data_8ZTN
# 
_entry.id   8ZTN 
# 
_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   8ZTN         pdb_00008ztn 10.2210/pdb8ztn/pdb 
WWPDB D_1300047467 ?            ?                   
EMDB  EMD-60468    ?            ?                   
# 
_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                        8ZTN 
_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 (trans2 class)' 
_pdbx_database_related.db_id          EMD-60468 
_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 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE        704.998   2 ? ? ? ? 
3 water       nat water                                     18.015    2 ? ? ? ? 
# 
_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 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE 3PH 
3 water                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   ALA n 
1 4   LYS n 
1 5   GLN n 
1 6   GLY n 
1 7   SER n 
1 8   PHE n 
1 9   ARG n 
1 10  HIS n 
1 11  GLY n 
1 12  ILE n 
1 13  LEU n 
1 14  GLU n 
1 15  LYS n 
1 16  ARG n 
1 17  GLU n 
1 18  ARG n 
1 19  LEU n 
1 20  LEU n 
1 21  SER n 
1 22  ASN n 
1 23  ASN n 
1 24  GLY n 
1 25  PHE n 
1 26  SER n 
1 27  ASP n 
1 28  PHE n 
1 29  ARG n 
1 30  PHE n 
1 31  THR n 
1 32  ASP n 
1 33  ILE n 
1 34  GLU n 
1 35  SER n 
1 36  ASN n 
1 37  ASP n 
1 38  LEU n 
1 39  LEU n 
1 40  GLU n 
1 41  ASN n 
1 42  GLU n 
1 43  ASN n 
1 44  CYS n 
1 45  GLY n 
1 46  ARG n 
1 47  ARG n 
1 48  THR n 
1 49  ARG n 
1 50  LEU n 
1 51  CYS n 
1 52  CYS n 
1 53  CYS n 
1 54  CYS n 
1 55  SER n 
1 56  CYS n 
1 57  GLY n 
1 58  ASN n 
1 59  LEU n 
1 60  SER n 
1 61  GLU n 
1 62  LYS n 
1 63  ILE n 
1 64  SER n 
1 65  GLY n 
1 66  VAL n 
1 67  TYR n 
1 68  ASP n 
1 69  ASP n 
1 70  ALA n 
1 71  LYS n 
1 72  ASP n 
1 73  VAL n 
1 74  ALA n 
1 75  ARG n 
1 76  LYS n 
1 77  ALA n 
1 78  TRP n 
1 79  GLU n 
1 80  MET n 
1 81  GLY n 
1 82  VAL n 
1 83  SER n 
1 84  ASP n 
1 85  PRO n 
1 86  ARG n 
1 87  LYS n 
1 88  ILE n 
1 89  VAL n 
1 90  PHE n 
1 91  SER n 
1 92  ALA n 
1 93  LYS n 
1 94  ILE n 
1 95  GLY n 
1 96  LEU n 
1 97  ALA n 
1 98  LEU n 
1 99  THR n 
1 100 ILE n 
1 101 VAL n 
1 102 ALA n 
1 103 LEU n 
1 104 LEU n 
1 105 ILE n 
1 106 PHE n 
1 107 TYR n 
1 108 GLN n 
1 109 GLU n 
1 110 PRO n 
1 111 ASN n 
1 112 PRO n 
1 113 ASP n 
1 114 LEU n 
1 115 SER n 
1 116 ARG n 
1 117 TYR n 
1 118 SER n 
1 119 VAL n 
1 120 TRP n 
1 121 ALA n 
1 122 ILE n 
1 123 LEU n 
1 124 THR n 
1 125 VAL n 
1 126 VAL n 
1 127 VAL n 
1 128 VAL n 
1 129 PHE n 
1 130 GLU n 
1 131 PHE n 
1 132 THR n 
1 133 ILE n 
1 134 GLY n 
1 135 ALA n 
1 136 THR n 
1 137 LEU n 
1 138 SER n 
1 139 LYS n 
1 140 GLY n 
1 141 PHE n 
1 142 ASN n 
1 143 ARG n 
1 144 ALA n 
1 145 LEU n 
1 146 GLY n 
1 147 THR n 
1 148 LEU n 
1 149 SER n 
1 150 ALA n 
1 151 GLY n 
1 152 GLY n 
1 153 LEU n 
1 154 ALA n 
1 155 LEU n 
1 156 GLY n 
1 157 MET n 
1 158 ALA n 
1 159 GLU n 
1 160 LEU n 
1 161 SER n 
1 162 THR n 
1 163 LEU n 
1 164 PHE n 
1 165 GLY n 
1 166 ASP n 
1 167 TRP n 
1 168 GLU n 
1 169 GLU n 
1 170 ILE n 
1 171 PHE n 
1 172 CYS n 
1 173 THR n 
1 174 LEU n 
1 175 SER n 
1 176 ILE n 
1 177 PHE n 
1 178 CYS n 
1 179 ILE n 
1 180 GLY n 
1 181 PHE n 
1 182 LEU n 
1 183 ALA n 
1 184 THR n 
1 185 PHE n 
1 186 MET n 
1 187 LYS n 
1 188 LEU n 
1 189 TYR n 
1 190 PRO n 
1 191 SER n 
1 192 MET n 
1 193 LYS n 
1 194 ALA n 
1 195 TYR n 
1 196 GLU n 
1 197 TYR n 
1 198 GLY n 
1 199 PHE n 
1 200 ARG n 
1 201 VAL n 
1 202 PHE n 
1 203 LEU n 
1 204 LEU n 
1 205 THR n 
1 206 TYR n 
1 207 CYS n 
1 208 TYR n 
1 209 ILE n 
1 210 LEU n 
1 211 ILE n 
1 212 SER n 
1 213 GLY n 
1 214 PHE n 
1 215 ARG n 
1 216 THR n 
1 217 GLY n 
1 218 GLN n 
1 219 PHE n 
1 220 ILE n 
1 221 GLU n 
1 222 VAL n 
1 223 ALA n 
1 224 ILE n 
1 225 SER n 
1 226 ARG n 
1 227 PHE n 
1 228 LEU n 
1 229 LEU n 
1 230 ILE n 
1 231 ALA n 
1 232 LEU n 
1 233 GLY n 
1 234 ALA n 
1 235 GLY n 
1 236 VAL n 
1 237 SER n 
1 238 LEU n 
1 239 GLY n 
1 240 VAL n 
1 241 ASN n 
1 242 MET n 
1 243 PHE n 
1 244 ILE n 
1 245 TYR n 
1 246 PRO n 
1 247 ILE n 
1 248 TRP n 
1 249 ALA n 
1 250 GLY n 
1 251 GLU n 
1 252 ASP n 
1 253 LEU n 
1 254 HIS n 
1 255 ASN n 
1 256 LEU n 
1 257 VAL n 
1 258 VAL n 
1 259 LYS n 
1 260 ASN n 
1 261 PHE n 
1 262 MET n 
1 263 ASN n 
1 264 VAL n 
1 265 ALA n 
1 266 THR n 
1 267 SER n 
1 268 LEU n 
1 269 GLU n 
1 270 GLY n 
1 271 CYS n 
1 272 VAL n 
1 273 ASN n 
1 274 GLY n 
1 275 TYR n 
1 276 LEU n 
1 277 ARG n 
1 278 CYS n 
1 279 LEU n 
1 280 GLU n 
1 281 TYR n 
1 282 GLU n 
1 283 ARG n 
1 284 ILE n 
1 285 PRO n 
1 286 SER n 
1 287 LYS n 
1 288 ILE n 
1 289 LEU n 
1 290 THR n 
1 291 TYR n 
1 292 GLN n 
1 293 ALA n 
1 294 SER n 
1 295 GLU n 
1 296 ASP n 
1 297 PRO n 
1 298 VAL n 
1 299 TYR n 
1 300 LYS n 
1 301 GLY n 
1 302 TYR n 
1 303 ARG n 
1 304 SER n 
1 305 ALA n 
1 306 VAL n 
1 307 GLU n 
1 308 SER n 
1 309 THR n 
1 310 SER n 
1 311 GLN n 
1 312 GLU n 
1 313 GLU n 
1 314 SER n 
1 315 LEU n 
1 316 MET n 
1 317 SER n 
1 318 PHE n 
1 319 ALA n 
1 320 ILE n 
1 321 TRP n 
1 322 GLU n 
1 323 PRO n 
1 324 PRO n 
1 325 HIS n 
1 326 GLY n 
1 327 PRO n 
1 328 TYR n 
1 329 LYS n 
1 330 SER n 
1 331 PHE n 
1 332 ASN n 
1 333 TYR n 
1 334 PRO n 
1 335 TRP n 
1 336 LYS n 
1 337 ASN n 
1 338 TYR n 
1 339 VAL n 
1 340 LYS n 
1 341 LEU n 
1 342 SER n 
1 343 GLY n 
1 344 ALA n 
1 345 LEU n 
1 346 LYS n 
1 347 HIS n 
1 348 CYS n 
1 349 ALA n 
1 350 PHE n 
1 351 THR n 
1 352 VAL n 
1 353 MET n 
1 354 ALA n 
1 355 LEU n 
1 356 HIS n 
1 357 GLY n 
1 358 CYS n 
1 359 ILE n 
1 360 LEU n 
1 361 SER n 
1 362 GLU n 
1 363 ILE n 
1 364 GLN n 
1 365 ALA n 
1 366 PRO n 
1 367 GLU n 
1 368 GLU n 
1 369 ARG n 
1 370 ARG n 
1 371 GLN n 
1 372 VAL n 
1 373 PHE n 
1 374 ARG n 
1 375 GLN n 
1 376 GLU n 
1 377 LEU n 
1 378 GLN n 
1 379 ARG n 
1 380 VAL n 
1 381 GLY n 
1 382 VAL n 
1 383 GLU n 
1 384 GLY n 
1 385 ALA n 
1 386 LYS n 
1 387 LEU n 
1 388 LEU n 
1 389 ARG n 
1 390 GLU n 
1 391 LEU n 
1 392 GLY n 
1 393 GLU n 
1 394 LYS n 
1 395 VAL n 
1 396 LYS n 
1 397 LYS n 
1 398 MET n 
1 399 GLU n 
1 400 LYS n 
1 401 LEU n 
1 402 GLY n 
1 403 PRO n 
1 404 VAL n 
1 405 ASP n 
1 406 LEU n 
1 407 LEU n 
1 408 PHE n 
1 409 GLU n 
1 410 VAL n 
1 411 HIS n 
1 412 LEU n 
1 413 ALA n 
1 414 ALA n 
1 415 GLU n 
1 416 GLU n 
1 417 LEU n 
1 418 GLN n 
1 419 HIS n 
1 420 LYS n 
1 421 ILE n 
1 422 ASP n 
1 423 LYS n 
1 424 LYS n 
1 425 SER n 
1 426 TYR n 
1 427 LEU n 
1 428 LEU n 
1 429 VAL n 
1 430 ASN n 
1 431 SER n 
1 432 GLU n 
1 433 CYS n 
1 434 TRP n 
1 435 GLU n 
1 436 ILE n 
1 437 GLY n 
1 438 ASN n 
1 439 ARG n 
1 440 ALA n 
1 441 THR n 
1 442 LYS n 
1 443 GLU n 
1 444 SER n 
1 445 GLU n 
1 446 PRO n 
1 447 GLN n 
1 448 GLU n 
1 449 LEU n 
1 450 LEU n 
1 451 SER n 
1 452 LEU n 
1 453 GLU n 
1 454 ASP n 
1 455 SER n 
1 456 ASP n 
1 457 PRO n 
1 458 PRO n 
1 459 GLU n 
1 460 ASN n 
1 461 HIS n 
1 462 ALA n 
1 463 PRO n 
1 464 PRO n 
1 465 ILE n 
1 466 TYR n 
1 467 ALA n 
1 468 PHE n 
1 469 LYS n 
1 470 SER n 
1 471 LEU n 
1 472 SER n 
1 473 GLU n 
1 474 ALA n 
1 475 VAL n 
1 476 LEU n 
1 477 GLU n 
1 478 ILE n 
1 479 PRO n 
1 480 PRO n 
1 481 SER n 
1 482 TRP n 
1 483 GLY n 
1 484 GLU n 
1 485 LYS n 
1 486 ASN n 
1 487 HIS n 
1 488 ARG n 
1 489 GLU n 
1 490 ALA n 
1 491 LEU n 
1 492 ASN n 
1 493 HIS n 
1 494 ARG n 
1 495 PRO n 
1 496 THR n 
1 497 PHE n 
1 498 SER n 
1 499 LYS n 
1 500 GLN n 
1 501 VAL n 
1 502 SER n 
1 503 TRP n 
1 504 PRO n 
1 505 ALA n 
1 506 ARG n 
1 507 LEU n 
1 508 VAL n 
1 509 LEU n 
1 510 PRO n 
1 511 PRO n 
1 512 HIS n 
1 513 LEU n 
1 514 GLU n 
1 515 THR n 
1 516 THR n 
1 517 ASN n 
1 518 GLY n 
1 519 ALA n 
1 520 SER n 
1 521 PRO n 
1 522 LEU n 
1 523 VAL n 
1 524 GLU n 
1 525 THR n 
1 526 THR n 
1 527 LYS n 
1 528 THR n 
1 529 TYR n 
1 530 GLU n 
1 531 SER n 
1 532 ALA n 
1 533 SER n 
1 534 ALA n 
1 535 LEU n 
1 536 SER n 
1 537 LEU n 
1 538 ALA n 
1 539 THR n 
1 540 PHE n 
1 541 ALA n 
1 542 SER n 
1 543 LEU n 
1 544 LEU n 
1 545 ILE n 
1 546 GLU n 
1 547 PHE n 
1 548 VAL n 
1 549 ALA n 
1 550 ARG n 
1 551 LEU n 
1 552 GLN n 
1 553 ASN n 
1 554 VAL n 
1 555 VAL n 
1 556 ASP n 
1 557 ALA n 
1 558 PHE n 
1 559 LYS n 
1 560 GLU n 
1 561 LEU n 
1 562 SER n 
1 563 GLN n 
1 564 LYS n 
1 565 ALA n 
1 566 ASN n 
1 567 PHE n 
1 568 LYS n 
1 569 GLU n 
1 570 PRO n 
1 571 GLU n 
1 572 ILE n 
1 573 VAL n 
1 574 THR n 
1 575 THR n 
1 576 GLY n 
1 577 THR n 
1 578 ASP n 
1 579 VAL n 
1 580 GLU n 
1 581 PHE n 
1 582 SER n 
1 583 GLY n 
1 584 GLU n 
1 585 ARG n 
1 586 VAL n 
1 587 GLY n 
1 588 LEU n 
1 589 GLY n 
1 590 GLN n 
1 591 LYS n 
1 592 ILE n 
1 593 ARG n 
1 594 ARG n 
1 595 CYS n 
1 596 PHE n 
1 597 GLY n 
1 598 MET n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   598 
_entity_src_gen.gene_src_common_name               'thale cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ALMT9, At3g18440, MYF24.16' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            Sf9 
_entity_src_gen.pdbx_host_org_atcc                 CRL-1711 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          Bacmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
3PH non-polymer         . 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE 'PHOSPHATIDIC ACID' 'C39 H77 O8 P'   704.998 
ALA 'L-peptide linking' y ALANINE                            ?                   'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                           ?                   'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                         ?                   'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                    ?                   'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                           ?                   'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                          ?                   'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ?                   'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                            ?                   'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                          ?                   'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                              ?                   'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                         ?                   'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                            ?                   'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                             ?                   'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                         ?                   'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                      ?                   'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                            ?                   'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                             ?                   'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                          ?                   'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                         ?                   'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                           ?                   'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                             ?                   'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   PHE 8   8   ?   ?   ?   A . n 
A 1 9   ARG 9   9   ?   ?   ?   A . n 
A 1 10  HIS 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  ?   ?   ?   A . n 
A 1 12  ILE 12  12  ?   ?   ?   A . n 
A 1 13  LEU 13  13  ?   ?   ?   A . n 
A 1 14  GLU 14  14  ?   ?   ?   A . n 
A 1 15  LYS 15  15  ?   ?   ?   A . n 
A 1 16  ARG 16  16  ?   ?   ?   A . n 
A 1 17  GLU 17  17  ?   ?   ?   A . n 
A 1 18  ARG 18  18  ?   ?   ?   A . n 
A 1 19  LEU 19  19  ?   ?   ?   A . n 
A 1 20  LEU 20  20  ?   ?   ?   A . n 
A 1 21  SER 21  21  ?   ?   ?   A . n 
A 1 22  ASN 22  22  ?   ?   ?   A . n 
A 1 23  ASN 23  23  ?   ?   ?   A . n 
A 1 24  GLY 24  24  ?   ?   ?   A . n 
A 1 25  PHE 25  25  ?   ?   ?   A . n 
A 1 26  SER 26  26  ?   ?   ?   A . n 
A 1 27  ASP 27  27  ?   ?   ?   A . n 
A 1 28  PHE 28  28  ?   ?   ?   A . n 
A 1 29  ARG 29  29  ?   ?   ?   A . n 
A 1 30  PHE 30  30  ?   ?   ?   A . n 
A 1 31  THR 31  31  ?   ?   ?   A . n 
A 1 32  ASP 32  32  ?   ?   ?   A . n 
A 1 33  ILE 33  33  ?   ?   ?   A . n 
A 1 34  GLU 34  34  ?   ?   ?   A . n 
A 1 35  SER 35  35  ?   ?   ?   A . n 
A 1 36  ASN 36  36  ?   ?   ?   A . n 
A 1 37  ASP 37  37  ?   ?   ?   A . n 
A 1 38  LEU 38  38  ?   ?   ?   A . n 
A 1 39  LEU 39  39  ?   ?   ?   A . n 
A 1 40  GLU 40  40  ?   ?   ?   A . n 
A 1 41  ASN 41  41  ?   ?   ?   A . n 
A 1 42  GLU 42  42  ?   ?   ?   A . n 
A 1 43  ASN 43  43  ?   ?   ?   A . n 
A 1 44  CYS 44  44  ?   ?   ?   A . n 
A 1 45  GLY 45  45  ?   ?   ?   A . n 
A 1 46  ARG 46  46  ?   ?   ?   A . n 
A 1 47  ARG 47  47  ?   ?   ?   A . n 
A 1 48  THR 48  48  ?   ?   ?   A . n 
A 1 49  ARG 49  49  ?   ?   ?   A . n 
A 1 50  LEU 50  50  ?   ?   ?   A . n 
A 1 51  CYS 51  51  ?   ?   ?   A . n 
A 1 52  CYS 52  52  ?   ?   ?   A . n 
A 1 53  CYS 53  53  ?   ?   ?   A . n 
A 1 54  CYS 54  54  ?   ?   ?   A . n 
A 1 55  SER 55  55  ?   ?   ?   A . n 
A 1 56  CYS 56  56  ?   ?   ?   A . n 
A 1 57  GLY 57  57  ?   ?   ?   A . n 
A 1 58  ASN 58  58  ?   ?   ?   A . n 
A 1 59  LEU 59  59  ?   ?   ?   A . n 
A 1 60  SER 60  60  ?   ?   ?   A . n 
A 1 61  GLU 61  61  ?   ?   ?   A . n 
A 1 62  LYS 62  62  ?   ?   ?   A . n 
A 1 63  ILE 63  63  ?   ?   ?   A . n 
A 1 64  SER 64  64  ?   ?   ?   A . n 
A 1 65  GLY 65  65  ?   ?   ?   A . n 
A 1 66  VAL 66  66  ?   ?   ?   A . n 
A 1 67  TYR 67  67  ?   ?   ?   A . n 
A 1 68  ASP 68  68  ?   ?   ?   A . n 
A 1 69  ASP 69  69  ?   ?   ?   A . n 
A 1 70  ALA 70  70  ?   ?   ?   A . n 
A 1 71  LYS 71  71  ?   ?   ?   A . n 
A 1 72  ASP 72  72  ?   ?   ?   A . n 
A 1 73  VAL 73  73  ?   ?   ?   A . n 
A 1 74  ALA 74  74  ?   ?   ?   A . n 
A 1 75  ARG 75  75  ?   ?   ?   A . n 
A 1 76  LYS 76  76  ?   ?   ?   A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  MET 80  80  80  MET MET A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 GLN 108 108 108 GLN GLN A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 TRP 120 120 120 TRP TRP A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 TRP 167 167 167 TRP TRP A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 CYS 172 172 172 CYS CYS A . n 
A 1 173 THR 173 173 173 THR THR A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 TYR 189 189 189 TYR TYR A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 CYS 207 207 207 CYS CYS A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 ASN 241 241 241 ASN ASN A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 TRP 248 248 248 TRP TRP A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 GLY 250 250 250 GLY GLY A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 HIS 254 254 254 HIS HIS A . n 
A 1 255 ASN 255 255 255 ASN ASN A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 CYS 271 271 271 CYS CYS A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 CYS 278 278 278 CYS CYS A . n 
A 1 279 LEU 279 279 ?   ?   ?   A . n 
A 1 280 GLU 280 280 ?   ?   ?   A . n 
A 1 281 TYR 281 281 ?   ?   ?   A . n 
A 1 282 GLU 282 282 ?   ?   ?   A . n 
A 1 283 ARG 283 283 ?   ?   ?   A . n 
A 1 284 ILE 284 284 ?   ?   ?   A . n 
A 1 285 PRO 285 285 ?   ?   ?   A . n 
A 1 286 SER 286 286 ?   ?   ?   A . n 
A 1 287 LYS 287 287 ?   ?   ?   A . n 
A 1 288 ILE 288 288 ?   ?   ?   A . n 
A 1 289 LEU 289 289 ?   ?   ?   A . n 
A 1 290 THR 290 290 ?   ?   ?   A . n 
A 1 291 TYR 291 291 ?   ?   ?   A . n 
A 1 292 GLN 292 292 ?   ?   ?   A . n 
A 1 293 ALA 293 293 ?   ?   ?   A . n 
A 1 294 SER 294 294 ?   ?   ?   A . n 
A 1 295 GLU 295 295 ?   ?   ?   A . n 
A 1 296 ASP 296 296 ?   ?   ?   A . n 
A 1 297 PRO 297 297 ?   ?   ?   A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 LYS 300 300 300 LYS LYS A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 GLN 311 311 311 GLN GLN A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 SER 314 314 314 SER SER A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 MET 316 316 316 MET MET A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 PRO 323 323 323 PRO PRO A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 HIS 325 325 325 HIS HIS A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 TYR 328 328 328 TYR TYR A . n 
A 1 329 LYS 329 329 329 LYS LYS A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 TYR 333 333 333 TYR TYR A . n 
A 1 334 PRO 334 334 334 PRO PRO A . n 
A 1 335 TRP 335 335 335 TRP TRP A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 TYR 338 338 338 TYR TYR A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 LYS 340 340 340 LYS LYS A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 HIS 347 347 347 HIS HIS A . n 
A 1 348 CYS 348 348 348 CYS CYS A . n 
A 1 349 ALA 349 349 349 ALA ALA A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 MET 353 353 353 MET MET A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 LEU 355 355 355 LEU LEU A . n 
A 1 356 HIS 356 356 356 HIS HIS A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 CYS 358 358 358 CYS CYS A . n 
A 1 359 ILE 359 359 359 ILE ILE A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 SER 361 361 361 SER SER A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 GLN 364 364 364 GLN GLN A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 ARG 370 370 370 ARG ARG A . n 
A 1 371 GLN 371 371 371 GLN GLN A . n 
A 1 372 VAL 372 372 372 VAL VAL A . n 
A 1 373 PHE 373 373 373 PHE PHE A . n 
A 1 374 ARG 374 374 374 ARG ARG A . n 
A 1 375 GLN 375 375 375 GLN GLN A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 GLN 378 378 378 GLN GLN A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 GLY 381 381 381 GLY GLY A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 LYS 386 386 386 LYS LYS A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 ARG 389 389 389 ARG ARG A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 LYS 397 397 397 LYS LYS A . n 
A 1 398 MET 398 398 398 MET MET A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 PHE 408 408 408 PHE PHE A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 VAL 410 410 410 VAL VAL A . n 
A 1 411 HIS 411 411 411 HIS HIS A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 ALA 414 414 414 ALA ALA A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 GLU 416 416 416 GLU GLU A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 GLN 418 418 418 GLN GLN A . n 
A 1 419 HIS 419 419 419 HIS HIS A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 ILE 421 421 421 ILE ILE A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 LYS 424 424 424 LYS LYS A . n 
A 1 425 SER 425 425 425 SER SER A . n 
A 1 426 TYR 426 426 426 TYR TYR A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 VAL 429 429 429 VAL VAL A . n 
A 1 430 ASN 430 430 430 ASN ASN A . n 
A 1 431 SER 431 431 431 SER SER A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 CYS 433 433 433 CYS CYS A . n 
A 1 434 TRP 434 434 434 TRP TRP A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 ILE 436 436 ?   ?   ?   A . n 
A 1 437 GLY 437 437 ?   ?   ?   A . n 
A 1 438 ASN 438 438 ?   ?   ?   A . n 
A 1 439 ARG 439 439 ?   ?   ?   A . n 
A 1 440 ALA 440 440 ?   ?   ?   A . n 
A 1 441 THR 441 441 ?   ?   ?   A . n 
A 1 442 LYS 442 442 ?   ?   ?   A . n 
A 1 443 GLU 443 443 ?   ?   ?   A . n 
A 1 444 SER 444 444 ?   ?   ?   A . n 
A 1 445 GLU 445 445 ?   ?   ?   A . n 
A 1 446 PRO 446 446 ?   ?   ?   A . n 
A 1 447 GLN 447 447 ?   ?   ?   A . n 
A 1 448 GLU 448 448 ?   ?   ?   A . n 
A 1 449 LEU 449 449 ?   ?   ?   A . n 
A 1 450 LEU 450 450 ?   ?   ?   A . n 
A 1 451 SER 451 451 ?   ?   ?   A . n 
A 1 452 LEU 452 452 ?   ?   ?   A . n 
A 1 453 GLU 453 453 ?   ?   ?   A . n 
A 1 454 ASP 454 454 ?   ?   ?   A . n 
A 1 455 SER 455 455 ?   ?   ?   A . n 
A 1 456 ASP 456 456 ?   ?   ?   A . n 
A 1 457 PRO 457 457 ?   ?   ?   A . n 
A 1 458 PRO 458 458 ?   ?   ?   A . n 
A 1 459 GLU 459 459 ?   ?   ?   A . n 
A 1 460 ASN 460 460 ?   ?   ?   A . n 
A 1 461 HIS 461 461 ?   ?   ?   A . n 
A 1 462 ALA 462 462 ?   ?   ?   A . n 
A 1 463 PRO 463 463 ?   ?   ?   A . n 
A 1 464 PRO 464 464 ?   ?   ?   A . n 
A 1 465 ILE 465 465 ?   ?   ?   A . n 
A 1 466 TYR 466 466 ?   ?   ?   A . n 
A 1 467 ALA 467 467 ?   ?   ?   A . n 
A 1 468 PHE 468 468 ?   ?   ?   A . n 
A 1 469 LYS 469 469 ?   ?   ?   A . n 
A 1 470 SER 470 470 ?   ?   ?   A . n 
A 1 471 LEU 471 471 ?   ?   ?   A . n 
A 1 472 SER 472 472 ?   ?   ?   A . n 
A 1 473 GLU 473 473 ?   ?   ?   A . n 
A 1 474 ALA 474 474 ?   ?   ?   A . n 
A 1 475 VAL 475 475 ?   ?   ?   A . n 
A 1 476 LEU 476 476 ?   ?   ?   A . n 
A 1 477 GLU 477 477 ?   ?   ?   A . n 
A 1 478 ILE 478 478 ?   ?   ?   A . n 
A 1 479 PRO 479 479 ?   ?   ?   A . n 
A 1 480 PRO 480 480 ?   ?   ?   A . n 
A 1 481 SER 481 481 ?   ?   ?   A . n 
A 1 482 TRP 482 482 ?   ?   ?   A . n 
A 1 483 GLY 483 483 ?   ?   ?   A . n 
A 1 484 GLU 484 484 ?   ?   ?   A . n 
A 1 485 LYS 485 485 ?   ?   ?   A . n 
A 1 486 ASN 486 486 ?   ?   ?   A . n 
A 1 487 HIS 487 487 ?   ?   ?   A . n 
A 1 488 ARG 488 488 ?   ?   ?   A . n 
A 1 489 GLU 489 489 ?   ?   ?   A . n 
A 1 490 ALA 490 490 ?   ?   ?   A . n 
A 1 491 LEU 491 491 ?   ?   ?   A . n 
A 1 492 ASN 492 492 ?   ?   ?   A . n 
A 1 493 HIS 493 493 ?   ?   ?   A . n 
A 1 494 ARG 494 494 ?   ?   ?   A . n 
A 1 495 PRO 495 495 ?   ?   ?   A . n 
A 1 496 THR 496 496 ?   ?   ?   A . n 
A 1 497 PHE 497 497 ?   ?   ?   A . n 
A 1 498 SER 498 498 ?   ?   ?   A . n 
A 1 499 LYS 499 499 ?   ?   ?   A . n 
A 1 500 GLN 500 500 ?   ?   ?   A . n 
A 1 501 VAL 501 501 ?   ?   ?   A . n 
A 1 502 SER 502 502 ?   ?   ?   A . n 
A 1 503 TRP 503 503 ?   ?   ?   A . n 
A 1 504 PRO 504 504 ?   ?   ?   A . n 
A 1 505 ALA 505 505 ?   ?   ?   A . n 
A 1 506 ARG 506 506 ?   ?   ?   A . n 
A 1 507 LEU 507 507 ?   ?   ?   A . n 
A 1 508 VAL 508 508 ?   ?   ?   A . n 
A 1 509 LEU 509 509 ?   ?   ?   A . n 
A 1 510 PRO 510 510 ?   ?   ?   A . n 
A 1 511 PRO 511 511 ?   ?   ?   A . n 
A 1 512 HIS 512 512 ?   ?   ?   A . n 
A 1 513 LEU 513 513 ?   ?   ?   A . n 
A 1 514 GLU 514 514 ?   ?   ?   A . n 
A 1 515 THR 515 515 ?   ?   ?   A . n 
A 1 516 THR 516 516 ?   ?   ?   A . n 
A 1 517 ASN 517 517 ?   ?   ?   A . n 
A 1 518 GLY 518 518 ?   ?   ?   A . n 
A 1 519 ALA 519 519 ?   ?   ?   A . n 
A 1 520 SER 520 520 ?   ?   ?   A . n 
A 1 521 PRO 521 521 ?   ?   ?   A . n 
A 1 522 LEU 522 522 ?   ?   ?   A . n 
A 1 523 VAL 523 523 ?   ?   ?   A . n 
A 1 524 GLU 524 524 ?   ?   ?   A . n 
A 1 525 THR 525 525 ?   ?   ?   A . n 
A 1 526 THR 526 526 ?   ?   ?   A . n 
A 1 527 LYS 527 527 527 LYS LYS A . n 
A 1 528 THR 528 528 528 THR THR A . n 
A 1 529 TYR 529 529 529 TYR TYR A . n 
A 1 530 GLU 530 530 530 GLU GLU A . n 
A 1 531 SER 531 531 531 SER SER A . n 
A 1 532 ALA 532 532 532 ALA ALA A . n 
A 1 533 SER 533 533 533 SER SER A . n 
A 1 534 ALA 534 534 534 ALA ALA A . n 
A 1 535 LEU 535 535 535 LEU LEU A . n 
A 1 536 SER 536 536 536 SER SER A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 ALA 538 538 538 ALA ALA A . n 
A 1 539 THR 539 539 539 THR THR A . n 
A 1 540 PHE 540 540 540 PHE PHE A . n 
A 1 541 ALA 541 541 541 ALA ALA A . n 
A 1 542 SER 542 542 542 SER SER A . n 
A 1 543 LEU 543 543 543 LEU LEU A . n 
A 1 544 LEU 544 544 544 LEU LEU A . n 
A 1 545 ILE 545 545 545 ILE ILE A . n 
A 1 546 GLU 546 546 546 GLU GLU A . n 
A 1 547 PHE 547 547 547 PHE PHE A . n 
A 1 548 VAL 548 548 548 VAL VAL A . n 
A 1 549 ALA 549 549 549 ALA ALA A . n 
A 1 550 ARG 550 550 550 ARG ARG A . n 
A 1 551 LEU 551 551 551 LEU LEU A . n 
A 1 552 GLN 552 552 552 GLN GLN A . n 
A 1 553 ASN 553 553 553 ASN ASN A . n 
A 1 554 VAL 554 554 554 VAL VAL A . n 
A 1 555 VAL 555 555 555 VAL VAL A . n 
A 1 556 ASP 556 556 556 ASP ASP A . n 
A 1 557 ALA 557 557 557 ALA ALA A . n 
A 1 558 PHE 558 558 558 PHE PHE A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 GLU 560 560 560 GLU GLU A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 SER 562 562 562 SER SER A . n 
A 1 563 GLN 563 563 563 GLN GLN A . n 
A 1 564 LYS 564 564 564 LYS LYS A . n 
A 1 565 ALA 565 565 565 ALA ALA A . n 
A 1 566 ASN 566 566 566 ASN ASN A . n 
A 1 567 PHE 567 567 567 PHE PHE A . n 
A 1 568 LYS 568 568 568 LYS LYS A . n 
A 1 569 GLU 569 569 569 GLU GLU A . n 
A 1 570 PRO 570 570 570 PRO PRO A . n 
A 1 571 GLU 571 571 571 GLU GLU A . n 
A 1 572 ILE 572 572 ?   ?   ?   A . n 
A 1 573 VAL 573 573 ?   ?   ?   A . n 
A 1 574 THR 574 574 ?   ?   ?   A . n 
A 1 575 THR 575 575 ?   ?   ?   A . n 
A 1 576 GLY 576 576 ?   ?   ?   A . n 
A 1 577 THR 577 577 ?   ?   ?   A . n 
A 1 578 ASP 578 578 ?   ?   ?   A . n 
A 1 579 VAL 579 579 ?   ?   ?   A . n 
A 1 580 GLU 580 580 ?   ?   ?   A . n 
A 1 581 PHE 581 581 ?   ?   ?   A . n 
A 1 582 SER 582 582 ?   ?   ?   A . n 
A 1 583 GLY 583 583 ?   ?   ?   A . n 
A 1 584 GLU 584 584 ?   ?   ?   A . n 
A 1 585 ARG 585 585 ?   ?   ?   A . n 
A 1 586 VAL 586 586 ?   ?   ?   A . n 
A 1 587 GLY 587 587 ?   ?   ?   A . n 
A 1 588 LEU 588 588 ?   ?   ?   A . n 
A 1 589 GLY 589 589 ?   ?   ?   A . n 
A 1 590 GLN 590 590 ?   ?   ?   A . n 
A 1 591 LYS 591 591 ?   ?   ?   A . n 
A 1 592 ILE 592 592 ?   ?   ?   A . n 
A 1 593 ARG 593 593 ?   ?   ?   A . n 
A 1 594 ARG 594 594 ?   ?   ?   A . n 
A 1 595 CYS 595 595 ?   ?   ?   A . n 
A 1 596 PHE 596 596 ?   ?   ?   A . n 
A 1 597 GLY 597 597 ?   ?   ?   A . n 
A 1 598 MET 598 598 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   ALA 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   SER 7   7   ?   ?   ?   B . n 
B 1 8   PHE 8   8   ?   ?   ?   B . n 
B 1 9   ARG 9   9   ?   ?   ?   B . n 
B 1 10  HIS 10  10  ?   ?   ?   B . n 
B 1 11  GLY 11  11  ?   ?   ?   B . n 
B 1 12  ILE 12  12  ?   ?   ?   B . n 
B 1 13  LEU 13  13  ?   ?   ?   B . n 
B 1 14  GLU 14  14  ?   ?   ?   B . n 
B 1 15  LYS 15  15  ?   ?   ?   B . n 
B 1 16  ARG 16  16  ?   ?   ?   B . n 
B 1 17  GLU 17  17  ?   ?   ?   B . n 
B 1 18  ARG 18  18  ?   ?   ?   B . n 
B 1 19  LEU 19  19  ?   ?   ?   B . n 
B 1 20  LEU 20  20  ?   ?   ?   B . n 
B 1 21  SER 21  21  ?   ?   ?   B . n 
B 1 22  ASN 22  22  ?   ?   ?   B . n 
B 1 23  ASN 23  23  ?   ?   ?   B . n 
B 1 24  GLY 24  24  ?   ?   ?   B . n 
B 1 25  PHE 25  25  ?   ?   ?   B . n 
B 1 26  SER 26  26  ?   ?   ?   B . n 
B 1 27  ASP 27  27  ?   ?   ?   B . n 
B 1 28  PHE 28  28  ?   ?   ?   B . n 
B 1 29  ARG 29  29  ?   ?   ?   B . n 
B 1 30  PHE 30  30  ?   ?   ?   B . n 
B 1 31  THR 31  31  ?   ?   ?   B . n 
B 1 32  ASP 32  32  ?   ?   ?   B . n 
B 1 33  ILE 33  33  ?   ?   ?   B . n 
B 1 34  GLU 34  34  ?   ?   ?   B . n 
B 1 35  SER 35  35  ?   ?   ?   B . n 
B 1 36  ASN 36  36  ?   ?   ?   B . n 
B 1 37  ASP 37  37  ?   ?   ?   B . n 
B 1 38  LEU 38  38  ?   ?   ?   B . n 
B 1 39  LEU 39  39  ?   ?   ?   B . n 
B 1 40  GLU 40  40  ?   ?   ?   B . n 
B 1 41  ASN 41  41  ?   ?   ?   B . n 
B 1 42  GLU 42  42  ?   ?   ?   B . n 
B 1 43  ASN 43  43  ?   ?   ?   B . n 
B 1 44  CYS 44  44  ?   ?   ?   B . n 
B 1 45  GLY 45  45  ?   ?   ?   B . n 
B 1 46  ARG 46  46  ?   ?   ?   B . n 
B 1 47  ARG 47  47  ?   ?   ?   B . n 
B 1 48  THR 48  48  ?   ?   ?   B . n 
B 1 49  ARG 49  49  ?   ?   ?   B . n 
B 1 50  LEU 50  50  ?   ?   ?   B . n 
B 1 51  CYS 51  51  ?   ?   ?   B . n 
B 1 52  CYS 52  52  ?   ?   ?   B . n 
B 1 53  CYS 53  53  ?   ?   ?   B . n 
B 1 54  CYS 54  54  ?   ?   ?   B . n 
B 1 55  SER 55  55  ?   ?   ?   B . n 
B 1 56  CYS 56  56  ?   ?   ?   B . n 
B 1 57  GLY 57  57  ?   ?   ?   B . n 
B 1 58  ASN 58  58  ?   ?   ?   B . n 
B 1 59  LEU 59  59  ?   ?   ?   B . n 
B 1 60  SER 60  60  ?   ?   ?   B . n 
B 1 61  GLU 61  61  ?   ?   ?   B . n 
B 1 62  LYS 62  62  ?   ?   ?   B . n 
B 1 63  ILE 63  63  ?   ?   ?   B . n 
B 1 64  SER 64  64  ?   ?   ?   B . n 
B 1 65  GLY 65  65  ?   ?   ?   B . n 
B 1 66  VAL 66  66  ?   ?   ?   B . n 
B 1 67  TYR 67  67  ?   ?   ?   B . n 
B 1 68  ASP 68  68  ?   ?   ?   B . n 
B 1 69  ASP 69  69  ?   ?   ?   B . n 
B 1 70  ALA 70  70  ?   ?   ?   B . n 
B 1 71  LYS 71  71  ?   ?   ?   B . n 
B 1 72  ASP 72  72  ?   ?   ?   B . n 
B 1 73  VAL 73  73  ?   ?   ?   B . n 
B 1 74  ALA 74  74  ?   ?   ?   B . n 
B 1 75  ARG 75  75  ?   ?   ?   B . n 
B 1 76  LYS 76  76  ?   ?   ?   B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  TRP 78  78  78  TRP TRP B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  MET 80  80  80  MET MET B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  ILE 88  88  88  ILE ILE B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  PHE 90  90  90  PHE PHE B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  LEU 96  96  96  LEU LEU B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 PHE 106 106 106 PHE PHE B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 GLN 108 108 108 GLN GLN B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 PRO 110 110 110 PRO PRO B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 PRO 112 112 112 PRO PRO B . n 
B 1 113 ASP 113 113 113 ASP ASP B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 TRP 120 120 120 TRP TRP B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 ILE 133 133 133 ILE ILE B . n 
B 1 134 GLY 134 134 134 GLY GLY B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 THR 136 136 136 THR THR B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 SER 138 138 138 SER SER B . n 
B 1 139 LYS 139 139 139 LYS LYS B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 PHE 141 141 141 PHE PHE B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 MET 157 157 157 MET MET B . n 
B 1 158 ALA 158 158 158 ALA ALA B . n 
B 1 159 GLU 159 159 159 GLU GLU B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 SER 161 161 161 SER SER B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 LEU 163 163 163 LEU LEU B . n 
B 1 164 PHE 164 164 164 PHE PHE B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 ASP 166 166 166 ASP ASP B . n 
B 1 167 TRP 167 167 167 TRP TRP B . n 
B 1 168 GLU 168 168 168 GLU GLU B . n 
B 1 169 GLU 169 169 169 GLU GLU B . n 
B 1 170 ILE 170 170 170 ILE ILE B . n 
B 1 171 PHE 171 171 171 PHE PHE B . n 
B 1 172 CYS 172 172 172 CYS CYS B . n 
B 1 173 THR 173 173 173 THR THR B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 ILE 176 176 176 ILE ILE B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 CYS 178 178 178 CYS CYS B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 THR 184 184 184 THR THR B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 MET 186 186 186 MET MET B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 TYR 189 189 189 TYR TYR B . n 
B 1 190 PRO 190 190 190 PRO PRO B . n 
B 1 191 SER 191 191 191 SER SER B . n 
B 1 192 MET 192 192 192 MET MET B . n 
B 1 193 LYS 193 193 193 LYS LYS B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 TYR 195 195 195 TYR TYR B . n 
B 1 196 GLU 196 196 196 GLU GLU B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 PHE 199 199 199 PHE PHE B . n 
B 1 200 ARG 200 200 200 ARG ARG B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 PHE 202 202 202 PHE PHE B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 TYR 206 206 206 TYR TYR B . n 
B 1 207 CYS 207 207 207 CYS CYS B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 SER 212 212 212 SER SER B . n 
B 1 213 GLY 213 213 213 GLY GLY B . n 
B 1 214 PHE 214 214 214 PHE PHE B . n 
B 1 215 ARG 215 215 215 ARG ARG B . n 
B 1 216 THR 216 216 216 THR THR B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 GLN 218 218 218 GLN GLN B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 VAL 222 222 222 VAL VAL B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ILE 224 224 224 ILE ILE B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 PHE 227 227 227 PHE PHE B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 ILE 230 230 230 ILE ILE B . n 
B 1 231 ALA 231 231 231 ALA ALA B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 GLY 233 233 233 GLY GLY B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 GLY 235 235 235 GLY GLY B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 SER 237 237 237 SER SER B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 VAL 240 240 240 VAL VAL B . n 
B 1 241 ASN 241 241 241 ASN ASN B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 TYR 245 245 245 TYR TYR B . n 
B 1 246 PRO 246 246 246 PRO PRO B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 TRP 248 248 248 TRP TRP B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 GLY 250 250 250 GLY GLY B . n 
B 1 251 GLU 251 251 251 GLU GLU B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 HIS 254 254 254 HIS HIS B . n 
B 1 255 ASN 255 255 255 ASN ASN B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 VAL 258 258 258 VAL VAL B . n 
B 1 259 LYS 259 259 259 LYS LYS B . n 
B 1 260 ASN 260 260 260 ASN ASN B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 MET 262 262 262 MET MET B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 VAL 264 264 264 VAL VAL B . n 
B 1 265 ALA 265 265 265 ALA ALA B . n 
B 1 266 THR 266 266 266 THR THR B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 CYS 271 271 271 CYS CYS B . n 
B 1 272 VAL 272 272 272 VAL VAL B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 GLY 274 274 274 GLY GLY B . n 
B 1 275 TYR 275 275 275 TYR TYR B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 ARG 277 277 277 ARG ARG B . n 
B 1 278 CYS 278 278 278 CYS CYS B . n 
B 1 279 LEU 279 279 ?   ?   ?   B . n 
B 1 280 GLU 280 280 ?   ?   ?   B . n 
B 1 281 TYR 281 281 ?   ?   ?   B . n 
B 1 282 GLU 282 282 ?   ?   ?   B . n 
B 1 283 ARG 283 283 ?   ?   ?   B . n 
B 1 284 ILE 284 284 ?   ?   ?   B . n 
B 1 285 PRO 285 285 ?   ?   ?   B . n 
B 1 286 SER 286 286 ?   ?   ?   B . n 
B 1 287 LYS 287 287 ?   ?   ?   B . n 
B 1 288 ILE 288 288 ?   ?   ?   B . n 
B 1 289 LEU 289 289 ?   ?   ?   B . n 
B 1 290 THR 290 290 ?   ?   ?   B . n 
B 1 291 TYR 291 291 ?   ?   ?   B . n 
B 1 292 GLN 292 292 ?   ?   ?   B . n 
B 1 293 ALA 293 293 ?   ?   ?   B . n 
B 1 294 SER 294 294 ?   ?   ?   B . n 
B 1 295 GLU 295 295 ?   ?   ?   B . n 
B 1 296 ASP 296 296 ?   ?   ?   B . n 
B 1 297 PRO 297 297 ?   ?   ?   B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 LYS 300 300 300 LYS LYS B . n 
B 1 301 GLY 301 301 301 GLY GLY B . n 
B 1 302 TYR 302 302 302 TYR TYR B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 VAL 306 306 306 VAL VAL B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 SER 308 308 308 SER SER B . n 
B 1 309 THR 309 309 309 THR THR B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 GLN 311 311 311 GLN GLN B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 GLU 313 313 313 GLU GLU B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 LEU 315 315 315 LEU LEU B . n 
B 1 316 MET 316 316 316 MET MET B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 PHE 318 318 318 PHE PHE B . n 
B 1 319 ALA 319 319 319 ALA ALA B . n 
B 1 320 ILE 320 320 320 ILE ILE B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 GLU 322 322 322 GLU GLU B . n 
B 1 323 PRO 323 323 323 PRO PRO B . n 
B 1 324 PRO 324 324 324 PRO PRO B . n 
B 1 325 HIS 325 325 325 HIS HIS B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 PRO 327 327 327 PRO PRO B . n 
B 1 328 TYR 328 328 328 TYR TYR B . n 
B 1 329 LYS 329 329 329 LYS LYS B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 PHE 331 331 331 PHE PHE B . n 
B 1 332 ASN 332 332 332 ASN ASN B . n 
B 1 333 TYR 333 333 333 TYR TYR B . n 
B 1 334 PRO 334 334 334 PRO PRO B . n 
B 1 335 TRP 335 335 335 TRP TRP B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ASN 337 337 337 ASN ASN B . n 
B 1 338 TYR 338 338 338 TYR TYR B . n 
B 1 339 VAL 339 339 339 VAL VAL B . n 
B 1 340 LYS 340 340 340 LYS LYS B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 SER 342 342 342 SER SER B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 ALA 344 344 344 ALA ALA B . n 
B 1 345 LEU 345 345 345 LEU LEU B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 HIS 347 347 347 HIS HIS B . n 
B 1 348 CYS 348 348 348 CYS CYS B . n 
B 1 349 ALA 349 349 349 ALA ALA B . n 
B 1 350 PHE 350 350 350 PHE PHE B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 VAL 352 352 352 VAL VAL B . n 
B 1 353 MET 353 353 353 MET MET B . n 
B 1 354 ALA 354 354 354 ALA ALA B . n 
B 1 355 LEU 355 355 355 LEU LEU B . n 
B 1 356 HIS 356 356 356 HIS HIS B . n 
B 1 357 GLY 357 357 357 GLY GLY B . n 
B 1 358 CYS 358 358 358 CYS CYS B . n 
B 1 359 ILE 359 359 359 ILE ILE B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 SER 361 361 361 SER SER B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 ILE 363 363 363 ILE ILE B . n 
B 1 364 GLN 364 364 364 GLN GLN B . n 
B 1 365 ALA 365 365 365 ALA ALA B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 GLU 367 367 367 GLU GLU B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ARG 369 369 369 ARG ARG B . n 
B 1 370 ARG 370 370 370 ARG ARG B . n 
B 1 371 GLN 371 371 371 GLN GLN B . n 
B 1 372 VAL 372 372 372 VAL VAL B . n 
B 1 373 PHE 373 373 373 PHE PHE B . n 
B 1 374 ARG 374 374 374 ARG ARG B . n 
B 1 375 GLN 375 375 375 GLN GLN B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 LEU 377 377 377 LEU LEU B . n 
B 1 378 GLN 378 378 378 GLN GLN B . n 
B 1 379 ARG 379 379 379 ARG ARG B . n 
B 1 380 VAL 380 380 380 VAL VAL B . n 
B 1 381 GLY 381 381 381 GLY GLY B . n 
B 1 382 VAL 382 382 382 VAL VAL B . n 
B 1 383 GLU 383 383 383 GLU GLU B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 ALA 385 385 385 ALA ALA B . n 
B 1 386 LYS 386 386 386 LYS LYS B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 LEU 388 388 388 LEU LEU B . n 
B 1 389 ARG 389 389 389 ARG ARG B . n 
B 1 390 GLU 390 390 390 GLU GLU B . n 
B 1 391 LEU 391 391 391 LEU LEU B . n 
B 1 392 GLY 392 392 392 GLY GLY B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 LYS 394 394 394 LYS LYS B . n 
B 1 395 VAL 395 395 395 VAL VAL B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 LYS 397 397 397 LYS LYS B . n 
B 1 398 MET 398 398 398 MET MET B . n 
B 1 399 GLU 399 399 399 GLU GLU B . n 
B 1 400 LYS 400 400 400 LYS LYS B . n 
B 1 401 LEU 401 401 401 LEU LEU B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 PRO 403 403 403 PRO PRO B . n 
B 1 404 VAL 404 404 404 VAL VAL B . n 
B 1 405 ASP 405 405 405 ASP ASP B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 PHE 408 408 408 PHE PHE B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 VAL 410 410 410 VAL VAL B . n 
B 1 411 HIS 411 411 411 HIS HIS B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 ALA 413 413 413 ALA ALA B . n 
B 1 414 ALA 414 414 414 ALA ALA B . n 
B 1 415 GLU 415 415 415 GLU GLU B . n 
B 1 416 GLU 416 416 416 GLU GLU B . n 
B 1 417 LEU 417 417 417 LEU LEU B . n 
B 1 418 GLN 418 418 418 GLN GLN B . n 
B 1 419 HIS 419 419 419 HIS HIS B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 ILE 421 421 421 ILE ILE B . n 
B 1 422 ASP 422 422 422 ASP ASP B . n 
B 1 423 LYS 423 423 423 LYS LYS B . n 
B 1 424 LYS 424 424 424 LYS LYS B . n 
B 1 425 SER 425 425 425 SER SER B . n 
B 1 426 TYR 426 426 426 TYR TYR B . n 
B 1 427 LEU 427 427 427 LEU LEU B . n 
B 1 428 LEU 428 428 428 LEU LEU B . n 
B 1 429 VAL 429 429 429 VAL VAL B . n 
B 1 430 ASN 430 430 430 ASN ASN B . n 
B 1 431 SER 431 431 431 SER SER B . n 
B 1 432 GLU 432 432 432 GLU GLU B . n 
B 1 433 CYS 433 433 433 CYS CYS B . n 
B 1 434 TRP 434 434 434 TRP TRP B . n 
B 1 435 GLU 435 435 435 GLU GLU B . n 
B 1 436 ILE 436 436 ?   ?   ?   B . n 
B 1 437 GLY 437 437 ?   ?   ?   B . n 
B 1 438 ASN 438 438 ?   ?   ?   B . n 
B 1 439 ARG 439 439 ?   ?   ?   B . n 
B 1 440 ALA 440 440 ?   ?   ?   B . n 
B 1 441 THR 441 441 ?   ?   ?   B . n 
B 1 442 LYS 442 442 ?   ?   ?   B . n 
B 1 443 GLU 443 443 ?   ?   ?   B . n 
B 1 444 SER 444 444 ?   ?   ?   B . n 
B 1 445 GLU 445 445 ?   ?   ?   B . n 
B 1 446 PRO 446 446 ?   ?   ?   B . n 
B 1 447 GLN 447 447 ?   ?   ?   B . n 
B 1 448 GLU 448 448 ?   ?   ?   B . n 
B 1 449 LEU 449 449 ?   ?   ?   B . n 
B 1 450 LEU 450 450 ?   ?   ?   B . n 
B 1 451 SER 451 451 ?   ?   ?   B . n 
B 1 452 LEU 452 452 ?   ?   ?   B . n 
B 1 453 GLU 453 453 ?   ?   ?   B . n 
B 1 454 ASP 454 454 ?   ?   ?   B . n 
B 1 455 SER 455 455 ?   ?   ?   B . n 
B 1 456 ASP 456 456 ?   ?   ?   B . n 
B 1 457 PRO 457 457 ?   ?   ?   B . n 
B 1 458 PRO 458 458 ?   ?   ?   B . n 
B 1 459 GLU 459 459 ?   ?   ?   B . n 
B 1 460 ASN 460 460 ?   ?   ?   B . n 
B 1 461 HIS 461 461 ?   ?   ?   B . n 
B 1 462 ALA 462 462 ?   ?   ?   B . n 
B 1 463 PRO 463 463 ?   ?   ?   B . n 
B 1 464 PRO 464 464 ?   ?   ?   B . n 
B 1 465 ILE 465 465 ?   ?   ?   B . n 
B 1 466 TYR 466 466 ?   ?   ?   B . n 
B 1 467 ALA 467 467 ?   ?   ?   B . n 
B 1 468 PHE 468 468 ?   ?   ?   B . n 
B 1 469 LYS 469 469 ?   ?   ?   B . n 
B 1 470 SER 470 470 ?   ?   ?   B . n 
B 1 471 LEU 471 471 ?   ?   ?   B . n 
B 1 472 SER 472 472 ?   ?   ?   B . n 
B 1 473 GLU 473 473 ?   ?   ?   B . n 
B 1 474 ALA 474 474 ?   ?   ?   B . n 
B 1 475 VAL 475 475 ?   ?   ?   B . n 
B 1 476 LEU 476 476 ?   ?   ?   B . n 
B 1 477 GLU 477 477 ?   ?   ?   B . n 
B 1 478 ILE 478 478 ?   ?   ?   B . n 
B 1 479 PRO 479 479 ?   ?   ?   B . n 
B 1 480 PRO 480 480 ?   ?   ?   B . n 
B 1 481 SER 481 481 ?   ?   ?   B . n 
B 1 482 TRP 482 482 ?   ?   ?   B . n 
B 1 483 GLY 483 483 ?   ?   ?   B . n 
B 1 484 GLU 484 484 ?   ?   ?   B . n 
B 1 485 LYS 485 485 ?   ?   ?   B . n 
B 1 486 ASN 486 486 ?   ?   ?   B . n 
B 1 487 HIS 487 487 ?   ?   ?   B . n 
B 1 488 ARG 488 488 ?   ?   ?   B . n 
B 1 489 GLU 489 489 ?   ?   ?   B . n 
B 1 490 ALA 490 490 ?   ?   ?   B . n 
B 1 491 LEU 491 491 ?   ?   ?   B . n 
B 1 492 ASN 492 492 ?   ?   ?   B . n 
B 1 493 HIS 493 493 ?   ?   ?   B . n 
B 1 494 ARG 494 494 ?   ?   ?   B . n 
B 1 495 PRO 495 495 ?   ?   ?   B . n 
B 1 496 THR 496 496 ?   ?   ?   B . n 
B 1 497 PHE 497 497 ?   ?   ?   B . n 
B 1 498 SER 498 498 ?   ?   ?   B . n 
B 1 499 LYS 499 499 ?   ?   ?   B . n 
B 1 500 GLN 500 500 ?   ?   ?   B . n 
B 1 501 VAL 501 501 ?   ?   ?   B . n 
B 1 502 SER 502 502 ?   ?   ?   B . n 
B 1 503 TRP 503 503 ?   ?   ?   B . n 
B 1 504 PRO 504 504 ?   ?   ?   B . n 
B 1 505 ALA 505 505 ?   ?   ?   B . n 
B 1 506 ARG 506 506 ?   ?   ?   B . n 
B 1 507 LEU 507 507 ?   ?   ?   B . n 
B 1 508 VAL 508 508 ?   ?   ?   B . n 
B 1 509 LEU 509 509 ?   ?   ?   B . n 
B 1 510 PRO 510 510 ?   ?   ?   B . n 
B 1 511 PRO 511 511 ?   ?   ?   B . n 
B 1 512 HIS 512 512 ?   ?   ?   B . n 
B 1 513 LEU 513 513 ?   ?   ?   B . n 
B 1 514 GLU 514 514 ?   ?   ?   B . n 
B 1 515 THR 515 515 ?   ?   ?   B . n 
B 1 516 THR 516 516 ?   ?   ?   B . n 
B 1 517 ASN 517 517 ?   ?   ?   B . n 
B 1 518 GLY 518 518 ?   ?   ?   B . n 
B 1 519 ALA 519 519 ?   ?   ?   B . n 
B 1 520 SER 520 520 ?   ?   ?   B . n 
B 1 521 PRO 521 521 ?   ?   ?   B . n 
B 1 522 LEU 522 522 ?   ?   ?   B . n 
B 1 523 VAL 523 523 ?   ?   ?   B . n 
B 1 524 GLU 524 524 ?   ?   ?   B . n 
B 1 525 THR 525 525 ?   ?   ?   B . n 
B 1 526 THR 526 526 ?   ?   ?   B . n 
B 1 527 LYS 527 527 527 LYS LYS B . n 
B 1 528 THR 528 528 528 THR THR B . n 
B 1 529 TYR 529 529 529 TYR TYR B . n 
B 1 530 GLU 530 530 530 GLU GLU B . n 
B 1 531 SER 531 531 531 SER SER B . n 
B 1 532 ALA 532 532 532 ALA ALA B . n 
B 1 533 SER 533 533 533 SER SER B . n 
B 1 534 ALA 534 534 534 ALA ALA B . n 
B 1 535 LEU 535 535 535 LEU LEU B . n 
B 1 536 SER 536 536 536 SER SER B . n 
B 1 537 LEU 537 537 537 LEU LEU B . n 
B 1 538 ALA 538 538 538 ALA ALA B . n 
B 1 539 THR 539 539 539 THR THR B . n 
B 1 540 PHE 540 540 540 PHE PHE B . n 
B 1 541 ALA 541 541 541 ALA ALA B . n 
B 1 542 SER 542 542 542 SER SER B . n 
B 1 543 LEU 543 543 543 LEU LEU B . n 
B 1 544 LEU 544 544 544 LEU LEU B . n 
B 1 545 ILE 545 545 545 ILE ILE B . n 
B 1 546 GLU 546 546 546 GLU GLU B . n 
B 1 547 PHE 547 547 547 PHE PHE B . n 
B 1 548 VAL 548 548 548 VAL VAL B . n 
B 1 549 ALA 549 549 549 ALA ALA B . n 
B 1 550 ARG 550 550 550 ARG ARG B . n 
B 1 551 LEU 551 551 551 LEU LEU B . n 
B 1 552 GLN 552 552 552 GLN GLN B . n 
B 1 553 ASN 553 553 553 ASN ASN B . n 
B 1 554 VAL 554 554 554 VAL VAL B . n 
B 1 555 VAL 555 555 555 VAL VAL B . n 
B 1 556 ASP 556 556 556 ASP ASP B . n 
B 1 557 ALA 557 557 557 ALA ALA B . n 
B 1 558 PHE 558 558 558 PHE PHE B . n 
B 1 559 LYS 559 559 559 LYS LYS B . n 
B 1 560 GLU 560 560 560 GLU GLU B . n 
B 1 561 LEU 561 561 561 LEU LEU B . n 
B 1 562 SER 562 562 562 SER SER B . n 
B 1 563 GLN 563 563 563 GLN GLN B . n 
B 1 564 LYS 564 564 564 LYS LYS B . n 
B 1 565 ALA 565 565 565 ALA ALA B . n 
B 1 566 ASN 566 566 566 ASN ASN B . n 
B 1 567 PHE 567 567 567 PHE PHE B . n 
B 1 568 LYS 568 568 568 LYS LYS B . n 
B 1 569 GLU 569 569 569 GLU GLU B . n 
B 1 570 PRO 570 570 570 PRO PRO B . n 
B 1 571 GLU 571 571 571 GLU GLU B . n 
B 1 572 ILE 572 572 ?   ?   ?   B . n 
B 1 573 VAL 573 573 ?   ?   ?   B . n 
B 1 574 THR 574 574 ?   ?   ?   B . n 
B 1 575 THR 575 575 ?   ?   ?   B . n 
B 1 576 GLY 576 576 ?   ?   ?   B . n 
B 1 577 THR 577 577 ?   ?   ?   B . n 
B 1 578 ASP 578 578 ?   ?   ?   B . n 
B 1 579 VAL 579 579 ?   ?   ?   B . n 
B 1 580 GLU 580 580 ?   ?   ?   B . n 
B 1 581 PHE 581 581 ?   ?   ?   B . n 
B 1 582 SER 582 582 ?   ?   ?   B . n 
B 1 583 GLY 583 583 ?   ?   ?   B . n 
B 1 584 GLU 584 584 ?   ?   ?   B . n 
B 1 585 ARG 585 585 ?   ?   ?   B . n 
B 1 586 VAL 586 586 ?   ?   ?   B . n 
B 1 587 GLY 587 587 ?   ?   ?   B . n 
B 1 588 LEU 588 588 ?   ?   ?   B . n 
B 1 589 GLY 589 589 ?   ?   ?   B . n 
B 1 590 GLN 590 590 ?   ?   ?   B . n 
B 1 591 LYS 591 591 ?   ?   ?   B . n 
B 1 592 ILE 592 592 ?   ?   ?   B . n 
B 1 593 ARG 593 593 ?   ?   ?   B . n 
B 1 594 ARG 594 594 ?   ?   ?   B . n 
B 1 595 CYS 595 595 ?   ?   ?   B . n 
B 1 596 PHE 596 596 ?   ?   ?   B . n 
B 1 597 GLY 597 597 ?   ?   ?   B . n 
B 1 598 MET 598 598 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        3PH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   3PH 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 3PH 1 601 601 3PH 3PH A . 
D 2 3PH 1 601 602 3PH 3PH B . 
E 3 HOH 1 701 1   HOH HOH A . 
F 3 HOH 1 701 2   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                     8ZTN 
_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                         8ZTN 
_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                   8ZTN 
_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                                 8ZTN 
_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                     8ZTN 
_struct.title                        'AtALMT9 with LMNG (trans2 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        8ZTN 
_struct_keywords.text            'Plant, Stomata, Vacuole, ALMT, Ion channel, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ALMT9_ARATH 
_struct_ref.pdbx_db_accession          Q9LS46 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAAKQGSFRHGILEKRERLLSNNGFSDFRFTDIESNDLLENENCGRRTRLCCCCSCGNLSEKISGVYDDAKDVARKAWEM
GVSDPRKIVFSAKIGLALTIVALLIFYQEPNPDLSRYSVWAILTVVVVFEFTIGATLSKGFNRALGTLSAGGLALGMAEL
STLFGDWEEIFCTLSIFCIGFLATFMKLYPSMKAYEYGFRVFLLTYCYILISGFRTGQFIEVAISRFLLIALGAGVSLGV
NMFIYPIWAGEDLHNLVVKNFMNVATSLEGCVNGYLRCLEYERIPSKILTYQASEDPVYKGYRSAVESTSQEESLMSFAI
WEPPHGPYKSFNYPWKNYVKLSGALKHCAFTVMALHGCILSEIQAPEERRQVFRQELQRVGVEGAKLLRELGEKVKKMEK
LGPVDLLFEVHLAAEELQHKIDKKSYLLVNSECWEIGNRATKESEPQELLSLEDSDPPENHAPPIYAFKSLSEAVLEIPP
SWGEKNHREALNHRPTFSKQVSWPARLVLPPHLETTNGASPLVETTKTYESASALSLATFASLLIEFVARLQNVVDAFKE
LSQKANFKEPEIVTTGTDVEFSGERVGLGQKIRRCFGM
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZTN A 1 ? 598 ? Q9LS46 1 ? 598 ? 1 598 
2 1 8ZTN B 1 ? 598 ? Q9LS46 1 ? 598 ? 1 598 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 77  ? ASP A 84  ? ALA A 77  ASP A 84  1 ? 8  
HELX_P HELX_P2  AA2 PRO A 85  ? TYR A 107 ? PRO A 85  TYR A 107 1 ? 23 
HELX_P HELX_P3  AA3 ASN A 111 ? SER A 118 ? ASN A 111 SER A 118 1 ? 8  
HELX_P HELX_P4  AA4 ALA A 121 ? PHE A 129 ? ALA A 121 PHE A 129 1 ? 9  
HELX_P HELX_P5  AA5 THR A 132 ? SER A 161 ? THR A 132 SER A 161 1 ? 30 
HELX_P HELX_P6  AA6 THR A 162 ? PHE A 164 ? THR A 162 PHE A 164 5 ? 3  
HELX_P HELX_P7  AA7 TRP A 167 ? MET A 186 ? TRP A 167 MET A 186 1 ? 20 
HELX_P HELX_P8  AA8 TYR A 189 ? LYS A 193 ? TYR A 189 LYS A 193 5 ? 5  
HELX_P HELX_P9  AA9 TYR A 195 ? SER A 212 ? TYR A 195 SER A 212 1 ? 18 
HELX_P HELX_P10 AB1 ILE A 220 ? ILE A 244 ? ILE A 220 ILE A 244 1 ? 25 
HELX_P HELX_P11 AB2 ALA A 249 ? ARG A 277 ? ALA A 249 ARG A 277 1 ? 29 
HELX_P HELX_P12 AB3 TYR A 299 ? GLU A 307 ? TYR A 299 GLU A 307 1 ? 9  
HELX_P HELX_P13 AB4 SER A 308 ? ALA A 319 ? SER A 308 ALA A 319 1 ? 12 
HELX_P HELX_P14 AB5 TRP A 335 ? LEU A 360 ? TRP A 335 LEU A 360 1 ? 26 
HELX_P HELX_P15 AB6 PRO A 366 ? GLN A 371 ? PRO A 366 GLN A 371 1 ? 6  
HELX_P HELX_P16 AB7 PHE A 373 ? MET A 398 ? PHE A 373 MET A 398 1 ? 26 
HELX_P HELX_P17 AB8 LEU A 407 ? LYS A 424 ? LEU A 407 LYS A 424 1 ? 18 
HELX_P HELX_P18 AB9 SER A 425 ? LEU A 428 ? SER A 425 LEU A 428 5 ? 4  
HELX_P HELX_P19 AC1 ASN A 430 ? TRP A 434 ? ASN A 430 TRP A 434 5 ? 5  
HELX_P HELX_P20 AC2 THR A 528 ? ALA A 565 ? THR A 528 ALA A 565 1 ? 38 
HELX_P HELX_P21 AC3 TRP B 78  ? ASP B 84  ? TRP B 78  ASP B 84  1 ? 7  
HELX_P HELX_P22 AC4 PRO B 85  ? TYR B 107 ? PRO B 85  TYR B 107 1 ? 23 
HELX_P HELX_P23 AC5 ASN B 111 ? SER B 118 ? ASN B 111 SER B 118 1 ? 8  
HELX_P HELX_P24 AC6 ALA B 121 ? PHE B 129 ? ALA B 121 PHE B 129 1 ? 9  
HELX_P HELX_P25 AC7 THR B 132 ? SER B 161 ? THR B 132 SER B 161 1 ? 30 
HELX_P HELX_P26 AC8 THR B 162 ? PHE B 164 ? THR B 162 PHE B 164 5 ? 3  
HELX_P HELX_P27 AC9 TRP B 167 ? MET B 186 ? TRP B 167 MET B 186 1 ? 20 
HELX_P HELX_P28 AD1 TYR B 189 ? LYS B 193 ? TYR B 189 LYS B 193 5 ? 5  
HELX_P HELX_P29 AD2 TYR B 195 ? PHE B 214 ? TYR B 195 PHE B 214 1 ? 20 
HELX_P HELX_P30 AD3 ARG B 215 ? GLN B 218 ? ARG B 215 GLN B 218 5 ? 4  
HELX_P HELX_P31 AD4 ILE B 220 ? ILE B 244 ? ILE B 220 ILE B 244 1 ? 25 
HELX_P HELX_P32 AD5 ALA B 249 ? ARG B 277 ? ALA B 249 ARG B 277 1 ? 29 
HELX_P HELX_P33 AD6 TYR B 299 ? GLU B 307 ? TYR B 299 GLU B 307 1 ? 9  
HELX_P HELX_P34 AD7 SER B 308 ? ALA B 319 ? SER B 308 ALA B 319 1 ? 12 
HELX_P HELX_P35 AD8 TRP B 335 ? LEU B 360 ? TRP B 335 LEU B 360 1 ? 26 
HELX_P HELX_P36 AD9 PRO B 366 ? GLN B 371 ? PRO B 366 GLN B 371 1 ? 6  
HELX_P HELX_P37 AE1 GLN B 375 ? MET B 398 ? GLN B 375 MET B 398 1 ? 24 
HELX_P HELX_P38 AE2 LEU B 407 ? LYS B 424 ? LEU B 407 LYS B 424 1 ? 18 
HELX_P HELX_P39 AE3 SER B 425 ? LEU B 428 ? SER B 425 LEU B 428 5 ? 4  
HELX_P HELX_P40 AE4 ASN B 430 ? TRP B 434 ? ASN B 430 TRP B 434 5 ? 5  
HELX_P HELX_P41 AE5 THR B 528 ? ALA B 565 ? THR B 528 ALA B 565 1 ? 38 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   8ZTN 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 216 ? ? 80.38   -9.55 
2 1 ARG A 226 ? ? -66.23  1.89  
3 1 TYR B 107 ? ? -102.73 62.96 
4 1 PRO B 334 ? ? -69.13  74.73 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8ZTN 
_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                    8ZTN 
_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                  2.77 
_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               40689 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          1 
_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                        8ZTN 
_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              8ZTN 
_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                8ZTN 
_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              8ZTN 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ALA 2   ? A ALA 2   
3   1 Y 1 A ALA 3   ? A ALA 3   
4   1 Y 1 A LYS 4   ? A LYS 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A GLY 6   ? A GLY 6   
7   1 Y 1 A SER 7   ? A SER 7   
8   1 Y 1 A PHE 8   ? A PHE 8   
9   1 Y 1 A ARG 9   ? A ARG 9   
10  1 Y 1 A HIS 10  ? A HIS 10  
11  1 Y 1 A GLY 11  ? A GLY 11  
12  1 Y 1 A ILE 12  ? A ILE 12  
13  1 Y 1 A LEU 13  ? A LEU 13  
14  1 Y 1 A GLU 14  ? A GLU 14  
15  1 Y 1 A LYS 15  ? A LYS 15  
16  1 Y 1 A ARG 16  ? A ARG 16  
17  1 Y 1 A GLU 17  ? A GLU 17  
18  1 Y 1 A ARG 18  ? A ARG 18  
19  1 Y 1 A LEU 19  ? A LEU 19  
20  1 Y 1 A LEU 20  ? A LEU 20  
21  1 Y 1 A SER 21  ? A SER 21  
22  1 Y 1 A ASN 22  ? A ASN 22  
23  1 Y 1 A ASN 23  ? A ASN 23  
24  1 Y 1 A GLY 24  ? A GLY 24  
25  1 Y 1 A PHE 25  ? A PHE 25  
26  1 Y 1 A SER 26  ? A SER 26  
27  1 Y 1 A ASP 27  ? A ASP 27  
28  1 Y 1 A PHE 28  ? A PHE 28  
29  1 Y 1 A ARG 29  ? A ARG 29  
30  1 Y 1 A PHE 30  ? A PHE 30  
31  1 Y 1 A THR 31  ? A THR 31  
32  1 Y 1 A ASP 32  ? A ASP 32  
33  1 Y 1 A ILE 33  ? A ILE 33  
34  1 Y 1 A GLU 34  ? A GLU 34  
35  1 Y 1 A SER 35  ? A SER 35  
36  1 Y 1 A ASN 36  ? A ASN 36  
37  1 Y 1 A ASP 37  ? A ASP 37  
38  1 Y 1 A LEU 38  ? A LEU 38  
39  1 Y 1 A LEU 39  ? A LEU 39  
40  1 Y 1 A GLU 40  ? A GLU 40  
41  1 Y 1 A ASN 41  ? A ASN 41  
42  1 Y 1 A GLU 42  ? A GLU 42  
43  1 Y 1 A ASN 43  ? A ASN 43  
44  1 Y 1 A CYS 44  ? A CYS 44  
45  1 Y 1 A GLY 45  ? A GLY 45  
46  1 Y 1 A ARG 46  ? A ARG 46  
47  1 Y 1 A ARG 47  ? A ARG 47  
48  1 Y 1 A THR 48  ? A THR 48  
49  1 Y 1 A ARG 49  ? A ARG 49  
50  1 Y 1 A LEU 50  ? A LEU 50  
51  1 Y 1 A CYS 51  ? A CYS 51  
52  1 Y 1 A CYS 52  ? A CYS 52  
53  1 Y 1 A CYS 53  ? A CYS 53  
54  1 Y 1 A CYS 54  ? A CYS 54  
55  1 Y 1 A SER 55  ? A SER 55  
56  1 Y 1 A CYS 56  ? A CYS 56  
57  1 Y 1 A GLY 57  ? A GLY 57  
58  1 Y 1 A ASN 58  ? A ASN 58  
59  1 Y 1 A LEU 59  ? A LEU 59  
60  1 Y 1 A SER 60  ? A SER 60  
61  1 Y 1 A GLU 61  ? A GLU 61  
62  1 Y 1 A LYS 62  ? A LYS 62  
63  1 Y 1 A ILE 63  ? A ILE 63  
64  1 Y 1 A SER 64  ? A SER 64  
65  1 Y 1 A GLY 65  ? A GLY 65  
66  1 Y 1 A VAL 66  ? A VAL 66  
67  1 Y 1 A TYR 67  ? A TYR 67  
68  1 Y 1 A ASP 68  ? A ASP 68  
69  1 Y 1 A ASP 69  ? A ASP 69  
70  1 Y 1 A ALA 70  ? A ALA 70  
71  1 Y 1 A LYS 71  ? A LYS 71  
72  1 Y 1 A ASP 72  ? A ASP 72  
73  1 Y 1 A VAL 73  ? A VAL 73  
74  1 Y 1 A ALA 74  ? A ALA 74  
75  1 Y 1 A ARG 75  ? A ARG 75  
76  1 Y 1 A LYS 76  ? A LYS 76  
77  1 Y 1 A LEU 279 ? A LEU 279 
78  1 Y 1 A GLU 280 ? A GLU 280 
79  1 Y 1 A TYR 281 ? A TYR 281 
80  1 Y 1 A GLU 282 ? A GLU 282 
81  1 Y 1 A ARG 283 ? A ARG 283 
82  1 Y 1 A ILE 284 ? A ILE 284 
83  1 Y 1 A PRO 285 ? A PRO 285 
84  1 Y 1 A SER 286 ? A SER 286 
85  1 Y 1 A LYS 287 ? A LYS 287 
86  1 Y 1 A ILE 288 ? A ILE 288 
87  1 Y 1 A LEU 289 ? A LEU 289 
88  1 Y 1 A THR 290 ? A THR 290 
89  1 Y 1 A TYR 291 ? A TYR 291 
90  1 Y 1 A GLN 292 ? A GLN 292 
91  1 Y 1 A ALA 293 ? A ALA 293 
92  1 Y 1 A SER 294 ? A SER 294 
93  1 Y 1 A GLU 295 ? A GLU 295 
94  1 Y 1 A ASP 296 ? A ASP 296 
95  1 Y 1 A PRO 297 ? A PRO 297 
96  1 Y 1 A ILE 436 ? A ILE 436 
97  1 Y 1 A GLY 437 ? A GLY 437 
98  1 Y 1 A ASN 438 ? A ASN 438 
99  1 Y 1 A ARG 439 ? A ARG 439 
100 1 Y 1 A ALA 440 ? A ALA 440 
101 1 Y 1 A THR 441 ? A THR 441 
102 1 Y 1 A LYS 442 ? A LYS 442 
103 1 Y 1 A GLU 443 ? A GLU 443 
104 1 Y 1 A SER 444 ? A SER 444 
105 1 Y 1 A GLU 445 ? A GLU 445 
106 1 Y 1 A PRO 446 ? A PRO 446 
107 1 Y 1 A GLN 447 ? A GLN 447 
108 1 Y 1 A GLU 448 ? A GLU 448 
109 1 Y 1 A LEU 449 ? A LEU 449 
110 1 Y 1 A LEU 450 ? A LEU 450 
111 1 Y 1 A SER 451 ? A SER 451 
112 1 Y 1 A LEU 452 ? A LEU 452 
113 1 Y 1 A GLU 453 ? A GLU 453 
114 1 Y 1 A ASP 454 ? A ASP 454 
115 1 Y 1 A SER 455 ? A SER 455 
116 1 Y 1 A ASP 456 ? A ASP 456 
117 1 Y 1 A PRO 457 ? A PRO 457 
118 1 Y 1 A PRO 458 ? A PRO 458 
119 1 Y 1 A GLU 459 ? A GLU 459 
120 1 Y 1 A ASN 460 ? A ASN 460 
121 1 Y 1 A HIS 461 ? A HIS 461 
122 1 Y 1 A ALA 462 ? A ALA 462 
123 1 Y 1 A PRO 463 ? A PRO 463 
124 1 Y 1 A PRO 464 ? A PRO 464 
125 1 Y 1 A ILE 465 ? A ILE 465 
126 1 Y 1 A TYR 466 ? A TYR 466 
127 1 Y 1 A ALA 467 ? A ALA 467 
128 1 Y 1 A PHE 468 ? A PHE 468 
129 1 Y 1 A LYS 469 ? A LYS 469 
130 1 Y 1 A SER 470 ? A SER 470 
131 1 Y 1 A LEU 471 ? A LEU 471 
132 1 Y 1 A SER 472 ? A SER 472 
133 1 Y 1 A GLU 473 ? A GLU 473 
134 1 Y 1 A ALA 474 ? A ALA 474 
135 1 Y 1 A VAL 475 ? A VAL 475 
136 1 Y 1 A LEU 476 ? A LEU 476 
137 1 Y 1 A GLU 477 ? A GLU 477 
138 1 Y 1 A ILE 478 ? A ILE 478 
139 1 Y 1 A PRO 479 ? A PRO 479 
140 1 Y 1 A PRO 480 ? A PRO 480 
141 1 Y 1 A SER 481 ? A SER 481 
142 1 Y 1 A TRP 482 ? A TRP 482 
143 1 Y 1 A GLY 483 ? A GLY 483 
144 1 Y 1 A GLU 484 ? A GLU 484 
145 1 Y 1 A LYS 485 ? A LYS 485 
146 1 Y 1 A ASN 486 ? A ASN 486 
147 1 Y 1 A HIS 487 ? A HIS 487 
148 1 Y 1 A ARG 488 ? A ARG 488 
149 1 Y 1 A GLU 489 ? A GLU 489 
150 1 Y 1 A ALA 490 ? A ALA 490 
151 1 Y 1 A LEU 491 ? A LEU 491 
152 1 Y 1 A ASN 492 ? A ASN 492 
153 1 Y 1 A HIS 493 ? A HIS 493 
154 1 Y 1 A ARG 494 ? A ARG 494 
155 1 Y 1 A PRO 495 ? A PRO 495 
156 1 Y 1 A THR 496 ? A THR 496 
157 1 Y 1 A PHE 497 ? A PHE 497 
158 1 Y 1 A SER 498 ? A SER 498 
159 1 Y 1 A LYS 499 ? A LYS 499 
160 1 Y 1 A GLN 500 ? A GLN 500 
161 1 Y 1 A VAL 501 ? A VAL 501 
162 1 Y 1 A SER 502 ? A SER 502 
163 1 Y 1 A TRP 503 ? A TRP 503 
164 1 Y 1 A PRO 504 ? A PRO 504 
165 1 Y 1 A ALA 505 ? A ALA 505 
166 1 Y 1 A ARG 506 ? A ARG 506 
167 1 Y 1 A LEU 507 ? A LEU 507 
168 1 Y 1 A VAL 508 ? A VAL 508 
169 1 Y 1 A LEU 509 ? A LEU 509 
170 1 Y 1 A PRO 510 ? A PRO 510 
171 1 Y 1 A PRO 511 ? A PRO 511 
172 1 Y 1 A HIS 512 ? A HIS 512 
173 1 Y 1 A LEU 513 ? A LEU 513 
174 1 Y 1 A GLU 514 ? A GLU 514 
175 1 Y 1 A THR 515 ? A THR 515 
176 1 Y 1 A THR 516 ? A THR 516 
177 1 Y 1 A ASN 517 ? A ASN 517 
178 1 Y 1 A GLY 518 ? A GLY 518 
179 1 Y 1 A ALA 519 ? A ALA 519 
180 1 Y 1 A SER 520 ? A SER 520 
181 1 Y 1 A PRO 521 ? A PRO 521 
182 1 Y 1 A LEU 522 ? A LEU 522 
183 1 Y 1 A VAL 523 ? A VAL 523 
184 1 Y 1 A GLU 524 ? A GLU 524 
185 1 Y 1 A THR 525 ? A THR 525 
186 1 Y 1 A THR 526 ? A THR 526 
187 1 Y 1 A ILE 572 ? A ILE 572 
188 1 Y 1 A VAL 573 ? A VAL 573 
189 1 Y 1 A THR 574 ? A THR 574 
190 1 Y 1 A THR 575 ? A THR 575 
191 1 Y 1 A GLY 576 ? A GLY 576 
192 1 Y 1 A THR 577 ? A THR 577 
193 1 Y 1 A ASP 578 ? A ASP 578 
194 1 Y 1 A VAL 579 ? A VAL 579 
195 1 Y 1 A GLU 580 ? A GLU 580 
196 1 Y 1 A PHE 581 ? A PHE 581 
197 1 Y 1 A SER 582 ? A SER 582 
198 1 Y 1 A GLY 583 ? A GLY 583 
199 1 Y 1 A GLU 584 ? A GLU 584 
200 1 Y 1 A ARG 585 ? A ARG 585 
201 1 Y 1 A VAL 586 ? A VAL 586 
202 1 Y 1 A GLY 587 ? A GLY 587 
203 1 Y 1 A LEU 588 ? A LEU 588 
204 1 Y 1 A GLY 589 ? A GLY 589 
205 1 Y 1 A GLN 590 ? A GLN 590 
206 1 Y 1 A LYS 591 ? A LYS 591 
207 1 Y 1 A ILE 592 ? A ILE 592 
208 1 Y 1 A ARG 593 ? A ARG 593 
209 1 Y 1 A ARG 594 ? A ARG 594 
210 1 Y 1 A CYS 595 ? A CYS 595 
211 1 Y 1 A PHE 596 ? A PHE 596 
212 1 Y 1 A GLY 597 ? A GLY 597 
213 1 Y 1 A MET 598 ? A MET 598 
214 1 Y 1 B MET 1   ? B MET 1   
215 1 Y 1 B ALA 2   ? B ALA 2   
216 1 Y 1 B ALA 3   ? B ALA 3   
217 1 Y 1 B LYS 4   ? B LYS 4   
218 1 Y 1 B GLN 5   ? B GLN 5   
219 1 Y 1 B GLY 6   ? B GLY 6   
220 1 Y 1 B SER 7   ? B SER 7   
221 1 Y 1 B PHE 8   ? B PHE 8   
222 1 Y 1 B ARG 9   ? B ARG 9   
223 1 Y 1 B HIS 10  ? B HIS 10  
224 1 Y 1 B GLY 11  ? B GLY 11  
225 1 Y 1 B ILE 12  ? B ILE 12  
226 1 Y 1 B LEU 13  ? B LEU 13  
227 1 Y 1 B GLU 14  ? B GLU 14  
228 1 Y 1 B LYS 15  ? B LYS 15  
229 1 Y 1 B ARG 16  ? B ARG 16  
230 1 Y 1 B GLU 17  ? B GLU 17  
231 1 Y 1 B ARG 18  ? B ARG 18  
232 1 Y 1 B LEU 19  ? B LEU 19  
233 1 Y 1 B LEU 20  ? B LEU 20  
234 1 Y 1 B SER 21  ? B SER 21  
235 1 Y 1 B ASN 22  ? B ASN 22  
236 1 Y 1 B ASN 23  ? B ASN 23  
237 1 Y 1 B GLY 24  ? B GLY 24  
238 1 Y 1 B PHE 25  ? B PHE 25  
239 1 Y 1 B SER 26  ? B SER 26  
240 1 Y 1 B ASP 27  ? B ASP 27  
241 1 Y 1 B PHE 28  ? B PHE 28  
242 1 Y 1 B ARG 29  ? B ARG 29  
243 1 Y 1 B PHE 30  ? B PHE 30  
244 1 Y 1 B THR 31  ? B THR 31  
245 1 Y 1 B ASP 32  ? B ASP 32  
246 1 Y 1 B ILE 33  ? B ILE 33  
247 1 Y 1 B GLU 34  ? B GLU 34  
248 1 Y 1 B SER 35  ? B SER 35  
249 1 Y 1 B ASN 36  ? B ASN 36  
250 1 Y 1 B ASP 37  ? B ASP 37  
251 1 Y 1 B LEU 38  ? B LEU 38  
252 1 Y 1 B LEU 39  ? B LEU 39  
253 1 Y 1 B GLU 40  ? B GLU 40  
254 1 Y 1 B ASN 41  ? B ASN 41  
255 1 Y 1 B GLU 42  ? B GLU 42  
256 1 Y 1 B ASN 43  ? B ASN 43  
257 1 Y 1 B CYS 44  ? B CYS 44  
258 1 Y 1 B GLY 45  ? B GLY 45  
259 1 Y 1 B ARG 46  ? B ARG 46  
260 1 Y 1 B ARG 47  ? B ARG 47  
261 1 Y 1 B THR 48  ? B THR 48  
262 1 Y 1 B ARG 49  ? B ARG 49  
263 1 Y 1 B LEU 50  ? B LEU 50  
264 1 Y 1 B CYS 51  ? B CYS 51  
265 1 Y 1 B CYS 52  ? B CYS 52  
266 1 Y 1 B CYS 53  ? B CYS 53  
267 1 Y 1 B CYS 54  ? B CYS 54  
268 1 Y 1 B SER 55  ? B SER 55  
269 1 Y 1 B CYS 56  ? B CYS 56  
270 1 Y 1 B GLY 57  ? B GLY 57  
271 1 Y 1 B ASN 58  ? B ASN 58  
272 1 Y 1 B LEU 59  ? B LEU 59  
273 1 Y 1 B SER 60  ? B SER 60  
274 1 Y 1 B GLU 61  ? B GLU 61  
275 1 Y 1 B LYS 62  ? B LYS 62  
276 1 Y 1 B ILE 63  ? B ILE 63  
277 1 Y 1 B SER 64  ? B SER 64  
278 1 Y 1 B GLY 65  ? B GLY 65  
279 1 Y 1 B VAL 66  ? B VAL 66  
280 1 Y 1 B TYR 67  ? B TYR 67  
281 1 Y 1 B ASP 68  ? B ASP 68  
282 1 Y 1 B ASP 69  ? B ASP 69  
283 1 Y 1 B ALA 70  ? B ALA 70  
284 1 Y 1 B LYS 71  ? B LYS 71  
285 1 Y 1 B ASP 72  ? B ASP 72  
286 1 Y 1 B VAL 73  ? B VAL 73  
287 1 Y 1 B ALA 74  ? B ALA 74  
288 1 Y 1 B ARG 75  ? B ARG 75  
289 1 Y 1 B LYS 76  ? B LYS 76  
290 1 Y 1 B LEU 279 ? B LEU 279 
291 1 Y 1 B GLU 280 ? B GLU 280 
292 1 Y 1 B TYR 281 ? B TYR 281 
293 1 Y 1 B GLU 282 ? B GLU 282 
294 1 Y 1 B ARG 283 ? B ARG 283 
295 1 Y 1 B ILE 284 ? B ILE 284 
296 1 Y 1 B PRO 285 ? B PRO 285 
297 1 Y 1 B SER 286 ? B SER 286 
298 1 Y 1 B LYS 287 ? B LYS 287 
299 1 Y 1 B ILE 288 ? B ILE 288 
300 1 Y 1 B LEU 289 ? B LEU 289 
301 1 Y 1 B THR 290 ? B THR 290 
302 1 Y 1 B TYR 291 ? B TYR 291 
303 1 Y 1 B GLN 292 ? B GLN 292 
304 1 Y 1 B ALA 293 ? B ALA 293 
305 1 Y 1 B SER 294 ? B SER 294 
306 1 Y 1 B GLU 295 ? B GLU 295 
307 1 Y 1 B ASP 296 ? B ASP 296 
308 1 Y 1 B PRO 297 ? B PRO 297 
309 1 Y 1 B ILE 436 ? B ILE 436 
310 1 Y 1 B GLY 437 ? B GLY 437 
311 1 Y 1 B ASN 438 ? B ASN 438 
312 1 Y 1 B ARG 439 ? B ARG 439 
313 1 Y 1 B ALA 440 ? B ALA 440 
314 1 Y 1 B THR 441 ? B THR 441 
315 1 Y 1 B LYS 442 ? B LYS 442 
316 1 Y 1 B GLU 443 ? B GLU 443 
317 1 Y 1 B SER 444 ? B SER 444 
318 1 Y 1 B GLU 445 ? B GLU 445 
319 1 Y 1 B PRO 446 ? B PRO 446 
320 1 Y 1 B GLN 447 ? B GLN 447 
321 1 Y 1 B GLU 448 ? B GLU 448 
322 1 Y 1 B LEU 449 ? B LEU 449 
323 1 Y 1 B LEU 450 ? B LEU 450 
324 1 Y 1 B SER 451 ? B SER 451 
325 1 Y 1 B LEU 452 ? B LEU 452 
326 1 Y 1 B GLU 453 ? B GLU 453 
327 1 Y 1 B ASP 454 ? B ASP 454 
328 1 Y 1 B SER 455 ? B SER 455 
329 1 Y 1 B ASP 456 ? B ASP 456 
330 1 Y 1 B PRO 457 ? B PRO 457 
331 1 Y 1 B PRO 458 ? B PRO 458 
332 1 Y 1 B GLU 459 ? B GLU 459 
333 1 Y 1 B ASN 460 ? B ASN 460 
334 1 Y 1 B HIS 461 ? B HIS 461 
335 1 Y 1 B ALA 462 ? B ALA 462 
336 1 Y 1 B PRO 463 ? B PRO 463 
337 1 Y 1 B PRO 464 ? B PRO 464 
338 1 Y 1 B ILE 465 ? B ILE 465 
339 1 Y 1 B TYR 466 ? B TYR 466 
340 1 Y 1 B ALA 467 ? B ALA 467 
341 1 Y 1 B PHE 468 ? B PHE 468 
342 1 Y 1 B LYS 469 ? B LYS 469 
343 1 Y 1 B SER 470 ? B SER 470 
344 1 Y 1 B LEU 471 ? B LEU 471 
345 1 Y 1 B SER 472 ? B SER 472 
346 1 Y 1 B GLU 473 ? B GLU 473 
347 1 Y 1 B ALA 474 ? B ALA 474 
348 1 Y 1 B VAL 475 ? B VAL 475 
349 1 Y 1 B LEU 476 ? B LEU 476 
350 1 Y 1 B GLU 477 ? B GLU 477 
351 1 Y 1 B ILE 478 ? B ILE 478 
352 1 Y 1 B PRO 479 ? B PRO 479 
353 1 Y 1 B PRO 480 ? B PRO 480 
354 1 Y 1 B SER 481 ? B SER 481 
355 1 Y 1 B TRP 482 ? B TRP 482 
356 1 Y 1 B GLY 483 ? B GLY 483 
357 1 Y 1 B GLU 484 ? B GLU 484 
358 1 Y 1 B LYS 485 ? B LYS 485 
359 1 Y 1 B ASN 486 ? B ASN 486 
360 1 Y 1 B HIS 487 ? B HIS 487 
361 1 Y 1 B ARG 488 ? B ARG 488 
362 1 Y 1 B GLU 489 ? B GLU 489 
363 1 Y 1 B ALA 490 ? B ALA 490 
364 1 Y 1 B LEU 491 ? B LEU 491 
365 1 Y 1 B ASN 492 ? B ASN 492 
366 1 Y 1 B HIS 493 ? B HIS 493 
367 1 Y 1 B ARG 494 ? B ARG 494 
368 1 Y 1 B PRO 495 ? B PRO 495 
369 1 Y 1 B THR 496 ? B THR 496 
370 1 Y 1 B PHE 497 ? B PHE 497 
371 1 Y 1 B SER 498 ? B SER 498 
372 1 Y 1 B LYS 499 ? B LYS 499 
373 1 Y 1 B GLN 500 ? B GLN 500 
374 1 Y 1 B VAL 501 ? B VAL 501 
375 1 Y 1 B SER 502 ? B SER 502 
376 1 Y 1 B TRP 503 ? B TRP 503 
377 1 Y 1 B PRO 504 ? B PRO 504 
378 1 Y 1 B ALA 505 ? B ALA 505 
379 1 Y 1 B ARG 506 ? B ARG 506 
380 1 Y 1 B LEU 507 ? B LEU 507 
381 1 Y 1 B VAL 508 ? B VAL 508 
382 1 Y 1 B LEU 509 ? B LEU 509 
383 1 Y 1 B PRO 510 ? B PRO 510 
384 1 Y 1 B PRO 511 ? B PRO 511 
385 1 Y 1 B HIS 512 ? B HIS 512 
386 1 Y 1 B LEU 513 ? B LEU 513 
387 1 Y 1 B GLU 514 ? B GLU 514 
388 1 Y 1 B THR 515 ? B THR 515 
389 1 Y 1 B THR 516 ? B THR 516 
390 1 Y 1 B ASN 517 ? B ASN 517 
391 1 Y 1 B GLY 518 ? B GLY 518 
392 1 Y 1 B ALA 519 ? B ALA 519 
393 1 Y 1 B SER 520 ? B SER 520 
394 1 Y 1 B PRO 521 ? B PRO 521 
395 1 Y 1 B LEU 522 ? B LEU 522 
396 1 Y 1 B VAL 523 ? B VAL 523 
397 1 Y 1 B GLU 524 ? B GLU 524 
398 1 Y 1 B THR 525 ? B THR 525 
399 1 Y 1 B THR 526 ? B THR 526 
400 1 Y 1 B ILE 572 ? B ILE 572 
401 1 Y 1 B VAL 573 ? B VAL 573 
402 1 Y 1 B THR 574 ? B THR 574 
403 1 Y 1 B THR 575 ? B THR 575 
404 1 Y 1 B GLY 576 ? B GLY 576 
405 1 Y 1 B THR 577 ? B THR 577 
406 1 Y 1 B ASP 578 ? B ASP 578 
407 1 Y 1 B VAL 579 ? B VAL 579 
408 1 Y 1 B GLU 580 ? B GLU 580 
409 1 Y 1 B PHE 581 ? B PHE 581 
410 1 Y 1 B SER 582 ? B SER 582 
411 1 Y 1 B GLY 583 ? B GLY 583 
412 1 Y 1 B GLU 584 ? B GLU 584 
413 1 Y 1 B ARG 585 ? B ARG 585 
414 1 Y 1 B VAL 586 ? B VAL 586 
415 1 Y 1 B GLY 587 ? B GLY 587 
416 1 Y 1 B LEU 588 ? B LEU 588 
417 1 Y 1 B GLY 589 ? B GLY 589 
418 1 Y 1 B GLN 590 ? B GLN 590 
419 1 Y 1 B LYS 591 ? B LYS 591 
420 1 Y 1 B ILE 592 ? B ILE 592 
421 1 Y 1 B ARG 593 ? B ARG 593 
422 1 Y 1 B ARG 594 ? B ARG 594 
423 1 Y 1 B CYS 595 ? B CYS 595 
424 1 Y 1 B PHE 596 ? B PHE 596 
425 1 Y 1 B GLY 597 ? B GLY 597 
426 1 Y 1 B MET 598 ? B MET 598 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
3PH O13  O N N 1   
3PH P    P N N 2   
3PH O14  O N N 3   
3PH O12  O N N 4   
3PH O11  O N N 5   
3PH C1   C N N 6   
3PH C2   C N R 7   
3PH O21  O N N 8   
3PH C21  C N N 9   
3PH O22  O N N 10  
3PH C22  C N N 11  
3PH C23  C N N 12  
3PH C24  C N N 13  
3PH C25  C N N 14  
3PH C26  C N N 15  
3PH C27  C N N 16  
3PH C28  C N N 17  
3PH C29  C N N 18  
3PH C2A  C N N 19  
3PH C2B  C N N 20  
3PH C2C  C N N 21  
3PH C2D  C N N 22  
3PH C2E  C N N 23  
3PH C2F  C N N 24  
3PH C2G  C N N 25  
3PH C2H  C N N 26  
3PH C2I  C N N 27  
3PH C3   C N N 28  
3PH O31  O N N 29  
3PH C31  C N N 30  
3PH O32  O N N 31  
3PH C32  C N N 32  
3PH C33  C N N 33  
3PH C34  C N N 34  
3PH C35  C N N 35  
3PH C36  C N N 36  
3PH C37  C N N 37  
3PH C38  C N N 38  
3PH C39  C N N 39  
3PH C3A  C N N 40  
3PH C3B  C N N 41  
3PH C3C  C N N 42  
3PH C3D  C N N 43  
3PH C3E  C N N 44  
3PH C3F  C N N 45  
3PH C3G  C N N 46  
3PH C3H  C N N 47  
3PH C3I  C N N 48  
3PH H13  H N N 49  
3PH H11  H N N 50  
3PH H12  H N N 51  
3PH H2   H N N 52  
3PH H221 H N N 53  
3PH H222 H N N 54  
3PH H231 H N N 55  
3PH H232 H N N 56  
3PH H241 H N N 57  
3PH H242 H N N 58  
3PH H251 H N N 59  
3PH H252 H N N 60  
3PH H261 H N N 61  
3PH H262 H N N 62  
3PH H271 H N N 63  
3PH H272 H N N 64  
3PH H281 H N N 65  
3PH H282 H N N 66  
3PH H291 H N N 67  
3PH H292 H N N 68  
3PH H2A1 H N N 69  
3PH H2A2 H N N 70  
3PH H2B1 H N N 71  
3PH H2B2 H N N 72  
3PH H2C1 H N N 73  
3PH H2C2 H N N 74  
3PH H2D1 H N N 75  
3PH H2D2 H N N 76  
3PH H2E1 H N N 77  
3PH H2E2 H N N 78  
3PH H2F1 H N N 79  
3PH H2F2 H N N 80  
3PH H2G1 H N N 81  
3PH H2G2 H N N 82  
3PH H2H1 H N N 83  
3PH H2H2 H N N 84  
3PH H2I1 H N N 85  
3PH H2I2 H N N 86  
3PH H2I3 H N N 87  
3PH H31  H N N 88  
3PH H32  H N N 89  
3PH H321 H N N 90  
3PH H322 H N N 91  
3PH H331 H N N 92  
3PH H332 H N N 93  
3PH H341 H N N 94  
3PH H342 H N N 95  
3PH H351 H N N 96  
3PH H352 H N N 97  
3PH H361 H N N 98  
3PH H362 H N N 99  
3PH H371 H N N 100 
3PH H372 H N N 101 
3PH H381 H N N 102 
3PH H382 H N N 103 
3PH H391 H N N 104 
3PH H392 H N N 105 
3PH H3A1 H N N 106 
3PH H3A2 H N N 107 
3PH H3B1 H N N 108 
3PH H3B2 H N N 109 
3PH H3C1 H N N 110 
3PH H3C2 H N N 111 
3PH H3D1 H N N 112 
3PH H3D2 H N N 113 
3PH H3E1 H N N 114 
3PH H3E2 H N N 115 
3PH H3F1 H N N 116 
3PH H3F2 H N N 117 
3PH H3G1 H N N 118 
3PH H3G2 H N N 119 
3PH H3H1 H N N 120 
3PH H3H2 H N N 121 
3PH H3I1 H N N 122 
3PH H3I2 H N N 123 
3PH H3I3 H N N 124 
3PH H77  H N N 125 
ALA N    N N N 126 
ALA CA   C N S 127 
ALA C    C N N 128 
ALA O    O N N 129 
ALA CB   C N N 130 
ALA OXT  O N N 131 
ALA H    H N N 132 
ALA H2   H N N 133 
ALA HA   H N N 134 
ALA HB1  H N N 135 
ALA HB2  H N N 136 
ALA HB3  H N N 137 
ALA HXT  H N N 138 
ARG N    N N N 139 
ARG CA   C N S 140 
ARG C    C N N 141 
ARG O    O N N 142 
ARG CB   C N N 143 
ARG CG   C N N 144 
ARG CD   C N N 145 
ARG NE   N N N 146 
ARG CZ   C N N 147 
ARG NH1  N N N 148 
ARG NH2  N N N 149 
ARG OXT  O N N 150 
ARG H    H N N 151 
ARG H2   H N N 152 
ARG HA   H N N 153 
ARG HB2  H N N 154 
ARG HB3  H N N 155 
ARG HG2  H N N 156 
ARG HG3  H N N 157 
ARG HD2  H N N 158 
ARG HD3  H N N 159 
ARG HE   H N N 160 
ARG HH11 H N N 161 
ARG HH12 H N N 162 
ARG HH21 H N N 163 
ARG HH22 H N N 164 
ARG HXT  H N N 165 
ASN N    N N N 166 
ASN CA   C N S 167 
ASN C    C N N 168 
ASN O    O N N 169 
ASN CB   C N N 170 
ASN CG   C N N 171 
ASN OD1  O N N 172 
ASN ND2  N N N 173 
ASN OXT  O N N 174 
ASN H    H N N 175 
ASN H2   H N N 176 
ASN HA   H N N 177 
ASN HB2  H N N 178 
ASN HB3  H N N 179 
ASN HD21 H N N 180 
ASN HD22 H N N 181 
ASN HXT  H N N 182 
ASP N    N N N 183 
ASP CA   C N S 184 
ASP C    C N N 185 
ASP O    O N N 186 
ASP CB   C N N 187 
ASP CG   C N N 188 
ASP OD1  O N N 189 
ASP OD2  O N N 190 
ASP OXT  O N N 191 
ASP H    H N N 192 
ASP H2   H N N 193 
ASP HA   H N N 194 
ASP HB2  H N N 195 
ASP HB3  H N N 196 
ASP HD2  H N N 197 
ASP HXT  H N N 198 
CYS N    N N N 199 
CYS CA   C N R 200 
CYS C    C N N 201 
CYS O    O N N 202 
CYS CB   C N N 203 
CYS SG   S N N 204 
CYS OXT  O N N 205 
CYS H    H N N 206 
CYS H2   H N N 207 
CYS HA   H N N 208 
CYS HB2  H N N 209 
CYS HB3  H N N 210 
CYS HG   H N N 211 
CYS HXT  H N N 212 
GLN N    N N N 213 
GLN CA   C N S 214 
GLN C    C N N 215 
GLN O    O N N 216 
GLN CB   C N N 217 
GLN CG   C N N 218 
GLN CD   C N N 219 
GLN OE1  O N N 220 
GLN NE2  N N N 221 
GLN OXT  O N N 222 
GLN H    H N N 223 
GLN H2   H N N 224 
GLN HA   H N N 225 
GLN HB2  H N N 226 
GLN HB3  H N N 227 
GLN HG2  H N N 228 
GLN HG3  H N N 229 
GLN HE21 H N N 230 
GLN HE22 H N N 231 
GLN HXT  H N N 232 
GLU N    N N N 233 
GLU CA   C N S 234 
GLU C    C N N 235 
GLU O    O N N 236 
GLU CB   C N N 237 
GLU CG   C N N 238 
GLU CD   C N N 239 
GLU OE1  O N N 240 
GLU OE2  O N N 241 
GLU OXT  O N N 242 
GLU H    H N N 243 
GLU H2   H N N 244 
GLU HA   H N N 245 
GLU HB2  H N N 246 
GLU HB3  H N N 247 
GLU HG2  H N N 248 
GLU HG3  H N N 249 
GLU HE2  H N N 250 
GLU HXT  H N N 251 
GLY N    N N N 252 
GLY CA   C N N 253 
GLY C    C N N 254 
GLY O    O N N 255 
GLY OXT  O N N 256 
GLY H    H N N 257 
GLY H2   H N N 258 
GLY HA2  H N N 259 
GLY HA3  H N N 260 
GLY HXT  H N N 261 
HIS N    N N N 262 
HIS CA   C N S 263 
HIS C    C N N 264 
HIS O    O N N 265 
HIS CB   C N N 266 
HIS CG   C Y N 267 
HIS ND1  N Y N 268 
HIS CD2  C Y N 269 
HIS CE1  C Y N 270 
HIS NE2  N Y N 271 
HIS OXT  O N N 272 
HIS H    H N N 273 
HIS H2   H N N 274 
HIS HA   H N N 275 
HIS HB2  H N N 276 
HIS HB3  H N N 277 
HIS HD1  H N N 278 
HIS HD2  H N N 279 
HIS HE1  H N N 280 
HIS HE2  H N N 281 
HIS HXT  H N N 282 
HOH O    O N N 283 
HOH H1   H N N 284 
HOH H2   H N N 285 
ILE N    N N N 286 
ILE CA   C N S 287 
ILE C    C N N 288 
ILE O    O N N 289 
ILE CB   C N S 290 
ILE CG1  C N N 291 
ILE CG2  C N N 292 
ILE CD1  C N N 293 
ILE OXT  O N N 294 
ILE H    H N N 295 
ILE H2   H N N 296 
ILE HA   H N N 297 
ILE HB   H N N 298 
ILE HG12 H N N 299 
ILE HG13 H N N 300 
ILE HG21 H N N 301 
ILE HG22 H N N 302 
ILE HG23 H N N 303 
ILE HD11 H N N 304 
ILE HD12 H N N 305 
ILE HD13 H N N 306 
ILE HXT  H N N 307 
LEU N    N N N 308 
LEU CA   C N S 309 
LEU C    C N N 310 
LEU O    O N N 311 
LEU CB   C N N 312 
LEU CG   C N N 313 
LEU CD1  C N N 314 
LEU CD2  C N N 315 
LEU OXT  O N N 316 
LEU H    H N N 317 
LEU H2   H N N 318 
LEU HA   H N N 319 
LEU HB2  H N N 320 
LEU HB3  H N N 321 
LEU HG   H N N 322 
LEU HD11 H N N 323 
LEU HD12 H N N 324 
LEU HD13 H N N 325 
LEU HD21 H N N 326 
LEU HD22 H N N 327 
LEU HD23 H N N 328 
LEU HXT  H N N 329 
LYS N    N N N 330 
LYS CA   C N S 331 
LYS C    C N N 332 
LYS O    O N N 333 
LYS CB   C N N 334 
LYS CG   C N N 335 
LYS CD   C N N 336 
LYS CE   C N N 337 
LYS NZ   N N N 338 
LYS OXT  O N N 339 
LYS H    H N N 340 
LYS H2   H N N 341 
LYS HA   H N N 342 
LYS HB2  H N N 343 
LYS HB3  H N N 344 
LYS HG2  H N N 345 
LYS HG3  H N N 346 
LYS HD2  H N N 347 
LYS HD3  H N N 348 
LYS HE2  H N N 349 
LYS HE3  H N N 350 
LYS HZ1  H N N 351 
LYS HZ2  H N N 352 
LYS HZ3  H N N 353 
LYS HXT  H N N 354 
MET N    N N N 355 
MET CA   C N S 356 
MET C    C N N 357 
MET O    O N N 358 
MET CB   C N N 359 
MET CG   C N N 360 
MET SD   S N N 361 
MET CE   C N N 362 
MET OXT  O N N 363 
MET H    H N N 364 
MET H2   H N N 365 
MET HA   H N N 366 
MET HB2  H N N 367 
MET HB3  H N N 368 
MET HG2  H N N 369 
MET HG3  H N N 370 
MET HE1  H N N 371 
MET HE2  H N N 372 
MET HE3  H N N 373 
MET HXT  H N N 374 
PHE N    N N N 375 
PHE CA   C N S 376 
PHE C    C N N 377 
PHE O    O N N 378 
PHE CB   C N N 379 
PHE CG   C Y N 380 
PHE CD1  C Y N 381 
PHE CD2  C Y N 382 
PHE CE1  C Y N 383 
PHE CE2  C Y N 384 
PHE CZ   C Y N 385 
PHE OXT  O N N 386 
PHE H    H N N 387 
PHE H2   H N N 388 
PHE HA   H N N 389 
PHE HB2  H N N 390 
PHE HB3  H N N 391 
PHE HD1  H N N 392 
PHE HD2  H N N 393 
PHE HE1  H N N 394 
PHE HE2  H N N 395 
PHE HZ   H N N 396 
PHE HXT  H N N 397 
PRO N    N N N 398 
PRO CA   C N S 399 
PRO C    C N N 400 
PRO O    O N N 401 
PRO CB   C N N 402 
PRO CG   C N N 403 
PRO CD   C N N 404 
PRO OXT  O N N 405 
PRO H    H N N 406 
PRO HA   H N N 407 
PRO HB2  H N N 408 
PRO HB3  H N N 409 
PRO HG2  H N N 410 
PRO HG3  H N N 411 
PRO HD2  H N N 412 
PRO HD3  H N N 413 
PRO HXT  H N N 414 
SER N    N N N 415 
SER CA   C N S 416 
SER C    C N N 417 
SER O    O N N 418 
SER CB   C N N 419 
SER OG   O N N 420 
SER OXT  O N N 421 
SER H    H N N 422 
SER H2   H N N 423 
SER HA   H N N 424 
SER HB2  H N N 425 
SER HB3  H N N 426 
SER HG   H N N 427 
SER HXT  H N N 428 
THR N    N N N 429 
THR CA   C N S 430 
THR C    C N N 431 
THR O    O N N 432 
THR CB   C N R 433 
THR OG1  O N N 434 
THR CG2  C N N 435 
THR OXT  O N N 436 
THR H    H N N 437 
THR H2   H N N 438 
THR HA   H N N 439 
THR HB   H N N 440 
THR HG1  H N N 441 
THR HG21 H N N 442 
THR HG22 H N N 443 
THR HG23 H N N 444 
THR HXT  H N N 445 
TRP N    N N N 446 
TRP CA   C N S 447 
TRP C    C N N 448 
TRP O    O N N 449 
TRP CB   C N N 450 
TRP CG   C Y N 451 
TRP CD1  C Y N 452 
TRP CD2  C Y N 453 
TRP NE1  N Y N 454 
TRP CE2  C Y N 455 
TRP CE3  C Y N 456 
TRP CZ2  C Y N 457 
TRP CZ3  C Y N 458 
TRP CH2  C Y N 459 
TRP OXT  O N N 460 
TRP H    H N N 461 
TRP H2   H N N 462 
TRP HA   H N N 463 
TRP HB2  H N N 464 
TRP HB3  H N N 465 
TRP HD1  H N N 466 
TRP HE1  H N N 467 
TRP HE3  H N N 468 
TRP HZ2  H N N 469 
TRP HZ3  H N N 470 
TRP HH2  H N N 471 
TRP HXT  H N N 472 
TYR N    N N N 473 
TYR CA   C N S 474 
TYR C    C N N 475 
TYR O    O N N 476 
TYR CB   C N N 477 
TYR CG   C Y N 478 
TYR CD1  C Y N 479 
TYR CD2  C Y N 480 
TYR CE1  C Y N 481 
TYR CE2  C Y N 482 
TYR CZ   C Y N 483 
TYR OH   O N N 484 
TYR OXT  O N N 485 
TYR H    H N N 486 
TYR H2   H N N 487 
TYR HA   H N N 488 
TYR HB2  H N N 489 
TYR HB3  H N N 490 
TYR HD1  H N N 491 
TYR HD2  H N N 492 
TYR HE1  H N N 493 
TYR HE2  H N N 494 
TYR HH   H N N 495 
TYR HXT  H N N 496 
VAL N    N N N 497 
VAL CA   C N S 498 
VAL C    C N N 499 
VAL O    O N N 500 
VAL CB   C N N 501 
VAL CG1  C N N 502 
VAL CG2  C N N 503 
VAL OXT  O N N 504 
VAL H    H N N 505 
VAL H2   H N N 506 
VAL HA   H N N 507 
VAL HB   H N N 508 
VAL HG11 H N N 509 
VAL HG12 H N N 510 
VAL HG13 H N N 511 
VAL HG21 H N N 512 
VAL HG22 H N N 513 
VAL HG23 H N N 514 
VAL HXT  H N N 515 
# 
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 
3PH O13 P    sing N N 1   
3PH O13 H13  sing N N 2   
3PH P   O14  sing N N 3   
3PH P   O12  doub N N 4   
3PH P   O11  sing N N 5   
3PH O11 C1   sing N N 6   
3PH C1  C2   sing N N 7   
3PH C1  H11  sing N N 8   
3PH C1  H12  sing N N 9   
3PH C2  O21  sing N N 10  
3PH C2  C3   sing N N 11  
3PH C2  H2   sing N N 12  
3PH O21 C21  sing N N 13  
3PH C21 O22  doub N N 14  
3PH C21 C22  sing N N 15  
3PH C22 C23  sing N N 16  
3PH C22 H221 sing N N 17  
3PH C22 H222 sing N N 18  
3PH C23 C24  sing N N 19  
3PH C23 H231 sing N N 20  
3PH C23 H232 sing N N 21  
3PH C24 C25  sing N N 22  
3PH C24 H241 sing N N 23  
3PH C24 H242 sing N N 24  
3PH C25 C26  sing N N 25  
3PH C25 H251 sing N N 26  
3PH C25 H252 sing N N 27  
3PH C26 C27  sing N N 28  
3PH C26 H261 sing N N 29  
3PH C26 H262 sing N N 30  
3PH C27 C28  sing N N 31  
3PH C27 H271 sing N N 32  
3PH C27 H272 sing N N 33  
3PH C28 C29  sing N N 34  
3PH C28 H281 sing N N 35  
3PH C28 H282 sing N N 36  
3PH C29 C2A  sing N N 37  
3PH C29 H291 sing N N 38  
3PH C29 H292 sing N N 39  
3PH C2A C2B  sing N N 40  
3PH C2A H2A1 sing N N 41  
3PH C2A H2A2 sing N N 42  
3PH C2B C2C  sing N N 43  
3PH C2B H2B1 sing N N 44  
3PH C2B H2B2 sing N N 45  
3PH C2C C2D  sing N N 46  
3PH C2C H2C1 sing N N 47  
3PH C2C H2C2 sing N N 48  
3PH C2D C2E  sing N N 49  
3PH C2D H2D1 sing N N 50  
3PH C2D H2D2 sing N N 51  
3PH C2E C2F  sing N N 52  
3PH C2E H2E1 sing N N 53  
3PH C2E H2E2 sing N N 54  
3PH C2F C2G  sing N N 55  
3PH C2F H2F1 sing N N 56  
3PH C2F H2F2 sing N N 57  
3PH C2G C2H  sing N N 58  
3PH C2G H2G1 sing N N 59  
3PH C2G H2G2 sing N N 60  
3PH C2H C2I  sing N N 61  
3PH C2H H2H1 sing N N 62  
3PH C2H H2H2 sing N N 63  
3PH C2I H2I1 sing N N 64  
3PH C2I H2I2 sing N N 65  
3PH C2I H2I3 sing N N 66  
3PH C3  O31  sing N N 67  
3PH C3  H31  sing N N 68  
3PH C3  H32  sing N N 69  
3PH O31 C31  sing N N 70  
3PH C31 O32  doub N N 71  
3PH C31 C32  sing N N 72  
3PH C32 C33  sing N N 73  
3PH C32 H321 sing N N 74  
3PH C32 H322 sing N N 75  
3PH C33 C34  sing N N 76  
3PH C33 H331 sing N N 77  
3PH C33 H332 sing N N 78  
3PH C34 C35  sing N N 79  
3PH C34 H341 sing N N 80  
3PH C34 H342 sing N N 81  
3PH C35 C36  sing N N 82  
3PH C35 H351 sing N N 83  
3PH C35 H352 sing N N 84  
3PH C36 C37  sing N N 85  
3PH C36 H361 sing N N 86  
3PH C36 H362 sing N N 87  
3PH C37 C38  sing N N 88  
3PH C37 H371 sing N N 89  
3PH C37 H372 sing N N 90  
3PH C38 C39  sing N N 91  
3PH C38 H381 sing N N 92  
3PH C38 H382 sing N N 93  
3PH C39 C3A  sing N N 94  
3PH C39 H391 sing N N 95  
3PH C39 H392 sing N N 96  
3PH C3A C3B  sing N N 97  
3PH C3A H3A1 sing N N 98  
3PH C3A H3A2 sing N N 99  
3PH C3B C3C  sing N N 100 
3PH C3B H3B1 sing N N 101 
3PH C3B H3B2 sing N N 102 
3PH C3C C3D  sing N N 103 
3PH C3C H3C1 sing N N 104 
3PH C3C H3C2 sing N N 105 
3PH C3D C3E  sing N N 106 
3PH C3D H3D1 sing N N 107 
3PH C3D H3D2 sing N N 108 
3PH C3E C3F  sing N N 109 
3PH C3E H3E1 sing N N 110 
3PH C3E H3E2 sing N N 111 
3PH C3F C3G  sing N N 112 
3PH C3F H3F1 sing N N 113 
3PH C3F H3F2 sing N N 114 
3PH C3G C3H  sing N N 115 
3PH C3G H3G1 sing N N 116 
3PH C3G H3G2 sing N N 117 
3PH C3H C3I  sing N N 118 
3PH C3H H3H1 sing N N 119 
3PH C3H H3H2 sing N N 120 
3PH C3I H3I1 sing N N 121 
3PH C3I H3I2 sing N N 122 
3PH C3I H3I3 sing N N 123 
3PH O14 H77  sing N N 124 
ALA N   CA   sing N N 125 
ALA N   H    sing N N 126 
ALA N   H2   sing N N 127 
ALA CA  C    sing N N 128 
ALA CA  CB   sing N N 129 
ALA CA  HA   sing N N 130 
ALA C   O    doub N N 131 
ALA C   OXT  sing N N 132 
ALA CB  HB1  sing N N 133 
ALA CB  HB2  sing N N 134 
ALA CB  HB3  sing N N 135 
ALA OXT HXT  sing N N 136 
ARG N   CA   sing N N 137 
ARG N   H    sing N N 138 
ARG N   H2   sing N N 139 
ARG CA  C    sing N N 140 
ARG CA  CB   sing N N 141 
ARG CA  HA   sing N N 142 
ARG C   O    doub N N 143 
ARG C   OXT  sing N N 144 
ARG CB  CG   sing N N 145 
ARG CB  HB2  sing N N 146 
ARG CB  HB3  sing N N 147 
ARG CG  CD   sing N N 148 
ARG CG  HG2  sing N N 149 
ARG CG  HG3  sing N N 150 
ARG CD  NE   sing N N 151 
ARG CD  HD2  sing N N 152 
ARG CD  HD3  sing N N 153 
ARG NE  CZ   sing N N 154 
ARG NE  HE   sing N N 155 
ARG CZ  NH1  sing N N 156 
ARG CZ  NH2  doub N N 157 
ARG NH1 HH11 sing N N 158 
ARG NH1 HH12 sing N N 159 
ARG NH2 HH21 sing N N 160 
ARG NH2 HH22 sing N N 161 
ARG OXT HXT  sing N N 162 
ASN N   CA   sing N N 163 
ASN N   H    sing N N 164 
ASN N   H2   sing N N 165 
ASN CA  C    sing N N 166 
ASN CA  CB   sing N N 167 
ASN CA  HA   sing N N 168 
ASN C   O    doub N N 169 
ASN C   OXT  sing N N 170 
ASN CB  CG   sing N N 171 
ASN CB  HB2  sing N N 172 
ASN CB  HB3  sing N N 173 
ASN CG  OD1  doub N N 174 
ASN CG  ND2  sing N N 175 
ASN ND2 HD21 sing N N 176 
ASN ND2 HD22 sing N N 177 
ASN OXT HXT  sing N N 178 
ASP N   CA   sing N N 179 
ASP N   H    sing N N 180 
ASP N   H2   sing N N 181 
ASP CA  C    sing N N 182 
ASP CA  CB   sing N N 183 
ASP CA  HA   sing N N 184 
ASP C   O    doub N N 185 
ASP C   OXT  sing N N 186 
ASP CB  CG   sing N N 187 
ASP CB  HB2  sing N N 188 
ASP CB  HB3  sing N N 189 
ASP CG  OD1  doub N N 190 
ASP CG  OD2  sing N N 191 
ASP OD2 HD2  sing N N 192 
ASP OXT HXT  sing N N 193 
CYS N   CA   sing N N 194 
CYS N   H    sing N N 195 
CYS N   H2   sing N N 196 
CYS CA  C    sing N N 197 
CYS CA  CB   sing N N 198 
CYS CA  HA   sing N N 199 
CYS C   O    doub N N 200 
CYS C   OXT  sing N N 201 
CYS CB  SG   sing N N 202 
CYS CB  HB2  sing N N 203 
CYS CB  HB3  sing N N 204 
CYS SG  HG   sing N N 205 
CYS OXT HXT  sing N N 206 
GLN N   CA   sing N N 207 
GLN N   H    sing N N 208 
GLN N   H2   sing N N 209 
GLN CA  C    sing N N 210 
GLN CA  CB   sing N N 211 
GLN CA  HA   sing N N 212 
GLN C   O    doub N N 213 
GLN C   OXT  sing N N 214 
GLN CB  CG   sing N N 215 
GLN CB  HB2  sing N N 216 
GLN CB  HB3  sing N N 217 
GLN CG  CD   sing N N 218 
GLN CG  HG2  sing N N 219 
GLN CG  HG3  sing N N 220 
GLN CD  OE1  doub N N 221 
GLN CD  NE2  sing N N 222 
GLN NE2 HE21 sing N N 223 
GLN NE2 HE22 sing N N 224 
GLN OXT HXT  sing N N 225 
GLU N   CA   sing N N 226 
GLU N   H    sing N N 227 
GLU N   H2   sing N N 228 
GLU CA  C    sing N N 229 
GLU CA  CB   sing N N 230 
GLU CA  HA   sing N N 231 
GLU C   O    doub N N 232 
GLU C   OXT  sing N N 233 
GLU CB  CG   sing N N 234 
GLU CB  HB2  sing N N 235 
GLU CB  HB3  sing N N 236 
GLU CG  CD   sing N N 237 
GLU CG  HG2  sing N N 238 
GLU CG  HG3  sing N N 239 
GLU CD  OE1  doub N N 240 
GLU CD  OE2  sing N N 241 
GLU OE2 HE2  sing N N 242 
GLU OXT HXT  sing N N 243 
GLY N   CA   sing N N 244 
GLY N   H    sing N N 245 
GLY N   H2   sing N N 246 
GLY CA  C    sing N N 247 
GLY CA  HA2  sing N N 248 
GLY CA  HA3  sing N N 249 
GLY C   O    doub N N 250 
GLY C   OXT  sing N N 251 
GLY OXT HXT  sing N N 252 
HIS N   CA   sing N N 253 
HIS N   H    sing N N 254 
HIS N   H2   sing N N 255 
HIS CA  C    sing N N 256 
HIS CA  CB   sing N N 257 
HIS CA  HA   sing N N 258 
HIS C   O    doub N N 259 
HIS C   OXT  sing N N 260 
HIS CB  CG   sing N N 261 
HIS CB  HB2  sing N N 262 
HIS CB  HB3  sing N N 263 
HIS CG  ND1  sing Y N 264 
HIS CG  CD2  doub Y N 265 
HIS ND1 CE1  doub Y N 266 
HIS ND1 HD1  sing N N 267 
HIS CD2 NE2  sing Y N 268 
HIS CD2 HD2  sing N N 269 
HIS CE1 NE2  sing Y N 270 
HIS CE1 HE1  sing N N 271 
HIS NE2 HE2  sing N N 272 
HIS OXT HXT  sing N N 273 
HOH O   H1   sing N N 274 
HOH O   H2   sing N N 275 
ILE N   CA   sing N N 276 
ILE N   H    sing N N 277 
ILE N   H2   sing N N 278 
ILE CA  C    sing N N 279 
ILE CA  CB   sing N N 280 
ILE CA  HA   sing N N 281 
ILE C   O    doub N N 282 
ILE C   OXT  sing N N 283 
ILE CB  CG1  sing N N 284 
ILE CB  CG2  sing N N 285 
ILE CB  HB   sing N N 286 
ILE CG1 CD1  sing N N 287 
ILE CG1 HG12 sing N N 288 
ILE CG1 HG13 sing N N 289 
ILE CG2 HG21 sing N N 290 
ILE CG2 HG22 sing N N 291 
ILE CG2 HG23 sing N N 292 
ILE CD1 HD11 sing N N 293 
ILE CD1 HD12 sing N N 294 
ILE CD1 HD13 sing N N 295 
ILE OXT HXT  sing N N 296 
LEU N   CA   sing N N 297 
LEU N   H    sing N N 298 
LEU N   H2   sing N N 299 
LEU CA  C    sing N N 300 
LEU CA  CB   sing N N 301 
LEU CA  HA   sing N N 302 
LEU C   O    doub N N 303 
LEU C   OXT  sing N N 304 
LEU CB  CG   sing N N 305 
LEU CB  HB2  sing N N 306 
LEU CB  HB3  sing N N 307 
LEU CG  CD1  sing N N 308 
LEU CG  CD2  sing N N 309 
LEU CG  HG   sing N N 310 
LEU CD1 HD11 sing N N 311 
LEU CD1 HD12 sing N N 312 
LEU CD1 HD13 sing N N 313 
LEU CD2 HD21 sing N N 314 
LEU CD2 HD22 sing N N 315 
LEU CD2 HD23 sing N N 316 
LEU OXT HXT  sing N N 317 
LYS N   CA   sing N N 318 
LYS N   H    sing N N 319 
LYS N   H2   sing N N 320 
LYS CA  C    sing N N 321 
LYS CA  CB   sing N N 322 
LYS CA  HA   sing N N 323 
LYS C   O    doub N N 324 
LYS C   OXT  sing N N 325 
LYS CB  CG   sing N N 326 
LYS CB  HB2  sing N N 327 
LYS CB  HB3  sing N N 328 
LYS CG  CD   sing N N 329 
LYS CG  HG2  sing N N 330 
LYS CG  HG3  sing N N 331 
LYS CD  CE   sing N N 332 
LYS CD  HD2  sing N N 333 
LYS CD  HD3  sing N N 334 
LYS CE  NZ   sing N N 335 
LYS CE  HE2  sing N N 336 
LYS CE  HE3  sing N N 337 
LYS NZ  HZ1  sing N N 338 
LYS NZ  HZ2  sing N N 339 
LYS NZ  HZ3  sing N N 340 
LYS OXT HXT  sing N N 341 
MET N   CA   sing N N 342 
MET N   H    sing N N 343 
MET N   H2   sing N N 344 
MET CA  C    sing N N 345 
MET CA  CB   sing N N 346 
MET CA  HA   sing N N 347 
MET C   O    doub N N 348 
MET C   OXT  sing N N 349 
MET CB  CG   sing N N 350 
MET CB  HB2  sing N N 351 
MET CB  HB3  sing N N 352 
MET CG  SD   sing N N 353 
MET CG  HG2  sing N N 354 
MET CG  HG3  sing N N 355 
MET SD  CE   sing N N 356 
MET CE  HE1  sing N N 357 
MET CE  HE2  sing N N 358 
MET CE  HE3  sing N N 359 
MET OXT HXT  sing N N 360 
PHE N   CA   sing N N 361 
PHE N   H    sing N N 362 
PHE N   H2   sing N N 363 
PHE CA  C    sing N N 364 
PHE CA  CB   sing N N 365 
PHE CA  HA   sing N N 366 
PHE C   O    doub N N 367 
PHE C   OXT  sing N N 368 
PHE CB  CG   sing N N 369 
PHE CB  HB2  sing N N 370 
PHE CB  HB3  sing N N 371 
PHE CG  CD1  doub Y N 372 
PHE CG  CD2  sing Y N 373 
PHE CD1 CE1  sing Y N 374 
PHE CD1 HD1  sing N N 375 
PHE CD2 CE2  doub Y N 376 
PHE CD2 HD2  sing N N 377 
PHE CE1 CZ   doub Y N 378 
PHE CE1 HE1  sing N N 379 
PHE CE2 CZ   sing Y N 380 
PHE CE2 HE2  sing N N 381 
PHE CZ  HZ   sing N N 382 
PHE OXT HXT  sing N N 383 
PRO N   CA   sing N N 384 
PRO N   CD   sing N N 385 
PRO N   H    sing N N 386 
PRO CA  C    sing N N 387 
PRO CA  CB   sing N N 388 
PRO CA  HA   sing N N 389 
PRO C   O    doub N N 390 
PRO C   OXT  sing N N 391 
PRO CB  CG   sing N N 392 
PRO CB  HB2  sing N N 393 
PRO CB  HB3  sing N N 394 
PRO CG  CD   sing N N 395 
PRO CG  HG2  sing N N 396 
PRO CG  HG3  sing N N 397 
PRO CD  HD2  sing N N 398 
PRO CD  HD3  sing N N 399 
PRO OXT HXT  sing N N 400 
SER N   CA   sing N N 401 
SER N   H    sing N N 402 
SER N   H2   sing N N 403 
SER CA  C    sing N N 404 
SER CA  CB   sing N N 405 
SER CA  HA   sing N N 406 
SER C   O    doub N N 407 
SER C   OXT  sing N N 408 
SER CB  OG   sing N N 409 
SER CB  HB2  sing N N 410 
SER CB  HB3  sing N N 411 
SER OG  HG   sing N N 412 
SER OXT HXT  sing N N 413 
THR N   CA   sing N N 414 
THR N   H    sing N N 415 
THR N   H2   sing N N 416 
THR CA  C    sing N N 417 
THR CA  CB   sing N N 418 
THR CA  HA   sing N N 419 
THR C   O    doub N N 420 
THR C   OXT  sing N N 421 
THR CB  OG1  sing N N 422 
THR CB  CG2  sing N N 423 
THR CB  HB   sing N N 424 
THR OG1 HG1  sing N N 425 
THR CG2 HG21 sing N N 426 
THR CG2 HG22 sing N N 427 
THR CG2 HG23 sing N N 428 
THR OXT HXT  sing N N 429 
TRP N   CA   sing N N 430 
TRP N   H    sing N N 431 
TRP N   H2   sing N N 432 
TRP CA  C    sing N N 433 
TRP CA  CB   sing N N 434 
TRP CA  HA   sing N N 435 
TRP C   O    doub N N 436 
TRP C   OXT  sing N N 437 
TRP CB  CG   sing N N 438 
TRP CB  HB2  sing N N 439 
TRP CB  HB3  sing N N 440 
TRP CG  CD1  doub Y N 441 
TRP CG  CD2  sing Y N 442 
TRP CD1 NE1  sing Y N 443 
TRP CD1 HD1  sing N N 444 
TRP CD2 CE2  doub Y N 445 
TRP CD2 CE3  sing Y N 446 
TRP NE1 CE2  sing Y N 447 
TRP NE1 HE1  sing N N 448 
TRP CE2 CZ2  sing Y N 449 
TRP CE3 CZ3  doub Y N 450 
TRP CE3 HE3  sing N N 451 
TRP CZ2 CH2  doub Y N 452 
TRP CZ2 HZ2  sing N N 453 
TRP CZ3 CH2  sing Y N 454 
TRP CZ3 HZ3  sing N N 455 
TRP CH2 HH2  sing N N 456 
TRP OXT HXT  sing N N 457 
TYR N   CA   sing N N 458 
TYR N   H    sing N N 459 
TYR N   H2   sing N N 460 
TYR CA  C    sing N N 461 
TYR CA  CB   sing N N 462 
TYR CA  HA   sing N N 463 
TYR C   O    doub N N 464 
TYR C   OXT  sing N N 465 
TYR CB  CG   sing N N 466 
TYR CB  HB2  sing N N 467 
TYR CB  HB3  sing N N 468 
TYR CG  CD1  doub Y N 469 
TYR CG  CD2  sing Y N 470 
TYR CD1 CE1  sing Y N 471 
TYR CD1 HD1  sing N N 472 
TYR CD2 CE2  doub Y N 473 
TYR CD2 HD2  sing N N 474 
TYR CE1 CZ   doub Y N 475 
TYR CE1 HE1  sing N N 476 
TYR CE2 CZ   sing Y N 477 
TYR CE2 HE2  sing N N 478 
TYR CZ  OH   sing N N 479 
TYR OH  HH   sing N N 480 
TYR OXT HXT  sing N N 481 
VAL N   CA   sing N N 482 
VAL N   H    sing N N 483 
VAL N   H2   sing N N 484 
VAL CA  C    sing N N 485 
VAL CA  CB   sing N N 486 
VAL CA  HA   sing N N 487 
VAL C   O    doub N N 488 
VAL C   OXT  sing N N 489 
VAL CB  CG1  sing N N 490 
VAL CB  CG2  sing N N 491 
VAL CB  HB   sing N N 492 
VAL CG1 HG11 sing N N 493 
VAL CG1 HG12 sing N N 494 
VAL CG1 HG13 sing N N 495 
VAL CG2 HG21 sing N N 496 
VAL CG2 HG22 sing N N 497 
VAL CG2 HG23 sing N N 498 
VAL OXT HXT  sing N N 499 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-07 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8ZTN 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'AtALMT9 with LMNG (trans2 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                   2 
_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                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               Sf9 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    18 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   2895997 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? Topaz     0.2.5a  
'IMAGE ACQUISITION'             ? 2  ? ? 1 ?         ?       
MASKING                         ? 3  ? ? ? ?         ?       
'CTF CORRECTION'                ? 4  1 ? ? cryoSPARC 4.4     
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ?       
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ?       
'MODEL FITTING'                 ? 7  ? 1 ? Coot      0.9.8.1 
OTHER                           ? 8  ? ? ? ?         ?       
'MODEL REFINEMENT'              ? 9  ? 1 ? PHENIX    1.20.1  
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? cryoSPARC 4.4     
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC 4.4     
CLASSIFICATION                  ? 12 1 ? ? cryoSPARC 4.4     
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC 4.4     
'VOLUME SELECTION'              ? 14 1 1 1 ?         ?       
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ?       
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ?       
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ?       
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ?       
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?         ?       
# 
_em_specimen.concentration           1.9 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' 2022R1A2C100988211 1 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' RS-2023-00223552   2 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' 2021M3A9I4022936   3 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZTN 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . ALA A 1 77  ? 118.69300 131.13400 106.35300 1.000 91.25225  ? 77  ALA A N    1 
ATOM   2    C CA   . ALA A 1 77  ? 118.24300 131.59100 107.66200 1.000 92.23891  ? 77  ALA A CA   1 
ATOM   3    C C    . ALA A 1 77  ? 117.35900 132.82600 107.53400 1.000 92.74994  ? 77  ALA A C    1 
ATOM   4    O O    . ALA A 1 77  ? 116.20600 132.73500 107.11500 1.000 93.37059  ? 77  ALA A O    1 
ATOM   5    C CB   . ALA A 1 77  ? 119.43400 131.88200 108.56000 1.000 91.37472  ? 77  ALA A CB   1 
ATOM   6    N N    . TRP A 1 78  ? 117.90800 133.98000 107.92000 1.000 94.38681  ? 78  TRP A N    1 
ATOM   7    C CA   . TRP A 1 78  ? 117.15500 135.22700 107.83600 1.000 94.09297  ? 78  TRP A CA   1 
ATOM   8    C C    . TRP A 1 78  ? 116.62700 135.45500 106.42500 1.000 93.84860  ? 78  TRP A C    1 
ATOM   9    O O    . TRP A 1 78  ? 115.50800 135.94800 106.24400 1.000 93.86338  ? 78  TRP A O    1 
ATOM   10   C CB   . TRP A 1 78  ? 118.03300 136.39400 108.30400 1.000 94.80114  ? 78  TRP A CB   1 
ATOM   11   C CG   . TRP A 1 78  ? 117.62200 137.76600 107.81900 1.000 95.69951  ? 78  TRP A CG   1 
ATOM   12   C CD1  . TRP A 1 78  ? 117.66800 138.24300 106.53800 1.000 95.06800  ? 78  TRP A CD1  1 
ATOM   13   C CD2  . TRP A 1 78  ? 117.09900 138.83100 108.62200 1.000 95.61814  ? 78  TRP A CD2  1 
ATOM   14   N NE1  . TRP A 1 78  ? 117.20800 139.53600 106.49700 1.000 95.32306  ? 78  TRP A NE1  1 
ATOM   15   C CE2  . TRP A 1 78  ? 116.85300 139.92100 107.76300 1.000 96.06548  ? 78  TRP A CE2  1 
ATOM   16   C CE3  . TRP A 1 78  ? 116.81700 138.97000 109.98400 1.000 95.26118  ? 78  TRP A CE3  1 
ATOM   17   C CZ2  . TRP A 1 78  ? 116.33800 141.13100 108.22200 1.000 95.27260  ? 78  TRP A CZ2  1 
ATOM   18   C CZ3  . TRP A 1 78  ? 116.30600 140.17200 110.43700 1.000 95.08067  ? 78  TRP A CZ3  1 
ATOM   19   C CH2  . TRP A 1 78  ? 116.07100 141.23600 109.55900 1.000 95.18300  ? 78  TRP A CH2  1 
ATOM   20   N N    . GLU A 1 79  ? 117.44000 135.14800 105.41100 1.000 87.29571  ? 79  GLU A N    1 
ATOM   21   C CA   . GLU A 1 79  ? 116.97600 135.27200 104.03300 1.000 87.54923  ? 79  GLU A CA   1 
ATOM   22   C C    . GLU A 1 79  ? 115.76300 134.38700 103.77300 1.000 88.05704  ? 79  GLU A C    1 
ATOM   23   O O    . GLU A 1 79  ? 114.84200 134.78000 103.04700 1.000 88.32332  ? 79  GLU A O    1 
ATOM   24   C CB   . GLU A 1 79  ? 118.10900 134.92700 103.06600 1.000 87.65160  ? 79  GLU A CB   1 
ATOM   25   N N    . MET A 1 80  ? 115.72800 133.19700 104.37800 1.000 84.34955  ? 80  MET A N    1 
ATOM   26   C CA   . MET A 1 80  ? 114.57400 132.32300 104.19600 1.000 83.33397  ? 80  MET A CA   1 
ATOM   27   C C    . MET A 1 80  ? 113.36100 132.83800 104.95500 1.000 81.46826  ? 80  MET A C    1 
ATOM   28   O O    . MET A 1 80  ? 112.22500 132.66800 104.49700 1.000 79.81580  ? 80  MET A O    1 
ATOM   29   C CB   . MET A 1 80  ? 114.91000 130.89900 104.64000 1.000 83.37281  ? 80  MET A CB   1 
ATOM   30   C CG   . MET A 1 80  ? 113.73700 130.15700 105.26300 1.000 83.87545  ? 80  MET A CG   1 
ATOM   31   S SD   . MET A 1 80  ? 114.15000 128.47800 105.77200 1.000 88.39851  ? 80  MET A SD   1 
ATOM   32   C CE   . MET A 1 80  ? 114.36900 128.69700 107.53600 1.000 82.09257  ? 80  MET A CE   1 
ATOM   33   N N    . GLY A 1 81  ? 113.57600 133.46300 106.11200 1.000 74.45564  ? 81  GLY A N    1 
ATOM   34   C CA   . GLY A 1 81  ? 112.46100 134.03800 106.84300 1.000 74.85810  ? 81  GLY A CA   1 
ATOM   35   C C    . GLY A 1 81  ? 111.85700 135.22600 106.12100 1.000 77.58535  ? 81  GLY A C    1 
ATOM   36   O O    . GLY A 1 81  ? 110.63600 135.39800 106.10000 1.000 77.75994  ? 81  GLY A O    1 
ATOM   37   N N    . VAL A 1 82  ? 112.70500 136.06400 105.52200 1.000 83.06377  ? 82  VAL A N    1 
ATOM   38   C CA   . VAL A 1 82  ? 112.20900 137.19800 104.74900 1.000 82.22342  ? 82  VAL A CA   1 
ATOM   39   C C    . VAL A 1 82  ? 111.53700 136.71800 103.46900 1.000 80.84312  ? 82  VAL A C    1 
ATOM   40   O O    . VAL A 1 82  ? 110.54300 137.30000 103.01800 1.000 81.07434  ? 82  VAL A O    1 
ATOM   41   C CB   . VAL A 1 82  ? 113.34800 138.19100 104.45500 1.000 82.27386  ? 82  VAL A CB   1 
ATOM   42   C CG1  . VAL A 1 82  ? 113.94100 138.71700 105.75300 1.000 82.41912  ? 82  VAL A CG1  1 
ATOM   43   C CG2  . VAL A 1 82  ? 114.41800 137.53800 103.60000 1.000 82.22312  ? 82  VAL A CG2  1 
ATOM   44   N N    . SER A 1 83  ? 112.06600 135.65400 102.86000 1.000 77.31863  ? 83  SER A N    1 
ATOM   45   C CA   . SER A 1 83  ? 111.44700 135.11000 101.65600 1.000 77.99879  ? 83  SER A CA   1 
ATOM   46   C C    . SER A 1 83  ? 110.06300 134.54500 101.95500 1.000 79.64313  ? 83  SER A C    1 
ATOM   47   O O    . SER A 1 83  ? 109.09400 134.84300 101.24700 1.000 77.44680  ? 83  SER A O    1 
ATOM   48   C CB   . SER A 1 83  ? 112.34800 134.03800 101.04400 1.000 77.29029  ? 83  SER A CB   1 
ATOM   49   O OG   . SER A 1 83  ? 111.79000 133.52300 99.84800  1.000 76.91408  ? 83  SER A OG   1 
ATOM   50   N N    . ASP A 1 84  ? 109.95200 133.72700 102.99500 1.000 74.96460  ? 84  ASP A N    1 
ATOM   51   C CA   . ASP A 1 84  ? 108.67900 133.12300 103.38700 1.000 70.01779  ? 84  ASP A CA   1 
ATOM   52   C C    . ASP A 1 84  ? 108.35500 133.47400 104.83100 1.000 67.61922  ? 84  ASP A C    1 
ATOM   53   O O    . ASP A 1 84  ? 109.04100 132.98800 105.75100 1.000 67.75550  ? 84  ASP A O    1 
ATOM   54   C CB   . ASP A 1 84  ? 108.72400 131.60600 103.20800 1.000 67.00391  ? 84  ASP A CB   1 
ATOM   55   C CG   . ASP A 1 84  ? 107.34300 130.98900 103.12300 1.000 70.43948  ? 84  ASP A CG   1 
ATOM   56   O OD1  . ASP A 1 84  ? 106.36600 131.74100 102.93000 1.000 72.71589  ? 84  ASP A OD1  1 
ATOM   57   O OD2  . ASP A 1 84  ? 107.23600 129.75100 103.24700 1.000 71.59312  ? 84  ASP A OD2  1 
ATOM   58   N N    . PRO A 1 85  ? 107.33800 134.29800 105.09100 1.000 53.91946  ? 85  PRO A N    1 
ATOM   59   C CA   . PRO A 1 85  ? 107.00200 134.65300 106.47400 1.000 54.20668  ? 85  PRO A CA   1 
ATOM   60   C C    . PRO A 1 85  ? 106.09600 133.65200 107.17000 1.000 52.95898  ? 85  PRO A C    1 
ATOM   61   O O    . PRO A 1 85  ? 105.78000 133.84600 108.34900 1.000 55.04253  ? 85  PRO A O    1 
ATOM   62   C CB   . PRO A 1 85  ? 106.29800 136.00600 106.31000 1.000 54.71945  ? 85  PRO A CB   1 
ATOM   63   C CG   . PRO A 1 85  ? 105.63700 135.90700 104.97900 1.000 54.73755  ? 85  PRO A CG   1 
ATOM   64   C CD   . PRO A 1 85  ? 106.51800 135.03500 104.11400 1.000 53.62969  ? 85  PRO A CD   1 
ATOM   65   N N    . ARG A 1 86  ? 105.66400 132.59500 106.48100 1.000 43.54754  ? 86  ARG A N    1 
ATOM   66   C CA   . ARG A 1 86  ? 104.83200 131.57500 107.10500 1.000 38.50155  ? 86  ARG A CA   1 
ATOM   67   C C    . ARG A 1 86  ? 105.61000 130.69300 108.07200 1.000 40.25915  ? 86  ARG A C    1 
ATOM   68   O O    . ARG A 1 86  ? 104.98800 129.98000 108.86500 1.000 47.31611  ? 86  ARG A O    1 
ATOM   69   C CB   . ARG A 1 86  ? 104.16500 130.71200 106.03200 1.000 40.22059  ? 86  ARG A CB   1 
ATOM   70   C CG   . ARG A 1 86  ? 102.67100 130.54300 106.23800 1.000 40.03119  ? 86  ARG A CG   1 
ATOM   71   C CD   . ARG A 1 86  ? 102.01700 129.76400 105.11000 1.000 41.40820  ? 86  ARG A CD   1 
ATOM   72   N NE   . ARG A 1 86  ? 102.72200 128.52700 104.79700 1.000 38.44388  ? 86  ARG A NE   1 
ATOM   73   C CZ   . ARG A 1 86  ? 102.48500 127.78700 103.72300 1.000 36.48228  ? 86  ARG A CZ   1 
ATOM   74   N NH1  . ARG A 1 86  ? 101.56000 128.12600 102.84200 1.000 43.77190  ? 86  ARG A NH1  1 
ATOM   75   N NH2  . ARG A 1 86  ? 103.19000 126.67700 103.53100 1.000 35.94539  ? 86  ARG A NH2  1 
ATOM   76   N N    . LYS A 1 87  ? 106.94000 130.72700 108.02900 1.000 36.26845  ? 87  LYS A N    1 
ATOM   77   C CA   . LYS A 1 87  ? 107.77800 129.90700 108.89100 1.000 30.48135  ? 87  LYS A CA   1 
ATOM   78   C C    . LYS A 1 87  ? 108.24600 130.64700 110.13500 1.000 27.66752  ? 87  LYS A C    1 
ATOM   79   O O    . LYS A 1 87  ? 108.91400 130.04700 110.98100 1.000 31.06809  ? 87  LYS A O    1 
ATOM   80   C CB   . LYS A 1 87  ? 108.99400 129.39300 108.11500 1.000 31.29867  ? 87  LYS A CB   1 
ATOM   81   C CG   . LYS A 1 87  ? 108.65600 128.70100 106.80800 1.000 33.29458  ? 87  LYS A CG   1 
ATOM   82   C CD   . LYS A 1 87  ? 109.78100 127.77800 106.37500 1.000 30.32498  ? 87  LYS A CD   1 
ATOM   83   C CE   . LYS A 1 87  ? 109.26700 126.66000 105.48500 1.000 35.23633  ? 87  LYS A CE   1 
ATOM   84   N NZ   . LYS A 1 87  ? 110.35600 126.04900 104.67600 1.000 32.36028  ? 87  LYS A NZ   1 
ATOM   85   N N    . ILE A 1 88  ? 107.90900 131.93100 110.26700 1.000 29.97702  ? 88  ILE A N    1 
ATOM   86   C CA   . ILE A 1 88  ? 108.27300 132.70700 111.44700 1.000 26.36046  ? 88  ILE A CA   1 
ATOM   87   C C    . ILE A 1 88  ? 107.11600 132.81900 112.42900 1.000 30.92561  ? 88  ILE A C    1 
ATOM   88   O O    . ILE A 1 88  ? 107.33700 133.18500 113.59500 1.000 40.25445  ? 88  ILE A O    1 
ATOM   89   C CB   . ILE A 1 88  ? 108.77600 134.11200 111.04600 1.000 31.70994  ? 88  ILE A CB   1 
ATOM   90   C CG1  . ILE A 1 88  ? 110.23900 134.04900 110.61000 1.000 32.88612  ? 88  ILE A CG1  1 
ATOM   91   C CG2  . ILE A 1 88  ? 108.61600 135.10500 112.18500 1.000 31.94070  ? 88  ILE A CG2  1 
ATOM   92   C CD1  . ILE A 1 88  ? 110.61100 135.09200 109.58500 1.000 32.87644  ? 88  ILE A CD1  1 
ATOM   93   N N    . VAL A 1 89  ? 105.90200 132.47500 112.01100 1.000 27.33529  ? 89  VAL A N    1 
ATOM   94   C CA   . VAL A 1 89  ? 104.75300 132.49200 112.90500 1.000 25.53228  ? 89  VAL A CA   1 
ATOM   95   C C    . VAL A 1 89  ? 104.55300 131.13200 113.56800 1.000 27.43361  ? 89  VAL A C    1 
ATOM   96   O O    . VAL A 1 89  ? 104.14300 131.06600 114.73000 1.000 33.57499  ? 89  VAL A O    1 
ATOM   97   C CB   . VAL A 1 89  ? 103.49300 132.93000 112.13900 1.000 28.40927  ? 89  VAL A CB   1 
ATOM   98   C CG1  . VAL A 1 89  ? 102.28100 132.93600 113.05700 1.000 28.39490  ? 89  VAL A CG1  1 
ATOM   99   C CG2  . VAL A 1 89  ? 103.70400 134.30000 111.51800 1.000 20.23768  ? 89  VAL A CG2  1 
ATOM   100  N N    . PHE A 1 90  ? 104.85000 130.04500 112.85300 1.000 14.78847  ? 90  PHE A N    1 
ATOM   101  C CA   . PHE A 1 90  ? 104.75000 128.70800 113.43000 1.000 15.94844  ? 90  PHE A CA   1 
ATOM   102  C C    . PHE A 1 90  ? 105.71500 128.53700 114.60100 1.000 18.42507  ? 90  PHE A C    1 
ATOM   103  O O    . PHE A 1 90  ? 105.35100 127.98500 115.65100 1.000 24.78789  ? 90  PHE A O    1 
ATOM   104  C CB   . PHE A 1 90  ? 105.02400 127.67700 112.33100 1.000 12.12741  ? 90  PHE A CB   1 
ATOM   105  C CG   . PHE A 1 90  ? 104.83200 126.25100 112.75800 1.000 25.09186  ? 90  PHE A CG   1 
ATOM   106  C CD1  . PHE A 1 90  ? 103.57200 125.76700 113.05500 1.000 20.19464  ? 90  PHE A CD1  1 
ATOM   107  C CD2  . PHE A 1 90  ? 105.91000 125.38700 112.83700 1.000 15.40068  ? 90  PHE A CD2  1 
ATOM   108  C CE1  . PHE A 1 90  ? 103.39400 124.45600 113.43800 1.000 14.14960  ? 90  PHE A CE1  1 
ATOM   109  C CE2  . PHE A 1 90  ? 105.73500 124.07600 113.22100 1.000 10.83386  ? 90  PHE A CE2  1 
ATOM   110  C CZ   . PHE A 1 90  ? 104.47600 123.61000 113.52100 1.000 11.16747  ? 90  PHE A CZ   1 
ATOM   111  N N    . SER A 1 91  ? 106.94800 129.02700 114.44600 1.000 11.37624  ? 91  SER A N    1 
ATOM   112  C CA   . SER A 1 91  ? 107.93300 128.92500 115.51700 1.000 11.28178  ? 91  SER A CA   1 
ATOM   113  C C    . SER A 1 91  ? 107.51200 129.72900 116.74100 1.000 15.97993  ? 91  SER A C    1 
ATOM   114  O O    . SER A 1 91  ? 107.63300 129.25500 117.87900 1.000 26.85863  ? 91  SER A O    1 
ATOM   115  C CB   . SER A 1 91  ? 109.29700 129.39300 115.01200 1.000 15.11972  ? 91  SER A CB   1 
ATOM   116  O OG   . SER A 1 91  ? 109.62100 128.77500 113.78100 1.000 14.24772  ? 91  SER A OG   1 
ATOM   117  N N    . ALA A 1 92  ? 107.00500 130.94500 116.53200 1.000 10.36417  ? 92  ALA A N    1 
ATOM   118  C CA   . ALA A 1 92  ? 106.54500 131.74100 117.66200 1.000 9.14580   ? 92  ALA A CA   1 
ATOM   119  C C    . ALA A 1 92  ? 105.28100 131.17100 118.28900 1.000 17.20529  ? 92  ALA A C    1 
ATOM   120  O O    . ALA A 1 92  ? 105.06800 131.34700 119.49100 1.000 25.97673  ? 92  ALA A O    1 
ATOM   121  C CB   . ALA A 1 92  ? 106.31100 133.18700 117.22700 1.000 11.73658  ? 92  ALA A CB   1 
ATOM   122  N N    . LYS A 1 93  ? 104.48300 130.41800 117.53100 1.000 11.51371  ? 93  LYS A N    1 
ATOM   123  C CA   . LYS A 1 93  ? 103.31100 129.78400 118.11900 1.000 8.42864   ? 93  LYS A CA   1 
ATOM   124  C C    . LYS A 1 93  ? 103.69500 128.57700 118.96200 1.000 10.24704  ? 93  LYS A C    1 
ATOM   125  O O    . LYS A 1 93  ? 103.08200 128.33100 120.01200 1.000 26.19590  ? 93  LYS A O    1 
ATOM   126  C CB   . LYS A 1 93  ? 102.34300 129.37400 117.00900 1.000 22.19219  ? 93  LYS A CB   1 
ATOM   127  C CG   . LYS A 1 93  ? 101.30200 130.42500 116.66600 1.000 20.89603  ? 93  LYS A CG   1 
ATOM   128  C CD   . LYS A 1 93  ? 100.72800 130.20100 115.27700 1.000 12.54859  ? 93  LYS A CD   1 
ATOM   129  C CE   . LYS A 1 93  ? 100.24700 128.77700 115.09200 1.000 12.76947  ? 93  LYS A CE   1 
ATOM   130  N NZ   . LYS A 1 93  ? 99.13100  128.70000 114.11400 1.000 15.49080  ? 93  LYS A NZ   1 
ATOM   131  N N    . ILE A 1 94  ? 104.77100 127.88600 118.58600 1.000 6.66535   ? 94  ILE A N    1 
ATOM   132  C CA   . ILE A 1 94  ? 105.21500 126.78500 119.43200 1.000 8.83865   ? 94  ILE A CA   1 
ATOM   133  C C    . ILE A 1 94  ? 105.94000 127.32500 120.65800 1.000 24.65887  ? 94  ILE A C    1 
ATOM   134  O O    . ILE A 1 94  ? 105.81800 126.76300 121.75600 1.000 32.86020  ? 94  ILE A O    1 
ATOM   135  C CB   . ILE A 1 94  ? 106.11000 125.81800 118.63900 1.000 16.43528  ? 94  ILE A CB   1 
ATOM   136  C CG1  . ILE A 1 94  ? 105.41600 125.37900 117.35100 1.000 18.41582  ? 94  ILE A CG1  1 
ATOM   137  C CG2  . ILE A 1 94  ? 106.49000 124.61600 119.49000 1.000 13.51527  ? 94  ILE A CG2  1 
ATOM   138  C CD1  . ILE A 1 94  ? 106.05700 124.18100 116.69700 1.000 14.62907  ? 94  ILE A CD1  1 
ATOM   139  N N    . GLY A 1 95  ? 106.60400 128.47400 120.52700 1.000 14.48503  ? 95  GLY A N    1 
ATOM   140  C CA   . GLY A 1 95  ? 107.18600 129.10400 121.69900 1.000 6.91029   ? 95  GLY A CA   1 
ATOM   141  C C    . GLY A 1 95  ? 106.12600 129.61500 122.65600 1.000 18.48624  ? 95  GLY A C    1 
ATOM   142  O O    . GLY A 1 95  ? 106.28100 129.51900 123.87600 1.000 24.02985  ? 95  GLY A O    1 
ATOM   143  N N    . LEU A 1 96  ? 105.01300 130.12100 122.11800 1.000 15.64445  ? 96  LEU A N    1 
ATOM   144  C CA   . LEU A 1 96  ? 103.93000 130.60200 122.97000 1.000 13.25936  ? 96  LEU A CA   1 
ATOM   145  C C    . LEU A 1 96  ? 103.24900 129.45600 123.70900 1.000 17.58764  ? 96  LEU A C    1 
ATOM   146  O O    . LEU A 1 96  ? 102.99000 129.55700 124.91500 1.000 28.26113  ? 96  LEU A O    1 
ATOM   147  C CB   . LEU A 1 96  ? 102.91600 131.38000 122.13200 1.000 19.82432  ? 96  LEU A CB   1 
ATOM   148  C CG   . LEU A 1 96  ? 101.63500 131.83500 122.83400 1.000 29.09525  ? 96  LEU A CG   1 
ATOM   149  C CD1  . LEU A 1 96  ? 101.92400 132.98600 123.78600 1.000 26.83709  ? 96  LEU A CD1  1 
ATOM   150  C CD2  . LEU A 1 96  ? 100.57600 132.22700 121.81900 1.000 12.10162  ? 96  LEU A CD2  1 
ATOM   151  N N    . ALA A 1 97  ? 102.96000 128.35100 123.01400 1.000 13.77743  ? 97  ALA A N    1 
ATOM   152  C CA   . ALA A 1 97  ? 102.36900 127.20500 123.70100 1.000 20.19334  ? 97  ALA A CA   1 
ATOM   153  C C    . ALA A 1 97  ? 103.30300 126.66300 124.78000 1.000 24.52986  ? 97  ALA A C    1 
ATOM   154  O O    . ALA A 1 97  ? 102.86800 126.35000 125.90200 1.000 18.12485  ? 97  ALA A O    1 
ATOM   155  C CB   . ALA A 1 97  ? 102.01900 126.11100 122.69400 1.000 14.92475  ? 97  ALA A CB   1 
ATOM   156  N N    . LEU A 1 98  ? 104.59900 126.56200 124.46600 1.000 25.52580  ? 98  LEU A N    1 
ATOM   157  C CA   . LEU A 1 98  ? 105.54600 126.04100 125.44300 1.000 17.65680  ? 98  LEU A CA   1 
ATOM   158  C C    . LEU A 1 98  ? 105.63700 126.95600 126.65700 1.000 19.82044  ? 98  LEU A C    1 
ATOM   159  O O    . LEU A 1 98  ? 105.65800 126.48300 127.79900 1.000 27.83279  ? 98  LEU A O    1 
ATOM   160  C CB   . LEU A 1 98  ? 106.91600 125.87000 124.78900 1.000 20.53769  ? 98  LEU A CB   1 
ATOM   161  C CG   . LEU A 1 98  ? 107.28200 124.46600 124.30200 1.000 19.42741  ? 98  LEU A CG   1 
ATOM   162  C CD1  . LEU A 1 98  ? 108.61700 124.48900 123.57500 1.000 18.89208  ? 98  LEU A CD1  1 
ATOM   163  C CD2  . LEU A 1 98  ? 107.29700 123.46600 125.43900 1.000 21.21415  ? 98  LEU A CD2  1 
ATOM   164  N N    . THR A 1 99  ? 105.68100 128.27300 126.43200 1.000 22.67586  ? 99  THR A N    1 
ATOM   165  C CA   . THR A 1 99  ? 105.73500 129.21900 127.54100 1.000 22.08792  ? 99  THR A CA   1 
ATOM   166  C C    . THR A 1 99  ? 104.47200 129.17300 128.39300 1.000 27.89529  ? 99  THR A C    1 
ATOM   167  O O    . THR A 1 99  ? 104.54900 129.31700 129.61900 1.000 34.93478  ? 99  THR A O    1 
ATOM   168  C CB   . THR A 1 99  ? 105.96400 130.63400 127.01000 1.000 26.08943  ? 99  THR A CB   1 
ATOM   169  O OG1  . THR A 1 99  ? 107.35800 130.82600 126.74700 1.000 33.63669  ? 99  THR A OG1  1 
ATOM   170  C CG2  . THR A 1 99  ? 105.50200 131.66600 128.02200 1.000 29.27496  ? 99  THR A CG2  1 
ATOM   171  N N    . ILE A 1 100 ? 103.30900 128.94600 127.77900 1.000 26.39264  ? 100 ILE A N    1 
ATOM   172  C CA   . ILE A 1 100 ? 102.08000 128.86800 128.56500 1.000 30.43283  ? 100 ILE A CA   1 
ATOM   173  C C    . ILE A 1 100 ? 102.11100 127.64500 129.47400 1.000 35.74758  ? 100 ILE A C    1 
ATOM   174  O O    . ILE A 1 100 ? 101.79400 127.72700 130.67000 1.000 34.09345  ? 100 ILE A O    1 
ATOM   175  C CB   . ILE A 1 100 ? 100.84500 128.85100 127.64700 1.000 29.11623  ? 100 ILE A CB   1 
ATOM   176  C CG1  . ILE A 1 100 ? 100.63600 130.21700 126.99300 1.000 28.93019  ? 100 ILE A CG1  1 
ATOM   177  C CG2  . ILE A 1 100 ? 99.60800  128.43900 128.42700 1.000 24.73682  ? 100 ILE A CG2  1 
ATOM   178  C CD1  . ILE A 1 100 ? 99.63400  130.19900 125.86200 1.000 30.69012  ? 100 ILE A CD1  1 
ATOM   179  N N    . VAL A 1 101 ? 102.51000 126.49400 128.92700 1.000 31.66835  ? 101 VAL A N    1 
ATOM   180  C CA   . VAL A 1 101 ? 102.57600 125.29700 129.76400 1.000 25.14713  ? 101 VAL A CA   1 
ATOM   181  C C    . VAL A 1 101 ? 103.62500 125.46700 130.85900 1.000 28.73673  ? 101 VAL A C    1 
ATOM   182  O O    . VAL A 1 101 ? 103.42500 125.04300 132.00600 1.000 25.88218  ? 101 VAL A O    1 
ATOM   183  C CB   . VAL A 1 101 ? 102.84200 124.04800 128.90600 1.000 24.57286  ? 101 VAL A CB   1 
ATOM   184  C CG1  . VAL A 1 101 ? 103.23500 122.88100 129.78900 1.000 19.58078  ? 101 VAL A CG1  1 
ATOM   185  C CG2  . VAL A 1 101 ? 101.60800 123.69900 128.09600 1.000 21.76463  ? 101 VAL A CG2  1 
ATOM   186  N N    . ALA A 1 102 ? 104.75100 126.10900 130.53400 1.000 36.90411  ? 102 ALA A N    1 
ATOM   187  C CA   . ALA A 1 102 ? 105.80000 126.30000 131.52900 1.000 32.55076  ? 102 ALA A CA   1 
ATOM   188  C C    . ALA A 1 102 ? 105.32900 127.19700 132.66500 1.000 35.75424  ? 102 ALA A C    1 
ATOM   189  O O    . ALA A 1 102 ? 105.62700 126.93500 133.83700 1.000 41.38115  ? 102 ALA A O    1 
ATOM   190  C CB   . ALA A 1 102 ? 107.05000 126.88100 130.87000 1.000 30.97163  ? 102 ALA A CB   1 
ATOM   191  N N    . LEU A 1 103 ? 104.60200 128.26900 132.34300 1.000 38.82510  ? 103 LEU A N    1 
ATOM   192  C CA   . LEU A 1 103 ? 104.08500 129.13300 133.39900 1.000 39.37077  ? 103 LEU A CA   1 
ATOM   193  C C    . LEU A 1 103 ? 103.06200 128.40000 134.25500 1.000 43.99527  ? 103 LEU A C    1 
ATOM   194  O O    . LEU A 1 103 ? 103.06000 128.53700 135.48600 1.000 45.15892  ? 103 LEU A O    1 
ATOM   195  C CB   . LEU A 1 103 ? 103.47600 130.39800 132.79900 1.000 40.27579  ? 103 LEU A CB   1 
ATOM   196  C CG   . LEU A 1 103 ? 104.45100 131.52700 132.46400 1.000 41.42215  ? 103 LEU A CG   1 
ATOM   197  C CD1  . LEU A 1 103 ? 103.70500 132.72900 131.91100 1.000 40.50071  ? 103 LEU A CD1  1 
ATOM   198  C CD2  . LEU A 1 103 ? 105.25900 131.91300 133.69000 1.000 40.56979  ? 103 LEU A CD2  1 
ATOM   199  N N    . LEU A 1 104 ? 102.20000 127.59400 133.62700 1.000 53.11228  ? 104 LEU A N    1 
ATOM   200  C CA   . LEU A 1 104 ? 101.21000 126.85100 134.39900 1.000 46.38200  ? 104 LEU A CA   1 
ATOM   201  C C    . LEU A 1 104 ? 101.84900 125.77900 135.26900 1.000 46.05749  ? 104 LEU A C    1 
ATOM   202  O O    . LEU A 1 104 ? 101.25000 125.37300 136.27000 1.000 44.63278  ? 104 LEU A O    1 
ATOM   203  C CB   . LEU A 1 104 ? 100.17700 126.21200 133.47300 1.000 45.08296  ? 104 LEU A CB   1 
ATOM   204  C CG   . LEU A 1 104 ? 98.92800  127.03700 133.16500 1.000 47.69155  ? 104 LEU A CG   1 
ATOM   205  C CD1  . LEU A 1 104 ? 98.34500  126.63500 131.82200 1.000 48.39093  ? 104 LEU A CD1  1 
ATOM   206  C CD2  . LEU A 1 104 ? 97.90000  126.87500 134.26900 1.000 47.11690  ? 104 LEU A CD2  1 
ATOM   207  N N    . ILE A 1 105 ? 103.04900 125.31800 134.91700 1.000 50.79872  ? 105 ILE A N    1 
ATOM   208  C CA   . ILE A 1 105 ? 103.72500 124.33200 135.75400 1.000 52.09821  ? 105 ILE A CA   1 
ATOM   209  C C    . ILE A 1 105 ? 104.49100 125.01100 136.88300 1.000 45.93288  ? 105 ILE A C    1 
ATOM   210  O O    . ILE A 1 105 ? 104.50200 124.52400 138.01800 1.000 50.26344  ? 105 ILE A O    1 
ATOM   211  C CB   . ILE A 1 105 ? 104.64700 123.44200 134.90100 1.000 51.28123  ? 105 ILE A CB   1 
ATOM   212  C CG1  . ILE A 1 105 ? 103.84500 122.32500 134.23200 1.000 44.25085  ? 105 ILE A CG1  1 
ATOM   213  C CG2  . ILE A 1 105 ? 105.76800 122.86700 135.75100 1.000 46.00520  ? 105 ILE A CG2  1 
ATOM   214  C CD1  . ILE A 1 105 ? 104.60200 121.60500 133.14300 1.000 43.30675  ? 105 ILE A CD1  1 
ATOM   215  N N    . PHE A 1 106 ? 105.14600 126.13700 136.59600 1.000 52.68782  ? 106 PHE A N    1 
ATOM   216  C CA   . PHE A 1 106 ? 105.87000 126.85100 137.64400 1.000 52.28358  ? 106 PHE A CA   1 
ATOM   217  C C    . PHE A 1 106 ? 104.92400 127.40900 138.70100 1.000 54.54050  ? 106 PHE A C    1 
ATOM   218  O O    . PHE A 1 106 ? 105.21100 127.32100 139.90100 1.000 57.80366  ? 106 PHE A O    1 
ATOM   219  C CB   . PHE A 1 106 ? 106.71700 127.97100 137.03900 1.000 50.92731  ? 106 PHE A CB   1 
ATOM   220  C CG   . PHE A 1 106 ? 107.99200 127.49300 136.40700 1.000 53.61974  ? 106 PHE A CG   1 
ATOM   221  C CD1  . PHE A 1 106 ? 108.63700 126.36600 136.88500 1.000 55.71349  ? 106 PHE A CD1  1 
ATOM   222  C CD2  . PHE A 1 106 ? 108.54700 128.17100 135.33600 1.000 51.51682  ? 106 PHE A CD2  1 
ATOM   223  C CE1  . PHE A 1 106 ? 109.81100 125.92400 136.30700 1.000 52.78053  ? 106 PHE A CE1  1 
ATOM   224  C CE2  . PHE A 1 106 ? 109.72000 127.73300 134.75400 1.000 51.57408  ? 106 PHE A CE2  1 
ATOM   225  C CZ   . PHE A 1 106 ? 110.35200 126.60800 135.24000 1.000 49.58077  ? 106 PHE A CZ   1 
ATOM   226  N N    . TYR A 1 107 ? 103.79700 127.98300 138.28800 1.000 65.01336  ? 107 TYR A N    1 
ATOM   227  C CA   . TYR A 1 107 ? 102.87800 128.64900 139.21400 1.000 65.25958  ? 107 TYR A CA   1 
ATOM   228  C C    . TYR A 1 107 ? 101.64500 127.77300 139.43100 1.000 69.22932  ? 107 TYR A C    1 
ATOM   229  O O    . TYR A 1 107 ? 100.63200 127.91800 138.74400 1.000 67.66365  ? 107 TYR A O    1 
ATOM   230  C CB   . TYR A 1 107 ? 102.48600 130.03400 138.70200 1.000 63.60953  ? 107 TYR A CB   1 
ATOM   231  C CG   . TYR A 1 107 ? 103.65500 130.96700 138.48400 1.000 64.87725  ? 107 TYR A CG   1 
ATOM   232  C CD1  . TYR A 1 107 ? 104.42800 131.40100 139.55100 1.000 65.78135  ? 107 TYR A CD1  1 
ATOM   233  C CD2  . TYR A 1 107 ? 103.97900 131.42100 137.21400 1.000 66.61824  ? 107 TYR A CD2  1 
ATOM   234  C CE1  . TYR A 1 107 ? 105.49500 132.25500 139.35900 1.000 65.66668  ? 107 TYR A CE1  1 
ATOM   235  C CE2  . TYR A 1 107 ? 105.04400 132.27600 137.01200 1.000 66.25795  ? 107 TYR A CE2  1 
ATOM   236  C CZ   . TYR A 1 107 ? 105.79800 132.69000 138.08800 1.000 66.37259  ? 107 TYR A CZ   1 
ATOM   237  O OH   . TYR A 1 107 ? 106.85900 133.54200 137.89100 1.000 68.94351  ? 107 TYR A OH   1 
ATOM   238  N N    . GLN A 1 108 ? 101.73900 126.86100 140.39700 1.000 80.30994  ? 108 GLN A N    1 
ATOM   239  C CA   . GLN A 1 108 ? 100.61100 126.02000 140.77400 1.000 81.21796  ? 108 GLN A CA   1 
ATOM   240  C C    . GLN A 1 108 ? 100.75600 125.64100 142.24000 1.000 84.07391  ? 108 GLN A C    1 
ATOM   241  O O    . GLN A 1 108 ? 101.84400 125.72500 142.81700 1.000 82.40301  ? 108 GLN A O    1 
ATOM   242  C CB   . GLN A 1 108 ? 100.51700 124.76800 139.89400 1.000 77.79455  ? 108 GLN A CB   1 
ATOM   243  C CG   . GLN A 1 108 ? 100.96800 123.48600 140.57500 1.000 79.67911  ? 108 GLN A CG   1 
ATOM   244  C CD   . GLN A 1 108 ? 102.47600 123.35300 140.62900 1.000 81.13275  ? 108 GLN A CD   1 
ATOM   245  O OE1  . GLN A 1 108 ? 103.19300 124.34500 140.75400 1.000 79.52010  ? 108 GLN A OE1  1 
ATOM   246  N NE2  . GLN A 1 108 ? 102.96500 122.12300 140.53000 1.000 79.40317  ? 108 GLN A NE2  1 
ATOM   247  N N    . GLU A 1 109 ? 99.64700  125.22100 142.83900 1.000 98.73507  ? 109 GLU A N    1 
ATOM   248  C CA   . GLU A 1 109 ? 99.67300  124.81200 144.23900 1.000 98.08502  ? 109 GLU A CA   1 
ATOM   249  C C    . GLU A 1 109 ? 100.47800 123.52600 144.39600 1.000 97.52314  ? 109 GLU A C    1 
ATOM   250  O O    . GLU A 1 109 ? 100.22900 122.55200 143.67500 1.000 94.74635  ? 109 GLU A O    1 
ATOM   251  C CB   . GLU A 1 109 ? 98.25300  124.61700 144.76300 1.000 96.71388  ? 109 GLU A CB   1 
ATOM   252  C CG   . GLU A 1 109 ? 98.13000  124.70500 146.27600 1.000 96.23757  ? 109 GLU A CG   1 
ATOM   253  C CD   . GLU A 1 109 ? 98.57700  123.43500 146.97300 1.000 97.93998  ? 109 GLU A CD   1 
ATOM   254  O OE1  . GLU A 1 109 ? 98.14900  122.34100 146.54900 1.000 98.06945  ? 109 GLU A OE1  1 
ATOM   255  O OE2  . GLU A 1 109 ? 99.35700  123.53100 147.94400 1.000 97.69123  ? 109 GLU A OE2  1 
ATOM   256  N N    . PRO A 1 110 ? 101.43900 123.47800 145.31700 1.000 100.49887 ? 110 PRO A N    1 
ATOM   257  C CA   . PRO A 1 110 ? 102.26300 122.27200 145.45700 1.000 100.40223 ? 110 PRO A CA   1 
ATOM   258  C C    . PRO A 1 110 ? 101.45700 121.08800 145.97000 1.000 101.50953 ? 110 PRO A C    1 
ATOM   259  O O    . PRO A 1 110 ? 100.55800 121.23700 146.80100 1.000 100.44904 ? 110 PRO A O    1 
ATOM   260  C CB   . PRO A 1 110 ? 103.33800 122.69400 146.46700 1.000 99.91776  ? 110 PRO A CB   1 
ATOM   261  C CG   . PRO A 1 110 ? 102.71200 123.81600 147.23100 1.000 99.50975  ? 110 PRO A CG   1 
ATOM   262  C CD   . PRO A 1 110 ? 101.85900 124.54700 146.23800 1.000 99.31660  ? 110 PRO A CD   1 
ATOM   263  N N    . ASN A 1 111 ? 101.79000 119.90200 145.46600 1.000 102.38070 ? 111 ASN A N    1 
ATOM   264  C CA   . ASN A 1 111 ? 101.15800 118.66200 145.89200 1.000 100.94752 ? 111 ASN A CA   1 
ATOM   265  C C    . ASN A 1 111 ? 102.16800 117.55500 145.62900 1.000 99.96430  ? 111 ASN A C    1 
ATOM   266  O O    . ASN A 1 111 ? 102.98400 117.67500 144.70700 1.000 98.74984  ? 111 ASN A O    1 
ATOM   267  C CB   . ASN A 1 111 ? 99.82300  118.44900 145.14000 1.000 100.24441 ? 111 ASN A CB   1 
ATOM   268  C CG   . ASN A 1 111 ? 99.39500  116.97900 145.00800 1.000 100.18501 ? 111 ASN A CG   1 
ATOM   269  O OD1  . ASN A 1 111 ? 99.76100  116.12100 145.79300 1.000 101.44659 ? 111 ASN A OD1  1 
ATOM   270  N ND2  . ASN A 1 111 ? 98.55400  116.71300 144.02300 1.000 99.23355  ? 111 ASN A ND2  1 
ATOM   271  N N    . PRO A 1 112 ? 102.14800 116.47600 146.41400 1.000 102.33834 ? 112 PRO A N    1 
ATOM   272  C CA   . PRO A 1 112 ? 103.17600 115.43300 146.23400 1.000 102.55032 ? 112 PRO A CA   1 
ATOM   273  C C    . PRO A 1 112 ? 103.17900 114.76600 144.86500 1.000 102.10843 ? 112 PRO A C    1 
ATOM   274  O O    . PRO A 1 112 ? 104.23200 114.71800 144.21700 1.000 102.31696 ? 112 PRO A O    1 
ATOM   275  C CB   . PRO A 1 112 ? 102.86800 114.44800 147.37100 1.000 101.91651 ? 112 PRO A CB   1 
ATOM   276  C CG   . PRO A 1 112 ? 102.22600 115.29100 148.41500 1.000 102.04391 ? 112 PRO A CG   1 
ATOM   277  C CD   . PRO A 1 112 ? 101.41800 116.31000 147.68500 1.000 101.71691 ? 112 PRO A CD   1 
ATOM   278  N N    . ASP A 1 113 ? 102.04200 114.24400 144.39700 1.000 96.41448  ? 113 ASP A N    1 
ATOM   279  C CA   . ASP A 1 113 ? 102.06800 113.46400 143.16100 1.000 96.02968  ? 113 ASP A CA   1 
ATOM   280  C C    . ASP A 1 113 ? 102.39100 114.32000 141.93800 1.000 98.31069  ? 113 ASP A C    1 
ATOM   281  O O    . ASP A 1 113 ? 103.18500 113.90300 141.08800 1.000 96.90833  ? 113 ASP A O    1 
ATOM   282  C CB   . ASP A 1 113 ? 100.73100 112.74900 142.97200 1.000 95.26347  ? 113 ASP A CB   1 
ATOM   283  C CG   . ASP A 1 113 ? 99.55200  113.70000 143.01200 1.000 97.41163  ? 113 ASP A CG   1 
ATOM   284  O OD1  . ASP A 1 113 ? 99.10300  114.04600 144.12500 1.000 98.45809  ? 113 ASP A OD1  1 
ATOM   285  O OD2  . ASP A 1 113 ? 99.07400  114.10200 141.93000 1.000 95.57124  ? 113 ASP A OD2  1 
ATOM   286  N N    . LEU A 1 114 ? 101.79100 115.50800 141.81300 1.000 92.53778  ? 114 LEU A N    1 
ATOM   287  C CA   . LEU A 1 114 ? 102.06400 116.32400 140.63000 1.000 89.54135  ? 114 LEU A CA   1 
ATOM   288  C C    . LEU A 1 114 ? 103.55200 116.61400 140.48100 1.000 88.37150  ? 114 LEU A C    1 
ATOM   289  O O    . LEU A 1 114 ? 104.09900 116.53500 139.37600 1.000 89.32828  ? 114 LEU A O    1 
ATOM   290  C CB   . LEU A 1 114 ? 101.27500 117.63400 140.64600 1.000 90.54486  ? 114 LEU A CB   1 
ATOM   291  C CG   . LEU A 1 114 ? 99.77800  117.61600 140.32500 1.000 90.34180  ? 114 LEU A CG   1 
ATOM   292  C CD1  . LEU A 1 114 ? 98.93700  117.86200 141.54700 1.000 89.94317  ? 114 LEU A CD1  1 
ATOM   293  C CD2  . LEU A 1 114 ? 99.45900  118.64000 139.24400 1.000 89.13408  ? 114 LEU A CD2  1 
ATOM   294  N N    . SER A 1 115 ? 104.21400 116.97700 141.58200 1.000 82.95754  ? 115 SER A N    1 
ATOM   295  C CA   . SER A 1 115 ? 105.60600 117.41700 141.52400 1.000 85.07265  ? 115 SER A CA   1 
ATOM   296  C C    . SER A 1 115 ? 106.47700 116.50800 140.66200 1.000 84.74891  ? 115 SER A C    1 
ATOM   297  O O    . SER A 1 115 ? 107.34000 116.99200 139.92100 1.000 84.83623  ? 115 SER A O    1 
ATOM   298  C CB   . SER A 1 115 ? 106.17600 117.50700 142.94100 1.000 86.29373  ? 115 SER A CB   1 
ATOM   299  O OG   . SER A 1 115 ? 106.11600 116.25300 143.59600 1.000 87.74874  ? 115 SER A OG   1 
ATOM   300  N N    . ARG A 1 116 ? 106.27400 115.19300 140.73800 1.000 74.18357  ? 116 ARG A N    1 
ATOM   301  C CA   . ARG A 1 116 ? 107.14200 114.28300 140.00100 1.000 74.54650  ? 116 ARG A CA   1 
ATOM   302  C C    . ARG A 1 116 ? 106.60300 113.90000 138.62900 1.000 74.94854  ? 116 ARG A C    1 
ATOM   303  O O    . ARG A 1 116 ? 107.37000 113.40100 137.79800 1.000 75.14214  ? 116 ARG A O    1 
ATOM   304  C CB   . ARG A 1 116 ? 107.38000 113.00800 140.81600 1.000 75.29464  ? 116 ARG A CB   1 
ATOM   305  C CG   . ARG A 1 116 ? 108.46300 113.13800 141.87600 1.000 76.66859  ? 116 ARG A CG   1 
ATOM   306  C CD   . ARG A 1 116 ? 109.85100 112.87000 141.31900 1.000 74.82125  ? 116 ARG A CD   1 
ATOM   307  N NE   . ARG A 1 116 ? 109.82500 112.03700 140.12400 1.000 73.91949  ? 116 ARG A NE   1 
ATOM   308  C CZ   . ARG A 1 116 ? 110.90800 111.65600 139.46000 1.000 75.93888  ? 116 ARG A CZ   1 
ATOM   309  N NH1  . ARG A 1 116 ? 112.12000 112.01400 139.85100 1.000 75.90390  ? 116 ARG A NH1  1 
ATOM   310  N NH2  . ARG A 1 116 ? 110.77100 110.90200 138.37300 1.000 75.97872  ? 116 ARG A NH2  1 
ATOM   311  N N    . TYR A 1 117 ? 105.31400 114.11800 138.36600 1.000 68.07544  ? 117 TYR A N    1 
ATOM   312  C CA   . TYR A 1 117 ? 104.70800 113.77100 137.08500 1.000 66.67482  ? 117 TYR A CA   1 
ATOM   313  C C    . TYR A 1 117 ? 104.16500 114.98500 136.34300 1.000 65.50694  ? 117 TYR A C    1 
ATOM   314  O O    . TYR A 1 117 ? 103.25700 114.84300 135.52000 1.000 69.33614  ? 117 TYR A O    1 
ATOM   315  C CB   . TYR A 1 117 ? 103.60800 112.72100 137.26500 1.000 65.70686  ? 117 TYR A CB   1 
ATOM   316  C CG   . TYR A 1 117 ? 103.88100 111.72500 138.36600 1.000 68.80307  ? 117 TYR A CG   1 
ATOM   317  C CD1  . TYR A 1 117 ? 105.08700 111.03600 138.41700 1.000 69.06149  ? 117 TYR A CD1  1 
ATOM   318  C CD2  . TYR A 1 117 ? 102.93300 111.45900 139.34200 1.000 68.57022  ? 117 TYR A CD2  1 
ATOM   319  C CE1  . TYR A 1 117 ? 105.34500 110.12100 139.41600 1.000 69.07377  ? 117 TYR A CE1  1 
ATOM   320  C CE2  . TYR A 1 117 ? 103.18200 110.54300 140.34600 1.000 71.63255  ? 117 TYR A CE2  1 
ATOM   321  C CZ   . TYR A 1 117 ? 104.39000 109.87700 140.37700 1.000 72.34192  ? 117 TYR A CZ   1 
ATOM   322  O OH   . TYR A 1 117 ? 104.64800 108.96300 141.37300 1.000 72.22748  ? 117 TYR A OH   1 
ATOM   323  N N    . SER A 1 118 ? 104.69700 116.17500 136.60600 1.000 52.80946  ? 118 SER A N    1 
ATOM   324  C CA   . SER A 1 118 ? 104.16400 117.38200 135.99100 1.000 48.58961  ? 118 SER A CA   1 
ATOM   325  C C    . SER A 1 118 ? 104.90300 117.76500 134.71900 1.000 45.64102  ? 118 SER A C    1 
ATOM   326  O O    . SER A 1 118 ? 104.42100 118.62500 133.97500 1.000 49.55196  ? 118 SER A O    1 
ATOM   327  C CB   . SER A 1 118 ? 104.20800 118.54900 136.98200 1.000 55.05492  ? 118 SER A CB   1 
ATOM   328  O OG   . SER A 1 118 ? 105.54300 118.87000 137.32600 1.000 60.67071  ? 118 SER A OG   1 
ATOM   329  N N    . VAL A 1 119 ? 106.05600 117.14400 134.45100 1.000 37.51347  ? 119 VAL A N    1 
ATOM   330  C CA   . VAL A 1 119 ? 106.80600 117.40200 133.22400 1.000 39.14407  ? 119 VAL A CA   1 
ATOM   331  C C    . VAL A 1 119 ? 106.20800 116.67800 132.03000 1.000 38.83733  ? 119 VAL A C    1 
ATOM   332  O O    . VAL A 1 119 ? 106.67800 116.87000 130.90100 1.000 35.93680  ? 119 VAL A O    1 
ATOM   333  C CB   . VAL A 1 119 ? 108.28400 117.00100 133.40900 1.000 39.63832  ? 119 VAL A CB   1 
ATOM   334  C CG1  . VAL A 1 119 ? 108.41300 115.49200 133.56000 1.000 32.70729  ? 119 VAL A CG1  1 
ATOM   335  C CG2  . VAL A 1 119 ? 109.13100 117.50900 132.25200 1.000 30.64504  ? 119 VAL A CG2  1 
ATOM   336  N N    . TRP A 1 120 ? 105.18100 115.85300 132.24700 1.000 37.79423  ? 120 TRP A N    1 
ATOM   337  C CA   . TRP A 1 120 ? 104.53000 115.09600 131.18600 1.000 34.59140  ? 120 TRP A CA   1 
ATOM   338  C C    . TRP A 1 120 ? 103.65500 115.96000 130.28900 1.000 31.08828  ? 120 TRP A C    1 
ATOM   339  O O    . TRP A 1 120 ? 103.18700 115.46900 129.25700 1.000 27.58986  ? 120 TRP A O    1 
ATOM   340  C CB   . TRP A 1 120 ? 103.67200 113.98400 131.79300 1.000 29.17858  ? 120 TRP A CB   1 
ATOM   341  C CG   . TRP A 1 120 ? 104.44500 112.79500 132.26900 1.000 35.96768  ? 120 TRP A CG   1 
ATOM   342  C CD1  . TRP A 1 120 ? 105.34400 112.76100 133.29200 1.000 37.12924  ? 120 TRP A CD1  1 
ATOM   343  C CD2  . TRP A 1 120 ? 104.36900 111.46000 131.75800 1.000 35.57659  ? 120 TRP A CD2  1 
ATOM   344  N NE1  . TRP A 1 120 ? 105.84300 111.49300 133.44200 1.000 39.83374  ? 120 TRP A NE1  1 
ATOM   345  C CE2  . TRP A 1 120 ? 105.25900 110.67300 132.51400 1.000 37.71025  ? 120 TRP A CE2  1 
ATOM   346  C CE3  . TRP A 1 120 ? 103.63800 110.85400 130.73200 1.000 37.95235  ? 120 TRP A CE3  1 
ATOM   347  C CZ2  . TRP A 1 120 ? 105.43900 109.31300 132.27700 1.000 34.68502  ? 120 TRP A CZ2  1 
ATOM   348  C CZ3  . TRP A 1 120 ? 103.81800 109.50300 130.49900 1.000 39.87171  ? 120 TRP A CZ3  1 
ATOM   349  C CH2  . TRP A 1 120 ? 104.71100 108.74800 131.26800 1.000 35.75592  ? 120 TRP A CH2  1 
ATOM   350  N N    . ALA A 1 121 ? 103.42400 117.22100 130.64900 1.000 27.10329  ? 121 ALA A N    1 
ATOM   351  C CA   . ALA A 1 121 ? 102.58500 118.10900 129.85500 1.000 21.55289  ? 121 ALA A CA   1 
ATOM   352  C C    . ALA A 1 121 ? 103.37200 119.01000 128.91600 1.000 23.10795  ? 121 ALA A C    1 
ATOM   353  O O    . ALA A 1 121 ? 102.87000 119.34900 127.84100 1.000 25.85373  ? 121 ALA A O    1 
ATOM   354  C CB   . ALA A 1 121 ? 101.71700 118.97700 130.77200 1.000 15.20207  ? 121 ALA A CB   1 
ATOM   355  N N    . ILE A 1 122 ? 104.59200 119.40700 129.28700 1.000 19.66164  ? 122 ILE A N    1 
ATOM   356  C CA   . ILE A 1 122 ? 105.42200 120.20000 128.38200 1.000 16.90924  ? 122 ILE A CA   1 
ATOM   357  C C    . ILE A 1 122 ? 106.08600 119.35600 127.30900 1.000 16.68325  ? 122 ILE A C    1 
ATOM   358  O O    . ILE A 1 122 ? 106.61000 119.91000 126.33600 1.000 19.71869  ? 122 ILE A O    1 
ATOM   359  C CB   . ILE A 1 122 ? 106.50000 120.98100 129.15600 1.000 22.64030  ? 122 ILE A CB   1 
ATOM   360  C CG1  . ILE A 1 122 ? 107.18100 122.00100 128.24100 1.000 20.95941  ? 122 ILE A CG1  1 
ATOM   361  C CG2  . ILE A 1 122 ? 107.52500 120.03400 129.75200 1.000 22.20264  ? 122 ILE A CG2  1 
ATOM   362  C CD1  . ILE A 1 122 ? 107.44300 123.33500 128.89500 1.000 19.43130  ? 122 ILE A CD1  1 
ATOM   363  N N    . LEU A 1 123 ? 106.07000 118.03200 127.45000 1.000 22.92419  ? 123 LEU A N    1 
ATOM   364  C CA   . LEU A 1 123 ? 106.67200 117.14900 126.46400 1.000 17.59942  ? 123 LEU A CA   1 
ATOM   365  C C    . LEU A 1 123 ? 105.67800 116.66500 125.41800 1.000 23.16166  ? 123 LEU A C    1 
ATOM   366  O O    . LEU A 1 123 ? 106.09800 116.14400 124.37900 1.000 25.43233  ? 123 LEU A O    1 
ATOM   367  C CB   . LEU A 1 123 ? 107.31700 115.94500 127.15900 1.000 21.01059  ? 123 LEU A CB   1 
ATOM   368  C CG   . LEU A 1 123 ? 108.53400 116.23300 128.04400 1.000 26.25438  ? 123 LEU A CG   1 
ATOM   369  C CD1  . LEU A 1 123 ? 109.27000 114.95300 128.38600 1.000 19.74808  ? 123 LEU A CD1  1 
ATOM   370  C CD2  . LEU A 1 123 ? 109.47800 117.22800 127.38600 1.000 26.75466  ? 123 LEU A CD2  1 
ATOM   371  N N    . THR A 1 124 ? 104.37500 116.81700 125.67000 1.000 24.05163  ? 124 THR A N    1 
ATOM   372  C CA   . THR A 1 124 ? 103.36400 116.48000 124.67400 1.000 13.25434  ? 124 THR A CA   1 
ATOM   373  C C    . THR A 1 124 ? 103.23800 117.56500 123.61000 1.000 17.33899  ? 124 THR A C    1 
ATOM   374  O O    . THR A 1 124 ? 102.93200 117.26300 122.44700 1.000 21.15551  ? 124 THR A O    1 
ATOM   375  C CB   . THR A 1 124 ? 102.01200 116.25600 125.35600 1.000 13.60983  ? 124 THR A CB   1 
ATOM   376  O OG1  . THR A 1 124 ? 102.10200 115.13500 126.24300 1.000 25.43392  ? 124 THR A OG1  1 
ATOM   377  C CG2  . THR A 1 124 ? 100.93200 115.98300 124.32500 1.000 15.70687  ? 124 THR A CG2  1 
ATOM   378  N N    . VAL A 1 125 ? 103.48000 118.82100 123.99100 1.000 16.94837  ? 125 VAL A N    1 
ATOM   379  C CA   . VAL A 1 125 ? 103.44400 119.92200 123.03400 1.000 12.60853  ? 125 VAL A CA   1 
ATOM   380  C C    . VAL A 1 125 ? 104.51000 119.72700 121.96700 1.000 13.13093  ? 125 VAL A C    1 
ATOM   381  O O    . VAL A 1 125 ? 104.29000 120.01500 120.78600 1.000 20.65863  ? 125 VAL A O    1 
ATOM   382  C CB   . VAL A 1 125 ? 103.61600 121.26700 123.76500 1.000 13.94672  ? 125 VAL A CB   1 
ATOM   383  C CG1  . VAL A 1 125 ? 103.68400 122.41400 122.76900 1.000 16.60220  ? 125 VAL A CG1  1 
ATOM   384  C CG2  . VAL A 1 125 ? 102.49200 121.47900 124.76300 1.000 15.94232  ? 125 VAL A CG2  1 
ATOM   385  N N    . VAL A 1 126 ? 105.68400 119.23300 122.36700 1.000 13.90379  ? 126 VAL A N    1 
ATOM   386  C CA   . VAL A 1 126 ? 106.77800 119.01800 121.43000 1.000 15.59769  ? 126 VAL A CA   1 
ATOM   387  C C    . VAL A 1 126 ? 106.54100 117.82900 120.51500 1.000 18.67386  ? 126 VAL A C    1 
ATOM   388  O O    . VAL A 1 126 ? 107.26300 117.66500 119.52600 1.000 24.31424  ? 126 VAL A O    1 
ATOM   389  C CB   . VAL A 1 126 ? 108.10200 118.82500 122.19700 1.000 13.43259  ? 126 VAL A CB   1 
ATOM   390  C CG1  . VAL A 1 126 ? 109.27100 118.71300 121.23400 1.000 17.14114  ? 126 VAL A CG1  1 
ATOM   391  C CG2  . VAL A 1 126 ? 108.31900 119.96400 123.17500 1.000 11.54230  ? 126 VAL A CG2  1 
ATOM   392  N N    . VAL A 1 127 ? 105.54100 116.99900 120.80700 1.000 21.33290  ? 127 VAL A N    1 
ATOM   393  C CA   . VAL A 1 127 ? 105.29000 115.79000 120.03100 1.000 15.52200  ? 127 VAL A CA   1 
ATOM   394  C C    . VAL A 1 127 ? 103.98000 115.83000 119.25800 1.000 11.37235  ? 127 VAL A C    1 
ATOM   395  O O    . VAL A 1 127 ? 103.77200 114.96600 118.39100 1.000 19.47847  ? 127 VAL A O    1 
ATOM   396  C CB   . VAL A 1 127 ? 105.33400 114.53200 120.92700 1.000 21.80087  ? 127 VAL A CB   1 
ATOM   397  C CG1  . VAL A 1 127 ? 105.14800 113.27000 120.10300 1.000 17.32158  ? 127 VAL A CG1  1 
ATOM   398  C CG2  . VAL A 1 127 ? 106.64100 114.47600 121.70100 1.000 12.48169  ? 127 VAL A CG2  1 
ATOM   399  N N    . VAL A 1 128 ? 103.10100 116.79900 119.51100 1.000 17.70817  ? 128 VAL A N    1 
ATOM   400  C CA   . VAL A 1 128 ? 101.80200 116.83400 118.84700 1.000 14.89583  ? 128 VAL A CA   1 
ATOM   401  C C    . VAL A 1 128 ? 101.59200 118.07100 117.98300 1.000 17.34793  ? 128 VAL A C    1 
ATOM   402  O O    . VAL A 1 128 ? 100.56900 118.16000 117.30000 1.000 22.88345  ? 128 VAL A O    1 
ATOM   403  C CB   . VAL A 1 128 ? 100.64700 116.69200 119.85900 1.000 23.96029  ? 128 VAL A CB   1 
ATOM   404  C CG1  . VAL A 1 128 ? 100.81600 115.42700 120.68200 1.000 15.52297  ? 128 VAL A CG1  1 
ATOM   405  C CG2  . VAL A 1 128 ? 100.56400 117.91900 120.75400 1.000 20.51046  ? 128 VAL A CG2  1 
ATOM   406  N N    . PHE A 1 129 ? 102.52300 119.02100 117.97600 1.000 20.24166  ? 129 PHE A N    1 
ATOM   407  C CA   . PHE A 1 129 ? 102.36300 120.26100 117.21700 1.000 20.20837  ? 129 PHE A CA   1 
ATOM   408  C C    . PHE A 1 129 ? 102.86500 120.04400 115.78900 1.000 18.04526  ? 129 PHE A C    1 
ATOM   409  O O    . PHE A 1 129 ? 104.06400 119.84400 115.57200 1.000 24.91703  ? 129 PHE A O    1 
ATOM   410  C CB   . PHE A 1 129 ? 103.12000 121.39300 117.90800 1.000 19.30886  ? 129 PHE A CB   1 
ATOM   411  C CG   . PHE A 1 129 ? 102.46400 122.74200 117.78200 1.000 19.45168  ? 129 PHE A CG   1 
ATOM   412  C CD1  . PHE A 1 129 ? 102.39900 123.39300 116.56300 1.000 22.07543  ? 129 PHE A CD1  1 
ATOM   413  C CD2  . PHE A 1 129 ? 101.92300 123.36400 118.89400 1.000 12.39839  ? 129 PHE A CD2  1 
ATOM   414  C CE1  . PHE A 1 129 ? 101.80200 124.63600 116.45600 1.000 17.75206  ? 129 PHE A CE1  1 
ATOM   415  C CE2  . PHE A 1 129 ? 101.32400 124.60600 118.79100 1.000 14.99966  ? 129 PHE A CE2  1 
ATOM   416  C CZ   . PHE A 1 129 ? 101.26400 125.24100 117.57100 1.000 6.33643   ? 129 PHE A CZ   1 
ATOM   417  N N    . GLU A 1 130 ? 101.95500 120.09300 114.81600 1.000 22.89817  ? 130 GLU A N    1 
ATOM   418  C CA   . GLU A 1 130 ? 102.28300 119.89900 113.40700 1.000 21.45700  ? 130 GLU A CA   1 
ATOM   419  C C    . GLU A 1 130 ? 101.99100 121.15500 112.59300 1.000 27.19414  ? 130 GLU A C    1 
ATOM   420  O O    . GLU A 1 130 ? 101.37200 122.11100 113.06600 1.000 27.99745  ? 130 GLU A O    1 
ATOM   421  C CB   . GLU A 1 130 ? 101.52600 118.70100 112.81700 1.000 17.49003  ? 130 GLU A CB   1 
ATOM   422  C CG   . GLU A 1 130 ? 101.34400 117.55000 113.78200 1.000 24.85726  ? 130 GLU A CG   1 
ATOM   423  C CD   . GLU A 1 130 ? 102.40700 116.48300 113.61200 1.000 30.39689  ? 130 GLU A CD   1 
ATOM   424  O OE1  . GLU A 1 130 ? 103.05100 116.44700 112.54400 1.000 35.76731  ? 130 GLU A OE1  1 
ATOM   425  O OE2  . GLU A 1 130 ? 102.61000 115.68900 114.55200 1.000 31.44603  ? 130 GLU A OE2  1 
ATOM   426  N N    . PHE A 1 131 ? 102.44300 121.12400 111.33500 1.000 20.00958  ? 131 PHE A N    1 
ATOM   427  C CA   . PHE A 1 131 ? 102.33800 122.28200 110.45000 1.000 15.35617  ? 131 PHE A CA   1 
ATOM   428  C C    . PHE A 1 131 ? 100.89000 122.62400 110.10700 1.000 19.31576  ? 131 PHE A C    1 
ATOM   429  O O    . PHE A 1 131 ? 100.52500 123.80400 110.06000 1.000 15.09479  ? 131 PHE A O    1 
ATOM   430  C CB   . PHE A 1 131 ? 103.14400 122.02800 109.17600 1.000 15.08198  ? 131 PHE A CB   1 
ATOM   431  C CG   . PHE A 1 131 ? 103.73600 123.26800 108.57300 1.000 24.08463  ? 131 PHE A CG   1 
ATOM   432  C CD1  . PHE A 1 131 ? 104.77100 123.93500 109.19900 1.000 18.36926  ? 131 PHE A CD1  1 
ATOM   433  C CD2  . PHE A 1 131 ? 103.26000 123.76100 107.36900 1.000 25.98716  ? 131 PHE A CD2  1 
ATOM   434  C CE1  . PHE A 1 131 ? 105.31300 125.07500 108.64400 1.000 18.68110  ? 131 PHE A CE1  1 
ATOM   435  C CE2  . PHE A 1 131 ? 103.80000 124.89900 106.81000 1.000 21.58688  ? 131 PHE A CE2  1 
ATOM   436  C CZ   . PHE A 1 131 ? 104.82700 125.55700 107.45000 1.000 22.04187  ? 131 PHE A CZ   1 
ATOM   437  N N    . THR A 1 132 ? 100.05800 121.61900 109.84900 1.000 27.21066  ? 132 THR A N    1 
ATOM   438  C CA   . THR A 1 132 ? 98.66800  121.82600 109.46700 1.000 11.44691  ? 132 THR A CA   1 
ATOM   439  C C    . THR A 1 132 ? 97.72600  121.28500 110.53700 1.000 13.37469  ? 132 THR A C    1 
ATOM   440  O O    . THR A 1 132 ? 98.11400  120.49200 111.39700 1.000 19.51407  ? 132 THR A O    1 
ATOM   441  C CB   . THR A 1 132 ? 98.35900  121.16400 108.11700 1.000 15.88538  ? 132 THR A CB   1 
ATOM   442  O OG1  . THR A 1 132 ? 98.69300  119.77200 108.17000 1.000 26.52227  ? 132 THR A OG1  1 
ATOM   443  C CG2  . THR A 1 132 ? 99.14500  121.82800 106.99800 1.000 7.94790   ? 132 THR A CG2  1 
ATOM   444  N N    . ILE A 1 133 ? 96.47400  121.74300 110.47900 1.000 10.54154  ? 133 ILE A N    1 
ATOM   445  C CA   . ILE A 1 133 ? 95.46700  121.29000 111.43400 1.000 11.90193  ? 133 ILE A CA   1 
ATOM   446  C C    . ILE A 1 133 ? 95.04200  119.85500 111.14000 1.000 13.50769  ? 133 ILE A C    1 
ATOM   447  O O    . ILE A 1 133 ? 94.83100  119.05300 112.06200 1.000 23.18474  ? 133 ILE A O    1 
ATOM   448  C CB   . ILE A 1 133 ? 94.25900  122.24600 111.41900 1.000 22.36990  ? 133 ILE A CB   1 
ATOM   449  C CG1  . ILE A 1 133 ? 94.72400  123.69700 111.28500 1.000 16.39007  ? 133 ILE A CG1  1 
ATOM   450  C CG2  . ILE A 1 133 ? 93.41300  122.06300 112.66600 1.000 21.90849  ? 133 ILE A CG2  1 
ATOM   451  C CD1  . ILE A 1 133 ? 95.17100  124.31900 112.58200 1.000 15.35866  ? 133 ILE A CD1  1 
ATOM   452  N N    . GLY A 1 134 ? 94.89200  119.52800 109.86100 1.000 11.62618  ? 134 GLY A N    1 
ATOM   453  C CA   . GLY A 1 134 ? 94.46200  118.19100 109.48800 1.000 3.73512   ? 134 GLY A CA   1 
ATOM   454  C C    . GLY A 1 134 ? 95.36800  117.11700 110.04700 1.000 13.82501  ? 134 GLY A C    1 
ATOM   455  O O    . GLY A 1 134 ? 94.91400  116.22700 110.76700 1.000 30.95189  ? 134 GLY A O    1 
ATOM   456  N N    . ALA A 1 135 ? 96.65300  117.19700 109.72300 1.000 4.05172   ? 135 ALA A N    1 
ATOM   457  C CA   . ALA A 1 135 ? 97.60200  116.20800 110.21300 1.000 4.13622   ? 135 ALA A CA   1 
ATOM   458  C C    . ALA A 1 135 ? 97.56900  116.17400 111.72600 1.000 13.85018  ? 135 ALA A C    1 
ATOM   459  O O    . ALA A 1 135 ? 97.50000  115.10200 112.32600 1.000 24.89243  ? 135 ALA A O    1 
ATOM   460  C CB   . ALA A 1 135 ? 99.00100  116.53200 109.72400 1.000 6.55393   ? 135 ALA A CB   1 
ATOM   461  N N    . THR A 1 136 ? 97.61000  117.34700 112.34600 1.000 12.82109  ? 136 THR A N    1 
ATOM   462  C CA   . THR A 1 136 ? 97.55700  117.41700 113.79700 1.000 16.67596  ? 136 THR A CA   1 
ATOM   463  C C    . THR A 1 136 ? 96.43400  116.53300 114.30600 1.000 14.74198  ? 136 THR A C    1 
ATOM   464  O O    . THR A 1 136 ? 96.62400  115.76600 115.24900 1.000 13.53772  ? 136 THR A O    1 
ATOM   465  C CB   . THR A 1 136 ? 97.34400  118.86000 114.28400 1.000 13.34636  ? 136 THR A CB   1 
ATOM   466  O OG1  . THR A 1 136 ? 98.43300  119.67900 113.84200 1.000 17.44781  ? 136 THR A OG1  1 
ATOM   467  C CG2  . THR A 1 136 ? 97.27100  118.90600 115.80000 1.000 14.10556  ? 136 THR A CG2  1 
ATOM   468  N N    . LEU A 1 137 ? 95.26800  116.60900 113.67500 1.000 7.77012   ? 137 LEU A N    1 
ATOM   469  C CA   . LEU A 1 137 ? 94.12000  115.80300 114.08000 1.000 3.54147   ? 137 LEU A CA   1 
ATOM   470  C C    . LEU A 1 137 ? 94.33600  114.32900 113.75900 1.000 11.11386  ? 137 LEU A C    1 
ATOM   471  O O    . LEU A 1 137 ? 94.12200  113.45900 114.61400 1.000 24.37631  ? 137 LEU A O    1 
ATOM   472  C CB   . LEU A 1 137 ? 92.85300  116.32500 113.40400 1.000 11.05183  ? 137 LEU A CB   1 
ATOM   473  C CG   . LEU A 1 137 ? 92.49200  117.78100 113.69700 1.000 12.06762  ? 137 LEU A CG   1 
ATOM   474  C CD1  . LEU A 1 137 ? 91.64700  118.36100 112.57700 1.000 14.85304  ? 137 LEU A CD1  1 
ATOM   475  C CD2  . LEU A 1 137 ? 91.77000  117.89400 115.02600 1.000 5.09281   ? 137 LEU A CD2  1 
ATOM   476  N N    . SER A 1 138 ? 94.78300  114.02500 112.53700 1.000 3.73414   ? 138 SER A N    1 
ATOM   477  C CA   . SER A 1 138 ? 94.97500  112.63000 112.14900 1.000 11.10530  ? 138 SER A CA   1 
ATOM   478  C C    . SER A 1 138 ? 96.00900  111.94200 113.03500 1.000 18.63767  ? 138 SER A C    1 
ATOM   479  O O    . SER A 1 138 ? 95.76400  110.85300 113.58200 1.000 24.73699  ? 138 SER A O    1 
ATOM   480  C CB   . SER A 1 138 ? 95.39600  112.55500 110.68200 1.000 11.48572  ? 138 SER A CB   1 
ATOM   481  O OG   . SER A 1 138 ? 94.36800  113.02000 109.83100 1.000 27.93071  ? 138 SER A OG   1 
ATOM   482  N N    . LYS A 1 139 ? 97.18500  112.55800 113.17800 1.000 7.95175   ? 139 LYS A N    1 
ATOM   483  C CA   . LYS A 1 139 ? 98.24400  111.92700 113.95000 1.000 5.96793   ? 139 LYS A CA   1 
ATOM   484  C C    . LYS A 1 139 ? 97.87900  111.82800 115.42500 1.000 12.68672  ? 139 LYS A C    1 
ATOM   485  O O    . LYS A 1 139 ? 98.20500  110.82700 116.07500 1.000 28.58152  ? 139 LYS A O    1 
ATOM   486  C CB   . LYS A 1 139 ? 99.55600  112.67800 113.74400 1.000 17.17427  ? 139 LYS A CB   1 
ATOM   487  C CG   . LYS A 1 139 ? 100.17400 112.39600 112.38600 1.000 5.94088   ? 139 LYS A CG   1 
ATOM   488  C CD   . LYS A 1 139 ? 100.94500 113.57400 111.84700 1.000 11.19420  ? 139 LYS A CD   1 
ATOM   489  C CE   . LYS A 1 139 ? 102.23700 113.11400 111.20700 1.000 17.59793  ? 139 LYS A CE   1 
ATOM   490  N NZ   . LYS A 1 139 ? 103.15700 112.50300 112.20300 1.000 22.38091  ? 139 LYS A NZ   1 
ATOM   491  N N    . GLY A 1 140 ? 97.19400  112.83400 115.97900 1.000 7.21354   ? 140 GLY A N    1 
ATOM   492  C CA   . GLY A 1 140 ? 96.77800  112.72500 117.36400 1.000 6.57295   ? 140 GLY A CA   1 
ATOM   493  C C    . GLY A 1 140 ? 95.75600  111.63000 117.57500 1.000 14.00047  ? 140 GLY A C    1 
ATOM   494  O O    . GLY A 1 140 ? 95.77700  110.94900 118.60600 1.000 20.10739  ? 140 GLY A O    1 
ATOM   495  N N    . PHE A 1 141 ? 94.91200  111.39200 116.58400 1.000 9.45996   ? 141 PHE A N    1 
ATOM   496  C CA   . PHE A 1 141 ? 93.94400  110.30900 116.67500 1.000 10.69035  ? 141 PHE A CA   1 
ATOM   497  C C    . PHE A 1 141 ? 94.61300  108.94900 116.71000 1.000 14.88148  ? 141 PHE A C    1 
ATOM   498  O O    . PHE A 1 141 ? 94.27100  108.11000 117.53600 1.000 21.53246  ? 141 PHE A O    1 
ATOM   499  C CB   . PHE A 1 141 ? 92.99800  110.36700 115.48800 1.000 9.34498   ? 141 PHE A CB   1 
ATOM   500  C CG   . PHE A 1 141 ? 92.00000  109.25300 115.45900 1.000 14.95932  ? 141 PHE A CG   1 
ATOM   501  C CD1  . PHE A 1 141 ? 90.83600  109.33600 116.19400 1.000 11.69604  ? 141 PHE A CD1  1 
ATOM   502  C CD2  . PHE A 1 141 ? 92.23100  108.11900 114.70300 1.000 21.10261  ? 141 PHE A CD2  1 
ATOM   503  C CE1  . PHE A 1 141 ? 89.91500  108.31000 116.17700 1.000 15.20400  ? 141 PHE A CE1  1 
ATOM   504  C CE2  . PHE A 1 141 ? 91.31400  107.08900 114.67900 1.000 15.26416  ? 141 PHE A CE2  1 
ATOM   505  C CZ   . PHE A 1 141 ? 90.15400  107.18400 115.41800 1.000 15.99634  ? 141 PHE A CZ   1 
ATOM   506  N N    . ASN A 1 142 ? 95.56100  108.72400 115.81200 1.000 11.46925  ? 142 ASN A N    1 
ATOM   507  C CA   . ASN A 1 142 ? 96.27400  107.45500 115.76100 1.000 1.72808   ? 142 ASN A CA   1 
ATOM   508  C C    . ASN A 1 142 ? 97.12700  107.23400 116.99500 1.000 14.35672  ? 142 ASN A C    1 
ATOM   509  O O    . ASN A 1 142 ? 97.25900  106.10800 117.45900 1.000 28.24294  ? 142 ASN A O    1 
ATOM   510  C CB   . ASN A 1 142 ? 97.14100  107.39800 114.51300 1.000 10.51155  ? 142 ASN A CB   1 
ATOM   511  C CG   . ASN A 1 142 ? 96.32700  107.40800 113.23800 1.000 21.72915  ? 142 ASN A CG   1 
ATOM   512  O OD1  . ASN A 1 142 ? 95.11000  107.24100 113.26300 1.000 23.03589  ? 142 ASN A OD1  1 
ATOM   513  N ND2  . ASN A 1 142 ? 97.00000  107.59800 112.11200 1.000 16.10813  ? 142 ASN A ND2  1 
ATOM   514  N N    . ARG A 1 143 ? 97.71300  108.29900 117.52800 1.000 10.66950  ? 143 ARG A N    1 
ATOM   515  C CA   . ARG A 1 143 ? 98.51100  108.18900 118.74100 1.000 8.66714   ? 143 ARG A CA   1 
ATOM   516  C C    . ARG A 1 143 ? 97.64200  107.89200 119.95700 1.000 10.16272  ? 143 ARG A C    1 
ATOM   517  O O    . ARG A 1 143 ? 98.03700  107.11700 120.81000 1.000 17.72149  ? 143 ARG A O    1 
ATOM   518  C CB   . ARG A 1 143 ? 99.32400  109.45900 118.98200 1.000 13.20955  ? 143 ARG A CB   1 
ATOM   519  C CG   . ARG A 1 143 ? 100.37500 109.77900 117.93700 1.000 10.83730  ? 143 ARG A CG   1 
ATOM   520  C CD   . ARG A 1 143 ? 101.22100 110.95600 118.39500 1.000 12.84516  ? 143 ARG A CD   1 
ATOM   521  N NE   . ARG A 1 143 ? 102.21800 111.35400 117.40700 1.000 20.31843  ? 143 ARG A NE   1 
ATOM   522  C CZ   . ARG A 1 143 ? 102.07400 112.37100 116.56300 1.000 21.01692  ? 143 ARG A CZ   1 
ATOM   523  N NH1  . ARG A 1 143 ? 100.97300 113.10700 116.58700 1.000 17.08160  ? 143 ARG A NH1  1 
ATOM   524  N NH2  . ARG A 1 143 ? 103.03800 112.65800 115.69900 1.000 12.15795  ? 143 ARG A NH2  1 
ATOM   525  N N    . ALA A 1 144 ? 96.46100  108.49200 120.04700 1.000 15.13063  ? 144 ALA A N    1 
ATOM   526  C CA   . ALA A 1 144 ? 95.56300  108.17700 121.15000 1.000 12.95644  ? 144 ALA A CA   1 
ATOM   527  C C    . ALA A 1 144 ? 95.07000  106.74100 121.06000 1.000 19.15662  ? 144 ALA A C    1 
ATOM   528  O O    . ALA A 1 144 ? 94.94700  106.05700 122.08400 1.000 20.80519  ? 144 ALA A O    1 
ATOM   529  C CB   . ALA A 1 144 ? 94.38700  109.15200 121.16500 1.000 15.19806  ? 144 ALA A CB   1 
ATOM   530  N N    . LEU A 1 145 ? 94.81600  106.25100 119.84300 1.000 18.52607  ? 145 LEU A N    1 
ATOM   531  C CA   . LEU A 1 145 ? 94.37900  104.86500 119.70900 1.000 17.95059  ? 145 LEU A CA   1 
ATOM   532  C C    . LEU A 1 145 ? 95.47000  103.90500 120.16200 1.000 21.77260  ? 145 LEU A C    1 
ATOM   533  O O    . LEU A 1 145 ? 95.20400  102.95600 120.91600 1.000 34.47757  ? 145 LEU A O    1 
ATOM   534  C CB   . LEU A 1 145 ? 93.98400  104.56800 118.26300 1.000 19.91549  ? 145 LEU A CB   1 
ATOM   535  C CG   . LEU A 1 145 ? 92.62000  105.04800 117.77100 1.000 27.69141  ? 145 LEU A CG   1 
ATOM   536  C CD1  . LEU A 1 145 ? 92.12700  104.15000 116.65200 1.000 18.95233  ? 145 LEU A CD1  1 
ATOM   537  C CD2  . LEU A 1 145 ? 91.61700  105.08500 118.91200 1.000 25.50815  ? 145 LEU A CD2  1 
ATOM   538  N N    . GLY A 1 146 ? 96.71400  104.16700 119.75500 1.000 17.36847  ? 146 GLY A N    1 
ATOM   539  C CA   . GLY A 1 146 ? 97.80700  103.31300 120.19100 1.000 5.65817   ? 146 GLY A CA   1 
ATOM   540  C C    . GLY A 1 146 ? 97.98900  103.33100 121.69600 1.000 14.87133  ? 146 GLY A C    1 
ATOM   541  O O    . GLY A 1 146 ? 98.13000  102.28200 122.33300 1.000 24.54304  ? 146 GLY A O    1 
ATOM   542  N N    . THR A 1 147 ? 97.95500  104.52600 122.29100 1.000 20.02703  ? 147 THR A N    1 
ATOM   543  C CA   . THR A 1 147 ? 98.15100  104.63700 123.73200 1.000 18.42298  ? 147 THR A CA   1 
ATOM   544  C C    . THR A 1 147 ? 97.05800  103.90200 124.49800 1.000 21.70359  ? 147 THR A C    1 
ATOM   545  O O    . THR A 1 147 ? 97.34100  103.16100 125.44600 1.000 28.16316  ? 147 THR A O    1 
ATOM   546  C CB   . THR A 1 147 ? 98.19800  106.10800 124.14300 1.000 20.19719  ? 147 THR A CB   1 
ATOM   547  O OG1  . THR A 1 147 ? 99.03100  106.83300 123.23100 1.000 30.84373  ? 147 THR A OG1  1 
ATOM   548  C CG2  . THR A 1 147 ? 98.75300  106.25100 125.54800 1.000 22.25807  ? 147 THR A CG2  1 
ATOM   549  N N    . LEU A 1 148 ? 95.79700  104.08800 124.09800 1.000 25.07876  ? 148 LEU A N    1 
ATOM   550  C CA   . LEU A 1 148 ? 94.70800  103.49500 124.86600 1.000 24.53934  ? 148 LEU A CA   1 
ATOM   551  C C    . LEU A 1 148 ? 94.68600  101.97800 124.71800 1.000 24.43523  ? 148 LEU A C    1 
ATOM   552  O O    . LEU A 1 148 ? 94.46300  101.25600 125.70100 1.000 29.19314  ? 148 LEU A O    1 
ATOM   553  C CB   . LEU A 1 148 ? 93.37400  104.10300 124.43400 1.000 29.96418  ? 148 LEU A CB   1 
ATOM   554  C CG   . LEU A 1 148 ? 92.93900  105.35600 125.19900 1.000 32.14268  ? 148 LEU A CG   1 
ATOM   555  C CD1  . LEU A 1 148 ? 92.11800  106.27400 124.30800 1.000 29.65786  ? 148 LEU A CD1  1 
ATOM   556  C CD2  . LEU A 1 148 ? 92.16100  104.98500 126.44700 1.000 31.47457  ? 148 LEU A CD2  1 
ATOM   557  N N    . SER A 1 149 ? 94.96300  101.46700 123.51300 1.000 25.75677  ? 149 SER A N    1 
ATOM   558  C CA   . SER A 1 149 ? 95.00800  100.01800 123.35300 1.000 25.48874  ? 149 SER A CA   1 
ATOM   559  C C    . SER A 1 149 ? 96.15600  99.41100  124.15200 1.000 29.18906  ? 149 SER A C    1 
ATOM   560  O O    . SER A 1 149 ? 95.97200  98.39600  124.84200 1.000 35.54826  ? 149 SER A O    1 
ATOM   561  C CB   . SER A 1 149 ? 95.12200  99.65500  121.87300 1.000 18.25021  ? 149 SER A CB   1 
ATOM   562  O OG   . SER A 1 149 ? 96.15700  100.38600 121.24300 1.000 28.54710  ? 149 SER A OG   1 
ATOM   563  N N    . ALA A 1 150 ? 97.34300  100.02500 124.09100 1.000 24.67701  ? 150 ALA A N    1 
ATOM   564  C CA   . ALA A 1 150 ? 98.47600  99.49500  124.83900 1.000 18.49436  ? 150 ALA A CA   1 
ATOM   565  C C    . ALA A 1 150 ? 98.21400  99.52500  126.33800 1.000 23.34892  ? 150 ALA A C    1 
ATOM   566  O O    . ALA A 1 150 ? 98.54600  98.57200  127.05100 1.000 24.77905  ? 150 ALA A O    1 
ATOM   567  C CB   . ALA A 1 150 ? 99.74300  100.27700 124.50000 1.000 18.24202  ? 150 ALA A CB   1 
ATOM   568  N N    . GLY A 1 151 ? 97.60800  100.60400 126.83800 1.000 33.22457  ? 151 GLY A N    1 
ATOM   569  C CA   . GLY A 1 151 ? 97.33000  100.68300 128.26200 1.000 30.12601  ? 151 GLY A CA   1 
ATOM   570  C C    . GLY A 1 151 ? 96.31300  99.65900  128.72600 1.000 29.66397  ? 151 GLY A C    1 
ATOM   571  O O    . GLY A 1 151 ? 96.49200  99.02500  129.77200 1.000 32.64972  ? 151 GLY A O    1 
ATOM   572  N N    . GLY A 1 152 ? 95.24900  99.45500  127.94600 1.000 28.82343  ? 152 GLY A N    1 
ATOM   573  C CA   . GLY A 1 152 ? 94.27700  98.44200  128.32200 1.000 27.59446  ? 152 GLY A CA   1 
ATOM   574  C C    . GLY A 1 152 ? 94.87000  97.04700  128.32200 1.000 34.46096  ? 152 GLY A C    1 
ATOM   575  O O    . GLY A 1 152 ? 94.63700  96.25700  129.24600 1.000 37.27918  ? 152 GLY A O    1 
ATOM   576  N N    . LEU A 1 153 ? 95.67900  96.73400  127.30500 1.000 30.12556  ? 153 LEU A N    1 
ATOM   577  C CA   . LEU A 1 153 ? 96.30200  95.41700  127.24900 1.000 23.19133  ? 153 LEU A CA   1 
ATOM   578  C C    . LEU A 1 153 ? 97.26500  95.21500  128.41300 1.000 28.03128  ? 153 LEU A C    1 
ATOM   579  O O    . LEU A 1 153 ? 97.28300  94.14700  129.03900 1.000 34.93876  ? 153 LEU A O    1 
ATOM   580  C CB   . LEU A 1 153 ? 97.01900  95.23500  125.91300 1.000 31.42647  ? 153 LEU A CB   1 
ATOM   581  C CG   . LEU A 1 153 ? 97.79100  93.93200  125.70600 1.000 33.53201  ? 153 LEU A CG   1 
ATOM   582  C CD1  . LEU A 1 153 ? 96.84900  92.74300  125.74000 1.000 29.54930  ? 153 LEU A CD1  1 
ATOM   583  C CD2  . LEU A 1 153 ? 98.55900  93.97300  124.39800 1.000 28.71306  ? 153 LEU A CD2  1 
ATOM   584  N N    . ALA A 1 154 ? 98.08700  96.22500  128.71100 1.000 32.17008  ? 154 ALA A N    1 
ATOM   585  C CA   . ALA A 1 154 ? 99.02600  96.10500  129.81900 1.000 30.36857  ? 154 ALA A CA   1 
ATOM   586  C C    . ALA A 1 154 ? 98.29800  95.89300  131.13800 1.000 32.81814  ? 154 ALA A C    1 
ATOM   587  O O    . ALA A 1 154 ? 98.70400  95.05400  131.94800 1.000 39.20488  ? 154 ALA A O    1 
ATOM   588  C CB   . ALA A 1 154 ? 99.92200  97.34100  129.89200 1.000 26.40988  ? 154 ALA A CB   1 
ATOM   589  N N    . LEU A 1 155 ? 97.22200  96.64700  131.37800 1.000 40.37576  ? 155 LEU A N    1 
ATOM   590  C CA   . LEU A 1 155 ? 96.49600  96.48400  132.63400 1.000 41.57583  ? 155 LEU A CA   1 
ATOM   591  C C    . LEU A 1 155 ? 95.87600  95.09500  132.73700 1.000 46.05049  ? 155 LEU A C    1 
ATOM   592  O O    . LEU A 1 155 ? 95.93300  94.45600  133.79700 1.000 47.29561  ? 155 LEU A O    1 
ATOM   593  C CB   . LEU A 1 155 ? 95.42600  97.56600  132.77000 1.000 37.54930  ? 155 LEU A CB   1 
ATOM   594  C CG   . LEU A 1 155 ? 95.89200  98.84600  133.46300 1.000 37.93884  ? 155 LEU A CG   1 
ATOM   595  C CD1  . LEU A 1 155 ? 95.02100  100.02400 133.06700 1.000 42.66803  ? 155 LEU A CD1  1 
ATOM   596  C CD2  . LEU A 1 155 ? 95.90100  98.66300  134.96700 1.000 43.77049  ? 155 LEU A CD2  1 
ATOM   597  N N    . GLY A 1 156 ? 95.29300  94.60100  131.64200 1.000 42.22329  ? 156 GLY A N    1 
ATOM   598  C CA   . GLY A 1 156 ? 94.72000  93.26400  131.67500 1.000 40.44134  ? 156 GLY A CA   1 
ATOM   599  C C    . GLY A 1 156 ? 95.75400  92.18400  131.93900 1.000 45.24532  ? 156 GLY A C    1 
ATOM   600  O O    . GLY A 1 156 ? 95.52500  91.27200  132.74100 1.000 48.05090  ? 156 GLY A O    1 
ATOM   601  N N    . MET A 1 157 ? 96.91200  92.27600  131.28000 1.000 54.29141  ? 157 MET A N    1 
ATOM   602  C CA   . MET A 1 157 ? 97.95800  91.28200  131.50700 1.000 53.27467  ? 157 MET A CA   1 
ATOM   603  C C    . MET A 1 157 ? 98.52400  91.37500  132.91900 1.000 50.96100  ? 157 MET A C    1 
ATOM   604  O O    . MET A 1 157 ? 98.84200  90.35000  133.53400 1.000 50.68406  ? 157 MET A O    1 
ATOM   605  C CB   . MET A 1 157 ? 99.06700  91.44200  130.46900 1.000 49.03919  ? 157 MET A CB   1 
ATOM   606  C CG   . MET A 1 157 ? 99.63600  90.12800  129.96900 1.000 51.29927  ? 157 MET A CG   1 
ATOM   607  S SD   . MET A 1 157 ? 98.66500  89.41000  128.62900 1.000 64.92315  ? 157 MET A SD   1 
ATOM   608  C CE   . MET A 1 157 ? 98.81600  90.68000  127.37700 1.000 52.69705  ? 157 MET A CE   1 
ATOM   609  N N    . ALA A 1 158 ? 98.64300  92.58900  133.45900 1.000 52.81109  ? 158 ALA A N    1 
ATOM   610  C CA   . ALA A 1 158 ? 99.11500  92.73600  134.83000 1.000 51.91321  ? 158 ALA A CA   1 
ATOM   611  C C    . ALA A 1 158 ? 98.13800  92.10900  135.81100 1.000 55.33689  ? 158 ALA A C    1 
ATOM   612  O O    . ALA A 1 158 ? 98.54800  91.49500  136.80300 1.000 57.36843  ? 158 ALA A O    1 
ATOM   613  C CB   . ALA A 1 158 ? 99.33200  94.21100  135.15800 1.000 54.61784  ? 158 ALA A CB   1 
ATOM   614  N N    . GLU A 1 159 ? 96.83800  92.26000  135.55600 1.000 59.87890  ? 159 GLU A N    1 
ATOM   615  C CA   . GLU A 1 159 ? 95.84700  91.59400  136.39400 1.000 57.32172  ? 159 GLU A CA   1 
ATOM   616  C C    . GLU A 1 159 ? 95.99000  90.08000  136.30200 1.000 59.13155  ? 159 GLU A C    1 
ATOM   617  O O    . GLU A 1 159 ? 96.01700  89.38100  137.32100 1.000 58.65193  ? 159 GLU A O    1 
ATOM   618  C CB   . GLU A 1 159 ? 94.43900  92.02800  135.98900 1.000 60.19053  ? 159 GLU A CB   1 
ATOM   619  C CG   . GLU A 1 159 ? 93.46100  92.12000  137.14900 1.000 61.15741  ? 159 GLU A CG   1 
ATOM   620  C CD   . GLU A 1 159 ? 93.57300  93.42700  137.90400 1.000 62.21959  ? 159 GLU A CD   1 
ATOM   621  O OE1  . GLU A 1 159 ? 94.37700  93.49700  138.85700 1.000 62.81155  ? 159 GLU A OE1  1 
ATOM   622  O OE2  . GLU A 1 159 ? 92.85900  94.38600  137.54200 1.000 59.52903  ? 159 GLU A OE2  1 
ATOM   623  N N    . LEU A 1 160 ? 96.08600  89.55400  135.07900 1.000 63.80854  ? 160 LEU A N    1 
ATOM   624  C CA   . LEU A 1 160 ? 96.16200  88.10700  134.89700 1.000 61.76196  ? 160 LEU A CA   1 
ATOM   625  C C    . LEU A 1 160 ? 97.42900  87.51500  135.50900 1.000 63.50744  ? 160 LEU A C    1 
ATOM   626  O O    . LEU A 1 160 ? 97.42600  86.35600  135.93600 1.000 62.10868  ? 160 LEU A O    1 
ATOM   627  C CB   . LEU A 1 160 ? 96.07400  87.77900  133.40300 1.000 62.58068  ? 160 LEU A CB   1 
ATOM   628  C CG   . LEU A 1 160 ? 95.87400  86.35300  132.87700 1.000 65.42306  ? 160 LEU A CG   1 
ATOM   629  C CD1  . LEU A 1 160 ? 95.93100  86.36500  131.35900 1.000 63.29429  ? 160 LEU A CD1  1 
ATOM   630  C CD2  . LEU A 1 160 ? 96.89500  85.37200  133.42100 1.000 66.49411  ? 160 LEU A CD2  1 
ATOM   631  N N    . SER A 1 161 ? 98.51000  88.29600  135.58500 1.000 71.38852  ? 161 SER A N    1 
ATOM   632  C CA   . SER A 1 161 ? 99.78600  87.75900  136.05900 1.000 69.01644  ? 161 SER A CA   1 
ATOM   633  C C    . SER A 1 161 ? 99.68300  87.13500  137.44700 1.000 70.26458  ? 161 SER A C    1 
ATOM   634  O O    . SER A 1 161 ? 100.46600 86.23800  137.77900 1.000 71.09671  ? 161 SER A O    1 
ATOM   635  C CB   . SER A 1 161 ? 100.84800 88.85600  136.06400 1.000 66.54834  ? 161 SER A CB   1 
ATOM   636  O OG   . SER A 1 161 ? 100.68800 89.71300  137.18000 1.000 68.83587  ? 161 SER A OG   1 
ATOM   637  N N    . THR A 1 162 ? 98.74000  87.59400  138.27200 1.000 76.59734  ? 162 THR A N    1 
ATOM   638  C CA   . THR A 1 162 ? 98.67800  87.13500  139.65800 1.000 74.41421  ? 162 THR A CA   1 
ATOM   639  C C    . THR A 1 162 ? 98.48100  85.62600  139.75000 1.000 74.71395  ? 162 THR A C    1 
ATOM   640  O O    . THR A 1 162 ? 99.07500  84.97100  140.61500 1.000 74.32192  ? 162 THR A O    1 
ATOM   641  C CB   . THR A 1 162 ? 97.56200  87.86400  140.40500 1.000 75.18649  ? 162 THR A CB   1 
ATOM   642  O OG1  . THR A 1 162 ? 96.30400  87.59100  139.77700 1.000 76.52160  ? 162 THR A OG1  1 
ATOM   643  C CG2  . THR A 1 162 ? 97.81200  89.36400  140.40400 1.000 73.94230  ? 162 THR A CG2  1 
ATOM   644  N N    . LEU A 1 163 ? 97.63700  85.05800  138.88300 1.000 82.35628  ? 163 LEU A N    1 
ATOM   645  C CA   . LEU A 1 163 ? 97.33300  83.63000  138.95100 1.000 81.47446  ? 163 LEU A CA   1 
ATOM   646  C C    . LEU A 1 163 ? 98.59200  82.78800  139.13100 1.000 83.17032  ? 163 LEU A C    1 
ATOM   647  O O    . LEU A 1 163 ? 98.65000  81.91700  140.00600 1.000 84.22469  ? 163 LEU A O    1 
ATOM   648  C CB   . LEU A 1 163 ? 96.57500  83.19600  137.69500 1.000 82.79926  ? 163 LEU A CB   1 
ATOM   649  C CG   . LEU A 1 163 ? 95.11300  83.63200  137.58600 1.000 83.94892  ? 163 LEU A CG   1 
ATOM   650  C CD1  . LEU A 1 163 ? 95.00600  85.12500  137.32600 1.000 83.15288  ? 163 LEU A CD1  1 
ATOM   651  C CD2  . LEU A 1 163 ? 94.40500  82.84400  136.49600 1.000 83.28241  ? 163 LEU A CD2  1 
ATOM   652  N N    . PHE A 1 164 ? 99.61600  83.03400  138.31200 1.000 86.61541  ? 164 PHE A N    1 
ATOM   653  C CA   . PHE A 1 164 ? 100.90300 82.35100  138.46400 1.000 85.64750  ? 164 PHE A CA   1 
ATOM   654  C C    . PHE A 1 164 ? 101.67600 82.99200  139.61800 1.000 87.26787  ? 164 PHE A C    1 
ATOM   655  O O    . PHE A 1 164 ? 102.65000 83.72600  139.44100 1.000 87.63335  ? 164 PHE A O    1 
ATOM   656  C CB   . PHE A 1 164 ? 101.69300 82.38500  137.16400 1.000 85.38881  ? 164 PHE A CB   1 
ATOM   657  C CG   . PHE A 1 164 ? 100.83500 82.38100  135.93200 1.000 86.80659  ? 164 PHE A CG   1 
ATOM   658  C CD1  . PHE A 1 164 ? 100.04100 81.28700  135.63200 1.000 85.59406  ? 164 PHE A CD1  1 
ATOM   659  C CD2  . PHE A 1 164 ? 100.82500 83.46400  135.07200 1.000 85.89002  ? 164 PHE A CD2  1 
ATOM   660  C CE1  . PHE A 1 164 ? 99.25200  81.27500  134.50000 1.000 86.07793  ? 164 PHE A CE1  1 
ATOM   661  C CE2  . PHE A 1 164 ? 100.03700 83.45700  133.93800 1.000 85.64611  ? 164 PHE A CE2  1 
ATOM   662  C CZ   . PHE A 1 164 ? 99.25000  82.36200  133.65200 1.000 86.46585  ? 164 PHE A CZ   1 
ATOM   663  N N    . GLY A 1 165 ? 101.21000 82.69200  140.83100 1.000 88.34649  ? 165 GLY A N    1 
ATOM   664  C CA   . GLY A 1 165 ? 101.78500 83.31200  142.01300 1.000 88.61842  ? 165 GLY A CA   1 
ATOM   665  C C    . GLY A 1 165 ? 103.27300 83.05700  142.15600 1.000 89.65189  ? 165 GLY A C    1 
ATOM   666  O O    . GLY A 1 165 ? 104.04300 83.97100  142.46000 1.000 87.61161  ? 165 GLY A O    1 
ATOM   667  N N    . ASP A 1 166 ? 103.69900 81.81000  141.94300 1.000 91.11803  ? 166 ASP A N    1 
ATOM   668  C CA   . ASP A 1 166 ? 105.09600 81.46100  142.18100 1.000 90.02247  ? 166 ASP A CA   1 
ATOM   669  C C    . ASP A 1 166 ? 106.03000 82.20300  141.23400 1.000 90.65398  ? 166 ASP A C    1 
ATOM   670  O O    . ASP A 1 166 ? 107.09700 82.67200  141.64800 1.000 89.17293  ? 166 ASP A O    1 
ATOM   671  C CB   . ASP A 1 166 ? 105.28700 79.95000  142.04700 1.000 89.40984  ? 166 ASP A CB   1 
ATOM   672  N N    . TRP A 1 167 ? 105.65500 82.32300  139.96300 1.000 90.87965  ? 167 TRP A N    1 
ATOM   673  C CA   . TRP A 1 167 ? 106.49800 82.96600  138.95500 1.000 89.08385  ? 167 TRP A CA   1 
ATOM   674  C C    . TRP A 1 167 ? 105.73300 84.13300  138.33900 1.000 87.56885  ? 167 TRP A C    1 
ATOM   675  O O    . TRP A 1 167 ? 105.16800 84.02100  137.24900 1.000 88.01548  ? 167 TRP A O    1 
ATOM   676  C CB   . TRP A 1 167 ? 106.94100 81.95400  137.88900 1.000 88.66620  ? 167 TRP A CB   1 
ATOM   677  C CG   . TRP A 1 167 ? 107.17200 80.57500  138.42300 1.000 89.59567  ? 167 TRP A CG   1 
ATOM   678  C CD1  . TRP A 1 167 ? 107.98400 80.22400  139.46200 1.000 89.29261  ? 167 TRP A CD1  1 
ATOM   679  C CD2  . TRP A 1 167 ? 106.59500 79.35800  137.93600 1.000 91.10269  ? 167 TRP A CD2  1 
ATOM   680  N NE1  . TRP A 1 167 ? 107.94300 78.86500  139.65600 1.000 89.98321  ? 167 TRP A NE1  1 
ATOM   681  C CE2  . TRP A 1 167 ? 107.09700 78.31000  138.73200 1.000 90.89235  ? 167 TRP A CE2  1 
ATOM   682  C CE3  . TRP A 1 167 ? 105.69900 79.05300  136.90700 1.000 90.45880  ? 167 TRP A CE3  1 
ATOM   683  C CZ2  . TRP A 1 167 ? 106.73500 76.98000  138.53100 1.000 90.54163  ? 167 TRP A CZ2  1 
ATOM   684  C CZ3  . TRP A 1 167 ? 105.34100 77.73200  136.70900 1.000 90.55976  ? 167 TRP A CZ3  1 
ATOM   685  C CH2  . TRP A 1 167 ? 105.85800 76.71200  137.51700 1.000 89.96860  ? 167 TRP A CH2  1 
ATOM   686  N N    . GLU A 1 168 ? 105.71900 85.26300  139.04800 1.000 79.10426  ? 168 GLU A N    1 
ATOM   687  C CA   . GLU A 1 168 ? 105.10100 86.47200  138.51500 1.000 79.69317  ? 168 GLU A CA   1 
ATOM   688  C C    . GLU A 1 168 ? 106.03500 87.18100  137.54200 1.000 78.27087  ? 168 GLU A C    1 
ATOM   689  O O    . GLU A 1 168 ? 105.64300 87.51500  136.41600 1.000 77.85289  ? 168 GLU A O    1 
ATOM   690  C CB   . GLU A 1 168 ? 104.70800 87.40800  139.65900 1.000 79.99454  ? 168 GLU A CB   1 
ATOM   691  C CG   . GLU A 1 168 ? 103.24300 87.33200  140.05100 1.000 81.01867  ? 168 GLU A CG   1 
ATOM   692  C CD   . GLU A 1 168 ? 102.67000 88.68600  140.41700 1.000 81.96978  ? 168 GLU A CD   1 
ATOM   693  O OE1  . GLU A 1 168 ? 102.92700 89.15700  141.54400 1.000 79.69454  ? 168 GLU A OE1  1 
ATOM   694  O OE2  . GLU A 1 168 ? 101.96300 89.28000  139.57600 1.000 83.35172  ? 168 GLU A OE2  1 
ATOM   695  N N    . GLU A 1 169 ? 107.28100 87.40600  137.96300 1.000 72.22086  ? 169 GLU A N    1 
ATOM   696  C CA   . GLU A 1 169 ? 108.22900 88.12900  137.12700 1.000 70.17793  ? 169 GLU A CA   1 
ATOM   697  C C    . GLU A 1 169 ? 108.58600 87.34300  135.87500 1.000 71.53183  ? 169 GLU A C    1 
ATOM   698  O O    . GLU A 1 169 ? 108.87000 87.94200  134.83500 1.000 73.19362  ? 169 GLU A O    1 
ATOM   699  C CB   . GLU A 1 169 ? 109.48900 88.45800  137.92500 1.000 71.35926  ? 169 GLU A CB   1 
ATOM   700  C CG   . GLU A 1 169 ? 110.03600 87.29000  138.72500 1.000 74.37951  ? 169 GLU A CG   1 
ATOM   701  C CD   . GLU A 1 169 ? 109.47200 87.22900  140.12900 1.000 75.40369  ? 169 GLU A CD   1 
ATOM   702  O OE1  . GLU A 1 169 ? 108.33700 87.70500  140.33500 1.000 75.67638  ? 169 GLU A OE1  1 
ATOM   703  O OE2  . GLU A 1 169 ? 110.16300 86.70300  141.02600 1.000 75.06127  ? 169 GLU A OE2  1 
ATOM   704  N N    . ILE A 1 170 ? 108.54700 86.01200  135.93800 1.000 68.63710  ? 170 ILE A N    1 
ATOM   705  C CA   . ILE A 1 170 ? 108.83100 85.21400  134.74900 1.000 66.85644  ? 170 ILE A CA   1 
ATOM   706  C C    . ILE A 1 170 ? 107.75400 85.43500  133.69500 1.000 66.07021  ? 170 ILE A C    1 
ATOM   707  O O    . ILE A 1 170 ? 108.05000 85.65400  132.51600 1.000 67.50633  ? 170 ILE A O    1 
ATOM   708  C CB   . ILE A 1 170 ? 108.96300 83.72600  135.11800 1.000 68.14159  ? 170 ILE A CB   1 
ATOM   709  C CG1  . ILE A 1 170 ? 110.14900 83.51400  136.06100 1.000 65.64176  ? 170 ILE A CG1  1 
ATOM   710  C CG2  . ILE A 1 170 ? 109.11200 82.87800  133.86600 1.000 66.53150  ? 170 ILE A CG2  1 
ATOM   711  C CD1  . ILE A 1 170 ? 111.41600 84.20400  135.61300 1.000 65.22058  ? 170 ILE A CD1  1 
ATOM   712  N N    . PHE A 1 171 ? 106.48600 85.40800  134.11000 1.000 60.59280  ? 171 PHE A N    1 
ATOM   713  C CA   . PHE A 1 171 ? 105.39200 85.63800  133.17200 1.000 59.46854  ? 171 PHE A CA   1 
ATOM   714  C C    . PHE A 1 171 ? 105.41500 87.06900  132.64500 1.000 60.08366  ? 171 PHE A C    1 
ATOM   715  O O    . PHE A 1 171 ? 105.17300 87.30800  131.45100 1.000 59.81757  ? 171 PHE A O    1 
ATOM   716  C CB   . PHE A 1 171 ? 104.06200 85.31400  133.85700 1.000 59.52148  ? 171 PHE A CB   1 
ATOM   717  C CG   . PHE A 1 171 ? 102.84800 85.79700  133.11500 1.000 63.25492  ? 171 PHE A CG   1 
ATOM   718  C CD1  . PHE A 1 171 ? 102.29200 85.03400  132.10300 1.000 61.66763  ? 171 PHE A CD1  1 
ATOM   719  C CD2  . PHE A 1 171 ? 102.24600 86.99700  133.44900 1.000 63.71209  ? 171 PHE A CD2  1 
ATOM   720  C CE1  . PHE A 1 171 ? 101.16900 85.46900  131.42700 1.000 61.33151  ? 171 PHE A CE1  1 
ATOM   721  C CE2  . PHE A 1 171 ? 101.12400 87.43600  132.77600 1.000 62.21707  ? 171 PHE A CE2  1 
ATOM   722  C CZ   . PHE A 1 171 ? 100.58500 86.67100  131.76400 1.000 62.95664  ? 171 PHE A CZ   1 
ATOM   723  N N    . CYS A 1 172 ? 105.74400 88.03200  133.50900 1.000 55.16508  ? 172 CYS A N    1 
ATOM   724  C CA   . CYS A 1 172 ? 105.77400 89.42100  133.06700 1.000 52.71198  ? 172 CYS A CA   1 
ATOM   725  C C    . CYS A 1 172 ? 106.91700 89.67100  132.08800 1.000 54.07381  ? 172 CYS A C    1 
ATOM   726  O O    . CYS A 1 172 ? 106.75800 90.43400  131.12900 1.000 57.64725  ? 172 CYS A O    1 
ATOM   727  C CB   . CYS A 1 172 ? 105.88400 90.35300  134.27200 1.000 53.78049  ? 172 CYS A CB   1 
ATOM   728  S SG   . CYS A 1 172 ? 104.31100 90.67400  135.10100 1.000 66.76727  ? 172 CYS A SG   1 
ATOM   729  N N    . THR A 1 173 ? 108.07400 89.04100  132.30800 1.000 48.11843  ? 173 THR A N    1 
ATOM   730  C CA   . THR A 1 173 ? 109.18400 89.16100  131.37300 1.000 45.47267  ? 173 THR A CA   1 
ATOM   731  C C    . THR A 1 173 ? 109.00400 88.30100  130.13000 1.000 41.30606  ? 173 THR A C    1 
ATOM   732  O O    . THR A 1 173 ? 109.70200 88.52200  129.13500 1.000 41.93368  ? 173 THR A O    1 
ATOM   733  C CB   . THR A 1 173 ? 110.49900 88.78900  132.06300 1.000 46.47641  ? 173 THR A CB   1 
ATOM   734  O OG1  . THR A 1 173 ? 111.60200 89.23200  131.26500 1.000 46.83821  ? 173 THR A OG1  1 
ATOM   735  C CG2  . THR A 1 173 ? 110.59200 87.28500  132.25300 1.000 50.14791  ? 173 THR A CG2  1 
ATOM   736  N N    . LEU A 1 174 ? 108.09200 87.33000  130.16100 1.000 42.36439  ? 174 LEU A N    1 
ATOM   737  C CA   . LEU A 1 174 ? 107.80000 86.52800  128.98300 1.000 42.76160  ? 174 LEU A CA   1 
ATOM   738  C C    . LEU A 1 174 ? 106.67900 87.11300  128.14000 1.000 44.61594  ? 174 LEU A C    1 
ATOM   739  O O    . LEU A 1 174 ? 106.48700 86.67600  127.00100 1.000 43.25812  ? 174 LEU A O    1 
ATOM   740  C CB   . LEU A 1 174 ? 107.43700 85.09900  129.39600 1.000 41.46269  ? 174 LEU A CB   1 
ATOM   741  C CG   . LEU A 1 174 ? 107.38800 84.05600  128.28000 1.000 45.30258  ? 174 LEU A CG   1 
ATOM   742  C CD1  . LEU A 1 174 ? 108.13900 82.80300  128.69100 1.000 43.17364  ? 174 LEU A CD1  1 
ATOM   743  C CD2  . LEU A 1 174 ? 105.94900 83.72800  127.91500 1.000 45.34107  ? 174 LEU A CD2  1 
ATOM   744  N N    . SER A 1 175 ? 105.93900 88.08700  128.67100 1.000 41.47032  ? 175 SER A N    1 
ATOM   745  C CA   . SER A 1 175 ? 104.93100 88.76200  127.85900 1.000 33.91083  ? 175 SER A CA   1 
ATOM   746  C C    . SER A 1 175 ? 105.54200 89.89400  127.04200 1.000 34.41099  ? 175 SER A C    1 
ATOM   747  O O    . SER A 1 175 ? 105.05900 90.20000  125.94300 1.000 39.46971  ? 175 SER A O    1 
ATOM   748  C CB   . SER A 1 175 ? 103.81100 89.30400  128.74700 1.000 43.34453  ? 175 SER A CB   1 
ATOM   749  O OG   . SER A 1 175 ? 103.15700 88.26100  129.44600 1.000 47.69667  ? 175 SER A OG   1 
ATOM   750  N N    . ILE A 1 176 ? 106.61600 90.49800  127.55500 1.000 34.29833  ? 176 ILE A N    1 
ATOM   751  C CA   . ILE A 1 176 ? 107.31700 91.55200  126.82800 1.000 26.05824  ? 176 ILE A CA   1 
ATOM   752  C C    . ILE A 1 176 ? 107.90800 91.01000  125.53400 1.000 26.01415  ? 176 ILE A C    1 
ATOM   753  O O    . ILE A 1 176 ? 107.85400 91.66900  124.49100 1.000 28.09870  ? 176 ILE A O    1 
ATOM   754  C CB   . ILE A 1 176 ? 108.39500 92.18600  127.72500 1.000 29.00523  ? 176 ILE A CB   1 
ATOM   755  C CG1  . ILE A 1 176 ? 107.73900 92.92000  128.89600 1.000 28.89457  ? 176 ILE A CG1  1 
ATOM   756  C CG2  . ILE A 1 176 ? 109.28600 93.12100  126.92500 1.000 31.41266  ? 176 ILE A CG2  1 
ATOM   757  C CD1  . ILE A 1 176 ? 108.70700 93.34800  129.96600 1.000 27.85225  ? 176 ILE A CD1  1 
ATOM   758  N N    . PHE A 1 177 ? 108.47200 89.80100  125.57700 1.000 24.92063  ? 177 PHE A N    1 
ATOM   759  C CA   . PHE A 1 177 ? 109.03400 89.20100  124.37000 1.000 26.85544  ? 177 PHE A CA   1 
ATOM   760  C C    . PHE A 1 177 ? 107.96700 89.02800  123.29600 1.000 29.68830  ? 177 PHE A C    1 
ATOM   761  O O    . PHE A 1 177 ? 108.16300 89.41800  122.13800 1.000 31.48087  ? 177 PHE A O    1 
ATOM   762  C CB   . PHE A 1 177 ? 109.67800 87.85500  124.71200 1.000 28.26414  ? 177 PHE A CB   1 
ATOM   763  C CG   . PHE A 1 177 ? 110.22400 87.12000  123.52000 1.000 33.97951  ? 177 PHE A CG   1 
ATOM   764  C CD1  . PHE A 1 177 ? 111.48900 87.39700  123.03500 1.000 37.22631  ? 177 PHE A CD1  1 
ATOM   765  C CD2  . PHE A 1 177 ? 109.46800 86.15200  122.88200 1.000 31.56272  ? 177 PHE A CD2  1 
ATOM   766  C CE1  . PHE A 1 177 ? 111.98800 86.72100  121.93700 1.000 31.96352  ? 177 PHE A CE1  1 
ATOM   767  C CE2  . PHE A 1 177 ? 109.96000 85.47800  121.78500 1.000 25.73767  ? 177 PHE A CE2  1 
ATOM   768  C CZ   . PHE A 1 177 ? 111.22200 85.76400  121.31200 1.000 26.42512  ? 177 PHE A CZ   1 
ATOM   769  N N    . CYS A 1 178 ? 106.82500 88.44600  123.66600 1.000 28.17500  ? 178 CYS A N    1 
ATOM   770  C CA   . CYS A 1 178 ? 105.76500 88.20100  122.69400 1.000 23.44024  ? 178 CYS A CA   1 
ATOM   771  C C    . CYS A 1 178 ? 105.21800 89.50400  122.12700 1.000 17.36409  ? 178 CYS A C    1 
ATOM   772  O O    . CYS A 1 178 ? 104.99900 89.62100  120.91300 1.000 29.63205  ? 178 CYS A O    1 
ATOM   773  C CB   . CYS A 1 178 ? 104.64500 87.38400  123.33800 1.000 23.74889  ? 178 CYS A CB   1 
ATOM   774  S SG   . CYS A 1 178 ? 105.18600 85.82000  124.06500 1.000 44.54046  ? 178 CYS A SG   1 
ATOM   775  N N    . ILE A 1 179 ? 105.00000 90.50400  122.98600 1.000 17.39599  ? 179 ILE A N    1 
ATOM   776  C CA   . ILE A 1 179 ? 104.43300 91.75600  122.49800 1.000 20.84405  ? 179 ILE A CA   1 
ATOM   777  C C    . ILE A 1 179 ? 105.43100 92.49000  121.61100 1.000 20.68420  ? 179 ILE A C    1 
ATOM   778  O O    . ILE A 1 179 ? 105.05300 93.06900  120.58600 1.000 22.89527  ? 179 ILE A O    1 
ATOM   779  C CB   . ILE A 1 179 ? 103.96700 92.63000  123.67600 1.000 20.22799  ? 179 ILE A CB   1 
ATOM   780  C CG1  . ILE A 1 179 ? 102.84100 91.93400  124.43700 1.000 27.63462  ? 179 ILE A CG1  1 
ATOM   781  C CG2  . ILE A 1 179 ? 103.51400 93.99000  123.18200 1.000 18.86447  ? 179 ILE A CG2  1 
ATOM   782  C CD1  . ILE A 1 179 ? 101.51700 91.94900  123.71100 1.000 22.75999  ? 179 ILE A CD1  1 
ATOM   783  N N    . GLY A 1 180 ? 106.71900 92.45200  121.96000 1.000 23.14488  ? 180 GLY A N    1 
ATOM   784  C CA   . GLY A 1 180 ? 107.71500 93.07700  121.10700 1.000 18.13095  ? 180 GLY A CA   1 
ATOM   785  C C    . GLY A 1 180 ? 107.82500 92.39300  119.76100 1.000 21.03507  ? 180 GLY A C    1 
ATOM   786  O O    . GLY A 1 180 ? 107.94400 93.05500  118.72600 1.000 22.02580  ? 180 GLY A O    1 
ATOM   787  N N    . PHE A 1 181 ? 107.71900 91.06200  119.74600 1.000 19.01624  ? 181 PHE A N    1 
ATOM   788  C CA   . PHE A 1 181 ? 107.80000 90.34000  118.48400 1.000 13.14816  ? 181 PHE A CA   1 
ATOM   789  C C    . PHE A 1 181 ? 106.61200 90.67500  117.59300 1.000 20.57006  ? 181 PHE A C    1 
ATOM   790  O O    . PHE A 1 181 ? 106.78100 90.95000  116.39800 1.000 25.60405  ? 181 PHE A O    1 
ATOM   791  C CB   . PHE A 1 181 ? 107.87300 88.83500  118.74400 1.000 18.35964  ? 181 PHE A CB   1 
ATOM   792  C CG   . PHE A 1 181 ? 107.83300 87.99800  117.49600 1.000 25.79012  ? 181 PHE A CG   1 
ATOM   793  C CD1  . PHE A 1 181 ? 108.99600 87.69600  116.81200 1.000 26.48918  ? 181 PHE A CD1  1 
ATOM   794  C CD2  . PHE A 1 181 ? 106.63300 87.51700  117.00300 1.000 24.81746  ? 181 PHE A CD2  1 
ATOM   795  C CE1  . PHE A 1 181 ? 108.96400 86.93100  115.66300 1.000 20.46156  ? 181 PHE A CE1  1 
ATOM   796  C CE2  . PHE A 1 181 ? 106.59600 86.75300  115.85500 1.000 24.91436  ? 181 PHE A CE2  1 
ATOM   797  C CZ   . PHE A 1 181 ? 107.76300 86.46000  115.18500 1.000 19.26001  ? 181 PHE A CZ   1 
ATOM   798  N N    . LEU A 1 182 ? 105.40400 90.69200  118.16200 1.000 21.20112  ? 182 LEU A N    1 
ATOM   799  C CA   . LEU A 1 182 ? 104.22900 90.95600  117.33800 1.000 17.03773  ? 182 LEU A CA   1 
ATOM   800  C C    . LEU A 1 182 ? 104.19100 92.40700  116.86900 1.000 18.04915  ? 182 LEU A C    1 
ATOM   801  O O    . LEU A 1 182 ? 103.82500 92.68300  115.71800 1.000 27.41495  ? 182 LEU A O    1 
ATOM   802  C CB   . LEU A 1 182 ? 102.95900 90.60600  118.11100 1.000 22.23761  ? 182 LEU A CB   1 
ATOM   803  C CG   . LEU A 1 182 ? 102.76500 89.12200  118.42100 1.000 20.89299  ? 182 LEU A CG   1 
ATOM   804  C CD1  . LEU A 1 182 ? 101.80300 88.93400  119.57900 1.000 26.51928  ? 182 LEU A CD1  1 
ATOM   805  C CD2  . LEU A 1 182 ? 102.27200 88.38700  117.19000 1.000 25.28024  ? 182 LEU A CD2  1 
ATOM   806  N N    . ALA A 1 183 ? 104.63000 93.34300  117.71600 1.000 22.83809  ? 183 ALA A N    1 
ATOM   807  C CA   . ALA A 1 183 ? 104.62500 94.74900  117.33600 1.000 20.39318  ? 183 ALA A CA   1 
ATOM   808  C C    . ALA A 1 183 ? 105.74000 95.09500  116.36400 1.000 22.69074  ? 183 ALA A C    1 
ATOM   809  O O    . ALA A 1 183 ? 105.62100 96.08700  115.64000 1.000 29.39076  ? 183 ALA A O    1 
ATOM   810  C CB   . ALA A 1 183 ? 104.72800 95.63300  118.58000 1.000 13.30295  ? 183 ALA A CB   1 
ATOM   811  N N    . THR A 1 184 ? 106.81100 94.30200  116.32000 1.000 23.15739  ? 184 THR A N    1 
ATOM   812  C CA   . THR A 1 184 ? 107.84300 94.51600  115.31800 1.000 18.68791  ? 184 THR A CA   1 
ATOM   813  C C    . THR A 1 184 ? 107.53300 93.80200  114.01400 1.000 24.61145  ? 184 THR A C    1 
ATOM   814  O O    . THR A 1 184 ? 108.01200 94.23300  112.95900 1.000 29.65783  ? 184 THR A O    1 
ATOM   815  C CB   . THR A 1 184 ? 109.20500 94.04600  115.83500 1.000 21.67999  ? 184 THR A CB   1 
ATOM   816  O OG1  . THR A 1 184 ? 109.36400 94.44700  117.20000 1.000 31.56135  ? 184 THR A OG1  1 
ATOM   817  C CG2  . THR A 1 184 ? 110.32500 94.63900  114.99800 1.000 18.20714  ? 184 THR A CG2  1 
ATOM   818  N N    . PHE A 1 185 ? 106.74100 92.73000  114.05800 1.000 29.24759  ? 185 PHE A N    1 
ATOM   819  C CA   . PHE A 1 185 ? 106.37300 92.04600  112.82800 1.000 22.30691  ? 185 PHE A CA   1 
ATOM   820  C C    . PHE A 1 185 ? 105.20600 92.72600  112.12600 1.000 24.42314  ? 185 PHE A C    1 
ATOM   821  O O    . PHE A 1 185 ? 105.11200 92.66300  110.89600 1.000 34.13659  ? 185 PHE A O    1 
ATOM   822  C CB   . PHE A 1 185 ? 106.03000 90.58400  113.11600 1.000 22.60972  ? 185 PHE A CB   1 
ATOM   823  C CG   . PHE A 1 185 ? 105.99500 89.72000  111.89100 1.000 24.31045  ? 185 PHE A CG   1 
ATOM   824  C CD1  . PHE A 1 185 ? 107.14100 89.50100  111.14900 1.000 27.82865  ? 185 PHE A CD1  1 
ATOM   825  C CD2  . PHE A 1 185 ? 104.81400 89.13300  111.47700 1.000 30.37159  ? 185 PHE A CD2  1 
ATOM   826  C CE1  . PHE A 1 185 ? 107.11100 88.70900  110.01900 1.000 25.77618  ? 185 PHE A CE1  1 
ATOM   827  C CE2  . PHE A 1 185 ? 104.77900 88.34000  110.34700 1.000 30.65303  ? 185 PHE A CE2  1 
ATOM   828  C CZ   . PHE A 1 185 ? 105.92900 88.12800  109.61800 1.000 23.77998  ? 185 PHE A CZ   1 
ATOM   829  N N    . MET A 1 186 ? 104.31900 93.38900  112.87200 1.000 33.99525  ? 186 MET A N    1 
ATOM   830  C CA   . MET A 1 186 ? 103.18700 94.05100  112.23600 1.000 26.45027  ? 186 MET A CA   1 
ATOM   831  C C    . MET A 1 186 ? 103.52700 95.42500  111.67100 1.000 24.80026  ? 186 MET A C    1 
ATOM   832  O O    . MET A 1 186 ? 102.73300 95.96600  110.89600 1.000 27.60198  ? 186 MET A O    1 
ATOM   833  C CB   . MET A 1 186 ? 102.02900 94.18000  113.22600 1.000 27.98965  ? 186 MET A CB   1 
ATOM   834  C CG   . MET A 1 186 ? 101.46200 92.84900  113.68400 1.000 35.61602  ? 186 MET A CG   1 
ATOM   835  S SD   . MET A 1 186 ? 100.38600 92.09600  112.44900 1.000 53.37839  ? 186 MET A SD   1 
ATOM   836  C CE   . MET A 1 186 ? 100.43600 90.38200  112.96300 1.000 34.18680  ? 186 MET A CE   1 
ATOM   837  N N    . LYS A 1 187 ? 104.67400 96.00000  112.02400 1.000 23.85406  ? 187 LYS A N    1 
ATOM   838  C CA   . LYS A 1 187 ? 105.08600 97.28300  111.47200 1.000 24.78963  ? 187 LYS A CA   1 
ATOM   839  C C    . LYS A 1 187 ? 105.95800 97.14400  110.23200 1.000 34.50942  ? 187 LYS A C    1 
ATOM   840  O O    . LYS A 1 187 ? 106.31000 98.16000  109.62500 1.000 32.78182  ? 187 LYS A O    1 
ATOM   841  C CB   . LYS A 1 187 ? 105.82900 98.10800  112.52800 1.000 28.17009  ? 187 LYS A CB   1 
ATOM   842  C CG   . LYS A 1 187 ? 107.30300 97.77900  112.64800 1.000 33.05119  ? 187 LYS A CG   1 
ATOM   843  C CD   . LYS A 1 187 ? 108.04600 98.85900  113.41200 1.000 28.73058  ? 187 LYS A CD   1 
ATOM   844  C CE   . LYS A 1 187 ? 109.53400 98.81300  113.11600 1.000 34.30994  ? 187 LYS A CE   1 
ATOM   845  N NZ   . LYS A 1 187 ? 110.35200 98.86400  114.35800 1.000 36.24287  ? 187 LYS A NZ   1 
ATOM   846  N N    . LEU A 1 188 ? 106.31700 95.92300  109.84500 1.000 33.27895  ? 188 LEU A N    1 
ATOM   847  C CA   . LEU A 1 188 ? 107.11900 95.68500  108.65500 1.000 27.29980  ? 188 LEU A CA   1 
ATOM   848  C C    . LEU A 1 188 ? 106.27100 95.33700  107.44100 1.000 34.44559  ? 188 LEU A C    1 
ATOM   849  O O    . LEU A 1 188 ? 106.82000 95.13900  106.35400 1.000 36.18986  ? 188 LEU A O    1 
ATOM   850  C CB   . LEU A 1 188 ? 108.13500 94.56800  108.91200 1.000 30.41180  ? 188 LEU A CB   1 
ATOM   851  C CG   . LEU A 1 188 ? 109.22300 94.85500  109.94700 1.000 30.45124  ? 188 LEU A CG   1 
ATOM   852  C CD1  . LEU A 1 188 ? 110.08200 93.62300  110.17600 1.000 27.45929  ? 188 LEU A CD1  1 
ATOM   853  C CD2  . LEU A 1 188 ? 110.07700 96.03200  109.51100 1.000 31.82477  ? 188 LEU A CD2  1 
ATOM   854  N N    . TYR A 1 189 ? 104.95600 95.25900  107.60100 1.000 42.91938  ? 189 TYR A N    1 
ATOM   855  C CA   . TYR A 1 189 ? 104.08200 95.05400  106.46000 1.000 40.79921  ? 189 TYR A CA   1 
ATOM   856  C C    . TYR A 1 189 ? 104.18300 96.25000  105.51600 1.000 45.66616  ? 189 TYR A C    1 
ATOM   857  O O    . TYR A 1 189 ? 104.32500 97.39100  105.97200 1.000 48.35075  ? 189 TYR A O    1 
ATOM   858  C CB   . TYR A 1 189 ? 102.63800 94.86500  106.92500 1.000 39.37882  ? 189 TYR A CB   1 
ATOM   859  C CG   . TYR A 1 189 ? 101.83300 93.91700  106.06900 1.000 44.96893  ? 189 TYR A CG   1 
ATOM   860  C CD1  . TYR A 1 189 ? 101.97800 92.54300  106.19600 1.000 44.79575  ? 189 TYR A CD1  1 
ATOM   861  C CD2  . TYR A 1 189 ? 100.92600 94.39600  105.13400 1.000 48.56183  ? 189 TYR A CD2  1 
ATOM   862  C CE1  . TYR A 1 189 ? 101.24400 91.67300  105.41500 1.000 46.22543  ? 189 TYR A CE1  1 
ATOM   863  C CE2  . TYR A 1 189 ? 100.18700 93.53400  104.34800 1.000 46.63673  ? 189 TYR A CE2  1 
ATOM   864  C CZ   . TYR A 1 189 ? 100.35000 92.17300  104.49300 1.000 50.59107  ? 189 TYR A CZ   1 
ATOM   865  O OH   . TYR A 1 189 ? 99.61500  91.31000  103.71200 1.000 51.60046  ? 189 TYR A OH   1 
ATOM   866  N N    . PRO A 1 190 ? 104.11400 96.03300  104.20000 1.000 44.24821  ? 190 PRO A N    1 
ATOM   867  C CA   . PRO A 1 190 ? 104.30900 97.15300  103.26500 1.000 45.06987  ? 190 PRO A CA   1 
ATOM   868  C C    . PRO A 1 190 ? 103.18900 98.17800  103.29300 1.000 46.35914  ? 190 PRO A C    1 
ATOM   869  O O    . PRO A 1 190 ? 103.41000 99.31800  102.86600 1.000 42.06995  ? 190 PRO A O    1 
ATOM   870  C CB   . PRO A 1 190 ? 104.39600 96.45900  101.89700 1.000 46.33015  ? 190 PRO A CB   1 
ATOM   871  C CG   . PRO A 1 190 ? 104.68600 95.01900  102.20700 1.000 45.62053  ? 190 PRO A CG   1 
ATOM   872  C CD   . PRO A 1 190 ? 103.98700 94.74800  103.49700 1.000 43.99358  ? 190 PRO A CD   1 
ATOM   873  N N    . SER A 1 191 ? 102.00000 97.82000  103.77800 1.000 46.58694  ? 191 SER A N    1 
ATOM   874  C CA   . SER A 1 191 ? 100.88400 98.75600  103.82100 1.000 41.73940  ? 191 SER A CA   1 
ATOM   875  C C    . SER A 1 191 ? 100.89400 99.64700  105.05700 1.000 49.07424  ? 191 SER A C    1 
ATOM   876  O O    . SER A 1 191 ? 100.09400 100.58600 105.12700 1.000 47.93359  ? 191 SER A O    1 
ATOM   877  C CB   . SER A 1 191 ? 99.56000  97.99100  103.74700 1.000 42.24229  ? 191 SER A CB   1 
ATOM   878  O OG   . SER A 1 191 ? 99.00700  97.80000  105.03500 1.000 49.86165  ? 191 SER A OG   1 
ATOM   879  N N    . MET A 1 192 ? 101.77300 99.38100  106.02500 1.000 51.03134  ? 192 MET A N    1 
ATOM   880  C CA   . MET A 1 192 ? 101.83500 100.12600 107.27700 1.000 41.70251  ? 192 MET A CA   1 
ATOM   881  C C    . MET A 1 192 ? 103.11100 100.95600 107.38400 1.000 42.05060  ? 192 MET A C    1 
ATOM   882  O O    . MET A 1 192 ? 103.58600 101.23400 108.48700 1.000 46.36797  ? 192 MET A O    1 
ATOM   883  C CB   . MET A 1 192 ? 101.72100 99.17900  108.47000 1.000 39.97364  ? 192 MET A CB   1 
ATOM   884  C CG   . MET A 1 192 ? 100.61700 98.14700  108.35700 1.000 42.91097  ? 192 MET A CG   1 
ATOM   885  S SD   . MET A 1 192 ? 99.06100  98.74800  109.04100 1.000 56.11901  ? 192 MET A SD   1 
ATOM   886  C CE   . MET A 1 192 ? 98.00300  98.68600  107.60200 1.000 45.98886  ? 192 MET A CE   1 
ATOM   887  N N    . LYS A 1 193 ? 103.67200 101.36200 106.24500 1.000 42.24923  ? 193 LYS A N    1 
ATOM   888  C CA   . LYS A 1 193 ? 104.94100 102.08200 106.26000 1.000 44.68695  ? 193 LYS A CA   1 
ATOM   889  C C    . LYS A 1 193 ? 104.79200 103.50100 106.79500 1.000 45.84365  ? 193 LYS A C    1 
ATOM   890  O O    . LYS A 1 193 ? 105.75700 104.06500 107.32200 1.000 49.88382  ? 193 LYS A O    1 
ATOM   891  C CB   . LYS A 1 193 ? 105.54000 102.10600 104.85500 1.000 46.83101  ? 193 LYS A CB   1 
ATOM   892  C CG   . LYS A 1 193 ? 106.43200 103.30000 104.57800 1.000 46.75187  ? 193 LYS A CG   1 
ATOM   893  C CD   . LYS A 1 193 ? 107.90100 102.93500 104.69200 1.000 47.38632  ? 193 LYS A CD   1 
ATOM   894  C CE   . LYS A 1 193 ? 108.78900 104.11200 104.32000 1.000 49.64804  ? 193 LYS A CE   1 
ATOM   895  N NZ   . LYS A 1 193 ? 110.14200 103.67300 103.88300 1.000 49.50322  ? 193 LYS A NZ   1 
ATOM   896  N N    . ALA A 1 194 ? 103.61300 104.09700 106.66200 1.000 41.47175  ? 194 ALA A N    1 
ATOM   897  C CA   . ALA A 1 194 ? 103.37700 105.46200 107.11000 1.000 41.56397  ? 194 ALA A CA   1 
ATOM   898  C C    . ALA A 1 194 ? 102.85400 105.54900 108.54000 1.000 40.83103  ? 194 ALA A C    1 
ATOM   899  O O    . ALA A 1 194 ? 102.49700 106.64400 108.98500 1.000 50.67563  ? 194 ALA A O    1 
ATOM   900  C CB   . ALA A 1 194 ? 102.40200 106.16400 106.16200 1.000 43.76424  ? 194 ALA A CB   1 
ATOM   901  N N    . TYR A 1 195 ? 102.79400 104.43400 109.26900 1.000 30.59856  ? 195 TYR A N    1 
ATOM   902  C CA   . TYR A 1 195 ? 102.19400 104.40700 110.59800 1.000 28.32557  ? 195 TYR A CA   1 
ATOM   903  C C    . TYR A 1 195 ? 103.15600 103.93000 111.68400 1.000 36.00749  ? 195 TYR A C    1 
ATOM   904  O O    . TYR A 1 195 ? 102.72100 103.34800 112.67700 1.000 49.50652  ? 195 TYR A O    1 
ATOM   905  C CB   . TYR A 1 195 ? 100.94100 103.53200 110.59300 1.000 35.48800  ? 195 TYR A CB   1 
ATOM   906  C CG   . TYR A 1 195 ? 99.82500  104.05000 109.71800 1.000 38.88304  ? 195 TYR A CG   1 
ATOM   907  C CD1  . TYR A 1 195 ? 99.44700  105.38400 109.75800 1.000 40.06219  ? 195 TYR A CD1  1 
ATOM   908  C CD2  . TYR A 1 195 ? 99.15000  103.20400 108.85000 1.000 38.64175  ? 195 TYR A CD2  1 
ATOM   909  C CE1  . TYR A 1 195 ? 98.42800  105.86100 108.96000 1.000 36.54547  ? 195 TYR A CE1  1 
ATOM   910  C CE2  . TYR A 1 195 ? 98.12900  103.67100 108.04800 1.000 39.80276  ? 195 TYR A CE2  1 
ATOM   911  C CZ   . TYR A 1 195 ? 97.77200  105.00000 108.10700 1.000 41.51150  ? 195 TYR A CZ   1 
ATOM   912  O OH   . TYR A 1 195 ? 96.75500  105.47100 107.31000 1.000 41.96924  ? 195 TYR A OH   1 
ATOM   913  N N    . GLU A 1 196 ? 104.46200 104.15700 111.52600 1.000 31.51827  ? 196 GLU A N    1 
ATOM   914  C CA   . GLU A 1 196 ? 105.39500 103.66500 112.53700 1.000 36.04305  ? 196 GLU A CA   1 
ATOM   915  C C    . GLU A 1 196 ? 105.32800 104.46500 113.83200 1.000 33.78276  ? 196 GLU A C    1 
ATOM   916  O O    . GLU A 1 196 ? 105.68400 103.93900 114.90000 1.000 39.97891  ? 196 GLU A O    1 
ATOM   917  C CB   . GLU A 1 196 ? 106.82100 103.68700 111.98800 1.000 35.66175  ? 196 GLU A CB   1 
ATOM   918  C CG   . GLU A 1 196 ? 107.27700 102.36000 111.41900 1.000 38.31157  ? 196 GLU A CG   1 
ATOM   919  C CD   . GLU A 1 196 ? 106.66500 102.07100 110.06400 1.000 41.96422  ? 196 GLU A CD   1 
ATOM   920  O OE1  . GLU A 1 196 ? 107.01500 102.77200 109.09300 1.000 44.58089  ? 196 GLU A OE1  1 
ATOM   921  O OE2  . GLU A 1 196 ? 105.83200 101.14600 109.97000 1.000 42.75331  ? 196 GLU A OE2  1 
ATOM   922  N N    . TYR A 1 197 ? 104.81200 105.69400 113.77500 1.000 20.23453  ? 197 TYR A N    1 
ATOM   923  C CA   . TYR A 1 197 ? 104.66800 106.50300 114.97500 1.000 18.37296  ? 197 TYR A CA   1 
ATOM   924  C C    . TYR A 1 197 ? 103.54300 106.00200 115.86400 1.000 24.34716  ? 197 TYR A C    1 
ATOM   925  O O    . TYR A 1 197 ? 103.46000 106.41800 117.02400 1.000 34.57829  ? 197 TYR A O    1 
ATOM   926  C CB   . TYR A 1 197 ? 104.44100 107.97400 114.60600 1.000 21.55577  ? 197 TYR A CB   1 
ATOM   927  C CG   . TYR A 1 197 ? 103.18800 108.24000 113.80200 1.000 21.16803  ? 197 TYR A CG   1 
ATOM   928  C CD1  . TYR A 1 197 ? 103.18100 108.09800 112.42200 1.000 16.80754  ? 197 TYR A CD1  1 
ATOM   929  C CD2  . TYR A 1 197 ? 102.01200 108.63400 114.42400 1.000 21.75336  ? 197 TYR A CD2  1 
ATOM   930  C CE1  . TYR A 1 197 ? 102.03800 108.33800 111.68800 1.000 14.09178  ? 197 TYR A CE1  1 
ATOM   931  C CE2  . TYR A 1 197 ? 100.86500 108.87400 113.69800 1.000 18.80824  ? 197 TYR A CE2  1 
ATOM   932  C CZ   . TYR A 1 197 ? 100.88300 108.72500 112.33000 1.000 21.04374  ? 197 TYR A CZ   1 
ATOM   933  O OH   . TYR A 1 197 ? 99.74200  108.96600 111.60200 1.000 22.04132  ? 197 TYR A OH   1 
ATOM   934  N N    . GLY A 1 198 ? 102.68600 105.12100 115.35300 1.000 18.05400  ? 198 GLY A N    1 
ATOM   935  C CA   . GLY A 1 198 ? 101.59300 104.58100 116.13000 1.000 13.93907  ? 198 GLY A CA   1 
ATOM   936  C C    . GLY A 1 198 ? 101.94700 103.23700 116.73000 1.000 20.79536  ? 198 GLY A C    1 
ATOM   937  O O    . GLY A 1 198 ? 101.31900 102.79900 117.69800 1.000 30.70228  ? 198 GLY A O    1 
ATOM   938  N N    . PHE A 1 199 ? 102.95400 102.57100 116.16200 1.000 21.57756  ? 199 PHE A N    1 
ATOM   939  C CA   . PHE A 1 199 ? 103.45700 101.33000 116.73700 1.000 19.70633  ? 199 PHE A CA   1 
ATOM   940  C C    . PHE A 1 199 ? 104.54000 101.58700 117.77600 1.000 19.97492  ? 199 PHE A C    1 
ATOM   941  O O    . PHE A 1 199 ? 104.64900 100.83700 118.76300 1.000 28.16751  ? 199 PHE A O    1 
ATOM   942  C CB   . PHE A 1 199 ? 104.01200 100.42600 115.63100 1.000 22.07173  ? 199 PHE A CB   1 
ATOM   943  C CG   . PHE A 1 199 ? 102.95200 99.73700  114.81800 1.000 25.73236  ? 199 PHE A CG   1 
ATOM   944  C CD1  . PHE A 1 199 ? 102.37900 98.55600  115.25300 1.000 20.35139  ? 199 PHE A CD1  1 
ATOM   945  C CD2  . PHE A 1 199 ? 102.53700 100.26800 113.60800 1.000 26.90966  ? 199 PHE A CD2  1 
ATOM   946  C CE1  . PHE A 1 199 ? 101.40700 97.92400  114.50000 1.000 21.74356  ? 199 PHE A CE1  1 
ATOM   947  C CE2  . PHE A 1 199 ? 101.56500 99.64000  112.85300 1.000 17.73202  ? 199 PHE A CE2  1 
ATOM   948  C CZ   . PHE A 1 199 ? 101.00100 98.46800  113.29900 1.000 12.52579  ? 199 PHE A CZ   1 
ATOM   949  N N    . ARG A 1 200 ? 105.27800 102.69100 117.62700 1.000 21.24162  ? 200 ARG A N    1 
ATOM   950  C CA   . ARG A 1 200 ? 106.28000 103.02000 118.63200 1.000 18.17395  ? 200 ARG A CA   1 
ATOM   951  C C    . ARG A 1 200 ? 105.62000 103.46500 119.93000 1.000 22.96955  ? 200 ARG A C    1 
ATOM   952  O O    . ARG A 1 200 ? 106.07500 103.10200 121.02400 1.000 30.06333  ? 200 ARG A O    1 
ATOM   953  C CB   . ARG A 1 200 ? 107.20800 104.10900 118.09800 1.000 22.83809  ? 200 ARG A CB   1 
ATOM   954  C CG   . ARG A 1 200 ? 108.66200 103.95500 118.49600 1.000 28.94065  ? 200 ARG A CG   1 
ATOM   955  C CD   . ARG A 1 200 ? 109.56300 104.76500 117.58200 1.000 31.48705  ? 200 ARG A CD   1 
ATOM   956  N NE   . ARG A 1 200 ? 109.01400 106.08600 117.29800 1.000 41.94032  ? 200 ARG A NE   1 
ATOM   957  C CZ   . ARG A 1 200 ? 108.96600 106.63300 116.09000 1.000 39.17053  ? 200 ARG A CZ   1 
ATOM   958  N NH1  . ARG A 1 200 ? 109.42300 105.99700 115.02400 1.000 30.96136  ? 200 ARG A NH1  1 
ATOM   959  N NH2  . ARG A 1 200 ? 108.44500 107.84900 115.94900 1.000 26.24819  ? 200 ARG A NH2  1 
ATOM   960  N N    . VAL A 1 201 ? 104.50900 104.19900 119.82900 1.000 15.26744  ? 201 VAL A N    1 
ATOM   961  C CA   . VAL A 1 201 ? 103.81200 104.64300 121.02900 1.000 20.19212  ? 201 VAL A CA   1 
ATOM   962  C C    . VAL A 1 201 ? 103.16000 103.45800 121.72400 1.000 14.85052  ? 201 VAL A C    1 
ATOM   963  O O    . VAL A 1 201 ? 103.09700 103.40900 122.95800 1.000 29.17819  ? 201 VAL A O    1 
ATOM   964  C CB   . VAL A 1 201 ? 102.78000 105.72900 120.66800 1.000 17.37060  ? 201 VAL A CB   1 
ATOM   965  C CG1  . VAL A 1 201 ? 101.68700 105.80200 121.72000 1.000 21.25626  ? 201 VAL A CG1  1 
ATOM   966  C CG2  . VAL A 1 201 ? 103.46000 107.07600 120.50500 1.000 19.88847  ? 201 VAL A CG2  1 
ATOM   967  N N    . PHE A 1 202 ? 102.75200 102.44800 120.95600 1.000 12.49276  ? 202 PHE A N    1 
ATOM   968  C CA   . PHE A 1 202 ? 102.15800 101.25200 121.54100 1.000 9.39637   ? 202 PHE A CA   1 
ATOM   969  C C    . PHE A 1 202 ? 103.19800 100.47500 122.33800 1.000 15.18083  ? 202 PHE A C    1 
ATOM   970  O O    . PHE A 1 202 ? 102.96500 100.10900 123.50000 1.000 20.69857  ? 202 PHE A O    1 
ATOM   971  C CB   . PHE A 1 202 ? 101.55700 100.39000 120.42700 1.000 11.57567  ? 202 PHE A CB   1 
ATOM   972  C CG   . PHE A 1 202 ? 100.93300 99.11100  120.90500 1.000 24.83883  ? 202 PHE A CG   1 
ATOM   973  C CD1  . PHE A 1 202 ? 101.68700 97.95500  121.02000 1.000 24.39976  ? 202 PHE A CD1  1 
ATOM   974  C CD2  . PHE A 1 202 ? 99.58600  99.05500  121.21100 1.000 16.33428  ? 202 PHE A CD2  1 
ATOM   975  C CE1  . PHE A 1 202 ? 101.11400 96.77800  121.45500 1.000 15.00625  ? 202 PHE A CE1  1 
ATOM   976  C CE2  . PHE A 1 202 ? 99.00900  97.87800  121.64400 1.000 17.96835  ? 202 PHE A CE2  1 
ATOM   977  C CZ   . PHE A 1 202 ? 99.77400  96.74000  121.76500 1.000 13.64184  ? 202 PHE A CZ   1 
ATOM   978  N N    . LEU A 1 203 ? 104.36600 100.23600 121.73500 1.000 18.05704  ? 203 LEU A N    1 
ATOM   979  C CA   . LEU A 1 203 ? 105.40600 99.50100  122.45100 1.000 11.44063  ? 203 LEU A CA   1 
ATOM   980  C C    . LEU A 1 203 ? 105.86900 100.26200 123.69000 1.000 19.48943  ? 203 LEU A C    1 
ATOM   981  O O    . LEU A 1 203 ? 106.03000 99.67100  124.77000 1.000 15.49332  ? 203 LEU A O    1 
ATOM   982  C CB   . LEU A 1 203 ? 106.58600 99.21800  121.52300 1.000 14.72670  ? 203 LEU A CB   1 
ATOM   983  C CG   . LEU A 1 203 ? 107.29900 97.87500  121.69800 1.000 17.00451  ? 203 LEU A CG   1 
ATOM   984  C CD1  . LEU A 1 203 ? 106.31800 96.76900  122.04100 1.000 16.35420  ? 203 LEU A CD1  1 
ATOM   985  C CD2  . LEU A 1 203 ? 108.09000 97.52200  120.45200 1.000 10.95169  ? 203 LEU A CD2  1 
ATOM   986  N N    . LEU A 1 204 ? 106.05700 101.58000 123.56500 1.000 24.17284  ? 204 LEU A N    1 
ATOM   987  C CA   . LEU A 1 204 ? 106.49900 102.37000 124.71000 1.000 15.67395  ? 204 LEU A CA   1 
ATOM   988  C C    . LEU A 1 204 ? 105.47700 102.33000 125.84000 1.000 15.77816  ? 204 LEU A C    1 
ATOM   989  O O    . LEU A 1 204 ? 105.84000 102.15200 127.00800 1.000 16.24765  ? 204 LEU A O    1 
ATOM   990  C CB   . LEU A 1 204 ? 106.76900 103.81300 124.28300 1.000 24.77222  ? 204 LEU A CB   1 
ATOM   991  C CG   . LEU A 1 204 ? 107.92200 104.08300 123.31400 1.000 24.90027  ? 204 LEU A CG   1 
ATOM   992  C CD1  . LEU A 1 204 ? 107.86600 105.51300 122.80700 1.000 23.43580  ? 204 LEU A CD1  1 
ATOM   993  C CD2  . LEU A 1 204 ? 109.25700 103.81000 123.97900 1.000 19.24067  ? 204 LEU A CD2  1 
ATOM   994  N N    . THR A 1 205 ? 104.19200 102.49700 125.51700 1.000 20.00999  ? 205 THR A N    1 
ATOM   995  C CA   . THR A 1 205 ? 103.17100 102.49300 126.55800 1.000 19.49619  ? 205 THR A CA   1 
ATOM   996  C C    . THR A 1 205 ? 103.10800 101.14600 127.26400 1.000 19.13357  ? 205 THR A C    1 
ATOM   997  O O    . THR A 1 205 ? 103.06500 101.08100 128.50100 1.000 17.70196  ? 205 THR A O    1 
ATOM   998  C CB   . THR A 1 205 ? 101.81000 102.84900 125.96000 1.000 20.77863  ? 205 THR A CB   1 
ATOM   999  O OG1  . THR A 1 205 ? 101.96200 103.93600 125.04000 1.000 30.10471  ? 205 THR A OG1  1 
ATOM   1000 C CG2  . THR A 1 205 ? 100.83100 103.23900 127.05000 1.000 17.80371  ? 205 THR A CG2  1 
ATOM   1001 N N    . TYR A 1 206 ? 103.12900 100.05200 126.49700 1.000 22.37156  ? 206 TYR A N    1 
ATOM   1002 C CA   . TYR A 1 206 ? 103.05600 98.73700  127.12500 1.000 12.57358  ? 206 TYR A CA   1 
ATOM   1003 C C    . TYR A 1 206 ? 104.23100 98.52300  128.07100 1.000 18.84269  ? 206 TYR A C    1 
ATOM   1004 O O    . TYR A 1 206 ? 104.05000 98.12400  129.23100 1.000 21.78947  ? 206 TYR A O    1 
ATOM   1005 C CB   . TYR A 1 206 ? 103.01600 97.64100  126.06200 1.000 12.60385  ? 206 TYR A CB   1 
ATOM   1006 C CG   . TYR A 1 206 ? 102.80800 96.25700  126.63600 1.000 23.35047  ? 206 TYR A CG   1 
ATOM   1007 C CD1  . TYR A 1 206 ? 101.53300 95.79200  126.92400 1.000 19.08815  ? 206 TYR A CD1  1 
ATOM   1008 C CD2  . TYR A 1 206 ? 103.88500 95.42200  126.90400 1.000 25.29072  ? 206 TYR A CD2  1 
ATOM   1009 C CE1  . TYR A 1 206 ? 101.33400 94.53400  127.45200 1.000 18.59957  ? 206 TYR A CE1  1 
ATOM   1010 C CE2  . TYR A 1 206 ? 103.69700 94.16200  127.43400 1.000 19.02162  ? 206 TYR A CE2  1 
ATOM   1011 C CZ   . TYR A 1 206 ? 102.41800 93.72400  127.70600 1.000 26.86655  ? 206 TYR A CZ   1 
ATOM   1012 O OH   . TYR A 1 206 ? 102.21700 92.47000  128.23300 1.000 33.24763  ? 206 TYR A OH   1 
ATOM   1013 N N    . CYS A 1 207 ? 105.44900 98.81200  127.60100 1.000 29.70276  ? 207 CYS A N    1 
ATOM   1014 C CA   . CYS A 1 207 ? 106.62400 98.56400  128.42900 1.000 9.16640   ? 207 CYS A CA   1 
ATOM   1015 C C    . CYS A 1 207 ? 106.62100 99.44700  129.67100 1.000 20.42840  ? 207 CYS A C    1 
ATOM   1016 O O    . CYS A 1 207 ? 106.89700 98.97500  130.78000 1.000 30.19505  ? 207 CYS A O    1 
ATOM   1017 C CB   . CYS A 1 207 ? 107.90000 98.77500  127.61500 1.000 19.45857  ? 207 CYS A CB   1 
ATOM   1018 S SG   . CYS A 1 207 ? 108.21500 97.49900  126.37500 1.000 45.03567  ? 207 CYS A SG   1 
ATOM   1019 N N    . TYR A 1 208 ? 106.34800 100.74300 129.50200 1.000 27.43528  ? 208 TYR A N    1 
ATOM   1020 C CA   . TYR A 1 208 ? 106.33300 101.65000 130.64400 1.000 16.00328  ? 208 TYR A CA   1 
ATOM   1021 C C    . TYR A 1 208 ? 105.32400 101.20500 131.69500 1.000 25.97384  ? 208 TYR A C    1 
ATOM   1022 O O    . TYR A 1 208 ? 105.63300 101.17300 132.89200 1.000 20.86035  ? 208 TYR A O    1 
ATOM   1023 C CB   . TYR A 1 208 ? 106.02700 103.07300 130.18100 1.000 16.66787  ? 208 TYR A CB   1 
ATOM   1024 C CG   . TYR A 1 208 ? 106.14900 104.10500 131.27600 1.000 27.63637  ? 208 TYR A CG   1 
ATOM   1025 C CD1  . TYR A 1 208 ? 107.35300 104.74600 131.51700 1.000 30.90730  ? 208 TYR A CD1  1 
ATOM   1026 C CD2  . TYR A 1 208 ? 105.06100 104.43200 132.07600 1.000 33.40400  ? 208 TYR A CD2  1 
ATOM   1027 C CE1  . TYR A 1 208 ? 107.47300 105.68500 132.51800 1.000 28.53067  ? 208 TYR A CE1  1 
ATOM   1028 C CE2  . TYR A 1 208 ? 105.17200 105.37100 133.08200 1.000 24.65926  ? 208 TYR A CE2  1 
ATOM   1029 C CZ   . TYR A 1 208 ? 106.38200 105.99300 133.29700 1.000 29.92961  ? 208 TYR A CZ   1 
ATOM   1030 O OH   . TYR A 1 208 ? 106.50700 106.93200 134.29300 1.000 35.17198  ? 208 TYR A OH   1 
ATOM   1031 N N    . ILE A 1 209 ? 104.11300 100.83500 131.26800 1.000 31.14274  ? 209 ILE A N    1 
ATOM   1032 C CA   . ILE A 1 209 ? 103.09000 100.47300 132.24400 1.000 18.43534  ? 209 ILE A CA   1 
ATOM   1033 C C    . ILE A 1 209 ? 103.44900 99.17200  132.94600 1.000 26.03926  ? 209 ILE A C    1 
ATOM   1034 O O    . ILE A 1 209 ? 103.19800 99.01500  134.14600 1.000 27.04764  ? 209 ILE A O    1 
ATOM   1035 C CB   . ILE A 1 209 ? 101.70300 100.39300 131.58400 1.000 26.40092  ? 209 ILE A CB   1 
ATOM   1036 C CG1  . ILE A 1 209 ? 101.22100 101.78300 131.17200 1.000 21.75982  ? 209 ILE A CG1  1 
ATOM   1037 C CG2  . ILE A 1 209 ? 100.70100 99.75600  132.53100 1.000 28.95310  ? 209 ILE A CG2  1 
ATOM   1038 C CD1  . ILE A 1 209 ? 99.86700  101.77700 130.50700 1.000 18.99193  ? 209 ILE A CD1  1 
ATOM   1039 N N    . LEU A 1 210 ? 104.03700 98.21400  132.22300 1.000 35.43180  ? 210 LEU A N    1 
ATOM   1040 C CA   . LEU A 1 210 ? 104.35400 96.94300  132.86700 1.000 23.22785  ? 210 LEU A CA   1 
ATOM   1041 C C    . LEU A 1 210 ? 105.53200 97.07000  133.82700 1.000 29.71765  ? 210 LEU A C    1 
ATOM   1042 O O    . LEU A 1 210 ? 105.50800 96.49600  134.92100 1.000 34.91473  ? 210 LEU A O    1 
ATOM   1043 C CB   . LEU A 1 210 ? 104.63600 95.87000  131.81800 1.000 30.35999  ? 210 LEU A CB   1 
ATOM   1044 C CG   . LEU A 1 210 ? 104.03500 94.49900  132.13700 1.000 32.20478  ? 210 LEU A CG   1 
ATOM   1045 C CD1  . LEU A 1 210 ? 102.52500 94.52200  131.98300 1.000 32.43527  ? 210 LEU A CD1  1 
ATOM   1046 C CD2  . LEU A 1 210 ? 104.65100 93.42000  131.26500 1.000 28.95122  ? 210 LEU A CD2  1 
ATOM   1047 N N    . ILE A 1 211 ? 106.57100 97.81600  133.44500 1.000 36.28611  ? 211 ILE A N    1 
ATOM   1048 C CA   . ILE A 1 211 ? 107.76000 97.90500  134.28900 1.000 26.90028  ? 211 ILE A CA   1 
ATOM   1049 C C    . ILE A 1 211 ? 107.63600 98.93500  135.40800 1.000 31.79087  ? 211 ILE A C    1 
ATOM   1050 O O    . ILE A 1 211 ? 108.35100 98.82900  136.41100 1.000 35.03959  ? 211 ILE A O    1 
ATOM   1051 C CB   . ILE A 1 211 ? 109.00000 98.20600  133.42900 1.000 28.62335  ? 211 ILE A CB   1 
ATOM   1052 C CG1  . ILE A 1 211 ? 109.29800 97.02800  132.50000 1.000 29.42764  ? 211 ILE A CG1  1 
ATOM   1053 C CG2  . ILE A 1 211 ? 110.20500 98.50500  134.30200 1.000 30.44789  ? 211 ILE A CG2  1 
ATOM   1054 C CD1  . ILE A 1 211 ? 110.32900 97.32900  131.44100 1.000 33.50013  ? 211 ILE A CD1  1 
ATOM   1055 N N    . SER A 1 212 ? 106.74200 99.91400  135.28600 1.000 46.83522  ? 212 SER A N    1 
ATOM   1056 C CA   . SER A 1 212 ? 106.63800 100.97400 136.28200 1.000 40.37680  ? 212 SER A CA   1 
ATOM   1057 C C    . SER A 1 212 ? 105.60200 100.68500 137.35900 1.000 45.91593  ? 212 SER A C    1 
ATOM   1058 O O    . SER A 1 212 ? 105.38400 101.53400 138.22900 1.000 51.85033  ? 212 SER A O    1 
ATOM   1059 C CB   . SER A 1 212 ? 106.30900 102.30700 135.60400 1.000 39.90308  ? 212 SER A CB   1 
ATOM   1060 O OG   . SER A 1 212 ? 107.42700 102.80800 134.89500 1.000 43.72174  ? 212 SER A OG   1 
ATOM   1061 N N    . GLY A 1 213 ? 104.96700 99.51800  137.33000 1.000 55.85744  ? 213 GLY A N    1 
ATOM   1062 C CA   . GLY A 1 213 ? 103.93400 99.20500  138.29500 1.000 56.78263  ? 213 GLY A CA   1 
ATOM   1063 C C    . GLY A 1 213 ? 104.24300 97.96100  139.09900 1.000 61.08996  ? 213 GLY A C    1 
ATOM   1064 O O    . GLY A 1 213 ? 103.51700 97.62500  140.03900 1.000 67.51889  ? 213 GLY A O    1 
ATOM   1065 N N    . PHE A 1 214 ? 105.32400 97.26600  138.73700 1.000 66.62828  ? 214 PHE A N    1 
ATOM   1066 C CA   . PHE A 1 214 ? 105.70100 96.05900  139.46400 1.000 66.06568  ? 214 PHE A CA   1 
ATOM   1067 C C    . PHE A 1 214 ? 105.93500 96.35900  140.93800 1.000 67.80876  ? 214 PHE A C    1 
ATOM   1068 O O    . PHE A 1 214 ? 105.51400 95.59100  141.81100 1.000 67.36211  ? 214 PHE A O    1 
ATOM   1069 C CB   . PHE A 1 214 ? 106.95000 95.44000  138.83800 1.000 66.43918  ? 214 PHE A CB   1 
ATOM   1070 C CG   . PHE A 1 214 ? 107.15700 94.00000  139.20000 1.000 67.25657  ? 214 PHE A CG   1 
ATOM   1071 C CD1  . PHE A 1 214 ? 106.20400 93.04800  138.88100 1.000 68.36817  ? 214 PHE A CD1  1 
ATOM   1072 C CD2  . PHE A 1 214 ? 108.30300 93.59800  139.86400 1.000 67.52055  ? 214 PHE A CD2  1 
ATOM   1073 C CE1  . PHE A 1 214 ? 106.39300 91.72100  139.21400 1.000 68.65694  ? 214 PHE A CE1  1 
ATOM   1074 C CE2  . PHE A 1 214 ? 108.49700 92.27400  140.20100 1.000 68.00424  ? 214 PHE A CE2  1 
ATOM   1075 C CZ   . PHE A 1 214 ? 107.54000 91.33400  139.87500 1.000 68.78809  ? 214 PHE A CZ   1 
ATOM   1076 N N    . ARG A 1 215 ? 106.60700 97.46800  141.23500 1.000 74.11618  ? 215 ARG A N    1 
ATOM   1077 C CA   . ARG A 1 215 ? 106.79400 97.89600  142.61300 1.000 76.91401  ? 215 ARG A CA   1 
ATOM   1078 C C    . ARG A 1 215 ? 105.57500 98.67900  143.08200 1.000 78.47626  ? 215 ARG A C    1 
ATOM   1079 O O    . ARG A 1 215 ? 105.11000 99.59400  142.39500 1.000 77.30802  ? 215 ARG A O    1 
ATOM   1080 C CB   . ARG A 1 215 ? 108.05700 98.74700  142.74000 1.000 76.17174  ? 215 ARG A CB   1 
ATOM   1081 C CG   . ARG A 1 215 ? 108.43400 99.49800  141.47100 1.000 76.76432  ? 215 ARG A CG   1 
ATOM   1082 C CD   . ARG A 1 215 ? 107.83700 100.89600 141.45200 1.000 75.69533  ? 215 ARG A CD   1 
ATOM   1083 N NE   . ARG A 1 215 ? 108.52700 101.77100 140.51200 1.000 75.31862  ? 215 ARG A NE   1 
ATOM   1084 C CZ   . ARG A 1 215 ? 108.11900 102.98900 140.18300 1.000 74.94864  ? 215 ARG A CZ   1 
ATOM   1085 N NH1  . ARG A 1 215 ? 107.02300 103.51600 140.70500 1.000 75.16627  ? 215 ARG A NH1  1 
ATOM   1086 N NH2  . ARG A 1 215 ? 108.83100 103.70000 139.31500 1.000 75.01912  ? 215 ARG A NH2  1 
ATOM   1087 N N    . THR A 1 216 ? 105.05900 98.31800  144.25500 1.000 82.83459  ? 216 THR A N    1 
ATOM   1088 C CA   . THR A 1 216 ? 103.90100 98.91000  144.91100 1.000 84.08217  ? 216 THR A CA   1 
ATOM   1089 C C    . THR A 1 216 ? 102.58700 98.38000  144.34000 1.000 84.21380  ? 216 THR A C    1 
ATOM   1090 O O    . THR A 1 216 ? 101.53400 98.65200  144.91600 1.000 85.63152  ? 216 THR A O    1 
ATOM   1091 C CB   . THR A 1 216 ? 103.88500 100.44900 144.84400 1.000 84.49456  ? 216 THR A CB   1 
ATOM   1092 O OG1  . THR A 1 216 ? 105.21900 100.94900 145.00100 1.000 85.03696  ? 216 THR A OG1  1 
ATOM   1093 C CG2  . THR A 1 216 ? 103.00200 101.02100 145.94100 1.000 83.03947  ? 216 THR A CG2  1 
ATOM   1094 N N    . GLY A 1 217 ? 102.60700 97.63400  143.23800 1.000 77.00946  ? 217 GLY A N    1 
ATOM   1095 C CA   . GLY A 1 217 ? 101.38800 97.10000  142.66200 1.000 76.68555  ? 217 GLY A CA   1 
ATOM   1096 C C    . GLY A 1 217 ? 100.32100 98.13900  142.38800 1.000 78.06760  ? 217 GLY A C    1 
ATOM   1097 O O    . GLY A 1 217 ? 99.15700  97.94900  142.75300 1.000 79.25662  ? 217 GLY A O    1 
ATOM   1098 N N    . GLN A 1 218 ? 100.70000 99.24200  141.74600 1.000 77.93857  ? 218 GLN A N    1 
ATOM   1099 C CA   . GLN A 1 218 ? 99.77500  100.31900 141.40300 1.000 78.60536  ? 218 GLN A CA   1 
ATOM   1100 C C    . GLN A 1 218 ? 99.71500  100.44300 139.88600 1.000 78.26756  ? 218 GLN A C    1 
ATOM   1101 O O    . GLN A 1 218 ? 100.66000 100.93800 139.26100 1.000 80.45978  ? 218 GLN A O    1 
ATOM   1102 C CB   . GLN A 1 218 ? 100.20300 101.63900 142.04400 1.000 78.04120  ? 218 GLN A CB   1 
ATOM   1103 C CG   . GLN A 1 218 ? 100.10600 101.65700 143.56100 1.000 79.57375  ? 218 GLN A CG   1 
ATOM   1104 C CD   . GLN A 1 218 ? 100.60400 102.95600 144.16300 1.000 81.67577  ? 218 GLN A CD   1 
ATOM   1105 O OE1  . GLN A 1 218 ? 101.42100 103.65800 143.56800 1.000 83.99756  ? 218 GLN A OE1  1 
ATOM   1106 N NE2  . GLN A 1 218 ? 100.11400 103.28200 145.35400 1.000 79.52826  ? 218 GLN A NE2  1 
ATOM   1107 N N    . PHE A 1 219 ? 98.60400  100.00000 139.29700 1.000 66.97174  ? 219 PHE A N    1 
ATOM   1108 C CA   . PHE A 1 219 ? 98.44200  99.98300  137.85100 1.000 66.68268  ? 219 PHE A CA   1 
ATOM   1109 C C    . PHE A 1 219 ? 97.31500  100.87600 137.35400 1.000 66.69717  ? 219 PHE A C    1 
ATOM   1110 O O    . PHE A 1 219 ? 97.25700  101.15300 136.15100 1.000 70.72268  ? 219 PHE A O    1 
ATOM   1111 C CB   . PHE A 1 219 ? 98.20900  98.54900  137.34600 1.000 65.40657  ? 219 PHE A CB   1 
ATOM   1112 C CG   . PHE A 1 219 ? 99.44200  97.69100  137.36900 1.000 64.33869  ? 219 PHE A CG   1 
ATOM   1113 C CD1  . PHE A 1 219 ? 100.00000 97.29000  138.57000 1.000 67.05791  ? 219 PHE A CD1  1 
ATOM   1114 C CD2  . PHE A 1 219 ? 100.05600 97.30300  136.19100 1.000 65.18631  ? 219 PHE A CD2  1 
ATOM   1115 C CE1  . PHE A 1 219 ? 101.13700 96.50500  138.59500 1.000 66.72470  ? 219 PHE A CE1  1 
ATOM   1116 C CE2  . PHE A 1 219 ? 101.19600 96.52200  136.21100 1.000 65.88910  ? 219 PHE A CE2  1 
ATOM   1117 C CZ   . PHE A 1 219 ? 101.73600 96.12200  137.41500 1.000 64.55948  ? 219 PHE A CZ   1 
ATOM   1118 N N    . ILE A 1 220 ? 96.42400  101.33400 138.23600 1.000 57.43167  ? 220 ILE A N    1 
ATOM   1119 C CA   . ILE A 1 220 ? 95.31400  102.19700 137.84100 1.000 60.31153  ? 220 ILE A CA   1 
ATOM   1120 C C    . ILE A 1 220 ? 95.56000  103.64600 138.24100 1.000 61.73718  ? 220 ILE A C    1 
ATOM   1121 O O    . ILE A 1 220 ? 94.78800  104.53200 137.84100 1.000 62.06735  ? 220 ILE A O    1 
ATOM   1122 C CB   . ILE A 1 220 ? 93.98200  101.68000 138.43200 1.000 60.35061  ? 220 ILE A CB   1 
ATOM   1123 C CG1  . ILE A 1 220 ? 93.49200  100.46100 137.64800 1.000 57.86245  ? 220 ILE A CG1  1 
ATOM   1124 C CG2  . ILE A 1 220 ? 92.91000  102.75900 138.43100 1.000 60.72123  ? 220 ILE A CG2  1 
ATOM   1125 C CD1  . ILE A 1 220 ? 92.63300  100.81400 136.45400 1.000 56.72811  ? 220 ILE A CD1  1 
ATOM   1126 N N    . GLU A 1 221 ? 96.63900  103.92100 138.97500 1.000 60.90381  ? 221 GLU A N    1 
ATOM   1127 C CA   . GLU A 1 221 ? 97.03200  105.27300 139.33900 1.000 60.34586  ? 221 GLU A CA   1 
ATOM   1128 C C    . GLU A 1 221 ? 98.22300  105.77800 138.54100 1.000 59.46825  ? 221 GLU A C    1 
ATOM   1129 O O    . GLU A 1 221 ? 98.44700  106.99100 138.49900 1.000 58.18701  ? 221 GLU A O    1 
ATOM   1130 C CB   . GLU A 1 221 ? 97.36100  105.35300 140.83700 1.000 60.24834  ? 221 GLU A CB   1 
ATOM   1131 C CG   . GLU A 1 221 ? 96.16400  105.69400 141.70700 1.000 62.16470  ? 221 GLU A CG   1 
ATOM   1132 C CD   . GLU A 1 221 ? 95.19900  106.64200 141.02100 1.000 65.08121  ? 221 GLU A CD   1 
ATOM   1133 O OE1  . GLU A 1 221 ? 95.61300  107.77300 140.69100 1.000 63.48969  ? 221 GLU A OE1  1 
ATOM   1134 O OE2  . GLU A 1 221 ? 94.03000  106.25600 140.80900 1.000 62.00649  ? 221 GLU A OE2  1 
ATOM   1135 N N    . VAL A 1 222 ? 98.98800  104.87900 137.91100 1.000 61.01985  ? 222 VAL A N    1 
ATOM   1136 C CA   . VAL A 1 222 ? 100.12200 105.28600 137.08500 1.000 60.48451  ? 222 VAL A CA   1 
ATOM   1137 C C    . VAL A 1 222 ? 99.69500  105.64700 135.67300 1.000 59.99117  ? 222 VAL A C    1 
ATOM   1138 O O    . VAL A 1 222 ? 100.53400 106.07700 134.87000 1.000 61.70829  ? 222 VAL A O    1 
ATOM   1139 C CB   . VAL A 1 222 ? 101.17300 104.15600 137.06100 1.000 59.43009  ? 222 VAL A CB   1 
ATOM   1140 C CG1  . VAL A 1 222 ? 102.33900 104.50500 136.15000 1.000 58.23520  ? 222 VAL A CG1  1 
ATOM   1141 C CG2  . VAL A 1 222 ? 101.66400 103.85500 138.46900 1.000 59.84659  ? 222 VAL A CG2  1 
ATOM   1142 N N    . ALA A 1 223 ? 98.41300  105.50500 135.35000 1.000 51.08166  ? 223 ALA A N    1 
ATOM   1143 C CA   . ALA A 1 223 ? 97.88600  105.80900 134.02600 1.000 52.16600  ? 223 ALA A CA   1 
ATOM   1144 C C    . ALA A 1 223 ? 96.83200  106.90200 134.04700 1.000 53.47795  ? 223 ALA A C    1 
ATOM   1145 O O    . ALA A 1 223 ? 96.85000  107.79600 133.18900 1.000 51.11123  ? 223 ALA A O    1 
ATOM   1146 C CB   . ALA A 1 223 ? 97.29600  104.54000 133.39300 1.000 42.83955  ? 223 ALA A CB   1 
ATOM   1147 N N    . ILE A 1 224 ? 95.97700  106.91700 135.07200 1.000 50.45963  ? 224 ILE A N    1 
ATOM   1148 C CA   . ILE A 1 224 ? 94.90200  107.90000 135.12300 1.000 46.66705  ? 224 ILE A CA   1 
ATOM   1149 C C    . ILE A 1 224 ? 95.47800  109.28500 135.36000 1.000 48.34000  ? 224 ILE A C    1 
ATOM   1150 O O    . ILE A 1 224 ? 95.00400  110.27700 134.79400 1.000 49.27416  ? 224 ILE A O    1 
ATOM   1151 C CB   . ILE A 1 224 ? 93.87800  107.51500 136.20400 1.000 50.34386  ? 224 ILE A CB   1 
ATOM   1152 C CG1  . ILE A 1 224 ? 93.14000  106.23600 135.80500 1.000 49.89627  ? 224 ILE A CG1  1 
ATOM   1153 C CG2  . ILE A 1 224 ? 92.89400  108.64900 136.43200 1.000 50.56112  ? 224 ILE A CG2  1 
ATOM   1154 C CD1  . ILE A 1 224 ? 91.83200  106.48100 135.09500 1.000 51.67315  ? 224 ILE A CD1  1 
ATOM   1155 N N    . SER A 1 225 ? 96.50900  109.37700 136.19800 1.000 54.31161  ? 225 SER A N    1 
ATOM   1156 C CA   . SER A 1 225 ? 97.15100  110.66200 136.43800 1.000 53.35727  ? 225 SER A CA   1 
ATOM   1157 C C    . SER A 1 225 ? 97.94900  111.08900 135.21300 1.000 51.93355  ? 225 SER A C    1 
ATOM   1158 O O    . SER A 1 225 ? 97.74900  112.18200 134.67300 1.000 54.50334  ? 225 SER A O    1 
ATOM   1159 C CB   . SER A 1 225 ? 98.04700  110.58000 137.67400 1.000 53.84677  ? 225 SER A CB   1 
ATOM   1160 O OG   . SER A 1 225 ? 99.09300  109.64500 137.48000 1.000 56.41008  ? 225 SER A OG   1 
ATOM   1161 N N    . ARG A 1 226 ? 98.86600  110.23200 134.75900 1.000 46.29977  ? 226 ARG A N    1 
ATOM   1162 C CA   . ARG A 1 226 ? 99.71100  110.55500 133.61600 1.000 46.80751  ? 226 ARG A CA   1 
ATOM   1163 C C    . ARG A 1 226 ? 98.94300  110.67900 132.30300 1.000 50.84492  ? 226 ARG A C    1 
ATOM   1164 O O    . ARG A 1 226 ? 99.58100  110.91200 131.27200 1.000 55.41464  ? 226 ARG A O    1 
ATOM   1165 C CB   . ARG A 1 226 ? 100.81200 109.50200 133.46600 1.000 44.40740  ? 226 ARG A CB   1 
ATOM   1166 C CG   . ARG A 1 226 ? 101.38600 109.01700 134.78400 1.000 47.16915  ? 226 ARG A CG   1 
ATOM   1167 C CD   . ARG A 1 226 ? 102.80700 109.51600 134.98600 1.000 48.61829  ? 226 ARG A CD   1 
ATOM   1168 N NE   . ARG A 1 226 ? 103.66800 108.50600 135.59000 1.000 49.62131  ? 226 ARG A NE   1 
ATOM   1169 C CZ   . ARG A 1 226 ? 103.42900 107.90900 136.74900 1.000 51.14600  ? 226 ARG A CZ   1 
ATOM   1170 N NH1  . ARG A 1 226 ? 102.35900 108.20100 137.47000 1.000 49.15845  ? 226 ARG A NH1  1 
ATOM   1171 N NH2  . ARG A 1 226 ? 104.28500 106.99500 137.19700 1.000 50.44021  ? 226 ARG A NH2  1 
ATOM   1172 N N    . PHE A 1 227 ? 97.61800  110.53200 132.29100 1.000 43.46851  ? 227 PHE A N    1 
ATOM   1173 C CA   . PHE A 1 227 ? 96.87300  110.77800 131.06100 1.000 39.15686  ? 227 PHE A CA   1 
ATOM   1174 C C    . PHE A 1 227 ? 96.16900  112.13000 131.02900 1.000 41.09077  ? 227 PHE A C    1 
ATOM   1175 O O    . PHE A 1 227 ? 95.99100  112.70000 129.94400 1.000 43.25694  ? 227 PHE A O    1 
ATOM   1176 C CB   . PHE A 1 227 ? 95.83600  109.67200 130.83600 1.000 39.41189  ? 227 PHE A CB   1 
ATOM   1177 C CG   . PHE A 1 227 ? 95.26500  109.65400 129.44900 1.000 46.42962  ? 227 PHE A CG   1 
ATOM   1178 C CD1  . PHE A 1 227 ? 95.94500  109.03700 128.41300 1.000 46.85192  ? 227 PHE A CD1  1 
ATOM   1179 C CD2  . PHE A 1 227 ? 94.05100  110.26300 129.17700 1.000 46.94492  ? 227 PHE A CD2  1 
ATOM   1180 C CE1  . PHE A 1 227 ? 95.42400  109.02500 127.13300 1.000 47.63497  ? 227 PHE A CE1  1 
ATOM   1181 C CE2  . PHE A 1 227 ? 93.52400  110.25400 127.89900 1.000 42.16457  ? 227 PHE A CE2  1 
ATOM   1182 C CZ   . PHE A 1 227 ? 94.21200  109.63400 126.87600 1.000 45.51644  ? 227 PHE A CZ   1 
ATOM   1183 N N    . LEU A 1 228 ? 95.80700  112.68900 132.18700 1.000 38.36017  ? 228 LEU A N    1 
ATOM   1184 C CA   . LEU A 1 228 ? 95.18700  114.01000 132.18600 1.000 31.49936  ? 228 LEU A CA   1 
ATOM   1185 C C    . LEU A 1 228 ? 96.18700  115.10600 131.83800 1.000 37.41328  ? 228 LEU A C    1 
ATOM   1186 O O    . LEU A 1 228 ? 95.80700  116.12100 131.24200 1.000 42.20566  ? 228 LEU A O    1 
ATOM   1187 C CB   . LEU A 1 228 ? 94.54700  114.28700 133.54500 1.000 37.45857  ? 228 LEU A CB   1 
ATOM   1188 C CG   . LEU A 1 228 ? 93.49800  113.28000 134.02400 1.000 44.73555  ? 228 LEU A CG   1 
ATOM   1189 C CD1  . LEU A 1 228 ? 93.36900  113.31200 135.53900 1.000 40.40622  ? 228 LEU A CD1  1 
ATOM   1190 C CD2  . LEU A 1 228 ? 92.15400  113.54500 133.36500 1.000 43.46078  ? 228 LEU A CD2  1 
ATOM   1191 N N    . LEU A 1 229 ? 97.47400  114.89000 132.11100 1.000 33.62827  ? 229 LEU A N    1 
ATOM   1192 C CA   . LEU A 1 229 ? 98.46000  115.89700 131.74100 1.000 32.61976  ? 229 LEU A CA   1 
ATOM   1193 C C    . LEU A 1 229 ? 98.76300  115.84300 130.25100 1.000 30.41410  ? 229 LEU A C    1 
ATOM   1194 O O    . LEU A 1 229 ? 99.03600  116.88000 129.63100 1.000 42.57973  ? 229 LEU A O    1 
ATOM   1195 C CB   . LEU A 1 229 ? 99.73400  115.70000 132.56100 1.000 36.27921  ? 229 LEU A CB   1 
ATOM   1196 C CG   . LEU A 1 229 ? 99.56200  115.89600 134.06900 1.000 31.78242  ? 229 LEU A CG   1 
ATOM   1197 C CD1  . LEU A 1 229 ? 100.51800 115.00800 134.83800 1.000 32.76053  ? 229 LEU A CD1  1 
ATOM   1198 C CD2  . LEU A 1 229 ? 99.75100  117.35200 134.46000 1.000 33.00464  ? 229 LEU A CD2  1 
ATOM   1199 N N    . ILE A 1 230 ? 98.57500  114.67500 129.64000 1.000 21.22984  ? 230 ILE A N    1 
ATOM   1200 C CA   . ILE A 1 230 ? 98.72800  114.56000 128.19800 1.000 21.36962  ? 230 ILE A CA   1 
ATOM   1201 C C    . ILE A 1 230 ? 97.52400  115.17600 127.50900 1.000 25.41480  ? 230 ILE A C    1 
ATOM   1202 O O    . ILE A 1 230 ? 97.65500  115.85600 126.48300 1.000 33.20087  ? 230 ILE A O    1 
ATOM   1203 C CB   . ILE A 1 230 ? 98.91100  113.08200 127.80900 1.000 31.00103  ? 230 ILE A CB   1 
ATOM   1204 C CG1  . ILE A 1 230 ? 100.19300 112.51700 128.42100 1.000 27.91775  ? 230 ILE A CG1  1 
ATOM   1205 C CG2  . ILE A 1 230 ? 98.91800  112.92000 126.29800 1.000 30.12251  ? 230 ILE A CG2  1 
ATOM   1206 C CD1  . ILE A 1 230 ? 100.41700 111.05600 128.11700 1.000 27.13140  ? 230 ILE A CD1  1 
ATOM   1207 N N    . ALA A 1 231 ? 96.34000  114.99600 128.09700 1.000 24.58515  ? 231 ALA A N    1 
ATOM   1208 C CA   . ALA A 1 231 ? 95.15200  115.64400 127.55800 1.000 26.61055  ? 231 ALA A CA   1 
ATOM   1209 C C    . ALA A 1 231 ? 95.26200  117.16200 127.65500 1.000 26.23942  ? 231 ALA A C    1 
ATOM   1210 O O    . ALA A 1 231 ? 94.86800  117.87800 126.72700 1.000 30.10446  ? 231 ALA A O    1 
ATOM   1211 C CB   . ALA A 1 231 ? 93.90600  115.14700 128.28900 1.000 23.25990  ? 231 ALA A CB   1 
ATOM   1212 N N    . LEU A 1 232 ? 95.83500  117.67400 128.74800 1.000 23.43209  ? 232 LEU A N    1 
ATOM   1213 C CA   . LEU A 1 232 ? 95.97100  119.12200 128.88400 1.000 22.60912  ? 232 LEU A CA   1 
ATOM   1214 C C    . LEU A 1 232 ? 97.01000  119.68600 127.91900 1.000 30.25135  ? 232 LEU A C    1 
ATOM   1215 O O    . LEU A 1 232 ? 96.79700  120.75400 127.32100 1.000 36.10116  ? 232 LEU A O    1 
ATOM   1216 C CB   . LEU A 1 232 ? 96.33200  119.47500 130.32600 1.000 22.95342  ? 232 LEU A CB   1 
ATOM   1217 C CG   . LEU A 1 232 ? 96.59600  120.94700 130.64300 1.000 30.59843  ? 232 LEU A CG   1 
ATOM   1218 C CD1  . LEU A 1 232 ? 95.31900  121.63400 131.09900 1.000 31.18994  ? 232 LEU A CD1  1 
ATOM   1219 C CD2  . LEU A 1 232 ? 97.68400  121.08100 131.69500 1.000 28.84674  ? 232 LEU A CD2  1 
ATOM   1220 N N    . GLY A 1 233 ? 98.10900  118.96000 127.69800 1.000 20.53126  ? 233 GLY A N    1 
ATOM   1221 C CA   . GLY A 1 233 ? 99.08800  119.43100 126.73300 1.000 10.50312  ? 233 GLY A CA   1 
ATOM   1222 C C    . GLY A 1 233 ? 98.54900  119.41700 125.31500 1.000 19.60243  ? 233 GLY A C    1 
ATOM   1223 O O    . GLY A 1 233 ? 98.77700  120.35700 124.54300 1.000 26.77856  ? 233 GLY A O    1 
ATOM   1224 N N    . ALA A 1 234 ? 97.74900  118.40100 124.98000 1.000 22.99548  ? 234 ALA A N    1 
ATOM   1225 C CA   . ALA A 1 234 ? 97.18600  118.34700 123.63800 1.000 19.04239  ? 234 ALA A CA   1 
ATOM   1226 C C    . ALA A 1 234 ? 96.09400  119.39100 123.45200 1.000 22.51185  ? 234 ALA A C    1 
ATOM   1227 O O    . ALA A 1 234 ? 95.95900  119.95500 122.36000 1.000 24.98246  ? 234 ALA A O    1 
ATOM   1228 C CB   . ALA A 1 234 ? 96.64400  116.94900 123.35100 1.000 16.91280  ? 234 ALA A CB   1 
ATOM   1229 N N    . GLY A 1 235 ? 95.33600  119.69200 124.50700 1.000 16.66202  ? 235 GLY A N    1 
ATOM   1230 C CA   . GLY A 1 235 ? 94.33300  120.73700 124.40100 1.000 12.36752  ? 235 GLY A CA   1 
ATOM   1231 C C    . GLY A 1 235 ? 94.94500  122.10700 124.19200 1.000 18.13045  ? 235 GLY A C    1 
ATOM   1232 O O    . GLY A 1 235 ? 94.47400  122.88700 123.35600 1.000 27.28028  ? 235 GLY A O    1 
ATOM   1233 N N    . VAL A 1 236 ? 96.02000  122.41300 124.92500 1.000 18.15328  ? 236 VAL A N    1 
ATOM   1234 C CA   . VAL A 1 236 ? 96.67900  123.70000 124.71900 1.000 19.78267  ? 236 VAL A CA   1 
ATOM   1235 C C    . VAL A 1 236 ? 97.28800  123.77400 123.32300 1.000 19.86931  ? 236 VAL A C    1 
ATOM   1236 O O    . VAL A 1 236 ? 97.18500  124.80400 122.63800 1.000 24.98130  ? 236 VAL A O    1 
ATOM   1237 C CB   . VAL A 1 236 ? 97.73300  123.94600 125.81300 1.000 21.93537  ? 236 VAL A CB   1 
ATOM   1238 C CG1  . VAL A 1 236 ? 98.46000  125.25500 125.56200 1.000 17.35769  ? 236 VAL A CG1  1 
ATOM   1239 C CG2  . VAL A 1 236 ? 97.07900  123.95600 127.18500 1.000 19.22376  ? 236 VAL A CG2  1 
ATOM   1240 N N    . SER A 1 237 ? 97.89100  122.67400 122.85800 1.000 12.39312  ? 237 SER A N    1 
ATOM   1241 C CA   . SER A 1 237 ? 98.46800  122.67300 121.51700 1.000 7.16312   ? 237 SER A CA   1 
ATOM   1242 C C    . SER A 1 237 ? 97.39900  122.92600 120.46100 1.000 22.05861  ? 237 SER A C    1 
ATOM   1243 O O    . SER A 1 237 ? 97.58400  123.75000 119.55500 1.000 21.86133  ? 237 SER A O    1 
ATOM   1244 C CB   . SER A 1 237 ? 99.18100  121.34700 121.25200 1.000 13.48262  ? 237 SER A CB   1 
ATOM   1245 O OG   . SER A 1 237 ? 100.08200 121.03100 122.29500 1.000 22.83856  ? 237 SER A OG   1 
ATOM   1246 N N    . LEU A 1 238 ? 96.25500  122.24500 120.57700 1.000 27.43941  ? 238 LEU A N    1 
ATOM   1247 C CA   . LEU A 1 238 ? 95.21600  122.38300 119.56400 1.000 17.54412  ? 238 LEU A CA   1 
ATOM   1248 C C    . LEU A 1 238 ? 94.59400  123.77200 119.58700 1.000 25.71962  ? 238 LEU A C    1 
ATOM   1249 O O    . LEU A 1 238 ? 94.32300  124.34900 118.52800 1.000 33.07326  ? 238 LEU A O    1 
ATOM   1250 C CB   . LEU A 1 238 ? 94.14000  121.31800 119.76600 1.000 20.66489  ? 238 LEU A CB   1 
ATOM   1251 C CG   . LEU A 1 238 ? 93.27000  120.97200 118.55700 1.000 30.00494  ? 238 LEU A CG   1 
ATOM   1252 C CD1  . LEU A 1 238 ? 94.11000  120.43200 117.41300 1.000 29.59437  ? 238 LEU A CD1  1 
ATOM   1253 C CD2  . LEU A 1 238 ? 92.19100  119.98200 118.95100 1.000 27.09790  ? 238 LEU A CD2  1 
ATOM   1254 N N    . GLY A 1 239 ? 94.39700  124.34900 120.77400 1.000 17.56531  ? 239 GLY A N    1 
ATOM   1255 C CA   . GLY A 1 239 ? 93.83000  125.68500 120.82500 1.000 17.02169  ? 239 GLY A CA   1 
ATOM   1256 C C    . GLY A 1 239 ? 94.75200  126.72600 120.22200 1.000 21.49017  ? 239 GLY A C    1 
ATOM   1257 O O    . GLY A 1 239 ? 94.32300  127.55800 119.40800 1.000 25.23640  ? 239 GLY A O    1 
ATOM   1258 N N    . VAL A 1 240 ? 96.04500  126.65400 120.55300 1.000 26.76079  ? 240 VAL A N    1 
ATOM   1259 C CA   . VAL A 1 240 ? 96.97200  127.64700 120.02300 1.000 21.75819  ? 240 VAL A CA   1 
ATOM   1260 C C    . VAL A 1 240 ? 97.15100  127.46700 118.52300 1.000 17.74198  ? 240 VAL A C    1 
ATOM   1261 O O    . VAL A 1 240 ? 97.32200  128.45000 117.79200 1.000 14.38532  ? 240 VAL A O    1 
ATOM   1262 C CB   . VAL A 1 240 ? 98.31900  127.58400 120.76600 1.000 17.27431  ? 240 VAL A CB   1 
ATOM   1263 C CG1  . VAL A 1 240 ? 99.30300  128.57300 120.16300 1.000 13.16697  ? 240 VAL A CG1  1 
ATOM   1264 C CG2  . VAL A 1 240 ? 98.11500  127.87000 122.24000 1.000 17.01599  ? 240 VAL A CG2  1 
ATOM   1265 N N    . ASN A 1 241 ? 97.11500  126.22600 118.02900 1.000 14.80117  ? 241 ASN A N    1 
ATOM   1266 C CA   . ASN A 1 241 ? 97.29500  126.02100 116.59700 1.000 12.10717  ? 241 ASN A CA   1 
ATOM   1267 C C    . ASN A 1 241 ? 96.06500  126.46000 115.81300 1.000 26.51791  ? 241 ASN A C    1 
ATOM   1268 O O    . ASN A 1 241 ? 96.18900  127.03600 114.72700 1.000 23.56471  ? 241 ASN A O    1 
ATOM   1269 C CB   . ASN A 1 241 ? 97.61300  124.55600 116.30400 1.000 12.58951  ? 241 ASN A CB   1 
ATOM   1270 C CG   . ASN A 1 241 ? 98.49900  124.38500 115.08700 1.000 16.22760  ? 241 ASN A CG   1 
ATOM   1271 O OD1  . ASN A 1 241 ? 99.26300  125.27900 114.73300 1.000 25.94602  ? 241 ASN A OD1  1 
ATOM   1272 N ND2  . ASN A 1 241 ? 98.39200  123.23800 114.43300 1.000 11.40705  ? 241 ASN A ND2  1 
ATOM   1273 N N    . MET A 1 242 ? 94.86900  126.20400 116.34500 1.000 27.85521  ? 242 MET A N    1 
ATOM   1274 C CA   . MET A 1 242 ? 93.65800  126.47300 115.58600 1.000 19.56676  ? 242 MET A CA   1 
ATOM   1275 C C    . MET A 1 242 ? 93.17700  127.91600 115.67400 1.000 23.43637  ? 242 MET A C    1 
ATOM   1276 O O    . MET A 1 242 ? 92.43600  128.34900 114.78600 1.000 29.30753  ? 242 MET A O    1 
ATOM   1277 C CB   . MET A 1 242 ? 92.53900  125.53300 116.03900 1.000 30.90828  ? 242 MET A CB   1 
ATOM   1278 C CG   . MET A 1 242 ? 91.19000  125.82900 115.41000 1.000 30.57152  ? 242 MET A CG   1 
ATOM   1279 S SD   . MET A 1 242 ? 90.30400  124.33700 114.92600 1.000 53.45998  ? 242 MET A SD   1 
ATOM   1280 C CE   . MET A 1 242 ? 90.92500  123.16900 116.13100 1.000 31.82659  ? 242 MET A CE   1 
ATOM   1281 N N    . PHE A 1 243 ? 93.56500  128.68300 116.69600 1.000 24.15671  ? 243 PHE A N    1 
ATOM   1282 C CA   . PHE A 1 243 ? 92.99200  130.01900 116.84000 1.000 20.15220  ? 243 PHE A CA   1 
ATOM   1283 C C    . PHE A 1 243 ? 93.98100  131.16300 116.62900 1.000 18.72290  ? 243 PHE A C    1 
ATOM   1284 O O    . PHE A 1 243 ? 93.62600  132.31600 116.88800 1.000 25.92255  ? 243 PHE A O    1 
ATOM   1285 C CB   . PHE A 1 243 ? 92.31800  130.15900 118.20600 1.000 17.57353  ? 243 PHE A CB   1 
ATOM   1286 C CG   . PHE A 1 243 ? 91.22200  129.16400 118.44100 1.000 23.92629  ? 243 PHE A CG   1 
ATOM   1287 C CD1  . PHE A 1 243 ? 90.03300  129.25200 117.73900 1.000 26.02767  ? 243 PHE A CD1  1 
ATOM   1288 C CD2  . PHE A 1 243 ? 91.37800  128.13900 119.35600 1.000 25.32266  ? 243 PHE A CD2  1 
ATOM   1289 C CE1  . PHE A 1 243 ? 89.01900  128.33800 117.94700 1.000 26.28259  ? 243 PHE A CE1  1 
ATOM   1290 C CE2  . PHE A 1 243 ? 90.36800  127.22200 119.56800 1.000 21.57073  ? 243 PHE A CE2  1 
ATOM   1291 C CZ   . PHE A 1 243 ? 89.18700  127.32200 118.86200 1.000 24.72595  ? 243 PHE A CZ   1 
ATOM   1292 N N    . ILE A 1 244 ? 95.19800  130.89500 116.16100 1.000 21.46035  ? 244 ILE A N    1 
ATOM   1293 C CA   . ILE A 1 244 ? 96.18100  131.94600 115.88600 1.000 15.93271  ? 244 ILE A CA   1 
ATOM   1294 C C    . ILE A 1 244 ? 96.77400  131.68800 114.50300 1.000 18.96655  ? 244 ILE A C    1 
ATOM   1295 O O    . ILE A 1 244 ? 97.77500  130.97900 114.36100 1.000 29.40582  ? 244 ILE A O    1 
ATOM   1296 C CB   . ILE A 1 244 ? 97.27700  132.02700 116.95300 1.000 22.29662  ? 244 ILE A CB   1 
ATOM   1297 C CG1  . ILE A 1 244 ? 96.66300  131.95600 118.35300 1.000 19.64324  ? 244 ILE A CG1  1 
ATOM   1298 C CG2  . ILE A 1 244 ? 98.07800  133.30600 116.79500 1.000 13.62671  ? 244 ILE A CG2  1 
ATOM   1299 C CD1  . ILE A 1 244 ? 97.59400  132.40500 119.45000 1.000 11.56672  ? 244 ILE A CD1  1 
ATOM   1300 N N    . TYR A 1 245 ? 96.15900  132.26600 113.47100 1.000 17.46124  ? 245 TYR A N    1 
ATOM   1301 C CA   . TYR A 1 245 ? 96.64100  132.15900 112.09700 1.000 20.20599  ? 245 TYR A CA   1 
ATOM   1302 C C    . TYR A 1 245 ? 96.77200  130.70700 111.65100 1.000 23.33993  ? 245 TYR A C    1 
ATOM   1303 O O    . TYR A 1 245 ? 97.88500  130.23800 111.38300 1.000 28.60216  ? 245 TYR A O    1 
ATOM   1304 C CB   . TYR A 1 245 ? 97.97900  132.88300 111.94300 1.000 21.07757  ? 245 TYR A CB   1 
ATOM   1305 C CG   . TYR A 1 245 ? 97.86100  134.38500 112.04400 1.000 24.94858  ? 245 TYR A CG   1 
ATOM   1306 C CD1  . TYR A 1 245 ? 97.94900  135.02900 113.26900 1.000 26.83775  ? 245 TYR A CD1  1 
ATOM   1307 C CD2  . TYR A 1 245 ? 97.64600  135.16000 110.91300 1.000 29.46355  ? 245 TYR A CD2  1 
ATOM   1308 C CE1  . TYR A 1 245 ? 97.83300  136.40100 113.36600 1.000 24.01371  ? 245 TYR A CE1  1 
ATOM   1309 C CE2  . TYR A 1 245 ? 97.52800  136.53300 110.99900 1.000 31.66730  ? 245 TYR A CE2  1 
ATOM   1310 C CZ   . TYR A 1 245 ? 97.62300  137.14800 112.22900 1.000 32.95082  ? 245 TYR A CZ   1 
ATOM   1311 O OH   . TYR A 1 245 ? 97.50900  138.51600 112.31900 1.000 39.52160  ? 245 TYR A OH   1 
ATOM   1312 N N    . PRO A 1 246 ? 95.66700  129.97200 111.55100 1.000 21.52101  ? 246 PRO A N    1 
ATOM   1313 C CA   . PRO A 1 246 ? 95.74900  128.56800 111.13300 1.000 16.99615  ? 246 PRO A CA   1 
ATOM   1314 C C    . PRO A 1 246 ? 96.25200  128.41800 109.70500 1.000 15.14213  ? 246 PRO A C    1 
ATOM   1315 O O    . PRO A 1 246 ? 96.05700  129.28800 108.85500 1.000 19.42200  ? 246 PRO A O    1 
ATOM   1316 C CB   . PRO A 1 246 ? 94.30200  128.07500 111.26300 1.000 15.00643  ? 246 PRO A CB   1 
ATOM   1317 C CG   . PRO A 1 246 ? 93.47100  129.31700 111.26300 1.000 16.26364  ? 246 PRO A CG   1 
ATOM   1318 C CD   . PRO A 1 246 ? 94.29900  130.35700 111.92900 1.000 15.98951  ? 246 PRO A CD   1 
ATOM   1319 N N    . ILE A 1 247 ? 96.92200  127.29500 109.45500 1.000 17.78324  ? 247 ILE A N    1 
ATOM   1320 C CA   . ILE A 1 247 ? 97.38900  126.91700 108.12500 1.000 8.25109   ? 247 ILE A CA   1 
ATOM   1321 C C    . ILE A 1 247 ? 96.62800  125.66300 107.72400 1.000 9.69487   ? 247 ILE A C    1 
ATOM   1322 O O    . ILE A 1 247 ? 96.71100  124.63400 108.40500 1.000 22.40697  ? 247 ILE A O    1 
ATOM   1323 C CB   . ILE A 1 247 ? 98.90500  126.67800 108.09400 1.000 16.95361  ? 247 ILE A CB   1 
ATOM   1324 C CG1  . ILE A 1 247 ? 99.66200  127.98700 108.30600 1.000 18.36414  ? 247 ILE A CG1  1 
ATOM   1325 C CG2  . ILE A 1 247 ? 99.31800  126.03800 106.78000 1.000 5.04397   ? 247 ILE A CG2  1 
ATOM   1326 C CD1  . ILE A 1 247 ? 101.14900 127.80000 108.48000 1.000 17.52461  ? 247 ILE A CD1  1 
ATOM   1327 N N    . TRP A 1 248 ? 95.89500  125.74300 106.62000 1.000 24.20273  ? 248 TRP A N    1 
ATOM   1328 C CA   . TRP A 1 248 ? 95.03200  124.65900 106.17700 1.000 11.42324  ? 248 TRP A CA   1 
ATOM   1329 C C    . TRP A 1 248 ? 95.70400  123.83600 105.08500 1.000 10.16514  ? 248 TRP A C    1 
ATOM   1330 O O    . TRP A 1 248 ? 96.55200  124.33100 104.34100 1.000 24.13655  ? 248 TRP A O    1 
ATOM   1331 C CB   . TRP A 1 248 ? 93.69700  125.21000 105.67800 1.000 8.40904   ? 248 TRP A CB   1 
ATOM   1332 C CG   . TRP A 1 248 ? 93.06300  126.16200 106.64400 1.000 19.41391  ? 248 TRP A CG   1 
ATOM   1333 C CD1  . TRP A 1 248 ? 93.25300  127.51000 106.71100 1.000 17.55656  ? 248 TRP A CD1  1 
ATOM   1334 C CD2  . TRP A 1 248 ? 92.14000  125.83500 107.68900 1.000 19.20914  ? 248 TRP A CD2  1 
ATOM   1335 N NE1  . TRP A 1 248 ? 92.50300  128.04400 107.72700 1.000 13.04107  ? 248 TRP A NE1  1 
ATOM   1336 C CE2  . TRP A 1 248 ? 91.81000  127.03600 108.34300 1.000 16.82956  ? 248 TRP A CE2  1 
ATOM   1337 C CE3  . TRP A 1 248 ? 91.55900  124.64400 108.13100 1.000 20.49944  ? 248 TRP A CE3  1 
ATOM   1338 C CZ2  . TRP A 1 248 ? 90.92400  127.08000 109.41700 1.000 9.36089   ? 248 TRP A CZ2  1 
ATOM   1339 C CZ3  . TRP A 1 248 ? 90.68100  124.69000 109.19500 1.000 18.83037  ? 248 TRP A CZ3  1 
ATOM   1340 C CH2  . TRP A 1 248 ? 90.37200  125.89900 109.82700 1.000 16.36082  ? 248 TRP A CH2  1 
ATOM   1341 N N    . ALA A 1 249 ? 95.31000  122.56700 104.99800 1.000 12.68668  ? 249 ALA A N    1 
ATOM   1342 C CA   . ALA A 1 249 ? 95.90400  121.64000 104.04700 1.000 17.13851  ? 249 ALA A CA   1 
ATOM   1343 C C    . ALA A 1 249 ? 95.18400  121.59500 102.70500 1.000 25.14282  ? 249 ALA A C    1 
ATOM   1344 O O    . ALA A 1 249 ? 95.69900  120.97100 101.77200 1.000 32.46743  ? 249 ALA A O    1 
ATOM   1345 C CB   . ALA A 1 249 ? 95.94900  120.22900 104.64400 1.000 17.65798  ? 249 ALA A CB   1 
ATOM   1346 N N    . GLY A 1 250 ? 94.02600  122.24000 102.57000 1.000 18.07965  ? 250 GLY A N    1 
ATOM   1347 C CA   . GLY A 1 250 ? 93.40100  122.29400 101.26500 1.000 18.84897  ? 250 GLY A CA   1 
ATOM   1348 C C    . GLY A 1 250 ? 93.80400  123.49400 100.45100 1.000 32.96640  ? 250 GLY A C    1 
ATOM   1349 O O    . GLY A 1 250 ? 93.72100  123.47100 99.21500  1.000 46.65711  ? 250 GLY A O    1 
ATOM   1350 N N    . GLU A 1 251 ? 94.39400  124.48600 101.11100 1.000 29.27800  ? 251 GLU A N    1 
ATOM   1351 C CA   . GLU A 1 251 ? 94.86600  125.68400 100.44400 1.000 28.99099  ? 251 GLU A CA   1 
ATOM   1352 C C    . GLU A 1 251 ? 96.28500  125.52100 99.93800  1.000 31.33061  ? 251 GLU A C    1 
ATOM   1353 O O    . GLU A 1 251 ? 96.77100  126.38700 99.20300  1.000 40.57501  ? 251 GLU A O    1 
ATOM   1354 C CB   . GLU A 1 251 ? 94.79700  126.88700 101.38800 1.000 33.38769  ? 251 GLU A CB   1 
ATOM   1355 C CG   . GLU A 1 251 ? 93.41700  127.17600 101.93900 1.000 29.22391  ? 251 GLU A CG   1 
ATOM   1356 C CD   . GLU A 1 251 ? 93.33600  128.54000 102.59000 1.000 38.62493  ? 251 GLU A CD   1 
ATOM   1357 O OE1  . GLU A 1 251 ? 94.36400  129.24900 102.60600 1.000 42.26141  ? 251 GLU A OE1  1 
ATOM   1358 O OE2  . GLU A 1 251 ? 92.25000  128.90200 103.08900 1.000 41.95642  ? 251 GLU A OE2  1 
ATOM   1359 N N    . ASP A 1 252 ? 96.95400  124.43300 100.31200 1.000 28.95430  ? 252 ASP A N    1 
ATOM   1360 C CA   . ASP A 1 252 ? 98.23900  124.10700 99.72200  1.000 31.18415  ? 252 ASP A CA   1 
ATOM   1361 C C    . ASP A 1 252 ? 98.08000  123.19100 98.52300  1.000 35.18170  ? 252 ASP A C    1 
ATOM   1362 O O    . ASP A 1 252 ? 98.88900  123.26200 97.59500  1.000 39.98592  ? 252 ASP A O    1 
ATOM   1363 C CB   . ASP A 1 252 ? 99.14700  123.43700 100.75700 1.000 32.22991  ? 252 ASP A CB   1 
ATOM   1364 C CG   . ASP A 1 252 ? 99.31900  124.26900 102.00600 1.000 36.10893  ? 252 ASP A CG   1 
ATOM   1365 O OD1  . ASP A 1 252 ? 98.30500  124.76500 102.53300 1.000 38.52475  ? 252 ASP A OD1  1 
ATOM   1366 O OD2  . ASP A 1 252 ? 100.46900 124.42200 102.46400 1.000 41.60103  ? 252 ASP A OD2  1 
ATOM   1367 N N    . LEU A 1 253 ? 96.96400  122.46900 98.44200  1.000 34.97357  ? 253 LEU A N    1 
ATOM   1368 C CA   . LEU A 1 253 ? 96.67500  121.62200 97.29400  1.000 32.84116  ? 253 LEU A CA   1 
ATOM   1369 C C    . LEU A 1 253 ? 96.01100  122.42600 96.18500  1.000 30.73307  ? 253 LEU A C    1 
ATOM   1370 O O    . LEU A 1 253 ? 96.34800  122.26200 95.00000  1.000 44.14906  ? 253 LEU A O    1 
ATOM   1371 C CB   . LEU A 1 253 ? 95.78000  120.45700 97.72800  1.000 29.60437  ? 253 LEU A CB   1 
ATOM   1372 C CG   . LEU A 1 253 ? 95.34200  119.40900 96.70500  1.000 35.57978  ? 253 LEU A CG   1 
ATOM   1373 C CD1  . LEU A 1 253 ? 96.52700  118.59100 96.22700  1.000 35.79077  ? 253 LEU A CD1  1 
ATOM   1374 C CD2  . LEU A 1 253 ? 94.27700  118.50900 97.30800  1.000 25.55834  ? 253 LEU A CD2  1 
ATOM   1375 N N    . HIS A 1 254 ? 95.14200  123.36700 96.56800  1.000 24.41419  ? 254 HIS A N    1 
ATOM   1376 C CA   . HIS A 1 254 ? 94.56400  124.26800 95.58300  1.000 27.09965  ? 254 HIS A CA   1 
ATOM   1377 C C    . HIS A 1 254 ? 95.65600  125.11800 94.94200  1.000 30.46142  ? 254 HIS A C    1 
ATOM   1378 O O    . HIS A 1 254 ? 95.58900  125.43500 93.74900  1.000 36.49706  ? 254 HIS A O    1 
ATOM   1379 C CB   . HIS A 1 254 ? 93.49600  125.13600 96.25500  1.000 22.03665  ? 254 HIS A CB   1 
ATOM   1380 C CG   . HIS A 1 254 ? 92.96300  126.23600 95.39100  1.000 35.08460  ? 254 HIS A CG   1 
ATOM   1381 N ND1  . HIS A 1 254 ? 91.75300  126.14600 94.73800  1.000 35.81986  ? 254 HIS A ND1  1 
ATOM   1382 C CD2  . HIS A 1 254 ? 93.46200  127.45800 95.09100  1.000 40.45966  ? 254 HIS A CD2  1 
ATOM   1383 C CE1  . HIS A 1 254 ? 91.53500  127.26000 94.06400  1.000 30.11641  ? 254 HIS A CE1  1 
ATOM   1384 N NE2  . HIS A 1 254 ? 92.55700  128.07200 94.26000  1.000 37.70886  ? 254 HIS A NE2  1 
ATOM   1385 N N    . ASN A 1 255 ? 96.67300  125.49200 95.72300  1.000 21.18562  ? 255 ASN A N    1 
ATOM   1386 C CA   . ASN A 1 255 ? 97.79500  126.26600 95.20300  1.000 25.21199  ? 255 ASN A CA   1 
ATOM   1387 C C    . ASN A 1 255 ? 98.76800  125.40300 94.40100  1.000 32.70766  ? 255 ASN A C    1 
ATOM   1388 O O    . ASN A 1 255 ? 99.33000  125.86300 93.39900  1.000 36.92816  ? 255 ASN A O    1 
ATOM   1389 C CB   . ASN A 1 255 ? 98.53100  126.94700 96.35700  1.000 31.98433  ? 255 ASN A CB   1 
ATOM   1390 C CG   . ASN A 1 255 ? 97.77600  128.13800 96.91200  1.000 35.09141  ? 255 ASN A CG   1 
ATOM   1391 O OD1  . ASN A 1 255 ? 96.74800  128.54400 96.37400  1.000 37.33014  ? 255 ASN A OD1  1 
ATOM   1392 N ND2  . ASN A 1 255 ? 98.28500  128.70200 97.99900  1.000 32.44904  ? 255 ASN A ND2  1 
ATOM   1393 N N    . LEU A 1 256 ? 98.98600  124.15500 94.83000  1.000 31.08963  ? 256 LEU A N    1 
ATOM   1394 C CA   . LEU A 1 256 ? 99.89900  123.27000 94.11700  1.000 30.69059  ? 256 LEU A CA   1 
ATOM   1395 C C    . LEU A 1 256 ? 99.40000  122.97100 92.70900  1.000 32.56524  ? 256 LEU A C    1 
ATOM   1396 O O    . LEU A 1 256 ? 100.19400 122.91700 91.75800  1.000 39.39907  ? 256 LEU A O    1 
ATOM   1397 C CB   . LEU A 1 256 ? 100.09300 121.98200 94.91700  1.000 29.77930  ? 256 LEU A CB   1 
ATOM   1398 C CG   . LEU A 1 256 ? 101.00600 120.89600 94.35000  1.000 38.29176  ? 256 LEU A CG   1 
ATOM   1399 C CD1  . LEU A 1 256 ? 102.45500 121.33700 94.40400  1.000 35.05144  ? 256 LEU A CD1  1 
ATOM   1400 C CD2  . LEU A 1 256 ? 100.81700 119.60900 95.12700  1.000 34.06573  ? 256 LEU A CD2  1 
ATOM   1401 N N    . VAL A 1 257 ? 98.08800  122.77400 92.54800  1.000 22.92149  ? 257 VAL A N    1 
ATOM   1402 C CA   . VAL A 1 257 ? 97.56600  122.51400 91.20700  1.000 29.21210  ? 257 VAL A CA   1 
ATOM   1403 C C    . VAL A 1 257 ? 97.84200  123.70200 90.28700  1.000 28.56545  ? 257 VAL A C    1 
ATOM   1404 O O    . VAL A 1 257 ? 98.28600  123.54000 89.13700  1.000 34.29903  ? 257 VAL A O    1 
ATOM   1405 C CB   . VAL A 1 257 ? 96.06300  122.18700 91.27800  1.000 28.40072  ? 257 VAL A CB   1 
ATOM   1406 C CG1  . VAL A 1 257 ? 95.45800  122.14100 89.88500  1.000 25.89760  ? 257 VAL A CG1  1 
ATOM   1407 C CG2  . VAL A 1 257 ? 95.83900  120.87300 92.00800  1.000 26.06542  ? 257 VAL A CG2  1 
ATOM   1408 N N    . VAL A 1 258 ? 97.63000  124.91700 90.79800  1.000 28.79453  ? 258 VAL A N    1 
ATOM   1409 C CA   . VAL A 1 258 ? 97.83300  126.11500 89.99300  1.000 30.75012  ? 258 VAL A CA   1 
ATOM   1410 C C    . VAL A 1 258 ? 99.30700  126.30900 89.67000  1.000 29.60367  ? 258 VAL A C    1 
ATOM   1411 O O    . VAL A 1 258 ? 99.65100  126.82100 88.59900  1.000 33.68306  ? 258 VAL A O    1 
ATOM   1412 C CB   . VAL A 1 258 ? 97.24700  127.34400 90.71100  1.000 36.03299  ? 258 VAL A CB   1 
ATOM   1413 C CG1  . VAL A 1 258 ? 97.47100  128.59800 89.88400  1.000 35.32774  ? 258 VAL A CG1  1 
ATOM   1414 C CG2  . VAL A 1 258 ? 95.77000  127.14200 90.98300  1.000 29.45263  ? 258 VAL A CG2  1 
ATOM   1415 N N    . LYS A 1 259 ? 100.20200 125.92000 90.58000  1.000 32.28277  ? 259 LYS A N    1 
ATOM   1416 C CA   . LYS A 1 259 ? 101.62700 126.05200 90.29200  1.000 30.69792  ? 259 LYS A CA   1 
ATOM   1417 C C    . LYS A 1 259 ? 102.07200 125.05400 89.22800  1.000 35.39666  ? 259 LYS A C    1 
ATOM   1418 O O    . LYS A 1 259 ? 102.89400 125.38100 88.35900  1.000 40.71138  ? 259 LYS A O    1 
ATOM   1419 C CB   . LYS A 1 259 ? 102.44100 125.87100 91.57100  1.000 32.94060  ? 259 LYS A CB   1 
ATOM   1420 C CG   . LYS A 1 259 ? 103.90600 126.24200 91.42400  1.000 41.56625  ? 259 LYS A CG   1 
ATOM   1421 C CD   . LYS A 1 259 ? 104.64400 126.12400 92.74500  1.000 42.10620  ? 259 LYS A CD   1 
ATOM   1422 C CE   . LYS A 1 259 ? 105.74300 125.07800 92.66400  1.000 44.09240  ? 259 LYS A CE   1 
ATOM   1423 N NZ   . LYS A 1 259 ? 105.19800 123.69300 92.73600  1.000 39.24730  ? 259 LYS A NZ   1 
ATOM   1424 N N    . ASN A 1 260 ? 101.53900 123.83100 89.27600  1.000 35.12283  ? 260 ASN A N    1 
ATOM   1425 C CA   . ASN A 1 260 ? 101.91000 122.84100 88.27000  1.000 35.96814  ? 260 ASN A CA   1 
ATOM   1426 C C    . ASN A 1 260 ? 101.42100 123.25900 86.88800  1.000 34.52520  ? 260 ASN A C    1 
ATOM   1427 O O    . ASN A 1 260 ? 102.11400 123.04300 85.87800  1.000 32.26109  ? 260 ASN A O    1 
ATOM   1428 C CB   . ASN A 1 260 ? 101.35100 121.47000 88.64900  1.000 34.94857  ? 260 ASN A CB   1 
ATOM   1429 C CG   . ASN A 1 260 ? 102.13200 120.81400 89.76900  1.000 38.89502  ? 260 ASN A CG   1 
ATOM   1430 O OD1  . ASN A 1 260 ? 103.28700 121.15200 90.01700  1.000 42.05423  ? 260 ASN A OD1  1 
ATOM   1431 N ND2  . ASN A 1 260 ? 101.50300 119.86500 90.45200  1.000 41.09570  ? 260 ASN A ND2  1 
ATOM   1432 N N    . PHE A 1 261 ? 100.23400 123.87600 86.82400  1.000 38.50789  ? 261 PHE A N    1 
ATOM   1433 C CA   . PHE A 1 261 ? 99.71400  124.30900 85.53000  1.000 30.40800  ? 261 PHE A CA   1 
ATOM   1434 C C    . PHE A 1 261 ? 100.62000 125.33800 84.86400  1.000 33.22671  ? 261 PHE A C    1 
ATOM   1435 O O    . PHE A 1 261 ? 100.63900 125.43700 83.63200  1.000 34.84943  ? 261 PHE A O    1 
ATOM   1436 C CB   . PHE A 1 261 ? 98.30100  124.86800 85.68100  1.000 29.30942  ? 261 PHE A CB   1 
ATOM   1437 C CG   . PHE A 1 261 ? 97.22300  123.89400 85.30700  1.000 32.97752  ? 261 PHE A CG   1 
ATOM   1438 C CD1  . PHE A 1 261 ? 96.91600  123.66400 83.97900  1.000 35.59476  ? 261 PHE A CD1  1 
ATOM   1439 C CD2  . PHE A 1 261 ? 96.52000  123.20700 86.27900  1.000 34.83070  ? 261 PHE A CD2  1 
ATOM   1440 C CE1  . PHE A 1 261 ? 95.92800  122.77000 83.62700  1.000 36.56757  ? 261 PHE A CE1  1 
ATOM   1441 C CE2  . PHE A 1 261 ? 95.53200  122.31100 85.93200  1.000 37.81885  ? 261 PHE A CE2  1 
ATOM   1442 C CZ   . PHE A 1 261 ? 95.23600  122.09300 84.60400  1.000 33.55778  ? 261 PHE A CZ   1 
ATOM   1443 N N    . MET A 1 262 ? 101.37300 126.11100 85.64600  1.000 29.47701  ? 262 MET A N    1 
ATOM   1444 C CA   . MET A 1 262 ? 102.28000 127.09800 85.07200  1.000 30.38202  ? 262 MET A CA   1 
ATOM   1445 C C    . MET A 1 262 ? 103.66100 126.52100 84.80500  1.000 34.72193  ? 262 MET A C    1 
ATOM   1446 O O    . MET A 1 262 ? 104.32000 126.91300 83.82800  1.000 36.42956  ? 262 MET A O    1 
ATOM   1447 C CB   . MET A 1 262 ? 102.40400 128.31400 85.99500  1.000 34.18327  ? 262 MET A CB   1 
ATOM   1448 C CG   . MET A 1 262 ? 101.09700 128.77300 86.61600  1.000 37.41487  ? 262 MET A CG   1 
ATOM   1449 S SD   . MET A 1 262 ? 100.10500 129.71700 85.44300  1.000 48.79550  ? 262 MET A SD   1 
ATOM   1450 C CE   . MET A 1 262 ? 98.51100  129.70900 86.25300  1.000 38.49297  ? 262 MET A CE   1 
ATOM   1451 N N    . ASN A 1 263 ? 104.09500 125.56800 85.63200  1.000 40.01629  ? 263 ASN A N    1 
ATOM   1452 C CA   . ASN A 1 263 ? 105.39000 124.94300 85.39300  1.000 33.51035  ? 263 ASN A CA   1 
ATOM   1453 C C    . ASN A 1 263 ? 105.38400 124.15400 84.09200  1.000 32.00269  ? 263 ASN A C    1 
ATOM   1454 O O    . ASN A 1 263 ? 106.37000 124.17400 83.34400  1.000 37.26798  ? 263 ASN A O    1 
ATOM   1455 C CB   . ASN A 1 263 ? 105.77100 124.04100 86.56600  1.000 35.68835  ? 263 ASN A CB   1 
ATOM   1456 C CG   . ASN A 1 263 ? 106.07400 124.82200 87.82600  1.000 42.18014  ? 263 ASN A CG   1 
ATOM   1457 O OD1  . ASN A 1 263 ? 106.25000 126.03800 87.78900  1.000 41.29389  ? 263 ASN A OD1  1 
ATOM   1458 N ND2  . ASN A 1 263 ? 106.14200 124.12300 88.95200  1.000 39.39919  ? 263 ASN A ND2  1 
ATOM   1459 N N    . VAL A 1 264 ? 104.28300 123.46000 83.79200  1.000 36.33854  ? 264 VAL A N    1 
ATOM   1460 C CA   . VAL A 1 264 ? 104.25200 122.68200 82.55500  1.000 35.28579  ? 264 VAL A CA   1 
ATOM   1461 C C    . VAL A 1 264 ? 104.32100 123.59700 81.33400  1.000 35.20429  ? 264 VAL A C    1 
ATOM   1462 O O    . VAL A 1 264 ? 105.00200 123.28800 80.34600  1.000 36.61450  ? 264 VAL A O    1 
ATOM   1463 C CB   . VAL A 1 264 ? 103.00500 121.78100 82.51900  1.000 28.90204  ? 264 VAL A CB   1 
ATOM   1464 C CG1  . VAL A 1 264 ? 102.92400 121.04500 81.19300  1.000 32.76198  ? 264 VAL A CG1  1 
ATOM   1465 C CG2  . VAL A 1 264 ? 103.03400 120.79500 83.67000  1.000 32.36489  ? 264 VAL A CG2  1 
ATOM   1466 N N    . ALA A 1 265 ? 103.64700 124.74900 81.38900  1.000 36.07038  ? 265 ALA A N    1 
ATOM   1467 C CA   . ALA A 1 265 ? 103.69400 125.68500 80.27000  1.000 35.36316  ? 265 ALA A CA   1 
ATOM   1468 C C    . ALA A 1 265 ? 105.09100 126.26600 80.09200  1.000 38.10419  ? 265 ALA A C    1 
ATOM   1469 O O    . ALA A 1 265 ? 105.59000 126.37700 78.96100  1.000 40.05180  ? 265 ALA A O    1 
ATOM   1470 C CB   . ALA A 1 265 ? 102.67100 126.80100 80.47400  1.000 34.65982  ? 265 ALA A CB   1 
ATOM   1471 N N    . THR A 1 266 ? 105.74600 126.62600 81.19900  1.000 39.04868  ? 266 THR A N    1 
ATOM   1472 C CA   . THR A 1 266 ? 107.10100 127.15300 81.08700  1.000 37.25803  ? 266 THR A CA   1 
ATOM   1473 C C    . THR A 1 266 ? 108.04200 126.10900 80.50200  1.000 40.02125  ? 266 THR A C    1 
ATOM   1474 O O    . THR A 1 266 ? 108.87900 126.42500 79.64800  1.000 41.58326  ? 266 THR A O    1 
ATOM   1475 C CB   . THR A 1 266 ? 107.60300 127.62500 82.45100  1.000 37.54193  ? 266 THR A CB   1 
ATOM   1476 O OG1  . THR A 1 266 ? 106.89100 128.80400 82.84200  1.000 40.03050  ? 266 THR A OG1  1 
ATOM   1477 C CG2  . THR A 1 266 ? 109.08700 127.93900 82.38900  1.000 37.47788  ? 266 THR A CG2  1 
ATOM   1478 N N    . SER A 1 267 ? 107.91800 124.85500 80.94600  1.000 44.31292  ? 267 SER A N    1 
ATOM   1479 C CA   . SER A 1 267 ? 108.77500 123.80000 80.41700  1.000 41.26779  ? 267 SER A CA   1 
ATOM   1480 C C    . SER A 1 267 ? 108.54600 123.59100 78.92500  1.000 43.64887  ? 267 SER A C    1 
ATOM   1481 O O    . SER A 1 267 ? 109.50600 123.43100 78.16100  1.000 46.45005  ? 267 SER A O    1 
ATOM   1482 C CB   . SER A 1 267 ? 108.54200 122.49900 81.18300  1.000 44.99511  ? 267 SER A CB   1 
ATOM   1483 O OG   . SER A 1 267 ? 109.07300 122.58300 82.49300  1.000 52.41384  ? 267 SER A OG   1 
ATOM   1484 N N    . LEU A 1 268 ? 107.28400 123.57800 78.48900  1.000 38.64151  ? 268 LEU A N    1 
ATOM   1485 C CA   . LEU A 1 268 ? 107.00700 123.38700 77.06700  1.000 35.80508  ? 268 LEU A CA   1 
ATOM   1486 C C    . LEU A 1 268 ? 107.62400 124.50500 76.23600  1.000 40.93473  ? 268 LEU A C    1 
ATOM   1487 O O    . LEU A 1 268 ? 108.26400 124.25400 75.20200  1.000 44.77246  ? 268 LEU A O    1 
ATOM   1488 C CB   . LEU A 1 268 ? 105.49900 123.31000 76.82700  1.000 36.22690  ? 268 LEU A CB   1 
ATOM   1489 C CG   . LEU A 1 268 ? 105.06500 123.19900 75.36200  1.000 36.69436  ? 268 LEU A CG   1 
ATOM   1490 C CD1  . LEU A 1 268 ? 105.16900 121.76700 74.86500  1.000 38.39816  ? 268 LEU A CD1  1 
ATOM   1491 C CD2  . LEU A 1 268 ? 103.65600 123.73300 75.17200  1.000 37.95938  ? 268 LEU A CD2  1 
ATOM   1492 N N    . GLU A 1 269 ? 107.45500 125.75300 76.68100  1.000 49.90315  ? 269 GLU A N    1 
ATOM   1493 C CA   . GLU A 1 269 ? 108.01600 126.86800 75.92600  1.000 46.05147  ? 269 GLU A CA   1 
ATOM   1494 C C    . GLU A 1 269 ? 109.53700 126.79800 75.89200  1.000 49.23130  ? 269 GLU A C    1 
ATOM   1495 O O    . GLU A 1 269 ? 110.15600 127.02100 74.84100  1.000 45.20216  ? 269 GLU A O    1 
ATOM   1496 C CB   . GLU A 1 269 ? 107.55500 128.19400 76.52700  1.000 47.67982  ? 269 GLU A CB   1 
ATOM   1497 C CG   . GLU A 1 269 ? 106.34700 128.80500 75.84300  1.000 49.72161  ? 269 GLU A CG   1 
ATOM   1498 C CD   . GLU A 1 269 ? 105.97300 130.15400 76.42400  1.000 55.63682  ? 269 GLU A CD   1 
ATOM   1499 O OE1  . GLU A 1 269 ? 106.24700 130.38300 77.62100  1.000 48.73940  ? 269 GLU A OE1  1 
ATOM   1500 O OE2  . GLU A 1 269 ? 105.40700 130.98600 75.68400  1.000 53.30264  ? 269 GLU A OE2  1 
ATOM   1501 N N    . GLY A 1 270 ? 110.15700 126.45500 77.02400  1.000 53.72218  ? 270 GLY A N    1 
ATOM   1502 C CA   . GLY A 1 270 ? 111.60500 126.35900 77.05700  1.000 48.82152  ? 270 GLY A CA   1 
ATOM   1503 C C    . GLY A 1 270 ? 112.14500 125.25500 76.16900  1.000 48.16479  ? 270 GLY A C    1 
ATOM   1504 O O    . GLY A 1 270 ? 113.17500 125.42300 75.51800  1.000 53.08955  ? 270 GLY A O    1 
ATOM   1505 N N    . CYS A 1 271 ? 111.43400 124.12800 76.09200  1.000 46.82725  ? 271 CYS A N    1 
ATOM   1506 C CA   . CYS A 1 271 ? 111.89600 123.04000 75.23400  1.000 46.51706  ? 271 CYS A CA   1 
ATOM   1507 C C    . CYS A 1 271 ? 111.77000 123.41100 73.76400  1.000 46.12550  ? 271 CYS A C    1 
ATOM   1508 O O    . CYS A 1 271 ? 112.69000 123.16200 72.96800  1.000 46.95930  ? 271 CYS A O    1 
ATOM   1509 C CB   . CYS A 1 271 ? 111.11300 121.76100 75.53000  1.000 47.47767  ? 271 CYS A CB   1 
ATOM   1510 S SG   . CYS A 1 271 ? 111.56200 120.94200 77.07500  1.000 59.78977  ? 271 CYS A SG   1 
ATOM   1511 N N    . VAL A 1 272 ? 110.64900 124.03200 73.38600  1.000 51.65897  ? 272 VAL A N    1 
ATOM   1512 C CA   . VAL A 1 272 ? 110.47200 124.36500 71.97700  1.000 50.46086  ? 272 VAL A CA   1 
ATOM   1513 C C    . VAL A 1 272 ? 111.46200 125.44100 71.55900  1.000 52.01524  ? 272 VAL A C    1 
ATOM   1514 O O    . VAL A 1 272 ? 111.93200 125.44700 70.41500  1.000 47.79022  ? 272 VAL A O    1 
ATOM   1515 C CB   . VAL A 1 272 ? 109.02100 124.78900 71.69000  1.000 52.64635  ? 272 VAL A CB   1 
ATOM   1516 C CG1  . VAL A 1 272 ? 108.87000 125.17700 70.23000  1.000 48.44014  ? 272 VAL A CG1  1 
ATOM   1517 C CG2  . VAL A 1 272 ? 108.06300 123.66500 72.04500  1.000 51.51074  ? 272 VAL A CG2  1 
ATOM   1518 N N    . ASN A 1 273 ? 111.79900 126.36700 72.46200  1.000 55.20877  ? 273 ASN A N    1 
ATOM   1519 C CA   . ASN A 1 273 ? 112.80900 127.36800 72.12800  1.000 53.07453  ? 273 ASN A CA   1 
ATOM   1520 C C    . ASN A 1 273 ? 114.20600 126.75800 72.08300  1.000 51.09186  ? 273 ASN A C    1 
ATOM   1521 O O    . ASN A 1 273 ? 115.00600 127.09400 71.20200  1.000 51.53089  ? 273 ASN A O    1 
ATOM   1522 C CB   . ASN A 1 273 ? 112.75900 128.52200 73.12800  1.000 50.99340  ? 273 ASN A CB   1 
ATOM   1523 C CG   . ASN A 1 273 ? 111.71500 129.55900 72.76900  1.000 53.22015  ? 273 ASN A CG   1 
ATOM   1524 O OD1  . ASN A 1 273 ? 111.23200 129.60500 71.63800  1.000 52.38271  ? 273 ASN A OD1  1 
ATOM   1525 N ND2  . ASN A 1 273 ? 111.36100 130.40000 73.73300  1.000 53.16964  ? 273 ASN A ND2  1 
ATOM   1526 N N    . GLY A 1 274 ? 114.51800 125.86200 73.02100  1.000 51.78884  ? 274 GLY A N    1 
ATOM   1527 C CA   . GLY A 1 274 ? 115.83500 125.24900 73.04500  1.000 50.95449  ? 274 GLY A CA   1 
ATOM   1528 C C    . GLY A 1 274 ? 116.13100 124.40100 71.82400  1.000 51.55513  ? 274 GLY A C    1 
ATOM   1529 O O    . GLY A 1 274 ? 117.27300 124.34700 71.36100  1.000 50.55155  ? 274 GLY A O    1 
ATOM   1530 N N    . TYR A 1 275 ? 115.11600 123.71800 71.28800  1.000 52.45756  ? 275 TYR A N    1 
ATOM   1531 C CA   . TYR A 1 275 ? 115.37400 122.87200 70.12400  1.000 49.57100  ? 275 TYR A CA   1 
ATOM   1532 C C    . TYR A 1 275 ? 115.80700 123.68900 68.91100  1.000 53.07800  ? 275 TYR A C    1 
ATOM   1533 O O    . TYR A 1 275 ? 116.68600 123.26500 68.15300  1.000 53.48356  ? 275 TYR A O    1 
ATOM   1534 C CB   . TYR A 1 275 ? 114.15000 122.02800 69.78300  1.000 51.18468  ? 275 TYR A CB   1 
ATOM   1535 C CG   . TYR A 1 275 ? 114.41000 121.05300 68.65500  1.000 53.35840  ? 275 TYR A CG   1 
ATOM   1536 C CD1  . TYR A 1 275 ? 115.04300 119.84000 68.89000  1.000 52.89107  ? 275 TYR A CD1  1 
ATOM   1537 C CD2  . TYR A 1 275 ? 114.01900 121.34500 67.35600  1.000 52.07040  ? 275 TYR A CD2  1 
ATOM   1538 C CE1  . TYR A 1 275 ? 115.28400 118.94900 67.86300  1.000 51.35919  ? 275 TYR A CE1  1 
ATOM   1539 C CE2  . TYR A 1 275 ? 114.25200 120.45900 66.32200  1.000 51.01382  ? 275 TYR A CE2  1 
ATOM   1540 C CZ   . TYR A 1 275 ? 114.88500 119.26300 66.58100  1.000 54.34631  ? 275 TYR A CZ   1 
ATOM   1541 O OH   . TYR A 1 275 ? 115.11800 118.37900 65.55500  1.000 54.36470  ? 275 TYR A OH   1 
ATOM   1542 N N    . LEU A 1 276 ? 115.20400 124.85600 68.70500  1.000 59.64168  ? 276 LEU A N    1 
ATOM   1543 C CA   . LEU A 1 276 ? 115.50000 125.67200 67.53500  1.000 57.28387  ? 276 LEU A CA   1 
ATOM   1544 C C    . LEU A 1 276 ? 116.64600 126.64800 67.75800  1.000 57.99068  ? 276 LEU A C    1 
ATOM   1545 O O    . LEU A 1 276 ? 116.97300 127.41300 66.84500  1.000 60.20760  ? 276 LEU A O    1 
ATOM   1546 C CB   . LEU A 1 276 ? 114.25100 126.44500 67.09800  1.000 60.21190  ? 276 LEU A CB   1 
ATOM   1547 C CG   . LEU A 1 276 ? 113.18600 125.66700 66.32300  1.000 58.65690  ? 276 LEU A CG   1 
ATOM   1548 C CD1  . LEU A 1 276 ? 111.95900 126.53200 66.09200  1.000 59.43433  ? 276 LEU A CD1  1 
ATOM   1549 C CD2  . LEU A 1 276 ? 113.74000 125.15900 65.00300  1.000 57.11836  ? 276 LEU A CD2  1 
ATOM   1550 N N    . ARG A 1 277 ? 117.26000 126.64500 68.93800  1.000 68.47088  ? 277 ARG A N    1 
ATOM   1551 C CA   . ARG A 1 277 ? 118.37800 127.54000 69.20000  1.000 69.95677  ? 277 ARG A CA   1 
ATOM   1552 C C    . ARG A 1 277 ? 119.51100 127.29000 68.21300  1.000 70.36594  ? 277 ARG A C    1 
ATOM   1553 O O    . ARG A 1 277 ? 119.77400 126.15100 67.81600  1.000 71.09253  ? 277 ARG A O    1 
ATOM   1554 C CB   . ARG A 1 277 ? 118.87700 127.35600 70.63300  1.000 70.17416  ? 277 ARG A CB   1 
ATOM   1555 C CG   . ARG A 1 277 ? 120.38200 127.47300 70.78900  1.000 69.02747  ? 277 ARG A CG   1 
ATOM   1556 C CD   . ARG A 1 277 ? 120.87300 126.67100 71.98100  1.000 70.95479  ? 277 ARG A CD   1 
ATOM   1557 N NE   . ARG A 1 277 ? 121.14200 125.28200 71.62800  1.000 73.36521  ? 277 ARG A NE   1 
ATOM   1558 C CZ   . ARG A 1 277 ? 121.19100 124.28400 72.50000  1.000 73.12815  ? 277 ARG A CZ   1 
ATOM   1559 N NH1  . ARG A 1 277 ? 120.99600 124.48400 73.79200  1.000 71.88761  ? 277 ARG A NH1  1 
ATOM   1560 N NH2  . ARG A 1 277 ? 121.44000 123.05300 72.06200  1.000 70.63514  ? 277 ARG A NH2  1 
ATOM   1561 N N    . CYS A 1 278 ? 120.18500 128.36500 67.81900  1.000 77.97696  ? 278 CYS A N    1 
ATOM   1562 C CA   . CYS A 1 278 ? 121.26500 128.27900 66.84300  1.000 79.43467  ? 278 CYS A CA   1 
ATOM   1563 C C    . CYS A 1 278 ? 122.59200 127.95600 67.52300  1.000 81.00456  ? 278 CYS A C    1 
ATOM   1564 O O    . CYS A 1 278 ? 123.61600 127.79000 66.86100  1.000 80.35927  ? 278 CYS A O    1 
ATOM   1565 C CB   . CYS A 1 278 ? 121.38300 129.58500 66.05500  1.000 79.48177  ? 278 CYS A CB   1 
ATOM   1566 S SG   . CYS A 1 278 ? 120.48400 129.59600 64.48700  1.000 84.96010  ? 278 CYS A SG   1 
ATOM   1567 N N    . VAL A 1 298 ? 113.13200 124.21700 82.06200  1.000 60.26197  ? 298 VAL A N    1 
ATOM   1568 C CA   . VAL A 1 298 ? 113.00100 123.21200 81.01600  1.000 64.94165  ? 298 VAL A CA   1 
ATOM   1569 C C    . VAL A 1 298 ? 113.00400 121.81700 81.62800  1.000 63.15914  ? 298 VAL A C    1 
ATOM   1570 O O    . VAL A 1 298 ? 112.61500 120.84200 80.98700  1.000 63.03665  ? 298 VAL A O    1 
ATOM   1571 C CB   . VAL A 1 298 ? 114.12300 123.35200 79.97400  1.000 61.68286  ? 298 VAL A CB   1 
ATOM   1572 C CG1  . VAL A 1 298 ? 113.91700 122.37200 78.83200  1.000 56.57779  ? 298 VAL A CG1  1 
ATOM   1573 C CG2  . VAL A 1 298 ? 114.18700 124.78000 79.45700  1.000 61.13074  ? 298 VAL A CG2  1 
ATOM   1574 N N    . TYR A 1 299 ? 113.45000 121.73600 82.87800  1.000 63.72524  ? 299 TYR A N    1 
ATOM   1575 C CA   . TYR A 1 299 ? 113.54200 120.48300 83.61600  1.000 66.69143  ? 299 TYR A CA   1 
ATOM   1576 C C    . TYR A 1 299 ? 112.75400 120.52100 84.91500  1.000 68.67842  ? 299 TYR A C    1 
ATOM   1577 O O    . TYR A 1 299 ? 111.97700 119.59700 85.20000  1.000 68.84805  ? 299 TYR A O    1 
ATOM   1578 C CB   . TYR A 1 299 ? 115.02300 120.16500 83.89000  1.000 69.25119  ? 299 TYR A CB   1 
ATOM   1579 C CG   . TYR A 1 299 ? 115.30300 118.76800 84.39500  1.000 69.77895  ? 299 TYR A CG   1 
ATOM   1580 C CD1  . TYR A 1 299 ? 115.19500 118.45900 85.74400  1.000 69.19146  ? 299 TYR A CD1  1 
ATOM   1581 C CD2  . TYR A 1 299 ? 115.68000 117.75800 83.52100  1.000 68.67402  ? 299 TYR A CD2  1 
ATOM   1582 C CE1  . TYR A 1 299 ? 115.46100 117.18400 86.20800  1.000 69.35623  ? 299 TYR A CE1  1 
ATOM   1583 C CE2  . TYR A 1 299 ? 115.94100 116.47900 83.97400  1.000 69.41917  ? 299 TYR A CE2  1 
ATOM   1584 C CZ   . TYR A 1 299 ? 115.82800 116.19800 85.31800  1.000 70.29436  ? 299 TYR A CZ   1 
ATOM   1585 O OH   . TYR A 1 299 ? 116.08800 114.92600 85.77400  1.000 66.94565  ? 299 TYR A OH   1 
ATOM   1586 N N    . LYS A 1 300 ? 112.92100 121.58600 85.70400  1.000 72.11026  ? 300 LYS A N    1 
ATOM   1587 C CA   . LYS A 1 300 ? 112.27700 121.65800 87.00900  1.000 72.26647  ? 300 LYS A CA   1 
ATOM   1588 C C    . LYS A 1 300 ? 110.76000 121.61900 86.88500  1.000 72.30261  ? 300 LYS A C    1 
ATOM   1589 O O    . LYS A 1 300 ? 110.08400 120.98800 87.70200  1.000 72.04522  ? 300 LYS A O    1 
ATOM   1590 C CB   . LYS A 1 300 ? 112.72200 122.92300 87.74300  1.000 70.30805  ? 300 LYS A CB   1 
ATOM   1591 N N    . GLY A 1 301 ? 110.20400 122.29100 85.88100  1.000 63.39448  ? 301 GLY A N    1 
ATOM   1592 C CA   . GLY A 1 301 ? 108.76200 122.33800 85.73600  1.000 59.18516  ? 301 GLY A CA   1 
ATOM   1593 C C    . GLY A 1 301 ? 108.11500 120.97300 85.61500  1.000 60.69441  ? 301 GLY A C    1 
ATOM   1594 O O    . GLY A 1 301 ? 107.28500 120.58700 86.44900  1.000 66.28937  ? 301 GLY A O    1 
ATOM   1595 N N    . TYR A 1 302 ? 108.50000 120.21900 84.58300  1.000 57.00554  ? 302 TYR A N    1 
ATOM   1596 C CA   . TYR A 1 302 ? 107.91500 118.89700 84.39800  1.000 60.32251  ? 302 TYR A CA   1 
ATOM   1597 C C    . TYR A 1 302 ? 108.35500 117.93000 85.49000  1.000 59.99710  ? 302 TYR A C    1 
ATOM   1598 O O    . TYR A 1 302 ? 107.59200 117.03000 85.85500  1.000 62.97313  ? 302 TYR A O    1 
ATOM   1599 C CB   . TYR A 1 302 ? 108.22900 118.36600 82.99100  1.000 60.34882  ? 302 TYR A CB   1 
ATOM   1600 C CG   . TYR A 1 302 ? 109.62400 117.82300 82.74700  1.000 60.15859  ? 302 TYR A CG   1 
ATOM   1601 C CD1  . TYR A 1 302 ? 110.05500 116.64100 83.33800  1.000 59.97918  ? 302 TYR A CD1  1 
ATOM   1602 C CD2  . TYR A 1 302 ? 110.49900 118.48100 81.89400  1.000 60.06385  ? 302 TYR A CD2  1 
ATOM   1603 C CE1  . TYR A 1 302 ? 111.32200 116.14500 83.10200  1.000 59.64546  ? 302 TYR A CE1  1 
ATOM   1604 C CE2  . TYR A 1 302 ? 111.76600 117.99200 81.65200  1.000 59.85894  ? 302 TYR A CE2  1 
ATOM   1605 C CZ   . TYR A 1 302 ? 112.17200 116.82400 82.25900  1.000 61.26615  ? 302 TYR A CZ   1 
ATOM   1606 O OH   . TYR A 1 302 ? 113.43500 116.33400 82.02100  1.000 60.91496  ? 302 TYR A OH   1 
ATOM   1607 N N    . ARG A 1 303 ? 109.56600 118.09500 86.03400  1.000 64.13300  ? 303 ARG A N    1 
ATOM   1608 C CA   . ARG A 1 303 ? 109.98200 117.22200 87.12800  1.000 65.89525  ? 303 ARG A CA   1 
ATOM   1609 C C    . ARG A 1 303 ? 109.10100 117.41900 88.35500  1.000 66.51873  ? 303 ARG A C    1 
ATOM   1610 O O    . ARG A 1 303 ? 108.76000 116.45300 89.04700  1.000 65.34845  ? 303 ARG A O    1 
ATOM   1611 C CB   . ARG A 1 303 ? 111.44600 117.47700 87.47500  1.000 66.47496  ? 303 ARG A CB   1 
ATOM   1612 C CG   . ARG A 1 303 ? 112.42700 116.78200 86.55700  1.000 65.36124  ? 303 ARG A CG   1 
ATOM   1613 C CD   . ARG A 1 303 ? 112.19000 115.28200 86.52900  1.000 67.62781  ? 303 ARG A CD   1 
ATOM   1614 N NE   . ARG A 1 303 ? 113.03000 114.61800 85.54100  1.000 69.38530  ? 303 ARG A NE   1 
ATOM   1615 C CZ   . ARG A 1 303 ? 113.00100 113.31700 85.28700  1.000 67.57502  ? 303 ARG A CZ   1 
ATOM   1616 N NH1  . ARG A 1 303 ? 112.18200 112.50400 85.93400  1.000 65.83165  ? 303 ARG A NH1  1 
ATOM   1617 N NH2  . ARG A 1 303 ? 113.81500 112.81900 84.36000  1.000 68.08886  ? 303 ARG A NH2  1 
ATOM   1618 N N    . SER A 1 304 ? 108.72200 118.66700 88.63900  1.000 63.43879  ? 304 SER A N    1 
ATOM   1619 C CA   . SER A 1 304 ? 107.83900 118.94400 89.76500  1.000 64.23741  ? 304 SER A CA   1 
ATOM   1620 C C    . SER A 1 304 ? 106.41900 118.48200 89.47300  1.000 64.45338  ? 304 SER A C    1 
ATOM   1621 O O    . SER A 1 304 ? 105.71700 118.00500 90.37200  1.000 62.11189  ? 304 SER A O    1 
ATOM   1622 C CB   . SER A 1 304 ? 107.86300 120.43600 90.09400  1.000 62.81467  ? 304 SER A CB   1 
ATOM   1623 O OG   . SER A 1 304 ? 109.14200 120.83900 90.55200  1.000 64.47434  ? 304 SER A OG   1 
ATOM   1624 N N    . ALA A 1 305 ? 105.97900 118.61500 88.22100  1.000 60.30531  ? 305 ALA A N    1 
ATOM   1625 C CA   . ALA A 1 305 ? 104.62300 118.22200 87.86500  1.000 56.16005  ? 305 ALA A CA   1 
ATOM   1626 C C    . ALA A 1 305 ? 104.47100 116.72200 87.64100  1.000 55.58855  ? 305 ALA A C    1 
ATOM   1627 O O    . ALA A 1 305 ? 103.34200 116.25300 87.47000  1.000 56.84294  ? 305 ALA A O    1 
ATOM   1628 C CB   . ALA A 1 305 ? 104.17300 118.97300 86.61000  1.000 55.18831  ? 305 ALA A CB   1 
ATOM   1629 N N    . VAL A 1 306 ? 105.56600 115.96300 87.63800  1.000 61.59581  ? 306 VAL A N    1 
ATOM   1630 C CA   . VAL A 1 306 ? 105.51900 114.52000 87.43400  1.000 62.32457  ? 306 VAL A CA   1 
ATOM   1631 C C    . VAL A 1 306 ? 105.94300 113.74200 88.67300  1.000 60.18184  ? 306 VAL A C    1 
ATOM   1632 O O    . VAL A 1 306 ? 105.83400 112.50600 88.68400  1.000 61.16190  ? 306 VAL A O    1 
ATOM   1633 C CB   . VAL A 1 306 ? 106.37500 114.11800 86.21400  1.000 61.17195  ? 306 VAL A CB   1 
ATOM   1634 C CG1  . VAL A 1 306 ? 106.85400 112.67600 86.30000  1.000 60.65816  ? 306 VAL A CG1  1 
ATOM   1635 C CG2  . VAL A 1 306 ? 105.59900 114.34600 84.92400  1.000 55.73029  ? 306 VAL A CG2  1 
ATOM   1636 N N    . GLU A 1 307 ? 106.35500 114.42500 89.74300  1.000 67.08295  ? 307 GLU A N    1 
ATOM   1637 C CA   . GLU A 1 307 ? 106.90800 113.75600 90.91500  1.000 66.85903  ? 307 GLU A CA   1 
ATOM   1638 C C    . GLU A 1 307 ? 106.23500 114.15300 92.22600  1.000 68.69479  ? 307 GLU A C    1 
ATOM   1639 O O    . GLU A 1 307 ? 106.75100 113.80700 93.29500  1.000 70.85540  ? 307 GLU A O    1 
ATOM   1640 C CB   . GLU A 1 307 ? 108.41500 114.02100 91.01300  1.000 64.39895  ? 307 GLU A CB   1 
ATOM   1641 N N    . SER A 1 308 ? 105.10900 114.86600 92.18500  1.000 60.72363  ? 308 SER A N    1 
ATOM   1642 C CA   . SER A 1 308 ? 104.44600 115.32500 93.40000  1.000 60.36878  ? 308 SER A CA   1 
ATOM   1643 C C    . SER A 1 308 ? 103.11600 114.62200 93.66000  1.000 58.76924  ? 308 SER A C    1 
ATOM   1644 O O    . SER A 1 308 ? 102.29100 115.13300 94.42300  1.000 57.88567  ? 308 SER A O    1 
ATOM   1645 C CB   . SER A 1 308 ? 104.24000 116.83900 93.34400  1.000 61.68303  ? 308 SER A CB   1 
ATOM   1646 O OG   . SER A 1 308 ? 103.07900 117.17100 92.60200  1.000 61.51281  ? 308 SER A OG   1 
ATOM   1647 N N    . THR A 1 309 ? 102.88600 113.46000 93.04200  1.000 58.27383  ? 309 THR A N    1 
ATOM   1648 C CA   . THR A 1 309 ? 101.63700 112.73900 93.27600  1.000 60.48369  ? 309 THR A CA   1 
ATOM   1649 C C    . THR A 1 309 ? 101.47100 112.37800 94.74900  1.000 56.35818  ? 309 THR A C    1 
ATOM   1650 O O    . THR A 1 309 ? 100.35900 112.43400 95.29300  1.000 56.86066  ? 309 THR A O    1 
ATOM   1651 C CB   . THR A 1 309 ? 101.58700 111.48000 92.41100  1.000 59.81231  ? 309 THR A CB   1 
ATOM   1652 O OG1  . THR A 1 309 ? 101.67600 111.84400 91.02800  1.000 56.83044  ? 309 THR A OG1  1 
ATOM   1653 C CG2  . THR A 1 309 ? 100.29000 110.72500 92.64800  1.000 54.94320  ? 309 THR A CG2  1 
ATOM   1654 N N    . SER A 1 310 ? 102.57600 112.06500 95.43000  1.000 51.77341  ? 310 SER A N    1 
ATOM   1655 C CA   . SER A 1 310 ? 102.47800 111.69000 96.83500  1.000 52.71565  ? 310 SER A CA   1 
ATOM   1656 C C    . SER A 1 310 ? 102.18000 112.90500 97.69900  1.000 54.87070  ? 310 SER A C    1 
ATOM   1657 O O    . SER A 1 310 ? 101.44300 112.80500 98.68700  1.000 55.21507  ? 310 SER A O    1 
ATOM   1658 C CB   . SER A 1 310 ? 103.76800 111.00800 97.28700  1.000 54.04664  ? 310 SER A CB   1 
ATOM   1659 O OG   . SER A 1 310 ? 104.90500 111.71900 96.83200  1.000 55.32284  ? 310 SER A OG   1 
ATOM   1660 N N    . GLN A 1 311 ? 102.76100 114.05700 97.36200  1.000 52.94841  ? 311 GLN A N    1 
ATOM   1661 C CA   . GLN A 1 311 ? 102.43200 115.27000 98.09800  1.000 53.03124  ? 311 GLN A CA   1 
ATOM   1662 C C    . GLN A 1 311 ? 100.95000 115.59000 97.95500  1.000 48.28072  ? 311 GLN A C    1 
ATOM   1663 O O    . GLN A 1 311 ? 100.28400 115.94900 98.93500  1.000 49.89332  ? 311 GLN A O    1 
ATOM   1664 C CB   . GLN A 1 311 ? 103.28900 116.43500 97.60500  1.000 53.98290  ? 311 GLN A CB   1 
ATOM   1665 C CG   . GLN A 1 311 ? 103.80200 117.33900 98.71300  1.000 53.92251  ? 311 GLN A CG   1 
ATOM   1666 C CD   . GLN A 1 311 ? 104.24700 118.69200 98.19900  1.000 56.42143  ? 311 GLN A CD   1 
ATOM   1667 O OE1  . GLN A 1 311 ? 104.89200 118.79100 97.15600  1.000 57.56331  ? 311 GLN A OE1  1 
ATOM   1668 N NE2  . GLN A 1 311 ? 103.90300 119.74500 98.93100  1.000 54.28181  ? 311 GLN A NE2  1 
ATOM   1669 N N    . GLU A 1 312 ? 100.40500 115.40600 96.74900  1.000 42.00395  ? 312 GLU A N    1 
ATOM   1670 C CA   . GLU A 1 312 ? 99.00400  115.69000 96.47500  1.000 43.95994  ? 312 GLU A CA   1 
ATOM   1671 C C    . GLU A 1 312 ? 98.06800  114.62100 97.01200  1.000 46.13073  ? 312 GLU A C    1 
ATOM   1672 O O    . GLU A 1 312 ? 96.85200  114.83700 97.02300  1.000 49.55281  ? 312 GLU A O    1 
ATOM   1673 C CB   . GLU A 1 312 ? 98.77900  115.85100 94.97100  1.000 46.08493  ? 312 GLU A CB   1 
ATOM   1674 C CG   . GLU A 1 312 ? 99.83300  116.68500 94.27100  1.000 51.47585  ? 312 GLU A CG   1 
ATOM   1675 C CD   . GLU A 1 312 ? 99.70200  116.63800 92.76500  1.000 51.11770  ? 312 GLU A CD   1 
ATOM   1676 O OE1  . GLU A 1 312 ? 98.55600  116.60500 92.27200  1.000 52.17238  ? 312 GLU A OE1  1 
ATOM   1677 O OE2  . GLU A 1 312 ? 100.74200 116.63500 92.07500  1.000 51.96630  ? 312 GLU A OE2  1 
ATOM   1678 N N    . GLU A 1 313 ? 98.59400  113.48000 97.45300  1.000 47.43067  ? 313 GLU A N    1 
ATOM   1679 C CA   . GLU A 1 313 ? 97.75400  112.48300 98.10300  1.000 41.35705  ? 313 GLU A CA   1 
ATOM   1680 C C    . GLU A 1 313 ? 97.81100  112.58800 99.61800  1.000 41.64652  ? 313 GLU A C    1 
ATOM   1681 O O    . GLU A 1 313 ? 96.79500  112.37400 100.28800 1.000 44.18230  ? 313 GLU A O    1 
ATOM   1682 C CB   . GLU A 1 313 ? 98.15600  111.06900 97.67100  1.000 44.39835  ? 313 GLU A CB   1 
ATOM   1683 C CG   . GLU A 1 313 ? 98.18500  110.87200 96.16700  1.000 49.15411  ? 313 GLU A CG   1 
ATOM   1684 C CD   . GLU A 1 313 ? 96.97100  110.12300 95.65600  1.000 49.53741  ? 313 GLU A CD   1 
ATOM   1685 O OE1  . GLU A 1 313 ? 96.00000  109.96600 96.42600  1.000 50.89748  ? 313 GLU A OE1  1 
ATOM   1686 O OE2  . GLU A 1 313 ? 96.98500  109.69600 94.48200  1.000 49.72237  ? 313 GLU A OE2  1 
ATOM   1687 N N    . SER A 1 314 ? 98.95200  113.00300 100.16900 1.000 31.01909  ? 314 SER A N    1 
ATOM   1688 C CA   . SER A 1 314 ? 99.01500  113.27200 101.60000 1.000 31.16520  ? 314 SER A CA   1 
ATOM   1689 C C    . SER A 1 314 ? 98.23700  114.53600 101.95100 1.000 32.93042  ? 314 SER A C    1 
ATOM   1690 O O    . SER A 1 314 ? 97.51600  114.57000 102.95800 1.000 28.24439  ? 314 SER A O    1 
ATOM   1691 C CB   . SER A 1 314 ? 100.47000 113.38600 102.04900 1.000 29.44059  ? 314 SER A CB   1 
ATOM   1692 O OG   . SER A 1 314 ? 100.94500 114.71300 101.91400 1.000 40.10509  ? 314 SER A OG   1 
ATOM   1693 N N    . LEU A 1 315 ? 98.35300  115.58400 101.12700 1.000 28.53677  ? 315 LEU A N    1 
ATOM   1694 C CA   . LEU A 1 315 ? 97.57200  116.78800 101.37800 1.000 19.36904  ? 315 LEU A CA   1 
ATOM   1695 C C    . LEU A 1 315 ? 96.07900  116.51500 101.26300 1.000 28.88954  ? 315 LEU A C    1 
ATOM   1696 O O    . LEU A 1 315 ? 95.27600  117.18400 101.92100 1.000 39.44690  ? 315 LEU A O    1 
ATOM   1697 C CB   . LEU A 1 315 ? 97.98400  117.89600 100.40900 1.000 27.09793  ? 315 LEU A CB   1 
ATOM   1698 C CG   . LEU A 1 315 ? 99.27200  118.65000 100.73900 1.000 33.29399  ? 315 LEU A CG   1 
ATOM   1699 C CD1  . LEU A 1 315 ? 99.66700  119.55900 99.58900  1.000 27.12111  ? 315 LEU A CD1  1 
ATOM   1700 C CD2  . LEU A 1 315 ? 99.12800  119.43700 102.02900 1.000 32.83985  ? 315 LEU A CD2  1 
ATOM   1701 N N    . MET A 1 316 ? 95.68700  115.54100 100.43800 1.000 25.61355  ? 316 MET A N    1 
ATOM   1702 C CA   . MET A 1 316 ? 94.28500  115.15100 100.36000 1.000 28.32465  ? 316 MET A CA   1 
ATOM   1703 C C    . MET A 1 316 ? 93.87400  114.23200 101.50100 1.000 32.84221  ? 316 MET A C    1 
ATOM   1704 O O    . MET A 1 316 ? 92.68300  114.16000 101.82200 1.000 35.99406  ? 316 MET A O    1 
ATOM   1705 C CB   . MET A 1 316 ? 93.99700  114.47000 99.02100  1.000 30.39206  ? 316 MET A CB   1 
ATOM   1706 C CG   . MET A 1 316 ? 92.52900  114.46600 98.63300  1.000 32.28354  ? 316 MET A CG   1 
ATOM   1707 S SD   . MET A 1 316 ? 91.78500  112.82700 98.67000  1.000 48.77700  ? 316 MET A SD   1 
ATOM   1708 C CE   . MET A 1 316 ? 92.60100  112.05200 97.27900  1.000 37.62292  ? 316 MET A CE   1 
ATOM   1709 N N    . SER A 1 317 ? 94.82800  113.53400 102.11700 1.000 37.96442  ? 317 SER A N    1 
ATOM   1710 C CA   . SER A 1 317 ? 94.52800  112.72700 103.29200 1.000 19.47637  ? 317 SER A CA   1 
ATOM   1711 C C    . SER A 1 317 ? 94.52100  113.55100 104.57000 1.000 26.64702  ? 317 SER A C    1 
ATOM   1712 O O    . SER A 1 317 ? 94.06100  113.05800 105.60500 1.000 25.88353  ? 317 SER A O    1 
ATOM   1713 C CB   . SER A 1 317 ? 95.53400  111.58300 103.42300 1.000 25.55348  ? 317 SER A CB   1 
ATOM   1714 O OG   . SER A 1 317 ? 96.79500  112.06100 103.85500 1.000 29.51389  ? 317 SER A OG   1 
ATOM   1715 N N    . PHE A 1 318 ? 95.01200  114.79000 104.52000 1.000 33.05129  ? 318 PHE A N    1 
ATOM   1716 C CA   . PHE A 1 318 ? 94.94300  115.69600 105.66000 1.000 10.06843  ? 318 PHE A CA   1 
ATOM   1717 C C    . PHE A 1 318 ? 93.79900  116.69500 105.56100 1.000 13.98427  ? 318 PHE A C    1 
ATOM   1718 O O    . PHE A 1 318 ? 93.34600  117.19500 106.59400 1.000 22.43732  ? 318 PHE A O    1 
ATOM   1719 C CB   . PHE A 1 318 ? 96.25400  116.47900 105.81300 1.000 15.17227  ? 318 PHE A CB   1 
ATOM   1720 C CG   . PHE A 1 318 ? 97.41600  115.64700 106.26200 1.000 17.04992  ? 318 PHE A CG   1 
ATOM   1721 C CD1  . PHE A 1 318 ? 97.21700  114.45800 106.93600 1.000 15.78930  ? 318 PHE A CD1  1 
ATOM   1722 C CD2  . PHE A 1 318 ? 98.71200  116.05800 106.00800 1.000 14.24905  ? 318 PHE A CD2  1 
ATOM   1723 C CE1  . PHE A 1 318 ? 98.28800  113.69500 107.35000 1.000 17.39416  ? 318 PHE A CE1  1 
ATOM   1724 C CE2  . PHE A 1 318 ? 99.78700  115.29700 106.41700 1.000 6.91565   ? 318 PHE A CE2  1 
ATOM   1725 C CZ   . PHE A 1 318 ? 99.57500  114.11600 107.09000 1.000 13.10672  ? 318 PHE A CZ   1 
ATOM   1726 N N    . ALA A 1 319 ? 93.31700  116.98500 104.35200 1.000 24.83827  ? 319 ALA A N    1 
ATOM   1727 C CA   . ALA A 1 319 ? 92.26200  117.97000 104.15400 1.000 17.88375  ? 319 ALA A CA   1 
ATOM   1728 C C    . ALA A 1 319 ? 90.86800  117.43000 104.43900 1.000 18.74931  ? 319 ALA A C    1 
ATOM   1729 O O    . ALA A 1 319 ? 89.92100  118.22000 104.50000 1.000 27.82859  ? 319 ALA A O    1 
ATOM   1730 C CB   . ALA A 1 319 ? 92.31600  118.51000 102.72400 1.000 14.67375  ? 319 ALA A CB   1 
ATOM   1731 N N    . ILE A 1 320 ? 90.71400  116.11600 104.61900 1.000 15.92611  ? 320 ILE A N    1 
ATOM   1732 C CA   . ILE A 1 320 ? 89.39500  115.54400 104.88500 1.000 18.33096  ? 320 ILE A CA   1 
ATOM   1733 C C    . ILE A 1 320 ? 89.01500  115.60200 106.35400 1.000 22.18774  ? 320 ILE A C    1 
ATOM   1734 O O    . ILE A 1 320 ? 87.88100  115.25300 106.70400 1.000 29.76293  ? 320 ILE A O    1 
ATOM   1735 C CB   . ILE A 1 320 ? 89.31100  114.08500 104.39800 1.000 22.18635  ? 320 ILE A CB   1 
ATOM   1736 C CG1  . ILE A 1 320 ? 90.44500  113.25300 104.99800 1.000 23.97386  ? 320 ILE A CG1  1 
ATOM   1737 C CG2  . ILE A 1 320 ? 89.34000  114.02600 102.87900 1.000 20.80562  ? 320 ILE A CG2  1 
ATOM   1738 C CD1  . ILE A 1 320 ? 90.09700  111.79300 105.17400 1.000 26.65829  ? 320 ILE A CD1  1 
ATOM   1739 N N    . TRP A 1 321 ? 89.92700  116.03300 107.22200 1.000 20.06524  ? 321 TRP A N    1 
ATOM   1740 C CA   . TRP A 1 321 ? 89.67300  116.13300 108.65100 1.000 11.54555  ? 321 TRP A CA   1 
ATOM   1741 C C    . TRP A 1 321 ? 89.31400  117.54300 109.09700 1.000 19.76913  ? 321 TRP A C    1 
ATOM   1742 O O    . TRP A 1 321 ? 88.88000  117.72000 110.23800 1.000 27.55012  ? 321 TRP A O    1 
ATOM   1743 C CB   . TRP A 1 321 ? 90.91100  115.67700 109.43500 1.000 16.60902  ? 321 TRP A CB   1 
ATOM   1744 C CG   . TRP A 1 321 ? 91.07800  114.19800 109.56200 1.000 13.64769  ? 321 TRP A CG   1 
ATOM   1745 C CD1  . TRP A 1 321 ? 91.58600  113.35000 108.62600 1.000 12.95434  ? 321 TRP A CD1  1 
ATOM   1746 C CD2  . TRP A 1 321 ? 90.78500  113.39600 110.71200 1.000 14.61581  ? 321 TRP A CD2  1 
ATOM   1747 N NE1  . TRP A 1 321 ? 91.60500  112.06600 109.10900 1.000 12.20211  ? 321 TRP A NE1  1 
ATOM   1748 C CE2  . TRP A 1 321 ? 91.11900  112.06700 110.39000 1.000 13.64932  ? 321 TRP A CE2  1 
ATOM   1749 C CE3  . TRP A 1 321 ? 90.25900  113.67100 111.97800 1.000 17.41904  ? 321 TRP A CE3  1 
ATOM   1750 C CZ2  . TRP A 1 321 ? 90.94800  111.01600 111.28600 1.000 15.18015  ? 321 TRP A CZ2  1 
ATOM   1751 C CZ3  . TRP A 1 321 ? 90.09100  112.62600 112.86600 1.000 17.91281  ? 321 TRP A CZ3  1 
ATOM   1752 C CH2  . TRP A 1 321 ? 90.43300  111.31600 112.51500 1.000 14.43489  ? 321 TRP A CH2  1 
ATOM   1753 N N    . GLU A 1 322 ? 89.47700  118.54200 108.23100 1.000 18.41313  ? 322 GLU A N    1 
ATOM   1754 C CA   . GLU A 1 322 ? 89.32400  119.96300 108.52300 1.000 16.70500  ? 322 GLU A CA   1 
ATOM   1755 C C    . GLU A 1 322 ? 87.87400  120.41400 108.35700 1.000 24.03736  ? 322 GLU A C    1 
ATOM   1756 O O    . GLU A 1 322 ? 87.18300  119.96800 107.43800 1.000 31.59646  ? 322 GLU A O    1 
ATOM   1757 C CB   . GLU A 1 322 ? 90.22600  120.78800 107.61400 1.000 19.75175  ? 322 GLU A CB   1 
ATOM   1758 C CG   . GLU A 1 322 ? 91.70400  120.50300 107.82000 1.000 18.64995  ? 322 GLU A CG   1 
ATOM   1759 C CD   . GLU A 1 322 ? 92.58700  121.22300 106.82900 1.000 15.59849  ? 322 GLU A CD   1 
ATOM   1760 O OE1  . GLU A 1 322 ? 92.05600  121.75500 105.83500 1.000 29.73179  ? 322 GLU A OE1  1 
ATOM   1761 O OE2  . GLU A 1 322 ? 93.81400  121.26300 107.04700 1.000 8.21133   ? 322 GLU A OE2  1 
ATOM   1762 N N    . PRO A 1 323 ? 87.41300  121.28800 109.24800 1.000 30.96432  ? 323 PRO A N    1 
ATOM   1763 C CA   . PRO A 1 323 ? 86.03800  121.79700 109.17000 1.000 31.94001  ? 323 PRO A CA   1 
ATOM   1764 C C    . PRO A 1 323 ? 85.87300  122.78800 108.03200 1.000 35.67891  ? 323 PRO A C    1 
ATOM   1765 O O    . PRO A 1 323 ? 86.86000  123.35000 107.53600 1.000 32.79837  ? 323 PRO A O    1 
ATOM   1766 C CB   . PRO A 1 323 ? 85.83800  122.47500 110.53300 1.000 28.42040  ? 323 PRO A CB   1 
ATOM   1767 C CG   . PRO A 1 323 ? 87.21500  122.84600 110.96500 1.000 30.01370  ? 323 PRO A CG   1 
ATOM   1768 C CD   . PRO A 1 323 ? 88.10800  121.75300 110.46000 1.000 25.63704  ? 323 PRO A CD   1 
ATOM   1769 N N    . PRO A 1 324 ? 84.63800  123.02700 107.59000 1.000 41.33970  ? 324 PRO A N    1 
ATOM   1770 C CA   . PRO A 1 324 ? 84.40700  124.00800 106.52200 1.000 38.03408  ? 324 PRO A CA   1 
ATOM   1771 C C    . PRO A 1 324 ? 84.90600  125.39200 106.91000 1.000 39.63499  ? 324 PRO A C    1 
ATOM   1772 O O    . PRO A 1 324 ? 84.89700  125.77600 108.08100 1.000 43.08795  ? 324 PRO A O    1 
ATOM   1773 C CB   . PRO A 1 324 ? 82.88300  123.99600 106.35800 1.000 37.56775  ? 324 PRO A CB   1 
ATOM   1774 C CG   . PRO A 1 324 ? 82.47200  122.64800 106.83300 1.000 40.35297  ? 324 PRO A CG   1 
ATOM   1775 C CD   . PRO A 1 324 ? 83.40000  122.32600 107.96900 1.000 37.08806  ? 324 PRO A CD   1 
ATOM   1776 N N    . HIS A 1 325 ? 85.34700  126.14800 105.90600 1.000 33.14949  ? 325 HIS A N    1 
ATOM   1777 C CA   . HIS A 1 325 ? 85.87400  127.48100 106.16200 1.000 32.97447  ? 325 HIS A CA   1 
ATOM   1778 C C    . HIS A 1 325 ? 86.09900  128.20700 104.84500 1.000 35.56555  ? 325 HIS A C    1 
ATOM   1779 O O    . HIS A 1 325 ? 86.31700  127.58100 103.80400 1.000 41.31789  ? 325 HIS A O    1 
ATOM   1780 C CB   . HIS A 1 325 ? 87.18600  127.41500 106.95000 1.000 30.38089  ? 325 HIS A CB   1 
ATOM   1781 C CG   . HIS A 1 325 ? 88.33400  126.87600 106.15600 1.000 29.93588  ? 325 HIS A CG   1 
ATOM   1782 N ND1  . HIS A 1 325 ? 88.59900  125.52800 106.05100 1.000 31.24088  ? 325 HIS A ND1  1 
ATOM   1783 C CD2  . HIS A 1 325 ? 89.28000  127.50300 105.41800 1.000 29.34299  ? 325 HIS A CD2  1 
ATOM   1784 C CE1  . HIS A 1 325 ? 89.66100  125.34800 105.28700 1.000 29.79019  ? 325 HIS A CE1  1 
ATOM   1785 N NE2  . HIS A 1 325 ? 90.09300  126.53100 104.89000 1.000 28.24285  ? 325 HIS A NE2  1 
ATOM   1786 N N    . GLY A 1 326 ? 86.04000  129.53600 104.91000 1.000 42.77502  ? 326 GLY A N    1 
ATOM   1787 C CA   . GLY A 1 326 ? 86.33700  130.39600 103.78800 1.000 42.00245  ? 326 GLY A CA   1 
ATOM   1788 C C    . GLY A 1 326 ? 85.50200  130.14500 102.54900 1.000 42.87057  ? 326 GLY A C    1 
ATOM   1789 O O    . GLY A 1 326 ? 84.26800  130.12300 102.59000 1.000 45.46195  ? 326 GLY A O    1 
ATOM   1790 N N    . PRO A 1 327 ? 86.17500  129.95800 101.41000 1.000 47.82864  ? 327 PRO A N    1 
ATOM   1791 C CA   . PRO A 1 327 ? 85.46100  129.70600 100.15100 1.000 43.66334  ? 327 PRO A CA   1 
ATOM   1792 C C    . PRO A 1 327 ? 84.97900  128.27100 100.01100 1.000 41.92147  ? 327 PRO A C    1 
ATOM   1793 O O    . PRO A 1 327 ? 83.99400  128.00800 99.31500  1.000 43.65973  ? 327 PRO A O    1 
ATOM   1794 C CB   . PRO A 1 327 ? 86.50900  130.05000 99.08700  1.000 40.27660  ? 327 PRO A CB   1 
ATOM   1795 C CG   . PRO A 1 327 ? 87.80400  129.76200 99.74900  1.000 38.99756  ? 327 PRO A CG   1 
ATOM   1796 C CD   . PRO A 1 327 ? 87.62200  130.13400 101.19600 1.000 43.78287  ? 327 PRO A CD   1 
ATOM   1797 N N    . TYR A 1 328 ? 85.66500  127.33500 100.66300 1.000 41.23419  ? 328 TYR A N    1 
ATOM   1798 C CA   . TYR A 1 328 ? 85.32900  125.91500 100.55400 1.000 42.37668  ? 328 TYR A CA   1 
ATOM   1799 C C    . TYR A 1 328 ? 84.38500  125.53200 101.69200 1.000 45.40261  ? 328 TYR A C    1 
ATOM   1800 O O    . TYR A 1 328 ? 84.75300  124.87200 102.66500 1.000 48.92261  ? 328 TYR A O    1 
ATOM   1801 C CB   . TYR A 1 328 ? 86.59000  125.06100 100.57400 1.000 38.28388  ? 328 TYR A CB   1 
ATOM   1802 C CG   . TYR A 1 328 ? 87.83500  125.75000 100.07100 1.000 35.70645  ? 328 TYR A CG   1 
ATOM   1803 C CD1  . TYR A 1 328 ? 88.08800  125.86800 98.71300  1.000 42.23656  ? 328 TYR A CD1  1 
ATOM   1804 C CD2  . TYR A 1 328 ? 88.76400  126.27500 100.95700 1.000 37.94511  ? 328 TYR A CD2  1 
ATOM   1805 C CE1  . TYR A 1 328 ? 89.23000  126.49300 98.25100  1.000 42.65537  ? 328 TYR A CE1  1 
ATOM   1806 C CE2  . TYR A 1 328 ? 89.90600  126.90200 100.50600 1.000 42.23231  ? 328 TYR A CE2  1 
ATOM   1807 C CZ   . TYR A 1 328 ? 90.13600  127.00800 99.15300  1.000 42.06878  ? 328 TYR A CZ   1 
ATOM   1808 O OH   . TYR A 1 328 ? 91.27400  127.63300 98.70200  1.000 41.70717  ? 328 TYR A OH   1 
ATOM   1809 N N    . LYS A 1 329 ? 83.13600  125.96200 101.54900 1.000 49.82420  ? 329 LYS A N    1 
ATOM   1810 C CA   . LYS A 1 329 ? 82.10800  125.74200 102.56200 1.000 52.98198  ? 329 LYS A CA   1 
ATOM   1811 C C    . LYS A 1 329 ? 81.11700  124.71100 102.03000 1.000 55.43044  ? 329 LYS A C    1 
ATOM   1812 O O    . LYS A 1 329 ? 80.26500  125.02300 101.19400 1.000 55.61276  ? 329 LYS A O    1 
ATOM   1813 C CB   . LYS A 1 329 ? 81.41600  127.05400 102.92200 1.000 54.64631  ? 329 LYS A CB   1 
ATOM   1814 C CG   . LYS A 1 329 ? 80.79400  127.77600 101.73900 1.000 55.40469  ? 329 LYS A CG   1 
ATOM   1815 C CD   . LYS A 1 329 ? 81.08800  129.26600 101.78900 1.000 54.56030  ? 329 LYS A CD   1 
ATOM   1816 C CE   . LYS A 1 329 ? 80.65200  129.96000 100.51100 1.000 53.90736  ? 329 LYS A CE   1 
ATOM   1817 N NZ   . LYS A 1 329 ? 81.39700  131.22900 100.28900 1.000 52.46297  ? 329 LYS A NZ   1 
ATOM   1818 N N    . SER A 1 330 ? 81.24300  123.47900 102.52100 1.000 61.35929  ? 330 SER A N    1 
ATOM   1819 C CA   . SER A 1 330 ? 80.32700  122.39500 102.19100 1.000 58.75621  ? 330 SER A CA   1 
ATOM   1820 C C    . SER A 1 330 ? 80.70700  121.16700 103.00800 1.000 59.20271  ? 330 SER A C    1 
ATOM   1821 O O    . SER A 1 330 ? 81.87600  121.00100 103.37300 1.000 59.36837  ? 330 SER A O    1 
ATOM   1822 C CB   . SER A 1 330 ? 80.35200  122.09100 100.69200 1.000 60.22532  ? 330 SER A CB   1 
ATOM   1823 O OG   . SER A 1 330 ? 80.07300  120.72500 100.44400 1.000 63.43512  ? 330 SER A OG   1 
ATOM   1824 N N    . PHE A 1 331 ? 79.73700  120.30300 103.30600 1.000 70.20642  ? 331 PHE A N    1 
ATOM   1825 C CA   . PHE A 1 331 ? 80.01100  119.17300 104.18900 1.000 71.30840  ? 331 PHE A CA   1 
ATOM   1826 C C    . PHE A 1 331 ? 81.03500  118.22100 103.58000 1.000 72.80884  ? 331 PHE A C    1 
ATOM   1827 O O    . PHE A 1 331 ? 82.00700  117.83400 104.23900 1.000 73.04947  ? 331 PHE A O    1 
ATOM   1828 C CB   . PHE A 1 331 ? 78.71100  118.43800 104.51300 1.000 71.00049  ? 331 PHE A CB   1 
ATOM   1829 C CG   . PHE A 1 331 ? 77.82000  119.18100 105.46500 1.000 74.59776  ? 331 PHE A CG   1 
ATOM   1830 C CD1  . PHE A 1 331 ? 78.35400  120.07900 106.37400 1.000 74.09411  ? 331 PHE A CD1  1 
ATOM   1831 C CD2  . PHE A 1 331 ? 76.44900  118.98600 105.45000 1.000 73.01591  ? 331 PHE A CD2  1 
ATOM   1832 C CE1  . PHE A 1 331 ? 77.54000  120.76700 107.25200 1.000 72.93240  ? 331 PHE A CE1  1 
ATOM   1833 C CE2  . PHE A 1 331 ? 75.62900  119.67100 106.32600 1.000 73.92032  ? 331 PHE A CE2  1 
ATOM   1834 C CZ   . PHE A 1 331 ? 76.17500  120.56200 107.22800 1.000 73.90764  ? 331 PHE A CZ   1 
ATOM   1835 N N    . ASN A 1 332 ? 80.83700  117.83200 102.32300 1.000 62.48521  ? 332 ASN A N    1 
ATOM   1836 C CA   . ASN A 1 332 ? 81.76500  116.95200 101.61100 1.000 59.88130  ? 332 ASN A CA   1 
ATOM   1837 C C    . ASN A 1 332 ? 82.35700  117.70000 100.42100 1.000 58.62732  ? 332 ASN A C    1 
ATOM   1838 O O    . ASN A 1 332 ? 81.69300  117.86600 99.39300  1.000 61.51446  ? 332 ASN A O    1 
ATOM   1839 C CB   . ASN A 1 332 ? 81.06200  115.67400 101.16500 1.000 59.97234  ? 332 ASN A CB   1 
ATOM   1840 C CG   . ASN A 1 332 ? 80.73300  114.75600 102.32400 1.000 62.89969  ? 332 ASN A CG   1 
ATOM   1841 O OD1  . ASN A 1 332 ? 79.79500  115.00500 103.08100 1.000 63.05816  ? 332 ASN A OD1  1 
ATOM   1842 N ND2  . ASN A 1 332 ? 81.50700  113.68700 102.47000 1.000 63.91979  ? 332 ASN A ND2  1 
ATOM   1843 N N    . TYR A 1 333 ? 83.60100  118.15400 100.55400 1.000 40.42252  ? 333 TYR A N    1 
ATOM   1844 C CA   . TYR A 1 333 ? 84.19300  118.88900 99.44500  1.000 43.35539  ? 333 TYR A CA   1 
ATOM   1845 C C    . TYR A 1 333 ? 84.80500  117.92400 98.42900  1.000 43.95345  ? 333 TYR A C    1 
ATOM   1846 O O    . TYR A 1 333 ? 85.48000  116.96500 98.81100  1.000 42.27237  ? 333 TYR A O    1 
ATOM   1847 C CB   . TYR A 1 333 ? 85.25500  119.86600 99.93900  1.000 40.31015  ? 333 TYR A CB   1 
ATOM   1848 C CG   . TYR A 1 333 ? 85.39800  121.06900 99.03900  1.000 39.97290  ? 333 TYR A CG   1 
ATOM   1849 C CD1  . TYR A 1 333 ? 84.37900  122.00500 98.93700  1.000 39.24356  ? 333 TYR A CD1  1 
ATOM   1850 C CD2  . TYR A 1 333 ? 86.53900  121.25700 98.27300  1.000 32.68946  ? 333 TYR A CD2  1 
ATOM   1851 C CE1  . TYR A 1 333 ? 84.49800  123.10100 98.10700  1.000 38.25732  ? 333 TYR A CE1  1 
ATOM   1852 C CE2  . TYR A 1 333 ? 86.66800  122.35000 97.44200  1.000 36.37728  ? 333 TYR A CE2  1 
ATOM   1853 C CZ   . TYR A 1 333 ? 85.64500  123.26900 97.36300  1.000 39.66546  ? 333 TYR A CZ   1 
ATOM   1854 O OH   . TYR A 1 333 ? 85.76800  124.36000 96.53600  1.000 36.24907  ? 333 TYR A OH   1 
ATOM   1855 N N    . PRO A 1 334 ? 84.58600  118.15700 97.13400  1.000 36.37074  ? 334 PRO A N    1 
ATOM   1856 C CA   . PRO A 1 334 ? 85.17400  117.28500 96.10800  1.000 31.64078  ? 334 PRO A CA   1 
ATOM   1857 C C    . PRO A 1 334 ? 86.68100  117.45200 95.97800  1.000 35.04618  ? 334 PRO A C    1 
ATOM   1858 O O    . PRO A 1 334 ? 87.16600  117.99600 94.98300  1.000 42.82291  ? 334 PRO A O    1 
ATOM   1859 C CB   . PRO A 1 334 ? 84.45100  117.72400 94.82900  1.000 36.52832  ? 334 PRO A CB   1 
ATOM   1860 C CG   . PRO A 1 334 ? 84.05400  119.13600 95.10300  1.000 34.90305  ? 334 PRO A CG   1 
ATOM   1861 C CD   . PRO A 1 334 ? 83.67100  119.15000 96.54800  1.000 32.73353  ? 334 PRO A CD   1 
ATOM   1862 N N    . TRP A 1 335 ? 87.43100  116.99100 96.98100  1.000 35.11731  ? 335 TRP A N    1 
ATOM   1863 C CA   . TRP A 1 335 ? 88.88400  117.11900 96.95700  1.000 32.86341  ? 335 TRP A CA   1 
ATOM   1864 C C    . TRP A 1 335 ? 89.54900  116.16200 95.97300  1.000 36.82987  ? 335 TRP A C    1 
ATOM   1865 O O    . TRP A 1 335 ? 90.68300  116.41500 95.55600  1.000 39.86940  ? 335 TRP A O    1 
ATOM   1866 C CB   . TRP A 1 335 ? 89.44600  116.87700 98.35900  1.000 34.02368  ? 335 TRP A CB   1 
ATOM   1867 C CG   . TRP A 1 335 ? 89.30200  118.04100 99.29600  1.000 35.66210  ? 335 TRP A CG   1 
ATOM   1868 C CD1  . TRP A 1 335 ? 88.76300  118.01900 100.54700 1.000 33.37170  ? 335 TRP A CD1  1 
ATOM   1869 C CD2  . TRP A 1 335 ? 89.71800  119.39300 99.06300  1.000 35.82084  ? 335 TRP A CD2  1 
ATOM   1870 N NE1  . TRP A 1 335 ? 88.80600  119.27200 101.10500 1.000 34.95915  ? 335 TRP A NE1  1 
ATOM   1871 C CE2  . TRP A 1 335 ? 89.38800  120.13400 100.21500 1.000 32.68496  ? 335 TRP A CE2  1 
ATOM   1872 C CE3  . TRP A 1 335 ? 90.33200  120.04900 97.99300  1.000 36.68100  ? 335 TRP A CE3  1 
ATOM   1873 C CZ2  . TRP A 1 335 ? 89.65100  121.49600 100.32700 1.000 33.65668  ? 335 TRP A CZ2  1 
ATOM   1874 C CZ3  . TRP A 1 335 ? 90.59200  121.40200 98.10600  1.000 37.47731  ? 335 TRP A CZ3  1 
ATOM   1875 C CH2  . TRP A 1 335 ? 90.25200  122.11100 99.26400  1.000 35.81048  ? 335 TRP A CH2  1 
ATOM   1876 N N    . LYS A 1 336 ? 88.87600  115.07300 95.59600  1.000 38.77578  ? 336 LYS A N    1 
ATOM   1877 C CA   . LYS A 1 336 ? 89.46000  114.10100 94.67400  1.000 36.02630  ? 336 LYS A CA   1 
ATOM   1878 C C    . LYS A 1 336 ? 89.51000  114.59900 93.23100  1.000 41.27698  ? 336 LYS A C    1 
ATOM   1879 O O    . LYS A 1 336 ? 90.38000  114.16800 92.45900  1.000 45.91181  ? 336 LYS A O    1 
ATOM   1880 C CB   . LYS A 1 336 ? 88.68200  112.78900 94.76000  1.000 40.46024  ? 336 LYS A CB   1 
ATOM   1881 C CG   . LYS A 1 336 ? 87.22400  112.91300 94.36500  1.000 42.56263  ? 336 LYS A CG   1 
ATOM   1882 C CD   . LYS A 1 336 ? 86.50600  111.58200 94.47400  1.000 39.96599  ? 336 LYS A CD   1 
ATOM   1883 C CE   . LYS A 1 336 ? 85.04600  111.71500 94.07900  1.000 45.21576  ? 336 LYS A CE   1 
ATOM   1884 N NZ   . LYS A 1 336 ? 84.30000  112.59200 95.02300  1.000 45.81319  ? 336 LYS A NZ   1 
ATOM   1885 N N    . ASN A 1 337 ? 88.60500  115.50000 92.84200  1.000 33.62560  ? 337 ASN A N    1 
ATOM   1886 C CA   . ASN A 1 337 ? 88.64200  116.01400 91.47800  1.000 35.40029  ? 337 ASN A CA   1 
ATOM   1887 C C    . ASN A 1 337 ? 89.88800  116.84600 91.20500  1.000 39.70241  ? 337 ASN A C    1 
ATOM   1888 O O    . ASN A 1 337 ? 90.32800  116.92700 90.05000  1.000 46.65455  ? 337 ASN A O    1 
ATOM   1889 C CB   . ASN A 1 337 ? 87.38700  116.84100 91.20300  1.000 39.89102  ? 337 ASN A CB   1 
ATOM   1890 C CG   . ASN A 1 337 ? 86.18900  115.98100 90.85200  1.000 45.40274  ? 337 ASN A CG   1 
ATOM   1891 O OD1  . ASN A 1 337 ? 85.99900  115.60600 89.69600  1.000 47.93974  ? 337 ASN A OD1  1 
ATOM   1892 N ND2  . ASN A 1 337 ? 85.37600  115.66200 91.84900  1.000 42.30735  ? 337 ASN A ND2  1 
ATOM   1893 N N    . TYR A 1 338 ? 90.53300  117.36800 92.25000  1.000 33.52143  ? 338 TYR A N    1 
ATOM   1894 C CA   . TYR A 1 338 ? 91.79700  118.06600 92.05000  1.000 33.46032  ? 338 TYR A CA   1 
ATOM   1895 C C    . TYR A 1 338 ? 92.90000  117.07700 91.70000  1.000 35.95419  ? 338 TYR A C    1 
ATOM   1896 O O    . TYR A 1 338 ? 93.74200  117.34900 90.83400  1.000 43.27727  ? 338 TYR A O    1 
ATOM   1897 C CB   . TYR A 1 338 ? 92.16300  118.84900 93.31100  1.000 30.95349  ? 338 TYR A CB   1 
ATOM   1898 C CG   . TYR A 1 338 ? 91.33000  120.08900 93.55000  1.000 34.18420  ? 338 TYR A CG   1 
ATOM   1899 C CD1  . TYR A 1 338 ? 90.06100  119.99700 94.10500  1.000 32.54334  ? 338 TYR A CD1  1 
ATOM   1900 C CD2  . TYR A 1 338 ? 91.81300  121.35000 93.23200  1.000 27.99741  ? 338 TYR A CD2  1 
ATOM   1901 C CE1  . TYR A 1 338 ? 89.29600  121.12400 94.33100  1.000 26.51298  ? 338 TYR A CE1  1 
ATOM   1902 C CE2  . TYR A 1 338 ? 91.05500  122.48200 93.45400  1.000 29.29711  ? 338 TYR A CE2  1 
ATOM   1903 C CZ   . TYR A 1 338 ? 89.79800  122.36300 94.00300  1.000 35.46724  ? 338 TYR A CZ   1 
ATOM   1904 O OH   . TYR A 1 338 ? 89.04000  123.48800 94.22700  1.000 37.39040  ? 338 TYR A OH   1 
ATOM   1905 N N    . VAL A 1 339 ? 92.87600  115.90100 92.32700  1.000 30.02988  ? 339 VAL A N    1 
ATOM   1906 C CA   . VAL A 1 339 ? 93.84400  114.86000 92.00500  1.000 33.57384  ? 339 VAL A CA   1 
ATOM   1907 C C    . VAL A 1 339 ? 93.59800  114.32500 90.60000  1.000 31.32156  ? 339 VAL A C    1 
ATOM   1908 O O    . VAL A 1 339 ? 94.54300  114.02800 89.85800  1.000 36.83678  ? 339 VAL A O    1 
ATOM   1909 C CB   . VAL A 1 339 ? 93.78700  113.74000 93.05900  1.000 36.85304  ? 339 VAL A CB   1 
ATOM   1910 C CG1  . VAL A 1 339 ? 94.85500  112.69500 92.78400  1.000 34.91728  ? 339 VAL A CG1  1 
ATOM   1911 C CG2  . VAL A 1 339 ? 93.94300  114.31800 94.45600  1.000 30.39703  ? 339 VAL A CG2  1 
ATOM   1912 N N    . LYS A 1 340 ? 92.32800  114.18800 90.21300  1.000 28.38624  ? 340 LYS A N    1 
ATOM   1913 C CA   . LYS A 1 340 ? 92.02400  113.74200 88.85600  1.000 30.15651  ? 340 LYS A CA   1 
ATOM   1914 C C    . LYS A 1 340 ? 92.54000  114.73200 87.81300  1.000 34.02289  ? 340 LYS A C    1 
ATOM   1915 O O    . LYS A 1 340 ? 93.13400  114.33300 86.79900  1.000 42.41483  ? 340 LYS A O    1 
ATOM   1916 C CB   . LYS A 1 340 ? 90.51500  113.53900 88.71400  1.000 29.67638  ? 340 LYS A CB   1 
ATOM   1917 C CG   . LYS A 1 340 ? 90.10400  112.52600 87.66500  1.000 37.60573  ? 340 LYS A CG   1 
ATOM   1918 C CD   . LYS A 1 340 ? 88.64200  112.69700 87.28700  1.000 41.21037  ? 340 LYS A CD   1 
ATOM   1919 C CE   . LYS A 1 340 ? 88.43600  112.55200 85.79000  1.000 40.73099  ? 340 LYS A CE   1 
ATOM   1920 N NZ   . LYS A 1 340 ? 87.10500  111.96800 85.46900  1.000 39.72161  ? 340 LYS A NZ   1 
ATOM   1921 N N    . LEU A 1 341 ? 92.35700  116.03200 88.06100  1.000 27.35414  ? 341 LEU A N    1 
ATOM   1922 C CA   . LEU A 1 341 ? 92.89500  117.03500 87.14700  1.000 27.18625  ? 341 LEU A CA   1 
ATOM   1923 C C    . LEU A 1 341 ? 94.42200  116.99000 87.10300  1.000 28.15757  ? 341 LEU A C    1 
ATOM   1924 O O    . LEU A 1 341 ? 95.03000  117.11400 86.02800  1.000 37.84484  ? 341 LEU A O    1 
ATOM   1925 C CB   . LEU A 1 341 ? 92.39700  118.42200 87.55400  1.000 32.72189  ? 341 LEU A CB   1 
ATOM   1926 C CG   . LEU A 1 341 ? 92.71100  119.60200 86.63600  1.000 32.14533  ? 341 LEU A CG   1 
ATOM   1927 C CD1  . LEU A 1 341 ? 92.09600  119.38400 85.26600  1.000 26.77296  ? 341 LEU A CD1  1 
ATOM   1928 C CD2  . LEU A 1 341 ? 92.20800  120.89700 87.24700  1.000 23.66844  ? 341 LEU A CD2  1 
ATOM   1929 N N    . SER A 1 342 ? 95.06200  116.80400 88.26200  1.000 22.17529  ? 342 SER A N    1 
ATOM   1930 C CA   . SER A 1 342 ? 96.52000  116.71000 88.29100  1.000 24.85905  ? 342 SER A CA   1 
ATOM   1931 C C    . SER A 1 342 ? 97.02300  115.50800 87.49700  1.000 32.91996  ? 342 SER A C    1 
ATOM   1932 O O    . SER A 1 342 ? 98.04800  115.59500 86.80900  1.000 35.00174  ? 342 SER A O    1 
ATOM   1933 C CB   . SER A 1 342 ? 97.00800  116.63900 89.73600  1.000 26.57156  ? 342 SER A CB   1 
ATOM   1934 O OG   . SER A 1 342 ? 96.99500  117.91900 90.33700  1.000 29.47613  ? 342 SER A OG   1 
ATOM   1935 N N    . GLY A 1 343 ? 96.31300  114.38100 87.56600  1.000 30.71839  ? 343 GLY A N    1 
ATOM   1936 C CA   . GLY A 1 343 ? 96.72000  113.22400 86.78300  1.000 25.32394  ? 343 GLY A CA   1 
ATOM   1937 C C    . GLY A 1 343 ? 96.55700  113.46400 85.29500  1.000 29.38036  ? 343 GLY A C    1 
ATOM   1938 O O    . GLY A 1 343 ? 97.41100  113.06900 84.48400  1.000 40.89047  ? 343 GLY A O    1 
ATOM   1939 N N    . ALA A 1 344 ? 95.47400  114.14600 84.91600  1.000 26.74914  ? 344 ALA A N    1 
ATOM   1940 C CA   . ALA A 1 344 ? 95.27300  114.45400 83.50700  1.000 24.07472  ? 344 ALA A CA   1 
ATOM   1941 C C    . ALA A 1 344 ? 96.39000  115.35100 82.98400  1.000 28.87063  ? 344 ALA A C    1 
ATOM   1942 O O    . ALA A 1 344 ? 96.81600  115.21400 81.83200  1.000 28.23544  ? 344 ALA A O    1 
ATOM   1943 C CB   . ALA A 1 344 ? 93.90800  115.10900 83.29900  1.000 23.06118  ? 344 ALA A CB   1 
ATOM   1944 N N    . LEU A 1 345 ? 96.87800  116.27600 83.81700  1.000 26.14701  ? 345 LEU A N    1 
ATOM   1945 C CA   . LEU A 1 345 ? 97.99300  117.12400 83.39100  1.000 29.41966  ? 345 LEU A CA   1 
ATOM   1946 C C    . LEU A 1 345 ? 99.32800  116.37600 83.37500  1.000 30.44812  ? 345 LEU A C    1 
ATOM   1947 O O    . LEU A 1 345 ? 100.18700 116.64700 82.52200  1.000 36.31884  ? 345 LEU A O    1 
ATOM   1948 C CB   . LEU A 1 345 ? 98.09000  118.34800 84.30000  1.000 33.69464  ? 345 LEU A CB   1 
ATOM   1949 C CG   . LEU A 1 345 ? 99.08500  119.43400 83.88900  1.000 32.25365  ? 345 LEU A CG   1 
ATOM   1950 C CD1  . LEU A 1 345 ? 98.61600  120.15200 82.63600  1.000 30.57885  ? 345 LEU A CD1  1 
ATOM   1951 C CD2  . LEU A 1 345 ? 99.30200  120.41300 85.02500  1.000 29.06759  ? 345 LEU A CD2  1 
ATOM   1952 N N    . LYS A 1 346 ? 99.52100  115.42300 84.28900  1.000 30.29645  ? 346 LYS A N    1 
ATOM   1953 C CA   . LYS A 1 346 ? 100.77100 114.66700 84.29700  1.000 29.59911  ? 346 LYS A CA   1 
ATOM   1954 C C    . LYS A 1 346 ? 100.88600 113.76600 83.07200  1.000 30.71121  ? 346 LYS A C    1 
ATOM   1955 O O    . LYS A 1 346 ? 102.00000 113.49700 82.58800  1.000 29.07808  ? 346 LYS A O    1 
ATOM   1956 C CB   . LYS A 1 346 ? 100.87000 113.85800 85.59000  1.000 32.47926  ? 346 LYS A CB   1 
ATOM   1957 C CG   . LYS A 1 346 ? 101.71500 112.60500 85.50600  1.000 37.18229  ? 346 LYS A CG   1 
ATOM   1958 C CD   . LYS A 1 346 ? 101.48500 111.73000 86.72500  1.000 37.88782  ? 346 LYS A CD   1 
ATOM   1959 C CE   . LYS A 1 346 ? 102.45100 110.56200 86.76700  1.000 41.29530  ? 346 LYS A CE   1 
ATOM   1960 N NZ   . LYS A 1 346 ? 102.98800 110.33500 88.13700  1.000 40.45298  ? 346 LYS A NZ   1 
ATOM   1961 N N    . HIS A 1 347 ? 99.74800  113.32200 82.53600  1.000 35.62501  ? 347 HIS A N    1 
ATOM   1962 C CA   . HIS A 1 347 ? 99.79500  112.51700 81.31900  1.000 30.32028  ? 347 HIS A CA   1 
ATOM   1963 C C    . HIS A 1 347 ? 100.40800 113.30300 80.15800  1.000 33.12343  ? 347 HIS A C    1 
ATOM   1964 O O    . HIS A 1 347 ? 101.16700 112.74700 79.35700  1.000 37.04097  ? 347 HIS A O    1 
ATOM   1965 C CB   . HIS A 1 347 ? 98.38900  112.02200 80.97500  1.000 31.03932  ? 347 HIS A CB   1 
ATOM   1966 C CG   . HIS A 1 347 ? 98.36000  110.93200 79.94900  1.000 36.97745  ? 347 HIS A CG   1 
ATOM   1967 N ND1  . HIS A 1 347 ? 97.83300  111.10700 78.68800  1.000 41.02016  ? 347 HIS A ND1  1 
ATOM   1968 C CD2  . HIS A 1 347 ? 98.79000  109.64900 80.00100  1.000 36.57859  ? 347 HIS A CD2  1 
ATOM   1969 C CE1  . HIS A 1 347 ? 97.94100  109.98000 78.00700  1.000 36.83786  ? 347 HIS A CE1  1 
ATOM   1970 N NE2  . HIS A 1 347 ? 98.52000  109.08000 78.78100  1.000 34.66102  ? 347 HIS A NE2  1 
ATOM   1971 N N    . CYS A 1 348 ? 100.08200 114.59700 80.04400  1.000 31.38558  ? 348 CYS A N    1 
ATOM   1972 C CA   . CYS A 1 348 ? 100.75100 115.47800 79.08200  1.000 33.58932  ? 348 CYS A CA   1 
ATOM   1973 C C    . CYS A 1 348 ? 102.21100 115.73000 79.45700  1.000 34.87064  ? 348 CYS A C    1 
ATOM   1974 O O    . CYS A 1 348 ? 103.09000 115.83000 78.58100  1.000 31.19847  ? 348 CYS A O    1 
ATOM   1975 C CB   . CYS A 1 348 ? 99.99500  116.80200 78.97900  1.000 35.99160  ? 348 CYS A CB   1 
ATOM   1976 S SG   . CYS A 1 348 ? 98.64500  116.81800 77.78400  1.000 50.72643  ? 348 CYS A SG   1 
ATOM   1977 N N    . ALA A 1 349 ? 102.48500 115.87900 80.75300  1.000 39.99255  ? 349 ALA A N    1 
ATOM   1978 C CA   . ALA A 1 349 ? 103.85500 116.17200 81.15400  1.000 36.59557  ? 349 ALA A CA   1 
ATOM   1979 C C    . ALA A 1 349 ? 104.81000 115.04300 80.78200  1.000 38.87431  ? 349 ALA A C    1 
ATOM   1980 O O    . ALA A 1 349 ? 106.00700 115.29100 80.60200  1.000 42.68115  ? 349 ALA A O    1 
ATOM   1981 C CB   . ALA A 1 349 ? 103.92100 116.44600 82.65600  1.000 34.21225  ? 349 ALA A CB   1 
ATOM   1982 N N    . PHE A 1 350 ? 104.31100 113.81300 80.64500  1.000 33.82425  ? 350 PHE A N    1 
ATOM   1983 C CA   . PHE A 1 350 ? 105.15900 112.74400 80.10900  1.000 33.16009  ? 350 PHE A CA   1 
ATOM   1984 C C    . PHE A 1 350 ? 105.63600 113.05100 78.68600  1.000 30.82324  ? 350 PHE A C    1 
ATOM   1985 O O    . PHE A 1 350 ? 106.82200 112.88900 78.36500  1.000 33.98438  ? 350 PHE A O    1 
ATOM   1986 C CB   . PHE A 1 350 ? 104.42300 111.40400 80.14200  1.000 33.20495  ? 350 PHE A CB   1 
ATOM   1987 C CG   . PHE A 1 350 ? 104.24800 110.83900 81.51800  1.000 34.61155  ? 350 PHE A CG   1 
ATOM   1988 C CD1  . PHE A 1 350 ? 105.31900 110.77500 82.39100  1.000 37.00877  ? 350 PHE A CD1  1 
ATOM   1989 C CD2  . PHE A 1 350 ? 103.02300 110.35200 81.93400  1.000 38.42914  ? 350 PHE A CD2  1 
ATOM   1990 C CE1  . PHE A 1 350 ? 105.16900 110.25000 83.65700  1.000 37.97823  ? 350 PHE A CE1  1 
ATOM   1991 C CE2  . PHE A 1 350 ? 102.86700 109.82500 83.19900  1.000 41.17694  ? 350 PHE A CE2  1 
ATOM   1992 C CZ   . PHE A 1 350 ? 103.94200 109.77400 84.06000  1.000 37.75562  ? 350 PHE A CZ   1 
ATOM   1993 N N    . THR A 1 351 ? 104.72100 113.47400 77.81000  1.000 28.23034  ? 351 THR A N    1 
ATOM   1994 C CA   . THR A 1 351 ? 105.12400 113.87900 76.46500  1.000 32.57184  ? 351 THR A CA   1 
ATOM   1995 C C    . THR A 1 351 ? 106.13500 115.01700 76.51400  1.000 31.28204  ? 351 THR A C    1 
ATOM   1996 O O    . THR A 1 351 ? 107.06900 115.07200 75.70300  1.000 29.71055  ? 351 THR A O    1 
ATOM   1997 C CB   . THR A 1 351 ? 103.90400 114.28200 75.64000  1.000 38.84382  ? 351 THR A CB   1 
ATOM   1998 O OG1  . THR A 1 351 ? 102.90500 113.26000 75.73000  1.000 41.17832  ? 351 THR A OG1  1 
ATOM   1999 C CG2  . THR A 1 351 ? 104.29100 114.47000 74.18400  1.000 33.18575  ? 351 THR A CG2  1 
ATOM   2000 N N    . VAL A 1 352 ? 105.95800 115.94500 77.45400  1.000 39.45091  ? 352 VAL A N    1 
ATOM   2001 C CA   . VAL A 1 352 ? 106.90800 117.05400 77.54100  1.000 34.30743  ? 352 VAL A CA   1 
ATOM   2002 C C    . VAL A 1 352 ? 108.29100 116.54600 77.94900  1.000 36.18401  ? 352 VAL A C    1 
ATOM   2003 O O    . VAL A 1 352 ? 109.32100 117.00600 77.43300  1.000 37.24189  ? 352 VAL A O    1 
ATOM   2004 C CB   . VAL A 1 352 ? 106.39200 118.13400 78.50800  1.000 40.08029  ? 352 VAL A CB   1 
ATOM   2005 C CG1  . VAL A 1 352 ? 107.34400 119.31500 78.53100  1.000 39.37564  ? 352 VAL A CG1  1 
ATOM   2006 C CG2  . VAL A 1 352 ? 105.00400 118.58900 78.09600  1.000 42.23878  ? 352 VAL A CG2  1 
ATOM   2007 N N    . MET A 1 353 ? 108.33900 115.59700 78.88500  1.000 38.24626  ? 353 MET A N    1 
ATOM   2008 C CA   . MET A 1 353 ? 109.60500 114.95600 79.23300  1.000 33.12440  ? 353 MET A CA   1 
ATOM   2009 C C    . MET A 1 353 ? 110.24700 114.28000 78.02700  1.000 36.70052  ? 353 MET A C    1 
ATOM   2010 O O    . MET A 1 353 ? 111.47100 114.31900 77.86400  1.000 38.53316  ? 353 MET A O    1 
ATOM   2011 C CB   . MET A 1 353 ? 109.39000 113.94300 80.35600  1.000 36.39904  ? 353 MET A CB   1 
ATOM   2012 C CG   . MET A 1 353 ? 110.67600 113.46000 80.99900  1.000 41.19214  ? 353 MET A CG   1 
ATOM   2013 S SD   . MET A 1 353 ? 110.61500 111.72100 81.46600  1.000 53.59626  ? 353 MET A SD   1 
ATOM   2014 C CE   . MET A 1 353 ? 109.77100 111.82200 83.04200  1.000 44.77808  ? 353 MET A CE   1 
ATOM   2015 N N    . ALA A 1 354 ? 109.44200 113.64500 77.17300  1.000 38.68628  ? 354 ALA A N    1 
ATOM   2016 C CA   . ALA A 1 354 ? 110.01700 113.02300 75.97900  1.000 32.61143  ? 354 ALA A CA   1 
ATOM   2017 C C    . ALA A 1 354 ? 110.55400 114.06400 74.99900  1.000 37.52869  ? 354 ALA A C    1 
ATOM   2018 O O    . ALA A 1 354 ? 111.58100 113.83500 74.34100  1.000 33.14883  ? 354 ALA A O    1 
ATOM   2019 C CB   . ALA A 1 354 ? 108.98100 112.13400 75.29400  1.000 31.21479  ? 354 ALA A CB   1 
ATOM   2020 N N    . LEU A 1 355 ? 109.91200 115.23200 74.92800  1.000 40.03566  ? 355 LEU A N    1 
ATOM   2021 C CA   . LEU A 1 355 ? 110.43400 116.28000 74.05500  1.000 39.02364  ? 355 LEU A CA   1 
ATOM   2022 C C    . LEU A 1 355 ? 111.72900 116.86000 74.60300  1.000 41.74912  ? 355 LEU A C    1 
ATOM   2023 O O    . LEU A 1 355 ? 112.59500 117.28100 73.82900  1.000 36.71866  ? 355 LEU A O    1 
ATOM   2024 C CB   . LEU A 1 355 ? 109.40100 117.39100 73.86700  1.000 41.03278  ? 355 LEU A CB   1 
ATOM   2025 C CG   . LEU A 1 355 ? 108.26000 117.14200 72.88100  1.000 42.44318  ? 355 LEU A CG   1 
ATOM   2026 C CD1  . LEU A 1 355 ? 107.11200 118.10400 73.13600  1.000 38.03076  ? 355 LEU A CD1  1 
ATOM   2027 C CD2  . LEU A 1 355 ? 108.76300 117.27400 71.45500  1.000 38.21687  ? 355 LEU A CD2  1 
ATOM   2028 N N    . HIS A 1 356 ? 111.88300 116.88500 75.92800  1.000 47.88760  ? 356 HIS A N    1 
ATOM   2029 C CA   . HIS A 1 356 ? 113.17000 117.28300 76.49400  1.000 41.92292  ? 356 HIS A CA   1 
ATOM   2030 C C    . HIS A 1 356 ? 114.23600 116.22100 76.25100  1.000 45.76205  ? 356 HIS A C    1 
ATOM   2031 O O    . HIS A 1 356 ? 115.39600 116.54700 75.97300  1.000 44.78449  ? 356 HIS A O    1 
ATOM   2032 C CB   . HIS A 1 356 ? 113.03400 117.55500 77.99000  1.000 44.65583  ? 356 HIS A CB   1 
ATOM   2033 C CG   . HIS A 1 356 ? 114.27500 118.11500 78.61300  1.000 52.72164  ? 356 HIS A CG   1 
ATOM   2034 N ND1  . HIS A 1 356 ? 114.72200 117.73100 79.85800  1.000 52.20559  ? 356 HIS A ND1  1 
ATOM   2035 C CD2  . HIS A 1 356 ? 115.16700 119.02600 78.15800  1.000 50.39484  ? 356 HIS A CD2  1 
ATOM   2036 C CE1  . HIS A 1 356 ? 115.83400 118.38300 80.14500  1.000 48.57703  ? 356 HIS A CE1  1 
ATOM   2037 N NE2  . HIS A 1 356 ? 116.12500 119.17600 79.13100  1.000 49.33499  ? 356 HIS A NE2  1 
ATOM   2038 N N    . GLY A 1 357 ? 113.86000 114.94700 76.35200  1.000 47.49162  ? 357 GLY A N    1 
ATOM   2039 C CA   . GLY A 1 357 ? 114.78700 113.87500 76.02100  1.000 44.83145  ? 357 GLY A CA   1 
ATOM   2040 C C    . GLY A 1 357 ? 115.30300 113.95000 74.59700  1.000 45.00767  ? 357 GLY A C    1 
ATOM   2041 O O    . GLY A 1 357 ? 116.46000 113.61700 74.32800  1.000 44.37261  ? 357 GLY A O    1 
ATOM   2042 N N    . CYS A 1 358 ? 114.45300 114.37800 73.66300  1.000 51.99110  ? 358 CYS A N    1 
ATOM   2043 C CA   . CYS A 1 358 ? 114.90100 114.50300 72.27600  1.000 47.55474  ? 358 CYS A CA   1 
ATOM   2044 C C    . CYS A 1 358 ? 116.07600 115.46800 72.12200  1.000 46.85464  ? 358 CYS A C    1 
ATOM   2045 O O    . CYS A 1 358 ? 116.90500 115.29000 71.22400  1.000 44.64928  ? 358 CYS A O    1 
ATOM   2046 C CB   . CYS A 1 358 ? 113.74500 114.95000 71.38100  1.000 45.26875  ? 358 CYS A CB   1 
ATOM   2047 S SG   . CYS A 1 358 ? 112.91300 113.61200 70.50100  1.000 51.69306  ? 358 CYS A SG   1 
ATOM   2048 N N    . ILE A 1 359 ? 116.16600 116.49500 72.97200  1.000 52.15751  ? 359 ILE A N    1 
ATOM   2049 C CA   . ILE A 1 359 ? 117.28300 117.43600 72.88000  1.000 50.73094  ? 359 ILE A CA   1 
ATOM   2050 C C    . ILE A 1 359 ? 118.59900 116.81700 73.34400  1.000 52.77351  ? 359 ILE A C    1 
ATOM   2051 O O    . ILE A 1 359 ? 119.67200 117.20300 72.86600  1.000 53.19971  ? 359 ILE A O    1 
ATOM   2052 C CB   . ILE A 1 359 ? 116.97100 118.72300 73.66700  1.000 52.72940  ? 359 ILE A CB   1 
ATOM   2053 C CG1  . ILE A 1 359 ? 115.88300 119.53500 72.96300  1.000 50.81276  ? 359 ILE A CG1  1 
ATOM   2054 C CG2  . ILE A 1 359 ? 118.22600 119.56200 73.83400  1.000 49.11633  ? 359 ILE A CG2  1 
ATOM   2055 C CD1  . ILE A 1 359 ? 114.91000 120.19400 73.90900  1.000 52.00242  ? 359 ILE A CD1  1 
ATOM   2056 N N    . LEU A 1 360 ? 118.55500 115.86600 74.27400  1.000 55.29009  ? 360 LEU A N    1 
ATOM   2057 C CA   . LEU A 1 360 ? 119.76500 115.24300 74.79800  1.000 52.82918  ? 360 LEU A CA   1 
ATOM   2058 C C    . LEU A 1 360 ? 120.21700 114.02400 74.00500  1.000 56.44029  ? 360 LEU A C    1 
ATOM   2059 O O    . LEU A 1 360 ? 121.19600 113.38000 74.39600  1.000 55.66319  ? 360 LEU A O    1 
ATOM   2060 C CB   . LEU A 1 360 ? 119.56600 114.84700 76.26500  1.000 52.75538  ? 360 LEU A CB   1 
ATOM   2061 C CG   . LEU A 1 360 ? 118.97500 115.90500 77.19700  1.000 55.66861  ? 360 LEU A CG   1 
ATOM   2062 C CD1  . LEU A 1 360 ? 118.40800 115.25800 78.45100  1.000 50.81499  ? 360 LEU A CD1  1 
ATOM   2063 C CD2  . LEU A 1 360 ? 120.02200 116.94500 77.55500  1.000 53.94304  ? 360 LEU A CD2  1 
ATOM   2064 N N    . SER A 1 361 ? 119.54300 113.69100 72.90900  1.000 64.70936  ? 361 SER A N    1 
ATOM   2065 C CA   . SER A 1 361 ? 119.86900 112.47900 72.17200  1.000 61.57977  ? 361 SER A CA   1 
ATOM   2066 C C    . SER A 1 361 ? 121.22900 112.60300 71.49400  1.000 63.40132  ? 361 SER A C    1 
ATOM   2067 O O    . SER A 1 361 ? 121.60600 113.67000 71.00500  1.000 65.52913  ? 361 SER A O    1 
ATOM   2068 C CB   . SER A 1 361 ? 118.79000 112.18700 71.13200  1.000 63.31845  ? 361 SER A CB   1 
ATOM   2069 O OG   . SER A 1 361 ? 119.07400 112.83900 69.90700  1.000 66.17254  ? 361 SER A OG   1 
ATOM   2070 N N    . GLU A 1 362 ? 121.97100 111.49300 71.48200  1.000 67.70398  ? 362 GLU A N    1 
ATOM   2071 C CA   . GLU A 1 362 ? 123.27200 111.46500 70.82200  1.000 68.50553  ? 362 GLU A CA   1 
ATOM   2072 C C    . GLU A 1 362 ? 123.15800 111.79300 69.33700  1.000 69.31560  ? 362 GLU A C    1 
ATOM   2073 O O    . GLU A 1 362 ? 124.03500 112.45400 68.77000  1.000 70.47429  ? 362 GLU A O    1 
ATOM   2074 C CB   . GLU A 1 362 ? 123.92300 110.09500 71.01300  1.000 67.79787  ? 362 GLU A CB   1 
ATOM   2075 C CG   . GLU A 1 362 ? 123.75700 109.52100 72.40600  1.000 69.16329  ? 362 GLU A CG   1 
ATOM   2076 C CD   . GLU A 1 362 ? 125.07800 109.16200 73.04600  1.000 70.41526  ? 362 GLU A CD   1 
ATOM   2077 O OE1  . GLU A 1 362 ? 126.09500 109.12000 72.32300  1.000 72.08186  ? 362 GLU A OE1  1 
ATOM   2078 O OE2  . GLU A 1 362 ? 125.10100 108.92500 74.27200  1.000 70.59434  ? 362 GLU A OE2  1 
ATOM   2079 N N    . ILE A 1 363 ? 122.09100 111.33300 68.69100  1.000 67.94664  ? 363 ILE A N    1 
ATOM   2080 C CA   . ILE A 1 363 ? 121.89700 111.50200 67.25500  1.000 68.57360  ? 363 ILE A CA   1 
ATOM   2081 C C    . ILE A 1 363 ? 120.95700 112.67700 67.02200  1.000 70.41742  ? 363 ILE A C    1 
ATOM   2082 O O    . ILE A 1 363 ? 119.80000 112.65300 67.45800  1.000 70.60041  ? 363 ILE A O    1 
ATOM   2083 C CB   . ILE A 1 363 ? 121.34400 110.21900 66.61500  1.000 70.42997  ? 363 ILE A CB   1 
ATOM   2084 C CG1  . ILE A 1 363 ? 122.33700 109.06800 66.78800  1.000 71.04391  ? 363 ILE A CG1  1 
ATOM   2085 C CG2  . ILE A 1 363 ? 121.03100 110.44700 65.14600  1.000 71.01117  ? 363 ILE A CG2  1 
ATOM   2086 C CD1  . ILE A 1 363 ? 121.89200 107.77500 66.14800  1.000 70.63910  ? 363 ILE A CD1  1 
ATOM   2087 N N    . GLN A 1 364 ? 121.45400 113.70800 66.34100  1.000 71.36220  ? 364 GLN A N    1 
ATOM   2088 C CA   . GLN A 1 364 ? 120.68600 114.91300 66.06500  1.000 69.98391  ? 364 GLN A CA   1 
ATOM   2089 C C    . GLN A 1 364 ? 120.79800 115.27500 64.59000  1.000 70.03003  ? 364 GLN A C    1 
ATOM   2090 O O    . GLN A 1 364 ? 121.73000 114.86300 63.89500  1.000 71.99519  ? 364 GLN A O    1 
ATOM   2091 C CB   . GLN A 1 364 ? 121.15000 116.08800 66.93600  1.000 68.92707  ? 364 GLN A CB   1 
ATOM   2092 C CG   . GLN A 1 364 ? 121.69900 115.67400 68.28800  1.000 68.86578  ? 364 GLN A CG   1 
ATOM   2093 C CD   . GLN A 1 364 ? 121.39700 116.68600 69.37300  1.000 69.86342  ? 364 GLN A CD   1 
ATOM   2094 O OE1  . GLN A 1 364 ? 120.86600 117.76200 69.10200  1.000 71.06218  ? 364 GLN A OE1  1 
ATOM   2095 N NE2  . GLN A 1 364 ? 121.73400 116.34600 70.61000  1.000 68.21349  ? 364 GLN A NE2  1 
ATOM   2096 N N    . ALA A 1 365 ? 119.80900 116.07500 64.11100  1.000 74.21016  ? 365 ALA A N    1 
ATOM   2097 C CA   . ALA A 1 365 ? 119.59300 116.52100 62.74200  1.000 75.14865  ? 365 ALA A CA   1 
ATOM   2098 C C    . ALA A 1 365 ? 120.30200 117.84500 62.47100  1.000 76.71634  ? 365 ALA A C    1 
ATOM   2099 O O    . ALA A 1 365 ? 120.47100 118.66600 63.37900  1.000 76.88779  ? 365 ALA A O    1 
ATOM   2100 C CB   . ALA A 1 365 ? 118.10200 116.67900 62.46500  1.000 72.15685  ? 365 ALA A CB   1 
ATOM   2101 N N    . PRO A 1 366 ? 120.73100 118.06600 61.22900  1.000 76.84664  ? 366 PRO A N    1 
ATOM   2102 C CA   . PRO A 1 366 ? 121.34500 119.35300 60.87700  1.000 76.86753  ? 366 PRO A CA   1 
ATOM   2103 C C    . PRO A 1 366 ? 120.40100 120.52000 61.13400  1.000 76.87776  ? 366 PRO A C    1 
ATOM   2104 O O    . PRO A 1 366 ? 119.21400 120.47200 60.80600  1.000 77.96090  ? 366 PRO A O    1 
ATOM   2105 C CB   . PRO A 1 366 ? 121.67100 119.20300 59.38700  1.000 76.28919  ? 366 PRO A CB   1 
ATOM   2106 C CG   . PRO A 1 366 ? 120.83300 118.08000 58.89800  1.000 75.61541  ? 366 PRO A CG   1 
ATOM   2107 C CD   . PRO A 1 366 ? 120.51400 117.19600 60.06100  1.000 73.96688  ? 366 PRO A CD   1 
ATOM   2108 N N    . GLU A 1 367 ? 120.95000 121.57900 61.73400  1.000 77.92819  ? 367 GLU A N    1 
ATOM   2109 C CA   . GLU A 1 367 ? 120.15000 122.75200 62.08100  1.000 78.48699  ? 367 GLU A CA   1 
ATOM   2110 C C    . GLU A 1 367 ? 119.53400 123.40900 60.85000  1.000 77.91727  ? 367 GLU A C    1 
ATOM   2111 O O    . GLU A 1 367 ? 118.38600 123.87300 60.89500  1.000 77.29304  ? 367 GLU A O    1 
ATOM   2112 C CB   . GLU A 1 367 ? 121.00600 123.75200 62.85900  1.000 78.80256  ? 367 GLU A CB   1 
ATOM   2113 C CG   . GLU A 1 367 ? 121.61800 124.85600 62.01500  1.000 80.94109  ? 367 GLU A CG   1 
ATOM   2114 C CD   . GLU A 1 367 ? 122.17100 125.99100 62.85400  1.000 81.01796  ? 367 GLU A CD   1 
ATOM   2115 O OE1  . GLU A 1 367 ? 123.29700 125.85200 63.37600  1.000 80.66853  ? 367 GLU A OE1  1 
ATOM   2116 O OE2  . GLU A 1 367 ? 121.47900 127.02100 62.99400  1.000 78.86746  ? 367 GLU A OE2  1 
ATOM   2117 N N    . GLU A 1 368 ? 120.29300 123.49700 59.75400  1.000 81.25635  ? 368 GLU A N    1 
ATOM   2118 C CA   . GLU A 1 368 ? 119.76200 124.09000 58.53000  1.000 82.12522  ? 368 GLU A CA   1 
ATOM   2119 C C    . GLU A 1 368 ? 118.46600 123.42600 58.08600  1.000 83.36412  ? 368 GLU A C    1 
ATOM   2120 O O    . GLU A 1 368 ? 117.59900 124.08700 57.50200  1.000 83.33563  ? 368 GLU A O    1 
ATOM   2121 C CB   . GLU A 1 368 ? 120.80100 124.01800 57.40800  1.000 80.07123  ? 368 GLU A CB   1 
ATOM   2122 C CG   . GLU A 1 368 ? 121.52500 122.68600 57.28900  1.000 82.99330  ? 368 GLU A CG   1 
ATOM   2123 C CD   . GLU A 1 368 ? 122.66600 122.55100 58.27900  1.000 85.01195  ? 368 GLU A CD   1 
ATOM   2124 O OE1  . GLU A 1 368 ? 122.73300 123.36600 59.22200  1.000 84.33847  ? 368 GLU A OE1  1 
ATOM   2125 O OE2  . GLU A 1 368 ? 123.49600 121.63400 58.11100  1.000 84.19684  ? 368 GLU A OE2  1 
ATOM   2126 N N    . ARG A 1 369 ? 118.31200 122.12600 58.34100  1.000 78.84894  ? 369 ARG A N    1 
ATOM   2127 C CA   . ARG A 1 369 ? 117.05700 121.46000 58.01300  1.000 76.84782  ? 369 ARG A CA   1 
ATOM   2128 C C    . ARG A 1 369 ? 115.95600 121.78000 59.01700  1.000 77.53070  ? 369 ARG A C    1 
ATOM   2129 O O    . ARG A 1 369 ? 114.78500 121.87100 58.63300  1.000 78.72224  ? 369 ARG A O    1 
ATOM   2130 C CB   . ARG A 1 369 ? 117.26900 119.94900 57.91700  1.000 76.38114  ? 369 ARG A CB   1 
ATOM   2131 C CG   . ARG A 1 369 ? 117.59100 119.47700 56.50800  1.000 78.35207  ? 369 ARG A CG   1 
ATOM   2132 C CD   . ARG A 1 369 ? 118.59900 118.34300 56.50000  1.000 79.36070  ? 369 ARG A CD   1 
ATOM   2133 N NE   . ARG A 1 369 ? 118.50600 117.55400 55.27800  1.000 81.17120  ? 369 ARG A NE   1 
ATOM   2134 C CZ   . ARG A 1 369 ? 119.21800 116.46400 55.03100  1.000 81.35374  ? 369 ARG A CZ   1 
ATOM   2135 N NH1  . ARG A 1 369 ? 120.09600 116.00000 55.90400  1.000 80.31018  ? 369 ARG A NH1  1 
ATOM   2136 N NH2  . ARG A 1 369 ? 119.04600 115.82300 53.87800  1.000 79.08945  ? 369 ARG A NH2  1 
ATOM   2137 N N    . ARG A 1 370 ? 116.30100 121.94800 60.29600  1.000 66.15004  ? 370 ARG A N    1 
ATOM   2138 C CA   . ARG A 1 370 ? 115.29700 122.33500 61.28200  1.000 66.51905  ? 370 ARG A CA   1 
ATOM   2139 C C    . ARG A 1 370 ? 114.71900 123.71000 60.97500  1.000 68.59239  ? 370 ARG A C    1 
ATOM   2140 O O    . ARG A 1 370 ? 113.50700 123.92500 61.09600  1.000 68.78249  ? 370 ARG A O    1 
ATOM   2141 C CB   . ARG A 1 370 ? 115.89700 122.32600 62.68800  1.000 66.24730  ? 370 ARG A CB   1 
ATOM   2142 C CG   . ARG A 1 370 ? 116.87200 121.20500 62.98000  1.000 64.86438  ? 370 ARG A CG   1 
ATOM   2143 C CD   . ARG A 1 370 ? 117.42700 121.36700 64.38500  1.000 64.38753  ? 370 ARG A CD   1 
ATOM   2144 N NE   . ARG A 1 370 ? 118.40300 120.34300 64.73300  1.000 65.09524  ? 370 ARG A NE   1 
ATOM   2145 C CZ   . ARG A 1 370 ? 118.83800 120.11700 65.96400  1.000 67.00699  ? 370 ARG A CZ   1 
ATOM   2146 N NH1  . ARG A 1 370 ? 118.41000 120.83300 66.99100  1.000 65.03745  ? 370 ARG A NH1  1 
ATOM   2147 N NH2  . ARG A 1 370 ? 119.72700 119.15000 66.17200  1.000 66.27596  ? 370 ARG A NH2  1 
ATOM   2148 N N    . GLN A 1 371 ? 115.57300 124.65500 60.57800  1.000 73.93682  ? 371 GLN A N    1 
ATOM   2149 C CA   . GLN A 1 371 ? 115.13200 126.02800 60.34200  1.000 73.92779  ? 371 GLN A CA   1 
ATOM   2150 C C    . GLN A 1 371 ? 113.98600 126.13200 59.34300  1.000 75.38928  ? 371 GLN A C    1 
ATOM   2151 O O    . GLN A 1 371 ? 113.28500 127.15000 59.33000  1.000 79.26295  ? 371 GLN A O    1 
ATOM   2152 C CB   . GLN A 1 371 ? 116.31000 126.87900 59.86800  1.000 73.18537  ? 371 GLN A CB   1 
ATOM   2153 C CG   . GLN A 1 371 ? 117.49900 126.86700 60.81200  1.000 74.96039  ? 371 GLN A CG   1 
ATOM   2154 C CD   . GLN A 1 371 ? 117.14000 127.34900 62.20400  1.000 75.68770  ? 371 GLN A CD   1 
ATOM   2155 O OE1  . GLN A 1 371 ? 116.49600 128.38400 62.36700  1.000 77.31310  ? 371 GLN A OE1  1 
ATOM   2156 N NE2  . GLN A 1 371 ? 117.55400 126.59700 63.21700  1.000 74.17519  ? 371 GLN A NE2  1 
ATOM   2157 N N    . VAL A 1 372 ? 113.78300 125.12000 58.49900  1.000 69.06888  ? 372 VAL A N    1 
ATOM   2158 C CA   . VAL A 1 372 ? 112.67800 125.16300 57.54500  1.000 69.11712  ? 372 VAL A CA   1 
ATOM   2159 C C    . VAL A 1 372 ? 111.31500 125.10000 58.23300  1.000 70.91643  ? 372 VAL A C    1 
ATOM   2160 O O    . VAL A 1 372 ? 110.32500 125.61000 57.69500  1.000 73.06798  ? 372 VAL A O    1 
ATOM   2161 C CB   . VAL A 1 372 ? 112.83500 124.02900 56.51600  1.000 68.35690  ? 372 VAL A CB   1 
ATOM   2162 C CG1  . VAL A 1 372 ? 111.52700 123.79200 55.77900  1.000 68.30162  ? 372 VAL A CG1  1 
ATOM   2163 C CG2  . VAL A 1 372 ? 113.95300 124.35100 55.53900  1.000 71.47112  ? 372 VAL A CG2  1 
ATOM   2164 N N    . PHE A 1 373 ? 111.22600 124.49000 59.41600  1.000 69.63187  ? 373 PHE A N    1 
ATOM   2165 C CA   . PHE A 1 373 ? 109.94700 124.29900 60.09600  1.000 69.75766  ? 373 PHE A CA   1 
ATOM   2166 C C    . PHE A 1 373 ? 109.78100 125.15300 61.35000  1.000 69.41712  ? 373 PHE A C    1 
ATOM   2167 O O    . PHE A 1 373 ? 108.81800 124.95100 62.09700  1.000 71.98978  ? 373 PHE A O    1 
ATOM   2168 C CB   . PHE A 1 373 ? 109.77100 122.82300 60.46500  1.000 71.04561  ? 373 PHE A CB   1 
ATOM   2169 C CG   . PHE A 1 373 ? 109.86500 121.88400 59.29700  1.000 68.34518  ? 373 PHE A CG   1 
ATOM   2170 C CD1  . PHE A 1 373 ? 108.74000 121.54500 58.56800  1.000 69.78293  ? 373 PHE A CD1  1 
ATOM   2171 C CD2  . PHE A 1 373 ? 111.08100 121.32700 58.94000  1.000 68.26354  ? 373 PHE A CD2  1 
ATOM   2172 C CE1  . PHE A 1 373 ? 108.82700 120.67500 57.49800  1.000 70.07971  ? 373 PHE A CE1  1 
ATOM   2173 C CE2  . PHE A 1 373 ? 111.17400 120.45800 57.87100  1.000 69.49678  ? 373 PHE A CE2  1 
ATOM   2174 C CZ   . PHE A 1 373 ? 110.04500 120.13100 57.15000  1.000 69.61901  ? 373 PHE A CZ   1 
ATOM   2175 N N    . ARG A 1 374 ? 110.68900 126.09600 61.60200  1.000 69.29381  ? 374 ARG A N    1 
ATOM   2176 C CA   . ARG A 1 374 ? 110.67200 126.85800 62.85000  1.000 71.92554  ? 374 ARG A CA   1 
ATOM   2177 C C    . ARG A 1 374 ? 109.31800 127.50800 63.14200  1.000 72.97359  ? 374 ARG A C    1 
ATOM   2178 O O    . ARG A 1 374 ? 108.81900 127.44600 64.27300  1.000 75.87760  ? 374 ARG A O    1 
ATOM   2179 C CB   . ARG A 1 374 ? 111.77900 127.91300 62.81800  1.000 72.76717  ? 374 ARG A CB   1 
ATOM   2180 C CG   . ARG A 1 374 ? 111.42700 129.20800 63.52300  1.000 72.38946  ? 374 ARG A CG   1 
ATOM   2181 C CD   . ARG A 1 374 ? 112.26700 130.35600 62.99700  1.000 73.35355  ? 374 ARG A CD   1 
ATOM   2182 N NE   . ARG A 1 374 ? 113.65200 130.24500 63.43700  1.000 75.14008  ? 374 ARG A NE   1 
ATOM   2183 C CZ   . ARG A 1 374 ? 114.14900 130.85300 64.50500  1.000 74.77161  ? 374 ARG A CZ   1 
ATOM   2184 N NH1  . ARG A 1 374 ? 113.40000 131.62800 65.27100  1.000 73.04848  ? 374 ARG A NH1  1 
ATOM   2185 N NH2  . ARG A 1 374 ? 115.43000 130.67600 64.81600  1.000 72.95707  ? 374 ARG A NH2  1 
ATOM   2186 N N    . GLN A 1 375 ? 108.70900 128.14000 62.13600  1.000 71.90057  ? 375 GLN A N    1 
ATOM   2187 C CA   . GLN A 1 375 ? 107.50500 128.93400 62.38500  1.000 72.42509  ? 375 GLN A CA   1 
ATOM   2188 C C    . GLN A 1 375 ? 106.34000 128.08900 62.89700  1.000 73.47065  ? 375 GLN A C    1 
ATOM   2189 O O    . GLN A 1 375 ? 105.64400 128.49100 63.84100  1.000 75.33714  ? 375 GLN A O    1 
ATOM   2190 C CB   . GLN A 1 375 ? 107.10000 129.68200 61.11400  1.000 71.09223  ? 375 GLN A CB   1 
ATOM   2191 C CG   . GLN A 1 375 ? 108.23300 129.91500 60.12200  1.000 72.71855  ? 375 GLN A CG   1 
ATOM   2192 C CD   . GLN A 1 375 ? 108.52600 128.70200 59.25900  1.000 74.44884  ? 375 GLN A CD   1 
ATOM   2193 O OE1  . GLN A 1 375 ? 107.61500 128.07400 58.71900  1.000 75.39407  ? 375 GLN A OE1  1 
ATOM   2194 N NE2  . GLN A 1 375 ? 109.80500 128.37000 59.12100  1.000 73.76371  ? 375 GLN A NE2  1 
ATOM   2195 N N    . GLU A 1 376 ? 106.11500 126.91400 62.30700  1.000 67.52376  ? 376 GLU A N    1 
ATOM   2196 C CA   . GLU A 1 376 ? 104.98700 126.09500 62.74300  1.000 68.42377  ? 376 GLU A CA   1 
ATOM   2197 C C    . GLU A 1 376 ? 105.20000 125.57000 64.15700  1.000 69.59401  ? 376 GLU A C    1 
ATOM   2198 O O    . GLU A 1 376 ? 104.26300 125.54600 64.97000  1.000 72.42110  ? 376 GLU A O    1 
ATOM   2199 C CB   . GLU A 1 376 ? 104.77300 124.93900 61.76900  1.000 68.17818  ? 376 GLU A CB   1 
ATOM   2200 C CG   . GLU A 1 376 ? 103.92500 125.29400 60.56100  1.000 68.54795  ? 376 GLU A CG   1 
ATOM   2201 C CD   . GLU A 1 376 ? 104.71000 126.03100 59.49800  1.000 70.87091  ? 376 GLU A CD   1 
ATOM   2202 O OE1  . GLU A 1 376 ? 105.94500 126.14100 59.64100  1.000 70.20897  ? 376 GLU A OE1  1 
ATOM   2203 O OE2  . GLU A 1 376 ? 104.09300 126.50000 58.51900  1.000 72.20916  ? 376 GLU A OE2  1 
ATOM   2204 N N    . LEU A 1 377 ? 106.43800 125.20000 64.48700  1.000 58.19908  ? 377 LEU A N    1 
ATOM   2205 C CA   . LEU A 1 377 ? 106.71700 124.69300 65.82200  1.000 61.61792  ? 377 LEU A CA   1 
ATOM   2206 C C    . LEU A 1 377 ? 106.55900 125.79500 66.85900  1.000 65.26425  ? 377 LEU A C    1 
ATOM   2207 O O    . LEU A 1 377 ? 106.03600 125.55800 67.95700  1.000 66.08553  ? 377 LEU A O    1 
ATOM   2208 C CB   . LEU A 1 377 ? 108.12500 124.10000 65.86600  1.000 63.72281  ? 377 LEU A CB   1 
ATOM   2209 C CG   . LEU A 1 377 ? 108.41200 122.96200 64.88200  1.000 62.41684  ? 377 LEU A CG   1 
ATOM   2210 C CD1  . LEU A 1 377 ? 109.88800 122.92100 64.51700  1.000 58.74204  ? 377 LEU A CD1  1 
ATOM   2211 C CD2  . LEU A 1 377 ? 107.95900 121.62200 65.43700  1.000 62.36625  ? 377 LEU A CD2  1 
ATOM   2212 N N    . GLN A 1 378 ? 106.94000 127.02500 66.50400  1.000 63.47389  ? 378 GLN A N    1 
ATOM   2213 C CA   . GLN A 1 378 ? 106.82900 128.10900 67.47000  1.000 63.42135  ? 378 GLN A CA   1 
ATOM   2214 C C    . GLN A 1 378 ? 105.38100 128.54000 67.65200  1.000 62.73764  ? 378 GLN A C    1 
ATOM   2215 O O    . GLN A 1 378 ? 104.97800 128.89500 68.76600  1.000 65.75885  ? 378 GLN A O    1 
ATOM   2216 C CB   . GLN A 1 378 ? 107.68600 129.29500 67.03200  1.000 61.85981  ? 378 GLN A CB   1 
ATOM   2217 C CG   . GLN A 1 378 ? 109.16500 128.98300 66.92700  1.000 68.00432  ? 378 GLN A CG   1 
ATOM   2218 C CD   . GLN A 1 378 ? 110.02200 130.23100 66.92200  1.000 70.51133  ? 378 GLN A CD   1 
ATOM   2219 O OE1  . GLN A 1 378 ? 110.90100 130.39800 67.76800  1.000 67.98878  ? 378 GLN A OE1  1 
ATOM   2220 N NE2  . GLN A 1 378 ? 109.77000 131.11800 65.96800  1.000 69.49983  ? 378 GLN A NE2  1 
ATOM   2221 N N    . ARG A 1 379 ? 104.57200 128.46900 66.59200  1.000 54.31116  ? 379 ARG A N    1 
ATOM   2222 C CA   . ARG A 1 379 ? 103.15300 128.76400 66.75400  1.000 56.33581  ? 379 ARG A CA   1 
ATOM   2223 C C    . ARG A 1 379 ? 102.47100 127.71600 67.62800  1.000 56.08861  ? 379 ARG A C    1 
ATOM   2224 O O    . ARG A 1 379 ? 101.67400 128.06000 68.51400  1.000 59.15694  ? 379 ARG A O    1 
ATOM   2225 C CB   . ARG A 1 379 ? 102.47400 128.85600 65.38800  1.000 56.99714  ? 379 ARG A CB   1 
ATOM   2226 C CG   . ARG A 1 379 ? 101.39100 129.92000 65.31700  1.000 58.89855  ? 379 ARG A CG   1 
ATOM   2227 C CD   . ARG A 1 379 ? 100.44300 129.69000 64.15400  1.000 59.49619  ? 379 ARG A CD   1 
ATOM   2228 N NE   . ARG A 1 379 ? 99.05900  129.95400 64.53000  1.000 61.36866  ? 379 ARG A NE   1 
ATOM   2229 C CZ   . ARG A 1 379 ? 98.00300  129.43000 63.92300  1.000 62.62939  ? 379 ARG A CZ   1 
ATOM   2230 N NH1  . ARG A 1 379 ? 98.13400  128.59300 62.90700  1.000 63.10875  ? 379 ARG A NH1  1 
ATOM   2231 N NH2  . ARG A 1 379 ? 96.78500  129.74800 64.35200  1.000 57.63577  ? 379 ARG A NH2  1 
ATOM   2232 N N    . VAL A 1 380 ? 102.80000 126.43700 67.42300  1.000 51.38793  ? 380 VAL A N    1 
ATOM   2233 C CA   . VAL A 1 380 ? 102.22400 125.39200 68.26700  1.000 51.36077  ? 380 VAL A CA   1 
ATOM   2234 C C    . VAL A 1 380 ? 102.62200 125.59900 69.72300  1.000 52.46988  ? 380 VAL A C    1 
ATOM   2235 O O    . VAL A 1 380 ? 101.79000 125.48300 70.63500  1.000 53.53511  ? 380 VAL A O    1 
ATOM   2236 C CB   . VAL A 1 380 ? 102.64200 124.00000 67.76000  1.000 52.87651  ? 380 VAL A CB   1 
ATOM   2237 C CG1  . VAL A 1 380 ? 101.94200 122.91300 68.55800  1.000 53.97001  ? 380 VAL A CG1  1 
ATOM   2238 C CG2  . VAL A 1 380 ? 102.32600 123.85800 66.28200  1.000 53.45166  ? 380 VAL A CG2  1 
ATOM   2239 N N    . GLY A 1 381 ? 103.89300 125.92900 69.96600  1.000 48.39035  ? 381 GLY A N    1 
ATOM   2240 C CA   . GLY A 1 381 ? 104.33700 126.13900 71.33400  1.000 48.04274  ? 381 GLY A CA   1 
ATOM   2241 C C    . GLY A 1 381 ? 103.64100 127.31000 72.00100  1.000 50.52494  ? 381 GLY A C    1 
ATOM   2242 O O    . GLY A 1 381 ? 103.17400 127.20800 73.14200  1.000 52.15483  ? 381 GLY A O    1 
ATOM   2243 N N    . VAL A 1 382 ? 103.58200 128.44900 71.30600  1.000 48.23154  ? 382 VAL A N    1 
ATOM   2244 C CA   . VAL A 1 382 ? 102.92000 129.62700 71.86000  1.000 49.29230  ? 382 VAL A CA   1 
ATOM   2245 C C    . VAL A 1 382 ? 101.46400 129.32500 72.19400  1.000 49.02462  ? 382 VAL A C    1 
ATOM   2246 O O    . VAL A 1 382 ? 100.97100 129.68700 73.27400  1.000 54.34178  ? 382 VAL A O    1 
ATOM   2247 C CB   . VAL A 1 382 ? 103.04000 130.81000 70.88200  1.000 50.59042  ? 382 VAL A CB   1 
ATOM   2248 C CG1  . VAL A 1 382 ? 101.97100 131.85000 71.17000  1.000 50.22815  ? 382 VAL A CG1  1 
ATOM   2249 C CG2  . VAL A 1 382 ? 104.42600 131.42600 70.96200  1.000 49.95220  ? 382 VAL A CG2  1 
ATOM   2250 N N    . GLU A 1 383 ? 100.75700 128.63200 71.29600  1.000 49.44611  ? 383 GLU A N    1 
ATOM   2251 C CA   . GLU A 1 383 ? 99.34200  128.37800 71.54800  1.000 51.45855  ? 383 GLU A CA   1 
ATOM   2252 C C    . GLU A 1 383 ? 99.14500  127.41300 72.71200  1.000 51.24478  ? 383 GLU A C    1 
ATOM   2253 O O    . GLU A 1 383 ? 98.25200  127.61500 73.54800  1.000 51.14083  ? 383 GLU A O    1 
ATOM   2254 C CB   . GLU A 1 383 ? 98.67200  127.84100 70.28500  1.000 49.22373  ? 383 GLU A CB   1 
ATOM   2255 C CG   . GLU A 1 383 ? 98.79000  128.76500 69.08600  1.000 52.05578  ? 383 GLU A CG   1 
ATOM   2256 C CD   . GLU A 1 383 ? 97.83400  129.93700 69.15100  1.000 59.38635  ? 383 GLU A CD   1 
ATOM   2257 O OE1  . GLU A 1 383 ? 97.43900  130.32500 70.27000  1.000 58.48257  ? 383 GLU A OE1  1 
ATOM   2258 O OE2  . GLU A 1 383 ? 97.47800  130.47500 68.08200  1.000 63.14040  ? 383 GLU A OE2  1 
ATOM   2259 N N    . GLY A 1 384 ? 99.98900  126.38300 72.81200  1.000 45.13720  ? 384 GLY A N    1 
ATOM   2260 C CA   . GLY A 1 384 ? 99.86900  125.46500 73.93300  1.000 42.57220  ? 384 GLY A CA   1 
ATOM   2261 C C    . GLY A 1 384 ? 100.14500 126.13400 75.26500  1.000 45.93859  ? 384 GLY A C    1 
ATOM   2262 O O    . GLY A 1 384 ? 99.44000  125.89600 76.25300  1.000 46.38759  ? 384 GLY A O    1 
ATOM   2263 N N    . ALA A 1 385 ? 101.15800 127.00400 75.30600  1.000 43.99211  ? 385 ALA A N    1 
ATOM   2264 C CA   . ALA A 1 385 ? 101.47500 127.68100 76.55800  1.000 43.10938  ? 385 ALA A CA   1 
ATOM   2265 C C    . ALA A 1 385 ? 100.36400 128.64200 76.95900  1.000 43.33613  ? 385 ALA A C    1 
ATOM   2266 O O    . ALA A 1 385 ? 99.99400  128.71800 78.14000  1.000 45.30553  ? 385 ALA A O    1 
ATOM   2267 C CB   . ALA A 1 385 ? 102.80800 128.41600 76.43500  1.000 42.79771  ? 385 ALA A CB   1 
ATOM   2268 N N    . LYS A 1 386 ? 99.78900  129.35500 75.98700  1.000 46.74534  ? 386 LYS A N    1 
ATOM   2269 C CA   . LYS A 1 386 ? 98.69400  130.26400 76.30700  1.000 45.20579  ? 386 LYS A CA   1 
ATOM   2270 C C    . LYS A 1 386 ? 97.47900  129.50200 76.82500  1.000 43.89410  ? 386 LYS A C    1 
ATOM   2271 O O    . LYS A 1 386 ? 96.82000  129.93800 77.77800  1.000 44.99214  ? 386 LYS A O    1 
ATOM   2272 C CB   . LYS A 1 386 ? 98.33300  131.09700 75.07800  1.000 44.90197  ? 386 LYS A CB   1 
ATOM   2273 C CG   . LYS A 1 386 ? 96.89300  131.56800 75.04000  1.000 45.01532  ? 386 LYS A CG   1 
ATOM   2274 C CD   . LYS A 1 386 ? 96.66700  132.50500 73.87000  1.000 46.62736  ? 386 LYS A CD   1 
ATOM   2275 C CE   . LYS A 1 386 ? 97.80300  133.50600 73.74900  1.000 47.32651  ? 386 LYS A CE   1 
ATOM   2276 N NZ   . LYS A 1 386 ? 97.98500  133.97900 72.34900  1.000 49.43782  ? 386 LYS A NZ   1 
ATOM   2277 N N    . LEU A 1 387 ? 97.17400  128.35200 76.22200  1.000 41.58519  ? 387 LEU A N    1 
ATOM   2278 C CA   . LEU A 1 387 ? 96.03700  127.56100 76.68400  1.000 39.82404  ? 387 LEU A CA   1 
ATOM   2279 C C    . LEU A 1 387 ? 96.25600  127.04900 78.10600  1.000 40.21803  ? 387 LEU A C    1 
ATOM   2280 O O    . LEU A 1 387 ? 95.35100  127.12000 78.95300  1.000 41.24092  ? 387 LEU A O    1 
ATOM   2281 C CB   . LEU A 1 387 ? 95.78800  126.40400 75.71600  1.000 44.16546  ? 387 LEU A CB   1 
ATOM   2282 C CG   . LEU A 1 387 ? 94.46900  125.63100 75.78300  1.000 42.37067  ? 387 LEU A CG   1 
ATOM   2283 C CD1  . LEU A 1 387 ? 94.44000  124.60600 74.67200  1.000 44.45331  ? 387 LEU A CD1  1 
ATOM   2284 C CD2  . LEU A 1 387 ? 94.27300  124.95100 77.12600  1.000 43.71739  ? 387 LEU A CD2  1 
ATOM   2285 N N    . LEU A 1 388 ? 97.44800  126.51300 78.38800  1.000 39.28447  ? 388 LEU A N    1 
ATOM   2286 C CA   . LEU A 1 388 ? 97.71900  126.04200 79.74500  1.000 37.54202  ? 388 LEU A CA   1 
ATOM   2287 C C    . LEU A 1 388 ? 97.67500  127.17300 80.76700  1.000 42.08632  ? 388 LEU A C    1 
ATOM   2288 O O    . LEU A 1 388 ? 97.18200  126.97700 81.88800  1.000 43.57895  ? 388 LEU A O    1 
ATOM   2289 C CB   . LEU A 1 388 ? 99.07100  125.33000 79.79600  1.000 42.42861  ? 388 LEU A CB   1 
ATOM   2290 C CG   . LEU A 1 388 ? 99.16600  124.00800 79.03100  1.000 44.41259  ? 388 LEU A CG   1 
ATOM   2291 C CD1  . LEU A 1 388 ? 100.60000 123.51900 78.96900  1.000 39.18911  ? 388 LEU A CD1  1 
ATOM   2292 C CD2  . LEU A 1 388 ? 98.27400  122.96000 79.67300  1.000 38.71655  ? 388 LEU A CD2  1 
ATOM   2293 N N    . ARG A 1 389 ? 98.09500  128.38300 80.38600  1.000 47.09840  ? 389 ARG A N    1 
ATOM   2294 C CA   . ARG A 1 389 ? 98.03800  129.47300 81.35400  1.000 40.28110  ? 389 ARG A CA   1 
ATOM   2295 C C    . ARG A 1 389 ? 96.61900  129.98400 81.54900  1.000 44.76873  ? 389 ARG A C    1 
ATOM   2296 O O    . ARG A 1 389 ? 96.26500  130.41600 82.65400  1.000 44.79067  ? 389 ARG A O    1 
ATOM   2297 C CB   . ARG A 1 389 ? 98.95000  130.62300 80.92700  1.000 38.89142  ? 389 ARG A CB   1 
ATOM   2298 C CG   . ARG A 1 389 ? 100.42900 130.36200 81.13600  1.000 43.84447  ? 389 ARG A CG   1 
ATOM   2299 C CD   . ARG A 1 389 ? 101.27000 131.49100 80.56900  1.000 43.00926  ? 389 ARG A CD   1 
ATOM   2300 N NE   . ARG A 1 389 ? 102.69600 131.20000 80.64700  1.000 46.28202  ? 389 ARG A NE   1 
ATOM   2301 C CZ   . ARG A 1 389 ? 103.51700 131.19900 79.60700  1.000 45.06412  ? 389 ARG A CZ   1 
ATOM   2302 N NH1  . ARG A 1 389 ? 103.09100 131.48900 78.38900  1.000 41.91854  ? 389 ARG A NH1  1 
ATOM   2303 N NH2  . ARG A 1 389 ? 104.80000 130.90300 79.79400  1.000 41.54500  ? 389 ARG A NH2  1 
ATOM   2304 N N    . GLU A 1 390 ? 95.77100  129.86900 80.52800  1.000 48.35026  ? 390 GLU A N    1 
ATOM   2305 C CA   . GLU A 1 390 ? 94.38200  130.27300 80.70600  1.000 43.65585  ? 390 GLU A CA   1 
ATOM   2306 C C    . GLU A 1 390 ? 93.64000  129.28300 81.59400  1.000 44.09777  ? 390 GLU A C    1 
ATOM   2307 O O    . GLU A 1 390 ? 92.84200  129.68400 82.45200  1.000 42.58892  ? 390 GLU A O    1 
ATOM   2308 C CB   . GLU A 1 390 ? 93.69500  130.40600 79.34800  1.000 42.75851  ? 390 GLU A CB   1 
ATOM   2309 C CG   . GLU A 1 390 ? 92.17900  130.38500 79.41200  1.000 47.11203  ? 390 GLU A CG   1 
ATOM   2310 C CD   . GLU A 1 390 ? 91.57600  131.77500 79.36300  1.000 54.21717  ? 390 GLU A CD   1 
ATOM   2311 O OE1  . GLU A 1 390 ? 92.24600  132.73100 79.80600  1.000 54.63284  ? 390 GLU A OE1  1 
ATOM   2312 O OE2  . GLU A 1 390 ? 90.43200  131.91200 78.88200  1.000 54.51398  ? 390 GLU A OE2  1 
ATOM   2313 N N    . LEU A 1 391 ? 93.91300  127.98600 81.42700  1.000 47.72853  ? 391 LEU A N    1 
ATOM   2314 C CA   . LEU A 1 391 ? 93.32700  127.00100 82.33300  1.000 44.32971  ? 391 LEU A CA   1 
ATOM   2315 C C    . LEU A 1 391 ? 93.80100  127.20800 83.76800  1.000 41.66082  ? 391 LEU A C    1 
ATOM   2316 O O    . LEU A 1 391 ? 93.00400  127.11800 84.71100  1.000 40.89114  ? 391 LEU A O    1 
ATOM   2317 C CB   . LEU A 1 391 ? 93.65000  125.58200 81.86600  1.000 43.40965  ? 391 LEU A CB   1 
ATOM   2318 C CG   . LEU A 1 391 ? 92.79700  125.02500 80.72600  1.000 42.87279  ? 391 LEU A CG   1 
ATOM   2319 C CD1  . LEU A 1 391 ? 93.21400  123.60200 80.39800  1.000 41.44342  ? 391 LEU A CD1  1 
ATOM   2320 C CD2  . LEU A 1 391 ? 91.32100  125.08800 81.08100  1.000 41.55002  ? 391 LEU A CD2  1 
ATOM   2321 N N    . GLY A 1 392 ? 95.09200  127.49300 83.95700  1.000 42.11269  ? 392 GLY A N    1 
ATOM   2322 C CA   . GLY A 1 392 ? 95.57500  127.78600 85.29900  1.000 43.81547  ? 392 GLY A CA   1 
ATOM   2323 C C    . GLY A 1 392 ? 94.88800  128.98800 85.92300  1.000 45.50303  ? 392 GLY A C    1 
ATOM   2324 O O    . GLY A 1 392 ? 94.45700  128.94700 87.08200  1.000 41.85449  ? 392 GLY A O    1 
ATOM   2325 N N    . GLU A 1 393 ? 94.76100  130.07300 85.15400  1.000 52.04652  ? 393 GLU A N    1 
ATOM   2326 C CA   . GLU A 1 393 ? 94.13800  131.28200 85.68100  1.000 47.26752  ? 393 GLU A CA   1 
ATOM   2327 C C    . GLU A 1 393 ? 92.67100  131.05100 86.02200  1.000 44.52117  ? 393 GLU A C    1 
ATOM   2328 O O    . GLU A 1 393 ? 92.17300  131.57100 87.02600  1.000 43.00858  ? 393 GLU A O    1 
ATOM   2329 C CB   . GLU A 1 393 ? 94.27700  132.42100 84.67000  1.000 47.81347  ? 393 GLU A CB   1 
ATOM   2330 C CG   . GLU A 1 393 ? 94.49000  133.79100 85.28500  1.000 47.77511  ? 393 GLU A CG   1 
ATOM   2331 C CD   . GLU A 1 393 ? 95.70500  133.84300 86.18700  1.000 54.86882  ? 393 GLU A CD   1 
ATOM   2332 O OE1  . GLU A 1 393 ? 96.83700  133.84600 85.66100  1.000 58.93651  ? 393 GLU A OE1  1 
ATOM   2333 O OE2  . GLU A 1 393 ? 95.53000  133.88800 87.42100  1.000 52.61338  ? 393 GLU A OE2  1 
ATOM   2334 N N    . LYS A 1 394 ? 91.96100  130.27200 85.20300  1.000 49.09692  ? 394 LYS A N    1 
ATOM   2335 C CA   . LYS A 1 394 ? 90.57000  129.96200 85.52100  1.000 47.21259  ? 394 LYS A CA   1 
ATOM   2336 C C    . LYS A 1 394 ? 90.45300  129.09700 86.77000  1.000 44.35021  ? 394 LYS A C    1 
ATOM   2337 O O    . LYS A 1 394 ? 89.56600  129.32000 87.60100  1.000 40.54323  ? 394 LYS A O    1 
ATOM   2338 C CB   . LYS A 1 394 ? 89.88800  129.28600 84.33400  1.000 46.34637  ? 394 LYS A CB   1 
ATOM   2339 C CG   . LYS A 1 394 ? 88.87300  130.17400 83.64100  1.000 45.23756  ? 394 LYS A CG   1 
ATOM   2340 C CD   . LYS A 1 394 ? 88.71200  129.81300 82.18000  1.000 47.82768  ? 394 LYS A CD   1 
ATOM   2341 C CE   . LYS A 1 394 ? 87.46200  130.45200 81.60400  1.000 49.82699  ? 394 LYS A CE   1 
ATOM   2342 N NZ   . LYS A 1 394 ? 87.68200  131.87900 81.24900  1.000 48.30474  ? 394 LYS A NZ   1 
ATOM   2343 N N    . VAL A 1 395 ? 91.32700  128.10000 86.92200  1.000 46.42265  ? 395 VAL A N    1 
ATOM   2344 C CA   . VAL A 1 395 ? 91.28600  127.27300 88.12600  1.000 38.13805  ? 395 VAL A CA   1 
ATOM   2345 C C    . VAL A 1 395 ? 91.52900  128.11500 89.37100  1.000 44.12551  ? 395 VAL A C    1 
ATOM   2346 O O    . VAL A 1 395 ? 90.85800  127.94000 90.39500  1.000 48.45941  ? 395 VAL A O    1 
ATOM   2347 C CB   . VAL A 1 395 ? 92.29600  126.11500 88.02800  1.000 43.35625  ? 395 VAL A CB   1 
ATOM   2348 C CG1  . VAL A 1 395 ? 92.52000  125.49900 89.40000  1.000 37.28573  ? 395 VAL A CG1  1 
ATOM   2349 C CG2  . VAL A 1 395 ? 91.80600  125.06400 87.05500  1.000 45.02965  ? 395 VAL A CG2  1 
ATOM   2350 N N    . LYS A 1 396 ? 92.49200  129.03900 89.31200  1.000 48.10416  ? 396 LYS A N    1 
ATOM   2351 C CA   . LYS A 1 396 ? 92.80800  129.83200 90.49900  1.000 44.90574  ? 396 LYS A CA   1 
ATOM   2352 C C    . LYS A 1 396 ? 91.63900  130.70400 90.94700  1.000 46.37066  ? 396 LYS A C    1 
ATOM   2353 O O    . LYS A 1 396 ? 91.35700  130.80200 92.14700  1.000 44.76752  ? 396 LYS A O    1 
ATOM   2354 C CB   . LYS A 1 396 ? 94.03400  130.70500 90.24300  1.000 46.04428  ? 396 LYS A CB   1 
ATOM   2355 C CG   . LYS A 1 396 ? 94.68600  131.21100 91.51700  1.000 47.33185  ? 396 LYS A CG   1 
ATOM   2356 C CD   . LYS A 1 396 ? 95.81400  132.17700 91.21900  1.000 46.30342  ? 396 LYS A CD   1 
ATOM   2357 C CE   . LYS A 1 396 ? 95.39700  133.18800 90.17000  1.000 47.47918  ? 396 LYS A CE   1 
ATOM   2358 N NZ   . LYS A 1 396 ? 94.56300  134.27400 90.75200  1.000 49.16006  ? 396 LYS A NZ   1 
ATOM   2359 N N    . LYS A 1 397 ? 90.94500  131.34500 90.01000  1.000 50.93155  ? 397 LYS A N    1 
ATOM   2360 C CA   . LYS A 1 397 ? 89.84800  132.24200 90.35900  1.000 48.98582  ? 397 LYS A CA   1 
ATOM   2361 C C    . LYS A 1 397 ? 88.49700  131.54900 90.50200  1.000 52.72249  ? 397 LYS A C    1 
ATOM   2362 O O    . LYS A 1 397 ? 87.50300  132.22500 90.78000  1.000 51.62848  ? 397 LYS A O    1 
ATOM   2363 C CB   . LYS A 1 397 ? 89.74800  133.37200 89.33400  1.000 49.44071  ? 397 LYS A CB   1 
ATOM   2364 C CG   . LYS A 1 397 ? 90.77800  134.47200 89.52200  1.000 52.77953  ? 397 LYS A CG   1 
ATOM   2365 C CD   . LYS A 1 397 ? 91.61800  134.67600 88.27400  1.000 56.52254  ? 397 LYS A CD   1 
ATOM   2366 C CE   . LYS A 1 397 ? 92.37600  135.99300 88.33500  1.000 53.59729  ? 397 LYS A CE   1 
ATOM   2367 N NZ   . LYS A 1 397 ? 92.89800  136.40000 87.00200  1.000 52.66514  ? 397 LYS A NZ   1 
ATOM   2368 N N    . MET A 1 398 ? 88.43500  130.23100 90.33900  1.000 60.87155  ? 398 MET A N    1 
ATOM   2369 C CA   . MET A 1 398 ? 87.19400  129.46800 90.46200  1.000 56.05541  ? 398 MET A CA   1 
ATOM   2370 C C    . MET A 1 398 ? 86.06200  130.01900 89.58800  1.000 56.42016  ? 398 MET A C    1 
ATOM   2371 O O    . MET A 1 398 ? 85.02700  130.47100 90.08000  1.000 56.10522  ? 398 MET A O    1 
ATOM   2372 C CB   . MET A 1 398 ? 86.75900  129.41200 91.93000  1.000 46.20648  ? 398 MET A CB   1 
ATOM   2373 C CG   . MET A 1 398 ? 87.54100  128.42300 92.77700  1.000 52.39070  ? 398 MET A CG   1 
ATOM   2374 S SD   . MET A 1 398 ? 87.56900  128.86500 94.52500  1.000 64.39621  ? 398 MET A SD   1 
ATOM   2375 C CE   . MET A 1 398 ? 86.60500  127.53700 95.23600  1.000 54.56742  ? 398 MET A CE   1 
ATOM   2376 N N    . GLU A 1 399 ? 86.26700  129.97300 88.26900  1.000 57.55920  ? 399 GLU A N    1 
ATOM   2377 C CA   . GLU A 1 399 ? 85.25100  130.41500 87.32000  1.000 55.06555  ? 399 GLU A CA   1 
ATOM   2378 C C    . GLU A 1 399 ? 85.04000  129.35200 86.25200  1.000 59.11599  ? 399 GLU A C    1 
ATOM   2379 O O    . GLU A 1 399 ? 85.98900  128.69900 85.81100  1.000 64.14750  ? 399 GLU A O    1 
ATOM   2380 C CB   . GLU A 1 399 ? 85.59100  131.73700 86.61700  1.000 56.73769  ? 399 GLU A CB   1 
ATOM   2381 C CG   . GLU A 1 399 ? 85.86100  132.92600 87.50800  1.000 60.89767  ? 399 GLU A CG   1 
ATOM   2382 C CD   . GLU A 1 399 ? 86.89900  133.85200 86.90800  1.000 65.15243  ? 399 GLU A CD   1 
ATOM   2383 O OE1  . GLU A 1 399 ? 88.06300  133.82400 87.34700  1.000 61.03584  ? 399 GLU A OE1  1 
ATOM   2384 O OE2  . GLU A 1 399 ? 86.54500  134.61400 85.98400  1.000 65.21998  ? 399 GLU A OE2  1 
ATOM   2385 N N    . LYS A 1 400 ? 83.78300  129.19100 85.84300  1.000 56.74906  ? 400 LYS A N    1 
ATOM   2386 C CA   . LYS A 1 400 ? 83.41700  128.25300 84.79100  1.000 54.11435  ? 400 LYS A CA   1 
ATOM   2387 C C    . LYS A 1 400 ? 84.02700  128.66400 83.45100  1.000 56.49522  ? 400 LYS A C    1 
ATOM   2388 O O    . LYS A 1 400 ? 84.38700  129.82200 83.22600  1.000 60.72023  ? 400 LYS A O    1 
ATOM   2389 C CB   . LYS A 1 400 ? 81.89700  128.16600 84.67100  1.000 54.52396  ? 400 LYS A CB   1 
ATOM   2390 C CG   . LYS A 1 400 ? 81.24900  127.24400 85.68800  1.000 54.08303  ? 400 LYS A CG   1 
ATOM   2391 C CD   . LYS A 1 400 ? 79.95100  126.66200 85.16200  1.000 58.27387  ? 400 LYS A CD   1 
ATOM   2392 C CE   . LYS A 1 400 ? 79.42000  125.58300 86.08800  1.000 56.48809  ? 400 LYS A CE   1 
ATOM   2393 N NZ   . LYS A 1 400 ? 79.56300  125.96400 87.51900  1.000 55.95329  ? 400 LYS A NZ   1 
ATOM   2394 N N    . LEU A 1 401 ? 84.14100  127.68700 82.55300  1.000 59.86133  ? 401 LEU A N    1 
ATOM   2395 C CA   . LEU A 1 401 ? 84.60700  127.95400 81.19700  1.000 59.34234  ? 401 LEU A CA   1 
ATOM   2396 C C    . LEU A 1 401 ? 83.52600  128.65100 80.37900  1.000 60.60935  ? 401 LEU A C    1 
ATOM   2397 O O    . LEU A 1 401 ? 82.34900  128.28300 80.43000  1.000 59.88940  ? 401 LEU A O    1 
ATOM   2398 C CB   . LEU A 1 401 ? 85.01800  126.65500 80.50400  1.000 59.98198  ? 401 LEU A CB   1 
ATOM   2399 C CG   . LEU A 1 401 ? 86.33300  125.99400 80.91500  1.000 57.27425  ? 401 LEU A CG   1 
ATOM   2400 C CD1  . LEU A 1 401 ? 86.74200  124.96000 79.88200  1.000 55.78995  ? 401 LEU A CD1  1 
ATOM   2401 C CD2  . LEU A 1 401 ? 87.42500  127.03200 81.09100  1.000 60.12981  ? 401 LEU A CD2  1 
ATOM   2402 N N    . GLY A 1 402 ? 83.93500  129.67000 79.62000  1.000 72.28202  ? 402 GLY A N    1 
ATOM   2403 C CA   . GLY A 1 402 ? 83.02500  130.38000 78.76800  1.000 72.38762  ? 402 GLY A CA   1 
ATOM   2404 C C    . GLY A 1 402 ? 82.62300  129.57100 77.54600  1.000 75.64875  ? 402 GLY A C    1 
ATOM   2405 O O    . GLY A 1 402 ? 83.00100  128.40300 77.38400  1.000 77.04081  ? 402 GLY A O    1 
ATOM   2406 N N    . PRO A 1 403 ? 81.83700  130.20000 76.66800  1.000 83.11193  ? 403 PRO A N    1 
ATOM   2407 C CA   . PRO A 1 403 ? 81.32600  129.47200 75.49200  1.000 82.90528  ? 403 PRO A CA   1 
ATOM   2408 C C    . PRO A 1 403 ? 82.37600  129.19700 74.42800  1.000 82.67105  ? 403 PRO A C    1 
ATOM   2409 O O    . PRO A 1 403 ? 82.38400  128.10600 73.84400  1.000 82.65240  ? 403 PRO A O    1 
ATOM   2410 C CB   . PRO A 1 403 ? 80.21800  130.39700 74.97400  1.000 81.44078  ? 403 PRO A CB   1 
ATOM   2411 C CG   . PRO A 1 403 ? 80.65000  131.76200 75.39200  1.000 81.91827  ? 403 PRO A CG   1 
ATOM   2412 C CD   . PRO A 1 403 ? 81.39400  131.60500 76.69400  1.000 81.42068  ? 403 PRO A CD   1 
ATOM   2413 N N    . VAL A 1 404 ? 83.25800  130.16000 74.15300  1.000 81.00895  ? 404 VAL A N    1 
ATOM   2414 C CA   . VAL A 1 404 ? 84.24300  129.99900 73.08900  1.000 80.71516  ? 404 VAL A CA   1 
ATOM   2415 C C    . VAL A 1 404 ? 85.12500  128.78100 73.33400  1.000 82.08054  ? 404 VAL A C    1 
ATOM   2416 O O    . VAL A 1 404 ? 85.59300  128.53300 74.45300  1.000 79.70582  ? 404 VAL A O    1 
ATOM   2417 C CB   . VAL A 1 404 ? 85.08800  131.27800 72.95500  1.000 80.67161  ? 404 VAL A CB   1 
ATOM   2418 C CG1  . VAL A 1 404 ? 86.21900  131.27900 73.97000  1.000 80.90622  ? 404 VAL A CG1  1 
ATOM   2419 C CG2  . VAL A 1 404 ? 85.63200  131.40800 71.54100  1.000 80.00261  ? 404 VAL A CG2  1 
ATOM   2420 N N    . ASP A 1 405 ? 85.34400  128.00600 72.27100  1.000 74.47829  ? 405 ASP A N    1 
ATOM   2421 C CA   . ASP A 1 405 ? 86.17600  126.80900 72.33500  1.000 74.84102  ? 405 ASP A CA   1 
ATOM   2422 C C    . ASP A 1 405 ? 87.65200  127.19100 72.40200  1.000 74.99035  ? 405 ASP A C    1 
ATOM   2423 O O    . ASP A 1 405 ? 88.17300  127.85200 71.49700  1.000 72.53529  ? 405 ASP A O    1 
ATOM   2424 C CB   . ASP A 1 405 ? 85.90600  125.92000 71.12500  1.000 73.71148  ? 405 ASP A CB   1 
ATOM   2425 C CG   . ASP A 1 405 ? 86.16800  124.45500 71.40900  1.000 75.68221  ? 405 ASP A CG   1 
ATOM   2426 O OD1  . ASP A 1 405 ? 86.69800  124.14400 72.49600  1.000 76.37947  ? 405 ASP A OD1  1 
ATOM   2427 O OD2  . ASP A 1 405 ? 85.84600  123.61300 70.54400  1.000 74.79225  ? 405 ASP A OD2  1 
ATOM   2428 N N    . LEU A 1 406 ? 88.32100  126.77600 73.48000  1.000 65.25836  ? 406 LEU A N    1 
ATOM   2429 C CA   . LEU A 1 406 ? 89.71700  127.13700 73.70800  1.000 61.32121  ? 406 LEU A CA   1 
ATOM   2430 C C    . LEU A 1 406 ? 90.69200  126.41900 72.77900  1.000 63.98668  ? 406 LEU A C    1 
ATOM   2431 O O    . LEU A 1 406 ? 91.83800  126.86100 72.65400  1.000 63.84405  ? 406 LEU A O    1 
ATOM   2432 C CB   . LEU A 1 406 ? 90.09900  126.84600 75.15900  1.000 64.59140  ? 406 LEU A CB   1 
ATOM   2433 C CG   . LEU A 1 406 ? 89.23000  127.45500 76.26000  1.000 64.56916  ? 406 LEU A CG   1 
ATOM   2434 C CD1  . LEU A 1 406 ? 89.70700  126.98400 77.62300  1.000 60.66636  ? 406 LEU A CD1  1 
ATOM   2435 C CD2  . LEU A 1 406 ? 89.24000  128.97200 76.18000  1.000 65.03637  ? 406 LEU A CD2  1 
ATOM   2436 N N    . LEU A 1 407 ? 90.27700  125.32900 72.13400  1.000 60.37026  ? 407 LEU A N    1 
ATOM   2437 C CA   . LEU A 1 407 ? 91.18400  124.47900 71.36900  1.000 56.70934  ? 407 LEU A CA   1 
ATOM   2438 C C    . LEU A 1 407 ? 91.22500  124.78900 69.87600  1.000 57.72183  ? 407 LEU A C    1 
ATOM   2439 O O    . LEU A 1 407 ? 92.00200  124.16000 69.15400  1.000 60.81216  ? 407 LEU A O    1 
ATOM   2440 C CB   . LEU A 1 407 ? 90.79700  123.00800 71.56500  1.000 53.90312  ? 407 LEU A CB   1 
ATOM   2441 C CG   . LEU A 1 407 ? 90.88600  122.41500 72.97300  1.000 54.94654  ? 407 LEU A CG   1 
ATOM   2442 C CD1  . LEU A 1 407 ? 90.68900  120.91000 72.93500  1.000 52.86044  ? 407 LEU A CD1  1 
ATOM   2443 C CD2  . LEU A 1 407 ? 92.21000  122.75300 73.62200  1.000 54.61771  ? 407 LEU A CD2  1 
ATOM   2444 N N    . PHE A 1 408 ? 90.41100  125.72900 69.39200  1.000 59.74445  ? 408 PHE A N    1 
ATOM   2445 C CA   . PHE A 1 408 ? 90.37900  126.03100 67.96100  1.000 61.12313  ? 408 PHE A CA   1 
ATOM   2446 C C    . PHE A 1 408 ? 91.75600  126.42100 67.42300  1.000 62.73302  ? 408 PHE A C    1 
ATOM   2447 O O    . PHE A 1 408 ? 92.24500  125.83900 66.44400  1.000 63.55006  ? 408 PHE A O    1 
ATOM   2448 C CB   . PHE A 1 408 ? 89.35500  127.14000 67.70600  1.000 60.61010  ? 408 PHE A CB   1 
ATOM   2449 C CG   . PHE A 1 408 ? 89.27100  127.58400 66.27400  1.000 61.44453  ? 408 PHE A CG   1 
ATOM   2450 C CD1  . PHE A 1 408 ? 90.07700  128.60500 65.80100  1.000 61.28174  ? 408 PHE A CD1  1 
ATOM   2451 C CD2  . PHE A 1 408 ? 88.38100  126.98300 65.40200  1.000 59.72364  ? 408 PHE A CD2  1 
ATOM   2452 C CE1  . PHE A 1 408 ? 89.99800  129.01500 64.48500  1.000 61.72785  ? 408 PHE A CE1  1 
ATOM   2453 C CE2  . PHE A 1 408 ? 88.30000  127.38700 64.08500  1.000 60.64463  ? 408 PHE A CE2  1 
ATOM   2454 C CZ   . PHE A 1 408 ? 89.10900  128.40500 63.62700  1.000 63.16427  ? 408 PHE A CZ   1 
ATOM   2455 N N    . GLU A 1 409 ? 92.40600  127.39500 68.06600  1.000 60.19578  ? 409 GLU A N    1 
ATOM   2456 C CA   . GLU A 1 409 ? 93.69100  127.89100 67.57800  1.000 62.05376  ? 409 GLU A CA   1 
ATOM   2457 C C    . GLU A 1 409 ? 94.76300  126.80700 67.56400  1.000 63.65315  ? 409 GLU A C    1 
ATOM   2458 O O    . GLU A 1 409 ? 95.54600  126.71100 66.61000  1.000 65.92521  ? 409 GLU A O    1 
ATOM   2459 C CB   . GLU A 1 409 ? 94.14300  129.08100 68.42300  1.000 60.97607  ? 409 GLU A CB   1 
ATOM   2460 C CG   . GLU A 1 409 ? 93.87000  130.43000 67.78200  1.000 62.67287  ? 409 GLU A CG   1 
ATOM   2461 C CD   . GLU A 1 409 ? 92.43100  130.58500 67.33100  1.000 67.51307  ? 409 GLU A CD   1 
ATOM   2462 O OE1  . GLU A 1 409 ? 91.52400  130.49600 68.18500  1.000 68.96603  ? 409 GLU A OE1  1 
ATOM   2463 O OE2  . GLU A 1 409 ? 92.20600  130.79300 66.12100  1.000 65.30908  ? 409 GLU A OE2  1 
ATOM   2464 N N    . VAL A 1 410 ? 94.83100  125.99200 68.61700  1.000 55.62737  ? 410 VAL A N    1 
ATOM   2465 C CA   . VAL A 1 410 ? 95.87500  124.97500 68.69300  1.000 52.73412  ? 410 VAL A CA   1 
ATOM   2466 C C    . VAL A 1 410 ? 95.66600  123.91400 67.61700  1.000 51.29271  ? 410 VAL A C    1 
ATOM   2467 O O    . VAL A 1 410 ? 96.61100  123.51300 66.92600  1.000 53.12279  ? 410 VAL A O    1 
ATOM   2468 C CB   . VAL A 1 410 ? 95.93100  124.36700 70.10800  1.000 50.60687  ? 410 VAL A CB   1 
ATOM   2469 C CG1  . VAL A 1 410 ? 94.80200  123.37300 70.33000  1.000 49.64007  ? 410 VAL A CG1  1 
ATOM   2470 C CG2  . VAL A 1 410 ? 97.28500  123.72000 70.35800  1.000 51.15905  ? 410 VAL A CG2  1 
ATOM   2471 N N    . HIS A 1 411 ? 94.43000  123.43500 67.46600  1.000 50.48281  ? 411 HIS A N    1 
ATOM   2472 C CA   . HIS A 1 411 ? 94.12400  122.49200 66.39500  1.000 53.85979  ? 411 HIS A CA   1 
ATOM   2473 C C    . HIS A 1 411 ? 94.48400  123.05900 65.02600  1.000 56.15963  ? 411 HIS A C    1 
ATOM   2474 O O    . HIS A 1 411 ? 94.99400  122.33500 64.15900  1.000 59.07805  ? 411 HIS A O    1 
ATOM   2475 C CB   . HIS A 1 411 ? 92.64700  122.10500 66.45100  1.000 50.88880  ? 411 HIS A CB   1 
ATOM   2476 C CG   . HIS A 1 411 ? 92.28000  121.30200 67.66000  1.000 53.65788  ? 411 HIS A CG   1 
ATOM   2477 N ND1  . HIS A 1 411 ? 90.97800  120.97100 67.96700  1.000 56.11245  ? 411 HIS A ND1  1 
ATOM   2478 C CD2  . HIS A 1 411 ? 93.04600  120.76100 68.63700  1.000 53.57468  ? 411 HIS A CD2  1 
ATOM   2479 C CE1  . HIS A 1 411 ? 90.95800  120.26200 69.08200  1.000 55.10011  ? 411 HIS A CE1  1 
ATOM   2480 N NE2  . HIS A 1 411 ? 92.19900  120.12000 69.50800  1.000 53.03751  ? 411 HIS A NE2  1 
ATOM   2481 N N    . LEU A 1 412 ? 94.24900  124.35700 64.81400  1.000 56.39201  ? 412 LEU A N    1 
ATOM   2482 C CA   . LEU A 1 412 ? 94.55900  124.93200 63.50800  1.000 60.32627  ? 412 LEU A CA   1 
ATOM   2483 C C    . LEU A 1 412 ? 96.06500  125.02200 63.28100  1.000 62.59800  ? 412 LEU A C    1 
ATOM   2484 O O    . LEU A 1 412 ? 96.55700  124.70200 62.18800  1.000 65.41918  ? 412 LEU A O    1 
ATOM   2485 C CB   . LEU A 1 412 ? 93.91000  126.31000 63.38100  1.000 62.01787  ? 412 LEU A CB   1 
ATOM   2486 C CG   . LEU A 1 412 ? 94.34300  127.17300 62.19600  1.000 62.18033  ? 412 LEU A CG   1 
ATOM   2487 C CD1  . LEU A 1 412 ? 93.72600  126.65300 60.90800  1.000 62.00776  ? 412 LEU A CD1  1 
ATOM   2488 C CD2  . LEU A 1 412 ? 93.96500  128.62600 62.42700  1.000 59.73452  ? 412 LEU A CD2  1 
ATOM   2489 N N    . ALA A 1 413 ? 96.81800  125.42500 64.30800  1.000 55.57521  ? 413 ALA A N    1 
ATOM   2490 C CA   . ALA A 1 413 ? 98.27200  125.43900 64.17500  1.000 55.34979  ? 413 ALA A CA   1 
ATOM   2491 C C    . ALA A 1 413 ? 98.82400  124.03700 63.95700  1.000 59.69054  ? 413 ALA A C    1 
ATOM   2492 O O    . ALA A 1 413 ? 99.82400  123.86300 63.24900  1.000 59.46678  ? 413 ALA A O    1 
ATOM   2493 C CB   . ALA A 1 413 ? 98.90800  126.07800 65.40800  1.000 53.60832  ? 413 ALA A CB   1 
ATOM   2494 N N    . ALA A 1 414 ? 98.14200  123.01800 64.48100  1.000 59.61222  ? 414 ALA A N    1 
ATOM   2495 C CA   . ALA A 1 414 ? 98.64300  121.65800 64.32200  1.000 52.77786  ? 414 ALA A CA   1 
ATOM   2496 C C    . ALA A 1 414 ? 98.35100  121.13000 62.92500  1.000 54.68686  ? 414 ALA A C    1 
ATOM   2497 O O    . ALA A 1 414 ? 99.17900  120.42300 62.33700  1.000 57.15224  ? 414 ALA A O    1 
ATOM   2498 C CB   . ALA A 1 414 ? 98.03400  120.74200 65.38300  1.000 50.40845  ? 414 ALA A CB   1 
ATOM   2499 N N    . GLU A 1 415 ? 97.18700  121.47400 62.37100  1.000 61.11781  ? 415 GLU A N    1 
ATOM   2500 C CA   . GLU A 1 415 ? 96.91700  121.11800 60.98200  1.000 61.23931  ? 415 GLU A CA   1 
ATOM   2501 C C    . GLU A 1 415 ? 97.88200  121.82400 60.03700  1.000 64.38264  ? 415 GLU A C    1 
ATOM   2502 O O    . GLU A 1 415 ? 98.32400  121.24400 59.03500  1.000 66.32025  ? 415 GLU A O    1 
ATOM   2503 C CB   . GLU A 1 415 ? 95.47100  121.45500 60.62400  1.000 61.77887  ? 415 GLU A CB   1 
ATOM   2504 C CG   . GLU A 1 415 ? 94.45100  120.47700 61.17800  1.000 64.74965  ? 415 GLU A CG   1 
ATOM   2505 C CD   . GLU A 1 415 ? 93.03900  121.01800 61.12000  1.000 69.53659  ? 415 GLU A CD   1 
ATOM   2506 O OE1  . GLU A 1 415 ? 92.63700  121.52500 60.05100  1.000 69.50176  ? 415 GLU A OE1  1 
ATOM   2507 O OE2  . GLU A 1 415 ? 92.33000  120.93900 62.14500  1.000 69.48118  ? 415 GLU A OE2  1 
ATOM   2508 N N    . GLU A 1 416 ? 98.25300  123.06800 60.35600  1.000 62.34746  ? 416 GLU A N    1 
ATOM   2509 C CA   . GLU A 1 416 ? 99.23100  123.76000 59.52000  1.000 62.69056  ? 416 GLU A CA   1 
ATOM   2510 C C    . GLU A 1 416 ? 100.60400 123.10100 59.61000  1.000 65.49180  ? 416 GLU A C    1 
ATOM   2511 O O    . GLU A 1 416 ? 101.29800 122.95400 58.59500  1.000 66.90460  ? 416 GLU A O    1 
ATOM   2512 C CB   . GLU A 1 416 ? 99.31000  125.23700 59.91000  1.000 62.40200  ? 416 GLU A CB   1 
ATOM   2513 C CG   . GLU A 1 416 ? 100.49100 125.59700 60.79500  1.000 68.50559  ? 416 GLU A CG   1 
ATOM   2514 C CD   . GLU A 1 416 ? 100.43600 127.03000 61.29000  1.000 70.24967  ? 416 GLU A CD   1 
ATOM   2515 O OE1  . GLU A 1 416 ? 101.28200 127.40400 62.12900  1.000 67.55192  ? 416 GLU A OE1  1 
ATOM   2516 O OE2  . GLU A 1 416 ? 99.54600  127.78100 60.84000  1.000 69.28238  ? 416 GLU A OE2  1 
ATOM   2517 N N    . LEU A 1 417 ? 101.01700 122.70300 60.81700  1.000 60.39893  ? 417 LEU A N    1 
ATOM   2518 C CA   . LEU A 1 417 ? 102.23200 121.90600 60.96400  1.000 57.38702  ? 417 LEU A CA   1 
ATOM   2519 C C    . LEU A 1 417 ? 102.18900 120.65400 60.09500  1.000 57.15840  ? 417 LEU A C    1 
ATOM   2520 O O    . LEU A 1 417 ? 103.14900 120.34400 59.38200  1.000 54.16835  ? 417 LEU A O    1 
ATOM   2521 C CB   . LEU A 1 417 ? 102.44300 121.53100 62.43200  1.000 57.65063  ? 417 LEU A CB   1 
ATOM   2522 C CG   . LEU A 1 417 ? 103.78500 120.87100 62.75600  1.000 55.53256  ? 417 LEU A CG   1 
ATOM   2523 C CD1  . LEU A 1 417 ? 104.94700 121.72600 62.27400  1.000 55.73911  ? 417 LEU A CD1  1 
ATOM   2524 C CD2  . LEU A 1 417 ? 103.90200 120.59300 64.24600  1.000 54.75803  ? 417 LEU A CD2  1 
ATOM   2525 N N    . GLN A 1 418 ? 101.10700 119.88100 60.20600  1.000 68.48772  ? 418 GLN A N    1 
ATOM   2526 C CA   . GLN A 1 418 ? 100.95500 118.67500 59.39500  1.000 68.37899  ? 418 GLN A CA   1 
ATOM   2527 C C    . GLN A 1 418 ? 101.12300 118.96500 57.90600  1.000 68.99672  ? 418 GLN A C    1 
ATOM   2528 O O    . GLN A 1 418 ? 101.82700 118.23900 57.19500  1.000 70.28699  ? 418 GLN A O    1 
ATOM   2529 C CB   . GLN A 1 418 ? 99.59400  118.03500 59.66500  1.000 66.56874  ? 418 GLN A CB   1 
ATOM   2530 C CG   . GLN A 1 418 ? 99.51100  116.56700 59.28500  1.000 68.45661  ? 418 GLN A CG   1 
ATOM   2531 C CD   . GLN A 1 418 ? 100.69700 115.76700 59.77800  1.000 72.72445  ? 418 GLN A CD   1 
ATOM   2532 O OE1  . GLN A 1 418 ? 100.80800 115.47000 60.96600  1.000 75.49231  ? 418 GLN A OE1  1 
ATOM   2533 N NE2  . GLN A 1 418 ? 101.59100 115.41000 58.86300  1.000 70.39829  ? 418 GLN A NE2  1 
ATOM   2534 N N    . HIS A 1 419 ? 100.47700 120.02400 57.41400  1.000 73.39636  ? 419 HIS A N    1 
ATOM   2535 C CA   . HIS A 1 419 ? 100.60200 120.35600 55.99600  1.000 74.31711  ? 419 HIS A CA   1 
ATOM   2536 C C    . HIS A 1 419 ? 102.03800 120.71500 55.62300  1.000 73.96663  ? 419 HIS A C    1 
ATOM   2537 O O    . HIS A 1 419 ? 102.54600 120.28200 54.57800  1.000 71.90336  ? 419 HIS A O    1 
ATOM   2538 C CB   . HIS A 1 419 ? 99.65500  121.50300 55.64100  1.000 74.43182  ? 419 HIS A CB   1 
ATOM   2539 C CG   . HIS A 1 419 ? 98.22000  121.09200 55.53900  1.000 74.98656  ? 419 HIS A CG   1 
ATOM   2540 N ND1  . HIS A 1 419 ? 97.82300  119.91800 54.93700  1.000 75.62955  ? 419 HIS A ND1  1 
ATOM   2541 C CD2  . HIS A 1 419 ? 97.08600  121.70000 55.96200  1.000 73.87711  ? 419 HIS A CD2  1 
ATOM   2542 C CE1  . HIS A 1 419 ? 96.50700  119.81900 54.99400  1.000 76.18187  ? 419 HIS A CE1  1 
ATOM   2543 N NE2  . HIS A 1 419 ? 96.03600  120.88800 55.61100  1.000 74.59677  ? 419 HIS A NE2  1 
ATOM   2544 N N    . LYS A 1 420 ? 102.71600 121.49100 56.47300  1.000 72.03798  ? 420 LYS A N    1 
ATOM   2545 C CA   . LYS A 1 420 ? 104.10400 121.84000 56.18700  1.000 70.85579  ? 420 LYS A CA   1 
ATOM   2546 C C    . LYS A 1 420 ? 104.99300 120.60400 56.15800  1.000 72.37595  ? 420 LYS A C    1 
ATOM   2547 O O    . LYS A 1 420 ? 105.89300 120.49700 55.31700  1.000 73.34966  ? 420 LYS A O    1 
ATOM   2548 C CB   . LYS A 1 420 ? 104.61900 122.84800 57.21400  1.000 73.17557  ? 420 LYS A CB   1 
ATOM   2549 C CG   . LYS A 1 420 ? 105.97800 123.43200 56.87100  1.000 73.34878  ? 420 LYS A CG   1 
ATOM   2550 C CD   . LYS A 1 420 ? 105.92600 124.22600 55.58000  1.000 73.49806  ? 420 LYS A CD   1 
ATOM   2551 C CE   . LYS A 1 420 ? 107.20500 125.01500 55.36600  1.000 73.71130  ? 420 LYS A CE   1 
ATOM   2552 N NZ   . LYS A 1 420 ? 107.45900 125.27000 53.92300  1.000 72.05456  ? 420 LYS A NZ   1 
ATOM   2553 N N    . ILE A 1 421 ? 104.75700 119.65700 57.06800  1.000 72.67010  ? 421 ILE A N    1 
ATOM   2554 C CA   . ILE A 1 421 ? 105.53200 118.41800 57.05200  1.000 72.44207  ? 421 ILE A CA   1 
ATOM   2555 C C    . ILE A 1 421 ? 105.24600 117.63700 55.77900  1.000 70.50358  ? 421 ILE A C    1 
ATOM   2556 O O    . ILE A 1 421 ? 106.14500 117.01900 55.19500  1.000 71.17769  ? 421 ILE A O    1 
ATOM   2557 C CB   . ILE A 1 421 ? 105.24300 117.57500 58.30900  1.000 71.21198  ? 421 ILE A CB   1 
ATOM   2558 C CG1  . ILE A 1 421 ? 105.60500 118.35000 59.57500  1.000 72.03327  ? 421 ILE A CG1  1 
ATOM   2559 C CG2  . ILE A 1 421 ? 106.00200 116.26000 58.25500  1.000 69.31623  ? 421 ILE A CG2  1 
ATOM   2560 C CD1  . ILE A 1 421 ? 104.72000 118.02500 60.75800  1.000 72.11681  ? 421 ILE A CD1  1 
ATOM   2561 N N    . ASP A 1 422 ? 103.99200 117.65300 55.32800  1.000 73.75495  ? 422 ASP A N    1 
ATOM   2562 C CA   . ASP A 1 422 ? 103.63100 116.90400 54.13000  1.000 73.55938  ? 422 ASP A CA   1 
ATOM   2563 C C    . ASP A 1 422 ? 104.32400 117.47000 52.89600  1.000 73.78404  ? 422 ASP A C    1 
ATOM   2564 O O    . ASP A 1 422 ? 104.76800 116.71300 52.02600  1.000 70.63016  ? 422 ASP A O    1 
ATOM   2565 C CB   . ASP A 1 422 ? 102.11500 116.91300 53.94100  1.000 73.45252  ? 422 ASP A CB   1 
ATOM   2566 C CG   . ASP A 1 422 ? 101.45300 115.67000 54.49600  1.000 75.95494  ? 422 ASP A CG   1 
ATOM   2567 O OD1  . ASP A 1 422 ? 102.07300 114.99400 55.34300  1.000 76.51178  ? 422 ASP A OD1  1 
ATOM   2568 O OD2  . ASP A 1 422 ? 100.31200 115.37000 54.08600  1.000 74.98461  ? 422 ASP A OD2  1 
ATOM   2569 N N    . LYS A 1 423 ? 104.42000 118.79900 52.79900  1.000 80.20321  ? 423 LYS A N    1 
ATOM   2570 C CA   . LYS A 1 423 ? 105.02900 119.39800 51.61300  1.000 78.82780  ? 423 LYS A CA   1 
ATOM   2571 C C    . LYS A 1 423 ? 106.53100 119.13800 51.52300  1.000 81.13531  ? 423 LYS A C    1 
ATOM   2572 O O    . LYS A 1 423 ? 107.08500 119.12900 50.41800  1.000 82.28138  ? 423 LYS A O    1 
ATOM   2573 C CB   . LYS A 1 423 ? 104.76000 120.90300 51.58400  1.000 80.19688  ? 423 LYS A CB   1 
ATOM   2574 C CG   . LYS A 1 423 ? 103.34400 121.27500 51.18500  1.000 81.45700  ? 423 LYS A CG   1 
ATOM   2575 C CD   . LYS A 1 423 ? 103.09300 122.76000 51.38200  1.000 82.12465  ? 423 LYS A CD   1 
ATOM   2576 C CE   . LYS A 1 423 ? 104.37700 123.55900 51.23700  1.000 82.19804  ? 423 LYS A CE   1 
ATOM   2577 N NZ   . LYS A 1 423 ? 104.29200 124.87200 51.93400  1.000 80.88320  ? 423 LYS A NZ   1 
ATOM   2578 N N    . LYS A 1 424 ? 107.20900 118.92500 52.65300  1.000 80.54698  ? 424 LYS A N    1 
ATOM   2579 C CA   . LYS A 1 424 ? 108.66700 118.84200 52.67500  1.000 79.11517  ? 424 LYS A CA   1 
ATOM   2580 C C    . LYS A 1 424 ? 109.18000 117.48300 53.14300  1.000 80.20899  ? 424 LYS A C    1 
ATOM   2581 O O    . LYS A 1 424 ? 110.33100 117.37800 53.57700  1.000 80.21151  ? 424 LYS A O    1 
ATOM   2582 C CB   . LYS A 1 424 ? 109.25400 119.95000 53.55200  1.000 78.73327  ? 424 LYS A CB   1 
ATOM   2583 C CG   . LYS A 1 424 ? 108.75700 121.34500 53.21900  1.000 79.36053  ? 424 LYS A CG   1 
ATOM   2584 C CD   . LYS A 1 424 ? 109.75600 122.08800 52.34800  1.000 79.50753  ? 424 LYS A CD   1 
ATOM   2585 C CE   . LYS A 1 424 ? 109.09600 122.65900 51.10500  1.000 80.02390  ? 424 LYS A CE   1 
ATOM   2586 N NZ   . LYS A 1 424 ? 110.09900 123.20700 50.15100  1.000 80.86876  ? 424 LYS A NZ   1 
ATOM   2587 N N    . SER A 1 425 ? 108.35400 116.43800 53.06800  1.000 81.36258  ? 425 SER A N    1 
ATOM   2588 C CA   . SER A 1 425 ? 108.77200 115.11700 53.52400  1.000 79.72618  ? 425 SER A CA   1 
ATOM   2589 C C    . SER A 1 425 ? 109.96800 114.56200 52.75900  1.000 80.22820  ? 425 SER A C    1 
ATOM   2590 O O    . SER A 1 425 ? 110.52800 113.54400 53.18200  1.000 79.15527  ? 425 SER A O    1 
ATOM   2591 C CB   . SER A 1 425 ? 107.60300 114.13800 53.41900  1.000 79.33357  ? 425 SER A CB   1 
ATOM   2592 O OG   . SER A 1 425 ? 107.21100 113.96100 52.06900  1.000 82.67629  ? 425 SER A OG   1 
ATOM   2593 N N    . TYR A 1 426 ? 110.37900 115.19200 51.65700  1.000 80.39342  ? 426 TYR A N    1 
ATOM   2594 C CA   . TYR A 1 426 ? 111.55500 114.73000 50.92700  1.000 78.68144  ? 426 TYR A CA   1 
ATOM   2595 C C    . TYR A 1 426 ? 112.86300 114.99700 51.66300  1.000 77.41959  ? 426 TYR A C    1 
ATOM   2596 O O    . TYR A 1 426 ? 113.91100 114.52600 51.20900  1.000 77.00402  ? 426 TYR A O    1 
ATOM   2597 C CB   . TYR A 1 426 ? 111.56300 115.35300 49.52000  1.000 79.02081  ? 426 TYR A CB   1 
ATOM   2598 C CG   . TYR A 1 426 ? 111.96100 116.81700 49.41900  1.000 79.74729  ? 426 TYR A CG   1 
ATOM   2599 C CD1  . TYR A 1 426 ? 113.22500 117.25700 49.79400  1.000 77.31850  ? 426 TYR A CD1  1 
ATOM   2600 C CD2  . TYR A 1 426 ? 111.05900 117.76000 48.94500  1.000 78.63522  ? 426 TYR A CD2  1 
ATOM   2601 C CE1  . TYR A 1 426 ? 113.57500 118.58900 49.69800  1.000 77.70110  ? 426 TYR A CE1  1 
ATOM   2602 C CE2  . TYR A 1 426 ? 111.40200 119.09200 48.84700  1.000 79.26254  ? 426 TYR A CE2  1 
ATOM   2603 C CZ   . TYR A 1 426 ? 112.66000 119.50200 49.22600  1.000 79.86867  ? 426 TYR A CZ   1 
ATOM   2604 O OH   . TYR A 1 426 ? 113.00700 120.82900 49.12800  1.000 79.27611  ? 426 TYR A OH   1 
ATOM   2605 N N    . LEU A 1 427 ? 112.83400 115.72600 52.77700  1.000 75.93274  ? 427 LEU A N    1 
ATOM   2606 C CA   . LEU A 1 427 ? 114.02400 115.94100 53.58900  1.000 75.34706  ? 427 LEU A CA   1 
ATOM   2607 C C    . LEU A 1 427 ? 114.15400 114.94600 54.73200  1.000 76.36206  ? 427 LEU A C    1 
ATOM   2608 O O    . LEU A 1 427 ? 115.19500 114.92500 55.39900  1.000 75.39230  ? 427 LEU A O    1 
ATOM   2609 C CB   . LEU A 1 427 ? 114.03200 117.36300 54.16100  1.000 77.27605  ? 427 LEU A CB   1 
ATOM   2610 C CG   . LEU A 1 427 ? 114.11600 118.52200 53.17000  1.000 77.14616  ? 427 LEU A CG   1 
ATOM   2611 C CD1  . LEU A 1 427 ? 114.11100 119.84600 53.91200  1.000 76.53271  ? 427 LEU A CD1  1 
ATOM   2612 C CD2  . LEU A 1 427 ? 115.37100 118.39200 52.32700  1.000 77.36670  ? 427 LEU A CD2  1 
ATOM   2613 N N    . LEU A 1 428 ? 113.13200 114.12900 54.97600  1.000 78.06488  ? 428 LEU A N    1 
ATOM   2614 C CA   . LEU A 1 428 ? 113.15800 113.18200 56.08300  1.000 75.83752  ? 428 LEU A CA   1 
ATOM   2615 C C    . LEU A 1 428 ? 113.75400 111.83900 55.69200  1.000 74.64027  ? 428 LEU A C    1 
ATOM   2616 O O    . LEU A 1 428 ? 114.36200 111.17000 56.53500  1.000 75.50000  ? 428 LEU A O    1 
ATOM   2617 C CB   . LEU A 1 428 ? 111.74400 112.98000 56.63000  1.000 77.05888  ? 428 LEU A CB   1 
ATOM   2618 C CG   . LEU A 1 428 ? 111.13800 114.21500 57.29700  1.000 75.73762  ? 428 LEU A CG   1 
ATOM   2619 C CD1  . LEU A 1 428 ? 109.73700 113.92300 57.81000  1.000 73.95935  ? 428 LEU A CD1  1 
ATOM   2620 C CD2  . LEU A 1 428 ? 112.03900 114.72000 58.41300  1.000 75.48694  ? 428 LEU A CD2  1 
ATOM   2621 N N    . VAL A 1 429 ? 113.59500 111.43000 54.43500  1.000 83.94913  ? 429 VAL A N    1 
ATOM   2622 C CA   . VAL A 1 429 ? 114.06700 110.13100 53.97200  1.000 84.77580  ? 429 VAL A CA   1 
ATOM   2623 C C    . VAL A 1 429 ? 114.93600 110.33400 52.74000  1.000 84.88031  ? 429 VAL A C    1 
ATOM   2624 O O    . VAL A 1 429 ? 115.24900 111.47000 52.36800  1.000 83.32498  ? 429 VAL A O    1 
ATOM   2625 C CB   . VAL A 1 429 ? 112.89200 109.18300 53.66800  1.000 84.69306  ? 429 VAL A CB   1 
ATOM   2626 C CG1  . VAL A 1 429 ? 112.00600 109.02100 54.89300  1.000 83.97861  ? 429 VAL A CG1  1 
ATOM   2627 C CG2  . VAL A 1 429 ? 112.08900 109.69800 52.48500  1.000 84.44193  ? 429 VAL A CG2  1 
ATOM   2628 N N    . ASN A 1 430 ? 115.33500 109.23600 52.10200  1.000 95.84707  ? 430 ASN A N    1 
ATOM   2629 C CA   . ASN A 1 430 ? 116.16800 109.28500 50.90300  1.000 95.09445  ? 430 ASN A CA   1 
ATOM   2630 C C    . ASN A 1 430 ? 115.59300 108.30100 49.89500  1.000 95.95760  ? 430 ASN A C    1 
ATOM   2631 O O    . ASN A 1 430 ? 115.73700 107.08600 50.05900  1.000 96.04115  ? 430 ASN A O    1 
ATOM   2632 C CB   . ASN A 1 430 ? 117.62700 108.95800 51.22100  1.000 95.23893  ? 430 ASN A CB   1 
ATOM   2633 C CG   . ASN A 1 430 ? 117.76700 107.80900 52.19900  1.000 97.41323  ? 430 ASN A CG   1 
ATOM   2634 O OD1  . ASN A 1 430 ? 117.82000 108.01300 53.41100  1.000 96.45726  ? 430 ASN A OD1  1 
ATOM   2635 N ND2  . ASN A 1 430 ? 117.82800 106.59000 51.67500  1.000 97.28193  ? 430 ASN A ND2  1 
ATOM   2636 N N    . SER A 1 431 ? 114.94300 108.82800 48.85600  1.000 100.90506 ? 431 SER A N    1 
ATOM   2637 C CA   . SER A 1 431 ? 114.26800 107.98000 47.88000  1.000 101.35893 ? 431 SER A CA   1 
ATOM   2638 C C    . SER A 1 431 ? 115.24300 107.24500 46.97100  1.000 101.14330 ? 431 SER A C    1 
ATOM   2639 O O    . SER A 1 431 ? 114.84400 106.28100 46.31000  1.000 101.16258 ? 431 SER A O    1 
ATOM   2640 C CB   . SER A 1 431 ? 113.30500 108.81700 47.03800  1.000 101.18688 ? 431 SER A CB   1 
ATOM   2641 O OG   . SER A 1 431 ? 113.17300 110.12400 47.56900  1.000 100.70701 ? 431 SER A OG   1 
ATOM   2642 N N    . GLU A 1 432 ? 116.50400 107.67900 46.91900  1.000 104.14616 ? 432 GLU A N    1 
ATOM   2643 C CA   . GLU A 1 432 ? 117.47100 107.03000 46.03900  1.000 104.12416 ? 432 GLU A CA   1 
ATOM   2644 C C    . GLU A 1 432 ? 117.58700 105.54200 46.34500  1.000 104.17474 ? 432 GLU A C    1 
ATOM   2645 O O    . GLU A 1 432 ? 117.75800 104.72500 45.43200  1.000 104.25172 ? 432 GLU A O    1 
ATOM   2646 C CB   . GLU A 1 432 ? 118.83300 107.71200 46.16300  1.000 103.76841 ? 432 GLU A CB   1 
ATOM   2647 C CG   . GLU A 1 432 ? 119.21500 108.08300 47.58600  1.000 103.66660 ? 432 GLU A CG   1 
ATOM   2648 C CD   . GLU A 1 432 ? 118.77600 109.48500 47.95800  1.000 104.76634 ? 432 GLU A CD   1 
ATOM   2649 O OE1  . GLU A 1 432 ? 117.70500 109.91900 47.48300  1.000 104.48537 ? 432 GLU A OE1  1 
ATOM   2650 O OE2  . GLU A 1 432 ? 119.49900 110.15200 48.72700  1.000 105.09026 ? 432 GLU A OE2  1 
ATOM   2651 N N    . CYS A 1 433 ? 117.49500 105.16800 47.62100  1.000 104.19227 ? 433 CYS A N    1 
ATOM   2652 C CA   . CYS A 1 433 ? 117.65200 103.78300 48.04000  1.000 103.71684 ? 433 CYS A CA   1 
ATOM   2653 C C    . CYS A 1 433 ? 116.32900 103.02700 48.09200  1.000 104.56753 ? 433 CYS A C    1 
ATOM   2654 O O    . CYS A 1 433 ? 116.25200 101.97500 48.73800  1.000 104.14331 ? 433 CYS A O    1 
ATOM   2655 C CB   . CYS A 1 433 ? 118.34300 103.72400 49.40400  1.000 103.51327 ? 433 CYS A CB   1 
ATOM   2656 S SG   . CYS A 1 433 ? 119.13300 102.14100 49.77700  1.000 106.31758 ? 433 CYS A SG   1 
ATOM   2657 N N    . TRP A 1 434 ? 115.29100 103.53400 47.43200  1.000 104.87857 ? 434 TRP A N    1 
ATOM   2658 C CA   . TRP A 1 434 ? 113.98400 102.89700 47.49600  1.000 103.99389 ? 434 TRP A CA   1 
ATOM   2659 C C    . TRP A 1 434 ? 113.99600 101.56700 46.75300  1.000 104.23650 ? 434 TRP A C    1 
ATOM   2660 O O    . TRP A 1 434 ? 114.78300 101.35100 45.82700  1.000 104.02476 ? 434 TRP A O    1 
ATOM   2661 C CB   . TRP A 1 434 ? 112.91000 103.81500 46.91300  1.000 102.99631 ? 434 TRP A CB   1 
ATOM   2662 C CG   . TRP A 1 434 ? 112.42800 104.85900 47.87400  1.000 103.77446 ? 434 TRP A CG   1 
ATOM   2663 C CD1  . TRP A 1 434 ? 112.89800 105.09300 49.13300  1.000 103.01778 ? 434 TRP A CD1  1 
ATOM   2664 C CD2  . TRP A 1 434 ? 111.38100 105.81100 47.65300  1.000 104.37007 ? 434 TRP A CD2  1 
ATOM   2665 N NE1  . TRP A 1 434 ? 112.20900 106.13100 49.71000  1.000 102.15847 ? 434 TRP A NE1  1 
ATOM   2666 C CE2  . TRP A 1 434 ? 111.27200 106.59000 48.82200  1.000 103.00557 ? 434 TRP A CE2  1 
ATOM   2667 C CE3  . TRP A 1 434 ? 110.52600 106.08100 46.58100  1.000 103.90265 ? 434 TRP A CE3  1 
ATOM   2668 C CZ2  . TRP A 1 434 ? 110.34300 107.62000 48.94900  1.000 102.61796 ? 434 TRP A CZ2  1 
ATOM   2669 C CZ3  . TRP A 1 434 ? 109.60400 107.10400 46.70900  1.000 103.56418 ? 434 TRP A CZ3  1 
ATOM   2670 C CH2  . TRP A 1 434 ? 109.52000 107.86100 47.88400  1.000 103.40929 ? 434 TRP A CH2  1 
ATOM   2671 N N    . GLU A 1 435 ? 113.10900 100.66900 47.16900  1.000 110.32997 ? 435 GLU A N    1 
ATOM   2672 C CA   . GLU A 1 435 ? 112.99200 99.36000  46.53800  1.000 110.63120 ? 435 GLU A CA   1 
ATOM   2673 C C    . GLU A 1 435 ? 111.58700 98.79100  46.71100  1.000 110.88646 ? 435 GLU A C    1 
ATOM   2674 O O    . GLU A 1 435 ? 111.08900 98.67000  47.82900  1.000 110.07723 ? 435 GLU A O    1 
ATOM   2675 C CB   . GLU A 1 435 ? 114.02600 98.39100  47.11300  1.000 109.91649 ? 435 GLU A CB   1 
ATOM   2676 C CG   . GLU A 1 435 ? 114.19300 97.11500  46.30600  1.000 109.71069 ? 435 GLU A CG   1 
ATOM   2677 C CD   . GLU A 1 435 ? 114.97700 96.05200  47.04900  1.000 110.79047 ? 435 GLU A CD   1 
ATOM   2678 O OE1  . GLU A 1 435 ? 116.18600 96.25900  47.28500  1.000 110.83555 ? 435 GLU A OE1  1 
ATOM   2679 O OE2  . GLU A 1 435 ? 114.38400 95.00900  47.39800  1.000 110.75005 ? 435 GLU A OE2  1 
ATOM   2680 N N    . LYS A 1 527 ? 125.76600 106.14900 54.48700  1.000 107.13360 ? 527 LYS A N    1 
ATOM   2681 C CA   . LYS A 1 527 ? 125.96100 105.86400 55.90300  1.000 108.01645 ? 527 LYS A CA   1 
ATOM   2682 C C    . LYS A 1 527 ? 124.62900 105.83100 56.64300  1.000 108.00489 ? 527 LYS A C    1 
ATOM   2683 O O    . LYS A 1 527 ? 123.63200 106.37800 56.17100  1.000 107.50990 ? 527 LYS A O    1 
ATOM   2684 C CB   . LYS A 1 527 ? 126.88900 106.90100 56.53700  1.000 108.02400 ? 527 LYS A CB   1 
ATOM   2685 C CG   . LYS A 1 527 ? 128.02200 106.30200 57.35500  1.000 107.36825 ? 527 LYS A CG   1 
ATOM   2686 C CD   . LYS A 1 527 ? 128.75400 107.37100 58.15000  1.000 107.32159 ? 527 LYS A CD   1 
ATOM   2687 C CE   . LYS A 1 527 ? 128.91500 108.64800 57.34200  1.000 107.64833 ? 527 LYS A CE   1 
ATOM   2688 N NZ   . LYS A 1 527 ? 129.87500 109.59100 57.97900  1.000 106.96621 ? 527 LYS A NZ   1 
ATOM   2689 N N    . THR A 1 528 ? 124.61900 105.18300 57.80800  1.000 103.11414 ? 528 THR A N    1 
ATOM   2690 C CA   . THR A 1 528 ? 123.41300 105.07900 58.61800  1.000 102.75491 ? 528 THR A CA   1 
ATOM   2691 C C    . THR A 1 528 ? 123.26900 106.21500 59.62000  1.000 102.09803 ? 528 THR A C    1 
ATOM   2692 O O    . THR A 1 528 ? 122.14100 106.53100 60.02200  1.000 102.46249 ? 528 THR A O    1 
ATOM   2693 C CB   . THR A 1 528 ? 123.39100 103.74200 59.36800  1.000 102.90350 ? 528 THR A CB   1 
ATOM   2694 O OG1  . THR A 1 528 ? 124.54900 103.64200 60.20500  1.000 102.70291 ? 528 THR A OG1  1 
ATOM   2695 C CG2  . THR A 1 528 ? 123.37900 102.58200 58.38500  1.000 101.75942 ? 528 THR A CG2  1 
ATOM   2696 N N    . TYR A 1 529 ? 124.37500 106.84900 60.01500  1.000 97.31915  ? 529 TYR A N    1 
ATOM   2697 C CA   . TYR A 1 529 ? 124.28900 107.93500 60.98400  1.000 97.10305  ? 529 TYR A CA   1 
ATOM   2698 C C    . TYR A 1 529 ? 123.59100 109.15000 60.38900  1.000 98.05325  ? 529 TYR A C    1 
ATOM   2699 O O    . TYR A 1 529 ? 122.80200 109.81400 61.07200  1.000 97.61060  ? 529 TYR A O    1 
ATOM   2700 C CB   . TYR A 1 529 ? 125.68600 108.30900 61.47900  1.000 96.21176  ? 529 TYR A CB   1 
ATOM   2701 C CG   . TYR A 1 529 ? 125.68500 109.28200 62.63600  1.000 97.23387  ? 529 TYR A CG   1 
ATOM   2702 C CD1  . TYR A 1 529 ? 125.00900 108.99100 63.81300  1.000 97.58148  ? 529 TYR A CD1  1 
ATOM   2703 C CD2  . TYR A 1 529 ? 126.35600 110.49400 62.54900  1.000 96.44206  ? 529 TYR A CD2  1 
ATOM   2704 C CE1  . TYR A 1 529 ? 125.00500 109.87900 64.87200  1.000 97.74716  ? 529 TYR A CE1  1 
ATOM   2705 C CE2  . TYR A 1 529 ? 126.35700 111.38800 63.60200  1.000 97.22803  ? 529 TYR A CE2  1 
ATOM   2706 C CZ   . TYR A 1 529 ? 125.68000 111.07500 64.76100  1.000 97.41368  ? 529 TYR A CZ   1 
ATOM   2707 O OH   . TYR A 1 529 ? 125.67800 111.96200 65.81200  1.000 96.15875  ? 529 TYR A OH   1 
ATOM   2708 N N    . GLU A 1 530 ? 123.83300 109.43500 59.10800  1.000 96.51569  ? 530 GLU A N    1 
ATOM   2709 C CA   . GLU A 1 530 ? 123.15100 110.55700 58.47400  1.000 96.02566  ? 530 GLU A CA   1 
ATOM   2710 C C    . GLU A 1 530 ? 121.67400 110.25400 58.25900  1.000 96.14561  ? 530 GLU A C    1 
ATOM   2711 O O    . GLU A 1 530 ? 120.82300 111.13900 58.41200  1.000 96.43377  ? 530 GLU A O    1 
ATOM   2712 C CB   . GLU A 1 530 ? 123.82900 110.90100 57.14900  1.000 95.80493  ? 530 GLU A CB   1 
ATOM   2713 C CG   . GLU A 1 530 ? 125.20800 111.52100 57.30100  1.000 96.92960  ? 530 GLU A CG   1 
ATOM   2714 C CD   . GLU A 1 530 ? 125.84300 111.86600 55.96800  1.000 98.49419  ? 530 GLU A CD   1 
ATOM   2715 O OE1  . GLU A 1 530 ? 125.09600 112.12900 55.00300  1.000 97.53642  ? 530 GLU A OE1  1 
ATOM   2716 O OE2  . GLU A 1 530 ? 127.08900 111.87400 55.88600  1.000 98.31877  ? 530 GLU A OE2  1 
ATOM   2717 N N    . SER A 1 531 ? 121.34400 108.99600 57.95500  1.000 88.28848  ? 531 SER A N    1 
ATOM   2718 C CA   . SER A 1 531 ? 119.94100 108.61600 57.83800  1.000 87.32965  ? 531 SER A CA   1 
ATOM   2719 C C    . SER A 1 531 ? 119.21900 108.76400 59.17000  1.000 87.01130  ? 531 SER A C    1 
ATOM   2720 O O    . SER A 1 531 ? 118.08700 109.26000 59.22100  1.000 88.88142  ? 531 SER A O    1 
ATOM   2721 C CB   . SER A 1 531 ? 119.82900 107.18200 57.32100  1.000 87.75085  ? 531 SER A CB   1 
ATOM   2722 O OG   . SER A 1 531 ? 120.74200 106.95000 56.26400  1.000 88.35965  ? 531 SER A OG   1 
ATOM   2723 N N    . ALA A 1 532 ? 119.86500 108.35700 60.26600  1.000 79.31867  ? 532 ALA A N    1 
ATOM   2724 C CA   . ALA A 1 532 ? 119.23100 108.48600 61.57400  1.000 78.94019  ? 532 ALA A CA   1 
ATOM   2725 C C    . ALA A 1 532 ? 119.10300 109.94800 61.98200  1.000 81.30771  ? 532 ALA A C    1 
ATOM   2726 O O    . ALA A 1 532 ? 118.07200 110.36100 62.53100  1.000 83.74582  ? 532 ALA A O    1 
ATOM   2727 C CB   . ALA A 1 532 ? 120.02100 107.69900 62.61800  1.000 79.52726  ? 532 ALA A CB   1 
ATOM   2728 N N    . SER A 1 533 ? 120.13500 110.75100 61.71700  1.000 78.01103  ? 533 SER A N    1 
ATOM   2729 C CA   . SER A 1 533 ? 120.05000 112.17600 62.00700  1.000 77.89519  ? 533 SER A CA   1 
ATOM   2730 C C    . SER A 1 533 ? 118.90800 112.82800 61.24000  1.000 77.98425  ? 533 SER A C    1 
ATOM   2731 O O    . SER A 1 533 ? 118.17900 113.66400 61.78800  1.000 78.77548  ? 533 SER A O    1 
ATOM   2732 C CB   . SER A 1 533 ? 121.37900 112.85400 61.67700  1.000 78.53106  ? 533 SER A CB   1 
ATOM   2733 O OG   . SER A 1 533 ? 121.37700 113.35800 60.35300  1.000 78.63746  ? 533 SER A OG   1 
ATOM   2734 N N    . ALA A 1 534 ? 118.73200 112.46000 59.96900  1.000 73.93932  ? 534 ALA A N    1 
ATOM   2735 C CA   . ALA A 1 534 ? 117.61300 112.98800 59.19600  1.000 74.36235  ? 534 ALA A CA   1 
ATOM   2736 C C    . ALA A 1 534 ? 116.27200 112.54500 59.77400  1.000 74.92912  ? 534 ALA A C    1 
ATOM   2737 O O    . ALA A 1 534 ? 115.36000 113.35900 59.95000  1.000 76.70571  ? 534 ALA A O    1 
ATOM   2738 C CB   . ALA A 1 534 ? 117.74000 112.55600 57.73500  1.000 74.46260  ? 534 ALA A CB   1 
ATOM   2739 N N    . LEU A 1 535 ? 116.13300 111.25300 60.07500  1.000 68.15707  ? 535 LEU A N    1 
ATOM   2740 C CA   . LEU A 1 535 ? 114.88400 110.73000 60.62100  1.000 67.49211  ? 535 LEU A CA   1 
ATOM   2741 C C    . LEU A 1 535 ? 114.60500 111.16600 62.05600  1.000 68.01699  ? 535 LEU A C    1 
ATOM   2742 O O    . LEU A 1 535 ? 113.51900 110.87200 62.56700  1.000 68.20254  ? 535 LEU A O    1 
ATOM   2743 C CB   . LEU A 1 535 ? 114.88300 109.20300 60.54200  1.000 69.02128  ? 535 LEU A CB   1 
ATOM   2744 C CG   . LEU A 1 535 ? 113.50400 108.54200 60.53000  1.000 70.34420  ? 535 LEU A CG   1 
ATOM   2745 C CD1  . LEU A 1 535 ? 112.82600 108.74500 59.18500  1.000 67.79733  ? 535 LEU A CD1  1 
ATOM   2746 C CD2  . LEU A 1 535 ? 113.61500 107.06200 60.86100  1.000 69.72195  ? 535 LEU A CD2  1 
ATOM   2747 N N    . SER A 1 536 ? 115.54000 111.84700 62.71800  1.000 64.39047  ? 536 SER A N    1 
ATOM   2748 C CA   . SER A 1 536 ? 115.30000 112.27400 64.09500  1.000 64.45431  ? 536 SER A CA   1 
ATOM   2749 C C    . SER A 1 536 ? 114.39000 113.49700 64.22100  1.000 66.12297  ? 536 SER A C    1 
ATOM   2750 O O    . SER A 1 536 ? 113.87300 113.74700 65.31500  1.000 67.12230  ? 536 SER A O    1 
ATOM   2751 C CB   . SER A 1 536 ? 116.63300 112.55600 64.79100  1.000 61.70699  ? 536 SER A CB   1 
ATOM   2752 O OG   . SER A 1 536 ? 117.34900 113.58100 64.12800  1.000 65.70022  ? 536 SER A OG   1 
ATOM   2753 N N    . LEU A 1 537 ? 114.18500 114.26700 63.15000  1.000 57.22275  ? 537 LEU A N    1 
ATOM   2754 C CA   . LEU A 1 537 ? 113.31300 115.44000 63.22400  1.000 56.22269  ? 537 LEU A CA   1 
ATOM   2755 C C    . LEU A 1 537 ? 111.83600 115.04800 63.25100  1.000 58.52865  ? 537 LEU A C    1 
ATOM   2756 O O    . LEU A 1 537 ? 111.01500 115.70400 63.91800  1.000 61.11625  ? 537 LEU A O    1 
ATOM   2757 C CB   . LEU A 1 537 ? 113.60300 116.36900 62.04400  1.000 57.03731  ? 537 LEU A CB   1 
ATOM   2758 C CG   . LEU A 1 537 ? 113.00600 117.77700 62.04600  1.000 61.33112  ? 537 LEU A CG   1 
ATOM   2759 C CD1  . LEU A 1 537 ? 113.80600 118.69900 62.94700  1.000 59.99309  ? 537 LEU A CD1  1 
ATOM   2760 C CD2  . LEU A 1 537 ? 112.95700 118.32800 60.63100  1.000 56.89632  ? 537 LEU A CD2  1 
ATOM   2761 N N    . ALA A 1 538 ? 111.48400 113.98400 62.52800  1.000 52.64979  ? 538 ALA A N    1 
ATOM   2762 C CA   . ALA A 1 538 ? 110.10600 113.51600 62.51700  1.000 50.54536  ? 538 ALA A CA   1 
ATOM   2763 C C    . ALA A 1 538 ? 109.66100 113.05800 63.89700  1.000 47.95986  ? 538 ALA A C    1 
ATOM   2764 O O    . ALA A 1 538 ? 108.48700 113.20300 64.24500  1.000 50.67730  ? 538 ALA A O    1 
ATOM   2765 C CB   . ALA A 1 538 ? 109.94400 112.38500 61.50100  1.000 50.63286  ? 538 ALA A CB   1 
ATOM   2766 N N    . THR A 1 539 ? 110.56900 112.48600 64.68900  1.000 39.06184  ? 539 THR A N    1 
ATOM   2767 C CA   . THR A 1 539 ? 110.23100 112.12700 66.06300  1.000 45.91397  ? 539 THR A CA   1 
ATOM   2768 C C    . THR A 1 539 ? 109.76900 113.34700 66.85400  1.000 46.82698  ? 539 THR A C    1 
ATOM   2769 O O    . THR A 1 539 ? 108.73800 113.31000 67.53500  1.000 47.94805  ? 539 THR A O    1 
ATOM   2770 C CB   . THR A 1 539 ? 111.43300 111.47100 66.74200  1.000 45.16841  ? 539 THR A CB   1 
ATOM   2771 O OG1  . THR A 1 539 ? 111.63100 110.15900 66.20400  1.000 47.57416  ? 539 THR A OG1  1 
ATOM   2772 C CG2  . THR A 1 539 ? 111.20300 111.36400 68.24000  1.000 42.17041  ? 539 THR A CG2  1 
ATOM   2773 N N    . PHE A 1 540 ? 110.53000 114.44000 66.77500  1.000 38.70961  ? 540 PHE A N    1 
ATOM   2774 C CA   . PHE A 1 540 ? 110.17800 115.66300 67.48900  1.000 41.07423  ? 540 PHE A CA   1 
ATOM   2775 C C    . PHE A 1 540 ? 108.83100 116.21000 67.02100  1.000 42.80720  ? 540 PHE A C    1 
ATOM   2776 O O    . PHE A 1 540 ? 107.98500 116.60500 67.84100  1.000 40.96175  ? 540 PHE A O    1 
ATOM   2777 C CB   . PHE A 1 540 ? 111.30300 116.68800 67.29200  1.000 38.28774  ? 540 PHE A CB   1 
ATOM   2778 C CG   . PHE A 1 540 ? 111.11300 117.98000 68.04100  1.000 42.77128  ? 540 PHE A CG   1 
ATOM   2779 C CD1  . PHE A 1 540 ? 110.23300 118.94700 67.58800  1.000 44.40718  ? 540 PHE A CD1  1 
ATOM   2780 C CD2  . PHE A 1 540 ? 111.83400 118.23000 69.19600  1.000 41.82479  ? 540 PHE A CD2  1 
ATOM   2781 C CE1  . PHE A 1 540 ? 110.06900 120.13300 68.27800  1.000 42.93183  ? 540 PHE A CE1  1 
ATOM   2782 C CE2  . PHE A 1 540 ? 111.67300 119.41200 69.89000  1.000 40.30682  ? 540 PHE A CE2  1 
ATOM   2783 C CZ   . PHE A 1 540 ? 110.79000 120.36400 69.43100  1.000 39.86959  ? 540 PHE A CZ   1 
ATOM   2784 N N    . ALA A 1 541 ? 108.60300 116.21400 65.70400  1.000 35.51847  ? 541 ALA A N    1 
ATOM   2785 C CA   . ALA A 1 541 ? 107.32500 116.70600 65.19000  1.000 32.51951  ? 541 ALA A CA   1 
ATOM   2786 C C    . ALA A 1 541 ? 106.15400 115.83100 65.63800  1.000 37.88144  ? 541 ALA A C    1 
ATOM   2787 O O    . ALA A 1 541 ? 105.11200 116.34500 66.07300  1.000 40.77492  ? 541 ALA A O    1 
ATOM   2788 C CB   . ALA A 1 541 ? 107.37400 116.79300 63.66600  1.000 33.14495  ? 541 ALA A CB   1 
ATOM   2789 N N    . SER A 1 542 ? 106.31100 114.50800 65.56000  1.000 37.51827  ? 542 SER A N    1 
ATOM   2790 C CA   . SER A 1 542 ? 105.25800 113.60200 66.00500  1.000 33.84998  ? 542 SER A CA   1 
ATOM   2791 C C    . SER A 1 542 ? 104.98700 113.74000 67.49400  1.000 37.10810  ? 542 SER A C    1 
ATOM   2792 O O    . SER A 1 542 ? 103.84100 113.59100 67.93000  1.000 39.50405  ? 542 SER A O    1 
ATOM   2793 C CB   . SER A 1 542 ? 105.63200 112.15900 65.66700  1.000 34.02246  ? 542 SER A CB   1 
ATOM   2794 O OG   . SER A 1 542 ? 105.48400 111.90500 64.28300  1.000 41.17025  ? 542 SER A OG   1 
ATOM   2795 N N    . LEU A 1 543 ? 106.01400 114.04000 68.28700  1.000 35.61898  ? 543 LEU A N    1 
ATOM   2796 C CA   . LEU A 1 543 ? 105.80500 114.19600 69.72200  1.000 35.14333  ? 543 LEU A CA   1 
ATOM   2797 C C    . LEU A 1 543 ? 105.01000 115.46000 70.02400  1.000 35.10369  ? 543 LEU A C    1 
ATOM   2798 O O    . LEU A 1 543 ? 104.08600 115.44200 70.84700  1.000 42.27707  ? 543 LEU A O    1 
ATOM   2799 C CB   . LEU A 1 543 ? 107.14800 114.20800 70.45200  1.000 43.24392  ? 543 LEU A CB   1 
ATOM   2800 C CG   . LEU A 1 543 ? 107.84800 112.85400 70.58300  1.000 43.08263  ? 543 LEU A CG   1 
ATOM   2801 C CD1  . LEU A 1 543 ? 109.22700 113.01600 71.19900  1.000 37.22418  ? 543 LEU A CD1  1 
ATOM   2802 C CD2  . LEU A 1 543 ? 107.00100 111.89000 71.39600  1.000 36.08440  ? 543 LEU A CD2  1 
ATOM   2803 N N    . LEU A 1 544 ? 105.38800 116.58100 69.40500  1.000 36.12312  ? 544 LEU A N    1 
ATOM   2804 C CA   . LEU A 1 544 ? 104.56600 117.78600 69.51500  1.000 35.43107  ? 544 LEU A CA   1 
ATOM   2805 C C    . LEU A 1 544 ? 103.10900 117.51600 69.13100  1.000 37.19812  ? 544 LEU A C    1 
ATOM   2806 O O    . LEU A 1 544 ? 102.17100 117.93700 69.83400  1.000 43.13750  ? 544 LEU A O    1 
ATOM   2807 C CB   . LEU A 1 544 ? 105.15900 118.89100 68.64000  1.000 37.35898  ? 544 LEU A CB   1 
ATOM   2808 C CG   . LEU A 1 544 ? 105.05200 120.32600 69.15300  1.000 42.01557  ? 544 LEU A CG   1 
ATOM   2809 C CD1  . LEU A 1 544 ? 105.56100 120.41700 70.58000  1.000 38.61985  ? 544 LEU A CD1  1 
ATOM   2810 C CD2  . LEU A 1 544 ? 105.82600 121.26500 68.24700  1.000 38.48879  ? 544 LEU A CD2  1 
ATOM   2811 N N    . ILE A 1 545 ? 102.90200 116.78400 68.03300  1.000 31.06240  ? 545 ILE A N    1 
ATOM   2812 C CA   . ILE A 1 545 ? 101.54300 116.48600 67.58400  1.000 30.23101  ? 545 ILE A CA   1 
ATOM   2813 C C    . ILE A 1 545 ? 100.79500 115.65700 68.62400  1.000 33.70017  ? 545 ILE A C    1 
ATOM   2814 O O    . ILE A 1 545 ? 99.61100  115.89400 68.89200  1.000 31.90904  ? 545 ILE A O    1 
ATOM   2815 C CB   . ILE A 1 545 ? 101.57700 115.78200 66.21500  1.000 34.04598  ? 545 ILE A CB   1 
ATOM   2816 C CG1  . ILE A 1 545 ? 102.08700 116.73900 65.13700  1.000 31.95945  ? 545 ILE A CG1  1 
ATOM   2817 C CG2  . ILE A 1 545 ? 100.19500 115.26700 65.84800  1.000 31.62177  ? 545 ILE A CG2  1 
ATOM   2818 C CD1  . ILE A 1 545 ? 100.99500 117.41300 64.35100  1.000 31.96367  ? 545 ILE A CD1  1 
ATOM   2819 N N    . GLU A 1 546 ? 101.45600 114.64600 69.19200  1.000 33.26397  ? 546 GLU A N    1 
ATOM   2820 C CA   . GLU A 1 546 ? 100.83200 113.83600 70.23600  1.000 36.97048  ? 546 GLU A CA   1 
ATOM   2821 C C    . GLU A 1 546 ? 100.45800 114.66900 71.46000  1.000 36.77637  ? 546 GLU A C    1 
ATOM   2822 O O    . GLU A 1 546 ? 99.38400  114.48000 72.04500  1.000 36.41052  ? 546 GLU A O    1 
ATOM   2823 C CB   . GLU A 1 546 ? 101.76400 112.69100 70.63200  1.000 32.83605  ? 546 GLU A CB   1 
ATOM   2824 C CG   . GLU A 1 546 ? 101.32600 111.94500 71.87700  1.000 34.39386  ? 546 GLU A CG   1 
ATOM   2825 C CD   . GLU A 1 546 ? 100.15300 111.02300 71.61600  1.000 41.48472  ? 546 GLU A CD   1 
ATOM   2826 O OE1  . GLU A 1 546 ? 99.93900  110.64700 70.44500  1.000 42.77473  ? 546 GLU A OE1  1 
ATOM   2827 O OE2  . GLU A 1 546 ? 99.44100  110.67900 72.58100  1.000 39.87235  ? 546 GLU A OE2  1 
ATOM   2828 N N    . PHE A 1 547 ? 101.35000 115.56300 71.89000  1.000 27.60528  ? 547 PHE A N    1 
ATOM   2829 C CA   . PHE A 1 547 ? 101.02300 116.48200 72.97900  1.000 31.00556  ? 547 PHE A CA   1 
ATOM   2830 C C    . PHE A 1 547 ? 99.71500  117.21800 72.70100  1.000 30.39854  ? 547 PHE A C    1 
ATOM   2831 O O    . PHE A 1 547 ? 98.81800  117.29300 73.55900  1.000 24.94521  ? 547 PHE A O    1 
ATOM   2832 C CB   . PHE A 1 547 ? 102.17600 117.46900 73.17700  1.000 33.60963  ? 547 PHE A CB   1 
ATOM   2833 C CG   . PHE A 1 547 ? 101.84500 118.63000 74.07300  1.000 33.65285  ? 547 PHE A CG   1 
ATOM   2834 C CD1  . PHE A 1 547 ? 101.94900 118.51000 75.44800  1.000 34.31333  ? 547 PHE A CD1  1 
ATOM   2835 C CD2  . PHE A 1 547 ? 101.44000 119.84100 73.54200  1.000 30.45733  ? 547 PHE A CD2  1 
ATOM   2836 C CE1  . PHE A 1 547 ? 101.65000 119.57400 76.27400  1.000 33.13500  ? 547 PHE A CE1  1 
ATOM   2837 C CE2  . PHE A 1 547 ? 101.13900 120.90600 74.36300  1.000 30.42482  ? 547 PHE A CE2  1 
ATOM   2838 C CZ   . PHE A 1 547 ? 101.24400 120.77300 75.73100  1.000 31.02033  ? 547 PHE A CZ   1 
ATOM   2839 N N    . VAL A 1 548 ? 99.59300  117.77200 71.49400  1.000 33.30340  ? 548 VAL A N    1 
ATOM   2840 C CA   . VAL A 1 548 ? 98.36500  118.48600 71.14700  1.000 30.17155  ? 548 VAL A CA   1 
ATOM   2841 C C    . VAL A 1 548 ? 97.16600  117.54200 71.18800  1.000 28.14308  ? 548 VAL A C    1 
ATOM   2842 O O    . VAL A 1 548 ? 96.11200  117.87100 71.74500  1.000 24.83252  ? 548 VAL A O    1 
ATOM   2843 C CB   . VAL A 1 548 ? 98.50300  119.16400 69.77300  1.000 27.87204  ? 548 VAL A CB   1 
ATOM   2844 C CG1  . VAL A 1 548 ? 97.20500  119.85300 69.39600  1.000 28.50473  ? 548 VAL A CG1  1 
ATOM   2845 C CG2  . VAL A 1 548 ? 99.64400  120.16200 69.79000  1.000 27.27343  ? 548 VAL A CG2  1 
ATOM   2846 N N    . ALA A 1 549 ? 97.31000  116.35400 70.59600  1.000 35.83828  ? 549 ALA A N    1 
ATOM   2847 C CA   . ALA A 1 549 ? 96.22800  115.37100 70.60300  1.000 29.41681  ? 549 ALA A CA   1 
ATOM   2848 C C    . ALA A 1 549 ? 95.79900  114.97600 72.01200  1.000 27.95412  ? 549 ALA A C    1 
ATOM   2849 O O    . ALA A 1 549 ? 94.65500  114.55200 72.21300  1.000 29.39792  ? 549 ALA A O    1 
ATOM   2850 C CB   . ALA A 1 549 ? 96.64500  114.13000 69.81400  1.000 27.11415  ? 549 ALA A CB   1 
ATOM   2851 N N    . ARG A 1 550 ? 96.68700  115.10200 72.99500  1.000 35.28444  ? 550 ARG A N    1 
ATOM   2852 C CA   . ARG A 1 550 ? 96.33700  114.74500 74.36700  1.000 29.26492  ? 550 ARG A CA   1 
ATOM   2853 C C    . ARG A 1 550 ? 95.73100  115.89500 75.16000  1.000 35.45513  ? 550 ARG A C    1 
ATOM   2854 O O    . ARG A 1 550 ? 95.01600  115.64500 76.13700  1.000 33.57244  ? 550 ARG A O    1 
ATOM   2855 C CB   . ARG A 1 550 ? 97.56200  114.22300 75.12400  1.000 30.64002  ? 550 ARG A CB   1 
ATOM   2856 C CG   . ARG A 1 550 ? 98.10500  112.90200 74.61900  1.000 34.68769  ? 550 ARG A CG   1 
ATOM   2857 C CD   . ARG A 1 550 ? 99.24000  112.40700 75.50300  1.000 33.37015  ? 550 ARG A CD   1 
ATOM   2858 N NE   . ARG A 1 550 ? 99.87500  111.21200 74.95900  1.000 35.75747  ? 550 ARG A NE   1 
ATOM   2859 C CZ   . ARG A 1 550 ? 100.84800 110.54000 75.55900  1.000 32.78817  ? 550 ARG A CZ   1 
ATOM   2860 N NH1  . ARG A 1 550 ? 101.33200 110.92100 76.72900  1.000 29.53478  ? 550 ARG A NH1  1 
ATOM   2861 N NH2  . ARG A 1 550 ? 101.34600 109.45700 74.97100  1.000 30.72160  ? 550 ARG A NH2  1 
ATOM   2862 N N    . LEU A 1 551 ? 96.01600  117.14000 74.77900  1.000 40.66585  ? 551 LEU A N    1 
ATOM   2863 C CA   . LEU A 1 551 ? 95.49900  118.29700 75.51400  1.000 37.12321  ? 551 LEU A CA   1 
ATOM   2864 C C    . LEU A 1 551 ? 94.00800  118.22000 75.88200  1.000 33.19471  ? 551 LEU A C    1 
ATOM   2865 O O    . LEU A 1 551 ? 93.59100  118.88000 76.83900  1.000 44.26016  ? 551 LEU A O    1 
ATOM   2866 C CB   . LEU A 1 551 ? 95.74500  119.56600 74.69800  1.000 37.63950  ? 551 LEU A CB   1 
ATOM   2867 C CG   . LEU A 1 551 ? 97.00300  120.35200 75.07100  1.000 41.00700  ? 551 LEU A CG   1 
ATOM   2868 C CD1  . LEU A 1 551 ? 97.09500  121.63400 74.25700  1.000 37.57698  ? 551 LEU A CD1  1 
ATOM   2869 C CD2  . LEU A 1 551 ? 97.04900  120.63800 76.56400  1.000 32.23604  ? 551 LEU A CD2  1 
ATOM   2870 N N    . GLN A 1 552 ? 93.19300  117.45100 75.15100  1.000 37.37283  ? 552 GLN A N    1 
ATOM   2871 C CA   . GLN A 1 552 ? 91.73800  117.46200 75.35600  1.000 37.75236  ? 552 GLN A CA   1 
ATOM   2872 C C    . GLN A 1 552 ? 91.31300  116.87600 76.70500  1.000 42.24476  ? 552 GLN A C    1 
ATOM   2873 O O    . GLN A 1 552 ? 90.32300  117.32900 77.30500  1.000 45.10402  ? 552 GLN A O    1 
ATOM   2874 C CB   . GLN A 1 552 ? 91.05600  116.70700 74.21600  1.000 38.34255  ? 552 GLN A CB   1 
ATOM   2875 C CG   . GLN A 1 552 ? 89.60100  116.35400 74.47900  1.000 43.60212  ? 552 GLN A CG   1 
ATOM   2876 C CD   . GLN A 1 552 ? 88.63700  117.32300 73.82400  1.000 45.06706  ? 552 GLN A CD   1 
ATOM   2877 O OE1  . GLN A 1 552 ? 88.71100  117.57000 72.62100  1.000 45.84753  ? 552 GLN A OE1  1 
ATOM   2878 N NE2  . GLN A 1 552 ? 87.72400  117.87400 74.61400  1.000 38.34633  ? 552 GLN A NE2  1 
ATOM   2879 N N    . ASN A 1 553 ? 92.00600  115.83600 77.17200  1.000 42.22987  ? 553 ASN A N    1 
ATOM   2880 C CA   . ASN A 1 553 ? 91.61200  115.18800 78.41900  1.000 37.64907  ? 553 ASN A CA   1 
ATOM   2881 C C    . ASN A 1 553 ? 91.67700  116.14600 79.60200  1.000 36.04485  ? 553 ASN A C    1 
ATOM   2882 O O    . ASN A 1 553 ? 90.86500  116.04400 80.53200  1.000 38.62776  ? 553 ASN A O    1 
ATOM   2883 C CB   . ASN A 1 553 ? 92.50000  113.96800 78.66900  1.000 44.98168  ? 553 ASN A CB   1 
ATOM   2884 C CG   . ASN A 1 553 ? 91.78200  112.86500 79.41500  1.000 44.47519  ? 553 ASN A CG   1 
ATOM   2885 O OD1  . ASN A 1 553 ? 92.24400  112.40200 80.45700  1.000 43.96181  ? 553 ASN A OD1  1 
ATOM   2886 N ND2  . ASN A 1 553 ? 90.64500  112.43600 78.88300  1.000 47.91800  ? 553 ASN A ND2  1 
ATOM   2887 N N    . VAL A 1 554 ? 92.61300  117.09600 79.57800  1.000 28.63341  ? 554 VAL A N    1 
ATOM   2888 C CA   . VAL A 1 554 ? 92.71300  118.05800 80.66900  1.000 33.04558  ? 554 VAL A CA   1 
ATOM   2889 C C    . VAL A 1 554 ? 91.48000  118.95200 80.70200  1.000 37.80801  ? 554 VAL A C    1 
ATOM   2890 O O    . VAL A 1 554 ? 90.95200  119.26800 81.77400  1.000 36.11818  ? 554 VAL A O    1 
ATOM   2891 C CB   . VAL A 1 554 ? 94.00900  118.88000 80.53700  1.000 34.24807  ? 554 VAL A CB   1 
ATOM   2892 C CG1  . VAL A 1 554 ? 94.29100  119.64200 81.82000  1.000 36.49090  ? 554 VAL A CG1  1 
ATOM   2893 C CG2  . VAL A 1 554 ? 95.17600  117.97500 80.18100  1.000 29.44472  ? 554 VAL A CG2  1 
ATOM   2894 N N    . VAL A 1 555 ? 90.98600  119.35300 79.52900  1.000 38.22795  ? 555 VAL A N    1 
ATOM   2895 C CA   . VAL A 1 555 ? 89.78900  120.18300 79.47900  1.000 33.02974  ? 555 VAL A CA   1 
ATOM   2896 C C    . VAL A 1 555 ? 88.58200  119.40000 79.97400  1.000 33.44096  ? 555 VAL A C    1 
ATOM   2897 O O    . VAL A 1 555 ? 87.72700  119.93400 80.69400  1.000 41.06816  ? 555 VAL A O    1 
ATOM   2898 C CB   . VAL A 1 555 ? 89.57100  120.72300 78.05500  1.000 37.52189  ? 555 VAL A CB   1 
ATOM   2899 C CG1  . VAL A 1 555 ? 88.15600  121.25400 77.89900  1.000 36.43892  ? 555 VAL A CG1  1 
ATOM   2900 C CG2  . VAL A 1 555 ? 90.59300  121.80400 77.73700  1.000 34.07111  ? 555 VAL A CG2  1 
ATOM   2901 N N    . ASP A 1 556 ? 88.48900  118.12300 79.59800  1.000 37.66562  ? 556 ASP A N    1 
ATOM   2902 C CA   . ASP A 1 556 ? 87.37100  117.31500 80.08400  1.000 38.56688  ? 556 ASP A CA   1 
ATOM   2903 C C    . ASP A 1 556 ? 87.39900  117.18900 81.60600  1.000 42.65509  ? 556 ASP A C    1 
ATOM   2904 O O    . ASP A 1 556 ? 86.36500  117.34400 82.27600  1.000 42.80209  ? 556 ASP A O    1 
ATOM   2905 C CB   . ASP A 1 556 ? 87.39700  115.93400 79.43100  1.000 41.90413  ? 556 ASP A CB   1 
ATOM   2906 C CG   . ASP A 1 556 ? 86.68400  115.90800 78.09700  1.000 50.66447  ? 556 ASP A CG   1 
ATOM   2907 O OD1  . ASP A 1 556 ? 86.10400  116.94400 77.71000  1.000 47.69040  ? 556 ASP A OD1  1 
ATOM   2908 O OD2  . ASP A 1 556 ? 86.70400  114.85000 77.43300  1.000 51.41968  ? 556 ASP A OD2  1 
ATOM   2909 N N    . ALA A 1 557 ? 88.58000  116.93000 82.17200  1.000 40.43222  ? 557 ALA A N    1 
ATOM   2910 C CA   . ALA A 1 557 ? 88.69200  116.82700 83.62400  1.000 37.21561  ? 557 ALA A CA   1 
ATOM   2911 C C    . ALA A 1 557 ? 88.34200  118.14800 84.29700  1.000 35.96563  ? 557 ALA A C    1 
ATOM   2912 O O    . ALA A 1 557 ? 87.68700  118.16500 85.34700  1.000 37.09911  ? 557 ALA A O    1 
ATOM   2913 C CB   . ALA A 1 557 ? 90.09800  116.37700 84.01700  1.000 32.90226  ? 557 ALA A CB   1 
ATOM   2914 N N    . PHE A 1 558 ? 88.78700  119.26800 83.72000  1.000 38.92259  ? 558 PHE A N    1 
ATOM   2915 C CA   . PHE A 1 558 ? 88.46100  120.56400 84.30200  1.000 36.43160  ? 558 PHE A CA   1 
ATOM   2916 C C    . PHE A 1 558 ? 86.95900  120.80400 84.29900  1.000 38.20254  ? 558 PHE A C    1 
ATOM   2917 O O    . PHE A 1 558 ? 86.41000  121.34500 85.26400  1.000 42.60972  ? 558 PHE A O    1 
ATOM   2918 C CB   . PHE A 1 558 ? 89.17600  121.68800 83.55600  1.000 37.69093  ? 558 PHE A CB   1 
ATOM   2919 C CG   . PHE A 1 558 ? 88.77700  123.06000 84.02100  1.000 38.65342  ? 558 PHE A CG   1 
ATOM   2920 C CD1  . PHE A 1 558 ? 89.39600  123.64200 85.11100  1.000 36.01850  ? 558 PHE A CD1  1 
ATOM   2921 C CD2  . PHE A 1 558 ? 87.77000  123.75900 83.37900  1.000 39.85765  ? 558 PHE A CD2  1 
ATOM   2922 C CE1  . PHE A 1 558 ? 89.02400  124.89800 85.54500  1.000 38.41741  ? 558 PHE A CE1  1 
ATOM   2923 C CE2  . PHE A 1 558 ? 87.39600  125.01400 83.81300  1.000 37.62642  ? 558 PHE A CE2  1 
ATOM   2924 C CZ   . PHE A 1 558 ? 88.02500  125.58400 84.89500  1.000 39.35365  ? 558 PHE A CZ   1 
ATOM   2925 N N    . LYS A 1 559 ? 86.28100  120.44500 83.20800  1.000 44.88604  ? 559 LYS A N    1 
ATOM   2926 C CA   . LYS A 1 559 ? 84.83400  120.62600 83.16900  1.000 43.12635  ? 559 LYS A CA   1 
ATOM   2927 C C    . LYS A 1 559 ? 84.15500  119.78400 84.24200  1.000 47.10639  ? 559 LYS A C    1 
ATOM   2928 O O    . LYS A 1 559 ? 83.24000  120.25600 84.93300  1.000 51.24805  ? 559 LYS A O    1 
ATOM   2929 C CB   . LYS A 1 559 ? 84.29600  120.27100 81.78400  1.000 42.55943  ? 559 LYS A CB   1 
ATOM   2930 C CG   . LYS A 1 559 ? 83.09200  121.08800 81.36000  1.000 46.10905  ? 559 LYS A CG   1 
ATOM   2931 C CD   . LYS A 1 559 ? 83.34500  121.79000 80.03900  1.000 46.31117  ? 559 LYS A CD   1 
ATOM   2932 C CE   . LYS A 1 559 ? 83.33900  120.80500 78.88500  1.000 47.93922  ? 559 LYS A CE   1 
ATOM   2933 N NZ   . LYS A 1 559 ? 83.40600  121.50200 77.57200  1.000 47.16640  ? 559 LYS A NZ   1 
ATOM   2934 N N    . GLU A 1 560 ? 84.61400  118.54300 84.42100  1.000 51.66660  ? 560 GLU A N    1 
ATOM   2935 C CA   . GLU A 1 560 ? 84.03400  117.70900 85.47000  1.000 46.02903  ? 560 GLU A CA   1 
ATOM   2936 C C    . GLU A 1 560 ? 84.24200  118.32700 86.84800  1.000 48.41195  ? 560 GLU A C    1 
ATOM   2937 O O    . GLU A 1 560 ? 83.31900  118.35200 87.67300  1.000 50.32550  ? 560 GLU A O    1 
ATOM   2938 C CB   . GLU A 1 560 ? 84.63100  116.30300 85.42100  1.000 45.47489  ? 560 GLU A CB   1 
ATOM   2939 C CG   . GLU A 1 560 ? 84.44800  115.51700 86.70800  1.000 51.88471  ? 560 GLU A CG   1 
ATOM   2940 C CD   . GLU A 1 560 ? 84.22700  114.03700 86.46500  1.000 57.85956  ? 560 GLU A CD   1 
ATOM   2941 O OE1  . GLU A 1 560 ? 84.03100  113.29500 87.45100  1.000 57.75217  ? 560 GLU A OE1  1 
ATOM   2942 O OE2  . GLU A 1 560 ? 84.24800  113.61600 85.28900  1.000 53.48247  ? 560 GLU A OE2  1 
ATOM   2943 N N    . LEU A 1 561 ? 85.44800  118.83600 87.11700  1.000 44.51231  ? 561 LEU A N    1 
ATOM   2944 C CA   . LEU A 1 561 ? 85.71400  119.45500 88.41400  1.000 41.44693  ? 561 LEU A CA   1 
ATOM   2945 C C    . LEU A 1 561 ? 84.86000  120.69900 88.62500  1.000 42.50456  ? 561 LEU A C    1 
ATOM   2946 O O    . LEU A 1 561 ? 84.30300  120.90000 89.71000  1.000 40.40952  ? 561 LEU A O    1 
ATOM   2947 C CB   . LEU A 1 561 ? 87.19600  119.80300 88.54500  1.000 44.55413  ? 561 LEU A CB   1 
ATOM   2948 C CG   . LEU A 1 561 ? 87.53500  120.84700 89.61600  1.000 40.64688  ? 561 LEU A CG   1 
ATOM   2949 C CD1  . LEU A 1 561 ? 87.44700  120.24300 91.00600  1.000 40.42064  ? 561 LEU A CD1  1 
ATOM   2950 C CD2  . LEU A 1 561 ? 88.91000  121.44800 89.38300  1.000 35.46336  ? 561 LEU A CD2  1 
ATOM   2951 N N    . SER A 1 562 ? 84.74700  121.54900 87.60300  1.000 51.79115  ? 562 SER A N    1 
ATOM   2952 C CA   . SER A 1 562 ? 83.94700  122.75900 87.73000  1.000 47.66327  ? 562 SER A CA   1 
ATOM   2953 C C    . SER A 1 562 ? 82.46300  122.45500 87.85900  1.000 47.58947  ? 562 SER A C    1 
ATOM   2954 O O    . SER A 1 562 ? 81.70800  123.31100 88.33000  1.000 44.92237  ? 562 SER A O    1 
ATOM   2955 C CB   . SER A 1 562 ? 84.18400  123.68100 86.53500  1.000 46.04244  ? 562 SER A CB   1 
ATOM   2956 O OG   . SER A 1 562 ? 83.37800  124.84300 86.62100  1.000 53.36800  ? 562 SER A OG   1 
ATOM   2957 N N    . GLN A 1 563 ? 82.02900  121.26000 87.45900  1.000 60.77222  ? 563 GLN A N    1 
ATOM   2958 C CA   . GLN A 1 563 ? 80.62800  120.90500 87.65400  1.000 59.43238  ? 563 GLN A CA   1 
ATOM   2959 C C    . GLN A 1 563 ? 80.37600  120.28100 89.02200  1.000 59.62535  ? 563 GLN A C    1 
ATOM   2960 O O    . GLN A 1 563 ? 79.35200  120.56900 89.65100  1.000 58.33201  ? 563 GLN A O    1 
ATOM   2961 C CB   . GLN A 1 563 ? 80.16100  119.94900 86.55400  1.000 58.90791  ? 563 GLN A CB   1 
ATOM   2962 C CG   . GLN A 1 563 ? 80.10700  120.57300 85.17100  1.000 63.31154  ? 563 GLN A CG   1 
ATOM   2963 C CD   . GLN A 1 563 ? 79.65100  119.59300 84.10900  1.000 67.34680  ? 563 GLN A CD   1 
ATOM   2964 O OE1  . GLN A 1 563 ? 79.43200  118.41500 84.38900  1.000 66.08205  ? 563 GLN A OE1  1 
ATOM   2965 N NE2  . GLN A 1 563 ? 79.50600  120.07700 82.88100  1.000 65.07526  ? 563 GLN A NE2  1 
ATOM   2966 N N    . LYS A 1 564 ? 81.28900  119.43100 89.50100  1.000 58.74095  ? 564 LYS A N    1 
ATOM   2967 C CA   . LYS A 1 564 ? 81.11000  118.83400 90.82300  1.000 55.10984  ? 564 LYS A CA   1 
ATOM   2968 C C    . LYS A 1 564 ? 81.08500  119.89700 91.91500  1.000 54.07592  ? 564 LYS A C    1 
ATOM   2969 O O    . LYS A 1 564 ? 80.27400  119.82400 92.84500  1.000 55.92626  ? 564 LYS A O    1 
ATOM   2970 C CB   . LYS A 1 564 ? 82.21000  117.81000 91.09500  1.000 52.94113  ? 564 LYS A CB   1 
ATOM   2971 C CG   . LYS A 1 564 ? 82.13100  116.57700 90.21700  1.000 53.84466  ? 564 LYS A CG   1 
ATOM   2972 C CD   . LYS A 1 564 ? 80.71700  116.02600 90.17400  1.000 53.68866  ? 564 LYS A CD   1 
ATOM   2973 C CE   . LYS A 1 564 ? 80.71800  114.50900 90.21100  1.000 54.52036  ? 564 LYS A CE   1 
ATOM   2974 N NZ   . LYS A 1 564 ? 81.07100  113.99000 91.56100  1.000 59.14186  ? 564 LYS A NZ   1 
ATOM   2975 N N    . ALA A 1 565 ? 81.96900  120.88500 91.82600  1.000 54.60731  ? 565 ALA A N    1 
ATOM   2976 C CA   . ALA A 1 565 ? 81.98900  122.00700 92.75300  1.000 52.51395  ? 565 ALA A CA   1 
ATOM   2977 C C    . ALA A 1 565 ? 81.32600  123.21300 92.10200  1.000 57.77505  ? 565 ALA A C    1 
ATOM   2978 O O    . ALA A 1 565 ? 81.52200  123.47400 90.91200  1.000 63.53909  ? 565 ALA A O    1 
ATOM   2979 C CB   . ALA A 1 565 ? 83.41900  122.35400 93.17000  1.000 46.52965  ? 565 ALA A CB   1 
ATOM   2980 N N    . ASN A 1 566 ? 80.53200  123.94100 92.88300  1.000 48.84509  ? 566 ASN A N    1 
ATOM   2981 C CA   . ASN A 1 566 ? 79.79400  125.07000 92.33400  1.000 49.22223  ? 566 ASN A CA   1 
ATOM   2982 C C    . ASN A 1 566 ? 80.73500  126.22700 92.03200  1.000 51.00501  ? 566 ASN A C    1 
ATOM   2983 O O    . ASN A 1 566 ? 81.00700  127.05800 92.90400  1.000 55.21531  ? 566 ASN A O    1 
ATOM   2984 C CB   . ASN A 1 566 ? 78.69600  125.51200 93.30300  1.000 52.70737  ? 566 ASN A CB   1 
ATOM   2985 C CG   . ASN A 1 566 ? 77.37400  125.76800 92.60700  1.000 58.32013  ? 566 ASN A CG   1 
ATOM   2986 O OD1  . ASN A 1 566 ? 76.77800  124.86100 92.02800  1.000 59.59660  ? 566 ASN A OD1  1 
ATOM   2987 N ND2  . ASN A 1 566 ? 76.90800  127.01100 92.66200  1.000 55.01597  ? 566 ASN A ND2  1 
ATOM   2988 N N    . PHE A 1 567 ? 81.22800  126.29500 90.79900  1.000 47.78544  ? 567 PHE A N    1 
ATOM   2989 C CA   . PHE A 1 567 ? 82.10000  127.37800 90.37300  1.000 46.03694  ? 567 PHE A CA   1 
ATOM   2990 C C    . PHE A 1 567 ? 81.27100  128.56300 89.89200  1.000 51.22722  ? 567 PHE A C    1 
ATOM   2991 O O    . PHE A 1 567 ? 80.18100  128.40100 89.33700  1.000 52.25547  ? 567 PHE A O    1 
ATOM   2992 C CB   . PHE A 1 567 ? 83.04300  126.91500 89.26200  1.000 46.21955  ? 567 PHE A CB   1 
ATOM   2993 C CG   . PHE A 1 567 ? 84.32800  126.31600 89.76300  1.000 49.37190  ? 567 PHE A CG   1 
ATOM   2994 C CD1  . PHE A 1 567 ? 84.47000  125.95200 91.08900  1.000 52.37417  ? 567 PHE A CD1  1 
ATOM   2995 C CD2  . PHE A 1 567 ? 85.39900  126.12700 88.90500  1.000 46.10598  ? 567 PHE A CD2  1 
ATOM   2996 C CE1  . PHE A 1 567 ? 85.65200  125.40300 91.54900  1.000 46.29784  ? 567 PHE A CE1  1 
ATOM   2997 C CE2  . PHE A 1 567 ? 86.58200  125.58000 89.36100  1.000 44.09247  ? 567 PHE A CE2  1 
ATOM   2998 C CZ   . PHE A 1 567 ? 86.70800  125.21900 90.68500  1.000 41.29529  ? 567 PHE A CZ   1 
ATOM   2999 N N    . LYS A 1 568 ? 81.80200  129.76100 90.11300  1.000 62.27150  ? 568 LYS A N    1 
ATOM   3000 C CA   . LYS A 1 568 ? 81.08700  130.97400 89.74700  1.000 58.95197  ? 568 LYS A CA   1 
ATOM   3001 C C    . LYS A 1 568 ? 80.92600  131.07800 88.23500  1.000 62.24401  ? 568 LYS A C    1 
ATOM   3002 O O    . LYS A 1 568 ? 81.78900  130.65500 87.46200  1.000 66.60677  ? 568 LYS A O    1 
ATOM   3003 C CB   . LYS A 1 568 ? 81.82400  132.20100 90.28200  1.000 60.32830  ? 568 LYS A CB   1 
ATOM   3004 C CG   . LYS A 1 568 ? 81.48500  133.49900 89.57700  1.000 62.79203  ? 568 LYS A CG   1 
ATOM   3005 C CD   . LYS A 1 568 ? 82.27500  134.65700 90.16200  1.000 64.90547  ? 568 LYS A CD   1 
ATOM   3006 C CE   . LYS A 1 568 ? 83.74800  134.55600 89.80100  1.000 65.48346  ? 568 LYS A CE   1 
ATOM   3007 N NZ   . LYS A 1 568 ? 84.62600  134.65900 91.00000  1.000 65.50710  ? 568 LYS A NZ   1 
ATOM   3008 N N    . GLU A 1 569 ? 79.80600  131.65700 87.81800  1.000 74.84361  ? 569 GLU A N    1 
ATOM   3009 C CA   . GLU A 1 569 ? 79.57700  131.90100 86.40400  1.000 74.04809  ? 569 GLU A CA   1 
ATOM   3010 C C    . GLU A 1 569 ? 80.60500  132.90200 85.87800  1.000 77.67891  ? 569 GLU A C    1 
ATOM   3011 O O    . GLU A 1 569 ? 80.90200  133.89700 86.55000  1.000 77.98896  ? 569 GLU A O    1 
ATOM   3012 C CB   . GLU A 1 569 ? 78.16100  132.43400 86.17800  1.000 74.91639  ? 569 GLU A CB   1 
ATOM   3013 C CG   . GLU A 1 569 ? 77.60100  132.17000 84.79200  1.000 76.29546  ? 569 GLU A CG   1 
ATOM   3014 C CD   . GLU A 1 569 ? 77.47600  130.69100 84.48800  1.000 78.37621  ? 569 GLU A CD   1 
ATOM   3015 O OE1  . GLU A 1 569 ? 77.34900  129.89600 85.44200  1.000 76.78765  ? 569 GLU A OE1  1 
ATOM   3016 O OE2  . GLU A 1 569 ? 77.50200  130.32300 83.29500  1.000 79.31369  ? 569 GLU A OE2  1 
ATOM   3017 N N    . PRO A 1 570 ? 81.16600  132.67600 84.69200  1.000 81.46049  ? 570 PRO A N    1 
ATOM   3018 C CA   . PRO A 1 570 ? 82.11200  133.64900 84.14100  1.000 80.81407  ? 570 PRO A CA   1 
ATOM   3019 C C    . PRO A 1 570 ? 81.44600  134.99400 83.89100  1.000 82.09712  ? 570 PRO A C    1 
ATOM   3020 O O    . PRO A 1 570 ? 80.28700  135.06700 83.47600  1.000 83.27975  ? 570 PRO A O    1 
ATOM   3021 C CB   . PRO A 1 570 ? 82.58700  132.98500 82.84400  1.000 78.19432  ? 570 PRO A CB   1 
ATOM   3022 C CG   . PRO A 1 570 ? 81.51600  131.97100 82.49400  1.000 79.01473  ? 570 PRO A CG   1 
ATOM   3023 C CD   . PRO A 1 570 ? 80.51400  131.90900 83.62000  1.000 78.71540  ? 570 PRO A CD   1 
ATOM   3024 N N    . GLU A 1 571 ? 82.19300  136.06200 84.14600  1.000 85.48678  ? 571 GLU A N    1 
ATOM   3025 C CA   . GLU A 1 571 ? 81.67100  137.41500 83.99300  1.000 87.32364  ? 571 GLU A CA   1 
ATOM   3026 C C    . GLU A 1 571 ? 81.51500  137.78100 82.52100  1.000 88.72983  ? 571 GLU A C    1 
ATOM   3027 O O    . GLU A 1 571 ? 80.63700  138.56200 82.15600  1.000 87.45214  ? 571 GLU A O    1 
ATOM   3028 C CB   . GLU A 1 571 ? 82.58300  138.42400 84.69200  1.000 85.61304  ? 571 GLU A CB   1 
ATOM   3029 N N    . ALA B 1 77  ? 100.94700 88.49600  106.35900 1.000 86.85962  ? 77  ALA B N    1 
ATOM   3030 C CA   . ALA B 1 77  ? 101.39500 88.03900  107.66800 1.000 87.72369  ? 77  ALA B CA   1 
ATOM   3031 C C    . ALA B 1 77  ? 102.27900 86.80400  107.54100 1.000 87.65092  ? 77  ALA B C    1 
ATOM   3032 O O    . ALA B 1 77  ? 103.43400 86.89600  107.12500 1.000 88.23930  ? 77  ALA B O    1 
ATOM   3033 C CB   . ALA B 1 77  ? 100.20300 87.74700  108.56500 1.000 87.11218  ? 77  ALA B CB   1 
ATOM   3034 N N    . TRP B 1 78  ? 101.73000 85.65000  107.92500 1.000 89.04064  ? 78  TRP B N    1 
ATOM   3035 C CA   . TRP B 1 78  ? 102.48400 84.40300  107.84100 1.000 88.86273  ? 78  TRP B CA   1 
ATOM   3036 C C    . TRP B 1 78  ? 103.01300 84.17600  106.43000 1.000 88.84988  ? 78  TRP B C    1 
ATOM   3037 O O    . TRP B 1 78  ? 104.13400 83.68500  106.25100 1.000 88.33258  ? 78  TRP B O    1 
ATOM   3038 C CB   . TRP B 1 78  ? 101.60700 83.23500  108.30700 1.000 89.13878  ? 78  TRP B CB   1 
ATOM   3039 C CG   . TRP B 1 78  ? 102.02600 81.86300  107.83100 1.000 89.28143  ? 78  TRP B CG   1 
ATOM   3040 C CD1  . TRP B 1 78  ? 101.99300 81.38100  106.55100 1.000 89.30370  ? 78  TRP B CD1  1 
ATOM   3041 C CD2  . TRP B 1 78  ? 102.54800 80.80300  108.64200 1.000 89.59898  ? 78  TRP B CD2  1 
ATOM   3042 N NE1  . TRP B 1 78  ? 102.45800 80.08900  106.52000 1.000 90.27648  ? 78  TRP B NE1  1 
ATOM   3043 C CE2  . TRP B 1 78  ? 102.80600 79.71100  107.79000 1.000 91.21129  ? 78  TRP B CE2  1 
ATOM   3044 C CE3  . TRP B 1 78  ? 102.82100 80.67200  110.00700 1.000 89.52627  ? 78  TRP B CE3  1 
ATOM   3045 C CZ2  . TRP B 1 78  ? 103.32300 78.50500  108.25700 1.000 90.24665  ? 78  TRP B CZ2  1 
ATOM   3046 C CZ3  . TRP B 1 78  ? 103.33500 79.47400  110.46900 1.000 89.89016  ? 78  TRP B CZ3  1 
ATOM   3047 C CH2  . TRP B 1 78  ? 103.58000 78.40700  109.59700 1.000 89.69107  ? 78  TRP B CH2  1 
ATOM   3048 N N    . GLU B 1 79  ? 102.20000 84.47900  105.41500 1.000 84.65363  ? 79  GLU B N    1 
ATOM   3049 C CA   . GLU B 1 79  ? 102.66600 84.35600  104.03800 1.000 84.27338  ? 79  GLU B CA   1 
ATOM   3050 C C    . GLU B 1 79  ? 103.87700 85.24300  103.77800 1.000 84.65679  ? 79  GLU B C    1 
ATOM   3051 O O    . GLU B 1 79  ? 104.80100 84.85000  103.05400 1.000 85.14022  ? 79  GLU B O    1 
ATOM   3052 C CB   . GLU B 1 79  ? 101.53300 84.69700  103.07000 1.000 83.71259  ? 79  GLU B CB   1 
ATOM   3053 N N    . MET B 1 80  ? 103.90800 86.43500  104.38000 1.000 83.29267  ? 80  MET B N    1 
ATOM   3054 C CA   . MET B 1 80  ? 105.06000 87.31100  104.19800 1.000 82.90313  ? 80  MET B CA   1 
ATOM   3055 C C    . MET B 1 80  ? 106.27500 86.79900  104.95600 1.000 81.64958  ? 80  MET B C    1 
ATOM   3056 O O    . MET B 1 80  ? 107.41000 86.97100  104.49700 1.000 79.00371  ? 80  MET B O    1 
ATOM   3057 C CB   . MET B 1 80  ? 104.72100 88.73400  104.64200 1.000 82.70774  ? 80  MET B CB   1 
ATOM   3058 C CG   . MET B 1 80  ? 105.89700 89.48400  105.24900 1.000 84.17326  ? 80  MET B CG   1 
ATOM   3059 S SD   . MET B 1 80  ? 105.48200 91.16400  105.75500 1.000 89.27912  ? 80  MET B SD   1 
ATOM   3060 C CE   . MET B 1 80  ? 105.28500 90.95300  107.52200 1.000 81.55071  ? 80  MET B CE   1 
ATOM   3061 N N    . GLY B 1 81  ? 106.06200 86.17600  106.11400 1.000 74.01248  ? 81  GLY B N    1 
ATOM   3062 C CA   . GLY B 1 81  ? 107.18000 85.60400  106.84400 1.000 73.83204  ? 81  GLY B CA   1 
ATOM   3063 C C    . GLY B 1 81  ? 107.78400 84.41500  106.12500 1.000 75.71443  ? 81  GLY B C    1 
ATOM   3064 O O    . GLY B 1 81  ? 109.00600 84.24600  106.10100 1.000 75.51847  ? 81  GLY B O    1 
ATOM   3065 N N    . VAL B 1 82  ? 106.93700 83.57400  105.53000 1.000 81.61400  ? 82  VAL B N    1 
ATOM   3066 C CA   . VAL B 1 82  ? 107.43400 82.43700  104.76100 1.000 81.10477  ? 82  VAL B CA   1 
ATOM   3067 C C    . VAL B 1 82  ? 108.10500 82.91300  103.47900 1.000 79.52587  ? 82  VAL B C    1 
ATOM   3068 O O    . VAL B 1 82  ? 109.09700 82.32800  103.02800 1.000 79.39306  ? 82  VAL B O    1 
ATOM   3069 C CB   . VAL B 1 82  ? 106.29600 81.44200  104.47100 1.000 81.24786  ? 82  VAL B CB   1 
ATOM   3070 C CG1  . VAL B 1 82  ? 105.70500 80.91900  105.77100 1.000 81.09881  ? 82  VAL B CG1  1 
ATOM   3071 C CG2  . VAL B 1 82  ? 105.22400 82.09200  103.61500 1.000 80.85911  ? 82  VAL B CG2  1 
ATOM   3072 N N    . SER B 1 83  ? 107.57800 83.97800  102.86900 1.000 76.92729  ? 83  SER B N    1 
ATOM   3073 C CA   . SER B 1 83  ? 108.19700 84.51800  101.66300 1.000 77.50789  ? 83  SER B CA   1 
ATOM   3074 C C    . SER B 1 83  ? 109.58400 85.07600  101.95900 1.000 78.83577  ? 83  SER B C    1 
ATOM   3075 O O    . SER B 1 83  ? 110.54900 84.77600  101.24700 1.000 76.80236  ? 83  SER B O    1 
ATOM   3076 C CB   . SER B 1 83  ? 107.30000 85.59500  101.05300 1.000 76.49705  ? 83  SER B CB   1 
ATOM   3077 O OG   . SER B 1 83  ? 107.84400 86.08500  99.84100  1.000 77.06556  ? 83  SER B OG   1 
ATOM   3078 N N    . ASP B 1 84  ? 109.70200 85.88900  103.00200 1.000 73.16040  ? 84  ASP B N    1 
ATOM   3079 C CA   . ASP B 1 84  ? 110.98100 86.48000  103.39700 1.000 68.98115  ? 84  ASP B CA   1 
ATOM   3080 C C    . ASP B 1 84  ? 111.29900 86.12800  104.84200 1.000 66.62633  ? 84  ASP B C    1 
ATOM   3081 O O    . ASP B 1 84  ? 110.62200 86.62900  105.76000 1.000 67.57015  ? 84  ASP B O    1 
ATOM   3082 C CB   . ASP B 1 84  ? 110.95100 87.99700  103.21500 1.000 65.34414  ? 84  ASP B CB   1 
ATOM   3083 C CG   . ASP B 1 84  ? 112.33800 88.60000  103.13000 1.000 68.94774  ? 84  ASP B CG   1 
ATOM   3084 O OD1  . ASP B 1 84  ? 113.30800 87.83800  102.93900 1.000 69.84651  ? 84  ASP B OD1  1 
ATOM   3085 O OD2  . ASP B 1 84  ? 112.45800 89.83700  103.25100 1.000 71.70168  ? 84  ASP B OD2  1 
ATOM   3086 N N    . PRO B 1 85  ? 112.30300 85.28900  105.10500 1.000 52.86289  ? 85  PRO B N    1 
ATOM   3087 C CA   . PRO B 1 85  ? 112.63300 84.93300  106.48900 1.000 54.34409  ? 85  PRO B CA   1 
ATOM   3088 C C    . PRO B 1 85  ? 113.55200 85.92600  107.18000 1.000 52.49437  ? 85  PRO B C    1 
ATOM   3089 O O    . PRO B 1 85  ? 113.86000 85.73800  108.36200 1.000 53.47007  ? 85  PRO B O    1 
ATOM   3090 C CB   . PRO B 1 85  ? 113.32100 83.57200  106.32800 1.000 53.01692  ? 85  PRO B CB   1 
ATOM   3091 C CG   . PRO B 1 85  ? 113.98500 83.66100  104.99800 1.000 52.24472  ? 85  PRO B CG   1 
ATOM   3092 C CD   . PRO B 1 85  ? 113.11600 84.54000  104.13000 1.000 52.84427  ? 85  PRO B CD   1 
ATOM   3093 N N    . ARG B 1 86  ? 113.99800 86.97100  106.48200 1.000 41.01480  ? 86  ARG B N    1 
ATOM   3094 C CA   . ARG B 1 86  ? 114.83900 87.99100  107.09200 1.000 36.88679  ? 86  ARG B CA   1 
ATOM   3095 C C    . ARG B 1 86  ? 114.06700 88.89300  108.04400 1.000 39.57303  ? 86  ARG B C    1 
ATOM   3096 O O    . ARG B 1 86  ? 114.69100 89.61400  108.82900 1.000 45.54242  ? 86  ARG B O    1 
ATOM   3097 C CB   . ARG B 1 86  ? 115.51200 88.83000  106.00400 1.000 39.02815  ? 86  ARG B CB   1 
ATOM   3098 C CG   . ARG B 1 86  ? 116.95600 89.17900  106.30500 1.000 38.31927  ? 86  ARG B CG   1 
ATOM   3099 C CD   . ARG B 1 86  ? 117.63500 89.85200  105.12400 1.000 38.95081  ? 86  ARG B CD   1 
ATOM   3100 N NE   . ARG B 1 86  ? 116.80800 90.88000  104.50500 1.000 38.31766  ? 86  ARG B NE   1 
ATOM   3101 C CZ   . ARG B 1 86  ? 117.27800 91.84400  103.72600 1.000 35.50024  ? 86  ARG B CZ   1 
ATOM   3102 N NH1  . ARG B 1 86  ? 118.56800 91.94500  103.45500 1.000 39.35957  ? 86  ARG B NH1  1 
ATOM   3103 N NH2  . ARG B 1 86  ? 116.43400 92.73000  103.20700 1.000 30.78592  ? 86  ARG B NH2  1 
ATOM   3104 N N    . LYS B 1 87  ? 112.73600 88.86700  107.99600 1.000 37.24438  ? 87  LYS B N    1 
ATOM   3105 C CA   . LYS B 1 87  ? 111.89600 89.70800  108.83500 1.000 30.20644  ? 87  LYS B CA   1 
ATOM   3106 C C    . LYS B 1 87  ? 111.41300 88.99700  110.09000 1.000 27.67642  ? 87  LYS B C    1 
ATOM   3107 O O    . LYS B 1 87  ? 110.74700 89.62000  110.92100 1.000 31.47945  ? 87  LYS B O    1 
ATOM   3108 C CB   . LYS B 1 87  ? 110.69100 90.20900  108.03300 1.000 30.17067  ? 87  LYS B CB   1 
ATOM   3109 C CG   . LYS B 1 87  ? 111.05200 91.11100  106.86700 1.000 33.01755  ? 87  LYS B CG   1 
ATOM   3110 C CD   . LYS B 1 87  ? 109.87500 91.97600  106.45300 1.000 32.36580  ? 87  LYS B CD   1 
ATOM   3111 C CE   . LYS B 1 87  ? 110.30000 93.04300  105.45800 1.000 35.57476  ? 87  LYS B CE   1 
ATOM   3112 N NZ   . LYS B 1 87  ? 109.14700 93.57800  104.68500 1.000 31.33689  ? 87  LYS B NZ   1 
ATOM   3113 N N    . ILE B 1 88  ? 111.73700 87.71200  110.25000 1.000 31.14130  ? 88  ILE B N    1 
ATOM   3114 C CA   . ILE B 1 88  ? 111.36700 86.96300  111.44600 1.000 27.81866  ? 88  ILE B CA   1 
ATOM   3115 C C    . ILE B 1 88  ? 112.52000 86.85700  112.43100 1.000 31.48030  ? 88  ILE B C    1 
ATOM   3116 O O    . ILE B 1 88  ? 112.29500 86.50600  113.60100 1.000 39.94249  ? 88  ILE B O    1 
ATOM   3117 C CB   . ILE B 1 88  ? 110.84900 85.55500  111.07600 1.000 31.55217  ? 88  ILE B CB   1 
ATOM   3118 C CG1  . ILE B 1 88  ? 109.46700 85.64800  110.43000 1.000 33.47067  ? 88  ILE B CG1  1 
ATOM   3119 C CG2  . ILE B 1 88  ? 110.79000 84.65100  112.29500 1.000 32.20965  ? 88  ILE B CG2  1 
ATOM   3120 C CD1  . ILE B 1 88  ? 109.23300 84.62100  109.34900 1.000 35.06996  ? 88  ILE B CD1  1 
ATOM   3121 N N    . VAL B 1 89  ? 113.73900 87.18100  112.01000 1.000 29.35862  ? 89  VAL B N    1 
ATOM   3122 C CA   . VAL B 1 89  ? 114.88700 87.15900  112.90500 1.000 27.07710  ? 89  VAL B CA   1 
ATOM   3123 C C    . VAL B 1 89  ? 115.09700 88.51800  113.56700 1.000 24.13602  ? 89  VAL B C    1 
ATOM   3124 O O    . VAL B 1 89  ? 115.51800 88.58200  114.72600 1.000 30.08062  ? 89  VAL B O    1 
ATOM   3125 C CB   . VAL B 1 89  ? 116.14400 86.71200  112.13900 1.000 29.22736  ? 89  VAL B CB   1 
ATOM   3126 C CG1  . VAL B 1 89  ? 117.35700 86.70100  113.05600 1.000 29.96916  ? 89  VAL B CG1  1 
ATOM   3127 C CG2  . VAL B 1 89  ? 115.92600 85.34300  111.52100 1.000 22.32021  ? 89  VAL B CG2  1 
ATOM   3128 N N    . PHE B 1 90  ? 114.80200 89.60600  112.85300 1.000 14.06827  ? 90  PHE B N    1 
ATOM   3129 C CA   . PHE B 1 90  ? 114.90900 90.94300  113.42800 1.000 16.99943  ? 90  PHE B CA   1 
ATOM   3130 C C    . PHE B 1 90  ? 113.95200 91.12000  114.60500 1.000 16.49049  ? 90  PHE B C    1 
ATOM   3131 O O    . PHE B 1 90  ? 114.32800 91.67000  115.65200 1.000 21.45977  ? 90  PHE B O    1 
ATOM   3132 C CB   . PHE B 1 90  ? 114.63300 91.97500  112.33100 1.000 9.75022   ? 90  PHE B CB   1 
ATOM   3133 C CG   . PHE B 1 90  ? 114.82900 93.40000  112.75700 1.000 23.11477  ? 90  PHE B CG   1 
ATOM   3134 C CD1  . PHE B 1 90  ? 116.09200 93.88200  113.04800 1.000 19.79238  ? 90  PHE B CD1  1 
ATOM   3135 C CD2  . PHE B 1 90  ? 113.75300 94.26500  112.84300 1.000 16.49352  ? 90  PHE B CD2  1 
ATOM   3136 C CE1  . PHE B 1 90  ? 116.27400 95.19200  113.43100 1.000 18.53096  ? 90  PHE B CE1  1 
ATOM   3137 C CE2  . PHE B 1 90  ? 113.93200 95.57600  113.22600 1.000 8.86768   ? 90  PHE B CE2  1 
ATOM   3138 C CZ   . PHE B 1 90  ? 115.19300 96.03900  113.52000 1.000 12.40216  ? 90  PHE B CZ   1 
ATOM   3139 N N    . SER B 1 91  ? 112.71300 90.64300  114.45800 1.000 10.91977  ? 91  SER B N    1 
ATOM   3140 C CA   . SER B 1 91  ? 111.73300 90.75800  115.53300 1.000 12.14410  ? 91  SER B CA   1 
ATOM   3141 C C    . SER B 1 91  ? 112.14400 89.94500  116.75400 1.000 16.85307  ? 91  SER B C    1 
ATOM   3142 O O    . SER B 1 91  ? 111.97800 90.39500  117.89600 1.000 25.02186  ? 91  SER B O    1 
ATOM   3143 C CB   . SER B 1 91  ? 110.36100 90.31200  115.03200 1.000 14.75671  ? 91  SER B CB   1 
ATOM   3144 O OG   . SER B 1 91  ? 110.04400 90.93500  113.80100 1.000 14.93524  ? 91  SER B OG   1 
ATOM   3145 N N    . ALA B 1 92  ? 112.72600 88.76400  116.53800 1.000 12.92865  ? 92  ALA B N    1 
ATOM   3146 C CA   . ALA B 1 92  ? 113.15900 87.95300  117.66900 1.000 10.15941  ? 92  ALA B CA   1 
ATOM   3147 C C    . ALA B 1 92  ? 114.41100 88.52700  118.31500 1.000 16.98807  ? 92  ALA B C    1 
ATOM   3148 O O    . ALA B 1 92  ? 114.60300 88.38000  119.52500 1.000 24.38729  ? 92  ALA B O    1 
ATOM   3149 C CB   . ALA B 1 92  ? 113.39400 86.51100  117.22400 1.000 13.11792  ? 92  ALA B CB   1 
ATOM   3150 N N    . LYS B 1 93  ? 115.24700 89.21900  117.54200 1.000 10.07950  ? 93  LYS B N    1 
ATOM   3151 C CA   . LYS B 1 93  ? 116.40500 89.88500  118.12800 1.000 8.37425   ? 93  LYS B CA   1 
ATOM   3152 C C    . LYS B 1 93  ? 115.97500 91.05200  119.01000 1.000 11.06505  ? 93  LYS B C    1 
ATOM   3153 O O    . LYS B 1 93  ? 116.53000 91.26000  120.09900 1.000 25.94677  ? 93  LYS B O    1 
ATOM   3154 C CB   . LYS B 1 93  ? 117.34000 90.35700  117.01700 1.000 22.88220  ? 93  LYS B CB   1 
ATOM   3155 C CG   . LYS B 1 93  ? 118.09600 89.23200  116.33200 1.000 20.53539  ? 93  LYS B CG   1 
ATOM   3156 C CD   . LYS B 1 93  ? 119.44000 89.70000  115.81800 1.000 17.49249  ? 93  LYS B CD   1 
ATOM   3157 C CE   . LYS B 1 93  ? 119.28700 90.83300  114.82600 1.000 13.40647  ? 93  LYS B CE   1 
ATOM   3158 N NZ   . LYS B 1 93  ? 120.48000 90.95600  113.95000 1.000 13.57932  ? 93  LYS B NZ   1 
ATOM   3159 N N    . ILE B 1 94  ? 114.96600 91.80600  118.57100 1.000 4.54048   ? 94  ILE B N    1 
ATOM   3160 C CA   . ILE B 1 94  ? 114.43900 92.87500  119.41600 1.000 7.86079   ? 94  ILE B CA   1 
ATOM   3161 C C    . ILE B 1 94  ? 113.80100 92.29600  120.67400 1.000 21.70423  ? 94  ILE B C    1 
ATOM   3162 O O    . ILE B 1 94  ? 113.99300 92.81800  121.78200 1.000 29.57037  ? 94  ILE B O    1 
ATOM   3163 C CB   . ILE B 1 94  ? 113.45100 93.75300  118.62700 1.000 17.59954  ? 94  ILE B CB   1 
ATOM   3164 C CG1  . ILE B 1 94  ? 114.11400 94.28700  117.35800 1.000 16.62742  ? 94  ILE B CG1  1 
ATOM   3165 C CG2  . ILE B 1 94  ? 112.94000 94.89400  119.49000 1.000 12.34003  ? 94  ILE B CG2  1 
ATOM   3166 C CD1  . ILE B 1 94  ? 113.23100 95.20900  116.55800 1.000 17.17545  ? 94  ILE B CD1  1 
ATOM   3167 N N    . GLY B 1 95  ? 113.04100 91.20800  120.53200 1.000 11.87416  ? 95  GLY B N    1 
ATOM   3168 C CA   . GLY B 1 95  ? 112.46600 90.57500  121.70700 1.000 5.94027   ? 95  GLY B CA   1 
ATOM   3169 C C    . GLY B 1 95  ? 113.52000 90.08100  122.68100 1.000 17.32051  ? 95  GLY B C    1 
ATOM   3170 O O    . GLY B 1 95  ? 113.35700 90.19700  123.89800 1.000 19.64453  ? 95  GLY B O    1 
ATOM   3171 N N    . LEU B 1 96  ? 114.63200 89.55400  122.16000 1.000 15.09833  ? 96  LEU B N    1 
ATOM   3172 C CA   . LEU B 1 96  ? 115.70000 89.06300  123.02500 1.000 14.72220  ? 96  LEU B CA   1 
ATOM   3173 C C    . LEU B 1 96  ? 116.39200 90.20100  123.76700 1.000 18.27564  ? 96  LEU B C    1 
ATOM   3174 O O    . LEU B 1 96  ? 116.66400 90.09000  124.97000 1.000 28.00745  ? 96  LEU B O    1 
ATOM   3175 C CB   . LEU B 1 96  ? 116.71100 88.26900  122.19900 1.000 18.31438  ? 96  LEU B CB   1 
ATOM   3176 C CG   . LEU B 1 96  ? 117.96700 87.77400  122.91900 1.000 27.38252  ? 96  LEU B CG   1 
ATOM   3177 C CD1  . LEU B 1 96  ? 117.65000 86.56500  123.78400 1.000 24.18660  ? 96  LEU B CD1  1 
ATOM   3178 C CD2  . LEU B 1 96  ? 119.06400 87.45100  121.91800 1.000 13.30344  ? 96  LEU B CD2  1 
ATOM   3179 N N    . ALA B 1 97  ? 116.66900 91.31200  123.08000 1.000 12.18990  ? 97  ALA B N    1 
ATOM   3180 C CA   . ALA B 1 97  ? 117.28200 92.44700  123.76600 1.000 19.60129  ? 97  ALA B CA   1 
ATOM   3181 C C    . ALA B 1 97  ? 116.35900 92.99100  124.85000 1.000 22.52992  ? 97  ALA B C    1 
ATOM   3182 O O    . ALA B 1 97  ? 116.80200 93.30800  125.96900 1.000 16.14155  ? 97  ALA B O    1 
ATOM   3183 C CB   . ALA B 1 97  ? 117.63800 93.54000  122.76000 1.000 14.18455  ? 97  ALA B CB   1 
ATOM   3184 N N    . LEU B 1 98  ? 115.06500 93.09500  124.54100 1.000 18.70636  ? 98  LEU B N    1 
ATOM   3185 C CA   . LEU B 1 98  ? 114.11400 93.60900  125.51700 1.000 11.69815  ? 98  LEU B CA   1 
ATOM   3186 C C    . LEU B 1 98  ? 114.02500 92.68500  126.72600 1.000 16.33265  ? 98  LEU B C    1 
ATOM   3187 O O    . LEU B 1 98  ? 114.01300 93.14900  127.87300 1.000 22.93773  ? 98  LEU B O    1 
ATOM   3188 C CB   . LEU B 1 98  ? 112.74500 93.77700  124.86000 1.000 18.09511  ? 98  LEU B CB   1 
ATOM   3189 C CG   . LEU B 1 98  ? 112.37600 95.17900  124.36900 1.000 16.08827  ? 98  LEU B CG   1 
ATOM   3190 C CD1  . LEU B 1 98  ? 111.05100 95.14700  123.62500 1.000 16.51438  ? 98  LEU B CD1  1 
ATOM   3191 C CD2  . LEU B 1 98  ? 112.33800 96.17900  125.50500 1.000 18.31969  ? 98  LEU B CD2  1 
ATOM   3192 N N    . THR B 1 99  ? 113.98200 91.36900  126.48800 1.000 20.24672  ? 99  THR B N    1 
ATOM   3193 C CA   . THR B 1 99  ? 113.93200 90.41400  127.59000 1.000 21.01604  ? 99  THR B CA   1 
ATOM   3194 C C    . THR B 1 99  ? 115.19200 90.46800  128.44400 1.000 26.66559  ? 99  THR B C    1 
ATOM   3195 O O    . THR B 1 99  ? 115.11400 90.32800  129.67000 1.000 34.05275  ? 99  THR B O    1 
ATOM   3196 C CB   . THR B 1 99  ? 113.72000 89.00100  127.04500 1.000 24.25876  ? 99  THR B CB   1 
ATOM   3197 O OG1  . THR B 1 99  ? 112.32900 88.79700  126.77400 1.000 27.34912  ? 99  THR B OG1  1 
ATOM   3198 C CG2  . THR B 1 99  ? 114.18800 87.96500  128.05100 1.000 26.82068  ? 99  THR B CG2  1 
ATOM   3199 N N    . ILE B 1 100 ? 116.35200 90.71300  127.83200 1.000 21.24606  ? 100 ILE B N    1 
ATOM   3200 C CA   . ILE B 1 100 ? 117.57700 90.80800  128.62000 1.000 26.96673  ? 100 ILE B CA   1 
ATOM   3201 C C    . ILE B 1 100 ? 117.50700 92.01700  129.54300 1.000 32.33726  ? 100 ILE B C    1 
ATOM   3202 O O    . ILE B 1 100 ? 117.78500 91.92200  130.75000 1.000 33.96822  ? 100 ILE B O    1 
ATOM   3203 C CB   . ILE B 1 100 ? 118.81400 90.87000  127.70500 1.000 27.72197  ? 100 ILE B CB   1 
ATOM   3204 C CG1  . ILE B 1 100 ? 119.05600 89.51900  127.03200 1.000 27.38372  ? 100 ILE B CG1  1 
ATOM   3205 C CG2  . ILE B 1 100 ? 120.03900 91.29900  128.49500 1.000 23.67541  ? 100 ILE B CG2  1 
ATOM   3206 C CD1  . ILE B 1 100 ? 120.05700 89.57500  125.90200 1.000 25.86500  ? 100 ILE B CD1  1 
ATOM   3207 N N    . VAL B 1 101 ? 117.16300 93.18200  128.98700 1.000 28.95447  ? 101 VAL B N    1 
ATOM   3208 C CA   . VAL B 1 101 ? 117.13500 94.37400  129.82800 1.000 24.34140  ? 101 VAL B CA   1 
ATOM   3209 C C    . VAL B 1 101 ? 116.09300 94.20800  130.92900 1.000 25.71313  ? 101 VAL B C    1 
ATOM   3210 O O    . VAL B 1 101 ? 116.29500 94.64500  132.07100 1.000 23.27934  ? 101 VAL B O    1 
ATOM   3211 C CB   . VAL B 1 101 ? 116.87900 95.63300  128.98000 1.000 22.32536  ? 101 VAL B CB   1 
ATOM   3212 C CG1  . VAL B 1 101 ? 116.34000 96.75000  129.85000 1.000 18.16715  ? 101 VAL B CG1  1 
ATOM   3213 C CG2  . VAL B 1 101 ? 118.15800 96.06900  128.29000 1.000 18.33528  ? 101 VAL B CG2  1 
ATOM   3214 N N    . ALA B 1 102 ? 114.97200 93.54700  130.61700 1.000 35.59511  ? 102 ALA B N    1 
ATOM   3215 C CA   . ALA B 1 102 ? 113.93400 93.37100  131.62600 1.000 29.50445  ? 102 ALA B CA   1 
ATOM   3216 C C    . ALA B 1 102 ? 114.41900 92.46200  132.74700 1.000 34.18451  ? 102 ALA B C    1 
ATOM   3217 O O    . ALA B 1 102 ? 114.11800 92.69800  133.92500 1.000 41.75955  ? 102 ALA B O    1 
ATOM   3218 C CB   . ALA B 1 102 ? 112.66500 92.81200  130.98700 1.000 27.00330  ? 102 ALA B CB   1 
ATOM   3219 N N    . LEU B 1 103 ? 115.14600 91.39700  132.39700 1.000 34.06248  ? 103 LEU B N    1 
ATOM   3220 C CA   . LEU B 1 103 ? 115.65700 90.50100  133.42600 1.000 36.91796  ? 103 LEU B CA   1 
ATOM   3221 C C    . LEU B 1 103 ? 116.64200 91.22600  134.32800 1.000 41.83306  ? 103 LEU B C    1 
ATOM   3222 O O    . LEU B 1 103 ? 116.65000 91.01900  135.54800 1.000 44.55932  ? 103 LEU B O    1 
ATOM   3223 C CB   . LEU B 1 103 ? 116.30800 89.27400  132.79000 1.000 37.70876  ? 103 LEU B CB   1 
ATOM   3224 C CG   . LEU B 1 103 ? 115.35700 88.16800  132.33100 1.000 39.95982  ? 103 LEU B CG   1 
ATOM   3225 C CD1  . LEU B 1 103 ? 116.13700 86.99200  131.77100 1.000 40.41001  ? 103 LEU B CD1  1 
ATOM   3226 C CD2  . LEU B 1 103 ? 114.46700 87.72400  133.47900 1.000 37.01987  ? 103 LEU B CD2  1 
ATOM   3227 N N    . LEU B 1 104 ? 117.46700 92.10600  133.74900 1.000 46.23117  ? 104 LEU B N    1 
ATOM   3228 C CA   . LEU B 1 104 ? 118.40300 92.85400  134.58300 1.000 40.24242  ? 104 LEU B CA   1 
ATOM   3229 C C    . LEU B 1 104 ? 117.70400 93.90700  135.43100 1.000 41.24421  ? 104 LEU B C    1 
ATOM   3230 O O    . LEU B 1 104 ? 118.22700 94.28500  136.48400 1.000 42.66374  ? 104 LEU B O    1 
ATOM   3231 C CB   . LEU B 1 104 ? 119.48400 93.52100  133.73100 1.000 39.18920  ? 104 LEU B CB   1 
ATOM   3232 C CG   . LEU B 1 104 ? 120.20800 92.66400  132.69500 1.000 44.74706  ? 104 LEU B CG   1 
ATOM   3233 C CD1  . LEU B 1 104 ? 120.79900 93.54100  131.60500 1.000 42.18108  ? 104 LEU B CD1  1 
ATOM   3234 C CD2  . LEU B 1 104 ? 121.29100 91.83900  133.36500 1.000 43.21185  ? 104 LEU B CD2  1 
ATOM   3235 N N    . ILE B 1 105 ? 116.53600 94.38400  135.00000 1.000 45.36009  ? 105 ILE B N    1 
ATOM   3236 C CA   . ILE B 1 105 ? 115.79600 95.35100  135.80700 1.000 47.54567  ? 105 ILE B CA   1 
ATOM   3237 C C    . ILE B 1 105 ? 115.09600 94.66500  136.97400 1.000 43.52321  ? 105 ILE B C    1 
ATOM   3238 O O    . ILE B 1 105 ? 115.08000 95.18700  138.09400 1.000 47.77245  ? 105 ILE B O    1 
ATOM   3239 C CB   . ILE B 1 105 ? 114.80100 96.14300  134.93900 1.000 47.83416  ? 105 ILE B CB   1 
ATOM   3240 C CG1  . ILE B 1 105 ? 115.54600 97.02500  133.93500 1.000 42.76207  ? 105 ILE B CG1  1 
ATOM   3241 C CG2  . ILE B 1 105 ? 113.88200 96.98100  135.81100 1.000 42.98397  ? 105 ILE B CG2  1 
ATOM   3242 C CD1  . ILE B 1 105 ? 114.64900 97.63100  132.87700 1.000 39.91844  ? 105 ILE B CD1  1 
ATOM   3243 N N    . PHE B 1 106 ? 114.50400 93.49300  136.73700 1.000 50.24286  ? 106 PHE B N    1 
ATOM   3244 C CA   . PHE B 1 106 ? 113.83000 92.77800  137.81900 1.000 49.13023  ? 106 PHE B CA   1 
ATOM   3245 C C    . PHE B 1 106 ? 114.81300 92.15200  138.80600 1.000 51.28984  ? 106 PHE B C    1 
ATOM   3246 O O    . PHE B 1 106 ? 114.58200 92.19100  140.02000 1.000 53.86507  ? 106 PHE B O    1 
ATOM   3247 C CB   . PHE B 1 106 ? 112.90200 91.70100  137.25400 1.000 47.02240  ? 106 PHE B CB   1 
ATOM   3248 C CG   . PHE B 1 106 ? 111.69700 92.24400  136.54200 1.000 50.28490  ? 106 PHE B CG   1 
ATOM   3249 C CD1  . PHE B 1 106 ? 111.11600 93.43400  136.94300 1.000 52.23635  ? 106 PHE B CD1  1 
ATOM   3250 C CD2  . PHE B 1 106 ? 111.13700 91.55700  135.47900 1.000 48.89070  ? 106 PHE B CD2  1 
ATOM   3251 C CE1  . PHE B 1 106 ? 110.00300 93.93100  136.29300 1.000 49.47671  ? 106 PHE B CE1  1 
ATOM   3252 C CE2  . PHE B 1 106 ? 110.02600 92.05000  134.82500 1.000 49.09549  ? 106 PHE B CE2  1 
ATOM   3253 C CZ   . PHE B 1 106 ? 109.45800 93.23900  135.23300 1.000 47.74076  ? 106 PHE B CZ   1 
ATOM   3254 N N    . TYR B 1 107 ? 115.90800 91.57500  138.32100 1.000 60.56404  ? 107 TYR B N    1 
ATOM   3255 C CA   . TYR B 1 107 ? 116.83100 90.83900  139.18900 1.000 61.59952  ? 107 TYR B CA   1 
ATOM   3256 C C    . TYR B 1 107 ? 118.08700 91.65000  139.51000 1.000 64.74068  ? 107 TYR B C    1 
ATOM   3257 O O    . TYR B 1 107 ? 119.20600 91.27600  139.16200 1.000 64.18151  ? 107 TYR B O    1 
ATOM   3258 C CB   . TYR B 1 107 ? 117.19000 89.49500  138.56100 1.000 61.10404  ? 107 TYR B CB   1 
ATOM   3259 C CG   . TYR B 1 107 ? 116.00100 88.59300  138.32400 1.000 61.75425  ? 107 TYR B CG   1 
ATOM   3260 C CD1  . TYR B 1 107 ? 115.13800 88.26800  139.36000 1.000 62.39983  ? 107 TYR B CD1  1 
ATOM   3261 C CD2  . TYR B 1 107 ? 115.74600 88.06200  137.06800 1.000 63.30170  ? 107 TYR B CD2  1 
ATOM   3262 C CE1  . TYR B 1 107 ? 114.05100 87.44300  139.15200 1.000 62.43746  ? 107 TYR B CE1  1 
ATOM   3263 C CE2  . TYR B 1 107 ? 114.66200 87.23500  136.85100 1.000 63.58918  ? 107 TYR B CE2  1 
ATOM   3264 C CZ   . TYR B 1 107 ? 113.81800 86.93000  137.89600 1.000 62.82818  ? 107 TYR B CZ   1 
ATOM   3265 O OH   . TYR B 1 107 ? 112.73800 86.10600  137.68400 1.000 65.60506  ? 107 TYR B OH   1 
ATOM   3266 N N    . GLN B 1 108 ? 117.89400 92.77900  140.19000 1.000 75.14879  ? 108 GLN B N    1 
ATOM   3267 C CA   . GLN B 1 108 ? 119.00800 93.61300  140.61800 1.000 75.72441  ? 108 GLN B CA   1 
ATOM   3268 C C    . GLN B 1 108 ? 118.82000 94.00000  142.07900 1.000 79.48128  ? 108 GLN B C    1 
ATOM   3269 O O    . GLN B 1 108 ? 117.71700 93.93000  142.62700 1.000 78.08364  ? 108 GLN B O    1 
ATOM   3270 C CB   . GLN B 1 108 ? 119.14500 94.87000  139.74500 1.000 71.85534  ? 108 GLN B CB   1 
ATOM   3271 C CG   . GLN B 1 108 ? 118.70400 96.16300  140.41600 1.000 74.23075  ? 108 GLN B CG   1 
ATOM   3272 C CD   . GLN B 1 108 ? 117.20000 96.26400  140.56900 1.000 76.04550  ? 108 GLN B CD   1 
ATOM   3273 O OE1  . GLN B 1 108 ? 116.51200 95.25800  140.73600 1.000 74.97701  ? 108 GLN B OE1  1 
ATOM   3274 N NE2  . GLN B 1 108 ? 116.68100 97.48500  140.51000 1.000 73.70191  ? 108 GLN B NE2  1 
ATOM   3275 N N    . GLU B 1 109 ? 119.91900 94.40800  142.70700 1.000 94.00514  ? 109 GLU B N    1 
ATOM   3276 C CA   . GLU B 1 109 ? 119.87200 94.80600  144.11100 1.000 92.97608  ? 109 GLU B CA   1 
ATOM   3277 C C    . GLU B 1 109 ? 119.07600 96.09600  144.27100 1.000 92.85372  ? 109 GLU B C    1 
ATOM   3278 O O    . GLU B 1 109 ? 119.34200 97.07500  143.56300 1.000 90.12628  ? 109 GLU B O    1 
ATOM   3279 C CB   . GLU B 1 109 ? 121.28500 94.98300  144.66000 1.000 91.83578  ? 109 GLU B CB   1 
ATOM   3280 C CG   . GLU B 1 109 ? 121.38100 94.88100  146.17400 1.000 91.45031  ? 109 GLU B CG   1 
ATOM   3281 C CD   . GLU B 1 109 ? 120.93600 96.14900  146.87500 1.000 93.31511  ? 109 GLU B CD   1 
ATOM   3282 O OE1  . GLU B 1 109 ? 121.38100 97.24200  146.46700 1.000 93.56887  ? 109 GLU B OE1  1 
ATOM   3283 O OE2  . GLU B 1 109 ? 120.14000 96.05200  147.83200 1.000 92.90018  ? 109 GLU B OE2  1 
ATOM   3284 N N    . PRO B 1 110 ? 118.10400 96.14400  145.18000 1.000 96.56972  ? 110 PRO B N    1 
ATOM   3285 C CA   . PRO B 1 110 ? 117.29100 97.35800  145.32100 1.000 96.43840  ? 110 PRO B CA   1 
ATOM   3286 C C    . PRO B 1 110 ? 118.11300 98.52300  145.85200 1.000 97.23468  ? 110 PRO B C    1 
ATOM   3287 O O    . PRO B 1 110 ? 119.00100 98.35200  146.69000 1.000 95.14264  ? 110 PRO B O    1 
ATOM   3288 C CB   . PRO B 1 110 ? 116.20200 96.94200  146.31600 1.000 95.48021  ? 110 PRO B CB   1 
ATOM   3289 C CG   . PRO B 1 110 ? 116.80700 95.80700  147.07900 1.000 94.67451  ? 110 PRO B CG   1 
ATOM   3290 C CD   . PRO B 1 110 ? 117.66200 95.07300  146.08900 1.000 94.73624  ? 110 PRO B CD   1 
ATOM   3291 N N    . ASN B 1 111 ? 117.80200 99.71800  145.35700 1.000 101.85788 ? 111 ASN B N    1 
ATOM   3292 C CA   . ASN B 1 111 ? 118.45000 100.94500 145.79500 1.000 100.61886 ? 111 ASN B CA   1 
ATOM   3293 C C    . ASN B 1 111 ? 117.45600 102.06700 145.53900 1.000 99.38951  ? 111 ASN B C    1 
ATOM   3294 O O    . ASN B 1 111 ? 116.63900 101.96300 144.61600 1.000 98.52728  ? 111 ASN B O    1 
ATOM   3295 C CB   . ASN B 1 111 ? 119.78900 101.14400 145.04700 1.000 99.98068  ? 111 ASN B CB   1 
ATOM   3296 C CG   . ASN B 1 111 ? 120.23800 102.60600 144.92300 1.000 100.01093 ? 111 ASN B CG   1 
ATOM   3297 O OD1  . ASN B 1 111 ? 119.90000 103.46100 145.72400 1.000 100.35737 ? 111 ASN B OD1  1 
ATOM   3298 N ND2  . ASN B 1 111 ? 121.06400 102.87000 143.92500 1.000 98.69173  ? 111 ASN B ND2  1 
ATOM   3299 N N    . PRO B 1 112 ? 117.49100 103.14300 146.32700 1.000 100.24781 ? 112 PRO B N    1 
ATOM   3300 C CA   . PRO B 1 112 ? 116.47300 104.19700 146.15200 1.000 100.76229 ? 112 PRO B CA   1 
ATOM   3301 C C    . PRO B 1 112 ? 116.47600 104.86300 144.78300 1.000 99.84551  ? 112 PRO B C    1 
ATOM   3302 O O    . PRO B 1 112 ? 115.42100 104.92100 144.13800 1.000 99.89114  ? 112 PRO B O    1 
ATOM   3303 C CB   . PRO B 1 112 ? 116.79400 105.17700 147.28900 1.000 100.38004 ? 112 PRO B CB   1 
ATOM   3304 C CG   . PRO B 1 112 ? 117.42800 104.32600 148.33000 1.000 99.99749  ? 112 PRO B CG   1 
ATOM   3305 C CD   . PRO B 1 112 ? 118.22500 103.29900 147.59700 1.000 99.44474  ? 112 PRO B CD   1 
ATOM   3306 N N    . ASP B 1 113 ? 117.61600 105.37400 144.31100 1.000 95.44739  ? 113 ASP B N    1 
ATOM   3307 C CA   . ASP B 1 113 ? 117.58500 106.14800 143.07300 1.000 96.10517  ? 113 ASP B CA   1 
ATOM   3308 C C    . ASP B 1 113 ? 117.24900 105.28500 141.85900 1.000 97.78426  ? 113 ASP B C    1 
ATOM   3309 O O    . ASP B 1 113 ? 116.44000 105.69400 141.01800 1.000 97.37755  ? 113 ASP B O    1 
ATOM   3310 C CB   . ASP B 1 113 ? 118.92400 106.85600 142.86800 1.000 95.18090  ? 113 ASP B CB   1 
ATOM   3311 C CG   . ASP B 1 113 ? 120.09900 105.90000 142.90300 1.000 97.92060  ? 113 ASP B CG   1 
ATOM   3312 O OD1  . ASP B 1 113 ? 120.55600 105.55800 144.01300 1.000 98.08835  ? 113 ASP B OD1  1 
ATOM   3313 O OD2  . ASP B 1 113 ? 120.56600 105.49100 141.81800 1.000 96.02413  ? 113 ASP B OD2  1 
ATOM   3314 N N    . LEU B 1 114 ? 117.84800 104.09600 141.73500 1.000 90.60233  ? 114 LEU B N    1 
ATOM   3315 C CA   . LEU B 1 114 ? 117.55600 103.27500 140.56100 1.000 88.82151  ? 114 LEU B CA   1 
ATOM   3316 C C    . LEU B 1 114 ? 116.06700 102.98000 140.44100 1.000 88.09189  ? 114 LEU B C    1 
ATOM   3317 O O    . LEU B 1 114 ? 115.50100 103.04900 139.34500 1.000 88.84881  ? 114 LEU B O    1 
ATOM   3318 C CB   . LEU B 1 114 ? 118.35500 101.97000 140.56700 1.000 90.12492  ? 114 LEU B CB   1 
ATOM   3319 C CG   . LEU B 1 114 ? 119.84000 102.01500 140.19800 1.000 90.01312  ? 114 LEU B CG   1 
ATOM   3320 C CD1  . LEU B 1 114 ? 120.73300 101.82300 141.39300 1.000 88.92545  ? 114 LEU B CD1  1 
ATOM   3321 C CD2  . LEU B 1 114 ? 120.14800 100.97300 139.13000 1.000 89.37753  ? 114 LEU B CD2  1 
ATOM   3322 N N    . SER B 1 115 ? 115.42400 102.61900 141.55400 1.000 83.57741  ? 115 SER B N    1 
ATOM   3323 C CA   . SER B 1 115 ? 114.03300 102.17600 141.51400 1.000 85.49822  ? 115 SER B CA   1 
ATOM   3324 C C    . SER B 1 115 ? 113.15400 103.09100 140.66800 1.000 86.07817  ? 115 SER B C    1 
ATOM   3325 O O    . SER B 1 115 ? 112.28200 102.61600 139.93200 1.000 85.40750  ? 115 SER B O    1 
ATOM   3326 C CB   . SER B 1 115 ? 113.48000 102.07800 142.93700 1.000 86.18684  ? 115 SER B CB   1 
ATOM   3327 O OG   . SER B 1 115 ? 113.54800 103.32900 143.59900 1.000 87.18918  ? 115 SER B OG   1 
ATOM   3328 N N    . ARG B 1 116 ? 113.36400 104.40500 140.75200 1.000 76.48822  ? 116 ARG B N    1 
ATOM   3329 C CA   . ARG B 1 116 ? 112.50100 105.33400 140.03400 1.000 76.37856  ? 116 ARG B CA   1 
ATOM   3330 C C    . ARG B 1 116 ? 113.03900 105.73300 138.66600 1.000 76.78799  ? 116 ARG B C    1 
ATOM   3331 O O    . ARG B 1 116 ? 112.27400 106.25500 137.84700 1.000 77.19090  ? 116 ARG B O    1 
ATOM   3332 C CB   . ARG B 1 116 ? 112.27500 106.59900 140.86800 1.000 77.07044  ? 116 ARG B CB   1 
ATOM   3333 C CG   . ARG B 1 116 ? 111.18300 106.46400 141.91800 1.000 79.07977  ? 116 ARG B CG   1 
ATOM   3334 C CD   . ARG B 1 116 ? 109.80300 106.75500 141.35100 1.000 77.91550  ? 116 ARG B CD   1 
ATOM   3335 N NE   . ARG B 1 116 ? 109.84600 107.60700 140.16900 1.000 77.08644  ? 116 ARG B NE   1 
ATOM   3336 C CZ   . ARG B 1 116 ? 108.77300 108.01100 139.50300 1.000 78.77257  ? 116 ARG B CZ   1 
ATOM   3337 N NH1  . ARG B 1 116 ? 107.55400 107.65700 139.87700 1.000 79.07534  ? 116 ARG B NH1  1 
ATOM   3338 N NH2  . ARG B 1 116 ? 108.92600 108.78300 138.43200 1.000 79.33985  ? 116 ARG B NH2  1 
ATOM   3339 N N    . TYR B 1 117 ? 114.32400 105.50500 138.39500 1.000 67.61427  ? 117 TYR B N    1 
ATOM   3340 C CA   . TYR B 1 117 ? 114.92600 105.86700 137.11700 1.000 66.26977  ? 117 TYR B CA   1 
ATOM   3341 C C    . TYR B 1 117 ? 115.45300 104.65800 136.35500 1.000 64.91136  ? 117 TYR B C    1 
ATOM   3342 O O    . TYR B 1 117 ? 116.35300 104.80300 135.52400 1.000 67.74907  ? 117 TYR B O    1 
ATOM   3343 C CB   . TYR B 1 117 ? 116.04300 106.89500 137.31400 1.000 64.53095  ? 117 TYR B CB   1 
ATOM   3344 C CG   . TYR B 1 117 ? 115.77200 107.89200 138.41600 1.000 67.11318  ? 117 TYR B CG   1 
ATOM   3345 C CD1  . TYR B 1 117 ? 114.58600 108.61600 138.44600 1.000 68.10582  ? 117 TYR B CD1  1 
ATOM   3346 C CD2  . TYR B 1 117 ? 116.70200 108.11800 139.42100 1.000 67.19325  ? 117 TYR B CD2  1 
ATOM   3347 C CE1  . TYR B 1 117 ? 114.33100 109.52900 139.44900 1.000 68.76045  ? 117 TYR B CE1  1 
ATOM   3348 C CE2  . TYR B 1 117 ? 116.45500 109.03100 140.42900 1.000 69.78586  ? 117 TYR B CE2  1 
ATOM   3349 C CZ   . TYR B 1 117 ? 115.26800 109.73400 140.43700 1.000 71.47720  ? 117 TYR B CZ   1 
ATOM   3350 O OH   . TYR B 1 117 ? 115.01500 110.64500 141.43600 1.000 70.28984  ? 117 TYR B OH   1 
ATOM   3351 N N    . SER B 1 118 ? 114.91000 103.46900 136.60400 1.000 52.46704  ? 118 SER B N    1 
ATOM   3352 C CA   . SER B 1 118 ? 115.42800 102.26300 135.97500 1.000 46.53097  ? 118 SER B CA   1 
ATOM   3353 C C    . SER B 1 118 ? 114.68900 101.89900 134.69700 1.000 45.50888  ? 118 SER B C    1 
ATOM   3354 O O    . SER B 1 118 ? 115.16500 101.04000 133.94700 1.000 49.49564  ? 118 SER B O    1 
ATOM   3355 C CB   . SER B 1 118 ? 115.36700 101.08500 136.95200 1.000 53.60120  ? 118 SER B CB   1 
ATOM   3356 O OG   . SER B 1 118 ? 114.02600 100.77700 137.29000 1.000 58.15570  ? 118 SER B OG   1 
ATOM   3357 N N    . VAL B 1 119 ? 113.54500 102.53100 134.42700 1.000 37.81742  ? 119 VAL B N    1 
ATOM   3358 C CA   . VAL B 1 119 ? 112.80900 102.27900 133.19100 1.000 38.68368  ? 119 VAL B CA   1 
ATOM   3359 C C    . VAL B 1 119 ? 113.42400 103.00200 132.00500 1.000 36.94055  ? 119 VAL B C    1 
ATOM   3360 O O    . VAL B 1 119 ? 112.98100 102.79900 130.86800 1.000 30.13707  ? 119 VAL B O    1 
ATOM   3361 C CB   . VAL B 1 119 ? 111.33200 102.68600 133.35700 1.000 38.35583  ? 119 VAL B CB   1 
ATOM   3362 C CG1  . VAL B 1 119 ? 111.20700 104.19400 133.50700 1.000 29.58265  ? 119 VAL B CG1  1 
ATOM   3363 C CG2  . VAL B 1 119 ? 110.49900 102.18100 132.18700 1.000 30.79196  ? 119 VAL B CG2  1 
ATOM   3364 N N    . TRP B 1 120 ? 114.43700 103.83900 132.24100 1.000 34.96225  ? 120 TRP B N    1 
ATOM   3365 C CA   . TRP B 1 120 ? 115.11300 104.58300 131.18600 1.000 27.78689  ? 120 TRP B CA   1 
ATOM   3366 C C    . TRP B 1 120 ? 115.99400 103.70700 130.30600 1.000 27.51968  ? 120 TRP B C    1 
ATOM   3367 O O    . TRP B 1 120 ? 116.47600 104.18700 129.27600 1.000 24.47322  ? 120 TRP B O    1 
ATOM   3368 C CB   . TRP B 1 120 ? 115.96600 105.69500 131.80100 1.000 23.81494  ? 120 TRP B CB   1 
ATOM   3369 C CG   . TRP B 1 120 ? 115.18500 106.88600 132.25800 1.000 31.37298  ? 120 TRP B CG   1 
ATOM   3370 C CD1  . TRP B 1 120 ? 114.24700 106.91900 133.24600 1.000 30.58907  ? 120 TRP B CD1  1 
ATOM   3371 C CD2  . TRP B 1 120 ? 115.28700 108.22400 131.75900 1.000 33.55428  ? 120 TRP B CD2  1 
ATOM   3372 N NE1  . TRP B 1 120 ? 113.75000 108.18900 133.38700 1.000 31.17533  ? 120 TRP B NE1  1 
ATOM   3373 C CE2  . TRP B 1 120 ? 114.37300 109.01100 132.48600 1.000 32.39224  ? 120 TRP B CE2  1 
ATOM   3374 C CE3  . TRP B 1 120 ? 116.05900 108.83200 130.76600 1.000 34.98157  ? 120 TRP B CE3  1 
ATOM   3375 C CZ2  . TRP B 1 120 ? 114.21000 110.37400 132.25100 1.000 30.89116  ? 120 TRP B CZ2  1 
ATOM   3376 C CZ3  . TRP B 1 120 ? 115.89500 110.18500 130.53400 1.000 35.72572  ? 120 TRP B CZ3  1 
ATOM   3377 C CH2  . TRP B 1 120 ? 114.97900 110.94100 131.27400 1.000 34.65653  ? 120 TRP B CH2  1 
ATOM   3378 N N    . ALA B 1 121 ? 116.21500 102.44700 130.67700 1.000 25.26573  ? 121 ALA B N    1 
ATOM   3379 C CA   . ALA B 1 121 ? 117.06300 101.55300 129.90000 1.000 16.18726  ? 121 ALA B CA   1 
ATOM   3380 C C    . ALA B 1 121 ? 116.28700 100.64400 128.95900 1.000 19.87227  ? 121 ALA B C    1 
ATOM   3381 O O    . ALA B 1 121 ? 116.81900 100.25700 127.91500 1.000 26.58849  ? 121 ALA B O    1 
ATOM   3382 C CB   . ALA B 1 121 ? 117.91900 100.69100 130.83400 1.000 8.21180   ? 121 ALA B CB   1 
ATOM   3383 N N    . ILE B 1 122 ? 115.04100 100.29900 129.29300 1.000 19.29838  ? 122 ILE B N    1 
ATOM   3384 C CA   . ILE B 1 122 ? 114.22400 99.49100  128.39000 1.000 12.89238  ? 122 ILE B CA   1 
ATOM   3385 C C    . ILE B 1 122 ? 113.55600 100.32400 127.31000 1.000 14.66622  ? 122 ILE B C    1 
ATOM   3386 O O    . ILE B 1 122 ? 113.03700 99.76000  126.34000 1.000 19.35626  ? 122 ILE B O    1 
ATOM   3387 C CB   . ILE B 1 122 ? 113.15100 98.70400  129.16600 1.000 18.55457  ? 122 ILE B CB   1 
ATOM   3388 C CG1  . ILE B 1 122 ? 112.48400 97.67100  128.25600 1.000 15.29173  ? 122 ILE B CG1  1 
ATOM   3389 C CG2  . ILE B 1 122 ? 112.11300 99.64500  129.75200 1.000 22.95663  ? 122 ILE B CG2  1 
ATOM   3390 C CD1  . ILE B 1 122 ? 112.23300 96.33900  128.91900 1.000 18.16799  ? 122 ILE B CD1  1 
ATOM   3391 N N    . LEU B 1 123 ? 113.56600 101.64800 127.44300 1.000 17.86464  ? 123 LEU B N    1 
ATOM   3392 C CA   . LEU B 1 123 ? 112.96500 102.52500 126.45000 1.000 11.52114  ? 123 LEU B CA   1 
ATOM   3393 C C    . LEU B 1 123 ? 113.96300 103.00300 125.40400 1.000 18.56784  ? 123 LEU B C    1 
ATOM   3394 O O    . LEU B 1 123 ? 113.54600 103.52000 124.36300 1.000 20.43459  ? 123 LEU B O    1 
ATOM   3395 C CB   . LEU B 1 123 ? 112.32200 103.73400 127.13800 1.000 13.55759  ? 123 LEU B CB   1 
ATOM   3396 C CG   . LEU B 1 123 ? 111.10500 103.45600 128.02600 1.000 20.37152  ? 123 LEU B CG   1 
ATOM   3397 C CD1  . LEU B 1 123 ? 110.37300 104.74100 128.35600 1.000 13.91855  ? 123 LEU B CD1  1 
ATOM   3398 C CD2  . LEU B 1 123 ? 110.15800 102.45600 127.37800 1.000 20.97132  ? 123 LEU B CD2  1 
ATOM   3399 N N    . THR B 1 124 ? 115.26400 102.85100 125.66000 1.000 17.74196  ? 124 THR B N    1 
ATOM   3400 C CA   . THR B 1 124 ? 116.27900 103.18300 124.66600 1.000 10.70788  ? 124 THR B CA   1 
ATOM   3401 C C    . THR B 1 124 ? 116.40900 102.09300 123.60800 1.000 16.12774  ? 124 THR B C    1 
ATOM   3402 O O    . THR B 1 124 ? 116.71800 102.39000 122.44400 1.000 19.94853  ? 124 THR B O    1 
ATOM   3403 C CB   . THR B 1 124 ? 117.62800 103.41000 125.35300 1.000 12.82221  ? 124 THR B CB   1 
ATOM   3404 O OG1  . THR B 1 124 ? 117.55000 104.56900 126.19000 1.000 20.55701  ? 124 THR B OG1  1 
ATOM   3405 C CG2  . THR B 1 124 ? 118.72300 103.61900 124.32300 1.000 12.09017  ? 124 THR B CG2  1 
ATOM   3406 N N    . VAL B 1 125 ? 116.16200 100.83900 123.99200 1.000 15.93098  ? 125 VAL B N    1 
ATOM   3407 C CA   . VAL B 1 125 ? 116.19900 99.73500  123.03800 1.000 14.50745  ? 125 VAL B CA   1 
ATOM   3408 C C    . VAL B 1 125 ? 115.13600 99.92900  121.96900 1.000 12.57102  ? 125 VAL B C    1 
ATOM   3409 O O    . VAL B 1 125 ? 115.35800 99.63800  120.78800 1.000 18.14420  ? 125 VAL B O    1 
ATOM   3410 C CB   . VAL B 1 125 ? 116.02600 98.39200  123.77200 1.000 15.82707  ? 125 VAL B CB   1 
ATOM   3411 C CG1  . VAL B 1 125 ? 115.95800 97.24300  122.77900 1.000 14.97600  ? 125 VAL B CG1  1 
ATOM   3412 C CG2  . VAL B 1 125 ? 117.14900 98.18200  124.77200 1.000 12.65848  ? 125 VAL B CG2  1 
ATOM   3413 N N    . VAL B 1 126 ? 113.96100 100.42200 122.36500 1.000 12.63880  ? 126 VAL B N    1 
ATOM   3414 C CA   . VAL B 1 126 ? 112.86800 100.63300 121.42600 1.000 14.51603  ? 126 VAL B CA   1 
ATOM   3415 C C    . VAL B 1 126 ? 113.10600 101.82100 120.51000 1.000 20.11019  ? 126 VAL B C    1 
ATOM   3416 O O    . VAL B 1 126 ? 112.38400 101.98400 119.52100 1.000 25.25662  ? 126 VAL B O    1 
ATOM   3417 C CB   . VAL B 1 126 ? 111.54200 100.82500 122.19100 1.000 15.64948  ? 126 VAL B CB   1 
ATOM   3418 C CG1  . VAL B 1 126 ? 110.37500 100.93500 121.22600 1.000 18.30543  ? 126 VAL B CG1  1 
ATOM   3419 C CG2  . VAL B 1 126 ? 111.32500 99.68800  123.17000 1.000 10.71650  ? 126 VAL B CG2  1 
ATOM   3420 N N    . VAL B 1 127 ? 114.10600 102.65000 120.80300 1.000 18.90691  ? 127 VAL B N    1 
ATOM   3421 C CA   . VAL B 1 127 ? 114.35800 103.85900 120.02700 1.000 12.00600  ? 127 VAL B CA   1 
ATOM   3422 C C    . VAL B 1 127 ? 115.66900 103.81800 119.25400 1.000 8.20346   ? 127 VAL B C    1 
ATOM   3423 O O    . VAL B 1 127 ? 115.88000 104.68400 118.39100 1.000 15.86268  ? 127 VAL B O    1 
ATOM   3424 C CB   . VAL B 1 127 ? 114.31500 105.11600 120.92400 1.000 17.97885  ? 127 VAL B CB   1 
ATOM   3425 C CG1  . VAL B 1 127 ? 114.50500 106.37900 120.10100 1.000 13.36384  ? 127 VAL B CG1  1 
ATOM   3426 C CG2  . VAL B 1 127 ? 113.00700 105.17500 121.69600 1.000 7.66276   ? 127 VAL B CG2  1 
ATOM   3427 N N    . VAL B 1 128 ? 116.54500 102.84500 119.50400 1.000 14.71350  ? 128 VAL B N    1 
ATOM   3428 C CA   . VAL B 1 128 ? 117.84500 102.81100 118.84300 1.000 15.33541  ? 128 VAL B CA   1 
ATOM   3429 C C    . VAL B 1 128 ? 118.05700 101.57400 117.97900 1.000 18.11692  ? 128 VAL B C    1 
ATOM   3430 O O    . VAL B 1 128 ? 119.08000 101.48500 117.29700 1.000 20.43512  ? 128 VAL B O    1 
ATOM   3431 C CB   . VAL B 1 128 ? 118.99900 102.95200 119.85800 1.000 18.31338  ? 128 VAL B CB   1 
ATOM   3432 C CG1  . VAL B 1 128 ? 118.82700 104.21700 120.68200 1.000 12.14564  ? 128 VAL B CG1  1 
ATOM   3433 C CG2  . VAL B 1 128 ? 119.07900 101.72500 120.75200 1.000 15.82346  ? 128 VAL B CG2  1 
ATOM   3434 N N    . PHE B 1 129 ? 117.12600 100.62300 117.97100 1.000 16.10624  ? 129 PHE B N    1 
ATOM   3435 C CA   . PHE B 1 129 ? 117.28600 99.38400  117.21200 1.000 18.97826  ? 129 PHE B CA   1 
ATOM   3436 C C    . PHE B 1 129 ? 116.78300 99.60100  115.78400 1.000 18.95289  ? 129 PHE B C    1 
ATOM   3437 O O    . PHE B 1 129 ? 115.58500 99.80100  115.56800 1.000 24.01417  ? 129 PHE B O    1 
ATOM   3438 C CB   . PHE B 1 129 ? 116.52900 98.25200  117.90300 1.000 16.29951  ? 129 PHE B CB   1 
ATOM   3439 C CG   . PHE B 1 129 ? 117.18700 96.90400  117.78000 1.000 17.78006  ? 129 PHE B CG   1 
ATOM   3440 C CD1  . PHE B 1 129 ? 117.25600 96.25200  116.56100 1.000 23.60320  ? 129 PHE B CD1  1 
ATOM   3441 C CD2  . PHE B 1 129 ? 117.72400 96.28100  118.89400 1.000 9.64248   ? 129 PHE B CD2  1 
ATOM   3442 C CE1  . PHE B 1 129 ? 117.85400 95.01000  116.45600 1.000 17.31975  ? 129 PHE B CE1  1 
ATOM   3443 C CE2  . PHE B 1 129 ? 118.32400 95.04000  118.79300 1.000 13.92380  ? 129 PHE B CE2  1 
ATOM   3444 C CZ   . PHE B 1 129 ? 118.38900 94.40500  117.57400 1.000 9.21050   ? 129 PHE B CZ   1 
ATOM   3445 N N    . GLU B 1 130 ? 117.69300 99.55300  114.81100 1.000 20.60695  ? 130 GLU B N    1 
ATOM   3446 C CA   . GLU B 1 130 ? 117.36500 99.74600  113.40200 1.000 19.36261  ? 130 GLU B CA   1 
ATOM   3447 C C    . GLU B 1 130 ? 117.65500 98.49000  112.58700 1.000 23.36108  ? 130 GLU B C    1 
ATOM   3448 O O    . GLU B 1 130 ? 118.27600 97.53500  113.06000 1.000 25.62924  ? 130 GLU B O    1 
ATOM   3449 C CB   . GLU B 1 130 ? 118.12100 100.94400 112.81100 1.000 14.02285  ? 130 GLU B CB   1 
ATOM   3450 C CG   . GLU B 1 130 ? 118.30500 102.09500 113.77500 1.000 22.61636  ? 130 GLU B CG   1 
ATOM   3451 C CD   . GLU B 1 130 ? 117.23900 103.16000 113.61100 1.000 29.69339  ? 130 GLU B CD   1 
ATOM   3452 O OE1  . GLU B 1 130 ? 116.59100 103.19700 112.54500 1.000 29.30690  ? 130 GLU B OE1  1 
ATOM   3453 O OE2  . GLU B 1 130 ? 117.03700 103.95200 114.55400 1.000 28.18384  ? 130 GLU B OE2  1 
ATOM   3454 N N    . PHE B 1 131 ? 117.20100 98.52100  111.33100 1.000 17.14573  ? 131 PHE B N    1 
ATOM   3455 C CA   . PHE B 1 131 ? 117.30600 97.36200  110.44500 1.000 12.90292  ? 131 PHE B CA   1 
ATOM   3456 C C    . PHE B 1 131 ? 118.75200 97.01900  110.10100 1.000 16.05010  ? 131 PHE B C    1 
ATOM   3457 O O    . PHE B 1 131 ? 119.11600 95.83900  110.05300 1.000 12.20032  ? 131 PHE B O    1 
ATOM   3458 C CB   . PHE B 1 131 ? 116.49800 97.61700  109.17200 1.000 13.62358  ? 131 PHE B CB   1 
ATOM   3459 C CG   . PHE B 1 131 ? 115.90500 96.37700  108.56900 1.000 22.56610  ? 131 PHE B CG   1 
ATOM   3460 C CD1  . PHE B 1 131 ? 114.87000 95.71200  109.19600 1.000 19.48719  ? 131 PHE B CD1  1 
ATOM   3461 C CD2  . PHE B 1 131 ? 116.38100 95.88300  107.36700 1.000 24.96811  ? 131 PHE B CD2  1 
ATOM   3462 C CE1  . PHE B 1 131 ? 114.32700 94.57200  108.64300 1.000 17.15621  ? 131 PHE B CE1  1 
ATOM   3463 C CE2  . PHE B 1 131 ? 115.84000 94.74400  106.80900 1.000 21.10614  ? 131 PHE B CE2  1 
ATOM   3464 C CZ   . PHE B 1 131 ? 114.81200 94.08800  107.44900 1.000 18.95909  ? 131 PHE B CZ   1 
ATOM   3465 N N    . THR B 1 132 ? 119.58000 98.01400  109.83600 1.000 20.41223  ? 132 THR B N    1 
ATOM   3466 C CA   . THR B 1 132 ? 120.95600 97.74500  109.46400 1.000 9.56005   ? 132 THR B CA   1 
ATOM   3467 C C    . THR B 1 132 ? 121.92600 98.25700  110.51000 1.000 8.42229   ? 132 THR B C    1 
ATOM   3468 O O    . THR B 1 132 ? 121.54600 99.00900  111.39500 1.000 14.57855  ? 132 THR B O    1 
ATOM   3469 C CB   . THR B 1 132 ? 121.29500 98.37300  108.09600 1.000 10.08627  ? 132 THR B CB   1 
ATOM   3470 O OG1  . THR B 1 132 ? 121.03200 99.78000  108.13500 1.000 18.33656  ? 132 THR B OG1  1 
ATOM   3471 C CG2  . THR B 1 132 ? 120.46700 97.73500  106.99500 1.000 5.40955   ? 132 THR B CG2  1 
ATOM   3472 N N    . ILE B 1 133 ? 123.17700 97.83600  110.42000 1.000 3.20406   ? 133 ILE B N    1 
ATOM   3473 C CA   . ILE B 1 133 ? 124.19400 98.30800  111.34500 1.000 8.61161   ? 133 ILE B CA   1 
ATOM   3474 C C    . ILE B 1 133 ? 124.58100 99.74900  111.06800 1.000 12.43067  ? 133 ILE B C    1 
ATOM   3475 O O    . ILE B 1 133 ? 124.70400 100.53700 111.99700 1.000 19.61066  ? 133 ILE B O    1 
ATOM   3476 C CB   . ILE B 1 133 ? 125.45700 97.42400  111.27700 1.000 17.54481  ? 133 ILE B CB   1 
ATOM   3477 C CG1  . ILE B 1 133 ? 125.07700 95.94000  111.25900 1.000 12.86282  ? 133 ILE B CG1  1 
ATOM   3478 C CG2  . ILE B 1 133 ? 126.39300 97.73400  112.43500 1.000 15.25703  ? 133 ILE B CG2  1 
ATOM   3479 C CD1  . ILE B 1 133 ? 124.36200 95.46900  112.50600 1.000 12.20528  ? 133 ILE B CD1  1 
ATOM   3480 N N    . GLY B 1 134 ? 124.75900 100.10900 109.80200 1.000 8.96880   ? 134 GLY B N    1 
ATOM   3481 C CA   . GLY B 1 134 ? 125.18600 101.45200 109.44800 1.000 3.53393   ? 134 GLY B CA   1 
ATOM   3482 C C    . GLY B 1 134 ? 124.29400 102.57400 109.90200 1.000 10.46112  ? 134 GLY B C    1 
ATOM   3483 O O    . GLY B 1 134 ? 124.79800 103.57900 110.38200 1.000 23.71831  ? 134 GLY B O    1 
ATOM   3484 N N    . ALA B 1 135 ? 122.98900 102.44800 109.72200 1.000 0.48746   ? 135 ALA B N    1 
ATOM   3485 C CA   . ALA B 1 135 ? 122.04000 103.43700 110.21200 1.000 3.41909   ? 135 ALA B CA   1 
ATOM   3486 C C    . ALA B 1 135 ? 122.07200 103.47100 111.72500 1.000 13.62567  ? 135 ALA B C    1 
ATOM   3487 O O    . ALA B 1 135 ? 122.14100 104.54300 112.32500 1.000 23.29222  ? 135 ALA B O    1 
ATOM   3488 C CB   . ALA B 1 135 ? 120.64100 103.11200 109.72200 1.000 1.65100   ? 135 ALA B CB   1 
ATOM   3489 N N    . THR B 1 136 ? 122.03500 102.29800 112.34700 1.000 7.78227   ? 136 THR B N    1 
ATOM   3490 C CA   . THR B 1 136 ? 122.13100 102.22400 113.80000 1.000 13.68827  ? 136 THR B CA   1 
ATOM   3491 C C    . THR B 1 136 ? 123.33600 103.01200 114.29200 1.000 10.98401  ? 136 THR B C    1 
ATOM   3492 O O    . THR B 1 136 ? 123.25200 103.71200 115.29500 1.000 8.49000   ? 136 THR B O    1 
ATOM   3493 C CB   . THR B 1 136 ? 122.20800 100.76100 114.28900 1.000 14.14059  ? 136 THR B CB   1 
ATOM   3494 O OG1  . THR B 1 136 ? 121.06600 100.03700 113.82000 1.000 20.87955  ? 136 THR B OG1  1 
ATOM   3495 C CG2  . THR B 1 136 ? 122.24000 100.69700 115.80200 1.000 7.15048   ? 136 THR B CG2  1 
ATOM   3496 N N    . LEU B 1 137 ? 124.45600 102.91100 113.59000 1.000 8.18070   ? 137 LEU B N    1 
ATOM   3497 C CA   . LEU B 1 137 ? 125.65400 103.66300 113.95400 1.000 2.51227   ? 137 LEU B CA   1 
ATOM   3498 C C    . LEU B 1 137 ? 125.54600 105.12800 113.58200 1.000 9.05701   ? 137 LEU B C    1 
ATOM   3499 O O    . LEU B 1 137 ? 125.96600 105.99100 114.34300 1.000 16.05418  ? 137 LEU B O    1 
ATOM   3500 C CB   . LEU B 1 137 ? 126.86700 103.06000 113.26200 1.000 4.75210   ? 137 LEU B CB   1 
ATOM   3501 C CG   . LEU B 1 137 ? 127.15100 101.58500 113.51300 1.000 9.24706   ? 137 LEU B CG   1 
ATOM   3502 C CD1  . LEU B 1 137 ? 128.20200 101.07800 112.53900 1.000 10.42907  ? 137 LEU B CD1  1 
ATOM   3503 C CD2  . LEU B 1 137 ? 127.58000 101.36500 114.95300 1.000 6.59681   ? 137 LEU B CD2  1 
ATOM   3504 N N    . SER B 1 138 ? 124.99600 105.41300 112.40900 1.000 2.68599   ? 138 SER B N    1 
ATOM   3505 C CA   . SER B 1 138 ? 124.88200 106.79000 111.93600 1.000 6.66554   ? 138 SER B CA   1 
ATOM   3506 C C    . SER B 1 138 ? 123.85100 107.63100 112.68600 1.000 16.06325  ? 138 SER B C    1 
ATOM   3507 O O    . SER B 1 138 ? 124.06400 108.82100 112.89600 1.000 18.37991  ? 138 SER B O    1 
ATOM   3508 C CB   . SER B 1 138 ? 124.55200 106.79700 110.44500 1.000 4.36401   ? 138 SER B CB   1 
ATOM   3509 O OG   . SER B 1 138 ? 123.25800 106.28400 110.21000 1.000 25.75139  ? 138 SER B OG   1 
ATOM   3510 N N    . LYS B 1 139 ? 122.74100 107.02900 113.09100 1.000 8.11441   ? 139 LYS B N    1 
ATOM   3511 C CA   . LYS B 1 139 ? 121.68600 107.77700 113.76800 1.000 3.58740   ? 139 LYS B CA   1 
ATOM   3512 C C    . LYS B 1 139 ? 121.90600 107.86900 115.26900 1.000 12.20904  ? 139 LYS B C    1 
ATOM   3513 O O    . LYS B 1 139 ? 121.57600 108.88600 115.86700 1.000 24.86151  ? 139 LYS B O    1 
ATOM   3514 C CB   . LYS B 1 139 ? 120.32100 107.17500 113.44000 1.000 4.39200   ? 139 LYS B CB   1 
ATOM   3515 C CG   . LYS B 1 139 ? 119.92000 107.39100 111.99500 1.000 9.93228   ? 139 LYS B CG   1 
ATOM   3516 C CD   . LYS B 1 139 ? 118.63400 106.65900 111.66500 1.000 3.94819   ? 139 LYS B CD   1 
ATOM   3517 C CE   . LYS B 1 139 ? 117.47200 107.22500 112.44900 1.000 14.96142  ? 139 LYS B CE   1 
ATOM   3518 N NZ   . LYS B 1 139 ? 116.20100 106.58000 112.02700 1.000 22.60449  ? 139 LYS B NZ   1 
ATOM   3519 N N    . GLY B 1 140 ? 122.45600 106.83000 115.88700 1.000 10.48908  ? 140 GLY B N    1 
ATOM   3520 C CA   . GLY B 1 140 ? 122.78100 106.88900 117.29800 1.000 4.63980   ? 140 GLY B CA   1 
ATOM   3521 C C    . GLY B 1 140 ? 123.75600 108.00900 117.55600 1.000 11.01116  ? 140 GLY B C    1 
ATOM   3522 O O    . GLY B 1 140 ? 123.70300 108.64600 118.60400 1.000 13.18191  ? 140 GLY B O    1 
ATOM   3523 N N    . PHE B 1 141 ? 124.64000 108.26100 116.60000 1.000 6.42101   ? 141 PHE B N    1 
ATOM   3524 C CA   . PHE B 1 141 ? 125.61200 109.33800 116.72500 1.000 10.27291  ? 141 PHE B CA   1 
ATOM   3525 C C    . PHE B 1 141 ? 124.96400 110.70600 116.74900 1.000 13.38230  ? 141 PHE B C    1 
ATOM   3526 O O    . PHE B 1 141 ? 125.28400 111.53200 117.59500 1.000 13.71361  ? 141 PHE B O    1 
ATOM   3527 C CB   . PHE B 1 141 ? 126.58300 109.26200 115.55800 1.000 10.13283  ? 141 PHE B CB   1 
ATOM   3528 C CG   . PHE B 1 141 ? 127.57600 110.38100 115.52100 1.000 16.62898  ? 141 PHE B CG   1 
ATOM   3529 C CD1  . PHE B 1 141 ? 128.74600 110.30600 116.25000 1.000 10.07451  ? 141 PHE B CD1  1 
ATOM   3530 C CD2  . PHE B 1 141 ? 127.34200 111.50600 114.75200 1.000 21.17850  ? 141 PHE B CD2  1 
ATOM   3531 C CE1  . PHE B 1 141 ? 129.66400 111.33400 116.21800 1.000 11.92853  ? 141 PHE B CE1  1 
ATOM   3532 C CE2  . PHE B 1 141 ? 128.25500 112.53800 114.71500 1.000 11.93662  ? 141 PHE B CE2  1 
ATOM   3533 C CZ   . PHE B 1 141 ? 129.41900 112.45300 115.45000 1.000 12.08130  ? 141 PHE B CZ   1 
ATOM   3534 N N    . ASN B 1 142 ? 124.04400 110.94700 115.82700 1.000 9.72570   ? 142 ASN B N    1 
ATOM   3535 C CA   . ASN B 1 142 ? 123.34800 112.22200 115.77000 1.000 3.21469   ? 142 ASN B CA   1 
ATOM   3536 C C    . ASN B 1 142 ? 122.49200 112.43900 117.00200 1.000 12.72629  ? 142 ASN B C    1 
ATOM   3537 O O    . ASN B 1 142 ? 122.41700 113.54900 117.51600 1.000 24.84358  ? 142 ASN B O    1 
ATOM   3538 C CB   . ASN B 1 142 ? 122.49100 112.28400 114.51700 1.000 7.54311   ? 142 ASN B CB   1 
ATOM   3539 C CG   . ASN B 1 142 ? 123.31100 112.25000 113.24900 1.000 19.26107  ? 142 ASN B CG   1 
ATOM   3540 O OD1  . ASN B 1 142 ? 124.52800 112.42400 113.27800 1.000 22.22581  ? 142 ASN B OD1  1 
ATOM   3541 N ND2  . ASN B 1 142 ? 122.64700 112.03100 112.12300 1.000 13.44589  ? 142 ASN B ND2  1 
ATOM   3542 N N    . ARG B 1 143 ? 121.84700 111.38300 117.48300 1.000 5.20938   ? 143 ARG B N    1 
ATOM   3543 C CA   . ARG B 1 143 ? 121.02300 111.48800 118.67800 1.000 5.20350   ? 143 ARG B CA   1 
ATOM   3544 C C    . ARG B 1 143 ? 121.87100 111.82000 119.89100 1.000 6.12594   ? 143 ARG B C    1 
ATOM   3545 O O    . ARG B 1 143 ? 121.47400 112.62200 120.71800 1.000 16.51949  ? 143 ARG B O    1 
ATOM   3546 C CB   . ARG B 1 143 ? 120.25500 110.19600 118.92700 1.000 4.05373   ? 143 ARG B CB   1 
ATOM   3547 C CG   . ARG B 1 143 ? 119.24200 109.81900 117.86500 1.000 9.16560   ? 143 ARG B CG   1 
ATOM   3548 C CD   . ARG B 1 143 ? 118.42500 108.63000 118.34200 1.000 5.03615   ? 143 ARG B CD   1 
ATOM   3549 N NE   . ARG B 1 143 ? 117.38600 108.24400 117.39400 1.000 17.00492  ? 143 ARG B NE   1 
ATOM   3550 C CZ   . ARG B 1 143 ? 117.49800 107.24700 116.52300 1.000 20.74213  ? 143 ARG B CZ   1 
ATOM   3551 N NH1  . ARG B 1 143 ? 118.60500 106.52100 116.47700 1.000 14.98853  ? 143 ARG B NH1  1 
ATOM   3552 N NH2  . ARG B 1 143 ? 116.49600 106.96900 115.70200 1.000 6.23043   ? 143 ARG B NH2  1 
ATOM   3553 N N    . ALA B 1 144 ? 123.03900 111.21200 120.00000 1.000 9.95827   ? 144 ALA B N    1 
ATOM   3554 C CA   . ALA B 1 144 ? 123.93300 111.49300 121.11300 1.000 12.64186  ? 144 ALA B CA   1 
ATOM   3555 C C    . ALA B 1 144 ? 124.40600 112.93000 121.07600 1.000 16.88854  ? 144 ALA B C    1 
ATOM   3556 O O    . ALA B 1 144 ? 124.53800 113.56400 122.11500 1.000 19.02197  ? 144 ALA B O    1 
ATOM   3557 C CB   . ALA B 1 144 ? 125.11600 110.55000 121.08400 1.000 9.20672   ? 144 ALA B CB   1 
ATOM   3558 N N    . LEU B 1 145 ? 124.67200 113.44500 119.88500 1.000 13.68893  ? 145 LEU B N    1 
ATOM   3559 C CA   . LEU B 1 145 ? 125.09400 114.82800 119.74000 1.000 12.46992  ? 145 LEU B CA   1 
ATOM   3560 C C    . LEU B 1 145 ? 124.00300 115.75300 120.20000 1.000 21.04096  ? 145 LEU B C    1 
ATOM   3561 O O    . LEU B 1 145 ? 124.26200 116.67600 120.96100 1.000 29.51766  ? 145 LEU B O    1 
ATOM   3562 C CB   . LEU B 1 145 ? 125.42700 115.12800 118.28500 1.000 15.64270  ? 145 LEU B CB   1 
ATOM   3563 C CG   . LEU B 1 145 ? 126.88000 114.93400 117.85000 1.000 24.53514  ? 145 LEU B CG   1 
ATOM   3564 C CD1  . LEU B 1 145 ? 127.36400 113.52200 118.13600 1.000 23.75138  ? 145 LEU B CD1  1 
ATOM   3565 C CD2  . LEU B 1 145 ? 127.04600 115.27400 116.37900 1.000 17.42829  ? 145 LEU B CD2  1 
ATOM   3566 N N    . GLY B 1 146 ? 122.78000 115.51100 119.74800 1.000 14.37479  ? 146 GLY B N    1 
ATOM   3567 C CA   . GLY B 1 146 ? 121.65400 116.31500 120.17000 1.000 2.52168   ? 146 GLY B CA   1 
ATOM   3568 C C    . GLY B 1 146 ? 121.47300 116.27300 121.66800 1.000 11.86905  ? 146 GLY B C    1 
ATOM   3569 O O    . GLY B 1 146 ? 121.14100 117.27600 122.28400 1.000 19.52795  ? 146 GLY B O    1 
ATOM   3570 N N    . THR B 1 147 ? 121.68700 115.10800 122.26600 1.000 14.48682  ? 147 THR B N    1 
ATOM   3571 C CA   . THR B 1 147 ? 121.48000 114.99400 123.70500 1.000 11.28446  ? 147 THR B CA   1 
ATOM   3572 C C    . THR B 1 147 ? 122.56300 115.73400 124.48100 1.000 14.07509  ? 147 THR B C    1 
ATOM   3573 O O    . THR B 1 147 ? 122.26700 116.48100 125.42100 1.000 18.48271  ? 147 THR B O    1 
ATOM   3574 C CB   . THR B 1 147 ? 121.43700 113.52300 124.11500 1.000 13.51633  ? 147 THR B CB   1 
ATOM   3575 O OG1  . THR B 1 147 ? 120.61900 112.79300 123.19400 1.000 24.52223  ? 147 THR B OG1  1 
ATOM   3576 C CG2  . THR B 1 147 ? 120.86900 113.37500 125.51500 1.000 13.92929  ? 147 THR B CG2  1 
ATOM   3577 N N    . LEU B 1 148 ? 123.82900 115.54600 124.10200 1.000 20.32951  ? 148 LEU B N    1 
ATOM   3578 C CA   . LEU B 1 148 ? 124.90400 116.15300 124.87900 1.000 17.18333  ? 148 LEU B CA   1 
ATOM   3579 C C    . LEU B 1 148 ? 124.93100 117.66700 124.71200 1.000 17.53596  ? 148 LEU B C    1 
ATOM   3580 O O    . LEU B 1 148 ? 125.15400 118.40000 125.68700 1.000 21.15383  ? 148 LEU B O    1 
ATOM   3581 C CB   . LEU B 1 148 ? 126.24600 115.53700 124.49100 1.000 18.98946  ? 148 LEU B CB   1 
ATOM   3582 C CG   . LEU B 1 148 ? 126.65700 114.32300 125.32700 1.000 25.46307  ? 148 LEU B CG   1 
ATOM   3583 C CD1  . LEU B 1 148 ? 125.73200 113.15000 125.06000 1.000 22.07773  ? 148 LEU B CD1  1 
ATOM   3584 C CD2  . LEU B 1 148 ? 128.09700 113.94200 125.04500 1.000 25.19820  ? 148 LEU B CD2  1 
ATOM   3585 N N    . SER B 1 149 ? 124.66300 118.16800 123.50000 1.000 21.69416  ? 149 SER B N    1 
ATOM   3586 C CA   . SER B 1 149 ? 124.62600 119.61600 123.33400 1.000 19.49203  ? 149 SER B CA   1 
ATOM   3587 C C    . SER B 1 149 ? 123.47800 120.22900 124.12800 1.000 25.29160  ? 149 SER B C    1 
ATOM   3588 O O    . SER B 1 149 ? 123.66300 121.24300 124.81800 1.000 31.53880  ? 149 SER B O    1 
ATOM   3589 C CB   . SER B 1 149 ? 124.51800 119.97700 121.85300 1.000 15.38431  ? 149 SER B CB   1 
ATOM   3590 O OG   . SER B 1 149 ? 123.48300 119.24900 121.22000 1.000 22.57024  ? 149 SER B OG   1 
ATOM   3591 N N    . ALA B 1 150 ? 122.29000 119.61700 124.06600 1.000 19.57960  ? 150 ALA B N    1 
ATOM   3592 C CA   . ALA B 1 150 ? 121.15500 120.15000 124.81100 1.000 13.14608  ? 150 ALA B CA   1 
ATOM   3593 C C    . ALA B 1 150 ? 121.41300 120.12000 126.31100 1.000 19.75790  ? 150 ALA B C    1 
ATOM   3594 O O    . ALA B 1 150 ? 121.08100 121.07500 127.02200 1.000 18.67176  ? 150 ALA B O    1 
ATOM   3595 C CB   . ALA B 1 150 ? 119.88700 119.37100 124.46800 1.000 11.92156  ? 150 ALA B CB   1 
ATOM   3596 N N    . GLY B 1 151 ? 122.01400 119.03900 126.81400 1.000 29.14223  ? 151 GLY B N    1 
ATOM   3597 C CA   . GLY B 1 151 ? 122.28300 118.96000 128.24000 1.000 23.54305  ? 151 GLY B CA   1 
ATOM   3598 C C    . GLY B 1 151 ? 123.29900 119.98300 128.70900 1.000 24.68251  ? 151 GLY B C    1 
ATOM   3599 O O    . GLY B 1 151 ? 123.11400 120.62000 129.75300 1.000 29.08571  ? 151 GLY B O    1 
ATOM   3600 N N    . GLY B 1 152 ? 124.36800 120.18500 127.93600 1.000 22.73023  ? 152 GLY B N    1 
ATOM   3601 C CA   . GLY B 1 152 ? 125.34200 121.19500 128.31600 1.000 22.09457  ? 152 GLY B CA   1 
ATOM   3602 C C    . GLY B 1 152 ? 124.75300 122.59200 128.30900 1.000 31.33644  ? 152 GLY B C    1 
ATOM   3603 O O    . GLY B 1 152 ? 124.98700 123.38500 129.22900 1.000 34.71578  ? 152 GLY B O    1 
ATOM   3604 N N    . LEU B 1 153 ? 123.94900 122.90200 127.28800 1.000 26.10505  ? 153 LEU B N    1 
ATOM   3605 C CA   . LEU B 1 153 ? 123.32900 124.22100 127.22000 1.000 19.02468  ? 153 LEU B CA   1 
ATOM   3606 C C    . LEU B 1 153 ? 122.36000 124.43300 128.37800 1.000 25.67778  ? 153 LEU B C    1 
ATOM   3607 O O    . LEU B 1 153 ? 122.34400 125.50500 129.00000 1.000 33.01645  ? 153 LEU B O    1 
ATOM   3608 C CB   . LEU B 1 153 ? 122.61900 124.38600 125.87700 1.000 27.87252  ? 153 LEU B CB   1 
ATOM   3609 C CG   . LEU B 1 153 ? 122.65000 125.76700 125.22500 1.000 25.47971  ? 153 LEU B CG   1 
ATOM   3610 C CD1  . LEU B 1 153 ? 121.97500 125.72200 123.86700 1.000 27.35113  ? 153 LEU B CD1  1 
ATOM   3611 C CD2  . LEU B 1 153 ? 121.98600 126.78800 126.11700 1.000 28.28107  ? 153 LEU B CD2  1 
ATOM   3612 N N    . ALA B 1 154 ? 121.53300 123.42600 128.67500 1.000 31.48220  ? 154 ALA B N    1 
ATOM   3613 C CA   . ALA B 1 154 ? 120.59000 123.55000 129.77900 1.000 27.77627  ? 154 ALA B CA   1 
ATOM   3614 C C    . ALA B 1 154 ? 121.31400 123.76200 131.09900 1.000 29.37915  ? 154 ALA B C    1 
ATOM   3615 O O    . ALA B 1 154 ? 120.90600 124.60100 131.90800 1.000 36.38270  ? 154 ALA B O    1 
ATOM   3616 C CB   . ALA B 1 154 ? 119.69300 122.31400 129.85100 1.000 24.79555  ? 154 ALA B CB   1 
ATOM   3617 N N    . LEU B 1 155 ? 122.39000 123.00900 131.34000 1.000 37.80035  ? 155 LEU B N    1 
ATOM   3618 C CA   . LEU B 1 155 ? 123.11800 123.17000 132.59500 1.000 39.76738  ? 155 LEU B CA   1 
ATOM   3619 C C    . LEU B 1 155 ? 123.73900 124.55800 132.69600 1.000 43.84905  ? 155 LEU B C    1 
ATOM   3620 O O    . LEU B 1 155 ? 123.69500 125.19200 133.76000 1.000 44.55994  ? 155 LEU B O    1 
ATOM   3621 C CB   . LEU B 1 155 ? 124.18600 122.08600 132.72800 1.000 38.49600  ? 155 LEU B CB   1 
ATOM   3622 C CG   . LEU B 1 155 ? 123.76100 120.86600 133.54600 1.000 38.97129  ? 155 LEU B CG   1 
ATOM   3623 C CD1  . LEU B 1 155 ? 124.62700 119.66400 133.21700 1.000 40.97395  ? 155 LEU B CD1  1 
ATOM   3624 C CD2  . LEU B 1 155 ? 123.81100 121.17900 135.02800 1.000 43.86160  ? 155 LEU B CD2  1 
ATOM   3625 N N    . GLY B 1 156 ? 124.31100 125.05700 131.59800 1.000 42.75985  ? 156 GLY B N    1 
ATOM   3626 C CA   . GLY B 1 156 ? 124.88300 126.39400 131.63100 1.000 40.28906  ? 156 GLY B CA   1 
ATOM   3627 C C    . GLY B 1 156 ? 123.85300 127.47300 131.91200 1.000 46.00461  ? 156 GLY B C    1 
ATOM   3628 O O    . GLY B 1 156 ? 124.08800 128.37500 132.72200 1.000 45.95949  ? 156 GLY B O    1 
ATOM   3629 N N    . MET B 1 157 ? 122.69100 127.39300 131.25700 1.000 50.98922  ? 157 MET B N    1 
ATOM   3630 C CA   . MET B 1 157 ? 121.65200 128.38800 131.51500 1.000 49.99074  ? 157 MET B CA   1 
ATOM   3631 C C    . MET B 1 157 ? 121.09300 128.26800 132.92800 1.000 49.23170  ? 157 MET B C    1 
ATOM   3632 O O    . MET B 1 157 ? 120.77400 129.28200 133.56100 1.000 48.39961  ? 157 MET B O    1 
ATOM   3633 C CB   . MET B 1 157 ? 120.53300 128.28000 130.48000 1.000 45.36655  ? 157 MET B CB   1 
ATOM   3634 C CG   . MET B 1 157 ? 120.01300 129.63500 130.02100 1.000 49.55239  ? 157 MET B CG   1 
ATOM   3635 S SD   . MET B 1 157 ? 120.96400 130.40400 128.70000 1.000 63.51172  ? 157 MET B SD   1 
ATOM   3636 C CE   . MET B 1 157 ? 120.68000 129.25100 127.36700 1.000 51.47660  ? 157 MET B CE   1 
ATOM   3637 N N    . ALA B 1 158 ? 120.97700 127.04500 133.44900 1.000 51.63176  ? 158 ALA B N    1 
ATOM   3638 C CA   . ALA B 1 158 ? 120.50700 126.88200 134.81900 1.000 50.50389  ? 158 ALA B CA   1 
ATOM   3639 C C    . ALA B 1 158 ? 121.48400 127.50100 135.80600 1.000 53.43258  ? 158 ALA B C    1 
ATOM   3640 O O    . ALA B 1 158 ? 121.07500 128.10500 136.80400 1.000 55.23623  ? 158 ALA B O    1 
ATOM   3641 C CB   . ALA B 1 158 ? 120.29400 125.40300 135.13000 1.000 53.08174  ? 158 ALA B CB   1 
ATOM   3642 N N    . GLU B 1 159 ? 122.78400 127.35500 135.54700 1.000 60.86246  ? 159 GLU B N    1 
ATOM   3643 C CA   . GLU B 1 159 ? 123.77600 128.01300 136.39000 1.000 58.88173  ? 159 GLU B CA   1 
ATOM   3644 C C    . GLU B 1 159 ? 123.64100 129.52900 136.30500 1.000 61.64129  ? 159 GLU B C    1 
ATOM   3645 O O    . GLU B 1 159 ? 123.61600 130.22200 137.32800 1.000 59.22816  ? 159 GLU B O    1 
ATOM   3646 C CB   . GLU B 1 159 ? 125.18200 127.57100 135.98600 1.000 61.56095  ? 159 GLU B CB   1 
ATOM   3647 C CG   . GLU B 1 159 ? 126.26300 127.97300 136.97200 1.000 62.72208  ? 159 GLU B CG   1 
ATOM   3648 C CD   . GLU B 1 159 ? 126.13300 127.25800 138.30100 1.000 65.34296  ? 159 GLU B CD   1 
ATOM   3649 O OE1  . GLU B 1 159 ? 126.05800 126.01200 138.30100 1.000 63.17729  ? 159 GLU B OE1  1 
ATOM   3650 O OE2  . GLU B 1 159 ? 126.10300 127.94200 139.34600 1.000 66.81882  ? 159 GLU B OE2  1 
ATOM   3651 N N    . LEU B 1 160 ? 123.55100 130.06100 135.08400 1.000 65.97243  ? 160 LEU B N    1 
ATOM   3652 C CA   . LEU B 1 160 ? 123.48600 131.51000 134.90700 1.000 63.23321  ? 160 LEU B CA   1 
ATOM   3653 C C    . LEU B 1 160 ? 122.22400 132.11200 135.52200 1.000 64.69048  ? 160 LEU B C    1 
ATOM   3654 O O    . LEU B 1 160 ? 122.23800 133.26900 135.95300 1.000 63.75952  ? 160 LEU B O    1 
ATOM   3655 C CB   . LEU B 1 160 ? 123.57400 131.84300 133.41400 1.000 62.60461  ? 160 LEU B CB   1 
ATOM   3656 C CG   . LEU B 1 160 ? 123.78800 133.26800 132.89300 1.000 65.36279  ? 160 LEU B CG   1 
ATOM   3657 C CD1  . LEU B 1 160 ? 123.73100 133.26400 131.37500 1.000 64.24200  ? 160 LEU B CD1  1 
ATOM   3658 C CD2  . LEU B 1 160 ? 122.77800 134.25800 133.44300 1.000 66.51681  ? 160 LEU B CD2  1 
ATOM   3659 N N    . SER B 1 161 ? 121.13500 131.34100 135.59400 1.000 71.37799  ? 161 SER B N    1 
ATOM   3660 C CA   . SER B 1 161 ? 119.86400 131.88800 136.06800 1.000 68.53634  ? 161 SER B CA   1 
ATOM   3661 C C    . SER B 1 161 ? 119.97200 132.51000 137.45700 1.000 69.33927  ? 161 SER B C    1 
ATOM   3662 O O    . SER B 1 161 ? 119.19300 133.40900 137.79100 1.000 70.48480  ? 161 SER B O    1 
ATOM   3663 C CB   . SER B 1 161 ? 118.79300 130.79900 136.07200 1.000 65.71085  ? 161 SER B CB   1 
ATOM   3664 O OG   . SER B 1 161 ? 118.94700 129.93900 137.18600 1.000 67.86973  ? 161 SER B OG   1 
ATOM   3665 N N    . THR B 1 162 ? 120.91400 132.04600 138.28000 1.000 76.93690  ? 162 THR B N    1 
ATOM   3666 C CA   . THR B 1 162 ? 120.97800 132.50500 139.66500 1.000 75.01892  ? 162 THR B CA   1 
ATOM   3667 C C    . THR B 1 162 ? 121.18100 134.01300 139.75600 1.000 74.76697  ? 162 THR B C    1 
ATOM   3668 O O    . THR B 1 162 ? 120.58900 134.67100 140.62100 1.000 74.37384  ? 162 THR B O    1 
ATOM   3669 C CB   . THR B 1 162 ? 122.09200 131.77200 140.41200 1.000 75.45645  ? 162 THR B CB   1 
ATOM   3670 O OG1  . THR B 1 162 ? 123.35100 132.04000 139.78200 1.000 77.27679  ? 162 THR B OG1  1 
ATOM   3671 C CG2  . THR B 1 162 ? 121.83600 130.27300 140.41200 1.000 73.93931  ? 162 THR B CG2  1 
ATOM   3672 N N    . LEU B 1 163 ? 122.02600 134.57700 138.88800 1.000 80.42997  ? 163 LEU B N    1 
ATOM   3673 C CA   . LEU B 1 163 ? 122.33200 136.00500 138.95200 1.000 79.40029  ? 163 LEU B CA   1 
ATOM   3674 C C    . LEU B 1 163 ? 121.07400 136.84800 139.13200 1.000 80.44552  ? 163 LEU B C    1 
ATOM   3675 O O    . LEU B 1 163 ? 121.01800 137.72200 140.00400 1.000 81.45617  ? 163 LEU B O    1 
ATOM   3676 C CB   . LEU B 1 163 ? 123.08900 136.43500 137.69400 1.000 80.17301  ? 163 LEU B CB   1 
ATOM   3677 C CG   . LEU B 1 163 ? 124.55000 135.99700 137.58400 1.000 81.11713  ? 163 LEU B CG   1 
ATOM   3678 C CD1  . LEU B 1 163 ? 124.65400 134.50400 137.32400 1.000 80.23839  ? 163 LEU B CD1  1 
ATOM   3679 C CD2  . LEU B 1 163 ? 125.25900 136.78400 136.49400 1.000 80.63167  ? 163 LEU B CD2  1 
ATOM   3680 N N    . PHE B 1 164 ? 120.04900 136.60100 138.31400 1.000 83.65886  ? 164 PHE B N    1 
ATOM   3681 C CA   . PHE B 1 164 ? 118.76300 137.28300 138.46800 1.000 83.10551  ? 164 PHE B CA   1 
ATOM   3682 C C    . PHE B 1 164 ? 117.99100 136.64100 139.62200 1.000 85.09679  ? 164 PHE B C    1 
ATOM   3683 O O    . PHE B 1 164 ? 117.01700 135.90700 139.44500 1.000 84.92821  ? 164 PHE B O    1 
ATOM   3684 C CB   . PHE B 1 164 ? 117.96900 137.25000 137.16900 1.000 81.97762  ? 164 PHE B CB   1 
ATOM   3685 C CG   . PHE B 1 164 ? 118.82300 137.25500 135.93500 1.000 84.03660  ? 164 PHE B CG   1 
ATOM   3686 C CD1  . PHE B 1 164 ? 119.61500 138.35000 135.63200 1.000 83.09114  ? 164 PHE B CD1  1 
ATOM   3687 C CD2  . PHE B 1 164 ? 118.82900 136.17300 135.07300 1.000 83.92086  ? 164 PHE B CD2  1 
ATOM   3688 C CE1  . PHE B 1 164 ? 120.39900 138.36300 134.49700 1.000 83.47448  ? 164 PHE B CE1  1 
ATOM   3689 C CE2  . PHE B 1 164 ? 119.61200 136.18100 133.93600 1.000 83.38410  ? 164 PHE B CE2  1 
ATOM   3690 C CZ   . PHE B 1 164 ? 120.39800 137.27700 133.64700 1.000 83.63113  ? 164 PHE B CZ   1 
ATOM   3691 N N    . GLY B 1 165 ? 118.46000 136.93800 140.83500 1.000 88.01063  ? 165 GLY B N    1 
ATOM   3692 C CA   . GLY B 1 165 ? 117.88500 136.31500 142.01600 1.000 88.19044  ? 165 GLY B CA   1 
ATOM   3693 C C    . GLY B 1 165 ? 116.39600 136.56800 142.15600 1.000 89.22911  ? 165 GLY B C    1 
ATOM   3694 O O    . GLY B 1 165 ? 115.62700 135.65200 142.45700 1.000 87.40678  ? 165 GLY B O    1 
ATOM   3695 N N    . ASP B 1 166 ? 115.96900 137.81400 141.94200 1.000 90.53707  ? 166 ASP B N    1 
ATOM   3696 C CA   . ASP B 1 166 ? 114.57200 138.16200 142.17600 1.000 90.09466  ? 166 ASP B CA   1 
ATOM   3697 C C    . ASP B 1 166 ? 113.64100 137.41500 141.22800 1.000 90.80641  ? 166 ASP B C    1 
ATOM   3698 O O    . ASP B 1 166 ? 112.57200 136.95000 141.63900 1.000 89.87611  ? 166 ASP B O    1 
ATOM   3699 C CB   . ASP B 1 166 ? 114.37800 139.67200 142.03600 1.000 89.25909  ? 166 ASP B CB   1 
ATOM   3700 N N    . TRP B 1 167 ? 114.02400 137.28900 139.95900 1.000 88.97967  ? 167 TRP B N    1 
ATOM   3701 C CA   . TRP B 1 167 ? 113.18300 136.64600 138.94900 1.000 87.44277  ? 167 TRP B CA   1 
ATOM   3702 C C    . TRP B 1 167 ? 113.93900 135.46800 138.34100 1.000 86.32559  ? 167 TRP B C    1 
ATOM   3703 O O    . TRP B 1 167 ? 114.51100 135.56900 137.25400 1.000 87.47151  ? 167 TRP B O    1 
ATOM   3704 C CB   . TRP B 1 167 ? 112.75300 137.65700 137.87500 1.000 86.93460  ? 167 TRP B CB   1 
ATOM   3705 C CG   . TRP B 1 167 ? 112.52500 139.03900 138.40300 1.000 87.78763  ? 167 TRP B CG   1 
ATOM   3706 C CD1  . TRP B 1 167 ? 111.70500 139.39800 139.43200 1.000 87.68973  ? 167 TRP B CD1  1 
ATOM   3707 C CD2  . TRP B 1 167 ? 113.11400 140.25200 137.91900 1.000 89.59973  ? 167 TRP B CD2  1 
ATOM   3708 N NE1  . TRP B 1 167 ? 111.75200 140.75800 139.62300 1.000 88.01683  ? 167 TRP B NE1  1 
ATOM   3709 C CE2  . TRP B 1 167 ? 112.60900 141.30500 138.70600 1.000 88.89412  ? 167 TRP B CE2  1 
ATOM   3710 C CE3  . TRP B 1 167 ? 114.02200 140.54900 136.89700 1.000 89.36543  ? 167 TRP B CE3  1 
ATOM   3711 C CZ2  . TRP B 1 167 ? 112.98100 142.63200 138.50500 1.000 88.26400  ? 167 TRP B CZ2  1 
ATOM   3712 C CZ3  . TRP B 1 167 ? 114.39000 141.86700 136.69900 1.000 88.96288  ? 167 TRP B CZ3  1 
ATOM   3713 C CH2  . TRP B 1 167 ? 113.87100 142.89200 137.49900 1.000 87.96071  ? 167 TRP B CH2  1 
ATOM   3714 N N    . GLU B 1 168 ? 113.93300 134.34000 139.05300 1.000 77.06921  ? 168 GLU B N    1 
ATOM   3715 C CA   . GLU B 1 168 ? 114.53600 133.11900 138.53000 1.000 77.63871  ? 168 GLU B CA   1 
ATOM   3716 C C    . GLU B 1 168 ? 113.59700 132.42800 137.54900 1.000 76.40039  ? 168 GLU B C    1 
ATOM   3717 O O    . GLU B 1 168 ? 113.98800 132.09100 136.42300 1.000 75.71114  ? 168 GLU B O    1 
ATOM   3718 C CB   . GLU B 1 168 ? 114.89500 132.17700 139.68100 1.000 77.71400  ? 168 GLU B CB   1 
ATOM   3719 C CG   . GLU B 1 168 ? 115.96600 131.15500 139.34000 1.000 79.43520  ? 168 GLU B CG   1 
ATOM   3720 C CD   . GLU B 1 168 ? 117.31500 131.50300 139.93400 1.000 80.79069  ? 168 GLU B CD   1 
ATOM   3721 O OE1  . GLU B 1 168 ? 117.51200 132.67500 140.31800 1.000 79.46854  ? 168 GLU B OE1  1 
ATOM   3722 O OE2  . GLU B 1 168 ? 118.17700 130.60400 140.01800 1.000 79.74667  ? 168 GLU B OE2  1 
ATOM   3723 N N    . GLU B 1 169 ? 112.34400 132.22600 137.96300 1.000 71.01004  ? 169 GLU B N    1 
ATOM   3724 C CA   . GLU B 1 169 ? 111.38600 131.52200 137.12400 1.000 69.60897  ? 169 GLU B CA   1 
ATOM   3725 C C    . GLU B 1 169 ? 111.04700 132.32000 135.87500 1.000 69.43496  ? 169 GLU B C    1 
ATOM   3726 O O    . GLU B 1 169 ? 110.75300 131.73000 134.83300 1.000 70.41805  ? 169 GLU B O    1 
ATOM   3727 C CB   . GLU B 1 169 ? 110.11900 131.21400 137.92000 1.000 71.46973  ? 169 GLU B CB   1 
ATOM   3728 C CG   . GLU B 1 169 ? 109.59000 132.39000 138.72000 1.000 73.17539  ? 169 GLU B CG   1 
ATOM   3729 C CD   . GLU B 1 169 ? 110.15200 132.43900 140.12500 1.000 72.82610  ? 169 GLU B CD   1 
ATOM   3730 O OE1  . GLU B 1 169 ? 111.27700 131.94200 140.33300 1.000 72.08948  ? 169 GLU B OE1  1 
ATOM   3731 O OE2  . GLU B 1 169 ? 109.46800 132.97600 141.02200 1.000 73.97803  ? 169 GLU B OE2  1 
ATOM   3732 N N    . ILE B 1 170 ? 111.10900 133.65000 135.94400 1.000 64.97197  ? 170 ILE B N    1 
ATOM   3733 C CA   . ILE B 1 170 ? 110.83600 134.45700 134.76000 1.000 63.66413  ? 170 ILE B CA   1 
ATOM   3734 C C    . ILE B 1 170 ? 111.90600 134.22300 133.70100 1.000 62.41920  ? 170 ILE B C    1 
ATOM   3735 O O    . ILE B 1 170 ? 111.60200 134.01700 132.52200 1.000 64.05014  ? 170 ILE B O    1 
ATOM   3736 C CB   . ILE B 1 170 ? 110.73000 135.94600 135.13500 1.000 64.20762  ? 170 ILE B CB   1 
ATOM   3737 C CG1  . ILE B 1 170 ? 109.54900 136.17500 136.08000 1.000 62.58913  ? 170 ILE B CG1  1 
ATOM   3738 C CG2  . ILE B 1 170 ? 110.59400 136.80100 133.88600 1.000 63.58540  ? 170 ILE B CG2  1 
ATOM   3739 C CD1  . ILE B 1 170 ? 108.27100 135.50600 135.63200 1.000 61.37946  ? 170 ILE B CD1  1 
ATOM   3740 N N    . PHE B 1 171 ? 113.17600 134.22800 134.10800 1.000 57.55028  ? 171 PHE B N    1 
ATOM   3741 C CA   . PHE B 1 171 ? 114.26000 133.98200 133.16000 1.000 58.40233  ? 171 PHE B CA   1 
ATOM   3742 C C    . PHE B 1 171 ? 114.21100 132.55000 132.63300 1.000 58.30844  ? 171 PHE B C    1 
ATOM   3743 O O    . PHE B 1 171 ? 114.41500 132.30700 131.43000 1.000 59.16250  ? 171 PHE B O    1 
ATOM   3744 C CB   . PHE B 1 171 ? 115.59800 134.28900 133.83800 1.000 57.87783  ? 171 PHE B CB   1 
ATOM   3745 C CG   . PHE B 1 171 ? 116.80200 133.79400 133.08900 1.000 60.45225  ? 171 PHE B CG   1 
ATOM   3746 C CD1  . PHE B 1 171 ? 117.36400 134.55200 132.07700 1.000 60.31572  ? 171 PHE B CD1  1 
ATOM   3747 C CD2  . PHE B 1 171 ? 117.39400 132.58700 133.42100 1.000 61.63066  ? 171 PHE B CD2  1 
ATOM   3748 C CE1  . PHE B 1 171 ? 118.47900 134.10600 131.39700 1.000 60.90391  ? 171 PHE B CE1  1 
ATOM   3749 C CE2  . PHE B 1 171 ? 118.50800 132.13700 132.74300 1.000 60.09750  ? 171 PHE B CE2  1 
ATOM   3750 C CZ   . PHE B 1 171 ? 119.05200 132.89800 131.73000 1.000 60.42894  ? 171 PHE B CZ   1 
ATOM   3751 N N    . CYS B 1 172 ? 113.87400 131.59400 133.50200 1.000 52.49585  ? 172 CYS B N    1 
ATOM   3752 C CA   . CYS B 1 172 ? 113.82500 130.20900 133.05100 1.000 50.87345  ? 172 CYS B CA   1 
ATOM   3753 C C    . CYS B 1 172 ? 112.67700 129.99100 132.07500 1.000 53.48928  ? 172 CYS B C    1 
ATOM   3754 O O    . CYS B 1 172 ? 112.82100 129.24300 131.10100 1.000 57.31869  ? 172 CYS B O    1 
ATOM   3755 C CB   . CYS B 1 172 ? 113.70200 129.27100 134.25000 1.000 51.68718  ? 172 CYS B CB   1 
ATOM   3756 S SG   . CYS B 1 172 ? 115.27100 128.92000 135.07400 1.000 65.05066  ? 172 CYS B SG   1 
ATOM   3757 N N    . THR B 1 173 ? 111.53200 130.63400 132.30900 1.000 48.48635  ? 173 THR B N    1 
ATOM   3758 C CA   . THR B 1 173 ? 110.42500 130.55100 131.36900 1.000 44.94579  ? 173 THR B CA   1 
ATOM   3759 C C    . THR B 1 173 ? 110.62500 131.44400 130.15400 1.000 42.27769  ? 173 THR B C    1 
ATOM   3760 O O    . THR B 1 173 ? 109.88200 131.30400 129.17700 1.000 45.21206  ? 173 THR B O    1 
ATOM   3761 C CB   . THR B 1 173 ? 109.11100 130.91600 132.06400 1.000 46.80450  ? 173 THR B CB   1 
ATOM   3762 O OG1  . THR B 1 173 ? 108.00600 130.47400 131.26700 1.000 45.48620  ? 173 THR B OG1  1 
ATOM   3763 C CG2  . THR B 1 173 ? 109.01500 132.41800 132.25800 1.000 49.16281  ? 173 THR B CG2  1 
ATOM   3764 N N    . LEU B 1 174 ? 111.60600 132.34900 130.18500 1.000 40.26158  ? 174 LEU B N    1 
ATOM   3765 C CA   . LEU B 1 174 ? 111.91100 133.15600 129.01500 1.000 39.89615  ? 174 LEU B CA   1 
ATOM   3766 C C    . LEU B 1 174 ? 112.99400 132.52700 128.15700 1.000 42.27331  ? 174 LEU B C    1 
ATOM   3767 O O    . LEU B 1 174 ? 113.27700 133.03300 127.06700 1.000 41.26778  ? 174 LEU B O    1 
ATOM   3768 C CB   . LEU B 1 174 ? 112.34200 134.56400 129.43700 1.000 42.11160  ? 174 LEU B CB   1 
ATOM   3769 C CG   . LEU B 1 174 ? 112.51300 135.58400 128.31100 1.000 44.61279  ? 174 LEU B CG   1 
ATOM   3770 C CD1  . LEU B 1 174 ? 112.13800 136.97400 128.79000 1.000 43.00584  ? 174 LEU B CD1  1 
ATOM   3771 C CD2  . LEU B 1 174 ? 113.93900 135.56300 127.78700 1.000 44.71426  ? 174 LEU B CD2  1 
ATOM   3772 N N    . SER B 1 175 ? 113.59500 131.43700 128.62700 1.000 39.18160  ? 175 SER B N    1 
ATOM   3773 C CA   . SER B 1 175 ? 114.64000 130.77700 127.85500 1.000 31.00694  ? 175 SER B CA   1 
ATOM   3774 C C    . SER B 1 175 ? 114.05500 129.64600 127.02100 1.000 32.00826  ? 175 SER B C    1 
ATOM   3775 O O    . SER B 1 175 ? 114.56300 129.34100 125.93000 1.000 35.35775  ? 175 SER B O    1 
ATOM   3776 C CB   . SER B 1 175 ? 115.72900 130.22900 128.78100 1.000 37.00616  ? 175 SER B CB   1 
ATOM   3777 O OG   . SER B 1 175 ? 116.40300 131.27400 129.45800 1.000 44.59068  ? 175 SER B OG   1 
ATOM   3778 N N    . ILE B 1 176 ? 112.94100 129.08400 127.49300 1.000 31.81360  ? 176 ILE B N    1 
ATOM   3779 C CA   . ILE B 1 176 ? 112.23100 128.03300 126.77400 1.000 25.05974  ? 176 ILE B CA   1 
ATOM   3780 C C    . ILE B 1 176 ? 111.63700 128.57700 125.48300 1.000 23.23131  ? 176 ILE B C    1 
ATOM   3781 O O    . ILE B 1 176 ? 111.66300 127.90800 124.44700 1.000 22.78222  ? 176 ILE B O    1 
ATOM   3782 C CB   . ILE B 1 176 ? 111.14500 127.41500 127.67600 1.000 25.71900  ? 176 ILE B CB   1 
ATOM   3783 C CG1  . ILE B 1 176 ? 111.77600 126.67800 128.86000 1.000 24.62661  ? 176 ILE B CG1  1 
ATOM   3784 C CG2  . ILE B 1 176 ? 110.24400 126.48700 126.87800 1.000 26.95891  ? 176 ILE B CG2  1 
ATOM   3785 C CD1  . ILE B 1 176 ? 110.78800 126.26900 129.92900 1.000 27.05212  ? 176 ILE B CD1  1 
ATOM   3786 N N    . PHE B 1 177 ? 111.11100 129.80300 125.51800 1.000 19.53046  ? 177 PHE B N    1 
ATOM   3787 C CA   . PHE B 1 177 ? 110.56800 130.42100 124.31200 1.000 23.14898  ? 177 PHE B CA   1 
ATOM   3788 C C    . PHE B 1 177 ? 111.64400 130.63000 123.25200 1.000 28.16470  ? 177 PHE B C    1 
ATOM   3789 O O    . PHE B 1 177 ? 111.45500 130.27000 122.08300 1.000 31.68271  ? 177 PHE B O    1 
ATOM   3790 C CB   . PHE B 1 177 ? 109.90700 131.75500 124.67500 1.000 24.81467  ? 177 PHE B CB   1 
ATOM   3791 C CG   . PHE B 1 177 ? 109.27800 132.46800 123.50800 1.000 30.49808  ? 177 PHE B CG   1 
ATOM   3792 C CD1  . PHE B 1 177 ? 110.03500 133.29600 122.69500 1.000 27.19252  ? 177 PHE B CD1  1 
ATOM   3793 C CD2  . PHE B 1 177 ? 107.93100 132.32600 123.23300 1.000 33.27077  ? 177 PHE B CD2  1 
ATOM   3794 C CE1  . PHE B 1 177 ? 109.46500 133.95200 121.62400 1.000 19.78579  ? 177 PHE B CE1  1 
ATOM   3795 C CE2  . PHE B 1 177 ? 107.35400 132.98400 122.16200 1.000 29.72585  ? 177 PHE B CE2  1 
ATOM   3796 C CZ   . PHE B 1 177 ? 108.12200 133.79600 121.35800 1.000 22.30019  ? 177 PHE B CZ   1 
ATOM   3797 N N    . CYS B 1 178 ? 112.79900 131.16700 123.64800 1.000 24.40963  ? 178 CYS B N    1 
ATOM   3798 C CA   . CYS B 1 178 ? 113.85000 131.44900 122.67500 1.000 22.48877  ? 178 CYS B CA   1 
ATOM   3799 C C    . CYS B 1 178 ? 114.51400 130.18000 122.15800 1.000 15.82888  ? 178 CYS B C    1 
ATOM   3800 O O    . CYS B 1 178 ? 114.86200 130.10700 120.96800 1.000 26.35375  ? 178 CYS B O    1 
ATOM   3801 C CB   . CYS B 1 178 ? 114.89700 132.37400 123.29400 1.000 23.34114  ? 178 CYS B CB   1 
ATOM   3802 S SG   . CYS B 1 178 ? 114.21800 133.85500 124.07400 1.000 42.36958  ? 178 CYS B SG   1 
ATOM   3803 N N    . ILE B 1 179 ? 114.52300 129.11400 122.95100 1.000 17.76348  ? 179 ILE B N    1 
ATOM   3804 C CA   . ILE B 1 179 ? 115.11200 127.87800 122.45100 1.000 21.16903  ? 179 ILE B CA   1 
ATOM   3805 C C    . ILE B 1 179 ? 114.11600 127.09400 121.61200 1.000 22.16679  ? 179 ILE B C    1 
ATOM   3806 O O    . ILE B 1 179 ? 114.49300 126.50000 120.60000 1.000 25.81736  ? 179 ILE B O    1 
ATOM   3807 C CB   . ILE B 1 179 ? 115.64900 127.03700 123.62600 1.000 22.90738  ? 179 ILE B CB   1 
ATOM   3808 C CG1  . ILE B 1 179 ? 116.66300 127.84400 124.43600 1.000 27.29960  ? 179 ILE B CG1  1 
ATOM   3809 C CG2  . ILE B 1 179 ? 116.26700 125.74600 123.12100 1.000 17.92286  ? 179 ILE B CG2  1 
ATOM   3810 C CD1  . ILE B 1 179 ? 117.84800 128.31100 123.62800 1.000 23.93823  ? 179 ILE B CD1  1 
ATOM   3811 N N    . GLY B 1 180 ? 112.83100 127.11100 121.96300 1.000 20.82185  ? 180 GLY B N    1 
ATOM   3812 C CA   . GLY B 1 180 ? 111.84800 126.49200 121.09700 1.000 17.61797  ? 180 GLY B CA   1 
ATOM   3813 C C    . GLY B 1 180 ? 111.77200 127.19500 119.75700 1.000 17.75330  ? 180 GLY B C    1 
ATOM   3814 O O    . GLY B 1 180 ? 111.67000 126.55000 118.71100 1.000 21.72663  ? 180 GLY B O    1 
ATOM   3815 N N    . PHE B 1 181 ? 111.88400 128.52800 119.76500 1.000 18.47607  ? 181 PHE B N    1 
ATOM   3816 C CA   . PHE B 1 181 ? 111.84100 129.27100 118.51300 1.000 14.22036  ? 181 PHE B CA   1 
ATOM   3817 C C    . PHE B 1 181 ? 113.05300 128.95400 117.64700 1.000 21.06128  ? 181 PHE B C    1 
ATOM   3818 O O    . PHE B 1 181 ? 112.91000 128.69700 116.44400 1.000 21.56186  ? 181 PHE B O    1 
ATOM   3819 C CB   . PHE B 1 181 ? 111.75600 130.77300 118.79500 1.000 18.00576  ? 181 PHE B CB   1 
ATOM   3820 C CG   . PHE B 1 181 ? 111.82800 131.62800 117.56000 1.000 28.01931  ? 181 PHE B CG   1 
ATOM   3821 C CD1  . PHE B 1 181 ? 110.68200 131.93700 116.85100 1.000 27.34356  ? 181 PHE B CD1  1 
ATOM   3822 C CD2  . PHE B 1 181 ? 113.03900 132.11900 117.10700 1.000 27.34679  ? 181 PHE B CD2  1 
ATOM   3823 C CE1  . PHE B 1 181 ? 110.74200 132.71700 115.71400 1.000 20.68935  ? 181 PHE B CE1  1 
ATOM   3824 C CE2  . PHE B 1 181 ? 113.10400 132.89800 115.97000 1.000 26.11178  ? 181 PHE B CE2  1 
ATOM   3825 C CZ   . PHE B 1 181 ? 111.95400 133.19800 115.27400 1.000 18.53495  ? 181 PHE B CZ   1 
ATOM   3826 N N    . LEU B 1 182 ? 114.25300 128.92600 118.23800 1.000 22.74762  ? 182 LEU B N    1 
ATOM   3827 C CA   . LEU B 1 182 ? 115.43100 128.67400 117.41400 1.000 16.57424  ? 182 LEU B CA   1 
ATOM   3828 C C    . LEU B 1 182 ? 115.46600 127.23200 116.91600 1.000 19.90814  ? 182 LEU B C    1 
ATOM   3829 O O    . LEU B 1 182 ? 115.83000 126.97900 115.75800 1.000 26.44684  ? 182 LEU B O    1 
ATOM   3830 C CB   . LEU B 1 182 ? 116.69900 129.00700 118.19700 1.000 22.55177  ? 182 LEU B CB   1 
ATOM   3831 C CG   . LEU B 1 182 ? 116.89200 130.48700 118.53200 1.000 22.37182  ? 182 LEU B CG   1 
ATOM   3832 C CD1  . LEU B 1 182 ? 117.84800 130.66200 119.69900 1.000 26.37663  ? 182 LEU B CD1  1 
ATOM   3833 C CD2  . LEU B 1 182 ? 117.38800 131.24200 117.31400 1.000 23.58212  ? 182 LEU B CD2  1 
ATOM   3834 N N    . ALA B 1 183 ? 115.02500 126.27900 117.74300 1.000 24.30948  ? 183 ALA B N    1 
ATOM   3835 C CA   . ALA B 1 183 ? 115.02700 124.88000 117.34000 1.000 20.11929  ? 183 ALA B CA   1 
ATOM   3836 C C    . ALA B 1 183 ? 113.91300 124.54800 116.36100 1.000 20.99579  ? 183 ALA B C    1 
ATOM   3837 O O    . ALA B 1 183 ? 114.03200 123.56400 115.62400 1.000 25.99262  ? 183 ALA B O    1 
ATOM   3838 C CB   . ALA B 1 183 ? 114.92200 123.97600 118.56900 1.000 14.88893  ? 183 ALA B CB   1 
ATOM   3839 N N    . THR B 1 184 ? 112.84300 125.34200 116.32100 1.000 21.58025  ? 184 THR B N    1 
ATOM   3840 C CA   . THR B 1 184 ? 111.81500 125.13500 115.31400 1.000 20.25736  ? 184 THR B CA   1 
ATOM   3841 C C    . THR B 1 184 ? 112.13300 125.85900 114.01800 1.000 24.79239  ? 184 THR B C    1 
ATOM   3842 O O    . THR B 1 184 ? 111.66400 125.44200 112.95400 1.000 28.35695  ? 184 THR B O    1 
ATOM   3843 C CB   . THR B 1 184 ? 110.45200 125.60000 115.83100 1.000 19.29051  ? 184 THR B CB   1 
ATOM   3844 O OG1  . THR B 1 184 ? 110.28800 125.18400 117.19100 1.000 30.33867  ? 184 THR B OG1  1 
ATOM   3845 C CG2  . THR B 1 184 ? 109.33400 125.01400 114.98400 1.000 16.47971  ? 184 THR B CG2  1 
ATOM   3846 N N    . PHE B 1 185 ? 112.92500 126.93100 114.07900 1.000 27.54379  ? 185 PHE B N    1 
ATOM   3847 C CA   . PHE B 1 185 ? 113.29600 127.61800 112.85100 1.000 23.91144  ? 185 PHE B CA   1 
ATOM   3848 C C    . PHE B 1 185 ? 114.46600 126.94100 112.15300 1.000 27.18277  ? 185 PHE B C    1 
ATOM   3849 O O    . PHE B 1 185 ? 114.56000 126.99900 110.92200 1.000 34.53490  ? 185 PHE B O    1 
ATOM   3850 C CB   . PHE B 1 185 ? 113.63500 129.08000 113.14000 1.000 24.96676  ? 185 PHE B CB   1 
ATOM   3851 C CG   . PHE B 1 185 ? 113.66900 129.94500 111.91500 1.000 25.01542  ? 185 PHE B CG   1 
ATOM   3852 C CD1  . PHE B 1 185 ? 112.52400 130.16100 111.17100 1.000 27.43279  ? 185 PHE B CD1  1 
ATOM   3853 C CD2  . PHE B 1 185 ? 114.85000 130.53200 111.50100 1.000 31.03058  ? 185 PHE B CD2  1 
ATOM   3854 C CE1  . PHE B 1 185 ? 112.55400 130.95200 110.04000 1.000 26.37441  ? 185 PHE B CE1  1 
ATOM   3855 C CE2  . PHE B 1 185 ? 114.88500 131.32400 110.37100 1.000 30.52605  ? 185 PHE B CE2  1 
ATOM   3856 C CZ   . PHE B 1 185 ? 113.73600 131.53300 109.64100 1.000 25.10450  ? 185 PHE B CZ   1 
ATOM   3857 N N    . MET B 1 186 ? 115.35500 126.28400 112.90200 1.000 34.27997  ? 186 MET B N    1 
ATOM   3858 C CA   . MET B 1 186 ? 116.48900 125.62200 112.26900 1.000 25.45474  ? 186 MET B CA   1 
ATOM   3859 C C    . MET B 1 186 ? 116.15600 124.24000 111.71800 1.000 25.13087  ? 186 MET B C    1 
ATOM   3860 O O    . MET B 1 186 ? 116.98500 123.66400 111.00700 1.000 30.07242  ? 186 MET B O    1 
ATOM   3861 C CB   . MET B 1 186 ? 117.65000 125.50800 113.25800 1.000 27.91967  ? 186 MET B CB   1 
ATOM   3862 C CG   . MET B 1 186 ? 118.21300 126.84500 113.70100 1.000 37.30979  ? 186 MET B CG   1 
ATOM   3863 S SD   . MET B 1 186 ? 119.26100 127.60300 112.44700 1.000 55.64737  ? 186 MET B SD   1 
ATOM   3864 C CE   . MET B 1 186 ? 119.18900 129.32100 112.94300 1.000 34.92463  ? 186 MET B CE   1 
ATOM   3865 N N    . LYS B 1 187 ? 114.97500 123.69600 112.01100 1.000 25.40454  ? 187 LYS B N    1 
ATOM   3866 C CA   . LYS B 1 187 ? 114.57200 122.40700 111.46500 1.000 26.44272  ? 187 LYS B CA   1 
ATOM   3867 C C    . LYS B 1 187 ? 113.70800 122.52600 110.21700 1.000 34.91330  ? 187 LYS B C    1 
ATOM   3868 O O    . LYS B 1 187 ? 113.38700 121.50100 109.60800 1.000 31.79546  ? 187 LYS B O    1 
ATOM   3869 C CB   . LYS B 1 187 ? 113.82400 121.58500 112.52100 1.000 28.88048  ? 187 LYS B CB   1 
ATOM   3870 C CG   . LYS B 1 187 ? 112.33700 121.86600 112.59400 1.000 32.69632  ? 187 LYS B CG   1 
ATOM   3871 C CD   . LYS B 1 187 ? 111.61900 120.80700 113.40700 1.000 29.35263  ? 187 LYS B CD   1 
ATOM   3872 C CE   . LYS B 1 187 ? 110.13800 120.77400 113.07900 1.000 34.28418  ? 187 LYS B CE   1 
ATOM   3873 N NZ   . LYS B 1 187 ? 109.29300 120.86600 114.30100 1.000 35.97345  ? 187 LYS B NZ   1 
ATOM   3874 N N    . LEU B 1 188 ? 113.32100 123.73800 109.82700 1.000 32.21181  ? 188 LEU B N    1 
ATOM   3875 C CA   . LEU B 1 188 ? 112.53200 123.95600 108.62400 1.000 25.94379  ? 188 LEU B CA   1 
ATOM   3876 C C    . LEU B 1 188 ? 113.39300 124.30600 107.42000 1.000 33.30586  ? 188 LEU B C    1 
ATOM   3877 O O    . LEU B 1 188 ? 112.85400 124.56000 106.34000 1.000 34.81969  ? 188 LEU B O    1 
ATOM   3878 C CB   . LEU B 1 188 ? 111.49500 125.05900 108.85700 1.000 30.38196  ? 188 LEU B CB   1 
ATOM   3879 C CG   . LEU B 1 188 ? 110.46800 124.81400 109.96200 1.000 30.04541  ? 188 LEU B CG   1 
ATOM   3880 C CD1  . LEU B 1 188 ? 109.63800 126.06100 110.21000 1.000 24.89601  ? 188 LEU B CD1  1 
ATOM   3881 C CD2  . LEU B 1 188 ? 109.57600 123.63800 109.60600 1.000 29.48092  ? 188 LEU B CD2  1 
ATOM   3882 N N    . TYR B 1 189 ? 114.71100 124.32200 107.58200 1.000 41.05835  ? 189 TYR B N    1 
ATOM   3883 C CA   . TYR B 1 189 ? 115.59800 124.56200 106.45700 1.000 38.84937  ? 189 TYR B CA   1 
ATOM   3884 C C    . TYR B 1 189 ? 115.56500 123.36600 105.50800 1.000 42.70127  ? 189 TYR B C    1 
ATOM   3885 O O    . TYR B 1 189 ? 115.55500 122.21600 105.95600 1.000 46.42459  ? 189 TYR B O    1 
ATOM   3886 C CB   . TYR B 1 189 ? 117.02300 124.80700 106.94900 1.000 37.02058  ? 189 TYR B CB   1 
ATOM   3887 C CG   . TYR B 1 189 ? 117.82200 125.74700 106.07900 1.000 43.89231  ? 189 TYR B CG   1 
ATOM   3888 C CD1  . TYR B 1 189 ? 117.68100 127.12200 106.19900 1.000 43.16665  ? 189 TYR B CD1  1 
ATOM   3889 C CD2  . TYR B 1 189 ? 118.71800 125.26000 105.13800 1.000 46.71931  ? 189 TYR B CD2  1 
ATOM   3890 C CE1  . TYR B 1 189 ? 118.41000 127.98600 105.40600 1.000 45.56181  ? 189 TYR B CE1  1 
ATOM   3891 C CE2  . TYR B 1 189 ? 119.45100 126.11500 104.33900 1.000 44.03224  ? 189 TYR B CE2  1 
ATOM   3892 C CZ   . TYR B 1 189 ? 119.29400 127.47700 104.47700 1.000 49.54436  ? 189 TYR B CZ   1 
ATOM   3893 O OH   . TYR B 1 189 ? 120.02200 128.33400 103.68400 1.000 49.44908  ? 189 TYR B OH   1 
ATOM   3894 N N    . PRO B 1 190 ? 115.54500 123.60200 104.19500 1.000 41.38541  ? 190 PRO B N    1 
ATOM   3895 C CA   . PRO B 1 190 ? 115.36800 122.48200 103.25500 1.000 43.48408  ? 190 PRO B CA   1 
ATOM   3896 C C    . PRO B 1 190 ? 116.47100 121.43900 103.32000 1.000 44.19366  ? 190 PRO B C    1 
ATOM   3897 O O    . PRO B 1 190 ? 116.22500 120.27500 102.97800 1.000 40.24713  ? 190 PRO B O    1 
ATOM   3898 C CB   . PRO B 1 190 ? 115.32900 123.18200 101.88800 1.000 45.37731  ? 190 PRO B CB   1 
ATOM   3899 C CG   . PRO B 1 190 ? 114.94700 124.59600 102.19500 1.000 43.78876  ? 190 PRO B CG   1 
ATOM   3900 C CD   . PRO B 1 190 ? 115.61100 124.89700 103.50000 1.000 41.88682  ? 190 PRO B CD   1 
ATOM   3901 N N    . SER B 1 191 ? 117.67900 121.81200 103.74400 1.000 44.03463  ? 191 SER B N    1 
ATOM   3902 C CA   . SER B 1 191 ? 118.78000 120.86000 103.82000 1.000 40.54974  ? 191 SER B CA   1 
ATOM   3903 C C    . SER B 1 191 ? 118.74800 119.99900 105.07700 1.000 47.40879  ? 191 SER B C    1 
ATOM   3904 O O    . SER B 1 191 ? 119.55400 119.07000 105.18800 1.000 47.71768  ? 191 SER B O    1 
ATOM   3905 C CB   . SER B 1 191 ? 120.11800 121.60000 103.74000 1.000 41.54974  ? 191 SER B CB   1 
ATOM   3906 O OG   . SER B 1 191 ? 120.19700 122.61900 104.71900 1.000 46.92853  ? 191 SER B OG   1 
ATOM   3907 N N    . MET B 1 192 ? 117.84500 120.27900 106.01700 1.000 47.02648  ? 192 MET B N    1 
ATOM   3908 C CA   . MET B 1 192 ? 117.76300 119.55700 107.28100 1.000 40.89103  ? 192 MET B CA   1 
ATOM   3909 C C    . MET B 1 192 ? 116.50600 118.70000 107.37900 1.000 40.83028  ? 192 MET B C    1 
ATOM   3910 O O    . MET B 1 192 ? 116.04700 118.40300 108.48600 1.000 46.10088  ? 192 MET B O    1 
ATOM   3911 C CB   . MET B 1 192 ? 117.82700 120.53300 108.45600 1.000 39.97663  ? 192 MET B CB   1 
ATOM   3912 C CG   . MET B 1 192 ? 118.93500 121.56300 108.36100 1.000 41.94307  ? 192 MET B CG   1 
ATOM   3913 S SD   . MET B 1 192 ? 120.50100 120.94400 109.00500 1.000 53.31221  ? 192 MET B SD   1 
ATOM   3914 C CE   . MET B 1 192 ? 121.50100 120.93400 107.52300 1.000 44.26109  ? 192 MET B CE   1 
ATOM   3915 N N    . LYS B 1 193 ? 115.93800 118.29800 106.24100 1.000 37.99845  ? 193 LYS B N    1 
ATOM   3916 C CA   . LYS B 1 193 ? 114.68200 117.55700 106.25700 1.000 41.86020  ? 193 LYS B CA   1 
ATOM   3917 C C    . LYS B 1 193 ? 114.85100 116.14300 106.79800 1.000 42.51351  ? 193 LYS B C    1 
ATOM   3918 O O    . LYS B 1 193 ? 113.89400 115.56700 107.32700 1.000 47.73449  ? 193 LYS B O    1 
ATOM   3919 C CB   . LYS B 1 193 ? 114.08400 117.51700 104.85100 1.000 43.84429  ? 193 LYS B CB   1 
ATOM   3920 C CG   . LYS B 1 193 ? 113.13900 116.35600 104.61100 1.000 42.90033  ? 193 LYS B CG   1 
ATOM   3921 C CD   . LYS B 1 193 ? 111.68800 116.79100 104.70200 1.000 44.48046  ? 193 LYS B CD   1 
ATOM   3922 C CE   . LYS B 1 193 ? 110.74700 115.61900 104.47700 1.000 47.67795  ? 193 LYS B CE   1 
ATOM   3923 N NZ   . LYS B 1 193 ? 109.54400 116.01200 103.69700 1.000 46.94604  ? 193 LYS B NZ   1 
ATOM   3924 N N    . ALA B 1 194 ? 116.03800 115.56100 106.66500 1.000 38.28840  ? 194 ALA B N    1 
ATOM   3925 C CA   . ALA B 1 194 ? 116.28600 114.19700 107.11000 1.000 40.31254  ? 194 ALA B CA   1 
ATOM   3926 C C    . ALA B 1 194 ? 116.81600 114.11000 108.53800 1.000 40.17852  ? 194 ALA B C    1 
ATOM   3927 O O    . ALA B 1 194 ? 117.19000 113.01800 108.97500 1.000 46.18449  ? 194 ALA B O    1 
ATOM   3928 C CB   . ALA B 1 194 ? 117.26200 113.50500 106.15600 1.000 40.13916  ? 194 ALA B CB   1 
ATOM   3929 N N    . TYR B 1 195 ? 116.86200 115.22300 109.27200 1.000 30.51236  ? 195 TYR B N    1 
ATOM   3930 C CA   . TYR B 1 195 ? 117.46600 115.24900 110.59900 1.000 26.70652  ? 195 TYR B CA   1 
ATOM   3931 C C    . TYR B 1 195 ? 116.50800 115.72400 111.68900 1.000 32.57255  ? 195 TYR B C    1 
ATOM   3932 O O    . TYR B 1 195 ? 116.94500 116.31100 112.67900 1.000 48.07180  ? 195 TYR B O    1 
ATOM   3933 C CB   . TYR B 1 195 ? 118.71700 116.12600 110.59100 1.000 33.26315  ? 195 TYR B CB   1 
ATOM   3934 C CG   . TYR B 1 195 ? 119.83300 115.60800 109.71500 1.000 37.30540  ? 195 TYR B CG   1 
ATOM   3935 C CD1  . TYR B 1 195 ? 120.22000 114.27700 109.76400 1.000 38.69408  ? 195 TYR B CD1  1 
ATOM   3936 C CD2  . TYR B 1 195 ? 120.49900 116.45200 108.83800 1.000 36.50082  ? 195 TYR B CD2  1 
ATOM   3937 C CE1  . TYR B 1 195 ? 121.23900 113.80100 108.96500 1.000 34.37679  ? 195 TYR B CE1  1 
ATOM   3938 C CE2  . TYR B 1 195 ? 121.51900 115.98500 108.03500 1.000 38.65443  ? 195 TYR B CE2  1 
ATOM   3939 C CZ   . TYR B 1 195 ? 121.88500 114.65900 108.10300 1.000 40.55251  ? 195 TYR B CZ   1 
ATOM   3940 O OH   . TYR B 1 195 ? 122.90200 114.18900 107.30500 1.000 41.46760  ? 195 TYR B OH   1 
ATOM   3941 N N    . GLU B 1 196 ? 115.20200 115.49200 111.53900 1.000 28.15823  ? 196 GLU B N    1 
ATOM   3942 C CA   . GLU B 1 196 ? 114.27300 115.98900 112.55100 1.000 34.69142  ? 196 GLU B CA   1 
ATOM   3943 C C    . GLU B 1 196 ? 114.32800 115.18100 113.84200 1.000 32.62065  ? 196 GLU B C    1 
ATOM   3944 O O    . GLU B 1 196 ? 113.95800 115.70000 114.90900 1.000 37.69171  ? 196 GLU B O    1 
ATOM   3945 C CB   . GLU B 1 196 ? 112.84800 115.98800 112.00000 1.000 33.17792  ? 196 GLU B CB   1 
ATOM   3946 C CG   . GLU B 1 196 ? 112.40600 117.32700 111.44900 1.000 37.66438  ? 196 GLU B CG   1 
ATOM   3947 C CD   . GLU B 1 196 ? 113.02200 117.62800 110.09900 1.000 41.61058  ? 196 GLU B CD   1 
ATOM   3948 O OE1  . GLU B 1 196 ? 112.75700 116.87100 109.14500 1.000 42.72390  ? 196 GLU B OE1  1 
ATOM   3949 O OE2  . GLU B 1 196 ? 113.77500 118.61700 109.99300 1.000 40.74090  ? 196 GLU B OE2  1 
ATOM   3950 N N    . TYR B 1 197 ? 114.85000 113.95500 113.78500 1.000 17.94979  ? 197 TYR B N    1 
ATOM   3951 C CA   . TYR B 1 197 ? 114.98900 113.14500 114.98500 1.000 17.18629  ? 197 TYR B CA   1 
ATOM   3952 C C    . TYR B 1 197 ? 116.11000 113.64400 115.88000 1.000 24.32134  ? 197 TYR B C    1 
ATOM   3953 O O    . TYR B 1 197 ? 116.18700 113.22700 117.03900 1.000 32.48259  ? 197 TYR B O    1 
ATOM   3954 C CB   . TYR B 1 197 ? 115.21600 111.67300 114.61700 1.000 19.44165  ? 197 TYR B CB   1 
ATOM   3955 C CG   . TYR B 1 197 ? 116.46500 111.40800 113.80500 1.000 20.40568  ? 197 TYR B CG   1 
ATOM   3956 C CD1  . TYR B 1 197 ? 116.46700 111.55500 112.42700 1.000 16.88262  ? 197 TYR B CD1  1 
ATOM   3957 C CD2  . TYR B 1 197 ? 117.64300 111.00800 114.42100 1.000 17.41619  ? 197 TYR B CD2  1 
ATOM   3958 C CE1  . TYR B 1 197 ? 117.60600 111.31600 111.68600 1.000 12.18855  ? 197 TYR B CE1  1 
ATOM   3959 C CE2  . TYR B 1 197 ? 118.78600 110.76800 113.68900 1.000 16.31059  ? 197 TYR B CE2  1 
ATOM   3960 C CZ   . TYR B 1 197 ? 118.76200 110.92300 112.32300 1.000 19.64671  ? 197 TYR B CZ   1 
ATOM   3961 O OH   . TYR B 1 197 ? 119.90000 110.68200 111.58800 1.000 19.98903  ? 197 TYR B OH   1 
ATOM   3962 N N    . GLY B 1 198 ? 116.97000 114.52500 115.37400 1.000 15.52839  ? 198 GLY B N    1 
ATOM   3963 C CA   . GLY B 1 198 ? 118.06100 115.06200 116.15800 1.000 12.93723  ? 198 GLY B CA   1 
ATOM   3964 C C    . GLY B 1 198 ? 117.70400 116.40600 116.75500 1.000 19.94740  ? 198 GLY B C    1 
ATOM   3965 O O    . GLY B 1 198 ? 118.33300 116.85000 117.71900 1.000 26.71353  ? 198 GLY B O    1 
ATOM   3966 N N    . PHE B 1 199 ? 116.69500 117.06700 116.18700 1.000 22.23527  ? 199 PHE B N    1 
ATOM   3967 C CA   . PHE B 1 199 ? 116.18200 118.30500 116.75900 1.000 19.92386  ? 199 PHE B CA   1 
ATOM   3968 C C    . PHE B 1 199 ? 115.10000 118.04300 117.79800 1.000 20.58587  ? 199 PHE B C    1 
ATOM   3969 O O    . PHE B 1 199 ? 114.98800 118.79200 118.78600 1.000 28.79665  ? 199 PHE B O    1 
ATOM   3970 C CB   . PHE B 1 199 ? 115.62300 119.20400 115.65200 1.000 20.93297  ? 199 PHE B CB   1 
ATOM   3971 C CG   . PHE B 1 199 ? 116.68000 119.89100 114.83200 1.000 23.34668  ? 199 PHE B CG   1 
ATOM   3972 C CD1  . PHE B 1 199 ? 117.24800 121.07800 115.25700 1.000 21.58368  ? 199 PHE B CD1  1 
ATOM   3973 C CD2  . PHE B 1 199 ? 117.09700 119.35100 113.62600 1.000 25.84158  ? 199 PHE B CD2  1 
ATOM   3974 C CE1  . PHE B 1 199 ? 118.21700 121.70800 114.49800 1.000 23.30188  ? 199 PHE B CE1  1 
ATOM   3975 C CE2  . PHE B 1 199 ? 118.06500 119.97800 112.86600 1.000 19.89912  ? 199 PHE B CE2  1 
ATOM   3976 C CZ   . PHE B 1 199 ? 118.62400 121.15600 113.30200 1.000 15.12700  ? 199 PHE B CZ   1 
ATOM   3977 N N    . ARG B 1 200 ? 114.35000 116.94900 117.63700 1.000 17.61916  ? 200 ARG B N    1 
ATOM   3978 C CA   . ARG B 1 200 ? 113.35200 116.61200 118.64400 1.000 17.08049  ? 200 ARG B CA   1 
ATOM   3979 C C    . ARG B 1 200 ? 114.01500 116.18000 119.94600 1.000 22.01535  ? 200 ARG B C    1 
ATOM   3980 O O    . ARG B 1 200 ? 113.55600 116.54800 121.03700 1.000 25.77442  ? 200 ARG B O    1 
ATOM   3981 C CB   . ARG B 1 200 ? 112.43600 115.51000 118.11400 1.000 22.45812  ? 200 ARG B CB   1 
ATOM   3982 C CG   . ARG B 1 200 ? 110.97000 115.68700 118.45500 1.000 25.81981  ? 200 ARG B CG   1 
ATOM   3983 C CD   . ARG B 1 200 ? 110.09300 114.87100 117.52400 1.000 28.50185  ? 200 ARG B CD   1 
ATOM   3984 N NE   . ARG B 1 200 ? 110.63200 113.53800 117.28600 1.000 38.80478  ? 200 ARG B NE   1 
ATOM   3985 C CZ   . ARG B 1 200 ? 110.69900 112.95800 116.09500 1.000 37.81623  ? 200 ARG B CZ   1 
ATOM   3986 N NH1  . ARG B 1 200 ? 110.27200 113.57200 115.00300 1.000 26.59369  ? 200 ARG B NH1  1 
ATOM   3987 N NH2  . ARG B 1 200 ? 111.20900 111.73400 115.99600 1.000 26.32524  ? 200 ARG B NH2  1 
ATOM   3988 N N    . VAL B 1 201 ? 115.13100 115.45200 119.85300 1.000 12.01279  ? 201 VAL B N    1 
ATOM   3989 C CA   . VAL B 1 201 ? 115.81700 115.01100 121.06100 1.000 19.37672  ? 201 VAL B CA   1 
ATOM   3990 C C    . VAL B 1 201 ? 116.47600 116.19300 121.75200 1.000 13.50774  ? 201 VAL B C    1 
ATOM   3991 O O    . VAL B 1 201 ? 116.56500 116.23200 122.98600 1.000 25.19835  ? 201 VAL B O    1 
ATOM   3992 C CB   . VAL B 1 201 ? 116.84100 113.91300 120.71400 1.000 12.49107  ? 201 VAL B CB   1 
ATOM   3993 C CG1  . VAL B 1 201 ? 117.87300 113.77200 121.81900 1.000 14.34354  ? 201 VAL B CG1  1 
ATOM   3994 C CG2  . VAL B 1 201 ? 116.13900 112.59200 120.46200 1.000 10.59338  ? 201 VAL B CG2  1 
ATOM   3995 N N    . PHE B 1 202 ? 116.82900 117.22500 120.98800 1.000 7.54605   ? 202 PHE B N    1 
ATOM   3996 C CA   . PHE B 1 202 ? 117.44900 118.40900 121.56800 1.000 6.67477   ? 202 PHE B CA   1 
ATOM   3997 C C    . PHE B 1 202 ? 116.42000 119.21800 122.34500 1.000 10.99372  ? 202 PHE B C    1 
ATOM   3998 O O    . PHE B 1 202 ? 116.65600 119.60500 123.49900 1.000 13.98794  ? 202 PHE B O    1 
ATOM   3999 C CB   . PHE B 1 202 ? 118.08600 119.24300 120.45100 1.000 6.91836   ? 202 PHE B CB   1 
ATOM   4000 C CG   . PHE B 1 202 ? 118.74100 120.51200 120.92000 1.000 19.40639  ? 202 PHE B CG   1 
ATOM   4001 C CD1  . PHE B 1 202 ? 117.99200 121.65500 121.14800 1.000 20.47431  ? 202 PHE B CD1  1 
ATOM   4002 C CD2  . PHE B 1 202 ? 120.10900 120.57000 121.10800 1.000 11.17698  ? 202 PHE B CD2  1 
ATOM   4003 C CE1  . PHE B 1 202 ? 118.59300 122.82200 121.57300 1.000 10.22219  ? 202 PHE B CE1  1 
ATOM   4004 C CE2  . PHE B 1 202 ? 120.71400 121.73600 121.53200 1.000 17.16224  ? 202 PHE B CE2  1 
ATOM   4005 C CZ   . PHE B 1 202 ? 119.95600 122.86100 121.76400 1.000 12.87385  ? 202 PHE B CZ   1 
ATOM   4006 N N    . LEU B 1 203 ? 115.24900 119.44400 121.74200 1.000 14.07912  ? 203 LEU B N    1 
ATOM   4007 C CA   . LEU B 1 203 ? 114.19700 120.15600 122.46100 1.000 8.09937   ? 203 LEU B CA   1 
ATOM   4008 C C    . LEU B 1 203 ? 113.75400 119.38900 123.70300 1.000 16.04429  ? 203 LEU B C    1 
ATOM   4009 O O    . LEU B 1 203 ? 113.58600 119.98000 124.78100 1.000 10.84981  ? 203 LEU B O    1 
ATOM   4010 C CB   . LEU B 1 203 ? 113.00700 120.41500 121.53800 1.000 13.36029  ? 203 LEU B CB   1 
ATOM   4011 C CG   . LEU B 1 203 ? 112.35600 121.79800 121.62300 1.000 15.64874  ? 203 LEU B CG   1 
ATOM   4012 C CD1  . LEU B 1 203 ? 113.38200 122.87400 121.92500 1.000 18.68084  ? 203 LEU B CD1  1 
ATOM   4013 C CD2  . LEU B 1 203 ? 111.60400 122.11700 120.34500 1.000 9.89416   ? 203 LEU B CD2  1 
ATOM   4014 N N    . LEU B 1 204 ? 113.58100 118.06800 123.58200 1.000 17.60161  ? 204 LEU B N    1 
ATOM   4015 C CA   . LEU B 1 204 ? 113.14400 117.28200 124.73200 1.000 5.70117   ? 204 LEU B CA   1 
ATOM   4016 C C    . LEU B 1 204 ? 114.16300 117.33500 125.86500 1.000 10.59094  ? 204 LEU B C    1 
ATOM   4017 O O    . LEU B 1 204 ? 113.79800 117.53500 127.02800 1.000 10.77202  ? 204 LEU B O    1 
ATOM   4018 C CB   . LEU B 1 204 ? 112.88400 115.83500 124.31200 1.000 17.92715  ? 204 LEU B CB   1 
ATOM   4019 C CG   . LEU B 1 204 ? 111.73200 115.56000 123.34200 1.000 20.93468  ? 204 LEU B CG   1 
ATOM   4020 C CD1  . LEU B 1 204 ? 111.79000 114.12800 122.84000 1.000 13.64625  ? 204 LEU B CD1  1 
ATOM   4021 C CD2  . LEU B 1 204 ? 110.39600 115.83500 124.00300 1.000 11.63850  ? 204 LEU B CD2  1 
ATOM   4022 N N    . THR B 1 205 ? 115.45100 117.16700 125.54700 1.000 12.65189  ? 205 THR B N    1 
ATOM   4023 C CA   . THR B 1 205 ? 116.46700 117.18800 126.59400 1.000 9.52545   ? 205 THR B CA   1 
ATOM   4024 C C    . THR B 1 205 ? 116.52600 118.54700 127.27700 1.000 10.17808  ? 205 THR B C    1 
ATOM   4025 O O    . THR B 1 205 ? 116.55900 118.63600 128.51500 1.000 9.63203   ? 205 THR B O    1 
ATOM   4026 C CB   . THR B 1 205 ? 117.83100 116.81900 126.01000 1.000 14.86850  ? 205 THR B CB   1 
ATOM   4027 O OG1  . THR B 1 205 ? 117.68000 115.72200 125.10200 1.000 23.11149  ? 205 THR B OG1  1 
ATOM   4028 C CG2  . THR B 1 205 ? 118.79700 116.43000 127.11300 1.000 6.31878   ? 205 THR B CG2  1 
ATOM   4029 N N    . TYR B 1 206 ? 116.50900 119.62600 126.48700 1.000 13.90643  ? 206 TYR B N    1 
ATOM   4030 C CA   . TYR B 1 206 ? 116.58700 120.95100 127.08600 1.000 7.55921   ? 206 TYR B CA   1 
ATOM   4031 C C    . TYR B 1 206 ? 115.41600 121.18500 128.02800 1.000 17.15532  ? 206 TYR B C    1 
ATOM   4032 O O    . TYR B 1 206 ? 115.60200 121.63400 129.16400 1.000 17.69044  ? 206 TYR B O    1 
ATOM   4033 C CB   . TYR B 1 206 ? 116.63100 122.03200 126.00900 1.000 8.94577   ? 206 TYR B CB   1 
ATOM   4034 C CG   . TYR B 1 206 ? 116.84600 123.41500 126.58200 1.000 18.96317  ? 206 TYR B CG   1 
ATOM   4035 C CD1  . TYR B 1 206 ? 118.12300 123.87600 126.86500 1.000 14.55422  ? 206 TYR B CD1  1 
ATOM   4036 C CD2  . TYR B 1 206 ? 115.77200 124.25200 126.86100 1.000 20.72896  ? 206 TYR B CD2  1 
ATOM   4037 C CE1  . TYR B 1 206 ? 118.32800 125.13100 127.39600 1.000 17.70081  ? 206 TYR B CE1  1 
ATOM   4038 C CE2  . TYR B 1 206 ? 115.96700 125.51000 127.39400 1.000 15.18637  ? 206 TYR B CE2  1 
ATOM   4039 C CZ   . TYR B 1 206 ? 117.24800 125.94400 127.66000 1.000 24.34403  ? 206 TYR B CZ   1 
ATOM   4040 O OH   . TYR B 1 206 ? 117.45700 127.19600 128.18800 1.000 29.85756  ? 206 TYR B OH   1 
ATOM   4041 N N    . CYS B 1 207 ? 114.19400 120.89500 127.57400 1.000 25.52182  ? 207 CYS B N    1 
ATOM   4042 C CA   . CYS B 1 207 ? 113.03600 121.16000 128.42100 1.000 10.77488  ? 207 CYS B CA   1 
ATOM   4043 C C    . CYS B 1 207 ? 113.05900 120.29500 129.67700 1.000 20.08921  ? 207 CYS B C    1 
ATOM   4044 O O    . CYS B 1 207 ? 112.78000 120.77800 130.78200 1.000 29.44317  ? 207 CYS B O    1 
ATOM   4045 C CB   . CYS B 1 207 ? 111.74500 120.94200 127.63400 1.000 17.59808  ? 207 CYS B CB   1 
ATOM   4046 S SG   . CYS B 1 207 ? 111.41200 122.19900 126.37800 1.000 42.14053  ? 207 CYS B SG   1 
ATOM   4047 N N    . TYR B 1 208 ? 113.34800 118.99800 129.52100 1.000 21.89820  ? 208 TYR B N    1 
ATOM   4048 C CA   . TYR B 1 208 ? 113.31600 118.08700 130.66000 1.000 14.23021  ? 208 TYR B CA   1 
ATOM   4049 C C    . TYR B 1 208 ? 114.32600 118.47600 131.73300 1.000 21.36413  ? 208 TYR B C    1 
ATOM   4050 O O    . TYR B 1 208 ? 114.02100 118.41400 132.93100 1.000 15.83587  ? 208 TYR B O    1 
ATOM   4051 C CB   . TYR B 1 208 ? 113.57200 116.65600 130.18800 1.000 10.17594  ? 208 TYR B CB   1 
ATOM   4052 C CG   . TYR B 1 208 ? 113.48100 115.61900 131.28100 1.000 21.51164  ? 208 TYR B CG   1 
ATOM   4053 C CD1  . TYR B 1 208 ? 114.58500 115.30400 132.06500 1.000 27.19784  ? 208 TYR B CD1  1 
ATOM   4054 C CD2  . TYR B 1 208 ? 112.29400 114.94900 131.52700 1.000 25.94552  ? 208 TYR B CD2  1 
ATOM   4055 C CE1  . TYR B 1 208 ? 114.50300 114.35800 133.06700 1.000 20.47281  ? 208 TYR B CE1  1 
ATOM   4056 C CE2  . TYR B 1 208 ? 112.20300 114.00200 132.52400 1.000 21.45283  ? 208 TYR B CE2  1 
ATOM   4057 C CZ   . TYR B 1 208 ? 113.30700 113.71000 133.29000 1.000 26.11127  ? 208 TYR B CZ   1 
ATOM   4058 O OH   . TYR B 1 208 ? 113.21000 112.76200 134.28000 1.000 36.30693  ? 208 TYR B OH   1 
ATOM   4059 N N    . ILE B 1 209 ? 115.51600 118.93300 131.33100 1.000 27.14304  ? 209 ILE B N    1 
ATOM   4060 C CA   . ILE B 1 209 ? 116.52300 119.24200 132.34400 1.000 17.80153  ? 209 ILE B CA   1 
ATOM   4061 C C    . ILE B 1 209 ? 116.19600 120.53400 133.07900 1.000 24.38716  ? 209 ILE B C    1 
ATOM   4062 O O    . ILE B 1 209 ? 116.52000 120.67700 134.26500 1.000 25.33555  ? 209 ILE B O    1 
ATOM   4063 C CB   . ILE B 1 209 ? 117.92800 119.30100 131.71800 1.000 21.70714  ? 209 ILE B CB   1 
ATOM   4064 C CG1  . ILE B 1 209 ? 118.45200 117.89400 131.43400 1.000 14.68292  ? 209 ILE B CG1  1 
ATOM   4065 C CG2  . ILE B 1 209 ? 118.88900 120.03800 132.63500 1.000 25.77715  ? 209 ILE B CG2  1 
ATOM   4066 C CD1  . ILE B 1 209 ? 119.71000 117.87800 130.60000 1.000 13.67304  ? 209 ILE B CD1  1 
ATOM   4067 N N    . LEU B 1 210 ? 115.55700 121.49100 132.40800 1.000 30.60015  ? 210 LEU B N    1 
ATOM   4068 C CA   . LEU B 1 210 ? 115.20500 122.74200 133.06900 1.000 21.83748  ? 210 LEU B CA   1 
ATOM   4069 C C    . LEU B 1 210 ? 113.97700 122.59300 133.95900 1.000 32.22736  ? 210 LEU B C    1 
ATOM   4070 O O    . LEU B 1 210 ? 113.91100 123.20300 135.03200 1.000 34.27380  ? 210 LEU B O    1 
ATOM   4071 C CB   . LEU B 1 210 ? 114.97800 123.83800 132.02800 1.000 27.97445  ? 210 LEU B CB   1 
ATOM   4072 C CG   . LEU B 1 210 ? 115.59800 125.20000 132.34100 1.000 28.23629  ? 210 LEU B CG   1 
ATOM   4073 C CD1  . LEU B 1 210 ? 117.10600 125.14500 132.19200 1.000 30.82182  ? 210 LEU B CD1  1 
ATOM   4074 C CD2  . LEU B 1 210 ? 115.01000 126.27200 131.44100 1.000 29.00739  ? 210 LEU B CD2  1 
ATOM   4075 N N    . ILE B 1 211 ? 112.99800 121.78400 133.54200 1.000 34.94958  ? 211 ILE B N    1 
ATOM   4076 C CA   . ILE B 1 211 ? 111.77000 121.61900 134.31900 1.000 28.76554  ? 211 ILE B CA   1 
ATOM   4077 C C    . ILE B 1 211 ? 111.86300 120.51900 135.37100 1.000 35.69502  ? 211 ILE B C    1 
ATOM   4078 O O    . ILE B 1 211 ? 110.98900 120.44100 136.24800 1.000 37.11216  ? 211 ILE B O    1 
ATOM   4079 C CB   . ILE B 1 211 ? 110.58000 121.36800 133.37000 1.000 27.73329  ? 211 ILE B CB   1 
ATOM   4080 C CG1  . ILE B 1 211 ? 110.13700 122.68300 132.72700 1.000 29.69243  ? 211 ILE B CG1  1 
ATOM   4081 C CG2  . ILE B 1 211 ? 109.41200 120.73400 134.10300 1.000 28.57364  ? 211 ILE B CG2  1 
ATOM   4082 C CD1  . ILE B 1 211 ? 109.78800 122.56300 131.26600 1.000 34.03018  ? 211 ILE B CD1  1 
ATOM   4083 N N    . SER B 1 212 ? 112.90800 119.69300 135.34300 1.000 43.93558  ? 212 SER B N    1 
ATOM   4084 C CA   . SER B 1 212 ? 113.06000 118.60700 136.30200 1.000 36.87688  ? 212 SER B CA   1 
ATOM   4085 C C    . SER B 1 212 ? 114.07500 118.90600 137.39600 1.000 44.89023  ? 212 SER B C    1 
ATOM   4086 O O    . SER B 1 212 ? 114.20700 118.10800 138.32900 1.000 50.41735  ? 212 SER B O    1 
ATOM   4087 C CB   . SER B 1 212 ? 113.45900 117.31300 135.58300 1.000 37.93423  ? 212 SER B CB   1 
ATOM   4088 O OG   . SER B 1 212 ? 112.35200 116.74300 134.91000 1.000 41.88819  ? 212 SER B OG   1 
ATOM   4089 N N    . GLY B 1 213 ? 114.78400 120.02600 137.31100 1.000 53.56518  ? 213 GLY B N    1 
ATOM   4090 C CA   . GLY B 1 213 ? 115.77400 120.37600 138.30900 1.000 54.42362  ? 213 GLY B CA   1 
ATOM   4091 C C    . GLY B 1 213 ? 115.43000 121.61800 139.10400 1.000 59.16198  ? 213 GLY B C    1 
ATOM   4092 O O    . GLY B 1 213 ? 116.10000 121.92900 140.09200 1.000 64.18647  ? 213 GLY B O    1 
ATOM   4093 N N    . PHE B 1 214 ? 114.38800 122.34000 138.68400 1.000 65.24111  ? 214 PHE B N    1 
ATOM   4094 C CA   . PHE B 1 214 ? 114.00000 123.55500 139.39500 1.000 62.67565  ? 214 PHE B CA   1 
ATOM   4095 C C    . PHE B 1 214 ? 113.72600 123.26800 140.86500 1.000 64.07852  ? 214 PHE B C    1 
ATOM   4096 O O    . PHE B 1 214 ? 114.12500 124.04500 141.74100 1.000 64.13273  ? 214 PHE B O    1 
ATOM   4097 C CB   . PHE B 1 214 ? 112.77100 124.17600 138.73300 1.000 63.67369  ? 214 PHE B CB   1 
ATOM   4098 C CG   . PHE B 1 214 ? 112.44600 125.55500 139.22800 1.000 64.33451  ? 214 PHE B CG   1 
ATOM   4099 C CD1  . PHE B 1 214 ? 113.28400 126.62000 138.95100 1.000 65.92907  ? 214 PHE B CD1  1 
ATOM   4100 C CD2  . PHE B 1 214 ? 111.29800 125.78500 139.96800 1.000 65.15025  ? 214 PHE B CD2  1 
ATOM   4101 C CE1  . PHE B 1 214 ? 112.98500 127.89000 139.40500 1.000 65.98963  ? 214 PHE B CE1  1 
ATOM   4102 C CE2  . PHE B 1 214 ? 110.99400 127.05200 140.42400 1.000 65.77309  ? 214 PHE B CE2  1 
ATOM   4103 C CZ   . PHE B 1 214 ? 111.83800 128.10600 140.14200 1.000 66.24867  ? 214 PHE B CZ   1 
ATOM   4104 N N    . ARG B 1 215 ? 113.04800 122.16200 141.15700 1.000 70.50707  ? 215 ARG B N    1 
ATOM   4105 C CA   . ARG B 1 215 ? 112.81200 121.74700 142.53300 1.000 72.39125  ? 215 ARG B CA   1 
ATOM   4106 C C    . ARG B 1 215 ? 114.01000 120.94300 143.02500 1.000 74.44568  ? 215 ARG B C    1 
ATOM   4107 O O    . ARG B 1 215 ? 114.45600 120.00800 142.35200 1.000 73.29504  ? 215 ARG B O    1 
ATOM   4108 C CB   . ARG B 1 215 ? 111.52700 120.92400 142.64100 1.000 71.81989  ? 215 ARG B CB   1 
ATOM   4109 C CG   . ARG B 1 215 ? 111.64100 119.49900 142.12400 1.000 72.66359  ? 215 ARG B CG   1 
ATOM   4110 C CD   . ARG B 1 215 ? 111.43800 119.43300 140.61800 1.000 70.92944  ? 215 ARG B CD   1 
ATOM   4111 N NE   . ARG B 1 215 ? 110.99500 118.11300 140.18600 1.000 71.52361  ? 215 ARG B NE   1 
ATOM   4112 C CZ   . ARG B 1 215 ? 111.72400 117.00900 140.28400 1.000 72.17154  ? 215 ARG B CZ   1 
ATOM   4113 N NH1  . ARG B 1 215 ? 112.94300 117.02900 140.79500 1.000 72.88880  ? 215 ARG B NH1  1 
ATOM   4114 N NH2  . ARG B 1 215 ? 111.21600 115.85600 139.85800 1.000 68.65158  ? 215 ARG B NH2  1 
ATOM   4115 N N    . THR B 1 216 ? 114.53000 121.31300 144.19300 1.000 77.15006  ? 216 THR B N    1 
ATOM   4116 C CA   . THR B 1 216 ? 115.67600 120.67000 144.83400 1.000 78.25994  ? 216 THR B CA   1 
ATOM   4117 C C    . THR B 1 216 ? 116.99500 121.09000 144.19900 1.000 78.25584  ? 216 THR B C    1 
ATOM   4118 O O    . THR B 1 216 ? 118.03900 120.51400 144.54100 1.000 78.65466  ? 216 THR B O    1 
ATOM   4119 C CB   . THR B 1 216 ? 115.58000 119.14100 144.81300 1.000 79.05854  ? 216 THR B CB   1 
ATOM   4120 O OG1  . THR B 1 216 ? 114.41100 118.72000 145.52600 1.000 79.95342  ? 216 THR B OG1  1 
ATOM   4121 C CG2  . THR B 1 216 ? 116.81200 118.52100 145.45800 1.000 77.59438  ? 216 THR B CG2  1 
ATOM   4122 N N    . GLY B 1 217 ? 116.98600 122.08000 143.30700 1.000 73.14094  ? 217 GLY B N    1 
ATOM   4123 C CA   . GLY B 1 217 ? 118.18200 122.56700 142.64000 1.000 73.03966  ? 217 GLY B CA   1 
ATOM   4124 C C    . GLY B 1 217 ? 119.27100 121.54100 142.40000 1.000 75.21019  ? 217 GLY B C    1 
ATOM   4125 O O    . GLY B 1 217 ? 120.42400 121.74900 142.78600 1.000 75.88429  ? 217 GLY B O    1 
ATOM   4126 N N    . GLN B 1 218 ? 118.91500 120.42700 141.76300 1.000 72.70123  ? 218 GLN B N    1 
ATOM   4127 C CA   . GLN B 1 218 ? 119.85800 119.36600 141.41800 1.000 72.87489  ? 218 GLN B CA   1 
ATOM   4128 C C    . GLN B 1 218 ? 119.90700 119.23500 139.90100 1.000 71.89368  ? 218 GLN B C    1 
ATOM   4129 O O    . GLN B 1 218 ? 118.96600 118.72200 139.28700 1.000 74.16471  ? 218 GLN B O    1 
ATOM   4130 C CB   . GLN B 1 218 ? 119.46200 118.04200 142.07000 1.000 72.05804  ? 218 GLN B CB   1 
ATOM   4131 C CG   . GLN B 1 218 ? 119.57500 118.03600 143.58600 1.000 72.99505  ? 218 GLN B CG   1 
ATOM   4132 C CD   . GLN B 1 218 ? 119.10700 116.73200 144.20000 1.000 75.78729  ? 218 GLN B CD   1 
ATOM   4133 O OE1  . GLN B 1 218 ? 118.29800 116.01100 143.61500 1.000 78.01726  ? 218 GLN B OE1  1 
ATOM   4134 N NE2  . GLN B 1 218 ? 119.61600 116.42000 145.38500 1.000 73.25931  ? 218 GLN B NE2  1 
ATOM   4135 N N    . PHE B 1 219 ? 121.00500 119.69300 139.30100 1.000 61.62196  ? 219 PHE B N    1 
ATOM   4136 C CA   . PHE B 1 219 ? 121.15700 119.70900 137.85400 1.000 62.08357  ? 219 PHE B CA   1 
ATOM   4137 C C    . PHE B 1 219 ? 122.29000 118.82800 137.35100 1.000 62.08780  ? 219 PHE B C    1 
ATOM   4138 O O    . PHE B 1 219 ? 122.34300 118.54800 136.14900 1.000 65.95714  ? 219 PHE B O    1 
ATOM   4139 C CB   . PHE B 1 219 ? 121.37200 121.14400 137.34600 1.000 60.23646  ? 219 PHE B CB   1 
ATOM   4140 C CG   . PHE B 1 219 ? 120.13000 121.99100 137.37700 1.000 59.55570  ? 219 PHE B CG   1 
ATOM   4141 C CD1  . PHE B 1 219 ? 119.57700 122.38900 138.58200 1.000 62.60663  ? 219 PHE B CD1  1 
ATOM   4142 C CD2  . PHE B 1 219 ? 119.50700 122.37400 136.20300 1.000 61.31797  ? 219 PHE B CD2  1 
ATOM   4143 C CE1  . PHE B 1 219 ? 118.43300 123.16500 138.61300 1.000 61.35359  ? 219 PHE B CE1  1 
ATOM   4144 C CE2  . PHE B 1 219 ? 118.36100 123.14600 136.22900 1.000 60.68937  ? 219 PHE B CE2  1 
ATOM   4145 C CZ   . PHE B 1 219 ? 117.82500 123.54200 137.43600 1.000 59.61293  ? 219 PHE B CZ   1 
ATOM   4146 N N    . ILE B 1 220 ? 123.19300 118.38300 138.22800 1.000 55.10371  ? 220 ILE B N    1 
ATOM   4147 C CA   . ILE B 1 220 ? 124.30900 117.53000 137.82900 1.000 57.61469  ? 220 ILE B CA   1 
ATOM   4148 C C    . ILE B 1 220 ? 124.08200 116.08100 138.23800 1.000 60.22844  ? 220 ILE B C    1 
ATOM   4149 O O    . ILE B 1 220 ? 124.86500 115.20200 137.84400 1.000 61.82623  ? 220 ILE B O    1 
ATOM   4150 C CB   . ILE B 1 220 ? 125.64000 118.05800 138.41200 1.000 58.09722  ? 220 ILE B CB   1 
ATOM   4151 C CG1  . ILE B 1 220 ? 126.06100 119.34200 137.69800 1.000 56.72167  ? 220 ILE B CG1  1 
ATOM   4152 C CG2  . ILE B 1 220 ? 126.74900 117.02700 138.28900 1.000 58.77084  ? 220 ILE B CG2  1 
ATOM   4153 C CD1  . ILE B 1 220 ? 126.98400 119.10800 136.52400 1.000 55.64889  ? 220 ILE B CD1  1 
ATOM   4154 N N    . GLU B 1 221 ? 123.01000 115.79900 138.97900 1.000 59.58990  ? 221 GLU B N    1 
ATOM   4155 C CA   . GLU B 1 221 ? 122.63300 114.44500 139.35400 1.000 60.16556  ? 221 GLU B CA   1 
ATOM   4156 C C    . GLU B 1 221 ? 121.44400 113.92200 138.56600 1.000 59.93539  ? 221 GLU B C    1 
ATOM   4157 O O    . GLU B 1 221 ? 121.22200 112.70800 138.54600 1.000 58.75134  ? 221 GLU B O    1 
ATOM   4158 C CB   . GLU B 1 221 ? 122.31300 114.37100 140.85400 1.000 59.26580  ? 221 GLU B CB   1 
ATOM   4159 C CG   . GLU B 1 221 ? 123.50400 113.99500 141.71600 1.000 61.33988  ? 221 GLU B CG   1 
ATOM   4160 C CD   . GLU B 1 221 ? 124.43500 113.01900 141.02300 1.000 64.86151  ? 221 GLU B CD   1 
ATOM   4161 O OE1  . GLU B 1 221 ? 123.99500 111.88900 140.72100 1.000 63.30133  ? 221 GLU B OE1  1 
ATOM   4162 O OE2  . GLU B 1 221 ? 125.60600 113.38100 140.77900 1.000 61.97836  ? 221 GLU B OE2  1 
ATOM   4163 N N    . VAL B 1 222 ? 120.67700 114.80800 137.91800 1.000 62.38743  ? 222 VAL B N    1 
ATOM   4164 C CA   . VAL B 1 222 ? 119.54700 114.39100 137.09700 1.000 61.92586  ? 222 VAL B CA   1 
ATOM   4165 C C    . VAL B 1 222 ? 119.97300 114.02700 135.68100 1.000 60.78320  ? 222 VAL B C    1 
ATOM   4166 O O    . VAL B 1 222 ? 119.13600 113.58900 134.88100 1.000 62.40691  ? 222 VAL B O    1 
ATOM   4167 C CB   . VAL B 1 222 ? 118.48000 115.50800 137.07300 1.000 61.00966  ? 222 VAL B CB   1 
ATOM   4168 C CG1  . VAL B 1 222 ? 117.31800 115.14400 136.16300 1.000 59.40239  ? 222 VAL B CG1  1 
ATOM   4169 C CG2  . VAL B 1 222 ? 117.98900 115.80900 138.48100 1.000 60.16794  ? 222 VAL B CG2  1 
ATOM   4170 N N    . ALA B 1 223 ? 121.25300 114.17700 135.35200 1.000 52.87793  ? 223 ALA B N    1 
ATOM   4171 C CA   . ALA B 1 223 ? 121.77200 113.87400 134.02400 1.000 55.51189  ? 223 ALA B CA   1 
ATOM   4172 C C    . ALA B 1 223 ? 122.83300 112.78600 134.03800 1.000 57.50756  ? 223 ALA B C    1 
ATOM   4173 O O    . ALA B 1 223 ? 122.82000 111.89900 133.17400 1.000 54.62158  ? 223 ALA B O    1 
ATOM   4174 C CB   . ALA B 1 223 ? 122.35100 115.14300 133.38300 1.000 49.35540  ? 223 ALA B CB   1 
ATOM   4175 N N    . ILE B 1 224 ? 123.69100 112.77000 135.06000 1.000 53.97017  ? 224 ILE B N    1 
ATOM   4176 C CA   . ILE B 1 224 ? 124.77400 111.79600 135.10200 1.000 49.74480  ? 224 ILE B CA   1 
ATOM   4177 C C    . ILE B 1 224 ? 124.21200 110.40400 135.33100 1.000 50.69820  ? 224 ILE B C    1 
ATOM   4178 O O    . ILE B 1 224 ? 124.69600 109.42100 134.75900 1.000 51.79767  ? 224 ILE B O    1 
ATOM   4179 C CB   . ILE B 1 224 ? 125.79700 112.18300 136.18300 1.000 52.31407  ? 224 ILE B CB   1 
ATOM   4180 C CG1  . ILE B 1 224 ? 126.55900 113.44200 135.76600 1.000 51.49890  ? 224 ILE B CG1  1 
ATOM   4181 C CG2  . ILE B 1 224 ? 126.76100 111.03800 136.43800 1.000 50.67219  ? 224 ILE B CG2  1 
ATOM   4182 C CD1  . ILE B 1 224 ? 127.85000 113.16300 135.03900 1.000 52.01161  ? 224 ILE B CD1  1 
ATOM   4183 N N    . SER B 1 225 ? 123.18200 110.29500 136.16800 1.000 54.34055  ? 225 SER B N    1 
ATOM   4184 C CA   . SER B 1 225 ? 122.55700 109.00000 136.40100 1.000 54.34258  ? 225 SER B CA   1 
ATOM   4185 C C    . SER B 1 225 ? 121.76900 108.56800 135.17100 1.000 50.95842  ? 225 SER B C    1 
ATOM   4186 O O    . SER B 1 225 ? 121.98700 107.48000 134.62700 1.000 55.10859  ? 225 SER B O    1 
ATOM   4187 C CB   . SER B 1 225 ? 121.65500 109.06500 137.63400 1.000 52.94668  ? 225 SER B CB   1 
ATOM   4188 O OG   . SER B 1 225 ? 120.59600 109.98500 137.43900 1.000 54.13457  ? 225 SER B OG   1 
ATOM   4189 N N    . ARG B 1 226 ? 120.84100 109.41300 134.71900 1.000 43.77632  ? 226 ARG B N    1 
ATOM   4190 C CA   . ARG B 1 226 ? 119.99700 109.08700 133.57700 1.000 45.81534  ? 226 ARG B CA   1 
ATOM   4191 C C    . ARG B 1 226 ? 120.76600 108.96600 132.26400 1.000 49.26436  ? 226 ARG B C    1 
ATOM   4192 O O    . ARG B 1 226 ? 120.13800 108.68200 131.24000 1.000 54.44372  ? 226 ARG B O    1 
ATOM   4193 C CB   . ARG B 1 226 ? 118.89000 110.13400 133.42800 1.000 42.94323  ? 226 ARG B CB   1 
ATOM   4194 C CG   . ARG B 1 226 ? 118.31400 110.61400 134.74700 1.000 44.51363  ? 226 ARG B CG   1 
ATOM   4195 C CD   . ARG B 1 226 ? 116.89500 110.10800 134.94700 1.000 46.87379  ? 226 ARG B CD   1 
ATOM   4196 N NE   . ARG B 1 226 ? 116.02800 111.11100 135.55500 1.000 49.89482  ? 226 ARG B NE   1 
ATOM   4197 C CZ   . ARG B 1 226 ? 116.26600 111.70800 136.71500 1.000 51.07905  ? 226 ARG B CZ   1 
ATOM   4198 N NH1  . ARG B 1 226 ? 117.33700 111.42000 137.43500 1.000 48.42356  ? 226 ARG B NH1  1 
ATOM   4199 N NH2  . ARG B 1 226 ? 115.40500 112.61600 137.16500 1.000 48.94592  ? 226 ARG B NH2  1 
ATOM   4200 N N    . PHE B 1 227 ? 122.08400 109.16900 132.24700 1.000 42.25810  ? 227 PHE B N    1 
ATOM   4201 C CA   . PHE B 1 227 ? 122.84700 108.90200 131.03200 1.000 38.07108  ? 227 PHE B CA   1 
ATOM   4202 C C    . PHE B 1 227 ? 123.50800 107.52800 131.01200 1.000 41.04801  ? 227 PHE B C    1 
ATOM   4203 O O    . PHE B 1 227 ? 123.62900 106.92500 129.93800 1.000 42.49402  ? 227 PHE B O    1 
ATOM   4204 C CB   . PHE B 1 227 ? 123.92200 109.97400 130.82700 1.000 37.61929  ? 227 PHE B CB   1 
ATOM   4205 C CG   . PHE B 1 227 ? 124.49300 109.99400 129.44000 1.000 45.00582  ? 227 PHE B CG   1 
ATOM   4206 C CD1  . PHE B 1 227 ? 123.77300 110.53600 128.38900 1.000 47.04427  ? 227 PHE B CD1  1 
ATOM   4207 C CD2  . PHE B 1 227 ? 125.74300 109.45700 129.18300 1.000 44.60621  ? 227 PHE B CD2  1 
ATOM   4208 C CE1  . PHE B 1 227 ? 124.29300 110.54900 127.10800 1.000 46.97792  ? 227 PHE B CE1  1 
ATOM   4209 C CE2  . PHE B 1 227 ? 126.26900 109.46800 127.90500 1.000 41.85747  ? 227 PHE B CE2  1 
ATOM   4210 C CZ   . PHE B 1 227 ? 125.54300 110.01400 126.86700 1.000 45.98439  ? 227 PHE B CZ   1 
ATOM   4211 N N    . LEU B 1 228 ? 123.93000 107.01000 132.16800 1.000 33.92306  ? 228 LEU B N    1 
ATOM   4212 C CA   . LEU B 1 228 ? 124.52800 105.67800 132.20400 1.000 28.37709  ? 228 LEU B CA   1 
ATOM   4213 C C    . LEU B 1 228 ? 123.52500 104.60200 131.80200 1.000 34.59389  ? 228 LEU B C    1 
ATOM   4214 O O    . LEU B 1 228 ? 123.88400 103.62600 131.13300 1.000 40.54450  ? 228 LEU B O    1 
ATOM   4215 C CB   . LEU B 1 228 ? 125.08900 105.39600 133.59700 1.000 36.08680  ? 228 LEU B CB   1 
ATOM   4216 C CG   . LEU B 1 228 ? 126.08900 106.41400 134.14800 1.000 42.45604  ? 228 LEU B CG   1 
ATOM   4217 C CD1  . LEU B 1 228 ? 126.18900 106.31100 135.66200 1.000 39.00671  ? 228 LEU B CD1  1 
ATOM   4218 C CD2  . LEU B 1 228 ? 127.45600 106.22700 133.50700 1.000 38.64986  ? 228 LEU B CD2  1 
ATOM   4219 N N    . LEU B 1 229 ? 122.26200 104.76000 132.19900 1.000 31.33185  ? 229 LEU B N    1 
ATOM   4220 C CA   . LEU B 1 229 ? 121.24800 103.77800 131.82600 1.000 31.78037  ? 229 LEU B CA   1 
ATOM   4221 C C    . LEU B 1 229 ? 120.98500 103.80100 130.32300 1.000 28.02679  ? 229 LEU B C    1 
ATOM   4222 O O    . LEU B 1 229 ? 120.78600 102.74800 129.70000 1.000 42.33875  ? 229 LEU B O    1 
ATOM   4223 C CB   . LEU B 1 229 ? 119.96900 104.04300 132.61600 1.000 32.59301  ? 229 LEU B CB   1 
ATOM   4224 C CG   . LEU B 1 229 ? 120.03200 103.53900 134.06100 1.000 31.63413  ? 229 LEU B CG   1 
ATOM   4225 C CD1  . LEU B 1 229 ? 119.00400 104.24000 134.92100 1.000 27.39037  ? 229 LEU B CD1  1 
ATOM   4226 C CD2  . LEU B 1 229 ? 119.84800 102.03200 134.12800 1.000 34.61512  ? 229 LEU B CD2  1 
ATOM   4227 N N    . ILE B 1 230 ? 121.04000 104.98600 129.71600 1.000 15.92168  ? 230 ILE B N    1 
ATOM   4228 C CA   . ILE B 1 230 ? 120.87700 105.08700 128.27100 1.000 20.11358  ? 230 ILE B CA   1 
ATOM   4229 C C    . ILE B 1 230 ? 122.06600 104.45200 127.56800 1.000 25.01137  ? 230 ILE B C    1 
ATOM   4230 O O    . ILE B 1 230 ? 121.91600 103.76400 126.54800 1.000 30.98658  ? 230 ILE B O    1 
ATOM   4231 C CB   . ILE B 1 230 ? 120.70300 106.56200 127.86600 1.000 27.37490  ? 230 ILE B CB   1 
ATOM   4232 C CG1  . ILE B 1 230 ? 119.42800 107.14300 128.47700 1.000 23.14567  ? 230 ILE B CG1  1 
ATOM   4233 C CG2  . ILE B 1 230 ? 120.69300 106.70800 126.35300 1.000 22.09181  ? 230 ILE B CG2  1 
ATOM   4234 C CD1  . ILE B 1 230 ? 119.21300 108.60200 128.15500 1.000 18.38016  ? 230 ILE B CD1  1 
ATOM   4235 N N    . ALA B 1 231 ? 123.26500 104.63900 128.12400 1.000 22.04564  ? 231 ALA B N    1 
ATOM   4236 C CA   . ALA B 1 231 ? 124.44800 104.01000 127.55000 1.000 25.21390  ? 231 ALA B CA   1 
ATOM   4237 C C    . ALA B 1 231 ? 124.36500 102.49200 127.63700 1.000 26.28785  ? 231 ALA B C    1 
ATOM   4238 O O    . ALA B 1 231 ? 124.75900 101.78800 126.70100 1.000 28.76039  ? 231 ALA B O    1 
ATOM   4239 C CB   . ALA B 1 231 ? 125.70500 104.52100 128.25100 1.000 23.47213  ? 231 ALA B CB   1 
ATOM   4240 N N    . LEU B 1 232 ? 123.82400 101.96700 128.73800 1.000 20.49307  ? 232 LEU B N    1 
ATOM   4241 C CA   . LEU B 1 232 ? 123.71400 100.51700 128.87500 1.000 18.44520  ? 232 LEU B CA   1 
ATOM   4242 C C    . LEU B 1 232 ? 122.67000 99.94200  127.92300 1.000 28.30203  ? 232 LEU B C    1 
ATOM   4243 O O    . LEU B 1 232 ? 122.88500 98.87700  127.32200 1.000 35.26655  ? 232 LEU B O    1 
ATOM   4244 C CB   . LEU B 1 232 ? 123.37500 100.15700 130.32000 1.000 21.09518  ? 232 LEU B CB   1 
ATOM   4245 C CG   . LEU B 1 232 ? 123.13700 98.68100  130.63800 1.000 28.86984  ? 232 LEU B CG   1 
ATOM   4246 C CD1  . LEU B 1 232 ? 124.42600 98.01100  131.08500 1.000 25.93109  ? 232 LEU B CD1  1 
ATOM   4247 C CD2  . LEU B 1 232 ? 122.05700 98.53000  131.69600 1.000 27.48357  ? 232 LEU B CD2  1 
ATOM   4248 N N    . GLY B 1 233 ? 121.56500 100.66100 127.71700 1.000 21.73111  ? 233 GLY B N    1 
ATOM   4249 C CA   . GLY B 1 233 ? 120.57600 100.18900 126.76300 1.000 9.71031   ? 233 GLY B CA   1 
ATOM   4250 C C    . GLY B 1 233 ? 121.09800 100.21400 125.33900 1.000 18.85031  ? 233 GLY B C    1 
ATOM   4251 O O    . GLY B 1 233 ? 120.86900 99.27700  124.56400 1.000 26.69191  ? 233 GLY B O    1 
ATOM   4252 N N    . ALA B 1 234 ? 121.88800 101.23700 125.00100 1.000 20.38029  ? 234 ALA B N    1 
ATOM   4253 C CA   . ALA B 1 234 ? 122.43900 101.30100 123.65400 1.000 16.95428  ? 234 ALA B CA   1 
ATOM   4254 C C    . ALA B 1 234 ? 123.53400 100.26400 123.45300 1.000 21.23452  ? 234 ALA B C    1 
ATOM   4255 O O    . ALA B 1 234 ? 123.66300 99.70500  122.35800 1.000 23.70645  ? 234 ALA B O    1 
ATOM   4256 C CB   . ALA B 1 234 ? 122.97100 102.70400 123.36900 1.000 12.32548  ? 234 ALA B CB   1 
ATOM   4257 N N    . GLY B 1 235 ? 124.30400 99.96300  124.50100 1.000 14.01628  ? 235 GLY B N    1 
ATOM   4258 C CA   . GLY B 1 235 ? 125.31300 98.92600  124.38500 1.000 13.11777  ? 235 GLY B CA   1 
ATOM   4259 C C    . GLY B 1 235 ? 124.70900 97.55200  124.17600 1.000 17.48991  ? 235 GLY B C    1 
ATOM   4260 O O    . GLY B 1 235 ? 125.18100 96.77700  123.33700 1.000 26.80437  ? 235 GLY B O    1 
ATOM   4261 N N    . VAL B 1 236 ? 123.64000 97.23700  124.91400 1.000 14.80578  ? 236 VAL B N    1 
ATOM   4262 C CA   . VAL B 1 236 ? 122.98700 95.94700  124.70900 1.000 17.60205  ? 236 VAL B CA   1 
ATOM   4263 C C    . VAL B 1 236 ? 122.36700 95.87600  123.31800 1.000 18.20071  ? 236 VAL B C    1 
ATOM   4264 O O    . VAL B 1 236 ? 122.46900 94.84800  122.62800 1.000 20.20530  ? 236 VAL B O    1 
ATOM   4265 C CB   . VAL B 1 236 ? 121.94100 95.69200  125.81000 1.000 20.06672  ? 236 VAL B CB   1 
ATOM   4266 C CG1  . VAL B 1 236 ? 121.21900 94.38100  125.56000 1.000 16.10490  ? 236 VAL B CG1  1 
ATOM   4267 C CG2  . VAL B 1 236 ? 122.60400 95.68300  127.17700 1.000 19.48819  ? 236 VAL B CG2  1 
ATOM   4268 N N    . SER B 1 237 ? 121.75800 96.97500  122.86000 1.000 14.13635  ? 237 SER B N    1 
ATOM   4269 C CA   . SER B 1 237 ? 121.17200 96.97900  121.52400 1.000 8.46746   ? 237 SER B CA   1 
ATOM   4270 C C    . SER B 1 237 ? 122.23400 96.73300  120.45900 1.000 22.05143  ? 237 SER B C    1 
ATOM   4271 O O    . SER B 1 237 ? 122.04300 95.91400  119.55100 1.000 18.59833  ? 237 SER B O    1 
ATOM   4272 C CB   . SER B 1 237 ? 120.45300 98.30400  121.26800 1.000 10.73215  ? 237 SER B CB   1 
ATOM   4273 O OG   . SER B 1 237 ? 119.55700 98.61200  122.31800 1.000 25.54433  ? 237 SER B OG   1 
ATOM   4274 N N    . LEU B 1 238 ? 123.37700 97.41500  120.57100 1.000 23.82454  ? 238 LEU B N    1 
ATOM   4275 C CA   . LEU B 1 238 ? 124.41000 97.27900  119.55100 1.000 18.48994  ? 238 LEU B CA   1 
ATOM   4276 C C    . LEU B 1 238 ? 125.03800 95.89300  119.57300 1.000 23.64996  ? 238 LEU B C    1 
ATOM   4277 O O    . LEU B 1 238 ? 125.30500 95.31400  118.51400 1.000 29.61200  ? 238 LEU B O    1 
ATOM   4278 C CB   . LEU B 1 238 ? 125.48200 98.35000  119.74400 1.000 19.50607  ? 238 LEU B CB   1 
ATOM   4279 C CG   . LEU B 1 238 ? 126.36300 98.67300  118.53700 1.000 27.41987  ? 238 LEU B CG   1 
ATOM   4280 C CD1  . LEU B 1 238 ? 125.55200 99.30900  117.42100 1.000 27.42483  ? 238 LEU B CD1  1 
ATOM   4281 C CD2  . LEU B 1 238 ? 127.51200 99.57400  118.95000 1.000 23.71298  ? 238 LEU B CD2  1 
ATOM   4282 N N    . GLY B 1 239 ? 125.24100 95.31900  120.76000 1.000 15.53446  ? 239 GLY B N    1 
ATOM   4283 C CA   . GLY B 1 239 ? 125.81800 93.98700  120.81500 1.000 14.91626  ? 239 GLY B CA   1 
ATOM   4284 C C    . GLY B 1 239 ? 124.90500 92.94000  120.20800 1.000 20.68773  ? 239 GLY B C    1 
ATOM   4285 O O    . GLY B 1 239 ? 125.34400 92.10500  119.40500 1.000 21.68219  ? 239 GLY B O    1 
ATOM   4286 N N    . VAL B 1 240 ? 123.61000 93.00800  120.52800 1.000 24.06914  ? 240 VAL B N    1 
ATOM   4287 C CA   . VAL B 1 240 ? 122.68600 92.01500  119.99300 1.000 19.53083  ? 240 VAL B CA   1 
ATOM   4288 C C    . VAL B 1 240 ? 122.51900 92.19700  118.49000 1.000 16.89514  ? 240 VAL B C    1 
ATOM   4289 O O    . VAL B 1 240 ? 122.41700 91.21700  117.74300 1.000 12.37903  ? 240 VAL B O    1 
ATOM   4290 C CB   . VAL B 1 240 ? 121.33600 92.07900  120.72900 1.000 17.54497  ? 240 VAL B CB   1 
ATOM   4291 C CG1  . VAL B 1 240 ? 120.35500 91.08700  120.12600 1.000 10.75219  ? 240 VAL B CG1  1 
ATOM   4292 C CG2  . VAL B 1 240 ? 121.53300 91.79800  122.20500 1.000 13.45880  ? 240 VAL B CG2  1 
ATOM   4293 N N    . ASN B 1 241 ? 122.48900 93.44600  118.01500 1.000 12.67255  ? 241 ASN B N    1 
ATOM   4294 C CA   . ASN B 1 241 ? 122.33100 93.66500  116.58200 1.000 14.40089  ? 241 ASN B CA   1 
ATOM   4295 C C    . ASN B 1 241 ? 123.56000 93.21000  115.80600 1.000 23.29707  ? 241 ASN B C    1 
ATOM   4296 O O    . ASN B 1 241 ? 123.43400 92.65400  114.70900 1.000 19.93970  ? 241 ASN B O    1 
ATOM   4297 C CB   . ASN B 1 241 ? 122.04500 95.13900  116.29600 1.000 12.40197  ? 241 ASN B CB   1 
ATOM   4298 C CG   . ASN B 1 241 ? 121.19800 95.33600  115.05400 1.000 12.66566  ? 241 ASN B CG   1 
ATOM   4299 O OD1  . ASN B 1 241 ? 120.93300 94.39200  114.31600 1.000 24.74401  ? 241 ASN B OD1  1 
ATOM   4300 N ND2  . ASN B 1 241 ? 120.78300 96.57000  114.81000 1.000 17.08672  ? 241 ASN B ND2  1 
ATOM   4301 N N    . MET B 1 242 ? 124.75600 93.42500  116.35400 1.000 23.06769  ? 242 MET B N    1 
ATOM   4302 C CA   . MET B 1 242 ? 125.96900 93.16100  115.59500 1.000 14.77634  ? 242 MET B CA   1 
ATOM   4303 C C    . MET B 1 242 ? 126.47200 91.72700  115.68900 1.000 20.92324  ? 242 MET B C    1 
ATOM   4304 O O    . MET B 1 242 ? 127.22200 91.30300  114.80400 1.000 26.47510  ? 242 MET B O    1 
ATOM   4305 C CB   . MET B 1 242 ? 127.08300 94.11400  116.04100 1.000 28.40836  ? 242 MET B CB   1 
ATOM   4306 C CG   . MET B 1 242 ? 128.43300 93.82400  115.41000 1.000 27.62560  ? 242 MET B CG   1 
ATOM   4307 S SD   . MET B 1 242 ? 129.31800 95.31500  114.92000 1.000 48.88480  ? 242 MET B SD   1 
ATOM   4308 C CE   . MET B 1 242 ? 128.69200 96.49100  116.11400 1.000 28.59848  ? 242 MET B CE   1 
ATOM   4309 N N    . PHE B 1 243 ? 126.09200 90.95700  116.71100 1.000 22.36475  ? 243 PHE B N    1 
ATOM   4310 C CA   . PHE B 1 243 ? 126.67100 89.62400  116.85400 1.000 16.75033  ? 243 PHE B CA   1 
ATOM   4311 C C    . PHE B 1 243 ? 125.68400 88.48000  116.64700 1.000 15.74512  ? 243 PHE B C    1 
ATOM   4312 O O    . PHE B 1 243 ? 126.03400 87.32800  116.92100 1.000 24.69753  ? 243 PHE B O    1 
ATOM   4313 C CB   . PHE B 1 243 ? 127.35100 89.48700  118.21800 1.000 14.97530  ? 243 PHE B CB   1 
ATOM   4314 C CG   . PHE B 1 243 ? 128.43600 90.49500  118.45500 1.000 20.49518  ? 243 PHE B CG   1 
ATOM   4315 C CD1  . PHE B 1 243 ? 129.63500 90.40800  117.77000 1.000 22.08273  ? 243 PHE B CD1  1 
ATOM   4316 C CD2  . PHE B 1 243 ? 128.26000 91.53000  119.35400 1.000 24.07773  ? 243 PHE B CD2  1 
ATOM   4317 C CE1  . PHE B 1 243 ? 130.63800 91.33300  117.97900 1.000 22.69024  ? 243 PHE B CE1  1 
ATOM   4318 C CE2  . PHE B 1 243 ? 129.25900 92.45800  119.56700 1.000 21.90509  ? 243 PHE B CE2  1 
ATOM   4319 C CZ   . PHE B 1 243 ? 130.44900 92.35900  118.87800 1.000 23.35605  ? 243 PHE B CZ   1 
ATOM   4320 N N    . ILE B 1 244 ? 124.47200 88.74700  116.16400 1.000 19.03421  ? 244 ILE B N    1 
ATOM   4321 C CA   . ILE B 1 244 ? 123.48800 87.69800  115.88800 1.000 15.61963  ? 244 ILE B CA   1 
ATOM   4322 C C    . ILE B 1 244 ? 122.90400 87.95600  114.50100 1.000 15.88432  ? 244 ILE B C    1 
ATOM   4323 O O    . ILE B 1 244 ? 121.92900 88.69700  114.34900 1.000 27.42378  ? 244 ILE B O    1 
ATOM   4324 C CB   . ILE B 1 244 ? 122.38700 87.62500  116.95000 1.000 20.19764  ? 244 ILE B CB   1 
ATOM   4325 C CG1  . ILE B 1 244 ? 122.99600 87.66500  118.35200 1.000 18.44387  ? 244 ILE B CG1  1 
ATOM   4326 C CG2  . ILE B 1 244 ? 121.56100 86.36400  116.77300 1.000 14.51599  ? 244 ILE B CG2  1 
ATOM   4327 C CD1  . ILE B 1 244 ? 122.04700 87.23800  119.44300 1.000 9.23340   ? 244 ILE B CD1  1 
ATOM   4328 N N    . TYR B 1 245 ? 123.49700 87.33900  113.47800 1.000 14.07946  ? 245 TYR B N    1 
ATOM   4329 C CA   . TYR B 1 245 ? 123.02200 87.44600  112.10200 1.000 20.24691  ? 245 TYR B CA   1 
ATOM   4330 C C    . TYR B 1 245 ? 122.91300 88.89500  111.64300 1.000 21.06191  ? 245 TYR B C    1 
ATOM   4331 O O    . TYR B 1 245 ? 121.80500 89.38500  111.39300 1.000 23.96096  ? 245 TYR B O    1 
ATOM   4332 C CB   . TYR B 1 245 ? 121.67500 86.73800  111.94600 1.000 17.89837  ? 245 TYR B CB   1 
ATOM   4333 C CG   . TYR B 1 245 ? 121.77200 85.23600  112.06900 1.000 22.65860  ? 245 TYR B CG   1 
ATOM   4334 C CD1  . TYR B 1 245 ? 121.72000 84.61500  113.30800 1.000 26.08524  ? 245 TYR B CD1  1 
ATOM   4335 C CD2  . TYR B 1 245 ? 121.93200 84.43900  110.94500 1.000 27.09737  ? 245 TYR B CD2  1 
ATOM   4336 C CE1  . TYR B 1 245 ? 121.81600 83.24200  113.42400 1.000 24.31065  ? 245 TYR B CE1  1 
ATOM   4337 C CE2  . TYR B 1 245 ? 122.02900 83.06600  111.05000 1.000 30.21630  ? 245 TYR B CE2  1 
ATOM   4338 C CZ   . TYR B 1 245 ? 121.97000 82.47300  112.29200 1.000 32.16632  ? 245 TYR B CZ   1 
ATOM   4339 O OH   . TYR B 1 245 ? 122.06500 81.10500  112.40200 1.000 35.89434  ? 245 TYR B OH   1 
ATOM   4340 N N    . PRO B 1 246 ? 124.03200 89.60400  111.51200 1.000 18.01810  ? 246 PRO B N    1 
ATOM   4341 C CA   . PRO B 1 246 ? 123.97200 91.00900  111.09600 1.000 12.81862  ? 246 PRO B CA   1 
ATOM   4342 C C    . PRO B 1 246 ? 123.42700 91.16800  109.68400 1.000 13.43187  ? 246 PRO B C    1 
ATOM   4343 O O    . PRO B 1 246 ? 123.56100 90.28400  108.83600 1.000 19.31428  ? 246 PRO B O    1 
ATOM   4344 C CB   . PRO B 1 246 ? 125.43500 91.46500  111.17600 1.000 13.18931  ? 246 PRO B CB   1 
ATOM   4345 C CG   . PRO B 1 246 ? 126.12200 90.43600  112.02100 1.000 15.86735  ? 246 PRO B CG   1 
ATOM   4346 C CD   . PRO B 1 246 ? 125.41400 89.15800  111.73900 1.000 14.33689  ? 246 PRO B CD   1 
ATOM   4347 N N    . ILE B 1 247 ? 122.79200 92.31200  109.44400 1.000 13.76320  ? 247 ILE B N    1 
ATOM   4348 C CA   . ILE B 1 247 ? 122.32700 92.70700  108.12000 1.000 7.65834   ? 247 ILE B CA   1 
ATOM   4349 C C    . ILE B 1 247 ? 123.08200 93.96700  107.72700 1.000 11.64849  ? 247 ILE B C    1 
ATOM   4350 O O    . ILE B 1 247 ? 123.10800 94.94100  108.48700 1.000 19.19079  ? 247 ILE B O    1 
ATOM   4351 C CB   . ILE B 1 247 ? 120.80700 92.95200  108.09200 1.000 15.49151  ? 247 ILE B CB   1 
ATOM   4352 C CG1  . ILE B 1 247 ? 120.04600 91.63900  108.26200 1.000 15.42932  ? 247 ILE B CG1  1 
ATOM   4353 C CG2  . ILE B 1 247 ? 120.39900 93.63000  106.79600 1.000 7.38957   ? 247 ILE B CG2  1 
ATOM   4354 C CD1  . ILE B 1 247 ? 118.56200 91.82700  108.45900 1.000 18.89193  ? 247 ILE B CD1  1 
ATOM   4355 N N    . TRP B 1 248 ? 123.68500 93.95200  106.54400 1.000 23.21556  ? 248 TRP B N    1 
ATOM   4356 C CA   . TRP B 1 248 ? 124.56400 95.02500  106.10600 1.000 10.31156  ? 248 TRP B CA   1 
ATOM   4357 C C    . TRP B 1 248 ? 123.91400 95.83400  104.99200 1.000 11.87870  ? 248 TRP B C    1 
ATOM   4358 O O    . TRP B 1 248 ? 123.08600 95.32600  104.23300 1.000 27.85010  ? 248 TRP B O    1 
ATOM   4359 C CB   . TRP B 1 248 ? 125.90800 94.46700  105.63400 1.000 9.79442   ? 248 TRP B CB   1 
ATOM   4360 C CG   . TRP B 1 248 ? 126.52100 93.49600  106.59500 1.000 19.49785  ? 248 TRP B CG   1 
ATOM   4361 C CD1  . TRP B 1 248 ? 126.32300 92.14800  106.63700 1.000 16.07363  ? 248 TRP B CD1  1 
ATOM   4362 C CD2  . TRP B 1 248 ? 127.44000 93.79900  107.65100 1.000 19.69502  ? 248 TRP B CD2  1 
ATOM   4363 N NE1  . TRP B 1 248 ? 127.05900 91.59300  107.65300 1.000 10.10506  ? 248 TRP B NE1  1 
ATOM   4364 C CE2  . TRP B 1 248 ? 127.75500 92.58600  108.29100 1.000 18.23605  ? 248 TRP B CE2  1 
ATOM   4365 C CE3  . TRP B 1 248 ? 128.02800 94.97900  108.11600 1.000 19.29607  ? 248 TRP B CE3  1 
ATOM   4366 C CZ2  . TRP B 1 248 ? 128.63100 92.51800  109.37200 1.000 12.47885  ? 248 TRP B CZ2  1 
ATOM   4367 C CZ3  . TRP B 1 248 ? 128.89500 94.91000  109.18800 1.000 17.12567  ? 248 TRP B CZ3  1 
ATOM   4368 C CH2  . TRP B 1 248 ? 129.18900 93.68800  109.80400 1.000 13.87299  ? 248 TRP B CH2  1 
ATOM   4369 N N    . ALA B 1 249 ? 124.30400 97.10400  104.90500 1.000 11.55807  ? 249 ALA B N    1 
ATOM   4370 C CA   . ALA B 1 249 ? 123.72500 98.03100  103.94400 1.000 17.39573  ? 249 ALA B CA   1 
ATOM   4371 C C    . ALA B 1 249 ? 124.47000 98.08700  102.61700 1.000 26.77533  ? 249 ALA B C    1 
ATOM   4372 O O    . ALA B 1 249 ? 123.96900 98.71300  101.67800 1.000 32.27279  ? 249 ALA B O    1 
ATOM   4373 C CB   . ALA B 1 249 ? 123.66100 99.43800  104.54700 1.000 18.24127  ? 249 ALA B CB   1 
ATOM   4374 N N    . GLY B 1 250 ? 125.63300 97.45000  102.49700 1.000 17.91266  ? 250 GLY B N    1 
ATOM   4375 C CA   . GLY B 1 250 ? 126.28500 97.40600  101.20300 1.000 20.87397  ? 250 GLY B CA   1 
ATOM   4376 C C    . GLY B 1 250 ? 125.86600 96.18600  100.41300 1.000 34.30494  ? 250 GLY B C    1 
ATOM   4377 O O    . GLY B 1 250 ? 125.93800 96.16800  99.17600  1.000 47.53837  ? 250 GLY B O    1 
ATOM   4378 N N    . GLU B 1 251 ? 125.27200 95.22400  101.11200 1.000 28.93322  ? 251 GLU B N    1 
ATOM   4379 C CA   . GLU B 1 251 ? 124.78600 94.01600  100.47200 1.000 27.20033  ? 251 GLU B CA   1 
ATOM   4380 C C    . GLU B 1 251 ? 123.36300 94.17400  99.97100  1.000 27.84832  ? 251 GLU B C    1 
ATOM   4381 O O    . GLU B 1 251 ? 122.87200 93.29600  99.25500  1.000 37.03300  ? 251 GLU B O    1 
ATOM   4382 C CB   . GLU B 1 251 ? 124.85700 92.82900  101.43600 1.000 32.00973  ? 251 GLU B CB   1 
ATOM   4383 C CG   . GLU B 1 251 ? 126.24200 92.54000  101.97400 1.000 30.45322  ? 251 GLU B CG   1 
ATOM   4384 C CD   . GLU B 1 251 ? 126.32300 91.18700  102.64800 1.000 40.85970  ? 251 GLU B CD   1 
ATOM   4385 O OE1  . GLU B 1 251 ? 125.29100 90.48500  102.69000 1.000 39.20134  ? 251 GLU B OE1  1 
ATOM   4386 O OE2  . GLU B 1 251 ? 127.41300 90.82700  103.13800 1.000 41.46252  ? 251 GLU B OE2  1 
ATOM   4387 N N    . ASP B 1 252 ? 122.69800 95.27000  100.32600 1.000 27.27359  ? 252 ASP B N    1 
ATOM   4388 C CA   . ASP B 1 252 ? 121.41100 95.58600  99.73500  1.000 32.35526  ? 252 ASP B CA   1 
ATOM   4389 C C    . ASP B 1 252 ? 121.56500 96.47600  98.51500  1.000 37.19987  ? 252 ASP B C    1 
ATOM   4390 O O    . ASP B 1 252 ? 120.75700 96.38000  97.58800  1.000 40.55634  ? 252 ASP B O    1 
ATOM   4391 C CB   . ASP B 1 252 ? 120.51200 96.28000  100.76200 1.000 30.75921  ? 252 ASP B CB   1 
ATOM   4392 C CG   . ASP B 1 252 ? 120.23900 95.41900  101.97300 1.000 37.14518  ? 252 ASP B CG   1 
ATOM   4393 O OD1  . ASP B 1 252 ? 121.20600 94.89100  102.55600 1.000 36.80576  ? 252 ASP B OD1  1 
ATOM   4394 O OD2  . ASP B 1 252 ? 119.05800 95.27400  102.34700 1.000 42.55692  ? 252 ASP B OD2  1 
ATOM   4395 N N    . LEU B 1 253 ? 122.68100 97.19700  98.41700  1.000 35.04685  ? 253 LEU B N    1 
ATOM   4396 C CA   . LEU B 1 253 ? 122.96800 98.02800  97.25700  1.000 32.07062  ? 253 LEU B CA   1 
ATOM   4397 C C    . LEU B 1 253 ? 123.63100 97.21400  96.15500  1.000 29.81738  ? 253 LEU B C    1 
ATOM   4398 O O    . LEU B 1 253 ? 123.29400 97.37000  94.96800  1.000 42.59183  ? 253 LEU B O    1 
ATOM   4399 C CB   . LEU B 1 253 ? 123.86300 99.19900  97.67500  1.000 28.18900  ? 253 LEU B CB   1 
ATOM   4400 C CG   . LEU B 1 253 ? 124.30200 100.23700 96.64300  1.000 35.16439  ? 253 LEU B CG   1 
ATOM   4401 C CD1  . LEU B 1 253 ? 123.11500 101.04700 96.15300  1.000 35.19326  ? 253 LEU B CD1  1 
ATOM   4402 C CD2  . LEU B 1 253 ? 125.36100 101.14700 97.24100  1.000 26.26585  ? 253 LEU B CD2  1 
ATOM   4403 N N    . HIS B 1 254 ? 124.50000 96.27600  96.54200  1.000 23.82119  ? 254 HIS B N    1 
ATOM   4404 C CA   . HIS B 1 254 ? 125.07600 95.36900  95.56100  1.000 25.52015  ? 254 HIS B CA   1 
ATOM   4405 C C    . HIS B 1 254 ? 123.98200 94.51900  94.92400  1.000 30.90016  ? 254 HIS B C    1 
ATOM   4406 O O    . HIS B 1 254 ? 124.04800 94.19900  93.73200  1.000 34.10697  ? 254 HIS B O    1 
ATOM   4407 C CB   . HIS B 1 254 ? 126.14200 94.50100  96.23700  1.000 18.57122  ? 254 HIS B CB   1 
ATOM   4408 C CG   . HIS B 1 254 ? 126.67300 93.39700  95.37900  1.000 33.08460  ? 254 HIS B CG   1 
ATOM   4409 N ND1  . HIS B 1 254 ? 127.88400 93.48200  94.72600  1.000 35.53569  ? 254 HIS B ND1  1 
ATOM   4410 C CD2  . HIS B 1 254 ? 126.17200 92.17500  95.08300  1.000 39.55894  ? 254 HIS B CD2  1 
ATOM   4411 C CE1  . HIS B 1 254 ? 128.10000 92.36500  94.05600  1.000 29.90897  ? 254 HIS B CE1  1 
ATOM   4412 N NE2  . HIS B 1 254 ? 127.07600 91.55600  94.25500  1.000 33.64168  ? 254 HIS B NE2  1 
ATOM   4413 N N    . ASN B 1 255 ? 122.96500 94.15000  95.70600  1.000 22.52529  ? 255 ASN B N    1 
ATOM   4414 C CA   . ASN B 1 255 ? 121.84100 93.37600  95.18700  1.000 24.50683  ? 255 ASN B CA   1 
ATOM   4415 C C    . ASN B 1 255 ? 120.86800 94.24000  94.38600  1.000 31.60457  ? 255 ASN B C    1 
ATOM   4416 O O    . ASN B 1 255 ? 120.30300 93.77900  93.38400  1.000 36.28191  ? 255 ASN B O    1 
ATOM   4417 C CB   . ASN B 1 255 ? 121.10600 92.69700  96.34300  1.000 28.69975  ? 255 ASN B CB   1 
ATOM   4418 C CG   . ASN B 1 255 ? 121.86000 91.50400  96.89600  1.000 33.94055  ? 255 ASN B CG   1 
ATOM   4419 O OD1  . ASN B 1 255 ? 122.88100 91.09000  96.35100  1.000 35.34563  ? 255 ASN B OD1  1 
ATOM   4420 N ND2  . ASN B 1 255 ? 121.35800 90.94800  97.99100  1.000 33.11794  ? 255 ASN B ND2  1 
ATOM   4421 N N    . LEU B 1 256 ? 120.65300 95.49000  94.81200  1.000 29.72937  ? 256 LEU B N    1 
ATOM   4422 C CA   . LEU B 1 256 ? 119.73900 96.37400  94.09700  1.000 29.85527  ? 256 LEU B CA   1 
ATOM   4423 C C    . LEU B 1 256 ? 120.23500 96.66800  92.68600  1.000 33.54544  ? 256 LEU B C    1 
ATOM   4424 O O    . LEU B 1 256 ? 119.43900 96.71600  91.73600  1.000 38.66638  ? 256 LEU B O    1 
ATOM   4425 C CB   . LEU B 1 256 ? 119.55000 97.66400  94.89300  1.000 29.13298  ? 256 LEU B CB   1 
ATOM   4426 C CG   . LEU B 1 256 ? 118.63700 98.75100  94.32600  1.000 36.81534  ? 256 LEU B CG   1 
ATOM   4427 C CD1  . LEU B 1 256 ? 117.18700 98.31200  94.38400  1.000 33.39243  ? 256 LEU B CD1  1 
ATOM   4428 C CD2  . LEU B 1 256 ? 118.82900 100.04000 95.09900  1.000 32.91677  ? 256 LEU B CD2  1 
ATOM   4429 N N    . VAL B 1 257 ? 121.54600 96.86400  92.52200  1.000 22.20397  ? 257 VAL B N    1 
ATOM   4430 C CA   . VAL B 1 257 ? 122.06700 97.12000  91.17900  1.000 28.75485  ? 257 VAL B CA   1 
ATOM   4431 C C    . VAL B 1 257 ? 121.78800 95.93100  90.26200  1.000 29.12992  ? 257 VAL B C    1 
ATOM   4432 O O    . VAL B 1 257 ? 121.34000 96.09100  89.11300  1.000 34.39250  ? 257 VAL B O    1 
ATOM   4433 C CB   . VAL B 1 257 ? 123.57100 97.44400  91.24800  1.000 28.44690  ? 257 VAL B CB   1 
ATOM   4434 C CG1  . VAL B 1 257 ? 124.17500 97.48600  89.85400  1.000 26.18502  ? 257 VAL B CG1  1 
ATOM   4435 C CG2  . VAL B 1 257 ? 123.79900 98.75800  91.97600  1.000 25.27221  ? 257 VAL B CG2  1 
ATOM   4436 N N    . VAL B 1 258 ? 122.00200 94.71700  90.77400  1.000 28.40574  ? 258 VAL B N    1 
ATOM   4437 C CA   . VAL B 1 258 ? 121.79800 93.51600  89.97400  1.000 33.28088  ? 258 VAL B CA   1 
ATOM   4438 C C    . VAL B 1 258 ? 120.32400 93.32300  89.65000  1.000 29.82652  ? 258 VAL B C    1 
ATOM   4439 O O    . VAL B 1 258 ? 119.98100 92.81200  88.57900  1.000 33.47628  ? 258 VAL B O    1 
ATOM   4440 C CB   . VAL B 1 258 ? 122.38100 92.28900  90.69700  1.000 35.63677  ? 258 VAL B CB   1 
ATOM   4441 C CG1  . VAL B 1 258 ? 122.15600 91.03200  89.87500  1.000 35.18222  ? 258 VAL B CG1  1 
ATOM   4442 C CG2  . VAL B 1 258 ? 123.85800 92.49000  90.97100  1.000 28.27530  ? 258 VAL B CG2  1 
ATOM   4443 N N    . LYS B 1 259 ? 119.42900 93.71400  90.55900  1.000 29.55342  ? 259 LYS B N    1 
ATOM   4444 C CA   . LYS B 1 259 ? 118.00400 93.58000  90.27000  1.000 31.40326  ? 259 LYS B CA   1 
ATOM   4445 C C    . LYS B 1 259 ? 117.56000 94.57500  89.20100  1.000 35.65880  ? 259 LYS B C    1 
ATOM   4446 O O    . LYS B 1 259 ? 116.74100 94.24300  88.33000  1.000 39.42353  ? 259 LYS B O    1 
ATOM   4447 C CB   . LYS B 1 259 ? 117.19000 93.76600  91.54900  1.000 31.00484  ? 259 LYS B CB   1 
ATOM   4448 C CG   . LYS B 1 259 ? 115.72500 93.39500  91.40700  1.000 40.38690  ? 259 LYS B CG   1 
ATOM   4449 C CD   . LYS B 1 259 ? 114.99000 93.53100  92.72700  1.000 40.37447  ? 259 LYS B CD   1 
ATOM   4450 C CE   . LYS B 1 259 ? 113.89300 94.57900  92.63900  1.000 42.84840  ? 259 LYS B CE   1 
ATOM   4451 N NZ   . LYS B 1 259 ? 114.44300 95.96300  92.69600  1.000 38.21061  ? 259 LYS B NZ   1 
ATOM   4452 N N    . ASN B 1 260 ? 118.09300 95.79800  89.24600  1.000 36.00440  ? 260 ASN B N    1 
ATOM   4453 C CA   . ASN B 1 260 ? 117.72100 96.78500  88.23700  1.000 34.45513  ? 260 ASN B CA   1 
ATOM   4454 C C    . ASN B 1 260 ? 118.20900 96.36500  86.85500  1.000 32.84279  ? 260 ASN B C    1 
ATOM   4455 O O    . ASN B 1 260 ? 117.51600 96.57900  85.84500  1.000 33.56968  ? 260 ASN B O    1 
ATOM   4456 C CB   . ASN B 1 260 ? 118.28000 98.15700  88.61300  1.000 34.65005  ? 260 ASN B CB   1 
ATOM   4457 C CG   . ASN B 1 260 ? 117.50400 98.81400  89.73600  1.000 37.65766  ? 260 ASN B CG   1 
ATOM   4458 O OD1  . ASN B 1 260 ? 116.34700 98.47800  89.98600  1.000 41.27997  ? 260 ASN B OD1  1 
ATOM   4459 N ND2  . ASN B 1 260 ? 118.13700 99.75900  90.41800  1.000 36.75997  ? 260 ASN B ND2  1 
ATOM   4460 N N    . PHE B 1 261 ? 119.39600 95.74500  86.79300  1.000 38.04956  ? 261 PHE B N    1 
ATOM   4461 C CA   . PHE B 1 261 ? 119.91700 95.31200  85.49900  1.000 29.66880  ? 261 PHE B CA   1 
ATOM   4462 C C    . PHE B 1 261 ? 119.01100 94.28500  84.83000  1.000 32.92342  ? 261 PHE B C    1 
ATOM   4463 O O    . PHE B 1 261 ? 118.99300 94.18900  83.59800  1.000 37.57636  ? 261 PHE B O    1 
ATOM   4464 C CB   . PHE B 1 261 ? 121.32800 94.74900  85.65400  1.000 27.34693  ? 261 PHE B CB   1 
ATOM   4465 C CG   . PHE B 1 261 ? 122.40900 95.72100  85.28300  1.000 33.95992  ? 261 PHE B CG   1 
ATOM   4466 C CD1  . PHE B 1 261 ? 122.71600 95.95700  83.95600  1.000 36.04190  ? 261 PHE B CD1  1 
ATOM   4467 C CD2  . PHE B 1 261 ? 123.11500 96.40100  86.25800  1.000 35.60865  ? 261 PHE B CD2  1 
ATOM   4468 C CE1  . PHE B 1 261 ? 123.70700 96.85000  83.60800  1.000 36.48834  ? 261 PHE B CE1  1 
ATOM   4469 C CE2  . PHE B 1 261 ? 124.10800 97.29500  85.91500  1.000 37.99364  ? 261 PHE B CE2  1 
ATOM   4470 C CZ   . PHE B 1 261 ? 124.40400 97.51900  84.58800  1.000 33.83182  ? 261 PHE B CZ   1 
ATOM   4471 N N    . MET B 1 262 ? 118.25500 93.51200  85.60900  1.000 30.63881  ? 262 MET B N    1 
ATOM   4472 C CA   . MET B 1 262 ? 117.34600 92.52800  85.03200  1.000 32.21483  ? 262 MET B CA   1 
ATOM   4473 C C    . MET B 1 262 ? 115.96800 93.11000  84.76200  1.000 34.61879  ? 262 MET B C    1 
ATOM   4474 O O    . MET B 1 262 ? 115.31000 92.72400  83.78100  1.000 37.38440  ? 262 MET B O    1 
ATOM   4475 C CB   . MET B 1 262 ? 117.21600 91.31200  85.95400  1.000 33.43850  ? 262 MET B CB   1 
ATOM   4476 C CG   . MET B 1 262 ? 118.51800 90.86100  86.58800  1.000 34.97680  ? 262 MET B CG   1 
ATOM   4477 S SD   . MET B 1 262 ? 119.56700 89.99000  85.40800  1.000 53.12116  ? 262 MET B SD   1 
ATOM   4478 C CE   . MET B 1 262 ? 121.13100 89.97500  86.27600  1.000 39.98609  ? 262 MET B CE   1 
ATOM   4479 N N    . ASN B 1 263 ? 115.53800 94.06200  85.59100  1.000 38.34634  ? 263 ASN B N    1 
ATOM   4480 C CA   . ASN B 1 263 ? 114.24400 94.69000  85.35400  1.000 36.06060  ? 263 ASN B CA   1 
ATOM   4481 C C    . ASN B 1 263 ? 114.24900 95.47500  84.04900  1.000 33.02436  ? 263 ASN B C    1 
ATOM   4482 O O    . ASN B 1 263 ? 113.25900 95.45600  83.30600  1.000 33.52834  ? 263 ASN B O    1 
ATOM   4483 C CB   . ASN B 1 263 ? 113.87000 95.59800  86.52400  1.000 36.13322  ? 263 ASN B CB   1 
ATOM   4484 C CG   . ASN B 1 263 ? 113.57000 94.82400  87.78900  1.000 42.63906  ? 263 ASN B CG   1 
ATOM   4485 O OD1  . ASN B 1 263 ? 113.39000 93.60800  87.75700  1.000 40.10263  ? 263 ASN B OD1  1 
ATOM   4486 N ND2  . ASN B 1 263 ? 113.50800 95.52800  88.91100  1.000 41.20275  ? 263 ASN B ND2  1 
ATOM   4487 N N    . VAL B 1 264 ? 115.35300 96.16000  83.74000  1.000 34.08733  ? 264 VAL B N    1 
ATOM   4488 C CA   . VAL B 1 264 ? 115.37900 96.93900  82.50300  1.000 33.40080  ? 264 VAL B CA   1 
ATOM   4489 C C    . VAL B 1 264 ? 115.29600 96.02600  81.28000  1.000 36.58838  ? 264 VAL B C    1 
ATOM   4490 O O    . VAL B 1 264 ? 114.60700 96.34000  80.29800  1.000 38.43214  ? 264 VAL B O    1 
ATOM   4491 C CB   . VAL B 1 264 ? 116.63100 97.83300  82.45900  1.000 29.74291  ? 264 VAL B CB   1 
ATOM   4492 C CG1  . VAL B 1 264 ? 116.70700 98.57000  81.13300  1.000 31.39649  ? 264 VAL B CG1  1 
ATOM   4493 C CG2  . VAL B 1 264 ? 116.61600 98.81600  83.61200  1.000 32.32620  ? 264 VAL B CG2  1 
ATOM   4494 N N    . ALA B 1 265 ? 115.96500 94.87100  81.32600  1.000 34.43715  ? 265 ALA B N    1 
ATOM   4495 C CA   . ALA B 1 265 ? 115.90500 93.93700  80.20400  1.000 34.78833  ? 265 ALA B CA   1 
ATOM   4496 C C    . ALA B 1 265 ? 114.50400 93.36300  80.03600  1.000 38.90596  ? 265 ALA B C    1 
ATOM   4497 O O    . ALA B 1 265 ? 113.99300 93.26000  78.90800  1.000 41.42141  ? 265 ALA B O    1 
ATOM   4498 C CB   . ALA B 1 265 ? 116.92500 92.81600  80.39800  1.000 34.41734  ? 265 ALA B CB   1 
ATOM   4499 N N    . THR B 1 266 ? 113.85800 93.00200  81.14800  1.000 38.61850  ? 266 THR B N    1 
ATOM   4500 C CA   . THR B 1 266 ? 112.50000 92.48200  81.04600  1.000 37.91849  ? 266 THR B CA   1 
ATOM   4501 C C    . THR B 1 266 ? 111.56200 93.53300  80.46600  1.000 39.10040  ? 266 THR B C    1 
ATOM   4502 O O    . THR B 1 266 ? 110.71900 93.22400  79.61500  1.000 39.89430  ? 266 THR B O    1 
ATOM   4503 C CB   . THR B 1 266 ? 112.00500 92.01400  82.41400  1.000 38.29901  ? 266 THR B CB   1 
ATOM   4504 O OG1  . THR B 1 266 ? 112.71500 90.83300  82.80300  1.000 39.42439  ? 266 THR B OG1  1 
ATOM   4505 C CG2  . THR B 1 266 ? 110.51900 91.71000  82.36700  1.000 37.25859  ? 266 THR B CG2  1 
ATOM   4506 N N    . SER B 1 267 ? 111.70100 94.78500  80.91000  1.000 41.83709  ? 267 SER B N    1 
ATOM   4507 C CA   . SER B 1 267 ? 110.84900 95.84800  80.39100  1.000 40.49561  ? 267 SER B CA   1 
ATOM   4508 C C    . SER B 1 267 ? 111.05900 96.05100  78.89600  1.000 43.22576  ? 267 SER B C    1 
ATOM   4509 O O    . SER B 1 267 ? 110.09100 96.22100  78.14700  1.000 46.12510  ? 267 SER B O    1 
ATOM   4510 C CB   . SER B 1 267 ? 111.10800 97.14700  81.15100  1.000 45.94395  ? 267 SER B CB   1 
ATOM   4511 O OG   . SER B 1 267 ? 110.59800 97.07100  82.47000  1.000 51.90346  ? 267 SER B OG   1 
ATOM   4512 N N    . LEU B 1 268 ? 112.31400 96.04800  78.44000  1.000 37.70858  ? 268 LEU B N    1 
ATOM   4513 C CA   . LEU B 1 268 ? 112.56900 96.24200  77.01400  1.000 37.51037  ? 268 LEU B CA   1 
ATOM   4514 C C    . LEU B 1 268 ? 111.93300 95.13100  76.18500  1.000 42.44806  ? 268 LEU B C    1 
ATOM   4515 O O    . LEU B 1 268 ? 111.27800 95.39000  75.16100  1.000 45.80837  ? 268 LEU B O    1 
ATOM   4516 C CB   . LEU B 1 268 ? 114.07400 96.31200  76.75300  1.000 37.08104  ? 268 LEU B CB   1 
ATOM   4517 C CG   . LEU B 1 268 ? 114.50600 96.42900  75.28800  1.000 37.80876  ? 268 LEU B CG   1 
ATOM   4518 C CD1  . LEU B 1 268 ? 114.40600 97.86600  74.80200  1.000 37.49368  ? 268 LEU B CD1  1 
ATOM   4519 C CD2  . LEU B 1 268 ? 115.91200 95.89200  75.09300  1.000 37.05622  ? 268 LEU B CD2  1 
ATOM   4520 N N    . GLU B 1 269 ? 112.10300 93.87900  76.62200  1.000 47.89853  ? 269 GLU B N    1 
ATOM   4521 C CA   . GLU B 1 269 ? 111.52800 92.77300  75.86300  1.000 46.36373  ? 269 GLU B CA   1 
ATOM   4522 C C    . GLU B 1 269 ? 110.00600 92.85100  75.84600  1.000 50.10846  ? 269 GLU B C    1 
ATOM   4523 O O    . GLU B 1 269 ? 109.37300 92.65100  74.79800  1.000 46.68067  ? 269 GLU B O    1 
ATOM   4524 C CB   . GLU B 1 269 ? 111.98800 91.43900  76.44800  1.000 48.11747  ? 269 GLU B CB   1 
ATOM   4525 C CG   . GLU B 1 269 ? 113.28800 90.91700  75.86700  1.000 50.81813  ? 269 GLU B CG   1 
ATOM   4526 C CD   . GLU B 1 269 ? 113.66100 89.55400  76.41500  1.000 55.71904  ? 269 GLU B CD   1 
ATOM   4527 O OE1  . GLU B 1 269 ? 113.41800 89.30800  77.61500  1.000 49.85748  ? 269 GLU B OE1  1 
ATOM   4528 O OE2  . GLU B 1 269 ? 114.19600 88.72800  75.64600  1.000 53.01356  ? 269 GLU B OE2  1 
ATOM   4529 N N    . GLY B 1 270 ? 109.40200 93.18200  76.99100  1.000 53.83180  ? 270 GLY B N    1 
ATOM   4530 C CA   . GLY B 1 270 ? 107.95600 93.30200  77.03900  1.000 49.38763  ? 270 GLY B CA   1 
ATOM   4531 C C    . GLY B 1 270 ? 107.43100 94.43100  76.17600  1.000 48.60567  ? 270 GLY B C    1 
ATOM   4532 O O    . GLY B 1 270 ? 106.37600 94.30600  75.55400  1.000 52.32616  ? 270 GLY B O    1 
ATOM   4533 N N    . CYS B 1 271 ? 108.17900 95.53300  76.09000  1.000 50.67358  ? 271 CYS B N    1 
ATOM   4534 C CA   . CYS B 1 271 ? 107.73300 96.64700  75.26000  1.000 49.98343  ? 271 CYS B CA   1 
ATOM   4535 C C    . CYS B 1 271 ? 107.77800 96.28400  73.78400  1.000 47.63240  ? 271 CYS B C    1 
ATOM   4536 O O    . CYS B 1 271 ? 106.83700 96.58200  73.03700  1.000 47.91014  ? 271 CYS B O    1 
ATOM   4537 C CB   . CYS B 1 271 ? 108.58200 97.88800  75.53400  1.000 50.19543  ? 271 CYS B CB   1 
ATOM   4538 S SG   . CYS B 1 271 ? 108.22500 98.70600  77.10400  1.000 64.91502  ? 271 CYS B SG   1 
ATOM   4539 N N    . VAL B 1 272 ? 108.84700 95.61700  73.34300  1.000 51.24853  ? 272 VAL B N    1 
ATOM   4540 C CA   . VAL B 1 272 ? 108.92100 95.28900  71.92100  1.000 51.85885  ? 272 VAL B CA   1 
ATOM   4541 C C    . VAL B 1 272 ? 107.86600 94.24700  71.56400  1.000 53.00558  ? 272 VAL B C    1 
ATOM   4542 O O    . VAL B 1 272 ? 107.23000 94.32000  70.50000  1.000 49.11354  ? 272 VAL B O    1 
ATOM   4543 C CB   . VAL B 1 272 ? 110.33600 94.81900  71.54300  1.000 52.20496  ? 272 VAL B CB   1 
ATOM   4544 C CG1  . VAL B 1 272 ? 110.38300 94.43000  70.07600  1.000 49.28622  ? 272 VAL B CG1  1 
ATOM   4545 C CG2  . VAL B 1 272 ? 111.35200 95.90900  71.83800  1.000 52.91198  ? 272 VAL B CG2  1 
ATOM   4546 N N    . ASN B 1 273 ? 107.60600 93.30300  72.47600  1.000 56.69761  ? 273 ASN B N    1 
ATOM   4547 C CA   . ASN B 1 273 ? 106.58000 92.30300  72.20100  1.000 53.60490  ? 273 ASN B CA   1 
ATOM   4548 C C    . ASN B 1 273 ? 105.19200 92.93000  72.18500  1.000 52.83316  ? 273 ASN B C    1 
ATOM   4549 O O    . ASN B 1 273 ? 104.36200 92.59100  71.33400  1.000 52.22063  ? 273 ASN B O    1 
ATOM   4550 C CB   . ASN B 1 273 ? 106.65000 91.17400  73.22800  1.000 51.75058  ? 273 ASN B CB   1 
ATOM   4551 C CG   . ASN B 1 273 ? 107.73600 90.16500  72.91100  1.000 55.07816  ? 273 ASN B CG   1 
ATOM   4552 O OD1  . ASN B 1 273 ? 108.22600 90.09500  71.78400  1.000 54.23112  ? 273 ASN B OD1  1 
ATOM   4553 N ND2  . ASN B 1 273 ? 108.11800 89.37600  73.90700  1.000 53.73749  ? 273 ASN B ND2  1 
ATOM   4554 N N    . GLY B 1 274 ? 104.91900 93.84900  73.11400  1.000 54.11761  ? 274 GLY B N    1 
ATOM   4555 C CA   . GLY B 1 274 ? 103.63100 94.51700  73.11600  1.000 54.01778  ? 274 GLY B CA   1 
ATOM   4556 C C    . GLY B 1 274 ? 103.40400 95.35600  71.87500  1.000 54.69806  ? 274 GLY B C    1 
ATOM   4557 O O    . GLY B 1 274 ? 102.28800 95.41900  71.35500  1.000 54.07828  ? 274 GLY B O    1 
ATOM   4558 N N    . TYR B 1 275 ? 104.45500 96.01900  71.38200  1.000 53.80433  ? 275 TYR B N    1 
ATOM   4559 C CA   . TYR B 1 275 ? 104.28500 96.79500  70.15800  1.000 51.19790  ? 275 TYR B CA   1 
ATOM   4560 C C    . TYR B 1 275 ? 104.03400 95.89300  68.95700  1.000 54.57368  ? 275 TYR B C    1 
ATOM   4561 O O    . TYR B 1 275 ? 103.21700 96.22500  68.09000  1.000 54.06018  ? 275 TYR B O    1 
ATOM   4562 C CB   . TYR B 1 275 ? 105.49000 97.69300  69.89800  1.000 52.71736  ? 275 TYR B CB   1 
ATOM   4563 C CG   . TYR B 1 275 ? 105.27300 98.60900  68.71300  1.000 54.18275  ? 275 TYR B CG   1 
ATOM   4564 C CD1  . TYR B 1 275 ? 104.56300 99.79500  68.85000  1.000 54.19905  ? 275 TYR B CD1  1 
ATOM   4565 C CD2  . TYR B 1 275 ? 105.76400 98.28400  67.45700  1.000 52.84510  ? 275 TYR B CD2  1 
ATOM   4566 C CE1  . TYR B 1 275 ? 104.35400 100.63200 67.77200  1.000 51.61376  ? 275 TYR B CE1  1 
ATOM   4567 C CE2  . TYR B 1 275 ? 105.56300 99.11700  66.37200  1.000 52.71979  ? 275 TYR B CE2  1 
ATOM   4568 C CZ   . TYR B 1 275 ? 104.85700 100.28900 66.53600  1.000 55.73027  ? 275 TYR B CZ   1 
ATOM   4569 O OH   . TYR B 1 275 ? 104.65600 101.12200 65.46000  1.000 56.30172  ? 275 TYR B OH   1 
ATOM   4570 N N    . LEU B 1 276 ? 104.71800 94.75200  68.87900  1.000 64.77392  ? 276 LEU B N    1 
ATOM   4571 C CA   . LEU B 1 276 ? 104.53600 93.88900  67.71800  1.000 61.79951  ? 276 LEU B CA   1 
ATOM   4572 C C    . LEU B 1 276 ? 103.38300 92.90600  67.88000  1.000 62.89022  ? 276 LEU B C    1 
ATOM   4573 O O    . LEU B 1 276 ? 103.13700 92.10900  66.97000  1.000 64.79448  ? 276 LEU B O    1 
ATOM   4574 C CB   . LEU B 1 276 ? 105.82400 93.12100  67.40800  1.000 63.18494  ? 276 LEU B CB   1 
ATOM   4575 C CG   . LEU B 1 276 ? 106.91400 93.90000  66.67300  1.000 63.16929  ? 276 LEU B CG   1 
ATOM   4576 C CD1  . LEU B 1 276 ? 108.17700 93.06400  66.55100  1.000 65.03385  ? 276 LEU B CD1  1 
ATOM   4577 C CD2  . LEU B 1 276 ? 106.42200 94.33900  65.30300  1.000 59.14673  ? 276 LEU B CD2  1 
ATOM   4578 N N    . ARG B 1 277 ? 102.67000 92.94800  69.00300  1.000 72.21775  ? 277 ARG B N    1 
ATOM   4579 C CA   . ARG B 1 277 ? 101.53500 92.05900  69.20400  1.000 72.93567  ? 277 ARG B CA   1 
ATOM   4580 C C    . ARG B 1 277 ? 100.48500 92.26800  68.12000  1.000 73.33371  ? 277 ARG B C    1 
ATOM   4581 O O    . ARG B 1 277 ? 100.26200 93.38800  67.65400  1.000 72.96006  ? 277 ARG B O    1 
ATOM   4582 C CB   . ARG B 1 277 ? 100.91800 92.29000  70.58200  1.000 72.79309  ? 277 ARG B CB   1 
ATOM   4583 C CG   . ARG B 1 277 ? 99.82000  91.30200  70.94100  1.000 73.08994  ? 277 ARG B CG   1 
ATOM   4584 C CD   . ARG B 1 277 ? 99.19500  91.61400  72.29500  1.000 74.19213  ? 277 ARG B CD   1 
ATOM   4585 N NE   . ARG B 1 277 ? 99.11000  93.04300  72.58000  1.000 75.22853  ? 277 ARG B NE   1 
ATOM   4586 C CZ   . ARG B 1 277 ? 98.58400  93.94900  71.76600  1.000 75.46341  ? 277 ARG B CZ   1 
ATOM   4587 N NH1  . ARG B 1 277 ? 98.07700  93.61500  70.59100  1.000 73.94371  ? 277 ARG B NH1  1 
ATOM   4588 N NH2  . ARG B 1 277 ? 98.56300  95.22400  72.14400  1.000 73.94835  ? 277 ARG B NH2  1 
ATOM   4589 N N    . CYS B 1 278 ? 99.83800  91.17800  67.72100  1.000 81.85040  ? 278 CYS B N    1 
ATOM   4590 C CA   . CYS B 1 278 ? 98.83500  91.22700  66.66400  1.000 82.77051  ? 278 CYS B CA   1 
ATOM   4591 C C    . CYS B 1 278 ? 97.46400  91.58400  67.22900  1.000 82.85935  ? 278 CYS B C    1 
ATOM   4592 O O    . CYS B 1 278 ? 96.43900  91.37100  66.58000  1.000 82.25665  ? 278 CYS B O    1 
ATOM   4593 C CB   . CYS B 1 278 ? 98.76600  89.88900  65.92500  1.000 82.84053  ? 278 CYS B CB   1 
ATOM   4594 S SG   . CYS B 1 278 ? 99.77600  89.80600  64.42900  1.000 86.45198  ? 278 CYS B SG   1 
ATOM   4595 N N    . VAL B 1 298 ? 106.50800 95.46700  82.00100  1.000 61.47697  ? 298 VAL B N    1 
ATOM   4596 C CA   . VAL B 1 298 ? 106.64700 96.48200  80.96400  1.000 65.74653  ? 298 VAL B CA   1 
ATOM   4597 C C    . VAL B 1 298 ? 106.64800 97.87000  81.59000  1.000 65.59049  ? 298 VAL B C    1 
ATOM   4598 O O    . VAL B 1 298 ? 107.04100 98.85000  80.95800  1.000 66.83641  ? 298 VAL B O    1 
ATOM   4599 C CB   . VAL B 1 298 ? 105.52800 96.35700  79.91700  1.000 64.41395  ? 298 VAL B CB   1 
ATOM   4600 C CG1  . VAL B 1 298 ? 105.74500 97.34700  78.78500  1.000 59.05981  ? 298 VAL B CG1  1 
ATOM   4601 C CG2  . VAL B 1 298 ? 105.45800 94.93500  79.38600  1.000 63.40384  ? 298 VAL B CG2  1 
ATOM   4602 N N    . TYR B 1 299 ? 106.20100 97.94100  82.84100  1.000 65.53500  ? 299 TYR B N    1 
ATOM   4603 C CA   . TYR B 1 299 ? 106.11000 99.18900  83.58900  1.000 67.90023  ? 299 TYR B CA   1 
ATOM   4604 C C    . TYR B 1 299 ? 106.89900 99.14000  84.88700  1.000 69.68617  ? 299 TYR B C    1 
ATOM   4605 O O    . TYR B 1 299 ? 107.67900 100.06100 85.17600  1.000 69.55241  ? 299 TYR B O    1 
ATOM   4606 C CB   . TYR B 1 299 ? 104.63000 99.50400  83.86700  1.000 70.16482  ? 299 TYR B CB   1 
ATOM   4607 C CG   . TYR B 1 299 ? 104.35000 100.89800 84.38300  1.000 70.68158  ? 299 TYR B CG   1 
ATOM   4608 C CD1  . TYR B 1 299 ? 104.45900 101.19600 85.73400  1.000 70.01129  ? 299 TYR B CD1  1 
ATOM   4609 C CD2  . TYR B 1 299 ? 103.97100 101.91400 83.51700  1.000 69.94581  ? 299 TYR B CD2  1 
ATOM   4610 C CE1  . TYR B 1 299 ? 104.19300 102.46700 86.20800  1.000 70.28551  ? 299 TYR B CE1  1 
ATOM   4611 C CE2  . TYR B 1 299 ? 103.70900 103.18900 83.98100  1.000 70.53241  ? 299 TYR B CE2  1 
ATOM   4612 C CZ   . TYR B 1 299 ? 103.82400 103.46000 85.32700  1.000 71.41158  ? 299 TYR B CZ   1 
ATOM   4613 O OH   . TYR B 1 299 ? 103.56400 104.72800 85.79300  1.000 68.69214  ? 299 TYR B OH   1 
ATOM   4614 N N    . LYS B 1 300 ? 106.72900 98.07200  85.66900  1.000 71.97154  ? 300 LYS B N    1 
ATOM   4615 C CA   . LYS B 1 300 ? 107.37500 97.99000  86.97300  1.000 72.99163  ? 300 LYS B CA   1 
ATOM   4616 C C    . LYS B 1 300 ? 108.89200 98.02900  86.84800  1.000 73.09092  ? 300 LYS B C    1 
ATOM   4617 O O    . LYS B 1 300 ? 109.56900 98.65700  87.66600  1.000 71.39294  ? 300 LYS B O    1 
ATOM   4618 C CB   . LYS B 1 300 ? 106.93000 96.72100  87.69900  1.000 70.58613  ? 300 LYS B CB   1 
ATOM   4619 N N    . GLY B 1 301 ? 109.44600 97.36200  85.83900  1.000 65.07720  ? 301 GLY B N    1 
ATOM   4620 C CA   . GLY B 1 301 ? 110.88700 97.31500  85.69200  1.000 59.75112  ? 301 GLY B CA   1 
ATOM   4621 C C    . GLY B 1 301 ? 111.53700 98.67900  85.57900  1.000 59.88322  ? 301 GLY B C    1 
ATOM   4622 O O    . GLY B 1 301 ? 112.36700 99.05700  86.41500  1.000 64.46561  ? 301 GLY B O    1 
ATOM   4623 N N    . TYR B 1 302 ? 111.15300 99.44100  84.55200  1.000 59.16237  ? 302 TYR B N    1 
ATOM   4624 C CA   . TYR B 1 302 ? 111.74400 100.76200 84.37700  1.000 62.19485  ? 302 TYR B CA   1 
ATOM   4625 C C    . TYR B 1 302 ? 111.30400 101.72200 85.47500  1.000 61.79771  ? 302 TYR B C    1 
ATOM   4626 O O    . TYR B 1 302 ? 112.06900 102.61900 85.84600  1.000 64.46885  ? 302 TYR B O    1 
ATOM   4627 C CB   . TYR B 1 302 ? 111.43200 101.31100 82.97800  1.000 62.82084  ? 302 TYR B CB   1 
ATOM   4628 C CG   . TYR B 1 302 ? 110.03100 101.83700 82.74200  1.000 61.57594  ? 302 TYR B CG   1 
ATOM   4629 C CD1  . TYR B 1 302 ? 109.61700 103.04900 83.28000  1.000 60.87544  ? 302 TYR B CD1  1 
ATOM   4630 C CD2  . TYR B 1 302 ? 109.13600 101.13600 81.94700  1.000 60.46145  ? 302 TYR B CD2  1 
ATOM   4631 C CE1  . TYR B 1 302 ? 108.34400 103.53200 83.05400  1.000 60.82347  ? 302 TYR B CE1  1 
ATOM   4632 C CE2  . TYR B 1 302 ? 107.86200 101.61400 81.71400  1.000 61.83592  ? 302 TYR B CE2  1 
ATOM   4633 C CZ   . TYR B 1 302 ? 107.47200 102.81200 82.27000  1.000 63.22605  ? 302 TYR B CZ   1 
ATOM   4634 O OH   . TYR B 1 302 ? 106.20300 103.29100 82.04000  1.000 61.87424  ? 302 TYR B OH   1 
ATOM   4635 N N    . ARG B 1 303 ? 110.09200 101.55900 86.01500  1.000 65.84460  ? 303 ARG B N    1 
ATOM   4636 C CA   . ARG B 1 303 ? 109.67700 102.42700 87.11200  1.000 67.95850  ? 303 ARG B CA   1 
ATOM   4637 C C    . ARG B 1 303 ? 110.55700 102.22200 88.33900  1.000 68.60921  ? 303 ARG B C    1 
ATOM   4638 O O    . ARG B 1 303 ? 110.90100 103.18500 89.03500  1.000 67.95350  ? 303 ARG B O    1 
ATOM   4639 C CB   . ARG B 1 303 ? 108.21200 102.17200 87.45800  1.000 68.95440  ? 303 ARG B CB   1 
ATOM   4640 C CG   . ARG B 1 303 ? 107.23100 102.87100 86.54400  1.000 68.12597  ? 303 ARG B CG   1 
ATOM   4641 C CD   . ARG B 1 303 ? 107.46900 104.37000 86.52200  1.000 70.00857  ? 303 ARG B CD   1 
ATOM   4642 N NE   . ARG B 1 303 ? 106.62700 105.03900 85.53800  1.000 72.13482  ? 303 ARG B NE   1 
ATOM   4643 C CZ   . ARG B 1 303 ? 106.65600 106.34100 85.29000  1.000 70.87280  ? 303 ARG B CZ   1 
ATOM   4644 N NH1  . ARG B 1 303 ? 107.47400 107.15100 85.94100  1.000 69.11541  ? 303 ARG B NH1  1 
ATOM   4645 N NH2  . ARG B 1 303 ? 105.84100 106.84400 84.36600  1.000 70.56574  ? 303 ARG B NH2  1 
ATOM   4646 N N    . SER B 1 304 ? 110.93300 100.97300 88.61900  1.000 65.56349  ? 304 SER B N    1 
ATOM   4647 C CA   . SER B 1 304 ? 111.81700 100.69000 89.74300  1.000 66.30702  ? 304 SER B CA   1 
ATOM   4648 C C    . SER B 1 304 ? 113.23800 101.14700 89.45100  1.000 65.88981  ? 304 SER B C    1 
ATOM   4649 O O    . SER B 1 304 ? 113.94100 101.62100 90.35100  1.000 63.31647  ? 304 SER B O    1 
ATOM   4650 C CB   . SER B 1 304 ? 111.78800 99.19600  90.06700  1.000 65.27734  ? 304 SER B CB   1 
ATOM   4651 O OG   . SER B 1 304 ? 110.50900 98.79700  90.52600  1.000 65.36211  ? 304 SER B OG   1 
ATOM   4652 N N    . ALA B 1 305 ? 113.67800 101.01400 88.19900  1.000 62.38953  ? 305 ALA B N    1 
ATOM   4653 C CA   . ALA B 1 305 ? 115.03700 101.40300 87.84400  1.000 58.30969  ? 305 ALA B CA   1 
ATOM   4654 C C    . ALA B 1 305 ? 115.19500 102.90200 87.62400  1.000 58.62792  ? 305 ALA B C    1 
ATOM   4655 O O    . ALA B 1 305 ? 116.32700 103.36600 87.45200  1.000 60.69745  ? 305 ALA B O    1 
ATOM   4656 C CB   . ALA B 1 305 ? 115.48400 100.65300 86.58700  1.000 56.51787  ? 305 ALA B CB   1 
ATOM   4657 N N    . VAL B 1 306 ? 114.10500 103.66700 87.62400  1.000 62.09881  ? 306 VAL B N    1 
ATOM   4658 C CA   . VAL B 1 306 ? 114.15900 105.11100 87.42900  1.000 62.52974  ? 306 VAL B CA   1 
ATOM   4659 C C    . VAL B 1 306 ? 113.73800 105.88300 88.67200  1.000 61.17812  ? 306 VAL B C    1 
ATOM   4660 O O    . VAL B 1 306 ? 113.85400 107.11800 88.69200  1.000 63.12229  ? 306 VAL B O    1 
ATOM   4661 C CB   . VAL B 1 306 ? 113.30500 105.52500 86.21100  1.000 62.12815  ? 306 VAL B CB   1 
ATOM   4662 C CG1  . VAL B 1 306 ? 112.80900 106.95900 86.31900  1.000 60.82943  ? 306 VAL B CG1  1 
ATOM   4663 C CG2  . VAL B 1 306 ? 114.09000 105.32700 84.92100  1.000 57.71139  ? 306 VAL B CG2  1 
ATOM   4664 N N    . GLU B 1 307 ? 113.32200 105.19500 89.73700  1.000 67.58339  ? 307 GLU B N    1 
ATOM   4665 C CA   . GLU B 1 307 ? 112.77000 105.85700 90.91300  1.000 67.76641  ? 307 GLU B CA   1 
ATOM   4666 C C    . GLU B 1 307 ? 113.43900 105.44700 92.22100  1.000 68.34539  ? 307 GLU B C    1 
ATOM   4667 O O    . GLU B 1 307 ? 112.92300 105.78700 93.29300  1.000 70.41301  ? 307 GLU B O    1 
ATOM   4668 C CB   . GLU B 1 307 ? 111.26200 105.59800 91.00700  1.000 65.77571  ? 307 GLU B CB   1 
ATOM   4669 N N    . SER B 1 308 ? 114.56300 104.73100 92.17700  1.000 62.10869  ? 308 SER B N    1 
ATOM   4670 C CA   . SER B 1 308 ? 115.21800 104.25900 93.39100  1.000 62.72407  ? 308 SER B CA   1 
ATOM   4671 C C    . SER B 1 308 ? 116.54500 104.96100 93.67000  1.000 61.98186  ? 308 SER B C    1 
ATOM   4672 O O    . SER B 1 308 ? 117.36200 104.44400 94.43800  1.000 62.49062  ? 308 SER B O    1 
ATOM   4673 C CB   . SER B 1 308 ? 115.42800 102.74500 93.31800  1.000 62.00129  ? 308 SER B CB   1 
ATOM   4674 O OG   . SER B 1 308 ? 116.59500 102.42500 92.58200  1.000 60.95000  ? 308 SER B OG   1 
ATOM   4675 N N    . THR B 1 309 ? 116.78100 106.12600 93.06300  1.000 59.39817  ? 309 THR B N    1 
ATOM   4676 C CA   . THR B 1 309 ? 118.02400 106.84900 93.32200  1.000 61.79167  ? 309 THR B CA   1 
ATOM   4677 C C    . THR B 1 309 ? 118.16800 107.21000 94.79700  1.000 57.65299  ? 309 THR B C    1 
ATOM   4678 O O    . THR B 1 309 ? 119.28000 107.17700 95.34300  1.000 57.04445  ? 309 THR B O    1 
ATOM   4679 C CB   . THR B 1 309 ? 118.09800 108.10700 92.45600  1.000 60.27881  ? 309 THR B CB   1 
ATOM   4680 O OG1  . THR B 1 309 ? 119.43500 108.62100 92.47100  1.000 57.26830  ? 309 THR B OG1  1 
ATOM   4681 C CG2  . THR B 1 309 ? 117.14700 109.17200 92.97600  1.000 61.38008  ? 309 THR B CG2  1 
ATOM   4682 N N    . SER B 1 310 ? 117.05500 107.50100 95.47400  1.000 53.95430  ? 310 SER B N    1 
ATOM   4683 C CA   . SER B 1 310 ? 117.13900 107.87800 96.88000  1.000 55.73188  ? 310 SER B CA   1 
ATOM   4684 C C    . SER B 1 310 ? 117.46700 106.67100 97.74500  1.000 56.78550  ? 310 SER B C    1 
ATOM   4685 O O    . SER B 1 310 ? 118.19900 106.79200 98.73400  1.000 55.41542  ? 310 SER B O    1 
ATOM   4686 C CB   . SER B 1 310 ? 115.83000 108.52600 97.32800  1.000 56.33970  ? 310 SER B CB   1 
ATOM   4687 O OG   . SER B 1 310 ? 114.71300 107.78500 96.87000  1.000 58.52224  ? 310 SER B OG   1 
ATOM   4688 N N    . GLN B 1 311 ? 116.91900 105.50300 97.40700  1.000 54.71331  ? 311 GLN B N    1 
ATOM   4689 C CA   . GLN B 1 311 ? 117.29700 104.29900 98.13400  1.000 54.75924  ? 311 GLN B CA   1 
ATOM   4690 C C    . GLN B 1 311 ? 118.78600 104.03100 97.97400  1.000 49.92217  ? 311 GLN B C    1 
ATOM   4691 O O    . GLN B 1 311 ? 119.46900 103.66700 98.93900  1.000 50.88670  ? 311 GLN B O    1 
ATOM   4692 C CB   . GLN B 1 311 ? 116.47900 103.10400 97.64700  1.000 55.82834  ? 311 GLN B CB   1 
ATOM   4693 C CG   . GLN B 1 311 ? 115.81400 102.31700 98.76300  1.000 55.58182  ? 311 GLN B CG   1 
ATOM   4694 C CD   . GLN B 1 311 ? 114.95700 101.18200 98.24300  1.000 58.66179  ? 311 GLN B CD   1 
ATOM   4695 O OE1  . GLN B 1 311 ? 115.33400 100.48600 97.30100  1.000 59.42871  ? 311 GLN B OE1  1 
ATOM   4696 N NE2  . GLN B 1 311 ? 113.79700 100.98600 98.85900  1.000 59.91732  ? 311 GLN B NE2  1 
ATOM   4697 N N    . GLU B 1 312 ? 119.31500 104.25900 96.76900  1.000 40.18728  ? 312 GLU B N    1 
ATOM   4698 C CA   . GLU B 1 312 ? 120.72100 104.02300 96.47600  1.000 43.58663  ? 312 GLU B CA   1 
ATOM   4699 C C    . GLU B 1 312 ? 121.62900 105.10400 97.03900  1.000 47.75725  ? 312 GLU B C    1 
ATOM   4700 O O    . GLU B 1 312 ? 122.85100 104.92300 97.04000  1.000 51.43324  ? 312 GLU B O    1 
ATOM   4701 C CB   . GLU B 1 312 ? 120.93300 103.91500 94.96600  1.000 45.23792  ? 312 GLU B CB   1 
ATOM   4702 C CG   . GLU B 1 312 ? 119.99300 102.94200 94.28300  1.000 51.34046  ? 312 GLU B CG   1 
ATOM   4703 C CD   . GLU B 1 312 ? 120.10600 102.99200 92.77600  1.000 50.07071  ? 312 GLU B CD   1 
ATOM   4704 O OE1  . GLU B 1 312 ? 121.24400 103.06300 92.27000  1.000 51.39836  ? 312 GLU B OE1  1 
ATOM   4705 O OE2  . GLU B 1 312 ? 119.05700 102.96200 92.09800  1.000 49.01925  ? 312 GLU B OE2  1 
ATOM   4706 N N    . GLU B 1 313 ? 121.07100 106.21500 97.51500  1.000 46.92450  ? 313 GLU B N    1 
ATOM   4707 C CA   . GLU B 1 313 ? 121.87600 107.21900 98.19800  1.000 39.78931  ? 313 GLU B CA   1 
ATOM   4708 C C    . GLU B 1 313 ? 121.81500 107.07000 99.70900  1.000 41.88265  ? 313 GLU B C    1 
ATOM   4709 O O    . GLU B 1 313 ? 122.82300 107.29000 100.39000 1.000 44.11487  ? 313 GLU B O    1 
ATOM   4710 C CB   . GLU B 1 313 ? 121.42800 108.63200 97.81200  1.000 43.88263  ? 313 GLU B CB   1 
ATOM   4711 C CG   . GLU B 1 313 ? 121.28900 108.86000 96.32000  1.000 48.26461  ? 313 GLU B CG   1 
ATOM   4712 C CD   . GLU B 1 313 ? 122.59400 109.27000 95.67000  1.000 50.11635  ? 313 GLU B CD   1 
ATOM   4713 O OE1  . GLU B 1 313 ? 123.50100 109.73200 96.39300  1.000 48.87515  ? 313 GLU B OE1  1 
ATOM   4714 O OE2  . GLU B 1 313 ? 122.71100 109.13400 94.43400  1.000 51.29437  ? 313 GLU B OE2  1 
ATOM   4715 N N    . SER B 1 314 ? 120.68000 106.61600 100.24000 1.000 33.89956  ? 314 SER B N    1 
ATOM   4716 C CA   . SER B 1 314 ? 120.60200 106.32200 101.66600 1.000 30.64374  ? 314 SER B CA   1 
ATOM   4717 C C    . SER B 1 314 ? 121.40500 105.07300 102.01200 1.000 32.40761  ? 314 SER B C    1 
ATOM   4718 O O    . SER B 1 314 ? 122.10100 105.03800 103.03600 1.000 27.72803  ? 314 SER B O    1 
ATOM   4719 C CB   . SER B 1 314 ? 119.14300 106.16700 102.09100 1.000 31.02346  ? 314 SER B CB   1 
ATOM   4720 O OG   . SER B 1 314 ? 118.70400 104.83100 101.93100 1.000 39.34737  ? 314 SER B OG   1 
ATOM   4721 N N    . LEU B 1 315 ? 121.33200 104.03500 101.17300 1.000 28.43836  ? 315 LEU B N    1 
ATOM   4722 C CA   . LEU B 1 315 ? 122.13800 102.85000 101.43100 1.000 20.56158  ? 315 LEU B CA   1 
ATOM   4723 C C    . LEU B 1 315 ? 123.62500 103.16100 101.33900 1.000 29.05696  ? 315 LEU B C    1 
ATOM   4724 O O    . LEU B 1 315 ? 124.43100 102.55000 102.05000 1.000 36.93005  ? 315 LEU B O    1 
ATOM   4725 C CB   . LEU B 1 315 ? 121.76300 101.74100 100.44900 1.000 27.55569  ? 315 LEU B CB   1 
ATOM   4726 C CG   . LEU B 1 315 ? 120.47900 100.97100 100.76000 1.000 30.61028  ? 315 LEU B CG   1 
ATOM   4727 C CD1  . LEU B 1 315 ? 120.10800 100.05900 99.60400  1.000 27.37606  ? 315 LEU B CD1  1 
ATOM   4728 C CD2  . LEU B 1 315 ? 120.61100 100.18400 102.05200 1.000 32.30041  ? 315 LEU B CD2  1 
ATOM   4729 N N    . MET B 1 316 ? 124.00600 104.13100 100.50400 1.000 21.81710  ? 316 MET B N    1 
ATOM   4730 C CA   . MET B 1 316 ? 125.40200 104.54000 100.42400 1.000 27.56623  ? 316 MET B CA   1 
ATOM   4731 C C    . MET B 1 316 ? 125.80700 105.46700 101.56100 1.000 31.27019  ? 316 MET B C    1 
ATOM   4732 O O    . MET B 1 316 ? 126.99600 105.54500 101.88400 1.000 34.61946  ? 316 MET B O    1 
ATOM   4733 C CB   . MET B 1 316 ? 125.67900 105.22500 99.08500  1.000 29.47527  ? 316 MET B CB   1 
ATOM   4734 C CG   . MET B 1 316 ? 127.14600 105.52600 98.83900  1.000 28.40538  ? 316 MET B CG   1 
ATOM   4735 S SD   . MET B 1 316 ? 127.40000 107.09400 97.99000  1.000 50.70592  ? 316 MET B SD   1 
ATOM   4736 C CE   . MET B 1 316 ? 129.12700 106.95800 97.54400  1.000 31.91201  ? 316 MET B CE   1 
ATOM   4737 N N    . SER B 1 317 ? 124.85100 106.16400 102.17500 1.000 33.54899  ? 317 SER B N    1 
ATOM   4738 C CA   . SER B 1 317 ? 125.15500 106.95600 103.35900 1.000 15.31435  ? 317 SER B CA   1 
ATOM   4739 C C    . SER B 1 317 ? 125.14500 106.11300 104.62500 1.000 23.63568  ? 317 SER B C    1 
ATOM   4740 O O    . SER B 1 317 ? 125.61700 106.57700 105.66800 1.000 22.78067  ? 317 SER B O    1 
ATOM   4741 C CB   . SER B 1 317 ? 124.16100 108.10900 103.49800 1.000 22.68696  ? 317 SER B CB   1 
ATOM   4742 O OG   . SER B 1 317 ? 122.89300 107.64000 103.91900 1.000 25.89042  ? 317 SER B OG   1 
ATOM   4743 N N    . PHE B 1 318 ? 124.62400 104.88800 104.54800 1.000 29.06183  ? 318 PHE B N    1 
ATOM   4744 C CA   . PHE B 1 318 ? 124.67900 103.95200 105.66400 1.000 9.35055   ? 318 PHE B CA   1 
ATOM   4745 C C    . PHE B 1 318 ? 125.80500 102.93700 105.53600 1.000 14.00934  ? 318 PHE B C    1 
ATOM   4746 O O    . PHE B 1 318 ? 126.26500 102.41800 106.55700 1.000 20.16037  ? 318 PHE B O    1 
ATOM   4747 C CB   . PHE B 1 318 ? 123.35700 103.18400 105.79800 1.000 12.26920  ? 318 PHE B CB   1 
ATOM   4748 C CG   . PHE B 1 318 ? 122.20600 104.01900 106.26500 1.000 13.63142  ? 318 PHE B CG   1 
ATOM   4749 C CD1  . PHE B 1 318 ? 122.41800 105.19000 106.96600 1.000 11.12859  ? 318 PHE B CD1  1 
ATOM   4750 C CD2  . PHE B 1 318 ? 120.90500 103.62700 106.00300 1.000 12.78575  ? 318 PHE B CD2  1 
ATOM   4751 C CE1  . PHE B 1 318 ? 121.35400 105.95500 107.39600 1.000 12.54071  ? 318 PHE B CE1  1 
ATOM   4752 C CE2  . PHE B 1 318 ? 119.83900 104.38900 106.43000 1.000 6.96857   ? 318 PHE B CE2  1 
ATOM   4753 C CZ   . PHE B 1 318 ? 120.06300 105.55300 107.12700 1.000 14.67842  ? 318 PHE B CZ   1 
ATOM   4754 N N    . ALA B 1 319 ? 126.27000 102.65400 104.31800 1.000 24.49773  ? 319 ALA B N    1 
ATOM   4755 C CA   . ALA B 1 319 ? 127.31900 101.66500 104.11200 1.000 15.68228  ? 319 ALA B CA   1 
ATOM   4756 C C    . ALA B 1 319 ? 128.71700 102.19700 104.39300 1.000 18.08534  ? 319 ALA B C    1 
ATOM   4757 O O    . ALA B 1 319 ? 129.66100 101.40200 104.44800 1.000 26.41052  ? 319 ALA B O    1 
ATOM   4758 C CB   . ALA B 1 319 ? 127.25700 101.12800 102.68200 1.000 11.57205  ? 319 ALA B CB   1 
ATOM   4759 N N    . ILE B 1 320 ? 128.87900 103.51000 104.57700 1.000 15.08104  ? 320 ILE B N    1 
ATOM   4760 C CA   . ILE B 1 320 ? 130.20200 104.07600 104.83500 1.000 17.32936  ? 320 ILE B CA   1 
ATOM   4761 C C    . ILE B 1 320 ? 130.59400 104.01700 106.30100 1.000 19.22391  ? 320 ILE B C    1 
ATOM   4762 O O    . ILE B 1 320 ? 131.73200 104.36300 106.64100 1.000 24.24605  ? 320 ILE B O    1 
ATOM   4763 C CB   . ILE B 1 320 ? 130.28900 105.53500 104.35000 1.000 21.52368  ? 320 ILE B CB   1 
ATOM   4764 C CG1  . ILE B 1 320 ? 129.16100 106.37100 104.95700 1.000 23.27488  ? 320 ILE B CG1  1 
ATOM   4765 C CG2  . ILE B 1 320 ? 130.25500 105.59700 102.83100 1.000 19.19104  ? 320 ILE B CG2  1 
ATOM   4766 C CD1  . ILE B 1 320 ? 129.54500 107.81000 105.21400 1.000 24.36581  ? 320 ILE B CD1  1 
ATOM   4767 N N    . TRP B 1 321 ? 129.68800 103.59000 107.17800 1.000 20.14896  ? 321 TRP B N    1 
ATOM   4768 C CA   . TRP B 1 321 ? 129.95400 103.49800 108.60600 1.000 11.17664  ? 321 TRP B CA   1 
ATOM   4769 C C    . TRP B 1 321 ? 130.32500 102.09100 109.05600 1.000 15.57818  ? 321 TRP B C    1 
ATOM   4770 O O    . TRP B 1 321 ? 130.76900 101.92200 110.19500 1.000 23.65769  ? 321 TRP B O    1 
ATOM   4771 C CB   . TRP B 1 321 ? 128.72200 103.95400 109.39800 1.000 12.91066  ? 321 TRP B CB   1 
ATOM   4772 C CG   . TRP B 1 321 ? 128.55700 105.43300 109.52500 1.000 10.25022  ? 321 TRP B CG   1 
ATOM   4773 C CD1  . TRP B 1 321 ? 128.04500 106.28100 108.59100 1.000 11.65783  ? 321 TRP B CD1  1 
ATOM   4774 C CD2  . TRP B 1 321 ? 128.85500 106.23500 110.67300 1.000 14.60980  ? 321 TRP B CD2  1 
ATOM   4775 N NE1  . TRP B 1 321 ? 128.03000 107.56500 109.07300 1.000 13.61920  ? 321 TRP B NE1  1 
ATOM   4776 C CE2  . TRP B 1 321 ? 128.52000 107.56400 110.35200 1.000 13.17146  ? 321 TRP B CE2  1 
ATOM   4777 C CE3  . TRP B 1 321 ? 129.38500 105.96000 111.93700 1.000 17.13946  ? 321 TRP B CE3  1 
ATOM   4778 C CZ2  . TRP B 1 321 ? 128.69600 108.61500 111.24700 1.000 9.43568   ? 321 TRP B CZ2  1 
ATOM   4779 C CZ3  . TRP B 1 321 ? 129.55800 107.00500 112.82400 1.000 16.90700  ? 321 TRP B CZ3  1 
ATOM   4780 C CH2  . TRP B 1 321 ? 129.21500 108.31600 112.47500 1.000 9.95167   ? 321 TRP B CH2  1 
ATOM   4781 N N    . GLU B 1 322 ? 130.16100 101.08700 108.19600 1.000 15.40942  ? 322 GLU B N    1 
ATOM   4782 C CA   . GLU B 1 322 ? 130.33000 99.66900  108.49200 1.000 17.51567  ? 322 GLU B CA   1 
ATOM   4783 C C    . GLU B 1 322 ? 131.78600 99.23800  108.32400 1.000 22.33167  ? 322 GLU B C    1 
ATOM   4784 O O    . GLU B 1 322 ? 132.47400 99.70900  107.41400 1.000 26.02868  ? 322 GLU B O    1 
ATOM   4785 C CB   . GLU B 1 322 ? 129.43500 98.83300  107.58800 1.000 19.02602  ? 322 GLU B CB   1 
ATOM   4786 C CG   . GLU B 1 322 ? 127.95600 99.11200  107.79400 1.000 19.46157  ? 322 GLU B CG   1 
ATOM   4787 C CD   . GLU B 1 322 ? 127.07400 98.38700  106.80600 1.000 15.92494  ? 322 GLU B CD   1 
ATOM   4788 O OE1  . GLU B 1 322 ? 127.60500 97.85300  105.81300 1.000 27.05521  ? 322 GLU B OE1  1 
ATOM   4789 O OE2  . GLU B 1 322 ? 125.84700 98.34600  107.02600 1.000 7.20705   ? 322 GLU B OE2  1 
ATOM   4790 N N    . PRO B 1 323 ? 132.26100 98.35400  109.19800 1.000 30.80257  ? 323 PRO B N    1 
ATOM   4791 C CA   . PRO B 1 323 ? 133.65000 97.88600  109.12100 1.000 33.42283  ? 323 PRO B CA   1 
ATOM   4792 C C    . PRO B 1 323 ? 133.84700 96.88300  107.99800 1.000 34.91471  ? 323 PRO B C    1 
ATOM   4793 O O    . PRO B 1 323 ? 132.87600 96.30700  107.48400 1.000 33.98468  ? 323 PRO B O    1 
ATOM   4794 C CB   . PRO B 1 323 ? 133.87100 97.23500  110.49300 1.000 28.96806  ? 323 PRO B CB   1 
ATOM   4795 C CG   . PRO B 1 323 ? 132.50800 96.78200  110.89600 1.000 29.72599  ? 323 PRO B CG   1 
ATOM   4796 C CD   . PRO B 1 323 ? 131.58200 97.85900  110.40800 1.000 24.03854  ? 323 PRO B CD   1 
ATOM   4797 N N    . PRO B 1 324 ? 135.09500 96.65100  107.58900 1.000 38.07379  ? 324 PRO B N    1 
ATOM   4798 C CA   . PRO B 1 324 ? 135.36900 95.66000  106.54000 1.000 38.01272  ? 324 PRO B CA   1 
ATOM   4799 C C    . PRO B 1 324 ? 134.85300 94.27800  106.91400 1.000 40.67152  ? 324 PRO B C    1 
ATOM   4800 O O    . PRO B 1 324 ? 134.94800 93.85100  108.06600 1.000 45.17900  ? 324 PRO B O    1 
ATOM   4801 C CB   . PRO B 1 324 ? 136.89700 95.67500  106.43600 1.000 35.62461  ? 324 PRO B CB   1 
ATOM   4802 C CG   . PRO B 1 324 ? 137.28100 97.03700  106.89400 1.000 42.00988  ? 324 PRO B CG   1 
ATOM   4803 C CD   . PRO B 1 324 ? 136.31300 97.37200  107.99400 1.000 37.40448  ? 324 PRO B CD   1 
ATOM   4804 N N    . HIS B 1 325 ? 134.30200 93.57500  105.92800 1.000 32.76699  ? 325 HIS B N    1 
ATOM   4805 C CA   . HIS B 1 325 ? 133.73500 92.25700  106.18200 1.000 31.42319  ? 325 HIS B CA   1 
ATOM   4806 C C    . HIS B 1 325 ? 133.49600 91.54000  104.86200 1.000 35.44702  ? 325 HIS B C    1 
ATOM   4807 O O    . HIS B 1 325 ? 133.38400 92.16400  103.80300 1.000 39.99142  ? 325 HIS B O    1 
ATOM   4808 C CB   . HIS B 1 325 ? 132.42600 92.35900  106.96900 1.000 29.46274  ? 325 HIS B CB   1 
ATOM   4809 C CG   . HIS B 1 325 ? 131.26300 92.80400  106.13900 1.000 29.33852  ? 325 HIS B CG   1 
ATOM   4810 N ND1  . HIS B 1 325 ? 130.94100 94.13100  105.96100 1.000 29.36110  ? 325 HIS B ND1  1 
ATOM   4811 C CD2  . HIS B 1 325 ? 130.35000 92.09800  105.43100 1.000 28.55770  ? 325 HIS B CD2  1 
ATOM   4812 C CE1  . HIS B 1 325 ? 129.87800 94.22400  105.18200 1.000 28.90161  ? 325 HIS B CE1  1 
ATOM   4813 N NE2  . HIS B 1 325 ? 129.50100 93.00400  104.84600 1.000 27.80678  ? 325 HIS B NE2  1 
ATOM   4814 N N    . GLY B 1 326 ? 133.42300 90.21300  104.94700 1.000 39.01792  ? 326 GLY B N    1 
ATOM   4815 C CA   . GLY B 1 326 ? 133.10500 89.36200  103.82400 1.000 38.57344  ? 326 GLY B CA   1 
ATOM   4816 C C    . GLY B 1 326 ? 134.01000 89.52200  102.61900 1.000 41.42222  ? 326 GLY B C    1 
ATOM   4817 O O    . GLY B 1 326 ? 135.23800 89.43000  102.71200 1.000 40.79026  ? 326 GLY B O    1 
ATOM   4818 N N    . PRO B 1 327 ? 133.40500 89.76000  101.45200 1.000 45.88687  ? 327 PRO B N    1 
ATOM   4819 C CA   . PRO B 1 327 ? 134.19000 89.93700  100.22400 1.000 39.67089  ? 327 PRO B CA   1 
ATOM   4820 C C    . PRO B 1 327 ? 134.68200 91.36200  100.03000 1.000 37.58271  ? 327 PRO B C    1 
ATOM   4821 O O    . PRO B 1 327 ? 135.60400 91.60500  99.24600  1.000 40.43283  ? 327 PRO B O    1 
ATOM   4822 C CB   . PRO B 1 327 ? 133.20200 89.53100  99.12700  1.000 37.54668  ? 327 PRO B CB   1 
ATOM   4823 C CG   . PRO B 1 327 ? 131.88100 89.91500  99.68300  1.000 35.59996  ? 327 PRO B CG   1 
ATOM   4824 C CD   . PRO B 1 327 ? 131.96100 89.67200  101.17100 1.000 39.82580  ? 327 PRO B CD   1 
ATOM   4825 N N    . TYR B 1 328 ? 134.07100 92.31300  100.73500 1.000 38.12613  ? 328 TYR B N    1 
ATOM   4826 C CA   . TYR B 1 328 ? 134.41500 93.72600  100.60300 1.000 40.69142  ? 328 TYR B CA   1 
ATOM   4827 C C    . TYR B 1 328 ? 135.36600 94.08200  101.74000 1.000 43.18419  ? 328 TYR B C    1 
ATOM   4828 O O    . TYR B 1 328 ? 134.98200 94.66100  102.75600 1.000 46.71400  ? 328 TYR B O    1 
ATOM   4829 C CB   . TYR B 1 328 ? 133.16200 94.59600  100.63100 1.000 35.62781  ? 328 TYR B CB   1 
ATOM   4830 C CG   . TYR B 1 328 ? 131.91300 93.92600  100.11200 1.000 35.11255  ? 328 TYR B CG   1 
ATOM   4831 C CD1  . TYR B 1 328 ? 131.64000 93.87200  98.75300  1.000 39.21012  ? 328 TYR B CD1  1 
ATOM   4832 C CD2  . TYR B 1 328 ? 130.99900 93.35400  100.98500 1.000 36.31688  ? 328 TYR B CD2  1 
ATOM   4833 C CE1  . TYR B 1 328 ? 130.49400 93.26300  98.27900  1.000 39.32426  ? 328 TYR B CE1  1 
ATOM   4834 C CE2  . TYR B 1 328 ? 129.85300 92.74300  100.52100 1.000 38.09951  ? 328 TYR B CE2  1 
ATOM   4835 C CZ   . TYR B 1 328 ? 129.60400 92.70000  99.16800  1.000 39.17213  ? 328 TYR B CZ   1 
ATOM   4836 O OH   . TYR B 1 328 ? 128.46300 92.09100  98.70500  1.000 38.00682  ? 328 TYR B OH   1 
ATOM   4837 N N    . LYS B 1 329 ? 136.63300 93.72900  101.55600 1.000 48.96336  ? 329 LYS B N    1 
ATOM   4838 C CA   . LYS B 1 329 ? 137.65900 93.91500  102.57900 1.000 52.07426  ? 329 LYS B CA   1 
ATOM   4839 C C    . LYS B 1 329 ? 138.65000 94.97000  102.09000 1.000 52.54513  ? 329 LYS B C    1 
ATOM   4840 O O    . LYS B 1 329 ? 139.60700 94.66800  101.37600 1.000 53.74720  ? 329 LYS B O    1 
ATOM   4841 C CB   . LYS B 1 329 ? 138.35400 92.59100  102.89200 1.000 52.36513  ? 329 LYS B CB   1 
ATOM   4842 C CG   . LYS B 1 329 ? 138.97100 91.91000  101.68100 1.000 53.90994  ? 329 LYS B CG   1 
ATOM   4843 C CD   . LYS B 1 329 ? 138.96400 90.39800  101.83500 1.000 54.01530  ? 329 LYS B CD   1 
ATOM   4844 C CE   . LYS B 1 329 ? 138.94200 89.70700  100.48300 1.000 52.62981  ? 329 LYS B CE   1 
ATOM   4845 N NZ   . LYS B 1 329 ? 138.13800 88.45500  100.51200 1.000 52.11521  ? 329 LYS B NZ   1 
ATOM   4846 N N    . SER B 1 330 ? 138.40300 96.21600  102.48200 1.000 60.15011  ? 330 SER B N    1 
ATOM   4847 C CA   . SER B 1 330 ? 139.28300 97.34000  102.19800 1.000 59.47781  ? 330 SER B CA   1 
ATOM   4848 C C    . SER B 1 330 ? 138.82800 98.51600  103.04700 1.000 61.26983  ? 330 SER B C    1 
ATOM   4849 O O    . SER B 1 330 ? 137.64100 98.64200  103.36100 1.000 60.35286  ? 330 SER B O    1 
ATOM   4850 C CB   . SER B 1 330 ? 139.27700 97.71200  100.71100 1.000 60.14995  ? 330 SER B CB   1 
ATOM   4851 O OG   . SER B 1 330 ? 139.69300 96.62000  99.91000  1.000 59.96699  ? 330 SER B OG   1 
ATOM   4852 N N    . PHE B 1 331 ? 139.78000 99.37300  103.41600 1.000 71.59921  ? 331 PHE B N    1 
ATOM   4853 C CA   . PHE B 1 331 ? 139.45600 100.47300 104.31600 1.000 72.31226  ? 331 PHE B CA   1 
ATOM   4854 C C    . PHE B 1 331 ? 138.49000 101.45900 103.67000 1.000 72.47817  ? 331 PHE B C    1 
ATOM   4855 O O    . PHE B 1 331 ? 137.52200 101.89400 104.30500 1.000 72.33602  ? 331 PHE B O    1 
ATOM   4856 C CB   . PHE B 1 331 ? 140.73600 101.17900 104.76000 1.000 71.44718  ? 331 PHE B CB   1 
ATOM   4857 C CG   . PHE B 1 331 ? 141.49900 100.43400 105.81600 1.000 75.13202  ? 331 PHE B CG   1 
ATOM   4858 C CD1  . PHE B 1 331 ? 140.84800 99.55800  106.66900 1.000 74.52603  ? 331 PHE B CD1  1 
ATOM   4859 C CD2  . PHE B 1 331 ? 142.86600 100.60400 105.95400 1.000 73.87047  ? 331 PHE B CD2  1 
ATOM   4860 C CE1  . PHE B 1 331 ? 141.54500 98.86800  107.64200 1.000 73.56187  ? 331 PHE B CE1  1 
ATOM   4861 C CE2  . PHE B 1 331 ? 143.56900 99.91600  106.92500 1.000 74.59770  ? 331 PHE B CE2  1 
ATOM   4862 C CZ   . PHE B 1 331 ? 142.90800 99.04700  107.77000 1.000 74.60536  ? 331 PHE B CZ   1 
ATOM   4863 N N    . ASN B 1 332 ? 138.73200 101.82400 102.41300 1.000 64.86812  ? 332 ASN B N    1 
ATOM   4864 C CA   . ASN B 1 332 ? 137.85300 102.71600 101.65800 1.000 63.06090  ? 332 ASN B CA   1 
ATOM   4865 C C    . ASN B 1 332 ? 137.26900 101.94800 100.47600 1.000 62.15043  ? 332 ASN B C    1 
ATOM   4866 O O    . ASN B 1 332 ? 137.95100 101.74000 99.46800  1.000 62.69879  ? 332 ASN B O    1 
ATOM   4867 C CB   . ASN B 1 332 ? 138.60800 103.95700 101.19400 1.000 62.81376  ? 332 ASN B CB   1 
ATOM   4868 C CG   . ASN B 1 332 ? 138.94400 104.89400 102.33600 1.000 67.51154  ? 332 ASN B CG   1 
ATOM   4869 O OD1  . ASN B 1 332 ? 139.89200 104.66100 103.08600 1.000 67.20388  ? 332 ASN B OD1  1 
ATOM   4870 N ND2  . ASN B 1 332 ? 138.16600 105.96100 102.47500 1.000 66.45744  ? 332 ASN B ND2  1 
ATOM   4871 N N    . TYR B 1 333 ? 136.01300 101.52600 100.59400 1.000 42.37889  ? 333 TYR B N    1 
ATOM   4872 C CA   . TYR B 1 333 ? 135.43100 100.77200 99.48900  1.000 42.91808  ? 333 TYR B CA   1 
ATOM   4873 C C    . TYR B 1 333 ? 134.81300 101.72100 98.47000  1.000 43.98630  ? 333 TYR B C    1 
ATOM   4874 O O    . TYR B 1 333 ? 134.08300 102.64100 98.85400  1.000 43.40420  ? 333 TYR B O    1 
ATOM   4875 C CB   . TYR B 1 333 ? 134.38000 99.78900  99.98000  1.000 40.48175  ? 333 TYR B CB   1 
ATOM   4876 C CG   . TYR B 1 333 ? 134.24300 98.58800  99.07500  1.000 39.42168  ? 333 TYR B CG   1 
ATOM   4877 C CD1  . TYR B 1 333 ? 135.25100 97.63800  98.99500  1.000 38.63922  ? 333 TYR B CD1  1 
ATOM   4878 C CD2  . TYR B 1 333 ? 133.11500 98.41400  98.28600  1.000 33.16952  ? 333 TYR B CD2  1 
ATOM   4879 C CE1  . TYR B 1 333 ? 135.13600 96.54500  98.16200  1.000 40.36075  ? 333 TYR B CE1  1 
ATOM   4880 C CE2  . TYR B 1 333 ? 132.99000 97.32500  97.45000  1.000 37.99240  ? 333 TYR B CE2  1 
ATOM   4881 C CZ   . TYR B 1 333 ? 134.00300 96.39200  97.39200  1.000 40.82306  ? 333 TYR B CZ   1 
ATOM   4882 O OH   . TYR B 1 333 ? 133.88300 95.30300  96.56200  1.000 37.64441  ? 333 TYR B OH   1 
ATOM   4883 N N    . PRO B 1 334 ? 135.07900 101.53000 97.17800  1.000 36.26362  ? 334 PRO B N    1 
ATOM   4884 C CA   . PRO B 1 334 ? 134.47700 102.39700 96.15600  1.000 31.26013  ? 334 PRO B CA   1 
ATOM   4885 C C    . PRO B 1 334 ? 132.97800 102.19400 96.00600  1.000 36.34921  ? 334 PRO B C    1 
ATOM   4886 O O    . PRO B 1 334 ? 132.52500 101.58300 95.03400  1.000 45.19543  ? 334 PRO B O    1 
ATOM   4887 C CB   . PRO B 1 334 ? 135.22500 101.99300 94.88000  1.000 36.32214  ? 334 PRO B CB   1 
ATOM   4888 C CG   . PRO B 1 334 ? 135.65100 100.58800 95.13900  1.000 33.32681  ? 334 PRO B CG   1 
ATOM   4889 C CD   . PRO B 1 334 ? 136.01700 100.56000 96.58900  1.000 32.07579  ? 334 PRO B CD   1 
ATOM   4890 N N    . TRP B 1 335 ? 132.19700 102.69800 96.96200  1.000 34.52734  ? 335 TRP B N    1 
ATOM   4891 C CA   . TRP B 1 335 ? 130.74600 102.57600 96.89500  1.000 31.98903  ? 335 TRP B CA   1 
ATOM   4892 C C    . TRP B 1 335 ? 130.11400 103.53300 95.89100  1.000 37.05172  ? 335 TRP B C    1 
ATOM   4893 O O    . TRP B 1 335 ? 129.01900 103.25200 95.39500  1.000 39.94330  ? 335 TRP B O    1 
ATOM   4894 C CB   . TRP B 1 335 ? 130.13100 102.81800 98.27500  1.000 32.47034  ? 335 TRP B CB   1 
ATOM   4895 C CG   . TRP B 1 335 ? 130.37600 101.71600 99.26400  1.000 36.32273  ? 335 TRP B CG   1 
ATOM   4896 C CD1  . TRP B 1 335 ? 131.01000 101.82200 100.46500 1.000 35.35329  ? 335 TRP B CD1  1 
ATOM   4897 C CD2  . TRP B 1 335 ? 129.98200 100.34400 99.13800  1.000 36.18632  ? 335 TRP B CD2  1 
ATOM   4898 N NE1  . TRP B 1 335 ? 131.04000 100.60200 101.09500 1.000 37.83575  ? 335 TRP B NE1  1 
ATOM   4899 C CE2  . TRP B 1 335 ? 130.41600 99.67800  100.30100 1.000 32.25711  ? 335 TRP B CE2  1 
ATOM   4900 C CE3  . TRP B 1 335 ? 129.30800 99.61400  98.15500  1.000 36.03822  ? 335 TRP B CE3  1 
ATOM   4901 C CZ2  . TRP B 1 335 ? 130.19900 98.31800  100.50700 1.000 32.40012  ? 335 TRP B CZ2  1 
ATOM   4902 C CZ3  . TRP B 1 335 ? 129.09300 98.26300  98.36200  1.000 36.32376  ? 335 TRP B CZ3  1 
ATOM   4903 C CH2  . TRP B 1 335 ? 129.53800 97.63000  99.52800  1.000 33.91018  ? 335 TRP B CH2  1 
ATOM   4904 N N    . LYS B 1 336 ? 130.77400 104.65200 95.58300  1.000 39.77325  ? 336 LYS B N    1 
ATOM   4905 C CA   . LYS B 1 336 ? 130.21100 105.62800 94.65400  1.000 39.09288  ? 336 LYS B CA   1 
ATOM   4906 C C    . LYS B 1 336 ? 130.16100 105.11600 93.21700  1.000 41.95876  ? 336 LYS B C    1 
ATOM   4907 O O    . LYS B 1 336 ? 129.30200 105.55200 92.43700  1.000 44.50493  ? 336 LYS B O    1 
ATOM   4908 C CB   . LYS B 1 336 ? 131.01400 106.92600 94.72300  1.000 41.13721  ? 336 LYS B CB   1 
ATOM   4909 C CG   . LYS B 1 336 ? 132.39900 106.83000 94.10800  1.000 42.66011  ? 336 LYS B CG   1 
ATOM   4910 C CD   . LYS B 1 336 ? 133.27000 108.00800 94.51100  1.000 41.43901  ? 336 LYS B CD   1 
ATOM   4911 C CE   . LYS B 1 336 ? 134.66200 107.55400 94.92200  1.000 45.75466  ? 336 LYS B CE   1 
ATOM   4912 N NZ   . LYS B 1 336 ? 134.62600 106.51400 95.98500  1.000 49.71230  ? 336 LYS B NZ   1 
ATOM   4913 N N    . ASN B 1 337 ? 131.05400 104.19700 92.84300  1.000 34.95404  ? 337 ASN B N    1 
ATOM   4914 C CA   . ASN B 1 337 ? 131.01500 103.66300 91.48600  1.000 36.15915  ? 337 ASN B CA   1 
ATOM   4915 C C    . ASN B 1 337 ? 129.76600 102.83100 91.22200  1.000 41.25550  ? 337 ASN B C    1 
ATOM   4916 O O    . ASN B 1 337 ? 129.32500 102.74500 90.06800  1.000 47.34305  ? 337 ASN B O    1 
ATOM   4917 C CB   . ASN B 1 337 ? 132.26700 102.82800 91.22400  1.000 39.79601  ? 337 ASN B CB   1 
ATOM   4918 C CG   . ASN B 1 337 ? 133.46700 103.67800 90.85800  1.000 47.74844  ? 337 ASN B CG   1 
ATOM   4919 O OD1  . ASN B 1 337 ? 133.66200 104.03100 89.69600  1.000 50.09666  ? 337 ASN B OD1  1 
ATOM   4920 N ND2  . ASN B 1 337 ? 134.27700 104.01500 91.85200  1.000 45.15108  ? 337 ASN B ND2  1 
ATOM   4921 N N    . TYR B 1 338 ? 129.12500 102.31100 92.27000  1.000 32.67573  ? 338 TYR B N    1 
ATOM   4922 C CA   . TYR B 1 338 ? 127.86200 101.61100 92.07200  1.000 33.20946  ? 338 TYR B CA   1 
ATOM   4923 C C    . TYR B 1 338 ? 126.75500 102.59700 91.72500  1.000 35.43456  ? 338 TYR B C    1 
ATOM   4924 O O    . TYR B 1 338 ? 125.90900 102.32200 90.86400  1.000 40.74898  ? 338 TYR B O    1 
ATOM   4925 C CB   . TYR B 1 338 ? 127.49900 100.82400 93.33100  1.000 30.40461  ? 338 TYR B CB   1 
ATOM   4926 C CG   . TYR B 1 338 ? 128.33400 99.58500  93.56700  1.000 33.08136  ? 338 TYR B CG   1 
ATOM   4927 C CD1  . TYR B 1 338 ? 129.60400 99.67700  94.12000  1.000 33.29063  ? 338 TYR B CD1  1 
ATOM   4928 C CD2  . TYR B 1 338 ? 127.85000 98.32400  93.24900  1.000 27.95275  ? 338 TYR B CD2  1 
ATOM   4929 C CE1  . TYR B 1 338 ? 130.37000 98.55000  94.34300  1.000 28.89243  ? 338 TYR B CE1  1 
ATOM   4930 C CE2  . TYR B 1 338 ? 128.60900 97.19200  93.46800  1.000 28.94984  ? 338 TYR B CE2  1 
ATOM   4931 C CZ   . TYR B 1 338 ? 129.86800 97.31100  94.01500  1.000 34.01215  ? 338 TYR B CZ   1 
ATOM   4932 O OH   . TYR B 1 338 ? 130.62700 96.18600  94.23600  1.000 36.78567  ? 338 TYR B OH   1 
ATOM   4933 N N    . VAL B 1 339 ? 126.78300 103.77700 92.34600  1.000 29.44629  ? 339 VAL B N    1 
ATOM   4934 C CA   . VAL B 1 339 ? 125.81500 104.81700 92.02000  1.000 33.22721  ? 339 VAL B CA   1 
ATOM   4935 C C    . VAL B 1 339 ? 126.06400 105.35100 90.61600  1.000 29.61188  ? 339 VAL B C    1 
ATOM   4936 O O    . VAL B 1 339 ? 125.12100 105.65300 89.87400  1.000 34.43556  ? 339 VAL B O    1 
ATOM   4937 C CB   . VAL B 1 339 ? 125.86700 105.93700 93.07400  1.000 37.08021  ? 339 VAL B CB   1 
ATOM   4938 C CG1  . VAL B 1 339 ? 124.79900 106.98000 92.79400  1.000 33.50998  ? 339 VAL B CG1  1 
ATOM   4939 C CG2  . VAL B 1 339 ? 125.70700 105.36000 94.47000  1.000 31.45171  ? 339 VAL B CG2  1 
ATOM   4940 N N    . LYS B 1 340 ? 127.33400 105.47900 90.22700  1.000 28.03986  ? 340 LYS B N    1 
ATOM   4941 C CA   . LYS B 1 340 ? 127.64100 105.92500 88.87100  1.000 32.42891  ? 340 LYS B CA   1 
ATOM   4942 C C    . LYS B 1 340 ? 127.12300 104.93600 87.82900  1.000 35.72389  ? 340 LYS B C    1 
ATOM   4943 O O    . LYS B 1 340 ? 126.52900 105.33600 86.81500  1.000 40.67142  ? 340 LYS B O    1 
ATOM   4944 C CB   . LYS B 1 340 ? 129.15000 106.12200 88.72700  1.000 30.02969  ? 340 LYS B CB   1 
ATOM   4945 C CG   . LYS B 1 340 ? 129.56000 107.12900 87.67300  1.000 35.45886  ? 340 LYS B CG   1 
ATOM   4946 C CD   . LYS B 1 340 ? 131.04700 107.03500 87.38100  1.000 40.76282  ? 340 LYS B CD   1 
ATOM   4947 C CE   . LYS B 1 340 ? 131.32400 107.11000 85.89000  1.000 40.15102  ? 340 LYS B CE   1 
ATOM   4948 N NZ   . LYS B 1 340 ? 132.49600 107.97500 85.58600  1.000 39.83957  ? 340 LYS B NZ   1 
ATOM   4949 N N    . LEU B 1 341 ? 127.30400 103.63700 88.07800  1.000 27.51826  ? 341 LEU B N    1 
ATOM   4950 C CA   . LEU B 1 341 ? 126.76900 102.63300 87.16200  1.000 25.00063  ? 341 LEU B CA   1 
ATOM   4951 C C    . LEU B 1 341 ? 125.24200 102.67400 87.11900  1.000 28.25426  ? 341 LEU B C    1 
ATOM   4952 O O    . LEU B 1 341 ? 124.63700 102.55600 86.04300  1.000 35.15333  ? 341 LEU B O    1 
ATOM   4953 C CB   . LEU B 1 341 ? 127.27100 101.24700 87.56900  1.000 30.18584  ? 341 LEU B CB   1 
ATOM   4954 C CG   . LEU B 1 341 ? 126.96000 100.06800 86.64800  1.000 32.33252  ? 341 LEU B CG   1 
ATOM   4955 C CD1  . LEU B 1 341 ? 127.57200 100.29100 85.27700  1.000 27.27034  ? 341 LEU B CD1  1 
ATOM   4956 C CD2  . LEU B 1 341 ? 127.46700 98.77300  87.25600  1.000 23.77689  ? 341 LEU B CD2  1 
ATOM   4957 N N    . SER B 1 342 ? 124.60000 102.84500 88.27800  1.000 24.52555  ? 342 SER B N    1 
ATOM   4958 C CA   . SER B 1 342 ? 123.14200 102.93300 88.30500  1.000 23.36312  ? 342 SER B CA   1 
ATOM   4959 C C    . SER B 1 342 ? 122.63100 104.14200 87.52500  1.000 28.05725  ? 342 SER B C    1 
ATOM   4960 O O    . SER B 1 342 ? 121.60600 104.05700 86.83600  1.000 31.45407  ? 342 SER B O    1 
ATOM   4961 C CB   . SER B 1 342 ? 122.65200 102.98500 89.75000  1.000 25.21811  ? 342 SER B CB   1 
ATOM   4962 O OG   . SER B 1 342 ? 122.68900 101.70100 90.34200  1.000 29.40036  ? 342 SER B OG   1 
ATOM   4963 N N    . GLY B 1 343 ? 123.32900 105.27500 87.61300  1.000 27.90965  ? 343 GLY B N    1 
ATOM   4964 C CA   . GLY B 1 343 ? 122.91800 106.43700 86.84100  1.000 21.48117  ? 343 GLY B CA   1 
ATOM   4965 C C    . GLY B 1 343 ? 123.09200 106.22400 85.35000  1.000 27.32320  ? 343 GLY B C    1 
ATOM   4966 O O    . GLY B 1 343 ? 122.23900 106.62700 84.54400  1.000 35.34716  ? 343 GLY B O    1 
ATOM   4967 N N    . ALA B 1 344 ? 124.17900 105.55300 84.96400  1.000 26.27224  ? 344 ALA B N    1 
ATOM   4968 C CA   . ALA B 1 344 ? 124.37700 105.25400 83.55200  1.000 23.82258  ? 344 ALA B CA   1 
ATOM   4969 C C    . ALA B 1 344 ? 123.27100 104.34600 83.03000  1.000 28.72617  ? 344 ALA B C    1 
ATOM   4970 O O    . ALA B 1 344 ? 122.84400 104.47500 81.87700  1.000 27.38590  ? 344 ALA B O    1 
ATOM   4971 C CB   . ALA B 1 344 ? 125.74900 104.61700 83.33500  1.000 22.21232  ? 344 ALA B CB   1 
ATOM   4972 N N    . LEU B 1 345 ? 122.79200 103.41800 83.86400  1.000 24.95428  ? 345 LEU B N    1 
ATOM   4973 C CA   . LEU B 1 345 ? 121.69300 102.55200 83.43800  1.000 27.60536  ? 345 LEU B CA   1 
ATOM   4974 C C    . LEU B 1 345 ? 120.34600 103.27500 83.40900  1.000 30.06037  ? 345 LEU B C    1 
ATOM   4975 O O    . LEU B 1 345 ? 119.50400 102.98400 82.54800  1.000 32.97786  ? 345 LEU B O    1 
ATOM   4976 C CB   . LEU B 1 345 ? 121.60900 101.33100 84.35300  1.000 31.93769  ? 345 LEU B CB   1 
ATOM   4977 C CG   . LEU B 1 345 ? 120.62600 100.23400 83.93800  1.000 32.10304  ? 345 LEU B CG   1 
ATOM   4978 C CD1  . LEU B 1 345 ? 121.11000 99.51400  82.69100  1.000 30.24268  ? 345 LEU B CD1  1 
ATOM   4979 C CD2  . LEU B 1 345 ? 120.40500 99.25800  85.07600  1.000 29.66702  ? 345 LEU B CD2  1 
ATOM   4980 N N    . LYS B 1 346 ? 120.11800 104.22300 84.32100  1.000 30.94726  ? 346 LYS B N    1 
ATOM   4981 C CA   . LYS B 1 346 ? 118.85000 104.95200 84.29900  1.000 30.10042  ? 346 LYS B CA   1 
ATOM   4982 C C    . LYS B 1 346 ? 118.75300 105.88000 83.09200  1.000 33.33851  ? 346 LYS B C    1 
ATOM   4983 O O    . LYS B 1 346 ? 117.65400 106.09700 82.54800  1.000 31.73284  ? 346 LYS B O    1 
ATOM   4984 C CB   . LYS B 1 346 ? 118.67700 105.73300 85.60100  1.000 30.41588  ? 346 LYS B CB   1 
ATOM   4985 C CG   . LYS B 1 346 ? 117.79700 106.96100 85.48800  1.000 37.25134  ? 346 LYS B CG   1 
ATOM   4986 C CD   . LYS B 1 346 ? 117.68100 107.66800 86.82600  1.000 38.90153  ? 346 LYS B CD   1 
ATOM   4987 C CE   . LYS B 1 346 ? 117.91600 109.16000 86.69100  1.000 40.56476  ? 346 LYS B CE   1 
ATOM   4988 N NZ   . LYS B 1 346 ? 116.93700 109.94300 87.49600  1.000 42.74805  ? 346 LYS B NZ   1 
ATOM   4989 N N    . HIS B 1 347 ? 119.89400 106.39400 82.62900  1.000 37.50803  ? 347 HIS B N    1 
ATOM   4990 C CA   . HIS B 1 347 ? 119.87200 107.20800 81.41900  1.000 29.23667  ? 347 HIS B CA   1 
ATOM   4991 C C    . HIS B 1 347 ? 119.37800 106.39100 80.22900  1.000 33.31413  ? 347 HIS B C    1 
ATOM   4992 O O    . HIS B 1 347 ? 118.64000 106.90100 79.37800  1.000 34.21044  ? 347 HIS B O    1 
ATOM   4993 C CB   . HIS B 1 347 ? 121.26100 107.78700 81.14900  1.000 28.02625  ? 347 HIS B CB   1 
ATOM   4994 C CG   . HIS B 1 347 ? 121.27800 108.86100 80.10700  1.000 36.66297  ? 347 HIS B CG   1 
ATOM   4995 N ND1  . HIS B 1 347 ? 121.88400 108.70000 78.88000  1.000 38.61001  ? 347 HIS B ND1  1 
ATOM   4996 C CD2  . HIS B 1 347 ? 120.76300 110.11300 80.10900  1.000 37.12407  ? 347 HIS B CD2  1 
ATOM   4997 C CE1  . HIS B 1 347 ? 121.74200 109.80500 78.17100  1.000 35.44419  ? 347 HIS B CE1  1 
ATOM   4998 N NE2  . HIS B 1 347 ? 121.06500 110.67900 78.89400  1.000 35.28472  ? 347 HIS B NE2  1 
ATOM   4999 N N    . CYS B 1 348 ? 119.78200 105.12000 80.14900  1.000 38.04234  ? 348 CYS B N    1 
ATOM   5000 C CA   . CYS B 1 348 ? 119.23600 104.21600 79.14000  1.000 36.68955  ? 348 CYS B CA   1 
ATOM   5001 C C    . CYS B 1 348 ? 117.76000 103.91300 79.37900  1.000 36.39382  ? 348 CYS B C    1 
ATOM   5002 O O    . CYS B 1 348 ? 116.97600 103.83300 78.42600  1.000 33.38543  ? 348 CYS B O    1 
ATOM   5003 C CB   . CYS B 1 348 ? 120.04300 102.91700 79.11200  1.000 34.89828  ? 348 CYS B CB   1 
ATOM   5004 S SG   . CYS B 1 348 ? 121.48600 102.94600 78.03300  1.000 56.72816  ? 348 CYS B SG   1 
ATOM   5005 N N    . ALA B 1 349 ? 117.36200 103.72800 80.64100  1.000 38.83268  ? 349 ALA B N    1 
ATOM   5006 C CA   . ALA B 1 349 ? 115.97400 103.36800 80.93800  1.000 37.67351  ? 349 ALA B CA   1 
ATOM   5007 C C    . ALA B 1 349 ? 114.97700 104.46300 80.56300  1.000 38.18046  ? 349 ALA B C    1 
ATOM   5008 O O    . ALA B 1 349 ? 113.78800 104.17000 80.36300  1.000 40.97856  ? 349 ALA B O    1 
ATOM   5009 C CB   . ALA B 1 349 ? 115.82900 103.02300 82.42000  1.000 33.45584  ? 349 ALA B CB   1 
ATOM   5010 N N    . PHE B 1 350 ? 115.42400 105.71600 80.46900  1.000 33.84598  ? 350 PHE B N    1 
ATOM   5011 C CA   . PHE B 1 350 ? 114.52000 106.75800 79.97200  1.000 31.79992  ? 350 PHE B CA   1 
ATOM   5012 C C    . PHE B 1 350 ? 113.99300 106.44200 78.56800  1.000 31.52321  ? 350 PHE B C    1 
ATOM   5013 O O    . PHE B 1 350 ? 112.80100 106.63400 78.28500  1.000 33.29210  ? 350 PHE B O    1 
ATOM   5014 C CB   . PHE B 1 350 ? 115.21200 108.12100 79.97900  1.000 36.04820  ? 350 PHE B CB   1 
ATOM   5015 C CG   . PHE B 1 350 ? 115.41900 108.69300 81.35000  1.000 36.94889  ? 350 PHE B CG   1 
ATOM   5016 C CD1  . PHE B 1 350 ? 114.38100 108.72100 82.26400  1.000 38.82329  ? 350 PHE B CD1  1 
ATOM   5017 C CD2  . PHE B 1 350 ? 116.64400 109.21900 81.72000  1.000 39.11660  ? 350 PHE B CD2  1 
ATOM   5018 C CE1  . PHE B 1 350 ? 114.56400 109.25100 83.52600  1.000 40.12403  ? 350 PHE B CE1  1 
ATOM   5019 C CE2  . PHE B 1 350 ? 116.83200 109.75100 82.98000  1.000 41.11326  ? 350 PHE B CE2  1 
ATOM   5020 C CZ   . PHE B 1 350 ? 115.79000 109.76700 83.88300  1.000 39.32533  ? 350 PHE B CZ   1 
ATOM   5021 N N    . THR B 1 351 ? 114.86600 105.98800 77.66500  1.000 31.48478  ? 351 THR B N    1 
ATOM   5022 C CA   . THR B 1 351 ? 114.41700 105.60100 76.32800  1.000 36.51896  ? 351 THR B CA   1 
ATOM   5023 C C    . THR B 1 351 ? 113.35000 104.51100 76.38000  1.000 31.81060  ? 351 THR B C    1 
ATOM   5024 O O    . THR B 1 351 ? 112.41100 104.51200 75.57600  1.000 32.25235  ? 351 THR B O    1 
ATOM   5025 C CB   . THR B 1 351 ? 115.60500 105.14600 75.48100  1.000 41.07131  ? 351 THR B CB   1 
ATOM   5026 O OG1  . THR B 1 351 ? 116.64700 106.12500 75.55200  1.000 41.01939  ? 351 THR B OG1  1 
ATOM   5027 C CG2  . THR B 1 351 ? 115.18300 104.97300 74.03200  1.000 34.24649  ? 351 THR B CG2  1 
ATOM   5028 N N    . VAL B 1 352 ? 113.48300 103.56300 77.30800  1.000 35.32937  ? 352 VAL B N    1 
ATOM   5029 C CA   . VAL B 1 352 ? 112.49100 102.49800 77.41500  1.000 35.12412  ? 352 VAL B CA   1 
ATOM   5030 C C    . VAL B 1 352 ? 111.16100 103.05800 77.90100  1.000 34.95875  ? 352 VAL B C    1 
ATOM   5031 O O    . VAL B 1 352 ? 110.08800 102.63600 77.44900  1.000 36.23627  ? 352 VAL B O    1 
ATOM   5032 C CB   . VAL B 1 352 ? 113.00400 101.37600 78.33500  1.000 37.47509  ? 352 VAL B CB   1 
ATOM   5033 C CG1  . VAL B 1 352 ? 112.01100 100.22900 78.37100  1.000 40.50293  ? 352 VAL B CG1  1 
ATOM   5034 C CG2  . VAL B 1 352 ? 114.36200 100.88500 77.86600  1.000 39.32387  ? 352 VAL B CG2  1 
ATOM   5035 N N    . MET B 1 353 ? 111.20500 104.00100 78.84200  1.000 36.67353  ? 353 MET B N    1 
ATOM   5036 C CA   . MET B 1 353 ? 109.97400 104.68200 79.23500  1.000 32.85156  ? 353 MET B CA   1 
ATOM   5037 C C    . MET B 1 353 ? 109.31700 105.37800 78.04600  1.000 35.36319  ? 353 MET B C    1 
ATOM   5038 O O    . MET B 1 353 ? 108.08800 105.35500 77.90200  1.000 39.21358  ? 353 MET B O    1 
ATOM   5039 C CB   . MET B 1 353 ? 110.25600 105.68600 80.35100  1.000 36.54563  ? 353 MET B CB   1 
ATOM   5040 C CG   . MET B 1 353 ? 109.00000 106.28400 80.96300  1.000 42.07777  ? 353 MET B CG   1 
ATOM   5041 S SD   . MET B 1 353 ? 109.15800 108.03700 81.34400  1.000 56.95097  ? 353 MET B SD   1 
ATOM   5042 C CE   . MET B 1 353 ? 110.00800 107.96500 82.91700  1.000 44.48957  ? 353 MET B CE   1 
ATOM   5043 N N    . ALA B 1 354 ? 110.11900 105.98300 77.16700  1.000 38.90003  ? 354 ALA B N    1 
ATOM   5044 C CA   . ALA B 1 354 ? 109.54300 106.61900 75.98100  1.000 32.93649  ? 354 ALA B CA   1 
ATOM   5045 C C    . ALA B 1 354 ? 108.97200 105.59800 74.99900  1.000 36.42973  ? 354 ALA B C    1 
ATOM   5046 O O    . ALA B 1 354 ? 107.95000 105.86100 74.34800  1.000 32.96014  ? 354 ALA B O    1 
ATOM   5047 C CB   . ALA B 1 354 ? 110.59100 107.48900 75.28900  1.000 31.40426  ? 354 ALA B CB   1 
ATOM   5048 N N    . LEU B 1 355 ? 109.57900 104.41300 74.91300  1.000 36.72450  ? 355 LEU B N    1 
ATOM   5049 C CA   . LEU B 1 355 ? 109.03200 103.38600 74.03200  1.000 36.96678  ? 355 LEU B CA   1 
ATOM   5050 C C    . LEU B 1 355 ? 107.73300 102.81900 74.58400  1.000 39.75035  ? 355 LEU B C    1 
ATOM   5051 O O    . LEU B 1 355 ? 106.85300 102.42100 73.81200  1.000 34.71710  ? 355 LEU B O    1 
ATOM   5052 C CB   . LEU B 1 355 ? 110.04700 102.26100 73.82200  1.000 39.95818  ? 355 LEU B CB   1 
ATOM   5053 C CG   . LEU B 1 355 ? 111.18700 102.50500 72.83500  1.000 41.57696  ? 355 LEU B CG   1 
ATOM   5054 C CD1  . LEU B 1 355 ? 112.31900 101.52300 73.07600  1.000 37.10040  ? 355 LEU B CD1  1 
ATOM   5055 C CD2  . LEU B 1 355 ? 110.68300 102.40200 71.40700  1.000 36.24354  ? 355 LEU B CD2  1 
ATOM   5056 N N    . HIS B 1 356 ? 107.59300 102.77600 75.90800  1.000 45.35022  ? 356 HIS B N    1 
ATOM   5057 C CA   . HIS B 1 356 ? 106.31200 102.39100 76.49200  1.000 41.03634  ? 356 HIS B CA   1 
ATOM   5058 C C    . HIS B 1 356 ? 105.26200 103.47300 76.27400  1.000 45.86199  ? 356 HIS B C    1 
ATOM   5059 O O    . HIS B 1 356 ? 104.09400 103.17000 76.00700  1.000 44.63280  ? 356 HIS B O    1 
ATOM   5060 C CB   . HIS B 1 356 ? 106.47400 102.10200 77.98300  1.000 43.17856  ? 356 HIS B CB   1 
ATOM   5061 C CG   . HIS B 1 356 ? 105.23900 101.55400 78.62600  1.000 51.92653  ? 356 HIS B CG   1 
ATOM   5062 N ND1  . HIS B 1 356 ? 104.82400 101.93200 79.88500  1.000 53.02401  ? 356 HIS B ND1  1 
ATOM   5063 C CD2  . HIS B 1 356 ? 104.32700 100.65500 78.18400  1.000 50.30773  ? 356 HIS B CD2  1 
ATOM   5064 C CE1  . HIS B 1 356 ? 103.71000 101.29100 80.19000  1.000 49.17400  ? 356 HIS B CE1  1 
ATOM   5065 N NE2  . HIS B 1 356 ? 103.38800 100.50900 79.17600  1.000 49.76095  ? 356 HIS B NE2  1 
ATOM   5066 N N    . GLY B 1 357 ? 105.66100 104.74100 76.38300  1.000 46.42222  ? 357 GLY B N    1 
ATOM   5067 C CA   . GLY B 1 357 ? 104.75200 105.82600 76.04500  1.000 43.83130  ? 357 GLY B CA   1 
ATOM   5068 C C    . GLY B 1 357 ? 104.24600 105.75600 74.61700  1.000 44.35500  ? 357 GLY B C    1 
ATOM   5069 O O    . GLY B 1 357 ? 103.09400 106.09600 74.33900  1.000 45.33206  ? 357 GLY B O    1 
ATOM   5070 N N    . CYS B 1 358 ? 105.10100 105.32400 73.68900  1.000 49.98124  ? 358 CYS B N    1 
ATOM   5071 C CA   . CYS B 1 358 ? 104.66600 105.18600 72.29900  1.000 45.95382  ? 358 CYS B CA   1 
ATOM   5072 C C    . CYS B 1 358 ? 103.50100 104.21100 72.14400  1.000 44.91639  ? 358 CYS B C    1 
ATOM   5073 O O    . CYS B 1 358 ? 102.67500 104.37700 71.24000  1.000 44.17164  ? 358 CYS B O    1 
ATOM   5074 C CB   . CYS B 1 358 ? 105.83400 104.74000 71.41800  1.000 44.77366  ? 358 CYS B CB   1 
ATOM   5075 S SG   . CYS B 1 358 ? 106.63900 106.06900 70.50000  1.000 50.62335  ? 358 CYS B SG   1 
ATOM   5076 N N    . ILE B 1 359 ? 103.41900 103.18800 72.99800  1.000 50.26399  ? 359 ILE B N    1 
ATOM   5077 C CA   . ILE B 1 359 ? 102.31300 102.23500 72.91100  1.000 48.74815  ? 359 ILE B CA   1 
ATOM   5078 C C    . ILE B 1 359 ? 100.99200 102.84700 73.36800  1.000 50.55242  ? 359 ILE B C    1 
ATOM   5079 O O    . ILE B 1 359 ? 99.92300  102.45600 72.88500  1.000 49.44295  ? 359 ILE B O    1 
ATOM   5080 C CB   . ILE B 1 359 ? 102.63900 100.96200 73.71400  1.000 50.86697  ? 359 ILE B CB   1 
ATOM   5081 C CG1  . ILE B 1 359 ? 103.64000 100.09100 72.95700  1.000 48.65048  ? 359 ILE B CG1  1 
ATOM   5082 C CG2  . ILE B 1 359 ? 101.37300 100.17500 74.00100  1.000 46.64339  ? 359 ILE B CG2  1 
ATOM   5083 C CD1  . ILE B 1 359 ? 104.21100 98.96600  73.78700  1.000 47.52859  ? 359 ILE B CD1  1 
ATOM   5084 N N    . LEU B 1 360 ? 101.02900 103.79900 74.29700  1.000 54.62837  ? 360 LEU B N    1 
ATOM   5085 C CA   . LEU B 1 360 ? 99.81700  104.42100 74.81700  1.000 51.67620  ? 360 LEU B CA   1 
ATOM   5086 C C    . LEU B 1 360 ? 99.36800  105.63900 74.02100  1.000 54.37526  ? 360 LEU B C    1 
ATOM   5087 O O    . LEU B 1 360 ? 98.38900  106.28400 74.40800  1.000 53.75029  ? 360 LEU B O    1 
ATOM   5088 C CB   . LEU B 1 360 ? 100.01400 104.81800 76.28400  1.000 49.09687  ? 360 LEU B CB   1 
ATOM   5089 C CG   . LEU B 1 360 ? 100.60900 103.75900 77.21300  1.000 53.38265  ? 360 LEU B CG   1 
ATOM   5090 C CD1  . LEU B 1 360 ? 101.17700 104.40400 78.46700  1.000 50.09060  ? 360 LEU B CD1  1 
ATOM   5091 C CD2  . LEU B 1 360 ? 99.56600  102.71400 77.57000  1.000 52.25573  ? 360 LEU B CD2  1 
ATOM   5092 N N    . SER B 1 361 ? 100.04700 105.96900 72.92700  1.000 62.88963  ? 361 SER B N    1 
ATOM   5093 C CA   . SER B 1 361 ? 99.72600  107.18000 72.18600  1.000 61.07621  ? 361 SER B CA   1 
ATOM   5094 C C    . SER B 1 361 ? 98.36900  107.05700 71.50300  1.000 62.93072  ? 361 SER B C    1 
ATOM   5095 O O    . SER B 1 361 ? 97.99400  105.99100 71.00900  1.000 65.15729  ? 361 SER B O    1 
ATOM   5096 C CB   . SER B 1 361 ? 100.81000 107.46700 71.15000  1.000 62.23418  ? 361 SER B CB   1 
ATOM   5097 O OG   . SER B 1 361 ? 100.49800 106.86700 69.90600  1.000 63.87103  ? 361 SER B OG   1 
ATOM   5098 N N    . GLU B 1 362 ? 97.62600  108.16600 71.49200  1.000 68.23076  ? 362 GLU B N    1 
ATOM   5099 C CA   . GLU B 1 362 ? 96.32800  108.19600 70.82500  1.000 69.04772  ? 362 GLU B CA   1 
ATOM   5100 C C    . GLU B 1 362 ? 96.44900  107.87500 69.34000  1.000 70.23833  ? 362 GLU B C    1 
ATOM   5101 O O    . GLU B 1 362 ? 95.57000  107.22400 68.76500  1.000 71.56610  ? 362 GLU B O    1 
ATOM   5102 C CB   . GLU B 1 362 ? 95.67600  109.56500 71.02000  1.000 68.26146  ? 362 GLU B CB   1 
ATOM   5103 C CG   . GLU B 1 362 ? 95.83900  110.13300 72.41600  1.000 69.35262  ? 362 GLU B CG   1 
ATOM   5104 C CD   . GLU B 1 362 ? 94.52200  110.55400 73.02700  1.000 72.22404  ? 362 GLU B CD   1 
ATOM   5105 O OE1  . GLU B 1 362 ? 93.55000  110.74300 72.26700  1.000 73.76114  ? 362 GLU B OE1  1 
ATOM   5106 O OE2  . GLU B 1 362 ? 94.45900  110.69400 74.26600  1.000 71.94476  ? 362 GLU B OE2  1 
ATOM   5107 N N    . ILE B 1 363 ? 97.52400  108.32800 68.70300  1.000 66.32904  ? 363 ILE B N    1 
ATOM   5108 C CA   . ILE B 1 363 ? 97.72700  108.16100 67.26800  1.000 66.78674  ? 363 ILE B CA   1 
ATOM   5109 C C    . ILE B 1 363 ? 98.64600  106.97000 67.04100  1.000 68.40779  ? 363 ILE B C    1 
ATOM   5110 O O    . ILE B 1 363 ? 99.79600  106.96600 67.49500  1.000 67.34081  ? 363 ILE B O    1 
ATOM   5111 C CB   . ILE B 1 363 ? 98.30900  109.43600 66.63700  1.000 68.65768  ? 363 ILE B CB   1 
ATOM   5112 C CG1  . ILE B 1 363 ? 97.33500  110.60400 66.80600  1.000 69.64700  ? 363 ILE B CG1  1 
ATOM   5113 C CG2  . ILE B 1 363 ? 98.62900  109.20700 65.17000  1.000 68.71012  ? 363 ILE B CG2  1 
ATOM   5114 C CD1  . ILE B 1 363 ? 97.80800  111.89000 66.17300  1.000 68.62912  ? 363 ILE B CD1  1 
ATOM   5115 N N    . GLN B 1 364 ? 98.13900  105.95500 66.34100  1.000 69.08329  ? 364 GLN B N    1 
ATOM   5116 C CA   . GLN B 1 364 ? 98.88400  104.73400 66.07500  1.000 68.34184  ? 364 GLN B CA   1 
ATOM   5117 C C    . GLN B 1 364 ? 98.80600  104.39100 64.59300  1.000 68.07269  ? 364 GLN B C    1 
ATOM   5118 O O    . GLN B 1 364 ? 97.90400  104.83100 63.87700  1.000 69.76654  ? 364 GLN B O    1 
ATOM   5119 C CB   . GLN B 1 364 ? 98.35900  103.56400 66.91800  1.000 67.27887  ? 364 GLN B CB   1 
ATOM   5120 C CG   . GLN B 1 364 ? 97.90100  103.96600 68.30700  1.000 67.10502  ? 364 GLN B CG   1 
ATOM   5121 C CD   . GLN B 1 364 ? 98.28700  102.95400 69.36400  1.000 67.27582  ? 364 GLN B CD   1 
ATOM   5122 O OE1  . GLN B 1 364 ? 98.93900  101.95300 69.07200  1.000 67.96537  ? 364 GLN B OE1  1 
ATOM   5123 N NE2  . GLN B 1 364 ? 97.88700  103.21100 70.60300  1.000 66.42121  ? 364 GLN B NE2  1 
ATOM   5124 N N    . ALA B 1 365 ? 99.78900  103.57600 64.13500  1.000 71.67948  ? 365 ALA B N    1 
ATOM   5125 C CA   . ALA B 1 365 ? 100.02700 103.14400 62.76600  1.000 71.16799  ? 365 ALA B CA   1 
ATOM   5126 C C    . ALA B 1 365 ? 99.29800  101.83800 62.46200  1.000 72.28098  ? 365 ALA B C    1 
ATOM   5127 O O    . ALA B 1 365 ? 99.09200  101.01000 63.35500  1.000 73.45894  ? 365 ALA B O    1 
ATOM   5128 C CB   . ALA B 1 365 ? 101.52100 102.96000 62.51800  1.000 69.00608  ? 365 ALA B CB   1 
ATOM   5129 N N    . PRO B 1 366 ? 98.89600  101.64200 61.20700  1.000 73.36117  ? 366 PRO B N    1 
ATOM   5130 C CA   . PRO B 1 366 ? 98.26600  100.37100 60.82300  1.000 74.84436  ? 366 PRO B CA   1 
ATOM   5131 C C    . PRO B 1 366 ? 99.18300  99.18400  61.08700  1.000 74.69893  ? 366 PRO B C    1 
ATOM   5132 O O    . PRO B 1 366 ? 100.38000 99.21900  60.79300  1.000 74.11099  ? 366 PRO B O    1 
ATOM   5133 C CB   . PRO B 1 366 ? 97.98000  100.54700 59.32700  1.000 73.22944  ? 366 PRO B CB   1 
ATOM   5134 C CG   . PRO B 1 366 ? 98.84800  101.66200 58.87500  1.000 72.82541  ? 366 PRO B CG   1 
ATOM   5135 C CD   . PRO B 1 366 ? 99.15400  102.52400 60.05700  1.000 70.16543  ? 366 PRO B CD   1 
ATOM   5136 N N    . GLU B 1 367 ? 98.60100  98.12400  61.65200  1.000 74.49007  ? 367 GLU B N    1 
ATOM   5137 C CA   . GLU B 1 367 ? 99.37500  96.93400  61.99600  1.000 74.76784  ? 367 GLU B CA   1 
ATOM   5138 C C    . GLU B 1 367 ? 100.01600 96.29900  60.76700  1.000 74.32484  ? 367 GLU B C    1 
ATOM   5139 O O    . GLU B 1 367 ? 101.16400 95.83900  60.82300  1.000 73.31764  ? 367 GLU B O    1 
ATOM   5140 C CB   . GLU B 1 367 ? 98.48200  95.92400  62.71600  1.000 74.83207  ? 367 GLU B CB   1 
ATOM   5141 C CG   . GLU B 1 367 ? 97.87000  96.44800  64.00600  1.000 76.87808  ? 367 GLU B CG   1 
ATOM   5142 C CD   . GLU B 1 367 ? 98.57900  95.93700  65.24500  1.000 76.93150  ? 367 GLU B CD   1 
ATOM   5143 O OE1  . GLU B 1 367 ? 99.68400  95.37200  65.11200  1.000 77.11647  ? 367 GLU B OE1  1 
ATOM   5144 O OE2  . GLU B 1 367 ? 98.02700  96.09900  66.35400  1.000 74.00803  ? 367 GLU B OE2  1 
ATOM   5145 N N    . GLU B 1 368 ? 99.27700  96.23200  59.65500  1.000 77.00370  ? 368 GLU B N    1 
ATOM   5146 C CA   . GLU B 1 368 ? 99.83000  95.66500  58.43000  1.000 77.41961  ? 368 GLU B CA   1 
ATOM   5147 C C    . GLU B 1 368 ? 101.13200 96.34100  58.02200  1.000 78.75932  ? 368 GLU B C    1 
ATOM   5148 O O    . GLU B 1 368 ? 102.01000 95.69400  57.44000  1.000 78.55208  ? 368 GLU B O    1 
ATOM   5149 C CB   . GLU B 1 368 ? 98.81000  95.75400  57.29000  1.000 75.81070  ? 368 GLU B CB   1 
ATOM   5150 C CG   . GLU B 1 368 ? 98.05700  97.07200  57.19600  1.000 78.16608  ? 368 GLU B CG   1 
ATOM   5151 C CD   . GLU B 1 368 ? 96.93400  97.18100  58.20900  1.000 80.25351  ? 368 GLU B CD   1 
ATOM   5152 O OE1  . GLU B 1 368 ? 96.79300  96.26200  59.04200  1.000 79.41641  ? 368 GLU B OE1  1 
ATOM   5153 O OE2  . GLU B 1 368 ? 96.19200  98.18400  58.17200  1.000 79.85579  ? 368 GLU B OE2  1 
ATOM   5154 N N    . ARG B 1 369 ? 101.27800 97.63600  58.30700  1.000 75.90071  ? 369 ARG B N    1 
ATOM   5155 C CA   . ARG B 1 369 ? 102.53600 98.31000  58.00400  1.000 73.53542  ? 369 ARG B CA   1 
ATOM   5156 C C    . ARG B 1 369 ? 103.61900 97.96100  59.01800  1.000 74.97987  ? 369 ARG B C    1 
ATOM   5157 O O    . ARG B 1 369 ? 104.79700 97.86000  58.65800  1.000 75.56682  ? 369 ARG B O    1 
ATOM   5158 C CB   . ARG B 1 369 ? 102.32500 99.82200  57.93400  1.000 73.17061  ? 369 ARG B CB   1 
ATOM   5159 C CG   . ARG B 1 369 ? 102.10400 100.33000 56.51900  1.000 74.33632  ? 369 ARG B CG   1 
ATOM   5160 C CD   . ARG B 1 369 ? 101.01500 101.38500 56.45000  1.000 76.16350  ? 369 ARG B CD   1 
ATOM   5161 N NE   . ARG B 1 369 ? 101.09600 102.14900 55.21100  1.000 77.25447  ? 369 ARG B NE   1 
ATOM   5162 C CZ   . ARG B 1 369 ? 100.38500 103.23700 54.95100  1.000 77.52792  ? 369 ARG B CZ   1 
ATOM   5163 N NH1  . ARG B 1 369 ? 99.51700  103.72100 55.82500  1.000 76.83634  ? 369 ARG B NH1  1 
ATOM   5164 N NH2  . ARG B 1 369 ? 100.54800 103.85500 53.78500  1.000 75.00641  ? 369 ARG B NH2  1 
ATOM   5165 N N    . ARG B 1 370 ? 103.24700 97.77500  60.28700  1.000 65.94126  ? 370 ARG B N    1 
ATOM   5166 C CA   . ARG B 1 370 ? 104.23000 97.34800  61.27800  1.000 66.19838  ? 370 ARG B CA   1 
ATOM   5167 C C    . ARG B 1 370 ? 104.78800 95.97000  60.95200  1.000 67.52477  ? 370 ARG B C    1 
ATOM   5168 O O    . ARG B 1 370 ? 105.96500 95.69800  61.21400  1.000 66.29106  ? 370 ARG B O    1 
ATOM   5169 C CB   . ARG B 1 370 ? 103.62500 97.34100  62.68200  1.000 65.78939  ? 370 ARG B CB   1 
ATOM   5170 C CG   . ARG B 1 370 ? 102.67600 98.47600  62.99800  1.000 64.03542  ? 370 ARG B CG   1 
ATOM   5171 C CD   . ARG B 1 370 ? 102.11900 98.29400  64.40000  1.000 64.47337  ? 370 ARG B CD   1 
ATOM   5172 N NE   . ARG B 1 370 ? 101.17000 99.33400  64.77400  1.000 66.02672  ? 370 ARG B NE   1 
ATOM   5173 C CZ   . ARG B 1 370 ? 100.74500 99.54400  66.01200  1.000 66.49898  ? 370 ARG B CZ   1 
ATOM   5174 N NH1  . ARG B 1 370 ? 101.16200 98.79700  67.02100  1.000 64.06502  ? 370 ARG B NH1  1 
ATOM   5175 N NH2  . ARG B 1 370 ? 99.88000  100.52600 66.24400  1.000 64.90528  ? 370 ARG B NH2  1 
ATOM   5176 N N    . GLN B 1 371 ? 103.96400 95.09000  60.38200  1.000 71.16286  ? 371 GLN B N    1 
ATOM   5177 C CA   . GLN B 1 371 ? 104.39300 93.72700  60.08500  1.000 69.37368  ? 371 GLN B CA   1 
ATOM   5178 C C    . GLN B 1 371 ? 105.39700 93.63800  58.94300  1.000 70.48683  ? 371 GLN B C    1 
ATOM   5179 O O    . GLN B 1 371 ? 105.77100 92.52100  58.57000  1.000 71.83508  ? 371 GLN B O    1 
ATOM   5180 C CB   . GLN B 1 371 ? 103.17900 92.85300  59.77300  1.000 69.22702  ? 371 GLN B CB   1 
ATOM   5181 C CG   . GLN B 1 371 ? 102.12600 92.85100  60.86600  1.000 71.59352  ? 371 GLN B CG   1 
ATOM   5182 C CD   . GLN B 1 371 ? 102.57300 92.08700  62.09700  1.000 72.69798  ? 371 GLN B CD   1 
ATOM   5183 O OE1  . GLN B 1 371 ? 102.87700 90.89700  62.02500  1.000 73.74476  ? 371 GLN B OE1  1 
ATOM   5184 N NE2  . GLN B 1 371 ? 102.61800 92.77000  63.23400  1.000 70.55607  ? 371 GLN B NE2  1 
ATOM   5185 N N    . VAL B 1 372 ? 105.84100 94.75900  58.37900  1.000 68.96090  ? 372 VAL B N    1 
ATOM   5186 C CA   . VAL B 1 372 ? 106.88900 94.71100  57.36700  1.000 67.77220  ? 372 VAL B CA   1 
ATOM   5187 C C    . VAL B 1 372 ? 108.28200 94.69500  57.99500  1.000 68.54050  ? 372 VAL B C    1 
ATOM   5188 O O    . VAL B 1 372 ? 109.19700 94.06900  57.44900  1.000 70.92291  ? 372 VAL B O    1 
ATOM   5189 C CB   . VAL B 1 372 ? 106.74200 95.88700  56.38700  1.000 67.78426  ? 372 VAL B CB   1 
ATOM   5190 C CG1  . VAL B 1 372 ? 108.02600 96.08600  55.60000  1.000 66.52238  ? 372 VAL B CG1  1 
ATOM   5191 C CG2  . VAL B 1 372 ? 105.56800 95.65100  55.45100  1.000 68.63053  ? 372 VAL B CG2  1 
ATOM   5192 N N    . PHE B 1 373 ? 108.46400 95.36700  59.13200  1.000 68.38917  ? 373 PHE B N    1 
ATOM   5193 C CA   . PHE B 1 373 ? 109.74400 95.44000  59.82600  1.000 68.25694  ? 373 PHE B CA   1 
ATOM   5194 C C    . PHE B 1 373 ? 109.78600 94.51300  61.03500  1.000 68.01738  ? 373 PHE B C    1 
ATOM   5195 O O    . PHE B 1 373 ? 110.66200 94.65300  61.89500  1.000 70.28913  ? 373 PHE B O    1 
ATOM   5196 C CB   . PHE B 1 373 ? 110.03100 96.87900  60.25600  1.000 68.86844  ? 373 PHE B CB   1 
ATOM   5197 C CG   . PHE B 1 373 ? 109.81100 97.89500  59.17100  1.000 67.00287  ? 373 PHE B CG   1 
ATOM   5198 C CD1  . PHE B 1 373 ? 108.55300 98.43000  58.95200  1.000 66.72719  ? 373 PHE B CD1  1 
ATOM   5199 C CD2  . PHE B 1 373 ? 110.86000 98.31900  58.37500  1.000 68.53569  ? 373 PHE B CD2  1 
ATOM   5200 C CE1  . PHE B 1 373 ? 108.34600 99.36600  57.95800  1.000 67.34389  ? 373 PHE B CE1  1 
ATOM   5201 C CE2  . PHE B 1 373 ? 110.65900 99.25500  57.38000  1.000 68.19641  ? 373 PHE B CE2  1 
ATOM   5202 C CZ   . PHE B 1 373 ? 109.40100 99.77900  57.17100  1.000 66.94664  ? 373 PHE B CZ   1 
ATOM   5203 N N    . ARG B 1 374 ? 108.85200 93.56700  61.10500  1.000 67.72112  ? 374 ARG B N    1 
ATOM   5204 C CA   . ARG B 1 374 ? 108.68700 92.63600  62.21400  1.000 68.16577  ? 374 ARG B CA   1 
ATOM   5205 C C    . ARG B 1 374 ? 109.93100 91.81200  62.53900  1.000 68.45386  ? 374 ARG B C    1 
ATOM   5206 O O    . ARG B 1 374 ? 109.97200 91.20500  63.61500  1.000 68.49916  ? 374 ARG B O    1 
ATOM   5207 C CB   . ARG B 1 374 ? 107.50800 91.70600  61.90300  1.000 68.09036  ? 374 ARG B CB   1 
ATOM   5208 C CG   . ARG B 1 374 ? 107.56100 90.34700  62.57600  1.000 68.81785  ? 374 ARG B CG   1 
ATOM   5209 C CD   . ARG B 1 374 ? 106.26900 90.05400  63.31300  1.000 69.45695  ? 374 ARG B CD   1 
ATOM   5210 N NE   . ARG B 1 374 ? 106.38800 88.89000  64.18100  1.000 71.98272  ? 374 ARG B NE   1 
ATOM   5211 C CZ   . ARG B 1 374 ? 105.48800 88.53800  65.08900  1.000 70.31684  ? 374 ARG B CZ   1 
ATOM   5212 N NH1  . ARG B 1 374 ? 104.38200 89.24000  65.27300  1.000 68.99213  ? 374 ARG B NH1  1 
ATOM   5213 N NH2  . ARG B 1 374 ? 105.70400 87.45600  65.83100  1.000 69.34905  ? 374 ARG B NH2  1 
ATOM   5214 N N    . GLN B 1 375 ? 110.94700 91.77600  61.67600  1.000 71.77417  ? 375 GLN B N    1 
ATOM   5215 C CA   . GLN B 1 375 ? 112.08000 90.89300  61.93000  1.000 71.24414  ? 375 GLN B CA   1 
ATOM   5216 C C    . GLN B 1 375 ? 113.33600 91.58700  62.44800  1.000 72.03115  ? 375 GLN B C    1 
ATOM   5217 O O    . GLN B 1 375 ? 114.23400 90.89600  62.94000  1.000 72.41604  ? 375 GLN B O    1 
ATOM   5218 C CB   . GLN B 1 375 ? 112.43600 90.12600  60.65000  1.000 70.30273  ? 375 GLN B CB   1 
ATOM   5219 C CG   . GLN B 1 375 ? 111.31100 89.25600  60.11500  1.000 72.07132  ? 375 GLN B CG   1 
ATOM   5220 C CD   . GLN B 1 375 ? 111.34300 87.85000  60.67700  1.000 75.14000  ? 375 GLN B CD   1 
ATOM   5221 O OE1  . GLN B 1 375 ? 110.65500 87.54200  61.65000  1.000 74.80101  ? 375 GLN B OE1  1 
ATOM   5222 N NE2  . GLN B 1 375 ? 112.14100 86.98600  60.06200  1.000 72.94011  ? 375 GLN B NE2  1 
ATOM   5223 N N    . GLU B 1 376 ? 113.44000 92.91300  62.36000  1.000 65.22749  ? 376 GLU B N    1 
ATOM   5224 C CA   . GLU B 1 376 ? 114.64000 93.58500  62.84700  1.000 65.10068  ? 376 GLU B CA   1 
ATOM   5225 C C    . GLU B 1 376 ? 114.47400 94.17000  64.24300  1.000 66.90203  ? 376 GLU B C    1 
ATOM   5226 O O    . GLU B 1 376 ? 115.46000 94.24500  64.99500  1.000 69.58449  ? 376 GLU B O    1 
ATOM   5227 C CB   . GLU B 1 376 ? 115.04900 94.70300  61.88200  1.000 65.53878  ? 376 GLU B CB   1 
ATOM   5228 C CG   . GLU B 1 376 ? 115.94000 94.23900  60.74800  1.000 66.60521  ? 376 GLU B CG   1 
ATOM   5229 C CD   . GLU B 1 376 ? 115.14900 93.79300  59.53900  1.000 68.65753  ? 376 GLU B CD   1 
ATOM   5230 O OE1  . GLU B 1 376 ? 113.90400 93.74200  59.62900  1.000 66.79981  ? 376 GLU B OE1  1 
ATOM   5231 O OE2  . GLU B 1 376 ? 115.76900 93.49200  58.49900  1.000 69.80833  ? 376 GLU B OE2  1 
ATOM   5232 N N    . LEU B 1 377 ? 113.23300 94.39600  64.66900  1.000 56.79059  ? 377 LEU B N    1 
ATOM   5233 C CA   . LEU B 1 377 ? 112.99300 94.91200  66.00700  1.000 60.22772  ? 377 LEU B CA   1 
ATOM   5234 C C    . LEU B 1 377 ? 113.12000 93.80900  67.04300  1.000 63.19501  ? 377 LEU B C    1 
ATOM   5235 O O    . LEU B 1 377 ? 113.64200 94.04100  68.13900  1.000 63.15927  ? 377 LEU B O    1 
ATOM   5236 C CB   . LEU B 1 377 ? 111.60800 95.55700  66.06900  1.000 61.92967  ? 377 LEU B CB   1 
ATOM   5237 C CG   . LEU B 1 377 ? 111.30700 96.59700  64.98500  1.000 61.19108  ? 377 LEU B CG   1 
ATOM   5238 C CD1  . LEU B 1 377 ? 109.83000 96.59200  64.62400  1.000 57.46885  ? 377 LEU B CD1  1 
ATOM   5239 C CD2  . LEU B 1 377 ? 111.75000 97.98700  65.41200  1.000 59.43952  ? 377 LEU B CD2  1 
ATOM   5240 N N    . GLN B 1 378 ? 112.70500 92.59100  66.69800  1.000 63.79773  ? 378 GLN B N    1 
ATOM   5241 C CA   . GLN B 1 378 ? 112.80700 91.51200  67.66700  1.000 63.66560  ? 378 GLN B CA   1 
ATOM   5242 C C    . GLN B 1 378 ? 114.25400 91.07400  67.82900  1.000 64.23395  ? 378 GLN B C    1 
ATOM   5243 O O    . GLN B 1 378 ? 114.67400 90.72200  68.93500  1.000 65.94318  ? 378 GLN B O    1 
ATOM   5244 C CB   . GLN B 1 378 ? 111.93600 90.33300  67.23700  1.000 62.06984  ? 378 GLN B CB   1 
ATOM   5245 C CG   . GLN B 1 378 ? 110.45800 90.66000  67.14400  1.000 67.24929  ? 378 GLN B CG   1 
ATOM   5246 C CD   . GLN B 1 378 ? 109.59100 89.41900  67.10700  1.000 70.22140  ? 378 GLN B CD   1 
ATOM   5247 O OE1  . GLN B 1 378 ? 108.67700 89.26200  67.91600  1.000 68.85018  ? 378 GLN B OE1  1 
ATOM   5248 N NE2  . GLN B 1 378 ? 109.87300 88.52800  66.16400  1.000 68.37557  ? 378 GLN B NE2  1 
ATOM   5249 N N    . ARG B 1 379 ? 115.03900 91.13300  66.75100  1.000 55.40533  ? 379 ARG B N    1 
ATOM   5250 C CA   . ARG B 1 379 ? 116.46300 90.84400  66.86400  1.000 55.14104  ? 379 ARG B CA   1 
ATOM   5251 C C    . ARG B 1 379 ? 117.17700 91.90600  67.69400  1.000 55.85559  ? 379 ARG B C    1 
ATOM   5252 O O    . ARG B 1 379 ? 117.99700 91.57400  68.56500  1.000 59.39917  ? 379 ARG B O    1 
ATOM   5253 C CB   . ARG B 1 379 ? 117.07700 90.73200  65.46800  1.000 55.52438  ? 379 ARG B CB   1 
ATOM   5254 C CG   . ARG B 1 379 ? 118.19700 89.71200  65.35700  1.000 59.74315  ? 379 ARG B CG   1 
ATOM   5255 C CD   . ARG B 1 379 ? 119.22700 90.11200  64.31700  1.000 60.20707  ? 379 ARG B CD   1 
ATOM   5256 N NE   . ARG B 1 379 ? 120.59000 89.85600  64.76700  1.000 61.74815  ? 379 ARG B NE   1 
ATOM   5257 C CZ   . ARG B 1 379 ? 121.67800 90.30800  64.15900  1.000 62.16917  ? 379 ARG B CZ   1 
ATOM   5258 N NH1  . ARG B 1 379 ? 121.60100 91.06000  63.07400  1.000 63.24900  ? 379 ARG B NH1  1 
ATOM   5259 N NH2  . ARG B 1 379 ? 122.87300 89.99800  64.65200  1.000 56.72092  ? 379 ARG B NH2  1 
ATOM   5260 N N    . VAL B 1 380 ? 116.84700 93.18600  67.47900  1.000 53.37846  ? 380 VAL B N    1 
ATOM   5261 C CA   . VAL B 1 380 ? 117.45800 94.23300  68.29500  1.000 53.39024  ? 380 VAL B CA   1 
ATOM   5262 C C    . VAL B 1 380 ? 117.09600 94.04400  69.76500  1.000 52.38401  ? 380 VAL B C    1 
ATOM   5263 O O    . VAL B 1 380 ? 117.95300 94.16100  70.65400  1.000 54.19625  ? 380 VAL B O    1 
ATOM   5264 C CB   . VAL B 1 380 ? 117.03700 95.62300  67.78400  1.000 53.91639  ? 380 VAL B CB   1 
ATOM   5265 C CG1  . VAL B 1 380 ? 117.33300 96.68500  68.83000  1.000 54.83783  ? 380 VAL B CG1  1 
ATOM   5266 C CG2  . VAL B 1 380 ? 117.74000 95.94500  66.47700  1.000 55.54524  ? 380 VAL B CG2  1 
ATOM   5267 N N    . GLY B 1 381 ? 115.82900 93.73200  70.04200  1.000 46.47508  ? 381 GLY B N    1 
ATOM   5268 C CA   . GLY B 1 381 ? 115.40800 93.53600  71.42000  1.000 46.73298  ? 381 GLY B CA   1 
ATOM   5269 C C    . GLY B 1 381 ? 116.09800 92.35900  72.08200  1.000 51.28698  ? 381 GLY B C    1 
ATOM   5270 O O    . GLY B 1 381 ? 116.56800 92.45600  73.22000  1.000 54.17202  ? 381 GLY B O    1 
ATOM   5271 N N    . VAL B 1 382 ? 116.13400 91.21800  71.39100  1.000 48.31186  ? 382 VAL B N    1 
ATOM   5272 C CA   . VAL B 1 382 ? 116.79200 90.03500  71.93600  1.000 48.85058  ? 382 VAL B CA   1 
ATOM   5273 C C    . VAL B 1 382 ? 118.25300 90.32800  72.25200  1.000 49.31054  ? 382 VAL B C    1 
ATOM   5274 O O    . VAL B 1 382 ? 118.75700 89.96400  73.32400  1.000 55.31685  ? 382 VAL B O    1 
ATOM   5275 C CB   . VAL B 1 382 ? 116.65200 88.85300  70.95900  1.000 49.50944  ? 382 VAL B CB   1 
ATOM   5276 C CG1  . VAL B 1 382 ? 117.71600 87.80400  71.23300  1.000 49.96975  ? 382 VAL B CG1  1 
ATOM   5277 C CG2  . VAL B 1 382 ? 115.26200 88.24900  71.05200  1.000 49.69770  ? 382 VAL B CG2  1 
ATOM   5278 N N    . GLU B 1 383 ? 118.95100 91.02000  71.34600  1.000 46.80537  ? 383 GLU B N    1 
ATOM   5279 C CA   . GLU B 1 383 ? 120.36800 91.27600  71.58600  1.000 48.54082  ? 383 GLU B CA   1 
ATOM   5280 C C    . GLU B 1 383 ? 120.57200 92.24100  72.74900  1.000 48.84764  ? 383 GLU B C    1 
ATOM   5281 O O    . GLU B 1 383 ? 121.46800 92.03700  73.58300  1.000 49.38970  ? 383 GLU B O    1 
ATOM   5282 C CB   . GLU B 1 383 ? 121.02400 91.81400  70.31600  1.000 45.87838  ? 383 GLU B CB   1 
ATOM   5283 C CG   . GLU B 1 383 ? 120.89200 90.88600  69.12100  1.000 49.35438  ? 383 GLU B CG   1 
ATOM   5284 C CD   . GLU B 1 383 ? 121.84900 89.71500  69.18000  1.000 56.21055  ? 383 GLU B CD   1 
ATOM   5285 O OE1  . GLU B 1 383 ? 121.86100 89.00600  70.20800  1.000 54.18293  ? 383 GLU B OE1  1 
ATOM   5286 O OE2  . GLU B 1 383 ? 122.58700 89.49800  68.19700  1.000 58.55233  ? 383 GLU B OE2  1 
ATOM   5287 N N    . GLY B 1 384 ? 119.72900 93.27100  72.85300  1.000 42.24388  ? 384 GLY B N    1 
ATOM   5288 C CA   . GLY B 1 384 ? 119.85400 94.19100  73.97200  1.000 38.14670  ? 384 GLY B CA   1 
ATOM   5289 C C    . GLY B 1 384 ? 119.58000 93.52800  75.30700  1.000 43.58708  ? 384 GLY B C    1 
ATOM   5290 O O    . GLY B 1 384 ? 120.28500 93.77100  76.29300  1.000 45.67919  ? 384 GLY B O    1 
ATOM   5291 N N    . ALA B 1 385 ? 118.56600 92.66100  75.35400  1.000 41.35267  ? 385 ALA B N    1 
ATOM   5292 C CA   . ALA B 1 385 ? 118.24600 91.98500  76.60500  1.000 41.99666  ? 385 ALA B CA   1 
ATOM   5293 C C    . ALA B 1 385 ? 119.35200 91.01900  77.00400  1.000 41.51159  ? 385 ALA B C    1 
ATOM   5294 O O    . ALA B 1 385 ? 119.71400 90.93200  78.18500  1.000 44.77501  ? 385 ALA B O    1 
ATOM   5295 C CB   . ALA B 1 385 ? 116.90900 91.25600  76.48100  1.000 40.71925  ? 385 ALA B CB   1 
ATOM   5296 N N    . LYS B 1 386 ? 119.92700 90.30800  76.03000  1.000 40.48924  ? 386 LYS B N    1 
ATOM   5297 C CA   . LYS B 1 386 ? 121.02200 89.40000  76.34800  1.000 41.88594  ? 386 LYS B CA   1 
ATOM   5298 C C    . LYS B 1 386 ? 122.23600 90.16200  76.86700  1.000 41.22093  ? 386 LYS B C    1 
ATOM   5299 O O    . LYS B 1 386 ? 122.89300 89.72500  77.82100  1.000 41.14303  ? 386 LYS B O    1 
ATOM   5300 C CB   . LYS B 1 386 ? 121.38200 88.56800  75.11900  1.000 42.71242  ? 386 LYS B CB   1 
ATOM   5301 C CG   . LYS B 1 386 ? 122.82100 88.09700  75.07600  1.000 45.03606  ? 386 LYS B CG   1 
ATOM   5302 C CD   . LYS B 1 386 ? 123.04100 87.16000  73.90500  1.000 44.81329  ? 386 LYS B CD   1 
ATOM   5303 C CE   . LYS B 1 386 ? 121.90100 86.16300  73.78700  1.000 45.03013  ? 386 LYS B CE   1 
ATOM   5304 N NZ   . LYS B 1 386 ? 121.71300 85.69100  72.38700  1.000 46.55399  ? 386 LYS B NZ   1 
ATOM   5305 N N    . LEU B 1 387 ? 122.54000 91.31500  76.26700  1.000 41.04941  ? 387 LEU B N    1 
ATOM   5306 C CA   . LEU B 1 387 ? 123.67500 92.10400  76.73800  1.000 39.31241  ? 387 LEU B CA   1 
ATOM   5307 C C    . LEU B 1 387 ? 123.44800 92.61300  78.16000  1.000 39.17711  ? 387 LEU B C    1 
ATOM   5308 O O    . LEU B 1 387 ? 124.34700 92.54200  79.01100  1.000 38.42176  ? 387 LEU B O    1 
ATOM   5309 C CB   . LEU B 1 387 ? 123.93600 93.26500  75.77900  1.000 40.78165  ? 387 LEU B CB   1 
ATOM   5310 C CG   . LEU B 1 387 ? 125.18400 94.11500  76.02500  1.000 41.11700  ? 387 LEU B CG   1 
ATOM   5311 C CD1  . LEU B 1 387 ? 125.61200 94.78700  74.73800  1.000 41.27982  ? 387 LEU B CD1  1 
ATOM   5312 C CD2  . LEU B 1 387 ? 124.93900 95.15500  77.10600  1.000 41.02954  ? 387 LEU B CD2  1 
ATOM   5313 N N    . LEU B 1 388 ? 122.25200 93.14600  78.43600  1.000 35.34024  ? 388 LEU B N    1 
ATOM   5314 C CA   . LEU B 1 388 ? 121.97100 93.61700  79.79100  1.000 36.46635  ? 388 LEU B CA   1 
ATOM   5315 C C    . LEU B 1 388 ? 122.00700 92.48600  80.81400  1.000 39.74960  ? 388 LEU B C    1 
ATOM   5316 O O    . LEU B 1 388 ? 122.49100 92.68300  81.93800  1.000 40.36189  ? 388 LEU B O    1 
ATOM   5317 C CB   . LEU B 1 388 ? 120.61900 94.32900  79.83000  1.000 40.03203  ? 388 LEU B CB   1 
ATOM   5318 C CG   . LEU B 1 388 ? 120.53100 95.65300  79.06600  1.000 40.25499  ? 388 LEU B CG   1 
ATOM   5319 C CD1  . LEU B 1 388 ? 119.09700 96.14300  78.99200  1.000 35.36012  ? 388 LEU B CD1  1 
ATOM   5320 C CD2  . LEU B 1 388 ? 121.41800 96.70000  79.71500  1.000 35.81838  ? 388 LEU B CD2  1 
ATOM   5321 N N    . ARG B 1 389 ? 121.58800 91.27600  80.43000  1.000 43.65699  ? 389 ARG B N    1 
ATOM   5322 C CA   . ARG B 1 389 ? 121.63400 90.18600  81.39700  1.000 38.71588  ? 389 ARG B CA   1 
ATOM   5323 C C    . ARG B 1 389 ? 123.05000 89.67100  81.60200  1.000 42.38943  ? 389 ARG B C    1 
ATOM   5324 O O    . ARG B 1 389 ? 123.39500 89.23700  82.70800  1.000 42.01582  ? 389 ARG B O    1 
ATOM   5325 C CB   . ARG B 1 389 ? 120.72300 89.03700  80.96100  1.000 35.01626  ? 389 ARG B CB   1 
ATOM   5326 C CG   . ARG B 1 389 ? 119.24200 89.29900  81.15800  1.000 41.00283  ? 389 ARG B CG   1 
ATOM   5327 C CD   . ARG B 1 389 ? 118.40600 88.16700  80.58800  1.000 40.88811  ? 389 ARG B CD   1 
ATOM   5328 N NE   . ARG B 1 389 ? 116.97900 88.45600  80.65400  1.000 41.44276  ? 389 ARG B NE   1 
ATOM   5329 C CZ   . ARG B 1 389 ? 116.16400 88.45700  79.60800  1.000 41.08959  ? 389 ARG B CZ   1 
ATOM   5330 N NH1  . ARG B 1 389 ? 116.60000 88.16800  78.39400  1.000 39.78253  ? 389 ARG B NH1  1 
ATOM   5331 N NH2  . ARG B 1 389 ? 114.88000 88.75000  79.78700  1.000 38.76169  ? 389 ARG B NH2  1 
ATOM   5332 N N    . GLU B 1 390 ? 123.90500 89.78400  80.58600  1.000 44.48856  ? 390 GLU B N    1 
ATOM   5333 C CA   . GLU B 1 390 ? 125.29000 89.37500  80.77200  1.000 40.98986  ? 390 GLU B CA   1 
ATOM   5334 C C    . GLU B 1 390 ? 126.03200 90.36700  81.65800  1.000 42.82662  ? 390 GLU B C    1 
ATOM   5335 O O    . GLU B 1 390 ? 126.82900 89.96800  82.51700  1.000 40.89839  ? 390 GLU B O    1 
ATOM   5336 C CB   . GLU B 1 390 ? 125.98100 89.23200  79.41800  1.000 40.63079  ? 390 GLU B CB   1 
ATOM   5337 C CG   . GLU B 1 390 ? 127.49500 89.27700  79.48600  1.000 45.18256  ? 390 GLU B CG   1 
ATOM   5338 C CD   . GLU B 1 390 ? 128.14600 88.69100  78.25100  1.000 52.80849  ? 390 GLU B CD   1 
ATOM   5339 O OE1  . GLU B 1 390 ? 127.92700 89.23400  77.14700  1.000 51.78163  ? 390 GLU B OE1  1 
ATOM   5340 O OE2  . GLU B 1 390 ? 128.87700 87.68700  78.38300  1.000 54.67078  ? 390 GLU B OE2  1 
ATOM   5341 N N    . LEU B 1 391 ? 125.76300 91.66400  81.48500  1.000 46.37157  ? 391 LEU B N    1 
ATOM   5342 C CA   . LEU B 1 391 ? 126.34600 92.65100  82.39100  1.000 42.52196  ? 391 LEU B CA   1 
ATOM   5343 C C    . LEU B 1 391 ? 125.86500 92.44800  83.82400  1.000 40.11880  ? 391 LEU B C    1 
ATOM   5344 O O    . LEU B 1 391 ? 126.65800 92.53900  84.77000  1.000 39.42913  ? 391 LEU B O    1 
ATOM   5345 C CB   . LEU B 1 391 ? 126.02500 94.06800  81.91600  1.000 41.73749  ? 391 LEU B CB   1 
ATOM   5346 C CG   . LEU B 1 391 ? 126.88000 94.62000  80.77500  1.000 43.21222  ? 391 LEU B CG   1 
ATOM   5347 C CD1  . LEU B 1 391 ? 126.46300 96.04000  80.43800  1.000 40.42550  ? 391 LEU B CD1  1 
ATOM   5348 C CD2  . LEU B 1 391 ? 128.35600 94.55800  81.13100  1.000 40.90941  ? 391 LEU B CD2  1 
ATOM   5349 N N    . GLY B 1 392 ? 124.57400 92.16300  84.00700  1.000 38.04033  ? 392 GLY B N    1 
ATOM   5350 C CA   . GLY B 1 392 ? 124.08400 91.87000  85.34700  1.000 41.49761  ? 392 GLY B CA   1 
ATOM   5351 C C    . GLY B 1 392 ? 124.76700 90.66800  85.97400  1.000 44.14960  ? 392 GLY B C    1 
ATOM   5352 O O    . GLY B 1 392 ? 125.19300 90.70900  87.13500  1.000 38.60669  ? 392 GLY B O    1 
ATOM   5353 N N    . GLU B 1 393 ? 124.89200 89.58100  85.20800  1.000 51.10995  ? 393 GLU B N    1 
ATOM   5354 C CA   . GLU B 1 393 ? 125.51000 88.37100  85.73900  1.000 45.86177  ? 393 GLU B CA   1 
ATOM   5355 C C    . GLU B 1 393 ? 126.97600 88.59900  86.08600  1.000 41.96742  ? 393 GLU B C    1 
ATOM   5356 O O    . GLU B 1 393 ? 127.46900 88.07800  87.09200  1.000 41.04112  ? 393 GLU B O    1 
ATOM   5357 C CB   . GLU B 1 393 ? 125.37300 87.23200  84.72900  1.000 45.10946  ? 393 GLU B CB   1 
ATOM   5358 C CG   . GLU B 1 393 ? 125.16800 85.86100  85.34600  1.000 43.64255  ? 393 GLU B CG   1 
ATOM   5359 C CD   . GLU B 1 393 ? 123.94400 85.79900  86.23400  1.000 52.93433  ? 393 GLU B CD   1 
ATOM   5360 O OE1  . GLU B 1 393 ? 122.81700 85.88200  85.70200  1.000 57.51444  ? 393 GLU B OE1  1 
ATOM   5361 O OE2  . GLU B 1 393 ? 124.10600 85.66100  87.46300  1.000 49.71461  ? 393 GLU B OE2  1 
ATOM   5362 N N    . LYS B 1 394 ? 127.69100 89.37500  85.26900  1.000 44.91805  ? 394 LYS B N    1 
ATOM   5363 C CA   . LYS B 1 394 ? 129.08100 89.68200  85.59300  1.000 45.05834  ? 394 LYS B CA   1 
ATOM   5364 C C    . LYS B 1 394 ? 129.19500 90.55100  86.84000  1.000 40.89660  ? 394 LYS B C    1 
ATOM   5365 O O    . LYS B 1 394 ? 130.08000 90.33000  87.67400  1.000 35.86744  ? 394 LYS B O    1 
ATOM   5366 C CB   . LYS B 1 394 ? 129.77000 90.35300  84.40700  1.000 43.81432  ? 394 LYS B CB   1 
ATOM   5367 C CG   . LYS B 1 394 ? 130.78800 89.46300  83.72100  1.000 42.35662  ? 394 LYS B CG   1 
ATOM   5368 C CD   . LYS B 1 394 ? 130.95200 89.82200  82.26000  1.000 47.08534  ? 394 LYS B CD   1 
ATOM   5369 C CE   . LYS B 1 394 ? 132.20300 89.18400  81.68700  1.000 48.18313  ? 394 LYS B CE   1 
ATOM   5370 N NZ   . LYS B 1 394 ? 131.98300 87.75700  81.33400  1.000 45.80382  ? 394 LYS B NZ   1 
ATOM   5371 N N    . VAL B 1 395 ? 128.32300 91.55000  86.98500  1.000 44.26925  ? 395 VAL B N    1 
ATOM   5372 C CA   . VAL B 1 395 ? 128.36300 92.38100  88.18700  1.000 37.94000  ? 395 VAL B CA   1 
ATOM   5373 C C    . VAL B 1 395 ? 128.11000 91.54500  89.43500  1.000 42.14642  ? 395 VAL B C    1 
ATOM   5374 O O    . VAL B 1 395 ? 128.78200 91.71800  90.45800  1.000 44.44797  ? 395 VAL B O    1 
ATOM   5375 C CB   . VAL B 1 395 ? 127.35600 93.54100  88.08000  1.000 39.00463  ? 395 VAL B CB   1 
ATOM   5376 C CG1  . VAL B 1 395 ? 127.13400 94.16800  89.44800  1.000 33.59125  ? 395 VAL B CG1  1 
ATOM   5377 C CG2  . VAL B 1 395 ? 127.84500 94.58200  87.09500  1.000 40.61965  ? 395 VAL B CG2  1 
ATOM   5378 N N    . LYS B 1 396 ? 127.13900 90.63000  89.37800  1.000 45.16298  ? 396 LYS B N    1 
ATOM   5379 C CA   . LYS B 1 396 ? 126.81800 89.84200  90.56600  1.000 41.32081  ? 396 LYS B CA   1 
ATOM   5380 C C    . LYS B 1 396 ? 127.97900 88.95600  91.00900  1.000 43.36075  ? 396 LYS B C    1 
ATOM   5381 O O    . LYS B 1 396 ? 128.26800 88.85800  92.20700  1.000 44.16426  ? 396 LYS B O    1 
ATOM   5382 C CB   . LYS B 1 396 ? 125.57800 88.98700  90.31700  1.000 42.78229  ? 396 LYS B CB   1 
ATOM   5383 C CG   . LYS B 1 396 ? 124.91500 88.50300  91.59600  1.000 47.34496  ? 396 LYS B CG   1 
ATOM   5384 C CD   . LYS B 1 396 ? 123.75800 87.56400  91.30500  1.000 45.33648  ? 396 LYS B CD   1 
ATOM   5385 C CE   . LYS B 1 396 ? 124.06600 86.67000  90.12100  1.000 45.03363  ? 396 LYS B CE   1 
ATOM   5386 N NZ   . LYS B 1 396 ? 125.19200 85.74300  90.41000  1.000 46.94738  ? 396 LYS B NZ   1 
ATOM   5387 N N    . LYS B 1 397 ? 128.65900 88.30700  90.06800  1.000 49.38988  ? 397 LYS B N    1 
ATOM   5388 C CA   . LYS B 1 397 ? 129.75500 87.40600  90.40500  1.000 47.69478  ? 397 LYS B CA   1 
ATOM   5389 C C    . LYS B 1 397 ? 131.11500 88.08800  90.52600  1.000 49.58836  ? 397 LYS B C    1 
ATOM   5390 O O    . LYS B 1 397 ? 132.11000 87.40400  90.78200  1.000 49.71990  ? 397 LYS B O    1 
ATOM   5391 C CB   . LYS B 1 397 ? 129.81800 86.27000  89.38700  1.000 49.36454  ? 397 LYS B CB   1 
ATOM   5392 C CG   . LYS B 1 397 ? 128.76300 85.20100  89.60400  1.000 51.18558  ? 397 LYS B CG   1 
ATOM   5393 C CD   . LYS B 1 397 ? 127.89200 85.01300  88.37700  1.000 54.27328  ? 397 LYS B CD   1 
ATOM   5394 C CE   . LYS B 1 397 ? 127.18700 83.66700  88.41500  1.000 52.56098  ? 397 LYS B CE   1 
ATOM   5395 N NZ   . LYS B 1 397 ? 126.78900 83.21100  87.05700  1.000 51.98978  ? 397 LYS B NZ   1 
ATOM   5396 N N    . MET B 1 398 ? 131.18400 89.40500  90.36200  1.000 56.10535  ? 398 MET B N    1 
ATOM   5397 C CA   . MET B 1 398 ? 132.42600 90.17200  90.47300  1.000 52.83542  ? 398 MET B CA   1 
ATOM   5398 C C    . MET B 1 398 ? 133.56100 89.63500  89.59200  1.000 53.51120  ? 398 MET B C    1 
ATOM   5399 O O    . MET B 1 398 ? 134.60300 89.19500  90.08000  1.000 54.99955  ? 398 MET B O    1 
ATOM   5400 C CB   . MET B 1 398 ? 132.87100 90.23200  91.93800  1.000 46.33999  ? 398 MET B CB   1 
ATOM   5401 C CG   . MET B 1 398 ? 132.09900 91.23000  92.78700  1.000 50.84963  ? 398 MET B CG   1 
ATOM   5402 S SD   . MET B 1 398 ? 132.06900 90.78500  94.53500  1.000 63.10781  ? 398 MET B SD   1 
ATOM   5403 C CE   . MET B 1 398 ? 133.01400 92.11800  95.26100  1.000 52.12462  ? 398 MET B CE   1 
ATOM   5404 N N    . GLU B 1 399 ? 133.35000 89.67800  88.27300  1.000 54.92062  ? 399 GLU B N    1 
ATOM   5405 C CA   . GLU B 1 399 ? 134.38000 89.28100  87.31700  1.000 55.14968  ? 399 GLU B CA   1 
ATOM   5406 C C    . GLU B 1 399 ? 134.52700 90.35100  86.24500  1.000 59.31793  ? 399 GLU B C    1 
ATOM   5407 O O    . GLU B 1 399 ? 133.53800 90.94200  85.80100  1.000 63.45248  ? 399 GLU B O    1 
ATOM   5408 C CB   . GLU B 1 399 ? 134.12700 87.94100  86.60700  1.000 55.88202  ? 399 GLU B CB   1 
ATOM   5409 C CG   . GLU B 1 399 ? 134.01600 86.70500  87.46900  1.000 59.30929  ? 399 GLU B CG   1 
ATOM   5410 C CD   . GLU B 1 399 ? 132.84100 85.84000  87.06900  1.000 64.06270  ? 399 GLU B CD   1 
ATOM   5411 O OE1  . GLU B 1 399 ? 132.95800 85.12100  86.05400  1.000 63.71392  ? 399 GLU B OE1  1 
ATOM   5412 O OE2  . GLU B 1 399 ? 131.80800 85.86900  87.75800  1.000 60.59612  ? 399 GLU B OE2  1 
ATOM   5413 N N    . LYS B 1 400 ? 135.76900 90.58600  85.83200  1.000 56.57308  ? 400 LYS B N    1 
ATOM   5414 C CA   . LYS B 1 400 ? 136.07300 91.52500  84.76400  1.000 55.14523  ? 400 LYS B CA   1 
ATOM   5415 C C    . LYS B 1 400 ? 135.50800 91.04900  83.42600  1.000 55.41450  ? 400 LYS B C    1 
ATOM   5416 O O    . LYS B 1 400 ? 135.21700 89.86800  83.22200  1.000 58.51335  ? 400 LYS B O    1 
ATOM   5417 C CB   . LYS B 1 400 ? 137.58300 91.73400  84.65000  1.000 54.48275  ? 400 LYS B CB   1 
ATOM   5418 C CG   . LYS B 1 400 ? 138.13600 92.76200  85.62000  1.000 55.77159  ? 400 LYS B CG   1 
ATOM   5419 C CD   . LYS B 1 400 ? 139.64800 92.69000  85.70000  1.000 57.58994  ? 400 LYS B CD   1 
ATOM   5420 C CE   . LYS B 1 400 ? 140.13700 92.94900  87.11300  1.000 57.80789  ? 400 LYS B CE   1 
ATOM   5421 N NZ   . LYS B 1 400 ? 140.72300 94.31100  87.25400  1.000 57.28633  ? 400 LYS B NZ   1 
ATOM   5422 N N    . LEU B 1 401 ? 135.35200 92.00000  82.50800  1.000 57.61328  ? 401 LEU B N    1 
ATOM   5423 C CA   . LEU B 1 401 ? 134.90900 91.68900  81.15600  1.000 57.71860  ? 401 LEU B CA   1 
ATOM   5424 C C    . LEU B 1 401 ? 136.01700 91.00200  80.36800  1.000 58.56392  ? 401 LEU B C    1 
ATOM   5425 O O    . LEU B 1 401 ? 137.18500 91.39600  80.43300  1.000 57.05110  ? 401 LEU B O    1 
ATOM   5426 C CB   . LEU B 1 401 ? 134.47900 92.96400  80.42900  1.000 58.17600  ? 401 LEU B CB   1 
ATOM   5427 C CG   . LEU B 1 401 ? 133.15600 93.61900  80.82300  1.000 55.34042  ? 401 LEU B CG   1 
ATOM   5428 C CD1  . LEU B 1 401 ? 132.73900 94.62200  79.76400  1.000 54.52129  ? 401 LEU B CD1  1 
ATOM   5429 C CD2  . LEU B 1 401 ? 132.07700 92.57300  81.02100  1.000 56.46073  ? 401 LEU B CD2  1 
ATOM   5430 N N    . GLY B 1 402 ? 135.64400 89.96100  79.61900  1.000 67.09309  ? 402 GLY B N    1 
ATOM   5431 C CA   . GLY B 1 402 ? 136.58700 89.26300  78.79400  1.000 66.44778  ? 402 GLY B CA   1 
ATOM   5432 C C    . GLY B 1 402 ? 136.98800 90.07300  77.57300  1.000 70.13185  ? 402 GLY B C    1 
ATOM   5433 O O    . GLY B 1 402 ? 136.58900 91.23200  77.40200  1.000 70.23370  ? 402 GLY B O    1 
ATOM   5434 N N    . PRO B 1 403 ? 137.79700 89.45700  76.70600  1.000 79.85714  ? 403 PRO B N    1 
ATOM   5435 C CA   . PRO B 1 403 ? 138.30700 90.20000  75.54100  1.000 79.35013  ? 403 PRO B CA   1 
ATOM   5436 C C    . PRO B 1 403 ? 137.26900 90.47100  74.46400  1.000 78.22629  ? 403 PRO B C    1 
ATOM   5437 O O    . PRO B 1 403 ? 137.25500 91.56800  73.89200  1.000 77.05377  ? 403 PRO B O    1 
ATOM   5438 C CB   . PRO B 1 403 ? 139.43400 89.29400  75.02900  1.000 78.20926  ? 403 PRO B CB   1 
ATOM   5439 C CG   . PRO B 1 403 ? 139.01700 87.91800  75.43400  1.000 77.88721  ? 403 PRO B CG   1 
ATOM   5440 C CD   . PRO B 1 403 ? 138.26100 88.05900  76.73000  1.000 77.35622  ? 403 PRO B CD   1 
ATOM   5441 N N    . VAL B 1 404 ? 136.40300 89.50100  74.16300  1.000 76.24201  ? 404 VAL B N    1 
ATOM   5442 C CA   . VAL B 1 404 ? 135.42900 89.66900  73.08900  1.000 76.46738  ? 404 VAL B CA   1 
ATOM   5443 C C    . VAL B 1 404 ? 134.52700 90.86500  73.35900  1.000 77.46258  ? 404 VAL B C    1 
ATOM   5444 O O    . VAL B 1 404 ? 134.00600 91.04100  74.46800  1.000 75.91029  ? 404 VAL B O    1 
ATOM   5445 C CB   . VAL B 1 404 ? 134.61500 88.37800  72.91000  1.000 77.27385  ? 404 VAL B CB   1 
ATOM   5446 C CG1  . VAL B 1 404 ? 133.47500 88.32300  73.91100  1.000 77.04390  ? 404 VAL B CG1  1 
ATOM   5447 C CG2  . VAL B 1 404 ? 134.08400 88.27400  71.48700  1.000 75.78820  ? 404 VAL B CG2  1 
ATOM   5448 N N    . ASP B 1 405 ? 134.35500 91.70700  72.34000  1.000 69.31725  ? 405 ASP B N    1 
ATOM   5449 C CA   . ASP B 1 405 ? 133.49300 92.88000  72.44100  1.000 70.36827  ? 405 ASP B CA   1 
ATOM   5450 C C    . ASP B 1 405 ? 132.03000 92.44600  72.47000  1.000 70.42722  ? 405 ASP B C    1 
ATOM   5451 O O    . ASP B 1 405 ? 131.56200 91.75900  71.55600  1.000 67.64223  ? 405 ASP B O    1 
ATOM   5452 C CB   . ASP B 1 405 ? 133.75500 93.82700  71.27400  1.000 68.84471  ? 405 ASP B CB   1 
ATOM   5453 C CG   . ASP B 1 405 ? 133.11400 95.18300  71.47100  1.000 70.99278  ? 405 ASP B CG   1 
ATOM   5454 O OD1  . ASP B 1 405 ? 132.58100 95.43200  72.57300  1.000 71.11801  ? 405 ASP B OD1  1 
ATOM   5455 O OD2  . ASP B 1 405 ? 133.14200 96.00000  70.52700  1.000 69.13074  ? 405 ASP B OD2  1 
ATOM   5456 N N    . LEU B 1 406 ? 131.30800 92.84000  73.51900  1.000 61.31087  ? 406 LEU B N    1 
ATOM   5457 C CA   . LEU B 1 406 ? 129.91400 92.44600  73.68700  1.000 59.77974  ? 406 LEU B CA   1 
ATOM   5458 C C    . LEU B 1 406 ? 128.93400 93.25100  72.83900  1.000 61.79097  ? 406 LEU B C    1 
ATOM   5459 O O    . LEU B 1 406 ? 127.77400 92.84300  72.72000  1.000 60.76444  ? 406 LEU B O    1 
ATOM   5460 C CB   . LEU B 1 406 ? 129.51000 92.57200  75.15800  1.000 61.60574  ? 406 LEU B CB   1 
ATOM   5461 C CG   . LEU B 1 406 ? 130.54200 92.20100  76.22300  1.000 62.15001  ? 406 LEU B CG   1 
ATOM   5462 C CD1  . LEU B 1 406 ? 130.04800 92.61900  77.59600  1.000 59.27192  ? 406 LEU B CD1  1 
ATOM   5463 C CD2  . LEU B 1 406 ? 130.83100 90.71000  76.18800  1.000 62.73935  ? 406 LEU B CD2  1 
ATOM   5464 N N    . LEU B 1 407 ? 129.35900 94.36800  72.25300  1.000 55.73370  ? 407 LEU B N    1 
ATOM   5465 C CA   . LEU B 1 407 ? 128.48000 95.23600  71.47800  1.000 52.05958  ? 407 LEU B CA   1 
ATOM   5466 C C    . LEU B 1 407 ? 128.50500 94.96400  69.97500  1.000 54.21713  ? 407 LEU B C    1 
ATOM   5467 O O    . LEU B 1 407 ? 127.90600 95.73100  69.21500  1.000 59.43608  ? 407 LEU B O    1 
ATOM   5468 C CB   . LEU B 1 407 ? 128.84600 96.70000  71.73700  1.000 51.78987  ? 407 LEU B CB   1 
ATOM   5469 C CG   . LEU B 1 407 ? 128.46800 97.27400  73.10500  1.000 51.50695  ? 407 LEU B CG   1 
ATOM   5470 C CD1  . LEU B 1 407 ? 129.03900 98.67200  73.28400  1.000 48.42621  ? 407 LEU B CD1  1 
ATOM   5471 C CD2  . LEU B 1 407 ? 126.96500 97.27900  73.30100  1.000 53.82033  ? 407 LEU B CD2  1 
ATOM   5472 N N    . PHE B 1 408 ? 129.17300 93.90200  69.52600  1.000 57.18159  ? 408 PHE B N    1 
ATOM   5473 C CA   . PHE B 1 408 ? 129.29700 93.65200  68.09000  1.000 58.35460  ? 408 PHE B CA   1 
ATOM   5474 C C    . PHE B 1 408 ? 127.97300 93.21800  67.46000  1.000 61.13821  ? 408 PHE B C    1 
ATOM   5475 O O    . PHE B 1 408 ? 127.54000 93.78300  66.44500  1.000 61.31491  ? 408 PHE B O    1 
ATOM   5476 C CB   . PHE B 1 408 ? 130.38100 92.60000  67.84800  1.000 59.57621  ? 408 PHE B CB   1 
ATOM   5477 C CG   . PHE B 1 408 ? 130.56900 92.23900  66.40300  1.000 59.94228  ? 408 PHE B CG   1 
ATOM   5478 C CD1  . PHE B 1 408 ? 131.21400 93.10500  65.53800  1.000 60.20951  ? 408 PHE B CD1  1 
ATOM   5479 C CD2  . PHE B 1 408 ? 130.10700 91.03100  65.91000  1.000 59.23695  ? 408 PHE B CD2  1 
ATOM   5480 C CE1  . PHE B 1 408 ? 131.39000 92.77700  64.20800  1.000 60.54642  ? 408 PHE B CE1  1 
ATOM   5481 C CE2  . PHE B 1 408 ? 130.28100 90.69700  64.58000  1.000 59.08514  ? 408 PHE B CE2  1 
ATOM   5482 C CZ   . PHE B 1 408 ? 130.92300 91.57100  63.72900  1.000 60.56656  ? 408 PHE B CZ   1 
ATOM   5483 N N    . GLU B 1 409 ? 127.29900 92.23800  68.06700  1.000 59.95637  ? 409 GLU B N    1 
ATOM   5484 C CA   . GLU B 1 409 ? 126.03800 91.74600  67.51600  1.000 60.78727  ? 409 GLU B CA   1 
ATOM   5485 C C    . GLU B 1 409 ? 124.92200 92.78300  67.58400  1.000 61.10900  ? 409 GLU B C    1 
ATOM   5486 O O    . GLU B 1 409 ? 124.09400 92.86200  66.66600  1.000 64.05363  ? 409 GLU B O    1 
ATOM   5487 C CB   . GLU B 1 409 ? 125.61700 90.47300  68.24600  1.000 58.65675  ? 409 GLU B CB   1 
ATOM   5488 C CG   . GLU B 1 409 ? 126.28700 89.20700  67.73200  1.000 62.73352  ? 409 GLU B CG   1 
ATOM   5489 C CD   . GLU B 1 409 ? 126.33800 89.13700  66.21700  1.000 69.31363  ? 409 GLU B CD   1 
ATOM   5490 O OE1  . GLU B 1 409 ? 125.27900 88.92100  65.59100  1.000 69.29548  ? 409 GLU B OE1  1 
ATOM   5491 O OE2  . GLU B 1 409 ? 127.44100 89.29400  65.65100  1.000 63.16280  ? 409 GLU B OE2  1 
ATOM   5492 N N    . VAL B 1 410 ? 124.90700 93.61900  68.62300  1.000 52.09835  ? 410 VAL B N    1 
ATOM   5493 C CA   . VAL B 1 410 ? 123.86900 94.63900  68.71600  1.000 49.24185  ? 410 VAL B CA   1 
ATOM   5494 C C    . VAL B 1 410 ? 124.07200 95.70400  67.64600  1.000 49.45688  ? 410 VAL B C    1 
ATOM   5495 O O    . VAL B 1 410 ? 123.11000 96.15300  67.00700  1.000 50.27529  ? 410 VAL B O    1 
ATOM   5496 C CB   . VAL B 1 410 ? 123.83400 95.23800  70.13600  1.000 47.50023  ? 410 VAL B CB   1 
ATOM   5497 C CG1  . VAL B 1 410 ? 125.13800 95.94500  70.46700  1.000 50.24468  ? 410 VAL B CG1  1 
ATOM   5498 C CG2  . VAL B 1 410 ? 122.65300 96.18200  70.28700  1.000 48.96042  ? 410 VAL B CG2  1 
ATOM   5499 N N    . HIS B 1 411 ? 125.32100 96.10900  67.41000  1.000 48.59437  ? 411 HIS B N    1 
ATOM   5500 C CA   . HIS B 1 411 ? 125.56700 97.08300  66.35500  1.000 50.48481  ? 411 HIS B CA   1 
ATOM   5501 C C    . HIS B 1 411 ? 125.26700 96.49300  64.98200  1.000 53.80571  ? 411 HIS B C    1 
ATOM   5502 O O    . HIS B 1 411 ? 124.76500 97.20200  64.09800  1.000 56.95050  ? 411 HIS B O    1 
ATOM   5503 C CB   . HIS B 1 411 ? 127.01400 97.56900  66.43000  1.000 48.04882  ? 411 HIS B CB   1 
ATOM   5504 C CG   . HIS B 1 411 ? 127.30300 98.42000  67.62700  1.000 52.51600  ? 411 HIS B CG   1 
ATOM   5505 N ND1  . HIS B 1 411 ? 128.58400 98.73200  68.02800  1.000 52.52492  ? 411 HIS B ND1  1 
ATOM   5506 C CD2  . HIS B 1 411 ? 126.47600 99.01300  68.52000  1.000 52.28632  ? 411 HIS B CD2  1 
ATOM   5507 C CE1  . HIS B 1 411 ? 128.53400 99.48700  69.11100  1.000 50.26686  ? 411 HIS B CE1  1 
ATOM   5508 N NE2  . HIS B 1 411 ? 127.26600 99.67200  69.43100  1.000 50.46515  ? 411 HIS B NE2  1 
ATOM   5509 N N    . LEU B 1 412 ? 125.51200 95.19100  64.79900  1.000 54.98749  ? 412 LEU B N    1 
ATOM   5510 C CA   . LEU B 1 412 ? 125.16800 94.56300  63.52700  1.000 58.75391  ? 412 LEU B CA   1 
ATOM   5511 C C    . LEU B 1 412 ? 123.65900 94.56600  63.31400  1.000 61.70628  ? 412 LEU B C    1 
ATOM   5512 O O    . LEU B 1 412 ? 123.17300 94.87900  62.21500  1.000 62.13500  ? 412 LEU B O    1 
ATOM   5513 C CB   . LEU B 1 412 ? 125.71900 93.13700  63.48200  1.000 60.76407  ? 412 LEU B CB   1 
ATOM   5514 C CG   . LEU B 1 412 ? 125.39600 92.29300  62.24800  1.000 61.54295  ? 412 LEU B CG   1 
ATOM   5515 C CD1  . LEU B 1 412 ? 126.00200 92.91400  61.00000  1.000 61.39340  ? 412 LEU B CD1  1 
ATOM   5516 C CD2  . LEU B 1 412 ? 125.87500 90.86100  62.43100  1.000 58.13808  ? 412 LEU B CD2  1 
ATOM   5517 N N    . ALA B 1 413 ? 122.89600 94.29500  64.37800  1.000 56.51634  ? 413 ALA B N    1 
ATOM   5518 C CA   . ALA B 1 413 ? 121.44800 94.24600  64.22200  1.000 55.29386  ? 413 ALA B CA   1 
ATOM   5519 C C    . ALA B 1 413 ? 120.88800 95.64200  64.00900  1.000 59.76895  ? 413 ALA B C    1 
ATOM   5520 O O    . ALA B 1 413 ? 119.89300 95.81200  63.29300  1.000 58.44840  ? 413 ALA B O    1 
ATOM   5521 C CB   . ALA B 1 413 ? 120.80500 93.58600  65.44100  1.000 52.21450  ? 413 ALA B CB   1 
ATOM   5522 N N    . ALA B 1 414 ? 121.55100 96.66000  64.55900  1.000 59.30680  ? 414 ALA B N    1 
ATOM   5523 C CA   . ALA B 1 414 ? 121.03700 98.01100  64.39400  1.000 52.73122  ? 414 ALA B CA   1 
ATOM   5524 C C    . ALA B 1 414 ? 121.32400 98.51600  62.98700  1.000 55.01571  ? 414 ALA B C    1 
ATOM   5525 O O    . ALA B 1 414 ? 120.48800 99.19900  62.38500  1.000 56.68293  ? 414 ALA B O    1 
ATOM   5526 C CB   . ALA B 1 414 ? 121.64300 98.94400  65.44100  1.000 49.80494  ? 414 ALA B CB   1 
ATOM   5527 N N    . GLU B 1 415 ? 122.50700 98.20100  62.45000  1.000 58.51445  ? 415 GLU B N    1 
ATOM   5528 C CA   . GLU B 1 415 ? 122.78300 98.53900  61.05700  1.000 58.36195  ? 415 GLU B CA   1 
ATOM   5529 C C    . GLU B 1 415 ? 121.81500 97.82800  60.11500  1.000 61.79886  ? 415 GLU B C    1 
ATOM   5530 O O    . GLU B 1 415 ? 121.37600 98.40200  59.10800  1.000 64.07695  ? 415 GLU B O    1 
ATOM   5531 C CB   . GLU B 1 415 ? 124.22800 98.19100  60.70600  1.000 59.60057  ? 415 GLU B CB   1 
ATOM   5532 C CG   . GLU B 1 415 ? 125.25000 99.16500  61.26300  1.000 63.07693  ? 415 GLU B CG   1 
ATOM   5533 C CD   . GLU B 1 415 ? 126.66100 98.61700  61.21600  1.000 67.55359  ? 415 GLU B CD   1 
ATOM   5534 O OE1  . GLU B 1 415 ? 127.07000 98.10800  60.15100  1.000 67.53351  ? 415 GLU B OE1  1 
ATOM   5535 O OE2  . GLU B 1 415 ? 127.36300 98.69000  62.24600  1.000 66.92990  ? 415 GLU B OE2  1 
ATOM   5536 N N    . GLU B 1 416 ? 121.44000 96.58700  60.44400  1.000 60.84422  ? 416 GLU B N    1 
ATOM   5537 C CA   . GLU B 1 416 ? 120.46600 95.88700  59.60800  1.000 58.61448  ? 416 GLU B CA   1 
ATOM   5538 C C    . GLU B 1 416 ? 119.09300 96.54700  59.67800  1.000 62.00758  ? 416 GLU B C    1 
ATOM   5539 O O    . GLU B 1 416 ? 118.41000 96.68900  58.65400  1.000 63.05389  ? 416 GLU B O    1 
ATOM   5540 C CB   . GLU B 1 416 ? 120.37400 94.42100  60.02900  1.000 59.63055  ? 416 GLU B CB   1 
ATOM   5541 C CG   . GLU B 1 416 ? 121.24000 93.48500  59.20800  1.000 62.08809  ? 416 GLU B CG   1 
ATOM   5542 C CD   . GLU B 1 416 ? 121.22000 92.06400  59.73500  1.000 65.69074  ? 416 GLU B CD   1 
ATOM   5543 O OE1  . GLU B 1 416 ? 120.56100 91.82100  60.76800  1.000 66.77812  ? 416 GLU B OE1  1 
ATOM   5544 O OE2  . GLU B 1 416 ? 121.86400 91.19000  59.12100  1.000 63.88751  ? 416 GLU B OE2  1 
ATOM   5545 N N    . LEU B 1 417 ? 118.67200 96.95300  60.87800  1.000 60.64326  ? 417 LEU B N    1 
ATOM   5546 C CA   . LEU B 1 417 ? 117.45400 97.74700  61.01500  1.000 56.20633  ? 417 LEU B CA   1 
ATOM   5547 C C    . LEU B 1 417 ? 117.49900 98.99200  60.13700  1.000 56.04766  ? 417 LEU B C    1 
ATOM   5548 O O    . LEU B 1 417 ? 116.54200 99.29500  59.41700  1.000 52.12586  ? 417 LEU B O    1 
ATOM   5549 C CB   . LEU B 1 417 ? 117.23600 98.13000  62.47900  1.000 56.85961  ? 417 LEU B CB   1 
ATOM   5550 C CG   . LEU B 1 417 ? 115.89000 98.79000  62.79100  1.000 54.66382  ? 417 LEU B CG   1 
ATOM   5551 C CD1  . LEU B 1 417 ? 114.73800 97.92500  62.30500  1.000 55.79525  ? 417 LEU B CD1  1 
ATOM   5552 C CD2  . LEU B 1 417 ? 115.76000 99.07200  64.28100  1.000 53.51240  ? 417 LEU B CD2  1 
ATOM   5553 N N    . GLN B 1 418 ? 118.57800 99.76800  60.25000  1.000 65.64611  ? 418 GLN B N    1 
ATOM   5554 C CA   . GLN B 1 418 ? 118.73100 100.97000 59.43500  1.000 65.45983  ? 418 GLN B CA   1 
ATOM   5555 C C    . GLN B 1 418 ? 118.57800 100.67300 57.94600  1.000 65.86350  ? 418 GLN B C    1 
ATOM   5556 O O    . GLN B 1 418 ? 117.88300 101.39700 57.22500  1.000 67.62250  ? 418 GLN B O    1 
ATOM   5557 C CB   . GLN B 1 418 ? 120.08800 101.61700 59.71200  1.000 63.56473  ? 418 GLN B CB   1 
ATOM   5558 C CG   . GLN B 1 418 ? 120.16700 103.08500 59.33000  1.000 66.00505  ? 418 GLN B CG   1 
ATOM   5559 C CD   . GLN B 1 418 ? 118.97600 103.88000 59.81700  1.000 69.22074  ? 418 GLN B CD   1 
ATOM   5560 O OE1  . GLN B 1 418 ? 118.85800 104.17700 61.00500  1.000 71.12041  ? 418 GLN B OE1  1 
ATOM   5561 N NE2  . GLN B 1 418 ? 118.08500 104.23500 58.89800  1.000 66.28073  ? 418 GLN B NE2  1 
ATOM   5562 N N    . HIS B 1 419 ? 119.22200 99.60700  57.46500  1.000 71.01679  ? 419 HIS B N    1 
ATOM   5563 C CA   . HIS B 1 419 ? 119.10500 99.27100  56.04800  1.000 71.03616  ? 419 HIS B CA   1 
ATOM   5564 C C    . HIS B 1 419 ? 117.67000 98.91300  55.66900  1.000 70.00541  ? 419 HIS B C    1 
ATOM   5565 O O    . HIS B 1 419 ? 117.16700 99.34500  54.62000  1.000 68.06747  ? 419 HIS B O    1 
ATOM   5566 C CB   . HIS B 1 419 ? 120.05000 98.12100  55.70200  1.000 72.08906  ? 419 HIS B CB   1 
ATOM   5567 C CG   . HIS B 1 419 ? 121.48100 98.53700  55.56400  1.000 71.91268  ? 419 HIS B CG   1 
ATOM   5568 N ND1  . HIS B 1 419 ? 121.85900 99.70900  54.94500  1.000 73.37632  ? 419 HIS B ND1  1 
ATOM   5569 C CD2  . HIS B 1 419 ? 122.62700 97.93700  55.96400  1.000 71.30192  ? 419 HIS B CD2  1 
ATOM   5570 C CE1  . HIS B 1 419 ? 123.17600 99.81300  54.97100  1.000 74.08777  ? 419 HIS B CE1  1 
ATOM   5571 N NE2  . HIS B 1 419 ? 123.66600 98.75000  55.58400  1.000 72.99916  ? 419 HIS B NE2  1 
ATOM   5572 N N    . LYS B 1 420 ? 116.98700 98.14200  56.51800  1.000 69.86067  ? 420 LYS B N    1 
ATOM   5573 C CA   . LYS B 1 420 ? 115.59800 97.79500  56.22900  1.000 69.13355  ? 420 LYS B CA   1 
ATOM   5574 C C    . LYS B 1 420 ? 114.71000 99.03200  56.19400  1.000 70.52756  ? 420 LYS B C    1 
ATOM   5575 O O    . LYS B 1 420 ? 113.81700 99.13900  55.34600  1.000 69.55172  ? 420 LYS B O    1 
ATOM   5576 C CB   . LYS B 1 420 ? 115.07700 96.79100  57.25600  1.000 71.09287  ? 420 LYS B CB   1 
ATOM   5577 C CG   . LYS B 1 420 ? 113.71400 96.21700  56.91200  1.000 70.72401  ? 420 LYS B CG   1 
ATOM   5578 C CD   . LYS B 1 420 ? 113.75900 95.42300  55.61900  1.000 70.63546  ? 420 LYS B CD   1 
ATOM   5579 C CE   . LYS B 1 420 ? 112.47400 94.64100  55.40700  1.000 70.77371  ? 420 LYS B CE   1 
ATOM   5580 N NZ   . LYS B 1 420 ? 112.22800 94.36400  53.96600  1.000 69.99496  ? 420 LYS B NZ   1 
ATOM   5581 N N    . ILE B 1 421 ? 114.94000 99.98000  57.10400  1.000 72.39692  ? 421 ILE B N    1 
ATOM   5582 C CA   . ILE B 1 421 ? 114.16600 101.21800 57.08300  1.000 71.48751  ? 421 ILE B CA   1 
ATOM   5583 C C    . ILE B 1 421 ? 114.45500 101.99900 55.81100  1.000 70.15485  ? 421 ILE B C    1 
ATOM   5584 O O    . ILE B 1 421 ? 113.55800 102.61400 55.22200  1.000 70.39455  ? 421 ILE B O    1 
ATOM   5585 C CB   . ILE B 1 421 ? 114.44900 102.06300 58.34000  1.000 69.84122  ? 421 ILE B CB   1 
ATOM   5586 C CG1  . ILE B 1 421 ? 114.08500 101.28700 59.60600  1.000 71.69523  ? 421 ILE B CG1  1 
ATOM   5587 C CG2  . ILE B 1 421 ? 113.68800 103.37600 58.28400  1.000 67.91775  ? 421 ILE B CG2  1 
ATOM   5588 C CD1  . ILE B 1 421 ? 114.96800 101.61300 60.79100  1.000 71.56374  ? 421 ILE B CD1  1 
ATOM   5589 N N    . ASP B 1 422 ? 115.71200 101.98600 55.36600  1.000 73.83994  ? 422 ASP B N    1 
ATOM   5590 C CA   . ASP B 1 422 ? 116.07700 102.73700 54.17000  1.000 73.09685  ? 422 ASP B CA   1 
ATOM   5591 C C    . ASP B 1 422 ? 115.39500 102.17300 52.93100  1.000 74.28655  ? 422 ASP B C    1 
ATOM   5592 O O    . ASP B 1 422 ? 114.95700 102.93100 52.05800  1.000 70.28897  ? 422 ASP B O    1 
ATOM   5593 C CB   . ASP B 1 422 ? 117.59500 102.73600 53.99300  1.000 71.75442  ? 422 ASP B CB   1 
ATOM   5594 C CG   . ASP B 1 422 ? 118.24500 103.98700 54.54100  1.000 73.92270  ? 422 ASP B CG   1 
ATOM   5595 O OD1  . ASP B 1 422 ? 117.64700 104.62600 55.43200  1.000 76.24010  ? 422 ASP B OD1  1 
ATOM   5596 O OD2  . ASP B 1 422 ? 119.35500 104.33200 54.08300  1.000 73.17714  ? 422 ASP B OD2  1 
ATOM   5597 N N    . LYS B 1 423 ? 115.30200 100.84400 52.82900  1.000 80.44442  ? 423 LYS B N    1 
ATOM   5598 C CA   . LYS B 1 423 ? 114.70300 100.24900 51.63500  1.000 78.05529  ? 423 LYS B CA   1 
ATOM   5599 C C    . LYS B 1 423 ? 113.20100 100.50500 51.53100  1.000 80.17695  ? 423 LYS B C    1 
ATOM   5600 O O    . LYS B 1 423 ? 112.66000 100.52000 50.42000  1.000 81.26320  ? 423 LYS B O    1 
ATOM   5601 C CB   . LYS B 1 423 ? 114.97600 98.74600  51.60100  1.000 79.32767  ? 423 LYS B CB   1 
ATOM   5602 C CG   . LYS B 1 423 ? 116.39800 98.38100  51.21000  1.000 80.61338  ? 423 LYS B CG   1 
ATOM   5603 C CD   . LYS B 1 423 ? 116.65300 96.89500  51.39900  1.000 81.28716  ? 423 LYS B CD   1 
ATOM   5604 C CE   . LYS B 1 423 ? 115.37100 96.09300  51.25000  1.000 80.96710  ? 423 LYS B CE   1 
ATOM   5605 N NZ   . LYS B 1 423 ? 115.45700 94.77900  51.94600  1.000 79.22346  ? 423 LYS B NZ   1 
ATOM   5606 N N    . LYS B 1 424 ? 112.50800 100.70900 52.65400  1.000 79.72334  ? 424 LYS B N    1 
ATOM   5607 C CA   . LYS B 1 424 ? 111.04900 100.79200 52.65400  1.000 78.00351  ? 424 LYS B CA   1 
ATOM   5608 C C    . LYS B 1 424 ? 110.52500 102.14400 53.13100  1.000 78.65174  ? 424 LYS B C    1 
ATOM   5609 O O    . LYS B 1 424 ? 109.36700 102.24000 53.54900  1.000 77.70170  ? 424 LYS B O    1 
ATOM   5610 C CB   . LYS B 1 424 ? 110.45000 99.67000  53.50400  1.000 77.23891  ? 424 LYS B CB   1 
ATOM   5611 C CG   . LYS B 1 424 ? 111.00000 98.29200  53.18900  1.000 77.99639  ? 424 LYS B CG   1 
ATOM   5612 C CD   . LYS B 1 424 ? 110.00200 97.47500  52.38600  1.000 77.45460  ? 424 LYS B CD   1 
ATOM   5613 C CE   . LYS B 1 424 ? 110.67500 96.77300  51.21900  1.000 77.70657  ? 424 LYS B CE   1 
ATOM   5614 N NZ   . LYS B 1 424 ? 109.68600 96.10700  50.32700  1.000 78.69668  ? 424 LYS B NZ   1 
ATOM   5615 N N    . SER B 1 425 ? 111.34700 103.19300 53.08000  1.000 79.93518  ? 425 SER B N    1 
ATOM   5616 C CA   . SER B 1 425 ? 110.91800 104.50800 53.54400  1.000 79.27642  ? 425 SER B CA   1 
ATOM   5617 C C    . SER B 1 425 ? 109.72800 105.06900 52.77300  1.000 79.60346  ? 425 SER B C    1 
ATOM   5618 O O    . SER B 1 425 ? 109.16900 106.08600 53.19500  1.000 78.06694  ? 425 SER B O    1 
ATOM   5619 C CB   . SER B 1 425 ? 112.08400 105.49300 53.45900  1.000 78.12454  ? 425 SER B CB   1 
ATOM   5620 O OG   . SER B 1 425 ? 112.47700 105.69700 52.11300  1.000 80.66425  ? 425 SER B OG   1 
ATOM   5621 N N    . TYR B 1 426 ? 109.32100 104.44300 51.66700  1.000 79.63981  ? 426 TYR B N    1 
ATOM   5622 C CA   . TYR B 1 426 ? 108.15000 104.91100 50.93300  1.000 77.31749  ? 426 TYR B CA   1 
ATOM   5623 C C    . TYR B 1 426 ? 106.83600 104.65300 51.66200  1.000 76.70927  ? 426 TYR B C    1 
ATOM   5624 O O    . TYR B 1 426 ? 105.79400 105.13200 51.20400  1.000 75.01514  ? 426 TYR B O    1 
ATOM   5625 C CB   . TYR B 1 426 ? 108.14300 104.29200 49.52500  1.000 77.28558  ? 426 TYR B CB   1 
ATOM   5626 C CG   . TYR B 1 426 ? 107.72200 102.83500 49.41500  1.000 79.13475  ? 426 TYR B CG   1 
ATOM   5627 C CD1  . TYR B 1 426 ? 106.44400 102.41600 49.76400  1.000 77.23225  ? 426 TYR B CD1  1 
ATOM   5628 C CD2  . TYR B 1 426 ? 108.61600 101.87700 48.95700  1.000 78.29753  ? 426 TYR B CD2  1 
ATOM   5629 C CE1  . TYR B 1 426 ? 106.07200 101.09200 49.66000  1.000 77.38416  ? 426 TYR B CE1  1 
ATOM   5630 C CE2  . TYR B 1 426 ? 108.25200 100.55000 48.85000  1.000 78.84109  ? 426 TYR B CE2  1 
ATOM   5631 C CZ   . TYR B 1 426 ? 106.97900 100.16300 49.20400  1.000 79.54032  ? 426 TYR B CZ   1 
ATOM   5632 O OH   . TYR B 1 426 ? 106.61100 98.84200  49.09800  1.000 79.14801  ? 426 TYR B OH   1 
ATOM   5633 N N    . LEU B 1 427 ? 106.85300 103.92000 52.77400  1.000 76.54026  ? 427 LEU B N    1 
ATOM   5634 C CA   . LEU B 1 427 ? 105.65700 103.71500 53.58100  1.000 75.76748  ? 427 LEU B CA   1 
ATOM   5635 C C    . LEU B 1 427 ? 105.52700 104.71100 54.72400  1.000 76.95207  ? 427 LEU B C    1 
ATOM   5636 O O    . LEU B 1 427 ? 104.48300 104.73900 55.38400  1.000 75.05852  ? 427 LEU B O    1 
ATOM   5637 C CB   . LEU B 1 427 ? 105.63500 102.29400 54.15500  1.000 76.58752  ? 427 LEU B CB   1 
ATOM   5638 C CG   . LEU B 1 427 ? 105.57700 101.12800 53.17200  1.000 76.10870  ? 427 LEU B CG   1 
ATOM   5639 C CD1  . LEU B 1 427 ? 105.58700 99.81000  53.92200  1.000 74.98162  ? 427 LEU B CD1  1 
ATOM   5640 C CD2  . LEU B 1 427 ? 104.33000 101.24000 52.31500  1.000 76.73110  ? 427 LEU B CD2  1 
ATOM   5641 N N    . LEU B 1 428 ? 106.55200 105.52300 54.97400  1.000 77.75741  ? 428 LEU B N    1 
ATOM   5642 C CA   . LEU B 1 428 ? 106.52200 106.46800 56.08300  1.000 75.24041  ? 428 LEU B CA   1 
ATOM   5643 C C    . LEU B 1 428 ? 105.93500 107.81500 55.69200  1.000 74.23335  ? 428 LEU B C    1 
ATOM   5644 O O    . LEU B 1 428 ? 105.34500 108.49400 56.54000  1.000 75.56089  ? 428 LEU B O    1 
ATOM   5645 C CB   . LEU B 1 428 ? 107.93300 106.66300 56.64100  1.000 76.67151  ? 428 LEU B CB   1 
ATOM   5646 C CG   . LEU B 1 428 ? 108.52900 105.42300 57.30900  1.000 74.44554  ? 428 LEU B CG   1 
ATOM   5647 C CD1  . LEU B 1 428 ? 109.92700 105.70800 57.83300  1.000 73.40617  ? 428 LEU B CD1  1 
ATOM   5648 C CD2  . LEU B 1 428 ? 107.61800 104.91800 58.41600  1.000 73.71324  ? 428 LEU B CD2  1 
ATOM   5649 N N    . VAL B 1 429 ? 106.08000 108.21600 54.43100  1.000 83.27244  ? 429 VAL B N    1 
ATOM   5650 C CA   . VAL B 1 429 ? 105.60500 109.51400 53.96700  1.000 83.24214  ? 429 VAL B CA   1 
ATOM   5651 C C    . VAL B 1 429 ? 104.74200 109.30900 52.73100  1.000 83.45699  ? 429 VAL B C    1 
ATOM   5652 O O    . VAL B 1 429 ? 104.43500 108.17200 52.35600  1.000 83.14266  ? 429 VAL B O    1 
ATOM   5653 C CB   . VAL B 1 429 ? 106.77700 110.46700 53.67000  1.000 83.53189  ? 429 VAL B CB   1 
ATOM   5654 C CG1  . VAL B 1 429 ? 107.66500 110.61900 54.89500  1.000 82.52767  ? 429 VAL B CG1  1 
ATOM   5655 C CG2  . VAL B 1 429 ? 107.57900 109.96500 52.48000  1.000 83.41244  ? 429 VAL B CG2  1 
ATOM   5656 N N    . ASN B 1 430 ? 104.34100 110.40600 52.09200  1.000 94.23012  ? 430 ASN B N    1 
ATOM   5657 C CA   . ASN B 1 430 ? 103.51500 110.35400 50.88900  1.000 93.88402  ? 430 ASN B CA   1 
ATOM   5658 C C    . ASN B 1 430 ? 104.08900 111.34300 49.88500  1.000 94.63335  ? 430 ASN B C    1 
ATOM   5659 O O    . ASN B 1 430 ? 103.93700 112.55700 50.05100  1.000 94.01485  ? 430 ASN B O    1 
ATOM   5660 C CB   . ASN B 1 430 ? 102.05300 110.67200 51.20000  1.000 94.29263  ? 430 ASN B CB   1 
ATOM   5661 C CG   . ASN B 1 430 ? 101.90100 111.81600 52.18100  1.000 96.44943  ? 430 ASN B CG   1 
ATOM   5662 O OD1  . ASN B 1 430 ? 101.86700 112.98300 51.79100  1.000 96.70645  ? 430 ASN B OD1  1 
ATOM   5663 N ND2  . ASN B 1 430 ? 101.80900 111.48800 53.46500  1.000 94.44555  ? 430 ASN B ND2  1 
ATOM   5664 N N    . SER B 1 431 ? 104.74700 110.82300 48.84700  1.000 100.80573 ? 431 SER B N    1 
ATOM   5665 C CA   . SER B 1 431 ? 105.42000 111.67800 47.87800  1.000 102.24709 ? 431 SER B CA   1 
ATOM   5666 C C    . SER B 1 431 ? 104.44300 112.40900 46.96700  1.000 101.90558 ? 431 SER B C    1 
ATOM   5667 O O    . SER B 1 431 ? 104.83700 113.37800 46.30900  1.000 101.82936 ? 431 SER B O    1 
ATOM   5668 C CB   . SER B 1 431 ? 106.39500 110.85300 47.03700  1.000 102.04383 ? 431 SER B CB   1 
ATOM   5669 O OG   . SER B 1 431 ? 105.70700 109.88700 46.26300  1.000 101.81732 ? 431 SER B OG   1 
ATOM   5670 N N    . GLU B 1 432 ? 103.18500 111.96600 46.90700  1.000 102.42228 ? 432 GLU B N    1 
ATOM   5671 C CA   . GLU B 1 432 ? 102.21700 112.61000 46.02600  1.000 102.25808 ? 432 GLU B CA   1 
ATOM   5672 C C    . GLU B 1 432 ? 102.09000 114.09700 46.33300  1.000 102.26377 ? 432 GLU B C    1 
ATOM   5673 O O    . GLU B 1 432 ? 101.91700 114.91400 45.42100  1.000 101.59051 ? 432 GLU B O    1 
ATOM   5674 C CB   . GLU B 1 432 ? 100.85800 111.92000 46.14500  1.000 102.40595 ? 432 GLU B CB   1 
ATOM   5675 C CG   . GLU B 1 432 ? 100.47400 111.54600 47.56600  1.000 102.34613 ? 432 GLU B CG   1 
ATOM   5676 C CD   . GLU B 1 432 ? 100.92000 110.14600 47.94000  1.000 103.20211 ? 432 GLU B CD   1 
ATOM   5677 O OE1  . GLU B 1 432 ? 101.99400 109.71800 47.46600  1.000 103.14883 ? 432 GLU B OE1  1 
ATOM   5678 O OE2  . GLU B 1 432 ? 100.19900 109.47600 48.70800  1.000 103.08121 ? 432 GLU B OE2  1 
ATOM   5679 N N    . CYS B 1 433 ? 102.17700 114.47000 47.61000  1.000 104.15960 ? 433 CYS B N    1 
ATOM   5680 C CA   . CYS B 1 433 ? 102.01100 115.85400 48.03000  1.000 103.70884 ? 433 CYS B CA   1 
ATOM   5681 C C    . CYS B 1 433 ? 103.33100 116.61600 48.08500  1.000 104.33699 ? 433 CYS B C    1 
ATOM   5682 O O    . CYS B 1 433 ? 103.40200 117.66700 48.73100  1.000 104.24120 ? 433 CYS B O    1 
ATOM   5683 C CB   . CYS B 1 433 ? 101.31700 115.90900 49.39300  1.000 103.15783 ? 433 CYS B CB   1 
ATOM   5684 S SG   . CYS B 1 433 ? 100.51800 117.48700 49.76500  1.000 106.42536 ? 433 CYS B SG   1 
ATOM   5685 N N    . TRP B 1 434 ? 104.37100 116.11400 47.42600  1.000 104.62932 ? 434 TRP B N    1 
ATOM   5686 C CA   . TRP B 1 434 ? 105.67700 116.75300 47.49200  1.000 103.75846 ? 434 TRP B CA   1 
ATOM   5687 C C    . TRP B 1 434 ? 105.66200 118.08500 46.75000  1.000 104.18651 ? 434 TRP B C    1 
ATOM   5688 O O    . TRP B 1 434 ? 104.87500 118.30100 45.82500  1.000 104.21781 ? 434 TRP B O    1 
ATOM   5689 C CB   . TRP B 1 434 ? 106.75300 115.83900 46.90700  1.000 103.20667 ? 434 TRP B CB   1 
ATOM   5690 C CG   . TRP B 1 434 ? 107.23700 114.79500 47.86600  1.000 104.22284 ? 434 TRP B CG   1 
ATOM   5691 C CD1  . TRP B 1 434 ? 106.76800 114.55800 49.12500  1.000 103.21105 ? 434 TRP B CD1  1 
ATOM   5692 C CD2  . TRP B 1 434 ? 108.28500 113.84400 47.64400  1.000 104.96549 ? 434 TRP B CD2  1 
ATOM   5693 N NE1  . TRP B 1 434 ? 107.45800 113.52000 49.70100  1.000 102.14809 ? 434 TRP B NE1  1 
ATOM   5694 C CE2  . TRP B 1 434 ? 108.39500 113.06400 48.81200  1.000 103.47398 ? 434 TRP B CE2  1 
ATOM   5695 C CE3  . TRP B 1 434 ? 109.14100 113.57700 46.57100  1.000 104.38488 ? 434 TRP B CE3  1 
ATOM   5696 C CZ2  . TRP B 1 434 ? 109.32600 112.03600 48.93700  1.000 103.09046 ? 434 TRP B CZ2  1 
ATOM   5697 C CZ3  . TRP B 1 434 ? 110.06400 112.55600 46.69800  1.000 103.94405 ? 434 TRP B CZ3  1 
ATOM   5698 C CH2  . TRP B 1 434 ? 110.14900 111.79800 47.87200  1.000 103.65601 ? 434 TRP B CH2  1 
ATOM   5699 N N    . GLU B 1 435 ? 106.54600 118.98400 47.16900  1.000 110.72042 ? 435 GLU B N    1 
ATOM   5700 C CA   . GLU B 1 435 ? 106.66100 120.29500 46.54000  1.000 111.38757 ? 435 GLU B CA   1 
ATOM   5701 C C    . GLU B 1 435 ? 108.06400 120.86600 46.71400  1.000 111.32955 ? 435 GLU B C    1 
ATOM   5702 O O    . GLU B 1 435 ? 108.56500 120.97800 47.83200  1.000 110.71532 ? 435 GLU B O    1 
ATOM   5703 C CB   . GLU B 1 435 ? 105.62400 121.26000 47.11700  1.000 110.81492 ? 435 GLU B CB   1 
ATOM   5704 C CG   . GLU B 1 435 ? 105.45400 122.53700 46.31100  1.000 110.56212 ? 435 GLU B CG   1 
ATOM   5705 C CD   . GLU B 1 435 ? 104.67100 123.59800 47.05800  1.000 111.37658 ? 435 GLU B CD   1 
ATOM   5706 O OE1  . GLU B 1 435 ? 103.46200 123.39200 47.29300  1.000 111.52468 ? 435 GLU B OE1  1 
ATOM   5707 O OE2  . GLU B 1 435 ? 105.26500 124.63900 47.41000  1.000 111.52254 ? 435 GLU B OE2  1 
ATOM   5708 N N    . LYS B 1 527 ? 94.02900  113.60400 54.44100  1.000 104.48078 ? 527 LYS B N    1 
ATOM   5709 C CA   . LYS B 1 527 ? 93.79500  113.84600 55.85900  1.000 105.30340 ? 527 LYS B CA   1 
ATOM   5710 C C    . LYS B 1 527 ? 95.10900  113.87300 56.63100  1.000 105.08336 ? 527 LYS B C    1 
ATOM   5711 O O    . LYS B 1 527 ? 96.11900  113.34000 56.17300  1.000 105.22857 ? 527 LYS B O    1 
ATOM   5712 C CB   . LYS B 1 527 ? 92.86300  112.78100 56.43900  1.000 105.22386 ? 527 LYS B CB   1 
ATOM   5713 C CG   . LYS B 1 527 ? 91.97500  113.28100 57.56600  1.000 104.55299 ? 527 LYS B CG   1 
ATOM   5714 C CD   . LYS B 1 527 ? 90.66800  112.50800 57.62200  1.000 104.53959 ? 527 LYS B CD   1 
ATOM   5715 C CE   . LYS B 1 527 ? 90.83600  111.19100 58.36200  1.000 104.15736 ? 527 LYS B CE   1 
ATOM   5716 N NZ   . LYS B 1 527 ? 89.95300  110.12800 57.80900  1.000 104.48553 ? 527 LYS B NZ   1 
ATOM   5717 N N    . THR B 1 528 ? 95.08900  114.49800 57.80800  1.000 99.58523  ? 528 THR B N    1 
ATOM   5718 C CA   . THR B 1 528 ? 96.27700  114.59400 58.64500  1.000 99.25625  ? 528 THR B CA   1 
ATOM   5719 C C    . THR B 1 528 ? 96.40400  113.44300 59.63200  1.000 99.25347  ? 528 THR B C    1 
ATOM   5720 O O    . THR B 1 528 ? 97.52500  113.11500 60.04400  1.000 99.46290  ? 528 THR B O    1 
ATOM   5721 C CB   . THR B 1 528 ? 96.27500  115.91900 59.41600  1.000 98.93625  ? 528 THR B CB   1 
ATOM   5722 O OG1  . THR B 1 528 ? 95.02300  116.07600 60.09500  1.000 98.95732  ? 528 THR B OG1  1 
ATOM   5723 C CG2  . THR B 1 528 ? 96.47400  117.08700 58.46200  1.000 97.99450  ? 528 THR B CG2  1 
ATOM   5724 N N    . TYR B 1 529 ? 95.29100  112.80300 59.99800  1.000 94.03985  ? 529 TYR B N    1 
ATOM   5725 C CA   . TYR B 1 529 ? 95.35900  111.70100 60.94900  1.000 93.23070  ? 529 TYR B CA   1 
ATOM   5726 C C    . TYR B 1 529 ? 96.05600  110.49300 60.34000  1.000 93.97227  ? 529 TYR B C    1 
ATOM   5727 O O    . TYR B 1 529 ? 96.83800  109.81500 61.01700  1.000 94.06398  ? 529 TYR B O    1 
ATOM   5728 C CB   . TYR B 1 529 ? 93.95500  111.32700 61.42300  1.000 93.51031  ? 529 TYR B CB   1 
ATOM   5729 C CG   . TYR B 1 529 ? 93.94100  110.34000 62.56700  1.000 94.00341  ? 529 TYR B CG   1 
ATOM   5730 C CD1  . TYR B 1 529 ? 94.60700  110.61200 63.75400  1.000 93.64701  ? 529 TYR B CD1  1 
ATOM   5731 C CD2  . TYR B 1 529 ? 93.26500  109.13200 62.45900  1.000 92.93194  ? 529 TYR B CD2  1 
ATOM   5732 C CE1  . TYR B 1 529 ? 94.59800  109.71200 64.80200  1.000 93.68978  ? 529 TYR B CE1  1 
ATOM   5733 C CE2  . TYR B 1 529 ? 93.25100  108.22500 63.50100  1.000 93.92576  ? 529 TYR B CE2  1 
ATOM   5734 C CZ   . TYR B 1 529 ? 93.91900  108.52100 64.67100  1.000 93.56090  ? 529 TYR B CZ   1 
ATOM   5735 O OH   . TYR B 1 529 ? 93.90800  107.62100 65.71100  1.000 92.20927  ? 529 TYR B OH   1 
ATOM   5736 N N    . GLU B 1 530 ? 95.82200  110.23100 59.05300  1.000 92.64262  ? 530 GLU B N    1 
ATOM   5737 C CA   . GLU B 1 530 ? 96.50800  109.11900 58.40600  1.000 92.22648  ? 530 GLU B CA   1 
ATOM   5738 C C    . GLU B 1 530 ? 97.98700  109.42100 58.20400  1.000 91.95088  ? 530 GLU B C    1 
ATOM   5739 O O    . GLU B 1 530 ? 98.82700  108.52400 58.34500  1.000 92.16827  ? 530 GLU B O    1 
ATOM   5740 C CB   . GLU B 1 530 ? 95.84200  108.80000 57.06800  1.000 92.32776  ? 530 GLU B CB   1 
ATOM   5741 C CG   . GLU B 1 530 ? 94.54600  108.01600 57.19300  1.000 93.33516  ? 530 GLU B CG   1 
ATOM   5742 C CD   . GLU B 1 530 ? 94.00000  107.57400 55.85000  1.000 94.61968  ? 530 GLU B CD   1 
ATOM   5743 O OE1  . GLU B 1 530 ? 94.80400  107.39000 54.91100  1.000 93.59082  ? 530 GLU B OE1  1 
ATOM   5744 O OE2  . GLU B 1 530 ? 92.76800  107.41000 55.73200  1.000 93.93390  ? 530 GLU B OE2  1 
ATOM   5745 N N    . SER B 1 531 ? 98.32800  110.68100 57.92600  1.000 85.30811  ? 531 SER B N    1 
ATOM   5746 C CA   . SER B 1 531 ? 99.73400  111.05400 57.82600  1.000 85.33481  ? 531 SER B CA   1 
ATOM   5747 C C    . SER B 1 531 ? 100.44500 110.87200 59.16000  1.000 84.56126  ? 531 SER B C    1 
ATOM   5748 O O    . SER B 1 531 ? 101.57200 110.36500 59.20800  1.000 86.46367  ? 531 SER B O    1 
ATOM   5749 C CB   . SER B 1 531 ? 99.86100  112.49700 57.33900  1.000 84.63098  ? 531 SER B CB   1 
ATOM   5750 O OG   . SER B 1 531 ? 98.86500  112.79800 56.37900  1.000 84.98479  ? 531 SER B OG   1 
ATOM   5751 N N    . ALA B 1 532 ? 99.79500  111.26100 60.26000  1.000 76.36471  ? 532 ALA B N    1 
ATOM   5752 C CA   . ALA B 1 532 ? 100.41900 111.09600 61.56900  1.000 76.91790  ? 532 ALA B CA   1 
ATOM   5753 C C    . ALA B 1 532 ? 100.53000 109.62300 61.94500  1.000 77.86254  ? 532 ALA B C    1 
ATOM   5754 O O    . ALA B 1 532 ? 101.55200 109.18700 62.49300  1.000 79.88061  ? 532 ALA B O    1 
ATOM   5755 C CB   . ALA B 1 532 ? 99.63100  111.86700 62.62600  1.000 76.93955  ? 532 ALA B CB   1 
ATOM   5756 N N    . SER B 1 533 ? 99.49200  108.83700 61.65400  1.000 73.22527  ? 533 SER B N    1 
ATOM   5757 C CA   . SER B 1 533 ? 99.56100  107.40400 61.91200  1.000 72.45725  ? 533 SER B CA   1 
ATOM   5758 C C    . SER B 1 533 ? 100.70800 106.76100 61.14300  1.000 72.96987  ? 533 SER B C    1 
ATOM   5759 O O    . SER B 1 533 ? 101.42300 105.90700 61.68100  1.000 74.55902  ? 533 SER B O    1 
ATOM   5760 C CB   . SER B 1 533 ? 98.23100  106.74500 61.55000  1.000 73.79587  ? 533 SER B CB   1 
ATOM   5761 O OG   . SER B 1 533 ? 98.26900  106.21000 60.24000  1.000 74.73980  ? 533 SER B OG   1 
ATOM   5762 N N    . ALA B 1 534 ? 100.90200 107.15800 59.88400  1.000 70.41257  ? 534 ALA B N    1 
ATOM   5763 C CA   . ALA B 1 534 ? 102.03000 106.64200 59.11400  1.000 71.55215  ? 534 ALA B CA   1 
ATOM   5764 C C    . ALA B 1 534 ? 103.36300 107.06700 59.72100  1.000 71.13877  ? 534 ALA B C    1 
ATOM   5765 O O    . ALA B 1 534 ? 104.27100 106.24500 59.88900  1.000 72.50512  ? 534 ALA B O    1 
ATOM   5766 C CB   . ALA B 1 534 ? 101.92500 107.10700 57.66200  1.000 71.14685  ? 534 ALA B CB   1 
ATOM   5767 N N    . LEU B 1 535 ? 103.50200 108.35000 60.05600  1.000 64.79075  ? 535 LEU B N    1 
ATOM   5768 C CA   . LEU B 1 535 ? 104.74100 108.86300 60.63300  1.000 64.16212  ? 535 LEU B CA   1 
ATOM   5769 C C    . LEU B 1 535 ? 105.00000 108.38700 62.06000  1.000 65.58873  ? 535 LEU B C    1 
ATOM   5770 O O    . LEU B 1 535 ? 106.06600 108.69300 62.60300  1.000 64.47759  ? 535 LEU B O    1 
ATOM   5771 C CB   . LEU B 1 535 ? 104.73400 110.39200 60.59500  1.000 65.68258  ? 535 LEU B CB   1 
ATOM   5772 C CG   . LEU B 1 535 ? 106.10700 111.06400 60.61600  1.000 66.82719  ? 535 LEU B CG   1 
ATOM   5773 C CD1  . LEU B 1 535 ? 106.83900 110.81700 59.30700  1.000 64.92354  ? 535 LEU B CD1  1 
ATOM   5774 C CD2  . LEU B 1 535 ? 105.97200 112.55400 60.88700  1.000 65.80078  ? 535 LEU B CD2  1 
ATOM   5775 N N    . SER B 1 536 ? 104.07000 107.65900 62.67900  1.000 63.13851  ? 536 SER B N    1 
ATOM   5776 C CA   . SER B 1 536 ? 104.28400 107.19200 64.04700  1.000 61.29680  ? 536 SER B CA   1 
ATOM   5777 C C    . SER B 1 536 ? 105.23400 105.99900 64.16200  1.000 62.96613  ? 536 SER B C    1 
ATOM   5778 O O    . SER B 1 536 ? 105.74200 105.74300 65.25800  1.000 64.27647  ? 536 SER B O    1 
ATOM   5779 C CB   . SER B 1 536 ? 102.94300 106.82400 64.68300  1.000 58.35318  ? 536 SER B CB   1 
ATOM   5780 O OG   . SER B 1 536 ? 102.24300 107.98300 65.09400  1.000 60.18150  ? 536 SER B OG   1 
ATOM   5781 N N    . LEU B 1 537 ? 105.48500 105.26400 63.07700  1.000 54.98269  ? 537 LEU B N    1 
ATOM   5782 C CA   . LEU B 1 537 ? 106.38900 104.11500 63.14100  1.000 54.34459  ? 537 LEU B CA   1 
ATOM   5783 C C    . LEU B 1 537 ? 107.85400 104.54500 63.19600  1.000 57.55257  ? 537 LEU B C    1 
ATOM   5784 O O    . LEU B 1 537 ? 108.68100 103.90400 63.86800  1.000 59.21921  ? 537 LEU B O    1 
ATOM   5785 C CB   . LEU B 1 537 ? 106.14000 103.20200 61.93900  1.000 54.94239  ? 537 LEU B CB   1 
ATOM   5786 C CG   . LEU B 1 537 ? 106.74000 101.79600 61.93800  1.000 59.97797  ? 537 LEU B CG   1 
ATOM   5787 C CD1  . LEU B 1 537 ? 105.92200 100.86000 62.80900  1.000 58.23164  ? 537 LEU B CD1  1 
ATOM   5788 C CD2  . LEU B 1 537 ? 106.82100 101.26300 60.51900  1.000 56.45716  ? 537 LEU B CD2  1 
ATOM   5789 N N    . ALA B 1 538 ? 108.19000 105.62800 62.49200  1.000 51.97125  ? 538 ALA B N    1 
ATOM   5790 C CA   . ALA B 1 538 ? 109.55900 106.12400 62.49400  1.000 49.14240  ? 538 ALA B CA   1 
ATOM   5791 C C    . ALA B 1 538 ? 109.99100 106.57600 63.88100  1.000 46.85423  ? 538 ALA B C    1 
ATOM   5792 O O    . ALA B 1 538 ? 111.16400 106.43500 64.23500  1.000 50.11653  ? 538 ALA B O    1 
ATOM   5793 C CB   . ALA B 1 538 ? 109.70300 107.26800 61.49100  1.000 48.83778  ? 538 ALA B CB   1 
ATOM   5794 N N    . THR B 1 539 ? 109.07500 107.13700 64.67100  1.000 40.69000  ? 539 THR B N    1 
ATOM   5795 C CA   . THR B 1 539 ? 109.40900 107.49800 66.04500  1.000 46.76309  ? 539 THR B CA   1 
ATOM   5796 C C    . THR B 1 539 ? 109.87500 106.28200 66.83900  1.000 46.75957  ? 539 THR B C    1 
ATOM   5797 O O    . THR B 1 539 ? 110.90600 106.32400 67.52200  1.000 47.11351  ? 539 THR B O    1 
ATOM   5798 C CB   . THR B 1 539 ? 108.20200 108.14900 66.72200  1.000 46.31854  ? 539 THR B CB   1 
ATOM   5799 O OG1  . THR B 1 539 ? 107.99900 109.46000 66.18200  1.000 49.37020  ? 539 THR B OG1  1 
ATOM   5800 C CG2  . THR B 1 539 ? 108.43000 108.26000 68.21900  1.000 42.05834  ? 539 THR B CG2  1 
ATOM   5801 N N    . PHE B 1 540 ? 109.12000 105.18500 66.75700  1.000 40.18918  ? 540 PHE B N    1 
ATOM   5802 C CA   . PHE B 1 540 ? 109.47700 103.96300 67.47300  1.000 42.23202  ? 540 PHE B CA   1 
ATOM   5803 C C    . PHE B 1 540 ? 110.82900 103.42400 67.00800  1.000 43.07329  ? 540 PHE B C    1 
ATOM   5804 O O    . PHE B 1 540 ? 111.67400 103.03400 67.83100  1.000 42.06703  ? 540 PHE B O    1 
ATOM   5805 C CB   . PHE B 1 540 ? 108.35900 102.93200 67.27400  1.000 38.13541  ? 540 PHE B CB   1 
ATOM   5806 C CG   . PHE B 1 540 ? 108.55200 101.64500 68.02900  1.000 40.88236  ? 540 PHE B CG   1 
ATOM   5807 C CD1  . PHE B 1 540 ? 109.43800 100.68000 67.58300  1.000 43.30392  ? 540 PHE B CD1  1 
ATOM   5808 C CD2  . PHE B 1 540 ? 107.82800 101.39600 69.18300  1.000 41.28234  ? 540 PHE B CD2  1 
ATOM   5809 C CE1  . PHE B 1 540 ? 109.60400 99.49700  68.28000  1.000 43.71485  ? 540 PHE B CE1  1 
ATOM   5810 C CE2  . PHE B 1 540 ? 107.99200 100.21800 69.88300  1.000 41.47545  ? 540 PHE B CE2  1 
ATOM   5811 C CZ   . PHE B 1 540 ? 108.88100 99.26800  69.43100  1.000 41.99487  ? 540 PHE B CZ   1 
ATOM   5812 N N    . ALA B 1 541 ? 111.06100 103.41900 65.69200  1.000 36.51263  ? 541 ALA B N    1 
ATOM   5813 C CA   . ALA B 1 541 ? 112.34200 102.93300 65.18300  1.000 33.80795  ? 541 ALA B CA   1 
ATOM   5814 C C    . ALA B 1 541 ? 113.50700 103.81300 65.63300  1.000 38.81328  ? 541 ALA B C    1 
ATOM   5815 O O    . ALA B 1 541 ? 114.55200 103.30500 66.06700  1.000 41.58574  ? 541 ALA B O    1 
ATOM   5816 C CB   . ALA B 1 541 ? 112.29700 102.84300 63.65800  1.000 34.59301  ? 541 ALA B CB   1 
ATOM   5817 N N    . SER B 1 542 ? 113.34400 105.13600 65.55300  1.000 38.71832  ? 542 SER B N    1 
ATOM   5818 C CA   . SER B 1 542 ? 114.39200 106.04600 66.00100  1.000 35.66130  ? 542 SER B CA   1 
ATOM   5819 C C    . SER B 1 542 ? 114.66200 105.90900 67.49100  1.000 39.38613  ? 542 SER B C    1 
ATOM   5820 O O    . SER B 1 542 ? 115.80800 106.05900 67.92900  1.000 43.23102  ? 542 SER B O    1 
ATOM   5821 C CB   . SER B 1 542 ? 114.01200 107.48800 65.66400  1.000 35.74371  ? 542 SER B CB   1 
ATOM   5822 O OG   . SER B 1 542 ? 114.14200 107.73800 64.27800  1.000 41.19712  ? 542 SER B OG   1 
ATOM   5823 N N    . LEU B 1 543 ? 113.63400 105.60600 68.28300  1.000 36.32971  ? 543 LEU B N    1 
ATOM   5824 C CA   . LEU B 1 543 ? 113.84200 105.45100 69.71800  1.000 35.27274  ? 543 LEU B CA   1 
ATOM   5825 C C    . LEU B 1 543 ? 114.64000 104.18900 70.02100  1.000 37.07058  ? 543 LEU B C    1 
ATOM   5826 O O    . LEU B 1 543 ? 115.56300 104.20800 70.84500  1.000 42.40245  ? 543 LEU B O    1 
ATOM   5827 C CB   . LEU B 1 543 ? 112.49900 105.43700 70.44700  1.000 43.38064  ? 543 LEU B CB   1 
ATOM   5828 C CG   . LEU B 1 543 ? 111.79700 106.79000 70.57600  1.000 45.07256  ? 543 LEU B CG   1 
ATOM   5829 C CD1  . LEU B 1 543 ? 110.41900 106.62600 71.19500  1.000 39.73852  ? 543 LEU B CD1  1 
ATOM   5830 C CD2  . LEU B 1 543 ? 112.64300 107.75600 71.38700  1.000 38.22234  ? 543 LEU B CD2  1 
ATOM   5831 N N    . LEU B 1 544 ? 114.26400 103.06700 69.40200  1.000 40.29778  ? 544 LEU B N    1 
ATOM   5832 C CA   . LEU B 1 544 ? 115.08700 101.86200 69.51300  1.000 37.61791  ? 544 LEU B CA   1 
ATOM   5833 C C    . LEU B 1 544 ? 116.54400 102.13400 69.13100  1.000 38.10402  ? 544 LEU B C    1 
ATOM   5834 O O    . LEU B 1 544 ? 117.48200 101.71300 69.83400  1.000 46.16050  ? 544 LEU B O    1 
ATOM   5835 C CB   . LEU B 1 544 ? 114.49600 100.75700 68.63800  1.000 38.56020  ? 544 LEU B CB   1 
ATOM   5836 C CG   . LEU B 1 544 ? 114.60700 99.32200  69.15000  1.000 43.98225  ? 544 LEU B CG   1 
ATOM   5837 C CD1  . LEU B 1 544 ? 114.09400 99.22900  70.57600  1.000 39.90130  ? 544 LEU B CD1  1 
ATOM   5838 C CD2  . LEU B 1 544 ? 113.83700 98.38100  68.24300  1.000 41.22084  ? 544 LEU B CD2  1 
ATOM   5839 N N    . ILE B 1 545 ? 116.75200 102.86500 68.03300  1.000 29.10471  ? 545 ILE B N    1 
ATOM   5840 C CA   . ILE B 1 545 ? 118.11100 103.16600 67.58600  1.000 30.22968  ? 545 ILE B CA   1 
ATOM   5841 C C    . ILE B 1 545 ? 118.85700 103.99600 68.62600  1.000 33.43412  ? 545 ILE B C    1 
ATOM   5842 O O    . ILE B 1 545 ? 120.04100 103.76100 68.89400  1.000 33.05791  ? 545 ILE B O    1 
ATOM   5843 C CB   . ILE B 1 545 ? 118.07800 103.86900 66.21700  1.000 35.46682  ? 545 ILE B CB   1 
ATOM   5844 C CG1  . ILE B 1 545 ? 117.54600 102.91900 65.14300  1.000 32.97909  ? 545 ILE B CG1  1 
ATOM   5845 C CG2  . ILE B 1 545 ? 119.46400 104.36400 65.83900  1.000 30.68995  ? 545 ILE B CG2  1 
ATOM   5846 C CD1  . ILE B 1 545 ? 118.62200 102.22700 64.35100  1.000 32.39301  ? 545 ILE B CD1  1 
ATOM   5847 N N    . GLU B 1 546 ? 118.19400 105.00500 69.19400  1.000 34.37801  ? 546 GLU B N    1 
ATOM   5848 C CA   . GLU B 1 546 ? 118.81700 105.81400 70.24000  1.000 39.15669  ? 546 GLU B CA   1 
ATOM   5849 C C    . GLU B 1 546 ? 119.19000 104.97900 71.46300  1.000 35.70548  ? 546 GLU B C    1 
ATOM   5850 O O    . GLU B 1 546 ? 120.26400 105.16700 72.04900  1.000 34.03159  ? 546 GLU B O    1 
ATOM   5851 C CB   . GLU B 1 546 ? 117.88400 106.95800 70.63700  1.000 34.46726  ? 546 GLU B CB   1 
ATOM   5852 C CG   . GLU B 1 546 ? 118.31900 107.70100 71.88400  1.000 35.76289  ? 546 GLU B CG   1 
ATOM   5853 C CD   . GLU B 1 546 ? 119.49000 108.62700 71.62700  1.000 43.45950  ? 546 GLU B CD   1 
ATOM   5854 O OE1  . GLU B 1 546 ? 119.70400 109.00600 70.45700  1.000 43.95066  ? 546 GLU B OE1  1 
ATOM   5855 O OE2  . GLU B 1 546 ? 120.19900 108.97100 72.59400  1.000 42.80932  ? 546 GLU B OE2  1 
ATOM   5856 N N    . PHE B 1 547 ? 118.29800 104.08400 71.89000  1.000 24.86727  ? 547 PHE B N    1 
ATOM   5857 C CA   . PHE B 1 547 ? 118.62400 103.16400 72.97900  1.000 29.56782  ? 547 PHE B CA   1 
ATOM   5858 C C    . PHE B 1 547 ? 119.93200 102.42900 72.70200  1.000 29.67222  ? 547 PHE B C    1 
ATOM   5859 O O    . PHE B 1 547 ? 120.82800 102.35400 73.56200  1.000 26.32045  ? 547 PHE B O    1 
ATOM   5860 C CB   . PHE B 1 547 ? 117.47100 102.17700 73.17600  1.000 32.72730  ? 547 PHE B CB   1 
ATOM   5861 C CG   . PHE B 1 547 ? 117.80200 101.01400 74.06900  1.000 33.40144  ? 547 PHE B CG   1 
ATOM   5862 C CD1  . PHE B 1 547 ? 117.69300 101.12900 75.44300  1.000 33.07543  ? 547 PHE B CD1  1 
ATOM   5863 C CD2  . PHE B 1 547 ? 118.21300 99.80600  73.53500  1.000 27.37323  ? 547 PHE B CD2  1 
ATOM   5864 C CE1  . PHE B 1 547 ? 117.99200 100.06300 76.26700  1.000 32.18292  ? 547 PHE B CE1  1 
ATOM   5865 C CE2  . PHE B 1 547 ? 118.51400 98.73900  74.35400  1.000 28.30689  ? 547 PHE B CE2  1 
ATOM   5866 C CZ   . PHE B 1 547 ? 118.40400 98.86800  75.72100  1.000 30.55192  ? 547 PHE B CZ   1 
ATOM   5867 N N    . VAL B 1 548 ? 120.05700 101.87700 71.49500  1.000 31.54018  ? 548 VAL B N    1 
ATOM   5868 C CA   . VAL B 1 548 ? 121.28500 101.16200 71.14900  1.000 28.36439  ? 548 VAL B CA   1 
ATOM   5869 C C    . VAL B 1 548 ? 122.48400 102.10600 71.19200  1.000 27.27639  ? 548 VAL B C    1 
ATOM   5870 O O    . VAL B 1 548 ? 123.53600 101.77800 71.75100  1.000 23.10072  ? 548 VAL B O    1 
ATOM   5871 C CB   . VAL B 1 548 ? 121.14800 100.48400 69.77500  1.000 27.45059  ? 548 VAL B CB   1 
ATOM   5872 C CG1  . VAL B 1 548 ? 122.44700 99.79600  69.39900  1.000 26.86828  ? 548 VAL B CG1  1 
ATOM   5873 C CG2  . VAL B 1 548 ? 120.00800 99.48600  69.79100  1.000 29.68761  ? 548 VAL B CG2  1 
ATOM   5874 N N    . ALA B 1 549 ? 122.34100 103.29400 70.59700  1.000 35.62856  ? 549 ALA B N    1 
ATOM   5875 C CA   . ALA B 1 549 ? 123.42500 104.27500 70.60300  1.000 29.69986  ? 549 ALA B CA   1 
ATOM   5876 C C    . ALA B 1 549 ? 123.85500 104.66800 72.01200  1.000 28.74774  ? 549 ALA B C    1 
ATOM   5877 O O    . ALA B 1 549 ? 125.00000 105.08600 72.21400  1.000 29.68789  ? 549 ALA B O    1 
ATOM   5878 C CB   . ALA B 1 549 ? 123.01000 105.51600 69.81500  1.000 28.20224  ? 549 ALA B CB   1 
ATOM   5879 N N    . ARG B 1 550 ? 122.96500 104.54700 72.99400  1.000 35.46345  ? 550 ARG B N    1 
ATOM   5880 C CA   . ARG B 1 550 ? 123.31500 104.90100 74.36700  1.000 29.81553  ? 550 ARG B CA   1 
ATOM   5881 C C    . ARG B 1 550 ? 123.92200 103.74900 75.15700  1.000 36.68421  ? 550 ARG B C    1 
ATOM   5882 O O    . ARG B 1 550 ? 124.64400 103.99700 76.12900  1.000 34.41681  ? 550 ARG B O    1 
ATOM   5883 C CB   . ARG B 1 550 ? 122.09000 105.42200 75.12600  1.000 30.65956  ? 550 ARG B CB   1 
ATOM   5884 C CG   . ARG B 1 550 ? 121.54500 106.74100 74.61900  1.000 34.77103  ? 550 ARG B CG   1 
ATOM   5885 C CD   . ARG B 1 550 ? 120.41100 107.23700 75.50400  1.000 35.76631  ? 550 ARG B CD   1 
ATOM   5886 N NE   . ARG B 1 550 ? 119.77500 108.43100 74.96200  1.000 38.75518  ? 550 ARG B NE   1 
ATOM   5887 C CZ   . ARG B 1 550 ? 118.80200 109.10200 75.56300  1.000 34.31339  ? 550 ARG B CZ   1 
ATOM   5888 N NH1  . ARG B 1 550 ? 118.32000 108.72000 76.73300  1.000 31.40987  ? 550 ARG B NH1  1 
ATOM   5889 N NH2  . ARG B 1 550 ? 118.30200 110.18500 74.97500  1.000 30.28113  ? 550 ARG B NH2  1 
ATOM   5890 N N    . LEU B 1 551 ? 123.63000 102.50500 74.77700  1.000 39.55565  ? 551 LEU B N    1 
ATOM   5891 C CA   . LEU B 1 551 ? 124.14500 101.34700 75.51200  1.000 33.10879  ? 551 LEU B CA   1 
ATOM   5892 C C    . LEU B 1 551 ? 125.63700 101.41700 75.87500  1.000 32.16692  ? 551 LEU B C    1 
ATOM   5893 O O    . LEU B 1 551 ? 126.05400 100.75700 76.83200  1.000 41.71865  ? 551 LEU B O    1 
ATOM   5894 C CB   . LEU B 1 551 ? 123.88900 100.07700 74.70000  1.000 36.64795  ? 551 LEU B CB   1 
ATOM   5895 C CG   . LEU B 1 551 ? 122.63100 99.29500  75.07800  1.000 40.70379  ? 551 LEU B CG   1 
ATOM   5896 C CD1  . LEU B 1 551 ? 122.53200 98.01300  74.26700  1.000 36.90728  ? 551 LEU B CD1  1 
ATOM   5897 C CD2  . LEU B 1 551 ? 122.58900 99.01100  76.57200  1.000 32.79797  ? 551 LEU B CD2  1 
ATOM   5898 N N    . GLN B 1 552 ? 126.45300 102.17900 75.13800  1.000 38.97878  ? 552 GLN B N    1 
ATOM   5899 C CA   . GLN B 1 552 ? 127.90900 102.15200 75.33000  1.000 36.59913  ? 552 GLN B CA   1 
ATOM   5900 C C    . GLN B 1 552 ? 128.34800 102.73600 76.67700  1.000 39.43990  ? 552 GLN B C    1 
ATOM   5901 O O    . GLN B 1 552 ? 129.33700 102.27400 77.27300  1.000 42.69154  ? 552 GLN B O    1 
ATOM   5902 C CB   . GLN B 1 552 ? 128.59000 102.89900 74.18400  1.000 36.89095  ? 552 GLN B CB   1 
ATOM   5903 C CG   . GLN B 1 552 ? 130.00400 103.36500 74.48900  1.000 41.82370  ? 552 GLN B CG   1 
ATOM   5904 C CD   . GLN B 1 552 ? 131.05800 102.39200 73.99600  1.000 44.23350  ? 552 GLN B CD   1 
ATOM   5905 O OE1  . GLN B 1 552 ? 131.01000 101.93600 72.85400  1.000 44.36779  ? 552 GLN B OE1  1 
ATOM   5906 N NE2  . GLN B 1 552 ? 132.01500 102.06800 74.85700  1.000 36.79223  ? 552 GLN B NE2  1 
ATOM   5907 N N    . ASN B 1 553 ? 127.66600 103.78200 77.14600  1.000 41.32879  ? 553 ASN B N    1 
ATOM   5908 C CA   . ASN B 1 553 ? 128.07100 104.42900 78.39100  1.000 37.33296  ? 553 ASN B CA   1 
ATOM   5909 C C    . ASN B 1 553 ? 128.00500 103.47200 79.57500  1.000 36.46432  ? 553 ASN B C    1 
ATOM   5910 O O    . ASN B 1 553 ? 128.81900 103.57300 80.50200  1.000 36.22105  ? 553 ASN B O    1 
ATOM   5911 C CB   . ASN B 1 553 ? 127.19100 105.65400 78.64600  1.000 43.80901  ? 553 ASN B CB   1 
ATOM   5912 C CG   . ASN B 1 553 ? 127.93700 106.77600 79.33300  1.000 44.15136  ? 553 ASN B CG   1 
ATOM   5913 O OD1  . ASN B 1 553 ? 127.52700 107.25000 80.39200  1.000 42.67880  ? 553 ASN B OD1  1 
ATOM   5914 N ND2  . ASN B 1 553 ? 129.03800 107.21000 78.73200  1.000 46.95382  ? 553 ASN B ND2  1 
ATOM   5915 N N    . VAL B 1 554 ? 127.06400 102.52700 79.55500  1.000 32.55436  ? 554 VAL B N    1 
ATOM   5916 C CA   . VAL B 1 554 ? 126.96100 101.57000 80.64900  1.000 35.88160  ? 554 VAL B CA   1 
ATOM   5917 C C    . VAL B 1 554 ? 128.19000 100.67000 80.68400  1.000 38.39751  ? 554 VAL B C    1 
ATOM   5918 O O    . VAL B 1 554 ? 128.71800 100.35600 81.75700  1.000 37.91414  ? 554 VAL B O    1 
ATOM   5919 C CB   . VAL B 1 554 ? 125.66100 100.75400 80.52400  1.000 36.10724  ? 554 VAL B CB   1 
ATOM   5920 C CG1  . VAL B 1 554 ? 125.38000 99.99700  81.81000  1.000 38.69956  ? 554 VAL B CG1  1 
ATOM   5921 C CG2  . VAL B 1 554 ? 124.49700 101.66400 80.17000  1.000 30.72529  ? 554 VAL B CG2  1 
ATOM   5922 N N    . VAL B 1 555 ? 128.68000 100.26200 79.51300  1.000 35.72788  ? 555 VAL B N    1 
ATOM   5923 C CA   . VAL B 1 555 ? 129.87600 99.42900  79.46200  1.000 31.68811  ? 555 VAL B CA   1 
ATOM   5924 C C    . VAL B 1 555 ? 131.08700 100.21200 79.94800  1.000 33.66611  ? 555 VAL B C    1 
ATOM   5925 O O    . VAL B 1 555 ? 131.94400 99.67900  80.66800  1.000 41.54801  ? 555 VAL B O    1 
ATOM   5926 C CB   . VAL B 1 555 ? 130.08700 98.88200  78.04000  1.000 36.81257  ? 555 VAL B CB   1 
ATOM   5927 C CG1  . VAL B 1 555 ? 131.50000 98.34500  77.88200  1.000 35.45960  ? 555 VAL B CG1  1 
ATOM   5928 C CG2  . VAL B 1 555 ? 129.06000 97.80400  77.73000  1.000 34.66852  ? 555 VAL B CG2  1 
ATOM   5929 N N    . ASP B 1 556 ? 131.18300 101.48600 79.56400  1.000 36.89863  ? 556 ASP B N    1 
ATOM   5930 C CA   . ASP B 1 556 ? 132.30800 102.29100 80.03900  1.000 37.51816  ? 556 ASP B CA   1 
ATOM   5931 C C    . ASP B 1 556 ? 132.28700 102.42300 81.56100  1.000 42.71202  ? 556 ASP B C    1 
ATOM   5932 O O    . ASP B 1 556 ? 133.32200 102.26400 82.22800  1.000 44.29161  ? 556 ASP B O    1 
ATOM   5933 C CB   . ASP B 1 556 ? 132.28700 103.66900 79.38000  1.000 39.60768  ? 556 ASP B CB   1 
ATOM   5934 C CG   . ASP B 1 556 ? 132.96500 103.67600 78.02600  1.000 48.33315  ? 556 ASP B CG   1 
ATOM   5935 O OD1  . ASP B 1 556 ? 133.50900 102.62600 77.62600  1.000 48.52273  ? 556 ASP B OD1  1 
ATOM   5936 O OD2  . ASP B 1 556 ? 132.95600 104.73400 77.36200  1.000 47.88634  ? 556 ASP B OD2  1 
ATOM   5937 N N    . ALA B 1 557 ? 131.10800 102.68800 82.13000  1.000 41.19825  ? 557 ALA B N    1 
ATOM   5938 C CA   . ALA B 1 557 ? 130.99900 102.79500 83.58100  1.000 36.25302  ? 557 ALA B CA   1 
ATOM   5939 C C    . ALA B 1 557 ? 131.34500 101.47500 84.25700  1.000 38.88214  ? 557 ALA B C    1 
ATOM   5940 O O    . ALA B 1 557 ? 131.99500 101.45900 85.31000  1.000 39.64128  ? 557 ALA B O    1 
ATOM   5941 C CB   . ALA B 1 557 ? 129.59500 103.25100 83.97500  1.000 33.97550  ? 557 ALA B CB   1 
ATOM   5942 N N    . PHE B 1 558 ? 130.90000 100.35500 83.68100  1.000 40.03662  ? 558 PHE B N    1 
ATOM   5943 C CA   . PHE B 1 558 ? 131.21700 99.06000  84.27100  1.000 37.48494  ? 558 PHE B CA   1 
ATOM   5944 C C    . PHE B 1 558 ? 132.71700 98.81000  84.27700  1.000 37.20485  ? 558 PHE B C    1 
ATOM   5945 O O    . PHE B 1 558 ? 133.25900 98.28400  85.25400  1.000 41.51735  ? 558 PHE B O    1 
ATOM   5946 C CB   . PHE B 1 558 ? 130.49900 97.93500  83.52800  1.000 40.91695  ? 558 PHE B CB   1 
ATOM   5947 C CG   . PHE B 1 558 ? 130.88600 96.56400  84.00300  1.000 40.73417  ? 558 PHE B CG   1 
ATOM   5948 C CD1  . PHE B 1 558 ? 130.25500 95.99100  85.09200  1.000 35.98569  ? 558 PHE B CD1  1 
ATOM   5949 C CD2  . PHE B 1 558 ? 131.89400 95.85600  83.37300  1.000 40.82737  ? 558 PHE B CD2  1 
ATOM   5950 C CE1  . PHE B 1 558 ? 130.61600 94.73500  85.53500  1.000 39.94502  ? 558 PHE B CE1  1 
ATOM   5951 C CE2  . PHE B 1 558 ? 132.25700 94.60000  83.81500  1.000 39.73991  ? 558 PHE B CE2  1 
ATOM   5952 C CZ   . PHE B 1 558 ? 131.61700 94.04000  84.89600  1.000 40.27463  ? 558 PHE B CZ   1 
ATOM   5953 N N    . LYS B 1 559 ? 133.40500 99.14900  83.18500  1.000 42.93227  ? 559 LYS B N    1 
ATOM   5954 C CA   . LYS B 1 559 ? 134.85200 98.95800  83.16600  1.000 46.27552  ? 559 LYS B CA   1 
ATOM   5955 C C    . LYS B 1 559 ? 135.52600 99.82100  84.22400  1.000 48.83230  ? 559 LYS B C    1 
ATOM   5956 O O    . LYS B 1 559 ? 136.44200 99.36500  84.92400  1.000 50.65870  ? 559 LYS B O    1 
ATOM   5957 C CB   . LYS B 1 559 ? 135.41600 99.26600  81.77900  1.000 44.36678  ? 559 LYS B CB   1 
ATOM   5958 C CG   . LYS B 1 559 ? 134.96200 98.30500  80.69700  1.000 48.41787  ? 559 LYS B CG   1 
ATOM   5959 C CD   . LYS B 1 559 ? 136.00400 98.18100  79.59900  1.000 46.00496  ? 559 LYS B CD   1 
ATOM   5960 C CE   . LYS B 1 559 ? 136.32800 99.53300  78.98900  1.000 51.92016  ? 559 LYS B CE   1 
ATOM   5961 N NZ   . LYS B 1 559 ? 136.38300 99.47100  77.50300  1.000 52.33532  ? 559 LYS B NZ   1 
ATOM   5962 N N    . GLU B 1 560 ? 135.07000 101.06600 84.37700  1.000 51.89692  ? 560 GLU B N    1 
ATOM   5963 C CA   . GLU B 1 560 ? 135.64800 101.92000 85.41100  1.000 47.46288  ? 560 GLU B CA   1 
ATOM   5964 C C    . GLU B 1 560 ? 135.44200 101.32400 86.80100  1.000 49.31229  ? 560 GLU B C    1 
ATOM   5965 O O    . GLU B 1 560 ? 136.36600 101.31100 87.62500  1.000 49.44406  ? 560 GLU B O    1 
ATOM   5966 C CB   . GLU B 1 560 ? 135.04500 103.32000 85.33500  1.000 47.09608  ? 560 GLU B CB   1 
ATOM   5967 C CG   . GLU B 1 560 ? 135.14200 104.10300 86.63100  1.000 52.62922  ? 560 GLU B CG   1 
ATOM   5968 C CD   . GLU B 1 560 ? 135.47300 105.56400 86.40600  1.000 59.15510  ? 560 GLU B CD   1 
ATOM   5969 O OE1  . GLU B 1 560 ? 135.56900 105.97800 85.23200  1.000 56.91579  ? 560 GLU B OE1  1 
ATOM   5970 O OE2  . GLU B 1 560 ? 135.63400 106.29900 87.40300  1.000 58.14787  ? 560 GLU B OE2  1 
ATOM   5971 N N    . LEU B 1 561 ? 134.23600 100.81900 87.07700  1.000 46.43970  ? 561 LEU B N    1 
ATOM   5972 C CA   . LEU B 1 561 ? 133.96900 100.21700 88.38200  1.000 42.07719  ? 561 LEU B CA   1 
ATOM   5973 C C    . LEU B 1 561 ? 134.81800 98.97200  88.60800  1.000 42.60584  ? 561 LEU B C    1 
ATOM   5974 O O    . LEU B 1 561 ? 135.37400 98.78200  89.69500  1.000 42.84231  ? 561 LEU B O    1 
ATOM   5975 C CB   . LEU B 1 561 ? 132.48500 99.87800  88.51900  1.000 43.66350  ? 561 LEU B CB   1 
ATOM   5976 C CG   . LEU B 1 561 ? 132.14400 98.84800  89.60100  1.000 39.50287  ? 561 LEU B CG   1 
ATOM   5977 C CD1  . LEU B 1 561 ? 132.23500 99.46500  90.98600  1.000 40.63150  ? 561 LEU B CD1  1 
ATOM   5978 C CD2  . LEU B 1 561 ? 130.76700 98.24900  89.37500  1.000 36.02968  ? 561 LEU B CD2  1 
ATOM   5979 N N    . SER B 1 562 ? 134.92500 98.10900  87.59600  1.000 49.29234  ? 562 SER B N    1 
ATOM   5980 C CA   . SER B 1 562 ? 135.71900 96.89500  87.74100  1.000 44.94047  ? 562 SER B CA   1 
ATOM   5981 C C    . SER B 1 562 ? 137.20400 97.19400  87.86700  1.000 45.07569  ? 562 SER B C    1 
ATOM   5982 O O    . SER B 1 562 ? 137.95600 96.33900  88.34400  1.000 42.52468  ? 562 SER B O    1 
ATOM   5983 C CB   . SER B 1 562 ? 135.47700 95.95700  86.55900  1.000 45.44913  ? 562 SER B CB   1 
ATOM   5984 O OG   . SER B 1 562 ? 136.47200 96.12300  85.56500  1.000 49.06371  ? 562 SER B OG   1 
ATOM   5985 N N    . GLN B 1 563 ? 137.64300 98.38400  87.45500  1.000 58.77459  ? 563 GLN B N    1 
ATOM   5986 C CA   . GLN B 1 563 ? 139.04300 98.73800  87.64700  1.000 57.51055  ? 563 GLN B CA   1 
ATOM   5987 C C    . GLN B 1 563 ? 139.29200 99.37500  89.00900  1.000 58.87144  ? 563 GLN B C    1 
ATOM   5988 O O    . GLN B 1 563 ? 140.31600 99.09500  89.64200  1.000 57.02484  ? 563 GLN B O    1 
ATOM   5989 C CB   . GLN B 1 563 ? 139.51300 99.68300  86.53800  1.000 56.12342  ? 563 GLN B CB   1 
ATOM   5990 C CG   . GLN B 1 563 ? 139.56700 99.04500  85.16100  1.000 60.80721  ? 563 GLN B CG   1 
ATOM   5991 C CD   . GLN B 1 563 ? 140.02800 100.01300 84.08900  1.000 65.90487  ? 563 GLN B CD   1 
ATOM   5992 O OE1  . GLN B 1 563 ? 140.24600 101.19500 84.35700  1.000 64.19934  ? 563 GLN B OE1  1 
ATOM   5993 N NE2  . GLN B 1 563 ? 140.17900 99.51500  82.86800  1.000 63.00890  ? 563 GLN B NE2  1 
ATOM   5994 N N    . LYS B 1 564 ? 138.37600 100.22800 89.48000  1.000 57.81066  ? 564 LYS B N    1 
ATOM   5995 C CA   . LYS B 1 564 ? 138.55300 100.83400 90.79700  1.000 54.07800  ? 564 LYS B CA   1 
ATOM   5996 C C    . LYS B 1 564 ? 138.57300 99.77900  91.89700  1.000 52.42378  ? 564 LYS B C    1 
ATOM   5997 O O    . LYS B 1 564 ? 139.38200 99.85800  92.82900  1.000 54.31238  ? 564 LYS B O    1 
ATOM   5998 C CB   . LYS B 1 564 ? 137.45300 101.86200 91.05900  1.000 53.29400  ? 564 LYS B CB   1 
ATOM   5999 C CG   . LYS B 1 564 ? 137.53700 103.08900 90.17100  1.000 54.69652  ? 564 LYS B CG   1 
ATOM   6000 C CD   . LYS B 1 564 ? 138.95100 103.64000 90.13200  1.000 53.80551  ? 564 LYS B CD   1 
ATOM   6001 C CE   . LYS B 1 564 ? 138.95100 105.15700 90.16100  1.000 55.69726  ? 564 LYS B CE   1 
ATOM   6002 N NZ   . LYS B 1 564 ? 138.59100 105.68200 91.50600  1.000 58.98145  ? 564 LYS B NZ   1 
ATOM   6003 N N    . ALA B 1 565 ? 137.68900 98.79100  91.81200  1.000 55.58252  ? 565 ALA B N    1 
ATOM   6004 C CA   . ALA B 1 565 ? 137.66700 97.67300  92.74400  1.000 53.30523  ? 565 ALA B CA   1 
ATOM   6005 C C    . ALA B 1 565 ? 138.32600 96.46200  92.09800  1.000 58.37669  ? 565 ALA B C    1 
ATOM   6006 O O    . ALA B 1 565 ? 138.13000 96.19700  90.90900  1.000 64.62084  ? 565 ALA B O    1 
ATOM   6007 C CB   . ALA B 1 565 ? 136.23600 97.33100  93.16300  1.000 46.44641  ? 565 ALA B CB   1 
ATOM   6008 N N    . ASN B 1 566 ? 139.11800 95.73500  92.88300  1.000 52.41541  ? 566 ASN B N    1 
ATOM   6009 C CA   . ASN B 1 566 ? 139.85300 94.60200  92.33900  1.000 51.52955  ? 566 ASN B CA   1 
ATOM   6010 C C    . ASN B 1 566 ? 138.91300 93.44200  92.04300  1.000 54.67448  ? 566 ASN B C    1 
ATOM   6011 O O    . ASN B 1 566 ? 138.63900 92.61700  92.91900  1.000 57.73929  ? 566 ASN B O    1 
ATOM   6012 C CB   . ASN B 1 566 ? 140.95200 94.16300  93.30900  1.000 56.09505  ? 566 ASN B CB   1 
ATOM   6013 C CG   . ASN B 1 566 ? 142.27300 93.90300  92.61300  1.000 61.78644  ? 566 ASN B CG   1 
ATOM   6014 O OD1  . ASN B 1 566 ? 142.87300 94.81000  92.03600  1.000 61.22270  ? 566 ASN B OD1  1 
ATOM   6015 N ND2  . ASN B 1 566 ? 142.73300 92.65900  92.66300  1.000 58.78606  ? 566 ASN B ND2  1 
ATOM   6016 N N    . PHE B 1 567 ? 138.42300 93.36600  90.80900  1.000 50.69545  ? 567 PHE B N    1 
ATOM   6017 C CA   . PHE B 1 567 ? 137.55200 92.28100  90.38600  1.000 47.29921  ? 567 PHE B CA   1 
ATOM   6018 C C    . PHE B 1 567 ? 138.38200 91.09300  89.91500  1.000 53.42858  ? 567 PHE B C    1 
ATOM   6019 O O    . PHE B 1 567 ? 139.47600 91.25000  89.36800  1.000 54.86128  ? 567 PHE B O    1 
ATOM   6020 C CB   . PHE B 1 567 ? 136.61100 92.73700  89.27000  1.000 46.23428  ? 567 PHE B CB   1 
ATOM   6021 C CG   . PHE B 1 567 ? 135.32500 93.33700  89.76500  1.000 50.75032  ? 567 PHE B CG   1 
ATOM   6022 C CD1  . PHE B 1 567 ? 135.17900 93.70700  91.09000  1.000 53.74449  ? 567 PHE B CD1  1 
ATOM   6023 C CD2  . PHE B 1 567 ? 134.25600 93.52200  88.90500  1.000 48.57042  ? 567 PHE B CD2  1 
ATOM   6024 C CE1  . PHE B 1 567 ? 133.99600 94.25800  91.54500  1.000 47.71192  ? 567 PHE B CE1  1 
ATOM   6025 C CE2  . PHE B 1 567 ? 133.07200 94.07000  89.35500  1.000 47.03044  ? 567 PHE B CE2  1 
ATOM   6026 C CZ   . PHE B 1 567 ? 132.94200 94.43700  90.67700  1.000 42.91052  ? 567 PHE B CZ   1 
ATOM   6027 N N    . LYS B 1 568 ? 137.84800 89.89600  90.13500  1.000 62.63739  ? 568 LYS B N    1 
ATOM   6028 C CA   . LYS B 1 568 ? 138.56400 88.68200  89.77600  1.000 60.13516  ? 568 LYS B CA   1 
ATOM   6029 C C    . LYS B 1 568 ? 138.72600 88.57200  88.26400  1.000 62.74904  ? 568 LYS B C    1 
ATOM   6030 O O    . LYS B 1 568 ? 137.86300 88.99300  87.49000  1.000 65.82787  ? 568 LYS B O    1 
ATOM   6031 C CB   . LYS B 1 568 ? 137.82700 87.45700  90.31600  1.000 62.64805  ? 568 LYS B CB   1 
ATOM   6032 C CG   . LYS B 1 568 ? 138.09800 86.17200  89.56000  1.000 63.44455  ? 568 LYS B CG   1 
ATOM   6033 C CD   . LYS B 1 568 ? 137.31800 85.01500  90.16200  1.000 64.16797  ? 568 LYS B CD   1 
ATOM   6034 C CE   . LYS B 1 568 ? 135.83700 85.12500  89.83800  1.000 65.66091  ? 568 LYS B CE   1 
ATOM   6035 N NZ   . LYS B 1 568 ? 134.98200 84.75000  90.99800  1.000 66.34090  ? 568 LYS B NZ   1 
ATOM   6036 N N    . GLU B 1 569 ? 139.84500 87.99000  87.85000  1.000 74.30326  ? 569 GLU B N    1 
ATOM   6037 C CA   . GLU B 1 569 ? 140.07500 87.74500  86.43500  1.000 74.19551  ? 569 GLU B CA   1 
ATOM   6038 C C    . GLU B 1 569 ? 139.04200 86.75100  85.90700  1.000 77.25138  ? 569 GLU B C    1 
ATOM   6039 O O    . GLU B 1 569 ? 138.73600 85.75800  86.57800  1.000 77.62775  ? 569 GLU B O    1 
ATOM   6040 C CB   . GLU B 1 569 ? 141.48800 87.20300  86.21200  1.000 74.40351  ? 569 GLU B CB   1 
ATOM   6041 C CG   . GLU B 1 569 ? 142.06700 87.49700  84.84000  1.000 75.31865  ? 569 GLU B CG   1 
ATOM   6042 C CD   . GLU B 1 569 ? 142.14800 88.98100  84.54900  1.000 77.78031  ? 569 GLU B CD   1 
ATOM   6043 O OE1  . GLU B 1 569 ? 142.22800 89.77200  85.51200  1.000 77.30142  ? 569 GLU B OE1  1 
ATOM   6044 O OE2  . GLU B 1 569 ? 142.13300 89.35800  83.35900  1.000 77.42751  ? 569 GLU B OE2  1 
ATOM   6045 N N    . PRO B 1 570 ? 138.48600 86.98100  84.72000  1.000 81.38274  ? 570 PRO B N    1 
ATOM   6046 C CA   . PRO B 1 570 ? 137.53300 86.01600  84.16500  1.000 81.07714  ? 570 PRO B CA   1 
ATOM   6047 C C    . PRO B 1 570 ? 138.19100 84.66700  83.91600  1.000 81.19964  ? 570 PRO B C    1 
ATOM   6048 O O    . PRO B 1 570 ? 139.35000 84.58400  83.50600  1.000 81.18520  ? 570 PRO B O    1 
ATOM   6049 C CB   . PRO B 1 570 ? 137.06800 86.68400  82.86700  1.000 78.28505  ? 570 PRO B CB   1 
ATOM   6050 C CG   . PRO B 1 570 ? 138.15500 87.67500  82.51200  1.000 78.78810  ? 570 PRO B CG   1 
ATOM   6051 C CD   . PRO B 1 570 ? 139.14200 87.75000  83.65100  1.000 78.59476  ? 570 PRO B CD   1 
ATOM   6052 N N    . GLU B 1 571 ? 137.43400 83.60400  84.16700  1.000 84.95193  ? 571 GLU B N    1 
ATOM   6053 C CA   . GLU B 1 571 ? 137.94800 82.24700  84.01600  1.000 87.30183  ? 571 GLU B CA   1 
ATOM   6054 C C    . GLU B 1 571 ? 138.10500 81.88100  82.54400  1.000 87.86268  ? 571 GLU B C    1 
ATOM   6055 O O    . GLU B 1 571 ? 138.99900 81.11800  82.17700  1.000 86.16853  ? 571 GLU B O    1 
ATOM   6056 C CB   . GLU B 1 571 ? 137.02600 81.24400  84.71200  1.000 85.93899  ? 571 GLU B CB   1 
HETATM 6057 O O13  . 3PH C 2 .   ? 109.67200 111.03800 135.35200 1.000 35.40351  ? 601 3PH A O13  1 
HETATM 6058 P P    . 3PH C 2 .   ? 109.78100 109.62100 134.85400 1.000 52.90245  ? 601 3PH A P    1 
HETATM 6059 O O14  . 3PH C 2 .   ? 108.46200 108.92100 134.99900 1.000 47.07389  ? 601 3PH A O14  1 
HETATM 6060 O O12  . 3PH C 2 .   ? 110.81100 108.86900 135.65400 1.000 37.12095  ? 601 3PH A O12  1 
HETATM 6061 O O11  . 3PH C 2 .   ? 110.20000 109.60800 133.26800 1.000 41.63252  ? 601 3PH A O11  1 
HETATM 6062 C C1   . 3PH C 2 .   ? 109.54700 108.68600 132.43300 1.000 36.76328  ? 601 3PH A C1   1 
HETATM 6063 C C2   . 3PH C 2 .   ? 109.87300 109.01000 130.98100 1.000 36.88084  ? 601 3PH A C2   1 
HETATM 6064 O O21  . 3PH C 2 .   ? 110.28000 110.35600 130.91200 1.000 38.21950  ? 601 3PH A O21  1 
HETATM 6065 C C21  . 3PH C 2 .   ? 111.05900 110.64700 129.79300 1.000 41.64258  ? 601 3PH A C21  1 
HETATM 6066 O O22  . 3PH C 2 .   ? 110.67800 111.44600 129.01100 1.000 35.50845  ? 601 3PH A O22  1 
HETATM 6067 C C22  . 3PH C 2 .   ? 112.39100 109.92700 129.58900 1.000 43.75620  ? 601 3PH A C22  1 
HETATM 6068 C C23  . 3PH C 2 .   ? 112.27700 108.81100 128.54500 1.000 38.62324  ? 601 3PH A C23  1 
HETATM 6069 C C24  . 3PH C 2 .   ? 113.70700 108.44800 128.12200 1.000 35.20633  ? 601 3PH A C24  1 
HETATM 6070 C C25  . 3PH C 2 .   ? 113.68400 107.24600 127.16500 1.000 37.15515  ? 601 3PH A C25  1 
HETATM 6071 C C26  . 3PH C 2 .   ? 113.79100 107.74100 125.71300 1.000 34.85060  ? 601 3PH A C26  1 
HETATM 6072 C C27  . 3PH C 2 .   ? 115.02900 107.12100 125.04400 1.000 36.94917  ? 601 3PH A C27  1 
HETATM 6073 C C28  . 3PH C 2 .   ? 116.25900 108.02100 125.28700 1.000 36.60354  ? 601 3PH A C28  1 
HETATM 6074 C C29  . 3PH C 2 .   ? 116.65900 108.66500 123.94700 1.000 36.79416  ? 601 3PH A C29  1 
HETATM 6075 C C2A  . 3PH C 2 .   ? 118.12200 109.15800 124.01900 1.000 33.89435  ? 601 3PH A C2A  1 
HETATM 6076 C C2B  . 3PH C 2 .   ? 118.78200 108.93500 122.65900 1.000 31.90513  ? 601 3PH A C2B  1 
HETATM 6077 C C2C  . 3PH C 2 .   ? 120.27800 109.27000 122.76000 1.000 34.36628  ? 601 3PH A C2C  1 
HETATM 6078 C C2D  . 3PH C 2 .   ? 121.06200 108.40900 121.77400 1.000 32.02829  ? 601 3PH A C2D  1 
HETATM 6079 C C2E  . 3PH C 2 .   ? 121.31000 107.03600 122.38800 1.000 30.36816  ? 601 3PH A C2E  1 
HETATM 6080 C C2F  . 3PH C 2 .   ? 122.74300 106.92200 122.89600 1.000 30.27905  ? 601 3PH A C2F  1 
HETATM 6081 C C2G  . 3PH C 2 .   ? 123.70500 107.06100 121.73400 1.000 37.60809  ? 601 3PH A C2G  1 
HETATM 6082 C C2H  . 3PH C 2 .   ? 124.97900 106.26400 121.99200 1.000 38.43020  ? 601 3PH A C2H  1 
HETATM 6083 C C2I  . 3PH C 2 .   ? 125.68000 106.73200 123.25900 1.000 36.44546  ? 601 3PH A C2I  1 
HETATM 6084 C C3   . 3PH C 2 .   ? 108.64900 108.78500 130.10900 1.000 41.91856  ? 601 3PH A C3   1 
HETATM 6085 O O31  . 3PH C 2 .   ? 107.68500 109.74300 130.44900 1.000 46.85490  ? 601 3PH A O31  1 
HETATM 6086 C C31  . 3PH C 2 .   ? 107.12100 110.39400 129.35100 1.000 42.20214  ? 601 3PH A C31  1 
HETATM 6087 O O32  . 3PH C 2 .   ? 106.52700 109.77100 128.54400 1.000 41.44601  ? 601 3PH A O32  1 
HETATM 6088 C C32  . 3PH C 2 .   ? 107.27400 111.90700 129.22700 1.000 36.72279  ? 601 3PH A C32  1 
HETATM 6089 C C33  . 3PH C 2 .   ? 106.87900 112.37100 127.82100 1.000 42.44784  ? 601 3PH A C33  1 
HETATM 6090 C C34  . 3PH C 2 .   ? 105.41800 112.83000 127.82200 1.000 45.10171  ? 601 3PH A C34  1 
HETATM 6091 C C35  . 3PH C 2 .   ? 104.59000 111.83900 127.01700 1.000 38.68582  ? 601 3PH A C35  1 
HETATM 6092 C C36  . 3PH C 2 .   ? 105.02700 111.88400 125.55300 1.000 33.93715  ? 601 3PH A C36  1 
HETATM 6093 C C37  . 3PH C 2 .   ? 103.78100 111.72400 124.68200 1.000 36.04943  ? 601 3PH A C37  1 
HETATM 6094 C C38  . 3PH C 2 .   ? 103.02300 110.46100 125.14000 1.000 37.91862  ? 601 3PH A C38  1 
HETATM 6095 C C39  . 3PH C 2 .   ? 102.09400 109.88000 124.04200 1.000 34.45684  ? 601 3PH A C39  1 
HETATM 6096 C C3A  . 3PH C 2 .   ? 101.82100 110.90600 122.92500 1.000 32.09705  ? 601 3PH A C3A  1 
HETATM 6097 C C3B  . 3PH C 2 .   ? 100.49300 110.54700 122.24900 1.000 31.01645  ? 601 3PH A C3B  1 
HETATM 6098 C C3C  . 3PH C 2 .   ? 99.41200  111.41900 122.88800 1.000 36.87249  ? 601 3PH A C3C  1 
HETATM 6099 C C3D  . 3PH C 2 .   ? 98.14200  111.36500 122.04900 1.000 32.25540  ? 601 3PH A C3D  1 
HETATM 6100 C C3E  . 3PH C 2 .   ? 97.31900  112.59700 122.37600 1.000 26.37115  ? 601 3PH A C3E  1 
HETATM 6101 C C3F  . 3PH C 2 .   ? 95.86500  112.25100 122.14200 1.000 34.19191  ? 601 3PH A C3F  1 
HETATM 6102 C C3G  . 3PH C 2 .   ? 95.04700  113.52900 122.07900 1.000 38.85990  ? 601 3PH A C3G  1 
HETATM 6103 C C3H  . 3PH C 2 .   ? 93.63800  113.23200 122.56300 1.000 39.84588  ? 601 3PH A C3H  1 
HETATM 6104 C C3I  . 3PH C 2 .   ? 93.61500  113.29800 124.08200 1.000 41.11242  ? 601 3PH A C3I  1 
HETATM 6105 H H11  . 3PH C 2 .   ? 108.47400 108.74900 132.58100 1.000 35.55061  ? 601 3PH A H11  1 
HETATM 6106 H H12  . 3PH C 2 .   ? 109.88600 107.67500 132.66400 1.000 35.30990  ? 601 3PH A H12  1 
HETATM 6107 H H2   . 3PH C 2 .   ? 110.66900 108.36300 130.65200 1.000 34.93394  ? 601 3PH A H2   1 
HETATM 6108 H H221 . 3PH C 2 .   ? 112.68500 109.47400 130.52300 1.000 36.78870  ? 601 3PH A H221 1 
HETATM 6109 H H222 . 3PH C 2 .   ? 113.14800 110.63700 129.27400 1.000 36.46393  ? 601 3PH A H222 1 
HETATM 6110 H H231 . 3PH C 2 .   ? 111.80400 107.94000 128.98500 1.000 35.66840  ? 601 3PH A H231 1 
HETATM 6111 H H232 . 3PH C 2 .   ? 111.69800 109.14400 127.69200 1.000 36.23959  ? 601 3PH A H232 1 
HETATM 6112 H H241 . 3PH C 2 .   ? 114.26700 108.17800 129.01000 1.000 35.81564  ? 601 3PH A H241 1 
HETATM 6113 H H242 . 3PH C 2 .   ? 114.18100 109.30000 127.64700 1.000 35.73906  ? 601 3PH A H242 1 
HETATM 6114 H H251 . 3PH C 2 .   ? 114.52400 106.59800 127.38900 1.000 36.55400  ? 601 3PH A H251 1 
HETATM 6115 H H252 . 3PH C 2 .   ? 112.75700 106.69600 127.29400 1.000 36.00411  ? 601 3PH A H252 1 
HETATM 6116 H H261 . 3PH C 2 .   ? 113.87000 108.81800 125.68800 1.000 35.89485  ? 601 3PH A H261 1 
HETATM 6117 H H262 . 3PH C 2 .   ? 112.90700 107.43600 125.16900 1.000 35.80856  ? 601 3PH A H262 1 
HETATM 6118 H H271 . 3PH C 2 .   ? 114.84900 107.03400 123.97400 1.000 36.46406  ? 601 3PH A H271 1 
HETATM 6119 H H272 . 3PH C 2 .   ? 115.21300 106.13400 125.45600 1.000 36.62176  ? 601 3PH A H272 1 
HETATM 6120 H H281 . 3PH C 2 .   ? 117.07800 107.42000 125.66400 1.000 36.60766  ? 601 3PH A H281 1 
HETATM 6121 H H282 . 3PH C 2 .   ? 116.01100 108.79300 126.00400 1.000 35.74664  ? 601 3PH A H282 1 
HETATM 6122 H H291 . 3PH C 2 .   ? 116.56700 107.93500 123.14800 1.000 35.90059  ? 601 3PH A H291 1 
HETATM 6123 H H292 . 3PH C 2 .   ? 116.00300 109.51000 123.74700 1.000 36.19650  ? 601 3PH A H292 1 
HETATM 6124 H H2A1 . 3PH C 2 .   ? 118.65900 108.59800 124.77600 1.000 36.20277  ? 601 3PH A H2A1 1 
HETATM 6125 H H2A2 . 3PH C 2 .   ? 118.14000 110.21400 124.26200 1.000 35.76820  ? 601 3PH A H2A2 1 
HETATM 6126 H H2B1 . 3PH C 2 .   ? 118.66300 107.90000 122.36300 1.000 35.31766  ? 601 3PH A H2B1 1 
HETATM 6127 H H2B2 . 3PH C 2 .   ? 118.31900 109.57800 121.92200 1.000 35.86792  ? 601 3PH A H2B2 1 
HETATM 6128 H H2C1 . 3PH C 2 .   ? 120.43100 110.31800 122.52100 1.000 36.50181  ? 601 3PH A H2C1 1 
HETATM 6129 H H2C2 . 3PH C 2 .   ? 120.62600 109.07000 123.77000 1.000 35.50348  ? 601 3PH A H2C2 1 
HETATM 6130 H H2D1 . 3PH C 2 .   ? 121.99900 108.90100 121.54200 1.000 36.19766  ? 601 3PH A H2D1 1 
HETATM 6131 H H2D2 . 3PH C 2 .   ? 120.48200 108.29000 120.86600 1.000 36.13656  ? 601 3PH A H2D2 1 
HETATM 6132 H H2E1 . 3PH C 2 .   ? 121.13500 106.27300 121.63600 1.000 35.94147  ? 601 3PH A H2E1 1 
HETATM 6133 H H2E2 . 3PH C 2 .   ? 120.62400 106.88700 123.21700 1.000 36.12048  ? 601 3PH A H2E2 1 
HETATM 6134 H H2F1 . 3PH C 2 .   ? 122.88500 105.95800 123.36900 1.000 35.45588  ? 601 3PH A H2F1 1 
HETATM 6135 H H2F2 . 3PH C 2 .   ? 122.92800 107.71200 123.61600 1.000 35.60993  ? 601 3PH A H2F2 1 
HETATM 6136 H H2G1 . 3PH C 2 .   ? 123.96400 108.10500 121.60800 1.000 36.31301  ? 601 3PH A H2G1 1 
HETATM 6137 H H2G2 . 3PH C 2 .   ? 123.23100 106.69900 120.83100 1.000 36.60967  ? 601 3PH A H2G2 1 
HETATM 6138 H H2H1 . 3PH C 2 .   ? 124.72300 105.21400 122.09600 1.000 36.40297  ? 601 3PH A H2H1 1 
HETATM 6139 H H2H2 . 3PH C 2 .   ? 125.64900 106.38600 121.14800 1.000 36.08276  ? 601 3PH A H2H2 1 
HETATM 6140 H H2I1 . 3PH C 2 .   ? 126.62100 107.20300 122.99300 1.000 35.68684  ? 601 3PH A H2I1 1 
HETATM 6141 H H2I2 . 3PH C 2 .   ? 125.86800 105.88000 123.90500 1.000 35.52390  ? 601 3PH A H2I2 1 
HETATM 6142 H H2I3 . 3PH C 2 .   ? 125.06100 107.45400 123.78200 1.000 36.31829  ? 601 3PH A H2I3 1 
HETATM 6143 H H31  . 3PH C 2 .   ? 108.92800 108.90300 129.06800 1.000 35.87043  ? 601 3PH A H31  1 
HETATM 6144 H H32  . 3PH C 2 .   ? 108.25500 107.78800 130.28000 1.000 36.28819  ? 601 3PH A H32  1 
HETATM 6145 H H321 . 3PH C 2 .   ? 106.64700 112.39000 129.96700 1.000 35.63528  ? 601 3PH A H321 1 
HETATM 6146 H H322 . 3PH C 2 .   ? 108.30500 112.17200 129.41000 1.000 35.07308  ? 601 3PH A H322 1 
HETATM 6147 H H331 . 3PH C 2 .   ? 107.01800 111.56100 127.11100 1.000 35.96021  ? 601 3PH A H331 1 
HETATM 6148 H H332 . 3PH C 2 .   ? 107.51000 113.20500 127.52900 1.000 35.26825  ? 601 3PH A H332 1 
HETATM 6149 H H341 . 3PH C 2 .   ? 105.03800 112.87400 128.83700 1.000 36.43920  ? 601 3PH A H341 1 
HETATM 6150 H H342 . 3PH C 2 .   ? 105.34500 113.81200 127.36500 1.000 35.86315  ? 601 3PH A H342 1 
HETATM 6151 H H351 . 3PH C 2 .   ? 103.54500 112.12000 127.09300 1.000 35.88010  ? 601 3PH A H351 1 
HETATM 6152 H H352 . 3PH C 2 .   ? 104.72500 110.83500 127.40800 1.000 35.27570  ? 601 3PH A H352 1 
HETATM 6153 H H361 . 3PH C 2 .   ? 105.49900 112.83600 125.34400 1.000 33.77887  ? 601 3PH A H361 1 
HETATM 6154 H H362 . 3PH C 2 .   ? 105.72400 111.08000 125.34900 1.000 35.84287  ? 601 3PH A H362 1 
HETATM 6155 H H371 . 3PH C 2 .   ? 103.14600 112.59700 124.79700 1.000 34.58529  ? 601 3PH A H371 1 
HETATM 6156 H H372 . 3PH C 2 .   ? 104.09300 111.62400 123.64800 1.000 35.28394  ? 601 3PH A H372 1 
HETATM 6157 H H381 . 3PH C 2 .   ? 103.75000 109.70100 125.42200 1.000 35.98883  ? 601 3PH A H381 1 
HETATM 6158 H H382 . 3PH C 2 .   ? 102.41600 110.70600 126.00600 1.000 36.17400  ? 601 3PH A H382 1 
HETATM 6159 H H391 . 3PH C 2 .   ? 102.56200 109.00300 123.61100 1.000 35.93052  ? 601 3PH A H391 1 
HETATM 6160 H H392 . 3PH C 2 .   ? 101.14900 109.59300 124.49400 1.000 35.17666  ? 601 3PH A H392 1 
HETATM 6161 H H3A1 . 3PH C 2 .   ? 101.73400 111.90500 123.34400 1.000 35.14783  ? 601 3PH A H3A1 1 
HETATM 6162 H H3A2 . 3PH C 2 .   ? 102.62400 110.87800 122.19500 1.000 34.65856  ? 601 3PH A H3A2 1 
HETATM 6163 H H3B1 . 3PH C 2 .   ? 100.26600 109.49700 122.41100 1.000 32.94535  ? 601 3PH A H3B1 1 
HETATM 6164 H H3B2 . 3PH C 2 .   ? 100.55300 110.75500 121.18800 1.000 34.17747  ? 601 3PH A H3B2 1 
HETATM 6165 H H3C1 . 3PH C 2 .   ? 99.75500  112.44600 122.94300 1.000 35.68625  ? 601 3PH A H3C1 1 
HETATM 6166 H H3C2 . 3PH C 2 .   ? 99.20000  111.05300 123.89100 1.000 36.19757  ? 601 3PH A H3C2 1 
HETATM 6167 H H3D1 . 3PH C 2 .   ? 97.57600  110.47100 122.29100 1.000 34.20920  ? 601 3PH A H3D1 1 
HETATM 6168 H H3D2 . 3PH C 2 .   ? 98.39800  111.36400 120.99600 1.000 33.04231  ? 601 3PH A H3D2 1 
HETATM 6169 H H3E1 . 3PH C 2 .   ? 97.60900  113.41700 121.72900 1.000 33.79819  ? 601 3PH A H3E1 1 
HETATM 6170 H H3E2 . 3PH C 2 .   ? 97.46800  112.87300 123.41300 1.000 34.77366  ? 601 3PH A H3E2 1 
HETATM 6171 H H3F1 . 3PH C 2 .   ? 95.50700  111.62600 122.95300 1.000 34.89783  ? 601 3PH A H3F1 1 
HETATM 6172 H H3F2 . 3PH C 2 .   ? 95.77100  111.71300 121.20400 1.000 34.31241  ? 601 3PH A H3F2 1 
HETATM 6173 H H3G1 . 3PH C 2 .   ? 95.01500  113.89000 121.05600 1.000 35.46330  ? 601 3PH A H3G1 1 
HETATM 6174 H H3G2 . 3PH C 2 .   ? 95.50000  114.27800 122.71900 1.000 35.76331  ? 601 3PH A H3G2 1 
HETATM 6175 H H3H1 . 3PH C 2 .   ? 92.95000  113.96500 122.15600 1.000 35.83397  ? 601 3PH A H3H1 1 
HETATM 6176 H H3H2 . 3PH C 2 .   ? 93.34900  112.23800 122.23900 1.000 35.46009  ? 601 3PH A H3H2 1 
HETATM 6177 H H3I1 . 3PH C 2 .   ? 94.53600  112.88300 124.47400 1.000 35.99623  ? 601 3PH A H3I1 1 
HETATM 6178 H H3I2 . 3PH C 2 .   ? 93.52400  114.33100 124.39500 1.000 35.67607  ? 601 3PH A H3I2 1 
HETATM 6179 H H3I3 . 3PH C 2 .   ? 92.77300  112.72800 124.45600 1.000 36.42399  ? 601 3PH A H3I3 1 
HETATM 6180 O O13  . 3PH D 2 .   ? 111.89600 110.59900 122.08100 1.000 45.42704  ? 601 3PH B O13  1 
HETATM 6181 P P    . 3PH D 2 .   ? 110.73300 109.63700 122.08700 1.000 64.39057  ? 601 3PH B P    1 
HETATM 6182 O O14  . 3PH D 2 .   ? 110.84200 108.74400 120.88100 1.000 41.68767  ? 601 3PH B O14  1 
HETATM 6183 O O12  . 3PH D 2 .   ? 109.42600 110.38700 122.01900 1.000 38.31976  ? 601 3PH B O12  1 
HETATM 6184 O O11  . 3PH D 2 .   ? 110.78700 108.72900 123.46400 1.000 40.53208  ? 601 3PH B O11  1 
HETATM 6185 C C1   . 3PH D 2 .   ? 111.07000 109.36600 124.68500 1.000 39.68907  ? 601 3PH B C1   1 
HETATM 6186 C C2   . 3PH D 2 .   ? 109.99300 110.40200 125.00800 1.000 42.54389  ? 601 3PH B C2   1 
HETATM 6187 O O21  . 3PH D 2 .   ? 110.26500 110.98100 126.25400 1.000 43.80497  ? 601 3PH B O21  1 
HETATM 6188 C C21  . 3PH D 2 .   ? 111.27000 111.95200 126.23500 1.000 44.91725  ? 601 3PH B C21  1 
HETATM 6189 O O22  . 3PH D 2 .   ? 111.01000 113.07700 125.98400 1.000 52.12649  ? 601 3PH B O22  1 
HETATM 6190 C C22  . 3PH D 2 .   ? 112.70800 111.56500 126.55000 1.000 39.74437  ? 601 3PH B C22  1 
HETATM 6191 C C23  . 3PH D 2 .   ? 113.66100 112.09400 125.47300 1.000 39.76893  ? 601 3PH B C23  1 
HETATM 6192 C C24  . 3PH D 2 .   ? 115.09900 111.80000 125.92900 1.000 38.33734  ? 601 3PH B C24  1 
HETATM 6193 C C25  . 3PH D 2 .   ? 115.70200 113.10300 126.47700 1.000 39.79534  ? 601 3PH B C25  1 
HETATM 6194 C C26  . 3PH D 2 .   ? 115.05300 113.41900 127.83200 1.000 38.84445  ? 601 3PH B C26  1 
HETATM 6195 C C27  . 3PH D 2 .   ? 116.06600 114.17800 128.70400 1.000 42.88487  ? 601 3PH B C27  1 
HETATM 6196 C C28  . 3PH D 2 .   ? 116.95600 113.16400 129.45100 1.000 37.60949  ? 601 3PH B C28  1 
HETATM 6197 C C29  . 3PH D 2 .   ? 118.41800 113.61700 129.33400 1.000 34.98390  ? 601 3PH B C29  1 
HETATM 6198 C C2A  . 3PH D 2 .   ? 119.27100 112.86000 130.37400 1.000 41.33176  ? 601 3PH B C2A  1 
HETATM 6199 C C2B  . 3PH D 2 .   ? 120.68500 112.73600 129.81300 1.000 40.65555  ? 601 3PH B C2B  1 
HETATM 6200 C C2C  . 3PH D 2 .   ? 121.24000 114.15200 129.61600 1.000 34.69548  ? 601 3PH B C2C  1 
HETATM 6201 C C2D  . 3PH D 2 .   ? 122.75500 114.10000 129.50000 1.000 30.60919  ? 601 3PH B C2D  1 
HETATM 6202 C C2E  . 3PH D 2 .   ? 123.24700 115.53800 129.46400 1.000 34.69376  ? 601 3PH B C2E  1 
HETATM 6203 C C2F  . 3PH D 2 .   ? 124.76200 115.56800 129.63300 1.000 38.47976  ? 601 3PH B C2F  1 
HETATM 6204 C C2G  . 3PH D 2 .   ? 125.13700 116.88400 130.28100 1.000 43.13478  ? 601 3PH B C2G  1 
HETATM 6205 C C2H  . 3PH D 2 .   ? 126.65300 116.97200 130.36500 1.000 38.18632  ? 601 3PH B C2H  1 
HETATM 6206 C C2I  . 3PH D 2 .   ? 127.19500 117.42700 129.02000 1.000 37.54466  ? 601 3PH B C2I  1 
HETATM 6207 C C3   . 3PH D 2 .   ? 108.63500 109.72700 125.07900 1.000 41.16509  ? 601 3PH B C3   1 
HETATM 6208 O O31  . 3PH D 2 .   ? 108.72100 108.61800 125.93800 1.000 43.39801  ? 601 3PH B O31  1 
HETATM 6209 C C31  . 3PH D 2 .   ? 107.55600 107.84800 126.06000 1.000 45.89849  ? 601 3PH B C31  1 
HETATM 6210 O O32  . 3PH D 2 .   ? 107.62300 106.80100 126.60500 1.000 42.49433  ? 601 3PH B O32  1 
HETATM 6211 C C32  . 3PH D 2 .   ? 106.21200 108.36000 125.53500 1.000 42.74302  ? 601 3PH B C32  1 
HETATM 6212 C C33  . 3PH D 2 .   ? 105.19000 107.22200 125.44900 1.000 39.15277  ? 601 3PH B C33  1 
HETATM 6213 C C34  . 3PH D 2 .   ? 104.28900 107.20600 126.68700 1.000 36.92401  ? 601 3PH B C34  1 
HETATM 6214 C C35  . 3PH D 2 .   ? 104.82900 106.15900 127.66500 1.000 33.15619  ? 601 3PH B C35  1 
HETATM 6215 C C36  . 3PH D 2 .   ? 103.85200 105.79200 128.79300 1.000 42.43238  ? 601 3PH B C36  1 
HETATM 6216 C C37  . 3PH D 2 .   ? 102.41800 106.27200 128.52200 1.000 40.73214  ? 601 3PH B C37  1 
HETATM 6217 C C38  . 3PH D 2 .   ? 101.50100 105.81900 129.66900 1.000 37.65023  ? 601 3PH B C38  1 
HETATM 6218 C C39  . 3PH D 2 .   ? 100.72600 107.02800 130.25000 1.000 38.81606  ? 601 3PH B C39  1 
HETATM 6219 C C3A  . 3PH D 2 .   ? 99.25500  106.91200 129.80600 1.000 41.41683  ? 601 3PH B C3A  1 
HETATM 6220 C C3B  . 3PH D 2 .   ? 98.56400  105.82400 130.64200 1.000 40.67394  ? 601 3PH B C3B  1 
HETATM 6221 C C3C  . 3PH D 2 .   ? 97.85600  104.84400 129.70500 1.000 31.74473  ? 601 3PH B C3C  1 
HETATM 6222 C C3D  . 3PH D 2 .   ? 96.73400  105.58100 128.98100 1.000 36.39389  ? 601 3PH B C3D  1 
HETATM 6223 C C3E  . 3PH D 2 .   ? 95.66700  104.57300 128.57900 1.000 42.57801  ? 601 3PH B C3E  1 
HETATM 6224 C C3F  . 3PH D 2 .   ? 94.78600  104.25200 129.77300 1.000 40.33063  ? 601 3PH B C3F  1 
HETATM 6225 C C3G  . 3PH D 2 .   ? 94.06200  102.94400 129.49900 1.000 41.42956  ? 601 3PH B C3G  1 
HETATM 6226 C C3H  . 3PH D 2 .   ? 92.92000  102.80700 130.48800 1.000 39.18316  ? 601 3PH B C3H  1 
HETATM 6227 C C3I  . 3PH D 2 .   ? 92.45500  101.36200 130.50400 1.000 42.16417  ? 601 3PH B C3I  1 
HETATM 6228 H H11  . 3PH D 2 .   ? 112.03200 109.86000 124.60600 1.000 38.18836  ? 601 3PH B H11  1 
HETATM 6229 H H12  . 3PH D 2 .   ? 111.11600 108.62600 125.48700 1.000 38.01534  ? 601 3PH B H12  1 
HETATM 6230 H H2   . 3PH D 2 .   ? 109.98500 111.17600 124.25500 1.000 38.05623  ? 601 3PH B H2   1 
HETATM 6231 H H221 . 3PH D 2 .   ? 112.97400 111.96300 127.51700 1.000 37.32437  ? 601 3PH B H221 1 
HETATM 6232 H H222 . 3PH D 2 .   ? 112.78600 110.48600 126.57300 1.000 38.73720  ? 601 3PH B H222 1 
HETATM 6233 H H231 . 3PH D 2 .   ? 113.46200 111.59100 124.53200 1.000 37.89210  ? 601 3PH B H231 1 
HETATM 6234 H H232 . 3PH D 2 .   ? 113.52400 113.16400 125.35500 1.000 39.30296  ? 601 3PH B H232 1 
HETATM 6235 H H241 . 3PH D 2 .   ? 115.68600 111.44700 125.08700 1.000 37.88159  ? 601 3PH B H241 1 
HETATM 6236 H H242 . 3PH D 2 .   ? 115.08600 111.04600 126.71000 1.000 38.93829  ? 601 3PH B H242 1 
HETATM 6237 H H251 . 3PH D 2 .   ? 116.77000 112.97900 126.61300 1.000 38.84795  ? 601 3PH B H251 1 
HETATM 6238 H H252 . 3PH D 2 .   ? 115.51600 113.91800 125.78400 1.000 39.22170  ? 601 3PH B H252 1 
HETATM 6239 H H261 . 3PH D 2 .   ? 114.78100 112.49700 128.32800 1.000 38.02064  ? 601 3PH B H261 1 
HETATM 6240 H H262 . 3PH D 2 .   ? 114.17200 114.02700 127.67900 1.000 38.14525  ? 601 3PH B H262 1 
HETATM 6241 H H271 . 3PH D 2 .   ? 115.53400 114.79800 129.42300 1.000 39.18645  ? 601 3PH B H271 1 
HETATM 6242 H H272 . 3PH D 2 .   ? 116.68600 114.80300 128.07100 1.000 39.11256  ? 601 3PH B H272 1 
HETATM 6243 H H281 . 3PH D 2 .   ? 116.84500 112.18500 129.00100 1.000 38.08749  ? 601 3PH B H281 1 
HETATM 6244 H H282 . 3PH D 2 .   ? 116.66900 113.12300 130.49300 1.000 39.29509  ? 601 3PH B H282 1 
HETATM 6245 H H291 . 3PH D 2 .   ? 118.78300 113.39900 128.33400 1.000 38.34844  ? 601 3PH B H291 1 
HETATM 6246 H H292 . 3PH D 2 .   ? 118.48200 114.68700 129.51800 1.000 38.07886  ? 601 3PH B H292 1 
HETATM 6247 H H2A1 . 3PH D 2 .   ? 118.85300 111.87300 130.54300 1.000 39.07480  ? 601 3PH B H2A1 1 
HETATM 6248 H H2A2 . 3PH D 2 .   ? 119.29300 113.41600 131.30500 1.000 38.74240  ? 601 3PH B H2A2 1 
HETATM 6249 H H2B1 . 3PH D 2 .   ? 121.31100 112.19200 130.51200 1.000 39.15077  ? 601 3PH B H2B1 1 
HETATM 6250 H H2B2 . 3PH D 2 .   ? 120.65800 112.22000 128.86300 1.000 38.64633  ? 601 3PH B H2B2 1 
HETATM 6251 H H2C1 . 3PH D 2 .   ? 120.83000 114.57600 128.70500 1.000 39.00518  ? 601 3PH B H2C1 1 
HETATM 6252 H H2C2 . 3PH D 2 .   ? 120.96100 114.77300 130.46400 1.000 38.01640  ? 601 3PH B H2C2 1 
HETATM 6253 H H2D1 . 3PH D 2 .   ? 123.03700 113.58800 128.58800 1.000 38.07387  ? 601 3PH B H2D1 1 
HETATM 6254 H H2D2 . 3PH D 2 .   ? 123.17100 113.58600 130.35900 1.000 38.49857  ? 601 3PH B H2D2 1 
HETATM 6255 H H2E1 . 3PH D 2 .   ? 122.78300 116.09900 130.26900 1.000 38.61424  ? 601 3PH B H2E1 1 
HETATM 6256 H H2E2 . 3PH D 2 .   ? 122.98100 115.98600 128.51100 1.000 38.17524  ? 601 3PH B H2E2 1 
HETATM 6257 H H2F1 . 3PH D 2 .   ? 125.23900 115.49100 128.66300 1.000 38.46056  ? 601 3PH B H2F1 1 
HETATM 6258 H H2F2 . 3PH D 2 .   ? 125.07800 114.74700 130.26600 1.000 38.07460  ? 601 3PH B H2F2 1 
HETATM 6259 H H2G1 . 3PH D 2 .   ? 124.71500 116.92800 131.27800 1.000 38.84593  ? 601 3PH B H2G1 1 
HETATM 6260 H H2G2 . 3PH D 2 .   ? 124.74800 117.70400 129.68900 1.000 39.53714  ? 601 3PH B H2G2 1 
HETATM 6261 H H2H1 . 3PH D 2 .   ? 127.05600 115.99300 130.60700 1.000 38.27548  ? 601 3PH B H2H1 1 
HETATM 6262 H H2H2 . 3PH D 2 .   ? 126.93400 117.68300 131.13400 1.000 38.01374  ? 601 3PH B H2H2 1 
HETATM 6263 H H2I1 . 3PH D 2 .   ? 127.98300 118.15500 129.17500 1.000 38.03076  ? 601 3PH B H2I1 1 
HETATM 6264 H H2I2 . 3PH D 2 .   ? 126.39600 117.87800 128.43800 1.000 38.50441  ? 601 3PH B H2I2 1 
HETATM 6265 H H2I3 . 3PH D 2 .   ? 127.58900 116.56900 128.48200 1.000 38.72617  ? 601 3PH B H2I3 1 
HETATM 6266 H H31  . 3PH D 2 .   ? 107.90800 110.42900 125.46600 1.000 38.72574  ? 601 3PH B H31  1 
HETATM 6267 H H32  . 3PH D 2 .   ? 108.33800 109.39900 124.09000 1.000 38.00988  ? 601 3PH B H32  1 
HETATM 6268 H H321 . 3PH D 2 .   ? 105.84100 109.13100 126.20000 1.000 38.56811  ? 601 3PH B H321 1 
HETATM 6269 H H322 . 3PH D 2 .   ? 106.33900 108.77900 124.54800 1.000 38.67627  ? 601 3PH B H322 1 
HETATM 6270 H H331 . 3PH D 2 .   ? 105.69700 106.26600 125.35200 1.000 37.38117  ? 601 3PH B H331 1 
HETATM 6271 H H332 . 3PH D 2 .   ? 104.56900 107.38000 124.57200 1.000 36.83781  ? 601 3PH B H332 1 
HETATM 6272 H H341 . 3PH D 2 .   ? 104.27800 108.18300 127.15900 1.000 38.24640  ? 601 3PH B H341 1 
HETATM 6273 H H342 . 3PH D 2 .   ? 103.28900 106.94600 126.35800 1.000 37.29951  ? 601 3PH B H342 1 
HETATM 6274 H H351 . 3PH D 2 .   ? 105.73500 106.54800 128.11600 1.000 36.04737  ? 601 3PH B H351 1 
HETATM 6275 H H352 . 3PH D 2 .   ? 105.07200 105.25500 127.11200 1.000 36.32387  ? 601 3PH B H352 1 
HETATM 6276 H H361 . 3PH D 2 .   ? 103.84000 104.71400 128.90600 1.000 36.92085  ? 601 3PH B H361 1 
HETATM 6277 H H362 . 3PH D 2 .   ? 104.20200 106.23600 129.72000 1.000 38.68428  ? 601 3PH B H362 1 
HETATM 6278 H H371 . 3PH D 2 .   ? 102.40700 107.35500 128.44900 1.000 38.27447  ? 601 3PH B H371 1 
HETATM 6279 H H372 . 3PH D 2 .   ? 102.06000 105.83700 127.59600 1.000 37.34387  ? 601 3PH B H372 1 
HETATM 6280 H H381 . 3PH D 2 .   ? 100.79100 105.08400 129.29100 1.000 37.15323  ? 601 3PH B H381 1 
HETATM 6281 H H382 . 3PH D 2 .   ? 102.10300 105.36900 130.45200 1.000 37.57629  ? 601 3PH B H382 1 
HETATM 6282 H H391 . 3PH D 2 .   ? 100.77600 107.00400 131.33300 1.000 39.42459  ? 601 3PH B H391 1 
HETATM 6283 H H392 . 3PH D 2 .   ? 101.14600 107.96300 129.89000 1.000 38.60458  ? 601 3PH B H392 1 
HETATM 6284 H H3A1 . 3PH D 2 .   ? 98.75000  107.86400 129.96000 1.000 40.29865  ? 601 3PH B H3A1 1 
HETATM 6285 H H3A2 . 3PH D 2 .   ? 99.21800  106.64400 128.75400 1.000 37.67174  ? 601 3PH B H3A2 1 
HETATM 6286 H H3B1 . 3PH D 2 .   ? 97.83300  106.28400 131.29900 1.000 40.20740  ? 601 3PH B H3B1 1 
HETATM 6287 H H3B2 . 3PH D 2 .   ? 99.30100  105.29100 131.23100 1.000 39.47796  ? 601 3PH B H3B2 1 
HETATM 6288 H H3C1 . 3PH D 2 .   ? 97.44800  104.02100 130.28100 1.000 37.43862  ? 601 3PH B H3C1 1 
HETATM 6289 H H3C2 . 3PH D 2 .   ? 98.56800  104.46100 128.97700 1.000 37.73893  ? 601 3PH B H3C2 1 
HETATM 6290 H H3D1 . 3PH D 2 .   ? 97.12900  106.06400 128.09300 1.000 37.70953  ? 601 3PH B H3D1 1 
HETATM 6291 H H3D2 . 3PH D 2 .   ? 96.30200  106.32500 129.64100 1.000 39.14175  ? 601 3PH B H3D2 1 
HETATM 6292 H H3E1 . 3PH D 2 .   ? 96.14300  103.66500 128.23000 1.000 36.77779  ? 601 3PH B H3E1 1 
HETATM 6293 H H3E2 . 3PH D 2 .   ? 95.05800  104.99000 127.78600 1.000 38.02574  ? 601 3PH B H3E2 1 
HETATM 6294 H H3F1 . 3PH D 2 .   ? 94.05900  105.04500 129.91000 1.000 38.20488  ? 601 3PH B H3F1 1 
HETATM 6295 H H3F2 . 3PH D 2 .   ? 95.39100  104.15300 130.66900 1.000 38.43018  ? 601 3PH B H3F2 1 
HETATM 6296 H H3G1 . 3PH D 2 .   ? 94.75100  102.11400 129.61800 1.000 38.18818  ? 601 3PH B H3G1 1 
HETATM 6297 H H3G2 . 3PH D 2 .   ? 93.67300  102.95200 128.48600 1.000 37.91209  ? 601 3PH B H3G2 1 
HETATM 6298 H H3H1 . 3PH D 2 .   ? 93.26400  103.09100 131.47600 1.000 37.54495  ? 601 3PH B H3H1 1 
HETATM 6299 H H3H2 . 3PH D 2 .   ? 92.10100  103.45000 130.18600 1.000 38.98003  ? 601 3PH B H3H2 1 
HETATM 6300 H H3I1 . 3PH D 2 .   ? 91.42900  101.31800 130.84600 1.000 39.02626  ? 601 3PH B H3I1 1 
HETATM 6301 H H3I2 . 3PH D 2 .   ? 92.52500  100.95300 129.50300 1.000 38.60684  ? 601 3PH B H3I2 1 
HETATM 6302 H H3I3 . 3PH D 2 .   ? 93.08400  100.78700 131.17300 1.000 38.40763  ? 601 3PH B H3I3 1 
HETATM 6303 O O    . HOH E 3 .   ? 104.99200 109.99500 117.54600 1.000 22.24286  ? 701 HOH A O    1 
HETATM 6304 O O    . HOH F 3 .   ? 114.65600 109.65300 117.54600 1.000 21.94618  ? 701 HOH B O    1 
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