.04592  ? 105 ILE A C    1 
ATOM   210  O O    . ILE A 1 105 ? 115.28400 95.52800  138.13600 1.000 52.63839  ? 105 ILE A O    1 
ATOM   211  C CB   . ILE A 1 105 ? 114.87800 96.86700  135.13100 1.000 42.23570  ? 105 ILE A CB   1 
ATOM   212  C CG1  . ILE A 1 105 ? 115.59700 97.78300  134.14100 1.000 42.58888  ? 105 ILE A CG1  1 
ATOM   213  C CG2  . ILE A 1 105 ? 114.09500 97.68400  136.14300 1.000 42.02413  ? 105 ILE A CG2  1 
ATOM   214  C CD1  . ILE A 1 105 ? 114.68900 98.37200  133.08900 1.000 43.03600  ? 105 ILE A CD1  1 
ATOM   215  N N    . PHE A 1 106 ? 114.58500 94.02700  136.61600 1.000 49.58049  ? 106 PHE A N    1 
ATOM   216  C CA   . PHE A 1 106 ? 113.88400 93.22400  137.61500 1.000 44.21171  ? 106 PHE A CA   1 
ATOM   217  C C    . PHE A 1 106 ? 114.83300 92.60800  138.63700 1.000 50.56681  ? 106 PHE A C    1 
ATOM   218  O O    . PHE A 1 106 ? 114.50100 92.53500  139.82500 1.000 54.20365  ? 106 PHE A O    1 
ATOM   219  C CB   . PHE A 1 106 ? 113.07800 92.11900  136.93200 1.000 45.89088  ? 106 PHE A CB   1 
ATOM   220  C CG   . PHE A 1 106 ? 111.71700 92.55000  136.47100 1.000 52.17335  ? 106 PHE A CG   1 
ATOM   221  C CD1  . PHE A 1 106 ? 111.18800 93.76800  136.86100 1.000 51.26665  ? 106 PHE A CD1  1 
ATOM   222  C CD2  . PHE A 1 106 ? 110.96300 91.73000  135.64900 1.000 47.68107  ? 106 PHE A CD2  1 
ATOM   223  C CE1  . PHE A 1 106 ? 109.93600 94.16000  136.43800 1.000 47.75869  ? 106 PHE A CE1  1 
ATOM   224  C CE2  . PHE A 1 106 ? 109.71200 92.11900  135.22200 1.000 48.12163  ? 106 PHE A CE2  1 
ATOM   225  C CZ   . PHE A 1 106 ? 109.19700 93.33500  135.61700 1.000 50.24627  ? 106 PHE A CZ   1 
ATOM   226  N N    . TYR A 1 107 ? 116.01600 92.15700  138.20700 1.000 61.47989  ? 107 TYR A N    1 
ATOM   227  C CA   . TYR A 1 107 ? 116.84300 91.32900  139.07700 1.000 62.35257  ? 107 TYR A CA   1 
ATOM   228  C C    . TYR A 1 107 ? 118.09700 91.99900  139.61900 1.000 64.27723  ? 107 TYR A C    1 
ATOM   229  O O    . TYR A 1 107 ? 118.67100 91.48900  140.58500 1.000 66.37540  ? 107 TYR A O    1 
ATOM   230  C CB   . TYR A 1 107 ? 117.26300 90.04400  138.34600 1.000 63.68803  ? 107 TYR A CB   1 
ATOM   231  C CG   . TYR A 1 107 ? 116.15200 89.03000  138.19800 1.000 65.24729  ? 107 TYR A CG   1 
ATOM   232  C CD1  . TYR A 1 107 ? 115.29100 89.06800  137.11100 1.000 63.66941  ? 107 TYR A CD1  1 
ATOM   233  C CD2  . TYR A 1 107 ? 115.96500 88.03400  139.14700 1.000 64.56322  ? 107 TYR A CD2  1 
ATOM   234  C CE1  . TYR A 1 107 ? 114.27500 88.14200  136.97100 1.000 63.23473  ? 107 TYR A CE1  1 
ATOM   235  C CE2  . TYR A 1 107 ? 114.95100 87.10500  139.01700 1.000 65.10487  ? 107 TYR A CE2  1 
ATOM   236  C CZ   . TYR A 1 107 ? 114.11000 87.16300  137.92700 1.000 66.04695  ? 107 TYR A CZ   1 
ATOM   237  O OH   . TYR A 1 107 ? 113.09900 86.24100  137.79100 1.000 67.16781  ? 107 TYR A OH   1 
ATOM   238  N N    . GLN A 1 108 ? 118.54000 93.11500  139.04300 1.000 72.57254  ? 108 GLN A N    1 
ATOM   239  C CA   . GLN A 1 108 ? 119.79600 93.73000  139.45300 1.000 73.64212  ? 108 GLN A CA   1 
ATOM   240  C C    . GLN A 1 108 ? 119.58900 95.01000  140.25500 1.000 72.58687  ? 108 GLN A C    1 
ATOM   241  O O    . GLN A 1 108 ? 120.50500 95.83300  140.34900 1.000 71.66470  ? 108 GLN A O    1 
ATOM   242  C CB   . GLN A 1 108 ? 120.67500 94.00100  138.23200 1.000 75.49907  ? 108 GLN A CB   1 
ATOM   243  C CG   . GLN A 1 108 ? 120.88100 92.78200  137.34900 1.000 74.05111  ? 108 GLN A CG   1 
ATOM   244  C CD   . GLN A 1 108 ? 121.43800 91.59700  138.11600 1.000 74.38811  ? 108 GLN A CD   1 
ATOM   245  O OE1  . GLN A 1 108 ? 120.69000 90.73300  138.57300 1.000 74.18730  ? 108 GLN A OE1  1 
ATOM   246  N NE2  . GLN A 1 108 ? 122.75700 91.55000  138.25600 1.000 74.62008  ? 108 GLN A NE2  1 
ATOM   247  N N    . GLU A 1 109 ? 118.40300 95.19600  140.83700 1.000 82.45340  ? 109 GLU A N    1 
ATOM   248  C CA   . GLU A 1 109 ? 118.16400 96.35800  141.67100 1.000 87.19874  ? 109 GLU A CA   1 
ATOM   249  C C    . GLU A 1 109 ? 117.17700 96.04100  142.78600 1.000 87.57379  ? 109 GLU A C    1 
ATOM   250  O O    . GLU A 1 109 ? 116.11400 95.46300  142.51100 1.000 86.64424  ? 109 GLU A O    1 
ATOM   251  C CB   . GLU A 1 109 ? 117.64800 97.53900  140.84900 1.000 86.01570  ? 109 GLU A CB   1 
ATOM   252  C CG   . GLU A 1 109 ? 118.59600 98.72400  140.81900 1.000 86.81304  ? 109 GLU A CG   1 
ATOM   253  C CD   . GLU A 1 109 ? 118.59000 99.50700  142.12000 1.000 88.12023  ? 109 GLU A CD   1 
ATOM   254  O OE1  . GLU A 1 109 ? 117.69700 99.26300  142.95900 1.000 84.29745  ? 109 GLU A OE1  1 
ATOM   255  O OE2  . GLU A 1 109 ? 119.47700 100.36600 142.30400 1.000 87.71280  ? 109 GLU A OE2  1 
ATOM   256  N N    . PRO A 1 110 ? 117.49600 96.39400  144.03100 1.000 92.58058  ? 110 PRO A N    1 
ATOM   257  C CA   . PRO A 1 110 ? 116.53200 96.25300  145.13600 1.000 92.84119  ? 110 PRO A CA   1 
ATOM   258  C C    . PRO A 1 110 ? 115.82500 97.54800  145.51900 1.000 92.35882  ? 110 PRO A C    1 
ATOM   259  O O    . PRO A 1 110 ? 115.19200 97.58000  146.57900 1.000 91.35258  ? 110 PRO A O    1 
ATOM   260  C CB   . PRO A 1 110 ? 117.43300 95.78000  146.28100 1.000 91.05093  ? 110 PRO A CB   1 
ATOM   261  C CG   . PRO A 1 110 ? 118.76900 96.43500  146.00000 1.000 90.85385  ? 110 PRO A CG   1 
ATOM   262  C CD   . PRO A 1 110 ? 118.83500 96.76200  144.52000 1.000 90.72569  ? 110 PRO A CD   1 
ATOM   263  N N    . ASN A 1 111 ? 115.91700 98.59000  144.69700 1.000 90.73097  ? 111 ASN A N    1 
ATOM   264  C CA   . ASN A 1 111 ? 115.31600 99.88600  144.96000 1.000 90.76564  ? 111 ASN A CA   1 
ATOM   265  C C    . ASN A 1 111 ? 114.48200 100.31800 143.76400 1.000 91.09040  ? 111 ASN A C    1 
ATOM   266  O O    . ASN A 1 111 ? 114.82400 100.01400 142.61700 1.000 90.44076  ? 111 ASN A O    1 
ATOM   267  C CB   . ASN A 1 111 ? 116.38800 100.94600 145.24800 1.000 91.84281  ? 111 ASN A CB   1 
ATOM   268  C CG   . ASN A 1 111 ? 115.79600 102.30500 145.56400 1.000 92.01155  ? 111 ASN A CG   1 
ATOM   269  O OD1  . ASN A 1 111 ? 115.49400 103.08800 144.66300 1.000 89.96625  ? 111 ASN A OD1  1 
ATOM   270  N ND2  . ASN A 1 111 ? 115.62600 102.59200 146.84900 1.000 92.03099  ? 111 ASN A ND2  1 
ATOM   271  N N    . PRO A 1 112 ? 113.38000 101.03400 144.00500 1.000 86.93087  ? 112 PRO A N    1 
ATOM   272  C CA   . PRO A 1 112 ? 112.48700 101.41100 142.89700 1.000 87.09347  ? 112 PRO A CA   1 
ATOM   273  C C    . PRO A 1 112 ? 113.04700 102.47900 141.97200 1.000 89.37374  ? 112 PRO A C    1 
ATOM   274  O O    . PRO A 1 112 ? 112.45000 102.71500 140.91300 1.000 89.52995  ? 112 PRO A O    1 
ATOM   275  C CB   . PRO A 1 112 ? 111.23200 101.92000 143.62000 1.000 86.57049  ? 112 PRO A CB   1 
ATOM   276  C CG   . PRO A 1 112 ? 111.72800 102.35400 144.96200 1.000 87.02694  ? 112 PRO A CG   1 
ATOM   277  C CD   . PRO A 1 112 ? 112.80200 101.37100 145.31600 1.000 86.84952  ? 112 PRO A CD   1 
ATOM   278  N N    . ASP A 1 113 ? 114.15500 103.13700 142.32300 1.000 84.14372  ? 113 ASP A N    1 
ATOM   279  C CA   . ASP A 1 113 ? 114.64000 104.23300 141.48900 1.000 82.87063  ? 113 ASP A CA   1 
ATOM   280  C C    . ASP A 1 113 ? 114.88700 103.77100 140.05800 1.000 82.67512  ? 113 ASP A C    1 
ATOM   281  O O    . ASP A 1 113 ? 114.37200 104.37000 139.10500 1.000 83.90914  ? 113 ASP A O    1 
ATOM   282  C CB   . ASP A 1 113 ? 115.91300 104.82700 142.09400 1.000 84.10765  ? 113 ASP A CB   1 
ATOM   283  C CG   . ASP A 1 113 ? 115.65200 106.11400 142.85100 1.000 85.03437  ? 113 ASP A CG   1 
ATOM   284  O OD1  . ASP A 1 113 ? 114.46800 106.47300 143.02400 1.000 82.56206  ? 113 ASP A OD1  1 
ATOM   285  O OD2  . ASP A 1 113 ? 116.62900 106.76600 143.27300 1.000 84.50009  ? 113 ASP A OD2  1 
ATOM   286  N N    . LEU A 1 114 ? 115.57500 102.63800 139.89000 1.000 76.68021  ? 114 LEU A N    1 
ATOM   287  C CA   . LEU A 1 114 ? 115.83300 102.15100 138.54100 1.000 76.45869  ? 114 LEU A CA   1 
ATOM   288  C C    . LEU A 1 114 ? 114.57000 101.63200 137.88300 1.000 76.98551  ? 114 LEU A C    1 
ATOM   289  O O    . LEU A 1 114 ? 114.56000 101.42000 136.66600 1.000 79.53008  ? 114 LEU A O    1 
ATOM   290  C CB   . LEU A 1 114 ? 116.90400 101.06000 138.54800 1.000 76.92483  ? 114 LEU A CB   1 
ATOM   291  C CG   . LEU A 1 114 ? 118.33200 101.54800 138.29600 1.000 77.87740  ? 114 LEU A CG   1 
ATOM   292  C CD1  . LEU A 1 114 ? 118.74900 102.57200 139.34000 1.000 78.73699  ? 114 LEU A CD1  1 
ATOM   293  C CD2  . LEU A 1 114 ? 119.30900 100.38400 138.24900 1.000 77.73222  ? 114 LEU A CD2  1 
ATOM   294  N N    . SER A 1 115 ? 113.51400 101.42700 138.66300 1.000 68.90450  ? 115 SER A N    1 
ATOM   295  C CA   . SER A 1 115 ? 112.21900 101.04600 138.13000 1.000 68.29626  ? 115 SER A CA   1 
ATOM   296  C C    . SER A 1 115 ? 111.36500 102.27000 137.84800 1.000 68.38114  ? 115 SER A C    1 
ATOM   297  O O    . SER A 1 115 ? 110.47200 102.21200 136.99400 1.000 66.53361  ? 115 SER A O    1 
ATOM   298  C CB   . SER A 1 115 ? 111.49600 100.11100 139.10400 1.000 69.76630  ? 115 SER A CB   1 
ATOM   299  O OG   . SER A 1 115 ? 110.55500 100.81900 139.89000 1.000 72.62586  ? 115 SER A OG   1 
ATOM   300  N N    . ARG A 1 116 ? 111.62000 103.37800 138.54700 1.000 73.49704  ? 116 ARG A N    1 
ATOM   301  C CA   . ARG A 1 116 ? 110.83900 104.59000 138.34500 1.000 71.73315  ? 116 ARG A CA   1 
ATOM   302  C C    . ARG A 1 116 ? 111.36500 105.43700 137.19600 1.000 73.10961  ? 116 ARG A C    1 
ATOM   303  O O    . ARG A 1 116 ? 110.59700 106.19800 136.59500 1.000 75.47197  ? 116 ARG A O    1 
ATOM   304  C CB   . ARG A 1 116 ? 110.81000 105.41900 139.63200 1.000 74.21219  ? 116 ARG A CB   1 
ATOM   305  C CG   . ARG A 1 116 ? 110.14700 104.70600 140.80000 1.000 74.87555  ? 116 ARG A CG   1 
ATOM   306  C CD   . ARG A 1 116 ? 109.86900 105.64800 141.96000 1.000 76.70286  ? 116 ARG A CD   1 
ATOM   307  N NE   . ARG A 1 116 ? 110.75700 106.80500 141.96600 1.000 76.93945  ? 116 ARG A NE   1 
ATOM   308  C CZ   . ARG A 1 116 ? 111.58000 107.11100 142.96000 1.000 78.94949  ? 116 ARG A CZ   1 
ATOM   309  N NH1  . ARG A 1 116 ? 111.65700 106.36300 144.04800 1.000 78.46845  ? 116 ARG A NH1  1 
ATOM   310  N NH2  . ARG A 1 116 ? 112.34200 108.19600 142.86000 1.000 77.14633  ? 116 ARG A NH2  1 
ATOM   311  N N    . TYR A 1 117 ? 112.65500 105.32100 136.87600 1.000 61.34653  ? 117 TYR A N    1 
ATOM   312  C CA   . TYR A 1 117 ? 113.25800 105.99400 135.73300 1.000 56.98522  ? 117 TYR A CA   1 
ATOM   313  C C    . TYR A 1 117 ? 113.46600 105.04700 134.55700 1.000 60.51054  ? 117 TYR A C    1 
ATOM   314  O O    . TYR A 1 117 ? 114.34600 105.28000 133.72200 1.000 60.84907  ? 117 TYR A O    1 
ATOM   315  C CB   . TYR A 1 117 ? 114.59000 106.62900 136.13300 1.000 56.68932  ? 117 TYR A CB   1 
ATOM   316  C CG   . TYR A 1 117 ? 114.54700 107.43000 137.41300 1.000 61.58997  ? 117 TYR A CG   1 
ATOM   317  C CD1  . TYR A 1 117 ? 113.46200 108.23900 137.71600 1.000 61.79721  ? 117 TYR A CD1  1 
ATOM   318  C CD2  . TYR A 1 117 ? 115.60000 107.38200 138.31600 1.000 60.85880  ? 117 TYR A CD2  1 
ATOM   319  C CE1  . TYR A 1 117 ? 113.42400 108.97400 138.88700 1.000 62.35371  ? 117 TYR A CE1  1 
ATOM   320  C CE2  . TYR A 1 117 ? 115.57100 108.11200 139.48700 1.000 59.44404  ? 117 TYR A CE2  1 
ATOM   321  C CZ   . TYR A 1 117 ? 114.48200 108.90600 139.76800 1.000 62.43352  ? 117 TYR A CZ   1 
ATOM   322  O OH   . TYR A 1 117 ? 114.45000 109.63500 140.93300 1.000 61.41285  ? 117 TYR A OH   1 
ATOM   323  N N    . SER A 1 118 ? 112.67300 103.98200 134.47400 1.000 54.20048  ? 118 SER A N    1 
ATOM   324  C CA   . SER A 1 118 ? 112.86300 102.94200 133.47000 1.000 45.27830  ? 118 SER A CA   1 
ATOM   325  C C    . SER A 1 118 ? 112.27600 103.28500 132.10700 1.000 44.23383  ? 118 SER A C    1 
ATOM   326  O O    . SER A 1 118 ? 112.37900 102.46300 131.19100 1.000 48.36415  ? 118 SER A O    1 
ATOM   327  C CB   . SER A 1 118 ? 112.25600 101.62800 133.96600 1.000 46.05569  ? 118 SER A CB   1 
ATOM   328  O OG   . SER A 1 118 ? 110.86900 101.77400 134.21700 1.000 46.34341  ? 118 SER A OG   1 
ATOM   329  N N    . VAL A 1 119 ? 111.66500 104.45900 131.94100 1.000 31.16831  ? 119 VAL A N    1 
ATOM   330  C CA   . VAL A 1 119 ? 111.14800 104.83500 130.62900 1.000 28.73592  ? 119 VAL A CA   1 
ATOM   331  C C    . VAL A 1 119 ? 112.24900 105.30800 129.68700 1.000 32.16025  ? 119 VAL A C    1 
ATOM   332  O O    . VAL A 1 119 ? 112.06600 105.26900 128.46200 1.000 30.67946  ? 119 VAL A O    1 
ATOM   333  C CB   . VAL A 1 119 ? 110.05800 105.91100 130.76900 1.000 33.16875  ? 119 VAL A CB   1 
ATOM   334  C CG1  . VAL A 1 119 ? 110.66800 107.24600 131.15200 1.000 32.81496  ? 119 VAL A CG1  1 
ATOM   335  C CG2  . VAL A 1 119 ? 109.26400 106.03300 129.47900 1.000 36.57330  ? 119 VAL A CG2  1 
ATOM   336  N N    . TRP A 1 120 ? 113.41500 105.68200 130.21800 1.000 35.54236  ? 120 TRP A N    1 
ATOM   337  C CA   . TRP A 1 120 ? 114.49300 106.17600 129.37000 1.000 28.77209  ? 120 TRP A CA   1 
ATOM   338  C C    . TRP A 1 120 ? 115.23000 105.04800 128.66600 1.000 31.24705  ? 120 TRP A C    1 
ATOM   339  O O    . TRP A 1 120 ? 115.59900 105.19500 127.49600 1.000 34.98386  ? 120 TRP A O    1 
ATOM   340  C CB   . TRP A 1 120 ? 115.47900 106.99600 130.20400 1.000 26.28918  ? 120 TRP A CB   1 
ATOM   341  C CG   . TRP A 1 120 ? 114.85200 108.17200 130.87600 1.000 29.87698  ? 120 TRP A CG   1 
ATOM   342  C CD1  . TRP A 1 120 ? 114.27300 108.19600 132.10900 1.000 36.04262  ? 120 TRP A CD1  1 
ATOM   343  C CD2  . TRP A 1 120 ? 114.73900 109.49900 130.35200 1.000 28.49004  ? 120 TRP A CD2  1 
ATOM   344  N NE1  . TRP A 1 120 ? 113.80200 109.45600 132.38600 1.000 37.13124  ? 120 TRP A NE1  1 
ATOM   345  C CE2  . TRP A 1 120 ? 114.07700 110.27500 131.32300 1.000 33.74476  ? 120 TRP A CE2  1 
ATOM   346  C CE3  . TRP A 1 120 ? 115.13300 110.10700 129.15700 1.000 27.43592  ? 120 TRP A CE3  1 
ATOM   347  C CZ2  . TRP A 1 120 ? 113.80000 111.62500 131.13700 1.000 28.06802  ? 120 TRP A CZ2  1 
ATOM   348  C CZ3  . TRP A 1 120 ? 114.85800 111.44700 128.97400 1.000 34.89977  ? 120 TRP A CZ3  1 
ATOM   349  C CH2  . TRP A 1 120 ? 114.19700 112.19200 129.95900 1.000 33.33176  ? 120 TRP A CH2  1 
ATOM   350  N N    . ALA A 1 121 ? 115.36100 103.88800 129.31000 1.000 23.00966  ? 121 ALA A N    1 
ATOM   351  C CA   . ALA A 1 121 ? 115.98700 102.75700 128.63600 1.000 23.02389  ? 121 ALA A CA   1 
ATOM   352  C C    . ALA A 1 121 ? 115.07500 102.18500 127.55800 1.000 26.80165  ? 121 ALA A C    1 
ATOM   353  O O    . ALA A 1 121 ? 115.54000 101.83100 126.46800 1.000 31.58038  ? 121 ALA A O    1 
ATOM   354  C CB   . ALA A 1 121 ? 116.35900 101.68200 129.65700 1.000 16.94261  ? 121 ALA A CB   1 
ATOM   355  N N    . ILE A 1 122 ? 113.77000 102.11900 127.82700 1.000 18.27775  ? 122 ILE A N    1 
ATOM   356  C CA   . ILE A 1 122 ? 112.83400 101.61100 126.83100 1.000 22.61730  ? 122 ILE A CA   1 
ATOM   357  C C    . ILE A 1 122 ? 112.73300 102.57100 125.65300 1.000 18.44907  ? 122 ILE A C    1 
ATOM   358  O O    . ILE A 1 122 ? 112.71900 102.14900 124.48900 1.000 23.18559  ? 122 ILE A O    1 
ATOM   359  C CB   . ILE A 1 122 ? 111.45800 101.35800 127.47500 1.000 29.25893  ? 122 ILE A CB   1 
ATOM   360  C CG1  . ILE A 1 122 ? 111.61400 100.51600 128.74100 1.000 26.13391  ? 122 ILE A CG1  1 
ATOM   361  C CG2  . ILE A 1 122 ? 110.50900 100.68700 126.48700 1.000 21.41284  ? 122 ILE A CG2  1 
ATOM   362  C CD1  . ILE A 1 122 ? 110.30900 100.19800 129.42700 1.000 24.82693  ? 122 ILE A CD1  1 
ATOM   363  N N    . LEU A 1 123 ? 112.67200 103.87700 125.93000 1.000 16.02935  ? 123 LEU A N    1 
ATOM   364  C CA   . LEU A 1 123 ? 112.65500 104.84300 124.83900 1.000 18.41128  ? 123 LEU A CA   1 
ATOM   365  C C    . LEU A 1 123 ? 113.93700 104.77300 124.01700 1.000 21.36042  ? 123 LEU A C    1 
ATOM   366  O O    . LEU A 1 123 ? 113.89300 104.85800 122.78600 1.000 27.84369  ? 123 LEU A O    1 
ATOM   367  C CB   . LEU A 1 123 ? 112.44100 106.24900 125.39600 1.000 23.65039  ? 123 LEU A CB   1 
ATOM   368  C CG   . LEU A 1 123 ? 112.17800 107.39900 124.42300 1.000 26.14757  ? 123 LEU A CG   1 
ATOM   369  C CD1  . LEU A 1 123 ? 110.90500 107.17500 123.62000 1.000 18.85809  ? 123 LEU A CD1  1 
ATOM   370  C CD2  . LEU A 1 123 ? 112.10400 108.70600 125.18800 1.000 23.20893  ? 123 LEU A CD2  1 
ATOM   371  N N    . THR A 1 124 ? 115.09000 104.60600 124.67200 1.000 19.08963  ? 124 THR A N    1 
ATOM   372  C CA   . THR A 1 124 ? 116.34200 104.50200 123.93100 1.000 18.80068  ? 124 THR A CA   1 
ATOM   373  C C    . THR A 1 124 ? 116.37100 103.25600 123.05300 1.000 22.32417  ? 124 THR A C    1 
ATOM   374  O O    . THR A 1 124 ? 116.78500 103.31300 121.88800 1.000 24.98679  ? 124 THR A O    1 
ATOM   375  C CB   . THR A 1 124 ? 117.52600 104.50300 124.89700 1.000 22.09650  ? 124 THR A CB   1 
ATOM   376  O OG1  . THR A 1 124 ? 117.43400 105.63900 125.76400 1.000 28.89908  ? 124 THR A OG1  1 
ATOM   377  C CG2  . THR A 1 124 ? 118.83500 104.57100 124.13200 1.000 23.51717  ? 124 THR A CG2  1 
ATOM   378  N N    . VAL A 1 125 ? 115.92400 102.12100 123.59400 1.000 22.36387  ? 125 VAL A N    1 
ATOM   379  C CA   . VAL A 1 125 ? 115.90000 100.87800 122.82700 1.000 21.25497  ? 125 VAL A CA   1 
ATOM   380  C C    . VAL A 1 125 ? 114.99100 101.00700 121.61100 1.000 23.33199  ? 125 VAL A C    1 
ATOM   381  O O    . VAL A 1 125 ? 115.35600 100.61300 120.49700 1.000 27.90360  ? 125 VAL A O    1 
ATOM   382  C CB   . VAL A 1 125 ? 115.47300 99.70100  123.72200 1.000 21.33205  ? 125 VAL A CB   1 
ATOM   383  C CG1  . VAL A 1 125 ? 114.99800 98.53600  122.87000 1.000 17.34712  ? 125 VAL A CG1  1 
ATOM   384  C CG2  . VAL A 1 125 ? 116.61900 99.26900  124.61900 1.000 14.08546  ? 125 VAL A CG2  1 
ATOM   385  N N    . VAL A 1 126 ? 113.79400 101.56500 121.80200 1.000 17.44806  ? 126 VAL A N    1 
ATOM   386  C CA   . VAL A 1 126 ? 112.87500 101.73700 120.68100 1.000 13.26610  ? 126 VAL A CA   1 
ATOM   387  C C    . VAL A 1 126 ? 113.31000 102.81800 119.69400 1.000 25.04542  ? 126 VAL A C    1 
ATOM   388  O O    . VAL A 1 126 ? 112.91900 102.76500 118.52300 1.000 28.44030  ? 126 VAL A O    1 
ATOM   389  C CB   . VAL A 1 126 ? 111.46300 102.03900 121.21900 1.000 24.50117  ? 126 VAL A CB   1 
ATOM   390  C CG1  . VAL A 1 126 ? 110.49200 102.26600 120.07700 1.000 27.59977  ? 126 VAL A CG1  1 
ATOM   391  C CG2  . VAL A 1 126 ? 110.98400 100.90900 122.11500 1.000 21.82133  ? 126 VAL A CG2  1 
ATOM   392  N N    . VAL A 1 127 ? 114.11100 103.79300 120.11800 1.000 29.12955  ? 127 VAL A N    1 
ATOM   393  C CA   . VAL A 1 127 ? 114.56600 104.83500 119.20200 1.000 18.32511  ? 127 VAL A CA   1 
ATOM   394  C C    . VAL A 1 127 ? 115.82600 104.47900 118.40600 1.000 17.16146  ? 127 VAL A C    1 
ATOM   395  O O    . VAL A 1 127 ? 115.95500 104.88900 117.24800 1.000 23.50118  ? 127 VAL A O    1 
ATOM   396  C CB   . VAL A 1 127 ? 114.77200 106.13800 119.99400 1.000 19.41948  ? 127 VAL A CB   1 
ATOM   397  C CG1  . VAL A 1 127 ? 115.54700 107.15000 119.17500 1.000 22.85107  ? 127 VAL A CG1  1 
ATOM   398  C CG2  . VAL A 1 127 ? 113.43400 106.70800 120.42500 1.000 19.65794  ? 127 VAL A CG2  1 
ATOM   399  N N    . VAL A 1 128 ? 116.76000 103.71700 118.98100 1.000 12.01275  ? 128 VAL A N    1 
ATOM   400  C CA   . VAL A 1 128 ? 118.10400 103.59600 118.41600 1.000 22.52781  ? 128 VAL A CA   1 
ATOM   401  C C    . VAL A 1 128 ? 118.32900 102.29700 117.65100 1.000 19.79580  ? 128 VAL A C    1 
ATOM   402  O O    . VAL A 1 128 ? 119.43600 102.07800 117.14400 1.000 23.25400  ? 128 VAL A O    1 
ATOM   403  C CB   . VAL A 1 128 ? 119.18300 103.75800 119.50500 1.000 19.93864  ? 128 VAL A CB   1 
ATOM   404  C CG1  . VAL A 1 128 ? 118.86500 104.94600 120.38900 1.000 17.79877  ? 128 VAL A CG1  1 
ATOM   405  C CG2  . VAL A 1 128 ? 119.30500 102.49000 120.32500 1.000 23.24268  ? 128 VAL A CG2  1 
ATOM   406  N N    . PHE A 1 129 ? 117.32200 101.43900 117.53800 1.000 24.18879  ? 129 PHE A N    1 
ATOM   407  C CA   . PHE A 1 129 ? 117.44700 100.17700 116.81400 1.000 20.65750  ? 129 PHE A CA   1 
ATOM   408  C C    . PHE A 1 129 ? 117.03100 100.36400 115.35700 1.000 23.16692  ? 129 PHE A C    1 
ATOM   409  O O    . PHE A 1 129 ? 115.88000 100.71300 115.07600 1.000 28.57579  ? 129 PHE A O    1 
ATOM   410  C CB   . PHE A 1 129 ? 116.58100 99.11300  117.48900 1.000 21.86202  ? 129 PHE A CB   1 
ATOM   411  C CG   . PHE A 1 129 ? 117.22900 97.76000  117.59300 1.000 24.55482  ? 129 PHE A CG   1 
ATOM   412  C CD1  . PHE A 1 129 ? 117.36900 96.95100  116.48100 1.000 24.16160  ? 129 PHE A CD1  1 
ATOM   413  C CD2  . PHE A 1 129 ? 117.67600 97.28900  118.81500 1.000 18.77164  ? 129 PHE A CD2  1 
ATOM   414  C CE1  . PHE A 1 129 ? 117.95400 95.70400  116.58300 1.000 21.18487  ? 129 PHE A CE1  1 
ATOM   415  C CE2  . PHE A 1 129 ? 118.26300 96.04400  118.92200 1.000 14.62953  ? 129 PHE A CE2  1 
ATOM   416  C CZ   . PHE A 1 129 ? 118.40200 95.25100  117.80600 1.000 15.73224  ? 129 PHE A CZ   1 
ATOM   417  N N    . GLU A 1 130 ? 117.96800 100.13600 114.43300 1.000 27.02672  ? 130 GLU A N    1 
ATOM   418  C CA   . GLU A 1 130 ? 117.72400 100.30600 113.00700 1.000 25.89738  ? 130 GLU A CA   1 
ATOM   419  C C    . GLU A 1 130 ? 117.99600 99.00800  112.25300 1.000 26.07803  ? 130 GLU A C    1 
ATOM   420  O O    . GLU A 1 130 ? 118.63100 98.08300  112.76500 1.000 25.07467  ? 130 GLU A O    1 
ATOM   421  C CB   . GLU A 1 130 ? 118.58500 101.42700 112.41100 1.000 18.43152  ? 130 GLU A CB   1 
ATOM   422  C CG   . GLU A 1 130 ? 118.70000 102.66500 113.27800 1.000 24.16300  ? 130 GLU A CG   1 
ATOM   423  C CD   . GLU A 1 130 ? 117.66700 103.71600 112.92500 1.000 30.32849  ? 130 GLU A CD   1 
ATOM   424  O OE1  . GLU A 1 130 ? 116.65000 103.81900 113.64100 1.000 37.30835  ? 130 GLU A OE1  1 
ATOM   425  O OE2  . GLU A 1 130 ? 117.86000 104.42800 111.92100 1.000 30.03542  ? 130 GLU A OE2  1 
ATOM   426  N N    . PHE A 1 131 ? 117.49500 98.96300  111.01500 1.000 22.30347  ? 131 PHE A N    1 
ATOM   427  C CA   . PHE A 1 131 ? 117.65900 97.78600  110.16500 1.000 21.40344  ? 131 PHE A CA   1 
ATOM   428  C C    . PHE A 1 131 ? 119.11900 97.45500  109.86600 1.000 20.83310  ? 131 PHE A C    1 
ATOM   429  O O    . PHE A 1 131 ? 119.48700 96.27600  109.79800 1.000 24.10387  ? 131 PHE A O    1 
ATOM   430  C CB   . PHE A 1 131 ? 116.88900 97.99300  108.86000 1.000 21.43718  ? 131 PHE A CB   1 
ATOM   431  C CG   . PHE A 1 131 ? 116.15800 96.77200  108.38600 1.000 24.34466  ? 131 PHE A CG   1 
ATOM   432  C CD1  . PHE A 1 131 ? 115.12100 96.23700  109.12700 1.000 18.03329  ? 131 PHE A CD1  1 
ATOM   433  C CD2  . PHE A 1 131 ? 116.51000 96.16200  107.19500 1.000 31.50509  ? 131 PHE A CD2  1 
ATOM   434  C CE1  . PHE A 1 131 ? 114.45200 95.11400  108.69300 1.000 25.29158  ? 131 PHE A CE1  1 
ATOM   435  C CE2  . PHE A 1 131 ? 115.84300 95.03900  106.75500 1.000 34.07050  ? 131 PHE A CE2  1 
ATOM   436  C CZ   . PHE A 1 131 ? 114.81200 94.51300  107.50500 1.000 30.79345  ? 131 PHE A CZ   1 
ATOM   437  N N    . THR A 1 132 ? 119.97100 98.46200  109.69100 1.000 26.36442  ? 132 THR A N    1 
ATOM   438  C CA   . THR A 1 132 ? 121.36700 98.21800  109.35500 1.000 9.09805   ? 132 THR A CA   1 
ATOM   439  C C    . THR A 1 132 ? 122.30700 98.70900  110.44900 1.000 9.70739   ? 132 THR A C    1 
ATOM   440  O O    . THR A 1 132 ? 121.94300 99.52800  111.29600 1.000 19.90790  ? 132 THR A O    1 
ATOM   441  C CB   . THR A 1 132 ? 121.74400 98.87600  108.01800 1.000 17.29198  ? 132 THR A CB   1 
ATOM   442  O OG1  . THR A 1 132 ? 121.43100 100.27200 108.05700 1.000 25.16176  ? 132 THR A OG1  1 
ATOM   443  C CG2  . THR A 1 132 ? 120.98900 98.22700  106.87200 1.000 14.44038  ? 132 THR A CG2  1 
ATOM   444  N N    . ILE A 1 133 ? 123.53000 98.17500  110.41800 1.000 11.48237  ? 133 ILE A N    1 
ATOM   445  C CA   . ILE A 1 133 ? 124.54700 98.55200  111.39400 1.000 23.07004  ? 133 ILE A CA   1 
ATOM   446  C C    . ILE A 1 133 ? 125.05500 99.96900  111.14500 1.000 17.73265  ? 133 ILE A C    1 
ATOM   447  O O    . ILE A 1 133 ? 125.27100 100.74000 112.08900 1.000 28.57951  ? 133 ILE A O    1 
ATOM   448  C CB   . ILE A 1 133 ? 125.69800 97.52900  111.37100 1.000 27.24430  ? 133 ILE A CB   1 
ATOM   449  C CG1  . ILE A 1 133 ? 125.33800 96.29800  112.20300 1.000 22.91022  ? 133 ILE A CG1  1 
ATOM   450  C CG2  . ILE A 1 133 ? 126.99100 98.15900  111.86500 1.000 22.54418  ? 133 ILE A CG2  1 
ATOM   451  C CD1  . ILE A 1 133 ? 125.92400 95.01900  111.66500 1.000 24.49764  ? 133 ILE A CD1  1 
ATOM   452  N N    . GLY A 1 134 ? 125.23300 100.34800 109.87500 1.000 12.97580  ? 134 GLY A N    1 
ATOM   453  C CA   . GLY A 1 134 ? 125.76800 101.66800 109.58600 1.000 14.01416  ? 134 GLY A CA   1 
ATOM   454  C C    . GLY A 1 134 ? 124.77100 102.78100 109.81700 1.000 19.90194  ? 134 GLY A C    1 
ATOM   455  O O    . GLY A 1 134 ? 125.14600 103.87600 110.25500 1.000 27.14615  ? 134 GLY A O    1 
ATOM   456  N N    . ALA A 1 135 ? 123.48400 102.50000 109.61200 1.000 13.39668  ? 135 ALA A N    1 
ATOM   457  C CA   . ALA A 1 135 ? 122.47900 103.49500 109.94700 1.000 13.69014  ? 135 ALA A CA   1 
ATOM   458  C C    . ALA A 1 135 ? 122.38000 103.65000 111.45100 1.000 13.51908  ? 135 ALA A C    1 
ATOM   459  O O    . ALA A 1 135 ? 122.21500 104.76900 111.95100 1.000 22.15104  ? 135 ALA A O    1 
ATOM   460  C CB   . ALA A 1 135 ? 121.12500 103.10300 109.35800 1.000 12.90370  ? 135 ALA A CB   1 
ATOM   461  N N    . THR A 1 136 ? 122.58600 102.55600 112.18500 1.000 15.78580  ? 136 THR A N    1 
ATOM   462  C CA   . THR A 1 136 ? 122.54100 102.62800 113.63500 1.000 6.39265   ? 136 THR A CA   1 
ATOM   463  C C    . THR A 1 136 ? 123.71500 103.43500 114.15800 1.000 14.41584  ? 136 THR A C    1 
ATOM   464  O O    . THR A 1 136 ? 123.54300 104.28900 115.03100 1.000 25.22382  ? 136 THR A O    1 
ATOM   465  C CB   . THR A 1 136 ? 122.55100 101.22000 114.23400 1.000 17.85198  ? 136 THR A CB   1 
ATOM   466  O OG1  . THR A 1 136 ? 121.40700 100.49000 113.77700 1.000 25.16272  ? 136 THR A OG1  1 
ATOM   467  C CG2  . THR A 1 136 ? 122.53600 101.27800 115.75000 1.000 24.58458  ? 136 THR A CG2  1 
ATOM   468  N N    . LEU A 1 137 ? 124.89000 103.26900 113.55000 1.000 18.72769  ? 137 LEU A N    1 
ATOM   469  C CA   . LEU A 1 137 ? 126.06100 103.99000 114.03400 1.000 10.04034  ? 137 LEU A CA   1 
ATOM   470  C C    . LEU A 1 137 ? 125.97000 105.47700 113.71000 1.000 15.23216  ? 137 LEU A C    1 
ATOM   471  O O    . LEU A 1 137 ? 126.20800 106.32300 114.58400 1.000 28.86196  ? 137 LEU A O    1 
ATOM   472  C CB   . LEU A 1 137 ? 127.32800 103.38700 113.43100 1.000 15.21869  ? 137 LEU A CB   1 
ATOM   473  C CG   . LEU A 1 137 ? 127.79800 102.04300 113.99300 1.000 19.35705  ? 137 LEU A CG   1 
ATOM   474  C CD1  . LEU A 1 137 ? 129.10100 101.61900 113.33900 1.000 20.04001  ? 137 LEU A CD1  1 
ATOM   475  C CD2  . LEU A 1 137 ? 127.95000 102.10600 115.50200 1.000 14.03065  ? 137 LEU A CD2  1 
ATOM   476  N N    . SER A 1 138 ? 125.54900 105.82200 112.48900 1.000 18.05962  ? 138 SER A N    1 
ATOM   477  C CA   . SER A 1 138 ? 125.50200 107.23500 112.12700 1.000 15.33907  ? 138 SER A CA   1 
ATOM   478  C C    . SER A 1 138 ? 124.38500 107.96600 112.86500 1.000 18.50830  ? 138 SER A C    1 
ATOM   479  O O    . SER A 1 138 ? 124.60200 109.06100 113.40900 1.000 33.06166  ? 138 SER A O    1 
ATOM   480  C CB   . SER A 1 138 ? 125.33900 107.38300 110.61500 1.000 22.47752  ? 138 SER A CB   1 
ATOM   481  O OG   . SER A 1 138 ? 124.04800 106.98000 110.19900 1.000 32.50387  ? 138 SER A OG   1 
ATOM   482  N N    . LYS A 1 139 ? 123.19000 107.37200 112.92900 1.000 14.46612  ? 139 LYS A N    1 
ATOM   483  C CA   . LYS A 1 139 ? 122.10900 108.03700 113.64000 1.000 12.22902  ? 139 LYS A CA   1 
ATOM   484  C C    . LYS A 1 139 ? 122.35800 108.07000 115.14100 1.000 18.85429  ? 139 LYS A C    1 
ATOM   485  O O    . LYS A 1 139 ? 121.95600 109.03100 115.80000 1.000 31.99540  ? 139 LYS A O    1 
ATOM   486  C CB   . LYS A 1 139 ? 120.77200 107.37800 113.31400 1.000 20.87582  ? 139 LYS A CB   1 
ATOM   487  C CG   . LYS A 1 139 ? 120.34300 107.60300 111.87500 1.000 19.01168  ? 139 LYS A CG   1 
ATOM   488  C CD   . LYS A 1 139 ? 119.01400 106.95400 111.58100 1.000 22.91864  ? 139 LYS A CD   1 
ATOM   489  C CE   . LYS A 1 139 ? 118.58700 107.20800 110.15100 1.000 22.21789  ? 139 LYS A CE   1 
ATOM   490  N NZ   . LYS A 1 139 ? 117.28600 106.55300 109.84500 1.000 28.89637  ? 139 LYS A NZ   1 
ATOM   491  N N    . GLY A 1 140 ? 123.02400 107.05800 115.70600 1.000 20.66226  ? 140 GLY A N    1 
ATOM   492  C CA   . GLY A 1 140 ? 123.36100 107.12300 117.11300 1.000 13.30508  ? 140 GLY A CA   1 
ATOM   493  C C    . GLY A 1 140 ? 124.38700 108.19000 117.42200 1.000 15.22626  ? 140 GLY A C    1 
ATOM   494  O O    . GLY A 1 140 ? 124.31100 108.84000 118.46500 1.000 22.58598  ? 140 GLY A O    1 
ATOM   495  N N    . PHE A 1 141 ? 125.33300 108.42100 116.50900 1.000 17.25129  ? 141 PHE A N    1 
ATOM   496  C CA   . PHE A 1 141 ? 126.28200 109.51000 116.71800 1.000 16.23980  ? 141 PHE A CA   1 
ATOM   497  C C    . PHE A 1 141 ? 125.57900 110.86500 116.65400 1.000 22.47677  ? 141 PHE A C    1 
ATOM   498  O O    . PHE A 1 141 ? 125.81100 111.74200 117.50300 1.000 26.56360  ? 141 PHE A O    1 
ATOM   499  C CB   . PHE A 1 141 ? 127.40100 109.41100 115.67900 1.000 13.86593  ? 141 PHE A CB   1 
ATOM   500  C CG   . PHE A 1 141 ? 128.40100 110.52700 115.73900 1.000 18.12994  ? 141 PHE A CG   1 
ATOM   501  C CD1  . PHE A 1 141 ? 129.48600 110.45500 116.59600 1.000 22.84218  ? 141 PHE A CD1  1 
ATOM   502  C CD2  . PHE A 1 141 ? 128.27500 111.63600 114.92200 1.000 21.44887  ? 141 PHE A CD2  1 
ATOM   503  C CE1  . PHE A 1 141 ? 130.41600 111.47400 116.64700 1.000 23.02445  ? 141 PHE A CE1  1 
ATOM   504  C CE2  . PHE A 1 141 ? 129.20100 112.65700 114.97100 1.000 20.02248  ? 141 PHE A CE2  1 
ATOM   505  C CZ   . PHE A 1 141 ? 130.27200 112.57500 115.83300 1.000 18.62665  ? 141 PHE A CZ   1 
ATOM   506  N N    . ASN A 1 142 ? 124.66300 111.03000 115.69600 1.000 24.27664  ? 142 ASN A N    1 
ATOM   507  C CA   . ASN A 1 142 ? 123.96500 112.30900 115.58800 1.000 17.46306  ? 142 ASN A CA   1 
ATOM   508  C C    . ASN A 1 142 ? 122.95500 112.51100 116.71500 1.000 23.49223  ? 142 ASN A C    1 
ATOM   509  O O    . ASN A 1 142 ? 122.65000 113.65500 117.06700 1.000 31.01033  ? 142 ASN A O    1 
ATOM   510  C CB   . ASN A 1 142 ? 123.27000 112.42300 114.23200 1.000 18.65495  ? 142 ASN A CB   1 
ATOM   511  C CG   . ASN A 1 142 ? 124.24200 112.68200 113.10100 1.000 26.42334  ? 142 ASN A CG   1 
ATOM   512  O OD1  . ASN A 1 142 ? 125.18000 113.46400 113.24300 1.000 35.00547  ? 142 ASN A OD1  1 
ATOM   513  N ND2  . ASN A 1 142 ? 124.01900 112.03100 111.96700 1.000 31.36549  ? 142 ASN A ND2  1 
ATOM   514  N N    . ARG A 1 143 ? 122.42800 111.42900 117.29100 1.000 23.22832  ? 143 ARG A N    1 
ATOM   515  C CA   . ARG A 1 143 ? 121.54300 111.54900 118.44300 1.000 17.88329  ? 143 ARG A CA   1 
ATOM   516  C C    . ARG A 1 143 ? 122.29900 111.67600 119.75800 1.000 16.12714  ? 143 ARG A C    1 
ATOM   517  O O    . ARG A 1 143 ? 121.72500 112.15200 120.74200 1.000 27.80035  ? 143 ARG A O    1 
ATOM   518  C CB   . ARG A 1 143 ? 120.59600 110.34800 118.50400 1.000 18.66385  ? 143 ARG A CB   1 
ATOM   519  C CG   . ARG A 1 143 ? 119.53100 110.35300 117.42300 1.000 17.49717  ? 143 ARG A CG   1 
ATOM   520  C CD   . ARG A 1 143 ? 118.45300 109.31900 117.68400 1.000 18.73152  ? 143 ARG A CD   1 
ATOM   521  N NE   . ARG A 1 143 ? 118.65800 108.11100 116.89400 1.000 20.82213  ? 143 ARG A NE   1 
ATOM   522  C CZ   . ARG A 1 143 ? 117.79300 107.63800 116.00600 1.000 27.19982  ? 143 ARG A CZ   1 
ATOM   523  N NH1  . ARG A 1 143 ? 116.64800 108.25300 115.76100 1.000 23.97720  ? 143 ARG A NH1  1 
ATOM   524  N NH2  . ARG A 1 143 ? 118.08500 106.52200 115.34800 1.000 24.80404  ? 143 ARG A NH2  1 
ATOM   525  N N    . ALA A 1 144 ? 123.56700 111.27400 119.79900 1.000 23.14361  ? 144 ALA A N    1 
ATOM   526  C CA   . ALA A 1 144 ? 124.38800 111.47800 120.98000 1.000 24.37333  ? 144 ALA A CA   1 
ATOM   527  C C    . ALA A 1 144 ? 125.13100 112.80200 120.94600 1.000 31.65296  ? 144 ALA A C    1 
ATOM   528  O O    . ALA A 1 144 ? 125.77600 113.16000 121.93600 1.000 31.09405  ? 144 ALA A O    1 
ATOM   529  C CB   . ALA A 1 144 ? 125.39100 110.33200 121.13800 1.000 23.69324  ? 144 ALA A CB   1 
ATOM   530  N N    . LEU A 1 145 ? 125.05400 113.53400 119.83600 1.000 33.24001  ? 145 LEU A N    1 
ATOM   531  C CA   . LEU A 1 145 ? 125.57000 114.89900 119.86400 1.000 30.27474  ? 145 LEU A CA   1 
ATOM   532  C C    . LEU A 1 145 ? 124.52600 115.89800 120.35800 1.000 29.66874  ? 145 LEU A C    1 
ATOM   533  O O    . LEU A 1 145 ? 124.86000 116.82100 121.11100 1.000 38.03200  ? 145 LEU A O    1 
ATOM   534  C CB   . LEU A 1 145 ? 126.05300 115.32200 118.47500 1.000 31.98520  ? 145 LEU A CB   1 
ATOM   535  C CG   . LEU A 1 145 ? 127.43000 114.85800 118.00500 1.000 36.91734  ? 145 LEU A CG   1 
ATOM   536  C CD1  . LEU A 1 145 ? 127.58600 115.10800 116.51400 1.000 32.88134  ? 145 LEU A CD1  1 
ATOM   537  C CD2  . LEU A 1 145 ? 128.52600 115.56300 118.78400 1.000 30.88616  ? 145 LEU A CD2  1 
ATOM   538  N N    . GLY A 1 146 ? 123.25700 115.70800 119.98500 1.000 26.20147  ? 146 GLY A N    1 
ATOM   539  C CA   . GLY A 1 146 ? 122.22000 116.62300 120.43100 1.000 18.22981  ? 146 GLY A CA   1 
ATOM   540  C C    . GLY A 1 146 ? 121.94900 116.56700 121.92000 1.000 28.27472  ? 146 GLY A C    1 
ATOM   541  O O    . GLY A 1 146 ? 121.69200 117.60200 122.54200 1.000 34.71886  ? 146 GLY A O    1 
ATOM   542  N N    . THR A 1 147 ? 122.08000 115.38800 122.53100 1.000 26.06029  ? 147 THR A N    1 
ATOM   543  C CA   . THR A 1 147 ? 121.81900 115.28300 123.96400 1.000 20.83656  ? 147 THR A CA   1 
ATOM   544  C C    . THR A 1 147 ? 122.95000 115.90300 124.77200 1.000 26.00746  ? 147 THR A C    1 
ATOM   545  O O    . THR A 1 147 ? 122.70600 116.59100 125.77100 1.000 36.96015  ? 147 THR A O    1 
ATOM   546  C CB   . THR A 1 147 ? 121.62800 113.81800 124.35700 1.000 25.50509  ? 147 THR A CB   1 
ATOM   547  O OG1  . THR A 1 147 ? 120.83300 113.15500 123.36800 1.000 32.33293  ? 147 THR A OG1  1 
ATOM   548  C CG2  . THR A 1 147 ? 120.94100 113.70800 125.70500 1.000 25.99551  ? 147 THR A CG2  1 
ATOM   549  N N    . LEU A 1 148 ? 124.18800 115.74900 124.30500 1.000 23.70937  ? 148 LEU A N    1 
ATOM   550  C CA   . LEU A 1 148 ? 125.31900 116.31400 125.02200 1.000 28.04795  ? 148 LEU A CA   1 
ATOM   551  C C    . LEU A 1 148 ? 125.49300 117.79600 124.73600 1.000 28.90681  ? 148 LEU A C    1 
ATOM   552  O O    . LEU A 1 148 ? 126.16900 118.48400 125.50700 1.000 37.70680  ? 148 LEU A O    1 
ATOM   553  C CB   . LEU A 1 148 ? 126.60200 115.56300 124.66400 1.000 32.46364  ? 148 LEU A CB   1 
ATOM   554  C CG   . LEU A 1 148 ? 126.64200 114.07300 125.00700 1.000 32.19291  ? 148 LEU A CG   1 
ATOM   555  C CD1  . LEU A 1 148 ? 128.07600 113.60100 125.15800 1.000 29.11152  ? 148 LEU A CD1  1 
ATOM   556  C CD2  . LEU A 1 148 ? 125.84500 113.78400 126.26800 1.000 31.04774  ? 148 LEU A CD2  1 
ATOM   557  N N    . SER A 1 149 ? 124.89000 118.30500 123.66100 1.000 28.01874  ? 149 SER A N    1 
ATOM   558  C CA   . SER A 1 149 ? 124.88400 119.74400 123.43700 1.000 26.50312  ? 149 SER A CA   1 
ATOM   559  C C    . SER A 1 149 ? 123.69900 120.42900 124.10300 1.000 29.53119  ? 149 SER A C    1 
ATOM   560  O O    . SER A 1 149 ? 123.78300 121.62300 124.41400 1.000 35.33709  ? 149 SER A O    1 
ATOM   561  C CB   . SER A 1 149 ? 124.87900 120.04800 121.93800 1.000 23.93443  ? 149 SER A CB   1 
ATOM   562  O OG   . SER A 1 149 ? 123.64200 119.69300 121.35000 1.000 32.35385  ? 149 SER A OG   1 
ATOM   563  N N    . ALA A 1 150 ? 122.60000 119.70800 124.33500 1.000 34.56757  ? 150 ALA A N    1 
ATOM   564  C CA   . ALA A 1 150 ? 121.46300 120.26300 125.05500 1.000 21.65208  ? 150 ALA A CA   1 
ATOM   565  C C    . ALA A 1 150 ? 121.53500 120.03600 126.55800 1.000 32.62042  ? 150 ALA A C    1 
ATOM   566  O O    . ALA A 1 150 ? 120.70900 120.59200 127.28900 1.000 37.57243  ? 150 ALA A O    1 
ATOM   567  C CB   . ALA A 1 150 ? 120.15700 119.67500 124.51400 1.000 8.99906   ? 150 ALA A CB   1 
ATOM   568  N N    . GLY A 1 151 ? 122.49000 119.24300 127.04000 1.000 34.79128  ? 151 GLY A N    1 
ATOM   569  C CA   . GLY A 1 151 ? 122.62900 119.08200 128.47300 1.000 25.42568  ? 151 GLY A CA   1 
ATOM   570  C C    . GLY A 1 151 ? 123.57500 120.07500 129.11600 1.000 29.68097  ? 151 GLY A C    1 
ATOM   571  O O    . GLY A 1 151 ? 123.50400 120.30300 130.32700 1.000 37.09644  ? 151 GLY A O    1 
ATOM   572  N N    . GLY A 1 152 ? 124.46600 120.67300 128.32800 1.000 28.24230  ? 152 GLY A N    1 
ATOM   573  C CA   . GLY A 1 152 ? 125.39200 121.65100 128.86500 1.000 26.27707  ? 152 GLY A CA   1 
ATOM   574  C C    . GLY A 1 152 ? 124.82800 123.05500 128.80400 1.000 35.11646  ? 152 GLY A C    1 
ATOM   575  O O    . GLY A 1 152 ? 125.08500 123.88700 129.68300 1.000 44.30980  ? 152 GLY A O    1 
ATOM   576  N N    . LEU A 1 153 ? 123.99300 123.30700 127.79500 1.000 29.35230  ? 153 LEU A N    1 
ATOM   577  C CA   . LEU A 1 153 ? 123.34800 124.60900 127.68100 1.000 21.93333  ? 153 LEU A CA   1 
ATOM   578  C C    . LEU A 1 153 ? 122.32800 124.80700 128.79300 1.000 32.18545  ? 153 LEU A C    1 
ATOM   579  O O    . LEU A 1 153 ? 122.21200 125.90600 129.35100 1.000 34.57036  ? 153 LEU A O    1 
ATOM   580  C CB   . LEU A 1 153 ? 122.68500 124.74300 126.30900 1.000 26.56558  ? 153 LEU A CB   1 
ATOM   581  C CG   . LEU A 1 153 ? 122.26500 126.14000 125.85200 1.000 30.41032  ? 153 LEU A CG   1 
ATOM   582  C CD1  . LEU A 1 153 ? 123.37900 127.14800 126.08500 1.000 36.71375  ? 153 LEU A CD1  1 
ATOM   583  C CD2  . LEU A 1 153 ? 121.85000 126.12500 124.39300 1.000 27.73000  ? 153 LEU A CD2  1 
ATOM   584  N N    . ALA A 1 154 ? 121.59700 123.74800 129.14800 1.000 33.55599  ? 154 ALA A N    1 
ATOM   585  C CA   . ALA A 1 154 ? 120.60300 123.88200 130.20200 1.000 25.79674  ? 154 ALA A CA   1 
ATOM   586  C C    . ALA A 1 154 ? 121.26300 124.08300 131.55700 1.000 29.89693  ? 154 ALA A C    1 
ATOM   587  O O    . ALA A 1 154 ? 120.73400 124.81800 132.39500 1.000 43.26299  ? 154 ALA A O    1 
ATOM   588  C CB   . ALA A 1 154 ? 119.69300 122.65500 130.22600 1.000 25.79841  ? 154 ALA A CB   1 
ATOM   589  N N    . LEU A 1 155 ? 122.47000 123.55000 131.74700 1.000 30.23628  ? 155 LEU A N    1 
ATOM   590  C CA   . LEU A 1 155 ? 123.15400 123.74700 133.01700 1.000 38.38910  ? 155 LEU A CA   1 
ATOM   591  C C    . LEU A 1 155 ? 123.90100 125.06900 133.04900 1.000 41.57593  ? 155 LEU A C    1 
ATOM   592  O O    . LEU A 1 155 ? 124.04300 125.66500 134.12400 1.000 47.02611  ? 155 LEU A O    1 
ATOM   593  C CB   . LEU A 1 155 ? 124.12700 122.59400 133.27700 1.000 40.39392  ? 155 LEU A CB   1 
ATOM   594  C CG   . LEU A 1 155 ? 123.52400 121.21400 133.55900 1.000 37.56047  ? 155 LEU A CG   1 
ATOM   595  C CD1  . LEU A 1 155 ? 124.59900 120.14300 133.52300 1.000 35.74828  ? 155 LEU A CD1  1 
ATOM   596  C CD2  . LEU A 1 155 ? 122.79500 121.19500 134.88900 1.000 40.39779  ? 155 LEU A CD2  1 
ATOM   597  N N    . GLY A 1 156 ? 124.19600 125.63600 131.88600 1.000 36.88357  ? 156 GLY A N    1 
ATOM   598  C CA   . GLY A 1 156 ? 124.83000 126.93200 131.86900 1.000 37.78759  ? 156 GLY A CA   1 
ATOM   599  C C    . GLY A 1 156 ? 123.77200 127.97800 132.13100 1.000 43.72888  ? 156 GLY A C    1 
ATOM   600  O O    . GLY A 1 156 ? 124.02200 128.94400 132.85400 1.000 49.53864  ? 156 GLY A O    1 
ATOM   601  N N    . MET A 1 157 ? 122.57800 127.79900 131.56200 1.000 47.59306  ? 157 MET A N    1 
ATOM   602  C CA   . MET A 1 157 ? 121.49000 128.71600 131.88400 1.000 44.65734  ? 157 MET A CA   1 
ATOM   603  C C    . MET A 1 157 ? 121.04900 128.56300 133.33800 1.000 44.56960  ? 157 MET A C    1 
ATOM   604  O O    . MET A 1 157 ? 120.78000 129.56300 134.01600 1.000 47.83175  ? 157 MET A O    1 
ATOM   605  C CB   . MET A 1 157 ? 120.31700 128.49900 130.93200 1.000 42.57947  ? 157 MET A CB   1 
ATOM   606  C CG   . MET A 1 157 ? 120.66400 128.76000 129.47800 1.000 45.88937  ? 157 MET A CG   1 
ATOM   607  S SD   . MET A 1 157 ? 120.06100 130.35600 128.90100 1.000 54.67306  ? 157 MET A SD   1 
ATOM   608  C CE   . MET A 1 157 ? 120.05800 130.09400 127.13100 1.000 47.37963  ? 157 MET A CE   1 
ATOM   609  N N    . ALA A 1 158 ? 120.99400 127.32700 133.84800 1.000 42.84557  ? 158 ALA A N    1 
ATOM   610  C CA   . ALA A 1 158 ? 120.60700 127.12000 135.23600 1.000 42.11412  ? 158 ALA A CA   1 
ATOM   611  C C    . ALA A 1 158 ? 121.68700 127.55400 136.21400 1.000 50.09614  ? 158 ALA A C    1 
ATOM   612  O O    . ALA A 1 158 ? 121.43000 127.58400 137.42200 1.000 52.10366  ? 158 ALA A O    1 
ATOM   613  C CB   . ALA A 1 158 ? 120.25600 125.65100 135.47100 1.000 46.96855  ? 158 ALA A CB   1 
ATOM   614  N N    . GLU A 1 159 ? 122.88000 127.89100 135.72600 1.000 56.92491  ? 159 GLU A N    1 
ATOM   615  C CA   . GLU A 1 159 ? 123.91900 128.45000 136.57800 1.000 52.65645  ? 159 GLU A CA   1 
ATOM   616  C C    . GLU A 1 159 ? 124.05300 129.95600 136.42300 1.000 51.10265  ? 159 GLU A C    1 
ATOM   617  O O    . GLU A 1 159 ? 124.47800 130.63100 137.36500 1.000 56.08737  ? 159 GLU A O    1 
ATOM   618  C CB   . GLU A 1 159 ? 125.26800 127.79100 136.27300 1.000 55.23239  ? 159 GLU A CB   1 
ATOM   619  C CG   . GLU A 1 159 ? 126.46900 128.66000 136.59700 1.000 57.23238  ? 159 GLU A CG   1 
ATOM   620  C CD   . GLU A 1 159 ? 127.61000 128.45400 135.62400 1.000 60.62728  ? 159 GLU A CD   1 
ATOM   621  O OE1  . GLU A 1 159 ? 128.22300 127.36500 135.64600 1.000 60.16637  ? 159 GLU A OE1  1 
ATOM   622  O OE2  . GLU A 1 159 ? 127.89000 129.37800 134.83100 1.000 57.77437  ? 159 GLU A OE2  1 
ATOM   623  N N    . LEU A 1 160 ? 123.69200 130.49400 135.26000 1.000 56.25527  ? 160 LEU A N    1 
ATOM   624  C CA   . LEU A 1 160 ? 123.71500 131.92700 135.00800 1.000 55.26796  ? 160 LEU A CA   1 
ATOM   625  C C    . LEU A 1 160 ? 122.41700 132.62500 135.39700 1.000 59.39203  ? 160 LEU A C    1 
ATOM   626  O O    . LEU A 1 160 ? 122.38900 133.85900 135.44100 1.000 59.90956  ? 160 LEU A O    1 
ATOM   627  C CB   . LEU A 1 160 ? 124.03200 132.17100 133.52300 1.000 52.87692  ? 160 LEU A CB   1 
ATOM   628  C CG   . LEU A 1 160 ? 124.13800 133.55600 132.87900 1.000 58.07621  ? 160 LEU A CG   1 
ATOM   629  C CD1  . LEU A 1 160 ? 124.67700 133.40500 131.47100 1.000 57.58434  ? 160 LEU A CD1  1 
ATOM   630  C CD2  . LEU A 1 160 ? 122.79400 134.25300 132.81500 1.000 58.99621  ? 160 LEU A CD2  1 
ATOM   631  N N    . SER A 1 161 ? 121.36200 131.87900 135.72700 1.000 64.84028  ? 161 SER A N    1 
ATOM   632  C CA   . SER A 1 161 ? 120.12100 132.51800 136.14900 1.000 62.16994  ? 161 SER A CA   1 
ATOM   633  C C    . SER A 1 161 ? 120.16200 133.01400 137.58800 1.000 65.72522  ? 161 SER A C    1 
ATOM   634  O O    . SER A 1 161 ? 119.28400 133.78900 137.98100 1.000 68.25560  ? 161 SER A O    1 
ATOM   635  C CB   . SER A 1 161 ? 118.94600 131.55300 135.98100 1.000 64.01458  ? 161 SER A CB   1 
ATOM   636  O OG   . SER A 1 161 ? 118.65300 130.89300 137.19900 1.000 64.92422  ? 161 SER A OG   1 
ATOM   637  N N    . THR A 1 162 ? 121.14900 132.59000 138.37900 1.000 70.35849  ? 162 THR A N    1 
ATOM   638  C CA   . THR A 1 162 ? 121.23500 133.04500 139.76300 1.000 70.29102  ? 162 THR A CA   1 
ATOM   639  C C    . THR A 1 162 ? 121.51800 134.54000 139.84900 1.000 71.21334  ? 162 THR A C    1 
ATOM   640  O O    . THR A 1 162 ? 121.04900 135.20500 140.77900 1.000 71.48306  ? 162 THR A O    1 
ATOM   641  C CB   . THR A 1 162 ? 122.31200 132.26200 140.51300 1.000 70.64969  ? 162 THR A CB   1 
ATOM   642  O OG1  . THR A 1 162 ? 123.59500 132.54300 139.94000 1.000 70.77084  ? 162 THR A OG1  1 
ATOM   643  C CG2  . THR A 1 162 ? 122.03900 130.76800 140.43300 1.000 71.46776  ? 162 THR A CG2  1 
ATOM   644  N N    . LEU A 1 163 ? 122.28600 135.08000 138.90000 1.000 70.96215  ? 163 LEU A N    1 
ATOM   645  C CA   . LEU A 1 163 ? 122.62400 136.49900 138.92500 1.000 71.29885  ? 163 LEU A CA   1 
ATOM   646  C C    . LEU A 1 163 ? 121.37300 137.36700 139.00200 1.000 75.41121  ? 163 LEU A C    1 
ATOM   647  O O    . LEU A 1 163 ? 121.28000 138.27400 139.83700 1.000 76.00113  ? 163 LEU A O    1 
ATOM   648  C CB   . LEU A 1 163 ? 123.44500 136.85600 137.68500 1.000 73.61082  ? 163 LEU A CB   1 
ATOM   649  C CG   . LEU A 1 163 ? 124.81600 136.19300 137.54700 1.000 75.76696  ? 163 LEU A CG   1 
ATOM   650  C CD1  . LEU A 1 163 ? 125.43600 136.53000 136.20100 1.000 73.78093  ? 163 LEU A CD1  1 
ATOM   651  C CD2  . LEU A 1 163 ? 125.73600 136.60600 138.68400 1.000 75.64393  ? 163 LEU A CD2  1 
ATOM   652  N N    . PHE A 1 164 ? 120.39700 137.10100 138.13500 1.000 78.99017  ? 164 PHE A N    1 
ATOM   653  C CA   . PHE A 1 164 ? 119.13700 137.83500 138.14700 1.000 77.08864  ? 164 PHE A CA   1 
ATOM   654  C C    . PHE A 1 164 ? 118.26400 137.41200 139.32100 1.000 76.92645  ? 164 PHE A C    1 
ATOM   655  O O    . PHE A 1 164 ? 117.25500 136.72600 139.13500 1.000 79.55426  ? 164 PHE A O    1 
ATOM   656  C CB   . PHE A 1 164 ? 118.38700 137.63200 136.82800 1.000 75.13075  ? 164 PHE A CB   1 
ATOM   657  C CG   . PHE A 1 164 ? 119.28000 137.60400 135.62400 1.000 75.35216  ? 164 PHE A CG   1 
ATOM   658  C CD1  . PHE A 1 164 ? 119.76300 138.78100 135.07900 1.000 75.75041  ? 164 PHE A CD1  1 
ATOM   659  C CD2  . PHE A 1 164 ? 119.64100 136.40400 135.04000 1.000 75.36045  ? 164 PHE A CD2  1 
ATOM   660  C CE1  . PHE A 1 164 ? 120.58600 138.76000 133.97200 1.000 77.65606  ? 164 PHE A CE1  1 
ATOM   661  C CE2  . PHE A 1 164 ? 120.46500 136.37800 133.93300 1.000 74.85870  ? 164 PHE A CE2  1 
ATOM   662  C CZ   . PHE A 1 164 ? 120.93800 137.55700 133.39800 1.000 76.16497  ? 164 PHE A CZ   1 
ATOM   663  N N    . GLY A 1 165 ? 118.64400 137.81600 140.52900 1.000 82.08683  ? 165 GLY A N    1 
ATOM   664  C CA   . GLY A 1 165 ? 117.91100 137.39700 141.70600 1.000 84.71250  ? 165 GLY A CA   1 
ATOM   665  C C    . GLY A 1 165 ? 116.48500 137.91000 141.70900 1.000 85.34513  ? 165 GLY A C    1 
ATOM   666  O O    . GLY A 1 165 ? 116.11200 138.81800 140.96500 1.000 85.64654  ? 165 GLY A O    1 
ATOM   667  N N    . ASP A 1 166 ? 115.67100 137.29900 142.56900 1.000 87.48090  ? 166 ASP A N    1 
ATOM   668  C CA   . ASP A 1 166 ? 114.26500 137.66400 142.69400 1.000 88.63297  ? 166 ASP A CA   1 
ATOM   669  C C    . ASP A 1 166 ? 113.49400 137.30100 141.43100 1.000 89.54431  ? 166 ASP A C    1 
ATOM   670  O O    . ASP A 1 166 ? 112.65300 136.39800 141.45100 1.000 90.39025  ? 166 ASP A O    1 
ATOM   671  C CB   . ASP A 1 166 ? 114.12300 139.15800 142.99600 1.000 87.73443  ? 166 ASP A CB   1 
ATOM   672  N N    . TRP A 1 167 ? 113.77100 137.99700 140.32900 1.000 87.92506  ? 167 TRP A N    1 
ATOM   673  C CA   . TRP A 1 167 ? 113.12000 137.69600 139.06000 1.000 86.78022  ? 167 TRP A CA   1 
ATOM   674  C C    . TRP A 1 167 ? 113.84500 136.57100 138.33400 1.000 86.41212  ? 167 TRP A C    1 
ATOM   675  O O    . TRP A 1 167 ? 114.16100 136.69400 137.14700 1.000 87.41779  ? 167 TRP A O    1 
ATOM   676  C CB   . TRP A 1 167 ? 113.06200 138.94100 138.17300 1.000 86.70365  ? 167 TRP A CB   1 
ATOM   677  C CG   . TRP A 1 167 ? 112.39000 140.11200 138.81400 1.000 89.39373  ? 167 TRP A CG   1 
ATOM   678  C CD1  . TRP A 1 167 ? 111.52000 140.08500 139.86500 1.000 89.44277  ? 167 TRP A CD1  1 
ATOM   679  C CD2  . TRP A 1 167 ? 112.52600 141.48800 138.44100 1.000 90.69961  ? 167 TRP A CD2  1 
ATOM   680  N NE1  . TRP A 1 167 ? 111.10900 141.36000 140.17100 1.000 89.67469  ? 167 TRP A NE1  1 
ATOM   681  C CE2  . TRP A 1 167 ? 111.71200 142.23900 139.31100 1.000 91.18783  ? 167 TRP A CE2  1 
ATOM   682  C CE3  . TRP A 1 167 ? 113.25800 142.15700 137.45500 1.000 88.26124  ? 167 TRP A CE3  1 
ATOM   683  C CZ2  . TRP A 1 167 ? 111.61000 143.62600 139.22600 1.000 89.63033  ? 167 TRP A CZ2  1 
ATOM   684  C CZ3  . TRP A 1 167 ? 113.15600 143.53300 137.37300 1.000 88.92897  ? 167 TRP A CZ3  1 
ATOM   685  C CH2  . TRP A 1 167 ? 112.33800 144.25300 138.25300 1.000 89.43579  ? 167 TRP A CH2  1 
ATOM   686  N N    . GLU A 1 168 ? 114.11100 135.47300 139.03600 1.000 79.25874  ? 168 GLU A N    1 
ATOM   687  C CA   . GLU A 1 168 ? 114.86300 134.35600 138.48500 1.000 78.11162  ? 168 GLU A CA   1 
ATOM   688  C C    . GLU A 1 168 ? 113.97200 133.24900 137.93900 1.000 79.05870  ? 168 GLU A C    1 
ATOM   689  O O    . GLU A 1 168 ? 114.49000 132.23500 137.46200 1.000 79.75222  ? 168 GLU A O    1 
ATOM   690  C CB   . GLU A 1 168 ? 115.81000 133.78700 139.54700 1.000 77.54733  ? 168 GLU A CB   1 
ATOM   691  C CG   . GLU A 1 168 ? 115.32600 132.50600 140.20000 1.000 79.42405  ? 168 GLU A CG   1 
ATOM   692  C CD   . GLU A 1 168 ? 116.40200 131.83500 141.02700 1.000 80.52238  ? 168 GLU A CD   1 
ATOM   693  O OE1  . GLU A 1 168 ? 117.59700 132.02300 140.71500 1.000 81.07274  ? 168 GLU A OE1  1 
ATOM   694  O OE2  . GLU A 1 168 ? 116.05500 131.12100 141.99100 1.000 81.22441  ? 168 GLU A OE2  1 
ATOM   695  N N    . GLU A 1 169 ? 112.65100 133.41700 137.99000 1.000 74.66005  ? 169 GLU A N    1 
ATOM   696  C CA   . GLU A 1 169 ? 111.72300 132.44900 137.42300 1.000 73.44152  ? 169 GLU A CA   1 
ATOM   697  C C    . GLU A 1 169 ? 111.18300 132.86100 136.06000 1.000 74.85617  ? 169 GLU A C    1 
ATOM   698  O O    . GLU A 1 169 ? 110.60700 132.02100 135.36200 1.000 74.86198  ? 169 GLU A O    1 
ATOM   699  C CB   . GLU A 1 169 ? 110.55200 132.21300 138.38500 1.000 74.80664  ? 169 GLU A CB   1 
ATOM   700  C CG   . GLU A 1 169 ? 110.91100 132.39700 139.85100 1.000 75.66402  ? 169 GLU A CG   1 
ATOM   701  C CD   . GLU A 1 169 ? 109.73000 132.17500 140.77200 1.000 78.02251  ? 169 GLU A CD   1 
ATOM   702  O OE1  . GLU A 1 169 ? 108.70700 131.63100 140.30800 1.000 77.96929  ? 169 GLU A OE1  1 
ATOM   703  O OE2  . GLU A 1 169 ? 109.82400 132.54400 141.96200 1.000 78.14005  ? 169 GLU A OE2  1 
ATOM   704  N N    . ILE A 1 170 ? 111.34500 134.12400 135.67100 1.000 61.82123  ? 170 ILE A N    1 
ATOM   705  C CA   . ILE A 1 170 ? 110.95100 134.55900 134.33600 1.000 61.19749  ? 170 ILE A CA   1 
ATOM   706  C C    . ILE A 1 170 ? 112.06600 134.31400 133.32400 1.000 64.59800  ? 170 ILE A C    1 
ATOM   707  O O    . ILE A 1 170 ? 111.79300 134.07500 132.13800 1.000 66.59134  ? 170 ILE A O    1 
ATOM   708  C CB   . ILE A 1 170 ? 110.55100 136.04300 134.36900 1.000 60.93186  ? 170 ILE A CB   1 
ATOM   709  C CG1  . ILE A 1 170 ? 109.26900 136.23300 135.18100 1.000 60.50414  ? 170 ILE A CG1  1 
ATOM   710  C CG2  . ILE A 1 170 ? 110.38200 136.58400 132.95900 1.000 62.09415  ? 170 ILE A CG2  1 
ATOM   711  C CD1  . ILE A 1 170 ? 109.27300 137.47600 136.03900 1.000 61.98706  ? 170 ILE A CD1  1 
ATOM   712  N N    . PHE A 1 171 ? 113.32100 134.35600 133.78000 1.000 60.71074  ? 171 PHE A N    1 
ATOM   713  C CA   . PHE A 1 171 ? 114.46200 134.11500 132.91100 1.000 58.10918  ? 171 PHE A CA   1 
ATOM   714  C C    . PHE A 1 171 ? 114.53900 132.65900 132.48100 1.000 55.09255  ? 171 PHE A C    1 
ATOM   715  O O    . PHE A 1 171 ? 115.17600 132.35600 131.46800 1.000 59.20808  ? 171 PHE A O    1 
ATOM   716  C CB   . PHE A 1 171 ? 115.74800 134.54100 133.62800 1.000 56.60903  ? 171 PHE A CB   1 
ATOM   717  C CG   . PHE A 1 171 ? 117.00200 134.30400 132.83500 1.000 57.54127  ? 171 PHE A CG   1 
ATOM   718  C CD1  . PHE A 1 171 ? 117.63400 133.07200 132.85800 1.000 59.37319  ? 171 PHE A CD1  1 
ATOM   719  C CD2  . PHE A 1 171 ? 117.55000 135.31600 132.06900 1.000 58.79508  ? 171 PHE A CD2  1 
ATOM   720  C CE1  . PHE A 1 171 ? 118.78500 132.85500 132.12900 1.000 56.99660  ? 171 PHE A CE1  1 
ATOM   721  C CE2  . PHE A 1 171 ? 118.70100 135.10300 131.33900 1.000 60.38102  ? 171 PHE A CE2  1 
ATOM   722  C CZ   . PHE A 1 171 ? 119.31900 133.87100 131.36900 1.000 58.57599  ? 171 PHE A CZ   1 
ATOM   723  N N    . CYS A 1 172 ? 113.89400 131.75900 133.22100 1.000 47.66451  ? 172 CYS A N    1 
ATOM   724  C CA   . CYS A 1 172 ? 113.87300 130.34700 132.87300 1.000 51.81375  ? 172 CYS A CA   1 
ATOM   725  C C    . CYS A 1 172 ? 112.73600 129.99200 131.92700 1.000 51.93497  ? 172 CYS A C    1 
ATOM   726  O O    . CYS A 1 172 ? 112.76500 128.91700 131.31900 1.000 53.36818  ? 172 CYS A O    1 
ATOM   727  C CB   . CYS A 1 172 ? 113.76700 129.49200 134.13900 1.000 52.97134  ? 172 CYS A CB   1 
ATOM   728  S SG   . CYS A 1 172 ? 115.31700 129.31100 135.04800 1.000 58.39827  ? 172 CYS A SG   1 
ATOM   729  N N    . THR A 1 173 ? 111.73800 130.86500 131.79300 1.000 48.52504  ? 173 THR A N    1 
ATOM   730  C CA   . THR A 1 173 ? 110.67800 130.67400 130.81200 1.000 46.36110  ? 173 THR A CA   1 
ATOM   731  C C    . THR A 1 173 ? 110.96100 131.40000 129.50500 1.000 46.48025  ? 173 THR A C    1 
ATOM   732  O O    . THR A 1 173 ? 110.62400 130.88900 128.42200 1.000 52.26966  ? 173 THR A O    1 
ATOM   733  C CB   . THR A 1 173 ? 109.34600 131.16100 131.38800 1.000 47.67322  ? 173 THR A CB   1 
ATOM   734  O OG1  . THR A 1 173 ? 109.03000 130.40700 132.56500 1.000 49.45829  ? 173 THR A OG1  1 
ATOM   735  C CG2  . THR A 1 173 ? 108.24000 130.99200 130.37800 1.000 50.77312  ? 173 THR A CG2  1 
ATOM   736  N N    . LEU A 1 174 ? 111.65200 132.54200 129.57000 1.000 41.89406  ? 174 LEU A N    1 
ATOM   737  C CA   . LEU A 1 174 ? 112.01500 133.20800 128.32800 1.000 38.47208  ? 174 LEU A CA   1 
ATOM   738  C C    . LEU A 1 174 ? 113.07800 132.42700 127.57600 1.000 38.89011  ? 174 LEU A C    1 
ATOM   739  O O    . LEU A 1 174 ? 113.16400 132.53400 126.34700 1.000 44.85713  ? 174 LEU A O    1 
ATOM   740  C CB   . LEU A 1 174 ? 112.51700 134.62100 128.61600 1.000 39.43352  ? 174 LEU A CB   1 
ATOM   741  C CG   . LEU A 1 174 ? 111.51200 135.61900 129.18800 1.000 40.25711  ? 174 LEU A CG   1 
ATOM   742  C CD1  . LEU A 1 174 ? 112.22400 136.89800 129.59000 1.000 44.05444  ? 174 LEU A CD1  1 
ATOM   743  C CD2  . LEU A 1 174 ? 110.40600 135.90900 128.18800 1.000 41.85333  ? 174 LEU A CD2  1 
ATOM   744  N N    . SER A 1 175 ? 113.77600 131.52500 128.26400 1.000 34.53097  ? 175 SER A N    1 
ATOM   745  C CA   . SER A 1 175 ? 114.78000 130.70500 127.60500 1.000 35.16615  ? 175 SER A CA   1 
ATOM   746  C C    . SER A 1 175 ? 114.15100 129.49100 126.94500 1.000 34.29690  ? 175 SER A C    1 
ATOM   747  O O    . SER A 1 175 ? 114.59700 129.07900 125.87100 1.000 35.94041  ? 175 SER A O    1 
ATOM   748  C CB   . SER A 1 175 ? 115.84400 130.26500 128.60800 1.000 35.21158  ? 175 SER A CB   1 
ATOM   749  O OG   . SER A 1 175 ? 116.13800 131.30600 129.52000 1.000 46.45891  ? 175 SER A OG   1 
ATOM   750  N N    . ILE A 1 176 ? 113.08800 128.94400 127.53300 1.000 25.22672  ? 176 ILE A N    1 
ATOM   751  C CA   . ILE A 1 176 ? 112.34900 127.89400 126.84800 1.000 29.67087  ? 176 ILE A CA   1 
ATOM   752  C C    . ILE A 1 176 ? 111.68400 128.45700 125.60100 1.000 31.55795  ? 176 ILE A C    1 
ATOM   753  O O    . ILE A 1 176 ? 111.70400 127.82800 124.53400 1.000 31.98376  ? 176 ILE A O    1 
ATOM   754  C CB   . ILE A 1 176 ? 111.32400 127.25200 127.80100 1.000 28.93003  ? 176 ILE A CB   1 
ATOM   755  C CG1  . ILE A 1 176 ? 112.04000 126.60100 128.98500 1.000 35.65869  ? 176 ILE A CG1  1 
ATOM   756  C CG2  . ILE A 1 176 ? 110.46900 126.23600 127.06400 1.000 30.95267  ? 176 ILE A CG2  1 
ATOM   757  C CD1  . ILE A 1 176 ? 111.30300 125.42800 129.57700 1.000 32.08223  ? 176 ILE A CD1  1 
ATOM   758  N N    . PHE A 1 177 ? 111.18800 129.69600 125.68000 1.000 32.70051  ? 177 PHE A N    1 
ATOM   759  C CA   . PHE A 1 177 ? 110.59100 130.30400 124.49300 1.000 20.73183  ? 177 PHE A CA   1 
ATOM   760  C C    . PHE A 1 177 ? 111.63800 130.54800 123.40900 1.000 29.31691  ? 177 PHE A C    1 
ATOM   761  O O    . PHE A 1 177 ? 111.41800 130.21300 122.23300 1.000 37.83032  ? 177 PHE A O    1 
ATOM   762  C CB   . PHE A 1 177 ? 109.89100 131.60900 124.87600 1.000 26.65517  ? 177 PHE A CB   1 
ATOM   763  C CG   . PHE A 1 177 ? 109.42300 132.41700 123.69900 1.000 37.03779  ? 177 PHE A CG   1 
ATOM   764  C CD1  . PHE A 1 177 ? 108.27200 132.06900 123.01400 1.000 39.05314  ? 177 PHE A CD1  1 
ATOM   765  C CD2  . PHE A 1 177 ? 110.13200 133.53000 123.28100 1.000 32.79524  ? 177 PHE A CD2  1 
ATOM   766  C CE1  . PHE A 1 177 ? 107.84100 132.81000 121.93100 1.000 30.86413  ? 177 PHE A CE1  1 
ATOM   767  C CE2  . PHE A 1 177 ? 109.70600 134.27400 122.20000 1.000 32.63740  ? 177 PHE A CE2  1 
ATOM   768  C CZ   . PHE A 1 177 ? 108.55700 133.91200 121.52400 1.000 31.89205  ? 177 PHE A CZ   1 
ATOM   769  N N    . CYS A 1 178 ? 112.79900 131.08900 123.78900 1.000 34.04454  ? 178 CYS A N    1 
ATOM   770  C CA   . CYS A 1 178 ? 113.84000 131.38000 122.80800 1.000 28.00661  ? 178 CYS A CA   1 
ATOM   771  C C    . CYS A 1 178 ? 114.37400 130.10400 122.16400 1.000 30.27272  ? 178 CYS A C    1 
ATOM   772  O O    . CYS A 1 178 ? 114.51900 130.03100 120.93700 1.000 41.19465  ? 178 CYS A O    1 
ATOM   773  C CB   . CYS A 1 178 ? 114.96800 132.17300 123.46600 1.000 26.67209  ? 178 CYS A CB   1 
ATOM   774  S SG   . CYS A 1 178 ? 114.52000 133.87000 123.88900 1.000 46.31959  ? 178 CYS A SG   1 
ATOM   775  N N    . ILE A 1 179 ? 114.72000 129.10300 122.97800 1.000 26.18653  ? 179 ILE A N    1 
ATOM   776  C CA   . ILE A 1 179 ? 115.23700 127.84800 122.44000 1.000 25.96832  ? 179 ILE A CA   1 
ATOM   777  C C    . ILE A 1 179 ? 114.21500 127.18200 121.52700 1.000 29.21595  ? 179 ILE A C    1 
ATOM   778  O O    . ILE A 1 179 ? 114.56900 126.66100 120.46400 1.000 34.76992  ? 179 ILE A O    1 
ATOM   779  C CB   . ILE A 1 179 ? 115.68300 126.91400 123.57900 1.000 35.61168  ? 179 ILE A CB   1 
ATOM   780  C CG1  . ILE A 1 179 ? 116.69800 127.62400 124.47500 1.000 32.12759  ? 179 ILE A CG1  1 
ATOM   781  C CG2  . ILE A 1 179 ? 116.28500 125.63800 123.01800 1.000 31.84804  ? 179 ILE A CG2  1 
ATOM   782  C CD1  . ILE A 1 179 ? 117.98800 127.98200 123.77000 1.000 30.11995  ? 179 ILE A CD1  1 
ATOM   783  N N    . GLY A 1 180 ? 112.94000 127.15400 121.92900 1.000 26.37594  ? 180 GLY A N    1 
ATOM   784  C CA   . GLY A 1 180 ? 111.92500 126.60000 121.04400 1.000 23.30653  ? 180 GLY A CA   1 
ATOM   785  C C    . GLY A 1 180 ? 111.90100 127.28400 119.69100 1.000 29.10812  ? 180 GLY A C    1 
ATOM   786  O O    . GLY A 1 180 ? 111.97300 126.62900 118.64100 1.000 31.55355  ? 180 GLY A O    1 
ATOM   787  N N    . PHE A 1 181 ? 111.78700 128.61600 119.69600 1.000 24.78854  ? 181 PHE A N    1 
ATOM   788  C CA   . PHE A 1 181 ? 111.77900 129.36000 118.43900 1.000 25.00352  ? 181 PHE A CA   1 
ATOM   789  C C    . PHE A 1 181 ? 113.00000 129.02700 117.58400 1.000 26.94111  ? 181 PHE A C    1 
ATOM   790  O O    . PHE A 1 181 ? 112.87500 128.69900 116.39600 1.000 30.56242  ? 181 PHE A O    1 
ATOM   791  C CB   . PHE A 1 181 ? 111.70600 130.86200 118.73000 1.000 20.41955  ? 181 PHE A CB   1 
ATOM   792  C CG   . PHE A 1 181 ? 111.72900 131.72400 117.49800 1.000 28.60648  ? 181 PHE A CG   1 
ATOM   793  C CD1  . PHE A 1 181 ? 112.92900 132.13900 116.94800 1.000 34.82428  ? 181 PHE A CD1  1 
ATOM   794  C CD2  . PHE A 1 181 ? 110.55100 132.12000 116.89000 1.000 30.01840  ? 181 PHE A CD2  1 
ATOM   795  C CE1  . PHE A 1 181 ? 112.95200 132.92900 115.81700 1.000 30.25146  ? 181 PHE A CE1  1 
ATOM   796  C CE2  . PHE A 1 181 ? 110.56900 132.91000 115.75800 1.000 27.54414  ? 181 PHE A CE2  1 
ATOM   797  C CZ   . PHE A 1 181 ? 111.77000 133.31400 115.22200 1.000 25.96871  ? 181 PHE A CZ   1 
ATOM   798  N N    . LEU A 1 182 ? 114.19400 129.11700 118.17500 1.000 26.67935  ? 182 LEU A N    1 
ATOM   799  C CA   . LEU A 1 182 ? 115.42500 128.91900 117.41400 1.000 22.96286  ? 182 LEU A CA   1 
ATOM   800  C C    . LEU A 1 182 ? 115.50700 127.51300 116.83200 1.000 28.26957  ? 182 LEU A C    1 
ATOM   801  O O    . LEU A 1 182 ? 115.85400 127.33500 115.65700 1.000 33.83403  ? 182 LEU A O    1 
ATOM   802  C CB   . LEU A 1 182 ? 116.64100 129.21200 118.29300 1.000 29.55604  ? 182 LEU A CB   1 
ATOM   803  C CG   . LEU A 1 182 ? 116.91400 130.68400 118.60500 1.000 31.18056  ? 182 LEU A CG   1 
ATOM   804  C CD1  . LEU A 1 182 ? 117.92300 130.82000 119.72700 1.000 33.20041  ? 182 LEU A CD1  1 
ATOM   805  C CD2  . LEU A 1 182 ? 117.40200 131.41400 117.36500 1.000 32.65325  ? 182 LEU A CD2  1 
ATOM   806  N N    . ALA A 1 183 ? 115.21500 126.49300 117.64400 1.000 31.18537  ? 183 ALA A N    1 
ATOM   807  C CA   . ALA A 1 183 ? 115.34200 125.12900 117.15000 1.000 27.77846  ? 183 ALA A CA   1 
ATOM   808  C C    . ALA A 1 183 ? 114.31900 124.81800 116.06800 1.000 32.15455  ? 183 ALA A C    1 
ATOM   809  O O    . ALA A 1 183 ? 114.63800 124.09600 115.11500 1.000 40.63886  ? 183 ALA A O    1 
ATOM   810  C CB   . ALA A 1 183 ? 115.20500 124.14000 118.30700 1.000 22.06214  ? 183 ALA A CB   1 
ATOM   811  N N    . THR A 1 184 ? 113.13500 125.43800 116.11100 1.000 28.80756  ? 184 THR A N    1 
ATOM   812  C CA   . THR A 1 184 ? 112.20400 125.14000 115.02900 1.000 26.73703  ? 184 THR A CA   1 
ATOM   813  C C    . THR A 1 184 ? 112.57100 125.89600 113.76100 1.000 29.97721  ? 184 THR A C    1 
ATOM   814  O O    . THR A 1 184 ? 112.43100 125.35400 112.65200 1.000 29.33640  ? 184 THR A O    1 
ATOM   815  C CB   . THR A 1 184 ? 110.77200 125.47800 115.44500 1.000 31.32377  ? 184 THR A CB   1 
ATOM   816  O OG1  . THR A 1 184 ? 110.56300 125.08000 116.80300 1.000 31.97509  ? 184 THR A OG1  1 
ATOM   817  C CG2  . THR A 1 184 ? 109.77600 124.75300 114.55400 1.000 28.05438  ? 184 THR A CG2  1 
ATOM   818  N N    . PHE A 1 185 ? 113.11500 127.10900 113.90000 1.000 31.11552  ? 185 PHE A N    1 
ATOM   819  C CA   . PHE A 1 185 ? 113.54900 127.82400 112.70700 1.000 28.57708  ? 185 PHE A CA   1 
ATOM   820  C C    . PHE A 1 185 ? 114.68300 127.07400 112.03200 1.000 32.14444  ? 185 PHE A C    1 
ATOM   821  O O    . PHE A 1 185 ? 114.70200 126.93100 110.80400 1.000 38.17947  ? 185 PHE A O    1 
ATOM   822  C CB   . PHE A 1 185 ? 113.97800 129.25000 113.05200 1.000 31.89958  ? 185 PHE A CB   1 
ATOM   823  C CG   . PHE A 1 185 ? 113.73600 130.24100 111.94300 1.000 36.60075  ? 185 PHE A CG   1 
ATOM   824  C CD1  . PHE A 1 185 ? 112.49700 130.33600 111.33600 1.000 34.62368  ? 185 PHE A CD1  1 
ATOM   825  C CD2  . PHE A 1 185 ? 114.75500 131.07000 111.50200 1.000 34.18083  ? 185 PHE A CD2  1 
ATOM   826  C CE1  . PHE A 1 185 ? 112.27800 131.24300 110.31500 1.000 36.56792  ? 185 PHE A CE1  1 
ATOM   827  C CE2  . PHE A 1 185 ? 114.54000 131.97700 110.48300 1.000 32.38958  ? 185 PHE A CE2  1 
ATOM   828  C CZ   . PHE A 1 185 ? 113.30100 132.06300 109.89000 1.000 35.47766  ? 185 PHE A CZ   1 
ATOM   829  N N    . MET A 1 186 ? 115.64200 126.58700 112.82200 1.000 38.75876  ? 186 MET A N    1 
ATOM   830  C CA   . MET A 1 186 ? 116.74800 125.83500 112.24500 1.000 31.48996  ? 186 MET A CA   1 
ATOM   831  C C    . MET A 1 186 ? 116.27300 124.52900 111.61700 1.000 31.80951  ? 186 MET A C    1 
ATOM   832  O O    . MET A 1 186 ? 116.78400 124.11800 110.56900 1.000 32.60759  ? 186 MET A O    1 
ATOM   833  C CB   . MET A 1 186 ? 117.81200 125.57300 113.30800 1.000 31.68415  ? 186 MET A CB   1 
ATOM   834  C CG   . MET A 1 186 ? 119.14900 126.22800 113.00500 1.000 36.01414  ? 186 MET A CG   1 
ATOM   835  S SD   . MET A 1 186 ? 119.14200 128.01600 113.22700 1.000 59.92575  ? 186 MET A SD   1 
ATOM   836  C CE   . MET A 1 186 ? 119.26300 128.13700 115.00800 1.000 41.59916  ? 186 MET A CE   1 
ATOM   837  N N    . LYS A 1 187 ? 115.29400 123.85700 112.23300 1.000 33.19732  ? 187 LYS A N    1 
ATOM   838  C CA   . LYS A 1 187 ? 114.81600 122.61200 111.64200 1.000 33.73380  ? 187 LYS A CA   1 
ATOM   839  C C    . LYS A 1 187 ? 114.03000 122.83800 110.35600 1.000 39.61716  ? 187 LYS A C    1 
ATOM   840  O O    . LYS A 1 187 ? 113.92200 121.91300 109.54500 1.000 40.44035  ? 187 LYS A O    1 
ATOM   841  C CB   . LYS A 1 187 ? 113.96600 121.81200 112.62600 1.000 35.51333  ? 187 LYS A CB   1 
ATOM   842  C CG   . LYS A 1 187 ? 112.49500 121.76400 112.27300 1.000 37.63183  ? 187 LYS A CG   1 
ATOM   843  C CD   . LYS A 1 187 ? 111.69600 121.11500 113.38100 1.000 37.36597  ? 187 LYS A CD   1 
ATOM   844  C CE   . LYS A 1 187 ? 112.17300 119.69300 113.62100 1.000 38.75160  ? 187 LYS A CE   1 
ATOM   845  N NZ   . LYS A 1 187 ? 111.23200 118.91700 114.47500 1.000 46.97275  ? 187 LYS A NZ   1 
ATOM   846  N N    . LEU A 1 188 ? 113.48600 124.04000 110.13900 1.000 44.10325  ? 188 LEU A N    1 
ATOM   847  C CA   . LEU A 1 188 ? 112.68800 124.27500 108.93700 1.000 37.93687  ? 188 LEU A CA   1 
ATOM   848  C C    . LEU A 1 188 ? 113.51000 124.61900 107.70100 1.000 41.08575  ? 188 LEU A C    1 
ATOM   849  O O    . LEU A 1 188 ? 112.96000 124.60700 106.59800 1.000 47.39456  ? 188 LEU A O    1 
ATOM   850  C CB   . LEU A 1 188 ? 111.66800 125.38800 109.17700 1.000 41.31099  ? 188 LEU A CB   1 
ATOM   851  C CG   . LEU A 1 188 ? 110.49800 125.06700 110.10700 1.000 38.72753  ? 188 LEU A CG   1 
ATOM   852  C CD1  . LEU A 1 188 ? 109.66100 126.30300 110.38300 1.000 37.83056  ? 188 LEU A CD1  1 
ATOM   853  C CD2  . LEU A 1 188 ? 109.64400 123.96800 109.50300 1.000 38.16075  ? 188 LEU A CD2  1 
ATOM   854  N N    . TYR A 1 189 ? 114.79600 124.93100 107.84000 1.000 52.46888  ? 189 TYR A N    1 
ATOM   855  C CA   . TYR A 1 189 ? 115.64200 125.16900 106.67700 1.000 52.11612  ? 189 TYR A CA   1 
ATOM   856  C C    . TYR A 1 189 ? 115.55900 124.00800 105.68500 1.000 54.97152  ? 189 TYR A C    1 
ATOM   857  O O    . TYR A 1 189 ? 115.37800 122.85500 106.09400 1.000 54.12293  ? 189 TYR A O    1 
ATOM   858  C CB   . TYR A 1 189 ? 117.08300 125.38200 107.14900 1.000 49.91712  ? 189 TYR A CB   1 
ATOM   859  C CG   . TYR A 1 189 ? 117.91900 126.30600 106.29300 1.000 53.36292  ? 189 TYR A CG   1 
ATOM   860  C CD1  . TYR A 1 189 ? 118.55500 125.83600 105.15200 1.000 54.58701  ? 189 TYR A CD1  1 
ATOM   861  C CD2  . TYR A 1 189 ? 118.12600 127.62500 106.66400 1.000 55.30556  ? 189 TYR A CD2  1 
ATOM   862  C CE1  . TYR A 1 189 ? 119.33300 126.67200 104.37800 1.000 56.36605  ? 189 TYR A CE1  1 
ATOM   863  C CE2  . TYR A 1 189 ? 118.90500 128.46700 105.89600 1.000 59.11167  ? 189 TYR A CE2  1 
ATOM   864  C CZ   . TYR A 1 189 ? 119.50900 127.98400 104.75600 1.000 60.52679  ? 189 TYR A CZ   1 
ATOM   865  O OH   . TYR A 1 189 ? 120.28700 128.81400 103.98400 1.000 58.45346  ? 189 TYR A OH   1 
ATOM   866  N N    . PRO A 1 190 ? 115.68800 124.28400 104.36900 1.000 59.32082  ? 190 PRO A N    1 
ATOM   867  C CA   . PRO A 1 190 ? 115.50100 123.20000 103.39000 1.000 57.90237  ? 190 PRO A CA   1 
ATOM   868  C C    . PRO A 1 190 ? 116.69500 122.24700 103.20100 1.000 57.99378  ? 190 PRO A C    1 
ATOM   869  O O    . PRO A 1 190 ? 116.51600 121.18800 102.61100 1.000 55.11812  ? 190 PRO A O    1 
ATOM   870  C CB   . PRO A 1 190 ? 115.20500 123.96200 102.08300 1.000 57.64731  ? 190 PRO A CB   1 
ATOM   871  C CG   . PRO A 1 190 ? 114.95200 125.37800 102.47700 1.000 57.05620  ? 190 PRO A CG   1 
ATOM   872  C CD   . PRO A 1 190 ? 115.78700 125.59000 103.69500 1.000 58.77568  ? 190 PRO A CD   1 
ATOM   873  N N    . SER A 1 191 ? 117.85400 122.59600 103.74600 1.000 62.99623  ? 191 SER A N    1 
ATOM   874  C CA   . SER A 1 191 ? 119.03200 121.73300 103.67200 1.000 61.92936  ? 191 SER A CA   1 
ATOM   875  C C    . SER A 1 191 ? 119.20200 120.86500 104.90600 1.000 62.53712  ? 191 SER A C    1 
ATOM   876  O O    . SER A 1 191 ? 120.08100 120.00900 104.92600 1.000 63.50904  ? 191 SER A O    1 
ATOM   877  C CB   . SER A 1 191 ? 120.28200 122.58600 103.51600 1.000 59.85860  ? 191 SER A CB   1 
ATOM   878  O OG   . SER A 1 191 ? 120.48900 123.40300 104.65400 1.000 60.10216  ? 191 SER A OG   1 
ATOM   879  N N    . MET A 1 192 ? 118.38800 121.08600 105.94100 1.000 57.95004  ? 192 MET A N    1 
ATOM   880  C CA   . MET A 1 192 ? 118.48900 120.32300 107.18300 1.000 52.30005  ? 192 MET A CA   1 
ATOM   881  C C    . MET A 1 192 ? 117.36600 119.33400 107.31900 1.000 53.98624  ? 192 MET A C    1 
ATOM   882  O O    . MET A 1 192 ? 117.21400 118.71900 108.36100 1.000 56.99976  ? 192 MET A O    1 
ATOM   883  C CB   . MET A 1 192 ? 118.44700 121.26300 108.37700 1.000 50.47774  ? 192 MET A CB   1 
ATOM   884  C CG   . MET A 1 192 ? 119.43200 122.41000 108.30700 1.000 55.46092  ? 192 MET A CG   1 
ATOM   885  S SD   . MET A 1 192 ? 120.95700 122.00300 109.16200 1.000 55.08555  ? 192 MET A SD   1 
ATOM   886  C CE   . MET A 1 192 ? 121.93300 121.35700 107.80900 1.000 54.96019  ? 192 MET A CE   1 
ATOM   887  N N    . LYS A 1 193 ? 116.57800 119.16100 106.27300 1.000 55.98283  ? 193 LYS A N    1 
ATOM   888  C CA   . LYS A 1 193 ? 115.41200 118.29000 106.35700 1.000 55.86838  ? 193 LYS A CA   1 
ATOM   889  C C    . LYS A 1 193 ? 115.73400 116.85000 106.68800 1.000 57.31996  ? 193 LYS A C    1 
ATOM   890  O O    . LYS A 1 193 ? 114.87700 116.12100 107.16600 1.000 61.80985  ? 193 LYS A O    1 
ATOM   891  C CB   . LYS A 1 193 ? 114.65200 118.32700 105.03800 1.000 55.96434  ? 193 LYS A CB   1 
ATOM   892  C CG   . LYS A 1 193 ? 113.31600 119.04600 105.11300 1.000 58.63129  ? 193 LYS A CG   1 
ATOM   893  C CD   . LYS A 1 193 ? 113.51100 120.54200 105.28400 1.000 58.12357  ? 193 LYS A CD   1 
ATOM   894  C CE   . LYS A 1 193 ? 112.17900 121.26200 105.40200 1.000 58.42515  ? 193 LYS A CE   1 
ATOM   895  N NZ   . LYS A 1 193 ? 111.35800 120.72600 106.52100 1.000 59.23809  ? 193 LYS A NZ   1 
ATOM   896  N N    . ALA A 1 194 ? 116.95400 116.42500 106.41500 1.000 56.79243  ? 194 ALA A N    1 
ATOM   897  C CA   . ALA A 1 194 ? 117.34800 115.05200 106.66600 1.000 55.12444  ? 194 ALA A CA   1 
ATOM   898  C C    . ALA A 1 194 ? 117.69300 114.79600 108.12800 1.000 57.51529  ? 194 ALA A C    1 
ATOM   899  O O    . ALA A 1 194 ? 117.67100 113.65300 108.57000 1.000 57.98374  ? 194 ALA A O    1 
ATOM   900  C CB   . ALA A 1 194 ? 118.52700 114.71000 105.78500 1.000 56.71941  ? 194 ALA A CB   1 
ATOM   901  N N    . TYR A 1 195 ? 118.00000 115.84800 108.88100 1.000 52.26011  ? 195 TYR A N    1 
ATOM   902  C CA   . TYR A 1 195 ? 118.39800 115.69300 110.28000 1.000 45.49690  ? 195 TYR A CA   1 
ATOM   903  C C    . TYR A 1 195 ? 117.30500 116.10200 111.25900 1.000 45.65043  ? 195 TYR A C    1 
ATOM   904  O O    . TYR A 1 195 ? 117.58500 116.73900 112.27800 1.000 51.92272  ? 195 TYR A O    1 
ATOM   905  C CB   . TYR A 1 195 ? 119.67200 116.48400 110.55000 1.000 48.61216  ? 195 TYR A CB   1 
ATOM   906  C CG   . TYR A 1 195 ? 120.81500 116.12800 109.63100 1.000 51.03628  ? 195 TYR A CG   1 
ATOM   907  C CD1  . TYR A 1 195 ? 121.54400 114.96200 109.81800 1.000 54.54670  ? 195 TYR A CD1  1 
ATOM   908  C CD2  . TYR A 1 195 ? 121.16900 116.95800 108.57600 1.000 53.35269  ? 195 TYR A CD2  1 
ATOM   909  C CE1  . TYR A 1 195 ? 122.59000 114.63100 108.98200 1.000 53.53527  ? 195 TYR A CE1  1 
ATOM   910  C CE2  . TYR A 1 195 ? 122.21500 116.63500 107.73400 1.000 56.49625  ? 195 TYR A CE2  1 
ATOM   911  C CZ   . TYR A 1 195 ? 122.92200 115.47000 107.94300 1.000 55.62886  ? 195 TYR A CZ   1 
ATOM   912  O OH   . TYR A 1 195 ? 123.96500 115.13800 107.11100 1.000 55.41176  ? 195 TYR A OH   1 
ATOM   913  N N    . GLU A 1 196 ? 116.04900 115.75800 110.98300 1.000 38.58314  ? 196 GLU A N    1 
ATOM   914  C CA   . GLU A 1 196 ? 114.96000 116.17700 111.85500 1.000 42.93999  ? 196 GLU A CA   1 
ATOM   915  C C    . GLU A 1 196 ? 114.89200 115.37800 113.14900 1.000 44.55647  ? 196 GLU A C    1 
ATOM   916  O O    . GLU A 1 196 ? 114.08600 115.71600 114.02100 1.000 49.89575  ? 196 GLU A O    1 
ATOM   917  C CB   . GLU A 1 196 ? 113.62300 116.06800 111.12300 1.000 43.03859  ? 196 GLU A CB   1 
ATOM   918  C CG   . GLU A 1 196 ? 113.44300 117.07900 110.01000 1.000 45.02386  ? 196 GLU A CG   1 
ATOM   919  C CD   . GLU A 1 196 ? 112.00300 117.52700 109.87000 1.000 53.45740  ? 196 GLU A CD   1 
ATOM   920  O OE1  . GLU A 1 196 ? 111.17100 117.11100 110.70200 1.000 53.21187  ? 196 GLU A OE1  1 
ATOM   921  O OE2  . GLU A 1 196 ? 111.70400 118.29600 108.93200 1.000 51.40080  ? 196 GLU A OE2  1 
ATOM   922  N N    . TYR A 1 197 ? 115.71300 114.34000 113.30000 1.000 35.37658  ? 197 TYR A N    1 
ATOM   923  C CA   . TYR A 1 197 ? 115.67000 113.49800 114.48700 1.000 29.29938  ? 197 TYR A CA   1 
ATOM   924  C C    . TYR A 1 197 ? 116.59300 113.97100 115.60400 1.000 31.02222  ? 197 TYR A C    1 
ATOM   925  O O    . TYR A 1 197 ? 116.41800 113.54400 116.75000 1.000 35.92079  ? 197 TYR A O    1 
ATOM   926  C CB   . TYR A 1 197 ? 115.99400 112.04500 114.10600 1.000 29.79972  ? 197 TYR A CB   1 
ATOM   927  C CG   . TYR A 1 197 ? 117.34900 111.85100 113.45900 1.000 26.47555  ? 197 TYR A CG   1 
ATOM   928  C CD1  . TYR A 1 197 ? 118.49700 111.71300 114.22500 1.000 31.31362  ? 197 TYR A CD1  1 
ATOM   929  C CD2  . TYR A 1 197 ? 117.47500 111.80300 112.07800 1.000 26.01986  ? 197 TYR A CD2  1 
ATOM   930  C CE1  . TYR A 1 197 ? 119.73200 111.54000 113.63300 1.000 30.78683  ? 197 TYR A CE1  1 
ATOM   931  C CE2  . TYR A 1 197 ? 118.70400 111.63100 111.47800 1.000 29.97661  ? 197 TYR A CE2  1 
ATOM   932  C CZ   . TYR A 1 197 ? 119.83000 111.50100 112.25900 1.000 36.32541  ? 197 TYR A CZ   1 
ATOM   933  O OH   . TYR A 1 197 ? 121.05600 111.32700 111.66200 1.000 35.24066  ? 197 TYR A OH   1 
ATOM   934  N N    . GLY A 1 198 ? 117.56500 114.83100 115.30600 1.000 27.97343  ? 198 GLY A N    1 
ATOM   935  C CA   . GLY A 1 198 ? 118.46100 115.35400 116.32200 1.000 23.49655  ? 198 GLY A CA   1 
ATOM   936  C C    . GLY A 1 198 ? 117.94000 116.59900 117.01400 1.000 27.43925  ? 198 GLY A C    1 
ATOM   937  O O    . GLY A 1 198 ? 118.20100 116.82900 118.20200 1.000 40.31965  ? 198 GLY A O    1 
ATOM   938  N N    . PHE A 1 199 ? 117.12400 117.37100 116.29300 1.000 28.06351  ? 199 PHE A N    1 
ATOM   939  C CA   . PHE A 1 199 ? 116.51300 118.55700 116.88100 1.000 28.11463  ? 199 PHE A CA   1 
ATOM   940  C C    . PHE A 1 199 ? 115.44600 118.18600 117.90100 1.000 29.88280  ? 199 PHE A C    1 
ATOM   941  O O    . PHE A 1 199 ? 115.28300 118.88400 118.91000 1.000 35.15215  ? 199 PHE A O    1 
ATOM   942  C CB   . PHE A 1 199 ? 115.91000 119.43100 115.78100 1.000 29.81349  ? 199 PHE A CB   1 
ATOM   943  C CG   . PHE A 1 199 ? 116.93300 120.10100 114.90800 1.000 34.45976  ? 199 PHE A CG   1 
ATOM   944  C CD1  . PHE A 1 199 ? 117.57000 121.25700 115.32200 1.000 29.07742  ? 199 PHE A CD1  1 
ATOM   945  C CD2  . PHE A 1 199 ? 117.25900 119.57200 113.67000 1.000 35.81823  ? 199 PHE A CD2  1 
ATOM   946  C CE1  . PHE A 1 199 ? 118.51100 121.87200 114.51800 1.000 29.02476  ? 199 PHE A CE1  1 
ATOM   947  C CE2  . PHE A 1 199 ? 118.20000 120.18400 112.86300 1.000 28.15351  ? 199 PHE A CE2  1 
ATOM   948  C CZ   . PHE A 1 199 ? 118.82600 121.33400 113.28800 1.000 22.93135  ? 199 PHE A CZ   1 
ATOM   949  N N    . ARG A 1 200 ? 114.75100 117.06800 117.68700 1.000 26.43546  ? 200 ARG A N    1 
ATOM   950  C CA   . ARG A 1 200 ? 113.75100 116.63600 118.65400 1.000 22.12475  ? 200 ARG A CA   1 
ATOM   951  C C    . ARG A 1 200 ? 114.41300 116.18800 119.95000 1.000 26.60770  ? 200 ARG A C    1 
ATOM   952  O O    . ARG A 1 200 ? 113.93500 116.51300 121.04500 1.000 32.51124  ? 200 ARG A O    1 
ATOM   953  C CB   . ARG A 1 200 ? 112.91500 115.50500 118.05700 1.000 28.24644  ? 200 ARG A CB   1 
ATOM   954  C CG   . ARG A 1 200 ? 112.12500 115.91000 116.82900 1.000 35.59921  ? 200 ARG A CG   1 
ATOM   955  C CD   . ARG A 1 200 ? 111.11700 114.84600 116.43700 1.000 35.83791  ? 200 ARG A CD   1 
ATOM   956  N NE   . ARG A 1 200 ? 111.19600 114.53300 115.01500 1.000 37.59628  ? 200 ARG A NE   1 
ATOM   957  C CZ   . ARG A 1 200 ? 111.48500 113.33500 114.52500 1.000 40.34887  ? 200 ARG A CZ   1 
ATOM   958  N NH1  . ARG A 1 200 ? 111.72800 112.30400 115.31600 1.000 35.88099  ? 200 ARG A NH1  1 
ATOM   959  N NH2  . ARG A 1 200 ? 111.53300 113.16900 113.20700 1.000 35.84563  ? 200 ARG A NH2  1 
ATOM   960  N N    . VAL A 1 201 ? 115.53900 115.47900 119.84400 1.000 16.61058  ? 201 VAL A N    1 
ATOM   961  C CA   . VAL A 1 201 ? 116.27100 115.07400 121.03900 1.000 27.37096  ? 201 VAL A CA   1 
ATOM   962  C C    . VAL A 1 201 ? 116.80200 116.30000 121.76800 1.000 24.74168  ? 201 VAL A C    1 
ATOM   963  O O    . VAL A 1 201 ? 116.70800 116.40000 122.99900 1.000 27.88467  ? 201 VAL A O    1 
ATOM   964  C CB   . VAL A 1 201 ? 117.40700 114.10200 120.66200 1.000 22.54782  ? 201 VAL A CB   1 
ATOM   965  C CG1  . VAL A 1 201 ? 118.24100 113.74900 121.88400 1.000 23.46581  ? 201 VAL A CG1  1 
ATOM   966  C CG2  . VAL A 1 201 ? 116.84700 112.85200 120.01200 1.000 15.05685  ? 201 VAL A CG2  1 
ATOM   967  N N    . PHE A 1 202 ? 117.32000 117.27600 121.01800 1.000 11.34843  ? 202 PHE A N    1 
ATOM   968  C CA   . PHE A 1 202 ? 117.83700 118.48800 121.64500 1.000 16.89740  ? 202 PHE A CA   1 
ATOM   969  C C    . PHE A 1 202 ? 116.74200 119.20800 122.42500 1.000 20.01245  ? 202 PHE A C    1 
ATOM   970  O O    . PHE A 1 202 ? 116.92200 119.56000 123.60200 1.000 22.05311  ? 202 PHE A O    1 
ATOM   971  C CB   . PHE A 1 202 ? 118.43500 119.39500 120.56400 1.000 19.69659  ? 202 PHE A CB   1 
ATOM   972  C CG   . PHE A 1 202 ? 119.02900 120.67300 121.08600 1.000 21.22677  ? 202 PHE A CG   1 
ATOM   973  C CD1  . PHE A 1 202 ? 118.22300 121.75900 121.38700 1.000 22.00756  ? 202 PHE A CD1  1 
ATOM   974  C CD2  . PHE A 1 202 ? 120.39500 120.79500 121.26000 1.000 21.17912  ? 202 PHE A CD2  1 
ATOM   975  C CE1  . PHE A 1 202 ? 118.76700 122.93200 121.86100 1.000 19.82041  ? 202 PHE A CE1  1 
ATOM   976  C CE2  . PHE A 1 202 ? 120.94500 121.96800 121.73500 1.000 23.46949  ? 202 PHE A CE2  1 
ATOM   977  C CZ   . PHE A 1 202 ? 120.13100 123.03700 122.03500 1.000 23.81502  ? 202 PHE A CZ   1 
ATOM   978  N N    . LEU A 1 203 ? 115.57500 119.38700 121.80100 1.000 18.78287  ? 203 LEU A N    1 
ATOM   979  C CA   . LEU A 1 203 ? 114.50900 120.14200 122.44800 1.000 19.64857  ? 203 LEU A CA   1 
ATOM   980  C C    . LEU A 1 203 ? 113.95700 119.39700 123.65600 1.000 22.01625  ? 203 LEU A C    1 
ATOM   981  O O    . LEU A 1 203 ? 113.71800 120.00200 124.71200 1.000 29.68519  ? 203 LEU A O    1 
ATOM   982  C CB   . LEU A 1 203 ? 113.40000 120.43700 121.44000 1.000 21.76408  ? 203 LEU A CB   1 
ATOM   983  C CG   . LEU A 1 203 ? 112.51000 121.65400 121.69500 1.000 24.40901  ? 203 LEU A CG   1 
ATOM   984  C CD1  . LEU A 1 203 ? 113.34500 122.86700 122.05900 1.000 25.09476  ? 203 LEU A CD1  1 
ATOM   985  C CD2  . LEU A 1 203 ? 111.65500 121.93800 120.47400 1.000 12.41362  ? 203 LEU A CD2  1 
ATOM   986  N N    . LEU A 1 204 ? 113.79400 118.07600 123.54300 1.000 20.28643  ? 204 LEU A N    1 
ATOM   987  C CA   . LEU A 1 204 ? 113.25600 117.32100 124.66700 1.000 14.71996  ? 204 LEU A CA   1 
ATOM   988  C C    . LEU A 1 204 ? 114.20700 117.34100 125.85400 1.000 17.41152  ? 204 LEU A C    1 
ATOM   989  O O    . LEU A 1 204 ? 113.77400 117.54800 126.99400 1.000 18.96089  ? 204 LEU A O    1 
ATOM   990  C CB   . LEU A 1 204 ? 112.95700 115.88300 124.24700 1.000 22.57647  ? 204 LEU A CB   1 
ATOM   991  C CG   . LEU A 1 204 ? 112.32100 115.02300 125.34000 1.000 19.96952  ? 204 LEU A CG   1 
ATOM   992  C CD1  . LEU A 1 204 ? 110.81000 115.04500 125.23100 1.000 22.17765  ? 204 LEU A CD1  1 
ATOM   993  C CD2  . LEU A 1 204 ? 112.84400 113.60100 125.28900 1.000 22.69315  ? 204 LEU A CD2  1 
ATOM   994  N N    . THR A 1 205 ? 115.50900 117.14500 125.61800 1.000 18.71262  ? 205 THR A N    1 
ATOM   995  C CA   . THR A 1 205 ? 116.42600 117.11100 126.75200 1.000 19.23788  ? 205 THR A CA   1 
ATOM   996  C C    . THR A 1 205 ? 116.56000 118.48500 127.39500 1.000 18.49933  ? 205 THR A C    1 
ATOM   997  O O    . THR A 1 205 ? 116.61400 118.59100 128.62700 1.000 24.44328  ? 205 THR A O    1 
ATOM   998  C CB   . THR A 1 205 ? 117.79500 116.56600 126.33700 1.000 17.46641  ? 205 THR A CB   1 
ATOM   999  O OG1  . THR A 1 205 ? 118.59300 117.61600 125.78000 1.000 32.29642  ? 205 THR A OG1  1 
ATOM   1000 C CG2  . THR A 1 205 ? 117.65000 115.43600 125.34000 1.000 17.65571  ? 205 THR A CG2  1 
ATOM   1001 N N    . TYR A 1 206 ? 116.57800 119.55600 126.59500 1.000 12.08280  ? 206 TYR A N    1 
ATOM   1002 C CA   . TYR A 1 206 ? 116.65900 120.88300 127.19800 1.000 18.17798  ? 206 TYR A CA   1 
ATOM   1003 C C    . TYR A 1 206 ? 115.42900 121.16900 128.05300 1.000 24.30405  ? 206 TYR A C    1 
ATOM   1004 O O    . TYR A 1 206 ? 115.54500 121.61000 129.20800 1.000 22.39386  ? 206 TYR A O    1 
ATOM   1005 C CB   . TYR A 1 206 ? 116.82000 121.95000 126.11600 1.000 18.20186  ? 206 TYR A CB   1 
ATOM   1006 C CG   . TYR A 1 206 ? 117.01300 123.34300 126.67100 1.000 23.56581  ? 206 TYR A CG   1 
ATOM   1007 C CD1  . TYR A 1 206 ? 118.27800 123.81700 126.98200 1.000 19.25364  ? 206 TYR A CD1  1 
ATOM   1008 C CD2  . TYR A 1 206 ? 115.92800 124.18100 126.89200 1.000 25.83953  ? 206 TYR A CD2  1 
ATOM   1009 C CE1  . TYR A 1 206 ? 118.45700 125.08500 127.49400 1.000 23.73306  ? 206 TYR A CE1  1 
ATOM   1010 C CE2  . TYR A 1 206 ? 116.09800 125.45100 127.40400 1.000 19.22032  ? 206 TYR A CE2  1 
ATOM   1011 C CZ   . TYR A 1 206 ? 117.36600 125.89800 127.70300 1.000 24.28222  ? 206 TYR A CZ   1 
ATOM   1012 O OH   . TYR A 1 206 ? 117.54600 127.16100 128.21100 1.000 25.59614  ? 206 TYR A OH   1 
ATOM   1013 N N    . CYS A 1 207 ? 114.23700 120.87400 127.52500 1.000 29.27912  ? 207 CYS A N    1 
ATOM   1014 C CA   . CYS A 1 207 ? 113.03300 121.19400 128.28100 1.000 19.30083  ? 207 CYS A CA   1 
ATOM   1015 C C    . CYS A 1 207 ? 112.90800 120.33000 129.52700 1.000 18.95113  ? 207 CYS A C    1 
ATOM   1016 O O    . CYS A 1 207 ? 112.46100 120.81900 130.57000 1.000 25.98183  ? 207 CYS A O    1 
ATOM   1017 C CB   . CYS A 1 207 ? 111.79700 121.04300 127.39700 1.000 22.69125  ? 207 CYS A CB   1 
ATOM   1018 S SG   . CYS A 1 207 ? 111.53700 122.41600 126.25300 1.000 42.14568  ? 207 CYS A SG   1 
ATOM   1019 N N    . TYR A 1 208 ? 113.33900 119.06800 129.46500 1.000 21.97618  ? 208 TYR A N    1 
ATOM   1020 C CA   . TYR A 1 208 ? 113.24000 118.22300 130.64800 1.000 22.23724  ? 208 TYR A CA   1 
ATOM   1021 C C    . TYR A 1 208 ? 114.23900 118.64800 131.71600 1.000 24.65269  ? 208 TYR A C    1 
ATOM   1022 O O    . TYR A 1 208 ? 113.88700 118.73500 132.89900 1.000 27.00475  ? 208 TYR A O    1 
ATOM   1023 C CB   . TYR A 1 208 ? 113.44900 116.75700 130.27500 1.000 24.51510  ? 208 TYR A CB   1 
ATOM   1024 C CG   . TYR A 1 208 ? 113.36200 115.82700 131.46200 1.000 29.78297  ? 208 TYR A CG   1 
ATOM   1025 C CD1  . TYR A 1 208 ? 112.13500 115.48800 132.01200 1.000 25.31249  ? 208 TYR A CD1  1 
ATOM   1026 C CD2  . TYR A 1 208 ? 114.50600 115.29800 132.04100 1.000 29.20826  ? 208 TYR A CD2  1 
ATOM   1027 C CE1  . TYR A 1 208 ? 112.04900 114.64500 133.09800 1.000 23.15211  ? 208 TYR A CE1  1 
ATOM   1028 C CE2  . TYR A 1 208 ? 114.42900 114.45400 133.12800 1.000 26.92925  ? 208 TYR A CE2  1 
ATOM   1029 C CZ   . TYR A 1 208 ? 113.19700 114.13100 133.65200 1.000 27.43479  ? 208 TYR A CZ   1 
ATOM   1030 O OH   . TYR A 1 208 ? 113.11400 113.28900 134.73500 1.000 32.65701  ? 208 TYR A OH   1 
ATOM   1031 N N    . ILE A 1 209 ? 115.47900 118.95200 131.32100 1.000 24.80797  ? 209 ILE A N    1 
ATOM   1032 C CA   . ILE A 1 209 ? 116.48100 119.34500 132.30300 1.000 19.68279  ? 209 ILE A CA   1 
ATOM   1033 C C    . ILE A 1 209 ? 116.23700 120.74200 132.84400 1.000 25.68661  ? 209 ILE A C    1 
ATOM   1034 O O    . ILE A 1 209 ? 116.83000 121.11200 133.86300 1.000 35.58141  ? 209 ILE A O    1 
ATOM   1035 C CB   . ILE A 1 209 ? 117.90200 119.25300 131.70700 1.000 26.27887  ? 209 ILE A CB   1 
ATOM   1036 C CG1  . ILE A 1 209 ? 118.27000 117.79900 131.41600 1.000 27.66783  ? 209 ILE A CG1  1 
ATOM   1037 C CG2  . ILE A 1 209 ? 118.93000 119.86400 132.64500 1.000 23.69178  ? 209 ILE A CG2  1 
ATOM   1038 C CD1  . ILE A 1 209 ? 119.65500 117.63300 130.84700 1.000 24.35814  ? 209 ILE A CD1  1 
ATOM   1039 N N    . LEU A 1 210 ? 115.35400 121.51900 132.21800 1.000 35.47500  ? 210 LEU A N    1 
ATOM   1040 C CA   . LEU A 1 210 ? 115.00600 122.81200 132.79100 1.000 25.83378  ? 210 LEU A CA   1 
ATOM   1041 C C    . LEU A 1 210 ? 113.71900 122.79100 133.60100 1.000 28.66940  ? 210 LEU A C    1 
ATOM   1042 O O    . LEU A 1 210 ? 113.59900 123.55700 134.56200 1.000 35.53058  ? 210 LEU A O    1 
ATOM   1043 C CB   . LEU A 1 210 ? 114.88500 123.87500 131.69400 1.000 29.64163  ? 210 LEU A CB   1 
ATOM   1044 C CG   . LEU A 1 210 ? 115.57600 125.20400 132.00500 1.000 30.12716  ? 210 LEU A CG   1 
ATOM   1045 C CD1  . LEU A 1 210 ? 116.92200 124.96800 132.66300 1.000 29.66845  ? 210 LEU A CD1  1 
ATOM   1046 C CD2  . LEU A 1 210 ? 115.73100 126.04000 130.74900 1.000 35.64851  ? 210 LEU A CD2  1 
ATOM   1047 N N    . ILE A 1 211 ? 112.75300 121.93500 133.25600 1.000 36.24895  ? 211 ILE A N    1 
ATOM   1048 C CA   . ILE A 1 211 ? 111.51300 121.85900 134.02500 1.000 22.82598  ? 211 ILE A CA   1 
ATOM   1049 C C    . ILE A 1 211 ? 111.56700 120.83800 135.15300 1.000 33.50759  ? 211 ILE A C    1 
ATOM   1050 O O    . ILE A 1 211 ? 110.65300 120.81100 135.99000 1.000 35.89588  ? 211 ILE A O    1 
ATOM   1051 C CB   . ILE A 1 211 ? 110.31800 121.54300 133.10400 1.000 26.59626  ? 211 ILE A CB   1 
ATOM   1052 C CG1  . ILE A 1 211 ? 110.30900 122.48600 131.90100 1.000 28.12671  ? 211 ILE A CG1  1 
ATOM   1053 C CG2  . ILE A 1 211 ? 109.01100 121.65000 133.86500 1.000 32.66162  ? 211 ILE A CG2  1 
ATOM   1054 C CD1  . ILE A 1 211 ? 109.36500 122.06500 130.80300 1.000 30.53719  ? 211 ILE A CD1  1 
ATOM   1055 N N    . SER A 1 212 ? 112.60800 120.00700 135.21800 1.000 45.01277  ? 212 SER A N    1 
ATOM   1056 C CA   . SER A 1 212 ? 112.65600 118.96100 136.23200 1.000 37.09203  ? 212 SER A CA   1 
ATOM   1057 C C    . SER A 1 212 ? 113.36500 119.38600 137.51100 1.000 43.70973  ? 212 SER A C    1 
ATOM   1058 O O    . SER A 1 212 ? 113.01300 118.89900 138.59200 1.000 47.24268  ? 212 SER A O    1 
ATOM   1059 C CB   . SER A 1 212 ? 113.34300 117.71600 135.66500 1.000 34.13520  ? 212 SER A CB   1 
ATOM   1060 O OG   . SER A 1 212 ? 113.21900 116.61900 136.55000 1.000 44.64163  ? 212 SER A OG   1 
ATOM   1061 N N    . GLY A 1 213 ? 114.35100 120.27400 137.42400 1.000 51.31662  ? 213 GLY A N    1 
ATOM   1062 C CA   . GLY A 1 213 ? 115.09000 120.68500 138.60200 1.000 52.03269  ? 213 GLY A CA   1 
ATOM   1063 C C    . GLY A 1 213 ? 114.80000 122.09200 139.08200 1.000 54.01917  ? 213 GLY A C    1 
ATOM   1064 O O    . GLY A 1 213 ? 115.58600 122.66300 139.84200 1.000 55.54979  ? 213 GLY A O    1 
ATOM   1065 N N    . PHE A 1 214 ? 113.67400 122.66400 138.65300 1.000 63.12196  ? 214 PHE A N    1 
ATOM   1066 C CA   . PHE A 1 214 ? 113.40500 124.06600 138.95900 1.000 64.28777  ? 214 PHE A CA   1 
ATOM   1067 C C    . PHE A 1 214 ? 113.10300 124.28300 140.43700 1.000 63.16311  ? 214 PHE A C    1 
ATOM   1068 O O    . PHE A 1 214 ? 113.59700 125.24400 141.03800 1.000 63.11477  ? 214 PHE A O    1 
ATOM   1069 C CB   . PHE A 1 214 ? 112.25000 124.58200 138.10500 1.000 63.48220  ? 214 PHE A CB   1 
ATOM   1070 C CG   . PHE A 1 214 ? 112.00300 126.05400 138.25800 1.000 65.84060  ? 214 PHE A CG   1 
ATOM   1071 C CD1  . PHE A 1 214 ? 113.02200 126.96500 138.04300 1.000 64.54570  ? 214 PHE A CD1  1 
ATOM   1072 C CD2  . PHE A 1 214 ? 110.75700 126.52600 138.63100 1.000 67.16704  ? 214 PHE A CD2  1 
ATOM   1073 C CE1  . PHE A 1 214 ? 112.80100 128.32000 138.18900 1.000 65.99896  ? 214 PHE A CE1  1 
ATOM   1074 C CE2  . PHE A 1 214 ? 110.52900 127.88000 138.77700 1.000 67.38958  ? 214 PHE A CE2  1 
ATOM   1075 C CZ   . PHE A 1 214 ? 111.55200 128.77800 138.55600 1.000 67.43480  ? 214 PHE A CZ   1 
ATOM   1076 N N    . ARG A 1 215 ? 112.30100 123.41100 141.04300 1.000 66.45554  ? 215 ARG A N    1 
ATOM   1077 C CA   . ARG A 1 215 ? 111.82000 123.63600 142.40000 1.000 68.57043  ? 215 ARG A CA   1 
ATOM   1078 C C    . ARG A 1 215 ? 112.73200 123.04600 143.46800 1.000 66.79993  ? 215 ARG A C    1 
ATOM   1079 O O    . ARG A 1 215 ? 112.35000 123.01700 144.64200 1.000 66.69404  ? 215 ARG A O    1 
ATOM   1080 C CB   . ARG A 1 215 ? 110.40600 123.07100 142.55900 1.000 66.52522  ? 215 ARG A CB   1 
ATOM   1081 C CG   . ARG A 1 215 ? 109.39900 123.61500 141.55600 1.000 67.29515  ? 215 ARG A CG   1 
ATOM   1082 C CD   . ARG A 1 215 ? 108.63500 122.49600 140.86300 1.000 68.16970  ? 215 ARG A CD   1 
ATOM   1083 N NE   . ARG A 1 215 ? 109.51700 121.57100 140.16200 1.000 67.25543  ? 215 ARG A NE   1 
ATOM   1084 C CZ   . ARG A 1 215 ? 109.78700 121.63300 138.86600 1.000 66.86596  ? 215 ARG A CZ   1 
ATOM   1085 N NH1  . ARG A 1 215 ? 109.25900 122.56800 138.09400 1.000 65.28506  ? 215 ARG A NH1  1 
ATOM   1086 N NH2  . ARG A 1 215 ? 110.60300 120.73100 138.32900 1.000 66.26538  ? 215 ARG A NH2  1 
ATOM   1087 N N    . THR A 1 216 ? 113.92100 122.58100 143.09500 1.000 66.85916  ? 216 THR A N    1 
ATOM   1088 C CA   . THR A 1 216 ? 114.85200 122.01000 144.06300 1.000 63.80551  ? 216 THR A CA   1 
ATOM   1089 C C    . THR A 1 216 ? 116.29300 122.47100 143.89200 1.000 65.30198  ? 216 THR A C    1 
ATOM   1090 O O    . THR A 1 216 ? 117.03100 122.48400 144.88100 1.000 68.81327  ? 216 THR A O    1 
ATOM   1091 C CB   . THR A 1 216 ? 114.81700 120.47800 144.00200 1.000 65.31492  ? 216 THR A CB   1 
ATOM   1092 O OG1  . THR A 1 216 ? 115.23900 120.03900 142.70400 1.000 64.25999  ? 216 THR A OG1  1 
ATOM   1093 C CG2  . THR A 1 216 ? 113.41100 119.96700 144.27000 1.000 66.81798  ? 216 THR A CG2  1 
ATOM   1094 N N    . GLY A 1 217 ? 116.72400 122.84700 142.69100 1.000 64.02894  ? 217 GLY A N    1 
ATOM   1095 C CA   . GLY A 1 217 ? 118.10300 123.20500 142.44400 1.000 61.51014  ? 217 GLY A CA   1 
ATOM   1096 C C    . GLY A 1 217 ? 118.99100 122.04300 142.06300 1.000 64.31166  ? 217 GLY A C    1 
ATOM   1097 O O    . GLY A 1 217 ? 120.18500 122.25200 141.81300 1.000 64.46997  ? 217 GLY A O    1 
ATOM   1098 N N    . GLN A 1 218 ? 118.44600 120.82800 142.00500 1.000 62.28083  ? 218 GLN A N    1 
ATOM   1099 C CA   . GLN A 1 218 ? 119.22300 119.63100 141.68300 1.000 58.66225  ? 218 GLN A CA   1 
ATOM   1100 C C    . GLN A 1 218 ? 119.29800 119.46800 140.16500 1.000 60.80419  ? 218 GLN A C    1 
ATOM   1101 O O    . GLN A 1 218 ? 118.68700 118.58400 139.56200 1.000 63.95032  ? 218 GLN A O    1 
ATOM   1102 C CB   . GLN A 1 218 ? 118.61400 118.40400 142.35000 1.000 60.96338  ? 218 GLN A CB   1 
ATOM   1103 C CG   . GLN A 1 218 ? 118.59800 118.44700 143.87200 1.000 60.92511  ? 218 GLN A CG   1 
ATOM   1104 C CD   . GLN A 1 218 ? 119.54500 119.48400 144.44300 1.000 64.46992  ? 218 GLN A CD   1 
ATOM   1105 O OE1  . GLN A 1 218 ? 120.76400 119.34800 144.34700 1.000 63.25615  ? 218 GLN A OE1  1 
ATOM   1106 N NE2  . GLN A 1 218 ? 118.98600 120.52900 145.04000 1.000 60.87894  ? 218 GLN A NE2  1 
ATOM   1107 N N    . PHE A 1 219 ? 120.07300 120.35800 139.54500 1.000 51.42966  ? 219 PHE A N    1 
ATOM   1108 C CA   . PHE A 1 219 ? 120.21500 120.32300 138.09600 1.000 43.75963  ? 219 PHE A CA   1 
ATOM   1109 C C    . PHE A 1 219 ? 121.26500 119.31400 137.65700 1.000 50.75833  ? 219 PHE A C    1 
ATOM   1110 O O    . PHE A 1 219 ? 121.11800 118.69500 136.59800 1.000 53.68817  ? 219 PHE A O    1 
ATOM   1111 C CB   . PHE A 1 219 ? 120.56700 121.71200 137.56300 1.000 46.33578  ? 219 PHE A CB   1 
ATOM   1112 C CG   . PHE A 1 219 ? 119.41500 122.67500 137.56700 1.000 48.48720  ? 219 PHE A CG   1 
ATOM   1113 C CD1  . PHE A 1 219 ? 118.36400 122.52100 136.68100 1.000 48.98635  ? 219 PHE A CD1  1 
ATOM   1114 C CD2  . PHE A 1 219 ? 119.38800 123.74000 138.45000 1.000 50.98300  ? 219 PHE A CD2  1 
ATOM   1115 C CE1  . PHE A 1 219 ? 117.30600 123.40600 136.68100 1.000 52.13708  ? 219 PHE A CE1  1 
ATOM   1116 C CE2  . PHE A 1 219 ? 118.33300 124.62900 138.45400 1.000 47.82901  ? 219 PHE A CE2  1 
ATOM   1117 C CZ   . PHE A 1 219 ? 117.29000 124.46200 137.56700 1.000 49.54117  ? 219 PHE A CZ   1 
ATOM   1118 N N    . ILE A 1 220 ? 122.32100 119.12800 138.45500 1.000 52.21181  ? 220 ILE A N    1 
ATOM   1119 C CA   . ILE A 1 220 ? 123.37000 118.17000 138.11600 1.000 49.96278  ? 220 ILE A CA   1 
ATOM   1120 C C    . ILE A 1 220 ? 123.06000 116.77200 138.62700 1.000 51.74528  ? 220 ILE A C    1 
ATOM   1121 O O    . ILE A 1 220 ? 123.70400 115.80500 138.19300 1.000 54.74201  ? 220 ILE A O    1 
ATOM   1122 C CB   . ILE A 1 220 ? 124.73200 118.63800 138.66800 1.000 53.75074  ? 220 ILE A CB   1 
ATOM   1123 C CG1  . ILE A 1 220 ? 125.06700 120.03400 138.14200 1.000 53.77698  ? 220 ILE A CG1  1 
ATOM   1124 C CG2  . ILE A 1 220 ? 125.83300 117.66200 138.28700 1.000 54.23006  ? 220 ILE A CG2  1 
ATOM   1125 C CD1  . ILE A 1 220 ? 126.54600 120.34700 138.14600 1.000 53.26246  ? 220 ILE A CD1  1 
ATOM   1126 N N    . GLU A 1 221 ? 122.08500 116.62800 139.52100 1.000 53.88695  ? 221 GLU A N    1 
ATOM   1127 C CA   . GLU A 1 221 ? 121.65200 115.32500 140.00300 1.000 55.44626  ? 221 GLU A CA   1 
ATOM   1128 C C    . GLU A 1 221 ? 120.48600 114.76900 139.19800 1.000 55.79361  ? 221 GLU A C    1 
ATOM   1129 O O    . GLU A 1 221 ? 119.97600 113.69400 139.52800 1.000 54.16279  ? 221 GLU A O    1 
ATOM   1130 C CB   . GLU A 1 221 ? 121.26900 115.40900 141.48300 1.000 56.88386  ? 221 GLU A CB   1 
ATOM   1131 C CG   . GLU A 1 221 ? 122.45900 115.39900 142.42800 1.000 57.31257  ? 221 GLU A CG   1 
ATOM   1132 C CD   . GLU A 1 221 ? 122.65600 116.72500 143.13400 1.000 60.85323  ? 221 GLU A CD   1 
ATOM   1133 O OE1  . GLU A 1 221 ? 122.54600 117.77600 142.46800 1.000 61.04428  ? 221 GLU A OE1  1 
ATOM   1134 O OE2  . GLU A 1 221 ? 122.92100 116.71800 144.35400 1.000 60.82723  ? 221 GLU A OE2  1 
ATOM   1135 N N    . VAL A 1 222 ? 120.05700 115.47900 138.15900 1.000 52.93978  ? 222 VAL A N    1 
ATOM   1136 C CA   . VAL A 1 222 ? 119.02400 114.99200 137.25700 1.000 47.33264  ? 222 VAL A CA   1 
ATOM   1137 C C    . VAL A 1 222 ? 119.58200 114.65100 135.88200 1.000 48.01408  ? 222 VAL A C    1 
ATOM   1138 O O    . VAL A 1 222 ? 118.93600 113.89500 135.14000 1.000 52.75881  ? 222 VAL A O    1 
ATOM   1139 C CB   . VAL A 1 222 ? 117.87200 116.01100 137.12900 1.000 46.09986  ? 222 VAL A CB   1 
ATOM   1140 C CG1  . VAL A 1 222 ? 116.98100 115.67500 135.94400 1.000 48.12088  ? 222 VAL A CG1  1 
ATOM   1141 C CG2  . VAL A 1 222 ? 117.06300 116.06200 138.41200 1.000 48.25534  ? 222 VAL A CG2  1 
ATOM   1142 N N    . ALA A 1 223 ? 120.76100 115.15600 135.52800 1.000 44.44283  ? 223 ALA A N    1 
ATOM   1143 C CA   . ALA A 1 223 ? 121.38700 114.87800 134.24600 1.000 42.33171  ? 223 ALA A CA   1 
ATOM   1144 C C    . ALA A 1 223 ? 122.42900 113.77500 134.33500 1.000 45.00200  ? 223 ALA A C    1 
ATOM   1145 O O    . ALA A 1 223 ? 122.97500 113.37000 133.30500 1.000 48.49720  ? 223 ALA A O    1 
ATOM   1146 C CB   . ALA A 1 223 ? 122.02500 116.15100 133.68200 1.000 39.75421  ? 223 ALA A CB   1 
ATOM   1147 N N    . ILE A 1 224 ? 122.71300 113.28000 135.53700 1.000 47.10445  ? 224 ILE A N    1 
ATOM   1148 C CA   . ILE A 1 224 ? 123.65900 112.18900 135.71800 1.000 45.52067  ? 224 ILE A CA   1 
ATOM   1149 C C    . ILE A 1 224 ? 122.96800 110.87600 136.06400 1.000 46.62441  ? 224 ILE A C    1 
ATOM   1150 O O    . ILE A 1 224 ? 123.54400 109.80700 135.80500 1.000 53.61106  ? 224 ILE A O    1 
ATOM   1151 C CB   . ILE A 1 224 ? 124.71000 112.53900 136.79200 1.000 44.97240  ? 224 ILE A CB   1 
ATOM   1152 C CG1  . ILE A 1 224 ? 125.90400 113.25400 136.15900 1.000 47.21896  ? 224 ILE A CG1  1 
ATOM   1153 C CG2  . ILE A 1 224 ? 125.16700 111.29400 137.53500 1.000 45.07944  ? 224 ILE A CG2  1 
ATOM   1154 C CD1  . ILE A 1 224 ? 126.95500 113.68300 137.15800 1.000 48.36282  ? 224 ILE A CD1  1 
ATOM   1155 N N    . SER A 1 225 ? 121.75500 110.91400 136.61100 1.000 40.13058  ? 225 SER A N    1 
ATOM   1156 C CA   . SER A 1 225 ? 121.00600 109.70800 136.93000 1.000 41.54797  ? 225 SER A CA   1 
ATOM   1157 C C    . SER A 1 225 ? 120.17400 109.20500 135.76000 1.000 44.74549  ? 225 SER A C    1 
ATOM   1158 O O    . SER A 1 225 ? 119.67900 108.07500 135.81300 1.000 51.80653  ? 225 SER A O    1 
ATOM   1159 C CB   . SER A 1 225 ? 120.09600 109.95100 138.13800 1.000 43.80059  ? 225 SER A CB   1 
ATOM   1160 O OG   . SER A 1 225 ? 118.96300 110.72000 137.77800 1.000 45.89771  ? 225 SER A OG   1 
ATOM   1161 N N    . ARG A 1 226 ? 120.00700 110.01200 134.71500 1.000 41.23289  ? 226 ARG A N    1 
ATOM   1162 C CA   . ARG A 1 226 ? 119.22700 109.63500 133.54700 1.000 36.87096  ? 226 ARG A CA   1 
ATOM   1163 C C    . ARG A 1 226 ? 120.09900 109.32700 132.34000 1.000 41.35567  ? 226 ARG A C    1 
ATOM   1164 O O    . ARG A 1 226 ? 119.56800 109.01200 131.27100 1.000 50.31783  ? 226 ARG A O    1 
ATOM   1165 C CB   . ARG A 1 226 ? 118.23100 110.74600 133.19600 1.000 36.11874  ? 226 ARG A CB   1 
ATOM   1166 C CG   . ARG A 1 226 ? 116.80200 110.44300 133.59600 1.000 38.04214  ? 226 ARG A CG   1 
ATOM   1167 C CD   . ARG A 1 226 ? 116.16700 111.63100 134.28700 1.000 39.29722  ? 226 ARG A CD   1 
ATOM   1168 N NE   . ARG A 1 226 ? 116.44300 111.63700 135.71800 1.000 42.12903  ? 226 ARG A NE   1 
ATOM   1169 C CZ   . ARG A 1 226 ? 115.51500 111.55200 136.66000 1.000 41.91390  ? 226 ARG A CZ   1 
ATOM   1170 N NH1  . ARG A 1 226 ? 114.23200 111.45300 136.35900 1.000 39.83573  ? 226 ARG A NH1  1 
ATOM   1171 N NH2  . ARG A 1 226 ? 115.88400 111.57000 137.93700 1.000 44.43859  ? 226 ARG A NH2  1 
ATOM   1172 N N    . PHE A 1 227 ? 121.42100 109.40900 132.48400 1.000 38.44372  ? 227 PHE A N    1 
ATOM   1173 C CA   . PHE A 1 227 ? 122.34700 109.10300 131.40400 1.000 38.45533  ? 227 PHE A CA   1 
ATOM   1174 C C    . PHE A 1 227 ? 122.88600 107.68200 131.48200 1.000 42.55242  ? 227 PHE A C    1 
ATOM   1175 O O    . PHE A 1 227 ? 123.25500 107.11100 130.44800 1.000 40.75605  ? 227 PHE A O    1 
ATOM   1176 C CB   . PHE A 1 227 ? 123.51500 110.09900 131.42900 1.000 38.95774  ? 227 PHE A CB   1 
ATOM   1177 C CG   . PHE A 1 227 ? 124.57400 109.82900 130.40100 1.000 45.11292  ? 227 PHE A CG   1 
ATOM   1178 C CD1  . PHE A 1 227 ? 124.27500 109.86500 129.05000 1.000 47.81023  ? 227 PHE A CD1  1 
ATOM   1179 C CD2  . PHE A 1 227 ? 125.87400 109.54500 130.78700 1.000 42.45442  ? 227 PHE A CD2  1 
ATOM   1180 C CE1  . PHE A 1 227 ? 125.25100 109.62100 128.10500 1.000 39.94204  ? 227 PHE A CE1  1 
ATOM   1181 C CE2  . PHE A 1 227 ? 126.85200 109.29800 129.84600 1.000 44.07545  ? 227 PHE A CE2  1 
ATOM   1182 C CZ   . PHE A 1 227 ? 126.54000 109.33600 128.50400 1.000 43.20136  ? 227 PHE A CZ   1 
ATOM   1183 N N    . LEU A 1 228 ? 122.81500 107.05100 132.65400 1.000 41.28170  ? 228 LEU A N    1 
ATOM   1184 C CA   . LEU A 1 228 ? 123.24800 105.66600 132.76000 1.000 39.29268  ? 228 LEU A CA   1 
ATOM   1185 C C    . LEU A 1 228 ? 122.18200 104.70500 132.25600 1.000 45.25787  ? 228 LEU A C    1 
ATOM   1186 O O    . LEU A 1 228 ? 122.51900 103.64300 131.72300 1.000 50.64013  ? 228 LEU A O    1 
ATOM   1187 C CB   . LEU A 1 228 ? 123.60900 105.34300 134.20900 1.000 44.54546  ? 228 LEU A CB   1 
ATOM   1188 C CG   . LEU A 1 228 ? 124.62400 106.28100 134.86600 1.000 44.37167  ? 228 LEU A CG   1 
ATOM   1189 C CD1  . LEU A 1 228 ? 124.45800 106.28200 136.37600 1.000 45.15721  ? 228 LEU A CD1  1 
ATOM   1190 C CD2  . LEU A 1 228 ? 126.04300 105.89900 134.48100 1.000 43.35440  ? 228 LEU A CD2  1 
ATOM   1191 N N    . LEU A 1 229 ? 120.90400 105.07300 132.35500 1.000 33.52748  ? 229 LEU A N    1 
ATOM   1192 C CA   . LEU A 1 229 ? 119.87200 104.22900 131.76500 1.000 32.56075  ? 229 LEU A CA   1 
ATOM   1193 C C    . LEU A 1 229 ? 119.88700 104.33300 130.24600 1.000 34.49229  ? 229 LEU A C    1 
ATOM   1194 O O    . LEU A 1 229 ? 119.62400 103.34200 129.54900 1.000 42.92650  ? 229 LEU A O    1 
ATOM   1195 C CB   . LEU A 1 229 ? 118.50200 104.62000 132.31600 1.000 38.46659  ? 229 LEU A CB   1 
ATOM   1196 C CG   . LEU A 1 229 ? 118.18200 104.14500 133.73400 1.000 37.12652  ? 229 LEU A CG   1 
ATOM   1197 C CD1  . LEU A 1 229 ? 117.39100 105.20200 134.47900 1.000 35.72509  ? 229 LEU A CD1  1 
ATOM   1198 C CD2  . LEU A 1 229 ? 117.43000 102.82600 133.71300 1.000 39.04797  ? 229 LEU A CD2  1 
ATOM   1199 N N    . ILE A 1 230 ? 120.34200 105.47000 129.71800 1.000 25.58001  ? 230 ILE A N    1 
ATOM   1200 C CA   . ILE A 1 230 ? 120.46100 105.58800 128.27300 1.000 28.43011  ? 230 ILE A CA   1 
ATOM   1201 C C    . ILE A 1 230 ? 121.73000 104.90400 127.79500 1.000 30.19094  ? 230 ILE A C    1 
ATOM   1202 O O    . ILE A 1 230 ? 121.76400 104.36000 126.68400 1.000 38.53558  ? 230 ILE A O    1 
ATOM   1203 C CB   . ILE A 1 230 ? 120.42900 107.07000 127.86500 1.000 29.96861  ? 230 ILE A CB   1 
ATOM   1204 C CG1  . ILE A 1 230 ? 119.00400 107.61900 127.96200 1.000 28.48018  ? 230 ILE A CG1  1 
ATOM   1205 C CG2  . ILE A 1 230 ? 120.98500 107.25300 126.46400 1.000 25.67948  ? 230 ILE A CG2  1 
ATOM   1206 C CD1  . ILE A 1 230 ? 118.89300 109.09200 127.64700 1.000 28.33203  ? 230 ILE A CD1  1 
ATOM   1207 N N    . ALA A 1 231 ? 122.74900 104.80900 128.65100 1.000 27.62432  ? 231 ALA A N    1 
ATOM   1208 C CA   . ALA A 1 231 ? 123.92700 104.05200 128.25200 1.000 29.85008  ? 231 ALA A CA   1 
ATOM   1209 C C    . ALA A 1 231 ? 123.63400 102.55900 128.29500 1.000 31.58708  ? 231 ALA A C    1 
ATOM   1210 O O    . ALA A 1 231 ? 124.09100 101.80400 127.43000 1.000 35.64934  ? 231 ALA A O    1 
ATOM   1211 C CB   . ALA A 1 231 ? 125.11100 104.40300 129.15200 1.000 29.56088  ? 231 ALA A CB   1 
ATOM   1212 N N    . LEU A 1 232 ? 122.83300 102.12500 129.27200 1.000 24.36327  ? 232 LEU A N    1 
ATOM   1213 C CA   . LEU A 1 232 ? 122.39500 100.73400 129.32500 1.000 30.37931  ? 232 LEU A CA   1 
ATOM   1214 C C    . LEU A 1 232 ? 121.60000 100.36400 128.07900 1.000 29.34619  ? 232 LEU A C    1 
ATOM   1215 O O    . LEU A 1 232 ? 121.85800 99.33200  127.43900 1.000 37.02482  ? 232 LEU A O    1 
ATOM   1216 C CB   . LEU A 1 232 ? 121.56000 100.50700 130.58700 1.000 31.67309  ? 232 LEU A CB   1 
ATOM   1217 C CG   . LEU A 1 232 ? 120.80500 99.18500  130.74500 1.000 35.62134  ? 232 LEU A CG   1 
ATOM   1218 C CD1  . LEU A 1 232 ? 121.72600 98.08000  131.24000 1.000 38.18782  ? 232 LEU A CD1  1 
ATOM   1219 C CD2  . LEU A 1 232 ? 119.61800 99.35900  131.68100 1.000 25.15304  ? 232 LEU A CD2  1 
ATOM   1220 N N    . GLY A 1 233 ? 120.65200 101.22300 127.69100 1.000 27.86187  ? 233 GLY A N    1 
ATOM   1221 C CA   . GLY A 1 233 ? 119.85700 100.92900 126.51100 1.000 22.21752  ? 233 GLY A CA   1 
ATOM   1222 C C    . GLY A 1 233 ? 120.68200 100.91600 125.23900 1.000 24.42988  ? 233 GLY A C    1 
ATOM   1223 O O    . GLY A 1 233 ? 120.53300 100.01600 124.40400 1.000 30.44043  ? 233 GLY A O    1 
ATOM   1224 N N    . ALA A 1 234 ? 121.60200 101.87300 125.09400 1.000 26.53419  ? 234 ALA A N    1 
ATOM   1225 C CA   . ALA A 1 234 ? 122.39400 101.92500 123.87200 1.000 25.01306  ? 234 ALA A CA   1 
ATOM   1226 C C    . ALA A 1 234 ? 123.34800 100.74100 123.78800 1.000 32.82273  ? 234 ALA A C    1 
ATOM   1227 O O    . ALA A 1 234 ? 123.53300 100.16300 122.71200 1.000 30.68123  ? 234 ALA A O    1 
ATOM   1228 C CB   . ALA A 1 234 ? 123.16300 103.24200 123.79700 1.000 18.56882  ? 234 ALA A CB   1 
ATOM   1229 N N    . GLY A 1 235 ? 123.94300 100.34900 124.91500 1.000 27.29560  ? 235 GLY A N    1 
ATOM   1230 C CA   . GLY A 1 235 ? 124.83900 99.20600  124.90700 1.000 17.76233  ? 235 GLY A CA   1 
ATOM   1231 C C    . GLY A 1 235 ? 124.13500 97.90500  124.57300 1.000 28.23836  ? 235 GLY A C    1 
ATOM   1232 O O    . GLY A 1 235 ? 124.61800 97.11800  123.75000 1.000 32.29444  ? 235 GLY A O    1 
ATOM   1233 N N    . VAL A 1 236 ? 122.98600 97.65300  125.20800 1.000 25.58969  ? 236 VAL A N    1 
ATOM   1234 C CA   . VAL A 1 236 ? 122.23900 96.43800  124.89100 1.000 24.84681  ? 236 VAL A CA   1 
ATOM   1235 C C    . VAL A 1 236 ? 121.79700 96.42600  123.43100 1.000 30.95954  ? 236 VAL A C    1 
ATOM   1236 O O    . VAL A 1 236 ? 121.93200 95.40700  122.73600 1.000 34.60484  ? 236 VAL A O    1 
ATOM   1237 C CB   . VAL A 1 236 ? 121.03900 96.28800  125.84600 1.000 23.60062  ? 236 VAL A CB   1 
ATOM   1238 C CG1  . VAL A 1 236 ? 120.19600 95.08800  125.45500 1.000 24.00693  ? 236 VAL A CG1  1 
ATOM   1239 C CG2  . VAL A 1 236 ? 121.51900 96.15700  127.28000 1.000 26.26660  ? 236 VAL A CG2  1 
ATOM   1240 N N    . SER A 1 237 ? 121.28900 97.55700  122.93000 1.000 23.60310  ? 237 SER A N    1 
ATOM   1241 C CA   . SER A 1 237 ? 120.86000 97.61100  121.53600 1.000 18.99438  ? 237 SER A CA   1 
ATOM   1242 C C    . SER A 1 237 ? 122.01600 97.37800  120.57000 1.000 24.60478  ? 237 SER A C    1 
ATOM   1243 O O    . SER A 1 237 ? 121.87800 96.62500  119.59900 1.000 30.40823  ? 237 SER A O    1 
ATOM   1244 C CB   . SER A 1 237 ? 120.19000 98.95300  121.24400 1.000 18.60766  ? 237 SER A CB   1 
ATOM   1245 O OG   . SER A 1 237 ? 118.99600 99.09900  121.98600 1.000 31.81998  ? 237 SER A OG   1 
ATOM   1246 N N    . LEU A 1 238 ? 123.17800 97.97600  120.84200 1.000 26.98025  ? 238 LEU A N    1 
ATOM   1247 C CA   . LEU A 1 238 ? 124.33000 97.78300  119.96700 1.000 23.83027  ? 238 LEU A CA   1 
ATOM   1248 C C    . LEU A 1 238 ? 124.84300 96.34900  119.98900 1.000 26.20749  ? 238 LEU A C    1 
ATOM   1249 O O    . LEU A 1 238 ? 125.13400 95.77900  118.93200 1.000 29.58715  ? 238 LEU A O    1 
ATOM   1250 C CB   . LEU A 1 238 ? 125.45000 98.74100  120.36900 1.000 28.33382  ? 238 LEU A CB   1 
ATOM   1251 C CG   . LEU A 1 238 ? 125.92900 99.76600  119.34400 1.000 31.04270  ? 238 LEU A CG   1 
ATOM   1252 C CD1  . LEU A 1 238 ? 125.70100 101.17700 119.85600 1.000 31.12445  ? 238 LEU A CD1  1 
ATOM   1253 C CD2  . LEU A 1 238 ? 127.39600 99.53900  119.02800 1.000 29.55043  ? 238 LEU A CD2  1 
ATOM   1254 N N    . GLY A 1 239 ? 124.94000 95.73600  121.16700 1.000 26.47725  ? 239 GLY A N    1 
ATOM   1255 C CA   . GLY A 1 239 ? 125.40100 94.35800  121.21500 1.000 22.00357  ? 239 GLY A CA   1 
ATOM   1256 C C    . GLY A 1 239 ? 124.46400 93.37500  120.53900 1.000 31.48238  ? 239 GLY A C    1 
ATOM   1257 O O    . GLY A 1 239 ? 124.90500 92.51200  119.76800 1.000 30.98122  ? 239 GLY A O    1 
ATOM   1258 N N    . VAL A 1 240 ? 123.15300 93.55100  120.73000 1.000 25.68147  ? 240 VAL A N    1 
ATOM   1259 C CA   . VAL A 1 240 ? 122.20600 92.64000  120.09400 1.000 20.89362  ? 240 VAL A CA   1 
ATOM   1260 C C    . VAL A 1 240 ? 122.14200 92.86700  118.58700 1.000 27.87363  ? 240 VAL A C    1 
ATOM   1261 O O    . VAL A 1 240 ? 122.03000 91.90900  117.81500 1.000 31.32708  ? 240 VAL A O    1 
ATOM   1262 C CB   . VAL A 1 240 ? 120.81800 92.76600  120.74800 1.000 26.83130  ? 240 VAL A CB   1 
ATOM   1263 C CG1  . VAL A 1 240 ? 119.80300 91.92400  119.99600 1.000 19.61721  ? 240 VAL A CG1  1 
ATOM   1264 C CG2  . VAL A 1 240 ? 120.88200 92.34000  122.20200 1.000 21.43611  ? 240 VAL A CG2  1 
ATOM   1265 N N    . ASN A 1 241 ? 122.21400 94.12000  118.13600 1.000 26.20116  ? 241 ASN A N    1 
ATOM   1266 C CA   . ASN A 1 241 ? 122.16900 94.37600  116.70100 1.000 14.20619  ? 241 ASN A CA   1 
ATOM   1267 C C    . ASN A 1 241 ? 123.43200 93.88800  115.99800 1.000 27.05990  ? 241 ASN A C    1 
ATOM   1268 O O    . ASN A 1 241 ? 123.35500 93.23300  114.95100 1.000 28.36547  ? 241 ASN A O    1 
ATOM   1269 C CB   . ASN A 1 241 ? 121.95600 95.86800  116.44200 1.000 13.79546  ? 241 ASN A CB   1 
ATOM   1270 C CG   . ASN A 1 241 ? 121.15700 96.13200  115.18300 1.000 18.99720  ? 241 ASN A CG   1 
ATOM   1271 O OD1  . ASN A 1 241 ? 120.98400 95.24800  114.34700 1.000 28.62390  ? 241 ASN A OD1  1 
ATOM   1272 N ND2  . ASN A 1 241 ? 120.66900 97.35500  115.03900 1.000 22.01151  ? 241 ASN A ND2  1 
ATOM   1273 N N    . MET A 1 242 ? 124.60500 94.18900  116.55500 1.000 32.83620  ? 242 MET A N    1 
ATOM   1274 C CA   . MET A 1 242 ? 125.85800 93.85000  115.89400 1.000 27.00284  ? 242 MET A CA   1 
ATOM   1275 C C    . MET A 1 242 ? 126.26200 92.38400  116.00800 1.000 31.74241  ? 242 MET A C    1 
ATOM   1276 O O    . MET A 1 242 ? 127.00300 91.90600  115.14400 1.000 30.47529  ? 242 MET A O    1 
ATOM   1277 C CB   . MET A 1 242 ? 126.98600 94.72900  116.44200 1.000 27.65267  ? 242 MET A CB   1 
ATOM   1278 C CG   . MET A 1 242 ? 128.38200 94.25700  116.07200 1.000 37.60500  ? 242 MET A CG   1 
ATOM   1279 S SD   . MET A 1 242 ? 129.17500 95.27600  114.81200 1.000 58.03501  ? 242 MET A SD   1 
ATOM   1280 C CE   . MET A 1 242 ? 129.35500 96.83000  115.68300 1.000 37.11596  ? 242 MET A CE   1 
ATOM   1281 N N    . PHE A 1 243 ? 125.80600 91.64300  117.02300 1.000 36.78259  ? 243 PHE A N    1 
ATOM   1282 C CA   . PHE A 1 243 ? 126.31200 90.28500  117.18500 1.000 25.84979  ? 243 PHE A CA   1 
ATOM   1283 C C    . PHE A 1 243 ? 125.33100 89.16800  116.85200 1.000 25.90979  ? 243 PHE A C    1 
ATOM   1284 O O    . PHE A 1 243 ? 125.75800 88.01200  116.77000 1.000 32.23761  ? 243 PHE A O    1 
ATOM   1285 C CB   . PHE A 1 243 ? 126.83900 90.08700  118.61400 1.000 27.91890  ? 243 PHE A CB   1 
ATOM   1286 C CG   . PHE A 1 243 ? 127.99000 90.98900  118.95700 1.000 33.58276  ? 243 PHE A CG   1 
ATOM   1287 C CD1  . PHE A 1 243 ? 129.16800 90.93300  118.23100 1.000 32.09019  ? 243 PHE A CD1  1 
ATOM   1288 C CD2  . PHE A 1 243 ? 127.89600 91.89500  119.99700 1.000 33.43981  ? 243 PHE A CD2  1 
ATOM   1289 C CE1  . PHE A 1 243 ? 130.22800 91.76100  118.53500 1.000 28.52229  ? 243 PHE A CE1  1 
ATOM   1290 C CE2  . PHE A 1 243 ? 128.95500 92.72500  120.30700 1.000 34.95817  ? 243 PHE A CE2  1 
ATOM   1291 C CZ   . PHE A 1 243 ? 130.12100 92.65700  119.57400 1.000 33.96305  ? 243 PHE A CZ   1 
ATOM   1292 N N    . ILE A 1 244 ? 124.04900 89.45300  116.65600 1.000 28.47446  ? 244 ILE A N    1 
ATOM   1293 C CA   . ILE A 1 244 ? 123.09300 88.43300  116.23400 1.000 26.23947  ? 244 ILE A CA   1 
ATOM   1294 C C    . ILE A 1 244 ? 122.59800 88.77700  114.83200 1.000 26.77457  ? 244 ILE A C    1 
ATOM   1295 O O    . ILE A 1 244 ? 121.74800 89.65700  114.65800 1.000 31.16799  ? 244 ILE A O    1 
ATOM   1296 C CB   . ILE A 1 244 ? 121.93300 88.29400  117.22600 1.000 30.86073  ? 244 ILE A CB   1 
ATOM   1297 C CG1  . ILE A 1 244 ? 122.46000 87.82300  118.58300 1.000 21.94079  ? 244 ILE A CG1  1 
ATOM   1298 C CG2  . ILE A 1 244 ? 120.89600 87.31700  116.70200 1.000 28.34241  ? 244 ILE A CG2  1 
ATOM   1299 C CD1  . ILE A 1 244 ? 121.65800 88.31900  119.75800 1.000 22.47677  ? 244 ILE A CD1  1 
ATOM   1300 N N    . TYR A 1 245 ? 123.12900 88.07400  113.82600 1.000 21.33683  ? 245 TYR A N    1 
ATOM   1301 C CA   . TYR A 1 245 ? 122.76600 88.20800  112.41500 1.000 22.67203  ? 245 TYR A CA   1 
ATOM   1302 C C    . TYR A 1 245 ? 122.84400 89.64000  111.89400 1.000 27.64976  ? 245 TYR A C    1 
ATOM   1303 O O    . TYR A 1 245 ? 121.80900 90.25700  111.61400 1.000 28.37658  ? 245 TYR A O    1 
ATOM   1304 C CB   . TYR A 1 245 ? 121.36300 87.64400  112.18800 1.000 25.07297  ? 245 TYR A CB   1 
ATOM   1305 C CG   . TYR A 1 245 ? 121.27200 86.15800  112.44500 1.000 29.98087  ? 245 TYR A CG   1 
ATOM   1306 C CD1  . TYR A 1 245 ? 121.90700 85.25100  111.61000 1.000 31.92252  ? 245 TYR A CD1  1 
ATOM   1307 C CD2  . TYR A 1 245 ? 120.56300 85.66200  113.52900 1.000 32.93641  ? 245 TYR A CD2  1 
ATOM   1308 C CE1  . TYR A 1 245 ? 121.83500 83.89200  111.84300 1.000 31.30863  ? 245 TYR A CE1  1 
ATOM   1309 C CE2  . TYR A 1 245 ? 120.48400 84.30400  113.77000 1.000 32.04311  ? 245 TYR A CE2  1 
ATOM   1310 C CZ   . TYR A 1 245 ? 121.12100 83.42400  112.92400 1.000 34.99057  ? 245 TYR A CZ   1 
ATOM   1311 O OH   . TYR A 1 245 ? 121.04500 82.07100  113.16000 1.000 41.69605  ? 245 TYR A OH   1 
ATOM   1312 N N    . PRO A 1 246 ? 124.04400 90.19500  111.73700 1.000 28.01409  ? 246 PRO A N    1 
ATOM   1313 C CA   . PRO A 1 246 ? 124.16300 91.57300  111.24500 1.000 20.08225  ? 246 PRO A CA   1 
ATOM   1314 C C    . PRO A 1 246 ? 123.69500 91.71300  109.80300 1.000 19.32170  ? 246 PRO A C    1 
ATOM   1315 O O    . PRO A 1 246 ? 123.89800 90.82300  108.97400 1.000 26.56736  ? 246 PRO A O    1 
ATOM   1316 C CB   . PRO A 1 246 ? 125.66400 91.86300  111.36600 1.000 17.92066  ? 246 PRO A CB   1 
ATOM   1317 C CG   . PRO A 1 246 ? 126.17700 90.84600  112.33500 1.000 23.23421  ? 246 PRO A CG   1 
ATOM   1318 C CD   . PRO A 1 246 ? 125.35200 89.62700  112.09800 1.000 18.80666  ? 246 PRO A CD   1 
ATOM   1319 N N    . ILE A 1 247 ? 123.05700 92.84600  109.51200 1.000 26.94022  ? 247 ILE A N    1 
ATOM   1320 C CA   . ILE A 1 247 ? 122.62600 93.20600  108.16500 1.000 17.52911  ? 247 ILE A CA   1 
ATOM   1321 C C    . ILE A 1 247 ? 123.48100 94.37200  107.68500 1.000 24.30749  ? 247 ILE A C    1 
ATOM   1322 O O    . ILE A 1 247 ? 123.57100 95.40200  108.36200 1.000 27.26093  ? 247 ILE A O    1 
ATOM   1323 C CB   . ILE A 1 247 ? 121.13200 93.56600  108.12300 1.000 19.65833  ? 247 ILE A CB   1 
ATOM   1324 C CG1  . ILE A 1 247 ? 120.27500 92.30900  108.27500 1.000 25.59822  ? 247 ILE A CG1  1 
ATOM   1325 C CG2  . ILE A 1 247 ? 120.79500 94.28700  106.83000 1.000 21.82195  ? 247 ILE A CG2  1 
ATOM   1326 C CD1  . ILE A 1 247 ? 118.79800 92.55400  108.08000 1.000 23.54331  ? 247 ILE A CD1  1 
ATOM   1327 N N    . TRP A 1 248 ? 124.10200 94.21100  106.52000 1.000 28.39150  ? 248 TRP A N    1 
ATOM   1328 C CA   . TRP A 1 248 ? 125.03400 95.18600  105.96900 1.000 11.67651  ? 248 TRP A CA   1 
ATOM   1329 C C    . TRP A 1 248 ? 124.39400 95.94400  104.81200 1.000 20.69594  ? 248 TRP A C    1 
ATOM   1330 O O    . TRP A 1 248 ? 123.61700 95.37400  104.04200 1.000 30.56978  ? 248 TRP A O    1 
ATOM   1331 C CB   . TRP A 1 248 ? 126.31300 94.49100  105.50600 1.000 15.72804  ? 248 TRP A CB   1 
ATOM   1332 C CG   . TRP A 1 248 ? 126.85800 93.53000  106.52200 1.000 20.20418  ? 248 TRP A CG   1 
ATOM   1333 C CD1  . TRP A 1 248 ? 126.67300 92.18000  106.55100 1.000 24.01629  ? 248 TRP A CD1  1 
ATOM   1334 C CD2  . TRP A 1 248 ? 127.67400 93.84600  107.65600 1.000 16.00256  ? 248 TRP A CD2  1 
ATOM   1335 N NE1  . TRP A 1 248 ? 127.32300 91.63500  107.62800 1.000 18.07138  ? 248 TRP A NE1  1 
ATOM   1336 C CE2  . TRP A 1 248 ? 127.94600 92.63700  108.32300 1.000 18.56075  ? 248 TRP A CE2  1 
ATOM   1337 C CE3  . TRP A 1 248 ? 128.20100 95.03300  108.17000 1.000 16.19130  ? 248 TRP A CE3  1 
ATOM   1338 C CZ2  . TRP A 1 248 ? 128.72100 92.58000  109.47800 1.000 18.13696  ? 248 TRP A CZ2  1 
ATOM   1339 C CZ3  . TRP A 1 248 ? 128.97000 94.97500  109.31500 1.000 21.07189  ? 248 TRP A CZ3  1 
ATOM   1340 C CH2  . TRP A 1 248 ? 129.22200 93.75800  109.95700 1.000 19.74466  ? 248 TRP A CH2  1 
ATOM   1341 N N    . ALA A 1 249 ? 124.71900 97.23700  104.69700 1.000 22.26599  ? 249 ALA A N    1 
ATOM   1342 C CA   . ALA A 1 249 ? 124.17700 98.06700  103.62500 1.000 23.41381  ? 249 ALA A CA   1 
ATOM   1343 C C    . ALA A 1 249 ? 124.94300 97.94700  102.30900 1.000 26.35856  ? 249 ALA A C    1 
ATOM   1344 O O    . ALA A 1 249 ? 124.37400 98.24000  101.24700 1.000 35.64085  ? 249 ALA A O    1 
ATOM   1345 C CB   . ALA A 1 249 ? 124.14800 99.53100  104.06700 1.000 19.19920  ? 249 ALA A CB   1 
ATOM   1346 N N    . GLY A 1 250 ? 126.19500 97.48900  102.34000 1.000 13.25559  ? 250 GLY A N    1 
ATOM   1347 C CA   . GLY A 1 250 ? 126.92400 97.30600  101.09500 1.000 19.27911  ? 250 GLY A CA   1 
ATOM   1348 C C    . GLY A 1 250 ? 126.36300 96.16300  100.27300 1.000 29.04332  ? 250 GLY A C    1 
ATOM   1349 O O    . GLY A 1 250 ? 126.27700 96.24800  99.04200  1.000 37.92746  ? 250 GLY A O    1 
ATOM   1350 N N    . GLU A 1 251 ? 125.92600 95.09800  100.94600 1.000 24.41117  ? 251 GLU A N    1 
ATOM   1351 C CA   . GLU A 1 251 ? 125.27600 94.00400  100.24200 1.000 30.35508  ? 251 GLU A CA   1 
ATOM   1352 C C    . GLU A 1 251 ? 123.92900 94.44200  99.69200  1.000 26.37268  ? 251 GLU A C    1 
ATOM   1353 O O    . GLU A 1 251 ? 123.53000 94.01000  98.60400  1.000 33.22021  ? 251 GLU A O    1 
ATOM   1354 C CB   . GLU A 1 251 ? 125.10500 92.81200  101.18100 1.000 30.14468  ? 251 GLU A CB   1 
ATOM   1355 C CG   . GLU A 1 251 ? 126.34100 92.48400  101.99700 1.000 29.70232  ? 251 GLU A CG   1 
ATOM   1356 C CD   . GLU A 1 251 ? 126.42000 91.01900  102.36600 1.000 38.43045  ? 251 GLU A CD   1 
ATOM   1357 O OE1  . GLU A 1 251 ? 125.59000 90.23400  101.86500 1.000 38.74456  ? 251 GLU A OE1  1 
ATOM   1358 O OE2  . GLU A 1 251 ? 127.31000 90.65200  103.16100 1.000 37.89874  ? 251 GLU A OE2  1 
ATOM   1359 N N    . ASP A 1 252 ? 123.24000 95.33300  100.40700 1.000 18.83742  ? 252 ASP A N    1 
ATOM   1360 C CA   . ASP A 1 252 ? 121.98100 95.86800  99.90600  1.000 27.90481  ? 252 ASP A CA   1 
ATOM   1361 C C    . ASP A 1 252 ? 122.20100 96.66900  98.63100  1.000 31.73199  ? 252 ASP A C    1 
ATOM   1362 O O    . ASP A 1 252 ? 121.43300 96.54500  97.66900  1.000 37.96605  ? 252 ASP A O    1 
ATOM   1363 C CB   . ASP A 1 252 ? 121.32400 96.73900  100.97700 1.000 26.27462  ? 252 ASP A CB   1 
ATOM   1364 C CG   . ASP A 1 252 ? 120.57900 95.92500  102.01400 1.000 38.57952  ? 252 ASP A CG   1 
ATOM   1365 O OD1  . ASP A 1 252 ? 120.90300 94.73200  102.18200 1.000 40.93119  ? 252 ASP A OD1  1 
ATOM   1366 O OD2  . ASP A 1 252 ? 119.66700 96.47900  102.66200 1.000 41.19980  ? 252 ASP A OD2  1 
ATOM   1367 N N    . LEU A 1 253 ? 123.27400 97.46200  98.58500  1.000 30.44375  ? 253 LEU A N    1 
ATOM   1368 C CA   . LEU A 1 253 ? 123.56000 98.23600  97.38000  1.000 27.23300  ? 253 LEU A CA   1 
ATOM   1369 C C    . LEU A 1 253 ? 123.93900 97.32700  96.21000  1.000 24.59877  ? 253 LEU A C    1 
ATOM   1370 O O    . LEU A 1 253 ? 123.46900 97.52400  95.07700  1.000 31.92857  ? 253 LEU A O    1 
ATOM   1371 C CB   . LEU A 1 253 ? 124.67100 99.24400  97.67500  1.000 26.54560  ? 253 LEU A CB   1 
ATOM   1372 C CG   . LEU A 1 253 ? 124.85800 100.41900 96.71600  1.000 31.85652  ? 253 LEU A CG   1 
ATOM   1373 C CD1  . LEU A 1 253 ? 123.66600 101.35100 96.79000  1.000 28.56533  ? 253 LEU A CD1  1 
ATOM   1374 C CD2  . LEU A 1 253 ? 126.13800 101.16500 97.04400  1.000 24.01116  ? 253 LEU A CD2  1 
ATOM   1375 N N    . HIS A 1 254 ? 124.77000 96.31500  96.47200  1.000 21.31372  ? 254 HIS A N    1 
ATOM   1376 C CA   . HIS A 1 254 ? 125.15500 95.37200  95.42400  1.000 25.61744  ? 254 HIS A CA   1 
ATOM   1377 C C    . HIS A 1 254 ? 123.93300 94.65700  94.84600  1.000 29.62536  ? 254 HIS A C    1 
ATOM   1378 O O    . HIS A 1 254 ? 123.77400 94.54900  93.61400  1.000 34.39535  ? 254 HIS A O    1 
ATOM   1379 C CB   . HIS A 1 254 ? 126.15400 94.37300  96.01100  1.000 25.38585  ? 254 HIS A CB   1 
ATOM   1380 C CG   . HIS A 1 254 ? 126.90900 93.58000  94.99200  1.000 35.50593  ? 254 HIS A CG   1 
ATOM   1381 N ND1  . HIS A 1 254 ? 127.83900 92.62500  95.33900  1.000 31.56705  ? 254 HIS A ND1  1 
ATOM   1382 C CD2  . HIS A 1 254 ? 126.87900 93.60000  93.63900  1.000 40.79739  ? 254 HIS A CD2  1 
ATOM   1383 C CE1  . HIS A 1 254 ? 128.34800 92.08900  94.24600  1.000 28.16991  ? 254 HIS A CE1  1 
ATOM   1384 N NE2  . HIS A 1 254 ? 127.78200 92.66300  93.20000  1.000 37.79655  ? 254 HIS A NE2  1 
ATOM   1385 N N    . ASN A 1 255 ? 123.02200 94.22200  95.72100  1.000 24.86233  ? 255 ASN A N    1 
ATOM   1386 C CA   . ASN A 1 255 ? 121.84900 93.49800  95.25600  1.000 21.11934  ? 255 ASN A CA   1 
ATOM   1387 C C    . ASN A 1 255 ? 120.88900 94.41900  94.52000  1.000 26.13624  ? 255 ASN A C    1 
ATOM   1388 O O    . ASN A 1 255 ? 120.24400 93.99800  93.55100  1.000 36.58711  ? 255 ASN A O    1 
ATOM   1389 C CB   . ASN A 1 255 ? 121.14600 92.83600  96.44000  1.000 26.00484  ? 255 ASN A CB   1 
ATOM   1390 C CG   . ASN A 1 255 ? 121.93100 91.67200  97.01000  1.000 27.39592  ? 255 ASN A CG   1 
ATOM   1391 O OD1  . ASN A 1 255 ? 122.94200 91.25200  96.44900  1.000 36.74825  ? 255 ASN A OD1  1 
ATOM   1392 N ND2  . ASN A 1 255 ? 121.47000 91.14700  98.13700  1.000 28.61899  ? 255 ASN A ND2  1 
ATOM   1393 N N    . LEU A 1 256 ? 120.80400 95.68400  94.94000  1.000 18.84555  ? 256 LEU A N    1 
ATOM   1394 C CA   . LEU A 1 256 ? 119.95900 96.63700  94.23300  1.000 21.71351  ? 256 LEU A CA   1 
ATOM   1395 C C    . LEU A 1 256 ? 120.46000 96.85600  92.81200  1.000 25.82713  ? 256 LEU A C    1 
ATOM   1396 O O    . LEU A 1 256 ? 119.66500 96.90400  91.86200  1.000 32.54233  ? 256 LEU A O    1 
ATOM   1397 C CB   . LEU A 1 256 ? 119.91300 97.95500  95.00500  1.000 28.75716  ? 256 LEU A CB   1 
ATOM   1398 C CG   . LEU A 1 256 ? 118.95200 99.04100  94.51900  1.000 32.92294  ? 256 LEU A CG   1 
ATOM   1399 C CD1  . LEU A 1 256 ? 117.51200 98.58200  94.65600  1.000 23.41833  ? 256 LEU A CD1  1 
ATOM   1400 C CD2  . LEU A 1 256 ? 119.18300 100.32900 95.28800  1.000 31.95990  ? 256 LEU A CD2  1 
ATOM   1401 N N    . VAL A 1 257 ? 121.77900 96.96500  92.64200  1.000 24.07525  ? 257 VAL A N    1 
ATOM   1402 C CA   . VAL A 1 257 ? 122.32200 97.17200  91.30000  1.000 19.64921  ? 257 VAL A CA   1 
ATOM   1403 C C    . VAL A 1 257 ? 122.01900 95.97000  90.40900  1.000 19.17063  ? 257 VAL A C    1 
ATOM   1404 O O    . VAL A 1 257 ? 121.58400 96.12000  89.25300  1.000 29.73169  ? 257 VAL A O    1 
ATOM   1405 C CB   . VAL A 1 257 ? 123.83400 97.45800  91.37600  1.000 26.44243  ? 257 VAL A CB   1 
ATOM   1406 C CG1  . VAL A 1 257 ? 124.46200 97.38700  89.99400  1.000 22.22169  ? 257 VAL A CG1  1 
ATOM   1407 C CG2  . VAL A 1 257 ? 124.08700 98.81400  92.01200  1.000 23.75358  ? 257 VAL A CG2  1 
ATOM   1408 N N    . VAL A 1 258 ? 122.20800 94.75700  90.93900  1.000 20.92857  ? 258 VAL A N    1 
ATOM   1409 C CA   . VAL A 1 258 ? 121.93700 93.57000  90.12300  1.000 22.67629  ? 258 VAL A CA   1 
ATOM   1410 C C    . VAL A 1 258 ? 120.45800 93.50100  89.73800  1.000 23.99348  ? 258 VAL A C    1 
ATOM   1411 O O    . VAL A 1 258 ? 120.10400 93.21200  88.58000  1.000 20.44010  ? 258 VAL A O    1 
ATOM   1412 C CB   . VAL A 1 258 ? 122.39600 92.30000  90.86400  1.000 22.17309  ? 258 VAL A CB   1 
ATOM   1413 C CG1  . VAL A 1 258 ? 121.93300 91.05600  90.12600  1.000 25.03777  ? 258 VAL A CG1  1 
ATOM   1414 C CG2  . VAL A 1 258 ? 123.90500 92.29700  91.01900  1.000 19.93189  ? 258 VAL A CG2  1 
ATOM   1415 N N    . LYS A 1 259 ? 119.57000 93.77600  90.69800  1.000 23.80969  ? 259 LYS A N    1 
ATOM   1416 C CA   . LYS A 1 259 ? 118.14000 93.70600  90.42200  1.000 22.68631  ? 259 LYS A CA   1 
ATOM   1417 C C    . LYS A 1 259 ? 117.72400 94.72900  89.37100  1.000 25.23609  ? 259 LYS A C    1 
ATOM   1418 O O    . LYS A 1 259 ? 116.87700 94.44100  88.51400  1.000 29.01097  ? 259 LYS A O    1 
ATOM   1419 C CB   . LYS A 1 259 ? 117.35600 93.90800  91.71800  1.000 25.33718  ? 259 LYS A CB   1 
ATOM   1420 C CG   . LYS A 1 259 ? 115.88300 93.56200  91.62600  1.000 28.89337  ? 259 LYS A CG   1 
ATOM   1421 C CD   . LYS A 1 259 ? 115.10200 94.21600  92.74800  1.000 31.60204  ? 259 LYS A CD   1 
ATOM   1422 C CE   . LYS A 1 259 ? 113.60500 94.07600  92.53600  1.000 35.85570  ? 259 LYS A CE   1 
ATOM   1423 N NZ   . LYS A 1 259 ? 113.23800 92.71300  92.06500  1.000 34.79327  ? 259 LYS A NZ   1 
ATOM   1424 N N    . ASN A 1 260 ? 118.31200 95.92800  89.41100  1.000 29.67434  ? 260 ASN A N    1 
ATOM   1425 C CA   . ASN A 1 260 ? 117.96600 96.93200  88.40800  1.000 25.12632  ? 260 ASN A CA   1 
ATOM   1426 C C    . ASN A 1 260 ? 118.42000 96.49800  87.02000  1.000 23.58796  ? 260 ASN A C    1 
ATOM   1427 O O    . ASN A 1 260 ? 117.70000 96.69900  86.02500  1.000 29.05672  ? 260 ASN A O    1 
ATOM   1428 C CB   . ASN A 1 260 ? 118.58200 98.28100  88.77800  1.000 27.00944  ? 260 ASN A CB   1 
ATOM   1429 C CG   . ASN A 1 260 ? 117.78100 99.01700  89.82900  1.000 32.10265  ? 260 ASN A CG   1 
ATOM   1430 O OD1  . ASN A 1 260 ? 116.57200 98.82500  89.95000  1.000 37.29588  ? 260 ASN A OD1  1 
ATOM   1431 N ND2  . ASN A 1 260 ? 118.45100 99.86700  90.59500  1.000 32.02234  ? 260 ASN A ND2  1 
ATOM   1432 N N    . PHE A 1 261 ? 119.60100 95.87600  86.93800  1.000 26.46807  ? 261 PHE A N    1 
ATOM   1433 C CA   . PHE A 1 261 ? 120.05500 95.37800  85.64300  1.000 26.25066  ? 261 PHE A CA   1 
ATOM   1434 C C    . PHE A 1 261 ? 119.09200 94.33900  85.08200  1.000 28.12857  ? 261 PHE A C    1 
ATOM   1435 O O    . PHE A 1 261 ? 118.84100 94.30900  83.87200  1.000 29.35061  ? 261 PHE A O    1 
ATOM   1436 C CB   . PHE A 1 261 ? 121.46500 94.80100  85.74900  1.000 24.93909  ? 261 PHE A CB   1 
ATOM   1437 C CG   . PHE A 1 261 ? 122.54500 95.78000  85.39400  1.000 26.60029  ? 261 PHE A CG   1 
ATOM   1438 C CD1  . PHE A 1 261 ? 122.97900 95.89900  84.08500  1.000 31.29048  ? 261 PHE A CD1  1 
ATOM   1439 C CD2  . PHE A 1 261 ? 123.12600 96.57800  86.36100  1.000 29.97984  ? 261 PHE A CD2  1 
ATOM   1440 C CE1  . PHE A 1 261 ? 123.97000 96.79600  83.74800  1.000 30.66209  ? 261 PHE A CE1  1 
ATOM   1441 C CE2  . PHE A 1 261 ? 124.11800 97.47800  86.02900  1.000 31.94237  ? 261 PHE A CE2  1 
ATOM   1442 C CZ   . PHE A 1 261 ? 124.54000 97.58600  84.72100  1.000 29.02244  ? 261 PHE A CZ   1 
ATOM   1443 N N    . MET A 1 262 ? 118.54900 93.47100  85.93900  1.000 31.21431  ? 262 MET A N    1 
ATOM   1444 C CA   . MET A 1 262 ? 117.59900 92.47300  85.43500  1.000 28.16506  ? 262 MET A CA   1 
ATOM   1445 C C    . MET A 1 262 ? 116.27300 93.11200  85.00900  1.000 30.09935  ? 262 MET A C    1 
ATOM   1446 O O    . MET A 1 262 ? 115.68800 92.74600  83.97000  1.000 36.43296  ? 262 MET A O    1 
ATOM   1447 C CB   . MET A 1 262 ? 117.35900 91.40100  86.49700  1.000 31.72915  ? 262 MET A CB   1 
ATOM   1448 C CG   . MET A 1 262 ? 118.53300 90.46100  86.72100  1.000 30.51537  ? 262 MET A CG   1 
ATOM   1449 S SD   . MET A 1 262 ? 119.45300 90.09700  85.21600  1.000 53.22221  ? 262 MET A SD   1 
ATOM   1450 C CE   . MET A 1 262 ? 120.88600 89.26600  85.89100  1.000 31.93337  ? 262 MET A CE   1 
ATOM   1451 N N    . ASN A 1 263 ? 115.79200 94.08300  85.79200  1.000 27.45861  ? 263 ASN A N    1 
ATOM   1452 C CA   . ASN A 1 263 ? 114.49300 94.68700  85.51000  1.000 25.54895  ? 263 ASN A CA   1 
ATOM   1453 C C    . ASN A 1 263 ? 114.49500 95.44400  84.18700  1.000 30.90704  ? 263 ASN A C    1 
ATOM   1454 O O    . ASN A 1 263 ? 113.50800 95.39700  83.43800  1.000 30.05655  ? 263 ASN A O    1 
ATOM   1455 C CB   . ASN A 1 263 ? 114.08600 95.61800  86.65100  1.000 29.38588  ? 263 ASN A CB   1 
ATOM   1456 C CG   . ASN A 1 263 ? 113.82200 94.87700  87.94400  1.000 34.98275  ? 263 ASN A CG   1 
ATOM   1457 O OD1  . ASN A 1 263 ? 113.42900 93.71100  87.93600  1.000 38.88893  ? 263 ASN A OD1  1 
ATOM   1458 N ND2  . ASN A 1 263 ? 114.03100 95.55300  89.06500  1.000 31.63297  ? 263 ASN A ND2  1 
ATOM   1459 N N    . VAL A 1 264 ? 115.58000 96.16400  83.88500  1.000 31.80227  ? 264 VAL A N    1 
ATOM   1460 C CA   . VAL A 1 264 ? 115.58800 96.93400  82.64200  1.000 27.12364  ? 264 VAL A CA   1 
ATOM   1461 C C    . VAL A 1 264 ? 115.50500 96.00800  81.43100  1.000 29.40693  ? 264 VAL A C    1 
ATOM   1462 O O    . VAL A 1 264 ? 114.82800 96.31500  80.44000  1.000 31.72325  ? 264 VAL A O    1 
ATOM   1463 C CB   . VAL A 1 264 ? 116.82600 97.84700  82.57800  1.000 24.58415  ? 264 VAL A CB   1 
ATOM   1464 C CG1  . VAL A 1 264 ? 116.95300 98.46700  81.19800  1.000 25.66656  ? 264 VAL A CG1  1 
ATOM   1465 C CG2  . VAL A 1 264 ? 116.73000 98.93300  83.63300  1.000 28.87712  ? 264 VAL A CG2  1 
ATOM   1466 N N    . ALA A 1 265 ? 116.15500 94.84400  81.50300  1.000 27.00844  ? 265 ALA A N    1 
ATOM   1467 C CA   . ALA A 1 265 ? 116.08300 93.89600  80.39500  1.000 26.81865  ? 265 ALA A CA   1 
ATOM   1468 C C    . ALA A 1 265 ? 114.67600 93.33400  80.23900  1.000 34.28318  ? 265 ALA A C    1 
ATOM   1469 O O    . ALA A 1 265 ? 114.17100 93.19300  79.11100  1.000 30.71637  ? 265 ALA A O    1 
ATOM   1470 C CB   . ALA A 1 265 ? 117.09000 92.76700  80.60200  1.000 24.80034  ? 265 ALA A CB   1 
ATOM   1471 N N    . THR A 1 266 ? 114.01300 93.02800  81.35800  1.000 34.26263  ? 266 THR A N    1 
ATOM   1472 C CA   . THR A 1 266 ? 112.65700 92.49900  81.23300  1.000 28.38174  ? 266 THR A CA   1 
ATOM   1473 C C    . THR A 1 266 ? 111.71800 93.53800  80.62500  1.000 33.51685  ? 266 THR A C    1 
ATOM   1474 O O    . THR A 1 266 ? 110.88400 93.21200  79.76700  1.000 32.97552  ? 266 THR A O    1 
ATOM   1475 C CB   . THR A 1 266 ? 112.13600 92.03300  82.59100  1.000 31.07892  ? 266 THR A CB   1 
ATOM   1476 O OG1  . THR A 1 266 ? 112.96800 90.97700  83.08500  1.000 37.09097  ? 266 THR A OG1  1 
ATOM   1477 C CG2  . THR A 1 266 ? 110.71100 91.52200  82.46100  1.000 30.38444  ? 266 THR A CG2  1 
ATOM   1478 N N    . SER A 1 267 ? 111.86600 94.80500  81.02500  1.000 37.67011  ? 267 SER A N    1 
ATOM   1479 C CA   . SER A 1 267 ? 111.02900 95.85300  80.44500  1.000 28.65466  ? 267 SER A CA   1 
ATOM   1480 C C    . SER A 1 267 ? 111.30800 96.02800  78.95500  1.000 32.94450  ? 267 SER A C    1 
ATOM   1481 O O    . SER A 1 267 ? 110.37800 96.22300  78.15800  1.000 29.55426  ? 267 SER A O    1 
ATOM   1482 C CB   . SER A 1 267 ? 111.24000 97.17200  81.18700  1.000 32.56362  ? 267 SER A CB   1 
ATOM   1483 O OG   . SER A 1 267 ? 110.71400 97.11000  82.49900  1.000 39.83379  ? 267 SER A OG   1 
ATOM   1484 N N    . LEU A 1 268 ? 112.58300 95.97300  78.55800  1.000 32.28795  ? 268 LEU A N    1 
ATOM   1485 C CA   . LEU A 1 268 ? 112.90400 96.13300  77.14400  1.000 28.91208  ? 268 LEU A CA   1 
ATOM   1486 C C    . LEU A 1 268 ? 112.26400 95.03500  76.30700  1.000 30.80640  ? 268 LEU A C    1 
ATOM   1487 O O    . LEU A 1 268 ? 111.73200 95.30300  75.22400  1.000 29.03516  ? 268 LEU A O    1 
ATOM   1488 C CB   . LEU A 1 268 ? 114.41700 96.15000  76.93300  1.000 25.12399  ? 268 LEU A CB   1 
ATOM   1489 C CG   . LEU A 1 268 ? 114.83600 96.35500  75.47300  1.000 29.46135  ? 268 LEU A CG   1 
ATOM   1490 C CD1  . LEU A 1 268 ? 114.72300 97.81600  75.06300  1.000 26.25991  ? 268 LEU A CD1  1 
ATOM   1491 C CD2  . LEU A 1 268 ? 116.24300 95.83600  75.22800  1.000 26.30529  ? 268 LEU A CD2  1 
ATOM   1492 N N    . GLU A 1 269 ? 112.30400 93.78900  76.78500  1.000 41.61487  ? 269 GLU A N    1 
ATOM   1493 C CA   . GLU A 1 269 ? 111.65700 92.72400  76.02000  1.000 39.42639  ? 269 GLU A CA   1 
ATOM   1494 C C    . GLU A 1 269 ? 110.14300 92.91600  75.97300  1.000 41.42470  ? 269 GLU A C    1 
ATOM   1495 O O    . GLU A 1 269 ? 109.51100 92.73400  74.91500  1.000 35.92556  ? 269 GLU A O    1 
ATOM   1496 C CB   . GLU A 1 269 ? 112.00200 91.36200  76.62000  1.000 39.48879  ? 269 GLU A CB   1 
ATOM   1497 C CG   . GLU A 1 269 ? 112.70400 90.41900  75.66200  1.000 41.89454  ? 269 GLU A CG   1 
ATOM   1498 C CD   . GLU A 1 269 ? 113.28300 89.21000  76.36800  1.000 47.51662  ? 269 GLU A CD   1 
ATOM   1499 O OE1  . GLU A 1 269 ? 112.70100 88.78300  77.38700  1.000 45.89449  ? 269 GLU A OE1  1 
ATOM   1500 O OE2  . GLU A 1 269 ? 114.31900 88.68800  75.90700  1.000 46.70384  ? 269 GLU A OE2  1 
ATOM   1501 N N    . GLY A 1 270 ? 109.55100 93.31600  77.10200  1.000 43.36024  ? 270 GLY A N    1 
ATOM   1502 C CA   . GLY A 1 270 ? 108.11000 93.49100  77.14700  1.000 37.30735  ? 270 GLY A CA   1 
ATOM   1503 C C    . GLY A 1 270 ? 107.61100 94.55900  76.19400  1.000 38.37734  ? 270 GLY A C    1 
ATOM   1504 O O    . GLY A 1 270 ? 106.55200 94.40900  75.58400  1.000 42.07100  ? 270 GLY A O    1 
ATOM   1505 N N    . CYS A 1 271 ? 108.37000 95.64600  76.04100  1.000 42.63575  ? 271 CYS A N    1 
ATOM   1506 C CA   . CYS A 1 271 ? 107.90300 96.73800  75.18800  1.000 38.64900  ? 271 CYS A CA   1 
ATOM   1507 C C    . CYS A 1 271 ? 107.77000 96.29200  73.73500  1.000 34.93267  ? 271 CYS A C    1 
ATOM   1508 O O    . CYS A 1 271 ? 106.73500 96.51700  73.09500  1.000 32.16948  ? 271 CYS A O    1 
ATOM   1509 C CB   . CYS A 1 271 ? 108.84500 97.93700  75.29800  1.000 37.18550  ? 271 CYS A CB   1 
ATOM   1510 S SG   . CYS A 1 271 ? 108.70000 98.86000  76.84200  1.000 57.29908  ? 271 CYS A SG   1 
ATOM   1511 N N    . VAL A 1 272 ? 108.80900 95.65300  73.19600  1.000 40.38807  ? 272 VAL A N    1 
ATOM   1512 C CA   . VAL A 1 272 ? 108.76100 95.22700  71.80100  1.000 38.18339  ? 272 VAL A CA   1 
ATOM   1513 C C    . VAL A 1 272 ? 107.71300 94.13900  71.60800  1.000 43.77096  ? 272 VAL A C    1 
ATOM   1514 O O    . VAL A 1 272 ? 106.97500 94.13900  70.61000  1.000 40.11965  ? 272 VAL A O    1 
ATOM   1515 C CB   . VAL A 1 272 ? 110.15200 94.77000  71.32800  1.000 40.66272  ? 272 VAL A CB   1 
ATOM   1516 C CG1  . VAL A 1 272 ? 110.09200 94.32100  69.87900  1.000 38.24175  ? 272 VAL A CG1  1 
ATOM   1517 C CG2  . VAL A 1 272 ? 111.16100 95.89200  71.49300  1.000 36.83889  ? 272 VAL A CG2  1 
ATOM   1518 N N    . ASN A 1 273 ? 107.60600 93.20400  72.56100  1.000 44.99015  ? 273 ASN A N    1 
ATOM   1519 C CA   . ASN A 1 273 ? 106.59400 92.16400  72.40500  1.000 43.74142  ? 273 ASN A CA   1 
ATOM   1520 C C    . ASN A 1 273 ? 105.18900 92.75600  72.41300  1.000 43.28518  ? 273 ASN A C    1 
ATOM   1521 O O    . ASN A 1 273 ? 104.33100 92.34600  71.62300  1.000 42.84737  ? 273 ASN A O    1 
ATOM   1522 C CB   . ASN A 1 273 ? 106.74400 91.10300  73.49500  1.000 43.90546  ? 273 ASN A CB   1 
ATOM   1523 C CG   . ASN A 1 273 ? 107.82900 90.09400  73.17600  1.000 45.32222  ? 273 ASN A CG   1 
ATOM   1524 O OD1  . ASN A 1 273 ? 108.17100 89.88200  72.01400  1.000 42.31281  ? 273 ASN A OD1  1 
ATOM   1525 N ND2  . ASN A 1 273 ? 108.37300 89.46200  74.20900  1.000 49.99543  ? 273 ASN A ND2  1 
ATOM   1526 N N    . GLY A 1 274 ? 104.93600 93.72800  73.29100  1.000 42.61175  ? 274 GLY A N    1 
ATOM   1527 C CA   . GLY A 1 274 ? 103.63600 94.37600  73.30700  1.000 40.07937  ? 274 GLY A CA   1 
ATOM   1528 C C    . GLY A 1 274 ? 103.35100 95.17500  72.05000  1.000 39.39888  ? 274 GLY A C    1 
ATOM   1529 O O    . GLY A 1 274 ? 102.21100 95.22300  71.58200  1.000 43.56955  ? 274 GLY A O    1 
ATOM   1530 N N    . TYR A 1 275 ? 104.37600 95.82200  71.48800  1.000 38.38911  ? 275 TYR A N    1 
ATOM   1531 C CA   . TYR A 1 275 ? 104.15000 96.60500  70.27600  1.000 36.39472  ? 275 TYR A CA   1 
ATOM   1532 C C    . TYR A 1 275 ? 103.87400 95.72400  69.06400  1.000 39.82622  ? 275 TYR A C    1 
ATOM   1533 O O    . TYR A 1 275 ? 103.07800 96.10400  68.19900  1.000 35.38472  ? 275 TYR A O    1 
ATOM   1534 C CB   . TYR A 1 275 ? 105.34000 97.51700  69.99300  1.000 36.20432  ? 275 TYR A CB   1 
ATOM   1535 C CG   . TYR A 1 275 ? 105.08800 98.50500  68.87500  1.000 32.91178  ? 275 TYR A CG   1 
ATOM   1536 C CD1  . TYR A 1 275 ? 104.35200 99.65900  69.09700  1.000 37.15975  ? 275 TYR A CD1  1 
ATOM   1537 C CD2  . TYR A 1 275 ? 105.57800 98.27800  67.59700  1.000 33.22069  ? 275 TYR A CD2  1 
ATOM   1538 C CE1  . TYR A 1 275 ? 104.11900 100.56400 68.08100  1.000 34.37884  ? 275 TYR A CE1  1 
ATOM   1539 C CE2  . TYR A 1 275 ? 105.34800 99.17600  66.57600  1.000 31.62179  ? 275 TYR A CE2  1 
ATOM   1540 C CZ   . TYR A 1 275 ? 104.61900 100.31700 66.82300  1.000 35.30071  ? 275 TYR A CZ   1 
ATOM   1541 O OH   . TYR A 1 275 ? 104.38600 101.21500 65.80900  1.000 35.69118  ? 275 TYR A OH   1 
ATOM   1542 N N    . LEU A 1 276 ? 104.49900 94.55100  68.97900  1.000 50.78618  ? 276 LEU A N    1 
ATOM   1543 C CA   . LEU A 1 276 ? 104.31900 93.70800  67.80200  1.000 47.51232  ? 276 LEU A CA   1 
ATOM   1544 C C    . LEU A 1 276 ? 103.19800 92.68800  67.96300  1.000 50.48530  ? 276 LEU A C    1 
ATOM   1545 O O    . LEU A 1 276 ? 103.02400 91.83600  67.08600  1.000 53.60733  ? 276 LEU A O    1 
ATOM   1546 C CB   . LEU A 1 276 ? 105.62600 92.99000  67.45400  1.000 50.58915  ? 276 LEU A CB   1 
ATOM   1547 C CG   . LEU A 1 276 ? 106.71700 93.84400  66.80500  1.000 50.06163  ? 276 LEU A CG   1 
ATOM   1548 C CD1  . LEU A 1 276 ? 108.04200 93.10500  66.79200  1.000 48.94752  ? 276 LEU A CD1  1 
ATOM   1549 C CD2  . LEU A 1 276 ? 106.31400 94.25100  65.39600  1.000 50.32813  ? 276 LEU A CD2  1 
ATOM   1550 N N    . ARG A 1 277 ? 102.43200 92.75900  69.04700  1.000 57.72930  ? 277 ARG A N    1 
ATOM   1551 C CA   . ARG A 1 277 ? 101.32600 91.83400  69.24700  1.000 57.78598  ? 277 ARG A CA   1 
ATOM   1552 C C    . ARG A 1 277 ? 100.23500 92.06000  68.20800  1.000 60.14483  ? 277 ARG A C    1 
ATOM   1553 O O    . ARG A 1 277 ? 99.94400  93.19500  67.82300  1.000 60.75072  ? 277 ARG A O    1 
ATOM   1554 C CB   . ARG A 1 277 ? 100.74900 91.98900  70.65300  1.000 57.63943  ? 277 ARG A CB   1 
ATOM   1555 C CG   . ARG A 1 277 ? 100.08900 90.73200  71.19100  1.000 62.58345  ? 277 ARG A CG   1 
ATOM   1556 C CD   . ARG A 1 277 ? 100.60800 90.38300  72.57500  1.000 62.57364  ? 277 ARG A CD   1 
ATOM   1557 N NE   . ARG A 1 277 ? 100.45100 91.48700  73.51400  1.000 62.26807  ? 277 ARG A NE   1 
ATOM   1558 C CZ   . ARG A 1 277 ? 101.26300 91.72200  74.53500  1.000 60.91210  ? 277 ARG A CZ   1 
ATOM   1559 N NH1  . ARG A 1 277 ? 102.30800 90.94800  74.77900  1.000 59.38464  ? 277 ARG A NH1  1 
ATOM   1560 N NH2  . ARG A 1 277 ? 101.02200 92.76000  75.33000  1.000 61.33080  ? 277 ARG A NH2  1 
ATOM   1561 N N    . CYS A 1 278 ? 99.62700  90.96700  67.75800  1.000 73.32320  ? 278 CYS A N    1 
ATOM   1562 C CA   . CYS A 1 278 ? 98.53300  91.03800  66.79400  1.000 74.38940  ? 278 CYS A CA   1 
ATOM   1563 C C    . CYS A 1 278 ? 97.18100  91.01200  67.50000  1.000 73.61777  ? 278 CYS A C    1 
ATOM   1564 O O    . CYS A 1 278 ? 96.54900  92.05000  67.69000  1.000 73.11546  ? 278 CYS A O    1 
ATOM   1565 C CB   . CYS A 1 278 ? 98.62300  89.88600  65.79000  1.000 74.64473  ? 278 CYS A CB   1 
ATOM   1566 S SG   . CYS A 1 278 ? 100.30400 89.46700  65.27400  1.000 80.21082  ? 278 CYS A SG   1 
ATOM   1567 N N    . VAL A 1 298 ? 105.71000 95.92500  82.53100  1.000 61.40049  ? 298 VAL A N    1 
ATOM   1568 C CA   . VAL A 1 298 ? 106.54500 96.91500  81.86300  1.000 60.09680  ? 298 VAL A CA   1 
ATOM   1569 C C    . VAL A 1 298 ? 106.85600 98.06400  82.81200  1.000 59.90770  ? 298 VAL A C    1 
ATOM   1570 O O    . VAL A 1 298 ? 107.98000 98.56100  82.85400  1.000 62.28827  ? 298 VAL A O    1 
ATOM   1571 C CB   . VAL A 1 298 ? 105.87300 97.43300  80.58100  1.000 59.42229  ? 298 VAL A CB   1 
ATOM   1572 C CG1  . VAL A 1 298 ? 106.83100 98.32400  79.80400  1.000 54.72681  ? 298 VAL A CG1  1 
ATOM   1573 C CG2  . VAL A 1 298 ? 105.40300 96.27000  79.72300  1.000 57.42088  ? 298 VAL A CG2  1 
ATOM   1574 N N    . TYR A 1 299 ? 105.84700 98.48500  83.57500  1.000 64.60235  ? 299 TYR A N    1 
ATOM   1575 C CA   . TYR A 1 299 ? 106.02300 99.61600  84.47900  1.000 66.05740  ? 299 TYR A CA   1 
ATOM   1576 C C    . TYR A 1 299 ? 107.07000 99.31700  85.54400  1.000 64.89123  ? 299 TYR A C    1 
ATOM   1577 O O    . TYR A 1 299 ? 107.96700 100.13000 85.79600  1.000 62.81314  ? 299 TYR A O    1 
ATOM   1578 C CB   . TYR A 1 299 ? 104.69000 99.97600  85.13900  1.000 65.30836  ? 299 TYR A CB   1 
ATOM   1579 C CG   . TYR A 1 299 ? 104.05600 101.24800 84.62600  1.000 65.12154  ? 299 TYR A CG   1 
ATOM   1580 C CD1  . TYR A 1 299 ? 104.37500 102.47800 85.18800  1.000 64.31904  ? 299 TYR A CD1  1 
ATOM   1581 C CD2  . TYR A 1 299 ? 103.12300 101.22000 83.60000  1.000 64.41995  ? 299 TYR A CD2  1 
ATOM   1582 C CE1  . TYR A 1 299 ? 103.79700 103.64500 84.72900  1.000 65.20139  ? 299 TYR A CE1  1 
ATOM   1583 C CE2  . TYR A 1 299 ? 102.53600 102.38400 83.13700  1.000 65.02692  ? 299 TYR A CE2  1 
ATOM   1584 C CZ   . TYR A 1 299 ? 102.87700 103.59300 83.70400  1.000 66.42168  ? 299 TYR A CZ   1 
ATOM   1585 O OH   . TYR A 1 299 ? 102.29700 104.75300 83.24600  1.000 66.57733  ? 299 TYR A OH   1 
ATOM   1586 N N    . LYS A 1 300 ? 106.96200 98.15300  86.19000  1.000 65.35268  ? 300 LYS A N    1 
ATOM   1587 C CA   . LYS A 1 300 ? 107.79200 97.87300  87.35700  1.000 66.26919  ? 300 LYS A CA   1 
ATOM   1588 C C    . LYS A 1 300 ? 109.27700 98.04300  87.06100  1.000 66.36438  ? 300 LYS A C    1 
ATOM   1589 O O    . LYS A 1 300 ? 110.00300 98.64700  87.85600  1.000 63.58138  ? 300 LYS A O    1 
ATOM   1590 C CB   . LYS A 1 300 ? 107.51000 96.45900  87.86600  1.000 63.54414  ? 300 LYS A CB   1 
ATOM   1591 N N    . GLY A 1 301 ? 109.72400 97.62800  85.88000  1.000 58.02244  ? 301 GLY A N    1 
ATOM   1592 C CA   . GLY A 1 301 ? 111.14900 97.61900  85.60500  1.000 56.14601  ? 301 GLY A CA   1 
ATOM   1593 C C    . GLY A 1 301 ? 111.77500 98.99500  85.51800  1.000 59.21848  ? 301 GLY A C    1 
ATOM   1594 O O    . GLY A 1 301 ? 112.59100 99.37200  86.37100  1.000 59.13032  ? 301 GLY A O    1 
ATOM   1595 N N    . TYR A 1 302 ? 111.40900 99.76000  84.49000  1.000 56.11201  ? 302 TYR A N    1 
ATOM   1596 C CA   . TYR A 1 302 ? 111.97700 101.09300 84.35400  1.000 55.09822  ? 302 TYR A CA   1 
ATOM   1597 C C    . TYR A 1 302 ? 111.54400 101.99800 85.50000  1.000 55.95308  ? 302 TYR A C    1 
ATOM   1598 O O    . TYR A 1 302 ? 112.31700 102.86300 85.92600  1.000 59.28236  ? 302 TYR A O    1 
ATOM   1599 C CB   . TYR A 1 302 ? 111.62200 101.69300 82.98800  1.000 56.85017  ? 302 TYR A CB   1 
ATOM   1600 C CG   . TYR A 1 302 ? 110.17700 102.09300 82.78200  1.000 55.36043  ? 302 TYR A CG   1 
ATOM   1601 C CD1  . TYR A 1 302 ? 109.66200 103.24600 83.35900  1.000 55.19322  ? 302 TYR A CD1  1 
ATOM   1602 C CD2  . TYR A 1 302 ? 109.33500 101.32900 81.98600  1.000 53.66075  ? 302 TYR A CD2  1 
ATOM   1603 C CE1  . TYR A 1 302 ? 108.34700 103.61600 83.16500  1.000 55.51313  ? 302 TYR A CE1  1 
ATOM   1604 C CE2  . TYR A 1 302 ? 108.01900 101.69200 81.78500  1.000 54.95377  ? 302 TYR A CE2  1 
ATOM   1605 C CZ   . TYR A 1 302 ? 107.53100 102.83600 82.37600  1.000 55.84287  ? 302 TYR A CZ   1 
ATOM   1606 O OH   . TYR A 1 302 ? 106.22100 103.20300 82.17900  1.000 55.95627  ? 302 TYR A OH   1 
ATOM   1607 N N    . ARG A 1 303 ? 110.32000 101.82800 86.00900  1.000 59.37995  ? 303 ARG A N    1 
ATOM   1608 C CA   . ARG A 1 303 ? 109.87500 102.66000 87.12100  1.000 61.38306  ? 303 ARG A CA   1 
ATOM   1609 C C    . ARG A 1 303 ? 110.69500 102.40800 88.38100  1.000 63.39203  ? 303 ARG A C    1 
ATOM   1610 O O    . ARG A 1 303 ? 110.87900 103.32300 89.19100  1.000 64.23428  ? 303 ARG A O    1 
ATOM   1611 C CB   . ARG A 1 303 ? 108.39100 102.41600 87.39600  1.000 61.81061  ? 303 ARG A CB   1 
ATOM   1612 C CG   . ARG A 1 303 ? 107.46000 102.99400 86.34200  1.000 63.12215  ? 303 ARG A CG   1 
ATOM   1613 C CD   . ARG A 1 303 ? 106.80000 104.27700 86.82000  1.000 66.49273  ? 303 ARG A CD   1 
ATOM   1614 N NE   . ARG A 1 303 ? 107.56600 105.45900 86.44200  1.000 67.40943  ? 303 ARG A NE   1 
ATOM   1615 C CZ   . ARG A 1 303 ? 107.67300 106.55200 87.18400  1.000 66.09668  ? 303 ARG A CZ   1 
ATOM   1616 N NH1  . ARG A 1 303 ? 107.07300 106.65300 88.35800  1.000 65.41722  ? 303 ARG A NH1  1 
ATOM   1617 N NH2  . ARG A 1 303 ? 108.39900 107.57200 86.73500  1.000 63.03195  ? 303 ARG A NH2  1 
ATOM   1618 N N    . SER A 1 304 ? 111.19300 101.18200 88.57200  1.000 59.54400  ? 304 SER A N    1 
ATOM   1619 C CA   . SER A 1 304 ? 112.07900 100.90800 89.69600  1.000 58.99086  ? 304 SER A CA   1 
ATOM   1620 C C    . SER A 1 304 ? 113.49500 101.39200 89.42100  1.000 60.75594  ? 304 SER A C    1 
ATOM   1621 O O    . SER A 1 304 ? 114.18300 101.86000 90.33500  1.000 57.18852  ? 304 SER A O    1 
ATOM   1622 C CB   . SER A 1 304 ? 112.07900 99.41300  90.01300  1.000 58.84153  ? 304 SER A CB   1 
ATOM   1623 O OG   . SER A 1 304 ? 112.23300 98.64500  88.83300  1.000 59.96002  ? 304 SER A OG   1 
ATOM   1624 N N    . ALA A 1 305 ? 113.94700 101.28700 88.17200  1.000 53.84989  ? 305 ALA A N    1 
ATOM   1625 C CA   . ALA A 1 305 ? 115.31900 101.65600 87.84500  1.000 50.37715  ? 305 ALA A CA   1 
ATOM   1626 C C    . ALA A 1 305 ? 115.49600 103.14900 87.60000  1.000 48.78323  ? 305 ALA A C    1 
ATOM   1627 O O    . ALA A 1 305 ? 116.63100 103.59400 87.40200  1.000 51.94496  ? 305 ALA A O    1 
ATOM   1628 C CB   . ALA A 1 305 ? 115.79500 100.87500 86.61900  1.000 49.42558  ? 305 ALA A CB   1 
ATOM   1629 N N    . VAL A 1 306 ? 114.41600 103.92800 87.60700  1.000 50.29666  ? 306 VAL A N    1 
ATOM   1630 C CA   . VAL A 1 306 ? 114.49600 105.37300 87.41900  1.000 48.27220  ? 306 VAL A CA   1 
ATOM   1631 C C    . VAL A 1 306 ? 114.08700 106.15700 88.66000  1.000 50.18144  ? 306 VAL A C    1 
ATOM   1632 O O    . VAL A 1 306 ? 114.30000 107.38000 88.69900  1.000 49.76549  ? 306 VAL A O    1 
ATOM   1633 C CB   . VAL A 1 306 ? 113.65600 105.82000 86.20000  1.000 50.65044  ? 306 VAL A CB   1 
ATOM   1634 C CG1  . VAL A 1 306 ? 113.15000 107.24600 86.35100  1.000 49.49427  ? 306 VAL A CG1  1 
ATOM   1635 C CG2  . VAL A 1 306 ? 114.46100 105.67200 84.91700  1.000 48.76261  ? 306 VAL A CG2  1 
ATOM   1636 N N    . GLU A 1 307 ? 113.56500 105.49800 89.69200  1.000 58.79990  ? 307 GLU A N    1 
ATOM   1637 C CA   . GLU A 1 307 ? 113.04200 106.17700 90.87300  1.000 58.12820  ? 307 GLU A CA   1 
ATOM   1638 C C    . GLU A 1 307 ? 113.66800 105.63500 92.15100  1.000 59.53754  ? 307 GLU A C    1 
ATOM   1639 O O    . GLU A 1 307 ? 112.99000 105.46600 93.16800  1.000 62.88199  ? 307 GLU A O    1 
ATOM   1640 C CB   . GLU A 1 307 ? 111.52100 106.06300 90.93400  1.000 58.54607  ? 307 GLU A CB   1 
ATOM   1641 N N    . SER A 1 308 ? 114.97300 105.35100 92.13100  1.000 57.12672  ? 308 SER A N    1 
ATOM   1642 C CA   . SER A 1 308 ? 115.63600 104.78900 93.30200  1.000 56.66001  ? 308 SER A CA   1 
ATOM   1643 C C    . SER A 1 308 ? 116.96300 105.46300 93.63200  1.000 54.98300  ? 308 SER A C    1 
ATOM   1644 O O    . SER A 1 308 ? 117.66400 104.99900 94.53800  1.000 58.55384  ? 308 SER A O    1 
ATOM   1645 C CB   . SER A 1 308 ? 115.86000 103.28300 93.11800  1.000 58.25794  ? 308 SER A CB   1 
ATOM   1646 O OG   . SER A 1 308 ? 117.06000 103.02700 92.40900  1.000 56.31471  ? 308 SER A OG   1 
ATOM   1647 N N    . THR A 1 309 ? 117.32200 106.54900 92.94100  1.000 54.54230  ? 309 THR A N    1 
ATOM   1648 C CA   . THR A 1 309 ? 118.60400 107.20000 93.19700  1.000 56.19646  ? 309 THR A CA   1 
ATOM   1649 C C    . THR A 1 309 ? 118.76200 107.56900 94.66800  1.000 56.23153  ? 309 THR A C    1 
ATOM   1650 O O    . THR A 1 309 ? 119.86100 107.47500 95.23000  1.000 60.36451  ? 309 THR A O    1 
ATOM   1651 C CB   . THR A 1 309 ? 118.74400 108.44600 92.32000  1.000 60.28615  ? 309 THR A CB   1 
ATOM   1652 O OG1  . THR A 1 309 ? 118.40500 108.12100 90.96600  1.000 57.15752  ? 309 THR A OG1  1 
ATOM   1653 C CG2  . THR A 1 309 ? 120.17000 108.97300 92.36800  1.000 58.40478  ? 309 THR A CG2  1 
ATOM   1654 N N    . SER A 1 310 ? 117.66900 107.98100 95.31200  1.000 51.65643  ? 310 SER A N    1 
ATOM   1655 C CA   . SER A 1 310 ? 117.73400 108.32900 96.72700  1.000 53.45852  ? 310 SER A CA   1 
ATOM   1656 C C    . SER A 1 310 ? 118.08100 107.11400 97.57700  1.000 54.72727  ? 310 SER A C    1 
ATOM   1657 O O    . SER A 1 310 ? 118.83900 107.22300 98.54800  1.000 54.04113  ? 310 SER A O    1 
ATOM   1658 C CB   . SER A 1 310 ? 116.40800 108.94100 97.17600  1.000 55.78517  ? 310 SER A CB   1 
ATOM   1659 O OG   . SER A 1 310 ? 115.31300 108.29700 96.54800  1.000 57.21025  ? 310 SER A OG   1 
ATOM   1660 N N    . GLN A 1 311 ? 117.52400 105.94900 97.23700  1.000 51.12645  ? 311 GLN A N    1 
ATOM   1661 C CA   . GLN A 1 311 ? 117.83800 104.74000 97.99000  1.000 51.19680  ? 311 GLN A CA   1 
ATOM   1662 C C    . GLN A 1 311 ? 119.31400 104.38300 97.86700  1.000 48.53414  ? 311 GLN A C    1 
ATOM   1663 O O    . GLN A 1 311 ? 119.95400 104.00300 98.85700  1.000 49.99927  ? 311 GLN A O    1 
ATOM   1664 C CB   . GLN A 1 311 ? 116.95900 103.58400 97.51300  1.000 49.63312  ? 311 GLN A CB   1 
ATOM   1665 C CG   . GLN A 1 311 ? 117.10700 102.31500 98.33200  1.000 53.40869  ? 311 GLN A CG   1 
ATOM   1666 C CD   . GLN A 1 311 ? 116.10500 101.25000 97.94100  1.000 55.81678  ? 311 GLN A CD   1 
ATOM   1667 O OE1  . GLN A 1 311 ? 115.22600 101.48300 97.11100  1.000 59.49113  ? 311 GLN A OE1  1 
ATOM   1668 N NE2  . GLN A 1 311 ? 116.23000 100.07200 98.53900  1.000 49.33667  ? 311 GLN A NE2  1 
ATOM   1669 N N    . GLU A 1 312 ? 119.88100 104.52400 96.66600  1.000 40.03644  ? 312 GLU A N    1 
ATOM   1670 C CA   . GLU A 1 312 ? 121.30100 104.23700 96.49600  1.000 40.93704  ? 312 GLU A CA   1 
ATOM   1671 C C    . GLU A 1 312 ? 122.15700 105.24000 97.25300  1.000 45.04441  ? 312 GLU A C    1 
ATOM   1672 O O    . GLU A 1 312 ? 123.18000 104.87100 97.84100  1.000 48.12082  ? 312 GLU A O    1 
ATOM   1673 C CB   . GLU A 1 312 ? 121.67900 104.22600 95.01400  1.000 41.04202  ? 312 GLU A CB   1 
ATOM   1674 C CG   . GLU A 1 312 ? 121.47100 102.89000 94.31900  1.000 46.50041  ? 312 GLU A CG   1 
ATOM   1675 C CD   . GLU A 1 312 ? 120.39100 102.93200 93.25900  1.000 51.50268  ? 312 GLU A CD   1 
ATOM   1676 O OE1  . GLU A 1 312 ? 119.48100 103.77700 93.36200  1.000 50.31183  ? 312 GLU A OE1  1 
ATOM   1677 O OE2  . GLU A 1 312 ? 120.45300 102.11500 92.31700  1.000 47.42396  ? 312 GLU A OE2  1 
ATOM   1678 N N    . GLU A 1 313 ? 121.74300 106.50900 97.28100  1.000 43.45991  ? 313 GLU A N    1 
ATOM   1679 C CA   . GLU A 1 313 ? 122.52200 107.50200 98.01200  1.000 42.06102  ? 313 GLU A CA   1 
ATOM   1680 C C    . GLU A 1 313 ? 122.47000 107.24900 99.51400  1.000 43.61638  ? 313 GLU A C    1 
ATOM   1681 O O    . GLU A 1 313 ? 123.48500 107.38100 100.20800 1.000 45.63255  ? 313 GLU A O    1 
ATOM   1682 C CB   . GLU A 1 313 ? 122.01600 108.90600 97.68500  1.000 46.77830  ? 313 GLU A CB   1 
ATOM   1683 C CG   . GLU A 1 313 ? 122.21100 109.31400 96.23700  1.000 47.20278  ? 313 GLU A CG   1 
ATOM   1684 C CD   . GLU A 1 313 ? 123.67000 109.49600 95.87300  1.000 51.67807  ? 313 GLU A CD   1 
ATOM   1685 O OE1  . GLU A 1 313 ? 123.94800 110.12500 94.83000  1.000 54.75261  ? 313 GLU A OE1  1 
ATOM   1686 O OE2  . GLU A 1 313 ? 124.53900 109.01600 96.63000  1.000 49.37035  ? 313 GLU A OE2  1 
ATOM   1687 N N    . SER A 1 314 ? 121.30700 106.84500 100.03000 1.000 30.45234  ? 314 SER A N    1 
ATOM   1688 C CA   . SER A 1 314 ? 121.20800 106.51700 101.44900 1.000 31.50878  ? 314 SER A CA   1 
ATOM   1689 C C    . SER A 1 314 ? 122.05100 105.29600 101.79600 1.000 36.59743  ? 314 SER A C    1 
ATOM   1690 O O    . SER A 1 314 ? 122.77400 105.29600 102.80200 1.000 31.60362  ? 314 SER A O    1 
ATOM   1691 C CB   . SER A 1 314 ? 119.74700 106.28600 101.83200 1.000 32.02080  ? 314 SER A CB   1 
ATOM   1692 O OG   . SER A 1 314 ? 118.90000 107.20900 101.17400 1.000 40.25441  ? 314 SER A OG   1 
ATOM   1693 N N    . LEU A 1 315 ? 121.98700 104.25100 100.96800 1.000 30.27726  ? 315 LEU A N    1 
ATOM   1694 C CA   . LEU A 1 315 ? 122.76800 103.05400 101.25000 1.000 22.76820  ? 315 LEU A CA   1 
ATOM   1695 C C    . LEU A 1 315 ? 124.26000 103.34600 101.18100 1.000 25.31319  ? 315 LEU A C    1 
ATOM   1696 O O    . LEU A 1 315 ? 125.04300 102.79700 101.96400 1.000 33.97584  ? 315 LEU A O    1 
ATOM   1697 C CB   . LEU A 1 315 ? 122.38800 101.93400 100.28400 1.000 32.08774  ? 315 LEU A CB   1 
ATOM   1698 C CG   . LEU A 1 315 ? 120.99300 101.34200 100.48500 1.000 30.38265  ? 315 LEU A CG   1 
ATOM   1699 C CD1  . LEU A 1 315 ? 120.70400 100.27600 99.44500  1.000 24.20786  ? 315 LEU A CD1  1 
ATOM   1700 C CD2  . LEU A 1 315 ? 120.84900 100.78200 101.89000 1.000 28.91329  ? 315 LEU A CD2  1 
ATOM   1701 N N    . MET A 1 316 ? 124.67600 104.21000 100.25200 1.000 24.90272  ? 316 MET A N    1 
ATOM   1702 C CA   . MET A 1 316 ? 126.07900 104.60400 100.20200 1.000 30.05367  ? 316 MET A CA   1 
ATOM   1703 C C    . MET A 1 316 ? 126.47100 105.43600 101.41600 1.000 31.32010  ? 316 MET A C    1 
ATOM   1704 O O    . MET A 1 316 ? 127.60800 105.33900 101.89000 1.000 34.18667  ? 316 MET A O    1 
ATOM   1705 C CB   . MET A 1 316 ? 126.36500 105.37200 98.91400  1.000 29.51125  ? 316 MET A CB   1 
ATOM   1706 C CG   . MET A 1 316 ? 127.84200 105.59000 98.65000  1.000 31.80556  ? 316 MET A CG   1 
ATOM   1707 S SD   . MET A 1 316 ? 128.18900 107.14700 97.81800  1.000 46.58886  ? 316 MET A SD   1 
ATOM   1708 C CE   . MET A 1 316 ? 129.82000 107.50600 98.46300  1.000 35.06733  ? 316 MET A CE   1 
ATOM   1709 N N    . SER A 1 317 ? 125.55400 106.25900 101.93000 1.000 28.11719  ? 317 SER A N    1 
ATOM   1710 C CA   . SER A 1 317 ? 125.86000 107.04400 103.12000 1.000 26.29539  ? 317 SER A CA   1 
ATOM   1711 C C    . SER A 1 317 ? 125.96000 106.16900 104.36300 1.000 31.05086  ? 317 SER A C    1 
ATOM   1712 O O    . SER A 1 317 ? 126.66800 106.52200 105.31200 1.000 27.84624  ? 317 SER A O    1 
ATOM   1713 C CB   . SER A 1 317 ? 124.80300 108.12800 103.32400 1.000 25.23702  ? 317 SER A CB   1 
ATOM   1714 O OG   . SER A 1 317 ? 123.54700 107.55600 103.64400 1.000 32.57290  ? 317 SER A OG   1 
ATOM   1715 N N    . PHE A 1 318 ? 125.26800 105.02900 104.37800 1.000 33.32856  ? 318 PHE A N    1 
ATOM   1716 C CA   . PHE A 1 318 ? 125.31900 104.14000 105.53400 1.000 15.61978  ? 318 PHE A CA   1 
ATOM   1717 C C    . PHE A 1 318 ? 126.48800 103.16600 105.48700 1.000 25.06668  ? 318 PHE A C    1 
ATOM   1718 O O    . PHE A 1 318 ? 126.98300 102.75500 106.54200 1.000 24.31619  ? 318 PHE A O    1 
ATOM   1719 C CB   . PHE A 1 318 ? 124.02000 103.33500 105.64700 1.000 17.71198  ? 318 PHE A CB   1 
ATOM   1720 C CG   . PHE A 1 318 ? 122.81800 104.15600 106.00000 1.000 19.71874  ? 318 PHE A CG   1 
ATOM   1721 C CD1  . PHE A 1 318 ? 122.94600 105.32100 106.73500 1.000 22.00928  ? 318 PHE A CD1  1 
ATOM   1722 C CD2  . PHE A 1 318 ? 121.55400 103.75700 105.60300 1.000 15.61574  ? 318 PHE A CD2  1 
ATOM   1723 C CE1  . PHE A 1 318 ? 121.83600 106.07500 107.06200 1.000 19.10797  ? 318 PHE A CE1  1 
ATOM   1724 C CE2  . PHE A 1 318 ? 120.44200 104.50500 105.92800 1.000 19.21151  ? 318 PHE A CE2  1 
ATOM   1725 C CZ   . PHE A 1 318 ? 120.58300 105.66600 106.65800 1.000 19.73369  ? 318 PHE A CZ   1 
ATOM   1726 N N    . ALA A 1 319 ? 126.94800 102.79500 104.29100 1.000 26.69371  ? 319 ALA A N    1 
ATOM   1727 C CA   . ALA A 1 319 ? 127.96600 101.76500 104.13400 1.000 7.76047   ? 319 ALA A CA   1 
ATOM   1728 C C    . ALA A 1 319 ? 129.37500 102.24400 104.45000 1.000 19.98658  ? 319 ALA A C    1 
ATOM   1729 O O    . ALA A 1 319 ? 130.28300 101.41200 104.55200 1.000 24.10503  ? 319 ALA A O    1 
ATOM   1730 C CB   . ALA A 1 319 ? 127.93000 101.21000 102.70900 1.000 6.10924   ? 319 ALA A CB   1 
ATOM   1731 N N    . ILE A 1 320 ? 129.58700 103.55100 104.60900 1.000 26.56549  ? 320 ILE A N    1 
ATOM   1732 C CA   . ILE A 1 320 ? 130.92800 104.04800 104.89300 1.000 19.35238  ? 320 ILE A CA   1 
ATOM   1733 C C    . ILE A 1 320 ? 131.29200 103.91300 106.36500 1.000 22.81144  ? 320 ILE A C    1 
ATOM   1734 O O    . ILE A 1 320 ? 132.47800 103.98300 106.71100 1.000 29.75651  ? 320 ILE A O    1 
ATOM   1735 C CB   . ILE A 1 320 ? 131.07000 105.51200 104.44700 1.000 22.54968  ? 320 ILE A CB   1 
ATOM   1736 C CG1  . ILE A 1 320 ? 129.82900 106.31300 104.84000 1.000 29.75077  ? 320 ILE A CG1  1 
ATOM   1737 C CG2  . ILE A 1 320 ? 131.28500 105.58800 102.94500 1.000 23.83295  ? 320 ILE A CG2  1 
ATOM   1738 C CD1  . ILE A 1 320 ? 130.04300 107.80700 104.82300 1.000 26.45252  ? 320 ILE A CD1  1 
ATOM   1739 N N    . TRP A 1 321 ? 130.30800 103.72300 107.24100 1.000 18.28823  ? 321 TRP A N    1 
ATOM   1740 C CA   . TRP A 1 321 ? 130.55800 103.58400 108.66900 1.000 12.95447  ? 321 TRP A CA   1 
ATOM   1741 C C    . TRP A 1 321 ? 130.87400 102.15400 109.08400 1.000 20.79658  ? 321 TRP A C    1 
ATOM   1742 O O    . TRP A 1 321 ? 131.39400 101.94600 110.18500 1.000 31.03711  ? 321 TRP A O    1 
ATOM   1743 C CB   . TRP A 1 321 ? 129.34000 104.07000 109.46000 1.000 25.17021  ? 321 TRP A CB   1 
ATOM   1744 C CG   . TRP A 1 321 ? 129.27900 105.55200 109.66200 1.000 21.63108  ? 321 TRP A CG   1 
ATOM   1745 C CD1  . TRP A 1 321 ? 128.84700 106.48100 108.76400 1.000 17.30952  ? 321 TRP A CD1  1 
ATOM   1746 C CD2  . TRP A 1 321 ? 129.63700 106.27400 110.84600 1.000 24.94883  ? 321 TRP A CD2  1 
ATOM   1747 N NE1  . TRP A 1 321 ? 128.92600 107.73900 109.30800 1.000 25.74007  ? 321 TRP A NE1  1 
ATOM   1748 C CE2  . TRP A 1 321 ? 129.40700 107.63900 110.58700 1.000 27.00119  ? 321 TRP A CE2  1 
ATOM   1749 C CE3  . TRP A 1 321 ? 130.13500 105.90100 112.09800 1.000 17.17522  ? 321 TRP A CE3  1 
ATOM   1750 C CZ2  . TRP A 1 321 ? 129.65600 108.63100 111.53100 1.000 19.94835  ? 321 TRP A CZ2  1 
ATOM   1751 C CZ3  . TRP A 1 321 ? 130.38200 106.88600 113.03300 1.000 18.74416  ? 321 TRP A CZ3  1 
ATOM   1752 C CH2  . TRP A 1 321 ? 130.14300 108.23400 112.74600 1.000 18.24750  ? 321 TRP A CH2  1 
ATOM   1753 N N    . GLU A 1 322 ? 130.57200 101.17100 108.23600 1.000 25.82805  ? 322 GLU A N    1 
ATOM   1754 C CA   . GLU A 1 322 ? 130.73000 99.76200  108.56100 1.000 18.63979  ? 322 GLU A CA   1 
ATOM   1755 C C    . GLU A 1 322 ? 132.17800 99.30000  108.38900 1.000 19.92526  ? 322 GLU A C    1 
ATOM   1756 O O    . GLU A 1 322 ? 132.90000 99.79600  107.52100 1.000 23.36291  ? 322 GLU A O    1 
ATOM   1757 C CB   . GLU A 1 322 ? 129.81000 98.91900  107.68700 1.000 16.34654  ? 322 GLU A CB   1 
ATOM   1758 C CG   . GLU A 1 322 ? 128.33600 99.18500  107.93800 1.000 13.99281  ? 322 GLU A CG   1 
ATOM   1759 C CD   . GLU A 1 322 ? 127.43500 98.50600  106.93200 1.000 20.97640  ? 322 GLU A CD   1 
ATOM   1760 O OE1  . GLU A 1 322 ? 127.94600 98.03200  105.89800 1.000 34.83810  ? 322 GLU A OE1  1 
ATOM   1761 O OE2  . GLU A 1 322 ? 126.21200 98.44700  107.17500 1.000 17.37146  ? 322 GLU A OE2  1 
ATOM   1762 N N    . PRO A 1 323 ? 132.62100 98.35100  109.21000 1.000 31.51935  ? 323 PRO A N    1 
ATOM   1763 C CA   . PRO A 1 323 ? 133.99900 97.85700  109.11800 1.000 31.53558  ? 323 PRO A CA   1 
ATOM   1764 C C    . PRO A 1 323 ? 134.14900 96.82100  108.01800 1.000 31.14698  ? 323 PRO A C    1 
ATOM   1765 O O    . PRO A 1 323 ? 133.15400 96.24900  107.54700 1.000 37.24757  ? 323 PRO A O    1 
ATOM   1766 C CB   . PRO A 1 323 ? 134.23600 97.23800  110.50200 1.000 28.87233  ? 323 PRO A CB   1 
ATOM   1767 C CG   . PRO A 1 323 ? 132.88100 96.78600  110.91500 1.000 28.84245  ? 323 PRO A CG   1 
ATOM   1768 C CD   . PRO A 1 323 ? 131.94800 97.86000  110.42600 1.000 30.66656  ? 323 PRO A CD   1 
ATOM   1769 N N    . PRO A 1 324 ? 135.38000 96.54700  107.58700 1.000 36.09428  ? 324 PRO A N    1 
ATOM   1770 C CA   . PRO A 1 324 ? 135.59200 95.57500  106.50800 1.000 35.38565  ? 324 PRO A CA   1 
ATOM   1771 C C    . PRO A 1 324 ? 135.13800 94.17500  106.89800 1.000 36.97771  ? 324 PRO A C    1 
ATOM   1772 O O    . PRO A 1 324 ? 135.40100 93.70100  108.00400 1.000 45.56765  ? 324 PRO A O    1 
ATOM   1773 C CB   . PRO A 1 324 ? 137.10700 95.62700  106.28200 1.000 32.89050  ? 324 PRO A CB   1 
ATOM   1774 C CG   . PRO A 1 324 ? 137.50900 96.97700  106.76900 1.000 39.69308  ? 324 PRO A CG   1 
ATOM   1775 C CD   . PRO A 1 324 ? 136.62400 97.24500  107.95100 1.000 35.66499  ? 324 PRO A CD   1 
ATOM   1776 N N    . HIS A 1 325 ? 134.45300 93.51100  105.96800 1.000 34.55522  ? 325 HIS A N    1 
ATOM   1777 C CA   . HIS A 1 325 ? 133.91600 92.18000  106.20800 1.000 27.60847  ? 325 HIS A CA   1 
ATOM   1778 C C    . HIS A 1 325 ? 133.76000 91.45000  104.88200 1.000 31.53074  ? 325 HIS A C    1 
ATOM   1779 O O    . HIS A 1 325 ? 133.56900 92.07100  103.83400 1.000 36.59568  ? 325 HIS A O    1 
ATOM   1780 C CB   . HIS A 1 325 ? 132.56700 92.24200  106.93600 1.000 28.08264  ? 325 HIS A CB   1 
ATOM   1781 C CG   . HIS A 1 325 ? 131.42200 92.62000  106.04900 1.000 31.19816  ? 325 HIS A CG   1 
ATOM   1782 N ND1  . HIS A 1 325 ? 131.15100 93.92500  105.69900 1.000 32.39118  ? 325 HIS A ND1  1 
ATOM   1783 C CD2  . HIS A 1 325 ? 130.48200 91.86400  105.43500 1.000 30.06616  ? 325 HIS A CD2  1 
ATOM   1784 C CE1  . HIS A 1 325 ? 130.09400 93.95700  104.90900 1.000 29.91899  ? 325 HIS A CE1  1 
ATOM   1785 N NE2  . HIS A 1 325 ? 129.66900 92.71900  104.73300 1.000 30.37364  ? 325 HIS A NE2  1 
ATOM   1786 N N    . GLY A 1 326 ? 133.84700 90.12300  104.94200 1.000 38.98280  ? 326 GLY A N    1 
ATOM   1787 C CA   . GLY A 1 326 ? 133.62700 89.27300  103.79500 1.000 35.48743  ? 326 GLY A CA   1 
ATOM   1788 C C    . GLY A 1 326 ? 134.46400 89.63800  102.58500 1.000 41.51047  ? 326 GLY A C    1 
ATOM   1789 O O    . GLY A 1 326 ? 135.68500 89.80100  102.66700 1.000 42.75956  ? 326 GLY A O    1 
ATOM   1790 N N    . PRO A 1 327 ? 133.81200 89.76900  101.42400 1.000 43.67881  ? 327 PRO A N    1 
ATOM   1791 C CA   . PRO A 1 327 ? 134.55100 90.09700  100.19600 1.000 38.63803  ? 327 PRO A CA   1 
ATOM   1792 C C    . PRO A 1 327 ? 134.96800 91.55100  100.10400 1.000 40.06915  ? 327 PRO A C    1 
ATOM   1793 O O    . PRO A 1 327 ? 135.85200 91.87400  99.29900  1.000 40.43671  ? 327 PRO A O    1 
ATOM   1794 C CB   . PRO A 1 327 ? 133.55400 89.74500  99.07600  1.000 34.61593  ? 327 PRO A CB   1 
ATOM   1795 C CG   . PRO A 1 327 ? 132.39900 89.04900  99.76100  1.000 33.43169  ? 327 PRO A CG   1 
ATOM   1796 C CD   . PRO A 1 327 ? 132.38100 89.57700  101.15200 1.000 40.40753  ? 327 PRO A CD   1 
ATOM   1797 N N    . TYR A 1 328 ? 134.35800 92.43500  100.89100 1.000 35.79279  ? 328 TYR A N    1 
ATOM   1798 C CA   . TYR A 1 328 ? 134.64300 93.86700  100.83200 1.000 34.50992  ? 328 TYR A CA   1 
ATOM   1799 C C    . TYR A 1 328 ? 135.76000 94.19000  101.82500 1.000 38.91059  ? 328 TYR A C    1 
ATOM   1800 O O    . TYR A 1 328 ? 135.57800 94.87700  102.83100 1.000 42.60092  ? 328 TYR A O    1 
ATOM   1801 C CB   . TYR A 1 328 ? 133.37700 94.66300  101.11900 1.000 34.44322  ? 328 TYR A CB   1 
ATOM   1802 C CG   . TYR A 1 328 ? 132.14500 94.06900  100.47600 1.000 34.90774  ? 328 TYR A CG   1 
ATOM   1803 C CD1  . TYR A 1 328 ? 131.97100 94.09600  99.10000  1.000 37.07354  ? 328 TYR A CD1  1 
ATOM   1804 C CD2  . TYR A 1 328 ? 131.16100 93.46600  101.24700 1.000 34.61192  ? 328 TYR A CD2  1 
ATOM   1805 C CE1  . TYR A 1 328 ? 130.84700 93.54700  98.51200  1.000 37.60452  ? 328 TYR A CE1  1 
ATOM   1806 C CE2  . TYR A 1 328 ? 130.03700 92.91600  100.66900 1.000 35.67528  ? 328 TYR A CE2  1 
ATOM   1807 C CZ   . TYR A 1 328 ? 129.88400 92.95800  99.30300  1.000 36.92888  ? 328 TYR A CZ   1 
ATOM   1808 O OH   . TYR A 1 328 ? 128.76300 92.41000  98.72700  1.000 35.17334  ? 328 TYR A OH   1 
ATOM   1809 N N    . LYS A 1 329 ? 136.94500 93.67500  101.51000 1.000 42.76064  ? 329 LYS A N    1 
ATOM   1810 C CA   . LYS A 1 329 ? 138.11500 93.79000  102.37900 1.000 45.05891  ? 329 LYS A CA   1 
ATOM   1811 C C    . LYS A 1 329 ? 138.99500 94.93400  101.88700 1.000 49.47960  ? 329 LYS A C    1 
ATOM   1812 O O    . LYS A 1 329 ? 139.85800 94.75600  101.02700 1.000 55.34434  ? 329 LYS A O    1 
ATOM   1813 C CB   . LYS A 1 329 ? 138.88200 92.47400  102.41500 1.000 45.53480  ? 329 LYS A CB   1 
ATOM   1814 C CG   . LYS A 1 329 ? 138.92100 91.75000  101.07900 1.000 45.90045  ? 329 LYS A CG   1 
ATOM   1815 C CD   . LYS A 1 329 ? 139.68200 90.43900  101.17700 1.000 49.19284  ? 329 LYS A CD   1 
ATOM   1816 C CE   . LYS A 1 329 ? 138.81500 89.33700  101.76200 1.000 50.34448  ? 329 LYS A CE   1 
ATOM   1817 N NZ   . LYS A 1 329 ? 137.55600 89.15100  100.99100 1.000 50.11766  ? 329 LYS A NZ   1 
ATOM   1818 N N    . SER A 1 330 ? 138.77000 96.12000  102.44300 1.000 49.58216  ? 330 SER A N    1 
ATOM   1819 C CA   . SER A 1 330 ? 139.58600 97.28700  102.14300 1.000 50.66131  ? 330 SER A CA   1 
ATOM   1820 C C    . SER A 1 330 ? 139.17700 98.41100  103.08100 1.000 54.36145  ? 330 SER A C    1 
ATOM   1821 O O    . SER A 1 330 ? 138.02800 98.47300  103.52800 1.000 53.44436  ? 330 SER A O    1 
ATOM   1822 C CB   . SER A 1 330 ? 139.43300 97.72500  100.68200 1.000 53.12816  ? 330 SER A CB   1 
ATOM   1823 O OG   . SER A 1 330 ? 140.45300 97.16600  99.87300  1.000 54.88232  ? 330 SER A OG   1 
ATOM   1824 N N    . PHE A 1 331 ? 140.13000 99.29900  103.37100 1.000 63.16156  ? 331 PHE A N    1 
ATOM   1825 C CA   . PHE A 1 331 ? 139.86100 100.37000 104.32500 1.000 63.42170  ? 331 PHE A CA   1 
ATOM   1826 C C    . PHE A 1 331 ? 138.84300 101.36300 103.77800 1.000 65.20937  ? 331 PHE A C    1 
ATOM   1827 O O    . PHE A 1 331 ? 137.96200 101.82500 104.51300 1.000 66.34653  ? 331 PHE A O    1 
ATOM   1828 C CB   . PHE A 1 331 ? 141.16300 101.07700 104.69600 1.000 65.27671  ? 331 PHE A CB   1 
ATOM   1829 C CG   . PHE A 1 331 ? 141.95800 100.36000 105.74900 1.000 68.06588  ? 331 PHE A CG   1 
ATOM   1830 C CD1  . PHE A 1 331 ? 141.33800 99.48300  106.62400 1.000 65.93427  ? 331 PHE A CD1  1 
ATOM   1831 C CD2  . PHE A 1 331 ? 143.32300 100.56000 105.86400 1.000 66.59622  ? 331 PHE A CD2  1 
ATOM   1832 C CE1  . PHE A 1 331 ? 142.06400 98.82000  107.59400 1.000 65.97849  ? 331 PHE A CE1  1 
ATOM   1833 C CE2  . PHE A 1 331 ? 144.05500 99.89900  106.83300 1.000 66.28163  ? 331 PHE A CE2  1 
ATOM   1834 C CZ   . PHE A 1 331 ? 143.42400 99.02900  107.69800 1.000 67.95374  ? 331 PHE A CZ   1 
ATOM   1835 N N    . ASN A 1 332 ? 138.94600 101.70500 102.49400 1.000 58.40304  ? 332 ASN A N    1 
ATOM   1836 C CA   . ASN A 1 332 ? 138.00300 102.60400 101.82700 1.000 55.66724  ? 332 ASN A CA   1 
ATOM   1837 C C    . ASN A 1 332 ? 137.48900 101.92300 100.56100 1.000 55.28428  ? 332 ASN A C    1 
ATOM   1838 O O    . ASN A 1 332 ? 138.06700 102.08500 99.48300  1.000 56.18610  ? 332 ASN A O    1 
ATOM   1839 C CB   . ASN A 1 332 ? 138.65900 103.94600 101.52000 1.000 57.33589  ? 332 ASN A CB   1 
ATOM   1840 C CG   . ASN A 1 332 ? 138.90500 104.77200 102.76600 1.000 62.40521  ? 332 ASN A CG   1 
ATOM   1841 O OD1  . ASN A 1 332 ? 137.98100 105.36000 103.32700 1.000 62.87820  ? 332 ASN A OD1  1 
ATOM   1842 N ND2  . ASN A 1 332 ? 140.15700 104.82300 103.20500 1.000 60.86906  ? 332 ASN A ND2  1 
ATOM   1843 N N    . TYR A 1 333 ? 136.41100 101.16300 100.69000 1.000 39.58550  ? 333 TYR A N    1 
ATOM   1844 C CA   . TYR A 1 333 ? 135.82100 100.52400 99.52100  1.000 37.03604  ? 333 TYR A CA   1 
ATOM   1845 C C    . TYR A 1 333 ? 135.21800 101.58100 98.60200  1.000 38.94608  ? 333 TYR A C    1 
ATOM   1846 O O    . TYR A 1 333 ? 134.50500 102.47300 99.07500  1.000 36.51159  ? 333 TYR A O    1 
ATOM   1847 C CB   . TYR A 1 333 ? 134.75900 99.50700  99.92700  1.000 33.71459  ? 333 TYR A CB   1 
ATOM   1848 C CG   . TYR A 1 333 ? 134.64000 98.36100  98.95000  1.000 34.53108  ? 333 TYR A CG   1 
ATOM   1849 C CD1  . TYR A 1 333 ? 135.66300 97.43400  98.81300  1.000 35.84195  ? 333 TYR A CD1  1 
ATOM   1850 C CD2  . TYR A 1 333 ? 133.51200 98.21500  98.15400  1.000 28.38076  ? 333 TYR A CD2  1 
ATOM   1851 C CE1  . TYR A 1 333 ? 135.56300 96.39000  97.91700  1.000 34.07403  ? 333 TYR A CE1  1 
ATOM   1852 C CE2  . TYR A 1 333 ? 133.40300 97.17400  97.25600  1.000 29.41239  ? 333 TYR A CE2  1 
ATOM   1853 C CZ   . TYR A 1 333 ? 134.43200 96.26400  97.14200  1.000 34.88192  ? 333 TYR A CZ   1 
ATOM   1854 O OH   . TYR A 1 333 ? 134.33200 95.22500  96.24800  1.000 39.48401  ? 333 TYR A OH   1 
ATOM   1855 N N    . PRO A 1 334 ? 135.48000 101.52100 97.29700  1.000 37.91890  ? 334 PRO A N    1 
ATOM   1856 C CA   . PRO A 1 334 ? 134.90800 102.51300 96.37800  1.000 32.34081  ? 334 PRO A CA   1 
ATOM   1857 C C    . PRO A 1 334 ? 133.41600 102.32900 96.14800  1.000 27.26155  ? 334 PRO A C    1 
ATOM   1858 O O    . PRO A 1 334 ? 132.99500 101.94900 95.05200  1.000 32.56879  ? 334 PRO A O    1 
ATOM   1859 C CB   . PRO A 1 334 ? 135.70900 102.28800 95.09100  1.000 32.89268  ? 334 PRO A CB   1 
ATOM   1860 C CG   . PRO A 1 334 ? 136.08600 100.84900 95.14900  1.000 31.57667  ? 334 PRO A CG   1 
ATOM   1861 C CD   . PRO A 1 334 ? 136.35500 100.56200 96.60000  1.000 31.59598  ? 334 PRO A CD   1 
ATOM   1862 N N    . TRP A 1 335 ? 132.60600 102.60100 97.17300  1.000 29.63481  ? 335 TRP A N    1 
ATOM   1863 C CA   . TRP A 1 335 ? 131.15700 102.48400 97.04700  1.000 25.04106  ? 335 TRP A CA   1 
ATOM   1864 C C    . TRP A 1 335 ? 130.56000 103.51100 96.09500  1.000 31.43647  ? 335 TRP A C    1 
ATOM   1865 O O    . TRP A 1 335 ? 129.39400 103.36600 95.71300  1.000 32.54052  ? 335 TRP A O    1 
ATOM   1866 C CB   . TRP A 1 335 ? 130.49200 102.62700 98.41900  1.000 26.08669  ? 335 TRP A CB   1 
ATOM   1867 C CG   . TRP A 1 335 ? 130.71900 101.46900 99.34100  1.000 28.09742  ? 335 TRP A CG   1 
ATOM   1868 C CD1  . TRP A 1 335 ? 131.36000 101.49500 100.54300 1.000 22.63976  ? 335 TRP A CD1  1 
ATOM   1869 C CD2  . TRP A 1 335 ? 130.28900 100.11700 99.14400  1.000 35.63625  ? 335 TRP A CD2  1 
ATOM   1870 N NE1  . TRP A 1 335 ? 131.36600 100.24200 101.10400 1.000 26.37988  ? 335 TRP A NE1  1 
ATOM   1871 C CE2  . TRP A 1 335 ? 130.71400 99.37700  100.26500 1.000 31.06870  ? 335 TRP A CE2  1 
ATOM   1872 C CE3  . TRP A 1 335 ? 129.59000 99.45900  98.12800  1.000 33.05926  ? 335 TRP A CE3  1 
ATOM   1873 C CZ2  . TRP A 1 335 ? 130.46400 98.01400  100.39700 1.000 28.73484  ? 335 TRP A CZ2  1 
ATOM   1874 C CZ3  . TRP A 1 335 ? 129.34400 98.10600  98.26100  1.000 29.42416  ? 335 TRP A CZ3  1 
ATOM   1875 C CH2  . TRP A 1 335 ? 129.78000 97.39800  99.38700  1.000 31.27809  ? 335 TRP A CH2  1 
ATOM   1876 N N    . LYS A 1 336 ? 131.31900 104.53300 95.70200  1.000 39.02869  ? 336 LYS A N    1 
ATOM   1877 C CA   . LYS A 1 336 ? 130.81600 105.57000 94.81000  1.000 33.46377  ? 336 LYS A CA   1 
ATOM   1878 C C    . LYS A 1 336 ? 130.87800 105.18700 93.33700  1.000 38.11753  ? 336 LYS A C    1 
ATOM   1879 O O    . LYS A 1 336 ? 130.36100 105.93700 92.50300  1.000 41.54285  ? 336 LYS A O    1 
ATOM   1880 C CB   . LYS A 1 336 ? 131.59300 106.87000 95.02700  1.000 33.77956  ? 336 LYS A CB   1 
ATOM   1881 C CG   . LYS A 1 336 ? 133.07300 106.76500 94.71100  1.000 35.50318  ? 336 LYS A CG   1 
ATOM   1882 C CD   . LYS A 1 336 ? 133.69800 108.13900 94.54500  1.000 42.70324  ? 336 LYS A CD   1 
ATOM   1883 C CE   . LYS A 1 336 ? 134.98500 108.06500 93.74200  1.000 43.06294  ? 336 LYS A CE   1 
ATOM   1884 N NZ   . LYS A 1 336 ? 135.65800 106.74700 93.89300  1.000 43.12910  ? 336 LYS A NZ   1 
ATOM   1885 N N    . ASN A 1 337 ? 131.49000 104.05600 92.99100  1.000 30.05839  ? 337 ASN A N    1 
ATOM   1886 C CA   . ASN A 1 337 ? 131.52400 103.60300 91.60800  1.000 24.31540  ? 337 ASN A CA   1 
ATOM   1887 C C    . ASN A 1 337 ? 130.33300 102.72800 91.24200  1.000 34.22721  ? 337 ASN A C    1 
ATOM   1888 O O    . ASN A 1 337 ? 130.18600 102.36400 90.07100  1.000 36.93161  ? 337 ASN A O    1 
ATOM   1889 C CB   . ASN A 1 337 ? 132.82300 102.84300 91.32900  1.000 26.86346  ? 337 ASN A CB   1 
ATOM   1890 C CG   . ASN A 1 337 ? 133.99700 103.76800 91.09100  1.000 32.04116  ? 337 ASN A CG   1 
ATOM   1891 O OD1  . ASN A 1 337 ? 134.45300 104.45700 92.00100  1.000 39.02112  ? 337 ASN A OD1  1 
ATOM   1892 N ND2  . ASN A 1 337 ? 134.49300 103.79000 89.86200  1.000 33.90620  ? 337 ASN A ND2  1 
ATOM   1893 N N    . TYR A 1 338 ? 129.49200 102.37800 92.21500  1.000 33.61352  ? 338 TYR A N    1 
ATOM   1894 C CA   . TYR A 1 338 ? 128.24000 101.68600 91.93800  1.000 19.89099  ? 338 TYR A CA   1 
ATOM   1895 C C    . TYR A 1 338 ? 127.16700 102.67300 91.48900  1.000 27.20854  ? 338 TYR A C    1 
ATOM   1896 O O    . TYR A 1 338 ? 126.35700 102.37300 90.60000  1.000 40.09137  ? 338 TYR A O    1 
ATOM   1897 C CB   . TYR A 1 338 ? 127.78900 100.93300 93.19100  1.000 27.09064  ? 338 TYR A CB   1 
ATOM   1898 C CG   . TYR A 1 338 ? 128.53800 99.64300  93.44900  1.000 28.27570  ? 338 TYR A CG   1 
ATOM   1899 C CD1  . TYR A 1 338 ? 129.80300 99.66000  94.02200  1.000 29.12114  ? 338 TYR A CD1  1 
ATOM   1900 C CD2  . TYR A 1 338 ? 127.97700 98.41100  93.14400  1.000 24.92576  ? 338 TYR A CD2  1 
ATOM   1901 C CE1  . TYR A 1 338 ? 130.49500 98.49200  94.26800  1.000 22.32373  ? 338 TYR A CE1  1 
ATOM   1902 C CE2  . TYR A 1 338 ? 128.66200 97.23500  93.38700  1.000 28.76337  ? 338 TYR A CE2  1 
ATOM   1903 C CZ   . TYR A 1 338 ? 129.92100 97.28200  93.94900  1.000 31.02476  ? 338 TYR A CZ   1 
ATOM   1904 O OH   . TYR A 1 338 ? 130.60800 96.11600  94.19500  1.000 29.32630  ? 338 TYR A OH   1 
ATOM   1905 N N    . VAL A 1 339 ? 127.17300 103.86600 92.08700  1.000 24.12032  ? 339 VAL A N    1 
ATOM   1906 C CA   . VAL A 1 339 ? 126.18900 104.89100 91.75900  1.000 23.97350  ? 339 VAL A CA   1 
ATOM   1907 C C    . VAL A 1 339 ? 126.37900 105.39000 90.33100  1.000 19.30859  ? 339 VAL A C    1 
ATOM   1908 O O    . VAL A 1 339 ? 125.40700 105.71900 89.64400  1.000 31.00540  ? 339 VAL A O    1 
ATOM   1909 C CB   . VAL A 1 339 ? 126.27000 106.04000 92.78000  1.000 29.67432  ? 339 VAL A CB   1 
ATOM   1910 C CG1  . VAL A 1 339 ? 125.18900 107.07200 92.51200  1.000 30.76227  ? 339 VAL A CG1  1 
ATOM   1911 C CG2  . VAL A 1 339 ? 126.16500 105.50000 94.19800  1.000 22.67320  ? 339 VAL A CG2  1 
ATOM   1912 N N    . LYS A 1 340 ? 127.62700 105.46800 89.86200  1.000 12.16646  ? 340 LYS A N    1 
ATOM   1913 C CA   . LYS A 1 340 ? 127.86200 105.90100 88.48800  1.000 21.27703  ? 340 LYS A CA   1 
ATOM   1914 C C    . LYS A 1 340 ? 127.25600 104.92500 87.48500  1.000 21.38597  ? 340 LYS A C    1 
ATOM   1915 O O    . LYS A 1 340 ? 126.63200 105.33700 86.49600  1.000 30.83684  ? 340 LYS A O    1 
ATOM   1916 C CB   . LYS A 1 340 ? 129.36100 106.05600 88.23700  1.000 23.55411  ? 340 LYS A CB   1 
ATOM   1917 C CG   . LYS A 1 340 ? 129.86900 107.47600 88.36900  1.000 28.42711  ? 340 LYS A CG   1 
ATOM   1918 C CD   . LYS A 1 340 ? 131.22900 107.63200 87.72000  1.000 26.04108  ? 340 LYS A CD   1 
ATOM   1919 C CE   . LYS A 1 340 ? 131.38500 106.67900 86.55100  1.000 28.79782  ? 340 LYS A CE   1 
ATOM   1920 N NZ   . LYS A 1 340 ? 132.63300 106.94200 85.78300  1.000 31.42160  ? 340 LYS A NZ   1 
ATOM   1921 N N    . LEU A 1 341 ? 127.41400 103.62400 87.73500  1.000 15.95637  ? 341 LEU A N    1 
ATOM   1922 C CA   . LEU A 1 341 ? 126.82800 102.62200 86.85300  1.000 20.47887  ? 341 LEU A CA   1 
ATOM   1923 C C    . LEU A 1 341 ? 125.30600 102.65700 86.93000  1.000 17.18337  ? 341 LEU A C    1 
ATOM   1924 O O    . LEU A 1 341 ? 124.61900 102.51100 85.90800  1.000 24.95847  ? 341 LEU A O    1 
ATOM   1925 C CB   . LEU A 1 341 ? 127.37200 101.24000 87.21800  1.000 23.53645  ? 341 LEU A CB   1 
ATOM   1926 C CG   . LEU A 1 341 ? 127.02500 100.03400 86.34500  1.000 27.92598  ? 341 LEU A CG   1 
ATOM   1927 C CD1  . LEU A 1 341 ? 127.46500 100.26500 84.91100  1.000 16.01036  ? 341 LEU A CD1  1 
ATOM   1928 C CD2  . LEU A 1 341 ? 127.67300 98.78200  86.90600  1.000 23.21479  ? 341 LEU A CD2  1 
ATOM   1929 N N    . SER A 1 342 ? 124.76100 102.89400 88.12600  1.000 6.14940   ? 342 SER A N    1 
ATOM   1930 C CA   . SER A 1 342 ? 123.31200 103.02400 88.24900  1.000 19.24978  ? 342 SER A CA   1 
ATOM   1931 C C    . SER A 1 342 ? 122.79500 104.22800 87.46500  1.000 28.92139  ? 342 SER A C    1 
ATOM   1932 O O    . SER A 1 342 ? 121.73500 104.15900 86.82900  1.000 33.70861  ? 342 SER A O    1 
ATOM   1933 C CB   . SER A 1 342 ? 122.91800 103.13100 89.72100  1.000 18.41786  ? 342 SER A CB   1 
ATOM   1934 O OG   . SER A 1 342 ? 122.61500 101.85800 90.25900  1.000 30.95219  ? 342 SER A OG   1 
ATOM   1935 N N    . GLY A 1 343 ? 123.53400 105.33900 87.48900  1.000 20.71792  ? 343 GLY A N    1 
ATOM   1936 C CA   . GLY A 1 343 ? 123.12000 106.50700 86.72800  1.000 12.72367  ? 343 GLY A CA   1 
ATOM   1937 C C    . GLY A 1 343 ? 123.18300 106.28600 85.22900  1.000 19.82356  ? 343 GLY A C    1 
ATOM   1938 O O    . GLY A 1 343 ? 122.29700 106.72700 84.48600  1.000 29.21788  ? 343 GLY A O    1 
ATOM   1939 N N    . ALA A 1 344 ? 124.22100 105.58900 84.76100  1.000 17.86807  ? 344 ALA A N    1 
ATOM   1940 C CA   . ALA A 1 344 ? 124.28600 105.26000 83.34000  1.000 21.77566  ? 344 ALA A CA   1 
ATOM   1941 C C    . ALA A 1 344 ? 123.11300 104.37100 82.93400  1.000 22.79733  ? 344 ALA A C    1 
ATOM   1942 O O    . ALA A 1 344 ? 122.52500 104.54600 81.85600  1.000 25.88275  ? 344 ALA A O    1 
ATOM   1943 C CB   . ALA A 1 344 ? 125.61900 104.58700 83.01900  1.000 14.61856  ? 344 ALA A CB   1 
ATOM   1944 N N    . LEU A 1 345 ? 122.71800 103.44700 83.81400  1.000 20.04144  ? 345 LEU A N    1 
ATOM   1945 C CA   . LEU A 1 345 ? 121.58800 102.58500 83.48700  1.000 18.71892  ? 345 LEU A CA   1 
ATOM   1946 C C    . LEU A 1 345 ? 120.26800 103.35200 83.50900  1.000 21.76589  ? 345 LEU A C    1 
ATOM   1947 O O    . LEU A 1 345 ? 119.36400 103.04900 82.72300  1.000 28.28403  ? 345 LEU A O    1 
ATOM   1948 C CB   . LEU A 1 345 ? 121.54000 101.40300 84.45400  1.000 26.58469  ? 345 LEU A CB   1 
ATOM   1949 C CG   . LEU A 1 345 ? 120.51500 100.30700 84.16400  1.000 26.73965  ? 345 LEU A CG   1 
ATOM   1950 C CD1  . LEU A 1 345 ? 120.95900 99.45200  82.98800  1.000 21.61399  ? 345 LEU A CD1  1 
ATOM   1951 C CD2  . LEU A 1 345 ? 120.29800 99.45400  85.39500  1.000 25.85518  ? 345 LEU A CD2  1 
ATOM   1952 N N    . LYS A 1 346 ? 120.14400 104.35900 84.37500  1.000 17.99363  ? 346 LYS A N    1 
ATOM   1953 C CA   . LYS A 1 346 ? 118.94300 105.19300 84.36900  1.000 23.44198  ? 346 LYS A CA   1 
ATOM   1954 C C    . LYS A 1 346 ? 118.84800 106.01600 83.08600  1.000 19.65333  ? 346 LYS A C    1 
ATOM   1955 O O    . LYS A 1 346 ? 117.75800 106.17300 82.50200  1.000 22.09810  ? 346 LYS A O    1 
ATOM   1956 C CB   . LYS A 1 346 ? 118.95400 106.10300 85.59700  1.000 22.77869  ? 346 LYS A CB   1 
ATOM   1957 C CG   . LYS A 1 346 ? 117.63900 106.78200 85.90900  1.000 26.13340  ? 346 LYS A CG   1 
ATOM   1958 C CD   . LYS A 1 346 ? 117.87700 108.05400 86.70300  1.000 28.00430  ? 346 LYS A CD   1 
ATOM   1959 C CE   . LYS A 1 346 ? 116.58100 108.79100 86.98000  1.000 36.90628  ? 346 LYS A CE   1 
ATOM   1960 N NZ   . LYS A 1 346 ? 116.62100 109.49000 88.29300  1.000 31.32247  ? 346 LYS A NZ   1 
ATOM   1961 N N    . HIS A 1 347 ? 119.99100 106.52100 82.61500  1.000 17.59775  ? 347 HIS A N    1 
ATOM   1962 C CA   . HIS A 1 347 ? 120.00100 107.23700 81.34600  1.000 19.85316  ? 347 HIS A CA   1 
ATOM   1963 C C    . HIS A 1 347 ? 119.62000 106.31500 80.19900  1.000 29.52797  ? 347 HIS A C    1 
ATOM   1964 O O    . HIS A 1 347 ? 118.97600 106.75000 79.23900  1.000 29.93981  ? 347 HIS A O    1 
ATOM   1965 C CB   . HIS A 1 347 ? 121.37300 107.85800 81.09300  1.000 17.56619  ? 347 HIS A CB   1 
ATOM   1966 C CG   . HIS A 1 347 ? 121.38400 108.85800 79.97800  1.000 24.82200  ? 347 HIS A CG   1 
ATOM   1967 N ND1  . HIS A 1 347 ? 122.20400 108.73600 78.87800  1.000 25.42446  ? 347 HIS A ND1  1 
ATOM   1968 C CD2  . HIS A 1 347 ? 120.67300 109.99500 79.79300  1.000 26.20560  ? 347 HIS A CD2  1 
ATOM   1969 C CE1  . HIS A 1 347 ? 121.99800 109.75400 78.06200  1.000 23.68131  ? 347 HIS A CE1  1 
ATOM   1970 N NE2  . HIS A 1 347 ? 121.07400 110.53300 78.59500  1.000 25.97761  ? 347 HIS A NE2  1 
ATOM   1971 N N    . CYS A 1 348 ? 120.00700 105.04100 80.28000  1.000 30.35108  ? 348 CYS A N    1 
ATOM   1972 C CA   . CYS A 1 348 ? 119.58600 104.09600 79.24900  1.000 23.04436  ? 348 CYS A CA   1 
ATOM   1973 C C    . CYS A 1 348 ? 118.10800 103.72400 79.37200  1.000 29.12368  ? 348 CYS A C    1 
ATOM   1974 O O    . CYS A 1 348 ? 117.47200 103.39800 78.36400  1.000 29.30421  ? 348 CYS A O    1 
ATOM   1975 C CB   . CYS A 1 348 ? 120.45200 102.83700 79.31000  1.000 24.31187  ? 348 CYS A CB   1 
ATOM   1976 S SG   . CYS A 1 348 ? 120.09500 101.61700 78.03300  1.000 43.13726  ? 348 CYS A SG   1 
ATOM   1977 N N    . ALA A 1 349 ? 117.54400 103.77200 80.58300  1.000 30.66688  ? 349 ALA A N    1 
ATOM   1978 C CA   . ALA A 1 349 ? 116.15200 103.37800 80.79400  1.000 22.78219  ? 349 ALA A CA   1 
ATOM   1979 C C    . ALA A 1 349 ? 115.14200 104.46800 80.44800  1.000 29.03874  ? 349 ALA A C    1 
ATOM   1980 O O    . ALA A 1 349 ? 113.95200 104.16200 80.25400  1.000 34.34558  ? 349 ALA A O    1 
ATOM   1981 C CB   . ALA A 1 349 ? 115.94600 102.94400 82.24600  1.000 22.32550  ? 349 ALA A CB   1 
ATOM   1982 N N    . PHE A 1 350 ? 115.57300 105.72800 80.35600  1.000 31.29556  ? 350 PHE A N    1 
ATOM   1983 C CA   . PHE A 1 350 ? 114.61200 106.74700 79.92900  1.000 25.66089  ? 350 PHE A CA   1 
ATOM   1984 C C    . PHE A 1 350 ? 114.09300 106.50700 78.50800  1.000 28.03274  ? 350 PHE A C    1 
ATOM   1985 O O    . PHE A 1 350 ? 112.94800 106.87000 78.20000  1.000 32.23996  ? 350 PHE A O    1 
ATOM   1986 C CB   . PHE A 1 350 ? 115.24000 108.14000 80.00800  1.000 26.21943  ? 350 PHE A CB   1 
ATOM   1987 C CG   . PHE A 1 350 ? 115.24700 108.73000 81.38800  1.000 28.11581  ? 350 PHE A CG   1 
ATOM   1988 C CD1  . PHE A 1 350 ? 114.13000 108.64200 82.19900  1.000 36.20130  ? 350 PHE A CD1  1 
ATOM   1989 C CD2  . PHE A 1 350 ? 116.37100 109.37700 81.87200  1.000 32.48473  ? 350 PHE A CD2  1 
ATOM   1990 C CE1  . PHE A 1 350 ? 114.13600 109.18600 83.46900  1.000 37.63514  ? 350 PHE A CE1  1 
ATOM   1991 C CE2  . PHE A 1 350 ? 116.38100 109.92100 83.14100  1.000 28.87378  ? 350 PHE A CE2  1 
ATOM   1992 C CZ   . PHE A 1 350 ? 115.26300 109.82600 83.94000  1.000 29.19475  ? 350 PHE A CZ   1 
ATOM   1993 N N    . THR A 1 351 ? 114.84500 105.78700 77.67400  1.000 28.93356  ? 351 THR A N    1 
ATOM   1994 C CA   . THR A 1 351 ? 114.36300 105.50000 76.32800  1.000 23.72072  ? 351 THR A CA   1 
ATOM   1995 C C    . THR A 1 351 ? 113.36600 104.34900 76.31700  1.000 24.52804  ? 351 THR A C    1 
ATOM   1996 O O    . THR A 1 351 ? 112.43700 104.34200 75.50000  1.000 27.07177  ? 351 THR A O    1 
ATOM   1997 C CB   . THR A 1 351 ? 115.53800 105.18900 75.39900  1.000 30.75143  ? 351 THR A CB   1 
ATOM   1998 O OG1  . THR A 1 351 ? 116.40700 106.32500 75.33100  1.000 27.75802  ? 351 THR A OG1  1 
ATOM   1999 C CG2  . THR A 1 351 ? 115.04100 104.86100 74.00200  1.000 30.97859  ? 351 THR A CG2  1 
ATOM   2000 N N    . VAL A 1 352 ? 113.50400 103.39500 77.23800  1.000 26.47192  ? 352 VAL A N    1 
ATOM   2001 C CA   . VAL A 1 352 ? 112.49400 102.35100 77.33400  1.000 26.95281  ? 352 VAL A CA   1 
ATOM   2002 C C    . VAL A 1 352 ? 111.20700 102.93900 77.88800  1.000 25.23632  ? 352 VAL A C    1 
ATOM   2003 O O    . VAL A 1 352 ? 110.10400 102.53300 77.49400  1.000 31.64840  ? 352 VAL A O    1 
ATOM   2004 C CB   . VAL A 1 352 ? 113.00700 101.18300 78.19700  1.000 29.10432  ? 352 VAL A CB   1 
ATOM   2005 C CG1  . VAL A 1 352 ? 112.14300 99.95100  77.99600  1.000 25.29866  ? 352 VAL A CG1  1 
ATOM   2006 C CG2  . VAL A 1 352 ? 114.45500 100.87900 77.86400  1.000 30.77277  ? 352 VAL A CG2  1 
ATOM   2007 N N    . MET A 1 353 ? 111.31700 103.93900 78.76700  1.000 26.12129  ? 353 MET A N    1 
ATOM   2008 C CA   . MET A 1 353 ? 110.10300 104.61700 79.20900  1.000 26.04271  ? 353 MET A CA   1 
ATOM   2009 C C    . MET A 1 353 ? 109.45600 105.40400 78.07300  1.000 29.80586  ? 353 MET A C    1 
ATOM   2010 O O    . MET A 1 353 ? 108.22200 105.45100 77.97400  1.000 33.70226  ? 353 MET A O    1 
ATOM   2011 C CB   . MET A 1 353 ? 110.40900 105.54300 80.38400  1.000 29.61198  ? 353 MET A CB   1 
ATOM   2012 C CG   . MET A 1 353 ? 109.28900 106.51500 80.70000  1.000 32.74310  ? 353 MET A CG   1 
ATOM   2013 S SD   . MET A 1 353 ? 109.84700 107.96600 81.60900  1.000 58.71975  ? 353 MET A SD   1 
ATOM   2014 C CE   . MET A 1 353 ? 109.86400 107.33100 83.28100  1.000 41.37207  ? 353 MET A CE   1 
ATOM   2015 N N    . ALA A 1 354 ? 110.26100 105.96300 77.16300  1.000 29.49559  ? 354 ALA A N    1 
ATOM   2016 C CA   . ALA A 1 354 ? 109.66200 106.65500 76.02400  1.000 20.31130  ? 354 ALA A CA   1 
ATOM   2017 C C    . ALA A 1 354 ? 109.04100 105.68200 75.02200  1.000 22.61225  ? 354 ALA A C    1 
ATOM   2018 O O    . ALA A 1 354 ? 108.03300 106.00900 74.38500  1.000 19.79069  ? 354 ALA A O    1 
ATOM   2019 C CB   . ALA A 1 354 ? 110.70400 107.53300 75.33400  1.000 24.10681  ? 354 ALA A CB   1 
ATOM   2020 N N    . LEU A 1 355 ? 109.56200 104.45700 74.92600  1.000 24.06212  ? 355 LEU A N    1 
ATOM   2021 C CA   . LEU A 1 355 ? 108.92500 103.48100 74.04400  1.000 20.71674  ? 355 LEU A CA   1 
ATOM   2022 C C    . LEU A 1 355 ? 107.63100 102.94500 74.64500  1.000 32.92424  ? 355 LEU A C    1 
ATOM   2023 O O    . LEU A 1 355 ? 106.65400 102.70000 73.91600  1.000 24.72214  ? 355 LEU A O    1 
ATOM   2024 C CB   . LEU A 1 355 ? 109.88100 102.32300 73.75400  1.000 27.87742  ? 355 LEU A CB   1 
ATOM   2025 C CG   . LEU A 1 355 ? 111.01300 102.56200 72.75400  1.000 26.41631  ? 355 LEU A CG   1 
ATOM   2026 C CD1  . LEU A 1 355 ? 112.16100 101.60300 73.01800  1.000 24.65827  ? 355 LEU A CD1  1 
ATOM   2027 C CD2  . LEU A 1 355 ? 110.51800 102.42900 71.32500  1.000 22.26694  ? 355 LEU A CD2  1 
ATOM   2028 N N    . HIS A 1 356 ? 107.57600 102.82500 75.97300  1.000 41.80457  ? 356 HIS A N    1 
ATOM   2029 C CA   . HIS A 1 356 ? 106.31600 102.44600 76.59700  1.000 32.56372  ? 356 HIS A CA   1 
ATOM   2030 C C    . HIS A 1 356 ? 105.28400 103.55000 76.42500  1.000 32.94944  ? 356 HIS A C    1 
ATOM   2031 O O    . HIS A 1 356 ? 104.10100 103.27200 76.20000  1.000 34.37222  ? 356 HIS A O    1 
ATOM   2032 C CB   . HIS A 1 356 ? 106.51900 102.13000 78.07600  1.000 34.22032  ? 356 HIS A CB   1 
ATOM   2033 C CG   . HIS A 1 356 ? 105.28200 101.62800 78.75200  1.000 44.17294  ? 356 HIS A CG   1 
ATOM   2034 N ND1  . HIS A 1 356 ? 104.92300 102.00800 80.02700  1.000 43.89842  ? 356 HIS A ND1  1 
ATOM   2035 C CD2  . HIS A 1 356 ? 104.31700 100.78000 78.32600  1.000 41.57406  ? 356 HIS A CD2  1 
ATOM   2036 C CE1  . HIS A 1 356 ? 103.79100 101.41300 80.35800  1.000 41.58855  ? 356 HIS A CE1  1 
ATOM   2037 N NE2  . HIS A 1 356 ? 103.40200 100.66200 79.34400  1.000 39.56512  ? 356 HIS A NE2  1 
ATOM   2038 N N    . GLY A 1 357 ? 105.71000 104.81100 76.52100  1.000 34.05014  ? 357 GLY A N    1 
ATOM   2039 C CA   . GLY A 1 357 ? 104.79300 105.89700 76.22300  1.000 35.31030  ? 357 GLY A CA   1 
ATOM   2040 C C    . GLY A 1 357 ? 104.34900 105.90200 74.77300  1.000 35.61253  ? 357 GLY A C    1 
ATOM   2041 O O    . GLY A 1 357 ? 103.23500 106.33000 74.46100  1.000 31.79595  ? 357 GLY A O    1 
ATOM   2042 N N    . CYS A 1 358 ? 105.20900 105.42300 73.86800  1.000 42.81528  ? 358 CYS A N    1 
ATOM   2043 C CA   . CYS A 1 358 ? 104.80100 105.25300 72.47600  1.000 34.42504  ? 358 CYS A CA   1 
ATOM   2044 C C    . CYS A 1 358 ? 103.72100 104.19000 72.32400  1.000 32.92282  ? 358 CYS A C    1 
ATOM   2045 O O    . CYS A 1 358 ? 102.85500 104.31300 71.45100  1.000 33.47469  ? 358 CYS A O    1 
ATOM   2046 C CB   . CYS A 1 358 ? 106.00200 104.89100 71.60200  1.000 30.39466  ? 358 CYS A CB   1 
ATOM   2047 S SG   . CYS A 1 358 ? 106.88600 106.29800 70.90400  1.000 51.84219  ? 358 CYS A SG   1 
ATOM   2048 N N    . ILE A 1 359 ? 103.74900 103.14200 73.15100  1.000 42.28958  ? 359 ILE A N    1 
ATOM   2049 C CA   . ILE A 1 359 ? 102.71100 102.11700 73.02200  1.000 41.52665  ? 359 ILE A CA   1 
ATOM   2050 C C    . ILE A 1 359 ? 101.33300 102.64400 73.42500  1.000 41.10886  ? 359 ILE A C    1 
ATOM   2051 O O    . ILE A 1 359 ? 100.31600 102.21600 72.86600  1.000 42.76873  ? 359 ILE A O    1 
ATOM   2052 C CB   . ILE A 1 359 ? 103.07100 100.85800 73.83100  1.000 45.34782  ? 359 ILE A CB   1 
ATOM   2053 C CG1  . ILE A 1 359 ? 104.15800 100.05100 73.12200  1.000 41.68341  ? 359 ILE A CG1  1 
ATOM   2054 C CG2  . ILE A 1 359 ? 101.83700 99.99800  74.05400  1.000 39.04673  ? 359 ILE A CG2  1 
ATOM   2055 C CD1  . ILE A 1 359 ? 104.90100 99.10600  74.03600  1.000 38.62982  ? 359 ILE A CD1  1 
ATOM   2056 N N    . LEU A 1 360 ? 101.26200 103.56200 74.39200  1.000 47.35312  ? 360 LEU A N    1 
ATOM   2057 C CA   . LEU A 1 360 ? 99.99100  104.05900 74.91200  1.000 42.14802  ? 360 LEU A CA   1 
ATOM   2058 C C    . LEU A 1 360 ? 99.55000  105.37100 74.26800  1.000 44.24955  ? 360 LEU A C    1 
ATOM   2059 O O    . LEU A 1 360 ? 98.80600  106.14100 74.88500  1.000 45.19461  ? 360 LEU A O    1 
ATOM   2060 C CB   . LEU A 1 360 ? 100.06800 104.23400 76.42900  1.000 38.61284  ? 360 LEU A CB   1 
ATOM   2061 C CG   . LEU A 1 360 ? 100.32600 103.00400 77.29600  1.000 43.74706  ? 360 LEU A CG   1 
ATOM   2062 C CD1  . LEU A 1 360 ? 101.27900 103.35700 78.42300  1.000 42.56354  ? 360 LEU A CD1  1 
ATOM   2063 C CD2  . LEU A 1 360 ? 99.02400  102.45500 77.84700  1.000 45.27055  ? 360 LEU A CD2  1 
ATOM   2064 N N    . SER A 1 361 ? 99.97700  105.64300 73.04000  1.000 47.71440  ? 361 SER A N    1 
ATOM   2065 C CA   . SER A 1 361 ? 99.65000  106.91400 72.41300  1.000 43.20538  ? 361 SER A CA   1 
ATOM   2066 C C    . SER A 1 361 ? 98.23900  106.89800 71.82900  1.000 46.90442  ? 361 SER A C    1 
ATOM   2067 O O    . SER A 1 361 ? 97.61400  105.84800 71.66000  1.000 49.77589  ? 361 SER A O    1 
ATOM   2068 C CB   . SER A 1 361 ? 100.66200 107.24800 71.31700  1.000 46.69679  ? 361 SER A CB   1 
ATOM   2069 O OG   . SER A 1 361 ? 101.79300 107.91000 71.85400  1.000 50.51209  ? 361 SER A OG   1 
ATOM   2070 N N    . GLU A 1 362 ? 97.73900  108.09700 71.52300  1.000 53.22824  ? 362 GLU A N    1 
ATOM   2071 C CA   . GLU A 1 362 ? 96.39200  108.23800 70.98200  1.000 49.12417  ? 362 GLU A CA   1 
ATOM   2072 C C    . GLU A 1 362 ? 96.35800  108.00400 69.47800  1.000 51.42360  ? 362 GLU A C    1 
ATOM   2073 O O    . GLU A 1 362 ? 95.31400  107.62600 68.93600  1.000 54.95199  ? 362 GLU A O    1 
ATOM   2074 C CB   . GLU A 1 362 ? 95.83800  109.62700 71.30300  1.000 49.51609  ? 362 GLU A CB   1 
ATOM   2075 C CG   . GLU A 1 362 ? 95.39600  109.81200 72.74600  1.000 49.64535  ? 362 GLU A CG   1 
ATOM   2076 C CD   . GLU A 1 362 ? 93.89000  109.80200 72.90400  1.000 55.90425  ? 362 GLU A CD   1 
ATOM   2077 O OE1  . GLU A 1 362 ? 93.22600  110.69300 72.33600  1.000 60.12596  ? 362 GLU A OE1  1 
ATOM   2078 O OE2  . GLU A 1 362 ? 93.36900  108.90400 73.59800  1.000 56.04408  ? 362 GLU A OE2  1 
ATOM   2079 N N    . ILE A 1 363 ? 97.47700  108.22900 68.79500  1.000 49.63222  ? 363 ILE A N    1 
ATOM   2080 C CA   . ILE A 1 363 ? 97.60300  108.00600 67.35900  1.000 51.27678  ? 363 ILE A CA   1 
ATOM   2081 C C    . ILE A 1 363 ? 98.47900  106.77800 67.15100  1.000 51.26464  ? 363 ILE A C    1 
ATOM   2082 O O    . ILE A 1 363 ? 99.60700  106.72000 67.65600  1.000 50.01012  ? 363 ILE A O    1 
ATOM   2083 C CB   . ILE A 1 363 ? 98.18800  109.23500 66.64700  1.000 50.78527  ? 363 ILE A CB   1 
ATOM   2084 C CG1  . ILE A 1 363 ? 97.32500  110.46800 66.92400  1.000 49.07066  ? 363 ILE A CG1  1 
ATOM   2085 C CG2  . ILE A 1 363 ? 98.30500  108.98200 65.15300  1.000 48.96443  ? 363 ILE A CG2  1 
ATOM   2086 C CD1  . ILE A 1 363 ? 98.08400  111.77500 66.87900  1.000 45.41768  ? 363 ILE A CD1  1 
ATOM   2087 N N    . GLN A 1 364 ? 97.96200  105.79800 66.41200  1.000 53.45996  ? 364 GLN A N    1 
ATOM   2088 C CA   . GLN A 1 364 ? 98.66100  104.54400 66.17300  1.000 51.31500  ? 364 GLN A CA   1 
ATOM   2089 C C    . GLN A 1 364 ? 98.68200  104.23100 64.68400  1.000 50.27990  ? 364 GLN A C    1 
ATOM   2090 O O    . GLN A 1 364 ? 97.80200  104.65500 63.93100  1.000 54.26418  ? 364 GLN A O    1 
ATOM   2091 C CB   . GLN A 1 364 ? 98.00900  103.38700 66.93900  1.000 48.88826  ? 364 GLN A CB   1 
ATOM   2092 C CG   . GLN A 1 364 ? 97.52500  103.76500 68.32800  1.000 50.20069  ? 364 GLN A CG   1 
ATOM   2093 C CD   . GLN A 1 364 ? 98.31500  103.08200 69.42400  1.000 51.59498  ? 364 GLN A CD   1 
ATOM   2094 O OE1  . GLN A 1 364 ? 98.67000  101.91000 69.31000  1.000 55.15927  ? 364 GLN A OE1  1 
ATOM   2095 N NE2  . GLN A 1 364 ? 98.59700  103.81300 70.49300  1.000 49.57095  ? 364 GLN A NE2  1 
ATOM   2096 N N    . ALA A 1 365 ? 99.72100  103.46600 64.26100  1.000 51.68314  ? 365 ALA A N    1 
ATOM   2097 C CA   . ALA A 1 365 ? 99.93700  103.05300 62.88300  1.000 50.82459  ? 365 ALA A CA   1 
ATOM   2098 C C    . ALA A 1 365 ? 99.22800  101.73400 62.58600  1.000 52.37213  ? 365 ALA A C    1 
ATOM   2099 O O    . ALA A 1 365 ? 98.99400  100.92800 63.49200  1.000 51.16341  ? 365 ALA A O    1 
ATOM   2100 C CB   . ALA A 1 365 ? 101.42800 102.90300 62.60100  1.000 49.16355  ? 365 ALA A CB   1 
ATOM   2101 N N    . PRO A 1 366 ? 98.87800  101.49900 61.32400  1.000 59.18396  ? 366 PRO A N    1 
ATOM   2102 C CA   . PRO A 1 366 ? 98.18900  100.25400 60.96600  1.000 59.29293  ? 366 PRO A CA   1 
ATOM   2103 C C    . PRO A 1 366 ? 99.08000  99.03100  61.13100  1.000 59.66939  ? 366 PRO A C    1 
ATOM   2104 O O    . PRO A 1 366 ? 100.29600 99.08000  60.93600  1.000 59.30170  ? 366 PRO A O    1 
ATOM   2105 C CB   . PRO A 1 366 ? 97.80700  100.46900 59.49600  1.000 56.21317  ? 366 PRO A CB   1 
ATOM   2106 C CG   . PRO A 1 366 ? 98.75000  101.51200 59.00500  1.000 58.94516  ? 366 PRO A CG   1 
ATOM   2107 C CD   . PRO A 1 366 ? 99.01400  102.40900 60.17400  1.000 57.96161  ? 366 PRO A CD   1 
ATOM   2108 N N    . GLU A 1 367 ? 98.44200  97.91500  61.49500  1.000 62.15483  ? 367 GLU A N    1 
ATOM   2109 C CA   . GLU A 1 367 ? 99.16900  96.67100  61.73400  1.000 60.99947  ? 367 GLU A CA   1 
ATOM   2110 C C    . GLU A 1 367 ? 99.86500  96.17400  60.47200  1.000 61.32436  ? 367 GLU A C    1 
ATOM   2111 O O    . GLU A 1 367 ? 100.97500 95.62600  60.53700  1.000 60.78012  ? 367 GLU A O    1 
ATOM   2112 C CB   . GLU A 1 367 ? 98.20800  95.61000  62.27000  1.000 59.41774  ? 367 GLU A CB   1 
ATOM   2113 C CG   . GLU A 1 367 ? 98.86200  94.28900  62.62700  1.000 62.68433  ? 367 GLU A CG   1 
ATOM   2114 C CD   . GLU A 1 367 ? 97.96500  93.41100  63.47700  1.000 66.24986  ? 367 GLU A CD   1 
ATOM   2115 O OE1  . GLU A 1 367 ? 96.92300  93.90900  63.95200  1.000 64.68008  ? 367 GLU A OE1  1 
ATOM   2116 O OE2  . GLU A 1 367 ? 98.30100  92.22400  63.67000  1.000 64.94880  ? 367 GLU A OE2  1 
ATOM   2117 N N    . GLU A 1 368 ? 99.21800  96.33500  59.31500  1.000 63.73217  ? 368 GLU A N    1 
ATOM   2118 C CA   . GLU A 1 368 ? 99.78500  95.82500  58.07100  1.000 63.84063  ? 368 GLU A CA   1 
ATOM   2119 C C    . GLU A 1 368 ? 101.15300 96.43500  57.79900  1.000 64.62708  ? 368 GLU A C    1 
ATOM   2120 O O    . GLU A 1 368 ? 102.05100 95.76100  57.28100  1.000 63.47307  ? 368 GLU A O    1 
ATOM   2121 C CB   . GLU A 1 368 ? 98.83700  96.09700  56.90100  1.000 63.80886  ? 368 GLU A CB   1 
ATOM   2122 C CG   . GLU A 1 368 ? 97.49400  95.37300  56.96500  1.000 65.79575  ? 368 GLU A CG   1 
ATOM   2123 C CD   . GLU A 1 368 ? 96.65800  95.76000  58.17100  1.000 68.38809  ? 368 GLU A CD   1 
ATOM   2124 O OE1  . GLU A 1 368 ? 96.39200  96.96700  58.34800  1.000 66.61094  ? 368 GLU A OE1  1 
ATOM   2125 O OE2  . GLU A 1 368 ? 96.26600  94.85700  58.93900  1.000 69.68451  ? 368 GLU A OE2  1 
ATOM   2126 N N    . ARG A 1 369 ? 101.33000 97.71300  58.13500  1.000 60.73770  ? 369 ARG A N    1 
ATOM   2127 C CA   . ARG A 1 369 ? 102.63100 98.35000  57.98600  1.000 57.36777  ? 369 ARG A CA   1 
ATOM   2128 C C    . ARG A 1 369 ? 103.58100 98.00800  59.12400  1.000 55.61421  ? 369 ARG A C    1 
ATOM   2129 O O    . ARG A 1 369 ? 104.80000 98.06400  58.93200  1.000 58.50516  ? 369 ARG A O    1 
ATOM   2130 C CB   . ARG A 1 369 ? 102.46800 99.86700  57.88500  1.000 58.10911  ? 369 ARG A CB   1 
ATOM   2131 C CG   . ARG A 1 369 ? 102.12900 100.36000 56.48900  1.000 58.75858  ? 369 ARG A CG   1 
ATOM   2132 C CD   . ARG A 1 369 ? 101.35400 101.66500 56.53200  1.000 60.42760  ? 369 ARG A CD   1 
ATOM   2133 N NE   . ARG A 1 369 ? 100.47500 101.81600 55.37900  1.000 62.06154  ? 369 ARG A NE   1 
ATOM   2134 C CZ   . ARG A 1 369 ? 100.43300 102.89200 54.60600  1.000 61.92606  ? 369 ARG A CZ   1 
ATOM   2135 N NH1  . ARG A 1 369 ? 101.20800 103.93900 54.83500  1.000 59.08810  ? 369 ARG A NH1  1 
ATOM   2136 N NH2  . ARG A 1 369 ? 99.59100  102.91800 53.57700  1.000 61.59184  ? 369 ARG A NH2  1 
ATOM   2137 N N    . ARG A 1 370 ? 103.05600 97.65400  60.30000  1.000 47.54340  ? 370 ARG A N    1 
ATOM   2138 C CA   . ARG A 1 370 ? 103.92300 97.24400  61.39900  1.000 49.33466  ? 370 ARG A CA   1 
ATOM   2139 C C    . ARG A 1 370 ? 104.58500 95.90300  61.11200  1.000 51.43361  ? 370 ARG A C    1 
ATOM   2140 O O    . ARG A 1 370 ? 105.75200 95.69300  61.46300  1.000 50.90916  ? 370 ARG A O    1 
ATOM   2141 C CB   . ARG A 1 370 ? 103.13100 97.16300  62.70300  1.000 47.97974  ? 370 ARG A CB   1 
ATOM   2142 C CG   . ARG A 1 370 ? 102.72600 98.49500  63.29700  1.000 45.36557  ? 370 ARG A CG   1 
ATOM   2143 C CD   . ARG A 1 370 ? 102.10100 98.27800  64.66100  1.000 47.59538  ? 370 ARG A CD   1 
ATOM   2144 N NE   . ARG A 1 370 ? 101.20200 99.35800  65.04600  1.000 48.69271  ? 370 ARG A NE   1 
ATOM   2145 C CZ   . ARG A 1 370 ? 100.72900 99.53000  66.27200  1.000 43.62971  ? 370 ARG A CZ   1 
ATOM   2146 N NH1  . ARG A 1 370 ? 101.04700 98.70800  67.25700  1.000 39.64992  ? 370 ARG A NH1  1 
ATOM   2147 N NH2  . ARG A 1 370 ? 99.91400  100.55200 66.51400  1.000 48.29421  ? 370 ARG A NH2  1 
ATOM   2148 N N    . GLN A 1 371 ? 103.86000 94.98500  60.47200  1.000 57.76203  ? 371 GLN A N    1 
ATOM   2149 C CA   . GLN A 1 371 ? 104.38000 93.63600  60.27800  1.000 57.06506  ? 371 GLN A CA   1 
ATOM   2150 C C    . GLN A 1 371 ? 105.51100 93.56700  59.26000  1.000 55.50198  ? 371 GLN A C    1 
ATOM   2151 O O    . GLN A 1 371 ? 106.14900 92.51600  59.14400  1.000 61.33036  ? 371 GLN A O    1 
ATOM   2152 C CB   . GLN A 1 371 ? 103.25200 92.69200  59.86300  1.000 56.52952  ? 371 GLN A CB   1 
ATOM   2153 C CG   . GLN A 1 371 ? 102.01700 92.79100  60.74000  1.000 58.74096  ? 371 GLN A CG   1 
ATOM   2154 C CD   . GLN A 1 371 ? 102.33600 92.60600  62.21000  1.000 60.51134  ? 371 GLN A CD   1 
ATOM   2155 O OE1  . GLN A 1 371 ? 101.99100 93.44200  63.04400  1.000 61.24545  ? 371 GLN A OE1  1 
ATOM   2156 N NE2  . GLN A 1 371 ? 103.00000 91.50500  62.53600  1.000 59.99782  ? 371 GLN A NE2  1 
ATOM   2157 N N    . VAL A 1 372 ? 105.77200 94.64600  58.52000  1.000 52.29112  ? 372 VAL A N    1 
ATOM   2158 C CA   . VAL A 1 372 ? 106.87800 94.65300  57.57000  1.000 53.69292  ? 372 VAL A CA   1 
ATOM   2159 C C    . VAL A 1 372 ? 108.24400 94.70100  58.25200  1.000 53.71833  ? 372 VAL A C    1 
ATOM   2160 O O    . VAL A 1 372 ? 109.24200 94.29200  57.64700  1.000 56.49199  ? 372 VAL A O    1 
ATOM   2161 C CB   . VAL A 1 372 ? 106.71700 95.83100  56.59100  1.000 55.44223  ? 372 VAL A CB   1 
ATOM   2162 C CG1  . VAL A 1 372 ? 108.01600 96.09600  55.84800  1.000 53.14746  ? 372 VAL A CG1  1 
ATOM   2163 C CG2  . VAL A 1 372 ? 105.58600 95.55200  55.61500  1.000 51.75946  ? 372 VAL A CG2  1 
ATOM   2164 N N    . PHE A 1 373 ? 108.32600 95.18400  59.49500  1.000 52.73854  ? 373 PHE A N    1 
ATOM   2165 C CA   . PHE A 1 373 ? 109.60500 95.35300  60.18300  1.000 51.49009  ? 373 PHE A CA   1 
ATOM   2166 C C    . PHE A 1 373 ? 109.74000 94.46500  61.41900  1.000 52.37471  ? 373 PHE A C    1 
ATOM   2167 O O    . PHE A 1 373 ? 110.51500 94.78800  62.32400  1.000 54.98276  ? 373 PHE A O    1 
ATOM   2168 C CB   . PHE A 1 373 ? 109.80700 96.82000  60.56700  1.000 54.23410  ? 373 PHE A CB   1 
ATOM   2169 C CG   . PHE A 1 373 ? 109.64200 97.77900  59.42100  1.000 54.48459  ? 373 PHE A CG   1 
ATOM   2170 C CD1  . PHE A 1 373 ? 110.68600 98.01900  58.54500  1.000 55.79798  ? 373 PHE A CD1  1 
ATOM   2171 C CD2  . PHE A 1 373 ? 108.44300 98.44100  59.22100  1.000 51.31385  ? 373 PHE A CD2  1 
ATOM   2172 C CE1  . PHE A 1 373 ? 110.53700 98.90000  57.49100  1.000 53.11722  ? 373 PHE A CE1  1 
ATOM   2173 C CE2  . PHE A 1 373 ? 108.28800 99.32200  58.16900  1.000 52.61847  ? 373 PHE A CE2  1 
ATOM   2174 C CZ   . PHE A 1 373 ? 109.33600 99.55200  57.30300  1.000 51.43041  ? 373 PHE A CZ   1 
ATOM   2175 N N    . ARG A 1 374 ? 109.00700 93.35300  61.47600  1.000 53.50778  ? 374 ARG A N    1 
ATOM   2176 C CA   . ARG A 1 374 ? 108.97800 92.52900  62.68300  1.000 55.30403  ? 374 ARG A CA   1 
ATOM   2177 C C    . ARG A 1 374 ? 110.35100 91.93900  63.00500  1.000 59.70675  ? 374 ARG A C    1 
ATOM   2178 O O    . ARG A 1 374 ? 110.80800 91.97600  64.15800  1.000 62.02286  ? 374 ARG A O    1 
ATOM   2179 C CB   . ARG A 1 374 ? 107.94000 91.42000  62.50500  1.000 57.04705  ? 374 ARG A CB   1 
ATOM   2180 C CG   . ARG A 1 374 ? 107.50800 90.72300  63.78000  1.000 60.14137  ? 374 ARG A CG   1 
ATOM   2181 C CD   . ARG A 1 374 ? 106.95400 89.34100  63.47200  1.000 58.52429  ? 374 ARG A CD   1 
ATOM   2182 N NE   . ARG A 1 374 ? 106.38300 88.70000  64.64900  1.000 59.79105  ? 374 ARG A NE   1 
ATOM   2183 C CZ   . ARG A 1 374 ? 105.20400 89.00800  65.17000  1.000 61.51045  ? 374 ARG A CZ   1 
ATOM   2184 N NH1  . ARG A 1 374 ? 104.43900 89.94700  64.63900  1.000 61.72047  ? 374 ARG A NH1  1 
ATOM   2185 N NH2  . ARG A 1 374 ? 104.78000 88.35500  66.24800  1.000 59.31199  ? 374 ARG A NH2  1 
ATOM   2186 N N    . GLN A 1 375 ? 111.02700 91.39400  61.99000  1.000 60.57181  ? 375 GLN A N    1 
ATOM   2187 C CA   . GLN A 1 375 ? 112.24900 90.62700  62.21800  1.000 58.59614  ? 375 GLN A CA   1 
ATOM   2188 C C    . GLN A 1 375 ? 113.35100 91.48300  62.83600  1.000 58.63714  ? 375 GLN A C    1 
ATOM   2189 O O    . GLN A 1 375 ? 114.00800 91.07200  63.80200  1.000 64.07361  ? 375 GLN A O    1 
ATOM   2190 C CB   . GLN A 1 375 ? 112.72100 90.02400  60.89400  1.000 60.01045  ? 375 GLN A CB   1 
ATOM   2191 C CG   . GLN A 1 375 ? 111.87400 88.86200  60.39400  1.000 59.73225  ? 375 GLN A CG   1 
ATOM   2192 C CD   . GLN A 1 375 ? 112.22600 87.54700  61.05300  1.000 64.57958  ? 375 GLN A CD   1 
ATOM   2193 O OE1  . GLN A 1 375 ? 111.36300 86.87000  61.61300  1.000 63.97259  ? 375 GLN A OE1  1 
ATOM   2194 N NE2  . GLN A 1 375 ? 113.49700 87.17100  60.98100  1.000 64.61593  ? 375 GLN A NE2  1 
ATOM   2195 N N    . GLU A 1 376 ? 113.56100 92.68600  62.29500  1.000 46.06140  ? 376 GLU A N    1 
ATOM   2196 C CA   . GLU A 1 376 ? 114.65600 93.52700  62.76800  1.000 54.87369  ? 376 GLU A CA   1 
ATOM   2197 C C    . GLU A 1 376 ? 114.42000 94.00000  64.19600  1.000 54.36195  ? 376 GLU A C    1 
ATOM   2198 O O    . GLU A 1 376 ? 115.35400 94.03800  65.01100  1.000 59.28832  ? 376 GLU A O    1 
ATOM   2199 C CB   . GLU A 1 376 ? 114.83500 94.71900  61.83000  1.000 57.73413  ? 376 GLU A CB   1 
ATOM   2200 C CG   . GLU A 1 376 ? 115.75200 94.44500  60.65300  1.000 55.90780  ? 376 GLU A CG   1 
ATOM   2201 C CD   . GLU A 1 376 ? 115.01200 93.86600  59.46700  1.000 56.13523  ? 376 GLU A CD   1 
ATOM   2202 O OE1  . GLU A 1 376 ? 113.77600 93.71900  59.55300  1.000 55.54485  ? 376 GLU A OE1  1 
ATOM   2203 O OE2  . GLU A 1 376 ? 115.66700 93.55400  58.45100  1.000 58.24161  ? 376 GLU A OE2  1 
ATOM   2204 N N    . LEU A 1 377 ? 113.17200 94.33300  64.52900  1.000 40.03783  ? 377 LEU A N    1 
ATOM   2205 C CA   . LEU A 1 377 ? 112.88000 94.78700  65.88200  1.000 44.21755  ? 377 LEU A CA   1 
ATOM   2206 C C    . LEU A 1 377 ? 113.03800 93.64700  66.87700  1.000 46.35320  ? 377 LEU A C    1 
ATOM   2207 O O    . LEU A 1 377 ? 113.58300 93.84100  67.97500  1.000 50.70112  ? 377 LEU A O    1 
ATOM   2208 C CB   . LEU A 1 377 ? 111.46800 95.37000  65.94100  1.000 49.04881  ? 377 LEU A CB   1 
ATOM   2209 C CG   . LEU A 1 377 ? 111.12900 96.43400  64.89400  1.000 44.48107  ? 377 LEU A CG   1 
ATOM   2210 C CD1  . LEU A 1 377 ? 109.63200 96.48400  64.64000  1.000 45.20982  ? 377 LEU A CD1  1 
ATOM   2211 C CD2  . LEU A 1 377 ? 111.64800 97.80000  65.30500  1.000 45.35002  ? 377 LEU A CD2  1 
ATOM   2212 N N    . GLN A 1 378 ? 112.61200 92.43900  66.49700  1.000 44.97867  ? 378 GLN A N    1 
ATOM   2213 C CA   . GLN A 1 378 ? 112.77800 91.30600  67.40000  1.000 50.13818  ? 378 GLN A CA   1 
ATOM   2214 C C    . GLN A 1 378 ? 114.25500 91.01000  67.62600  1.000 50.52476  ? 378 GLN A C    1 
ATOM   2215 O O    . GLN A 1 378 ? 114.67600 90.72100  68.75500  1.000 54.86444  ? 378 GLN A O    1 
ATOM   2216 C CB   . GLN A 1 378 ? 112.05800 90.07800  66.84400  1.000 49.55961  ? 378 GLN A CB   1 
ATOM   2217 C CG   . GLN A 1 378 ? 110.54800 90.12500  66.99200  1.000 50.01746  ? 378 GLN A CG   1 
ATOM   2218 C CD   . GLN A 1 378 ? 109.86700 88.89900  66.41700  1.000 55.19117  ? 378 GLN A CD   1 
ATOM   2219 O OE1  . GLN A 1 378 ? 110.29700 88.35700  65.39900  1.000 57.70367  ? 378 GLN A OE1  1 
ATOM   2220 N NE2  . GLN A 1 378 ? 108.79700 88.45600  67.06500  1.000 56.85549  ? 378 GLN A NE2  1 
ATOM   2221 N N    . ARG A 1 379 ? 115.06300 91.10400  66.56700  1.000 39.52411  ? 379 ARG A N    1 
ATOM   2222 C CA   . ARG A 1 379 ? 116.49200 90.85400  66.71400  1.000 40.47988  ? 379 ARG A CA   1 
ATOM   2223 C C    . ARG A 1 379 ? 117.13900 91.88000  67.63700  1.000 44.25407  ? 379 ARG A C    1 
ATOM   2224 O O    . ARG A 1 379 ? 117.93600 91.52200  68.51700  1.000 50.28238  ? 379 ARG A O    1 
ATOM   2225 C CB   . ARG A 1 379 ? 117.17000 90.85900  65.34400  1.000 42.58665  ? 379 ARG A CB   1 
ATOM   2226 C CG   . ARG A 1 379 ? 117.77600 89.52200  64.94900  1.000 45.36758  ? 379 ARG A CG   1 
ATOM   2227 C CD   . ARG A 1 379 ? 118.98400 89.69700  64.04600  1.000 45.74395  ? 379 ARG A CD   1 
ATOM   2228 N NE   . ARG A 1 379 ? 120.23800 89.65300  64.78800  1.000 51.93453  ? 379 ARG A NE   1 
ATOM   2229 C CZ   . ARG A 1 379 ? 121.43300 89.86200  64.25300  1.000 51.50351  ? 379 ARG A CZ   1 
ATOM   2230 N NH1  . ARG A 1 379 ? 121.57700 90.12700  62.96500  1.000 47.25086  ? 379 ARG A NH1  1 
ATOM   2231 N NH2  . ARG A 1 379 ? 122.51100 89.80300  65.03000  1.000 45.38895  ? 379 ARG A NH2  1 
ATOM   2232 N N    . VAL A 1 380 ? 116.80700 93.16200  67.45800  1.000 41.40403  ? 380 VAL A N    1 
ATOM   2233 C CA   . VAL A 1 380 ? 117.42800 94.18400  68.29400  1.000 40.24589  ? 380 VAL A CA   1 
ATOM   2234 C C    . VAL A 1 380 ? 117.01100 94.02700  69.75200  1.000 38.50929  ? 380 VAL A C    1 
ATOM   2235 O O    . VAL A 1 380 ? 117.83600 94.20000  70.66400  1.000 44.16998  ? 380 VAL A O    1 
ATOM   2236 C CB   . VAL A 1 380 ? 117.08200 95.58600  67.76000  1.000 39.91963  ? 380 VAL A CB   1 
ATOM   2237 C CG1  . VAL A 1 380 ? 117.61100 96.66100  68.69500  1.000 40.83160  ? 380 VAL A CG1  1 
ATOM   2238 C CG2  . VAL A 1 380 ? 117.63600 95.77200  66.35900  1.000 41.01767  ? 380 VAL A CG2  1 
ATOM   2239 N N    . GLY A 1 381 ? 115.76500 93.61700  70.00100  1.000 32.61476  ? 381 GLY A N    1 
ATOM   2240 C CA   . GLY A 1 381 ? 115.34500 93.39800  71.37500  1.000 36.00156  ? 381 GLY A CA   1 
ATOM   2241 C C    . GLY A 1 381 ? 116.05000 92.21800  72.01600  1.000 39.69819  ? 381 GLY A C    1 
ATOM   2242 O O    . GLY A 1 381 ? 116.51000 92.30100  73.16300  1.000 39.30386  ? 381 GLY A O    1 
ATOM   2243 N N    . VAL A 1 382 ? 116.17500 91.11300  71.27600  1.000 37.05703  ? 382 VAL A N    1 
ATOM   2244 C CA   . VAL A 1 382 ? 116.86500 89.94200  71.80800  1.000 38.53780  ? 382 VAL A CA   1 
ATOM   2245 C C    . VAL A 1 382 ? 118.30800 90.29200  72.15200  1.000 38.67855  ? 382 VAL A C    1 
ATOM   2246 O O    . VAL A 1 382 ? 118.81300 89.94600  73.22900  1.000 42.59933  ? 382 VAL A O    1 
ATOM   2247 C CB   . VAL A 1 382 ? 116.79100 88.77600  70.80500  1.000 39.06831  ? 382 VAL A CB   1 
ATOM   2248 C CG1  . VAL A 1 382 ? 117.56800 87.57600  71.31900  1.000 40.27187  ? 382 VAL A CG1  1 
ATOM   2249 C CG2  . VAL A 1 382 ? 115.34500 88.40000  70.53300  1.000 37.97296  ? 382 VAL A CG2  1 
ATOM   2250 N N    . GLU A 1 383 ? 118.98700 91.00500  71.24800  1.000 36.42412  ? 383 GLU A N    1 
ATOM   2251 C CA   . GLU A 1 383 ? 120.39300 91.32100  71.47900  1.000 34.04739  ? 383 GLU A CA   1 
ATOM   2252 C C    . GLU A 1 383 ? 120.57100 92.24800  72.67700  1.000 34.55033  ? 383 GLU A C    1 
ATOM   2253 O O    . GLU A 1 383 ? 121.46500 92.03000  73.50900  1.000 34.50867  ? 383 GLU A O    1 
ATOM   2254 C CB   . GLU A 1 383 ? 121.00300 91.94100  70.22400  1.000 33.27971  ? 383 GLU A CB   1 
ATOM   2255 C CG   . GLU A 1 383 ? 120.85400 91.08900  68.97900  1.000 38.45420  ? 383 GLU A CG   1 
ATOM   2256 C CD   . GLU A 1 383 ? 121.61400 89.78300  69.07300  1.000 46.36870  ? 383 GLU A CD   1 
ATOM   2257 O OE1  . GLU A 1 383 ? 122.74500 89.78600  69.60200  1.000 47.50591  ? 383 GLU A OE1  1 
ATOM   2258 O OE2  . GLU A 1 383 ? 121.07900 88.75000  68.62000  1.000 49.00563  ? 383 GLU A OE2  1 
ATOM   2259 N N    . GLY A 1 384 ? 119.72000 93.27000  72.80600  1.000 23.65000  ? 384 GLY A N    1 
ATOM   2260 C CA   . GLY A 1 384 ? 119.87000 94.18000  73.93000  1.000 20.13679  ? 384 GLY A CA   1 
ATOM   2261 C C    . GLY A 1 384 ? 119.57600 93.51700  75.26200  1.000 31.28567  ? 384 GLY A C    1 
ATOM   2262 O O    . GLY A 1 384 ? 120.26600 93.76900  76.26000  1.000 32.44630  ? 384 GLY A O    1 
ATOM   2263 N N    . ALA A 1 385 ? 118.59600 92.60900  75.28800  1.000 31.94857  ? 385 ALA A N    1 
ATOM   2264 C CA   . ALA A 1 385 ? 118.29400 91.92600  76.54100  1.000 25.03044  ? 385 ALA A CA   1 
ATOM   2265 C C    . ALA A 1 385 ? 119.41300 90.96900  76.92500  1.000 34.59505  ? 385 ALA A C    1 
ATOM   2266 O O    . ALA A 1 385 ? 119.78700 90.87800  78.10500  1.000 37.70208  ? 385 ALA A O    1 
ATOM   2267 C CB   . ALA A 1 385 ? 116.96300 91.18600  76.43000  1.000 34.22493  ? 385 ALA A CB   1 
ATOM   2268 N N    . LYS A 1 386 ? 119.99100 90.27500  75.94000  1.000 33.15625  ? 386 LYS A N    1 
ATOM   2269 C CA   . LYS A 1 386 ? 121.10800 89.38700  76.24000  1.000 24.07877  ? 386 LYS A CA   1 
ATOM   2270 C C    . LYS A 1 386 ? 122.30000 90.16900  76.77600  1.000 27.14650  ? 386 LYS A C    1 
ATOM   2271 O O    . LYS A 1 386 ? 122.95600 89.73700  77.73300  1.000 35.34593  ? 386 LYS A O    1 
ATOM   2272 C CB   . LYS A 1 386 ? 121.49400 88.59400  74.99200  1.000 28.18956  ? 386 LYS A CB   1 
ATOM   2273 C CG   . LYS A 1 386 ? 122.69200 87.68400  75.17800  1.000 31.20193  ? 386 LYS A CG   1 
ATOM   2274 C CD   . LYS A 1 386 ? 122.70900 86.59400  74.12700  1.000 29.78729  ? 386 LYS A CD   1 
ATOM   2275 C CE   . LYS A 1 386 ? 121.83600 86.96500  72.94200  1.000 35.36223  ? 386 LYS A CE   1 
ATOM   2276 N NZ   . LYS A 1 386 ? 121.46600 85.77400  72.12700  1.000 37.80339  ? 386 LYS A NZ   1 
ATOM   2277 N N    . LEU A 1 387 ? 122.58200 91.33700  76.19200  1.000 28.84988  ? 387 LEU A N    1 
ATOM   2278 C CA   . LEU A 1 387 ? 123.71400 92.12800  76.67000  1.000 26.77630  ? 387 LEU A CA   1 
ATOM   2279 C C    . LEU A 1 387 ? 123.48800 92.61800  78.09700  1.000 28.77557  ? 387 LEU A C    1 
ATOM   2280 O O    . LEU A 1 387 ? 124.39900 92.55000  78.93800  1.000 27.90327  ? 387 LEU A O    1 
ATOM   2281 C CB   . LEU A 1 387 ? 123.96600 93.30600  75.73000  1.000 27.77564  ? 387 LEU A CB   1 
ATOM   2282 C CG   . LEU A 1 387 ? 124.95300 94.36400  76.23000  1.000 35.05819  ? 387 LEU A CG   1 
ATOM   2283 C CD1  . LEU A 1 387 ? 126.36300 93.80200  76.29900  1.000 34.40945  ? 387 LEU A CD1  1 
ATOM   2284 C CD2  . LEU A 1 387 ? 124.91000 95.59800  75.35200  1.000 32.16313  ? 387 LEU A CD2  1 
ATOM   2285 N N    . LEU A 1 388 ? 122.27900 93.10200  78.40000  1.000 27.09162  ? 388 LEU A N    1 
ATOM   2286 C CA   . LEU A 1 388 ? 122.02800 93.58700  79.75400  1.000 23.96286  ? 388 LEU A CA   1 
ATOM   2287 C C    . LEU A 1 388 ? 122.11300 92.45700  80.77500  1.000 33.42737  ? 388 LEU A C    1 
ATOM   2288 O O    . LEU A 1 388 ? 122.65500 92.64300  81.87300  1.000 27.66168  ? 388 LEU A O    1 
ATOM   2289 C CB   . LEU A 1 388 ? 120.66800 94.28200  79.82900  1.000 28.94812  ? 388 LEU A CB   1 
ATOM   2290 C CG   . LEU A 1 388 ? 120.55300 95.62800  79.11000  1.000 30.38034  ? 388 LEU A CG   1 
ATOM   2291 C CD1  . LEU A 1 388 ? 119.11000 96.09600  79.05000  1.000 21.82036  ? 388 LEU A CD1  1 
ATOM   2292 C CD2  . LEU A 1 388 ? 121.42400 96.66700  79.79300  1.000 26.32769  ? 388 LEU A CD2  1 
ATOM   2293 N N    . ARG A 1 389 ? 121.61500 91.26700  80.42500  1.000 38.84066  ? 389 ARG A N    1 
ATOM   2294 C CA   . ARG A 1 389 ? 121.67200 90.15900  81.37400  1.000 32.17403  ? 389 ARG A CA   1 
ATOM   2295 C C    . ARG A 1 389 ? 123.10300 89.67400  81.57700  1.000 30.85946  ? 389 ARG A C    1 
ATOM   2296 O O    . ARG A 1 389 ? 123.48700 89.29600  82.69300  1.000 34.76040  ? 389 ARG A O    1 
ATOM   2297 C CB   . ARG A 1 389 ? 120.76700 89.02300  80.90100  1.000 30.22328  ? 389 ARG A CB   1 
ATOM   2298 C CG   . ARG A 1 389 ? 119.32200 89.20300  81.32200  1.000 29.59072  ? 389 ARG A CG   1 
ATOM   2299 C CD   . ARG A 1 389 ? 118.41500 88.16300  80.69900  1.000 34.33748  ? 389 ARG A CD   1 
ATOM   2300 N NE   . ARG A 1 389 ? 117.01100 88.50400  80.89500  1.000 39.24240  ? 389 ARG A NE   1 
ATOM   2301 C CZ   . ARG A 1 389 ? 116.09700 88.49000  79.93500  1.000 34.62907  ? 389 ARG A CZ   1 
ATOM   2302 N NH1  . ARG A 1 389 ? 116.40100 88.14500  78.69600  1.000 33.29491  ? 389 ARG A NH1  1 
ATOM   2303 N NH2  . ARG A 1 389 ? 114.84600 88.83600  80.22700  1.000 31.89369  ? 389 ARG A NH2  1 
ATOM   2304 N N    . GLU A 1 390 ? 123.91800 89.70400  80.51900  1.000 32.36720  ? 390 GLU A N    1 
ATOM   2305 C CA   . GLU A 1 390 ? 125.32400 89.34800  80.67800  1.000 28.34524  ? 390 GLU A CA   1 
ATOM   2306 C C    . GLU A 1 390 ? 126.03700 90.32600  81.60500  1.000 27.96538  ? 390 GLU A C    1 
ATOM   2307 O O    . GLU A 1 390 ? 126.81300 89.91300  82.47600  1.000 32.68353  ? 390 GLU A O    1 
ATOM   2308 C CB   . GLU A 1 390 ? 126.01200 89.29900  79.31500  1.000 33.82121  ? 390 GLU A CB   1 
ATOM   2309 C CG   . GLU A 1 390 ? 127.52500 89.23300  79.38700  1.000 31.71499  ? 390 GLU A CG   1 
ATOM   2310 C CD   . GLU A 1 390 ? 128.03000 87.85200  79.75600  1.000 44.09682  ? 390 GLU A CD   1 
ATOM   2311 O OE1  . GLU A 1 390 ? 127.84200 87.43800  80.91900  1.000 45.31266  ? 390 GLU A OE1  1 
ATOM   2312 O OE2  . GLU A 1 390 ? 128.61800 87.18000  78.88300  1.000 45.72462  ? 390 GLU A OE2  1 
ATOM   2313 N N    . LEU A 1 391 ? 125.78700 91.62900  81.43900  1.000 34.16344  ? 391 LEU A N    1 
ATOM   2314 C CA   . LEU A 1 391 ? 126.41900 92.59200  82.33900  1.000 30.17663  ? 391 LEU A CA   1 
ATOM   2315 C C    . LEU A 1 391 ? 125.93100 92.43600  83.77600  1.000 33.25822  ? 391 LEU A C    1 
ATOM   2316 O O    . LEU A 1 391 ? 126.71700 92.60900  84.71700  1.000 29.31147  ? 391 LEU A O    1 
ATOM   2317 C CB   . LEU A 1 391 ? 126.17300 94.02100  81.85400  1.000 32.09297  ? 391 LEU A CB   1 
ATOM   2318 C CG   . LEU A 1 391 ? 127.12800 94.57100  80.79500  1.000 35.12702  ? 391 LEU A CG   1 
ATOM   2319 C CD1  . LEU A 1 391 ? 126.94300 96.06800  80.64800  1.000 34.53922  ? 391 LEU A CD1  1 
ATOM   2320 C CD2  . LEU A 1 391 ? 128.56700 94.24400  81.15100  1.000 32.27694  ? 391 LEU A CD2  1 
ATOM   2321 N N    . GLY A 1 392 ? 124.66200 92.07300  83.97100  1.000 33.64944  ? 392 GLY A N    1 
ATOM   2322 C CA   . GLY A 1 392 ? 124.18300 91.84100  85.32600  1.000 29.92025  ? 392 GLY A CA   1 
ATOM   2323 C C    . GLY A 1 392 ? 124.84000 90.64000  85.98000  1.000 36.75899  ? 392 GLY A C    1 
ATOM   2324 O O    . GLY A 1 392 ? 125.21300 90.68500  87.16000  1.000 35.10128  ? 392 GLY A O    1 
ATOM   2325 N N    . GLU A 1 393 ? 125.02600 89.56000  85.21600  1.000 40.89449  ? 393 GLU A N    1 
ATOM   2326 C CA   . GLU A 1 393 ? 125.68900 88.38500  85.77200  1.000 33.16270  ? 393 GLU A CA   1 
ATOM   2327 C C    . GLU A 1 393 ? 127.16700 88.64500  86.02400  1.000 37.97686  ? 393 GLU A C    1 
ATOM   2328 O O    . GLU A 1 393 ? 127.74300 88.07900  86.95900  1.000 33.61430  ? 393 GLU A O    1 
ATOM   2329 C CB   . GLU A 1 393 ? 125.51400 87.18600  84.84100  1.000 37.60337  ? 393 GLU A CB   1 
ATOM   2330 C CG   . GLU A 1 393 ? 124.24600 86.38400  85.08400  1.000 41.03656  ? 393 GLU A CG   1 
ATOM   2331 C CD   . GLU A 1 393 ? 124.11900 85.90200  86.51700  1.000 48.27066  ? 393 GLU A CD   1 
ATOM   2332 O OE1  . GLU A 1 393 ? 123.05400 85.35300  86.86700  1.000 49.99228  ? 393 GLU A OE1  1 
ATOM   2333 O OE2  . GLU A 1 393 ? 125.08500 86.06400  87.29200  1.000 49.91933  ? 393 GLU A OE2  1 
ATOM   2334 N N    . LYS A 1 394 ? 127.79700 89.49700  85.21200  1.000 43.82020  ? 394 LYS A N    1 
ATOM   2335 C CA   . LYS A 1 394 ? 129.19200 89.84300  85.46600  1.000 40.44316  ? 394 LYS A CA   1 
ATOM   2336 C C    . LYS A 1 394 ? 129.33400 90.73100  86.69500  1.000 32.70252  ? 394 LYS A C    1 
ATOM   2337 O O    . LYS A 1 394 ? 130.32200 90.61800  87.42800  1.000 28.53989  ? 394 LYS A O    1 
ATOM   2338 C CB   . LYS A 1 394 ? 129.79700 90.53600  84.24600  1.000 36.36590  ? 394 LYS A CB   1 
ATOM   2339 C CG   . LYS A 1 394 ? 131.20300 90.08700  83.91000  1.000 33.71213  ? 394 LYS A CG   1 
ATOM   2340 C CD   . LYS A 1 394 ? 131.20100 88.88000  82.99300  1.000 38.73703  ? 394 LYS A CD   1 
ATOM   2341 C CE   . LYS A 1 394 ? 132.46200 88.84000  82.14900  1.000 40.34715  ? 394 LYS A CE   1 
ATOM   2342 N NZ   . LYS A 1 394 ? 132.90700 87.44800  81.87400  1.000 43.01161  ? 394 LYS A NZ   1 
ATOM   2343 N N    . VAL A 1 395 ? 128.36000 91.60700  86.94500  1.000 32.85799  ? 395 VAL A N    1 
ATOM   2344 C CA   . VAL A 1 395 ? 128.41000 92.42500  88.15200  1.000 29.85894  ? 395 VAL A CA   1 
ATOM   2345 C C    . VAL A 1 395 ? 128.20000 91.56600  89.39200  1.000 34.80936  ? 395 VAL A C    1 
ATOM   2346 O O    . VAL A 1 395 ? 128.89000 91.73600  90.40300  1.000 33.36842  ? 395 VAL A O    1 
ATOM   2347 C CB   . VAL A 1 395 ? 127.38000 93.56500  88.08000  1.000 32.94628  ? 395 VAL A CB   1 
ATOM   2348 C CG1  . VAL A 1 395 ? 127.05200 94.06400  89.47700  1.000 27.61248  ? 395 VAL A CG1  1 
ATOM   2349 C CG2  . VAL A 1 395 ? 127.90600 94.70100  87.22400  1.000 34.40586  ? 395 VAL A CG2  1 
ATOM   2350 N N    . LYS A 1 396 ? 127.24900 90.62800  89.33900  1.000 44.51536  ? 396 LYS A N    1 
ATOM   2351 C CA   . LYS A 1 396 ? 126.93400 89.85200  90.53600  1.000 33.26404  ? 396 LYS A CA   1 
ATOM   2352 C C    . LYS A 1 396 ? 128.10800 88.98300  90.98100  1.000 38.77795  ? 396 LYS A C    1 
ATOM   2353 O O    . LYS A 1 396 ? 128.38200 88.87000  92.18100  1.000 38.67861  ? 396 LYS A O    1 
ATOM   2354 C CB   . LYS A 1 396 ? 125.69700 88.98800  90.29900  1.000 36.56318  ? 396 LYS A CB   1 
ATOM   2355 C CG   . LYS A 1 396 ? 125.36200 88.08400  91.47300  1.000 35.76033  ? 396 LYS A CG   1 
ATOM   2356 C CD   . LYS A 1 396 ? 124.74500 86.77800  91.01900  1.000 38.71344  ? 396 LYS A CD   1 
ATOM   2357 C CE   . LYS A 1 396 ? 123.24900 86.91800  90.81700  1.000 43.47951  ? 396 LYS A CE   1 
ATOM   2358 N NZ   . LYS A 1 396 ? 122.53100 85.65300  91.13100  1.000 48.94490  ? 396 LYS A NZ   1 
ATOM   2359 N N    . LYS A 1 397 ? 128.81200 88.35900  90.03600  1.000 46.59883  ? 397 LYS A N    1 
ATOM   2360 C CA   . LYS A 1 397 ? 129.91500 87.46600  90.37700  1.000 41.38895  ? 397 LYS A CA   1 
ATOM   2361 C C    . LYS A 1 397 ? 131.23900 88.18100  90.61500  1.000 41.31060  ? 397 LYS A C    1 
ATOM   2362 O O    . LYS A 1 397 ? 132.22400 87.51500  90.94800  1.000 44.77656  ? 397 LYS A O    1 
ATOM   2363 C CB   . LYS A 1 397 ? 130.10100 86.41100  89.28300  1.000 41.45893  ? 397 LYS A CB   1 
ATOM   2364 C CG   . LYS A 1 397 ? 128.96400 85.40900  89.18600  1.000 45.89236  ? 397 LYS A CG   1 
ATOM   2365 C CD   . LYS A 1 397 ? 129.31700 84.27600  88.24000  1.000 44.26225  ? 397 LYS A CD   1 
ATOM   2366 C CE   . LYS A 1 397 ? 130.29000 84.73700  87.16700  1.000 45.04770  ? 397 LYS A CE   1 
ATOM   2367 N NZ   . LYS A 1 397 ? 129.58900 85.34100  86.00000  1.000 45.19941  ? 397 LYS A NZ   1 
ATOM   2368 N N    . MET A 1 398 ? 131.29400 89.50100  90.46800  1.000 45.19452  ? 398 MET A N    1 
ATOM   2369 C CA   . MET A 1 398 ? 132.52800 90.26500  90.64800  1.000 40.04390  ? 398 MET A CA   1 
ATOM   2370 C C    . MET A 1 398 ? 133.64600 89.72800  89.75200  1.000 40.91715  ? 398 MET A C    1 
ATOM   2371 O O    . MET A 1 398 ? 134.67400 89.23200  90.21500  1.000 42.73893  ? 398 MET A O    1 
ATOM   2372 C CB   . MET A 1 398 ? 132.95100 90.25600  92.11800  1.000 35.73705  ? 398 MET A CB   1 
ATOM   2373 C CG   . MET A 1 398 ? 132.27700 91.32000  92.96500  1.000 43.69973  ? 398 MET A CG   1 
ATOM   2374 S SD   . MET A 1 398 ? 132.08700 90.81800  94.68600  1.000 55.38410  ? 398 MET A SD   1 
ATOM   2375 C CE   . MET A 1 398 ? 133.26500 91.89800  95.48800  1.000 39.28286  ? 398 MET A CE   1 
ATOM   2376 N N    . GLU A 1 399 ? 133.42700 89.84400  88.44400  1.000 47.15740  ? 399 GLU A N    1 
ATOM   2377 C CA   . GLU A 1 399 ? 134.34800 89.32400  87.44400  1.000 43.66449  ? 399 GLU A CA   1 
ATOM   2378 C C    . GLU A 1 399 ? 134.59500 90.37000  86.36500  1.000 47.21925  ? 399 GLU A C    1 
ATOM   2379 O O    . GLU A 1 399 ? 133.76200 91.24800  86.12600  1.000 49.27095  ? 399 GLU A O    1 
ATOM   2380 C CB   . GLU A 1 399 ? 133.80500 88.03600  86.81500  1.000 43.79798  ? 399 GLU A CB   1 
ATOM   2381 C CG   . GLU A 1 399 ? 134.86900 87.12300  86.23800  1.000 52.74550  ? 399 GLU A CG   1 
ATOM   2382 C CD   . GLU A 1 399 ? 134.29700 85.81300  85.73200  1.000 56.03243  ? 399 GLU A CD   1 
ATOM   2383 O OE1  . GLU A 1 399 ? 133.56600 85.83200  84.72100  1.000 54.34338  ? 399 GLU A OE1  1 
ATOM   2384 O OE2  . GLU A 1 399 ? 134.57500 84.76400  86.34900  1.000 55.94104  ? 399 GLU A OE2  1 
ATOM   2385 N N    . LYS A 1 400 ? 135.75100 90.26800  85.71600  1.000 45.94004  ? 400 LYS A N    1 
ATOM   2386 C CA   . LYS A 1 400 ? 136.13700 91.18900  84.65800  1.000 45.44269  ? 400 LYS A CA   1 
ATOM   2387 C C    . LYS A 1 400 ? 135.57000 90.75000  83.31000  1.000 45.67878  ? 400 LYS A C    1 
ATOM   2388 O O    . LYS A 1 400 ? 135.15200 89.60600  83.12300  1.000 49.35561  ? 400 LYS A O    1 
ATOM   2389 C CB   . LYS A 1 400 ? 137.65900 91.29600  84.56100  1.000 44.04077  ? 400 LYS A CB   1 
ATOM   2390 C CG   . LYS A 1 400 ? 138.30900 92.06700  85.68900  1.000 44.21219  ? 400 LYS A CG   1 
ATOM   2391 C CD   . LYS A 1 400 ? 139.76300 92.36700  85.37000  1.000 47.88113  ? 400 LYS A CD   1 
ATOM   2392 C CE   . LYS A 1 400 ? 140.18200 93.71700  85.92100  1.000 47.97044  ? 400 LYS A CE   1 
ATOM   2393 N NZ   . LYS A 1 400 ? 140.60900 93.62500  87.34200  1.000 48.45728  ? 400 LYS A NZ   1 
ATOM   2394 N N    . LEU A 1 401 ? 135.56400 91.68800  82.36600  1.000 43.85358  ? 401 LEU A N    1 
ATOM   2395 C CA   . LEU A 1 401 ? 135.14400 91.40000  81.00200  1.000 47.64477  ? 401 LEU A CA   1 
ATOM   2396 C C    . LEU A 1 401 ? 136.23400 90.64800  80.24900  1.000 47.80651  ? 401 LEU A C    1 
ATOM   2397 O O    . LEU A 1 401 ? 137.42900 90.82000  80.50400  1.000 48.78434  ? 401 LEU A O    1 
ATOM   2398 C CB   . LEU A 1 401 ? 134.79700 92.68800  80.25600  1.000 47.66139  ? 401 LEU A CB   1 
ATOM   2399 C CG   . LEU A 1 401 ? 133.54100 93.43700  80.70400  1.000 47.89889  ? 401 LEU A CG   1 
ATOM   2400 C CD1  . LEU A 1 401 ? 133.35500 94.70500  79.88700  1.000 43.27728  ? 401 LEU A CD1  1 
ATOM   2401 C CD2  . LEU A 1 401 ? 132.32000 92.54200  80.59700  1.000 48.38750  ? 401 LEU A CD2  1 
ATOM   2402 N N    . GLY A 1 402 ? 135.80800 89.80800  79.31000  1.000 57.10976  ? 402 GLY A N    1 
ATOM   2403 C CA   . GLY A 1 402 ? 136.72400 89.00500  78.53700  1.000 58.24491  ? 402 GLY A CA   1 
ATOM   2404 C C    . GLY A 1 402 ? 137.31000 89.75500  77.35700  1.000 60.19063  ? 402 GLY A C    1 
ATOM   2405 O O    . GLY A 1 402 ? 137.15200 90.97200  77.22000  1.000 60.39027  ? 402 GLY A O    1 
ATOM   2406 N N    . PRO A 1 403 ? 138.00800 89.03300  76.48000  1.000 66.78357  ? 403 PRO A N    1 
ATOM   2407 C CA   . PRO A 1 403 ? 138.66800 89.68500  75.34000  1.000 66.99412  ? 403 PRO A CA   1 
ATOM   2408 C C    . PRO A 1 403 ? 137.70700 90.09600  74.23400  1.000 66.60884  ? 403 PRO A C    1 
ATOM   2409 O O    . PRO A 1 403 ? 137.86900 91.16000  73.62800  1.000 65.91966  ? 403 PRO A O    1 
ATOM   2410 C CB   . PRO A 1 403 ? 139.65200 88.61500  74.85400  1.000 65.51903  ? 403 PRO A CB   1 
ATOM   2411 C CG   . PRO A 1 403 ? 139.00600 87.32700  75.23500  1.000 64.73635  ? 403 PRO A CG   1 
ATOM   2412 C CD   . PRO A 1 403 ? 138.28100 87.58600  76.52800  1.000 65.47789  ? 403 PRO A CD   1 
ATOM   2413 N N    . VAL A 1 404 ? 136.70500 89.25900  73.96100  1.000 64.87640  ? 404 VAL A N    1 
ATOM   2414 C CA   . VAL A 1 404 ? 135.80900 89.50500  72.83800  1.000 65.37008  ? 404 VAL A CA   1 
ATOM   2415 C C    . VAL A 1 404 ? 134.95300 90.74000  73.09900  1.000 66.83776  ? 404 VAL A C    1 
ATOM   2416 O O    . VAL A 1 404 ? 134.62400 91.07200  74.24600  1.000 68.02202  ? 404 VAL A O    1 
ATOM   2417 C CB   . VAL A 1 404 ? 134.93000 88.27000  72.57000  1.000 65.77790  ? 404 VAL A CB   1 
ATOM   2418 C CG1  . VAL A 1 404 ? 133.92700 88.08000  73.69600  1.000 65.63968  ? 404 VAL A CG1  1 
ATOM   2419 C CG2  . VAL A 1 404 ? 134.22100 88.40500  71.23200  1.000 64.24323  ? 404 VAL A CG2  1 
ATOM   2420 N N    . ASP A 1 405 ? 134.58900 91.42800  72.01800  1.000 61.97389  ? 405 ASP A N    1 
ATOM   2421 C CA   . ASP A 1 405 ? 133.71900 92.59300  72.11400  1.000 60.95785  ? 405 ASP A CA   1 
ATOM   2422 C C    . ASP A 1 405 ? 132.28000 92.16900  72.38500  1.000 60.67831  ? 405 ASP A C    1 
ATOM   2423 O O    . ASP A 1 405 ? 131.76800 91.22400  71.77900  1.000 60.79036  ? 405 ASP A O    1 
ATOM   2424 C CB   . ASP A 1 405 ? 133.79400 93.41600  70.82900  1.000 59.84170  ? 405 ASP A CB   1 
ATOM   2425 C CG   . ASP A 1 405 ? 133.20300 94.80200  70.99100  1.000 61.89259  ? 405 ASP A CG   1 
ATOM   2426 O OD1  . ASP A 1 405 ? 132.96800 95.21900  72.14400  1.000 64.83097  ? 405 ASP A OD1  1 
ATOM   2427 O OD2  . ASP A 1 405 ? 132.97800 95.47800  69.96500  1.000 61.38673  ? 405 ASP A OD2  1 
ATOM   2428 N N    . LEU A 1 406 ? 131.62700 92.87800  73.30400  1.000 51.07521  ? 406 LEU A N    1 
ATOM   2429 C CA   . LEU A 1 406 ? 130.27100 92.55300  73.72500  1.000 50.72187  ? 406 LEU A CA   1 
ATOM   2430 C C    . LEU A 1 406 ? 129.18700 93.30300  72.95700  1.000 51.48904  ? 406 LEU A C    1 
ATOM   2431 O O    . LEU A 1 406 ? 128.00400 93.01100  73.15600  1.000 52.79427  ? 406 LEU A O    1 
ATOM   2432 C CB   . LEU A 1 406 ? 130.10800 92.83900  75.22200  1.000 52.58238  ? 406 LEU A CB   1 
ATOM   2433 C CG   . LEU A 1 406 ? 130.57600 91.76000  76.19800  1.000 54.41072  ? 406 LEU A CG   1 
ATOM   2434 C CD1  . LEU A 1 406 ? 129.81700 91.86400  77.50900  1.000 51.73312  ? 406 LEU A CD1  1 
ATOM   2435 C CD2  . LEU A 1 406 ? 130.41500 90.37600  75.59100  1.000 54.57504  ? 406 LEU A CD2  1 
ATOM   2436 N N    . LEU A 1 407 ? 129.54600 94.25100  72.09100  1.000 47.47711  ? 407 LEU A N    1 
ATOM   2437 C CA   . LEU A 1 407 ? 128.56800 95.08900  71.40600  1.000 44.96060  ? 407 LEU A CA   1 
ATOM   2438 C C    . LEU A 1 407 ? 128.49400 94.82700  69.90500  1.000 45.08116  ? 407 LEU A C    1 
ATOM   2439 O O    . LEU A 1 407 ? 127.86700 95.60500  69.18200  1.000 49.37321  ? 407 LEU A O    1 
ATOM   2440 C CB   . LEU A 1 407 ? 128.87900 96.56500  71.66300  1.000 42.38323  ? 407 LEU A CB   1 
ATOM   2441 C CG   . LEU A 1 407 ? 128.62100 97.09400  73.07800  1.000 42.77199  ? 407 LEU A CG   1 
ATOM   2442 C CD1  . LEU A 1 407 ? 129.01800 98.55600  73.19000  1.000 40.54315  ? 407 LEU A CD1  1 
ATOM   2443 C CD2  . LEU A 1 407 ? 127.16900 96.90700  73.47500  1.000 42.27466  ? 407 LEU A CD2  1 
ATOM   2444 N N    . PHE A 1 408 ? 129.11400 93.74900  69.42200  1.000 41.44952  ? 408 PHE A N    1 
ATOM   2445 C CA   . PHE A 1 408 ? 129.19600 93.50800  67.98300  1.000 40.86499  ? 408 PHE A CA   1 
ATOM   2446 C C    . PHE A 1 408 ? 127.84500 93.12100  67.37800  1.000 44.78987  ? 408 PHE A C    1 
ATOM   2447 O O    . PHE A 1 408 ? 127.45100 93.65300  66.32900  1.000 47.39125  ? 408 PHE A O    1 
ATOM   2448 C CB   . PHE A 1 408 ? 130.24700 92.42600  67.72100  1.000 47.54988  ? 408 PHE A CB   1 
ATOM   2449 C CG   . PHE A 1 408 ? 130.27200 91.91600  66.30900  1.000 47.56389  ? 408 PHE A CG   1 
ATOM   2450 C CD1  . PHE A 1 408 ? 131.03800 92.54700  65.34500  1.000 45.87634  ? 408 PHE A CD1  1 
ATOM   2451 C CD2  . PHE A 1 408 ? 129.55300 90.78900  65.95200  1.000 45.68032  ? 408 PHE A CD2  1 
ATOM   2452 C CE1  . PHE A 1 408 ? 131.06800 92.07700  64.04900  1.000 44.89492  ? 408 PHE A CE1  1 
ATOM   2453 C CE2  . PHE A 1 408 ? 129.57900 90.31500  64.65800  1.000 47.42627  ? 408 PHE A CE2  1 
ATOM   2454 C CZ   . PHE A 1 408 ? 130.33900 90.96000  63.70500  1.000 49.11039  ? 408 PHE A CZ   1 
ATOM   2455 N N    . GLU A 1 409 ? 127.10500 92.22700  68.03700  1.000 47.73861  ? 409 GLU A N    1 
ATOM   2456 C CA   . GLU A 1 409 ? 125.85600 91.74000  67.45700  1.000 45.56460  ? 409 GLU A CA   1 
ATOM   2457 C C    . GLU A 1 409 ? 124.74100 92.78000  67.51300  1.000 46.32749  ? 409 GLU A C    1 
ATOM   2458 O O    . GLU A 1 409 ? 123.95300 92.89700  66.56600  1.000 53.77636  ? 409 GLU A O    1 
ATOM   2459 C CB   . GLU A 1 409 ? 125.42500 90.45600  68.16300  1.000 45.81894  ? 409 GLU A CB   1 
ATOM   2460 C CG   . GLU A 1 409 ? 126.25400 89.24000  67.78800  1.000 47.03452  ? 409 GLU A CG   1 
ATOM   2461 C CD   . GLU A 1 409 ? 126.06700 88.82500  66.34100  1.000 53.86829  ? 409 GLU A CD   1 
ATOM   2462 O OE1  . GLU A 1 409 ? 126.70100 89.44000  65.45700  1.000 52.83705  ? 409 GLU A OE1  1 
ATOM   2463 O OE2  . GLU A 1 409 ? 125.28800 87.88300  66.08600  1.000 54.96905  ? 409 GLU A OE2  1 
ATOM   2464 N N    . VAL A 1 410 ? 124.66400 93.56300  68.59000  1.000 36.31455  ? 410 VAL A N    1 
ATOM   2465 C CA   . VAL A 1 410 ? 123.64800 94.61200  68.62600  1.000 39.55661  ? 410 VAL A CA   1 
ATOM   2466 C C    . VAL A 1 410 ? 124.00200 95.72300  67.64600  1.000 36.13395  ? 410 VAL A C    1 
ATOM   2467 O O    . VAL A 1 410 ? 123.11300 96.32900  67.02500  1.000 43.91331  ? 410 VAL A O    1 
ATOM   2468 C CB   . VAL A 1 410 ? 123.47300 95.13800  70.06500  1.000 35.31331  ? 410 VAL A CB   1 
ATOM   2469 C CG1  . VAL A 1 410 ? 124.52300 96.18600  70.38800  1.000 38.42981  ? 410 VAL A CG1  1 
ATOM   2470 C CG2  . VAL A 1 410 ? 122.07200 95.68900  70.26700  1.000 34.26130  ? 410 VAL A CG2  1 
ATOM   2471 N N    . HIS A 1 411 ? 125.29900 95.93800  67.41100  1.000 28.47133  ? 411 HIS A N    1 
ATOM   2472 C CA   . HIS A 1 411 ? 125.71200 96.95300  66.45300  1.000 35.25889  ? 411 HIS A CA   1 
ATOM   2473 C C    . HIS A 1 411 ? 125.44100 96.49600  65.02900  1.000 39.07861  ? 411 HIS A C    1 
ATOM   2474 O O    . HIS A 1 411 ? 125.26800 97.33000  64.13400  1.000 41.31053  ? 411 HIS A O    1 
ATOM   2475 C CB   . HIS A 1 411 ? 127.19400 97.28100  66.63800  1.000 35.23850  ? 411 HIS A CB   1 
ATOM   2476 C CG   . HIS A 1 411 ? 127.46700 98.23900  67.75500  1.000 39.21716  ? 411 HIS A CG   1 
ATOM   2477 N ND1  . HIS A 1 411 ? 128.73100 98.70500  68.04300  1.000 38.23721  ? 411 HIS A ND1  1 
ATOM   2478 C CD2  . HIS A 1 411 ? 126.64000 98.81400  68.66000  1.000 40.61884  ? 411 HIS A CD2  1 
ATOM   2479 C CE1  . HIS A 1 411 ? 128.67100 99.52800  69.07400  1.000 39.35143  ? 411 HIS A CE1  1 
ATOM   2480 N NE2  . HIS A 1 411 ? 127.41400 99.61100  69.46800  1.000 36.03188  ? 411 HIS A NE2  1 
ATOM   2481 N N    . LEU A 1 412 ? 125.39000 95.18300  64.80200  1.000 37.89566  ? 412 LEU A N    1 
ATOM   2482 C CA   . LEU A 1 412 ? 125.05400 94.68900  63.47100  1.000 41.07390  ? 412 LEU A CA   1 
ATOM   2483 C C    . LEU A 1 412 ? 123.54300 94.68400  63.25900  1.000 45.54862  ? 412 LEU A C    1 
ATOM   2484 O O    . LEU A 1 412 ? 123.05700 94.99900  62.16200  1.000 46.04176  ? 412 LEU A O    1 
ATOM   2485 C CB   . LEU A 1 412 ? 125.62900 93.28600  63.27700  1.000 47.62998  ? 412 LEU A CB   1 
ATOM   2486 C CG   . LEU A 1 412 ? 126.08800 92.90600  61.87000  1.000 49.22393  ? 412 LEU A CG   1 
ATOM   2487 C CD1  . LEU A 1 412 ? 127.47200 93.46600  61.59000  1.000 48.26545  ? 412 LEU A CD1  1 
ATOM   2488 C CD2  . LEU A 1 412 ? 126.07200 91.39700  61.70200  1.000 41.96113  ? 412 LEU A CD2  1 
ATOM   2489 N N    . ALA A 1 413 ? 122.78900 94.34600  64.30800  1.000 43.62250  ? 413 ALA A N    1 
ATOM   2490 C CA   . ALA A 1 413 ? 121.33300 94.38900  64.22500  1.000 42.12749  ? 413 ALA A CA   1 
ATOM   2491 C C    . ALA A 1 413 ? 120.83400 95.80000  63.93700  1.000 48.16612  ? 413 ALA A C    1 
ATOM   2492 O O    . ALA A 1 413 ? 119.89600 95.98700  63.14900  1.000 49.74933  ? 413 ALA A O    1 
ATOM   2493 C CB   . ALA A 1 413 ? 120.72000 93.85300  65.51800  1.000 39.36986  ? 413 ALA A CB   1 
ATOM   2494 N N    . ALA A 1 414 ? 121.44100 96.81100  64.56900  1.000 43.76669  ? 414 ALA A N    1 
ATOM   2495 C CA   . ALA A 1 414 ? 120.98400 98.17600  64.32400  1.000 42.67210  ? 414 ALA A CA   1 
ATOM   2496 C C    . ALA A 1 414 ? 121.23600 98.59900  62.87900  1.000 40.07175  ? 414 ALA A C    1 
ATOM   2497 O O    . ALA A 1 414 ? 120.40100 99.28200  62.27100  1.000 44.57445  ? 414 ALA A O    1 
ATOM   2498 C CB   . ALA A 1 414 ? 121.66400 99.13900  65.29600  1.000 39.15789  ? 414 ALA A CB   1 
ATOM   2499 N N    . GLU A 1 415 ? 122.36300 98.17900  62.30000  1.000 45.51477  ? 415 GLU A N    1 
ATOM   2500 C CA   . GLU A 1 415 ? 122.62600 98.49200  60.89900  1.000 47.03194  ? 415 GLU A CA   1 
ATOM   2501 C C    . GLU A 1 415 ? 121.65000 97.77200  59.97600  1.000 47.90399  ? 415 GLU A C    1 
ATOM   2502 O O    . GLU A 1 415 ? 121.21600 98.33500  58.96100  1.000 50.13438  ? 415 GLU A O    1 
ATOM   2503 C CB   . GLU A 1 415 ? 124.06800 98.13800  60.53500  1.000 47.51768  ? 415 GLU A CB   1 
ATOM   2504 C CG   . GLU A 1 415 ? 125.11500 98.68500  61.49000  1.000 48.50910  ? 415 GLU A CG   1 
ATOM   2505 C CD   . GLU A 1 415 ? 126.42300 97.91800  61.42100  1.000 56.07044  ? 415 GLU A CD   1 
ATOM   2506 O OE1  . GLU A 1 415 ? 126.75100 97.40000  60.33200  1.000 58.30019  ? 415 GLU A OE1  1 
ATOM   2507 O OE2  . GLU A 1 415 ? 127.12900 97.83900  62.44800  1.000 55.99211  ? 415 GLU A OE2  1 
ATOM   2508 N N    . GLU A 1 416 ? 121.27900 96.53400  60.31400  1.000 45.23442  ? 416 GLU A N    1 
ATOM   2509 C CA   . GLU A 1 416 ? 120.29200 95.83900  59.49100  1.000 45.64131  ? 416 GLU A CA   1 
ATOM   2510 C C    . GLU A 1 416 ? 118.94600 96.55200  59.53900  1.000 50.24358  ? 416 GLU A C    1 
ATOM   2511 O O    . GLU A 1 416 ? 118.27500 96.70600  58.50800  1.000 48.48408  ? 416 GLU A O    1 
ATOM   2512 C CB   . GLU A 1 416 ? 120.14100 94.38800  59.94500  1.000 46.56052  ? 416 GLU A CB   1 
ATOM   2513 C CG   . GLU A 1 416 ? 121.44500 93.62700  60.07800  1.000 53.75918  ? 416 GLU A CG   1 
ATOM   2514 C CD   . GLU A 1 416 ? 121.30900 92.40500  60.96300  1.000 56.37047  ? 416 GLU A CD   1 
ATOM   2515 O OE1  . GLU A 1 416 ? 120.18000 91.88600  61.08600  1.000 53.94712  ? 416 GLU A OE1  1 
ATOM   2516 O OE2  . GLU A 1 416 ? 122.32600 91.96300  61.53700  1.000 55.07185  ? 416 GLU A OE2  1 
ATOM   2517 N N    . LEU A 1 417 ? 118.54200 97.00800  60.72700  1.000 50.74069  ? 417 LEU A N    1 
ATOM   2518 C CA   . LEU A 1 417 ? 117.29400 97.75600  60.84000  1.000 41.99230  ? 417 LEU A CA   1 
ATOM   2519 C C    . LEU A 1 417 ? 117.34800 99.04500  60.02900  1.000 43.08870  ? 417 LEU A C    1 
ATOM   2520 O O    . LEU A 1 417 ? 116.37400 99.40800  59.35600  1.000 41.46236  ? 417 LEU A O    1 
ATOM   2521 C CB   . LEU A 1 417 ? 116.98700 98.05800  62.30700  1.000 41.46574  ? 417 LEU A CB   1 
ATOM   2522 C CG   . LEU A 1 417 ? 115.67800 98.80400  62.57700  1.000 41.95866  ? 417 LEU A CG   1 
ATOM   2523 C CD1  . LEU A 1 417 ? 114.48600 98.01400  62.06200  1.000 45.49706  ? 417 LEU A CD1  1 
ATOM   2524 C CD2  . LEU A 1 417 ? 115.52100 99.10400  64.05700  1.000 38.01226  ? 417 LEU A CD2  1 
ATOM   2525 N N    . GLN A 1 418 ? 118.47500 99.75800  60.08700  1.000 46.92073  ? 418 GLN A N    1 
ATOM   2526 C CA   . GLN A 1 418 ? 118.60900 100.98600 59.30900  1.000 48.36429  ? 418 GLN A CA   1 
ATOM   2527 C C    . GLN A 1 418 ? 118.48200 100.71000 57.81500  1.000 50.11946  ? 418 GLN A C    1 
ATOM   2528 O O    . GLN A 1 418 ? 117.78500 101.43500 57.09400  1.000 45.88024  ? 418 GLN A O    1 
ATOM   2529 C CB   . GLN A 1 418 ? 119.94100 101.66600 59.62000  1.000 46.50964  ? 418 GLN A CB   1 
ATOM   2530 C CG   . GLN A 1 418 ? 119.98400 103.13100 59.22500  1.000 47.23211  ? 418 GLN A CG   1 
ATOM   2531 C CD   . GLN A 1 418 ? 118.79100 103.90600 59.74500  1.000 52.50188  ? 418 GLN A CD   1 
ATOM   2532 O OE1  . GLN A 1 418 ? 118.12400 104.61900 58.99500  1.000 53.40579  ? 418 GLN A OE1  1 
ATOM   2533 N NE2  . GLN A 1 418 ? 118.51200 103.76600 61.03500  1.000 51.31261  ? 418 GLN A NE2  1 
ATOM   2534 N N    . HIS A 1 419 ? 119.15800 99.66700  57.32600  1.000 54.26736  ? 419 HIS A N    1 
ATOM   2535 C CA   . HIS A 1 419 ? 119.06900 99.34500  55.90400  1.000 52.98149  ? 419 HIS A CA   1 
ATOM   2536 C C    . HIS A 1 419 ? 117.63800 99.00200  55.50900  1.000 57.10164  ? 419 HIS A C    1 
ATOM   2537 O O    . HIS A 1 419 ? 117.14500 99.44600  54.46000  1.000 55.93867  ? 419 HIS A O    1 
ATOM   2538 C CB   . HIS A 1 419 ? 120.00800 98.18700  55.56600  1.000 55.78487  ? 419 HIS A CB   1 
ATOM   2539 C CG   . HIS A 1 419 ? 121.44700 98.58500  55.46100  1.000 60.52618  ? 419 HIS A CG   1 
ATOM   2540 N ND1  . HIS A 1 419 ? 122.47300 97.79200  55.92600  1.000 60.02729  ? 419 HIS A ND1  1 
ATOM   2541 C CD2  . HIS A 1 419 ? 122.03100 99.68900  54.93800  1.000 60.17642  ? 419 HIS A CD2  1 
ATOM   2542 C CE1  . HIS A 1 419 ? 123.62800 98.39200  55.69800  1.000 59.69631  ? 419 HIS A CE1  1 
ATOM   2543 N NE2  . HIS A 1 419 ? 123.38800 99.54400  55.10000  1.000 60.50108  ? 419 HIS A NE2  1 
ATOM   2544 N N    . LYS A 1 420 ? 116.94300 98.23200  56.34900  1.000 56.16043  ? 420 LYS A N    1 
ATOM   2545 C CA   . LYS A 1 420 ? 115.56400 97.87600  56.03600  1.000 54.04440  ? 420 LYS A CA   1 
ATOM   2546 C C    . LYS A 1 420 ? 114.68300 99.11800  55.97000  1.000 55.16831  ? 420 LYS A C    1 
ATOM   2547 O O    . LYS A 1 420 ? 113.87600 99.27200  55.04600  1.000 54.54260  ? 420 LYS A O    1 
ATOM   2548 C CB   . LYS A 1 420 ? 115.02700 96.88300  57.06400  1.000 54.19940  ? 420 LYS A CB   1 
ATOM   2549 C CG   . LYS A 1 420 ? 113.54100 96.61400  56.93200  1.000 56.66128  ? 420 LYS A CG   1 
ATOM   2550 C CD   . LYS A 1 420 ? 113.25700 95.73900  55.72300  1.000 54.47873  ? 420 LYS A CD   1 
ATOM   2551 C CE   . LYS A 1 420 ? 112.14700 94.74400  56.00600  1.000 57.16264  ? 420 LYS A CE   1 
ATOM   2552 N NZ   . LYS A 1 420 ? 111.93300 93.82200  54.85800  1.000 56.17277  ? 420 LYS A NZ   1 
ATOM   2553 N N    . ILE A 1 421 ? 114.82300 100.02000 56.94400  1.000 57.33029  ? 421 ILE A N    1 
ATOM   2554 C CA   . ILE A 1 421 ? 114.03300 101.25000 56.91900  1.000 53.75945  ? 421 ILE A CA   1 
ATOM   2555 C C    . ILE A 1 421 ? 114.34300 102.05500 55.66500  1.000 50.83084  ? 421 ILE A C    1 
ATOM   2556 O O    . ILE A 1 421 ? 113.44600 102.64800 55.05300  1.000 51.05199  ? 421 ILE A O    1 
ATOM   2557 C CB   . ILE A 1 421 ? 114.27300 102.08000 58.19400  1.000 53.01666  ? 421 ILE A CB   1 
ATOM   2558 C CG1  . ILE A 1 421 ? 113.69900 101.37000 59.41800  1.000 49.70284  ? 421 ILE A CG1  1 
ATOM   2559 C CG2  . ILE A 1 421 ? 113.66200 103.46400 58.04900  1.000 50.18280  ? 421 ILE A CG2  1 
ATOM   2560 C CD1  . ILE A 1 421 ? 114.22100 101.91200 60.72500  1.000 50.11252  ? 421 ILE A CD1  1 
ATOM   2561 N N    . ASP A 1 422 ? 115.61500 102.09100 55.26000  1.000 56.93241  ? 422 ASP A N    1 
ATOM   2562 C CA   . ASP A 1 422 ? 115.97600 102.82200 54.05000  1.000 57.55854  ? 422 ASP A CA   1 
ATOM   2563 C C    . ASP A 1 422 ? 115.33700 102.21300 52.81000  1.000 58.97836  ? 422 ASP A C    1 
ATOM   2564 O O    . ASP A 1 422 ? 115.03500 102.93300 51.85200  1.000 57.14551  ? 422 ASP A O    1 
ATOM   2565 C CB   . ASP A 1 422 ? 117.49500 102.86600 53.88400  1.000 55.52680  ? 422 ASP A CB   1 
ATOM   2566 C CG   . ASP A 1 422 ? 118.13900 103.98500 54.67700  1.000 60.82137  ? 422 ASP A CG   1 
ATOM   2567 O OD1  . ASP A 1 422 ? 117.42600 104.94100 55.04800  1.000 61.98770  ? 422 ASP A OD1  1 
ATOM   2568 O OD2  . ASP A 1 422 ? 119.36100 103.91100 54.92300  1.000 61.88092  ? 422 ASP A OD2  1 
ATOM   2569 N N    . LYS A 1 423 ? 115.12200 100.89600 52.80300  1.000 63.49304  ? 423 LYS A N    1 
ATOM   2570 C CA   . LYS A 1 423 ? 114.56600 100.26400 51.61000  1.000 58.94096  ? 423 LYS A CA   1 
ATOM   2571 C C    . LYS A 1 423 ? 113.05300 100.41500 51.48200  1.000 63.36221  ? 423 LYS A C    1 
ATOM   2572 O O    . LYS A 1 423 ? 112.52600 100.25200 50.37600  1.000 64.05127  ? 423 LYS A O    1 
ATOM   2573 C CB   . LYS A 1 423 ? 114.92900 98.77800  51.58500  1.000 60.10793  ? 423 LYS A CB   1 
ATOM   2574 C CG   . LYS A 1 423 ? 116.00300 98.42000  50.57300  1.000 62.27644  ? 423 LYS A CG   1 
ATOM   2575 C CD   . LYS A 1 423 ? 116.62300 97.06700  50.87800  1.000 64.58859  ? 423 LYS A CD   1 
ATOM   2576 C CE   . LYS A 1 423 ? 117.94100 97.21800  51.62300  1.000 65.70442  ? 423 LYS A CE   1 
ATOM   2577 N NZ   . LYS A 1 423 ? 118.29600 95.98900  52.38500  1.000 62.19878  ? 423 LYS A NZ   1 
ATOM   2578 N N    . LYS A 1 424 ? 112.33800 100.72400 52.56700  1.000 65.92551  ? 424 LYS A N    1 
ATOM   2579 C CA   . LYS A 1 424 ? 110.88100 100.81900 52.52500  1.000 61.32252  ? 424 LYS A CA   1 
ATOM   2580 C C    . LYS A 1 424 ? 110.37000 102.15000 53.06800  1.000 62.97639  ? 424 LYS A C    1 
ATOM   2581 O O    . LYS A 1 424 ? 109.23400 102.23500 53.53800  1.000 65.16374  ? 424 LYS A O    1 
ATOM   2582 C CB   . LYS A 1 424 ? 110.23600 99.65800  53.28000  1.000 62.48682  ? 424 LYS A CB   1 
ATOM   2583 C CG   . LYS A 1 424 ? 110.97100 98.34100  53.13700  1.000 63.88590  ? 424 LYS A CG   1 
ATOM   2584 C CD   . LYS A 1 424 ? 109.99200 97.18800  52.99500  1.000 65.15045  ? 424 LYS A CD   1 
ATOM   2585 C CE   . LYS A 1 424 ? 109.59400 96.97900  51.54300  1.000 64.69287  ? 424 LYS A CE   1 
ATOM   2586 N NZ   . LYS A 1 424 ? 110.77400 96.73800  50.67000  1.000 63.90060  ? 424 LYS A NZ   1 
ATOM   2587 N N    . SER A 1 425 ? 111.19000 103.20000 53.00700  1.000 65.37698  ? 425 SER A N    1 
ATOM   2588 C CA   . SER A 1 425 ? 110.79400 104.48400 53.57700  1.000 61.00059  ? 425 SER A CA   1 
ATOM   2589 C C    . SER A 1 425 ? 109.54900 105.06700 52.91700  1.000 63.59554  ? 425 SER A C    1 
ATOM   2590 O O    . SER A 1 425 ? 108.92600 105.96600 53.49100  1.000 64.92396  ? 425 SER A O    1 
ATOM   2591 C CB   . SER A 1 425 ? 111.94800 105.48200 53.47100  1.000 62.77572  ? 425 SER A CB   1 
ATOM   2592 O OG   . SER A 1 425 ? 112.33000 105.67600 52.12100  1.000 66.82676  ? 425 SER A OG   1 
ATOM   2593 N N    . TYR A 1 426 ? 109.17000 104.58500 51.73200  1.000 66.01255  ? 426 TYR A N    1 
ATOM   2594 C CA   . TYR A 1 426 ? 108.00300 105.13100 51.05100  1.000 62.78896  ? 426 TYR A CA   1 
ATOM   2595 C C    . TYR A 1 426 ? 106.69700 104.81400 51.76500  1.000 64.05557  ? 426 TYR A C    1 
ATOM   2596 O O    . TYR A 1 426 ? 105.66400 105.39500 51.41500  1.000 64.93704  ? 426 TYR A O    1 
ATOM   2597 C CB   . TYR A 1 426 ? 107.95000 104.62300 49.60500  1.000 62.13829  ? 426 TYR A CB   1 
ATOM   2598 C CG   . TYR A 1 426 ? 107.77300 103.12500 49.45800  1.000 65.01410  ? 426 TYR A CG   1 
ATOM   2599 C CD1  . TYR A 1 426 ? 106.55500 102.51600 49.73400  1.000 63.43721  ? 426 TYR A CD1  1 
ATOM   2600 C CD2  . TYR A 1 426 ? 108.82500 102.32100 49.04200  1.000 65.82118  ? 426 TYR A CD2  1 
ATOM   2601 C CE1  . TYR A 1 426 ? 106.39100 101.15300 49.60000  1.000 62.99156  ? 426 TYR A CE1  1 
ATOM   2602 C CE2  . TYR A 1 426 ? 108.66900 100.95500 48.90600  1.000 64.44117  ? 426 TYR A CE2  1 
ATOM   2603 C CZ   . TYR A 1 426 ? 107.45000 100.37800 49.18700  1.000 65.81231  ? 426 TYR A CZ   1 
ATOM   2604 O OH   . TYR A 1 426 ? 107.28700 99.01900  49.05500  1.000 68.15108  ? 426 TYR A OH   1 
ATOM   2605 N N    . LEU A 1 427 ? 106.71200 103.91500 52.74600  1.000 62.81222  ? 427 LEU A N    1 
ATOM   2606 C CA   . LEU A 1 427 ? 105.52400 103.58200 53.51700  1.000 60.04401  ? 427 LEU A CA   1 
ATOM   2607 C C    . LEU A 1 427 ? 105.31100 104.50200 54.71100  1.000 61.82279  ? 427 LEU A C    1 
ATOM   2608 O O    . LEU A 1 427 ? 104.29400 104.37100 55.40000  1.000 63.53535  ? 427 LEU A O    1 
ATOM   2609 C CB   . LEU A 1 427 ? 105.59700 102.13100 54.00300  1.000 61.71392  ? 427 LEU A CB   1 
ATOM   2610 C CG   . LEU A 1 427 ? 105.52400 101.03100 52.94300  1.000 62.71830  ? 427 LEU A CG   1 
ATOM   2611 C CD1  . LEU A 1 427 ? 105.60500 99.66100  53.59500  1.000 62.98290  ? 427 LEU A CD1  1 
ATOM   2612 C CD2  . LEU A 1 427 ? 104.25100 101.15900 52.12600  1.000 63.98178  ? 427 LEU A CD2  1 
ATOM   2613 N N    . LEU A 1 428 ? 106.23700 105.42500 54.97500  1.000 58.86273  ? 428 LEU A N    1 
ATOM   2614 C CA   . LEU A 1 428 ? 106.13700 106.30100 56.13100  1.000 58.18008  ? 428 LEU A CA   1 
ATOM   2615 C C    . LEU A 1 428 ? 105.78100 107.73700 55.78000  1.000 60.81711  ? 428 LEU A C    1 
ATOM   2616 O O    . LEU A 1 428 ? 105.39700 108.49700 56.67500  1.000 62.92491  ? 428 LEU A O    1 
ATOM   2617 C CB   . LEU A 1 428 ? 107.45600 106.29200 56.91600  1.000 60.70867  ? 428 LEU A CB   1 
ATOM   2618 C CG   . LEU A 1 428 ? 108.02800 104.92200 57.28500  1.000 60.85510  ? 428 LEU A CG   1 
ATOM   2619 C CD1  . LEU A 1 428 ? 109.49200 105.04700 57.67200  1.000 59.63903  ? 428 LEU A CD1  1 
ATOM   2620 C CD2  . LEU A 1 428 ? 107.22800 104.28000 58.40300  1.000 58.08636  ? 428 LEU A CD2  1 
ATOM   2621 N N    . VAL A 1 429 ? 105.89600 108.13200 54.51300  1.000 73.20508  ? 429 VAL A N    1 
ATOM   2622 C CA   . VAL A 1 429 ? 105.59400 109.48800 54.08200  1.000 74.15906  ? 429 VAL A CA   1 
ATOM   2623 C C    . VAL A 1 429 ? 104.64700 109.43100 52.89100  1.000 74.91706  ? 429 VAL A C    1 
ATOM   2624 O O    . VAL A 1 429 ? 104.40800 108.37600 52.30400  1.000 74.50595  ? 429 VAL A O    1 
ATOM   2625 C CB   . VAL A 1 429 ? 106.86500 110.28500 53.72400  1.000 73.25278  ? 429 VAL A CB   1 
ATOM   2626 C CG1  . VAL A 1 429 ? 107.89200 110.17600 54.84000  1.000 72.02724  ? 429 VAL A CG1  1 
ATOM   2627 C CG2  . VAL A 1 429 ? 107.44200 109.79300 52.40700  1.000 74.27895  ? 429 VAL A CG2  1 
ATOM   2628 N N    . ASN A 1 430 ? 104.10500 110.59400 52.54300  1.000 88.36432  ? 430 ASN A N    1 
ATOM   2629 C CA   . ASN A 1 430 ? 103.23800 110.75000 51.38100  1.000 88.77255  ? 430 ASN A CA   1 
ATOM   2630 C C    . ASN A 1 430 ? 104.04600 111.41100 50.27200  1.000 90.21425  ? 430 ASN A C    1 
ATOM   2631 O O    . ASN A 1 430 ? 104.48000 112.55900 50.41800  1.000 90.83399  ? 430 ASN A O    1 
ATOM   2632 C CB   . ASN A 1 430 ? 102.00300 111.58400 51.72100  1.000 88.65650  ? 430 ASN A CB   1 
ATOM   2633 C CG   . ASN A 1 430 ? 101.10300 110.90800 52.73600  1.000 90.81376  ? 430 ASN A CG   1 
ATOM   2634 O OD1  . ASN A 1 430 ? 101.37300 110.93000 53.93700  1.000 91.17764  ? 430 ASN A OD1  1 
ATOM   2635 N ND2  . ASN A 1 430 ? 100.02200 110.30100 52.25700  1.000 90.98472  ? 430 ASN A ND2  1 
ATOM   2636 N N    . SER A 1 431 ? 104.26200 110.70600 49.17000  1.000 99.55580  ? 431 SER A N    1 
ATOM   2637 C CA   . SER A 1 431 ? 105.11000 111.24400 48.11200  1.000 99.75053  ? 431 SER A CA   1 
ATOM   2638 C C    . SER A 1 431 ? 104.32400 111.86800 46.97500  1.000 99.91561  ? 431 SER A C    1 
ATOM   2639 O O    . SER A 1 431 ? 104.87300 112.12600 45.90600  1.000 100.66948 ? 431 SER A O    1 
ATOM   2640 C CB   . SER A 1 431 ? 106.00100 110.13600 47.56100  1.000 99.76811  ? 431 SER A CB   1 
ATOM   2641 O OG   . SER A 1 431 ? 105.23200 109.12000 46.94400  1.000 100.46964 ? 431 SER A OG   1 
ATOM   2642 N N    . GLU A 1 432 ? 103.04300 112.11400 47.19400  1.000 103.48630 ? 432 GLU A N    1 
ATOM   2643 C CA   . GLU A 1 432 ? 102.20900 112.66900 46.14300  1.000 103.52938 ? 432 GLU A CA   1 
ATOM   2644 C C    . GLU A 1 432 ? 102.01500 114.15400 46.33600  1.000 104.12642 ? 432 GLU A C    1 
ATOM   2645 O O    . GLU A 1 432 ? 101.28500 114.78600 45.57900  1.000 104.31934 ? 432 GLU A O    1 
ATOM   2646 C CB   . GLU A 1 432 ? 100.85400 111.97100 46.13800  1.000 104.27978 ? 432 GLU A CB   1 
ATOM   2647 C CG   . GLU A 1 432 ? 100.05200 112.17300 47.41300  1.000 104.85898 ? 432 GLU A CG   1 
ATOM   2648 C CD   . GLU A 1 432 ? 98.76300  111.37200 47.43300  1.000 104.83047 ? 432 GLU A CD   1 
ATOM   2649 O OE1  . GLU A 1 432 ? 98.31300  110.93100 46.35400  1.000 105.56333 ? 432 GLU A OE1  1 
ATOM   2650 O OE2  . GLU A 1 432 ? 98.20000  111.18200 48.53000  1.000 104.35239 ? 432 GLU A OE2  1 
ATOM   2651 N N    . CYS A 1 433 ? 102.65800 114.71600 47.34900  1.000 103.79725 ? 433 CYS A N    1 
ATOM   2652 C CA   . CYS A 1 433 ? 102.49100 116.13100 47.64400  1.000 103.19355 ? 433 CYS A CA   1 
ATOM   2653 C C    . CYS A 1 433 ? 103.81400 116.85100 47.63700  1.000 102.83763 ? 433 CYS A C    1 
ATOM   2654 O O    . CYS A 1 433 ? 103.88600 118.01800 48.01100  1.000 103.60296 ? 433 CYS A O    1 
ATOM   2655 C CB   . CYS A 1 433 ? 101.84500 116.29600 49.01700  1.000 103.59840 ? 433 CYS A CB   1 
ATOM   2656 S SG   . CYS A 1 433 ? 100.15900 115.66000 49.13700  1.000 105.55569 ? 433 CYS A SG   1 
ATOM   2657 N N    . TRP A 1 434 ? 104.86700 116.17400 47.21100  1.000 101.11695 ? 434 TRP A N    1 
ATOM   2658 C CA   . TRP A 1 434 ? 106.19200 116.77500 47.29000  1.000 101.22557 ? 434 TRP A CA   1 
ATOM   2659 C C    . TRP A 1 434 ? 106.33700 118.01800 46.42900  1.000 101.69388 ? 434 TRP A C    1 
ATOM   2660 O O    . TRP A 1 434 ? 106.02100 117.99900 45.24200  1.000 101.21534 ? 434 TRP A O    1 
ATOM   2661 C CB   . TRP A 1 434 ? 107.25800 115.73200 46.95500  1.000 101.02909 ? 434 TRP A CB   1 
ATOM   2662 C CG   . TRP A 1 434 ? 107.50500 114.80600 48.10200  1.000 100.71815 ? 434 TRP A CG   1 
ATOM   2663 C CD1  . TRP A 1 434 ? 106.99800 114.91700 49.36200  1.000 99.74876  ? 434 TRP A CD1  1 
ATOM   2664 C CD2  . TRP A 1 434 ? 108.31700 113.62800 48.09900  1.000 101.33699 ? 434 TRP A CD2  1 
ATOM   2665 N NE1  . TRP A 1 434 ? 107.44100 113.88300 50.14400  1.000 100.18369 ? 434 TRP A NE1  1 
ATOM   2666 C CE2  . TRP A 1 434 ? 108.25400 113.07600 49.39400  1.000 100.77715 ? 434 TRP A CE2  1 
ATOM   2667 C CE3  . TRP A 1 434 ? 109.09000 112.98500 47.12900  1.000 100.77482 ? 434 TRP A CE3  1 
ATOM   2668 C CZ2  . TRP A 1 434 ? 108.93400 111.91500 49.74300  1.000 100.51326 ? 434 TRP A CZ2  1 
ATOM   2669 C CZ3  . TRP A 1 434 ? 109.76500 111.83200 47.47800  1.000 100.45296 ? 434 TRP A CZ3  1 
ATOM   2670 C CH2  . TRP A 1 434 ? 109.68300 111.30900 48.77300  1.000 100.95536 ? 434 TRP A CH2  1 
ATOM   2671 N N    . GLU A 1 435 ? 106.81300 119.10000 47.03500  1.000 109.13758 ? 435 GLU A N    1 
ATOM   2672 C CA   . GLU A 1 435 ? 106.99500 120.34600 46.30600  1.000 109.61038 ? 435 GLU A CA   1 
ATOM   2673 C C    . GLU A 1 435 ? 108.27200 121.03700 46.75600  1.000 110.13173 ? 435 GLU A C    1 
ATOM   2674 O O    . GLU A 1 435 ? 108.64100 120.97600 47.92700  1.000 110.74591 ? 435 GLU A O    1 
ATOM   2675 C CB   . GLU A 1 435 ? 105.80200 121.26900 46.52800  1.000 109.71479 ? 435 GLU A CB   1 
ATOM   2676 C CG   . GLU A 1 435 ? 105.41200 121.43000 47.98700  1.000 111.35163 ? 435 GLU A CG   1 
ATOM   2677 C CD   . GLU A 1 435 ? 106.17600 122.54300 48.68000  1.000 112.22998 ? 435 GLU A CD   1 
ATOM   2678 O OE1  . GLU A 1 435 ? 106.74000 123.40800 47.97800  1.000 110.89506 ? 435 GLU A OE1  1 
ATOM   2679 O OE2  . GLU A 1 435 ? 106.21400 122.55200 49.92900  1.000 112.28587 ? 435 GLU A OE2  1 
ATOM   2680 N N    . LYS A 1 527 ? 94.20200  112.89600 55.04900  1.000 88.64230  ? 527 LYS A N    1 
ATOM   2681 C CA   . LYS A 1 527 ? 93.84300  113.43200 56.35700  1.000 88.56572  ? 527 LYS A CA   1 
ATOM   2682 C C    . LYS A 1 527 ? 95.07000  113.54500 57.25500  1.000 88.70708  ? 527 LYS A C    1 
ATOM   2683 O O    . LYS A 1 527 ? 96.08900  112.89600 57.01700  1.000 87.78390  ? 527 LYS A O    1 
ATOM   2684 C CB   . LYS A 1 527 ? 92.77800  112.55600 57.02100  1.000 87.99092  ? 527 LYS A CB   1 
ATOM   2685 C CG   . LYS A 1 527 ? 91.35500  112.87500 56.58700  1.000 87.83133  ? 527 LYS A CG   1 
ATOM   2686 C CD   . LYS A 1 527 ? 90.36100  111.86800 57.14700  1.000 88.42570  ? 527 LYS A CD   1 
ATOM   2687 C CE   . LYS A 1 527 ? 90.20300  112.01500 58.65200  1.000 87.46771  ? 527 LYS A CE   1 
ATOM   2688 N NZ   . LYS A 1 527 ? 90.67400  113.34000 59.14000  1.000 88.10448  ? 527 LYS A NZ   1 
ATOM   2689 N N    . THR A 1 528 ? 94.96600  114.38200 58.28900  1.000 84.78569  ? 528 THR A N    1 
ATOM   2690 C CA   . THR A 1 528 ? 96.06600  114.53300 59.23700  1.000 83.99038  ? 528 THR A CA   1 
ATOM   2691 C C    . THR A 1 528 ? 96.30500  113.24600 60.02000  1.000 83.87453  ? 528 THR A C    1 
ATOM   2692 O O    . THR A 1 528 ? 97.45800  112.87000 60.27300  1.000 83.70017  ? 528 THR A O    1 
ATOM   2693 C CB   . THR A 1 528 ? 95.77800  115.69300 60.19000  1.000 82.93343  ? 528 THR A CB   1 
ATOM   2694 O OG1  . THR A 1 528 ? 96.04100  116.93600 59.52700  1.000 83.20011  ? 528 THR A OG1  1 
ATOM   2695 C CG2  . THR A 1 528 ? 96.65000  115.59300 61.43200  1.000 81.93816  ? 528 THR A CG2  1 
ATOM   2696 N N    . TYR A 1 529 ? 95.22900  112.55600 60.40500  1.000 76.49646  ? 529 TYR A N    1 
ATOM   2697 C CA   . TYR A 1 529 ? 95.37500  111.36100 61.22800  1.000 76.25111  ? 529 TYR A CA   1 
ATOM   2698 C C    . TYR A 1 529 ? 96.16300  110.28100 60.49900  1.000 77.28025  ? 529 TYR A C    1 
ATOM   2699 O O    . TYR A 1 529 ? 97.00400  109.60500 61.10200  1.000 76.64037  ? 529 TYR A O    1 
ATOM   2700 C CB   . TYR A 1 529 ? 94.00400  110.83400 61.64900  1.000 75.44288  ? 529 TYR A CB   1 
ATOM   2701 C CG   . TYR A 1 529 ? 94.07900  109.68400 62.62600  1.000 76.74049  ? 529 TYR A CG   1 
ATOM   2702 C CD1  . TYR A 1 529 ? 94.33900  109.90800 63.97200  1.000 75.06201  ? 529 TYR A CD1  1 
ATOM   2703 C CD2  . TYR A 1 529 ? 93.90100  108.37300 62.20400  1.000 75.83293  ? 529 TYR A CD2  1 
ATOM   2704 C CE1  . TYR A 1 529 ? 94.41400  108.86100 64.87000  1.000 74.68922  ? 529 TYR A CE1  1 
ATOM   2705 C CE2  . TYR A 1 529 ? 93.97500  107.31800 63.09500  1.000 76.82296  ? 529 TYR A CE2  1 
ATOM   2706 C CZ   . TYR A 1 529 ? 94.23300  107.56900 64.42700  1.000 77.11600  ? 529 TYR A CZ   1 
ATOM   2707 O OH   . TYR A 1 529 ? 94.30700  106.52300 65.31900  1.000 74.67953  ? 529 TYR A OH   1 
ATOM   2708 N N    . GLU A 1 530 ? 95.90100  110.09800 59.20300  1.000 74.14600  ? 530 GLU A N    1 
ATOM   2709 C CA   . GLU A 1 530 ? 96.61100  109.06900 58.44800  1.000 76.81992  ? 530 GLU A CA   1 
ATOM   2710 C C    . GLU A 1 530 ? 98.10200  109.37800 58.36700  1.000 78.83088  ? 530 GLU A C    1 
ATOM   2711 O O    . GLU A 1 530 ? 98.94300  108.48800 58.55200  1.000 76.50634  ? 530 GLU A O    1 
ATOM   2712 C CB   . GLU A 1 530 ? 96.00800  108.94200 57.05000  1.000 75.14295  ? 530 GLU A CB   1 
ATOM   2713 C CG   . GLU A 1 530 ? 96.94800  108.34800 56.01500  1.000 76.99323  ? 530 GLU A CG   1 
ATOM   2714 C CD   . GLU A 1 530 ? 96.25300  107.36700 55.09400  1.000 77.77394  ? 530 GLU A CD   1 
ATOM   2715 O OE1  . GLU A 1 530 ? 95.03600  107.52700 54.86300  1.000 77.45732  ? 530 GLU A OE1  1 
ATOM   2716 O OE2  . GLU A 1 530 ? 96.92300  106.43500 54.60100  1.000 78.46944  ? 530 GLU A OE2  1 
ATOM   2717 N N    . SER A 1 531 ? 98.44800  110.63800 58.09400  1.000 67.81955  ? 531 SER A N    1 
ATOM   2718 C CA   . SER A 1 531 ? 99.85300  111.02400 58.04000  1.000 66.80911  ? 531 SER A CA   1 
ATOM   2719 C C    . SER A 1 531 ? 100.53700 110.81100 59.38500  1.000 66.79339  ? 531 SER A C    1 
ATOM   2720 O O    . SER A 1 531 ? 101.66600 110.30700 59.44300  1.000 70.90114  ? 531 SER A O    1 
ATOM   2721 C CB   . SER A 1 531 ? 99.97500  112.48100 57.59700  1.000 69.51868  ? 531 SER A CB   1 
ATOM   2722 O OG   . SER A 1 531 ? 99.94000  112.59000 56.18500  1.000 71.55294  ? 531 SER A OG   1 
ATOM   2723 N N    . ALA A 1 532 ? 99.87000  111.18300 60.48100  1.000 58.52690  ? 532 ALA A N    1 
ATOM   2724 C CA   . ALA A 1 532 ? 100.47700 110.99500 61.79600  1.000 60.27950  ? 532 ALA A CA   1 
ATOM   2725 C C    . ALA A 1 532 ? 100.65000 109.51400 62.11800  1.000 63.66892  ? 532 ALA A C    1 
ATOM   2726 O O    . ALA A 1 532 ? 101.67300 109.10500 62.68800  1.000 63.23221  ? 532 ALA A O    1 
ATOM   2727 C CB   . ALA A 1 532 ? 99.63300  111.68900 62.86400  1.000 61.11805  ? 532 ALA A CB   1 
ATOM   2728 N N    . SER A 1 533 ? 99.66200  108.69400 61.75200  1.000 59.47598  ? 533 SER A N    1 
ATOM   2729 C CA   . SER A 1 533 ? 99.76800  107.26000 61.98400  1.000 57.86885  ? 533 SER A CA   1 
ATOM   2730 C C    . SER A 1 533 ? 100.93900 106.67600 61.21000  1.000 59.83150  ? 533 SER A C    1 
ATOM   2731 O O    . SER A 1 533 ? 101.67400 105.82500 61.72500  1.000 60.31585  ? 533 SER A O    1 
ATOM   2732 C CB   . SER A 1 533 ? 98.46300  106.56900 61.59100  1.000 58.01867  ? 533 SER A CB   1 
ATOM   2733 O OG   . SER A 1 533 ? 97.39500  106.97900 62.42500  1.000 60.94629  ? 533 SER A OG   1 
ATOM   2734 N N    . ALA A 1 534 ? 101.13000 107.12400 59.96800  1.000 57.57010  ? 534 ALA A N    1 
ATOM   2735 C CA   . ALA A 1 534 ? 102.27700 106.66200 59.19500  1.000 56.42332  ? 534 ALA A CA   1 
ATOM   2736 C C    . ALA A 1 534 ? 103.58800 107.10300 59.83700  1.000 53.89870  ? 534 ALA A C    1 
ATOM   2737 O O    . ALA A 1 534 ? 104.55500 106.33400 59.88100  1.000 55.04905  ? 534 ALA A O    1 
ATOM   2738 C CB   . ALA A 1 534 ? 102.18100 107.17400 57.75900  1.000 56.06606  ? 534 ALA A CB   1 
ATOM   2739 N N    . LEU A 1 535 ? 103.63900 108.33600 60.34000  1.000 45.47179  ? 535 LEU A N    1 
ATOM   2740 C CA   . LEU A 1 535 ? 104.86700 108.87700 60.91200  1.000 43.77864  ? 535 LEU A CA   1 
ATOM   2741 C C    . LEU A 1 535 ? 105.20600 108.32200 62.29400  1.000 45.54623  ? 535 LEU A C    1 
ATOM   2742 O O    . LEU A 1 535 ? 106.33500 108.51900 62.75400  1.000 50.29062  ? 535 LEU A O    1 
ATOM   2743 C CB   . LEU A 1 535 ? 104.77200 110.40300 60.98900  1.000 48.64260  ? 535 LEU A CB   1 
ATOM   2744 C CG   . LEU A 1 535 ? 106.03400 111.19300 60.64000  1.000 49.95860  ? 535 LEU A CG   1 
ATOM   2745 C CD1  . LEU A 1 535 ? 106.45900 110.92300 59.20800  1.000 47.56778  ? 535 LEU A CD1  1 
ATOM   2746 C CD2  . LEU A 1 535 ? 105.81100 112.67900 60.86400  1.000 45.66475  ? 535 LEU A CD2  1 
ATOM   2747 N N    . SER A 1 536 ? 104.27000 107.64900 62.96900  1.000 41.90802  ? 536 SER A N    1 
ATOM   2748 C CA   . SER A 1 536 ? 104.57500 107.11500 64.30000  1.000 42.91467  ? 536 SER A CA   1 
ATOM   2749 C C    . SER A 1 536 ? 105.55500 105.93700 64.26000  1.000 45.63567  ? 536 SER A C    1 
ATOM   2750 O O    . SER A 1 536 ? 106.33600 105.73700 65.20900  1.000 44.71003  ? 536 SER A O    1 
ATOM   2751 C CB   . SER A 1 536 ? 103.27900 106.69300 64.99100  1.000 42.64810  ? 536 SER A CB   1 
ATOM   2752 O OG   . SER A 1 536 ? 102.44700 107.81000 65.23200  1.000 44.62111  ? 536 SER A OG   1 
ATOM   2753 N N    . LEU A 1 537 ? 105.52600 105.14600 63.18500  1.000 40.06270  ? 537 LEU A N    1 
ATOM   2754 C CA   . LEU A 1 537 ? 106.41200 103.98900 63.09100  1.000 38.15487  ? 537 LEU A CA   1 
ATOM   2755 C C    . LEU A 1 537 ? 107.87500 104.41500 63.04300  1.000 38.82857  ? 537 LEU A C    1 
ATOM   2756 O O    . LEU A 1 537 ? 108.74500 103.77300 63.65300  1.000 39.53256  ? 537 LEU A O    1 
ATOM   2757 C CB   . LEU A 1 537 ? 106.04400 103.16600 61.85600  1.000 38.21327  ? 537 LEU A CB   1 
ATOM   2758 C CG   . LEU A 1 537 ? 106.47900 101.70300 61.78000  1.000 45.16546  ? 537 LEU A CG   1 
ATOM   2759 C CD1  . LEU A 1 537 ? 105.58300 100.83200 62.64100  1.000 45.67123  ? 537 LEU A CD1  1 
ATOM   2760 C CD2  . LEU A 1 537 ? 106.45300 101.23200 60.34000  1.000 39.68307  ? 537 LEU A CD2  1 
ATOM   2761 N N    . ALA A 1 538 ? 108.16300 105.52000 62.35100  1.000 32.02027  ? 538 ALA A N    1 
ATOM   2762 C CA   . ALA A 1 538 ? 109.53200 106.01200 62.30600  1.000 35.36723  ? 538 ALA A CA   1 
ATOM   2763 C C    . ALA A 1 538 ? 109.97700 106.52600 63.66600  1.000 31.01503  ? 538 ALA A C    1 
ATOM   2764 O O    . ALA A 1 538 ? 111.16600 106.45400 63.99300  1.000 34.18040  ? 538 ALA A O    1 
ATOM   2765 C CB   . ALA A 1 538 ? 109.66000 107.10900 61.25100  1.000 35.72916  ? 538 ALA A CB   1 
ATOM   2766 N N    . THR A 1 539 ? 109.03400 106.96300 64.50100  1.000 18.62910  ? 539 THR A N    1 
ATOM   2767 C CA   . THR A 1 539 ? 109.40000 107.42000 65.83600  1.000 28.32229  ? 539 THR A CA   1 
ATOM   2768 C C    . THR A 1 539 ? 109.74800 106.23700 66.72600  1.000 28.33296  ? 539 THR A C    1 
ATOM   2769 O O    . THR A 1 539 ? 110.72500 106.28200 67.48700  1.000 26.61325  ? 539 THR A O    1 
ATOM   2770 C CB   . THR A 1 539 ? 108.25300 108.23000 66.44400  1.000 30.58203  ? 539 THR A CB   1 
ATOM   2771 O OG1  . THR A 1 539 ? 108.24100 109.54700 65.88100  1.000 36.88735  ? 539 THR A OG1  1 
ATOM   2772 C CG2  . THR A 1 539 ? 108.40400 108.33000 67.95500  1.000 23.22674  ? 539 THR A CG2  1 
ATOM   2773 N N    . PHE A 1 540 ? 108.98900 105.14900 66.59900  1.000 23.72966  ? 540 PHE A N    1 
ATOM   2774 C CA   . PHE A 1 540 ? 109.32300 103.92900 67.33400  1.000 23.43686  ? 540 PHE A CA   1 
ATOM   2775 C C    . PHE A 1 540 ? 110.70600 103.41200 66.92900  1.000 26.41327  ? 540 PHE A C    1 
ATOM   2776 O O    . PHE A 1 540 ? 111.54600 103.08300 67.78500  1.000 26.56122  ? 540 PHE A O    1 
ATOM   2777 C CB   . PHE A 1 540 ? 108.24000 102.87500 67.08600  1.000 23.37885  ? 540 PHE A CB   1 
ATOM   2778 C CG   . PHE A 1 540 ? 108.27500 101.71600 68.04400  1.000 19.41418  ? 540 PHE A CG   1 
ATOM   2779 C CD1  . PHE A 1 540 ? 107.55500 101.75700 69.22400  1.000 23.31518  ? 540 PHE A CD1  1 
ATOM   2780 C CD2  . PHE A 1 540 ? 109.00600 100.57900 67.75300  1.000 25.86215  ? 540 PHE A CD2  1 
ATOM   2781 C CE1  . PHE A 1 540 ? 107.57900 100.69500 70.10600  1.000 23.32575  ? 540 PHE A CE1  1 
ATOM   2782 C CE2  . PHE A 1 540 ? 109.03300 99.51300  68.63100  1.000 24.44159  ? 540 PHE A CE2  1 
ATOM   2783 C CZ   . PHE A 1 540 ? 108.31900 99.57100  69.80800  1.000 21.51633  ? 540 PHE A CZ   1 
ATOM   2784 N N    . ALA A 1 541 ? 110.97500 103.37500 65.62000  1.000 27.45863  ? 541 ALA A N    1 
ATOM   2785 C CA   . ALA A 1 541 ? 112.27500 102.90300 65.14700  1.000 20.17634  ? 541 ALA A CA   1 
ATOM   2786 C C    . ALA A 1 541 ? 113.41500 103.80100 65.62400  1.000 27.67797  ? 541 ALA A C    1 
ATOM   2787 O O    . ALA A 1 541 ? 114.46400 103.30800 66.06600  1.000 28.63567  ? 541 ALA A O    1 
ATOM   2788 C CB   . ALA A 1 541 ? 112.27100 102.80500 63.62200  1.000 24.35685  ? 541 ALA A CB   1 
ATOM   2789 N N    . SER A 1 542 ? 113.23600 105.12200 65.53600  1.000 18.56839  ? 542 SER A N    1 
ATOM   2790 C CA   . SER A 1 542 ? 114.28500 106.03800 65.97200  1.000 18.58914  ? 542 SER A CA   1 
ATOM   2791 C C    . SER A 1 542 ? 114.56100 105.89600 67.46200  1.000 24.04205  ? 542 SER A C    1 
ATOM   2792 O O    . SER A 1 542 ? 115.71600 105.98300 67.89800  1.000 31.30980  ? 542 SER A O    1 
ATOM   2793 C CB   . SER A 1 542 ? 113.89900 107.47600 65.62800  1.000 27.10540  ? 542 SER A CB   1 
ATOM   2794 O OG   . SER A 1 542 ? 113.20300 107.53200 64.39600  1.000 34.09619  ? 542 SER A OG   1 
ATOM   2795 N N    . LEU A 1 543 ? 113.51800 105.66500 68.26400  1.000 16.40392  ? 543 LEU A N    1 
ATOM   2796 C CA   . LEU A 1 543 ? 113.74900 105.51600 69.69500  1.000 16.90097  ? 543 LEU A CA   1 
ATOM   2797 C C    . LEU A 1 543 ? 114.50000 104.22700 70.00000  1.000 21.21284  ? 543 LEU A C    1 
ATOM   2798 O O    . LEU A 1 543 ? 115.35900 104.20100 70.89500  1.000 28.16319  ? 543 LEU A O    1 
ATOM   2799 C CB   . LEU A 1 543 ? 112.42000 105.55400 70.44800  1.000 25.24948  ? 543 LEU A CB   1 
ATOM   2800 C CG   . LEU A 1 543 ? 111.76200 106.92800 70.59000  1.000 21.35301  ? 543 LEU A CG   1 
ATOM   2801 C CD1  . LEU A 1 543 ? 110.42400 106.81200 71.30000  1.000 17.09646  ? 543 LEU A CD1  1 
ATOM   2802 C CD2  . LEU A 1 543 ? 112.67900 107.89500 71.31800  1.000 25.51493  ? 543 LEU A CD2  1 
ATOM   2803 N N    . LEU A 1 544 ? 114.24800 103.16800 69.22700  1.000 24.51621  ? 544 LEU A N    1 
ATOM   2804 C CA   . LEU A 1 544 ? 115.02500 101.94600 69.42300  1.000 22.84990  ? 544 LEU A CA   1 
ATOM   2805 C C    . LEU A 1 544 ? 116.48600 102.15000 69.02900  1.000 21.34322  ? 544 LEU A C    1 
ATOM   2806 O O    . LEU A 1 544 ? 117.40000 101.64500 69.70000  1.000 23.53575  ? 544 LEU A O    1 
ATOM   2807 C CB   . LEU A 1 544 ? 114.40700 100.80000 68.62400  1.000 25.16825  ? 544 LEU A CB   1 
ATOM   2808 C CG   . LEU A 1 544 ? 114.31700 99.43200  69.30000  1.000 28.68455  ? 544 LEU A CG   1 
ATOM   2809 C CD1  . LEU A 1 544 ? 113.87700 99.56500  70.74800  1.000 20.28710  ? 544 LEU A CD1  1 
ATOM   2810 C CD2  . LEU A 1 544 ? 113.37400 98.52400  68.53100  1.000 26.45448  ? 544 LEU A CD2  1 
ATOM   2811 N N    . ILE A 1 545 ? 116.73100 102.92600 67.97100  1.000 20.37780  ? 545 ILE A N    1 
ATOM   2812 C CA   . ILE A 1 545 ? 118.11000 103.18600 67.56400  1.000 18.55549  ? 545 ILE A CA   1 
ATOM   2813 C C    . ILE A 1 545 ? 118.83700 104.02500 68.61300  1.000 21.71222  ? 545 ILE A C    1 
ATOM   2814 O O    . ILE A 1 545 ? 120.02800 103.81800 68.88000  1.000 25.74199  ? 545 ILE A O    1 
ATOM   2815 C CB   . ILE A 1 545 ? 118.13900 103.85400 66.17800  1.000 23.63718  ? 545 ILE A CB   1 
ATOM   2816 C CG1  . ILE A 1 545 ? 117.40900 102.98600 65.15200  1.000 24.60542  ? 545 ILE A CG1  1 
ATOM   2817 C CG2  . ILE A 1 545 ? 119.56800 104.10700 65.73200  1.000 19.08724  ? 545 ILE A CG2  1 
ATOM   2818 C CD1  . ILE A 1 545 ? 118.32200 102.10600 64.33600  1.000 25.65879  ? 545 ILE A CD1  1 
ATOM   2819 N N    . GLU A 1 546 ? 118.12900 104.96100 69.25100  1.000 27.50124  ? 546 GLU A N    1 
ATOM   2820 C CA   . GLU A 1 546 ? 118.75500 105.75100 70.30900  1.000 24.96052  ? 546 GLU A CA   1 
ATOM   2821 C C    . GLU A 1 546 ? 119.07700 104.88700 71.52700  1.000 23.99386  ? 546 GLU A C    1 
ATOM   2822 O O    . GLU A 1 546 ? 120.14700 105.03400 72.14800  1.000 27.72294  ? 546 GLU A O    1 
ATOM   2823 C CB   . GLU A 1 546 ? 117.84000 106.91500 70.69600  1.000 24.36001  ? 546 GLU A CB   1 
ATOM   2824 C CG   . GLU A 1 546 ? 118.44800 107.90500 71.67900  1.000 25.05990  ? 546 GLU A CG   1 
ATOM   2825 C CD   . GLU A 1 546 ? 119.68000 108.59700 71.12900  1.000 37.08332  ? 546 GLU A CD   1 
ATOM   2826 O OE1  . GLU A 1 546 ? 119.74700 108.81400 69.90100  1.000 30.92596  ? 546 GLU A OE1  1 
ATOM   2827 O OE2  . GLU A 1 546 ? 120.58100 108.93000 71.92600  1.000 40.21245  ? 546 GLU A OE2  1 
ATOM   2828 N N    . PHE A 1 547 ? 118.17900 103.95800 71.86600  1.000 18.14516  ? 547 PHE A N    1 
ATOM   2829 C CA   . PHE A 1 547 ? 118.48300 103.04500 72.96100  1.000 21.67859  ? 547 PHE A CA   1 
ATOM   2830 C C    . PHE A 1 547 ? 119.73100 102.23400 72.65300  1.000 25.91225  ? 547 PHE A C    1 
ATOM   2831 O O    . PHE A 1 547 ? 120.57800 102.02500 73.52900  1.000 22.88408  ? 547 PHE A O    1 
ATOM   2832 C CB   . PHE A 1 547 ? 117.30900 102.10700 73.23400  1.000 21.03608  ? 547 PHE A CB   1 
ATOM   2833 C CG   . PHE A 1 547 ? 117.66100 100.96400 74.14500  1.000 21.57900  ? 547 PHE A CG   1 
ATOM   2834 C CD1  . PHE A 1 547 ? 117.62500 101.11800 75.51900  1.000 20.99787  ? 547 PHE A CD1  1 
ATOM   2835 C CD2  . PHE A 1 547 ? 118.06100 99.74300  73.62600  1.000 19.76774  ? 547 PHE A CD2  1 
ATOM   2836 C CE1  . PHE A 1 547 ? 117.96100 100.07400 76.35700  1.000 20.83577  ? 547 PHE A CE1  1 
ATOM   2837 C CE2  . PHE A 1 547 ? 118.39900 98.69800  74.45900  1.000 21.34711  ? 547 PHE A CE2  1 
ATOM   2838 C CZ   . PHE A 1 547 ? 118.35000 98.86400  75.82600  1.000 20.07312  ? 547 PHE A CZ   1 
ATOM   2839 N N    . VAL A 1 548 ? 119.87300 101.78200 71.40500  1.000 25.24854  ? 548 VAL A N    1 
ATOM   2840 C CA   . VAL A 1 548 ? 121.06200 101.00400 71.07500  1.000 18.46611  ? 548 VAL A CA   1 
ATOM   2841 C C    . VAL A 1 548 ? 122.30900 101.87900 71.10700  1.000 19.06132  ? 548 VAL A C    1 
ATOM   2842 O O    . VAL A 1 548 ? 123.40700 101.39600 71.40400  1.000 25.28562  ? 548 VAL A O    1 
ATOM   2843 C CB   . VAL A 1 548 ? 120.90100 100.31500 69.70800  1.000 24.34013  ? 548 VAL A CB   1 
ATOM   2844 C CG1  . VAL A 1 548 ? 122.14900 99.52000  69.37200  1.000 17.04285  ? 548 VAL A CG1  1 
ATOM   2845 C CG2  . VAL A 1 548 ? 119.68100 99.41400  69.71000  1.000 24.58495  ? 548 VAL A CG2  1 
ATOM   2846 N N    . ALA A 1 549 ? 122.17100 103.17000 70.80700  1.000 29.46974  ? 549 ALA A N    1 
ATOM   2847 C CA   . ALA A 1 549 ? 123.32500 104.06200 70.83000  1.000 23.92561  ? 549 ALA A CA   1 
ATOM   2848 C C    . ALA A 1 549 ? 123.77800 104.44900 72.23600  1.000 27.99527  ? 549 ALA A C    1 
ATOM   2849 O O    . ALA A 1 549 ? 124.91800 104.89600 72.39400  1.000 31.77626  ? 549 ALA A O    1 
ATOM   2850 C CB   . ALA A 1 549 ? 123.02600 105.33200 70.03100  1.000 18.16435  ? 549 ALA A CB   1 
ATOM   2851 N N    . ARG A 1 550 ? 122.92900 104.29900 73.25400  1.000 27.74712  ? 550 ARG A N    1 
ATOM   2852 C CA   . ARG A 1 550 ? 123.30600 104.73700 74.60300  1.000 19.91203  ? 550 ARG A CA   1 
ATOM   2853 C C    . ARG A 1 550 ? 124.03700 103.69200 75.47100  1.000 25.31798  ? 550 ARG A C    1 
ATOM   2854 O O    . ARG A 1 550 ? 124.25000 103.95700 76.65800  1.000 25.06105  ? 550 ARG A O    1 
ATOM   2855 C CB   . ARG A 1 550 ? 122.07400 105.23100 75.36700  1.000 25.28438  ? 550 ARG A CB   1 
ATOM   2856 C CG   . ARG A 1 550 ? 121.46400 106.50900 74.83100  1.000 29.66351  ? 550 ARG A CG   1 
ATOM   2857 C CD   . ARG A 1 550 ? 120.21900 106.88500 75.61600  1.000 24.19744  ? 550 ARG A CD   1 
ATOM   2858 N NE   . ARG A 1 550 ? 119.67900 108.17300 75.19900  1.000 28.36107  ? 550 ARG A NE   1 
ATOM   2859 C CZ   . ARG A 1 550 ? 118.83600 108.90100 75.91700  1.000 26.98084  ? 550 ARG A CZ   1 
ATOM   2860 N NH1  . ARG A 1 550 ? 118.40400 108.49300 77.09900  1.000 25.31643  ? 550 ARG A NH1  1 
ATOM   2861 N NH2  . ARG A 1 550 ? 118.41800 110.06900 75.43900  1.000 20.61950  ? 550 ARG A NH2  1 
ATOM   2862 N N    . LEU A 1 551 ? 124.43100 102.53100 74.93800  1.000 29.49698  ? 551 LEU A N    1 
ATOM   2863 C CA   . LEU A 1 551 ? 125.00400 101.47100 75.77800  1.000 24.38449  ? 551 LEU A CA   1 
ATOM   2864 C C    . LEU A 1 551 ? 126.51200 101.58900 76.03000  1.000 31.37013  ? 551 LEU A C    1 
ATOM   2865 O O    . LEU A 1 551 ? 127.02500 100.98100 76.99100  1.000 36.47990  ? 551 LEU A O    1 
ATOM   2866 C CB   . LEU A 1 551 ? 124.71100 100.10500 75.15100  1.000 26.86285  ? 551 LEU A CB   1 
ATOM   2867 C CG   . LEU A 1 551 ? 123.23900 99.68400  75.10500  1.000 27.92630  ? 551 LEU A CG   1 
ATOM   2868 C CD1  . LEU A 1 551 ? 123.05600 98.45900  74.22100  1.000 27.06980  ? 551 LEU A CD1  1 
ATOM   2869 C CD2  . LEU A 1 551 ? 122.69400 99.42900  76.50100  1.000 19.93980  ? 551 LEU A CD2  1 
ATOM   2870 N N    . GLN A 1 552 ? 127.23300 102.35300 75.20600  1.000 32.04338  ? 552 GLN A N    1 
ATOM   2871 C CA   . GLN A 1 552 ? 128.67900 102.47000 75.37900  1.000 26.67927  ? 552 GLN A CA   1 
ATOM   2872 C C    . GLN A 1 552 ? 129.03300 103.09200 76.72500  1.000 30.37273  ? 552 GLN A C    1 
ATOM   2873 O O    . GLN A 1 552 ? 130.03700 102.72100 77.34700  1.000 35.96441  ? 552 GLN A O    1 
ATOM   2874 C CB   . GLN A 1 552 ? 129.27100 103.29000 74.23400  1.000 26.66104  ? 552 GLN A CB   1 
ATOM   2875 C CG   . GLN A 1 552 ? 130.78200 103.40300 74.26200  1.000 33.62431  ? 552 GLN A CG   1 
ATOM   2876 C CD   . GLN A 1 552 ? 131.46200 102.17900 73.68900  1.000 39.20557  ? 552 GLN A CD   1 
ATOM   2877 O OE1  . GLN A 1 552 ? 132.10800 101.41900 74.41000  1.000 42.32354  ? 552 GLN A OE1  1 
ATOM   2878 N NE2  . GLN A 1 552 ? 131.31800 101.97900 72.38600  1.000 36.06407  ? 552 GLN A NE2  1 
ATOM   2879 N N    . ASN A 1 553 ? 128.21600 104.03400 77.19600  1.000 27.73058  ? 553 ASN A N    1 
ATOM   2880 C CA   . ASN A 1 553 ? 128.50800 104.69100 78.46500  1.000 32.52191  ? 553 ASN A CA   1 
ATOM   2881 C C    . ASN A 1 553 ? 128.38900 103.71200 79.62500  1.000 35.57500  ? 553 ASN A C    1 
ATOM   2882 O O    . ASN A 1 553 ? 129.19100 103.75100 80.56900  1.000 40.56086  ? 553 ASN A O    1 
ATOM   2883 C CB   . ASN A 1 553 ? 127.56700 105.87900 78.65800  1.000 37.12474  ? 553 ASN A CB   1 
ATOM   2884 C CG   . ASN A 1 553 ? 128.16100 106.95700 79.53700  1.000 45.55565  ? 553 ASN A CG   1 
ATOM   2885 O OD1  . ASN A 1 553 ? 127.70300 107.18200 80.65700  1.000 41.63614  ? 553 ASN A OD1  1 
ATOM   2886 N ND2  . ASN A 1 553 ? 129.18500 107.63400 79.03300  1.000 42.39189  ? 553 ASN A ND2  1 
ATOM   2887 N N    . VAL A 1 554 ? 127.41800 102.80100 79.55400  1.000 24.53515  ? 554 VAL A N    1 
ATOM   2888 C CA   . VAL A 1 554 ? 127.25700 101.80800 80.60900  1.000 28.06943  ? 554 VAL A CA   1 
ATOM   2889 C C    . VAL A 1 554 ? 128.41500 100.82200 80.58600  1.000 28.11530  ? 554 VAL A C    1 
ATOM   2890 O O    . VAL A 1 554 ? 128.91400 100.40100 81.64000  1.000 31.27372  ? 554 VAL A O    1 
ATOM   2891 C CB   . VAL A 1 554 ? 125.90100 101.09300 80.46200  1.000 28.55546  ? 554 VAL A CB   1 
ATOM   2892 C CG1  . VAL A 1 554 ? 125.76900 99.97800  81.48700  1.000 31.43739  ? 554 VAL A CG1  1 
ATOM   2893 C CG2  . VAL A 1 554 ? 124.75900 102.08300 80.58600  1.000 26.09923  ? 554 VAL A CG2  1 
ATOM   2894 N N    . VAL A 1 555 ? 128.89600 100.47200 79.39100  1.000 31.61652  ? 555 VAL A N    1 
ATOM   2895 C CA   . VAL A 1 555 ? 130.03700 99.55900  79.33100  1.000 27.03432  ? 555 VAL A CA   1 
ATOM   2896 C C    . VAL A 1 555 ? 131.29700 100.22700 79.88400  1.000 32.04160  ? 555 VAL A C    1 
ATOM   2897 O O    . VAL A 1 555 ? 132.10700 99.59000  80.57700  1.000 36.42586  ? 555 VAL A O    1 
ATOM   2898 C CB   . VAL A 1 555 ? 130.24400 99.05600  77.89100  1.000 30.68689  ? 555 VAL A CB   1 
ATOM   2899 C CG1  . VAL A 1 555 ? 131.57800 98.33700  77.76600  1.000 31.16629  ? 555 VAL A CG1  1 
ATOM   2900 C CG2  . VAL A 1 555 ? 129.10200 98.13900  77.48500  1.000 29.07968  ? 555 VAL A CG2  1 
ATOM   2901 N N    . ASP A 1 556 ? 131.45600 101.53100 79.64400  1.000 34.26758  ? 556 ASP A N    1 
ATOM   2902 C CA   . ASP A 1 556 ? 132.62200 102.23000 80.18300  1.000 31.32508  ? 556 ASP A CA   1 
ATOM   2903 C C    . ASP A 1 556 ? 132.54300 102.36400 81.70000  1.000 32.93317  ? 556 ASP A C    1 
ATOM   2904 O O    . ASP A 1 556 ? 133.55700 102.21700 82.39800  1.000 40.00541  ? 556 ASP A O    1 
ATOM   2905 C CB   . ASP A 1 556 ? 132.75800 103.60400 79.53100  1.000 30.89075  ? 556 ASP A CB   1 
ATOM   2906 C CG   . ASP A 1 556 ? 132.97500 103.52000 78.03700  1.000 40.09726  ? 556 ASP A CG   1 
ATOM   2907 O OD1  . ASP A 1 556 ? 133.83100 102.72200 77.60200  1.000 43.37732  ? 556 ASP A OD1  1 
ATOM   2908 O OD2  . ASP A 1 556 ? 132.29100 104.25400 77.29500  1.000 45.07517  ? 556 ASP A OD2  1 
ATOM   2909 N N    . ALA A 1 557 ? 131.34700 102.62300 82.23400  1.000 28.83285  ? 557 ALA A N    1 
ATOM   2910 C CA   . ALA A 1 557 ? 131.20500 102.68600 83.68500  1.000 29.70930  ? 557 ALA A CA   1 
ATOM   2911 C C    . ALA A 1 557 ? 131.49200 101.33100 84.32000  1.000 29.39996  ? 557 ALA A C    1 
ATOM   2912 O O    . ALA A 1 557 ? 132.11300 101.25400 85.39000  1.000 27.61526  ? 557 ALA A O    1 
ATOM   2913 C CB   . ALA A 1 557 ? 129.80700 103.17400 84.06000  1.000 21.61479  ? 557 ALA A CB   1 
ATOM   2914 N N    . PHE A 1 558 ? 131.06700 100.24600 83.66600  1.000 32.49302  ? 558 PHE A N    1 
ATOM   2915 C CA   . PHE A 1 558 ? 131.38200 98.92600  84.19700  1.000 28.83233  ? 558 PHE A CA   1 
ATOM   2916 C C    . PHE A 1 558 ? 132.88400 98.68100  84.21000  1.000 29.40757  ? 558 PHE A C    1 
ATOM   2917 O O    . PHE A 1 558 ? 133.41700 98.12300  85.17500  1.000 32.97377  ? 558 PHE A O    1 
ATOM   2918 C CB   . PHE A 1 558 ? 130.67800 97.82800  83.40300  1.000 23.48104  ? 558 PHE A CB   1 
ATOM   2919 C CG   . PHE A 1 558 ? 131.01100 96.44300  83.88400  1.000 34.43356  ? 558 PHE A CG   1 
ATOM   2920 C CD1  . PHE A 1 558 ? 130.26300 95.84500  84.88200  1.000 32.43121  ? 558 PHE A CD1  1 
ATOM   2921 C CD2  . PHE A 1 558 ? 132.08800 95.75000  83.35600  1.000 33.34905  ? 558 PHE A CD2  1 
ATOM   2922 C CE1  . PHE A 1 558 ? 130.57400 94.58000  85.33500  1.000 31.84020  ? 558 PHE A CE1  1 
ATOM   2923 C CE2  . PHE A 1 558 ? 132.40300 94.48600  83.80700  1.000 31.17900  ? 558 PHE A CE2  1 
ATOM   2924 C CZ   . PHE A 1 558 ? 131.64400 93.90000  84.79700  1.000 31.60789  ? 558 PHE A CZ   1 
ATOM   2925 N N    . LYS A 1 559 ? 133.58500 99.06400  83.13900  1.000 32.66766  ? 559 LYS A N    1 
ATOM   2926 C CA   . LYS A 1 559 ? 135.03200 98.85900  83.13100  1.000 29.41790  ? 559 LYS A CA   1 
ATOM   2927 C C    . LYS A 1 559 ? 135.71400 99.67200  84.22700  1.000 35.30528  ? 559 LYS A C    1 
ATOM   2928 O O    . LYS A 1 559 ? 136.64600 99.18900  84.88800  1.000 40.20152  ? 559 LYS A O    1 
ATOM   2929 C CB   . LYS A 1 559 ? 135.61100 99.21200  81.76300  1.000 31.07039  ? 559 LYS A CB   1 
ATOM   2930 C CG   . LYS A 1 559 ? 135.52800 98.08600  80.75200  1.000 35.24045  ? 559 LYS A CG   1 
ATOM   2931 C CD   . LYS A 1 559 ? 135.52300 98.61500  79.33200  1.000 36.65960  ? 559 LYS A CD   1 
ATOM   2932 C CE   . LYS A 1 559 ? 136.42500 97.78200  78.43800  1.000 41.03659  ? 559 LYS A CE   1 
ATOM   2933 N NZ   . LYS A 1 559 ? 135.74300 96.54700  77.96600  1.000 41.99095  ? 559 LYS A NZ   1 
ATOM   2934 N N    . GLU A 1 560 ? 135.22700 100.89000 84.47800  1.000 38.49560  ? 560 GLU A N    1 
ATOM   2935 C CA   . GLU A 1 560 ? 135.82100 101.69800 85.54000  1.000 34.41114  ? 560 GLU A CA   1 
ATOM   2936 C C    . GLU A 1 560 ? 135.61400 101.05200 86.90500  1.000 36.71498  ? 560 GLU A C    1 
ATOM   2937 O O    . GLU A 1 560 ? 136.54800 100.97700 87.71700  1.000 38.54469  ? 560 GLU A O    1 
ATOM   2938 C CB   . GLU A 1 560 ? 135.23300 103.10700 85.52500  1.000 34.88599  ? 560 GLU A CB   1 
ATOM   2939 C CG   . GLU A 1 560 ? 136.22100 104.19000 85.14000  1.000 41.75975  ? 560 GLU A CG   1 
ATOM   2940 C CD   . GLU A 1 560 ? 135.54000 105.49600 84.78800  1.000 46.86815  ? 560 GLU A CD   1 
ATOM   2941 O OE1  . GLU A 1 560 ? 134.30300 105.58300 84.93900  1.000 41.78300  ? 560 GLU A OE1  1 
ATOM   2942 O OE2  . GLU A 1 560 ? 136.24000 106.43700 84.35800  1.000 45.21052  ? 560 GLU A OE2  1 
ATOM   2943 N N    . LEU A 1 561 ? 134.40000 100.56300 87.17100  1.000 33.58015  ? 561 LEU A N    1 
ATOM   2944 C CA   . LEU A 1 561 ? 134.15700 99.89000  88.44300  1.000 28.20182  ? 561 LEU A CA   1 
ATOM   2945 C C    . LEU A 1 561 ? 135.00500 98.63000  88.57300  1.000 36.57372  ? 561 LEU A C    1 
ATOM   2946 O O    . LEU A 1 561 ? 135.58200 98.36900  89.63400  1.000 35.40849  ? 561 LEU A O    1 
ATOM   2947 C CB   . LEU A 1 561 ? 132.67500 99.55500  88.59600  1.000 30.79861  ? 561 LEU A CB   1 
ATOM   2948 C CG   . LEU A 1 561 ? 132.33700 98.66400  89.79300  1.000 24.81466  ? 561 LEU A CG   1 
ATOM   2949 C CD1  . LEU A 1 561 ? 132.63800 99.38400  91.09400  1.000 31.02829  ? 561 LEU A CD1  1 
ATOM   2950 C CD2  . LEU A 1 561 ? 130.88500 98.22100  89.75000  1.000 23.84218  ? 561 LEU A CD2  1 
ATOM   2951 N N    . SER A 1 562 ? 135.09800 97.83700  87.50300  1.000 36.25333  ? 562 SER A N    1 
ATOM   2952 C CA   . SER A 1 562 ? 135.87800 96.60800  87.56500  1.000 30.98752  ? 562 SER A CA   1 
ATOM   2953 C C    . SER A 1 562 ? 137.36000 96.88300  87.75500  1.000 37.40056  ? 562 SER A C    1 
ATOM   2954 O O    . SER A 1 562 ? 138.08400 96.00300  88.23100  1.000 39.41379  ? 562 SER A O    1 
ATOM   2955 C CB   . SER A 1 562 ? 135.66600 95.77400  86.30200  1.000 31.60488  ? 562 SER A CB   1 
ATOM   2956 O OG   . SER A 1 562 ? 136.37600 96.32000  85.20700  1.000 42.53586  ? 562 SER A OG   1 
ATOM   2957 N N    . GLN A 1 563 ? 137.82800 98.08000  87.40300  1.000 46.55548  ? 563 GLN A N    1 
ATOM   2958 C CA   . GLN A 1 563 ? 139.23900 98.37500  87.62300  1.000 40.54710  ? 563 GLN A CA   1 
ATOM   2959 C C    . GLN A 1 563 ? 139.50300 98.95200  89.00800  1.000 42.63626  ? 563 GLN A C    1 
ATOM   2960 O O    . GLN A 1 563 ? 140.51700 98.61700  89.62900  1.000 43.53151  ? 563 GLN A O    1 
ATOM   2961 C CB   . GLN A 1 563 ? 139.75700 99.34400  86.55900  1.000 43.66147  ? 563 GLN A CB   1 
ATOM   2962 C CG   . GLN A 1 563 ? 140.43700 98.67300  85.37800  1.000 46.56455  ? 563 GLN A CG   1 
ATOM   2963 C CD   . GLN A 1 563 ? 140.48600 99.56500  84.15300  1.000 50.50684  ? 563 GLN A CD   1 
ATOM   2964 O OE1  . GLN A 1 563 ? 140.58500 100.78600 84.26600  1.000 52.92903  ? 563 GLN A OE1  1 
ATOM   2965 N NE2  . GLN A 1 563 ? 140.42000 98.95700  82.97500  1.000 47.23914  ? 563 GLN A NE2  1 
ATOM   2966 N N    . LYS A 1 564 ? 138.61500 99.81200  89.51600  1.000 49.25461  ? 564 LYS A N    1 
ATOM   2967 C CA   . LYS A 1 564 ? 138.84600 100.38800 90.83900  1.000 41.89228  ? 564 LYS A CA   1 
ATOM   2968 C C    . LYS A 1 564 ? 138.58800 99.41200  91.98300  1.000 44.18422  ? 564 LYS A C    1 
ATOM   2969 O O    . LYS A 1 564 ? 139.12600 99.61400  93.07600  1.000 44.54950  ? 564 LYS A O    1 
ATOM   2970 C CB   . LYS A 1 564 ? 137.99100 101.64000 91.03400  1.000 39.91102  ? 564 LYS A CB   1 
ATOM   2971 C CG   . LYS A 1 564 ? 138.22300 102.71200 89.98900  1.000 42.53737  ? 564 LYS A CG   1 
ATOM   2972 C CD   . LYS A 1 564 ? 137.85000 104.08100 90.52700  1.000 44.68295  ? 564 LYS A CD   1 
ATOM   2973 C CE   . LYS A 1 564 ? 139.05700 105.00400 90.55600  1.000 47.32977  ? 564 LYS A CE   1 
ATOM   2974 N NZ   . LYS A 1 564 ? 139.82500 104.95200 89.28300  1.000 45.03908  ? 564 LYS A NZ   1 
ATOM   2975 N N    . ALA A 1 565 ? 137.78900 98.36700  91.77100  1.000 45.87175  ? 565 ALA A N    1 
ATOM   2976 C CA   . ALA A 1 565 ? 137.40900 97.45900  92.84700  1.000 35.42862  ? 565 ALA A CA   1 
ATOM   2977 C C    . ALA A 1 565 ? 138.14800 96.12700  92.80300  1.000 39.11070  ? 565 ALA A C    1 
ATOM   2978 O O    . ALA A 1 565 ? 137.82600 95.22800  93.58500  1.000 43.39239  ? 565 ALA A O    1 
ATOM   2979 C CB   . ALA A 1 565 ? 135.90000 97.21600  92.82200  1.000 37.93712  ? 565 ALA A CB   1 
ATOM   2980 N N    . ASN A 1 566 ? 139.13300 95.98200  91.91900  1.000 45.54012  ? 566 ASN A N    1 
ATOM   2981 C CA   . ASN A 1 566 ? 139.95000 94.77100  91.83000  1.000 38.76538  ? 566 ASN A CA   1 
ATOM   2982 C C    . ASN A 1 566 ? 139.08900 93.52200  91.62800  1.000 43.85668  ? 566 ASN A C    1 
ATOM   2983 O O    . ASN A 1 566 ? 139.13200 92.56800  92.40700  1.000 47.73645  ? 566 ASN A O    1 
ATOM   2984 C CB   . ASN A 1 566 ? 140.84100 94.62600  93.06700  1.000 41.38169  ? 566 ASN A CB   1 
ATOM   2985 C CG   . ASN A 1 566 ? 142.27300 95.03700  92.80300  1.000 49.32768  ? 566 ASN A CG   1 
ATOM   2986 O OD1  . ASN A 1 566 ? 143.16000 94.19300  92.68000  1.000 50.52324  ? 566 ASN A OD1  1 
ATOM   2987 N ND2  . ASN A 1 566 ? 142.50800 96.34100  92.71800  1.000 47.07209  ? 566 ASN A ND2  1 
ATOM   2988 N N    . PHE A 1 567 ? 138.29900 93.54200  90.55800  1.000 39.07965  ? 567 PHE A N    1 
ATOM   2989 C CA   . PHE A 1 567 ? 137.58600 92.34400  90.14500  1.000 35.21653  ? 567 PHE A CA   1 
ATOM   2990 C C    . PHE A 1 567 ? 138.57700 91.31000  89.61100  1.000 41.00334  ? 567 PHE A C    1 
ATOM   2991 O O    . PHE A 1 567 ? 139.72500 91.62300  89.28500  1.000 45.24941  ? 567 PHE A O    1 
ATOM   2992 C CB   . PHE A 1 567 ? 136.53300 92.68200  89.09100  1.000 36.00141  ? 567 PHE A CB   1 
ATOM   2993 C CG   . PHE A 1 567 ? 135.28400 93.30100  89.65700  1.000 37.37957  ? 567 PHE A CG   1 
ATOM   2994 C CD1  . PHE A 1 567 ? 135.24400 93.73900  90.96900  1.000 35.64578  ? 567 PHE A CD1  1 
ATOM   2995 C CD2  . PHE A 1 567 ? 134.15200 93.44900  88.87400  1.000 37.97145  ? 567 PHE A CD2  1 
ATOM   2996 C CE1  . PHE A 1 567 ? 134.09900 94.30800  91.48900  1.000 34.59107  ? 567 PHE A CE1  1 
ATOM   2997 C CE2  . PHE A 1 567 ? 133.00400 94.01600  89.39000  1.000 37.19865  ? 567 PHE A CE2  1 
ATOM   2998 C CZ   . PHE A 1 567 ? 132.97800 94.44600  90.69900  1.000 33.03610  ? 567 PHE A CZ   1 
ATOM   2999 N N    . LYS A 1 568 ? 138.12300 90.06500  89.51700  1.000 47.94560  ? 568 LYS A N    1 
ATOM   3000 C CA   . LYS A 1 568 ? 139.00000 88.95600  89.17300  1.000 48.46431  ? 568 LYS A CA   1 
ATOM   3001 C C    . LYS A 1 568 ? 138.91800 88.61900  87.68800  1.000 51.16375  ? 568 LYS A C    1 
ATOM   3002 O O    . LYS A 1 568 ? 137.93800 88.92200  87.00500  1.000 55.79796  ? 568 LYS A O    1 
ATOM   3003 C CB   . LYS A 1 568 ? 138.65500 87.71900  90.00500  1.000 48.79536  ? 568 LYS A CB   1 
ATOM   3004 C CG   . LYS A 1 568 ? 137.64900 86.79000  89.35000  1.000 52.33862  ? 568 LYS A CG   1 
ATOM   3005 C CD   . LYS A 1 568 ? 137.10900 85.77500  90.34300  1.000 51.36070  ? 568 LYS A CD   1 
ATOM   3006 C CE   . LYS A 1 568 ? 135.79800 85.17300  89.86200  1.000 53.97062  ? 568 LYS A CE   1 
ATOM   3007 N NZ   . LYS A 1 568 ? 136.00900 84.12800  88.82200  1.000 54.53666  ? 568 LYS A NZ   1 
ATOM   3008 N N    . GLU A 1 569 ? 139.97500 87.97800  87.19900  1.000 59.78723  ? 569 GLU A N    1 
ATOM   3009 C CA   . GLU A 1 569 ? 140.03300 87.58100  85.80100  1.000 60.80351  ? 569 GLU A CA   1 
ATOM   3010 C C    . GLU A 1 569 ? 138.88600 86.62400  85.48200  1.000 64.90717  ? 569 GLU A C    1 
ATOM   3011 O O    . GLU A 1 569 ? 138.56800 85.74200  86.28900  1.000 62.81691  ? 569 GLU A O    1 
ATOM   3012 C CB   . GLU A 1 569 ? 141.38000 86.92800  85.48900  1.000 61.54156  ? 569 GLU A CB   1 
ATOM   3013 C CG   . GLU A 1 569 ? 141.82300 87.05700  84.03900  1.000 64.67887  ? 569 GLU A CG   1 
ATOM   3014 C CD   . GLU A 1 569 ? 141.50700 85.82600  83.21300  1.000 69.24032  ? 569 GLU A CD   1 
ATOM   3015 O OE1  . GLU A 1 569 ? 141.86700 84.71300  83.64700  1.000 67.40058  ? 569 GLU A OE1  1 
ATOM   3016 O OE2  . GLU A 1 569 ? 140.90600 85.97100  82.12800  1.000 66.15643  ? 569 GLU A OE2  1 
ATOM   3017 N N    . PRO A 1 570 ? 138.24900 86.76000  84.31800  1.000 63.00213  ? 570 PRO A N    1 
ATOM   3018 C CA   . PRO A 1 570 ? 137.07600 85.93400  84.01600  1.000 60.54581  ? 570 PRO A CA   1 
ATOM   3019 C C    . PRO A 1 570 ? 137.41900 84.54100  83.51300  1.000 61.91022  ? 570 PRO A C    1 
ATOM   3020 O O    . PRO A 1 570 ? 136.57200 83.87700  82.90900  1.000 63.12836  ? 570 PRO A O    1 
ATOM   3021 C CB   . PRO A 1 570 ? 136.35400 86.75700  82.94500  1.000 57.92453  ? 570 PRO A CB   1 
ATOM   3022 C CG   . PRO A 1 570 ? 137.46100 87.52200  82.24500  1.000 59.80016  ? 570 PRO A CG   1 
ATOM   3023 C CD   . PRO A 1 570 ? 138.69100 87.51500  83.13500  1.000 59.04566  ? 570 PRO A CD   1 
ATOM   3024 N N    . GLU A 1 571 ? 138.65500 84.10200  83.74100  1.000 65.24997  ? 571 GLU A N    1 
ATOM   3025 C CA   . GLU A 1 571 ? 139.13700 82.79700  83.28100  1.000 67.38168  ? 571 GLU A CA   1 
ATOM   3026 C C    . GLU A 1 571 ? 138.06200 81.71300  83.32100  1.000 67.44071  ? 571 GLU A C    1 
ATOM   3027 O O    . GLU A 1 571 ? 137.25500 81.65800  84.24900  1.000 67.33611  ? 571 GLU A O    1 
ATOM   3028 C CB   . GLU A 1 571 ? 140.33800 82.35300  84.11900  1.000 67.59558  ? 571 GLU A CB   1 
ATOM   3029 N N    . ALA B 1 77  ? 118.86300 132.36300 106.76100 1.000 84.41282  ? 77  ALA B N    1 
ATOM   3030 C CA   . ALA B 1 77  ? 118.31700 132.94100 107.98300 1.000 84.79513  ? 77  ALA B CA   1 
ATOM   3031 C C    . ALA B 1 77  ? 117.37400 134.09500 107.66600 1.000 83.79341  ? 77  ALA B C    1 
ATOM   3032 O O    . ALA B 1 77  ? 116.19500 133.88300 107.38500 1.000 82.16746  ? 77  ALA B O    1 
ATOM   3033 C CB   . ALA B 1 77  ? 119.43900 133.40900 108.89600 1.000 83.76935  ? 77  ALA B CB   1 
ATOM   3034 N N    . TRP B 1 78  ? 117.90300 135.31900 107.72700 1.000 88.56173  ? 78  TRP B N    1 
ATOM   3035 C CA   . TRP B 1 78  ? 117.08400 136.49400 107.44700 1.000 89.00351  ? 78  TRP B CA   1 
ATOM   3036 C C    . TRP B 1 78  ? 116.45200 136.41400 106.06300 1.000 88.79319  ? 78  TRP B C    1 
ATOM   3037 O O    . TRP B 1 78  ? 115.31500 136.85900 105.86400 1.000 87.21619  ? 78  TRP B O    1 
ATOM   3038 C CB   . TRP B 1 78  ? 117.92700 137.76200 107.58300 1.000 87.68074  ? 78  TRP B CB   1 
ATOM   3039 C CG   . TRP B 1 78  ? 117.12300 139.02500 107.56100 1.000 88.42256  ? 78  TRP B CG   1 
ATOM   3040 C CD1  . TRP B 1 78  ? 116.79500 139.76900 106.46600 1.000 87.45250  ? 78  TRP B CD1  1 
ATOM   3041 C CD2  . TRP B 1 78  ? 116.54300 139.69300 108.68800 1.000 89.53835  ? 78  TRP B CD2  1 
ATOM   3042 N NE1  . TRP B 1 78  ? 116.04800 140.85900 106.84000 1.000 88.12307  ? 78  TRP B NE1  1 
ATOM   3043 C CE2  . TRP B 1 78  ? 115.87900 140.83500 108.20000 1.000 89.90145  ? 78  TRP B CE2  1 
ATOM   3044 C CE3  . TRP B 1 78  ? 116.52100 139.43600 110.06200 1.000 88.38692  ? 78  TRP B CE3  1 
ATOM   3045 C CZ2  . TRP B 1 78  ? 115.20100 141.71900 109.03700 1.000 88.97305  ? 78  TRP B CZ2  1 
ATOM   3046 C CZ3  . TRP B 1 78  ? 115.84800 140.31400 110.89100 1.000 88.73774  ? 78  TRP B CZ3  1 
ATOM   3047 C CH2  . TRP B 1 78  ? 115.19700 141.44100 110.37600 1.000 88.65622  ? 78  TRP B CH2  1 
ATOM   3048 N N    . GLU B 1 79  ? 117.17400 135.85400 105.09100 1.000 83.32281  ? 79  GLU B N    1 
ATOM   3049 C CA   . GLU B 1 79  ? 116.62900 135.73300 103.74200 1.000 81.78751  ? 79  GLU B CA   1 
ATOM   3050 C C    . GLU B 1 79  ? 115.37000 134.87500 103.73700 1.000 83.66696  ? 79  GLU B C    1 
ATOM   3051 O O    . GLU B 1 79  ? 114.33800 135.26600 103.17900 1.000 82.63990  ? 79  GLU B O    1 
ATOM   3052 C CB   . GLU B 1 79  ? 117.68400 135.15100 102.80100 1.000 80.35419  ? 79  GLU B CB   1 
ATOM   3053 N N    . MET B 1 80  ? 115.43600 133.69700 104.36300 1.000 81.14865  ? 80  MET B N    1 
ATOM   3054 C CA   . MET B 1 80  ? 114.26800 132.82500 104.41600 1.000 78.09694  ? 80  MET B CA   1 
ATOM   3055 C C    . MET B 1 80  ? 113.15600 133.43300 105.25800 1.000 76.90883  ? 80  MET B C    1 
ATOM   3056 O O    . MET B 1 80  ? 111.97400 133.24300 104.95100 1.000 76.18027  ? 80  MET B O    1 
ATOM   3057 C CB   . MET B 1 80  ? 114.66000 131.45200 104.96100 1.000 77.48774  ? 80  MET B CB   1 
ATOM   3058 C CG   . MET B 1 80  ? 113.64500 130.35900 104.67200 1.000 78.96268  ? 80  MET B CG   1 
ATOM   3059 S SD   . MET B 1 80  ? 114.02000 128.81400 105.52200 1.000 82.37117  ? 80  MET B SD   1 
ATOM   3060 C CE   . MET B 1 80  ? 114.15100 129.38000 107.21400 1.000 77.15157  ? 80  MET B CE   1 
ATOM   3061 N N    . GLY B 1 81  ? 113.51000 134.15800 106.31900 1.000 74.75845  ? 81  GLY B N    1 
ATOM   3062 C CA   . GLY B 1 81  ? 112.49000 134.80800 107.12500 1.000 74.79185  ? 81  GLY B CA   1 
ATOM   3063 C C    . GLY B 1 81  ? 111.72300 135.86200 106.35100 1.000 75.20173  ? 81  GLY B C    1 
ATOM   3064 O O    . GLY B 1 81  ? 110.50000 135.96200 106.46300 1.000 73.88579  ? 81  GLY B O    1 
ATOM   3065 N N    . VAL B 1 82  ? 112.43200 136.66500 105.55500 1.000 79.00452  ? 82  VAL B N    1 
ATOM   3066 C CA   . VAL B 1 82  ? 111.76700 137.69200 104.76000 1.000 77.85864  ? 82  VAL B CA   1 
ATOM   3067 C C    . VAL B 1 82  ? 110.97600 137.06000 103.62200 1.000 76.82284  ? 82  VAL B C    1 
ATOM   3068 O O    . VAL B 1 82  ? 109.87300 137.51000 103.29200 1.000 75.52775  ? 82  VAL B O    1 
ATOM   3069 C CB   . VAL B 1 82  ? 112.79100 138.71900 104.24200 1.000 77.45001  ? 82  VAL B CB   1 
ATOM   3070 C CG1  . VAL B 1 82  ? 113.67100 139.21100 105.38000 1.000 77.64377  ? 82  VAL B CG1  1 
ATOM   3071 C CG2  . VAL B 1 82  ? 113.63400 138.12100 103.12800 1.000 75.78542  ? 82  VAL B CG2  1 
ATOM   3072 N N    . SER B 1 83  ? 111.52500 136.01300 103.00100 1.000 76.56360  ? 83  SER B N    1 
ATOM   3073 C CA   . SER B 1 83  ? 110.81800 135.35400 101.90700 1.000 75.46976  ? 83  SER B CA   1 
ATOM   3074 C C    . SER B 1 83  ? 109.49400 134.76600 102.37600 1.000 78.34749  ? 83  SER B C    1 
ATOM   3075 O O    . SER B 1 83  ? 108.47300 134.89100 101.68900 1.000 77.57414  ? 83  SER B O    1 
ATOM   3076 C CB   . SER B 1 83  ? 111.69900 134.26700 101.29200 1.000 74.13588  ? 83  SER B CB   1 
ATOM   3077 O OG   . SER B 1 83  ? 112.95600 134.79200 100.90100 1.000 76.71105  ? 83  SER B OG   1 
ATOM   3078 N N    . ASP B 1 84  ? 109.48800 134.12200 103.54300 1.000 70.17901  ? 84  ASP B N    1 
ATOM   3079 C CA   . ASP B 1 84  ? 108.28700 133.47400 104.05200 1.000 63.28479  ? 84  ASP B CA   1 
ATOM   3080 C C    . ASP B 1 84  ? 108.11400 133.76700 105.53700 1.000 64.17562  ? 84  ASP B C    1 
ATOM   3081 O O    . ASP B 1 84  ? 108.89000 133.27200 106.36400 1.000 64.27456  ? 84  ASP B O    1 
ATOM   3082 C CB   . ASP B 1 84  ? 108.35100 131.96500 103.81300 1.000 62.27082  ? 84  ASP B CB   1 
ATOM   3083 C CG   . ASP B 1 84  ? 107.00000 131.36900 103.47500 1.000 67.49980  ? 84  ASP B CG   1 
ATOM   3084 O OD1  . ASP B 1 84  ? 106.01500 132.13200 103.39100 1.000 66.96334  ? 84  ASP B OD1  1 
ATOM   3085 O OD2  . ASP B 1 84  ? 106.92300 130.13600 103.29300 1.000 66.74786  ? 84  ASP B OD2  1 
ATOM   3086 N N    . PRO B 1 85  ? 107.11400 134.56700 105.91600 1.000 55.92161  ? 85  PRO B N    1 
ATOM   3087 C CA   . PRO B 1 85  ? 106.84000 134.80200 107.33900 1.000 52.40482  ? 85  PRO B CA   1 
ATOM   3088 C C    . PRO B 1 85  ? 105.98400 133.73400 108.00300 1.000 48.33947  ? 85  PRO B C    1 
ATOM   3089 O O    . PRO B 1 85  ? 105.69800 133.85800 109.19900 1.000 52.63495  ? 85  PRO B O    1 
ATOM   3090 C CB   . PRO B 1 85  ? 106.11000 136.15200 107.32500 1.000 49.80994  ? 85  PRO B CB   1 
ATOM   3091 C CG   . PRO B 1 85  ? 105.44700 136.20300 105.99500 1.000 48.62502  ? 85  PRO B CG   1 
ATOM   3092 C CD   . PRO B 1 85  ? 106.32600 135.44900 105.03800 1.000 48.55809  ? 85  PRO B CD   1 
ATOM   3093 N N    . ARG B 1 86  ? 105.56200 132.69900 107.27500 1.000 34.97618  ? 86  ARG B N    1 
ATOM   3094 C CA   . ARG B 1 86  ? 104.75600 131.64400 107.88200 1.000 41.25792  ? 86  ARG B CA   1 
ATOM   3095 C C    . ARG B 1 86  ? 105.56600 130.80200 108.86500 1.000 43.42607  ? 86  ARG B C    1 
ATOM   3096 O O    . ARG B 1 86  ? 105.02000 130.30900 109.86400 1.000 43.85652  ? 86  ARG B O    1 
ATOM   3097 C CB   . ARG B 1 86  ? 104.16200 130.76900 106.77700 1.000 41.54821  ? 86  ARG B CB   1 
ATOM   3098 C CG   . ARG B 1 86  ? 102.91000 131.35900 106.14700 1.000 42.43614  ? 86  ARG B CG   1 
ATOM   3099 C CD   . ARG B 1 86  ? 102.09000 130.32600 105.39100 1.000 41.97862  ? 86  ARG B CD   1 
ATOM   3100 N NE   . ARG B 1 86  ? 102.92500 129.31400 104.75500 1.000 44.91053  ? 86  ARG B NE   1 
ATOM   3101 C CZ   . ARG B 1 86  ? 102.45800 128.29000 104.05400 1.000 39.81034  ? 86  ARG B CZ   1 
ATOM   3102 N NH1  . ARG B 1 86  ? 101.16000 128.11200 103.87200 1.000 37.16540  ? 86  ARG B NH1  1 
ATOM   3103 N NH2  . ARG B 1 86  ? 103.31400 127.42500 103.51900 1.000 37.97783  ? 86  ARG B NH2  1 
ATOM   3104 N N    . LYS B 1 87  ? 106.87800 130.69900 108.65300 1.000 38.97977  ? 87  LYS B N    1 
ATOM   3105 C CA   . LYS B 1 87  ? 107.69800 129.85400 109.50800 1.000 34.88520  ? 87  LYS B CA   1 
ATOM   3106 C C    . LYS B 1 87  ? 108.11900 130.56700 110.78300 1.000 33.60226  ? 87  LYS B C    1 
ATOM   3107 O O    . LYS B 1 87  ? 108.37900 129.90300 111.79300 1.000 40.50847  ? 87  LYS B O    1 
ATOM   3108 C CB   . LYS B 1 87  ? 108.92900 129.39000 108.73100 1.000 34.11097  ? 87  LYS B CB   1 
ATOM   3109 C CG   . LYS B 1 87  ? 108.69000 129.33500 107.23100 1.000 37.86172  ? 87  LYS B CG   1 
ATOM   3110 C CD   . LYS B 1 87  ? 109.95900 129.05100 106.45000 1.000 41.16900  ? 87  LYS B CD   1 
ATOM   3111 C CE   . LYS B 1 87  ? 110.44400 127.63300 106.66600 1.000 41.59611  ? 87  LYS B CE   1 
ATOM   3112 N NZ   . LYS B 1 87  ? 110.84000 126.99700 105.38100 1.000 37.53176  ? 87  LYS B NZ   1 
ATOM   3113 N N    . ILE B 1 88  ? 108.03500 131.89600 110.80700 1.000 27.13431  ? 88  ILE B N    1 
ATOM   3114 C CA   . ILE B 1 88  ? 108.34300 132.61500 112.03200 1.000 30.45519  ? 88  ILE B CA   1 
ATOM   3115 C C    . ILE B 1 88  ? 107.14000 132.57100 112.95600 1.000 31.33969  ? 88  ILE B C    1 
ATOM   3116 O O    . ILE B 1 88  ? 107.28800 132.42000 114.17700 1.000 37.88431  ? 88  ILE B O    1 
ATOM   3117 C CB   . ILE B 1 88  ? 108.75300 134.06200 111.71000 1.000 29.70167  ? 88  ILE B CB   1 
ATOM   3118 C CG1  . ILE B 1 88  ? 109.92500 134.08100 110.73000 1.000 30.81735  ? 88  ILE B CG1  1 
ATOM   3119 C CG2  . ILE B 1 88  ? 109.10800 134.81800 112.97900 1.000 31.63177  ? 88  ILE B CG2  1 
ATOM   3120 C CD1  . ILE B 1 88  ? 110.61000 135.41700 110.64200 1.000 31.95664  ? 88  ILE B CD1  1 
ATOM   3121 N N    . VAL B 1 89  ? 105.93600 132.60200 112.38600 1.000 19.59945  ? 89  VAL B N    1 
ATOM   3122 C CA   . VAL B 1 89  ? 104.73600 132.41200 113.18600 1.000 23.41717  ? 89  VAL B CA   1 
ATOM   3123 C C    . VAL B 1 89  ? 104.66600 130.97800 113.69000 1.000 22.89169  ? 89  VAL B C    1 
ATOM   3124 O O    . VAL B 1 89  ? 104.27900 130.73100 114.83700 1.000 34.93213  ? 89  VAL B O    1 
ATOM   3125 C CB   . VAL B 1 89  ? 103.48600 132.79700 112.37500 1.000 26.70955  ? 89  VAL B CB   1 
ATOM   3126 C CG1  . VAL B 1 89  ? 102.24800 132.77200 113.25500 1.000 27.38629  ? 89  VAL B CG1  1 
ATOM   3127 C CG2  . VAL B 1 89  ? 103.66300 134.16900 111.74600 1.000 22.79998  ? 89  VAL B CG2  1 
ATOM   3128 N N    . PHE B 1 90  ? 105.06400 130.00900 112.86000 1.000 11.37379  ? 90  PHE B N    1 
ATOM   3129 C CA   . PHE B 1 90  ? 105.08900 128.62400 113.32300 1.000 12.51629  ? 90  PHE B CA   1 
ATOM   3130 C C    . PHE B 1 90  ? 106.05400 128.44200 114.49700 1.000 15.79308  ? 90  PHE B C    1 
ATOM   3131 O O    . PHE B 1 90  ? 105.71100 127.81500 115.51400 1.000 19.53341  ? 90  PHE B O    1 
ATOM   3132 C CB   . PHE B 1 90  ? 105.45700 127.69400 112.16600 1.000 13.70133  ? 90  PHE B CB   1 
ATOM   3133 C CG   . PHE B 1 90  ? 105.27100 126.23900 112.47900 1.000 21.73500  ? 90  PHE B CG   1 
ATOM   3134 C CD1  . PHE B 1 90  ? 104.00600 125.72000 112.68800 1.000 18.62358  ? 90  PHE B CD1  1 
ATOM   3135 C CD2  . PHE B 1 90  ? 106.36000 125.39100 112.56800 1.000 17.30809  ? 90  PHE B CD2  1 
ATOM   3136 C CE1  . PHE B 1 90  ? 103.83200 124.38500 112.98300 1.000 21.08133  ? 90  PHE B CE1  1 
ATOM   3137 C CE2  . PHE B 1 90  ? 106.19000 124.05500 112.86000 1.000 12.54349  ? 90  PHE B CE2  1 
ATOM   3138 C CZ   . PHE B 1 90  ? 104.92500 123.55200 113.06700 1.000 11.35982  ? 90  PHE B CZ   1 
ATOM   3139 N N    . SER B 1 91  ? 107.27000 128.99000 114.38100 1.000 21.40830  ? 91  SER B N    1 
ATOM   3140 C CA   . SER B 1 91  ? 108.24500 128.83800 115.45700 1.000 14.01941  ? 91  SER B CA   1 
ATOM   3141 C C    . SER B 1 91  ? 107.79900 129.55500 116.72800 1.000 21.70690  ? 91  SER B C    1 
ATOM   3142 O O    . SER B 1 91  ? 107.98900 129.03900 117.84100 1.000 25.30343  ? 91  SER B O    1 
ATOM   3143 C CB   . SER B 1 91  ? 109.60500 129.35500 114.99700 1.000 13.97562  ? 91  SER B CB   1 
ATOM   3144 O OG   . SER B 1 91  ? 109.99100 128.73700 113.78300 1.000 19.96661  ? 91  SER B OG   1 
ATOM   3145 N N    . ALA B 1 92  ? 107.15600 130.71900 116.58900 1.000 14.73837  ? 92  ALA B N    1 
ATOM   3146 C CA   . ALA B 1 92  ? 106.68300 131.41100 117.78100 1.000 11.48574  ? 92  ALA B CA   1 
ATOM   3147 C C    . ALA B 1 92  ? 105.51200 130.67900 118.41800 1.000 19.27155  ? 92  ALA B C    1 
ATOM   3148 O O    . ALA B 1 92  ? 105.36600 130.69700 119.64600 1.000 33.79653  ? 92  ALA B O    1 
ATOM   3149 C CB   . ALA B 1 92  ? 106.29500 132.84700 117.43700 1.000 14.52753  ? 92  ALA B CB   1 
ATOM   3150 N N    . LYS B 1 93  ? 104.69900 129.99000 117.61400 1.000 18.96147  ? 93  LYS B N    1 
ATOM   3151 C CA   . LYS B 1 93  ? 103.60900 129.20200 118.17500 1.000 12.89969  ? 93  LYS B CA   1 
ATOM   3152 C C    . LYS B 1 93  ? 104.14300 128.01800 118.96900 1.000 10.90770  ? 93  LYS B C    1 
ATOM   3153 O O    . LYS B 1 93  ? 103.63200 127.70500 120.05200 1.000 22.14610  ? 93  LYS B O    1 
ATOM   3154 C CB   . LYS B 1 93  ? 102.68200 128.72600 117.05700 1.000 19.39600  ? 93  LYS B CB   1 
ATOM   3155 C CG   . LYS B 1 93  ? 101.90800 129.83900 116.37600 1.000 18.22642  ? 93  LYS B CG   1 
ATOM   3156 C CD   . LYS B 1 93  ? 100.52800 129.37100 115.95700 1.000 19.26503  ? 93  LYS B CD   1 
ATOM   3157 C CE   . LYS B 1 93  ? 100.50200 128.98800 114.49100 1.000 16.05758  ? 93  LYS B CE   1 
ATOM   3158 N NZ   . LYS B 1 93  ? 99.23800  128.30400 114.12000 1.000 8.25302   ? 93  LYS B NZ   1 
ATOM   3159 N N    . ILE B 1 94  ? 105.18400 127.35800 118.45600 1.000 8.81727   ? 94  ILE B N    1 
ATOM   3160 C CA   . ILE B 1 94  ? 105.77700 126.25000 119.20400 1.000 12.68681  ? 94  ILE B CA   1 
ATOM   3161 C C    . ILE B 1 94  ? 106.37400 126.75200 120.51700 1.000 22.02868  ? 94  ILE B C    1 
ATOM   3162 O O    . ILE B 1 94  ? 106.19200 126.13500 121.58100 1.000 24.48257  ? 94  ILE B O    1 
ATOM   3163 C CB   . ILE B 1 94  ? 106.83000 125.52500 118.34700 1.000 23.13915  ? 94  ILE B CB   1 
ATOM   3164 C CG1  . ILE B 1 94  ? 106.17100 124.82400 117.16100 1.000 19.44355  ? 94  ILE B CG1  1 
ATOM   3165 C CG2  . ILE B 1 94  ? 107.60200 124.52300 119.18900 1.000 18.09899  ? 94  ILE B CG2  1 
ATOM   3166 C CD1  . ILE B 1 94  ? 105.88800 123.36500 117.40500 1.000 14.51557  ? 94  ILE B CD1  1 
ATOM   3167 N N    . GLY B 1 95  ? 107.07700 127.88800 120.46900 1.000 21.16816  ? 95  GLY B N    1 
ATOM   3168 C CA   . GLY B 1 95  ? 107.61900 128.45300 121.69500 1.000 5.02251   ? 95  GLY B CA   1 
ATOM   3169 C C    . GLY B 1 95  ? 106.54400 128.79400 122.71200 1.000 19.42626  ? 95  GLY B C    1 
ATOM   3170 O O    . GLY B 1 95  ? 106.69600 128.52100 123.90700 1.000 27.67379  ? 95  GLY B O    1 
ATOM   3171 N N    . LEU B 1 96  ? 105.43400 129.37800 122.25000 1.000 23.42604  ? 96  LEU B N    1 
ATOM   3172 C CA   . LEU B 1 96  ? 104.34100 129.71500 123.15800 1.000 22.14213  ? 96  LEU B CA   1 
ATOM   3173 C C    . LEU B 1 96  ? 103.73400 128.46700 123.78400 1.000 23.42583  ? 96  LEU B C    1 
ATOM   3174 O O    . LEU B 1 96  ? 103.45600 128.43800 124.99200 1.000 30.02642  ? 96  LEU B O    1 
ATOM   3175 C CB   . LEU B 1 96  ? 103.27100 130.51000 122.41300 1.000 23.78158  ? 96  LEU B CB   1 
ATOM   3176 C CG   . LEU B 1 96  ? 102.08200 130.99500 123.24100 1.000 25.04606  ? 96  LEU B CG   1 
ATOM   3177 C CD1  . LEU B 1 96  ? 102.55200 131.87100 124.38900 1.000 24.79910  ? 96  LEU B CD1  1 
ATOM   3178 C CD2  . LEU B 1 96  ? 101.09300 131.73700 122.36600 1.000 20.19394  ? 96  LEU B CD2  1 
ATOM   3179 N N    . ALA B 1 97  ? 103.51500 127.42400 122.98100 1.000 22.26058  ? 97  ALA B N    1 
ATOM   3180 C CA   . ALA B 1 97  ? 102.90500 126.21400 123.51900 1.000 21.39637  ? 97  ALA B CA   1 
ATOM   3181 C C    . ALA B 1 97  ? 103.79000 125.59500 124.59000 1.000 24.82450  ? 97  ALA B C    1 
ATOM   3182 O O    . ALA B 1 97  ? 103.30000 125.15600 125.64000 1.000 29.82209  ? 97  ALA B O    1 
ATOM   3183 C CB   . ALA B 1 97  ? 102.63300 125.21400 122.39600 1.000 11.32035  ? 97  ALA B CB   1 
ATOM   3184 N N    . LEU B 1 98  ? 105.10300 125.56300 124.35100 1.000 27.00286  ? 98  LEU B N    1 
ATOM   3185 C CA   . LEU B 1 98  ? 105.99900 125.00300 125.35700 1.000 21.13924  ? 98  LEU B CA   1 
ATOM   3186 C C    . LEU B 1 98  ? 106.01800 125.86200 126.62100 1.000 25.33215  ? 98  LEU B C    1 
ATOM   3187 O O    . LEU B 1 98  ? 105.96500 125.33600 127.74300 1.000 24.46486  ? 98  LEU B O    1 
ATOM   3188 C CB   . LEU B 1 98  ? 107.40000 124.85600 124.77000 1.000 19.69700  ? 98  LEU B CB   1 
ATOM   3189 C CG   . LEU B 1 98  ? 107.75400 123.43700 124.32200 1.000 23.93502  ? 98  LEU B CG   1 
ATOM   3190 C CD1  . LEU B 1 98  ? 109.14300 123.40000 123.70800 1.000 24.41065  ? 98  LEU B CD1  1 
ATOM   3191 C CD2  . LEU B 1 98  ? 107.63200 122.45200 125.47100 1.000 27.58831  ? 98  LEU B CD2  1 
ATOM   3192 N N    . THR B 1 99  ? 106.06000 127.18900 126.46400 1.000 24.66523  ? 99  THR B N    1 
ATOM   3193 C CA   . THR B 1 99  ? 106.05700 128.05600 127.63700 1.000 22.31023  ? 99  THR B CA   1 
ATOM   3194 C C    . THR B 1 99  ? 104.77700 127.90500 128.44900 1.000 32.16958  ? 99  THR B C    1 
ATOM   3195 O O    . THR B 1 99  ? 104.80100 128.05000 129.67800 1.000 37.47746  ? 99  THR B O    1 
ATOM   3196 C CB   . THR B 1 99  ? 106.23900 129.51200 127.20900 1.000 23.50763  ? 99  THR B CB   1 
ATOM   3197 O OG1  . THR B 1 99  ? 107.56200 129.70100 126.69600 1.000 35.54265  ? 99  THR B OG1  1 
ATOM   3198 C CG2  . THR B 1 99  ? 106.00300 130.44800 128.37400 1.000 26.75379  ? 99  THR B CG2  1 
ATOM   3199 N N    . ILE B 1 100 ? 103.67100 127.53800 127.80500 1.000 33.66751  ? 100 ILE B N    1 
ATOM   3200 C CA   . ILE B 1 100 ? 102.43800 127.33900 128.56200 1.000 30.84703  ? 100 ILE B CA   1 
ATOM   3201 C C    . ILE B 1 100 ? 102.45000 125.98800 129.26700 1.000 27.42384  ? 100 ILE B C    1 
ATOM   3202 O O    . ILE B 1 100 ? 102.06700 125.88300 130.44300 1.000 30.49119  ? 100 ILE B O    1 
ATOM   3203 C CB   . ILE B 1 100 ? 101.21500 127.48600 127.64000 1.000 35.07141  ? 100 ILE B CB   1 
ATOM   3204 C CG1  . ILE B 1 100 ? 101.04400 128.94200 127.20700 1.000 32.69295  ? 100 ILE B CG1  1 
ATOM   3205 C CG2  . ILE B 1 100 ? 99.96100  126.98700 128.33800 1.000 34.03987  ? 100 ILE B CG2  1 
ATOM   3206 C CD1  . ILE B 1 100 ? 100.21700 129.11200 125.95500 1.000 31.65766  ? 100 ILE B CD1  1 
ATOM   3207 N N    . VAL B 1 101 ? 102.90300 124.94200 128.57400 1.000 33.56677  ? 101 VAL B N    1 
ATOM   3208 C CA   . VAL B 1 101 ? 102.99200 123.60800 129.16100 1.000 31.17586  ? 101 VAL B CA   1 
ATOM   3209 C C    . VAL B 1 101 ? 104.08100 123.58800 130.23100 1.000 35.95395  ? 101 VAL B C    1 
ATOM   3210 O O    . VAL B 1 101 ? 104.27000 122.58200 130.92400 1.000 35.74947  ? 101 VAL B O    1 
ATOM   3211 C CB   . VAL B 1 101 ? 103.24500 122.55000 128.06800 1.000 33.30585  ? 101 VAL B CB   1 
ATOM   3212 C CG1  . VAL B 1 101 ? 103.98000 121.34000 128.61800 1.000 30.55486  ? 101 VAL B CG1  1 
ATOM   3213 C CG2  . VAL B 1 101 ? 101.93200 122.12600 127.43400 1.000 37.65233  ? 101 VAL B CG2  1 
ATOM   3214 N N    . ALA B 1 102 ? 104.76600 124.71400 130.41400 1.000 45.75534  ? 102 ALA B N    1 
ATOM   3215 C CA   . ALA B 1 102 ? 105.73500 124.84000 131.50000 1.000 39.59765  ? 102 ALA B CA   1 
ATOM   3216 C C    . ALA B 1 102 ? 105.26000 125.74000 132.63100 1.000 41.40083  ? 102 ALA B C    1 
ATOM   3217 O O    . ALA B 1 102 ? 105.52200 125.44500 133.80400 1.000 42.82717  ? 102 ALA B O    1 
ATOM   3218 C CB   . ALA B 1 102 ? 107.06800 125.37000 130.96300 1.000 32.55525  ? 102 ALA B CB   1 
ATOM   3219 N N    . LEU B 1 103 ? 104.52700 126.81300 132.31900 1.000 48.53421  ? 103 LEU B N    1 
ATOM   3220 C CA   . LEU B 1 103 ? 103.93300 127.61600 133.38300 1.000 46.12120  ? 103 LEU B CA   1 
ATOM   3221 C C    . LEU B 1 103 ? 102.89400 126.80800 134.14800 1.000 49.70408  ? 103 LEU B C    1 
ATOM   3222 O O    . LEU B 1 103 ? 102.77400 126.93600 135.37600 1.000 49.23600  ? 103 LEU B O    1 
ATOM   3223 C CB   . LEU B 1 103 ? 103.30000 128.88100 132.80300 1.000 45.35390  ? 103 LEU B CB   1 
ATOM   3224 C CG   . LEU B 1 103 ? 104.23500 130.00900 132.36600 1.000 49.73323  ? 103 LEU B CG   1 
ATOM   3225 C CD1  . LEU B 1 103 ? 103.51400 130.95800 131.42400 1.000 49.40741  ? 103 LEU B CD1  1 
ATOM   3226 C CD2  . LEU B 1 103 ? 104.79000 130.75700 133.56200 1.000 47.43562  ? 103 LEU B CD2  1 
ATOM   3227 N N    . LEU B 1 104 ? 102.14600 125.95300 133.44200 1.000 56.91977  ? 104 LEU B N    1 
ATOM   3228 C CA   . LEU B 1 104 ? 101.17000 125.10700 134.12300 1.000 56.27006  ? 104 LEU B CA   1 
ATOM   3229 C C    . LEU B 1 104 ? 101.85400 124.16500 135.10400 1.000 56.44999  ? 104 LEU B C    1 
ATOM   3230 O O    . LEU B 1 104 ? 101.35900 123.94900 136.21700 1.000 62.09374  ? 104 LEU B O    1 
ATOM   3231 C CB   . LEU B 1 104 ? 100.35100 124.31800 133.10100 1.000 57.51543  ? 104 LEU B CB   1 
ATOM   3232 C CG   . LEU B 1 104 ? 98.88400  124.71400 132.94100 1.000 55.38423  ? 104 LEU B CG   1 
ATOM   3233 C CD1  . LEU B 1 104 ? 98.75500  126.18300 132.58400 1.000 56.36368  ? 104 LEU B CD1  1 
ATOM   3234 C CD2  . LEU B 1 104 ? 98.22000  123.84800 131.88600 1.000 52.63433  ? 104 LEU B CD2  1 
ATOM   3235 N N    . ILE B 1 105 ? 102.99000 123.58800 134.70800 1.000 60.31284  ? 105 ILE B N    1 
ATOM   3236 C CA   . ILE B 1 105 ? 103.74400 122.73200 135.62000 1.000 63.45400  ? 105 ILE B CA   1 
ATOM   3237 C C    . ILE B 1 105 ? 104.22000 123.53000 136.82700 1.000 60.04623  ? 105 ILE B C    1 
ATOM   3238 O O    . ILE B 1 105 ? 104.08300 123.09100 137.97500 1.000 57.95616  ? 105 ILE B O    1 
ATOM   3239 C CB   . ILE B 1 105 ? 104.92200 122.06400 134.88800 1.000 59.89910  ? 105 ILE B CB   1 
ATOM   3240 C CG1  . ILE B 1 105 ? 104.42600 121.25700 133.68700 1.000 56.59511  ? 105 ILE B CG1  1 
ATOM   3241 C CG2  . ILE B 1 105 ? 105.70400 121.17700 135.84200 1.000 57.50499  ? 105 ILE B CG2  1 
ATOM   3242 C CD1  . ILE B 1 105 ? 103.45000 120.16300 134.04500 1.000 57.07743  ? 105 ILE B CD1  1 
ATOM   3243 N N    . PHE B 1 106 ? 104.78400 124.71800 136.59000 1.000 60.56806  ? 106 PHE B N    1 
ATOM   3244 C CA   . PHE B 1 106 ? 105.35100 125.48100 137.70000 1.000 58.10449  ? 106 PHE B CA   1 
ATOM   3245 C C    . PHE B 1 106 ? 104.29000 125.86300 138.72700 1.000 59.95363  ? 106 PHE B C    1 
ATOM   3246 O O    . PHE B 1 106 ? 104.43900 125.57500 139.92000 1.000 61.46060  ? 106 PHE B O    1 
ATOM   3247 C CB   . PHE B 1 106 ? 106.06900 126.73300 137.19100 1.000 57.79164  ? 106 PHE B CB   1 
ATOM   3248 C CG   . PHE B 1 106 ? 107.35300 126.45000 136.46600 1.000 62.16254  ? 106 PHE B CG   1 
ATOM   3249 C CD1  . PHE B 1 106 ? 107.94400 125.20100 136.53200 1.000 59.97182  ? 106 PHE B CD1  1 
ATOM   3250 C CD2  . PHE B 1 106 ? 107.98300 127.44500 135.73800 1.000 58.64507  ? 106 PHE B CD2  1 
ATOM   3251 C CE1  . PHE B 1 106 ? 109.13000 124.94600 135.87300 1.000 60.17437  ? 106 PHE B CE1  1 
ATOM   3252 C CE2  . PHE B 1 106 ? 109.16800 127.19500 135.07700 1.000 57.71720  ? 106 PHE B CE2  1 
ATOM   3253 C CZ   . PHE B 1 106 ? 109.74200 125.94400 135.14500 1.000 58.30029  ? 106 PHE B CZ   1 
ATOM   3254 N N    . TYR B 1 107 ? 103.20600 126.50700 138.29300 1.000 70.34585  ? 107 TYR B N    1 
ATOM   3255 C CA   . TYR B 1 107 ? 102.25300 127.04400 139.26500 1.000 73.48589  ? 107 TYR B CA   1 
ATOM   3256 C C    . TYR B 1 107 ? 101.02900 126.16500 139.50000 1.000 73.52973  ? 107 TYR B C    1 
ATOM   3257 O O    . TYR B 1 107 ? 100.66200 125.92500 140.65300 1.000 72.46055  ? 107 TYR B O    1 
ATOM   3258 C CB   . TYR B 1 107 ? 101.80900 128.45600 138.86100 1.000 72.83604  ? 107 TYR B CB   1 
ATOM   3259 C CG   . TYR B 1 107 ? 102.92200 129.31800 138.31700 1.000 72.04588  ? 107 TYR B CG   1 
ATOM   3260 C CD1  . TYR B 1 107 ? 104.04800 129.58800 139.08300 1.000 68.67477  ? 107 TYR B CD1  1 
ATOM   3261 C CD2  . TYR B 1 107 ? 102.84200 129.87900 137.05200 1.000 71.97594  ? 107 TYR B CD2  1 
ATOM   3262 C CE1  . TYR B 1 107 ? 105.06800 130.38000 138.60100 1.000 70.76896  ? 107 TYR B CE1  1 
ATOM   3263 C CE2  . TYR B 1 107 ? 103.85800 130.67300 136.56200 1.000 72.60119  ? 107 TYR B CE2  1 
ATOM   3264 C CZ   . TYR B 1 107 ? 104.96900 130.92000 137.33900 1.000 72.40531  ? 107 TYR B CZ   1 
ATOM   3265 O OH   . TYR B 1 107 ? 105.98300 131.71200 136.85400 1.000 72.71313  ? 107 TYR B OH   1 
ATOM   3266 N N    . GLN B 1 108 ? 100.38200 125.67900 138.44100 1.000 82.52031  ? 108 GLN B N    1 
ATOM   3267 C CA   . GLN B 1 108 ? 99.15100  124.91800 138.62600 1.000 82.90723  ? 108 GLN B CA   1 
ATOM   3268 C C    . GLN B 1 108 ? 99.33000  123.65600 139.46300 1.000 81.86975  ? 108 GLN B C    1 
ATOM   3269 O O    . GLN B 1 108 ? 98.32600  123.01600 139.79400 1.000 80.68211  ? 108 GLN B O    1 
ATOM   3270 C CB   . GLN B 1 108 ? 98.55000  124.54800 137.26900 1.000 83.61887  ? 108 GLN B CB   1 
ATOM   3271 C CG   . GLN B 1 108 ? 97.04700  124.31600 137.31000 1.000 83.35545  ? 108 GLN B CG   1 
ATOM   3272 C CD   . GLN B 1 108 ? 96.25900  125.60800 137.38900 1.000 85.05104  ? 108 GLN B CD   1 
ATOM   3273 O OE1  . GLN B 1 108 ? 96.17700  126.23400 138.44500 1.000 83.31827  ? 108 GLN B OE1  1 
ATOM   3274 N NE2  . GLN B 1 108 ? 95.67000  126.01200 136.27000 1.000 83.83226  ? 108 GLN B NE2  1 
ATOM   3275 N N    . GLU B 1 109 ? 100.56100 123.27600 139.81300 1.000 82.51404  ? 109 GLU B N    1 
ATOM   3276 C CA   . GLU B 1 109 ? 100.73800 122.10100 140.65600 1.000 84.05704  ? 109 GLU B CA   1 
ATOM   3277 C C    . GLU B 1 109 ? 101.94400 122.25400 141.57500 1.000 86.94081  ? 109 GLU B C    1 
ATOM   3278 O O    . GLU B 1 109 ? 103.03900 122.58000 141.09000 1.000 85.39442  ? 109 GLU B O    1 
ATOM   3279 C CB   . GLU B 1 109 ? 100.89600 120.83700 139.80900 1.000 83.85208  ? 109 GLU B CB   1 
ATOM   3280 C CG   . GLU B 1 109 ? 99.62500  120.39900 139.09800 1.000 85.82120  ? 109 GLU B CG   1 
ATOM   3281 C CD   . GLU B 1 109 ? 99.45000  121.06800 137.74800 1.000 88.12429  ? 109 GLU B CD   1 
ATOM   3282 O OE1  . GLU B 1 109 ? 100.46300 121.26800 137.04500 1.000 87.20628  ? 109 GLU B OE1  1 
ATOM   3283 O OE2  . GLU B 1 109 ? 98.29900  121.39600 137.39200 1.000 87.02247  ? 109 GLU B OE2  1 
ATOM   3284 N N    . PRO B 1 110 ? 101.78100 122.03000 142.87800 1.000 98.15870  ? 110 PRO B N    1 
ATOM   3285 C CA   . PRO B 1 110 ? 102.91900 122.06600 143.81200 1.000 97.84078  ? 110 PRO B CA   1 
ATOM   3286 C C    . PRO B 1 110 ? 103.45400 120.70300 144.23400 1.000 97.88970  ? 110 PRO B C    1 
ATOM   3287 O O    . PRO B 1 110 ? 104.36700 120.66100 145.06600 1.000 97.15276  ? 110 PRO B O    1 
ATOM   3288 C CB   . PRO B 1 110 ? 102.30800 122.79100 145.01600 1.000 96.47426  ? 110 PRO B CB   1 
ATOM   3289 C CG   . PRO B 1 110 ? 100.84200 122.39000 144.99300 1.000 97.53752  ? 110 PRO B CG   1 
ATOM   3290 C CD   . PRO B 1 110 ? 100.50000 121.91700 143.59200 1.000 96.55073  ? 110 PRO B CD   1 
ATOM   3291 N N    . ASN B 1 111 ? 102.92000 119.60900 143.69500 1.000 100.69007 ? 111 ASN B N    1 
ATOM   3292 C CA   . ASN B 1 111 ? 103.32600 118.28400 144.13200 1.000 99.81679  ? 111 ASN B CA   1 
ATOM   3293 C C    . ASN B 1 111 ? 104.77000 117.99000 143.72400 1.000 98.39057  ? 111 ASN B C    1 
ATOM   3294 O O    . ASN B 1 111 ? 105.26000 118.50900 142.71900 1.000 98.08528  ? 111 ASN B O    1 
ATOM   3295 C CB   . ASN B 1 111 ? 102.40000 117.22400 143.54200 1.000 100.56806 ? 111 ASN B CB   1 
ATOM   3296 C CG   . ASN B 1 111 ? 101.01600 117.25600 144.15600 1.000 101.10472 ? 111 ASN B CG   1 
ATOM   3297 O OD1  . ASN B 1 111 ? 100.82800 117.74300 145.27000 1.000 101.85207 ? 111 ASN B OD1  1 
ATOM   3298 N ND2  . ASN B 1 111 ? 100.03500 116.73600 143.42700 1.000 98.17907  ? 111 ASN B ND2  1 
ATOM   3299 N N    . PRO B 1 112 ? 105.47100 117.15200 144.49400 1.000 97.15269  ? 112 PRO B N    1 
ATOM   3300 C CA   . PRO B 1 112 ? 106.87200 116.85700 144.15000 1.000 97.45932  ? 112 PRO B CA   1 
ATOM   3301 C C    . PRO B 1 112 ? 107.01600 116.00100 142.90400 1.000 97.71394  ? 112 PRO B C    1 
ATOM   3302 O O    . PRO B 1 112 ? 107.88700 116.27500 142.06900 1.000 94.47175  ? 112 PRO B O    1 
ATOM   3303 C CB   . PRO B 1 112 ? 107.39000 116.13600 145.40200 1.000 95.23820  ? 112 PRO B CB   1 
ATOM   3304 C CG   . PRO B 1 112 ? 106.17000 115.52100 146.00300 1.000 95.34624  ? 112 PRO B CG   1 
ATOM   3305 C CD   . PRO B 1 112 ? 105.05900 116.50100 145.74900 1.000 96.35945  ? 112 PRO B CD   1 
ATOM   3306 N N    . ASP B 1 113 ? 106.18700 114.96500 142.75600 1.000 90.96412  ? 113 ASP B N    1 
ATOM   3307 C CA   . ASP B 1 113 ? 106.30500 114.05700 141.62200 1.000 88.02923  ? 113 ASP B CA   1 
ATOM   3308 C C    . ASP B 1 113 ? 105.75600 114.64800 140.33200 1.000 86.05307  ? 113 ASP B C    1 
ATOM   3309 O O    . ASP B 1 113 ? 106.15200 114.20500 139.25000 1.000 82.25354  ? 113 ASP B O    1 
ATOM   3310 C CB   . ASP B 1 113 ? 105.59100 112.73800 141.92200 1.000 85.67794  ? 113 ASP B CB   1 
ATOM   3311 C CG   . ASP B 1 113 ? 105.94900 112.17800 143.28200 1.000 87.87268  ? 113 ASP B CG   1 
ATOM   3312 O OD1  . ASP B 1 113 ? 107.06600 112.45900 143.76500 1.000 88.39684  ? 113 ASP B OD1  1 
ATOM   3313 O OD2  . ASP B 1 113 ? 105.11400 111.45800 143.86800 1.000 87.88316  ? 113 ASP B OD2  1 
ATOM   3314 N N    . LEU B 1 114 ? 104.84400 115.62000 140.42400 1.000 85.45304  ? 114 LEU B N    1 
ATOM   3315 C CA   . LEU B 1 114 ? 104.27300 116.23100 139.22800 1.000 85.91634  ? 114 LEU B CA   1 
ATOM   3316 C C    . LEU B 1 114 ? 105.34800 116.66300 138.23900 1.000 85.11930  ? 114 LEU B C    1 
ATOM   3317 O O    . LEU B 1 114 ? 105.09700 116.70900 137.02900 1.000 82.37118  ? 114 LEU B O    1 
ATOM   3318 C CB   . LEU B 1 114 ? 103.39700 117.42400 139.62300 1.000 84.39830  ? 114 LEU B CB   1 
ATOM   3319 C CG   . LEU B 1 114 ? 102.33800 117.92200 138.63200 1.000 86.74313  ? 114 LEU B CG   1 
ATOM   3320 C CD1  . LEU B 1 114 ? 102.95800 118.48500 137.36200 1.000 85.68348  ? 114 LEU B CD1  1 
ATOM   3321 C CD2  . LEU B 1 114 ? 101.35400 116.80800 138.29900 1.000 84.04225  ? 114 LEU B CD2  1 
ATOM   3322 N N    . SER B 1 115 ? 106.55000 116.96500 138.72400 1.000 81.58618  ? 115 SER B N    1 
ATOM   3323 C CA   . SER B 1 115 ? 107.60800 117.51900 137.89000 1.000 79.05945  ? 115 SER B CA   1 
ATOM   3324 C C    . SER B 1 115 ? 108.55900 116.46300 137.34000 1.000 79.44489  ? 115 SER B C    1 
ATOM   3325 O O    . SER B 1 115 ? 109.46900 116.80900 136.58000 1.000 80.32595  ? 115 SER B O    1 
ATOM   3326 C CB   . SER B 1 115 ? 108.40300 118.56200 138.68000 1.000 79.19118  ? 115 SER B CB   1 
ATOM   3327 O OG   . SER B 1 115 ? 107.53600 119.42000 139.39900 1.000 80.88848  ? 115 SER B OG   1 
ATOM   3328 N N    . ARG B 1 116 ? 108.37800 115.19400 137.70000 1.000 74.42134  ? 116 ARG B N    1 
ATOM   3329 C CA   . ARG B 1 116 ? 109.13900 114.11100 137.09000 1.000 72.17777  ? 116 ARG B CA   1 
ATOM   3330 C C    . ARG B 1 116 ? 108.39800 113.45000 135.93900 1.000 75.24666  ? 116 ARG B C    1 
ATOM   3331 O O    . ARG B 1 116 ? 109.03800 112.89200 135.04300 1.000 76.34250  ? 116 ARG B O    1 
ATOM   3332 C CB   . ARG B 1 116 ? 109.50200 113.04800 138.13300 1.000 75.69760  ? 116 ARG B CB   1 
ATOM   3333 C CG   . ARG B 1 116 ? 110.50800 113.51700 139.17500 1.000 76.37366  ? 116 ARG B CG   1 
ATOM   3334 C CD   . ARG B 1 116 ? 111.16600 112.34000 139.88300 1.000 75.23876  ? 116 ARG B CD   1 
ATOM   3335 N NE   . ARG B 1 116 ? 110.21700 111.56100 140.67000 1.000 76.97607  ? 116 ARG B NE   1 
ATOM   3336 C CZ   . ARG B 1 116 ? 109.72100 110.38800 140.29900 1.000 76.99302  ? 116 ARG B CZ   1 
ATOM   3337 N NH1  . ARG B 1 116 ? 110.05900 109.82600 139.15000 1.000 74.49442  ? 116 ARG B NH1  1 
ATOM   3338 N NH2  . ARG B 1 116 ? 108.86400 109.76300 141.10200 1.000 74.34191  ? 116 ARG B NH2  1 
ATOM   3339 N N    . TYR B 1 117 ? 107.06600 113.50600 135.94400 1.000 68.78065  ? 117 TYR B N    1 
ATOM   3340 C CA   . TYR B 1 117 ? 106.24800 112.98400 134.85900 1.000 63.61393  ? 117 TYR B CA   1 
ATOM   3341 C C    . TYR B 1 117 ? 106.02500 114.01500 133.76100 1.000 62.06047  ? 117 TYR B C    1 
ATOM   3342 O O    . TYR B 1 117 ? 105.07900 113.88000 132.97700 1.000 61.18084  ? 117 TYR B O    1 
ATOM   3343 C CB   . TYR B 1 117 ? 104.89300 112.49700 135.38700 1.000 60.02179  ? 117 TYR B CB   1 
ATOM   3344 C CG   . TYR B 1 117 ? 104.91600 111.76000 136.71200 1.000 64.55828  ? 117 TYR B CG   1 
ATOM   3345 C CD1  . TYR B 1 117 ? 106.06500 111.12500 137.17000 1.000 63.39840  ? 117 TYR B CD1  1 
ATOM   3346 C CD2  . TYR B 1 117 ? 103.77900 111.70400 137.50800 1.000 64.42306  ? 117 TYR B CD2  1 
ATOM   3347 C CE1  . TYR B 1 117 ? 106.07800 110.45500 138.38000 1.000 65.81929  ? 117 TYR B CE1  1 
ATOM   3348 C CE2  . TYR B 1 117 ? 103.78200 111.03800 138.71700 1.000 65.22513  ? 117 TYR B CE2  1 
ATOM   3349 C CZ   . TYR B 1 117 ? 104.93400 110.41600 139.14800 1.000 69.57344  ? 117 TYR B CZ   1 
ATOM   3350 O OH   . TYR B 1 117 ? 104.94000 109.75200 140.35300 1.000 68.23239  ? 117 TYR B OH   1 
ATOM   3351 N N    . SER B 1 118 ? 106.87200 115.04200 133.69000 1.000 52.90523  ? 118 SER B N    1 
ATOM   3352 C CA   . SER B 1 118 ? 106.74200 116.07600 132.67400 1.000 47.22463  ? 118 SER B CA   1 
ATOM   3353 C C    . SER B 1 118 ? 107.19200 115.61900 131.29600 1.000 47.30139  ? 118 SER B C    1 
ATOM   3354 O O    . SER B 1 118 ? 107.00200 116.36100 130.32700 1.000 49.90997  ? 118 SER B O    1 
ATOM   3355 C CB   . SER B 1 118 ? 107.53800 117.31700 133.08300 1.000 47.62820  ? 118 SER B CB   1 
ATOM   3356 O OG   . SER B 1 118 ? 108.75800 116.95800 133.70600 1.000 49.03491  ? 118 SER B OG   1 
ATOM   3357 N N    . VAL B 1 119 ? 107.78000 114.42800 131.17800 1.000 39.91431  ? 119 VAL B N    1 
ATOM   3358 C CA   . VAL B 1 119 ? 108.26300 113.98000 129.87800 1.000 36.15395  ? 119 VAL B CA   1 
ATOM   3359 C C    . VAL B 1 119 ? 107.13600 113.41700 129.02300 1.000 39.28250  ? 119 VAL B C    1 
ATOM   3360 O O    . VAL B 1 119 ? 107.22900 113.44900 127.78700 1.000 45.05719  ? 119 VAL B O    1 
ATOM   3361 C CB   . VAL B 1 119 ? 109.39000 112.94700 130.05700 1.000 37.82259  ? 119 VAL B CB   1 
ATOM   3362 C CG1  . VAL B 1 119 ? 108.86400 111.69300 130.73700 1.000 36.51847  ? 119 VAL B CG1  1 
ATOM   3363 C CG2  . VAL B 1 119 ? 110.02900 112.61200 128.71900 1.000 40.85446  ? 119 VAL B CG2  1 
ATOM   3364 N N    . TRP B 1 120 ? 106.03300 112.99200 129.64600 1.000 34.71741  ? 120 TRP B N    1 
ATOM   3365 C CA   . TRP B 1 120 ? 104.89200 112.45400 128.91900 1.000 28.78029  ? 120 TRP B CA   1 
ATOM   3366 C C    . TRP B 1 120 ? 104.03600 113.54800 128.30400 1.000 32.53614  ? 120 TRP B C    1 
ATOM   3367 O O    . TRP B 1 120 ? 103.17900 113.24800 127.46600 1.000 38.25304  ? 120 TRP B O    1 
ATOM   3368 C CB   . TRP B 1 120 ? 104.02500 111.59700 129.84800 1.000 29.12705  ? 120 TRP B CB   1 
ATOM   3369 C CG   . TRP B 1 120 ? 104.67500 110.32800 130.31000 1.000 31.31735  ? 120 TRP B CG   1 
ATOM   3370 C CD1  . TRP B 1 120 ? 105.51300 110.17900 131.37500 1.000 34.51087  ? 120 TRP B CD1  1 
ATOM   3371 C CD2  . TRP B 1 120 ? 104.53300 109.02700 129.72900 1.000 35.02551  ? 120 TRP B CD2  1 
ATOM   3372 N NE1  . TRP B 1 120 ? 105.90600 108.87000 131.49000 1.000 32.56628  ? 120 TRP B NE1  1 
ATOM   3373 C CE2  . TRP B 1 120 ? 105.31700 108.14100 130.49100 1.000 33.26143  ? 120 TRP B CE2  1 
ATOM   3374 C CE3  . TRP B 1 120 ? 103.82100 108.52600 128.63500 1.000 35.10399  ? 120 TRP B CE3  1 
ATOM   3375 C CZ2  . TRP B 1 120 ? 105.40900 106.78400 130.19700 1.000 33.16078  ? 120 TRP B CZ2  1 
ATOM   3376 C CZ3  . TRP B 1 120 ? 103.91300 107.17700 128.34400 1.000 29.76303  ? 120 TRP B CZ3  1 
ATOM   3377 C CH2  . TRP B 1 120 ? 104.70100 106.32300 129.12100 1.000 32.29854  ? 120 TRP B CH2  1 
ATOM   3378 N N    . ALA B 1 121 ? 104.25100 114.80100 128.69800 1.000 29.35506  ? 121 ALA B N    1 
ATOM   3379 C CA   . ALA B 1 121 ? 103.60000 115.94600 128.08200 1.000 24.74281  ? 121 ALA B CA   1 
ATOM   3380 C C    . ALA B 1 121 ? 104.49900 116.64300 127.07600 1.000 27.12806  ? 121 ALA B C    1 
ATOM   3381 O O    . ALA B 1 121 ? 104.01400 117.11600 126.04300 1.000 36.03634  ? 121 ALA B O    1 
ATOM   3382 C CB   . ALA B 1 121 ? 103.15900 116.94900 129.15300 1.000 22.98674  ? 121 ALA B CB   1 
ATOM   3383 N N    . ILE B 1 122 ? 105.80700 116.66600 127.33300 1.000 25.21428  ? 122 ILE B N    1 
ATOM   3384 C CA   . ILE B 1 122 ? 106.73600 117.30100 126.40700 1.000 22.99592  ? 122 ILE B CA   1 
ATOM   3385 C C    . ILE B 1 122 ? 106.91600 116.44000 125.16500 1.000 20.69009  ? 122 ILE B C    1 
ATOM   3386 O O    . ILE B 1 122 ? 106.96400 116.95500 124.04200 1.000 29.01218  ? 122 ILE B O    1 
ATOM   3387 C CB   . ILE B 1 122 ? 108.07900 117.58100 127.10600 1.000 32.79342  ? 122 ILE B CB   1 
ATOM   3388 C CG1  . ILE B 1 122 ? 107.86800 118.46600 128.33500 1.000 29.09488  ? 122 ILE B CG1  1 
ATOM   3389 C CG2  . ILE B 1 122 ? 109.05900 118.23800 126.14500 1.000 25.53710  ? 122 ILE B CG2  1 
ATOM   3390 C CD1  . ILE B 1 122 ? 109.01000 118.41700 129.32400 1.000 23.45739  ? 122 ILE B CD1  1 
ATOM   3391 N N    . LEU B 1 123 ? 107.00400 115.11800 125.33300 1.000 18.83967  ? 123 LEU B N    1 
ATOM   3392 C CA   . LEU B 1 123 ? 107.05100 114.24900 124.16200 1.000 24.52372  ? 123 LEU B CA   1 
ATOM   3393 C C    . LEU B 1 123 ? 105.78500 114.39400 123.32000 1.000 33.33767  ? 123 LEU B C    1 
ATOM   3394 O O    . LEU B 1 123 ? 105.84600 114.40600 122.08300 1.000 33.03747  ? 123 LEU B O    1 
ATOM   3395 C CB   . LEU B 1 123 ? 107.25000 112.79900 124.60100 1.000 26.28840  ? 123 LEU B CB   1 
ATOM   3396 C CG   . LEU B 1 123 ? 107.77600 111.80600 123.56500 1.000 28.91857  ? 123 LEU B CG   1 
ATOM   3397 C CD1  . LEU B 1 123 ? 109.16200 112.20800 123.09400 1.000 25.70703  ? 123 LEU B CD1  1 
ATOM   3398 C CD2  . LEU B 1 123 ? 107.79500 110.40600 124.14400 1.000 24.20701  ? 123 LEU B CD2  1 
ATOM   3399 N N    . THR B 1 124 ? 104.63200 114.54700 123.97300 1.000 28.84005  ? 124 THR B N    1 
ATOM   3400 C CA   . THR B 1 124 ? 103.38600 114.73500 123.23700 1.000 24.12342  ? 124 THR B CA   1 
ATOM   3401 C C    . THR B 1 124 ? 103.37900 116.05700 122.47800 1.000 25.97755  ? 124 THR B C    1 
ATOM   3402 O O    . THR B 1 124 ? 102.98300 116.10400 121.30700 1.000 29.39139  ? 124 THR B O    1 
ATOM   3403 C CB   . THR B 1 124 ? 102.19500 114.66500 124.19400 1.000 26.16036  ? 124 THR B CB   1 
ATOM   3404 O OG1  . THR B 1 124 ? 102.25200 113.44500 124.94200 1.000 36.47603  ? 124 THR B OG1  1 
ATOM   3405 C CG2  . THR B 1 124 ? 100.88900 114.71300 123.42200 1.000 19.33213  ? 124 THR B CG2  1 
ATOM   3406 N N    . VAL B 1 125 ? 103.81800 117.14200 123.12300 1.000 21.25202  ? 125 VAL B N    1 
ATOM   3407 C CA   . VAL B 1 125 ? 103.83000 118.43700 122.45500 1.000 16.74707  ? 125 VAL B CA   1 
ATOM   3408 C C    . VAL B 1 125 ? 104.92200 118.52200 121.39800 1.000 24.92451  ? 125 VAL B C    1 
ATOM   3409 O O    . VAL B 1 125 ? 104.88700 119.41800 120.54900 1.000 33.70830  ? 125 VAL B O    1 
ATOM   3410 C CB   . VAL B 1 125 ? 103.98800 119.57400 123.48100 1.000 23.94221  ? 125 VAL B CB   1 
ATOM   3411 C CG1  . VAL B 1 125 ? 103.90800 120.92200 122.79200 1.000 19.96372  ? 125 VAL B CG1  1 
ATOM   3412 C CG2  . VAL B 1 125 ? 102.92700 119.46400 124.55600 1.000 23.58490  ? 125 VAL B CG2  1 
ATOM   3413 N N    . VAL B 1 126 ? 105.89300 117.60600 121.41800 1.000 25.33244  ? 126 VAL B N    1 
ATOM   3414 C CA   . VAL B 1 126 ? 106.94200 117.58300 120.40600 1.000 22.64952  ? 126 VAL B CA   1 
ATOM   3415 C C    . VAL B 1 126 ? 106.67900 116.53500 119.33700 1.000 27.67634  ? 126 VAL B C    1 
ATOM   3416 O O    . VAL B 1 126 ? 107.43300 116.44500 118.36000 1.000 28.89212  ? 126 VAL B O    1 
ATOM   3417 C CB   . VAL B 1 126 ? 108.32200 117.36100 121.06300 1.000 26.63495  ? 126 VAL B CB   1 
ATOM   3418 C CG1  . VAL B 1 126 ? 109.41200 117.19400 120.02000 1.000 25.25221  ? 126 VAL B CG1  1 
ATOM   3419 C CG2  . VAL B 1 126 ? 108.65400 118.51400 121.99700 1.000 23.29034  ? 126 VAL B CG2  1 
ATOM   3420 N N    . VAL B 1 127 ? 105.60700 115.76100 119.47600 1.000 28.75445  ? 127 VAL B N    1 
ATOM   3421 C CA   . VAL B 1 127 ? 105.23700 114.78300 118.46200 1.000 19.34200  ? 127 VAL B CA   1 
ATOM   3422 C C    . VAL B 1 127 ? 103.90900 115.09600 117.78200 1.000 18.20086  ? 127 VAL B C    1 
ATOM   3423 O O    . VAL B 1 127 ? 103.68200 114.61800 116.65900 1.000 24.40412  ? 127 VAL B O    1 
ATOM   3424 C CB   . VAL B 1 127 ? 105.20500 113.36000 119.06100 1.000 26.34866  ? 127 VAL B CB   1 
ATOM   3425 C CG1  . VAL B 1 127 ? 104.56400 112.37700 118.09400 1.000 19.49637  ? 127 VAL B CG1  1 
ATOM   3426 C CG2  . VAL B 1 127 ? 106.60700 112.91000 119.43800 1.000 25.69468  ? 127 VAL B CG2  1 
ATOM   3427 N N    . VAL B 1 128 ? 103.02500 115.88900 118.38800 1.000 19.99890  ? 128 VAL B N    1 
ATOM   3428 C CA   . VAL B 1 128 ? 101.70400 116.12300 117.81100 1.000 24.71804  ? 128 VAL B CA   1 
ATOM   3429 C C    . VAL B 1 128 ? 101.55400 117.48900 117.13700 1.000 21.63360  ? 128 VAL B C    1 
ATOM   3430 O O    . VAL B 1 128 ? 100.61400 117.67300 116.35000 1.000 21.42263  ? 128 VAL B O    1 
ATOM   3431 C CB   . VAL B 1 128 ? 100.61200 115.93500 118.88800 1.000 21.71939  ? 128 VAL B CB   1 
ATOM   3432 C CG1  . VAL B 1 128 ? 99.30100  116.56700 118.45300 1.000 25.29869  ? 128 VAL B CG1  1 
ATOM   3433 C CG2  . VAL B 1 128 ? 100.41300 114.45900 119.18800 1.000 12.54644  ? 128 VAL B CG2  1 
ATOM   3434 N N    . PHE B 1 129 ? 102.45900 118.43300 117.39000 1.000 19.44347  ? 129 PHE B N    1 
ATOM   3435 C CA   . PHE B 1 129 ? 102.38100 119.76500 116.79200 1.000 23.49639  ? 129 PHE B CA   1 
ATOM   3436 C C    . PHE B 1 129 ? 102.91200 119.71500 115.36100 1.000 23.18949  ? 129 PHE B C    1 
ATOM   3437 O O    . PHE B 1 129 ? 104.12000 119.58100 115.14600 1.000 30.27462  ? 129 PHE B O    1 
ATOM   3438 C CB   . PHE B 1 129 ? 103.16700 120.76300 117.63800 1.000 18.85558  ? 129 PHE B CB   1 
ATOM   3439 C CG   . PHE B 1 129 ? 102.59000 122.15100 117.64500 1.000 22.97901  ? 129 PHE B CG   1 
ATOM   3440 C CD1  . PHE B 1 129 ? 102.54700 122.90800 116.48800 1.000 26.23767  ? 129 PHE B CD1  1 
ATOM   3441 C CD2  . PHE B 1 129 ? 102.10100 122.70400 118.81500 1.000 23.11552  ? 129 PHE B CD2  1 
ATOM   3442 C CE1  . PHE B 1 129 ? 102.02100 124.18600 116.49900 1.000 18.52159  ? 129 PHE B CE1  1 
ATOM   3443 C CE2  . PHE B 1 129 ? 101.57200 123.98100 118.83000 1.000 13.95999  ? 129 PHE B CE2  1 
ATOM   3444 C CZ   . PHE B 1 129 ? 101.53300 124.72200 117.67100 1.000 9.51079   ? 129 PHE B CZ   1 
ATOM   3445 N N    . GLU B 1 130 ? 102.01700 119.83100 114.38300 1.000 18.86742  ? 130 GLU B N    1 
ATOM   3446 C CA   . GLU B 1 130 ? 102.36800 119.76100 112.97000 1.000 14.58547  ? 130 GLU B CA   1 
ATOM   3447 C C    . GLU B 1 130 ? 102.00200 121.05100 112.24300 1.000 24.93012  ? 130 GLU B C    1 
ATOM   3448 O O    . GLU B 1 130 ? 101.31200 121.92600 112.77100 1.000 28.33425  ? 130 GLU B O    1 
ATOM   3449 C CB   . GLU B 1 130 ? 101.69400 118.56400 112.29000 1.000 14.34517  ? 130 GLU B CB   1 
ATOM   3450 C CG   . GLU B 1 130 ? 101.75200 117.28400 113.10000 1.000 21.19930  ? 130 GLU B CG   1 
ATOM   3451 C CD   . GLU B 1 130 ? 102.86300 116.36500 112.63700 1.000 29.01695  ? 130 GLU B CD   1 
ATOM   3452 O OE1  . GLU B 1 130 ? 103.06700 116.24500 111.41200 1.000 36.86492  ? 130 GLU B OE1  1 
ATOM   3453 O OE2  . GLU B 1 130 ? 103.54200 115.77000 113.49900 1.000 30.27878  ? 130 GLU B OE2  1 
ATOM   3454 N N    . PHE B 1 131 ? 102.48300 121.14400 111.00000 1.000 18.39240  ? 131 PHE B N    1 
ATOM   3455 C CA   . PHE B 1 131 ? 102.30200 122.34700 110.19200 1.000 14.11549  ? 131 PHE B CA   1 
ATOM   3456 C C    . PHE B 1 131 ? 100.83300 122.64700 109.90700 1.000 16.31729  ? 131 PHE B C    1 
ATOM   3457 O O    . PHE B 1 131 ? 100.44500 123.81800 109.84200 1.000 19.38680  ? 131 PHE B O    1 
ATOM   3458 C CB   . PHE B 1 131 ? 103.07600 122.20300 108.87900 1.000 23.03252  ? 131 PHE B CB   1 
ATOM   3459 C CG   . PHE B 1 131 ? 103.69300 123.48100 108.38800 1.000 24.74274  ? 131 PHE B CG   1 
ATOM   3460 C CD1  . PHE B 1 131 ? 104.75500 124.05600 109.05900 1.000 16.89144  ? 131 PHE B CD1  1 
ATOM   3461 C CD2  . PHE B 1 131 ? 103.22000 124.09800 107.24300 1.000 27.13913  ? 131 PHE B CD2  1 
ATOM   3462 C CE1  . PHE B 1 131 ? 105.32500 125.23000 108.60600 1.000 20.66575  ? 131 PHE B CE1  1 
ATOM   3463 C CE2  . PHE B 1 131 ? 103.78800 125.27100 106.78500 1.000 21.94509  ? 131 PHE B CE2  1 
ATOM   3464 C CZ   . PHE B 1 131 ? 104.84100 125.83700 107.46900 1.000 23.92107  ? 131 PHE B CZ   1 
ATOM   3465 N N    . THR B 1 132 ? 100.00600 121.61900 109.73100 1.000 19.70382  ? 132 THR B N    1 
ATOM   3466 C CA   . THR B 1 132 ? 98.60100  121.79400 109.39100 1.000 10.74457  ? 132 THR B CA   1 
ATOM   3467 C C    . THR B 1 132 ? 97.70900  121.27000 110.50900 1.000 12.66800  ? 132 THR B C    1 
ATOM   3468 O O    . THR B 1 132 ? 98.13300  120.48700 111.36100 1.000 16.78955  ? 132 THR B O    1 
ATOM   3469 C CB   . THR B 1 132 ? 98.24700  121.09000 108.07000 1.000 13.88549  ? 132 THR B CB   1 
ATOM   3470 O OG1  . THR B 1 132 ? 98.69300  119.73100 108.11100 1.000 28.35165  ? 132 THR B OG1  1 
ATOM   3471 C CG2  . THR B 1 132 ? 98.89600  121.79700 106.89300 1.000 10.42106  ? 132 THR B CG2  1 
ATOM   3472 N N    . ILE B 1 133 ? 96.45700  121.73100 110.49800 1.000 9.29848   ? 133 ILE B N    1 
ATOM   3473 C CA   . ILE B 1 133 ? 95.48300  121.30400 111.50000 1.000 17.41100  ? 133 ILE B CA   1 
ATOM   3474 C C    . ILE B 1 133 ? 95.07900  119.84600 111.29900 1.000 22.82821  ? 133 ILE B C    1 
ATOM   3475 O O    . ILE B 1 133 ? 94.92500  119.09600 112.27100 1.000 30.63395  ? 133 ILE B O    1 
ATOM   3476 C CB   . ILE B 1 133 ? 94.26300  122.24300 111.47600 1.000 19.38684  ? 133 ILE B CB   1 
ATOM   3477 C CG1  . ILE B 1 133 ? 94.72000  123.70000 111.57500 1.000 14.86256  ? 133 ILE B CG1  1 
ATOM   3478 C CG2  . ILE B 1 133 ? 93.29100  121.89700 112.59000 1.000 21.05903  ? 133 ILE B CG2  1 
ATOM   3479 C CD1  . ILE B 1 133 ? 93.73500  124.68800 111.02200 1.000 24.47065  ? 133 ILE B CD1  1 
ATOM   3480 N N    . GLY B 1 134 ? 94.89900  119.41700 110.04600 1.000 2.76642   ? 134 GLY B N    1 
ATOM   3481 C CA   . GLY B 1 134 ? 94.45600  118.05300 109.80600 1.000 11.57788  ? 134 GLY B CA   1 
ATOM   3482 C C    . GLY B 1 134 ? 95.48100  117.00600 110.19100 1.000 17.68026  ? 134 GLY B C    1 
ATOM   3483 O O    . GLY B 1 134 ? 95.12400  115.93600 110.70100 1.000 30.31561  ? 134 GLY B O    1 
ATOM   3484 N N    . ALA B 1 135 ? 96.76500  117.32000 110.02000 1.000 10.72755  ? 135 ALA B N    1 
ATOM   3485 C CA   . ALA B 1 135 ? 97.80600  116.39600 110.45000 1.000 16.93954  ? 135 ALA B CA   1 
ATOM   3486 C C    . ALA B 1 135 ? 97.85900  116.30700 111.96900 1.000 13.41359  ? 135 ALA B C    1 
ATOM   3487 O O    . ALA B 1 135 ? 98.02000  115.21500 112.52800 1.000 23.61985  ? 135 ALA B O    1 
ATOM   3488 C CB   . ALA B 1 135 ? 99.15600  116.82700 109.88200 1.000 1.65032   ? 135 ALA B CB   1 
ATOM   3489 N N    . THR B 1 136 ? 97.71300  117.44500 112.65100 1.000 12.77903  ? 136 THR B N    1 
ATOM   3490 C CA   . THR B 1 136 ? 97.67500  117.43500 114.10800 1.000 19.61313  ? 136 THR B CA   1 
ATOM   3491 C C    . THR B 1 136 ? 96.49900  116.61000 114.61700 1.000 16.85096  ? 136 THR B C    1 
ATOM   3492 O O    . THR B 1 136 ? 96.64300  115.82600 115.56300 1.000 17.57730  ? 136 THR B O    1 
ATOM   3493 C CB   . THR B 1 136 ? 97.59600  118.86900 114.63600 1.000 12.75482  ? 136 THR B CB   1 
ATOM   3494 O OG1  . THR B 1 136 ? 98.69100  119.63200 114.11700 1.000 16.34562  ? 136 THR B OG1  1 
ATOM   3495 C CG2  . THR B 1 136 ? 97.64900  118.89400 116.15100 1.000 12.98276  ? 136 THR B CG2  1 
ATOM   3496 N N    . LEU B 1 137 ? 95.33500  116.74800 113.97800 1.000 15.23079  ? 137 LEU B N    1 
ATOM   3497 C CA   . LEU B 1 137 ? 94.16500  115.97700 114.38800 1.000 12.80488  ? 137 LEU B CA   1 
ATOM   3498 C C    . LEU B 1 137 ? 94.40000  114.48200 114.21000 1.000 20.40605  ? 137 LEU B C    1 
ATOM   3499 O O    . LEU B 1 137 ? 94.12700  113.68100 115.11800 1.000 29.40157  ? 137 LEU B O    1 
ATOM   3500 C CB   . LEU B 1 137 ? 92.94100  116.43000 113.59000 1.000 13.03847  ? 137 LEU B CB   1 
ATOM   3501 C CG   . LEU B 1 137 ? 92.41700  117.84200 113.86700 1.000 19.82688  ? 137 LEU B CG   1 
ATOM   3502 C CD1  . LEU B 1 137 ? 91.40500  118.26000 112.81400 1.000 15.62134  ? 137 LEU B CD1  1 
ATOM   3503 C CD2  . LEU B 1 137 ? 91.80700  117.93100 115.25400 1.000 16.35333  ? 137 LEU B CD2  1 
ATOM   3504 N N    . SER B 1 138 ? 94.91800  114.08500 113.04400 1.000 16.09299  ? 138 SER B N    1 
ATOM   3505 C CA   . SER B 1 138 ? 95.16200  112.66800 112.79300 1.000 13.38632  ? 138 SER B CA   1 
ATOM   3506 C C    . SER B 1 138 ? 96.16300  112.08900 113.78900 1.000 13.50731  ? 138 SER B C    1 
ATOM   3507 O O    . SER B 1 138 ? 95.94800  111.00400 114.34600 1.000 28.98176  ? 138 SER B O    1 
ATOM   3508 C CB   . SER B 1 138 ? 95.65400  112.47100 111.35900 1.000 21.69337  ? 138 SER B CB   1 
ATOM   3509 O OG   . SER B 1 138 ? 94.61600  112.71500 110.42700 1.000 28.64382  ? 138 SER B OG   1 
ATOM   3510 N N    . LYS B 1 139 ? 97.27200  112.79700 114.02000 1.000 18.00736  ? 139 LYS B N    1 
ATOM   3511 C CA   . LYS B 1 139 ? 98.28700  112.29400 114.94000 1.000 15.75056  ? 139 LYS B CA   1 
ATOM   3512 C C    . LYS B 1 139 ? 97.75200  112.19300 116.36400 1.000 14.86222  ? 139 LYS B C    1 
ATOM   3513 O O    . LYS B 1 139 ? 98.03300  111.21500 117.07000 1.000 22.95486  ? 139 LYS B O    1 
ATOM   3514 C CB   . LYS B 1 139 ? 99.52900  113.18300 114.88900 1.000 14.56435  ? 139 LYS B CB   1 
ATOM   3515 C CG   . LYS B 1 139 ? 100.10400 113.34500 113.49400 1.000 21.14483  ? 139 LYS B CG   1 
ATOM   3516 C CD   . LYS B 1 139 ? 101.35600 112.51000 113.29800 1.000 18.26743  ? 139 LYS B CD   1 
ATOM   3517 C CE   . LYS B 1 139 ? 102.38800 112.79500 114.37300 1.000 30.12669  ? 139 LYS B CE   1 
ATOM   3518 N NZ   . LYS B 1 139 ? 103.76300 112.45300 113.92000 1.000 23.55241  ? 139 LYS B NZ   1 
ATOM   3519 N N    . GLY B 1 140 ? 96.98900  113.19300 116.81200 1.000 13.45341  ? 140 GLY B N    1 
ATOM   3520 C CA   . GLY B 1 140 ? 96.38900  113.10700 118.13300 1.000 11.85975  ? 140 GLY B CA   1 
ATOM   3521 C C    . GLY B 1 140 ? 95.49200  111.89400 118.27800 1.000 22.82175  ? 140 GLY B C    1 
ATOM   3522 O O    . GLY B 1 140 ? 95.55800  111.16500 119.27500 1.000 33.05855  ? 140 GLY B O    1 
ATOM   3523 N N    . PHE B 1 141 ? 94.62100  111.67500 117.29000 1.000 11.40299  ? 141 PHE B N    1 
ATOM   3524 C CA   . PHE B 1 141 ? 93.73600  110.51600 117.33000 1.000 12.58670  ? 141 PHE B CA   1 
ATOM   3525 C C    . PHE B 1 141 ? 94.53300  109.21800 117.42500 1.000 22.58076  ? 141 PHE B C    1 
ATOM   3526 O O    . PHE B 1 141 ? 94.23500  108.34600 118.25500 1.000 34.99332  ? 141 PHE B O    1 
ATOM   3527 C CB   . PHE B 1 141 ? 92.83500  110.51600 116.09600 1.000 18.10717  ? 141 PHE B CB   1 
ATOM   3528 C CG   . PHE B 1 141 ? 91.71000  109.52700 116.16500 1.000 21.00067  ? 141 PHE B CG   1 
ATOM   3529 C CD1  . PHE B 1 141 ? 90.64400  109.73300 117.01900 1.000 17.94798  ? 141 PHE B CD1  1 
ATOM   3530 C CD2  . PHE B 1 141 ? 91.71500  108.39600 115.37000 1.000 25.88959  ? 141 PHE B CD2  1 
ATOM   3531 C CE1  . PHE B 1 141 ? 89.61000  108.82800 117.08500 1.000 20.58609  ? 141 PHE B CE1  1 
ATOM   3532 C CE2  . PHE B 1 141 ? 90.68400  107.48900 115.43200 1.000 24.36453  ? 141 PHE B CE2  1 
ATOM   3533 C CZ   . PHE B 1 141 ? 89.62900  107.70500 116.29000 1.000 22.56011  ? 141 PHE B CZ   1 
ATOM   3534 N N    . ASN B 1 142 ? 95.54600  109.06600 116.56600 1.000 20.73474  ? 142 ASN B N    1 
ATOM   3535 C CA   . ASN B 1 142 ? 96.35300  107.84700 116.58300 1.000 13.50824  ? 142 ASN B CA   1 
ATOM   3536 C C    . ASN B 1 142 ? 97.01900  107.63000 117.93700 1.000 20.44823  ? 142 ASN B C    1 
ATOM   3537 O O    . ASN B 1 142 ? 97.04000  106.50500 118.45400 1.000 24.16330  ? 142 ASN B O    1 
ATOM   3538 C CB   . ASN B 1 142 ? 97.40500  107.89500 115.47600 1.000 17.88608  ? 142 ASN B CB   1 
ATOM   3539 C CG   . ASN B 1 142 ? 96.79500  107.89700 114.09200 1.000 25.36723  ? 142 ASN B CG   1 
ATOM   3540 O OD1  . ASN B 1 142 ? 95.57700  107.85900 113.93800 1.000 28.89002  ? 142 ASN B OD1  1 
ATOM   3541 N ND2  . ASN B 1 142 ? 97.64300  107.94400 113.07400 1.000 25.87403  ? 142 ASN B ND2  1 
ATOM   3542 N N    . ARG B 1 143 ? 97.59500  108.68800 118.51500 1.000 26.35252  ? 143 ARG B N    1 
ATOM   3543 C CA   . ARG B 1 143 ? 98.27100  108.54700 119.80100 1.000 12.61874  ? 143 ARG B CA   1 
ATOM   3544 C C    . ARG B 1 143 ? 97.29700  108.11700 120.89100 1.000 13.10619  ? 143 ARG B C    1 
ATOM   3545 O O    . ARG B 1 143 ? 97.60300  107.23400 121.70400 1.000 37.48065  ? 143 ARG B O    1 
ATOM   3546 C CB   . ARG B 1 143 ? 98.95900  109.85900 120.17800 1.000 15.27753  ? 143 ARG B CB   1 
ATOM   3547 C CG   . ARG B 1 143 ? 99.52900  109.87500 121.58800 1.000 27.53966  ? 143 ARG B CG   1 
ATOM   3548 C CD   . ARG B 1 143 ? 100.65300 110.88700 121.73000 1.000 19.30694  ? 143 ARG B CD   1 
ATOM   3549 N NE   . ARG B 1 143 ? 101.92300 110.37300 121.23200 1.000 28.42815  ? 143 ARG B NE   1 
ATOM   3550 C CZ   . ARG B 1 143 ? 103.03700 110.30500 121.94700 1.000 24.15935  ? 143 ARG B CZ   1 
ATOM   3551 N NH1  . ARG B 1 143 ? 103.07600 110.70700 123.20600 1.000 17.01318  ? 143 ARG B NH1  1 
ATOM   3552 N NH2  . ARG B 1 143 ? 104.14000 109.82100 121.38500 1.000 16.36560  ? 143 ARG B NH2  1 
ATOM   3553 N N    . ALA B 1 144 ? 96.12700  108.75900 120.94600 1.000 13.45545  ? 144 ALA B N    1 
ATOM   3554 C CA   . ALA B 1 144 ? 95.11400  108.36000 121.91900 1.000 22.08083  ? 144 ALA B CA   1 
ATOM   3555 C C    . ALA B 1 144 ? 94.76400  106.88200 121.77800 1.000 27.60588  ? 144 ALA B C    1 
ATOM   3556 O O    . ALA B 1 144 ? 94.72100  106.13900 122.77100 1.000 25.61879  ? 144 ALA B O    1 
ATOM   3557 C CB   . ALA B 1 144 ? 93.86700  109.22900 121.76200 1.000 16.63694  ? 144 ALA B CB   1 
ATOM   3558 N N    . LEU B 1 145 ? 94.48000  106.44500 120.54700 1.000 22.86008  ? 145 LEU B N    1 
ATOM   3559 C CA   . LEU B 1 145 ? 94.14400  105.04200 120.31700 1.000 14.19885  ? 145 LEU B CA   1 
ATOM   3560 C C    . LEU B 1 145 ? 95.24300  104.11700 120.82600 1.000 27.85901  ? 145 LEU B C    1 
ATOM   3561 O O    . LEU B 1 145 ? 94.97000  103.14700 121.54500 1.000 39.38461  ? 145 LEU B O    1 
ATOM   3562 C CB   . LEU B 1 145 ? 93.88700  104.79900 118.83100 1.000 22.42205  ? 145 LEU B CB   1 
ATOM   3563 C CG   . LEU B 1 145 ? 92.45200  104.99000 118.34300 1.000 34.95378  ? 145 LEU B CG   1 
ATOM   3564 C CD1  . LEU B 1 145 ? 92.40400  104.95900 116.82500 1.000 34.48223  ? 145 LEU B CD1  1 
ATOM   3565 C CD2  . LEU B 1 145 ? 91.53900  103.92800 118.93400 1.000 28.26407  ? 145 LEU B CD2  1 
ATOM   3566 N N    . GLY B 1 146 ? 96.48500  104.36600 120.40700 1.000 27.86288  ? 146 GLY B N    1 
ATOM   3567 C CA   . GLY B 1 146 ? 97.59600  103.54400 120.86700 1.000 10.16694  ? 146 GLY B CA   1 
ATOM   3568 C C    . GLY B 1 146 ? 97.67000  103.44100 122.37700 1.000 16.70287  ? 146 GLY B C    1 
ATOM   3569 O O    . GLY B 1 146 ? 97.75800  102.34200 122.93900 1.000 25.90189  ? 146 GLY B O    1 
ATOM   3570 N N    . THR B 1 147 ? 97.65900  104.59100 123.05600 1.000 15.75273  ? 147 THR B N    1 
ATOM   3571 C CA   . THR B 1 147 ? 97.78300  104.59000 124.51000 1.000 22.69220  ? 147 THR B CA   1 
ATOM   3572 C C    . THR B 1 147 ? 96.66500  103.79000 125.17000 1.000 23.99126  ? 147 THR B C    1 
ATOM   3573 O O    . THR B 1 147 ? 96.91900  102.98000 126.07200 1.000 32.55465  ? 147 THR B O    1 
ATOM   3574 C CB   . THR B 1 147 ? 97.78800  106.02500 125.03500 1.000 19.44061  ? 147 THR B CB   1 
ATOM   3575 O OG1  . THR B 1 147 ? 98.69700  106.81500 124.26000 1.000 21.16358  ? 147 THR B OG1  1 
ATOM   3576 C CG2  . THR B 1 147 ? 98.21100  106.05700 126.48900 1.000 21.97283  ? 147 THR B CG2  1 
ATOM   3577 N N    . LEU B 1 148 ? 95.42300  103.97100 124.71400 1.000 26.32422  ? 148 LEU B N    1 
ATOM   3578 C CA   . LEU B 1 148 ? 94.32200  103.28000 125.37800 1.000 24.60629  ? 148 LEU B CA   1 
ATOM   3579 C C    . LEU B 1 148 ? 94.34900  101.78200 125.10400 1.000 26.00942  ? 148 LEU B C    1 
ATOM   3580 O O    . LEU B 1 148 ? 94.09900  100.97500 126.01200 1.000 31.04136  ? 148 LEU B O    1 
ATOM   3581 C CB   . LEU B 1 148 ? 92.98400  103.87400 124.94400 1.000 32.90061  ? 148 LEU B CB   1 
ATOM   3582 C CG   . LEU B 1 148 ? 92.30200  104.77400 125.97100 1.000 33.97239  ? 148 LEU B CG   1 
ATOM   3583 C CD1  . LEU B 1 148 ? 92.99900  106.11200 126.03400 1.000 35.70416  ? 148 LEU B CD1  1 
ATOM   3584 C CD2  . LEU B 1 148 ? 90.83300  104.95000 125.64100 1.000 26.52019  ? 148 LEU B CD2  1 
ATOM   3585 N N    . SER B 1 149 ? 94.69200  101.38400 123.87700 1.000 26.71821  ? 149 SER B N    1 
ATOM   3586 C CA   . SER B 1 149 ? 94.76800  99.95900  123.58100 1.000 27.20863  ? 149 SER B CA   1 
ATOM   3587 C C    . SER B 1 149 ? 95.86800  99.28600  124.38700 1.000 24.55687  ? 149 SER B C    1 
ATOM   3588 O O    . SER B 1 149 ? 95.67600  98.17600  124.90500 1.000 29.02908  ? 149 SER B O    1 
ATOM   3589 C CB   . SER B 1 149 ? 94.99600  99.74300  122.08700 1.000 21.45735  ? 149 SER B CB   1 
ATOM   3590 O OG   . SER B 1 149 ? 93.88900  100.19700 121.33000 1.000 36.27080  ? 149 SER B OG   1 
ATOM   3591 N N    . ALA B 1 150 ? 96.98600  99.98000  124.60800 1.000 27.52066  ? 150 ALA B N    1 
ATOM   3592 C CA   . ALA B 1 150 ? 98.04100  99.31800  125.35600 1.000 21.65830  ? 150 ALA B CA   1 
ATOM   3593 C C    . ALA B 1 150 ? 97.86300  99.43500  126.85900 1.000 20.35027  ? 150 ALA B C    1 
ATOM   3594 O O    . ALA B 1 150 ? 98.38200  98.58300  127.58700 1.000 35.28434  ? 150 ALA B O    1 
ATOM   3595 C CB   . ALA B 1 150 ? 99.40700  99.88700  124.96400 1.000 19.63200  ? 150 ALA B CB   1 
ATOM   3596 N N    . GLY B 1 151 ? 96.95500  100.28700 127.32100 1.000 27.96730  ? 151 GLY B N    1 
ATOM   3597 C CA   . GLY B 1 151 ? 96.73400  100.34500 128.74900 1.000 25.06731  ? 151 GLY B CA   1 
ATOM   3598 C C    . GLY B 1 151 ? 95.72300  99.27900  129.09800 1.000 31.25056  ? 151 GLY B C    1 
ATOM   3599 O O    . GLY B 1 151 ? 95.84600  98.59800  130.12400 1.000 34.92761  ? 151 GLY B O    1 
ATOM   3600 N N    . GLY B 1 152 ? 94.77600  99.05200  128.18700 1.000 34.99074  ? 152 GLY B N    1 
ATOM   3601 C CA   . GLY B 1 152 ? 93.84700  97.95400  128.38200 1.000 28.06931  ? 152 GLY B CA   1 
ATOM   3602 C C    . GLY B 1 152 ? 94.55500  96.61400  128.33000 1.000 32.83741  ? 152 GLY B C    1 
ATOM   3603 O O    . GLY B 1 152 ? 94.34200  95.74900  129.18800 1.000 33.81793  ? 152 GLY B O    1 
ATOM   3604 N N    . LEU B 1 153 ? 95.39800  96.41500  127.31100 1.000 35.58919  ? 153 LEU B N    1 
ATOM   3605 C CA   . LEU B 1 153 ? 96.13700  95.16100  127.20600 1.000 33.49220  ? 153 LEU B CA   1 
ATOM   3606 C C    . LEU B 1 153 ? 97.01900  94.93000  128.43200 1.000 34.17647  ? 153 LEU B C    1 
ATOM   3607 O O    . LEU B 1 153 ? 97.05400  93.82100  128.98400 1.000 29.75757  ? 153 LEU B O    1 
ATOM   3608 C CB   . LEU B 1 153 ? 96.96800  95.15100  125.92300 1.000 36.29207  ? 153 LEU B CB   1 
ATOM   3609 C CG   . LEU B 1 153 ? 97.65600  93.83500  125.55800 1.000 35.37381  ? 153 LEU B CG   1 
ATOM   3610 C CD1  . LEU B 1 153 ? 96.63300  92.75300  125.27100 1.000 27.85728  ? 153 LEU B CD1  1 
ATOM   3611 C CD2  . LEU B 1 153 ? 98.56300  94.03800  124.36100 1.000 34.89703  ? 153 LEU B CD2  1 
ATOM   3612 N N    . ALA B 1 154 ? 97.75700  95.96100  128.86800 1.000 37.47301  ? 154 ALA B N    1 
ATOM   3613 C CA   . ALA B 1 154 ? 98.63200  95.79200  130.02400 1.000 30.86622  ? 154 ALA B CA   1 
ATOM   3614 C C    . ALA B 1 154 ? 97.83900  95.42200  131.27200 1.000 29.73103  ? 154 ALA B C    1 
ATOM   3615 O O    . ALA B 1 154 ? 98.23000  94.51800  132.02100 1.000 31.68039  ? 154 ALA B O    1 
ATOM   3616 C CB   . ALA B 1 154 ? 99.44500  97.06400  130.25700 1.000 29.17331  ? 154 ALA B CB   1 
ATOM   3617 N N    . LEU B 1 155 ? 96.72600  96.11800  131.52500 1.000 41.84886  ? 155 LEU B N    1 
ATOM   3618 C CA   . LEU B 1 155 ? 95.89900  95.77900  132.68000 1.000 41.25218  ? 155 LEU B CA   1 
ATOM   3619 C C    . LEU B 1 155 ? 95.40700  94.33800  132.60800 1.000 40.18628  ? 155 LEU B C    1 
ATOM   3620 O O    . LEU B 1 155 ? 95.49100  93.58900  133.59100 1.000 41.02689  ? 155 LEU B O    1 
ATOM   3621 C CB   . LEU B 1 155 ? 94.72000  96.74600  132.78400 1.000 42.56372  ? 155 LEU B CB   1 
ATOM   3622 C CG   . LEU B 1 155 ? 94.80100  97.82400  133.86700 1.000 40.32018  ? 155 LEU B CG   1 
ATOM   3623 C CD1  . LEU B 1 155 ? 96.14800  98.52300  133.84400 1.000 40.32387  ? 155 LEU B CD1  1 
ATOM   3624 C CD2  . LEU B 1 155 ? 93.67500  98.82800  133.69600 1.000 42.34884  ? 155 LEU B CD2  1 
ATOM   3625 N N    . GLY B 1 156 ? 94.87300  93.93700  131.45300 1.000 45.76861  ? 156 GLY B N    1 
ATOM   3626 C CA   . GLY B 1 156 ? 94.37800  92.57600  131.31700 1.000 41.71512  ? 156 GLY B CA   1 
ATOM   3627 C C    . GLY B 1 156 ? 95.44100  91.53100  131.59600 1.000 46.48595  ? 156 GLY B C    1 
ATOM   3628 O O    . GLY B 1 156 ? 95.19700  90.55100  132.30400 1.000 47.14737  ? 156 GLY B O    1 
ATOM   3629 N N    . MET B 1 157 ? 96.64000  91.72500  131.03900 1.000 49.95710  ? 157 MET B N    1 
ATOM   3630 C CA   . MET B 1 157 ? 97.70900  90.75500  131.26200 1.000 46.38157  ? 157 MET B CA   1 
ATOM   3631 C C    . MET B 1 157 ? 98.15300  90.73600  132.72100 1.000 49.19145  ? 157 MET B C    1 
ATOM   3632 O O    . MET B 1 157 ? 98.39500  89.66300  133.28900 1.000 48.72642  ? 157 MET B O    1 
ATOM   3633 C CB   . MET B 1 157 ? 98.89100  91.04900  130.34200 1.000 45.94205  ? 157 MET B CB   1 
ATOM   3634 C CG   . MET B 1 157 ? 98.58700  90.83200  128.87100 1.000 49.83108  ? 157 MET B CG   1 
ATOM   3635 S SD   . MET B 1 157 ? 98.67000  89.09600  128.39300 1.000 57.93159  ? 157 MET B SD   1 
ATOM   3636 C CE   . MET B 1 157 ? 99.32400  89.23300  126.73200 1.000 49.81030  ? 157 MET B CE   1 
ATOM   3637 N N    . ALA B 1 158 ? 98.28100  91.91300  133.34000 1.000 52.02813  ? 158 ALA B N    1 
ATOM   3638 C CA   . ALA B 1 158 ? 98.66300  91.96100  134.74600 1.000 43.84275  ? 158 ALA B CA   1 
ATOM   3639 C C    . ALA B 1 158 ? 97.66400  91.20900  135.61400 1.000 48.84307  ? 158 ALA B C    1 
ATOM   3640 O O    . ALA B 1 158 ? 98.05400  90.51000  136.55600 1.000 55.50027  ? 158 ALA B O    1 
ATOM   3641 C CB   . ALA B 1 158 ? 98.78900  93.41200  135.20800 1.000 46.92435  ? 158 ALA B CB   1 
ATOM   3642 N N    . GLU B 1 159 ? 96.37000  91.34100  135.31800 1.000 55.54325  ? 159 GLU B N    1 
ATOM   3643 C CA   . GLU B 1 159 ? 95.37700  90.55700  136.05000 1.000 57.48033  ? 159 GLU B CA   1 
ATOM   3644 C C    . GLU B 1 159 ? 95.54800  89.06500  135.78700 1.000 56.13725  ? 159 GLU B C    1 
ATOM   3645 O O    . GLU B 1 159 ? 95.64600  88.26400  136.72300 1.000 55.89221  ? 159 GLU B O    1 
ATOM   3646 C CB   . GLU B 1 159 ? 93.96100  91.00900  135.69100 1.000 59.61259  ? 159 GLU B CB   1 
ATOM   3647 C CG   . GLU B 1 159 ? 93.80900  92.50100  135.45600 1.000 61.30270  ? 159 GLU B CG   1 
ATOM   3648 C CD   . GLU B 1 159 ? 94.30400  93.33300  136.62200 1.000 63.82703  ? 159 GLU B CD   1 
ATOM   3649 O OE1  . GLU B 1 159 ? 93.93700  93.02100  137.77500 1.000 61.70799  ? 159 GLU B OE1  1 
ATOM   3650 O OE2  . GLU B 1 159 ? 95.05800  94.30000  136.38600 1.000 61.50282  ? 159 GLU B OE2  1 
ATOM   3651 N N    . LEU B 1 160 ? 95.58400  88.67100  134.51100 1.000 58.02822  ? 160 LEU B N    1 
ATOM   3652 C CA   . LEU B 1 160 ? 95.62800  87.25300  134.16400 1.000 59.22506  ? 160 LEU B CA   1 
ATOM   3653 C C    . LEU B 1 160 ? 96.88300  86.54800  134.66600 1.000 57.95410  ? 160 LEU B C    1 
ATOM   3654 O O    . LEU B 1 160 ? 96.88600  85.31700  134.76600 1.000 54.49178  ? 160 LEU B O    1 
ATOM   3655 C CB   . LEU B 1 160 ? 95.52300  87.08500  132.64800 1.000 59.89003  ? 160 LEU B CB   1 
ATOM   3656 C CG   . LEU B 1 160 ? 95.67400  85.65900  132.11800 1.000 56.85969  ? 160 LEU B CG   1 
ATOM   3657 C CD1  . LEU B 1 160 ? 94.31400  85.05000  131.82700 1.000 57.29485  ? 160 LEU B CD1  1 
ATOM   3658 C CD2  . LEU B 1 160 ? 96.55300  85.63800  130.87900 1.000 57.31068  ? 160 LEU B CD2  1 
ATOM   3659 N N    . SER B 1 161 ? 97.94700  87.28900  134.98300 1.000 66.66006  ? 161 SER B N    1 
ATOM   3660 C CA   . SER B 1 161 ? 99.19000  86.63800  135.39500 1.000 66.06523  ? 161 SER B CA   1 
ATOM   3661 C C    . SER B 1 161 ? 99.02100  85.85800  136.69600 1.000 67.74512  ? 161 SER B C    1 
ATOM   3662 O O    . SER B 1 161 ? 99.61600  84.78800  136.86700 1.000 67.86791  ? 161 SER B O    1 
ATOM   3663 C CB   . SER B 1 161 ? 100.30300 87.67500  135.53900 1.000 64.05276  ? 161 SER B CB   1 
ATOM   3664 O OG   . SER B 1 161 ? 100.34400 88.19900  136.85500 1.000 62.40256  ? 161 SER B OG   1 
ATOM   3665 N N    . THR B 1 162 ? 98.21900  86.38000  137.62600 1.000 74.54024  ? 162 THR B N    1 
ATOM   3666 C CA   . THR B 1 162 ? 98.08800  85.77400  138.94900 1.000 74.70470  ? 162 THR B CA   1 
ATOM   3667 C C    . THR B 1 162 ? 97.50200  84.36400  138.92500 1.000 73.10593  ? 162 THR B C    1 
ATOM   3668 O O    . THR B 1 162 ? 97.63800  83.64200  139.91900 1.000 71.39693  ? 162 THR B O    1 
ATOM   3669 C CB   . THR B 1 162 ? 97.22900  86.66200  139.84900 1.000 74.67029  ? 162 THR B CB   1 
ATOM   3670 O OG1  . THR B 1 162 ? 95.85200  86.54000  139.46900 1.000 73.30083  ? 162 THR B OG1  1 
ATOM   3671 C CG2  . THR B 1 162 ? 97.65800  88.11500  139.72900 1.000 72.19198  ? 162 THR B CG2  1 
ATOM   3672 N N    . LEU B 1 163 ? 96.85100  83.95600  137.83300 1.000 72.40335  ? 163 LEU B N    1 
ATOM   3673 C CA   . LEU B 1 163 ? 96.14100  82.67700  137.82900 1.000 72.90170  ? 163 LEU B CA   1 
ATOM   3674 C C    . LEU B 1 163 ? 97.03500  81.52500  138.27700 1.000 75.25541  ? 163 LEU B C    1 
ATOM   3675 O O    . LEU B 1 163 ? 96.68000  80.76700  139.18600 1.000 75.87586  ? 163 LEU B O    1 
ATOM   3676 C CB   . LEU B 1 163 ? 95.57100  82.39600  136.43800 1.000 73.58035  ? 163 LEU B CB   1 
ATOM   3677 C CG   . LEU B 1 163 ? 94.52900  83.37900  135.90700 1.000 77.41193  ? 163 LEU B CG   1 
ATOM   3678 C CD1  . LEU B 1 163 ? 93.80000  82.78100  134.71500 1.000 73.01300  ? 163 LEU B CD1  1 
ATOM   3679 C CD2  . LEU B 1 163 ? 93.54700  83.76300  137.00300 1.000 75.60292  ? 163 LEU B CD2  1 
ATOM   3680 N N    . PHE B 1 164 ? 98.20100  81.37700  137.65400 1.000 79.37621  ? 164 PHE B N    1 
ATOM   3681 C CA   . PHE B 1 164 ? 99.15100  80.32500  138.00800 1.000 79.04111  ? 164 PHE B CA   1 
ATOM   3682 C C    . PHE B 1 164 ? 100.26600 80.91700  138.86500 1.000 80.15347  ? 164 PHE B C    1 
ATOM   3683 O O    . PHE B 1 164 ? 101.05600 81.74100  138.39500 1.000 78.53935  ? 164 PHE B O    1 
ATOM   3684 C CB   . PHE B 1 164 ? 99.68300  79.62400  136.75600 1.000 76.82608  ? 164 PHE B CB   1 
ATOM   3685 C CG   . PHE B 1 164 ? 99.94800  80.54400  135.59100 1.000 78.58790  ? 164 PHE B CG   1 
ATOM   3686 C CD1  . PHE B 1 164 ? 100.76900 81.64900  135.71400 1.000 78.08661  ? 164 PHE B CD1  1 
ATOM   3687 C CD2  . PHE B 1 164 ? 99.36400  80.29000  134.36100 1.000 78.97701  ? 164 PHE B CD2  1 
ATOM   3688 C CE1  . PHE B 1 164 ? 101.00000 82.48100  134.63800 1.000 77.94228  ? 164 PHE B CE1  1 
ATOM   3689 C CE2  . PHE B 1 164 ? 99.59300  81.11800  133.28200 1.000 75.22285  ? 164 PHE B CE2  1 
ATOM   3690 C CZ   . PHE B 1 164 ? 100.41100 82.21400  133.42000 1.000 76.42984  ? 164 PHE B CZ   1 
ATOM   3691 N N    . GLY B 1 165 ? 100.31900 80.50400  140.12800 1.000 87.28005  ? 165 GLY B N    1 
ATOM   3692 C CA   . GLY B 1 165 ? 101.32800 81.01200  141.03200 1.000 87.35277  ? 165 GLY B CA   1 
ATOM   3693 C C    . GLY B 1 165 ? 102.72400 80.51200  140.71600 1.000 87.75907  ? 165 GLY B C    1 
ATOM   3694 O O    . GLY B 1 165 ? 102.94000 79.56600  139.96000 1.000 87.11379  ? 165 GLY B O    1 
ATOM   3695 N N    . ASP B 1 166 ? 103.69400 81.18600  141.33200 1.000 90.40577  ? 166 ASP B N    1 
ATOM   3696 C CA   . ASP B 1 166 ? 105.11900 80.93300  141.15100 1.000 91.57460  ? 166 ASP B CA   1 
ATOM   3697 C C    . ASP B 1 166 ? 105.59800 81.41900  139.78700 1.000 91.43443  ? 166 ASP B C    1 
ATOM   3698 O O    . ASP B 1 166 ? 106.76200 81.80000  139.63100 1.000 89.07815  ? 166 ASP B O    1 
ATOM   3699 C CB   . ASP B 1 166 ? 105.42600 79.44300  141.32100 1.000 88.66235  ? 166 ASP B CB   1 
ATOM   3700 N N    . TRP B 1 167 ? 104.70800 81.41100  138.79400 1.000 88.77124  ? 167 TRP B N    1 
ATOM   3701 C CA   . TRP B 1 167 ? 105.00300 81.97700  137.47700 1.000 86.57438  ? 167 TRP B CA   1 
ATOM   3702 C C    . TRP B 1 167 ? 104.66500 83.46900  137.46800 1.000 86.27049  ? 167 TRP B C    1 
ATOM   3703 O O    . TRP B 1 167 ? 103.74600 83.93700  136.79500 1.000 86.45625  ? 167 TRP B O    1 
ATOM   3704 C CB   . TRP B 1 167 ? 104.27100 81.20900  136.38500 1.000 87.16286  ? 167 TRP B CB   1 
ATOM   3705 C CG   . TRP B 1 167 ? 104.97100 79.94000  135.98700 1.000 87.79536  ? 167 TRP B CG   1 
ATOM   3706 C CD1  . TRP B 1 167 ? 105.70900 79.73700  134.85700 1.000 87.17473  ? 167 TRP B CD1  1 
ATOM   3707 C CD2  . TRP B 1 167 ? 105.02700 78.71300  136.72600 1.000 89.66622  ? 167 TRP B CD2  1 
ATOM   3708 N NE1  . TRP B 1 167 ? 106.20700 78.45800  134.83800 1.000 88.50298  ? 167 TRP B NE1  1 
ATOM   3709 C CE2  . TRP B 1 167 ? 105.80300 77.80800  135.97400 1.000 89.46656  ? 167 TRP B CE2  1 
ATOM   3710 C CE3  . TRP B 1 167 ? 104.49000 78.28800  137.94400 1.000 88.74625  ? 167 TRP B CE3  1 
ATOM   3711 C CZ2  . TRP B 1 167 ? 106.05600 76.50600  136.40100 1.000 87.30379  ? 167 TRP B CZ2  1 
ATOM   3712 C CZ3  . TRP B 1 167 ? 104.74200 76.99600  138.36600 1.000 88.45875  ? 167 TRP B CZ3  1 
ATOM   3713 C CH2  . TRP B 1 167 ? 105.51800 76.12000  137.59700 1.000 86.54220  ? 167 TRP B CH2  1 
ATOM   3714 N N    . GLU B 1 168 ? 105.44000 84.21800  138.24400 1.000 84.38954  ? 168 GLU B N    1 
ATOM   3715 C CA   . GLU B 1 168 ? 105.34700 85.66900  138.27700 1.000 84.54462  ? 168 GLU B CA   1 
ATOM   3716 C C    . GLU B 1 168 ? 106.74600 86.23700  138.12000 1.000 84.47923  ? 168 GLU B C    1 
ATOM   3717 O O    . GLU B 1 168 ? 107.69000 85.75800  138.75200 1.000 86.33005  ? 168 GLU B O    1 
ATOM   3718 C CB   . GLU B 1 168 ? 104.70600 86.17500  139.57400 1.000 86.52539  ? 168 GLU B CB   1 
ATOM   3719 C CG   . GLU B 1 168 ? 103.23700 85.81700  139.72000 1.000 86.21353  ? 168 GLU B CG   1 
ATOM   3720 C CD   . GLU B 1 168 ? 102.65600 86.27800  141.04000 1.000 88.02081  ? 168 GLU B CD   1 
ATOM   3721 O OE1  . GLU B 1 168 ? 103.43600 86.70700  141.91600 1.000 86.69587  ? 168 GLU B OE1  1 
ATOM   3722 O OE2  . GLU B 1 168 ? 101.42000 86.21300  141.20200 1.000 88.43272  ? 168 GLU B OE2  1 
ATOM   3723 N N    . GLU B 1 169 ? 106.86200 87.25700  137.27400 1.000 73.70083  ? 169 GLU B N    1 
ATOM   3724 C CA   . GLU B 1 169 ? 108.08500 87.88800  136.77600 1.000 75.02642  ? 169 GLU B CA   1 
ATOM   3725 C C    . GLU B 1 169 ? 108.70700 86.99800  135.70600 1.000 77.45726  ? 169 GLU B C    1 
ATOM   3726 O O    . GLU B 1 169 ? 109.70500 87.39600  135.09300 1.000 74.93818  ? 169 GLU B O    1 
ATOM   3727 C CB   . GLU B 1 169 ? 109.12800 88.21100  137.86200 1.000 76.33687  ? 169 GLU B CB   1 
ATOM   3728 C CG   . GLU B 1 169 ? 109.91000 87.03400  138.41700 1.000 76.53365  ? 169 GLU B CG   1 
ATOM   3729 C CD   . GLU B 1 169 ? 110.72900 87.41000  139.63600 1.000 77.57560  ? 169 GLU B CD   1 
ATOM   3730 O OE1  . GLU B 1 169 ? 111.30800 88.51600  139.64700 1.000 75.28986  ? 169 GLU B OE1  1 
ATOM   3731 O OE2  . GLU B 1 169 ? 110.79000 86.60000  140.58600 1.000 76.62069  ? 169 GLU B OE2  1 
ATOM   3732 N N    . ILE B 1 170 ? 108.15500 85.81000  135.46200 1.000 69.20910  ? 170 ILE B N    1 
ATOM   3733 C CA   . ILE B 1 170 ? 108.55100 84.97400  134.34100 1.000 66.31003  ? 170 ILE B CA   1 
ATOM   3734 C C    . ILE B 1 170 ? 107.47800 84.95600  133.26000 1.000 64.43249  ? 170 ILE B C    1 
ATOM   3735 O O    . ILE B 1 170 ? 107.78300 85.09900  132.07300 1.000 65.88825  ? 170 ILE B O    1 
ATOM   3736 C CB   . ILE B 1 170 ? 108.87300 83.54000  134.81700 1.000 67.81674  ? 170 ILE B CB   1 
ATOM   3737 C CG1  . ILE B 1 170 ? 110.13300 83.53200  135.68400 1.000 66.82053  ? 170 ILE B CG1  1 
ATOM   3738 C CG2  . ILE B 1 170 ? 109.02600 82.60200  133.62800 1.000 62.91506  ? 170 ILE B CG2  1 
ATOM   3739 C CD1  . ILE B 1 170 ? 110.71600 82.15300  135.89500 1.000 65.25662  ? 170 ILE B CD1  1 
ATOM   3740 N N    . PHE B 1 171 ? 106.20800 84.90100  133.66300 1.000 65.76244  ? 171 PHE B N    1 
ATOM   3741 C CA   . PHE B 1 171 ? 105.11400 84.99300  132.70900 1.000 61.75102  ? 171 PHE B CA   1 
ATOM   3742 C C    . PHE B 1 171 ? 104.83100 86.43600  132.32700 1.000 59.35812  ? 171 PHE B C    1 
ATOM   3743 O O    . PHE B 1 171 ? 104.12500 86.68100  131.34300 1.000 59.72656  ? 171 PHE B O    1 
ATOM   3744 C CB   . PHE B 1 171 ? 103.85600 84.33500  133.28700 1.000 59.33052  ? 171 PHE B CB   1 
ATOM   3745 C CG   . PHE B 1 171 ? 102.60000 84.64900  132.52800 1.000 64.45843  ? 171 PHE B CG   1 
ATOM   3746 C CD1  . PHE B 1 171 ? 102.37100 84.09100  131.28400 1.000 63.87582  ? 171 PHE B CD1  1 
ATOM   3747 C CD2  . PHE B 1 171 ? 101.65200 85.50800  133.05600 1.000 66.43303  ? 171 PHE B CD2  1 
ATOM   3748 C CE1  . PHE B 1 171 ? 101.21700 84.38100  130.58100 1.000 61.64792  ? 171 PHE B CE1  1 
ATOM   3749 C CE2  . PHE B 1 171 ? 100.49800 85.80200  132.35700 1.000 64.99613  ? 171 PHE B CE2  1 
ATOM   3750 C CZ   . PHE B 1 171 ? 100.28100 85.23700  131.11800 1.000 62.32376  ? 171 PHE B CZ   1 
ATOM   3751 N N    . CYS B 1 172 ? 105.39200 87.38800  133.07000 1.000 53.85543  ? 172 CYS B N    1 
ATOM   3752 C CA   . CYS B 1 172 ? 105.34300 88.79500  132.71000 1.000 53.56924  ? 172 CYS B CA   1 
ATOM   3753 C C    . CYS B 1 172 ? 106.51200 89.17800  131.81900 1.000 55.22901  ? 172 CYS B C    1 
ATOM   3754 O O    . CYS B 1 172 ? 106.39500 90.11100  131.01700 1.000 55.19731  ? 172 CYS B O    1 
ATOM   3755 C CB   . CYS B 1 172 ? 105.34300 89.66600  133.96800 1.000 53.94042  ? 172 CYS B CB   1 
ATOM   3756 S SG   . CYS B 1 172 ? 103.69700 90.12600  134.55800 1.000 65.28919  ? 172 CYS B SG   1 
ATOM   3757 N N    . THR B 1 173 ? 107.63200 88.46600  131.94500 1.000 52.40887  ? 173 THR B N    1 
ATOM   3758 C CA   . THR B 1 173 ? 108.80300 88.68600  131.11000 1.000 47.68377  ? 173 THR B CA   1 
ATOM   3759 C C    . THR B 1 173 ? 108.75700 87.89200  129.81300 1.000 47.31549  ? 173 THR B C    1 
ATOM   3760 O O    . THR B 1 173 ? 109.51500 88.20200  128.88800 1.000 50.76040  ? 173 THR B O    1 
ATOM   3761 C CB   . THR B 1 173 ? 110.07800 88.31700  131.87500 1.000 51.49531  ? 173 THR B CB   1 
ATOM   3762 O OG1  . THR B 1 173 ? 109.92500 88.65900  133.25800 1.000 56.01662  ? 173 THR B OG1  1 
ATOM   3763 C CG2  . THR B 1 173 ? 111.28000 89.05100  131.30300 1.000 50.03540  ? 173 THR B CG2  1 
ATOM   3764 N N    . LEU B 1 174 ? 107.89000 86.88300  129.72400 1.000 42.64265  ? 174 LEU B N    1 
ATOM   3765 C CA   . LEU B 1 174 ? 107.69500 86.16300  128.47300 1.000 36.75150  ? 174 LEU B CA   1 
ATOM   3766 C C    . LEU B 1 174 ? 106.65400 86.80400  127.56700 1.000 36.38207  ? 174 LEU B C    1 
ATOM   3767 O O    . LEU B 1 174 ? 106.54900 86.41100  126.40100 1.000 40.33518  ? 174 LEU B O    1 
ATOM   3768 C CB   . LEU B 1 174 ? 107.28000 84.71500  128.75600 1.000 43.94856  ? 174 LEU B CB   1 
ATOM   3769 C CG   . LEU B 1 174 ? 108.38100 83.67900  128.97600 1.000 45.19554  ? 174 LEU B CG   1 
ATOM   3770 C CD1  . LEU B 1 174 ? 107.83200 82.48900  129.74200 1.000 44.38732  ? 174 LEU B CD1  1 
ATOM   3771 C CD2  . LEU B 1 174 ? 108.96900 83.23400  127.64900 1.000 40.92260  ? 174 LEU B CD2  1 
ATOM   3772 N N    . SER B 1 175 ? 105.88600 87.77400  128.06300 1.000 36.39735  ? 175 SER B N    1 
ATOM   3773 C CA   . SER B 1 175 ? 104.91400 88.47800  127.23600 1.000 35.11832  ? 175 SER B CA   1 
ATOM   3774 C C    . SER B 1 175 ? 105.47700 89.72900  126.57400 1.000 30.54366  ? 175 SER B C    1 
ATOM   3775 O O    . SER B 1 175 ? 104.93300 90.17100  125.55500 1.000 34.55715  ? 175 SER B O    1 
ATOM   3776 C CB   . SER B 1 175 ? 103.68800 88.85600  128.07200 1.000 36.01686  ? 175 SER B CB   1 
ATOM   3777 O OG   . SER B 1 175 ? 104.07100 89.40300  129.32100 1.000 39.07855  ? 175 SER B OG   1 
ATOM   3778 N N    . ILE B 1 176 ? 106.58200 90.27200  127.08800 1.000 25.47210  ? 176 ILE B N    1 
ATOM   3779 C CA   . ILE B 1 176 ? 107.18700 91.44200  126.46200 1.000 28.64517  ? 176 ILE B CA   1 
ATOM   3780 C C    . ILE B 1 176 ? 107.86000 91.06400  125.15200 1.000 29.05626  ? 176 ILE B C    1 
ATOM   3781 O O    . ILE B 1 176 ? 107.81700 91.83000  124.18100 1.000 27.60526  ? 176 ILE B O    1 
ATOM   3782 C CB   . ILE B 1 176 ? 108.17600 92.10700  127.43800 1.000 34.63187  ? 176 ILE B CB   1 
ATOM   3783 C CG1  . ILE B 1 176 ? 107.50100 92.34100  128.79100 1.000 33.86741  ? 176 ILE B CG1  1 
ATOM   3784 C CG2  . ILE B 1 176 ? 108.73900 93.39500  126.85300 1.000 28.72489  ? 176 ILE B CG2  1 
ATOM   3785 C CD1  . ILE B 1 176 ? 108.16600 93.39300  129.63800 1.000 26.20746  ? 176 ILE B CD1  1 
ATOM   3786 N N    . PHE B 1 177 ? 108.41200 89.85300  125.07100 1.000 23.28723  ? 177 PHE B N    1 
ATOM   3787 C CA   . PHE B 1 177 ? 109.00100 89.39400  123.81900 1.000 25.79217  ? 177 PHE B CA   1 
ATOM   3788 C C    . PHE B 1 177 ? 107.93300 89.20600  122.74900 1.000 27.66566  ? 177 PHE B C    1 
ATOM   3789 O O    . PHE B 1 177 ? 108.10800 89.63900  121.60200 1.000 29.45276  ? 177 PHE B O    1 
ATOM   3790 C CB   . PHE B 1 177 ? 109.76400 88.09100  124.07300 1.000 25.28265  ? 177 PHE B CB   1 
ATOM   3791 C CG   . PHE B 1 177 ? 110.22200 87.39400  122.82800 1.000 29.43865  ? 177 PHE B CG   1 
ATOM   3792 C CD1  . PHE B 1 177 ? 111.28300 87.88300  122.08800 1.000 30.63132  ? 177 PHE B CD1  1 
ATOM   3793 C CD2  . PHE B 1 177 ? 109.59400 86.23700  122.40200 1.000 29.34925  ? 177 PHE B CD2  1 
ATOM   3794 C CE1  . PHE B 1 177 ? 111.70000 87.23700  120.94500 1.000 29.83303  ? 177 PHE B CE1  1 
ATOM   3795 C CE2  . PHE B 1 177 ? 110.00900 85.58900  121.25900 1.000 31.06359  ? 177 PHE B CE2  1 
ATOM   3796 C CZ   . PHE B 1 177 ? 111.06400 86.09000  120.53000 1.000 30.42812  ? 177 PHE B CZ   1 
ATOM   3797 N N    . CYS B 1 178 ? 106.77600 88.66300  123.13300 1.000 28.53399  ? 178 CYS B N    1 
ATOM   3798 C CA   . CYS B 1 178 ? 105.72500 88.41200  122.15500 1.000 24.27726  ? 178 CYS B CA   1 
ATOM   3799 C C    . CYS B 1 178 ? 105.03700 89.70200  121.73800 1.000 24.98405  ? 178 CYS B C    1 
ATOM   3800 O O    . CYS B 1 178 ? 104.68900 89.86500  120.56100 1.000 29.45364  ? 178 CYS B O    1 
ATOM   3801 C CB   . CYS B 1 178 ? 104.70400 87.42600  122.71900 1.000 23.73894  ? 178 CYS B CB   1 
ATOM   3802 S SG   . CYS B 1 178 ? 105.40000 85.83900  123.23400 1.000 45.34620  ? 178 CYS B SG   1 
ATOM   3803 N N    . ILE B 1 179 ? 104.90000 90.65600  122.65900 1.000 27.50601  ? 179 ILE B N    1 
ATOM   3804 C CA   . ILE B 1 179 ? 104.27400 91.91700  122.29100 1.000 24.95820  ? 179 ILE B CA   1 
ATOM   3805 C C    . ILE B 1 179 ? 105.20800 92.74500  121.42100 1.000 24.93486  ? 179 ILE B C    1 
ATOM   3806 O O    . ILE B 1 179 ? 104.77300 93.34400  120.43100 1.000 31.10137  ? 179 ILE B O    1 
ATOM   3807 C CB   . ILE B 1 179 ? 103.82800 92.68400  123.54700 1.000 28.95510  ? 179 ILE B CB   1 
ATOM   3808 C CG1  . ILE B 1 179 ? 102.58000 92.03000  124.13800 1.000 27.99925  ? 179 ILE B CG1  1 
ATOM   3809 C CG2  . ILE B 1 179 ? 103.54800 94.13700  123.21200 1.000 28.65315  ? 179 ILE B CG2  1 
ATOM   3810 C CD1  . ILE B 1 179 ? 101.29200 92.62800  123.63700 1.000 24.17346  ? 179 ILE B CD1  1 
ATOM   3811 N N    . GLY B 1 180 ? 106.50700 92.77000  121.73600 1.000 19.84205  ? 180 GLY B N    1 
ATOM   3812 C CA   . GLY B 1 180 ? 107.42300 93.49900  120.87800 1.000 18.11420  ? 180 GLY B CA   1 
ATOM   3813 C C    . GLY B 1 180 ? 107.57400 92.86400  119.51200 1.000 22.87065  ? 180 GLY B C    1 
ATOM   3814 O O    . GLY B 1 180 ? 107.70300 93.57400  118.50700 1.000 31.99305  ? 180 GLY B O    1 
ATOM   3815 N N    . PHE B 1 181 ? 107.40500 91.54100  119.42900 1.000 27.36983  ? 181 PHE B N    1 
ATOM   3816 C CA   . PHE B 1 181 ? 107.54200 90.88200  118.13700 1.000 23.61834  ? 181 PHE B CA   1 
ATOM   3817 C C    . PHE B 1 181 ? 106.31100 91.12900  117.27600 1.000 29.93298  ? 181 PHE B C    1 
ATOM   3818 O O    . PHE B 1 181 ? 106.43000 91.48800  116.09800 1.000 32.39446  ? 181 PHE B O    1 
ATOM   3819 C CB   . PHE B 1 181 ? 107.78300 89.38300  118.33700 1.000 21.52602  ? 181 PHE B CB   1 
ATOM   3820 C CG   . PHE B 1 181 ? 107.72300 88.58000  117.06700 1.000 28.80828  ? 181 PHE B CG   1 
ATOM   3821 C CD1  . PHE B 1 181 ? 108.85800 88.38100  116.30200 1.000 33.00517  ? 181 PHE B CD1  1 
ATOM   3822 C CD2  . PHE B 1 181 ? 106.53300 88.01500  116.64300 1.000 31.22616  ? 181 PHE B CD2  1 
ATOM   3823 C CE1  . PHE B 1 181 ? 108.80600 87.64600  115.13500 1.000 29.69617  ? 181 PHE B CE1  1 
ATOM   3824 C CE2  . PHE B 1 181 ? 106.47700 87.28000  115.47800 1.000 31.18073  ? 181 PHE B CE2  1 
ATOM   3825 C CZ   . PHE B 1 181 ? 107.61500 87.09500  114.72400 1.000 28.80266  ? 181 PHE B CZ   1 
ATOM   3826 N N    . LEU B 1 182 ? 105.11800 90.97800  117.85700 1.000 28.89692  ? 182 LEU B N    1 
ATOM   3827 C CA   . LEU B 1 182 ? 103.90300 91.27600  117.10900 1.000 21.26895  ? 182 LEU B CA   1 
ATOM   3828 C C    . LEU B 1 182 ? 103.86000 92.74100  116.69000 1.000 24.02615  ? 182 LEU B C    1 
ATOM   3829 O O    . LEU B 1 182 ? 103.49200 93.05400  115.55200 1.000 32.32481  ? 182 LEU B O    1 
ATOM   3830 C CB   . LEU B 1 182 ? 102.66900 90.90500  117.93100 1.000 25.58931  ? 182 LEU B CB   1 
ATOM   3831 C CG   . LEU B 1 182 ? 102.50000 89.41000  118.21900 1.000 35.70018  ? 182 LEU B CG   1 
ATOM   3832 C CD1  . LEU B 1 182 ? 101.32900 89.15100  119.15700 1.000 31.07499  ? 182 LEU B CD1  1 
ATOM   3833 C CD2  . LEU B 1 182 ? 102.32900 88.63500  116.92100 1.000 31.85725  ? 182 LEU B CD2  1 
ATOM   3834 N N    . ALA B 1 183 ? 104.23200 93.65600  117.59100 1.000 21.60729  ? 183 ALA B N    1 
ATOM   3835 C CA   . ALA B 1 183 ? 104.21300 95.07600  117.25600 1.000 23.32055  ? 183 ALA B CA   1 
ATOM   3836 C C    . ALA B 1 183 ? 105.16000 95.39600  116.10500 1.000 31.16590  ? 183 ALA B C    1 
ATOM   3837 O O    . ALA B 1 183 ? 104.78100 96.09400  115.15700 1.000 38.62506  ? 183 ALA B O    1 
ATOM   3838 C CB   . ALA B 1 183 ? 104.56400 95.90700  118.49100 1.000 21.46146  ? 183 ALA B CB   1 
ATOM   3839 N N    . THR B 1 184 ? 106.39500 94.88200  116.14800 1.000 25.39903  ? 184 THR B N    1 
ATOM   3840 C CA   . THR B 1 184 ? 107.32100 95.19700  115.06300 1.000 27.99101  ? 184 THR B CA   1 
ATOM   3841 C C    . THR B 1 184 ? 106.86000 94.57900  113.74500 1.000 31.19583  ? 184 THR B C    1 
ATOM   3842 O O    . THR B 1 184 ? 106.90400 95.23400  112.68700 1.000 32.98118  ? 184 THR B O    1 
ATOM   3843 C CB   . THR B 1 184 ? 108.72900 94.72100  115.42100 1.000 30.87991  ? 184 THR B CB   1 
ATOM   3844 O OG1  . THR B 1 184 ? 109.10100 95.24900  116.69900 1.000 28.61004  ? 184 THR B OG1  1 
ATOM   3845 C CG2  . THR B 1 184 ? 109.73300 95.20200  114.38700 1.000 26.04533  ? 184 THR B CG2  1 
ATOM   3846 N N    . PHE B 1 185 ? 106.37400 93.33300  113.78900 1.000 31.80583  ? 185 PHE B N    1 
ATOM   3847 C CA   . PHE B 1 185 ? 105.94600 92.69300  112.55300 1.000 28.59838  ? 185 PHE B CA   1 
ATOM   3848 C C    . PHE B 1 185 ? 104.77200 93.44500  111.94400 1.000 29.49746  ? 185 PHE B C    1 
ATOM   3849 O O    . PHE B 1 185 ? 104.72900 93.66100  110.72800 1.000 39.01930  ? 185 PHE B O    1 
ATOM   3850 C CB   . PHE B 1 185 ? 105.58300 91.23000  112.82500 1.000 33.35903  ? 185 PHE B CB   1 
ATOM   3851 C CG   . PHE B 1 185 ? 105.53200 90.36900  111.58900 1.000 36.48407  ? 185 PHE B CG   1 
ATOM   3852 C CD1  . PHE B 1 185 ? 106.67800 90.11600  110.85400 1.000 33.86839  ? 185 PHE B CD1  1 
ATOM   3853 C CD2  . PHE B 1 185 ? 104.34100 89.79700  111.17600 1.000 36.76823  ? 185 PHE B CD2  1 
ATOM   3854 C CE1  . PHE B 1 185 ? 106.63400 89.31900  109.72300 1.000 30.73863  ? 185 PHE B CE1  1 
ATOM   3855 C CE2  . PHE B 1 185 ? 104.29200 89.00100  110.04800 1.000 37.63006  ? 185 PHE B CE2  1 
ATOM   3856 C CZ   . PHE B 1 185 ? 105.43800 88.76200  109.32000 1.000 37.35084  ? 185 PHE B CZ   1 
ATOM   3857 N N    . MET B 1 186 ? 103.81000 93.86300  112.77300 1.000 35.61304  ? 186 MET B N    1 
ATOM   3858 C CA   . MET B 1 186 ? 102.69000 94.64000  112.26400 1.000 32.54271  ? 186 MET B CA   1 
ATOM   3859 C C    . MET B 1 186 ? 103.11500 96.02800  111.80200 1.000 33.75398  ? 186 MET B C    1 
ATOM   3860 O O    . MET B 1 186 ? 102.44400 96.61300  110.94700 1.000 33.96648  ? 186 MET B O    1 
ATOM   3861 C CB   . MET B 1 186 ? 101.60600 94.75300  113.33400 1.000 34.93809  ? 186 MET B CB   1 
ATOM   3862 C CG   . MET B 1 186 ? 100.81300 93.47500  113.53700 1.000 39.27789  ? 186 MET B CG   1 
ATOM   3863 S SD   . MET B 1 186 ? 100.38900 92.67100  111.98200 1.000 63.94690  ? 186 MET B SD   1 
ATOM   3864 C CE   . MET B 1 186 ? 100.69800 90.95600  112.38700 1.000 40.94369  ? 186 MET B CE   1 
ATOM   3865 N N    . LYS B 1 187 ? 104.21400 96.56500  112.34000 1.000 32.20100  ? 187 LYS B N    1 
ATOM   3866 C CA   . LYS B 1 187 ? 104.63200 97.90400  111.95000 1.000 31.82028  ? 187 LYS B CA   1 
ATOM   3867 C C    . LYS B 1 187 ? 105.43800 97.90700  110.66100 1.000 38.38261  ? 187 LYS B C    1 
ATOM   3868 O O    . LYS B 1 187 ? 105.58500 98.97000  110.05000 1.000 33.69263  ? 187 LYS B O    1 
ATOM   3869 C CB   . LYS B 1 187 ? 105.45400 98.57000  113.06200 1.000 33.90112  ? 187 LYS B CB   1 
ATOM   3870 C CG   . LYS B 1 187 ? 106.54700 99.51100  112.54900 1.000 37.97261  ? 187 LYS B CG   1 
ATOM   3871 C CD   . LYS B 1 187 ? 107.53800 99.91800  113.63700 1.000 36.77623  ? 187 LYS B CD   1 
ATOM   3872 C CE   . LYS B 1 187 ? 107.08500 101.14600 114.41000 1.000 38.55609  ? 187 LYS B CE   1 
ATOM   3873 N NZ   . LYS B 1 187 ? 108.24200 101.85800 115.02600 1.000 37.27775  ? 187 LYS B NZ   1 
ATOM   3874 N N    . LEU B 1 188 ? 105.91400 96.74600  110.20000 1.000 44.89146  ? 188 LEU B N    1 
ATOM   3875 C CA   . LEU B 1 188 ? 106.75100 96.74000  109.00100 1.000 42.61295  ? 188 LEU B CA   1 
ATOM   3876 C C    . LEU B 1 188 ? 105.97700 96.55900  107.69500 1.000 47.37313  ? 188 LEU B C    1 
ATOM   3877 O O    . LEU B 1 188 ? 106.58800 96.64800  106.62400 1.000 44.45796  ? 188 LEU B O    1 
ATOM   3878 C CB   . LEU B 1 188 ? 107.80700 95.63200  109.10000 1.000 41.30392  ? 188 LEU B CB   1 
ATOM   3879 C CG   . LEU B 1 188 ? 108.86000 95.74900  110.20400 1.000 43.79701  ? 188 LEU B CG   1 
ATOM   3880 C CD1  . LEU B 1 188 ? 109.89600 94.64200  110.09700 1.000 40.35727  ? 188 LEU B CD1  1 
ATOM   3881 C CD2  . LEU B 1 188 ? 109.52800 97.11500  110.17600 1.000 40.54444  ? 188 LEU B CD2  1 
ATOM   3882 N N    . TYR B 1 189 ? 104.67000 96.29700  107.74100 1.000 58.29044  ? 189 TYR B N    1 
ATOM   3883 C CA   . TYR B 1 189 ? 103.88400 96.22700  106.51400 1.000 54.80735  ? 189 TYR B CA   1 
ATOM   3884 C C    . TYR B 1 189 ? 103.73000 97.58300  105.82400 1.000 61.21053  ? 189 TYR B C    1 
ATOM   3885 O O    . TYR B 1 189 ? 103.63200 98.62300  106.47900 1.000 59.93828  ? 189 TYR B O    1 
ATOM   3886 C CB   . TYR B 1 189 ? 102.51400 95.61600  106.77700 1.000 54.19738  ? 189 TYR B CB   1 
ATOM   3887 C CG   . TYR B 1 189 ? 102.46100 94.15600  106.41600 1.000 58.54020  ? 189 TYR B CG   1 
ATOM   3888 C CD1  . TYR B 1 189 ? 102.46400 93.78100  105.08000 1.000 62.58263  ? 189 TYR B CD1  1 
ATOM   3889 C CD2  . TYR B 1 189 ? 102.35100 93.16300  107.37800 1.000 59.05209  ? 189 TYR B CD2  1 
ATOM   3890 C CE1  . TYR B 1 189 ? 102.39100 92.47000  104.70700 1.000 62.37795  ? 189 TYR B CE1  1 
ATOM   3891 C CE2  . TYR B 1 189 ? 102.29100 91.83300  107.01000 1.000 61.83590  ? 189 TYR B CE2  1 
ATOM   3892 C CZ   . TYR B 1 189 ? 102.31200 91.50100  105.67000 1.000 64.63050  ? 189 TYR B CZ   1 
ATOM   3893 O OH   . TYR B 1 189 ? 102.25000 90.19500  105.27200 1.000 63.53410  ? 189 TYR B OH   1 
ATOM   3894 N N    . PRO B 1 190 ? 103.70100 97.58200  104.48700 1.000 65.52310  ? 190 PRO B N    1 
ATOM   3895 C CA   . PRO B 1 190 ? 103.62900 98.84700  103.73600 1.000 63.87965  ? 190 PRO B CA   1 
ATOM   3896 C C    . PRO B 1 190 ? 102.32100 99.59900  103.91100 1.000 60.97497  ? 190 PRO B C    1 
ATOM   3897 O O    . PRO B 1 190 ? 102.31900 100.83500 103.85800 1.000 62.35345  ? 190 PRO B O    1 
ATOM   3898 C CB   . PRO B 1 190 ? 103.82700 98.40100  102.27900 1.000 60.98279  ? 190 PRO B CB   1 
ATOM   3899 C CG   . PRO B 1 190 ? 104.44900 97.03900  102.36900 1.000 62.31124  ? 190 PRO B CG   1 
ATOM   3900 C CD   . PRO B 1 190 ? 103.88100 96.42200  103.60200 1.000 60.90816  ? 190 PRO B CD   1 
ATOM   3901 N N    . SER B 1 191 ? 101.20700 98.89600  104.12300 1.000 57.57785  ? 191 SER B N    1 
ATOM   3902 C CA   . SER B 1 191 ? 99.93400  99.58400  104.31600 1.000 58.25937  ? 191 SER B CA   1 
ATOM   3903 C C    . SER B 1 191 ? 99.95200  100.44300 105.57200 1.000 62.25359  ? 191 SER B C    1 
ATOM   3904 O O    . SER B 1 191 ? 99.41400  101.55500 105.57700 1.000 60.46423  ? 191 SER B O    1 
ATOM   3905 C CB   . SER B 1 191 ? 98.78400  98.57500  104.38000 1.000 59.28203  ? 191 SER B CB   1 
ATOM   3906 O OG   . SER B 1 191 ? 98.89700  97.71600  105.50100 1.000 65.07593  ? 191 SER B OG   1 
ATOM   3907 N N    . MET B 1 192 ? 100.56800 99.95300  106.64200 1.000 64.33251  ? 192 MET B N    1 
ATOM   3908 C CA   . MET B 1 192 ? 100.56400 100.67200 107.91500 1.000 58.20807  ? 192 MET B CA   1 
ATOM   3909 C C    . MET B 1 192 ? 101.75800 101.61300 108.05900 1.000 59.86973  ? 192 MET B C    1 
ATOM   3910 O O    . MET B 1 192 ? 102.46200 101.58500 109.06500 1.000 61.72867  ? 192 MET B O    1 
ATOM   3911 C CB   . MET B 1 192 ? 100.52300 99.67600  109.06700 1.000 55.01594  ? 192 MET B CB   1 
ATOM   3912 C CG   . MET B 1 192 ? 99.23200  98.89000  109.16500 1.000 52.66462  ? 192 MET B CG   1 
ATOM   3913 S SD   . MET B 1 192 ? 99.29400  97.67700  110.49200 1.000 77.81983  ? 192 MET B SD   1 
ATOM   3914 C CE   . MET B 1 192 ? 97.69000  96.90700  110.29700 1.000 59.81362  ? 192 MET B CE   1 
ATOM   3915 N N    . LYS B 1 193 ? 101.99900 102.46600 107.06500 1.000 55.60051  ? 193 LYS B N    1 
ATOM   3916 C CA   . LYS B 1 193 ? 103.10300 103.41100 107.15800 1.000 54.90777  ? 193 LYS B CA   1 
ATOM   3917 C C    . LYS B 1 193 ? 102.65700 104.76600 107.68500 1.000 59.37835  ? 193 LYS B C    1 
ATOM   3918 O O    . LYS B 1 193 ? 103.49800 105.64700 107.89100 1.000 55.40124  ? 193 LYS B O    1 
ATOM   3919 C CB   . LYS B 1 193 ? 103.78100 103.59000 105.79700 1.000 53.46573  ? 193 LYS B CB   1 
ATOM   3920 C CG   . LYS B 1 193 ? 104.97800 102.67800 105.58500 1.000 58.04782  ? 193 LYS B CG   1 
ATOM   3921 C CD   . LYS B 1 193 ? 106.27100 103.35800 106.00600 1.000 59.13924  ? 193 LYS B CD   1 
ATOM   3922 C CE   . LYS B 1 193 ? 106.39100 104.74700 105.40800 1.000 60.02207  ? 193 LYS B CE   1 
ATOM   3923 N NZ   . LYS B 1 193 ? 107.41000 105.56900 106.11300 1.000 56.86890  ? 193 LYS B NZ   1 
ATOM   3924 N N    . ALA B 1 194 ? 101.35600 104.94500 107.90700 1.000 59.23679  ? 194 ALA B N    1 
ATOM   3925 C CA   . ALA B 1 194 ? 100.79400 106.17900 108.43700 1.000 53.02108  ? 194 ALA B CA   1 
ATOM   3926 C C    . ALA B 1 194 ? 100.37600 106.01800 109.89300 1.000 53.67708  ? 194 ALA B C    1 
ATOM   3927 O O    . ALA B 1 194 ? 99.58400  106.81700 110.40300 1.000 51.94434  ? 194 ALA B O    1 
ATOM   3928 C CB   . ALA B 1 194 ? 99.61000  106.63200 107.58200 1.000 50.40965  ? 194 ALA B CB   1 
ATOM   3929 N N    . TYR B 1 195 ? 100.88700 104.98600 110.56800 1.000 42.70545  ? 195 TYR B N    1 
ATOM   3930 C CA   . TYR B 1 195 ? 100.62100 104.75500 111.98200 1.000 36.79591  ? 195 TYR B CA   1 
ATOM   3931 C C    . TYR B 1 195 ? 101.91200 104.40600 112.71000 1.000 39.30262  ? 195 TYR B C    1 
ATOM   3932 O O    . TYR B 1 195 ? 101.89300 103.70800 113.72600 1.000 46.74621  ? 195 TYR B O    1 
ATOM   3933 C CB   . TYR B 1 195 ? 99.59800  103.63600 112.16200 1.000 42.32272  ? 195 TYR B CB   1 
ATOM   3934 C CG   . TYR B 1 195 ? 98.33200  103.82300 111.35800 1.000 42.02119  ? 195 TYR B CG   1 
ATOM   3935 C CD1  . TYR B 1 195 ? 97.45700  104.86400 111.62500 1.000 46.96296  ? 195 TYR B CD1  1 
ATOM   3936 C CD2  . TYR B 1 195 ? 98.01100  102.94500 110.33200 1.000 41.26110  ? 195 TYR B CD2  1 
ATOM   3937 C CE1  . TYR B 1 195 ? 96.30200  105.03100 110.88500 1.000 45.11253  ? 195 TYR B CE1  1 
ATOM   3938 C CE2  . TYR B 1 195 ? 96.86000  103.10400 109.59100 1.000 45.34640  ? 195 TYR B CE2  1 
ATOM   3939 C CZ   . TYR B 1 195 ? 96.00900  104.14700 109.87000 1.000 46.82358  ? 195 TYR B CZ   1 
ATOM   3940 O OH   . TYR B 1 195 ? 94.86100  104.30200 109.13000 1.000 45.93235  ? 195 TYR B OH   1 
ATOM   3941 N N    . GLU B 1 196 ? 103.04200 104.89900 112.20000 1.000 39.35751  ? 196 GLU B N    1 
ATOM   3942 C CA   . GLU B 1 196 ? 104.33700 104.52800 112.75500 1.000 38.02535  ? 196 GLU B CA   1 
ATOM   3943 C C    . GLU B 1 196 ? 104.49900 104.96900 114.20400 1.000 40.32331  ? 196 GLU B C    1 
ATOM   3944 O O    . GLU B 1 196 ? 105.21800 104.31600 114.96800 1.000 42.14147  ? 196 GLU B O    1 
ATOM   3945 C CB   . GLU B 1 196 ? 105.45600 105.11500 111.89500 1.000 39.25576  ? 196 GLU B CB   1 
ATOM   3946 C CG   . GLU B 1 196 ? 106.85600 104.75800 112.36500 1.000 43.47925  ? 196 GLU B CG   1 
ATOM   3947 C CD   . GLU B 1 196 ? 107.83200 105.90100 112.19700 1.000 46.52203  ? 196 GLU B CD   1 
ATOM   3948 O OE1  . GLU B 1 196 ? 107.40500 106.98200 111.74100 1.000 47.39058  ? 196 GLU B OE1  1 
ATOM   3949 O OE2  . GLU B 1 196 ? 109.02500 105.72100 112.51900 1.000 44.91391  ? 196 GLU B OE2  1 
ATOM   3950 N N    . TYR B 1 197 ? 103.85300 106.06300 114.60600 1.000 33.63324  ? 197 TYR B N    1 
ATOM   3951 C CA   . TYR B 1 197 ? 104.03900 106.56100 115.96100 1.000 28.04611  ? 197 TYR B CA   1 
ATOM   3952 C C    . TYR B 1 197 ? 103.04900 105.98600 116.96400 1.000 36.73416  ? 197 TYR B C    1 
ATOM   3953 O O    . TYR B 1 197 ? 103.36700 105.93100 118.16100 1.000 37.55129  ? 197 TYR B O    1 
ATOM   3954 C CB   . TYR B 1 197 ? 103.95200 108.08800 115.96600 1.000 30.35738  ? 197 TYR B CB   1 
ATOM   3955 C CG   . TYR B 1 197 ? 105.14000 108.74600 115.30600 1.000 39.36363  ? 197 TYR B CG   1 
ATOM   3956 C CD1  . TYR B 1 197 ? 106.35900 108.83500 115.96000 1.000 37.51100  ? 197 TYR B CD1  1 
ATOM   3957 C CD2  . TYR B 1 197 ? 105.04600 109.26500 114.02400 1.000 41.40146  ? 197 TYR B CD2  1 
ATOM   3958 C CE1  . TYR B 1 197 ? 107.44900 109.42800 115.35800 1.000 37.55870  ? 197 TYR B CE1  1 
ATOM   3959 C CE2  . TYR B 1 197 ? 106.13100 109.86100 113.41500 1.000 37.08275  ? 197 TYR B CE2  1 
ATOM   3960 C CZ   . TYR B 1 197 ? 107.33000 109.93800 114.08600 1.000 36.75673  ? 197 TYR B CZ   1 
ATOM   3961 O OH   . TYR B 1 197 ? 108.41300 110.53100 113.48200 1.000 35.48754  ? 197 TYR B OH   1 
ATOM   3962 N N    . GLY B 1 198 ? 101.91500 105.44700 116.50900 1.000 29.22222  ? 198 GLY B N    1 
ATOM   3963 C CA   . GLY B 1 198 ? 101.01400 104.83300 117.46400 1.000 20.28607  ? 198 GLY B CA   1 
ATOM   3964 C C    . GLY B 1 198 ? 101.42200 103.43500 117.85300 1.000 27.90143  ? 198 GLY B C    1 
ATOM   3965 O O    . GLY B 1 198 ? 101.11800 103.00100 118.96800 1.000 37.13881  ? 198 GLY B O    1 
ATOM   3966 N N    . PHE B 1 199 ? 102.26400 102.79800 117.04200 1.000 22.56415  ? 199 PHE B N    1 
ATOM   3967 C CA   . PHE B 1 199 ? 102.80100 101.49700 117.40800 1.000 24.95333  ? 199 PHE B CA   1 
ATOM   3968 C C    . PHE B 1 199 ? 103.94400 101.66300 118.39500 1.000 29.55804  ? 199 PHE B C    1 
ATOM   3969 O O    . PHE B 1 199 ? 104.07900 100.87100 119.33900 1.000 33.35344  ? 199 PHE B O    1 
ATOM   3970 C CB   . PHE B 1 199 ? 103.29100 100.76900 116.15600 1.000 25.48564  ? 199 PHE B CB   1 
ATOM   3971 C CG   . PHE B 1 199 ? 102.21800 100.01300 115.42700 1.000 30.07087  ? 199 PHE B CG   1 
ATOM   3972 C CD1  . PHE B 1 199 ? 101.56200 98.95400  116.02600 1.000 27.26986  ? 199 PHE B CD1  1 
ATOM   3973 C CD2  . PHE B 1 199 ? 101.86700 100.36800 114.13600 1.000 28.09293  ? 199 PHE B CD2  1 
ATOM   3974 C CE1  . PHE B 1 199 ? 100.57700 98.26100  115.34900 1.000 30.39883  ? 199 PHE B CE1  1 
ATOM   3975 C CE2  . PHE B 1 199 ? 100.88200 99.68100  113.45500 1.000 21.23796  ? 199 PHE B CE2  1 
ATOM   3976 C CZ   . PHE B 1 199 ? 100.23700 98.62600  114.06200 1.000 25.35597  ? 199 PHE B CZ   1 
ATOM   3977 N N    . ARG B 1 200 ? 104.71900 102.73600 118.23100 1.000 16.51586  ? 200 ARG B N    1 
ATOM   3978 C CA   . ARG B 1 200 ? 105.78300 103.04200 119.17500 1.000 7.63709   ? 200 ARG B CA   1 
ATOM   3979 C C    . ARG B 1 200 ? 105.21000 103.47500 120.51800 1.000 20.24698  ? 200 ARG B C    1 
ATOM   3980 O O    . ARG B 1 200 ? 105.70800 103.05800 121.57200 1.000 32.97622  ? 200 ARG B O    1 
ATOM   3981 C CB   . ARG B 1 200 ? 106.68600 104.12800 118.59300 1.000 11.72855  ? 200 ARG B CB   1 
ATOM   3982 C CG   . ARG B 1 200 ? 107.99900 104.32000 119.32100 1.000 23.02659  ? 200 ARG B CG   1 
ATOM   3983 C CD   . ARG B 1 200 ? 108.78000 105.48700 118.74400 1.000 22.06947  ? 200 ARG B CD   1 
ATOM   3984 N NE   . ARG B 1 200 ? 108.31800 106.76500 119.27100 1.000 26.29499  ? 200 ARG B NE   1 
ATOM   3985 C CZ   . ARG B 1 200 ? 108.83600 107.94100 118.94600 1.000 31.37238  ? 200 ARG B CZ   1 
ATOM   3986 N NH1  . ARG B 1 200 ? 109.83700 108.04300 118.08900 1.000 27.73941  ? 200 ARG B NH1  1 
ATOM   3987 N NH2  . ARG B 1 200 ? 108.33800 109.04300 119.49800 1.000 29.37375  ? 200 ARG B NH2  1 
ATOM   3988 N N    . VAL B 1 201 ? 104.12900 104.26100 120.50700 1.000 14.21378  ? 201 VAL B N    1 
ATOM   3989 C CA   . VAL B 1 201 ? 103.52400 104.63600 121.78000 1.000 19.63434  ? 201 VAL B CA   1 
ATOM   3990 C C    . VAL B 1 201 ? 102.82500 103.44000 122.41900 1.000 20.86247  ? 201 VAL B C    1 
ATOM   3991 O O    . VAL B 1 201 ? 102.82400 103.30200 123.65000 1.000 21.85147  ? 201 VAL B O    1 
ATOM   3992 C CB   . VAL B 1 201 ? 102.56400 105.82700 121.59000 1.000 19.77013  ? 201 VAL B CB   1 
ATOM   3993 C CG1  . VAL B 1 201 ? 101.25200 105.37400 120.97800 1.000 21.68029  ? 201 VAL B CG1  1 
ATOM   3994 C CG2  . VAL B 1 201 ? 102.32400 106.53200 122.91200 1.000 22.35245  ? 201 VAL B CG2  1 
ATOM   3995 N N    . PHE B 1 202 ? 102.30200 102.51200 121.60900 1.000 15.92404  ? 202 PHE B N    1 
ATOM   3996 C CA   . PHE B 1 202 ? 101.69600 101.30700 122.16400 1.000 14.65357  ? 202 PHE B CA   1 
ATOM   3997 C C    . PHE B 1 202 ? 102.73600 100.44400 122.86800 1.000 16.96127  ? 202 PHE B C    1 
ATOM   3998 O O    . PHE B 1 202 ? 102.52200 100.00400 124.00700 1.000 19.24483  ? 202 PHE B O    1 
ATOM   3999 C CB   . PHE B 1 202 ? 101.00800 100.53300 121.03600 1.000 22.18858  ? 202 PHE B CB   1 
ATOM   4000 C CG   . PHE B 1 202 ? 100.47200 99.18800  121.44000 1.000 24.50827  ? 202 PHE B CG   1 
ATOM   4001 C CD1  . PHE B 1 202 ? 101.27500 98.06300  121.39000 1.000 26.70439  ? 202 PHE B CD1  1 
ATOM   4002 C CD2  . PHE B 1 202 ? 99.15700  99.04300  121.83600 1.000 20.85866  ? 202 PHE B CD2  1 
ATOM   4003 C CE1  . PHE B 1 202 ? 100.78300 96.82600  121.75100 1.000 20.09472  ? 202 PHE B CE1  1 
ATOM   4004 C CE2  . PHE B 1 202 ? 98.66100  97.80700  122.19600 1.000 21.32211  ? 202 PHE B CE2  1 
ATOM   4005 C CZ   . PHE B 1 202 ? 99.47500  96.69900  122.15300 1.000 20.27240  ? 202 PHE B CZ   1 
ATOM   4006 N N    . LEU B 1 203 ? 103.89900 100.25500 122.23900 1.000 19.20833  ? 203 LEU B N    1 
ATOM   4007 C CA   . LEU B 1 203 ? 104.93300 99.42900  122.85500 1.000 23.34672  ? 203 LEU B CA   1 
ATOM   4008 C C    . LEU B 1 203 ? 105.51300 100.10500 124.09100 1.000 21.58753  ? 203 LEU B C    1 
ATOM   4009 O O    . LEU B 1 203 ? 105.73900 99.44900  125.12000 1.000 30.74112  ? 203 LEU B O    1 
ATOM   4010 C CB   . LEU B 1 203 ? 106.03600 99.13500  121.83700 1.000 24.30763  ? 203 LEU B CB   1 
ATOM   4011 C CG   . LEU B 1 203 ? 106.91500 97.90100  122.05100 1.000 24.30301  ? 203 LEU B CG   1 
ATOM   4012 C CD1  . LEU B 1 203 ? 106.06800 96.65800  122.28000 1.000 25.60597  ? 203 LEU B CD1  1 
ATOM   4013 C CD2  . LEU B 1 203 ? 107.84100 97.70700  120.86600 1.000 17.28789  ? 203 LEU B CD2  1 
ATOM   4014 N N    . LEU B 1 204 ? 105.71100 101.42400 124.02700 1.000 10.27080  ? 204 LEU B N    1 
ATOM   4015 C CA   . LEU B 1 204 ? 106.26600 102.13900 125.16700 1.000 15.59908  ? 204 LEU B CA   1 
ATOM   4016 C C    . LEU B 1 204 ? 105.33000 102.07800 126.36600 1.000 11.12119  ? 204 LEU B C    1 
ATOM   4017 O O    . LEU B 1 204 ? 105.76900 101.79400 127.48800 1.000 18.42364  ? 204 LEU B O    1 
ATOM   4018 C CB   . LEU B 1 204 ? 106.55300 103.58900 124.78000 1.000 24.40285  ? 204 LEU B CB   1 
ATOM   4019 C CG   . LEU B 1 204 ? 107.09800 104.51400 125.86700 1.000 23.04259  ? 204 LEU B CG   1 
ATOM   4020 C CD1  . LEU B 1 204 ? 108.59400 104.32000 126.03500 1.000 16.84008  ? 204 LEU B CD1  1 
ATOM   4021 C CD2  . LEU B 1 204 ? 106.77700 105.96200 125.53900 1.000 20.87941  ? 204 LEU B CD2  1 
ATOM   4022 N N    . THR B 1 205 ? 104.02900 102.29700 126.15000 1.000 12.94994  ? 205 THR B N    1 
ATOM   4023 C CA   . THR B 1 205 ? 103.11200 102.27900 127.28300 1.000 21.35050  ? 205 THR B CA   1 
ATOM   4024 C C    . THR B 1 205 ? 102.94100 100.86900 127.83100 1.000 20.96490  ? 205 THR B C    1 
ATOM   4025 O O    . THR B 1 205 ? 102.87500 100.68300 129.05100 1.000 25.62539  ? 205 THR B O    1 
ATOM   4026 C CB   . THR B 1 205 ? 101.75800 102.87400 126.89300 1.000 21.84240  ? 205 THR B CB   1 
ATOM   4027 O OG1  . THR B 1 205 ? 101.06700 101.97600 126.01900 1.000 25.15265  ? 205 THR B OG1  1 
ATOM   4028 C CG2  . THR B 1 205 ? 101.94400 104.20900 126.19700 1.000 24.20235  ? 205 THR B CG2  1 
ATOM   4029 N N    . TYR B 1 206 ? 102.90800 99.85500  126.96100 1.000 19.02806  ? 206 TYR B N    1 
ATOM   4030 C CA   . TYR B 1 206 ? 102.78700 98.49100  127.46300 1.000 16.78743  ? 206 TYR B CA   1 
ATOM   4031 C C    . TYR B 1 206 ? 103.96800 98.13500  128.35800 1.000 25.11858  ? 206 TYR B C    1 
ATOM   4032 O O    . TYR B 1 206 ? 103.78900 97.67700  129.49700 1.000 27.21911  ? 206 TYR B O    1 
ATOM   4033 C CB   . TYR B 1 206 ? 102.68000 97.50300  126.30200 1.000 25.95322  ? 206 TYR B CB   1 
ATOM   4034 C CG   . TYR B 1 206 ? 102.50700 96.07300  126.75700 1.000 24.02229  ? 206 TYR B CG   1 
ATOM   4035 C CD1  . TYR B 1 206 ? 101.27600 95.60800  127.19300 1.000 21.69651  ? 206 TYR B CD1  1 
ATOM   4036 C CD2  . TYR B 1 206 ? 103.58000 95.19400  126.77100 1.000 24.40188  ? 206 TYR B CD2  1 
ATOM   4037 C CE1  . TYR B 1 206 ? 101.11700 94.30800  127.61900 1.000 23.68905  ? 206 TYR B CE1  1 
ATOM   4038 C CE2  . TYR B 1 206 ? 103.42900 93.89200  127.19500 1.000 23.84850  ? 206 TYR B CE2  1 
ATOM   4039 C CZ   . TYR B 1 206 ? 102.19600 93.45400  127.61800 1.000 25.57899  ? 206 TYR B CZ   1 
ATOM   4040 O OH   . TYR B 1 206 ? 102.03900 92.15600  128.04000 1.000 29.07921  ? 206 TYR B OH   1 
ATOM   4041 N N    . CYS B 1 207 ? 105.18900 98.37200  127.87000 1.000 34.15985  ? 207 CYS B N    1 
ATOM   4042 C CA   . CYS B 1 207 ? 106.35700 97.98500  128.65100 1.000 18.76581  ? 207 CYS B CA   1 
ATOM   4043 C C    . CYS B 1 207 ? 106.46200 98.80000  129.93400 1.000 20.45466  ? 207 CYS B C    1 
ATOM   4044 O O    . CYS B 1 207 ? 106.78600 98.25000  130.99500 1.000 28.98484  ? 207 CYS B O    1 
ATOM   4045 C CB   . CYS B 1 207 ? 107.62500 98.12900  127.81100 1.000 25.22437  ? 207 CYS B CB   1 
ATOM   4046 S SG   . CYS B 1 207 ? 107.72600 96.99200  126.41000 1.000 34.99372  ? 207 CYS B SG   1 
ATOM   4047 N N    . TYR B 1 208 ? 106.18700 100.10600 129.86900 1.000 26.19377  ? 208 TYR B N    1 
ATOM   4048 C CA   . TYR B 1 208 ? 106.27800 100.92300 131.07400 1.000 22.56720  ? 208 TYR B CA   1 
ATOM   4049 C C    . TYR B 1 208 ? 105.26300 100.48000 132.11900 1.000 28.58966  ? 208 TYR B C    1 
ATOM   4050 O O    . TYR B 1 208 ? 105.59500 100.34300 133.30100 1.000 30.35268  ? 208 TYR B O    1 
ATOM   4051 C CB   . TYR B 1 208 ? 106.08500 102.40000 130.73800 1.000 24.95786  ? 208 TYR B CB   1 
ATOM   4052 C CG   . TYR B 1 208 ? 106.11500 103.27900 131.96500 1.000 35.38245  ? 208 TYR B CG   1 
ATOM   4053 C CD1  . TYR B 1 208 ? 107.29400 103.47400 132.67100 1.000 28.40489  ? 208 TYR B CD1  1 
ATOM   4054 C CD2  . TYR B 1 208 ? 104.96300 103.89400 132.43300 1.000 36.31751  ? 208 TYR B CD2  1 
ATOM   4055 C CE1  . TYR B 1 208 ? 107.32800 104.26700 133.79700 1.000 24.01823  ? 208 TYR B CE1  1 
ATOM   4056 C CE2  . TYR B 1 208 ? 104.98800 104.68900 133.56100 1.000 31.79675  ? 208 TYR B CE2  1 
ATOM   4057 C CZ   . TYR B 1 208 ? 106.17400 104.87100 134.23700 1.000 29.26416  ? 208 TYR B CZ   1 
ATOM   4058 O OH   . TYR B 1 208 ? 106.20700 105.66300 135.36000 1.000 40.64272  ? 208 TYR B OH   1 
ATOM   4059 N N    . ILE B 1 209 ? 104.01400 100.25200 131.70600 1.000 31.04531  ? 209 ILE B N    1 
ATOM   4060 C CA   . ILE B 1 209 ? 102.99500 99.85300  132.67000 1.000 24.42863  ? 209 ILE B CA   1 
ATOM   4061 C C    . ILE B 1 209 ? 103.35600 98.51700  133.29900 1.000 27.24552  ? 209 ILE B C    1 
ATOM   4062 O O    . ILE B 1 209 ? 103.17400 98.31500  134.50500 1.000 34.26001  ? 209 ILE B O    1 
ATOM   4063 C CB   . ILE B 1 209 ? 101.60500 99.80800  132.01200 1.000 30.80433  ? 209 ILE B CB   1 
ATOM   4064 C CG1  . ILE B 1 209 ? 101.09600 101.22200 131.73200 1.000 28.32125  ? 209 ILE B CG1  1 
ATOM   4065 C CG2  . ILE B 1 209 ? 100.62200 99.05900  132.89800 1.000 29.08711  ? 209 ILE B CG2  1 
ATOM   4066 C CD1  . ILE B 1 209 ? 99.77900  101.25300 130.99400 1.000 30.38052  ? 209 ILE B CD1  1 
ATOM   4067 N N    . LEU B 1 210 ? 103.87100 97.58000  132.49900 1.000 37.80586  ? 210 LEU B N    1 
ATOM   4068 C CA   . LEU B 1 210 ? 104.19100 96.26900  133.05600 1.000 28.40095  ? 210 LEU B CA   1 
ATOM   4069 C C    . LEU B 1 210 ? 105.35900 96.34800  134.03400 1.000 29.25536  ? 210 LEU B C    1 
ATOM   4070 O O    . LEU B 1 210 ? 105.29400 95.78900  135.13500 1.000 29.89386  ? 210 LEU B O    1 
ATOM   4071 C CB   . LEU B 1 210 ? 104.49200 95.27700  131.93500 1.000 29.61949  ? 210 LEU B CB   1 
ATOM   4072 C CG   . LEU B 1 210 ? 103.46100 94.16100  131.77500 1.000 30.36079  ? 210 LEU B CG   1 
ATOM   4073 C CD1  . LEU B 1 210 ? 103.80500 93.27600  130.59200 1.000 33.98739  ? 210 LEU B CD1  1 
ATOM   4074 C CD2  . LEU B 1 210 ? 103.35400 93.34400  133.04800 1.000 29.71040  ? 210 LEU B CD2  1 
ATOM   4075 N N    . ILE B 1 211 ? 106.43600 97.04100  133.65600 1.000 38.15819  ? 211 ILE B N    1 
ATOM   4076 C CA   . ILE B 1 211 ? 107.63400 97.05300  134.49500 1.000 31.10103  ? 211 ILE B CA   1 
ATOM   4077 C C    . ILE B 1 211 ? 107.43300 97.90300  135.74600 1.000 35.56465  ? 211 ILE B C    1 
ATOM   4078 O O    . ILE B 1 211 ? 107.83300 97.50900  136.84700 1.000 39.58455  ? 211 ILE B O    1 
ATOM   4079 C CB   . ILE B 1 211 ? 108.85000 97.53200  133.68300 1.000 32.24780  ? 211 ILE B CB   1 
ATOM   4080 C CG1  . ILE B 1 211 ? 109.33300 96.42700  132.74400 1.000 36.29646  ? 211 ILE B CG1  1 
ATOM   4081 C CG2  . ILE B 1 211 ? 109.96600 97.96800  134.61400 1.000 31.62406  ? 211 ILE B CG2  1 
ATOM   4082 C CD1  . ILE B 1 211 ? 110.10600 96.93500  131.55000 1.000 31.98536  ? 211 ILE B CD1  1 
ATOM   4083 N N    . SER B 1 212 ? 106.82000 99.08000  135.60300 1.000 45.92063  ? 212 SER B N    1 
ATOM   4084 C CA   . SER B 1 212 ? 106.75300 100.02400 136.71700 1.000 43.64518  ? 212 SER B CA   1 
ATOM   4085 C C    . SER B 1 212 ? 105.91400 99.49100  137.87300 1.000 46.02564  ? 212 SER B C    1 
ATOM   4086 O O    . SER B 1 212 ? 106.32500 99.57000  139.03700 1.000 45.24429  ? 212 SER B O    1 
ATOM   4087 C CB   . SER B 1 212 ? 106.20200 101.36200 136.22900 1.000 39.29762  ? 212 SER B CB   1 
ATOM   4088 O OG   . SER B 1 212 ? 106.52000 102.40200 137.13500 1.000 45.69844  ? 212 SER B OG   1 
ATOM   4089 N N    . GLY B 1 213 ? 104.73700 98.94600  137.58000 1.000 52.06940  ? 213 GLY B N    1 
ATOM   4090 C CA   . GLY B 1 213 ? 103.82600 98.54500  138.63400 1.000 54.31430  ? 213 GLY B CA   1 
ATOM   4091 C C    . GLY B 1 213 ? 103.92800 97.09200  139.04700 1.000 58.61947  ? 213 GLY B C    1 
ATOM   4092 O O    . GLY B 1 213 ? 103.00700 96.55200  139.66600 1.000 58.92642  ? 213 GLY B O    1 
ATOM   4093 N N    . PHE B 1 214 ? 105.04500 96.44700  138.71400 1.000 66.01750  ? 214 PHE B N    1 
ATOM   4094 C CA   . PHE B 1 214 ? 105.18900 95.02400  138.99900 1.000 65.10753  ? 214 PHE B CA   1 
ATOM   4095 C C    . PHE B 1 214 ? 105.38100 94.77300  140.49000 1.000 64.86790  ? 214 PHE B C    1 
ATOM   4096 O O    . PHE B 1 214 ? 104.74100 93.88700  141.06900 1.000 64.88691  ? 214 PHE B O    1 
ATOM   4097 C CB   . PHE B 1 214 ? 106.35800 94.45100  138.19800 1.000 65.41476  ? 214 PHE B CB   1 
ATOM   4098 C CG   . PHE B 1 214 ? 106.95300 93.20900  138.79200 1.000 68.51676  ? 214 PHE B CG   1 
ATOM   4099 C CD1  . PHE B 1 214 ? 106.25400 92.01400  138.77600 1.000 67.68055  ? 214 PHE B CD1  1 
ATOM   4100 C CD2  . PHE B 1 214 ? 108.21500 93.23300  139.36200 1.000 67.32678  ? 214 PHE B CD2  1 
ATOM   4101 C CE1  . PHE B 1 214 ? 106.80000 90.86800  139.32000 1.000 67.79370  ? 214 PHE B CE1  1 
ATOM   4102 C CE2  . PHE B 1 214 ? 108.76700 92.09100  139.90800 1.000 65.62688  ? 214 PHE B CE2  1 
ATOM   4103 C CZ   . PHE B 1 214 ? 108.05900 90.90700  139.88600 1.000 67.28823  ? 214 PHE B CZ   1 
ATOM   4104 N N    . ARG B 1 215 ? 106.26100 95.54400  141.13100 1.000 74.71751  ? 215 ARG B N    1 
ATOM   4105 C CA   . ARG B 1 215 ? 106.58600 95.29000  142.53100 1.000 77.18746  ? 215 ARG B CA   1 
ATOM   4106 C C    . ARG B 1 215 ? 105.44800 95.70000  143.45900 1.000 78.36789  ? 215 ARG B C    1 
ATOM   4107 O O    . ARG B 1 215 ? 105.15400 94.99900  144.43400 1.000 76.88966  ? 215 ARG B O    1 
ATOM   4108 C CB   . ARG B 1 215 ? 107.87300 96.02300  142.90300 1.000 75.58725  ? 215 ARG B CB   1 
ATOM   4109 C CG   . ARG B 1 215 ? 109.09300 95.47100  142.19200 1.000 78.13090  ? 215 ARG B CG   1 
ATOM   4110 C CD   . ARG B 1 215 ? 110.34100 96.25800  142.55200 1.000 79.07087  ? 215 ARG B CD   1 
ATOM   4111 N NE   . ARG B 1 215 ? 111.53200 95.73000  141.89700 1.000 80.31428  ? 215 ARG B NE   1 
ATOM   4112 C CZ   . ARG B 1 215 ? 111.90300 96.01900  140.65800 1.000 80.97516  ? 215 ARG B CZ   1 
ATOM   4113 N NH1  . ARG B 1 215 ? 111.20100 96.84400  139.90000 1.000 77.69592  ? 215 ARG B NH1  1 
ATOM   4114 N NH2  . ARG B 1 215 ? 113.01000 95.46900  140.16800 1.000 80.80433  ? 215 ARG B NH2  1 
ATOM   4115 N N    . THR B 1 216 ? 104.79900 96.83000  143.17800 1.000 73.94005  ? 216 THR B N    1 
ATOM   4116 C CA   . THR B 1 216 ? 103.76600 97.35300  144.06400 1.000 73.92953  ? 216 THR B CA   1 
ATOM   4117 C C    . THR B 1 216 ? 102.35900 96.89900  143.69800 1.000 71.59278  ? 216 THR B C    1 
ATOM   4118 O O    . THR B 1 216 ? 101.47000 96.94100  144.55500 1.000 69.45804  ? 216 THR B O    1 
ATOM   4119 C CB   . THR B 1 216 ? 103.81100 98.88400  144.07900 1.000 71.66775  ? 216 THR B CB   1 
ATOM   4120 O OG1  . THR B 1 216 ? 103.14900 99.39600  142.91600 1.000 70.93942  ? 216 THR B OG1  1 
ATOM   4121 C CG2  . THR B 1 216 ? 105.25100 99.37300  144.09100 1.000 68.15047  ? 216 THR B CG2  1 
ATOM   4122 N N    . GLY B 1 217 ? 102.13200 96.46900  142.45800 1.000 65.50946  ? 217 GLY B N    1 
ATOM   4123 C CA   . GLY B 1 217 ? 100.81800 96.02800  142.03900 1.000 62.65369  ? 217 GLY B CA   1 
ATOM   4124 C C    . GLY B 1 217 ? 99.86800  97.12500  141.60900 1.000 65.52063  ? 217 GLY B C    1 
ATOM   4125 O O    . GLY B 1 217 ? 98.75100  96.81500  141.17500 1.000 64.69630  ? 217 GLY B O    1 
ATOM   4126 N N    . GLN B 1 218 ? 100.26400 98.39100  141.71800 1.000 69.01843  ? 218 GLN B N    1 
ATOM   4127 C CA   . GLN B 1 218 ? 99.40400  99.52100  141.36800 1.000 67.98383  ? 218 GLN B CA   1 
ATOM   4128 C C    . GLN B 1 218 ? 99.59900  99.85300  139.89300 1.000 65.91285  ? 218 GLN B C    1 
ATOM   4129 O O    . GLN B 1 218 ? 100.59400 100.47500 139.51100 1.000 66.21709  ? 218 GLN B O    1 
ATOM   4130 C CB   . GLN B 1 218 ? 99.71600  100.72200 142.25300 1.000 67.75436  ? 218 GLN B CB   1 
ATOM   4131 C CG   . GLN B 1 218 ? 99.24100  100.57700 143.68900 1.000 69.15341  ? 218 GLN B CG   1 
ATOM   4132 C CD   . GLN B 1 218 ? 99.92900  101.54600 144.63000 1.000 72.58903  ? 218 GLN B CD   1 
ATOM   4133 O OE1  . GLN B 1 218 ? 100.37100 102.61900 144.22000 1.000 70.28928  ? 218 GLN B OE1  1 
ATOM   4134 N NE2  . GLN B 1 218 ? 100.02400 101.17000 145.90000 1.000 69.70555  ? 218 GLN B NE2  1 
ATOM   4135 N N    . PHE B 1 219 ? 98.64700  99.43800  139.05700 1.000 54.49465  ? 219 PHE B N    1 
ATOM   4136 C CA   . PHE B 1 219 ? 98.73600  99.64100  137.61700 1.000 55.51317  ? 219 PHE B CA   1 
ATOM   4137 C C    . PHE B 1 219 ? 97.79300  100.71500 137.09600 1.000 59.75021  ? 219 PHE B C    1 
ATOM   4138 O O    . PHE B 1 219 ? 98.13700  101.42500 136.13900 1.000 64.27115  ? 219 PHE B O    1 
ATOM   4139 C CB   . PHE B 1 219 ? 98.42400  98.32900  136.88400 1.000 52.35159  ? 219 PHE B CB   1 
ATOM   4140 C CG   . PHE B 1 219 ? 99.39200  97.21700  137.17900 1.000 57.05138  ? 219 PHE B CG   1 
ATOM   4141 C CD1  . PHE B 1 219 ? 100.68800 97.25400  136.69800 1.000 57.30571  ? 219 PHE B CD1  1 
ATOM   4142 C CD2  . PHE B 1 219 ? 98.99800  96.12700  137.93700 1.000 61.43519  ? 219 PHE B CD2  1 
ATOM   4143 C CE1  . PHE B 1 219 ? 101.57400 96.22700  136.97000 1.000 53.91571  ? 219 PHE B CE1  1 
ATOM   4144 C CE2  . PHE B 1 219 ? 99.88000  95.09700  138.21400 1.000 59.25282  ? 219 PHE B CE2  1 
ATOM   4145 C CZ   . PHE B 1 219 ? 101.16900 95.14800  137.72900 1.000 52.84856  ? 219 PHE B CZ   1 
ATOM   4146 N N    . ILE B 1 220 ? 96.64900  100.90600 137.75500 1.000 58.43018  ? 220 ILE B N    1 
ATOM   4147 C CA   . ILE B 1 220 ? 95.63500  101.80500 137.22100 1.000 55.38766  ? 220 ILE B CA   1 
ATOM   4148 C C    . ILE B 1 220 ? 95.97700  103.25200 137.52700 1.000 55.61069  ? 220 ILE B C    1 
ATOM   4149 O O    . ILE B 1 220 ? 95.66700  104.14500 136.73200 1.000 61.57648  ? 220 ILE B O    1 
ATOM   4150 C CB   . ILE B 1 220 ? 94.24300  101.44000 137.76700 1.000 54.29391  ? 220 ILE B CB   1 
ATOM   4151 C CG1  . ILE B 1 220 ? 94.02300  99.92500  137.74100 1.000 55.93225  ? 220 ILE B CG1  1 
ATOM   4152 C CG2  . ILE B 1 220 ? 93.15900  102.14700 136.97300 1.000 56.71060  ? 220 ILE B CG2  1 
ATOM   4153 C CD1  . ILE B 1 220 ? 94.59400  99.19400  138.93700 1.000 58.62629  ? 220 ILE B CD1  1 
ATOM   4154 N N    . GLU B 1 221 ? 96.64800  103.51300 138.64900 1.000 51.09086  ? 221 GLU B N    1 
ATOM   4155 C CA   . GLU B 1 221 ? 97.07300  104.87700 138.93100 1.000 55.71879  ? 221 GLU B CA   1 
ATOM   4156 C C    . GLU B 1 221 ? 98.08700  105.34500 137.89900 1.000 56.13039  ? 221 GLU B C    1 
ATOM   4157 O O    . GLU B 1 221 ? 97.99100  106.46700 137.38600 1.000 58.93364  ? 221 GLU B O    1 
ATOM   4158 C CB   . GLU B 1 221 ? 97.65500  104.98600 140.34400 1.000 56.56404  ? 221 GLU B CB   1 
ATOM   4159 C CG   . GLU B 1 221 ? 96.83100  104.35500 141.47300 1.000 58.57547  ? 221 GLU B CG   1 
ATOM   4160 C CD   . GLU B 1 221 ? 96.64900  102.85500 141.33400 1.000 62.48008  ? 221 GLU B CD   1 
ATOM   4161 O OE1  . GLU B 1 221 ? 97.19400  102.27900 140.37000 1.000 60.96627  ? 221 GLU B OE1  1 
ATOM   4162 O OE2  . GLU B 1 221 ? 95.96200  102.25400 142.18700 1.000 60.89013  ? 221 GLU B OE2  1 
ATOM   4163 N N    . VAL B 1 222 ? 99.03000  104.47500 137.53600 1.000 46.33219  ? 222 VAL B N    1 
ATOM   4164 C CA   . VAL B 1 222 ? 100.02300 104.83000 136.52800 1.000 48.50382  ? 222 VAL B CA   1 
ATOM   4165 C C    . VAL B 1 222 ? 99.34800  105.04200 135.18100 1.000 46.11300  ? 222 VAL B C    1 
ATOM   4166 O O    . VAL B 1 222 ? 99.60300  106.03700 134.48500 1.000 52.44226  ? 222 VAL B O    1 
ATOM   4167 C CB   . VAL B 1 222 ? 101.11300 103.74600 136.44600 1.000 51.13509  ? 222 VAL B CB   1 
ATOM   4168 C CG1  . VAL B 1 222 ? 102.33600 104.27400 135.71900 1.000 49.50589  ? 222 VAL B CG1  1 
ATOM   4169 C CG2  . VAL B 1 222 ? 101.48200 103.25600 137.83700 1.000 49.23254  ? 222 VAL B CG2  1 
ATOM   4170 N N    . ALA B 1 223 ? 98.46100  104.11900 134.80100 1.000 36.01979  ? 223 ALA B N    1 
ATOM   4171 C CA   . ALA B 1 223 ? 97.77600  104.25000 133.52000 1.000 41.60641  ? 223 ALA B CA   1 
ATOM   4172 C C    . ALA B 1 223 ? 97.01100  105.56800 133.43400 1.000 50.85404  ? 223 ALA B C    1 
ATOM   4173 O O    . ALA B 1 223 ? 97.18600  106.34500 132.48300 1.000 53.07244  ? 223 ALA B O    1 
ATOM   4174 C CB   . ALA B 1 223 ? 96.83900  103.06000 133.31200 1.000 39.19590  ? 223 ALA B CB   1 
ATOM   4175 N N    . ILE B 1 224 ? 96.17100  105.84600 134.43400 1.000 44.12701  ? 224 ILE B N    1 
ATOM   4176 C CA   . ILE B 1 224 ? 95.33900  107.04600 134.41700 1.000 37.84556  ? 224 ILE B CA   1 
ATOM   4177 C C    . ILE B 1 224 ? 96.20100  108.30300 134.42100 1.000 37.99641  ? 224 ILE B C    1 
ATOM   4178 O O    . ILE B 1 224 ? 95.94900  109.24800 133.66400 1.000 48.57575  ? 224 ILE B O    1 
ATOM   4179 C CB   . ILE B 1 224 ? 94.35200  107.02900 135.59700 1.000 43.58856  ? 224 ILE B CB   1 
ATOM   4180 C CG1  . ILE B 1 224 ? 93.36200  105.87400 135.43800 1.000 42.87142  ? 224 ILE B CG1  1 
ATOM   4181 C CG2  . ILE B 1 224 ? 93.61400  108.35300 135.69600 1.000 43.29531  ? 224 ILE B CG2  1 
ATOM   4182 C CD1  . ILE B 1 224 ? 92.22700  105.90100 136.43200 1.000 42.56135  ? 224 ILE B CD1  1 
ATOM   4183 N N    . SER B 1 225 ? 97.20200  108.35400 135.30100 1.000 34.83613  ? 225 SER B N    1 
ATOM   4184 C CA   . SER B 1 225 ? 98.07700  109.51900 135.36500 1.000 38.79777  ? 225 SER B CA   1 
ATOM   4185 C C    . SER B 1 225 ? 98.70500  109.81500 134.00700 1.000 41.57273  ? 225 SER B C    1 
ATOM   4186 O O    . SER B 1 225 ? 98.63300  110.94600 133.50600 1.000 44.22332  ? 225 SER B O    1 
ATOM   4187 C CB   . SER B 1 225 ? 99.15900  109.29700 136.42200 1.000 42.21788  ? 225 SER B CB   1 
ATOM   4188 O OG   . SER B 1 225 ? 98.60300  109.26800 137.72400 1.000 45.96988  ? 225 SER B OG   1 
ATOM   4189 N N    . ARG B 1 226 ? 99.36900  108.82000 133.41500 1.000 44.38786  ? 226 ARG B N    1 
ATOM   4190 C CA   . ARG B 1 226 ? 100.04700 109.06500 132.14700 1.000 44.64286  ? 226 ARG B CA   1 
ATOM   4191 C C    . ARG B 1 226 ? 99.06000  109.46000 131.04900 1.000 42.58120  ? 226 ARG B C    1 
ATOM   4192 O O    . ARG B 1 226 ? 99.35200  110.34000 130.22500 1.000 45.48938  ? 226 ARG B O    1 
ATOM   4193 C CB   . ARG B 1 226 ? 100.85100 107.82600 131.75300 1.000 40.79160  ? 226 ARG B CB   1 
ATOM   4194 C CG   . ARG B 1 226 ? 101.86300 107.42200 132.82000 1.000 38.08220  ? 226 ARG B CG   1 
ATOM   4195 C CD   . ARG B 1 226 ? 102.61400 108.63400 133.34700 1.000 42.53277  ? 226 ARG B CD   1 
ATOM   4196 N NE   . ARG B 1 226 ? 103.75000 108.27200 134.18600 1.000 38.91074  ? 226 ARG B NE   1 
ATOM   4197 C CZ   . ARG B 1 226 ? 103.67300 108.03000 135.48800 1.000 38.47055  ? 226 ARG B CZ   1 
ATOM   4198 N NH1  . ARG B 1 226 ? 102.52400 108.09900 136.13800 1.000 38.92375  ? 226 ARG B NH1  1 
ATOM   4199 N NH2  . ARG B 1 226 ? 104.77800 107.71000 136.15500 1.000 37.93584  ? 226 ARG B NH2  1 
ATOM   4200 N N    . PHE B 1 227 ? 97.86700  108.85400 131.03900 1.000 37.74738  ? 227 PHE B N    1 
ATOM   4201 C CA   . PHE B 1 227 ? 96.88500  109.23100 130.02500 1.000 39.98557  ? 227 PHE B CA   1 
ATOM   4202 C C    . PHE B 1 227 ? 96.43400  110.67700 130.19600 1.000 41.07703  ? 227 PHE B C    1 
ATOM   4203 O O    . PHE B 1 227 ? 96.25300  111.40600 129.20800 1.000 40.25454  ? 227 PHE B O    1 
ATOM   4204 C CB   . PHE B 1 227 ? 95.68500  108.28700 130.06300 1.000 38.03640  ? 227 PHE B CB   1 
ATOM   4205 C CG   . PHE B 1 227 ? 94.60600  108.65300 129.08500 1.000 45.06756  ? 227 PHE B CG   1 
ATOM   4206 C CD1  . PHE B 1 227 ? 94.85400  108.63500 127.72400 1.000 42.65276  ? 227 PHE B CD1  1 
ATOM   4207 C CD2  . PHE B 1 227 ? 93.34500  109.01400 129.52600 1.000 42.26994  ? 227 PHE B CD2  1 
ATOM   4208 C CE1  . PHE B 1 227 ? 93.86800  108.97800 126.82200 1.000 41.60038  ? 227 PHE B CE1  1 
ATOM   4209 C CE2  . PHE B 1 227 ? 92.35200  109.35200 128.62800 1.000 39.05302  ? 227 PHE B CE2  1 
ATOM   4210 C CZ   . PHE B 1 227 ? 92.61400  109.33300 127.27400 1.000 40.74828  ? 227 PHE B CZ   1 
ATOM   4211 N N    . LEU B 1 228 ? 96.25700  111.11900 131.44200 1.000 36.59886  ? 228 LEU B N    1 
ATOM   4212 C CA   . LEU B 1 228 ? 95.86700  112.50700 131.64100 1.000 32.04795  ? 228 LEU B CA   1 
ATOM   4213 C C    . LEU B 1 228 ? 96.98600  113.45400 131.24200 1.000 37.60233  ? 228 LEU B C    1 
ATOM   4214 O O    . LEU B 1 228 ? 96.71500  114.53200 130.70200 1.000 41.48782  ? 228 LEU B O    1 
ATOM   4215 C CB   . LEU B 1 228 ? 95.46600  112.74600 133.09600 1.000 37.44754  ? 228 LEU B CB   1 
ATOM   4216 C CG   . LEU B 1 228 ? 94.37400  111.84800 133.68100 1.000 42.82196  ? 228 LEU B CG   1 
ATOM   4217 C CD1  . LEU B 1 228 ? 94.16200  112.16600 135.15100 1.000 36.61735  ? 228 LEU B CD1  1 
ATOM   4218 C CD2  . LEU B 1 228 ? 93.07500  111.99000 132.90500 1.000 37.42213  ? 228 LEU B CD2  1 
ATOM   4219 N N    . LEU B 1 229 ? 98.24600  113.07300 131.47800 1.000 39.42412  ? 229 LEU B N    1 
ATOM   4220 C CA   . LEU B 1 229 ? 99.33800  113.93100 131.03000 1.000 30.83174  ? 229 LEU B CA   1 
ATOM   4221 C C    . LEU B 1 229 ? 99.42500  113.99000 129.51100 1.000 27.67836  ? 229 LEU B C    1 
ATOM   4222 O O    . LEU B 1 229 ? 99.78400  115.03800 128.95500 1.000 31.96507  ? 229 LEU B O    1 
ATOM   4223 C CB   . LEU B 1 229 ? 100.67200 113.45100 131.60300 1.000 36.79960  ? 229 LEU B CB   1 
ATOM   4224 C CG   . LEU B 1 229 ? 100.87100 113.51800 133.11700 1.000 35.70206  ? 229 LEU B CG   1 
ATOM   4225 C CD1  . LEU B 1 229 ? 101.98600 112.58000 133.54100 1.000 37.30341  ? 229 LEU B CD1  1 
ATOM   4226 C CD2  . LEU B 1 229 ? 101.16900 114.94100 133.56200 1.000 25.04121  ? 229 LEU B CD2  1 
ATOM   4227 N N    . ILE B 1 230 ? 98.93500  112.95900 128.82200 1.000 28.95789  ? 230 ILE B N    1 
ATOM   4228 C CA   . ILE B 1 230 ? 98.97500  113.02200 127.36500 1.000 33.44217  ? 230 ILE B CA   1 
ATOM   4229 C C    . ILE B 1 230 ? 97.80800  113.83700 126.82500 1.000 34.54387  ? 230 ILE B C    1 
ATOM   4230 O O    . ILE B 1 230 ? 97.95600  114.55600 125.82500 1.000 31.65649  ? 230 ILE B O    1 
ATOM   4231 C CB   . ILE B 1 230 ? 98.99100  111.60300 126.77200 1.000 27.97398  ? 230 ILE B CB   1 
ATOM   4232 C CG1  . ILE B 1 230 ? 100.20400 110.82500 127.28300 1.000 28.38926  ? 230 ILE B CG1  1 
ATOM   4233 C CG2  . ILE B 1 230 ? 98.98500  111.65300 125.25500 1.000 27.26754  ? 230 ILE B CG2  1 
ATOM   4234 C CD1  . ILE B 1 230 ? 100.45100 109.53300 126.54400 1.000 29.68804  ? 230 ILE B CD1  1 
ATOM   4235 N N    . ALA B 1 231 ? 96.67100  113.84100 127.51900 1.000 36.59768  ? 231 ALA B N    1 
ATOM   4236 C CA   . ALA B 1 231 ? 95.59300  114.69800 127.03900 1.000 31.74190  ? 231 ALA B CA   1 
ATOM   4237 C C    . ALA B 1 231 ? 95.87800  116.15500 127.38000 1.000 29.57125  ? 231 ALA B C    1 
ATOM   4238 O O    . ALA B 1 231 ? 95.53900  117.05800 126.59700 1.000 36.44187  ? 231 ALA B O    1 
ATOM   4239 C CB   . ALA B 1 231 ? 94.25700  114.25900 127.63700 1.000 28.14422  ? 231 ALA B CB   1 
ATOM   4240 N N    . LEU B 1 232 ? 96.61100  116.38200 128.47300 1.000 32.53659  ? 232 LEU B N    1 
ATOM   4241 C CA   . LEU B 1 232 ? 97.03100  117.72300 128.84900 1.000 33.75523  ? 232 LEU B CA   1 
ATOM   4242 C C    . LEU B 1 232 ? 98.12200  118.23500 127.92700 1.000 32.02213  ? 232 LEU B C    1 
ATOM   4243 O O    . LEU B 1 232 ? 98.29700  119.45200 127.81100 1.000 33.17161  ? 232 LEU B O    1 
ATOM   4244 C CB   . LEU B 1 232 ? 97.51000  117.73700 130.30300 1.000 33.54140  ? 232 LEU B CB   1 
ATOM   4245 C CG   . LEU B 1 232 ? 98.05800  119.04100 130.89100 1.000 38.03285  ? 232 LEU B CG   1 
ATOM   4246 C CD1  . LEU B 1 232 ? 99.50400  119.28700 130.47700 1.000 29.53612  ? 232 LEU B CD1  1 
ATOM   4247 C CD2  . LEU B 1 232 ? 97.17900  120.21700 130.49700 1.000 34.57017  ? 232 LEU B CD2  1 
ATOM   4248 N N    . GLY B 1 233 ? 98.85600  117.34100 127.27000 1.000 30.81966  ? 233 GLY B N    1 
ATOM   4249 C CA   . GLY B 1 233 ? 99.88700  117.81500 126.37500 1.000 32.60667  ? 233 GLY B CA   1 
ATOM   4250 C C    . GLY B 1 233 ? 99.39500  117.89800 124.94300 1.000 27.92070  ? 233 GLY B C    1 
ATOM   4251 O O    . GLY B 1 233 ? 100.04400 118.53000 124.10600 1.000 23.57817  ? 233 GLY B O    1 
ATOM   4252 N N    . ALA B 1 234 ? 98.25100  117.27600 124.64200 1.000 36.51257  ? 234 ALA B N    1 
ATOM   4253 C CA   . ALA B 1 234 ? 97.69800  117.36400 123.29300 1.000 31.49235  ? 234 ALA B CA   1 
ATOM   4254 C C    . ALA B 1 234 ? 96.62100  118.43400 123.13800 1.000 30.40248  ? 234 ALA B C    1 
ATOM   4255 O O    . ALA B 1 234 ? 96.45900  118.97500 122.03100 1.000 27.24599  ? 234 ALA B O    1 
ATOM   4256 C CB   . ALA B 1 234 ? 97.11600  116.01000 122.86900 1.000 18.45302  ? 234 ALA B CB   1 
ATOM   4257 N N    . GLY B 1 235 ? 96.00900  118.88500 124.23200 1.000 29.46916  ? 235 GLY B N    1 
ATOM   4258 C CA   . GLY B 1 235 ? 94.93700  119.84900 124.07400 1.000 12.48441  ? 235 GLY B CA   1 
ATOM   4259 C C    . GLY B 1 235 ? 95.42900  121.27500 123.97800 1.000 20.55560  ? 235 GLY B C    1 
ATOM   4260 O O    . GLY B 1 235 ? 94.84400  122.09100 123.25600 1.000 32.54814  ? 235 GLY B O    1 
ATOM   4261 N N    . VAL B 1 236 ? 96.55900  121.57000 124.61800 1.000 27.87155  ? 236 VAL B N    1 
ATOM   4262 C CA   . VAL B 1 236 ? 97.14700  122.89400 124.46600 1.000 27.45046  ? 236 VAL B CA   1 
ATOM   4263 C C    . VAL B 1 236 ? 97.73300  123.04500 123.07000 1.000 21.58801  ? 236 VAL B C    1 
ATOM   4264 O O    . VAL B 1 236 ? 97.62300  124.10900 122.44700 1.000 27.83843  ? 236 VAL B O    1 
ATOM   4265 C CB   . VAL B 1 236 ? 98.21100  123.13200 125.55300 1.000 25.66460  ? 236 VAL B CB   1 
ATOM   4266 C CG1  . VAL B 1 236 ? 98.96500  124.42700 125.28900 1.000 24.92977  ? 236 VAL B CG1  1 
ATOM   4267 C CG2  . VAL B 1 236 ? 97.56700  123.15100 126.92900 1.000 29.04177  ? 236 VAL B CG2  1 
ATOM   4268 N N    . SER B 1 237 ? 98.31800  121.97300 122.53400 1.000 19.38144  ? 237 SER B N    1 
ATOM   4269 C CA   . SER B 1 237 ? 98.82700  122.03000 121.17000 1.000 17.90510  ? 237 SER B CA   1 
ATOM   4270 C C    . SER B 1 237 ? 97.69500  122.24000 120.17500 1.000 24.15980  ? 237 SER B C    1 
ATOM   4271 O O    . SER B 1 237 ? 97.80500  123.07600 119.26800 1.000 23.53330  ? 237 SER B O    1 
ATOM   4272 C CB   . SER B 1 237 ? 99.59900  120.75400 120.83800 1.000 20.09403  ? 237 SER B CB   1 
ATOM   4273 O OG   . SER B 1 237 ? 100.55100 120.45800 121.84100 1.000 36.16520  ? 237 SER B OG   1 
ATOM   4274 N N    . LEU B 1 238 ? 96.57300  121.53300 120.35400 1.000 31.72679  ? 238 LEU B N    1 
ATOM   4275 C CA   . LEU B 1 238 ? 95.48500  121.70500 119.39500 1.000 20.84066  ? 238 LEU B CA   1 
ATOM   4276 C C    . LEU B 1 238 ? 94.86100  123.09300 119.50300 1.000 25.36146  ? 238 LEU B C    1 
ATOM   4277 O O    . LEU B 1 238 ? 94.56900  123.72700 118.48000 1.000 28.95602  ? 238 LEU B O    1 
ATOM   4278 C CB   . LEU B 1 238 ? 94.42700  120.62200 119.59300 1.000 26.96729  ? 238 LEU B CB   1 
ATOM   4279 C CG   . LEU B 1 238 ? 93.21700  120.72100 118.66100 1.000 38.40918  ? 238 LEU B CG   1 
ATOM   4280 C CD1  . LEU B 1 238 ? 93.53100  120.08900 117.31400 1.000 35.74830  ? 238 LEU B CD1  1 
ATOM   4281 C CD2  . LEU B 1 238 ? 91.99200  120.07400 119.28600 1.000 26.02042  ? 238 LEU B CD2  1 
ATOM   4282 N N    . GLY B 1 239 ? 94.68500  123.60500 120.72500 1.000 26.47465  ? 239 GLY B N    1 
ATOM   4283 C CA   . GLY B 1 239 ? 94.13400  124.94300 120.87100 1.000 18.85343  ? 239 GLY B CA   1 
ATOM   4284 C C    . GLY B 1 239 ? 95.02500  126.01600 120.27400 1.000 24.37344  ? 239 GLY B C    1 
ATOM   4285 O O    . GLY B 1 239 ? 94.55800  126.89200 119.53500 1.000 31.38118  ? 239 GLY B O    1 
ATOM   4286 N N    . VAL B 1 240 ? 96.32900  125.94100 120.55100 1.000 24.08997  ? 240 VAL B N    1 
ATOM   4287 C CA   . VAL B 1 240 ? 97.23700  126.96200 120.04300 1.000 24.28129  ? 240 VAL B CA   1 
ATOM   4288 C C    . VAL B 1 240 ? 97.31200  126.89800 118.52500 1.000 25.08205  ? 240 VAL B C    1 
ATOM   4289 O O    . VAL B 1 240 ? 97.35300  127.93400 117.85200 1.000 25.66739  ? 240 VAL B O    1 
ATOM   4290 C CB   . VAL B 1 240 ? 98.62800  126.82100 120.68800 1.000 23.19938  ? 240 VAL B CB   1 
ATOM   4291 C CG1  . VAL B 1 240 ? 99.66800  127.56200 119.86500 1.000 17.63424  ? 240 VAL B CG1  1 
ATOM   4292 C CG2  . VAL B 1 240 ? 98.60600  127.34600 122.11000 1.000 19.74475  ? 240 VAL B CG2  1 
ATOM   4293 N N    . ASN B 1 241 ? 97.32700  125.69000 117.95400 1.000 23.83491  ? 241 ASN B N    1 
ATOM   4294 C CA   . ASN B 1 241 ? 97.39700  125.59100 116.50200 1.000 16.99988  ? 241 ASN B CA   1 
ATOM   4295 C C    . ASN B 1 241 ? 96.12800  126.12100 115.84500 1.000 25.00941  ? 241 ASN B C    1 
ATOM   4296 O O    . ASN B 1 241 ? 96.19800  126.83900 114.84200 1.000 17.20374  ? 241 ASN B O    1 
ATOM   4297 C CB   . ASN B 1 241 ? 97.65100  124.14500 116.07700 1.000 10.20756  ? 241 ASN B CB   1 
ATOM   4298 C CG   . ASN B 1 241 ? 98.68300  124.03700 114.97700 1.000 15.01324  ? 241 ASN B CG   1 
ATOM   4299 O OD1  . ASN B 1 241 ? 99.48500  124.94500 114.77600 1.000 32.66693  ? 241 ASN B OD1  1 
ATOM   4300 N ND2  . ASN B 1 241 ? 98.66800  122.92600 114.25600 1.000 8.95692   ? 241 ASN B ND2  1 
ATOM   4301 N N    . MET B 1 242 ? 94.95900  125.79200 116.39900 1.000 29.63986  ? 242 MET B N    1 
ATOM   4302 C CA   . MET B 1 242 ? 93.72100  126.16400 115.72600 1.000 25.89619  ? 242 MET B CA   1 
ATOM   4303 C C    . MET B 1 242 ? 93.34300  127.62900 115.91200 1.000 28.69893  ? 242 MET B C    1 
ATOM   4304 O O    . MET B 1 242 ? 92.65900  128.18900 115.05000 1.000 33.37577  ? 242 MET B O    1 
ATOM   4305 C CB   . MET B 1 242 ? 92.57600  125.27500 116.20900 1.000 31.14765  ? 242 MET B CB   1 
ATOM   4306 C CG   . MET B 1 242 ? 91.49300  125.04800 115.17000 1.000 30.85287  ? 242 MET B CG   1 
ATOM   4307 S SD   . MET B 1 242 ? 90.90700  123.34300 115.15000 1.000 51.33073  ? 242 MET B SD   1 
ATOM   4308 C CE   . MET B 1 242 ? 89.43500  123.50300 114.14600 1.000 33.26366  ? 242 MET B CE   1 
ATOM   4309 N N    . PHE B 1 243 ? 93.76800  128.28000 116.99600 1.000 31.18048  ? 243 PHE B N    1 
ATOM   4310 C CA   . PHE B 1 243 ? 93.26300  129.62700 117.24100 1.000 23.98324  ? 243 PHE B CA   1 
ATOM   4311 C C    . PHE B 1 243 ? 94.21700  130.75900 116.87300 1.000 26.10119  ? 243 PHE B C    1 
ATOM   4312 O O    . PHE B 1 243 ? 93.75900  131.90000 116.74800 1.000 34.88672  ? 243 PHE B O    1 
ATOM   4313 C CB   . PHE B 1 243 ? 92.83600  129.77100 118.70600 1.000 26.49896  ? 243 PHE B CB   1 
ATOM   4314 C CG   . PHE B 1 243 ? 91.73000  128.83300 119.09700 1.000 35.36250  ? 243 PHE B CG   1 
ATOM   4315 C CD1  . PHE B 1 243 ? 90.50600  128.88800 118.45300 1.000 28.29848  ? 243 PHE B CD1  1 
ATOM   4316 C CD2  . PHE B 1 243 ? 91.91100  127.89700 120.09900 1.000 35.79889  ? 243 PHE B CD2  1 
ATOM   4317 C CE1  . PHE B 1 243 ? 89.48500  128.02800 118.80100 1.000 29.37634  ? 243 PHE B CE1  1 
ATOM   4318 C CE2  . PHE B 1 243 ? 90.89200  127.03400 120.45200 1.000 31.54213  ? 243 PHE B CE2  1 
ATOM   4319 C CZ   . PHE B 1 243 ? 89.67800  127.10000 119.80200 1.000 29.58164  ? 243 PHE B CZ   1 
ATOM   4320 N N    . ILE B 1 244 ? 95.50700  130.50300 116.69400 1.000 21.32487  ? 244 ILE B N    1 
ATOM   4321 C CA   . ILE B 1 244 ? 96.45000  131.54600 116.29500 1.000 19.16388  ? 244 ILE B CA   1 
ATOM   4322 C C    . ILE B 1 244 ? 96.91900  131.24600 114.87500 1.000 20.22919  ? 244 ILE B C    1 
ATOM   4323 O O    . ILE B 1 244 ? 97.76400  130.37100 114.65800 1.000 33.12375  ? 244 ILE B O    1 
ATOM   4324 C CB   . ILE B 1 244 ? 97.62700  131.66600 117.26900 1.000 27.21628  ? 244 ILE B CB   1 
ATOM   4325 C CG1  . ILE B 1 244 ? 97.11900  131.94700 118.68500 1.000 23.01357  ? 244 ILE B CG1  1 
ATOM   4326 C CG2  . ILE B 1 244 ? 98.57400  132.76800 116.82700 1.000 18.21857  ? 244 ILE B CG2  1 
ATOM   4327 C CD1  . ILE B 1 244 ? 97.94600  131.30800 119.77300 1.000 21.36104  ? 244 ILE B CD1  1 
ATOM   4328 N N    . TYR B 1 245 ? 96.36900  131.98100 113.90200 1.000 16.00620  ? 245 TYR B N    1 
ATOM   4329 C CA   . TYR B 1 245 ? 96.75500  131.94600 112.49300 1.000 23.58889  ? 245 TYR B CA   1 
ATOM   4330 C C    . TYR B 1 245 ? 96.83900  130.52900 111.93500 1.000 27.02066  ? 245 TYR B C    1 
ATOM   4331 O O    . TYR B 1 245 ? 97.93700  130.03600 111.65100 1.000 27.65190  ? 245 TYR B O    1 
ATOM   4332 C CB   . TYR B 1 245 ? 98.09200  132.66400 112.29800 1.000 24.77747  ? 245 TYR B CB   1 
ATOM   4333 C CG   . TYR B 1 245 ? 97.98600  134.17000 112.37500 1.000 28.05296  ? 245 TYR B CG   1 
ATOM   4334 C CD1  . TYR B 1 245 ? 97.12200  134.86800 111.54200 1.000 29.20581  ? 245 TYR B CD1  1 
ATOM   4335 C CD2  . TYR B 1 245 ? 98.74300  134.89400 113.28400 1.000 28.23235  ? 245 TYR B CD2  1 
ATOM   4336 C CE1  . TYR B 1 245 ? 97.01900  136.24300 111.60900 1.000 25.25370  ? 245 TYR B CE1  1 
ATOM   4337 C CE2  . TYR B 1 245 ? 98.64500  136.27100 113.36000 1.000 28.49612  ? 245 TYR B CE2  1 
ATOM   4338 C CZ   . TYR B 1 245 ? 97.78100  136.93900 112.52000 1.000 29.95270  ? 245 TYR B CZ   1 
ATOM   4339 O OH   . TYR B 1 245 ? 97.68000  138.30800 112.59200 1.000 38.16004  ? 245 TYR B OH   1 
ATOM   4340 N N    . PRO B 1 246 ? 95.70800  129.85300 111.74800 1.000 20.79332  ? 246 PRO B N    1 
ATOM   4341 C CA   . PRO B 1 246 ? 95.74500  128.46600 111.27400 1.000 12.98486  ? 246 PRO B CA   1 
ATOM   4342 C C    . PRO B 1 246 ? 96.20700  128.35800 109.82900 1.000 15.55172  ? 246 PRO B C    1 
ATOM   4343 O O    . PRO B 1 246 ? 96.00200  129.26000 109.01300 1.000 24.84790  ? 246 PRO B O    1 
ATOM   4344 C CB   . PRO B 1 246 ? 94.29100  128.00000 111.42100 1.000 10.79785  ? 246 PRO B CB   1 
ATOM   4345 C CG   . PRO B 1 246 ? 93.62300  129.02900 112.28400 1.000 15.69610  ? 246 PRO B CG   1 
ATOM   4346 C CD   . PRO B 1 246 ? 94.33700  130.30700 112.01800 1.000 17.15468  ? 246 PRO B CD   1 
ATOM   4347 N N    . ILE B 1 247 ? 96.84900  127.23300 109.52100 1.000 15.99224  ? 247 ILE B N    1 
ATOM   4348 C CA   . ILE B 1 247 ? 97.21200  126.86200 108.15700 1.000 12.26612  ? 247 ILE B CA   1 
ATOM   4349 C C    . ILE B 1 247 ? 96.39300  125.64000 107.76800 1.000 17.89540  ? 247 ILE B C    1 
ATOM   4350 O O    . ILE B 1 247 ? 96.30900  124.67200 108.53300 1.000 23.73997  ? 247 ILE B O    1 
ATOM   4351 C CB   . ILE B 1 247 ? 98.71900  126.58300 108.02200 1.000 12.10487  ? 247 ILE B CB   1 
ATOM   4352 C CG1  . ILE B 1 247 ? 99.52200  127.87300 108.18900 1.000 18.33537  ? 247 ILE B CG1  1 
ATOM   4353 C CG2  . ILE B 1 247 ? 99.02100  125.93900 106.68100 1.000 8.10691   ? 247 ILE B CG2  1 
ATOM   4354 C CD1  . ILE B 1 247 ? 101.01600 127.67800 108.08000 1.000 19.48757  ? 247 ILE B CD1  1 
ATOM   4355 N N    . TRP B 1 248 ? 95.79200  125.68100 106.58300 1.000 20.44009  ? 248 TRP B N    1 
ATOM   4356 C CA   . TRP B 1 248 ? 94.92100  124.61900 106.10000 1.000 5.11693   ? 248 TRP B CA   1 
ATOM   4357 C C    . TRP B 1 248 ? 95.58300  123.87600 104.94600 1.000 15.02765  ? 248 TRP B C    1 
ATOM   4358 O O    . TRP B 1 248 ? 96.25500  124.48300 104.10900 1.000 35.14963  ? 248 TRP B O    1 
ATOM   4359 C CB   . TRP B 1 248 ? 93.57200  125.19000 105.66000 1.000 10.39253  ? 248 TRP B CB   1 
ATOM   4360 C CG   . TRP B 1 248 ? 92.94900  126.09200 106.68600 1.000 14.60362  ? 248 TRP B CG   1 
ATOM   4361 C CD1  . TRP B 1 248 ? 93.06800  127.44800 106.76500 1.000 11.98280  ? 248 TRP B CD1  1 
ATOM   4362 C CD2  . TRP B 1 248 ? 92.11400  125.70000 107.78300 1.000 19.11694  ? 248 TRP B CD2  1 
ATOM   4363 N NE1  . TRP B 1 248 ? 92.35900  127.92500 107.83700 1.000 4.22701   ? 248 TRP B NE1  1 
ATOM   4364 C CE2  . TRP B 1 248 ? 91.76300  126.87200 108.47900 1.000 7.16732   ? 248 TRP B CE2  1 
ATOM   4365 C CE3  . TRP B 1 248 ? 91.62700  124.47300 108.24100 1.000 17.90642  ? 248 TRP B CE3  1 
ATOM   4366 C CZ2  . TRP B 1 248 ? 90.94800  126.85400 109.60700 1.000 10.53011  ? 248 TRP B CZ2  1 
ATOM   4367 C CZ3  . TRP B 1 248 ? 90.82000  124.45600 109.36000 1.000 8.97290   ? 248 TRP B CZ3  1 
ATOM   4368 C CH2  . TRP B 1 248 ? 90.48900  125.63800 110.03100 1.000 17.29943  ? 248 TRP B CH2  1 
ATOM   4369 N N    . ALA B 1 249 ? 95.38800  122.55500 104.90700 1.000 15.65567  ? 249 ALA B N    1 
ATOM   4370 C CA   . ALA B 1 249 ? 95.98000  121.73300 103.85600 1.000 17.51227  ? 249 ALA B CA   1 
ATOM   4371 C C    . ALA B 1 249 ? 95.20300  121.80200 102.54600 1.000 27.89471  ? 249 ALA B C    1 
ATOM   4372 O O    . ALA B 1 249 ? 95.79300  121.62000 101.47100 1.000 28.75753  ? 249 ALA B O    1 
ATOM   4373 C CB   . ALA B 1 249 ? 96.08400  120.28200 104.32500 1.000 5.05784   ? 249 ALA B CB   1 
ATOM   4374 N N    . GLY B 1 250 ? 93.89700  122.06900 102.60400 1.000 15.32866  ? 250 GLY B N    1 
ATOM   4375 C CA   . GLY B 1 250 ? 93.12700  122.19300 101.37700 1.000 12.47850  ? 250 GLY B CA   1 
ATOM   4376 C C    . GLY B 1 250 ? 93.57200  123.36900 100.53100 1.000 25.40414  ? 250 GLY B C    1 
ATOM   4377 O O    . GLY B 1 250 ? 93.61900  123.28300 99.30000  1.000 34.27688  ? 250 GLY B O    1 
ATOM   4378 N N    . GLU B 1 251 ? 93.93600  124.47600 101.18000 1.000 19.06134  ? 251 GLU B N    1 
ATOM   4379 C CA   . GLU B 1 251 ? 94.43800  125.62600 100.44100 1.000 26.47936  ? 251 GLU B CA   1 
ATOM   4380 C C    . GLU B 1 251 ? 95.81000  125.34600 99.84200  1.000 13.79607  ? 251 GLU B C    1 
ATOM   4381 O O    . GLU B 1 251 ? 96.12000  125.82500 98.74300  1.000 14.87736  ? 251 GLU B O    1 
ATOM   4382 C CB   . GLU B 1 251 ? 94.47900  126.84300 101.36500 1.000 25.99521  ? 251 GLU B CB   1 
ATOM   4383 C CG   . GLU B 1 251 ? 94.52200  128.17800 100.65400 1.000 32.90879  ? 251 GLU B CG   1 
ATOM   4384 C CD   . GLU B 1 251 ? 94.83200  129.31900 101.59800 1.000 35.07571  ? 251 GLU B CD   1 
ATOM   4385 O OE1  . GLU B 1 251 ? 94.38000  129.26200 102.76000 1.000 36.33601  ? 251 GLU B OE1  1 
ATOM   4386 O OE2  . GLU B 1 251 ? 95.52700  130.27000 101.18000 1.000 38.94109  ? 251 GLU B OE2  1 
ATOM   4387 N N    . ASP B 1 252 ? 96.61600  124.51500 100.50600 1.000 11.63409  ? 252 ASP B N    1 
ATOM   4388 C CA   . ASP B 1 252 ? 97.90600  124.13800 99.94300  1.000 25.68117  ? 252 ASP B CA   1 
ATOM   4389 C C    . ASP B 1 252 ? 97.72600  123.23800 98.72700  1.000 32.27071  ? 252 ASP B C    1 
ATOM   4390 O O    . ASP B 1 252 ? 98.46400  123.35900 97.74100  1.000 35.59356  ? 252 ASP B O    1 
ATOM   4391 C CB   . ASP B 1 252 ? 98.76000  123.44200 101.00200 1.000 26.29356  ? 252 ASP B CB   1 
ATOM   4392 C CG   . ASP B 1 252 ? 99.00800  124.31100 102.21500 1.000 28.64171  ? 252 ASP B CG   1 
ATOM   4393 O OD1  . ASP B 1 252 ? 98.68400  125.51500 102.16400 1.000 30.09655  ? 252 ASP B OD1  1 
ATOM   4394 O OD2  . ASP B 1 252 ? 99.53300  123.79000 103.22000 1.000 29.60110  ? 252 ASP B OD2  1 
ATOM   4395 N N    . LEU B 1 253 ? 96.73200  122.34900 98.76700  1.000 16.48736  ? 253 LEU B N    1 
ATOM   4396 C CA   . LEU B 1 253 ? 96.43500  121.53700 97.59200  1.000 16.87434  ? 253 LEU B CA   1 
ATOM   4397 C C    . LEU B 1 253 ? 95.94200  122.40300 96.43600  1.000 20.35648  ? 253 LEU B C    1 
ATOM   4398 O O    . LEU B 1 253 ? 96.34800  122.20700 95.28100  1.000 26.06784  ? 253 LEU B O    1 
ATOM   4399 C CB   . LEU B 1 253 ? 95.40000  120.47300 97.95700  1.000 22.69419  ? 253 LEU B CB   1 
ATOM   4400 C CG   . LEU B 1 253 ? 95.13400  119.31500 96.99500  1.000 26.27772  ? 253 LEU B CG   1 
ATOM   4401 C CD1  . LEU B 1 253 ? 96.38500  118.48100 96.80100  1.000 21.98887  ? 253 LEU B CD1  1 
ATOM   4402 C CD2  . LEU B 1 253 ? 93.99100  118.45900 97.51600  1.000 13.48644  ? 253 LEU B CD2  1 
ATOM   4403 N N    . HIS B 1 254 ? 95.08700  123.38300 96.73600  1.000 14.20200  ? 254 HIS B N    1 
ATOM   4404 C CA   . HIS B 1 254 ? 94.60000  124.29600 95.70500  1.000 14.29262  ? 254 HIS B CA   1 
ATOM   4405 C C    . HIS B 1 254 ? 95.74700  125.08300 95.07400  1.000 23.97704  ? 254 HIS B C    1 
ATOM   4406 O O    . HIS B 1 254 ? 95.80700  125.24400 93.84400  1.000 25.55502  ? 254 HIS B O    1 
ATOM   4407 C CB   . HIS B 1 254 ? 93.56700  125.23700 96.33000  1.000 15.38379  ? 254 HIS B CB   1 
ATOM   4408 C CG   . HIS B 1 254 ? 92.92600  126.18500 95.36500  1.000 27.51227  ? 254 HIS B CG   1 
ATOM   4409 N ND1  . HIS B 1 254 ? 91.64800  126.00400 94.88400  1.000 29.33278  ? 254 HIS B ND1  1 
ATOM   4410 C CD2  . HIS B 1 254 ? 93.37400  127.33900 94.81700  1.000 29.46575  ? 254 HIS B CD2  1 
ATOM   4411 C CE1  . HIS B 1 254 ? 91.34100  126.99700 94.06900  1.000 28.28543  ? 254 HIS B CE1  1 
ATOM   4412 N NE2  . HIS B 1 254 ? 92.37200  127.82000 94.01000  1.000 24.15530  ? 254 HIS B NE2  1 
ATOM   4413 N N    . ASN B 1 255 ? 96.74800  125.44600 95.87900  1.000 27.10681  ? 255 ASN B N    1 
ATOM   4414 C CA   . ASN B 1 255 ? 97.84000  126.23800 95.32800  1.000 17.11509  ? 255 ASN B CA   1 
ATOM   4415 C C    . ASN B 1 255 ? 98.85200  125.37400 94.59200  1.000 18.01353  ? 255 ASN B C    1 
ATOM   4416 O O    . ASN B 1 255 ? 99.47600  125.84100 93.63200  1.000 31.21761  ? 255 ASN B O    1 
ATOM   4417 C CB   . ASN B 1 255 ? 98.53000  127.01800 96.44600  1.000 20.40697  ? 255 ASN B CB   1 
ATOM   4418 C CG   . ASN B 1 255 ? 97.66100  128.12600 97.00800  1.000 27.17383  ? 255 ASN B CG   1 
ATOM   4419 O OD1  . ASN B 1 255 ? 96.69900  128.55800 96.37500  1.000 27.44907  ? 255 ASN B OD1  1 
ATOM   4420 N ND2  . ASN B 1 255 ? 97.99400  128.58800 98.20500  1.000 24.25437  ? 255 ASN B ND2  1 
ATOM   4421 N N    . LEU B 1 256 ? 98.96300  124.09600 94.95000  1.000 17.18179  ? 256 LEU B N    1 
ATOM   4422 C CA   . LEU B 1 256 ? 99.89400  123.24300 94.22400  1.000 23.05264  ? 256 LEU B CA   1 
ATOM   4423 C C    . LEU B 1 256 ? 99.30700  122.87200 92.86900  1.000 19.36183  ? 256 LEU B C    1 
ATOM   4424 O O    . LEU B 1 256 ? 100.02600 122.82000 91.85600  1.000 28.89127  ? 256 LEU B O    1 
ATOM   4425 C CB   . LEU B 1 256 ? 100.20500 121.99300 95.04800  1.000 20.07000  ? 256 LEU B CB   1 
ATOM   4426 C CG   . LEU B 1 256 ? 101.05700 120.89800 94.40900  1.000 28.39815  ? 256 LEU B CG   1 
ATOM   4427 C CD1  . LEU B 1 256 ? 102.45300 121.41300 94.10400  1.000 26.91621  ? 256 LEU B CD1  1 
ATOM   4428 C CD2  . LEU B 1 256 ? 101.11500 119.67800 95.31100  1.000 22.14760  ? 256 LEU B CD2  1 
ATOM   4429 N N    . VAL B 1 257 ? 97.98700  122.66800 92.83100  1.000 14.12149  ? 257 VAL B N    1 
ATOM   4430 C CA   . VAL B 1 257 ? 97.31600  122.41400 91.56300  1.000 16.29104  ? 257 VAL B CA   1 
ATOM   4431 C C    . VAL B 1 257 ? 97.43900  123.62800 90.65400  1.000 15.74271  ? 257 VAL B C    1 
ATOM   4432 O O    . VAL B 1 257 ? 97.64800  123.49400 89.44300  1.000 16.32808  ? 257 VAL B O    1 
ATOM   4433 C CB   . VAL B 1 257 ? 95.84600  122.02100 91.79900  1.000 24.71060  ? 257 VAL B CB   1 
ATOM   4434 C CG1  . VAL B 1 257 ? 95.05700  122.10900 90.50200  1.000 12.33480  ? 257 VAL B CG1  1 
ATOM   4435 C CG2  . VAL B 1 257 ? 95.76300  120.62000 92.37700  1.000 18.73555  ? 257 VAL B CG2  1 
ATOM   4436 N N    . VAL B 1 258 ? 97.31800  124.83400 91.21700  1.000 21.85354  ? 258 VAL B N    1 
ATOM   4437 C CA   . VAL B 1 258 ? 97.49500  126.02600 90.39000  1.000 22.78851  ? 258 VAL B CA   1 
ATOM   4438 C C    . VAL B 1 258 ? 98.93100  126.13400 89.87300  1.000 21.03891  ? 258 VAL B C    1 
ATOM   4439 O O    . VAL B 1 258 ? 99.15700  126.48000 88.70700  1.000 16.07118  ? 258 VAL B O    1 
ATOM   4440 C CB   . VAL B 1 258 ? 97.07500  127.28700 91.16700  1.000 25.34259  ? 258 VAL B CB   1 
ATOM   4441 C CG1  . VAL B 1 258 ? 97.50300  128.53700 90.41600  1.000 22.21820  ? 258 VAL B CG1  1 
ATOM   4442 C CG2  . VAL B 1 258 ? 95.57400  127.29600 91.38800  1.000 19.56516  ? 258 VAL B CG2  1 
ATOM   4443 N N    . LYS B 1 259 ? 99.92300  125.85200 90.72600  1.000 28.71257  ? 259 LYS B N    1 
ATOM   4444 C CA   . LYS B 1 259 ? 101.32900 126.00900 90.34200  1.000 28.59996  ? 259 LYS B CA   1 
ATOM   4445 C C    . LYS B 1 259 ? 101.78300 125.02700 89.25600  1.000 30.19627  ? 259 LYS B C    1 
ATOM   4446 O O    . LYS B 1 259 ? 102.62900 125.38100 88.41300  1.000 39.11317  ? 259 LYS B O    1 
ATOM   4447 C CB   . LYS B 1 259 ? 102.20400 125.87600 91.58800  1.000 24.02077  ? 259 LYS B CB   1 
ATOM   4448 C CG   . LYS B 1 259 ? 103.65600 126.26700 91.40000  1.000 26.46166  ? 259 LYS B CG   1 
ATOM   4449 C CD   . LYS B 1 259 ? 104.52500 125.63200 92.47400  1.000 32.91705  ? 259 LYS B CD   1 
ATOM   4450 C CE   . LYS B 1 259 ? 104.50800 124.11500 92.38500  1.000 35.63382  ? 259 LYS B CE   1 
ATOM   4451 N NZ   . LYS B 1 259 ? 105.88100 123.54000 92.37700  1.000 34.27399  ? 259 LYS B NZ   1 
ATOM   4452 N N    . ASN B 1 260 ? 101.24900 123.80100 89.25300  1.000 21.37163  ? 260 ASN B N    1 
ATOM   4453 C CA   . ASN B 1 260 ? 101.70400 122.82400 88.26000  1.000 21.36044  ? 260 ASN B CA   1 
ATOM   4454 C C    . ASN B 1 260 ? 101.42000 123.28500 86.83000  1.000 20.77443  ? 260 ASN B C    1 
ATOM   4455 O O    . ASN B 1 260 ? 102.22400 123.04000 85.91700  1.000 22.68565  ? 260 ASN B O    1 
ATOM   4456 C CB   . ASN B 1 260 ? 101.05300 121.46500 88.51800  1.000 29.61150  ? 260 ASN B CB   1 
ATOM   4457 C CG   . ASN B 1 260 ? 101.61200 120.77000 89.74400  1.000 35.45315  ? 260 ASN B CG   1 
ATOM   4458 O OD1  . ASN B 1 260 ? 102.73600 121.03600 90.16600  1.000 35.56983  ? 260 ASN B OD1  1 
ATOM   4459 N ND2  . ASN B 1 260 ? 100.82700 119.86900 90.32200  1.000 31.00366  ? 260 ASN B ND2  1 
ATOM   4460 N N    . PHE B 1 261 ? 100.28200 123.94900 86.61200  1.000 24.75338  ? 261 PHE B N    1 
ATOM   4461 C CA   . PHE B 1 261 ? 99.92400  124.37700 85.26400  1.000 17.07171  ? 261 PHE B CA   1 
ATOM   4462 C C    . PHE B 1 261 ? 100.94300 125.36900 84.71800  1.000 25.89361  ? 261 PHE B C    1 
ATOM   4463 O O    . PHE B 1 261 ? 101.35800 125.27800 83.55300  1.000 30.43910  ? 261 PHE B O    1 
ATOM   4464 C CB   . PHE B 1 261 ? 98.52900  125.00300 85.27800  1.000 17.35759  ? 261 PHE B CB   1 
ATOM   4465 C CG   . PHE B 1 261 ? 97.42800  124.05100 84.91100  1.000 24.31431  ? 261 PHE B CG   1 
ATOM   4466 C CD1  . PHE B 1 261 ? 97.15300  123.75900 83.58700  1.000 31.87389  ? 261 PHE B CD1  1 
ATOM   4467 C CD2  . PHE B 1 261 ? 96.66400  123.44800 85.89600  1.000 19.32335  ? 261 PHE B CD2  1 
ATOM   4468 C CE1  . PHE B 1 261 ? 96.13700  122.88500 83.25300  1.000 30.46886  ? 261 PHE B CE1  1 
ATOM   4469 C CE2  . PHE B 1 261 ? 95.64900  122.57400 85.56900  1.000 21.43354  ? 261 PHE B CE2  1 
ATOM   4470 C CZ   . PHE B 1 261 ? 95.38500  122.29100 84.24600  1.000 26.73825  ? 261 PHE B CZ   1 
ATOM   4471 N N    . MET B 1 262 ? 101.41300 126.28000 85.57100  1.000 29.78773  ? 262 MET B N    1 
ATOM   4472 C CA   . MET B 1 262 ? 102.38900 127.26700 85.13200  1.000 25.60361  ? 262 MET B CA   1 
ATOM   4473 C C    . MET B 1 262 ? 103.74400 126.61900 84.90500  1.000 24.62487  ? 262 MET B C    1 
ATOM   4474 O O    . MET B 1 262 ? 104.46800 126.98700 83.97000  1.000 31.95272  ? 262 MET B O    1 
ATOM   4475 C CB   . MET B 1 262 ? 102.49900 128.39000 86.16200  1.000 25.67326  ? 262 MET B CB   1 
ATOM   4476 C CG   . MET B 1 262 ? 101.16800 128.86500 86.71600  1.000 31.49806  ? 262 MET B CG   1 
ATOM   4477 S SD   . MET B 1 262 ? 100.39900 130.13800 85.70000  1.000 45.34773  ? 262 MET B SD   1 
ATOM   4478 C CE   . MET B 1 262 ? 98.69600  129.59300 85.71000  1.000 29.42660  ? 262 MET B CE   1 
ATOM   4479 N N    . ASN B 1 263 ? 104.09900 125.63500 85.73500  1.000 29.15398  ? 263 ASN B N    1 
ATOM   4480 C CA   . ASN B 1 263 ? 105.38100 124.97200 85.52300  1.000 30.77141  ? 263 ASN B CA   1 
ATOM   4481 C C    . ASN B 1 263 ? 105.40900 124.24800 84.18000  1.000 29.20434  ? 263 ASN B C    1 
ATOM   4482 O O    . ASN B 1 263 ? 106.39300 124.34200 83.43100  1.000 33.98394  ? 263 ASN B O    1 
ATOM   4483 C CB   . ASN B 1 263 ? 105.66600 123.99900 86.66600  1.000 31.95983  ? 263 ASN B CB   1 
ATOM   4484 C CG   . ASN B 1 263 ? 106.08600 124.70400 87.93800  1.000 35.64719  ? 263 ASN B CG   1 
ATOM   4485 O OD1  . ASN B 1 263 ? 106.23300 125.92400 87.96500  1.000 34.71145  ? 263 ASN B OD1  1 
ATOM   4486 N ND2  . ASN B 1 263 ? 106.28300 123.93600 89.00200  1.000 38.78892  ? 263 ASN B ND2  1 
ATOM   4487 N N    . VAL B 1 264 ? 104.31500 123.56800 83.82900  1.000 27.57509  ? 264 VAL B N    1 
ATOM   4488 C CA   . VAL B 1 264 ? 104.27000 122.87100 82.54400  1.000 26.14932  ? 264 VAL B CA   1 
ATOM   4489 C C    . VAL B 1 264 ? 104.26600 123.86400 81.38400  1.000 29.48336  ? 264 VAL B C    1 
ATOM   4490 O O    . VAL B 1 264 ? 104.90900 123.63700 80.34500  1.000 34.65256  ? 264 VAL B O    1 
ATOM   4491 C CB   . VAL B 1 264 ? 103.05400 121.92900 82.49000  1.000 30.64588  ? 264 VAL B CB   1 
ATOM   4492 C CG1  . VAL B 1 264 ? 103.07900 121.10400 81.21500  1.000 33.96167  ? 264 VAL B CG1  1 
ATOM   4493 C CG2  . VAL B 1 264 ? 103.03300 121.02300 83.70700  1.000 27.69353  ? 264 VAL B CG2  1 
ATOM   4494 N N    . ALA B 1 265 ? 103.54900 124.98300 81.54000  1.000 29.34525  ? 265 ALA B N    1 
ATOM   4495 C CA   . ALA B 1 265 ? 103.51500 125.97600 80.47100  1.000 26.06917  ? 265 ALA B CA   1 
ATOM   4496 C C    . ALA B 1 265 ? 104.90000 126.55400 80.20800  1.000 29.27450  ? 265 ALA B C    1 
ATOM   4497 O O    . ALA B 1 265 ? 105.28000 126.77200 79.05100  1.000 29.60299  ? 265 ALA B O    1 
ATOM   4498 C CB   . ALA B 1 265 ? 102.52400 127.08700 80.81400  1.000 28.04782  ? 265 ALA B CB   1 
ATOM   4499 N N    . THR B 1 266 ? 105.67100 126.81600 81.26600  1.000 32.27853  ? 266 THR B N    1 
ATOM   4500 C CA   . THR B 1 266 ? 107.03800 127.28900 81.06000  1.000 32.55026  ? 266 THR B CA   1 
ATOM   4501 C C    . THR B 1 266 ? 107.91000 126.21500 80.41500  1.000 34.30047  ? 266 THR B C    1 
ATOM   4502 O O    . THR B 1 266 ? 108.72100 126.51300 79.52500  1.000 33.92322  ? 266 THR B O    1 
ATOM   4503 C CB   . THR B 1 266 ? 107.64600 127.74900 82.38500  1.000 31.21073  ? 266 THR B CB   1 
ATOM   4504 O OG1  . THR B 1 266 ? 107.20300 129.07900 82.67800  1.000 36.29430  ? 266 THR B OG1  1 
ATOM   4505 C CG2  . THR B 1 266 ? 109.16100 127.73800 82.30700  1.000 28.70253  ? 266 THR B CG2  1 
ATOM   4506 N N    . SER B 1 267 ? 107.75500 124.95900 80.85000  1.000 39.06030  ? 267 SER B N    1 
ATOM   4507 C CA   . SER B 1 267 ? 108.59200 123.88500 80.32200  1.000 29.45019  ? 267 SER B CA   1 
ATOM   4508 C C    . SER B 1 267 ? 108.41500 123.71200 78.81600  1.000 29.86494  ? 267 SER B C    1 
ATOM   4509 O O    . SER B 1 267 ? 109.39500 123.49500 78.09200  1.000 29.32153  ? 267 SER B O    1 
ATOM   4510 C CB   . SER B 1 267 ? 108.28100 122.57600 81.04600  1.000 35.27004  ? 267 SER B CB   1 
ATOM   4511 O OG   . SER B 1 267 ? 109.13900 122.39500 82.15500  1.000 39.14801  ? 267 SER B OG   1 
ATOM   4512 N N    . LEU B 1 268 ? 107.17300 123.77800 78.32500  1.000 27.33346  ? 268 LEU B N    1 
ATOM   4513 C CA   . LEU B 1 268 ? 106.95900 123.53300 76.89700  1.000 24.32557  ? 268 LEU B CA   1 
ATOM   4514 C C    . LEU B 1 268 ? 107.67300 124.57200 76.03200  1.000 31.40049  ? 268 LEU B C    1 
ATOM   4515 O O    . LEU B 1 268 ? 108.34300 124.22500 75.04400  1.000 33.16839  ? 268 LEU B O    1 
ATOM   4516 C CB   . LEU B 1 268 ? 105.46200 123.51200 76.58600  1.000 26.17767  ? 268 LEU B CB   1 
ATOM   4517 C CG   . LEU B 1 268 ? 105.07100 123.23400 75.13100  1.000 31.68360  ? 268 LEU B CG   1 
ATOM   4518 C CD1  . LEU B 1 268 ? 105.12700 121.74700 74.82000  1.000 26.45131  ? 268 LEU B CD1  1 
ATOM   4519 C CD2  . LEU B 1 268 ? 103.69200 123.79300 74.83000  1.000 24.55871  ? 268 LEU B CD2  1 
ATOM   4520 N N    . GLU B 1 269 ? 107.56700 125.85000 76.40400  1.000 37.75312  ? 269 GLU B N    1 
ATOM   4521 C CA   . GLU B 1 269 ? 108.22900 126.89400 75.62900  1.000 35.16921  ? 269 GLU B CA   1 
ATOM   4522 C C    . GLU B 1 269 ? 109.73900 126.78700 75.75700  1.000 38.06586  ? 269 GLU B C    1 
ATOM   4523 O O    . GLU B 1 269 ? 110.47000 127.00800 74.78100  1.000 38.06887  ? 269 GLU B O    1 
ATOM   4524 C CB   . GLU B 1 269 ? 107.75500 128.27300 76.08600  1.000 36.14858  ? 269 GLU B CB   1 
ATOM   4525 C CG   . GLU B 1 269 ? 106.68000 128.88900 75.21500  1.000 40.46289  ? 269 GLU B CG   1 
ATOM   4526 C CD   . GLU B 1 269 ? 106.08900 130.14200 75.82900  1.000 50.58991  ? 269 GLU B CD   1 
ATOM   4527 O OE1  . GLU B 1 269 ? 106.42800 130.45000 76.99100  1.000 45.47315  ? 269 GLU B OE1  1 
ATOM   4528 O OE2  . GLU B 1 269 ? 105.28600 130.82000 75.15000  1.000 47.26504  ? 269 GLU B OE2  1 
ATOM   4529 N N    . GLY B 1 270 ? 110.22500 126.42200 76.94600  1.000 39.28406  ? 270 GLY B N    1 
ATOM   4530 C CA   . GLY B 1 270 ? 111.65300 126.21800 77.09700  1.000 34.00627  ? 270 GLY B CA   1 
ATOM   4531 C C    . GLY B 1 270 ? 112.17100 125.14800 76.16000  1.000 38.26142  ? 270 GLY B C    1 
ATOM   4532 O O    . GLY B 1 270 ? 113.19500 125.32500 75.50000  1.000 40.95274  ? 270 GLY B O    1 
ATOM   4533 N N    . CYS B 1 271 ? 111.45200 124.02600 76.07200  1.000 39.61602  ? 271 CYS B N    1 
ATOM   4534 C CA   . CYS B 1 271 ? 111.89300 122.93800 75.20500  1.000 33.66584  ? 271 CYS B CA   1 
ATOM   4535 C C    . CYS B 1 271 ? 111.88100 123.35200 73.73800  1.000 35.68709  ? 271 CYS B C    1 
ATOM   4536 O O    . CYS B 1 271 ? 112.82800 123.05900 72.99600  1.000 40.81288  ? 271 CYS B O    1 
ATOM   4537 C CB   . CYS B 1 271 ? 111.02000 121.70100 75.41900  1.000 31.90818  ? 271 CYS B CB   1 
ATOM   4538 S SG   . CYS B 1 271 ? 111.22000 120.91400 77.03300  1.000 52.19655  ? 271 CYS B SG   1 
ATOM   4539 N N    . VAL B 1 272 ? 110.82300 124.03700 73.29600  1.000 36.21498  ? 272 VAL B N    1 
ATOM   4540 C CA   . VAL B 1 272 ? 110.76000 124.39300 71.87800  1.000 35.50601  ? 272 VAL B CA   1 
ATOM   4541 C C    . VAL B 1 272 ? 111.86400 125.38600 71.52000  1.000 40.29307  ? 272 VAL B C    1 
ATOM   4542 O O    . VAL B 1 272 ? 112.53200 125.25000 70.48100  1.000 40.10072  ? 272 VAL B O    1 
ATOM   4543 C CB   . VAL B 1 272 ? 109.36600 124.93600 71.51800  1.000 42.90881  ? 272 VAL B CB   1 
ATOM   4544 C CG1  . VAL B 1 272 ? 109.29700 125.27300 70.03800  1.000 35.07019  ? 272 VAL B CG1  1 
ATOM   4545 C CG2  . VAL B 1 272 ? 108.29500 123.92000 71.87800  1.000 37.53451  ? 272 VAL B CG2  1 
ATOM   4546 N N    . ASN B 1 273 ? 112.11000 126.37300 72.38800  1.000 44.52469  ? 273 ASN B N    1 
ATOM   4547 C CA   . ASN B 1 273 ? 113.16800 127.33600 72.09900  1.000 40.98845  ? 273 ASN B CA   1 
ATOM   4548 C C    . ASN B 1 273 ? 114.54300 126.68400 72.16700  1.000 39.84808  ? 273 ASN B C    1 
ATOM   4549 O O    . ASN B 1 273 ? 115.43100 127.01800 71.37500  1.000 40.37914  ? 273 ASN B O    1 
ATOM   4550 C CB   . ASN B 1 273 ? 113.08800 128.52200 73.06100  1.000 42.75719  ? 273 ASN B CB   1 
ATOM   4551 C CG   . ASN B 1 273 ? 111.89500 129.41700 72.78900  1.000 42.83100  ? 273 ASN B CG   1 
ATOM   4552 O OD1  . ASN B 1 273 ? 111.45400 129.55400 71.64800  1.000 42.19866  ? 273 ASN B OD1  1 
ATOM   4553 N ND2  . ASN B 1 273 ? 111.36800 130.03500 73.83800  1.000 41.24278  ? 273 ASN B ND2  1 
ATOM   4554 N N    . GLY B 1 274 ? 114.74000 125.75100 73.10000  1.000 45.40469  ? 274 GLY B N    1 
ATOM   4555 C CA   . GLY B 1 274 ? 116.00700 125.04500 73.16000  1.000 40.64103  ? 274 GLY B CA   1 
ATOM   4556 C C    . GLY B 1 274 ? 116.26400 124.20200 71.92800  1.000 40.85304  ? 274 GLY B C    1 
ATOM   4557 O O    . GLY B 1 274 ? 117.40500 124.07200 71.48100  1.000 43.09820  ? 274 GLY B O    1 
ATOM   4558 N N    . TYR B 1 275 ? 115.20800 123.61700 71.36000  1.000 41.18190  ? 275 TYR B N    1 
ATOM   4559 C CA   . TYR B 1 275 ? 115.40400 122.82600 70.15200  1.000 33.48256  ? 275 TYR B CA   1 
ATOM   4560 C C    . TYR B 1 275 ? 115.61300 123.69400 68.92000  1.000 38.21760  ? 275 TYR B C    1 
ATOM   4561 O O    . TYR B 1 275 ? 116.27000 123.25400 67.97000  1.000 35.48305  ? 275 TYR B O    1 
ATOM   4562 C CB   . TYR B 1 275 ? 114.22100 121.88900 69.91100  1.000 35.40265  ? 275 TYR B CB   1 
ATOM   4563 C CG   . TYR B 1 275 ? 114.45100 120.94200 68.75300  1.000 37.17671  ? 275 TYR B CG   1 
ATOM   4564 C CD1  . TYR B 1 275 ? 115.26000 119.82200 68.89500  1.000 39.12332  ? 275 TYR B CD1  1 
ATOM   4565 C CD2  . TYR B 1 275 ? 113.88300 121.18400 67.51000  1.000 32.55743  ? 275 TYR B CD2  1 
ATOM   4566 C CE1  . TYR B 1 275 ? 115.47800 118.96000 67.83700  1.000 30.83245  ? 275 TYR B CE1  1 
ATOM   4567 C CE2  . TYR B 1 275 ? 114.09800 120.32900 66.44800  1.000 33.61635  ? 275 TYR B CE2  1 
ATOM   4568 C CZ   . TYR B 1 275 ? 114.89500 119.22000 66.61600  1.000 35.16003  ? 275 TYR B CZ   1 
ATOM   4569 O OH   . TYR B 1 275 ? 115.10800 118.36800 65.55800  1.000 34.46688  ? 275 TYR B OH   1 
ATOM   4570 N N    . LEU B 1 276 ? 115.08600 124.91800 68.90400  1.000 48.10855  ? 276 LEU B N    1 
ATOM   4571 C CA   . LEU B 1 276 ? 115.22000 125.74500 67.71100  1.000 46.67539  ? 276 LEU B CA   1 
ATOM   4572 C C    . LEU B 1 276 ? 116.34100 126.77400 67.79800  1.000 51.96786  ? 276 LEU B C    1 
ATOM   4573 O O    . LEU B 1 276 ? 116.59300 127.47000 66.81000  1.000 53.74320  ? 276 LEU B O    1 
ATOM   4574 C CB   . LEU B 1 276 ? 113.89900 126.45400 67.39700  1.000 50.67165  ? 276 LEU B CB   1 
ATOM   4575 C CG   . LEU B 1 276 ? 112.87300 125.61300 66.63600  1.000 49.20810  ? 276 LEU B CG   1 
ATOM   4576 C CD1  . LEU B 1 276 ? 111.51100 126.28600 66.63800  1.000 50.63226  ? 276 LEU B CD1  1 
ATOM   4577 C CD2  . LEU B 1 276 ? 113.34500 125.34700 65.21500  1.000 47.22584  ? 276 LEU B CD2  1 
ATOM   4578 N N    . ARG B 1 277 ? 117.02800 126.88500 68.93200  1.000 60.17109  ? 277 ARG B N    1 
ATOM   4579 C CA   . ARG B 1 277 ? 118.13100 127.83000 69.01100  1.000 58.49332  ? 277 ARG B CA   1 
ATOM   4580 C C    . ARG B 1 277 ? 119.30200 127.35900 68.15300  1.000 59.36136  ? 277 ARG B C    1 
ATOM   4581 O O    . ARG B 1 277 ? 119.42900 126.17900 67.81600  1.000 62.47497  ? 277 ARG B O    1 
ATOM   4582 C CB   . ARG B 1 277 ? 118.59100 128.02500 70.45500  1.000 57.49332  ? 277 ARG B CB   1 
ATOM   4583 C CG   . ARG B 1 277 ? 119.67300 127.05600 70.90000  1.000 59.04746  ? 277 ARG B CG   1 
ATOM   4584 C CD   . ARG B 1 277 ? 120.19800 127.40500 72.28600  1.000 60.63599  ? 277 ARG B CD   1 
ATOM   4585 N NE   . ARG B 1 277 ? 119.28900 127.00500 73.35400  1.000 63.42557  ? 277 ARG B NE   1 
ATOM   4586 C CZ   . ARG B 1 277 ? 118.42100 127.81600 73.94300  1.000 64.08110  ? 277 ARG B CZ   1 
ATOM   4587 N NH1  . ARG B 1 277 ? 118.31200 129.08700 73.58900  1.000 60.75387  ? 277 ARG B NH1  1 
ATOM   4588 N NH2  . ARG B 1 277 ? 117.64700 127.34300 74.91400  1.000 61.91566  ? 277 ARG B NH2  1 
ATOM   4589 N N    . CYS B 1 278 ? 120.16800 128.30400 67.80200  1.000 70.64179  ? 278 CYS B N    1 
ATOM   4590 C CA   . CYS B 1 278 ? 121.32800 128.01100 66.96800  1.000 72.33848  ? 278 CYS B CA   1 
ATOM   4591 C C    . CYS B 1 278 ? 122.47400 127.44100 67.79700  1.000 72.32090  ? 278 CYS B C    1 
ATOM   4592 O O    . CYS B 1 278 ? 123.50900 127.05100 67.25700  1.000 71.56112  ? 278 CYS B O    1 
ATOM   4593 C CB   . CYS B 1 278 ? 121.78800 129.27000 66.23100  1.000 71.18694  ? 278 CYS B CB   1 
ATOM   4594 S SG   . CYS B 1 278 ? 120.44600 130.36000 65.70400  1.000 77.00877  ? 278 CYS B SG   1 
ATOM   4595 N N    . VAL B 1 298 ? 113.47600 124.02300 82.57700  1.000 59.29427  ? 298 VAL B N    1 
ATOM   4596 C CA   . VAL B 1 298 ? 112.95000 122.89500 81.82100  1.000 62.22278  ? 298 VAL B CA   1 
ATOM   4597 C C    . VAL B 1 298 ? 112.75100 121.69500 82.73900  1.000 60.76242  ? 298 VAL B C    1 
ATOM   4598 O O    . VAL B 1 298 ? 111.63800 121.19300 82.88400  1.000 63.45825  ? 298 VAL B O    1 
ATOM   4599 C CB   . VAL B 1 298 ? 113.87000 122.53200 80.64500  1.000 61.39129  ? 298 VAL B CB   1 
ATOM   4600 C CG1  . VAL B 1 298 ? 113.36300 121.28400 79.94300  1.000 57.94102  ? 298 VAL B CG1  1 
ATOM   4601 C CG2  . VAL B 1 298 ? 113.96900 123.69500 79.67100  1.000 58.69325  ? 298 VAL B CG2  1 
ATOM   4602 N N    . TYR B 1 299 ? 113.84500 121.23400 83.34900  1.000 63.21011  ? 299 TYR B N    1 
ATOM   4603 C CA   . TYR B 1 299 ? 113.79400 120.04200 84.18900  1.000 64.29212  ? 299 TYR B CA   1 
ATOM   4604 C C    . TYR B 1 299 ? 112.68300 120.14900 85.22800  1.000 64.32354  ? 299 TYR B C    1 
ATOM   4605 O O    . TYR B 1 299 ? 111.75400 119.33200 85.26100  1.000 65.68796  ? 299 TYR B O    1 
ATOM   4606 C CB   . TYR B 1 299 ? 115.14600 119.83600 84.87600  1.000 64.49879  ? 299 TYR B CB   1 
ATOM   4607 C CG   . TYR B 1 299 ? 116.09900 118.91900 84.14400  1.000 66.36454  ? 299 TYR B CG   1 
ATOM   4608 C CD1  . TYR B 1 299 ? 115.97300 117.54200 84.23500  1.000 66.53028  ? 299 TYR B CD1  1 
ATOM   4609 C CD2  . TYR B 1 299 ? 117.14000 119.43200 83.38300  1.000 65.90184  ? 299 TYR B CD2  1 
ATOM   4610 C CE1  . TYR B 1 299 ? 116.84500 116.69700 83.57600  1.000 65.82144  ? 299 TYR B CE1  1 
ATOM   4611 C CE2  . TYR B 1 299 ? 118.02000 118.59600 82.72000  1.000 65.79277  ? 299 TYR B CE2  1 
ATOM   4612 C CZ   . TYR B 1 299 ? 117.86700 117.22900 82.82000  1.000 67.07949  ? 299 TYR B CZ   1 
ATOM   4613 O OH   . TYR B 1 299 ? 118.73900 116.39000 82.16500  1.000 67.62766  ? 299 TYR B OH   1 
ATOM   4614 N N    . LYS B 1 300 ? 112.76900 121.16800 86.08600  1.000 65.64119  ? 300 LYS B N    1 
ATOM   4615 C CA   . LYS B 1 300 ? 111.82400 121.29600 87.19000  1.000 69.58208  ? 300 LYS B CA   1 
ATOM   4616 C C    . LYS B 1 300 ? 110.39100 121.39700 86.68700  1.000 67.86947  ? 300 LYS B C    1 
ATOM   4617 O O    . LYS B 1 300 ? 109.47100 120.85300 87.30700  1.000 64.72284  ? 300 LYS B O    1 
ATOM   4618 C CB   . LYS B 1 300 ? 112.18000 122.51200 88.04600  1.000 63.14217  ? 300 LYS B CB   1 
ATOM   4619 N N    . GLY B 1 301 ? 110.19000 122.05200 85.54200  1.000 56.96771  ? 301 GLY B N    1 
ATOM   4620 C CA   . GLY B 1 301 ? 108.83700 122.29900 85.07200  1.000 53.12804  ? 301 GLY B CA   1 
ATOM   4621 C C    . GLY B 1 301 ? 108.02500 121.02600 84.94300  1.000 55.81571  ? 301 GLY B C    1 
ATOM   4622 O O    . GLY B 1 301 ? 106.87700 120.96000 85.38700  1.000 57.43959  ? 301 GLY B O    1 
ATOM   4623 N N    . TYR B 1 302 ? 108.60800 119.99700 84.33400  1.000 56.11673  ? 302 TYR B N    1 
ATOM   4624 C CA   . TYR B 1 302 ? 107.89100 118.73800 84.18700  1.000 58.61959  ? 302 TYR B CA   1 
ATOM   4625 C C    . TYR B 1 302 ? 108.15200 117.78400 85.34500  1.000 59.53002  ? 302 TYR B C    1 
ATOM   4626 O O    . TYR B 1 302 ? 107.29600 116.94400 85.64500  1.000 59.17001  ? 302 TYR B O    1 
ATOM   4627 C CB   . TYR B 1 302 ? 108.24000 118.07400 82.84700  1.000 55.20192  ? 302 TYR B CB   1 
ATOM   4628 C CG   . TYR B 1 302 ? 109.67400 117.61600 82.69400  1.000 57.55805  ? 302 TYR B CG   1 
ATOM   4629 C CD1  . TYR B 1 302 ? 110.14000 116.48400 83.35000  1.000 57.83997  ? 302 TYR B CD1  1 
ATOM   4630 C CD2  . TYR B 1 302 ? 110.55800 118.30500 81.87500  1.000 54.56156  ? 302 TYR B CD2  1 
ATOM   4631 C CE1  . TYR B 1 302 ? 111.44500 116.06200 83.20700  1.000 56.92089  ? 302 TYR B CE1  1 
ATOM   4632 C CE2  . TYR B 1 302 ? 111.86500 117.88900 81.72500  1.000 55.10259  ? 302 TYR B CE2  1 
ATOM   4633 C CZ   . TYR B 1 302 ? 112.30300 116.76700 82.39300  1.000 56.32063  ? 302 TYR B CZ   1 
ATOM   4634 O OH   . TYR B 1 302 ? 113.60300 116.34500 82.24900  1.000 58.98695  ? 302 TYR B OH   1 
ATOM   4635 N N    . ARG B 1 303 ? 109.30200 117.90200 86.01700  1.000 62.04001  ? 303 ARG B N    1 
ATOM   4636 C CA   . ARG B 1 303 ? 109.58400 117.00300 87.13200  1.000 63.50726  ? 303 ARG B CA   1 
ATOM   4637 C C    . ARG B 1 303 ? 108.64100 117.24800 88.30400  1.000 64.45100  ? 303 ARG B C    1 
ATOM   4638 O O    . ARG B 1 303 ? 108.15000 116.29400 88.91800  1.000 63.71309  ? 303 ARG B O    1 
ATOM   4639 C CB   . ARG B 1 303 ? 111.03800 117.14200 87.57900  1.000 64.61809  ? 303 ARG B CB   1 
ATOM   4640 C CG   . ARG B 1 303 ? 111.39300 116.22600 88.74200  1.000 67.38711  ? 303 ARG B CG   1 
ATOM   4641 C CD   . ARG B 1 303 ? 112.88800 116.17800 89.00800  1.000 69.16648  ? 303 ARG B CD   1 
ATOM   4642 N NE   . ARG B 1 303 ? 113.61300 115.53200 87.92200  1.000 71.28226  ? 303 ARG B NE   1 
ATOM   4643 C CZ   . ARG B 1 303 ? 114.37800 116.16300 87.04400  1.000 68.44338  ? 303 ARG B CZ   1 
ATOM   4644 N NH1  . ARG B 1 303 ? 114.54700 117.47400 87.08900  1.000 65.47798  ? 303 ARG B NH1  1 
ATOM   4645 N NH2  . ARG B 1 303 ? 114.99400 115.45900 86.09800  1.000 67.20896  ? 303 ARG B NH2  1 
ATOM   4646 N N    . SER B 1 304 ? 108.37800 118.51400 88.63500  1.000 64.31647  ? 304 SER B N    1 
ATOM   4647 C CA   . SER B 1 304 ? 107.52300 118.80600 89.78100  1.000 62.77015  ? 304 SER B CA   1 
ATOM   4648 C C    . SER B 1 304 ? 106.11500 118.26800 89.56500  1.000 62.85395  ? 304 SER B C    1 
ATOM   4649 O O    . SER B 1 304 ? 105.48600 117.75900 90.50000  1.000 59.81070  ? 304 SER B O    1 
ATOM   4650 C CB   . SER B 1 304 ? 107.49200 120.31100 90.04200  1.000 60.30908  ? 304 SER B CB   1 
ATOM   4651 O OG   . SER B 1 304 ? 108.78000 120.88100 89.88400  1.000 61.74547  ? 304 SER B OG   1 
ATOM   4652 N N    . ALA B 1 305 ? 105.60400 118.37100 88.33800  1.000 58.11338  ? 305 ALA B N    1 
ATOM   4653 C CA   . ALA B 1 305 ? 104.28500 117.82600 88.03900  1.000 56.49715  ? 305 ALA B CA   1 
ATOM   4654 C C    . ALA B 1 305 ? 104.30800 116.30300 87.99200  1.000 53.74963  ? 305 ALA B C    1 
ATOM   4655 O O    . ALA B 1 305 ? 103.34500 115.65000 88.41200  1.000 56.20101  ? 305 ALA B O    1 
ATOM   4656 C CB   . ALA B 1 305 ? 103.76800 118.39700 86.72000  1.000 52.18234  ? 305 ALA B CB   1 
ATOM   4657 N N    . VAL B 1 306 ? 105.39700 115.71700 87.48600  1.000 49.15084  ? 306 VAL B N    1 
ATOM   4658 C CA   . VAL B 1 306 ? 105.50200 114.26100 87.39400  1.000 50.38496  ? 306 VAL B CA   1 
ATOM   4659 C C    . VAL B 1 306 ? 105.97600 113.60800 88.68300  1.000 54.12564  ? 306 VAL B C    1 
ATOM   4660 O O    . VAL B 1 306 ? 105.86400 112.38300 88.82100  1.000 53.88955  ? 306 VAL B O    1 
ATOM   4661 C CB   . VAL B 1 306 ? 106.43900 113.89200 86.22600  1.000 50.88345  ? 306 VAL B CB   1 
ATOM   4662 C CG1  . VAL B 1 306 ? 106.97700 112.47800 86.37500  1.000 48.58813  ? 306 VAL B CG1  1 
ATOM   4663 C CG2  . VAL B 1 306 ? 105.71300 114.05100 84.89700  1.000 49.44626  ? 306 VAL B CG2  1 
ATOM   4664 N N    . GLU B 1 307 ? 106.46500 114.38300 89.64700  1.000 58.26877  ? 307 GLU B N    1 
ATOM   4665 C CA   . GLU B 1 307 ? 106.98400 113.84700 90.90300  1.000 57.20000  ? 307 GLU B CA   1 
ATOM   4666 C C    . GLU B 1 307 ? 106.30600 114.50800 92.09800  1.000 59.13865  ? 307 GLU B C    1 
ATOM   4667 O O    . GLU B 1 307 ? 106.95900 115.04500 92.99500  1.000 60.48044  ? 307 GLU B O    1 
ATOM   4668 C CB   . GLU B 1 307 ? 108.49700 114.02400 90.98000  1.000 55.64018  ? 307 GLU B CB   1 
ATOM   4669 N N    . SER B 1 308 ? 104.96900 114.47800 92.12900  1.000 56.72575  ? 308 SER B N    1 
ATOM   4670 C CA   . SER B 1 308 ? 104.26600 115.04400 93.27500  1.000 59.13609  ? 308 SER B CA   1 
ATOM   4671 C C    . SER B 1 308 ? 102.98000 114.31000 93.64200  1.000 55.34005  ? 308 SER B C    1 
ATOM   4672 O O    . SER B 1 308 ? 102.24600 114.80300 94.50600  1.000 56.04664  ? 308 SER B O    1 
ATOM   4673 C CB   . SER B 1 308 ? 103.94600 116.52400 93.02100  1.000 58.45940  ? 308 SER B CB   1 
ATOM   4674 O OG   . SER B 1 308 ? 102.64200 116.67900 92.49000  1.000 56.68309  ? 308 SER B OG   1 
ATOM   4675 N N    . THR B 1 309 ? 102.68600 113.15100 93.04800  1.000 55.22901  ? 309 THR B N    1 
ATOM   4676 C CA   . THR B 1 309 ? 101.43700 112.45500 93.35400  1.000 58.68669  ? 309 THR B CA   1 
ATOM   4677 C C    . THR B 1 309 ? 101.32700 112.14200 94.84200  1.000 55.32835  ? 309 THR B C    1 
ATOM   4678 O O    . THR B 1 309 ? 100.25000 112.27600 95.43900  1.000 55.59698  ? 309 THR B O    1 
ATOM   4679 C CB   . THR B 1 309 ? 101.33600 111.17200 92.52900  1.000 60.66956  ? 309 THR B CB   1 
ATOM   4680 O OG1  . THR B 1 309 ? 101.90900 111.39000 91.23500  1.000 59.10377  ? 309 THR B OG1  1 
ATOM   4681 C CG2  . THR B 1 309 ? 99.88200  110.75800 92.36800  1.000 56.25709  ? 309 THR B CG2  1 
ATOM   4682 N N    . SER B 1 310 ? 102.43800 111.74500 95.46300  1.000 49.21247  ? 310 SER B N    1 
ATOM   4683 C CA   . SER B 1 310 ? 102.41100 111.43100 96.88600  1.000 55.81323  ? 310 SER B CA   1 
ATOM   4684 C C    . SER B 1 310 ? 102.08100 112.66700 97.71000  1.000 56.07340  ? 310 SER B C    1 
ATOM   4685 O O    . SER B 1 310 ? 101.34400 112.58300 98.70200  1.000 54.65093  ? 310 SER B O    1 
ATOM   4686 C CB   . SER B 1 310 ? 103.75100 110.83600 97.31700  1.000 54.64435  ? 310 SER B CB   1 
ATOM   4687 O OG   . SER B 1 310 ? 104.83200 111.59300 96.80000  1.000 55.89186  ? 310 SER B OG   1 
ATOM   4688 N N    . GLN B 1 311 ? 102.63300 113.82300 97.33300  1.000 48.00373  ? 311 GLN B N    1 
ATOM   4689 C CA   . GLN B 1 311 ? 102.34300 115.03000 98.09500  1.000 46.86184  ? 311 GLN B CA   1 
ATOM   4690 C C    . GLN B 1 311 ? 100.86600 115.38900 97.99800  1.000 42.96244  ? 311 GLN B C    1 
ATOM   4691 O O    . GLN B 1 311 ? 100.25800 115.80600 98.99200  1.000 44.98165  ? 311 GLN B O    1 
ATOM   4692 C CB   . GLN B 1 311 ? 103.21300 116.18500 97.60100  1.000 47.61137  ? 311 GLN B CB   1 
ATOM   4693 C CG   . GLN B 1 311 ? 103.09100 117.45500 98.42600  1.000 51.05770  ? 311 GLN B CG   1 
ATOM   4694 C CD   . GLN B 1 311 ? 104.08900 118.51800 98.01100  1.000 52.09706  ? 311 GLN B CD   1 
ATOM   4695 O OE1  . GLN B 1 311 ? 104.94500 118.28200 97.16000  1.000 51.19851  ? 311 GLN B OE1  1 
ATOM   4696 N NE2  . GLN B 1 311 ? 103.98200 119.69700 98.61200  1.000 44.91257  ? 311 GLN B NE2  1 
ATOM   4697 N N    . GLU B 1 312 ? 100.24700 115.16300 96.83300  1.000 36.61811  ? 312 GLU B N    1 
ATOM   4698 C CA   . GLU B 1 312 ? 98.83600  115.49600 96.70300  1.000 40.32655  ? 312 GLU B CA   1 
ATOM   4699 C C    . GLU B 1 312 ? 97.95000  114.46700 97.38000  1.000 44.17382  ? 312 GLU B C    1 
ATOM   4700 O O    . GLU B 1 312 ? 96.87800  114.82700 97.87900  1.000 46.98174  ? 312 GLU B O    1 
ATOM   4701 C CB   . GLU B 1 312 ? 98.42200  115.63100 95.23200  1.000 39.42287  ? 312 GLU B CB   1 
ATOM   4702 C CG   . GLU B 1 312 ? 98.79100  116.95700 94.58600  1.000 46.57088  ? 312 GLU B CG   1 
ATOM   4703 C CD   . GLU B 1 312 ? 99.75400  116.81100 93.42600  1.000 50.94693  ? 312 GLU B CD   1 
ATOM   4704 O OE1  . GLU B 1 312 ? 99.88300  117.77300 92.64000  1.000 49.09637  ? 312 GLU B OE1  1 
ATOM   4705 O OE2  . GLU B 1 312 ? 100.35600 115.73000 93.27700  1.000 50.37336  ? 312 GLU B OE2  1 
ATOM   4706 N N    . GLU B 1 313 ? 98.45200  113.24900 97.58000  1.000 42.39555  ? 313 GLU B N    1 
ATOM   4707 C CA   . GLU B 1 313 ? 97.65000  112.25800 98.28200  1.000 36.66126  ? 313 GLU B CA   1 
ATOM   4708 C C    . GLU B 1 313 ? 97.74200  112.45800 99.78500  1.000 34.92438  ? 313 GLU B C    1 
ATOM   4709 O O    . GLU B 1 313 ? 96.74800  112.27200 100.49500 1.000 38.95043  ? 313 GLU B O    1 
ATOM   4710 C CB   . GLU B 1 313 ? 98.09800  110.84600 97.90300  1.000 42.18657  ? 313 GLU B CB   1 
ATOM   4711 C CG   . GLU B 1 313 ? 98.08900  110.57000 96.40900  1.000 43.54552  ? 313 GLU B CG   1 
ATOM   4712 C CD   . GLU B 1 313 ? 96.71000  110.22600 95.88500  1.000 46.98762  ? 313 GLU B CD   1 
ATOM   4713 O OE1  . GLU B 1 313 ? 95.72100  110.45700 96.61100  1.000 45.10114  ? 313 GLU B OE1  1 
ATOM   4714 O OE2  . GLU B 1 313 ? 96.61300  109.73000 94.74300  1.000 44.50360  ? 313 GLU B OE2  1 
ATOM   4715 N N    . SER B 1 314 ? 98.89600  112.90400 100.27900 1.000 26.73516  ? 314 SER B N    1 
ATOM   4716 C CA   . SER B 1 314 ? 98.99500  113.21600 101.69900 1.000 27.70153  ? 314 SER B CA   1 
ATOM   4717 C C    . SER B 1 314 ? 98.21200  114.48300 102.02800 1.000 27.38457  ? 314 SER B C    1 
ATOM   4718 O O    . SER B 1 314 ? 97.50100  114.53800 103.04200 1.000 29.97011  ? 314 SER B O    1 
ATOM   4719 C CB   . SER B 1 314 ? 100.46000 113.35900 102.10800 1.000 28.75538  ? 314 SER B CB   1 
ATOM   4720 O OG   . SER B 1 314 ? 101.07100 114.45500 101.45200 1.000 35.19853  ? 314 SER B OG   1 
ATOM   4721 N N    . LEU B 1 315 ? 98.30200  115.50400 101.16700 1.000 27.54358  ? 315 LEU B N    1 
ATOM   4722 C CA   . LEU B 1 315 ? 97.51000  116.70900 101.38200 1.000 21.44465  ? 315 LEU B CA   1 
ATOM   4723 C C    . LEU B 1 315 ? 96.01700  116.42700 101.27400 1.000 24.43556  ? 315 LEU B C    1 
ATOM   4724 O O    . LEU B 1 315 ? 95.21600  117.10500 101.92700 1.000 33.39362  ? 315 LEU B O    1 
ATOM   4725 C CB   . LEU B 1 315 ? 97.91900  117.79700 100.39000 1.000 24.01776  ? 315 LEU B CB   1 
ATOM   4726 C CG   . LEU B 1 315 ? 99.17700  118.59100 100.74500 1.000 21.98532  ? 315 LEU B CG   1 
ATOM   4727 C CD1  . LEU B 1 315 ? 99.56600  119.52600 99.61100  1.000 18.92492  ? 315 LEU B CD1  1 
ATOM   4728 C CD2  . LEU B 1 315 ? 98.98600  119.35900 102.04100 1.000 21.54803  ? 315 LEU B CD2  1 
ATOM   4729 N N    . MET B 1 316 ? 95.61700  115.43500 100.46900 1.000 16.30324  ? 316 MET B N    1 
ATOM   4730 C CA   . MET B 1 316 ? 94.20800  115.07000 100.41600 1.000 18.68005  ? 316 MET B CA   1 
ATOM   4731 C C    . MET B 1 316 ? 93.78700  114.20100 101.59100 1.000 26.47261  ? 316 MET B C    1 
ATOM   4732 O O    . MET B 1 316 ? 92.60300  114.18900 101.94200 1.000 30.45369  ? 316 MET B O    1 
ATOM   4733 C CB   . MET B 1 316 ? 93.89300  114.34200 99.10900  1.000 24.54864  ? 316 MET B CB   1 
ATOM   4734 C CG   . MET B 1 316 ? 92.46700  114.53500 98.63000  1.000 20.74931  ? 316 MET B CG   1 
ATOM   4735 S SD   . MET B 1 316 ? 91.47800  113.03500 98.74800  1.000 36.02166  ? 316 MET B SD   1 
ATOM   4736 C CE   . MET B 1 316 ? 91.94500  112.20200 97.23700  1.000 32.26670  ? 316 MET B CE   1 
ATOM   4737 N N    . SER B 1 317 ? 94.72400  113.47800 102.20600 1.000 34.27847  ? 317 SER B N    1 
ATOM   4738 C CA   . SER B 1 317 ? 94.39700  112.72800 103.41300 1.000 22.99518  ? 317 SER B CA   1 
ATOM   4739 C C    . SER B 1 317 ? 94.27200  113.64100 104.62400 1.000 26.81819  ? 317 SER B C    1 
ATOM   4740 O O    . SER B 1 317 ? 93.52000  113.32800 105.55200 1.000 27.70095  ? 317 SER B O    1 
ATOM   4741 C CB   . SER B 1 317 ? 95.45300  111.65500 103.67800 1.000 19.27393  ? 317 SER B CB   1 
ATOM   4742 O OG   . SER B 1 317 ? 96.75800  112.20300 103.65000 1.000 29.64376  ? 317 SER B OG   1 
ATOM   4743 N N    . PHE B 1 318 ? 94.99100  114.76600 104.63500 1.000 28.87040  ? 318 PHE B N    1 
ATOM   4744 C CA   . PHE B 1 318 ? 94.86100  115.71000 105.74000 1.000 14.04714  ? 318 PHE B CA   1 
ATOM   4745 C C    . PHE B 1 318 ? 93.66600  116.64700 105.59300 1.000 19.85027  ? 318 PHE B C    1 
ATOM   4746 O O    . PHE B 1 318 ? 93.21300  117.20600 106.59500 1.000 14.14445  ? 318 PHE B O    1 
ATOM   4747 C CB   . PHE B 1 318 ? 96.13200  116.55200 105.88000 1.000 10.22826  ? 318 PHE B CB   1 
ATOM   4748 C CG   . PHE B 1 318 ? 97.36400  115.75200 106.17200 1.000 12.61049  ? 318 PHE B CG   1 
ATOM   4749 C CD1  . PHE B 1 318 ? 97.29800  114.60900 106.94600 1.000 16.53949  ? 318 PHE B CD1  1 
ATOM   4750 C CD2  . PHE B 1 318 ? 98.59300  116.14900 105.67700 1.000 14.27050  ? 318 PHE B CD2  1 
ATOM   4751 C CE1  . PHE B 1 318 ? 98.43400  113.87400 107.21800 1.000 14.22433  ? 318 PHE B CE1  1 
ATOM   4752 C CE2  . PHE B 1 318 ? 99.73200  115.41800 105.94500 1.000 9.32458   ? 318 PHE B CE2  1 
ATOM   4753 C CZ   . PHE B 1 318 ? 99.65200  114.27900 106.71600 1.000 13.09580  ? 318 PHE B CZ   1 
ATOM   4754 N N    . ALA B 1 319 ? 93.14400  116.82900 104.37900 1.000 22.33095  ? 319 ALA B N    1 
ATOM   4755 C CA   . ALA B 1 319 ? 92.06700  117.78800 104.16200 1.000 4.68034   ? 319 ALA B CA   1 
ATOM   4756 C C    . ALA B 1 319 ? 90.68900  117.24300 104.51200 1.000 20.44241  ? 319 ALA B C    1 
ATOM   4757 O O    . ALA B 1 319 ? 89.75400  118.03300 104.67600 1.000 30.34326  ? 319 ALA B O    1 
ATOM   4758 C CB   . ALA B 1 319 ? 92.07300  118.26200 102.70800 1.000 0.82483   ? 319 ALA B CB   1 
ATOM   4759 N N    . ILE B 1 320 ? 90.53600  115.92100 104.63700 1.000 25.84427  ? 320 ILE B N    1 
ATOM   4760 C CA   . ILE B 1 320 ? 89.23800  115.34600 104.98700 1.000 18.05277  ? 320 ILE B CA   1 
ATOM   4761 C C    . ILE B 1 320 ? 88.97000  115.38300 106.48000 1.000 27.03204  ? 320 ILE B C    1 
ATOM   4762 O O    . ILE B 1 320 ? 87.89600  114.95400 106.91900 1.000 29.12781  ? 320 ILE B O    1 
ATOM   4763 C CB   . ILE B 1 320 ? 89.11500  113.89500 104.48300 1.000 21.19676  ? 320 ILE B CB   1 
ATOM   4764 C CG1  . ILE B 1 320 ? 90.10900  112.98900 105.21000 1.000 27.87183  ? 320 ILE B CG1  1 
ATOM   4765 C CG2  . ILE B 1 320 ? 89.33100  113.83600 102.97800 1.000 21.32418  ? 320 ILE B CG2  1 
ATOM   4766 C CD1  . ILE B 1 320 ? 90.10300  111.56000 104.71700 1.000 26.80536  ? 320 ILE B CD1  1 
ATOM   4767 N N    . TRP B 1 321 ? 89.91300  115.88700 107.27400 1.000 24.87809  ? 321 TRP B N    1 
ATOM   4768 C CA   . TRP B 1 321 ? 89.76100  115.98800 108.71700 1.000 12.15762  ? 321 TRP B CA   1 
ATOM   4769 C C    . TRP B 1 321 ? 89.33900  117.37800 109.16800 1.000 19.33415  ? 321 TRP B C    1 
ATOM   4770 O O    . TRP B 1 321 ? 88.83000  117.52300 110.28400 1.000 23.30716  ? 321 TRP B O    1 
ATOM   4771 C CB   . TRP B 1 321 ? 91.08600  115.63400 109.40400 1.000 15.65920  ? 321 TRP B CB   1 
ATOM   4772 C CG   . TRP B 1 321 ? 91.23900  114.19800 109.79500 1.000 17.69948  ? 321 TRP B CG   1 
ATOM   4773 C CD1  . TRP B 1 321 ? 91.80600  113.20600 109.05000 1.000 20.46800  ? 321 TRP B CD1  1 
ATOM   4774 C CD2  . TRP B 1 321 ? 90.85700  113.59600 111.03700 1.000 22.44492  ? 321 TRP B CD2  1 
ATOM   4775 N NE1  . TRP B 1 321 ? 91.78400  112.02200 109.74300 1.000 15.39983  ? 321 TRP B NE1  1 
ATOM   4776 C CE2  . TRP B 1 321 ? 91.20700  112.23400 110.96600 1.000 24.31890  ? 321 TRP B CE2  1 
ATOM   4777 C CE3  . TRP B 1 321 ? 90.24400  114.07500 112.19900 1.000 17.01786  ? 321 TRP B CE3  1 
ATOM   4778 C CZ2  . TRP B 1 321 ? 90.96700  111.34700 112.01100 1.000 15.88482  ? 321 TRP B CZ2  1 
ATOM   4779 C CZ3  . TRP B 1 321 ? 90.00800  113.19300 113.23400 1.000 14.57465  ? 321 TRP B CZ3  1 
ATOM   4780 C CH2  . TRP B 1 321 ? 90.36800  111.84500 113.13300 1.000 17.73028  ? 321 TRP B CH2  1 
ATOM   4781 N N    . GLU B 1 322 ? 89.53700  118.39100 108.32700 1.000 25.64649  ? 322 GLU B N    1 
ATOM   4782 C CA   . GLU B 1 322 ? 89.34900  119.79700 108.65500 1.000 20.49813  ? 322 GLU B CA   1 
ATOM   4783 C C    . GLU B 1 322 ? 87.88300  120.20100 108.50600 1.000 21.29256  ? 322 GLU B C    1 
ATOM   4784 O O    . GLU B 1 322 ? 87.18900  119.70800 107.61400 1.000 30.02686  ? 322 GLU B O    1 
ATOM   4785 C CB   . GLU B 1 322 ? 90.22300  120.66200 107.75300 1.000 18.16143  ? 322 GLU B CB   1 
ATOM   4786 C CG   . GLU B 1 322 ? 91.71000  120.43200 107.95400 1.000 14.06528  ? 322 GLU B CG   1 
ATOM   4787 C CD   . GLU B 1 322 ? 92.56300  121.19100 106.96100 1.000 22.76921  ? 322 GLU B CD   1 
ATOM   4788 O OE1  . GLU B 1 322 ? 92.01400  121.66500 105.94600 1.000 29.12166  ? 322 GLU B OE1  1 
ATOM   4789 O OE2  . GLU B 1 322 ? 93.78300  121.31100 107.19200 1.000 17.87865  ? 322 GLU B OE2  1 
ATOM   4790 N N    . PRO B 1 323 ? 87.39100  121.08900 109.36500 1.000 26.61102  ? 323 PRO B N    1 
ATOM   4791 C CA   . PRO B 1 323 ? 85.99500  121.53500 109.26800 1.000 33.82114  ? 323 PRO B CA   1 
ATOM   4792 C C    . PRO B 1 323 ? 85.80300  122.51400 108.12400 1.000 33.12820  ? 323 PRO B C    1 
ATOM   4793 O O    . PRO B 1 323 ? 86.77900  123.05500 107.58400 1.000 33.55222  ? 323 PRO B O    1 
ATOM   4794 C CB   . PRO B 1 323 ? 85.75300  122.20800 110.62700 1.000 30.53478  ? 323 PRO B CB   1 
ATOM   4795 C CG   . PRO B 1 323 ? 87.10500  122.69100 111.02700 1.000 24.73750  ? 323 PRO B CG   1 
ATOM   4796 C CD   . PRO B 1 323 ? 88.05000  121.61400 110.57300 1.000 18.20364  ? 323 PRO B CD   1 
ATOM   4797 N N    . PRO B 1 324 ? 84.55700  122.76600 107.72300 1.000 32.91308  ? 324 PRO B N    1 
ATOM   4798 C CA   . PRO B 1 324 ? 84.30200  123.75200 106.66500 1.000 36.36915  ? 324 PRO B CA   1 
ATOM   4799 C C    . PRO B 1 324 ? 84.78400  125.14100 107.05800 1.000 39.69556  ? 324 PRO B C    1 
ATOM   4800 O O    . PRO B 1 324 ? 84.60100  125.58500 108.19300 1.000 38.81684  ? 324 PRO B O    1 
ATOM   4801 C CB   . PRO B 1 324 ? 82.77800  123.71500 106.50600 1.000 30.25626  ? 324 PRO B CB   1 
ATOM   4802 C CG   . PRO B 1 324 ? 82.37500  122.38200 107.02800 1.000 36.30146  ? 324 PRO B CG   1 
ATOM   4803 C CD   . PRO B 1 324 ? 83.32600  122.08200 108.14800 1.000 33.08436  ? 324 PRO B CD   1 
ATOM   4804 N N    . HIS B 1 325 ? 85.40400  125.83100 106.10300 1.000 27.77810  ? 325 HIS B N    1 
ATOM   4805 C CA   . HIS B 1 325 ? 85.93200  127.16200 106.36300 1.000 20.65679  ? 325 HIS B CA   1 
ATOM   4806 C C    . HIS B 1 325 ? 86.06800  127.92200 105.05100 1.000 28.87200  ? 325 HIS B C    1 
ATOM   4807 O O    . HIS B 1 325 ? 86.21900  127.32400 103.98400 1.000 37.44939  ? 325 HIS B O    1 
ATOM   4808 C CB   . HIS B 1 325 ? 87.28800  127.09200 107.07200 1.000 22.83636  ? 325 HIS B CB   1 
ATOM   4809 C CG   . HIS B 1 325 ? 88.41000  126.66300 106.17900 1.000 26.60388  ? 325 HIS B CG   1 
ATOM   4810 N ND1  . HIS B 1 325 ? 88.69300  125.33900 105.92500 1.000 26.20393  ? 325 HIS B ND1  1 
ATOM   4811 C CD2  . HIS B 1 325 ? 89.31300  127.38200 105.47500 1.000 21.56943  ? 325 HIS B CD2  1 
ATOM   4812 C CE1  . HIS B 1 325 ? 89.72400  125.26100 105.10300 1.000 18.46872  ? 325 HIS B CE1  1 
ATOM   4813 N NE2  . HIS B 1 325 ? 90.11900  126.48700 104.81500 1.000 19.92240  ? 325 HIS B NE2  1 
ATOM   4814 N N    . GLY B 1 326 ? 86.00900  129.24800 105.15100 1.000 35.21532  ? 326 GLY B N    1 
ATOM   4815 C CA   . GLY B 1 326 ? 86.25200  130.13100 104.03400 1.000 32.86632  ? 326 GLY B CA   1 
ATOM   4816 C C    . GLY B 1 326 ? 85.41500  129.85000 102.80200 1.000 38.00085  ? 326 GLY B C    1 
ATOM   4817 O O    . GLY B 1 326 ? 84.19000  129.71000 102.86800 1.000 37.07493  ? 326 GLY B O    1 
ATOM   4818 N N    . PRO B 1 327 ? 86.07500  129.76900 101.64200 1.000 42.25895  ? 327 PRO B N    1 
ATOM   4819 C CA   . PRO B 1 327 ? 85.33900  129.53200 100.39000 1.000 36.85540  ? 327 PRO B CA   1 
ATOM   4820 C C    . PRO B 1 327 ? 84.73100  128.14700 100.28600 1.000 38.82148  ? 327 PRO B C    1 
ATOM   4821 O O    . PRO B 1 327 ? 83.83100  127.94800 99.46100  1.000 42.23030  ? 327 PRO B O    1 
ATOM   4822 C CB   . PRO B 1 327 ? 86.40900  129.74600 99.30800  1.000 32.31454  ? 327 PRO B CB   1 
ATOM   4823 C CG   . PRO B 1 327 ? 87.50500  130.50800 99.98800  1.000 31.11966  ? 327 PRO B CG   1 
ATOM   4824 C CD   . PRO B 1 327 ? 87.50300  130.01700 101.39700 1.000 38.68676  ? 327 PRO B CD   1 
ATOM   4825 N N    . TYR B 1 328 ? 85.18900  127.18800 101.08200 1.000 30.54695  ? 328 TYR B N    1 
ATOM   4826 C CA   . TYR B 1 328 ? 84.73600  125.80300 100.99700 1.000 26.03704  ? 328 TYR B CA   1 
ATOM   4827 C C    . TYR B 1 328 ? 83.74200  125.58000 102.13000 1.000 36.63580  ? 328 TYR B C    1 
ATOM   4828 O O    . TYR B 1 328 ? 84.13200  125.38600 103.28300 1.000 44.53486  ? 328 TYR B O    1 
ATOM   4829 C CB   . TYR B 1 328 ? 85.92200  124.85100 101.08700 1.000 29.27297  ? 328 TYR B CB   1 
ATOM   4830 C CG   . TYR B 1 328 ? 87.20500  125.43600 100.54200 1.000 29.88174  ? 328 TYR B CG   1 
ATOM   4831 C CD1  . TYR B 1 328 ? 87.51600  125.35200 99.19300  1.000 32.00680  ? 328 TYR B CD1  1 
ATOM   4832 C CD2  . TYR B 1 328 ? 88.10400  126.08200 101.38000 1.000 32.71826  ? 328 TYR B CD2  1 
ATOM   4833 C CE1  . TYR B 1 328 ? 88.68600  125.89200 98.69500  1.000 31.42597  ? 328 TYR B CE1  1 
ATOM   4834 C CE2  . TYR B 1 328 ? 89.27500  126.62300 100.89200 1.000 28.83132  ? 328 TYR B CE2  1 
ATOM   4835 C CZ   . TYR B 1 328 ? 89.56200  126.52600 99.54900  1.000 33.51382  ? 328 TYR B CZ   1 
ATOM   4836 O OH   . TYR B 1 328 ? 90.73000  127.06300 99.06300  1.000 34.83388  ? 328 TYR B OH   1 
ATOM   4837 N N    . LYS B 1 329 ? 82.45000  125.59900 101.79800 1.000 42.87448  ? 329 LYS B N    1 
ATOM   4838 C CA   . LYS B 1 329 ? 81.40200  125.56200 102.80600 1.000 45.90288  ? 329 LYS B CA   1 
ATOM   4839 C C    . LYS B 1 329 ? 80.63200  124.25200 102.86000 1.000 49.47438  ? 329 LYS B C    1 
ATOM   4840 O O    . LYS B 1 329 ? 80.02500  123.95900 103.89400 1.000 52.34037  ? 329 LYS B O    1 
ATOM   4841 C CB   . LYS B 1 329 ? 80.40500  126.70800 102.57800 1.000 49.31409  ? 329 LYS B CB   1 
ATOM   4842 C CG   . LYS B 1 329 ? 80.30300  127.16200 101.13400 1.000 50.71745  ? 329 LYS B CG   1 
ATOM   4843 C CD   . LYS B 1 329 ? 79.61800  128.51400 101.03000 1.000 51.75757  ? 329 LYS B CD   1 
ATOM   4844 C CE   . LYS B 1 329 ? 80.60500  129.64900 101.23600 1.000 49.60757  ? 329 LYS B CE   1 
ATOM   4845 N NZ   . LYS B 1 329 ? 81.75700  129.55600 100.29900 1.000 49.12343  ? 329 LYS B NZ   1 
ATOM   4846 N N    . SER B 1 330 ? 80.63300  123.46500 101.78800 1.000 48.88701  ? 330 SER B N    1 
ATOM   4847 C CA   . SER B 1 330 ? 79.96700  122.17400 101.83500 1.000 49.38515  ? 330 SER B CA   1 
ATOM   4848 C C    . SER B 1 330 ? 80.64600  121.27400 102.86400 1.000 52.39401  ? 330 SER B C    1 
ATOM   4849 O O    . SER B 1 330 ? 81.81100  121.46200 103.22100 1.000 52.05547  ? 330 SER B O    1 
ATOM   4850 C CB   . SER B 1 330 ? 79.98100  121.51100 100.45800 1.000 50.63463  ? 330 SER B CB   1 
ATOM   4851 O OG   . SER B 1 330 ? 79.88900  120.10200 100.57100 1.000 56.66651  ? 330 SER B OG   1 
ATOM   4852 N N    . PHE B 1 331 ? 79.89900  120.28300 103.34600 1.000 56.56064  ? 331 PHE B N    1 
ATOM   4853 C CA   . PHE B 1 331 ? 80.42400  119.38500 104.36400 1.000 57.03787  ? 331 PHE B CA   1 
ATOM   4854 C C    . PHE B 1 331 ? 81.19500  118.20700 103.78300 1.000 59.70264  ? 331 PHE B C    1 
ATOM   4855 O O    . PHE B 1 331 ? 81.83300  117.47100 104.54400 1.000 63.05291  ? 331 PHE B O    1 
ATOM   4856 C CB   . PHE B 1 331 ? 79.28700  118.86900 105.25000 1.000 57.99500  ? 331 PHE B CB   1 
ATOM   4857 C CG   . PHE B 1 331 ? 79.18800  119.57200 106.57400 1.000 61.79480  ? 331 PHE B CG   1 
ATOM   4858 C CD1  . PHE B 1 331 ? 78.56700  120.80500 106.67300 1.000 62.51359  ? 331 PHE B CD1  1 
ATOM   4859 C CD2  . PHE B 1 331 ? 79.72400  119.00400 107.71800 1.000 59.77338  ? 331 PHE B CD2  1 
ATOM   4860 C CE1  . PHE B 1 331 ? 78.47700  121.45700 107.88800 1.000 60.54708  ? 331 PHE B CE1  1 
ATOM   4861 C CE2  . PHE B 1 331 ? 79.63700  119.65100 108.93500 1.000 59.29045  ? 331 PHE B CE2  1 
ATOM   4862 C CZ   . PHE B 1 331 ? 79.01300  120.87900 109.02000 1.000 58.83784  ? 331 PHE B CZ   1 
ATOM   4863 N N    . ASN B 1 332 ? 81.15400  118.00700 102.45900 1.000 51.03026  ? 332 ASN B N    1 
ATOM   4864 C CA   . ASN B 1 332 ? 81.95600  116.98300 101.78500 1.000 46.22555  ? 332 ASN B CA   1 
ATOM   4865 C C    . ASN B 1 332 ? 82.50000  117.61700 100.50300 1.000 48.77295  ? 332 ASN B C    1 
ATOM   4866 O O    . ASN B 1 332 ? 81.93600  117.46100 99.41800  1.000 49.38696  ? 332 ASN B O    1 
ATOM   4867 C CB   . ASN B 1 332 ? 81.14000  115.72500 101.49400 1.000 47.81438  ? 332 ASN B CB   1 
ATOM   4868 C CG   . ASN B 1 332 ? 80.65500  115.04000 102.75400 1.000 53.21124  ? 332 ASN B CG   1 
ATOM   4869 O OD1  . ASN B 1 332 ? 79.51400  115.22700 103.17600 1.000 57.21965  ? 332 ASN B OD1  1 
ATOM   4870 N ND2  . ASN B 1 332 ? 81.52100  114.23800 103.36300 1.000 53.14702  ? 332 ASN B ND2  1 
ATOM   4871 N N    . TYR B 1 333 ? 83.60200  118.34100 100.63100 1.000 34.77009  ? 333 TYR B N    1 
ATOM   4872 C CA   . TYR B 1 333 ? 84.18000  119.00400 99.47200  1.000 36.38845  ? 333 TYR B CA   1 
ATOM   4873 C C    . TYR B 1 333 ? 84.79900  117.96700 98.53900  1.000 40.75908  ? 333 TYR B C    1 
ATOM   4874 O O    . TYR B 1 333 ? 85.52700  117.08100 99.00100  1.000 32.70787  ? 333 TYR B O    1 
ATOM   4875 C CB   . TYR B 1 333 ? 85.22100  120.03400 99.90200  1.000 32.20313  ? 333 TYR B CB   1 
ATOM   4876 C CG   . TYR B 1 333 ? 85.37600  121.17000 98.91700  1.000 30.82203  ? 333 TYR B CG   1 
ATOM   4877 C CD1  . TYR B 1 333 ? 84.34300  122.07500 98.71000  1.000 26.25298  ? 333 TYR B CD1  1 
ATOM   4878 C CD2  . TYR B 1 333 ? 86.54600  121.33400 98.19100  1.000 21.67603  ? 333 TYR B CD2  1 
ATOM   4879 C CE1  . TYR B 1 333 ? 84.47200  123.11100 97.81000  1.000 21.80062  ? 333 TYR B CE1  1 
ATOM   4880 C CE2  . TYR B 1 333 ? 86.68400  122.36700 97.28900  1.000 29.04269  ? 333 TYR B CE2  1 
ATOM   4881 C CZ   . TYR B 1 333 ? 85.64500  123.25300 97.10200  1.000 29.90109  ? 333 TYR B CZ   1 
ATOM   4882 O OH   . TYR B 1 333 ? 85.78000  124.28600 96.20300  1.000 28.78326  ? 333 TYR B OH   1 
ATOM   4883 N N    . PRO B 1 334 ? 84.54000  118.04100 97.23300  1.000 33.37755  ? 334 PRO B N    1 
ATOM   4884 C CA   . PRO B 1 334 ? 85.13700  117.07400 96.30000  1.000 23.01759  ? 334 PRO B CA   1 
ATOM   4885 C C    . PRO B 1 334 ? 86.63800  117.24900 96.12700  1.000 26.02404  ? 334 PRO B C    1 
ATOM   4886 O O    . PRO B 1 334 ? 87.09800  117.65600 95.05600  1.000 36.18919  ? 334 PRO B O    1 
ATOM   4887 C CB   . PRO B 1 334 ? 84.39000  117.35200 94.98900  1.000 31.59572  ? 334 PRO B CB   1 
ATOM   4888 C CG   . PRO B 1 334 ? 83.89500  118.75200 95.12800  1.000 26.34675  ? 334 PRO B CG   1 
ATOM   4889 C CD   . PRO B 1 334 ? 83.54700  118.90200 96.57100  1.000 23.80215  ? 334 PRO B CD   1 
ATOM   4890 N N    . TRP B 1 335 ? 87.41300  116.94100 97.16800  1.000 25.66688  ? 335 TRP B N    1 
ATOM   4891 C CA   . TRP B 1 335 ? 88.86400  117.06800 97.10300  1.000 22.92380  ? 335 TRP B CA   1 
ATOM   4892 C C    . TRP B 1 335 ? 89.51400  116.08800 96.13100  1.000 25.45502  ? 335 TRP B C    1 
ATOM   4893 O O    . TRP B 1 335 ? 90.69300  116.26300 95.80600  1.000 31.71389  ? 335 TRP B O    1 
ATOM   4894 C CB   . TRP B 1 335 ? 89.47300  116.88100 98.49700  1.000 20.20207  ? 335 TRP B CB   1 
ATOM   4895 C CG   . TRP B 1 335 ? 89.24700  118.03400 99.44100  1.000 25.67262  ? 335 TRP B CG   1 
ATOM   4896 C CD1  . TRP B 1 335 ? 88.64800  117.98300 100.66500 1.000 23.15072  ? 335 TRP B CD1  1 
ATOM   4897 C CD2  . TRP B 1 335 ? 89.63800  119.40000 99.24400  1.000 26.09412  ? 335 TRP B CD2  1 
ATOM   4898 N NE1  . TRP B 1 335 ? 88.62900  119.23100 101.23700 1.000 21.50233  ? 335 TRP B NE1  1 
ATOM   4899 C CE2  . TRP B 1 335 ? 89.23200  120.11800 100.38600 1.000 26.86751  ? 335 TRP B CE2  1 
ATOM   4900 C CE3  . TRP B 1 335 ? 90.28400  120.08600 98.21200  1.000 28.36021  ? 335 TRP B CE3  1 
ATOM   4901 C CZ2  . TRP B 1 335 ? 89.45100  121.48800 100.52300 1.000 25.20743  ? 335 TRP B CZ2  1 
ATOM   4902 C CZ3  . TRP B 1 335 ? 90.50100  121.44400 98.35100  1.000 24.52408  ? 335 TRP B CZ3  1 
ATOM   4903 C CH2  . TRP B 1 335 ? 90.08600  122.13000 99.49800  1.000 15.91631  ? 335 TRP B CH2  1 
ATOM   4904 N N    . LYS B 1 336 ? 88.79100  115.06500 95.66600  1.000 26.47274  ? 336 LYS B N    1 
ATOM   4905 C CA   . LYS B 1 336 ? 89.37200  114.07400 94.76300  1.000 30.95264  ? 336 LYS B CA   1 
ATOM   4906 C C    . LYS B 1 336 ? 89.38700  114.51400 93.30200  1.000 36.32457  ? 336 LYS B C    1 
ATOM   4907 O O    . LYS B 1 336 ? 90.20400  114.00400 92.52100  1.000 35.05809  ? 336 LYS B O    1 
ATOM   4908 C CB   . LYS B 1 336 ? 88.61900  112.75000 94.89400  1.000 32.73348  ? 336 LYS B CB   1 
ATOM   4909 C CG   . LYS B 1 336 ? 87.12200  112.90600 95.06800  1.000 32.16482  ? 336 LYS B CG   1 
ATOM   4910 C CD   . LYS B 1 336 ? 86.37200  111.71800 94.49900  1.000 33.94310  ? 336 LYS B CD   1 
ATOM   4911 C CE   . LYS B 1 336 ? 84.87400  111.86700 94.70800  1.000 40.72114  ? 336 LYS B CE   1 
ATOM   4912 N NZ   . LYS B 1 336 ? 84.41300  113.25400 94.42600  1.000 40.19010  ? 336 LYS B NZ   1 
ATOM   4913 N N    . ASN B 1 337 ? 88.53300  115.46400 92.91400  1.000 25.20822  ? 337 ASN B N    1 
ATOM   4914 C CA   . ASN B 1 337 ? 88.56100  115.93100 91.53500  1.000 27.60068  ? 337 ASN B CA   1 
ATOM   4915 C C    . ASN B 1 337 ? 89.79700  116.77400 91.25900  1.000 31.13211  ? 337 ASN B C    1 
ATOM   4916 O O    . ASN B 1 337 ? 90.25300  116.83900 90.11000  1.000 38.38682  ? 337 ASN B O    1 
ATOM   4917 C CB   . ASN B 1 337 ? 87.29300  116.72800 91.22500  1.000 30.00896  ? 337 ASN B CB   1 
ATOM   4918 C CG   . ASN B 1 337 ? 86.08400  115.83900 90.99800  1.000 35.17863  ? 337 ASN B CG   1 
ATOM   4919 O OD1  . ASN B 1 337 ? 85.80000  115.43300 89.87300  1.000 35.20937  ? 337 ASN B OD1  1 
ATOM   4920 N ND2  . ASN B 1 337 ? 85.36500  115.53400 92.07000  1.000 32.47522  ? 337 ASN B ND2  1 
ATOM   4921 N N    . TYR B 1 338 ? 90.40900  117.33100 92.30600  1.000 20.53464  ? 338 TYR B N    1 
ATOM   4922 C CA   . TYR B 1 338 ? 91.67100  118.03900 92.13600  1.000 21.08139  ? 338 TYR B CA   1 
ATOM   4923 C C    . TYR B 1 338 ? 92.78500  117.05800 91.80000  1.000 23.05529  ? 338 TYR B C    1 
ATOM   4924 O O    . TYR B 1 338 ? 93.62100  117.32300 90.92600  1.000 34.95167  ? 338 TYR B O    1 
ATOM   4925 C CB   . TYR B 1 338 ? 92.00800  118.80800 93.41400  1.000 22.19943  ? 338 TYR B CB   1 
ATOM   4926 C CG   . TYR B 1 338 ? 91.19100  120.06200 93.63600  1.000 26.80205  ? 338 TYR B CG   1 
ATOM   4927 C CD1  . TYR B 1 338 ? 89.93800  119.99700 94.23000  1.000 24.76652  ? 338 TYR B CD1  1 
ATOM   4928 C CD2  . TYR B 1 338 ? 91.67700  121.31100 93.27600  1.000 21.72245  ? 338 TYR B CD2  1 
ATOM   4929 C CE1  . TYR B 1 338 ? 89.18800  121.13400 94.44300  1.000 20.17426  ? 338 TYR B CE1  1 
ATOM   4930 C CE2  . TYR B 1 338 ? 90.93200  122.45500 93.48700  1.000 21.18859  ? 338 TYR B CE2  1 
ATOM   4931 C CZ   . TYR B 1 338 ? 89.68900  122.35900 94.07100  1.000 27.43102  ? 338 TYR B CZ   1 
ATOM   4932 O OH   . TYR B 1 338 ? 88.94200  123.49400 94.28300  1.000 32.21437  ? 338 TYR B OH   1 
ATOM   4933 N N    . VAL B 1 339 ? 92.77400  115.89100 92.44800  1.000 16.06190  ? 339 VAL B N    1 
ATOM   4934 C CA   . VAL B 1 339 ? 93.76200  114.86000 92.15300  1.000 25.39526  ? 339 VAL B CA   1 
ATOM   4935 C C    . VAL B 1 339 ? 93.53000  114.28300 90.76300  1.000 24.56830  ? 339 VAL B C    1 
ATOM   4936 O O    . VAL B 1 339 ? 94.48300  113.96900 90.03800  1.000 24.17800  ? 339 VAL B O    1 
ATOM   4937 C CB   . VAL B 1 339 ? 93.72300  113.76700 93.23700  1.000 27.78875  ? 339 VAL B CB   1 
ATOM   4938 C CG1  . VAL B 1 339 ? 94.66400  112.63200 92.88200  1.000 24.53572  ? 339 VAL B CG1  1 
ATOM   4939 C CG2  . VAL B 1 339 ? 94.07300  114.35200 94.59500  1.000 22.02148  ? 339 VAL B CG2  1 
ATOM   4940 N N    . LYS B 1 340 ? 92.26400  114.14500 90.36100  1.000 19.20908  ? 340 LYS B N    1 
ATOM   4941 C CA   . LYS B 1 340 ? 91.98800  113.64100 89.02000  1.000 22.49027  ? 340 LYS B CA   1 
ATOM   4942 C C    . LYS B 1 340 ? 92.48900  114.61000 87.94900  1.000 22.40186  ? 340 LYS B C    1 
ATOM   4943 O O    . LYS B 1 340 ? 93.08600  114.18900 86.94700  1.000 23.85443  ? 340 LYS B O    1 
ATOM   4944 C CB   . LYS B 1 340 ? 90.49000  113.37600 88.87100  1.000 19.14021  ? 340 LYS B CB   1 
ATOM   4945 C CG   . LYS B 1 340 ? 90.05800  112.91300 87.49400  1.000 29.71598  ? 340 LYS B CG   1 
ATOM   4946 C CD   . LYS B 1 340 ? 88.60700  113.27700 87.23200  1.000 36.62580  ? 340 LYS B CD   1 
ATOM   4947 C CE   . LYS B 1 340 ? 87.96900  112.32700 86.23200  1.000 28.20559  ? 340 LYS B CE   1 
ATOM   4948 N NZ   . LYS B 1 340 ? 86.71500  111.72600 86.76200  1.000 30.47933  ? 340 LYS B NZ   1 
ATOM   4949 N N    . LEU B 1 341 ? 92.30400  115.91500 88.16800  1.000 18.66324  ? 341 LEU B N    1 
ATOM   4950 C CA   . LEU B 1 341 ? 92.82700  116.89600 87.22100  1.000 24.37388  ? 341 LEU B CA   1 
ATOM   4951 C C    . LEU B 1 341 ? 94.35500  116.90200 87.21200  1.000 18.10768  ? 341 LEU B C    1 
ATOM   4952 O O    . LEU B 1 341 ? 94.97900  117.04100 86.14900  1.000 24.59454  ? 341 LEU B O    1 
ATOM   4953 C CB   . LEU B 1 341 ? 92.27500  118.28200 87.55800  1.000 26.86928  ? 341 LEU B CB   1 
ATOM   4954 C CG   . LEU B 1 341 ? 92.61700  119.45800 86.64000  1.000 22.75895  ? 341 LEU B CG   1 
ATOM   4955 C CD1  . LEU B 1 341 ? 92.09600  119.22100 85.23500  1.000 20.17892  ? 341 LEU B CD1  1 
ATOM   4956 C CD2  . LEU B 1 341 ? 92.05400  120.74700 87.20800  1.000 19.41270  ? 341 LEU B CD2  1 
ATOM   4957 N N    . SER B 1 342 ? 94.97600  116.72300 88.38000  1.000 17.40344  ? 342 SER B N    1 
ATOM   4958 C CA   . SER B 1 342 ? 96.43500  116.67700 88.43400  1.000 22.01170  ? 342 SER B CA   1 
ATOM   4959 C C    . SER B 1 342 ? 96.98400  115.47700 87.66400  1.000 27.85984  ? 342 SER B C    1 
ATOM   4960 O O    . SER B 1 342 ? 98.00000  115.58700 86.96500  1.000 28.66901  ? 342 SER B O    1 
ATOM   4961 C CB   . SER B 1 342 ? 96.89500  116.65200 89.89200  1.000 20.00567  ? 342 SER B CB   1 
ATOM   4962 O OG   . SER B 1 342 ? 98.30400  116.57000 89.98800  1.000 33.79515  ? 342 SER B OG   1 
ATOM   4963 N N    . GLY B 1 343 ? 96.31900  114.32400 87.76600  1.000 20.06795  ? 343 GLY B N    1 
ATOM   4964 C CA   . GLY B 1 343 ? 96.75200  113.17100 86.98900  1.000 12.49792  ? 343 GLY B CA   1 
ATOM   4965 C C    . GLY B 1 343 ? 96.56600  113.37800 85.49700  1.000 19.49238  ? 343 GLY B C    1 
ATOM   4966 O O    . GLY B 1 343 ? 97.42600  112.99600 84.68600  1.000 26.22313  ? 343 GLY B O    1 
ATOM   4967 N N    . ALA B 1 344 ? 95.45000  114.00300 85.11200  1.000 15.65123  ? 344 ALA B N    1 
ATOM   4968 C CA   . ALA B 1 344 ? 95.24800  114.32300 83.70500  1.000 17.24574  ? 344 ALA B CA   1 
ATOM   4969 C C    . ALA B 1 344 ? 96.37000  115.21100 83.18200  1.000 16.46303  ? 344 ALA B C    1 
ATOM   4970 O O    . ALA B 1 344 ? 96.79100  115.07600 82.02800  1.000 19.96775  ? 344 ALA B O    1 
ATOM   4971 C CB   . ALA B 1 344 ? 93.88900  114.99100 83.50400  1.000 16.41025  ? 344 ALA B CB   1 
ATOM   4972 N N    . LEU B 1 345 ? 96.86400  116.13200 84.01500  1.000 18.97862  ? 345 LEU B N    1 
ATOM   4973 C CA   . LEU B 1 345 ? 97.95800  116.99500 83.57200  1.000 21.35135  ? 345 LEU B CA   1 
ATOM   4974 C C    . LEU B 1 345 ? 99.30600  116.27300 83.55200  1.000 21.69243  ? 345 LEU B C    1 
ATOM   4975 O O    . LEU B 1 345 ? 100.16100 116.58000 82.70800  1.000 26.60900  ? 345 LEU B O    1 
ATOM   4976 C CB   . LEU B 1 345 ? 98.03900  118.23600 84.46100  1.000 28.55467  ? 345 LEU B CB   1 
ATOM   4977 C CG   . LEU B 1 345 ? 99.10500  119.26800 84.08300  1.000 26.36045  ? 345 LEU B CG   1 
ATOM   4978 C CD1  . LEU B 1 345 ? 98.63100  120.14100 82.93500  1.000 20.76534  ? 345 LEU B CD1  1 
ATOM   4979 C CD2  . LEU B 1 345 ? 99.47800  120.11900 85.28400  1.000 14.59038  ? 345 LEU B CD2  1 
ATOM   4980 N N    . LYS B 1 346 ? 99.51300  115.30300 84.44500  1.000 19.67929  ? 346 LYS B N    1 
ATOM   4981 C CA   . LYS B 1 346 ? 100.76700 114.55100 84.42000  1.000 21.69841  ? 346 LYS B CA   1 
ATOM   4982 C C    . LYS B 1 346 ? 100.86700 113.67800 83.17400  1.000 23.74741  ? 346 LYS B C    1 
ATOM   4983 O O    . LYS B 1 346 ? 101.96800 113.48400 82.61700  1.000 22.51023  ? 346 LYS B O    1 
ATOM   4984 C CB   . LYS B 1 346 ? 100.87200 113.69700 85.68300  1.000 25.06715  ? 346 LYS B CB   1 
ATOM   4985 C CG   . LYS B 1 346 ? 102.09900 112.81400 85.75800  1.000 32.71720  ? 346 LYS B CG   1 
ATOM   4986 C CD   . LYS B 1 346 ? 102.28900 112.28300 87.16600  1.000 30.66758  ? 346 LYS B CD   1 
ATOM   4987 C CE   . LYS B 1 346 ? 102.47000 110.77500 87.16700  1.000 34.05353  ? 346 LYS B CE   1 
ATOM   4988 N NZ   . LYS B 1 346 ? 103.30400 110.31500 88.31200  1.000 34.47721  ? 346 LYS B NZ   1 
ATOM   4989 N N    . HIS B 1 347 ? 99.71700  113.22300 82.66900  1.000 29.55733  ? 347 HIS B N    1 
ATOM   4990 C CA   . HIS B 1 347 ? 99.74800  112.42200 81.45200  1.000 22.37440  ? 347 HIS B CA   1 
ATOM   4991 C C    . HIS B 1 347 ? 100.21600 113.25300 80.26300  1.000 28.54646  ? 347 HIS B C    1 
ATOM   4992 O O    . HIS B 1 347 ? 100.87400 112.72600 79.35900  1.000 25.78377  ? 347 HIS B O    1 
ATOM   4993 C CB   . HIS B 1 347 ? 98.37200  111.82000 81.17600  1.000 18.92356  ? 347 HIS B CB   1 
ATOM   4994 C CG   . HIS B 1 347 ? 98.37700  110.76300 80.11500  1.000 29.29727  ? 347 HIS B CG   1 
ATOM   4995 N ND1  . HIS B 1 347 ? 97.60300  110.84700 78.97700  1.000 25.80714  ? 347 HIS B ND1  1 
ATOM   4996 C CD2  . HIS B 1 347 ? 99.06100  109.59900 80.01900  1.000 30.22263  ? 347 HIS B CD2  1 
ATOM   4997 C CE1  . HIS B 1 347 ? 97.81200  109.78100 78.22600  1.000 25.12585  ? 347 HIS B CE1  1 
ATOM   4998 N NE2  . HIS B 1 347 ? 98.69200  109.00800 78.83600  1.000 31.93491  ? 347 HIS B NE2  1 
ATOM   4999 N N    . CYS B 1 348 ? 99.88500  114.54500 80.24400  1.000 33.80661  ? 348 CYS B N    1 
ATOM   5000 C CA   . CYS B 1 348 ? 100.39900 115.44300 79.21700  1.000 31.61153  ? 348 CYS B CA   1 
ATOM   5001 C C    . CYS B 1 348 ? 101.85100 115.83900 79.46500  1.000 31.05846  ? 348 CYS B C    1 
ATOM   5002 O O    . CYS B 1 348 ? 102.59200 116.07700 78.50600  1.000 24.68222  ? 348 CYS B O    1 
ATOM   5003 C CB   . CYS B 1 348 ? 99.52800  116.69900 79.13600  1.000 30.92247  ? 348 CYS B CB   1 
ATOM   5004 S SG   . CYS B 1 348 ? 99.99800  117.86300 77.84700  1.000 52.88271  ? 348 CYS B SG   1 
ATOM   5005 N N    . ALA B 1 349 ? 102.27800 115.91700 80.72900  1.000 30.11643  ? 349 ALA B N    1 
ATOM   5006 C CA   . ALA B 1 349 ? 103.66100 116.30200 81.00500  1.000 24.44031  ? 349 ALA B CA   1 
ATOM   5007 C C    . ALA B 1 349 ? 104.66200 115.20600 80.64800  1.000 32.73377  ? 349 ALA B C    1 
ATOM   5008 O O    . ALA B 1 349 ? 105.85800 115.49900 80.46800  1.000 38.49840  ? 349 ALA B O    1 
ATOM   5009 C CB   . ALA B 1 349 ? 103.81900 116.68800 82.47600  1.000 23.68724  ? 349 ALA B CB   1 
ATOM   5010 N N    . PHE B 1 350 ? 104.20300 113.96400 80.48000  1.000 30.48647  ? 350 PHE B N    1 
ATOM   5011 C CA   . PHE B 1 350 ? 105.16100 112.93900 80.05900  1.000 27.15911  ? 350 PHE B CA   1 
ATOM   5012 C C    . PHE B 1 350 ? 105.65600 113.16200 78.62600  1.000 30.42340  ? 350 PHE B C    1 
ATOM   5013 O O    . PHE B 1 350 ? 106.80100 112.81000 78.30200  1.000 29.36625  ? 350 PHE B O    1 
ATOM   5014 C CB   . PHE B 1 350 ? 104.54400 111.54600 80.18100  1.000 26.55128  ? 350 PHE B CB   1 
ATOM   5015 C CG   . PHE B 1 350 ? 104.58400 110.98000 81.57000  1.000 36.77291  ? 350 PHE B CG   1 
ATOM   5016 C CD1  . PHE B 1 350 ? 105.72900 111.08000 82.33900  1.000 33.18084  ? 350 PHE B CD1  1 
ATOM   5017 C CD2  . PHE B 1 350 ? 103.48200 110.33600 82.10300  1.000 35.95913  ? 350 PHE B CD2  1 
ATOM   5018 C CE1  . PHE B 1 350 ? 105.77100 110.55600 83.61600  1.000 34.52604  ? 350 PHE B CE1  1 
ATOM   5019 C CE2  . PHE B 1 350 ? 103.51900 109.81000 83.37800  1.000 31.63082  ? 350 PHE B CE2  1 
ATOM   5020 C CZ   . PHE B 1 350 ? 104.66500 109.92000 84.13500  1.000 26.77228  ? 350 PHE B CZ   1 
ATOM   5021 N N    . THR B 1 351 ? 104.86600 113.82900 77.78200  1.000 28.19539  ? 351 THR B N    1 
ATOM   5022 C CA   . THR B 1 351 ? 105.34100 114.12700 76.43400  1.000 28.29382  ? 351 THR B CA   1 
ATOM   5023 C C    . THR B 1 351 ? 106.36200 115.26000 76.42500  1.000 28.47910  ? 351 THR B C    1 
ATOM   5024 O O    . THR B 1 351 ? 107.29100 115.24800 75.60800  1.000 29.57277  ? 351 THR B O    1 
ATOM   5025 C CB   . THR B 1 351 ? 104.16500 114.47200 75.52000  1.000 30.58695  ? 351 THR B CB   1 
ATOM   5026 O OG1  . THR B 1 351 ? 103.16200 113.45700 75.62700  1.000 33.81422  ? 351 THR B OG1  1 
ATOM   5027 C CG2  . THR B 1 351 ? 104.62300 114.56100 74.07400  1.000 28.57331  ? 351 THR B CG2  1 
ATOM   5028 N N    . VAL B 1 352 ? 106.23400 116.22400 77.33700  1.000 33.05005  ? 352 VAL B N    1 
ATOM   5029 C CA   . VAL B 1 352 ? 107.25800 117.25600 77.44300  1.000 31.77177  ? 352 VAL B CA   1 
ATOM   5030 C C    . VAL B 1 352 ? 108.54800 116.64900 77.96900  1.000 29.10272  ? 352 VAL B C    1 
ATOM   5031 O O    . VAL B 1 352 ? 109.64900 117.04400 77.55500  1.000 27.32729  ? 352 VAL B O    1 
ATOM   5032 C CB   . VAL B 1 352 ? 106.77100 118.41500 78.33200  1.000 33.16209  ? 352 VAL B CB   1 
ATOM   5033 C CG1  . VAL B 1 352 ? 107.68100 119.62200 78.17700  1.000 27.23277  ? 352 VAL B CG1  1 
ATOM   5034 C CG2  . VAL B 1 352 ? 105.33700 118.77900 77.99100  1.000 34.21043  ? 352 VAL B CG2  1 
ATOM   5035 N N    . MET B 1 353 ? 108.44200 115.66400 78.86400  1.000 35.07349  ? 353 MET B N    1 
ATOM   5036 C CA   . MET B 1 353 ? 109.64500 114.95600 79.29300  1.000 29.06304  ? 353 MET B CA   1 
ATOM   5037 C C    . MET B 1 353 ? 110.30200 114.23000 78.12200  1.000 30.86648  ? 353 MET B C    1 
ATOM   5038 O O    . MET B 1 353 ? 111.53400 114.23500 77.98500  1.000 33.48994  ? 353 MET B O    1 
ATOM   5039 C CB   . MET B 1 353 ? 109.30800 113.97500 80.41400  1.000 33.25025  ? 353 MET B CB   1 
ATOM   5040 C CG   . MET B 1 353 ? 110.36300 112.90700 80.63800  1.000 36.54998  ? 353 MET B CG   1 
ATOM   5041 S SD   . MET B 1 353 ? 110.51500 112.42900 82.36800  1.000 50.28177  ? 353 MET B SD   1 
ATOM   5042 C CE   . MET B 1 353 ? 111.47700 110.92700 82.21900  1.000 39.35629  ? 353 MET B CE   1 
ATOM   5043 N N    . ALA B 1 354 ? 109.49600 113.62600 77.24400  1.000 40.34700  ? 354 ALA B N    1 
ATOM   5044 C CA   . ALA B 1 354 ? 110.08400 112.95400 76.08600  1.000 30.12693  ? 354 ALA B CA   1 
ATOM   5045 C C    . ALA B 1 354 ? 110.70000 113.94200 75.09600  1.000 33.61687  ? 354 ALA B C    1 
ATOM   5046 O O    . ALA B 1 354 ? 111.70700 113.62400 74.45500  1.000 35.55293  ? 354 ALA B O    1 
ATOM   5047 C CB   . ALA B 1 354 ? 109.03400 112.09100 75.38800  1.000 26.10580  ? 354 ALA B CB   1 
ATOM   5048 N N    . LEU B 1 355 ? 110.16000 115.15900 74.99400  1.000 32.44086  ? 355 LEU B N    1 
ATOM   5049 C CA   . LEU B 1 355 ? 110.77900 116.14900 74.11100  1.000 28.69312  ? 355 LEU B CA   1 
ATOM   5050 C C    . LEU B 1 355 ? 112.09900 116.65400 74.68400  1.000 33.57096  ? 355 LEU B C    1 
ATOM   5051 O O    . LEU B 1 355 ? 113.07800 116.85500 73.94500  1.000 26.47682  ? 355 LEU B O    1 
ATOM   5052 C CB   . LEU B 1 355 ? 109.82400 117.31900 73.87300  1.000 35.79275  ? 355 LEU B CB   1 
ATOM   5053 C CG   . LEU B 1 355 ? 108.66300 117.12800 72.89800  1.000 34.92926  ? 355 LEU B CG   1 
ATOM   5054 C CD1  . LEU B 1 355 ? 107.60300 118.18900 73.13500  1.000 31.88044  ? 355 LEU B CD1  1 
ATOM   5055 C CD2  . LEU B 1 355 ? 109.15200 117.17200 71.46000  1.000 28.12338  ? 355 LEU B CD2  1 
ATOM   5056 N N    . HIS B 1 356 ? 112.16300 116.82100 76.00700  1.000 41.83734  ? 356 HIS B N    1 
ATOM   5057 C CA   . HIS B 1 356 ? 113.43100 117.19900 76.62000  1.000 33.93287  ? 356 HIS B CA   1 
ATOM   5058 C C    . HIS B 1 356 ? 114.46900 116.10200 76.44000  1.000 38.78480  ? 356 HIS B C    1 
ATOM   5059 O O    . HIS B 1 356 ? 115.65000 116.38600 76.20900  1.000 41.12585  ? 356 HIS B O    1 
ATOM   5060 C CB   . HIS B 1 356 ? 113.24200 117.51300 78.10100  1.000 39.09661  ? 356 HIS B CB   1 
ATOM   5061 C CG   . HIS B 1 356 ? 114.47400 118.05100 78.76000  1.000 48.69568  ? 356 HIS B CG   1 
ATOM   5062 N ND1  . HIS B 1 356 ? 115.33400 118.92400 78.12900  1.000 46.00442  ? 356 HIS B ND1  1 
ATOM   5063 C CD2  . HIS B 1 356 ? 114.99900 117.82700 79.98800  1.000 45.81597  ? 356 HIS B CD2  1 
ATOM   5064 C CE1  . HIS B 1 356 ? 116.33100 119.22200 78.94300  1.000 43.38209  ? 356 HIS B CE1  1 
ATOM   5065 N NE2  . HIS B 1 356 ? 116.15200 118.56900 80.07700  1.000 42.89863  ? 356 HIS B NE2  1 
ATOM   5066 N N    . GLY B 1 357 ? 114.05100 114.83900 76.53400  1.000 36.35594  ? 357 GLY B N    1 
ATOM   5067 C CA   . GLY B 1 357 ? 114.97800 113.76000 76.24200  1.000 35.44801  ? 357 GLY B CA   1 
ATOM   5068 C C    . GLY B 1 357 ? 115.37000 113.71000 74.77900  1.000 35.07339  ? 357 GLY B C    1 
ATOM   5069 O O    . GLY B 1 357 ? 116.45500 113.23200 74.43900  1.000 30.67131  ? 357 GLY B O    1 
ATOM   5070 N N    . CYS B 1 358 ? 114.50200 114.21300 73.89900  1.000 43.82396  ? 358 CYS B N    1 
ATOM   5071 C CA   . CYS B 1 358 ? 114.84600 114.31500 72.48500  1.000 38.20053  ? 358 CYS B CA   1 
ATOM   5072 C C    . CYS B 1 358 ? 115.91200 115.37400 72.24000  1.000 37.98403  ? 358 CYS B C    1 
ATOM   5073 O O    . CYS B 1 358 ? 116.70600 115.24500 71.30200  1.000 32.72105  ? 358 CYS B O    1 
ATOM   5074 C CB   . CYS B 1 358 ? 113.59500 114.62700 71.66300  1.000 40.18995  ? 358 CYS B CB   1 
ATOM   5075 S SG   . CYS B 1 358 ? 113.85300 114.69900 69.88000  1.000 51.69334  ? 358 CYS B SG   1 
ATOM   5076 N N    . ILE B 1 359 ? 115.94500 116.42600 73.06100  1.000 48.97608  ? 359 ILE B N    1 
ATOM   5077 C CA   . ILE B 1 359 ? 116.98100 117.44500 72.87900  1.000 44.14158  ? 359 ILE B CA   1 
ATOM   5078 C C    . ILE B 1 359 ? 118.36500 116.92800 73.27300  1.000 43.73247  ? 359 ILE B C    1 
ATOM   5079 O O    . ILE B 1 359 ? 119.37700 117.37000 72.71600  1.000 41.22047  ? 359 ILE B O    1 
ATOM   5080 C CB   . ILE B 1 359 ? 116.63300 118.72600 73.66100  1.000 47.28393  ? 359 ILE B CB   1 
ATOM   5081 C CG1  . ILE B 1 359 ? 115.48700 119.47900 72.98600  1.000 46.49084  ? 359 ILE B CG1  1 
ATOM   5082 C CG2  . ILE B 1 359 ? 117.85200 119.62500 73.78800  1.000 39.84811  ? 359 ILE B CG2  1 
ATOM   5083 C CD1  . ILE B 1 359 ? 114.71000 120.36600 73.92800  1.000 44.88203  ? 359 ILE B CD1  1 
ATOM   5084 N N    . LEU B 1 360 ? 118.44500 116.00100 74.23000  1.000 47.62623  ? 360 LEU B N    1 
ATOM   5085 C CA   . LEU B 1 360 ? 119.71400 115.53300 74.78000  1.000 44.04417  ? 360 LEU B CA   1 
ATOM   5086 C C    . LEU B 1 360 ? 120.18300 114.21000 74.17700  1.000 45.71416  ? 360 LEU B C    1 
ATOM   5087 O O    . LEU B 1 360 ? 120.80400 113.40400 74.87700  1.000 45.19787  ? 360 LEU B O    1 
ATOM   5088 C CB   . LEU B 1 360 ? 119.61200 115.40300 76.29900  1.000 42.90599  ? 360 LEU B CB   1 
ATOM   5089 C CG   . LEU B 1 360 ? 119.66100 116.68800 77.12400  1.000 45.85172  ? 360 LEU B CG   1 
ATOM   5090 C CD1  . LEU B 1 360 ? 119.24600 116.41300 78.55800  1.000 42.90508  ? 360 LEU B CD1  1 
ATOM   5091 C CD2  . LEU B 1 360 ? 121.04900 117.30000 77.07400  1.000 45.15843  ? 360 LEU B CD2  1 
ATOM   5092 N N    . SER B 1 361 ? 119.92100 113.97000 72.89800  1.000 49.60621  ? 361 SER B N    1 
ATOM   5093 C CA   . SER B 1 361 ? 120.21100 112.67600 72.30000  1.000 46.09985  ? 361 SER B CA   1 
ATOM   5094 C C    . SER B 1 361 ? 121.58900 112.65000 71.64000  1.000 46.50618  ? 361 SER B C    1 
ATOM   5095 O O    . SER B 1 361 ? 122.18300 113.68500 71.33100  1.000 48.41074  ? 361 SER B O    1 
ATOM   5096 C CB   . SER B 1 361 ? 119.14200 112.31300 71.27000  1.000 46.01323  ? 361 SER B CB   1 
ATOM   5097 O OG   . SER B 1 361 ? 118.03100 111.69100 71.88800  1.000 48.24742  ? 361 SER B OG   1 
ATOM   5098 N N    . GLU B 1 362 ? 122.09400 111.43000 71.43300  1.000 50.24524  ? 362 GLU B N    1 
ATOM   5099 C CA   . GLU B 1 362 ? 123.38600 111.25400 70.77600  1.000 48.74719  ? 362 GLU B CA   1 
ATOM   5100 C C    . GLU B 1 362 ? 123.30500 111.60600 69.29700  1.000 48.50955  ? 362 GLU B C    1 
ATOM   5101 O O    . GLU B 1 362 ? 124.20700 112.25600 68.75600  1.000 50.01088  ? 362 GLU B O    1 
ATOM   5102 C CB   . GLU B 1 362 ? 123.87500 109.81500 70.94600  1.000 47.61093  ? 362 GLU B CB   1 
ATOM   5103 C CG   . GLU B 1 362 ? 123.81900 109.28700 72.36800  1.000 50.43231  ? 362 GLU B CG   1 
ATOM   5104 C CD   . GLU B 1 362 ? 125.11800 109.49900 73.11600  1.000 53.25378  ? 362 GLU B CD   1 
ATOM   5105 O OE1  . GLU B 1 362 ? 126.10000 109.94500 72.48800  1.000 55.41012  ? 362 GLU B OE1  1 
ATOM   5106 O OE2  . GLU B 1 362 ? 125.15800 109.21700 74.33200  1.000 50.09685  ? 362 GLU B OE2  1 
ATOM   5107 N N    . ILE B 1 363 ? 122.24000 111.17700 68.62800  1.000 49.92932  ? 363 ILE B N    1 
ATOM   5108 C CA   . ILE B 1 363 ? 122.03800 111.42000 67.20500  1.000 51.45551  ? 363 ILE B CA   1 
ATOM   5109 C C    . ILE B 1 363 ? 121.17200 112.66200 67.05300  1.000 50.79634  ? 363 ILE B C    1 
ATOM   5110 O O    . ILE B 1 363 ? 120.07400 112.73600 67.61600  1.000 51.37750  ? 363 ILE B O    1 
ATOM   5111 C CB   . ILE B 1 363 ? 121.39700 110.20400 66.51800  1.000 50.49768  ? 363 ILE B CB   1 
ATOM   5112 C CG1  . ILE B 1 363 ? 122.36400 109.01800 66.52400  1.000 48.10551  ? 363 ILE B CG1  1 
ATOM   5113 C CG2  . ILE B 1 363 ? 120.97400 110.54900 65.10000  1.000 50.19111  ? 363 ILE B CG2  1 
ATOM   5114 C CD1  . ILE B 1 363 ? 121.71500 107.69700 66.86500  1.000 46.80124  ? 363 ILE B CD1  1 
ATOM   5115 N N    . GLN B 1 364 ? 121.66500 113.64100 66.29700  1.000 52.74725  ? 364 GLN B N    1 
ATOM   5116 C CA   . GLN B 1 364 ? 120.96700 114.90000 66.08200  1.000 50.25883  ? 364 GLN B CA   1 
ATOM   5117 C C    . GLN B 1 364 ? 120.85400 115.17000 64.58800  1.000 49.40885  ? 364 GLN B C    1 
ATOM   5118 O O    . GLN B 1 364 ? 121.40900 114.44800 63.75700  1.000 57.46375  ? 364 GLN B O    1 
ATOM   5119 C CB   . GLN B 1 364 ? 121.68000 116.06200 66.78400  1.000 49.14493  ? 364 GLN B CB   1 
ATOM   5120 C CG   . GLN B 1 364 ? 122.12000 115.74800 68.20200  1.000 50.95306  ? 364 GLN B CG   1 
ATOM   5121 C CD   . GLN B 1 364 ? 121.28400 116.46100 69.24400  1.000 51.27272  ? 364 GLN B CD   1 
ATOM   5122 O OE1  . GLN B 1 364 ? 120.87400 117.60400 69.05000  1.000 53.37046  ? 364 GLN B OE1  1 
ATOM   5123 N NE2  . GLN B 1 364 ? 121.02500 115.78700 70.35600  1.000 47.39962  ? 364 GLN B NE2  1 
ATOM   5124 N N    . ALA B 1 365 ? 120.12200 116.23100 64.24900  1.000 49.14903  ? 365 ALA B N    1 
ATOM   5125 C CA   . ALA B 1 365 ? 119.88500 116.60400 62.86500  1.000 50.89770  ? 365 ALA B CA   1 
ATOM   5126 C C    . ALA B 1 365 ? 120.62000 117.89300 62.50800  1.000 51.81863  ? 365 ALA B C    1 
ATOM   5127 O O    . ALA B 1 365 ? 120.91500 118.71200 63.38300  1.000 47.33554  ? 365 ALA B O    1 
ATOM   5128 C CB   . ALA B 1 365 ? 118.38700 116.78700 62.59100  1.000 47.12071  ? 365 ALA B CB   1 
ATOM   5129 N N    . PRO B 1 366 ? 120.93800 118.09400 61.23000  1.000 58.37761  ? 366 PRO B N    1 
ATOM   5130 C CA   . PRO B 1 366 ? 121.54300 119.36500 60.81200  1.000 59.02444  ? 366 PRO B CA   1 
ATOM   5131 C C    . PRO B 1 366 ? 120.59800 120.53600 61.04400  1.000 57.83102  ? 366 PRO B C    1 
ATOM   5132 O O    . PRO B 1 366 ? 119.40100 120.46100 60.75700  1.000 55.30838  ? 366 PRO B O    1 
ATOM   5133 C CB   . PRO B 1 366 ? 121.82600 119.15300 59.32000  1.000 53.58366  ? 366 PRO B CB   1 
ATOM   5134 C CG   . PRO B 1 366 ? 120.96000 118.00200 58.91700  1.000 54.42442  ? 366 PRO B CG   1 
ATOM   5135 C CD   . PRO B 1 366 ? 120.84900 117.13000 60.12200  1.000 51.62328  ? 366 PRO B CD   1 
ATOM   5136 N N    . GLU B 1 367 ? 121.15400 121.62900 61.57300  1.000 55.88714  ? 367 GLU B N    1 
ATOM   5137 C CA   . GLU B 1 367 ? 120.34400 122.79500 61.91500  1.000 57.25997  ? 367 GLU B CA   1 
ATOM   5138 C C    . GLU B 1 367 ? 119.62600 123.36100 60.69400  1.000 54.66078  ? 367 GLU B C    1 
ATOM   5139 O O    . GLU B 1 367 ? 118.48200 123.82600 60.79400  1.000 54.63177  ? 367 GLU B O    1 
ATOM   5140 C CB   . GLU B 1 367 ? 121.22300 123.86300 62.56400  1.000 55.85782  ? 367 GLU B CB   1 
ATOM   5141 C CG   . GLU B 1 367 ? 122.00200 123.36900 63.77500  1.000 57.61961  ? 367 GLU B CG   1 
ATOM   5142 C CD   . GLU B 1 367 ? 121.19500 123.41600 65.05800  1.000 60.69892  ? 367 GLU B CD   1 
ATOM   5143 O OE1  . GLU B 1 367 ? 120.10100 124.01800 65.05600  1.000 61.59465  ? 367 GLU B OE1  1 
ATOM   5144 O OE2  . GLU B 1 367 ? 121.65500 122.84800 66.07100  1.000 56.83399  ? 367 GLU B OE2  1 
ATOM   5145 N N    . GLU B 1 368 ? 120.28900 123.34200 59.53400  1.000 56.60450  ? 368 GLU B N    1 
ATOM   5146 C CA   . GLU B 1 368 ? 119.67900 123.88900 58.32600  1.000 58.52134  ? 368 GLU B CA   1 
ATOM   5147 C C    . GLU B 1 368 ? 118.34700 123.21400 58.02900  1.000 58.73124  ? 368 GLU B C    1 
ATOM   5148 O O    . GLU B 1 368 ? 117.40400 123.86400 57.56400  1.000 59.79194  ? 368 GLU B O    1 
ATOM   5149 C CB   . GLU B 1 368 ? 120.63100 123.74100 57.14000  1.000 57.92500  ? 368 GLU B CB   1 
ATOM   5150 C CG   . GLU B 1 368 ? 121.32700 122.39200 57.05500  1.000 61.29557  ? 368 GLU B CG   1 
ATOM   5151 C CD   . GLU B 1 368 ? 122.64900 122.36700 57.79500  1.000 64.09703  ? 368 GLU B CD   1 
ATOM   5152 O OE1  . GLU B 1 368 ? 122.98300 123.37200 58.45600  1.000 62.62538  ? 368 GLU B OE1  1 
ATOM   5153 O OE2  . GLU B 1 368 ? 123.35600 121.34000 57.71400  1.000 60.32884  ? 368 GLU B OE2  1 
ATOM   5154 N N    . ARG B 1 369 ? 118.25200 121.90800 58.28100  1.000 56.27176  ? 369 ARG B N    1 
ATOM   5155 C CA   . ARG B 1 369 ? 116.99000 121.21200 58.06200  1.000 54.96227  ? 369 ARG B CA   1 
ATOM   5156 C C    . ARG B 1 369 ? 115.94300 121.62300 59.09100  1.000 54.31679  ? 369 ARG B C    1 
ATOM   5157 O O    . ARG B 1 369 ? 114.76200 121.76700 58.75500  1.000 54.73690  ? 369 ARG B O    1 
ATOM   5158 C CB   . ARG B 1 369 ? 117.20900 119.70100 58.08700  1.000 55.07330  ? 369 ARG B CB   1 
ATOM   5159 C CG   . ARG B 1 369 ? 118.25700 119.21100 57.10200  1.000 54.09879  ? 369 ARG B CG   1 
ATOM   5160 C CD   . ARG B 1 369 ? 117.86100 117.87300 56.50200  1.000 52.87018  ? 369 ARG B CD   1 
ATOM   5161 N NE   . ARG B 1 369 ? 118.28900 117.74800 55.11400  1.000 57.95857  ? 369 ARG B NE   1 
ATOM   5162 C CZ   . ARG B 1 369 ? 118.94600 116.70600 54.62400  1.000 58.17403  ? 369 ARG B CZ   1 
ATOM   5163 N NH1  . ARG B 1 369 ? 119.26800 115.67200 55.38300  1.000 56.19907  ? 369 ARG B NH1  1 
ATOM   5164 N NH2  . ARG B 1 369 ? 119.28600 116.70000 53.33800  1.000 54.61113  ? 369 ARG B NH2  1 
ATOM   5165 N N    . ARG B 1 370 ? 116.35100 121.82400 60.34700  1.000 45.72965  ? 370 ARG B N    1 
ATOM   5166 C CA   . ARG B 1 370 ? 115.37700 122.20700 61.36500  1.000 47.03729  ? 370 ARG B CA   1 
ATOM   5167 C C    . ARG B 1 370 ? 114.83800 123.61100 61.13400  1.000 43.39797  ? 370 ARG B C    1 
ATOM   5168 O O    . ARG B 1 370 ? 113.71400 123.91400 61.55000  1.000 45.13375  ? 370 ARG B O    1 
ATOM   5169 C CB   . ARG B 1 370 ? 115.97900 122.11800 62.76800  1.000 48.08008  ? 370 ARG B CB   1 
ATOM   5170 C CG   . ARG B 1 370 ? 117.13500 121.15700 62.93900  1.000 43.64261  ? 370 ARG B CG   1 
ATOM   5171 C CD   . ARG B 1 370 ? 117.81300 121.41900 64.27200  1.000 41.70407  ? 370 ARG B CD   1 
ATOM   5172 N NE   . ARG B 1 370 ? 118.52900 120.25700 64.78000  1.000 47.23162  ? 370 ARG B NE   1 
ATOM   5173 C CZ   . ARG B 1 370 ? 118.80400 120.05200 66.06100  1.000 44.39432  ? 370 ARG B CZ   1 
ATOM   5174 N NH1  . ARG B 1 370 ? 118.43200 120.91300 66.99300  1.000 41.28820  ? 370 ARG B NH1  1 
ATOM   5175 N NH2  . ARG B 1 370 ? 119.47200 118.95900 66.41400  1.000 42.72165  ? 370 ARG B NH2  1 
ATOM   5176 N N    . GLN B 1 371 ? 115.60600 124.47700 60.47900  1.000 52.22525  ? 371 GLN B N    1 
ATOM   5177 C CA   . GLN B 1 371 ? 115.15500 125.85000 60.27700  1.000 50.61495  ? 371 GLN B CA   1 
ATOM   5178 C C    . GLN B 1 371 ? 114.13000 125.98500 59.15600  1.000 48.98971  ? 371 GLN B C    1 
ATOM   5179 O O    . GLN B 1 371 ? 113.75200 127.11000 58.81500  1.000 51.68163  ? 371 GLN B O    1 
ATOM   5180 C CB   . GLN B 1 371 ? 116.34800 126.77100 60.01000  1.000 45.90864  ? 371 GLN B CB   1 
ATOM   5181 C CG   . GLN B 1 371 ? 117.52300 126.53500 60.93800  1.000 52.05709  ? 371 GLN B CG   1 
ATOM   5182 C CD   . GLN B 1 371 ? 117.26500 127.05700 62.34000  1.000 53.02743  ? 371 GLN B CD   1 
ATOM   5183 O OE1  . GLN B 1 371 ? 116.74000 128.15500 62.51800  1.000 54.27574  ? 371 GLN B OE1  1 
ATOM   5184 N NE2  . GLN B 1 371 ? 117.63000 126.26700 63.34200  1.000 50.19462  ? 371 GLN B NE2  1 
ATOM   5185 N N    . VAL B 1 372 ? 113.68000 124.87400 58.57400  1.000 47.53693  ? 372 VAL B N    1 
ATOM   5186 C CA   . VAL B 1 372 ? 112.61000 124.92000 57.58400  1.000 47.71618  ? 372 VAL B CA   1 
ATOM   5187 C C    . VAL B 1 372 ? 111.21800 124.83200 58.20700  1.000 47.68869  ? 372 VAL B C    1 
ATOM   5188 O O    . VAL B 1 372 ? 110.22900 125.16100 57.53700  1.000 51.12309  ? 372 VAL B O    1 
ATOM   5189 C CB   . VAL B 1 372 ? 112.79600 123.79400 56.54900  1.000 47.63492  ? 372 VAL B CB   1 
ATOM   5190 C CG1  . VAL B 1 372 ? 111.60300 123.71600 55.61100  1.000 47.66109  ? 372 VAL B CG1  1 
ATOM   5191 C CG2  . VAL B 1 372 ? 114.07900 124.00400 55.76400  1.000 46.51359  ? 372 VAL B CG2  1 
ATOM   5192 N N    . PHE B 1 373 ? 111.11100 124.41300 59.47200  1.000 48.63349  ? 373 PHE B N    1 
ATOM   5193 C CA   . PHE B 1 373 ? 109.82400 124.22400 60.13500  1.000 52.04228  ? 373 PHE B CA   1 
ATOM   5194 C C    . PHE B 1 373 ? 109.64100 125.14200 61.34100  1.000 55.72373  ? 373 PHE B C    1 
ATOM   5195 O O    . PHE B 1 373 ? 108.77100 124.88700 62.17900  1.000 60.01328  ? 373 PHE B O    1 
ATOM   5196 C CB   . PHE B 1 373 ? 109.66000 122.76300 60.56300  1.000 49.24945  ? 373 PHE B CB   1 
ATOM   5197 C CG   . PHE B 1 373 ? 109.86600 121.77400 59.45200  1.000 53.74030  ? 373 PHE B CG   1 
ATOM   5198 C CD1  . PHE B 1 373 ? 111.12800 121.27500 59.17600  1.000 51.16595  ? 373 PHE B CD1  1 
ATOM   5199 C CD2  . PHE B 1 373 ? 108.79700 121.33300 58.69000  1.000 53.47191  ? 373 PHE B CD2  1 
ATOM   5200 C CE1  . PHE B 1 373 ? 111.32200 120.36100 58.15700  1.000 47.69557  ? 373 PHE B CE1  1 
ATOM   5201 C CE2  . PHE B 1 373 ? 108.98500 120.41900 57.67000  1.000 51.94091  ? 373 PHE B CE2  1 
ATOM   5202 C CZ   . PHE B 1 373 ? 110.24900 119.93300 57.40400  1.000 50.33975  ? 373 PHE B CZ   1 
ATOM   5203 N N    . ARG B 1 374 ? 110.43900 126.20500 61.44500  1.000 53.49460  ? 374 ARG B N    1 
ATOM   5204 C CA   . ARG B 1 374 ? 110.46300 127.02000 62.65900  1.000 56.00300  ? 374 ARG B CA   1 
ATOM   5205 C C    . ARG B 1 374 ? 109.09400 127.61600 62.98400  1.000 56.93556  ? 374 ARG B C    1 
ATOM   5206 O O    . ARG B 1 374 ? 108.63100 127.55400 64.13300  1.000 61.88004  ? 374 ARG B O    1 
ATOM   5207 C CB   . ARG B 1 374 ? 111.50800 128.12600 62.50300  1.000 52.84426  ? 374 ARG B CB   1 
ATOM   5208 C CG   . ARG B 1 374 ? 111.80600 128.90800 63.76800  1.000 55.56159  ? 374 ARG B CG   1 
ATOM   5209 C CD   . ARG B 1 374 ? 112.30500 130.30400 63.43000  1.000 57.70183  ? 374 ARG B CD   1 
ATOM   5210 N NE   . ARG B 1 374 ? 113.74400 130.43700 63.62300  1.000 61.47952  ? 374 ARG B NE   1 
ATOM   5211 C CZ   . ARG B 1 374 ? 114.35000 130.37600 64.80000  1.000 59.36352  ? 374 ARG B CZ   1 
ATOM   5212 N NH1  . ARG B 1 374 ? 113.67000 130.19300 65.91900  1.000 57.28012  ? 374 ARG B NH1  1 
ATOM   5213 N NH2  . ARG B 1 374 ? 115.67200 130.50500 64.85600  1.000 55.80106  ? 374 ARG B NH2  1 
ATOM   5214 N N    . GLN B 1 375 ? 108.43100 128.20000 61.98400  1.000 52.69795  ? 375 GLN B N    1 
ATOM   5215 C CA   . GLN B 1 375 ? 107.20500 128.95500 62.23500  1.000 54.58172  ? 375 GLN B CA   1 
ATOM   5216 C C    . GLN B 1 375 ? 106.11100 128.08100 62.84100  1.000 53.69288  ? 375 GLN B C    1 
ATOM   5217 O O    . GLN B 1 375 ? 105.47300 128.46500 63.83000  1.000 56.71229  ? 375 GLN B O    1 
ATOM   5218 C CB   . GLN B 1 375 ? 106.71100 129.60700 60.94100  1.000 52.78647  ? 375 GLN B CB   1 
ATOM   5219 C CG   . GLN B 1 375 ? 107.69900 130.54800 60.25900  1.000 56.04807  ? 375 GLN B CG   1 
ATOM   5220 C CD   . GLN B 1 375 ? 108.92200 129.83800 59.70600  1.000 62.53266  ? 375 GLN B CD   1 
ATOM   5221 O OE1  . GLN B 1 375 ? 108.89100 128.63500 59.44500  1.000 55.94904  ? 375 GLN B OE1  1 
ATOM   5222 N NE2  . GLN B 1 375 ? 110.00700 130.58400 59.52400  1.000 58.70788  ? 375 GLN B NE2  1 
ATOM   5223 N N    . GLU B 1 376 ? 105.87400 126.90400 62.25800  1.000 44.69018  ? 376 GLU B N    1 
ATOM   5224 C CA   . GLU B 1 376 ? 104.79000 126.05100 62.73600  1.000 46.59030  ? 376 GLU B CA   1 
ATOM   5225 C C    . GLU B 1 376 ? 105.04300 125.57100 64.15900  1.000 49.87213  ? 376 GLU B C    1 
ATOM   5226 O O    . GLU B 1 376 ? 104.12600 125.55500 64.99400  1.000 56.56549  ? 376 GLU B O    1 
ATOM   5227 C CB   . GLU B 1 376 ? 104.61100 124.86400 61.79200  1.000 48.95297  ? 376 GLU B CB   1 
ATOM   5228 C CG   . GLU B 1 376 ? 103.88500 125.20300 60.50200  1.000 49.04450  ? 376 GLU B CG   1 
ATOM   5229 C CD   . GLU B 1 376 ? 104.79500 125.84000 59.47600  1.000 50.30205  ? 376 GLU B CD   1 
ATOM   5230 O OE1  . GLU B 1 376 ? 106.02700 125.79300 59.66400  1.000 51.58752  ? 376 GLU B OE1  1 
ATOM   5231 O OE2  . GLU B 1 376 ? 104.28000 126.39000 58.48100  1.000 52.91058  ? 376 GLU B OE2  1 
ATOM   5232 N N    . LEU B 1 377 ? 106.28900 125.20700 64.46600  1.000 39.55129  ? 377 LEU B N    1 
ATOM   5233 C CA   . LEU B 1 377 ? 106.59800 124.72400 65.80600  1.000 45.54001  ? 377 LEU B CA   1 
ATOM   5234 C C    . LEU B 1 377 ? 106.44800 125.83900 66.83300  1.000 46.39675  ? 377 LEU B C    1 
ATOM   5235 O O    . LEU B 1 377 ? 105.91200 125.61800 67.93000  1.000 46.56505  ? 377 LEU B O    1 
ATOM   5236 C CB   . LEU B 1 377 ? 108.01000 124.13900 65.83500  1.000 50.97458  ? 377 LEU B CB   1 
ATOM   5237 C CG   . LEU B 1 377 ? 108.26300 122.94600 64.90700  1.000 47.98680  ? 377 LEU B CG   1 
ATOM   5238 C CD1  . LEU B 1 377 ? 109.72300 122.87500 64.49500  1.000 41.17392  ? 377 LEU B CD1  1 
ATOM   5239 C CD2  . LEU B 1 377 ? 107.83100 121.64600 65.56100  1.000 46.79127  ? 377 LEU B CD2  1 
ATOM   5240 N N    . GLN B 1 378 ? 106.87600 127.05400 66.48200  1.000 44.17563  ? 378 GLN B N    1 
ATOM   5241 C CA   . GLN B 1 378 ? 106.74100 128.15800 67.42500  1.000 45.67492  ? 378 GLN B CA   1 
ATOM   5242 C C    . GLN B 1 378 ? 105.27500 128.51400 67.64000  1.000 46.16981  ? 378 GLN B C    1 
ATOM   5243 O O    . GLN B 1 378 ? 104.86600 128.84000 68.76300  1.000 47.64401  ? 378 GLN B O    1 
ATOM   5244 C CB   . GLN B 1 378 ? 107.52400 129.37000 66.92500  1.000 44.56818  ? 378 GLN B CB   1 
ATOM   5245 C CG   . GLN B 1 378 ? 109.02600 129.17800 66.93100  1.000 46.99183  ? 378 GLN B CG   1 
ATOM   5246 C CD   . GLN B 1 378 ? 109.77700 130.49000 66.86700  1.000 53.47076  ? 378 GLN B CD   1 
ATOM   5247 O OE1  . GLN B 1 378 ? 110.58500 130.80000 67.74200  1.000 53.62460  ? 378 GLN B OE1  1 
ATOM   5248 N NE2  . GLN B 1 378 ? 109.51500 131.27200 65.82500  1.000 53.10106  ? 378 GLN B NE2  1 
ATOM   5249 N N    . ARG B 1 379 ? 104.46000 128.41400 66.58600  1.000 43.72776  ? 379 ARG B N    1 
ATOM   5250 C CA   . ARG B 1 379 ? 103.03100 128.66300 66.74100  1.000 42.00617  ? 379 ARG B CA   1 
ATOM   5251 C C    . ARG B 1 379 ? 102.39100 127.64000 67.67100  1.000 39.87069  ? 379 ARG B C    1 
ATOM   5252 O O    . ARG B 1 379 ? 101.59000 127.99900 68.54700  1.000 42.78261  ? 379 ARG B O    1 
ATOM   5253 C CB   . ARG B 1 379 ? 102.34500 128.65000 65.37500  1.000 37.76288  ? 379 ARG B CB   1 
ATOM   5254 C CG   . ARG B 1 379 ? 101.68700 129.96500 65.00100  1.000 39.71579  ? 379 ARG B CG   1 
ATOM   5255 C CD   . ARG B 1 379 ? 100.61400 129.75900 63.94800  1.000 43.08271  ? 379 ARG B CD   1 
ATOM   5256 N NE   . ARG B 1 379 ? 99.27100  129.88000 64.50300  1.000 50.73431  ? 379 ARG B NE   1 
ATOM   5257 C CZ   . ARG B 1 379 ? 98.16200  129.54200 63.85900  1.000 50.53575  ? 379 ARG B CZ   1 
ATOM   5258 N NH1  . ARG B 1 379 ? 98.19800  129.05400 62.63000  1.000 47.60185  ? 379 ARG B NH1  1 
ATOM   5259 N NH2  . ARG B 1 379 ? 96.98800  129.69500 64.46400  1.000 43.01202  ? 379 ARG B NH2  1 
ATOM   5260 N N    . VAL B 1 380 ? 102.73800 126.36200 67.50600  1.000 39.49896  ? 380 VAL B N    1 
ATOM   5261 C CA   . VAL B 1 380 ? 102.13400 125.33500 68.35100  1.000 37.45134  ? 380 VAL B CA   1 
ATOM   5262 C C    . VAL B 1 380 ? 102.55100 125.52600 69.80400  1.000 38.06952  ? 380 VAL B C    1 
ATOM   5263 O O    . VAL B 1 380 ? 101.73100 125.38300 70.72500  1.000 39.33116  ? 380 VAL B O    1 
ATOM   5264 C CB   . VAL B 1 380 ? 102.50200 123.93100 67.83600  1.000 36.93372  ? 380 VAL B CB   1 
ATOM   5265 C CG1  . VAL B 1 380 ? 101.67700 122.87400 68.54400  1.000 39.07773  ? 380 VAL B CG1  1 
ATOM   5266 C CG2  . VAL B 1 380 ? 102.28500 123.84500 66.33700  1.000 35.53712  ? 380 VAL B CG2  1 
ATOM   5267 N N    . GLY B 1 381 ? 103.80900 125.90900 70.03400  1.000 33.95227  ? 381 GLY B N    1 
ATOM   5268 C CA   . GLY B 1 381 ? 104.24600 126.15300 71.39900  1.000 31.08728  ? 381 GLY B CA   1 
ATOM   5269 C C    . GLY B 1 381 ? 103.53200 127.33100 72.03500  1.000 37.69564  ? 381 GLY B C    1 
ATOM   5270 O O    . GLY B 1 381 ? 103.08900 127.25500 73.18900  1.000 37.85396  ? 381 GLY B O    1 
ATOM   5271 N N    . VAL B 1 382 ? 103.37900 128.42300 71.28100  1.000 40.96892  ? 382 VAL B N    1 
ATOM   5272 C CA   . VAL B 1 382 ? 102.69300 129.59800 71.81200  1.000 34.25821  ? 382 VAL B CA   1 
ATOM   5273 C C    . VAL B 1 382 ? 101.25200 129.25700 72.16700  1.000 32.65254  ? 382 VAL B C    1 
ATOM   5274 O O    . VAL B 1 382 ? 100.75500 129.62300 73.24300  1.000 39.14501  ? 382 VAL B O    1 
ATOM   5275 C CB   . VAL B 1 382 ? 102.77000 130.75700 70.80000  1.000 33.06451  ? 382 VAL B CB   1 
ATOM   5276 C CG1  . VAL B 1 382 ? 101.85000 131.89300 71.21400  1.000 35.18635  ? 382 VAL B CG1  1 
ATOM   5277 C CG2  . VAL B 1 382 ? 104.20000 131.24800 70.66000  1.000 31.98763  ? 382 VAL B CG2  1 
ATOM   5278 N N    . GLU B 1 383 ? 100.56200 128.53300 71.28000  1.000 29.52570  ? 383 GLU B N    1 
ATOM   5279 C CA   . GLU B 1 383 ? 99.15600  128.23300 71.52600  1.000 30.07994  ? 383 GLU B CA   1 
ATOM   5280 C C    . GLU B 1 383 ? 98.98300  127.30600 72.72600  1.000 32.97299  ? 383 GLU B C    1 
ATOM   5281 O O    . GLU B 1 383 ? 98.06800  127.49800 73.54100  1.000 35.16453  ? 383 GLU B O    1 
ATOM   5282 C CB   . GLU B 1 383 ? 98.52700  127.61900 70.27600  1.000 30.57888  ? 383 GLU B CB   1 
ATOM   5283 C CG   . GLU B 1 383 ? 98.38300  128.58800 69.11600  1.000 31.77045  ? 383 GLU B CG   1 
ATOM   5284 C CD   . GLU B 1 383 ? 97.68800  129.87400 69.51100  1.000 41.73317  ? 383 GLU B CD   1 
ATOM   5285 O OE1  . GLU B 1 383 ? 96.44300  129.87800 69.59200  1.000 44.84198  ? 383 GLU B OE1  1 
ATOM   5286 O OE2  . GLU B 1 383 ? 98.38600  130.88300 69.74000  1.000 42.86967  ? 383 GLU B OE2  1 
ATOM   5287 N N    . GLY B 1 384 ? 99.87000  126.31900 72.87900  1.000 27.88716  ? 384 GLY B N    1 
ATOM   5288 C CA   . GLY B 1 384 ? 99.74800  125.42500 74.01800  1.000 23.42710  ? 384 GLY B CA   1 
ATOM   5289 C C    . GLY B 1 384 ? 100.04400 126.11700 75.33400  1.000 29.80868  ? 384 GLY B C    1 
ATOM   5290 O O    . GLY B 1 384 ? 99.37300  125.86800 76.34600  1.000 28.73150  ? 384 GLY B O    1 
ATOM   5291 N N    . ALA B 1 385 ? 101.01600 127.03400 75.33400  1.000 29.23724  ? 385 ALA B N    1 
ATOM   5292 C CA   . ALA B 1 385 ? 101.29700 127.77400 76.55900  1.000 28.98119  ? 385 ALA B CA   1 
ATOM   5293 C C    . ALA B 1 385 ? 100.12900 128.68100 76.92700  1.000 31.57384  ? 385 ALA B C    1 
ATOM   5294 O O    . ALA B 1 385 ? 99.76200  128.78600 78.10700  1.000 28.93701  ? 385 ALA B O    1 
ATOM   5295 C CB   . ALA B 1 385 ? 102.58500 128.58000 76.40500  1.000 27.84974  ? 385 ALA B CB   1 
ATOM   5296 N N    . LYS B 1 386 ? 99.50300  129.30900 75.92700  1.000 31.85982  ? 386 LYS B N    1 
ATOM   5297 C CA   . LYS B 1 386 ? 98.33300  130.13400 76.20900  1.000 31.24207  ? 386 LYS B CA   1 
ATOM   5298 C C    . LYS B 1 386 ? 97.20300  129.30500 76.80700  1.000 28.12599  ? 386 LYS B C    1 
ATOM   5299 O O    . LYS B 1 386 ? 96.55900  129.72700 77.77600  1.000 24.16445  ? 386 LYS B O    1 
ATOM   5300 C CB   . LYS B 1 386 ? 97.85400  130.83100 74.93700  1.000 30.46578  ? 386 LYS B CB   1 
ATOM   5301 C CG   . LYS B 1 386 ? 98.29700  132.26900 74.80200  1.000 33.61674  ? 386 LYS B CG   1 
ATOM   5302 C CD   . LYS B 1 386 ? 97.64800  132.91100 73.59100  1.000 35.21380  ? 386 LYS B CD   1 
ATOM   5303 C CE   . LYS B 1 386 ? 96.19200  133.25000 73.86800  1.000 35.04387  ? 386 LYS B CE   1 
ATOM   5304 N NZ   . LYS B 1 386 ? 95.91100  134.70200 73.70800  1.000 36.30383  ? 386 LYS B NZ   1 
ATOM   5305 N N    . LEU B 1 387 ? 96.95300  128.11700 76.25200  1.000 32.67754  ? 387 LEU B N    1 
ATOM   5306 C CA   . LEU B 1 387 ? 95.86000  127.30000 76.77300  1.000 30.12096  ? 387 LEU B CA   1 
ATOM   5307 C C    . LEU B 1 387 ? 96.12700  126.86400 78.21100  1.000 31.55735  ? 387 LEU B C    1 
ATOM   5308 O O    . LEU B 1 387 ? 95.23000  126.92400 79.06500  1.000 26.42514  ? 387 LEU B O    1 
ATOM   5309 C CB   . LEU B 1 387 ? 95.63400  126.08300 75.87700  1.000 29.84250  ? 387 LEU B CB   1 
ATOM   5310 C CG   . LEU B 1 387 ? 94.54000  125.12300 76.35000  1.000 31.30482  ? 387 LEU B CG   1 
ATOM   5311 C CD1  . LEU B 1 387 ? 93.47500  124.95900 75.28300  1.000 26.41965  ? 387 LEU B CD1  1 
ATOM   5312 C CD2  . LEU B 1 387 ? 95.12500  123.77500 76.74000  1.000 25.41256  ? 387 LEU B CD2  1 
ATOM   5313 N N    . LEU B 1 388 ? 97.36000  126.44300 78.50700  1.000 29.37035  ? 388 LEU B N    1 
ATOM   5314 C CA   . LEU B 1 388 ? 97.64700  125.98600 79.86500  1.000 28.42594  ? 388 LEU B CA   1 
ATOM   5315 C C    . LEU B 1 388 ? 97.57600  127.13400 80.86700  1.000 32.54538  ? 388 LEU B C    1 
ATOM   5316 O O    . LEU B 1 388 ? 97.08300  126.95700 81.99100  1.000 27.77591  ? 388 LEU B O    1 
ATOM   5317 C CB   . LEU B 1 388 ? 99.01400  125.30400 79.91400  1.000 30.65627  ? 388 LEU B CB   1 
ATOM   5318 C CG   . LEU B 1 388 ? 99.13900  124.00400 79.11600  1.000 26.37376  ? 388 LEU B CG   1 
ATOM   5319 C CD1  . LEU B 1 388 ? 100.58800 123.57600 78.98800  1.000 19.43051  ? 388 LEU B CD1  1 
ATOM   5320 C CD2  . LEU B 1 388 ? 98.31200  122.90600 79.76100  1.000 22.61631  ? 388 LEU B CD2  1 
ATOM   5321 N N    . ARG B 1 389 ? 97.99800  128.33600 80.46300  1.000 36.95745  ? 389 ARG B N    1 
ATOM   5322 C CA   . ARG B 1 389 ? 97.91300  129.45900 81.39000  1.000 25.98655  ? 389 ARG B CA   1 
ATOM   5323 C C    . ARG B 1 389 ? 96.47300  129.90700 81.59700  1.000 29.75144  ? 389 ARG B C    1 
ATOM   5324 O O    . ARG B 1 389 ? 96.10600  130.31300 82.70700  1.000 32.51266  ? 389 ARG B O    1 
ATOM   5325 C CB   . ARG B 1 389 ? 98.77700  130.61600 80.89500  1.000 26.35993  ? 389 ARG B CB   1 
ATOM   5326 C CG   . ARG B 1 389 ? 100.21600 130.53500 81.37000  1.000 31.29608  ? 389 ARG B CG   1 
ATOM   5327 C CD   . ARG B 1 389 ? 101.13100 131.41900 80.54600  1.000 29.25755  ? 389 ARG B CD   1 
ATOM   5328 N NE   . ARG B 1 389 ? 102.53100 131.06500 80.74200  1.000 30.14735  ? 389 ARG B NE   1 
ATOM   5329 C CZ   . ARG B 1 389 ? 103.45200 131.09800 79.79000  1.000 34.87755  ? 389 ARG B CZ   1 
ATOM   5330 N NH1  . ARG B 1 389 ? 103.15800 131.47200 78.55600  1.000 34.27396  ? 389 ARG B NH1  1 
ATOM   5331 N NH2  . ARG B 1 389 ? 104.70000 130.74600 80.08300  1.000 29.15988  ? 389 ARG B NH2  1 
ATOM   5332 N N    . GLU B 1 390 ? 95.63000  129.80000 80.56700  1.000 37.69744  ? 390 GLU B N    1 
ATOM   5333 C CA   . GLU B 1 390 ? 94.22500  130.14900 80.74700  1.000 30.66193  ? 390 GLU B CA   1 
ATOM   5334 C C    . GLU B 1 390 ? 93.52800  129.15900 81.67100  1.000 26.29140  ? 390 GLU B C    1 
ATOM   5335 O O    . GLU B 1 390 ? 92.71100  129.55500 82.51500  1.000 26.90213  ? 390 GLU B O    1 
ATOM   5336 C CB   . GLU B 1 390 ? 93.52200  130.20700 79.39100  1.000 32.22058  ? 390 GLU B CB   1 
ATOM   5337 C CG   . GLU B 1 390 ? 92.60300  131.40100 79.21900  1.000 36.10786  ? 390 GLU B CG   1 
ATOM   5338 C CD   . GLU B 1 390 ? 91.16200  131.08400 79.56500  1.000 47.90765  ? 390 GLU B CD   1 
ATOM   5339 O OE1  . GLU B 1 390 ? 90.81500  129.88700 79.62900  1.000 48.21502  ? 390 GLU B OE1  1 
ATOM   5340 O OE2  . GLU B 1 390 ? 90.37700  132.03300 79.77300  1.000 45.92697  ? 390 GLU B OE2  1 
ATOM   5341 N N    . LEU B 1 391 ? 93.86500  127.87000 81.56000  1.000 31.51747  ? 391 LEU B N    1 
ATOM   5342 C CA   . LEU B 1 391 ? 93.26300  126.89400 82.46500  1.000 30.67016  ? 391 LEU B CA   1 
ATOM   5343 C C    . LEU B 1 391 ? 93.73900  127.09600 83.89900  1.000 25.40751  ? 391 LEU B C    1 
ATOM   5344 O O    . LEU B 1 391 ? 92.94900  126.97300 84.84400  1.000 26.92163  ? 391 LEU B O    1 
ATOM   5345 C CB   . LEU B 1 391 ? 93.56500  125.47200 81.99300  1.000 32.33317  ? 391 LEU B CB   1 
ATOM   5346 C CG   . LEU B 1 391 ? 92.60800  124.88800 80.95300  1.000 27.20766  ? 391 LEU B CG   1 
ATOM   5347 C CD1  . LEU B 1 391 ? 92.70500  123.37400 80.92600  1.000 25.94246  ? 391 LEU B CD1  1 
ATOM   5348 C CD2  . LEU B 1 391 ? 91.18100  125.32600 81.23600  1.000 23.47199  ? 391 LEU B CD2  1 
ATOM   5349 N N    . GLY B 1 392 ? 95.01100  127.45600 84.08500  1.000 32.57535  ? 392 GLY B N    1 
ATOM   5350 C CA   . GLY B 1 392 ? 95.48100  127.73700 85.43200  1.000 30.84169  ? 392 GLY B CA   1 
ATOM   5351 C C    . GLY B 1 392 ? 94.82400  128.96600 86.03300  1.000 31.25996  ? 392 GLY B C    1 
ATOM   5352 O O    . GLY B 1 392 ? 94.46000  128.97600 87.21500  1.000 25.00500  ? 392 GLY B O    1 
ATOM   5353 N N    . GLU B 1 393 ? 94.63100  130.00800 85.22100  1.000 35.03167  ? 393 GLU B N    1 
ATOM   5354 C CA   . GLU B 1 393 ? 93.98100  131.21600 85.71600  1.000 29.64153  ? 393 GLU B CA   1 
ATOM   5355 C C    . GLU B 1 393 ? 92.52300  130.95400 86.07500  1.000 31.64690  ? 393 GLU B C    1 
ATOM   5356 O O    . GLU B 1 393 ? 92.02300  131.48200 87.07400  1.000 27.05356  ? 393 GLU B O    1 
ATOM   5357 C CB   . GLU B 1 393 ? 94.09300  132.33100 84.67700  1.000 33.03435  ? 393 GLU B CB   1 
ATOM   5358 C CG   . GLU B 1 393 ? 93.44500  133.64300 85.08000  1.000 39.35867  ? 393 GLU B CG   1 
ATOM   5359 C CD   . GLU B 1 393 ? 92.08800  133.84800 84.43600  1.000 46.83797  ? 393 GLU B CD   1 
ATOM   5360 O OE1  . GLU B 1 393 ? 92.03900  134.05400 83.20500  1.000 44.80868  ? 393 GLU B OE1  1 
ATOM   5361 O OE2  . GLU B 1 393 ? 91.07000  133.81700 85.16000  1.000 45.16024  ? 393 GLU B OE2  1 
ATOM   5362 N N    . LYS B 1 394 ? 91.82200  130.14200 85.27800  1.000 44.92969  ? 394 LYS B N    1 
ATOM   5363 C CA   . LYS B 1 394 ? 90.43700  129.82900 85.61400  1.000 34.01831  ? 394 LYS B CA   1 
ATOM   5364 C C    . LYS B 1 394 ? 90.31700  128.86900 86.79000  1.000 33.05614  ? 394 LYS B C    1 
ATOM   5365 O O    . LYS B 1 394 ? 89.27800  128.85800 87.45600  1.000 30.44280  ? 394 LYS B O    1 
ATOM   5366 C CB   . LYS B 1 394 ? 89.70200  129.25900 84.40200  1.000 32.04162  ? 394 LYS B CB   1 
ATOM   5367 C CG   . LYS B 1 394 ? 88.68000  130.21300 83.81600  1.000 30.47406  ? 394 LYS B CG   1 
ATOM   5368 C CD   . LYS B 1 394 ? 88.14200  129.71500 82.49100  1.000 37.15794  ? 394 LYS B CD   1 
ATOM   5369 C CE   . LYS B 1 394 ? 87.67400  130.87100 81.62600  1.000 39.92338  ? 394 LYS B CE   1 
ATOM   5370 N NZ   . LYS B 1 394 ? 86.64700  131.69400 82.31900  1.000 38.39627  ? 394 LYS B NZ   1 
ATOM   5371 N N    . VAL B 1 395 ? 91.34500  128.06500 87.06700  1.000 36.40297  ? 395 VAL B N    1 
ATOM   5372 C CA   . VAL B 1 395 ? 91.28700  127.25600 88.28000  1.000 26.40618  ? 395 VAL B CA   1 
ATOM   5373 C C    . VAL B 1 395 ? 91.59300  128.10100 89.51300  1.000 32.15581  ? 395 VAL B C    1 
ATOM   5374 O O    . VAL B 1 395 ? 91.06000  127.83600 90.59600  1.000 23.35967  ? 395 VAL B O    1 
ATOM   5375 C CB   . VAL B 1 395 ? 92.24000  126.05200 88.18800  1.000 31.12110  ? 395 VAL B CB   1 
ATOM   5376 C CG1  . VAL B 1 395 ? 92.28800  125.31800 89.51800  1.000 28.18454  ? 395 VAL B CG1  1 
ATOM   5377 C CG2  . VAL B 1 395 ? 91.80600  125.11200 87.08400  1.000 31.02005  ? 395 VAL B CG2  1 
ATOM   5378 N N    . LYS B 1 396 ? 92.43300  129.13000 89.37600  1.000 40.52008  ? 396 LYS B N    1 
ATOM   5379 C CA   . LYS B 1 396 ? 92.79700  129.93500 90.54000  1.000 29.50417  ? 396 LYS B CA   1 
ATOM   5380 C C    . LYS B 1 396 ? 91.62800  130.77600 91.04500  1.000 38.10323  ? 396 LYS B C    1 
ATOM   5381 O O    . LYS B 1 396 ? 91.47800  130.96800 92.25700  1.000 36.82888  ? 396 LYS B O    1 
ATOM   5382 C CB   . LYS B 1 396 ? 93.98600  130.83400 90.20700  1.000 29.07542  ? 396 LYS B CB   1 
ATOM   5383 C CG   . LYS B 1 396 ? 94.11100  132.03800 91.12400  1.000 34.78672  ? 396 LYS B CG   1 
ATOM   5384 C CD   . LYS B 1 396 ? 95.39200  132.81200 90.87100  1.000 34.80642  ? 396 LYS B CD   1 
ATOM   5385 C CE   . LYS B 1 396 ? 96.41200  132.56800 91.97000  1.000 37.28170  ? 396 LYS B CE   1 
ATOM   5386 N NZ   . LYS B 1 396 ? 97.80900  132.62000 91.46000  1.000 38.79033  ? 396 LYS B NZ   1 
ATOM   5387 N N    . LYS B 1 397 ? 90.79400  131.29000 90.14300  1.000 44.44767  ? 397 LYS B N    1 
ATOM   5388 C CA   . LYS B 1 397 ? 89.67300  132.13900 90.53000  1.000 37.00707  ? 397 LYS B CA   1 
ATOM   5389 C C    . LYS B 1 397 ? 88.36800  131.38200 90.73100  1.000 43.69268  ? 397 LYS B C    1 
ATOM   5390 O O    . LYS B 1 397 ? 87.35200  132.01100 91.04400  1.000 47.19708  ? 397 LYS B O    1 
ATOM   5391 C CB   . LYS B 1 397 ? 89.45700  133.24000 89.48900  1.000 38.97275  ? 397 LYS B CB   1 
ATOM   5392 C CG   . LYS B 1 397 ? 90.64900  134.15500 89.29000  1.000 43.57969  ? 397 LYS B CG   1 
ATOM   5393 C CD   . LYS B 1 397 ? 90.28000  135.40200 88.49400  1.000 46.70292  ? 397 LYS B CD   1 
ATOM   5394 C CE   . LYS B 1 397 ? 89.11000  135.17900 87.53900  1.000 45.67998  ? 397 LYS B CE   1 
ATOM   5395 N NZ   . LYS B 1 397 ? 89.22400  133.92700 86.73400  1.000 45.92751  ? 397 LYS B NZ   1 
ATOM   5396 N N    . MET B 1 398 ? 88.36300  130.06100 90.56700  1.000 43.34941  ? 398 MET B N    1 
ATOM   5397 C CA   . MET B 1 398 ? 87.15800  129.25600 90.75000  1.000 37.92191  ? 398 MET B CA   1 
ATOM   5398 C C    . MET B 1 398 ? 86.01900  129.76500 89.86200  1.000 42.84781  ? 398 MET B C    1 
ATOM   5399 O O    . MET B 1 398 ? 84.97400  130.21400 90.33600  1.000 42.15835  ? 398 MET B O    1 
ATOM   5400 C CB   . MET B 1 398 ? 86.74700  129.24200 92.22400  1.000 34.52451  ? 398 MET B CB   1 
ATOM   5401 C CG   . MET B 1 398 ? 87.62200  128.36700 93.10100  1.000 44.11599  ? 398 MET B CG   1 
ATOM   5402 S SD   . MET B 1 398 ? 87.47700  128.76700 94.85100  1.000 50.54904  ? 398 MET B SD   1 
ATOM   5403 C CE   . MET B 1 398 ? 86.59700  127.33300 95.45500  1.000 43.33058  ? 398 MET B CE   1 
ATOM   5404 N N    . GLU B 1 399 ? 86.24000  129.68300 88.55200  1.000 47.55457  ? 399 GLU B N    1 
ATOM   5405 C CA   . GLU B 1 399 ? 85.27800  130.14800 87.56400  1.000 44.83503  ? 399 GLU B CA   1 
ATOM   5406 C C    . GLU B 1 399 ? 85.03600  129.07100 86.51400  1.000 49.38586  ? 399 GLU B C    1 
ATOM   5407 O O    . GLU B 1 399 ? 85.88200  128.20700 86.27100  1.000 50.91728  ? 399 GLU B O    1 
ATOM   5408 C CB   . GLU B 1 399 ? 85.75500  131.43700 86.88600  1.000 46.12196  ? 399 GLU B CB   1 
ATOM   5409 C CG   . GLU B 1 399 ? 84.64900  132.43400 86.60400  1.000 50.76722  ? 399 GLU B CG   1 
ATOM   5410 C CD   . GLU B 1 399 ? 85.17000  133.84800 86.46200  1.000 56.51718  ? 399 GLU B CD   1 
ATOM   5411 O OE1  . GLU B 1 399 ? 85.84300  134.13400 85.45000  1.000 54.47091  ? 399 GLU B OE1  1 
ATOM   5412 O OE2  . GLU B 1 399 ? 84.90900  134.67300 87.36200  1.000 56.75464  ? 399 GLU B OE2  1 
ATOM   5413 N N    . LYS B 1 400 ? 83.86400  129.13800 85.88900  1.000 42.64121  ? 400 LYS B N    1 
ATOM   5414 C CA   . LYS B 1 400 ? 83.48200  128.17700 84.86800  1.000 41.52760  ? 400 LYS B CA   1 
ATOM   5415 C C    . LYS B 1 400 ? 84.02400  128.58200 83.49900  1.000 43.02522  ? 400 LYS B C    1 
ATOM   5416 O O    . LYS B 1 400 ? 84.44700  129.71800 83.27500  1.000 43.21311  ? 400 LYS B O    1 
ATOM   5417 C CB   . LYS B 1 400 ? 81.96200  128.03600 84.80100  1.000 44.60770  ? 400 LYS B CB   1 
ATOM   5418 C CG   . LYS B 1 400 ? 81.35400  127.28200 85.96700  1.000 45.71004  ? 400 LYS B CG   1 
ATOM   5419 C CD   . LYS B 1 400 ? 79.88800  126.97600 85.71900  1.000 41.88634  ? 400 LYS B CD   1 
ATOM   5420 C CE   . LYS B 1 400 ? 79.47100  125.69000 86.40900  1.000 41.60553  ? 400 LYS B CE   1 
ATOM   5421 N NZ   . LYS B 1 400 ? 78.75900  125.94900 87.68900  1.000 43.76507  ? 400 LYS B NZ   1 
ATOM   5422 N N    . LEU B 1 401 ? 84.00100  127.62400 82.57600  1.000 48.36025  ? 401 LEU B N    1 
ATOM   5423 C CA   . LEU B 1 401 ? 84.42000  127.87000 81.20400  1.000 49.07716  ? 401 LEU B CA   1 
ATOM   5424 C C    . LEU B 1 401 ? 83.35500  128.65300 80.44800  1.000 48.16578  ? 401 LEU B C    1 
ATOM   5425 O O    . LEU B 1 401 ? 82.15400  128.46400 80.66100  1.000 51.16065  ? 401 LEU B O    1 
ATOM   5426 C CB   . LEU B 1 401 ? 84.69900  126.55000 80.48400  1.000 46.36806  ? 401 LEU B CB   1 
ATOM   5427 C CG   . LEU B 1 401 ? 86.03300  125.86600 80.78000  1.000 47.27444  ? 401 LEU B CG   1 
ATOM   5428 C CD1  . LEU B 1 401 ? 86.26000  124.71100 79.82100  1.000 44.77408  ? 401 LEU B CD1  1 
ATOM   5429 C CD2  . LEU B 1 401 ? 87.17400  126.86300 80.70300  1.000 47.81455  ? 401 LEU B CD2  1 
ATOM   5430 N N    . GLY B 1 402 ? 83.80100  129.53400 79.55800  1.000 52.75935  ? 402 GLY B N    1 
ATOM   5431 C CA   . GLY B 1 402 ? 82.89800  130.34200 78.77600  1.000 57.84404  ? 402 GLY B CA   1 
ATOM   5432 C C    . GLY B 1 402 ? 82.24400  129.56100 77.65400  1.000 61.14591  ? 402 GLY B C    1 
ATOM   5433 O O    . GLY B 1 402 ? 82.33500  128.33100 77.58100  1.000 58.76679  ? 402 GLY B O    1 
ATOM   5434 N N    . PRO B 1 403 ? 81.56100  130.26800 76.75500  1.000 71.02548  ? 403 PRO B N    1 
ATOM   5435 C CA   . PRO B 1 403 ? 80.88600  129.59400 75.63700  1.000 71.97392  ? 403 PRO B CA   1 
ATOM   5436 C C    . PRO B 1 403 ? 81.82900  129.18000 74.51600  1.000 72.79659  ? 403 PRO B C    1 
ATOM   5437 O O    . PRO B 1 403 ? 81.61500  128.15000 73.86800  1.000 70.21624  ? 403 PRO B O    1 
ATOM   5438 C CB   . PRO B 1 403 ? 79.88100  130.64900 75.15900  1.000 68.69002  ? 403 PRO B CB   1 
ATOM   5439 C CG   . PRO B 1 403 ? 80.53200  131.94600 75.49600  1.000 67.82198  ? 403 PRO B CG   1 
ATOM   5440 C CD   . PRO B 1 403 ? 81.28800  131.71500 76.77800  1.000 69.19638  ? 403 PRO B CD   1 
ATOM   5441 N N    . VAL B 1 404 ? 82.87300  129.97600 74.27600  1.000 67.17250  ? 404 VAL B N    1 
ATOM   5442 C CA   . VAL B 1 404 ? 83.76500  129.72800 73.14900  1.000 67.54056  ? 404 VAL B CA   1 
ATOM   5443 C C    . VAL B 1 404 ? 84.62200  128.49100 73.39800  1.000 65.78159  ? 404 VAL B C    1 
ATOM   5444 O O    . VAL B 1 404 ? 84.88300  128.09800 74.54300  1.000 62.04717  ? 404 VAL B O    1 
ATOM   5445 C CB   . VAL B 1 404 ? 84.64400  130.96200 72.88300  1.000 67.18646  ? 404 VAL B CB   1 
ATOM   5446 C CG1  . VAL B 1 404 ? 85.79900  131.01100 73.87100  1.000 66.74226  ? 404 VAL B CG1  1 
ATOM   5447 C CG2  . VAL B 1 404 ? 85.15900  130.94700 71.45400  1.000 63.87709  ? 404 VAL B CG2  1 
ATOM   5448 N N    . ASP B 1 405 ? 85.06700  127.87400 72.30300  1.000 56.82910  ? 405 ASP B N    1 
ATOM   5449 C CA   . ASP B 1 405 ? 85.94300  126.70900 72.36000  1.000 57.25673  ? 405 ASP B CA   1 
ATOM   5450 C C    . ASP B 1 405 ? 87.39400  127.15100 72.51500  1.000 55.61856  ? 405 ASP B C    1 
ATOM   5451 O O    . ASP B 1 405 ? 87.86100  128.03900 71.79600  1.000 54.27690  ? 405 ASP B O    1 
ATOM   5452 C CB   . ASP B 1 405 ? 85.77500  125.85900 71.10100  1.000 57.55160  ? 405 ASP B CB   1 
ATOM   5453 C CG   . ASP B 1 405 ? 86.38900  124.48100 71.24100  1.000 57.36631  ? 405 ASP B CG   1 
ATOM   5454 O OD1  . ASP B 1 405 ? 86.42000  123.95500 72.37300  1.000 60.99185  ? 405 ASP B OD1  1 
ATOM   5455 O OD2  . ASP B 1 405 ? 86.83800  123.92300 70.21900  1.000 53.68945  ? 405 ASP B OD2  1 
ATOM   5456 N N    . LEU B 1 406 ? 88.10500  126.53100 73.45700  1.000 43.92148  ? 406 LEU B N    1 
ATOM   5457 C CA   . LEU B 1 406 ? 89.47200  126.92500 73.77100  1.000 47.47968  ? 406 LEU B CA   1 
ATOM   5458 C C    . LEU B 1 406 ? 90.53300  126.22100 72.93200  1.000 52.01776  ? 406 LEU B C    1 
ATOM   5459 O O    . LEU B 1 406 ? 91.67100  126.70200 72.87700  1.000 50.76163  ? 406 LEU B O    1 
ATOM   5460 C CB   . LEU B 1 406 ? 89.76700  126.65900 75.25100  1.000 48.28995  ? 406 LEU B CB   1 
ATOM   5461 C CG   . LEU B 1 406 ? 88.94400  127.41900 76.29100  1.000 51.70986  ? 406 LEU B CG   1 
ATOM   5462 C CD1  . LEU B 1 406 ? 89.23100  126.88000 77.68100  1.000 48.16311  ? 406 LEU B CD1  1 
ATOM   5463 C CD2  . LEU B 1 406 ? 89.22500  128.91000 76.22400  1.000 50.50896  ? 406 LEU B CD2  1 
ATOM   5464 N N    . LEU B 1 407 ? 90.20300  125.10600 72.28100  1.000 47.32712  ? 407 LEU B N    1 
ATOM   5465 C CA   . LEU B 1 407 ? 91.18400  124.31500 71.54700  1.000 41.81177  ? 407 LEU B CA   1 
ATOM   5466 C C    . LEU B 1 407 ? 91.16700  124.56800 70.04200  1.000 41.87254  ? 407 LEU B C    1 
ATOM   5467 O O    . LEU B 1 407 ? 91.84800  123.85600 69.29900  1.000 43.72904  ? 407 LEU B O    1 
ATOM   5468 C CB   . LEU B 1 407 ? 90.95900  122.82800 71.82600  1.000 39.36733  ? 407 LEU B CB   1 
ATOM   5469 C CG   . LEU B 1 407 ? 91.20200  122.34500 73.26000  1.000 41.50897  ? 407 LEU B CG   1 
ATOM   5470 C CD1  . LEU B 1 407 ? 90.51500  121.01100 73.50400  1.000 37.55771  ? 407 LEU B CD1  1 
ATOM   5471 C CD2  . LEU B 1 407 ? 92.68400  122.24700 73.56700  1.000 38.26662  ? 407 LEU B CD2  1 
ATOM   5472 N N    . PHE B 1 408 ? 90.40900  125.56200 69.57800  1.000 38.93983  ? 408 PHE B N    1 
ATOM   5473 C CA   . PHE B 1 408 ? 90.30800  125.83800 68.14600  1.000 39.95886  ? 408 PHE B CA   1 
ATOM   5474 C C    . PHE B 1 408 ? 91.65000  126.24400 67.53700  1.000 42.80165  ? 408 PHE B C    1 
ATOM   5475 O O    . PHE B 1 408 ? 92.08100  125.68900 66.51400  1.000 42.86392  ? 408 PHE B O    1 
ATOM   5476 C CB   . PHE B 1 408 ? 89.25800  126.92900 67.92000  1.000 43.70960  ? 408 PHE B CB   1 
ATOM   5477 C CG   . PHE B 1 408 ? 89.06000  127.30100 66.47900  1.000 46.25451  ? 408 PHE B CG   1 
ATOM   5478 C CD1  . PHE B 1 408 ? 88.34700  126.47500 65.62900  1.000 43.13166  ? 408 PHE B CD1  1 
ATOM   5479 C CD2  . PHE B 1 408 ? 89.57500  128.48200 65.97900  1.000 43.44637  ? 408 PHE B CD2  1 
ATOM   5480 C CE1  . PHE B 1 408 ? 88.15900  126.81700 64.30500  1.000 42.69692  ? 408 PHE B CE1  1 
ATOM   5481 C CE2  . PHE B 1 408 ? 89.39100  128.82800 64.65500  1.000 43.08650  ? 408 PHE B CE2  1 
ATOM   5482 C CZ   . PHE B 1 408 ? 88.68200  127.99400 63.81900  1.000 40.93607  ? 408 PHE B CZ   1 
ATOM   5483 N N    . GLU B 1 409 ? 92.34400  127.19300 68.17100  1.000 44.93581  ? 409 GLU B N    1 
ATOM   5484 C CA   . GLU B 1 409 ? 93.59200  127.70400 67.60800  1.000 42.34391  ? 409 GLU B CA   1 
ATOM   5485 C C    . GLU B 1 409 ? 94.72000  126.68000 67.66400  1.000 42.25081  ? 409 GLU B C    1 
ATOM   5486 O O    . GLU B 1 409 ? 95.50900  126.57400 66.71700  1.000 46.81620  ? 409 GLU B O    1 
ATOM   5487 C CB   . GLU B 1 409 ? 93.99900  128.98400 68.33500  1.000 44.29673  ? 409 GLU B CB   1 
ATOM   5488 C CG   . GLU B 1 409 ? 93.08300  130.16600 68.07200  1.000 48.48409  ? 409 GLU B CG   1 
ATOM   5489 C CD   . GLU B 1 409 ? 93.13800  130.64200 66.63400  1.000 52.28925  ? 409 GLU B CD   1 
ATOM   5490 O OE1  . GLU B 1 409 ? 94.21800  131.08800 66.19500  1.000 52.35603  ? 409 GLU B OE1  1 
ATOM   5491 O OE2  . GLU B 1 409 ? 92.09900  130.57200 65.94300  1.000 48.00676  ? 409 GLU B OE2  1 
ATOM   5492 N N    . VAL B 1 410 ? 94.81700  125.90800 68.74700  1.000 32.79957  ? 410 VAL B N    1 
ATOM   5493 C CA   . VAL B 1 410 ? 95.87700  124.90700 68.81200  1.000 38.75028  ? 410 VAL B CA   1 
ATOM   5494 C C    . VAL B 1 410 ? 95.63600  123.81500 67.77800  1.000 37.56250  ? 410 VAL B C    1 
ATOM   5495 O O    . VAL B 1 410 ? 96.57700  123.31500 67.14700  1.000 36.39649  ? 410 VAL B O    1 
ATOM   5496 C CB   . VAL B 1 410 ? 95.99700  124.34100 70.24000  1.000 33.02952  ? 410 VAL B CB   1 
ATOM   5497 C CG1  . VAL B 1 410 ? 94.72400  123.62100 70.65000  1.000 37.08078  ? 410 VAL B CG1  1 
ATOM   5498 C CG2  . VAL B 1 410 ? 97.19900  123.41600 70.34000  1.000 30.94407  ? 410 VAL B CG2  1 
ATOM   5499 N N    . HIS B 1 411 ? 94.37000  123.45800 67.55600  1.000 35.66453  ? 411 HIS B N    1 
ATOM   5500 C CA   . HIS B 1 411 ? 94.05800  122.45900 66.54200  1.000 30.33545  ? 411 HIS B CA   1 
ATOM   5501 C C    . HIS B 1 411 ? 94.41700  122.97100 65.15300  1.000 37.40465  ? 411 HIS B C    1 
ATOM   5502 O O    . HIS B 1 411 ? 94.99200  122.23500 64.33800  1.000 41.82244  ? 411 HIS B O    1 
ATOM   5503 C CB   . HIS B 1 411 ? 92.57800  122.09100 66.61900  1.000 30.63142  ? 411 HIS B CB   1 
ATOM   5504 C CG   . HIS B 1 411 ? 92.23800  121.18900 67.76500  1.000 40.55694  ? 411 HIS B CG   1 
ATOM   5505 N ND1  . HIS B 1 411 ? 90.94900  120.78800 68.04000  1.000 38.11655  ? 411 HIS B ND1  1 
ATOM   5506 C CD2  . HIS B 1 411 ? 93.01900  120.61900 68.71200  1.000 35.87029  ? 411 HIS B CD2  1 
ATOM   5507 C CE1  . HIS B 1 411 ? 90.95100  120.00700 69.10400  1.000 34.34190  ? 411 HIS B CE1  1 
ATOM   5508 N NE2  . HIS B 1 411 ? 92.19400  119.88800 69.53100  1.000 32.61924  ? 411 HIS B NE2  1 
ATOM   5509 N N    . LEU B 1 412 ? 94.12200  124.24300 64.87600  1.000 40.07375  ? 412 LEU B N    1 
ATOM   5510 C CA   . LEU B 1 412 ? 94.45400  124.78500 63.56200  1.000 42.91157  ? 412 LEU B CA   1 
ATOM   5511 C C    . LEU B 1 412 ? 95.96500  124.86700 63.36900  1.000 46.66576  ? 412 LEU B C    1 
ATOM   5512 O O    . LEU B 1 412 ? 96.47500  124.59900 62.27200  1.000 49.05045  ? 412 LEU B O    1 
ATOM   5513 C CB   . LEU B 1 412 ? 93.80300  126.15600 63.38600  1.000 46.69569  ? 412 LEU B CB   1 
ATOM   5514 C CG   . LEU B 1 412 ? 94.29800  127.02600 62.23000  1.000 52.66544  ? 412 LEU B CG   1 
ATOM   5515 C CD1  . LEU B 1 412 ? 93.48300  126.75800 60.97500  1.000 48.29199  ? 412 LEU B CD1  1 
ATOM   5516 C CD2  . LEU B 1 412 ? 94.23800  128.49700 62.60400  1.000 49.02180  ? 412 LEU B CD2  1 
ATOM   5517 N N    . ALA B 1 413 ? 96.70100  125.21100 64.43000  1.000 41.22483  ? 413 ALA B N    1 
ATOM   5518 C CA   . ALA B 1 413 ? 98.15700  125.25800 64.32900  1.000 37.67119  ? 413 ALA B CA   1 
ATOM   5519 C C    . ALA B 1 413 ? 98.73700  123.87400 64.06100  1.000 41.87129  ? 413 ALA B C    1 
ATOM   5520 O O    . ALA B 1 413 ? 99.65700  123.72200 63.24500  1.000 42.82172  ? 413 ALA B O    1 
ATOM   5521 C CB   . ALA B 1 413 ? 98.75200  125.85500 65.60300  1.000 34.15674  ? 413 ALA B CB   1 
ATOM   5522 N N    . ALA B 1 414 ? 98.18700  122.84100 64.70800  1.000 48.22223  ? 414 ALA B N    1 
ATOM   5523 C CA   . ALA B 1 414 ? 98.71400  121.50000 64.47700  1.000 42.28415  ? 414 ALA B CA   1 
ATOM   5524 C C    . ALA B 1 414 ? 98.33700  120.99200 63.09400  1.000 43.84778  ? 414 ALA B C    1 
ATOM   5525 O O    . ALA B 1 414 ? 99.08900  120.21700 62.48700  1.000 42.34788  ? 414 ALA B O    1 
ATOM   5526 C CB   . ALA B 1 414 ? 98.21100  120.54000 65.55400  1.000 35.21339  ? 414 ALA B CB   1 
ATOM   5527 N N    . GLU B 1 415 ? 97.22900  121.48600 62.53900  1.000 46.93902  ? 415 GLU B N    1 
ATOM   5528 C CA   . GLU B 1 415 ? 96.85900  121.07500 61.19000  1.000 49.46225  ? 415 GLU B CA   1 
ATOM   5529 C C    . GLU B 1 415 ? 97.75800  121.74500 60.15800  1.000 50.17517  ? 415 GLU B C    1 
ATOM   5530 O O    . GLU B 1 415 ? 98.15200  121.12100 59.16300  1.000 51.57986  ? 415 GLU B O    1 
ATOM   5531 C CB   . GLU B 1 415 ? 95.39000  121.40400 60.93000  1.000 52.70735  ? 415 GLU B CB   1 
ATOM   5532 C CG   . GLU B 1 415 ? 94.65300  120.36900 60.10100  1.000 54.64117  ? 415 GLU B CG   1 
ATOM   5533 C CD   . GLU B 1 415 ? 93.51000  120.96800 59.30800  1.000 58.09305  ? 415 GLU B CD   1 
ATOM   5534 O OE1  . GLU B 1 415 ? 92.70400  120.19600 58.74800  1.000 59.60694  ? 415 GLU B OE1  1 
ATOM   5535 O OE2  . GLU B 1 415 ? 93.41500  122.21200 59.24700  1.000 57.32668  ? 415 GLU B OE2  1 
ATOM   5536 N N    . GLU B 1 416 ? 98.12700  123.00600 60.39800  1.000 47.79970  ? 416 GLU B N    1 
ATOM   5537 C CA   . GLU B 1 416 ? 99.09000  123.65800 59.51600  1.000 49.09049  ? 416 GLU B CA   1 
ATOM   5538 C C    . GLU B 1 416 ? 100.45600 122.98700 59.60500  1.000 50.27143  ? 416 GLU B C    1 
ATOM   5539 O O    . GLU B 1 416 ? 101.15500 122.84900 58.59200  1.000 49.21138  ? 416 GLU B O    1 
ATOM   5540 C CB   . GLU B 1 416 ? 99.19700  125.14400 59.85400  1.000 49.78246  ? 416 GLU B CB   1 
ATOM   5541 C CG   . GLU B 1 416 ? 97.86700  125.80700 60.16300  1.000 54.51657  ? 416 GLU B CG   1 
ATOM   5542 C CD   . GLU B 1 416 ? 97.24400  126.46800 58.95000  1.000 56.87660  ? 416 GLU B CD   1 
ATOM   5543 O OE1  . GLU B 1 416 ? 97.10700  125.79400 57.90800  1.000 52.98503  ? 416 GLU B OE1  1 
ATOM   5544 O OE2  . GLU B 1 416 ? 96.88700  127.66100 59.04100  1.000 55.95178  ? 416 GLU B OE2  1 
ATOM   5545 N N    . LEU B 1 417 ? 100.85000 122.55100 60.80500  1.000 49.04327  ? 417 LEU B N    1 
ATOM   5546 C CA   . LEU B 1 417 ? 102.10000 121.80900 60.94600  1.000 41.73791  ? 417 LEU B CA   1 
ATOM   5547 C C    . LEU B 1 417 ? 102.06600 120.51900 60.13600  1.000 42.05141  ? 417 LEU B C    1 
ATOM   5548 O O    . LEU B 1 417 ? 103.02800 120.18300 59.43500  1.000 38.72338  ? 417 LEU B O    1 
ATOM   5549 C CB   . LEU B 1 417 ? 102.37400 121.50800 62.42000  1.000 43.34599  ? 417 LEU B CB   1 
ATOM   5550 C CG   . LEU B 1 417 ? 103.71400 120.83500 62.73000  1.000 44.52904  ? 417 LEU B CG   1 
ATOM   5551 C CD1  . LEU B 1 417 ? 104.88700 121.68900 62.27600  1.000 44.32925  ? 417 LEU B CD1  1 
ATOM   5552 C CD2  . LEU B 1 417 ? 103.82600 120.50900 64.21000  1.000 40.41109  ? 417 LEU B CD2  1 
ATOM   5553 N N    . GLN B 1 418 ? 100.96500 119.77000 60.23700  1.000 50.19139  ? 418 GLN B N    1 
ATOM   5554 C CA   . GLN B 1 418 ? 100.84300 118.53900 59.46400  1.000 47.43371  ? 418 GLN B CA   1 
ATOM   5555 C C    . GLN B 1 418 ? 100.92000 118.81200 57.96500  1.000 49.13728  ? 418 GLN B C    1 
ATOM   5556 O O    . GLN B 1 418 ? 101.59300 118.08200 57.22600  1.000 49.68438  ? 418 GLN B O    1 
ATOM   5557 C CB   . GLN B 1 418 ? 99.53400  117.83200 59.81200  1.000 48.11407  ? 418 GLN B CB   1 
ATOM   5558 C CG   . GLN B 1 418 ? 99.71700  116.53000 60.56500  1.000 51.43186  ? 418 GLN B CG   1 
ATOM   5559 C CD   . GLN B 1 418 ? 100.25000 115.42600 59.67900  1.000 53.99288  ? 418 GLN B CD   1 
ATOM   5560 O OE1  . GLN B 1 418 ? 99.63200  115.07200 58.67700  1.000 50.68965  ? 418 GLN B OE1  1 
ATOM   5561 N NE2  . GLN B 1 418 ? 101.40200 114.87600 60.04400  1.000 53.84087  ? 418 GLN B NE2  1 
ATOM   5562 N N    . HIS B 1 419 ? 100.24700 119.86700 57.49700  1.000 52.39904  ? 419 HIS B N    1 
ATOM   5563 C CA   . HIS B 1 419 ? 100.29800 120.19100 56.07400  1.000 49.80691  ? 419 HIS B CA   1 
ATOM   5564 C C    . HIS B 1 419 ? 101.71900 120.52400 55.63000  1.000 50.33844  ? 419 HIS B C    1 
ATOM   5565 O O    . HIS B 1 419 ? 102.18200 120.05100 54.58300  1.000 49.14587  ? 419 HIS B O    1 
ATOM   5566 C CB   . HIS B 1 419 ? 99.35700  121.35400 55.76400  1.000 53.71227  ? 419 HIS B CB   1 
ATOM   5567 C CG   . HIS B 1 419 ? 97.93800  120.93900 55.53000  1.000 57.87494  ? 419 HIS B CG   1 
ATOM   5568 N ND1  . HIS B 1 419 ? 96.87400  121.53000 56.17500  1.000 55.69032  ? 419 HIS B ND1  1 
ATOM   5569 C CD2  . HIS B 1 419 ? 97.40800  119.99400 54.71800  1.000 56.80930  ? 419 HIS B CD2  1 
ATOM   5570 C CE1  . HIS B 1 419 ? 95.74900  120.96600 55.77300  1.000 55.93708  ? 419 HIS B CE1  1 
ATOM   5571 N NE2  . HIS B 1 419 ? 96.04500  120.03000 54.88900  1.000 60.37835  ? 419 HIS B NE2  1 
ATOM   5572 N N    . LYS B 1 420 ? 102.43300 121.32900 56.42100  1.000 55.32415  ? 420 LYS B N    1 
ATOM   5573 C CA   . LYS B 1 420 ? 103.80100 121.67800 56.05600  1.000 52.40605  ? 420 LYS B CA   1 
ATOM   5574 C C    . LYS B 1 420 ? 104.69600 120.44600 56.02400  1.000 52.29255  ? 420 LYS B C    1 
ATOM   5575 O O    . LYS B 1 420 ? 105.50800 120.28400 55.10600  1.000 50.59083  ? 420 LYS B O    1 
ATOM   5576 C CB   . LYS B 1 420 ? 104.36000 122.72400 57.01900  1.000 51.26417  ? 420 LYS B CB   1 
ATOM   5577 C CG   . LYS B 1 420 ? 105.77200 123.16700 56.67700  1.000 53.46008  ? 420 LYS B CG   1 
ATOM   5578 C CD   . LYS B 1 420 ? 105.79100 124.03500 55.43100  1.000 53.39116  ? 420 LYS B CD   1 
ATOM   5579 C CE   . LYS B 1 420 ? 107.18200 124.58100 55.15900  1.000 54.13294  ? 420 LYS B CE   1 
ATOM   5580 N NZ   . LYS B 1 420 ? 107.16100 126.03600 54.85200  1.000 51.95875  ? 420 LYS B NZ   1 
ATOM   5581 N N    . ILE B 1 421 ? 104.56400 119.56300 57.01800  1.000 52.49793  ? 421 ILE B N    1 
ATOM   5582 C CA   . ILE B 1 421 ? 105.36300 118.34000 57.02000  1.000 52.18438  ? 421 ILE B CA   1 
ATOM   5583 C C    . ILE B 1 421 ? 105.05200 117.50100 55.78900  1.000 49.78503  ? 421 ILE B C    1 
ATOM   5584 O O    . ILE B 1 421 ? 105.94600 116.88100 55.20000  1.000 46.80747  ? 421 ILE B O    1 
ATOM   5585 C CB   . ILE B 1 421 ? 105.13300 117.54500 58.31900  1.000 53.09582  ? 421 ILE B CB   1 
ATOM   5586 C CG1  . ILE B 1 421 ? 106.22300 117.86700 59.34100  1.000 49.55628  ? 421 ILE B CG1  1 
ATOM   5587 C CG2  . ILE B 1 421 ? 105.11300 116.05500 58.03300  1.000 47.12191  ? 421 ILE B CG2  1 
ATOM   5588 C CD1  . ILE B 1 421 ? 106.29600 119.32600 59.71500  1.000 52.42442  ? 421 ILE B CD1  1 
ATOM   5589 N N    . ASP B 1 422 ? 103.78200 117.46500 55.37900  1.000 60.17680  ? 422 ASP B N    1 
ATOM   5590 C CA   . ASP B 1 422 ? 103.42200 116.71600 54.18000  1.000 56.80369  ? 422 ASP B CA   1 
ATOM   5591 C C    . ASP B 1 422 ? 104.01300 117.33800 52.92200  1.000 55.05392  ? 422 ASP B C    1 
ATOM   5592 O O    . ASP B 1 422 ? 104.29600 116.62100 51.95600  1.000 52.72909  ? 422 ASP B O    1 
ATOM   5593 C CB   . ASP B 1 422 ? 101.90200 116.62100 54.05000  1.000 54.55608  ? 422 ASP B CB   1 
ATOM   5594 C CG   . ASP B 1 422 ? 101.31500 115.49900 54.88000  1.000 60.57172  ? 422 ASP B CG   1 
ATOM   5595 O OD1  . ASP B 1 422 ? 101.99500 115.02900 55.81600  1.000 59.90102  ? 422 ASP B OD1  1 
ATOM   5596 O OD2  . ASP B 1 422 ? 100.17200 115.08600 54.59400  1.000 59.24101  ? 422 ASP B OD2  1 
ATOM   5597 N N    . LYS B 1 423 ? 104.20500 118.65800 52.90600  1.000 60.77733  ? 423 LYS B N    1 
ATOM   5598 C CA   . LYS B 1 423 ? 104.70800 119.30700 51.69900  1.000 61.07153  ? 423 LYS B CA   1 
ATOM   5599 C C    . LYS B 1 423 ? 106.21600 119.17100 51.50900  1.000 60.69381  ? 423 LYS B C    1 
ATOM   5600 O O    . LYS B 1 423 ? 106.69000 119.27900 50.37300  1.000 61.53446  ? 423 LYS B O    1 
ATOM   5601 C CB   . LYS B 1 423 ? 104.33500 120.79100 51.70300  1.000 61.00636  ? 423 LYS B CB   1 
ATOM   5602 C CG   . LYS B 1 423 ? 103.27800 121.16900 50.68000  1.000 62.02232  ? 423 LYS B CG   1 
ATOM   5603 C CD   . LYS B 1 423 ? 102.19500 120.10700 50.57900  1.000 64.01770  ? 423 LYS B CD   1 
ATOM   5604 C CE   . LYS B 1 423 ? 101.20800 120.21200 51.73100  1.000 63.56168  ? 423 LYS B CE   1 
ATOM   5605 N NZ   . LYS B 1 423 ? 100.08300 119.24700 51.59200  1.000 63.20040  ? 423 LYS B NZ   1 
ATOM   5606 N N    . LYS B 1 424 ? 106.98000 118.93700 52.57400  1.000 64.30321  ? 424 LYS B N    1 
ATOM   5607 C CA   . LYS B 1 424 ? 108.43800 118.88400 52.50200  1.000 63.43013  ? 424 LYS B CA   1 
ATOM   5608 C C    . LYS B 1 424 ? 108.98400 117.57100 53.05100  1.000 63.26219  ? 424 LYS B C    1 
ATOM   5609 O O    . LYS B 1 424 ? 110.05000 117.53100 53.66800  1.000 64.27885  ? 424 LYS B O    1 
ATOM   5610 C CB   . LYS B 1 424 ? 109.06100 120.06600 53.24100  1.000 62.62165  ? 424 LYS B CB   1 
ATOM   5611 C CG   . LYS B 1 424 ? 108.67600 121.42400 52.68500  1.000 62.79047  ? 424 LYS B CG   1 
ATOM   5612 C CD   . LYS B 1 424 ? 109.80000 122.00000 51.84100  1.000 64.58788  ? 424 LYS B CD   1 
ATOM   5613 C CE   . LYS B 1 424 ? 109.26100 122.86600 50.71700  1.000 64.94931  ? 424 LYS B CE   1 
ATOM   5614 N NZ   . LYS B 1 424 ? 110.05600 124.11300 50.55200  1.000 64.46509  ? 424 LYS B NZ   1 
ATOM   5615 N N    . SER B 1 425 ? 108.26200 116.47300 52.82700  1.000 66.64944  ? 425 SER B N    1 
ATOM   5616 C CA   . SER B 1 425 ? 108.64600 115.19000 53.40200  1.000 65.40383  ? 425 SER B CA   1 
ATOM   5617 C C    . SER B 1 425 ? 109.89100 114.58300 52.76400  1.000 66.47837  ? 425 SER B C    1 
ATOM   5618 O O    . SER B 1 425 ? 110.40800 113.59300 53.29100  1.000 64.61737  ? 425 SER B O    1 
ATOM   5619 C CB   . SER B 1 425 ? 107.48500 114.20300 53.29100  1.000 62.08563  ? 425 SER B CB   1 
ATOM   5620 O OG   . SER B 1 425 ? 107.80000 112.98600 53.94000  1.000 64.62535  ? 425 SER B OG   1 
ATOM   5621 N N    . TYR B 1 426 ? 110.38700 115.13800 51.65600  1.000 67.28845  ? 426 TYR B N    1 
ATOM   5622 C CA   . TYR B 1 426 ? 111.55000 114.55500 50.99600  1.000 65.97605  ? 426 TYR B CA   1 
ATOM   5623 C C    . TYR B 1 426 ? 112.84900 114.78600 51.76000  1.000 66.20798  ? 426 TYR B C    1 
ATOM   5624 O O    . TYR B 1 426 ? 113.87500 114.21000 51.38500  1.000 65.77301  ? 426 TYR B O    1 
ATOM   5625 C CB   . TYR B 1 426 ? 111.67300 115.09300 49.56500  1.000 63.07471  ? 426 TYR B CB   1 
ATOM   5626 C CG   . TYR B 1 426 ? 111.90700 116.58400 49.45700  1.000 65.40951  ? 426 TYR B CG   1 
ATOM   5627 C CD1  . TYR B 1 426 ? 113.14000 117.14200 49.77100  1.000 65.12114  ? 426 TYR B CD1  1 
ATOM   5628 C CD2  . TYR B 1 426 ? 110.89400 117.43500 49.03800  1.000 65.29587  ? 426 TYR B CD2  1 
ATOM   5629 C CE1  . TYR B 1 426 ? 113.35500 118.50100 49.67200  1.000 66.43208  ? 426 TYR B CE1  1 
ATOM   5630 C CE2  . TYR B 1 426 ? 111.10000 118.79500 48.93700  1.000 65.70453  ? 426 TYR B CE2  1 
ATOM   5631 C CZ   . TYR B 1 426 ? 112.33200 119.32300 49.25600  1.000 67.76658  ? 426 TYR B CZ   1 
ATOM   5632 O OH   . TYR B 1 426 ? 112.54300 120.67800 49.15600  1.000 66.16163  ? 426 TYR B OH   1 
ATOM   5633 N N    . LEU B 1 427 ? 112.83300 115.60300 52.81000  1.000 62.57132  ? 427 LEU B N    1 
ATOM   5634 C CA   . LEU B 1 427 ? 114.01700 115.86900 53.61300  1.000 62.64603  ? 427 LEU B CA   1 
ATOM   5635 C C    . LEU B 1 427 ? 114.12200 114.95700 54.82900  1.000 62.91530  ? 427 LEU B C    1 
ATOM   5636 O O    . LEU B 1 427 ? 115.01600 115.15100 55.65900  1.000 59.03864  ? 427 LEU B O    1 
ATOM   5637 C CB   . LEU B 1 427 ? 114.03200 117.33200 54.06400  1.000 63.36351  ? 427 LEU B CB   1 
ATOM   5638 C CG   . LEU B 1 427 ? 114.10400 118.39800 52.97100  1.000 61.79230  ? 427 LEU B CG   1 
ATOM   5639 C CD1  . LEU B 1 427 ? 113.77400 119.76700 53.53900  1.000 59.65345  ? 427 LEU B CD1  1 
ATOM   5640 C CD2  . LEU B 1 427 ? 115.47800 118.40400 52.32100  1.000 63.34223  ? 427 LEU B CD2  1 
ATOM   5641 N N    . LEU B 1 428 ? 113.23700 113.97000 54.95100  1.000 62.37937  ? 428 LEU B N    1 
ATOM   5642 C CA   . LEU B 1 428 ? 113.23800 113.05500 56.08500  1.000 59.90034  ? 428 LEU B CA   1 
ATOM   5643 C C    . LEU B 1 428 ? 113.61900 111.63000 55.72100  1.000 64.83183  ? 428 LEU B C    1 
ATOM   5644 O O    . LEU B 1 428 ? 114.22100 110.93900 56.54400  1.000 63.66951  ? 428 LEU B O    1 
ATOM   5645 C CB   . LEU B 1 428 ? 111.86000 113.04200 56.76000  1.000 60.76056  ? 428 LEU B CB   1 
ATOM   5646 C CG   . LEU B 1 428 ? 111.29100 114.40600 57.15700  1.000 64.99233  ? 428 LEU B CG   1 
ATOM   5647 C CD1  . LEU B 1 428 ? 109.84400 114.27200 57.59600  1.000 63.06682  ? 428 LEU B CD1  1 
ATOM   5648 C CD2  . LEU B 1 428 ? 112.13000 115.04700 58.25100  1.000 63.62624  ? 428 LEU B CD2  1 
ATOM   5649 N N    . VAL B 1 429 ? 113.27300 111.19700 54.51900  1.000 75.32277  ? 429 VAL B N    1 
ATOM   5650 C CA   . VAL B 1 429 ? 113.55100 109.83800 54.10100  1.000 74.23715  ? 429 VAL B CA   1 
ATOM   5651 C C    . VAL B 1 429 ? 114.49800 109.82100 52.92300  1.000 74.69047  ? 429 VAL B C    1 
ATOM   5652 O O    . VAL B 1 429 ? 114.65300 110.82700 52.23900  1.000 73.18122  ? 429 VAL B O    1 
ATOM   5653 C CB   . VAL B 1 429 ? 112.25800 109.11900 53.70500  1.000 72.44324  ? 429 VAL B CB   1 
ATOM   5654 C CG1  . VAL B 1 429 ? 111.35000 108.95300 54.91200  1.000 71.06269  ? 429 VAL B CG1  1 
ATOM   5655 C CG2  . VAL B 1 429 ? 111.54900 109.87900 52.59400  1.000 73.51338  ? 429 VAL B CG2  1 
ATOM   5656 N N    . ASN B 1 430 ? 115.14500 108.68400 52.68600  1.000 86.91368  ? 430 ASN B N    1 
ATOM   5657 C CA   . ASN B 1 430 ? 116.05600 108.54900 51.55300  1.000 88.04776  ? 430 ASN B CA   1 
ATOM   5658 C C    . ASN B 1 430 ? 115.30700 107.98900 50.36200  1.000 89.76966  ? 430 ASN B C    1 
ATOM   5659 O O    . ASN B 1 430 ? 114.94600 106.81600 50.35600  1.000 89.48023  ? 430 ASN B O    1 
ATOM   5660 C CB   . ASN B 1 430 ? 117.21700 107.63300 51.91500  1.000 86.89060  ? 430 ASN B CB   1 
ATOM   5661 C CG   . ASN B 1 430 ? 118.00900 108.13900 53.10300  1.000 88.90589  ? 430 ASN B CG   1 
ATOM   5662 O OD1  . ASN B 1 430 ? 117.44600 108.67000 54.05900  1.000 88.65088  ? 430 ASN B OD1  1 
ATOM   5663 N ND2  . ASN B 1 430 ? 119.32500 107.97500 53.04800  1.000 87.59778  ? 430 ASN B ND2  1 
ATOM   5664 N N    . SER B 1 431 ? 115.07000 108.81100 49.34900  1.000 98.32703  ? 431 SER B N    1 
ATOM   5665 C CA   . SER B 1 431 ? 114.27400 108.36400 48.21100  1.000 97.57082  ? 431 SER B CA   1 
ATOM   5666 C C    . SER B 1 431 ? 115.08800 107.61300 47.17200  1.000 98.63284  ? 431 SER B C    1 
ATOM   5667 O O    . SER B 1 431 ? 114.52600 106.91200 46.33200  1.000 99.44344  ? 431 SER B O    1 
ATOM   5668 C CB   . SER B 1 431 ? 113.58800 109.56200 47.55500  1.000 96.63267  ? 431 SER B CB   1 
ATOM   5669 O OG   . SER B 1 431 ? 113.00300 109.19600 46.31800  1.000 97.52203  ? 431 SER B OG   1 
ATOM   5670 N N    . GLU B 1 432 ? 116.40500 107.74600 47.22600  1.000 101.05789 ? 432 GLU B N    1 
ATOM   5671 C CA   . GLU B 1 432 ? 117.25800 107.09500 46.24000  1.000 101.39149 ? 432 GLU B CA   1 
ATOM   5672 C C    . GLU B 1 432 ? 117.05800 105.58700 46.22100  1.000 102.66838 ? 432 GLU B C    1 
ATOM   5673 O O    . GLU B 1 432 ? 116.97900 104.98600 45.15400  1.000 103.16254 ? 432 GLU B O    1 
ATOM   5674 C CB   . GLU B 1 432 ? 118.72600 107.41700 46.51900  1.000 101.93627 ? 432 GLU B CB   1 
ATOM   5675 C CG   . GLU B 1 432 ? 119.08700 108.87900 46.30600  1.000 102.37211 ? 432 GLU B CG   1 
ATOM   5676 C CD   . GLU B 1 432 ? 120.53000 109.18100 46.66000  1.000 103.59950 ? 432 GLU B CD   1 
ATOM   5677 O OE1  . GLU B 1 432 ? 121.19800 108.30400 47.24800  1.000 102.68035 ? 432 GLU B OE1  1 
ATOM   5678 O OE2  . GLU B 1 432 ? 120.99900 110.29600 46.35000  1.000 103.08086 ? 432 GLU B OE2  1 
ATOM   5679 N N    . CYS B 1 433 ? 116.98000 104.97100 47.39300  1.000 103.23008 ? 433 CYS B N    1 
ATOM   5680 C CA   . CYS B 1 433 ? 116.81100 103.52700 47.47800  1.000 102.76594 ? 433 CYS B CA   1 
ATOM   5681 C C    . CYS B 1 433 ? 115.38600 103.19200 47.81400  1.000 102.37902 ? 433 CYS B C    1 
ATOM   5682 O O    . CYS B 1 433 ? 114.90500 103.56900 48.88000  1.000 103.60614 ? 433 CYS B O    1 
ATOM   5683 C CB   . CYS B 1 433 ? 117.71300 102.96500 48.56800  1.000 102.22861 ? 433 CYS B CB   1 
ATOM   5684 S SG   . CYS B 1 433 ? 117.47400 103.73500 50.18500  1.000 103.24222 ? 433 CYS B SG   1 
ATOM   5685 N N    . TRP B 1 434 ? 114.69800 102.49100 46.92400  1.000 101.14934 ? 434 TRP B N    1 
ATOM   5686 C CA   . TRP B 1 434 ? 113.31500 102.12500 47.19700  1.000 103.42319 ? 434 TRP B CA   1 
ATOM   5687 C C    . TRP B 1 434 ? 112.86600 100.83100 46.53900  1.000 103.27791 ? 434 TRP B C    1 
ATOM   5688 O O    . TRP B 1 434 ? 112.80100 100.73800 45.31400  1.000 102.14573 ? 434 TRP B O    1 
ATOM   5689 C CB   . TRP B 1 434 ? 112.37200 103.26700 46.79900  1.000 101.76217 ? 434 TRP B CB   1 
ATOM   5690 C CG   . TRP B 1 434 ? 111.93600 104.07700 47.96800  1.000 101.91750 ? 434 TRP B CG   1 
ATOM   5691 C CD1  . TRP B 1 434 ? 111.99800 103.71100 49.27700  1.000 102.47417 ? 434 TRP B CD1  1 
ATOM   5692 C CD2  . TRP B 1 434 ? 111.37600 105.39300 47.94400  1.000 102.76317 ? 434 TRP B CD2  1 
ATOM   5693 N NE1  . TRP B 1 434 ? 111.51100 104.71400 50.07000  1.000 102.17960 ? 434 TRP B NE1  1 
ATOM   5694 C CE2  . TRP B 1 434 ? 111.12400 105.76000 49.27800  1.000 102.61003 ? 434 TRP B CE2  1 
ATOM   5695 C CE3  . TRP B 1 434 ? 111.06200 106.29500 46.92500  1.000 101.97298 ? 434 TRP B CE3  1 
ATOM   5696 C CZ2  . TRP B 1 434 ? 110.57200 106.99100 49.62200  1.000 101.45950 ? 434 TRP B CZ2  1 
ATOM   5697 C CZ3  . TRP B 1 434 ? 110.51300 107.51600 47.26800  1.000 101.28279 ? 434 TRP B CZ3  1 
ATOM   5698 C CH2  . TRP B 1 434 ? 110.27400 107.85200 48.60500  1.000 101.29451 ? 434 TRP B CH2  1 
ATOM   5699 N N    . GLU B 1 435 ? 112.54400 99.83400  47.35500  1.000 103.04174 ? 435 GLU B N    1 
ATOM   5700 C CA   . GLU B 1 435 ? 112.06600 98.57200  46.82200  1.000 101.98926 ? 435 GLU B CA   1 
ATOM   5701 C C    . GLU B 1 435 ? 110.66300 98.29300  47.32400  1.000 101.31186 ? 435 GLU B C    1 
ATOM   5702 O O    . GLU B 1 435 ? 110.45100 97.36700  48.10400  1.000 101.66506 ? 435 GLU B O    1 
ATOM   5703 C CB   . GLU B 1 435 ? 112.99600 97.43700  47.23100  1.000 103.36318 ? 435 GLU B CB   1 
ATOM   5704 C CG   . GLU B 1 435 ? 114.47100 97.79300  47.17600  1.000 102.58681 ? 435 GLU B CG   1 
ATOM   5705 C CD   . GLU B 1 435 ? 115.35600 96.66100  47.65400  1.000 102.62580 ? 435 GLU B CD   1 
ATOM   5706 O OE1  . GLU B 1 435 ? 114.82700 95.71000  48.26800  1.000 101.16007 ? 435 GLU B OE1  1 
ATOM   5707 O OE2  . GLU B 1 435 ? 116.58100 96.72100  47.41700  1.000 103.18327 ? 435 GLU B OE2  1 
ATOM   5708 N N    . LYS B 1 527 ? 124.87300 106.14600 54.88000  1.000 91.90162  ? 527 LYS B N    1 
ATOM   5709 C CA   . LYS B 1 527 ? 125.33400 106.02000 56.25700  1.000 93.50122  ? 527 LYS B CA   1 
ATOM   5710 C C    . LYS B 1 527 ? 124.15600 105.98000 57.22500  1.000 93.69573  ? 527 LYS B C    1 
ATOM   5711 O O    . LYS B 1 527 ? 123.18400 106.71700 57.06700  1.000 93.59203  ? 527 LYS B O    1 
ATOM   5712 C CB   . LYS B 1 527 ? 126.27500 107.17200 56.61400  1.000 94.04654  ? 527 LYS B CB   1 
ATOM   5713 C CG   . LYS B 1 527 ? 127.74200 106.88100 56.34200  1.000 92.60064  ? 527 LYS B CG   1 
ATOM   5714 C CD   . LYS B 1 527 ? 128.40300 106.20000 57.52900  1.000 91.88548  ? 527 LYS B CD   1 
ATOM   5715 C CE   . LYS B 1 527 ? 128.76900 107.20500 58.60800  1.000 92.06409  ? 527 LYS B CE   1 
ATOM   5716 N NZ   . LYS B 1 527 ? 128.79500 106.58200 59.96000  1.000 91.18218  ? 527 LYS B NZ   1 
ATOM   5717 N N    . THR B 1 528 ? 124.25200 105.10700 58.23000  1.000 85.93172  ? 528 THR B N    1 
ATOM   5718 C CA   . THR B 1 528 ? 123.18600 104.99500 59.22100  1.000 86.68383  ? 528 THR B CA   1 
ATOM   5719 C C    . THR B 1 528 ? 123.00100 106.29800 59.98900  1.000 86.74644  ? 528 THR B C    1 
ATOM   5720 O O    . THR B 1 528 ? 121.87100 106.67800 60.32500  1.000 86.36684  ? 528 THR B O    1 
ATOM   5721 C CB   . THR B 1 528 ? 123.48400 103.84500 60.18400  1.000 87.15054  ? 528 THR B CB   1 
ATOM   5722 O OG1  . THR B 1 528 ? 123.36200 102.59600 59.49200  1.000 85.88425  ? 528 THR B OG1  1 
ATOM   5723 C CG2  . THR B 1 528 ? 122.51300 103.86600 61.35600  1.000 84.11113  ? 528 THR B CG2  1 
ATOM   5724 N N    . TYR B 1 529 ? 124.10000 107.00100 60.27200  1.000 81.10804  ? 529 TYR B N    1 
ATOM   5725 C CA   . TYR B 1 529 ? 124.00000 108.23700 61.04200  1.000 81.46381  ? 529 TYR B CA   1 
ATOM   5726 C C    . TYR B 1 529 ? 123.21700 109.30100 60.28400  1.000 80.96181  ? 529 TYR B C    1 
ATOM   5727 O O    . TYR B 1 529 ? 122.43100 110.04200 60.88400  1.000 79.51876  ? 529 TYR B O    1 
ATOM   5728 C CB   . TYR B 1 529 ? 125.39300 108.75100 61.40300  1.000 79.16891  ? 529 TYR B CB   1 
ATOM   5729 C CG   . TYR B 1 529 ? 125.36900 109.93100 62.34800  1.000 81.42078  ? 529 TYR B CG   1 
ATOM   5730 C CD1  . TYR B 1 529 ? 124.85000 109.80500 63.63000  1.000 79.12024  ? 529 TYR B CD1  1 
ATOM   5731 C CD2  . TYR B 1 529 ? 125.85500 111.17100 61.95700  1.000 81.12822  ? 529 TYR B CD2  1 
ATOM   5732 C CE1  . TYR B 1 529 ? 124.82000 110.88000 64.49800  1.000 79.46990  ? 529 TYR B CE1  1 
ATOM   5733 C CE2  . TYR B 1 529 ? 125.82900 112.25200 62.81900  1.000 82.17037  ? 529 TYR B CE2  1 
ATOM   5734 C CZ   . TYR B 1 529 ? 125.31000 112.10000 64.08900  1.000 81.36642  ? 529 TYR B CZ   1 
ATOM   5735 O OH   . TYR B 1 529 ? 125.28100 113.17100 64.95200  1.000 75.62764  ? 529 TYR B OH   1 
ATOM   5736 N N    . GLU B 1 530 ? 123.40900 109.39000 58.96600  1.000 77.29633  ? 530 GLU B N    1 
ATOM   5737 C CA   . GLU B 1 530 ? 122.67400 110.38200 58.18700  1.000 80.05207  ? 530 GLU B CA   1 
ATOM   5738 C C    . GLU B 1 530 ? 121.17500 110.11000 58.23200  1.000 82.77263  ? 530 GLU B C    1 
ATOM   5739 O O    . GLU B 1 530 ? 120.36800 111.03600 58.39000  1.000 81.28799  ? 530 GLU B O    1 
ATOM   5740 C CB   . GLU B 1 530 ? 123.17700 110.38800 56.74500  1.000 78.95778  ? 530 GLU B CB   1 
ATOM   5741 C CG   . GLU B 1 530 ? 124.52800 111.06100 56.56100  1.000 81.54953  ? 530 GLU B CG   1 
ATOM   5742 C CD   . GLU B 1 530 ? 124.62200 111.83100 55.25800  1.000 83.26493  ? 530 GLU B CD   1 
ATOM   5743 O OE1  . GLU B 1 530 ? 123.91800 111.46200 54.29500  1.000 82.41342  ? 530 GLU B OE1  1 
ATOM   5744 O OE2  . GLU B 1 530 ? 125.40100 112.80600 55.19700  1.000 82.03023  ? 530 GLU B OE2  1 
ATOM   5745 N N    . SER B 1 531 ? 120.78500 108.83800 58.13600  1.000 69.88144  ? 531 SER B N    1 
ATOM   5746 C CA   . SER B 1 531 ? 119.36800 108.49600 58.16600  1.000 66.81436  ? 531 SER B CA   1 
ATOM   5747 C C    . SER B 1 531 ? 118.76800 108.74300 59.54500  1.000 65.96395  ? 531 SER B C    1 
ATOM   5748 O O    . SER B 1 531 ? 117.63900 109.23900 59.65700  1.000 68.77521  ? 531 SER B O    1 
ATOM   5749 C CB   . SER B 1 531 ? 119.17800 107.04100 57.74400  1.000 70.77363  ? 531 SER B CB   1 
ATOM   5750 O OG   . SER B 1 531 ? 119.74300 106.80900 56.46500  1.000 67.91324  ? 531 SER B OG   1 
ATOM   5751 N N    . ALA B 1 532 ? 119.50200 108.40700 60.60800  1.000 59.64001  ? 532 ALA B N    1 
ATOM   5752 C CA   . ALA B 1 532 ? 118.98900 108.67100 61.94900  1.000 62.89277  ? 532 ALA B CA   1 
ATOM   5753 C C    . ALA B 1 532 ? 118.85200 110.16900 62.19700  1.000 65.68662  ? 532 ALA B C    1 
ATOM   5754 O O    . ALA B 1 532 ? 117.87200 110.62500 62.80700  1.000 66.29721  ? 532 ALA B O    1 
ATOM   5755 C CB   . ALA B 1 532 ? 119.89800 108.02700 62.99400  1.000 62.32270  ? 532 ALA B CB   1 
ATOM   5756 N N    . SER B 1 533 ? 119.81900 110.95300 61.71200  1.000 59.19997  ? 533 SER B N    1 
ATOM   5757 C CA   . SER B 1 533 ? 119.73300 112.40200 61.83300  1.000 58.39322  ? 533 SER B CA   1 
ATOM   5758 C C    . SER B 1 533 ? 118.52400 112.93600 61.08200  1.000 56.32676  ? 533 SER B C    1 
ATOM   5759 O O    . SER B 1 533 ? 117.85300 113.86500 61.54700  1.000 58.34283  ? 533 SER B O    1 
ATOM   5760 C CB   . SER B 1 533 ? 121.01800 113.04400 61.31000  1.000 58.77796  ? 533 SER B CB   1 
ATOM   5761 O OG   . SER B 1 533 ? 122.12900 112.69000 62.11200  1.000 57.51783  ? 533 SER B OG   1 
ATOM   5762 N N    . ALA B 1 534 ? 118.23100 112.35900 59.91600  1.000 49.64705  ? 534 ALA B N    1 
ATOM   5763 C CA   . ALA B 1 534 ? 117.04900 112.77200 59.16900  1.000 52.51892  ? 534 ALA B CA   1 
ATOM   5764 C C    . ALA B 1 534 ? 115.76500 112.43400 59.92100  1.000 53.63583  ? 534 ALA B C    1 
ATOM   5765 O O    . ALA B 1 534 ? 114.82100 113.23200 59.93100  1.000 54.73390  ? 534 ALA B O    1 
ATOM   5766 C CB   . ALA B 1 534 ? 117.05000 112.12400 57.78600  1.000 56.11828  ? 534 ALA B CB   1 
ATOM   5767 N N    . LEU B 1 535 ? 115.70700 111.26100 60.55400  1.000 42.70758  ? 535 LEU B N    1 
ATOM   5768 C CA   . LEU B 1 535 ? 114.46700 110.82800 61.19400  1.000 45.41244  ? 535 LEU B CA   1 
ATOM   5769 C C    . LEU B 1 535 ? 114.25000 111.42700 62.58100  1.000 40.95959  ? 535 LEU B C    1 
ATOM   5770 O O    . LEU B 1 535 ? 113.12600 111.35700 63.10700  1.000 46.85425  ? 535 LEU B O    1 
ATOM   5771 C CB   . LEU B 1 535 ? 114.44800 109.30100 61.30300  1.000 48.28061  ? 535 LEU B CB   1 
ATOM   5772 C CG   . LEU B 1 535 ? 114.07400 108.49100 60.06300  1.000 43.47698  ? 535 LEU B CG   1 
ATOM   5773 C CD1  . LEU B 1 535 ? 113.97200 107.01900 60.42000  1.000 44.68058  ? 535 LEU B CD1  1 
ATOM   5774 C CD2  . LEU B 1 535 ? 112.77300 108.98900 59.45700  1.000 46.18084  ? 535 LEU B CD2  1 
ATOM   5775 N N    . SER B 1 536 ? 115.26900 112.05800 63.16900  1.000 38.19204  ? 536 SER B N    1 
ATOM   5776 C CA   . SER B 1 536 ? 115.05300 112.66700 64.47800  1.000 44.48831  ? 536 SER B CA   1 
ATOM   5777 C C    . SER B 1 536 ? 114.13100 113.88200 64.40800  1.000 46.23341  ? 536 SER B C    1 
ATOM   5778 O O    . SER B 1 536 ? 113.43800 114.18800 65.39100  1.000 43.64202  ? 536 SER B O    1 
ATOM   5779 C CB   . SER B 1 536 ? 116.39700 113.06500 65.08600  1.000 44.09718  ? 536 SER B CB   1 
ATOM   5780 O OG   . SER B 1 536 ? 117.08800 111.93200 65.57700  1.000 48.27012  ? 536 SER B OG   1 
ATOM   5781 N N    . LEU B 1 537 ? 113.98600 114.48400 63.22700  1.000 33.84223  ? 537 LEU B N    1 
ATOM   5782 C CA   . LEU B 1 537 ? 113.08500 115.62000 63.09400  1.000 36.66776  ? 537 LEU B CA   1 
ATOM   5783 C C    . LEU B 1 537 ? 111.64400 115.14600 62.99000  1.000 38.94457  ? 537 LEU B C    1 
ATOM   5784 O O    . LEU B 1 537 ? 110.73400 115.76700 63.55800  1.000 43.97077  ? 537 LEU B O    1 
ATOM   5785 C CB   . LEU B 1 537 ? 113.47400 116.45100 61.87100  1.000 38.47231  ? 537 LEU B CB   1 
ATOM   5786 C CG   . LEU B 1 537 ? 113.33500 117.97300 61.94200  1.000 43.87509  ? 537 LEU B CG   1 
ATOM   5787 C CD1  . LEU B 1 537 ? 114.03800 118.61300 60.75900  1.000 37.41892  ? 537 LEU B CD1  1 
ATOM   5788 C CD2  . LEU B 1 537 ? 111.87700 118.39200 61.98900  1.000 44.01106  ? 537 LEU B CD2  1 
ATOM   5789 N N    . ALA B 1 538 ? 111.42400 114.03000 62.29600  1.000 33.11252  ? 538 ALA B N    1 
ATOM   5790 C CA   . ALA B 1 538 ? 110.08600 113.46600 62.25500  1.000 37.70000  ? 538 ALA B CA   1 
ATOM   5791 C C    . ALA B 1 538 ? 109.68100 112.95900 63.62900  1.000 31.28696  ? 538 ALA B C    1 
ATOM   5792 O O    . ALA B 1 538 ? 108.50300 113.04000 63.99700  1.000 33.46477  ? 538 ALA B O    1 
ATOM   5793 C CB   . ALA B 1 538 ? 110.01700 112.34300 61.22200  1.000 35.84680  ? 538 ALA B CB   1 
ATOM   5794 N N    . THR B 1 539 ? 110.64900 112.49200 64.42300  1.000 22.46464  ? 539 THR B N    1 
ATOM   5795 C CA   . THR B 1 539 ? 110.34100 112.10900 65.79900  1.000 29.93162  ? 539 THR B CA   1 
ATOM   5796 C C    . THR B 1 539 ? 109.90300 113.31800 66.62300  1.000 33.43429  ? 539 THR B C    1 
ATOM   5797 O O    . THR B 1 539 ? 108.89700 113.26500 67.34700  1.000 34.80342  ? 539 THR B O    1 
ATOM   5798 C CB   . THR B 1 539 ? 111.55500 111.43500 66.43800  1.000 29.76761  ? 539 THR B CB   1 
ATOM   5799 O OG1  . THR B 1 539 ? 112.05600 110.42100 65.56000  1.000 33.31901  ? 539 THR B OG1  1 
ATOM   5800 C CG2  . THR B 1 539 ? 111.18100 110.80600 67.77200  1.000 27.35632  ? 539 THR B CG2  1 
ATOM   5801 N N    . PHE B 1 540 ? 110.63700 114.43100 66.50900  1.000 31.70256  ? 540 PHE B N    1 
ATOM   5802 C CA   . PHE B 1 540 ? 110.26500 115.63500 67.25200  1.000 31.50421  ? 540 PHE B CA   1 
ATOM   5803 C C    . PHE B 1 540 ? 108.87200 116.12700 66.85600  1.000 26.88622  ? 540 PHE B C    1 
ATOM   5804 O O    . PHE B 1 540 ? 108.05400 116.48800 67.72000  1.000 25.23994  ? 540 PHE B O    1 
ATOM   5805 C CB   . PHE B 1 540 ? 111.31900 116.72200 67.01800  1.000 28.61000  ? 540 PHE B CB   1 
ATOM   5806 C CG   . PHE B 1 540 ? 111.24800 117.87000 67.98700  1.000 24.90536  ? 540 PHE B CG   1 
ATOM   5807 C CD1  . PHE B 1 540 ? 111.96000 117.83800 69.17400  1.000 25.91288  ? 540 PHE B CD1  1 
ATOM   5808 C CD2  . PHE B 1 540 ? 110.48900 118.99300 67.70000  1.000 29.64115  ? 540 PHE B CD2  1 
ATOM   5809 C CE1  . PHE B 1 540 ? 111.90100 118.89300 70.06400  1.000 30.28534  ? 540 PHE B CE1  1 
ATOM   5810 C CE2  . PHE B 1 540 ? 110.42600 120.05200 68.58700  1.000 28.94609  ? 540 PHE B CE2  1 
ATOM   5811 C CZ   . PHE B 1 540 ? 111.13200 120.00200 69.77000  1.000 30.16283  ? 540 PHE B CZ   1 
ATOM   5812 N N    . ALA B 1 541 ? 108.57000 116.11700 65.55400  1.000 22.01230  ? 541 ALA B N    1 
ATOM   5813 C CA   . ALA B 1 541 ? 107.26000 116.57300 65.09600  1.000 19.75791  ? 541 ALA B CA   1 
ATOM   5814 C C    . ALA B 1 541 ? 106.14300 115.65200 65.57800  1.000 26.13825  ? 541 ALA B C    1 
ATOM   5815 O O    . ALA B 1 541 ? 105.08600 116.12600 66.02200  1.000 30.48517  ? 541 ALA B O    1 
ATOM   5816 C CB   . ALA B 1 541 ? 107.24700 116.68100 63.57200  1.000 25.08529  ? 541 ALA B CB   1 
ATOM   5817 N N    . SER B 1 542 ? 106.35100 114.33400 65.49400  1.000 21.67933  ? 542 SER B N    1 
ATOM   5818 C CA   . SER B 1 542 ? 105.33800 113.40000 65.97100  1.000 20.51014  ? 542 SER B CA   1 
ATOM   5819 C C    . SER B 1 542 ? 105.06400 113.60600 67.45400  1.000 21.42396  ? 542 SER B C    1 
ATOM   5820 O O    . SER B 1 542 ? 103.91100 113.52600 67.90200  1.000 17.15562  ? 542 SER B O    1 
ATOM   5821 C CB   . SER B 1 542 ? 105.78200 111.96300 65.70300  1.000 17.60234  ? 542 SER B CB   1 
ATOM   5822 O OG   . SER B 1 542 ? 105.38900 111.53800 64.41200  1.000 25.04846  ? 542 SER B OG   1 
ATOM   5823 N N    . LEU B 1 543 ? 106.10900 113.90100 68.23000  1.000 22.93835  ? 543 LEU B N    1 
ATOM   5824 C CA   . LEU B 1 543 ? 105.90800 114.07500 69.66400  1.000 23.34701  ? 543 LEU B CA   1 
ATOM   5825 C C    . LEU B 1 543 ? 105.13000 115.35200 69.95600  1.000 25.98868  ? 543 LEU B C    1 
ATOM   5826 O O    . LEU B 1 543 ? 104.25200 115.36700 70.83200  1.000 27.00125  ? 543 LEU B O    1 
ATOM   5827 C CB   . LEU B 1 543 ? 107.25600 114.08200 70.38200  1.000 30.77608  ? 543 LEU B CB   1 
ATOM   5828 C CG   . LEU B 1 543 ? 107.80300 112.71100 70.78400  1.000 28.76953  ? 543 LEU B CG   1 
ATOM   5829 C CD1  . LEU B 1 543 ? 109.24800 112.82000 71.24100  1.000 26.25113  ? 543 LEU B CD1  1 
ATOM   5830 C CD2  . LEU B 1 543 ? 106.94000 112.09000 71.86800  1.000 26.50387  ? 543 LEU B CD2  1 
ATOM   5831 N N    . LEU B 1 544 ? 105.41000 116.42700 69.21500  1.000 27.31484  ? 544 LEU B N    1 
ATOM   5832 C CA   . LEU B 1 544 ? 104.63300 117.65000 69.40900  1.000 25.53243  ? 544 LEU B CA   1 
ATOM   5833 C C    . LEU B 1 544 ? 103.16500 117.44500 69.03500  1.000 19.70602  ? 544 LEU B C    1 
ATOM   5834 O O    . LEU B 1 544 ? 102.26000 117.96400 69.70900  1.000 20.30158  ? 544 LEU B O    1 
ATOM   5835 C CB   . LEU B 1 544 ? 105.24300 118.79200 68.59800  1.000 25.17021  ? 544 LEU B CB   1 
ATOM   5836 C CG   . LEU B 1 544 ? 105.15200 120.18600 69.22100  1.000 23.07590  ? 544 LEU B CG   1 
ATOM   5837 C CD1  . LEU B 1 544 ? 105.51400 120.14100 70.69600  1.000 22.67932  ? 544 LEU B CD1  1 
ATOM   5838 C CD2  . LEU B 1 544 ? 106.04500 121.16300 68.47800  1.000 21.46425  ? 544 LEU B CD2  1 
ATOM   5839 N N    . ILE B 1 545 ? 102.90100 116.65900 67.98900  1.000 21.29226  ? 545 ILE B N    1 
ATOM   5840 C CA   . ILE B 1 545 ? 101.51200 116.42000 67.60300  1.000 21.62036  ? 545 ILE B CA   1 
ATOM   5841 C C    . ILE B 1 545 ? 100.79300 115.57100 68.65100  1.000 25.03944  ? 545 ILE B C    1 
ATOM   5842 O O    . ILE B 1 545 ? 99.61400  115.79900 68.95200  1.000 21.95037  ? 545 ILE B O    1 
ATOM   5843 C CB   . ILE B 1 545 ? 101.44100 115.78700 66.20200  1.000 23.23868  ? 545 ILE B CB   1 
ATOM   5844 C CG1  . ILE B 1 545 ? 101.52300 116.87400 65.12900  1.000 23.30395  ? 545 ILE B CG1  1 
ATOM   5845 C CG2  . ILE B 1 545 ? 100.15900 114.99100 66.03800  1.000 19.76045  ? 545 ILE B CG2  1 
ATOM   5846 C CD1  . ILE B 1 545 ? 102.21200 116.43800 63.85500  1.000 26.96483  ? 545 ILE B CD1  1 
ATOM   5847 N N    . GLU B 1 546 ? 101.49000 114.59900 69.24700  1.000 25.47075  ? 546 GLU B N    1 
ATOM   5848 C CA   . GLU B 1 546 ? 100.87100 113.81600 70.31600  1.000 24.02664  ? 546 GLU B CA   1 
ATOM   5849 C C    . GLU B 1 546 ? 100.57300 114.68300 71.53900  1.000 20.77392  ? 546 GLU B C    1 
ATOM   5850 O O    . GLU B 1 546 ? 99.52300  114.53000 72.19000  1.000 23.89450  ? 546 GLU B O    1 
ATOM   5851 C CB   . GLU B 1 546 ? 101.78000 112.64400 70.69000  1.000 26.31085  ? 546 GLU B CB   1 
ATOM   5852 C CG   . GLU B 1 546 ? 101.25900 111.76200 71.81400  1.000 25.43425  ? 546 GLU B CG   1 
ATOM   5853 C CD   . GLU B 1 546 ? 99.99700  111.01400 71.43300  1.000 31.61625  ? 546 GLU B CD   1 
ATOM   5854 O OE1  . GLU B 1 546 ? 99.83900  110.68200 70.24100  1.000 34.97945  ? 546 GLU B OE1  1 
ATOM   5855 O OE2  . GLU B 1 546 ? 99.16600  110.75500 72.32600  1.000 29.10304  ? 546 GLU B OE2  1 
ATOM   5856 N N    . PHE B 1 547 ? 101.47100 115.62100 71.85100  1.000 24.73258  ? 547 PHE B N    1 
ATOM   5857 C CA   . PHE B 1 547 ? 101.18900 116.54300 72.94400  1.000 25.28568  ? 547 PHE B CA   1 
ATOM   5858 C C    . PHE B 1 547 ? 99.93900  117.35900 72.65800  1.000 28.41449  ? 547 PHE B C    1 
ATOM   5859 O O    . PHE B 1 547 ? 99.09600  117.54700 73.54300  1.000 16.32246  ? 547 PHE B O    1 
ATOM   5860 C CB   . PHE B 1 547 ? 102.36800 117.48000 73.19100  1.000 20.08808  ? 547 PHE B CB   1 
ATOM   5861 C CG   . PHE B 1 547 ? 102.07300 118.54900 74.20400  1.000 24.65224  ? 547 PHE B CG   1 
ATOM   5862 C CD1  . PHE B 1 547 ? 102.16200 118.28300 75.55900  1.000 23.21161  ? 547 PHE B CD1  1 
ATOM   5863 C CD2  . PHE B 1 547 ? 101.66500 119.80900 73.80100  1.000 21.98259  ? 547 PHE B CD2  1 
ATOM   5864 C CE1  . PHE B 1 547 ? 101.87500 119.26000 76.48900  1.000 21.75708  ? 547 PHE B CE1  1 
ATOM   5865 C CE2  . PHE B 1 547 ? 101.37400 120.78700 74.72700  1.000 24.71345  ? 547 PHE B CE2  1 
ATOM   5866 C CZ   . PHE B 1 547 ? 101.48100 120.51200 76.07200  1.000 25.83054  ? 547 PHE B CZ   1 
ATOM   5867 N N    . VAL B 1 548 ? 99.79300  117.84500 71.42300  1.000 27.45019  ? 548 VAL B N    1 
ATOM   5868 C CA   . VAL B 1 548 ? 98.59300  118.60900 71.10800  1.000 20.69438  ? 548 VAL B CA   1 
ATOM   5869 C C    . VAL B 1 548 ? 97.35200  117.72800 71.12800  1.000 21.27051  ? 548 VAL B C    1 
ATOM   5870 O O    . VAL B 1 548 ? 96.24300  118.22700 71.34800  1.000 26.49129  ? 548 VAL B O    1 
ATOM   5871 C CB   . VAL B 1 548 ? 98.73000  119.31600 69.74700  1.000 25.14702  ? 548 VAL B CB   1 
ATOM   5872 C CG1  . VAL B 1 548 ? 97.40700  119.94200 69.34200  1.000 20.42011  ? 548 VAL B CG1  1 
ATOM   5873 C CG2  . VAL B 1 548 ? 99.82000  120.37400 69.80700  1.000 21.27628  ? 548 VAL B CG2  1 
ATOM   5874 N N    . ALA B 1 549 ? 97.50700  116.42300 70.90800  1.000 31.40142  ? 549 ALA B N    1 
ATOM   5875 C CA   . ALA B 1 549 ? 96.36200  115.52100 70.91200  1.000 20.64074  ? 549 ALA B CA   1 
ATOM   5876 C C    . ALA B 1 549 ? 95.94300  115.05800 72.30500  1.000 24.11058  ? 549 ALA B C    1 
ATOM   5877 O O    . ALA B 1 549 ? 94.85200  114.49500 72.44200  1.000 19.22523  ? 549 ALA B O    1 
ATOM   5878 C CB   . ALA B 1 549 ? 96.65700  114.29800 70.04200  1.000 19.15245  ? 549 ALA B CB   1 
ATOM   5879 N N    . ARG B 1 550 ? 96.76300  115.26700 73.33500  1.000 34.70805  ? 550 ARG B N    1 
ATOM   5880 C CA   . ARG B 1 550 ? 96.38400  114.81600 74.67900  1.000 20.08527  ? 550 ARG B CA   1 
ATOM   5881 C C    . ARG B 1 550 ? 95.68100  115.87100 75.55300  1.000 26.99604  ? 550 ARG B C    1 
ATOM   5882 O O    . ARG B 1 550 ? 95.47600  115.61400 76.74300  1.000 21.98299  ? 550 ARG B O    1 
ATOM   5883 C CB   . ARG B 1 550 ? 97.60500  114.28700 75.43800  1.000 23.97380  ? 550 ARG B CB   1 
ATOM   5884 C CG   . ARG B 1 550 ? 98.31800  113.12800 74.77800  1.000 26.21394  ? 550 ARG B CG   1 
ATOM   5885 C CD   . ARG B 1 550 ? 99.42800  112.60100 75.67400  1.000 24.95120  ? 550 ARG B CD   1 
ATOM   5886 N NE   . ARG B 1 550 ? 99.94000  111.31600 75.21300  1.000 32.60156  ? 550 ARG B NE   1 
ATOM   5887 C CZ   . ARG B 1 550 ? 100.85800 110.60100 75.85000  1.000 28.14932  ? 550 ARG B CZ   1 
ATOM   5888 N NH1  . ARG B 1 550 ? 101.39700 111.02000 76.98300  1.000 19.30631  ? 550 ARG B NH1  1 
ATOM   5889 N NH2  . ARG B 1 550 ? 101.24300 109.43700 75.33600  1.000 22.18047  ? 550 ARG B NH2  1 
ATOM   5890 N N    . LEU B 1 551 ? 95.30300  117.03500 75.01400  1.000 29.93673  ? 551 LEU B N    1 
ATOM   5891 C CA   . LEU B 1 551 ? 94.74500  118.11000 75.84100  1.000 20.18912  ? 551 LEU B CA   1 
ATOM   5892 C C    . LEU B 1 551 ? 93.24700  117.97100 76.13100  1.000 23.83600  ? 551 LEU B C    1 
ATOM   5893 O O    . LEU B 1 551 ? 92.75400  118.54600 77.12000  1.000 30.12911  ? 551 LEU B O    1 
ATOM   5894 C CB   . LEU B 1 551 ? 95.00300  119.45900 75.16600  1.000 20.41112  ? 551 LEU B CB   1 
ATOM   5895 C CG   . LEU B 1 551 ? 96.45500  119.93600 75.09200  1.000 29.47697  ? 551 LEU B CG   1 
ATOM   5896 C CD1  . LEU B 1 551 ? 96.55000  121.22500 74.29100  1.000 18.96832  ? 551 LEU B CD1  1 
ATOM   5897 C CD2  . LEU B 1 551 ? 97.04400  120.12000 76.48300  1.000 15.91697  ? 551 LEU B CD2  1 
ATOM   5898 N N    . GLN B 1 552 ? 92.51100  117.23900 75.29400  1.000 28.88546  ? 552 GLN B N    1 
ATOM   5899 C CA   . GLN B 1 552 ? 91.06800  117.12400 75.47800  1.000 25.10654  ? 552 GLN B CA   1 
ATOM   5900 C C    . GLN B 1 552 ? 90.71000  116.44800 76.79800  1.000 25.13656  ? 552 GLN B C    1 
ATOM   5901 O O    . GLN B 1 552 ? 89.69700  116.79300 77.41800  1.000 26.95383  ? 552 GLN B O    1 
ATOM   5902 C CB   . GLN B 1 552 ? 90.45800  116.36300 74.30200  1.000 24.60197  ? 552 GLN B CB   1 
ATOM   5903 C CG   . GLN B 1 552 ? 88.98300  116.05900 74.45000  1.000 30.10564  ? 552 GLN B CG   1 
ATOM   5904 C CD   . GLN B 1 552 ? 88.11400  117.12100 73.81400  1.000 34.63328  ? 552 GLN B CD   1 
ATOM   5905 O OE1  . GLN B 1 552 ? 88.26500  117.43600 72.63500  1.000 31.92209  ? 552 GLN B OE1  1 
ATOM   5906 N NE2  . GLN B 1 552 ? 87.20000  117.68300 74.59400  1.000 29.80935  ? 552 GLN B NE2  1 
ATOM   5907 N N    . ASN B 1 553 ? 91.52700  115.49500 77.24800  1.000 22.39462  ? 553 ASN B N    1 
ATOM   5908 C CA   . ASN B 1 553 ? 91.24900  114.82800 78.51600  1.000 26.48906  ? 553 ASN B CA   1 
ATOM   5909 C C    . ASN B 1 553 ? 91.39800  115.79100 79.68800  1.000 31.27181  ? 553 ASN B C    1 
ATOM   5910 O O    . ASN B 1 553 ? 90.60500  115.75100 80.64000  1.000 33.60887  ? 553 ASN B O    1 
ATOM   5911 C CB   . ASN B 1 553 ? 92.17500  113.62200 78.67500  1.000 32.54610  ? 553 ASN B CB   1 
ATOM   5912 C CG   . ASN B 1 553 ? 91.80900  112.75200 79.85800  1.000 36.45219  ? 553 ASN B CG   1 
ATOM   5913 O OD1  . ASN B 1 553 ? 92.66300  112.39800 80.67000  1.000 32.76180  ? 553 ASN B OD1  1 
ATOM   5914 N ND2  . ASN B 1 553 ? 90.53400  112.39800 79.96100  1.000 34.55749  ? 553 ASN B ND2  1 
ATOM   5915 N N    . VAL B 1 554 ? 92.38400  116.68700 79.62100  1.000 24.41419  ? 554 VAL B N    1 
ATOM   5916 C CA   . VAL B 1 554 ? 92.53900  117.69400 80.66500  1.000 26.48424  ? 554 VAL B CA   1 
ATOM   5917 C C    . VAL B 1 554 ? 91.34600  118.63900 80.66600  1.000 24.39086  ? 554 VAL B C    1 
ATOM   5918 O O    . VAL B 1 554 ? 90.83800  119.02300 81.72800  1.000 25.49001  ? 554 VAL B O    1 
ATOM   5919 C CB   . VAL B 1 554 ? 93.86400  118.45700 80.48300  1.000 28.15736  ? 554 VAL B CB   1 
ATOM   5920 C CG1  . VAL B 1 554 ? 94.25600  119.16200 81.77000  1.000 22.97094  ? 554 VAL B CG1  1 
ATOM   5921 C CG2  . VAL B 1 554 ? 94.96600  117.51500 80.03100  1.000 27.07822  ? 554 VAL B CG2  1 
ATOM   5922 N N    . VAL B 1 555 ? 90.85800  119.00600 79.47900  1.000 26.24370  ? 555 VAL B N    1 
ATOM   5923 C CA   . VAL B 1 555 ? 89.71100  119.91100 79.43300  1.000 24.47831  ? 555 VAL B CA   1 
ATOM   5924 C C    . VAL B 1 555 ? 88.46100  119.23300 79.99700  1.000 28.67251  ? 555 VAL B C    1 
ATOM   5925 O O    . VAL B 1 555 ? 87.65900  119.86100 80.70500  1.000 26.94345  ? 555 VAL B O    1 
ATOM   5926 C CB   . VAL B 1 555 ? 89.48800  120.41700 77.99700  1.000 30.69371  ? 555 VAL B CB   1 
ATOM   5927 C CG1  . VAL B 1 555 ? 88.10800  121.03600 77.86100  1.000 32.77985  ? 555 VAL B CG1  1 
ATOM   5928 C CG2  . VAL B 1 555 ? 90.56400  121.42300 77.62200  1.000 23.10649  ? 555 VAL B CG2  1 
ATOM   5929 N N    . ASP B 1 556 ? 88.29200  117.93600 79.72600  1.000 32.51524  ? 556 ASP B N    1 
ATOM   5930 C CA   . ASP B 1 556 ? 87.13800  117.21600 80.26200  1.000 22.41838  ? 556 ASP B CA   1 
ATOM   5931 C C    . ASP B 1 556 ? 87.21300  117.08800 81.78000  1.000 29.86178  ? 556 ASP B C    1 
ATOM   5932 O O    . ASP B 1 556 ? 86.20100  117.25900 82.47900  1.000 36.09511  ? 556 ASP B O    1 
ATOM   5933 C CB   . ASP B 1 556 ? 87.03900  115.83600 79.61500  1.000 31.21278  ? 556 ASP B CB   1 
ATOM   5934 C CG   . ASP B 1 556 ? 86.64400  115.90300 78.15500  1.000 42.19136  ? 556 ASP B CG   1 
ATOM   5935 O OD1  . ASP B 1 556 ? 86.32100  117.01000 77.67600  1.000 44.74290  ? 556 ASP B OD1  1 
ATOM   5936 O OD2  . ASP B 1 556 ? 86.65800  114.85000 77.48500  1.000 36.37252  ? 556 ASP B OD2  1 
ATOM   5937 N N    . ALA B 1 557 ? 88.40400  116.80100 82.31200  1.000 29.30641  ? 557 ALA B N    1 
ATOM   5938 C CA   . ALA B 1 557 ? 88.55100  116.73500 83.76100  1.000 24.83620  ? 557 ALA B CA   1 
ATOM   5939 C C    . ALA B 1 557 ? 88.26400  118.08800 84.39900  1.000 27.88834  ? 557 ALA B C    1 
ATOM   5940 O O    . ALA B 1 557 ? 87.64700  118.16100 85.47200  1.000 28.25918  ? 557 ALA B O    1 
ATOM   5941 C CB   . ALA B 1 557 ? 89.95400  116.25000 84.12800  1.000 23.63560  ? 557 ALA B CB   1 
ATOM   5942 N N    . PHE B 1 558 ? 88.68600  119.17600 83.74800  1.000 31.15386  ? 558 PHE B N    1 
ATOM   5943 C CA   . PHE B 1 558 ? 88.39300  120.49200 84.30200  1.000 26.03789  ? 558 PHE B CA   1 
ATOM   5944 C C    . PHE B 1 558 ? 86.89500  120.76200 84.31200  1.000 24.85685  ? 558 PHE B C    1 
ATOM   5945 O O    . PHE B 1 558 ? 86.37400  121.33800 85.27200  1.000 27.33040  ? 558 PHE B O    1 
ATOM   5946 C CB   . PHE B 1 558 ? 89.11700  121.59400 83.53100  1.000 25.65486  ? 558 PHE B CB   1 
ATOM   5947 C CG   . PHE B 1 558 ? 88.73100  122.97900 83.97100  1.000 31.81378  ? 558 PHE B CG   1 
ATOM   5948 C CD1  . PHE B 1 558 ? 87.65500  123.63200 83.39400  1.000 33.22752  ? 558 PHE B CD1  1 
ATOM   5949 C CD2  . PHE B 1 558 ? 89.42200  123.61200 84.98900  1.000 24.20886  ? 558 PHE B CD2  1 
ATOM   5950 C CE1  . PHE B 1 558 ? 87.28900  124.89600 83.81200  1.000 34.41101  ? 558 PHE B CE1  1 
ATOM   5951 C CE2  . PHE B 1 558 ? 89.06000  124.87600 85.40900  1.000 21.07833  ? 558 PHE B CE2  1 
ATOM   5952 C CZ   . PHE B 1 558 ? 87.99400  125.51800 84.82100  1.000 25.80405  ? 558 PHE B CZ   1 
ATOM   5953 N N    . LYS B 1 559 ? 86.18800  120.37500 83.24800  1.000 32.96999  ? 559 LYS B N    1 
ATOM   5954 C CA   . LYS B 1 559 ? 84.74100  120.58100 83.24300  1.000 29.30344  ? 559 LYS B CA   1 
ATOM   5955 C C    . LYS B 1 559 ? 84.07300  119.80100 84.36800  1.000 35.20158  ? 559 LYS B C    1 
ATOM   5956 O O    . LYS B 1 559 ? 83.18300  120.32100 85.05900  1.000 32.14555  ? 559 LYS B O    1 
ATOM   5957 C CB   . LYS B 1 559 ? 84.14500  120.17400 81.89600  1.000 29.26938  ? 559 LYS B CB   1 
ATOM   5958 C CG   . LYS B 1 559 ? 84.12500  121.27200 80.85500  1.000 34.44597  ? 559 LYS B CG   1 
ATOM   5959 C CD   . LYS B 1 559 ? 83.31200  120.84900 79.64300  1.000 34.82273  ? 559 LYS B CD   1 
ATOM   5960 C CE   . LYS B 1 559 ? 84.13900  120.88900 78.37100  1.000 37.17596  ? 559 LYS B CE   1 
ATOM   5961 N NZ   . LYS B 1 559 ? 83.54800  121.81000 77.36200  1.000 32.61250  ? 559 LYS B NZ   1 
ATOM   5962 N N    . GLU B 1 560 ? 84.51600  118.56400 84.59800  1.000 41.04843  ? 560 GLU B N    1 
ATOM   5963 C CA   . GLU B 1 560 ? 83.90000  117.77200 85.65900  1.000 35.60499  ? 560 GLU B CA   1 
ATOM   5964 C C    . GLU B 1 560 ? 84.16900  118.38000 87.03300  1.000 37.00713  ? 560 GLU B C    1 
ATOM   5965 O O    . GLU B 1 560 ? 83.27200  118.42100 87.88700  1.000 31.98785  ? 560 GLU B O    1 
ATOM   5966 C CB   . GLU B 1 560 ? 84.39600  116.33000 85.60200  1.000 36.13099  ? 560 GLU B CB   1 
ATOM   5967 C CG   . GLU B 1 560 ? 84.12100  115.54000 86.86600  1.000 39.25786  ? 560 GLU B CG   1 
ATOM   5968 C CD   . GLU B 1 560 ? 84.21300  114.04600 86.65000  1.000 44.61234  ? 560 GLU B CD   1 
ATOM   5969 O OE1  . GLU B 1 560 ? 84.27000  113.61700 85.47900  1.000 42.25991  ? 560 GLU B OE1  1 
ATOM   5970 O OE2  . GLU B 1 560 ? 84.22700  113.29800 87.65000  1.000 46.43246  ? 560 GLU B OE2  1 
ATOM   5971 N N    . LEU B 1 561 ? 85.39000  118.87300 87.26100  1.000 32.23100  ? 561 LEU B N    1 
ATOM   5972 C CA   . LEU B 1 561 ? 85.68200  119.51400 88.54100  1.000 27.29958  ? 561 LEU B CA   1 
ATOM   5973 C C    . LEU B 1 561 ? 84.88700  120.80100 88.71600  1.000 34.13941  ? 561 LEU B C    1 
ATOM   5974 O O    . LEU B 1 561 ? 84.37200  121.07500 89.80600  1.000 30.43405  ? 561 LEU B O    1 
ATOM   5975 C CB   . LEU B 1 561 ? 87.17700  119.79700 88.67200  1.000 33.21723  ? 561 LEU B CB   1 
ATOM   5976 C CG   . LEU B 1 561 ? 87.55200  120.69200 89.85900  1.000 28.14016  ? 561 LEU B CG   1 
ATOM   5977 C CD1  . LEU B 1 561 ? 87.26600  119.99900 91.17800  1.000 29.77085  ? 561 LEU B CD1  1 
ATOM   5978 C CD2  . LEU B 1 561 ? 89.00700  121.12100 89.78600  1.000 26.07358  ? 561 LEU B CD2  1 
ATOM   5979 N N    . SER B 1 562 ? 84.77000  121.60500 87.65700  1.000 36.77680  ? 562 SER B N    1 
ATOM   5980 C CA   . SER B 1 562 ? 84.00000  122.83700 87.75300  1.000 29.11224  ? 562 SER B CA   1 
ATOM   5981 C C    . SER B 1 562 ? 82.51600  122.57000 87.94100  1.000 32.22952  ? 562 SER B C    1 
ATOM   5982 O O    . SER B 1 562 ? 81.79100  123.46500 88.38700  1.000 33.99346  ? 562 SER B O    1 
ATOM   5983 C CB   . SER B 1 562 ? 84.21900  123.70200 86.51200  1.000 30.57410  ? 562 SER B CB   1 
ATOM   5984 O OG   . SER B 1 562 ? 83.21000  123.47100 85.54600  1.000 39.15789  ? 562 SER B OG   1 
ATOM   5985 N N    . GLN B 1 563 ? 82.04800  121.36500 87.61600  1.000 47.55119  ? 563 GLN B N    1 
ATOM   5986 C CA   . GLN B 1 563 ? 80.63100  121.08200 87.81700  1.000 41.55621  ? 563 GLN B CA   1 
ATOM   5987 C C    . GLN B 1 563 ? 80.34400  120.46900 89.18300  1.000 40.42301  ? 563 GLN B C    1 
ATOM   5988 O O    . GLN B 1 563 ? 79.33500  120.81000 89.80800  1.000 41.54017  ? 563 GLN B O    1 
ATOM   5989 C CB   . GLN B 1 563 ? 80.10900  120.15300 86.71900  1.000 40.10741  ? 563 GLN B CB   1 
ATOM   5990 C CG   . GLN B 1 563 ? 79.40700  120.87400 85.58000  1.000 44.94044  ? 563 GLN B CG   1 
ATOM   5991 C CD   . GLN B 1 563 ? 79.08900  119.95600 84.41600  1.000 50.96153  ? 563 GLN B CD   1 
ATOM   5992 O OE1  . GLN B 1 563 ? 79.82400  119.00900 84.13800  1.000 50.81375  ? 563 GLN B OE1  1 
ATOM   5993 N NE2  . GLN B 1 563 ? 77.98800  120.23300 83.72800  1.000 46.31387  ? 563 GLN B NE2  1 
ATOM   5994 N N    . LYS B 1 564 ? 81.20500  119.57300 89.67400  1.000 43.93096  ? 564 LYS B N    1 
ATOM   5995 C CA   . LYS B 1 564 ? 80.96300  118.99700 90.99400  1.000 36.07976  ? 564 LYS B CA   1 
ATOM   5996 C C    . LYS B 1 564 ? 81.27500  119.95900 92.13600  1.000 41.63893  ? 564 LYS B C    1 
ATOM   5997 O O    . LYS B 1 564 ? 80.75600  119.77000 93.24000  1.000 34.36767  ? 564 LYS B O    1 
ATOM   5998 C CB   . LYS B 1 564 ? 81.76700  117.71000 91.17800  1.000 33.92561  ? 564 LYS B CB   1 
ATOM   5999 C CG   . LYS B 1 564 ? 81.77800  116.79800 89.97000  1.000 40.80432  ? 564 LYS B CG   1 
ATOM   6000 C CD   . LYS B 1 564 ? 81.83800  115.34200 90.39900  1.000 42.11751  ? 564 LYS B CD   1 
ATOM   6001 C CE   . LYS B 1 564 ? 81.58400  114.40700 89.23100  1.000 39.34596  ? 564 LYS B CE   1 
ATOM   6002 N NZ   . LYS B 1 564 ? 82.33300  113.12900 89.37900  1.000 44.40890  ? 564 LYS B NZ   1 
ATOM   6003 N N    . ALA B 1 565 ? 82.09900  120.98000 91.90600  1.000 47.43796  ? 565 ALA B N    1 
ATOM   6004 C CA   . ALA B 1 565 ? 82.50800  121.89700 92.96200  1.000 29.04458  ? 565 ALA B CA   1 
ATOM   6005 C C    . ALA B 1 565 ? 81.74700  123.21600 92.93200  1.000 39.53884  ? 565 ALA B C    1 
ATOM   6006 O O    . ALA B 1 565 ? 82.06400  124.12000 93.71000  1.000 39.24352  ? 565 ALA B O    1 
ATOM   6007 C CB   . ALA B 1 565 ? 84.01200  122.16200 92.87700  1.000 31.54145  ? 565 ALA B CB   1 
ATOM   6008 N N    . ASN B 1 566 ? 80.74900  123.34100 92.06200  1.000 47.69642  ? 566 ASN B N    1 
ATOM   6009 C CA   . ASN B 1 566 ? 79.88200  124.51500 92.00100  1.000 41.29221  ? 566 ASN B CA   1 
ATOM   6010 C C    . ASN B 1 566 ? 80.68900  125.80300 91.83200  1.000 40.64487  ? 566 ASN B C    1 
ATOM   6011 O O    . ASN B 1 566 ? 80.68500  126.69300 92.68300  1.000 43.67363  ? 566 ASN B O    1 
ATOM   6012 C CB   . ASN B 1 566 ? 78.98800  124.58500 93.24000  1.000 40.67722  ? 566 ASN B CB   1 
ATOM   6013 C CG   . ASN B 1 566 ? 77.86100  125.58500 93.08800  1.000 49.68839  ? 566 ASN B CG   1 
ATOM   6014 O OD1  . ASN B 1 566 ? 76.79500  125.25900 92.56700  1.000 48.70937  ? 566 ASN B OD1  1 
ATOM   6015 N ND2  . ASN B 1 566 ? 78.09200  126.81000 93.54300  1.000 46.30209  ? 566 ASN B ND2  1 
ATOM   6016 N N    . PHE B 1 567 ? 81.38800  125.89100 90.70400  1.000 37.96680  ? 567 PHE B N    1 
ATOM   6017 C CA   . PHE B 1 567 ? 82.06000  127.12700 90.33300  1.000 33.15695  ? 567 PHE B CA   1 
ATOM   6018 C C    . PHE B 1 567 ? 81.04400  128.13400 89.80100  1.000 38.47324  ? 567 PHE B C    1 
ATOM   6019 O O    . PHE B 1 567 ? 79.94700  127.77700 89.36500  1.000 47.78519  ? 567 PHE B O    1 
ATOM   6020 C CB   . PHE B 1 567 ? 83.14500  126.86200 89.28800  1.000 34.35888  ? 567 PHE B CB   1 
ATOM   6021 C CG   . PHE B 1 567 ? 84.40600  126.26800 89.85400  1.000 35.98780  ? 567 PHE B CG   1 
ATOM   6022 C CD1  . PHE B 1 567 ? 84.47200  125.87700 91.17900  1.000 33.61860  ? 567 PHE B CD1  1 
ATOM   6023 C CD2  . PHE B 1 567 ? 85.52500  126.09800 89.05600  1.000 36.85716  ? 567 PHE B CD2  1 
ATOM   6024 C CE1  . PHE B 1 567 ? 85.63000  125.32900 91.69900  1.000 33.75694  ? 567 PHE B CE1  1 
ATOM   6025 C CE2  . PHE B 1 567 ? 86.68500  125.55000 89.57100  1.000 32.82940  ? 567 PHE B CE2  1 
ATOM   6026 C CZ   . PHE B 1 567 ? 86.73700  125.16700 90.89400  1.000 30.23235  ? 567 PHE B CZ   1 
ATOM   6027 N N    . LYS B 1 568 ? 81.41800  129.40800 89.83800  1.000 45.05217  ? 568 LYS B N    1 
ATOM   6028 C CA   . LYS B 1 568 ? 80.50100  130.46900 89.45200  1.000 44.50728  ? 568 LYS B CA   1 
ATOM   6029 C C    . LYS B 1 568 ? 80.58600  130.75800 87.95600  1.000 48.03068  ? 568 LYS B C    1 
ATOM   6030 O O    . LYS B 1 568 ? 81.56500  130.42900 87.28400  1.000 50.44896  ? 568 LYS B O    1 
ATOM   6031 C CB   . LYS B 1 568 ? 80.78300  131.74300 90.24800  1.000 45.46953  ? 568 LYS B CB   1 
ATOM   6032 C CG   . LYS B 1 568 ? 82.15400  132.34200 90.00500  1.000 47.38036  ? 568 LYS B CG   1 
ATOM   6033 C CD   . LYS B 1 568 ? 82.09200  133.85900 89.99600  1.000 46.92211  ? 568 LYS B CD   1 
ATOM   6034 C CE   . LYS B 1 568 ? 83.41000  134.46700 90.44100  1.000 50.45312  ? 568 LYS B CE   1 
ATOM   6035 N NZ   . LYS B 1 568 ? 83.66500  134.22600 91.88700  1.000 51.17336  ? 568 LYS B NZ   1 
ATOM   6036 N N    . GLU B 1 569 ? 79.56700  131.41100 87.41800  1.000 54.24600  ? 569 GLU B N    1 
ATOM   6037 C CA   . GLU B 1 569 ? 79.54000  131.72700 85.98600  1.000 57.68945  ? 569 GLU B CA   1 
ATOM   6038 C C    . GLU B 1 569 ? 80.58600  132.75300 85.58200  1.000 60.44309  ? 569 GLU B C    1 
ATOM   6039 O O    . GLU B 1 569 ? 80.75000  133.76500 86.25400  1.000 59.38909  ? 569 GLU B O    1 
ATOM   6040 C CB   . GLU B 1 569 ? 78.15400  132.22100 85.58600  1.000 58.58422  ? 569 GLU B CB   1 
ATOM   6041 C CG   . GLU B 1 569 ? 77.67900  131.71100 84.23800  1.000 61.22485  ? 569 GLU B CG   1 
ATOM   6042 C CD   . GLU B 1 569 ? 77.31400  130.24200 84.27200  1.000 63.07337  ? 569 GLU B CD   1 
ATOM   6043 O OE1  . GLU B 1 569 ? 76.95100  129.74600 85.35800  1.000 64.03317  ? 569 GLU B OE1  1 
ATOM   6044 O OE2  . GLU B 1 569 ? 77.38800  129.58300 83.21400  1.000 60.96337  ? 569 GLU B OE2  1 
ATOM   6045 N N    . PRO B 1 570 ? 81.27400  132.51900 84.45200  1.000 63.57594  ? 570 PRO B N    1 
ATOM   6046 C CA   . PRO B 1 570 ? 82.36600  133.41600 84.04800  1.000 59.86445  ? 570 PRO B CA   1 
ATOM   6047 C C    . PRO B 1 570 ? 81.95100  134.86700 83.94500  1.000 60.88210  ? 570 PRO B C    1 
ATOM   6048 O O    . PRO B 1 570 ? 82.64900  135.72200 84.48200  1.000 59.71114  ? 570 PRO B O    1 
ATOM   6049 C CB   . PRO B 1 570 ? 82.73500  132.91100 82.65500  1.000 57.11699  ? 570 PRO B CB   1 
ATOM   6050 C CG   . PRO B 1 570 ? 81.60500  132.03400 82.22300  1.000 60.94376  ? 570 PRO B CG   1 
ATOM   6051 C CD   . PRO B 1 570 ? 81.05600  131.44200 83.47800  1.000 60.33285  ? 570 PRO B CD   1 
ATOM   6052 N N    . GLU B 1 571 ? 80.84200  135.14100 83.27300  1.000 70.60719  ? 571 GLU B N    1 
ATOM   6053 C CA   . GLU B 1 571 ? 80.36600  136.50500 83.09800  1.000 70.39575  ? 571 GLU B CA   1 
ATOM   6054 C C    . GLU B 1 571 ? 81.08100  137.49100 84.01200  1.000 70.50757  ? 571 GLU B C    1 
ATOM   6055 O O    . GLU B 1 571 ? 81.69100  138.45000 83.54300  1.000 68.81754  ? 571 GLU B O    1 
ATOM   6056 C CB   . GLU B 1 571 ? 78.86100  136.55800 83.34500  1.000 67.36607  ? 571 GLU B CB   1 
HETATM 6057 C C1   . D10 C 2 .   ? 127.53100 118.22300 129.65900 1.000 38.88491  ? 601 D10 A C1   1 
HETATM 6058 C C2   . D10 C 2 .   ? 126.76800 117.05300 130.23500 1.000 39.49638  ? 601 D10 A C2   1 
HETATM 6059 C C3   . D10 C 2 .   ? 125.67000 116.60400 129.28100 1.000 37.47894  ? 601 D10 A C3   1 
HETATM 6060 C C4   . D10 C 2 .   ? 124.39400 116.30800 130.05300 1.000 35.34590  ? 601 D10 A C4   1 
HETATM 6061 C C5   . D10 C 2 .   ? 123.40400 115.53400 129.19700 1.000 33.98682  ? 601 D10 A C5   1 
HETATM 6062 C C6   . D10 C 2 .   ? 122.78100 114.41000 130.00600 1.000 33.81755  ? 601 D10 A C6   1 
HETATM 6063 C C7   . D10 C 2 .   ? 121.45300 113.97300 129.41400 1.000 31.58927  ? 601 D10 A C7   1 
HETATM 6064 C C8   . D10 C 2 .   ? 120.45100 113.71900 130.52800 1.000 37.58755  ? 601 D10 A C8   1 
HETATM 6065 C C9   . D10 C 2 .   ? 119.15500 113.14100 129.97400 1.000 44.94550  ? 601 D10 A C9   1 
HETATM 6066 C C10  . D10 C 2 .   ? 117.95600 113.86000 130.55000 1.000 39.58429  ? 601 D10 A C10  1 
HETATM 6067 H H11  . D10 C 2 .   ? 126.86800 119.03700 129.52200 1.000 35.81740  ? 601 D10 A H11  1 
HETATM 6068 H H12  . D10 C 2 .   ? 127.94500 117.94400 128.72500 1.000 35.14542  ? 601 D10 A H12  1 
HETATM 6069 H H13  . D10 C 2 .   ? 128.30600 118.50300 130.32400 1.000 35.31634  ? 601 D10 A H13  1 
HETATM 6070 H H21  . D10 C 2 .   ? 127.45200 116.22400 130.42100 1.000 36.20042  ? 601 D10 A H21  1 
HETATM 6071 H H22  . D10 C 2 .   ? 126.32000 117.34400 131.18700 1.000 35.13933  ? 601 D10 A H22  1 
HETATM 6072 H H31  . D10 C 2 .   ? 125.47800 117.39100 128.54900 1.000 35.21854  ? 601 D10 A H31  1 
HETATM 6073 H H32  . D10 C 2 .   ? 125.99300 115.71100 128.74400 1.000 35.28768  ? 601 D10 A H32  1 
HETATM 6074 H H41  . D10 C 2 .   ? 124.63700 115.72500 130.94300 1.000 34.81276  ? 601 D10 A H41  1 
HETATM 6075 H H42  . D10 C 2 .   ? 123.94100 117.24600 130.37700 1.000 35.63308  ? 601 D10 A H42  1 
HETATM 6076 H H51  . D10 C 2 .   ? 123.91300 115.12200 128.32300 1.000 33.83460  ? 601 D10 A H51  1 
HETATM 6077 H H52  . D10 C 2 .   ? 122.62300 116.21100 128.84500 1.000 35.41665  ? 601 D10 A H52  1 
HETATM 6078 H H61  . D10 C 2 .   ? 123.46600 113.56000 130.03600 1.000 36.65423  ? 601 D10 A H61  1 
HETATM 6079 H H62  . D10 C 2 .   ? 122.62100 114.74900 131.03100 1.000 35.77582  ? 601 D10 A H62  1 
HETATM 6080 H H71  . D10 C 2 .   ? 121.59300 113.05900 128.83400 1.000 34.98814  ? 601 D10 A H71  1 
HETATM 6081 H H72  . D10 C 2 .   ? 121.07100 114.74500 128.74500 1.000 34.77451  ? 601 D10 A H72  1 
HETATM 6082 H H81  . D10 C 2 .   ? 120.88300 113.02300 131.25100 1.000 37.05747  ? 601 D10 A H81  1 
HETATM 6083 H H82  . D10 C 2 .   ? 120.23900 114.65500 131.04700 1.000 35.66798  ? 601 D10 A H82  1 
HETATM 6084 H H91  . D10 C 2 .   ? 119.15100 113.23800 128.88700 1.000 35.43957  ? 601 D10 A H91  1 
HETATM 6085 H H92  . D10 C 2 .   ? 119.09600 112.07900 130.22200 1.000 36.35176  ? 601 D10 A H92  1 
HETATM 6086 H H101 . D10 C 2 .   ? 118.02200 114.89200 130.32300 1.000 34.59713  ? 601 D10 A H101 1 
HETATM 6087 H H102 . D10 C 2 .   ? 117.06900 113.45900 130.13300 1.000 34.59267  ? 601 D10 A H102 1 
HETATM 6088 H H103 . D10 C 2 .   ? 117.94300 113.73000 131.60200 1.000 36.14413  ? 601 D10 A H103 1 
HETATM 6089 C C1   . PLM D 3 .   ? 125.20300 107.23100 124.79500 1.000 39.90009  ? 602 PLM A C1   1 
HETATM 6090 O O1   . PLM D 3 .   ? 125.10000 107.65200 125.96700 1.000 37.66305  ? 602 PLM A O1   1 
HETATM 6091 O O2   . PLM D 3 .   ? 126.27400 106.78000 124.33700 1.000 39.15776  ? 602 PLM A O2   1 
HETATM 6092 C C2   . PLM D 3 .   ? 124.06900 107.52200 123.84400 1.000 31.15975  ? 602 PLM A C2   1 
HETATM 6093 C C3   . PLM D 3 .   ? 124.21200 106.71800 122.55900 1.000 30.44363  ? 602 PLM A C3   1 
HETATM 6094 C C4   . PLM D 3 .   ? 123.26200 107.23300 121.49100 1.000 29.35913  ? 602 PLM A C4   1 
HETATM 6095 C C5   . PLM D 3 .   ? 121.82800 107.21600 121.99100 1.000 21.87016  ? 602 PLM A C5   1 
HETATM 6096 C C6   . PLM D 3 .   ? 121.46400 108.54000 122.64100 1.000 23.79233  ? 602 PLM A C6   1 
HETATM 6097 C C7   . PLM D 3 .   ? 120.25900 109.15000 121.95200 1.000 29.65789  ? 602 PLM A C7   1 
HETATM 6098 C C8   . PLM D 3 .   ? 119.52600 110.06200 122.91500 1.000 28.05963  ? 602 PLM A C8   1 
HETATM 6099 C C9   . PLM D 3 .   ? 118.48900 109.26700 123.68300 1.000 30.03047  ? 602 PLM A C9   1 
HETATM 6100 C CA   . PLM D 3 .   ? 117.29300 108.97000 122.79800 1.000 21.78755  ? 602 PLM A CA   1 
HETATM 6101 C CB   . PLM D 3 .   ? 116.00900 109.07100 123.60400 1.000 24.96976  ? 602 PLM A CB   1 
HETATM 6102 C CC   . PLM D 3 .   ? 115.44000 110.47600 123.54100 1.000 28.39885  ? 602 PLM A CC   1 
HETATM 6103 C CD   . PLM D 3 .   ? 114.38700 110.56400 122.44800 1.000 28.32539  ? 602 PLM A CD   1 
HETATM 6104 C CE   . PLM D 3 .   ? 114.01700 112.01300 122.18400 1.000 30.78775  ? 602 PLM A CE   1 
HETATM 6105 C CF   . PLM D 3 .   ? 112.75400 112.10100 121.34500 1.000 31.47008  ? 602 PLM A CF   1 
HETATM 6106 C CG   . PLM D 3 .   ? 113.01200 111.59800 119.94600 1.000 30.21064  ? 602 PLM A CG   1 
HETATM 6107 H H21  . PLM D 3 .   ? 123.12300 107.27400 124.32900 1.000 28.32608  ? 602 PLM A H21  1 
HETATM 6108 H H22  . PLM D 3 .   ? 124.05900 108.58700 123.60400 1.000 27.61072  ? 602 PLM A H22  1 
HETATM 6109 H H31  . PLM D 3 .   ? 125.23400 106.79300 122.18600 1.000 28.29720  ? 602 PLM A H31  1 
HETATM 6110 H H32  . PLM D 3 .   ? 123.99900 105.66700 122.76100 1.000 27.38471  ? 602 PLM A H32  1 
HETATM 6111 H H41  . PLM D 3 .   ? 123.54300 108.25000 121.21200 1.000 27.33314  ? 602 PLM A H41  1 
HETATM 6112 H H42  . PLM D 3 .   ? 123.34400 106.60600 120.60000 1.000 27.01573  ? 602 PLM A H42  1 
HETATM 6113 H H51  . PLM D 3 .   ? 121.70600 106.41000 122.71700 1.000 27.31173  ? 602 PLM A H51  1 
HETATM 6114 H H52  . PLM D 3 .   ? 121.15600 107.02100 121.15400 1.000 26.31384  ? 602 PLM A H52  1 
HETATM 6115 H H61  . PLM D 3 .   ? 121.23700 108.37800 123.69700 1.000 26.95476  ? 602 PLM A H61  1 
HETATM 6116 H H62  . PLM D 3 .   ? 122.30300 109.23300 122.57700 1.000 26.77003  ? 602 PLM A H62  1 
HETATM 6117 H H71  . PLM D 3 .   ? 120.58700 109.72100 121.08300 1.000 27.81313  ? 602 PLM A H71  1 
HETATM 6118 H H72  . PLM D 3 .   ? 119.58800 108.36100 121.61000 1.000 26.65307  ? 602 PLM A H72  1 
HETATM 6119 H H81  . PLM D 3 .   ? 120.23900 110.50600 123.61100 1.000 27.90675  ? 602 PLM A H81  1 
HETATM 6120 H H82  . PLM D 3 .   ? 119.04100 110.86900 122.36200 1.000 27.49127  ? 602 PLM A H82  1 
HETATM 6121 H H91  . PLM D 3 .   ? 118.92900 108.33100 124.03000 1.000 28.47260  ? 602 PLM A H91  1 
HETATM 6122 H H92  . PLM D 3 .   ? 118.16500 109.83700 124.55600 1.000 28.10424  ? 602 PLM A H92  1 
HETATM 6123 H HA1  . PLM D 3 .   ? 117.26100 109.68100 121.97000 1.000 26.41504  ? 602 PLM A HA1  1 
HETATM 6124 H HA2  . PLM D 3 .   ? 117.38800 107.96600 122.37900 1.000 25.97807  ? 602 PLM A HA2  1 
HETATM 6125 H HB1  . PLM D 3 .   ? 116.20900 108.80100 124.64300 1.000 26.65902  ? 602 PLM A HB1  1 
HETATM 6126 H HB2  . PLM D 3 .   ? 115.27600 108.36700 123.20600 1.000 27.27103  ? 602 PLM A HB2  1 
HETATM 6127 H HC1  . PLM D 3 .   ? 114.99100 110.73600 124.50200 1.000 27.68850  ? 602 PLM A HC1  1 
HETATM 6128 H HC2  . PLM D 3 .   ? 116.24200 111.18800 123.33500 1.000 27.49541  ? 602 PLM A HC2  1 
HETATM 6129 H HD1  . PLM D 3 .   ? 114.77600 110.11100 121.53400 1.000 26.55582  ? 602 PLM A HD1  1 
HETATM 6130 H HD2  . PLM D 3 .   ? 113.49800 110.00800 122.75100 1.000 26.55471  ? 602 PLM A HD2  1 
HETATM 6131 H HE1  . PLM D 3 .   ? 113.86100 112.52400 123.13400 1.000 26.93224  ? 602 PLM A HE1  1 
HETATM 6132 H HE2  . PLM D 3 .   ? 114.83600 112.51300 121.66500 1.000 27.81335  ? 602 PLM A HE2  1 
HETATM 6133 H HF1  . PLM D 3 .   ? 111.96600 111.50500 121.81000 1.000 27.58139  ? 602 PLM A HF1  1 
HETATM 6134 H HF2  . PLM D 3 .   ? 112.41700 113.13800 121.30400 1.000 27.66648  ? 602 PLM A HF2  1 
HETATM 6135 H HG1  . PLM D 3 .   ? 113.06900 110.54100 119.95600 1.000 26.96711  ? 602 PLM A HG1  1 
HETATM 6136 H HG2  . PLM D 3 .   ? 113.92800 111.99900 119.59900 1.000 28.45455  ? 602 PLM A HG2  1 
HETATM 6137 H HG3  . PLM D 3 .   ? 112.22500 111.90600 119.30900 1.000 27.85185  ? 602 PLM A HG3  1 
HETATM 6138 C C1   . OCT E 4 .   ? 97.15100  104.78800 129.54800 1.000 35.56051  ? 601 OCT B C1   1 
HETATM 6139 C C2   . OCT E 4 .   ? 95.65600  104.59400 129.29700 1.000 39.51272  ? 601 OCT B C2   1 
HETATM 6140 C C3   . OCT E 4 .   ? 94.99700  103.94800 130.51500 1.000 36.43265  ? 601 OCT B C3   1 
HETATM 6141 C C4   . OCT E 4 .   ? 93.72900  103.20100 130.10800 1.000 40.26980  ? 601 OCT B C4   1 
HETATM 6142 C C5   . OCT E 4 .   ? 93.41500  102.14600 131.16900 1.000 39.59032  ? 601 OCT B C5   1 
HETATM 6143 C C6   . OCT E 4 .   ? 91.90500  101.94100 131.30300 1.000 37.37876  ? 601 OCT B C6   1 
HETATM 6144 C C7   . OCT E 4 .   ? 91.38800  101.02000 130.19700 1.000 38.99323  ? 601 OCT B C7   1 
HETATM 6145 C C8   . OCT E 4 .   ? 91.15200  101.79900 128.90200 1.000 34.99236  ? 601 OCT B C8   1 
HETATM 6146 H H11  . OCT E 4 .   ? 97.41600  104.42000 130.53100 1.000 36.67758  ? 601 OCT B H11  1 
HETATM 6147 H H12  . OCT E 4 .   ? 97.39100  105.84200 129.48300 1.000 36.40451  ? 601 OCT B H12  1 
HETATM 6148 H H13  . OCT E 4 .   ? 97.71400  104.24600 128.79800 1.000 35.58650  ? 601 OCT B H13  1 
HETATM 6149 H H21  . OCT E 4 .   ? 95.19700  105.55600 129.11100 1.000 36.79763  ? 601 OCT B H21  1 
HETATM 6150 H H22  . OCT E 4 .   ? 95.52200  103.95900 128.43000 1.000 35.82512  ? 601 OCT B H22  1 
HETATM 6151 H H31  . OCT E 4 .   ? 95.68200  103.23800 130.95800 1.000 37.03191  ? 601 OCT B H31  1 
HETATM 6152 H H32  . OCT E 4 .   ? 94.74900  104.71300 131.24100 1.000 36.66264  ? 601 OCT B H32  1 
HETATM 6153 H H41  . OCT E 4 .   ? 93.88100  102.71300 129.15400 1.000 36.43490  ? 601 OCT B H41  1 
HETATM 6154 H H42  . OCT E 4 .   ? 92.90800  103.90200 130.02900 1.000 36.32114  ? 601 OCT B H42  1 
HETATM 6155 H H51  . OCT E 4 .   ? 93.81300  102.47400 132.12200 1.000 36.92090  ? 601 OCT B H51  1 
HETATM 6156 H H52  . OCT E 4 .   ? 93.88400  101.21100 130.89200 1.000 36.83251  ? 601 OCT B H52  1 
HETATM 6157 H H61  . OCT E 4 .   ? 91.39900  102.89700 131.25300 1.000 36.71751  ? 601 OCT B H61  1 
HETATM 6158 H H62  . OCT E 4 .   ? 91.69800  101.48600 132.26400 1.000 36.18495  ? 601 OCT B H62  1 
HETATM 6159 H H71  . OCT E 4 .   ? 92.11000  100.23400 130.01300 1.000 35.97493  ? 601 OCT B H71  1 
HETATM 6160 H H72  . OCT E 4 .   ? 90.45400  100.57400 130.51600 1.000 36.64201  ? 601 OCT B H72  1 
HETATM 6161 H H81  . OCT E 4 .   ? 92.03100  101.72500 128.27300 1.000 35.49831  ? 601 OCT B H81  1 
HETATM 6162 H H82  . OCT E 4 .   ? 90.95600  102.83900 129.12700 1.000 36.51530  ? 601 OCT B H82  1 
HETATM 6163 H H83  . OCT E 4 .   ? 90.30200  101.37800 128.38100 1.000 35.78523  ? 601 OCT B H83  1 
HETATM 6164 O O    . HOH F 5 .   ? 114.31600 110.68200 117.40400 1.000 26.53202  ? 701 HOH A O    1 
HETATM 6165 O O    . HOH G 5 .   ? 106.18300 108.07000 121.15700 1.000 21.17271  ? 701 HOH B O    1 
HETATM 6166 O O    . HOH G 5 .   ? 111.00300 110.55500 134.48800 1.000 40.31354  ? 702 HOH B O    1 
HETATM 6167 O O    . HOH G 5 .   ? 107.92600 108.50700 134.32200 1.000 31.20773  ? 703 HOH B O    1 
# 
