data_8YG7
# 
_entry.id   8YG7 
# 
_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   8YG7         pdb_00008yg7 10.2210/pdb8yg7/pdb 
WWPDB D_1300045592 ?            ?                   
# 
_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                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YG7 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              zhangzhenlei18@foxmail.com 
_pdbx_contact_author.name_first         Yang 
_pdbx_contact_author.name_last          Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4201-1416 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, Z.L.' 1 ? 
'Yang, F.'    2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Human serum albumin-copper(II) agent-Indomethacin complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Man, X.Y.' 1 ? 
primary 'Yang, F.'  2 ? 
# 
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 Albumin 66214.844 2   ? ? ? ? 
2 non-polymer syn 
;~{N},~{N}-dimethyl-7-propan-2-yl-3-thia-5-aza-1,6-diazonia-2$l^{3}-cupratricyclo[6.4.0.0^{2,6}]dodeca-1(12),4,6,8,10-pentaen-4-amine
;
312.901   2   ? ? ? ? 
3 non-polymer syn INDOMETHACIN 357.788   2   ? ? ? ? 
4 non-polymer syn 'PALMITIC ACID' 256.424   12  ? ? ? ? 
5 water       nat water 18.015    246 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        HSA 
# 
_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       
;HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRE
TYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYK
AAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH
TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEA
KDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV
NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKAD
DKETCFAEEGKKLVAASQAAL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRE
TYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYK
AAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH
TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEA
KDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV
NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKAD
DKETCFAEEGKKLVAASQAAL
;
_entity_poly.pdbx_strand_id                 A,I 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;~{N},~{N}-dimethyl-7-propan-2-yl-3-thia-5-aza-1,6-diazonia-2$l^{3}-cupratricyclo[6.4.0.0^{2,6}]dodeca-1(12),4,6,8,10-pentaen-4-amine
;
A1D6U 
3 INDOMETHACIN IMN   
4 'PALMITIC ACID' PLM   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   LYS n 
1 3   SER n 
1 4   GLU n 
1 5   VAL n 
1 6   ALA n 
1 7   HIS n 
1 8   ARG n 
1 9   PHE n 
1 10  LYS n 
1 11  ASP n 
1 12  LEU n 
1 13  GLY n 
1 14  GLU n 
1 15  GLU n 
1 16  ASN n 
1 17  PHE n 
1 18  LYS n 
1 19  ALA n 
1 20  LEU n 
1 21  VAL n 
1 22  LEU n 
1 23  ILE n 
1 24  ALA n 
1 25  PHE n 
1 26  ALA n 
1 27  GLN n 
1 28  TYR n 
1 29  LEU n 
1 30  GLN n 
1 31  GLN n 
1 32  CYS n 
1 33  PRO n 
1 34  PHE n 
1 35  GLU n 
1 36  ASP n 
1 37  HIS n 
1 38  VAL n 
1 39  LYS n 
1 40  LEU n 
1 41  VAL n 
1 42  ASN n 
1 43  GLU n 
1 44  VAL n 
1 45  THR n 
1 46  GLU n 
1 47  PHE n 
1 48  ALA n 
1 49  LYS n 
1 50  THR n 
1 51  CYS n 
1 52  VAL n 
1 53  ALA n 
1 54  ASP n 
1 55  GLU n 
1 56  SER n 
1 57  ALA n 
1 58  GLU n 
1 59  ASN n 
1 60  CYS n 
1 61  ASP n 
1 62  LYS n 
1 63  SER n 
1 64  LEU n 
1 65  HIS n 
1 66  THR n 
1 67  LEU n 
1 68  PHE n 
1 69  GLY n 
1 70  ASP n 
1 71  LYS n 
1 72  LEU n 
1 73  CYS n 
1 74  THR n 
1 75  VAL n 
1 76  ALA n 
1 77  THR n 
1 78  LEU n 
1 79  ARG n 
1 80  GLU n 
1 81  THR n 
1 82  TYR n 
1 83  GLY n 
1 84  GLU n 
1 85  MET n 
1 86  ALA n 
1 87  ASP n 
1 88  CYS n 
1 89  CYS n 
1 90  ALA n 
1 91  LYS n 
1 92  GLN n 
1 93  GLU n 
1 94  PRO n 
1 95  GLU n 
1 96  ARG n 
1 97  ASN n 
1 98  GLU n 
1 99  CYS n 
1 100 PHE n 
1 101 LEU n 
1 102 GLN n 
1 103 HIS n 
1 104 LYS n 
1 105 ASP n 
1 106 ASP n 
1 107 ASN n 
1 108 PRO n 
1 109 ASN n 
1 110 LEU n 
1 111 PRO n 
1 112 ARG n 
1 113 LEU n 
1 114 VAL n 
1 115 ARG n 
1 116 PRO n 
1 117 GLU n 
1 118 VAL n 
1 119 ASP n 
1 120 VAL n 
1 121 MET n 
1 122 CYS n 
1 123 THR n 
1 124 ALA n 
1 125 PHE n 
1 126 HIS n 
1 127 ASP n 
1 128 ASN n 
1 129 GLU n 
1 130 GLU n 
1 131 THR n 
1 132 PHE n 
1 133 LEU n 
1 134 LYS n 
1 135 LYS n 
1 136 TYR n 
1 137 LEU n 
1 138 TYR n 
1 139 GLU n 
1 140 ILE n 
1 141 ALA n 
1 142 ARG n 
1 143 ARG n 
1 144 HIS n 
1 145 PRO n 
1 146 TYR n 
1 147 PHE n 
1 148 TYR n 
1 149 ALA n 
1 150 PRO n 
1 151 GLU n 
1 152 LEU n 
1 153 LEU n 
1 154 PHE n 
1 155 PHE n 
1 156 ALA n 
1 157 LYS n 
1 158 ARG n 
1 159 TYR n 
1 160 LYS n 
1 161 ALA n 
1 162 ALA n 
1 163 PHE n 
1 164 THR n 
1 165 GLU n 
1 166 CYS n 
1 167 CYS n 
1 168 GLN n 
1 169 ALA n 
1 170 ALA n 
1 171 ASP n 
1 172 LYS n 
1 173 ALA n 
1 174 ALA n 
1 175 CYS n 
1 176 LEU n 
1 177 LEU n 
1 178 PRO n 
1 179 LYS n 
1 180 LEU n 
1 181 ASP n 
1 182 GLU n 
1 183 LEU n 
1 184 ARG n 
1 185 ASP n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 ALA n 
1 190 SER n 
1 191 SER n 
1 192 ALA n 
1 193 LYS n 
1 194 GLN n 
1 195 ARG n 
1 196 LEU n 
1 197 LYS n 
1 198 CYS n 
1 199 ALA n 
1 200 SER n 
1 201 LEU n 
1 202 GLN n 
1 203 LYS n 
1 204 PHE n 
1 205 GLY n 
1 206 GLU n 
1 207 ARG n 
1 208 ALA n 
1 209 PHE n 
1 210 LYS n 
1 211 ALA n 
1 212 TRP n 
1 213 ALA n 
1 214 VAL n 
1 215 ALA n 
1 216 ARG n 
1 217 LEU n 
1 218 SER n 
1 219 GLN n 
1 220 ARG n 
1 221 PHE n 
1 222 PRO n 
1 223 LYS n 
1 224 ALA n 
1 225 GLU n 
1 226 PHE n 
1 227 ALA n 
1 228 GLU n 
1 229 VAL n 
1 230 SER n 
1 231 LYS n 
1 232 LEU n 
1 233 VAL n 
1 234 THR n 
1 235 ASP n 
1 236 LEU n 
1 237 THR n 
1 238 LYS n 
1 239 VAL n 
1 240 HIS n 
1 241 THR n 
1 242 GLU n 
1 243 CYS n 
1 244 CYS n 
1 245 HIS n 
1 246 GLY n 
1 247 ASP n 
1 248 LEU n 
1 249 LEU n 
1 250 GLU n 
1 251 CYS n 
1 252 ALA n 
1 253 ASP n 
1 254 ASP n 
1 255 ARG n 
1 256 ALA n 
1 257 ASP n 
1 258 LEU n 
1 259 ALA n 
1 260 LYS n 
1 261 TYR n 
1 262 ILE n 
1 263 CYS n 
1 264 GLU n 
1 265 ASN n 
1 266 GLN n 
1 267 ASP n 
1 268 SER n 
1 269 ILE n 
1 270 SER n 
1 271 SER n 
1 272 LYS n 
1 273 LEU n 
1 274 LYS n 
1 275 GLU n 
1 276 CYS n 
1 277 CYS n 
1 278 GLU n 
1 279 LYS n 
1 280 PRO n 
1 281 LEU n 
1 282 LEU n 
1 283 GLU n 
1 284 LYS n 
1 285 SER n 
1 286 HIS n 
1 287 CYS n 
1 288 ILE n 
1 289 ALA n 
1 290 GLU n 
1 291 VAL n 
1 292 GLU n 
1 293 ASN n 
1 294 ASP n 
1 295 GLU n 
1 296 MET n 
1 297 PRO n 
1 298 ALA n 
1 299 ASP n 
1 300 LEU n 
1 301 PRO n 
1 302 SER n 
1 303 LEU n 
1 304 ALA n 
1 305 ALA n 
1 306 ASP n 
1 307 PHE n 
1 308 VAL n 
1 309 GLU n 
1 310 SER n 
1 311 LYS n 
1 312 ASP n 
1 313 VAL n 
1 314 CYS n 
1 315 LYS n 
1 316 ASN n 
1 317 TYR n 
1 318 ALA n 
1 319 GLU n 
1 320 ALA n 
1 321 LYS n 
1 322 ASP n 
1 323 VAL n 
1 324 PHE n 
1 325 LEU n 
1 326 GLY n 
1 327 MET n 
1 328 PHE n 
1 329 LEU n 
1 330 TYR n 
1 331 GLU n 
1 332 TYR n 
1 333 ALA n 
1 334 ARG n 
1 335 ARG n 
1 336 HIS n 
1 337 PRO n 
1 338 ASP n 
1 339 TYR n 
1 340 SER n 
1 341 VAL n 
1 342 VAL n 
1 343 LEU n 
1 344 LEU n 
1 345 LEU n 
1 346 ARG n 
1 347 LEU n 
1 348 ALA n 
1 349 LYS n 
1 350 THR n 
1 351 TYR n 
1 352 GLU n 
1 353 THR n 
1 354 THR n 
1 355 LEU n 
1 356 GLU n 
1 357 LYS n 
1 358 CYS n 
1 359 CYS n 
1 360 ALA n 
1 361 ALA n 
1 362 ALA n 
1 363 ASP n 
1 364 PRO n 
1 365 HIS n 
1 366 GLU n 
1 367 CYS n 
1 368 TYR n 
1 369 ALA n 
1 370 LYS n 
1 371 VAL n 
1 372 PHE n 
1 373 ASP n 
1 374 GLU n 
1 375 PHE n 
1 376 LYS n 
1 377 PRO n 
1 378 LEU n 
1 379 VAL n 
1 380 GLU n 
1 381 GLU n 
1 382 PRO n 
1 383 GLN n 
1 384 ASN n 
1 385 LEU n 
1 386 ILE n 
1 387 LYS n 
1 388 GLN n 
1 389 ASN n 
1 390 CYS n 
1 391 GLU n 
1 392 LEU n 
1 393 PHE n 
1 394 GLU n 
1 395 GLN n 
1 396 LEU n 
1 397 GLY n 
1 398 GLU n 
1 399 TYR n 
1 400 LYS n 
1 401 PHE n 
1 402 GLN n 
1 403 ASN n 
1 404 ALA n 
1 405 LEU n 
1 406 LEU n 
1 407 VAL n 
1 408 ARG n 
1 409 TYR n 
1 410 THR n 
1 411 LYS n 
1 412 LYS n 
1 413 VAL n 
1 414 PRO n 
1 415 GLN n 
1 416 VAL n 
1 417 SER n 
1 418 THR n 
1 419 PRO n 
1 420 THR n 
1 421 LEU n 
1 422 VAL n 
1 423 GLU n 
1 424 VAL n 
1 425 SER n 
1 426 ARG n 
1 427 ASN n 
1 428 LEU n 
1 429 GLY n 
1 430 LYS n 
1 431 VAL n 
1 432 GLY n 
1 433 SER n 
1 434 LYS n 
1 435 CYS n 
1 436 CYS n 
1 437 LYS n 
1 438 HIS n 
1 439 PRO n 
1 440 GLU n 
1 441 ALA n 
1 442 LYS n 
1 443 ARG n 
1 444 MET n 
1 445 PRO n 
1 446 CYS n 
1 447 ALA n 
1 448 GLU n 
1 449 ASP n 
1 450 TYR n 
1 451 LEU n 
1 452 SER n 
1 453 VAL n 
1 454 VAL n 
1 455 LEU n 
1 456 ASN n 
1 457 GLN n 
1 458 LEU n 
1 459 CYS n 
1 460 VAL n 
1 461 LEU n 
1 462 HIS n 
1 463 GLU n 
1 464 LYS n 
1 465 THR n 
1 466 PRO n 
1 467 VAL n 
1 468 SER n 
1 469 ASP n 
1 470 ARG n 
1 471 VAL n 
1 472 THR n 
1 473 LYS n 
1 474 CYS n 
1 475 CYS n 
1 476 THR n 
1 477 GLU n 
1 478 SER n 
1 479 LEU n 
1 480 VAL n 
1 481 ASN n 
1 482 ARG n 
1 483 ARG n 
1 484 PRO n 
1 485 CYS n 
1 486 PHE n 
1 487 SER n 
1 488 ALA n 
1 489 LEU n 
1 490 GLU n 
1 491 VAL n 
1 492 ASP n 
1 493 GLU n 
1 494 THR n 
1 495 TYR n 
1 496 VAL n 
1 497 PRO n 
1 498 LYS n 
1 499 GLU n 
1 500 PHE n 
1 501 ASN n 
1 502 ALA n 
1 503 GLU n 
1 504 THR n 
1 505 PHE n 
1 506 THR n 
1 507 PHE n 
1 508 HIS n 
1 509 ALA n 
1 510 ASP n 
1 511 ILE n 
1 512 CYS n 
1 513 THR n 
1 514 LEU n 
1 515 SER n 
1 516 GLU n 
1 517 LYS n 
1 518 GLU n 
1 519 ARG n 
1 520 GLN n 
1 521 ILE n 
1 522 LYS n 
1 523 LYS n 
1 524 GLN n 
1 525 THR n 
1 526 ALA n 
1 527 LEU n 
1 528 VAL n 
1 529 GLU n 
1 530 LEU n 
1 531 VAL n 
1 532 LYS n 
1 533 HIS n 
1 534 LYS n 
1 535 PRO n 
1 536 LYS n 
1 537 ALA n 
1 538 THR n 
1 539 LYS n 
1 540 GLU n 
1 541 GLN n 
1 542 LEU n 
1 543 LYS n 
1 544 ALA n 
1 545 VAL n 
1 546 MET n 
1 547 ASP n 
1 548 ASP n 
1 549 PHE n 
1 550 ALA n 
1 551 ALA n 
1 552 PHE n 
1 553 VAL n 
1 554 GLU n 
1 555 LYS n 
1 556 CYS n 
1 557 CYS n 
1 558 LYS n 
1 559 ALA n 
1 560 ASP n 
1 561 ASP n 
1 562 LYS n 
1 563 GLU n 
1 564 THR n 
1 565 CYS n 
1 566 PHE n 
1 567 ALA n 
1 568 GLU n 
1 569 GLU n 
1 570 GLY n 
1 571 LYS n 
1 572 LYS n 
1 573 LEU n 
1 574 VAL n 
1 575 ALA n 
1 576 ALA n 
1 577 SER n 
1 578 GLN n 
1 579 ALA n 
1 580 ALA n 
1 581 LEU 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                   581 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ALB, GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1D6U non-polymer         . 
;~{N},~{N}-dimethyl-7-propan-2-yl-3-thia-5-aza-1,6-diazonia-2$l^{3}-cupratricyclo[6.4.0.0^{2,6}]dodeca-1(12),4,6,8,10-pentaen-4-amine
;
? 'C12 H17 Cu N4 S 2' 312.901 
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 
IMN   non-polymer         . INDOMETHACIN ? 'C19 H16 Cl N O4'   357.788 
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 
PLM   non-polymer         . 'PALMITIC ACID' ? 'C16 H32 O2'        256.424 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   3   3   HIS HIS A . n 
A 1 2   LYS 2   4   4   LYS LYS A . n 
A 1 3   SER 3   5   5   SER SER A . n 
A 1 4   GLU 4   6   6   GLU GLU A . n 
A 1 5   VAL 5   7   7   VAL VAL A . n 
A 1 6   ALA 6   8   8   ALA ALA A . n 
A 1 7   HIS 7   9   9   HIS HIS A . n 
A 1 8   ARG 8   10  10  ARG ARG A . n 
A 1 9   PHE 9   11  11  PHE PHE A . n 
A 1 10  LYS 10  12  12  LYS LYS A . n 
A 1 11  ASP 11  13  13  ASP ASP A . n 
A 1 12  LEU 12  14  14  LEU LEU A . n 
A 1 13  GLY 13  15  15  GLY GLY A . n 
A 1 14  GLU 14  16  16  GLU GLU A . n 
A 1 15  GLU 15  17  17  GLU GLU A . n 
A 1 16  ASN 16  18  18  ASN ASN A . n 
A 1 17  PHE 17  19  19  PHE PHE A . n 
A 1 18  LYS 18  20  20  LYS LYS A . n 
A 1 19  ALA 19  21  21  ALA ALA A . n 
A 1 20  LEU 20  22  22  LEU LEU A . n 
A 1 21  VAL 21  23  23  VAL VAL A . n 
A 1 22  LEU 22  24  24  LEU LEU A . n 
A 1 23  ILE 23  25  25  ILE ILE A . n 
A 1 24  ALA 24  26  26  ALA ALA A . n 
A 1 25  PHE 25  27  27  PHE PHE A . n 
A 1 26  ALA 26  28  28  ALA ALA A . n 
A 1 27  GLN 27  29  29  GLN GLN A . n 
A 1 28  TYR 28  30  30  TYR TYR A . n 
A 1 29  LEU 29  31  31  LEU LEU A . n 
A 1 30  GLN 30  32  32  GLN GLN A . n 
A 1 31  GLN 31  33  33  GLN GLN A . n 
A 1 32  CYS 32  34  34  CYS CYS A . n 
A 1 33  PRO 33  35  35  PRO PRO A . n 
A 1 34  PHE 34  36  36  PHE PHE A . n 
A 1 35  GLU 35  37  37  GLU GLU A . n 
A 1 36  ASP 36  38  38  ASP ASP A . n 
A 1 37  HIS 37  39  39  HIS HIS A . n 
A 1 38  VAL 38  40  40  VAL VAL A . n 
A 1 39  LYS 39  41  41  LYS LYS A . n 
A 1 40  LEU 40  42  42  LEU LEU A . n 
A 1 41  VAL 41  43  43  VAL VAL A . n 
A 1 42  ASN 42  44  44  ASN ASN A . n 
A 1 43  GLU 43  45  45  GLU GLU A . n 
A 1 44  VAL 44  46  46  VAL VAL A . n 
A 1 45  THR 45  47  47  THR THR A . n 
A 1 46  GLU 46  48  48  GLU GLU A . n 
A 1 47  PHE 47  49  49  PHE PHE A . n 
A 1 48  ALA 48  50  50  ALA ALA A . n 
A 1 49  LYS 49  51  51  LYS LYS A . n 
A 1 50  THR 50  52  52  THR THR A . n 
A 1 51  CYS 51  53  53  CYS CYS A . n 
A 1 52  VAL 52  54  54  VAL VAL A . n 
A 1 53  ALA 53  55  55  ALA ALA A . n 
A 1 54  ASP 54  56  56  ASP ASP A . n 
A 1 55  GLU 55  57  57  GLU GLU A . n 
A 1 56  SER 56  58  58  SER SER A . n 
A 1 57  ALA 57  59  59  ALA ALA A . n 
A 1 58  GLU 58  60  60  GLU GLU A . n 
A 1 59  ASN 59  61  61  ASN ASN A . n 
A 1 60  CYS 60  62  62  CYS CYS A . n 
A 1 61  ASP 61  63  63  ASP ASP A . n 
A 1 62  LYS 62  64  64  LYS LYS A . n 
A 1 63  SER 63  65  65  SER SER A . n 
A 1 64  LEU 64  66  66  LEU LEU A . n 
A 1 65  HIS 65  67  67  HIS HIS A . n 
A 1 66  THR 66  68  68  THR THR A . n 
A 1 67  LEU 67  69  69  LEU LEU A . n 
A 1 68  PHE 68  70  70  PHE PHE A . n 
A 1 69  GLY 69  71  71  GLY GLY A . n 
A 1 70  ASP 70  72  72  ASP ASP A . n 
A 1 71  LYS 71  73  73  LYS LYS A . n 
A 1 72  LEU 72  74  74  LEU LEU A . n 
A 1 73  CYS 73  75  75  CYS CYS A . n 
A 1 74  THR 74  76  76  THR THR A . n 
A 1 75  VAL 75  77  77  VAL VAL A . n 
A 1 76  ALA 76  78  78  ALA ALA A . n 
A 1 77  THR 77  79  79  THR THR A . n 
A 1 78  LEU 78  80  80  LEU LEU A . n 
A 1 79  ARG 79  81  81  ARG ARG A . n 
A 1 80  GLU 80  82  82  GLU GLU A . n 
A 1 81  THR 81  83  83  THR THR A . n 
A 1 82  TYR 82  84  84  TYR TYR A . n 
A 1 83  GLY 83  85  85  GLY GLY A . n 
A 1 84  GLU 84  86  86  GLU GLU A . n 
A 1 85  MET 85  87  87  MET MET A . n 
A 1 86  ALA 86  88  88  ALA ALA A . n 
A 1 87  ASP 87  89  89  ASP ASP A . n 
A 1 88  CYS 88  90  90  CYS CYS A . n 
A 1 89  CYS 89  91  91  CYS CYS A . n 
A 1 90  ALA 90  92  92  ALA ALA A . n 
A 1 91  LYS 91  93  93  LYS LYS A . n 
A 1 92  GLN 92  94  94  GLN GLN A . n 
A 1 93  GLU 93  95  95  GLU GLU A . n 
A 1 94  PRO 94  96  96  PRO PRO A . n 
A 1 95  GLU 95  97  97  GLU GLU A . n 
A 1 96  ARG 96  98  98  ARG ARG A . n 
A 1 97  ASN 97  99  99  ASN ASN A . n 
A 1 98  GLU 98  100 100 GLU GLU A . n 
A 1 99  CYS 99  101 101 CYS CYS A . n 
A 1 100 PHE 100 102 102 PHE PHE A . n 
A 1 101 LEU 101 103 103 LEU LEU A . n 
A 1 102 GLN 102 104 104 GLN GLN A . n 
A 1 103 HIS 103 105 105 HIS HIS A . n 
A 1 104 LYS 104 106 106 LYS LYS A . n 
A 1 105 ASP 105 107 107 ASP ASP A . n 
A 1 106 ASP 106 108 108 ASP ASP A . n 
A 1 107 ASN 107 109 109 ASN ASN A . n 
A 1 108 PRO 108 110 110 PRO PRO A . n 
A 1 109 ASN 109 111 111 ASN ASN A . n 
A 1 110 LEU 110 112 112 LEU LEU A . n 
A 1 111 PRO 111 113 113 PRO PRO A . n 
A 1 112 ARG 112 114 114 ARG ARG A . n 
A 1 113 LEU 113 115 115 LEU LEU A . n 
A 1 114 VAL 114 116 116 VAL VAL A . n 
A 1 115 ARG 115 117 117 ARG ARG A . n 
A 1 116 PRO 116 118 118 PRO PRO A . n 
A 1 117 GLU 117 119 119 GLU GLU A . n 
A 1 118 VAL 118 120 120 VAL VAL A . n 
A 1 119 ASP 119 121 121 ASP ASP A . n 
A 1 120 VAL 120 122 122 VAL VAL A . n 
A 1 121 MET 121 123 123 MET MET A . n 
A 1 122 CYS 122 124 124 CYS CYS A . n 
A 1 123 THR 123 125 125 THR THR A . n 
A 1 124 ALA 124 126 126 ALA ALA A . n 
A 1 125 PHE 125 127 127 PHE PHE A . n 
A 1 126 HIS 126 128 128 HIS HIS A . n 
A 1 127 ASP 127 129 129 ASP ASP A . n 
A 1 128 ASN 128 130 130 ASN ASN A . n 
A 1 129 GLU 129 131 131 GLU GLU A . n 
A 1 130 GLU 130 132 132 GLU GLU A . n 
A 1 131 THR 131 133 133 THR THR A . n 
A 1 132 PHE 132 134 134 PHE PHE A . n 
A 1 133 LEU 133 135 135 LEU LEU A . n 
A 1 134 LYS 134 136 136 LYS LYS A . n 
A 1 135 LYS 135 137 137 LYS LYS A . n 
A 1 136 TYR 136 138 138 TYR TYR A . n 
A 1 137 LEU 137 139 139 LEU LEU A . n 
A 1 138 TYR 138 140 140 TYR TYR A . n 
A 1 139 GLU 139 141 141 GLU GLU A . n 
A 1 140 ILE 140 142 142 ILE ILE A . n 
A 1 141 ALA 141 143 143 ALA ALA A . n 
A 1 142 ARG 142 144 144 ARG ARG A . n 
A 1 143 ARG 143 145 145 ARG ARG A . n 
A 1 144 HIS 144 146 146 HIS HIS A . n 
A 1 145 PRO 145 147 147 PRO PRO A . n 
A 1 146 TYR 146 148 148 TYR TYR A . n 
A 1 147 PHE 147 149 149 PHE PHE A . n 
A 1 148 TYR 148 150 150 TYR TYR A . n 
A 1 149 ALA 149 151 151 ALA ALA A . n 
A 1 150 PRO 150 152 152 PRO PRO A . n 
A 1 151 GLU 151 153 153 GLU GLU A . n 
A 1 152 LEU 152 154 154 LEU LEU A . n 
A 1 153 LEU 153 155 155 LEU LEU A . n 
A 1 154 PHE 154 156 156 PHE PHE A . n 
A 1 155 PHE 155 157 157 PHE PHE A . n 
A 1 156 ALA 156 158 158 ALA ALA A . n 
A 1 157 LYS 157 159 159 LYS LYS A . n 
A 1 158 ARG 158 160 160 ARG ARG A . n 
A 1 159 TYR 159 161 161 TYR TYR A . n 
A 1 160 LYS 160 162 162 LYS LYS A . n 
A 1 161 ALA 161 163 163 ALA ALA A . n 
A 1 162 ALA 162 164 164 ALA ALA A . n 
A 1 163 PHE 163 165 165 PHE PHE A . n 
A 1 164 THR 164 166 166 THR THR A . n 
A 1 165 GLU 165 167 167 GLU GLU A . n 
A 1 166 CYS 166 168 168 CYS CYS A . n 
A 1 167 CYS 167 169 169 CYS CYS A . n 
A 1 168 GLN 168 170 170 GLN GLN A . n 
A 1 169 ALA 169 171 171 ALA ALA A . n 
A 1 170 ALA 170 172 172 ALA ALA A . n 
A 1 171 ASP 171 173 173 ASP ASP A . n 
A 1 172 LYS 172 174 174 LYS LYS A . n 
A 1 173 ALA 173 175 175 ALA ALA A . n 
A 1 174 ALA 174 176 176 ALA ALA A . n 
A 1 175 CYS 175 177 177 CYS CYS A . n 
A 1 176 LEU 176 178 178 LEU LEU A . n 
A 1 177 LEU 177 179 179 LEU LEU A . n 
A 1 178 PRO 178 180 180 PRO PRO A . n 
A 1 179 LYS 179 181 181 LYS LYS A . n 
A 1 180 LEU 180 182 182 LEU LEU A . n 
A 1 181 ASP 181 183 183 ASP ASP A . n 
A 1 182 GLU 182 184 184 GLU GLU A . n 
A 1 183 LEU 183 185 185 LEU LEU A . n 
A 1 184 ARG 184 186 186 ARG ARG A . n 
A 1 185 ASP 185 187 187 ASP ASP A . n 
A 1 186 GLU 186 188 188 GLU GLU A . n 
A 1 187 GLY 187 189 189 GLY GLY A . n 
A 1 188 LYS 188 190 190 LYS LYS A . n 
A 1 189 ALA 189 191 191 ALA ALA A . n 
A 1 190 SER 190 192 192 SER SER A . n 
A 1 191 SER 191 193 193 SER SER A . n 
A 1 192 ALA 192 194 194 ALA ALA A . n 
A 1 193 LYS 193 195 195 LYS LYS A . n 
A 1 194 GLN 194 196 196 GLN GLN A . n 
A 1 195 ARG 195 197 197 ARG ARG A . n 
A 1 196 LEU 196 198 198 LEU LEU A . n 
A 1 197 LYS 197 199 199 LYS LYS A . n 
A 1 198 CYS 198 200 200 CYS CYS A . n 
A 1 199 ALA 199 201 201 ALA ALA A . n 
A 1 200 SER 200 202 202 SER SER A . n 
A 1 201 LEU 201 203 203 LEU LEU A . n 
A 1 202 GLN 202 204 204 GLN GLN A . n 
A 1 203 LYS 203 205 205 LYS LYS A . n 
A 1 204 PHE 204 206 206 PHE PHE A . n 
A 1 205 GLY 205 207 207 GLY GLY A . n 
A 1 206 GLU 206 208 208 GLU GLU A . n 
A 1 207 ARG 207 209 209 ARG ARG A . n 
A 1 208 ALA 208 210 210 ALA ALA A . n 
A 1 209 PHE 209 211 211 PHE PHE A . n 
A 1 210 LYS 210 212 212 LYS LYS A . n 
A 1 211 ALA 211 213 213 ALA ALA A . n 
A 1 212 TRP 212 214 214 TRP TRP A . n 
A 1 213 ALA 213 215 215 ALA ALA A . n 
A 1 214 VAL 214 216 216 VAL VAL A . n 
A 1 215 ALA 215 217 217 ALA ALA A . n 
A 1 216 ARG 216 218 218 ARG ARG A . n 
A 1 217 LEU 217 219 219 LEU LEU A . n 
A 1 218 SER 218 220 220 SER SER A . n 
A 1 219 GLN 219 221 221 GLN GLN A . n 
A 1 220 ARG 220 222 222 ARG ARG A . n 
A 1 221 PHE 221 223 223 PHE PHE A . n 
A 1 222 PRO 222 224 224 PRO PRO A . n 
A 1 223 LYS 223 225 225 LYS LYS A . n 
A 1 224 ALA 224 226 226 ALA ALA A . n 
A 1 225 GLU 225 227 227 GLU GLU A . n 
A 1 226 PHE 226 228 228 PHE PHE A . n 
A 1 227 ALA 227 229 229 ALA ALA A . n 
A 1 228 GLU 228 230 230 GLU GLU A . n 
A 1 229 VAL 229 231 231 VAL VAL A . n 
A 1 230 SER 230 232 232 SER SER A . n 
A 1 231 LYS 231 233 233 LYS LYS A . n 
A 1 232 LEU 232 234 234 LEU LEU A . n 
A 1 233 VAL 233 235 235 VAL VAL A . n 
A 1 234 THR 234 236 236 THR THR A . n 
A 1 235 ASP 235 237 237 ASP ASP A . n 
A 1 236 LEU 236 238 238 LEU LEU A . n 
A 1 237 THR 237 239 239 THR THR A . n 
A 1 238 LYS 238 240 240 LYS LYS A . n 
A 1 239 VAL 239 241 241 VAL VAL A . n 
A 1 240 HIS 240 242 242 HIS HIS A . n 
A 1 241 THR 241 243 243 THR THR A . n 
A 1 242 GLU 242 244 244 GLU GLU A . n 
A 1 243 CYS 243 245 245 CYS CYS A . n 
A 1 244 CYS 244 246 246 CYS CYS A . n 
A 1 245 HIS 245 247 247 HIS HIS A . n 
A 1 246 GLY 246 248 248 GLY GLY A . n 
A 1 247 ASP 247 249 249 ASP ASP A . n 
A 1 248 LEU 248 250 250 LEU LEU A . n 
A 1 249 LEU 249 251 251 LEU LEU A . n 
A 1 250 GLU 250 252 252 GLU GLU A . n 
A 1 251 CYS 251 253 253 CYS CYS A . n 
A 1 252 ALA 252 254 254 ALA ALA A . n 
A 1 253 ASP 253 255 255 ASP ASP A . n 
A 1 254 ASP 254 256 256 ASP ASP A . n 
A 1 255 ARG 255 257 257 ARG ARG A . n 
A 1 256 ALA 256 258 258 ALA ALA A . n 
A 1 257 ASP 257 259 259 ASP ASP A . n 
A 1 258 LEU 258 260 260 LEU LEU A . n 
A 1 259 ALA 259 261 261 ALA ALA A . n 
A 1 260 LYS 260 262 262 LYS LYS A . n 
A 1 261 TYR 261 263 263 TYR TYR A . n 
A 1 262 ILE 262 264 264 ILE ILE A . n 
A 1 263 CYS 263 265 265 CYS CYS A . n 
A 1 264 GLU 264 266 266 GLU GLU A . n 
A 1 265 ASN 265 267 267 ASN ASN A . n 
A 1 266 GLN 266 268 268 GLN GLN A . n 
A 1 267 ASP 267 269 269 ASP ASP A . n 
A 1 268 SER 268 270 270 SER SER A . n 
A 1 269 ILE 269 271 271 ILE ILE A . n 
A 1 270 SER 270 272 272 SER SER A . n 
A 1 271 SER 271 273 273 SER SER A . n 
A 1 272 LYS 272 274 274 LYS LYS A . n 
A 1 273 LEU 273 275 275 LEU LEU A . n 
A 1 274 LYS 274 276 276 LYS LYS A . n 
A 1 275 GLU 275 277 277 GLU GLU A . n 
A 1 276 CYS 276 278 278 CYS CYS A . n 
A 1 277 CYS 277 279 279 CYS CYS A . n 
A 1 278 GLU 278 280 280 GLU GLU A . n 
A 1 279 LYS 279 281 281 LYS LYS A . n 
A 1 280 PRO 280 282 282 PRO PRO A . n 
A 1 281 LEU 281 283 283 LEU LEU A . n 
A 1 282 LEU 282 284 284 LEU LEU A . n 
A 1 283 GLU 283 285 285 GLU GLU A . n 
A 1 284 LYS 284 286 286 LYS LYS A . n 
A 1 285 SER 285 287 287 SER SER A . n 
A 1 286 HIS 286 288 288 HIS HIS A . n 
A 1 287 CYS 287 289 289 CYS CYS A . n 
A 1 288 ILE 288 290 290 ILE ILE A . n 
A 1 289 ALA 289 291 291 ALA ALA A . n 
A 1 290 GLU 290 292 292 GLU GLU A . n 
A 1 291 VAL 291 293 293 VAL VAL A . n 
A 1 292 GLU 292 294 294 GLU GLU A . n 
A 1 293 ASN 293 295 295 ASN ASN A . n 
A 1 294 ASP 294 296 296 ASP ASP A . n 
A 1 295 GLU 295 297 297 GLU GLU A . n 
A 1 296 MET 296 298 298 MET MET A . n 
A 1 297 PRO 297 299 299 PRO PRO A . n 
A 1 298 ALA 298 300 300 ALA ALA A . n 
A 1 299 ASP 299 301 301 ASP ASP A . n 
A 1 300 LEU 300 302 302 LEU LEU A . n 
A 1 301 PRO 301 303 303 PRO PRO A . n 
A 1 302 SER 302 304 304 SER SER A . n 
A 1 303 LEU 303 305 305 LEU LEU A . n 
A 1 304 ALA 304 306 306 ALA ALA A . n 
A 1 305 ALA 305 307 307 ALA ALA A . n 
A 1 306 ASP 306 308 308 ASP ASP A . n 
A 1 307 PHE 307 309 309 PHE PHE A . n 
A 1 308 VAL 308 310 310 VAL VAL A . n 
A 1 309 GLU 309 311 311 GLU GLU A . n 
A 1 310 SER 310 312 312 SER SER A . n 
A 1 311 LYS 311 313 313 LYS LYS A . n 
A 1 312 ASP 312 314 314 ASP ASP A . n 
A 1 313 VAL 313 315 315 VAL VAL A . n 
A 1 314 CYS 314 316 316 CYS CYS A . n 
A 1 315 LYS 315 317 317 LYS LYS A . n 
A 1 316 ASN 316 318 318 ASN ASN A . n 
A 1 317 TYR 317 319 319 TYR TYR A . n 
A 1 318 ALA 318 320 320 ALA ALA A . n 
A 1 319 GLU 319 321 321 GLU GLU A . n 
A 1 320 ALA 320 322 322 ALA ALA A . n 
A 1 321 LYS 321 323 323 LYS LYS A . n 
A 1 322 ASP 322 324 324 ASP ASP A . n 
A 1 323 VAL 323 325 325 VAL VAL A . n 
A 1 324 PHE 324 326 326 PHE PHE A . n 
A 1 325 LEU 325 327 327 LEU LEU A . n 
A 1 326 GLY 326 328 328 GLY GLY A . n 
A 1 327 MET 327 329 329 MET MET A . n 
A 1 328 PHE 328 330 330 PHE PHE A . n 
A 1 329 LEU 329 331 331 LEU LEU A . n 
A 1 330 TYR 330 332 332 TYR TYR A . n 
A 1 331 GLU 331 333 333 GLU GLU A . n 
A 1 332 TYR 332 334 334 TYR TYR A . n 
A 1 333 ALA 333 335 335 ALA ALA A . n 
A 1 334 ARG 334 336 336 ARG ARG A . n 
A 1 335 ARG 335 337 337 ARG ARG A . n 
A 1 336 HIS 336 338 338 HIS HIS A . n 
A 1 337 PRO 337 339 339 PRO PRO A . n 
A 1 338 ASP 338 340 340 ASP ASP A . n 
A 1 339 TYR 339 341 341 TYR TYR A . n 
A 1 340 SER 340 342 342 SER SER A . n 
A 1 341 VAL 341 343 343 VAL VAL A . n 
A 1 342 VAL 342 344 344 VAL VAL A . n 
A 1 343 LEU 343 345 345 LEU LEU A . n 
A 1 344 LEU 344 346 346 LEU LEU A . n 
A 1 345 LEU 345 347 347 LEU LEU A . n 
A 1 346 ARG 346 348 348 ARG ARG A . n 
A 1 347 LEU 347 349 349 LEU LEU A . n 
A 1 348 ALA 348 350 350 ALA ALA A . n 
A 1 349 LYS 349 351 351 LYS LYS A . n 
A 1 350 THR 350 352 352 THR THR A . n 
A 1 351 TYR 351 353 353 TYR TYR A . n 
A 1 352 GLU 352 354 354 GLU GLU A . n 
A 1 353 THR 353 355 355 THR THR A . n 
A 1 354 THR 354 356 356 THR THR A . n 
A 1 355 LEU 355 357 357 LEU LEU A . n 
A 1 356 GLU 356 358 358 GLU GLU A . n 
A 1 357 LYS 357 359 359 LYS LYS A . n 
A 1 358 CYS 358 360 360 CYS CYS A . n 
A 1 359 CYS 359 361 361 CYS CYS A . n 
A 1 360 ALA 360 362 362 ALA ALA A . n 
A 1 361 ALA 361 363 363 ALA ALA A . n 
A 1 362 ALA 362 364 364 ALA ALA A . n 
A 1 363 ASP 363 365 365 ASP ASP A . n 
A 1 364 PRO 364 366 366 PRO PRO A . n 
A 1 365 HIS 365 367 367 HIS HIS A . n 
A 1 366 GLU 366 368 368 GLU GLU A . n 
A 1 367 CYS 367 369 369 CYS CYS A . n 
A 1 368 TYR 368 370 370 TYR TYR A . n 
A 1 369 ALA 369 371 371 ALA ALA A . n 
A 1 370 LYS 370 372 372 LYS LYS A . n 
A 1 371 VAL 371 373 373 VAL VAL A . n 
A 1 372 PHE 372 374 374 PHE PHE A . n 
A 1 373 ASP 373 375 375 ASP ASP A . n 
A 1 374 GLU 374 376 376 GLU GLU A . n 
A 1 375 PHE 375 377 377 PHE PHE A . n 
A 1 376 LYS 376 378 378 LYS LYS A . n 
A 1 377 PRO 377 379 379 PRO PRO A . n 
A 1 378 LEU 378 380 380 LEU LEU A . n 
A 1 379 VAL 379 381 381 VAL VAL A . n 
A 1 380 GLU 380 382 382 GLU GLU A . n 
A 1 381 GLU 381 383 383 GLU GLU A . n 
A 1 382 PRO 382 384 384 PRO PRO A . n 
A 1 383 GLN 383 385 385 GLN GLN A . n 
A 1 384 ASN 384 386 386 ASN ASN A . n 
A 1 385 LEU 385 387 387 LEU LEU A . n 
A 1 386 ILE 386 388 388 ILE ILE A . n 
A 1 387 LYS 387 389 389 LYS LYS A . n 
A 1 388 GLN 388 390 390 GLN GLN A . n 
A 1 389 ASN 389 391 391 ASN ASN A . n 
A 1 390 CYS 390 392 392 CYS CYS A . n 
A 1 391 GLU 391 393 393 GLU GLU A . n 
A 1 392 LEU 392 394 394 LEU LEU A . n 
A 1 393 PHE 393 395 395 PHE PHE A . n 
A 1 394 GLU 394 396 396 GLU GLU A . n 
A 1 395 GLN 395 397 397 GLN GLN A . n 
A 1 396 LEU 396 398 398 LEU LEU A . n 
A 1 397 GLY 397 399 399 GLY GLY A . n 
A 1 398 GLU 398 400 400 GLU GLU A . n 
A 1 399 TYR 399 401 401 TYR TYR A . n 
A 1 400 LYS 400 402 402 LYS LYS A . n 
A 1 401 PHE 401 403 403 PHE PHE A . n 
A 1 402 GLN 402 404 404 GLN GLN A . n 
A 1 403 ASN 403 405 405 ASN ASN A . n 
A 1 404 ALA 404 406 406 ALA ALA A . n 
A 1 405 LEU 405 407 407 LEU LEU A . n 
A 1 406 LEU 406 408 408 LEU LEU A . n 
A 1 407 VAL 407 409 409 VAL VAL A . n 
A 1 408 ARG 408 410 410 ARG ARG A . n 
A 1 409 TYR 409 411 411 TYR TYR A . n 
A 1 410 THR 410 412 412 THR THR A . n 
A 1 411 LYS 411 413 413 LYS LYS A . n 
A 1 412 LYS 412 414 414 LYS LYS A . n 
A 1 413 VAL 413 415 415 VAL VAL A . n 
A 1 414 PRO 414 416 416 PRO PRO A . n 
A 1 415 GLN 415 417 417 GLN GLN A . n 
A 1 416 VAL 416 418 418 VAL VAL A . n 
A 1 417 SER 417 419 419 SER SER A . n 
A 1 418 THR 418 420 420 THR THR A . n 
A 1 419 PRO 419 421 421 PRO PRO A . n 
A 1 420 THR 420 422 422 THR THR A . n 
A 1 421 LEU 421 423 423 LEU LEU A . n 
A 1 422 VAL 422 424 424 VAL VAL A . n 
A 1 423 GLU 423 425 425 GLU GLU A . n 
A 1 424 VAL 424 426 426 VAL VAL A . n 
A 1 425 SER 425 427 427 SER SER A . n 
A 1 426 ARG 426 428 428 ARG ARG A . n 
A 1 427 ASN 427 429 429 ASN ASN A . n 
A 1 428 LEU 428 430 430 LEU LEU A . n 
A 1 429 GLY 429 431 431 GLY GLY A . n 
A 1 430 LYS 430 432 432 LYS LYS A . n 
A 1 431 VAL 431 433 433 VAL VAL A . n 
A 1 432 GLY 432 434 434 GLY GLY A . n 
A 1 433 SER 433 435 435 SER SER A . n 
A 1 434 LYS 434 436 436 LYS LYS A . n 
A 1 435 CYS 435 437 437 CYS CYS A . n 
A 1 436 CYS 436 438 438 CYS CYS A . n 
A 1 437 LYS 437 439 439 LYS LYS A . n 
A 1 438 HIS 438 440 440 HIS HIS A . n 
A 1 439 PRO 439 441 441 PRO PRO A . n 
A 1 440 GLU 440 442 442 GLU GLU A . n 
A 1 441 ALA 441 443 443 ALA ALA A . n 
A 1 442 LYS 442 444 444 LYS LYS A . n 
A 1 443 ARG 443 445 445 ARG ARG A . n 
A 1 444 MET 444 446 446 MET MET A . n 
A 1 445 PRO 445 447 447 PRO PRO A . n 
A 1 446 CYS 446 448 448 CYS CYS A . n 
A 1 447 ALA 447 449 449 ALA ALA A . n 
A 1 448 GLU 448 450 450 GLU GLU A . n 
A 1 449 ASP 449 451 451 ASP ASP A . n 
A 1 450 TYR 450 452 452 TYR TYR A . n 
A 1 451 LEU 451 453 453 LEU LEU A . n 
A 1 452 SER 452 454 454 SER SER A . n 
A 1 453 VAL 453 455 455 VAL VAL A . n 
A 1 454 VAL 454 456 456 VAL VAL A . n 
A 1 455 LEU 455 457 457 LEU LEU A . n 
A 1 456 ASN 456 458 458 ASN ASN A . n 
A 1 457 GLN 457 459 459 GLN GLN A . n 
A 1 458 LEU 458 460 460 LEU LEU A . n 
A 1 459 CYS 459 461 461 CYS CYS A . n 
A 1 460 VAL 460 462 462 VAL VAL A . n 
A 1 461 LEU 461 463 463 LEU LEU A . n 
A 1 462 HIS 462 464 464 HIS HIS A . n 
A 1 463 GLU 463 465 465 GLU GLU A . n 
A 1 464 LYS 464 466 466 LYS LYS A . n 
A 1 465 THR 465 467 467 THR THR A . n 
A 1 466 PRO 466 468 468 PRO PRO A . n 
A 1 467 VAL 467 469 469 VAL VAL A . n 
A 1 468 SER 468 470 470 SER SER A . n 
A 1 469 ASP 469 471 471 ASP ASP A . n 
A 1 470 ARG 470 472 472 ARG ARG A . n 
A 1 471 VAL 471 473 473 VAL VAL A . n 
A 1 472 THR 472 474 474 THR THR A . n 
A 1 473 LYS 473 475 475 LYS LYS A . n 
A 1 474 CYS 474 476 476 CYS CYS A . n 
A 1 475 CYS 475 477 477 CYS CYS A . n 
A 1 476 THR 476 478 478 THR THR A . n 
A 1 477 GLU 477 479 479 GLU GLU A . n 
A 1 478 SER 478 480 480 SER SER A . n 
A 1 479 LEU 479 481 481 LEU LEU A . n 
A 1 480 VAL 480 482 482 VAL VAL A . n 
A 1 481 ASN 481 483 483 ASN ASN A . n 
A 1 482 ARG 482 484 484 ARG ARG A . n 
A 1 483 ARG 483 485 485 ARG ARG A . n 
A 1 484 PRO 484 486 486 PRO PRO A . n 
A 1 485 CYS 485 487 487 CYS CYS A . n 
A 1 486 PHE 486 488 488 PHE PHE A . n 
A 1 487 SER 487 489 489 SER SER A . n 
A 1 488 ALA 488 490 490 ALA ALA A . n 
A 1 489 LEU 489 491 491 LEU LEU A . n 
A 1 490 GLU 490 492 492 GLU GLU A . n 
A 1 491 VAL 491 493 493 VAL VAL A . n 
A 1 492 ASP 492 494 494 ASP ASP A . n 
A 1 493 GLU 493 495 495 GLU GLU A . n 
A 1 494 THR 494 496 496 THR THR A . n 
A 1 495 TYR 495 497 497 TYR TYR A . n 
A 1 496 VAL 496 498 498 VAL VAL A . n 
A 1 497 PRO 497 499 499 PRO PRO A . n 
A 1 498 LYS 498 500 500 LYS LYS A . n 
A 1 499 GLU 499 501 501 GLU GLU A . n 
A 1 500 PHE 500 502 502 PHE PHE A . n 
A 1 501 ASN 501 503 503 ASN ASN A . n 
A 1 502 ALA 502 504 504 ALA ALA A . n 
A 1 503 GLU 503 505 505 GLU GLU A . n 
A 1 504 THR 504 506 506 THR THR A . n 
A 1 505 PHE 505 507 507 PHE PHE A . n 
A 1 506 THR 506 508 508 THR THR A . n 
A 1 507 PHE 507 509 509 PHE PHE A . n 
A 1 508 HIS 508 510 510 HIS HIS A . n 
A 1 509 ALA 509 511 511 ALA ALA A . n 
A 1 510 ASP 510 512 512 ASP ASP A . n 
A 1 511 ILE 511 513 513 ILE ILE A . n 
A 1 512 CYS 512 514 514 CYS CYS A . n 
A 1 513 THR 513 515 515 THR THR A . n 
A 1 514 LEU 514 516 516 LEU LEU A . n 
A 1 515 SER 515 517 517 SER SER A . n 
A 1 516 GLU 516 518 518 GLU GLU A . n 
A 1 517 LYS 517 519 519 LYS LYS A . n 
A 1 518 GLU 518 520 520 GLU GLU A . n 
A 1 519 ARG 519 521 521 ARG ARG A . n 
A 1 520 GLN 520 522 522 GLN GLN A . n 
A 1 521 ILE 521 523 523 ILE ILE A . n 
A 1 522 LYS 522 524 524 LYS LYS A . n 
A 1 523 LYS 523 525 525 LYS LYS A . n 
A 1 524 GLN 524 526 526 GLN GLN A . n 
A 1 525 THR 525 527 527 THR THR A . n 
A 1 526 ALA 526 528 528 ALA ALA A . n 
A 1 527 LEU 527 529 529 LEU LEU A . n 
A 1 528 VAL 528 530 530 VAL VAL A . n 
A 1 529 GLU 529 531 531 GLU GLU A . n 
A 1 530 LEU 530 532 532 LEU LEU A . n 
A 1 531 VAL 531 533 533 VAL VAL A . n 
A 1 532 LYS 532 534 534 LYS LYS A . n 
A 1 533 HIS 533 535 535 HIS HIS A . n 
A 1 534 LYS 534 536 536 LYS LYS A . n 
A 1 535 PRO 535 537 537 PRO PRO A . n 
A 1 536 LYS 536 538 538 LYS LYS A . n 
A 1 537 ALA 537 539 539 ALA ALA A . n 
A 1 538 THR 538 540 540 THR THR A . n 
A 1 539 LYS 539 541 541 LYS LYS A . n 
A 1 540 GLU 540 542 542 GLU GLU A . n 
A 1 541 GLN 541 543 543 GLN GLN A . n 
A 1 542 LEU 542 544 544 LEU LEU A . n 
A 1 543 LYS 543 545 545 LYS LYS A . n 
A 1 544 ALA 544 546 546 ALA ALA A . n 
A 1 545 VAL 545 547 547 VAL VAL A . n 
A 1 546 MET 546 548 548 MET MET A . n 
A 1 547 ASP 547 549 549 ASP ASP A . n 
A 1 548 ASP 548 550 550 ASP ASP A . n 
A 1 549 PHE 549 551 551 PHE PHE A . n 
A 1 550 ALA 550 552 552 ALA ALA A . n 
A 1 551 ALA 551 553 553 ALA ALA A . n 
A 1 552 PHE 552 554 554 PHE PHE A . n 
A 1 553 VAL 553 555 555 VAL VAL A . n 
A 1 554 GLU 554 556 556 GLU GLU A . n 
A 1 555 LYS 555 557 557 LYS LYS A . n 
A 1 556 CYS 556 558 558 CYS CYS A . n 
A 1 557 CYS 557 559 559 CYS CYS A . n 
A 1 558 LYS 558 560 560 LYS LYS A . n 
A 1 559 ALA 559 561 561 ALA ALA A . n 
A 1 560 ASP 560 562 562 ASP ASP A . n 
A 1 561 ASP 561 563 563 ASP ASP A . n 
A 1 562 LYS 562 564 564 LYS LYS A . n 
A 1 563 GLU 563 565 565 GLU GLU A . n 
A 1 564 THR 564 566 566 THR THR A . n 
A 1 565 CYS 565 567 567 CYS CYS A . n 
A 1 566 PHE 566 568 568 PHE PHE A . n 
A 1 567 ALA 567 569 569 ALA ALA A . n 
A 1 568 GLU 568 570 570 GLU GLU A . n 
A 1 569 GLU 569 571 571 GLU GLU A . n 
A 1 570 GLY 570 572 572 GLY GLY A . n 
A 1 571 LYS 571 573 573 LYS LYS A . n 
A 1 572 LYS 572 574 574 LYS LYS A . n 
A 1 573 LEU 573 575 575 LEU LEU A . n 
A 1 574 VAL 574 576 576 VAL VAL A . n 
A 1 575 ALA 575 577 577 ALA ALA A . n 
A 1 576 ALA 576 578 578 ALA ALA A . n 
A 1 577 SER 577 579 579 SER SER A . n 
A 1 578 GLN 578 580 580 GLN GLN A . n 
A 1 579 ALA 579 581 581 ALA ALA A . n 
A 1 580 ALA 580 582 582 ALA ALA A . n 
A 1 581 LEU 581 583 583 LEU LEU A . n 
B 1 1   HIS 1   3   3   HIS HIS I . n 
B 1 2   LYS 2   4   4   LYS LYS I . n 
B 1 3   SER 3   5   5   SER SER I . n 
B 1 4   GLU 4   6   6   GLU GLU I . n 
B 1 5   VAL 5   7   7   VAL VAL I . n 
B 1 6   ALA 6   8   8   ALA ALA I . n 
B 1 7   HIS 7   9   9   HIS HIS I . n 
B 1 8   ARG 8   10  10  ARG ARG I . n 
B 1 9   PHE 9   11  11  PHE PHE I . n 
B 1 10  LYS 10  12  12  LYS LYS I . n 
B 1 11  ASP 11  13  13  ASP ASP I . n 
B 1 12  LEU 12  14  14  LEU LEU I . n 
B 1 13  GLY 13  15  15  GLY GLY I . n 
B 1 14  GLU 14  16  16  GLU GLU I . n 
B 1 15  GLU 15  17  17  GLU GLU I . n 
B 1 16  ASN 16  18  18  ASN ASN I . n 
B 1 17  PHE 17  19  19  PHE PHE I . n 
B 1 18  LYS 18  20  20  LYS LYS I . n 
B 1 19  ALA 19  21  21  ALA ALA I . n 
B 1 20  LEU 20  22  22  LEU LEU I . n 
B 1 21  VAL 21  23  23  VAL VAL I . n 
B 1 22  LEU 22  24  24  LEU LEU I . n 
B 1 23  ILE 23  25  25  ILE ILE I . n 
B 1 24  ALA 24  26  26  ALA ALA I . n 
B 1 25  PHE 25  27  27  PHE PHE I . n 
B 1 26  ALA 26  28  28  ALA ALA I . n 
B 1 27  GLN 27  29  29  GLN GLN I . n 
B 1 28  TYR 28  30  30  TYR TYR I . n 
B 1 29  LEU 29  31  31  LEU LEU I . n 
B 1 30  GLN 30  32  32  GLN GLN I . n 
B 1 31  GLN 31  33  33  GLN GLN I . n 
B 1 32  CYS 32  34  34  CYS CYS I . n 
B 1 33  PRO 33  35  35  PRO PRO I . n 
B 1 34  PHE 34  36  36  PHE PHE I . n 
B 1 35  GLU 35  37  37  GLU GLU I . n 
B 1 36  ASP 36  38  38  ASP ASP I . n 
B 1 37  HIS 37  39  39  HIS HIS I . n 
B 1 38  VAL 38  40  40  VAL VAL I . n 
B 1 39  LYS 39  41  41  LYS LYS I . n 
B 1 40  LEU 40  42  42  LEU LEU I . n 
B 1 41  VAL 41  43  43  VAL VAL I . n 
B 1 42  ASN 42  44  44  ASN ASN I . n 
B 1 43  GLU 43  45  45  GLU GLU I . n 
B 1 44  VAL 44  46  46  VAL VAL I . n 
B 1 45  THR 45  47  47  THR THR I . n 
B 1 46  GLU 46  48  48  GLU GLU I . n 
B 1 47  PHE 47  49  49  PHE PHE I . n 
B 1 48  ALA 48  50  50  ALA ALA I . n 
B 1 49  LYS 49  51  51  LYS LYS I . n 
B 1 50  THR 50  52  52  THR THR I . n 
B 1 51  CYS 51  53  53  CYS CYS I . n 
B 1 52  VAL 52  54  54  VAL VAL I . n 
B 1 53  ALA 53  55  55  ALA ALA I . n 
B 1 54  ASP 54  56  56  ASP ASP I . n 
B 1 55  GLU 55  57  57  GLU GLU I . n 
B 1 56  SER 56  58  58  SER SER I . n 
B 1 57  ALA 57  59  59  ALA ALA I . n 
B 1 58  GLU 58  60  60  GLU GLU I . n 
B 1 59  ASN 59  61  61  ASN ASN I . n 
B 1 60  CYS 60  62  62  CYS CYS I . n 
B 1 61  ASP 61  63  63  ASP ASP I . n 
B 1 62  LYS 62  64  64  LYS LYS I . n 
B 1 63  SER 63  65  65  SER SER I . n 
B 1 64  LEU 64  66  66  LEU LEU I . n 
B 1 65  HIS 65  67  67  HIS HIS I . n 
B 1 66  THR 66  68  68  THR THR I . n 
B 1 67  LEU 67  69  69  LEU LEU I . n 
B 1 68  PHE 68  70  70  PHE PHE I . n 
B 1 69  GLY 69  71  71  GLY GLY I . n 
B 1 70  ASP 70  72  72  ASP ASP I . n 
B 1 71  LYS 71  73  73  LYS LYS I . n 
B 1 72  LEU 72  74  74  LEU LEU I . n 
B 1 73  CYS 73  75  75  CYS CYS I . n 
B 1 74  THR 74  76  76  THR THR I . n 
B 1 75  VAL 75  77  77  VAL VAL I . n 
B 1 76  ALA 76  78  78  ALA ALA I . n 
B 1 77  THR 77  79  79  THR THR I . n 
B 1 78  LEU 78  80  80  LEU LEU I . n 
B 1 79  ARG 79  81  81  ARG ARG I . n 
B 1 80  GLU 80  82  82  GLU GLU I . n 
B 1 81  THR 81  83  83  THR THR I . n 
B 1 82  TYR 82  84  84  TYR TYR I . n 
B 1 83  GLY 83  85  85  GLY GLY I . n 
B 1 84  GLU 84  86  86  GLU GLU I . n 
B 1 85  MET 85  87  87  MET MET I . n 
B 1 86  ALA 86  88  88  ALA ALA I . n 
B 1 87  ASP 87  89  89  ASP ASP I . n 
B 1 88  CYS 88  90  90  CYS CYS I . n 
B 1 89  CYS 89  91  91  CYS CYS I . n 
B 1 90  ALA 90  92  92  ALA ALA I . n 
B 1 91  LYS 91  93  93  LYS LYS I . n 
B 1 92  GLN 92  94  94  GLN GLN I . n 
B 1 93  GLU 93  95  95  GLU GLU I . n 
B 1 94  PRO 94  96  96  PRO PRO I . n 
B 1 95  GLU 95  97  97  GLU GLU I . n 
B 1 96  ARG 96  98  98  ARG ARG I . n 
B 1 97  ASN 97  99  99  ASN ASN I . n 
B 1 98  GLU 98  100 100 GLU GLU I . n 
B 1 99  CYS 99  101 101 CYS CYS I . n 
B 1 100 PHE 100 102 102 PHE PHE I . n 
B 1 101 LEU 101 103 103 LEU LEU I . n 
B 1 102 GLN 102 104 104 GLN GLN I . n 
B 1 103 HIS 103 105 105 HIS HIS I . n 
B 1 104 LYS 104 106 106 LYS LYS I . n 
B 1 105 ASP 105 107 107 ASP ASP I . n 
B 1 106 ASP 106 108 108 ASP ASP I . n 
B 1 107 ASN 107 109 109 ASN ASN I . n 
B 1 108 PRO 108 110 110 PRO PRO I . n 
B 1 109 ASN 109 111 111 ASN ASN I . n 
B 1 110 LEU 110 112 112 LEU LEU I . n 
B 1 111 PRO 111 113 113 PRO PRO I . n 
B 1 112 ARG 112 114 114 ARG ARG I . n 
B 1 113 LEU 113 115 115 LEU LEU I . n 
B 1 114 VAL 114 116 116 VAL VAL I . n 
B 1 115 ARG 115 117 117 ARG ARG I . n 
B 1 116 PRO 116 118 118 PRO PRO I . n 
B 1 117 GLU 117 119 119 GLU GLU I . n 
B 1 118 VAL 118 120 120 VAL VAL I . n 
B 1 119 ASP 119 121 121 ASP ASP I . n 
B 1 120 VAL 120 122 122 VAL VAL I . n 
B 1 121 MET 121 123 123 MET MET I . n 
B 1 122 CYS 122 124 124 CYS CYS I . n 
B 1 123 THR 123 125 125 THR THR I . n 
B 1 124 ALA 124 126 126 ALA ALA I . n 
B 1 125 PHE 125 127 127 PHE PHE I . n 
B 1 126 HIS 126 128 128 HIS HIS I . n 
B 1 127 ASP 127 129 129 ASP ASP I . n 
B 1 128 ASN 128 130 130 ASN ASN I . n 
B 1 129 GLU 129 131 131 GLU GLU I . n 
B 1 130 GLU 130 132 132 GLU GLU I . n 
B 1 131 THR 131 133 133 THR THR I . n 
B 1 132 PHE 132 134 134 PHE PHE I . n 
B 1 133 LEU 133 135 135 LEU LEU I . n 
B 1 134 LYS 134 136 136 LYS LYS I . n 
B 1 135 LYS 135 137 137 LYS LYS I . n 
B 1 136 TYR 136 138 138 TYR TYR I . n 
B 1 137 LEU 137 139 139 LEU LEU I . n 
B 1 138 TYR 138 140 140 TYR TYR I . n 
B 1 139 GLU 139 141 141 GLU GLU I . n 
B 1 140 ILE 140 142 142 ILE ILE I . n 
B 1 141 ALA 141 143 143 ALA ALA I . n 
B 1 142 ARG 142 144 144 ARG ARG I . n 
B 1 143 ARG 143 145 145 ARG ARG I . n 
B 1 144 HIS 144 146 146 HIS HIS I . n 
B 1 145 PRO 145 147 147 PRO PRO I . n 
B 1 146 TYR 146 148 148 TYR TYR I . n 
B 1 147 PHE 147 149 149 PHE PHE I . n 
B 1 148 TYR 148 150 150 TYR TYR I . n 
B 1 149 ALA 149 151 151 ALA ALA I . n 
B 1 150 PRO 150 152 152 PRO PRO I . n 
B 1 151 GLU 151 153 153 GLU GLU I . n 
B 1 152 LEU 152 154 154 LEU LEU I . n 
B 1 153 LEU 153 155 155 LEU LEU I . n 
B 1 154 PHE 154 156 156 PHE PHE I . n 
B 1 155 PHE 155 157 157 PHE PHE I . n 
B 1 156 ALA 156 158 158 ALA ALA I . n 
B 1 157 LYS 157 159 159 LYS LYS I . n 
B 1 158 ARG 158 160 160 ARG ARG I . n 
B 1 159 TYR 159 161 161 TYR TYR I . n 
B 1 160 LYS 160 162 162 LYS LYS I . n 
B 1 161 ALA 161 163 163 ALA ALA I . n 
B 1 162 ALA 162 164 164 ALA ALA I . n 
B 1 163 PHE 163 165 165 PHE PHE I . n 
B 1 164 THR 164 166 166 THR THR I . n 
B 1 165 GLU 165 167 167 GLU GLU I . n 
B 1 166 CYS 166 168 168 CYS CYS I . n 
B 1 167 CYS 167 169 169 CYS CYS I . n 
B 1 168 GLN 168 170 170 GLN GLN I . n 
B 1 169 ALA 169 171 171 ALA ALA I . n 
B 1 170 ALA 170 172 172 ALA ALA I . n 
B 1 171 ASP 171 173 173 ASP ASP I . n 
B 1 172 LYS 172 174 174 LYS LYS I . n 
B 1 173 ALA 173 175 175 ALA ALA I . n 
B 1 174 ALA 174 176 176 ALA ALA I . n 
B 1 175 CYS 175 177 177 CYS CYS I . n 
B 1 176 LEU 176 178 178 LEU LEU I . n 
B 1 177 LEU 177 179 179 LEU LEU I . n 
B 1 178 PRO 178 180 180 PRO PRO I . n 
B 1 179 LYS 179 181 181 LYS LYS I . n 
B 1 180 LEU 180 182 182 LEU LEU I . n 
B 1 181 ASP 181 183 183 ASP ASP I . n 
B 1 182 GLU 182 184 184 GLU GLU I . n 
B 1 183 LEU 183 185 185 LEU LEU I . n 
B 1 184 ARG 184 186 186 ARG ARG I . n 
B 1 185 ASP 185 187 187 ASP ASP I . n 
B 1 186 GLU 186 188 188 GLU GLU I . n 
B 1 187 GLY 187 189 189 GLY GLY I . n 
B 1 188 LYS 188 190 190 LYS LYS I . n 
B 1 189 ALA 189 191 191 ALA ALA I . n 
B 1 190 SER 190 192 192 SER SER I . n 
B 1 191 SER 191 193 193 SER SER I . n 
B 1 192 ALA 192 194 194 ALA ALA I . n 
B 1 193 LYS 193 195 195 LYS LYS I . n 
B 1 194 GLN 194 196 196 GLN GLN I . n 
B 1 195 ARG 195 197 197 ARG ARG I . n 
B 1 196 LEU 196 198 198 LEU LEU I . n 
B 1 197 LYS 197 199 199 LYS LYS I . n 
B 1 198 CYS 198 200 200 CYS CYS I . n 
B 1 199 ALA 199 201 201 ALA ALA I . n 
B 1 200 SER 200 202 202 SER SER I . n 
B 1 201 LEU 201 203 203 LEU LEU I . n 
B 1 202 GLN 202 204 204 GLN GLN I . n 
B 1 203 LYS 203 205 205 LYS LYS I . n 
B 1 204 PHE 204 206 206 PHE PHE I . n 
B 1 205 GLY 205 207 207 GLY GLY I . n 
B 1 206 GLU 206 208 208 GLU GLU I . n 
B 1 207 ARG 207 209 209 ARG ARG I . n 
B 1 208 ALA 208 210 210 ALA ALA I . n 
B 1 209 PHE 209 211 211 PHE PHE I . n 
B 1 210 LYS 210 212 212 LYS LYS I . n 
B 1 211 ALA 211 213 213 ALA ALA I . n 
B 1 212 TRP 212 214 214 TRP TRP I . n 
B 1 213 ALA 213 215 215 ALA ALA I . n 
B 1 214 VAL 214 216 216 VAL VAL I . n 
B 1 215 ALA 215 217 217 ALA ALA I . n 
B 1 216 ARG 216 218 218 ARG ARG I . n 
B 1 217 LEU 217 219 219 LEU LEU I . n 
B 1 218 SER 218 220 220 SER SER I . n 
B 1 219 GLN 219 221 221 GLN GLN I . n 
B 1 220 ARG 220 222 222 ARG ARG I . n 
B 1 221 PHE 221 223 223 PHE PHE I . n 
B 1 222 PRO 222 224 224 PRO PRO I . n 
B 1 223 LYS 223 225 225 LYS LYS I . n 
B 1 224 ALA 224 226 226 ALA ALA I . n 
B 1 225 GLU 225 227 227 GLU GLU I . n 
B 1 226 PHE 226 228 228 PHE PHE I . n 
B 1 227 ALA 227 229 229 ALA ALA I . n 
B 1 228 GLU 228 230 230 GLU GLU I . n 
B 1 229 VAL 229 231 231 VAL VAL I . n 
B 1 230 SER 230 232 232 SER SER I . n 
B 1 231 LYS 231 233 233 LYS LYS I . n 
B 1 232 LEU 232 234 234 LEU LEU I . n 
B 1 233 VAL 233 235 235 VAL VAL I . n 
B 1 234 THR 234 236 236 THR THR I . n 
B 1 235 ASP 235 237 237 ASP ASP I . n 
B 1 236 LEU 236 238 238 LEU LEU I . n 
B 1 237 THR 237 239 239 THR THR I . n 
B 1 238 LYS 238 240 240 LYS LYS I . n 
B 1 239 VAL 239 241 241 VAL VAL I . n 
B 1 240 HIS 240 242 242 HIS HIS I . n 
B 1 241 THR 241 243 243 THR THR I . n 
B 1 242 GLU 242 244 244 GLU GLU I . n 
B 1 243 CYS 243 245 245 CYS CYS I . n 
B 1 244 CYS 244 246 246 CYS CYS I . n 
B 1 245 HIS 245 247 247 HIS HIS I . n 
B 1 246 GLY 246 248 248 GLY GLY I . n 
B 1 247 ASP 247 249 249 ASP ASP I . n 
B 1 248 LEU 248 250 250 LEU LEU I . n 
B 1 249 LEU 249 251 251 LEU LEU I . n 
B 1 250 GLU 250 252 252 GLU GLU I . n 
B 1 251 CYS 251 253 253 CYS CYS I . n 
B 1 252 ALA 252 254 254 ALA ALA I . n 
B 1 253 ASP 253 255 255 ASP ASP I . n 
B 1 254 ASP 254 256 256 ASP ASP I . n 
B 1 255 ARG 255 257 257 ARG ARG I . n 
B 1 256 ALA 256 258 258 ALA ALA I . n 
B 1 257 ASP 257 259 259 ASP ASP I . n 
B 1 258 LEU 258 260 260 LEU LEU I . n 
B 1 259 ALA 259 261 261 ALA ALA I . n 
B 1 260 LYS 260 262 262 LYS LYS I . n 
B 1 261 TYR 261 263 263 TYR TYR I . n 
B 1 262 ILE 262 264 264 ILE ILE I . n 
B 1 263 CYS 263 265 265 CYS CYS I . n 
B 1 264 GLU 264 266 266 GLU GLU I . n 
B 1 265 ASN 265 267 267 ASN ASN I . n 
B 1 266 GLN 266 268 268 GLN GLN I . n 
B 1 267 ASP 267 269 269 ASP ASP I . n 
B 1 268 SER 268 270 270 SER SER I . n 
B 1 269 ILE 269 271 271 ILE ILE I . n 
B 1 270 SER 270 272 272 SER SER I . n 
B 1 271 SER 271 273 273 SER SER I . n 
B 1 272 LYS 272 274 274 LYS LYS I . n 
B 1 273 LEU 273 275 275 LEU LEU I . n 
B 1 274 LYS 274 276 276 LYS LYS I . n 
B 1 275 GLU 275 277 277 GLU GLU I . n 
B 1 276 CYS 276 278 278 CYS CYS I . n 
B 1 277 CYS 277 279 279 CYS CYS I . n 
B 1 278 GLU 278 280 280 GLU GLU I . n 
B 1 279 LYS 279 281 281 LYS LYS I . n 
B 1 280 PRO 280 282 282 PRO PRO I . n 
B 1 281 LEU 281 283 283 LEU LEU I . n 
B 1 282 LEU 282 284 284 LEU LEU I . n 
B 1 283 GLU 283 285 285 GLU GLU I . n 
B 1 284 LYS 284 286 286 LYS LYS I . n 
B 1 285 SER 285 287 287 SER SER I . n 
B 1 286 HIS 286 288 288 HIS HIS I . n 
B 1 287 CYS 287 289 289 CYS CYS I . n 
B 1 288 ILE 288 290 290 ILE ILE I . n 
B 1 289 ALA 289 291 291 ALA ALA I . n 
B 1 290 GLU 290 292 292 GLU GLU I . n 
B 1 291 VAL 291 293 293 VAL VAL I . n 
B 1 292 GLU 292 294 294 GLU GLU I . n 
B 1 293 ASN 293 295 295 ASN ASN I . n 
B 1 294 ASP 294 296 296 ASP ASP I . n 
B 1 295 GLU 295 297 297 GLU GLU I . n 
B 1 296 MET 296 298 298 MET MET I . n 
B 1 297 PRO 297 299 299 PRO PRO I . n 
B 1 298 ALA 298 300 300 ALA ALA I . n 
B 1 299 ASP 299 301 301 ASP ASP I . n 
B 1 300 LEU 300 302 302 LEU LEU I . n 
B 1 301 PRO 301 303 303 PRO PRO I . n 
B 1 302 SER 302 304 304 SER SER I . n 
B 1 303 LEU 303 305 305 LEU LEU I . n 
B 1 304 ALA 304 306 306 ALA ALA I . n 
B 1 305 ALA 305 307 307 ALA ALA I . n 
B 1 306 ASP 306 308 308 ASP ASP I . n 
B 1 307 PHE 307 309 309 PHE PHE I . n 
B 1 308 VAL 308 310 310 VAL VAL I . n 
B 1 309 GLU 309 311 311 GLU GLU I . n 
B 1 310 SER 310 312 312 SER SER I . n 
B 1 311 LYS 311 313 313 LYS LYS I . n 
B 1 312 ASP 312 314 314 ASP ASP I . n 
B 1 313 VAL 313 315 315 VAL VAL I . n 
B 1 314 CYS 314 316 316 CYS CYS I . n 
B 1 315 LYS 315 317 317 LYS LYS I . n 
B 1 316 ASN 316 318 318 ASN ASN I . n 
B 1 317 TYR 317 319 319 TYR TYR I . n 
B 1 318 ALA 318 320 320 ALA ALA I . n 
B 1 319 GLU 319 321 321 GLU GLU I . n 
B 1 320 ALA 320 322 322 ALA ALA I . n 
B 1 321 LYS 321 323 323 LYS LYS I . n 
B 1 322 ASP 322 324 324 ASP ASP I . n 
B 1 323 VAL 323 325 325 VAL VAL I . n 
B 1 324 PHE 324 326 326 PHE PHE I . n 
B 1 325 LEU 325 327 327 LEU LEU I . n 
B 1 326 GLY 326 328 328 GLY GLY I . n 
B 1 327 MET 327 329 329 MET MET I . n 
B 1 328 PHE 328 330 330 PHE PHE I . n 
B 1 329 LEU 329 331 331 LEU LEU I . n 
B 1 330 TYR 330 332 332 TYR TYR I . n 
B 1 331 GLU 331 333 333 GLU GLU I . n 
B 1 332 TYR 332 334 334 TYR TYR I . n 
B 1 333 ALA 333 335 335 ALA ALA I . n 
B 1 334 ARG 334 336 336 ARG ARG I . n 
B 1 335 ARG 335 337 337 ARG ARG I . n 
B 1 336 HIS 336 338 338 HIS HIS I . n 
B 1 337 PRO 337 339 339 PRO PRO I . n 
B 1 338 ASP 338 340 340 ASP ASP I . n 
B 1 339 TYR 339 341 341 TYR TYR I . n 
B 1 340 SER 340 342 342 SER SER I . n 
B 1 341 VAL 341 343 343 VAL VAL I . n 
B 1 342 VAL 342 344 344 VAL VAL I . n 
B 1 343 LEU 343 345 345 LEU LEU I . n 
B 1 344 LEU 344 346 346 LEU LEU I . n 
B 1 345 LEU 345 347 347 LEU LEU I . n 
B 1 346 ARG 346 348 348 ARG ARG I . n 
B 1 347 LEU 347 349 349 LEU LEU I . n 
B 1 348 ALA 348 350 350 ALA ALA I . n 
B 1 349 LYS 349 351 351 LYS LYS I . n 
B 1 350 THR 350 352 352 THR THR I . n 
B 1 351 TYR 351 353 353 TYR TYR I . n 
B 1 352 GLU 352 354 354 GLU GLU I . n 
B 1 353 THR 353 355 355 THR THR I . n 
B 1 354 THR 354 356 356 THR THR I . n 
B 1 355 LEU 355 357 357 LEU LEU I . n 
B 1 356 GLU 356 358 358 GLU GLU I . n 
B 1 357 LYS 357 359 359 LYS LYS I . n 
B 1 358 CYS 358 360 360 CYS CYS I . n 
B 1 359 CYS 359 361 361 CYS CYS I . n 
B 1 360 ALA 360 362 362 ALA ALA I . n 
B 1 361 ALA 361 363 363 ALA ALA I . n 
B 1 362 ALA 362 364 364 ALA ALA I . n 
B 1 363 ASP 363 365 365 ASP ASP I . n 
B 1 364 PRO 364 366 366 PRO PRO I . n 
B 1 365 HIS 365 367 367 HIS HIS I . n 
B 1 366 GLU 366 368 368 GLU GLU I . n 
B 1 367 CYS 367 369 369 CYS CYS I . n 
B 1 368 TYR 368 370 370 TYR TYR I . n 
B 1 369 ALA 369 371 371 ALA ALA I . n 
B 1 370 LYS 370 372 372 LYS LYS I . n 
B 1 371 VAL 371 373 373 VAL VAL I . n 
B 1 372 PHE 372 374 374 PHE PHE I . n 
B 1 373 ASP 373 375 375 ASP ASP I . n 
B 1 374 GLU 374 376 376 GLU GLU I . n 
B 1 375 PHE 375 377 377 PHE PHE I . n 
B 1 376 LYS 376 378 378 LYS LYS I . n 
B 1 377 PRO 377 379 379 PRO PRO I . n 
B 1 378 LEU 378 380 380 LEU LEU I . n 
B 1 379 VAL 379 381 381 VAL VAL I . n 
B 1 380 GLU 380 382 382 GLU GLU I . n 
B 1 381 GLU 381 383 383 GLU GLU I . n 
B 1 382 PRO 382 384 384 PRO PRO I . n 
B 1 383 GLN 383 385 385 GLN GLN I . n 
B 1 384 ASN 384 386 386 ASN ASN I . n 
B 1 385 LEU 385 387 387 LEU LEU I . n 
B 1 386 ILE 386 388 388 ILE ILE I . n 
B 1 387 LYS 387 389 389 LYS LYS I . n 
B 1 388 GLN 388 390 390 GLN GLN I . n 
B 1 389 ASN 389 391 391 ASN ASN I . n 
B 1 390 CYS 390 392 392 CYS CYS I . n 
B 1 391 GLU 391 393 393 GLU GLU I . n 
B 1 392 LEU 392 394 394 LEU LEU I . n 
B 1 393 PHE 393 395 395 PHE PHE I . n 
B 1 394 GLU 394 396 396 GLU GLU I . n 
B 1 395 GLN 395 397 397 GLN GLN I . n 
B 1 396 LEU 396 398 398 LEU LEU I . n 
B 1 397 GLY 397 399 399 GLY GLY I . n 
B 1 398 GLU 398 400 400 GLU GLU I . n 
B 1 399 TYR 399 401 401 TYR TYR I . n 
B 1 400 LYS 400 402 402 LYS LYS I . n 
B 1 401 PHE 401 403 403 PHE PHE I . n 
B 1 402 GLN 402 404 404 GLN GLN I . n 
B 1 403 ASN 403 405 405 ASN ASN I . n 
B 1 404 ALA 404 406 406 ALA ALA I . n 
B 1 405 LEU 405 407 407 LEU LEU I . n 
B 1 406 LEU 406 408 408 LEU LEU I . n 
B 1 407 VAL 407 409 409 VAL VAL I . n 
B 1 408 ARG 408 410 410 ARG ARG I . n 
B 1 409 TYR 409 411 411 TYR TYR I . n 
B 1 410 THR 410 412 412 THR THR I . n 
B 1 411 LYS 411 413 413 LYS LYS I . n 
B 1 412 LYS 412 414 414 LYS LYS I . n 
B 1 413 VAL 413 415 415 VAL VAL I . n 
B 1 414 PRO 414 416 416 PRO PRO I . n 
B 1 415 GLN 415 417 417 GLN GLN I . n 
B 1 416 VAL 416 418 418 VAL VAL I . n 
B 1 417 SER 417 419 419 SER SER I . n 
B 1 418 THR 418 420 420 THR THR I . n 
B 1 419 PRO 419 421 421 PRO PRO I . n 
B 1 420 THR 420 422 422 THR THR I . n 
B 1 421 LEU 421 423 423 LEU LEU I . n 
B 1 422 VAL 422 424 424 VAL VAL I . n 
B 1 423 GLU 423 425 425 GLU GLU I . n 
B 1 424 VAL 424 426 426 VAL VAL I . n 
B 1 425 SER 425 427 427 SER SER I . n 
B 1 426 ARG 426 428 428 ARG ARG I . n 
B 1 427 ASN 427 429 429 ASN ASN I . n 
B 1 428 LEU 428 430 430 LEU LEU I . n 
B 1 429 GLY 429 431 431 GLY GLY I . n 
B 1 430 LYS 430 432 432 LYS LYS I . n 
B 1 431 VAL 431 433 433 VAL VAL I . n 
B 1 432 GLY 432 434 434 GLY GLY I . n 
B 1 433 SER 433 435 435 SER SER I . n 
B 1 434 LYS 434 436 436 LYS LYS I . n 
B 1 435 CYS 435 437 437 CYS CYS I . n 
B 1 436 CYS 436 438 438 CYS CYS I . n 
B 1 437 LYS 437 439 439 LYS LYS I . n 
B 1 438 HIS 438 440 440 HIS HIS I . n 
B 1 439 PRO 439 441 441 PRO PRO I . n 
B 1 440 GLU 440 442 442 GLU GLU I . n 
B 1 441 ALA 441 443 443 ALA ALA I . n 
B 1 442 LYS 442 444 444 LYS LYS I . n 
B 1 443 ARG 443 445 445 ARG ARG I . n 
B 1 444 MET 444 446 446 MET MET I . n 
B 1 445 PRO 445 447 447 PRO PRO I . n 
B 1 446 CYS 446 448 448 CYS CYS I . n 
B 1 447 ALA 447 449 449 ALA ALA I . n 
B 1 448 GLU 448 450 450 GLU GLU I . n 
B 1 449 ASP 449 451 451 ASP ASP I . n 
B 1 450 TYR 450 452 452 TYR TYR I . n 
B 1 451 LEU 451 453 453 LEU LEU I . n 
B 1 452 SER 452 454 454 SER SER I . n 
B 1 453 VAL 453 455 455 VAL VAL I . n 
B 1 454 VAL 454 456 456 VAL VAL I . n 
B 1 455 LEU 455 457 457 LEU LEU I . n 
B 1 456 ASN 456 458 458 ASN ASN I . n 
B 1 457 GLN 457 459 459 GLN GLN I . n 
B 1 458 LEU 458 460 460 LEU LEU I . n 
B 1 459 CYS 459 461 461 CYS CYS I . n 
B 1 460 VAL 460 462 462 VAL VAL I . n 
B 1 461 LEU 461 463 463 LEU LEU I . n 
B 1 462 HIS 462 464 464 HIS HIS I . n 
B 1 463 GLU 463 465 465 GLU GLU I . n 
B 1 464 LYS 464 466 466 LYS LYS I . n 
B 1 465 THR 465 467 467 THR THR I . n 
B 1 466 PRO 466 468 468 PRO PRO I . n 
B 1 467 VAL 467 469 469 VAL VAL I . n 
B 1 468 SER 468 470 470 SER SER I . n 
B 1 469 ASP 469 471 471 ASP ASP I . n 
B 1 470 ARG 470 472 472 ARG ARG I . n 
B 1 471 VAL 471 473 473 VAL VAL I . n 
B 1 472 THR 472 474 474 THR THR I . n 
B 1 473 LYS 473 475 475 LYS LYS I . n 
B 1 474 CYS 474 476 476 CYS CYS I . n 
B 1 475 CYS 475 477 477 CYS CYS I . n 
B 1 476 THR 476 478 478 THR THR I . n 
B 1 477 GLU 477 479 479 GLU GLU I . n 
B 1 478 SER 478 480 480 SER SER I . n 
B 1 479 LEU 479 481 481 LEU LEU I . n 
B 1 480 VAL 480 482 482 VAL VAL I . n 
B 1 481 ASN 481 483 483 ASN ASN I . n 
B 1 482 ARG 482 484 484 ARG ARG I . n 
B 1 483 ARG 483 485 485 ARG ARG I . n 
B 1 484 PRO 484 486 486 PRO PRO I . n 
B 1 485 CYS 485 487 487 CYS CYS I . n 
B 1 486 PHE 486 488 488 PHE PHE I . n 
B 1 487 SER 487 489 489 SER SER I . n 
B 1 488 ALA 488 490 490 ALA ALA I . n 
B 1 489 LEU 489 491 491 LEU LEU I . n 
B 1 490 GLU 490 492 492 GLU GLU I . n 
B 1 491 VAL 491 493 493 VAL VAL I . n 
B 1 492 ASP 492 494 494 ASP ASP I . n 
B 1 493 GLU 493 495 495 GLU GLU I . n 
B 1 494 THR 494 496 496 THR THR I . n 
B 1 495 TYR 495 497 497 TYR TYR I . n 
B 1 496 VAL 496 498 498 VAL VAL I . n 
B 1 497 PRO 497 499 499 PRO PRO I . n 
B 1 498 LYS 498 500 500 LYS LYS I . n 
B 1 499 GLU 499 501 501 GLU GLU I . n 
B 1 500 PHE 500 502 502 PHE PHE I . n 
B 1 501 ASN 501 503 503 ASN ASN I . n 
B 1 502 ALA 502 504 504 ALA ALA I . n 
B 1 503 GLU 503 505 505 GLU GLU I . n 
B 1 504 THR 504 506 506 THR THR I . n 
B 1 505 PHE 505 507 507 PHE PHE I . n 
B 1 506 THR 506 508 508 THR THR I . n 
B 1 507 PHE 507 509 509 PHE PHE I . n 
B 1 508 HIS 508 510 510 HIS HIS I . n 
B 1 509 ALA 509 511 511 ALA ALA I . n 
B 1 510 ASP 510 512 512 ASP ASP I . n 
B 1 511 ILE 511 513 513 ILE ILE I . n 
B 1 512 CYS 512 514 514 CYS CYS I . n 
B 1 513 THR 513 515 515 THR THR I . n 
B 1 514 LEU 514 516 516 LEU LEU I . n 
B 1 515 SER 515 517 517 SER SER I . n 
B 1 516 GLU 516 518 518 GLU GLU I . n 
B 1 517 LYS 517 519 519 LYS LYS I . n 
B 1 518 GLU 518 520 520 GLU GLU I . n 
B 1 519 ARG 519 521 521 ARG ARG I . n 
B 1 520 GLN 520 522 522 GLN GLN I . n 
B 1 521 ILE 521 523 523 ILE ILE I . n 
B 1 522 LYS 522 524 524 LYS LYS I . n 
B 1 523 LYS 523 525 525 LYS LYS I . n 
B 1 524 GLN 524 526 526 GLN GLN I . n 
B 1 525 THR 525 527 527 THR THR I . n 
B 1 526 ALA 526 528 528 ALA ALA I . n 
B 1 527 LEU 527 529 529 LEU LEU I . n 
B 1 528 VAL 528 530 530 VAL VAL I . n 
B 1 529 GLU 529 531 531 GLU GLU I . n 
B 1 530 LEU 530 532 532 LEU LEU I . n 
B 1 531 VAL 531 533 533 VAL VAL I . n 
B 1 532 LYS 532 534 534 LYS LYS I . n 
B 1 533 HIS 533 535 535 HIS HIS I . n 
B 1 534 LYS 534 536 536 LYS LYS I . n 
B 1 535 PRO 535 537 537 PRO PRO I . n 
B 1 536 LYS 536 538 538 LYS LYS I . n 
B 1 537 ALA 537 539 539 ALA ALA I . n 
B 1 538 THR 538 540 540 THR THR I . n 
B 1 539 LYS 539 541 541 LYS LYS I . n 
B 1 540 GLU 540 542 542 GLU GLU I . n 
B 1 541 GLN 541 543 543 GLN GLN I . n 
B 1 542 LEU 542 544 544 LEU LEU I . n 
B 1 543 LYS 543 545 545 LYS LYS I . n 
B 1 544 ALA 544 546 546 ALA ALA I . n 
B 1 545 VAL 545 547 547 VAL VAL I . n 
B 1 546 MET 546 548 548 MET MET I . n 
B 1 547 ASP 547 549 549 ASP ASP I . n 
B 1 548 ASP 548 550 550 ASP ASP I . n 
B 1 549 PHE 549 551 551 PHE PHE I . n 
B 1 550 ALA 550 552 552 ALA ALA I . n 
B 1 551 ALA 551 553 553 ALA ALA I . n 
B 1 552 PHE 552 554 554 PHE PHE I . n 
B 1 553 VAL 553 555 555 VAL VAL I . n 
B 1 554 GLU 554 556 556 GLU GLU I . n 
B 1 555 LYS 555 557 557 LYS LYS I . n 
B 1 556 CYS 556 558 558 CYS CYS I . n 
B 1 557 CYS 557 559 559 CYS CYS I . n 
B 1 558 LYS 558 560 560 LYS LYS I . n 
B 1 559 ALA 559 561 561 ALA ALA I . n 
B 1 560 ASP 560 562 562 ASP ASP I . n 
B 1 561 ASP 561 563 563 ASP ASP I . n 
B 1 562 LYS 562 564 564 LYS LYS I . n 
B 1 563 GLU 563 565 565 GLU GLU I . n 
B 1 564 THR 564 566 566 THR THR I . n 
B 1 565 CYS 565 567 567 CYS CYS I . n 
B 1 566 PHE 566 568 568 PHE PHE I . n 
B 1 567 ALA 567 569 569 ALA ALA I . n 
B 1 568 GLU 568 570 570 GLU GLU I . n 
B 1 569 GLU 569 571 571 GLU GLU I . n 
B 1 570 GLY 570 572 572 GLY GLY I . n 
B 1 571 LYS 571 573 573 LYS LYS I . n 
B 1 572 LYS 572 574 574 LYS LYS I . n 
B 1 573 LEU 573 575 575 LEU LEU I . n 
B 1 574 VAL 574 576 576 VAL VAL I . n 
B 1 575 ALA 575 577 577 ALA ALA I . n 
B 1 576 ALA 576 578 578 ALA ALA I . n 
B 1 577 SER 577 579 579 SER SER I . n 
B 1 578 GLN 578 580 580 GLN GLN I . n 
B 1 579 ALA 579 581 581 ALA ALA I . n 
B 1 580 ALA 580 582 582 ALA ALA I . n 
B 1 581 LEU 581 583 583 LEU LEU I . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 IMN   ? ? IMN   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1D6U ? ? A1D6U ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1D6U 1   601 601  A1D6U LIG A . 
D 3 IMN   1   602 602  IMN   IND A . 
E 4 PLM   1   603 1001 PLM   PLM A . 
F 4 PLM   1   604 1002 PLM   PLM A . 
G 4 PLM   1   605 1003 PLM   PLM A . 
H 4 PLM   1   606 1004 PLM   PLM A . 
I 4 PLM   1   607 1005 PLM   PLM A . 
J 4 PLM   1   608 1006 PLM   PLM A . 
K 2 A1D6U 1   601 601  A1D6U LIG I . 
L 3 IMN   1   602 602  IMN   IND I . 
M 4 PLM   1   603 1001 PLM   PLM I . 
N 4 PLM   1   604 1002 PLM   PLM I . 
O 4 PLM   1   605 1003 PLM   PLM I . 
P 4 PLM   1   606 1004 PLM   PLM I . 
Q 4 PLM   1   607 1005 PLM   PLM I . 
R 4 PLM   1   608 1006 PLM   PLM I . 
S 5 HOH   1   701 201  HOH   HOH A . 
S 5 HOH   2   702 47   HOH   HOH A . 
S 5 HOH   3   703 118  HOH   HOH A . 
S 5 HOH   4   704 188  HOH   HOH A . 
S 5 HOH   5   705 17   HOH   HOH A . 
S 5 HOH   6   706 14   HOH   HOH A . 
S 5 HOH   7   707 10   HOH   HOH A . 
S 5 HOH   8   708 75   HOH   HOH A . 
S 5 HOH   9   709 99   HOH   HOH A . 
S 5 HOH   10  710 107  HOH   HOH A . 
S 5 HOH   11  711 123  HOH   HOH A . 
S 5 HOH   12  712 151  HOH   HOH A . 
S 5 HOH   13  713 162  HOH   HOH A . 
S 5 HOH   14  714 23   HOH   HOH A . 
S 5 HOH   15  715 69   HOH   HOH A . 
S 5 HOH   16  716 37   HOH   HOH A . 
S 5 HOH   17  717 157  HOH   HOH A . 
S 5 HOH   18  718 236  HOH   HOH A . 
S 5 HOH   19  719 217  HOH   HOH A . 
S 5 HOH   20  720 54   HOH   HOH A . 
S 5 HOH   21  721 228  HOH   HOH A . 
S 5 HOH   22  722 96   HOH   HOH A . 
S 5 HOH   23  723 156  HOH   HOH A . 
S 5 HOH   24  724 116  HOH   HOH A . 
S 5 HOH   25  725 190  HOH   HOH A . 
S 5 HOH   26  726 80   HOH   HOH A . 
S 5 HOH   27  727 127  HOH   HOH A . 
S 5 HOH   28  728 166  HOH   HOH A . 
S 5 HOH   29  729 205  HOH   HOH A . 
S 5 HOH   30  730 90   HOH   HOH A . 
S 5 HOH   31  731 112  HOH   HOH A . 
S 5 HOH   32  732 5    HOH   HOH A . 
S 5 HOH   33  733 141  HOH   HOH A . 
S 5 HOH   34  734 142  HOH   HOH A . 
S 5 HOH   35  735 241  HOH   HOH A . 
S 5 HOH   36  736 222  HOH   HOH A . 
S 5 HOH   37  737 161  HOH   HOH A . 
S 5 HOH   38  738 97   HOH   HOH A . 
S 5 HOH   39  739 8    HOH   HOH A . 
S 5 HOH   40  740 171  HOH   HOH A . 
S 5 HOH   41  741 221  HOH   HOH A . 
S 5 HOH   42  742 13   HOH   HOH A . 
S 5 HOH   43  743 27   HOH   HOH A . 
S 5 HOH   44  744 50   HOH   HOH A . 
S 5 HOH   45  745 139  HOH   HOH A . 
S 5 HOH   46  746 40   HOH   HOH A . 
S 5 HOH   47  747 4    HOH   HOH A . 
S 5 HOH   48  748 213  HOH   HOH A . 
S 5 HOH   49  749 74   HOH   HOH A . 
S 5 HOH   50  750 146  HOH   HOH A . 
S 5 HOH   51  751 33   HOH   HOH A . 
S 5 HOH   52  752 115  HOH   HOH A . 
S 5 HOH   53  753 169  HOH   HOH A . 
S 5 HOH   54  754 137  HOH   HOH A . 
S 5 HOH   55  755 25   HOH   HOH A . 
S 5 HOH   56  756 170  HOH   HOH A . 
S 5 HOH   57  757 9    HOH   HOH A . 
S 5 HOH   58  758 85   HOH   HOH A . 
S 5 HOH   59  759 93   HOH   HOH A . 
S 5 HOH   60  760 197  HOH   HOH A . 
S 5 HOH   61  761 65   HOH   HOH A . 
S 5 HOH   62  762 7    HOH   HOH A . 
S 5 HOH   63  763 148  HOH   HOH A . 
S 5 HOH   64  764 73   HOH   HOH A . 
S 5 HOH   65  765 219  HOH   HOH A . 
S 5 HOH   66  766 94   HOH   HOH A . 
S 5 HOH   67  767 1    HOH   HOH A . 
S 5 HOH   68  768 52   HOH   HOH A . 
S 5 HOH   69  769 114  HOH   HOH A . 
S 5 HOH   70  770 63   HOH   HOH A . 
S 5 HOH   71  771 18   HOH   HOH A . 
S 5 HOH   72  772 68   HOH   HOH A . 
S 5 HOH   73  773 174  HOH   HOH A . 
S 5 HOH   74  774 59   HOH   HOH A . 
S 5 HOH   75  775 60   HOH   HOH A . 
S 5 HOH   76  776 56   HOH   HOH A . 
S 5 HOH   77  777 83   HOH   HOH A . 
S 5 HOH   78  778 35   HOH   HOH A . 
S 5 HOH   79  779 31   HOH   HOH A . 
S 5 HOH   80  780 150  HOH   HOH A . 
S 5 HOH   81  781 159  HOH   HOH A . 
S 5 HOH   82  782 152  HOH   HOH A . 
S 5 HOH   83  783 30   HOH   HOH A . 
S 5 HOH   84  784 184  HOH   HOH A . 
S 5 HOH   85  785 53   HOH   HOH A . 
S 5 HOH   86  786 235  HOH   HOH A . 
S 5 HOH   87  787 132  HOH   HOH A . 
S 5 HOH   88  788 155  HOH   HOH A . 
S 5 HOH   89  789 154  HOH   HOH A . 
S 5 HOH   90  790 186  HOH   HOH A . 
S 5 HOH   91  791 238  HOH   HOH A . 
S 5 HOH   92  792 95   HOH   HOH A . 
S 5 HOH   93  793 43   HOH   HOH A . 
S 5 HOH   94  794 101  HOH   HOH A . 
S 5 HOH   95  795 193  HOH   HOH A . 
S 5 HOH   96  796 183  HOH   HOH A . 
S 5 HOH   97  797 26   HOH   HOH A . 
S 5 HOH   98  798 58   HOH   HOH A . 
S 5 HOH   99  799 111  HOH   HOH A . 
S 5 HOH   100 800 245  HOH   HOH A . 
S 5 HOH   101 801 220  HOH   HOH A . 
S 5 HOH   102 802 153  HOH   HOH A . 
S 5 HOH   103 803 120  HOH   HOH A . 
S 5 HOH   104 804 165  HOH   HOH A . 
S 5 HOH   105 805 79   HOH   HOH A . 
S 5 HOH   106 806 78   HOH   HOH A . 
S 5 HOH   107 807 211  HOH   HOH A . 
S 5 HOH   108 808 103  HOH   HOH A . 
S 5 HOH   109 809 200  HOH   HOH A . 
S 5 HOH   110 810 232  HOH   HOH A . 
S 5 HOH   111 811 106  HOH   HOH A . 
S 5 HOH   112 812 55   HOH   HOH A . 
S 5 HOH   113 813 131  HOH   HOH A . 
S 5 HOH   114 814 202  HOH   HOH A . 
S 5 HOH   115 815 117  HOH   HOH A . 
S 5 HOH   116 816 227  HOH   HOH A . 
S 5 HOH   117 817 104  HOH   HOH A . 
S 5 HOH   118 818 234  HOH   HOH A . 
S 5 HOH   119 819 119  HOH   HOH A . 
S 5 HOH   120 820 204  HOH   HOH A . 
S 5 HOH   121 821 206  HOH   HOH A . 
S 5 HOH   122 822 181  HOH   HOH A . 
S 5 HOH   123 823 71   HOH   HOH A . 
S 5 HOH   124 824 230  HOH   HOH A . 
S 5 HOH   125 825 189  HOH   HOH A . 
S 5 HOH   126 826 67   HOH   HOH A . 
S 5 HOH   127 827 212  HOH   HOH A . 
S 5 HOH   128 828 242  HOH   HOH A . 
S 5 HOH   129 829 225  HOH   HOH A . 
T 5 HOH   1   701 160  HOH   HOH I . 
T 5 HOH   2   702 198  HOH   HOH I . 
T 5 HOH   3   703 167  HOH   HOH I . 
T 5 HOH   4   704 108  HOH   HOH I . 
T 5 HOH   5   705 231  HOH   HOH I . 
T 5 HOH   6   706 86   HOH   HOH I . 
T 5 HOH   7   707 239  HOH   HOH I . 
T 5 HOH   8   708 41   HOH   HOH I . 
T 5 HOH   9   709 129  HOH   HOH I . 
T 5 HOH   10  710 51   HOH   HOH I . 
T 5 HOH   11  711 210  HOH   HOH I . 
T 5 HOH   12  712 66   HOH   HOH I . 
T 5 HOH   13  713 207  HOH   HOH I . 
T 5 HOH   14  714 180  HOH   HOH I . 
T 5 HOH   15  715 147  HOH   HOH I . 
T 5 HOH   16  716 76   HOH   HOH I . 
T 5 HOH   17  717 175  HOH   HOH I . 
T 5 HOH   18  718 32   HOH   HOH I . 
T 5 HOH   19  719 62   HOH   HOH I . 
T 5 HOH   20  720 145  HOH   HOH I . 
T 5 HOH   21  721 130  HOH   HOH I . 
T 5 HOH   22  722 22   HOH   HOH I . 
T 5 HOH   23  723 16   HOH   HOH I . 
T 5 HOH   24  724 89   HOH   HOH I . 
T 5 HOH   25  725 109  HOH   HOH I . 
T 5 HOH   26  726 36   HOH   HOH I . 
T 5 HOH   27  727 233  HOH   HOH I . 
T 5 HOH   28  728 3    HOH   HOH I . 
T 5 HOH   29  729 125  HOH   HOH I . 
T 5 HOH   30  730 46   HOH   HOH I . 
T 5 HOH   31  731 2    HOH   HOH I . 
T 5 HOH   32  732 92   HOH   HOH I . 
T 5 HOH   33  733 28   HOH   HOH I . 
T 5 HOH   34  734 133  HOH   HOH I . 
T 5 HOH   35  735 20   HOH   HOH I . 
T 5 HOH   36  736 11   HOH   HOH I . 
T 5 HOH   37  737 12   HOH   HOH I . 
T 5 HOH   38  738 15   HOH   HOH I . 
T 5 HOH   39  739 138  HOH   HOH I . 
T 5 HOH   40  740 64   HOH   HOH I . 
T 5 HOH   41  741 102  HOH   HOH I . 
T 5 HOH   42  742 176  HOH   HOH I . 
T 5 HOH   43  743 194  HOH   HOH I . 
T 5 HOH   44  744 168  HOH   HOH I . 
T 5 HOH   45  745 81   HOH   HOH I . 
T 5 HOH   46  746 178  HOH   HOH I . 
T 5 HOH   47  747 240  HOH   HOH I . 
T 5 HOH   48  748 226  HOH   HOH I . 
T 5 HOH   49  749 38   HOH   HOH I . 
T 5 HOH   50  750 44   HOH   HOH I . 
T 5 HOH   51  751 216  HOH   HOH I . 
T 5 HOH   52  752 246  HOH   HOH I . 
T 5 HOH   53  753 122  HOH   HOH I . 
T 5 HOH   54  754 77   HOH   HOH I . 
T 5 HOH   55  755 87   HOH   HOH I . 
T 5 HOH   56  756 187  HOH   HOH I . 
T 5 HOH   57  757 110  HOH   HOH I . 
T 5 HOH   58  758 121  HOH   HOH I . 
T 5 HOH   59  759 39   HOH   HOH I . 
T 5 HOH   60  760 24   HOH   HOH I . 
T 5 HOH   61  761 126  HOH   HOH I . 
T 5 HOH   62  762 243  HOH   HOH I . 
T 5 HOH   63  763 179  HOH   HOH I . 
T 5 HOH   64  764 208  HOH   HOH I . 
T 5 HOH   65  765 218  HOH   HOH I . 
T 5 HOH   66  766 135  HOH   HOH I . 
T 5 HOH   67  767 158  HOH   HOH I . 
T 5 HOH   68  768 128  HOH   HOH I . 
T 5 HOH   69  769 105  HOH   HOH I . 
T 5 HOH   70  770 244  HOH   HOH I . 
T 5 HOH   71  771 88   HOH   HOH I . 
T 5 HOH   72  772 72   HOH   HOH I . 
T 5 HOH   73  773 172  HOH   HOH I . 
T 5 HOH   74  774 134  HOH   HOH I . 
T 5 HOH   75  775 143  HOH   HOH I . 
T 5 HOH   76  776 45   HOH   HOH I . 
T 5 HOH   77  777 42   HOH   HOH I . 
T 5 HOH   78  778 82   HOH   HOH I . 
T 5 HOH   79  779 29   HOH   HOH I . 
T 5 HOH   80  780 214  HOH   HOH I . 
T 5 HOH   81  781 199  HOH   HOH I . 
T 5 HOH   82  782 113  HOH   HOH I . 
T 5 HOH   83  783 98   HOH   HOH I . 
T 5 HOH   84  784 100  HOH   HOH I . 
T 5 HOH   85  785 164  HOH   HOH I . 
T 5 HOH   86  786 61   HOH   HOH I . 
T 5 HOH   87  787 70   HOH   HOH I . 
T 5 HOH   88  788 223  HOH   HOH I . 
T 5 HOH   89  789 124  HOH   HOH I . 
T 5 HOH   90  790 91   HOH   HOH I . 
T 5 HOH   91  791 191  HOH   HOH I . 
T 5 HOH   92  792 6    HOH   HOH I . 
T 5 HOH   93  793 49   HOH   HOH I . 
T 5 HOH   94  794 84   HOH   HOH I . 
T 5 HOH   95  795 57   HOH   HOH I . 
T 5 HOH   96  796 19   HOH   HOH I . 
T 5 HOH   97  797 192  HOH   HOH I . 
T 5 HOH   98  798 195  HOH   HOH I . 
T 5 HOH   99  799 173  HOH   HOH I . 
T 5 HOH   100 800 149  HOH   HOH I . 
T 5 HOH   101 801 215  HOH   HOH I . 
T 5 HOH   102 802 144  HOH   HOH I . 
T 5 HOH   103 803 136  HOH   HOH I . 
T 5 HOH   104 804 48   HOH   HOH I . 
T 5 HOH   105 805 203  HOH   HOH I . 
T 5 HOH   106 806 196  HOH   HOH I . 
T 5 HOH   107 807 177  HOH   HOH I . 
T 5 HOH   108 808 237  HOH   HOH I . 
T 5 HOH   109 809 209  HOH   HOH I . 
T 5 HOH   110 810 185  HOH   HOH I . 
T 5 HOH   111 811 224  HOH   HOH I . 
T 5 HOH   112 812 140  HOH   HOH I . 
T 5 HOH   113 813 163  HOH   HOH I . 
T 5 HOH   114 814 34   HOH   HOH I . 
T 5 HOH   115 815 21   HOH   HOH I . 
T 5 HOH   116 816 182  HOH   HOH I . 
T 5 HOH   117 817 229  HOH   HOH I . 
# 
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 HIS 3   ? ND1 ? A HIS 1   ND1 
2   1 Y 1 A HIS 3   ? CD2 ? A HIS 1   CD2 
3   1 Y 1 A HIS 3   ? CE1 ? A HIS 1   CE1 
4   1 Y 1 A HIS 3   ? NE2 ? A HIS 1   NE2 
5   1 Y 1 A LYS 4   ? CG  ? A LYS 2   CG  
6   1 Y 1 A LYS 4   ? CD  ? A LYS 2   CD  
7   1 Y 1 A LYS 4   ? CE  ? A LYS 2   CE  
8   1 Y 1 A LYS 4   ? NZ  ? A LYS 2   NZ  
9   1 Y 1 A GLU 6   ? CG  ? A GLU 4   CG  
10  1 Y 1 A GLU 6   ? CD  ? A GLU 4   CD  
11  1 Y 1 A GLU 6   ? OE1 ? A GLU 4   OE1 
12  1 Y 1 A GLU 6   ? OE2 ? A GLU 4   OE2 
13  1 Y 1 A LYS 41  ? CG  ? A LYS 39  CG  
14  1 Y 1 A LYS 41  ? CD  ? A LYS 39  CD  
15  1 Y 1 A LYS 41  ? CE  ? A LYS 39  CE  
16  1 Y 1 A LYS 41  ? NZ  ? A LYS 39  NZ  
17  1 Y 1 A GLU 48  ? CG  ? A GLU 46  CG  
18  1 Y 1 A GLU 48  ? CD  ? A GLU 46  CD  
19  1 Y 1 A GLU 48  ? OE1 ? A GLU 46  OE1 
20  1 Y 1 A GLU 48  ? OE2 ? A GLU 46  OE2 
21  1 Y 1 A GLU 57  ? CG  ? A GLU 55  CG  
22  1 Y 1 A GLU 57  ? CD  ? A GLU 55  CD  
23  1 Y 1 A GLU 57  ? OE1 ? A GLU 55  OE1 
24  1 Y 1 A GLU 57  ? OE2 ? A GLU 55  OE2 
25  1 Y 1 A GLU 60  ? CG  ? A GLU 58  CG  
26  1 Y 1 A GLU 60  ? CD  ? A GLU 58  CD  
27  1 Y 1 A GLU 60  ? OE1 ? A GLU 58  OE1 
28  1 Y 1 A GLU 60  ? OE2 ? A GLU 58  OE2 
29  1 Y 1 A LYS 64  ? CE  ? A LYS 62  CE  
30  1 Y 1 A LYS 64  ? NZ  ? A LYS 62  NZ  
31  1 Y 1 A THR 79  ? OG1 ? A THR 77  OG1 
32  1 Y 1 A THR 79  ? CG2 ? A THR 77  CG2 
33  1 Y 1 A GLU 82  ? CG  ? A GLU 80  CG  
34  1 Y 1 A GLU 82  ? CD  ? A GLU 80  CD  
35  1 Y 1 A GLU 82  ? OE1 ? A GLU 80  OE1 
36  1 Y 1 A GLU 82  ? OE2 ? A GLU 80  OE2 
37  1 Y 1 A GLN 94  ? CG  ? A GLN 92  CG  
38  1 Y 1 A GLN 94  ? CD  ? A GLN 92  CD  
39  1 Y 1 A GLN 94  ? OE1 ? A GLN 92  OE1 
40  1 Y 1 A GLN 94  ? NE2 ? A GLN 92  NE2 
41  1 Y 1 A ASP 108 ? CG  ? A ASP 106 CG  
42  1 Y 1 A ASP 108 ? OD1 ? A ASP 106 OD1 
43  1 Y 1 A ASP 108 ? OD2 ? A ASP 106 OD2 
44  1 Y 1 A ASN 111 ? CG  ? A ASN 109 CG  
45  1 Y 1 A ASN 111 ? OD1 ? A ASN 109 OD1 
46  1 Y 1 A ASN 111 ? ND2 ? A ASN 109 ND2 
47  1 Y 1 A GLU 119 ? CG  ? A GLU 117 CG  
48  1 Y 1 A GLU 119 ? CD  ? A GLU 117 CD  
49  1 Y 1 A GLU 119 ? OE1 ? A GLU 117 OE1 
50  1 Y 1 A GLU 119 ? OE2 ? A GLU 117 OE2 
51  1 Y 1 A LYS 137 ? CG  ? A LYS 135 CG  
52  1 Y 1 A LYS 137 ? CD  ? A LYS 135 CD  
53  1 Y 1 A LYS 137 ? CE  ? A LYS 135 CE  
54  1 Y 1 A LYS 137 ? NZ  ? A LYS 135 NZ  
55  1 Y 1 A LYS 181 ? CE  ? A LYS 179 CE  
56  1 Y 1 A LYS 181 ? NZ  ? A LYS 179 NZ  
57  1 Y 1 A GLU 184 ? CG  ? A GLU 182 CG  
58  1 Y 1 A GLU 184 ? CD  ? A GLU 182 CD  
59  1 Y 1 A GLU 184 ? OE1 ? A GLU 182 OE1 
60  1 Y 1 A GLU 184 ? OE2 ? A GLU 182 OE2 
61  1 Y 1 A ARG 186 ? CZ  ? A ARG 184 CZ  
62  1 Y 1 A ARG 186 ? NH1 ? A ARG 184 NH1 
63  1 Y 1 A ARG 186 ? NH2 ? A ARG 184 NH2 
64  1 Y 1 A LYS 195 ? NZ  ? A LYS 193 NZ  
65  1 Y 1 A ARG 197 ? CG  ? A ARG 195 CG  
66  1 Y 1 A ARG 197 ? CD  ? A ARG 195 CD  
67  1 Y 1 A ARG 197 ? NE  ? A ARG 195 NE  
68  1 Y 1 A ARG 197 ? CZ  ? A ARG 195 CZ  
69  1 Y 1 A ARG 197 ? NH1 ? A ARG 195 NH1 
70  1 Y 1 A ARG 197 ? NH2 ? A ARG 195 NH2 
71  1 Y 1 A GLN 204 ? CG  ? A GLN 202 CG  
72  1 Y 1 A GLN 204 ? CD  ? A GLN 202 CD  
73  1 Y 1 A GLN 204 ? OE1 ? A GLN 202 OE1 
74  1 Y 1 A GLN 204 ? NE2 ? A GLN 202 NE2 
75  1 Y 1 A GLU 227 ? CG  ? A GLU 225 CG  
76  1 Y 1 A GLU 227 ? CD  ? A GLU 225 CD  
77  1 Y 1 A GLU 227 ? OE1 ? A GLU 225 OE1 
78  1 Y 1 A GLU 227 ? OE2 ? A GLU 225 OE2 
79  1 Y 1 A LYS 240 ? CD  ? A LYS 238 CD  
80  1 Y 1 A LYS 240 ? CE  ? A LYS 238 CE  
81  1 Y 1 A LYS 240 ? NZ  ? A LYS 238 NZ  
82  1 Y 1 A GLU 244 ? CD  ? A GLU 242 CD  
83  1 Y 1 A GLU 244 ? OE1 ? A GLU 242 OE1 
84  1 Y 1 A GLU 244 ? OE2 ? A GLU 242 OE2 
85  1 Y 1 A LYS 262 ? CG  ? A LYS 260 CG  
86  1 Y 1 A LYS 262 ? CD  ? A LYS 260 CD  
87  1 Y 1 A LYS 262 ? CE  ? A LYS 260 CE  
88  1 Y 1 A LYS 262 ? NZ  ? A LYS 260 NZ  
89  1 Y 1 A LYS 276 ? CG  ? A LYS 274 CG  
90  1 Y 1 A LYS 276 ? CD  ? A LYS 274 CD  
91  1 Y 1 A LYS 276 ? CE  ? A LYS 274 CE  
92  1 Y 1 A LYS 276 ? NZ  ? A LYS 274 NZ  
93  1 Y 1 A GLU 280 ? CG  ? A GLU 278 CG  
94  1 Y 1 A GLU 280 ? CD  ? A GLU 278 CD  
95  1 Y 1 A GLU 280 ? OE1 ? A GLU 278 OE1 
96  1 Y 1 A GLU 280 ? OE2 ? A GLU 278 OE2 
97  1 Y 1 A ASP 301 ? CG  ? A ASP 299 CG  
98  1 Y 1 A ASP 301 ? OD1 ? A ASP 299 OD1 
99  1 Y 1 A ASP 301 ? OD2 ? A ASP 299 OD2 
100 1 Y 1 A LYS 313 ? CG  ? A LYS 311 CG  
101 1 Y 1 A LYS 313 ? CD  ? A LYS 311 CD  
102 1 Y 1 A LYS 313 ? CE  ? A LYS 311 CE  
103 1 Y 1 A LYS 313 ? NZ  ? A LYS 311 NZ  
104 1 Y 1 A ASP 314 ? CG  ? A ASP 312 CG  
105 1 Y 1 A ASP 314 ? OD1 ? A ASP 312 OD1 
106 1 Y 1 A ASP 314 ? OD2 ? A ASP 312 OD2 
107 1 Y 1 A LYS 317 ? CG  ? A LYS 315 CG  
108 1 Y 1 A LYS 317 ? CD  ? A LYS 315 CD  
109 1 Y 1 A LYS 317 ? CE  ? A LYS 315 CE  
110 1 Y 1 A LYS 317 ? NZ  ? A LYS 315 NZ  
111 1 Y 1 A LYS 351 ? CE  ? A LYS 349 CE  
112 1 Y 1 A LYS 351 ? NZ  ? A LYS 349 NZ  
113 1 Y 1 A LYS 372 ? CG  ? A LYS 370 CG  
114 1 Y 1 A LYS 372 ? CD  ? A LYS 370 CD  
115 1 Y 1 A LYS 372 ? CE  ? A LYS 370 CE  
116 1 Y 1 A LYS 372 ? NZ  ? A LYS 370 NZ  
117 1 Y 1 A LYS 389 ? CG  ? A LYS 387 CG  
118 1 Y 1 A LYS 389 ? CD  ? A LYS 387 CD  
119 1 Y 1 A LYS 389 ? CE  ? A LYS 387 CE  
120 1 Y 1 A LYS 389 ? NZ  ? A LYS 387 NZ  
121 1 Y 1 A GLU 396 ? CG  ? A GLU 394 CG  
122 1 Y 1 A GLU 396 ? CD  ? A GLU 394 CD  
123 1 Y 1 A GLU 396 ? OE1 ? A GLU 394 OE1 
124 1 Y 1 A GLU 396 ? OE2 ? A GLU 394 OE2 
125 1 Y 1 A LYS 402 ? CD  ? A LYS 400 CD  
126 1 Y 1 A LYS 402 ? CE  ? A LYS 400 CE  
127 1 Y 1 A LYS 402 ? NZ  ? A LYS 400 NZ  
128 1 Y 1 A GLU 425 ? CD  ? A GLU 423 CD  
129 1 Y 1 A GLU 425 ? OE1 ? A GLU 423 OE1 
130 1 Y 1 A GLU 425 ? OE2 ? A GLU 423 OE2 
131 1 Y 1 A LYS 439 ? CG  ? A LYS 437 CG  
132 1 Y 1 A LYS 439 ? CD  ? A LYS 437 CD  
133 1 Y 1 A LYS 439 ? CE  ? A LYS 437 CE  
134 1 Y 1 A LYS 439 ? NZ  ? A LYS 437 NZ  
135 1 Y 1 A LYS 466 ? CE  ? A LYS 464 CE  
136 1 Y 1 A LYS 466 ? NZ  ? A LYS 464 NZ  
137 1 Y 1 A GLU 495 ? CG  ? A GLU 493 CG  
138 1 Y 1 A GLU 495 ? CD  ? A GLU 493 CD  
139 1 Y 1 A GLU 495 ? OE1 ? A GLU 493 OE1 
140 1 Y 1 A GLU 495 ? OE2 ? A GLU 493 OE2 
141 1 Y 1 A GLU 505 ? CG  ? A GLU 503 CG  
142 1 Y 1 A GLU 505 ? CD  ? A GLU 503 CD  
143 1 Y 1 A GLU 505 ? OE1 ? A GLU 503 OE1 
144 1 Y 1 A GLU 505 ? OE2 ? A GLU 503 OE2 
145 1 Y 1 A GLU 518 ? CG  ? A GLU 516 CG  
146 1 Y 1 A GLU 518 ? CD  ? A GLU 516 CD  
147 1 Y 1 A GLU 518 ? OE1 ? A GLU 516 OE1 
148 1 Y 1 A GLU 518 ? OE2 ? A GLU 516 OE2 
149 1 Y 1 A LYS 519 ? CE  ? A LYS 517 CE  
150 1 Y 1 A LYS 519 ? NZ  ? A LYS 517 NZ  
151 1 Y 1 A ARG 521 ? CZ  ? A ARG 519 CZ  
152 1 Y 1 A ARG 521 ? NH1 ? A ARG 519 NH1 
153 1 Y 1 A ARG 521 ? NH2 ? A ARG 519 NH2 
154 1 Y 1 A LYS 524 ? CE  ? A LYS 522 CE  
155 1 Y 1 A LYS 524 ? NZ  ? A LYS 522 NZ  
156 1 Y 1 A LYS 538 ? CG  ? A LYS 536 CG  
157 1 Y 1 A LYS 538 ? CD  ? A LYS 536 CD  
158 1 Y 1 A LYS 538 ? CE  ? A LYS 536 CE  
159 1 Y 1 A LYS 538 ? NZ  ? A LYS 536 NZ  
160 1 Y 1 A LYS 541 ? CE  ? A LYS 539 CE  
161 1 Y 1 A LYS 541 ? NZ  ? A LYS 539 NZ  
162 1 Y 1 A LYS 545 ? CD  ? A LYS 543 CD  
163 1 Y 1 A LYS 545 ? CE  ? A LYS 543 CE  
164 1 Y 1 A LYS 545 ? NZ  ? A LYS 543 NZ  
165 1 Y 1 A LYS 557 ? CD  ? A LYS 555 CD  
166 1 Y 1 A LYS 557 ? CE  ? A LYS 555 CE  
167 1 Y 1 A LYS 557 ? NZ  ? A LYS 555 NZ  
168 1 Y 1 A LYS 560 ? CD  ? A LYS 558 CD  
169 1 Y 1 A LYS 560 ? CE  ? A LYS 558 CE  
170 1 Y 1 A LYS 560 ? NZ  ? A LYS 558 NZ  
171 1 Y 1 A LYS 564 ? CG  ? A LYS 562 CG  
172 1 Y 1 A LYS 564 ? CD  ? A LYS 562 CD  
173 1 Y 1 A LYS 564 ? CE  ? A LYS 562 CE  
174 1 Y 1 A LYS 564 ? NZ  ? A LYS 562 NZ  
175 1 Y 1 A THR 566 ? OG1 ? A THR 564 OG1 
176 1 Y 1 A THR 566 ? CG2 ? A THR 564 CG2 
177 1 Y 1 A GLU 570 ? CG  ? A GLU 568 CG  
178 1 Y 1 A GLU 570 ? CD  ? A GLU 568 CD  
179 1 Y 1 A GLU 570 ? OE1 ? A GLU 568 OE1 
180 1 Y 1 A GLU 570 ? OE2 ? A GLU 568 OE2 
181 1 Y 1 A LYS 573 ? CD  ? A LYS 571 CD  
182 1 Y 1 A LYS 573 ? CE  ? A LYS 571 CE  
183 1 Y 1 A LYS 573 ? NZ  ? A LYS 571 NZ  
184 1 Y 1 I HIS 3   ? ND1 ? B HIS 1   ND1 
185 1 Y 1 I HIS 3   ? CD2 ? B HIS 1   CD2 
186 1 Y 1 I HIS 3   ? CE1 ? B HIS 1   CE1 
187 1 Y 1 I HIS 3   ? NE2 ? B HIS 1   NE2 
188 1 Y 1 I LYS 4   ? CG  ? B LYS 2   CG  
189 1 Y 1 I LYS 4   ? CD  ? B LYS 2   CD  
190 1 Y 1 I LYS 4   ? CE  ? B LYS 2   CE  
191 1 Y 1 I LYS 4   ? NZ  ? B LYS 2   NZ  
192 1 Y 1 I GLU 6   ? CG  ? B GLU 4   CG  
193 1 Y 1 I GLU 6   ? CD  ? B GLU 4   CD  
194 1 Y 1 I GLU 6   ? OE1 ? B GLU 4   OE1 
195 1 Y 1 I GLU 6   ? OE2 ? B GLU 4   OE2 
196 1 Y 1 I LYS 41  ? CG  ? B LYS 39  CG  
197 1 Y 1 I LYS 41  ? CD  ? B LYS 39  CD  
198 1 Y 1 I LYS 41  ? CE  ? B LYS 39  CE  
199 1 Y 1 I LYS 41  ? NZ  ? B LYS 39  NZ  
200 1 Y 1 I GLU 48  ? CG  ? B GLU 46  CG  
201 1 Y 1 I GLU 48  ? CD  ? B GLU 46  CD  
202 1 Y 1 I GLU 48  ? OE1 ? B GLU 46  OE1 
203 1 Y 1 I GLU 48  ? OE2 ? B GLU 46  OE2 
204 1 Y 1 I GLU 57  ? CG  ? B GLU 55  CG  
205 1 Y 1 I GLU 57  ? CD  ? B GLU 55  CD  
206 1 Y 1 I GLU 57  ? OE1 ? B GLU 55  OE1 
207 1 Y 1 I GLU 57  ? OE2 ? B GLU 55  OE2 
208 1 Y 1 I GLU 60  ? CG  ? B GLU 58  CG  
209 1 Y 1 I GLU 60  ? CD  ? B GLU 58  CD  
210 1 Y 1 I GLU 60  ? OE1 ? B GLU 58  OE1 
211 1 Y 1 I GLU 60  ? OE2 ? B GLU 58  OE2 
212 1 Y 1 I LYS 64  ? CE  ? B LYS 62  CE  
213 1 Y 1 I LYS 64  ? NZ  ? B LYS 62  NZ  
214 1 Y 1 I THR 79  ? OG1 ? B THR 77  OG1 
215 1 Y 1 I THR 79  ? CG2 ? B THR 77  CG2 
216 1 Y 1 I GLU 82  ? CG  ? B GLU 80  CG  
217 1 Y 1 I GLU 82  ? CD  ? B GLU 80  CD  
218 1 Y 1 I GLU 82  ? OE1 ? B GLU 80  OE1 
219 1 Y 1 I GLU 82  ? OE2 ? B GLU 80  OE2 
220 1 Y 1 I GLN 94  ? CG  ? B GLN 92  CG  
221 1 Y 1 I GLN 94  ? CD  ? B GLN 92  CD  
222 1 Y 1 I GLN 94  ? OE1 ? B GLN 92  OE1 
223 1 Y 1 I GLN 94  ? NE2 ? B GLN 92  NE2 
224 1 Y 1 I ASP 108 ? CG  ? B ASP 106 CG  
225 1 Y 1 I ASP 108 ? OD1 ? B ASP 106 OD1 
226 1 Y 1 I ASP 108 ? OD2 ? B ASP 106 OD2 
227 1 Y 1 I ASN 111 ? CG  ? B ASN 109 CG  
228 1 Y 1 I ASN 111 ? OD1 ? B ASN 109 OD1 
229 1 Y 1 I ASN 111 ? ND2 ? B ASN 109 ND2 
230 1 Y 1 I GLU 119 ? CG  ? B GLU 117 CG  
231 1 Y 1 I GLU 119 ? CD  ? B GLU 117 CD  
232 1 Y 1 I GLU 119 ? OE1 ? B GLU 117 OE1 
233 1 Y 1 I GLU 119 ? OE2 ? B GLU 117 OE2 
234 1 Y 1 I LYS 137 ? CG  ? B LYS 135 CG  
235 1 Y 1 I LYS 137 ? CD  ? B LYS 135 CD  
236 1 Y 1 I LYS 137 ? CE  ? B LYS 135 CE  
237 1 Y 1 I LYS 137 ? NZ  ? B LYS 135 NZ  
238 1 Y 1 I LYS 181 ? CE  ? B LYS 179 CE  
239 1 Y 1 I LYS 181 ? NZ  ? B LYS 179 NZ  
240 1 Y 1 I GLU 184 ? CG  ? B GLU 182 CG  
241 1 Y 1 I GLU 184 ? CD  ? B GLU 182 CD  
242 1 Y 1 I GLU 184 ? OE1 ? B GLU 182 OE1 
243 1 Y 1 I GLU 184 ? OE2 ? B GLU 182 OE2 
244 1 Y 1 I ARG 186 ? CZ  ? B ARG 184 CZ  
245 1 Y 1 I ARG 186 ? NH1 ? B ARG 184 NH1 
246 1 Y 1 I ARG 186 ? NH2 ? B ARG 184 NH2 
247 1 Y 1 I LYS 195 ? NZ  ? B LYS 193 NZ  
248 1 Y 1 I ARG 197 ? CG  ? B ARG 195 CG  
249 1 Y 1 I ARG 197 ? CD  ? B ARG 195 CD  
250 1 Y 1 I ARG 197 ? NE  ? B ARG 195 NE  
251 1 Y 1 I ARG 197 ? CZ  ? B ARG 195 CZ  
252 1 Y 1 I ARG 197 ? NH1 ? B ARG 195 NH1 
253 1 Y 1 I ARG 197 ? NH2 ? B ARG 195 NH2 
254 1 Y 1 I GLN 204 ? CG  ? B GLN 202 CG  
255 1 Y 1 I GLN 204 ? CD  ? B GLN 202 CD  
256 1 Y 1 I GLN 204 ? OE1 ? B GLN 202 OE1 
257 1 Y 1 I GLN 204 ? NE2 ? B GLN 202 NE2 
258 1 Y 1 I GLU 227 ? CG  ? B GLU 225 CG  
259 1 Y 1 I GLU 227 ? CD  ? B GLU 225 CD  
260 1 Y 1 I GLU 227 ? OE1 ? B GLU 225 OE1 
261 1 Y 1 I GLU 227 ? OE2 ? B GLU 225 OE2 
262 1 Y 1 I LYS 240 ? CD  ? B LYS 238 CD  
263 1 Y 1 I LYS 240 ? CE  ? B LYS 238 CE  
264 1 Y 1 I LYS 240 ? NZ  ? B LYS 238 NZ  
265 1 Y 1 I GLU 244 ? CD  ? B GLU 242 CD  
266 1 Y 1 I GLU 244 ? OE1 ? B GLU 242 OE1 
267 1 Y 1 I GLU 244 ? OE2 ? B GLU 242 OE2 
268 1 Y 1 I LYS 262 ? CG  ? B LYS 260 CG  
269 1 Y 1 I LYS 262 ? CD  ? B LYS 260 CD  
270 1 Y 1 I LYS 262 ? CE  ? B LYS 260 CE  
271 1 Y 1 I LYS 262 ? NZ  ? B LYS 260 NZ  
272 1 Y 1 I LYS 276 ? CG  ? B LYS 274 CG  
273 1 Y 1 I LYS 276 ? CD  ? B LYS 274 CD  
274 1 Y 1 I LYS 276 ? CE  ? B LYS 274 CE  
275 1 Y 1 I LYS 276 ? NZ  ? B LYS 274 NZ  
276 1 Y 1 I GLU 280 ? CG  ? B GLU 278 CG  
277 1 Y 1 I GLU 280 ? CD  ? B GLU 278 CD  
278 1 Y 1 I GLU 280 ? OE1 ? B GLU 278 OE1 
279 1 Y 1 I GLU 280 ? OE2 ? B GLU 278 OE2 
280 1 Y 1 I ASP 301 ? CG  ? B ASP 299 CG  
281 1 Y 1 I ASP 301 ? OD1 ? B ASP 299 OD1 
282 1 Y 1 I ASP 301 ? OD2 ? B ASP 299 OD2 
283 1 Y 1 I LYS 313 ? CG  ? B LYS 311 CG  
284 1 Y 1 I LYS 313 ? CD  ? B LYS 311 CD  
285 1 Y 1 I LYS 313 ? CE  ? B LYS 311 CE  
286 1 Y 1 I LYS 313 ? NZ  ? B LYS 311 NZ  
287 1 Y 1 I ASP 314 ? CG  ? B ASP 312 CG  
288 1 Y 1 I ASP 314 ? OD1 ? B ASP 312 OD1 
289 1 Y 1 I ASP 314 ? OD2 ? B ASP 312 OD2 
290 1 Y 1 I LYS 317 ? CG  ? B LYS 315 CG  
291 1 Y 1 I LYS 317 ? CD  ? B LYS 315 CD  
292 1 Y 1 I LYS 317 ? CE  ? B LYS 315 CE  
293 1 Y 1 I LYS 317 ? NZ  ? B LYS 315 NZ  
294 1 Y 1 I LYS 351 ? CE  ? B LYS 349 CE  
295 1 Y 1 I LYS 351 ? NZ  ? B LYS 349 NZ  
296 1 Y 1 I LYS 372 ? CG  ? B LYS 370 CG  
297 1 Y 1 I LYS 372 ? CD  ? B LYS 370 CD  
298 1 Y 1 I LYS 372 ? CE  ? B LYS 370 CE  
299 1 Y 1 I LYS 372 ? NZ  ? B LYS 370 NZ  
300 1 Y 1 I LYS 389 ? CG  ? B LYS 387 CG  
301 1 Y 1 I LYS 389 ? CD  ? B LYS 387 CD  
302 1 Y 1 I LYS 389 ? CE  ? B LYS 387 CE  
303 1 Y 1 I LYS 389 ? NZ  ? B LYS 387 NZ  
304 1 Y 1 I GLU 396 ? CG  ? B GLU 394 CG  
305 1 Y 1 I GLU 396 ? CD  ? B GLU 394 CD  
306 1 Y 1 I GLU 396 ? OE1 ? B GLU 394 OE1 
307 1 Y 1 I GLU 396 ? OE2 ? B GLU 394 OE2 
308 1 Y 1 I LYS 402 ? CD  ? B LYS 400 CD  
309 1 Y 1 I LYS 402 ? CE  ? B LYS 400 CE  
310 1 Y 1 I LYS 402 ? NZ  ? B LYS 400 NZ  
311 1 Y 1 I GLU 425 ? CD  ? B GLU 423 CD  
312 1 Y 1 I GLU 425 ? OE1 ? B GLU 423 OE1 
313 1 Y 1 I GLU 425 ? OE2 ? B GLU 423 OE2 
314 1 Y 1 I LYS 439 ? CG  ? B LYS 437 CG  
315 1 Y 1 I LYS 439 ? CD  ? B LYS 437 CD  
316 1 Y 1 I LYS 439 ? CE  ? B LYS 437 CE  
317 1 Y 1 I LYS 439 ? NZ  ? B LYS 437 NZ  
318 1 Y 1 I LYS 466 ? CE  ? B LYS 464 CE  
319 1 Y 1 I LYS 466 ? NZ  ? B LYS 464 NZ  
320 1 Y 1 I GLU 495 ? CG  ? B GLU 493 CG  
321 1 Y 1 I GLU 495 ? CD  ? B GLU 493 CD  
322 1 Y 1 I GLU 495 ? OE1 ? B GLU 493 OE1 
323 1 Y 1 I GLU 495 ? OE2 ? B GLU 493 OE2 
324 1 Y 1 I GLU 505 ? CG  ? B GLU 503 CG  
325 1 Y 1 I GLU 505 ? CD  ? B GLU 503 CD  
326 1 Y 1 I GLU 505 ? OE1 ? B GLU 503 OE1 
327 1 Y 1 I GLU 505 ? OE2 ? B GLU 503 OE2 
328 1 Y 1 I GLU 518 ? CG  ? B GLU 516 CG  
329 1 Y 1 I GLU 518 ? CD  ? B GLU 516 CD  
330 1 Y 1 I GLU 518 ? OE1 ? B GLU 516 OE1 
331 1 Y 1 I GLU 518 ? OE2 ? B GLU 516 OE2 
332 1 Y 1 I LYS 519 ? CE  ? B LYS 517 CE  
333 1 Y 1 I LYS 519 ? NZ  ? B LYS 517 NZ  
334 1 Y 1 I ARG 521 ? CZ  ? B ARG 519 CZ  
335 1 Y 1 I ARG 521 ? NH1 ? B ARG 519 NH1 
336 1 Y 1 I ARG 521 ? NH2 ? B ARG 519 NH2 
337 1 Y 1 I LYS 524 ? CE  ? B LYS 522 CE  
338 1 Y 1 I LYS 524 ? NZ  ? B LYS 522 NZ  
339 1 Y 1 I LYS 538 ? CG  ? B LYS 536 CG  
340 1 Y 1 I LYS 538 ? CD  ? B LYS 536 CD  
341 1 Y 1 I LYS 538 ? CE  ? B LYS 536 CE  
342 1 Y 1 I LYS 538 ? NZ  ? B LYS 536 NZ  
343 1 Y 1 I LYS 541 ? CE  ? B LYS 539 CE  
344 1 Y 1 I LYS 541 ? NZ  ? B LYS 539 NZ  
345 1 Y 1 I LYS 545 ? CD  ? B LYS 543 CD  
346 1 Y 1 I LYS 545 ? CE  ? B LYS 543 CE  
347 1 Y 1 I LYS 545 ? NZ  ? B LYS 543 NZ  
348 1 Y 1 I LYS 557 ? CD  ? B LYS 555 CD  
349 1 Y 1 I LYS 557 ? CE  ? B LYS 555 CE  
350 1 Y 1 I LYS 557 ? NZ  ? B LYS 555 NZ  
351 1 Y 1 I LYS 560 ? CD  ? B LYS 558 CD  
352 1 Y 1 I LYS 560 ? CE  ? B LYS 558 CE  
353 1 Y 1 I LYS 560 ? NZ  ? B LYS 558 NZ  
354 1 Y 1 I LYS 564 ? CG  ? B LYS 562 CG  
355 1 Y 1 I LYS 564 ? CD  ? B LYS 562 CD  
356 1 Y 1 I LYS 564 ? CE  ? B LYS 562 CE  
357 1 Y 1 I LYS 564 ? NZ  ? B LYS 562 NZ  
358 1 Y 1 I THR 566 ? OG1 ? B THR 564 OG1 
359 1 Y 1 I THR 566 ? CG2 ? B THR 564 CG2 
360 1 Y 1 I GLU 570 ? CG  ? B GLU 568 CG  
361 1 Y 1 I GLU 570 ? CD  ? B GLU 568 CD  
362 1 Y 1 I GLU 570 ? OE1 ? B GLU 568 OE1 
363 1 Y 1 I GLU 570 ? OE2 ? B GLU 568 OE2 
364 1 Y 1 I LYS 573 ? CD  ? B LYS 571 CD  
365 1 Y 1 I LYS 573 ? CE  ? B LYS 571 CE  
366 1 Y 1 I LYS 573 ? NZ  ? B LYS 571 NZ  
367 1 N 1 A PLM 603 ? CC  ? E PLM 1   CC  
368 1 N 1 A PLM 603 ? CD  ? E PLM 1   CD  
369 1 N 1 A PLM 603 ? CE  ? E PLM 1   CE  
370 1 N 1 A PLM 603 ? CF  ? E PLM 1   CF  
371 1 N 1 A PLM 603 ? CG  ? E PLM 1   CG  
372 1 N 1 A PLM 605 ? CG  ? G PLM 1   CG  
373 1 N 1 A PLM 607 ? CG  ? I PLM 1   CG  
374 1 N 1 I PLM 603 ? CC  ? M PLM 1   CC  
375 1 N 1 I PLM 603 ? CD  ? M PLM 1   CD  
376 1 N 1 I PLM 603 ? CE  ? M PLM 1   CE  
377 1 N 1 I PLM 603 ? CF  ? M PLM 1   CF  
378 1 N 1 I PLM 603 ? CG  ? M PLM 1   CG  
379 1 N 1 I PLM 605 ? CG  ? O PLM 1   CG  
380 1 N 1 I PLM 607 ? CG  ? Q PLM 1   CG  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? 7.21     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? 7.21     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? 2.7.0    4 
# 
_cell.angle_alpha                  75.02 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   89.28 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  79.82 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YG7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.347 
_cell.length_a_esd                 ? 
_cell.length_b                     92.608 
_cell.length_b_esd                 ? 
_cell.length_c                     95.219 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8YG7 
_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                   8YG7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.31 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG3350, 50 mM potassium phosphate (pH 7.5), 5% glycerol, 4% DMSO' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YG7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.09 
_reflns.d_resolution_low                               91.93 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     68329 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.55 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.70 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.051 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.0900 
_reflns_shell.d_res_low                                     2.1175 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2644 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.0301 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.03 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.04 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.780 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.904 
_refine.correlation_coeff_Fo_to_Fc_free          0.850 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8YG7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.09 
_refine.ls_d_res_low                             91.93 
_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                     68174 
_refine.ls_number_reflns_R_free                  3593 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.32 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.26507 
_refine.ls_R_factor_R_free                       0.32452 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.26191 
_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                    MASK 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.312 
_refine.pdbx_overall_ESU_R_Free                  0.259 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                           1 
_refine.overall_SU_B                             10.032 
_refine.overall_SU_ML                            0.258 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.09 
_refine_hist.d_res_low                        91.93 
_refine_hist.number_atoms_solvent             246 
_refine_hist.number_atoms_total               9420 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8886 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         288 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.014  0.019  9382  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  8586  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.724  1.991  12692 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.058  3.000  19928 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.369  5.000  1160  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.056 24.596 396   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.737 15.000 1496  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 22.686 15.000 42    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.092  0.200  1410  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.021  10334 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1828  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.369  3.329  4646  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.368  3.328  4645  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.628  4.986  5804  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.627  4.986  5805  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.836  3.708  4736  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.835  3.709  4737  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.486  5.449  6889  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.378  41.716 11110 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.366  41.694 11079 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.34 ? 0.50 1 'medium positional' ? A 8538 ? ? 1 
'X-RAY DIFFRACTION' 1 ? ? 3.24 ? 2.00 2 'medium thermal'    ? I 8538 ? ? 1 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.090 
_refine_ls_shell.d_res_low                        2.144 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             248 
_refine_ls_shell.number_reflns_R_work             5033 
_refine_ls_shell.percent_reflns_obs               96.25 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.335 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.380 
# 
_struct_ncs_dom.id            1 
_struct_ncs_dom.details       ? 
_struct_ncs_dom.pdbx_ens_id   1 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     8YG7 
_struct.title                        'HSA Copper Indomethacin Complex' 
_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        8YG7 
_struct_keywords.text            'Complex, PROTEIN BINDING' 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 5 ? 
T N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ALBU_HUMAN 
_struct_ref.pdbx_db_accession          P02768 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRE
TYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYK
AAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH
TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEA
KDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV
NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKAD
DKETCFAEEGKKLVAASQAAL
;
_struct_ref.pdbx_align_begin           27 
# 
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 8YG7 A 1 ? 581 ? P02768 27 ? 607 ? 3 583 
2 1 8YG7 I 1 ? 581 ? P02768 27 ? 607 ? 3 583 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,S 
2 1 B,K,L,M,N,O,P,Q,R,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 3   ? GLY A 13  ? SER A 5   GLY A 15  1 ? 11 
HELX_P HELX_P2  AA2 GLY A 13  ? LEU A 29  ? GLY A 15  LEU A 31  1 ? 17 
HELX_P HELX_P3  AA3 PRO A 33  ? ASP A 54  ? PRO A 35  ASP A 56  1 ? 22 
HELX_P HELX_P4  AA4 SER A 63  ? CYS A 73  ? SER A 65  CYS A 75  1 ? 11 
HELX_P HELX_P5  AA5 THR A 77  ? GLY A 83  ? THR A 79  GLY A 85  1 ? 7  
HELX_P HELX_P6  AA6 GLY A 83  ? CYS A 88  ? GLY A 85  CYS A 90  1 ? 6  
HELX_P HELX_P7  AA7 CYS A 89  ? LYS A 91  ? CYS A 91  LYS A 93  5 ? 3  
HELX_P HELX_P8  AA8 GLN A 92  ? HIS A 103 ? GLN A 94  HIS A 105 1 ? 12 
HELX_P HELX_P9  AA9 GLU A 117 ? ASN A 128 ? GLU A 119 ASN A 130 1 ? 12 
HELX_P HELX_P10 AB1 ASN A 128 ? HIS A 144 ? ASN A 130 HIS A 146 1 ? 17 
HELX_P HELX_P11 AB2 TYR A 148 ? CYS A 167 ? TYR A 150 CYS A 169 1 ? 20 
HELX_P HELX_P12 AB3 ASP A 171 ? PHE A 221 ? ASP A 173 PHE A 223 1 ? 51 
HELX_P HELX_P13 AB4 GLU A 225 ? GLY A 246 ? GLU A 227 GLY A 248 1 ? 22 
HELX_P HELX_P14 AB5 ASP A 247 ? ASN A 265 ? ASP A 249 ASN A 267 1 ? 19 
HELX_P HELX_P15 AB6 LEU A 273 ? GLU A 278 ? LEU A 275 GLU A 280 1 ? 6  
HELX_P HELX_P16 AB7 PRO A 280 ? VAL A 291 ? PRO A 282 VAL A 293 1 ? 12 
HELX_P HELX_P17 AB8 LEU A 303 ? VAL A 308 ? LEU A 305 VAL A 310 1 ? 6  
HELX_P HELX_P18 AB9 ASP A 312 ? ALA A 320 ? ASP A 314 ALA A 322 1 ? 9  
HELX_P HELX_P19 AC1 ALA A 320 ? HIS A 336 ? ALA A 322 HIS A 338 1 ? 17 
HELX_P HELX_P20 AC2 SER A 340 ? CYS A 359 ? SER A 342 CYS A 361 1 ? 20 
HELX_P HELX_P21 AC3 ASP A 363 ? ALA A 369 ? ASP A 365 ALA A 371 1 ? 7  
HELX_P HELX_P22 AC4 LYS A 370 ? LEU A 396 ? LYS A 372 LEU A 398 1 ? 27 
HELX_P HELX_P23 AC5 GLY A 397 ? VAL A 413 ? GLY A 399 VAL A 415 1 ? 17 
HELX_P HELX_P24 AC6 SER A 417 ? CYS A 436 ? SER A 419 CYS A 438 1 ? 20 
HELX_P HELX_P25 AC7 PRO A 439 ? THR A 465 ? PRO A 441 THR A 467 1 ? 27 
HELX_P HELX_P26 AC8 SER A 468 ? THR A 476 ? SER A 470 THR A 478 1 ? 9  
HELX_P HELX_P27 AC9 ASN A 481 ? LEU A 489 ? ASN A 483 LEU A 491 1 ? 9  
HELX_P HELX_P28 AD1 ALA A 509 ? LEU A 514 ? ALA A 511 LEU A 516 1 ? 6  
HELX_P HELX_P29 AD2 SER A 515 ? LYS A 534 ? SER A 517 LYS A 536 1 ? 20 
HELX_P HELX_P30 AD3 THR A 538 ? ALA A 559 ? THR A 540 ALA A 561 1 ? 22 
HELX_P HELX_P31 AD4 THR A 564 ? ALA A 580 ? THR A 566 ALA A 582 1 ? 17 
HELX_P HELX_P32 AD5 SER B 3   ? GLY B 13  ? SER I 5   GLY I 15  1 ? 11 
HELX_P HELX_P33 AD6 GLY B 13  ? LEU B 29  ? GLY I 15  LEU I 31  1 ? 17 
HELX_P HELX_P34 AD7 PRO B 33  ? ASP B 54  ? PRO I 35  ASP I 56  1 ? 22 
HELX_P HELX_P35 AD8 SER B 63  ? VAL B 75  ? SER I 65  VAL I 77  1 ? 13 
HELX_P HELX_P36 AD9 THR B 77  ? GLY B 83  ? THR I 79  GLY I 85  1 ? 7  
HELX_P HELX_P37 AE1 GLU B 84  ? LYS B 91  ? GLU I 86  LYS I 93  5 ? 8  
HELX_P HELX_P38 AE2 PRO B 94  ? HIS B 103 ? PRO I 96  HIS I 105 1 ? 10 
HELX_P HELX_P39 AE3 GLU B 117 ? ASN B 128 ? GLU I 119 ASN I 130 1 ? 12 
HELX_P HELX_P40 AE4 ASN B 128 ? HIS B 144 ? ASN I 130 HIS I 146 1 ? 17 
HELX_P HELX_P41 AE5 TYR B 148 ? CYS B 167 ? TYR I 150 CYS I 169 1 ? 20 
HELX_P HELX_P42 AE6 ASP B 171 ? PHE B 221 ? ASP I 173 PHE I 223 1 ? 51 
HELX_P HELX_P43 AE7 GLU B 225 ? GLY B 246 ? GLU I 227 GLY I 248 1 ? 22 
HELX_P HELX_P44 AE8 ASP B 247 ? ASN B 265 ? ASP I 249 ASN I 267 1 ? 19 
HELX_P HELX_P45 AE9 GLN B 266 ? ILE B 269 ? GLN I 268 ILE I 271 5 ? 4  
HELX_P HELX_P46 AF1 LEU B 273 ? LYS B 279 ? LEU I 275 LYS I 281 1 ? 7  
HELX_P HELX_P47 AF2 PRO B 280 ? VAL B 291 ? PRO I 282 VAL I 293 1 ? 12 
HELX_P HELX_P48 AF3 LEU B 303 ? VAL B 308 ? LEU I 305 VAL I 310 1 ? 6  
HELX_P HELX_P49 AF4 ASP B 312 ? ALA B 320 ? ASP I 314 ALA I 322 1 ? 9  
HELX_P HELX_P50 AF5 ALA B 320 ? HIS B 336 ? ALA I 322 HIS I 338 1 ? 17 
HELX_P HELX_P51 AF6 SER B 340 ? CYS B 359 ? SER I 342 CYS I 361 1 ? 20 
HELX_P HELX_P52 AF7 ASP B 363 ? TYR B 368 ? ASP I 365 TYR I 370 1 ? 6  
HELX_P HELX_P53 AF8 LYS B 370 ? LEU B 396 ? LYS I 372 LEU I 398 1 ? 27 
HELX_P HELX_P54 AF9 GLY B 397 ? VAL B 413 ? GLY I 399 VAL I 415 1 ? 17 
HELX_P HELX_P55 AG1 SER B 417 ? CYS B 436 ? SER I 419 CYS I 438 1 ? 20 
HELX_P HELX_P56 AG2 PRO B 439 ? THR B 465 ? PRO I 441 THR I 467 1 ? 27 
HELX_P HELX_P57 AG3 SER B 468 ? THR B 476 ? SER I 470 THR I 478 1 ? 9  
HELX_P HELX_P58 AG4 ASN B 481 ? ALA B 488 ? ASN I 483 ALA I 490 1 ? 8  
HELX_P HELX_P59 AG5 ALA B 502 ? THR B 506 ? ALA I 504 THR I 508 5 ? 5  
HELX_P HELX_P60 AG6 HIS B 508 ? CYS B 512 ? HIS I 510 CYS I 514 5 ? 5  
HELX_P HELX_P61 AG7 SER B 515 ? LYS B 534 ? SER I 517 LYS I 536 1 ? 20 
HELX_P HELX_P62 AG8 THR B 538 ? ALA B 559 ? THR I 540 ALA I 561 1 ? 22 
HELX_P HELX_P63 AG9 LYS B 562 ? LEU B 581 ? LYS I 564 LEU I 583 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 51  SG  ? ? ? 1_555 A CYS   60  SG   ? ? A CYS 53  A CYS   62  1_555 ? ? ? ? ? ? ? 2.078 ? ? 
disulf2  disulf ? ? A CYS 73  SG  ? ? ? 1_555 A CYS   89  SG   ? ? A CYS 75  A CYS   91  1_555 ? ? ? ? ? ? ? 2.067 ? ? 
disulf3  disulf ? ? A CYS 88  SG  ? ? ? 1_555 A CYS   99  SG   ? ? A CYS 90  A CYS   101 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf4  disulf ? ? A CYS 122 SG  ? ? ? 1_555 A CYS   167 SG   ? ? A CYS 124 A CYS   169 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
disulf5  disulf ? ? A CYS 166 SG  ? ? ? 1_555 A CYS   175 SG   ? ? A CYS 168 A CYS   177 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
disulf6  disulf ? ? A CYS 198 SG  ? ? ? 1_555 A CYS   244 SG   ? ? A CYS 200 A CYS   246 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf7  disulf ? ? A CYS 243 SG  ? ? ? 1_555 A CYS   251 SG   ? ? A CYS 245 A CYS   253 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf8  disulf ? ? A CYS 263 SG  ? ? ? 1_555 A CYS   277 SG   ? ? A CYS 265 A CYS   279 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf9  disulf ? ? A CYS 276 SG  ? ? ? 1_555 A CYS   287 SG   ? ? A CYS 278 A CYS   289 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
disulf10 disulf ? ? A CYS 314 SG  ? ? ? 1_555 A CYS   359 SG   ? ? A CYS 316 A CYS   361 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
disulf11 disulf ? ? A CYS 358 SG  ? ? ? 1_555 A CYS   367 SG   ? ? A CYS 360 A CYS   369 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
disulf12 disulf ? ? A CYS 390 SG  ? ? ? 1_555 A CYS   436 SG   ? ? A CYS 392 A CYS   438 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf13 disulf ? ? A CYS 435 SG  ? ? ? 1_555 A CYS   446 SG   ? ? A CYS 437 A CYS   448 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf14 disulf ? ? A CYS 459 SG  ? ? ? 1_555 A CYS   475 SG   ? ? A CYS 461 A CYS   477 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
disulf15 disulf ? ? A CYS 474 SG  ? ? ? 1_555 A CYS   485 SG   ? ? A CYS 476 A CYS   487 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
disulf16 disulf ? ? A CYS 512 SG  ? ? ? 1_555 A CYS   557 SG   ? ? A CYS 514 A CYS   559 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf17 disulf ? ? A CYS 556 SG  ? ? ? 1_555 A CYS   565 SG   ? ? A CYS 558 A CYS   567 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf18 disulf ? ? B CYS 51  SG  ? ? ? 1_555 B CYS   60  SG   ? ? I CYS 53  I CYS   62  1_555 ? ? ? ? ? ? ? 2.102 ? ? 
disulf19 disulf ? ? B CYS 73  SG  ? ? ? 1_555 B CYS   89  SG   ? ? I CYS 75  I CYS   91  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
disulf20 disulf ? ? B CYS 88  SG  ? ? ? 1_555 B CYS   99  SG   ? ? I CYS 90  I CYS   101 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
disulf21 disulf ? ? B CYS 122 SG  ? ? ? 1_555 B CYS   167 SG   ? ? I CYS 124 I CYS   169 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf22 disulf ? ? B CYS 166 SG  ? ? ? 1_555 B CYS   175 SG   ? ? I CYS 168 I CYS   177 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf23 disulf ? ? B CYS 198 SG  ? ? ? 1_555 B CYS   244 SG   ? ? I CYS 200 I CYS   246 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf24 disulf ? ? B CYS 243 SG  ? ? ? 1_555 B CYS   251 SG   ? ? I CYS 245 I CYS   253 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
disulf25 disulf ? ? B CYS 263 SG  ? ? ? 1_555 B CYS   277 SG   ? ? I CYS 265 I CYS   279 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf26 disulf ? ? B CYS 276 SG  ? ? ? 1_555 B CYS   287 SG   ? ? I CYS 278 I CYS   289 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
disulf27 disulf ? ? B CYS 314 SG  ? ? ? 1_555 B CYS   359 SG   ? ? I CYS 316 I CYS   361 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
disulf28 disulf ? ? B CYS 358 SG  ? ? ? 1_555 B CYS   367 SG   ? ? I CYS 360 I CYS   369 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
disulf29 disulf ? ? B CYS 390 SG  ? ? ? 1_555 B CYS   436 SG   ? ? I CYS 392 I CYS   438 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
disulf30 disulf ? ? B CYS 435 SG  ? ? ? 1_555 B CYS   446 SG   ? ? I CYS 437 I CYS   448 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf31 disulf ? ? B CYS 459 SG  ? ? ? 1_555 B CYS   475 SG   ? ? I CYS 461 I CYS   477 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf32 disulf ? ? B CYS 474 SG  ? ? ? 1_555 B CYS   485 SG   ? ? I CYS 476 I CYS   487 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
disulf33 disulf ? ? B CYS 512 SG  ? ? ? 1_555 B CYS   557 SG   ? ? I CYS 514 I CYS   559 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
disulf34 disulf ? ? B CYS 556 SG  ? ? ? 1_555 B CYS   565 SG   ? ? I CYS 558 I CYS   567 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc1  metalc ? ? A HIS 144 NE2 ? ? ? 1_555 C A1D6U .   CU01 ? ? A HIS 146 A A1D6U 601 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
metalc2  metalc ? ? B HIS 144 NE2 ? ? ? 1_555 K A1D6U .   CU01 ? ? I HIS 146 I A1D6U 601 1_555 ? ? ? ? ? ? ? 2.496 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2  ? A HIS   144 ? A HIS   146 ? 1_555 CU01 ? C A1D6U . ? A A1D6U 601 ? 1_555 N007 ? C A1D6U . ? A A1D6U 601 ? 1_555 153.5 ? 
2  NE2  ? A HIS   144 ? A HIS   146 ? 1_555 CU01 ? C A1D6U . ? A A1D6U 601 ? 1_555 S003 ? C A1D6U . ? A A1D6U 601 ? 1_555 73.3  ? 
3  N007 ? C A1D6U .   ? A A1D6U 601 ? 1_555 CU01 ? C A1D6U . ? A A1D6U 601 ? 1_555 S003 ? C A1D6U . ? A A1D6U 601 ? 1_555 84.7  ? 
4  NE2  ? A HIS   144 ? A HIS   146 ? 1_555 CU01 ? C A1D6U . ? A A1D6U 601 ? 1_555 N008 ? C A1D6U . ? A A1D6U 601 ? 1_555 123.0 ? 
5  N007 ? C A1D6U .   ? A A1D6U 601 ? 1_555 CU01 ? C A1D6U . ? A A1D6U 601 ? 1_555 N008 ? C A1D6U . ? A A1D6U 601 ? 1_555 78.6  ? 
6  S003 ? C A1D6U .   ? A A1D6U 601 ? 1_555 CU01 ? C A1D6U . ? A A1D6U 601 ? 1_555 N008 ? C A1D6U . ? A A1D6U 601 ? 1_555 163.3 ? 
7  NE2  ? B HIS   144 ? I HIS   146 ? 1_555 CU01 ? K A1D6U . ? I A1D6U 601 ? 1_555 N007 ? K A1D6U . ? I A1D6U 601 ? 1_555 156.2 ? 
8  NE2  ? B HIS   144 ? I HIS   146 ? 1_555 CU01 ? K A1D6U . ? I A1D6U 601 ? 1_555 S003 ? K A1D6U . ? I A1D6U 601 ? 1_555 75.2  ? 
9  N007 ? K A1D6U .   ? I A1D6U 601 ? 1_555 CU01 ? K A1D6U . ? I A1D6U 601 ? 1_555 S003 ? K A1D6U . ? I A1D6U 601 ? 1_555 84.7  ? 
10 NE2  ? B HIS   144 ? I HIS   146 ? 1_555 CU01 ? K A1D6U . ? I A1D6U 601 ? 1_555 N008 ? K A1D6U . ? I A1D6U 601 ? 1_555 120.8 ? 
11 N007 ? K A1D6U .   ? I A1D6U 601 ? 1_555 CU01 ? K A1D6U . ? I A1D6U 601 ? 1_555 N008 ? K A1D6U . ? I A1D6U 601 ? 1_555 78.9  ? 
12 S003 ? K A1D6U .   ? I A1D6U 601 ? 1_555 CU01 ? K A1D6U . ? I A1D6U 601 ? 1_555 N008 ? K A1D6U . ? I A1D6U 601 ? 1_555 163.6 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 51  ? CYS A 60  ? CYS A 53  ? 1_555 CYS A 62  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 73  ? CYS A 89  ? CYS A 75  ? 1_555 CYS A 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 88  ? CYS A 99  ? CYS A 90  ? 1_555 CYS A 101 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 122 ? CYS A 167 ? CYS A 124 ? 1_555 CYS A 169 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 166 ? CYS A 175 ? CYS A 168 ? 1_555 CYS A 177 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS A 198 ? CYS A 244 ? CYS A 200 ? 1_555 CYS A 246 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS A 243 ? CYS A 251 ? CYS A 245 ? 1_555 CYS A 253 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS A 263 ? CYS A 277 ? CYS A 265 ? 1_555 CYS A 279 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS A 276 ? CYS A 287 ? CYS A 278 ? 1_555 CYS A 289 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS A 314 ? CYS A 359 ? CYS A 316 ? 1_555 CYS A 361 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS A 358 ? CYS A 367 ? CYS A 360 ? 1_555 CYS A 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS A 390 ? CYS A 436 ? CYS A 392 ? 1_555 CYS A 438 ? 1_555 SG SG . . . None 'Disulfide bridge' 
13 CYS A 435 ? CYS A 446 ? CYS A 437 ? 1_555 CYS A 448 ? 1_555 SG SG . . . None 'Disulfide bridge' 
14 CYS A 459 ? CYS A 475 ? CYS A 461 ? 1_555 CYS A 477 ? 1_555 SG SG . . . None 'Disulfide bridge' 
15 CYS A 474 ? CYS A 485 ? CYS A 476 ? 1_555 CYS A 487 ? 1_555 SG SG . . . None 'Disulfide bridge' 
16 CYS A 512 ? CYS A 557 ? CYS A 514 ? 1_555 CYS A 559 ? 1_555 SG SG . . . None 'Disulfide bridge' 
17 CYS A 556 ? CYS A 565 ? CYS A 558 ? 1_555 CYS A 567 ? 1_555 SG SG . . . None 'Disulfide bridge' 
18 CYS B 51  ? CYS B 60  ? CYS I 53  ? 1_555 CYS I 62  ? 1_555 SG SG . . . None 'Disulfide bridge' 
19 CYS B 73  ? CYS B 89  ? CYS I 75  ? 1_555 CYS I 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
20 CYS B 88  ? CYS B 99  ? CYS I 90  ? 1_555 CYS I 101 ? 1_555 SG SG . . . None 'Disulfide bridge' 
21 CYS B 122 ? CYS B 167 ? CYS I 124 ? 1_555 CYS I 169 ? 1_555 SG SG . . . None 'Disulfide bridge' 
22 CYS B 166 ? CYS B 175 ? CYS I 168 ? 1_555 CYS I 177 ? 1_555 SG SG . . . None 'Disulfide bridge' 
23 CYS B 198 ? CYS B 244 ? CYS I 200 ? 1_555 CYS I 246 ? 1_555 SG SG . . . None 'Disulfide bridge' 
24 CYS B 243 ? CYS B 251 ? CYS I 245 ? 1_555 CYS I 253 ? 1_555 SG SG . . . None 'Disulfide bridge' 
25 CYS B 263 ? CYS B 277 ? CYS I 265 ? 1_555 CYS I 279 ? 1_555 SG SG . . . None 'Disulfide bridge' 
26 CYS B 276 ? CYS B 287 ? CYS I 278 ? 1_555 CYS I 289 ? 1_555 SG SG . . . None 'Disulfide bridge' 
27 CYS B 314 ? CYS B 359 ? CYS I 316 ? 1_555 CYS I 361 ? 1_555 SG SG . . . None 'Disulfide bridge' 
28 CYS B 358 ? CYS B 367 ? CYS I 360 ? 1_555 CYS I 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
29 CYS B 390 ? CYS B 436 ? CYS I 392 ? 1_555 CYS I 438 ? 1_555 SG SG . . . None 'Disulfide bridge' 
30 CYS B 435 ? CYS B 446 ? CYS I 437 ? 1_555 CYS I 448 ? 1_555 SG SG . . . None 'Disulfide bridge' 
31 CYS B 459 ? CYS B 475 ? CYS I 461 ? 1_555 CYS I 477 ? 1_555 SG SG . . . None 'Disulfide bridge' 
32 CYS B 474 ? CYS B 485 ? CYS I 476 ? 1_555 CYS I 487 ? 1_555 SG SG . . . None 'Disulfide bridge' 
33 CYS B 512 ? CYS B 557 ? CYS I 514 ? 1_555 CYS I 559 ? 1_555 SG SG . . . None 'Disulfide bridge' 
34 CYS B 556 ? CYS B 565 ? CYS I 558 ? 1_555 CYS I 567 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_pdbx_entry_details.entry_id                   8YG7 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NE2 I HIS 464 ? ? O  I HOH 701 ? ? 1.90 
2 1 N   A TYR 411 ? ? O  A HOH 701 ? ? 1.97 
3 1 O   A LEU 408 ? ? O  A HOH 701 ? ? 2.02 
4 1 OE1 A GLU 383 ? ? O  A HOH 702 ? ? 2.04 
5 1 N   I VAL 40  ? ? O  I HOH 702 ? ? 2.05 
6 1 O   I GLU 37  ? ? O  I HOH 702 ? ? 2.09 
7 1 OE2 A GLU 16  ? ? NZ A LYS 51  ? ? 2.16 
8 1 OE2 A GLU 153 ? ? O  A HOH 703 ? ? 2.17 
9 1 O   A HOH 709 ? ? O  A HOH 823 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 144 ? ? CZ A ARG 144 ? ? NH2 A ARG 144 ? ? 116.99 120.30 -3.31 0.50 N 
2 1 NE A ARG 218 ? ? CZ A ARG 218 ? ? NH1 A ARG 218 ? ? 123.31 120.30 3.01  0.50 N 
3 1 CA A CYS 559 ? ? CB A CYS 559 ? ? SG  A CYS 559 ? ? 120.95 114.20 6.75  1.10 N 
4 1 NE I ARG 81  ? ? CZ I ARG 81  ? ? NH1 I ARG 81  ? ? 123.31 120.30 3.01  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 31  ? ? -114.33 66.35  
2  1 ASN A 61  ? ? 67.71   -2.55  
3  1 ASN A 109 ? ? 76.02   95.30  
4  1 ASN A 111 ? ? -67.86  89.37  
5  1 ILE A 271 ? ? -124.45 -62.40 
6  1 VAL A 310 ? ? -125.95 -55.28 
7  1 ALA A 322 ? ? -170.59 86.64  
8  1 ALA A 363 ? ? -49.35  155.35 
9  1 VAL A 469 ? ? -167.61 -37.60 
10 1 PRO A 499 ? ? -38.07  133.26 
11 1 ASP A 512 ? ? -38.59  -35.54 
12 1 ASP A 563 ? ? 107.08  122.12 
13 1 ALA A 569 ? ? 175.12  -46.31 
14 1 LEU I 31  ? ? -115.48 58.33  
15 1 ASP I 56  ? ? -161.13 107.92 
16 1 GLU I 60  ? ? -33.16  131.69 
17 1 ASN I 61  ? ? 70.05   -6.08  
18 1 ARG I 114 ? ? -39.19  125.44 
19 1 ASN I 130 ? ? -157.14 88.06  
20 1 GLN I 170 ? ? -116.89 58.22  
21 1 ASP I 173 ? ? -100.17 72.70  
22 1 PHE I 223 ? ? -119.75 52.16  
23 1 ILE I 271 ? ? -125.17 -60.94 
24 1 VAL I 310 ? ? -129.39 -57.47 
25 1 ASP I 314 ? ? 104.48  -0.20  
26 1 ALA I 322 ? ? -165.96 85.37  
27 1 LYS I 372 ? ? -108.18 40.19  
28 1 VAL I 469 ? ? -168.16 -36.85 
29 1 ASP I 563 ? ? 67.57   123.10 
30 1 LYS I 564 ? ? -94.75  -62.37 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_1   I 
_pdbx_validate_peptide_omega.auth_seq_id_1    95 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   I 
_pdbx_validate_peptide_omega.auth_seq_id_2    96 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            143.83 
# 
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 
A1D6U CU01 CU N N 1   
A1D6U S003 S  N N 2   
A1D6U N007 N  N N 3   
A1D6U N008 N  Y N 4   
A1D6U N00C N  N N 5   
A1D6U N00E N  N N 6   
A1D6U C00F C  N N 7   
A1D6U C00G C  Y N 8   
A1D6U C00J C  N N 9   
A1D6U C00L C  Y N 10  
A1D6U C00O C  N N 11  
A1D6U C00Q C  Y N 12  
A1D6U C00T C  Y N 13  
A1D6U C00U C  N N 14  
A1D6U C00V C  Y N 15  
A1D6U C00Y C  N N 16  
A1D6U C00Z C  N N 17  
A1D6U C012 C  N N 18  
A1D6U H2   H  N N 19  
A1D6U H3   H  N N 20  
A1D6U H4   H  N N 21  
A1D6U H5   H  N N 22  
A1D6U H6   H  N N 23  
A1D6U H7   H  N N 24  
A1D6U H8   H  N N 25  
A1D6U H9   H  N N 26  
A1D6U H10  H  N N 27  
A1D6U H11  H  N N 28  
A1D6U H12  H  N N 29  
A1D6U H13  H  N N 30  
A1D6U H14  H  N N 31  
A1D6U H15  H  N N 32  
A1D6U H16  H  N N 33  
A1D6U H17  H  N N 34  
A1D6U H18  H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HIS   N    N  N N 172 
HIS   CA   C  N S 173 
HIS   C    C  N N 174 
HIS   O    O  N N 175 
HIS   CB   C  N N 176 
HIS   CG   C  Y N 177 
HIS   ND1  N  Y N 178 
HIS   CD2  C  Y N 179 
HIS   CE1  C  Y N 180 
HIS   NE2  N  Y N 181 
HIS   OXT  O  N N 182 
HIS   H    H  N N 183 
HIS   H2   H  N N 184 
HIS   HA   H  N N 185 
HIS   HB2  H  N N 186 
HIS   HB3  H  N N 187 
HIS   HD1  H  N N 188 
HIS   HD2  H  N N 189 
HIS   HE1  H  N N 190 
HIS   HE2  H  N N 191 
HIS   HXT  H  N N 192 
HOH   O    O  N N 193 
HOH   H1   H  N N 194 
HOH   H2   H  N N 195 
ILE   N    N  N N 196 
ILE   CA   C  N S 197 
ILE   C    C  N N 198 
ILE   O    O  N N 199 
ILE   CB   C  N S 200 
ILE   CG1  C  N N 201 
ILE   CG2  C  N N 202 
ILE   CD1  C  N N 203 
ILE   OXT  O  N N 204 
ILE   H    H  N N 205 
ILE   H2   H  N N 206 
ILE   HA   H  N N 207 
ILE   HB   H  N N 208 
ILE   HG12 H  N N 209 
ILE   HG13 H  N N 210 
ILE   HG21 H  N N 211 
ILE   HG22 H  N N 212 
ILE   HG23 H  N N 213 
ILE   HD11 H  N N 214 
ILE   HD12 H  N N 215 
ILE   HD13 H  N N 216 
ILE   HXT  H  N N 217 
IMN   C    C  Y N 218 
IMN   C1   C  Y N 219 
IMN   C2   C  Y N 220 
IMN   C3   C  Y N 221 
IMN   C4   C  Y N 222 
IMN   C5   C  Y N 223 
IMN   C6   C  N N 224 
IMN   C7   C  Y N 225 
IMN   C8   C  Y N 226 
IMN   C9   C  N N 227 
IMN   C10  C  Y N 228 
IMN   C11  C  Y N 229 
IMN   C12  C  Y N 230 
IMN   C13  C  Y N 231 
IMN   C14  C  Y N 232 
IMN   C15  C  Y N 233 
IMN   C16  C  N N 234 
IMN   C17  C  N N 235 
IMN   C18  C  N N 236 
IMN   N    N  Y N 237 
IMN   O    O  N N 238 
IMN   O1   O  N N 239 
IMN   O2   O  N N 240 
IMN   O3   O  N N 241 
IMN   CL   CL N N 242 
IMN   H2   H  N N 243 
IMN   H4   H  N N 244 
IMN   H5   H  N N 245 
IMN   H61  H  N N 246 
IMN   H62  H  N N 247 
IMN   H63  H  N N 248 
IMN   H11  H  N N 249 
IMN   H12  H  N N 250 
IMN   H14  H  N N 251 
IMN   H15  H  N N 252 
IMN   H161 H  N N 253 
IMN   H162 H  N N 254 
IMN   H163 H  N N 255 
IMN   H171 H  N N 256 
IMN   H172 H  N N 257 
IMN   HO3  H  N N 258 
LEU   N    N  N N 259 
LEU   CA   C  N S 260 
LEU   C    C  N N 261 
LEU   O    O  N N 262 
LEU   CB   C  N N 263 
LEU   CG   C  N N 264 
LEU   CD1  C  N N 265 
LEU   CD2  C  N N 266 
LEU   OXT  O  N N 267 
LEU   H    H  N N 268 
LEU   H2   H  N N 269 
LEU   HA   H  N N 270 
LEU   HB2  H  N N 271 
LEU   HB3  H  N N 272 
LEU   HG   H  N N 273 
LEU   HD11 H  N N 274 
LEU   HD12 H  N N 275 
LEU   HD13 H  N N 276 
LEU   HD21 H  N N 277 
LEU   HD22 H  N N 278 
LEU   HD23 H  N N 279 
LEU   HXT  H  N N 280 
LYS   N    N  N N 281 
LYS   CA   C  N S 282 
LYS   C    C  N N 283 
LYS   O    O  N N 284 
LYS   CB   C  N N 285 
LYS   CG   C  N N 286 
LYS   CD   C  N N 287 
LYS   CE   C  N N 288 
LYS   NZ   N  N N 289 
LYS   OXT  O  N N 290 
LYS   H    H  N N 291 
LYS   H2   H  N N 292 
LYS   HA   H  N N 293 
LYS   HB2  H  N N 294 
LYS   HB3  H  N N 295 
LYS   HG2  H  N N 296 
LYS   HG3  H  N N 297 
LYS   HD2  H  N N 298 
LYS   HD3  H  N N 299 
LYS   HE2  H  N N 300 
LYS   HE3  H  N N 301 
LYS   HZ1  H  N N 302 
LYS   HZ2  H  N N 303 
LYS   HZ3  H  N N 304 
LYS   HXT  H  N N 305 
MET   N    N  N N 306 
MET   CA   C  N S 307 
MET   C    C  N N 308 
MET   O    O  N N 309 
MET   CB   C  N N 310 
MET   CG   C  N N 311 
MET   SD   S  N N 312 
MET   CE   C  N N 313 
MET   OXT  O  N N 314 
MET   H    H  N N 315 
MET   H2   H  N N 316 
MET   HA   H  N N 317 
MET   HB2  H  N N 318 
MET   HB3  H  N N 319 
MET   HG2  H  N N 320 
MET   HG3  H  N N 321 
MET   HE1  H  N N 322 
MET   HE2  H  N N 323 
MET   HE3  H  N N 324 
MET   HXT  H  N N 325 
PHE   N    N  N N 326 
PHE   CA   C  N S 327 
PHE   C    C  N N 328 
PHE   O    O  N N 329 
PHE   CB   C  N N 330 
PHE   CG   C  Y N 331 
PHE   CD1  C  Y N 332 
PHE   CD2  C  Y N 333 
PHE   CE1  C  Y N 334 
PHE   CE2  C  Y N 335 
PHE   CZ   C  Y N 336 
PHE   OXT  O  N N 337 
PHE   H    H  N N 338 
PHE   H2   H  N N 339 
PHE   HA   H  N N 340 
PHE   HB2  H  N N 341 
PHE   HB3  H  N N 342 
PHE   HD1  H  N N 343 
PHE   HD2  H  N N 344 
PHE   HE1  H  N N 345 
PHE   HE2  H  N N 346 
PHE   HZ   H  N N 347 
PHE   HXT  H  N N 348 
PLM   C1   C  N N 349 
PLM   O1   O  N N 350 
PLM   O2   O  N N 351 
PLM   C2   C  N N 352 
PLM   C3   C  N N 353 
PLM   C4   C  N N 354 
PLM   C5   C  N N 355 
PLM   C6   C  N N 356 
PLM   C7   C  N N 357 
PLM   C8   C  N N 358 
PLM   C9   C  N N 359 
PLM   CA   C  N N 360 
PLM   CB   C  N N 361 
PLM   CC   C  N N 362 
PLM   CD   C  N N 363 
PLM   CE   C  N N 364 
PLM   CF   C  N N 365 
PLM   CG   C  N N 366 
PLM   H    H  N N 367 
PLM   H21  H  N N 368 
PLM   H22  H  N N 369 
PLM   H31  H  N N 370 
PLM   H32  H  N N 371 
PLM   H41  H  N N 372 
PLM   H42  H  N N 373 
PLM   H51  H  N N 374 
PLM   H52  H  N N 375 
PLM   H61  H  N N 376 
PLM   H62  H  N N 377 
PLM   H71  H  N N 378 
PLM   H72  H  N N 379 
PLM   H81  H  N N 380 
PLM   H82  H  N N 381 
PLM   H91  H  N N 382 
PLM   H92  H  N N 383 
PLM   HA1  H  N N 384 
PLM   HA2  H  N N 385 
PLM   HB1  H  N N 386 
PLM   HB2  H  N N 387 
PLM   HC1  H  N N 388 
PLM   HC2  H  N N 389 
PLM   HD1  H  N N 390 
PLM   HD2  H  N N 391 
PLM   HE1  H  N N 392 
PLM   HE2  H  N N 393 
PLM   HF1  H  N N 394 
PLM   HF2  H  N N 395 
PLM   HG1  H  N N 396 
PLM   HG2  H  N N 397 
PLM   HG3  H  N N 398 
PRO   N    N  N N 399 
PRO   CA   C  N S 400 
PRO   C    C  N N 401 
PRO   O    O  N N 402 
PRO   CB   C  N N 403 
PRO   CG   C  N N 404 
PRO   CD   C  N N 405 
PRO   OXT  O  N N 406 
PRO   H    H  N N 407 
PRO   HA   H  N N 408 
PRO   HB2  H  N N 409 
PRO   HB3  H  N N 410 
PRO   HG2  H  N N 411 
PRO   HG3  H  N N 412 
PRO   HD2  H  N N 413 
PRO   HD3  H  N N 414 
PRO   HXT  H  N N 415 
SER   N    N  N N 416 
SER   CA   C  N S 417 
SER   C    C  N N 418 
SER   O    O  N N 419 
SER   CB   C  N N 420 
SER   OG   O  N N 421 
SER   OXT  O  N N 422 
SER   H    H  N N 423 
SER   H2   H  N N 424 
SER   HA   H  N N 425 
SER   HB2  H  N N 426 
SER   HB3  H  N N 427 
SER   HG   H  N N 428 
SER   HXT  H  N N 429 
THR   N    N  N N 430 
THR   CA   C  N S 431 
THR   C    C  N N 432 
THR   O    O  N N 433 
THR   CB   C  N R 434 
THR   OG1  O  N N 435 
THR   CG2  C  N N 436 
THR   OXT  O  N N 437 
THR   H    H  N N 438 
THR   H2   H  N N 439 
THR   HA   H  N N 440 
THR   HB   H  N N 441 
THR   HG1  H  N N 442 
THR   HG21 H  N N 443 
THR   HG22 H  N N 444 
THR   HG23 H  N N 445 
THR   HXT  H  N N 446 
TRP   N    N  N N 447 
TRP   CA   C  N S 448 
TRP   C    C  N N 449 
TRP   O    O  N N 450 
TRP   CB   C  N N 451 
TRP   CG   C  Y N 452 
TRP   CD1  C  Y N 453 
TRP   CD2  C  Y N 454 
TRP   NE1  N  Y N 455 
TRP   CE2  C  Y N 456 
TRP   CE3  C  Y N 457 
TRP   CZ2  C  Y N 458 
TRP   CZ3  C  Y N 459 
TRP   CH2  C  Y N 460 
TRP   OXT  O  N N 461 
TRP   H    H  N N 462 
TRP   H2   H  N N 463 
TRP   HA   H  N N 464 
TRP   HB2  H  N N 465 
TRP   HB3  H  N N 466 
TRP   HD1  H  N N 467 
TRP   HE1  H  N N 468 
TRP   HE3  H  N N 469 
TRP   HZ2  H  N N 470 
TRP   HZ3  H  N N 471 
TRP   HH2  H  N N 472 
TRP   HXT  H  N N 473 
TYR   N    N  N N 474 
TYR   CA   C  N S 475 
TYR   C    C  N N 476 
TYR   O    O  N N 477 
TYR   CB   C  N N 478 
TYR   CG   C  Y N 479 
TYR   CD1  C  Y N 480 
TYR   CD2  C  Y N 481 
TYR   CE1  C  Y N 482 
TYR   CE2  C  Y N 483 
TYR   CZ   C  Y N 484 
TYR   OH   O  N N 485 
TYR   OXT  O  N N 486 
TYR   H    H  N N 487 
TYR   H2   H  N N 488 
TYR   HA   H  N N 489 
TYR   HB2  H  N N 490 
TYR   HB3  H  N N 491 
TYR   HD1  H  N N 492 
TYR   HD2  H  N N 493 
TYR   HE1  H  N N 494 
TYR   HE2  H  N N 495 
TYR   HH   H  N N 496 
TYR   HXT  H  N N 497 
VAL   N    N  N N 498 
VAL   CA   C  N S 499 
VAL   C    C  N N 500 
VAL   O    O  N N 501 
VAL   CB   C  N N 502 
VAL   CG1  C  N N 503 
VAL   CG2  C  N N 504 
VAL   OXT  O  N N 505 
VAL   H    H  N N 506 
VAL   H2   H  N N 507 
VAL   HA   H  N N 508 
VAL   HB   H  N N 509 
VAL   HG11 H  N N 510 
VAL   HG12 H  N N 511 
VAL   HG13 H  N N 512 
VAL   HG21 H  N N 513 
VAL   HG22 H  N N 514 
VAL   HG23 H  N N 515 
VAL   HXT  H  N N 516 
# 
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 
A1D6U C00Z N00E sing N N 1   
A1D6U C00U N00E sing N N 2   
A1D6U N00E C00J sing N N 3   
A1D6U C012 C00O sing N N 4   
A1D6U C00J N00C doub N N 5   
A1D6U C00J S003 sing N N 6   
A1D6U N00C N007 sing N N 7   
A1D6U C00O C00Y sing N N 8   
A1D6U C00O C00F sing N N 9   
A1D6U N007 C00F doub N N 10  
A1D6U N007 CU01 sing N N 11  
A1D6U C00F C00G sing N N 12  
A1D6U S003 CU01 sing N N 13  
A1D6U C00G C00T doub Y N 14  
A1D6U C00G N008 sing Y N 15  
A1D6U CU01 N008 sing N N 16  
A1D6U C00T C00V sing Y N 17  
A1D6U N008 C00L doub Y N 18  
A1D6U C00V C00Q doub Y N 19  
A1D6U C00L C00Q sing Y N 20  
A1D6U C00L H2   sing N N 21  
A1D6U C00O H3   sing N N 22  
A1D6U C00Q H4   sing N N 23  
A1D6U C00T H5   sing N N 24  
A1D6U C00U H6   sing N N 25  
A1D6U C00U H7   sing N N 26  
A1D6U C00U H8   sing N N 27  
A1D6U C00V H9   sing N N 28  
A1D6U C00Y H10  sing N N 29  
A1D6U C00Y H11  sing N N 30  
A1D6U C00Y H12  sing N N 31  
A1D6U C00Z H13  sing N N 32  
A1D6U C00Z H14  sing N N 33  
A1D6U C00Z H15  sing N N 34  
A1D6U C012 H16  sing N N 35  
A1D6U C012 H17  sing N N 36  
A1D6U C012 H18  sing N N 37  
ALA   N    CA   sing N N 38  
ALA   N    H    sing N N 39  
ALA   N    H2   sing N N 40  
ALA   CA   C    sing N N 41  
ALA   CA   CB   sing N N 42  
ALA   CA   HA   sing N N 43  
ALA   C    O    doub N N 44  
ALA   C    OXT  sing N N 45  
ALA   CB   HB1  sing N N 46  
ALA   CB   HB2  sing N N 47  
ALA   CB   HB3  sing N N 48  
ALA   OXT  HXT  sing N N 49  
ARG   N    CA   sing N N 50  
ARG   N    H    sing N N 51  
ARG   N    H2   sing N N 52  
ARG   CA   C    sing N N 53  
ARG   CA   CB   sing N N 54  
ARG   CA   HA   sing N N 55  
ARG   C    O    doub N N 56  
ARG   C    OXT  sing N N 57  
ARG   CB   CG   sing N N 58  
ARG   CB   HB2  sing N N 59  
ARG   CB   HB3  sing N N 60  
ARG   CG   CD   sing N N 61  
ARG   CG   HG2  sing N N 62  
ARG   CG   HG3  sing N N 63  
ARG   CD   NE   sing N N 64  
ARG   CD   HD2  sing N N 65  
ARG   CD   HD3  sing N N 66  
ARG   NE   CZ   sing N N 67  
ARG   NE   HE   sing N N 68  
ARG   CZ   NH1  sing N N 69  
ARG   CZ   NH2  doub N N 70  
ARG   NH1  HH11 sing N N 71  
ARG   NH1  HH12 sing N N 72  
ARG   NH2  HH21 sing N N 73  
ARG   NH2  HH22 sing N N 74  
ARG   OXT  HXT  sing N N 75  
ASN   N    CA   sing N N 76  
ASN   N    H    sing N N 77  
ASN   N    H2   sing N N 78  
ASN   CA   C    sing N N 79  
ASN   CA   CB   sing N N 80  
ASN   CA   HA   sing N N 81  
ASN   C    O    doub N N 82  
ASN   C    OXT  sing N N 83  
ASN   CB   CG   sing N N 84  
ASN   CB   HB2  sing N N 85  
ASN   CB   HB3  sing N N 86  
ASN   CG   OD1  doub N N 87  
ASN   CG   ND2  sing N N 88  
ASN   ND2  HD21 sing N N 89  
ASN   ND2  HD22 sing N N 90  
ASN   OXT  HXT  sing N N 91  
ASP   N    CA   sing N N 92  
ASP   N    H    sing N N 93  
ASP   N    H2   sing N N 94  
ASP   CA   C    sing N N 95  
ASP   CA   CB   sing N N 96  
ASP   CA   HA   sing N N 97  
ASP   C    O    doub N N 98  
ASP   C    OXT  sing N N 99  
ASP   CB   CG   sing N N 100 
ASP   CB   HB2  sing N N 101 
ASP   CB   HB3  sing N N 102 
ASP   CG   OD1  doub N N 103 
ASP   CG   OD2  sing N N 104 
ASP   OD2  HD2  sing N N 105 
ASP   OXT  HXT  sing N N 106 
CYS   N    CA   sing N N 107 
CYS   N    H    sing N N 108 
CYS   N    H2   sing N N 109 
CYS   CA   C    sing N N 110 
CYS   CA   CB   sing N N 111 
CYS   CA   HA   sing N N 112 
CYS   C    O    doub N N 113 
CYS   C    OXT  sing N N 114 
CYS   CB   SG   sing N N 115 
CYS   CB   HB2  sing N N 116 
CYS   CB   HB3  sing N N 117 
CYS   SG   HG   sing N N 118 
CYS   OXT  HXT  sing N N 119 
GLN   N    CA   sing N N 120 
GLN   N    H    sing N N 121 
GLN   N    H2   sing N N 122 
GLN   CA   C    sing N N 123 
GLN   CA   CB   sing N N 124 
GLN   CA   HA   sing N N 125 
GLN   C    O    doub N N 126 
GLN   C    OXT  sing N N 127 
GLN   CB   CG   sing N N 128 
GLN   CB   HB2  sing N N 129 
GLN   CB   HB3  sing N N 130 
GLN   CG   CD   sing N N 131 
GLN   CG   HG2  sing N N 132 
GLN   CG   HG3  sing N N 133 
GLN   CD   OE1  doub N N 134 
GLN   CD   NE2  sing N N 135 
GLN   NE2  HE21 sing N N 136 
GLN   NE2  HE22 sing N N 137 
GLN   OXT  HXT  sing N N 138 
GLU   N    CA   sing N N 139 
GLU   N    H    sing N N 140 
GLU   N    H2   sing N N 141 
GLU   CA   C    sing N N 142 
GLU   CA   CB   sing N N 143 
GLU   CA   HA   sing N N 144 
GLU   C    O    doub N N 145 
GLU   C    OXT  sing N N 146 
GLU   CB   CG   sing N N 147 
GLU   CB   HB2  sing N N 148 
GLU   CB   HB3  sing N N 149 
GLU   CG   CD   sing N N 150 
GLU   CG   HG2  sing N N 151 
GLU   CG   HG3  sing N N 152 
GLU   CD   OE1  doub N N 153 
GLU   CD   OE2  sing N N 154 
GLU   OE2  HE2  sing N N 155 
GLU   OXT  HXT  sing N N 156 
GLY   N    CA   sing N N 157 
GLY   N    H    sing N N 158 
GLY   N    H2   sing N N 159 
GLY   CA   C    sing N N 160 
GLY   CA   HA2  sing N N 161 
GLY   CA   HA3  sing N N 162 
GLY   C    O    doub N N 163 
GLY   C    OXT  sing N N 164 
GLY   OXT  HXT  sing N N 165 
HIS   N    CA   sing N N 166 
HIS   N    H    sing N N 167 
HIS   N    H2   sing N N 168 
HIS   CA   C    sing N N 169 
HIS   CA   CB   sing N N 170 
HIS   CA   HA   sing N N 171 
HIS   C    O    doub N N 172 
HIS   C    OXT  sing N N 173 
HIS   CB   CG   sing N N 174 
HIS   CB   HB2  sing N N 175 
HIS   CB   HB3  sing N N 176 
HIS   CG   ND1  sing Y N 177 
HIS   CG   CD2  doub Y N 178 
HIS   ND1  CE1  doub Y N 179 
HIS   ND1  HD1  sing N N 180 
HIS   CD2  NE2  sing Y N 181 
HIS   CD2  HD2  sing N N 182 
HIS   CE1  NE2  sing Y N 183 
HIS   CE1  HE1  sing N N 184 
HIS   NE2  HE2  sing N N 185 
HIS   OXT  HXT  sing N N 186 
HOH   O    H1   sing N N 187 
HOH   O    H2   sing N N 188 
ILE   N    CA   sing N N 189 
ILE   N    H    sing N N 190 
ILE   N    H2   sing N N 191 
ILE   CA   C    sing N N 192 
ILE   CA   CB   sing N N 193 
ILE   CA   HA   sing N N 194 
ILE   C    O    doub N N 195 
ILE   C    OXT  sing N N 196 
ILE   CB   CG1  sing N N 197 
ILE   CB   CG2  sing N N 198 
ILE   CB   HB   sing N N 199 
ILE   CG1  CD1  sing N N 200 
ILE   CG1  HG12 sing N N 201 
ILE   CG1  HG13 sing N N 202 
ILE   CG2  HG21 sing N N 203 
ILE   CG2  HG22 sing N N 204 
ILE   CG2  HG23 sing N N 205 
ILE   CD1  HD11 sing N N 206 
ILE   CD1  HD12 sing N N 207 
ILE   CD1  HD13 sing N N 208 
ILE   OXT  HXT  sing N N 209 
IMN   C    C1   doub Y N 210 
IMN   C    C5   sing Y N 211 
IMN   C    N    sing Y N 212 
IMN   C1   C2   sing Y N 213 
IMN   C1   C7   sing Y N 214 
IMN   C2   C3   doub Y N 215 
IMN   C2   H2   sing N N 216 
IMN   C3   C4   sing Y N 217 
IMN   C3   O    sing N N 218 
IMN   C4   C5   doub Y N 219 
IMN   C4   H4   sing N N 220 
IMN   C5   H5   sing N N 221 
IMN   C6   O    sing N N 222 
IMN   C6   H61  sing N N 223 
IMN   C6   H62  sing N N 224 
IMN   C6   H63  sing N N 225 
IMN   C7   C8   doub Y N 226 
IMN   C7   C17  sing N N 227 
IMN   C8   C16  sing N N 228 
IMN   C8   N    sing Y N 229 
IMN   C9   C10  sing N N 230 
IMN   C9   N    sing N N 231 
IMN   C9   O1   doub N N 232 
IMN   C10  C11  doub Y N 233 
IMN   C10  C15  sing Y N 234 
IMN   C11  C12  sing Y N 235 
IMN   C11  H11  sing N N 236 
IMN   C12  C13  doub Y N 237 
IMN   C12  H12  sing N N 238 
IMN   C13  C14  sing Y N 239 
IMN   C13  CL   sing N N 240 
IMN   C14  C15  doub Y N 241 
IMN   C14  H14  sing N N 242 
IMN   C15  H15  sing N N 243 
IMN   C16  H161 sing N N 244 
IMN   C16  H162 sing N N 245 
IMN   C16  H163 sing N N 246 
IMN   C17  C18  sing N N 247 
IMN   C17  H171 sing N N 248 
IMN   C17  H172 sing N N 249 
IMN   C18  O2   doub N N 250 
IMN   C18  O3   sing N N 251 
IMN   O3   HO3  sing N N 252 
LEU   N    CA   sing N N 253 
LEU   N    H    sing N N 254 
LEU   N    H2   sing N N 255 
LEU   CA   C    sing N N 256 
LEU   CA   CB   sing N N 257 
LEU   CA   HA   sing N N 258 
LEU   C    O    doub N N 259 
LEU   C    OXT  sing N N 260 
LEU   CB   CG   sing N N 261 
LEU   CB   HB2  sing N N 262 
LEU   CB   HB3  sing N N 263 
LEU   CG   CD1  sing N N 264 
LEU   CG   CD2  sing N N 265 
LEU   CG   HG   sing N N 266 
LEU   CD1  HD11 sing N N 267 
LEU   CD1  HD12 sing N N 268 
LEU   CD1  HD13 sing N N 269 
LEU   CD2  HD21 sing N N 270 
LEU   CD2  HD22 sing N N 271 
LEU   CD2  HD23 sing N N 272 
LEU   OXT  HXT  sing N N 273 
LYS   N    CA   sing N N 274 
LYS   N    H    sing N N 275 
LYS   N    H2   sing N N 276 
LYS   CA   C    sing N N 277 
LYS   CA   CB   sing N N 278 
LYS   CA   HA   sing N N 279 
LYS   C    O    doub N N 280 
LYS   C    OXT  sing N N 281 
LYS   CB   CG   sing N N 282 
LYS   CB   HB2  sing N N 283 
LYS   CB   HB3  sing N N 284 
LYS   CG   CD   sing N N 285 
LYS   CG   HG2  sing N N 286 
LYS   CG   HG3  sing N N 287 
LYS   CD   CE   sing N N 288 
LYS   CD   HD2  sing N N 289 
LYS   CD   HD3  sing N N 290 
LYS   CE   NZ   sing N N 291 
LYS   CE   HE2  sing N N 292 
LYS   CE   HE3  sing N N 293 
LYS   NZ   HZ1  sing N N 294 
LYS   NZ   HZ2  sing N N 295 
LYS   NZ   HZ3  sing N N 296 
LYS   OXT  HXT  sing N N 297 
MET   N    CA   sing N N 298 
MET   N    H    sing N N 299 
MET   N    H2   sing N N 300 
MET   CA   C    sing N N 301 
MET   CA   CB   sing N N 302 
MET   CA   HA   sing N N 303 
MET   C    O    doub N N 304 
MET   C    OXT  sing N N 305 
MET   CB   CG   sing N N 306 
MET   CB   HB2  sing N N 307 
MET   CB   HB3  sing N N 308 
MET   CG   SD   sing N N 309 
MET   CG   HG2  sing N N 310 
MET   CG   HG3  sing N N 311 
MET   SD   CE   sing N N 312 
MET   CE   HE1  sing N N 313 
MET   CE   HE2  sing N N 314 
MET   CE   HE3  sing N N 315 
MET   OXT  HXT  sing N N 316 
PHE   N    CA   sing N N 317 
PHE   N    H    sing N N 318 
PHE   N    H2   sing N N 319 
PHE   CA   C    sing N N 320 
PHE   CA   CB   sing N N 321 
PHE   CA   HA   sing N N 322 
PHE   C    O    doub N N 323 
PHE   C    OXT  sing N N 324 
PHE   CB   CG   sing N N 325 
PHE   CB   HB2  sing N N 326 
PHE   CB   HB3  sing N N 327 
PHE   CG   CD1  doub Y N 328 
PHE   CG   CD2  sing Y N 329 
PHE   CD1  CE1  sing Y N 330 
PHE   CD1  HD1  sing N N 331 
PHE   CD2  CE2  doub Y N 332 
PHE   CD2  HD2  sing N N 333 
PHE   CE1  CZ   doub Y N 334 
PHE   CE1  HE1  sing N N 335 
PHE   CE2  CZ   sing Y N 336 
PHE   CE2  HE2  sing N N 337 
PHE   CZ   HZ   sing N N 338 
PHE   OXT  HXT  sing N N 339 
PLM   C1   O1   sing N N 340 
PLM   C1   O2   doub N N 341 
PLM   C1   C2   sing N N 342 
PLM   O1   H    sing N N 343 
PLM   C2   C3   sing N N 344 
PLM   C2   H21  sing N N 345 
PLM   C2   H22  sing N N 346 
PLM   C3   C4   sing N N 347 
PLM   C3   H31  sing N N 348 
PLM   C3   H32  sing N N 349 
PLM   C4   C5   sing N N 350 
PLM   C4   H41  sing N N 351 
PLM   C4   H42  sing N N 352 
PLM   C5   C6   sing N N 353 
PLM   C5   H51  sing N N 354 
PLM   C5   H52  sing N N 355 
PLM   C6   C7   sing N N 356 
PLM   C6   H61  sing N N 357 
PLM   C6   H62  sing N N 358 
PLM   C7   C8   sing N N 359 
PLM   C7   H71  sing N N 360 
PLM   C7   H72  sing N N 361 
PLM   C8   C9   sing N N 362 
PLM   C8   H81  sing N N 363 
PLM   C8   H82  sing N N 364 
PLM   C9   CA   sing N N 365 
PLM   C9   H91  sing N N 366 
PLM   C9   H92  sing N N 367 
PLM   CA   CB   sing N N 368 
PLM   CA   HA1  sing N N 369 
PLM   CA   HA2  sing N N 370 
PLM   CB   CC   sing N N 371 
PLM   CB   HB1  sing N N 372 
PLM   CB   HB2  sing N N 373 
PLM   CC   CD   sing N N 374 
PLM   CC   HC1  sing N N 375 
PLM   CC   HC2  sing N N 376 
PLM   CD   CE   sing N N 377 
PLM   CD   HD1  sing N N 378 
PLM   CD   HD2  sing N N 379 
PLM   CE   CF   sing N N 380 
PLM   CE   HE1  sing N N 381 
PLM   CE   HE2  sing N N 382 
PLM   CF   CG   sing N N 383 
PLM   CF   HF1  sing N N 384 
PLM   CF   HF2  sing N N 385 
PLM   CG   HG1  sing N N 386 
PLM   CG   HG2  sing N N 387 
PLM   CG   HG3  sing N N 388 
PRO   N    CA   sing N N 389 
PRO   N    CD   sing N N 390 
PRO   N    H    sing N N 391 
PRO   CA   C    sing N N 392 
PRO   CA   CB   sing N N 393 
PRO   CA   HA   sing N N 394 
PRO   C    O    doub N N 395 
PRO   C    OXT  sing N N 396 
PRO   CB   CG   sing N N 397 
PRO   CB   HB2  sing N N 398 
PRO   CB   HB3  sing N N 399 
PRO   CG   CD   sing N N 400 
PRO   CG   HG2  sing N N 401 
PRO   CG   HG3  sing N N 402 
PRO   CD   HD2  sing N N 403 
PRO   CD   HD3  sing N N 404 
PRO   OXT  HXT  sing N N 405 
SER   N    CA   sing N N 406 
SER   N    H    sing N N 407 
SER   N    H2   sing N N 408 
SER   CA   C    sing N N 409 
SER   CA   CB   sing N N 410 
SER   CA   HA   sing N N 411 
SER   C    O    doub N N 412 
SER   C    OXT  sing N N 413 
SER   CB   OG   sing N N 414 
SER   CB   HB2  sing N N 415 
SER   CB   HB3  sing N N 416 
SER   OG   HG   sing N N 417 
SER   OXT  HXT  sing N N 418 
THR   N    CA   sing N N 419 
THR   N    H    sing N N 420 
THR   N    H2   sing N N 421 
THR   CA   C    sing N N 422 
THR   CA   CB   sing N N 423 
THR   CA   HA   sing N N 424 
THR   C    O    doub N N 425 
THR   C    OXT  sing N N 426 
THR   CB   OG1  sing N N 427 
THR   CB   CG2  sing N N 428 
THR   CB   HB   sing N N 429 
THR   OG1  HG1  sing N N 430 
THR   CG2  HG21 sing N N 431 
THR   CG2  HG22 sing N N 432 
THR   CG2  HG23 sing N N 433 
THR   OXT  HXT  sing N N 434 
TRP   N    CA   sing N N 435 
TRP   N    H    sing N N 436 
TRP   N    H2   sing N N 437 
TRP   CA   C    sing N N 438 
TRP   CA   CB   sing N N 439 
TRP   CA   HA   sing N N 440 
TRP   C    O    doub N N 441 
TRP   C    OXT  sing N N 442 
TRP   CB   CG   sing N N 443 
TRP   CB   HB2  sing N N 444 
TRP   CB   HB3  sing N N 445 
TRP   CG   CD1  doub Y N 446 
TRP   CG   CD2  sing Y N 447 
TRP   CD1  NE1  sing Y N 448 
TRP   CD1  HD1  sing N N 449 
TRP   CD2  CE2  doub Y N 450 
TRP   CD2  CE3  sing Y N 451 
TRP   NE1  CE2  sing Y N 452 
TRP   NE1  HE1  sing N N 453 
TRP   CE2  CZ2  sing Y N 454 
TRP   CE3  CZ3  doub Y N 455 
TRP   CE3  HE3  sing N N 456 
TRP   CZ2  CH2  doub Y N 457 
TRP   CZ2  HZ2  sing N N 458 
TRP   CZ3  CH2  sing Y N 459 
TRP   CZ3  HZ3  sing N N 460 
TRP   CH2  HH2  sing N N 461 
TRP   OXT  HXT  sing N N 462 
TYR   N    CA   sing N N 463 
TYR   N    H    sing N N 464 
TYR   N    H2   sing N N 465 
TYR   CA   C    sing N N 466 
TYR   CA   CB   sing N N 467 
TYR   CA   HA   sing N N 468 
TYR   C    O    doub N N 469 
TYR   C    OXT  sing N N 470 
TYR   CB   CG   sing N N 471 
TYR   CB   HB2  sing N N 472 
TYR   CB   HB3  sing N N 473 
TYR   CG   CD1  doub Y N 474 
TYR   CG   CD2  sing Y N 475 
TYR   CD1  CE1  sing Y N 476 
TYR   CD1  HD1  sing N N 477 
TYR   CD2  CE2  doub Y N 478 
TYR   CD2  HD2  sing N N 479 
TYR   CE1  CZ   doub Y N 480 
TYR   CE1  HE1  sing N N 481 
TYR   CE2  CZ   sing Y N 482 
TYR   CE2  HE2  sing N N 483 
TYR   CZ   OH   sing N N 484 
TYR   OH   HH   sing N N 485 
TYR   OXT  HXT  sing N N 486 
VAL   N    CA   sing N N 487 
VAL   N    H    sing N N 488 
VAL   N    H2   sing N N 489 
VAL   CA   C    sing N N 490 
VAL   CA   CB   sing N N 491 
VAL   CA   HA   sing N N 492 
VAL   C    O    doub N N 493 
VAL   C    OXT  sing N N 494 
VAL   CB   CG1  sing N N 495 
VAL   CB   CG2  sing N N 496 
VAL   CB   HB   sing N N 497 
VAL   CG1  HG11 sing N N 498 
VAL   CG1  HG12 sing N N 499 
VAL   CG1  HG13 sing N N 500 
VAL   CG2  HG21 sing N N 501 
VAL   CG2  HG22 sing N N 502 
VAL   CG2  HG23 sing N N 503 
VAL   OXT  HXT  sing N N 504 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22077021 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1BJ5 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YG7 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.026078 
_atom_sites.fract_transf_matrix[1][2]   -0.004683 
_atom_sites.fract_transf_matrix[1][3]   0.000923 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010971 
_atom_sites.fract_transf_matrix[2][3]   -0.002958 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.010878 
_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  
CL 
CU 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . HIS   A 1 1   ? 5.780   -33.779 -9.078  1.00 50.96  ?  3   HIS   A N    1 
ATOM   2    C  CA   . HIS   A 1 1   ? 4.803   -33.734 -7.945  1.00 45.48  ?  3   HIS   A CA   1 
ATOM   3    C  C    . HIS   A 1 1   ? 3.910   -34.985 -8.016  1.00 42.69  ?  3   HIS   A C    1 
ATOM   4    O  O    . HIS   A 1 1   ? 2.695   -34.882 -8.173  1.00 50.39  ?  3   HIS   A O    1 
ATOM   5    C  CB   . HIS   A 1 1   ? 3.954   -32.437 -7.957  1.00 41.19  ?  3   HIS   A CB   1 
ATOM   6    C  CG   . HIS   A 1 1   ? 4.689   -31.216 -7.501  1.00 37.50  ?  3   HIS   A CG   1 
ATOM   7    N  N    . LYS   A 1 2   ? 4.516   -36.165 -7.920  1.00 41.37  ?  4   LYS   A N    1 
ATOM   8    C  CA   . LYS   A 1 2   ? 3.769   -37.349 -7.471  1.00 39.09  ?  4   LYS   A CA   1 
ATOM   9    C  C    . LYS   A 1 2   ? 3.159   -37.046 -6.098  1.00 37.03  ?  4   LYS   A C    1 
ATOM   10   O  O    . LYS   A 1 2   ? 2.011   -37.410 -5.836  1.00 38.98  ?  4   LYS   A O    1 
ATOM   11   C  CB   . LYS   A 1 2   ? 4.632   -38.601 -7.399  1.00 39.17  ?  4   LYS   A CB   1 
ATOM   12   N  N    . SER   A 1 3   ? 3.901   -36.336 -5.245  1.00 32.46  ?  5   SER   A N    1 
ATOM   13   C  CA   . SER   A 1 3   ? 3.379   -35.894 -3.933  1.00 26.18  ?  5   SER   A CA   1 
ATOM   14   C  C    . SER   A 1 3   ? 3.573   -34.398 -3.747  1.00 21.71  ?  5   SER   A C    1 
ATOM   15   O  O    . SER   A 1 3   ? 4.678   -33.962 -3.513  1.00 18.17  ?  5   SER   A O    1 
ATOM   16   C  CB   . SER   A 1 3   ? 4.108   -36.638 -2.848  1.00 24.48  ?  5   SER   A CB   1 
ATOM   17   O  OG   . SER   A 1 3   ? 3.859   -36.056 -1.589  1.00 25.61  ?  5   SER   A OG   1 
ATOM   18   N  N    . GLU   A 1 4   ? 2.511   -33.614 -3.826  1.00 21.99  ?  6   GLU   A N    1 
ATOM   19   C  CA   . GLU   A 1 4   ? 2.656   -32.128 -3.751  1.00 21.54  ?  6   GLU   A CA   1 
ATOM   20   C  C    . GLU   A 1 4   ? 3.162   -31.622 -2.388  1.00 23.28  ?  6   GLU   A C    1 
ATOM   21   O  O    . GLU   A 1 4   ? 3.913   -30.606 -2.352  1.00 23.95  ?  6   GLU   A O    1 
ATOM   22   C  CB   . GLU   A 1 4   ? 1.354   -31.404 -4.111  1.00 22.15  ?  6   GLU   A CB   1 
ATOM   23   N  N    . VAL   A 1 5   ? 2.801   -32.302 -1.282  1.00 21.97  ?  7   VAL   A N    1 
ATOM   24   C  CA   . VAL   A 1 5   ? 3.378   -31.944 0.038   1.00 21.94  ?  7   VAL   A CA   1 
ATOM   25   C  C    . VAL   A 1 5   ? 4.887   -32.141 0.050   1.00 21.53  ?  7   VAL   A C    1 
ATOM   26   O  O    . VAL   A 1 5   ? 5.588   -31.228 0.422   1.00 20.07  ?  7   VAL   A O    1 
ATOM   27   C  CB   . VAL   A 1 5   ? 2.821   -32.612 1.362   1.00 22.41  ?  7   VAL   A CB   1 
ATOM   28   C  CG1  . VAL   A 1 5   ? 1.471   -32.114 1.715   1.00 26.73  ?  7   VAL   A CG1  1 
ATOM   29   C  CG2  . VAL   A 1 5   ? 2.905   -34.121 1.418   1.00 22.63  ?  7   VAL   A CG2  1 
ATOM   30   N  N    . ALA   A 1 6   ? 5.374   -33.328 -0.316  1.00 23.26  ?  8   ALA   A N    1 
ATOM   31   C  CA   . ALA   A 1 6   ? 6.808   -33.574 -0.282  1.00 24.27  ?  8   ALA   A CA   1 
ATOM   32   C  C    . ALA   A 1 6   ? 7.545   -32.568 -1.127  1.00 23.77  ?  8   ALA   A C    1 
ATOM   33   O  O    . ALA   A 1 6   ? 8.573   -32.089 -0.718  1.00 22.46  ?  8   ALA   A O    1 
ATOM   34   C  CB   . ALA   A 1 6   ? 7.170   -34.985 -0.716  1.00 25.27  ?  8   ALA   A CB   1 
ATOM   35   N  N    . HIS   A 1 7   ? 7.041   -32.286 -2.320  1.00 26.60  ?  9   HIS   A N    1 
ATOM   36   C  CA   . HIS   A 1 7   ? 7.706   -31.342 -3.183  1.00 30.39  ?  9   HIS   A CA   1 
ATOM   37   C  C    . HIS   A 1 7   ? 7.785   -29.937 -2.541  1.00 29.15  ?  9   HIS   A C    1 
ATOM   38   O  O    . HIS   A 1 7   ? 8.870   -29.320 -2.547  1.00 28.52  ?  9   HIS   A O    1 
ATOM   39   C  CB   . HIS   A 1 7   ? 7.115   -31.340 -4.603  1.00 35.95  ?  9   HIS   A CB   1 
ATOM   40   C  CG   . HIS   A 1 7   ? 7.749   -30.327 -5.501  1.00 43.52  ?  9   HIS   A CG   1 
ATOM   41   N  ND1  . HIS   A 1 7   ? 7.017   -29.448 -6.271  1.00 50.60  ?  9   HIS   A ND1  1 
ATOM   42   C  CD2  . HIS   A 1 7   ? 9.048   -29.997 -5.687  1.00 49.69  ?  9   HIS   A CD2  1 
ATOM   43   C  CE1  . HIS   A 1 7   ? 7.838   -28.636 -6.914  1.00 53.71  ?  9   HIS   A CE1  1 
ATOM   44   N  NE2  . HIS   A 1 7   ? 9.078   -28.950 -6.578  1.00 53.16  ?  9   HIS   A NE2  1 
ATOM   45   N  N    . ARG   A 1 8   ? 6.677   -29.448 -1.978  1.00 26.84  ?  10  ARG   A N    1 
ATOM   46   C  CA   . ARG   A 1 8   ? 6.675   -28.131 -1.310  1.00 27.58  ?  10  ARG   A CA   1 
ATOM   47   C  C    . ARG   A 1 8   ? 7.590   -28.135 -0.085  1.00 22.78  ?  10  ARG   A C    1 
ATOM   48   O  O    . ARG   A 1 8   ? 8.303   -27.187 0.117   1.00 18.83  ?  10  ARG   A O    1 
ATOM   49   C  CB   . ARG   A 1 8   ? 5.248   -27.672 -0.935  1.00 31.38  ?  10  ARG   A CB   1 
ATOM   50   C  CG   . ARG   A 1 8   ? 4.400   -27.224 -2.135  1.00 39.81  ?  10  ARG   A CG   1 
ATOM   51   C  CD   . ARG   A 1 8   ? 4.133   -25.703 -2.209  1.00 47.40  ?  10  ARG   A CD   1 
ATOM   52   N  NE   . ARG   A 1 8   ? 4.190   -25.160 -3.581  1.00 49.42  ?  10  ARG   A NE   1 
ATOM   53   C  CZ   . ARG   A 1 8   ? 5.285   -24.645 -4.168  1.00 59.66  ?  10  ARG   A CZ   1 
ATOM   54   N  NH1  . ARG   A 1 8   ? 6.473   -24.575 -3.543  1.00 55.95  ?  10  ARG   A NH1  1 
ATOM   55   N  NH2  . ARG   A 1 8   ? 5.200   -24.195 -5.421  1.00 63.73  ?  10  ARG   A NH2  1 
ATOM   56   N  N    . PHE   A 1 9   ? 7.614   -29.230 0.690   1.00 20.42  ?  11  PHE   A N    1 
ATOM   57   C  CA   . PHE   A 1 9   ? 8.478   -29.327 1.869   1.00 19.81  ?  11  PHE   A CA   1 
ATOM   58   C  C    . PHE   A 1 9   ? 9.936   -29.231 1.466   1.00 21.15  ?  11  PHE   A C    1 
ATOM   59   O  O    . PHE   A 1 9   ? 10.744  -28.592 2.160   1.00 18.98  ?  11  PHE   A O    1 
ATOM   60   C  CB   . PHE   A 1 9   ? 8.245   -30.654 2.595   1.00 20.28  ?  11  PHE   A CB   1 
ATOM   61   C  CG   . PHE   A 1 9   ? 8.928   -30.757 3.927   1.00 20.59  ?  11  PHE   A CG   1 
ATOM   62   C  CD1  . PHE   A 1 9   ? 10.231  -31.205 4.024   1.00 21.12  ?  11  PHE   A CD1  1 
ATOM   63   C  CD2  . PHE   A 1 9   ? 8.268   -30.430 5.079   1.00 21.51  ?  11  PHE   A CD2  1 
ATOM   64   C  CE1  . PHE   A 1 9   ? 10.864  -31.364 5.266   1.00 20.80  ?  11  PHE   A CE1  1 
ATOM   65   C  CE2  . PHE   A 1 9   ? 8.891   -30.581 6.316   1.00 23.79  ?  11  PHE   A CE2  1 
ATOM   66   C  CZ   . PHE   A 1 9   ? 10.209  -31.044 6.414   1.00 21.79  ?  11  PHE   A CZ   1 
ATOM   67   N  N    . LYS   A 1 10  ? 10.277  -29.901 0.355   1.00 24.21  ?  12  LYS   A N    1 
ATOM   68   C  CA   . LYS   A 1 10  ? 11.647  -29.888 -0.180  1.00 27.40  ?  12  LYS   A CA   1 
ATOM   69   C  C    . LYS   A 1 10  ? 12.007  -28.500 -0.713  1.00 27.21  ?  12  LYS   A C    1 
ATOM   70   O  O    . LYS   A 1 10  ? 13.138  -28.054 -0.536  1.00 30.84  ?  12  LYS   A O    1 
ATOM   71   C  CB   . LYS   A 1 10  ? 11.824  -30.929 -1.299  1.00 29.54  ?  12  LYS   A CB   1 
ATOM   72   C  CG   . LYS   A 1 10  ? 11.860  -32.392 -0.840  1.00 32.10  ?  12  LYS   A CG   1 
ATOM   73   C  CD   . LYS   A 1 10  ? 12.005  -33.323 -2.033  1.00 33.14  ?  12  LYS   A CD   1 
ATOM   74   C  CE   . LYS   A 1 10  ? 12.010  -34.772 -1.591  1.00 39.71  ?  12  LYS   A CE   1 
ATOM   75   N  NZ   . LYS   A 1 10  ? 12.077  -35.715 -2.744  1.00 42.66  ?  12  LYS   A NZ   1 
ATOM   76   N  N    . ASP   A 1 11  ? 11.080  -27.861 -1.405  1.00 26.95  ?  13  ASP   A N    1 
ATOM   77   C  CA   . ASP   A 1 11  ? 11.310  -26.527 -1.964  1.00 29.46  ?  13  ASP   A CA   1 
ATOM   78   C  C    . ASP   A 1 11  ? 11.413  -25.455 -0.902  1.00 27.99  ?  13  ASP   A C    1 
ATOM   79   O  O    . ASP   A 1 11  ? 12.185  -24.539 -1.060  1.00 33.14  ?  13  ASP   A O    1 
ATOM   80   C  CB   . ASP   A 1 11  ? 10.220  -26.117 -2.984  1.00 33.06  ?  13  ASP   A CB   1 
ATOM   81   C  CG   . ASP   A 1 11  ? 10.378  -26.811 -4.391  1.00 37.71  ?  13  ASP   A CG   1 
ATOM   82   O  OD1  . ASP   A 1 11  ? 11.243  -27.707 -4.539  1.00 48.74  ?  13  ASP   A OD1  1 
ATOM   83   O  OD2  . ASP   A 1 11  ? 9.628   -26.467 -5.349  1.00 35.35  ?  13  ASP   A OD2  1 
ATOM   84   N  N    . LEU   A 1 12  ? 10.603  -25.547 0.150   1.00 26.20  ?  14  LEU   A N    1 
ATOM   85   C  CA   . LEU   A 1 12  ? 10.597  -24.560 1.232   1.00 24.74  ?  14  LEU   A CA   1 
ATOM   86   C  C    . LEU   A 1 12  ? 11.662  -24.786 2.253   1.00 22.99  ?  14  LEU   A C    1 
ATOM   87   O  O    . LEU   A 1 12  ? 12.245  -23.820 2.741   1.00 21.86  ?  14  LEU   A O    1 
ATOM   88   C  CB   . LEU   A 1 12  ? 9.228   -24.522 1.961   1.00 24.82  ?  14  LEU   A CB   1 
ATOM   89   C  CG   . LEU   A 1 12  ? 8.100   -23.596 1.450   1.00 25.62  ?  14  LEU   A CG   1 
ATOM   90   C  CD1  . LEU   A 1 12  ? 8.442   -22.882 0.163   1.00 28.17  ?  14  LEU   A CD1  1 
ATOM   91   C  CD2  . LEU   A 1 12  ? 6.725   -24.244 1.345   1.00 23.04  ?  14  LEU   A CD2  1 
ATOM   92   N  N    . GLY   A 1 13  ? 11.898  -26.044 2.624   1.00 20.09  ?  15  GLY   A N    1 
ATOM   93   C  CA   . GLY   A 1 13  ? 12.650  -26.309 3.843   1.00 19.69  ?  15  GLY   A CA   1 
ATOM   94   C  C    . GLY   A 1 13  ? 11.697  -26.324 5.046   1.00 20.07  ?  15  GLY   A C    1 
ATOM   95   O  O    . GLY   A 1 13  ? 10.659  -25.663 5.054   1.00 18.34  ?  15  GLY   A O    1 
ATOM   96   N  N    . GLU   A 1 14  ? 12.072  -27.075 6.070   1.00 20.82  ?  16  GLU   A N    1 
ATOM   97   C  CA   . GLU   A 1 14  ? 11.230  -27.296 7.229   1.00 22.72  ?  16  GLU   A CA   1 
ATOM   98   C  C    . GLU   A 1 14  ? 10.779  -26.059 7.972   1.00 21.44  ?  16  GLU   A C    1 
ATOM   99   O  O    . GLU   A 1 14  ? 9.599   -25.953 8.289   1.00 18.31  ?  16  GLU   A O    1 
ATOM   100  C  CB   . GLU   A 1 14  ? 11.932  -28.200 8.231   1.00 24.03  ?  16  GLU   A CB   1 
ATOM   101  C  CG   . GLU   A 1 14  ? 11.080  -28.568 9.412   1.00 26.18  ?  16  GLU   A CG   1 
ATOM   102  C  CD   . GLU   A 1 14  ? 11.660  -29.762 10.157  1.00 31.74  ?  16  GLU   A CD   1 
ATOM   103  O  OE1  . GLU   A 1 14  ? 12.742  -29.641 10.771  1.00 43.30  ?  16  GLU   A OE1  1 
ATOM   104  O  OE2  . GLU   A 1 14  ? 11.043  -30.831 10.132  1.00 35.50  ?  16  GLU   A OE2  1 
ATOM   105  N  N    . GLU   A 1 15  ? 11.710  -25.154 8.267   1.00 20.62  ?  17  GLU   A N    1 
ATOM   106  C  CA   . GLU   A 1 15  ? 11.376  -23.945 9.007   1.00 23.15  ?  17  GLU   A CA   1 
ATOM   107  C  C    . GLU   A 1 15  ? 10.382  -23.051 8.294   1.00 20.08  ?  17  GLU   A C    1 
ATOM   108  O  O    . GLU   A 1 15  ? 9.460   -22.587 8.914   1.00 17.70  ?  17  GLU   A O    1 
ATOM   109  C  CB   . GLU   A 1 15  ? 12.608  -23.095 9.368   1.00 26.03  ?  17  GLU   A CB   1 
ATOM   110  C  CG   . GLU   A 1 15  ? 13.654  -23.810 10.203  1.00 31.37  ?  17  GLU   A CG   1 
ATOM   111  C  CD   . GLU   A 1 15  ? 13.136  -24.301 11.546  1.00 37.35  ?  17  GLU   A CD   1 
ATOM   112  O  OE1  . GLU   A 1 15  ? 12.127  -23.738 12.053  1.00 42.25  ?  17  GLU   A OE1  1 
ATOM   113  O  OE2  . GLU   A 1 15  ? 13.759  -25.242 12.099  1.00 41.02  ?  17  GLU   A OE2  1 
ATOM   114  N  N    . ASN   A 1 16  ? 10.596  -22.783 7.008   1.00 19.99  ?  18  ASN   A N    1 
ATOM   115  C  CA   . ASN   A 1 16  ? 9.631   -22.001 6.203   1.00 17.93  ?  18  ASN   A CA   1 
ATOM   116  C  C    . ASN   A 1 16  ? 8.262   -22.718 6.061   1.00 15.67  ?  18  ASN   A C    1 
ATOM   117  O  O    . ASN   A 1 16  ? 7.247   -22.114 6.216   1.00 14.51  ?  18  ASN   A O    1 
ATOM   118  C  CB   . ASN   A 1 16  ? 10.231  -21.667 4.844   1.00 19.00  ?  18  ASN   A CB   1 
ATOM   119  C  CG   . ASN   A 1 16  ? 11.332  -20.610 4.950   1.00 21.85  ?  18  ASN   A CG   1 
ATOM   120  O  OD1  . ASN   A 1 16  ? 11.354  -19.818 5.905   1.00 22.11  ?  18  ASN   A OD1  1 
ATOM   121  N  ND2  . ASN   A 1 16  ? 12.265  -20.618 3.999   1.00 19.16  ?  18  ASN   A ND2  1 
ATOM   122  N  N    . PHE   A 1 17  ? 8.287   -24.019 5.782   1.00 15.43  ?  19  PHE   A N    1 
ATOM   123  C  CA   . PHE   A 1 17  ? 7.079   -24.848 5.655   1.00 14.29  ?  19  PHE   A CA   1 
ATOM   124  C  C    . PHE   A 1 17  ? 6.211   -24.700 6.878   1.00 14.29  ?  19  PHE   A C    1 
ATOM   125  O  O    . PHE   A 1 17  ? 5.027   -24.323 6.782   1.00 13.07  ?  19  PHE   A O    1 
ATOM   126  C  CB   . PHE   A 1 17  ? 7.478   -26.313 5.436   1.00 14.16  ?  19  PHE   A CB   1 
ATOM   127  C  CG   . PHE   A 1 17  ? 6.318   -27.240 5.215   1.00 14.39  ?  19  PHE   A CG   1 
ATOM   128  C  CD1  . PHE   A 1 17  ? 5.797   -27.403 3.950   1.00 14.65  ?  19  PHE   A CD1  1 
ATOM   129  C  CD2  . PHE   A 1 17  ? 5.744   -27.923 6.274   1.00 14.19  ?  19  PHE   A CD2  1 
ATOM   130  C  CE1  . PHE   A 1 17  ? 4.742   -28.261 3.716   1.00 14.86  ?  19  PHE   A CE1  1 
ATOM   131  C  CE2  . PHE   A 1 17  ? 4.689   -28.792 6.052   1.00 14.83  ?  19  PHE   A CE2  1 
ATOM   132  C  CZ   . PHE   A 1 17  ? 4.184   -28.953 4.774   1.00 15.16  ?  19  PHE   A CZ   1 
ATOM   133  N  N    . LYS   A 1 18  ? 6.811   -24.992 8.053   1.00 15.28  ?  20  LYS   A N    1 
ATOM   134  C  CA   . LYS   A 1 18  ? 6.118   -24.905 9.342   1.00 13.97  ?  20  LYS   A CA   1 
ATOM   135  C  C    . LYS   A 1 18  ? 5.527   -23.494 9.539   1.00 12.61  ?  20  LYS   A C    1 
ATOM   136  O  O    . LYS   A 1 18  ? 4.362   -23.372 9.875   1.00 11.55  ?  20  LYS   A O    1 
ATOM   137  C  CB   . LYS   A 1 18  ? 7.043   -25.216 10.511  1.00 16.28  ?  20  LYS   A CB   1 
ATOM   138  C  CG   . LYS   A 1 18  ? 7.549   -26.671 10.690  1.00 17.78  ?  20  LYS   A CG   1 
ATOM   139  C  CD   . LYS   A 1 18  ? 8.601   -26.714 11.836  1.00 20.46  ?  20  LYS   A CD   1 
ATOM   140  C  CE   . LYS   A 1 18  ? 8.183   -27.531 13.031  1.00 22.47  ?  20  LYS   A CE   1 
ATOM   141  N  NZ   . LYS   A 1 18  ? 8.692   -28.959 12.944  1.00 24.85  ?  20  LYS   A NZ   1 
ATOM   142  N  N    . ALA   A 1 19  ? 6.299   -22.439 9.328   1.00 10.54  ?  21  ALA   A N    1 
ATOM   143  C  CA   . ALA   A 1 19  ? 5.715   -21.096 9.393   1.00 11.09  ?  21  ALA   A CA   1 
ATOM   144  C  C    . ALA   A 1 19  ? 4.563   -20.821 8.476   1.00 11.89  ?  21  ALA   A C    1 
ATOM   145  O  O    . ALA   A 1 19  ? 3.643   -20.124 8.893   1.00 12.70  ?  21  ALA   A O    1 
ATOM   146  C  CB   . ALA   A 1 19  ? 6.735   -20.003 9.108   1.00 10.57  ?  21  ALA   A CB   1 
ATOM   147  N  N    . LEU   A 1 20  ? 4.681   -21.236 7.187   1.00 12.23  ?  22  LEU   A N    1 
ATOM   148  C  CA   . LEU   A 1 20  ? 3.662   -20.947 6.218   1.00 12.46  ?  22  LEU   A CA   1 
ATOM   149  C  C    . LEU   A 1 20  ? 2.398   -21.715 6.533   1.00 11.65  ?  22  LEU   A C    1 
ATOM   150  O  O    . LEU   A 1 20  ? 1.343   -21.179 6.413   1.00 10.24  ?  22  LEU   A O    1 
ATOM   151  C  CB   . LEU   A 1 20  ? 4.138   -21.280 4.790   1.00 13.12  ?  22  LEU   A CB   1 
ATOM   152  C  CG   . LEU   A 1 20  ? 5.238   -20.332 4.342   1.00 14.06  ?  22  LEU   A CG   1 
ATOM   153  C  CD1  . LEU   A 1 20  ? 5.927   -20.861 3.069   1.00 14.96  ?  22  LEU   A CD1  1 
ATOM   154  C  CD2  . LEU   A 1 20  ? 4.765   -18.889 4.210   1.00 15.77  ?  22  LEU   A CD2  1 
ATOM   155  N  N    . VAL   A 1 21  ? 2.535   -22.952 7.009   1.00 11.34  ?  23  VAL   A N    1 
ATOM   156  C  CA   . VAL   A 1 21  ? 1.386   -23.743 7.386   1.00 12.12  ?  23  VAL   A CA   1 
ATOM   157  C  C    . VAL   A 1 21  ? 0.709   -23.101 8.604   1.00 12.67  ?  23  VAL   A C    1 
ATOM   158  O  O    . VAL   A 1 21  ? -0.533  -23.042 8.660   1.00 12.29  ?  23  VAL   A O    1 
ATOM   159  C  CB   . VAL   A 1 21  ? 1.771   -25.214 7.694   1.00 12.32  ?  23  VAL   A CB   1 
ATOM   160  C  CG1  . VAL   A 1 21  ? 0.618   -25.965 8.329   1.00 12.62  ?  23  VAL   A CG1  1 
ATOM   161  C  CG2  . VAL   A 1 21  ? 2.189   -25.921 6.417   1.00 13.70  ?  23  VAL   A CG2  1 
ATOM   162  N  N    . LEU   A 1 22  ? 1.511   -22.600 9.559   1.00 13.51  ?  24  LEU   A N    1 
ATOM   163  C  CA   . LEU   A 1 22  ? 0.953   -21.892 10.707  1.00 14.85  ?  24  LEU   A CA   1 
ATOM   164  C  C    . LEU   A 1 22  ? 0.180   -20.659 10.253  1.00 14.66  ?  24  LEU   A C    1 
ATOM   165  O  O    . LEU   A 1 22  ? -0.973  -20.406 10.706  1.00 14.64  ?  24  LEU   A O    1 
ATOM   166  C  CB   . LEU   A 1 22  ? 2.019   -21.482 11.736  1.00 16.05  ?  24  LEU   A CB   1 
ATOM   167  C  CG   . LEU   A 1 22  ? 1.490   -20.589 12.882  1.00 16.93  ?  24  LEU   A CG   1 
ATOM   168  C  CD1  . LEU   A 1 22  ? 0.471   -21.330 13.742  1.00 17.62  ?  24  LEU   A CD1  1 
ATOM   169  C  CD2  . LEU   A 1 22  ? 2.630   -20.154 13.769  1.00 18.14  ?  24  LEU   A CD2  1 
ATOM   170  N  N    . ILE   A 1 23  ? 0.776   -19.901 9.351   1.00 15.32  ?  25  ILE   A N    1 
ATOM   171  C  CA   . ILE   A 1 23  ? 0.021   -18.710 8.825   1.00 16.80  ?  25  ILE   A CA   1 
ATOM   172  C  C    . ILE   A 1 23  ? -1.262  -19.140 8.074   1.00 18.68  ?  25  ILE   A C    1 
ATOM   173  O  O    . ILE   A 1 23  ? -2.304  -18.527 8.230   1.00 17.21  ?  25  ILE   A O    1 
ATOM   174  C  CB   . ILE   A 1 23  ? 0.879   -17.885 7.928   1.00 16.99  ?  25  ILE   A CB   1 
ATOM   175  C  CG1  . ILE   A 1 23  ? 2.074   -17.353 8.722   1.00 16.68  ?  25  ILE   A CG1  1 
ATOM   176  C  CG2  . ILE   A 1 23  ? 0.095   -16.739 7.309   1.00 18.38  ?  25  ILE   A CG2  1 
ATOM   177  C  CD1  . ILE   A 1 23  ? 3.264   -17.019 7.855   1.00 16.64  ?  25  ILE   A CD1  1 
ATOM   178  N  N    . ALA   A 1 24  ? -1.207  -20.210 7.297   1.00 20.19  ?  26  ALA   A N    1 
ATOM   179  C  CA   . ALA   A 1 24  ? -2.365  -20.551 6.454   1.00 22.03  ?  26  ALA   A CA   1 
ATOM   180  C  C    . ALA   A 1 24  ? -3.565  -20.959 7.295   1.00 21.23  ?  26  ALA   A C    1 
ATOM   181  O  O    . ALA   A 1 24  ? -4.674  -20.488 7.058   1.00 19.96  ?  26  ALA   A O    1 
ATOM   182  C  CB   . ALA   A 1 24  ? -2.046  -21.618 5.414   1.00 21.17  ?  26  ALA   A CB   1 
ATOM   183  N  N    . PHE   A 1 25  ? -3.337  -21.828 8.274   1.00 23.06  ?  27  PHE   A N    1 
ATOM   184  C  CA   . PHE   A 1 25  ? -4.364  -22.178 9.242   1.00 24.26  ?  27  PHE   A CA   1 
ATOM   185  C  C    . PHE   A 1 25  ? -4.795  -21.006 10.160  1.00 22.53  ?  27  PHE   A C    1 
ATOM   186  O  O    . PHE   A 1 25  ? -6.001  -20.860 10.501  1.00 18.33  ?  27  PHE   A O    1 
ATOM   187  C  CB   . PHE   A 1 25  ? -3.903  -23.384 10.094  1.00 27.07  ?  27  PHE   A CB   1 
ATOM   188  C  CG   . PHE   A 1 25  ? -3.943  -24.683 9.335   1.00 27.75  ?  27  PHE   A CG   1 
ATOM   189  C  CD1  . PHE   A 1 25  ? -5.144  -25.150 8.807   1.00 28.70  ?  27  PHE   A CD1  1 
ATOM   190  C  CD2  . PHE   A 1 25  ? -2.798  -25.410 9.118   1.00 29.35  ?  27  PHE   A CD2  1 
ATOM   191  C  CE1  . PHE   A 1 25  ? -5.192  -26.343 8.105   1.00 30.30  ?  27  PHE   A CE1  1 
ATOM   192  C  CE2  . PHE   A 1 25  ? -2.837  -26.597 8.422   1.00 32.21  ?  27  PHE   A CE2  1 
ATOM   193  C  CZ   . PHE   A 1 25  ? -4.026  -27.057 7.894   1.00 32.04  ?  27  PHE   A CZ   1 
ATOM   194  N  N    . ALA   A 1 26  ? -3.829  -20.193 10.583  1.00 19.31  ?  28  ALA   A N    1 
ATOM   195  C  CA   . ALA   A 1 26  ? -4.179  -18.986 11.322  1.00 18.92  ?  28  ALA   A CA   1 
ATOM   196  C  C    . ALA   A 1 26  ? -5.198  -18.120 10.569  1.00 18.73  ?  28  ALA   A C    1 
ATOM   197  O  O    . ALA   A 1 26  ? -6.101  -17.552 11.196  1.00 18.97  ?  28  ALA   A O    1 
ATOM   198  C  CB   . ALA   A 1 26  ? -2.939  -18.191 11.670  1.00 20.86  ?  28  ALA   A CB   1 
ATOM   199  N  N    . GLN   A 1 27  ? -5.132  -18.067 9.245   1.00 18.51  ?  29  GLN   A N    1 
ATOM   200  C  CA   . GLN   A 1 27  ? -6.007  -17.160 8.490   1.00 19.25  ?  29  GLN   A CA   1 
ATOM   201  C  C    . GLN   A 1 27  ? -7.447  -17.723 8.284   1.00 20.57  ?  29  GLN   A C    1 
ATOM   202  O  O    . GLN   A 1 27  ? -8.382  -16.964 8.053   1.00 17.35  ?  29  GLN   A O    1 
ATOM   203  C  CB   . GLN   A 1 27  ? -5.338  -16.782 7.193   1.00 19.99  ?  29  GLN   A CB   1 
ATOM   204  C  CG   . GLN   A 1 27  ? -4.059  -15.974 7.410   1.00 19.06  ?  29  GLN   A CG   1 
ATOM   205  C  CD   . GLN   A 1 27  ? -3.308  -15.636 6.141   1.00 20.46  ?  29  GLN   A CD   1 
ATOM   206  O  OE1  . GLN   A 1 27  ? -3.220  -16.442 5.206   1.00 16.34  ?  29  GLN   A OE1  1 
ATOM   207  N  NE2  . GLN   A 1 27  ? -2.699  -14.406 6.120   1.00 21.77  ?  29  GLN   A NE2  1 
ATOM   208  N  N    . TYR   A 1 28  ? -7.584  -19.045 8.422   1.00 21.46  ?  30  TYR   A N    1 
ATOM   209  C  CA   . TYR   A 1 28  ? -8.869  -19.769 8.329   1.00 23.43  ?  30  TYR   A CA   1 
ATOM   210  C  C    . TYR   A 1 28  ? -9.509  -20.116 9.666   1.00 25.11  ?  30  TYR   A C    1 
ATOM   211  O  O    . TYR   A 1 28  ? -10.736 -20.159 9.746   1.00 32.41  ?  30  TYR   A O    1 
ATOM   212  C  CB   . TYR   A 1 28  ? -8.697  -21.052 7.493   1.00 25.08  ?  30  TYR   A CB   1 
ATOM   213  C  CG   . TYR   A 1 28  ? -8.644  -20.740 6.026   1.00 26.24  ?  30  TYR   A CG   1 
ATOM   214  C  CD1  . TYR   A 1 28  ? -7.441  -20.353 5.404   1.00 28.34  ?  30  TYR   A CD1  1 
ATOM   215  C  CD2  . TYR   A 1 28  ? -9.790  -20.789 5.266   1.00 29.45  ?  30  TYR   A CD2  1 
ATOM   216  C  CE1  . TYR   A 1 28  ? -7.394  -20.026 4.057   1.00 31.99  ?  30  TYR   A CE1  1 
ATOM   217  C  CE2  . TYR   A 1 28  ? -9.772  -20.466 3.910   1.00 31.34  ?  30  TYR   A CE2  1 
ATOM   218  C  CZ   . TYR   A 1 28  ? -8.586  -20.082 3.300   1.00 34.32  ?  30  TYR   A CZ   1 
ATOM   219  O  OH   . TYR   A 1 28  ? -8.611  -19.745 1.942   1.00 36.26  ?  30  TYR   A OH   1 
ATOM   220  N  N    . LEU   A 1 29  ? -8.702  -20.407 10.695  1.00 22.61  ?  31  LEU   A N    1 
ATOM   221  C  CA   . LEU   A 1 29  ? -9.209  -20.751 12.011  1.00 21.42  ?  31  LEU   A CA   1 
ATOM   222  C  C    . LEU   A 1 29  ? -8.785  -19.663 12.924  1.00 21.26  ?  31  LEU   A C    1 
ATOM   223  O  O    . LEU   A 1 29  ? -7.991  -19.850 13.835  1.00 19.61  ?  31  LEU   A O    1 
ATOM   224  C  CB   . LEU   A 1 29  ? -8.708  -22.117 12.452  1.00 20.74  ?  31  LEU   A CB   1 
ATOM   225  C  CG   . LEU   A 1 29  ? -9.003  -23.259 11.489  1.00 20.17  ?  31  LEU   A CG   1 
ATOM   226  C  CD1  . LEU   A 1 29  ? -8.421  -24.527 12.049  1.00 21.27  ?  31  LEU   A CD1  1 
ATOM   227  C  CD2  . LEU   A 1 29  ? -10.483 -23.491 11.279  1.00 21.80  ?  31  LEU   A CD2  1 
ATOM   228  N  N    . GLN   A 1 30  ? -9.347  -18.486 12.675  1.00 24.44  ?  32  GLN   A N    1 
ATOM   229  C  CA   . GLN   A 1 30  ? -8.904  -17.257 13.352  1.00 25.35  ?  32  GLN   A CA   1 
ATOM   230  C  C    . GLN   A 1 30  ? -9.197  -17.219 14.877  1.00 30.31  ?  32  GLN   A C    1 
ATOM   231  O  O    . GLN   A 1 30  ? -8.578  -16.422 15.634  1.00 25.94  ?  32  GLN   A O    1 
ATOM   232  C  CB   . GLN   A 1 30  ? -9.536  -16.061 12.668  1.00 26.55  ?  32  GLN   A CB   1 
ATOM   233  C  CG   . GLN   A 1 30  ? -9.194  -15.945 11.193  1.00 24.96  ?  32  GLN   A CG   1 
ATOM   234  C  CD   . GLN   A 1 30  ? -10.047 -14.912 10.503  1.00 27.03  ?  32  GLN   A CD   1 
ATOM   235  O  OE1  . GLN   A 1 30  ? -9.899  -13.708 10.751  1.00 33.69  ?  32  GLN   A OE1  1 
ATOM   236  N  NE2  . GLN   A 1 30  ? -10.931 -15.358 9.622   1.00 24.06  ?  32  GLN   A NE2  1 
ATOM   237  N  N    . GLN   A 1 31  ? -10.122 -18.076 15.329  1.00 29.56  ?  33  GLN   A N    1 
ATOM   238  C  CA   . GLN   A 1 31  ? -10.554 -18.078 16.720  1.00 33.82  ?  33  GLN   A CA   1 
ATOM   239  C  C    . GLN   A 1 31  ? -9.893  -19.192 17.510  1.00 31.14  ?  33  GLN   A C    1 
ATOM   240  O  O    . GLN   A 1 31  ? -9.884  -19.124 18.725  1.00 30.66  ?  33  GLN   A O    1 
ATOM   241  C  CB   . GLN   A 1 31  ? -12.119 -18.123 16.846  1.00 34.15  ?  33  GLN   A CB   1 
ATOM   242  C  CG   . GLN   A 1 31  ? -12.855 -17.034 16.035  1.00 36.96  ?  33  GLN   A CG   1 
ATOM   243  C  CD   . GLN   A 1 31  ? -12.370 -15.593 16.308  1.00 41.82  ?  33  GLN   A CD   1 
ATOM   244  O  OE1  . GLN   A 1 31  ? -11.982 -15.264 17.432  1.00 48.90  ?  33  GLN   A OE1  1 
ATOM   245  N  NE2  . GLN   A 1 31  ? -12.406 -14.724 15.282  1.00 42.70  ?  33  GLN   A NE2  1 
ATOM   246  N  N    . CYS   A 1 32  ? -9.314  -20.198 16.848  1.00 31.99  ?  34  CYS   A N    1 
ATOM   247  C  CA   . CYS   A 1 32  ? -8.701  -21.294 17.590  1.00 32.57  ?  34  CYS   A CA   1 
ATOM   248  C  C    . CYS   A 1 32  ? -7.396  -20.816 18.197  1.00 31.41  ?  34  CYS   A C    1 
ATOM   249  O  O    . CYS   A 1 32  ? -6.689  -20.039 17.578  1.00 29.84  ?  34  CYS   A O    1 
ATOM   250  C  CB   . CYS   A 1 32  ? -8.473  -22.535 16.730  1.00 36.07  ?  34  CYS   A CB   1 
ATOM   251  S  SG   . CYS   A 1 32  ? -10.039 -23.223 16.134  1.00 44.64  ?  34  CYS   A SG   1 
ATOM   252  N  N    . PRO   A 1 33  ? -7.094  -21.266 19.423  1.00 28.93  ?  35  PRO   A N    1 
ATOM   253  C  CA   . PRO   A 1 33  ? -5.933  -20.737 20.103  1.00 28.74  ?  35  PRO   A CA   1 
ATOM   254  C  C    . PRO   A 1 33  ? -4.593  -21.271 19.515  1.00 27.50  ?  35  PRO   A C    1 
ATOM   255  O  O    . PRO   A 1 33  ? -4.561  -22.269 18.753  1.00 24.28  ?  35  PRO   A O    1 
ATOM   256  C  CB   . PRO   A 1 33  ? -6.158  -21.141 21.568  1.00 27.30  ?  35  PRO   A CB   1 
ATOM   257  C  CG   . PRO   A 1 33  ? -7.069  -22.327 21.520  1.00 26.91  ?  35  PRO   A CG   1 
ATOM   258  C  CD   . PRO   A 1 33  ? -7.810  -22.287 20.218  1.00 27.02  ?  35  PRO   A CD   1 
ATOM   259  N  N    . PHE   A 1 34  ? -3.529  -20.534 19.835  1.00 25.28  ?  36  PHE   A N    1 
ATOM   260  C  CA   . PHE   A 1 34  ? -2.175  -20.855 19.438  1.00 26.53  ?  36  PHE   A CA   1 
ATOM   261  C  C    . PHE   A 1 34  ? -1.848  -22.333 19.624  1.00 26.66  ?  36  PHE   A C    1 
ATOM   262  O  O    . PHE   A 1 34  ? -1.437  -22.980 18.707  1.00 27.25  ?  36  PHE   A O    1 
ATOM   263  C  CB   . PHE   A 1 34  ? -1.166  -20.018 20.234  1.00 26.78  ?  36  PHE   A CB   1 
ATOM   264  C  CG   . PHE   A 1 34  ? 0.265   -20.247 19.828  1.00 29.22  ?  36  PHE   A CG   1 
ATOM   265  C  CD1  . PHE   A 1 34  ? 0.715   -19.882 18.546  1.00 30.28  ?  36  PHE   A CD1  1 
ATOM   266  C  CD2  . PHE   A 1 34  ? 1.165   -20.851 20.704  1.00 31.27  ?  36  PHE   A CD2  1 
ATOM   267  C  CE1  . PHE   A 1 34  ? 2.039   -20.107 18.162  1.00 31.06  ?  36  PHE   A CE1  1 
ATOM   268  C  CE2  . PHE   A 1 34  ? 2.479   -21.086 20.322  1.00 31.03  ?  36  PHE   A CE2  1 
ATOM   269  C  CZ   . PHE   A 1 34  ? 2.918   -20.706 19.048  1.00 31.92  ?  36  PHE   A CZ   1 
ATOM   270  N  N    . GLU   A 1 35  ? -2.054  -22.867 20.810  1.00 29.11  ?  37  GLU   A N    1 
ATOM   271  C  CA   . GLU   A 1 35  ? -1.654  -24.254 21.085  1.00 33.10  ?  37  GLU   A CA   1 
ATOM   272  C  C    . GLU   A 1 35  ? -2.333  -25.255 20.139  1.00 32.11  ?  37  GLU   A C    1 
ATOM   273  O  O    . GLU   A 1 35  ? -1.715  -26.230 19.802  1.00 31.35  ?  37  GLU   A O    1 
ATOM   274  C  CB   . GLU   A 1 35  ? -1.881  -24.655 22.545  1.00 33.97  ?  37  GLU   A CB   1 
ATOM   275  C  CG   . GLU   A 1 35  ? -1.085  -23.799 23.520  1.00 37.69  ?  37  GLU   A CG   1 
ATOM   276  C  CD   . GLU   A 1 35  ? -1.526  -22.330 23.537  1.00 41.06  ?  37  GLU   A CD   1 
ATOM   277  O  OE1  . GLU   A 1 35  ? -2.731  -22.037 23.293  1.00 46.07  ?  37  GLU   A OE1  1 
ATOM   278  O  OE2  . GLU   A 1 35  ? -0.683  -21.450 23.783  1.00 40.41  ?  37  GLU   A OE2  1 
ATOM   279  N  N    . ASP   A 1 36  ? -3.574  -24.996 19.693  1.00 33.55  ?  38  ASP   A N    1 
ATOM   280  C  CA   . ASP   A 1 36  ? -4.254  -25.892 18.735  1.00 33.46  ?  38  ASP   A CA   1 
ATOM   281  C  C    . ASP   A 1 36  ? -3.602  -25.809 17.349  1.00 30.79  ?  38  ASP   A C    1 
ATOM   282  O  O    . ASP   A 1 36  ? -3.411  -26.814 16.708  1.00 29.74  ?  38  ASP   A O    1 
ATOM   283  C  CB   . ASP   A 1 36  ? -5.755  -25.589 18.635  1.00 36.79  ?  38  ASP   A CB   1 
ATOM   284  C  CG   . ASP   A 1 36  ? -6.511  -25.872 19.954  1.00 40.70  ?  38  ASP   A CG   1 
ATOM   285  O  OD1  . ASP   A 1 36  ? -5.900  -26.445 20.890  1.00 40.21  ?  38  ASP   A OD1  1 
ATOM   286  O  OD2  . ASP   A 1 36  ? -7.718  -25.517 20.056  1.00 41.73  ?  38  ASP   A OD2  1 
ATOM   287  N  N    . HIS   A 1 37  ? -3.243  -24.603 16.915  1.00 29.69  ?  39  HIS   A N    1 
ATOM   288  C  CA   . HIS   A 1 37  ? -2.449  -24.403 15.698  1.00 28.33  ?  39  HIS   A CA   1 
ATOM   289  C  C    . HIS   A 1 37  ? -1.059  -25.057 15.745  1.00 29.74  ?  39  HIS   A C    1 
ATOM   290  O  O    . HIS   A 1 37  ? -0.636  -25.643 14.748  1.00 28.60  ?  39  HIS   A O    1 
ATOM   291  C  CB   . HIS   A 1 37  ? -2.280  -22.908 15.413  1.00 26.92  ?  39  HIS   A CB   1 
ATOM   292  C  CG   . HIS   A 1 37  ? -3.540  -22.276 14.975  1.00 30.29  ?  39  HIS   A CG   1 
ATOM   293  N  ND1  . HIS   A 1 37  ? -4.040  -21.130 15.546  1.00 36.79  ?  39  HIS   A ND1  1 
ATOM   294  C  CD2  . HIS   A 1 37  ? -4.459  -22.688 14.078  1.00 31.63  ?  39  HIS   A CD2  1 
ATOM   295  C  CE1  . HIS   A 1 37  ? -5.188  -20.828 14.967  1.00 33.18  ?  39  HIS   A CE1  1 
ATOM   296  N  NE2  . HIS   A 1 37  ? -5.477  -21.772 14.098  1.00 32.23  ?  39  HIS   A NE2  1 
ATOM   297  N  N    . VAL   A 1 38  ? -0.338  -24.900 16.872  1.00 28.56  ?  40  VAL   A N    1 
ATOM   298  C  CA   . VAL   A 1 38  ? 0.946   -25.575 17.066  1.00 27.54  ?  40  VAL   A CA   1 
ATOM   299  C  C    . VAL   A 1 38  ? 0.702   -27.058 16.827  1.00 28.30  ?  40  VAL   A C    1 
ATOM   300  O  O    . VAL   A 1 38  ? 1.473   -27.688 16.091  1.00 25.49  ?  40  VAL   A O    1 
ATOM   301  C  CB   . VAL   A 1 38  ? 1.591   -25.310 18.447  1.00 26.91  ?  40  VAL   A CB   1 
ATOM   302  C  CG1  . VAL   A 1 38  ? 2.689   -26.328 18.779  1.00 27.63  ?  40  VAL   A CG1  1 
ATOM   303  C  CG2  . VAL   A 1 38  ? 2.197   -23.916 18.478  1.00 26.58  ?  40  VAL   A CG2  1 
ATOM   304  N  N    . LYS   A 1 39  ? -0.383  -27.600 17.386  1.00 28.52  ?  41  LYS   A N    1 
ATOM   305  C  CA   . LYS   A 1 39  ? -0.703  -29.026 17.158  1.00 29.71  ?  41  LYS   A CA   1 
ATOM   306  C  C    . LYS   A 1 39  ? -1.023  -29.367 15.675  1.00 28.23  ?  41  LYS   A C    1 
ATOM   307  O  O    . LYS   A 1 39  ? -0.692  -30.478 15.226  1.00 25.24  ?  41  LYS   A O    1 
ATOM   308  C  CB   . LYS   A 1 39  ? -1.861  -29.502 18.041  1.00 27.65  ?  41  LYS   A CB   1 
ATOM   309  N  N    . LEU   A 1 40  ? -1.697  -28.472 14.941  1.00 26.38  ?  42  LEU   A N    1 
ATOM   310  C  CA   . LEU   A 1 40  ? -1.993  -28.748 13.519  1.00 27.21  ?  42  LEU   A CA   1 
ATOM   311  C  C    . LEU   A 1 40  ? -0.709  -28.733 12.711  1.00 23.28  ?  42  LEU   A C    1 
ATOM   312  O  O    . LEU   A 1 40  ? -0.447  -29.624 11.935  1.00 24.62  ?  42  LEU   A O    1 
ATOM   313  C  CB   . LEU   A 1 40  ? -3.002  -27.764 12.896  1.00 29.95  ?  42  LEU   A CB   1 
ATOM   314  C  CG   . LEU   A 1 40  ? -4.461  -27.782 13.404  1.00 33.41  ?  42  LEU   A CG   1 
ATOM   315  C  CD1  . LEU   A 1 40  ? -5.305  -26.954 12.462  1.00 35.43  ?  42  LEU   A CD1  1 
ATOM   316  C  CD2  . LEU   A 1 40  ? -5.081  -29.175 13.565  1.00 34.32  ?  42  LEU   A CD2  1 
ATOM   317  N  N    . VAL   A 1 41  ? 0.064   -27.693 12.887  1.00 20.02  ?  43  VAL   A N    1 
ATOM   318  C  CA   . VAL   A 1 41  ? 1.330   -27.594 12.233  1.00 19.71  ?  43  VAL   A CA   1 
ATOM   319  C  C    . VAL   A 1 41  ? 2.236   -28.826 12.466  1.00 19.40  ?  43  VAL   A C    1 
ATOM   320  O  O    . VAL   A 1 41  ? 2.845   -29.323 11.530  1.00 20.09  ?  43  VAL   A O    1 
ATOM   321  C  CB   . VAL   A 1 41  ? 2.054   -26.321 12.662  1.00 18.42  ?  43  VAL   A CB   1 
ATOM   322  C  CG1  . VAL   A 1 41  ? 3.517   -26.388 12.316  1.00 18.43  ?  43  VAL   A CG1  1 
ATOM   323  C  CG2  . VAL   A 1 41  ? 1.380   -25.069 12.045  1.00 19.27  ?  43  VAL   A CG2  1 
ATOM   324  N  N    . ASN   A 1 42  ? 2.378   -29.282 13.686  1.00 19.74  ?  44  ASN   A N    1 
ATOM   325  C  CA   . ASN   A 1 42  ? 3.253   -30.429 13.960  1.00 21.43  ?  44  ASN   A CA   1 
ATOM   326  C  C    . ASN   A 1 42  ? 2.698   -31.651 13.240  1.00 20.22  ?  44  ASN   A C    1 
ATOM   327  O  O    . ASN   A 1 42  ? 3.439   -32.344 12.603  1.00 20.04  ?  44  ASN   A O    1 
ATOM   328  C  CB   . ASN   A 1 42  ? 3.413   -30.684 15.469  1.00 21.87  ?  44  ASN   A CB   1 
ATOM   329  C  CG   . ASN   A 1 42  ? 4.154   -29.581 16.162  1.00 22.12  ?  44  ASN   A CG   1 
ATOM   330  O  OD1  . ASN   A 1 42  ? 4.977   -28.914 15.560  1.00 23.78  ?  44  ASN   A OD1  1 
ATOM   331  N  ND2  . ASN   A 1 42  ? 3.866   -29.369 17.446  1.00 23.91  ?  44  ASN   A ND2  1 
ATOM   332  N  N    . GLU   A 1 43  ? 1.390   -31.828 13.221  1.00 21.36  ?  45  GLU   A N    1 
ATOM   333  C  CA   . GLU   A 1 43  ? 0.793   -32.992 12.536  1.00 23.38  ?  45  GLU   A CA   1 
ATOM   334  C  C    . GLU   A 1 43  ? 0.954   -32.910 11.013  1.00 21.10  ?  45  GLU   A C    1 
ATOM   335  O  O    . GLU   A 1 43  ? 1.193   -33.917 10.351  1.00 17.59  ?  45  GLU   A O    1 
ATOM   336  C  CB   . GLU   A 1 43  ? -0.699  -33.082 12.794  1.00 25.55  ?  45  GLU   A CB   1 
ATOM   337  C  CG   . GLU   A 1 43  ? -1.168  -33.605 14.115  1.00 29.98  ?  45  GLU   A CG   1 
ATOM   338  C  CD   . GLU   A 1 43  ? -2.692  -33.683 14.108  1.00 33.50  ?  45  GLU   A CD   1 
ATOM   339  O  OE1  . GLU   A 1 43  ? -3.345  -32.650 13.828  1.00 32.98  ?  45  GLU   A OE1  1 
ATOM   340  O  OE2  . GLU   A 1 43  ? -3.240  -34.790 14.334  1.00 41.35  ?  45  GLU   A OE2  1 
ATOM   341  N  N    . VAL   A 1 44  ? 0.752   -31.728 10.436  1.00 19.34  ?  46  VAL   A N    1 
ATOM   342  C  CA   . VAL   A 1 44  ? 0.922   -31.609 8.996   1.00 19.59  ?  46  VAL   A CA   1 
ATOM   343  C  C    . VAL   A 1 44  ? 2.402   -31.806 8.652   1.00 19.23  ?  46  VAL   A C    1 
ATOM   344  O  O    . VAL   A 1 44  ? 2.718   -32.383 7.636   1.00 16.97  ?  46  VAL   A O    1 
ATOM   345  C  CB   . VAL   A 1 44  ? 0.433   -30.249 8.460   1.00 21.27  ?  46  VAL   A CB   1 
ATOM   346  C  CG1  . VAL   A 1 44  ? 1.068   -29.937 7.126   1.00 21.26  ?  46  VAL   A CG1  1 
ATOM   347  C  CG2  . VAL   A 1 44  ? -1.079  -30.263 8.321   1.00 21.97  ?  46  VAL   A CG2  1 
ATOM   348  N  N    . THR   A 1 45  ? 3.292   -31.304 9.500   1.00 19.89  ?  47  THR   A N    1 
ATOM   349  C  CA   . THR   A 1 45  ? 4.721   -31.433 9.286   1.00 21.23  ?  47  THR   A CA   1 
ATOM   350  C  C    . THR   A 1 45  ? 5.202   -32.888 9.478   1.00 21.52  ?  47  THR   A C    1 
ATOM   351  O  O    . THR   A 1 45  ? 6.044   -33.352 8.716   1.00 22.98  ?  47  THR   A O    1 
ATOM   352  C  CB   . THR   A 1 45  ? 5.463   -30.485 10.217  1.00 24.50  ?  47  THR   A CB   1 
ATOM   353  O  OG1  . THR   A 1 45  ? 4.969   -29.141 10.017  1.00 22.05  ?  47  THR   A OG1  1 
ATOM   354  C  CG2  . THR   A 1 45  ? 6.972   -30.537 9.958   1.00 25.33  ?  47  THR   A CG2  1 
ATOM   355  N  N    . GLU   A 1 46  ? 4.702   -33.607 10.477  1.00 21.40  ?  48  GLU   A N    1 
ATOM   356  C  CA   . GLU   A 1 46  ? 5.057   -35.043 10.586  1.00 22.91  ?  48  GLU   A CA   1 
ATOM   357  C  C    . GLU   A 1 46  ? 4.632   -35.688 9.287   1.00 22.31  ?  48  GLU   A C    1 
ATOM   358  O  O    . GLU   A 1 46  ? 5.349   -36.494 8.754   1.00 22.17  ?  48  GLU   A O    1 
ATOM   359  C  CB   . GLU   A 1 46  ? 4.354   -35.792 11.727  1.00 21.33  ?  48  GLU   A CB   1 
ATOM   360  N  N    . PHE   A 1 47  ? 3.448   -35.326 8.800   1.00 21.31  ?  49  PHE   A N    1 
ATOM   361  C  CA   . PHE   A 1 47  ? 2.888   -35.983 7.643   1.00 20.96  ?  49  PHE   A CA   1 
ATOM   362  C  C    . PHE   A 1 47  ? 3.751   -35.736 6.423   1.00 20.52  ?  49  PHE   A C    1 
ATOM   363  O  O    . PHE   A 1 47  ? 4.101   -36.674 5.722   1.00 19.65  ?  49  PHE   A O    1 
ATOM   364  C  CB   . PHE   A 1 47  ? 1.432   -35.548 7.390   1.00 21.72  ?  49  PHE   A CB   1 
ATOM   365  C  CG   . PHE   A 1 47  ? 0.891   -36.052 6.092   1.00 22.01  ?  49  PHE   A CG   1 
ATOM   366  C  CD1  . PHE   A 1 47  ? 0.717   -37.440 5.884   1.00 21.91  ?  49  PHE   A CD1  1 
ATOM   367  C  CD2  . PHE   A 1 47  ? 0.602   -35.166 5.058   1.00 22.01  ?  49  PHE   A CD2  1 
ATOM   368  C  CE1  . PHE   A 1 47  ? 0.266   -37.924 4.655   1.00 21.87  ?  49  PHE   A CE1  1 
ATOM   369  C  CE2  . PHE   A 1 47  ? 0.146   -35.657 3.839   1.00 23.88  ?  49  PHE   A CE2  1 
ATOM   370  C  CZ   . PHE   A 1 47  ? -0.029  -37.047 3.644   1.00 21.31  ?  49  PHE   A CZ   1 
ATOM   371  N  N    . ALA   A 1 48  ? 4.085   -34.462 6.179   1.00 18.02  ?  50  ALA   A N    1 
ATOM   372  C  CA   . ALA   A 1 48  ? 4.958   -34.079 5.110   1.00 18.16  ?  50  ALA   A CA   1 
ATOM   373  C  C    . ALA   A 1 48  ? 6.286   -34.896 5.048   1.00 17.96  ?  50  ALA   A C    1 
ATOM   374  O  O    . ALA   A 1 48  ? 6.712   -35.336 3.957   1.00 16.03  ?  50  ALA   A O    1 
ATOM   375  C  CB   . ALA   A 1 48  ? 5.275   -32.575 5.202   1.00 17.55  ?  50  ALA   A CB   1 
ATOM   376  N  N    . LYS   A 1 49  ? 6.932   -35.017 6.191   1.00 17.89  ?  51  LYS   A N    1 
ATOM   377  C  CA   . LYS   A 1 49  ? 8.136   -35.816 6.351   1.00 21.32  ?  51  LYS   A CA   1 
ATOM   378  C  C    . LYS   A 1 49  ? 7.995   -37.243 5.892   1.00 20.17  ?  51  LYS   A C    1 
ATOM   379  O  O    . LYS   A 1 49  ? 8.919   -37.817 5.386   1.00 19.61  ?  51  LYS   A O    1 
ATOM   380  C  CB   . LYS   A 1 49  ? 8.523   -35.918 7.832   1.00 23.33  ?  51  LYS   A CB   1 
ATOM   381  C  CG   . LYS   A 1 49  ? 9.350   -34.738 8.308   1.00 27.33  ?  51  LYS   A CG   1 
ATOM   382  C  CD   . LYS   A 1 49  ? 10.314  -35.174 9.410   1.00 29.38  ?  51  LYS   A CD   1 
ATOM   383  C  CE   . LYS   A 1 49  ? 11.190  -33.982 9.742   1.00 30.30  ?  51  LYS   A CE   1 
ATOM   384  N  NZ   . LYS   A 1 49  ? 10.387  -32.886 10.310  1.00 29.88  ?  51  LYS   A NZ   1 
ATOM   385  N  N    . THR   A 1 50  ? 6.828   -37.798 6.114   1.00 19.85  ?  52  THR   A N    1 
ATOM   386  C  CA   . THR   A 1 50  ? 6.554   -39.169 5.750   1.00 21.87  ?  52  THR   A CA   1 
ATOM   387  C  C    . THR   A 1 50  ? 6.596   -39.246 4.198   1.00 22.18  ?  52  THR   A C    1 
ATOM   388  O  O    . THR   A 1 50  ? 7.051   -40.241 3.597   1.00 20.91  ?  52  THR   A O    1 
ATOM   389  C  CB   . THR   A 1 50  ? 5.189   -39.541 6.398   1.00 24.02  ?  52  THR   A CB   1 
ATOM   390  O  OG1  . THR   A 1 50  ? 5.320   -40.777 7.097   1.00 31.27  ?  52  THR   A OG1  1 
ATOM   391  C  CG2  . THR   A 1 50  ? 4.007   -39.581 5.390   1.00 23.06  ?  52  THR   A CG2  1 
ATOM   392  N  N    . CYS   A 1 51  ? 6.134   -38.166 3.556   1.00 20.89  ?  53  CYS   A N    1 
ATOM   393  C  CA   . CYS   A 1 51  ? 6.031   -38.103 2.101   1.00 22.21  ?  53  CYS   A CA   1 
ATOM   394  C  C    . CYS   A 1 51  ? 7.396   -37.828 1.490   1.00 21.13  ?  53  CYS   A C    1 
ATOM   395  O  O    . CYS   A 1 51  ? 7.660   -38.317 0.417   1.00 20.61  ?  53  CYS   A O    1 
ATOM   396  C  CB   . CYS   A 1 51  ? 5.024   -37.044 1.649   1.00 22.58  ?  53  CYS   A CB   1 
ATOM   397  S  SG   . CYS   A 1 51  ? 3.366   -37.287 2.261   1.00 25.63  ?  53  CYS   A SG   1 
ATOM   398  N  N    . VAL   A 1 52  ? 8.220   -37.019 2.171   1.00 20.77  ?  54  VAL   A N    1 
ATOM   399  C  CA   . VAL   A 1 52  ? 9.581   -36.761 1.751   1.00 22.32  ?  54  VAL   A CA   1 
ATOM   400  C  C    . VAL   A 1 52  ? 10.366  -38.064 1.780   1.00 24.17  ?  54  VAL   A C    1 
ATOM   401  O  O    . VAL   A 1 52  ? 11.066  -38.356 0.824   1.00 24.62  ?  54  VAL   A O    1 
ATOM   402  C  CB   . VAL   A 1 52  ? 10.299  -35.700 2.614   1.00 21.47  ?  54  VAL   A CB   1 
ATOM   403  C  CG1  . VAL   A 1 52  ? 11.808  -35.677 2.360   1.00 21.20  ?  54  VAL   A CG1  1 
ATOM   404  C  CG2  . VAL   A 1 52  ? 9.736   -34.308 2.352   1.00 21.39  ?  54  VAL   A CG2  1 
ATOM   405  N  N    . ALA   A 1 53  ? 10.224  -38.837 2.847   1.00 24.41  ?  55  ALA   A N    1 
ATOM   406  C  CA   . ALA   A 1 53  ? 10.844  -40.174 2.902   1.00 28.49  ?  55  ALA   A CA   1 
ATOM   407  C  C    . ALA   A 1 53  ? 10.292  -41.133 1.839   1.00 29.36  ?  55  ALA   A C    1 
ATOM   408  O  O    . ALA   A 1 53  ? 11.031  -41.954 1.333   1.00 29.47  ?  55  ALA   A O    1 
ATOM   409  C  CB   . ALA   A 1 53  ? 10.678  -40.808 4.282   1.00 28.30  ?  55  ALA   A CB   1 
ATOM   410  N  N    . ASP   A 1 54  ? 9.003   -41.029 1.503   1.00 31.39  ?  56  ASP   A N    1 
ATOM   411  C  CA   . ASP   A 1 54  ? 8.374   -41.998 0.596   1.00 29.70  ?  56  ASP   A CA   1 
ATOM   412  C  C    . ASP   A 1 54  ? 7.192   -41.356 -0.112  1.00 32.21  ?  56  ASP   A C    1 
ATOM   413  O  O    . ASP   A 1 54  ? 6.094   -41.240 0.463   1.00 28.79  ?  56  ASP   A O    1 
ATOM   414  C  CB   . ASP   A 1 54  ? 7.953   -43.210 1.427   1.00 30.10  ?  56  ASP   A CB   1 
ATOM   415  C  CG   . ASP   A 1 54  ? 7.652   -44.442 0.608   1.00 32.73  ?  56  ASP   A CG   1 
ATOM   416  O  OD1  . ASP   A 1 54  ? 7.530   -44.387 -0.657  1.00 33.27  ?  56  ASP   A OD1  1 
ATOM   417  O  OD2  . ASP   A 1 54  ? 7.526   -45.501 1.286   1.00 35.88  ?  56  ASP   A OD2  1 
ATOM   418  N  N    . GLU   A 1 55  ? 7.403   -40.941 -1.371  1.00 35.66  ?  57  GLU   A N    1 
ATOM   419  C  CA   . GLU   A 1 55  ? 6.363   -40.221 -2.138  1.00 37.07  ?  57  GLU   A CA   1 
ATOM   420  C  C    . GLU   A 1 55  ? 5.115   -41.063 -2.368  1.00 38.60  ?  57  GLU   A C    1 
ATOM   421  O  O    . GLU   A 1 55  ? 4.029   -40.499 -2.607  1.00 36.86  ?  57  GLU   A O    1 
ATOM   422  C  CB   . GLU   A 1 55  ? 6.901   -39.697 -3.465  1.00 38.66  ?  57  GLU   A CB   1 
ATOM   423  N  N    . SER   A 1 56  ? 5.269   -42.391 -2.276  1.00 37.54  ?  58  SER   A N    1 
ATOM   424  C  CA   . SER   A 1 56  ? 4.142   -43.363 -2.385  1.00 37.35  ?  58  SER   A CA   1 
ATOM   425  C  C    . SER   A 1 56  ? 3.495   -43.747 -1.062  1.00 38.24  ?  58  SER   A C    1 
ATOM   426  O  O    . SER   A 1 56  ? 2.551   -44.555 -1.062  1.00 41.14  ?  58  SER   A O    1 
ATOM   427  C  CB   . SER   A 1 56  ? 4.619   -44.668 -3.051  1.00 35.99  ?  58  SER   A CB   1 
ATOM   428  O  OG   . SER   A 1 56  ? 5.103   -44.423 -4.351  1.00 35.41  ?  58  SER   A OG   1 
ATOM   429  N  N    . ALA   A 1 57  ? 3.998   -43.234 0.070   1.00 40.22  ?  59  ALA   A N    1 
ATOM   430  C  CA   . ALA   A 1 57  ? 3.324   -43.476 1.358   1.00 40.36  ?  59  ALA   A CA   1 
ATOM   431  C  C    . ALA   A 1 57  ? 1.909   -42.903 1.341   1.00 42.09  ?  59  ALA   A C    1 
ATOM   432  O  O    . ALA   A 1 57  ? 1.569   -41.991 0.573   1.00 42.14  ?  59  ALA   A O    1 
ATOM   433  C  CB   . ALA   A 1 57  ? 4.107   -42.927 2.542   1.00 41.04  ?  59  ALA   A CB   1 
ATOM   434  N  N    . GLU   A 1 58  ? 1.084   -43.477 2.198   1.00 42.58  ?  60  GLU   A N    1 
ATOM   435  C  CA   . GLU   A 1 58  ? -0.353  -43.321 2.132   1.00 39.29  ?  60  GLU   A CA   1 
ATOM   436  C  C    . GLU   A 1 58  ? -0.797  -41.860 2.348   1.00 38.73  ?  60  GLU   A C    1 
ATOM   437  O  O    . GLU   A 1 58  ? -0.239  -41.142 3.194   1.00 39.04  ?  60  GLU   A O    1 
ATOM   438  C  CB   . GLU   A 1 58  ? -0.984  -44.246 3.171   1.00 39.62  ?  60  GLU   A CB   1 
ATOM   439  N  N    . ASN   A 1 59  ? -1.789  -41.449 1.549   1.00 38.26  ?  61  ASN   A N    1 
ATOM   440  C  CA   . ASN   A 1 59  ? -2.320  -40.083 1.481   1.00 34.81  ?  61  ASN   A CA   1 
ATOM   441  C  C    . ASN   A 1 59  ? -1.348  -39.052 0.905   1.00 31.16  ?  61  ASN   A C    1 
ATOM   442  O  O    . ASN   A 1 59  ? -1.754  -37.903 0.783   1.00 27.91  ?  61  ASN   A O    1 
ATOM   443  C  CB   . ASN   A 1 59  ? -2.834  -39.552 2.855   1.00 38.48  ?  61  ASN   A CB   1 
ATOM   444  C  CG   . ASN   A 1 59  ? -3.819  -40.494 3.550   1.00 39.57  ?  61  ASN   A CG   1 
ATOM   445  O  OD1  . ASN   A 1 59  ? -3.508  -41.649 3.847   1.00 46.51  ?  61  ASN   A OD1  1 
ATOM   446  N  ND2  . ASN   A 1 59  ? -5.005  -39.985 3.840   1.00 42.55  ?  61  ASN   A ND2  1 
ATOM   447  N  N    . CYS   A 1 60  ? -0.102  -39.419 0.558   1.00 29.10  ?  62  CYS   A N    1 
ATOM   448  C  CA   . CYS   A 1 60  ? 0.919   -38.435 0.084   1.00 28.19  ?  62  CYS   A CA   1 
ATOM   449  C  C    . CYS   A 1 60  ? 0.664   -37.887 -1.303  1.00 28.93  ?  62  CYS   A C    1 
ATOM   450  O  O    . CYS   A 1 60  ? 1.061   -36.758 -1.592  1.00 29.37  ?  62  CYS   A O    1 
ATOM   451  C  CB   . CYS   A 1 60  ? 2.324   -39.012 0.081   1.00 26.93  ?  62  CYS   A CB   1 
ATOM   452  S  SG   . CYS   A 1 60  ? 2.971   -39.256 1.729   1.00 28.59  ?  62  CYS   A SG   1 
ATOM   453  N  N    . ASP   A 1 61  ? -0.006  -38.681 -2.138  1.00 29.06  ?  63  ASP   A N    1 
ATOM   454  C  CA   . ASP   A 1 61  ? -0.407  -38.300 -3.499  1.00 29.32  ?  63  ASP   A CA   1 
ATOM   455  C  C    . ASP   A 1 61  ? -1.619  -37.349 -3.565  1.00 30.36  ?  63  ASP   A C    1 
ATOM   456  O  O    . ASP   A 1 61  ? -2.015  -36.939 -4.665  1.00 29.26  ?  63  ASP   A O    1 
ATOM   457  C  CB   . ASP   A 1 61  ? -0.732  -39.571 -4.309  1.00 32.81  ?  63  ASP   A CB   1 
ATOM   458  C  CG   . ASP   A 1 61  ? -2.061  -40.218 -3.878  1.00 37.79  ?  63  ASP   A CG   1 
ATOM   459  O  OD1  . ASP   A 1 61  ? -2.354  -40.204 -2.651  1.00 33.48  ?  63  ASP   A OD1  1 
ATOM   460  O  OD2  . ASP   A 1 61  ? -2.818  -40.718 -4.766  1.00 44.31  ?  63  ASP   A OD2  1 
ATOM   461  N  N    . LYS   A 1 62  ? -2.224  -37.029 -2.408  1.00 30.68  ?  64  LYS   A N    1 
ATOM   462  C  CA   . LYS   A 1 62  ? -3.368  -36.143 -2.349  1.00 29.11  ?  64  LYS   A CA   1 
ATOM   463  C  C    . LYS   A 1 62  ? -2.941  -34.676 -2.576  1.00 30.03  ?  64  LYS   A C    1 
ATOM   464  O  O    . LYS   A 1 62  ? -1.814  -34.250 -2.256  1.00 24.69  ?  64  LYS   A O    1 
ATOM   465  C  CB   . LYS   A 1 62  ? -4.123  -36.270 -1.036  1.00 30.53  ?  64  LYS   A CB   1 
ATOM   466  C  CG   . LYS   A 1 62  ? -4.660  -37.663 -0.726  1.00 32.59  ?  64  LYS   A CG   1 
ATOM   467  C  CD   . LYS   A 1 62  ? -5.638  -38.166 -1.763  1.00 33.88  ?  64  LYS   A CD   1 
ATOM   468  N  N    . SER   A 1 63  ? -3.862  -33.949 -3.198  1.00 28.95  ?  65  SER   A N    1 
ATOM   469  C  CA   . SER   A 1 63  ? -3.739  -32.525 -3.461  1.00 29.39  ?  65  SER   A CA   1 
ATOM   470  C  C    . SER   A 1 63  ? -3.491  -31.732 -2.170  1.00 27.88  ?  65  SER   A C    1 
ATOM   471  O  O    . SER   A 1 63  ? -3.952  -32.108 -1.062  1.00 24.17  ?  65  SER   A O    1 
ATOM   472  C  CB   . SER   A 1 63  ? -5.052  -32.064 -4.116  1.00 29.92  ?  65  SER   A CB   1 
ATOM   473  O  OG   . SER   A 1 63  ? -5.082  -30.684 -4.304  1.00 36.26  ?  65  SER   A OG   1 
ATOM   474  N  N    . LEU   A 1 64  ? -2.785  -30.615 -2.303  1.00 26.01  ?  66  LEU   A N    1 
ATOM   475  C  CA   . LEU   A 1 64  ? -2.567  -29.801 -1.147  1.00 27.00  ?  66  LEU   A CA   1 
ATOM   476  C  C    . LEU   A 1 64  ? -3.875  -29.204 -0.661  1.00 24.36  ?  66  LEU   A C    1 
ATOM   477  O  O    . LEU   A 1 64  ? -4.148  -29.147 0.541   1.00 24.34  ?  66  LEU   A O    1 
ATOM   478  C  CB   . LEU   A 1 64  ? -1.475  -28.763 -1.376  1.00 28.48  ?  66  LEU   A CB   1 
ATOM   479  C  CG   . LEU   A 1 64  ? -0.135  -29.290 -0.899  1.00 29.95  ?  66  LEU   A CG   1 
ATOM   480  C  CD1  . LEU   A 1 64  ? 0.945   -28.313 -1.258  1.00 31.03  ?  66  LEU   A CD1  1 
ATOM   481  C  CD2  . LEU   A 1 64  ? -0.135  -29.535 0.604   1.00 33.70  ?  66  LEU   A CD2  1 
ATOM   482  N  N    . HIS   A 1 65  ? -4.698  -28.802 -1.594  1.00 23.85  ?  67  HIS   A N    1 
ATOM   483  C  CA   . HIS   A 1 65  ? -6.062  -28.318 -1.277  1.00 23.90  ?  67  HIS   A CA   1 
ATOM   484  C  C    . HIS   A 1 65  ? -6.834  -29.334 -0.477  1.00 21.98  ?  67  HIS   A C    1 
ATOM   485  O  O    . HIS   A 1 65  ? -7.299  -29.041 0.630   1.00 21.21  ?  67  HIS   A O    1 
ATOM   486  C  CB   . HIS   A 1 65  ? -6.782  -27.915 -2.575  1.00 23.02  ?  67  HIS   A CB   1 
ATOM   487  C  CG   . HIS   A 1 65  ? -6.232  -26.659 -3.196  1.00 24.59  ?  67  HIS   A CG   1 
ATOM   488  N  ND1  . HIS   A 1 65  ? -5.354  -26.669 -4.264  1.00 24.36  ?  67  HIS   A ND1  1 
ATOM   489  C  CD2  . HIS   A 1 65  ? -6.427  -25.351 -2.882  1.00 26.10  ?  67  HIS   A CD2  1 
ATOM   490  C  CE1  . HIS   A 1 65  ? -5.041  -25.422 -4.580  1.00 25.81  ?  67  HIS   A CE1  1 
ATOM   491  N  NE2  . HIS   A 1 65  ? -5.687  -24.601 -3.763  1.00 24.71  ?  67  HIS   A NE2  1 
ATOM   492  N  N    . THR   A 1 66  ? -6.895  -30.553 -1.010  1.00 22.76  ?  68  THR   A N    1 
ATOM   493  C  CA   . THR   A 1 66  ? -7.494  -31.703 -0.325  1.00 22.22  ?  68  THR   A CA   1 
ATOM   494  C  C    . THR   A 1 66  ? -7.012  -31.885 1.063   1.00 21.85  ?  68  THR   A C    1 
ATOM   495  O  O    . THR   A 1 66  ? -7.841  -31.985 1.965   1.00 20.34  ?  68  THR   A O    1 
ATOM   496  C  CB   . THR   A 1 66  ? -7.285  -33.001 -1.091  1.00 22.56  ?  68  THR   A CB   1 
ATOM   497  O  OG1  . THR   A 1 66  ? -7.953  -32.865 -2.327  1.00 25.38  ?  68  THR   A OG1  1 
ATOM   498  C  CG2  . THR   A 1 66  ? -7.868  -34.231 -0.376  1.00 24.55  ?  68  THR   A CG2  1 
ATOM   499  N  N    . LEU   A 1 67  ? -5.684  -31.904 1.249   1.00 23.95  ?  69  LEU   A N    1 
ATOM   500  C  CA   . LEU   A 1 67  ? -5.094  -32.112 2.578   1.00 23.49  ?  69  LEU   A CA   1 
ATOM   501  C  C    . LEU   A 1 67  ? -5.399  -30.952 3.531   1.00 22.05  ?  69  LEU   A C    1 
ATOM   502  O  O    . LEU   A 1 67  ? -5.715  -31.169 4.703   1.00 22.89  ?  69  LEU   A O    1 
ATOM   503  C  CB   . LEU   A 1 67  ? -3.567  -32.326 2.481   1.00 26.56  ?  69  LEU   A CB   1 
ATOM   504  C  CG   . LEU   A 1 67  ? -3.074  -33.668 1.886   1.00 29.37  ?  69  LEU   A CG   1 
ATOM   505  C  CD1  . LEU   A 1 67  ? -1.637  -33.523 1.387   1.00 27.20  ?  69  LEU   A CD1  1 
ATOM   506  C  CD2  . LEU   A 1 67  ? -3.240  -34.883 2.826   1.00 28.80  ?  69  LEU   A CD2  1 
ATOM   507  N  N    . PHE   A 1 68  ? -5.301  -29.715 3.030   1.00 21.57  ?  70  PHE   A N    1 
ATOM   508  C  CA   . PHE   A 1 68  ? -5.648  -28.527 3.805   1.00 21.94  ?  70  PHE   A CA   1 
ATOM   509  C  C    . PHE   A 1 68  ? -7.136  -28.548 4.256   1.00 23.40  ?  70  PHE   A C    1 
ATOM   510  O  O    . PHE   A 1 68  ? -7.458  -28.397 5.449   1.00 23.76  ?  70  PHE   A O    1 
ATOM   511  C  CB   . PHE   A 1 68  ? -5.341  -27.259 2.989   1.00 23.06  ?  70  PHE   A CB   1 
ATOM   512  C  CG   . PHE   A 1 68  ? -5.648  -26.004 3.716   1.00 25.95  ?  70  PHE   A CG   1 
ATOM   513  C  CD1  . PHE   A 1 68  ? -4.753  -25.511 4.645   1.00 27.64  ?  70  PHE   A CD1  1 
ATOM   514  C  CD2  . PHE   A 1 68  ? -6.859  -25.359 3.540   1.00 28.32  ?  70  PHE   A CD2  1 
ATOM   515  C  CE1  . PHE   A 1 68  ? -5.032  -24.366 5.371   1.00 26.58  ?  70  PHE   A CE1  1 
ATOM   516  C  CE2  . PHE   A 1 68  ? -7.149  -24.203 4.266   1.00 30.82  ?  70  PHE   A CE2  1 
ATOM   517  C  CZ   . PHE   A 1 68  ? -6.226  -23.705 5.177   1.00 28.60  ?  70  PHE   A CZ   1 
ATOM   518  N  N    . GLY   A 1 69  ? -8.030  -28.763 3.309   1.00 23.32  ?  71  GLY   A N    1 
ATOM   519  C  CA   . GLY   A 1 69  ? -9.456  -28.875 3.614   1.00 25.07  ?  71  GLY   A CA   1 
ATOM   520  C  C    . GLY   A 1 69  ? -9.830  -30.021 4.549   1.00 25.46  ?  71  GLY   A C    1 
ATOM   521  O  O    . GLY   A 1 69  ? -10.759 -29.890 5.378   1.00 25.57  ?  71  GLY   A O    1 
ATOM   522  N  N    . ASP   A 1 70  ? -9.158  -31.157 4.405   1.00 26.88  ?  72  ASP   A N    1 
ATOM   523  C  CA   . ASP   A 1 70  ? -9.409  -32.281 5.309   1.00 26.76  ?  72  ASP   A CA   1 
ATOM   524  C  C    . ASP   A 1 70  ? -8.931  -31.957 6.708   1.00 25.23  ?  72  ASP   A C    1 
ATOM   525  O  O    . ASP   A 1 70  ? -9.605  -32.337 7.683   1.00 25.34  ?  72  ASP   A O    1 
ATOM   526  C  CB   . ASP   A 1 70  ? -8.713  -33.553 4.839   1.00 30.12  ?  72  ASP   A CB   1 
ATOM   527  C  CG   . ASP   A 1 70  ? -9.290  -34.101 3.578   1.00 31.89  ?  72  ASP   A CG   1 
ATOM   528  O  OD1  . ASP   A 1 70  ? -10.405 -33.697 3.211   1.00 38.83  ?  72  ASP   A OD1  1 
ATOM   529  O  OD2  . ASP   A 1 70  ? -8.629  -34.920 2.928   1.00 30.61  ?  72  ASP   A OD2  1 
ATOM   530  N  N    . LYS   A 1 71  ? -7.803  -31.250 6.856   1.00 23.64  ?  73  LYS   A N    1 
ATOM   531  C  CA   . LYS   A 1 71  ? -7.365  -30.883 8.239   1.00 22.45  ?  73  LYS   A CA   1 
ATOM   532  C  C    . LYS   A 1 71  ? -8.320  -29.907 8.908   1.00 22.60  ?  73  LYS   A C    1 
ATOM   533  O  O    . LYS   A 1 71  ? -8.574  -30.034 10.125  1.00 21.62  ?  73  LYS   A O    1 
ATOM   534  C  CB   . LYS   A 1 71  ? -5.906  -30.367 8.351   1.00 22.91  ?  73  LYS   A CB   1 
ATOM   535  C  CG   . LYS   A 1 71  ? -4.943  -31.467 8.844   1.00 26.46  ?  73  LYS   A CG   1 
ATOM   536  C  CD   . LYS   A 1 71  ? -4.561  -31.296 10.301  1.00 28.17  ?  73  LYS   A CD   1 
ATOM   537  C  CE   . LYS   A 1 71  ? -4.162  -32.579 11.012  1.00 30.53  ?  73  LYS   A CE   1 
ATOM   538  N  NZ   . LYS   A 1 71  ? -3.894  -33.823 10.235  1.00 33.23  ?  73  LYS   A NZ   1 
ATOM   539  N  N    . LEU   A 1 72  ? -8.809  -28.921 8.140   1.00 22.10  ?  74  LEU   A N    1 
ATOM   540  C  CA   . LEU   A 1 72  ? -9.825  -27.993 8.623   1.00 22.29  ?  74  LEU   A CA   1 
ATOM   541  C  C    . LEU   A 1 72  ? -11.018 -28.805 9.093   1.00 22.52  ?  74  LEU   A C    1 
ATOM   542  O  O    . LEU   A 1 72  ? -11.481 -28.624 10.211  1.00 21.18  ?  74  LEU   A O    1 
ATOM   543  C  CB   . LEU   A 1 72  ? -10.270 -27.008 7.539   1.00 21.46  ?  74  LEU   A CB   1 
ATOM   544  C  CG   . LEU   A 1 72  ? -9.816  -25.550 7.584   1.00 23.13  ?  74  LEU   A CG   1 
ATOM   545  C  CD1  . LEU   A 1 72  ? -8.483  -25.375 8.264   1.00 21.98  ?  74  LEU   A CD1  1 
ATOM   546  C  CD2  . LEU   A 1 72  ? -9.833  -24.949 6.166   1.00 22.91  ?  74  LEU   A CD2  1 
ATOM   547  N  N    . CYS   A 1 73  ? -11.455 -29.754 8.281   1.00 25.74  ?  75  CYS   A N    1 
ATOM   548  C  CA   . CYS   A 1 73  ? -12.669 -30.523 8.641   1.00 30.47  ?  75  CYS   A CA   1 
ATOM   549  C  C    . CYS   A 1 73  ? -12.495 -31.496 9.803   1.00 30.89  ?  75  CYS   A C    1 
ATOM   550  O  O    . CYS   A 1 73  ? -13.477 -32.079 10.221  1.00 29.81  ?  75  CYS   A O    1 
ATOM   551  C  CB   . CYS   A 1 73  ? -13.242 -31.221 7.411   1.00 31.53  ?  75  CYS   A CB   1 
ATOM   552  S  SG   . CYS   A 1 73  ? -13.798 -29.986 6.202   1.00 37.99  ?  75  CYS   A SG   1 
ATOM   553  N  N    . THR   A 1 74  ? -11.262 -31.676 10.306  1.00 30.31  ?  76  THR   A N    1 
ATOM   554  C  CA   . THR   A 1 74  ? -10.982 -32.541 11.471  1.00 31.36  ?  76  THR   A CA   1 
ATOM   555  C  C    . THR   A 1 74  ? -11.062 -31.749 12.755  1.00 33.26  ?  76  THR   A C    1 
ATOM   556  O  O    . THR   A 1 74  ? -11.025 -32.348 13.831  1.00 33.75  ?  76  THR   A O    1 
ATOM   557  C  CB   . THR   A 1 74  ? -9.540  -33.124 11.481  1.00 28.84  ?  76  THR   A CB   1 
ATOM   558  O  OG1  . THR   A 1 74  ? -8.583  -32.038 11.487  1.00 31.36  ?  76  THR   A OG1  1 
ATOM   559  C  CG2  . THR   A 1 74  ? -9.307  -34.028 10.334  1.00 29.09  ?  76  THR   A CG2  1 
ATOM   560  N  N    . VAL   A 1 75  ? -11.087 -30.417 12.652  1.00 31.06  ?  77  VAL   A N    1 
ATOM   561  C  CA   . VAL   A 1 75  ? -11.138 -29.556 13.810  1.00 31.93  ?  77  VAL   A CA   1 
ATOM   562  C  C    . VAL   A 1 75  ? -12.481 -29.839 14.461  1.00 33.27  ?  77  VAL   A C    1 
ATOM   563  O  O    . VAL   A 1 75  ? -13.517 -29.644 13.840  1.00 31.83  ?  77  VAL   A O    1 
ATOM   564  C  CB   . VAL   A 1 75  ? -10.990 -28.048 13.411  1.00 33.31  ?  77  VAL   A CB   1 
ATOM   565  C  CG1  . VAL   A 1 75  ? -11.300 -27.127 14.580  1.00 33.80  ?  77  VAL   A CG1  1 
ATOM   566  C  CG2  . VAL   A 1 75  ? -9.590  -27.759 12.869  1.00 32.12  ?  77  VAL   A CG2  1 
ATOM   567  N  N    . ALA   A 1 76  ? -12.469 -30.353 15.689  1.00 34.78  ?  78  ALA   A N    1 
ATOM   568  C  CA   . ALA   A 1 76  ? -13.702 -30.906 16.277  1.00 34.10  ?  78  ALA   A CA   1 
ATOM   569  C  C    . ALA   A 1 76  ? -14.653 -29.803 16.703  1.00 31.40  ?  78  ALA   A C    1 
ATOM   570  O  O    . ALA   A 1 76  ? -15.848 -29.989 16.694  1.00 32.43  ?  78  ALA   A O    1 
ATOM   571  C  CB   . ALA   A 1 76  ? -13.394 -31.833 17.437  1.00 35.69  ?  78  ALA   A CB   1 
ATOM   572  N  N    . THR   A 1 77  ? -14.117 -28.628 16.993  1.00 29.14  ?  79  THR   A N    1 
ATOM   573  C  CA   . THR   A 1 77  ? -14.931 -27.515 17.391  1.00 28.45  ?  79  THR   A CA   1 
ATOM   574  C  C    . THR   A 1 77  ? -15.417 -26.667 16.206  1.00 27.94  ?  79  THR   A C    1 
ATOM   575  O  O    . THR   A 1 77  ? -15.929 -25.560 16.421  1.00 28.63  ?  79  THR   A O    1 
ATOM   576  C  CB   . THR   A 1 77  ? -14.112 -26.627 18.364  1.00 28.94  ?  79  THR   A CB   1 
ATOM   577  N  N    . LEU   A 1 78  ? -15.290 -27.163 14.968  1.00 29.08  ?  80  LEU   A N    1 
ATOM   578  C  CA   . LEU   A 1 78  ? -15.434 -26.317 13.759  1.00 27.93  ?  80  LEU   A CA   1 
ATOM   579  C  C    . LEU   A 1 78  ? -16.819 -25.694 13.634  1.00 27.95  ?  80  LEU   A C    1 
ATOM   580  O  O    . LEU   A 1 78  ? -16.967 -24.460 13.498  1.00 28.42  ?  80  LEU   A O    1 
ATOM   581  C  CB   . LEU   A 1 78  ? -15.103 -27.125 12.489  1.00 29.16  ?  80  LEU   A CB   1 
ATOM   582  C  CG   . LEU   A 1 78  ? -14.946 -26.357 11.157  1.00 28.37  ?  80  LEU   A CG   1 
ATOM   583  C  CD1  . LEU   A 1 78  ? -13.692 -25.498 11.133  1.00 28.00  ?  80  LEU   A CD1  1 
ATOM   584  C  CD2  . LEU   A 1 78  ? -14.950 -27.305 9.962   1.00 31.88  ?  80  LEU   A CD2  1 
ATOM   585  N  N    . ARG   A 1 79  ? -17.828 -26.547 13.713  1.00 27.48  ?  81  ARG   A N    1 
ATOM   586  C  CA   . ARG   A 1 79  ? -19.222 -26.107 13.670  1.00 30.98  ?  81  ARG   A CA   1 
ATOM   587  C  C    . ARG   A 1 79  ? -19.577 -25.194 14.822  1.00 33.38  ?  81  ARG   A C    1 
ATOM   588  O  O    . ARG   A 1 79  ? -20.249 -24.174 14.593  1.00 36.23  ?  81  ARG   A O    1 
ATOM   589  C  CB   . ARG   A 1 79  ? -20.185 -27.297 13.656  1.00 31.24  ?  81  ARG   A CB   1 
ATOM   590  C  CG   . ARG   A 1 79  ? -21.661 -26.927 13.714  1.00 36.24  ?  81  ARG   A CG   1 
ATOM   591  C  CD   . ARG   A 1 79  ? -22.557 -28.088 13.301  1.00 36.74  ?  81  ARG   A CD   1 
ATOM   592  N  NE   . ARG   A 1 79  ? -22.861 -28.001 11.882  1.00 41.35  ?  81  ARG   A NE   1 
ATOM   593  C  CZ   . ARG   A 1 79  ? -22.208 -28.613 10.894  1.00 42.45  ?  81  ARG   A CZ   1 
ATOM   594  N  NH1  . ARG   A 1 79  ? -21.173 -29.415 11.117  1.00 48.92  ?  81  ARG   A NH1  1 
ATOM   595  N  NH2  . ARG   A 1 79  ? -22.598 -28.413 9.645   1.00 40.84  ?  81  ARG   A NH2  1 
ATOM   596  N  N    . GLU   A 1 80  ? -19.149 -25.552 16.048  1.00 29.35  ?  82  GLU   A N    1 
ATOM   597  C  CA   . GLU   A 1 80  ? -19.541 -24.781 17.212  1.00 29.59  ?  82  GLU   A CA   1 
ATOM   598  C  C    . GLU   A 1 80  ? -19.024 -23.366 17.059  1.00 30.12  ?  82  GLU   A C    1 
ATOM   599  O  O    . GLU   A 1 80  ? -19.703 -22.422 17.439  1.00 31.48  ?  82  GLU   A O    1 
ATOM   600  C  CB   . GLU   A 1 80  ? -19.063 -25.425 18.541  1.00 29.59  ?  82  GLU   A CB   1 
ATOM   601  N  N    . THR   A 1 81  ? -17.853 -23.213 16.445  1.00 29.06  ?  83  THR   A N    1 
ATOM   602  C  CA   . THR   A 1 81  ? -17.146 -21.949 16.474  1.00 29.54  ?  83  THR   A CA   1 
ATOM   603  C  C    . THR   A 1 81  ? -17.329 -21.104 15.228  1.00 28.02  ?  83  THR   A C    1 
ATOM   604  O  O    . THR   A 1 81  ? -17.345 -19.873 15.333  1.00 27.61  ?  83  THR   A O    1 
ATOM   605  C  CB   . THR   A 1 81  ? -15.613 -22.201 16.689  1.00 30.53  ?  83  THR   A CB   1 
ATOM   606  O  OG1  . THR   A 1 81  ? -15.403 -22.975 17.865  1.00 32.77  ?  83  THR   A OG1  1 
ATOM   607  C  CG2  . THR   A 1 81  ? -14.830 -20.887 16.799  1.00 30.20  ?  83  THR   A CG2  1 
ATOM   608  N  N    . TYR   A 1 82  ? -17.361 -21.765 14.062  1.00 29.43  ?  84  TYR   A N    1 
ATOM   609  C  CA   . TYR   A 1 82  ? -17.351 -21.108 12.735  1.00 31.69  ?  84  TYR   A CA   1 
ATOM   610  C  C    . TYR   A 1 82  ? -18.623 -21.371 11.910  1.00 33.59  ?  84  TYR   A C    1 
ATOM   611  O  O    . TYR   A 1 82  ? -18.900 -20.635 10.967  1.00 37.74  ?  84  TYR   A O    1 
ATOM   612  C  CB   . TYR   A 1 82  ? -16.118 -21.551 11.924  1.00 29.84  ?  84  TYR   A CB   1 
ATOM   613  C  CG   . TYR   A 1 82  ? -14.780 -21.402 12.669  1.00 28.79  ?  84  TYR   A CG   1 
ATOM   614  C  CD1  . TYR   A 1 82  ? -14.122 -20.166 12.745  1.00 27.82  ?  84  TYR   A CD1  1 
ATOM   615  C  CD2  . TYR   A 1 82  ? -14.182 -22.493 13.281  1.00 28.65  ?  84  TYR   A CD2  1 
ATOM   616  C  CE1  . TYR   A 1 82  ? -12.908 -20.034 13.409  1.00 28.55  ?  84  TYR   A CE1  1 
ATOM   617  C  CE2  . TYR   A 1 82  ? -12.965 -22.375 13.960  1.00 30.05  ?  84  TYR   A CE2  1 
ATOM   618  C  CZ   . TYR   A 1 82  ? -12.332 -21.147 14.012  1.00 30.09  ?  84  TYR   A CZ   1 
ATOM   619  O  OH   . TYR   A 1 82  ? -11.149 -21.042 14.708  1.00 33.33  ?  84  TYR   A OH   1 
ATOM   620  N  N    . GLY   A 1 83  ? -19.367 -22.437 12.226  1.00 37.86  ?  85  GLY   A N    1 
ATOM   621  C  CA   . GLY   A 1 83  ? -20.760 -22.576 11.786  1.00 36.88  ?  85  GLY   A CA   1 
ATOM   622  C  C    . GLY   A 1 83  ? -20.925 -22.896 10.317  1.00 36.88  ?  85  GLY   A C    1 
ATOM   623  O  O    . GLY   A 1 83  ? -20.799 -24.060 9.914   1.00 38.74  ?  85  GLY   A O    1 
ATOM   624  N  N    . GLU   A 1 84  ? -21.196 -21.866 9.510   1.00 34.47  ?  86  GLU   A N    1 
ATOM   625  C  CA   . GLU   A 1 84  ? -21.376 -22.033 8.045   1.00 37.20  ?  86  GLU   A CA   1 
ATOM   626  C  C    . GLU   A 1 84  ? -20.201 -22.738 7.402   1.00 32.60  ?  86  GLU   A C    1 
ATOM   627  O  O    . GLU   A 1 84  ? -20.380 -23.585 6.547   1.00 34.48  ?  86  GLU   A O    1 
ATOM   628  C  CB   . GLU   A 1 84  ? -21.540 -20.676 7.330   1.00 39.33  ?  86  GLU   A CB   1 
ATOM   629  C  CG   . GLU   A 1 84  ? -22.947 -20.084 7.333   1.00 41.55  ?  86  GLU   A CG   1 
ATOM   630  C  CD   . GLU   A 1 84  ? -23.046 -18.918 6.357   1.00 43.84  ?  86  GLU   A CD   1 
ATOM   631  O  OE1  . GLU   A 1 84  ? -22.862 -19.178 5.152   1.00 50.57  ?  86  GLU   A OE1  1 
ATOM   632  O  OE2  . GLU   A 1 84  ? -23.280 -17.755 6.771   1.00 43.96  ?  86  GLU   A OE2  1 
ATOM   633  N  N    . MET   A 1 85  ? -19.001 -22.346 7.812   1.00 31.67  ?  87  MET   A N    1 
ATOM   634  C  CA   . MET   A 1 85  ? -17.760 -22.928 7.319   1.00 29.19  ?  87  MET   A CA   1 
ATOM   635  C  C    . MET   A 1 85  ? -17.787 -24.469 7.437   1.00 25.83  ?  87  MET   A C    1 
ATOM   636  O  O    . MET   A 1 85  ? -17.294 -25.167 6.565   1.00 22.74  ?  87  MET   A O    1 
ATOM   637  C  CB   . MET   A 1 85  ? -16.593 -22.339 8.118   1.00 31.14  ?  87  MET   A CB   1 
ATOM   638  C  CG   . MET   A 1 85  ? -15.220 -22.817 7.681   1.00 36.42  ?  87  MET   A CG   1 
ATOM   639  S  SD   . MET   A 1 85  ? -13.877 -22.219 8.703   1.00 41.60  ?  87  MET   A SD   1 
ATOM   640  C  CE   . MET   A 1 85  ? -14.012 -20.465 8.326   1.00 44.00  ?  87  MET   A CE   1 
ATOM   641  N  N    . ALA   A 1 86  ? -18.344 -24.985 8.529   1.00 24.72  ?  88  ALA   A N    1 
ATOM   642  C  CA   . ALA   A 1 86  ? -18.432 -26.447 8.740   1.00 24.87  ?  88  ALA   A CA   1 
ATOM   643  C  C    . ALA   A 1 86  ? -19.287 -27.160 7.700   1.00 24.79  ?  88  ALA   A C    1 
ATOM   644  O  O    . ALA   A 1 86  ? -19.081 -28.358 7.508   1.00 25.11  ?  88  ALA   A O    1 
ATOM   645  C  CB   . ALA   A 1 86  ? -18.923 -26.777 10.150  1.00 24.96  ?  88  ALA   A CB   1 
ATOM   646  N  N    . ASP   A 1 87  ? -20.202 -26.430 7.025   1.00 23.14  ?  89  ASP   A N    1 
ATOM   647  C  CA   . ASP   A 1 87  ? -21.012 -26.964 5.917   1.00 24.39  ?  89  ASP   A CA   1 
ATOM   648  C  C    . ASP   A 1 87  ? -20.221 -27.073 4.649   1.00 23.59  ?  89  ASP   A C    1 
ATOM   649  O  O    . ASP   A 1 87  ? -20.609 -27.819 3.752   1.00 25.20  ?  89  ASP   A O    1 
ATOM   650  C  CB   . ASP   A 1 87  ? -22.298 -26.104 5.643   1.00 26.20  ?  89  ASP   A CB   1 
ATOM   651  C  CG   . ASP   A 1 87  ? -23.233 -25.999 6.896   1.00 28.39  ?  89  ASP   A CG   1 
ATOM   652  O  OD1  . ASP   A 1 87  ? -23.408 -27.017 7.622   1.00 25.59  ?  89  ASP   A OD1  1 
ATOM   653  O  OD2  . ASP   A 1 87  ? -23.757 -24.893 7.173   1.00 28.23  ?  89  ASP   A OD2  1 
ATOM   654  N  N    . CYS   A 1 88  ? -19.115 -26.348 4.517   1.00 23.19  ?  90  CYS   A N    1 
ATOM   655  C  CA   . CYS   A 1 88  ? -18.205 -26.628 3.395   1.00 23.65  ?  90  CYS   A CA   1 
ATOM   656  C  C    . CYS   A 1 88  ? -17.691 -28.087 3.379   1.00 23.01  ?  90  CYS   A C    1 
ATOM   657  O  O    . CYS   A 1 88  ? -17.403 -28.602 2.324   1.00 21.58  ?  90  CYS   A O    1 
ATOM   658  C  CB   . CYS   A 1 88  ? -16.999 -25.715 3.400   1.00 24.65  ?  90  CYS   A CB   1 
ATOM   659  S  SG   . CYS   A 1 88  ? -17.379 -23.951 3.433   1.00 26.93  ?  90  CYS   A SG   1 
ATOM   660  N  N    . CYS   A 1 89  ? -17.536 -28.709 4.539   1.00 25.10  ?  91  CYS   A N    1 
ATOM   661  C  CA   . CYS   A 1 89  ? -17.019 -30.077 4.649   1.00 28.52  ?  91  CYS   A CA   1 
ATOM   662  C  C    . CYS   A 1 89  ? -17.941 -31.140 4.060   1.00 28.40  ?  91  CYS   A C    1 
ATOM   663  O  O    . CYS   A 1 89  ? -17.500 -32.212 3.726   1.00 30.72  ?  91  CYS   A O    1 
ATOM   664  C  CB   . CYS   A 1 89  ? -16.790 -30.412 6.114   1.00 30.61  ?  91  CYS   A CB   1 
ATOM   665  S  SG   . CYS   A 1 89  ? -15.609 -29.314 6.938   1.00 37.75  ?  91  CYS   A SG   1 
ATOM   666  N  N    . ALA   A 1 90  ? -19.228 -30.852 3.971   1.00 28.46  ?  92  ALA   A N    1 
ATOM   667  C  CA   . ALA   A 1 90  ? -20.162 -31.714 3.243   1.00 30.76  ?  92  ALA   A CA   1 
ATOM   668  C  C    . ALA   A 1 90  ? -19.990 -31.663 1.697   1.00 31.91  ?  92  ALA   A C    1 
ATOM   669  O  O    . ALA   A 1 90  ? -20.593 -32.450 1.002   1.00 29.80  ?  92  ALA   A O    1 
ATOM   670  C  CB   . ALA   A 1 90  ? -21.605 -31.356 3.632   1.00 31.77  ?  92  ALA   A CB   1 
ATOM   671  N  N    . LYS   A 1 91  ? -19.205 -30.724 1.170   1.00 34.42  ?  93  LYS   A N    1 
ATOM   672  C  CA   . LYS   A 1 91  ? -18.952 -30.600 -0.280  1.00 37.47  ?  93  LYS   A CA   1 
ATOM   673  C  C    . LYS   A 1 91  ? -17.803 -31.497 -0.780  1.00 39.18  ?  93  LYS   A C    1 
ATOM   674  O  O    . LYS   A 1 91  ? -16.888 -31.846 -0.017  1.00 37.78  ?  93  LYS   A O    1 
ATOM   675  C  CB   . LYS   A 1 91  ? -18.629 -29.150 -0.619  1.00 39.18  ?  93  LYS   A CB   1 
ATOM   676  C  CG   . LYS   A 1 91  ? -19.694 -28.168 -0.132  1.00 41.26  ?  93  LYS   A CG   1 
ATOM   677  C  CD   . LYS   A 1 91  ? -19.335 -26.706 -0.373  1.00 43.16  ?  93  LYS   A CD   1 
ATOM   678  C  CE   . LYS   A 1 91  ? -20.574 -25.810 -0.529  1.00 43.38  ?  93  LYS   A CE   1 
ATOM   679  N  NZ   . LYS   A 1 91  ? -21.710 -26.106 0.398   1.00 44.20  ?  93  LYS   A NZ   1 
ATOM   680  N  N    . GLN   A 1 92  ? -17.874 -31.872 -2.062  1.00 42.15  ?  94  GLN   A N    1 
ATOM   681  C  CA   . GLN   A 1 92  ? -16.794 -32.588 -2.745  1.00 43.18  ?  94  GLN   A CA   1 
ATOM   682  C  C    . GLN   A 1 92  ? -15.753 -31.576 -3.176  1.00 42.72  ?  94  GLN   A C    1 
ATOM   683  O  O    . GLN   A 1 92  ? -16.101 -30.459 -3.608  1.00 39.81  ?  94  GLN   A O    1 
ATOM   684  C  CB   . GLN   A 1 92  ? -17.325 -33.349 -3.961  1.00 49.08  ?  94  GLN   A CB   1 
ATOM   685  N  N    . GLU   A 1 93  ? -14.490 -31.989 -3.118  1.00 42.14  ?  95  GLU   A N    1 
ATOM   686  C  CA   . GLU   A 1 93  ? -13.369 -31.049 -2.948  1.00 45.83  ?  95  GLU   A CA   1 
ATOM   687  C  C    . GLU   A 1 93  ? -13.328 -29.815 -3.871  1.00 47.49  ?  95  GLU   A C    1 
ATOM   688  O  O    . GLU   A 1 93  ? -13.073 -28.703 -3.368  1.00 50.05  ?  95  GLU   A O    1 
ATOM   689  C  CB   . GLU   A 1 93  ? -12.003 -31.775 -2.865  1.00 46.79  ?  95  GLU   A CB   1 
ATOM   690  C  CG   . GLU   A 1 93  ? -10.716 -30.924 -2.896  1.00 47.07  ?  95  GLU   A CG   1 
ATOM   691  C  CD   . GLU   A 1 93  ? -10.702 -29.581 -2.127  1.00 46.13  ?  95  GLU   A CD   1 
ATOM   692  O  OE1  . GLU   A 1 93  ? -11.120 -29.451 -0.957  1.00 44.08  ?  95  GLU   A OE1  1 
ATOM   693  O  OE2  . GLU   A 1 93  ? -10.206 -28.609 -2.720  1.00 51.97  ?  95  GLU   A OE2  1 
ATOM   694  N  N    . PRO   A 1 94  ? -13.601 -29.964 -5.188  1.00 41.57  ?  96  PRO   A N    1 
ATOM   695  C  CA   . PRO   A 1 94  ? -13.494 -28.682 -5.951  1.00 38.29  ?  96  PRO   A CA   1 
ATOM   696  C  C    . PRO   A 1 94  ? -14.366 -27.568 -5.324  1.00 36.35  ?  96  PRO   A C    1 
ATOM   697  O  O    . PRO   A 1 94  ? -13.859 -26.513 -4.938  1.00 32.06  ?  96  PRO   A O    1 
ATOM   698  C  CB   . PRO   A 1 94  ? -13.933 -29.051 -7.376  1.00 40.28  ?  96  PRO   A CB   1 
ATOM   699  C  CG   . PRO   A 1 94  ? -14.049 -30.550 -7.405  1.00 40.39  ?  96  PRO   A CG   1 
ATOM   700  C  CD   . PRO   A 1 94  ? -13.983 -31.122 -6.012  1.00 38.11  ?  96  PRO   A CD   1 
ATOM   701  N  N    . GLU   A 1 95  ? -15.642 -27.879 -5.109  1.00 36.85  ?  97  GLU   A N    1 
ATOM   702  C  CA   . GLU   A 1 95  ? -16.620 -26.923 -4.563  1.00 36.68  ?  97  GLU   A CA   1 
ATOM   703  C  C    . GLU   A 1 95  ? -16.378 -26.652 -3.056  1.00 32.12  ?  97  GLU   A C    1 
ATOM   704  O  O    . GLU   A 1 95  ? -16.641 -25.556 -2.563  1.00 29.13  ?  97  GLU   A O    1 
ATOM   705  C  CB   . GLU   A 1 95  ? -18.062 -27.407 -4.840  1.00 40.57  ?  97  GLU   A CB   1 
ATOM   706  C  CG   . GLU   A 1 95  ? -18.411 -27.692 -6.319  1.00 42.99  ?  97  GLU   A CG   1 
ATOM   707  C  CD   . GLU   A 1 95  ? -18.161 -29.158 -6.745  1.00 48.63  ?  97  GLU   A CD   1 
ATOM   708  O  OE1  . GLU   A 1 95  ? -17.005 -29.641 -6.615  1.00 46.96  ?  97  GLU   A OE1  1 
ATOM   709  O  OE2  . GLU   A 1 95  ? -19.110 -29.846 -7.207  1.00 51.86  ?  97  GLU   A OE2  1 
ATOM   710  N  N    . ARG   A 1 96  ? -15.837 -27.645 -2.349  1.00 30.17  ?  98  ARG   A N    1 
ATOM   711  C  CA   . ARG   A 1 96  ? -15.416 -27.479 -0.965  1.00 28.23  ?  98  ARG   A CA   1 
ATOM   712  C  C    . ARG   A 1 96  ? -14.403 -26.361 -0.770  1.00 27.14  ?  98  ARG   A C    1 
ATOM   713  O  O    . ARG   A 1 96  ? -14.524 -25.578 0.186   1.00 25.49  ?  98  ARG   A O    1 
ATOM   714  C  CB   . ARG   A 1 96  ? -14.782 -28.759 -0.402  1.00 25.89  ?  98  ARG   A CB   1 
ATOM   715  C  CG   . ARG   A 1 96  ? -14.378 -28.591 1.049   1.00 25.56  ?  98  ARG   A CG   1 
ATOM   716  C  CD   . ARG   A 1 96  ? -13.976 -29.901 1.729   1.00 26.18  ?  98  ARG   A CD   1 
ATOM   717  N  NE   . ARG   A 1 96  ? -12.610 -30.214 1.373   1.00 24.00  ?  98  ARG   A NE   1 
ATOM   718  C  CZ   . ARG   A 1 96  ? -11.920 -31.251 1.811   1.00 25.89  ?  98  ARG   A CZ   1 
ATOM   719  N  NH1  . ARG   A 1 96  ? -12.441 -32.097 2.668   1.00 24.74  ?  98  ARG   A NH1  1 
ATOM   720  N  NH2  . ARG   A 1 96  ? -10.673 -31.444 1.364   1.00 26.77  ?  98  ARG   A NH2  1 
ATOM   721  N  N    . ASN   A 1 97  ? -13.367 -26.337 -1.609  1.00 27.86  ?  99  ASN   A N    1 
ATOM   722  C  CA   . ASN   A 1 97  ? -12.275 -25.370 -1.391  1.00 28.72  ?  99  ASN   A CA   1 
ATOM   723  C  C    . ASN   A 1 97  ? -12.834 -23.976 -1.744  1.00 26.36  ?  99  ASN   A C    1 
ATOM   724  O  O    . ASN   A 1 97  ? -12.521 -22.982 -1.069  1.00 23.45  ?  99  ASN   A O    1 
ATOM   725  C  CB   . ASN   A 1 97  ? -11.001 -25.703 -2.179  1.00 27.18  ?  99  ASN   A CB   1 
ATOM   726  C  CG   . ASN   A 1 97  ? -9.927  -24.597 -2.058  1.00 29.62  ?  99  ASN   A CG   1 
ATOM   727  O  OD1  . ASN   A 1 97  ? -9.065  -24.671 -1.178  1.00 31.58  ?  99  ASN   A OD1  1 
ATOM   728  N  ND2  . ASN   A 1 97  ? -10.012 -23.549 -2.906  1.00 25.61  ?  99  ASN   A ND2  1 
ATOM   729  N  N    . GLU   A 1 98  ? -13.687 -23.921 -2.754  1.00 26.22  ?  100 GLU   A N    1 
ATOM   730  C  CA   . GLU   A 1 98  ? -14.331 -22.647 -3.077  1.00 29.84  ?  100 GLU   A CA   1 
ATOM   731  C  C    . GLU   A 1 98  ? -15.168 -22.120 -1.925  1.00 30.15  ?  100 GLU   A C    1 
ATOM   732  O  O    . GLU   A 1 98  ? -15.195 -20.902 -1.679  1.00 29.46  ?  100 GLU   A O    1 
ATOM   733  C  CB   . GLU   A 1 98  ? -15.164 -22.730 -4.357  1.00 31.87  ?  100 GLU   A CB   1 
ATOM   734  C  CG   . GLU   A 1 98  ? -15.566 -21.358 -4.914  1.00 35.37  ?  100 GLU   A CG   1 
ATOM   735  C  CD   . GLU   A 1 98  ? -14.367 -20.456 -5.264  1.00 40.37  ?  100 GLU   A CD   1 
ATOM   736  O  OE1  . GLU   A 1 98  ? -13.265 -20.995 -5.639  1.00 41.11  ?  100 GLU   A OE1  1 
ATOM   737  O  OE2  . GLU   A 1 98  ? -14.535 -19.202 -5.160  1.00 45.35  ?  100 GLU   A OE2  1 
ATOM   738  N  N    . CYS   A 1 99  ? -15.822 -23.032 -1.210  1.00 28.11  ?  101 CYS   A N    1 
ATOM   739  C  CA   . CYS   A 1 99  ? -16.670 -22.669 -0.064  1.00 28.61  ?  101 CYS   A CA   1 
ATOM   740  C  C    . CYS   A 1 99  ? -15.853 -22.129 1.137   1.00 26.82  ?  101 CYS   A C    1 
ATOM   741  O  O    . CYS   A 1 99  ? -16.276 -21.192 1.815   1.00 24.20  ?  101 CYS   A O    1 
ATOM   742  C  CB   . CYS   A 1 99  ? -17.536 -23.878 0.351   1.00 28.14  ?  101 CYS   A CB   1 
ATOM   743  S  SG   . CYS   A 1 99  ? -18.601 -23.644 1.799   1.00 31.07  ?  101 CYS   A SG   1 
ATOM   744  N  N    . PHE   A 1 100 ? -14.695 -22.722 1.410   1.00 25.79  ?  102 PHE   A N    1 
ATOM   745  C  CA   . PHE   A 1 100 ? -13.820 -22.211 2.492   1.00 25.09  ?  102 PHE   A CA   1 
ATOM   746  C  C    . PHE   A 1 100 ? -13.342 -20.785 2.224   1.00 24.82  ?  102 PHE   A C    1 
ATOM   747  O  O    . PHE   A 1 100 ? -13.261 -19.971 3.135   1.00 21.16  ?  102 PHE   A O    1 
ATOM   748  C  CB   . PHE   A 1 100 ? -12.616 -23.127 2.698   1.00 24.83  ?  102 PHE   A CB   1 
ATOM   749  C  CG   . PHE   A 1 100 ? -12.938 -24.353 3.459   1.00 24.05  ?  102 PHE   A CG   1 
ATOM   750  C  CD1  . PHE   A 1 100 ? -13.316 -24.256 4.772   1.00 25.02  ?  102 PHE   A CD1  1 
ATOM   751  C  CD2  . PHE   A 1 100 ? -12.843 -25.596 2.889   1.00 24.92  ?  102 PHE   A CD2  1 
ATOM   752  C  CE1  . PHE   A 1 100 ? -13.622 -25.381 5.502   1.00 25.94  ?  102 PHE   A CE1  1 
ATOM   753  C  CE2  . PHE   A 1 100 ? -13.132 -26.731 3.616   1.00 24.11  ?  102 PHE   A CE2  1 
ATOM   754  C  CZ   . PHE   A 1 100 ? -13.510 -26.621 4.931   1.00 24.93  ?  102 PHE   A CZ   1 
ATOM   755  N  N    . LEU   A 1 101 ? -13.022 -20.512 0.963   1.00 27.53  ?  103 LEU   A N    1 
ATOM   756  C  CA   . LEU   A 1 101 ? -12.561 -19.197 0.540   1.00 29.53  ?  103 LEU   A CA   1 
ATOM   757  C  C    . LEU   A 1 101 ? -13.563 -18.070 0.903   1.00 32.99  ?  103 LEU   A C    1 
ATOM   758  O  O    . LEU   A 1 101 ? -13.160 -17.024 1.403   1.00 34.27  ?  103 LEU   A O    1 
ATOM   759  C  CB   . LEU   A 1 101 ? -12.285 -19.210 -0.964  1.00 28.98  ?  103 LEU   A CB   1 
ATOM   760  C  CG   . LEU   A 1 101 ? -10.858 -19.547 -1.379  1.00 28.30  ?  103 LEU   A CG   1 
ATOM   761  C  CD1  . LEU   A 1 101 ? -10.771 -20.016 -2.839  1.00 29.58  ?  103 LEU   A CD1  1 
ATOM   762  C  CD2  . LEU   A 1 101 ? -10.026 -18.286 -1.195  1.00 29.71  ?  103 LEU   A CD2  1 
ATOM   763  N  N    . GLN   A 1 102 ? -14.855 -18.305 0.677   1.00 34.59  ?  104 GLN   A N    1 
ATOM   764  C  CA   . GLN   A 1 102 ? -15.897 -17.303 1.010   1.00 39.94  ?  104 GLN   A CA   1 
ATOM   765  C  C    . GLN   A 1 102 ? -16.168 -17.070 2.496   1.00 38.82  ?  104 GLN   A C    1 
ATOM   766  O  O    . GLN   A 1 102 ? -16.717 -16.035 2.881   1.00 40.00  ?  104 GLN   A O    1 
ATOM   767  C  CB   . GLN   A 1 102 ? -17.197 -17.698 0.373   1.00 46.44  ?  104 GLN   A CB   1 
ATOM   768  C  CG   . GLN   A 1 102 ? -17.171 -17.575 -1.133  1.00 52.54  ?  104 GLN   A CG   1 
ATOM   769  C  CD   . GLN   A 1 102 ? -18.176 -18.486 -1.773  1.00 56.43  ?  104 GLN   A CD   1 
ATOM   770  O  OE1  . GLN   A 1 102 ? -18.780 -19.320 -1.100  1.00 60.97  ?  104 GLN   A OE1  1 
ATOM   771  N  NE2  . GLN   A 1 102 ? -18.356 -18.346 -3.083  1.00 58.80  ?  104 GLN   A NE2  1 
ATOM   772  N  N    . HIS   A 1 103 ? -15.763 -18.021 3.327   1.00 39.97  ?  105 HIS   A N    1 
ATOM   773  C  CA   . HIS   A 1 103 ? -16.094 -18.043 4.741   1.00 37.10  ?  105 HIS   A CA   1 
ATOM   774  C  C    . HIS   A 1 103 ? -14.954 -17.638 5.686   1.00 38.67  ?  105 HIS   A C    1 
ATOM   775  O  O    . HIS   A 1 103 ? -15.057 -17.849 6.884   1.00 41.30  ?  105 HIS   A O    1 
ATOM   776  C  CB   . HIS   A 1 103 ? -16.667 -19.428 5.062   1.00 39.20  ?  105 HIS   A CB   1 
ATOM   777  C  CG   . HIS   A 1 103 ? -18.013 -19.663 4.446   1.00 41.55  ?  105 HIS   A CG   1 
ATOM   778  N  ND1  . HIS   A 1 103 ? -18.236 -20.590 3.452   1.00 45.11  ?  105 HIS   A ND1  1 
ATOM   779  C  CD2  . HIS   A 1 103 ? -19.203 -19.057 4.664   1.00 42.34  ?  105 HIS   A CD2  1 
ATOM   780  C  CE1  . HIS   A 1 103 ? -19.502 -20.545 3.084   1.00 44.09  ?  105 HIS   A CE1  1 
ATOM   781  N  NE2  . HIS   A 1 103 ? -20.114 -19.635 3.816   1.00 42.79  ?  105 HIS   A NE2  1 
ATOM   782  N  N    . LYS   A 1 104 ? -13.874 -17.050 5.170   1.00 38.36  ?  106 LYS   A N    1 
ATOM   783  C  CA   . LYS   A 1 104 ? -13.004 -16.249 6.023   1.00 38.48  ?  106 LYS   A CA   1 
ATOM   784  C  C    . LYS   A 1 104 ? -13.746 -14.976 6.328   1.00 42.13  ?  106 LYS   A C    1 
ATOM   785  O  O    . LYS   A 1 104 ? -14.481 -14.485 5.479   1.00 41.34  ?  106 LYS   A O    1 
ATOM   786  C  CB   . LYS   A 1 104 ? -11.738 -15.805 5.314   1.00 37.61  ?  106 LYS   A CB   1 
ATOM   787  C  CG   . LYS   A 1 104 ? -10.717 -16.854 5.013   1.00 37.53  ?  106 LYS   A CG   1 
ATOM   788  C  CD   . LYS   A 1 104 ? -9.708  -16.302 4.016   1.00 36.87  ?  106 LYS   A CD   1 
ATOM   789  C  CE   . LYS   A 1 104 ? -8.316  -16.727 4.406   1.00 38.08  ?  106 LYS   A CE   1 
ATOM   790  N  NZ   . LYS   A 1 104 ? -7.296  -16.402 3.394   1.00 39.28  ?  106 LYS   A NZ   1 
ATOM   791  N  N    . ASP   A 1 105 ? -13.507 -14.431 7.515   1.00 49.89  ?  107 ASP   A N    1 
ATOM   792  C  CA   . ASP   A 1 105 ? -13.978 -13.112 7.897   1.00 57.34  ?  107 ASP   A CA   1 
ATOM   793  C  C    . ASP   A 1 105 ? -12.810 -12.143 7.779   1.00 60.13  ?  107 ASP   A C    1 
ATOM   794  O  O    . ASP   A 1 105 ? -11.818 -12.277 8.512   1.00 63.81  ?  107 ASP   A O    1 
ATOM   795  C  CB   . ASP   A 1 105 ? -14.526 -13.134 9.340   1.00 62.38  ?  107 ASP   A CB   1 
ATOM   796  C  CG   . ASP   A 1 105 ? -14.834 -11.731 9.892   1.00 65.23  ?  107 ASP   A CG   1 
ATOM   797  O  OD1  . ASP   A 1 105 ? -15.407 -10.892 9.160   1.00 67.65  ?  107 ASP   A OD1  1 
ATOM   798  O  OD2  . ASP   A 1 105 ? -14.495 -11.469 11.066  1.00 67.13  ?  107 ASP   A OD2  1 
ATOM   799  N  N    . ASP   A 1 106 ? -12.931 -11.189 6.852   1.00 61.10  ?  108 ASP   A N    1 
ATOM   800  C  CA   . ASP   A 1 106 ? -12.037 -10.022 6.793   1.00 63.71  ?  108 ASP   A CA   1 
ATOM   801  C  C    . ASP   A 1 106 ? -12.302 -9.165  8.012   1.00 66.30  ?  108 ASP   A C    1 
ATOM   802  O  O    . ASP   A 1 106 ? -13.371 -8.569  8.123   1.00 74.89  ?  108 ASP   A O    1 
ATOM   803  C  CB   . ASP   A 1 106 ? -12.271 -9.169  5.539   1.00 59.98  ?  108 ASP   A CB   1 
ATOM   804  N  N    . ASN   A 1 107 ? -11.341 -9.133  8.935   1.00 71.66  ?  109 ASN   A N    1 
ATOM   805  C  CA   . ASN   A 1 107 ? -11.402 -8.281  10.133  1.00 71.15  ?  109 ASN   A CA   1 
ATOM   806  C  C    . ASN   A 1 107 ? -12.368 -8.849  11.197  1.00 70.22  ?  109 ASN   A C    1 
ATOM   807  O  O    . ASN   A 1 107 ? -13.590 -8.638  11.122  1.00 68.46  ?  109 ASN   A O    1 
ATOM   808  C  CB   . ASN   A 1 107 ? -11.754 -6.826  9.758   1.00 70.68  ?  109 ASN   A CB   1 
ATOM   809  C  CG   . ASN   A 1 107 ? -11.125 -5.816  10.687  1.00 65.75  ?  109 ASN   A CG   1 
ATOM   810  O  OD1  . ASN   A 1 107 ? -11.223 -5.935  11.905  1.00 68.25  ?  109 ASN   A OD1  1 
ATOM   811  N  ND2  . ASN   A 1 107 ? -10.484 -4.810  10.117  1.00 57.06  ?  109 ASN   A ND2  1 
ATOM   812  N  N    . PRO   A 1 108 ? -11.817 -9.608  12.169  1.00 64.49  ?  110 PRO   A N    1 
ATOM   813  C  CA   . PRO   A 1 108 ? -12.572 -10.067 13.343  1.00 65.15  ?  110 PRO   A CA   1 
ATOM   814  C  C    . PRO   A 1 108 ? -12.451 -9.144  14.572  1.00 59.45  ?  110 PRO   A C    1 
ATOM   815  O  O    . PRO   A 1 108 ? -11.487 -8.382  14.700  1.00 53.39  ?  110 PRO   A O    1 
ATOM   816  C  CB   . PRO   A 1 108 ? -11.949 -11.440 13.639  1.00 63.94  ?  110 PRO   A CB   1 
ATOM   817  C  CG   . PRO   A 1 108 ? -10.541 -11.318 13.165  1.00 65.52  ?  110 PRO   A CG   1 
ATOM   818  C  CD   . PRO   A 1 108 ? -10.502 -10.273 12.077  1.00 64.72  ?  110 PRO   A CD   1 
ATOM   819  N  N    . ASN   A 1 109 ? -13.443 -9.219  15.458  1.00 56.97  ?  111 ASN   A N    1 
ATOM   820  C  CA   . ASN   A 1 109 ? -13.371 -8.560  16.763  1.00 51.32  ?  111 ASN   A CA   1 
ATOM   821  C  C    . ASN   A 1 109 ? -12.298 -9.280  17.551  1.00 43.34  ?  111 ASN   A C    1 
ATOM   822  O  O    . ASN   A 1 109 ? -12.579 -10.301 18.183  1.00 41.91  ?  111 ASN   A O    1 
ATOM   823  C  CB   . ASN   A 1 109 ? -14.700 -8.658  17.516  1.00 51.57  ?  111 ASN   A CB   1 
ATOM   824  N  N    . LEU   A 1 110 ? -11.056 -8.804  17.414  1.00 38.09  ?  112 LEU   A N    1 
ATOM   825  C  CA   . LEU   A 1 110 ? -9.961  -9.244  18.267  1.00 33.01  ?  112 LEU   A CA   1 
ATOM   826  C  C    . LEU   A 1 110 ? -9.354  -8.019  18.889  1.00 32.58  ?  112 LEU   A C    1 
ATOM   827  O  O    . LEU   A 1 110 ? -9.244  -6.966  18.251  1.00 31.65  ?  112 LEU   A O    1 
ATOM   828  C  CB   . LEU   A 1 110 ? -8.884  -10.045 17.523  1.00 33.47  ?  112 LEU   A CB   1 
ATOM   829  C  CG   . LEU   A 1 110 ? -9.199  -11.535 17.273  1.00 32.72  ?  112 LEU   A CG   1 
ATOM   830  C  CD1  . LEU   A 1 110 ? -8.130  -12.153 16.397  1.00 32.90  ?  112 LEU   A CD1  1 
ATOM   831  C  CD2  . LEU   A 1 110 ? -9.347  -12.317 18.567  1.00 34.00  ?  112 LEU   A CD2  1 
ATOM   832  N  N    . PRO   A 1 111 ? -8.956  -8.151  20.145  1.00 29.10  ?  113 PRO   A N    1 
ATOM   833  C  CA   . PRO   A 1 111 ? -8.405  -7.015  20.814  1.00 30.99  ?  113 PRO   A CA   1 
ATOM   834  C  C    . PRO   A 1 111 ? -7.057  -6.568  20.218  1.00 33.70  ?  113 PRO   A C    1 
ATOM   835  O  O    . PRO   A 1 111 ? -6.257  -7.391  19.745  1.00 31.55  ?  113 PRO   A O    1 
ATOM   836  C  CB   . PRO   A 1 111 ? -8.240  -7.504  22.269  1.00 30.71  ?  113 PRO   A CB   1 
ATOM   837  C  CG   . PRO   A 1 111 ? -8.329  -8.992  22.230  1.00 31.15  ?  113 PRO   A CG   1 
ATOM   838  C  CD   . PRO   A 1 111 ? -9.152  -9.322  21.029  1.00 29.19  ?  113 PRO   A CD   1 
ATOM   839  N  N    . ARG   A 1 112 ? -6.809  -5.267  20.253  1.00 34.46  ?  114 ARG   A N    1 
ATOM   840  C  CA   . ARG   A 1 112 ? -5.558  -4.696  19.745  1.00 39.26  ?  114 ARG   A CA   1 
ATOM   841  C  C    . ARG   A 1 112 ? -4.352  -5.405  20.406  1.00 39.87  ?  114 ARG   A C    1 
ATOM   842  O  O    . ARG   A 1 112 ? -4.427  -5.797  21.562  1.00 36.48  ?  114 ARG   A O    1 
ATOM   843  C  CB   . ARG   A 1 112 ? -5.530  -3.152  19.932  1.00 43.14  ?  114 ARG   A CB   1 
ATOM   844  C  CG   . ARG   A 1 112 ? -4.482  -2.567  20.876  1.00 44.42  ?  114 ARG   A CG   1 
ATOM   845  C  CD   . ARG   A 1 112 ? -4.983  -1.342  21.659  1.00 48.53  ?  114 ARG   A CD   1 
ATOM   846  N  NE   . ARG   A 1 112 ? -4.072  -0.191  21.697  1.00 51.89  ?  114 ARG   A NE   1 
ATOM   847  C  CZ   . ARG   A 1 112 ? -2.776  -0.193  22.061  1.00 56.55  ?  114 ARG   A CZ   1 
ATOM   848  N  NH1  . ARG   A 1 112 ? -2.130  -1.302  22.402  1.00 55.32  ?  114 ARG   A NH1  1 
ATOM   849  N  NH2  . ARG   A 1 112 ? -2.091  0.954   22.046  1.00 59.08  ?  114 ARG   A NH2  1 
ATOM   850  N  N    . LEU   A 1 113 ? -3.285  -5.623  19.635  1.00 40.68  ?  115 LEU   A N    1 
ATOM   851  C  CA   . LEU   A 1 113 ? -2.042  -6.185  20.167  1.00 40.86  ?  115 LEU   A CA   1 
ATOM   852  C  C    . LEU   A 1 113 ? -1.250  -5.103  20.879  1.00 39.96  ?  115 LEU   A C    1 
ATOM   853  O  O    . LEU   A 1 113 ? -0.625  -4.266  20.227  1.00 41.93  ?  115 LEU   A O    1 
ATOM   854  C  CB   . LEU   A 1 113 ? -1.175  -6.827  19.057  1.00 37.17  ?  115 LEU   A CB   1 
ATOM   855  C  CG   . LEU   A 1 113 ? -1.496  -8.266  18.632  1.00 36.68  ?  115 LEU   A CG   1 
ATOM   856  C  CD1  . LEU   A 1 113 ? -0.462  -8.696  17.606  1.00 35.40  ?  115 LEU   A CD1  1 
ATOM   857  C  CD2  . LEU   A 1 113 ? -1.538  -9.244  19.810  1.00 35.28  ?  115 LEU   A CD2  1 
ATOM   858  N  N    . VAL   A 1 114 ? -1.276  -5.140  22.210  1.00 41.39  ?  116 VAL   A N    1 
ATOM   859  C  CA   . VAL   A 1 114 ? -0.433  -4.260  23.038  1.00 40.81  ?  116 VAL   A CA   1 
ATOM   860  C  C    . VAL   A 1 114 ? 1.047   -4.613  22.848  1.00 35.77  ?  116 VAL   A C    1 
ATOM   861  O  O    . VAL   A 1 114 ? 1.411   -5.768  22.901  1.00 35.33  ?  116 VAL   A O    1 
ATOM   862  C  CB   . VAL   A 1 114 ? -0.796  -4.256  24.590  1.00 44.92  ?  116 VAL   A CB   1 
ATOM   863  C  CG1  . VAL   A 1 114 ? -1.879  -3.233  24.906  1.00 46.66  ?  116 VAL   A CG1  1 
ATOM   864  C  CG2  . VAL   A 1 114 ? -1.176  -5.632  25.152  1.00 43.80  ?  116 VAL   A CG2  1 
ATOM   865  N  N    . ARG   A 1 115 ? 1.874   -3.606  22.602  1.00 33.34  ?  117 ARG   A N    1 
ATOM   866  C  CA   . ARG   A 1 115 ? 3.338   -3.747  22.570  1.00 33.99  ?  117 ARG   A CA   1 
ATOM   867  C  C    . ARG   A 1 115 ? 3.834   -3.845  24.010  1.00 32.23  ?  117 ARG   A C    1 
ATOM   868  O  O    . ARG   A 1 115 ? 3.734   -2.870  24.715  1.00 32.74  ?  117 ARG   A O    1 
ATOM   869  C  CB   . ARG   A 1 115 ? 3.961   -2.513  21.873  1.00 36.29  ?  117 ARG   A CB   1 
ATOM   870  C  CG   . ARG   A 1 115 ? 5.473   -2.308  21.997  1.00 40.27  ?  117 ARG   A CG   1 
ATOM   871  C  CD   . ARG   A 1 115 ? 5.984   -1.098  21.196  1.00 42.28  ?  117 ARG   A CD   1 
ATOM   872  N  NE   . ARG   A 1 115 ? 5.673   -1.228  19.762  1.00 43.00  ?  117 ARG   A NE   1 
ATOM   873  C  CZ   . ARG   A 1 115 ? 6.015   -0.365  18.808  1.00 41.12  ?  117 ARG   A CZ   1 
ATOM   874  N  NH1  . ARG   A 1 115 ? 6.719   0.729   19.081  1.00 45.54  ?  117 ARG   A NH1  1 
ATOM   875  N  NH2  . ARG   A 1 115 ? 5.649   -0.611  17.562  1.00 41.89  ?  117 ARG   A NH2  1 
ATOM   876  N  N    . PRO   A 1 116 ? 4.357   -5.010  24.451  1.00 31.21  ?  118 PRO   A N    1 
ATOM   877  C  CA   . PRO   A 1 116 ? 4.931   -5.094  25.794  1.00 31.46  ?  118 PRO   A CA   1 
ATOM   878  C  C    . PRO   A 1 116 ? 6.172   -4.234  26.011  1.00 33.59  ?  118 PRO   A C    1 
ATOM   879  O  O    . PRO   A 1 116 ? 6.710   -3.650  25.063  1.00 31.18  ?  118 PRO   A O    1 
ATOM   880  C  CB   . PRO   A 1 116 ? 5.298   -6.579  25.948  1.00 30.13  ?  118 PRO   A CB   1 
ATOM   881  C  CG   . PRO   A 1 116 ? 4.487   -7.303  24.931  1.00 31.37  ?  118 PRO   A CG   1 
ATOM   882  C  CD   . PRO   A 1 116 ? 4.390   -6.324  23.778  1.00 32.62  ?  118 PRO   A CD   1 
ATOM   883  N  N    . GLU   A 1 117 ? 6.604   -4.139  27.268  1.00 35.20  ?  119 GLU   A N    1 
ATOM   884  C  CA   . GLU   A 1 117 ? 7.805   -3.369  27.607  1.00 34.47  ?  119 GLU   A CA   1 
ATOM   885  C  C    . GLU   A 1 117 ? 8.986   -4.020  26.913  1.00 35.77  ?  119 GLU   A C    1 
ATOM   886  O  O    . GLU   A 1 117 ? 9.046   -5.267  26.794  1.00 32.37  ?  119 GLU   A O    1 
ATOM   887  C  CB   . GLU   A 1 117 ? 8.035   -3.330  29.128  1.00 34.75  ?  119 GLU   A CB   1 
ATOM   888  N  N    . VAL   A 1 118 ? 9.911   -3.185  26.441  1.00 33.87  ?  120 VAL   A N    1 
ATOM   889  C  CA   . VAL   A 1 118 ? 11.165  -3.677  25.825  1.00 34.08  ?  120 VAL   A CA   1 
ATOM   890  C  C    . VAL   A 1 118 ? 11.836  -4.840  26.572  1.00 34.48  ?  120 VAL   A C    1 
ATOM   891  O  O    . VAL   A 1 118 ? 12.315  -5.781  25.929  1.00 29.73  ?  120 VAL   A O    1 
ATOM   892  C  CB   . VAL   A 1 118 ? 12.165  -2.533  25.587  1.00 32.93  ?  120 VAL   A CB   1 
ATOM   893  C  CG1  . VAL   A 1 118 ? 13.570  -3.053  25.355  1.00 30.89  ?  120 VAL   A CG1  1 
ATOM   894  C  CG2  . VAL   A 1 118 ? 11.695  -1.713  24.398  1.00 36.56  ?  120 VAL   A CG2  1 
ATOM   895  N  N    . ASP   A 1 119 ? 11.855  -4.771  27.913  1.00 34.97  ?  121 ASP   A N    1 
ATOM   896  C  CA   . ASP   A 1 119 ? 12.533  -5.781  28.770  1.00 33.27  ?  121 ASP   A CA   1 
ATOM   897  C  C    . ASP   A 1 119 ? 11.791  -7.143  28.864  1.00 29.47  ?  121 ASP   A C    1 
ATOM   898  O  O    . ASP   A 1 119 ? 12.430  -8.227  28.981  1.00 25.82  ?  121 ASP   A O    1 
ATOM   899  C  CB   . ASP   A 1 119 ? 12.747  -5.200  30.172  1.00 36.29  ?  121 ASP   A CB   1 
ATOM   900  C  CG   . ASP   A 1 119 ? 13.466  -3.839  30.142  1.00 46.57  ?  121 ASP   A CG   1 
ATOM   901  O  OD1  . ASP   A 1 119 ? 12.790  -2.798  29.864  1.00 50.17  ?  121 ASP   A OD1  1 
ATOM   902  O  OD2  . ASP   A 1 119 ? 14.707  -3.813  30.395  1.00 52.04  ?  121 ASP   A OD2  1 
ATOM   903  N  N    . VAL   A 1 120 ? 10.457  -7.061  28.848  1.00 26.74  ?  122 VAL   A N    1 
ATOM   904  C  CA   . VAL   A 1 120 ? 9.561   -8.235  28.849  1.00 30.01  ?  122 VAL   A CA   1 
ATOM   905  C  C    . VAL   A 1 120 ? 9.712   -8.945  27.520  1.00 30.84  ?  122 VAL   A C    1 
ATOM   906  O  O    . VAL   A 1 120 ? 9.999   -10.144 27.521  1.00 32.49  ?  122 VAL   A O    1 
ATOM   907  C  CB   . VAL   A 1 120 ? 8.066   -7.852  29.071  1.00 28.35  ?  122 VAL   A CB   1 
ATOM   908  C  CG1  . VAL   A 1 120 ? 7.119   -8.984  28.688  1.00 28.57  ?  122 VAL   A CG1  1 
ATOM   909  C  CG2  . VAL   A 1 120 ? 7.851   -7.450  30.522  1.00 27.82  ?  122 VAL   A CG2  1 
ATOM   910  N  N    . MET   A 1 121 ? 9.543   -8.195  26.419  1.00 30.48  ?  123 MET   A N    1 
ATOM   911  C  CA   . MET   A 1 121 ? 9.803   -8.703  25.033  1.00 33.56  ?  123 MET   A CA   1 
ATOM   912  C  C    . MET   A 1 121 ? 11.194  -9.368  24.887  1.00 34.11  ?  123 MET   A C    1 
ATOM   913  O  O    . MET   A 1 121 ? 11.299  -10.519 24.397  1.00 30.57  ?  123 MET   A O    1 
ATOM   914  C  CB   . MET   A 1 121 ? 9.660   -7.574  23.982  1.00 36.25  ?  123 MET   A CB   1 
ATOM   915  C  CG   . MET   A 1 121 ? 8.225   -7.273  23.577  1.00 39.73  ?  123 MET   A CG   1 
ATOM   916  S  SD   . MET   A 1 121 ? 7.922   -6.138  22.191  1.00 40.68  ?  123 MET   A SD   1 
ATOM   917  C  CE   . MET   A 1 121 ? 9.039   -4.774  22.493  1.00 42.54  ?  123 MET   A CE   1 
ATOM   918  N  N    . CYS   A 1 122 ? 12.248  -8.661  25.331  1.00 32.70  ?  124 CYS   A N    1 
ATOM   919  C  CA   . CYS   A 1 122 ? 13.644  -9.174  25.161  1.00 30.68  ?  124 CYS   A CA   1 
ATOM   920  C  C    . CYS   A 1 122 ? 13.910  -10.440 25.942  1.00 28.02  ?  124 CYS   A C    1 
ATOM   921  O  O    . CYS   A 1 122 ? 14.546  -11.347 25.447  1.00 29.62  ?  124 CYS   A O    1 
ATOM   922  C  CB   . CYS   A 1 122 ? 14.690  -8.123  25.463  1.00 27.74  ?  124 CYS   A CB   1 
ATOM   923  S  SG   . CYS   A 1 122 ? 14.885  -6.894  24.160  1.00 33.56  ?  124 CYS   A SG   1 
ATOM   924  N  N    . THR   A 1 123 ? 13.392  -10.517 27.154  1.00 31.03  ?  125 THR   A N    1 
ATOM   925  C  CA   . THR   A 1 123 ? 13.459  -11.751 27.922  1.00 30.95  ?  125 THR   A CA   1 
ATOM   926  C  C    . THR   A 1 123 ? 12.617  -12.882 27.295  1.00 30.33  ?  125 THR   A C    1 
ATOM   927  O  O    . THR   A 1 123 ? 13.010  -14.060 27.334  1.00 31.76  ?  125 THR   A O    1 
ATOM   928  C  CB   . THR   A 1 123 ? 12.974  -11.524 29.364  1.00 31.44  ?  125 THR   A CB   1 
ATOM   929  O  OG1  . THR   A 1 123 ? 13.709  -10.462 29.956  1.00 31.73  ?  125 THR   A OG1  1 
ATOM   930  C  CG2  . THR   A 1 123 ? 13.153  -12.789 30.202  1.00 32.74  ?  125 THR   A CG2  1 
ATOM   931  N  N    . ALA   A 1 124 ? 11.446  -12.533 26.779  1.00 30.97  ?  126 ALA   A N    1 
ATOM   932  C  CA   . ALA   A 1 124 ? 10.561  -13.515 26.118  1.00 32.79  ?  126 ALA   A CA   1 
ATOM   933  C  C    . ALA   A 1 124 ? 11.262  -14.151 24.948  1.00 29.80  ?  126 ALA   A C    1 
ATOM   934  O  O    . ALA   A 1 124 ? 11.326  -15.351 24.851  1.00 24.80  ?  126 ALA   A O    1 
ATOM   935  C  CB   . ALA   A 1 124 ? 9.272   -12.860 25.655  1.00 32.94  ?  126 ALA   A CB   1 
ATOM   936  N  N    . PHE   A 1 125 ? 11.803  -13.297 24.093  1.00 32.04  ?  127 PHE   A N    1 
ATOM   937  C  CA   . PHE   A 1 125 ? 12.675  -13.688 22.978  1.00 35.38  ?  127 PHE   A CA   1 
ATOM   938  C  C    . PHE   A 1 125 ? 13.838  -14.595 23.370  1.00 36.30  ?  127 PHE   A C    1 
ATOM   939  O  O    . PHE   A 1 125 ? 14.088  -15.625 22.712  1.00 32.61  ?  127 PHE   A O    1 
ATOM   940  C  CB   . PHE   A 1 125 ? 13.256  -12.428 22.339  1.00 36.14  ?  127 PHE   A CB   1 
ATOM   941  C  CG   . PHE   A 1 125 ? 14.050  -12.684 21.107  1.00 37.15  ?  127 PHE   A CG   1 
ATOM   942  C  CD1  . PHE   A 1 125 ? 13.416  -12.815 19.878  1.00 37.69  ?  127 PHE   A CD1  1 
ATOM   943  C  CD2  . PHE   A 1 125 ? 15.445  -12.766 21.160  1.00 40.18  ?  127 PHE   A CD2  1 
ATOM   944  C  CE1  . PHE   A 1 125 ? 14.148  -13.042 18.729  1.00 37.66  ?  127 PHE   A CE1  1 
ATOM   945  C  CE2  . PHE   A 1 125 ? 16.184  -13.000 20.011  1.00 38.01  ?  127 PHE   A CE2  1 
ATOM   946  C  CZ   . PHE   A 1 125 ? 15.534  -13.134 18.795  1.00 37.81  ?  127 PHE   A CZ   1 
ATOM   947  N  N    . HIS   A 1 126 ? 14.567  -14.209 24.422  1.00 38.94  ?  128 HIS   A N    1 
ATOM   948  C  CA   . HIS   A 1 126 ? 15.758  -14.978 24.813  1.00 39.93  ?  128 HIS   A CA   1 
ATOM   949  C  C    . HIS   A 1 126 ? 15.368  -16.331 25.403  1.00 38.78  ?  128 HIS   A C    1 
ATOM   950  O  O    . HIS   A 1 126 ? 15.978  -17.328 25.071  1.00 40.53  ?  128 HIS   A O    1 
ATOM   951  C  CB   . HIS   A 1 126 ? 16.675  -14.204 25.770  1.00 41.46  ?  128 HIS   A CB   1 
ATOM   952  C  CG   . HIS   A 1 126 ? 17.936  -14.944 26.114  1.00 47.98  ?  128 HIS   A CG   1 
ATOM   953  N  ND1  . HIS   A 1 126 ? 18.003  -15.873 27.141  1.00 47.97  ?  128 HIS   A ND1  1 
ATOM   954  C  CD2  . HIS   A 1 126 ? 19.170  -14.919 25.549  1.00 48.25  ?  128 HIS   A CD2  1 
ATOM   955  C  CE1  . HIS   A 1 126 ? 19.223  -16.380 27.193  1.00 47.54  ?  128 HIS   A CE1  1 
ATOM   956  N  NE2  . HIS   A 1 126 ? 19.948  -15.821 26.237  1.00 46.87  ?  128 HIS   A NE2  1 
ATOM   957  N  N    . ASP   A 1 127 ? 14.361  -16.372 26.276  1.00 46.26  ?  129 ASP   A N    1 
ATOM   958  C  CA   . ASP   A 1 127 ? 13.983  -17.624 26.963  1.00 46.50  ?  129 ASP   A CA   1 
ATOM   959  C  C    . ASP   A 1 127 ? 13.502  -18.650 25.941  1.00 47.90  ?  129 ASP   A C    1 
ATOM   960  O  O    . ASP   A 1 127 ? 14.175  -19.675 25.732  1.00 49.36  ?  129 ASP   A O    1 
ATOM   961  C  CB   . ASP   A 1 127 ? 12.929  -17.390 28.053  1.00 46.16  ?  129 ASP   A CB   1 
ATOM   962  C  CG   . ASP   A 1 127 ? 13.487  -16.690 29.300  1.00 48.05  ?  129 ASP   A CG   1 
ATOM   963  O  OD1  . ASP   A 1 127 ? 14.700  -16.395 29.391  1.00 44.53  ?  129 ASP   A OD1  1 
ATOM   964  O  OD2  . ASP   A 1 127 ? 12.675  -16.413 30.209  1.00 54.25  ?  129 ASP   A OD2  1 
ATOM   965  N  N    . ASN   A 1 128 ? 12.399  -18.341 25.251  1.00 45.53  ?  130 ASN   A N    1 
ATOM   966  C  CA   . ASN   A 1 128 ? 11.893  -19.218 24.189  1.00 40.85  ?  130 ASN   A CA   1 
ATOM   967  C  C    . ASN   A 1 128 ? 11.608  -18.429 22.910  1.00 36.79  ?  130 ASN   A C    1 
ATOM   968  O  O    . ASN   A 1 128 ? 10.507  -17.932 22.692  1.00 35.01  ?  130 ASN   A O    1 
ATOM   969  C  CB   . ASN   A 1 128 ? 10.681  -19.999 24.685  1.00 39.58  ?  130 ASN   A CB   1 
ATOM   970  C  CG   . ASN   A 1 128 ? 10.434  -21.243 23.863  1.00 42.73  ?  130 ASN   A CG   1 
ATOM   971  O  OD1  . ASN   A 1 128 ? 10.388  -21.179 22.630  1.00 45.96  ?  130 ASN   A OD1  1 
ATOM   972  N  ND2  . ASN   A 1 128 ? 10.283  -22.391 24.531  1.00 41.17  ?  130 ASN   A ND2  1 
ATOM   973  N  N    . GLU   A 1 129 ? 12.627  -18.325 22.063  1.00 34.39  ?  131 GLU   A N    1 
ATOM   974  C  CA   . GLU   A 1 129 ? 12.542  -17.539 20.817  1.00 36.56  ?  131 GLU   A CA   1 
ATOM   975  C  C    . GLU   A 1 129 ? 11.422  -18.037 19.877  1.00 33.46  ?  131 GLU   A C    1 
ATOM   976  O  O    . GLU   A 1 129 ? 10.649  -17.243 19.342  1.00 27.54  ?  131 GLU   A O    1 
ATOM   977  C  CB   . GLU   A 1 129 ? 13.888  -17.624 20.109  1.00 38.38  ?  131 GLU   A CB   1 
ATOM   978  C  CG   . GLU   A 1 129 ? 14.231  -16.584 19.053  1.00 42.22  ?  131 GLU   A CG   1 
ATOM   979  C  CD   . GLU   A 1 129 ? 15.648  -16.846 18.485  1.00 43.09  ?  131 GLU   A CD   1 
ATOM   980  O  OE1  . GLU   A 1 129 ? 16.094  -18.025 18.470  1.00 43.46  ?  131 GLU   A OE1  1 
ATOM   981  O  OE2  . GLU   A 1 129 ? 16.340  -15.887 18.087  1.00 39.95  ?  131 GLU   A OE2  1 
ATOM   982  N  N    . GLU   A 1 130 ? 11.320  -19.352 19.730  1.00 33.14  ?  132 GLU   A N    1 
ATOM   983  C  CA   . GLU   A 1 130 ? 10.421  -19.896 18.740  1.00 36.66  ?  132 GLU   A CA   1 
ATOM   984  C  C    . GLU   A 1 130 ? 8.973   -19.574 19.070  1.00 35.19  ?  132 GLU   A C    1 
ATOM   985  O  O    . GLU   A 1 130 ? 8.252   -19.096 18.195  1.00 37.38  ?  132 GLU   A O    1 
ATOM   986  C  CB   . GLU   A 1 130 ? 10.622  -21.385 18.500  1.00 38.95  ?  132 GLU   A CB   1 
ATOM   987  C  CG   . GLU   A 1 130 ? 10.291  -21.729 17.046  1.00 46.81  ?  132 GLU   A CG   1 
ATOM   988  C  CD   . GLU   A 1 130 ? 10.349  -23.208 16.710  1.00 49.68  ?  132 GLU   A CD   1 
ATOM   989  O  OE1  . GLU   A 1 130 ? 11.029  -23.990 17.428  1.00 54.18  ?  132 GLU   A OE1  1 
ATOM   990  O  OE2  . GLU   A 1 130 ? 9.704   -23.579 15.707  1.00 54.50  ?  132 GLU   A OE2  1 
ATOM   991  N  N    . THR   A 1 131 ? 8.553   -19.776 20.321  1.00 37.38  ?  133 THR   A N    1 
ATOM   992  C  CA   . THR   A 1 131 ? 7.136   -19.525 20.681  1.00 34.70  ?  133 THR   A CA   1 
ATOM   993  C  C    . THR   A 1 131 ? 6.817   -18.041 20.810  1.00 31.50  ?  133 THR   A C    1 
ATOM   994  O  O    . THR   A 1 131 ? 5.673   -17.628 20.548  1.00 34.35  ?  133 THR   A O    1 
ATOM   995  C  CB   . THR   A 1 131 ? 6.671   -20.319 21.905  1.00 34.50  ?  133 THR   A CB   1 
ATOM   996  O  OG1  . THR   A 1 131 ? 7.473   -19.973 23.020  1.00 41.25  ?  133 THR   A OG1  1 
ATOM   997  C  CG2  . THR   A 1 131 ? 6.775   -21.810 21.645  1.00 34.29  ?  133 THR   A CG2  1 
ATOM   998  N  N    . PHE   A 1 132 ? 7.813   -17.230 21.145  1.00 27.99  ?  134 PHE   A N    1 
ATOM   999  C  CA   . PHE   A 1 132 ? 7.644   -15.772 21.151  1.00 26.27  ?  134 PHE   A CA   1 
ATOM   1000 C  C    . PHE   A 1 132 ? 7.327   -15.294 19.745  1.00 26.36  ?  134 PHE   A C    1 
ATOM   1001 O  O    . PHE   A 1 132 ? 6.263   -14.769 19.522  1.00 30.30  ?  134 PHE   A O    1 
ATOM   1002 C  CB   . PHE   A 1 132 ? 8.865   -15.071 21.731  1.00 25.72  ?  134 PHE   A CB   1 
ATOM   1003 C  CG   . PHE   A 1 132 ? 8.794   -13.574 21.664  1.00 26.63  ?  134 PHE   A CG   1 
ATOM   1004 C  CD1  . PHE   A 1 132 ? 7.899   -12.884 22.440  1.00 27.56  ?  134 PHE   A CD1  1 
ATOM   1005 C  CD2  . PHE   A 1 132 ? 9.604   -12.861 20.783  1.00 27.26  ?  134 PHE   A CD2  1 
ATOM   1006 C  CE1  . PHE   A 1 132 ? 7.810   -11.494 22.356  1.00 27.45  ?  134 PHE   A CE1  1 
ATOM   1007 C  CE2  . PHE   A 1 132 ? 9.525   -11.491 20.692  1.00 26.07  ?  134 PHE   A CE2  1 
ATOM   1008 C  CZ   . PHE   A 1 132 ? 8.642   -10.805 21.495  1.00 27.01  ?  134 PHE   A CZ   1 
ATOM   1009 N  N    . LEU   A 1 133 ? 8.192   -15.560 18.773  1.00 28.06  ?  135 LEU   A N    1 
ATOM   1010 C  CA   . LEU   A 1 133 ? 7.933   -15.146 17.380  1.00 25.60  ?  135 LEU   A CA   1 
ATOM   1011 C  C    . LEU   A 1 133 ? 6.689   -15.815 16.767  1.00 25.37  ?  135 LEU   A C    1 
ATOM   1012 O  O    . LEU   A 1 133 ? 5.850   -15.142 16.183  1.00 24.82  ?  135 LEU   A O    1 
ATOM   1013 C  CB   . LEU   A 1 133 ? 9.141   -15.401 16.500  1.00 24.12  ?  135 LEU   A CB   1 
ATOM   1014 C  CG   . LEU   A 1 133 ? 10.443  -14.674 16.820  1.00 23.71  ?  135 LEU   A CG   1 
ATOM   1015 C  CD1  . LEU   A 1 133 ? 11.586  -15.320 16.035  1.00 22.65  ?  135 LEU   A CD1  1 
ATOM   1016 C  CD2  . LEU   A 1 133 ? 10.333  -13.192 16.550  1.00 23.78  ?  135 LEU   A CD2  1 
ATOM   1017 N  N    . LYS   A 1 134 ? 6.580   -17.124 16.928  1.00 25.22  ?  136 LYS   A N    1 
ATOM   1018 C  CA   . LYS   A 1 134 ? 5.431   -17.872 16.421  1.00 27.64  ?  136 LYS   A CA   1 
ATOM   1019 C  C    . LYS   A 1 134 ? 4.070   -17.443 16.952  1.00 25.68  ?  136 LYS   A C    1 
ATOM   1020 O  O    . LYS   A 1 134 ? 3.168   -17.243 16.174  1.00 24.86  ?  136 LYS   A O    1 
ATOM   1021 C  CB   . LYS   A 1 134 ? 5.602   -19.377 16.692  1.00 28.67  ?  136 LYS   A CB   1 
ATOM   1022 C  CG   . LYS   A 1 134 ? 6.676   -20.033 15.845  1.00 31.66  ?  136 LYS   A CG   1 
ATOM   1023 C  CD   . LYS   A 1 134 ? 6.129   -20.346 14.470  1.00 34.33  ?  136 LYS   A CD   1 
ATOM   1024 C  CE   . LYS   A 1 134 ? 7.228   -20.765 13.520  1.00 36.56  ?  136 LYS   A CE   1 
ATOM   1025 N  NZ   . LYS   A 1 134 ? 7.885   -22.005 13.985  1.00 37.99  ?  136 LYS   A NZ   1 
ATOM   1026 N  N    . LYS   A 1 135 ? 3.913   -17.352 18.267  1.00 25.51  ?  137 LYS   A N    1 
ATOM   1027 C  CA   . LYS   A 1 135 ? 2.691   -16.788 18.868  1.00 25.92  ?  137 LYS   A CA   1 
ATOM   1028 C  C    . LYS   A 1 135 ? 2.327   -15.466 18.236  1.00 26.05  ?  137 LYS   A C    1 
ATOM   1029 O  O    . LYS   A 1 135 ? 1.164   -15.272 17.813  1.00 25.59  ?  137 LYS   A O    1 
ATOM   1030 C  CB   . LYS   A 1 135 ? 2.797   -16.626 20.397  1.00 24.66  ?  137 LYS   A CB   1 
ATOM   1031 N  N    . TYR   A 1 136 ? 3.289   -14.568 18.095  1.00 26.15  ?  138 TYR   A N    1 
ATOM   1032 C  CA   . TYR   A 1 136 ? 2.953   -13.291 17.466  1.00 28.90  ?  138 TYR   A CA   1 
ATOM   1033 C  C    . TYR   A 1 136 ? 2.674   -13.431 15.952  1.00 27.89  ?  138 TYR   A C    1 
ATOM   1034 O  O    . TYR   A 1 136 ? 1.787   -12.740 15.436  1.00 26.28  ?  138 TYR   A O    1 
ATOM   1035 C  CB   . TYR   A 1 136 ? 4.007   -12.228 17.745  1.00 32.21  ?  138 TYR   A CB   1 
ATOM   1036 C  CG   . TYR   A 1 136 ? 3.791   -11.484 19.023  1.00 35.49  ?  138 TYR   A CG   1 
ATOM   1037 C  CD1  . TYR   A 1 136 ? 2.814   -10.491 19.110  1.00 37.90  ?  138 TYR   A CD1  1 
ATOM   1038 C  CD2  . TYR   A 1 136 ? 4.583   -11.739 20.160  1.00 37.22  ?  138 TYR   A CD2  1 
ATOM   1039 C  CE1  . TYR   A 1 136 ? 2.613   -9.795  20.307  1.00 40.01  ?  138 TYR   A CE1  1 
ATOM   1040 C  CE2  . TYR   A 1 136 ? 4.394   -11.045 21.343  1.00 35.12  ?  138 TYR   A CE2  1 
ATOM   1041 C  CZ   . TYR   A 1 136 ? 3.413   -10.074 21.411  1.00 37.28  ?  138 TYR   A CZ   1 
ATOM   1042 O  OH   . TYR   A 1 136 ? 3.212   -9.374  22.576  1.00 43.59  ?  138 TYR   A OH   1 
ATOM   1043 N  N    . LEU   A 1 137 ? 3.362   -14.359 15.275  1.00 24.85  ?  139 LEU   A N    1 
ATOM   1044 C  CA   . LEU   A 1 137 ? 3.029   -14.691 13.861  1.00 24.03  ?  139 LEU   A CA   1 
ATOM   1045 C  C    . LEU   A 1 137 ? 1.557   -15.127 13.694  1.00 23.49  ?  139 LEU   A C    1 
ATOM   1046 O  O    . LEU   A 1 137 ? 0.828   -14.603 12.845  1.00 20.80  ?  139 LEU   A O    1 
ATOM   1047 C  CB   . LEU   A 1 137 ? 3.942   -15.764 13.299  1.00 22.77  ?  139 LEU   A CB   1 
ATOM   1048 C  CG   . LEU   A 1 137 ? 3.805   -16.106 11.803  1.00 22.84  ?  139 LEU   A CG   1 
ATOM   1049 C  CD1  . LEU   A 1 137 ? 3.839   -14.886 10.893  1.00 23.16  ?  139 LEU   A CD1  1 
ATOM   1050 C  CD2  . LEU   A 1 137 ? 4.913   -17.057 11.403  1.00 23.12  ?  139 LEU   A CD2  1 
ATOM   1051 N  N    . TYR   A 1 138 ? 1.148   -16.052 14.544  1.00 23.71  ?  140 TYR   A N    1 
ATOM   1052 C  CA   . TYR   A 1 138 ? -0.265  -16.435 14.713  1.00 24.83  ?  140 TYR   A CA   1 
ATOM   1053 C  C    . TYR   A 1 138 ? -1.175  -15.220 14.976  1.00 24.86  ?  140 TYR   A C    1 
ATOM   1054 O  O    . TYR   A 1 138 ? -2.203  -15.063 14.319  1.00 24.64  ?  140 TYR   A O    1 
ATOM   1055 C  CB   . TYR   A 1 138 ? -0.384  -17.510 15.794  1.00 23.27  ?  140 TYR   A CB   1 
ATOM   1056 C  CG   . TYR   A 1 138 ? -1.684  -17.578 16.557  1.00 25.00  ?  140 TYR   A CG   1 
ATOM   1057 C  CD1  . TYR   A 1 138 ? -2.763  -18.252 16.044  1.00 26.28  ?  140 TYR   A CD1  1 
ATOM   1058 C  CD2  . TYR   A 1 138 ? -1.796  -17.054 17.847  1.00 26.45  ?  140 TYR   A CD2  1 
ATOM   1059 C  CE1  . TYR   A 1 138 ? -3.946  -18.349 16.738  1.00 26.63  ?  140 TYR   A CE1  1 
ATOM   1060 C  CE2  . TYR   A 1 138 ? -2.985  -17.164 18.554  1.00 27.25  ?  140 TYR   A CE2  1 
ATOM   1061 C  CZ   . TYR   A 1 138 ? -4.068  -17.818 17.970  1.00 27.48  ?  140 TYR   A CZ   1 
ATOM   1062 O  OH   . TYR   A 1 138 ? -5.306  -17.954 18.567  1.00 25.51  ?  140 TYR   A OH   1 
ATOM   1063 N  N    . GLU   A 1 139 ? -0.759  -14.346 15.877  1.00 25.57  ?  141 GLU   A N    1 
ATOM   1064 C  CA   . GLU   A 1 139 ? -1.574  -13.198 16.237  1.00 26.63  ?  141 GLU   A CA   1 
ATOM   1065 C  C    . GLU   A 1 139 ? -1.739  -12.252 15.080  1.00 26.53  ?  141 GLU   A C    1 
ATOM   1066 O  O    . GLU   A 1 139 ? -2.827  -11.767 14.888  1.00 29.78  ?  141 GLU   A O    1 
ATOM   1067 C  CB   . GLU   A 1 139 ? -1.053  -12.426 17.478  1.00 26.23  ?  141 GLU   A CB   1 
ATOM   1068 C  CG   . GLU   A 1 139 ? -1.056  -13.199 18.773  1.00 27.42  ?  141 GLU   A CG   1 
ATOM   1069 C  CD   . GLU   A 1 139 ? -2.408  -13.515 19.384  1.00 28.36  ?  141 GLU   A CD   1 
ATOM   1070 O  OE1  . GLU   A 1 139 ? -3.495  -13.279 18.809  1.00 29.06  ?  141 GLU   A OE1  1 
ATOM   1071 O  OE2  . GLU   A 1 139 ? -2.362  -14.025 20.511  1.00 33.54  ?  141 GLU   A OE2  1 
ATOM   1072 N  N    . ILE   A 1 140 ? -0.692  -11.988 14.308  1.00 26.38  ?  142 ILE   A N    1 
ATOM   1073 C  CA   . ILE   A 1 140 ? -0.838  -11.127 13.133  1.00 26.78  ?  142 ILE   A CA   1 
ATOM   1074 C  C    . ILE   A 1 140 ? -1.714  -11.802 12.066  1.00 25.95  ?  142 ILE   A C    1 
ATOM   1075 O  O    . ILE   A 1 140 ? -2.628  -11.194 11.561  1.00 23.04  ?  142 ILE   A O    1 
ATOM   1076 C  CB   . ILE   A 1 140 ? 0.497   -10.762 12.468  1.00 30.06  ?  142 ILE   A CB   1 
ATOM   1077 C  CG1  . ILE   A 1 140 ? 1.529   -10.210 13.467  1.00 35.68  ?  142 ILE   A CG1  1 
ATOM   1078 C  CG2  . ILE   A 1 140 ? 0.274   -9.741  11.361  1.00 32.70  ?  142 ILE   A CG2  1 
ATOM   1079 C  CD1  . ILE   A 1 140 ? 0.991   -9.420  14.636  1.00 36.65  ?  142 ILE   A CD1  1 
ATOM   1080 N  N    . ALA   A 1 141 ? -1.380  -13.047 11.719  1.00 23.87  ?  143 ALA   A N    1 
ATOM   1081 C  CA   . ALA   A 1 141 ? -2.057  -13.814 10.674  1.00 22.01  ?  143 ALA   A CA   1 
ATOM   1082 C  C    . ALA   A 1 141 ? -3.585  -13.834 10.845  1.00 20.94  ?  143 ALA   A C    1 
ATOM   1083 O  O    . ALA   A 1 141 ? -4.325  -13.600 9.879   1.00 17.60  ?  143 ALA   A O    1 
ATOM   1084 C  CB   . ALA   A 1 141 ? -1.526  -15.256 10.680  1.00 22.16  ?  143 ALA   A CB   1 
ATOM   1085 N  N    . ARG   A 1 142 ? -4.032  -14.130 12.070  1.00 20.99  ?  144 ARG   A N    1 
ATOM   1086 C  CA   . ARG   A 1 142 ? -5.479  -14.221 12.374  1.00 23.40  ?  144 ARG   A CA   1 
ATOM   1087 C  C    . ARG   A 1 142 ? -6.138  -12.846 12.268  1.00 22.86  ?  144 ARG   A C    1 
ATOM   1088 O  O    . ARG   A 1 142 ? -7.240  -12.734 11.791  1.00 24.15  ?  144 ARG   A O    1 
ATOM   1089 C  CB   . ARG   A 1 142 ? -5.719  -14.866 13.729  1.00 25.78  ?  144 ARG   A CB   1 
ATOM   1090 C  CG   . ARG   A 1 142 ? -5.278  -14.017 14.934  1.00 28.40  ?  144 ARG   A CG   1 
ATOM   1091 C  CD   . ARG   A 1 142 ? -5.018  -14.875 16.150  1.00 32.06  ?  144 ARG   A CD   1 
ATOM   1092 N  NE   . ARG   A 1 142 ? -6.284  -15.262 16.736  1.00 36.74  ?  144 ARG   A NE   1 
ATOM   1093 C  CZ   . ARG   A 1 142 ? -6.694  -15.041 17.981  1.00 32.73  ?  144 ARG   A CZ   1 
ATOM   1094 N  NH1  . ARG   A 1 142 ? -5.927  -14.486 18.912  1.00 30.87  ?  144 ARG   A NH1  1 
ATOM   1095 N  NH2  . ARG   A 1 142 ? -7.908  -15.443 18.290  1.00 36.74  ?  144 ARG   A NH2  1 
ATOM   1096 N  N    . ARG   A 1 143 ? -5.435  -11.793 12.632  1.00 22.41  ?  145 ARG   A N    1 
ATOM   1097 C  CA   . ARG   A 1 143 ? -5.975  -10.457 12.412  1.00 25.51  ?  145 ARG   A CA   1 
ATOM   1098 C  C    . ARG   A 1 143 ? -5.972  -10.004 10.941  1.00 26.65  ?  145 ARG   A C    1 
ATOM   1099 O  O    . ARG   A 1 143 ? -6.779  -9.145  10.591  1.00 27.03  ?  145 ARG   A O    1 
ATOM   1100 C  CB   . ARG   A 1 143 ? -5.257  -9.443  13.312  1.00 26.45  ?  145 ARG   A CB   1 
ATOM   1101 C  CG   . ARG   A 1 143 ? -5.545  -9.684  14.790  1.00 26.43  ?  145 ARG   A CG   1 
ATOM   1102 C  CD   . ARG   A 1 143 ? -4.720  -8.788  15.697  1.00 26.24  ?  145 ARG   A CD   1 
ATOM   1103 N  NE   . ARG   A 1 143 ? -5.153  -8.895  17.078  1.00 26.38  ?  145 ARG   A NE   1 
ATOM   1104 C  CZ   . ARG   A 1 143 ? -4.889  -9.889  17.927  1.00 28.98  ?  145 ARG   A CZ   1 
ATOM   1105 N  NH1  . ARG   A 1 143 ? -4.149  -10.954 17.591  1.00 28.34  ?  145 ARG   A NH1  1 
ATOM   1106 N  NH2  . ARG   A 1 143 ? -5.414  -9.833  19.160  1.00 31.53  ?  145 ARG   A NH2  1 
ATOM   1107 N  N    . HIS   A 1 144 ? -5.106  -10.589 10.083  1.00 30.28  ?  146 HIS   A N    1 
ATOM   1108 C  CA   . HIS   A 1 144 ? -5.044  -10.298 8.623   1.00 28.88  ?  146 HIS   A CA   1 
ATOM   1109 C  C    . HIS   A 1 144 ? -5.181  -11.516 7.751   1.00 28.01  ?  146 HIS   A C    1 
ATOM   1110 O  O    . HIS   A 1 144 ? -4.200  -11.956 7.104   1.00 27.36  ?  146 HIS   A O    1 
ATOM   1111 C  CB   . HIS   A 1 144 ? -3.742  -9.632  8.277   1.00 31.70  ?  146 HIS   A CB   1 
ATOM   1112 C  CG   . HIS   A 1 144 ? -3.614  -8.302  8.907   1.00 36.67  ?  146 HIS   A CG   1 
ATOM   1113 N  ND1  . HIS   A 1 144 ? -3.900  -7.138  8.230   1.00 39.40  ?  146 HIS   A ND1  1 
ATOM   1114 C  CD2  . HIS   A 1 144 ? -3.339  -7.952  10.180  1.00 36.27  ?  146 HIS   A CD2  1 
ATOM   1115 C  CE1  . HIS   A 1 144 ? -3.759  -6.117  9.056   1.00 41.36  ?  146 HIS   A CE1  1 
ATOM   1116 N  NE2  . HIS   A 1 144 ? -3.431  -6.586  10.245  1.00 37.19  ?  146 HIS   A NE2  1 
ATOM   1117 N  N    . PRO   A 1 145 ? -6.413  -12.036 7.664   1.00 26.44  ?  147 PRO   A N    1 
ATOM   1118 C  CA   . PRO   A 1 145 ? -6.607  -13.332 7.019   1.00 25.98  ?  147 PRO   A CA   1 
ATOM   1119 C  C    . PRO   A 1 145 ? -6.374  -13.301 5.506   1.00 24.19  ?  147 PRO   A C    1 
ATOM   1120 O  O    . PRO   A 1 145 ? -6.312  -14.365 4.918   1.00 21.02  ?  147 PRO   A O    1 
ATOM   1121 C  CB   . PRO   A 1 145 ? -8.068  -13.658 7.355   1.00 25.36  ?  147 PRO   A CB   1 
ATOM   1122 C  CG   . PRO   A 1 145 ? -8.678  -12.304 7.368   1.00 24.67  ?  147 PRO   A CG   1 
ATOM   1123 C  CD   . PRO   A 1 145 ? -7.701  -11.441 8.066   1.00 23.78  ?  147 PRO   A CD   1 
ATOM   1124 N  N    . TYR   A 1 146 ? -6.241  -12.101 4.915   1.00 23.80  ?  148 TYR   A N    1 
ATOM   1125 C  CA   . TYR   A 1 146 ? -6.055  -11.920 3.493   1.00 27.69  ?  148 TYR   A CA   1 
ATOM   1126 C  C    . TYR   A 1 146 ? -4.622  -11.524 3.081   1.00 28.44  ?  148 TYR   A C    1 
ATOM   1127 O  O    . TYR   A 1 146 ? -4.275  -11.606 1.908   1.00 28.11  ?  148 TYR   A O    1 
ATOM   1128 C  CB   . TYR   A 1 146 ? -7.069  -10.901 2.967   1.00 31.33  ?  148 TYR   A CB   1 
ATOM   1129 C  CG   . TYR   A 1 146 ? -8.469  -11.484 2.854   1.00 33.54  ?  148 TYR   A CG   1 
ATOM   1130 C  CD1  . TYR   A 1 146 ? -8.819  -12.314 1.785   1.00 34.88  ?  148 TYR   A CD1  1 
ATOM   1131 C  CD2  . TYR   A 1 146 ? -9.448  -11.205 3.811   1.00 37.66  ?  148 TYR   A CD2  1 
ATOM   1132 C  CE1  . TYR   A 1 146 ? -10.103 -12.833 1.665   1.00 34.68  ?  148 TYR   A CE1  1 
ATOM   1133 C  CE2  . TYR   A 1 146 ? -10.744 -11.725 3.686   1.00 37.10  ?  148 TYR   A CE2  1 
ATOM   1134 C  CZ   . TYR   A 1 146 ? -11.057 -12.542 2.621   1.00 35.80  ?  148 TYR   A CZ   1 
ATOM   1135 O  OH   . TYR   A 1 146 ? -12.328 -13.088 2.531   1.00 40.52  ?  148 TYR   A OH   1 
ATOM   1136 N  N    . PHE   A 1 147 ? -3.781  -11.171 4.047   1.00 25.59  ?  149 PHE   A N    1 
ATOM   1137 C  CA   . PHE   A 1 147 ? -2.385  -10.758 3.786   1.00 25.08  ?  149 PHE   A CA   1 
ATOM   1138 C  C    . PHE   A 1 147 ? -1.662  -11.935 3.120   1.00 24.22  ?  149 PHE   A C    1 
ATOM   1139 O  O    . PHE   A 1 147 ? -1.805  -13.074 3.557   1.00 24.16  ?  149 PHE   A O    1 
ATOM   1140 C  CB   . PHE   A 1 147 ? -1.768  -10.391 5.141   1.00 25.58  ?  149 PHE   A CB   1 
ATOM   1141 C  CG   . PHE   A 1 147 ? -0.555  -9.518  5.100   1.00 26.61  ?  149 PHE   A CG   1 
ATOM   1142 C  CD1  . PHE   A 1 147 ? 0.700   -10.052 4.836   1.00 25.50  ?  149 PHE   A CD1  1 
ATOM   1143 C  CD2  . PHE   A 1 147 ? -0.639  -8.178  5.462   1.00 29.80  ?  149 PHE   A CD2  1 
ATOM   1144 C  CE1  . PHE   A 1 147 ? 1.822   -9.255  4.841   1.00 27.29  ?  149 PHE   A CE1  1 
ATOM   1145 C  CE2  . PHE   A 1 147 ? 0.508   -7.371  5.471   1.00 28.88  ?  149 PHE   A CE2  1 
ATOM   1146 C  CZ   . PHE   A 1 147 ? 1.731   -7.908  5.158   1.00 25.64  ?  149 PHE   A CZ   1 
ATOM   1147 N  N    . TYR   A 1 148 ? -0.958  -11.685 2.028   1.00 21.25  ?  150 TYR   A N    1 
ATOM   1148 C  CA   . TYR   A 1 148 ? -0.183  -12.747 1.377   1.00 20.75  ?  150 TYR   A CA   1 
ATOM   1149 C  C    . TYR   A 1 148 ? 0.776   -13.498 2.364   1.00 19.06  ?  150 TYR   A C    1 
ATOM   1150 O  O    . TYR   A 1 148 ? 1.649   -12.894 2.958   1.00 16.17  ?  150 TYR   A O    1 
ATOM   1151 C  CB   . TYR   A 1 148 ? 0.563   -12.180 0.148   1.00 20.51  ?  150 TYR   A CB   1 
ATOM   1152 C  CG   . TYR   A 1 148 ? 1.126   -13.214 -0.751  1.00 18.53  ?  150 TYR   A CG   1 
ATOM   1153 C  CD1  . TYR   A 1 148 ? 0.347   -14.262 -1.184  1.00 18.86  ?  150 TYR   A CD1  1 
ATOM   1154 C  CD2  . TYR   A 1 148 ? 2.463   -13.208 -1.106  1.00 19.82  ?  150 TYR   A CD2  1 
ATOM   1155 C  CE1  . TYR   A 1 148 ? 0.869   -15.244 -1.982  1.00 18.20  ?  150 TYR   A CE1  1 
ATOM   1156 C  CE2  . TYR   A 1 148 ? 2.983   -14.183 -1.931  1.00 18.47  ?  150 TYR   A CE2  1 
ATOM   1157 C  CZ   . TYR   A 1 148 ? 2.172   -15.212 -2.338  1.00 18.36  ?  150 TYR   A CZ   1 
ATOM   1158 O  OH   . TYR   A 1 148 ? 2.620   -16.239 -3.124  1.00 19.96  ?  150 TYR   A OH   1 
ATOM   1159 N  N    . ALA   A 1 149 ? 0.559   -14.807 2.589   1.00 17.31  ?  151 ALA   A N    1 
ATOM   1160 C  CA   . ALA   A 1 149 ? 1.278   -15.496 3.671   1.00 16.56  ?  151 ALA   A CA   1 
ATOM   1161 C  C    . ALA   A 1 149 ? 2.801   -15.354 3.591   1.00 16.33  ?  151 ALA   A C    1 
ATOM   1162 O  O    . ALA   A 1 149 ? 3.434   -15.077 4.607   1.00 15.83  ?  151 ALA   A O    1 
ATOM   1163 C  CB   . ALA   A 1 149 ? 0.859   -16.987 3.801   1.00 16.68  ?  151 ALA   A CB   1 
ATOM   1164 N  N    . PRO   A 1 150 ? 3.400   -15.530 2.409   1.00 17.47  ?  152 PRO   A N    1 
ATOM   1165 C  CA   . PRO   A 1 150 ? 4.856   -15.347 2.305   1.00 18.16  ?  152 PRO   A CA   1 
ATOM   1166 C  C    . PRO   A 1 150 ? 5.357   -13.937 2.596   1.00 19.30  ?  152 PRO   A C    1 
ATOM   1167 O  O    . PRO   A 1 150 ? 6.478   -13.788 3.050   1.00 17.40  ?  152 PRO   A O    1 
ATOM   1168 C  CB   . PRO   A 1 150 ? 5.134   -15.671 0.828   1.00 18.46  ?  152 PRO   A CB   1 
ATOM   1169 C  CG   . PRO   A 1 150 ? 4.037   -16.601 0.452   1.00 18.28  ?  152 PRO   A CG   1 
ATOM   1170 C  CD   . PRO   A 1 150 ? 2.850   -16.017 1.120   1.00 17.91  ?  152 PRO   A CD   1 
ATOM   1171 N  N    . GLU   A 1 151 ? 4.557   -12.900 2.342   1.00 21.49  ?  153 GLU   A N    1 
ATOM   1172 C  CA   . GLU   A 1 151 ? 4.992   -11.559 2.769   1.00 24.38  ?  153 GLU   A CA   1 
ATOM   1173 C  C    . GLU   A 1 151 ? 4.955   -11.430 4.349   1.00 24.34  ?  153 GLU   A C    1 
ATOM   1174 O  O    . GLU   A 1 151 ? 5.810   -10.776 4.975   1.00 21.29  ?  153 GLU   A O    1 
ATOM   1175 C  CB   . GLU   A 1 151 ? 4.144   -10.492 2.074   1.00 28.98  ?  153 GLU   A CB   1 
ATOM   1176 C  CG   . GLU   A 1 151 ? 4.581   -9.056  2.342   1.00 32.97  ?  153 GLU   A CG   1 
ATOM   1177 C  CD   . GLU   A 1 151 ? 5.784   -8.586  1.538   1.00 38.29  ?  153 GLU   A CD   1 
ATOM   1178 O  OE1  . GLU   A 1 151 ? 6.479   -9.428  0.929   1.00 43.09  ?  153 GLU   A OE1  1 
ATOM   1179 O  OE2  . GLU   A 1 151 ? 6.032   -7.343  1.526   1.00 40.63  ?  153 GLU   A OE2  1 
ATOM   1180 N  N    . LEU   A 1 152 ? 3.994   -12.094 4.990   1.00 23.97  ?  154 LEU   A N    1 
ATOM   1181 C  CA   . LEU   A 1 152 ? 3.898   -12.071 6.435   1.00 26.30  ?  154 LEU   A CA   1 
ATOM   1182 C  C    . LEU   A 1 152 ? 5.088   -12.801 7.013   1.00 26.68  ?  154 LEU   A C    1 
ATOM   1183 O  O    . LEU   A 1 152 ? 5.608   -12.425 8.083   1.00 28.85  ?  154 LEU   A O    1 
ATOM   1184 C  CB   . LEU   A 1 152 ? 2.581   -12.678 6.935   1.00 28.76  ?  154 LEU   A CB   1 
ATOM   1185 C  CG   . LEU   A 1 152 ? 2.160   -12.291 8.350   1.00 29.77  ?  154 LEU   A CG   1 
ATOM   1186 C  CD1  . LEU   A 1 152 ? 1.672   -10.828 8.415   1.00 30.97  ?  154 LEU   A CD1  1 
ATOM   1187 C  CD2  . LEU   A 1 152 ? 1.081   -13.236 8.864   1.00 28.54  ?  154 LEU   A CD2  1 
ATOM   1188 N  N    . LEU   A 1 153 ? 5.531   -13.831 6.302   1.00 24.82  ?  155 LEU   A N    1 
ATOM   1189 C  CA   . LEU   A 1 153 ? 6.711   -14.558 6.714   1.00 24.20  ?  155 LEU   A CA   1 
ATOM   1190 C  C    . LEU   A 1 153 ? 7.942   -13.657 6.567   1.00 22.63  ?  155 LEU   A C    1 
ATOM   1191 O  O    . LEU   A 1 153 ? 8.788   -13.643 7.438   1.00 20.32  ?  155 LEU   A O    1 
ATOM   1192 C  CB   . LEU   A 1 153 ? 6.833   -15.849 5.923   1.00 22.37  ?  155 LEU   A CB   1 
ATOM   1193 C  CG   . LEU   A 1 153 ? 8.052   -16.697 6.198   1.00 22.04  ?  155 LEU   A CG   1 
ATOM   1194 C  CD1  . LEU   A 1 153 ? 8.156   -17.039 7.666   1.00 22.84  ?  155 LEU   A CD1  1 
ATOM   1195 C  CD2  . LEU   A 1 153 ? 8.048   -17.939 5.338   1.00 21.08  ?  155 LEU   A CD2  1 
ATOM   1196 N  N    . PHE   A 1 154 ? 8.002   -12.892 5.481   1.00 24.82  ?  156 PHE   A N    1 
ATOM   1197 C  CA   . PHE   A 1 154 ? 9.023   -11.836 5.276   1.00 27.30  ?  156 PHE   A CA   1 
ATOM   1198 C  C    . PHE   A 1 154 ? 9.107   -10.830 6.434   1.00 27.49  ?  156 PHE   A C    1 
ATOM   1199 O  O    . PHE   A 1 154 ? 10.204  -10.443 6.813   1.00 30.88  ?  156 PHE   A O    1 
ATOM   1200 C  CB   . PHE   A 1 154 ? 8.808   -11.118 3.913   1.00 28.61  ?  156 PHE   A CB   1 
ATOM   1201 C  CG   . PHE   A 1 154 ? 9.600   -9.835  3.727   1.00 29.41  ?  156 PHE   A CG   1 
ATOM   1202 C  CD1  . PHE   A 1 154 ? 10.978  -9.866  3.463   1.00 30.94  ?  156 PHE   A CD1  1 
ATOM   1203 C  CD2  . PHE   A 1 154 ? 8.963   -8.590  3.777   1.00 33.25  ?  156 PHE   A CD2  1 
ATOM   1204 C  CE1  . PHE   A 1 154 ? 11.704  -8.690  3.273   1.00 32.22  ?  156 PHE   A CE1  1 
ATOM   1205 C  CE2  . PHE   A 1 154 ? 9.677   -7.408  3.575   1.00 33.28  ?  156 PHE   A CE2  1 
ATOM   1206 C  CZ   . PHE   A 1 154 ? 11.055  -7.457  3.316   1.00 33.53  ?  156 PHE   A CZ   1 
ATOM   1207 N  N    . PHE   A 1 155 ? 7.966   -10.388 6.958   1.00 26.71  ?  157 PHE   A N    1 
ATOM   1208 C  CA   . PHE   A 1 155 ? 7.940   -9.443  8.086   1.00 25.18  ?  157 PHE   A CA   1 
ATOM   1209 C  C    . PHE   A 1 155 ? 8.424   -10.053 9.386   1.00 24.55  ?  157 PHE   A C    1 
ATOM   1210 O  O    . PHE   A 1 155 ? 9.119   -9.392  10.139  1.00 26.31  ?  157 PHE   A O    1 
ATOM   1211 C  CB   . PHE   A 1 155 ? 6.544   -8.809  8.284   1.00 24.99  ?  157 PHE   A CB   1 
ATOM   1212 C  CG   . PHE   A 1 155 ? 6.302   -7.626  7.402   1.00 23.85  ?  157 PHE   A CG   1 
ATOM   1213 C  CD1  . PHE   A 1 155 ? 5.822   -7.788  6.121   1.00 24.95  ?  157 PHE   A CD1  1 
ATOM   1214 C  CD2  . PHE   A 1 155 ? 6.616   -6.356  7.836   1.00 25.69  ?  157 PHE   A CD2  1 
ATOM   1215 C  CE1  . PHE   A 1 155 ? 5.607   -6.694  5.288   1.00 26.37  ?  157 PHE   A CE1  1 
ATOM   1216 C  CE2  . PHE   A 1 155 ? 6.411   -5.247  7.020   1.00 25.54  ?  157 PHE   A CE2  1 
ATOM   1217 C  CZ   . PHE   A 1 155 ? 5.905   -5.421  5.738   1.00 24.93  ?  157 PHE   A CZ   1 
ATOM   1218 N  N    . ALA   A 1 156 ? 8.070   -11.312 9.631   1.00 21.93  ?  158 ALA   A N    1 
ATOM   1219 C  CA   . ALA   A 1 156 ? 8.497   -12.036 10.825  1.00 21.78  ?  158 ALA   A CA   1 
ATOM   1220 C  C    . ALA   A 1 156 ? 9.988   -12.122 10.922  1.00 21.85  ?  158 ALA   A C    1 
ATOM   1221 O  O    . ALA   A 1 156 ? 10.568  -11.934 12.031  1.00 23.59  ?  158 ALA   A O    1 
ATOM   1222 C  CB   . ALA   A 1 156 ? 7.911   -13.446 10.851  1.00 21.41  ?  158 ALA   A CB   1 
ATOM   1223 N  N    . LYS   A 1 157 ? 10.613  -12.393 9.782   1.00 20.72  ?  159 LYS   A N    1 
ATOM   1224 C  CA   . LYS   A 1 157 ? 12.063  -12.556 9.702   1.00 22.56  ?  159 LYS   A CA   1 
ATOM   1225 C  C    . LYS   A 1 157 ? 12.743  -11.251 10.009  1.00 23.40  ?  159 LYS   A C    1 
ATOM   1226 O  O    . LYS   A 1 157 ? 13.824  -11.269 10.607  1.00 26.89  ?  159 LYS   A O    1 
ATOM   1227 C  CB   . LYS   A 1 157 ? 12.537  -13.095 8.345   1.00 23.29  ?  159 LYS   A CB   1 
ATOM   1228 C  CG   . LYS   A 1 157 ? 12.353  -14.611 8.157   1.00 26.15  ?  159 LYS   A CG   1 
ATOM   1229 C  CD   . LYS   A 1 157 ? 12.470  -15.010 6.675   1.00 25.99  ?  159 LYS   A CD   1 
ATOM   1230 C  CE   . LYS   A 1 157 ? 11.643  -16.231 6.299   1.00 28.08  ?  159 LYS   A CE   1 
ATOM   1231 N  NZ   . LYS   A 1 157 ? 12.325  -17.531 6.406   1.00 27.04  ?  159 LYS   A NZ   1 
ATOM   1232 N  N    . ARG   A 1 158 ? 12.101  -10.132 9.662   1.00 22.95  ?  160 ARG   A N    1 
ATOM   1233 C  CA   . ARG   A 1 158 ? 12.650  -8.812  9.979   1.00 23.78  ?  160 ARG   A CA   1 
ATOM   1234 C  C    . ARG   A 1 158 ? 12.428  -8.481  11.460  1.00 24.20  ?  160 ARG   A C    1 
ATOM   1235 O  O    . ARG   A 1 158 ? 13.290  -7.919  12.121  1.00 22.16  ?  160 ARG   A O    1 
ATOM   1236 C  CB   . ARG   A 1 158 ? 12.036  -7.742  9.080   1.00 24.85  ?  160 ARG   A CB   1 
ATOM   1237 C  CG   . ARG   A 1 158 ? 12.156  -8.017  7.577   1.00 24.92  ?  160 ARG   A CG   1 
ATOM   1238 C  CD   . ARG   A 1 158 ? 11.466  -6.941  6.768   1.00 26.09  ?  160 ARG   A CD   1 
ATOM   1239 N  NE   . ARG   A 1 158 ? 12.161  -5.707  7.007   1.00 28.56  ?  160 ARG   A NE   1 
ATOM   1240 C  CZ   . ARG   A 1 158 ? 11.745  -4.480  6.694   1.00 32.25  ?  160 ARG   A CZ   1 
ATOM   1241 N  NH1  . ARG   A 1 158 ? 10.574  -4.251  6.093   1.00 31.06  ?  160 ARG   A NH1  1 
ATOM   1242 N  NH2  . ARG   A 1 158 ? 12.547  -3.455  7.006   1.00 34.15  ?  160 ARG   A NH2  1 
ATOM   1243 N  N    . TYR   A 1 159 ? 11.272  -8.840  12.010  1.00 24.16  ?  161 TYR   A N    1 
ATOM   1244 C  CA   . TYR   A 1 159 ? 11.105  -8.646  13.437  1.00 25.41  ?  161 TYR   A CA   1 
ATOM   1245 C  C    . TYR   A 1 159 ? 12.206  -9.389  14.170  1.00 26.83  ?  161 TYR   A C    1 
ATOM   1246 O  O    . TYR   A 1 159 ? 12.941  -8.785  14.967  1.00 26.05  ?  161 TYR   A O    1 
ATOM   1247 C  CB   . TYR   A 1 159 ? 9.730   -9.095  13.905  1.00 27.38  ?  161 TYR   A CB   1 
ATOM   1248 C  CG   . TYR   A 1 159 ? 8.712   -8.027  13.720  1.00 26.25  ?  161 TYR   A CG   1 
ATOM   1249 C  CD1  . TYR   A 1 159 ? 8.572   -7.018  14.672  1.00 27.00  ?  161 TYR   A CD1  1 
ATOM   1250 C  CD2  . TYR   A 1 159 ? 7.889   -8.005  12.600  1.00 27.69  ?  161 TYR   A CD2  1 
ATOM   1251 C  CE1  . TYR   A 1 159 ? 7.623   -6.030  14.525  1.00 27.30  ?  161 TYR   A CE1  1 
ATOM   1252 C  CE2  . TYR   A 1 159 ? 6.936   -7.019  12.435  1.00 28.93  ?  161 TYR   A CE2  1 
ATOM   1253 C  CZ   . TYR   A 1 159 ? 6.804   -6.032  13.410  1.00 28.52  ?  161 TYR   A CZ   1 
ATOM   1254 O  OH   . TYR   A 1 159 ? 5.842   -5.052  13.274  1.00 26.79  ?  161 TYR   A OH   1 
ATOM   1255 N  N    . LYS   A 1 160 ? 12.371  -10.662 13.824  1.00 25.51  ?  162 LYS   A N    1 
ATOM   1256 C  CA   . LYS   A 1 160 ? 13.338  -11.515 14.503  1.00 27.20  ?  162 LYS   A CA   1 
ATOM   1257 C  C    . LYS   A 1 160 ? 14.733  -10.894 14.466  1.00 28.17  ?  162 LYS   A C    1 
ATOM   1258 O  O    . LYS   A 1 160 ? 15.376  -10.744 15.496  1.00 30.10  ?  162 LYS   A O    1 
ATOM   1259 C  CB   . LYS   A 1 160 ? 13.375  -12.898 13.856  1.00 27.20  ?  162 LYS   A CB   1 
ATOM   1260 C  CG   . LYS   A 1 160 ? 14.654  -13.674 14.157  1.00 28.04  ?  162 LYS   A CG   1 
ATOM   1261 C  CD   . LYS   A 1 160 ? 14.450  -15.172 14.005  1.00 31.21  ?  162 LYS   A CD   1 
ATOM   1262 C  CE   . LYS   A 1 160 ? 14.950  -15.927 15.226  1.00 33.56  ?  162 LYS   A CE   1 
ATOM   1263 N  NZ   . LYS   A 1 160 ? 14.479  -17.341 15.280  1.00 36.74  ?  162 LYS   A NZ   1 
ATOM   1264 N  N    . ALA   A 1 161 ? 15.189  -10.561 13.265  1.00 30.84  ?  163 ALA   A N    1 
ATOM   1265 C  CA   . ALA   A 1 161 ? 16.403  -9.760  13.054  1.00 33.38  ?  163 ALA   A CA   1 
ATOM   1266 C  C    . ALA   A 1 161 ? 16.502  -8.526  13.978  1.00 35.24  ?  163 ALA   A C    1 
ATOM   1267 O  O    . ALA   A 1 161 ? 17.591  -8.186  14.455  1.00 39.44  ?  163 ALA   A O    1 
ATOM   1268 C  CB   . ALA   A 1 161 ? 16.497  -9.349  11.596  1.00 32.29  ?  163 ALA   A CB   1 
ATOM   1269 N  N    . ALA   A 1 162 ? 15.373  -7.872  14.242  1.00 38.48  ?  164 ALA   A N    1 
ATOM   1270 C  CA   . ALA   A 1 162 ? 15.332  -6.683  15.119  1.00 38.64  ?  164 ALA   A CA   1 
ATOM   1271 C  C    . ALA   A 1 162 ? 15.589  -7.021  16.601  1.00 40.27  ?  164 ALA   A C    1 
ATOM   1272 O  O    . ALA   A 1 162 ? 16.303  -6.274  17.312  1.00 35.52  ?  164 ALA   A O    1 
ATOM   1273 C  CB   . ALA   A 1 162 ? 14.007  -5.929  14.957  1.00 38.90  ?  164 ALA   A CB   1 
ATOM   1274 N  N    . PHE   A 1 163 ? 15.017  -8.137  17.059  1.00 38.27  ?  165 PHE   A N    1 
ATOM   1275 C  CA   . PHE   A 1 163 ? 15.210  -8.578  18.440  1.00 39.32  ?  165 PHE   A CA   1 
ATOM   1276 C  C    . PHE   A 1 163 ? 16.645  -9.089  18.624  1.00 37.31  ?  165 PHE   A C    1 
ATOM   1277 O  O    . PHE   A 1 163 ? 17.298  -8.706  19.577  1.00 35.79  ?  165 PHE   A O    1 
ATOM   1278 C  CB   . PHE   A 1 163 ? 14.140  -9.603  18.864  1.00 40.02  ?  165 PHE   A CB   1 
ATOM   1279 C  CG   . PHE   A 1 163 ? 12.758  -8.996  19.031  1.00 39.47  ?  165 PHE   A CG   1 
ATOM   1280 C  CD1  . PHE   A 1 163 ? 12.434  -8.286  20.166  1.00 38.79  ?  165 PHE   A CD1  1 
ATOM   1281 C  CD2  . PHE   A 1 163 ? 11.799  -9.115  18.036  1.00 39.26  ?  165 PHE   A CD2  1 
ATOM   1282 C  CE1  . PHE   A 1 163 ? 11.188  -7.713  20.322  1.00 38.52  ?  165 PHE   A CE1  1 
ATOM   1283 C  CE2  . PHE   A 1 163 ? 10.541  -8.543  18.178  1.00 39.36  ?  165 PHE   A CE2  1 
ATOM   1284 C  CZ   . PHE   A 1 163 ? 10.235  -7.837  19.332  1.00 39.43  ?  165 PHE   A CZ   1 
ATOM   1285 N  N    . THR   A 1 164 ? 17.139  -9.878  17.677  1.00 37.01  ?  166 THR   A N    1 
ATOM   1286 C  CA   . THR   A 1 164 ? 18.518  -10.408 17.707  1.00 39.50  ?  166 THR   A CA   1 
ATOM   1287 C  C    . THR   A 1 164 ? 19.593  -9.331  17.782  1.00 40.43  ?  166 THR   A C    1 
ATOM   1288 O  O    . THR   A 1 164 ? 20.593  -9.506  18.470  1.00 39.61  ?  166 THR   A O    1 
ATOM   1289 C  CB   . THR   A 1 164 ? 18.798  -11.358 16.524  1.00 37.03  ?  166 THR   A CB   1 
ATOM   1290 O  OG1  . THR   A 1 164 ? 18.133  -12.602 16.759  1.00 35.12  ?  166 THR   A OG1  1 
ATOM   1291 C  CG2  . THR   A 1 164 ? 20.270  -11.664 16.365  1.00 36.08  ?  166 THR   A CG2  1 
ATOM   1292 N  N    . GLU   A 1 165 ? 19.393  -8.231  17.079  1.00 45.28  ?  167 GLU   A N    1 
ATOM   1293 C  CA   . GLU   A 1 165 ? 20.306  -7.115  17.194  1.00 47.25  ?  167 GLU   A CA   1 
ATOM   1294 C  C    . GLU   A 1 165 ? 20.099  -6.435  18.548  1.00 52.43  ?  167 GLU   A C    1 
ATOM   1295 O  O    . GLU   A 1 165 ? 21.045  -6.387  19.354  1.00 56.56  ?  167 GLU   A O    1 
ATOM   1296 C  CB   . GLU   A 1 165 ? 20.133  -6.113  16.039  1.00 48.90  ?  167 GLU   A CB   1 
ATOM   1297 C  CG   . GLU   A 1 165 ? 21.161  -4.982  16.035  1.00 49.22  ?  167 GLU   A CG   1 
ATOM   1298 C  CD   . GLU   A 1 165 ? 20.850  -3.861  15.067  1.00 49.69  ?  167 GLU   A CD   1 
ATOM   1299 O  OE1  . GLU   A 1 165 ? 19.875  -3.934  14.293  1.00 52.40  ?  167 GLU   A OE1  1 
ATOM   1300 O  OE2  . GLU   A 1 165 ? 21.607  -2.882  15.085  1.00 52.55  ?  167 GLU   A OE2  1 
ATOM   1301 N  N    . CYS   A 1 166 ? 18.877  -5.943  18.811  1.00 50.09  ?  168 CYS   A N    1 
ATOM   1302 C  CA   . CYS   A 1 166 ? 18.681  -4.909  19.840  1.00 48.35  ?  168 CYS   A CA   1 
ATOM   1303 C  C    . CYS   A 1 166 ? 18.654  -5.353  21.300  1.00 48.46  ?  168 CYS   A C    1 
ATOM   1304 O  O    . CYS   A 1 166 ? 18.850  -4.523  22.193  1.00 46.85  ?  168 CYS   A O    1 
ATOM   1305 C  CB   . CYS   A 1 166 ? 17.432  -4.091  19.565  1.00 47.57  ?  168 CYS   A CB   1 
ATOM   1306 S  SG   . CYS   A 1 166 ? 17.562  -3.111  18.076  1.00 48.14  ?  168 CYS   A SG   1 
ATOM   1307 N  N    . CYS   A 1 167 ? 18.408  -6.640  21.538  1.00 46.55  ?  169 CYS   A N    1 
ATOM   1308 C  CA   . CYS   A 1 167 ? 18.213  -7.146  22.889  1.00 44.51  ?  169 CYS   A CA   1 
ATOM   1309 C  C    . CYS   A 1 167 ? 19.543  -7.381  23.654  1.00 49.80  ?  169 CYS   A C    1 
ATOM   1310 O  O    . CYS   A 1 167 ? 19.551  -7.305  24.879  1.00 57.61  ?  169 CYS   A O    1 
ATOM   1311 C  CB   . CYS   A 1 167 ? 17.293  -8.389  22.873  1.00 40.99  ?  169 CYS   A CB   1 
ATOM   1312 S  SG   . CYS   A 1 167 ? 15.534  -7.990  22.523  1.00 37.74  ?  169 CYS   A SG   1 
ATOM   1313 N  N    . GLN   A 1 168 ? 20.655  -7.642  22.950  1.00 56.76  ?  170 GLN   A N    1 
ATOM   1314 C  CA   . GLN   A 1 168 ? 22.000  -7.684  23.578  1.00 55.85  ?  170 GLN   A CA   1 
ATOM   1315 C  C    . GLN   A 1 168 ? 22.766  -6.454  23.130  1.00 58.01  ?  170 GLN   A C    1 
ATOM   1316 O  O    . GLN   A 1 168 ? 23.510  -6.507  22.163  1.00 61.09  ?  170 GLN   A O    1 
ATOM   1317 C  CB   . GLN   A 1 168 ? 22.754  -8.992  23.269  1.00 53.72  ?  170 GLN   A CB   1 
ATOM   1318 C  CG   . GLN   A 1 168 ? 21.986  -10.234 23.736  1.00 55.34  ?  170 GLN   A CG   1 
ATOM   1319 C  CD   . GLN   A 1 168 ? 22.805  -11.306 24.465  1.00 58.39  ?  170 GLN   A CD   1 
ATOM   1320 O  OE1  . GLN   A 1 168 ? 23.842  -11.035 25.090  1.00 56.58  ?  170 GLN   A OE1  1 
ATOM   1321 N  NE2  . GLN   A 1 168 ? 22.306  -12.544 24.414  1.00 56.86  ?  170 GLN   A NE2  1 
ATOM   1322 N  N    . ALA   A 1 169 ? 22.535  -5.342  23.837  1.00 59.70  ?  171 ALA   A N    1 
ATOM   1323 C  CA   . ALA   A 1 169 ? 23.078  -4.012  23.499  1.00 60.32  ?  171 ALA   A CA   1 
ATOM   1324 C  C    . ALA   A 1 169 ? 22.869  -3.028  24.669  1.00 62.34  ?  171 ALA   A C    1 
ATOM   1325 O  O    . ALA   A 1 169 ? 22.228  -3.370  25.663  1.00 63.94  ?  171 ALA   A O    1 
ATOM   1326 C  CB   . ALA   A 1 169 ? 22.433  -3.481  22.220  1.00 60.55  ?  171 ALA   A CB   1 
ATOM   1327 N  N    . ALA   A 1 170 ? 23.402  -1.814  24.551  1.00 66.52  ?  172 ALA   A N    1 
ATOM   1328 C  CA   . ALA   A 1 170 ? 23.506  -0.897  25.698  1.00 70.36  ?  172 ALA   A CA   1 
ATOM   1329 C  C    . ALA   A 1 170 ? 22.170  -0.302  26.121  1.00 75.37  ?  172 ALA   A C    1 
ATOM   1330 O  O    . ALA   A 1 170 ? 21.814  -0.347  27.306  1.00 81.46  ?  172 ALA   A O    1 
ATOM   1331 C  CB   . ALA   A 1 170 ? 24.504  0.221   25.408  1.00 70.13  ?  172 ALA   A CB   1 
ATOM   1332 N  N    . ASP   A 1 171 ? 21.444  0.268   25.157  1.00 75.21  ?  173 ASP   A N    1 
ATOM   1333 C  CA   . ASP   A 1 171 ? 20.122  0.845   25.416  1.00 69.46  ?  173 ASP   A CA   1 
ATOM   1334 C  C    . ASP   A 1 171 ? 19.091  0.225   24.472  1.00 64.67  ?  173 ASP   A C    1 
ATOM   1335 O  O    . ASP   A 1 171 ? 18.867  0.689   23.349  1.00 67.57  ?  173 ASP   A O    1 
ATOM   1336 C  CB   . ASP   A 1 171 ? 20.156  2.378   25.309  1.00 68.89  ?  173 ASP   A CB   1 
ATOM   1337 C  CG   . ASP   A 1 171 ? 19.104  3.053   26.189  1.00 69.62  ?  173 ASP   A CG   1 
ATOM   1338 O  OD1  . ASP   A 1 171 ? 18.310  2.339   26.860  1.00 69.08  ?  173 ASP   A OD1  1 
ATOM   1339 O  OD2  . ASP   A 1 171 ? 19.084  4.307   26.217  1.00 63.97  ?  173 ASP   A OD2  1 
ATOM   1340 N  N    . LYS   A 1 172 ? 18.466  -0.836  24.964  1.00 60.30  ?  174 LYS   A N    1 
ATOM   1341 C  CA   . LYS   A 1 172 ? 17.601  -1.694  24.166  1.00 56.56  ?  174 LYS   A CA   1 
ATOM   1342 C  C    . LYS   A 1 172 ? 16.474  -0.903  23.490  1.00 56.92  ?  174 LYS   A C    1 
ATOM   1343 O  O    . LYS   A 1 172 ? 16.353  -0.926  22.268  1.00 49.62  ?  174 LYS   A O    1 
ATOM   1344 C  CB   . LYS   A 1 172 ? 17.028  -2.817  25.045  1.00 56.02  ?  174 LYS   A CB   1 
ATOM   1345 C  CG   . LYS   A 1 172 ? 18.069  -3.810  25.548  1.00 55.07  ?  174 LYS   A CG   1 
ATOM   1346 C  CD   . LYS   A 1 172 ? 17.427  -5.010  26.239  1.00 57.30  ?  174 LYS   A CD   1 
ATOM   1347 C  CE   . LYS   A 1 172 ? 17.305  -4.829  27.745  1.00 57.55  ?  174 LYS   A CE   1 
ATOM   1348 N  NZ   . LYS   A 1 172 ? 18.575  -5.148  28.453  1.00 57.74  ?  174 LYS   A NZ   1 
ATOM   1349 N  N    . ALA   A 1 173 ? 15.698  -0.169  24.289  1.00 55.62  ?  175 ALA   A N    1 
ATOM   1350 C  CA   . ALA   A 1 173 ? 14.511  0.532   23.808  1.00 54.17  ?  175 ALA   A CA   1 
ATOM   1351 C  C    . ALA   A 1 173 ? 14.802  1.595   22.736  1.00 54.38  ?  175 ALA   A C    1 
ATOM   1352 O  O    . ALA   A 1 173 ? 14.004  1.750   21.821  1.00 58.40  ?  175 ALA   A O    1 
ATOM   1353 C  CB   . ALA   A 1 173 ? 13.735  1.137   24.978  1.00 53.64  ?  175 ALA   A CB   1 
ATOM   1354 N  N    . ALA   A 1 174 ? 15.930  2.303   22.831  1.00 52.46  ?  176 ALA   A N    1 
ATOM   1355 C  CA   . ALA   A 1 174 ? 16.305  3.321   21.816  1.00 54.75  ?  176 ALA   A CA   1 
ATOM   1356 C  C    . ALA   A 1 174 ? 16.745  2.714   20.456  1.00 51.97  ?  176 ALA   A C    1 
ATOM   1357 O  O    . ALA   A 1 174 ? 16.741  3.405   19.423  1.00 45.24  ?  176 ALA   A O    1 
ATOM   1358 C  CB   . ALA   A 1 174 ? 17.392  4.245   22.363  1.00 56.00  ?  176 ALA   A CB   1 
ATOM   1359 N  N    . CYS   A 1 175 ? 17.151  1.443   20.492  1.00 48.11  ?  177 CYS   A N    1 
ATOM   1360 C  CA   . CYS   A 1 175 ? 17.363  0.595   19.312  1.00 50.64  ?  177 CYS   A CA   1 
ATOM   1361 C  C    . CYS   A 1 175 ? 16.032  0.005   18.839  1.00 47.79  ?  177 CYS   A C    1 
ATOM   1362 O  O    . CYS   A 1 175 ? 15.639  0.176   17.689  1.00 50.94  ?  177 CYS   A O    1 
ATOM   1363 C  CB   . CYS   A 1 175 ? 18.321  -0.564  19.693  1.00 52.87  ?  177 CYS   A CB   1 
ATOM   1364 S  SG   . CYS   A 1 175 ? 18.992  -1.661  18.409  1.00 55.96  ?  177 CYS   A SG   1 
ATOM   1365 N  N    . LEU   A 1 176 ? 15.335  -0.679  19.740  1.00 46.67  ?  178 LEU   A N    1 
ATOM   1366 C  CA   . LEU   A 1 176 ? 14.191  -1.512  19.371  1.00 45.00  ?  178 LEU   A CA   1 
ATOM   1367 C  C    . LEU   A 1 176 ? 12.953  -0.712  18.989  1.00 47.70  ?  178 LEU   A C    1 
ATOM   1368 O  O    . LEU   A 1 176 ? 12.278  -1.072  18.032  1.00 44.03  ?  178 LEU   A O    1 
ATOM   1369 C  CB   . LEU   A 1 176 ? 13.867  -2.514  20.497  1.00 46.28  ?  178 LEU   A CB   1 
ATOM   1370 C  CG   . LEU   A 1 176 ? 12.933  -3.727  20.259  1.00 43.98  ?  178 LEU   A CG   1 
ATOM   1371 C  CD1  . LEU   A 1 176 ? 13.246  -4.412  18.940  1.00 43.86  ?  178 LEU   A CD1  1 
ATOM   1372 C  CD2  . LEU   A 1 176 ? 13.018  -4.744  21.400  1.00 43.92  ?  178 LEU   A CD2  1 
ATOM   1373 N  N    . LEU   A 1 177 ? 12.648  0.362   19.719  1.00 50.47  ?  179 LEU   A N    1 
ATOM   1374 C  CA   . LEU   A 1 177 ? 11.419  1.139   19.438  1.00 53.01  ?  179 LEU   A CA   1 
ATOM   1375 C  C    . LEU   A 1 177 ? 11.332  1.734   18.014  1.00 53.15  ?  179 LEU   A C    1 
ATOM   1376 O  O    . LEU   A 1 177 ? 10.248  1.688   17.414  1.00 53.20  ?  179 LEU   A O    1 
ATOM   1377 C  CB   . LEU   A 1 177 ? 11.166  2.232   20.487  1.00 54.04  ?  179 LEU   A CB   1 
ATOM   1378 C  CG   . LEU   A 1 177 ? 10.398  1.887   21.765  1.00 55.19  ?  179 LEU   A CG   1 
ATOM   1379 C  CD1  . LEU   A 1 177 ? 10.737  0.513   22.327  1.00 56.18  ?  179 LEU   A CD1  1 
ATOM   1380 C  CD2  . LEU   A 1 177 ? 10.632  2.981   22.806  1.00 54.14  ?  179 LEU   A CD2  1 
ATOM   1381 N  N    . PRO   A 1 178 ? 12.440  2.317   17.492  1.00 54.43  ?  180 PRO   A N    1 
ATOM   1382 C  CA   . PRO   A 1 178 ? 12.513  2.754   16.074  1.00 53.46  ?  180 PRO   A CA   1 
ATOM   1383 C  C    . PRO   A 1 178 ? 12.396  1.648   15.025  1.00 48.40  ?  180 PRO   A C    1 
ATOM   1384 O  O    . PRO   A 1 178 ? 11.848  1.883   13.946  1.00 46.74  ?  180 PRO   A O    1 
ATOM   1385 C  CB   . PRO   A 1 178 ? 13.899  3.392   15.972  1.00 51.48  ?  180 PRO   A CB   1 
ATOM   1386 C  CG   . PRO   A 1 178 ? 14.137  3.929   17.330  1.00 54.76  ?  180 PRO   A CG   1 
ATOM   1387 C  CD   . PRO   A 1 178 ? 13.546  2.906   18.270  1.00 56.03  ?  180 PRO   A CD   1 
ATOM   1388 N  N    . LYS   A 1 179 ? 12.950  0.477   15.321  1.00 41.57  ?  181 LYS   A N    1 
ATOM   1389 C  CA   . LYS   A 1 179 ? 12.774  -0.664  14.445  1.00 36.11  ?  181 LYS   A CA   1 
ATOM   1390 C  C    . LYS   A 1 179 ? 11.301  -1.089  14.409  1.00 33.38  ?  181 LYS   A C    1 
ATOM   1391 O  O    . LYS   A 1 179 ? 10.742  -1.279  13.309  1.00 31.17  ?  181 LYS   A O    1 
ATOM   1392 C  CB   . LYS   A 1 179 ? 13.716  -1.808  14.818  1.00 35.35  ?  181 LYS   A CB   1 
ATOM   1393 C  CG   . LYS   A 1 179 ? 15.166  -1.492  14.437  1.00 35.92  ?  181 LYS   A CG   1 
ATOM   1394 C  CD   . LYS   A 1 179 ? 16.083  -2.688  14.568  1.00 35.56  ?  181 LYS   A CD   1 
ATOM   1395 N  N    . LEU   A 1 180 ? 10.677  -1.195  15.583  1.00 28.03  ?  182 LEU   A N    1 
ATOM   1396 C  CA   . LEU   A 1 180 ? 9.295   -1.642  15.681  1.00 30.39  ?  182 LEU   A CA   1 
ATOM   1397 C  C    . LEU   A 1 180 ? 8.251   -0.673  15.138  1.00 30.20  ?  182 LEU   A C    1 
ATOM   1398 O  O    . LEU   A 1 180 ? 7.246   -1.117  14.662  1.00 30.34  ?  182 LEU   A O    1 
ATOM   1399 C  CB   . LEU   A 1 180 ? 8.930   -2.016  17.135  1.00 31.87  ?  182 LEU   A CB   1 
ATOM   1400 C  CG   . LEU   A 1 180 ? 9.647   -3.192  17.824  1.00 29.33  ?  182 LEU   A CG   1 
ATOM   1401 C  CD1  . LEU   A 1 180 ? 9.082   -3.394  19.219  1.00 30.55  ?  182 LEU   A CD1  1 
ATOM   1402 C  CD2  . LEU   A 1 180 ? 9.547   -4.474  17.052  1.00 30.75  ?  182 LEU   A CD2  1 
ATOM   1403 N  N    . ASP   A 1 181 ? 8.467   0.638   15.239  1.00 33.28  ?  183 ASP   A N    1 
ATOM   1404 C  CA   . ASP   A 1 181 ? 7.514   1.623   14.684  1.00 35.39  ?  183 ASP   A CA   1 
ATOM   1405 C  C    . ASP   A 1 181 ? 7.529   1.533   13.164  1.00 34.75  ?  183 ASP   A C    1 
ATOM   1406 O  O    . ASP   A 1 181 ? 6.459   1.545   12.532  1.00 34.72  ?  183 ASP   A O    1 
ATOM   1407 C  CB   . ASP   A 1 181 ? 7.848   3.069   15.091  1.00 36.90  ?  183 ASP   A CB   1 
ATOM   1408 C  CG   . ASP   A 1 181 ? 7.697   3.332   16.602  1.00 41.34  ?  183 ASP   A CG   1 
ATOM   1409 O  OD1  . ASP   A 1 181 ? 6.779   2.749   17.234  1.00 49.33  ?  183 ASP   A OD1  1 
ATOM   1410 O  OD2  . ASP   A 1 181 ? 8.493   4.138   17.161  1.00 39.59  ?  183 ASP   A OD2  1 
ATOM   1411 N  N    . GLU   A 1 182 ? 8.743   1.450   12.596  1.00 34.60  ?  184 GLU   A N    1 
ATOM   1412 C  CA   . GLU   A 1 182 ? 8.950   1.303   11.163  1.00 31.41  ?  184 GLU   A CA   1 
ATOM   1413 C  C    . GLU   A 1 182 ? 8.410   -0.034  10.671  1.00 30.94  ?  184 GLU   A C    1 
ATOM   1414 O  O    . GLU   A 1 182 ? 7.708   -0.050  9.668   1.00 28.73  ?  184 GLU   A O    1 
ATOM   1415 C  CB   . GLU   A 1 182 ? 10.419  1.427   10.776  1.00 34.62  ?  184 GLU   A CB   1 
ATOM   1416 N  N    . LEU   A 1 183 ? 8.670   -1.140  11.372  1.00 27.87  ?  185 LEU   A N    1 
ATOM   1417 C  CA   . LEU   A 1 183 ? 8.007   -2.383  10.958  1.00 29.84  ?  185 LEU   A CA   1 
ATOM   1418 C  C    . LEU   A 1 183 ? 6.478   -2.229  11.011  1.00 31.62  ?  185 LEU   A C    1 
ATOM   1419 O  O    . LEU   A 1 183 ? 5.775   -2.634  10.061  1.00 30.71  ?  185 LEU   A O    1 
ATOM   1420 C  CB   . LEU   A 1 183 ? 8.372   -3.580  11.818  1.00 27.66  ?  185 LEU   A CB   1 
ATOM   1421 C  CG   . LEU   A 1 183 ? 9.616   -4.432  11.541  1.00 29.27  ?  185 LEU   A CG   1 
ATOM   1422 C  CD1  . LEU   A 1 183 ? 10.142  -4.310  10.103  1.00 28.16  ?  185 LEU   A CD1  1 
ATOM   1423 C  CD2  . LEU   A 1 183 ? 10.729  -4.231  12.571  1.00 28.66  ?  185 LEU   A CD2  1 
ATOM   1424 N  N    . ARG   A 1 184 ? 5.980   -1.698  12.135  1.00 29.59  ?  186 ARG   A N    1 
ATOM   1425 C  CA   . ARG   A 1 184 ? 4.551   -1.500  12.322  1.00 31.74  ?  186 ARG   A CA   1 
ATOM   1426 C  C    . ARG   A 1 184 ? 4.004   -0.742  11.130  1.00 31.64  ?  186 ARG   A C    1 
ATOM   1427 O  O    . ARG   A 1 184 ? 3.113   -1.235  10.449  1.00 30.31  ?  186 ARG   A O    1 
ATOM   1428 C  CB   . ARG   A 1 184 ? 4.267   -0.750  13.642  1.00 32.78  ?  186 ARG   A CB   1 
ATOM   1429 C  CG   . ARG   A 1 184 ? 2.786   -0.574  13.998  1.00 32.50  ?  186 ARG   A CG   1 
ATOM   1430 C  CD   . ARG   A 1 184 ? 2.635   0.389   15.160  1.00 31.13  ?  186 ARG   A CD   1 
ATOM   1431 N  NE   . ARG   A 1 184 ? 3.175   1.712   14.837  1.00 32.69  ?  186 ARG   A NE   1 
ATOM   1432 N  N    . ASP   A 1 185 ? 4.572   0.435   10.883  1.00 31.20  ?  187 ASP   A N    1 
ATOM   1433 C  CA   . ASP   A 1 185 ? 4.181   1.295   9.768   1.00 35.55  ?  187 ASP   A CA   1 
ATOM   1434 C  C    . ASP   A 1 185 ? 4.156   0.551   8.416   1.00 35.36  ?  187 ASP   A C    1 
ATOM   1435 O  O    . ASP   A 1 185 ? 3.109   0.483   7.730   1.00 35.02  ?  187 ASP   A O    1 
ATOM   1436 C  CB   . ASP   A 1 185 ? 5.185   2.480   9.640   1.00 36.82  ?  187 ASP   A CB   1 
ATOM   1437 C  CG   . ASP   A 1 185 ? 4.968   3.585   10.665  1.00 39.83  ?  187 ASP   A CG   1 
ATOM   1438 O  OD1  . ASP   A 1 185 ? 4.173   3.412   11.624  1.00 49.59  ?  187 ASP   A OD1  1 
ATOM   1439 O  OD2  . ASP   A 1 185 ? 5.604   4.653   10.502  1.00 40.04  ?  187 ASP   A OD2  1 
ATOM   1440 N  N    . GLU   A 1 186 ? 5.320   -0.011  8.076   1.00 34.21  ?  188 GLU   A N    1 
ATOM   1441 C  CA   . GLU   A 1 186 ? 5.549   -0.729  6.836   1.00 34.89  ?  188 GLU   A CA   1 
ATOM   1442 C  C    . GLU   A 1 186 ? 4.625   -1.927  6.678   1.00 32.67  ?  188 GLU   A C    1 
ATOM   1443 O  O    . GLU   A 1 186 ? 4.215   -2.222  5.558   1.00 33.85  ?  188 GLU   A O    1 
ATOM   1444 C  CB   . GLU   A 1 186 ? 7.020   -1.201  6.738   1.00 38.26  ?  188 GLU   A CB   1 
ATOM   1445 C  CG   . GLU   A 1 186 ? 8.025   -0.080  6.521   1.00 42.16  ?  188 GLU   A CG   1 
ATOM   1446 C  CD   . GLU   A 1 186 ? 9.495   -0.504  6.676   1.00 48.56  ?  188 GLU   A CD   1 
ATOM   1447 O  OE1  . GLU   A 1 186 ? 9.829   -1.717  6.537   1.00 46.79  ?  188 GLU   A OE1  1 
ATOM   1448 O  OE2  . GLU   A 1 186 ? 10.338  0.408   6.923   1.00 54.83  ?  188 GLU   A OE2  1 
ATOM   1449 N  N    . GLY   A 1 187 ? 4.322   -2.620  7.783   1.00 31.46  ?  189 GLY   A N    1 
ATOM   1450 C  CA   . GLY   A 1 187 ? 3.329   -3.713  7.801   1.00 29.85  ?  189 GLY   A CA   1 
ATOM   1451 C  C    . GLY   A 1 187 ? 1.893   -3.255  7.584   1.00 31.66  ?  189 GLY   A C    1 
ATOM   1452 O  O    . GLY   A 1 187 ? 1.126   -3.876  6.826   1.00 32.00  ?  189 GLY   A O    1 
ATOM   1453 N  N    . LYS   A 1 188 ? 1.522   -2.150  8.219   1.00 33.10  ?  190 LYS   A N    1 
ATOM   1454 C  CA   . LYS   A 1 188 ? 0.208   -1.529  7.971   1.00 34.72  ?  190 LYS   A CA   1 
ATOM   1455 C  C    . LYS   A 1 188 ? 0.008   -1.067  6.498   1.00 30.77  ?  190 LYS   A C    1 
ATOM   1456 O  O    . LYS   A 1 188 ? -1.089  -1.232  5.926   1.00 32.05  ?  190 LYS   A O    1 
ATOM   1457 C  CB   . LYS   A 1 188 ? -0.024  -0.360  8.935   1.00 39.00  ?  190 LYS   A CB   1 
ATOM   1458 C  CG   . LYS   A 1 188 ? -0.250  -0.799  10.389  1.00 43.69  ?  190 LYS   A CG   1 
ATOM   1459 C  CD   . LYS   A 1 188 ? -1.732  -0.823  10.779  1.00 49.11  ?  190 LYS   A CD   1 
ATOM   1460 C  CE   . LYS   A 1 188 ? -2.393  0.552   10.719  1.00 50.87  ?  190 LYS   A CE   1 
ATOM   1461 N  NZ   . LYS   A 1 188 ? -1.578  1.621   11.366  1.00 52.30  ?  190 LYS   A NZ   1 
ATOM   1462 N  N    . ALA   A 1 189 ? 1.054   -0.501  5.911   1.00 30.28  ?  191 ALA   A N    1 
ATOM   1463 C  CA   . ALA   A 1 189 ? 1.031   -0.040  4.514   1.00 28.81  ?  191 ALA   A CA   1 
ATOM   1464 C  C    . ALA   A 1 189 ? 1.007   -1.219  3.538   1.00 28.61  ?  191 ALA   A C    1 
ATOM   1465 O  O    . ALA   A 1 189 ? 0.346   -1.159  2.498   1.00 28.42  ?  191 ALA   A O    1 
ATOM   1466 C  CB   . ALA   A 1 189 ? 2.221   0.840   4.239   1.00 27.73  ?  191 ALA   A CB   1 
ATOM   1467 N  N    . SER   A 1 190 ? 1.724   -2.295  3.868   1.00 27.70  ?  192 SER   A N    1 
ATOM   1468 C  CA   . SER   A 1 190 ? 1.688   -3.482  3.018   1.00 29.50  ?  192 SER   A CA   1 
ATOM   1469 C  C    . SER   A 1 190 ? 0.275   -4.072  2.933   1.00 26.89  ?  192 SER   A C    1 
ATOM   1470 O  O    . SER   A 1 190 ? -0.187  -4.417  1.868   1.00 28.36  ?  192 SER   A O    1 
ATOM   1471 C  CB   . SER   A 1 190 ? 2.683   -4.549  3.489   1.00 29.17  ?  192 SER   A CB   1 
ATOM   1472 O  OG   . SER   A 1 190 ? 2.500   -5.728  2.735   1.00 29.28  ?  192 SER   A OG   1 
ATOM   1473 N  N    . SER   A 1 191 ? -0.383  -4.171  4.073   1.00 29.84  ?  193 SER   A N    1 
ATOM   1474 C  CA   . SER   A 1 191 ? -1.722  -4.743  4.202   1.00 31.06  ?  193 SER   A CA   1 
ATOM   1475 C  C    . SER   A 1 191 ? -2.680  -3.899  3.366   1.00 30.27  ?  193 SER   A C    1 
ATOM   1476 O  O    . SER   A 1 191 ? -3.393  -4.449  2.568   1.00 28.44  ?  193 SER   A O    1 
ATOM   1477 C  CB   . SER   A 1 191 ? -2.124  -4.777  5.689   1.00 32.74  ?  193 SER   A CB   1 
ATOM   1478 O  OG   . SER   A 1 191 ? -3.437  -5.282  5.897   1.00 37.72  ?  193 SER   A OG   1 
ATOM   1479 N  N    . ALA   A 1 192 ? -2.633  -2.569  3.535   1.00 26.19  ?  194 ALA   A N    1 
ATOM   1480 C  CA   . ALA   A 1 192 ? -3.493  -1.626  2.814   1.00 26.35  ?  194 ALA   A CA   1 
ATOM   1481 C  C    . ALA   A 1 192 ? -3.262  -1.637  1.294   1.00 25.78  ?  194 ALA   A C    1 
ATOM   1482 O  O    . ALA   A 1 192 ? -4.229  -1.548  0.533   1.00 26.31  ?  194 ALA   A O    1 
ATOM   1483 C  CB   . ALA   A 1 192 ? -3.330  -0.201  3.367   1.00 25.23  ?  194 ALA   A CB   1 
ATOM   1484 N  N    . LYS   A 1 193 ? -2.008  -1.773  0.861   1.00 25.65  ?  195 LYS   A N    1 
ATOM   1485 C  CA   . LYS   A 1 193 ? -1.691  -1.892  -0.559  1.00 25.43  ?  195 LYS   A CA   1 
ATOM   1486 C  C    . LYS   A 1 193 ? -2.340  -3.122  -1.180  1.00 27.75  ?  195 LYS   A C    1 
ATOM   1487 O  O    . LYS   A 1 193 ? -2.829  -3.038  -2.328  1.00 27.63  ?  195 LYS   A O    1 
ATOM   1488 C  CB   . LYS   A 1 193 ? -0.185  -2.009  -0.825  1.00 28.24  ?  195 LYS   A CB   1 
ATOM   1489 C  CG   . LYS   A 1 193 ? 0.561   -0.723  -1.157  1.00 29.18  ?  195 LYS   A CG   1 
ATOM   1490 C  CD   . LYS   A 1 193 ? 1.880   -1.033  -1.848  1.00 30.09  ?  195 LYS   A CD   1 
ATOM   1491 C  CE   . LYS   A 1 193 ? 3.019   -0.162  -1.329  1.00 30.62  ?  195 LYS   A CE   1 
ATOM   1492 N  N    . GLN   A 1 194 ? -2.266  -4.270  -0.477  1.00 26.21  ?  196 GLN   A N    1 
ATOM   1493 C  CA   . GLN   A 1 194 ? -2.823  -5.535  -0.985  1.00 27.61  ?  196 GLN   A CA   1 
ATOM   1494 C  C    . GLN   A 1 194 ? -4.320  -5.420  -1.120  1.00 27.87  ?  196 GLN   A C    1 
ATOM   1495 O  O    . GLN   A 1 194 ? -4.905  -5.789  -2.145  1.00 26.53  ?  196 GLN   A O    1 
ATOM   1496 C  CB   . GLN   A 1 194 ? -2.475  -6.722  -0.071  1.00 27.60  ?  196 GLN   A CB   1 
ATOM   1497 C  CG   . GLN   A 1 194 ? -0.978  -7.051  -0.037  1.00 27.63  ?  196 GLN   A CG   1 
ATOM   1498 C  CD   . GLN   A 1 194 ? -0.658  -8.075  1.029   1.00 30.57  ?  196 GLN   A CD   1 
ATOM   1499 O  OE1  . GLN   A 1 194 ? -1.224  -9.184  1.026   1.00 27.31  ?  196 GLN   A OE1  1 
ATOM   1500 N  NE2  . GLN   A 1 194 ? 0.213   -7.707  1.977   1.00 31.15  ?  196 GLN   A NE2  1 
ATOM   1501 N  N    . ARG   A 1 195 ? -4.934  -4.876  -0.076  1.00 30.34  ?  197 ARG   A N    1 
ATOM   1502 C  CA   . ARG   A 1 195 ? -6.341  -4.538  -0.119  1.00 30.03  ?  197 ARG   A CA   1 
ATOM   1503 C  C    . ARG   A 1 195 ? -6.669  -3.618  -1.284  1.00 27.74  ?  197 ARG   A C    1 
ATOM   1504 O  O    . ARG   A 1 195 ? -7.586  -3.894  -2.022  1.00 26.02  ?  197 ARG   A O    1 
ATOM   1505 C  CB   . ARG   A 1 195 ? -6.751  -3.860  1.182   1.00 33.26  ?  197 ARG   A CB   1 
ATOM   1506 N  N    . LEU   A 1 196 ? -5.940  -2.513  -1.411  1.00 29.27  ?  198 LEU   A N    1 
ATOM   1507 C  CA   . LEU   A 1 196 ? -6.203  -1.472  -2.430  1.00 29.85  ?  198 LEU   A CA   1 
ATOM   1508 C  C    . LEU   A 1 196 ? -6.178  -2.067  -3.813  1.00 32.05  ?  198 LEU   A C    1 
ATOM   1509 O  O    . LEU   A 1 196 ? -7.036  -1.805  -4.650  1.00 33.29  ?  198 LEU   A O    1 
ATOM   1510 C  CB   . LEU   A 1 196 ? -5.140  -0.352  -2.391  1.00 29.65  ?  198 LEU   A CB   1 
ATOM   1511 C  CG   . LEU   A 1 196 ? -5.070  0.635   -3.578  1.00 30.53  ?  198 LEU   A CG   1 
ATOM   1512 C  CD1  . LEU   A 1 196 ? -6.245  1.566   -3.478  1.00 29.86  ?  198 LEU   A CD1  1 
ATOM   1513 C  CD2  . LEU   A 1 196 ? -3.773  1.457   -3.669  1.00 29.56  ?  198 LEU   A CD2  1 
ATOM   1514 N  N    . LYS   A 1 197 ? -5.181  -2.885  -4.052  1.00 32.94  ?  199 LYS   A N    1 
ATOM   1515 C  CA   . LYS   A 1 197 ? -4.943  -3.349  -5.395  1.00 34.53  ?  199 LYS   A CA   1 
ATOM   1516 C  C    . LYS   A 1 197 ? -6.016  -4.302  -5.886  1.00 30.44  ?  199 LYS   A C    1 
ATOM   1517 O  O    . LYS   A 1 197 ? -6.347  -4.280  -7.062  1.00 27.57  ?  199 LYS   A O    1 
ATOM   1518 C  CB   . LYS   A 1 197 ? -3.525  -3.885  -5.493  1.00 39.63  ?  199 LYS   A CB   1 
ATOM   1519 C  CG   . LYS   A 1 197 ? -2.533  -2.718  -5.548  1.00 46.81  ?  199 LYS   A CG   1 
ATOM   1520 C  CD   . LYS   A 1 197 ? -1.069  -3.133  -5.647  1.00 54.59  ?  199 LYS   A CD   1 
ATOM   1521 C  CE   . LYS   A 1 197 ? -0.407  -2.667  -6.957  1.00 64.05  ?  199 LYS   A CE   1 
ATOM   1522 N  NZ   . LYS   A 1 197 ? 0.644   -3.621  -7.457  1.00 70.59  ?  199 LYS   A NZ   1 
ATOM   1523 N  N    . CYS   A 1 198 ? -6.600  -5.075  -4.977  1.00 26.97  ?  200 CYS   A N    1 
ATOM   1524 C  CA   . CYS   A 1 198 ? -7.773  -5.926  -5.303  1.00 28.84  ?  200 CYS   A CA   1 
ATOM   1525 C  C    . CYS   A 1 198 ? -9.070  -5.111  -5.407  1.00 26.36  ?  200 CYS   A C    1 
ATOM   1526 O  O    . CYS   A 1 198 ? -9.907  -5.393  -6.272  1.00 24.92  ?  200 CYS   A O    1 
ATOM   1527 C  CB   . CYS   A 1 198 ? -7.912  -7.098  -4.300  1.00 27.74  ?  200 CYS   A CB   1 
ATOM   1528 S  SG   . CYS   A 1 198 ? -6.481  -8.230  -4.414  1.00 28.04  ?  200 CYS   A SG   1 
ATOM   1529 N  N    . ALA   A 1 199 ? -9.227  -4.081  -4.576  1.00 26.47  ?  201 ALA   A N    1 
ATOM   1530 C  CA   . ALA   A 1 199 ? -10.408 -3.225  -4.709  1.00 27.89  ?  201 ALA   A CA   1 
ATOM   1531 C  C    . ALA   A 1 199 ? -10.364 -2.507  -6.038  1.00 27.60  ?  201 ALA   A C    1 
ATOM   1532 O  O    . ALA   A 1 199 ? -11.311 -2.577  -6.781  1.00 28.47  ?  201 ALA   A O    1 
ATOM   1533 C  CB   . ALA   A 1 199 ? -10.541 -2.250  -3.569  1.00 29.41  ?  201 ALA   A CB   1 
ATOM   1534 N  N    . SER   A 1 200 ? -9.238  -1.883  -6.355  1.00 29.40  ?  202 SER   A N    1 
ATOM   1535 C  CA   . SER   A 1 200 ? -9.011  -1.247  -7.670  1.00 30.92  ?  202 SER   A CA   1 
ATOM   1536 C  C    . SER   A 1 200 ? -9.234  -2.142  -8.906  1.00 30.73  ?  202 SER   A C    1 
ATOM   1537 O  O    . SER   A 1 200 ? -9.768  -1.707  -9.925  1.00 30.76  ?  202 SER   A O    1 
ATOM   1538 C  CB   . SER   A 1 200 ? -7.583  -0.702  -7.729  1.00 30.60  ?  202 SER   A CB   1 
ATOM   1539 O  OG   . SER   A 1 200 ? -7.427  0.426   -6.886  1.00 30.59  ?  202 SER   A OG   1 
ATOM   1540 N  N    . LEU   A 1 201 ? -8.814  -3.385  -8.818  1.00 29.93  ?  203 LEU   A N    1 
ATOM   1541 C  CA   . LEU   A 1 201 ? -9.128  -4.353  -9.850  1.00 34.05  ?  203 LEU   A CA   1 
ATOM   1542 C  C    . LEU   A 1 201 ? -10.641 -4.472  -10.101 1.00 35.17  ?  203 LEU   A C    1 
ATOM   1543 O  O    . LEU   A 1 201 ? -11.088 -4.451  -11.257 1.00 40.06  ?  203 LEU   A O    1 
ATOM   1544 C  CB   . LEU   A 1 201 ? -8.554  -5.733  -9.486  1.00 35.38  ?  203 LEU   A CB   1 
ATOM   1545 C  CG   . LEU   A 1 201 ? -8.172  -6.734  -10.591 1.00 36.77  ?  203 LEU   A CG   1 
ATOM   1546 C  CD1  . LEU   A 1 201 ? -8.334  -8.169  -10.094 1.00 34.41  ?  203 LEU   A CD1  1 
ATOM   1547 C  CD2  . LEU   A 1 201 ? -8.906  -6.558  -11.906 1.00 37.21  ?  203 LEU   A CD2  1 
ATOM   1548 N  N    . GLN   A 1 202 ? -11.419 -4.629  -9.037  1.00 35.48  ?  204 GLN   A N    1 
ATOM   1549 C  CA   . GLN   A 1 202 ? -12.882 -4.754  -9.147  1.00 35.58  ?  204 GLN   A CA   1 
ATOM   1550 C  C    . GLN   A 1 202 ? -13.542 -3.451  -9.556  1.00 37.05  ?  204 GLN   A C    1 
ATOM   1551 O  O    . GLN   A 1 202 ? -14.379 -3.447  -10.446 1.00 37.43  ?  204 GLN   A O    1 
ATOM   1552 C  CB   . GLN   A 1 202 ? -13.487 -5.217  -7.824  1.00 37.67  ?  204 GLN   A CB   1 
ATOM   1553 N  N    . LYS   A 1 203 ? -13.163 -2.339  -8.936  1.00 39.65  ?  205 LYS   A N    1 
ATOM   1554 C  CA   . LYS   A 1 203 ? -13.849 -1.055  -9.203  1.00 44.72  ?  205 LYS   A CA   1 
ATOM   1555 C  C    . LYS   A 1 203 ? -13.554 -0.646  -10.624 1.00 44.89  ?  205 LYS   A C    1 
ATOM   1556 O  O    . LYS   A 1 203 ? -14.441 -0.593  -11.473 1.00 42.84  ?  205 LYS   A O    1 
ATOM   1557 C  CB   . LYS   A 1 203 ? -13.415 0.067   -8.228  1.00 49.32  ?  205 LYS   A CB   1 
ATOM   1558 C  CG   . LYS   A 1 203 ? -13.542 -0.315  -6.747  1.00 54.29  ?  205 LYS   A CG   1 
ATOM   1559 C  CD   . LYS   A 1 203 ? -14.111 0.769   -5.827  1.00 57.56  ?  205 LYS   A CD   1 
ATOM   1560 C  CE   . LYS   A 1 203 ? -13.050 1.692   -5.240  1.00 58.64  ?  205 LYS   A CE   1 
ATOM   1561 N  NZ   . LYS   A 1 203 ? -12.728 2.805   -6.170  1.00 57.95  ?  205 LYS   A NZ   1 
ATOM   1562 N  N    . PHE   A 1 204 ? -12.260 -0.462  -10.879 1.00 45.90  ?  206 PHE   A N    1 
ATOM   1563 C  CA   . PHE   A 1 204 ? -11.772 0.155   -12.099 1.00 39.81  ?  206 PHE   A CA   1 
ATOM   1564 C  C    . PHE   A 1 204 ? -11.488 -0.747  -13.281 1.00 33.49  ?  206 PHE   A C    1 
ATOM   1565 O  O    . PHE   A 1 204 ? -11.170 -0.236  -14.337 1.00 34.60  ?  206 PHE   A O    1 
ATOM   1566 C  CB   . PHE   A 1 204 ? -10.505 0.906   -11.785 1.00 41.35  ?  206 PHE   A CB   1 
ATOM   1567 C  CG   . PHE   A 1 204 ? -10.687 2.000   -10.815 1.00 44.20  ?  206 PHE   A CG   1 
ATOM   1568 C  CD1  . PHE   A 1 204 ? -11.440 3.123   -11.161 1.00 45.61  ?  206 PHE   A CD1  1 
ATOM   1569 C  CD2  . PHE   A 1 204 ? -10.068 1.955   -9.573  1.00 47.40  ?  206 PHE   A CD2  1 
ATOM   1570 C  CE1  . PHE   A 1 204 ? -11.598 4.172   -10.269 1.00 45.44  ?  206 PHE   A CE1  1 
ATOM   1571 C  CE2  . PHE   A 1 204 ? -10.210 3.008   -8.679  1.00 49.09  ?  206 PHE   A CE2  1 
ATOM   1572 C  CZ   . PHE   A 1 204 ? -10.978 4.117   -9.024  1.00 47.09  ?  206 PHE   A CZ   1 
ATOM   1573 N  N    . GLY   A 1 205 ? -11.544 -2.062  -13.116 1.00 28.95  ?  207 GLY   A N    1 
ATOM   1574 C  CA   . GLY   A 1 205 ? -11.375 -2.974  -14.229 1.00 29.40  ?  207 GLY   A CA   1 
ATOM   1575 C  C    . GLY   A 1 205 ? -9.977  -3.366  -14.712 1.00 29.54  ?  207 GLY   A C    1 
ATOM   1576 O  O    . GLY   A 1 205 ? -8.953  -2.697  -14.424 1.00 26.06  ?  207 GLY   A O    1 
ATOM   1577 N  N    . GLU   A 1 206 ? -10.006 -4.439  -15.511 1.00 31.11  ?  208 GLU   A N    1 
ATOM   1578 C  CA   . GLU   A 1 206 ? -8.845  -5.090  -16.153 1.00 33.38  ?  208 GLU   A CA   1 
ATOM   1579 C  C    . GLU   A 1 206 ? -8.024  -4.157  -17.065 1.00 32.00  ?  208 GLU   A C    1 
ATOM   1580 O  O    . GLU   A 1 206 ? -6.795  -4.149  -17.005 1.00 25.71  ?  208 GLU   A O    1 
ATOM   1581 C  CB   . GLU   A 1 206 ? -9.283  -6.352  -16.932 1.00 35.28  ?  208 GLU   A CB   1 
ATOM   1582 C  CG   . GLU   A 1 206 ? -8.232  -7.466  -16.925 1.00 40.05  ?  208 GLU   A CG   1 
ATOM   1583 C  CD   . GLU   A 1 206 ? -8.797  -8.897  -16.937 1.00 43.33  ?  208 GLU   A CD   1 
ATOM   1584 O  OE1  . GLU   A 1 206 ? -9.992  -9.110  -17.242 1.00 41.99  ?  208 GLU   A OE1  1 
ATOM   1585 O  OE2  . GLU   A 1 206 ? -8.021  -9.839  -16.635 1.00 48.94  ?  208 GLU   A OE2  1 
ATOM   1586 N  N    . ARG   A 1 207 ? -8.713  -3.348  -17.865 1.00 31.53  ?  209 ARG   A N    1 
ATOM   1587 C  CA   . ARG   A 1 207 ? -8.057  -2.332  -18.716 1.00 29.96  ?  209 ARG   A CA   1 
ATOM   1588 C  C    . ARG   A 1 207 ? -7.148  -1.403  -17.898 1.00 27.37  ?  209 ARG   A C    1 
ATOM   1589 O  O    . ARG   A 1 207 ? -5.951  -1.317  -18.123 1.00 26.41  ?  209 ARG   A O    1 
ATOM   1590 C  CB   . ARG   A 1 207 ? -9.106  -1.507  -19.484 1.00 30.91  ?  209 ARG   A CB   1 
ATOM   1591 C  CG   . ARG   A 1 207 ? -8.543  -0.783  -20.701 1.00 32.92  ?  209 ARG   A CG   1 
ATOM   1592 C  CD   . ARG   A 1 207 ? -9.655  -0.294  -21.601 1.00 34.25  ?  209 ARG   A CD   1 
ATOM   1593 N  NE   . ARG   A 1 207 ? -9.170  0.480   -22.728 1.00 32.72  ?  209 ARG   A NE   1 
ATOM   1594 C  CZ   . ARG   A 1 207 ? -8.985  1.802   -22.718 1.00 36.92  ?  209 ARG   A CZ   1 
ATOM   1595 N  NH1  . ARG   A 1 207 ? -9.229  2.554   -21.627 1.00 34.58  ?  209 ARG   A NH1  1 
ATOM   1596 N  NH2  . ARG   A 1 207 ? -8.551  2.394   -23.835 1.00 37.33  ?  209 ARG   A NH2  1 
ATOM   1597 N  N    . ALA   A 1 208 ? -7.740  -0.745  -16.916 1.00 28.26  ?  210 ALA   A N    1 
ATOM   1598 C  CA   . ALA   A 1 208 ? -7.040  0.148   -15.991 1.00 25.40  ?  210 ALA   A CA   1 
ATOM   1599 C  C    . ALA   A 1 208 ? -5.831  -0.554  -15.337 1.00 23.33  ?  210 ALA   A C    1 
ATOM   1600 O  O    . ALA   A 1 208 ? -4.780  0.053   -15.122 1.00 20.79  ?  210 ALA   A O    1 
ATOM   1601 C  CB   . ALA   A 1 208 ? -8.020  0.623   -14.935 1.00 24.56  ?  210 ALA   A CB   1 
ATOM   1602 N  N    . PHE   A 1 209 ? -5.982  -1.838  -15.024 1.00 22.41  ?  211 PHE   A N    1 
ATOM   1603 C  CA   . PHE   A 1 209 ? -4.927  -2.558  -14.371 1.00 21.01  ?  211 PHE   A CA   1 
ATOM   1604 C  C    . PHE   A 1 209 ? -3.789  -2.736  -15.342 1.00 19.58  ?  211 PHE   A C    1 
ATOM   1605 O  O    . PHE   A 1 209 ? -2.600  -2.501  -14.974 1.00 17.43  ?  211 PHE   A O    1 
ATOM   1606 C  CB   . PHE   A 1 209 ? -5.390  -3.899  -13.813 1.00 24.51  ?  211 PHE   A CB   1 
ATOM   1607 C  CG   . PHE   A 1 209 ? -4.285  -4.678  -13.173 1.00 25.81  ?  211 PHE   A CG   1 
ATOM   1608 C  CD1  . PHE   A 1 209 ? -3.515  -5.526  -13.923 1.00 26.45  ?  211 PHE   A CD1  1 
ATOM   1609 C  CD2  . PHE   A 1 209 ? -3.979  -4.509  -11.841 1.00 29.84  ?  211 PHE   A CD2  1 
ATOM   1610 C  CE1  . PHE   A 1 209 ? -2.480  -6.231  -13.366 1.00 27.80  ?  211 PHE   A CE1  1 
ATOM   1611 C  CE2  . PHE   A 1 209 ? -2.935  -5.225  -11.255 1.00 29.94  ?  211 PHE   A CE2  1 
ATOM   1612 C  CZ   . PHE   A 1 209 ? -2.177  -6.076  -12.034 1.00 29.15  ?  211 PHE   A CZ   1 
ATOM   1613 N  N    . LYS   A 1 210 ? -4.146  -3.095  -16.579 1.00 19.50  ?  212 LYS   A N    1 
ATOM   1614 C  CA   . LYS   A 1 210 ? -3.167  -3.313  -17.615 1.00 20.05  ?  212 LYS   A CA   1 
ATOM   1615 C  C    . LYS   A 1 210 ? -2.444  -2.037  -17.900 1.00 17.97  ?  212 LYS   A C    1 
ATOM   1616 O  O    . LYS   A 1 210 ? -1.231  -2.041  -18.026 1.00 17.13  ?  212 LYS   A O    1 
ATOM   1617 C  CB   . LYS   A 1 210 ? -3.766  -3.926  -18.888 1.00 23.47  ?  212 LYS   A CB   1 
ATOM   1618 C  CG   . LYS   A 1 210 ? -3.918  -5.431  -18.735 1.00 26.77  ?  212 LYS   A CG   1 
ATOM   1619 C  CD   . LYS   A 1 210 ? -4.777  -6.063  -19.782 1.00 27.34  ?  212 LYS   A CD   1 
ATOM   1620 C  CE   . LYS   A 1 210 ? -4.594  -7.562  -19.607 1.00 30.81  ?  212 LYS   A CE   1 
ATOM   1621 N  NZ   . LYS   A 1 210 ? -5.808  -8.318  -19.955 1.00 34.03  ?  212 LYS   A NZ   1 
ATOM   1622 N  N    . ALA   A 1 211 ? -3.162  -0.931  -17.937 1.00 16.53  ?  213 ALA   A N    1 
ATOM   1623 C  CA   . ALA   A 1 211 ? -2.459  0.342   -18.161 1.00 17.50  ?  213 ALA   A CA   1 
ATOM   1624 C  C    . ALA   A 1 211 ? -1.452  0.611   -17.056 1.00 16.93  ?  213 ALA   A C    1 
ATOM   1625 O  O    . ALA   A 1 211 ? -0.274  0.798   -17.343 1.00 18.38  ?  213 ALA   A O    1 
ATOM   1626 C  CB   . ALA   A 1 211 ? -3.440  1.487   -18.368 1.00 17.57  ?  213 ALA   A CB   1 
ATOM   1627 N  N    . TRP   A 1 212 ? -1.895  0.528   -15.807 1.00 18.16  ?  214 TRP   A N    1 
ATOM   1628 C  CA   . TRP   A 1 212 ? -1.030  0.688   -14.648 1.00 18.39  ?  214 TRP   A CA   1 
ATOM   1629 C  C    . TRP   A 1 212 ? 0.216   -0.166  -14.785 1.00 16.67  ?  214 TRP   A C    1 
ATOM   1630 O  O    . TRP   A 1 212 ? 1.303   0.331   -14.721 1.00 12.72  ?  214 TRP   A O    1 
ATOM   1631 C  CB   . TRP   A 1 212 ? -1.791  0.392   -13.323 1.00 22.30  ?  214 TRP   A CB   1 
ATOM   1632 C  CG   . TRP   A 1 212 ? -1.051  0.867   -12.132 1.00 28.37  ?  214 TRP   A CG   1 
ATOM   1633 C  CD1  . TRP   A 1 212 ? -0.986  2.161   -11.692 1.00 30.09  ?  214 TRP   A CD1  1 
ATOM   1634 C  CD2  . TRP   A 1 212 ? -0.242  0.088   -11.223 1.00 33.02  ?  214 TRP   A CD2  1 
ATOM   1635 N  NE1  . TRP   A 1 212 ? -0.179  2.242   -10.588 1.00 33.42  ?  214 TRP   A NE1  1 
ATOM   1636 C  CE2  . TRP   A 1 212 ? 0.276   0.986   -10.264 1.00 35.48  ?  214 TRP   A CE2  1 
ATOM   1637 C  CE3  . TRP   A 1 212 ? 0.046   -1.293  -11.094 1.00 40.47  ?  214 TRP   A CE3  1 
ATOM   1638 C  CZ2  . TRP   A 1 212 ? 1.111   0.565   -9.193  1.00 42.81  ?  214 TRP   A CZ2  1 
ATOM   1639 C  CZ3  . TRP   A 1 212 ? 0.881   -1.729  -10.012 1.00 42.02  ?  214 TRP   A CZ3  1 
ATOM   1640 C  CH2  . TRP   A 1 212 ? 1.400   -0.795  -9.083  1.00 44.11  ?  214 TRP   A CH2  1 
ATOM   1641 N  N    . ALA   A 1 213 ? 0.035   -1.458  -15.049 1.00 16.33  ?  215 ALA   A N    1 
ATOM   1642 C  CA   . ALA   A 1 213 ? 1.134   -2.381  -15.119 1.00 16.90  ?  215 ALA   A CA   1 
ATOM   1643 C  C    . ALA   A 1 213 ? 2.086   -2.105  -16.316 1.00 17.12  ?  215 ALA   A C    1 
ATOM   1644 O  O    . ALA   A 1 213 ? 3.294   -2.241  -16.157 1.00 16.86  ?  215 ALA   A O    1 
ATOM   1645 C  CB   . ALA   A 1 213 ? 0.600   -3.816  -15.155 1.00 18.33  ?  215 ALA   A CB   1 
ATOM   1646 N  N    . VAL   A 1 214 ? 1.549   -1.711  -17.478 1.00 16.25  ?  216 VAL   A N    1 
ATOM   1647 C  CA   . VAL   A 1 214 ? 2.343   -1.362  -18.622 1.00 17.06  ?  216 VAL   A CA   1 
ATOM   1648 C  C    . VAL   A 1 214 ? 3.212   -0.169  -18.268 1.00 16.47  ?  216 VAL   A C    1 
ATOM   1649 O  O    . VAL   A 1 214 ? 4.445   -0.160  -18.554 1.00 17.97  ?  216 VAL   A O    1 
ATOM   1650 C  CB   . VAL   A 1 214 ? 1.505   -0.992  -19.883 1.00 18.41  ?  216 VAL   A CB   1 
ATOM   1651 C  CG1  . VAL   A 1 214 ? 2.429   -0.537  -20.991 1.00 19.19  ?  216 VAL   A CG1  1 
ATOM   1652 C  CG2  . VAL   A 1 214 ? 0.658   -2.155  -20.341 1.00 19.65  ?  216 VAL   A CG2  1 
ATOM   1653 N  N    . ALA   A 1 215 ? 2.627   0.803   -17.602 1.00 15.38  ?  217 ALA   A N    1 
ATOM   1654 C  CA   . ALA   A 1 215 ? 3.437   1.946   -17.125 1.00 16.75  ?  217 ALA   A CA   1 
ATOM   1655 C  C    . ALA   A 1 215 ? 4.498   1.539   -16.099 1.00 17.75  ?  217 ALA   A C    1 
ATOM   1656 O  O    . ALA   A 1 215 ? 5.691   1.842   -16.277 1.00 17.07  ?  217 ALA   A O    1 
ATOM   1657 C  CB   . ALA   A 1 215 ? 2.572   3.062   -16.561 1.00 15.98  ?  217 ALA   A CB   1 
ATOM   1658 N  N    . ARG   A 1 216 ? 4.115   0.816   -15.053 1.00 19.39  ?  218 ARG   A N    1 
ATOM   1659 C  CA   . ARG   A 1 216 ? 5.116   0.478   -14.023 1.00 21.73  ?  218 ARG   A CA   1 
ATOM   1660 C  C    . ARG   A 1 216 ? 6.222   -0.433  -14.548 1.00 20.80  ?  218 ARG   A C    1 
ATOM   1661 O  O    . ARG   A 1 216 ? 7.378   -0.300  -14.139 1.00 18.96  ?  218 ARG   A O    1 
ATOM   1662 C  CB   . ARG   A 1 216 ? 4.494   -0.129  -12.747 1.00 23.70  ?  218 ARG   A CB   1 
ATOM   1663 C  CG   . ARG   A 1 216 ? 5.496   -0.395  -11.634 1.00 25.87  ?  218 ARG   A CG   1 
ATOM   1664 C  CD   . ARG   A 1 216 ? 6.246   0.866   -11.168 1.00 30.56  ?  218 ARG   A CD   1 
ATOM   1665 N  NE   . ARG   A 1 216 ? 5.703   1.293   -9.897  1.00 35.42  ?  218 ARG   A NE   1 
ATOM   1666 C  CZ   . ARG   A 1 216 ? 5.597   2.548   -9.451  1.00 43.11  ?  218 ARG   A CZ   1 
ATOM   1667 N  NH1  . ARG   A 1 216 ? 6.041   3.621   -10.142 1.00 45.89  ?  218 ARG   A NH1  1 
ATOM   1668 N  NH2  . ARG   A 1 216 ? 5.029   2.733   -8.252  1.00 47.74  ?  218 ARG   A NH2  1 
ATOM   1669 N  N    . LEU   A 1 217 ? 5.865   -1.353  -15.446 1.00 21.02  ?  219 LEU   A N    1 
ATOM   1670 C  CA   . LEU   A 1 217 ? 6.834   -2.318  -15.906 1.00 21.60  ?  219 LEU   A CA   1 
ATOM   1671 C  C    . LEU   A 1 217 ? 7.839   -1.703  -16.853 1.00 20.51  ?  219 LEU   A C    1 
ATOM   1672 O  O    . LEU   A 1 217 ? 9.014   -2.021  -16.775 1.00 18.21  ?  219 LEU   A O    1 
ATOM   1673 C  CB   . LEU   A 1 217 ? 6.165   -3.547  -16.491 1.00 21.91  ?  219 LEU   A CB   1 
ATOM   1674 C  CG   . LEU   A 1 217 ? 5.573   -4.460  -15.406 1.00 22.48  ?  219 LEU   A CG   1 
ATOM   1675 C  CD1  . LEU   A 1 217 ? 5.149   -5.772  -16.010 1.00 23.65  ?  219 LEU   A CD1  1 
ATOM   1676 C  CD2  . LEU   A 1 217 ? 6.531   -4.786  -14.271 1.00 23.45  ?  219 LEU   A CD2  1 
ATOM   1677 N  N    . SER   A 1 218 ? 7.373   -0.777  -17.688 1.00 20.40  ?  220 SER   A N    1 
ATOM   1678 C  CA   . SER   A 1 218 ? 8.221   -0.058  -18.604 1.00 21.84  ?  220 SER   A CA   1 
ATOM   1679 C  C    . SER   A 1 218 ? 9.225   0.845   -17.911 1.00 22.03  ?  220 SER   A C    1 
ATOM   1680 O  O    . SER   A 1 218 ? 10.339  0.990   -18.402 1.00 22.95  ?  220 SER   A O    1 
ATOM   1681 C  CB   . SER   A 1 218 ? 7.386   0.774   -19.555 1.00 22.11  ?  220 SER   A CB   1 
ATOM   1682 O  OG   . SER   A 1 218 ? 6.368   -0.038  -20.076 1.00 21.70  ?  220 SER   A OG   1 
ATOM   1683 N  N    . GLN   A 1 219 ? 8.843   1.449   -16.794 1.00 22.08  ?  221 GLN   A N    1 
ATOM   1684 C  CA   . GLN   A 1 219 ? 9.826   2.194   -15.954 1.00 22.35  ?  221 GLN   A CA   1 
ATOM   1685 C  C    . GLN   A 1 219 ? 10.873  1.262   -15.366 1.00 21.88  ?  221 GLN   A C    1 
ATOM   1686 O  O    . GLN   A 1 219 ? 12.048  1.553   -15.409 1.00 20.61  ?  221 GLN   A O    1 
ATOM   1687 C  CB   . GLN   A 1 219 ? 9.133   2.925   -14.817 1.00 22.02  ?  221 GLN   A CB   1 
ATOM   1688 C  CG   . GLN   A 1 219 ? 8.151   4.013   -15.236 1.00 21.31  ?  221 GLN   A CG   1 
ATOM   1689 C  CD   . GLN   A 1 219 ? 7.453   4.600   -14.045 1.00 21.11  ?  221 GLN   A CD   1 
ATOM   1690 O  OE1  . GLN   A 1 219 ? 6.876   3.861   -13.246 1.00 20.89  ?  221 GLN   A OE1  1 
ATOM   1691 N  NE2  . GLN   A 1 219 ? 7.529   5.928   -13.890 1.00 19.60  ?  221 GLN   A NE2  1 
ATOM   1692 N  N    . ARG   A 1 220 ? 10.417  0.126   -14.833 1.00 23.88  ?  222 ARG   A N    1 
ATOM   1693 C  CA   . ARG   A 1 220 ? 11.292  -0.879  -14.237 1.00 22.33  ?  222 ARG   A CA   1 
ATOM   1694 C  C    . ARG   A 1 220 ? 12.260  -1.556  -15.168 1.00 20.65  ?  222 ARG   A C    1 
ATOM   1695 O  O    . ARG   A 1 220 ? 13.413  -1.818  -14.786 1.00 20.28  ?  222 ARG   A O    1 
ATOM   1696 C  CB   . ARG   A 1 220 ? 10.471  -1.963  -13.526 1.00 27.39  ?  222 ARG   A CB   1 
ATOM   1697 C  CG   . ARG   A 1 220 ? 10.385  -1.769  -12.015 1.00 34.65  ?  222 ARG   A CG   1 
ATOM   1698 C  CD   . ARG   A 1 220 ? 9.651   -2.947  -11.362 1.00 38.86  ?  222 ARG   A CD   1 
ATOM   1699 N  NE   . ARG   A 1 220 ? 8.658   -2.470  -10.416 1.00 40.39  ?  222 ARG   A NE   1 
ATOM   1700 C  CZ   . ARG   A 1 220 ? 8.897   -2.175  -9.145  1.00 47.02  ?  222 ARG   A CZ   1 
ATOM   1701 N  NH1  . ARG   A 1 220 ? 10.103  -2.344  -8.595  1.00 48.69  ?  222 ARG   A NH1  1 
ATOM   1702 N  NH2  . ARG   A 1 220 ? 7.901   -1.733  -8.394  1.00 51.96  ?  222 ARG   A NH2  1 
ATOM   1703 N  N    . PHE   A 1 221 ? 11.785  -1.870  -16.371 1.00 19.97  ?  223 PHE   A N    1 
ATOM   1704 C  CA   . PHE   A 1 221 ? 12.512  -2.643  -17.357 1.00 20.22  ?  223 PHE   A CA   1 
ATOM   1705 C  C    . PHE   A 1 221 ? 12.511  -1.910  -18.677 1.00 19.67  ?  223 PHE   A C    1 
ATOM   1706 O  O    . PHE   A 1 221 ? 11.985  -2.407  -19.654 1.00 18.89  ?  223 PHE   A O    1 
ATOM   1707 C  CB   . PHE   A 1 221 ? 11.845  -3.995  -17.592 1.00 21.11  ?  223 PHE   A CB   1 
ATOM   1708 C  CG   . PHE   A 1 221 ? 11.548  -4.769  -16.347 1.00 22.40  ?  223 PHE   A CG   1 
ATOM   1709 C  CD1  . PHE   A 1 221 ? 12.516  -4.942  -15.364 1.00 22.89  ?  223 PHE   A CD1  1 
ATOM   1710 C  CD2  . PHE   A 1 221 ? 10.304  -5.390  -16.172 1.00 22.25  ?  223 PHE   A CD2  1 
ATOM   1711 C  CE1  . PHE   A 1 221 ? 12.254  -5.705  -14.245 1.00 22.18  ?  223 PHE   A CE1  1 
ATOM   1712 C  CE2  . PHE   A 1 221 ? 10.055  -6.162  -15.053 1.00 20.15  ?  223 PHE   A CE2  1 
ATOM   1713 C  CZ   . PHE   A 1 221 ? 11.018  -6.308  -14.092 1.00 20.16  ?  223 PHE   A CZ   1 
ATOM   1714 N  N    . PRO   A 1 222 ? 13.079  -0.698  -18.706 1.00 20.11  ?  224 PRO   A N    1 
ATOM   1715 C  CA   . PRO   A 1 222 ? 13.080  0.083   -19.906 1.00 21.16  ?  224 PRO   A CA   1 
ATOM   1716 C  C    . PRO   A 1 222 ? 13.822  -0.576  -21.098 1.00 23.33  ?  224 PRO   A C    1 
ATOM   1717 O  O    . PRO   A 1 222 ? 13.474  -0.270  -22.244 1.00 22.68  ?  224 PRO   A O    1 
ATOM   1718 C  CB   . PRO   A 1 222 ? 13.712  1.401   -19.454 1.00 20.48  ?  224 PRO   A CB   1 
ATOM   1719 C  CG   . PRO   A 1 222 ? 14.582  1.029   -18.332 1.00 20.60  ?  224 PRO   A CG   1 
ATOM   1720 C  CD   . PRO   A 1 222 ? 13.872  -0.076  -17.650 1.00 20.13  ?  224 PRO   A CD   1 
ATOM   1721 N  N    . LYS   A 1 223 ? 14.787  -1.476  -20.859 1.00 23.77  ?  225 LYS   A N    1 
ATOM   1722 C  CA   . LYS   A 1 223 ? 15.467  -2.170  -21.966 1.00 26.78  ?  225 LYS   A CA   1 
ATOM   1723 C  C    . LYS   A 1 223 ? 14.596  -3.241  -22.651 1.00 25.41  ?  225 LYS   A C    1 
ATOM   1724 O  O    . LYS   A 1 223 ? 14.890  -3.638  -23.764 1.00 24.67  ?  225 LYS   A O    1 
ATOM   1725 C  CB   . LYS   A 1 223 ? 16.812  -2.761  -21.528 1.00 28.88  ?  225 LYS   A CB   1 
ATOM   1726 C  CG   . LYS   A 1 223 ? 17.777  -1.661  -21.142 1.00 33.54  ?  225 LYS   A CG   1 
ATOM   1727 C  CD   . LYS   A 1 223 ? 19.199  -2.157  -20.904 1.00 38.62  ?  225 LYS   A CD   1 
ATOM   1728 C  CE   . LYS   A 1 223 ? 20.205  -1.054  -21.224 1.00 40.96  ?  225 LYS   A CE   1 
ATOM   1729 N  NZ   . LYS   A 1 223 ? 21.199  -0.848  -20.132 1.00 44.14  ?  225 LYS   A NZ   1 
ATOM   1730 N  N    . ALA   A 1 224 ? 13.532  -3.697  -21.982 1.00 25.27  ?  226 ALA   A N    1 
ATOM   1731 C  CA   . ALA   A 1 224 ? 12.620  -4.692  -22.568 1.00 24.96  ?  226 ALA   A CA   1 
ATOM   1732 C  C    . ALA   A 1 224 ? 11.811  -4.154  -23.763 1.00 24.60  ?  226 ALA   A C    1 
ATOM   1733 O  O    . ALA   A 1 224 ? 11.296  -3.020  -23.732 1.00 20.84  ?  226 ALA   A O    1 
ATOM   1734 C  CB   . ALA   A 1 224 ? 11.673  -5.216  -21.518 1.00 24.58  ?  226 ALA   A CB   1 
ATOM   1735 N  N    . GLU   A 1 225 ? 11.673  -4.992  -24.792 1.00 24.64  ?  227 GLU   A N    1 
ATOM   1736 C  CA   . GLU   A 1 225 ? 10.893  -4.608  -25.980 1.00 27.15  ?  227 GLU   A CA   1 
ATOM   1737 C  C    . GLU   A 1 225 ? 9.414   -4.645  -25.572 1.00 27.49  ?  227 GLU   A C    1 
ATOM   1738 O  O    . GLU   A 1 225 ? 9.057   -5.324  -24.596 1.00 29.34  ?  227 GLU   A O    1 
ATOM   1739 C  CB   . GLU   A 1 225 ? 11.202  -5.518  -27.193 1.00 26.09  ?  227 GLU   A CB   1 
ATOM   1740 N  N    . PHE   A 1 226 ? 8.576   -3.880  -26.276 1.00 24.74  ?  228 PHE   A N    1 
ATOM   1741 C  CA   . PHE   A 1 226 ? 7.152   -3.751  -25.922 1.00 22.93  ?  228 PHE   A CA   1 
ATOM   1742 C  C    . PHE   A 1 226 ? 6.378   -5.083  -25.866 1.00 21.42  ?  228 PHE   A C    1 
ATOM   1743 O  O    . PHE   A 1 226 ? 5.476   -5.242  -25.064 1.00 20.33  ?  228 PHE   A O    1 
ATOM   1744 C  CB   . PHE   A 1 226 ? 6.431   -2.849  -26.905 1.00 21.47  ?  228 PHE   A CB   1 
ATOM   1745 C  CG   . PHE   A 1 226 ? 4.954   -2.790  -26.659 1.00 22.28  ?  228 PHE   A CG   1 
ATOM   1746 C  CD1  . PHE   A 1 226 ? 4.460   -2.151  -25.532 1.00 21.77  ?  228 PHE   A CD1  1 
ATOM   1747 C  CD2  . PHE   A 1 226 ? 4.052   -3.397  -27.543 1.00 23.03  ?  228 PHE   A CD2  1 
ATOM   1748 C  CE1  . PHE   A 1 226 ? 3.095   -2.090  -25.295 1.00 21.98  ?  228 PHE   A CE1  1 
ATOM   1749 C  CE2  . PHE   A 1 226 ? 2.673   -3.354  -27.305 1.00 23.73  ?  228 PHE   A CE2  1 
ATOM   1750 C  CZ   . PHE   A 1 226 ? 2.199   -2.701  -26.182 1.00 23.17  ?  228 PHE   A CZ   1 
ATOM   1751 N  N    . ALA   A 1 227 ? 6.671   -5.974  -26.788 1.00 20.88  ?  229 ALA   A N    1 
ATOM   1752 C  CA   . ALA   A 1 227 ? 6.078   -7.307  -26.781 1.00 21.88  ?  229 ALA   A CA   1 
ATOM   1753 C  C    . ALA   A 1 227 ? 6.396   -8.065  -25.494 1.00 22.08  ?  229 ALA   A C    1 
ATOM   1754 O  O    . ALA   A 1 227 ? 5.526   -8.736  -24.978 1.00 22.79  ?  229 ALA   A O    1 
ATOM   1755 C  CB   . ALA   A 1 227 ? 6.568   -8.104  -27.964 1.00 21.92  ?  229 ALA   A CB   1 
ATOM   1756 N  N    . GLU   A 1 228 ? 7.625   -7.933  -24.978 1.00 22.05  ?  230 GLU   A N    1 
ATOM   1757 C  CA   . GLU   A 1 228 ? 7.977   -8.535  -23.685 1.00 23.15  ?  230 GLU   A CA   1 
ATOM   1758 C  C    . GLU   A 1 228 ? 7.209   -7.935  -22.518 1.00 20.76  ?  230 GLU   A C    1 
ATOM   1759 O  O    . GLU   A 1 228 ? 6.700   -8.667  -21.662 1.00 19.64  ?  230 GLU   A O    1 
ATOM   1760 C  CB   . GLU   A 1 228 ? 9.483   -8.472  -23.371 1.00 22.39  ?  230 GLU   A CB   1 
ATOM   1761 C  CG   . GLU   A 1 228 ? 9.841   -9.307  -22.166 1.00 21.89  ?  230 GLU   A CG   1 
ATOM   1762 C  CD   . GLU   A 1 228 ? 9.741   -10.806 -22.425 1.00 23.88  ?  230 GLU   A CD   1 
ATOM   1763 O  OE1  . GLU   A 1 228 ? 10.199  -11.237 -23.479 1.00 28.64  ?  230 GLU   A OE1  1 
ATOM   1764 O  OE2  . GLU   A 1 228 ? 9.252   -11.574 -21.570 1.00 24.16  ?  230 GLU   A OE2  1 
ATOM   1765 N  N    . VAL   A 1 229 ? 7.138   -6.605  -22.499 1.00 20.46  ?  231 VAL   A N    1 
ATOM   1766 C  CA   . VAL   A 1 229 ? 6.346   -5.891  -21.528 1.00 19.38  ?  231 VAL   A CA   1 
ATOM   1767 C  C    . VAL   A 1 229 ? 4.880   -6.368  -21.606 1.00 18.21  ?  231 VAL   A C    1 
ATOM   1768 O  O    . VAL   A 1 229 ? 4.301   -6.596  -20.593 1.00 16.43  ?  231 VAL   A O    1 
ATOM   1769 C  CB   . VAL   A 1 229 ? 6.421   -4.343  -21.723 1.00 19.86  ?  231 VAL   A CB   1 
ATOM   1770 C  CG1  . VAL   A 1 229 ? 5.232   -3.641  -21.063 1.00 19.57  ?  231 VAL   A CG1  1 
ATOM   1771 C  CG2  . VAL   A 1 229 ? 7.750   -3.779  -21.217 1.00 20.27  ?  231 VAL   A CG2  1 
ATOM   1772 N  N    . SER   A 1 230 ? 4.297   -6.507  -22.788 1.00 19.34  ?  232 SER   A N    1 
ATOM   1773 C  CA   . SER   A 1 230 ? 2.842   -6.840  -22.897 1.00 22.26  ?  232 SER   A CA   1 
ATOM   1774 C  C    . SER   A 1 230 ? 2.615   -8.267  -22.499 1.00 20.71  ?  232 SER   A C    1 
ATOM   1775 O  O    . SER   A 1 230 ? 1.516   -8.639  -22.112 1.00 21.30  ?  232 SER   A O    1 
ATOM   1776 C  CB   . SER   A 1 230 ? 2.303   -6.681  -24.318 1.00 25.40  ?  232 SER   A CB   1 
ATOM   1777 O  OG   . SER   A 1 230 ? 2.777   -5.451  -24.868 1.00 37.16  ?  232 SER   A OG   1 
ATOM   1778 N  N    . LYS   A 1 231 ? 3.650   -9.073  -22.647 1.00 21.70  ?  233 LYS   A N    1 
ATOM   1779 C  CA   . LYS   A 1 231 ? 3.583   -10.466 -22.233 1.00 22.28  ?  233 LYS   A CA   1 
ATOM   1780 C  C    . LYS   A 1 231 ? 3.621   -10.499 -20.703 1.00 22.42  ?  233 LYS   A C    1 
ATOM   1781 O  O    . LYS   A 1 231 ? 2.841   -11.193 -20.062 1.00 21.85  ?  233 LYS   A O    1 
ATOM   1782 C  CB   . LYS   A 1 231 ? 4.716   -11.236 -22.892 1.00 23.90  ?  233 LYS   A CB   1 
ATOM   1783 C  CG   . LYS   A 1 231 ? 4.366   -12.650 -23.279 1.00 25.23  ?  233 LYS   A CG   1 
ATOM   1784 C  CD   . LYS   A 1 231 ? 4.067   -13.465 -22.060 1.00 25.78  ?  233 LYS   A CD   1 
ATOM   1785 C  CE   . LYS   A 1 231 ? 4.091   -14.945 -22.384 1.00 27.39  ?  233 LYS   A CE   1 
ATOM   1786 N  NZ   . LYS   A 1 231 ? 3.848   -15.742 -21.179 1.00 26.91  ?  233 LYS   A NZ   1 
ATOM   1787 N  N    . LEU   A 1 232 ? 4.504   -9.720  -20.106 1.00 22.52  ?  234 LEU   A N    1 
ATOM   1788 C  CA   . LEU   A 1 232 ? 4.580   -9.719  -18.651 1.00 21.89  ?  234 LEU   A CA   1 
ATOM   1789 C  C    . LEU   A 1 232 ? 3.256   -9.245  -18.105 1.00 21.97  ?  234 LEU   A C    1 
ATOM   1790 O  O    . LEU   A 1 232 ? 2.667   -9.895  -17.286 1.00 24.14  ?  234 LEU   A O    1 
ATOM   1791 C  CB   . LEU   A 1 232 ? 5.723   -8.864  -18.138 1.00 20.80  ?  234 LEU   A CB   1 
ATOM   1792 C  CG   . LEU   A 1 232 ? 7.121   -9.358  -18.483 1.00 20.33  ?  234 LEU   A CG   1 
ATOM   1793 C  CD1  . LEU   A 1 232 ? 8.152   -8.316  -18.197 1.00 20.14  ?  234 LEU   A CD1  1 
ATOM   1794 C  CD2  . LEU   A 1 232 ? 7.456   -10.619 -17.756 1.00 21.37  ?  234 LEU   A CD2  1 
ATOM   1795 N  N    . VAL   A 1 233 ? 2.744   -8.153  -18.638 1.00 22.75  ?  235 VAL   A N    1 
ATOM   1796 C  CA   . VAL   A 1 233 ? 1.531   -7.555  -18.132 1.00 22.31  ?  235 VAL   A CA   1 
ATOM   1797 C  C    . VAL   A 1 233 ? 0.342   -8.500  -18.285 1.00 21.48  ?  235 VAL   A C    1 
ATOM   1798 O  O    . VAL   A 1 233 ? -0.513  -8.527  -17.458 1.00 22.54  ?  235 VAL   A O    1 
ATOM   1799 C  CB   . VAL   A 1 233 ? 1.249   -6.199  -18.857 1.00 21.66  ?  235 VAL   A CB   1 
ATOM   1800 C  CG1  . VAL   A 1 233 ? -0.220  -5.819  -18.812 1.00 20.59  ?  235 VAL   A CG1  1 
ATOM   1801 C  CG2  . VAL   A 1 233 ? 2.152   -5.114  -18.257 1.00 21.77  ?  235 VAL   A CG2  1 
ATOM   1802 N  N    . THR   A 1 234 ? 0.270   -9.231  -19.360 1.00 23.97  ?  236 THR   A N    1 
ATOM   1803 C  CA   . THR   A 1 234 ? -0.817  -10.210 -19.549 1.00 26.27  ?  236 THR   A CA   1 
ATOM   1804 C  C    . THR   A 1 234 ? -0.744  -11.357 -18.533 1.00 26.43  ?  236 THR   A C    1 
ATOM   1805 O  O    . THR   A 1 234 ? -1.764  -11.764 -18.000 1.00 26.98  ?  236 THR   A O    1 
ATOM   1806 C  CB   . THR   A 1 234 ? -0.788  -10.736 -20.996 1.00 28.08  ?  236 THR   A CB   1 
ATOM   1807 O  OG1  . THR   A 1 234 ? -1.123  -9.646  -21.865 1.00 28.16  ?  236 THR   A OG1  1 
ATOM   1808 C  CG2  . THR   A 1 234 ? -1.719  -11.925 -21.209 1.00 27.44  ?  236 THR   A CG2  1 
ATOM   1809 N  N    . ASP   A 1 235 ? 0.445   -11.860 -18.250 1.00 27.57  ?  237 ASP   A N    1 
ATOM   1810 C  CA   . ASP   A 1 235 ? 0.610   -12.873 -17.174 1.00 27.47  ?  237 ASP   A CA   1 
ATOM   1811 C  C    . ASP   A 1 235 ? 0.418   -12.278 -15.766 1.00 24.42  ?  237 ASP   A C    1 
ATOM   1812 O  O    . ASP   A 1 235 ? 0.019   -12.977 -14.860 1.00 19.59  ?  237 ASP   A O    1 
ATOM   1813 C  CB   . ASP   A 1 235 ? 2.002   -13.526 -17.239 1.00 31.48  ?  237 ASP   A CB   1 
ATOM   1814 C  CG   . ASP   A 1 235 ? 2.197   -14.407 -18.473 1.00 36.89  ?  237 ASP   A CG   1 
ATOM   1815 O  OD1  . ASP   A 1 235 ? 1.232   -15.075 -18.916 1.00 43.04  ?  237 ASP   A OD1  1 
ATOM   1816 O  OD2  . ASP   A 1 235 ? 3.350   -14.452 -18.985 1.00 44.07  ?  237 ASP   A OD2  1 
ATOM   1817 N  N    . LEU   A 1 236 ? 0.737   -10.988 -15.595 1.00 23.49  ?  238 LEU   A N    1 
ATOM   1818 C  CA   . LEU   A 1 236 ? 0.602   -10.330 -14.304 1.00 24.24  ?  238 LEU   A CA   1 
ATOM   1819 C  C    . LEU   A 1 236 ? -0.893  -10.182 -13.959 1.00 24.78  ?  238 LEU   A C    1 
ATOM   1820 O  O    . LEU   A 1 236 ? -1.321  -10.406 -12.824 1.00 24.19  ?  238 LEU   A O    1 
ATOM   1821 C  CB   . LEU   A 1 236 ? 1.297   -8.940  -14.291 1.00 26.07  ?  238 LEU   A CB   1 
ATOM   1822 C  CG   . LEU   A 1 236 ? 2.188   -8.541  -13.099 1.00 29.35  ?  238 LEU   A CG   1 
ATOM   1823 C  CD1  . LEU   A 1 236 ? 1.997   -7.077  -12.648 1.00 29.13  ?  238 LEU   A CD1  1 
ATOM   1824 C  CD2  . LEU   A 1 236 ? 2.016   -9.440  -11.898 1.00 31.97  ?  238 LEU   A CD2  1 
ATOM   1825 N  N    . THR   A 1 237 ? -1.673  -9.836  -14.978 1.00 23.91  ?  239 THR   A N    1 
ATOM   1826 C  CA   . THR   A 1 237 ? -3.110  -9.659  -14.866 1.00 24.18  ?  239 THR   A CA   1 
ATOM   1827 C  C    . THR   A 1 237 ? -3.766  -10.936 -14.430 1.00 21.15  ?  239 THR   A C    1 
ATOM   1828 O  O    . THR   A 1 237 ? -4.491  -10.924 -13.442 1.00 19.09  ?  239 THR   A O    1 
ATOM   1829 C  CB   . THR   A 1 237 ? -3.678  -9.154  -16.206 1.00 24.65  ?  239 THR   A CB   1 
ATOM   1830 O  OG1  . THR   A 1 237 ? -2.995  -7.936  -16.523 1.00 27.04  ?  239 THR   A OG1  1 
ATOM   1831 C  CG2  . THR   A 1 237 ? -5.143  -8.864  -16.110 1.00 24.31  ?  239 THR   A CG2  1 
ATOM   1832 N  N    . LYS   A 1 238 ? -3.460  -12.030 -15.121 1.00 20.93  ?  240 LYS   A N    1 
ATOM   1833 C  CA   . LYS   A 1 238 ? -3.864  -13.390 -14.646 1.00 20.64  ?  240 LYS   A CA   1 
ATOM   1834 C  C    . LYS   A 1 238 ? -3.527  -13.600 -13.162 1.00 20.69  ?  240 LYS   A C    1 
ATOM   1835 O  O    . LYS   A 1 238 ? -4.383  -13.954 -12.388 1.00 22.96  ?  240 LYS   A O    1 
ATOM   1836 C  CB   . LYS   A 1 238 ? -3.227  -14.515 -15.460 1.00 20.77  ?  240 LYS   A CB   1 
ATOM   1837 C  CG   . LYS   A 1 238 ? -3.679  -15.947 -14.999 1.00 20.94  ?  240 LYS   A CG   1 
ATOM   1838 N  N    . VAL   A 1 239 ? -2.293  -13.318 -12.779 1.00 20.61  ?  241 VAL   A N    1 
ATOM   1839 C  CA   . VAL   A 1 239 ? -1.779  -13.649 -11.463 1.00 23.18  ?  241 VAL   A CA   1 
ATOM   1840 C  C    . VAL   A 1 239 ? -2.475  -12.847 -10.387 1.00 23.25  ?  241 VAL   A C    1 
ATOM   1841 O  O    . VAL   A 1 239 ? -2.941  -13.397 -9.410  1.00 22.42  ?  241 VAL   A O    1 
ATOM   1842 C  CB   . VAL   A 1 239 ? -0.249  -13.379 -11.388 1.00 23.99  ?  241 VAL   A CB   1 
ATOM   1843 C  CG1  . VAL   A 1 239 ? 0.257   -13.271 -9.948  1.00 24.07  ?  241 VAL   A CG1  1 
ATOM   1844 C  CG2  . VAL   A 1 239 ? 0.530   -14.400 -12.227 1.00 23.94  ?  241 VAL   A CG2  1 
ATOM   1845 N  N    . HIS   A 1 240 ? -2.521  -11.529 -10.583 1.00 24.64  ?  242 HIS   A N    1 
ATOM   1846 C  CA   . HIS   A 1 240 ? -3.176  -10.660 -9.670  1.00 23.95  ?  242 HIS   A CA   1 
ATOM   1847 C  C    . HIS   A 1 240 ? -4.693  -10.951 -9.591  1.00 22.68  ?  242 HIS   A C    1 
ATOM   1848 O  O    . HIS   A 1 240 ? -5.265  -10.985 -8.523  1.00 24.16  ?  242 HIS   A O    1 
ATOM   1849 C  CB   . HIS   A 1 240 ? -2.883  -9.219  -10.050 1.00 28.37  ?  242 HIS   A CB   1 
ATOM   1850 C  CG   . HIS   A 1 240 ? -3.525  -8.239  -9.144  1.00 33.35  ?  242 HIS   A CG   1 
ATOM   1851 N  ND1  . HIS   A 1 240 ? -4.518  -7.387  -9.566  1.00 39.94  ?  242 HIS   A ND1  1 
ATOM   1852 C  CD2  . HIS   A 1 240 ? -3.399  -8.044  -7.813  1.00 37.16  ?  242 HIS   A CD2  1 
ATOM   1853 C  CE1  . HIS   A 1 240 ? -4.917  -6.643  -8.550  1.00 38.26  ?  242 HIS   A CE1  1 
ATOM   1854 N  NE2  . HIS   A 1 240 ? -4.238  -7.006  -7.479  1.00 40.58  ?  242 HIS   A NE2  1 
ATOM   1855 N  N    . THR   A 1 241 ? -5.307  -11.232 -10.716 1.00 22.05  ?  243 THR   A N    1 
ATOM   1856 C  CA   . THR   A 1 241 ? -6.693  -11.689 -10.778 1.00 25.30  ?  243 THR   A CA   1 
ATOM   1857 C  C    . THR   A 1 241 ? -6.927  -12.942 -9.921  1.00 25.49  ?  243 THR   A C    1 
ATOM   1858 O  O    . THR   A 1 241 ? -7.911  -12.996 -9.200  1.00 23.51  ?  243 THR   A O    1 
ATOM   1859 C  CB   . THR   A 1 241 ? -7.118  -11.978 -12.255 1.00 25.92  ?  243 THR   A CB   1 
ATOM   1860 O  OG1  . THR   A 1 241 ? -7.088  -10.746 -13.023 1.00 23.61  ?  243 THR   A OG1  1 
ATOM   1861 C  CG2  . THR   A 1 241 ? -8.494  -12.668 -12.333 1.00 26.17  ?  243 THR   A CG2  1 
ATOM   1862 N  N    . GLU   A 1 242 ? -6.012  -13.917 -9.995  1.00 26.17  ?  244 GLU   A N    1 
ATOM   1863 C  CA   . GLU   A 1 242 ? -6.103  -15.146 -9.187  1.00 27.06  ?  244 GLU   A CA   1 
ATOM   1864 C  C    . GLU   A 1 242 ? -5.791  -14.854 -7.693  1.00 27.44  ?  244 GLU   A C    1 
ATOM   1865 O  O    . GLU   A 1 242 ? -6.513  -15.276 -6.810  1.00 25.81  ?  244 GLU   A O    1 
ATOM   1866 C  CB   . GLU   A 1 242 ? -5.206  -16.239 -9.791  1.00 29.49  ?  244 GLU   A CB   1 
ATOM   1867 C  CG   . GLU   A 1 242 ? -5.034  -17.510 -8.957  1.00 33.02  ?  244 GLU   A CG   1 
ATOM   1868 N  N    . CYS   A 1 243 ? -4.752  -14.069 -7.413  1.00 27.40  ?  245 CYS   A N    1 
ATOM   1869 C  CA   . CYS   A 1 243 ? -4.406  -13.752 -6.035  1.00 25.53  ?  245 CYS   A CA   1 
ATOM   1870 C  C    . CYS   A 1 243 ? -5.525  -13.007 -5.301  1.00 28.27  ?  245 CYS   A C    1 
ATOM   1871 O  O    . CYS   A 1 243 ? -5.700  -13.199 -4.076  1.00 24.31  ?  245 CYS   A O    1 
ATOM   1872 C  CB   . CYS   A 1 243 ? -3.092  -12.988 -5.977  1.00 26.48  ?  245 CYS   A CB   1 
ATOM   1873 S  SG   . CYS   A 1 243 ? -1.707  -13.992 -6.589  1.00 26.85  ?  245 CYS   A SG   1 
ATOM   1874 N  N    . CYS   A 1 244 ? -6.292  -12.185 -6.038  1.00 26.75  ?  246 CYS   A N    1 
ATOM   1875 C  CA   . CYS   A 1 244 ? -7.364  -11.412 -5.439  1.00 26.40  ?  246 CYS   A CA   1 
ATOM   1876 C  C    . CYS   A 1 244 ? -8.549  -12.318 -5.132  1.00 25.96  ?  246 CYS   A C    1 
ATOM   1877 O  O    . CYS   A 1 244 ? -9.249  -12.094 -4.175  1.00 27.26  ?  246 CYS   A O    1 
ATOM   1878 C  CB   . CYS   A 1 244 ? -7.785  -10.199 -6.310  1.00 25.01  ?  246 CYS   A CB   1 
ATOM   1879 S  SG   . CYS   A 1 244 ? -6.556  -8.878  -6.344  1.00 26.68  ?  246 CYS   A SG   1 
ATOM   1880 N  N    . HIS   A 1 245 ? -8.770  -13.342 -5.940  1.00 26.71  ?  247 HIS   A N    1 
ATOM   1881 C  CA   . HIS   A 1 245 ? -9.782  -14.335 -5.626  1.00 25.97  ?  247 HIS   A CA   1 
ATOM   1882 C  C    . HIS   A 1 245 ? -9.434  -15.116 -4.323  1.00 25.54  ?  247 HIS   A C    1 
ATOM   1883 O  O    . HIS   A 1 245 ? -10.304 -15.655 -3.663  1.00 26.33  ?  247 HIS   A O    1 
ATOM   1884 C  CB   . HIS   A 1 245 ? -10.013 -15.216 -6.836  1.00 25.14  ?  247 HIS   A CB   1 
ATOM   1885 C  CG   . HIS   A 1 245 ? -11.102 -16.205 -6.653  1.00 25.74  ?  247 HIS   A CG   1 
ATOM   1886 N  ND1  . HIS   A 1 245 ? -10.847 -17.546 -6.484  1.00 26.67  ?  247 HIS   A ND1  1 
ATOM   1887 C  CD2  . HIS   A 1 245 ? -12.445 -16.057 -6.561  1.00 26.71  ?  247 HIS   A CD2  1 
ATOM   1888 C  CE1  . HIS   A 1 245 ? -11.988 -18.190 -6.326  1.00 26.45  ?  247 HIS   A CE1  1 
ATOM   1889 N  NE2  . HIS   A 1 245 ? -12.973 -17.308 -6.360  1.00 27.75  ?  247 HIS   A NE2  1 
ATOM   1890 N  N    . GLY   A 1 246 ? -8.160  -15.169 -3.963  1.00 26.42  ?  248 GLY   A N    1 
ATOM   1891 C  CA   . GLY   A 1 246 ? -7.755  -15.393 -2.573  1.00 27.67  ?  248 GLY   A CA   1 
ATOM   1892 C  C    . GLY   A 1 246 ? -7.185  -16.737 -2.185  1.00 26.23  ?  248 GLY   A C    1 
ATOM   1893 O  O    . GLY   A 1 246 ? -6.874  -16.952 -1.009  1.00 29.81  ?  248 GLY   A O    1 
ATOM   1894 N  N    . ASP   A 1 247 ? -7.055  -17.635 -3.144  1.00 25.83  ?  249 ASP   A N    1 
ATOM   1895 C  CA   . ASP   A 1 247 ? -6.560  -18.989 -2.905  1.00 25.19  ?  249 ASP   A CA   1 
ATOM   1896 C  C    . ASP   A 1 247 ? -5.012  -18.960 -2.857  1.00 24.17  ?  249 ASP   A C    1 
ATOM   1897 O  O    . ASP   A 1 247 ? -4.385  -18.757 -3.873  1.00 26.60  ?  249 ASP   A O    1 
ATOM   1898 C  CB   . ASP   A 1 247 ? -7.082  -19.887 -4.005  1.00 24.94  ?  249 ASP   A CB   1 
ATOM   1899 C  CG   . ASP   A 1 247 ? -6.678  -21.320 -3.835  1.00 25.58  ?  249 ASP   A CG   1 
ATOM   1900 O  OD1  . ASP   A 1 247 ? -5.531  -21.572 -3.470  1.00 22.56  ?  249 ASP   A OD1  1 
ATOM   1901 O  OD2  . ASP   A 1 247 ? -7.504  -22.197 -4.118  1.00 28.24  ?  249 ASP   A OD2  1 
ATOM   1902 N  N    . LEU   A 1 248 ? -4.430  -19.121 -1.667  1.00 22.84  ?  250 LEU   A N    1 
ATOM   1903 C  CA   . LEU   A 1 248 ? -2.978  -18.930 -1.453  1.00 23.71  ?  250 LEU   A CA   1 
ATOM   1904 C  C    . LEU   A 1 248 ? -2.146  -19.735 -2.352  1.00 20.61  ?  250 LEU   A C    1 
ATOM   1905 O  O    . LEU   A 1 248 ? -1.198  -19.227 -2.857  1.00 19.80  ?  250 LEU   A O    1 
ATOM   1906 C  CB   . LEU   A 1 248 ? -2.527  -19.294 -0.024  1.00 24.08  ?  250 LEU   A CB   1 
ATOM   1907 C  CG   . LEU   A 1 248 ? -1.006  -19.303 0.233   1.00 26.04  ?  250 LEU   A CG   1 
ATOM   1908 C  CD1  . LEU   A 1 248 ? -0.385  -17.929 -0.064  1.00 28.65  ?  250 LEU   A CD1  1 
ATOM   1909 C  CD2  . LEU   A 1 248 ? -0.661  -19.725 1.662   1.00 27.19  ?  250 LEU   A CD2  1 
ATOM   1910 N  N    . LEU   A 1 249 ? -2.457  -21.020 -2.462  1.00 19.94  ?  251 LEU   A N    1 
ATOM   1911 C  CA   . LEU   A 1 249 ? -1.656  -21.952 -3.221  1.00 22.21  ?  251 LEU   A CA   1 
ATOM   1912 C  C    . LEU   A 1 249 ? -1.653  -21.570 -4.726  1.00 22.90  ?  251 LEU   A C    1 
ATOM   1913 O  O    . LEU   A 1 249 ? -0.578  -21.425 -5.360  1.00 20.07  ?  251 LEU   A O    1 
ATOM   1914 C  CB   . LEU   A 1 249 ? -2.184  -23.374 -3.017  1.00 23.72  ?  251 LEU   A CB   1 
ATOM   1915 C  CG   . LEU   A 1 249 ? -2.159  -23.970 -1.622  1.00 24.82  ?  251 LEU   A CG   1 
ATOM   1916 C  CD1  . LEU   A 1 249 ? -2.867  -25.294 -1.585  1.00 26.60  ?  251 LEU   A CD1  1 
ATOM   1917 C  CD2  . LEU   A 1 249 ? -0.711  -24.148 -1.198  1.00 26.94  ?  251 LEU   A CD2  1 
ATOM   1918 N  N    . GLU   A 1 250 ? -2.841  -21.332 -5.278  1.00 23.42  ?  252 GLU   A N    1 
ATOM   1919 C  CA   . GLU   A 1 250 ? -2.948  -20.974 -6.697  1.00 26.11  ?  252 GLU   A CA   1 
ATOM   1920 C  C    . GLU   A 1 250 ? -2.194  -19.670 -6.977  1.00 24.04  ?  252 GLU   A C    1 
ATOM   1921 O  O    . GLU   A 1 250 ? -1.484  -19.602 -7.981  1.00 23.23  ?  252 GLU   A O    1 
ATOM   1922 C  CB   . GLU   A 1 250 ? -4.388  -20.858 -7.163  1.00 28.07  ?  252 GLU   A CB   1 
ATOM   1923 C  CG   . GLU   A 1 250 ? -5.137  -22.184 -7.039  1.00 35.25  ?  252 GLU   A CG   1 
ATOM   1924 C  CD   . GLU   A 1 250 ? -4.662  -23.290 -7.983  1.00 41.22  ?  252 GLU   A CD   1 
ATOM   1925 O  OE1  . GLU   A 1 250 ? -4.150  -22.997 -9.104  1.00 43.11  ?  252 GLU   A OE1  1 
ATOM   1926 O  OE2  . GLU   A 1 250 ? -4.836  -24.473 -7.605  1.00 45.53  ?  252 GLU   A OE2  1 
ATOM   1927 N  N    . CYS   A 1 251 ? -2.324  -18.693 -6.066  1.00 22.75  ?  253 CYS   A N    1 
ATOM   1928 C  CA   . CYS   A 1 251 ? -1.599  -17.400 -6.142  1.00 22.31  ?  253 CYS   A CA   1 
ATOM   1929 C  C    . CYS   A 1 251 ? -0.092  -17.602 -6.121  1.00 21.01  ?  253 CYS   A C    1 
ATOM   1930 O  O    . CYS   A 1 251 ? 0.666   -16.824 -6.712  1.00 20.08  ?  253 CYS   A O    1 
ATOM   1931 C  CB   . CYS   A 1 251 ? -2.006  -16.474 -4.963  1.00 21.91  ?  253 CYS   A CB   1 
ATOM   1932 S  SG   . CYS   A 1 251 ? -1.162  -14.859 -4.838  1.00 24.16  ?  253 CYS   A SG   1 
ATOM   1933 N  N    . ALA   A 1 252 ? 0.344   -18.607 -5.384  1.00 19.99  ?  254 ALA   A N    1 
ATOM   1934 C  CA   . ALA   A 1 252 ? 1.756   -18.761 -5.095  1.00 20.78  ?  254 ALA   A CA   1 
ATOM   1935 C  C    . ALA   A 1 252 ? 2.422   -19.462 -6.236  1.00 20.22  ?  254 ALA   A C    1 
ATOM   1936 O  O    . ALA   A 1 252 ? 3.506   -19.109 -6.642  1.00 18.27  ?  254 ALA   A O    1 
ATOM   1937 C  CB   . ALA   A 1 252 ? 1.964   -19.484 -3.762  1.00 22.81  ?  254 ALA   A CB   1 
ATOM   1938 N  N    . ASP   A 1 253 ? 1.734   -20.450 -6.772  1.00 22.78  ?  255 ASP   A N    1 
ATOM   1939 C  CA   . ASP   A 1 253 ? 2.126   -21.066 -8.025  1.00 22.57  ?  255 ASP   A CA   1 
ATOM   1940 C  C    . ASP   A 1 253 ? 2.097   -20.122 -9.196  1.00 21.94  ?  255 ASP   A C    1 
ATOM   1941 O  O    . ASP   A 1 253 ? 2.988   -20.168 -9.991  1.00 22.36  ?  255 ASP   A O    1 
ATOM   1942 C  CB   . ASP   A 1 253 ? 1.231   -22.235 -8.342  1.00 23.27  ?  255 ASP   A CB   1 
ATOM   1943 C  CG   . ASP   A 1 253 ? 1.411   -23.400 -7.354  1.00 25.49  ?  255 ASP   A CG   1 
ATOM   1944 O  OD1  . ASP   A 1 253 ? 2.204   -23.305 -6.373  1.00 26.05  ?  255 ASP   A OD1  1 
ATOM   1945 O  OD2  . ASP   A 1 253 ? 0.708   -24.394 -7.555  1.00 28.11  ?  255 ASP   A OD2  1 
ATOM   1946 N  N    . ASP   A 1 254 ? 1.071   -19.286 -9.322  1.00 22.59  ?  256 ASP   A N    1 
ATOM   1947 C  CA   . ASP   A 1 254 ? 1.070   -18.283 -10.388 1.00 23.30  ?  256 ASP   A CA   1 
ATOM   1948 C  C    . ASP   A 1 254 ? 2.230   -17.301 -10.234 1.00 21.84  ?  256 ASP   A C    1 
ATOM   1949 O  O    . ASP   A 1 254 ? 2.857   -16.935 -11.235 1.00 21.80  ?  256 ASP   A O    1 
ATOM   1950 C  CB   . ASP   A 1 254 ? -0.234  -17.485 -10.413 1.00 25.78  ?  256 ASP   A CB   1 
ATOM   1951 C  CG   . ASP   A 1 254 ? -1.420  -18.288 -10.862 1.00 25.70  ?  256 ASP   A CG   1 
ATOM   1952 O  OD1  . ASP   A 1 254 ? -1.260  -19.289 -11.586 1.00 27.55  ?  256 ASP   A OD1  1 
ATOM   1953 O  OD2  . ASP   A 1 254 ? -2.530  -17.885 -10.478 1.00 27.00  ?  256 ASP   A OD2  1 
ATOM   1954 N  N    . ARG   A 1 255 ? 2.542   -16.893 -9.008  1.00 20.06  ?  257 ARG   A N    1 
ATOM   1955 C  CA   . ARG   A 1 255 ? 3.617   -15.915 -8.817  1.00 20.39  ?  257 ARG   A CA   1 
ATOM   1956 C  C    . ARG   A 1 255 ? 4.954   -16.597 -9.097  1.00 20.65  ?  257 ARG   A C    1 
ATOM   1957 O  O    . ARG   A 1 255 ? 5.844   -15.998 -9.603  1.00 19.33  ?  257 ARG   A O    1 
ATOM   1958 C  CB   . ARG   A 1 255 ? 3.604   -15.331 -7.415  1.00 20.34  ?  257 ARG   A CB   1 
ATOM   1959 C  CG   . ARG   A 1 255 ? 2.514   -14.306 -7.136  1.00 22.03  ?  257 ARG   A CG   1 
ATOM   1960 C  CD   . ARG   A 1 255 ? 2.492   -13.813 -5.684  1.00 24.02  ?  257 ARG   A CD   1 
ATOM   1961 N  NE   . ARG   A 1 255 ? 3.317   -12.590 -5.515  1.00 29.79  ?  257 ARG   A NE   1 
ATOM   1962 C  CZ   . ARG   A 1 255 ? 4.558   -12.566 -5.023  1.00 30.45  ?  257 ARG   A CZ   1 
ATOM   1963 N  NH1  . ARG   A 1 255 ? 5.124   -13.682 -4.602  1.00 34.69  ?  257 ARG   A NH1  1 
ATOM   1964 N  NH2  . ARG   A 1 255 ? 5.241   -11.439 -4.965  1.00 29.55  ?  257 ARG   A NH2  1 
ATOM   1965 N  N    . ALA   A 1 256 ? 5.061   -17.875 -8.732  1.00 22.02  ?  258 ALA   A N    1 
ATOM   1966 C  CA   . ALA   A 1 256 ? 6.264   -18.661 -8.944  1.00 21.43  ?  258 ALA   A CA   1 
ATOM   1967 C  C    . ALA   A 1 256 ? 6.471   -18.914 -10.411 1.00 20.88  ?  258 ALA   A C    1 
ATOM   1968 O  O    . ALA   A 1 256 ? 7.594   -18.794 -10.883 1.00 22.40  ?  258 ALA   A O    1 
ATOM   1969 C  CB   . ALA   A 1 256 ? 6.200   -19.990 -8.182  1.00 21.74  ?  258 ALA   A CB   1 
ATOM   1970 N  N    . ASP   A 1 257 ? 5.393   -19.190 -11.146 1.00 21.43  ?  259 ASP   A N    1 
ATOM   1971 C  CA   . ASP   A 1 257 ? 5.487   -19.362 -12.601 1.00 22.45  ?  259 ASP   A CA   1 
ATOM   1972 C  C    . ASP   A 1 257 ? 5.984   -18.094 -13.260 1.00 23.78  ?  259 ASP   A C    1 
ATOM   1973 O  O    . ASP   A 1 257 ? 6.822   -18.172 -14.153 1.00 24.39  ?  259 ASP   A O    1 
ATOM   1974 C  CB   . ASP   A 1 257 ? 4.169   -19.773 -13.220 1.00 24.10  ?  259 ASP   A CB   1 
ATOM   1975 C  CG   . ASP   A 1 257 ? 3.784   -21.211 -12.861 1.00 29.16  ?  259 ASP   A CG   1 
ATOM   1976 O  OD1  . ASP   A 1 257 ? 4.646   -21.930 -12.306 1.00 29.68  ?  259 ASP   A OD1  1 
ATOM   1977 O  OD2  . ASP   A 1 257 ? 2.610   -21.605 -13.091 1.00 31.00  ?  259 ASP   A OD2  1 
ATOM   1978 N  N    . LEU   A 1 258 ? 5.522   -16.935 -12.795 1.00 22.63  ?  260 LEU   A N    1 
ATOM   1979 C  CA   . LEU   A 1 258 ? 5.982   -15.664 -13.396 1.00 21.44  ?  260 LEU   A CA   1 
ATOM   1980 C  C    . LEU   A 1 258 ? 7.440   -15.426 -13.120 1.00 22.36  ?  260 LEU   A C    1 
ATOM   1981 O  O    . LEU   A 1 258 ? 8.231   -15.090 -14.024 1.00 23.44  ?  260 LEU   A O    1 
ATOM   1982 C  CB   . LEU   A 1 258 ? 5.171   -14.489 -12.842 1.00 21.82  ?  260 LEU   A CB   1 
ATOM   1983 C  CG   . LEU   A 1 258 ? 5.298   -13.147 -13.610 1.00 21.79  ?  260 LEU   A CG   1 
ATOM   1984 C  CD1  . LEU   A 1 258 ? 5.199   -13.359 -15.130 1.00 21.51  ?  260 LEU   A CD1  1 
ATOM   1985 C  CD2  . LEU   A 1 258 ? 4.186   -12.221 -13.135 1.00 21.21  ?  260 LEU   A CD2  1 
ATOM   1986 N  N    . ALA   A 1 259 ? 7.819   -15.635 -11.869 1.00 22.04  ?  261 ALA   A N    1 
ATOM   1987 C  CA   . ALA   A 1 259 ? 9.171   -15.361 -11.453 1.00 23.21  ?  261 ALA   A CA   1 
ATOM   1988 C  C    . ALA   A 1 259 ? 10.185  -16.249 -12.162 1.00 24.04  ?  261 ALA   A C    1 
ATOM   1989 O  O    . ALA   A 1 259 ? 11.313  -15.803 -12.477 1.00 22.42  ?  261 ALA   A O    1 
ATOM   1990 C  CB   . ALA   A 1 259 ? 9.291   -15.525 -9.952  1.00 25.13  ?  261 ALA   A CB   1 
ATOM   1991 N  N    . LYS   A 1 260 ? 9.783   -17.499 -12.374 1.00 24.39  ?  262 LYS   A N    1 
ATOM   1992 C  CA   . LYS   A 1 260 ? 10.548  -18.507 -13.101 1.00 25.89  ?  262 LYS   A CA   1 
ATOM   1993 C  C    . LYS   A 1 260 ? 10.701  -18.065 -14.558 1.00 26.77  ?  262 LYS   A C    1 
ATOM   1994 O  O    . LYS   A 1 260 ? 11.834  -17.967 -15.033 1.00 22.21  ?  262 LYS   A O    1 
ATOM   1995 C  CB   . LYS   A 1 260 ? 9.818   -19.878 -13.030 1.00 26.15  ?  262 LYS   A CB   1 
ATOM   1996 N  N    . TYR   A 1 261 ? 9.574   -17.737 -15.228 1.00 24.98  ?  263 TYR   A N    1 
ATOM   1997 C  CA   . TYR   A 1 261 ? 9.624   -17.186 -16.587 1.00 25.74  ?  263 TYR   A CA   1 
ATOM   1998 C  C    . TYR   A 1 261 ? 10.498  -15.911 -16.658 1.00 27.78  ?  263 TYR   A C    1 
ATOM   1999 O  O    . TYR   A 1 261 ? 11.376  -15.785 -17.531 1.00 24.33  ?  263 TYR   A O    1 
ATOM   2000 C  CB   . TYR   A 1 261 ? 8.237   -16.925 -17.192 1.00 26.10  ?  263 TYR   A CB   1 
ATOM   2001 C  CG   . TYR   A 1 261 ? 8.353   -16.150 -18.477 1.00 26.29  ?  263 TYR   A CG   1 
ATOM   2002 C  CD1  . TYR   A 1 261 ? 8.542   -14.792 -18.442 1.00 25.59  ?  263 TYR   A CD1  1 
ATOM   2003 C  CD2  . TYR   A 1 261 ? 8.367   -16.780 -19.706 1.00 26.68  ?  263 TYR   A CD2  1 
ATOM   2004 C  CE1  . TYR   A 1 261 ? 8.733   -14.061 -19.576 1.00 27.31  ?  263 TYR   A CE1  1 
ATOM   2005 C  CE2  . TYR   A 1 261 ? 8.524   -16.042 -20.876 1.00 25.99  ?  263 TYR   A CE2  1 
ATOM   2006 C  CZ   . TYR   A 1 261 ? 8.695   -14.668 -20.787 1.00 27.13  ?  263 TYR   A CZ   1 
ATOM   2007 O  OH   . TYR   A 1 261 ? 8.902   -13.870 -21.876 1.00 26.20  ?  263 TYR   A OH   1 
ATOM   2008 N  N    . ILE   A 1 262 ? 10.284  -14.976 -15.743 1.00 29.16  ?  264 ILE   A N    1 
ATOM   2009 C  CA   . ILE   A 1 262 ? 11.132  -13.763 -15.720 1.00 29.28  ?  264 ILE   A CA   1 
ATOM   2010 C  C    . ILE   A 1 262 ? 12.599  -14.147 -15.542 1.00 29.57  ?  264 ILE   A C    1 
ATOM   2011 O  O    . ILE   A 1 262 ? 13.437  -13.614 -16.220 1.00 28.10  ?  264 ILE   A O    1 
ATOM   2012 C  CB   . ILE   A 1 262 ? 10.710  -12.766 -14.624 1.00 26.58  ?  264 ILE   A CB   1 
ATOM   2013 C  CG1  . ILE   A 1 262 ? 9.451   -12.046 -15.089 1.00 26.41  ?  264 ILE   A CG1  1 
ATOM   2014 C  CG2  . ILE   A 1 262 ? 11.799  -11.737 -14.328 1.00 27.28  ?  264 ILE   A CG2  1 
ATOM   2015 C  CD1  . ILE   A 1 262 ? 8.720   -11.320 -13.984 1.00 25.65  ?  264 ILE   A CD1  1 
ATOM   2016 N  N    . CYS   A 1 263 ? 12.898  -15.084 -14.652 1.00 31.19  ?  265 CYS   A N    1 
ATOM   2017 C  CA   . CYS   A 1 263 ? 14.305  -15.401 -14.353 1.00 31.50  ?  265 CYS   A CA   1 
ATOM   2018 C  C    . CYS   A 1 263 ? 14.995  -16.149 -15.469 1.00 30.67  ?  265 CYS   A C    1 
ATOM   2019 O  O    . CYS   A 1 263 ? 16.210  -16.061 -15.624 1.00 25.24  ?  265 CYS   A O    1 
ATOM   2020 C  CB   . CYS   A 1 263 ? 14.449  -16.180 -13.056 1.00 33.08  ?  265 CYS   A CB   1 
ATOM   2021 S  SG   . CYS   A 1 263 ? 14.355  -15.111 -11.618 1.00 35.80  ?  265 CYS   A SG   1 
ATOM   2022 N  N    . GLU   A 1 264 ? 14.192  -16.864 -16.248 1.00 32.90  ?  266 GLU   A N    1 
ATOM   2023 C  CA   . GLU   A 1 264 ? 14.669  -17.556 -17.407 1.00 32.62  ?  266 GLU   A CA   1 
ATOM   2024 C  C    . GLU   A 1 264 ? 14.799  -16.615 -18.613 1.00 31.94  ?  266 GLU   A C    1 
ATOM   2025 O  O    . GLU   A 1 264 ? 15.326  -17.025 -19.614 1.00 34.05  ?  266 GLU   A O    1 
ATOM   2026 C  CB   . GLU   A 1 264 ? 13.763  -18.762 -17.705 1.00 34.94  ?  266 GLU   A CB   1 
ATOM   2027 C  CG   . GLU   A 1 264 ? 13.916  -19.901 -16.692 1.00 36.13  ?  266 GLU   A CG   1 
ATOM   2028 C  CD   . GLU   A 1 264 ? 13.121  -21.152 -17.047 1.00 42.34  ?  266 GLU   A CD   1 
ATOM   2029 O  OE1  . GLU   A 1 264 ? 12.128  -21.036 -17.825 1.00 44.72  ?  266 GLU   A OE1  1 
ATOM   2030 O  OE2  . GLU   A 1 264 ? 13.477  -22.255 -16.539 1.00 45.18  ?  266 GLU   A OE2  1 
ATOM   2031 N  N    . ASN   A 1 265 ? 14.337  -15.370 -18.528 1.00 29.18  ?  267 ASN   A N    1 
ATOM   2032 C  CA   . ASN   A 1 265 ? 14.436  -14.425 -19.642 1.00 27.11  ?  267 ASN   A CA   1 
ATOM   2033 C  C    . ASN   A 1 265 ? 15.058  -13.113 -19.172 1.00 28.52  ?  267 ASN   A C    1 
ATOM   2034 O  O    . ASN   A 1 265 ? 14.662  -12.027 -19.607 1.00 28.44  ?  267 ASN   A O    1 
ATOM   2035 C  CB   . ASN   A 1 265 ? 13.049  -14.178 -20.250 1.00 27.91  ?  267 ASN   A CB   1 
ATOM   2036 C  CG   . ASN   A 1 265 ? 12.472  -15.400 -20.909 1.00 29.15  ?  267 ASN   A CG   1 
ATOM   2037 O  OD1  . ASN   A 1 265 ? 12.651  -15.608 -22.102 1.00 31.20  ?  267 ASN   A OD1  1 
ATOM   2038 N  ND2  . ASN   A 1 265 ? 11.775  -16.221 -20.141 1.00 28.36  ?  267 ASN   A ND2  1 
ATOM   2039 N  N    . GLN   A 1 266 ? 16.053  -13.188 -18.299 1.00 28.71  ?  268 GLN   A N    1 
ATOM   2040 C  CA   . GLN   A 1 266 ? 16.611  -11.958 -17.733 1.00 30.85  ?  268 GLN   A CA   1 
ATOM   2041 C  C    . GLN   A 1 266 ? 17.125  -11.045 -18.794 1.00 31.71  ?  268 GLN   A C    1 
ATOM   2042 O  O    . GLN   A 1 266 ? 16.821  -9.848  -18.788 1.00 31.14  ?  268 GLN   A O    1 
ATOM   2043 C  CB   . GLN   A 1 266 ? 17.772  -12.222 -16.781 1.00 32.90  ?  268 GLN   A CB   1 
ATOM   2044 C  CG   . GLN   A 1 266 ? 17.366  -12.743 -15.427 1.00 34.72  ?  268 GLN   A CG   1 
ATOM   2045 C  CD   . GLN   A 1 266 ? 18.586  -13.043 -14.574 1.00 34.07  ?  268 GLN   A CD   1 
ATOM   2046 O  OE1  . GLN   A 1 266 ? 19.356  -12.144 -14.273 1.00 29.87  ?  268 GLN   A OE1  1 
ATOM   2047 N  NE2  . GLN   A 1 266 ? 18.771  -14.320 -14.202 1.00 33.43  ?  268 GLN   A NE2  1 
ATOM   2048 N  N    . ASP   A 1 267 ? 17.930  -11.613 -19.691 1.00 35.54  ?  269 ASP   A N    1 
ATOM   2049 C  CA   . ASP   A 1 267 ? 18.635  -10.857 -20.726 1.00 37.99  ?  269 ASP   A CA   1 
ATOM   2050 C  C    . ASP   A 1 267 ? 17.685  -10.119 -21.653 1.00 36.49  ?  269 ASP   A C    1 
ATOM   2051 O  O    . ASP   A 1 267 ? 18.003  -9.025  -22.121 1.00 36.87  ?  269 ASP   A O    1 
ATOM   2052 C  CB   . ASP   A 1 267 ? 19.589  -11.783 -21.503 1.00 42.94  ?  269 ASP   A CB   1 
ATOM   2053 C  CG   . ASP   A 1 267 ? 20.844  -12.169 -20.681 1.00 49.28  ?  269 ASP   A CG   1 
ATOM   2054 O  OD1  . ASP   A 1 267 ? 20.856  -11.992 -19.426 1.00 53.76  ?  269 ASP   A OD1  1 
ATOM   2055 O  OD2  . ASP   A 1 267 ? 21.834  -12.647 -21.293 1.00 53.31  ?  269 ASP   A OD2  1 
ATOM   2056 N  N    . SER   A 1 268 ? 16.504  -10.702 -21.857 1.00 36.81  ?  270 SER   A N    1 
ATOM   2057 C  CA   . SER   A 1 268 ? 15.379  -10.065 -22.577 1.00 36.48  ?  270 SER   A CA   1 
ATOM   2058 C  C    . SER   A 1 268 ? 14.560  -9.005  -21.786 1.00 31.83  ?  270 SER   A C    1 
ATOM   2059 O  O    . SER   A 1 268 ? 13.679  -8.340  -22.372 1.00 29.73  ?  270 SER   A O    1 
ATOM   2060 C  CB   . SER   A 1 268 ? 14.427  -11.170 -23.059 1.00 38.23  ?  270 SER   A CB   1 
ATOM   2061 O  OG   . SER   A 1 268 ? 13.299  -10.658 -23.754 1.00 44.23  ?  270 SER   A OG   1 
ATOM   2062 N  N    . ILE   A 1 269 ? 14.831  -8.863  -20.479 1.00 27.09  ?  271 ILE   A N    1 
ATOM   2063 C  CA   . ILE   A 1 269 ? 14.014  -8.070  -19.566 1.00 26.00  ?  271 ILE   A CA   1 
ATOM   2064 C  C    . ILE   A 1 269 ? 14.818  -7.003  -18.835 1.00 25.52  ?  271 ILE   A C    1 
ATOM   2065 O  O    . ILE   A 1 269 ? 14.552  -5.807  -18.998 1.00 25.66  ?  271 ILE   A O    1 
ATOM   2066 C  CB   . ILE   A 1 269 ? 13.287  -8.976  -18.574 1.00 26.66  ?  271 ILE   A CB   1 
ATOM   2067 C  CG1  . ILE   A 1 269 ? 12.292  -9.877  -19.326 1.00 26.21  ?  271 ILE   A CG1  1 
ATOM   2068 C  CG2  . ILE   A 1 269 ? 12.597  -8.162  -17.460 1.00 24.96  ?  271 ILE   A CG2  1 
ATOM   2069 C  CD1  . ILE   A 1 269 ? 11.674  -10.969 -18.461 1.00 27.53  ?  271 ILE   A CD1  1 
ATOM   2070 N  N    . SER   A 1 270 ? 15.791  -7.403  -18.035 1.00 25.14  ?  272 SER   A N    1 
ATOM   2071 C  CA   . SER   A 1 270 ? 16.516  -6.437  -17.184 1.00 26.55  ?  272 SER   A CA   1 
ATOM   2072 C  C    . SER   A 1 270 ? 17.826  -6.957  -16.625 1.00 26.43  ?  272 SER   A C    1 
ATOM   2073 O  O    . SER   A 1 270 ? 17.942  -8.104  -16.186 1.00 27.37  ?  272 SER   A O    1 
ATOM   2074 C  CB   . SER   A 1 270 ? 15.632  -5.999  -16.010 1.00 26.57  ?  272 SER   A CB   1 
ATOM   2075 O  OG   . SER   A 1 270 ? 16.360  -5.340  -14.988 1.00 24.92  ?  272 SER   A OG   1 
ATOM   2076 N  N    . SER   A 1 271 ? 18.787  -6.061  -16.573 1.00 29.59  ?  273 SER   A N    1 
ATOM   2077 C  CA   . SER   A 1 271 ? 20.150  -6.384  -16.092 1.00 27.47  ?  273 SER   A CA   1 
ATOM   2078 C  C    . SER   A 1 271 ? 20.267  -6.367  -14.572 1.00 27.28  ?  273 SER   A C    1 
ATOM   2079 O  O    . SER   A 1 271 ? 21.365  -6.607  -14.045 1.00 31.40  ?  273 SER   A O    1 
ATOM   2080 C  CB   . SER   A 1 271 ? 21.088  -5.330  -16.677 1.00 28.06  ?  273 SER   A CB   1 
ATOM   2081 O  OG   . SER   A 1 271 ? 20.839  -4.071  -16.060 1.00 27.65  ?  273 SER   A OG   1 
ATOM   2082 N  N    . LYS   A 1 272 ? 19.174  -6.047  -13.851 1.00 26.19  ?  274 LYS   A N    1 
ATOM   2083 C  CA   . LYS   A 1 272 ? 19.179  -5.947  -12.372 1.00 24.75  ?  274 LYS   A CA   1 
ATOM   2084 C  C    . LYS   A 1 272 ? 18.622  -7.158  -11.639 1.00 23.07  ?  274 LYS   A C    1 
ATOM   2085 O  O    . LYS   A 1 272 ? 18.490  -7.108  -10.460 1.00 25.46  ?  274 LYS   A O    1 
ATOM   2086 C  CB   . LYS   A 1 272 ? 18.423  -4.701  -11.920 1.00 26.25  ?  274 LYS   A CB   1 
ATOM   2087 C  CG   . LYS   A 1 272 ? 18.844  -3.438  -12.679 1.00 29.39  ?  274 LYS   A CG   1 
ATOM   2088 C  CD   . LYS   A 1 272 ? 19.178  -2.266  -11.785 1.00 31.74  ?  274 LYS   A CD   1 
ATOM   2089 C  CE   . LYS   A 1 272 ? 20.019  -1.240  -12.525 1.00 34.03  ?  274 LYS   A CE   1 
ATOM   2090 N  NZ   . LYS   A 1 272 ? 20.776  -0.343  -11.623 1.00 36.17  ?  274 LYS   A NZ   1 
ATOM   2091 N  N    . LEU   A 1 273 ? 18.351  -8.243  -12.334 1.00 23.98  ?  275 LEU   A N    1 
ATOM   2092 C  CA   . LEU   A 1 273 ? 17.605  -9.406  -11.790 1.00 25.34  ?  275 LEU   A CA   1 
ATOM   2093 C  C    . LEU   A 1 273 ? 18.461  -10.568 -11.360 1.00 26.43  ?  275 LEU   A C    1 
ATOM   2094 O  O    . LEU   A 1 273 ? 17.926  -11.604 -11.007 1.00 29.25  ?  275 LEU   A O    1 
ATOM   2095 C  CB   . LEU   A 1 273 ? 16.658  -9.967  -12.860 1.00 23.97  ?  275 LEU   A CB   1 
ATOM   2096 C  CG   . LEU   A 1 273 ? 15.242  -9.444  -13.072 1.00 24.91  ?  275 LEU   A CG   1 
ATOM   2097 C  CD1  . LEU   A 1 273 ? 15.049  -8.071  -12.492 1.00 27.38  ?  275 LEU   A CD1  1 
ATOM   2098 C  CD2  . LEU   A 1 273 ? 14.874  -9.453  -14.536 1.00 23.55  ?  275 LEU   A CD2  1 
ATOM   2099 N  N    . LYS   A 1 274 ? 19.778  -10.437 -11.445 1.00 31.60  ?  276 LYS   A N    1 
ATOM   2100 C  CA   . LYS   A 1 274 ? 20.697  -11.544 -11.132 1.00 32.08  ?  276 LYS   A CA   1 
ATOM   2101 C  C    . LYS   A 1 274 ? 20.530  -12.018 -9.687  1.00 31.21  ?  276 LYS   A C    1 
ATOM   2102 O  O    . LYS   A 1 274 ? 20.326  -13.196 -9.434  1.00 32.97  ?  276 LYS   A O    1 
ATOM   2103 C  CB   . LYS   A 1 274 ? 22.162  -11.137 -11.384 1.00 32.32  ?  276 LYS   A CB   1 
ATOM   2104 N  N    . GLU   A 1 275 ? 20.572  -11.074 -8.766  1.00 33.41  ?  277 GLU   A N    1 
ATOM   2105 C  CA   . GLU   A 1 275 ? 20.543  -11.369 -7.336  1.00 36.17  ?  277 GLU   A CA   1 
ATOM   2106 C  C    . GLU   A 1 275 ? 19.190  -11.935 -6.881  1.00 35.06  ?  277 GLU   A C    1 
ATOM   2107 O  O    . GLU   A 1 275 ? 19.171  -12.904 -6.102  1.00 31.20  ?  277 GLU   A O    1 
ATOM   2108 C  CB   . GLU   A 1 275 ? 20.948  -10.142 -6.534  1.00 39.63  ?  277 GLU   A CB   1 
ATOM   2109 C  CG   . GLU   A 1 275 ? 22.284  -9.512  -6.980  1.00 46.36  ?  277 GLU   A CG   1 
ATOM   2110 C  CD   . GLU   A 1 275 ? 22.132  -8.367  -8.006  1.00 51.57  ?  277 GLU   A CD   1 
ATOM   2111 O  OE1  . GLU   A 1 275 ? 21.691  -8.629  -9.170  1.00 50.53  ?  277 GLU   A OE1  1 
ATOM   2112 O  OE2  . GLU   A 1 275 ? 22.443  -7.196  -7.640  1.00 55.74  ?  277 GLU   A OE2  1 
ATOM   2113 N  N    . CYS   A 1 276 ? 18.076  -11.410 -7.422  1.00 33.33  ?  278 CYS   A N    1 
ATOM   2114 C  CA   . CYS   A 1 276 ? 16.732  -12.034 -7.203  1.00 35.14  ?  278 CYS   A CA   1 
ATOM   2115 C  C    . CYS   A 1 276 ? 16.571  -13.417 -7.758  1.00 34.56  ?  278 CYS   A C    1 
ATOM   2116 O  O    . CYS   A 1 276 ? 15.849  -14.244 -7.194  1.00 30.17  ?  278 CYS   A O    1 
ATOM   2117 C  CB   . CYS   A 1 276 ? 15.621  -11.233 -7.868  1.00 37.07  ?  278 CYS   A CB   1 
ATOM   2118 S  SG   . CYS   A 1 276 ? 15.507  -9.547  -7.302  1.00 41.38  ?  278 CYS   A SG   1 
ATOM   2119 N  N    . CYS   A 1 277 ? 17.194  -13.645 -8.909  1.00 36.17  ?  279 CYS   A N    1 
ATOM   2120 C  CA   . CYS   A 1 277 ? 17.021  -14.897 -9.620  1.00 37.41  ?  279 CYS   A CA   1 
ATOM   2121 C  C    . CYS   A 1 277 ? 17.876  -16.018 -9.027  1.00 39.58  ?  279 CYS   A C    1 
ATOM   2122 O  O    . CYS   A 1 277 ? 17.565  -17.191 -9.214  1.00 37.27  ?  279 CYS   A O    1 
ATOM   2123 C  CB   . CYS   A 1 277 ? 17.243  -14.671 -11.114 1.00 37.13  ?  279 CYS   A CB   1 
ATOM   2124 S  SG   . CYS   A 1 277 ? 15.838  -13.739 -11.833 1.00 36.70  ?  279 CYS   A SG   1 
ATOM   2125 N  N    . GLU   A 1 278 ? 18.913  -15.637 -8.277  1.00 43.00  ?  280 GLU   A N    1 
ATOM   2126 C  CA   . GLU   A 1 278 ? 19.735  -16.582 -7.511  1.00 44.84  ?  280 GLU   A CA   1 
ATOM   2127 C  C    . GLU   A 1 278 ? 19.081  -17.019 -6.179  1.00 41.58  ?  280 GLU   A C    1 
ATOM   2128 O  O    . GLU   A 1 278 ? 19.527  -17.974 -5.588  1.00 43.55  ?  280 GLU   A O    1 
ATOM   2129 C  CB   . GLU   A 1 278 ? 21.123  -15.970 -7.271  1.00 44.23  ?  280 GLU   A CB   1 
ATOM   2130 N  N    . LYS   A 1 279 ? 18.002  -16.360 -5.737  1.00 42.76  ?  281 LYS   A N    1 
ATOM   2131 C  CA   . LYS   A 1 279 ? 17.351  -16.656 -4.433  1.00 39.04  ?  281 LYS   A CA   1 
ATOM   2132 C  C    . LYS   A 1 279 ? 16.431  -17.871 -4.509  1.00 35.27  ?  281 LYS   A C    1 
ATOM   2133 O  O    . LYS   A 1 279 ? 16.072  -18.301 -5.594  1.00 37.22  ?  281 LYS   A O    1 
ATOM   2134 C  CB   . LYS   A 1 279 ? 16.579  -15.437 -3.942  1.00 40.35  ?  281 LYS   A CB   1 
ATOM   2135 C  CG   . LYS   A 1 279 ? 17.441  -14.189 -3.876  1.00 42.54  ?  281 LYS   A CG   1 
ATOM   2136 C  CD   . LYS   A 1 279 ? 17.073  -13.247 -2.743  1.00 43.26  ?  281 LYS   A CD   1 
ATOM   2137 C  CE   . LYS   A 1 279 ? 18.127  -12.178 -2.554  1.00 43.94  ?  281 LYS   A CE   1 
ATOM   2138 N  NZ   . LYS   A 1 279 ? 18.388  -11.920 -1.124  1.00 48.10  ?  281 LYS   A NZ   1 
ATOM   2139 N  N    . PRO   A 1 280 ? 16.050  -18.453 -3.359  1.00 35.12  ?  282 PRO   A N    1 
ATOM   2140 C  CA   . PRO   A 1 280 ? 15.181  -19.639 -3.463  1.00 34.06  ?  282 PRO   A CA   1 
ATOM   2141 C  C    . PRO   A 1 280 ? 13.724  -19.265 -3.765  1.00 34.61  ?  282 PRO   A C    1 
ATOM   2142 O  O    . PRO   A 1 280 ? 13.341  -18.087 -3.728  1.00 30.31  ?  282 PRO   A O    1 
ATOM   2143 C  CB   . PRO   A 1 280 ? 15.335  -20.325 -2.112  1.00 33.58  ?  282 PRO   A CB   1 
ATOM   2144 C  CG   . PRO   A 1 280 ? 15.764  -19.254 -1.183  1.00 34.56  ?  282 PRO   A CG   1 
ATOM   2145 C  CD   . PRO   A 1 280 ? 16.393  -18.138 -1.964  1.00 35.42  ?  282 PRO   A CD   1 
ATOM   2146 N  N    . LEU   A 1 281 ? 12.935  -20.268 -4.123  1.00 36.07  ?  283 LEU   A N    1 
ATOM   2147 C  CA   . LEU   A 1 281 ? 11.608  -20.018 -4.614  1.00 36.37  ?  283 LEU   A CA   1 
ATOM   2148 C  C    . LEU   A 1 281 ? 10.890  -18.947 -3.790  1.00 38.86  ?  283 LEU   A C    1 
ATOM   2149 O  O    . LEU   A 1 281 ? 10.380  -17.959 -4.344  1.00 39.83  ?  283 LEU   A O    1 
ATOM   2150 C  CB   . LEU   A 1 281 ? 10.781  -21.296 -4.644  1.00 37.72  ?  283 LEU   A CB   1 
ATOM   2151 C  CG   . LEU   A 1 281 ? 9.522   -21.062 -5.500  1.00 39.54  ?  283 LEU   A CG   1 
ATOM   2152 C  CD1  . LEU   A 1 281 ? 9.863   -21.072 -6.993  1.00 37.93  ?  283 LEU   A CD1  1 
ATOM   2153 C  CD2  . LEU   A 1 281 ? 8.428   -22.048 -5.129  1.00 41.94  ?  283 LEU   A CD2  1 
ATOM   2154 N  N    . LEU   A 1 282 ? 10.918  -19.119 -2.470  1.00 36.42  ?  284 LEU   A N    1 
ATOM   2155 C  CA   . LEU   A 1 282 ? 10.139  -18.312 -1.565  1.00 33.63  ?  284 LEU   A CA   1 
ATOM   2156 C  C    . LEU   A 1 282 ? 10.311  -16.808 -1.657  1.00 31.17  ?  284 LEU   A C    1 
ATOM   2157 O  O    . LEU   A 1 282 ? 9.333   -16.079 -1.511  1.00 32.53  ?  284 LEU   A O    1 
ATOM   2158 C  CB   . LEU   A 1 282 ? 10.406  -18.755 -0.131  1.00 34.62  ?  284 LEU   A CB   1 
ATOM   2159 C  CG   . LEU   A 1 282 ? 9.459   -18.156 0.891   1.00 35.60  ?  284 LEU   A CG   1 
ATOM   2160 C  CD1  . LEU   A 1 282 ? 8.009   -18.266 0.446   1.00 34.81  ?  284 LEU   A CD1  1 
ATOM   2161 C  CD2  . LEU   A 1 282 ? 9.676   -18.855 2.210   1.00 39.07  ?  284 LEU   A CD2  1 
ATOM   2162 N  N    . GLU   A 1 283 ? 11.537  -16.357 -1.868  1.00 30.12  ?  285 GLU   A N    1 
ATOM   2163 C  CA   . GLU   A 1 283 ? 11.867  -14.925 -1.977  1.00 30.61  ?  285 GLU   A CA   1 
ATOM   2164 C  C    . GLU   A 1 283 ? 11.976  -14.346 -3.404  1.00 28.65  ?  285 GLU   A C    1 
ATOM   2165 O  O    . GLU   A 1 283 ? 12.045  -13.118 -3.563  1.00 26.10  ?  285 GLU   A O    1 
ATOM   2166 C  CB   . GLU   A 1 283 ? 13.227  -14.685 -1.359  1.00 33.28  ?  285 GLU   A CB   1 
ATOM   2167 C  CG   . GLU   A 1 283 ? 13.304  -14.928 0.127   1.00 41.76  ?  285 GLU   A CG   1 
ATOM   2168 C  CD   . GLU   A 1 283 ? 14.738  -15.054 0.615   1.00 40.65  ?  285 GLU   A CD   1 
ATOM   2169 O  OE1  . GLU   A 1 283 ? 15.507  -14.071 0.501   1.00 49.07  ?  285 GLU   A OE1  1 
ATOM   2170 O  OE2  . GLU   A 1 283 ? 15.080  -16.141 1.121   1.00 46.14  ?  285 GLU   A OE2  1 
ATOM   2171 N  N    . LYS   A 1 284 ? 12.071  -15.206 -4.421  1.00 27.55  ?  286 LYS   A N    1 
ATOM   2172 C  CA   . LYS   A 1 284 ? 12.357  -14.751 -5.792  1.00 28.25  ?  286 LYS   A CA   1 
ATOM   2173 C  C    . LYS   A 1 284 ? 11.383  -13.672 -6.207  1.00 25.88  ?  286 LYS   A C    1 
ATOM   2174 O  O    . LYS   A 1 284 ? 11.766  -12.543 -6.445  1.00 25.47  ?  286 LYS   A O    1 
ATOM   2175 C  CB   . LYS   A 1 284 ? 12.230  -15.882 -6.817  1.00 31.37  ?  286 LYS   A CB   1 
ATOM   2176 C  CG   . LYS   A 1 284 ? 13.471  -16.669 -7.164  1.00 34.91  ?  286 LYS   A CG   1 
ATOM   2177 C  CD   . LYS   A 1 284 ? 13.217  -17.443 -8.465  1.00 36.54  ?  286 LYS   A CD   1 
ATOM   2178 C  CE   . LYS   A 1 284 ? 14.095  -18.680 -8.597  1.00 39.15  ?  286 LYS   A CE   1 
ATOM   2179 N  NZ   . LYS   A 1 284 ? 13.670  -19.740 -7.636  1.00 41.58  ?  286 LYS   A NZ   1 
ATOM   2180 N  N    . SER   A 1 285 ? 10.107  -14.054 -6.277  1.00 27.26  ?  287 SER   A N    1 
ATOM   2181 C  CA   . SER   A 1 285 ? 9.032   -13.163 -6.694  1.00 26.09  ?  287 SER   A CA   1 
ATOM   2182 C  C    . SER   A 1 285 ? 8.945   -11.904 -5.841  1.00 26.02  ?  287 SER   A C    1 
ATOM   2183 O  O    . SER   A 1 285 ? 8.651   -10.844 -6.367  1.00 23.04  ?  287 SER   A O    1 
ATOM   2184 C  CB   . SER   A 1 285 ? 7.713   -13.906 -6.677  1.00 26.56  ?  287 SER   A CB   1 
ATOM   2185 O  OG   . SER   A 1 285 ? 7.431   -14.264 -5.338  1.00 27.19  ?  287 SER   A OG   1 
ATOM   2186 N  N    . HIS   A 1 286 ? 9.223   -12.019 -4.529  1.00 27.42  ?  288 HIS   A N    1 
ATOM   2187 C  CA   . HIS   A 1 286 ? 9.265   -10.874 -3.668  1.00 27.12  ?  288 HIS   A CA   1 
ATOM   2188 C  C    . HIS   A 1 286 ? 10.377  -9.926  -4.042  1.00 27.70  ?  288 HIS   A C    1 
ATOM   2189 O  O    . HIS   A 1 286 ? 10.140  -8.703  -4.165  1.00 25.71  ?  288 HIS   A O    1 
ATOM   2190 C  CB   . HIS   A 1 286 ? 9.431   -11.275 -2.207  1.00 31.68  ?  288 HIS   A CB   1 
ATOM   2191 C  CG   . HIS   A 1 286 ? 9.571   -10.098 -1.295  1.00 32.46  ?  288 HIS   A CG   1 
ATOM   2192 N  ND1  . HIS   A 1 286 ? 8.487   -9.376  -0.841  1.00 34.06  ?  288 HIS   A ND1  1 
ATOM   2193 C  CD2  . HIS   A 1 286 ? 10.667  -9.489  -0.792  1.00 35.26  ?  288 HIS   A CD2  1 
ATOM   2194 C  CE1  . HIS   A 1 286 ? 8.914   -8.374  -0.093  1.00 33.17  ?  288 HIS   A CE1  1 
ATOM   2195 N  NE2  . HIS   A 1 286 ? 10.230  -8.433  -0.035  1.00 33.60  ?  288 HIS   A NE2  1 
ATOM   2196 N  N    . CYS   A 1 287 ? 11.593  -10.465 -4.220  1.00 27.07  ?  289 CYS   A N    1 
ATOM   2197 C  CA   . CYS   A 1 287 ? 12.718  -9.658  -4.688  1.00 29.20  ?  289 CYS   A CA   1 
ATOM   2198 C  C    . CYS   A 1 287 ? 12.446  -9.051  -6.075  1.00 28.21  ?  289 CYS   A C    1 
ATOM   2199 O  O    . CYS   A 1 287 ? 12.702  -7.858  -6.318  1.00 26.64  ?  289 CYS   A O    1 
ATOM   2200 C  CB   . CYS   A 1 287 ? 13.980  -10.524 -4.769  1.00 36.24  ?  289 CYS   A CB   1 
ATOM   2201 S  SG   . CYS   A 1 287 ? 15.510  -9.662  -5.228  1.00 45.51  ?  289 CYS   A SG   1 
ATOM   2202 N  N    . ILE   A 1 288 ? 11.933  -9.843  -7.005  1.00 23.12  ?  290 ILE   A N    1 
ATOM   2203 C  CA   . ILE   A 1 288 ? 11.708  -9.258  -8.323  1.00 27.07  ?  290 ILE   A CA   1 
ATOM   2204 C  C    . ILE   A 1 288 ? 10.711  -8.071  -8.283  1.00 27.56  ?  290 ILE   A C    1 
ATOM   2205 O  O    . ILE   A 1 288 ? 10.987  -7.030  -8.917  1.00 28.17  ?  290 ILE   A O    1 
ATOM   2206 C  CB   . ILE   A 1 288 ? 11.306  -10.294 -9.376  1.00 27.58  ?  290 ILE   A CB   1 
ATOM   2207 C  CG1  . ILE   A 1 288 ? 12.453  -11.281 -9.645  1.00 26.29  ?  290 ILE   A CG1  1 
ATOM   2208 C  CG2  . ILE   A 1 288 ? 10.885  -9.623  -10.677 1.00 26.43  ?  290 ILE   A CG2  1 
ATOM   2209 C  CD1  . ILE   A 1 288 ? 11.940  -12.659 -9.996  1.00 27.38  ?  290 ILE   A CD1  1 
ATOM   2210 N  N    . ALA   A 1 289 ? 9.622   -8.193  -7.509  1.00 28.22  ?  291 ALA   A N    1 
ATOM   2211 C  CA   . ALA   A 1 289 ? 8.643   -7.119  -7.393  1.00 29.46  ?  291 ALA   A CA   1 
ATOM   2212 C  C    . ALA   A 1 289 ? 9.229   -5.791  -6.910  1.00 32.85  ?  291 ALA   A C    1 
ATOM   2213 O  O    . ALA   A 1 289 ? 8.740   -4.732  -7.328  1.00 32.96  ?  291 ALA   A O    1 
ATOM   2214 C  CB   . ALA   A 1 289 ? 7.481   -7.539  -6.535  1.00 28.02  ?  291 ALA   A CB   1 
ATOM   2215 N  N    . GLU   A 1 290 ? 10.283  -5.877  -6.080  1.00 34.77  ?  292 GLU   A N    1 
ATOM   2216 C  CA   . GLU   A 1 290 ? 11.002  -4.731  -5.510  1.00 34.05  ?  292 GLU   A CA   1 
ATOM   2217 C  C    . GLU   A 1 290 ? 12.274  -4.302  -6.237  1.00 31.79  ?  292 GLU   A C    1 
ATOM   2218 O  O    . GLU   A 1 290 ? 12.929  -3.346  -5.796  1.00 29.34  ?  292 GLU   A O    1 
ATOM   2219 C  CB   . GLU   A 1 290 ? 11.419  -5.052  -4.063  1.00 39.62  ?  292 GLU   A CB   1 
ATOM   2220 C  CG   . GLU   A 1 290 ? 10.285  -5.484  -3.137  1.00 44.63  ?  292 GLU   A CG   1 
ATOM   2221 C  CD   . GLU   A 1 290 ? 10.419  -4.980  -1.703  1.00 48.73  ?  292 GLU   A CD   1 
ATOM   2222 O  OE1  . GLU   A 1 290 ? 10.230  -5.781  -0.750  1.00 52.18  ?  292 GLU   A OE1  1 
ATOM   2223 O  OE2  . GLU   A 1 290 ? 10.690  -3.771  -1.517  1.00 52.00  ?  292 GLU   A OE2  1 
ATOM   2224 N  N    . VAL   A 1 291 ? 12.647  -4.971  -7.333  1.00 27.13  ?  293 VAL   A N    1 
ATOM   2225 C  CA   . VAL   A 1 291 ? 13.930  -4.692  -7.943  1.00 28.47  ?  293 VAL   A CA   1 
ATOM   2226 C  C    . VAL   A 1 291 ? 14.002  -3.213  -8.415  1.00 30.73  ?  293 VAL   A C    1 
ATOM   2227 O  O    . VAL   A 1 291 ? 12.964  -2.597  -8.733  1.00 27.03  ?  293 VAL   A O    1 
ATOM   2228 C  CB   . VAL   A 1 291 ? 14.214  -5.642  -9.107  1.00 28.68  ?  293 VAL   A CB   1 
ATOM   2229 C  CG1  . VAL   A 1 291 ? 13.322  -5.322  -10.323 1.00 30.42  ?  293 VAL   A CG1  1 
ATOM   2230 C  CG2  . VAL   A 1 291 ? 15.672  -5.607  -9.478  1.00 29.88  ?  293 VAL   A CG2  1 
ATOM   2231 N  N    . GLU   A 1 292 ? 15.230  -2.696  -8.477  1.00 29.70  ?  294 GLU   A N    1 
ATOM   2232 C  CA   . GLU   A 1 292 ? 15.510  -1.324  -8.891  1.00 31.47  ?  294 GLU   A CA   1 
ATOM   2233 C  C    . GLU   A 1 292 ? 15.277  -1.189  -10.377 1.00 27.16  ?  294 GLU   A C    1 
ATOM   2234 O  O    . GLU   A 1 292 ? 15.357  -2.168  -11.118 1.00 23.02  ?  294 GLU   A O    1 
ATOM   2235 C  CB   . GLU   A 1 292 ? 16.967  -0.925  -8.556  1.00 35.22  ?  294 GLU   A CB   1 
ATOM   2236 C  CG   . GLU   A 1 292 ? 17.144  0.556   -8.187  1.00 42.32  ?  294 GLU   A CG   1 
ATOM   2237 C  CD   . GLU   A 1 292 ? 17.976  0.772   -6.910  1.00 50.59  ?  294 GLU   A CD   1 
ATOM   2238 O  OE1  . GLU   A 1 292 ? 17.531  0.313   -5.824  1.00 55.65  ?  294 GLU   A OE1  1 
ATOM   2239 O  OE2  . GLU   A 1 292 ? 19.073  1.394   -6.990  1.00 52.38  ?  294 GLU   A OE2  1 
ATOM   2240 N  N    . ASN   A 1 293 ? 14.977  0.036   -10.789 1.00 25.01  ?  295 ASN   A N    1 
ATOM   2241 C  CA   . ASN   A 1 293 ? 14.790  0.336   -12.176 1.00 25.18  ?  295 ASN   A CA   1 
ATOM   2242 C  C    . ASN   A 1 293 ? 16.099  0.072   -12.937 1.00 26.60  ?  295 ASN   A C    1 
ATOM   2243 O  O    . ASN   A 1 293 ? 17.196  0.405   -12.446 1.00 24.60  ?  295 ASN   A O    1 
ATOM   2244 C  CB   . ASN   A 1 293 ? 14.420  1.806   -12.350 1.00 26.17  ?  295 ASN   A CB   1 
ATOM   2245 C  CG   . ASN   A 1 293 ? 12.987  2.101   -11.970 1.00 26.20  ?  295 ASN   A CG   1 
ATOM   2246 O  OD1  . ASN   A 1 293 ? 12.172  1.180   -11.726 1.00 20.90  ?  295 ASN   A OD1  1 
ATOM   2247 N  ND2  . ASN   A 1 293 ? 12.657  3.407   -11.959 1.00 23.46  ?  295 ASN   A ND2  1 
ATOM   2248 N  N    . ASP   A 1 294 ? 15.973  -0.541  -14.123 1.00 26.29  ?  296 ASP   A N    1 
ATOM   2249 C  CA   . ASP   A 1 294 ? 17.103  -0.712  -14.985 1.00 26.35  ?  296 ASP   A CA   1 
ATOM   2250 C  C    . ASP   A 1 294 ? 17.361  0.669   -15.572 1.00 29.60  ?  296 ASP   A C    1 
ATOM   2251 O  O    . ASP   A 1 294 ? 16.489  1.549   -15.542 1.00 26.73  ?  296 ASP   A O    1 
ATOM   2252 C  CB   . ASP   A 1 294 ? 16.848  -1.749  -16.068 1.00 26.56  ?  296 ASP   A CB   1 
ATOM   2253 C  CG   . ASP   A 1 294 ? 18.146  -2.377  -16.630 1.00 25.79  ?  296 ASP   A CG   1 
ATOM   2254 O  OD1  . ASP   A 1 294 ? 19.258  -2.027  -16.191 1.00 27.32  ?  296 ASP   A OD1  1 
ATOM   2255 O  OD2  . ASP   A 1 294 ? 18.041  -3.266  -17.490 1.00 23.01  ?  296 ASP   A OD2  1 
ATOM   2256 N  N    . GLU   A 1 295 ? 18.574  0.873   -16.059 1.00 32.47  ?  297 GLU   A N    1 
ATOM   2257 C  CA   . GLU   A 1 295 ? 18.914  2.147   -16.672 1.00 38.12  ?  297 GLU   A CA   1 
ATOM   2258 C  C    . GLU   A 1 295 ? 18.292  2.091   -18.057 1.00 35.35  ?  297 GLU   A C    1 
ATOM   2259 O  O    . GLU   A 1 295 ? 18.248  1.032   -18.666 1.00 29.67  ?  297 GLU   A O    1 
ATOM   2260 C  CB   . GLU   A 1 295 ? 20.440  2.350   -16.707 1.00 44.49  ?  297 GLU   A CB   1 
ATOM   2261 C  CG   . GLU   A 1 295 ? 20.881  3.778   -16.387 1.00 51.88  ?  297 GLU   A CG   1 
ATOM   2262 C  CD   . GLU   A 1 295 ? 22.132  3.846   -15.517 1.00 59.45  ?  297 GLU   A CD   1 
ATOM   2263 O  OE1  . GLU   A 1 295 ? 22.173  3.148   -14.471 1.00 60.00  ?  297 GLU   A OE1  1 
ATOM   2264 O  OE2  . GLU   A 1 295 ? 23.062  4.613   -15.882 1.00 63.86  ?  297 GLU   A OE2  1 
ATOM   2265 N  N    . MET   A 1 296 ? 17.762  3.213   -18.523 1.00 35.63  ?  298 MET   A N    1 
ATOM   2266 C  CA   . MET   A 1 296 ? 17.105  3.235   -19.835 1.00 38.64  ?  298 MET   A CA   1 
ATOM   2267 C  C    . MET   A 1 296 ? 18.204  3.194   -20.893 1.00 36.63  ?  298 MET   A C    1 
ATOM   2268 O  O    . MET   A 1 296 ? 19.312  3.656   -20.637 1.00 34.17  ?  298 MET   A O    1 
ATOM   2269 C  CB   . MET   A 1 296 ? 16.175  4.461   -19.999 1.00 38.74  ?  298 MET   A CB   1 
ATOM   2270 C  CG   . MET   A 1 296 ? 16.867  5.803   -20.101 1.00 38.36  ?  298 MET   A CG   1 
ATOM   2271 S  SD   . MET   A 1 296 ? 15.691  7.146   -20.254 1.00 38.68  ?  298 MET   A SD   1 
ATOM   2272 C  CE   . MET   A 1 296 ? 16.772  8.559   -20.555 1.00 39.48  ?  298 MET   A CE   1 
ATOM   2273 N  N    . PRO   A 1 297 ? 17.911  2.634   -22.074 1.00 36.77  ?  299 PRO   A N    1 
ATOM   2274 C  CA   . PRO   A 1 297 ? 18.858  2.766   -23.181 1.00 38.48  ?  299 PRO   A CA   1 
ATOM   2275 C  C    . PRO   A 1 297 ? 19.295  4.228   -23.385 1.00 37.93  ?  299 PRO   A C    1 
ATOM   2276 O  O    . PRO   A 1 297 ? 18.468  5.138   -23.283 1.00 33.05  ?  299 PRO   A O    1 
ATOM   2277 C  CB   . PRO   A 1 297 ? 18.077  2.240   -24.400 1.00 39.57  ?  299 PRO   A CB   1 
ATOM   2278 C  CG   . PRO   A 1 297 ? 16.981  1.409   -23.836 1.00 38.68  ?  299 PRO   A CG   1 
ATOM   2279 C  CD   . PRO   A 1 297 ? 16.698  1.886   -22.439 1.00 36.51  ?  299 PRO   A CD   1 
ATOM   2280 N  N    . ALA   A 1 298 ? 20.577  4.430   -23.675 1.00 42.00  ?  300 ALA   A N    1 
ATOM   2281 C  CA   . ALA   A 1 298 ? 21.226  5.736   -23.465 1.00 50.27  ?  300 ALA   A CA   1 
ATOM   2282 C  C    . ALA   A 1 298 ? 20.852  6.858   -24.448 1.00 52.42  ?  300 ALA   A C    1 
ATOM   2283 O  O    . ALA   A 1 298 ? 20.949  8.031   -24.076 1.00 60.71  ?  300 ALA   A O    1 
ATOM   2284 C  CB   . ALA   A 1 298 ? 22.751  5.577   -23.391 1.00 50.54  ?  300 ALA   A CB   1 
ATOM   2285 N  N    . ASP   A 1 299 ? 20.444  6.525   -25.673 1.00 49.61  ?  301 ASP   A N    1 
ATOM   2286 C  CA   . ASP   A 1 299 ? 20.101  7.551   -26.667 1.00 51.19  ?  301 ASP   A CA   1 
ATOM   2287 C  C    . ASP   A 1 299 ? 18.801  7.194   -27.372 1.00 48.77  ?  301 ASP   A C    1 
ATOM   2288 O  O    . ASP   A 1 299 ? 18.796  6.811   -28.537 1.00 52.28  ?  301 ASP   A O    1 
ATOM   2289 C  CB   . ASP   A 1 299 ? 21.255  7.749   -27.666 1.00 51.63  ?  301 ASP   A CB   1 
ATOM   2290 N  N    . LEU   A 1 300 ? 17.699  7.323   -26.635 1.00 44.82  ?  302 LEU   A N    1 
ATOM   2291 C  CA   . LEU   A 1 300 ? 16.373  6.976   -27.135 1.00 38.06  ?  302 LEU   A CA   1 
ATOM   2292 C  C    . LEU   A 1 300 ? 15.835  8.144   -27.939 1.00 37.47  ?  302 LEU   A C    1 
ATOM   2293 O  O    . LEU   A 1 300 ? 16.090  9.308   -27.599 1.00 34.79  ?  302 LEU   A O    1 
ATOM   2294 C  CB   . LEU   A 1 300 ? 15.418  6.648   -25.992 1.00 34.71  ?  302 LEU   A CB   1 
ATOM   2295 C  CG   . LEU   A 1 300 ? 15.676  5.316   -25.281 1.00 33.47  ?  302 LEU   A CG   1 
ATOM   2296 C  CD1  . LEU   A 1 300 ? 14.870  5.254   -24.000 1.00 33.27  ?  302 LEU   A CD1  1 
ATOM   2297 C  CD2  . LEU   A 1 300 ? 15.377  4.122   -26.174 1.00 33.73  ?  302 LEU   A CD2  1 
ATOM   2298 N  N    . PRO   A 1 301 ? 15.079  7.842   -28.994 1.00 38.93  ?  303 PRO   A N    1 
ATOM   2299 C  CA   . PRO   A 1 301 ? 14.480  8.908   -29.796 1.00 40.07  ?  303 PRO   A CA   1 
ATOM   2300 C  C    . PRO   A 1 301 ? 13.341  9.680   -29.103 1.00 41.66  ?  303 PRO   A C    1 
ATOM   2301 O  O    . PRO   A 1 301 ? 12.833  9.270   -28.045 1.00 43.55  ?  303 PRO   A O    1 
ATOM   2302 C  CB   . PRO   A 1 301 ? 13.934  8.175   -31.035 1.00 40.57  ?  303 PRO   A CB   1 
ATOM   2303 C  CG   . PRO   A 1 301 ? 14.112  6.705   -30.805 1.00 39.52  ?  303 PRO   A CG   1 
ATOM   2304 C  CD   . PRO   A 1 301 ? 14.742  6.486   -29.475 1.00 38.73  ?  303 PRO   A CD   1 
ATOM   2305 N  N    . SER   A 1 302 ? 12.966  10.799  -29.723 1.00 39.13  ?  304 SER   A N    1 
ATOM   2306 C  CA   . SER   A 1 302 ? 11.734  11.523  -29.423 1.00 36.55  ?  304 SER   A CA   1 
ATOM   2307 C  C    . SER   A 1 302 ? 10.485  10.700  -29.780 1.00 33.66  ?  304 SER   A C    1 
ATOM   2308 O  O    . SER   A 1 302 ? 10.467  9.973   -30.763 1.00 33.41  ?  304 SER   A O    1 
ATOM   2309 C  CB   . SER   A 1 302 ? 11.688  12.848  -30.215 1.00 38.44  ?  304 SER   A CB   1 
ATOM   2310 O  OG   . SER   A 1 302 ? 10.394  13.449  -30.198 1.00 37.91  ?  304 SER   A OG   1 
ATOM   2311 N  N    . LEU   A 1 303 ? 9.427   10.888  -29.005 1.00 34.14  ?  305 LEU   A N    1 
ATOM   2312 C  CA   . LEU   A 1 303 ? 8.139   10.210  -29.235 1.00 34.02  ?  305 LEU   A CA   1 
ATOM   2313 C  C    . LEU   A 1 303 ? 7.221   10.900  -30.275 1.00 32.62  ?  305 LEU   A C    1 
ATOM   2314 O  O    . LEU   A 1 303 ? 6.220   10.325  -30.666 1.00 27.11  ?  305 LEU   A O    1 
ATOM   2315 C  CB   . LEU   A 1 303 ? 7.395   10.132  -27.934 1.00 36.03  ?  305 LEU   A CB   1 
ATOM   2316 C  CG   . LEU   A 1 303 ? 8.212   9.520   -26.793 1.00 35.32  ?  305 LEU   A CG   1 
ATOM   2317 C  CD1  . LEU   A 1 303 ? 7.960   10.325  -25.533 1.00 37.86  ?  305 LEU   A CD1  1 
ATOM   2318 C  CD2  . LEU   A 1 303 ? 7.852   8.066   -26.608 1.00 34.59  ?  305 LEU   A CD2  1 
ATOM   2319 N  N    . ALA   A 1 304 ? 7.546   12.134  -30.683 1.00 30.12  ?  306 ALA   A N    1 
ATOM   2320 C  CA   . ALA   A 1 304 ? 6.802   12.830  -31.758 1.00 31.41  ?  306 ALA   A CA   1 
ATOM   2321 C  C    . ALA   A 1 304 ? 6.763   12.038  -33.071 1.00 30.28  ?  306 ALA   A C    1 
ATOM   2322 O  O    . ALA   A 1 304 ? 5.720   11.963  -33.708 1.00 29.39  ?  306 ALA   A O    1 
ATOM   2323 C  CB   . ALA   A 1 304 ? 7.365   14.249  -31.991 1.00 33.34  ?  306 ALA   A CB   1 
ATOM   2324 N  N    . ALA   A 1 305 ? 7.858   11.376  -33.434 1.00 33.09  ?  307 ALA   A N    1 
ATOM   2325 C  CA   . ALA   A 1 305 ? 7.911   10.566  -34.680 1.00 35.23  ?  307 ALA   A CA   1 
ATOM   2326 C  C    . ALA   A 1 305 ? 6.808   9.510   -34.841 1.00 35.55  ?  307 ALA   A C    1 
ATOM   2327 O  O    . ALA   A 1 305 ? 6.104   9.530   -35.811 1.00 34.92  ?  307 ALA   A O    1 
ATOM   2328 C  CB   . ALA   A 1 305 ? 9.265   9.893   -34.811 1.00 38.56  ?  307 ALA   A CB   1 
ATOM   2329 N  N    . ASP   A 1 306 ? 6.668   8.578   -33.900 1.00 39.48  ?  308 ASP   A N    1 
ATOM   2330 C  CA   . ASP   A 1 306 ? 5.655   7.500   -34.019 1.00 35.04  ?  308 ASP   A CA   1 
ATOM   2331 C  C    . ASP   A 1 306 ? 4.266   7.944   -33.599 1.00 32.45  ?  308 ASP   A C    1 
ATOM   2332 O  O    . ASP   A 1 306 ? 3.276   7.440   -34.129 1.00 37.00  ?  308 ASP   A O    1 
ATOM   2333 C  CB   . ASP   A 1 306 ? 6.053   6.276   -33.196 1.00 36.15  ?  308 ASP   A CB   1 
ATOM   2334 C  CG   . ASP   A 1 306 ? 7.363   5.651   -33.657 1.00 41.19  ?  308 ASP   A CG   1 
ATOM   2335 O  OD1  . ASP   A 1 306 ? 7.714   5.711   -34.881 1.00 36.66  ?  308 ASP   A OD1  1 
ATOM   2336 O  OD2  . ASP   A 1 306 ? 8.038   5.076   -32.761 1.00 44.35  ?  308 ASP   A OD2  1 
ATOM   2337 N  N    . PHE   A 1 307 ? 4.187   8.901   -32.676 1.00 28.08  ?  309 PHE   A N    1 
ATOM   2338 C  CA   . PHE   A 1 307 ? 2.912   9.333   -32.104 1.00 25.34  ?  309 PHE   A CA   1 
ATOM   2339 C  C    . PHE   A 1 307 ? 2.358   10.693  -32.515 1.00 25.88  ?  309 PHE   A C    1 
ATOM   2340 O  O    . PHE   A 1 307 ? 1.220   10.968  -32.225 1.00 24.23  ?  309 PHE   A O    1 
ATOM   2341 C  CB   . PHE   A 1 307 ? 3.050   9.234   -30.596 1.00 23.13  ?  309 PHE   A CB   1 
ATOM   2342 C  CG   . PHE   A 1 307 ? 3.423   7.848   -30.173 1.00 21.15  ?  309 PHE   A CG   1 
ATOM   2343 C  CD1  . PHE   A 1 307 ? 2.481   6.839   -30.226 1.00 20.07  ?  309 PHE   A CD1  1 
ATOM   2344 C  CD2  . PHE   A 1 307 ? 4.715   7.530   -29.836 1.00 21.01  ?  309 PHE   A CD2  1 
ATOM   2345 C  CE1  . PHE   A 1 307 ? 2.799   5.530   -29.887 1.00 20.33  ?  309 PHE   A CE1  1 
ATOM   2346 C  CE2  . PHE   A 1 307 ? 5.043   6.199   -29.509 1.00 22.01  ?  309 PHE   A CE2  1 
ATOM   2347 C  CZ   . PHE   A 1 307 ? 4.086   5.210   -29.541 1.00 19.44  ?  309 PHE   A CZ   1 
ATOM   2348 N  N    . VAL   A 1 308 ? 3.136   11.530  -33.190 1.00 27.55  ?  310 VAL   A N    1 
ATOM   2349 C  CA   . VAL   A 1 308 ? 2.620   12.829  -33.680 1.00 30.39  ?  310 VAL   A CA   1 
ATOM   2350 C  C    . VAL   A 1 308 ? 2.835   13.033  -35.184 1.00 33.48  ?  310 VAL   A C    1 
ATOM   2351 O  O    . VAL   A 1 308 ? 1.875   13.284  -35.929 1.00 33.34  ?  310 VAL   A O    1 
ATOM   2352 C  CB   . VAL   A 1 308 ? 3.258   14.018  -32.932 1.00 30.93  ?  310 VAL   A CB   1 
ATOM   2353 C  CG1  . VAL   A 1 308 ? 2.619   15.339  -33.354 1.00 32.71  ?  310 VAL   A CG1  1 
ATOM   2354 C  CG2  . VAL   A 1 308 ? 3.116   13.834  -31.436 1.00 32.58  ?  310 VAL   A CG2  1 
ATOM   2355 N  N    . GLU   A 1 309 ? 4.096   12.912  -35.606 1.00 35.55  ?  311 GLU   A N    1 
ATOM   2356 C  CA   . GLU   A 1 309 ? 4.559   13.262  -36.960 1.00 39.01  ?  311 GLU   A CA   1 
ATOM   2357 C  C    . GLU   A 1 309 ? 4.226   12.261  -38.054 1.00 38.14  ?  311 GLU   A C    1 
ATOM   2358 O  O    . GLU   A 1 309 ? 3.839   12.671  -39.115 1.00 36.10  ?  311 GLU   A O    1 
ATOM   2359 C  CB   . GLU   A 1 309 ? 6.076   13.511  -36.949 1.00 41.80  ?  311 GLU   A CB   1 
ATOM   2360 C  CG   . GLU   A 1 309 ? 6.466   14.718  -36.081 1.00 44.39  ?  311 GLU   A CG   1 
ATOM   2361 C  CD   . GLU   A 1 309 ? 7.927   14.751  -35.650 1.00 43.46  ?  311 GLU   A CD   1 
ATOM   2362 O  OE1  . GLU   A 1 309 ? 8.632   13.729  -35.708 1.00 43.71  ?  311 GLU   A OE1  1 
ATOM   2363 O  OE2  . GLU   A 1 309 ? 8.373   15.826  -35.228 1.00 45.75  ?  311 GLU   A OE2  1 
ATOM   2364 N  N    . SER   A 1 310 ? 4.351   10.958  -37.808 1.00 39.81  ?  312 SER   A N    1 
ATOM   2365 C  CA   . SER   A 1 310 ? 4.063   9.987   -38.864 1.00 38.55  ?  312 SER   A CA   1 
ATOM   2366 C  C    . SER   A 1 310 ? 2.608   10.100  -39.336 1.00 39.55  ?  312 SER   A C    1 
ATOM   2367 O  O    . SER   A 1 310 ? 1.712   10.385  -38.539 1.00 34.34  ?  312 SER   A O    1 
ATOM   2368 C  CB   . SER   A 1 310 ? 4.385   8.547   -38.455 1.00 39.41  ?  312 SER   A CB   1 
ATOM   2369 O  OG   . SER   A 1 310 ? 3.221   7.835   -38.093 1.00 40.03  ?  312 SER   A OG   1 
ATOM   2370 N  N    . LYS   A 1 311 ? 2.412   9.962   -40.655 1.00 40.55  ?  313 LYS   A N    1 
ATOM   2371 C  CA   . LYS   A 1 311 ? 1.105   9.629   -41.237 1.00 40.94  ?  313 LYS   A CA   1 
ATOM   2372 C  C    . LYS   A 1 311 ? 0.770   8.237   -40.731 1.00 42.01  ?  313 LYS   A C    1 
ATOM   2373 O  O    . LYS   A 1 311 ? 1.657   7.488   -40.309 1.00 46.93  ?  313 LYS   A O    1 
ATOM   2374 C  CB   . LYS   A 1 311 ? 1.171   9.605   -42.767 1.00 41.70  ?  313 LYS   A CB   1 
ATOM   2375 N  N    . ASP   A 1 312 ? -0.494  7.872   -40.741 1.00 41.41  ?  314 ASP   A N    1 
ATOM   2376 C  CA   . ASP   A 1 312 ? -0.892  6.578   -40.135 1.00 37.78  ?  314 ASP   A CA   1 
ATOM   2377 C  C    . ASP   A 1 312 ? -0.805  6.529   -38.582 1.00 35.29  ?  314 ASP   A C    1 
ATOM   2378 O  O    . ASP   A 1 312 ? -0.848  5.436   -37.994 1.00 33.66  ?  314 ASP   A O    1 
ATOM   2379 C  CB   . ASP   A 1 312 ? -0.097  5.412   -40.747 1.00 38.00  ?  314 ASP   A CB   1 
ATOM   2380 N  N    . VAL   A 1 313 ? -0.731  7.679   -37.895 1.00 30.80  ?  315 VAL   A N    1 
ATOM   2381 C  CA   . VAL   A 1 313 ? -0.975  7.647   -36.437 1.00 28.95  ?  315 VAL   A CA   1 
ATOM   2382 C  C    . VAL   A 1 313 ? -2.408  7.098   -36.270 1.00 27.17  ?  315 VAL   A C    1 
ATOM   2383 O  O    . VAL   A 1 313 ? -2.605  6.091   -35.582 1.00 25.41  ?  315 VAL   A O    1 
ATOM   2384 C  CB   . VAL   A 1 313 ? -0.771  9.012   -35.706 1.00 27.27  ?  315 VAL   A CB   1 
ATOM   2385 C  CG1  . VAL   A 1 313 ? -1.385  8.973   -34.304 1.00 26.59  ?  315 VAL   A CG1  1 
ATOM   2386 C  CG2  . VAL   A 1 313 ? 0.735   9.368   -35.611 1.00 24.58  ?  315 VAL   A CG2  1 
ATOM   2387 N  N    . CYS   A 1 314 ? -3.356  7.731   -36.963 1.00 25.83  ?  316 CYS   A N    1 
ATOM   2388 C  CA   . CYS   A 1 314 ? -4.769  7.337   -36.945 1.00 26.48  ?  316 CYS   A CA   1 
ATOM   2389 C  C    . CYS   A 1 314 ? -5.005  5.922   -37.439 1.00 24.57  ?  316 CYS   A C    1 
ATOM   2390 O  O    . CYS   A 1 314 ? -5.774  5.211   -36.827 1.00 25.08  ?  316 CYS   A O    1 
ATOM   2391 C  CB   . CYS   A 1 314 ? -5.614  8.317   -37.723 1.00 28.28  ?  316 CYS   A CB   1 
ATOM   2392 S  SG   . CYS   A 1 314 ? -5.594  9.967   -36.933 1.00 35.66  ?  316 CYS   A SG   1 
ATOM   2393 N  N    . LYS   A 1 315 ? -4.315  5.532   -38.504 1.00 24.54  ?  317 LYS   A N    1 
ATOM   2394 C  CA   . LYS   A 1 315 ? -4.384  4.173   -39.053 1.00 26.40  ?  317 LYS   A CA   1 
ATOM   2395 C  C    . LYS   A 1 315 ? -3.924  3.166   -38.011 1.00 24.32  ?  317 LYS   A C    1 
ATOM   2396 O  O    . LYS   A 1 315 ? -4.622  2.197   -37.730 1.00 21.06  ?  317 LYS   A O    1 
ATOM   2397 C  CB   . LYS   A 1 315 ? -3.539  4.045   -40.324 1.00 26.46  ?  317 LYS   A CB   1 
ATOM   2398 N  N    . ASN   A 1 316 ? -2.739  3.405   -37.455 1.00 24.64  ?  318 ASN   A N    1 
ATOM   2399 C  CA   . ASN   A 1 316 ? -2.172  2.524   -36.437 1.00 25.35  ?  318 ASN   A CA   1 
ATOM   2400 C  C    . ASN   A 1 316 ? -3.010  2.472   -35.219 1.00 25.42  ?  318 ASN   A C    1 
ATOM   2401 O  O    . ASN   A 1 316 ? -3.172  1.400   -34.602 1.00 24.58  ?  318 ASN   A O    1 
ATOM   2402 C  CB   . ASN   A 1 316 ? -0.785  2.977   -35.990 1.00 29.12  ?  318 ASN   A CB   1 
ATOM   2403 C  CG   . ASN   A 1 316 ? 0.269   2.625   -36.986 1.00 30.44  ?  318 ASN   A CG   1 
ATOM   2404 O  OD1  . ASN   A 1 316 ? -0.012  1.918   -37.955 1.00 31.85  ?  318 ASN   A OD1  1 
ATOM   2405 N  ND2  . ASN   A 1 316 ? 1.492   3.124   -36.774 1.00 30.90  ?  318 ASN   A ND2  1 
ATOM   2406 N  N    . TYR   A 1 317 ? -3.496  3.645   -34.833 1.00 23.08  ?  319 TYR   A N    1 
ATOM   2407 C  CA   . TYR   A 1 317 ? -4.429  3.757   -33.721 1.00 22.56  ?  319 TYR   A CA   1 
ATOM   2408 C  C    . TYR   A 1 317 ? -5.725  2.965   -33.957 1.00 21.88  ?  319 TYR   A C    1 
ATOM   2409 O  O    . TYR   A 1 317 ? -6.079  2.145   -33.140 1.00 22.12  ?  319 TYR   A O    1 
ATOM   2410 C  CB   . TYR   A 1 317 ? -4.786  5.215   -33.433 1.00 21.96  ?  319 TYR   A CB   1 
ATOM   2411 C  CG   . TYR   A 1 317 ? -5.767  5.391   -32.316 1.00 20.77  ?  319 TYR   A CG   1 
ATOM   2412 C  CD1  . TYR   A 1 317 ? -5.468  4.922   -31.050 1.00 21.13  ?  319 TYR   A CD1  1 
ATOM   2413 C  CD2  . TYR   A 1 317 ? -6.979  6.044   -32.512 1.00 20.48  ?  319 TYR   A CD2  1 
ATOM   2414 C  CE1  . TYR   A 1 317 ? -6.346  5.078   -30.016 1.00 21.08  ?  319 TYR   A CE1  1 
ATOM   2415 C  CE2  . TYR   A 1 317 ? -7.885  6.202   -31.479 1.00 21.39  ?  319 TYR   A CE2  1 
ATOM   2416 C  CZ   . TYR   A 1 317 ? -7.542  5.708   -30.221 1.00 21.97  ?  319 TYR   A CZ   1 
ATOM   2417 O  OH   . TYR   A 1 317 ? -8.376  5.825   -29.150 1.00 22.39  ?  319 TYR   A OH   1 
ATOM   2418 N  N    . ALA   A 1 318 ? -6.403  3.201   -35.071 1.00 22.10  ?  320 ALA   A N    1 
ATOM   2419 C  CA   . ALA   A 1 318 ? -7.721  2.593   -35.316 1.00 22.59  ?  320 ALA   A CA   1 
ATOM   2420 C  C    . ALA   A 1 318 ? -7.715  1.047   -35.370 1.00 24.33  ?  320 ALA   A C    1 
ATOM   2421 O  O    . ALA   A 1 318 ? -8.733  0.404   -35.074 1.00 21.63  ?  320 ALA   A O    1 
ATOM   2422 C  CB   . ALA   A 1 318 ? -8.306  3.140   -36.590 1.00 22.89  ?  320 ALA   A CB   1 
ATOM   2423 N  N    . GLU   A 1 319 ? -6.566  0.494   -35.740 1.00 25.28  ?  321 GLU   A N    1 
ATOM   2424 C  CA   . GLU   A 1 319 ? -6.395  -0.905  -36.026 1.00 30.35  ?  321 GLU   A CA   1 
ATOM   2425 C  C    . GLU   A 1 319 ? -6.344  -1.730  -34.738 1.00 32.09  ?  321 GLU   A C    1 
ATOM   2426 O  O    . GLU   A 1 319 ? -6.684  -2.915  -34.732 1.00 31.87  ?  321 GLU   A O    1 
ATOM   2427 C  CB   . GLU   A 1 319 ? -5.102  -1.055  -36.822 1.00 34.21  ?  321 GLU   A CB   1 
ATOM   2428 C  CG   . GLU   A 1 319 ? -4.905  -2.430  -37.424 1.00 40.04  ?  321 GLU   A CG   1 
ATOM   2429 C  CD   . GLU   A 1 319 ? -3.647  -2.545  -38.284 1.00 42.48  ?  321 GLU   A CD   1 
ATOM   2430 O  OE1  . GLU   A 1 319 ? -3.117  -3.671  -38.319 1.00 48.69  ?  321 GLU   A OE1  1 
ATOM   2431 O  OE2  . GLU   A 1 319 ? -3.192  -1.551  -38.915 1.00 38.30  ?  321 GLU   A OE2  1 
ATOM   2432 N  N    . ALA   A 1 320 ? -5.918  -1.098  -33.645 1.00 29.37  ?  322 ALA   A N    1 
ATOM   2433 C  CA   . ALA   A 1 320 ? -5.804  -1.771  -32.341 1.00 30.23  ?  322 ALA   A CA   1 
ATOM   2434 C  C    . ALA   A 1 320 ? -5.517  -0.673  -31.297 1.00 25.96  ?  322 ALA   A C    1 
ATOM   2435 O  O    . ALA   A 1 320 ? -4.359  -0.379  -30.987 1.00 22.51  ?  322 ALA   A O    1 
ATOM   2436 C  CB   . ALA   A 1 320 ? -4.675  -2.820  -32.366 1.00 31.88  ?  322 ALA   A CB   1 
ATOM   2437 N  N    . LYS   A 1 321 ? -6.589  -0.085  -30.793 1.00 24.33  ?  323 LYS   A N    1 
ATOM   2438 C  CA   . LYS   A 1 321 ? -6.520  1.158   -30.044 1.00 26.76  ?  323 LYS   A CA   1 
ATOM   2439 C  C    . LYS   A 1 321 ? -5.760  0.960   -28.736 1.00 26.14  ?  323 LYS   A C    1 
ATOM   2440 O  O    . LYS   A 1 321 ? -4.900  1.787   -28.374 1.00 21.55  ?  323 LYS   A O    1 
ATOM   2441 C  CB   . LYS   A 1 321 ? -7.927  1.736   -29.810 1.00 26.21  ?  323 LYS   A CB   1 
ATOM   2442 C  CG   . LYS   A 1 321 ? -8.624  2.147   -31.094 1.00 26.87  ?  323 LYS   A CG   1 
ATOM   2443 C  CD   . LYS   A 1 321 ? -9.980  2.813   -30.835 1.00 27.89  ?  323 LYS   A CD   1 
ATOM   2444 C  CE   . LYS   A 1 321 ? -10.594 3.370   -32.121 1.00 28.30  ?  323 LYS   A CE   1 
ATOM   2445 N  NZ   . LYS   A 1 321 ? -11.582 4.477   -31.859 1.00 27.72  ?  323 LYS   A NZ   1 
ATOM   2446 N  N    . ASP   A 1 322 ? -6.036  -0.159  -28.064 1.00 23.69  ?  324 ASP   A N    1 
ATOM   2447 C  CA   . ASP   A 1 322 ? -5.404  -0.427  -26.818 1.00 25.15  ?  324 ASP   A CA   1 
ATOM   2448 C  C    . ASP   A 1 322 ? -3.965  -0.781  -27.040 1.00 24.79  ?  324 ASP   A C    1 
ATOM   2449 O  O    . ASP   A 1 322 ? -3.132  -0.349  -26.255 1.00 24.23  ?  324 ASP   A O    1 
ATOM   2450 C  CB   . ASP   A 1 322 ? -6.162  -1.475  -25.988 1.00 29.85  ?  324 ASP   A CB   1 
ATOM   2451 C  CG   . ASP   A 1 322 ? -7.355  -0.864  -25.229 1.00 32.62  ?  324 ASP   A CG   1 
ATOM   2452 O  OD1  . ASP   A 1 322 ? -7.614  0.351   -25.415 1.00 33.58  ?  324 ASP   A OD1  1 
ATOM   2453 O  OD2  . ASP   A 1 322 ? -8.004  -1.574  -24.411 1.00 33.01  ?  324 ASP   A OD2  1 
ATOM   2454 N  N    . VAL   A 1 323 ? -3.634  -1.449  -28.146 1.00 25.40  ?  325 VAL   A N    1 
ATOM   2455 C  CA   . VAL   A 1 323 ? -2.238  -1.801  -28.407 1.00 24.66  ?  325 VAL   A CA   1 
ATOM   2456 C  C    . VAL   A 1 323 ? -1.459  -0.488  -28.682 1.00 24.57  ?  325 VAL   A C    1 
ATOM   2457 O  O    . VAL   A 1 323 ? -0.443  -0.192  -28.006 1.00 21.10  ?  325 VAL   A O    1 
ATOM   2458 C  CB   . VAL   A 1 323 ? -2.071  -2.865  -29.497 1.00 25.30  ?  325 VAL   A CB   1 
ATOM   2459 C  CG1  . VAL   A 1 323 ? -0.597  -3.078  -29.822 1.00 25.91  ?  325 VAL   A CG1  1 
ATOM   2460 C  CG2  . VAL   A 1 323 ? -2.682  -4.212  -29.071 1.00 24.63  ?  325 VAL   A CG2  1 
ATOM   2461 N  N    . PHE   A 1 324 ? -1.977  0.333   -29.578 1.00 22.46  ?  326 PHE   A N    1 
ATOM   2462 C  CA   . PHE   A 1 324 ? -1.343  1.664   -29.810 1.00 21.06  ?  326 PHE   A CA   1 
ATOM   2463 C  C    . PHE   A 1 324 ? -1.115  2.506   -28.543 1.00 20.34  ?  326 PHE   A C    1 
ATOM   2464 O  O    . PHE   A 1 324 ? 0.013   2.940   -28.275 1.00 19.58  ?  326 PHE   A O    1 
ATOM   2465 C  CB   . PHE   A 1 324 ? -2.060  2.466   -30.877 1.00 20.85  ?  326 PHE   A CB   1 
ATOM   2466 C  CG   . PHE   A 1 324 ? -1.208  3.548   -31.459 1.00 22.32  ?  326 PHE   A CG   1 
ATOM   2467 C  CD1  . PHE   A 1 324 ? -0.091  3.226   -32.227 1.00 23.43  ?  326 PHE   A CD1  1 
ATOM   2468 C  CD2  . PHE   A 1 324 ? -1.491  4.887   -31.207 1.00 22.71  ?  326 PHE   A CD2  1 
ATOM   2469 C  CE1  . PHE   A 1 324 ? 0.707   4.237   -32.760 1.00 23.84  ?  326 PHE   A CE1  1 
ATOM   2470 C  CE2  . PHE   A 1 324 ? -0.705  5.890   -31.739 1.00 22.02  ?  326 PHE   A CE2  1 
ATOM   2471 C  CZ   . PHE   A 1 324 ? 0.399   5.568   -32.489 1.00 22.77  ?  326 PHE   A CZ   1 
ATOM   2472 N  N    . LEU   A 1 325 ? -2.152  2.677   -27.732 1.00 19.61  ?  327 LEU   A N    1 
ATOM   2473 C  CA   . LEU   A 1 325 ? -2.046  3.428   -26.495 1.00 18.04  ?  327 LEU   A CA   1 
ATOM   2474 C  C    . LEU   A 1 325 ? -1.110  2.796   -25.464 1.00 19.42  ?  327 LEU   A C    1 
ATOM   2475 O  O    . LEU   A 1 325 ? -0.299  3.497   -24.810 1.00 16.38  ?  327 LEU   A O    1 
ATOM   2476 C  CB   . LEU   A 1 325 ? -3.422  3.670   -25.939 1.00 19.77  ?  327 LEU   A CB   1 
ATOM   2477 C  CG   . LEU   A 1 325 ? -4.322  4.499   -26.853 1.00 20.91  ?  327 LEU   A CG   1 
ATOM   2478 C  CD1  . LEU   A 1 325 ? -5.739  4.588   -26.297 1.00 22.71  ?  327 LEU   A CD1  1 
ATOM   2479 C  CD2  . LEU   A 1 325 ? -3.764  5.904   -27.017 1.00 22.37  ?  327 LEU   A CD2  1 
ATOM   2480 N  N    . GLY   A 1 326 ? -1.153  1.458   -25.360 1.00 19.03  ?  328 GLY   A N    1 
ATOM   2481 C  CA   . GLY   A 1 326 ? -0.128  0.713   -24.666 1.00 17.82  ?  328 GLY   A CA   1 
ATOM   2482 C  C    . GLY   A 1 326 ? 1.314   1.025   -25.120 1.00 18.64  ?  328 GLY   A C    1 
ATOM   2483 O  O    . GLY   A 1 326 ? 2.210   1.184   -24.298 1.00 18.18  ?  328 GLY   A O    1 
ATOM   2484 N  N    . MET   A 1 327 ? 1.540   1.085   -26.422 1.00 20.13  ?  329 MET   A N    1 
ATOM   2485 C  CA   . MET   A 1 327 ? 2.824   1.437   -26.954 1.00 22.62  ?  329 MET   A CA   1 
ATOM   2486 C  C    . MET   A 1 327 ? 3.236   2.860   -26.560 1.00 21.36  ?  329 MET   A C    1 
ATOM   2487 O  O    . MET   A 1 327 ? 4.387   3.075   -26.141 1.00 20.40  ?  329 MET   A O    1 
ATOM   2488 C  CB   . MET   A 1 327 ? 2.862   1.302   -28.485 1.00 27.80  ?  329 MET   A CB   1 
ATOM   2489 C  CG   . MET   A 1 327 ? 2.952   -0.133  -28.944 1.00 31.98  ?  329 MET   A CG   1 
ATOM   2490 S  SD   . MET   A 1 327 ? 2.259   -0.269  -30.580 1.00 36.34  ?  329 MET   A SD   1 
ATOM   2491 C  CE   . MET   A 1 327 ? 2.477   -2.050  -30.811 1.00 40.97  ?  329 MET   A CE   1 
ATOM   2492 N  N    . PHE   A 1 328 ? 2.308   3.797   -26.669 1.00 18.24  ?  330 PHE   A N    1 
ATOM   2493 C  CA   . PHE   A 1 328 ? 2.570   5.180   -26.299 1.00 19.19  ?  330 PHE   A CA   1 
ATOM   2494 C  C    . PHE   A 1 328 ? 2.992   5.220   -24.819 1.00 20.22  ?  330 PHE   A C    1 
ATOM   2495 O  O    . PHE   A 1 328 ? 4.000   5.874   -24.448 1.00 18.60  ?  330 PHE   A O    1 
ATOM   2496 C  CB   . PHE   A 1 328 ? 1.325   6.011   -26.514 1.00 19.02  ?  330 PHE   A CB   1 
ATOM   2497 C  CG   . PHE   A 1 328 ? 1.412   7.413   -25.962 1.00 21.00  ?  330 PHE   A CG   1 
ATOM   2498 C  CD1  . PHE   A 1 328 ? 1.963   8.435   -26.710 1.00 21.59  ?  330 PHE   A CD1  1 
ATOM   2499 C  CD2  . PHE   A 1 328 ? 0.916   7.709   -24.699 1.00 21.07  ?  330 PHE   A CD2  1 
ATOM   2500 C  CE1  . PHE   A 1 328 ? 2.021   9.747   -26.193 1.00 22.14  ?  330 PHE   A CE1  1 
ATOM   2501 C  CE2  . PHE   A 1 328 ? 1.003   8.988   -24.167 1.00 22.80  ?  330 PHE   A CE2  1 
ATOM   2502 C  CZ   . PHE   A 1 328 ? 1.552   10.017  -24.917 1.00 21.77  ?  330 PHE   A CZ   1 
ATOM   2503 N  N    . LEU   A 1 329 ? 2.257   4.471   -24.001 1.00 20.68  ?  331 LEU   A N    1 
ATOM   2504 C  CA   . LEU   A 1 329 ? 2.488   4.438   -22.543 1.00 22.35  ?  331 LEU   A CA   1 
ATOM   2505 C  C    . LEU   A 1 329 ? 3.831   3.804   -22.220 1.00 20.77  ?  331 LEU   A C    1 
ATOM   2506 O  O    . LEU   A 1 329 ? 4.590   4.344   -21.443 1.00 20.23  ?  331 LEU   A O    1 
ATOM   2507 C  CB   . LEU   A 1 329 ? 1.358   3.706   -21.810 1.00 24.21  ?  331 LEU   A CB   1 
ATOM   2508 C  CG   . LEU   A 1 329 ? 0.803   4.238   -20.483 1.00 26.79  ?  331 LEU   A CG   1 
ATOM   2509 C  CD1  . LEU   A 1 329 ? 0.313   3.068   -19.646 1.00 28.55  ?  331 LEU   A CD1  1 
ATOM   2510 C  CD2  . LEU   A 1 329 ? 1.770   5.091   -19.664 1.00 25.22  ?  331 LEU   A CD2  1 
ATOM   2511 N  N    . TYR   A 1 330 ? 4.093   2.652   -22.819 1.00 20.42  ?  332 TYR   A N    1 
ATOM   2512 C  CA   . TYR   A 1 330 ? 5.417   2.013   -22.751 1.00 20.94  ?  332 TYR   A CA   1 
ATOM   2513 C  C    . TYR   A 1 330 ? 6.535   2.984   -23.094 1.00 20.09  ?  332 TYR   A C    1 
ATOM   2514 O  O    . TYR   A 1 330 ? 7.505   3.078   -22.353 1.00 18.03  ?  332 TYR   A O    1 
ATOM   2515 C  CB   . TYR   A 1 330 ? 5.506   0.825   -23.716 1.00 20.84  ?  332 TYR   A CB   1 
ATOM   2516 C  CG   . TYR   A 1 330 ? 6.894   0.378   -24.051 1.00 23.66  ?  332 TYR   A CG   1 
ATOM   2517 C  CD1  . TYR   A 1 330 ? 7.641   -0.423  -23.156 1.00 24.83  ?  332 TYR   A CD1  1 
ATOM   2518 C  CD2  . TYR   A 1 330 ? 7.500   0.738   -25.256 1.00 24.90  ?  332 TYR   A CD2  1 
ATOM   2519 C  CE1  . TYR   A 1 330 ? 8.931   -0.861  -23.473 1.00 25.04  ?  332 TYR   A CE1  1 
ATOM   2520 C  CE2  . TYR   A 1 330 ? 8.786   0.294   -25.575 1.00 25.18  ?  332 TYR   A CE2  1 
ATOM   2521 C  CZ   . TYR   A 1 330 ? 9.498   -0.513  -24.687 1.00 25.80  ?  332 TYR   A CZ   1 
ATOM   2522 O  OH   . TYR   A 1 330 ? 10.807  -0.921  -24.958 1.00 25.17  ?  332 TYR   A OH   1 
ATOM   2523 N  N    . GLU   A 1 331 ? 6.430   3.646   -24.242 1.00 19.69  ?  333 GLU   A N    1 
ATOM   2524 C  CA   . GLU   A 1 331 ? 7.528   4.492   -24.704 1.00 20.26  ?  333 GLU   A CA   1 
ATOM   2525 C  C    . GLU   A 1 331 ? 7.679   5.712   -23.791 1.00 19.06  ?  333 GLU   A C    1 
ATOM   2526 O  O    . GLU   A 1 331 ? 8.806   6.065   -23.425 1.00 17.59  ?  333 GLU   A O    1 
ATOM   2527 C  CB   . GLU   A 1 331 ? 7.337   4.954   -26.149 1.00 21.85  ?  333 GLU   A CB   1 
ATOM   2528 C  CG   . GLU   A 1 331 ? 7.196   3.865   -27.202 1.00 21.13  ?  333 GLU   A CG   1 
ATOM   2529 C  CD   . GLU   A 1 331 ? 8.496   3.190   -27.551 1.00 22.62  ?  333 GLU   A CD   1 
ATOM   2530 O  OE1  . GLU   A 1 331 ? 9.573   3.534   -26.976 1.00 23.66  ?  333 GLU   A OE1  1 
ATOM   2531 O  OE2  . GLU   A 1 331 ? 8.432   2.301   -28.412 1.00 25.72  ?  333 GLU   A OE2  1 
ATOM   2532 N  N    . TYR   A 1 332 ? 6.573   6.345   -23.410 1.00 19.97  ?  334 TYR   A N    1 
ATOM   2533 C  CA   . TYR   A 1 332 ? 6.627   7.476   -22.437 1.00 22.35  ?  334 TYR   A CA   1 
ATOM   2534 C  C    . TYR   A 1 332 ? 7.201   7.035   -21.044 1.00 23.16  ?  334 TYR   A C    1 
ATOM   2535 O  O    . TYR   A 1 332 ? 8.165   7.637   -20.500 1.00 20.04  ?  334 TYR   A O    1 
ATOM   2536 C  CB   . TYR   A 1 332 ? 5.290   8.189   -22.266 1.00 23.00  ?  334 TYR   A CB   1 
ATOM   2537 C  CG   . TYR   A 1 332 ? 5.462   9.691   -22.121 1.00 26.48  ?  334 TYR   A CG   1 
ATOM   2538 C  CD1  . TYR   A 1 332 ? 6.141   10.225  -21.050 1.00 28.46  ?  334 TYR   A CD1  1 
ATOM   2539 C  CD2  . TYR   A 1 332 ? 4.953   10.582  -23.066 1.00 29.06  ?  334 TYR   A CD2  1 
ATOM   2540 C  CE1  . TYR   A 1 332 ? 6.325   11.596  -20.924 1.00 30.67  ?  334 TYR   A CE1  1 
ATOM   2541 C  CE2  . TYR   A 1 332 ? 5.133   11.960  -22.937 1.00 29.92  ?  334 TYR   A CE2  1 
ATOM   2542 C  CZ   . TYR   A 1 332 ? 5.831   12.461  -21.872 1.00 30.12  ?  334 TYR   A CZ   1 
ATOM   2543 O  OH   . TYR   A 1 332 ? 6.027   13.821  -21.693 1.00 35.35  ?  334 TYR   A OH   1 
ATOM   2544 N  N    . ALA   A 1 333 ? 6.633   5.956   -20.513 1.00 20.43  ?  335 ALA   A N    1 
ATOM   2545 C  CA   . ALA   A 1 333 ? 7.025   5.434   -19.209 1.00 19.98  ?  335 ALA   A CA   1 
ATOM   2546 C  C    . ALA   A 1 333 ? 8.505   5.064   -19.133 1.00 19.29  ?  335 ALA   A C    1 
ATOM   2547 O  O    . ALA   A 1 333 ? 9.210   5.458   -18.144 1.00 18.77  ?  335 ALA   A O    1 
ATOM   2548 C  CB   . ALA   A 1 333 ? 6.156   4.236   -18.860 1.00 20.08  ?  335 ALA   A CB   1 
ATOM   2549 N  N    . ARG   A 1 334 ? 9.036   4.386   -20.155 1.00 19.05  ?  336 ARG   A N    1 
ATOM   2550 C  CA   . ARG   A 1 334 ? 10.472  3.979   -20.049 1.00 20.91  ?  336 ARG   A CA   1 
ATOM   2551 C  C    . ARG   A 1 334 ? 11.411  5.176   -20.073 1.00 20.73  ?  336 ARG   A C    1 
ATOM   2552 O  O    . ARG   A 1 334 ? 12.542  5.089   -19.508 1.00 20.22  ?  336 ARG   A O    1 
ATOM   2553 C  CB   . ARG   A 1 334 ? 10.905  2.885   -21.014 1.00 21.36  ?  336 ARG   A CB   1 
ATOM   2554 C  CG   . ARG   A 1 334 ? 11.165  3.282   -22.443 1.00 24.30  ?  336 ARG   A CG   1 
ATOM   2555 C  CD   . ARG   A 1 334 ? 10.950  2.052   -23.262 1.00 26.82  ?  336 ARG   A CD   1 
ATOM   2556 N  NE   . ARG   A 1 334 ? 11.220  2.308   -24.650 1.00 29.14  ?  336 ARG   A NE   1 
ATOM   2557 C  CZ   . ARG   A 1 334 ? 12.176  1.725   -25.374 1.00 29.09  ?  336 ARG   A CZ   1 
ATOM   2558 N  NH1  . ARG   A 1 334 ? 12.992  0.789   -24.876 1.00 30.56  ?  336 ARG   A NH1  1 
ATOM   2559 N  NH2  . ARG   A 1 334 ? 12.320  2.088   -26.634 1.00 29.24  ?  336 ARG   A NH2  1 
ATOM   2560 N  N    . ARG   A 1 335 ? 10.944  6.279   -20.676 1.00 20.59  ?  337 ARG   A N    1 
ATOM   2561 C  CA   . ARG   A 1 335 ? 11.696  7.547   -20.664 1.00 21.72  ?  337 ARG   A CA   1 
ATOM   2562 C  C    . ARG   A 1 335 ? 11.580  8.296   -19.356 1.00 23.36  ?  337 ARG   A C    1 
ATOM   2563 O  O    . ARG   A 1 335 ? 12.473  9.100   -19.046 1.00 23.64  ?  337 ARG   A O    1 
ATOM   2564 C  CB   . ARG   A 1 335 ? 11.299  8.435   -21.839 1.00 20.98  ?  337 ARG   A CB   1 
ATOM   2565 C  CG   . ARG   A 1 335 ? 11.835  7.888   -23.156 1.00 21.77  ?  337 ARG   A CG   1 
ATOM   2566 C  CD   . ARG   A 1 335 ? 11.225  8.594   -24.336 1.00 22.85  ?  337 ARG   A CD   1 
ATOM   2567 N  NE   . ARG   A 1 335 ? 11.643  8.094   -25.646 1.00 24.01  ?  337 ARG   A NE   1 
ATOM   2568 C  CZ   . ARG   A 1 335 ? 11.338  6.902   -26.182 1.00 26.90  ?  337 ARG   A CZ   1 
ATOM   2569 N  NH1  . ARG   A 1 335 ? 10.664  5.977   -25.498 1.00 26.97  ?  337 ARG   A NH1  1 
ATOM   2570 N  NH2  . ARG   A 1 335 ? 11.738  6.612   -27.431 1.00 26.78  ?  337 ARG   A NH2  1 
ATOM   2571 N  N    . HIS   A 1 336 ? 10.526  8.007   -18.565 1.00 23.79  ?  338 HIS   A N    1 
ATOM   2572 C  CA   . HIS   A 1 336 ? 10.244  8.752   -17.345 1.00 23.12  ?  338 HIS   A CA   1 
ATOM   2573 C  C    . HIS   A 1 336 ? 10.095  7.975   -16.035 1.00 24.44  ?  338 HIS   A C    1 
ATOM   2574 O  O    . HIS   A 1 336 ? 8.996   7.890   -15.478 1.00 24.87  ?  338 HIS   A O    1 
ATOM   2575 C  CB   . HIS   A 1 336 ? 9.055   9.686   -17.616 1.00 21.55  ?  338 HIS   A CB   1 
ATOM   2576 C  CG   . HIS   A 1 336 ? 9.404   10.809  -18.520 1.00 21.12  ?  338 HIS   A CG   1 
ATOM   2577 N  ND1  . HIS   A 1 336 ? 9.177   10.771  -19.886 1.00 23.09  ?  338 HIS   A ND1  1 
ATOM   2578 C  CD2  . HIS   A 1 336 ? 10.052  11.974  -18.273 1.00 21.30  ?  338 HIS   A CD2  1 
ATOM   2579 C  CE1  . HIS   A 1 336 ? 9.634   11.894  -20.425 1.00 23.72  ?  338 HIS   A CE1  1 
ATOM   2580 N  NE2  . HIS   A 1 336 ? 10.186  12.629  -19.475 1.00 23.52  ?  338 HIS   A NE2  1 
ATOM   2581 N  N    . PRO   A 1 337 ? 11.212  7.417   -15.515 1.00 27.51  ?  339 PRO   A N    1 
ATOM   2582 C  CA   . PRO   A 1 337 ? 11.206  6.810   -14.165 1.00 28.58  ?  339 PRO   A CA   1 
ATOM   2583 C  C    . PRO   A 1 337 ? 10.833  7.788   -13.033 1.00 27.88  ?  339 PRO   A C    1 
ATOM   2584 O  O    . PRO   A 1 337 ? 10.369  7.367   -11.986 1.00 28.29  ?  339 PRO   A O    1 
ATOM   2585 C  CB   . PRO   A 1 337 ? 12.663  6.310   -13.970 1.00 30.77  ?  339 PRO   A CB   1 
ATOM   2586 C  CG   . PRO   A 1 337 ? 13.469  6.902   -15.092 1.00 30.04  ?  339 PRO   A CG   1 
ATOM   2587 C  CD   . PRO   A 1 337 ? 12.503  7.210   -16.203 1.00 29.25  ?  339 PRO   A CD   1 
ATOM   2588 N  N    . ASP   A 1 338 ? 11.068  9.072   -13.270 1.00 26.25  ?  340 ASP   A N    1 
ATOM   2589 C  CA   . ASP   A 1 338 ? 10.760  10.135  -12.347 1.00 24.19  ?  340 ASP   A CA   1 
ATOM   2590 C  C    . ASP   A 1 338 ? 9.277   10.477  -12.240 1.00 24.27  ?  340 ASP   A C    1 
ATOM   2591 O  O    . ASP   A 1 338 ? 8.909   11.247  -11.388 1.00 22.89  ?  340 ASP   A O    1 
ATOM   2592 C  CB   . ASP   A 1 338 ? 11.565  11.400  -12.713 1.00 25.34  ?  340 ASP   A CB   1 
ATOM   2593 C  CG   . ASP   A 1 338 ? 11.337  11.875  -14.146 1.00 27.44  ?  340 ASP   A CG   1 
ATOM   2594 O  OD1  . ASP   A 1 338 ? 11.096  11.034  -15.073 1.00 28.81  ?  340 ASP   A OD1  1 
ATOM   2595 O  OD2  . ASP   A 1 338 ? 11.422  13.106  -14.360 1.00 28.56  ?  340 ASP   A OD2  1 
ATOM   2596 N  N    . TYR   A 1 339 ? 8.429   9.933   -13.118 1.00 23.21  ?  341 TYR   A N    1 
ATOM   2597 C  CA   . TYR   A 1 339 ? 7.033   10.258  -13.117 1.00 20.79  ?  341 TYR   A CA   1 
ATOM   2598 C  C    . TYR   A 1 339 ? 6.271   9.291   -12.254 1.00 20.68  ?  341 TYR   A C    1 
ATOM   2599 O  O    . TYR   A 1 339 ? 6.649   8.116   -12.125 1.00 19.69  ?  341 TYR   A O    1 
ATOM   2600 C  CB   . TYR   A 1 339 ? 6.531   10.214  -14.547 1.00 21.40  ?  341 TYR   A CB   1 
ATOM   2601 C  CG   . TYR   A 1 339 ? 6.849   11.410  -15.378 1.00 19.54  ?  341 TYR   A CG   1 
ATOM   2602 C  CD1  . TYR   A 1 339 ? 7.717   12.424  -14.946 1.00 20.62  ?  341 TYR   A CD1  1 
ATOM   2603 C  CD2  . TYR   A 1 339 ? 6.296   11.529  -16.627 1.00 21.83  ?  341 TYR   A CD2  1 
ATOM   2604 C  CE1  . TYR   A 1 339 ? 8.011   13.514  -15.766 1.00 20.43  ?  341 TYR   A CE1  1 
ATOM   2605 C  CE2  . TYR   A 1 339 ? 6.558   12.634  -17.436 1.00 20.87  ?  341 TYR   A CE2  1 
ATOM   2606 C  CZ   . TYR   A 1 339 ? 7.424   13.599  -17.012 1.00 19.93  ?  341 TYR   A CZ   1 
ATOM   2607 O  OH   . TYR   A 1 339 ? 7.690   14.643  -17.842 1.00 21.80  ?  341 TYR   A OH   1 
ATOM   2608 N  N    . SER   A 1 340 ? 5.183   9.761   -11.651 1.00 19.68  ?  342 SER   A N    1 
ATOM   2609 C  CA   . SER   A 1 340 ? 4.278   8.835   -11.057 1.00 19.04  ?  342 SER   A CA   1 
ATOM   2610 C  C    . SER   A 1 340 ? 3.644   8.045   -12.215 1.00 19.36  ?  342 SER   A C    1 
ATOM   2611 O  O    . SER   A 1 340 ? 3.431   8.590   -13.304 1.00 21.29  ?  342 SER   A O    1 
ATOM   2612 C  CB   . SER   A 1 340 ? 3.227   9.532   -10.232 1.00 21.31  ?  342 SER   A CB   1 
ATOM   2613 O  OG   . SER   A 1 340 ? 2.472   10.444  -11.025 1.00 23.89  ?  342 SER   A OG   1 
ATOM   2614 N  N    . VAL   A 1 341 ? 3.413   6.754   -12.022 1.00 16.06  ?  343 VAL   A N    1 
ATOM   2615 C  CA   . VAL   A 1 341 ? 2.521   6.046   -12.893 1.00 15.70  ?  343 VAL   A CA   1 
ATOM   2616 C  C    . VAL   A 1 341 ? 1.219   6.794   -13.224 1.00 14.37  ?  343 VAL   A C    1 
ATOM   2617 O  O    . VAL   A 1 341 ? 0.813   6.801   -14.367 1.00 12.37  ?  343 VAL   A O    1 
ATOM   2618 C  CB   . VAL   A 1 341 ? 2.050   4.705   -12.272 1.00 15.29  ?  343 VAL   A CB   1 
ATOM   2619 C  CG1  . VAL   A 1 341 ? 0.900   4.133   -13.118 1.00 14.58  ?  343 VAL   A CG1  1 
ATOM   2620 C  CG2  . VAL   A 1 341 ? 3.224   3.735   -12.146 1.00 15.00  ?  343 VAL   A CG2  1 
ATOM   2621 N  N    . VAL   A 1 342 ? 0.527   7.317   -12.224 1.00 15.54  ?  344 VAL   A N    1 
ATOM   2622 C  CA   . VAL   A 1 342 ? -0.764  7.958   -12.463 1.00 18.23  ?  344 VAL   A CA   1 
ATOM   2623 C  C    . VAL   A 1 342 ? -0.628  9.159   -13.389 1.00 18.59  ?  344 VAL   A C    1 
ATOM   2624 O  O    . VAL   A 1 342 ? -1.542  9.416   -14.183 1.00 16.81  ?  344 VAL   A O    1 
ATOM   2625 C  CB   . VAL   A 1 342 ? -1.566  8.402   -11.211 1.00 20.90  ?  344 VAL   A CB   1 
ATOM   2626 C  CG1  . VAL   A 1 342 ? -2.070  7.183   -10.434 1.00 25.57  ?  344 VAL   A CG1  1 
ATOM   2627 C  CG2  . VAL   A 1 342 ? -0.784  9.384   -10.352 1.00 21.37  ?  344 VAL   A CG2  1 
ATOM   2628 N  N    . LEU   A 1 343 ? 0.502   9.875   -13.291 1.00 19.02  ?  345 LEU   A N    1 
ATOM   2629 C  CA   . LEU   A 1 343 ? 0.778   10.951  -14.231 1.00 19.05  ?  345 LEU   A CA   1 
ATOM   2630 C  C    . LEU   A 1 343 ? 1.011   10.349  -15.608 1.00 18.97  ?  345 LEU   A C    1 
ATOM   2631 O  O    . LEU   A 1 343 ? 0.586   10.941  -16.625 1.00 17.06  ?  345 LEU   A O    1 
ATOM   2632 C  CB   . LEU   A 1 343 ? 1.994   11.772  -13.833 1.00 19.80  ?  345 LEU   A CB   1 
ATOM   2633 C  CG   . LEU   A 1 343 ? 2.486   12.745  -14.908 1.00 19.54  ?  345 LEU   A CG   1 
ATOM   2634 C  CD1  . LEU   A 1 343 ? 1.436   13.812  -15.191 1.00 20.00  ?  345 LEU   A CD1  1 
ATOM   2635 C  CD2  . LEU   A 1 343 ? 3.847   13.298  -14.481 1.00 18.67  ?  345 LEU   A CD2  1 
ATOM   2636 N  N    . LEU   A 1 344 ? 1.667   9.191   -15.675 1.00 15.67  ?  346 LEU   A N    1 
ATOM   2637 C  CA   . LEU   A 1 344 ? 1.851   8.563   -17.011 1.00 16.52  ?  346 LEU   A CA   1 
ATOM   2638 C  C    . LEU   A 1 344 ? 0.474   8.156   -17.637 1.00 16.00  ?  346 LEU   A C    1 
ATOM   2639 O  O    . LEU   A 1 344 ? 0.302   8.255   -18.849 1.00 16.26  ?  346 LEU   A O    1 
ATOM   2640 C  CB   . LEU   A 1 344 ? 2.861   7.410   -16.989 1.00 15.87  ?  346 LEU   A CB   1 
ATOM   2641 C  CG   . LEU   A 1 344 ? 4.299   7.887   -16.810 1.00 16.14  ?  346 LEU   A CG   1 
ATOM   2642 C  CD1  . LEU   A 1 344 ? 5.102   6.819   -16.092 1.00 16.12  ?  346 LEU   A CD1  1 
ATOM   2643 C  CD2  . LEU   A 1 344 ? 4.984   8.281   -18.116 1.00 15.32  ?  346 LEU   A CD2  1 
ATOM   2644 N  N    . LEU   A 1 345 ? -0.489  7.757   -16.811 1.00 17.71  ?  347 LEU   A N    1 
ATOM   2645 C  CA   . LEU   A 1 345 ? -1.851  7.427   -17.265 1.00 19.27  ?  347 LEU   A CA   1 
ATOM   2646 C  C    . LEU   A 1 345 ? -2.707  8.640   -17.609 1.00 17.72  ?  347 LEU   A C    1 
ATOM   2647 O  O    . LEU   A 1 345 ? -3.534  8.550   -18.493 1.00 15.55  ?  347 LEU   A O    1 
ATOM   2648 C  CB   . LEU   A 1 345 ? -2.623  6.598   -16.239 1.00 21.75  ?  347 LEU   A CB   1 
ATOM   2649 C  CG   . LEU   A 1 345 ? -2.067  5.241   -15.773 1.00 23.41  ?  347 LEU   A CG   1 
ATOM   2650 C  CD1  . LEU   A 1 345 ? -3.167  4.441   -15.097 1.00 25.13  ?  347 LEU   A CD1  1 
ATOM   2651 C  CD2  . LEU   A 1 345 ? -1.474  4.480   -16.912 1.00 23.95  ?  347 LEU   A CD2  1 
ATOM   2652 N  N    . ARG   A 1 346 ? -2.492  9.761   -16.919 1.00 18.16  ?  348 ARG   A N    1 
ATOM   2653 C  CA   . ARG   A 1 346 ? -3.118  11.031  -17.329 1.00 18.15  ?  348 ARG   A CA   1 
ATOM   2654 C  C    . ARG   A 1 346 ? -2.773  11.429  -18.756 1.00 18.24  ?  348 ARG   A C    1 
ATOM   2655 O  O    . ARG   A 1 346 ? -3.657  11.695  -19.572 1.00 17.65  ?  348 ARG   A O    1 
ATOM   2656 C  CB   . ARG   A 1 346 ? -2.728  12.144  -16.370 1.00 19.34  ?  348 ARG   A CB   1 
ATOM   2657 C  CG   . ARG   A 1 346 ? -3.579  12.144  -15.162 1.00 19.19  ?  348 ARG   A CG   1 
ATOM   2658 C  CD   . ARG   A 1 346 ? -3.212  13.215  -14.182 1.00 20.92  ?  348 ARG   A CD   1 
ATOM   2659 N  NE   . ARG   A 1 346 ? -3.533  12.740  -12.839 1.00 19.67  ?  348 ARG   A NE   1 
ATOM   2660 C  CZ   . ARG   A 1 346 ? -2.702  12.711  -11.799 1.00 19.93  ?  348 ARG   A CZ   1 
ATOM   2661 N  NH1  . ARG   A 1 346 ? -1.453  13.208  -11.857 1.00 18.78  ?  348 ARG   A NH1  1 
ATOM   2662 N  NH2  . ARG   A 1 346 ? -3.159  12.220  -10.651 1.00 19.86  ?  348 ARG   A NH2  1 
ATOM   2663 N  N    . LEU   A 1 347 ? -1.472  11.428  -19.016 1.00 17.63  ?  349 LEU   A N    1 
ATOM   2664 C  CA   . LEU   A 1 347 ? -0.851  11.657  -20.294 1.00 17.73  ?  349 LEU   A CA   1 
ATOM   2665 C  C    . LEU   A 1 347 ? -1.324  10.726  -21.399 1.00 17.23  ?  349 LEU   A C    1 
ATOM   2666 O  O    . LEU   A 1 347 ? -1.576  11.179  -22.504 1.00 16.29  ?  349 LEU   A O    1 
ATOM   2667 C  CB   . LEU   A 1 347 ? 0.682   11.483  -20.168 1.00 18.49  ?  349 LEU   A CB   1 
ATOM   2668 C  CG   . LEU   A 1 347 ? 1.465   12.446  -19.264 1.00 19.67  ?  349 LEU   A CG   1 
ATOM   2669 C  CD1  . LEU   A 1 347 ? 2.959   12.147  -19.272 1.00 18.96  ?  349 LEU   A CD1  1 
ATOM   2670 C  CD2  . LEU   A 1 347 ? 1.222   13.886  -19.642 1.00 21.48  ?  349 LEU   A CD2  1 
ATOM   2671 N  N    . ALA   A 1 348 ? -1.394  9.421   -21.113 1.00 15.34  ?  350 ALA   A N    1 
ATOM   2672 C  CA   . ALA   A 1 348 ? -1.993  8.471   -22.016 1.00 15.22  ?  350 ALA   A CA   1 
ATOM   2673 C  C    . ALA   A 1 348 ? -3.476  8.759   -22.323 1.00 15.17  ?  350 ALA   A C    1 
ATOM   2674 O  O    . ALA   A 1 348 ? -3.904  8.719   -23.481 1.00 16.04  ?  350 ALA   A O    1 
ATOM   2675 C  CB   . ALA   A 1 348 ? -1.836  7.046   -21.475 1.00 15.65  ?  350 ALA   A CB   1 
ATOM   2676 N  N    . LYS   A 1 349 ? -4.253  9.067   -21.315 1.00 15.82  ?  351 LYS   A N    1 
ATOM   2677 C  CA   . LYS   A 1 349 ? -5.650  9.362   -21.543 1.00 17.37  ?  351 LYS   A CA   1 
ATOM   2678 C  C    . LYS   A 1 349 ? -5.796  10.681  -22.309 1.00 19.73  ?  351 LYS   A C    1 
ATOM   2679 O  O    . LYS   A 1 349 ? -6.751  10.830  -23.078 1.00 19.61  ?  351 LYS   A O    1 
ATOM   2680 C  CB   . LYS   A 1 349 ? -6.364  9.451   -20.225 1.00 18.61  ?  351 LYS   A CB   1 
ATOM   2681 C  CG   . LYS   A 1 349 ? -7.880  9.450   -20.299 1.00 20.34  ?  351 LYS   A CG   1 
ATOM   2682 C  CD   . LYS   A 1 349 ? -8.430  9.680   -18.909 1.00 22.63  ?  351 LYS   A CD   1 
ATOM   2683 N  N    . THR   A 1 350 ? -4.871  11.635  -22.098 1.00 19.92  ?  352 THR   A N    1 
ATOM   2684 C  CA   . THR   A 1 350 ? -4.914  12.912  -22.858 1.00 20.53  ?  352 THR   A CA   1 
ATOM   2685 C  C    . THR   A 1 350 ? -4.626  12.624  -24.319 1.00 20.40  ?  352 THR   A C    1 
ATOM   2686 O  O    . THR   A 1 350 ? -5.302  13.148  -25.184 1.00 19.49  ?  352 THR   A O    1 
ATOM   2687 C  CB   . THR   A 1 350 ? -3.912  13.943  -22.321 1.00 20.62  ?  352 THR   A CB   1 
ATOM   2688 O  OG1  . THR   A 1 350 ? -4.238  14.235  -20.966 1.00 20.92  ?  352 THR   A OG1  1 
ATOM   2689 C  CG2  . THR   A 1 350 ? -3.930  15.224  -23.148 1.00 21.22  ?  352 THR   A CG2  1 
ATOM   2690 N  N    . TYR   A 1 351 ? -3.670  11.740  -24.592 1.00 20.14  ?  353 TYR   A N    1 
ATOM   2691 C  CA   . TYR   A 1 351 ? -3.430  11.319  -25.964 1.00 21.18  ?  353 TYR   A CA   1 
ATOM   2692 C  C    . TYR   A 1 351 ? -4.629  10.582  -26.618 1.00 22.48  ?  353 TYR   A C    1 
ATOM   2693 O  O    . TYR   A 1 351 ? -4.942  10.811  -27.795 1.00 20.49  ?  353 TYR   A O    1 
ATOM   2694 C  CB   . TYR   A 1 351 ? -2.192  10.466  -26.021 1.00 20.86  ?  353 TYR   A CB   1 
ATOM   2695 C  CG   . TYR   A 1 351 ? -1.733  10.081  -27.381 1.00 20.29  ?  353 TYR   A CG   1 
ATOM   2696 C  CD1  . TYR   A 1 351 ? -1.240  11.042  -28.246 1.00 21.33  ?  353 TYR   A CD1  1 
ATOM   2697 C  CD2  . TYR   A 1 351 ? -1.736  8.743   -27.799 1.00 19.81  ?  353 TYR   A CD2  1 
ATOM   2698 C  CE1  . TYR   A 1 351 ? -0.802  10.723  -29.508 1.00 20.83  ?  353 TYR   A CE1  1 
ATOM   2699 C  CE2  . TYR   A 1 351 ? -1.289  8.404   -29.061 1.00 20.51  ?  353 TYR   A CE2  1 
ATOM   2700 C  CZ   . TYR   A 1 351 ? -0.816  9.405   -29.919 1.00 21.14  ?  353 TYR   A CZ   1 
ATOM   2701 O  OH   . TYR   A 1 351 ? -0.333  9.123   -31.192 1.00 19.71  ?  353 TYR   A OH   1 
ATOM   2702 N  N    . GLU   A 1 352 ? -5.256  9.685   -25.859 1.00 24.62  ?  354 GLU   A N    1 
ATOM   2703 C  CA   . GLU   A 1 352 ? -6.438  8.915   -26.325 1.00 24.93  ?  354 GLU   A CA   1 
ATOM   2704 C  C    . GLU   A 1 352 ? -7.519  9.880   -26.693 1.00 23.36  ?  354 GLU   A C    1 
ATOM   2705 O  O    . GLU   A 1 352 ? -8.135  9.753   -27.743 1.00 22.87  ?  354 GLU   A O    1 
ATOM   2706 C  CB   . GLU   A 1 352 ? -7.026  8.012   -25.227 1.00 24.97  ?  354 GLU   A CB   1 
ATOM   2707 C  CG   . GLU   A 1 352 ? -8.261  7.157   -25.620 1.00 26.34  ?  354 GLU   A CG   1 
ATOM   2708 C  CD   . GLU   A 1 352 ? -8.690  6.202   -24.503 1.00 28.73  ?  354 GLU   A CD   1 
ATOM   2709 O  OE1  . GLU   A 1 352 ? -8.675  6.628   -23.331 1.00 33.17  ?  354 GLU   A OE1  1 
ATOM   2710 O  OE2  . GLU   A 1 352 ? -9.025  5.011   -24.750 1.00 31.76  ?  354 GLU   A OE2  1 
ATOM   2711 N  N    . THR   A 1 353 ? -7.758  10.825  -25.806 1.00 23.54  ?  355 THR   A N    1 
ATOM   2712 C  CA   . THR   A 1 353 ? -8.887  11.736  -25.978 1.00 27.40  ?  355 THR   A CA   1 
ATOM   2713 C  C    . THR   A 1 353 ? -8.698  12.573  -27.250 1.00 27.47  ?  355 THR   A C    1 
ATOM   2714 O  O    . THR   A 1 353 ? -9.643  12.771  -28.013 1.00 29.83  ?  355 THR   A O    1 
ATOM   2715 C  CB   . THR   A 1 353 ? -9.056  12.631  -24.763 1.00 27.34  ?  355 THR   A CB   1 
ATOM   2716 O  OG1  . THR   A 1 353 ? -9.217  11.817  -23.607 1.00 26.65  ?  355 THR   A OG1  1 
ATOM   2717 C  CG2  . THR   A 1 353 ? -10.248 13.547  -24.908 1.00 29.20  ?  355 THR   A CG2  1 
ATOM   2718 N  N    . THR   A 1 354 ? -7.467  13.003  -27.496 1.00 28.80  ?  356 THR   A N    1 
ATOM   2719 C  CA   . THR   A 1 354 ? -7.156  13.800  -28.659 1.00 31.08  ?  356 THR   A CA   1 
ATOM   2720 C  C    . THR   A 1 354 ? -7.220  12.965  -29.934 1.00 31.53  ?  356 THR   A C    1 
ATOM   2721 O  O    . THR   A 1 354 ? -7.706  13.474  -30.967 1.00 28.54  ?  356 THR   A O    1 
ATOM   2722 C  CB   . THR   A 1 354 ? -5.758  14.421  -28.564 1.00 33.16  ?  356 THR   A CB   1 
ATOM   2723 O  OG1  . THR   A 1 354 ? -4.826  13.371  -28.316 1.00 38.21  ?  356 THR   A OG1  1 
ATOM   2724 C  CG2  . THR   A 1 354 ? -5.702  15.406  -27.436 1.00 32.36  ?  356 THR   A CG2  1 
ATOM   2725 N  N    . LEU   A 1 355 ? -6.744  11.705  -29.892 1.00 28.08  ?  357 LEU   A N    1 
ATOM   2726 C  CA   . LEU   A 1 355 ? -6.861  10.832  -31.074 1.00 27.50  ?  357 LEU   A CA   1 
ATOM   2727 C  C    . LEU   A 1 355 ? -8.302  10.618  -31.400 1.00 26.63  ?  357 LEU   A C    1 
ATOM   2728 O  O    . LEU   A 1 355 ? -8.677  10.679  -32.556 1.00 29.17  ?  357 LEU   A O    1 
ATOM   2729 C  CB   . LEU   A 1 355 ? -6.166  9.477   -30.905 1.00 27.36  ?  357 LEU   A CB   1 
ATOM   2730 C  CG   . LEU   A 1 355 ? -4.638  9.534   -30.909 1.00 26.52  ?  357 LEU   A CG   1 
ATOM   2731 C  CD1  . LEU   A 1 355 ? -4.117  8.156   -31.239 1.00 26.98  ?  357 LEU   A CD1  1 
ATOM   2732 C  CD2  . LEU   A 1 355 ? -4.063  10.537  -31.912 1.00 25.25  ?  357 LEU   A CD2  1 
ATOM   2733 N  N    . GLU   A 1 356 ? -9.117  10.431  -30.375 1.00 27.31  ?  358 GLU   A N    1 
ATOM   2734 C  CA   . GLU   A 1 356 ? -10.533 10.145  -30.569 1.00 29.23  ?  358 GLU   A CA   1 
ATOM   2735 C  C    . GLU   A 1 356 ? -11.216 11.284  -31.262 1.00 31.93  ?  358 GLU   A C    1 
ATOM   2736 O  O    . GLU   A 1 356 ? -12.034 11.045  -32.165 1.00 30.37  ?  358 GLU   A O    1 
ATOM   2737 C  CB   . GLU   A 1 356 ? -11.230 9.859   -29.260 1.00 28.01  ?  358 GLU   A CB   1 
ATOM   2738 C  CG   . GLU   A 1 356 ? -10.953 8.458   -28.750 1.00 30.14  ?  358 GLU   A CG   1 
ATOM   2739 C  CD   . GLU   A 1 356 ? -11.774 7.369   -29.411 1.00 32.77  ?  358 GLU   A CD   1 
ATOM   2740 O  OE1  . GLU   A 1 356 ? -12.967 7.616   -29.700 1.00 35.22  ?  358 GLU   A OE1  1 
ATOM   2741 O  OE2  . GLU   A 1 356 ? -11.236 6.241   -29.585 1.00 32.71  ?  358 GLU   A OE2  1 
ATOM   2742 N  N    . LYS   A 1 357 ? -10.879 12.510  -30.827 1.00 34.06  ?  359 LYS   A N    1 
ATOM   2743 C  CA   . LYS   A 1 357 ? -11.353 13.742  -31.465 1.00 32.70  ?  359 LYS   A CA   1 
ATOM   2744 C  C    . LYS   A 1 357 ? -10.766 13.942  -32.853 1.00 30.50  ?  359 LYS   A C    1 
ATOM   2745 O  O    . LYS   A 1 357 ? -11.470 14.176  -33.828 1.00 29.68  ?  359 LYS   A O    1 
ATOM   2746 C  CB   . LYS   A 1 357 ? -11.019 14.975  -30.597 1.00 36.93  ?  359 LYS   A CB   1 
ATOM   2747 C  CG   . LYS   A 1 357 ? -11.242 16.314  -31.318 1.00 37.98  ?  359 LYS   A CG   1 
ATOM   2748 C  CD   . LYS   A 1 357 ? -11.202 17.545  -30.418 1.00 42.73  ?  359 LYS   A CD   1 
ATOM   2749 C  CE   . LYS   A 1 357 ? -9.798  18.066  -30.161 1.00 45.77  ?  359 LYS   A CE   1 
ATOM   2750 N  NZ   . LYS   A 1 357 ? -9.691  19.531  -30.430 1.00 44.94  ?  359 LYS   A NZ   1 
ATOM   2751 N  N    . CYS   A 1 358 ? -9.448  13.864  -32.930 1.00 32.53  ?  360 CYS   A N    1 
ATOM   2752 C  CA   . CYS   A 1 358 ? -8.723  14.246  -34.126 1.00 30.12  ?  360 CYS   A CA   1 
ATOM   2753 C  C    . CYS   A 1 358 ? -8.757  13.285  -35.297 1.00 29.70  ?  360 CYS   A C    1 
ATOM   2754 O  O    . CYS   A 1 358 ? -8.752  13.749  -36.412 1.00 31.59  ?  360 CYS   A O    1 
ATOM   2755 C  CB   . CYS   A 1 358 ? -7.301  14.617  -33.765 1.00 31.24  ?  360 CYS   A CB   1 
ATOM   2756 S  SG   . CYS   A 1 358 ? -7.303  16.089  -32.723 1.00 33.62  ?  360 CYS   A SG   1 
ATOM   2757 N  N    . CYS   A 1 359 ? -8.843  11.980  -35.070 1.00 28.12  ?  361 CYS   A N    1 
ATOM   2758 C  CA   . CYS   A 1 359 ? -8.901  11.038  -36.173 1.00 33.50  ?  361 CYS   A CA   1 
ATOM   2759 C  C    . CYS   A 1 359 ? -10.230 11.104  -36.990 1.00 37.10  ?  361 CYS   A C    1 
ATOM   2760 O  O    . CYS   A 1 359 ? -10.237 10.747  -38.159 1.00 40.44  ?  361 CYS   A O    1 
ATOM   2761 C  CB   . CYS   A 1 359 ? -8.459  9.631   -35.710 1.00 33.59  ?  361 CYS   A CB   1 
ATOM   2762 S  SG   . CYS   A 1 359 ? -6.687  9.667   -35.192 1.00 33.05  ?  361 CYS   A SG   1 
ATOM   2763 N  N    . ALA   A 1 360 ? -11.300 11.641  -36.407 1.00 40.61  ?  362 ALA   A N    1 
ATOM   2764 C  CA   . ALA   A 1 360 ? -12.542 11.925  -37.123 1.00 44.97  ?  362 ALA   A CA   1 
ATOM   2765 C  C    . ALA   A 1 360 ? -12.392 13.094  -38.119 1.00 52.26  ?  362 ALA   A C    1 
ATOM   2766 O  O    . ALA   A 1 360 ? -12.717 12.961  -39.316 1.00 48.93  ?  362 ALA   A O    1 
ATOM   2767 C  CB   . ALA   A 1 360 ? -13.651 12.231  -36.127 1.00 45.71  ?  362 ALA   A CB   1 
ATOM   2768 N  N    . ALA   A 1 361 ? -11.888 14.226  -37.622 1.00 56.49  ?  363 ALA   A N    1 
ATOM   2769 C  CA   . ALA   A 1 361 ? -11.720 15.458  -38.421 1.00 55.52  ?  363 ALA   A CA   1 
ATOM   2770 C  C    . ALA   A 1 361 ? -11.010 15.201  -39.764 1.00 58.57  ?  363 ALA   A C    1 
ATOM   2771 O  O    . ALA   A 1 361 ? -10.277 14.221  -39.910 1.00 61.40  ?  363 ALA   A O    1 
ATOM   2772 C  CB   . ALA   A 1 361 ? -10.974 16.510  -37.609 1.00 54.04  ?  363 ALA   A CB   1 
ATOM   2773 N  N    . ALA   A 1 362 ? -11.244 16.069  -40.747 1.00 60.13  ?  364 ALA   A N    1 
ATOM   2774 C  CA   . ALA   A 1 362 ? -10.718 15.857  -42.103 1.00 56.41  ?  364 ALA   A CA   1 
ATOM   2775 C  C    . ALA   A 1 362 ? -9.188  15.940  -42.154 1.00 58.54  ?  364 ALA   A C    1 
ATOM   2776 O  O    . ALA   A 1 362 ? -8.553  15.228  -42.939 1.00 61.70  ?  364 ALA   A O    1 
ATOM   2777 C  CB   . ALA   A 1 362 ? -11.340 16.849  -43.078 1.00 58.78  ?  364 ALA   A CB   1 
ATOM   2778 N  N    . ASP   A 1 363 ? -8.588  16.791  -41.318 1.00 56.08  ?  365 ASP   A N    1 
ATOM   2779 C  CA   . ASP   A 1 363 ? -7.128  16.817  -41.174 1.00 49.50  ?  365 ASP   A CA   1 
ATOM   2780 C  C    . ASP   A 1 363 ? -6.712  16.512  -39.724 1.00 45.77  ?  365 ASP   A C    1 
ATOM   2781 O  O    . ASP   A 1 363 ? -6.418  17.443  -38.935 1.00 42.95  ?  365 ASP   A O    1 
ATOM   2782 C  CB   . ASP   A 1 363 ? -6.546  18.159  -41.660 1.00 49.10  ?  365 ASP   A CB   1 
ATOM   2783 C  CG   . ASP   A 1 363 ? -5.035  18.075  -41.956 1.00 51.82  ?  365 ASP   A CG   1 
ATOM   2784 O  OD1  . ASP   A 1 363 ? -4.468  16.954  -41.871 1.00 49.64  ?  365 ASP   A OD1  1 
ATOM   2785 O  OD2  . ASP   A 1 363 ? -4.415  19.121  -42.296 1.00 46.39  ?  365 ASP   A OD2  1 
ATOM   2786 N  N    . PRO   A 1 364 ? -6.670  15.204  -39.365 1.00 40.89  ?  366 PRO   A N    1 
ATOM   2787 C  CA   . PRO   A 1 364 ? -6.222  14.821  -38.016 1.00 35.46  ?  366 PRO   A CA   1 
ATOM   2788 C  C    . PRO   A 1 364 ? -4.895  15.436  -37.639 1.00 36.25  ?  366 PRO   A C    1 
ATOM   2789 O  O    . PRO   A 1 364 ? -4.722  15.907  -36.518 1.00 30.64  ?  366 PRO   A O    1 
ATOM   2790 C  CB   . PRO   A 1 364 ? -6.093  13.291  -38.105 1.00 36.63  ?  366 PRO   A CB   1 
ATOM   2791 C  CG   . PRO   A 1 364 ? -7.096  12.878  -39.147 1.00 37.03  ?  366 PRO   A CG   1 
ATOM   2792 C  CD   . PRO   A 1 364 ? -7.140  14.027  -40.138 1.00 40.06  ?  366 PRO   A CD   1 
ATOM   2793 N  N    . HIS   A 1 365 ? -3.977  15.454  -38.591 1.00 37.54  ?  367 HIS   A N    1 
ATOM   2794 C  CA   . HIS   A 1 365 ? -2.614  15.873  -38.335 1.00 44.52  ?  367 HIS   A CA   1 
ATOM   2795 C  C    . HIS   A 1 365 ? -2.497  17.283  -37.710 1.00 49.63  ?  367 HIS   A C    1 
ATOM   2796 O  O    . HIS   A 1 365 ? -1.752  17.472  -36.737 1.00 49.38  ?  367 HIS   A O    1 
ATOM   2797 C  CB   . HIS   A 1 365 ? -1.831  15.771  -39.628 1.00 46.16  ?  367 HIS   A CB   1 
ATOM   2798 C  CG   . HIS   A 1 365 ? -0.366  15.896  -39.454 1.00 48.23  ?  367 HIS   A CG   1 
ATOM   2799 N  ND1  . HIS   A 1 365 ? 0.228   17.049  -38.990 1.00 53.84  ?  367 HIS   A ND1  1 
ATOM   2800 C  CD2  . HIS   A 1 365 ? 0.636   15.032  -39.726 1.00 51.35  ?  367 HIS   A CD2  1 
ATOM   2801 C  CE1  . HIS   A 1 365 ? 1.537   16.878  -38.954 1.00 58.43  ?  367 HIS   A CE1  1 
ATOM   2802 N  NE2  . HIS   A 1 365 ? 1.811   15.664  -39.401 1.00 58.95  ?  367 HIS   A NE2  1 
ATOM   2803 N  N    . GLU   A 1 366 ? -3.239  18.256  -38.240 1.00 50.87  ?  368 GLU   A N    1 
ATOM   2804 C  CA   . GLU   A 1 366 ? -3.220  19.621  -37.653 1.00 54.20  ?  368 GLU   A CA   1 
ATOM   2805 C  C    . GLU   A 1 366 ? -3.851  19.607  -36.268 1.00 51.76  ?  368 GLU   A C    1 
ATOM   2806 O  O    . GLU   A 1 366 ? -3.410  20.314  -35.360 1.00 51.15  ?  368 GLU   A O    1 
ATOM   2807 C  CB   . GLU   A 1 366 ? -3.998  20.653  -38.488 1.00 55.84  ?  368 GLU   A CB   1 
ATOM   2808 C  CG   . GLU   A 1 366 ? -3.697  20.661  -39.967 1.00 60.41  ?  368 GLU   A CG   1 
ATOM   2809 C  CD   . GLU   A 1 366 ? -2.234  20.879  -40.303 1.00 68.37  ?  368 GLU   A CD   1 
ATOM   2810 O  OE1  . GLU   A 1 366 ? -1.805  22.065  -40.314 1.00 70.92  ?  368 GLU   A OE1  1 
ATOM   2811 O  OE2  . GLU   A 1 366 ? -1.533  19.866  -40.584 1.00 71.11  ?  368 GLU   A OE2  1 
ATOM   2812 N  N    . CYS   A 1 367 ? -4.919  18.825  -36.156 1.00 46.53  ?  369 CYS   A N    1 
ATOM   2813 C  CA   . CYS   A 1 367 ? -5.717  18.710  -34.957 1.00 44.45  ?  369 CYS   A CA   1 
ATOM   2814 C  C    . CYS   A 1 367 ? -4.864  18.272  -33.744 1.00 41.02  ?  369 CYS   A C    1 
ATOM   2815 O  O    . CYS   A 1 367 ? -4.864  18.946  -32.714 1.00 41.68  ?  369 CYS   A O    1 
ATOM   2816 C  CB   . CYS   A 1 367 ? -6.879  17.742  -35.266 1.00 45.55  ?  369 CYS   A CB   1 
ATOM   2817 S  SG   . CYS   A 1 367 ? -8.139  17.493  -34.007 1.00 46.65  ?  369 CYS   A SG   1 
ATOM   2818 N  N    . TYR   A 1 368 ? -4.109  17.180  -33.871 1.00 40.36  ?  370 TYR   A N    1 
ATOM   2819 C  CA   . TYR   A 1 368 ? -3.338  16.622  -32.717 1.00 40.21  ?  370 TYR   A CA   1 
ATOM   2820 C  C    . TYR   A 1 368 ? -1.850  17.055  -32.656 1.00 40.37  ?  370 TYR   A C    1 
ATOM   2821 O  O    . TYR   A 1 368 ? -1.063  16.576  -31.789 1.00 35.48  ?  370 TYR   A O    1 
ATOM   2822 C  CB   . TYR   A 1 368 ? -3.488  15.073  -32.615 1.00 39.09  ?  370 TYR   A CB   1 
ATOM   2823 C  CG   . TYR   A 1 368 ? -2.966  14.271  -33.787 1.00 34.18  ?  370 TYR   A CG   1 
ATOM   2824 C  CD1  . TYR   A 1 368 ? -1.589  14.164  -34.036 1.00 34.94  ?  370 TYR   A CD1  1 
ATOM   2825 C  CD2  . TYR   A 1 368 ? -3.838  13.613  -34.639 1.00 30.82  ?  370 TYR   A CD2  1 
ATOM   2826 C  CE1  . TYR   A 1 368 ? -1.119  13.430  -35.105 1.00 34.15  ?  370 TYR   A CE1  1 
ATOM   2827 C  CE2  . TYR   A 1 368 ? -3.369  12.881  -35.703 1.00 29.78  ?  370 TYR   A CE2  1 
ATOM   2828 C  CZ   . TYR   A 1 368 ? -2.014  12.804  -35.935 1.00 30.70  ?  370 TYR   A CZ   1 
ATOM   2829 O  OH   . TYR   A 1 368 ? -1.532  12.082  -36.982 1.00 32.29  ?  370 TYR   A OH   1 
ATOM   2830 N  N    . ALA   A 1 369 ? -1.473  17.960  -33.564 1.00 36.86  ?  371 ALA   A N    1 
ATOM   2831 C  CA   . ALA   A 1 369 ? -0.106  18.464  -33.648 1.00 34.01  ?  371 ALA   A CA   1 
ATOM   2832 C  C    . ALA   A 1 369 ? 0.345   19.057  -32.320 1.00 30.49  ?  371 ALA   A C    1 
ATOM   2833 O  O    . ALA   A 1 369 ? 1.481   18.901  -31.959 1.00 29.47  ?  371 ALA   A O    1 
ATOM   2834 C  CB   . ALA   A 1 369 ? 0.007   19.509  -34.754 1.00 36.29  ?  371 ALA   A CB   1 
ATOM   2835 N  N    . LYS   A 1 370 ? -0.552  19.721  -31.598 1.00 31.31  ?  372 LYS   A N    1 
ATOM   2836 C  CA   . LYS   A 1 370 ? -0.206  20.302  -30.287 1.00 32.88  ?  372 LYS   A CA   1 
ATOM   2837 C  C    . LYS   A 1 370 ? -0.556  19.448  -29.052 1.00 30.87  ?  372 LYS   A C    1 
ATOM   2838 O  O    . LYS   A 1 370 ? -0.604  19.990  -27.950 1.00 31.90  ?  372 LYS   A O    1 
ATOM   2839 C  CB   . LYS   A 1 370 ? -0.784  21.721  -30.131 1.00 32.16  ?  372 LYS   A CB   1 
ATOM   2840 N  N    . VAL   A 1 371 ? -0.736  18.130  -29.207 1.00 28.55  ?  373 VAL   A N    1 
ATOM   2841 C  CA   . VAL   A 1 371 ? -1.028  17.281  -28.052 1.00 29.10  ?  373 VAL   A CA   1 
ATOM   2842 C  C    . VAL   A 1 371 ? 0.100   17.243  -27.000 1.00 29.23  ?  373 VAL   A C    1 
ATOM   2843 O  O    . VAL   A 1 371 ? -0.174  17.249  -25.821 1.00 31.81  ?  373 VAL   A O    1 
ATOM   2844 C  CB   . VAL   A 1 371 ? -1.442  15.842  -28.465 1.00 30.32  ?  373 VAL   A CB   1 
ATOM   2845 C  CG1  . VAL   A 1 371 ? -0.311  15.081  -29.160 1.00 30.54  ?  373 VAL   A CG1  1 
ATOM   2846 C  CG2  . VAL   A 1 371 ? -1.966  15.080  -27.262 1.00 30.71  ?  373 VAL   A CG2  1 
ATOM   2847 N  N    . PHE   A 1 372 ? 1.363   17.251  -27.413 1.00 29.76  ?  374 PHE   A N    1 
ATOM   2848 C  CA   . PHE   A 1 372 ? 2.443   17.230  -26.446 1.00 33.09  ?  374 PHE   A CA   1 
ATOM   2849 C  C    . PHE   A 1 372 ? 2.443   18.474  -25.528 1.00 34.01  ?  374 PHE   A C    1 
ATOM   2850 O  O    . PHE   A 1 372 ? 2.741   18.380  -24.329 1.00 30.94  ?  374 PHE   A O    1 
ATOM   2851 C  CB   . PHE   A 1 372 ? 3.784   16.939  -27.145 1.00 35.85  ?  374 PHE   A CB   1 
ATOM   2852 C  CG   . PHE   A 1 372 ? 3.997   15.466  -27.461 1.00 37.92  ?  374 PHE   A CG   1 
ATOM   2853 C  CD1  . PHE   A 1 372 ? 2.918   14.586  -27.644 1.00 39.41  ?  374 PHE   A CD1  1 
ATOM   2854 C  CD2  . PHE   A 1 372 ? 5.280   14.956  -27.559 1.00 40.09  ?  374 PHE   A CD2  1 
ATOM   2855 C  CE1  . PHE   A 1 372 ? 3.125   13.237  -27.904 1.00 39.90  ?  374 PHE   A CE1  1 
ATOM   2856 C  CE2  . PHE   A 1 372 ? 5.488   13.612  -27.831 1.00 42.54  ?  374 PHE   A CE2  1 
ATOM   2857 C  CZ   . PHE   A 1 372 ? 4.414   12.748  -27.992 1.00 40.61  ?  374 PHE   A CZ   1 
ATOM   2858 N  N    . ASP   A 1 373 ? 1.987   19.609  -26.050 1.00 34.52  ?  375 ASP   A N    1 
ATOM   2859 C  CA   . ASP   A 1 373 ? 1.767   20.808  -25.213 1.00 34.28  ?  375 ASP   A CA   1 
ATOM   2860 C  C    . ASP   A 1 373 ? 0.809   20.582  -24.064 1.00 31.53  ?  375 ASP   A C    1 
ATOM   2861 O  O    . ASP   A 1 373 ? 0.958   21.200  -23.020 1.00 26.10  ?  375 ASP   A O    1 
ATOM   2862 C  CB   . ASP   A 1 373 ? 1.212   21.979  -26.043 1.00 34.93  ?  375 ASP   A CB   1 
ATOM   2863 C  CG   . ASP   A 1 373 ? 2.137   22.397  -27.114 1.00 39.37  ?  375 ASP   A CG   1 
ATOM   2864 O  OD1  . ASP   A 1 373 ? 3.336   22.002  -27.046 1.00 37.26  ?  375 ASP   A OD1  1 
ATOM   2865 O  OD2  . ASP   A 1 373 ? 1.661   23.108  -28.038 1.00 49.75  ?  375 ASP   A OD2  1 
ATOM   2866 N  N    . GLU   A 1 374 ? -0.207  19.751  -24.301 1.00 30.30  ?  376 GLU   A N    1 
ATOM   2867 C  CA   . GLU   A 1 374 ? -1.205  19.437  -23.292 1.00 33.14  ?  376 GLU   A CA   1 
ATOM   2868 C  C    . GLU   A 1 374 ? -0.593  18.636  -22.138 1.00 30.02  ?  376 GLU   A C    1 
ATOM   2869 O  O    . GLU   A 1 374 ? -1.147  18.607  -21.037 1.00 30.00  ?  376 GLU   A O    1 
ATOM   2870 C  CB   . GLU   A 1 374 ? -2.357  18.625  -23.872 1.00 35.33  ?  376 GLU   A CB   1 
ATOM   2871 C  CG   . GLU   A 1 374 ? -3.101  19.262  -25.026 1.00 41.16  ?  376 GLU   A CG   1 
ATOM   2872 C  CD   . GLU   A 1 374 ? -4.269  18.392  -25.436 1.00 48.56  ?  376 GLU   A CD   1 
ATOM   2873 O  OE1  . GLU   A 1 374 ? -5.112  18.079  -24.554 1.00 47.61  ?  376 GLU   A OE1  1 
ATOM   2874 O  OE2  . GLU   A 1 374 ? -4.322  18.002  -26.627 1.00 55.49  ?  376 GLU   A OE2  1 
ATOM   2875 N  N    . PHE   A 1 375 ? 0.541   18.000  -22.391 1.00 27.34  ?  377 PHE   A N    1 
ATOM   2876 C  CA   . PHE   A 1 375 ? 1.238   17.267  -21.312 1.00 30.58  ?  377 PHE   A CA   1 
ATOM   2877 C  C    . PHE   A 1 375 ? 1.901   18.203  -20.279 1.00 29.77  ?  377 PHE   A C    1 
ATOM   2878 O  O    . PHE   A 1 375 ? 1.931   17.898  -19.109 1.00 27.83  ?  377 PHE   A O    1 
ATOM   2879 C  CB   . PHE   A 1 375 ? 2.232   16.252  -21.914 1.00 29.58  ?  377 PHE   A CB   1 
ATOM   2880 C  CG   . PHE   A 1 375 ? 1.600   15.259  -22.900 1.00 27.55  ?  377 PHE   A CG   1 
ATOM   2881 C  CD1  . PHE   A 1 375 ? 0.247   14.926  -22.853 1.00 28.20  ?  377 PHE   A CD1  1 
ATOM   2882 C  CD2  . PHE   A 1 375 ? 2.382   14.642  -23.846 1.00 28.53  ?  377 PHE   A CD2  1 
ATOM   2883 C  CE1  . PHE   A 1 375 ? -0.301  14.000  -23.734 1.00 26.99  ?  377 PHE   A CE1  1 
ATOM   2884 C  CE2  . PHE   A 1 375 ? 1.827   13.731  -24.731 1.00 29.73  ?  377 PHE   A CE2  1 
ATOM   2885 C  CZ   . PHE   A 1 375 ? 0.487   13.412  -24.667 1.00 26.91  ?  377 PHE   A CZ   1 
ATOM   2886 N  N    . LYS   A 1 376 ? 2.372   19.364  -20.732 1.00 31.34  ?  378 LYS   A N    1 
ATOM   2887 C  CA   . LYS   A 1 376 ? 3.035   20.359  -19.889 1.00 33.08  ?  378 LYS   A CA   1 
ATOM   2888 C  C    . LYS   A 1 376 ? 2.302   20.636  -18.570 1.00 31.31  ?  378 LYS   A C    1 
ATOM   2889 O  O    . LYS   A 1 376 ? 2.809   20.271  -17.517 1.00 30.74  ?  378 LYS   A O    1 
ATOM   2890 C  CB   . LYS   A 1 376 ? 3.281   21.641  -20.711 1.00 37.46  ?  378 LYS   A CB   1 
ATOM   2891 C  CG   . LYS   A 1 376 ? 3.870   22.812  -19.931 1.00 43.03  ?  378 LYS   A CG   1 
ATOM   2892 C  CD   . LYS   A 1 376 ? 5.382   22.932  -20.081 1.00 45.23  ?  378 LYS   A CD   1 
ATOM   2893 C  CE   . LYS   A 1 376 ? 5.777   24.397  -20.029 1.00 42.89  ?  378 LYS   A CE   1 
ATOM   2894 N  NZ   . LYS   A 1 376 ? 7.230   24.497  -19.810 1.00 43.29  ?  378 LYS   A NZ   1 
ATOM   2895 N  N    . PRO   A 1 377 ? 1.099   21.249  -18.608 1.00 30.47  ?  379 PRO   A N    1 
ATOM   2896 C  CA   . PRO   A 1 377 ? 0.429   21.465  -17.334 1.00 28.37  ?  379 PRO   A CA   1 
ATOM   2897 C  C    . PRO   A 1 377 ? 0.229   20.186  -16.503 1.00 26.85  ?  379 PRO   A C    1 
ATOM   2898 O  O    . PRO   A 1 377 ? 0.274   20.219  -15.263 1.00 22.99  ?  379 PRO   A O    1 
ATOM   2899 C  CB   . PRO   A 1 377 ? -0.937  22.026  -17.748 1.00 30.43  ?  379 PRO   A CB   1 
ATOM   2900 C  CG   . PRO   A 1 377 ? -1.111  21.661  -19.186 1.00 31.90  ?  379 PRO   A CG   1 
ATOM   2901 C  CD   . PRO   A 1 377 ? 0.267   21.713  -19.737 1.00 31.00  ?  379 PRO   A CD   1 
ATOM   2902 N  N    . LEU   A 1 378 ? -0.034  19.077  -17.181 1.00 25.66  ?  380 LEU   A N    1 
ATOM   2903 C  CA   . LEU   A 1 378 ? -0.232  17.810  -16.458 1.00 25.42  ?  380 LEU   A CA   1 
ATOM   2904 C  C    . LEU   A 1 378 ? 0.968   17.418  -15.666 1.00 21.40  ?  380 LEU   A C    1 
ATOM   2905 O  O    . LEU   A 1 378 ? 0.800   17.139  -14.526 1.00 25.17  ?  380 LEU   A O    1 
ATOM   2906 C  CB   . LEU   A 1 378 ? -0.661  16.692  -17.377 1.00 23.66  ?  380 LEU   A CB   1 
ATOM   2907 C  CG   . LEU   A 1 378 ? -2.153  16.458  -17.514 1.00 24.75  ?  380 LEU   A CG   1 
ATOM   2908 C  CD1  . LEU   A 1 378 ? -3.104  17.356  -16.746 1.00 26.02  ?  380 LEU   A CD1  1 
ATOM   2909 C  CD2  . LEU   A 1 378 ? -2.510  16.401  -18.985 1.00 26.04  ?  380 LEU   A CD2  1 
ATOM   2910 N  N    . VAL   A 1 379 ? 2.154   17.469  -16.249 1.00 20.70  ?  381 VAL   A N    1 
ATOM   2911 C  CA   . VAL   A 1 379 ? 3.412   17.195  -15.525 1.00 20.92  ?  381 VAL   A CA   1 
ATOM   2912 C  C    . VAL   A 1 379 ? 3.700   18.184  -14.415 1.00 21.33  ?  381 VAL   A C    1 
ATOM   2913 O  O    . VAL   A 1 379 ? 4.070   17.788  -13.315 1.00 18.95  ?  381 VAL   A O    1 
ATOM   2914 C  CB   . VAL   A 1 379 ? 4.623   17.166  -16.466 1.00 20.86  ?  381 VAL   A CB   1 
ATOM   2915 C  CG1  . VAL   A 1 379 ? 5.921   17.022  -15.695 1.00 22.16  ?  381 VAL   A CG1  1 
ATOM   2916 C  CG2  . VAL   A 1 379 ? 4.524   16.054  -17.493 1.00 22.39  ?  381 VAL   A CG2  1 
ATOM   2917 N  N    . GLU   A 1 380 ? 3.544   19.476  -14.680 1.00 22.92  ?  382 GLU   A N    1 
ATOM   2918 C  CA   . GLU   A 1 380 ? 3.905   20.504  -13.689 1.00 24.07  ?  382 GLU   A CA   1 
ATOM   2919 C  C    . GLU   A 1 380 ? 3.012   20.595  -12.460 1.00 25.14  ?  382 GLU   A C    1 
ATOM   2920 O  O    . GLU   A 1 380 ? 3.443   21.076  -11.447 1.00 25.76  ?  382 GLU   A O    1 
ATOM   2921 C  CB   . GLU   A 1 380 ? 3.990   21.879  -14.357 1.00 26.28  ?  382 GLU   A CB   1 
ATOM   2922 C  CG   . GLU   A 1 380 ? 5.056   21.873  -15.392 1.00 28.40  ?  382 GLU   A CG   1 
ATOM   2923 C  CD   . GLU   A 1 380 ? 5.251   23.174  -16.097 1.00 32.87  ?  382 GLU   A CD   1 
ATOM   2924 O  OE1  . GLU   A 1 380 ? 4.483   24.130  -15.889 1.00 33.14  ?  382 GLU   A OE1  1 
ATOM   2925 O  OE2  . GLU   A 1 380 ? 6.211   23.193  -16.908 1.00 39.51  ?  382 GLU   A OE2  1 
ATOM   2926 N  N    . GLU   A 1 381 ? 1.767   20.141  -12.536 1.00 26.59  ?  383 GLU   A N    1 
ATOM   2927 C  CA   . GLU   A 1 381 ? 0.896   20.233  -11.397 1.00 25.85  ?  383 GLU   A CA   1 
ATOM   2928 C  C    . GLU   A 1 381 ? 1.468   19.414  -10.210 1.00 24.23  ?  383 GLU   A C    1 
ATOM   2929 O  O    . GLU   A 1 381 ? 1.601   19.963  -9.100  1.00 19.55  ?  383 GLU   A O    1 
ATOM   2930 C  CB   . GLU   A 1 381 ? -0.573  19.868  -11.759 1.00 29.78  ?  383 GLU   A CB   1 
ATOM   2931 C  CG   . GLU   A 1 381 ? -1.390  19.015  -10.718 1.00 34.38  ?  383 GLU   A CG   1 
ATOM   2932 C  CD   . GLU   A 1 381 ? -1.462  19.651  -9.354  1.00 36.55  ?  383 GLU   A CD   1 
ATOM   2933 O  OE1  . GLU   A 1 381 ? -1.019  20.825  -9.259  1.00 40.31  ?  383 GLU   A OE1  1 
ATOM   2934 O  OE2  . GLU   A 1 381 ? -1.952  19.028  -8.379  1.00 29.73  ?  383 GLU   A OE2  1 
ATOM   2935 N  N    . PRO   A 1 382 ? 1.739   18.097  -10.422 1.00 21.86  ?  384 PRO   A N    1 
ATOM   2936 C  CA   . PRO   A 1 382 ? 2.331   17.334  -9.323  1.00 22.27  ?  384 PRO   A CA   1 
ATOM   2937 C  C    . PRO   A 1 382 ? 3.728   17.794  -8.960  1.00 22.16  ?  384 PRO   A C    1 
ATOM   2938 O  O    . PRO   A 1 382 ? 4.079   17.809  -7.776  1.00 20.91  ?  384 PRO   A O    1 
ATOM   2939 C  CB   . PRO   A 1 382 ? 2.374   15.865  -9.823  1.00 21.13  ?  384 PRO   A CB   1 
ATOM   2940 C  CG   . PRO   A 1 382 ? 1.979   15.888  -11.237 1.00 21.78  ?  384 PRO   A CG   1 
ATOM   2941 C  CD   . PRO   A 1 382 ? 1.389   17.249  -11.570 1.00 21.52  ?  384 PRO   A CD   1 
ATOM   2942 N  N    . GLN   A 1 383 ? 4.534   18.152  -9.944  1.00 24.43  ?  385 GLN   A N    1 
ATOM   2943 C  CA   . GLN   A 1 383 ? 5.905   18.576  -9.618  1.00 27.39  ?  385 GLN   A CA   1 
ATOM   2944 C  C    . GLN   A 1 383 ? 5.927   19.786  -8.668  1.00 26.12  ?  385 GLN   A C    1 
ATOM   2945 O  O    . GLN   A 1 383 ? 6.711   19.788  -7.725  1.00 27.93  ?  385 GLN   A O    1 
ATOM   2946 C  CB   . GLN   A 1 383 ? 6.727   18.849  -10.859 1.00 30.65  ?  385 GLN   A CB   1 
ATOM   2947 C  CG   . GLN   A 1 383 ? 6.992   17.587  -11.646 1.00 35.25  ?  385 GLN   A CG   1 
ATOM   2948 C  CD   . GLN   A 1 383 ? 7.736   17.831  -12.941 1.00 38.24  ?  385 GLN   A CD   1 
ATOM   2949 O  OE1  . GLN   A 1 383 ? 7.523   18.836  -13.629 1.00 41.10  ?  385 GLN   A OE1  1 
ATOM   2950 N  NE2  . GLN   A 1 383 ? 8.631   16.905  -13.276 1.00 40.79  ?  385 GLN   A NE2  1 
ATOM   2951 N  N    . ASN   A 1 384 ? 5.033   20.751  -8.864  1.00 24.67  ?  386 ASN   A N    1 
ATOM   2952 C  CA   . ASN   A 1 384 ? 4.999   21.953  -8.020  1.00 27.60  ?  386 ASN   A CA   1 
ATOM   2953 C  C    . ASN   A 1 384 ? 4.407   21.715  -6.628  1.00 27.30  ?  386 ASN   A C    1 
ATOM   2954 O  O    . ASN   A 1 384 ? 4.877   22.281  -5.663  1.00 23.78  ?  386 ASN   A O    1 
ATOM   2955 C  CB   . ASN   A 1 384 ? 4.166   23.058  -8.650  1.00 28.43  ?  386 ASN   A CB   1 
ATOM   2956 C  CG   . ASN   A 1 384 ? 4.752   23.576  -9.901  1.00 30.16  ?  386 ASN   A CG   1 
ATOM   2957 O  OD1  . ASN   A 1 384 ? 5.968   23.589  -10.053 1.00 34.41  ?  386 ASN   A OD1  1 
ATOM   2958 N  ND2  . ASN   A 1 384 ? 3.888   23.990  -10.838 1.00 30.89  ?  386 ASN   A ND2  1 
ATOM   2959 N  N    . LEU   A 1 385 ? 3.334   20.930  -6.552  1.00 26.88  ?  387 LEU   A N    1 
ATOM   2960 C  CA   . LEU   A 1 385 ? 2.787   20.517  -5.275  1.00 26.97  ?  387 LEU   A CA   1 
ATOM   2961 C  C    . LEU   A 1 385 ? 3.870   19.907  -4.442  1.00 23.29  ?  387 LEU   A C    1 
ATOM   2962 O  O    . LEU   A 1 385 ? 3.946   20.174  -3.250  1.00 24.86  ?  387 LEU   A O    1 
ATOM   2963 C  CB   . LEU   A 1 385 ? 1.714   19.444  -5.424  1.00 29.54  ?  387 LEU   A CB   1 
ATOM   2964 C  CG   . LEU   A 1 385 ? 0.309   19.810  -5.813  1.00 33.06  ?  387 LEU   A CG   1 
ATOM   2965 C  CD1  . LEU   A 1 385 ? -0.562  18.609  -5.450  1.00 31.60  ?  387 LEU   A CD1  1 
ATOM   2966 C  CD2  . LEU   A 1 385 ? -0.197  21.077  -5.129  1.00 32.89  ?  387 LEU   A CD2  1 
ATOM   2967 N  N    . ILE   A 1 386 ? 4.658   19.045  -5.059  1.00 22.87  ?  388 ILE   A N    1 
ATOM   2968 C  CA   . ILE   A 1 386 ? 5.770   18.404  -4.370  1.00 24.98  ?  388 ILE   A CA   1 
ATOM   2969 C  C    . ILE   A 1 386 ? 6.896   19.430  -4.040  1.00 24.29  ?  388 ILE   A C    1 
ATOM   2970 O  O    . ILE   A 1 386 ? 7.417   19.436  -2.901  1.00 25.04  ?  388 ILE   A O    1 
ATOM   2971 C  CB   . ILE   A 1 386 ? 6.310   17.158  -5.125  1.00 23.82  ?  388 ILE   A CB   1 
ATOM   2972 C  CG1  . ILE   A 1 386 ? 5.219   16.103  -5.201  1.00 24.22  ?  388 ILE   A CG1  1 
ATOM   2973 C  CG2  . ILE   A 1 386 ? 7.512   16.583  -4.369  1.00 24.86  ?  388 ILE   A CG2  1 
ATOM   2974 C  CD1  . ILE   A 1 386 ? 5.555   14.835  -5.943  1.00 24.64  ?  388 ILE   A CD1  1 
ATOM   2975 N  N    . LYS   A 1 387 ? 7.244   20.296  -4.987  1.00 24.51  ?  389 LYS   A N    1 
ATOM   2976 C  CA   . LYS   A 1 387 ? 8.140   21.451  -4.690  1.00 25.13  ?  389 LYS   A CA   1 
ATOM   2977 C  C    . LYS   A 1 387 ? 7.727   22.071  -3.376  1.00 25.34  ?  389 LYS   A C    1 
ATOM   2978 O  O    . LYS   A 1 387 ? 8.406   21.925  -2.379  1.00 24.19  ?  389 LYS   A O    1 
ATOM   2979 C  CB   . LYS   A 1 387 ? 8.073   22.548  -5.756  1.00 25.57  ?  389 LYS   A CB   1 
ATOM   2980 N  N    . GLN   A 1 388 ? 6.525   22.631  -3.399  1.00 28.86  ?  390 GLN   A N    1 
ATOM   2981 C  CA   . GLN   A 1 388 ? 5.957   23.512  -2.394  1.00 30.93  ?  390 GLN   A CA   1 
ATOM   2982 C  C    . GLN   A 1 388 ? 5.882   22.764  -1.047  1.00 30.00  ?  390 GLN   A C    1 
ATOM   2983 O  O    . GLN   A 1 388 ? 6.325   23.257  -0.026  1.00 27.27  ?  390 GLN   A O    1 
ATOM   2984 C  CB   . GLN   A 1 388 ? 4.548   23.981  -2.874  1.00 34.54  ?  390 GLN   A CB   1 
ATOM   2985 C  CG   . GLN   A 1 388 ? 4.086   25.391  -2.449  1.00 38.44  ?  390 GLN   A CG   1 
ATOM   2986 C  CD   . GLN   A 1 388 ? 4.047   26.448  -3.569  1.00 40.65  ?  390 GLN   A CD   1 
ATOM   2987 O  OE1  . GLN   A 1 388 ? 4.365   26.181  -4.735  1.00 43.89  ?  390 GLN   A OE1  1 
ATOM   2988 N  NE2  . GLN   A 1 388 ? 3.642   27.666  -3.205  1.00 43.11  ?  390 GLN   A NE2  1 
ATOM   2989 N  N    . ASN   A 1 389 ? 5.343   21.553  -1.058  1.00 29.50  ?  391 ASN   A N    1 
ATOM   2990 C  CA   . ASN   A 1 389 ? 5.156   20.827  0.190   1.00 27.98  ?  391 ASN   A CA   1 
ATOM   2991 C  C    . ASN   A 1 389 ? 6.486   20.395  0.865   1.00 28.77  ?  391 ASN   A C    1 
ATOM   2992 O  O    . ASN   A 1 389 ? 6.597   20.464  2.098   1.00 30.13  ?  391 ASN   A O    1 
ATOM   2993 C  CB   . ASN   A 1 389 ? 4.129   19.708  -0.015  1.00 27.92  ?  391 ASN   A CB   1 
ATOM   2994 C  CG   . ASN   A 1 389 ? 2.687   20.255  -0.026  1.00 27.00  ?  391 ASN   A CG   1 
ATOM   2995 O  OD1  . ASN   A 1 389 ? 2.269   20.849  0.936   1.00 28.86  ?  391 ASN   A OD1  1 
ATOM   2996 N  ND2  . ASN   A 1 389 ? 1.975   20.117  -1.129  1.00 28.77  ?  391 ASN   A ND2  1 
ATOM   2997 N  N    . CYS   A 1 390 ? 7.506   20.010  0.094   1.00 29.82  ?  392 CYS   A N    1 
ATOM   2998 C  CA   . CYS   A 1 390 ? 8.847   19.690  0.687   1.00 29.28  ?  392 CYS   A CA   1 
ATOM   2999 C  C    . CYS   A 1 390 ? 9.581   20.922  1.188   1.00 29.92  ?  392 CYS   A C    1 
ATOM   3000 O  O    . CYS   A 1 390 ? 10.184  20.877  2.264   1.00 28.23  ?  392 CYS   A O    1 
ATOM   3001 C  CB   . CYS   A 1 390 ? 9.731   18.953  -0.277  1.00 27.83  ?  392 CYS   A CB   1 
ATOM   3002 S  SG   . CYS   A 1 390 ? 9.088   17.312  -0.591  1.00 30.57  ?  392 CYS   A SG   1 
ATOM   3003 N  N    . GLU   A 1 391 ? 9.513   22.019  0.428   1.00 31.86  ?  393 GLU   A N    1 
ATOM   3004 C  CA   . GLU   A 1 391 ? 10.072  23.287  0.902   1.00 33.83  ?  393 GLU   A CA   1 
ATOM   3005 C  C    . GLU   A 1 391 ? 9.457   23.718  2.228   1.00 36.25  ?  393 GLU   A C    1 
ATOM   3006 O  O    . GLU   A 1 391 ? 10.195  24.056  3.176   1.00 38.54  ?  393 GLU   A O    1 
ATOM   3007 C  CB   . GLU   A 1 391 ? 9.926   24.381  -0.125  1.00 36.53  ?  393 GLU   A CB   1 
ATOM   3008 C  CG   . GLU   A 1 391 ? 11.013  24.309  -1.175  1.00 40.11  ?  393 GLU   A CG   1 
ATOM   3009 C  CD   . GLU   A 1 391 ? 10.739  25.218  -2.353  1.00 44.66  ?  393 GLU   A CD   1 
ATOM   3010 O  OE1  . GLU   A 1 391 ? 10.927  24.768  -3.502  1.00 44.84  ?  393 GLU   A OE1  1 
ATOM   3011 O  OE2  . GLU   A 1 391 ? 10.345  26.387  -2.121  1.00 55.86  ?  393 GLU   A OE2  1 
ATOM   3012 N  N    . LEU   A 1 392 ? 8.120   23.673  2.300   1.00 33.08  ?  394 LEU   A N    1 
ATOM   3013 C  CA   . LEU   A 1 392 ? 7.424   23.865  3.549   1.00 30.59  ?  394 LEU   A CA   1 
ATOM   3014 C  C    . LEU   A 1 392 ? 7.865   22.875  4.647   1.00 30.97  ?  394 LEU   A C    1 
ATOM   3015 O  O    . LEU   A 1 392 ? 8.105   23.274  5.815   1.00 30.97  ?  394 LEU   A O    1 
ATOM   3016 C  CB   . LEU   A 1 392 ? 5.905   23.765  3.344   1.00 30.49  ?  394 LEU   A CB   1 
ATOM   3017 C  CG   . LEU   A 1 392 ? 5.071   24.216  4.536   1.00 28.16  ?  394 LEU   A CG   1 
ATOM   3018 C  CD1  . LEU   A 1 392 ? 5.233   25.736  4.700   1.00 30.67  ?  394 LEU   A CD1  1 
ATOM   3019 C  CD2  . LEU   A 1 392 ? 3.608   23.840  4.327   1.00 29.33  ?  394 LEU   A CD2  1 
ATOM   3020 N  N    . PHE   A 1 393 ? 7.953   21.592  4.303   1.00 28.82  ?  395 PHE   A N    1 
ATOM   3021 C  CA   . PHE   A 1 393 ? 8.409   20.608  5.275   1.00 29.38  ?  395 PHE   A CA   1 
ATOM   3022 C  C    . PHE   A 1 393 ? 9.808   20.936  5.838   1.00 29.85  ?  395 PHE   A C    1 
ATOM   3023 O  O    . PHE   A 1 393 ? 10.059  20.728  7.011   1.00 26.93  ?  395 PHE   A O    1 
ATOM   3024 C  CB   . PHE   A 1 393 ? 8.389   19.187  4.713   1.00 29.52  ?  395 PHE   A CB   1 
ATOM   3025 C  CG   . PHE   A 1 393 ? 9.113   18.194  5.581   1.00 30.63  ?  395 PHE   A CG   1 
ATOM   3026 C  CD1  . PHE   A 1 393 ? 10.498  18.044  5.479   1.00 30.82  ?  395 PHE   A CD1  1 
ATOM   3027 C  CD2  . PHE   A 1 393 ? 8.426   17.459  6.530   1.00 31.38  ?  395 PHE   A CD2  1 
ATOM   3028 C  CE1  . PHE   A 1 393 ? 11.165  17.145  6.287   1.00 34.18  ?  395 PHE   A CE1  1 
ATOM   3029 C  CE2  . PHE   A 1 393 ? 9.088   16.546  7.334   1.00 33.33  ?  395 PHE   A CE2  1 
ATOM   3030 C  CZ   . PHE   A 1 393 ? 10.462  16.397  7.221   1.00 33.93  ?  395 PHE   A CZ   1 
ATOM   3031 N  N    . GLU   A 1 394 ? 10.700  21.427  4.998   1.00 34.37  ?  396 GLU   A N    1 
ATOM   3032 C  CA   . GLU   A 1 394 ? 12.071  21.738  5.436   1.00 38.35  ?  396 GLU   A CA   1 
ATOM   3033 C  C    . GLU   A 1 394 ? 12.098  22.919  6.441   1.00 41.08  ?  396 GLU   A C    1 
ATOM   3034 O  O    . GLU   A 1 394 ? 12.757  22.830  7.483   1.00 39.27  ?  396 GLU   A O    1 
ATOM   3035 C  CB   . GLU   A 1 394 ? 12.958  22.021  4.218   1.00 40.48  ?  396 GLU   A CB   1 
ATOM   3036 N  N    . GLN   A 1 395 ? 11.345  23.989  6.151   1.00 42.57  ?  397 GLN   A N    1 
ATOM   3037 C  CA   . GLN   A 1 395 ? 11.308  25.182  7.019   1.00 45.03  ?  397 GLN   A CA   1 
ATOM   3038 C  C    . GLN   A 1 395 ? 10.762  24.873  8.403   1.00 45.25  ?  397 GLN   A C    1 
ATOM   3039 O  O    . GLN   A 1 395 ? 11.427  25.129  9.404   1.00 47.58  ?  397 GLN   A O    1 
ATOM   3040 C  CB   . GLN   A 1 395 ? 10.460  26.290  6.413   1.00 46.06  ?  397 GLN   A CB   1 
ATOM   3041 C  CG   . GLN   A 1 395 ? 11.077  26.930  5.198   1.00 49.38  ?  397 GLN   A CG   1 
ATOM   3042 C  CD   . GLN   A 1 395 ? 10.076  27.756  4.397   1.00 52.95  ?  397 GLN   A CD   1 
ATOM   3043 O  OE1  . GLN   A 1 395 ? 9.005   28.127  4.898   1.00 58.72  ?  397 GLN   A OE1  1 
ATOM   3044 N  NE2  . GLN   A 1 395 ? 10.422  28.051  3.140   1.00 54.73  ?  397 GLN   A NE2  1 
ATOM   3045 N  N    . LEU   A 1 396 ? 9.554   24.309  8.434   1.00 43.10  ?  398 LEU   A N    1 
ATOM   3046 C  CA   . LEU   A 1 396 ? 8.844   24.001  9.667   1.00 40.80  ?  398 LEU   A CA   1 
ATOM   3047 C  C    . LEU   A 1 396 ? 8.658   22.509  9.654   1.00 42.59  ?  398 LEU   A C    1 
ATOM   3048 O  O    . LEU   A 1 396 ? 7.751   22.029  8.977   1.00 54.01  ?  398 LEU   A O    1 
ATOM   3049 C  CB   . LEU   A 1 396 ? 7.478   24.715  9.751   1.00 41.47  ?  398 LEU   A CB   1 
ATOM   3050 C  CG   . LEU   A 1 396 ? 6.658   25.057  8.496   1.00 40.66  ?  398 LEU   A CG   1 
ATOM   3051 C  CD1  . LEU   A 1 396 ? 5.189   24.702  8.605   1.00 41.13  ?  398 LEU   A CD1  1 
ATOM   3052 C  CD2  . LEU   A 1 396 ? 6.817   26.534  8.168   1.00 41.37  ?  398 LEU   A CD2  1 
ATOM   3053 N  N    . GLY   A 1 397 ? 9.500   21.792  10.397  1.00 38.23  ?  399 GLY   A N    1 
ATOM   3054 C  CA   . GLY   A 1 397 ? 9.687   20.329  10.250  1.00 35.01  ?  399 GLY   A CA   1 
ATOM   3055 C  C    . GLY   A 1 397 ? 8.474   19.404  10.383  1.00 32.63  ?  399 GLY   A C    1 
ATOM   3056 O  O    . GLY   A 1 397 ? 7.303   19.840  10.389  1.00 28.11  ?  399 GLY   A O    1 
ATOM   3057 N  N    . GLU   A 1 398 ? 8.741   18.109  10.526  1.00 29.32  ?  400 GLU   A N    1 
ATOM   3058 C  CA   . GLU   A 1 398 ? 7.667   17.126  10.428  1.00 32.54  ?  400 GLU   A CA   1 
ATOM   3059 C  C    . GLU   A 1 398 ? 6.441   17.497  11.300  1.00 33.08  ?  400 GLU   A C    1 
ATOM   3060 O  O    . GLU   A 1 398 ? 5.339   17.647  10.811  1.00 35.69  ?  400 GLU   A O    1 
ATOM   3061 C  CB   . GLU   A 1 398 ? 8.174   15.709  10.755  1.00 32.50  ?  400 GLU   A CB   1 
ATOM   3062 C  CG   . GLU   A 1 398 ? 7.138   14.650  10.428  1.00 34.34  ?  400 GLU   A CG   1 
ATOM   3063 C  CD   . GLU   A 1 398 ? 7.488   13.261  10.906  1.00 37.39  ?  400 GLU   A CD   1 
ATOM   3064 O  OE1  . GLU   A 1 398 ? 8.565   12.752  10.537  1.00 40.45  ?  400 GLU   A OE1  1 
ATOM   3065 O  OE2  . GLU   A 1 398 ? 6.655   12.666  11.619  1.00 39.48  ?  400 GLU   A OE2  1 
ATOM   3066 N  N    . TYR   A 1 399 ? 6.666   17.673  12.586  1.00 32.37  ?  401 TYR   A N    1 
ATOM   3067 C  CA   . TYR   A 1 399 ? 5.615   18.031  13.514  1.00 30.74  ?  401 TYR   A CA   1 
ATOM   3068 C  C    . TYR   A 1 399 ? 4.879   19.328  13.131  1.00 28.20  ?  401 TYR   A C    1 
ATOM   3069 O  O    . TYR   A 1 399 ? 3.656   19.374  13.163  1.00 27.57  ?  401 TYR   A O    1 
ATOM   3070 C  CB   . TYR   A 1 399 ? 6.198   18.150  14.937  1.00 29.98  ?  401 TYR   A CB   1 
ATOM   3071 C  CG   . TYR   A 1 399 ? 5.221   18.747  15.885  1.00 30.67  ?  401 TYR   A CG   1 
ATOM   3072 C  CD1  . TYR   A 1 399 ? 3.973   18.118  16.119  1.00 30.36  ?  401 TYR   A CD1  1 
ATOM   3073 C  CD2  . TYR   A 1 399 ? 5.496   19.962  16.543  1.00 32.27  ?  401 TYR   A CD2  1 
ATOM   3074 C  CE1  . TYR   A 1 399 ? 3.044   18.675  16.982  1.00 28.06  ?  401 TYR   A CE1  1 
ATOM   3075 C  CE2  . TYR   A 1 399 ? 4.577   20.511  17.432  1.00 29.60  ?  401 TYR   A CE2  1 
ATOM   3076 C  CZ   . TYR   A 1 399 ? 3.364   19.869  17.628  1.00 28.72  ?  401 TYR   A CZ   1 
ATOM   3077 O  OH   . TYR   A 1 399 ? 2.463   20.421  18.480  1.00 30.20  ?  401 TYR   A OH   1 
ATOM   3078 N  N    . LYS   A 1 400 ? 5.613   20.365  12.770  1.00 27.11  ?  402 LYS   A N    1 
ATOM   3079 C  CA   . LYS   A 1 400 ? 4.990   21.645  12.428  1.00 26.98  ?  402 LYS   A CA   1 
ATOM   3080 C  C    . LYS   A 1 400 ? 4.384   21.567  11.022  1.00 30.36  ?  402 LYS   A C    1 
ATOM   3081 O  O    . LYS   A 1 400 ? 3.331   22.183  10.736  1.00 27.94  ?  402 LYS   A O    1 
ATOM   3082 C  CB   . LYS   A 1 400 ? 5.998   22.780  12.527  1.00 26.10  ?  402 LYS   A CB   1 
ATOM   3083 C  CG   . LYS   A 1 400 ? 6.517   23.021  13.956  1.00 27.62  ?  402 LYS   A CG   1 
ATOM   3084 N  N    . PHE   A 1 401 ? 5.008   20.760  10.163  1.00 29.47  ?  403 PHE   A N    1 
ATOM   3085 C  CA   . PHE   A 1 401 ? 4.459   20.497  8.842   1.00 28.16  ?  403 PHE   A CA   1 
ATOM   3086 C  C    . PHE   A 1 401 ? 3.101   19.846  8.994   1.00 27.09  ?  403 PHE   A C    1 
ATOM   3087 O  O    . PHE   A 1 401 ? 2.197   20.168  8.249   1.00 25.25  ?  403 PHE   A O    1 
ATOM   3088 C  CB   . PHE   A 1 401 ? 5.401   19.589  8.028   1.00 26.94  ?  403 PHE   A CB   1 
ATOM   3089 C  CG   . PHE   A 1 401 ? 4.949   19.311  6.625   1.00 23.96  ?  403 PHE   A CG   1 
ATOM   3090 C  CD1  . PHE   A 1 401 ? 4.812   20.355  5.709   1.00 23.00  ?  403 PHE   A CD1  1 
ATOM   3091 C  CD2  . PHE   A 1 401 ? 4.729   17.990  6.197   1.00 24.57  ?  403 PHE   A CD2  1 
ATOM   3092 C  CE1  . PHE   A 1 401 ? 4.425   20.076  4.415   1.00 23.01  ?  403 PHE   A CE1  1 
ATOM   3093 C  CE2  . PHE   A 1 401 ? 4.353   17.711  4.893   1.00 21.58  ?  403 PHE   A CE2  1 
ATOM   3094 C  CZ   . PHE   A 1 401 ? 4.197   18.752  4.017   1.00 22.35  ?  403 PHE   A CZ   1 
ATOM   3095 N  N    . GLN   A 1 402 ? 2.971   18.929  9.960   1.00 27.74  ?  404 GLN   A N    1 
ATOM   3096 C  CA   . GLN   A 1 402 ? 1.697   18.269  10.195  1.00 26.48  ?  404 GLN   A CA   1 
ATOM   3097 C  C    . GLN   A 1 402 ? 0.619   19.295  10.559  1.00 28.21  ?  404 GLN   A C    1 
ATOM   3098 O  O    . GLN   A 1 402 ? -0.544  19.154  10.177  1.00 24.67  ?  404 GLN   A O    1 
ATOM   3099 C  CB   . GLN   A 1 402 ? 1.812   17.212  11.291  1.00 27.26  ?  404 GLN   A CB   1 
ATOM   3100 C  CG   . GLN   A 1 402 ? 2.649   15.978  10.901  1.00 27.25  ?  404 GLN   A CG   1 
ATOM   3101 C  CD   . GLN   A 1 402 ? 2.893   15.002  12.044  1.00 28.05  ?  404 GLN   A CD   1 
ATOM   3102 O  OE1  . GLN   A 1 402 ? 2.931   15.378  13.222  1.00 28.35  ?  404 GLN   A OE1  1 
ATOM   3103 N  NE2  . GLN   A 1 402 ? 3.059   13.727  11.689  1.00 27.77  ?  404 GLN   A NE2  1 
ATOM   3104 N  N    . ASN   A 1 403 ? 1.016   20.308  11.324  1.00 28.81  ?  405 ASN   A N    1 
ATOM   3105 C  CA   . ASN   A 1 403 ? 0.066   21.279  11.852  1.00 28.27  ?  405 ASN   A CA   1 
ATOM   3106 C  C    . ASN   A 1 403 ? -0.424  22.198  10.737  1.00 25.40  ?  405 ASN   A C    1 
ATOM   3107 O  O    . ASN   A 1 403 ? -1.629  22.516  10.676  1.00 24.78  ?  405 ASN   A O    1 
ATOM   3108 C  CB   . ASN   A 1 403 ? 0.644   22.045  13.053  1.00 27.04  ?  405 ASN   A CB   1 
ATOM   3109 C  CG   . ASN   A 1 403 ? 0.793   21.170  14.311  1.00 28.07  ?  405 ASN   A CG   1 
ATOM   3110 O  OD1  . ASN   A 1 403 ? 0.292   20.053  14.408  1.00 28.39  ?  405 ASN   A OD1  1 
ATOM   3111 N  ND2  . ASN   A 1 403 ? 1.512   21.684  15.265  1.00 28.24  ?  405 ASN   A ND2  1 
ATOM   3112 N  N    . ALA   A 1 404 ? 0.490   22.568  9.856   1.00 24.11  ?  406 ALA   A N    1 
ATOM   3113 C  CA   . ALA   A 1 404 ? 0.139   23.193  8.546   1.00 27.39  ?  406 ALA   A CA   1 
ATOM   3114 C  C    . ALA   A 1 404 ? -0.868  22.369  7.711   1.00 26.91  ?  406 ALA   A C    1 
ATOM   3115 O  O    . ALA   A 1 404 ? -1.913  22.914  7.266   1.00 28.69  ?  406 ALA   A O    1 
ATOM   3116 C  CB   . ALA   A 1 404 ? 1.381   23.429  7.735   1.00 27.97  ?  406 ALA   A CB   1 
ATOM   3117 N  N    . LEU   A 1 405 ? -0.594  21.069  7.532   1.00 23.46  ?  407 LEU   A N    1 
ATOM   3118 C  CA   . LEU   A 1 405 ? -1.514  20.223  6.762   1.00 24.56  ?  407 LEU   A CA   1 
ATOM   3119 C  C    . LEU   A 1 405 ? -2.860  20.210  7.433   1.00 22.96  ?  407 LEU   A C    1 
ATOM   3120 O  O    . LEU   A 1 405 ? -3.868  20.268  6.760   1.00 21.62  ?  407 LEU   A O    1 
ATOM   3121 C  CB   . LEU   A 1 405 ? -1.008  18.775  6.561   1.00 24.09  ?  407 LEU   A CB   1 
ATOM   3122 C  CG   . LEU   A 1 405 ? 0.352   18.631  5.851   1.00 24.94  ?  407 LEU   A CG   1 
ATOM   3123 C  CD1  . LEU   A 1 405 ? 0.661   17.180  5.609   1.00 23.56  ?  407 LEU   A CD1  1 
ATOM   3124 C  CD2  . LEU   A 1 405 ? 0.414   19.350  4.510   1.00 26.44  ?  407 LEU   A CD2  1 
ATOM   3125 N  N    . LEU   A 1 406 ? -2.842  20.195  8.768   1.00 25.57  ?  408 LEU   A N    1 
ATOM   3126 C  CA   . LEU   A 1 406 ? -4.024  20.006  9.623   1.00 25.86  ?  408 LEU   A CA   1 
ATOM   3127 C  C    . LEU   A 1 406 ? -4.987  21.210  9.543   1.00 25.69  ?  408 LEU   A C    1 
ATOM   3128 O  O    . LEU   A 1 406 ? -6.230  21.034  9.479   1.00 22.26  ?  408 LEU   A O    1 
ATOM   3129 C  CB   . LEU   A 1 406 ? -3.565  19.789  11.056  1.00 27.68  ?  408 LEU   A CB   1 
ATOM   3130 C  CG   . LEU   A 1 406 ? -4.283  18.933  12.079  1.00 29.39  ?  408 LEU   A CG   1 
ATOM   3131 C  CD1  . LEU   A 1 406 ? -4.648  17.518  11.650  1.00 29.66  ?  408 LEU   A CD1  1 
ATOM   3132 C  CD2  . LEU   A 1 406 ? -3.381  18.873  13.300  1.00 30.12  ?  408 LEU   A CD2  1 
ATOM   3133 N  N    . VAL   A 1 407 ? -4.423  22.415  9.503   1.00 24.56  ?  409 VAL   A N    1 
ATOM   3134 C  CA   . VAL   A 1 407 ? -5.222  23.616  9.291   1.00 25.28  ?  409 VAL   A CA   1 
ATOM   3135 C  C    . VAL   A 1 407 ? -5.783  23.628  7.866   1.00 25.65  ?  409 VAL   A C    1 
ATOM   3136 O  O    . VAL   A 1 407 ? -6.982  23.830  7.673   1.00 28.85  ?  409 VAL   A O    1 
ATOM   3137 C  CB   . VAL   A 1 407 ? -4.384  24.901  9.557   1.00 26.49  ?  409 VAL   A CB   1 
ATOM   3138 C  CG1  . VAL   A 1 407 ? -5.155  26.153  9.150   1.00 26.65  ?  409 VAL   A CG1  1 
ATOM   3139 C  CG2  . VAL   A 1 407 ? -3.951  24.999  11.028  1.00 25.95  ?  409 VAL   A CG2  1 
ATOM   3140 N  N    . ARG   A 1 408 ? -4.930  23.410  6.867   1.00 25.81  ?  410 ARG   A N    1 
ATOM   3141 C  CA   . ARG   A 1 408 ? -5.361  23.362  5.452   1.00 25.70  ?  410 ARG   A CA   1 
ATOM   3142 C  C    . ARG   A 1 408 ? -6.610  22.487  5.229   1.00 24.06  ?  410 ARG   A C    1 
ATOM   3143 O  O    . ARG   A 1 408 ? -7.648  22.967  4.801   1.00 23.84  ?  410 ARG   A O    1 
ATOM   3144 C  CB   . ARG   A 1 408 ? -4.206  22.856  4.594   1.00 28.60  ?  410 ARG   A CB   1 
ATOM   3145 C  CG   . ARG   A 1 408 ? -4.401  22.999  3.103   1.00 30.21  ?  410 ARG   A CG   1 
ATOM   3146 C  CD   . ARG   A 1 408 ? -3.073  23.290  2.438   1.00 37.16  ?  410 ARG   A CD   1 
ATOM   3147 N  NE   . ARG   A 1 408 ? -2.198  22.112  2.327   1.00 38.81  ?  410 ARG   A NE   1 
ATOM   3148 C  CZ   . ARG   A 1 408 ? -0.852  22.132  2.350   1.00 39.31  ?  410 ARG   A CZ   1 
ATOM   3149 N  NH1  . ARG   A 1 408 ? -0.141  23.255  2.522   1.00 39.47  ?  410 ARG   A NH1  1 
ATOM   3150 N  NH2  . ARG   A 1 408 ? -0.197  20.993  2.215   1.00 39.14  ?  410 ARG   A NH2  1 
ATOM   3151 N  N    . TYR   A 1 409 ? -6.507  21.215  5.609   1.00 23.51  ?  411 TYR   A N    1 
ATOM   3152 C  CA   . TYR   A 1 409 ? -7.538  20.202  5.390   1.00 23.18  ?  411 TYR   A CA   1 
ATOM   3153 C  C    . TYR   A 1 409 ? -8.761  20.385  6.217   1.00 22.10  ?  411 TYR   A C    1 
ATOM   3154 O  O    . TYR   A 1 409 ? -9.852  20.246  5.692   1.00 23.50  ?  411 TYR   A O    1 
ATOM   3155 C  CB   . TYR   A 1 409 ? -6.951  18.769  5.553   1.00 25.87  ?  411 TYR   A CB   1 
ATOM   3156 C  CG   . TYR   A 1 409 ? -5.766  18.515  4.618   1.00 28.45  ?  411 TYR   A CG   1 
ATOM   3157 C  CD1  . TYR   A 1 409 ? -5.813  18.915  3.268   1.00 30.30  ?  411 TYR   A CD1  1 
ATOM   3158 C  CD2  . TYR   A 1 409 ? -4.611  17.888  5.063   1.00 29.59  ?  411 TYR   A CD2  1 
ATOM   3159 C  CE1  . TYR   A 1 409 ? -4.753  18.698  2.420   1.00 32.14  ?  411 TYR   A CE1  1 
ATOM   3160 C  CE2  . TYR   A 1 409 ? -3.546  17.665  4.209   1.00 31.31  ?  411 TYR   A CE2  1 
ATOM   3161 C  CZ   . TYR   A 1 409 ? -3.613  18.072  2.881   1.00 32.11  ?  411 TYR   A CZ   1 
ATOM   3162 O  OH   . TYR   A 1 409 ? -2.552  17.850  1.986   1.00 32.03  ?  411 TYR   A OH   1 
ATOM   3163 N  N    . THR   A 1 410 ? -8.603  20.748  7.486   1.00 23.42  ?  412 THR   A N    1 
ATOM   3164 C  CA   . THR   A 1 410 ? -9.733  21.092  8.353   1.00 24.93  ?  412 THR   A CA   1 
ATOM   3165 C  C    . THR   A 1 410 ? -10.647 22.198  7.791   1.00 26.10  ?  412 THR   A C    1 
ATOM   3166 O  O    . THR   A 1 410 ? -11.868 22.057  7.791   1.00 28.07  ?  412 THR   A O    1 
ATOM   3167 C  CB   . THR   A 1 410 ? -9.241  21.512  9.744   1.00 26.15  ?  412 THR   A CB   1 
ATOM   3168 O  OG1  . THR   A 1 410 ? -8.392  20.481  10.273  1.00 25.59  ?  412 THR   A OG1  1 
ATOM   3169 C  CG2  . THR   A 1 410 ? -10.421 21.704  10.689  1.00 26.76  ?  412 THR   A CG2  1 
ATOM   3170 N  N    . LYS   A 1 411 ? -10.067 23.291  7.330   1.00 23.20  ?  413 LYS   A N    1 
ATOM   3171 C  CA   . LYS   A 1 411 ? -10.843 24.281  6.585   1.00 26.16  ?  413 LYS   A CA   1 
ATOM   3172 C  C    . LYS   A 1 411 ? -11.487 23.784  5.234   1.00 26.98  ?  413 LYS   A C    1 
ATOM   3173 O  O    . LYS   A 1 411 ? -12.587 24.222  4.881   1.00 27.11  ?  413 LYS   A O    1 
ATOM   3174 C  CB   . LYS   A 1 411 ? -9.997  25.521  6.325   1.00 25.97  ?  413 LYS   A CB   1 
ATOM   3175 C  CG   . LYS   A 1 411 ? -9.755  26.349  7.567   1.00 24.63  ?  413 LYS   A CG   1 
ATOM   3176 C  CD   . LYS   A 1 411 ? -8.850  27.524  7.240   1.00 25.38  ?  413 LYS   A CD   1 
ATOM   3177 C  CE   . LYS   A 1 411 ? -8.310  28.185  8.488   1.00 24.25  ?  413 LYS   A CE   1 
ATOM   3178 N  NZ   . LYS   A 1 411 ? -7.877  29.578  8.156   1.00 25.17  ?  413 LYS   A NZ   1 
ATOM   3179 N  N    . LYS   A 1 412 ? -10.836 22.883  4.494   1.00 28.38  ?  414 LYS   A N    1 
ATOM   3180 C  CA   . LYS   A 1 412 ? -11.452 22.382  3.241   1.00 28.62  ?  414 LYS   A CA   1 
ATOM   3181 C  C    . LYS   A 1 412 ? -12.607 21.429  3.505   1.00 29.93  ?  414 LYS   A C    1 
ATOM   3182 O  O    . LYS   A 1 412 ? -13.617 21.475  2.790   1.00 32.08  ?  414 LYS   A O    1 
ATOM   3183 C  CB   . LYS   A 1 412 ? -10.451 21.701  2.324   1.00 28.17  ?  414 LYS   A CB   1 
ATOM   3184 C  CG   . LYS   A 1 412 ? -9.307  22.567  1.871   1.00 30.45  ?  414 LYS   A CG   1 
ATOM   3185 C  CD   . LYS   A 1 412 ? -8.182  21.731  1.277   1.00 31.78  ?  414 LYS   A CD   1 
ATOM   3186 C  CE   . LYS   A 1 412 ? -7.046  22.605  0.778   1.00 33.91  ?  414 LYS   A CE   1 
ATOM   3187 N  NZ   . LYS   A 1 412 ? -7.404  23.300  -0.488  1.00 35.69  ?  414 LYS   A NZ   1 
ATOM   3188 N  N    . VAL   A 1 413 ? -12.469 20.576  4.527   1.00 29.97  ?  415 VAL   A N    1 
ATOM   3189 C  CA   . VAL   A 1 413 ? -13.495 19.609  4.844   1.00 30.28  ?  415 VAL   A CA   1 
ATOM   3190 C  C    . VAL   A 1 413 ? -13.703 19.532  6.347   1.00 28.80  ?  415 VAL   A C    1 
ATOM   3191 O  O    . VAL   A 1 413 ? -13.421 18.474  6.957   1.00 27.79  ?  415 VAL   A O    1 
ATOM   3192 C  CB   . VAL   A 1 413 ? -13.150 18.205  4.311   1.00 32.75  ?  415 VAL   A CB   1 
ATOM   3193 C  CG1  . VAL   A 1 413 ? -14.408 17.363  4.276   1.00 34.83  ?  415 VAL   A CG1  1 
ATOM   3194 C  CG2  . VAL   A 1 413 ? -12.518 18.274  2.930   1.00 34.83  ?  415 VAL   A CG2  1 
ATOM   3195 N  N    . PRO   A 1 414 ? -14.273 20.611  6.946   1.00 30.89  ?  416 PRO   A N    1 
ATOM   3196 C  CA   . PRO   A 1 414 ? -14.469 20.639  8.396   1.00 29.44  ?  416 PRO   A CA   1 
ATOM   3197 C  C    . PRO   A 1 414 ? -15.430 19.589  8.872   1.00 28.07  ?  416 PRO   A C    1 
ATOM   3198 O  O    . PRO   A 1 414 ? -15.450 19.302  10.039  1.00 28.68  ?  416 PRO   A O    1 
ATOM   3199 C  CB   . PRO   A 1 414 ? -15.062 22.024  8.663   1.00 29.28  ?  416 PRO   A CB   1 
ATOM   3200 C  CG   . PRO   A 1 414 ? -14.952 22.790  7.416   1.00 30.39  ?  416 PRO   A CG   1 
ATOM   3201 C  CD   . PRO   A 1 414 ? -14.933 21.775  6.317   1.00 30.51  ?  416 PRO   A CD   1 
ATOM   3202 N  N    . GLN   A 1 415 ? -16.190 18.979  7.980   1.00 28.84  ?  417 GLN   A N    1 
ATOM   3203 C  CA   . GLN   A 1 415 ? -17.167 17.986  8.414   1.00 31.25  ?  417 GLN   A CA   1 
ATOM   3204 C  C    . GLN   A 1 415 ? -16.546 16.641  8.869   1.00 30.02  ?  417 GLN   A C    1 
ATOM   3205 O  O    . GLN   A 1 415 ? -17.235 15.804  9.483   1.00 30.00  ?  417 GLN   A O    1 
ATOM   3206 C  CB   . GLN   A 1 415 ? -18.203 17.757  7.301   1.00 32.20  ?  417 GLN   A CB   1 
ATOM   3207 C  CG   . GLN   A 1 415 ? -19.046 18.983  7.012   1.00 32.17  ?  417 GLN   A CG   1 
ATOM   3208 C  CD   . GLN   A 1 415 ? -18.474 19.884  5.945   1.00 35.13  ?  417 GLN   A CD   1 
ATOM   3209 O  OE1  . GLN   A 1 415 ? -17.419 19.601  5.361   1.00 32.66  ?  417 GLN   A OE1  1 
ATOM   3210 N  NE2  . GLN   A 1 415 ? -19.192 20.980  5.663   1.00 35.29  ?  417 GLN   A NE2  1 
ATOM   3211 N  N    . VAL   A 1 416 ? -15.268 16.438  8.560   1.00 28.66  ?  418 VAL   A N    1 
ATOM   3212 C  CA   . VAL   A 1 416 ? -14.578 15.179  8.844   1.00 29.32  ?  418 VAL   A CA   1 
ATOM   3213 C  C    . VAL   A 1 416 ? -14.198 15.135  10.321  1.00 30.01  ?  418 VAL   A C    1 
ATOM   3214 O  O    . VAL   A 1 416 ? -13.771 16.143  10.899  1.00 24.89  ?  418 VAL   A O    1 
ATOM   3215 C  CB   . VAL   A 1 416 ? -13.315 15.028  7.960   1.00 28.22  ?  418 VAL   A CB   1 
ATOM   3216 C  CG1  . VAL   A 1 416 ? -12.484 13.823  8.372   1.00 30.04  ?  418 VAL   A CG1  1 
ATOM   3217 C  CG2  . VAL   A 1 416 ? -13.706 14.904  6.517   1.00 28.03  ?  418 VAL   A CG2  1 
ATOM   3218 N  N    . SER   A 1 417 ? -14.370 13.952  10.911  1.00 28.99  ?  419 SER   A N    1 
ATOM   3219 C  CA   . SER   A 1 417 ? -14.019 13.673  12.299  1.00 30.99  ?  419 SER   A CA   1 
ATOM   3220 C  C    . SER   A 1 417 ? -12.633 14.174  12.670  1.00 29.82  ?  419 SER   A C    1 
ATOM   3221 O  O    . SER   A 1 417 ? -11.712 14.143  11.857  1.00 30.77  ?  419 SER   A O    1 
ATOM   3222 C  CB   . SER   A 1 417 ? -14.094 12.144  12.538  1.00 32.53  ?  419 SER   A CB   1 
ATOM   3223 O  OG   . SER   A 1 417 ? -13.234 11.754  13.582  1.00 35.89  ?  419 SER   A OG   1 
ATOM   3224 N  N    . THR   A 1 418 ? -12.474 14.601  13.910  1.00 32.51  ?  420 THR   A N    1 
ATOM   3225 C  CA   . THR   A 1 418 ? -11.183 15.102  14.349  1.00 33.53  ?  420 THR   A CA   1 
ATOM   3226 C  C    . THR   A 1 418 ? -10.067 14.043  14.334  1.00 33.23  ?  420 THR   A C    1 
ATOM   3227 O  O    . THR   A 1 418 ? -9.003  14.301  13.751  1.00 30.13  ?  420 THR   A O    1 
ATOM   3228 C  CB   . THR   A 1 418 ? -11.268 15.833  15.680  1.00 32.63  ?  420 THR   A CB   1 
ATOM   3229 O  OG1  . THR   A 1 418 ? -12.128 16.952  15.511  1.00 36.12  ?  420 THR   A OG1  1 
ATOM   3230 C  CG2  . THR   A 1 418 ? -9.908  16.352  16.088  1.00 32.69  ?  420 THR   A CG2  1 
ATOM   3231 N  N    . PRO   A 1 419 ? -10.295 12.860  14.961  1.00 36.98  ?  421 PRO   A N    1 
ATOM   3232 C  CA   . PRO   A 1 419 ? -9.314  11.769  14.803  1.00 34.35  ?  421 PRO   A CA   1 
ATOM   3233 C  C    . PRO   A 1 419 ? -8.915  11.507  13.344  1.00 34.61  ?  421 PRO   A C    1 
ATOM   3234 O  O    . PRO   A 1 419 ? -7.733  11.335  13.073  1.00 31.99  ?  421 PRO   A O    1 
ATOM   3235 C  CB   . PRO   A 1 419 ? -10.015 10.557  15.426  1.00 33.90  ?  421 PRO   A CB   1 
ATOM   3236 C  CG   . PRO   A 1 419 ? -10.920 11.148  16.465  1.00 36.84  ?  421 PRO   A CG   1 
ATOM   3237 C  CD   . PRO   A 1 419 ? -11.192 12.603  16.103  1.00 37.99  ?  421 PRO   A CD   1 
ATOM   3238 N  N    . THR   A 1 420 ? -9.871  11.531  12.410  1.00 33.58  ?  422 THR   A N    1 
ATOM   3239 C  CA   . THR   A 1 420 ? -9.515  11.277  11.034  1.00 34.64  ?  422 THR   A CA   1 
ATOM   3240 C  C    . THR   A 1 420 ? -8.597  12.365  10.517  1.00 33.28  ?  422 THR   A C    1 
ATOM   3241 O  O    . THR   A 1 420 ? -7.611  12.045  9.867   1.00 26.17  ?  422 THR   A O    1 
ATOM   3242 C  CB   . THR   A 1 420 ? -10.723 11.095  10.080  1.00 38.06  ?  422 THR   A CB   1 
ATOM   3243 O  OG1  . THR   A 1 420 ? -11.524 9.990   10.508  1.00 39.37  ?  422 THR   A OG1  1 
ATOM   3244 C  CG2  . THR   A 1 420 ? -10.232 10.789  8.667   1.00 36.31  ?  422 THR   A CG2  1 
ATOM   3245 N  N    . LEU   A 1 421 ? -8.918  13.637  10.797  1.00 31.95  ?  423 LEU   A N    1 
ATOM   3246 C  CA   . LEU   A 1 421 ? -8.085  14.729  10.286  1.00 30.91  ?  423 LEU   A CA   1 
ATOM   3247 C  C    . LEU   A 1 421 ? -6.692  14.647  10.848  1.00 32.45  ?  423 LEU   A C    1 
ATOM   3248 O  O    . LEU   A 1 421 ? -5.735  14.778  10.086  1.00 37.74  ?  423 LEU   A O    1 
ATOM   3249 C  CB   . LEU   A 1 421 ? -8.659  16.108  10.596  1.00 31.26  ?  423 LEU   A CB   1 
ATOM   3250 C  CG   . LEU   A 1 421 ? -9.856  16.427  9.712   1.00 29.61  ?  423 LEU   A CG   1 
ATOM   3251 C  CD1  . LEU   A 1 421 ? -10.776 17.443  10.369  1.00 28.64  ?  423 LEU   A CD1  1 
ATOM   3252 C  CD2  . LEU   A 1 421 ? -9.348  16.881  8.357   1.00 29.56  ?  423 LEU   A CD2  1 
ATOM   3253 N  N    . VAL   A 1 422 ? -6.584  14.445  12.165  1.00 32.78  ?  424 VAL   A N    1 
ATOM   3254 C  CA   . VAL   A 1 422 ? -5.282  14.233  12.845  1.00 31.62  ?  424 VAL   A CA   1 
ATOM   3255 C  C    . VAL   A 1 422 ? -4.476  13.089  12.211  1.00 29.55  ?  424 VAL   A C    1 
ATOM   3256 O  O    . VAL   A 1 422 ? -3.349  13.287  11.810  1.00 30.92  ?  424 VAL   A O    1 
ATOM   3257 C  CB   . VAL   A 1 422 ? -5.472  13.975  14.375  1.00 32.98  ?  424 VAL   A CB   1 
ATOM   3258 C  CG1  . VAL   A 1 422 ? -4.205  13.435  15.035  1.00 32.81  ?  424 VAL   A CG1  1 
ATOM   3259 C  CG2  . VAL   A 1 422 ? -5.896  15.250  15.078  1.00 33.02  ?  424 VAL   A CG2  1 
ATOM   3260 N  N    . GLU   A 1 423 ? -5.054  11.901  12.126  1.00 29.92  ?  425 GLU   A N    1 
ATOM   3261 C  CA   . GLU   A 1 423 ? -4.340  10.737  11.615  1.00 29.63  ?  425 GLU   A CA   1 
ATOM   3262 C  C    . GLU   A 1 423 ? -3.893  10.918  10.174  1.00 31.69  ?  425 GLU   A C    1 
ATOM   3263 O  O    . GLU   A 1 423 ? -2.735  10.651  9.846   1.00 34.05  ?  425 GLU   A O    1 
ATOM   3264 C  CB   . GLU   A 1 423 ? -5.172  9.462   11.733  1.00 30.66  ?  425 GLU   A CB   1 
ATOM   3265 C  CG   . GLU   A 1 423 ? -4.327  8.196   11.783  1.00 31.82  ?  425 GLU   A CG   1 
ATOM   3266 N  N    . VAL   A 1 424 ? -4.749  11.420  9.303   1.00 30.59  ?  426 VAL   A N    1 
ATOM   3267 C  CA   . VAL   A 1 424 ? -4.311  11.542  7.898   1.00 32.11  ?  426 VAL   A CA   1 
ATOM   3268 C  C    . VAL   A 1 424 ? -3.299  12.676  7.724   1.00 30.30  ?  426 VAL   A C    1 
ATOM   3269 O  O    . VAL   A 1 424 ? -2.387  12.575  6.900   1.00 28.88  ?  426 VAL   A O    1 
ATOM   3270 C  CB   . VAL   A 1 424 ? -5.478  11.641  6.899   1.00 34.32  ?  426 VAL   A CB   1 
ATOM   3271 C  CG1  . VAL   A 1 424 ? -6.487  10.499  7.154   1.00 32.41  ?  426 VAL   A CG1  1 
ATOM   3272 C  CG2  . VAL   A 1 424 ? -6.100  13.025  6.933   1.00 36.14  ?  426 VAL   A CG2  1 
ATOM   3273 N  N    . SER   A 1 425 ? -3.422  13.734  8.522   1.00 29.05  ?  427 SER   A N    1 
ATOM   3274 C  CA   . SER   A 1 425 ? -2.404  14.768  8.496   1.00 28.39  ?  427 SER   A CA   1 
ATOM   3275 C  C    . SER   A 1 425 ? -1.125  14.256  9.150   1.00 30.28  ?  427 SER   A C    1 
ATOM   3276 O  O    . SER   A 1 425 ? -0.024  14.548  8.691   1.00 28.33  ?  427 SER   A O    1 
ATOM   3277 C  CB   . SER   A 1 425 ? -2.888  15.995  9.193   1.00 30.20  ?  427 SER   A CB   1 
ATOM   3278 O  OG   . SER   A 1 425 ? -3.985  16.543  8.492   1.00 30.94  ?  427 SER   A OG   1 
ATOM   3279 N  N    . ARG   A 1 426 ? -1.234  13.486  10.229  1.00 33.14  ?  428 ARG   A N    1 
ATOM   3280 C  CA   . ARG   A 1 426 ? -0.033  12.818  10.720  1.00 32.28  ?  428 ARG   A CA   1 
ATOM   3281 C  C    . ARG   A 1 426 ? 0.611   11.994  9.570   1.00 28.14  ?  428 ARG   A C    1 
ATOM   3282 O  O    . ARG   A 1 426 ? 1.755   12.258  9.193   1.00 27.76  ?  428 ARG   A O    1 
ATOM   3283 C  CB   . ARG   A 1 426 ? -0.325  11.954  11.930  1.00 31.95  ?  428 ARG   A CB   1 
ATOM   3284 C  CG   . ARG   A 1 426 ? -0.290  12.716  13.249  1.00 34.49  ?  428 ARG   A CG   1 
ATOM   3285 C  CD   . ARG   A 1 426 ? 0.247   11.833  14.387  1.00 34.96  ?  428 ARG   A CD   1 
ATOM   3286 N  NE   . ARG   A 1 426 ? 1.234   12.546  15.198  1.00 35.66  ?  428 ARG   A NE   1 
ATOM   3287 C  CZ   . ARG   A 1 426 ? 2.283   11.995  15.806  1.00 41.40  ?  428 ARG   A CZ   1 
ATOM   3288 N  NH1  . ARG   A 1 426 ? 2.544   10.691  15.729  1.00 44.15  ?  428 ARG   A NH1  1 
ATOM   3289 N  NH2  . ARG   A 1 426 ? 3.096   12.772  16.508  1.00 45.32  ?  428 ARG   A NH2  1 
ATOM   3290 N  N    . ASN   A 1 427 ? -0.141  11.059  8.998   1.00 26.06  ?  429 ASN   A N    1 
ATOM   3291 C  CA   . ASN   A 1 427 ? 0.344   10.215  7.867   1.00 29.34  ?  429 ASN   A CA   1 
ATOM   3292 C  C    . ASN   A 1 427 ? 0.918   10.994  6.664   1.00 29.68  ?  429 ASN   A C    1 
ATOM   3293 O  O    . ASN   A 1 427 ? 2.013   10.683  6.182   1.00 28.80  ?  429 ASN   A O    1 
ATOM   3294 C  CB   . ASN   A 1 427 ? -0.742  9.256   7.327   1.00 29.48  ?  429 ASN   A CB   1 
ATOM   3295 C  CG   . ASN   A 1 427 ? -1.243  8.262   8.367   1.00 31.89  ?  429 ASN   A CG   1 
ATOM   3296 O  OD1  . ASN   A 1 427 ? -0.575  7.990   9.355   1.00 32.41  ?  429 ASN   A OD1  1 
ATOM   3297 N  ND2  . ASN   A 1 427 ? -2.459  7.741   8.156   1.00 35.25  ?  429 ASN   A ND2  1 
ATOM   3298 N  N    . LEU   A 1 428 ? 0.185   11.979  6.167   1.00 28.22  ?  430 LEU   A N    1 
ATOM   3299 C  CA   . LEU   A 1 428 ? 0.727   12.832  5.097   1.00 31.97  ?  430 LEU   A CA   1 
ATOM   3300 C  C    . LEU   A 1 428 ? 2.110   13.429  5.454   1.00 31.63  ?  430 LEU   A C    1 
ATOM   3301 O  O    . LEU   A 1 428 ? 3.055   13.428  4.636   1.00 29.31  ?  430 LEU   A O    1 
ATOM   3302 C  CB   . LEU   A 1 428 ? -0.260  13.932  4.708   1.00 31.78  ?  430 LEU   A CB   1 
ATOM   3303 C  CG   . LEU   A 1 428 ? -0.991  13.756  3.376   1.00 35.01  ?  430 LEU   A CG   1 
ATOM   3304 C  CD1  . LEU   A 1 428 ? -1.639  12.425  3.143   1.00 34.25  ?  430 LEU   A CD1  1 
ATOM   3305 C  CD2  . LEU   A 1 428 ? -2.055  14.841  3.226   1.00 37.59  ?  430 LEU   A CD2  1 
ATOM   3306 N  N    . GLY   A 1 429 ? 2.215   13.892  6.690   1.00 31.76  ?  431 GLY   A N    1 
ATOM   3307 C  CA   . GLY   A 1 429 ? 3.470   14.398  7.231   1.00 32.56  ?  431 GLY   A CA   1 
ATOM   3308 C  C    . GLY   A 1 429 ? 4.591   13.402  7.250   1.00 32.68  ?  431 GLY   A C    1 
ATOM   3309 O  O    . GLY   A 1 429 ? 5.732   13.763  6.963   1.00 37.63  ?  431 GLY   A O    1 
ATOM   3310 N  N    . LYS   A 1 430 ? 4.296   12.147  7.563   1.00 33.49  ?  432 LYS   A N    1 
ATOM   3311 C  CA   . LYS   A 1 430 ? 5.325   11.099  7.475   1.00 34.95  ?  432 LYS   A CA   1 
ATOM   3312 C  C    . LYS   A 1 430 ? 5.797   10.838  6.031   1.00 33.84  ?  432 LYS   A C    1 
ATOM   3313 O  O    . LYS   A 1 430 ? 7.000   10.589  5.777   1.00 27.09  ?  432 LYS   A O    1 
ATOM   3314 C  CB   . LYS   A 1 430 ? 4.839   9.801   8.130   1.00 38.41  ?  432 LYS   A CB   1 
ATOM   3315 C  CG   . LYS   A 1 430 ? 4.840   9.928   9.643   1.00 42.19  ?  432 LYS   A CG   1 
ATOM   3316 C  CD   . LYS   A 1 430 ? 4.340   8.683   10.341  1.00 45.41  ?  432 LYS   A CD   1 
ATOM   3317 C  CE   . LYS   A 1 430 ? 3.799   9.023   11.722  1.00 45.70  ?  432 LYS   A CE   1 
ATOM   3318 N  NZ   . LYS   A 1 430 ? 3.210   7.810   12.327  1.00 48.76  ?  432 LYS   A NZ   1 
ATOM   3319 N  N    . VAL   A 1 431 ? 4.859   10.920  5.087   1.00 33.14  ?  433 VAL   A N    1 
ATOM   3320 C  CA   . VAL   A 1 431 ? 5.205   10.766  3.680   1.00 36.76  ?  433 VAL   A CA   1 
ATOM   3321 C  C    . VAL   A 1 431 ? 6.026   11.958  3.234   1.00 35.97  ?  433 VAL   A C    1 
ATOM   3322 O  O    . VAL   A 1 431 ? 6.863   11.819  2.361   1.00 40.03  ?  433 VAL   A O    1 
ATOM   3323 C  CB   . VAL   A 1 431 ? 3.976   10.604  2.765   1.00 36.48  ?  433 VAL   A CB   1 
ATOM   3324 C  CG1  . VAL   A 1 431 ? 4.418   10.491  1.301   1.00 35.62  ?  433 VAL   A CG1  1 
ATOM   3325 C  CG2  . VAL   A 1 431 ? 3.183   9.376   3.199   1.00 36.09  ?  433 VAL   A CG2  1 
ATOM   3326 N  N    . GLY   A 1 432 ? 5.790   13.122  3.829   1.00 35.84  ?  434 GLY   A N    1 
ATOM   3327 C  CA   . GLY   A 1 432 ? 6.746   14.228  3.686   1.00 38.94  ?  434 GLY   A CA   1 
ATOM   3328 C  C    . GLY   A 1 432 ? 8.182   13.898  4.116   1.00 38.47  ?  434 GLY   A C    1 
ATOM   3329 O  O    . GLY   A 1 432 ? 9.117   14.151  3.372   1.00 39.64  ?  434 GLY   A O    1 
ATOM   3330 N  N    . SER   A 1 433 ? 8.356   13.351  5.322   1.00 41.34  ?  435 SER   A N    1 
ATOM   3331 C  CA   . SER   A 1 433 ? 9.700   13.116  5.897   1.00 44.00  ?  435 SER   A CA   1 
ATOM   3332 C  C    . SER   A 1 433 ? 10.488  12.244  4.950   1.00 43.12  ?  435 SER   A C    1 
ATOM   3333 O  O    . SER   A 1 433 ? 11.531  12.664  4.448   1.00 41.87  ?  435 SER   A O    1 
ATOM   3334 C  CB   . SER   A 1 433 ? 9.632   12.431  7.273   1.00 46.69  ?  435 SER   A CB   1 
ATOM   3335 O  OG   . SER   A 1 433 ? 9.229   13.333  8.273   1.00 49.28  ?  435 SER   A OG   1 
ATOM   3336 N  N    . LYS   A 1 434 ? 9.914   11.066  4.679   1.00 41.24  ?  436 LYS   A N    1 
ATOM   3337 C  CA   . LYS   A 1 434 ? 10.433  10.064  3.742   1.00 41.48  ?  436 LYS   A CA   1 
ATOM   3338 C  C    . LYS   A 1 434 ? 10.791  10.615  2.343   1.00 39.19  ?  436 LYS   A C    1 
ATOM   3339 O  O    . LYS   A 1 434 ? 11.979  10.621  1.954   1.00 41.69  ?  436 LYS   A O    1 
ATOM   3340 C  CB   . LYS   A 1 434 ? 9.400   8.933   3.625   1.00 43.42  ?  436 LYS   A CB   1 
ATOM   3341 C  CG   . LYS   A 1 434 ? 9.790   7.757   2.736   1.00 45.80  ?  436 LYS   A CG   1 
ATOM   3342 C  CD   . LYS   A 1 434 ? 10.682  6.737   3.423   1.00 46.78  ?  436 LYS   A CD   1 
ATOM   3343 C  CE   . LYS   A 1 434 ? 10.300  5.327   2.977   1.00 48.95  ?  436 LYS   A CE   1 
ATOM   3344 N  NZ   . LYS   A 1 434 ? 11.193  4.285   3.536   1.00 49.81  ?  436 LYS   A NZ   1 
ATOM   3345 N  N    . CYS   A 1 435 ? 9.783   11.079  1.602   1.00 37.19  ?  437 CYS   A N    1 
ATOM   3346 C  CA   . CYS   A 1 435 ? 9.965   11.421  0.183   1.00 35.04  ?  437 CYS   A CA   1 
ATOM   3347 C  C    . CYS   A 1 435 ? 10.692  12.711  -0.076  1.00 29.39  ?  437 CYS   A C    1 
ATOM   3348 O  O    . CYS   A 1 435 ? 11.386  12.771  -1.050  1.00 28.27  ?  437 CYS   A O    1 
ATOM   3349 C  CB   . CYS   A 1 435 ? 8.643   11.460  -0.570  1.00 39.60  ?  437 CYS   A CB   1 
ATOM   3350 S  SG   . CYS   A 1 435 ? 7.738   9.917   -0.403  1.00 46.53  ?  437 CYS   A SG   1 
ATOM   3351 N  N    . CYS   A 1 436 ? 10.564  13.734  0.767   1.00 25.54  ?  438 CYS   A N    1 
ATOM   3352 C  CA   . CYS   A 1 436 ? 11.412  14.936  0.587   1.00 26.82  ?  438 CYS   A CA   1 
ATOM   3353 C  C    . CYS   A 1 436 ? 12.937  14.708  0.819   1.00 23.93  ?  438 CYS   A C    1 
ATOM   3354 O  O    . CYS   A 1 436 ? 13.718  15.590  0.531   1.00 23.17  ?  438 CYS   A O    1 
ATOM   3355 C  CB   . CYS   A 1 436 ? 10.919  16.086  1.450   1.00 29.79  ?  438 CYS   A CB   1 
ATOM   3356 S  SG   . CYS   A 1 436 ? 9.157   16.408  1.221   1.00 34.11  ?  438 CYS   A SG   1 
ATOM   3357 N  N    . LYS   A 1 437 ? 13.345  13.536  1.313   1.00 24.68  ?  439 LYS   A N    1 
ATOM   3358 C  CA   . LYS   A 1 437 ? 14.787  13.124  1.377   1.00 26.91  ?  439 LYS   A CA   1 
ATOM   3359 C  C    . LYS   A 1 437 ? 15.342  12.590  0.060   1.00 28.46  ?  439 LYS   A C    1 
ATOM   3360 O  O    . LYS   A 1 437 ? 16.554  12.486  -0.107  1.00 31.26  ?  439 LYS   A O    1 
ATOM   3361 C  CB   . LYS   A 1 437 ? 14.994  12.035  2.459   1.00 27.55  ?  439 LYS   A CB   1 
ATOM   3362 N  N    . HIS   A 1 438 ? 14.458  12.190  -0.849  1.00 30.73  ?  440 HIS   A N    1 
ATOM   3363 C  CA   . HIS   A 1 438 ? 14.825  11.888  -2.215  1.00 30.64  ?  440 HIS   A CA   1 
ATOM   3364 C  C    . HIS   A 1 438 ? 15.010  13.150  -3.036  1.00 29.46  ?  440 HIS   A C    1 
ATOM   3365 O  O    . HIS   A 1 438 ? 14.267  14.121  -2.873  1.00 27.58  ?  440 HIS   A O    1 
ATOM   3366 C  CB   . HIS   A 1 438 ? 13.747  11.051  -2.896  1.00 31.94  ?  440 HIS   A CB   1 
ATOM   3367 C  CG   . HIS   A 1 438 ? 13.739  9.615   -2.491  1.00 35.02  ?  440 HIS   A CG   1 
ATOM   3368 N  ND1  . HIS   A 1 438 ? 14.883  8.853   -2.428  1.00 42.32  ?  440 HIS   A ND1  1 
ATOM   3369 C  CD2  . HIS   A 1 438 ? 12.716  8.788   -2.162  1.00 39.24  ?  440 HIS   A CD2  1 
ATOM   3370 C  CE1  . HIS   A 1 438 ? 14.571  7.622   -2.049  1.00 44.54  ?  440 HIS   A CE1  1 
ATOM   3371 N  NE2  . HIS   A 1 438 ? 13.259  7.554   -1.893  1.00 42.70  ?  440 HIS   A NE2  1 
ATOM   3372 N  N    . PRO   A 1 439 ? 15.949  13.120  -3.986  1.00 30.94  ?  441 PRO   A N    1 
ATOM   3373 C  CA   . PRO   A 1 439 ? 16.014  14.212  -4.984  1.00 33.07  ?  441 PRO   A CA   1 
ATOM   3374 C  C    . PRO   A 1 439 ? 14.709  14.317  -5.806  1.00 32.89  ?  441 PRO   A C    1 
ATOM   3375 O  O    . PRO   A 1 439 ? 13.965  13.346  -5.888  1.00 34.28  ?  441 PRO   A O    1 
ATOM   3376 C  CB   . PRO   A 1 439 ? 17.219  13.835  -5.867  1.00 32.90  ?  441 PRO   A CB   1 
ATOM   3377 C  CG   . PRO   A 1 439 ? 17.608  12.431  -5.509  1.00 32.40  ?  441 PRO   A CG   1 
ATOM   3378 C  CD   . PRO   A 1 439 ? 16.912  12.035  -4.244  1.00 33.11  ?  441 PRO   A CD   1 
ATOM   3379 N  N    . GLU   A 1 440 ? 14.427  15.482  -6.384  1.00 38.38  ?  442 GLU   A N    1 
ATOM   3380 C  CA   . GLU   A 1 440 ? 13.187  15.705  -7.164  1.00 43.01  ?  442 GLU   A CA   1 
ATOM   3381 C  C    . GLU   A 1 440 ? 12.850  14.497  -8.034  1.00 44.99  ?  442 GLU   A C    1 
ATOM   3382 O  O    . GLU   A 1 440 ? 11.775  13.904  -7.873  1.00 50.20  ?  442 GLU   A O    1 
ATOM   3383 C  CB   . GLU   A 1 440 ? 13.261  16.979  -8.037  1.00 44.70  ?  442 GLU   A CB   1 
ATOM   3384 C  CG   . GLU   A 1 440 ? 12.033  17.152  -8.946  1.00 48.13  ?  442 GLU   A CG   1 
ATOM   3385 C  CD   . GLU   A 1 440 ? 11.802  18.570  -9.476  1.00 55.54  ?  442 GLU   A CD   1 
ATOM   3386 O  OE1  . GLU   A 1 440 ? 12.592  19.498  -9.156  1.00 56.87  ?  442 GLU   A OE1  1 
ATOM   3387 O  OE2  . GLU   A 1 440 ? 10.803  18.759  -10.221 1.00 55.86  ?  442 GLU   A OE2  1 
ATOM   3388 N  N    . ALA   A 1 441 ? 13.801  14.121  -8.895  1.00 42.43  ?  443 ALA   A N    1 
ATOM   3389 C  CA   . ALA   A 1 441 ? 13.676  13.025  -9.865  1.00 42.39  ?  443 ALA   A CA   1 
ATOM   3390 C  C    . ALA   A 1 441 ? 13.230  11.669  -9.299  1.00 42.11  ?  443 ALA   A C    1 
ATOM   3391 O  O    . ALA   A 1 441 ? 12.796  10.822  -10.058 1.00 38.43  ?  443 ALA   A O    1 
ATOM   3392 C  CB   . ALA   A 1 441 ? 14.995  12.844  -10.607 1.00 43.87  ?  443 ALA   A CB   1 
ATOM   3393 N  N    . LYS   A 1 442 ? 13.357  11.454  -7.994  1.00 41.88  ?  444 LYS   A N    1 
ATOM   3394 C  CA   . LYS   A 1 442 ? 12.816  10.254  -7.347  1.00 40.93  ?  444 LYS   A CA   1 
ATOM   3395 C  C    . LYS   A 1 442 ? 11.554  10.513  -6.521  1.00 37.20  ?  444 LYS   A C    1 
ATOM   3396 O  O    . LYS   A 1 442 ? 10.944  9.551   -6.020  1.00 35.89  ?  444 LYS   A O    1 
ATOM   3397 C  CB   . LYS   A 1 442 ? 13.871  9.637   -6.444  1.00 46.00  ?  444 LYS   A CB   1 
ATOM   3398 C  CG   . LYS   A 1 442 ? 15.189  9.343   -7.150  1.00 49.58  ?  444 LYS   A CG   1 
ATOM   3399 C  CD   . LYS   A 1 442 ? 15.737  7.989   -6.747  1.00 50.90  ?  444 LYS   A CD   1 
ATOM   3400 C  CE   . LYS   A 1 442 ? 14.998  6.865   -7.464  1.00 53.12  ?  444 LYS   A CE   1 
ATOM   3401 N  NZ   . LYS   A 1 442 ? 15.098  5.562   -6.747  1.00 53.78  ?  444 LYS   A NZ   1 
ATOM   3402 N  N    . ARG   A 1 443 ? 11.128  11.774  -6.407  1.00 32.31  ?  445 ARG   A N    1 
ATOM   3403 C  CA   . ARG   A 1 443 ? 10.085  12.108  -5.434  1.00 33.33  ?  445 ARG   A CA   1 
ATOM   3404 C  C    . ARG   A 1 443 ? 8.696   11.717  -5.863  1.00 34.36  ?  445 ARG   A C    1 
ATOM   3405 O  O    . ARG   A 1 443 ? 7.986   11.126  -5.077  1.00 33.33  ?  445 ARG   A O    1 
ATOM   3406 C  CB   . ARG   A 1 443 ? 10.071  13.587  -5.097  1.00 34.01  ?  445 ARG   A CB   1 
ATOM   3407 C  CG   . ARG   A 1 443 ? 11.135  13.973  -4.083  1.00 32.24  ?  445 ARG   A CG   1 
ATOM   3408 C  CD   . ARG   A 1 443 ? 10.908  15.382  -3.592  1.00 31.74  ?  445 ARG   A CD   1 
ATOM   3409 N  NE   . ARG   A 1 443 ? 12.116  15.901  -2.984  1.00 30.01  ?  445 ARG   A NE   1 
ATOM   3410 C  CZ   . ARG   A 1 443 ? 12.420  17.190  -2.875  1.00 30.94  ?  445 ARG   A CZ   1 
ATOM   3411 N  NH1  . ARG   A 1 443 ? 11.610  18.158  -3.345  1.00 27.96  ?  445 ARG   A NH1  1 
ATOM   3412 N  NH2  . ARG   A 1 443 ? 13.589  17.508  -2.318  1.00 32.30  ?  445 ARG   A NH2  1 
ATOM   3413 N  N    . MET   A 1 444 ? 8.306   12.064  -7.091  1.00 33.56  ?  446 MET   A N    1 
ATOM   3414 C  CA   . MET   A 1 444 ? 6.951   11.764  -7.542  1.00 34.74  ?  446 MET   A CA   1 
ATOM   3415 C  C    . MET   A 1 444 ? 6.695   10.276  -7.325  1.00 30.77  ?  446 MET   A C    1 
ATOM   3416 O  O    . MET   A 1 444 ? 5.729   9.941   -6.700  1.00 29.07  ?  446 MET   A O    1 
ATOM   3417 C  CB   . MET   A 1 444 ? 6.701   12.202  -8.987  1.00 34.08  ?  446 MET   A CB   1 
ATOM   3418 C  CG   . MET   A 1 444 ? 5.288   12.686  -9.270  1.00 36.48  ?  446 MET   A CG   1 
ATOM   3419 S  SD   . MET   A 1 444 ? 5.042   12.974  -11.058 1.00 40.77  ?  446 MET   A SD   1 
ATOM   3420 C  CE   . MET   A 1 444 ? 6.363   14.158  -11.397 1.00 36.67  ?  446 MET   A CE   1 
ATOM   3421 N  N    . PRO   A 1 445 ? 7.630   9.391   -7.730  1.00 33.25  ?  447 PRO   A N    1 
ATOM   3422 C  CA   . PRO   A 1 445 ? 7.341   7.982   -7.419  1.00 33.52  ?  447 PRO   A CA   1 
ATOM   3423 C  C    . PRO   A 1 445 ? 7.062   7.734   -5.962  1.00 32.22  ?  447 PRO   A C    1 
ATOM   3424 O  O    . PRO   A 1 445 ? 6.093   7.038   -5.663  1.00 31.62  ?  447 PRO   A O    1 
ATOM   3425 C  CB   . PRO   A 1 445 ? 8.588   7.239   -7.878  1.00 30.15  ?  447 PRO   A CB   1 
ATOM   3426 C  CG   . PRO   A 1 445 ? 9.137   8.100   -8.943  1.00 30.21  ?  447 PRO   A CG   1 
ATOM   3427 C  CD   . PRO   A 1 445 ? 8.764   9.514   -8.661  1.00 30.16  ?  447 PRO   A CD   1 
ATOM   3428 N  N    . CYS   A 1 446 ? 7.898   8.294   -5.074  1.00 33.81  ?  448 CYS   A N    1 
ATOM   3429 C  CA   . CYS   A 1 446 ? 7.784   8.065   -3.602  1.00 33.93  ?  448 CYS   A CA   1 
ATOM   3430 C  C    . CYS   A 1 446 ? 6.430   8.577   -3.105  1.00 29.74  ?  448 CYS   A C    1 
ATOM   3431 O  O    . CYS   A 1 446 ? 5.682   7.867   -2.452  1.00 27.65  ?  448 CYS   A O    1 
ATOM   3432 C  CB   . CYS   A 1 446 ? 8.984   8.722   -2.860  1.00 36.72  ?  448 CYS   A CB   1 
ATOM   3433 S  SG   . CYS   A 1 446 ? 9.045   8.493   -1.058  1.00 40.97  ?  448 CYS   A SG   1 
ATOM   3434 N  N    . ALA   A 1 447 ? 6.101   9.812   -3.480  1.00 30.79  ?  449 ALA   A N    1 
ATOM   3435 C  CA   . ALA   A 1 447 ? 4.752   10.370  -3.260  1.00 32.18  ?  449 ALA   A CA   1 
ATOM   3436 C  C    . ALA   A 1 447 ? 3.629   9.353   -3.571  1.00 30.67  ?  449 ALA   A C    1 
ATOM   3437 O  O    . ALA   A 1 447 ? 2.884   8.935   -2.698  1.00 34.90  ?  449 ALA   A O    1 
ATOM   3438 C  CB   . ALA   A 1 447 ? 4.569   11.663  -4.072  1.00 32.37  ?  449 ALA   A CB   1 
ATOM   3439 N  N    . GLU   A 1 448 ? 3.595   8.889   -4.807  1.00 30.17  ?  450 GLU   A N    1 
ATOM   3440 C  CA   . GLU   A 1 448 ? 2.511   8.063   -5.305  1.00 28.73  ?  450 GLU   A CA   1 
ATOM   3441 C  C    . GLU   A 1 448 ? 2.204   6.809   -4.498  1.00 29.45  ?  450 GLU   A C    1 
ATOM   3442 O  O    . GLU   A 1 448 ? 1.036   6.518   -4.232  1.00 27.96  ?  450 GLU   A O    1 
ATOM   3443 C  CB   . GLU   A 1 448 ? 2.818   7.630   -6.725  1.00 25.92  ?  450 GLU   A CB   1 
ATOM   3444 C  CG   . GLU   A 1 448 ? 1.777   6.708   -7.277  1.00 24.33  ?  450 GLU   A CG   1 
ATOM   3445 C  CD   . GLU   A 1 448 ? 1.895   6.558   -8.755  1.00 23.96  ?  450 GLU   A CD   1 
ATOM   3446 O  OE1  . GLU   A 1 448 ? 3.002   6.227   -9.223  1.00 22.97  ?  450 GLU   A OE1  1 
ATOM   3447 O  OE2  . GLU   A 1 448 ? 0.875   6.788   -9.452  1.00 24.09  ?  450 GLU   A OE2  1 
ATOM   3448 N  N    . ASP   A 1 449 ? 3.232   6.043   -4.180  1.00 31.05  ?  451 ASP   A N    1 
ATOM   3449 C  CA   . ASP   A 1 449 ? 3.028   4.726   -3.565  1.00 35.24  ?  451 ASP   A CA   1 
ATOM   3450 C  C    . ASP   A 1 449 ? 2.397   4.865   -2.138  1.00 36.98  ?  451 ASP   A C    1 
ATOM   3451 O  O    . ASP   A 1 449 ? 1.464   4.119   -1.728  1.00 29.23  ?  451 ASP   A O    1 
ATOM   3452 C  CB   . ASP   A 1 449 ? 4.365   3.951   -3.524  1.00 40.45  ?  451 ASP   A CB   1 
ATOM   3453 C  CG   . ASP   A 1 449 ? 4.164   2.418   -3.587  1.00 46.83  ?  451 ASP   A CG   1 
ATOM   3454 O  OD1  . ASP   A 1 449 ? 3.444   1.933   -4.501  1.00 47.39  ?  451 ASP   A OD1  1 
ATOM   3455 O  OD2  . ASP   A 1 449 ? 4.751   1.696   -2.737  1.00 50.97  ?  451 ASP   A OD2  1 
ATOM   3456 N  N    . TYR   A 1 450 ? 2.866   5.879   -1.418  1.00 36.84  ?  452 TYR   A N    1 
ATOM   3457 C  CA   . TYR   A 1 450 ? 2.417   6.081   -0.052  1.00 39.97  ?  452 TYR   A CA   1 
ATOM   3458 C  C    . TYR   A 1 450 ? 1.133   6.889   -0.017  1.00 38.73  ?  452 TYR   A C    1 
ATOM   3459 O  O    . TYR   A 1 450 ? 0.246   6.607   0.794   1.00 38.64  ?  452 TYR   A O    1 
ATOM   3460 C  CB   . TYR   A 1 450 ? 3.526   6.714   0.807   1.00 41.05  ?  452 TYR   A CB   1 
ATOM   3461 C  CG   . TYR   A 1 450 ? 4.629   5.747   1.191   1.00 44.03  ?  452 TYR   A CG   1 
ATOM   3462 C  CD1  . TYR   A 1 450 ? 4.341   4.431   1.638   1.00 45.98  ?  452 TYR   A CD1  1 
ATOM   3463 C  CD2  . TYR   A 1 450 ? 5.961   6.142   1.138   1.00 44.25  ?  452 TYR   A CD2  1 
ATOM   3464 C  CE1  . TYR   A 1 450 ? 5.356   3.554   2.006   1.00 48.87  ?  452 TYR   A CE1  1 
ATOM   3465 C  CE2  . TYR   A 1 450 ? 6.991   5.273   1.516   1.00 48.67  ?  452 TYR   A CE2  1 
ATOM   3466 C  CZ   . TYR   A 1 450 ? 6.698   3.981   1.941   1.00 50.06  ?  452 TYR   A CZ   1 
ATOM   3467 O  OH   . TYR   A 1 450 ? 7.737   3.133   2.299   1.00 47.29  ?  452 TYR   A OH   1 
ATOM   3468 N  N    . LEU   A 1 451 ? 1.019   7.881   -0.896  1.00 34.61  ?  453 LEU   A N    1 
ATOM   3469 C  CA   . LEU   A 1 451 ? -0.174  8.663   -0.939  1.00 32.74  ?  453 LEU   A CA   1 
ATOM   3470 C  C    . LEU   A 1 451 ? -1.315  7.812   -1.410  1.00 30.99  ?  453 LEU   A C    1 
ATOM   3471 O  O    . LEU   A 1 451 ? -2.404  7.944   -0.895  1.00 31.80  ?  453 LEU   A O    1 
ATOM   3472 C  CB   . LEU   A 1 451 ? 0.004   9.917   -1.795  1.00 34.64  ?  453 LEU   A CB   1 
ATOM   3473 C  CG   . LEU   A 1 451 ? 0.549   11.184  -1.090  1.00 35.70  ?  453 LEU   A CG   1 
ATOM   3474 C  CD1  . LEU   A 1 451 ? 1.172   10.969  0.280   1.00 35.30  ?  453 LEU   A CD1  1 
ATOM   3475 C  CD2  . LEU   A 1 451 ? 1.511   11.947  -2.001  1.00 35.75  ?  453 LEU   A CD2  1 
ATOM   3476 N  N    . SER   A 1 452 ? -1.072  6.913   -2.357  1.00 33.12  ?  454 SER   A N    1 
ATOM   3477 C  CA   . SER   A 1 452 ? -2.123  5.995   -2.798  1.00 37.09  ?  454 SER   A CA   1 
ATOM   3478 C  C    . SER   A 1 452 ? -2.787  5.300   -1.601  1.00 34.97  ?  454 SER   A C    1 
ATOM   3479 O  O    . SER   A 1 452 ? -4.027  5.218   -1.552  1.00 35.07  ?  454 SER   A O    1 
ATOM   3480 C  CB   . SER   A 1 452 ? -1.589  4.953   -3.787  1.00 40.30  ?  454 SER   A CB   1 
ATOM   3481 O  OG   . SER   A 1 452 ? -0.508  4.219   -3.217  1.00 42.90  ?  454 SER   A OG   1 
ATOM   3482 N  N    . VAL   A 1 453 ? -1.974  4.851   -0.639  1.00 32.65  ?  455 VAL   A N    1 
ATOM   3483 C  CA   . VAL   A 1 453 ? -2.500  4.193   0.562   1.00 35.13  ?  455 VAL   A CA   1 
ATOM   3484 C  C    . VAL   A 1 453 ? -3.115  5.131   1.621   1.00 33.10  ?  455 VAL   A C    1 
ATOM   3485 O  O    . VAL   A 1 453 ? -4.108  4.782   2.278   1.00 31.79  ?  455 VAL   A O    1 
ATOM   3486 C  CB   . VAL   A 1 453 ? -1.502  3.217   1.224   1.00 35.60  ?  455 VAL   A CB   1 
ATOM   3487 C  CG1  . VAL   A 1 453 ? -1.036  2.168   0.207   1.00 35.51  ?  455 VAL   A CG1  1 
ATOM   3488 C  CG2  . VAL   A 1 453 ? -0.320  3.920   1.871   1.00 37.76  ?  455 VAL   A CG2  1 
ATOM   3489 N  N    . VAL   A 1 454 ? -2.573  6.336   1.747   1.00 29.48  ?  456 VAL   A N    1 
ATOM   3490 C  CA   . VAL   A 1 454 ? -3.217  7.310   2.601   1.00 28.45  ?  456 VAL   A CA   1 
ATOM   3491 C  C    . VAL   A 1 454 ? -4.631  7.695   2.074   1.00 27.53  ?  456 VAL   A C    1 
ATOM   3492 O  O    . VAL   A 1 454 ? -5.599  7.785   2.869   1.00 23.91  ?  456 VAL   A O    1 
ATOM   3493 C  CB   . VAL   A 1 454 ? -2.336  8.530   2.812   1.00 29.56  ?  456 VAL   A CB   1 
ATOM   3494 C  CG1  . VAL   A 1 454 ? -3.050  9.529   3.732   1.00 31.85  ?  456 VAL   A CG1  1 
ATOM   3495 C  CG2  . VAL   A 1 454 ? -0.989  8.100   3.397   1.00 29.15  ?  456 VAL   A CG2  1 
ATOM   3496 N  N    . LEU   A 1 455 ? -4.755  7.828   0.748   1.00 26.00  ?  457 LEU   A N    1 
ATOM   3497 C  CA   . LEU   A 1 455 ? -6.005  8.276   0.132   1.00 27.75  ?  457 LEU   A CA   1 
ATOM   3498 C  C    . LEU   A 1 455 ? -7.045  7.196   0.138   1.00 27.61  ?  457 LEU   A C    1 
ATOM   3499 O  O    . LEU   A 1 455 ? -8.193  7.473   0.449   1.00 27.39  ?  457 LEU   A O    1 
ATOM   3500 C  CB   . LEU   A 1 455 ? -5.811  8.806   -1.299  1.00 26.81  ?  457 LEU   A CB   1 
ATOM   3501 C  CG   . LEU   A 1 455 ? -5.853  10.324  -1.435  1.00 28.13  ?  457 LEU   A CG   1 
ATOM   3502 C  CD1  . LEU   A 1 455 ? -4.762  11.005  -0.580  1.00 30.05  ?  457 LEU   A CD1  1 
ATOM   3503 C  CD2  . LEU   A 1 455 ? -5.720  10.660  -2.908  1.00 26.54  ?  457 LEU   A CD2  1 
ATOM   3504 N  N    . ASN   A 1 456 ? -6.672  5.965   -0.189  1.00 30.21  ?  458 ASN   A N    1 
ATOM   3505 C  CA   . ASN   A 1 456 ? -7.629  4.848   -0.063  1.00 31.74  ?  458 ASN   A CA   1 
ATOM   3506 C  C    . ASN   A 1 456 ? -8.104  4.617   1.390   1.00 36.16  ?  458 ASN   A C    1 
ATOM   3507 O  O    . ASN   A 1 456 ? -9.311  4.436   1.629   1.00 41.28  ?  458 ASN   A O    1 
ATOM   3508 C  CB   . ASN   A 1 456 ? -7.056  3.554   -0.608  1.00 31.81  ?  458 ASN   A CB   1 
ATOM   3509 C  CG   . ASN   A 1 456 ? -8.088  2.440   -0.634  1.00 34.43  ?  458 ASN   A CG   1 
ATOM   3510 O  OD1  . ASN   A 1 456 ? -9.179  2.620   -1.158  1.00 37.82  ?  458 ASN   A OD1  1 
ATOM   3511 N  ND2  . ASN   A 1 456 ? -7.757  1.298   -0.059  1.00 32.21  ?  458 ASN   A ND2  1 
ATOM   3512 N  N    . GLN   A 1 457 ? -7.178  4.632   2.352   1.00 35.32  ?  459 GLN   A N    1 
ATOM   3513 C  CA   . GLN   A 1 457 ? -7.542  4.582   3.766   1.00 35.22  ?  459 GLN   A CA   1 
ATOM   3514 C  C    . GLN   A 1 457 ? -8.649  5.577   4.022   1.00 33.48  ?  459 GLN   A C    1 
ATOM   3515 O  O    . GLN   A 1 457 ? -9.672  5.233   4.598   1.00 27.73  ?  459 GLN   A O    1 
ATOM   3516 C  CB   . GLN   A 1 457 ? -6.377  4.998   4.674   1.00 39.63  ?  459 GLN   A CB   1 
ATOM   3517 C  CG   . GLN   A 1 457 ? -5.692  3.916   5.494   1.00 45.98  ?  459 GLN   A CG   1 
ATOM   3518 C  CD   . GLN   A 1 457 ? -4.495  4.473   6.278   1.00 46.24  ?  459 GLN   A CD   1 
ATOM   3519 O  OE1  . GLN   A 1 457 ? -4.366  5.706   6.489   1.00 43.60  ?  459 GLN   A OE1  1 
ATOM   3520 N  NE2  . GLN   A 1 457 ? -3.593  3.571   6.679   1.00 46.56  ?  459 GLN   A NE2  1 
ATOM   3521 N  N    . LEU   A 1 458 ? -8.360  6.825   3.628   1.00 30.24  ?  460 LEU   A N    1 
ATOM   3522 C  CA   . LEU   A 1 458 ? -9.238  7.974   3.759   1.00 31.21  ?  460 LEU   A CA   1 
ATOM   3523 C  C    . LEU   A 1 458 ? -10.643 7.662   3.219   1.00 33.40  ?  460 LEU   A C    1 
ATOM   3524 O  O    . LEU   A 1 458 ? -11.648 7.821   3.925   1.00 37.40  ?  460 LEU   A O    1 
ATOM   3525 C  CB   . LEU   A 1 458 ? -8.616  9.151   2.986   1.00 32.22  ?  460 LEU   A CB   1 
ATOM   3526 C  CG   . LEU   A 1 458 ? -8.969  10.587  3.234   1.00 35.50  ?  460 LEU   A CG   1 
ATOM   3527 C  CD1  . LEU   A 1 458 ? -8.262  11.007  4.515   1.00 42.87  ?  460 LEU   A CD1  1 
ATOM   3528 C  CD2  . LEU   A 1 458 ? -8.506  11.476  2.096   1.00 34.07  ?  460 LEU   A CD2  1 
ATOM   3529 N  N    . CYS   A 1 459 ? -10.696 7.181   1.981   1.00 31.86  ?  461 CYS   A N    1 
ATOM   3530 C  CA   . CYS   A 1 459 ? -11.947 6.848   1.318   1.00 32.27  ?  461 CYS   A CA   1 
ATOM   3531 C  C    . CYS   A 1 459 ? -12.759 5.651   1.877   1.00 34.89  ?  461 CYS   A C    1 
ATOM   3532 O  O    . CYS   A 1 459 ? -14.013 5.658   1.822   1.00 30.76  ?  461 CYS   A O    1 
ATOM   3533 C  CB   . CYS   A 1 459 ? -11.654 6.635   -0.172  1.00 32.50  ?  461 CYS   A CB   1 
ATOM   3534 S  SG   . CYS   A 1 459 ? -11.135 8.203   -0.865  1.00 34.53  ?  461 CYS   A SG   1 
ATOM   3535 N  N    . VAL   A 1 460 ? -12.069 4.640   2.397   1.00 33.25  ?  462 VAL   A N    1 
ATOM   3536 C  CA   . VAL   A 1 460 ? -12.748 3.492   2.974   1.00 36.37  ?  462 VAL   A CA   1 
ATOM   3537 C  C    . VAL   A 1 460 ? -13.407 3.935   4.278   1.00 39.07  ?  462 VAL   A C    1 
ATOM   3538 O  O    . VAL   A 1 460 ? -14.588 3.650   4.494   1.00 45.44  ?  462 VAL   A O    1 
ATOM   3539 C  CB   . VAL   A 1 460 ? -11.803 2.289   3.264   1.00 39.54  ?  462 VAL   A CB   1 
ATOM   3540 C  CG1  . VAL   A 1 460 ? -12.601 1.116   3.845   1.00 36.90  ?  462 VAL   A CG1  1 
ATOM   3541 C  CG2  . VAL   A 1 460 ? -11.014 1.856   2.020   1.00 39.05  ?  462 VAL   A CG2  1 
ATOM   3542 N  N    . LEU   A 1 461 ? -12.657 4.626   5.135   1.00 38.14  ?  463 LEU   A N    1 
ATOM   3543 C  CA   . LEU   A 1 461 ? -13.226 5.191   6.354   1.00 43.17  ?  463 LEU   A CA   1 
ATOM   3544 C  C    . LEU   A 1 461 ? -14.464 5.991   5.968   1.00 42.17  ?  463 LEU   A C    1 
ATOM   3545 O  O    . LEU   A 1 461 ? -15.582 5.662   6.397   1.00 45.29  ?  463 LEU   A O    1 
ATOM   3546 C  CB   . LEU   A 1 461 ? -12.214 6.075   7.114   1.00 45.18  ?  463 LEU   A CB   1 
ATOM   3547 C  CG   . LEU   A 1 461 ? -11.121 5.389   7.953   1.00 47.72  ?  463 LEU   A CG   1 
ATOM   3548 C  CD1  . LEU   A 1 461 ? -10.124 6.410   8.509   1.00 46.92  ?  463 LEU   A CD1  1 
ATOM   3549 C  CD2  . LEU   A 1 461 ? -11.722 4.574   9.096   1.00 47.94  ?  463 LEU   A CD2  1 
ATOM   3550 N  N    . HIS   A 1 462 ? -14.273 6.973   5.089   1.00 38.03  ?  464 HIS   A N    1 
ATOM   3551 C  CA   . HIS   A 1 462 ? -15.375 7.838   4.668   1.00 36.97  ?  464 HIS   A CA   1 
ATOM   3552 C  C    . HIS   A 1 462 ? -16.560 7.130   4.018   1.00 38.74  ?  464 HIS   A C    1 
ATOM   3553 O  O    . HIS   A 1 462 ? -17.669 7.609   4.106   1.00 40.83  ?  464 HIS   A O    1 
ATOM   3554 C  CB   . HIS   A 1 462 ? -14.882 8.895   3.720   1.00 35.10  ?  464 HIS   A CB   1 
ATOM   3555 C  CG   . HIS   A 1 462 ? -15.845 10.021  3.537   1.00 34.97  ?  464 HIS   A CG   1 
ATOM   3556 N  ND1  . HIS   A 1 462 ? -16.700 10.093  2.463   1.00 30.54  ?  464 HIS   A ND1  1 
ATOM   3557 C  CD2  . HIS   A 1 462 ? -16.102 11.113  4.298   1.00 35.87  ?  464 HIS   A CD2  1 
ATOM   3558 C  CE1  . HIS   A 1 462 ? -17.416 11.193  2.550   1.00 31.36  ?  464 HIS   A CE1  1 
ATOM   3559 N  NE2  . HIS   A 1 462 ? -17.084 11.823  3.659   1.00 34.28  ?  464 HIS   A NE2  1 
ATOM   3560 N  N    . GLU   A 1 463 ? -16.331 6.015   3.337   1.00 45.19  ?  465 GLU   A N    1 
ATOM   3561 C  CA   . GLU   A 1 463 ? -17.441 5.230   2.791   1.00 50.15  ?  465 GLU   A CA   1 
ATOM   3562 C  C    . GLU   A 1 463 ? -18.213 4.570   3.929   1.00 47.42  ?  465 GLU   A C    1 
ATOM   3563 O  O    . GLU   A 1 463 ? -19.419 4.438   3.828   1.00 47.17  ?  465 GLU   A O    1 
ATOM   3564 C  CB   . GLU   A 1 463 ? -16.960 4.207   1.730   1.00 55.95  ?  465 GLU   A CB   1 
ATOM   3565 C  CG   . GLU   A 1 463 ? -17.914 3.051   1.373   1.00 62.55  ?  465 GLU   A CG   1 
ATOM   3566 C  CD   . GLU   A 1 463 ? -19.229 3.457   0.692   1.00 68.82  ?  465 GLU   A CD   1 
ATOM   3567 O  OE1  . GLU   A 1 463 ? -19.547 4.671   0.587   1.00 75.71  ?  465 GLU   A OE1  1 
ATOM   3568 O  OE2  . GLU   A 1 463 ? -19.961 2.532   0.256   1.00 65.13  ?  465 GLU   A OE2  1 
ATOM   3569 N  N    . LYS   A 1 464 ? -17.525 4.167   4.999   1.00 49.52  ?  466 LYS   A N    1 
ATOM   3570 C  CA   . LYS   A 1 464 ? -18.196 3.550   6.155   1.00 53.54  ?  466 LYS   A CA   1 
ATOM   3571 C  C    . LYS   A 1 464 ? -19.158 4.530   6.858   1.00 49.17  ?  466 LYS   A C    1 
ATOM   3572 O  O    . LYS   A 1 464 ? -20.318 4.171   7.109   1.00 45.04  ?  466 LYS   A O    1 
ATOM   3573 C  CB   . LYS   A 1 464 ? -17.184 2.940   7.161   1.00 55.94  ?  466 LYS   A CB   1 
ATOM   3574 C  CG   . LYS   A 1 464 ? -16.496 1.656   6.690   1.00 57.95  ?  466 LYS   A CG   1 
ATOM   3575 C  CD   . LYS   A 1 464 ? -15.944 0.824   7.843   1.00 59.07  ?  466 LYS   A CD   1 
ATOM   3576 N  N    . THR   A 1 465 ? -18.684 5.751   7.158   1.00 47.25  ?  467 THR   A N    1 
ATOM   3577 C  CA   . THR   A 1 465 ? -19.546 6.802   7.754   1.00 45.14  ?  467 THR   A CA   1 
ATOM   3578 C  C    . THR   A 1 465 ? -19.418 8.131   7.012   1.00 40.76  ?  467 THR   A C    1 
ATOM   3579 O  O    . THR   A 1 465 ? -18.743 9.049   7.484   1.00 37.15  ?  467 THR   A O    1 
ATOM   3580 C  CB   . THR   A 1 465 ? -19.322 6.984   9.294   1.00 50.34  ?  467 THR   A CB   1 
ATOM   3581 O  OG1  . THR   A 1 465 ? -18.039 7.565   9.562   1.00 52.85  ?  467 THR   A OG1  1 
ATOM   3582 C  CG2  . THR   A 1 465 ? -19.444 5.631   10.055  1.00 49.76  ?  467 THR   A CG2  1 
ATOM   3583 N  N    . PRO   A 1 466 ? -20.106 8.259   5.853   1.00 38.11  ?  468 PRO   A N    1 
ATOM   3584 C  CA   . PRO   A 1 466 ? -19.969 9.490   5.064   1.00 37.41  ?  468 PRO   A CA   1 
ATOM   3585 C  C    . PRO   A 1 466 ? -20.416 10.745  5.797   1.00 35.50  ?  468 PRO   A C    1 
ATOM   3586 O  O    . PRO   A 1 466 ? -21.060 10.696  6.813   1.00 39.41  ?  468 PRO   A O    1 
ATOM   3587 C  CB   . PRO   A 1 466 ? -20.809 9.224   3.797   1.00 36.07  ?  468 PRO   A CB   1 
ATOM   3588 C  CG   . PRO   A 1 466 ? -21.004 7.744   3.750   1.00 36.34  ?  468 PRO   A CG   1 
ATOM   3589 C  CD   . PRO   A 1 466 ? -21.005 7.295   5.190   1.00 39.55  ?  468 PRO   A CD   1 
ATOM   3590 N  N    . VAL   A 1 467 ? -20.071 11.869  5.227   1.00 36.14  ?  469 VAL   A N    1 
ATOM   3591 C  CA   . VAL   A 1 467 ? -19.969 13.109  5.978   1.00 34.00  ?  469 VAL   A CA   1 
ATOM   3592 C  C    . VAL   A 1 467 ? -19.853 14.304  5.032   1.00 31.94  ?  469 VAL   A C    1 
ATOM   3593 O  O    . VAL   A 1 467 ? -20.387 15.366  5.317   1.00 31.18  ?  469 VAL   A O    1 
ATOM   3594 C  CB   . VAL   A 1 467 ? -18.769 12.984  7.000   1.00 36.81  ?  469 VAL   A CB   1 
ATOM   3595 C  CG1  . VAL   A 1 467 ? -17.757 14.128  6.914   1.00 36.47  ?  469 VAL   A CG1  1 
ATOM   3596 C  CG2  . VAL   A 1 467 ? -19.259 12.789  8.429   1.00 35.49  ?  469 VAL   A CG2  1 
ATOM   3597 N  N    . SER   A 1 468 ? -19.128 14.138  3.921   1.00 30.33  ?  470 SER   A N    1 
ATOM   3598 C  CA   . SER   A 1 468 ? -18.947 15.184  2.941   1.00 29.16  ?  470 SER   A CA   1 
ATOM   3599 C  C    . SER   A 1 468 ? -19.116 14.633  1.528   1.00 27.86  ?  470 SER   A C    1 
ATOM   3600 O  O    . SER   A 1 468 ? -18.385 13.750  1.089   1.00 26.47  ?  470 SER   A O    1 
ATOM   3601 C  CB   . SER   A 1 468 ? -17.569 15.810  3.114   1.00 28.56  ?  470 SER   A CB   1 
ATOM   3602 O  OG   . SER   A 1 468 ? -17.446 16.900  2.242   1.00 27.17  ?  470 SER   A OG   1 
ATOM   3603 N  N    . ASP   A 1 469 ? -20.115 15.154  0.828   1.00 28.22  ?  471 ASP   A N    1 
ATOM   3604 C  CA   . ASP   A 1 469 ? -20.312 14.869  -0.593  1.00 26.54  ?  471 ASP   A CA   1 
ATOM   3605 C  C    . ASP   A 1 469 ? -19.060 15.125  -1.455  1.00 28.20  ?  471 ASP   A C    1 
ATOM   3606 O  O    . ASP   A 1 469 ? -18.922 14.534  -2.524  1.00 27.67  ?  471 ASP   A O    1 
ATOM   3607 C  CB   . ASP   A 1 469 ? -21.460 15.701  -1.129  1.00 26.75  ?  471 ASP   A CB   1 
ATOM   3608 C  CG   . ASP   A 1 469 ? -21.158 17.191  -1.117  1.00 28.04  ?  471 ASP   A CG   1 
ATOM   3609 O  OD1  . ASP   A 1 469 ? -20.781 17.749  -0.059  1.00 28.13  ?  471 ASP   A OD1  1 
ATOM   3610 O  OD2  . ASP   A 1 469 ? -21.288 17.804  -2.185  1.00 31.49  ?  471 ASP   A OD2  1 
ATOM   3611 N  N    . ARG   A 1 470 ? -18.212 16.064  -1.020  1.00 26.90  ?  472 ARG   A N    1 
ATOM   3612 C  CA   . ARG   A 1 470 ? -16.993 16.404  -1.721  1.00 28.15  ?  472 ARG   A CA   1 
ATOM   3613 C  C    . ARG   A 1 470 ? -15.874 15.390  -1.547  1.00 26.72  ?  472 ARG   A C    1 
ATOM   3614 O  O    . ARG   A 1 470 ? -15.171 15.067  -2.506  1.00 29.96  ?  472 ARG   A O    1 
ATOM   3615 C  CB   . ARG   A 1 470 ? -16.536 17.791  -1.292  1.00 30.23  ?  472 ARG   A CB   1 
ATOM   3616 C  CG   . ARG   A 1 470 ? -17.521 18.841  -1.790  1.00 31.00  ?  472 ARG   A CG   1 
ATOM   3617 C  CD   . ARG   A 1 470 ? -17.449 20.092  -0.973  1.00 33.41  ?  472 ARG   A CD   1 
ATOM   3618 N  NE   . ARG   A 1 470 ? -16.461 20.986  -1.535  1.00 37.14  ?  472 ARG   A NE   1 
ATOM   3619 C  CZ   . ARG   A 1 470 ? -15.429 21.519  -0.894  1.00 39.93  ?  472 ARG   A CZ   1 
ATOM   3620 N  NH1  . ARG   A 1 470 ? -15.217 21.268  0.397   1.00 38.73  ?  472 ARG   A NH1  1 
ATOM   3621 N  NH2  . ARG   A 1 470 ? -14.597 22.332  -1.572  1.00 37.88  ?  472 ARG   A NH2  1 
ATOM   3622 N  N    . VAL   A 1 471 ? -15.696 14.913  -0.331  1.00 24.40  ?  473 VAL   A N    1 
ATOM   3623 C  CA   . VAL   A 1 471 ? -14.842 13.771  -0.087  1.00 25.37  ?  473 VAL   A CA   1 
ATOM   3624 C  C    . VAL   A 1 471 ? -15.411 12.541  -0.787  1.00 27.26  ?  473 VAL   A C    1 
ATOM   3625 O  O    . VAL   A 1 471 ? -14.653 11.751  -1.370  1.00 30.62  ?  473 VAL   A O    1 
ATOM   3626 C  CB   . VAL   A 1 471 ? -14.662 13.500  1.426   1.00 23.62  ?  473 VAL   A CB   1 
ATOM   3627 C  CG1  . VAL   A 1 471 ? -13.903 12.192  1.701   1.00 23.60  ?  473 VAL   A CG1  1 
ATOM   3628 C  CG2  . VAL   A 1 471 ? -13.919 14.655  2.044   1.00 22.46  ?  473 VAL   A CG2  1 
ATOM   3629 N  N    . THR   A 1 472 ? -16.725 12.367  -0.741  1.00 28.54  ?  474 THR   A N    1 
ATOM   3630 C  CA   . THR   A 1 472 ? -17.328 11.249  -1.461  1.00 31.19  ?  474 THR   A CA   1 
ATOM   3631 C  C    . THR   A 1 472 ? -17.108 11.361  -2.964  1.00 28.74  ?  474 THR   A C    1 
ATOM   3632 O  O    . THR   A 1 472 ? -16.851 10.340  -3.585  1.00 29.58  ?  474 THR   A O    1 
ATOM   3633 C  CB   . THR   A 1 472 ? -18.817 11.082  -1.161  1.00 31.75  ?  474 THR   A CB   1 
ATOM   3634 O  OG1  . THR   A 1 472 ? -18.934 10.653  0.193   1.00 33.54  ?  474 THR   A OG1  1 
ATOM   3635 C  CG2  . THR   A 1 472 ? -19.431 10.009  -2.074  1.00 33.99  ?  474 THR   A CG2  1 
ATOM   3636 N  N    . LYS   A 1 473 ? -17.178 12.580  -3.510  1.00 29.17  ?  475 LYS   A N    1 
ATOM   3637 C  CA   . LYS   A 1 473 ? -16.985 12.838  -4.951  1.00 34.04  ?  475 LYS   A CA   1 
ATOM   3638 C  C    . LYS   A 1 473 ? -15.595 12.382  -5.407  1.00 36.73  ?  475 LYS   A C    1 
ATOM   3639 O  O    . LYS   A 1 473 ? -15.470 11.658  -6.398  1.00 38.36  ?  475 LYS   A O    1 
ATOM   3640 C  CB   . LYS   A 1 473 ? -17.187 14.339  -5.265  1.00 34.49  ?  475 LYS   A CB   1 
ATOM   3641 C  CG   . LYS   A 1 473 ? -16.891 14.781  -6.701  1.00 38.20  ?  475 LYS   A CG   1 
ATOM   3642 C  CD   . LYS   A 1 473 ? -18.121 14.682  -7.590  1.00 43.55  ?  475 LYS   A CD   1 
ATOM   3643 C  CE   . LYS   A 1 473 ? -17.804 14.622  -9.083  1.00 47.03  ?  475 LYS   A CE   1 
ATOM   3644 N  NZ   . LYS   A 1 473 ? -17.443 15.952  -9.664  1.00 52.61  ?  475 LYS   A NZ   1 
ATOM   3645 N  N    . CYS   A 1 474 ? -14.569 12.803  -4.665  1.00 34.91  ?  476 CYS   A N    1 
ATOM   3646 C  CA   . CYS   A 1 474 ? -13.178 12.499  -4.987  1.00 33.76  ?  476 CYS   A CA   1 
ATOM   3647 C  C    . CYS   A 1 474 ? -12.918 10.993  -4.788  1.00 37.70  ?  476 CYS   A C    1 
ATOM   3648 O  O    . CYS   A 1 474 ? -12.346 10.331  -5.651  1.00 36.29  ?  476 CYS   A O    1 
ATOM   3649 C  CB   . CYS   A 1 474 ? -12.256 13.356  -4.088  1.00 33.10  ?  476 CYS   A CB   1 
ATOM   3650 S  SG   . CYS   A 1 474 ? -12.414 15.159  -4.343  1.00 32.75  ?  476 CYS   A SG   1 
ATOM   3651 N  N    . CYS   A 1 475 ? -13.414 10.443  -3.685  1.00 38.06  ?  477 CYS   A N    1 
ATOM   3652 C  CA   . CYS   A 1 475 ? -13.338 8.999   -3.436  1.00 39.34  ?  477 CYS   A CA   1 
ATOM   3653 C  C    . CYS   A 1 475 ? -13.974 8.090   -4.498  1.00 38.47  ?  477 CYS   A C    1 
ATOM   3654 O  O    . CYS   A 1 475 ? -13.627 6.917   -4.559  1.00 40.41  ?  477 CYS   A O    1 
ATOM   3655 C  CB   . CYS   A 1 475 ? -13.905 8.669   -2.052  1.00 37.36  ?  477 CYS   A CB   1 
ATOM   3656 S  SG   . CYS   A 1 475 ? -12.848 9.265   -0.704  1.00 38.86  ?  477 CYS   A SG   1 
ATOM   3657 N  N    . THR   A 1 476 ? -14.907 8.615   -5.296  1.00 39.61  ?  478 THR   A N    1 
ATOM   3658 C  CA   . THR   A 1 476 ? -15.617 7.847   -6.348  1.00 37.31  ?  478 THR   A CA   1 
ATOM   3659 C  C    . THR   A 1 476 ? -15.114 8.195   -7.764  1.00 38.95  ?  478 THR   A C    1 
ATOM   3660 O  O    . THR   A 1 476 ? -15.549 7.627   -8.755  1.00 37.03  ?  478 THR   A O    1 
ATOM   3661 C  CB   . THR   A 1 476 ? -17.153 8.105   -6.281  1.00 36.99  ?  478 THR   A CB   1 
ATOM   3662 O  OG1  . THR   A 1 476 ? -17.422 9.506   -6.039  1.00 32.95  ?  478 THR   A OG1  1 
ATOM   3663 C  CG2  . THR   A 1 476 ? -17.794 7.247   -5.210  1.00 37.89  ?  478 THR   A CG2  1 
ATOM   3664 N  N    . GLU   A 1 477 ? -14.187 9.142   -7.831  1.00 43.35  ?  479 GLU   A N    1 
ATOM   3665 C  CA   . GLU   A 1 477 ? -13.560 9.603   -9.063  1.00 39.26  ?  479 GLU   A CA   1 
ATOM   3666 C  C    . GLU   A 1 477 ? -12.710 8.506   -9.692  1.00 35.03  ?  479 GLU   A C    1 
ATOM   3667 O  O    . GLU   A 1 477 ? -12.303 7.564   -9.015  1.00 34.61  ?  479 GLU   A O    1 
ATOM   3668 C  CB   . GLU   A 1 477 ? -12.678 10.824  -8.739  1.00 41.65  ?  479 GLU   A CB   1 
ATOM   3669 C  CG   . GLU   A 1 477 ? -12.689 11.929  -9.747  1.00 44.22  ?  479 GLU   A CG   1 
ATOM   3670 C  CD   . GLU   A 1 477 ? -14.076 12.399  -10.127 1.00 50.91  ?  479 GLU   A CD   1 
ATOM   3671 O  OE1  . GLU   A 1 477 ? -15.012 12.334  -9.281  1.00 55.27  ?  479 GLU   A OE1  1 
ATOM   3672 O  OE2  . GLU   A 1 477 ? -14.218 12.811  -11.303 1.00 50.96  ?  479 GLU   A OE2  1 
ATOM   3673 N  N    . SER   A 1 478 ? -12.466 8.628   -10.999 1.00 35.87  ?  480 SER   A N    1 
ATOM   3674 C  CA   . SER   A 1 478 ? -11.528 7.757   -11.722 1.00 35.58  ?  480 SER   A CA   1 
ATOM   3675 C  C    . SER   A 1 478 ? -10.196 7.749   -11.008 1.00 35.67  ?  480 SER   A C    1 
ATOM   3676 O  O    . SER   A 1 478 ? -9.836  8.738   -10.365 1.00 36.84  ?  480 SER   A O    1 
ATOM   3677 C  CB   . SER   A 1 478 ? -11.351 8.240   -13.153 1.00 35.90  ?  480 SER   A CB   1 
ATOM   3678 O  OG   . SER   A 1 478 ? -10.860 9.576   -13.181 1.00 36.32  ?  480 SER   A OG   1 
ATOM   3679 N  N    . LEU   A 1 479 ? -9.451  6.652   -11.103 1.00 36.68  ?  481 LEU   A N    1 
ATOM   3680 C  CA   . LEU   A 1 479 ? -8.222  6.489   -10.300 1.00 34.78  ?  481 LEU   A CA   1 
ATOM   3681 C  C    . LEU   A 1 479 ? -7.183  7.567   -10.634 1.00 31.52  ?  481 LEU   A C    1 
ATOM   3682 O  O    . LEU   A 1 479 ? -6.373  7.921   -9.803  1.00 31.05  ?  481 LEU   A O    1 
ATOM   3683 C  CB   . LEU   A 1 479 ? -7.613  5.071   -10.454 1.00 40.52  ?  481 LEU   A CB   1 
ATOM   3684 C  CG   . LEU   A 1 479 ? -6.817  4.350   -9.309  1.00 44.31  ?  481 LEU   A CG   1 
ATOM   3685 C  CD1  . LEU   A 1 479 ? -5.335  4.709   -9.290  1.00 45.95  ?  481 LEU   A CD1  1 
ATOM   3686 C  CD2  . LEU   A 1 479 ? -7.391  4.503   -7.892  1.00 46.53  ?  481 LEU   A CD2  1 
ATOM   3687 N  N    . VAL   A 1 480 ? -7.229  8.085   -11.852 1.00 29.82  ?  482 VAL   A N    1 
ATOM   3688 C  CA   . VAL   A 1 480 ? -6.329  9.147   -12.317 1.00 30.62  ?  482 VAL   A CA   1 
ATOM   3689 C  C    . VAL   A 1 480 ? -6.711  10.560  -11.761 1.00 28.94  ?  482 VAL   A C    1 
ATOM   3690 O  O    . VAL   A 1 480 ? -5.885  11.477  -11.682 1.00 29.22  ?  482 VAL   A O    1 
ATOM   3691 C  CB   . VAL   A 1 480 ? -6.226  9.054   -13.888 1.00 29.52  ?  482 VAL   A CB   1 
ATOM   3692 C  CG1  . VAL   A 1 480 ? -6.598  10.326  -14.611 1.00 29.41  ?  482 VAL   A CG1  1 
ATOM   3693 C  CG2  . VAL   A 1 480 ? -4.837  8.578   -14.280 1.00 30.83  ?  482 VAL   A CG2  1 
ATOM   3694 N  N    . ASN   A 1 481 ? -7.983  10.711  -11.398 1.00 28.63  ?  483 ASN   A N    1 
ATOM   3695 C  CA   . ASN   A 1 481 ? -8.539  11.958  -10.902 1.00 27.99  ?  483 ASN   A CA   1 
ATOM   3696 C  C    . ASN   A 1 481 ? -8.611  12.014  -9.376  1.00 27.10  ?  483 ASN   A C    1 
ATOM   3697 O  O    . ASN   A 1 481 ? -8.731  13.083  -8.835  1.00 27.47  ?  483 ASN   A O    1 
ATOM   3698 C  CB   . ASN   A 1 481 ? -9.945  12.175  -11.488 1.00 29.69  ?  483 ASN   A CB   1 
ATOM   3699 C  CG   . ASN   A 1 481 ? -9.935  12.680  -12.920 1.00 29.34  ?  483 ASN   A CG   1 
ATOM   3700 O  OD1  . ASN   A 1 481 ? -8.898  12.793  -13.554 1.00 32.58  ?  483 ASN   A OD1  1 
ATOM   3701 N  ND2  . ASN   A 1 481 ? -11.101 13.012  -13.420 1.00 29.92  ?  483 ASN   A ND2  1 
ATOM   3702 N  N    . ARG   A 1 482 ? -8.514  10.894  -8.672  1.00 25.75  ?  484 ARG   A N    1 
ATOM   3703 C  CA   . ARG   A 1 482 ? -8.676  10.934  -7.221  1.00 26.60  ?  484 ARG   A CA   1 
ATOM   3704 C  C    . ARG   A 1 482 ? -7.994  12.099  -6.508  1.00 22.88  ?  484 ARG   A C    1 
ATOM   3705 O  O    . ARG   A 1 482 ? -8.644  12.895  -5.828  1.00 22.57  ?  484 ARG   A O    1 
ATOM   3706 C  CB   . ARG   A 1 482 ? -8.160  9.649   -6.612  1.00 29.38  ?  484 ARG   A CB   1 
ATOM   3707 C  CG   . ARG   A 1 482 ? -8.883  9.275   -5.356  1.00 32.29  ?  484 ARG   A CG   1 
ATOM   3708 C  CD   . ARG   A 1 482 ? -8.585  7.820   -5.064  1.00 34.57  ?  484 ARG   A CD   1 
ATOM   3709 N  NE   . ARG   A 1 482 ? -9.749  7.054   -4.683  1.00 35.17  ?  484 ARG   A NE   1 
ATOM   3710 C  CZ   . ARG   A 1 482 ? -9.677  5.777   -4.332  1.00 38.85  ?  484 ARG   A CZ   1 
ATOM   3711 N  NH1  . ARG   A 1 482 ? -8.506  5.141   -4.325  1.00 40.57  ?  484 ARG   A NH1  1 
ATOM   3712 N  NH2  . ARG   A 1 482 ? -10.771 5.128   -3.969  1.00 39.30  ?  484 ARG   A NH2  1 
ATOM   3713 N  N    . ARG   A 1 483 ? -6.683  12.165  -6.669  1.00 20.45  ?  485 ARG   A N    1 
ATOM   3714 C  CA   . ARG   A 1 483 ? -5.821  13.075  -5.930  1.00 19.79  ?  485 ARG   A CA   1 
ATOM   3715 C  C    . ARG   A 1 483 ? -5.986  14.529  -6.421  1.00 20.23  ?  485 ARG   A C    1 
ATOM   3716 O  O    . ARG   A 1 483 ? -6.081  15.429  -5.577  1.00 22.44  ?  485 ARG   A O    1 
ATOM   3717 C  CB   . ARG   A 1 483 ? -4.359  12.586  -6.026  1.00 19.32  ?  485 ARG   A CB   1 
ATOM   3718 C  CG   . ARG   A 1 483 ? -3.380  13.228  -5.068  1.00 19.04  ?  485 ARG   A CG   1 
ATOM   3719 C  CD   . ARG   A 1 483 ? -2.972  14.620  -5.522  1.00 18.97  ?  485 ARG   A CD   1 
ATOM   3720 N  NE   . ARG   A 1 483 ? -2.469  14.579  -6.902  1.00 19.87  ?  485 ARG   A NE   1 
ATOM   3721 C  CZ   . ARG   A 1 483 ? -2.313  15.624  -7.711  1.00 17.88  ?  485 ARG   A CZ   1 
ATOM   3722 N  NH1  . ARG   A 1 483 ? -2.629  16.829  -7.317  1.00 16.03  ?  485 ARG   A NH1  1 
ATOM   3723 N  NH2  . ARG   A 1 483 ? -1.819  15.448  -8.911  1.00 18.04  ?  485 ARG   A NH2  1 
ATOM   3724 N  N    . PRO   A 1 484 ? -6.020  14.762  -7.758  1.00 19.00  ?  486 PRO   A N    1 
ATOM   3725 C  CA   . PRO   A 1 484 ? -6.344  16.092  -8.251  1.00 20.43  ?  486 PRO   A CA   1 
ATOM   3726 C  C    . PRO   A 1 484 ? -7.725  16.572  -7.805  1.00 19.70  ?  486 PRO   A C    1 
ATOM   3727 O  O    . PRO   A 1 484 ? -7.876  17.741  -7.570  1.00 19.36  ?  486 PRO   A O    1 
ATOM   3728 C  CB   . PRO   A 1 484 ? -6.307  15.939  -9.802  1.00 20.25  ?  486 PRO   A CB   1 
ATOM   3729 C  CG   . PRO   A 1 484 ? -5.405  14.800  -10.053 1.00 19.57  ?  486 PRO   A CG   1 
ATOM   3730 C  CD   . PRO   A 1 484 ? -5.617  13.865  -8.866  1.00 19.98  ?  486 PRO   A CD   1 
ATOM   3731 N  N    . CYS   A 1 485 ? -8.700  15.689  -7.629  1.00 20.89  ?  487 CYS   A N    1 
ATOM   3732 C  CA   . CYS   A 1 485 ? -10.015 16.143  -7.113  1.00 22.81  ?  487 CYS   A CA   1 
ATOM   3733 C  C    . CYS   A 1 485 ? -9.798  16.659  -5.654  1.00 23.60  ?  487 CYS   A C    1 
ATOM   3734 O  O    . CYS   A 1 485 ? -10.127 17.790  -5.304  1.00 22.67  ?  487 CYS   A O    1 
ATOM   3735 C  CB   . CYS   A 1 485 ? -11.078 15.011  -7.201  1.00 24.03  ?  487 CYS   A CB   1 
ATOM   3736 S  SG   . CYS   A 1 485 ? -12.694 15.356  -6.413  1.00 29.79  ?  487 CYS   A SG   1 
ATOM   3737 N  N    . PHE   A 1 486 ? -9.167  15.866  -4.823  1.00 22.17  ?  488 PHE   A N    1 
ATOM   3738 C  CA   . PHE   A 1 486 ? -8.813  16.374  -3.490  1.00 24.90  ?  488 PHE   A CA   1 
ATOM   3739 C  C    . PHE   A 1 486 ? -8.011  17.709  -3.557  1.00 24.19  ?  488 PHE   A C    1 
ATOM   3740 O  O    . PHE   A 1 486 ? -8.321  18.680  -2.869  1.00 25.17  ?  488 PHE   A O    1 
ATOM   3741 C  CB   . PHE   A 1 486 ? -8.073  15.321  -2.704  1.00 25.46  ?  488 PHE   A CB   1 
ATOM   3742 C  CG   . PHE   A 1 486 ? -8.960  14.282  -2.143  1.00 25.63  ?  488 PHE   A CG   1 
ATOM   3743 C  CD1  . PHE   A 1 486 ? -9.963  14.632  -1.230  1.00 28.21  ?  488 PHE   A CD1  1 
ATOM   3744 C  CD2  . PHE   A 1 486 ? -8.806  12.967  -2.487  1.00 26.28  ?  488 PHE   A CD2  1 
ATOM   3745 C  CE1  . PHE   A 1 486 ? -10.808 13.675  -0.685  1.00 27.67  ?  488 PHE   A CE1  1 
ATOM   3746 C  CE2  . PHE   A 1 486 ? -9.646  11.996  -1.953  1.00 27.77  ?  488 PHE   A CE2  1 
ATOM   3747 C  CZ   . PHE   A 1 486 ? -10.644 12.345  -1.044  1.00 28.61  ?  488 PHE   A CZ   1 
ATOM   3748 N  N    . SER   A 1 487 ? -7.097  17.808  -4.488  1.00 22.89  ?  489 SER   A N    1 
ATOM   3749 C  CA   . SER   A 1 487 ? -6.306  19.021  -4.602  1.00 23.57  ?  489 SER   A CA   1 
ATOM   3750 C  C    . SER   A 1 487 ? -7.105  20.212  -5.091  1.00 25.25  ?  489 SER   A C    1 
ATOM   3751 O  O    . SER   A 1 487 ? -6.680  21.345  -4.927  1.00 26.00  ?  489 SER   A O    1 
ATOM   3752 C  CB   . SER   A 1 487 ? -5.091  18.777  -5.488  1.00 22.52  ?  489 SER   A CB   1 
ATOM   3753 O  OG   . SER   A 1 487 ? -4.237  17.893  -4.822  1.00 22.25  ?  489 SER   A OG   1 
ATOM   3754 N  N    . ALA   A 1 488 ? -8.249  19.971  -5.713  1.00 30.84  ?  490 ALA   A N    1 
ATOM   3755 C  CA   . ALA   A 1 488 ? -9.124  21.074  -6.124  1.00 31.33  ?  490 ALA   A CA   1 
ATOM   3756 C  C    . ALA   A 1 488 ? -10.171 21.442  -5.058  1.00 30.19  ?  490 ALA   A C    1 
ATOM   3757 O  O    . ALA   A 1 488 ? -10.959 22.348  -5.272  1.00 30.14  ?  490 ALA   A O    1 
ATOM   3758 C  CB   . ALA   A 1 488 ? -9.781  20.738  -7.452  1.00 31.40  ?  490 ALA   A CB   1 
ATOM   3759 N  N    . LEU   A 1 489 ? -10.208 20.730  -3.931  1.00 32.34  ?  491 LEU   A N    1 
ATOM   3760 C  CA   . LEU   A 1 489 ? -11.055 21.139  -2.800  1.00 31.51  ?  491 LEU   A CA   1 
ATOM   3761 C  C    . LEU   A 1 489 ? -10.569 22.494  -2.314  1.00 32.31  ?  491 LEU   A C    1 
ATOM   3762 O  O    . LEU   A 1 489 ? -9.376  22.687  -2.106  1.00 28.33  ?  491 LEU   A O    1 
ATOM   3763 C  CB   . LEU   A 1 489 ? -11.002 20.166  -1.629  1.00 30.79  ?  491 LEU   A CB   1 
ATOM   3764 C  CG   . LEU   A 1 489 ? -11.469 18.733  -1.871  1.00 31.44  ?  491 LEU   A CG   1 
ATOM   3765 C  CD1  . LEU   A 1 489 ? -11.537 18.058  -0.517  1.00 32.16  ?  491 LEU   A CD1  1 
ATOM   3766 C  CD2  . LEU   A 1 489 ? -12.792 18.670  -2.621  1.00 30.35  ?  491 LEU   A CD2  1 
ATOM   3767 N  N    . GLU   A 1 490 ? -11.522 23.416  -2.228  1.00 37.33  ?  492 GLU   A N    1 
ATOM   3768 C  CA   . GLU   A 1 490 ? -11.338 24.778  -1.734  1.00 38.72  ?  492 GLU   A CA   1 
ATOM   3769 C  C    . GLU   A 1 490 ? -11.811 24.803  -0.300  1.00 34.37  ?  492 GLU   A C    1 
ATOM   3770 O  O    . GLU   A 1 490 ? -12.328 23.787  0.213   1.00 31.91  ?  492 GLU   A O    1 
ATOM   3771 C  CB   . GLU   A 1 490 ? -12.129 25.754  -2.622  1.00 44.50  ?  492 GLU   A CB   1 
ATOM   3772 C  CG   . GLU   A 1 490 ? -11.674 25.688  -4.097  1.00 51.13  ?  492 GLU   A CG   1 
ATOM   3773 C  CD   . GLU   A 1 490 ? -12.436 26.606  -5.038  1.00 57.28  ?  492 GLU   A CD   1 
ATOM   3774 O  OE1  . GLU   A 1 490 ? -13.678 26.722  -4.900  1.00 63.57  ?  492 GLU   A OE1  1 
ATOM   3775 O  OE2  . GLU   A 1 490 ? -11.789 27.195  -5.933  1.00 59.32  ?  492 GLU   A OE2  1 
ATOM   3776 N  N    . VAL   A 1 491 ? -11.606 25.938  0.362   1.00 28.60  ?  493 VAL   A N    1 
ATOM   3777 C  CA   . VAL   A 1 491 ? -12.098 26.132  1.715   1.00 28.37  ?  493 VAL   A CA   1 
ATOM   3778 C  C    . VAL   A 1 491 ? -13.643 26.096  1.675   1.00 28.51  ?  493 VAL   A C    1 
ATOM   3779 O  O    . VAL   A 1 491 ? -14.254 26.612  0.754   1.00 27.13  ?  493 VAL   A O    1 
ATOM   3780 C  CB   . VAL   A 1 491 ? -11.562 27.433  2.347   1.00 27.09  ?  493 VAL   A CB   1 
ATOM   3781 C  CG1  . VAL   A 1 491 ? -12.273 27.717  3.671   1.00 27.23  ?  493 VAL   A CG1  1 
ATOM   3782 C  CG2  . VAL   A 1 491 ? -10.052 27.319  2.552   1.00 26.75  ?  493 VAL   A CG2  1 
ATOM   3783 N  N    . ASP   A 1 492 ? -14.249 25.429  2.650   1.00 31.49  ?  494 ASP   A N    1 
ATOM   3784 C  CA   . ASP   A 1 492 ? -15.697 25.161  2.601   1.00 32.41  ?  494 ASP   A CA   1 
ATOM   3785 C  C    . ASP   A 1 492 ? -16.442 26.403  3.022   1.00 32.38  ?  494 ASP   A C    1 
ATOM   3786 O  O    . ASP   A 1 492 ? -16.320 26.811  4.162   1.00 31.65  ?  494 ASP   A O    1 
ATOM   3787 C  CB   . ASP   A 1 492 ? -16.066 24.005  3.526   1.00 32.42  ?  494 ASP   A CB   1 
ATOM   3788 C  CG   . ASP   A 1 492 ? -17.470 23.481  3.273   1.00 34.06  ?  494 ASP   A CG   1 
ATOM   3789 O  OD1  . ASP   A 1 492 ? -18.338 24.246  2.816   1.00 28.38  ?  494 ASP   A OD1  1 
ATOM   3790 O  OD2  . ASP   A 1 492 ? -17.682 22.276  3.534   1.00 41.73  ?  494 ASP   A OD2  1 
ATOM   3791 N  N    . GLU   A 1 493 ? -17.178 27.012  2.100   1.00 34.42  ?  495 GLU   A N    1 
ATOM   3792 C  CA   . GLU   A 1 493 ? -17.889 28.274  2.382   1.00 39.04  ?  495 GLU   A CA   1 
ATOM   3793 C  C    . GLU   A 1 493 ? -19.248 28.014  3.058   1.00 41.16  ?  495 GLU   A C    1 
ATOM   3794 O  O    . GLU   A 1 493 ? -19.736 28.845  3.815   1.00 45.57  ?  495 GLU   A O    1 
ATOM   3795 C  CB   . GLU   A 1 493 ? -18.078 29.072  1.083   1.00 38.64  ?  495 GLU   A CB   1 
ATOM   3796 N  N    . THR   A 1 494 ? -19.849 26.857  2.780   1.00 43.17  ?  496 THR   A N    1 
ATOM   3797 C  CA   . THR   A 1 494 ? -21.125 26.443  3.380   1.00 43.59  ?  496 THR   A CA   1 
ATOM   3798 C  C    . THR   A 1 494 ? -21.077 26.279  4.904   1.00 41.40  ?  496 THR   A C    1 
ATOM   3799 O  O    . THR   A 1 494 ? -22.068 26.529  5.584   1.00 44.76  ?  496 THR   A O    1 
ATOM   3800 C  CB   . THR   A 1 494 ? -21.572 25.088  2.772   1.00 46.34  ?  496 THR   A CB   1 
ATOM   3801 O  OG1  . THR   A 1 494 ? -21.763 25.255  1.369   1.00 52.21  ?  496 THR   A OG1  1 
ATOM   3802 C  CG2  . THR   A 1 494 ? -22.875 24.579  3.370   1.00 49.20  ?  496 THR   A CG2  1 
ATOM   3803 N  N    . TYR   A 1 495 ? -19.924 25.879  5.430   1.00 37.42  ?  497 TYR   A N    1 
ATOM   3804 C  CA   . TYR   A 1 495 ? -19.846 25.267  6.747   1.00 36.06  ?  497 TYR   A CA   1 
ATOM   3805 C  C    . TYR   A 1 495 ? -20.183 26.219  7.871   1.00 36.70  ?  497 TYR   A C    1 
ATOM   3806 O  O    . TYR   A 1 495 ? -19.679 27.341  7.923   1.00 38.85  ?  497 TYR   A O    1 
ATOM   3807 C  CB   . TYR   A 1 495 ? -18.455 24.661  6.992   1.00 33.52  ?  497 TYR   A CB   1 
ATOM   3808 C  CG   . TYR   A 1 495 ? -18.192 24.094  8.389   1.00 31.07  ?  497 TYR   A CG   1 
ATOM   3809 C  CD1  . TYR   A 1 495 ? -18.670 22.836  8.763   1.00 29.99  ?  497 TYR   A CD1  1 
ATOM   3810 C  CD2  . TYR   A 1 495 ? -17.426 24.795  9.298   1.00 29.53  ?  497 TYR   A CD2  1 
ATOM   3811 C  CE1  . TYR   A 1 495 ? -18.405 22.308  10.024  1.00 32.72  ?  497 TYR   A CE1  1 
ATOM   3812 C  CE2  . TYR   A 1 495 ? -17.167 24.290  10.561  1.00 32.37  ?  497 TYR   A CE2  1 
ATOM   3813 C  CZ   . TYR   A 1 495 ? -17.645 23.046  10.924  1.00 32.05  ?  497 TYR   A CZ   1 
ATOM   3814 O  OH   . TYR   A 1 495 ? -17.344 22.542  12.170  1.00 34.70  ?  497 TYR   A OH   1 
ATOM   3815 N  N    . VAL   A 1 496 ? -20.999 25.717  8.791   1.00 35.31  ?  498 VAL   A N    1 
ATOM   3816 C  CA   . VAL   A 1 496 ? -21.405 26.489  9.947   1.00 36.87  ?  498 VAL   A CA   1 
ATOM   3817 C  C    . VAL   A 1 496 ? -20.452 26.108  11.090  1.00 34.22  ?  498 VAL   A C    1 
ATOM   3818 O  O    . VAL   A 1 496 ? -20.353 24.927  11.431  1.00 31.62  ?  498 VAL   A O    1 
ATOM   3819 C  CB   . VAL   A 1 496 ? -22.920 26.364  10.263  1.00 35.42  ?  498 VAL   A CB   1 
ATOM   3820 C  CG1  . VAL   A 1 496 ? -23.691 27.293  9.334   1.00 35.88  ?  498 VAL   A CG1  1 
ATOM   3821 C  CG2  . VAL   A 1 496 ? -23.448 24.931  10.123  1.00 36.63  ?  498 VAL   A CG2  1 
ATOM   3822 N  N    . PRO   A 1 497 ? -19.694 27.096  11.624  1.00 31.09  ?  499 PRO   A N    1 
ATOM   3823 C  CA   . PRO   A 1 497 ? -18.801 26.872  12.760  1.00 32.47  ?  499 PRO   A CA   1 
ATOM   3824 C  C    . PRO   A 1 497 ? -19.399 25.916  13.786  1.00 35.04  ?  499 PRO   A C    1 
ATOM   3825 O  O    . PRO   A 1 497 ? -20.582 26.061  14.130  1.00 35.52  ?  499 PRO   A O    1 
ATOM   3826 C  CB   . PRO   A 1 497 ? -18.658 28.293  13.361  1.00 30.82  ?  499 PRO   A CB   1 
ATOM   3827 C  CG   . PRO   A 1 497 ? -18.700 29.185  12.172  1.00 30.00  ?  499 PRO   A CG   1 
ATOM   3828 C  CD   . PRO   A 1 497 ? -19.645 28.510  11.193  1.00 30.69  ?  499 PRO   A CD   1 
ATOM   3829 N  N    . LYS   A 1 498 ? -18.628 24.933  14.253  1.00 35.73  ?  500 LYS   A N    1 
ATOM   3830 C  CA   . LYS   A 1 498 ? -19.067 24.207  15.430  1.00 38.85  ?  500 LYS   A CA   1 
ATOM   3831 C  C    . LYS   A 1 498 ? -19.106 25.148  16.618  1.00 41.41  ?  500 LYS   A C    1 
ATOM   3832 O  O    . LYS   A 1 498 ? -18.304 26.094  16.717  1.00 41.66  ?  500 LYS   A O    1 
ATOM   3833 C  CB   . LYS   A 1 498 ? -18.233 22.953  15.745  1.00 40.08  ?  500 LYS   A CB   1 
ATOM   3834 C  CG   . LYS   A 1 498 ? -16.819 23.143  16.289  1.00 40.04  ?  500 LYS   A CG   1 
ATOM   3835 C  CD   . LYS   A 1 498 ? -16.286 21.919  17.062  1.00 38.45  ?  500 LYS   A CD   1 
ATOM   3836 C  CE   . LYS   A 1 498 ? -16.787 20.564  16.553  1.00 35.86  ?  500 LYS   A CE   1 
ATOM   3837 N  NZ   . LYS   A 1 498 ? -16.429 19.415  17.438  1.00 34.50  ?  500 LYS   A NZ   1 
ATOM   3838 N  N    . GLU   A 1 499 ? -20.041 24.853  17.514  1.00 44.15  ?  501 GLU   A N    1 
ATOM   3839 C  CA   . GLU   A 1 499 ? -20.355 25.697  18.672  1.00 48.01  ?  501 GLU   A CA   1 
ATOM   3840 C  C    . GLU   A 1 499 ? -19.269 25.550  19.740  1.00 46.49  ?  501 GLU   A C    1 
ATOM   3841 O  O    . GLU   A 1 499 ? -18.574 24.524  19.765  1.00 43.33  ?  501 GLU   A O    1 
ATOM   3842 C  CB   . GLU   A 1 499 ? -21.742 25.311  19.225  1.00 48.19  ?  501 GLU   A CB   1 
ATOM   3843 C  CG   . GLU   A 1 499 ? -22.522 26.481  19.810  1.00 54.03  ?  501 GLU   A CG   1 
ATOM   3844 C  CD   . GLU   A 1 499 ? -24.003 26.506  19.439  1.00 55.83  ?  501 GLU   A CD   1 
ATOM   3845 O  OE1  . GLU   A 1 499 ? -24.588 25.425  19.178  1.00 53.50  ?  501 GLU   A OE1  1 
ATOM   3846 O  OE2  . GLU   A 1 499 ? -24.583 27.623  19.435  1.00 52.56  ?  501 GLU   A OE2  1 
ATOM   3847 N  N    . PHE   A 1 500 ? -19.130 26.556  20.609  1.00 47.62  ?  502 PHE   A N    1 
ATOM   3848 C  CA   . PHE   A 1 500 ? -18.103 26.518  21.671  1.00 51.21  ?  502 PHE   A CA   1 
ATOM   3849 C  C    . PHE   A 1 500 ? -18.342 25.393  22.684  1.00 50.43  ?  502 PHE   A C    1 
ATOM   3850 O  O    . PHE   A 1 500 ? -19.480 25.059  23.002  1.00 49.65  ?  502 PHE   A O    1 
ATOM   3851 C  CB   . PHE   A 1 500 ? -17.970 27.843  22.421  1.00 50.95  ?  502 PHE   A CB   1 
ATOM   3852 C  CG   . PHE   A 1 500 ? -16.807 27.862  23.386  1.00 55.78  ?  502 PHE   A CG   1 
ATOM   3853 C  CD1  . PHE   A 1 500 ? -15.502 28.077  22.930  1.00 57.95  ?  502 PHE   A CD1  1 
ATOM   3854 C  CD2  . PHE   A 1 500 ? -17.002 27.614  24.741  1.00 58.97  ?  502 PHE   A CD2  1 
ATOM   3855 C  CE1  . PHE   A 1 500 ? -14.424 28.080  23.811  1.00 57.34  ?  502 PHE   A CE1  1 
ATOM   3856 C  CE2  . PHE   A 1 500 ? -15.925 27.602  25.624  1.00 60.26  ?  502 PHE   A CE2  1 
ATOM   3857 C  CZ   . PHE   A 1 500 ? -14.637 27.842  25.159  1.00 59.25  ?  502 PHE   A CZ   1 
ATOM   3858 N  N    . ASN   A 1 501 ? -17.249 24.814  23.168  1.00 49.29  ?  503 ASN   A N    1 
ATOM   3859 C  CA   . ASN   A 1 501 ? -17.303 23.668  24.067  1.00 49.42  ?  503 ASN   A CA   1 
ATOM   3860 C  C    . ASN   A 1 501 ? -16.021 23.674  24.890  1.00 46.14  ?  503 ASN   A C    1 
ATOM   3861 O  O    . ASN   A 1 501 ? -14.958 23.292  24.405  1.00 44.51  ?  503 ASN   A O    1 
ATOM   3862 C  CB   . ASN   A 1 501 ? -17.459 22.389  23.235  1.00 50.86  ?  503 ASN   A CB   1 
ATOM   3863 C  CG   . ASN   A 1 501 ? -17.712 21.156  24.079  1.00 51.42  ?  503 ASN   A CG   1 
ATOM   3864 O  OD1  . ASN   A 1 501 ? -17.557 21.168  25.300  1.00 56.78  ?  503 ASN   A OD1  1 
ATOM   3865 N  ND2  . ASN   A 1 501 ? -18.094 20.076  23.422  1.00 52.61  ?  503 ASN   A ND2  1 
ATOM   3866 N  N    . ALA   A 1 502 ? -16.138 24.122  26.134  1.00 46.28  ?  504 ALA   A N    1 
ATOM   3867 C  CA   . ALA   A 1 502 ? -14.965 24.501  26.945  1.00 46.14  ?  504 ALA   A CA   1 
ATOM   3868 C  C    . ALA   A 1 502 ? -14.072 23.335  27.327  1.00 43.37  ?  504 ALA   A C    1 
ATOM   3869 O  O    . ALA   A 1 502 ? -12.873 23.529  27.490  1.00 40.92  ?  504 ALA   A O    1 
ATOM   3870 C  CB   . ALA   A 1 502 ? -15.401 25.238  28.207  1.00 50.30  ?  504 ALA   A CB   1 
ATOM   3871 N  N    . GLU   A 1 503 ? -14.653 22.137  27.476  1.00 42.17  ?  505 GLU   A N    1 
ATOM   3872 C  CA   . GLU   A 1 503 ? -13.871 20.928  27.802  1.00 40.64  ?  505 GLU   A CA   1 
ATOM   3873 C  C    . GLU   A 1 503 ? -12.863 20.653  26.698  1.00 40.81  ?  505 GLU   A C    1 
ATOM   3874 O  O    . GLU   A 1 503 ? -11.709 20.348  26.992  1.00 46.68  ?  505 GLU   A O    1 
ATOM   3875 C  CB   . GLU   A 1 503 ? -14.766 19.695  28.021  1.00 41.34  ?  505 GLU   A CB   1 
ATOM   3876 N  N    . THR   A 1 504 ? -13.282 20.821  25.437  1.00 40.13  ?  506 THR   A N    1 
ATOM   3877 C  CA   . THR   A 1 504 ? -12.390 20.661  24.280  1.00 37.75  ?  506 THR   A CA   1 
ATOM   3878 C  C    . THR   A 1 504 ? -11.101 21.472  24.395  1.00 36.50  ?  506 THR   A C    1 
ATOM   3879 O  O    . THR   A 1 504 ? -10.036 20.979  24.030  1.00 35.72  ?  506 THR   A O    1 
ATOM   3880 C  CB   . THR   A 1 504 ? -13.087 21.019  22.939  1.00 36.33  ?  506 THR   A CB   1 
ATOM   3881 O  OG1  . THR   A 1 504 ? -14.306 20.282  22.808  1.00 32.33  ?  506 THR   A OG1  1 
ATOM   3882 C  CG2  . THR   A 1 504 ? -12.185 20.697  21.769  1.00 34.70  ?  506 THR   A CG2  1 
ATOM   3883 N  N    . PHE   A 1 505 ? -11.196 22.698  24.917  1.00 38.91  ?  507 PHE   A N    1 
ATOM   3884 C  CA   . PHE   A 1 505 ? -10.020 23.569  25.086  1.00 39.61  ?  507 PHE   A CA   1 
ATOM   3885 C  C    . PHE   A 1 505 ? -9.665  23.745  26.572  1.00 42.63  ?  507 PHE   A C    1 
ATOM   3886 O  O    . PHE   A 1 505 ? -9.291  24.839  26.985  1.00 41.44  ?  507 PHE   A O    1 
ATOM   3887 C  CB   . PHE   A 1 505 ? -10.263 24.925  24.407  1.00 41.10  ?  507 PHE   A CB   1 
ATOM   3888 C  CG   . PHE   A 1 505 ? -10.883 24.817  23.037  1.00 39.26  ?  507 PHE   A CG   1 
ATOM   3889 C  CD1  . PHE   A 1 505 ? -12.266 24.774  22.884  1.00 39.79  ?  507 PHE   A CD1  1 
ATOM   3890 C  CD2  . PHE   A 1 505 ? -10.095 24.745  21.913  1.00 38.10  ?  507 PHE   A CD2  1 
ATOM   3891 C  CE1  . PHE   A 1 505 ? -12.834 24.668  21.623  1.00 38.09  ?  507 PHE   A CE1  1 
ATOM   3892 C  CE2  . PHE   A 1 505 ? -10.653 24.641  20.656  1.00 35.37  ?  507 PHE   A CE2  1 
ATOM   3893 C  CZ   . PHE   A 1 505 ? -12.019 24.597  20.510  1.00 37.13  ?  507 PHE   A CZ   1 
ATOM   3894 N  N    . THR   A 1 506 ? -9.797  22.664  27.354  1.00 44.26  ?  508 THR   A N    1 
ATOM   3895 C  CA   . THR   A 1 506 ? -9.317  22.587  28.750  1.00 47.52  ?  508 THR   A CA   1 
ATOM   3896 C  C    . THR   A 1 506 ? -8.202  21.535  28.782  1.00 49.30  ?  508 THR   A C    1 
ATOM   3897 O  O    . THR   A 1 506 ? -8.411  20.422  28.319  1.00 52.14  ?  508 THR   A O    1 
ATOM   3898 C  CB   . THR   A 1 506 ? -10.457 22.164  29.709  1.00 45.04  ?  508 THR   A CB   1 
ATOM   3899 O  OG1  . THR   A 1 506 ? -11.516 23.111  29.616  1.00 42.23  ?  508 THR   A OG1  1 
ATOM   3900 C  CG2  . THR   A 1 506 ? -10.000 22.095  31.163  1.00 45.70  ?  508 THR   A CG2  1 
ATOM   3901 N  N    . PHE   A 1 507 ? -7.030  21.896  29.305  1.00 50.85  ?  509 PHE   A N    1 
ATOM   3902 C  CA   . PHE   A 1 507 ? -5.867  21.003  29.354  1.00 54.03  ?  509 PHE   A CA   1 
ATOM   3903 C  C    . PHE   A 1 507 ? -5.313  20.913  30.770  1.00 55.02  ?  509 PHE   A C    1 
ATOM   3904 O  O    . PHE   A 1 507 ? -5.213  21.944  31.439  1.00 55.27  ?  509 PHE   A O    1 
ATOM   3905 C  CB   . PHE   A 1 507 ? -4.775  21.540  28.445  1.00 58.53  ?  509 PHE   A CB   1 
ATOM   3906 C  CG   . PHE   A 1 507 ? -5.278  21.982  27.115  1.00 61.03  ?  509 PHE   A CG   1 
ATOM   3907 C  CD1  . PHE   A 1 507 ? -5.691  23.302  26.922  1.00 59.08  ?  509 PHE   A CD1  1 
ATOM   3908 C  CD2  . PHE   A 1 507 ? -5.381  21.072  26.062  1.00 60.45  ?  509 PHE   A CD2  1 
ATOM   3909 C  CE1  . PHE   A 1 507 ? -6.176  23.715  25.691  1.00 60.30  ?  509 PHE   A CE1  1 
ATOM   3910 C  CE2  . PHE   A 1 507 ? -5.860  21.484  24.825  1.00 60.75  ?  509 PHE   A CE2  1 
ATOM   3911 C  CZ   . PHE   A 1 507 ? -6.261  22.809  24.641  1.00 59.48  ?  509 PHE   A CZ   1 
ATOM   3912 N  N    . HIS   A 1 508 ? -4.923  19.707  31.208  1.00 52.02  ?  510 HIS   A N    1 
ATOM   3913 C  CA   . HIS   A 1 508 ? -4.432  19.493  32.590  1.00 52.26  ?  510 HIS   A CA   1 
ATOM   3914 C  C    . HIS   A 1 508 ? -2.926  19.166  32.644  1.00 51.87  ?  510 HIS   A C    1 
ATOM   3915 O  O    . HIS   A 1 508 ? -2.266  19.087  31.612  1.00 53.92  ?  510 HIS   A O    1 
ATOM   3916 C  CB   . HIS   A 1 508 ? -5.255  18.410  33.300  1.00 51.16  ?  510 HIS   A CB   1 
ATOM   3917 C  CG   . HIS   A 1 508 ? -6.733  18.557  33.128  1.00 50.81  ?  510 HIS   A CG   1 
ATOM   3918 N  ND1  . HIS   A 1 508 ? -7.450  19.577  33.714  1.00 48.80  ?  510 HIS   A ND1  1 
ATOM   3919 C  CD2  . HIS   A 1 508 ? -7.632  17.800  32.454  1.00 48.81  ?  510 HIS   A CD2  1 
ATOM   3920 C  CE1  . HIS   A 1 508 ? -8.727  19.450  33.399  1.00 48.82  ?  510 HIS   A CE1  1 
ATOM   3921 N  NE2  . HIS   A 1 508 ? -8.863  18.385  32.630  1.00 47.79  ?  510 HIS   A NE2  1 
ATOM   3922 N  N    . ALA   A 1 509 ? -2.386  18.987  33.847  1.00 52.47  ?  511 ALA   A N    1 
ATOM   3923 C  CA   . ALA   A 1 509 ? -0.947  18.675  34.020  1.00 52.54  ?  511 ALA   A CA   1 
ATOM   3924 C  C    . ALA   A 1 509 ? -0.552  17.310  33.448  1.00 51.60  ?  511 ALA   A C    1 
ATOM   3925 O  O    . ALA   A 1 509 ? 0.614   17.094  33.131  1.00 47.92  ?  511 ALA   A O    1 
ATOM   3926 C  CB   . ALA   A 1 509 ? -0.544  18.765  35.491  1.00 52.51  ?  511 ALA   A CB   1 
ATOM   3927 N  N    . ASP   A 1 510 ? -1.519  16.400  33.306  1.00 53.14  ?  512 ASP   A N    1 
ATOM   3928 C  CA   . ASP   A 1 510 ? -1.313  15.139  32.565  1.00 52.60  ?  512 ASP   A CA   1 
ATOM   3929 C  C    . ASP   A 1 510 ? -0.439  15.269  31.280  1.00 50.49  ?  512 ASP   A C    1 
ATOM   3930 O  O    . ASP   A 1 510 ? 0.364   14.380  31.003  1.00 47.78  ?  512 ASP   A O    1 
ATOM   3931 C  CB   . ASP   A 1 510 ? -2.671  14.443  32.271  1.00 51.41  ?  512 ASP   A CB   1 
ATOM   3932 C  CG   . ASP   A 1 510 ? -3.614  15.279  31.365  1.00 53.73  ?  512 ASP   A CG   1 
ATOM   3933 O  OD1  . ASP   A 1 510 ? -3.458  16.521  31.257  1.00 48.77  ?  512 ASP   A OD1  1 
ATOM   3934 O  OD2  . ASP   A 1 510 ? -4.519  14.676  30.746  1.00 48.05  ?  512 ASP   A OD2  1 
ATOM   3935 N  N    . ILE   A 1 511 ? -0.547  16.389  30.553  1.00 49.62  ?  513 ILE   A N    1 
ATOM   3936 C  CA   . ILE   A 1 511 ? 0.145   16.568  29.250  1.00 50.88  ?  513 ILE   A CA   1 
ATOM   3937 C  C    . ILE   A 1 511 ? 1.684   16.701  29.275  1.00 50.31  ?  513 ILE   A C    1 
ATOM   3938 O  O    . ILE   A 1 511 ? 2.328   16.292  28.309  1.00 51.28  ?  513 ILE   A O    1 
ATOM   3939 C  CB   . ILE   A 1 511 ? -0.463  17.719  28.396  1.00 51.76  ?  513 ILE   A CB   1 
ATOM   3940 C  CG1  . ILE   A 1 511 ? -0.104  19.085  28.968  1.00 48.10  ?  513 ILE   A CG1  1 
ATOM   3941 C  CG2  . ILE   A 1 511 ? -1.977  17.548  28.261  1.00 54.67  ?  513 ILE   A CG2  1 
ATOM   3942 C  CD1  . ILE   A 1 511 ? -0.848  20.213  28.306  1.00 53.71  ?  513 ILE   A CD1  1 
ATOM   3943 N  N    . CYS   A 1 512 ? 2.273   17.251  30.348  1.00 51.98  ?  514 CYS   A N    1 
ATOM   3944 C  CA   . CYS   A 1 512 ? 3.749   17.372  30.436  1.00 50.22  ?  514 CYS   A CA   1 
ATOM   3945 C  C    . CYS   A 1 512 ? 4.451   16.066  30.770  1.00 50.39  ?  514 CYS   A C    1 
ATOM   3946 O  O    . CYS   A 1 512 ? 5.679   15.980  30.630  1.00 50.22  ?  514 CYS   A O    1 
ATOM   3947 C  CB   . CYS   A 1 512 ? 4.189   18.421  31.457  1.00 51.31  ?  514 CYS   A CB   1 
ATOM   3948 S  SG   . CYS   A 1 512 ? 2.976   19.713  31.678  1.00 46.71  ?  514 CYS   A SG   1 
ATOM   3949 N  N    . THR   A 1 513 ? 3.701   15.068  31.237  1.00 51.53  ?  515 THR   A N    1 
ATOM   3950 C  CA   . THR   A 1 513 ? 4.267   13.727  31.480  1.00 52.16  ?  515 THR   A CA   1 
ATOM   3951 C  C    . THR   A 1 513 ? 3.969   12.734  30.355  1.00 51.82  ?  515 THR   A C    1 
ATOM   3952 O  O    . THR   A 1 513 ? 4.655   11.706  30.248  1.00 46.29  ?  515 THR   A O    1 
ATOM   3953 C  CB   . THR   A 1 513 ? 3.756   13.126  32.793  1.00 51.39  ?  515 THR   A CB   1 
ATOM   3954 O  OG1  . THR   A 1 513 ? 2.341   12.918  32.709  1.00 46.11  ?  515 THR   A OG1  1 
ATOM   3955 C  CG2  . THR   A 1 513 ? 4.087   14.051  33.956  1.00 54.87  ?  515 THR   A CG2  1 
ATOM   3956 N  N    . LEU   A 1 514 ? 2.945   13.031  29.537  1.00 51.90  ?  516 LEU   A N    1 
ATOM   3957 C  CA   . LEU   A 1 514 ? 2.622   12.208  28.376  1.00 49.56  ?  516 LEU   A CA   1 
ATOM   3958 C  C    . LEU   A 1 514 ? 3.855   12.113  27.480  1.00 44.33  ?  516 LEU   A C    1 
ATOM   3959 O  O    . LEU   A 1 514 ? 4.725   12.976  27.491  1.00 38.68  ?  516 LEU   A O    1 
ATOM   3960 C  CB   . LEU   A 1 514 ? 1.416   12.767  27.588  1.00 50.85  ?  516 LEU   A CB   1 
ATOM   3961 C  CG   . LEU   A 1 514 ? -0.014  12.553  28.148  1.00 51.86  ?  516 LEU   A CG   1 
ATOM   3962 C  CD1  . LEU   A 1 514 ? -1.042  13.420  27.424  1.00 51.21  ?  516 LEU   A CD1  1 
ATOM   3963 C  CD2  . LEU   A 1 514 ? -0.453  11.088  28.120  1.00 49.38  ?  516 LEU   A CD2  1 
ATOM   3964 N  N    . SER   A 1 515 ? 3.939   11.031  26.724  1.00 45.87  ?  517 SER   A N    1 
ATOM   3965 C  CA   . SER   A 1 515 ? 4.993   10.893  25.731  1.00 45.97  ?  517 SER   A CA   1 
ATOM   3966 C  C    . SER   A 1 515 ? 4.895   11.998  24.667  1.00 45.98  ?  517 SER   A C    1 
ATOM   3967 O  O    . SER   A 1 515 ? 3.808   12.566  24.451  1.00 43.90  ?  517 SER   A O    1 
ATOM   3968 C  CB   . SER   A 1 515 ? 4.892   9.535   25.066  1.00 43.82  ?  517 SER   A CB   1 
ATOM   3969 O  OG   . SER   A 1 515 ? 3.683   9.448   24.351  1.00 44.34  ?  517 SER   A OG   1 
ATOM   3970 N  N    . GLU   A 1 516 ? 6.049   12.293  24.051  1.00 45.15  ?  518 GLU   A N    1 
ATOM   3971 C  CA   . GLU   A 1 516 ? 6.202   13.181  22.882  1.00 45.03  ?  518 GLU   A CA   1 
ATOM   3972 C  C    . GLU   A 1 516 ? 5.084   13.026  21.850  1.00 40.61  ?  518 GLU   A C    1 
ATOM   3973 O  O    . GLU   A 1 516 ? 4.398   13.995  21.526  1.00 36.60  ?  518 GLU   A O    1 
ATOM   3974 C  CB   . GLU   A 1 516 ? 7.550   12.911  22.198  1.00 45.40  ?  518 GLU   A CB   1 
ATOM   3975 N  N    . LYS   A 1 517 ? 4.885   11.798  21.391  1.00 41.04  ?  519 LYS   A N    1 
ATOM   3976 C  CA   . LYS   A 1 517 ? 3.803   11.480  20.472  1.00 45.82  ?  519 LYS   A CA   1 
ATOM   3977 C  C    . LYS   A 1 517 ? 2.464   11.903  21.029  1.00 47.14  ?  519 LYS   A C    1 
ATOM   3978 O  O    . LYS   A 1 517 ? 1.759   12.676  20.401  1.00 47.15  ?  519 LYS   A O    1 
ATOM   3979 C  CB   . LYS   A 1 517 ? 3.771   9.986   20.145  1.00 47.99  ?  519 LYS   A CB   1 
ATOM   3980 C  CG   . LYS   A 1 517 ? 2.710   9.589   19.113  1.00 46.64  ?  519 LYS   A CG   1 
ATOM   3981 C  CD   . LYS   A 1 517 ? 3.088   8.338   18.323  1.00 47.50  ?  519 LYS   A CD   1 
ATOM   3982 N  N    . GLU   A 1 518 ? 2.135   11.412  22.221  1.00 49.92  ?  520 GLU   A N    1 
ATOM   3983 C  CA   . GLU   A 1 518 ? 0.834   11.660  22.852  1.00 46.63  ?  520 GLU   A CA   1 
ATOM   3984 C  C    . GLU   A 1 518 ? 0.556   13.140  23.126  1.00 43.38  ?  520 GLU   A C    1 
ATOM   3985 O  O    . GLU   A 1 518 ? -0.609  13.536  23.198  1.00 43.32  ?  520 GLU   A O    1 
ATOM   3986 C  CB   . GLU   A 1 518 ? 0.728   10.906  24.183  1.00 53.95  ?  520 GLU   A CB   1 
ATOM   3987 C  CG   . GLU   A 1 518 ? 0.693   9.387   24.073  1.00 62.64  ?  520 GLU   A CG   1 
ATOM   3988 C  CD   . GLU   A 1 518 ? -0.708  8.822   23.919  1.00 71.68  ?  520 GLU   A CD   1 
ATOM   3989 O  OE1  . GLU   A 1 518 ? -1.579  9.101   24.792  1.00 75.51  ?  520 GLU   A OE1  1 
ATOM   3990 O  OE2  . GLU   A 1 518 ? -0.928  8.086   22.923  1.00 78.31  ?  520 GLU   A OE2  1 
ATOM   3991 N  N    . ARG   A 1 519 ? 1.609   13.930  23.321  1.00 37.81  ?  521 ARG   A N    1 
ATOM   3992 C  CA   . ARG   A 1 519 ? 1.481   15.364  23.585  1.00 38.78  ?  521 ARG   A CA   1 
ATOM   3993 C  C    . ARG   A 1 519 ? 1.210   16.056  22.256  1.00 38.31  ?  521 ARG   A C    1 
ATOM   3994 O  O    . ARG   A 1 519 ? 0.403   16.966  22.175  1.00 42.42  ?  521 ARG   A O    1 
ATOM   3995 C  CB   . ARG   A 1 519 ? 2.768   15.915  24.216  1.00 40.55  ?  521 ARG   A CB   1 
ATOM   3996 C  CG   . ARG   A 1 519 ? 2.616   17.150  25.116  1.00 41.75  ?  521 ARG   A CG   1 
ATOM   3997 C  CD   . ARG   A 1 519 ? 3.953   17.494  25.789  1.00 41.27  ?  521 ARG   A CD   1 
ATOM   3998 N  NE   . ARG   A 1 519 ? 4.557   16.338  26.477  1.00 42.75  ?  521 ARG   A NE   1 
ATOM   3999 N  N    . GLN   A 1 520 ? 1.884   15.579  21.216  1.00 37.69  ?  522 GLN   A N    1 
ATOM   4000 C  CA   . GLN   A 1 520 ? 1.681   16.062  19.866  1.00 34.92  ?  522 GLN   A CA   1 
ATOM   4001 C  C    . GLN   A 1 520 ? 0.278   15.790  19.395  1.00 33.16  ?  522 GLN   A C    1 
ATOM   4002 O  O    . GLN   A 1 520 ? -0.384  16.737  18.936  1.00 31.95  ?  522 GLN   A O    1 
ATOM   4003 C  CB   . GLN   A 1 520 ? 2.694   15.479  18.901  1.00 34.33  ?  522 GLN   A CB   1 
ATOM   4004 C  CG   . GLN   A 1 520 ? 4.083   16.082  19.045  1.00 37.26  ?  522 GLN   A CG   1 
ATOM   4005 C  CD   . GLN   A 1 520 ? 5.118   15.337  18.223  1.00 40.56  ?  522 GLN   A CD   1 
ATOM   4006 O  OE1  . GLN   A 1 520 ? 4.851   14.246  17.719  1.00 50.30  ?  522 GLN   A OE1  1 
ATOM   4007 N  NE2  . GLN   A 1 520 ? 6.302   15.918  18.079  1.00 39.11  ?  522 GLN   A NE2  1 
ATOM   4008 N  N    . ILE   A 1 521 ? -0.192  14.546  19.549  1.00 30.01  ?  523 ILE   A N    1 
ATOM   4009 C  CA   . ILE   A 1 521 ? -1.578  14.206  19.161  1.00 32.02  ?  523 ILE   A CA   1 
ATOM   4010 C  C    . ILE   A 1 521 ? -2.625  15.023  19.888  1.00 33.47  ?  523 ILE   A C    1 
ATOM   4011 O  O    . ILE   A 1 521 ? -3.626  15.423  19.271  1.00 31.68  ?  523 ILE   A O    1 
ATOM   4012 C  CB   . ILE   A 1 521 ? -2.024  12.745  19.436  1.00 33.14  ?  523 ILE   A CB   1 
ATOM   4013 C  CG1  . ILE   A 1 521 ? -1.032  11.683  18.927  1.00 35.38  ?  523 ILE   A CG1  1 
ATOM   4014 C  CG2  . ILE   A 1 521 ? -3.414  12.503  18.854  1.00 31.89  ?  523 ILE   A CG2  1 
ATOM   4015 C  CD1  . ILE   A 1 521 ? -0.566  11.886  17.537  1.00 32.96  ?  523 ILE   A CD1  1 
ATOM   4016 N  N    . LYS   A 1 522 ? -2.441  15.167  21.212  1.00 33.47  ?  524 LYS   A N    1 
ATOM   4017 C  CA   . LYS   A 1 522 ? -3.357  15.925  22.061  1.00 31.90  ?  524 LYS   A CA   1 
ATOM   4018 C  C    . LYS   A 1 522 ? -3.402  17.382  21.605  1.00 30.49  ?  524 LYS   A C    1 
ATOM   4019 O  O    . LYS   A 1 522 ? -4.468  17.989  21.647  1.00 27.64  ?  524 LYS   A O    1 
ATOM   4020 C  CB   . LYS   A 1 522 ? -2.942  15.878  23.552  1.00 37.71  ?  524 LYS   A CB   1 
ATOM   4021 C  CG   . LYS   A 1 522 ? -4.071  15.621  24.565  1.00 37.88  ?  524 LYS   A CG   1 
ATOM   4022 C  CD   . LYS   A 1 522 ? -5.254  16.573  24.423  1.00 37.98  ?  524 LYS   A CD   1 
ATOM   4023 N  N    . LYS   A 1 523 ? -2.249  17.952  21.228  1.00 29.83  ?  525 LYS   A N    1 
ATOM   4024 C  CA   . LYS   A 1 523 ? -2.190  19.338  20.700  1.00 31.13  ?  525 LYS   A CA   1 
ATOM   4025 C  C    . LYS   A 1 523 ? -2.817  19.481  19.285  1.00 31.08  ?  525 LYS   A C    1 
ATOM   4026 O  O    . LYS   A 1 523 ? -3.394  20.515  18.947  1.00 35.35  ?  525 LYS   A O    1 
ATOM   4027 C  CB   . LYS   A 1 523 ? -0.766  19.798  20.556  1.00 32.06  ?  525 LYS   A CB   1 
ATOM   4028 C  CG   . LYS   A 1 523 ? -0.080  20.235  21.825  1.00 33.68  ?  525 LYS   A CG   1 
ATOM   4029 C  CD   . LYS   A 1 523 ? 1.411   19.907  21.739  1.00 35.61  ?  525 LYS   A CD   1 
ATOM   4030 C  CE   . LYS   A 1 523 ? 2.295   21.118  21.896  1.00 34.72  ?  525 LYS   A CE   1 
ATOM   4031 N  NZ   . LYS   A 1 523 ? 3.635   20.703  21.415  1.00 36.21  ?  525 LYS   A NZ   1 
ATOM   4032 N  N    . GLN   A 1 524 ? -2.654  18.463  18.453  1.00 28.21  ?  526 GLN   A N    1 
ATOM   4033 C  CA   . GLN   A 1 524 ? -3.222  18.479  17.102  1.00 28.28  ?  526 GLN   A CA   1 
ATOM   4034 C  C    . GLN   A 1 524 ? -4.789  18.352  17.167  1.00 29.84  ?  526 GLN   A C    1 
ATOM   4035 O  O    . GLN   A 1 524 ? -5.522  18.966  16.365  1.00 26.30  ?  526 GLN   A O    1 
ATOM   4036 C  CB   . GLN   A 1 524 ? -2.545  17.385  16.280  1.00 25.05  ?  526 GLN   A CB   1 
ATOM   4037 C  CG   . GLN   A 1 524 ? -1.136  17.774  15.887  1.00 23.75  ?  526 GLN   A CG   1 
ATOM   4038 C  CD   . GLN   A 1 524 ? -0.221  16.638  15.459  1.00 22.68  ?  526 GLN   A CD   1 
ATOM   4039 O  OE1  . GLN   A 1 524 ? -0.438  15.453  15.760  1.00 23.25  ?  526 GLN   A OE1  1 
ATOM   4040 N  NE2  . GLN   A 1 524 ? 0.835   17.004  14.781  1.00 24.20  ?  526 GLN   A NE2  1 
ATOM   4041 N  N    . THR   A 1 525 ? -5.280  17.627  18.178  1.00 28.45  ?  527 THR   A N    1 
ATOM   4042 C  CA   . THR   A 1 525 ? -6.684  17.364  18.303  1.00 32.04  ?  527 THR   A CA   1 
ATOM   4043 C  C    . THR   A 1 525 ? -7.388  18.656  18.677  1.00 35.00  ?  527 THR   A C    1 
ATOM   4044 O  O    . THR   A 1 525 ? -8.521  18.888  18.245  1.00 35.20  ?  527 THR   A O    1 
ATOM   4045 C  CB   . THR   A 1 525 ? -6.967  16.206  19.281  1.00 32.69  ?  527 THR   A CB   1 
ATOM   4046 O  OG1  . THR   A 1 525 ? -6.288  15.024  18.831  1.00 30.09  ?  527 THR   A OG1  1 
ATOM   4047 C  CG2  . THR   A 1 525 ? -8.479  15.914  19.411  1.00 31.38  ?  527 THR   A CG2  1 
ATOM   4048 N  N    . ALA   A 1 526 ? -6.674  19.502  19.419  1.00 35.23  ?  528 ALA   A N    1 
ATOM   4049 C  CA   . ALA   A 1 526 ? -7.172  20.775  19.860  1.00 35.14  ?  528 ALA   A CA   1 
ATOM   4050 C  C    . ALA   A 1 526 ? -7.101  21.775  18.732  1.00 35.08  ?  528 ALA   A C    1 
ATOM   4051 O  O    . ALA   A 1 526 ? -8.025  22.587  18.591  1.00 35.44  ?  528 ALA   A O    1 
ATOM   4052 C  CB   . ALA   A 1 526 ? -6.365  21.279  21.053  1.00 34.86  ?  528 ALA   A CB   1 
ATOM   4053 N  N    . LEU   A 1 527 ? -6.006  21.728  17.959  1.00 32.80  ?  529 LEU   A N    1 
ATOM   4054 C  CA   . LEU   A 1 527 ? -5.871  22.533  16.742  1.00 32.40  ?  529 LEU   A CA   1 
ATOM   4055 C  C    . LEU   A 1 527 ? -7.054  22.399  15.788  1.00 31.33  ?  529 LEU   A C    1 
ATOM   4056 O  O    . LEU   A 1 527 ? -7.552  23.422  15.239  1.00 28.78  ?  529 LEU   A O    1 
ATOM   4057 C  CB   . LEU   A 1 527 ? -4.588  22.200  15.965  1.00 32.69  ?  529 LEU   A CB   1 
ATOM   4058 C  CG   . LEU   A 1 527 ? -4.192  23.135  14.788  1.00 33.42  ?  529 LEU   A CG   1 
ATOM   4059 C  CD1  . LEU   A 1 527 ? -4.445  24.621  15.047  1.00 32.15  ?  529 LEU   A CD1  1 
ATOM   4060 C  CD2  . LEU   A 1 527 ? -2.723  22.943  14.428  1.00 34.38  ?  529 LEU   A CD2  1 
ATOM   4061 N  N    . VAL   A 1 528 ? -7.475  21.156  15.547  1.00 30.03  ?  530 VAL   A N    1 
ATOM   4062 C  CA   . VAL   A 1 528 ? -8.584  20.877  14.603  1.00 30.79  ?  530 VAL   A CA   1 
ATOM   4063 C  C    . VAL   A 1 528 ? -9.908  21.460  15.151  1.00 33.71  ?  530 VAL   A C    1 
ATOM   4064 O  O    . VAL   A 1 528 ? -10.675 22.092  14.421  1.00 35.15  ?  530 VAL   A O    1 
ATOM   4065 C  CB   . VAL   A 1 528 ? -8.731  19.352  14.289  1.00 29.22  ?  530 VAL   A CB   1 
ATOM   4066 C  CG1  . VAL   A 1 528 ? -10.031 19.042  13.552  1.00 31.42  ?  530 VAL   A CG1  1 
ATOM   4067 C  CG2  . VAL   A 1 528 ? -7.567  18.852  13.450  1.00 27.52  ?  530 VAL   A CG2  1 
ATOM   4068 N  N    . GLU   A 1 529 ? -10.153 21.262  16.440  1.00 32.96  ?  531 GLU   A N    1 
ATOM   4069 C  CA   . GLU   A 1 529 ? -11.386 21.738  17.089  1.00 33.91  ?  531 GLU   A CA   1 
ATOM   4070 C  C    . GLU   A 1 529 ? -11.404 23.270  17.103  1.00 33.86  ?  531 GLU   A C    1 
ATOM   4071 O  O    . GLU   A 1 529 ? -12.433 23.886  16.862  1.00 33.12  ?  531 GLU   A O    1 
ATOM   4072 C  CB   . GLU   A 1 529 ? -11.473 21.177  18.504  1.00 34.45  ?  531 GLU   A CB   1 
ATOM   4073 C  CG   . GLU   A 1 529 ? -11.597 19.658  18.537  1.00 35.36  ?  531 GLU   A CG   1 
ATOM   4074 C  CD   . GLU   A 1 529 ? -12.994 19.190  18.194  1.00 41.99  ?  531 GLU   A CD   1 
ATOM   4075 O  OE1  . GLU   A 1 529 ? -13.922 20.036  18.177  1.00 44.79  ?  531 GLU   A OE1  1 
ATOM   4076 O  OE2  . GLU   A 1 529 ? -13.179 17.974  17.954  1.00 45.09  ?  531 GLU   A OE2  1 
ATOM   4077 N  N    . LEU   A 1 530 ? -10.240 23.871  17.359  1.00 31.63  ?  532 LEU   A N    1 
ATOM   4078 C  CA   . LEU   A 1 530 ? -10.050 25.285  17.184  1.00 29.02  ?  532 LEU   A CA   1 
ATOM   4079 C  C    . LEU   A 1 530 ? -10.480 25.723  15.768  1.00 29.23  ?  532 LEU   A C    1 
ATOM   4080 O  O    . LEU   A 1 530 ? -11.353 26.596  15.626  1.00 31.20  ?  532 LEU   A O    1 
ATOM   4081 C  CB   . LEU   A 1 530 ? -8.591  25.674  17.459  1.00 28.55  ?  532 LEU   A CB   1 
ATOM   4082 C  CG   . LEU   A 1 530 ? -8.237  27.148  17.267  1.00 28.78  ?  532 LEU   A CG   1 
ATOM   4083 C  CD1  . LEU   A 1 530 ? -9.089  28.013  18.175  1.00 29.38  ?  532 LEU   A CD1  1 
ATOM   4084 C  CD2  . LEU   A 1 530 ? -6.764  27.451  17.513  1.00 29.16  ?  532 LEU   A CD2  1 
ATOM   4085 N  N    . VAL   A 1 531 ? -9.891  25.130  14.736  1.00 25.59  ?  533 VAL   A N    1 
ATOM   4086 C  CA   . VAL   A 1 531 ? -10.245 25.509  13.361  1.00 26.23  ?  533 VAL   A CA   1 
ATOM   4087 C  C    . VAL   A 1 531 ? -11.741 25.244  13.067  1.00 27.00  ?  533 VAL   A C    1 
ATOM   4088 O  O    . VAL   A 1 531 ? -12.391 26.049  12.423  1.00 27.92  ?  533 VAL   A O    1 
ATOM   4089 C  CB   . VAL   A 1 531 ? -9.341  24.838  12.315  1.00 25.16  ?  533 VAL   A CB   1 
ATOM   4090 C  CG1  . VAL   A 1 531 ? -9.866  25.045  10.886  1.00 24.70  ?  533 VAL   A CG1  1 
ATOM   4091 C  CG2  . VAL   A 1 531 ? -7.909  25.372  12.442  1.00 23.65  ?  533 VAL   A CG2  1 
ATOM   4092 N  N    . LYS   A 1 532 ? -12.273 24.124  13.530  1.00 26.19  ?  534 LYS   A N    1 
ATOM   4093 C  CA   . LYS   A 1 532 ? -13.681 23.829  13.367  1.00 26.94  ?  534 LYS   A CA   1 
ATOM   4094 C  C    . LYS   A 1 532 ? -14.570 24.906  13.963  1.00 28.86  ?  534 LYS   A C    1 
ATOM   4095 O  O    . LYS   A 1 532 ? -15.601 25.249  13.381  1.00 27.84  ?  534 LYS   A O    1 
ATOM   4096 C  CB   . LYS   A 1 532 ? -14.035 22.464  13.974  1.00 26.84  ?  534 LYS   A CB   1 
ATOM   4097 C  CG   . LYS   A 1 532 ? -13.511 21.295  13.168  1.00 27.54  ?  534 LYS   A CG   1 
ATOM   4098 C  CD   . LYS   A 1 532 ? -14.028 19.966  13.689  1.00 28.43  ?  534 LYS   A CD   1 
ATOM   4099 C  CE   . LYS   A 1 532 ? -13.669 18.835  12.727  1.00 30.53  ?  534 LYS   A CE   1 
ATOM   4100 N  NZ   . LYS   A 1 532 ? -13.907 17.496  13.330  1.00 32.41  ?  534 LYS   A NZ   1 
ATOM   4101 N  N    . HIS   A 1 533 ? -14.165 25.404  15.134  1.00 31.22  ?  535 HIS   A N    1 
ATOM   4102 C  CA   . HIS   A 1 533 ? -14.888 26.415  15.837  1.00 32.57  ?  535 HIS   A CA   1 
ATOM   4103 C  C    . HIS   A 1 533 ? -14.644 27.775  15.202  1.00 33.95  ?  535 HIS   A C    1 
ATOM   4104 O  O    . HIS   A 1 533 ? -15.561 28.588  15.131  1.00 30.43  ?  535 HIS   A O    1 
ATOM   4105 C  CB   . HIS   A 1 533 ? -14.506 26.462  17.323  1.00 34.95  ?  535 HIS   A CB   1 
ATOM   4106 C  CG   . HIS   A 1 533 ? -15.193 27.566  18.067  1.00 35.67  ?  535 HIS   A CG   1 
ATOM   4107 N  ND1  . HIS   A 1 533 ? -16.566 27.644  18.168  1.00 36.13  ?  535 HIS   A ND1  1 
ATOM   4108 C  CD2  . HIS   A 1 533 ? -14.703 28.668  18.682  1.00 35.49  ?  535 HIS   A CD2  1 
ATOM   4109 C  CE1  . HIS   A 1 533 ? -16.891 28.738  18.832  1.00 36.93  ?  535 HIS   A CE1  1 
ATOM   4110 N  NE2  . HIS   A 1 533 ? -15.780 29.379  19.148  1.00 38.11  ?  535 HIS   A NE2  1 
ATOM   4111 N  N    . LYS   A 1 534 ? -13.417 28.041  14.761  1.00 35.39  ?  536 LYS   A N    1 
ATOM   4112 C  CA   . LYS   A 1 534 ? -13.139 29.308  14.071  1.00 37.41  ?  536 LYS   A CA   1 
ATOM   4113 C  C    . LYS   A 1 534 ? -12.530 29.157  12.673  1.00 34.02  ?  536 LYS   A C    1 
ATOM   4114 O  O    . LYS   A 1 534 ? -11.383 29.534  12.426  1.00 36.05  ?  536 LYS   A O    1 
ATOM   4115 C  CB   . LYS   A 1 534 ? -12.376 30.259  14.983  1.00 42.55  ?  536 LYS   A CB   1 
ATOM   4116 C  CG   . LYS   A 1 534 ? -13.321 30.975  15.953  1.00 44.83  ?  536 LYS   A CG   1 
ATOM   4117 C  CD   . LYS   A 1 534 ? -14.098 32.095  15.260  1.00 47.83  ?  536 LYS   A CD   1 
ATOM   4118 C  CE   . LYS   A 1 534 ? -15.296 32.561  16.078  1.00 49.96  ?  536 LYS   A CE   1 
ATOM   4119 N  NZ   . LYS   A 1 534 ? -14.896 32.917  17.472  1.00 50.90  ?  536 LYS   A NZ   1 
ATOM   4120 N  N    . PRO   A 1 535 ? -13.351 28.666  11.727  1.00 33.97  ?  537 PRO   A N    1 
ATOM   4121 C  CA   . PRO   A 1 535 ? -12.874 28.427  10.366  1.00 34.85  ?  537 PRO   A CA   1 
ATOM   4122 C  C    . PRO   A 1 535 ? -12.636 29.726  9.575   1.00 34.97  ?  537 PRO   A C    1 
ATOM   4123 O  O    . PRO   A 1 535 ? -11.829 29.724  8.641   1.00 39.07  ?  537 PRO   A O    1 
ATOM   4124 C  CB   . PRO   A 1 535 ? -13.988 27.560  9.761   1.00 33.44  ?  537 PRO   A CB   1 
ATOM   4125 C  CG   . PRO   A 1 535 ? -15.219 27.996  10.474  1.00 34.76  ?  537 PRO   A CG   1 
ATOM   4126 C  CD   . PRO   A 1 535 ? -14.812 28.438  11.844  1.00 33.27  ?  537 PRO   A CD   1 
ATOM   4127 N  N    . LYS   A 1 536 ? -13.285 30.825  9.961   1.00 37.63  ?  538 LYS   A N    1 
ATOM   4128 C  CA   . LYS   A 1 536 ? -12.931 32.174  9.420   1.00 39.82  ?  538 LYS   A CA   1 
ATOM   4129 C  C    . LYS   A 1 536 ? -11.519 32.704  9.802   1.00 39.09  ?  538 LYS   A C    1 
ATOM   4130 O  O    . LYS   A 1 536 ? -11.069 33.711  9.252   1.00 38.42  ?  538 LYS   A O    1 
ATOM   4131 C  CB   . LYS   A 1 536 ? -13.995 33.207  9.839   1.00 36.64  ?  538 LYS   A CB   1 
ATOM   4132 N  N    . ALA   A 1 537 ? -10.832 32.046  10.735  1.00 40.64  ?  539 ALA   A N    1 
ATOM   4133 C  CA   . ALA   A 1 537 ? -9.553  32.540  11.275  1.00 40.47  ?  539 ALA   A CA   1 
ATOM   4134 C  C    . ALA   A 1 537 ? -8.382  32.568  10.274  1.00 39.44  ?  539 ALA   A C    1 
ATOM   4135 O  O    . ALA   A 1 537 ? -8.025  31.535  9.707   1.00 35.88  ?  539 ALA   A O    1 
ATOM   4136 C  CB   . ALA   A 1 537 ? -9.159  31.731  12.524  1.00 40.67  ?  539 ALA   A CB   1 
ATOM   4137 N  N    . THR   A 1 538 ? -7.801  33.761  10.090  1.00 40.29  ?  540 THR   A N    1 
ATOM   4138 C  CA   . THR   A 1 538 ? -6.552  33.997  9.328   1.00 41.58  ?  540 THR   A CA   1 
ATOM   4139 C  C    . THR   A 1 538 ? -5.318  33.308  9.934   1.00 40.58  ?  540 THR   A C    1 
ATOM   4140 O  O    . THR   A 1 538 ? -5.302  32.980  11.131  1.00 38.04  ?  540 THR   A O    1 
ATOM   4141 C  CB   . THR   A 1 538 ? -6.259  35.532  9.263   1.00 47.40  ?  540 THR   A CB   1 
ATOM   4142 O  OG1  . THR   A 1 538 ? -7.417  36.221  8.775   1.00 51.52  ?  540 THR   A OG1  1 
ATOM   4143 C  CG2  . THR   A 1 538 ? -5.098  35.903  8.345   1.00 50.05  ?  540 THR   A CG2  1 
ATOM   4144 N  N    . LYS   A 1 539 ? -4.306  33.088  9.080   1.00 39.75  ?  541 LYS   A N    1 
ATOM   4145 C  CA   . LYS   A 1 539 ? -2.941  32.659  9.440   1.00 40.02  ?  541 LYS   A CA   1 
ATOM   4146 C  C    . LYS   A 1 539 ? -2.376  33.285  10.718  1.00 40.81  ?  541 LYS   A C    1 
ATOM   4147 O  O    . LYS   A 1 539 ? -1.997  32.574  11.647  1.00 36.69  ?  541 LYS   A O    1 
ATOM   4148 C  CB   . LYS   A 1 539 ? -1.951  32.979  8.299   1.00 43.51  ?  541 LYS   A CB   1 
ATOM   4149 C  CG   . LYS   A 1 539 ? -1.534  31.815  7.418   1.00 45.78  ?  541 LYS   A CG   1 
ATOM   4150 C  CD   . LYS   A 1 539 ? -0.507  32.263  6.375   1.00 46.16  ?  541 LYS   A CD   1 
ATOM   4151 N  N    . GLU   A 1 540 ? -2.275  34.609  10.741  1.00 42.93  ?  542 GLU   A N    1 
ATOM   4152 C  CA   . GLU   A 1 540 ? -1.641  35.282  11.884  1.00 46.36  ?  542 GLU   A CA   1 
ATOM   4153 C  C    . GLU   A 1 540 ? -2.414  35.149  13.210  1.00 41.41  ?  542 GLU   A C    1 
ATOM   4154 O  O    . GLU   A 1 540 ? -1.808  35.030  14.270  1.00 37.94  ?  542 GLU   A O    1 
ATOM   4155 C  CB   . GLU   A 1 540 ? -1.297  36.752  11.575  1.00 51.78  ?  542 GLU   A CB   1 
ATOM   4156 C  CG   . GLU   A 1 540 ? 0.205   36.982  11.323  1.00 57.72  ?  542 GLU   A CG   1 
ATOM   4157 C  CD   . GLU   A 1 540 ? 1.107   36.878  12.590  1.00 58.69  ?  542 GLU   A CD   1 
ATOM   4158 O  OE1  . GLU   A 1 540 ? 1.279   35.775  13.180  1.00 50.40  ?  542 GLU   A OE1  1 
ATOM   4159 O  OE2  . GLU   A 1 540 ? 1.683   37.917  12.980  1.00 56.19  ?  542 GLU   A OE2  1 
ATOM   4160 N  N    . GLN   A 1 541 ? -3.739  35.135  13.144  1.00 39.46  ?  543 GLN   A N    1 
ATOM   4161 C  CA   . GLN   A 1 541 ? -4.553  34.901  14.329  1.00 39.70  ?  543 GLN   A CA   1 
ATOM   4162 C  C    . GLN   A 1 541 ? -4.381  33.455  14.904  1.00 40.72  ?  543 GLN   A C    1 
ATOM   4163 O  O    . GLN   A 1 541 ? -4.396  33.255  16.119  1.00 45.87  ?  543 GLN   A O    1 
ATOM   4164 C  CB   . GLN   A 1 541 ? -6.034  35.141  14.012  1.00 40.31  ?  543 GLN   A CB   1 
ATOM   4165 C  CG   . GLN   A 1 541 ? -6.429  36.535  13.491  1.00 40.32  ?  543 GLN   A CG   1 
ATOM   4166 C  CD   . GLN   A 1 541 ? -7.881  36.572  13.010  1.00 39.18  ?  543 GLN   A CD   1 
ATOM   4167 O  OE1  . GLN   A 1 541 ? -8.365  35.619  12.375  1.00 34.87  ?  543 GLN   A OE1  1 
ATOM   4168 N  NE2  . GLN   A 1 541 ? -8.588  37.673  13.318  1.00 33.40  ?  543 GLN   A NE2  1 
ATOM   4169 N  N    . LEU   A 1 542 ? -4.260  32.463  14.033  1.00 38.65  ?  544 LEU   A N    1 
ATOM   4170 C  CA   . LEU   A 1 542 ? -3.997  31.104  14.471  1.00 45.12  ?  544 LEU   A CA   1 
ATOM   4171 C  C    . LEU   A 1 542 ? -2.623  31.030  15.107  1.00 44.76  ?  544 LEU   A C    1 
ATOM   4172 O  O    . LEU   A 1 542 ? -2.464  30.399  16.145  1.00 45.38  ?  544 LEU   A O    1 
ATOM   4173 C  CB   . LEU   A 1 542 ? -4.048  30.102  13.320  1.00 45.67  ?  544 LEU   A CB   1 
ATOM   4174 C  CG   . LEU   A 1 542 ? -5.214  29.144  13.383  1.00 49.32  ?  544 LEU   A CG   1 
ATOM   4175 C  CD1  . LEU   A 1 542 ? -6.517  29.889  13.177  1.00 54.73  ?  544 LEU   A CD1  1 
ATOM   4176 C  CD2  . LEU   A 1 542 ? -5.038  28.088  12.317  1.00 51.21  ?  544 LEU   A CD2  1 
ATOM   4177 N  N    . LYS   A 1 543 ? -1.639  31.676  14.484  1.00 42.67  ?  545 LYS   A N    1 
ATOM   4178 C  CA   . LYS   A 1 543 ? -0.253  31.582  14.953  1.00 41.25  ?  545 LYS   A CA   1 
ATOM   4179 C  C    . LYS   A 1 543 ? -0.152  32.234  16.336  1.00 42.75  ?  545 LYS   A C    1 
ATOM   4180 O  O    . LYS   A 1 543 ? 0.465   31.686  17.230  1.00 39.38  ?  545 LYS   A O    1 
ATOM   4181 C  CB   . LYS   A 1 543 ? 0.720   32.196  13.940  1.00 37.88  ?  545 LYS   A CB   1 
ATOM   4182 C  CG   . LYS   A 1 543 ? 2.190   31.922  14.214  1.00 35.94  ?  545 LYS   A CG   1 
ATOM   4183 N  N    . ALA   A 1 544 ? -0.804  33.378  16.503  1.00 43.56  ?  546 ALA   A N    1 
ATOM   4184 C  CA   . ALA   A 1 544 ? -0.931  34.019  17.805  1.00 44.51  ?  546 ALA   A CA   1 
ATOM   4185 C  C    . ALA   A 1 544 ? -1.659  33.148  18.876  1.00 44.50  ?  546 ALA   A C    1 
ATOM   4186 O  O    . ALA   A 1 544 ? -1.286  33.171  20.054  1.00 45.25  ?  546 ALA   A O    1 
ATOM   4187 C  CB   . ALA   A 1 544 ? -1.628  35.375  17.639  1.00 42.22  ?  546 ALA   A CB   1 
ATOM   4188 N  N    . VAL   A 1 545 ? -2.698  32.404  18.494  1.00 40.96  ?  547 VAL   A N    1 
ATOM   4189 C  CA   . VAL   A 1 545 ? -3.329  31.481  19.439  1.00 39.99  ?  547 VAL   A CA   1 
ATOM   4190 C  C    . VAL   A 1 545 ? -2.406  30.277  19.700  1.00 40.07  ?  547 VAL   A C    1 
ATOM   4191 O  O    . VAL   A 1 545 ? -2.317  29.817  20.828  1.00 45.46  ?  547 VAL   A O    1 
ATOM   4192 C  CB   . VAL   A 1 545 ? -4.751  31.074  18.991  1.00 39.05  ?  547 VAL   A CB   1 
ATOM   4193 C  CG1  . VAL   A 1 545 ? -5.295  29.929  19.818  1.00 36.34  ?  547 VAL   A CG1  1 
ATOM   4194 C  CG2  . VAL   A 1 545 ? -5.678  32.277  19.082  1.00 39.70  ?  547 VAL   A CG2  1 
ATOM   4195 N  N    . MET   A 1 546 ? -1.692  29.816  18.679  1.00 43.24  ?  548 MET   A N    1 
ATOM   4196 C  CA   . MET   A 1 546 ? -0.725  28.707  18.812  1.00 47.94  ?  548 MET   A CA   1 
ATOM   4197 C  C    . MET   A 1 546 ? 0.560   28.997  19.607  1.00 48.05  ?  548 MET   A C    1 
ATOM   4198 O  O    . MET   A 1 546 ? 1.015   28.139  20.360  1.00 51.02  ?  548 MET   A O    1 
ATOM   4199 C  CB   . MET   A 1 546 ? -0.324  28.182  17.441  1.00 46.83  ?  548 MET   A CB   1 
ATOM   4200 C  CG   . MET   A 1 546 ? -1.399  27.359  16.752  1.00 47.65  ?  548 MET   A CG   1 
ATOM   4201 S  SD   . MET   A 1 546 ? -0.837  26.571  15.223  1.00 48.47  ?  548 MET   A SD   1 
ATOM   4202 C  CE   . MET   A 1 546 ? 0.242   27.782  14.450  1.00 47.42  ?  548 MET   A CE   1 
ATOM   4203 N  N    . ASP   A 1 547 ? 1.172   30.158  19.412  1.00 48.49  ?  549 ASP   A N    1 
ATOM   4204 C  CA   . ASP   A 1 547 ? 2.391   30.524  20.171  1.00 52.65  ?  549 ASP   A CA   1 
ATOM   4205 C  C    . ASP   A 1 547 ? 2.074   30.729  21.654  1.00 49.90  ?  549 ASP   A C    1 
ATOM   4206 O  O    . ASP   A 1 547 ? 2.887   30.389  22.516  1.00 47.34  ?  549 ASP   A O    1 
ATOM   4207 C  CB   . ASP   A 1 547 ? 3.039   31.808  19.620  1.00 57.45  ?  549 ASP   A CB   1 
ATOM   4208 C  CG   . ASP   A 1 547 ? 3.876   31.577  18.354  1.00 61.43  ?  549 ASP   A CG   1 
ATOM   4209 O  OD1  . ASP   A 1 547 ? 4.172   30.409  17.995  1.00 69.60  ?  549 ASP   A OD1  1 
ATOM   4210 O  OD2  . ASP   A 1 547 ? 4.259   32.597  17.727  1.00 58.76  ?  549 ASP   A OD2  1 
ATOM   4211 N  N    . ASP   A 1 548 ? 0.889   31.298  21.910  1.00 48.74  ?  550 ASP   A N    1 
ATOM   4212 C  CA   . ASP   A 1 548 ? 0.330   31.492  23.251  1.00 46.23  ?  550 ASP   A CA   1 
ATOM   4213 C  C    . ASP   A 1 548 ? 0.081   30.163  23.956  1.00 45.93  ?  550 ASP   A C    1 
ATOM   4214 O  O    . ASP   A 1 548 ? 0.509   29.983  25.100  1.00 44.80  ?  550 ASP   A O    1 
ATOM   4215 C  CB   . ASP   A 1 548 ? -0.991  32.280  23.187  1.00 45.37  ?  550 ASP   A CB   1 
ATOM   4216 C  CG   . ASP   A 1 548 ? -0.785  33.801  23.009  1.00 48.00  ?  550 ASP   A CG   1 
ATOM   4217 O  OD1  . ASP   A 1 548 ? 0.334   34.317  23.247  1.00 48.50  ?  550 ASP   A OD1  1 
ATOM   4218 O  OD2  . ASP   A 1 548 ? -1.769  34.483  22.640  1.00 45.48  ?  550 ASP   A OD2  1 
ATOM   4219 N  N    . PHE   A 1 549 ? -0.603  29.234  23.286  1.00 43.00  ?  551 PHE   A N    1 
ATOM   4220 C  CA   . PHE   A 1 549 ? -0.762  27.901  23.852  1.00 42.93  ?  551 PHE   A CA   1 
ATOM   4221 C  C    . PHE   A 1 549 ? 0.591   27.299  24.193  1.00 43.46  ?  551 PHE   A C    1 
ATOM   4222 O  O    . PHE   A 1 549 ? 0.718   26.692  25.254  1.00 44.14  ?  551 PHE   A O    1 
ATOM   4223 C  CB   . PHE   A 1 549 ? -1.513  26.933  22.934  1.00 41.23  ?  551 PHE   A CB   1 
ATOM   4224 C  CG   . PHE   A 1 549 ? -1.599  25.532  23.497  1.00 42.17  ?  551 PHE   A CG   1 
ATOM   4225 C  CD1  . PHE   A 1 549 ? -2.613  25.183  24.390  1.00 43.70  ?  551 PHE   A CD1  1 
ATOM   4226 C  CD2  . PHE   A 1 549 ? -0.631  24.577  23.186  1.00 42.18  ?  551 PHE   A CD2  1 
ATOM   4227 C  CE1  . PHE   A 1 549 ? -2.678  23.901  24.923  1.00 44.28  ?  551 PHE   A CE1  1 
ATOM   4228 C  CE2  . PHE   A 1 549 ? -0.689  23.306  23.728  1.00 41.26  ?  551 PHE   A CE2  1 
ATOM   4229 C  CZ   . PHE   A 1 549 ? -1.723  22.962  24.584  1.00 42.50  ?  551 PHE   A CZ   1 
ATOM   4230 N  N    . ALA   A 1 550 ? 1.572   27.449  23.296  1.00 46.22  ?  552 ALA   A N    1 
ATOM   4231 C  CA   . ALA   A 1 550 ? 2.939   26.930  23.517  1.00 51.62  ?  552 ALA   A CA   1 
ATOM   4232 C  C    . ALA   A 1 550 ? 3.679   27.582  24.700  1.00 56.38  ?  552 ALA   A C    1 
ATOM   4233 O  O    . ALA   A 1 550 ? 4.476   26.909  25.371  1.00 59.70  ?  552 ALA   A O    1 
ATOM   4234 C  CB   . ALA   A 1 550 ? 3.781   27.053  22.253  1.00 47.83  ?  552 ALA   A CB   1 
ATOM   4235 N  N    . ALA   A 1 551 ? 3.450   28.880  24.921  1.00 59.16  ?  553 ALA   A N    1 
ATOM   4236 C  CA   . ALA   A 1 551 ? 4.007   29.612  26.086  1.00 56.60  ?  553 ALA   A CA   1 
ATOM   4237 C  C    . ALA   A 1 551 ? 3.306   29.237  27.387  1.00 54.08  ?  553 ALA   A C    1 
ATOM   4238 O  O    . ALA   A 1 551 ? 3.955   29.159  28.428  1.00 55.14  ?  553 ALA   A O    1 
ATOM   4239 C  CB   . ALA   A 1 551 ? 3.929   31.123  25.875  1.00 57.45  ?  553 ALA   A CB   1 
ATOM   4240 N  N    . PHE   A 1 552 ? 1.987   29.055  27.302  1.00 46.93  ?  554 PHE   A N    1 
ATOM   4241 C  CA   . PHE   A 1 552 ? 1.135   28.551  28.389  1.00 48.95  ?  554 PHE   A CA   1 
ATOM   4242 C  C    . PHE   A 1 552 ? 1.526   27.162  28.898  1.00 52.46  ?  554 PHE   A C    1 
ATOM   4243 O  O    . PHE   A 1 552 ? 1.472   26.913  30.105  1.00 55.13  ?  554 PHE   A O    1 
ATOM   4244 C  CB   . PHE   A 1 552 ? -0.344  28.568  27.937  1.00 45.52  ?  554 PHE   A CB   1 
ATOM   4245 C  CG   . PHE   A 1 552 ? -1.258  27.598  28.658  1.00 49.24  ?  554 PHE   A CG   1 
ATOM   4246 C  CD1  . PHE   A 1 552 ? -1.784  27.905  29.896  1.00 50.61  ?  554 PHE   A CD1  1 
ATOM   4247 C  CD2  . PHE   A 1 552 ? -1.656  26.398  28.050  1.00 49.27  ?  554 PHE   A CD2  1 
ATOM   4248 C  CE1  . PHE   A 1 552 ? -2.656  27.027  30.542  1.00 50.81  ?  554 PHE   A CE1  1 
ATOM   4249 C  CE2  . PHE   A 1 552 ? -2.532  25.529  28.682  1.00 50.11  ?  554 PHE   A CE2  1 
ATOM   4250 C  CZ   . PHE   A 1 552 ? -3.033  25.839  29.935  1.00 50.33  ?  554 PHE   A CZ   1 
ATOM   4251 N  N    . VAL   A 1 553 ? 1.886   26.258  27.993  1.00 49.51  ?  555 VAL   A N    1 
ATOM   4252 C  CA   . VAL   A 1 553 ? 2.285   24.900  28.392  1.00 50.24  ?  555 VAL   A CA   1 
ATOM   4253 C  C    . VAL   A 1 553 ? 3.671   24.883  29.045  1.00 51.49  ?  555 VAL   A C    1 
ATOM   4254 O  O    . VAL   A 1 553 ? 3.864   24.159  30.015  1.00 48.99  ?  555 VAL   A O    1 
ATOM   4255 C  CB   . VAL   A 1 553 ? 2.142   23.871  27.229  1.00 48.50  ?  555 VAL   A CB   1 
ATOM   4256 C  CG1  . VAL   A 1 553 ? 2.927   22.584  27.483  1.00 46.20  ?  555 VAL   A CG1  1 
ATOM   4257 C  CG2  . VAL   A 1 553 ? 0.661   23.538  27.028  1.00 46.75  ?  555 VAL   A CG2  1 
ATOM   4258 N  N    . GLU   A 1 554 ? 4.619   25.677  28.553  1.00 56.45  ?  556 GLU   A N    1 
ATOM   4259 C  CA   . GLU   A 1 554 ? 5.918   25.766  29.226  1.00 60.34  ?  556 GLU   A CA   1 
ATOM   4260 C  C    . GLU   A 1 554 ? 5.783   26.449  30.608  1.00 64.91  ?  556 GLU   A C    1 
ATOM   4261 O  O    . GLU   A 1 554 ? 6.395   25.992  31.580  1.00 67.42  ?  556 GLU   A O    1 
ATOM   4262 C  CB   . GLU   A 1 554 ? 6.953   26.483  28.376  1.00 59.47  ?  556 GLU   A CB   1 
ATOM   4263 C  CG   . GLU   A 1 554 ? 8.370   26.244  28.878  1.00 61.44  ?  556 GLU   A CG   1 
ATOM   4264 C  CD   . GLU   A 1 554 ? 9.330   27.385  28.592  1.00 64.07  ?  556 GLU   A CD   1 
ATOM   4265 O  OE1  . GLU   A 1 554 ? 8.892   28.557  28.502  1.00 65.73  ?  556 GLU   A OE1  1 
ATOM   4266 O  OE2  . GLU   A 1 554 ? 10.546  27.101  28.484  1.00 60.34  ?  556 GLU   A OE2  1 
ATOM   4267 N  N    . LYS   A 1 555 ? 4.981   27.515  30.699  1.00 61.45  ?  557 LYS   A N    1 
ATOM   4268 C  CA   . LYS   A 1 555 ? 4.706   28.174  31.997  1.00 60.83  ?  557 LYS   A CA   1 
ATOM   4269 C  C    . LYS   A 1 555 ? 4.167   27.192  33.047  1.00 59.99  ?  557 LYS   A C    1 
ATOM   4270 O  O    . LYS   A 1 555 ? 4.675   27.128  34.159  1.00 64.60  ?  557 LYS   A O    1 
ATOM   4271 C  CB   . LYS   A 1 555 ? 3.719   29.340  31.833  1.00 58.84  ?  557 LYS   A CB   1 
ATOM   4272 C  CG   . LYS   A 1 555 ? 3.505   30.168  33.090  1.00 57.06  ?  557 LYS   A CG   1 
ATOM   4273 N  N    . CYS   A 1 556 ? 3.158   26.414  32.686  1.00 57.86  ?  558 CYS   A N    1 
ATOM   4274 C  CA   . CYS   A 1 556 ? 2.529   25.495  33.640  1.00 59.29  ?  558 CYS   A CA   1 
ATOM   4275 C  C    . CYS   A 1 556 ? 3.283   24.196  33.963  1.00 53.45  ?  558 CYS   A C    1 
ATOM   4276 O  O    . CYS   A 1 556 ? 2.890   23.515  34.898  1.00 48.68  ?  558 CYS   A O    1 
ATOM   4277 C  CB   . CYS   A 1 556 ? 1.106   25.162  33.174  1.00 64.35  ?  558 CYS   A CB   1 
ATOM   4278 S  SG   . CYS   A 1 556 ? 0.007   26.587  33.031  1.00 69.03  ?  558 CYS   A SG   1 
ATOM   4279 N  N    . CYS   A 1 557 ? 4.317   23.851  33.185  1.00 57.06  ?  559 CYS   A N    1 
ATOM   4280 C  CA   . CYS   A 1 557 ? 5.161   22.643  33.406  1.00 57.80  ?  559 CYS   A CA   1 
ATOM   4281 C  C    . CYS   A 1 557 ? 6.601   22.961  33.850  1.00 59.49  ?  559 CYS   A C    1 
ATOM   4282 O  O    . CYS   A 1 557 ? 7.396   22.034  34.059  1.00 54.47  ?  559 CYS   A O    1 
ATOM   4283 C  CB   . CYS   A 1 557 ? 5.289   21.769  32.135  1.00 57.82  ?  559 CYS   A CB   1 
ATOM   4284 S  SG   . CYS   A 1 557 ? 3.858   21.456  31.073  1.00 52.23  ?  559 CYS   A SG   1 
ATOM   4285 N  N    . LYS   A 1 558 ? 6.946   24.249  33.917  1.00 60.94  ?  560 LYS   A N    1 
ATOM   4286 C  CA   . LYS   A 1 558 ? 8.195   24.725  34.524  1.00 64.81  ?  560 LYS   A CA   1 
ATOM   4287 C  C    . LYS   A 1 558 ? 7.948   25.116  36.002  1.00 68.72  ?  560 LYS   A C    1 
ATOM   4288 O  O    . LYS   A 1 558 ? 8.897   25.264  36.772  1.00 67.93  ?  560 LYS   A O    1 
ATOM   4289 C  CB   . LYS   A 1 558 ? 8.722   25.931  33.720  1.00 62.29  ?  560 LYS   A CB   1 
ATOM   4290 C  CG   . LYS   A 1 558 ? 10.082  26.469  34.138  1.00 61.21  ?  560 LYS   A CG   1 
ATOM   4291 N  N    . ALA   A 1 559 ? 6.671   25.225  36.394  1.00 69.82  ?  561 ALA   A N    1 
ATOM   4292 C  CA   . ALA   A 1 559 ? 6.256   25.920  37.617  1.00 72.16  ?  561 ALA   A CA   1 
ATOM   4293 C  C    . ALA   A 1 559 ? 6.352   25.078  38.886  1.00 71.85  ?  561 ALA   A C    1 
ATOM   4294 O  O    . ALA   A 1 559 ? 6.199   23.859  38.844  1.00 71.43  ?  561 ALA   A O    1 
ATOM   4295 C  CB   . ALA   A 1 559 ? 4.831   26.441  37.458  1.00 70.58  ?  561 ALA   A CB   1 
ATOM   4296 N  N    . ASP   A 1 560 ? 6.597   25.762  40.008  1.00 73.15  ?  562 ASP   A N    1 
ATOM   4297 C  CA   . ASP   A 1 560 ? 6.551   25.165  41.350  1.00 71.46  ?  562 ASP   A CA   1 
ATOM   4298 C  C    . ASP   A 1 560 ? 5.080   25.014  41.797  1.00 71.45  ?  562 ASP   A C    1 
ATOM   4299 O  O    . ASP   A 1 560 ? 4.585   25.823  42.592  1.00 73.56  ?  562 ASP   A O    1 
ATOM   4300 C  CB   . ASP   A 1 560 ? 7.331   26.040  42.347  1.00 72.89  ?  562 ASP   A CB   1 
ATOM   4301 C  CG   . ASP   A 1 560 ? 8.829   26.090  42.050  1.00 74.17  ?  562 ASP   A CG   1 
ATOM   4302 O  OD1  . ASP   A 1 560 ? 9.490   25.028  42.088  1.00 75.61  ?  562 ASP   A OD1  1 
ATOM   4303 O  OD2  . ASP   A 1 560 ? 9.351   27.193  41.792  1.00 68.62  ?  562 ASP   A OD2  1 
ATOM   4304 N  N    . ASP   A 1 561 ? 4.428   23.954  41.298  1.00 66.20  ?  563 ASP   A N    1 
ATOM   4305 C  CA   . ASP   A 1 561 ? 2.952   23.752  41.266  1.00 60.87  ?  563 ASP   A CA   1 
ATOM   4306 C  C    . ASP   A 1 561 ? 2.485   23.932  39.817  1.00 63.58  ?  563 ASP   A C    1 
ATOM   4307 O  O    . ASP   A 1 561 ? 2.706   24.984  39.218  1.00 69.42  ?  563 ASP   A O    1 
ATOM   4308 C  CB   . ASP   A 1 561 ? 2.158   24.674  42.204  1.00 56.36  ?  563 ASP   A CB   1 
ATOM   4309 C  CG   . ASP   A 1 561 ? 0.665   24.359  42.240  1.00 54.01  ?  563 ASP   A CG   1 
ATOM   4310 O  OD1  . ASP   A 1 561 ? 0.261   23.176  42.319  1.00 48.31  ?  563 ASP   A OD1  1 
ATOM   4311 O  OD2  . ASP   A 1 561 ? -0.117  25.326  42.220  1.00 56.57  ?  563 ASP   A OD2  1 
ATOM   4312 N  N    . LYS   A 1 562 ? 1.846   22.895  39.276  1.00 62.61  ?  564 LYS   A N    1 
ATOM   4313 C  CA   . LYS   A 1 562 ? 1.392   22.842  37.884  1.00 62.16  ?  564 LYS   A CA   1 
ATOM   4314 C  C    . LYS   A 1 562 ? -0.139  22.913  37.718  1.00 65.11  ?  564 LYS   A C    1 
ATOM   4315 O  O    . LYS   A 1 562 ? -0.627  23.643  36.849  1.00 63.52  ?  564 LYS   A O    1 
ATOM   4316 C  CB   . LYS   A 1 562 ? 1.906   21.554  37.235  1.00 58.87  ?  564 LYS   A CB   1 
ATOM   4317 N  N    . GLU   A 1 563 ? -0.891  22.167  38.534  1.00 63.83  ?  565 GLU   A N    1 
ATOM   4318 C  CA   . GLU   A 1 563 ? -2.331  21.999  38.311  1.00 62.96  ?  565 GLU   A CA   1 
ATOM   4319 C  C    . GLU   A 1 563 ? -3.150  23.276  38.459  1.00 63.44  ?  565 GLU   A C    1 
ATOM   4320 O  O    . GLU   A 1 563 ? -4.190  23.400  37.812  1.00 54.87  ?  565 GLU   A O    1 
ATOM   4321 C  CB   . GLU   A 1 563 ? -2.917  20.897  39.208  1.00 68.70  ?  565 GLU   A CB   1 
ATOM   4322 C  CG   . GLU   A 1 563 ? -4.300  20.403  38.787  1.00 71.36  ?  565 GLU   A CG   1 
ATOM   4323 C  CD   . GLU   A 1 563 ? -4.350  19.941  37.331  1.00 81.82  ?  565 GLU   A CD   1 
ATOM   4324 O  OE1  . GLU   A 1 563 ? -3.383  19.290  36.868  1.00 85.13  ?  565 GLU   A OE1  1 
ATOM   4325 O  OE2  . GLU   A 1 563 ? -5.349  20.236  36.635  1.00 85.56  ?  565 GLU   A OE2  1 
ATOM   4326 N  N    . THR   A 1 564 ? -2.691  24.213  39.297  1.00 65.91  ?  566 THR   A N    1 
ATOM   4327 C  CA   . THR   A 1 564 ? -3.326  25.536  39.425  1.00 64.16  ?  566 THR   A CA   1 
ATOM   4328 C  C    . THR   A 1 564 ? -3.144  26.350  38.139  1.00 58.56  ?  566 THR   A C    1 
ATOM   4329 O  O    . THR   A 1 564 ? -4.097  26.942  37.637  1.00 56.92  ?  566 THR   A O    1 
ATOM   4330 C  CB   . THR   A 1 564 ? -2.758  26.343  40.617  1.00 62.87  ?  566 THR   A CB   1 
ATOM   4331 N  N    . CYS   A 1 565 ? -1.917  26.357  37.625  1.00 57.51  ?  567 CYS   A N    1 
ATOM   4332 C  CA   . CYS   A 1 565 ? -1.577  26.975  36.340  1.00 61.50  ?  567 CYS   A CA   1 
ATOM   4333 C  C    . CYS   A 1 565 ? -2.375  26.404  35.146  1.00 60.44  ?  567 CYS   A C    1 
ATOM   4334 O  O    . CYS   A 1 565 ? -2.926  27.161  34.354  1.00 62.96  ?  567 CYS   A O    1 
ATOM   4335 C  CB   . CYS   A 1 565 ? -0.071  26.832  36.080  1.00 66.03  ?  567 CYS   A CB   1 
ATOM   4336 S  SG   . CYS   A 1 565 ? 0.528   27.745  34.639  1.00 80.74  ?  567 CYS   A SG   1 
ATOM   4337 N  N    . PHE   A 1 566 ? -2.431  25.080  35.018  1.00 58.01  ?  568 PHE   A N    1 
ATOM   4338 C  CA   . PHE   A 1 566 ? -3.248  24.405  33.982  1.00 55.12  ?  568 PHE   A CA   1 
ATOM   4339 C  C    . PHE   A 1 566 ? -4.765  24.510  34.233  1.00 56.82  ?  568 PHE   A C    1 
ATOM   4340 O  O    . PHE   A 1 566 ? -5.475  23.496  34.213  1.00 55.02  ?  568 PHE   A O    1 
ATOM   4341 C  CB   . PHE   A 1 566 ? -2.887  22.911  33.901  1.00 54.13  ?  568 PHE   A CB   1 
ATOM   4342 C  CG   . PHE   A 1 566 ? -1.724  22.615  33.026  1.00 53.53  ?  568 PHE   A CG   1 
ATOM   4343 C  CD1  . PHE   A 1 566 ? -1.858  22.700  31.659  1.00 50.64  ?  568 PHE   A CD1  1 
ATOM   4344 C  CD2  . PHE   A 1 566 ? -0.509  22.217  33.559  1.00 49.76  ?  568 PHE   A CD2  1 
ATOM   4345 C  CE1  . PHE   A 1 566 ? -0.791  22.436  30.829  1.00 48.70  ?  568 PHE   A CE1  1 
ATOM   4346 C  CE2  . PHE   A 1 566 ? 0.560   21.944  32.734  1.00 48.73  ?  568 PHE   A CE2  1 
ATOM   4347 C  CZ   . PHE   A 1 566 ? 0.416   22.055  31.361  1.00 47.64  ?  568 PHE   A CZ   1 
ATOM   4348 N  N    . ALA   A 1 567 ? -5.259  25.727  34.429  1.00 57.63  ?  569 ALA   A N    1 
ATOM   4349 C  CA   . ALA   A 1 567 ? -6.643  25.976  34.869  1.00 56.25  ?  569 ALA   A CA   1 
ATOM   4350 C  C    . ALA   A 1 567 ? -6.843  27.469  35.111  1.00 57.51  ?  569 ALA   A C    1 
ATOM   4351 O  O    . ALA   A 1 567 ? -7.854  28.031  34.685  1.00 66.89  ?  569 ALA   A O    1 
ATOM   4352 C  CB   . ALA   A 1 567 ? -6.979  25.194  36.131  1.00 56.65  ?  569 ALA   A CB   1 
ATOM   4353 N  N    . GLU   A 1 568 ? -5.895  28.094  35.813  1.00 55.23  ?  570 GLU   A N    1 
ATOM   4354 C  CA   . GLU   A 1 568 ? -5.838  29.560  35.940  1.00 55.31  ?  570 GLU   A CA   1 
ATOM   4355 C  C    . GLU   A 1 568 ? -5.507  30.180  34.586  1.00 52.13  ?  570 GLU   A C    1 
ATOM   4356 O  O    . GLU   A 1 568 ? -6.299  30.944  34.020  1.00 46.27  ?  570 GLU   A O    1 
ATOM   4357 C  CB   . GLU   A 1 568 ? -4.785  29.986  36.975  1.00 54.43  ?  570 GLU   A CB   1 
ATOM   4358 N  N    . GLU   A 1 569 ? -4.336  29.818  34.068  1.00 56.58  ?  571 GLU   A N    1 
ATOM   4359 C  CA   . GLU   A 1 569 ? -3.870  30.321  32.776  1.00 62.97  ?  571 GLU   A CA   1 
ATOM   4360 C  C    . GLU   A 1 569 ? -4.724  29.797  31.598  1.00 61.11  ?  571 GLU   A C    1 
ATOM   4361 O  O    . GLU   A 1 569 ? -4.800  30.449  30.563  1.00 59.97  ?  571 GLU   A O    1 
ATOM   4362 C  CB   . GLU   A 1 569 ? -2.390  29.997  32.576  1.00 65.67  ?  571 GLU   A CB   1 
ATOM   4363 C  CG   . GLU   A 1 569 ? -1.465  30.610  33.623  1.00 70.44  ?  571 GLU   A CG   1 
ATOM   4364 C  CD   . GLU   A 1 569 ? -0.509  31.637  33.050  1.00 76.00  ?  571 GLU   A CD   1 
ATOM   4365 O  OE1  . GLU   A 1 569 ? -0.991  32.589  32.397  1.00 82.10  ?  571 GLU   A OE1  1 
ATOM   4366 O  OE2  . GLU   A 1 569 ? 0.720   31.491  33.261  1.00 76.91  ?  571 GLU   A OE2  1 
ATOM   4367 N  N    . GLY   A 1 570 ? -5.371  28.638  31.783  1.00 63.73  ?  572 GLY   A N    1 
ATOM   4368 C  CA   . GLY   A 1 570 ? -6.370  28.089  30.851  1.00 58.58  ?  572 GLY   A CA   1 
ATOM   4369 C  C    . GLY   A 1 570 ? -7.607  28.964  30.689  1.00 61.16  ?  572 GLY   A C    1 
ATOM   4370 O  O    . GLY   A 1 570 ? -8.167  29.053  29.594  1.00 60.90  ?  572 GLY   A O    1 
ATOM   4371 N  N    . LYS   A 1 571 ? -8.044  29.608  31.769  1.00 58.64  ?  573 LYS   A N    1 
ATOM   4372 C  CA   . LYS   A 1 571 ? -9.004  30.711  31.661  1.00 55.16  ?  573 LYS   A CA   1 
ATOM   4373 C  C    . LYS   A 1 571 ? -8.374  31.916  30.923  1.00 54.03  ?  573 LYS   A C    1 
ATOM   4374 O  O    . LYS   A 1 571 ? -8.981  32.476  30.012  1.00 46.50  ?  573 LYS   A O    1 
ATOM   4375 C  CB   . LYS   A 1 571 ? -9.511  31.130  33.038  1.00 54.50  ?  573 LYS   A CB   1 
ATOM   4376 C  CG   . LYS   A 1 571 ? -10.357 30.077  33.732  1.00 55.40  ?  573 LYS   A CG   1 
ATOM   4377 N  N    . LYS   A 1 572 ? -7.146  32.276  31.291  1.00 55.14  ?  574 LYS   A N    1 
ATOM   4378 C  CA   . LYS   A 1 572 ? -6.428  33.390  30.630  1.00 60.75  ?  574 LYS   A CA   1 
ATOM   4379 C  C    . LYS   A 1 572 ? -5.857  33.117  29.195  1.00 62.05  ?  574 LYS   A C    1 
ATOM   4380 O  O    . LYS   A 1 572 ? -5.241  34.025  28.605  1.00 63.61  ?  574 LYS   A O    1 
ATOM   4381 C  CB   . LYS   A 1 572 ? -5.334  33.981  31.540  1.00 63.94  ?  574 LYS   A CB   1 
ATOM   4382 C  CG   . LYS   A 1 572 ? -5.666  35.355  32.084  1.00 65.74  ?  574 LYS   A CG   1 
ATOM   4383 C  CD   . LYS   A 1 572 ? -4.522  35.918  32.911  1.00 70.88  ?  574 LYS   A CD   1 
ATOM   4384 C  CE   . LYS   A 1 572 ? -4.856  37.310  33.434  1.00 74.67  ?  574 LYS   A CE   1 
ATOM   4385 N  NZ   . LYS   A 1 572 ? -3.815  37.847  34.357  1.00 74.11  ?  574 LYS   A NZ   1 
ATOM   4386 N  N    . LEU   A 1 573 ? -6.075  31.909  28.641  1.00 56.47  ?  575 LEU   A N    1 
ATOM   4387 C  CA   . LEU   A 1 573 ? -5.835  31.601  27.203  1.00 48.47  ?  575 LEU   A CA   1 
ATOM   4388 C  C    . LEU   A 1 573 ? -7.144  31.550  26.398  1.00 46.42  ?  575 LEU   A C    1 
ATOM   4389 O  O    . LEU   A 1 573 ? -7.316  32.283  25.412  1.00 43.95  ?  575 LEU   A O    1 
ATOM   4390 C  CB   . LEU   A 1 573 ? -5.139  30.249  27.072  1.00 48.11  ?  575 LEU   A CB   1 
ATOM   4391 C  CG   . LEU   A 1 573 ? -4.648  29.790  25.694  1.00 43.80  ?  575 LEU   A CG   1 
ATOM   4392 C  CD1  . LEU   A 1 573 ? -3.532  30.685  25.201  1.00 40.60  ?  575 LEU   A CD1  1 
ATOM   4393 C  CD2  . LEU   A 1 573 ? -4.158  28.353  25.792  1.00 43.36  ?  575 LEU   A CD2  1 
ATOM   4394 N  N    . VAL   A 1 574 ? -8.060  30.695  26.849  1.00 42.07  ?  576 VAL   A N    1 
ATOM   4395 C  CA   . VAL   A 1 574 ? -9.345  30.475  26.199  1.00 41.59  ?  576 VAL   A CA   1 
ATOM   4396 C  C    . VAL   A 1 574 ? -10.128 31.776  26.052  1.00 41.31  ?  576 VAL   A C    1 
ATOM   4397 O  O    . VAL   A 1 574 ? -10.684 32.029  24.993  1.00 45.46  ?  576 VAL   A O    1 
ATOM   4398 C  CB   . VAL   A 1 574 ? -10.191 29.403  26.937  1.00 42.14  ?  576 VAL   A CB   1 
ATOM   4399 C  CG1  . VAL   A 1 574 ? -11.599 29.293  26.371  1.00 42.74  ?  576 VAL   A CG1  1 
ATOM   4400 C  CG2  . VAL   A 1 574 ? -9.544  28.033  26.821  1.00 41.05  ?  576 VAL   A CG2  1 
ATOM   4401 N  N    . ALA   A 1 575 ? -10.159 32.599  27.094  1.00 41.63  ?  577 ALA   A N    1 
ATOM   4402 C  CA   . ALA   A 1 575 ? -10.942 33.857  27.078  1.00 39.52  ?  577 ALA   A CA   1 
ATOM   4403 C  C    . ALA   A 1 575 ? -10.373 34.939  26.139  1.00 39.69  ?  577 ALA   A C    1 
ATOM   4404 O  O    . ALA   A 1 575 ? -11.146 35.709  25.540  1.00 39.14  ?  577 ALA   A O    1 
ATOM   4405 C  CB   . ALA   A 1 575 ? -11.092 34.411  28.489  1.00 40.29  ?  577 ALA   A CB   1 
ATOM   4406 N  N    . ALA   A 1 576 ? -9.041  35.000  26.048  1.00 33.55  ?  578 ALA   A N    1 
ATOM   4407 C  CA   . ALA   A 1 576 ? -8.311  35.894  25.141  1.00 33.95  ?  578 ALA   A CA   1 
ATOM   4408 C  C    . ALA   A 1 576 ? -8.357  35.421  23.674  1.00 34.69  ?  578 ALA   A C    1 
ATOM   4409 O  O    . ALA   A 1 576 ? -8.296  36.243  22.751  1.00 31.30  ?  578 ALA   A O    1 
ATOM   4410 C  CB   . ALA   A 1 576 ? -6.845  35.994  25.560  1.00 31.86  ?  578 ALA   A CB   1 
ATOM   4411 N  N    . SER   A 1 577 ? -8.361  34.100  23.500  1.00 33.32  ?  579 SER   A N    1 
ATOM   4412 C  CA   . SER   A 1 577 ? -8.400  33.471  22.186  1.00 34.85  ?  579 SER   A CA   1 
ATOM   4413 C  C    . SER   A 1 577 ? -9.729  33.721  21.513  1.00 35.00  ?  579 SER   A C    1 
ATOM   4414 O  O    . SER   A 1 577 ? -9.745  34.141  20.379  1.00 37.28  ?  579 SER   A O    1 
ATOM   4415 C  CB   . SER   A 1 577 ? -8.178  31.950  22.281  1.00 34.63  ?  579 SER   A CB   1 
ATOM   4416 O  OG   . SER   A 1 577 ? -6.808  31.629  22.195  1.00 37.77  ?  579 SER   A OG   1 
ATOM   4417 N  N    . GLN   A 1 578 ? -10.838 33.454  22.205  1.00 35.78  ?  580 GLN   A N    1 
ATOM   4418 C  CA   . GLN   A 1 578 ? -12.171 33.732  21.653  1.00 38.87  ?  580 GLN   A CA   1 
ATOM   4419 C  C    . GLN   A 1 578 ? -12.288 35.170  21.170  1.00 39.14  ?  580 GLN   A C    1 
ATOM   4420 O  O    . GLN   A 1 578 ? -12.746 35.434  20.061  1.00 42.18  ?  580 GLN   A O    1 
ATOM   4421 C  CB   . GLN   A 1 578 ? -13.262 33.483  22.690  1.00 40.65  ?  580 GLN   A CB   1 
ATOM   4422 C  CG   . GLN   A 1 578 ? -13.642 32.016  22.825  1.00 42.09  ?  580 GLN   A CG   1 
ATOM   4423 C  CD   . GLN   A 1 578 ? -14.386 31.711  24.116  1.00 44.33  ?  580 GLN   A CD   1 
ATOM   4424 O  OE1  . GLN   A 1 578 ? -15.406 31.040  24.103  1.00 51.07  ?  580 GLN   A OE1  1 
ATOM   4425 N  NE2  . GLN   A 1 578 ? -13.870 32.201  25.237  1.00 48.24  ?  580 GLN   A NE2  1 
ATOM   4426 N  N    . ALA   A 1 579 ? -11.874 36.093  22.023  1.00 41.24  ?  581 ALA   A N    1 
ATOM   4427 C  CA   . ALA   A 1 579 ? -11.981 37.514  21.727  1.00 40.48  ?  581 ALA   A CA   1 
ATOM   4428 C  C    . ALA   A 1 579 ? -11.180 37.894  20.489  1.00 39.66  ?  581 ALA   A C    1 
ATOM   4429 O  O    . ALA   A 1 579 ? -11.653 38.682  19.685  1.00 42.54  ?  581 ALA   A O    1 
ATOM   4430 C  CB   . ALA   A 1 579 ? -11.554 38.343  22.929  1.00 41.05  ?  581 ALA   A CB   1 
ATOM   4431 N  N    . ALA   A 1 580 ? -10.005 37.283  20.311  1.00 41.72  ?  582 ALA   A N    1 
ATOM   4432 C  CA   . ALA   A 1 580 ? -9.136  37.540  19.152  1.00 44.64  ?  582 ALA   A CA   1 
ATOM   4433 C  C    . ALA   A 1 580 ? -9.497  36.783  17.841  1.00 45.34  ?  582 ALA   A C    1 
ATOM   4434 O  O    . ALA   A 1 580 ? -8.682  36.743  16.917  1.00 47.42  ?  582 ALA   A O    1 
ATOM   4435 C  CB   . ALA   A 1 580 ? -7.692  37.236  19.532  1.00 44.59  ?  582 ALA   A CB   1 
ATOM   4436 N  N    . LEU   A 1 581 ? -10.680 36.178  17.760  1.00 43.50  ?  583 LEU   A N    1 
ATOM   4437 C  CA   . LEU   A 1 581 ? -11.066 35.375  16.595  1.00 42.44  ?  583 LEU   A CA   1 
ATOM   4438 C  C    . LEU   A 1 581 ? -12.554 35.564  16.288  1.00 42.91  ?  583 LEU   A C    1 
ATOM   4439 O  O    . LEU   A 1 581 ? -13.348 35.859  17.186  1.00 48.31  ?  583 LEU   A O    1 
ATOM   4440 C  CB   . LEU   A 1 581 ? -10.749 33.882  16.851  1.00 39.35  ?  583 LEU   A CB   1 
ATOM   4441 C  CG   . LEU   A 1 581 ? -9.334  33.462  17.303  1.00 37.73  ?  583 LEU   A CG   1 
ATOM   4442 C  CD1  . LEU   A 1 581 ? -9.289  31.971  17.638  1.00 38.24  ?  583 LEU   A CD1  1 
ATOM   4443 C  CD2  . LEU   A 1 581 ? -8.263  33.786  16.285  1.00 36.91  ?  583 LEU   A CD2  1 
ATOM   4444 N  N    . HIS   B 1 1   ? -13.531 -6.676  -27.358 1.00 44.00  ?  3   HIS   I N    1 
ATOM   4445 C  CA   . HIS   B 1 1   ? -14.288 -7.323  -28.483 1.00 43.01  ?  3   HIS   I CA   1 
ATOM   4446 C  C    . HIS   B 1 1   ? -15.457 -6.381  -28.823 1.00 40.16  ?  3   HIS   I C    1 
ATOM   4447 O  O    . HIS   B 1 1   ? -16.626 -6.746  -28.737 1.00 42.84  ?  3   HIS   I O    1 
ATOM   4448 C  CB   . HIS   B 1 1   ? -14.724 -8.784  -28.131 1.00 42.35  ?  3   HIS   I CB   1 
ATOM   4449 C  CG   . HIS   B 1 1   ? -14.536 -9.774  -29.251 1.00 40.88  ?  3   HIS   I CG   1 
ATOM   4450 N  N    . LYS   B 1 2   ? -15.107 -5.144  -29.198 1.00 39.31  ?  4   LYS   I N    1 
ATOM   4451 C  CA   . LYS   B 1 2   ? -16.085 -4.180  -29.728 1.00 40.12  ?  4   LYS   I CA   1 
ATOM   4452 C  C    . LYS   B 1 2   ? -16.699 -4.692  -31.042 1.00 37.51  ?  4   LYS   I C    1 
ATOM   4453 O  O    . LYS   B 1 2   ? -17.903 -4.546  -31.258 1.00 44.37  ?  4   LYS   I O    1 
ATOM   4454 C  CB   . LYS   B 1 2   ? -15.436 -2.804  -29.950 1.00 36.76  ?  4   LYS   I CB   1 
ATOM   4455 N  N    . SER   B 1 3   ? -15.868 -5.314  -31.887 1.00 32.91  ?  5   SER   I N    1 
ATOM   4456 C  CA   . SER   B 1 3   ? -16.261 -5.738  -33.245 1.00 29.16  ?  5   SER   I CA   1 
ATOM   4457 C  C    . SER   B 1 3   ? -16.070 -7.243  -33.404 1.00 25.20  ?  5   SER   I C    1 
ATOM   4458 O  O    . SER   B 1 3   ? -14.977 -7.711  -33.544 1.00 22.01  ?  5   SER   I O    1 
ATOM   4459 C  CB   . SER   B 1 3   ? -15.456 -4.992  -34.281 1.00 26.78  ?  5   SER   I CB   1 
ATOM   4460 O  OG   . SER   B 1 3   ? -15.715 -5.527  -35.565 1.00 26.77  ?  5   SER   I OG   1 
ATOM   4461 N  N    . GLU   B 1 4   ? -17.158 -7.998  -33.374 1.00 26.99  ?  6   GLU   I N    1 
ATOM   4462 C  CA   . GLU   B 1 4   ? -17.065 -9.462  -33.431 1.00 25.16  ?  6   GLU   I CA   1 
ATOM   4463 C  C    . GLU   B 1 4   ? -16.540 -9.934  -34.789 1.00 24.46  ?  6   GLU   I C    1 
ATOM   4464 O  O    . GLU   B 1 4   ? -15.716 -10.846 -34.805 1.00 26.23  ?  6   GLU   I O    1 
ATOM   4465 C  CB   . GLU   B 1 4   ? -18.407 -10.132 -33.112 1.00 24.75  ?  6   GLU   I CB   1 
ATOM   4466 N  N    . VAL   B 1 5   ? -16.998 -9.355  -35.909 1.00 22.23  ?  7   VAL   I N    1 
ATOM   4467 C  CA   . VAL   B 1 5   ? -16.413 -9.711  -37.210 1.00 21.45  ?  7   VAL   I CA   1 
ATOM   4468 C  C    . VAL   B 1 5   ? -14.887 -9.480  -37.239 1.00 19.87  ?  7   VAL   I C    1 
ATOM   4469 O  O    . VAL   B 1 5   ? -14.165 -10.373 -37.656 1.00 15.97  ?  7   VAL   I O    1 
ATOM   4470 C  CB   . VAL   B 1 5   ? -17.049 -9.102  -38.507 1.00 20.67  ?  7   VAL   I CB   1 
ATOM   4471 C  CG1  . VAL   B 1 5   ? -18.468 -9.511  -38.607 1.00 26.23  ?  7   VAL   I CG1  1 
ATOM   4472 C  CG2  . VAL   B 1 5   ? -16.905 -7.585  -38.648 1.00 19.75  ?  7   VAL   I CG2  1 
ATOM   4473 N  N    . ALA   B 1 6   ? -14.416 -8.301  -36.816 1.00 20.68  ?  8   ALA   I N    1 
ATOM   4474 C  CA   . ALA   B 1 6   ? -12.964 -8.025  -36.820 1.00 21.51  ?  8   ALA   I CA   1 
ATOM   4475 C  C    . ALA   B 1 6   ? -12.204 -9.102  -36.058 1.00 21.20  ?  8   ALA   I C    1 
ATOM   4476 O  O    . ALA   B 1 6   ? -11.278 -9.660  -36.570 1.00 22.94  ?  8   ALA   I O    1 
ATOM   4477 C  CB   . ALA   B 1 6   ? -12.615 -6.647  -36.224 1.00 22.36  ?  8   ALA   I CB   1 
ATOM   4478 N  N    . HIS   B 1 7   ? -12.581 -9.345  -34.822 1.00 23.35  ?  9   HIS   I N    1 
ATOM   4479 C  CA   . HIS   B 1 7   ? -11.880 -10.305 -33.990 1.00 28.28  ?  9   HIS   I CA   1 
ATOM   4480 C  C    . HIS   B 1 7   ? -11.898 -11.734 -34.574 1.00 27.81  ?  9   HIS   I C    1 
ATOM   4481 O  O    . HIS   B 1 7   ? -10.884 -12.437 -34.468 1.00 28.99  ?  9   HIS   I O    1 
ATOM   4482 C  CB   . HIS   B 1 7   ? -12.436 -10.298 -32.556 1.00 32.08  ?  9   HIS   I CB   1 
ATOM   4483 C  CG   . HIS   B 1 7   ? -11.798 -11.305 -31.644 1.00 37.47  ?  9   HIS   I CG   1 
ATOM   4484 N  ND1  . HIS   B 1 7   ? -12.466 -12.423 -31.199 1.00 39.05  ?  9   HIS   I ND1  1 
ATOM   4485 C  CD2  . HIS   B 1 7   ? -10.565 -11.356 -31.080 1.00 42.18  ?  9   HIS   I CD2  1 
ATOM   4486 C  CE1  . HIS   B 1 7   ? -11.681 -13.115 -30.396 1.00 41.48  ?  9   HIS   I CE1  1 
ATOM   4487 N  NE2  . HIS   B 1 7   ? -10.521 -12.490 -30.305 1.00 41.29  ?  9   HIS   I NE2  1 
ATOM   4488 N  N    . ARG   B 1 8   ? -13.019 -12.163 -35.150 1.00 24.67  ?  10  ARG   I N    1 
ATOM   4489 C  CA   . ARG   B 1 8   ? -13.086 -13.461 -35.863 1.00 26.54  ?  10  ARG   I CA   1 
ATOM   4490 C  C    . ARG   B 1 8   ? -12.112 -13.498 -37.028 1.00 23.29  ?  10  ARG   I C    1 
ATOM   4491 O  O    . ARG   B 1 8   ? -11.414 -14.473 -37.227 1.00 22.10  ?  10  ARG   I O    1 
ATOM   4492 C  CB   . ARG   B 1 8   ? -14.521 -13.760 -36.404 1.00 28.31  ?  10  ARG   I CB   1 
ATOM   4493 C  CG   . ARG   B 1 8   ? -15.502 -14.292 -35.374 1.00 31.47  ?  10  ARG   I CG   1 
ATOM   4494 C  CD   . ARG   B 1 8   ? -15.582 -15.820 -35.330 1.00 38.60  ?  10  ARG   I CD   1 
ATOM   4495 N  NE   . ARG   B 1 8   ? -15.712 -16.356 -33.955 1.00 46.80  ?  10  ARG   I NE   1 
ATOM   4496 C  CZ   . ARG   B 1 8   ? -14.695 -16.733 -33.165 1.00 53.50  ?  10  ARG   I CZ   1 
ATOM   4497 N  NH1  . ARG   B 1 8   ? -13.417 -16.660 -33.565 1.00 55.35  ?  10  ARG   I NH1  1 
ATOM   4498 N  NH2  . ARG   B 1 8   ? -14.953 -17.193 -31.944 1.00 56.90  ?  10  ARG   I NH2  1 
ATOM   4499 N  N    . PHE   B 1 9   ? -12.069 -12.404 -37.785 1.00 22.17  ?  11  PHE   I N    1 
ATOM   4500 C  CA   . PHE   B 1 9   ? -11.270 -12.294 -38.985 1.00 20.46  ?  11  PHE   I CA   1 
ATOM   4501 C  C    . PHE   B 1 9   ? -9.777  -12.381 -38.662 1.00 21.66  ?  11  PHE   I C    1 
ATOM   4502 O  O    . PHE   B 1 9   ? -9.028  -12.976 -39.417 1.00 18.61  ?  11  PHE   I O    1 
ATOM   4503 C  CB   . PHE   B 1 9   ? -11.557 -10.958 -39.677 1.00 21.19  ?  11  PHE   I CB   1 
ATOM   4504 C  CG   . PHE   B 1 9   ? -11.029 -10.883 -41.060 1.00 21.42  ?  11  PHE   I CG   1 
ATOM   4505 C  CD1  . PHE   B 1 9   ? -9.717  -10.483 -41.284 1.00 20.81  ?  11  PHE   I CD1  1 
ATOM   4506 C  CD2  . PHE   B 1 9   ? -11.832 -11.243 -42.143 1.00 21.82  ?  11  PHE   I CD2  1 
ATOM   4507 C  CE1  . PHE   B 1 9   ? -9.215  -10.407 -42.556 1.00 20.60  ?  11  PHE   I CE1  1 
ATOM   4508 C  CE2  . PHE   B 1 9   ? -11.343 -11.159 -43.423 1.00 22.92  ?  11  PHE   I CE2  1 
ATOM   4509 C  CZ   . PHE   B 1 9   ? -10.027 -10.751 -43.632 1.00 23.95  ?  11  PHE   I CZ   1 
ATOM   4510 N  N    . LYS   B 1 10  ? -9.364  -11.727 -37.570 1.00 23.43  ?  12  LYS   I N    1 
ATOM   4511 C  CA   . LYS   B 1 10  ? -7.986  -11.798 -37.055 1.00 24.55  ?  12  LYS   I CA   1 
ATOM   4512 C  C    . LYS   B 1 10  ? -7.669  -13.185 -36.523 1.00 24.55  ?  12  LYS   I C    1 
ATOM   4513 O  O    . LYS   B 1 10  ? -6.621  -13.690 -36.811 1.00 27.23  ?  12  LYS   I O    1 
ATOM   4514 C  CB   . LYS   B 1 10  ? -7.739  -10.784 -35.958 1.00 24.77  ?  12  LYS   I CB   1 
ATOM   4515 C  CG   . LYS   B 1 10  ? -7.808  -9.324  -36.412 1.00 26.39  ?  12  LYS   I CG   1 
ATOM   4516 C  CD   . LYS   B 1 10  ? -7.774  -8.465  -35.168 1.00 26.42  ?  12  LYS   I CD   1 
ATOM   4517 C  CE   . LYS   B 1 10  ? -7.727  -7.012  -35.507 1.00 29.27  ?  12  LYS   I CE   1 
ATOM   4518 N  NZ   . LYS   B 1 10  ? -7.477  -6.237  -34.265 1.00 32.23  ?  12  LYS   I NZ   1 
ATOM   4519 N  N    . ASP   B 1 11  ? -8.536  -13.790 -35.737 1.00 26.25  ?  13  ASP   I N    1 
ATOM   4520 C  CA   . ASP   B 1 11  ? -8.263  -15.158 -35.253 1.00 28.99  ?  13  ASP   I CA   1 
ATOM   4521 C  C    . ASP   B 1 11  ? -8.154  -16.159 -36.421 1.00 29.36  ?  13  ASP   I C    1 
ATOM   4522 O  O    . ASP   B 1 11  ? -7.126  -16.795 -36.580 1.00 34.64  ?  13  ASP   I O    1 
ATOM   4523 C  CB   . ASP   B 1 11  ? -9.299  -15.635 -34.225 1.00 32.57  ?  13  ASP   I CB   1 
ATOM   4524 C  CG   . ASP   B 1 11  ? -9.183  -14.906 -32.837 1.00 35.04  ?  13  ASP   I CG   1 
ATOM   4525 O  OD1  . ASP   B 1 11  ? -8.640  -13.772 -32.749 1.00 42.80  ?  13  ASP   I OD1  1 
ATOM   4526 O  OD2  . ASP   B 1 11  ? -9.677  -15.463 -31.832 1.00 37.04  ?  13  ASP   I OD2  1 
ATOM   4527 N  N    . LEU   B 1 12  ? -9.176  -16.239 -37.266 1.00 26.60  ?  14  LEU   I N    1 
ATOM   4528 C  CA   . LEU   B 1 12  ? -9.208  -17.214 -38.359 1.00 25.58  ?  14  LEU   I CA   1 
ATOM   4529 C  C    . LEU   B 1 12  ? -8.168  -16.948 -39.452 1.00 22.38  ?  14  LEU   I C    1 
ATOM   4530 O  O    . LEU   B 1 12  ? -7.582  -17.875 -39.996 1.00 19.82  ?  14  LEU   I O    1 
ATOM   4531 C  CB   . LEU   B 1 12  ? -10.614 -17.257 -39.012 1.00 25.91  ?  14  LEU   I CB   1 
ATOM   4532 C  CG   . LEU   B 1 12  ? -11.834 -18.040 -38.492 1.00 27.60  ?  14  LEU   I CG   1 
ATOM   4533 C  CD1  . LEU   B 1 12  ? -11.495 -19.170 -37.522 1.00 29.84  ?  14  LEU   I CD1  1 
ATOM   4534 C  CD2  . LEU   B 1 12  ? -12.968 -17.204 -37.939 1.00 27.57  ?  14  LEU   I CD2  1 
ATOM   4535 N  N    . GLY   B 1 13  ? -7.975  -15.669 -39.777 1.00 20.98  ?  15  GLY   I N    1 
ATOM   4536 C  CA   . GLY   B 1 13  ? -7.184  -15.254 -40.920 1.00 21.34  ?  15  GLY   I CA   1 
ATOM   4537 C  C    . GLY   B 1 13  ? -8.082  -15.248 -42.154 1.00 20.91  ?  15  GLY   I C    1 
ATOM   4538 O  O    . GLY   B 1 13  ? -9.036  -15.991 -42.199 1.00 21.23  ?  15  GLY   I O    1 
ATOM   4539 N  N    . GLU   B 1 14  ? -7.795  -14.413 -43.140 1.00 20.36  ?  16  GLU   I N    1 
ATOM   4540 C  CA   . GLU   B 1 14  ? -8.672  -14.278 -44.313 1.00 23.99  ?  16  GLU   I CA   1 
ATOM   4541 C  C    . GLU   B 1 14  ? -9.089  -15.559 -45.113 1.00 22.84  ?  16  GLU   I C    1 
ATOM   4542 O  O    . GLU   B 1 14  ? -10.228 -15.697 -45.529 1.00 19.59  ?  16  GLU   I O    1 
ATOM   4543 C  CB   . GLU   B 1 14  ? -8.045  -13.322 -45.297 1.00 26.33  ?  16  GLU   I CB   1 
ATOM   4544 C  CG   . GLU   B 1 14  ? -9.008  -12.851 -46.362 1.00 28.68  ?  16  GLU   I CG   1 
ATOM   4545 C  CD   . GLU   B 1 14  ? -8.509  -11.597 -47.043 1.00 32.73  ?  16  GLU   I CD   1 
ATOM   4546 O  OE1  . GLU   B 1 14  ? -7.378  -11.161 -46.719 1.00 34.49  ?  16  GLU   I OE1  1 
ATOM   4547 O  OE2  . GLU   B 1 14  ? -9.232  -11.071 -47.921 1.00 33.73  ?  16  GLU   I OE2  1 
ATOM   4548 N  N    . GLU   B 1 15  ? -8.154  -16.456 -45.363 1.00 22.23  ?  17  GLU   I N    1 
ATOM   4549 C  CA   . GLU   B 1 15  ? -8.481  -17.667 -46.109 1.00 22.90  ?  17  GLU   I CA   1 
ATOM   4550 C  C    . GLU   B 1 15  ? -9.500  -18.505 -45.409 1.00 19.14  ?  17  GLU   I C    1 
ATOM   4551 O  O    . GLU   B 1 15  ? -10.420 -18.953 -46.031 1.00 16.82  ?  17  GLU   I O    1 
ATOM   4552 C  CB   . GLU   B 1 15  ? -7.233  -18.502 -46.433 1.00 24.99  ?  17  GLU   I CB   1 
ATOM   4553 C  CG   . GLU   B 1 15  ? -6.322  -17.837 -47.457 1.00 28.46  ?  17  GLU   I CG   1 
ATOM   4554 C  CD   . GLU   B 1 15  ? -7.050  -17.488 -48.766 1.00 31.15  ?  17  GLU   I CD   1 
ATOM   4555 O  OE1  . GLU   B 1 15  ? -7.794  -18.351 -49.280 1.00 31.28  ?  17  GLU   I OE1  1 
ATOM   4556 O  OE2  . GLU   B 1 15  ? -6.891  -16.345 -49.256 1.00 34.40  ?  17  GLU   I OE2  1 
ATOM   4557 N  N    . ASN   B 1 16  ? -9.307  -18.740 -44.125 1.00 19.02  ?  18  ASN   I N    1 
ATOM   4558 C  CA   . ASN   B 1 16  ? -10.223 -19.563 -43.325 1.00 18.77  ?  18  ASN   I CA   1 
ATOM   4559 C  C    . ASN   B 1 16  ? -11.585 -18.850 -43.164 1.00 17.52  ?  18  ASN   I C    1 
ATOM   4560 O  O    . ASN   B 1 16  ? -12.622 -19.454 -43.346 1.00 16.30  ?  18  ASN   I O    1 
ATOM   4561 C  CB   . ASN   B 1 16  ? -9.565  -19.937 -41.983 1.00 19.96  ?  18  ASN   I CB   1 
ATOM   4562 C  CG   . ASN   B 1 16  ? -8.389  -20.913 -42.162 1.00 20.77  ?  18  ASN   I CG   1 
ATOM   4563 O  OD1  . ASN   B 1 16  ? -8.449  -21.823 -42.966 1.00 22.06  ?  18  ASN   I OD1  1 
ATOM   4564 N  ND2  . ASN   B 1 16  ? -7.342  -20.734 -41.385 1.00 23.32  ?  18  ASN   I ND2  1 
ATOM   4565 N  N    . PHE   B 1 17  ? -11.556 -17.548 -42.889 1.00 16.99  ?  19  PHE   I N    1 
ATOM   4566 C  CA   . PHE   B 1 17  ? -12.755 -16.726 -42.863 1.00 16.53  ?  19  PHE   I CA   1 
ATOM   4567 C  C    . PHE   B 1 17  ? -13.607 -16.908 -44.099 1.00 17.35  ?  19  PHE   I C    1 
ATOM   4568 O  O    . PHE   B 1 17  ? -14.840 -17.207 -43.971 1.00 17.18  ?  19  PHE   I O    1 
ATOM   4569 C  CB   . PHE   B 1 17  ? -12.393 -15.258 -42.751 1.00 16.74  ?  19  PHE   I CB   1 
ATOM   4570 C  CG   . PHE   B 1 17  ? -13.532 -14.387 -42.391 1.00 17.97  ?  19  PHE   I CG   1 
ATOM   4571 C  CD1  . PHE   B 1 17  ? -13.980 -14.337 -41.083 1.00 18.32  ?  19  PHE   I CD1  1 
ATOM   4572 C  CD2  . PHE   B 1 17  ? -14.158 -13.591 -43.359 1.00 18.54  ?  19  PHE   I CD2  1 
ATOM   4573 C  CE1  . PHE   B 1 17  ? -15.039 -13.498 -40.717 1.00 20.03  ?  19  PHE   I CE1  1 
ATOM   4574 C  CE2  . PHE   B 1 17  ? -15.192 -12.723 -43.005 1.00 18.74  ?  19  PHE   I CE2  1 
ATOM   4575 C  CZ   . PHE   B 1 17  ? -15.654 -12.690 -41.687 1.00 19.25  ?  19  PHE   I CZ   1 
ATOM   4576 N  N    . LYS   B 1 18  ? -12.995 -16.720 -45.281 1.00 16.18  ?  20  LYS   I N    1 
ATOM   4577 C  CA   . LYS   B 1 18  ? -13.757 -16.775 -46.566 1.00 15.95  ?  20  LYS   I CA   1 
ATOM   4578 C  C    . LYS   B 1 18  ? -14.401 -18.135 -46.810 1.00 14.41  ?  20  LYS   I C    1 
ATOM   4579 O  O    . LYS   B 1 18  ? -15.606 -18.189 -47.151 1.00 13.98  ?  20  LYS   I O    1 
ATOM   4580 C  CB   . LYS   B 1 18  ? -12.918 -16.430 -47.761 1.00 17.41  ?  20  LYS   I CB   1 
ATOM   4581 C  CG   . LYS   B 1 18  ? -12.667 -14.929 -47.890 1.00 19.96  ?  20  LYS   I CG   1 
ATOM   4582 C  CD   . LYS   B 1 18  ? -11.910 -14.580 -49.163 1.00 23.32  ?  20  LYS   I CD   1 
ATOM   4583 C  CE   . LYS   B 1 18  ? -11.790 -13.050 -49.246 1.00 28.16  ?  20  LYS   I CE   1 
ATOM   4584 N  NZ   . LYS   B 1 18  ? -11.199 -12.497 -50.497 1.00 31.29  ?  20  LYS   I NZ   1 
ATOM   4585 N  N    . ALA   B 1 19  ? -13.637 -19.202 -46.609 1.00 11.94  ?  21  ALA   I N    1 
ATOM   4586 C  CA   . ALA   B 1 19  ? -14.196 -20.528 -46.731 1.00 12.43  ?  21  ALA   I CA   1 
ATOM   4587 C  C    . ALA   B 1 19  ? -15.351 -20.737 -45.800 1.00 12.84  ?  21  ALA   I C    1 
ATOM   4588 O  O    . ALA   B 1 19  ? -16.327 -21.383 -46.202 1.00 12.71  ?  21  ALA   I O    1 
ATOM   4589 C  CB   . ALA   B 1 19  ? -13.163 -21.635 -46.511 1.00 11.99  ?  21  ALA   I CB   1 
ATOM   4590 N  N    . LEU   B 1 20  ? -15.208 -20.239 -44.533 1.00 12.49  ?  22  LEU   I N    1 
ATOM   4591 C  CA   . LEU   B 1 20  ? -16.127 -20.523 -43.525 1.00 11.75  ?  22  LEU   I CA   1 
ATOM   4592 C  C    . LEU   B 1 20  ? -17.417 -19.794 -43.763 1.00 11.08  ?  22  LEU   I C    1 
ATOM   4593 O  O    . LEU   B 1 20  ? -18.460 -20.336 -43.547 1.00 9.95   ?  22  LEU   I O    1 
ATOM   4594 C  CB   . LEU   B 1 20  ? -15.549 -20.226 -42.117 1.00 11.66  ?  22  LEU   I CB   1 
ATOM   4595 C  CG   . LEU   B 1 20  ? -14.612 -21.335 -41.655 1.00 12.17  ?  22  LEU   I CG   1 
ATOM   4596 C  CD1  . LEU   B 1 20  ? -13.848 -20.894 -40.408 1.00 12.81  ?  22  LEU   I CD1  1 
ATOM   4597 C  CD2  . LEU   B 1 20  ? -15.264 -22.690 -41.444 1.00 12.55  ?  22  LEU   I CD2  1 
ATOM   4598 N  N    . VAL   B 1 21  ? -17.309 -18.548 -44.200 1.00 10.88  ?  23  VAL   I N    1 
ATOM   4599 C  CA   . VAL   B 1 21  ? -18.418 -17.816 -44.612 1.00 11.57  ?  23  VAL   I CA   1 
ATOM   4600 C  C    . VAL   B 1 21  ? -19.109 -18.478 -45.810 1.00 11.63  ?  23  VAL   I C    1 
ATOM   4601 O  O    . VAL   B 1 21  ? -20.334 -18.469 -45.862 1.00 11.89  ?  23  VAL   I O    1 
ATOM   4602 C  CB   . VAL   B 1 21  ? -18.020 -16.395 -44.975 1.00 11.98  ?  23  VAL   I CB   1 
ATOM   4603 C  CG1  . VAL   B 1 21  ? -19.097 -15.717 -45.804 1.00 12.01  ?  23  VAL   I CG1  1 
ATOM   4604 C  CG2  . VAL   B 1 21  ? -17.730 -15.603 -43.698 1.00 12.63  ?  23  VAL   I CG2  1 
ATOM   4605 N  N    . LEU   B 1 22  ? -18.355 -19.002 -46.772 1.00 12.35  ?  24  LEU   I N    1 
ATOM   4606 C  CA   . LEU   B 1 22  ? -18.956 -19.680 -47.912 1.00 13.80  ?  24  LEU   I CA   1 
ATOM   4607 C  C    . LEU   B 1 22  ? -19.717 -20.897 -47.409 1.00 13.67  ?  24  LEU   I C    1 
ATOM   4608 O  O    . LEU   B 1 22  ? -20.849 -21.149 -47.900 1.00 12.88  ?  24  LEU   I O    1 
ATOM   4609 C  CB   . LEU   B 1 22  ? -17.962 -20.105 -49.000 1.00 15.50  ?  24  LEU   I CB   1 
ATOM   4610 C  CG   . LEU   B 1 22  ? -18.500 -21.025 -50.119 1.00 15.95  ?  24  LEU   I CG   1 
ATOM   4611 C  CD1  . LEU   B 1 22  ? -19.440 -20.243 -50.979 1.00 15.89  ?  24  LEU   I CD1  1 
ATOM   4612 C  CD2  . LEU   B 1 22  ? -17.351 -21.514 -50.980 1.00 17.77  ?  24  LEU   I CD2  1 
ATOM   4613 N  N    . ILE   B 1 23  ? -19.145 -21.626 -46.439 1.00 13.38  ?  25  ILE   I N    1 
ATOM   4614 C  CA   . ILE   B 1 23  ? -19.841 -22.844 -45.984 1.00 14.57  ?  25  ILE   I CA   1 
ATOM   4615 C  C    . ILE   B 1 23  ? -21.122 -22.421 -45.277 1.00 16.87  ?  25  ILE   I C    1 
ATOM   4616 O  O    . ILE   B 1 23  ? -22.205 -23.000 -45.537 1.00 15.89  ?  25  ILE   I O    1 
ATOM   4617 C  CB   . ILE   B 1 23  ? -19.020 -23.756 -45.093 1.00 14.88  ?  25  ILE   I CB   1 
ATOM   4618 C  CG1  . ILE   B 1 23  ? -17.730 -24.208 -45.775 1.00 14.93  ?  25  ILE   I CG1  1 
ATOM   4619 C  CG2  . ILE   B 1 23  ? -19.823 -24.968 -44.719 1.00 14.97  ?  25  ILE   I CG2  1 
ATOM   4620 C  CD1  . ILE   B 1 23  ? -16.725 -24.762 -44.782 1.00 15.29  ?  25  ILE   I CD1  1 
ATOM   4621 N  N    . ALA   B 1 24  ? -21.032 -21.370 -44.456 1.00 18.07  ?  26  ALA   I N    1 
ATOM   4622 C  CA   . ALA   B 1 24  ? -22.160 -20.973 -43.655 1.00 19.52  ?  26  ALA   I CA   1 
ATOM   4623 C  C    . ALA   B 1 24  ? -23.337 -20.599 -44.526 1.00 20.23  ?  26  ALA   I C    1 
ATOM   4624 O  O    . ALA   B 1 24  ? -24.440 -21.102 -44.308 1.00 19.65  ?  26  ALA   I O    1 
ATOM   4625 C  CB   . ALA   B 1 24  ? -21.824 -19.844 -42.681 1.00 19.84  ?  26  ALA   I CB   1 
ATOM   4626 N  N    . PHE   B 1 25  ? -23.122 -19.685 -45.472 1.00 20.98  ?  27  PHE   I N    1 
ATOM   4627 C  CA   . PHE   B 1 25  ? -24.158 -19.350 -46.408 1.00 21.58  ?  27  PHE   I CA   1 
ATOM   4628 C  C    . PHE   B 1 25  ? -24.614 -20.560 -47.262 1.00 20.43  ?  27  PHE   I C    1 
ATOM   4629 O  O    . PHE   B 1 25  ? -25.821 -20.726 -47.486 1.00 18.95  ?  27  PHE   I O    1 
ATOM   4630 C  CB   . PHE   B 1 25  ? -23.770 -18.153 -47.265 1.00 22.86  ?  27  PHE   I CB   1 
ATOM   4631 C  CG   . PHE   B 1 25  ? -23.882 -16.875 -46.507 1.00 25.64  ?  27  PHE   I CG   1 
ATOM   4632 C  CD1  . PHE   B 1 25  ? -25.119 -16.368 -46.189 1.00 26.22  ?  27  PHE   I CD1  1 
ATOM   4633 C  CD2  . PHE   B 1 25  ? -22.766 -16.278 -45.972 1.00 28.82  ?  27  PHE   I CD2  1 
ATOM   4634 C  CE1  . PHE   B 1 25  ? -25.230 -15.209 -45.455 1.00 28.05  ?  27  PHE   I CE1  1 
ATOM   4635 C  CE2  . PHE   B 1 25  ? -22.865 -15.121 -45.231 1.00 31.23  ?  27  PHE   I CE2  1 
ATOM   4636 C  CZ   . PHE   B 1 25  ? -24.105 -14.586 -44.965 1.00 30.62  ?  27  PHE   I CZ   1 
ATOM   4637 N  N    . ALA   B 1 26  ? -23.690 -21.400 -47.687 1.00 17.05  ?  28  ALA   I N    1 
ATOM   4638 C  CA   . ALA   B 1 26  ? -24.095 -22.574 -48.483 1.00 18.81  ?  28  ALA   I CA   1 
ATOM   4639 C  C    . ALA   B 1 26  ? -25.116 -23.460 -47.785 1.00 18.18  ?  28  ALA   I C    1 
ATOM   4640 O  O    . ALA   B 1 26  ? -26.032 -23.976 -48.453 1.00 17.40  ?  28  ALA   I O    1 
ATOM   4641 C  CB   . ALA   B 1 26  ? -22.907 -23.400 -48.931 1.00 20.28  ?  28  ALA   I CB   1 
ATOM   4642 N  N    . GLN   B 1 27  ? -25.003 -23.581 -46.460 1.00 17.50  ?  29  GLN   I N    1 
ATOM   4643 C  CA   . GLN   B 1 27  ? -25.868 -24.438 -45.668 1.00 17.53  ?  29  GLN   I CA   1 
ATOM   4644 C  C    . GLN   B 1 27  ? -27.341 -23.888 -45.504 1.00 19.03  ?  29  GLN   I C    1 
ATOM   4645 O  O    . GLN   B 1 27  ? -28.271 -24.672 -45.344 1.00 16.96  ?  29  GLN   I O    1 
ATOM   4646 C  CB   . GLN   B 1 27  ? -25.177 -24.790 -44.341 1.00 17.13  ?  29  GLN   I CB   1 
ATOM   4647 C  CG   . GLN   B 1 27  ? -23.825 -25.554 -44.538 1.00 16.47  ?  29  GLN   I CG   1 
ATOM   4648 C  CD   . GLN   B 1 27  ? -23.123 -25.934 -43.235 1.00 16.79  ?  29  GLN   I CD   1 
ATOM   4649 O  OE1  . GLN   B 1 27  ? -22.953 -25.106 -42.336 1.00 13.93  ?  29  GLN   I OE1  1 
ATOM   4650 N  NE2  . GLN   B 1 27  ? -22.732 -27.218 -43.114 1.00 17.83  ?  29  GLN   I NE2  1 
ATOM   4651 N  N    . TYR   B 1 28  ? -27.519 -22.567 -45.600 1.00 21.76  ?  30  TYR   I N    1 
ATOM   4652 C  CA   . TYR   B 1 28  ? -28.834 -21.867 -45.513 1.00 25.14  ?  30  TYR   I CA   1 
ATOM   4653 C  C    . TYR   B 1 28  ? -29.456 -21.416 -46.848 1.00 26.39  ?  30  TYR   I C    1 
ATOM   4654 O  O    . TYR   B 1 28  ? -30.695 -21.193 -46.923 1.00 29.48  ?  30  TYR   I O    1 
ATOM   4655 C  CB   . TYR   B 1 28  ? -28.696 -20.590 -44.679 1.00 26.62  ?  30  TYR   I CB   1 
ATOM   4656 C  CG   . TYR   B 1 28  ? -28.507 -20.864 -43.212 1.00 28.69  ?  30  TYR   I CG   1 
ATOM   4657 C  CD1  . TYR   B 1 28  ? -27.252 -21.181 -42.709 1.00 30.15  ?  30  TYR   I CD1  1 
ATOM   4658 C  CD2  . TYR   B 1 28  ? -29.574 -20.816 -42.340 1.00 30.34  ?  30  TYR   I CD2  1 
ATOM   4659 C  CE1  . TYR   B 1 28  ? -27.056 -21.441 -41.378 1.00 32.27  ?  30  TYR   I CE1  1 
ATOM   4660 C  CE2  . TYR   B 1 28  ? -29.403 -21.065 -40.998 1.00 33.20  ?  30  TYR   I CE2  1 
ATOM   4661 C  CZ   . TYR   B 1 28  ? -28.139 -21.373 -40.518 1.00 36.18  ?  30  TYR   I CZ   1 
ATOM   4662 O  OH   . TYR   B 1 28  ? -27.964 -21.642 -39.184 1.00 41.50  ?  30  TYR   I OH   1 
ATOM   4663 N  N    . LEU   B 1 29  ? -28.607 -21.186 -47.851 1.00 22.85  ?  31  LEU   I N    1 
ATOM   4664 C  CA   . LEU   B 1 29  ? -29.043 -20.774 -49.146 1.00 22.22  ?  31  LEU   I CA   1 
ATOM   4665 C  C    . LEU   B 1 29  ? -28.686 -21.865 -50.085 1.00 21.55  ?  31  LEU   I C    1 
ATOM   4666 O  O    . LEU   B 1 29  ? -28.004 -21.654 -51.078 1.00 21.78  ?  31  LEU   I O    1 
ATOM   4667 C  CB   . LEU   B 1 29  ? -28.388 -19.433 -49.509 1.00 24.58  ?  31  LEU   I CB   1 
ATOM   4668 C  CG   . LEU   B 1 29  ? -28.850 -18.309 -48.587 1.00 23.69  ?  31  LEU   I CG   1 
ATOM   4669 C  CD1  . LEU   B 1 29  ? -28.034 -17.072 -48.796 1.00 25.66  ?  31  LEU   I CD1  1 
ATOM   4670 C  CD2  . LEU   B 1 29  ? -30.301 -17.961 -48.878 1.00 24.58  ?  31  LEU   I CD2  1 
ATOM   4671 N  N    . GLN   B 1 30  ? -29.210 -23.051 -49.801 1.00 22.52  ?  32  GLN   I N    1 
ATOM   4672 C  CA   . GLN   B 1 30  ? -28.758 -24.271 -50.459 1.00 22.96  ?  32  GLN   I CA   1 
ATOM   4673 C  C    . GLN   B 1 30  ? -29.132 -24.359 -51.944 1.00 27.79  ?  32  GLN   I C    1 
ATOM   4674 O  O    . GLN   B 1 30  ? -28.580 -25.212 -52.635 1.00 26.82  ?  32  GLN   I O    1 
ATOM   4675 C  CB   . GLN   B 1 30  ? -29.289 -25.491 -49.740 1.00 23.49  ?  32  GLN   I CB   1 
ATOM   4676 C  CG   . GLN   B 1 30  ? -29.041 -25.462 -48.247 1.00 22.98  ?  32  GLN   I CG   1 
ATOM   4677 C  CD   . GLN   B 1 30  ? -29.798 -26.534 -47.514 1.00 23.62  ?  32  GLN   I CD   1 
ATOM   4678 O  OE1  . GLN   B 1 30  ? -29.751 -27.683 -47.880 1.00 33.49  ?  32  GLN   I OE1  1 
ATOM   4679 N  NE2  . GLN   B 1 30  ? -30.423 -26.176 -46.439 1.00 26.32  ?  32  GLN   I NE2  1 
ATOM   4680 N  N    . GLN   B 1 31  ? -30.020 -23.482 -52.431 1.00 28.18  ?  33  GLN   I N    1 
ATOM   4681 C  CA   . GLN   B 1 31  ? -30.452 -23.445 -53.848 1.00 33.78  ?  33  GLN   I CA   1 
ATOM   4682 C  C    . GLN   B 1 31  ? -30.043 -22.176 -54.552 1.00 33.83  ?  33  GLN   I C    1 
ATOM   4683 O  O    . GLN   B 1 31  ? -30.382 -22.010 -55.708 1.00 36.12  ?  33  GLN   I O    1 
ATOM   4684 C  CB   . GLN   B 1 31  ? -31.991 -23.541 -53.979 1.00 37.90  ?  33  GLN   I CB   1 
ATOM   4685 C  CG   . GLN   B 1 31  ? -32.649 -24.667 -53.185 1.00 43.17  ?  33  GLN   I CG   1 
ATOM   4686 C  CD   . GLN   B 1 31  ? -32.112 -26.049 -53.538 1.00 50.44  ?  33  GLN   I CD   1 
ATOM   4687 O  OE1  . GLN   B 1 31  ? -31.652 -26.283 -54.660 1.00 58.12  ?  33  GLN   I OE1  1 
ATOM   4688 N  NE2  . GLN   B 1 31  ? -32.186 -26.984 -52.579 1.00 54.89  ?  33  GLN   I NE2  1 
ATOM   4689 N  N    . CYS   B 1 32  ? -29.377 -21.255 -53.856 1.00 33.59  ?  34  CYS   I N    1 
ATOM   4690 C  CA   . CYS   B 1 32  ? -28.693 -20.168 -54.528 1.00 35.36  ?  34  CYS   I CA   1 
ATOM   4691 C  C    . CYS   B 1 32  ? -27.472 -20.714 -55.253 1.00 33.28  ?  34  CYS   I C    1 
ATOM   4692 O  O    . CYS   B 1 32  ? -26.739 -21.502 -54.675 1.00 28.38  ?  34  CYS   I O    1 
ATOM   4693 C  CB   . CYS   B 1 32  ? -28.271 -19.077 -53.535 1.00 38.81  ?  34  CYS   I CB   1 
ATOM   4694 S  SG   . CYS   B 1 32  ? -29.698 -18.114 -53.038 1.00 46.05  ?  34  CYS   I SG   1 
ATOM   4695 N  N    . PRO   B 1 33  ? -27.258 -20.297 -56.516 1.00 32.88  ?  35  PRO   I N    1 
ATOM   4696 C  CA   . PRO   B 1 33  ? -26.123 -20.792 -57.257 1.00 32.61  ?  35  PRO   I CA   1 
ATOM   4697 C  C    . PRO   B 1 33  ? -24.795 -20.238 -56.747 1.00 30.07  ?  35  PRO   I C    1 
ATOM   4698 O  O    . PRO   B 1 33  ? -24.751 -19.159 -56.168 1.00 32.27  ?  35  PRO   I O    1 
ATOM   4699 C  CB   . PRO   B 1 33  ? -26.402 -20.306 -58.687 1.00 34.80  ?  35  PRO   I CB   1 
ATOM   4700 C  CG   . PRO   B 1 33  ? -27.289 -19.116 -58.534 1.00 34.74  ?  35  PRO   I CG   1 
ATOM   4701 C  CD   . PRO   B 1 33  ? -28.142 -19.462 -57.358 1.00 34.49  ?  35  PRO   I CD   1 
ATOM   4702 N  N    . PHE   B 1 34  ? -23.741 -21.005 -56.974 1.00 27.26  ?  36  PHE   I N    1 
ATOM   4703 C  CA   . PHE   B 1 34  ? -22.363 -20.660 -56.640 1.00 26.25  ?  36  PHE   I CA   1 
ATOM   4704 C  C    . PHE   B 1 34  ? -21.981 -19.185 -56.798 1.00 26.51  ?  36  PHE   I C    1 
ATOM   4705 O  O    . PHE   B 1 34  ? -21.388 -18.603 -55.882 1.00 22.66  ?  36  PHE   I O    1 
ATOM   4706 C  CB   . PHE   B 1 34  ? -21.383 -21.536 -57.434 1.00 25.83  ?  36  PHE   I CB   1 
ATOM   4707 C  CG   . PHE   B 1 34  ? -19.956 -21.289 -57.099 1.00 26.26  ?  36  PHE   I CG   1 
ATOM   4708 C  CD1  . PHE   B 1 34  ? -19.475 -21.584 -55.820 1.00 28.58  ?  36  PHE   I CD1  1 
ATOM   4709 C  CD2  . PHE   B 1 34  ? -19.092 -20.720 -58.023 1.00 27.09  ?  36  PHE   I CD2  1 
ATOM   4710 C  CE1  . PHE   B 1 34  ? -18.151 -21.344 -55.479 1.00 27.85  ?  36  PHE   I CE1  1 
ATOM   4711 C  CE2  . PHE   B 1 34  ? -17.765 -20.472 -57.694 1.00 26.91  ?  36  PHE   I CE2  1 
ATOM   4712 C  CZ   . PHE   B 1 34  ? -17.290 -20.790 -56.416 1.00 28.56  ?  36  PHE   I CZ   1 
ATOM   4713 N  N    . GLU   B 1 35  ? -22.329 -18.592 -57.930 1.00 29.33  ?  37  GLU   I N    1 
ATOM   4714 C  CA   . GLU   B 1 35  ? -21.900 -17.220 -58.247 1.00 32.35  ?  37  GLU   I CA   1 
ATOM   4715 C  C    . GLU   B 1 35  ? -22.579 -16.184 -57.365 1.00 33.69  ?  37  GLU   I C    1 
ATOM   4716 O  O    . GLU   B 1 35  ? -21.982 -15.119 -57.154 1.00 33.59  ?  37  GLU   I O    1 
ATOM   4717 C  CB   . GLU   B 1 35  ? -22.067 -16.838 -59.722 1.00 33.85  ?  37  GLU   I CB   1 
ATOM   4718 C  CG   . GLU   B 1 35  ? -21.175 -17.651 -60.645 1.00 37.88  ?  37  GLU   I CG   1 
ATOM   4719 C  CD   . GLU   B 1 35  ? -21.622 -19.112 -60.762 1.00 40.45  ?  37  GLU   I CD   1 
ATOM   4720 O  OE1  . GLU   B 1 35  ? -22.789 -19.431 -60.417 1.00 37.09  ?  37  GLU   I OE1  1 
ATOM   4721 O  OE2  . GLU   B 1 35  ? -20.803 -19.954 -61.184 1.00 45.64  ?  37  GLU   I OE2  1 
ATOM   4722 N  N    . ASP   B 1 36  ? -23.786 -16.482 -56.842 1.00 32.97  ?  38  ASP   I N    1 
ATOM   4723 C  CA   . ASP   B 1 36  ? -24.400 -15.633 -55.803 1.00 33.32  ?  38  ASP   I CA   1 
ATOM   4724 C  C    . ASP   B 1 36  ? -23.576 -15.729 -54.507 1.00 28.39  ?  38  ASP   I C    1 
ATOM   4725 O  O    . ASP   B 1 36  ? -23.184 -14.714 -53.986 1.00 29.93  ?  38  ASP   I O    1 
ATOM   4726 C  CB   . ASP   B 1 36  ? -25.861 -16.016 -55.502 1.00 37.17  ?  38  ASP   I CB   1 
ATOM   4727 C  CG   . ASP   B 1 36  ? -26.784 -15.895 -56.734 1.00 42.23  ?  38  ASP   I CG   1 
ATOM   4728 O  OD1  . ASP   B 1 36  ? -26.325 -15.443 -57.810 1.00 41.73  ?  38  ASP   I OD1  1 
ATOM   4729 O  OD2  . ASP   B 1 36  ? -27.982 -16.255 -56.614 1.00 47.03  ?  38  ASP   I OD2  1 
ATOM   4730 N  N    . HIS   B 1 37  ? -23.305 -16.940 -54.022 1.00 23.73  ?  39  HIS   I N    1 
ATOM   4731 C  CA   . HIS   B 1 37  ? -22.458 -17.150 -52.818 1.00 24.68  ?  39  HIS   I CA   1 
ATOM   4732 C  C    . HIS   B 1 37  ? -21.079 -16.489 -52.881 1.00 23.61  ?  39  HIS   I C    1 
ATOM   4733 O  O    . HIS   B 1 37  ? -20.686 -15.911 -51.879 1.00 20.55  ?  39  HIS   I O    1 
ATOM   4734 C  CB   . HIS   B 1 37  ? -22.238 -18.636 -52.526 1.00 23.95  ?  39  HIS   I CB   1 
ATOM   4735 C  CG   . HIS   B 1 37  ? -23.444 -19.302 -51.977 1.00 24.92  ?  39  HIS   I CG   1 
ATOM   4736 N  ND1  . HIS   B 1 37  ? -24.405 -19.867 -52.778 1.00 27.00  ?  39  HIS   I ND1  1 
ATOM   4737 C  CD2  . HIS   B 1 37  ? -23.881 -19.448 -50.704 1.00 24.98  ?  39  HIS   I CD2  1 
ATOM   4738 C  CE1  . HIS   B 1 37  ? -25.370 -20.364 -52.024 1.00 25.28  ?  39  HIS   I CE1  1 
ATOM   4739 N  NE2  . HIS   B 1 37  ? -25.071 -20.135 -50.761 1.00 26.38  ?  39  HIS   I NE2  1 
ATOM   4740 N  N    . VAL   B 1 38  ? -20.352 -16.601 -54.010 1.00 23.53  ?  40  VAL   I N    1 
ATOM   4741 C  CA   . VAL   B 1 38  ? -19.046 -15.888 -54.161 1.00 27.59  ?  40  VAL   I CA   1 
ATOM   4742 C  C    . VAL   B 1 38  ? -19.260 -14.376 -53.908 1.00 29.86  ?  40  VAL   I C    1 
ATOM   4743 O  O    . VAL   B 1 38  ? -18.416 -13.721 -53.249 1.00 28.32  ?  40  VAL   I O    1 
ATOM   4744 C  CB   . VAL   B 1 38  ? -18.307 -16.109 -55.534 1.00 26.42  ?  40  VAL   I CB   1 
ATOM   4745 C  CG1  . VAL   B 1 38  ? -17.086 -15.180 -55.680 1.00 26.94  ?  40  VAL   I CG1  1 
ATOM   4746 C  CG2  . VAL   B 1 38  ? -17.882 -17.561 -55.694 1.00 25.84  ?  40  VAL   I CG2  1 
ATOM   4747 N  N    . LYS   B 1 39  ? -20.370 -13.831 -54.411 1.00 28.84  ?  41  LYS   I N    1 
ATOM   4748 C  CA   . LYS   B 1 39  ? -20.663 -12.410 -54.183 1.00 28.86  ?  41  LYS   I CA   1 
ATOM   4749 C  C    . LYS   B 1 39  ? -20.962 -12.168 -52.688 1.00 27.93  ?  41  LYS   I C    1 
ATOM   4750 O  O    . LYS   B 1 39  ? -20.540 -11.122 -52.131 1.00 27.09  ?  41  LYS   I O    1 
ATOM   4751 C  CB   . LYS   B 1 39  ? -21.789 -11.893 -55.094 1.00 27.08  ?  41  LYS   I CB   1 
ATOM   4752 N  N    . LEU   B 1 40  ? -21.646 -13.106 -52.019 1.00 25.69  ?  42  LEU   I N    1 
ATOM   4753 C  CA   . LEU   B 1 40  ? -21.910 -12.912 -50.570 1.00 28.03  ?  42  LEU   I CA   1 
ATOM   4754 C  C    . LEU   B 1 40  ? -20.603 -12.885 -49.825 1.00 25.43  ?  42  LEU   I C    1 
ATOM   4755 O  O    . LEU   B 1 40  ? -20.322 -11.914 -49.173 1.00 25.88  ?  42  LEU   I O    1 
ATOM   4756 C  CB   . LEU   B 1 40  ? -22.828 -13.962 -49.947 1.00 29.65  ?  42  LEU   I CB   1 
ATOM   4757 C  CG   . LEU   B 1 40  ? -24.219 -14.024 -50.588 1.00 30.46  ?  42  LEU   I CG   1 
ATOM   4758 C  CD1  . LEU   B 1 40  ? -25.018 -15.083 -49.882 1.00 30.06  ?  42  LEU   I CD1  1 
ATOM   4759 C  CD2  . LEU   B 1 40  ? -24.936 -12.685 -50.569 1.00 31.53  ?  42  LEU   I CD2  1 
ATOM   4760 N  N    . VAL   B 1 41  ? -19.809 -13.942 -49.974 1.00 23.83  ?  43  VAL   I N    1 
ATOM   4761 C  CA   . VAL   B 1 41  ? -18.475 -14.036 -49.365 1.00 22.02  ?  43  VAL   I CA   1 
ATOM   4762 C  C    . VAL   B 1 41  ? -17.655 -12.756 -49.568 1.00 20.85  ?  43  VAL   I C    1 
ATOM   4763 O  O    . VAL   B 1 41  ? -17.147 -12.189 -48.607 1.00 17.99  ?  43  VAL   I O    1 
ATOM   4764 C  CB   . VAL   B 1 41  ? -17.728 -15.254 -49.855 1.00 20.39  ?  43  VAL   I CB   1 
ATOM   4765 C  CG1  . VAL   B 1 41  ? -16.237 -15.157 -49.569 1.00 21.34  ?  43  VAL   I CG1  1 
ATOM   4766 C  CG2  . VAL   B 1 41  ? -18.332 -16.499 -49.222 1.00 22.06  ?  43  VAL   I CG2  1 
ATOM   4767 N  N    . ASN   B 1 42  ? -17.578 -12.294 -50.793 1.00 21.65  ?  44  ASN   I N    1 
ATOM   4768 C  CA   . ASN   B 1 42  ? -16.709 -11.167 -51.117 1.00 25.23  ?  44  ASN   I CA   1 
ATOM   4769 C  C    . ASN   B 1 42  ? -17.249 -9.925  -50.406 1.00 23.15  ?  44  ASN   I C    1 
ATOM   4770 O  O    . ASN   B 1 42  ? -16.480 -9.217  -49.770 1.00 22.36  ?  44  ASN   I O    1 
ATOM   4771 C  CB   . ASN   B 1 42  ? -16.575 -10.974 -52.634 1.00 26.46  ?  44  ASN   I CB   1 
ATOM   4772 C  CG   . ASN   B 1 42  ? -15.832 -12.136 -53.332 1.00 28.50  ?  44  ASN   I CG   1 
ATOM   4773 O  OD1  . ASN   B 1 42  ? -15.005 -12.849 -52.751 1.00 27.81  ?  44  ASN   I OD1  1 
ATOM   4774 N  ND2  . ASN   B 1 42  ? -16.141 -12.318 -54.617 1.00 29.14  ?  44  ASN   I ND2  1 
ATOM   4775 N  N    . GLU   B 1 43  ? -18.578 -9.745  -50.402 1.00 24.00  ?  45  GLU   I N    1 
ATOM   4776 C  CA   . GLU   B 1 43  ? -19.231 -8.653  -49.659 1.00 25.22  ?  45  GLU   I CA   1 
ATOM   4777 C  C    . GLU   B 1 43  ? -19.044 -8.712  -48.127 1.00 24.47  ?  45  GLU   I C    1 
ATOM   4778 O  O    . GLU   B 1 43  ? -18.723 -7.709  -47.497 1.00 24.60  ?  45  GLU   I O    1 
ATOM   4779 C  CB   . GLU   B 1 43  ? -20.735 -8.567  -49.998 1.00 28.46  ?  45  GLU   I CB   1 
ATOM   4780 C  CG   . GLU   B 1 43  ? -21.053 -8.078  -51.413 1.00 30.05  ?  45  GLU   I CG   1 
ATOM   4781 C  CD   . GLU   B 1 43  ? -22.477 -8.450  -51.877 1.00 33.40  ?  45  GLU   I CD   1 
ATOM   4782 O  OE1  . GLU   B 1 43  ? -23.022 -9.495  -51.461 1.00 38.24  ?  45  GLU   I OE1  1 
ATOM   4783 O  OE2  . GLU   B 1 43  ? -23.064 -7.711  -52.691 1.00 38.08  ?  45  GLU   I OE2  1 
ATOM   4784 N  N    . VAL   B 1 44  ? -19.254 -9.878  -47.513 1.00 21.77  ?  46  VAL   I N    1 
ATOM   4785 C  CA   . VAL   B 1 44  ? -18.979 -10.035 -46.099 1.00 21.05  ?  46  VAL   I CA   1 
ATOM   4786 C  C    . VAL   B 1 44  ? -17.492 -9.737  -45.778 1.00 21.60  ?  46  VAL   I C    1 
ATOM   4787 O  O    . VAL   B 1 44  ? -17.186 -9.160  -44.736 1.00 22.04  ?  46  VAL   I O    1 
ATOM   4788 C  CB   . VAL   B 1 44  ? -19.262 -11.476 -45.628 1.00 21.36  ?  46  VAL   I CB   1 
ATOM   4789 C  CG1  . VAL   B 1 44  ? -19.022 -11.604 -44.143 1.00 20.79  ?  46  VAL   I CG1  1 
ATOM   4790 C  CG2  . VAL   B 1 44  ? -20.663 -11.922 -46.006 1.00 20.80  ?  46  VAL   I CG2  1 
ATOM   4791 N  N    . THR   B 1 45  ? -16.586 -10.209 -46.641 1.00 22.88  ?  47  THR   I N    1 
ATOM   4792 C  CA   . THR   B 1 45  ? -15.132 -10.072 -46.441 1.00 22.85  ?  47  THR   I CA   1 
ATOM   4793 C  C    . THR   B 1 45  ? -14.626 -8.608  -46.669 1.00 23.36  ?  47  THR   I C    1 
ATOM   4794 O  O    . THR   B 1 45  ? -13.756 -8.180  -45.920 1.00 26.68  ?  47  THR   I O    1 
ATOM   4795 C  CB   . THR   B 1 45  ? -14.363 -11.093 -47.277 1.00 22.86  ?  47  THR   I CB   1 
ATOM   4796 O  OG1  . THR   B 1 45  ? -14.828 -12.416 -46.961 1.00 21.84  ?  47  THR   I OG1  1 
ATOM   4797 C  CG2  . THR   B 1 45  ? -12.875 -11.055 -46.964 1.00 24.58  ?  47  THR   I CG2  1 
ATOM   4798 N  N    . GLU   B 1 46  ? -15.161 -7.862  -47.646 1.00 21.68  ?  48  GLU   I N    1 
ATOM   4799 C  CA   . GLU   B 1 46  ? -14.918 -6.392  -47.770 1.00 21.94  ?  48  GLU   I CA   1 
ATOM   4800 C  C    . GLU   B 1 46  ? -15.252 -5.714  -46.462 1.00 21.87  ?  48  GLU   I C    1 
ATOM   4801 O  O    . GLU   B 1 46  ? -14.449 -4.966  -45.921 1.00 22.82  ?  48  GLU   I O    1 
ATOM   4802 C  CB   . GLU   B 1 46  ? -15.789 -5.713  -48.851 1.00 20.30  ?  48  GLU   I CB   1 
ATOM   4803 N  N    . PHE   B 1 47  ? -16.462 -5.976  -45.973 1.00 20.98  ?  49  PHE   I N    1 
ATOM   4804 C  CA   . PHE   B 1 47  ? -16.923 -5.447  -44.712 1.00 21.50  ?  49  PHE   I CA   1 
ATOM   4805 C  C    . PHE   B 1 47  ? -16.011 -5.793  -43.505 1.00 21.46  ?  49  PHE   I C    1 
ATOM   4806 O  O    . PHE   B 1 47  ? -15.513 -4.888  -42.807 1.00 19.43  ?  49  PHE   I O    1 
ATOM   4807 C  CB   . PHE   B 1 47  ? -18.368 -5.894  -44.472 1.00 24.18  ?  49  PHE   I CB   1 
ATOM   4808 C  CG   . PHE   B 1 47  ? -18.875 -5.495  -43.149 1.00 24.90  ?  49  PHE   I CG   1 
ATOM   4809 C  CD1  . PHE   B 1 47  ? -19.046 -4.140  -42.859 1.00 26.71  ?  49  PHE   I CD1  1 
ATOM   4810 C  CD2  . PHE   B 1 47  ? -19.082 -6.447  -42.166 1.00 24.40  ?  49  PHE   I CD2  1 
ATOM   4811 C  CE1  . PHE   B 1 47  ? -19.461 -3.747  -41.603 1.00 26.86  ?  49  PHE   I CE1  1 
ATOM   4812 C  CE2  . PHE   B 1 47  ? -19.496 -6.063  -40.931 1.00 26.40  ?  49  PHE   I CE2  1 
ATOM   4813 C  CZ   . PHE   B 1 47  ? -19.703 -4.720  -40.651 1.00 26.45  ?  49  PHE   I CZ   1 
ATOM   4814 N  N    . ALA   B 1 48  ? -15.784 -7.086  -43.272 1.00 18.03  ?  50  ALA   I N    1 
ATOM   4815 C  CA   . ALA   B 1 48  ? -14.916 -7.549  -42.214 1.00 19.52  ?  50  ALA   I CA   1 
ATOM   4816 C  C    . ALA   B 1 48  ? -13.582 -6.762  -42.111 1.00 19.44  ?  50  ALA   I C    1 
ATOM   4817 O  O    . ALA   B 1 48  ? -13.164 -6.362  -40.993 1.00 17.29  ?  50  ALA   I O    1 
ATOM   4818 C  CB   . ALA   B 1 48  ? -14.602 -9.052  -42.393 1.00 18.74  ?  50  ALA   I CB   1 
ATOM   4819 N  N    . LYS   B 1 49  ? -12.958 -6.574  -43.267 1.00 20.14  ?  51  LYS   I N    1 
ATOM   4820 C  CA   . LYS   B 1 49  ? -11.700 -5.830  -43.422 1.00 24.86  ?  51  LYS   I CA   1 
ATOM   4821 C  C    . LYS   B 1 49  ? -11.790 -4.401  -42.963 1.00 23.88  ?  51  LYS   I C    1 
ATOM   4822 O  O    . LYS   B 1 49  ? -10.847 -3.895  -42.376 1.00 23.17  ?  51  LYS   I O    1 
ATOM   4823 C  CB   . LYS   B 1 49  ? -11.223 -5.849  -44.880 1.00 25.77  ?  51  LYS   I CB   1 
ATOM   4824 C  CG   . LYS   B 1 49  ? -10.505 -7.142  -45.214 1.00 28.66  ?  51  LYS   I CG   1 
ATOM   4825 C  CD   . LYS   B 1 49  ? -9.307  -6.868  -46.108 1.00 31.70  ?  51  LYS   I CD   1 
ATOM   4826 C  CE   . LYS   B 1 49  ? -8.688  -8.169  -46.623 1.00 33.64  ?  51  LYS   I CE   1 
ATOM   4827 N  NZ   . LYS   B 1 49  ? -9.401  -8.670  -47.831 1.00 34.45  ?  51  LYS   I NZ   1 
ATOM   4828 N  N    . THR   B 1 50  ? -12.943 -3.810  -43.239 1.00 23.62  ?  52  THR   I N    1 
ATOM   4829 C  CA   . THR   B 1 50  ? -13.388 -2.494  -42.768 1.00 25.79  ?  52  THR   I CA   1 
ATOM   4830 C  C    . THR   B 1 50  ? -13.333 -2.404  -41.243 1.00 25.53  ?  52  THR   I C    1 
ATOM   4831 O  O    . THR   B 1 50  ? -13.018 -1.349  -40.691 1.00 24.79  ?  52  THR   I O    1 
ATOM   4832 C  CB   . THR   B 1 50  ? -14.835 -2.223  -43.301 1.00 25.59  ?  52  THR   I CB   1 
ATOM   4833 O  OG1  . THR   B 1 50  ? -14.784 -1.382  -44.446 1.00 29.68  ?  52  THR   I OG1  1 
ATOM   4834 C  CG2  . THR   B 1 50  ? -15.732 -1.637  -42.334 1.00 26.27  ?  52  THR   I CG2  1 
ATOM   4835 N  N    . CYS   B 1 51  ? -13.666 -3.508  -40.588 1.00 21.28  ?  53  CYS   I N    1 
ATOM   4836 C  CA   . CYS   B 1 51  ? -13.784 -3.547  -39.165 1.00 21.11  ?  53  CYS   I CA   1 
ATOM   4837 C  C    . CYS   B 1 51  ? -12.402 -3.789  -38.578 1.00 20.47  ?  53  CYS   I C    1 
ATOM   4838 O  O    . CYS   B 1 51  ? -12.131 -3.321  -37.486 1.00 18.39  ?  53  CYS   I O    1 
ATOM   4839 C  CB   . CYS   B 1 51  ? -14.806 -4.625  -38.732 1.00 22.04  ?  53  CYS   I CB   1 
ATOM   4840 S  SG   . CYS   B 1 51  ? -16.496 -4.395  -39.375 1.00 21.77  ?  53  CYS   I SG   1 
ATOM   4841 N  N    . VAL   B 1 52  ? -11.567 -4.554  -39.297 1.00 22.47  ?  54  VAL   I N    1 
ATOM   4842 C  CA   . VAL   B 1 52  ? -10.156 -4.800  -38.932 1.00 21.51  ?  54  VAL   I CA   1 
ATOM   4843 C  C    . VAL   B 1 52  ? -9.455  -3.448  -38.961 1.00 22.37  ?  54  VAL   I C    1 
ATOM   4844 O  O    . VAL   B 1 52  ? -8.936  -3.029  -37.952 1.00 23.97  ?  54  VAL   I O    1 
ATOM   4845 C  CB   . VAL   B 1 52  ? -9.476  -5.838  -39.830 1.00 21.03  ?  54  VAL   I CB   1 
ATOM   4846 C  CG1  . VAL   B 1 52  ? -7.971  -5.944  -39.543 1.00 22.68  ?  54  VAL   I CG1  1 
ATOM   4847 C  CG2  . VAL   B 1 52  ? -10.078 -7.225  -39.627 1.00 20.38  ?  54  VAL   I CG2  1 
ATOM   4848 N  N    . ALA   B 1 53  ? -9.571  -2.724  -40.061 1.00 24.42  ?  55  ALA   I N    1 
ATOM   4849 C  CA   . ALA   B 1 53  ? -9.048  -1.349  -40.156 1.00 28.06  ?  55  ALA   I CA   1 
ATOM   4850 C  C    . ALA   B 1 53  ? -9.532  -0.416  -39.018 1.00 32.28  ?  55  ALA   I C    1 
ATOM   4851 O  O    . ALA   B 1 53  ? -8.745  0.381   -38.507 1.00 33.65  ?  55  ALA   I O    1 
ATOM   4852 C  CB   . ALA   B 1 53  ? -9.375  -0.739  -41.507 1.00 27.74  ?  55  ALA   I CB   1 
ATOM   4853 N  N    . ASP   B 1 54  ? -10.793 -0.540  -38.599 1.00 32.14  ?  56  ASP   I N    1 
ATOM   4854 C  CA   . ASP   B 1 54  ? -11.345 0.328   -37.568 1.00 32.45  ?  56  ASP   I CA   1 
ATOM   4855 C  C    . ASP   B 1 54  ? -12.608 -0.225  -36.898 1.00 32.24  ?  56  ASP   I C    1 
ATOM   4856 O  O    . ASP   B 1 54  ? -13.694 -0.203  -37.480 1.00 34.72  ?  56  ASP   I O    1 
ATOM   4857 C  CB   . ASP   B 1 54  ? -11.652 1.667   -38.247 1.00 36.06  ?  56  ASP   I CB   1 
ATOM   4858 C  CG   . ASP   B 1 54  ? -12.232 2.687   -37.312 1.00 35.56  ?  56  ASP   I CG   1 
ATOM   4859 O  OD1  . ASP   B 1 54  ? -12.282 2.462   -36.071 1.00 36.17  ?  56  ASP   I OD1  1 
ATOM   4860 O  OD2  . ASP   B 1 54  ? -12.624 3.738   -37.861 1.00 37.93  ?  56  ASP   I OD2  1 
ATOM   4861 N  N    . GLU   B 1 55  ? -12.482 -0.658  -35.655 1.00 34.98  ?  57  GLU   I N    1 
ATOM   4862 C  CA   . GLU   B 1 55  ? -13.602 -1.280  -34.904 1.00 35.92  ?  57  GLU   I CA   1 
ATOM   4863 C  C    . GLU   B 1 55  ? -14.810 -0.367  -34.655 1.00 36.01  ?  57  GLU   I C    1 
ATOM   4864 O  O    . GLU   B 1 55  ? -15.889 -0.851  -34.324 1.00 35.84  ?  57  GLU   I O    1 
ATOM   4865 C  CB   . GLU   B 1 55  ? -13.106 -1.841  -33.566 1.00 37.00  ?  57  GLU   I CB   1 
ATOM   4866 N  N    . SER   B 1 56  ? -14.621 0.942   -34.782 1.00 34.37  ?  58  SER   I N    1 
ATOM   4867 C  CA   . SER   B 1 56  ? -15.716 1.918   -34.637 1.00 32.82  ?  58  SER   I CA   1 
ATOM   4868 C  C    . SER   B 1 56  ? -16.493 2.205   -35.921 1.00 33.19  ?  58  SER   I C    1 
ATOM   4869 O  O    . SER   B 1 56  ? -17.508 2.891   -35.863 1.00 39.38  ?  58  SER   I O    1 
ATOM   4870 C  CB   . SER   B 1 56  ? -15.169 3.247   -34.110 1.00 32.64  ?  58  SER   I CB   1 
ATOM   4871 O  OG   . SER   B 1 56  ? -14.945 3.154   -32.716 1.00 36.40  ?  58  SER   I OG   1 
ATOM   4872 N  N    . ALA   B 1 57  ? -16.015 1.748   -37.081 1.00 33.72  ?  59  ALA   I N    1 
ATOM   4873 C  CA   . ALA   B 1 57  ? -16.711 2.029   -38.364 1.00 33.64  ?  59  ALA   I CA   1 
ATOM   4874 C  C    . ALA   B 1 57  ? -18.111 1.386   -38.417 1.00 36.45  ?  59  ALA   I C    1 
ATOM   4875 O  O    . ALA   B 1 57  ? -18.342 0.298   -37.859 1.00 35.42  ?  59  ALA   I O    1 
ATOM   4876 C  CB   . ALA   B 1 57  ? -15.873 1.579   -39.552 1.00 32.82  ?  59  ALA   I CB   1 
ATOM   4877 N  N    . GLU   B 1 58  ? -19.039 2.090   -39.073 1.00 38.57  ?  60  GLU   I N    1 
ATOM   4878 C  CA   . GLU   B 1 58  ? -20.435 1.683   -39.222 1.00 35.96  ?  60  GLU   I CA   1 
ATOM   4879 C  C    . GLU   B 1 58  ? -20.642 0.172   -39.317 1.00 34.28  ?  60  GLU   I C    1 
ATOM   4880 O  O    . GLU   B 1 58  ? -19.972 -0.506  -40.072 1.00 38.29  ?  60  GLU   I O    1 
ATOM   4881 C  CB   . GLU   B 1 58  ? -21.037 2.316   -40.479 1.00 37.84  ?  60  GLU   I CB   1 
ATOM   4882 N  N    . ASN   B 1 59  ? -21.583 -0.323  -38.533 1.00 33.62  ?  61  ASN   I N    1 
ATOM   4883 C  CA   . ASN   B 1 59  ? -22.048 -1.711  -38.552 1.00 32.93  ?  61  ASN   I CA   1 
ATOM   4884 C  C    . ASN   B 1 59  ? -21.049 -2.706  -38.028 1.00 27.04  ?  61  ASN   I C    1 
ATOM   4885 O  O    . ASN   B 1 59  ? -21.398 -3.849  -37.880 1.00 25.57  ?  61  ASN   I O    1 
ATOM   4886 C  CB   . ASN   B 1 59  ? -22.537 -2.151  -39.938 1.00 34.66  ?  61  ASN   I CB   1 
ATOM   4887 C  CG   . ASN   B 1 59  ? -23.548 -1.204  -40.537 1.00 37.46  ?  61  ASN   I CG   1 
ATOM   4888 O  OD1  . ASN   B 1 59  ? -23.521 -0.942  -41.756 1.00 38.35  ?  61  ASN   I OD1  1 
ATOM   4889 N  ND2  . ASN   B 1 59  ? -24.460 -0.691  -39.699 1.00 35.26  ?  61  ASN   I ND2  1 
ATOM   4890 N  N    . CYS   B 1 60  ? -19.829 -2.278  -37.722 1.00 25.59  ?  62  CYS   I N    1 
ATOM   4891 C  CA   . CYS   B 1 60  ? -18.812 -3.199  -37.229 1.00 28.41  ?  62  CYS   I CA   1 
ATOM   4892 C  C    . CYS   B 1 60  ? -19.083 -3.701  -35.823 1.00 27.74  ?  62  CYS   I C    1 
ATOM   4893 O  O    . CYS   B 1 60  ? -18.704 -4.819  -35.486 1.00 25.32  ?  62  CYS   I O    1 
ATOM   4894 C  CB   . CYS   B 1 60  ? -17.446 -2.552  -37.248 1.00 26.87  ?  62  CYS   I CB   1 
ATOM   4895 S  SG   . CYS   B 1 60  ? -16.863 -2.375  -38.922 1.00 28.20  ?  62  CYS   I SG   1 
ATOM   4896 N  N    . ASP   B 1 61  ? -19.746 -2.875  -35.021 1.00 28.60  ?  63  ASP   I N    1 
ATOM   4897 C  CA   . ASP   B 1 61  ? -20.155 -3.253  -33.657 1.00 30.62  ?  63  ASP   I CA   1 
ATOM   4898 C  C    . ASP   B 1 61  ? -21.379 -4.181  -33.568 1.00 29.42  ?  63  ASP   I C    1 
ATOM   4899 O  O    . ASP   B 1 61  ? -21.730 -4.608  -32.469 1.00 27.11  ?  63  ASP   I O    1 
ATOM   4900 C  CB   . ASP   B 1 61  ? -20.406 -1.997  -32.805 1.00 33.15  ?  63  ASP   I CB   1 
ATOM   4901 C  CG   . ASP   B 1 61  ? -21.551 -1.143  -33.330 1.00 36.85  ?  63  ASP   I CG   1 
ATOM   4902 O  OD1  . ASP   B 1 61  ? -21.833 -1.156  -34.582 1.00 35.99  ?  63  ASP   I OD1  1 
ATOM   4903 O  OD2  . ASP   B 1 61  ? -22.156 -0.447  -32.479 1.00 40.05  ?  63  ASP   I OD2  1 
ATOM   4904 N  N    . LYS   B 1 62  ? -22.021 -4.501  -34.693 1.00 27.04  ?  64  LYS   I N    1 
ATOM   4905 C  CA   . LYS   B 1 62  ? -23.081 -5.488  -34.658 1.00 27.74  ?  64  LYS   I CA   1 
ATOM   4906 C  C    . LYS   B 1 62  ? -22.590 -6.918  -34.510 1.00 27.79  ?  64  LYS   I C    1 
ATOM   4907 O  O    . LYS   B 1 62  ? -21.481 -7.289  -34.901 1.00 28.35  ?  64  LYS   I O    1 
ATOM   4908 C  CB   . LYS   B 1 62  ? -23.979 -5.370  -35.873 1.00 29.12  ?  64  LYS   I CB   1 
ATOM   4909 C  CG   . LYS   B 1 62  ? -24.722 -4.036  -35.931 1.00 32.27  ?  64  LYS   I CG   1 
ATOM   4910 C  CD   . LYS   B 1 62  ? -25.952 -3.953  -35.028 1.00 34.34  ?  64  LYS   I CD   1 
ATOM   4911 N  N    . SER   B 1 63  ? -23.478 -7.704  -33.942 1.00 27.69  ?  65  SER   I N    1 
ATOM   4912 C  CA   . SER   B 1 63  ? -23.333 -9.138  -33.724 1.00 29.54  ?  65  SER   I CA   1 
ATOM   4913 C  C    . SER   B 1 63  ? -23.109 -9.896  -35.035 1.00 28.22  ?  65  SER   I C    1 
ATOM   4914 O  O    . SER   B 1 63  ? -23.609 -9.491  -36.114 1.00 25.42  ?  65  SER   I O    1 
ATOM   4915 C  CB   . SER   B 1 63  ? -24.635 -9.626  -33.036 1.00 30.71  ?  65  SER   I CB   1 
ATOM   4916 O  OG   . SER   B 1 63  ? -24.690 -11.020 -32.903 1.00 35.58  ?  65  SER   I OG   1 
ATOM   4917 N  N    . LEU   B 1 64  ? -22.360 -10.990 -34.952 1.00 27.03  ?  66  LEU   I N    1 
ATOM   4918 C  CA   . LEU   B 1 64  ? -22.211 -11.869 -36.096 1.00 28.40  ?  66  LEU   I CA   1 
ATOM   4919 C  C    . LEU   B 1 64  ? -23.556 -12.436 -36.543 1.00 25.86  ?  66  LEU   I C    1 
ATOM   4920 O  O    . LEU   B 1 64  ? -23.785 -12.566 -37.764 1.00 26.00  ?  66  LEU   I O    1 
ATOM   4921 C  CB   . LEU   B 1 64  ? -21.195 -12.981 -35.837 1.00 30.21  ?  66  LEU   I CB   1 
ATOM   4922 C  CG   . LEU   B 1 64  ? -19.734 -12.536 -35.900 1.00 32.16  ?  66  LEU   I CG   1 
ATOM   4923 C  CD1  . LEU   B 1 64  ? -18.934 -13.047 -34.696 1.00 39.53  ?  66  LEU   I CD1  1 
ATOM   4924 C  CD2  . LEU   B 1 64  ? -19.067 -12.968 -37.189 1.00 33.91  ?  66  LEU   I CD2  1 
ATOM   4925 N  N    . HIS   B 1 65  ? -24.435 -12.747 -35.585 1.00 24.51  ?  67  HIS   I N    1 
ATOM   4926 C  CA   . HIS   B 1 65  ? -25.825 -13.262 -35.899 1.00 25.43  ?  67  HIS   I CA   1 
ATOM   4927 C  C    . HIS   B 1 65  ? -26.711 -12.240 -36.616 1.00 22.77  ?  67  HIS   I C    1 
ATOM   4928 O  O    . HIS   B 1 65  ? -27.461 -12.607 -37.514 1.00 21.38  ?  67  HIS   I O    1 
ATOM   4929 C  CB   . HIS   B 1 65  ? -26.547 -13.758 -34.633 1.00 25.90  ?  67  HIS   I CB   1 
ATOM   4930 C  CG   . HIS   B 1 65  ? -25.916 -14.948 -33.960 1.00 24.37  ?  67  HIS   I CG   1 
ATOM   4931 N  ND1  . HIS   B 1 65  ? -25.059 -14.815 -32.889 1.00 25.44  ?  67  HIS   I ND1  1 
ATOM   4932 C  CD2  . HIS   B 1 65  ? -26.082 -16.285 -34.139 1.00 27.37  ?  67  HIS   I CD2  1 
ATOM   4933 C  CE1  . HIS   B 1 65  ? -24.677 -16.013 -32.478 1.00 26.54  ?  67  HIS   I CE1  1 
ATOM   4934 N  NE2  . HIS   B 1 65  ? -25.285 -16.926 -33.221 1.00 26.79  ?  67  HIS   I NE2  1 
ATOM   4935 N  N    . THR   B 1 66  ? -26.596 -10.963 -36.216 1.00 22.37  ?  68  THR   I N    1 
ATOM   4936 C  CA   . THR   B 1 66  ? -27.284 -9.825  -36.864 1.00 21.78  ?  68  THR   I CA   1 
ATOM   4937 C  C    . THR   B 1 66  ? -26.878 -9.701  -38.312 1.00 22.59  ?  68  THR   I C    1 
ATOM   4938 O  O    . THR   B 1 66  ? -27.729 -9.699  -39.194 1.00 21.58  ?  68  THR   I O    1 
ATOM   4939 C  CB   . THR   B 1 66  ? -26.932 -8.491  -36.188 1.00 21.95  ?  68  THR   I CB   1 
ATOM   4940 O  OG1  . THR   B 1 66  ? -27.326 -8.542  -34.826 1.00 24.13  ?  68  THR   I OG1  1 
ATOM   4941 C  CG2  . THR   B 1 66  ? -27.644 -7.245  -36.863 1.00 22.56  ?  68  THR   I CG2  1 
ATOM   4942 N  N    . LEU   B 1 67  ? -25.561 -9.637  -38.560 1.00 21.90  ?  69  LEU   I N    1 
ATOM   4943 C  CA   . LEU   B 1 67  ? -25.007 -9.489  -39.903 1.00 20.92  ?  69  LEU   I CA   1 
ATOM   4944 C  C    . LEU   B 1 67  ? -25.318 -10.696 -40.801 1.00 19.73  ?  69  LEU   I C    1 
ATOM   4945 O  O    . LEU   B 1 67  ? -25.717 -10.527 -41.960 1.00 18.46  ?  69  LEU   I O    1 
ATOM   4946 C  CB   . LEU   B 1 67  ? -23.486 -9.262  -39.837 1.00 22.66  ?  69  LEU   I CB   1 
ATOM   4947 C  CG   . LEU   B 1 67  ? -22.983 -7.981  -39.158 1.00 25.10  ?  69  LEU   I CG   1 
ATOM   4948 C  CD1  . LEU   B 1 67  ? -21.513 -8.183  -38.768 1.00 25.00  ?  69  LEU   I CD1  1 
ATOM   4949 C  CD2  . LEU   B 1 67  ? -23.226 -6.707  -39.999 1.00 24.53  ?  69  LEU   I CD2  1 
ATOM   4950 N  N    . PHE   B 1 68  ? -25.147 -11.911 -40.270 1.00 18.01  ?  70  PHE   I N    1 
ATOM   4951 C  CA   . PHE   B 1 68  ? -25.529 -13.116 -41.018 1.00 18.56  ?  70  PHE   I CA   1 
ATOM   4952 C  C    . PHE   B 1 68  ? -26.989 -13.063 -41.461 1.00 18.16  ?  70  PHE   I C    1 
ATOM   4953 O  O    . PHE   B 1 68  ? -27.283 -13.304 -42.620 1.00 19.69  ?  70  PHE   I O    1 
ATOM   4954 C  CB   . PHE   B 1 68  ? -25.324 -14.376 -40.172 1.00 20.08  ?  70  PHE   I CB   1 
ATOM   4955 C  CG   . PHE   B 1 68  ? -25.548 -15.649 -40.922 1.00 22.66  ?  70  PHE   I CG   1 
ATOM   4956 C  CD1  . PHE   B 1 68  ? -24.593 -16.109 -41.831 1.00 23.83  ?  70  PHE   I CD1  1 
ATOM   4957 C  CD2  . PHE   B 1 68  ? -26.704 -16.400 -40.724 1.00 25.57  ?  70  PHE   I CD2  1 
ATOM   4958 C  CE1  . PHE   B 1 68  ? -24.788 -17.286 -42.530 1.00 23.63  ?  70  PHE   I CE1  1 
ATOM   4959 C  CE2  . PHE   B 1 68  ? -26.907 -17.593 -41.424 1.00 25.43  ?  70  PHE   I CE2  1 
ATOM   4960 C  CZ   . PHE   B 1 68  ? -25.928 -18.036 -42.320 1.00 25.23  ?  70  PHE   I CZ   1 
ATOM   4961 N  N    . GLY   B 1 69  ? -27.897 -12.783 -40.536 1.00 18.01  ?  71  GLY   I N    1 
ATOM   4962 C  CA   . GLY   B 1 69  ? -29.338 -12.736 -40.853 1.00 18.48  ?  71  GLY   I CA   1 
ATOM   4963 C  C    . GLY   B 1 69  ? -29.659 -11.540 -41.751 1.00 19.83  ?  71  GLY   I C    1 
ATOM   4964 O  O    . GLY   B 1 69  ? -30.383 -11.684 -42.767 1.00 21.32  ?  71  GLY   I O    1 
ATOM   4965 N  N    . ASP   B 1 70  ? -29.070 -10.375 -41.470 1.00 21.04  ?  72  ASP   I N    1 
ATOM   4966 C  CA   . ASP   B 1 70  ? -29.325 -9.202  -42.340 1.00 23.67  ?  72  ASP   I CA   1 
ATOM   4967 C  C    . ASP   B 1 70  ? -28.964 -9.534  -43.762 1.00 24.26  ?  72  ASP   I C    1 
ATOM   4968 O  O    . ASP   B 1 70  ? -29.666 -9.104  -44.693 1.00 26.06  ?  72  ASP   I O    1 
ATOM   4969 C  CB   . ASP   B 1 70  ? -28.524 -7.965  -41.911 1.00 29.03  ?  72  ASP   I CB   1 
ATOM   4970 C  CG   . ASP   B 1 70  ? -28.972 -7.369  -40.564 1.00 32.31  ?  72  ASP   I CG   1 
ATOM   4971 O  OD1  . ASP   B 1 70  ? -30.072 -7.717  -40.038 1.00 35.35  ?  72  ASP   I OD1  1 
ATOM   4972 O  OD2  . ASP   B 1 70  ? -28.206 -6.524  -40.039 1.00 35.58  ?  72  ASP   I OD2  1 
ATOM   4973 N  N    . LYS   B 1 71  ? -27.888 -10.326 -43.958 1.00 24.79  ?  73  LYS   I N    1 
ATOM   4974 C  CA   . LYS   B 1 71  ? -27.391 -10.653 -45.333 1.00 23.89  ?  73  LYS   I CA   1 
ATOM   4975 C  C    . LYS   B 1 71  ? -28.275 -11.649 -46.028 1.00 22.81  ?  73  LYS   I C    1 
ATOM   4976 O  O    . LYS   B 1 71  ? -28.573 -11.490 -47.189 1.00 21.68  ?  73  LYS   I O    1 
ATOM   4977 C  CB   . LYS   B 1 71  ? -25.914 -11.164 -45.360 1.00 24.40  ?  73  LYS   I CB   1 
ATOM   4978 C  CG   . LYS   B 1 71  ? -24.942 -10.114 -45.895 1.00 27.31  ?  73  LYS   I CG   1 
ATOM   4979 C  CD   . LYS   B 1 71  ? -24.638 -10.293 -47.384 1.00 28.73  ?  73  LYS   I CD   1 
ATOM   4980 C  CE   . LYS   B 1 71  ? -24.477 -8.996  -48.154 1.00 31.47  ?  73  LYS   I CE   1 
ATOM   4981 N  NZ   . LYS   B 1 71  ? -23.776 -7.916  -47.430 1.00 32.84  ?  73  LYS   I NZ   1 
ATOM   4982 N  N    . LEU   B 1 72  ? -28.636 -12.709 -45.326 1.00 24.78  ?  74  LEU   I N    1 
ATOM   4983 C  CA   . LEU   B 1 72  ? -29.737 -13.594 -45.748 1.00 27.47  ?  74  LEU   I CA   1 
ATOM   4984 C  C    . LEU   B 1 72  ? -30.980 -12.771 -46.183 1.00 27.60  ?  74  LEU   I C    1 
ATOM   4985 O  O    . LEU   B 1 72  ? -31.549 -12.984 -47.253 1.00 25.83  ?  74  LEU   I O    1 
ATOM   4986 C  CB   . LEU   B 1 72  ? -30.116 -14.555 -44.616 1.00 27.07  ?  74  LEU   I CB   1 
ATOM   4987 C  CG   . LEU   B 1 72  ? -29.702 -16.036 -44.618 1.00 29.65  ?  74  LEU   I CG   1 
ATOM   4988 C  CD1  . LEU   B 1 72  ? -28.332 -16.316 -45.177 1.00 29.31  ?  74  LEU   I CD1  1 
ATOM   4989 C  CD2  . LEU   B 1 72  ? -29.850 -16.655 -43.216 1.00 28.40  ?  74  LEU   I CD2  1 
ATOM   4990 N  N    . CYS   B 1 73  ? -31.353 -11.789 -45.384 1.00 30.38  ?  75  CYS   I N    1 
ATOM   4991 C  CA   . CYS   B 1 73  ? -32.560 -10.982 -45.705 1.00 32.37  ?  75  CYS   I CA   1 
ATOM   4992 C  C    . CYS   B 1 73  ? -32.422 -10.040 -46.896 1.00 32.38  ?  75  CYS   I C    1 
ATOM   4993 O  O    . CYS   B 1 73  ? -33.429 -9.557  -47.390 1.00 32.77  ?  75  CYS   I O    1 
ATOM   4994 C  CB   . CYS   B 1 73  ? -33.026 -10.225 -44.477 1.00 31.42  ?  75  CYS   I CB   1 
ATOM   4995 S  SG   . CYS   B 1 73  ? -33.598 -11.374 -43.205 1.00 35.52  ?  75  CYS   I SG   1 
ATOM   4996 N  N    . THR   B 1 74  ? -31.192 -9.811  -47.362 1.00 32.34  ?  76  THR   I N    1 
ATOM   4997 C  CA   . THR   B 1 74  ? -30.932 -9.004  -48.555 1.00 33.57  ?  76  THR   I CA   1 
ATOM   4998 C  C    . THR   B 1 74  ? -31.051 -9.764  -49.875 1.00 32.11  ?  76  THR   I C    1 
ATOM   4999 O  O    . THR   B 1 74  ? -31.119 -9.140  -50.933 1.00 30.69  ?  76  THR   I O    1 
ATOM   5000 C  CB   . THR   B 1 74  ? -29.517 -8.361  -48.504 1.00 35.94  ?  76  THR   I CB   1 
ATOM   5001 O  OG1  . THR   B 1 74  ? -28.497 -9.376  -48.457 1.00 38.07  ?  76  THR   I OG1  1 
ATOM   5002 C  CG2  . THR   B 1 74  ? -29.388 -7.438  -47.310 1.00 35.48  ?  76  THR   I CG2  1 
ATOM   5003 N  N    . VAL   B 1 75  ? -31.029 -11.095 -49.808 1.00 29.73  ?  77  VAL   I N    1 
ATOM   5004 C  CA   . VAL   B 1 75  ? -31.212 -11.954 -50.966 1.00 30.60  ?  77  VAL   I CA   1 
ATOM   5005 C  C    . VAL   B 1 75  ? -32.598 -11.667 -51.550 1.00 33.56  ?  77  VAL   I C    1 
ATOM   5006 O  O    . VAL   B 1 75  ? -33.606 -11.725 -50.826 1.00 33.03  ?  77  VAL   I O    1 
ATOM   5007 C  CB   . VAL   B 1 75  ? -31.076 -13.463 -50.574 1.00 31.61  ?  77  VAL   I CB   1 
ATOM   5008 C  CG1  . VAL   B 1 75  ? -31.570 -14.387 -51.679 1.00 33.58  ?  77  VAL   I CG1  1 
ATOM   5009 C  CG2  . VAL   B 1 75  ? -29.636 -13.812 -50.244 1.00 30.75  ?  77  VAL   I CG2  1 
ATOM   5010 N  N    . ALA   B 1 76  ? -32.652 -11.354 -52.847 1.00 34.83  ?  78  ALA   I N    1 
ATOM   5011 C  CA   . ALA   B 1 76  ? -33.883 -10.819 -53.466 1.00 35.94  ?  78  ALA   I CA   1 
ATOM   5012 C  C    . ALA   B 1 76  ? -34.908 -11.914 -53.772 1.00 33.54  ?  78  ALA   I C    1 
ATOM   5013 O  O    . ALA   B 1 76  ? -36.095 -11.731 -53.579 1.00 36.42  ?  78  ALA   I O    1 
ATOM   5014 C  CB   . ALA   B 1 76  ? -33.553 -10.035 -54.718 1.00 38.83  ?  78  ALA   I CB   1 
ATOM   5015 N  N    . THR   B 1 77  ? -34.444 -13.070 -54.197 1.00 29.98  ?  79  THR   I N    1 
ATOM   5016 C  CA   . THR   B 1 77  ? -35.337 -14.177 -54.479 1.00 28.83  ?  79  THR   I CA   1 
ATOM   5017 C  C    . THR   B 1 77  ? -35.660 -15.014 -53.235 1.00 26.74  ?  79  THR   I C    1 
ATOM   5018 O  O    . THR   B 1 77  ? -36.118 -16.140 -53.365 1.00 26.49  ?  79  THR   I O    1 
ATOM   5019 C  CB   . THR   B 1 77  ? -34.700 -15.090 -55.553 1.00 29.53  ?  79  THR   I CB   1 
ATOM   5020 N  N    . LEU   B 1 78  ? -35.385 -14.509 -52.035 1.00 27.82  ?  80  LEU   I N    1 
ATOM   5021 C  CA   . LEU   B 1 78  ? -35.488 -15.333 -50.825 1.00 28.64  ?  80  LEU   I CA   1 
ATOM   5022 C  C    . LEU   B 1 78  ? -36.888 -15.924 -50.720 1.00 28.36  ?  80  LEU   I C    1 
ATOM   5023 O  O    . LEU   B 1 78  ? -37.042 -17.141 -50.550 1.00 28.63  ?  80  LEU   I O    1 
ATOM   5024 C  CB   . LEU   B 1 78  ? -35.165 -14.526 -49.553 1.00 28.71  ?  80  LEU   I CB   1 
ATOM   5025 C  CG   . LEU   B 1 78  ? -34.978 -15.298 -48.217 1.00 28.21  ?  80  LEU   I CG   1 
ATOM   5026 C  CD1  . LEU   B 1 78  ? -33.730 -16.153 -48.269 1.00 28.91  ?  80  LEU   I CD1  1 
ATOM   5027 C  CD2  . LEU   B 1 78  ? -34.888 -14.342 -47.026 1.00 27.28  ?  80  LEU   I CD2  1 
ATOM   5028 N  N    . ARG   B 1 79  ? -37.885 -15.054 -50.839 1.00 27.45  ?  81  ARG   I N    1 
ATOM   5029 C  CA   . ARG   B 1 79  ? -39.279 -15.451 -50.873 1.00 30.53  ?  81  ARG   I CA   1 
ATOM   5030 C  C    . ARG   B 1 79  ? -39.584 -16.403 -52.000 1.00 32.51  ?  81  ARG   I C    1 
ATOM   5031 O  O    . ARG   B 1 79  ? -40.080 -17.502 -51.743 1.00 36.11  ?  81  ARG   I O    1 
ATOM   5032 C  CB   . ARG   B 1 79  ? -40.168 -14.208 -50.983 1.00 33.11  ?  81  ARG   I CB   1 
ATOM   5033 C  CG   . ARG   B 1 79  ? -41.637 -14.478 -51.271 1.00 38.82  ?  81  ARG   I CG   1 
ATOM   5034 C  CD   . ARG   B 1 79  ? -42.575 -13.447 -50.621 1.00 40.61  ?  81  ARG   I CD   1 
ATOM   5035 N  NE   . ARG   B 1 79  ? -43.089 -14.028 -49.387 1.00 44.33  ?  81  ARG   I NE   1 
ATOM   5036 C  CZ   . ARG   B 1 79  ? -42.769 -13.686 -48.136 1.00 45.50  ?  81  ARG   I CZ   1 
ATOM   5037 N  NH1  . ARG   B 1 79  ? -41.966 -12.659 -47.838 1.00 43.53  ?  81  ARG   I NH1  1 
ATOM   5038 N  NH2  . ARG   B 1 79  ? -43.306 -14.385 -47.147 1.00 46.41  ?  81  ARG   I NH2  1 
ATOM   5039 N  N    . GLU   B 1 80  ? -39.272 -16.016 -53.237 1.00 28.71  ?  82  GLU   I N    1 
ATOM   5040 C  CA   . GLU   B 1 80  ? -39.660 -16.838 -54.374 1.00 31.94  ?  82  GLU   I CA   1 
ATOM   5041 C  C    . GLU   B 1 80  ? -39.014 -18.228 -54.263 1.00 34.03  ?  82  GLU   I C    1 
ATOM   5042 O  O    . GLU   B 1 80  ? -39.627 -19.241 -54.619 1.00 34.49  ?  82  GLU   I O    1 
ATOM   5043 C  CB   . GLU   B 1 80  ? -39.311 -16.139 -55.703 1.00 30.49  ?  82  GLU   I CB   1 
ATOM   5044 N  N    . THR   B 1 81  ? -37.791 -18.275 -53.727 1.00 33.03  ?  83  THR   I N    1 
ATOM   5045 C  CA   . THR   B 1 81  ? -36.994 -19.476 -53.763 1.00 32.07  ?  83  THR   I CA   1 
ATOM   5046 C  C    . THR   B 1 81  ? -37.222 -20.306 -52.501 1.00 29.37  ?  83  THR   I C    1 
ATOM   5047 O  O    . THR   B 1 81  ? -37.400 -21.514 -52.615 1.00 27.01  ?  83  THR   I O    1 
ATOM   5048 C  CB   . THR   B 1 81  ? -35.486 -19.143 -53.992 1.00 33.77  ?  83  THR   I CB   1 
ATOM   5049 O  OG1  . THR   B 1 81  ? -35.325 -18.315 -55.154 1.00 35.30  ?  83  THR   I OG1  1 
ATOM   5050 C  CG2  . THR   B 1 81  ? -34.667 -20.382 -54.205 1.00 35.48  ?  83  THR   I CG2  1 
ATOM   5051 N  N    . TYR   B 1 82  ? -37.216 -19.671 -51.319 1.00 28.31  ?  84  TYR   I N    1 
ATOM   5052 C  CA   . TYR   B 1 82  ? -37.241 -20.395 -50.005 1.00 30.25  ?  84  TYR   I CA   1 
ATOM   5053 C  C    . TYR   B 1 82  ? -38.552 -20.261 -49.170 1.00 31.48  ?  84  TYR   I C    1 
ATOM   5054 O  O    . TYR   B 1 82  ? -38.707 -20.935 -48.163 1.00 30.44  ?  84  TYR   I O    1 
ATOM   5055 C  CB   . TYR   B 1 82  ? -36.008 -20.038 -49.156 1.00 30.39  ?  84  TYR   I CB   1 
ATOM   5056 C  CG   . TYR   B 1 82  ? -34.677 -20.194 -49.901 1.00 30.19  ?  84  TYR   I CG   1 
ATOM   5057 C  CD1  . TYR   B 1 82  ? -34.011 -21.426 -49.956 1.00 27.05  ?  84  TYR   I CD1  1 
ATOM   5058 C  CD2  . TYR   B 1 82  ? -34.099 -19.109 -50.540 1.00 29.16  ?  84  TYR   I CD2  1 
ATOM   5059 C  CE1  . TYR   B 1 82  ? -32.828 -21.567 -50.645 1.00 27.95  ?  84  TYR   I CE1  1 
ATOM   5060 C  CE2  . TYR   B 1 82  ? -32.908 -19.231 -51.206 1.00 29.40  ?  84  TYR   I CE2  1 
ATOM   5061 C  CZ   . TYR   B 1 82  ? -32.264 -20.450 -51.249 1.00 28.95  ?  84  TYR   I CZ   1 
ATOM   5062 O  OH   . TYR   B 1 82  ? -31.079 -20.519 -51.951 1.00 28.85  ?  84  TYR   I OH   1 
ATOM   5063 N  N    . GLY   B 1 83  ? -39.500 -19.430 -49.621 1.00 34.90  ?  85  GLY   I N    1 
ATOM   5064 C  CA   . GLY   B 1 83  ? -40.864 -19.431 -49.093 1.00 34.22  ?  85  GLY   I CA   1 
ATOM   5065 C  C    . GLY   B 1 83  ? -40.941 -18.903 -47.675 1.00 35.40  ?  85  GLY   I C    1 
ATOM   5066 O  O    . GLY   B 1 83  ? -40.691 -17.706 -47.434 1.00 38.42  ?  85  GLY   I O    1 
ATOM   5067 N  N    . GLU   B 1 84  ? -41.270 -19.793 -46.735 1.00 32.54  ?  86  GLU   I N    1 
ATOM   5068 C  CA   . GLU   B 1 84  ? -41.332 -19.443 -45.293 1.00 36.22  ?  86  GLU   I CA   1 
ATOM   5069 C  C    . GLU   B 1 84  ? -40.063 -18.833 -44.714 1.00 31.47  ?  86  GLU   I C    1 
ATOM   5070 O  O    . GLU   B 1 84  ? -40.141 -18.061 -43.760 1.00 28.29  ?  86  GLU   I O    1 
ATOM   5071 C  CB   . GLU   B 1 84  ? -41.535 -20.685 -44.434 1.00 39.23  ?  86  GLU   I CB   1 
ATOM   5072 C  CG   . GLU   B 1 84  ? -42.887 -21.321 -44.459 1.00 40.54  ?  86  GLU   I CG   1 
ATOM   5073 C  CD   . GLU   B 1 84  ? -42.898 -22.494 -43.506 1.00 43.62  ?  86  GLU   I CD   1 
ATOM   5074 O  OE1  . GLU   B 1 84  ? -42.620 -22.268 -42.312 1.00 48.53  ?  86  GLU   I OE1  1 
ATOM   5075 O  OE2  . GLU   B 1 84  ? -43.151 -23.630 -43.937 1.00 42.94  ?  86  GLU   I OE2  1 
ATOM   5076 N  N    . MET   B 1 85  ? -38.906 -19.233 -45.237 1.00 29.29  ?  87  MET   I N    1 
ATOM   5077 C  CA   . MET   B 1 85  ? -37.646 -18.750 -44.705 1.00 31.76  ?  87  MET   I CA   1 
ATOM   5078 C  C    . MET   B 1 85  ? -37.607 -17.217 -44.800 1.00 27.79  ?  87  MET   I C    1 
ATOM   5079 O  O    . MET   B 1 85  ? -37.034 -16.567 -43.935 1.00 25.41  ?  87  MET   I O    1 
ATOM   5080 C  CB   . MET   B 1 85  ? -36.451 -19.396 -45.420 1.00 34.44  ?  87  MET   I CB   1 
ATOM   5081 C  CG   . MET   B 1 85  ? -35.120 -18.983 -44.847 1.00 37.34  ?  87  MET   I CG   1 
ATOM   5082 S  SD   . MET   B 1 85  ? -33.689 -19.557 -45.775 1.00 43.29  ?  87  MET   I SD   1 
ATOM   5083 C  CE   . MET   B 1 85  ? -33.662 -21.284 -45.272 1.00 45.20  ?  87  MET   I CE   1 
ATOM   5084 N  N    . ALA   B 1 86  ? -38.236 -16.663 -45.842 1.00 25.72  ?  88  ALA   I N    1 
ATOM   5085 C  CA   . ALA   B 1 86  ? -38.371 -15.207 -46.015 1.00 23.55  ?  88  ALA   I CA   1 
ATOM   5086 C  C    . ALA   B 1 86  ? -39.186 -14.510 -44.918 1.00 22.69  ?  88  ALA   I C    1 
ATOM   5087 O  O    . ALA   B 1 86  ? -39.011 -13.319 -44.715 1.00 21.29  ?  88  ALA   I O    1 
ATOM   5088 C  CB   . ALA   B 1 86  ? -38.922 -14.867 -47.409 1.00 23.83  ?  88  ALA   I CB   1 
ATOM   5089 N  N    . ASP   B 1 87  ? -40.032 -15.243 -44.196 1.00 20.49  ?  89  ASP   I N    1 
ATOM   5090 C  CA   . ASP   B 1 87  ? -40.755 -14.655 -43.067 1.00 23.43  ?  89  ASP   I CA   1 
ATOM   5091 C  C    . ASP   B 1 87  ? -39.911 -14.532 -41.816 1.00 23.61  ?  89  ASP   I C    1 
ATOM   5092 O  O    . ASP   B 1 87  ? -40.304 -13.794 -40.908 1.00 21.87  ?  89  ASP   I O    1 
ATOM   5093 C  CB   . ASP   B 1 87  ? -41.979 -15.471 -42.655 1.00 23.81  ?  89  ASP   I CB   1 
ATOM   5094 C  CG   . ASP   B 1 87  ? -42.934 -15.664 -43.753 1.00 26.77  ?  89  ASP   I CG   1 
ATOM   5095 O  OD1  . ASP   B 1 87  ? -43.129 -14.730 -44.594 1.00 26.65  ?  89  ASP   I OD1  1 
ATOM   5096 O  OD2  . ASP   B 1 87  ? -43.488 -16.785 -43.763 1.00 31.18  ?  89  ASP   I OD2  1 
ATOM   5097 N  N    . CYS   B 1 88  ? -38.787 -15.259 -41.733 1.00 23.19  ?  90  CYS   I N    1 
ATOM   5098 C  CA   . CYS   B 1 88  ? -37.865 -15.025 -40.653 1.00 25.77  ?  90  CYS   I CA   1 
ATOM   5099 C  C    . CYS   B 1 88  ? -37.404 -13.566 -40.644 1.00 24.05  ?  90  CYS   I C    1 
ATOM   5100 O  O    . CYS   B 1 88  ? -37.204 -13.010 -39.600 1.00 23.38  ?  90  CYS   I O    1 
ATOM   5101 C  CB   . CYS   B 1 88  ? -36.709 -16.005 -40.717 1.00 28.26  ?  90  CYS   I CB   1 
ATOM   5102 S  SG   . CYS   B 1 88  ? -37.271 -17.728 -40.754 1.00 28.50  ?  90  CYS   I SG   1 
ATOM   5103 N  N    . CYS   B 1 89  ? -37.309 -12.925 -41.791 1.00 25.63  ?  91  CYS   I N    1 
ATOM   5104 C  CA   . CYS   B 1 89  ? -36.779 -11.559 -41.855 1.00 28.03  ?  91  CYS   I CA   1 
ATOM   5105 C  C    . CYS   B 1 89  ? -37.649 -10.490 -41.204 1.00 30.96  ?  91  CYS   I C    1 
ATOM   5106 O  O    . CYS   B 1 89  ? -37.157 -9.437  -40.808 1.00 30.24  ?  91  CYS   I O    1 
ATOM   5107 C  CB   . CYS   B 1 89  ? -36.550 -11.216 -43.306 1.00 30.20  ?  91  CYS   I CB   1 
ATOM   5108 S  SG   . CYS   B 1 89  ? -35.272 -12.285 -43.981 1.00 37.53  ?  91  CYS   I SG   1 
ATOM   5109 N  N    . ALA   B 1 90  ? -38.953 -10.779 -41.113 1.00 31.90  ?  92  ALA   I N    1 
ATOM   5110 C  CA   . ALA   B 1 90  ? -39.928 -9.951  -40.413 1.00 31.93  ?  92  ALA   I CA   1 
ATOM   5111 C  C    . ALA   B 1 90  ? -39.753 -9.955  -38.880 1.00 33.56  ?  92  ALA   I C    1 
ATOM   5112 O  O    . ALA   B 1 90  ? -40.397 -9.159  -38.198 1.00 29.33  ?  92  ALA   I O    1 
ATOM   5113 C  CB   . ALA   B 1 90  ? -41.350 -10.390 -40.793 1.00 29.48  ?  92  ALA   I CB   1 
ATOM   5114 N  N    . LYS   B 1 91  ? -38.913 -10.851 -38.347 1.00 34.00  ?  93  LYS   I N    1 
ATOM   5115 C  CA   . LYS   B 1 91  ? -38.647 -10.916 -36.902 1.00 33.89  ?  93  LYS   I CA   1 
ATOM   5116 C  C    . LYS   B 1 91  ? -37.465 -10.067 -36.422 1.00 36.66  ?  93  LYS   I C    1 
ATOM   5117 O  O    . LYS   B 1 91  ? -36.585 -9.693  -37.193 1.00 36.09  ?  93  LYS   I O    1 
ATOM   5118 C  CB   . LYS   B 1 91  ? -38.402 -12.361 -36.487 1.00 33.26  ?  93  LYS   I CB   1 
ATOM   5119 C  CG   . LYS   B 1 91  ? -39.579 -13.269 -36.750 1.00 34.08  ?  93  LYS   I CG   1 
ATOM   5120 C  CD   . LYS   B 1 91  ? -39.230 -14.738 -36.576 1.00 37.50  ?  93  LYS   I CD   1 
ATOM   5121 C  CE   . LYS   B 1 91  ? -40.463 -15.641 -36.590 1.00 39.50  ?  93  LYS   I CE   1 
ATOM   5122 N  NZ   . LYS   B 1 91  ? -41.477 -15.241 -37.621 1.00 40.32  ?  93  LYS   I NZ   1 
ATOM   5123 N  N    . GLN   B 1 92  ? -37.480 -9.796  -35.115 1.00 41.54  ?  94  GLN   I N    1 
ATOM   5124 C  CA   . GLN   B 1 92  ? -36.395 -9.163  -34.365 1.00 41.85  ?  94  GLN   I CA   1 
ATOM   5125 C  C    . GLN   B 1 92  ? -35.346 -10.212 -33.977 1.00 44.84  ?  94  GLN   I C    1 
ATOM   5126 O  O    . GLN   B 1 92  ? -35.684 -11.393 -33.806 1.00 36.32  ?  94  GLN   I O    1 
ATOM   5127 C  CB   . GLN   B 1 92  ? -36.975 -8.532  -33.086 1.00 42.48  ?  94  GLN   I CB   1 
ATOM   5128 N  N    . GLU   B 1 93  ? -34.105 -9.741  -33.761 1.00 52.61  ?  95  GLU   I N    1 
ATOM   5129 C  CA   . GLU   B 1 93  ? -32.874 -10.572 -33.687 1.00 55.23  ?  95  GLU   I CA   1 
ATOM   5130 C  C    . GLU   B 1 93  ? -32.573 -11.273 -32.336 1.00 59.09  ?  95  GLU   I C    1 
ATOM   5131 O  O    . GLU   B 1 93  ? -31.452 -11.722 -32.092 1.00 67.49  ?  95  GLU   I O    1 
ATOM   5132 C  CB   . GLU   B 1 93  ? -31.650 -9.745  -34.170 1.00 56.64  ?  95  GLU   I CB   1 
ATOM   5133 C  CG   . GLU   B 1 93  ? -30.300 -10.471 -34.398 1.00 57.91  ?  95  GLU   I CG   1 
ATOM   5134 C  CD   . GLU   B 1 93  ? -30.372 -11.961 -34.839 1.00 61.64  ?  95  GLU   I CD   1 
ATOM   5135 O  OE1  . GLU   B 1 93  ? -30.950 -12.301 -35.920 1.00 57.99  ?  95  GLU   I OE1  1 
ATOM   5136 O  OE2  . GLU   B 1 93  ? -29.803 -12.808 -34.096 1.00 58.86  ?  95  GLU   I OE2  1 
ATOM   5137 N  N    . PRO   B 1 94  ? -33.554 -11.362 -31.438 1.00 54.37  ?  96  PRO   I N    1 
ATOM   5138 C  CA   . PRO   B 1 94  ? -33.505 -12.637 -30.689 1.00 54.33  ?  96  PRO   I CA   1 
ATOM   5139 C  C    . PRO   B 1 94  ? -34.142 -13.773 -31.543 1.00 49.59  ?  96  PRO   I C    1 
ATOM   5140 O  O    . PRO   B 1 94  ? -33.474 -14.770 -31.846 1.00 45.10  ?  96  PRO   I O    1 
ATOM   5141 C  CB   . PRO   B 1 94  ? -34.303 -12.339 -29.405 1.00 57.69  ?  96  PRO   I CB   1 
ATOM   5142 C  CG   . PRO   B 1 94  ? -34.380 -10.844 -29.321 1.00 59.33  ?  96  PRO   I CG   1 
ATOM   5143 C  CD   . PRO   B 1 94  ? -34.315 -10.318 -30.733 1.00 57.21  ?  96  PRO   I CD   1 
ATOM   5144 N  N    . GLU   B 1 95  ? -35.396 -13.567 -31.977 1.00 43.96  ?  97  GLU   I N    1 
ATOM   5145 C  CA   . GLU   B 1 95  ? -36.203 -14.606 -32.639 1.00 39.82  ?  97  GLU   I CA   1 
ATOM   5146 C  C    . GLU   B 1 95  ? -35.868 -14.860 -34.104 1.00 34.71  ?  97  GLU   I C    1 
ATOM   5147 O  O    . GLU   B 1 95  ? -36.116 -15.969 -34.610 1.00 29.50  ?  97  GLU   I O    1 
ATOM   5148 C  CB   . GLU   B 1 95  ? -37.692 -14.287 -32.528 1.00 43.60  ?  97  GLU   I CB   1 
ATOM   5149 C  CG   . GLU   B 1 95  ? -38.200 -14.235 -31.102 1.00 50.78  ?  97  GLU   I CG   1 
ATOM   5150 C  CD   . GLU   B 1 95  ? -38.442 -12.819 -30.591 1.00 60.56  ?  97  GLU   I CD   1 
ATOM   5151 O  OE1  . GLU   B 1 95  ? -37.598 -11.920 -30.866 1.00 70.65  ?  97  GLU   I OE1  1 
ATOM   5152 O  OE2  . GLU   B 1 95  ? -39.480 -12.608 -29.909 1.00 66.32  ?  97  GLU   I OE2  1 
ATOM   5153 N  N    . ARG   B 1 96  ? -35.314 -13.860 -34.788 1.00 29.94  ?  98  ARG   I N    1 
ATOM   5154 C  CA   . ARG   B 1 96  ? -34.961 -14.046 -36.199 1.00 31.32  ?  98  ARG   I CA   1 
ATOM   5155 C  C    . ARG   B 1 96  ? -33.954 -15.183 -36.390 1.00 28.37  ?  98  ARG   I C    1 
ATOM   5156 O  O    . ARG   B 1 96  ? -34.170 -16.071 -37.239 1.00 22.74  ?  98  ARG   I O    1 
ATOM   5157 C  CB   . ARG   B 1 96  ? -34.392 -12.779 -36.854 1.00 30.17  ?  98  ARG   I CB   1 
ATOM   5158 C  CG   . ARG   B 1 96  ? -34.073 -13.009 -38.328 1.00 29.41  ?  98  ARG   I CG   1 
ATOM   5159 C  CD   . ARG   B 1 96  ? -33.611 -11.749 -39.076 1.00 27.66  ?  98  ARG   I CD   1 
ATOM   5160 N  NE   . ARG   B 1 96  ? -32.301 -11.394 -38.575 1.00 25.59  ?  98  ARG   I NE   1 
ATOM   5161 C  CZ   . ARG   B 1 96  ? -31.594 -10.344 -38.936 1.00 24.49  ?  98  ARG   I CZ   1 
ATOM   5162 N  NH1  . ARG   B 1 96  ? -32.018 -9.494  -39.864 1.00 23.31  ?  98  ARG   I NH1  1 
ATOM   5163 N  NH2  . ARG   B 1 96  ? -30.443 -10.152 -38.340 1.00 23.41  ?  98  ARG   I NH2  1 
ATOM   5164 N  N    . ASN   B 1 97  ? -32.864 -15.126 -35.616 1.00 28.53  ?  99  ASN   I N    1 
ATOM   5165 C  CA   . ASN   B 1 97  ? -31.822 -16.151 -35.676 1.00 31.90  ?  99  ASN   I CA   1 
ATOM   5166 C  C    . ASN   B 1 97  ? -32.439 -17.573 -35.483 1.00 30.00  ?  99  ASN   I C    1 
ATOM   5167 O  O    . ASN   B 1 97  ? -32.114 -18.523 -36.232 1.00 26.69  ?  99  ASN   I O    1 
ATOM   5168 C  CB   . ASN   B 1 97  ? -30.709 -15.914 -34.639 1.00 31.80  ?  99  ASN   I CB   1 
ATOM   5169 C  CG   . ASN   B 1 97  ? -29.735 -17.076 -34.592 1.00 33.82  ?  99  ASN   I CG   1 
ATOM   5170 O  OD1  . ASN   B 1 97  ? -29.119 -17.405 -35.618 1.00 36.15  ?  99  ASN   I OD1  1 
ATOM   5171 N  ND2  . ASN   B 1 97  ? -29.667 -17.764 -33.460 1.00 28.92  ?  99  ASN   I ND2  1 
ATOM   5172 N  N    . GLU   B 1 98  ? -33.346 -17.677 -34.523 1.00 28.60  ?  100 GLU   I N    1 
ATOM   5173 C  CA   . GLU   B 1 98  ? -33.966 -18.960 -34.204 1.00 30.61  ?  100 GLU   I CA   1 
ATOM   5174 C  C    . GLU   B 1 98  ? -34.877 -19.451 -35.325 1.00 29.88  ?  100 GLU   I C    1 
ATOM   5175 O  O    . GLU   B 1 98  ? -35.018 -20.635 -35.543 1.00 30.44  ?  100 GLU   I O    1 
ATOM   5176 C  CB   . GLU   B 1 98  ? -34.729 -18.848 -32.878 1.00 35.75  ?  100 GLU   I CB   1 
ATOM   5177 C  CG   . GLU   B 1 98  ? -34.946 -20.173 -32.172 1.00 39.94  ?  100 GLU   I CG   1 
ATOM   5178 C  CD   . GLU   B 1 98  ? -33.642 -20.902 -31.846 1.00 44.30  ?  100 GLU   I CD   1 
ATOM   5179 O  OE1  . GLU   B 1 98  ? -32.661 -20.273 -31.340 1.00 45.67  ?  100 GLU   I OE1  1 
ATOM   5180 O  OE2  . GLU   B 1 98  ? -33.611 -22.121 -32.122 1.00 51.42  ?  100 GLU   I OE2  1 
ATOM   5181 N  N    . CYS   B 1 99  ? -35.484 -18.535 -36.055 1.00 28.98  ?  101 CYS   I N    1 
ATOM   5182 C  CA   . CYS   B 1 99  ? -36.335 -18.910 -37.186 1.00 30.33  ?  101 CYS   I CA   1 
ATOM   5183 C  C    . CYS   B 1 99  ? -35.506 -19.470 -38.362 1.00 27.38  ?  101 CYS   I C    1 
ATOM   5184 O  O    . CYS   B 1 99  ? -35.911 -20.419 -39.011 1.00 24.67  ?  101 CYS   I O    1 
ATOM   5185 C  CB   . CYS   B 1 99  ? -37.167 -17.690 -37.616 1.00 30.15  ?  101 CYS   I CB   1 
ATOM   5186 S  SG   . CYS   B 1 99  ? -38.309 -17.995 -38.962 1.00 35.37  ?  101 CYS   I SG   1 
ATOM   5187 N  N    . PHE   B 1 100 ? -34.331 -18.895 -38.628 1.00 26.49  ?  102 PHE   I N    1 
ATOM   5188 C  CA   . PHE   B 1 100 ? -33.426 -19.441 -39.657 1.00 25.70  ?  102 PHE   I CA   1 
ATOM   5189 C  C    . PHE   B 1 100 ? -32.972 -20.850 -39.328 1.00 24.85  ?  102 PHE   I C    1 
ATOM   5190 O  O    . PHE   B 1 100 ? -32.971 -21.697 -40.188 1.00 23.66  ?  102 PHE   I O    1 
ATOM   5191 C  CB   . PHE   B 1 100 ? -32.225 -18.538 -39.878 1.00 24.89  ?  102 PHE   I CB   1 
ATOM   5192 C  CG   . PHE   B 1 100 ? -32.572 -17.271 -40.565 1.00 25.67  ?  102 PHE   I CG   1 
ATOM   5193 C  CD1  . PHE   B 1 100 ? -33.207 -17.300 -41.811 1.00 27.32  ?  102 PHE   I CD1  1 
ATOM   5194 C  CD2  . PHE   B 1 100 ? -32.279 -16.067 -40.004 1.00 27.19  ?  102 PHE   I CD2  1 
ATOM   5195 C  CE1  . PHE   B 1 100 ? -33.535 -16.150 -42.465 1.00 27.82  ?  102 PHE   I CE1  1 
ATOM   5196 C  CE2  . PHE   B 1 100 ? -32.621 -14.901 -40.656 1.00 27.36  ?  102 PHE   I CE2  1 
ATOM   5197 C  CZ   . PHE   B 1 100 ? -33.243 -14.944 -41.885 1.00 27.41  ?  102 PHE   I CZ   1 
ATOM   5198 N  N    . LEU   B 1 101 ? -32.631 -21.084 -38.074 1.00 28.10  ?  103 LEU   I N    1 
ATOM   5199 C  CA   . LEU   B 1 101 ? -32.220 -22.401 -37.625 1.00 30.70  ?  103 LEU   I CA   1 
ATOM   5200 C  C    . LEU   B 1 101 ? -33.273 -23.450 -37.923 1.00 31.66  ?  103 LEU   I C    1 
ATOM   5201 O  O    . LEU   B 1 101 ? -32.942 -24.558 -38.297 1.00 33.40  ?  103 LEU   I O    1 
ATOM   5202 C  CB   . LEU   B 1 101 ? -31.939 -22.394 -36.119 1.00 32.79  ?  103 LEU   I CB   1 
ATOM   5203 C  CG   . LEU   B 1 101 ? -30.589 -21.907 -35.593 1.00 33.92  ?  103 LEU   I CG   1 
ATOM   5204 C  CD1  . LEU   B 1 101 ? -30.628 -21.655 -34.080 1.00 36.70  ?  103 LEU   I CD1  1 
ATOM   5205 C  CD2  . LEU   B 1 101 ? -29.532 -22.935 -35.894 1.00 35.27  ?  103 LEU   I CD2  1 
ATOM   5206 N  N    . GLN   B 1 102 ? -34.536 -23.095 -37.747 1.00 36.27  ?  104 GLN   I N    1 
ATOM   5207 C  CA   . GLN   B 1 102 ? -35.644 -24.015 -38.001 1.00 38.11  ?  104 GLN   I CA   1 
ATOM   5208 C  C    . GLN   B 1 102 ? -35.955 -24.322 -39.481 1.00 38.47  ?  104 GLN   I C    1 
ATOM   5209 O  O    . GLN   B 1 102 ? -36.672 -25.272 -39.752 1.00 38.63  ?  104 GLN   I O    1 
ATOM   5210 C  CB   . GLN   B 1 102 ? -36.882 -23.483 -37.283 1.00 43.15  ?  104 GLN   I CB   1 
ATOM   5211 C  CG   . GLN   B 1 102 ? -36.751 -23.607 -35.765 1.00 50.38  ?  104 GLN   I CG   1 
ATOM   5212 C  CD   . GLN   B 1 102 ? -37.659 -22.673 -34.976 1.00 56.65  ?  104 GLN   I CD   1 
ATOM   5213 O  OE1  . GLN   B 1 102 ? -38.549 -22.006 -35.527 1.00 63.67  ?  104 GLN   I OE1  1 
ATOM   5214 N  NE2  . GLN   B 1 102 ? -37.430 -22.616 -33.667 1.00 58.18  ?  104 GLN   I NE2  1 
ATOM   5215 N  N    . HIS   B 1 103 ? -35.433 -23.547 -40.438 1.00 40.97  ?  105 HIS   I N    1 
ATOM   5216 C  CA   . HIS   B 1 103 ? -35.838 -23.670 -41.865 1.00 40.50  ?  105 HIS   I CA   1 
ATOM   5217 C  C    . HIS   B 1 103 ? -34.696 -24.050 -42.822 1.00 42.68  ?  105 HIS   I C    1 
ATOM   5218 O  O    . HIS   B 1 103 ? -34.759 -23.784 -44.020 1.00 44.94  ?  105 HIS   I O    1 
ATOM   5219 C  CB   . HIS   B 1 103 ? -36.569 -22.391 -42.317 1.00 41.60  ?  105 HIS   I CB   1 
ATOM   5220 C  CG   . HIS   B 1 103 ? -37.834 -22.127 -41.559 1.00 41.82  ?  105 HIS   I CG   1 
ATOM   5221 N  ND1  . HIS   B 1 103 ? -37.986 -21.067 -40.694 1.00 43.54  ?  105 HIS   I ND1  1 
ATOM   5222 C  CD2  . HIS   B 1 103 ? -38.997 -22.814 -41.514 1.00 42.83  ?  105 HIS   I CD2  1 
ATOM   5223 C  CE1  . HIS   B 1 103 ? -39.186 -21.113 -40.148 1.00 44.00  ?  105 HIS   I CE1  1 
ATOM   5224 N  NE2  . HIS   B 1 103 ? -39.829 -22.149 -40.650 1.00 44.60  ?  105 HIS   I NE2  1 
ATOM   5225 N  N    . LYS   B 1 104 ? -33.654 -24.690 -42.302 1.00 42.60  ?  106 LYS   I N    1 
ATOM   5226 C  CA   . LYS   B 1 104 ? -32.741 -25.417 -43.165 1.00 42.03  ?  106 LYS   I CA   1 
ATOM   5227 C  C    . LYS   B 1 104 ? -33.438 -26.677 -43.658 1.00 42.49  ?  106 LYS   I C    1 
ATOM   5228 O  O    . LYS   B 1 104 ? -34.231 -27.250 -42.925 1.00 41.17  ?  106 LYS   I O    1 
ATOM   5229 C  CB   . LYS   B 1 104 ? -31.516 -25.862 -42.399 1.00 44.01  ?  106 LYS   I CB   1 
ATOM   5230 C  CG   . LYS   B 1 104 ? -30.582 -24.764 -41.962 1.00 43.87  ?  106 LYS   I CG   1 
ATOM   5231 C  CD   . LYS   B 1 104 ? -29.520 -25.391 -41.077 1.00 41.31  ?  106 LYS   I CD   1 
ATOM   5232 C  CE   . LYS   B 1 104 ? -28.189 -24.725 -41.264 1.00 39.35  ?  106 LYS   I CE   1 
ATOM   5233 N  NZ   . LYS   B 1 104 ? -27.197 -25.455 -40.460 1.00 39.90  ?  106 LYS   I NZ   1 
ATOM   5234 N  N    . ASP   B 1 105 ? -33.113 -27.090 -44.887 1.00 45.62  ?  107 ASP   I N    1 
ATOM   5235 C  CA   . ASP   B 1 105 ? -33.579 -28.327 -45.505 1.00 50.30  ?  107 ASP   I CA   1 
ATOM   5236 C  C    . ASP   B 1 105 ? -32.511 -29.427 -45.431 1.00 53.36  ?  107 ASP   I C    1 
ATOM   5237 O  O    . ASP   B 1 105 ? -31.549 -29.416 -46.205 1.00 57.08  ?  107 ASP   I O    1 
ATOM   5238 C  CB   . ASP   B 1 105 ? -33.919 -28.015 -46.974 1.00 53.22  ?  107 ASP   I CB   1 
ATOM   5239 C  CG   . ASP   B 1 105 ? -34.689 -29.141 -47.688 1.00 54.31  ?  107 ASP   I CG   1 
ATOM   5240 O  OD1  . ASP   B 1 105 ? -34.497 -30.339 -47.384 1.00 58.04  ?  107 ASP   I OD1  1 
ATOM   5241 O  OD2  . ASP   B 1 105 ? -35.483 -28.809 -48.593 1.00 51.19  ?  107 ASP   I OD2  1 
ATOM   5242 N  N    . ASP   B 1 106 ? -32.673 -30.385 -44.520 1.00 57.21  ?  108 ASP   I N    1 
ATOM   5243 C  CA   . ASP   B 1 106 ? -31.754 -31.548 -44.465 1.00 60.96  ?  108 ASP   I CA   1 
ATOM   5244 C  C    . ASP   B 1 106 ? -32.099 -32.490 -45.606 1.00 63.66  ?  108 ASP   I C    1 
ATOM   5245 O  O    . ASP   B 1 106 ? -33.252 -32.574 -46.005 1.00 63.07  ?  108 ASP   I O    1 
ATOM   5246 C  CB   . ASP   B 1 106 ? -31.822 -32.305 -43.126 1.00 58.11  ?  108 ASP   I CB   1 
ATOM   5247 N  N    . ASN   B 1 107 ? -31.090 -33.181 -46.133 1.00 72.83  ?  109 ASN   I N    1 
ATOM   5248 C  CA   . ASN   B 1 107 ? -31.254 -34.161 -47.237 1.00 75.57  ?  109 ASN   I CA   1 
ATOM   5249 C  C    . ASN   B 1 107 ? -32.168 -33.644 -48.384 1.00 71.96  ?  109 ASN   I C    1 
ATOM   5250 O  O    . ASN   B 1 107 ? -33.182 -34.269 -48.701 1.00 70.74  ?  109 ASN   I O    1 
ATOM   5251 C  CB   . ASN   B 1 107 ? -31.750 -35.526 -46.665 1.00 79.34  ?  109 ASN   I CB   1 
ATOM   5252 C  CG   . ASN   B 1 107 ? -30.811 -36.705 -46.978 1.00 83.65  ?  109 ASN   I CG   1 
ATOM   5253 O  OD1  . ASN   B 1 107 ? -29.673 -36.525 -47.419 1.00 89.25  ?  109 ASN   I OD1  1 
ATOM   5254 N  ND2  . ASN   B 1 107 ? -31.286 -37.924 -46.708 1.00 80.61  ?  109 ASN   I ND2  1 
ATOM   5255 N  N    . PRO   B 1 108 ? -31.801 -32.497 -49.008 1.00 67.05  ?  110 PRO   I N    1 
ATOM   5256 C  CA   . PRO   B 1 108 ? -32.627 -31.943 -50.102 1.00 64.52  ?  110 PRO   I CA   1 
ATOM   5257 C  C    . PRO   B 1 108 ? -32.593 -32.772 -51.394 1.00 63.55  ?  110 PRO   I C    1 
ATOM   5258 O  O    . PRO   B 1 108 ? -31.908 -33.789 -51.464 1.00 65.62  ?  110 PRO   I O    1 
ATOM   5259 C  CB   . PRO   B 1 108 ? -32.029 -30.546 -50.356 1.00 64.73  ?  110 PRO   I CB   1 
ATOM   5260 C  CG   . PRO   B 1 108 ? -30.743 -30.486 -49.603 1.00 66.20  ?  110 PRO   I CG   1 
ATOM   5261 C  CD   . PRO   B 1 108 ? -30.548 -31.738 -48.804 1.00 65.29  ?  110 PRO   I CD   1 
ATOM   5262 N  N    . ASN   B 1 109 ? -33.354 -32.336 -52.392 1.00 60.10  ?  111 ASN   I N    1 
ATOM   5263 C  CA   . ASN   B 1 109 ? -33.365 -32.973 -53.707 1.00 53.59  ?  111 ASN   I CA   1 
ATOM   5264 C  C    . ASN   B 1 109 ? -32.338 -32.226 -54.533 1.00 46.61  ?  111 ASN   I C    1 
ATOM   5265 O  O    . ASN   B 1 109 ? -32.641 -31.207 -55.140 1.00 46.93  ?  111 ASN   I O    1 
ATOM   5266 C  CB   . ASN   B 1 109 ? -34.753 -32.903 -54.357 1.00 54.74  ?  111 ASN   I CB   1 
ATOM   5267 N  N    . LEU   B 1 110 ? -31.096 -32.694 -54.453 1.00 40.46  ?  112 LEU   I N    1 
ATOM   5268 C  CA   . LEU   B 1 110 ? -30.033 -32.284 -55.349 1.00 34.80  ?  112 LEU   I CA   1 
ATOM   5269 C  C    . LEU   B 1 110 ? -29.498 -33.559 -55.916 1.00 34.81  ?  112 LEU   I C    1 
ATOM   5270 O  O    . LEU   B 1 110 ? -29.504 -34.591 -55.217 1.00 32.52  ?  112 LEU   I O    1 
ATOM   5271 C  CB   . LEU   B 1 110 ? -28.906 -31.514 -54.658 1.00 32.84  ?  112 LEU   I CB   1 
ATOM   5272 C  CG   . LEU   B 1 110 ? -29.201 -30.081 -54.214 1.00 31.94  ?  112 LEU   I CG   1 
ATOM   5273 C  CD1  . LEU   B 1 110 ? -27.996 -29.513 -53.449 1.00 31.64  ?  112 LEU   I CD1  1 
ATOM   5274 C  CD2  . LEU   B 1 110 ? -29.571 -29.152 -55.352 1.00 30.45  ?  112 LEU   I CD2  1 
ATOM   5275 N  N    . PRO   B 1 111 ? -29.043 -33.496 -57.187 1.00 32.33  ?  113 PRO   I N    1 
ATOM   5276 C  CA   . PRO   B 1 111 ? -28.607 -34.681 -57.865 1.00 32.09  ?  113 PRO   I CA   1 
ATOM   5277 C  C    . PRO   B 1 111 ? -27.259 -35.086 -57.359 1.00 34.39  ?  113 PRO   I C    1 
ATOM   5278 O  O    . PRO   B 1 111 ? -26.481 -34.231 -56.885 1.00 33.73  ?  113 PRO   I O    1 
ATOM   5279 C  CB   . PRO   B 1 111 ? -28.512 -34.232 -59.325 1.00 30.16  ?  113 PRO   I CB   1 
ATOM   5280 C  CG   . PRO   B 1 111 ? -28.182 -32.783 -59.260 1.00 31.12  ?  113 PRO   I CG   1 
ATOM   5281 C  CD   . PRO   B 1 111 ? -28.881 -32.287 -58.032 1.00 32.29  ?  113 PRO   I CD   1 
ATOM   5282 N  N    . ARG   B 1 112 ? -27.026 -36.383 -57.450 1.00 36.54  ?  114 ARG   I N    1 
ATOM   5283 C  CA   . ARG   B 1 112 ? -25.726 -37.027 -57.273 1.00 43.76  ?  114 ARG   I CA   1 
ATOM   5284 C  C    . ARG   B 1 112 ? -24.579 -36.225 -57.884 1.00 42.14  ?  114 ARG   I C    1 
ATOM   5285 O  O    . ARG   B 1 112 ? -24.638 -35.841 -59.054 1.00 42.43  ?  114 ARG   I O    1 
ATOM   5286 C  CB   . ARG   B 1 112 ? -25.783 -38.425 -57.926 1.00 50.22  ?  114 ARG   I CB   1 
ATOM   5287 C  CG   . ARG   B 1 112 ? -24.623 -39.374 -57.663 1.00 59.28  ?  114 ARG   I CG   1 
ATOM   5288 C  CD   . ARG   B 1 112 ? -24.908 -40.712 -58.359 1.00 63.82  ?  114 ARG   I CD   1 
ATOM   5289 N  NE   . ARG   B 1 112 ? -23.860 -41.726 -58.181 1.00 73.61  ?  114 ARG   I NE   1 
ATOM   5290 C  CZ   . ARG   B 1 112 ? -22.702 -41.799 -58.854 1.00 77.77  ?  114 ARG   I CZ   1 
ATOM   5291 N  NH1  . ARG   B 1 112 ? -22.370 -40.898 -59.781 1.00 77.68  ?  114 ARG   I NH1  1 
ATOM   5292 N  NH2  . ARG   B 1 112 ? -21.852 -42.792 -58.582 1.00 79.12  ?  114 ARG   I NH2  1 
ATOM   5293 N  N    . LEU   B 1 113 ? -23.570 -35.932 -57.060 1.00 42.87  ?  115 LEU   I N    1 
ATOM   5294 C  CA   . LEU   B 1 113 ? -22.309 -35.397 -57.532 1.00 42.42  ?  115 LEU   I CA   1 
ATOM   5295 C  C    . LEU   B 1 113 ? -21.555 -36.554 -58.132 1.00 41.60  ?  115 LEU   I C    1 
ATOM   5296 O  O    . LEU   B 1 113 ? -21.155 -37.451 -57.400 1.00 43.06  ?  115 LEU   I O    1 
ATOM   5297 C  CB   . LEU   B 1 113 ? -21.493 -34.792 -56.392 1.00 39.92  ?  115 LEU   I CB   1 
ATOM   5298 C  CG   . LEU   B 1 113 ? -21.828 -33.359 -55.994 1.00 39.03  ?  115 LEU   I CG   1 
ATOM   5299 C  CD1  . LEU   B 1 113 ? -20.935 -32.954 -54.819 1.00 42.62  ?  115 LEU   I CD1  1 
ATOM   5300 C  CD2  . LEU   B 1 113 ? -21.720 -32.362 -57.146 1.00 35.63  ?  115 LEU   I CD2  1 
ATOM   5301 N  N    . VAL   B 1 114 ? -21.419 -36.546 -59.459 1.00 43.12  ?  116 VAL   I N    1 
ATOM   5302 C  CA   . VAL   B 1 114 ? -20.584 -37.522 -60.170 1.00 43.28  ?  116 VAL   I CA   1 
ATOM   5303 C  C    . VAL   B 1 114 ? -19.111 -37.112 -60.024 1.00 37.31  ?  116 VAL   I C    1 
ATOM   5304 O  O    . VAL   B 1 114 ? -18.780 -35.973 -60.228 1.00 35.05  ?  116 VAL   I O    1 
ATOM   5305 C  CB   . VAL   B 1 114 ? -20.986 -37.692 -61.685 1.00 46.45  ?  116 VAL   I CB   1 
ATOM   5306 C  CG1  . VAL   B 1 114 ? -22.456 -38.084 -61.817 1.00 49.31  ?  116 VAL   I CG1  1 
ATOM   5307 C  CG2  . VAL   B 1 114 ? -20.699 -36.456 -62.544 1.00 45.41  ?  116 VAL   I CG2  1 
ATOM   5308 N  N    . ARG   B 1 115 ? -18.249 -38.036 -59.640 1.00 36.12  ?  117 ARG   I N    1 
ATOM   5309 C  CA   . ARG   B 1 115 ? -16.799 -37.837 -59.722 1.00 37.00  ?  117 ARG   I CA   1 
ATOM   5310 C  C    . ARG   B 1 115 ? -16.405 -37.712 -61.206 1.00 36.06  ?  117 ARG   I C    1 
ATOM   5311 O  O    . ARG   B 1 115 ? -16.607 -38.648 -61.954 1.00 35.57  ?  117 ARG   I O    1 
ATOM   5312 C  CB   . ARG   B 1 115 ? -16.076 -39.037 -59.087 1.00 37.73  ?  117 ARG   I CB   1 
ATOM   5313 C  CG   . ARG   B 1 115 ? -14.558 -38.952 -59.113 1.00 41.52  ?  117 ARG   I CG   1 
ATOM   5314 C  CD   . ARG   B 1 115 ? -13.870 -40.165 -58.510 1.00 42.07  ?  117 ARG   I CD   1 
ATOM   5315 N  NE   . ARG   B 1 115 ? -14.153 -40.304 -57.089 1.00 43.91  ?  117 ARG   I NE   1 
ATOM   5316 C  CZ   . ARG   B 1 115 ? -13.979 -41.418 -56.385 1.00 42.41  ?  117 ARG   I CZ   1 
ATOM   5317 N  NH1  . ARG   B 1 115 ? -13.504 -42.527 -56.955 1.00 44.28  ?  117 ARG   I NH1  1 
ATOM   5318 N  NH2  . ARG   B 1 115 ? -14.279 -41.419 -55.091 1.00 42.61  ?  117 ARG   I NH2  1 
ATOM   5319 N  N    . PRO   B 1 116 ? -15.859 -36.561 -61.641 1.00 36.19  ?  118 PRO   I N    1 
ATOM   5320 C  CA   . PRO   B 1 116 ? -15.329 -36.508 -63.006 1.00 34.68  ?  118 PRO   I CA   1 
ATOM   5321 C  C    . PRO   B 1 116 ? -14.116 -37.431 -63.204 1.00 34.36  ?  118 PRO   I C    1 
ATOM   5322 O  O    . PRO   B 1 116 ? -13.642 -38.043 -62.256 1.00 30.78  ?  118 PRO   I O    1 
ATOM   5323 C  CB   . PRO   B 1 116 ? -14.891 -35.034 -63.168 1.00 34.49  ?  118 PRO   I CB   1 
ATOM   5324 C  CG   . PRO   B 1 116 ? -15.480 -34.293 -62.019 1.00 35.21  ?  118 PRO   I CG   1 
ATOM   5325 C  CD   . PRO   B 1 116 ? -15.593 -35.303 -60.914 1.00 36.10  ?  118 PRO   I CD   1 
ATOM   5326 N  N    . GLU   B 1 117 ? -13.645 -37.540 -64.441 1.00 35.47  ?  119 GLU   I N    1 
ATOM   5327 C  CA   . GLU   B 1 117 ? -12.341 -38.157 -64.755 1.00 36.53  ?  119 GLU   I CA   1 
ATOM   5328 C  C    . GLU   B 1 117 ? -11.168 -37.477 -64.001 1.00 33.46  ?  119 GLU   I C    1 
ATOM   5329 O  O    . GLU   B 1 117 ? -11.198 -36.274 -63.710 1.00 29.79  ?  119 GLU   I O    1 
ATOM   5330 C  CB   . GLU   B 1 117 ? -12.084 -38.069 -66.273 1.00 35.36  ?  119 GLU   I CB   1 
ATOM   5331 N  N    . VAL   B 1 118 ? -10.118 -38.240 -63.724 1.00 34.34  ?  120 VAL   I N    1 
ATOM   5332 C  CA   . VAL   B 1 118 ? -8.932  -37.678 -63.051 1.00 32.86  ?  120 VAL   I CA   1 
ATOM   5333 C  C    . VAL   B 1 118 ? -8.339  -36.507 -63.811 1.00 32.35  ?  120 VAL   I C    1 
ATOM   5334 O  O    . VAL   B 1 118 ? -7.932  -35.525 -63.200 1.00 31.70  ?  120 VAL   I O    1 
ATOM   5335 C  CB   . VAL   B 1 118 ? -7.861  -38.721 -62.777 1.00 31.74  ?  120 VAL   I CB   1 
ATOM   5336 C  CG1  . VAL   B 1 118 ? -6.603  -38.055 -62.216 1.00 31.67  ?  120 VAL   I CG1  1 
ATOM   5337 C  CG2  . VAL   B 1 118 ? -8.397  -39.751 -61.823 1.00 33.22  ?  120 VAL   I CG2  1 
ATOM   5338 N  N    . ASP   B 1 119 ? -8.305  -36.608 -65.142 1.00 32.91  ?  121 ASP   I N    1 
ATOM   5339 C  CA   . ASP   B 1 119 ? -7.752  -35.537 -65.964 1.00 32.28  ?  121 ASP   I CA   1 
ATOM   5340 C  C    . ASP   B 1 119 ? -8.619  -34.300 -66.016 1.00 26.99  ?  121 ASP   I C    1 
ATOM   5341 O  O    . ASP   B 1 119 ? -8.116  -33.184 -66.110 1.00 26.06  ?  121 ASP   I O    1 
ATOM   5342 C  CB   . ASP   B 1 119 ? -7.438  -36.059 -67.361 1.00 38.07  ?  121 ASP   I CB   1 
ATOM   5343 C  CG   . ASP   B 1 119 ? -6.247  -36.998 -67.355 1.00 45.54  ?  121 ASP   I CG   1 
ATOM   5344 O  OD1  . ASP   B 1 119 ? -6.404  -38.139 -66.858 1.00 51.23  ?  121 ASP   I OD1  1 
ATOM   5345 O  OD2  . ASP   B 1 119 ? -5.154  -36.582 -67.816 1.00 50.42  ?  121 ASP   I OD2  1 
ATOM   5346 N  N    . VAL   B 1 120 ? -9.929  -34.481 -65.962 1.00 28.31  ?  122 VAL   I N    1 
ATOM   5347 C  CA   . VAL   B 1 120 ? -10.845 -33.323 -65.881 1.00 28.73  ?  122 VAL   I CA   1 
ATOM   5348 C  C    . VAL   B 1 120 ? -10.628 -32.620 -64.525 1.00 28.14  ?  122 VAL   I C    1 
ATOM   5349 O  O    . VAL   B 1 120 ? -10.422 -31.409 -64.473 1.00 28.52  ?  122 VAL   I O    1 
ATOM   5350 C  CB   . VAL   B 1 120 ? -12.313 -33.735 -66.121 1.00 28.73  ?  122 VAL   I CB   1 
ATOM   5351 C  CG1  . VAL   B 1 120 ? -13.259 -32.588 -65.812 1.00 27.47  ?  122 VAL   I CG1  1 
ATOM   5352 C  CG2  . VAL   B 1 120 ? -12.493 -34.234 -67.570 1.00 28.46  ?  122 VAL   I CG2  1 
ATOM   5353 N  N    . MET   B 1 121 ? -10.615 -33.386 -63.440 1.00 30.05  ?  123 MET   I N    1 
ATOM   5354 C  CA   . MET   B 1 121 ? -10.331 -32.818 -62.089 1.00 31.97  ?  123 MET   I CA   1 
ATOM   5355 C  C    . MET   B 1 121 ? -8.983  -32.109 -62.014 1.00 32.51  ?  123 MET   I C    1 
ATOM   5356 O  O    . MET   B 1 121 ? -8.899  -30.958 -61.525 1.00 26.97  ?  123 MET   I O    1 
ATOM   5357 C  CB   . MET   B 1 121 ? -10.393 -33.900 -61.005 1.00 33.67  ?  123 MET   I CB   1 
ATOM   5358 C  CG   . MET   B 1 121 ? -11.811 -34.294 -60.614 1.00 36.50  ?  123 MET   I CG   1 
ATOM   5359 S  SD   . MET   B 1 121 ? -11.947 -35.578 -59.345 1.00 38.51  ?  123 MET   I SD   1 
ATOM   5360 C  CE   . MET   B 1 121 ? -10.804 -36.836 -59.905 1.00 37.51  ?  123 MET   I CE   1 
ATOM   5361 N  N    . CYS   B 1 122 ? -7.934  -32.798 -62.488 1.00 34.32  ?  124 CYS   I N    1 
ATOM   5362 C  CA   . CYS   B 1 122 ? -6.566  -32.268 -62.397 1.00 31.90  ?  124 CYS   I CA   1 
ATOM   5363 C  C    . CYS   B 1 122 ? -6.371  -31.046 -63.272 1.00 30.19  ?  124 CYS   I C    1 
ATOM   5364 O  O    . CYS   B 1 122 ? -5.729  -30.084 -62.858 1.00 30.55  ?  124 CYS   I O    1 
ATOM   5365 C  CB   . CYS   B 1 122 ? -5.529  -33.349 -62.702 1.00 33.05  ?  124 CYS   I CB   1 
ATOM   5366 S  SG   . CYS   B 1 122 ? -5.331  -34.588 -61.384 1.00 39.80  ?  124 CYS   I SG   1 
ATOM   5367 N  N    . THR   B 1 123 ? -6.940  -31.052 -64.472 1.00 30.94  ?  125 THR   I N    1 
ATOM   5368 C  CA   . THR   B 1 123 ? -6.855  -29.852 -65.315 1.00 30.72  ?  125 THR   I CA   1 
ATOM   5369 C  C    . THR   B 1 123 ? -7.498  -28.662 -64.636 1.00 30.93  ?  125 THR   I C    1 
ATOM   5370 O  O    . THR   B 1 123 ? -6.843  -27.609 -64.497 1.00 30.11  ?  125 THR   I O    1 
ATOM   5371 C  CB   . THR   B 1 123 ? -7.560  -30.039 -66.658 1.00 30.67  ?  125 THR   I CB   1 
ATOM   5372 O  OG1  . THR   B 1 123 ? -7.117  -31.252 -67.234 1.00 32.33  ?  125 THR   I OG1  1 
ATOM   5373 C  CG2  . THR   B 1 123 ? -7.257  -28.879 -67.590 1.00 32.61  ?  125 THR   I CG2  1 
ATOM   5374 N  N    . ALA   B 1 124 ? -8.763  -28.856 -64.214 1.00 27.72  ?  126 ALA   I N    1 
ATOM   5375 C  CA   . ALA   B 1 124 ? -9.558  -27.826 -63.510 1.00 27.71  ?  126 ALA   I CA   1 
ATOM   5376 C  C    . ALA   B 1 124 ? -8.885  -27.335 -62.201 1.00 23.05  ?  126 ALA   I C    1 
ATOM   5377 O  O    . ALA   B 1 124 ? -8.719  -26.126 -61.963 1.00 19.14  ?  126 ALA   I O    1 
ATOM   5378 C  CB   . ALA   B 1 124 ? -10.963 -28.354 -63.241 1.00 28.00  ?  126 ALA   I CB   1 
ATOM   5379 N  N    . PHE   B 1 125 ? -8.438  -28.281 -61.413 1.00 23.82  ?  127 PHE   I N    1 
ATOM   5380 C  CA   . PHE   B 1 125 ? -7.591  -27.969 -60.253 1.00 30.12  ?  127 PHE   I CA   1 
ATOM   5381 C  C    . PHE   B 1 125 ? -6.351  -27.114 -60.596 1.00 34.07  ?  127 PHE   I C    1 
ATOM   5382 O  O    . PHE   B 1 125 ? -5.948  -26.236 -59.823 1.00 33.58  ?  127 PHE   I O    1 
ATOM   5383 C  CB   . PHE   B 1 125 ? -7.151  -29.257 -59.546 1.00 30.79  ?  127 PHE   I CB   1 
ATOM   5384 C  CG   . PHE   B 1 125 ? -6.168  -29.028 -58.426 1.00 34.74  ?  127 PHE   I CG   1 
ATOM   5385 C  CD1  . PHE   B 1 125 ? -6.615  -28.684 -57.153 1.00 32.99  ?  127 PHE   I CD1  1 
ATOM   5386 C  CD2  . PHE   B 1 125 ? -4.795  -29.142 -58.648 1.00 34.63  ?  127 PHE   I CD2  1 
ATOM   5387 C  CE1  . PHE   B 1 125 ? -5.725  -28.465 -56.125 1.00 34.81  ?  127 PHE   I CE1  1 
ATOM   5388 C  CE2  . PHE   B 1 125 ? -3.896  -28.917 -57.616 1.00 35.58  ?  127 PHE   I CE2  1 
ATOM   5389 C  CZ   . PHE   B 1 125 ? -4.360  -28.578 -56.350 1.00 36.02  ?  127 PHE   I CZ   1 
ATOM   5390 N  N    . HIS   B 1 126 ? -5.720  -27.387 -61.734 1.00 38.26  ?  128 HIS   I N    1 
ATOM   5391 C  CA   . HIS   B 1 126 ? -4.586  -26.567 -62.136 1.00 40.02  ?  128 HIS   I CA   1 
ATOM   5392 C  C    . HIS   B 1 126 ? -5.113  -25.254 -62.716 1.00 38.42  ?  128 HIS   I C    1 
ATOM   5393 O  O    . HIS   B 1 126 ? -4.662  -24.202 -62.313 1.00 40.51  ?  128 HIS   I O    1 
ATOM   5394 C  CB   . HIS   B 1 126 ? -3.643  -27.307 -63.096 1.00 41.25  ?  128 HIS   I CB   1 
ATOM   5395 C  CG   . HIS   B 1 126 ? -2.339  -26.598 -63.302 1.00 47.33  ?  128 HIS   I CG   1 
ATOM   5396 N  ND1  . HIS   B 1 126 ? -2.094  -25.790 -64.394 1.00 45.00  ?  128 HIS   I ND1  1 
ATOM   5397 C  CD2  . HIS   B 1 126 ? -1.232  -26.523 -62.521 1.00 49.18  ?  128 HIS   I CD2  1 
ATOM   5398 C  CE1  . HIS   B 1 126 ? -0.881  -25.280 -64.297 1.00 45.57  ?  128 HIS   I CE1  1 
ATOM   5399 N  NE2  . HIS   B 1 126 ? -0.340  -25.701 -63.168 1.00 48.35  ?  128 HIS   I NE2  1 
ATOM   5400 N  N    . ASP   B 1 127 ? -6.081  -25.332 -63.632 1.00 42.37  ?  129 ASP   I N    1 
ATOM   5401 C  CA   . ASP   B 1 127 ? -6.645  -24.161 -64.340 1.00 45.85  ?  129 ASP   I CA   1 
ATOM   5402 C  C    . ASP   B 1 127 ? -7.143  -23.055 -63.403 1.00 45.07  ?  129 ASP   I C    1 
ATOM   5403 O  O    . ASP   B 1 127 ? -6.895  -21.874 -63.652 1.00 49.81  ?  129 ASP   I O    1 
ATOM   5404 C  CB   . ASP   B 1 127 ? -7.812  -24.578 -65.258 1.00 47.33  ?  129 ASP   I CB   1 
ATOM   5405 C  CG   . ASP   B 1 127 ? -7.359  -25.173 -66.586 1.00 54.87  ?  129 ASP   I CG   1 
ATOM   5406 O  OD1  . ASP   B 1 127 ? -6.132  -25.264 -66.844 1.00 58.15  ?  129 ASP   I OD1  1 
ATOM   5407 O  OD2  . ASP   B 1 127 ? -8.256  -25.546 -67.391 1.00 57.44  ?  129 ASP   I OD2  1 
ATOM   5408 N  N    . ASN   B 1 128 ? -7.863  -23.431 -62.347 1.00 40.08  ?  130 ASN   I N    1 
ATOM   5409 C  CA   . ASN   B 1 128 ? -8.268  -22.451 -61.341 1.00 39.48  ?  130 ASN   I CA   1 
ATOM   5410 C  C    . ASN   B 1 128 ? -8.568  -23.121 -59.991 1.00 35.10  ?  130 ASN   I C    1 
ATOM   5411 O  O    . ASN   B 1 128 ? -9.717  -23.477 -59.699 1.00 35.27  ?  130 ASN   I O    1 
ATOM   5412 C  CB   . ASN   B 1 128 ? -9.471  -21.631 -61.842 1.00 41.45  ?  130 ASN   I CB   1 
ATOM   5413 C  CG   . ASN   B 1 128 ? -9.647  -20.348 -61.067 1.00 43.51  ?  130 ASN   I CG   1 
ATOM   5414 O  OD1  . ASN   B 1 128 ? -9.149  -20.226 -59.953 1.00 45.13  ?  130 ASN   I OD1  1 
ATOM   5415 N  ND2  . ASN   B 1 128 ? -10.372 -19.392 -61.639 1.00 43.25  ?  130 ASN   I ND2  1 
ATOM   5416 N  N    . GLU   B 1 129 ? -7.529  -23.268 -59.178 1.00 29.38  ?  131 GLU   I N    1 
ATOM   5417 C  CA   . GLU   B 1 129 ? -7.605  -24.003 -57.923 1.00 31.31  ?  131 GLU   I CA   1 
ATOM   5418 C  C    . GLU   B 1 129 ? -8.724  -23.549 -56.981 1.00 32.22  ?  131 GLU   I C    1 
ATOM   5419 O  O    . GLU   B 1 129 ? -9.456  -24.368 -56.420 1.00 30.87  ?  131 GLU   I O    1 
ATOM   5420 C  CB   . GLU   B 1 129 ? -6.285  -23.889 -57.177 1.00 34.22  ?  131 GLU   I CB   1 
ATOM   5421 C  CG   . GLU   B 1 129 ? -6.002  -25.102 -56.337 1.00 37.29  ?  131 GLU   I CG   1 
ATOM   5422 C  CD   . GLU   B 1 129 ? -4.757  -24.960 -55.504 1.00 40.70  ?  131 GLU   I CD   1 
ATOM   5423 O  OE1  . GLU   B 1 129 ? -3.643  -24.844 -56.069 1.00 44.30  ?  131 GLU   I OE1  1 
ATOM   5424 O  OE2  . GLU   B 1 129 ? -4.902  -24.998 -54.273 1.00 43.94  ?  131 GLU   I OE2  1 
ATOM   5425 N  N    . GLU   B 1 130 ? -8.847  -22.234 -56.831 1.00 32.76  ?  132 GLU   I N    1 
ATOM   5426 C  CA   . GLU   B 1 130 ? -9.748  -21.643 -55.868 1.00 35.14  ?  132 GLU   I CA   1 
ATOM   5427 C  C    . GLU   B 1 130 ? -11.157 -21.903 -56.283 1.00 33.89  ?  132 GLU   I C    1 
ATOM   5428 O  O    . GLU   B 1 130 ? -11.924 -22.397 -55.471 1.00 38.38  ?  132 GLU   I O    1 
ATOM   5429 C  CB   . GLU   B 1 130 ? -9.519  -20.125 -55.701 1.00 38.13  ?  132 GLU   I CB   1 
ATOM   5430 C  CG   . GLU   B 1 130 ? -9.942  -19.612 -54.325 1.00 44.18  ?  132 GLU   I CG   1 
ATOM   5431 C  CD   . GLU   B 1 130 ? -10.173 -18.102 -54.283 1.00 48.64  ?  132 GLU   I CD   1 
ATOM   5432 O  OE1  . GLU   B 1 130 ? -9.369  -17.337 -54.893 1.00 49.34  ?  132 GLU   I OE1  1 
ATOM   5433 O  OE2  . GLU   B 1 130 ? -11.174 -17.683 -53.644 1.00 51.89  ?  132 GLU   I OE2  1 
ATOM   5434 N  N    . THR   B 1 131 ? -11.527 -21.589 -57.526 1.00 33.97  ?  133 THR   I N    1 
ATOM   5435 C  CA   . THR   B 1 131 ? -12.900 -21.891 -57.952 1.00 34.21  ?  133 THR   I CA   1 
ATOM   5436 C  C    . THR   B 1 131 ? -13.182 -23.401 -58.058 1.00 29.95  ?  133 THR   I C    1 
ATOM   5437 O  O    . THR   B 1 131 ? -14.327 -23.804 -57.830 1.00 32.49  ?  133 THR   I O    1 
ATOM   5438 C  CB   . THR   B 1 131 ? -13.348 -21.100 -59.202 1.00 38.63  ?  133 THR   I CB   1 
ATOM   5439 O  OG1  . THR   B 1 131 ? -12.272 -21.009 -60.125 1.00 45.15  ?  133 THR   I OG1  1 
ATOM   5440 C  CG2  . THR   B 1 131 ? -13.772 -19.660 -58.818 1.00 38.84  ?  133 THR   I CG2  1 
ATOM   5441 N  N    . PHE   B 1 132 ? -12.176 -24.236 -58.352 1.00 26.56  ?  134 PHE   I N    1 
ATOM   5442 C  CA   . PHE   B 1 132 ? -12.368 -25.714 -58.328 1.00 24.99  ?  134 PHE   I CA   1 
ATOM   5443 C  C    . PHE   B 1 132 ? -12.731 -26.195 -56.924 1.00 25.82  ?  134 PHE   I C    1 
ATOM   5444 O  O    . PHE   B 1 132 ? -13.711 -26.908 -56.751 1.00 24.49  ?  134 PHE   I O    1 
ATOM   5445 C  CB   . PHE   B 1 132 ? -11.147 -26.474 -58.897 1.00 24.27  ?  134 PHE   I CB   1 
ATOM   5446 C  CG   . PHE   B 1 132 ? -11.234 -27.979 -58.766 1.00 23.59  ?  134 PHE   I CG   1 
ATOM   5447 C  CD1  . PHE   B 1 132 ? -12.038 -28.722 -59.590 1.00 25.06  ?  134 PHE   I CD1  1 
ATOM   5448 C  CD2  . PHE   B 1 132 ? -10.524 -28.645 -57.785 1.00 24.68  ?  134 PHE   I CD2  1 
ATOM   5449 C  CE1  . PHE   B 1 132 ? -12.104 -30.117 -59.456 1.00 24.45  ?  134 PHE   I CE1  1 
ATOM   5450 C  CE2  . PHE   B 1 132 ? -10.617 -30.023 -57.618 1.00 23.61  ?  134 PHE   I CE2  1 
ATOM   5451 C  CZ   . PHE   B 1 132 ? -11.385 -30.756 -58.474 1.00 23.20  ?  134 PHE   I CZ   1 
ATOM   5452 N  N    . LEU   B 1 133 ? -11.958 -25.761 -55.922 1.00 26.64  ?  135 LEU   I N    1 
ATOM   5453 C  CA   . LEU   B 1 133 ? -12.099 -26.260 -54.536 1.00 26.23  ?  135 LEU   I CA   1 
ATOM   5454 C  C    . LEU   B 1 133 ? -13.325 -25.676 -53.841 1.00 25.03  ?  135 LEU   I C    1 
ATOM   5455 O  O    . LEU   B 1 133 ? -14.054 -26.392 -53.194 1.00 22.42  ?  135 LEU   I O    1 
ATOM   5456 C  CB   . LEU   B 1 133 ? -10.837 -25.962 -53.711 1.00 27.45  ?  135 LEU   I CB   1 
ATOM   5457 C  CG   . LEU   B 1 133 ? -9.504  -26.670 -54.058 1.00 27.73  ?  135 LEU   I CG   1 
ATOM   5458 C  CD1  . LEU   B 1 133 ? -8.319  -26.183 -53.186 1.00 26.24  ?  135 LEU   I CD1  1 
ATOM   5459 C  CD2  . LEU   B 1 133 ? -9.669  -28.179 -53.943 1.00 27.50  ?  135 LEU   I CD2  1 
ATOM   5460 N  N    . LYS   B 1 134 ? -13.551 -24.380 -54.038 1.00 24.86  ?  136 LYS   I N    1 
ATOM   5461 C  CA   . LYS   B 1 134 ? -14.665 -23.673 -53.444 1.00 22.81  ?  136 LYS   I CA   1 
ATOM   5462 C  C    . LYS   B 1 134 ? -16.016 -24.047 -54.059 1.00 22.08  ?  136 LYS   I C    1 
ATOM   5463 O  O    . LYS   B 1 134 ? -16.984 -24.143 -53.321 1.00 21.76  ?  136 LYS   I O    1 
ATOM   5464 C  CB   . LYS   B 1 134 ? -14.488 -22.154 -53.585 1.00 23.25  ?  136 LYS   I CB   1 
ATOM   5465 C  CG   . LYS   B 1 134 ? -13.284 -21.559 -52.898 1.00 26.18  ?  136 LYS   I CG   1 
ATOM   5466 C  CD   . LYS   B 1 134 ? -13.426 -21.553 -51.385 1.00 28.57  ?  136 LYS   I CD   1 
ATOM   5467 C  CE   . LYS   B 1 134 ? -12.220 -20.923 -50.711 1.00 27.79  ?  136 LYS   I CE   1 
ATOM   5468 N  NZ   . LYS   B 1 134 ? -12.331 -19.441 -50.727 1.00 26.20  ?  136 LYS   I NZ   1 
ATOM   5469 N  N    . LYS   B 1 135 ? -16.101 -24.181 -55.391 1.00 20.41  ?  137 LYS   I N    1 
ATOM   5470 C  CA   . LYS   B 1 135 ? -17.330 -24.644 -56.030 1.00 21.91  ?  137 LYS   I CA   1 
ATOM   5471 C  C    . LYS   B 1 135 ? -17.690 -25.967 -55.499 1.00 20.98  ?  137 LYS   I C    1 
ATOM   5472 O  O    . LYS   B 1 135 ? -18.832 -26.190 -55.213 1.00 22.50  ?  137 LYS   I O    1 
ATOM   5473 C  CB   . LYS   B 1 135 ? -17.247 -24.750 -57.569 1.00 22.69  ?  137 LYS   I CB   1 
ATOM   5474 N  N    . TYR   B 1 136 ? -16.727 -26.849 -55.314 1.00 21.72  ?  138 TYR   I N    1 
ATOM   5475 C  CA   . TYR   B 1 136 ? -17.040 -28.145 -54.716 1.00 23.60  ?  138 TYR   I CA   1 
ATOM   5476 C  C    . TYR   B 1 136 ? -17.283 -28.079 -53.190 1.00 21.69  ?  138 TYR   I C    1 
ATOM   5477 O  O    . TYR   B 1 136 ? -18.001 -28.912 -52.636 1.00 19.10  ?  138 TYR   I O    1 
ATOM   5478 C  CB   . TYR   B 1 136 ? -15.948 -29.157 -55.023 1.00 27.69  ?  138 TYR   I CB   1 
ATOM   5479 C  CG   . TYR   B 1 136 ? -16.203 -29.997 -56.238 1.00 30.55  ?  138 TYR   I CG   1 
ATOM   5480 C  CD1  . TYR   B 1 136 ? -16.880 -31.210 -56.129 1.00 31.78  ?  138 TYR   I CD1  1 
ATOM   5481 C  CD2  . TYR   B 1 136 ? -15.724 -29.610 -57.511 1.00 35.77  ?  138 TYR   I CD2  1 
ATOM   5482 C  CE1  . TYR   B 1 136 ? -17.091 -32.010 -57.252 1.00 34.09  ?  138 TYR   I CE1  1 
ATOM   5483 C  CE2  . TYR   B 1 136 ? -15.946 -30.404 -58.640 1.00 35.13  ?  138 TYR   I CE2  1 
ATOM   5484 C  CZ   . TYR   B 1 136 ? -16.627 -31.597 -58.494 1.00 34.89  ?  138 TYR   I CZ   1 
ATOM   5485 O  OH   . TYR   B 1 136 ? -16.838 -32.406 -59.569 1.00 42.79  ?  138 TYR   I OH   1 
ATOM   5486 N  N    . LEU   B 1 137 ? -16.694 -27.090 -52.517 1.00 19.22  ?  139 LEU   I N    1 
ATOM   5487 C  CA   . LEU   B 1 137 ? -16.948 -26.903 -51.066 1.00 18.46  ?  139 LEU   I CA   1 
ATOM   5488 C  C    . LEU   B 1 137 ? -18.430 -26.463 -50.904 1.00 19.39  ?  139 LEU   I C    1 
ATOM   5489 O  O    . LEU   B 1 137 ? -19.157 -26.998 -50.057 1.00 19.37  ?  139 LEU   I O    1 
ATOM   5490 C  CB   . LEU   B 1 137 ? -15.954 -25.922 -50.454 1.00 15.98  ?  139 LEU   I CB   1 
ATOM   5491 C  CG   . LEU   B 1 137 ? -16.023 -25.621 -48.941 1.00 16.00  ?  139 LEU   I CG   1 
ATOM   5492 C  CD1  . LEU   B 1 137 ? -15.789 -26.811 -48.032 1.00 15.48  ?  139 LEU   I CD1  1 
ATOM   5493 C  CD2  . LEU   B 1 137 ? -15.035 -24.513 -48.646 1.00 16.52  ?  139 LEU   I CD2  1 
ATOM   5494 N  N    . TYR   B 1 138 ? -18.855 -25.564 -51.784 1.00 20.10  ?  140 TYR   I N    1 
ATOM   5495 C  CA   . TYR   B 1 138 ? -20.268 -25.148 -51.930 1.00 22.46  ?  140 TYR   I CA   1 
ATOM   5496 C  C    . TYR   B 1 138 ? -21.204 -26.314 -52.221 1.00 21.48  ?  140 TYR   I C    1 
ATOM   5497 O  O    . TYR   B 1 138 ? -22.197 -26.472 -51.540 1.00 21.74  ?  140 TYR   I O    1 
ATOM   5498 C  CB   . TYR   B 1 138 ? -20.413 -24.039 -52.972 1.00 22.91  ?  140 TYR   I CB   1 
ATOM   5499 C  CG   . TYR   B 1 138 ? -21.757 -23.953 -53.665 1.00 24.00  ?  140 TYR   I CG   1 
ATOM   5500 C  CD1  . TYR   B 1 138 ? -22.803 -23.256 -53.111 1.00 27.25  ?  140 TYR   I CD1  1 
ATOM   5501 C  CD2  . TYR   B 1 138 ? -21.938 -24.505 -54.924 1.00 28.07  ?  140 TYR   I CD2  1 
ATOM   5502 C  CE1  . TYR   B 1 138 ? -24.036 -23.159 -53.757 1.00 26.49  ?  140 TYR   I CE1  1 
ATOM   5503 C  CE2  . TYR   B 1 138 ? -23.154 -24.410 -55.597 1.00 27.78  ?  140 TYR   I CE2  1 
ATOM   5504 C  CZ   . TYR   B 1 138 ? -24.205 -23.736 -55.003 1.00 28.13  ?  140 TYR   I CZ   1 
ATOM   5505 O  OH   . TYR   B 1 138 ? -25.417 -23.667 -55.653 1.00 24.04  ?  140 TYR   I OH   1 
ATOM   5506 N  N    . GLU   B 1 139 ? -20.859 -27.150 -53.180 1.00 23.53  ?  141 GLU   I N    1 
ATOM   5507 C  CA   . GLU   B 1 139 ? -21.716 -28.315 -53.527 1.00 24.43  ?  141 GLU   I CA   1 
ATOM   5508 C  C    . GLU   B 1 139 ? -21.871 -29.259 -52.368 1.00 23.97  ?  141 GLU   I C    1 
ATOM   5509 O  O    . GLU   B 1 139 ? -22.945 -29.767 -52.134 1.00 27.22  ?  141 GLU   I O    1 
ATOM   5510 C  CB   . GLU   B 1 139 ? -21.201 -29.080 -54.745 1.00 24.08  ?  141 GLU   I CB   1 
ATOM   5511 C  CG   . GLU   B 1 139 ? -21.280 -28.287 -56.045 1.00 25.81  ?  141 GLU   I CG   1 
ATOM   5512 C  CD   . GLU   B 1 139 ? -22.673 -28.081 -56.579 1.00 27.27  ?  141 GLU   I CD   1 
ATOM   5513 O  OE1  . GLU   B 1 139 ? -23.642 -28.606 -56.007 1.00 30.44  ?  141 GLU   I OE1  1 
ATOM   5514 O  OE2  . GLU   B 1 139 ? -22.812 -27.386 -57.594 1.00 29.66  ?  141 GLU   I OE2  1 
ATOM   5515 N  N    . ILE   B 1 140 ? -20.819 -29.453 -51.600 1.00 24.39  ?  142 ILE   I N    1 
ATOM   5516 C  CA   . ILE   B 1 140 ? -20.868 -30.392 -50.467 1.00 24.27  ?  142 ILE   I CA   1 
ATOM   5517 C  C    . ILE   B 1 140 ? -21.627 -29.773 -49.286 1.00 23.75  ?  142 ILE   I C    1 
ATOM   5518 O  O    . ILE   B 1 140 ? -22.399 -30.447 -48.600 1.00 23.17  ?  142 ILE   I O    1 
ATOM   5519 C  CB   . ILE   B 1 140 ? -19.449 -30.783 -50.032 1.00 24.77  ?  142 ILE   I CB   1 
ATOM   5520 C  CG1  . ILE   B 1 140 ? -18.628 -31.282 -51.259 1.00 29.15  ?  142 ILE   I CG1  1 
ATOM   5521 C  CG2  . ILE   B 1 140 ? -19.484 -31.852 -48.940 1.00 24.31  ?  142 ILE   I CG2  1 
ATOM   5522 C  CD1  . ILE   B 1 140 ? -18.943 -32.666 -51.761 1.00 31.45  ?  142 ILE   I CD1  1 
ATOM   5523 N  N    . ALA   B 1 141 ? -21.344 -28.500 -49.028 1.00 21.79  ?  143 ALA   I N    1 
ATOM   5524 C  CA   . ALA   B 1 141 ? -21.990 -27.743 -47.969 1.00 21.76  ?  143 ALA   I CA   1 
ATOM   5525 C  C    . ALA   B 1 141 ? -23.505 -27.699 -48.125 1.00 20.33  ?  143 ALA   I C    1 
ATOM   5526 O  O    . ALA   B 1 141 ? -24.220 -27.838 -47.143 1.00 16.18  ?  143 ALA   I O    1 
ATOM   5527 C  CB   . ALA   B 1 141 ? -21.466 -26.307 -47.978 1.00 22.88  ?  143 ALA   I CB   1 
ATOM   5528 N  N    . ARG   B 1 142 ? -23.957 -27.447 -49.361 1.00 20.85  ?  144 ARG   I N    1 
ATOM   5529 C  CA   . ARG   B 1 142 ? -25.386 -27.292 -49.667 1.00 23.22  ?  144 ARG   I CA   1 
ATOM   5530 C  C    . ARG   B 1 142 ? -26.146 -28.632 -49.589 1.00 23.18  ?  144 ARG   I C    1 
ATOM   5531 O  O    . ARG   B 1 142 ? -27.342 -28.648 -49.335 1.00 25.33  ?  144 ARG   I O    1 
ATOM   5532 C  CB   . ARG   B 1 142 ? -25.575 -26.628 -51.028 1.00 24.85  ?  144 ARG   I CB   1 
ATOM   5533 C  CG   . ARG   B 1 142 ? -25.308 -27.568 -52.206 1.00 27.81  ?  144 ARG   I CG   1 
ATOM   5534 C  CD   . ARG   B 1 142 ? -24.906 -26.884 -53.480 1.00 32.31  ?  144 ARG   I CD   1 
ATOM   5535 N  NE   . ARG   B 1 142 ? -26.005 -26.139 -54.063 1.00 36.04  ?  144 ARG   I NE   1 
ATOM   5536 C  CZ   . ARG   B 1 142 ? -26.552 -26.313 -55.266 1.00 33.14  ?  144 ARG   I CZ   1 
ATOM   5537 N  NH1  . ARG   B 1 142 ? -26.104 -27.197 -56.139 1.00 33.49  ?  144 ARG   I NH1  1 
ATOM   5538 N  NH2  . ARG   B 1 142 ? -27.558 -25.517 -55.606 1.00 34.95  ?  144 ARG   I NH2  1 
ATOM   5539 N  N    . ARG   B 1 143 ? -25.443 -29.727 -49.815 1.00 24.10  ?  145 ARG   I N    1 
ATOM   5540 C  CA   . ARG   B 1 143 ? -25.985 -31.071 -49.619 1.00 26.45  ?  145 ARG   I CA   1 
ATOM   5541 C  C    . ARG   B 1 143 ? -25.942 -31.551 -48.173 1.00 28.86  ?  145 ARG   I C    1 
ATOM   5542 O  O    . ARG   B 1 143 ? -26.742 -32.410 -47.810 1.00 29.56  ?  145 ARG   I O    1 
ATOM   5543 C  CB   . ARG   B 1 143 ? -25.234 -32.082 -50.517 1.00 27.06  ?  145 ARG   I CB   1 
ATOM   5544 C  CG   . ARG   B 1 143 ? -25.507 -31.909 -52.004 1.00 24.82  ?  145 ARG   I CG   1 
ATOM   5545 C  CD   . ARG   B 1 143 ? -24.627 -32.777 -52.911 1.00 24.05  ?  145 ARG   I CD   1 
ATOM   5546 N  NE   . ARG   B 1 143 ? -25.084 -32.711 -54.304 1.00 22.42  ?  145 ARG   I NE   1 
ATOM   5547 C  CZ   . ARG   B 1 143 ? -24.937 -31.677 -55.137 1.00 24.72  ?  145 ARG   I CZ   1 
ATOM   5548 N  NH1  . ARG   B 1 143 ? -24.294 -30.563 -54.799 1.00 24.90  ?  145 ARG   I NH1  1 
ATOM   5549 N  NH2  . ARG   B 1 143 ? -25.465 -31.735 -56.349 1.00 27.55  ?  145 ARG   I NH2  1 
ATOM   5550 N  N    . HIS   B 1 144 ? -25.043 -30.993 -47.343 1.00 30.41  ?  146 HIS   I N    1 
ATOM   5551 C  CA   . HIS   B 1 144 ? -24.885 -31.371 -45.927 1.00 29.01  ?  146 HIS   I CA   1 
ATOM   5552 C  C    . HIS   B 1 144 ? -25.024 -30.172 -44.994 1.00 29.72  ?  146 HIS   I C    1 
ATOM   5553 O  O    . HIS   B 1 144 ? -24.058 -29.798 -44.310 1.00 26.99  ?  146 HIS   I O    1 
ATOM   5554 C  CB   . HIS   B 1 144 ? -23.506 -31.984 -45.700 1.00 31.39  ?  146 HIS   I CB   1 
ATOM   5555 C  CG   . HIS   B 1 144 ? -23.343 -33.310 -46.346 1.00 32.65  ?  146 HIS   I CG   1 
ATOM   5556 N  ND1  . HIS   B 1 144 ? -23.280 -34.476 -45.622 1.00 33.63  ?  146 HIS   I ND1  1 
ATOM   5557 C  CD2  . HIS   B 1 144 ? -23.306 -33.667 -47.645 1.00 33.62  ?  146 HIS   I CD2  1 
ATOM   5558 C  CE1  . HIS   B 1 144 ? -23.181 -35.500 -46.448 1.00 35.53  ?  146 HIS   I CE1  1 
ATOM   5559 N  NE2  . HIS   B 1 144 ? -23.213 -35.038 -47.682 1.00 34.39  ?  146 HIS   I NE2  1 
ATOM   5560 N  N    . PRO   B 1 145 ? -26.240 -29.608 -44.906 1.00 27.63  ?  147 PRO   I N    1 
ATOM   5561 C  CA   . PRO   B 1 145 ? -26.385 -28.298 -44.283 1.00 28.18  ?  147 PRO   I CA   1 
ATOM   5562 C  C    . PRO   B 1 145 ? -26.148 -28.338 -42.774 1.00 27.78  ?  147 PRO   I C    1 
ATOM   5563 O  O    . PRO   B 1 145 ? -26.035 -27.284 -42.182 1.00 24.75  ?  147 PRO   I O    1 
ATOM   5564 C  CB   . PRO   B 1 145 ? -27.842 -27.923 -44.594 1.00 28.43  ?  147 PRO   I CB   1 
ATOM   5565 C  CG   . PRO   B 1 145 ? -28.528 -29.261 -44.627 1.00 27.21  ?  147 PRO   I CG   1 
ATOM   5566 C  CD   . PRO   B 1 145 ? -27.545 -30.235 -45.199 1.00 25.91  ?  147 PRO   I CD   1 
ATOM   5567 N  N    . TYR   B 1 146 ? -26.077 -29.530 -42.171 1.00 29.43  ?  148 TYR   I N    1 
ATOM   5568 C  CA   . TYR   B 1 146 ? -25.728 -29.691 -40.745 1.00 33.94  ?  148 TYR   I CA   1 
ATOM   5569 C  C    . TYR   B 1 146 ? -24.271 -30.094 -40.416 1.00 30.74  ?  148 TYR   I C    1 
ATOM   5570 O  O    . TYR   B 1 146 ? -23.906 -30.139 -39.255 1.00 33.62  ?  148 TYR   I O    1 
ATOM   5571 C  CB   . TYR   B 1 146 ? -26.711 -30.683 -40.081 1.00 39.29  ?  148 TYR   I CB   1 
ATOM   5572 C  CG   . TYR   B 1 146 ? -28.133 -30.152 -40.079 1.00 43.74  ?  148 TYR   I CG   1 
ATOM   5573 C  CD1  . TYR   B 1 146 ? -28.549 -29.203 -39.130 1.00 44.02  ?  148 TYR   I CD1  1 
ATOM   5574 C  CD2  . TYR   B 1 146 ? -29.056 -30.565 -41.044 1.00 44.28  ?  148 TYR   I CD2  1 
ATOM   5575 C  CE1  . TYR   B 1 146 ? -29.853 -28.698 -39.140 1.00 45.67  ?  148 TYR   I CE1  1 
ATOM   5576 C  CE2  . TYR   B 1 146 ? -30.353 -30.050 -41.062 1.00 45.87  ?  148 TYR   I CE2  1 
ATOM   5577 C  CZ   . TYR   B 1 146 ? -30.748 -29.124 -40.114 1.00 46.02  ?  148 TYR   I CZ   1 
ATOM   5578 O  OH   . TYR   B 1 146 ? -32.045 -28.635 -40.159 1.00 47.99  ?  148 TYR   I OH   1 
ATOM   5579 N  N    . PHE   B 1 147 ? -23.434 -30.348 -41.411 1.00 30.09  ?  149 PHE   I N    1 
ATOM   5580 C  CA   . PHE   B 1 147 ? -22.053 -30.841 -41.172 1.00 27.26  ?  149 PHE   I CA   1 
ATOM   5581 C  C    . PHE   B 1 147 ? -21.282 -29.695 -40.511 1.00 25.58  ?  149 PHE   I C    1 
ATOM   5582 O  O    . PHE   B 1 147 ? -21.322 -28.587 -41.015 1.00 24.00  ?  149 PHE   I O    1 
ATOM   5583 C  CB   . PHE   B 1 147 ? -21.463 -31.219 -42.530 1.00 27.72  ?  149 PHE   I CB   1 
ATOM   5584 C  CG   . PHE   B 1 147 ? -20.206 -32.057 -42.490 1.00 27.86  ?  149 PHE   I CG   1 
ATOM   5585 C  CD1  . PHE   B 1 147 ? -18.979 -31.488 -42.241 1.00 29.01  ?  149 PHE   I CD1  1 
ATOM   5586 C  CD2  . PHE   B 1 147 ? -20.250 -33.396 -42.828 1.00 30.47  ?  149 PHE   I CD2  1 
ATOM   5587 C  CE1  . PHE   B 1 147 ? -17.825 -32.253 -42.238 1.00 28.66  ?  149 PHE   I CE1  1 
ATOM   5588 C  CE2  . PHE   B 1 147 ? -19.101 -34.166 -42.825 1.00 29.42  ?  149 PHE   I CE2  1 
ATOM   5589 C  CZ   . PHE   B 1 147 ? -17.893 -33.597 -42.527 1.00 28.28  ?  149 PHE   I CZ   1 
ATOM   5590 N  N    . TYR   B 1 148 ? -20.623 -29.945 -39.375 1.00 23.74  ?  150 TYR   I N    1 
ATOM   5591 C  CA   . TYR   B 1 148 ? -19.986 -28.883 -38.643 1.00 21.55  ?  150 TYR   I CA   1 
ATOM   5592 C  C    . TYR   B 1 148 ? -19.047 -28.085 -39.569 1.00 20.13  ?  150 TYR   I C    1 
ATOM   5593 O  O    . TYR   B 1 148 ? -18.170 -28.688 -40.195 1.00 20.18  ?  150 TYR   I O    1 
ATOM   5594 C  CB   . TYR   B 1 148 ? -19.226 -29.491 -37.455 1.00 24.04  ?  150 TYR   I CB   1 
ATOM   5595 C  CG   . TYR   B 1 148 ? -18.622 -28.462 -36.558 1.00 21.79  ?  150 TYR   I CG   1 
ATOM   5596 C  CD1  . TYR   B 1 148 ? -19.402 -27.422 -36.060 1.00 21.90  ?  150 TYR   I CD1  1 
ATOM   5597 C  CD2  . TYR   B 1 148 ? -17.286 -28.499 -36.236 1.00 21.94  ?  150 TYR   I CD2  1 
ATOM   5598 C  CE1  . TYR   B 1 148 ? -18.862 -26.449 -35.234 1.00 23.66  ?  150 TYR   I CE1  1 
ATOM   5599 C  CE2  . TYR   B 1 148 ? -16.727 -27.525 -35.396 1.00 22.81  ?  150 TYR   I CE2  1 
ATOM   5600 C  CZ   . TYR   B 1 148 ? -17.524 -26.515 -34.897 1.00 22.63  ?  150 TYR   I CZ   1 
ATOM   5601 O  OH   . TYR   B 1 148 ? -17.030 -25.534 -34.146 1.00 21.58  ?  150 TYR   I OH   1 
ATOM   5602 N  N    . ALA   B 1 149 ? -19.251 -26.765 -39.743 1.00 17.37  ?  151 ALA   I N    1 
ATOM   5603 C  CA   . ALA   B 1 149 ? -18.500 -26.059 -40.779 1.00 16.53  ?  151 ALA   I CA   1 
ATOM   5604 C  C    . ALA   B 1 149 ? -16.997 -26.286 -40.729 1.00 15.69  ?  151 ALA   I C    1 
ATOM   5605 O  O    . ALA   B 1 149 ? -16.373 -26.487 -41.747 1.00 15.04  ?  151 ALA   I O    1 
ATOM   5606 C  CB   . ALA   B 1 149 ? -18.792 -24.557 -40.835 1.00 16.53  ?  151 ALA   I CB   1 
ATOM   5607 N  N    . PRO   B 1 150 ? -16.395 -26.223 -39.562 1.00 17.41  ?  152 PRO   I N    1 
ATOM   5608 C  CA   . PRO   B 1 150 ? -14.924 -26.326 -39.590 1.00 17.58  ?  152 PRO   I CA   1 
ATOM   5609 C  C    . PRO   B 1 150 ? -14.419 -27.762 -39.859 1.00 17.81  ?  152 PRO   I C    1 
ATOM   5610 O  O    . PRO   B 1 150 ? -13.248 -27.951 -40.203 1.00 18.50  ?  152 PRO   I O    1 
ATOM   5611 C  CB   . PRO   B 1 150 ? -14.511 -25.855 -38.177 1.00 19.45  ?  152 PRO   I CB   1 
ATOM   5612 C  CG   . PRO   B 1 150 ? -15.719 -25.110 -37.633 1.00 19.79  ?  152 PRO   I CG   1 
ATOM   5613 C  CD   . PRO   B 1 150 ? -16.912 -25.742 -38.264 1.00 19.10  ?  152 PRO   I CD   1 
ATOM   5614 N  N    . GLU   B 1 151 ? -15.228 -28.791 -39.674 1.00 17.86  ?  153 GLU   I N    1 
ATOM   5615 C  CA   . GLU   B 1 151 ? -14.708 -30.121 -40.038 1.00 20.31  ?  153 GLU   I CA   1 
ATOM   5616 C  C    . GLU   B 1 151 ? -14.789 -30.220 -41.628 1.00 19.11  ?  153 GLU   I C    1 
ATOM   5617 O  O    . GLU   B 1 151 ? -13.878 -30.724 -42.289 1.00 17.54  ?  153 GLU   I O    1 
ATOM   5618 C  CB   . GLU   B 1 151 ? -15.437 -31.211 -39.212 1.00 24.47  ?  153 GLU   I CB   1 
ATOM   5619 C  CG   . GLU   B 1 151 ? -14.889 -32.642 -39.252 1.00 30.54  ?  153 GLU   I CG   1 
ATOM   5620 C  CD   . GLU   B 1 151 ? -13.456 -32.846 -38.662 1.00 37.82  ?  153 GLU   I CD   1 
ATOM   5621 O  OE1  . GLU   B 1 151 ? -12.808 -31.844 -38.224 1.00 43.33  ?  153 GLU   I OE1  1 
ATOM   5622 O  OE2  . GLU   B 1 151 ? -12.976 -34.033 -38.632 1.00 37.59  ?  153 GLU   I OE2  1 
ATOM   5623 N  N    . LEU   B 1 152 ? -15.792 -29.604 -42.245 1.00 18.59  ?  154 LEU   I N    1 
ATOM   5624 C  CA   . LEU   B 1 152 ? -15.826 -29.551 -43.712 1.00 21.87  ?  154 LEU   I CA   1 
ATOM   5625 C  C    . LEU   B 1 152 ? -14.525 -28.906 -44.261 1.00 24.13  ?  154 LEU   I C    1 
ATOM   5626 O  O    . LEU   B 1 152 ? -13.907 -29.394 -45.218 1.00 22.70  ?  154 LEU   I O    1 
ATOM   5627 C  CB   . LEU   B 1 152 ? -17.066 -28.819 -44.195 1.00 23.05  ?  154 LEU   I CB   1 
ATOM   5628 C  CG   . LEU   B 1 152 ? -17.753 -29.304 -45.472 1.00 24.10  ?  154 LEU   I CG   1 
ATOM   5629 C  CD1  . LEU   B 1 152 ? -18.268 -30.752 -45.441 1.00 25.42  ?  154 LEU   I CD1  1 
ATOM   5630 C  CD2  . LEU   B 1 152 ? -18.873 -28.349 -45.776 1.00 23.96  ?  154 LEU   I CD2  1 
ATOM   5631 N  N    . LEU   B 1 153 ? -14.072 -27.870 -43.566 1.00 23.25  ?  155 LEU   I N    1 
ATOM   5632 C  CA   . LEU   B 1 153 ? -12.957 -27.120 -43.998 1.00 24.58  ?  155 LEU   I CA   1 
ATOM   5633 C  C    . LEU   B 1 153 ? -11.715 -27.973 -43.815 1.00 25.15  ?  155 LEU   I C    1 
ATOM   5634 O  O    . LEU   B 1 153 ? -10.827 -27.938 -44.619 1.00 24.08  ?  155 LEU   I O    1 
ATOM   5635 C  CB   . LEU   B 1 153 ? -12.897 -25.813 -43.210 1.00 23.45  ?  155 LEU   I CB   1 
ATOM   5636 C  CG   . LEU   B 1 153 ? -11.666 -24.961 -43.460 1.00 23.38  ?  155 LEU   I CG   1 
ATOM   5637 C  CD1  . LEU   B 1 153 ? -11.618 -24.510 -44.902 1.00 23.92  ?  155 LEU   I CD1  1 
ATOM   5638 C  CD2  . LEU   B 1 153 ? -11.674 -23.787 -42.501 1.00 21.71  ?  155 LEU   I CD2  1 
ATOM   5639 N  N    . PHE   B 1 154 ? -11.678 -28.774 -42.759 1.00 29.51  ?  156 PHE   I N    1 
ATOM   5640 C  CA   . PHE   B 1 154 ? -10.616 -29.769 -42.582 1.00 29.06  ?  156 PHE   I CA   1 
ATOM   5641 C  C    . PHE   B 1 154 ? -10.591 -30.858 -43.699 1.00 27.72  ?  156 PHE   I C    1 
ATOM   5642 O  O    . PHE   B 1 154 ? -9.523  -31.298 -44.108 1.00 26.31  ?  156 PHE   I O    1 
ATOM   5643 C  CB   . PHE   B 1 154 ? -10.725 -30.369 -41.166 1.00 32.47  ?  156 PHE   I CB   1 
ATOM   5644 C  CG   . PHE   B 1 154 ? -10.053 -31.719 -40.997 1.00 34.52  ?  156 PHE   I CG   1 
ATOM   5645 C  CD1  . PHE   B 1 154 ? -8.680  -31.806 -40.771 1.00 36.86  ?  156 PHE   I CD1  1 
ATOM   5646 C  CD2  . PHE   B 1 154 ? -10.798 -32.903 -41.080 1.00 35.75  ?  156 PHE   I CD2  1 
ATOM   5647 C  CE1  . PHE   B 1 154 ? -8.063  -33.048 -40.623 1.00 37.46  ?  156 PHE   I CE1  1 
ATOM   5648 C  CE2  . PHE   B 1 154 ? -10.196 -34.144 -40.921 1.00 35.96  ?  156 PHE   I CE2  1 
ATOM   5649 C  CZ   . PHE   B 1 154 ? -8.828  -34.216 -40.690 1.00 38.99  ?  156 PHE   I CZ   1 
ATOM   5650 N  N    . PHE   B 1 155 ? -11.760 -31.333 -44.126 1.00 27.05  ?  157 PHE   I N    1 
ATOM   5651 C  CA   . PHE   B 1 155 ? -11.881 -32.232 -45.301 1.00 26.71  ?  157 PHE   I CA   1 
ATOM   5652 C  C    . PHE   B 1 155 ? -11.450 -31.541 -46.600 1.00 25.02  ?  157 PHE   I C    1 
ATOM   5653 O  O    . PHE   B 1 155 ? -10.675 -32.096 -47.333 1.00 26.49  ?  157 PHE   I O    1 
ATOM   5654 C  CB   . PHE   B 1 155 ? -13.315 -32.795 -45.457 1.00 26.12  ?  157 PHE   I CB   1 
ATOM   5655 C  CG   . PHE   B 1 155 ? -13.567 -34.007 -44.627 1.00 26.21  ?  157 PHE   I CG   1 
ATOM   5656 C  CD1  . PHE   B 1 155 ? -13.903 -33.894 -43.301 1.00 28.79  ?  157 PHE   I CD1  1 
ATOM   5657 C  CD2  . PHE   B 1 155 ? -13.394 -35.269 -45.158 1.00 30.73  ?  157 PHE   I CD2  1 
ATOM   5658 C  CE1  . PHE   B 1 155 ? -14.111 -35.018 -42.519 1.00 30.33  ?  157 PHE   I CE1  1 
ATOM   5659 C  CE2  . PHE   B 1 155 ? -13.601 -36.405 -44.394 1.00 30.06  ?  157 PHE   I CE2  1 
ATOM   5660 C  CZ   . PHE   B 1 155 ? -13.953 -36.276 -43.069 1.00 31.06  ?  157 PHE   I CZ   1 
ATOM   5661 N  N    . ALA   B 1 156 ? -11.930 -30.310 -46.831 1.00 21.36  ?  158 ALA   I N    1 
ATOM   5662 C  CA   . ALA   B 1 156 ? -11.515 -29.500 -47.946 1.00 20.20  ?  158 ALA   I CA   1 
ATOM   5663 C  C    . ALA   B 1 156 ? -9.994  -29.494 -48.050 1.00 19.98  ?  158 ALA   I C    1 
ATOM   5664 O  O    . ALA   B 1 156 ? -9.423  -29.726 -49.140 1.00 21.49  ?  158 ALA   I O    1 
ATOM   5665 C  CB   . ALA   B 1 156 ? -12.075 -28.054 -47.848 1.00 18.94  ?  158 ALA   I CB   1 
ATOM   5666 N  N    . LYS   B 1 157 ? -9.347  -29.283 -46.922 1.00 19.44  ?  159 LYS   I N    1 
ATOM   5667 C  CA   . LYS   B 1 157 ? -7.893  -29.154 -46.875 1.00 21.02  ?  159 LYS   I CA   1 
ATOM   5668 C  C    . LYS   B 1 157 ? -7.182  -30.459 -47.181 1.00 21.25  ?  159 LYS   I C    1 
ATOM   5669 O  O    . LYS   B 1 157 ? -6.143  -30.447 -47.820 1.00 24.36  ?  159 LYS   I O    1 
ATOM   5670 C  CB   . LYS   B 1 157 ? -7.439  -28.541 -45.540 1.00 22.23  ?  159 LYS   I CB   1 
ATOM   5671 C  CG   . LYS   B 1 157 ? -7.678  -27.017 -45.463 1.00 22.57  ?  159 LYS   I CG   1 
ATOM   5672 C  CD   . LYS   B 1 157 ? -7.574  -26.517 -44.026 1.00 24.86  ?  159 LYS   I CD   1 
ATOM   5673 C  CE   . LYS   B 1 157 ? -7.811  -25.009 -43.803 1.00 25.41  ?  159 LYS   I CE   1 
ATOM   5674 N  NZ   . LYS   B 1 157 ? -7.912  -24.170 -45.037 1.00 26.95  ?  159 LYS   I NZ   1 
ATOM   5675 N  N    . ARG   B 1 158 ? -7.761  -31.588 -46.798 1.00 20.92  ?  160 ARG   I N    1 
ATOM   5676 C  CA   . ARG   B 1 158 ? -7.229  -32.871 -47.208 1.00 21.74  ?  160 ARG   I CA   1 
ATOM   5677 C  C    . ARG   B 1 158 ? -7.472  -33.086 -48.722 1.00 22.08  ?  160 ARG   I C    1 
ATOM   5678 O  O    . ARG   B 1 158 ? -6.566  -33.478 -49.420 1.00 20.70  ?  160 ARG   I O    1 
ATOM   5679 C  CB   . ARG   B 1 158 ? -7.841  -33.985 -46.379 1.00 23.53  ?  160 ARG   I CB   1 
ATOM   5680 C  CG   . ARG   B 1 158 ? -7.551  -33.808 -44.892 1.00 26.89  ?  160 ARG   I CG   1 
ATOM   5681 C  CD   . ARG   B 1 158 ? -8.538  -34.556 -44.036 1.00 29.81  ?  160 ARG   I CD   1 
ATOM   5682 N  NE   . ARG   B 1 158 ? -8.181  -35.974 -43.959 1.00 31.06  ?  160 ARG   I NE   1 
ATOM   5683 C  CZ   . ARG   B 1 158 ? -9.008  -36.949 -43.604 1.00 35.12  ?  160 ARG   I CZ   1 
ATOM   5684 N  NH1  . ARG   B 1 158 ? -10.275 -36.707 -43.270 1.00 40.83  ?  160 ARG   I NH1  1 
ATOM   5685 N  NH2  . ARG   B 1 158 ? -8.563  -38.184 -43.580 1.00 37.40  ?  160 ARG   I NH2  1 
ATOM   5686 N  N    . TYR   B 1 159 ? -8.659  -32.780 -49.249 1.00 21.84  ?  161 TYR   I N    1 
ATOM   5687 C  CA   . TYR   B 1 159 ? -8.833  -32.875 -50.708 1.00 23.56  ?  161 TYR   I CA   1 
ATOM   5688 C  C    . TYR   B 1 159 ? -7.805  -32.061 -51.482 1.00 27.10  ?  161 TYR   I C    1 
ATOM   5689 O  O    . TYR   B 1 159 ? -7.191  -32.554 -52.442 1.00 27.30  ?  161 TYR   I O    1 
ATOM   5690 C  CB   . TYR   B 1 159 ? -10.222 -32.447 -51.144 1.00 26.02  ?  161 TYR   I CB   1 
ATOM   5691 C  CG   . TYR   B 1 159 ? -11.226 -33.545 -51.021 1.00 25.29  ?  161 TYR   I CG   1 
ATOM   5692 C  CD1  . TYR   B 1 159 ? -11.238 -34.605 -51.912 1.00 24.61  ?  161 TYR   I CD1  1 
ATOM   5693 C  CD2  . TYR   B 1 159 ? -12.185 -33.518 -50.020 1.00 28.13  ?  161 TYR   I CD2  1 
ATOM   5694 C  CE1  . TYR   B 1 159 ? -12.182 -35.617 -51.806 1.00 24.59  ?  161 TYR   I CE1  1 
ATOM   5695 C  CE2  . TYR   B 1 159 ? -13.123 -34.515 -49.913 1.00 27.71  ?  161 TYR   I CE2  1 
ATOM   5696 C  CZ   . TYR   B 1 159 ? -13.118 -35.556 -50.817 1.00 25.51  ?  161 TYR   I CZ   1 
ATOM   5697 O  OH   . TYR   B 1 159 ? -14.050 -36.534 -50.663 1.00 27.04  ?  161 TYR   I OH   1 
ATOM   5698 N  N    . LYS   B 1 160 ? -7.582  -30.835 -51.039 1.00 27.76  ?  162 LYS   I N    1 
ATOM   5699 C  CA   . LYS   B 1 160 ? -6.592  -29.985 -51.672 1.00 28.60  ?  162 LYS   I CA   1 
ATOM   5700 C  C    . LYS   B 1 160 ? -5.245  -30.706 -51.705 1.00 29.40  ?  162 LYS   I C    1 
ATOM   5701 O  O    . LYS   B 1 160 ? -4.628  -30.803 -52.753 1.00 26.69  ?  162 LYS   I O    1 
ATOM   5702 C  CB   . LYS   B 1 160 ? -6.476  -28.657 -50.938 1.00 27.21  ?  162 LYS   I CB   1 
ATOM   5703 C  CG   . LYS   B 1 160 ? -5.259  -27.842 -51.312 1.00 29.33  ?  162 LYS   I CG   1 
ATOM   5704 C  CD   . LYS   B 1 160 ? -5.444  -26.371 -50.999 1.00 28.41  ?  162 LYS   I CD   1 
ATOM   5705 C  CE   . LYS   B 1 160 ? -4.197  -25.596 -51.345 1.00 32.09  ?  162 LYS   I CE   1 
ATOM   5706 N  NZ   . LYS   B 1 160 ? -4.448  -24.138 -51.581 1.00 34.62  ?  162 LYS   I NZ   1 
ATOM   5707 N  N    . ALA   B 1 161 ? -4.811  -31.217 -50.554 1.00 32.07  ?  163 ALA   I N    1 
ATOM   5708 C  CA   . ALA   B 1 161 ? -3.538  -31.949 -50.446 1.00 34.53  ?  163 ALA   I CA   1 
ATOM   5709 C  C    . ALA   B 1 161 ? -3.450  -33.164 -51.366 1.00 34.64  ?  163 ALA   I C    1 
ATOM   5710 O  O    . ALA   B 1 161 ? -2.364  -33.509 -51.878 1.00 34.84  ?  163 ALA   I O    1 
ATOM   5711 C  CB   . ALA   B 1 161 ? -3.294  -32.391 -49.013 1.00 37.68  ?  163 ALA   I CB   1 
ATOM   5712 N  N    . ALA   B 1 162 ? -4.580  -33.826 -51.556 1.00 31.74  ?  164 ALA   I N    1 
ATOM   5713 C  CA   . ALA   B 1 162 ? -4.612  -34.995 -52.380 1.00 31.00  ?  164 ALA   I CA   1 
ATOM   5714 C  C    . ALA   B 1 162 ? -4.469  -34.629 -53.868 1.00 32.88  ?  164 ALA   I C    1 
ATOM   5715 O  O    . ALA   B 1 162 ? -3.983  -35.425 -54.645 1.00 29.50  ?  164 ALA   I O    1 
ATOM   5716 C  CB   . ALA   B 1 162 ? -5.875  -35.799 -52.123 1.00 31.93  ?  164 ALA   I CB   1 
ATOM   5717 N  N    . PHE   B 1 163 ? -4.862  -33.429 -54.266 1.00 33.62  ?  165 PHE   I N    1 
ATOM   5718 C  CA   . PHE   B 1 163 ? -4.739  -33.042 -55.668 1.00 37.22  ?  165 PHE   I CA   1 
ATOM   5719 C  C    . PHE   B 1 163 ? -3.311  -32.556 -55.935 1.00 39.82  ?  165 PHE   I C    1 
ATOM   5720 O  O    . PHE   B 1 163 ? -2.753  -32.849 -56.989 1.00 37.12  ?  165 PHE   I O    1 
ATOM   5721 C  CB   . PHE   B 1 163 ? -5.819  -32.008 -56.095 1.00 36.97  ?  165 PHE   I CB   1 
ATOM   5722 C  CG   . PHE   B 1 163 ? -7.205  -32.601 -56.216 1.00 35.35  ?  165 PHE   I CG   1 
ATOM   5723 C  CD1  . PHE   B 1 163 ? -7.560  -33.372 -57.307 1.00 35.39  ?  165 PHE   I CD1  1 
ATOM   5724 C  CD2  . PHE   B 1 163 ? -8.143  -32.416 -55.214 1.00 34.43  ?  165 PHE   I CD2  1 
ATOM   5725 C  CE1  . PHE   B 1 163 ? -8.829  -33.938 -57.401 1.00 37.75  ?  165 PHE   I CE1  1 
ATOM   5726 C  CE2  . PHE   B 1 163 ? -9.403  -32.965 -55.295 1.00 33.15  ?  165 PHE   I CE2  1 
ATOM   5727 C  CZ   . PHE   B 1 163 ? -9.760  -33.724 -56.395 1.00 35.96  ?  165 PHE   I CZ   1 
ATOM   5728 N  N    . THR   B 1 164 ? -2.729  -31.835 -54.970 1.00 41.89  ?  166 THR   I N    1 
ATOM   5729 C  CA   . THR   B 1 164 ? -1.356  -31.343 -55.060 1.00 42.27  ?  166 THR   I CA   1 
ATOM   5730 C  C    . THR   B 1 164 ? -0.378  -32.485 -55.270 1.00 43.28  ?  166 THR   I C    1 
ATOM   5731 O  O    . THR   B 1 164 ? 0.456   -32.425 -56.170 1.00 44.02  ?  166 THR   I O    1 
ATOM   5732 C  CB   . THR   B 1 164 ? -0.955  -30.549 -53.806 1.00 43.08  ?  166 THR   I CB   1 
ATOM   5733 O  OG1  . THR   B 1 164 ? -1.931  -29.530 -53.543 1.00 40.55  ?  166 THR   I OG1  1 
ATOM   5734 C  CG2  . THR   B 1 164 ? 0.406   -29.911 -53.986 1.00 41.98  ?  166 THR   I CG2  1 
ATOM   5735 N  N    . GLU   B 1 165 ? -0.518  -33.531 -54.466 1.00 47.72  ?  167 GLU   I N    1 
ATOM   5736 C  CA   . GLU   B 1 165 ? 0.306   -34.724 -54.600 1.00 53.58  ?  167 GLU   I CA   1 
ATOM   5737 C  C    . GLU   B 1 165 ? 0.051   -35.426 -55.937 1.00 59.50  ?  167 GLU   I C    1 
ATOM   5738 O  O    . GLU   B 1 165 ? 0.995   -35.656 -56.708 1.00 63.17  ?  167 GLU   I O    1 
ATOM   5739 C  CB   . GLU   B 1 165 ? 0.057   -35.714 -53.442 1.00 56.91  ?  167 GLU   I CB   1 
ATOM   5740 C  CG   . GLU   B 1 165 ? 1.091   -36.845 -53.318 1.00 59.35  ?  167 GLU   I CG   1 
ATOM   5741 C  CD   . GLU   B 1 165 ? 0.683   -37.997 -52.388 1.00 64.73  ?  167 GLU   I CD   1 
ATOM   5742 O  OE1  . GLU   B 1 165 ? -0.527  -38.212 -52.118 1.00 65.04  ?  167 GLU   I OE1  1 
ATOM   5743 O  OE2  . GLU   B 1 165 ? 1.596   -38.726 -51.936 1.00 67.94  ?  167 GLU   I OE2  1 
ATOM   5744 N  N    . CYS   B 1 166 ? -1.212  -35.749 -56.216 1.00 54.62  ?  168 CYS   I N    1 
ATOM   5745 C  CA   . CYS   B 1 166 ? -1.526  -36.751 -57.228 1.00 54.07  ?  168 CYS   I CA   1 
ATOM   5746 C  C    . CYS   B 1 166 ? -1.742  -36.238 -58.640 1.00 51.63  ?  168 CYS   I C    1 
ATOM   5747 O  O    . CYS   B 1 166 ? -1.749  -37.044 -59.567 1.00 48.46  ?  168 CYS   I O    1 
ATOM   5748 C  CB   . CYS   B 1 166 ? -2.733  -37.585 -56.792 1.00 56.51  ?  168 CYS   I CB   1 
ATOM   5749 S  SG   . CYS   B 1 166 ? -2.438  -38.500 -55.258 1.00 64.27  ?  168 CYS   I SG   1 
ATOM   5750 N  N    . CYS   B 1 167 ? -1.927  -34.927 -58.815 1.00 48.94  ?  169 CYS   I N    1 
ATOM   5751 C  CA   . CYS   B 1 167 ? -2.060  -34.342 -60.155 1.00 46.06  ?  169 CYS   I CA   1 
ATOM   5752 C  C    . CYS   B 1 167 ? -0.702  -34.053 -60.864 1.00 51.74  ?  169 CYS   I C    1 
ATOM   5753 O  O    . CYS   B 1 167 ? -0.683  -33.774 -62.080 1.00 51.49  ?  169 CYS   I O    1 
ATOM   5754 C  CB   . CYS   B 1 167 ? -2.955  -33.092 -60.119 1.00 44.28  ?  169 CYS   I CB   1 
ATOM   5755 S  SG   . CYS   B 1 167 ? -4.719  -33.445 -59.804 1.00 40.68  ?  169 CYS   I SG   1 
ATOM   5756 N  N    . GLN   B 1 168 ? 0.408   -34.109 -60.109 1.00 55.49  ?  170 GLN   I N    1 
ATOM   5757 C  CA   . GLN   B 1 168 ? 1.777   -33.986 -60.656 1.00 55.51  ?  170 GLN   I CA   1 
ATOM   5758 C  C    . GLN   B 1 168 ? 2.519   -35.280 -60.404 1.00 56.38  ?  170 GLN   I C    1 
ATOM   5759 O  O    . GLN   B 1 168 ? 3.566   -35.299 -59.747 1.00 60.04  ?  170 GLN   I O    1 
ATOM   5760 C  CB   . GLN   B 1 168 ? 2.527   -32.816 -60.028 1.00 53.91  ?  170 GLN   I CB   1 
ATOM   5761 C  CG   . GLN   B 1 168 ? 1.959   -31.456 -60.385 1.00 55.97  ?  170 GLN   I CG   1 
ATOM   5762 C  CD   . GLN   B 1 168 ? 2.670   -30.330 -59.671 1.00 56.58  ?  170 GLN   I CD   1 
ATOM   5763 O  OE1  . GLN   B 1 168 ? 3.615   -30.554 -58.910 1.00 60.32  ?  170 GLN   I OE1  1 
ATOM   5764 N  NE2  . GLN   B 1 168 ? 2.216   -29.102 -59.908 1.00 55.79  ?  170 GLN   I NE2  1 
ATOM   5765 N  N    . ALA   B 1 169 ? 1.944   -36.359 -60.932 1.00 55.25  ?  171 ALA   I N    1 
ATOM   5766 C  CA   . ALA   B 1 169 ? 2.478   -37.706 -60.803 1.00 58.60  ?  171 ALA   I CA   1 
ATOM   5767 C  C    . ALA   B 1 169 ? 2.166   -38.494 -62.083 1.00 65.34  ?  171 ALA   I C    1 
ATOM   5768 O  O    . ALA   B 1 169 ? 1.185   -38.199 -62.776 1.00 65.34  ?  171 ALA   I O    1 
ATOM   5769 C  CB   . ALA   B 1 169 ? 1.903   -38.391 -59.578 1.00 54.41  ?  171 ALA   I CB   1 
ATOM   5770 N  N    . ALA   B 1 170 ? 3.014   -39.481 -62.389 1.00 69.23  ?  172 ALA   I N    1 
ATOM   5771 C  CA   . ALA   B 1 170 ? 2.970   -40.215 -63.666 1.00 68.67  ?  172 ALA   I CA   1 
ATOM   5772 C  C    . ALA   B 1 170 ? 1.620   -40.920 -63.911 1.00 68.18  ?  172 ALA   I C    1 
ATOM   5773 O  O    . ALA   B 1 170 ? 0.937   -40.669 -64.918 1.00 72.70  ?  172 ALA   I O    1 
ATOM   5774 C  CB   . ALA   B 1 170 ? 4.122   -41.221 -63.735 1.00 69.20  ?  172 ALA   I CB   1 
ATOM   5775 N  N    . ASP   B 1 171 ? 1.244   -41.790 -62.982 1.00 61.17  ?  173 ASP   I N    1 
ATOM   5776 C  CA   . ASP   B 1 171 ? -0.011  -42.521 -63.053 1.00 58.62  ?  173 ASP   I CA   1 
ATOM   5777 C  C    . ASP   B 1 171 ? -1.021  -41.820 -62.129 1.00 54.86  ?  173 ASP   I C    1 
ATOM   5778 O  O    . ASP   B 1 171 ? -1.373  -42.324 -61.062 1.00 57.61  ?  173 ASP   I O    1 
ATOM   5779 C  CB   . ASP   B 1 171 ? 0.245   -43.979 -62.656 1.00 57.10  ?  173 ASP   I CB   1 
ATOM   5780 C  CG   . ASP   B 1 171 ? -0.955  -44.875 -62.870 1.00 59.08  ?  173 ASP   I CG   1 
ATOM   5781 O  OD1  . ASP   B 1 171 ? -2.052  -44.371 -63.214 1.00 55.48  ?  173 ASP   I OD1  1 
ATOM   5782 O  OD2  . ASP   B 1 171 ? -0.791  -46.105 -62.683 1.00 62.36  ?  173 ASP   I OD2  1 
ATOM   5783 N  N    . LYS   B 1 172 ? -1.490  -40.656 -62.561 1.00 53.37  ?  174 LYS   I N    1 
ATOM   5784 C  CA   . LYS   B 1 172 ? -2.338  -39.789 -61.726 1.00 54.64  ?  174 LYS   I CA   1 
ATOM   5785 C  C    . LYS   B 1 172 ? -3.429  -40.568 -60.959 1.00 54.96  ?  174 LYS   I C    1 
ATOM   5786 O  O    . LYS   B 1 172 ? -3.441  -40.557 -59.730 1.00 53.66  ?  174 LYS   I O    1 
ATOM   5787 C  CB   . LYS   B 1 172 ? -2.931  -38.638 -62.564 1.00 53.06  ?  174 LYS   I CB   1 
ATOM   5788 C  CG   . LYS   B 1 172 ? -1.882  -37.626 -63.020 1.00 52.87  ?  174 LYS   I CG   1 
ATOM   5789 C  CD   . LYS   B 1 172 ? -2.480  -36.349 -63.595 1.00 55.61  ?  174 LYS   I CD   1 
ATOM   5790 C  CE   . LYS   B 1 172 ? -2.968  -36.503 -65.030 1.00 55.26  ?  174 LYS   I CE   1 
ATOM   5791 N  NZ   . LYS   B 1 172 ? -1.881  -36.305 -66.028 1.00 53.91  ?  174 LYS   I NZ   1 
ATOM   5792 N  N    . ALA   B 1 173 ? -4.268  -41.298 -61.698 1.00 55.17  ?  175 ALA   I N    1 
ATOM   5793 C  CA   . ALA   B 1 173 ? -5.391  -42.092 -61.152 1.00 54.72  ?  175 ALA   I CA   1 
ATOM   5794 C  C    . ALA   B 1 173 ? -5.030  -43.203 -60.147 1.00 53.08  ?  175 ALA   I C    1 
ATOM   5795 O  O    . ALA   B 1 173 ? -5.835  -43.529 -59.294 1.00 55.59  ?  175 ALA   I O    1 
ATOM   5796 C  CB   . ALA   B 1 173 ? -6.212  -42.687 -62.304 1.00 54.53  ?  175 ALA   I CB   1 
ATOM   5797 N  N    . ALA   B 1 174 ? -3.849  -43.798 -60.254 1.00 57.36  ?  176 ALA   I N    1 
ATOM   5798 C  CA   . ALA   B 1 174 ? -3.391  -44.773 -59.253 1.00 57.66  ?  176 ALA   I CA   1 
ATOM   5799 C  C    . ALA   B 1 174 ? -3.181  -44.096 -57.901 1.00 57.16  ?  176 ALA   I C    1 
ATOM   5800 O  O    . ALA   B 1 174 ? -3.516  -44.677 -56.868 1.00 57.77  ?  176 ALA   I O    1 
ATOM   5801 C  CB   . ALA   B 1 174 ? -2.105  -45.456 -59.701 1.00 59.01  ?  176 ALA   I CB   1 
ATOM   5802 N  N    . CYS   B 1 175 ? -2.629  -42.879 -57.923 1.00 56.37  ?  177 CYS   I N    1 
ATOM   5803 C  CA   . CYS   B 1 175 ? -2.452  -42.043 -56.719 1.00 56.64  ?  177 CYS   I CA   1 
ATOM   5804 C  C    . CYS   B 1 175 ? -3.804  -41.508 -56.169 1.00 52.64  ?  177 CYS   I C    1 
ATOM   5805 O  O    . CYS   B 1 175 ? -4.086  -41.572 -54.968 1.00 49.35  ?  177 CYS   I O    1 
ATOM   5806 C  CB   . CYS   B 1 175 ? -1.522  -40.866 -57.059 1.00 56.38  ?  177 CYS   I CB   1 
ATOM   5807 S  SG   . CYS   B 1 175 ? -0.921  -39.828 -55.696 1.00 65.17  ?  177 CYS   I SG   1 
ATOM   5808 N  N    . LEU   B 1 176 ? -4.633  -40.978 -57.057 1.00 47.83  ?  178 LEU   I N    1 
ATOM   5809 C  CA   . LEU   B 1 176 ? -5.759  -40.144 -56.650 1.00 46.43  ?  178 LEU   I CA   1 
ATOM   5810 C  C    . LEU   B 1 176 ? -7.012  -40.913 -56.263 1.00 46.06  ?  178 LEU   I C    1 
ATOM   5811 O  O    . LEU   B 1 176 ? -7.507  -40.754 -55.159 1.00 42.59  ?  178 LEU   I O    1 
ATOM   5812 C  CB   . LEU   B 1 176 ? -6.078  -39.137 -57.752 1.00 45.72  ?  178 LEU   I CB   1 
ATOM   5813 C  CG   . LEU   B 1 176 ? -7.083  -38.032 -57.443 1.00 47.35  ?  178 LEU   I CG   1 
ATOM   5814 C  CD1  . LEU   B 1 176 ? -6.850  -37.397 -56.072 1.00 48.12  ?  178 LEU   I CD1  1 
ATOM   5815 C  CD2  . LEU   B 1 176 ? -6.994  -36.979 -58.541 1.00 50.57  ?  178 LEU   I CD2  1 
ATOM   5816 N  N    . LEU   B 1 177 ? -7.515  -41.743 -57.169 1.00 48.10  ?  179 LEU   I N    1 
ATOM   5817 C  CA   . LEU   B 1 177 ? -8.782  -42.468 -56.949 1.00 49.85  ?  179 LEU   I CA   1 
ATOM   5818 C  C    . LEU   B 1 177 ? -8.941  -43.138 -55.570 1.00 49.35  ?  179 LEU   I C    1 
ATOM   5819 O  O    . LEU   B 1 177 ? -10.060 -43.204 -55.067 1.00 46.58  ?  179 LEU   I O    1 
ATOM   5820 C  CB   . LEU   B 1 177 ? -9.034  -43.514 -58.041 1.00 51.46  ?  179 LEU   I CB   1 
ATOM   5821 C  CG   . LEU   B 1 177 ? -9.982  -43.120 -59.169 1.00 56.50  ?  179 LEU   I CG   1 
ATOM   5822 C  CD1  . LEU   B 1 177 ? -9.481  -41.913 -59.936 1.00 58.63  ?  179 LEU   I CD1  1 
ATOM   5823 C  CD2  . LEU   B 1 177 ? -10.186 -44.302 -60.103 1.00 56.78  ?  179 LEU   I CD2  1 
ATOM   5824 N  N    . PRO   B 1 178 ? -7.846  -43.666 -54.980 1.00 50.73  ?  180 PRO   I N    1 
ATOM   5825 C  CA   . PRO   B 1 178 ? -7.965  -44.248 -53.632 1.00 49.78  ?  180 PRO   I CA   1 
ATOM   5826 C  C    . PRO   B 1 178 ? -7.829  -43.266 -52.463 1.00 45.29  ?  180 PRO   I C    1 
ATOM   5827 O  O    . PRO   B 1 178 ? -8.170  -43.622 -51.351 1.00 47.12  ?  180 PRO   I O    1 
ATOM   5828 C  CB   . PRO   B 1 178 ? -6.830  -45.292 -53.594 1.00 52.60  ?  180 PRO   I CB   1 
ATOM   5829 C  CG   . PRO   B 1 178 ? -6.450  -45.512 -55.014 1.00 52.05  ?  180 PRO   I CG   1 
ATOM   5830 C  CD   . PRO   B 1 178 ? -6.622  -44.156 -55.638 1.00 53.51  ?  180 PRO   I CD   1 
ATOM   5831 N  N    . LYS   B 1 179 ? -7.300  -42.068 -52.693 1.00 42.91  ?  181 LYS   I N    1 
ATOM   5832 C  CA   . LYS   B 1 179 ? -7.343  -41.010 -51.674 1.00 39.48  ?  181 LYS   I CA   1 
ATOM   5833 C  C    . LYS   B 1 179 ? -8.764  -40.464 -51.635 1.00 38.01  ?  181 LYS   I C    1 
ATOM   5834 O  O    . LYS   B 1 179 ? -9.331  -40.252 -50.550 1.00 36.34  ?  181 LYS   I O    1 
ATOM   5835 C  CB   . LYS   B 1 179 ? -6.337  -39.888 -51.949 1.00 39.99  ?  181 LYS   I CB   1 
ATOM   5836 C  CG   . LYS   B 1 179 ? -4.971  -40.120 -51.325 1.00 39.59  ?  181 LYS   I CG   1 
ATOM   5837 C  CD   . LYS   B 1 179 ? -4.006  -39.013 -51.695 1.00 40.28  ?  181 LYS   I CD   1 
ATOM   5838 N  N    . LEU   B 1 180 ? -9.342  -40.264 -52.821 1.00 31.71  ?  182 LEU   I N    1 
ATOM   5839 C  CA   . LEU   B 1 180 ? -10.690 -39.777 -52.926 1.00 30.19  ?  182 LEU   I CA   1 
ATOM   5840 C  C    . LEU   B 1 180 ? -11.655 -40.804 -52.336 1.00 31.27  ?  182 LEU   I C    1 
ATOM   5841 O  O    . LEU   B 1 180 ? -12.623 -40.428 -51.682 1.00 30.75  ?  182 LEU   I O    1 
ATOM   5842 C  CB   . LEU   B 1 180 ? -11.023 -39.449 -54.387 1.00 30.94  ?  182 LEU   I CB   1 
ATOM   5843 C  CG   . LEU   B 1 180 ? -10.141 -38.402 -55.095 1.00 31.37  ?  182 LEU   I CG   1 
ATOM   5844 C  CD1  . LEU   B 1 180 ? -10.723 -38.068 -56.457 1.00 31.56  ?  182 LEU   I CD1  1 
ATOM   5845 C  CD2  . LEU   B 1 180 ? -9.929  -37.119 -54.318 1.00 33.17  ?  182 LEU   I CD2  1 
ATOM   5846 N  N    . ASP   B 1 181 ? -11.367 -42.096 -52.512 1.00 32.51  ?  183 ASP   I N    1 
ATOM   5847 C  CA   . ASP   B 1 181 ? -12.179 -43.162 -51.907 1.00 35.45  ?  183 ASP   I CA   1 
ATOM   5848 C  C    . ASP   B 1 181 ? -12.156 -43.057 -50.385 1.00 35.47  ?  183 ASP   I C    1 
ATOM   5849 O  O    . ASP   B 1 181 ? -13.231 -43.017 -49.754 1.00 34.45  ?  183 ASP   I O    1 
ATOM   5850 C  CB   . ASP   B 1 181 ? -11.673 -44.566 -52.305 1.00 39.51  ?  183 ASP   I CB   1 
ATOM   5851 C  CG   . ASP   B 1 181 ? -12.036 -44.972 -53.748 1.00 46.58  ?  183 ASP   I CG   1 
ATOM   5852 O  OD1  . ASP   B 1 181 ? -13.139 -44.615 -54.250 1.00 50.04  ?  183 ASP   I OD1  1 
ATOM   5853 O  OD2  . ASP   B 1 181 ? -11.203 -45.698 -54.363 1.00 51.24  ?  183 ASP   I OD2  1 
ATOM   5854 N  N    . GLU   B 1 182 ? -10.937 -43.022 -49.815 1.00 33.60  ?  184 GLU   I N    1 
ATOM   5855 C  CA   . GLU   B 1 182 ? -10.703 -42.861 -48.350 1.00 35.16  ?  184 GLU   I CA   1 
ATOM   5856 C  C    . GLU   B 1 182 ? -11.389 -41.622 -47.759 1.00 35.19  ?  184 GLU   I C    1 
ATOM   5857 O  O    . GLU   B 1 182 ? -12.006 -41.724 -46.717 1.00 38.91  ?  184 GLU   I O    1 
ATOM   5858 C  CB   . GLU   B 1 182 ? -9.190  -42.801 -48.014 1.00 34.35  ?  184 GLU   I CB   1 
ATOM   5859 N  N    . LEU   B 1 183 ? -11.278 -40.470 -48.431 1.00 35.68  ?  185 LEU   I N    1 
ATOM   5860 C  CA   . LEU   B 1 183 ? -11.970 -39.229 -48.025 1.00 33.02  ?  185 LEU   I CA   1 
ATOM   5861 C  C    . LEU   B 1 183 ? -13.481 -39.339 -48.228 1.00 31.86  ?  185 LEU   I C    1 
ATOM   5862 O  O    . LEU   B 1 183 ? -14.251 -38.960 -47.346 1.00 30.62  ?  185 LEU   I O    1 
ATOM   5863 C  CB   . LEU   B 1 183 ? -11.441 -37.998 -48.791 1.00 34.05  ?  185 LEU   I CB   1 
ATOM   5864 C  CG   . LEU   B 1 183 ? -10.208 -37.165 -48.352 1.00 36.09  ?  185 LEU   I CG   1 
ATOM   5865 C  CD1  . LEU   B 1 183 ? -9.316  -37.842 -47.325 1.00 38.34  ?  185 LEU   I CD1  1 
ATOM   5866 C  CD2  . LEU   B 1 183 ? -9.353  -36.736 -49.552 1.00 35.69  ?  185 LEU   I CD2  1 
ATOM   5867 N  N    . ARG   B 1 184 ? -13.918 -39.809 -49.394 1.00 31.32  ?  186 ARG   I N    1 
ATOM   5868 C  CA   . ARG   B 1 184 ? -15.353 -40.080 -49.583 1.00 35.19  ?  186 ARG   I CA   1 
ATOM   5869 C  C    . ARG   B 1 184 ? -15.894 -40.904 -48.415 1.00 34.59  ?  186 ARG   I C    1 
ATOM   5870 O  O    . ARG   B 1 184 ? -16.880 -40.520 -47.809 1.00 32.65  ?  186 ARG   I O    1 
ATOM   5871 C  CB   . ARG   B 1 184 ? -15.652 -40.784 -50.942 1.00 34.84  ?  186 ARG   I CB   1 
ATOM   5872 C  CG   . ARG   B 1 184 ? -17.080 -41.324 -51.143 1.00 33.19  ?  186 ARG   I CG   1 
ATOM   5873 C  CD   . ARG   B 1 184 ? -17.101 -42.503 -52.126 1.00 32.23  ?  186 ARG   I CD   1 
ATOM   5874 N  NE   . ARG   B 1 184 ? -16.445 -43.732 -51.639 1.00 29.96  ?  186 ARG   I NE   1 
ATOM   5875 N  N    . ASP   B 1 185 ? -15.220 -42.007 -48.094 1.00 36.17  ?  187 ASP   I N    1 
ATOM   5876 C  CA   . ASP   B 1 185 ? -15.665 -42.898 -47.023 1.00 38.41  ?  187 ASP   I CA   1 
ATOM   5877 C  C    . ASP   B 1 185 ? -15.640 -42.189 -45.666 1.00 36.65  ?  187 ASP   I C    1 
ATOM   5878 O  O    . ASP   B 1 185 ? -16.667 -42.086 -44.977 1.00 34.26  ?  187 ASP   I O    1 
ATOM   5879 C  CB   . ASP   B 1 185 ? -14.774 -44.147 -46.956 1.00 41.25  ?  187 ASP   I CB   1 
ATOM   5880 C  CG   . ASP   B 1 185 ? -14.871 -45.027 -48.197 1.00 43.94  ?  187 ASP   I CG   1 
ATOM   5881 O  OD1  . ASP   B 1 185 ? -15.864 -44.914 -48.975 1.00 44.13  ?  187 ASP   I OD1  1 
ATOM   5882 O  OD2  . ASP   B 1 185 ? -13.924 -45.835 -48.381 1.00 44.91  ?  187 ASP   I OD2  1 
ATOM   5883 N  N    . GLU   B 1 186 ? -14.467 -41.668 -45.313 1.00 35.64  ?  188 GLU   I N    1 
ATOM   5884 C  CA   . GLU   B 1 186 ? -14.278 -40.925 -44.062 1.00 37.09  ?  188 GLU   I CA   1 
ATOM   5885 C  C    . GLU   B 1 186 ? -15.263 -39.760 -43.914 1.00 33.90  ?  188 GLU   I C    1 
ATOM   5886 O  O    . GLU   B 1 186 ? -15.742 -39.521 -42.805 1.00 30.56  ?  188 GLU   I O    1 
ATOM   5887 C  CB   . GLU   B 1 186 ? -12.822 -40.430 -43.943 1.00 42.18  ?  188 GLU   I CB   1 
ATOM   5888 C  CG   . GLU   B 1 186 ? -11.817 -41.542 -43.634 1.00 43.87  ?  188 GLU   I CG   1 
ATOM   5889 C  CD   . GLU   B 1 186 ? -10.373 -41.059 -43.540 1.00 45.72  ?  188 GLU   I CD   1 
ATOM   5890 O  OE1  . GLU   B 1 186 ? -10.139 -39.842 -43.392 1.00 41.77  ?  188 GLU   I OE1  1 
ATOM   5891 O  OE2  . GLU   B 1 186 ? -9.459  -41.911 -43.598 1.00 48.33  ?  188 GLU   I OE2  1 
ATOM   5892 N  N    . GLY   B 1 187 ? -15.601 -39.108 -45.043 1.00 30.32  ?  189 GLY   I N    1 
ATOM   5893 C  CA   . GLY   B 1 187 ? -16.551 -37.986 -45.087 1.00 31.29  ?  189 GLY   I CA   1 
ATOM   5894 C  C    . GLY   B 1 187 ? -17.961 -38.392 -44.748 1.00 32.27  ?  189 GLY   I C    1 
ATOM   5895 O  O    . GLY   B 1 187 ? -18.630 -37.816 -43.842 1.00 31.32  ?  189 GLY   I O    1 
ATOM   5896 N  N    . LYS   B 1 188 ? -18.404 -39.434 -45.435 1.00 35.77  ?  190 LYS   I N    1 
ATOM   5897 C  CA   . LYS   B 1 188 ? -19.667 -40.071 -45.117 1.00 38.20  ?  190 LYS   I CA   1 
ATOM   5898 C  C    . LYS   B 1 188 ? -19.730 -40.504 -43.639 1.00 34.34  ?  190 LYS   I C    1 
ATOM   5899 O  O    . LYS   B 1 188 ? -20.743 -40.281 -42.976 1.00 35.31  ?  190 LYS   I O    1 
ATOM   5900 C  CB   . LYS   B 1 188 ? -19.924 -41.267 -46.039 1.00 44.38  ?  190 LYS   I CB   1 
ATOM   5901 C  CG   . LYS   B 1 188 ? -20.324 -40.887 -47.462 1.00 51.54  ?  190 LYS   I CG   1 
ATOM   5902 C  CD   . LYS   B 1 188 ? -21.494 -41.733 -47.970 1.00 58.32  ?  190 LYS   I CD   1 
ATOM   5903 C  CE   . LYS   B 1 188 ? -21.191 -43.239 -47.992 1.00 64.23  ?  190 LYS   I CE   1 
ATOM   5904 N  NZ   . LYS   B 1 188 ? -20.003 -43.613 -48.825 1.00 66.04  ?  190 LYS   I NZ   1 
ATOM   5905 N  N    . ALA   B 1 189 ? -18.663 -41.095 -43.131 1.00 31.30  ?  191 ALA   I N    1 
ATOM   5906 C  CA   . ALA   B 1 189 ? -18.642 -41.544 -41.718 1.00 33.00  ?  191 ALA   I CA   1 
ATOM   5907 C  C    . ALA   B 1 189 ? -18.746 -40.359 -40.744 1.00 31.31  ?  191 ALA   I C    1 
ATOM   5908 O  O    . ALA   B 1 189 ? -19.494 -40.406 -39.741 1.00 27.73  ?  191 ALA   I O    1 
ATOM   5909 C  CB   . ALA   B 1 189 ? -17.372 -42.336 -41.438 1.00 33.11  ?  191 ALA   I CB   1 
ATOM   5910 N  N    . SER   B 1 190 ? -17.992 -39.298 -41.041 1.00 29.66  ?  192 SER   I N    1 
ATOM   5911 C  CA   . SER   B 1 190 ? -18.019 -38.120 -40.180 1.00 30.68  ?  192 SER   I CA   1 
ATOM   5912 C  C    . SER   B 1 190 ? -19.431 -37.553 -40.151 1.00 25.75  ?  192 SER   I C    1 
ATOM   5913 O  O    . SER   B 1 190 ? -19.952 -37.259 -39.099 1.00 23.68  ?  192 SER   I O    1 
ATOM   5914 C  CB   . SER   B 1 190 ? -17.005 -37.045 -40.609 1.00 31.84  ?  192 SER   I CB   1 
ATOM   5915 O  OG   . SER   B 1 190 ? -17.058 -35.938 -39.721 1.00 35.51  ?  192 SER   I OG   1 
ATOM   5916 N  N    . SER   B 1 191 ? -20.058 -37.444 -41.308 1.00 29.05  ?  193 SER   I N    1 
ATOM   5917 C  CA   . SER   B 1 191 ? -21.416 -36.878 -41.385 1.00 29.65  ?  193 SER   I CA   1 
ATOM   5918 C  C    . SER   B 1 191 ? -22.377 -37.770 -40.603 1.00 30.12  ?  193 SER   I C    1 
ATOM   5919 O  O    . SER   B 1 191 ? -23.159 -37.277 -39.797 1.00 28.55  ?  193 SER   I O    1 
ATOM   5920 C  CB   . SER   B 1 191 ? -21.840 -36.718 -42.826 1.00 28.77  ?  193 SER   I CB   1 
ATOM   5921 O  OG   . SER   B 1 191 ? -23.175 -36.289 -42.907 1.00 31.02  ?  193 SER   I OG   1 
ATOM   5922 N  N    . ALA   B 1 192 ? -22.259 -39.080 -40.826 1.00 28.04  ?  194 ALA   I N    1 
ATOM   5923 C  CA   . ALA   B 1 192 ? -22.952 -40.080 -40.033 1.00 28.71  ?  194 ALA   I CA   1 
ATOM   5924 C  C    . ALA   B 1 192 ? -22.662 -40.016 -38.538 1.00 30.35  ?  194 ALA   I C    1 
ATOM   5925 O  O    . ALA   B 1 192 ? -23.607 -40.106 -37.777 1.00 31.73  ?  194 ALA   I O    1 
ATOM   5926 C  CB   . ALA   B 1 192 ? -22.670 -41.479 -40.566 1.00 27.16  ?  194 ALA   I CB   1 
ATOM   5927 N  N    . LYS   B 1 193 ? -21.399 -39.838 -38.111 1.00 31.43  ?  195 LYS   I N    1 
ATOM   5928 C  CA   . LYS   B 1 193 ? -21.062 -39.733 -36.644 1.00 31.83  ?  195 LYS   I CA   1 
ATOM   5929 C  C    . LYS   B 1 193 ? -21.695 -38.520 -35.940 1.00 30.95  ?  195 LYS   I C    1 
ATOM   5930 O  O    . LYS   B 1 193 ? -22.144 -38.641 -34.814 1.00 29.38  ?  195 LYS   I O    1 
ATOM   5931 C  CB   . LYS   B 1 193 ? -19.530 -39.638 -36.398 1.00 36.33  ?  195 LYS   I CB   1 
ATOM   5932 C  CG   . LYS   B 1 193 ? -18.814 -40.881 -35.881 1.00 37.84  ?  195 LYS   I CG   1 
ATOM   5933 C  CD   . LYS   B 1 193 ? -17.395 -40.545 -35.413 1.00 35.26  ?  195 LYS   I CD   1 
ATOM   5934 C  CE   . LYS   B 1 193 ? -16.419 -41.674 -35.716 1.00 33.26  ?  195 LYS   I CE   1 
ATOM   5935 N  N    . GLN   B 1 194 ? -21.647 -37.346 -36.572 1.00 30.03  ?  196 GLN   I N    1 
ATOM   5936 C  CA   . GLN   B 1 194 ? -22.260 -36.121 -36.024 1.00 29.36  ?  196 GLN   I CA   1 
ATOM   5937 C  C    . GLN   B 1 194 ? -23.796 -36.268 -35.965 1.00 29.13  ?  196 GLN   I C    1 
ATOM   5938 O  O    . GLN   B 1 194 ? -24.478 -35.913 -34.986 1.00 26.10  ?  196 GLN   I O    1 
ATOM   5939 C  CB   . GLN   B 1 194 ? -21.963 -34.916 -36.917 1.00 29.98  ?  196 GLN   I CB   1 
ATOM   5940 C  CG   . GLN   B 1 194 ? -20.540 -34.452 -37.012 1.00 29.53  ?  196 GLN   I CG   1 
ATOM   5941 C  CD   . GLN   B 1 194 ? -20.336 -33.483 -38.162 1.00 30.75  ?  196 GLN   I CD   1 
ATOM   5942 O  OE1  . GLN   B 1 194 ? -20.847 -32.349 -38.128 1.00 24.68  ?  196 GLN   I OE1  1 
ATOM   5943 N  NE2  . GLN   B 1 194 ? -19.583 -33.928 -39.207 1.00 28.28  ?  196 GLN   I NE2  1 
ATOM   5944 N  N    . ARG   B 1 195 ? -24.339 -36.771 -37.054 1.00 31.06  ?  197 ARG   I N    1 
ATOM   5945 C  CA   . ARG   B 1 195 ? -25.764 -37.061 -37.117 1.00 32.42  ?  197 ARG   I CA   1 
ATOM   5946 C  C    . ARG   B 1 195 ? -26.173 -38.049 -36.005 1.00 31.67  ?  197 ARG   I C    1 
ATOM   5947 O  O    . ARG   B 1 195 ? -27.206 -37.838 -35.349 1.00 35.64  ?  197 ARG   I O    1 
ATOM   5948 C  CB   . ARG   B 1 195 ? -26.163 -37.531 -38.535 1.00 31.97  ?  197 ARG   I CB   1 
ATOM   5949 N  N    . LEU   B 1 196 ? -25.349 -39.064 -35.751 1.00 32.83  ?  198 LEU   I N    1 
ATOM   5950 C  CA   . LEU   B 1 196 ? -25.653 -40.097 -34.732 1.00 33.27  ?  198 LEU   I CA   1 
ATOM   5951 C  C    . LEU   B 1 196 ? -25.459 -39.567 -33.314 1.00 30.11  ?  198 LEU   I C    1 
ATOM   5952 O  O    . LEU   B 1 196 ? -26.221 -39.878 -32.434 1.00 30.14  ?  198 LEU   I O    1 
ATOM   5953 C  CB   . LEU   B 1 196 ? -24.834 -41.379 -34.955 1.00 34.82  ?  198 LEU   I CB   1 
ATOM   5954 C  CG   . LEU   B 1 196 ? -24.853 -42.475 -33.873 1.00 37.83  ?  198 LEU   I CG   1 
ATOM   5955 C  CD1  . LEU   B 1 196 ? -26.233 -42.874 -33.379 1.00 38.93  ?  198 LEU   I CD1  1 
ATOM   5956 C  CD2  . LEU   B 1 196 ? -24.132 -43.716 -34.387 1.00 39.24  ?  198 LEU   I CD2  1 
ATOM   5957 N  N    . LYS   B 1 197 ? -24.489 -38.711 -33.100 1.00 30.47  ?  199 LYS   I N    1 
ATOM   5958 C  CA   . LYS   B 1 197 ? -24.268 -38.174 -31.762 1.00 33.26  ?  199 LYS   I CA   1 
ATOM   5959 C  C    . LYS   B 1 197 ? -25.457 -37.358 -31.322 1.00 31.03  ?  199 LYS   I C    1 
ATOM   5960 O  O    . LYS   B 1 197 ? -25.877 -37.474 -30.184 1.00 29.27  ?  199 LYS   I O    1 
ATOM   5961 C  CB   . LYS   B 1 197 ? -23.000 -37.323 -31.699 1.00 35.12  ?  199 LYS   I CB   1 
ATOM   5962 C  CG   . LYS   B 1 197 ? -21.749 -38.178 -31.698 1.00 38.15  ?  199 LYS   I CG   1 
ATOM   5963 C  CD   . LYS   B 1 197 ? -20.531 -37.281 -31.775 1.00 41.21  ?  199 LYS   I CD   1 
ATOM   5964 C  CE   . LYS   B 1 197 ? -19.262 -38.054 -32.053 1.00 42.89  ?  199 LYS   I CE   1 
ATOM   5965 N  NZ   . LYS   B 1 197 ? -18.132 -37.105 -32.278 1.00 43.35  ?  199 LYS   I NZ   1 
ATOM   5966 N  N    . CYS   B 1 198 ? -25.985 -36.533 -32.219 1.00 26.85  ?  200 CYS   I N    1 
ATOM   5967 C  CA   . CYS   B 1 198 ? -27.135 -35.719 -31.882 1.00 28.05  ?  200 CYS   I CA   1 
ATOM   5968 C  C    . CYS   B 1 198 ? -28.404 -36.543 -31.779 1.00 24.87  ?  200 CYS   I C    1 
ATOM   5969 O  O    . CYS   B 1 198 ? -29.199 -36.284 -30.915 1.00 26.51  ?  200 CYS   I O    1 
ATOM   5970 C  CB   . CYS   B 1 198 ? -27.296 -34.522 -32.836 1.00 26.60  ?  200 CYS   I CB   1 
ATOM   5971 S  SG   . CYS   B 1 198 ? -25.861 -33.396 -32.687 1.00 26.22  ?  200 CYS   I SG   1 
ATOM   5972 N  N    . ALA   B 1 199 ? -28.613 -37.529 -32.629 1.00 26.31  ?  201 ALA   I N    1 
ATOM   5973 C  CA   . ALA   B 1 199 ? -29.819 -38.337 -32.474 1.00 27.18  ?  201 ALA   I CA   1 
ATOM   5974 C  C    . ALA   B 1 199 ? -29.770 -39.074 -31.125 1.00 27.91  ?  201 ALA   I C    1 
ATOM   5975 O  O    . ALA   B 1 199 ? -30.726 -39.037 -30.381 1.00 28.14  ?  201 ALA   I O    1 
ATOM   5976 C  CB   . ALA   B 1 199 ? -29.998 -39.303 -33.614 1.00 26.96  ?  201 ALA   I CB   1 
ATOM   5977 N  N    . SER   B 1 200 ? -28.648 -39.711 -30.818 1.00 28.36  ?  202 SER   I N    1 
ATOM   5978 C  CA   . SER   B 1 200 ? -28.471 -40.420 -29.530 1.00 30.40  ?  202 SER   I CA   1 
ATOM   5979 C  C    . SER   B 1 200 ? -28.736 -39.612 -28.244 1.00 29.70  ?  202 SER   I C    1 
ATOM   5980 O  O    . SER   B 1 200 ? -29.261 -40.155 -27.296 1.00 27.27  ?  202 SER   I O    1 
ATOM   5981 C  CB   . SER   B 1 200 ? -27.056 -40.955 -29.458 1.00 29.92  ?  202 SER   I CB   1 
ATOM   5982 O  OG   . SER   B 1 200 ? -26.870 -42.027 -30.340 1.00 29.33  ?  202 SER   I OG   1 
ATOM   5983 N  N    . LEU   B 1 201 ? -28.330 -38.342 -28.218 1.00 28.55  ?  203 LEU   I N    1 
ATOM   5984 C  CA   . LEU   B 1 201 ? -28.650 -37.429 -27.118 1.00 33.06  ?  203 LEU   I CA   1 
ATOM   5985 C  C    . LEU   B 1 201 ? -30.172 -37.249 -26.972 1.00 36.37  ?  203 LEU   I C    1 
ATOM   5986 O  O    . LEU   B 1 201 ? -30.682 -37.167 -25.848 1.00 41.83  ?  203 LEU   I O    1 
ATOM   5987 C  CB   . LEU   B 1 201 ? -27.994 -36.057 -27.356 1.00 34.17  ?  203 LEU   I CB   1 
ATOM   5988 C  CG   . LEU   B 1 201 ? -27.924 -34.927 -26.311 1.00 35.30  ?  203 LEU   I CG   1 
ATOM   5989 C  CD1  . LEU   B 1 201 ? -27.382 -33.666 -26.974 1.00 33.28  ?  203 LEU   I CD1  1 
ATOM   5990 C  CD2  . LEU   B 1 201 ? -29.228 -34.566 -25.617 1.00 39.24  ?  203 LEU   I CD2  1 
ATOM   5991 N  N    . GLN   B 1 202 ? -30.903 -37.156 -28.084 1.00 36.62  ?  204 GLN   I N    1 
ATOM   5992 C  CA   . GLN   B 1 202 ? -32.369 -36.993 -28.019 1.00 36.54  ?  204 GLN   I CA   1 
ATOM   5993 C  C    . GLN   B 1 202 ? -33.059 -38.284 -27.613 1.00 39.41  ?  204 GLN   I C    1 
ATOM   5994 O  O    . GLN   B 1 202 ? -33.997 -38.246 -26.818 1.00 45.26  ?  204 GLN   I O    1 
ATOM   5995 C  CB   . GLN   B 1 202 ? -32.958 -36.479 -29.328 1.00 35.95  ?  204 GLN   I CB   1 
ATOM   5996 N  N    . LYS   B 1 203 ? -32.613 -39.426 -28.121 1.00 39.39  ?  205 LYS   I N    1 
ATOM   5997 C  CA   . LYS   B 1 203 ? -33.281 -40.696 -27.785 1.00 41.81  ?  205 LYS   I CA   1 
ATOM   5998 C  C    . LYS   B 1 203 ? -33.041 -41.047 -26.314 1.00 43.84  ?  205 LYS   I C    1 
ATOM   5999 O  O    . LYS   B 1 203 ? -33.988 -41.313 -25.576 1.00 47.12  ?  205 LYS   I O    1 
ATOM   6000 C  CB   . LYS   B 1 203 ? -32.804 -41.849 -28.673 1.00 44.13  ?  205 LYS   I CB   1 
ATOM   6001 C  CG   . LYS   B 1 203 ? -32.910 -41.572 -30.171 1.00 46.93  ?  205 LYS   I CG   1 
ATOM   6002 C  CD   . LYS   B 1 203 ? -33.521 -42.720 -30.980 1.00 51.11  ?  205 LYS   I CD   1 
ATOM   6003 C  CE   . LYS   B 1 203 ? -32.557 -43.856 -31.306 1.00 51.92  ?  205 LYS   I CE   1 
ATOM   6004 N  NZ   . LYS   B 1 203 ? -32.641 -44.971 -30.320 1.00 53.16  ?  205 LYS   I NZ   1 
ATOM   6005 N  N    . PHE   B 1 204 ? -31.775 -40.973 -25.897 1.00 40.77  ?  206 PHE   I N    1 
ATOM   6006 C  CA   . PHE   B 1 204 ? -31.310 -41.489 -24.615 1.00 37.35  ?  206 PHE   I CA   1 
ATOM   6007 C  C    . PHE   B 1 204 ? -30.989 -40.453 -23.544 1.00 36.31  ?  206 PHE   I C    1 
ATOM   6008 O  O    . PHE   B 1 204 ? -30.727 -40.817 -22.412 1.00 43.65  ?  206 PHE   I O    1 
ATOM   6009 C  CB   . PHE   B 1 204 ? -30.051 -42.297 -24.849 1.00 38.75  ?  206 PHE   I CB   1 
ATOM   6010 C  CG   . PHE   B 1 204 ? -30.178 -43.341 -25.914 1.00 36.03  ?  206 PHE   I CG   1 
ATOM   6011 C  CD1  . PHE   B 1 204 ? -30.839 -44.534 -25.645 1.00 37.34  ?  206 PHE   I CD1  1 
ATOM   6012 C  CD2  . PHE   B 1 204 ? -29.600 -43.164 -27.160 1.00 34.60  ?  206 PHE   I CD2  1 
ATOM   6013 C  CE1  . PHE   B 1 204 ? -30.918 -45.532 -26.604 1.00 36.57  ?  206 PHE   I CE1  1 
ATOM   6014 C  CE2  . PHE   B 1 204 ? -29.697 -44.142 -28.129 1.00 38.27  ?  206 PHE   I CE2  1 
ATOM   6015 C  CZ   . PHE   B 1 204 ? -30.357 -45.330 -27.851 1.00 37.99  ?  206 PHE   I CZ   1 
ATOM   6016 N  N    . GLY   B 1 205 ? -30.983 -39.173 -23.872 1.00 32.88  ?  207 GLY   I N    1 
ATOM   6017 C  CA   . GLY   B 1 205 ? -30.752 -38.153 -22.857 1.00 32.52  ?  207 GLY   I CA   1 
ATOM   6018 C  C    . GLY   B 1 205 ? -29.317 -37.989 -22.350 1.00 33.58  ?  207 GLY   I C    1 
ATOM   6019 O  O    . GLY   B 1 205 ? -28.352 -38.651 -22.783 1.00 30.71  ?  207 GLY   I O    1 
ATOM   6020 N  N    . GLU   B 1 206 ? -29.225 -37.132 -21.350 1.00 32.83  ?  208 GLU   I N    1 
ATOM   6021 C  CA   . GLU   B 1 206 ? -27.967 -36.584 -20.895 1.00 32.34  ?  208 GLU   I CA   1 
ATOM   6022 C  C    . GLU   B 1 206 ? -27.198 -37.512 -19.966 1.00 30.45  ?  208 GLU   I C    1 
ATOM   6023 O  O    . GLU   B 1 206 ? -25.963 -37.517 -20.006 1.00 26.68  ?  208 GLU   I O    1 
ATOM   6024 C  CB   . GLU   B 1 206 ? -28.198 -35.254 -20.215 1.00 32.75  ?  208 GLU   I CB   1 
ATOM   6025 C  CG   . GLU   B 1 206 ? -27.190 -34.237 -20.625 1.00 36.06  ?  208 GLU   I CG   1 
ATOM   6026 C  CD   . GLU   B 1 206 ? -27.586 -32.850 -20.196 1.00 39.42  ?  208 GLU   I CD   1 
ATOM   6027 O  OE1  . GLU   B 1 206 ? -27.580 -32.590 -18.965 1.00 43.56  ?  208 GLU   I OE1  1 
ATOM   6028 O  OE2  . GLU   B 1 206 ? -27.892 -32.033 -21.079 1.00 43.13  ?  208 GLU   I OE2  1 
ATOM   6029 N  N    . ARG   B 1 207 ? -27.890 -38.317 -19.166 1.00 29.52  ?  209 ARG   I N    1 
ATOM   6030 C  CA   . ARG   B 1 207 ? -27.166 -39.304 -18.328 1.00 30.13  ?  209 ARG   I CA   1 
ATOM   6031 C  C    . ARG   B 1 207 ? -26.262 -40.209 -19.146 1.00 27.59  ?  209 ARG   I C    1 
ATOM   6032 O  O    . ARG   B 1 207 ? -25.068 -40.342 -18.845 1.00 27.76  ?  209 ARG   I O    1 
ATOM   6033 C  CB   . ARG   B 1 207 ? -28.107 -40.166 -17.505 1.00 32.70  ?  209 ARG   I CB   1 
ATOM   6034 C  CG   . ARG   B 1 207 ? -27.396 -40.873 -16.336 1.00 33.31  ?  209 ARG   I CG   1 
ATOM   6035 C  CD   . ARG   B 1 207 ? -28.410 -41.242 -15.277 1.00 34.54  ?  209 ARG   I CD   1 
ATOM   6036 N  NE   . ARG   B 1 207 ? -27.949 -42.132 -14.209 1.00 33.46  ?  209 ARG   I NE   1 
ATOM   6037 C  CZ   . ARG   B 1 207 ? -27.868 -43.458 -14.307 1.00 33.22  ?  209 ARG   I CZ   1 
ATOM   6038 N  NH1  . ARG   B 1 207 ? -28.152 -44.102 -15.441 1.00 35.23  ?  209 ARG   I NH1  1 
ATOM   6039 N  NH2  . ARG   B 1 207 ? -27.500 -44.167 -13.250 1.00 31.08  ?  209 ARG   I NH2  1 
ATOM   6040 N  N    . ALA   B 1 208 ? -26.844 -40.818 -20.182 1.00 27.77  ?  210 ALA   I N    1 
ATOM   6041 C  CA   . ALA   B 1 208 ? -26.148 -41.749 -21.086 1.00 25.81  ?  210 ALA   I CA   1 
ATOM   6042 C  C    . ALA   B 1 208 ? -25.002 -41.056 -21.794 1.00 23.93  ?  210 ALA   I C    1 
ATOM   6043 O  O    . ALA   B 1 208 ? -23.901 -41.612 -21.949 1.00 21.29  ?  210 ALA   I O    1 
ATOM   6044 C  CB   . ALA   B 1 208 ? -27.101 -42.313 -22.113 1.00 25.93  ?  210 ALA   I CB   1 
ATOM   6045 N  N    . PHE   B 1 209 ? -25.262 -39.842 -22.249 1.00 22.57  ?  211 PHE   I N    1 
ATOM   6046 C  CA   . PHE   B 1 209 ? -24.169 -39.039 -22.808 1.00 21.75  ?  211 PHE   I CA   1 
ATOM   6047 C  C    . PHE   B 1 209 ? -23.032 -38.865 -21.837 1.00 18.25  ?  211 PHE   I C    1 
ATOM   6048 O  O    . PHE   B 1 209 ? -21.863 -39.076 -22.163 1.00 18.37  ?  211 PHE   I O    1 
ATOM   6049 C  CB   . PHE   B 1 209 ? -24.625 -37.645 -23.209 1.00 23.62  ?  211 PHE   I CB   1 
ATOM   6050 C  CG   . PHE   B 1 209 ? -23.494 -36.805 -23.691 1.00 23.68  ?  211 PHE   I CG   1 
ATOM   6051 C  CD1  . PHE   B 1 209 ? -22.730 -36.062 -22.810 1.00 24.67  ?  211 PHE   I CD1  1 
ATOM   6052 C  CD2  . PHE   B 1 209 ? -23.146 -36.831 -24.993 1.00 25.03  ?  211 PHE   I CD2  1 
ATOM   6053 C  CE1  . PHE   B 1 209 ? -21.655 -35.321 -23.256 1.00 24.56  ?  211 PHE   I CE1  1 
ATOM   6054 C  CE2  . PHE   B 1 209 ? -22.078 -36.072 -25.467 1.00 27.88  ?  211 PHE   I CE2  1 
ATOM   6055 C  CZ   . PHE   B 1 209 ? -21.332 -35.332 -24.593 1.00 27.09  ?  211 PHE   I CZ   1 
ATOM   6056 N  N    . LYS   B 1 210 ? -23.356 -38.447 -20.635 1.00 20.01  ?  212 LYS   I N    1 
ATOM   6057 C  CA   . LYS   B 1 210 ? -22.324 -38.279 -19.613 1.00 19.52  ?  212 LYS   I CA   1 
ATOM   6058 C  C    . LYS   B 1 210 ? -21.571 -39.587 -19.269 1.00 18.10  ?  212 LYS   I C    1 
ATOM   6059 O  O    . LYS   B 1 210 ? -20.318 -39.626 -19.096 1.00 17.07  ?  212 LYS   I O    1 
ATOM   6060 C  CB   . LYS   B 1 210 ? -22.940 -37.628 -18.401 1.00 22.24  ?  212 LYS   I CB   1 
ATOM   6061 C  CG   . LYS   B 1 210 ? -23.164 -36.151 -18.664 1.00 25.06  ?  212 LYS   I CG   1 
ATOM   6062 C  CD   . LYS   B 1 210 ? -24.239 -35.548 -17.792 1.00 26.39  ?  212 LYS   I CD   1 
ATOM   6063 C  CE   . LYS   B 1 210 ? -24.074 -34.022 -17.796 1.00 29.16  ?  212 LYS   I CE   1 
ATOM   6064 N  NZ   . LYS   B 1 210 ? -25.349 -33.268 -17.868 1.00 32.50  ?  212 LYS   I NZ   1 
ATOM   6065 N  N    . ALA   B 1 211 ? -22.295 -40.674 -19.246 1.00 16.14  ?  213 ALA   I N    1 
ATOM   6066 C  CA   . ALA   B 1 211 ? -21.618 -41.968 -18.991 1.00 17.14  ?  213 ALA   I CA   1 
ATOM   6067 C  C    . ALA   B 1 211 ? -20.572 -42.229 -20.027 1.00 18.48  ?  213 ALA   I C    1 
ATOM   6068 O  O    . ALA   B 1 211 ? -19.413 -42.494 -19.691 1.00 18.47  ?  213 ALA   I O    1 
ATOM   6069 C  CB   . ALA   B 1 211 ? -22.618 -43.080 -18.928 1.00 17.48  ?  213 ALA   I CB   1 
ATOM   6070 N  N    . TRP   B 1 212 ? -20.980 -42.041 -21.291 1.00 19.95  ?  214 TRP   I N    1 
ATOM   6071 C  CA   . TRP   B 1 212 ? -20.154 -42.271 -22.431 1.00 19.25  ?  214 TRP   I CA   1 
ATOM   6072 C  C    . TRP   B 1 212 ? -18.931 -41.383 -22.368 1.00 19.48  ?  214 TRP   I C    1 
ATOM   6073 O  O    . TRP   B 1 212 ? -17.805 -41.861 -22.588 1.00 14.63  ?  214 TRP   I O    1 
ATOM   6074 C  CB   . TRP   B 1 212 ? -20.924 -41.983 -23.735 1.00 22.43  ?  214 TRP   I CB   1 
ATOM   6075 C  CG   . TRP   B 1 212 ? -20.628 -42.922 -24.798 1.00 27.81  ?  214 TRP   I CG   1 
ATOM   6076 C  CD1  . TRP   B 1 212 ? -21.349 -44.038 -25.132 1.00 29.19  ?  214 TRP   I CD1  1 
ATOM   6077 C  CD2  . TRP   B 1 212 ? -19.508 -42.888 -25.680 1.00 34.12  ?  214 TRP   I CD2  1 
ATOM   6078 N  NE1  . TRP   B 1 212 ? -20.746 -44.691 -26.162 1.00 34.91  ?  214 TRP   I NE1  1 
ATOM   6079 C  CE2  . TRP   B 1 212 ? -19.616 -44.004 -26.527 1.00 35.13  ?  214 TRP   I CE2  1 
ATOM   6080 C  CE3  . TRP   B 1 212 ? -18.422 -42.019 -25.836 1.00 35.99  ?  214 TRP   I CE3  1 
ATOM   6081 C  CZ2  . TRP   B 1 212 ? -18.669 -44.281 -27.516 1.00 39.79  ?  214 TRP   I CZ2  1 
ATOM   6082 C  CZ3  . TRP   B 1 212 ? -17.492 -42.292 -26.809 1.00 39.16  ?  214 TRP   I CZ3  1 
ATOM   6083 C  CH2  . TRP   B 1 212 ? -17.613 -43.403 -27.640 1.00 40.75  ?  214 TRP   I CH2  1 
ATOM   6084 N  N    . ALA   B 1 213 ? -19.155 -40.070 -22.127 1.00 18.96  ?  215 ALA   I N    1 
ATOM   6085 C  CA   . ALA   B 1 213 ? -18.032 -39.123 -22.075 1.00 18.31  ?  215 ALA   I CA   1 
ATOM   6086 C  C    . ALA   B 1 213 ? -17.024 -39.412 -20.918 1.00 18.36  ?  215 ALA   I C    1 
ATOM   6087 O  O    . ALA   B 1 213 ? -15.826 -39.460 -21.155 1.00 19.49  ?  215 ALA   I O    1 
ATOM   6088 C  CB   . ALA   B 1 213 ? -18.546 -37.706 -22.022 1.00 18.43  ?  215 ALA   I CB   1 
ATOM   6089 N  N    . VAL   B 1 214 ? -17.518 -39.658 -19.713 1.00 19.79  ?  216 VAL   I N    1 
ATOM   6090 C  CA   . VAL   B 1 214 ? -16.730 -40.159 -18.572 1.00 20.08  ?  216 VAL   I CA   1 
ATOM   6091 C  C    . VAL   B 1 214 ? -15.865 -41.340 -18.991 1.00 19.08  ?  216 VAL   I C    1 
ATOM   6092 O  O    . VAL   B 1 214 ? -14.646 -41.297 -18.805 1.00 18.67  ?  216 VAL   I O    1 
ATOM   6093 C  CB   . VAL   B 1 214 ? -17.621 -40.549 -17.351 1.00 21.53  ?  216 VAL   I CB   1 
ATOM   6094 C  CG1  . VAL   B 1 214 ? -16.827 -41.307 -16.278 1.00 22.43  ?  216 VAL   I CG1  1 
ATOM   6095 C  CG2  . VAL   B 1 214 ? -18.236 -39.329 -16.713 1.00 23.37  ?  216 VAL   I CG2  1 
ATOM   6096 N  N    . ALA   B 1 215 ? -16.466 -42.350 -19.627 1.00 18.57  ?  217 ALA   I N    1 
ATOM   6097 C  CA   . ALA   B 1 215 ? -15.688 -43.507 -20.082 1.00 19.03  ?  217 ALA   I CA   1 
ATOM   6098 C  C    . ALA   B 1 215 ? -14.619 -43.132 -21.033 1.00 20.74  ?  217 ALA   I C    1 
ATOM   6099 O  O    . ALA   B 1 215 ? -13.478 -43.589 -20.917 1.00 18.21  ?  217 ALA   I O    1 
ATOM   6100 C  CB   . ALA   B 1 215 ? -16.546 -44.544 -20.749 1.00 19.05  ?  217 ALA   I CB   1 
ATOM   6101 N  N    . ARG   B 1 216 ? -14.990 -42.351 -22.042 1.00 21.19  ?  218 ARG   I N    1 
ATOM   6102 C  CA   . ARG   B 1 216 ? -14.030 -42.102 -23.077 1.00 22.90  ?  218 ARG   I CA   1 
ATOM   6103 C  C    . ARG   B 1 216 ? -12.923 -41.194 -22.599 1.00 21.38  ?  218 ARG   I C    1 
ATOM   6104 O  O    . ARG   B 1 216 ? -11.765 -41.427 -22.944 1.00 22.39  ?  218 ARG   I O    1 
ATOM   6105 C  CB   . ARG   B 1 216 ? -14.691 -41.490 -24.322 1.00 25.72  ?  218 ARG   I CB   1 
ATOM   6106 C  CG   . ARG   B 1 216 ? -13.773 -41.421 -25.531 1.00 27.41  ?  218 ARG   I CG   1 
ATOM   6107 C  CD   . ARG   B 1 216 ? -13.002 -42.711 -25.765 1.00 29.93  ?  218 ARG   I CD   1 
ATOM   6108 N  NE   . ARG   B 1 216 ? -13.154 -43.106 -27.134 1.00 35.45  ?  218 ARG   I NE   1 
ATOM   6109 C  CZ   . ARG   B 1 216 ? -13.132 -44.362 -27.587 1.00 43.45  ?  218 ARG   I CZ   1 
ATOM   6110 N  NH1  . ARG   B 1 216 ? -12.850 -45.410 -26.777 1.00 41.97  ?  218 ARG   I NH1  1 
ATOM   6111 N  NH2  . ARG   B 1 216 ? -13.361 -44.575 -28.896 1.00 43.92  ?  218 ARG   I NH2  1 
ATOM   6112 N  N    . LEU   B 1 217 ? -13.283 -40.150 -21.849 1.00 21.32  ?  219 LEU   I N    1 
ATOM   6113 C  CA   . LEU   B 1 217 ? -12.297 -39.190 -21.377 1.00 21.76  ?  219 LEU   I CA   1 
ATOM   6114 C  C    . LEU   B 1 217 ? -11.361 -39.799 -20.330 1.00 22.16  ?  219 LEU   I C    1 
ATOM   6115 O  O    . LEU   B 1 217 ? -10.179 -39.463 -20.291 1.00 21.90  ?  219 LEU   I O    1 
ATOM   6116 C  CB   . LEU   B 1 217 ? -12.956 -37.923 -20.848 1.00 21.98  ?  219 LEU   I CB   1 
ATOM   6117 C  CG   . LEU   B 1 217 ? -13.523 -36.917 -21.877 1.00 22.98  ?  219 LEU   I CG   1 
ATOM   6118 C  CD1  . LEU   B 1 217 ? -13.276 -35.506 -21.376 1.00 23.98  ?  219 LEU   I CD1  1 
ATOM   6119 C  CD2  . LEU   B 1 217 ? -12.989 -37.004 -23.295 1.00 23.88  ?  219 LEU   I CD2  1 
ATOM   6120 N  N    . SER   B 1 218 ? -11.871 -40.713 -19.512 1.00 21.94  ?  220 SER   I N    1 
ATOM   6121 C  CA   . SER   B 1 218 ? -11.016 -41.411 -18.560 1.00 23.06  ?  220 SER   I CA   1 
ATOM   6122 C  C    . SER   B 1 218 ? -10.008 -42.329 -19.231 1.00 22.60  ?  220 SER   I C    1 
ATOM   6123 O  O    . SER   B 1 218 ? -8.920  -42.437 -18.738 1.00 21.98  ?  220 SER   I O    1 
ATOM   6124 C  CB   . SER   B 1 218 ? -11.834 -42.169 -17.539 1.00 23.37  ?  220 SER   I CB   1 
ATOM   6125 O  OG   . SER   B 1 218 ? -12.663 -41.281 -16.851 1.00 22.98  ?  220 SER   I OG   1 
ATOM   6126 N  N    . GLN   B 1 219 ? -10.350 -42.957 -20.372 1.00 24.28  ?  221 GLN   I N    1 
ATOM   6127 C  CA   . GLN   B 1 219 ? -9.343  -43.718 -21.162 1.00 22.40  ?  221 GLN   I CA   1 
ATOM   6128 C  C    . GLN   B 1 219 ? -8.270  -42.836 -21.728 1.00 22.63  ?  221 GLN   I C    1 
ATOM   6129 O  O    . GLN   B 1 219 ? -7.121  -43.225 -21.822 1.00 20.05  ?  221 GLN   I O    1 
ATOM   6130 C  CB   . GLN   B 1 219 ? -9.976  -44.423 -22.349 1.00 22.60  ?  221 GLN   I CB   1 
ATOM   6131 C  CG   . GLN   B 1 219 ? -10.798 -45.651 -21.991 1.00 21.85  ?  221 GLN   I CG   1 
ATOM   6132 C  CD   . GLN   B 1 219 ? -11.478 -46.208 -23.218 1.00 21.16  ?  221 GLN   I CD   1 
ATOM   6133 O  OE1  . GLN   B 1 219 ? -11.965 -45.446 -24.037 1.00 20.33  ?  221 GLN   I OE1  1 
ATOM   6134 N  NE2  . GLN   B 1 219 ? -11.543 -47.538 -23.337 1.00 19.33  ?  221 GLN   I NE2  1 
ATOM   6135 N  N    . ARG   B 1 220 ? -8.690  -41.660 -22.178 1.00 25.19  ?  222 ARG   I N    1 
ATOM   6136 C  CA   . ARG   B 1 220 ? -7.829  -40.706 -22.844 1.00 25.59  ?  222 ARG   I CA   1 
ATOM   6137 C  C    . ARG   B 1 220 ? -6.938  -39.971 -21.899 1.00 22.54  ?  222 ARG   I C    1 
ATOM   6138 O  O    . ARG   B 1 220 ? -5.808  -39.664 -22.256 1.00 23.33  ?  222 ARG   I O    1 
ATOM   6139 C  CB   . ARG   B 1 220 ? -8.650  -39.640 -23.639 1.00 29.97  ?  222 ARG   I CB   1 
ATOM   6140 C  CG   . ARG   B 1 220 ? -8.855  -39.976 -25.104 1.00 35.88  ?  222 ARG   I CG   1 
ATOM   6141 C  CD   . ARG   B 1 220 ? -8.924  -38.727 -25.994 1.00 39.80  ?  222 ARG   I CD   1 
ATOM   6142 N  NE   . ARG   B 1 220 ? -9.530  -39.131 -27.259 1.00 43.24  ?  222 ARG   I NE   1 
ATOM   6143 C  CZ   . ARG   B 1 220 ? -10.807 -38.954 -27.591 1.00 47.63  ?  222 ARG   I CZ   1 
ATOM   6144 N  NH1  . ARG   B 1 220 ? -11.655 -38.287 -26.803 1.00 48.88  ?  222 ARG   I NH1  1 
ATOM   6145 N  NH2  . ARG   B 1 220 ? -11.235 -39.411 -28.762 1.00 49.69  ?  222 ARG   I NH2  1 
ATOM   6146 N  N    . PHE   B 1 221 ? -7.484  -39.610 -20.749 1.00 21.56  ?  223 PHE   I N    1 
ATOM   6147 C  CA   . PHE   B 1 221 ? -6.804  -38.819 -19.728 1.00 22.11  ?  223 PHE   I CA   1 
ATOM   6148 C  C    . PHE   B 1 221 ? -6.681  -39.555 -18.378 1.00 21.89  ?  223 PHE   I C    1 
ATOM   6149 O  O    . PHE   B 1 221 ? -7.060  -39.029 -17.343 1.00 21.46  ?  223 PHE   I O    1 
ATOM   6150 C  CB   . PHE   B 1 221 ? -7.555  -37.498 -19.543 1.00 21.64  ?  223 PHE   I CB   1 
ATOM   6151 C  CG   . PHE   B 1 221 ? -7.750  -36.708 -20.815 1.00 21.42  ?  223 PHE   I CG   1 
ATOM   6152 C  CD1  . PHE   B 1 221 ? -6.758  -36.630 -21.789 1.00 20.43  ?  223 PHE   I CD1  1 
ATOM   6153 C  CD2  . PHE   B 1 221 ? -8.906  -35.958 -20.993 1.00 21.42  ?  223 PHE   I CD2  1 
ATOM   6154 C  CE1  . PHE   B 1 221 ? -6.952  -35.896 -22.938 1.00 19.83  ?  223 PHE   I CE1  1 
ATOM   6155 C  CE2  . PHE   B 1 221 ? -9.094  -35.191 -22.145 1.00 20.31  ?  223 PHE   I CE2  1 
ATOM   6156 C  CZ   . PHE   B 1 221 ? -8.117  -35.172 -23.116 1.00 20.33  ?  223 PHE   I CZ   1 
ATOM   6157 N  N    . PRO   B 1 222 ? -6.152  -40.788 -18.385 1.00 22.78  ?  224 PRO   I N    1 
ATOM   6158 C  CA   . PRO   B 1 222 ? -6.030  -41.575 -17.170 1.00 24.83  ?  224 PRO   I CA   1 
ATOM   6159 C  C    . PRO   B 1 222 ? -5.261  -40.928 -15.967 1.00 27.64  ?  224 PRO   I C    1 
ATOM   6160 O  O    . PRO   B 1 222 ? -5.598  -41.213 -14.818 1.00 30.38  ?  224 PRO   I O    1 
ATOM   6161 C  CB   . PRO   B 1 222 ? -5.324  -42.845 -17.673 1.00 24.12  ?  224 PRO   I CB   1 
ATOM   6162 C  CG   . PRO   B 1 222 ? -4.534  -42.391 -18.837 1.00 23.69  ?  224 PRO   I CG   1 
ATOM   6163 C  CD   . PRO   B 1 222 ? -5.512  -41.478 -19.508 1.00 23.36  ?  224 PRO   I CD   1 
ATOM   6164 N  N    . LYS   B 1 223 ? -4.280  -40.062 -16.211 1.00 27.58  ?  225 LYS   I N    1 
ATOM   6165 C  CA   . LYS   B 1 223 ? -3.590  -39.359 -15.116 1.00 28.88  ?  225 LYS   I CA   1 
ATOM   6166 C  C    . LYS   B 1 223 ? -4.404  -38.223 -14.482 1.00 27.33  ?  225 LYS   I C    1 
ATOM   6167 O  O    . LYS   B 1 223 ? -3.998  -37.718 -13.440 1.00 26.61  ?  225 LYS   I O    1 
ATOM   6168 C  CB   . LYS   B 1 223 ? -2.233  -38.810 -15.563 1.00 30.44  ?  225 LYS   I CB   1 
ATOM   6169 C  CG   . LYS   B 1 223 ? -1.368  -39.900 -16.181 1.00 36.07  ?  225 LYS   I CG   1 
ATOM   6170 C  CD   . LYS   B 1 223 ? 0.124   -39.594 -16.276 1.00 36.61  ?  225 LYS   I CD   1 
ATOM   6171 C  CE   . LYS   B 1 223 ? 0.910   -40.883 -16.069 1.00 37.00  ?  225 LYS   I CE   1 
ATOM   6172 N  NZ   . LYS   B 1 223 ? 2.278   -40.835 -16.647 1.00 42.15  ?  225 LYS   I NZ   1 
ATOM   6173 N  N    . ALA   B 1 224 ? -5.488  -37.780 -15.131 1.00 26.27  ?  226 ALA   I N    1 
ATOM   6174 C  CA   . ALA   B 1 224 ? -6.376  -36.758 -14.575 1.00 25.11  ?  226 ALA   I CA   1 
ATOM   6175 C  C    . ALA   B 1 224 ? -7.150  -37.320 -13.409 1.00 25.15  ?  226 ALA   I C    1 
ATOM   6176 O  O    . ALA   B 1 224 ? -7.560  -38.503 -13.423 1.00 23.33  ?  226 ALA   I O    1 
ATOM   6177 C  CB   . ALA   B 1 224 ? -7.351  -36.232 -15.603 1.00 24.89  ?  226 ALA   I CB   1 
ATOM   6178 N  N    . GLU   B 1 225 ? -7.408  -36.449 -12.434 1.00 22.03  ?  227 GLU   I N    1 
ATOM   6179 C  CA   . GLU   B 1 225 ? -8.207  -36.837 -11.287 1.00 24.73  ?  227 GLU   I CA   1 
ATOM   6180 C  C    . GLU   B 1 225 ? -9.696  -36.886 -11.703 1.00 24.35  ?  227 GLU   I C    1 
ATOM   6181 O  O    . GLU   B 1 225 ? -10.146 -36.150 -12.603 1.00 25.75  ?  227 GLU   I O    1 
ATOM   6182 C  CB   . GLU   B 1 225 ? -7.947  -35.896 -10.083 1.00 24.87  ?  227 GLU   I CB   1 
ATOM   6183 N  N    . PHE   B 1 226 ? -10.466 -37.766 -11.073 1.00 23.22  ?  228 PHE   I N    1 
ATOM   6184 C  CA   . PHE   B 1 226 ? -11.924 -37.800 -11.322 1.00 23.25  ?  228 PHE   I CA   1 
ATOM   6185 C  C    . PHE   B 1 226 ? -12.596 -36.392 -11.370 1.00 23.34  ?  228 PHE   I C    1 
ATOM   6186 O  O    . PHE   B 1 226 ? -13.507 -36.147 -12.165 1.00 21.63  ?  228 PHE   I O    1 
ATOM   6187 C  CB   . PHE   B 1 226 ? -12.636 -38.612 -10.279 1.00 22.08  ?  228 PHE   I CB   1 
ATOM   6188 C  CG   . PHE   B 1 226 ? -14.124 -38.681 -10.496 1.00 21.70  ?  228 PHE   I CG   1 
ATOM   6189 C  CD1  . PHE   B 1 226 ? -14.644 -39.406 -11.565 1.00 20.82  ?  228 PHE   I CD1  1 
ATOM   6190 C  CD2  . PHE   B 1 226 ? -15.002 -38.060 -9.621  1.00 21.19  ?  228 PHE   I CD2  1 
ATOM   6191 C  CE1  . PHE   B 1 226 ? -16.020 -39.501 -11.764 1.00 21.61  ?  228 PHE   I CE1  1 
ATOM   6192 C  CE2  . PHE   B 1 226 ? -16.373 -38.117 -9.844  1.00 21.81  ?  228 PHE   I CE2  1 
ATOM   6193 C  CZ   . PHE   B 1 226 ? -16.877 -38.833 -10.918 1.00 21.89  ?  228 PHE   I CZ   1 
ATOM   6194 N  N    . ALA   B 1 227 ? -12.173 -35.525 -10.476 1.00 21.61  ?  229 ALA   I N    1 
ATOM   6195 C  CA   . ALA   B 1 227 ? -12.700 -34.186 -10.392 1.00 23.79  ?  229 ALA   I CA   1 
ATOM   6196 C  C    . ALA   B 1 227 ? -12.498 -33.406 -11.681 1.00 23.72  ?  229 ALA   I C    1 
ATOM   6197 O  O    . ALA   B 1 227 ? -13.375 -32.702 -12.099 1.00 23.79  ?  229 ALA   I O    1 
ATOM   6198 C  CB   . ALA   B 1 227 ? -12.052 -33.451 -9.227  1.00 24.54  ?  229 ALA   I CB   1 
ATOM   6199 N  N    . GLU   B 1 228 ? -11.329 -33.543 -12.300 1.00 27.26  ?  230 GLU   I N    1 
ATOM   6200 C  CA   . GLU   B 1 228 ? -11.045 -32.929 -13.601 1.00 26.37  ?  230 GLU   I CA   1 
ATOM   6201 C  C    . GLU   B 1 228 ? -11.817 -33.582 -14.766 1.00 25.11  ?  230 GLU   I C    1 
ATOM   6202 O  O    . GLU   B 1 228 ? -12.356 -32.902 -15.641 1.00 20.88  ?  230 GLU   I O    1 
ATOM   6203 C  CB   . GLU   B 1 228 ? -9.571  -32.984 -13.895 1.00 26.29  ?  230 GLU   I CB   1 
ATOM   6204 C  CG   . GLU   B 1 228 ? -9.206  -32.136 -15.071 1.00 26.85  ?  230 GLU   I CG   1 
ATOM   6205 C  CD   . GLU   B 1 228 ? -9.302  -30.655 -14.760 1.00 28.07  ?  230 GLU   I CD   1 
ATOM   6206 O  OE1  . GLU   B 1 228 ? -8.978  -30.258 -13.644 1.00 32.29  ?  230 GLU   I OE1  1 
ATOM   6207 O  OE2  . GLU   B 1 228 ? -9.704  -29.884 -15.632 1.00 28.84  ?  230 GLU   I OE2  1 
ATOM   6208 N  N    . VAL   B 1 229 ? -11.870 -34.903 -14.750 1.00 23.89  ?  231 VAL   I N    1 
ATOM   6209 C  CA   . VAL   B 1 229 ? -12.757 -35.636 -15.655 1.00 24.11  ?  231 VAL   I CA   1 
ATOM   6210 C  C    . VAL   B 1 229 ? -14.212 -35.186 -15.580 1.00 22.18  ?  231 VAL   I C    1 
ATOM   6211 O  O    . VAL   B 1 229 ? -14.839 -35.008 -16.643 1.00 22.16  ?  231 VAL   I O    1 
ATOM   6212 C  CB   . VAL   B 1 229 ? -12.676 -37.174 -15.451 1.00 25.92  ?  231 VAL   I CB   1 
ATOM   6213 C  CG1  . VAL   B 1 229 ? -13.686 -37.898 -16.334 1.00 26.73  ?  231 VAL   I CG1  1 
ATOM   6214 C  CG2  . VAL   B 1 229 ? -11.257 -37.673 -15.761 1.00 27.02  ?  231 VAL   I CG2  1 
ATOM   6215 N  N    . SER   B 1 230 ? -14.754 -35.062 -14.371 1.00 21.31  ?  232 SER   I N    1 
ATOM   6216 C  CA   . SER   B 1 230 ? -16.179 -34.748 -14.153 1.00 21.91  ?  232 SER   I CA   1 
ATOM   6217 C  C    . SER   B 1 230 ? -16.471 -33.370 -14.709 1.00 21.41  ?  232 SER   I C    1 
ATOM   6218 O  O    . SER   B 1 230 ? -17.517 -33.134 -15.332 1.00 19.65  ?  232 SER   I O    1 
ATOM   6219 C  CB   . SER   B 1 230 ? -16.546 -34.695 -12.679 1.00 23.69  ?  232 SER   I CB   1 
ATOM   6220 O  OG   . SER   B 1 230 ? -16.479 -35.967 -12.073 1.00 33.26  ?  232 SER   I OG   1 
ATOM   6221 N  N    . LYS   B 1 231 ? -15.554 -32.457 -14.421 1.00 21.46  ?  233 LYS   I N    1 
ATOM   6222 C  CA   . LYS   B 1 231 ? -15.668 -31.101 -14.864 1.00 23.48  ?  233 LYS   I CA   1 
ATOM   6223 C  C    . LYS   B 1 231 ? -15.621 -31.041 -16.393 1.00 23.56  ?  233 LYS   I C    1 
ATOM   6224 O  O    . LYS   B 1 231 ? -16.530 -30.453 -16.982 1.00 25.31  ?  233 LYS   I O    1 
ATOM   6225 C  CB   . LYS   B 1 231 ? -14.630 -30.238 -14.207 1.00 26.15  ?  233 LYS   I CB   1 
ATOM   6226 C  CG   . LYS   B 1 231 ? -15.014 -28.775 -14.144 1.00 28.07  ?  233 LYS   I CG   1 
ATOM   6227 C  CD   . LYS   B 1 231 ? -14.523 -28.026 -15.344 1.00 30.20  ?  233 LYS   I CD   1 
ATOM   6228 C  CE   . LYS   B 1 231 ? -14.625 -26.522 -15.122 1.00 31.42  ?  233 LYS   I CE   1 
ATOM   6229 N  NZ   . LYS   B 1 231 ? -14.438 -25.802 -16.401 1.00 33.87  ?  233 LYS   I NZ   1 
ATOM   6230 N  N    . LEU   B 1 232 ? -14.649 -31.700 -17.029 1.00 21.53  ?  234 LEU   I N    1 
ATOM   6231 C  CA   . LEU   B 1 232 ? -14.641 -31.830 -18.502 1.00 21.40  ?  234 LEU   I CA   1 
ATOM   6232 C  C    . LEU   B 1 232 ? -15.990 -32.335 -19.059 1.00 22.00  ?  234 LEU   I C    1 
ATOM   6233 O  O    . LEU   B 1 232 ? -16.650 -31.642 -19.788 1.00 25.36  ?  234 LEU   I O    1 
ATOM   6234 C  CB   . LEU   B 1 232 ? -13.500 -32.696 -19.002 1.00 20.17  ?  234 LEU   I CB   1 
ATOM   6235 C  CG   . LEU   B 1 232 ? -12.078 -32.180 -18.749 1.00 20.94  ?  234 LEU   I CG   1 
ATOM   6236 C  CD1  . LEU   B 1 232 ? -11.069 -33.261 -18.865 1.00 20.11  ?  234 LEU   I CD1  1 
ATOM   6237 C  CD2  . LEU   B 1 232 ? -11.692 -31.035 -19.643 1.00 23.70  ?  234 LEU   I CD2  1 
ATOM   6238 N  N    . VAL   B 1 233 ? -16.433 -33.492 -18.625 1.00 22.09  ?  235 VAL   I N    1 
ATOM   6239 C  CA   . VAL   B 1 233 ? -17.714 -34.043 -19.044 1.00 23.15  ?  235 VAL   I CA   1 
ATOM   6240 C  C    . VAL   B 1 233 ? -18.850 -33.053 -18.893 1.00 23.28  ?  235 VAL   I C    1 
ATOM   6241 O  O    . VAL   B 1 233 ? -19.702 -32.994 -19.747 1.00 23.93  ?  235 VAL   I O    1 
ATOM   6242 C  CB   . VAL   B 1 233 ? -18.059 -35.325 -18.233 1.00 21.72  ?  235 VAL   I CB   1 
ATOM   6243 C  CG1  . VAL   B 1 233 ? -19.530 -35.730 -18.364 1.00 20.46  ?  235 VAL   I CG1  1 
ATOM   6244 C  CG2  . VAL   B 1 233 ? -17.133 -36.436 -18.648 1.00 22.39  ?  235 VAL   I CG2  1 
ATOM   6245 N  N    . THR   B 1 234 ? -18.892 -32.319 -17.794 1.00 25.79  ?  236 THR   I N    1 
ATOM   6246 C  CA   . THR   B 1 234 ? -19.978 -31.339 -17.575 1.00 27.70  ?  236 THR   I CA   1 
ATOM   6247 C  C    . THR   B 1 234 ? -19.928 -30.200 -18.622 1.00 26.68  ?  236 THR   I C    1 
ATOM   6248 O  O    . THR   B 1 234 ? -20.964 -29.761 -19.106 1.00 23.03  ?  236 THR   I O    1 
ATOM   6249 C  CB   . THR   B 1 234 ? -19.960 -30.774 -16.134 1.00 29.46  ?  236 THR   I CB   1 
ATOM   6250 O  OG1  . THR   B 1 234 ? -20.340 -31.809 -15.222 1.00 28.42  ?  236 THR   I OG1  1 
ATOM   6251 C  CG2  . THR   B 1 234 ? -20.912 -29.569 -15.973 1.00 28.57  ?  236 THR   I CG2  1 
ATOM   6252 N  N    . ASP   B 1 235 ? -18.723 -29.774 -18.983 1.00 26.88  ?  237 ASP   I N    1 
ATOM   6253 C  CA   . ASP   B 1 235 ? -18.530 -28.800 -20.063 1.00 27.41  ?  237 ASP   I CA   1 
ATOM   6254 C  C    . ASP   B 1 235 ? -18.774 -29.418 -21.456 1.00 23.67  ?  237 ASP   I C    1 
ATOM   6255 O  O    . ASP   B 1 235 ? -19.302 -28.763 -22.313 1.00 20.96  ?  237 ASP   I O    1 
ATOM   6256 C  CB   . ASP   B 1 235 ? -17.118 -28.170 -20.003 1.00 30.14  ?  237 ASP   I CB   1 
ATOM   6257 C  CG   . ASP   B 1 235 ? -16.868 -27.315 -18.725 1.00 33.61  ?  237 ASP   I CG   1 
ATOM   6258 O  OD1  . ASP   B 1 235 ? -17.834 -26.970 -17.987 1.00 35.87  ?  237 ASP   I OD1  1 
ATOM   6259 O  OD2  . ASP   B 1 235 ? -15.661 -27.006 -18.446 1.00 38.34  ?  237 ASP   I OD2  1 
ATOM   6260 N  N    . LEU   B 1 236 ? -18.415 -30.682 -21.672 1.00 23.12  ?  238 LEU   I N    1 
ATOM   6261 C  CA   . LEU   B 1 236 ? -18.645 -31.335 -22.973 1.00 23.86  ?  238 LEU   I CA   1 
ATOM   6262 C  C    . LEU   B 1 236 ? -20.157 -31.481 -23.242 1.00 25.41  ?  238 LEU   I C    1 
ATOM   6263 O  O    . LEU   B 1 236 ? -20.650 -31.349 -24.391 1.00 24.00  ?  238 LEU   I O    1 
ATOM   6264 C  CB   . LEU   B 1 236 ? -17.959 -32.731 -23.061 1.00 23.91  ?  238 LEU   I CB   1 
ATOM   6265 C  CG   . LEU   B 1 236 ? -17.207 -33.229 -24.327 1.00 23.62  ?  238 LEU   I CG   1 
ATOM   6266 C  CD1  . LEU   B 1 236 ? -17.325 -34.741 -24.510 1.00 23.51  ?  238 LEU   I CD1  1 
ATOM   6267 C  CD2  . LEU   B 1 236 ? -17.539 -32.540 -25.640 1.00 26.69  ?  238 LEU   I CD2  1 
ATOM   6268 N  N    . THR   B 1 237 ? -20.895 -31.762 -22.187 1.00 24.52  ?  239 THR   I N    1 
ATOM   6269 C  CA   . THR   B 1 237 ? -22.307 -31.983 -22.326 1.00 25.37  ?  239 THR   I CA   1 
ATOM   6270 C  C    . THR   B 1 237 ? -23.027 -30.716 -22.773 1.00 23.35  ?  239 THR   I C    1 
ATOM   6271 O  O    . THR   B 1 237 ? -23.860 -30.786 -23.667 1.00 18.95  ?  239 THR   I O    1 
ATOM   6272 C  CB   . THR   B 1 237 ? -22.895 -32.482 -21.015 1.00 27.38  ?  239 THR   I CB   1 
ATOM   6273 O  OG1  . THR   B 1 237 ? -22.172 -33.665 -20.611 1.00 33.16  ?  239 THR   I OG1  1 
ATOM   6274 C  CG2  . THR   B 1 237 ? -24.325 -32.812 -21.190 1.00 26.54  ?  239 THR   I CG2  1 
ATOM   6275 N  N    . LYS   B 1 238 ? -22.692 -29.575 -22.169 1.00 22.78  ?  240 LYS   I N    1 
ATOM   6276 C  CA   . LYS   B 1 238 ? -23.232 -28.283 -22.655 1.00 22.59  ?  240 LYS   I CA   1 
ATOM   6277 C  C    . LYS   B 1 238 ? -22.811 -28.066 -24.106 1.00 23.81  ?  240 LYS   I C    1 
ATOM   6278 O  O    . LYS   B 1 238 ? -23.660 -27.819 -24.931 1.00 26.55  ?  240 LYS   I O    1 
ATOM   6279 C  CB   . LYS   B 1 238 ? -22.838 -27.094 -21.783 1.00 22.77  ?  240 LYS   I CB   1 
ATOM   6280 C  CG   . LYS   B 1 238 ? -23.340 -25.736 -22.330 1.00 22.47  ?  240 LYS   I CG   1 
ATOM   6281 N  N    . VAL   B 1 239 ? -21.524 -28.241 -24.418 1.00 24.44  ?  241 VAL   I N    1 
ATOM   6282 C  CA   . VAL   B 1 239 ? -20.992 -28.097 -25.772 1.00 25.58  ?  241 VAL   I CA   1 
ATOM   6283 C  C    . VAL   B 1 239 ? -21.760 -28.910 -26.810 1.00 26.46  ?  241 VAL   I C    1 
ATOM   6284 O  O    . VAL   B 1 239 ? -22.251 -28.355 -27.794 1.00 23.06  ?  241 VAL   I O    1 
ATOM   6285 C  CB   . VAL   B 1 239 ? -19.482 -28.471 -25.858 1.00 26.18  ?  241 VAL   I CB   1 
ATOM   6286 C  CG1  . VAL   B 1 239 ? -19.020 -28.586 -27.294 1.00 27.14  ?  241 VAL   I CG1  1 
ATOM   6287 C  CG2  . VAL   B 1 239 ? -18.607 -27.461 -25.111 1.00 28.66  ?  241 VAL   I CG2  1 
ATOM   6288 N  N    . HIS   B 1 240 ? -21.829 -30.225 -26.608 1.00 27.08  ?  242 HIS   I N    1 
ATOM   6289 C  CA   . HIS   B 1 240 ? -22.567 -31.086 -27.511 1.00 27.64  ?  242 HIS   I CA   1 
ATOM   6290 C  C    . HIS   B 1 240 ? -24.053 -30.746 -27.536 1.00 25.73  ?  242 HIS   I C    1 
ATOM   6291 O  O    . HIS   B 1 240 ? -24.674 -30.855 -28.577 1.00 26.30  ?  242 HIS   I O    1 
ATOM   6292 C  CB   . HIS   B 1 240 ? -22.350 -32.577 -27.194 1.00 33.92  ?  242 HIS   I CB   1 
ATOM   6293 C  CG   . HIS   B 1 240 ? -21.108 -33.155 -27.811 1.00 41.86  ?  242 HIS   I CG   1 
ATOM   6294 N  ND1  . HIS   B 1 240 ? -20.981 -34.496 -28.113 1.00 48.27  ?  242 HIS   I ND1  1 
ATOM   6295 C  CD2  . HIS   B 1 240 ? -19.944 -32.573 -28.199 1.00 44.88  ?  242 HIS   I CD2  1 
ATOM   6296 C  CE1  . HIS   B 1 240 ? -19.789 -34.717 -28.643 1.00 49.23  ?  242 HIS   I CE1  1 
ATOM   6297 N  NE2  . HIS   B 1 240 ? -19.145 -33.564 -28.718 1.00 46.92  ?  242 HIS   I NE2  1 
ATOM   6298 N  N    . THR   B 1 241 ? -24.633 -30.358 -26.405 1.00 26.33  ?  243 THR   I N    1 
ATOM   6299 C  CA   . THR   B 1 241 ? -26.040 -29.958 -26.358 1.00 26.76  ?  243 THR   I CA   1 
ATOM   6300 C  C    . THR   B 1 241 ? -26.232 -28.754 -27.294 1.00 30.30  ?  243 THR   I C    1 
ATOM   6301 O  O    . THR   B 1 241 ? -26.952 -28.860 -28.306 1.00 30.67  ?  243 THR   I O    1 
ATOM   6302 C  CB   . THR   B 1 241 ? -26.472 -29.637 -24.922 1.00 27.40  ?  243 THR   I CB   1 
ATOM   6303 O  OG1  . THR   B 1 241 ? -26.396 -30.846 -24.136 1.00 25.71  ?  243 THR   I OG1  1 
ATOM   6304 C  CG2  . THR   B 1 241 ? -27.895 -28.986 -24.844 1.00 25.89  ?  243 THR   I CG2  1 
ATOM   6305 N  N    . GLU   B 1 242 ? -25.528 -27.650 -27.008 1.00 27.13  ?  244 GLU   I N    1 
ATOM   6306 C  CA   . GLU   B 1 242 ? -25.611 -26.464 -27.861 1.00 28.77  ?  244 GLU   I CA   1 
ATOM   6307 C  C    . GLU   B 1 242 ? -25.316 -26.785 -29.329 1.00 29.42  ?  244 GLU   I C    1 
ATOM   6308 O  O    . GLU   B 1 242 ? -26.040 -26.302 -30.189 1.00 30.99  ?  244 GLU   I O    1 
ATOM   6309 C  CB   . GLU   B 1 242 ? -24.723 -25.318 -27.344 1.00 28.62  ?  244 GLU   I CB   1 
ATOM   6310 C  CG   . GLU   B 1 242 ? -24.656 -24.109 -28.272 1.00 31.42  ?  244 GLU   I CG   1 
ATOM   6311 N  N    . CYS   B 1 243 ? -24.314 -27.618 -29.625 1.00 27.33  ?  245 CYS   I N    1 
ATOM   6312 C  CA   . CYS   B 1 243 ? -23.975 -27.901 -31.022 1.00 27.68  ?  245 CYS   I CA   1 
ATOM   6313 C  C    . CYS   B 1 243 ? -25.115 -28.613 -31.797 1.00 27.60  ?  245 CYS   I C    1 
ATOM   6314 O  O    . CYS   B 1 243 ? -25.433 -28.243 -32.960 1.00 22.92  ?  245 CYS   I O    1 
ATOM   6315 C  CB   . CYS   B 1 243 ? -22.631 -28.656 -31.154 1.00 28.50  ?  245 CYS   I CB   1 
ATOM   6316 S  SG   . CYS   B 1 243 ? -21.187 -27.678 -30.654 1.00 27.92  ?  245 CYS   I SG   1 
ATOM   6317 N  N    . CYS   B 1 244 ? -25.725 -29.608 -31.150 1.00 25.00  ?  246 CYS   I N    1 
ATOM   6318 C  CA   . CYS   B 1 244 ? -26.876 -30.283 -31.722 1.00 27.15  ?  246 CYS   I CA   1 
ATOM   6319 C  C    . CYS   B 1 244 ? -28.059 -29.330 -31.962 1.00 26.51  ?  246 CYS   I C    1 
ATOM   6320 O  O    . CYS   B 1 244 ? -28.806 -29.522 -32.901 1.00 26.42  ?  246 CYS   I O    1 
ATOM   6321 C  CB   . CYS   B 1 244 ? -27.315 -31.469 -30.851 1.00 27.24  ?  246 CYS   I CB   1 
ATOM   6322 S  SG   . CYS   B 1 244 ? -25.998 -32.696 -30.768 1.00 25.49  ?  246 CYS   I SG   1 
ATOM   6323 N  N    . HIS   B 1 245 ? -28.194 -28.293 -31.147 1.00 26.76  ?  247 HIS   I N    1 
ATOM   6324 C  CA   . HIS   B 1 245 ? -29.214 -27.286 -31.390 1.00 28.62  ?  247 HIS   I CA   1 
ATOM   6325 C  C    . HIS   B 1 245 ? -28.980 -26.501 -32.694 1.00 28.55  ?  247 HIS   I C    1 
ATOM   6326 O  O    . HIS   B 1 245 ? -29.911 -25.954 -33.285 1.00 29.95  ?  247 HIS   I O    1 
ATOM   6327 C  CB   . HIS   B 1 245 ? -29.364 -26.376 -30.198 1.00 28.76  ?  247 HIS   I CB   1 
ATOM   6328 C  CG   . HIS   B 1 245 ? -30.422 -25.343 -30.366 1.00 31.29  ?  247 HIS   I CG   1 
ATOM   6329 N  ND1  . HIS   B 1 245 ? -30.123 -24.020 -30.599 1.00 32.64  ?  247 HIS   I ND1  1 
ATOM   6330 C  CD2  . HIS   B 1 245 ? -31.776 -25.433 -30.351 1.00 30.93  ?  247 HIS   I CD2  1 
ATOM   6331 C  CE1  . HIS   B 1 245 ? -31.248 -23.328 -30.678 1.00 33.14  ?  247 HIS   I CE1  1 
ATOM   6332 N  NE2  . HIS   B 1 245 ? -32.265 -24.165 -30.553 1.00 31.72  ?  247 HIS   I NE2  1 
ATOM   6333 N  N    . GLY   B 1 246 ? -27.736 -26.412 -33.117 1.00 27.14  ?  248 GLY   I N    1 
ATOM   6334 C  CA   . GLY   B 1 246 ? -27.433 -26.145 -34.516 1.00 28.62  ?  248 GLY   I CA   1 
ATOM   6335 C  C    . GLY   B 1 246 ? -26.938 -24.770 -34.883 1.00 26.72  ?  248 GLY   I C    1 
ATOM   6336 O  O    . GLY   B 1 246 ? -26.687 -24.542 -36.040 1.00 29.58  ?  248 GLY   I O    1 
ATOM   6337 N  N    . ASP   B 1 247 ? -26.813 -23.854 -33.932 1.00 27.26  ?  249 ASP   I N    1 
ATOM   6338 C  CA   . ASP   B 1 247 ? -26.317 -22.496 -34.223 1.00 25.48  ?  249 ASP   I CA   1 
ATOM   6339 C  C    . ASP   B 1 247 ? -24.784 -22.567 -34.287 1.00 23.31  ?  249 ASP   I C    1 
ATOM   6340 O  O    . ASP   B 1 247 ? -24.150 -22.819 -33.260 1.00 26.69  ?  249 ASP   I O    1 
ATOM   6341 C  CB   . ASP   B 1 247 ? -26.800 -21.555 -33.150 1.00 26.15  ?  249 ASP   I CB   1 
ATOM   6342 C  CG   . ASP   B 1 247 ? -26.374 -20.115 -33.374 1.00 28.75  ?  249 ASP   I CG   1 
ATOM   6343 O  OD1  . ASP   B 1 247 ? -25.179 -19.834 -33.556 1.00 28.76  ?  249 ASP   I OD1  1 
ATOM   6344 O  OD2  . ASP   B 1 247 ? -27.249 -19.234 -33.356 1.00 37.31  ?  249 ASP   I OD2  1 
ATOM   6345 N  N    . LEU   B 1 248 ? -24.211 -22.403 -35.484 1.00 20.90  ?  250 LEU   I N    1 
ATOM   6346 C  CA   . LEU   B 1 248 ? -22.779 -22.656 -35.692 1.00 22.20  ?  250 LEU   I CA   1 
ATOM   6347 C  C    . LEU   B 1 248 ? -21.867 -21.828 -34.806 1.00 20.65  ?  250 LEU   I C    1 
ATOM   6348 O  O    . LEU   B 1 248 ? -20.952 -22.357 -34.246 1.00 19.11  ?  250 LEU   I O    1 
ATOM   6349 C  CB   . LEU   B 1 248 ? -22.350 -22.458 -37.138 1.00 21.88  ?  250 LEU   I CB   1 
ATOM   6350 C  CG   . LEU   B 1 248 ? -20.817 -22.402 -37.342 1.00 24.65  ?  250 LEU   I CG   1 
ATOM   6351 C  CD1  . LEU   B 1 248 ? -20.238 -23.831 -37.237 1.00 23.54  ?  250 LEU   I CD1  1 
ATOM   6352 C  CD2  . LEU   B 1 248 ? -20.447 -21.727 -38.653 1.00 24.84  ?  250 LEU   I CD2  1 
ATOM   6353 N  N    . LEU   B 1 249 ? -22.093 -20.525 -34.745 1.00 22.84  ?  251 LEU   I N    1 
ATOM   6354 C  CA   . LEU   B 1 249 ? -21.248 -19.622 -33.962 1.00 24.76  ?  251 LEU   I CA   1 
ATOM   6355 C  C    . LEU   B 1 249 ? -21.245 -20.012 -32.494 1.00 25.18  ?  251 LEU   I C    1 
ATOM   6356 O  O    . LEU   B 1 249 ? -20.205 -20.096 -31.896 1.00 26.21  ?  251 LEU   I O    1 
ATOM   6357 C  CB   . LEU   B 1 249 ? -21.713 -18.175 -34.096 1.00 26.36  ?  251 LEU   I CB   1 
ATOM   6358 C  CG   . LEU   B 1 249 ? -21.469 -17.568 -35.461 1.00 28.25  ?  251 LEU   I CG   1 
ATOM   6359 C  CD1  . LEU   B 1 249 ? -21.952 -16.153 -35.458 1.00 28.82  ?  251 LEU   I CD1  1 
ATOM   6360 C  CD2  . LEU   B 1 249 ? -19.985 -17.625 -35.830 1.00 29.34  ?  251 LEU   I CD2  1 
ATOM   6361 N  N    . GLU   B 1 250 ? -22.408 -20.316 -31.949 1.00 27.73  ?  252 GLU   I N    1 
ATOM   6362 C  CA   . GLU   B 1 250 ? -22.529 -20.671 -30.527 1.00 29.36  ?  252 GLU   I CA   1 
ATOM   6363 C  C    . GLU   B 1 250 ? -21.811 -21.976 -30.246 1.00 25.36  ?  252 GLU   I C    1 
ATOM   6364 O  O    . GLU   B 1 250 ? -21.164 -22.102 -29.215 1.00 21.24  ?  252 GLU   I O    1 
ATOM   6365 C  CB   . GLU   B 1 250 ? -24.003 -20.795 -30.118 1.00 33.35  ?  252 GLU   I CB   1 
ATOM   6366 C  CG   . GLU   B 1 250 ? -24.816 -19.498 -30.250 1.00 41.28  ?  252 GLU   I CG   1 
ATOM   6367 C  CD   . GLU   B 1 250 ? -24.399 -18.397 -29.270 1.00 43.24  ?  252 GLU   I CD   1 
ATOM   6368 O  OE1  . GLU   B 1 250 ? -24.082 -18.739 -28.111 1.00 52.15  ?  252 GLU   I OE1  1 
ATOM   6369 O  OE2  . GLU   B 1 250 ? -24.396 -17.195 -29.646 1.00 41.77  ?  252 GLU   I OE2  1 
ATOM   6370 N  N    . CYS   B 1 251 ? -21.931 -22.926 -31.177 1.00 25.19  ?  253 CYS   I N    1 
ATOM   6371 C  CA   . CYS   B 1 251 ? -21.199 -24.218 -31.113 1.00 25.39  ?  253 CYS   I CA   1 
ATOM   6372 C  C    . CYS   B 1 251 ? -19.673 -24.043 -31.250 1.00 24.49  ?  253 CYS   I C    1 
ATOM   6373 O  O    . CYS   B 1 251 ? -18.848 -24.776 -30.635 1.00 23.32  ?  253 CYS   I O    1 
ATOM   6374 C  CB   . CYS   B 1 251 ? -21.708 -25.155 -32.200 1.00 26.01  ?  253 CYS   I CB   1 
ATOM   6375 S  SG   . CYS   B 1 251 ? -20.776 -26.674 -32.342 1.00 31.47  ?  253 CYS   I SG   1 
ATOM   6376 N  N    . ALA   B 1 252 ? -19.285 -23.060 -32.039 1.00 22.41  ?  254 ALA   I N    1 
ATOM   6377 C  CA   . ALA   B 1 252 ? -17.857 -22.814 -32.289 1.00 22.00  ?  254 ALA   I CA   1 
ATOM   6378 C  C    . ALA   B 1 252 ? -17.217 -22.182 -31.070 1.00 20.56  ?  254 ALA   I C    1 
ATOM   6379 O  O    . ALA   B 1 252 ? -16.143 -22.596 -30.638 1.00 18.05  ?  254 ALA   I O    1 
ATOM   6380 C  CB   . ALA   B 1 252 ? -17.649 -21.965 -33.555 1.00 22.76  ?  254 ALA   I CB   1 
ATOM   6381 N  N    . ASP   B 1 253 ? -17.901 -21.205 -30.497 1.00 23.21  ?  255 ASP   I N    1 
ATOM   6382 C  CA   . ASP   B 1 253 ? -17.440 -20.568 -29.258 1.00 23.62  ?  255 ASP   I CA   1 
ATOM   6383 C  C    . ASP   B 1 253 ? -17.453 -21.526 -28.077 1.00 22.92  ?  255 ASP   I C    1 
ATOM   6384 O  O    . ASP   B 1 253 ? -16.549 -21.473 -27.276 1.00 20.86  ?  255 ASP   I O    1 
ATOM   6385 C  CB   . ASP   B 1 253 ? -18.283 -19.363 -28.889 1.00 24.37  ?  255 ASP   I CB   1 
ATOM   6386 C  CG   . ASP   B 1 253 ? -18.207 -18.250 -29.937 1.00 25.63  ?  255 ASP   I CG   1 
ATOM   6387 O  OD1  . ASP   B 1 253 ? -17.251 -18.255 -30.723 1.00 23.73  ?  255 ASP   I OD1  1 
ATOM   6388 O  OD2  . ASP   B 1 253 ? -19.156 -17.431 -30.010 1.00 27.69  ?  255 ASP   I OD2  1 
ATOM   6389 N  N    . ASP   B 1 254 ? -18.495 -22.355 -27.941 1.00 23.02  ?  256 ASP   I N    1 
ATOM   6390 C  CA   . ASP   B 1 254 ? -18.488 -23.339 -26.865 1.00 24.49  ?  256 ASP   I CA   1 
ATOM   6391 C  C    . ASP   B 1 254 ? -17.286 -24.246 -27.003 1.00 22.63  ?  256 ASP   I C    1 
ATOM   6392 O  O    . ASP   B 1 254 ? -16.569 -24.441 -26.043 1.00 24.57  ?  256 ASP   I O    1 
ATOM   6393 C  CB   . ASP   B 1 254 ? -19.772 -24.172 -26.792 1.00 24.87  ?  256 ASP   I CB   1 
ATOM   6394 C  CG   . ASP   B 1 254 ? -20.933 -23.406 -26.214 1.00 26.34  ?  256 ASP   I CG   1 
ATOM   6395 O  OD1  . ASP   B 1 254 ? -20.759 -22.275 -25.704 1.00 27.46  ?  256 ASP   I OD1  1 
ATOM   6396 O  OD2  . ASP   B 1 254 ? -22.053 -23.937 -26.306 1.00 28.34  ?  256 ASP   I OD2  1 
ATOM   6397 N  N    . ARG   B 1 255 ? -17.067 -24.784 -28.194 1.00 23.46  ?  257 ARG   I N    1 
ATOM   6398 C  CA   . ARG   B 1 255 ? -15.926 -25.676 -28.463 1.00 21.64  ?  257 ARG   I CA   1 
ATOM   6399 C  C    . ARG   B 1 255 ? -14.599 -24.994 -28.146 1.00 20.63  ?  257 ARG   I C    1 
ATOM   6400 O  O    . ARG   B 1 255 ? -13.752 -25.589 -27.541 1.00 20.53  ?  257 ARG   I O    1 
ATOM   6401 C  CB   . ARG   B 1 255 ? -15.923 -26.150 -29.906 1.00 23.46  ?  257 ARG   I CB   1 
ATOM   6402 C  CG   . ARG   B 1 255 ? -16.582 -27.507 -30.171 1.00 25.20  ?  257 ARG   I CG   1 
ATOM   6403 C  CD   . ARG   B 1 255 ? -16.354 -27.984 -31.610 1.00 27.34  ?  257 ARG   I CD   1 
ATOM   6404 N  NE   . ARG   B 1 255 ? -15.757 -29.358 -31.701 1.00 33.31  ?  257 ARG   I NE   1 
ATOM   6405 C  CZ   . ARG   B 1 255 ? -14.632 -29.676 -32.364 1.00 33.34  ?  257 ARG   I CZ   1 
ATOM   6406 N  NH1  . ARG   B 1 255 ? -13.952 -28.768 -33.038 1.00 35.67  ?  257 ARG   I NH1  1 
ATOM   6407 N  NH2  . ARG   B 1 255 ? -14.190 -30.925 -32.396 1.00 37.21  ?  257 ARG   I NH2  1 
ATOM   6408 N  N    . ALA   B 1 256 ? -14.450 -23.746 -28.577 1.00 19.03  ?  258 ALA   I N    1 
ATOM   6409 C  CA   . ALA   B 1 256 ? -13.264 -22.957 -28.373 1.00 20.11  ?  258 ALA   I CA   1 
ATOM   6410 C  C    . ALA   B 1 256 ? -12.895 -22.763 -26.904 1.00 21.26  ?  258 ALA   I C    1 
ATOM   6411 O  O    . ALA   B 1 256 ? -11.722 -22.931 -26.536 1.00 22.95  ?  258 ALA   I O    1 
ATOM   6412 C  CB   . ALA   B 1 256 ? -13.415 -21.596 -29.053 1.00 20.68  ?  258 ALA   I CB   1 
ATOM   6413 N  N    . ASP   B 1 257 ? -13.897 -22.431 -26.094 1.00 22.86  ?  259 ASP   I N    1 
ATOM   6414 C  CA   . ASP   B 1 257 ? -13.784 -22.219 -24.615 1.00 22.62  ?  259 ASP   I CA   1 
ATOM   6415 C  C    . ASP   B 1 257 ? -13.253 -23.484 -23.946 1.00 21.89  ?  259 ASP   I C    1 
ATOM   6416 O  O    . ASP   B 1 257 ? -12.271 -23.436 -23.184 1.00 21.52  ?  259 ASP   I O    1 
ATOM   6417 C  CB   . ASP   B 1 257 ? -15.162 -21.862 -23.984 1.00 23.81  ?  259 ASP   I CB   1 
ATOM   6418 C  CG   . ASP   B 1 257 ? -15.641 -20.407 -24.304 1.00 27.78  ?  259 ASP   I CG   1 
ATOM   6419 O  OD1  . ASP   B 1 257 ? -14.814 -19.510 -24.514 1.00 28.16  ?  259 ASP   I OD1  1 
ATOM   6420 O  OD2  . ASP   B 1 257 ? -16.876 -20.144 -24.347 1.00 29.37  ?  259 ASP   I OD2  1 
ATOM   6421 N  N    . LEU   B 1 258 ? -13.874 -24.624 -24.260 1.00 19.73  ?  260 LEU   I N    1 
ATOM   6422 C  CA   . LEU   B 1 258 ? -13.429 -25.884 -23.679 1.00 18.13  ?  260 LEU   I CA   1 
ATOM   6423 C  C    . LEU   B 1 258 ? -11.995 -26.178 -24.030 1.00 20.06  ?  260 LEU   I C    1 
ATOM   6424 O  O    . LEU   B 1 258 ? -11.198 -26.545 -23.165 1.00 25.05  ?  260 LEU   I O    1 
ATOM   6425 C  CB   . LEU   B 1 258 ? -14.354 -27.044 -24.112 1.00 17.80  ?  260 LEU   I CB   1 
ATOM   6426 C  CG   . LEU   B 1 258 ? -14.034 -28.427 -23.483 1.00 16.89  ?  260 LEU   I CG   1 
ATOM   6427 C  CD1  . LEU   B 1 258 ? -13.998 -28.348 -21.975 1.00 16.39  ?  260 LEU   I CD1  1 
ATOM   6428 C  CD2  . LEU   B 1 258 ? -15.058 -29.478 -23.895 1.00 17.20  ?  260 LEU   I CD2  1 
ATOM   6429 N  N    . ALA   B 1 259 ? -11.628 -26.017 -25.294 1.00 21.40  ?  261 ALA   I N    1 
ATOM   6430 C  CA   . ALA   B 1 259 ? -10.291 -26.331 -25.732 1.00 20.48  ?  261 ALA   I CA   1 
ATOM   6431 C  C    . ALA   B 1 259 ? -9.230  -25.441 -25.072 1.00 23.47  ?  261 ALA   I C    1 
ATOM   6432 O  O    . ALA   B 1 259 ? -8.112  -25.907 -24.755 1.00 20.47  ?  261 ALA   I O    1 
ATOM   6433 C  CB   . ALA   B 1 259 ? -10.206 -26.172 -27.228 1.00 22.62  ?  261 ALA   I CB   1 
ATOM   6434 N  N    . LYS   B 1 260 ? -9.560  -24.159 -24.921 1.00 24.30  ?  262 LYS   I N    1 
ATOM   6435 C  CA   . LYS   B 1 260 ? -8.705  -23.200 -24.191 1.00 27.62  ?  262 LYS   I CA   1 
ATOM   6436 C  C    . LYS   B 1 260 ? -8.612  -23.617 -22.734 1.00 28.70  ?  262 LYS   I C    1 
ATOM   6437 O  O    . LYS   B 1 260 ? -7.534  -23.565 -22.173 1.00 29.62  ?  262 LYS   I O    1 
ATOM   6438 C  CB   . LYS   B 1 260 ? -9.251  -21.753 -24.257 1.00 28.32  ?  262 LYS   I CB   1 
ATOM   6439 N  N    . TYR   B 1 261 ? -9.723  -24.037 -22.126 1.00 27.80  ?  263 TYR   I N    1 
ATOM   6440 C  CA   . TYR   B 1 261 ? -9.662  -24.517 -20.735 1.00 27.30  ?  263 TYR   I CA   1 
ATOM   6441 C  C    . TYR   B 1 261 ? -8.735  -25.735 -20.631 1.00 25.92  ?  263 TYR   I C    1 
ATOM   6442 O  O    . TYR   B 1 261 ? -7.893  -25.814 -19.715 1.00 21.57  ?  263 TYR   I O    1 
ATOM   6443 C  CB   . TYR   B 1 261 ? -11.044 -24.770 -20.094 1.00 26.86  ?  263 TYR   I CB   1 
ATOM   6444 C  CG   . TYR   B 1 261 ? -10.877 -25.485 -18.780 1.00 27.09  ?  263 TYR   I CG   1 
ATOM   6445 C  CD1  . TYR   B 1 261 ? -10.681 -24.786 -17.601 1.00 26.66  ?  263 TYR   I CD1  1 
ATOM   6446 C  CD2  . TYR   B 1 261 ? -10.831 -26.865 -18.743 1.00 26.47  ?  263 TYR   I CD2  1 
ATOM   6447 C  CE1  . TYR   B 1 261 ? -10.462 -25.463 -16.407 1.00 30.63  ?  263 TYR   I CE1  1 
ATOM   6448 C  CE2  . TYR   B 1 261 ? -10.609 -27.545 -17.582 1.00 29.53  ?  263 TYR   I CE2  1 
ATOM   6449 C  CZ   . TYR   B 1 261 ? -10.425 -26.852 -16.410 1.00 31.09  ?  263 TYR   I CZ   1 
ATOM   6450 O  OH   . TYR   B 1 261 ? -10.200 -27.556 -15.265 1.00 35.12  ?  263 TYR   I OH   1 
ATOM   6451 N  N    . ILE   B 1 262 ? -8.860  -26.658 -21.583 1.00 30.01  ?  264 ILE   I N    1 
ATOM   6452 C  CA   . ILE   B 1 262 ? -8.021  -27.893 -21.598 1.00 29.55  ?  264 ILE   I CA   1 
ATOM   6453 C  C    . ILE   B 1 262 ? -6.564  -27.490 -21.797 1.00 31.57  ?  264 ILE   I C    1 
ATOM   6454 O  O    . ILE   B 1 262 ? -5.660  -28.011 -21.123 1.00 31.01  ?  264 ILE   I O    1 
ATOM   6455 C  CB   . ILE   B 1 262 ? -8.445  -28.883 -22.722 1.00 27.51  ?  264 ILE   I CB   1 
ATOM   6456 C  CG1  . ILE   B 1 262 ? -9.759  -29.549 -22.334 1.00 27.15  ?  264 ILE   I CG1  1 
ATOM   6457 C  CG2  . ILE   B 1 262 ? -7.381  -29.963 -22.980 1.00 28.34  ?  264 ILE   I CG2  1 
ATOM   6458 C  CD1  . ILE   B 1 262 ? -10.409 -30.332 -23.460 1.00 25.63  ?  264 ILE   I CD1  1 
ATOM   6459 N  N    . CYS   B 1 263 ? -6.336  -26.534 -22.688 1.00 30.35  ?  265 CYS   I N    1 
ATOM   6460 C  CA   . CYS   B 1 263 ? -4.969  -26.103 -22.939 1.00 32.81  ?  265 CYS   I CA   1 
ATOM   6461 C  C    . CYS   B 1 263 ? -4.331  -25.351 -21.806 1.00 31.11  ?  265 CYS   I C    1 
ATOM   6462 O  O    . CYS   B 1 263 ? -3.115  -25.368 -21.676 1.00 32.71  ?  265 CYS   I O    1 
ATOM   6463 C  CB   . CYS   B 1 263 ? -4.862  -25.286 -24.217 1.00 34.24  ?  265 CYS   I CB   1 
ATOM   6464 S  SG   . CYS   B 1 263 ? -5.156  -26.330 -25.623 1.00 31.30  ?  265 CYS   I SG   1 
ATOM   6465 N  N    . GLU   B 1 264 ? -5.147  -24.712 -20.993 1.00 32.57  ?  266 GLU   I N    1 
ATOM   6466 C  CA   . GLU   B 1 264 ? -4.656  -23.947 -19.874 1.00 34.09  ?  266 GLU   I CA   1 
ATOM   6467 C  C    . GLU   B 1 264 ? -4.357  -24.848 -18.667 1.00 32.20  ?  266 GLU   I C    1 
ATOM   6468 O  O    . GLU   B 1 264 ? -3.703  -24.407 -17.761 1.00 30.01  ?  266 GLU   I O    1 
ATOM   6469 C  CB   . GLU   B 1 264 ? -5.637  -22.825 -19.523 1.00 35.66  ?  266 GLU   I CB   1 
ATOM   6470 C  CG   . GLU   B 1 264 ? -5.570  -21.653 -20.499 1.00 38.29  ?  266 GLU   I CG   1 
ATOM   6471 C  CD   . GLU   B 1 264 ? -6.460  -20.498 -20.098 1.00 42.39  ?  266 GLU   I CD   1 
ATOM   6472 O  OE1  . GLU   B 1 264 ? -7.367  -20.702 -19.255 1.00 44.64  ?  266 GLU   I OE1  1 
ATOM   6473 O  OE2  . GLU   B 1 264 ? -6.262  -19.382 -20.642 1.00 47.13  ?  266 GLU   I OE2  1 
ATOM   6474 N  N    . ASN   B 1 265 ? -4.830  -26.094 -18.692 1.00 30.92  ?  267 ASN   I N    1 
ATOM   6475 C  CA   . ASN   B 1 265 ? -4.684  -27.036 -17.591 1.00 32.11  ?  267 ASN   I CA   1 
ATOM   6476 C  C    . ASN   B 1 265 ? -4.101  -28.359 -18.068 1.00 31.32  ?  267 ASN   I C    1 
ATOM   6477 O  O    . ASN   B 1 265 ? -4.584  -29.436 -17.694 1.00 33.89  ?  267 ASN   I O    1 
ATOM   6478 C  CB   . ASN   B 1 265 ? -6.071  -27.306 -16.962 1.00 32.60  ?  267 ASN   I CB   1 
ATOM   6479 C  CG   . ASN   B 1 265 ? -6.669  -26.099 -16.313 1.00 33.50  ?  267 ASN   I CG   1 
ATOM   6480 O  OD1  . ASN   B 1 265 ? -6.364  -25.800 -15.171 1.00 37.26  ?  267 ASN   I OD1  1 
ATOM   6481 N  ND2  . ASN   B 1 265 ? -7.524  -25.376 -17.047 1.00 37.52  ?  267 ASN   I ND2  1 
ATOM   6482 N  N    . GLN   B 1 266 ? -3.052  -28.317 -18.869 1.00 32.37  ?  268 GLN   I N    1 
ATOM   6483 C  CA   . GLN   B 1 266 ? -2.510  -29.558 -19.426 1.00 35.51  ?  268 GLN   I CA   1 
ATOM   6484 C  C    . GLN   B 1 266 ? -1.974  -30.470 -18.334 1.00 35.20  ?  268 GLN   I C    1 
ATOM   6485 O  O    . GLN   B 1 266 ? -2.315  -31.655 -18.277 1.00 33.05  ?  268 GLN   I O    1 
ATOM   6486 C  CB   . GLN   B 1 266 ? -1.398  -29.293 -20.417 1.00 36.46  ?  268 GLN   I CB   1 
ATOM   6487 C  CG   . GLN   B 1 266 ? -1.777  -28.511 -21.663 1.00 36.68  ?  268 GLN   I CG   1 
ATOM   6488 C  CD   . GLN   B 1 266 ? -0.607  -28.464 -22.640 1.00 36.59  ?  268 GLN   I CD   1 
ATOM   6489 O  OE1  . GLN   B 1 266 ? 0.014   -29.490 -22.901 1.00 33.41  ?  268 GLN   I OE1  1 
ATOM   6490 N  NE2  . GLN   B 1 266 ? -0.275  -27.269 -23.149 1.00 36.16  ?  268 GLN   I NE2  1 
ATOM   6491 N  N    . ASP   B 1 267 ? -1.162  -29.904 -17.450 1.00 38.44  ?  269 ASP   I N    1 
ATOM   6492 C  CA   . ASP   B 1 267 ? -0.591  -30.645 -16.304 1.00 40.41  ?  269 ASP   I CA   1 
ATOM   6493 C  C    . ASP   B 1 267 ? -1.600  -31.361 -15.437 1.00 36.50  ?  269 ASP   I C    1 
ATOM   6494 O  O    . ASP   B 1 267 ? -1.270  -32.348 -14.801 1.00 40.25  ?  269 ASP   I O    1 
ATOM   6495 C  CB   . ASP   B 1 267 ? 0.211   -29.712 -15.388 1.00 46.22  ?  269 ASP   I CB   1 
ATOM   6496 C  CG   . ASP   B 1 267 ? 1.452   -29.187 -16.045 1.00 50.13  ?  269 ASP   I CG   1 
ATOM   6497 O  OD1  . ASP   B 1 267 ? 1.849   -29.718 -17.120 1.00 53.99  ?  269 ASP   I OD1  1 
ATOM   6498 O  OD2  . ASP   B 1 267 ? 2.019   -28.227 -15.479 1.00 55.40  ?  269 ASP   I OD2  1 
ATOM   6499 N  N    . SER   B 1 268 ? -2.820  -30.854 -15.398 1.00 34.40  ?  270 SER   I N    1 
ATOM   6500 C  CA   . SER   B 1 268 ? -3.882  -31.513 -14.693 1.00 32.26  ?  270 SER   I CA   1 
ATOM   6501 C  C    . SER   B 1 268 ? -4.639  -32.585 -15.526 1.00 28.68  ?  270 SER   I C    1 
ATOM   6502 O  O    . SER   B 1 268 ? -5.500  -33.266 -14.981 1.00 29.52  ?  270 SER   I O    1 
ATOM   6503 C  CB   . SER   B 1 268 ? -4.845  -30.444 -14.181 1.00 35.36  ?  270 SER   I CB   1 
ATOM   6504 O  OG   . SER   B 1 268 ? -5.988  -31.029 -13.555 1.00 43.59  ?  270 SER   I OG   1 
ATOM   6505 N  N    . ILE   B 1 269 ? -4.352  -32.710 -16.827 1.00 26.68  ?  271 ILE   I N    1 
ATOM   6506 C  CA   . ILE   B 1 269 ? -5.184  -33.460 -17.746 1.00 25.08  ?  271 ILE   I CA   1 
ATOM   6507 C  C    . ILE   B 1 269 ? -4.397  -34.541 -18.503 1.00 24.59  ?  271 ILE   I C    1 
ATOM   6508 O  O    . ILE   B 1 269 ? -4.700  -35.720 -18.381 1.00 22.80  ?  271 ILE   I O    1 
ATOM   6509 C  CB   . ILE   B 1 269 ? -5.958  -32.501 -18.682 1.00 26.31  ?  271 ILE   I CB   1 
ATOM   6510 C  CG1  . ILE   B 1 269 ? -6.931  -31.649 -17.841 1.00 26.82  ?  271 ILE   I CG1  1 
ATOM   6511 C  CG2  . ILE   B 1 269 ? -6.712  -33.282 -19.784 1.00 25.00  ?  271 ILE   I CG2  1 
ATOM   6512 C  CD1  . ILE   B 1 269 ? -7.717  -30.589 -18.633 1.00 27.14  ?  271 ILE   I CD1  1 
ATOM   6513 N  N    . SER   B 1 270 ? -3.393  -34.163 -19.277 1.00 26.20  ?  272 SER   I N    1 
ATOM   6514 C  CA   . SER   B 1 270 ? -2.578  -35.137 -20.023 1.00 26.39  ?  272 SER   I CA   1 
ATOM   6515 C  C    . SER   B 1 270 ? -1.305  -34.515 -20.601 1.00 30.87  ?  272 SER   I C    1 
ATOM   6516 O  O    . SER   B 1 270 ? -1.330  -33.394 -21.131 1.00 32.45  ?  272 SER   I O    1 
ATOM   6517 C  CB   . SER   B 1 270 ? -3.412  -35.730 -21.173 1.00 25.92  ?  272 SER   I CB   1 
ATOM   6518 O  OG   . SER   B 1 270 ? -2.619  -36.253 -22.209 1.00 22.57  ?  272 SER   I OG   1 
ATOM   6519 N  N    . SER   B 1 271 ? -0.227  -35.295 -20.560 1.00 33.52  ?  273 SER   I N    1 
ATOM   6520 C  CA   . SER   B 1 271 ? 1.098   -34.957 -21.138 1.00 33.49  ?  273 SER   I CA   1 
ATOM   6521 C  C    . SER   B 1 271 ? 1.185   -35.004 -22.678 1.00 32.93  ?  273 SER   I C    1 
ATOM   6522 O  O    . SER   B 1 271 ? 2.236   -34.738 -23.231 1.00 35.20  ?  273 SER   I O    1 
ATOM   6523 C  CB   . SER   B 1 271 ? 2.124   -35.960 -20.584 1.00 32.98  ?  273 SER   I CB   1 
ATOM   6524 O  OG   . SER   B 1 271 ? 1.712   -37.291 -20.886 1.00 33.07  ?  273 SER   I OG   1 
ATOM   6525 N  N    . LYS   B 1 272 ? 0.106   -35.361 -23.365 1.00 32.89  ?  274 LYS   I N    1 
ATOM   6526 C  CA   . LYS   B 1 272 ? 0.124   -35.466 -24.819 1.00 32.64  ?  274 LYS   I CA   1 
ATOM   6527 C  C    . LYS   B 1 272 ? -0.559  -34.299 -25.551 1.00 31.70  ?  274 LYS   I C    1 
ATOM   6528 O  O    . LYS   B 1 272 ? -0.759  -34.381 -26.743 1.00 35.66  ?  274 LYS   I O    1 
ATOM   6529 C  CB   . LYS   B 1 272 ? -0.463  -36.813 -25.221 1.00 32.68  ?  274 LYS   I CB   1 
ATOM   6530 C  CG   . LYS   B 1 272 ? 0.452   -37.942 -24.779 1.00 33.04  ?  274 LYS   I CG   1 
ATOM   6531 C  CD   . LYS   B 1 272 ? -0.048  -39.271 -25.228 1.00 33.71  ?  274 LYS   I CD   1 
ATOM   6532 C  CE   . LYS   B 1 272 ? 0.870   -40.365 -24.732 1.00 34.88  ?  274 LYS   I CE   1 
ATOM   6533 N  NZ   . LYS   B 1 272 ? 0.594   -41.605 -25.491 1.00 35.30  ?  274 LYS   I NZ   1 
ATOM   6534 N  N    . LEU   B 1 273 ? -0.846  -33.206 -24.857 1.00 32.29  ?  275 LEU   I N    1 
ATOM   6535 C  CA   . LEU   B 1 273 ? -1.601  -32.061 -25.444 1.00 35.41  ?  275 LEU   I CA   1 
ATOM   6536 C  C    . LEU   B 1 273 ? -0.738  -30.929 -25.993 1.00 35.37  ?  275 LEU   I C    1 
ATOM   6537 O  O    . LEU   B 1 273 ? -1.277  -29.994 -26.603 1.00 40.69  ?  275 LEU   I O    1 
ATOM   6538 C  CB   . LEU   B 1 273 ? -2.560  -31.453 -24.404 1.00 32.12  ?  275 LEU   I CB   1 
ATOM   6539 C  CG   . LEU   B 1 273 ? -4.021  -31.882 -24.292 1.00 32.12  ?  275 LEU   I CG   1 
ATOM   6540 C  CD1  . LEU   B 1 273 ? -4.437  -32.961 -25.264 1.00 31.09  ?  275 LEU   I CD1  1 
ATOM   6541 C  CD2  . LEU   B 1 273 ? -4.311  -32.272 -22.855 1.00 30.52  ?  275 LEU   I CD2  1 
ATOM   6542 N  N    . LYS   B 1 274 ? 0.573   -31.006 -25.778 1.00 35.21  ?  276 LYS   I N    1 
ATOM   6543 C  CA   . LYS   B 1 274 ? 1.506   -29.944 -26.147 1.00 33.76  ?  276 LYS   I CA   1 
ATOM   6544 C  C    . LYS   B 1 274 ? 1.288   -29.456 -27.561 1.00 32.57  ?  276 LYS   I C    1 
ATOM   6545 O  O    . LYS   B 1 274 ? 1.173   -28.256 -27.796 1.00 34.80  ?  276 LYS   I O    1 
ATOM   6546 C  CB   . LYS   B 1 274 ? 2.966   -30.429 -25.985 1.00 37.11  ?  276 LYS   I CB   1 
ATOM   6547 N  N    . GLU   B 1 275 ? 1.189   -30.398 -28.486 1.00 33.40  ?  277 GLU   I N    1 
ATOM   6548 C  CA   . GLU   B 1 275 ? 1.095   -30.099 -29.912 1.00 35.80  ?  277 GLU   I CA   1 
ATOM   6549 C  C    . GLU   B 1 275 ? -0.288  -29.527 -30.282 1.00 37.02  ?  277 GLU   I C    1 
ATOM   6550 O  O    . GLU   B 1 275 ? -0.382  -28.459 -30.949 1.00 38.56  ?  277 GLU   I O    1 
ATOM   6551 C  CB   . GLU   B 1 275 ? 1.392   -31.337 -30.741 1.00 37.91  ?  277 GLU   I CB   1 
ATOM   6552 C  CG   . GLU   B 1 275 ? 2.756   -31.968 -30.473 1.00 43.23  ?  277 GLU   I CG   1 
ATOM   6553 C  CD   . GLU   B 1 275 ? 2.696   -33.167 -29.518 1.00 47.68  ?  277 GLU   I CD   1 
ATOM   6554 O  OE1  . GLU   B 1 275 ? 2.188   -32.991 -28.379 1.00 47.64  ?  277 GLU   I OE1  1 
ATOM   6555 O  OE2  . GLU   B 1 275 ? 3.140   -34.286 -29.905 1.00 49.07  ?  277 GLU   I OE2  1 
ATOM   6556 N  N    . CYS   B 1 276 ? -1.356  -30.188 -29.826 1.00 32.56  ?  278 CYS   I N    1 
ATOM   6557 C  CA   . CYS   B 1 276 ? -2.706  -29.637 -30.037 1.00 32.73  ?  278 CYS   I CA   1 
ATOM   6558 C  C    . CYS   B 1 276 ? -2.855  -28.234 -29.530 1.00 31.18  ?  278 CYS   I C    1 
ATOM   6559 O  O    . CYS   B 1 276 ? -3.469  -27.414 -30.180 1.00 28.25  ?  278 CYS   I O    1 
ATOM   6560 C  CB   . CYS   B 1 276 ? -3.756  -30.486 -29.361 1.00 34.35  ?  278 CYS   I CB   1 
ATOM   6561 S  SG   . CYS   B 1 276 ? -3.721  -32.146 -30.034 1.00 37.85  ?  278 CYS   I SG   1 
ATOM   6562 N  N    . CYS   B 1 277 ? -2.267  -27.964 -28.367 1.00 31.96  ?  279 CYS   I N    1 
ATOM   6563 C  CA   . CYS   B 1 277 ? -2.463  -26.707 -27.689 1.00 30.71  ?  279 CYS   I CA   1 
ATOM   6564 C  C    . CYS   B 1 277 ? -1.643  -25.553 -28.258 1.00 30.14  ?  279 CYS   I C    1 
ATOM   6565 O  O    . CYS   B 1 277 ? -1.948  -24.393 -28.007 1.00 27.91  ?  279 CYS   I O    1 
ATOM   6566 C  CB   . CYS   B 1 277 ? -2.319  -26.934 -26.164 1.00 33.08  ?  279 CYS   I CB   1 
ATOM   6567 S  SG   . CYS   B 1 277 ? -3.783  -27.835 -25.520 1.00 33.99  ?  279 CYS   I SG   1 
ATOM   6568 N  N    . GLU   B 1 278 ? -0.638  -25.879 -29.070 1.00 36.29  ?  280 GLU   I N    1 
ATOM   6569 C  CA   . GLU   B 1 278 ? 0.195   -24.888 -29.790 1.00 39.10  ?  280 GLU   I CA   1 
ATOM   6570 C  C    . GLU   B 1 278 ? -0.371  -24.539 -31.201 1.00 40.80  ?  280 GLU   I C    1 
ATOM   6571 O  O    . GLU   B 1 278 ? 0.083   -23.578 -31.827 1.00 41.98  ?  280 GLU   I O    1 
ATOM   6572 C  CB   . GLU   B 1 278 ? 1.656   -25.384 -29.858 1.00 37.27  ?  280 GLU   I CB   1 
ATOM   6573 N  N    . LYS   B 1 279 ? -1.374  -25.291 -31.672 1.00 41.15  ?  281 LYS   I N    1 
ATOM   6574 C  CA   . LYS   B 1 279 ? -2.048  -25.022 -32.957 1.00 39.33  ?  281 LYS   I CA   1 
ATOM   6575 C  C    . LYS   B 1 279 ? -3.043  -23.843 -32.878 1.00 37.02  ?  281 LYS   I C    1 
ATOM   6576 O  O    . LYS   B 1 279 ? -3.434  -23.425 -31.794 1.00 31.66  ?  281 LYS   I O    1 
ATOM   6577 C  CB   . LYS   B 1 279 ? -2.727  -26.297 -33.472 1.00 41.11  ?  281 LYS   I CB   1 
ATOM   6578 C  CG   . LYS   B 1 279 ? -1.715  -27.283 -34.021 1.00 42.78  ?  281 LYS   I CG   1 
ATOM   6579 C  CD   . LYS   B 1 279 ? -2.327  -28.643 -34.270 1.00 40.63  ?  281 LYS   I CD   1 
ATOM   6580 C  CE   . LYS   B 1 279 ? -1.285  -29.575 -34.833 1.00 43.44  ?  281 LYS   I CE   1 
ATOM   6581 N  NZ   . LYS   B 1 279 ? -1.850  -30.966 -35.001 1.00 48.86  ?  281 LYS   I NZ   1 
ATOM   6582 N  N    . PRO   B 1 280 ? -3.434  -23.273 -34.040 1.00 39.55  ?  282 PRO   I N    1 
ATOM   6583 C  CA   . PRO   B 1 280 ? -4.302  -22.088 -33.950 1.00 38.85  ?  282 PRO   I CA   1 
ATOM   6584 C  C    . PRO   B 1 280 ? -5.773  -22.411 -33.527 1.00 38.37  ?  282 PRO   I C    1 
ATOM   6585 O  O    . PRO   B 1 280 ? -6.241  -23.551 -33.659 1.00 37.31  ?  282 PRO   I O    1 
ATOM   6586 C  CB   . PRO   B 1 280 ? -4.203  -21.488 -35.356 1.00 39.12  ?  282 PRO   I CB   1 
ATOM   6587 C  CG   . PRO   B 1 280 ? -3.902  -22.639 -36.254 1.00 37.76  ?  282 PRO   I CG   1 
ATOM   6588 C  CD   . PRO   B 1 280 ? -3.121  -23.634 -35.442 1.00 39.73  ?  282 PRO   I CD   1 
ATOM   6589 N  N    . LEU   B 1 281 ? -6.464  -21.412 -32.985 1.00 38.88  ?  283 LEU   I N    1 
ATOM   6590 C  CA   . LEU   B 1 281 ? -7.847  -21.538 -32.518 1.00 39.97  ?  283 LEU   I CA   1 
ATOM   6591 C  C    . LEU   B 1 281 ? -8.662  -22.556 -33.316 1.00 40.26  ?  283 LEU   I C    1 
ATOM   6592 O  O    . LEU   B 1 281 ? -9.294  -23.452 -32.730 1.00 39.44  ?  283 LEU   I O    1 
ATOM   6593 C  CB   . LEU   B 1 281 ? -8.542  -20.178 -32.564 1.00 41.82  ?  283 LEU   I CB   1 
ATOM   6594 C  CG   . LEU   B 1 281 ? -10.062 -20.128 -32.308 1.00 49.84  ?  283 LEU   I CG   1 
ATOM   6595 C  CD1  . LEU   B 1 281 ? -10.442 -20.769 -30.978 1.00 50.11  ?  283 LEU   I CD1  1 
ATOM   6596 C  CD2  . LEU   B 1 281 ? -10.551 -18.687 -32.368 1.00 52.31  ?  283 LEU   I CD2  1 
ATOM   6597 N  N    . LEU   B 1 282 ? -8.595  -22.416 -34.648 1.00 37.72  ?  284 LEU   I N    1 
ATOM   6598 C  CA   . LEU   B 1 282 ? -9.387  -23.206 -35.593 1.00 34.36  ?  284 LEU   I CA   1 
ATOM   6599 C  C    . LEU   B 1 282 ? -9.193  -24.719 -35.515 1.00 31.13  ?  284 LEU   I C    1 
ATOM   6600 O  O    . LEU   B 1 282 ? -10.179 -25.421 -35.607 1.00 26.79  ?  284 LEU   I O    1 
ATOM   6601 C  CB   . LEU   B 1 282 ? -9.138  -22.748 -37.030 1.00 32.75  ?  284 LEU   I CB   1 
ATOM   6602 C  CG   . LEU   B 1 282 ? -10.045 -23.381 -38.083 1.00 34.01  ?  284 LEU   I CG   1 
ATOM   6603 C  CD1  . LEU   B 1 282 ? -11.526 -23.161 -37.794 1.00 34.40  ?  284 LEU   I CD1  1 
ATOM   6604 C  CD2  . LEU   B 1 282 ? -9.708  -22.849 -39.467 1.00 35.61  ?  284 LEU   I CD2  1 
ATOM   6605 N  N    . GLU   B 1 283 ? -7.945  -25.195 -35.384 1.00 30.33  ?  285 GLU   I N    1 
ATOM   6606 C  CA   . GLU   B 1 283 ? -7.641  -26.643 -35.305 1.00 31.53  ?  285 GLU   I CA   1 
ATOM   6607 C  C    . GLU   B 1 283 ? -7.607  -27.221 -33.879 1.00 28.64  ?  285 GLU   I C    1 
ATOM   6608 O  O    . GLU   B 1 283 ? -7.576  -28.472 -33.697 1.00 28.16  ?  285 GLU   I O    1 
ATOM   6609 C  CB   . GLU   B 1 283 ? -6.283  -26.938 -35.965 1.00 37.75  ?  285 GLU   I CB   1 
ATOM   6610 C  CG   . GLU   B 1 283 ? -6.328  -27.008 -37.489 1.00 44.72  ?  285 GLU   I CG   1 
ATOM   6611 C  CD   . GLU   B 1 283 ? -5.118  -26.351 -38.133 1.00 50.12  ?  285 GLU   I CD   1 
ATOM   6612 O  OE1  . GLU   B 1 283 ? -3.976  -26.728 -37.775 1.00 54.94  ?  285 GLU   I OE1  1 
ATOM   6613 O  OE2  . GLU   B 1 283 ? -5.315  -25.442 -38.985 1.00 55.54  ?  285 GLU   I OE2  1 
ATOM   6614 N  N    . LYS   B 1 284 ? -7.609  -26.344 -32.876 1.00 26.39  ?  286 LYS   I N    1 
ATOM   6615 C  CA   . LYS   B 1 284 ? -7.364  -26.769 -31.480 1.00 27.40  ?  286 LYS   I CA   1 
ATOM   6616 C  C    . LYS   B 1 284 ? -8.282  -27.878 -30.992 1.00 25.98  ?  286 LYS   I C    1 
ATOM   6617 O  O    . LYS   B 1 284 ? -7.817  -28.965 -30.640 1.00 23.81  ?  286 LYS   I O    1 
ATOM   6618 C  CB   . LYS   B 1 284 ? -7.492  -25.605 -30.510 1.00 28.16  ?  286 LYS   I CB   1 
ATOM   6619 C  CG   . LYS   B 1 284 ? -6.175  -25.012 -30.091 1.00 30.42  ?  286 LYS   I CG   1 
ATOM   6620 C  CD   . LYS   B 1 284 ? -6.261  -24.493 -28.672 1.00 31.28  ?  286 LYS   I CD   1 
ATOM   6621 C  CE   . LYS   B 1 284 ? -4.976  -23.768 -28.317 1.00 33.44  ?  286 LYS   I CE   1 
ATOM   6622 N  NZ   . LYS   B 1 284 ? -5.035  -22.321 -28.603 1.00 33.40  ?  286 LYS   I NZ   1 
ATOM   6623 N  N    . SER   B 1 285 ? -9.580  -27.591 -30.973 1.00 27.11  ?  287 SER   I N    1 
ATOM   6624 C  CA   . SER   B 1 285 ? -10.552 -28.524 -30.422 1.00 30.09  ?  287 SER   I CA   1 
ATOM   6625 C  C    . SER   B 1 285 ? -10.610 -29.819 -31.234 1.00 31.02  ?  287 SER   I C    1 
ATOM   6626 O  O    . SER   B 1 285 ? -10.843 -30.861 -30.658 1.00 30.60  ?  287 SER   I O    1 
ATOM   6627 C  CB   . SER   B 1 285 ? -11.939 -27.880 -30.277 1.00 29.86  ?  287 SER   I CB   1 
ATOM   6628 O  OG   . SER   B 1 285 ? -12.425 -27.428 -31.514 1.00 33.11  ?  287 SER   I OG   1 
ATOM   6629 N  N    . HIS   B 1 286 ? -10.377 -29.738 -32.558 1.00 31.73  ?  288 HIS   I N    1 
ATOM   6630 C  CA   . HIS   B 1 286 ? -10.307 -30.899 -33.429 1.00 31.75  ?  288 HIS   I CA   1 
ATOM   6631 C  C    . HIS   B 1 286 ? -9.121  -31.762 -33.033 1.00 28.81  ?  288 HIS   I C    1 
ATOM   6632 O  O    . HIS   B 1 286 ? -9.273  -32.972 -32.865 1.00 26.86  ?  288 HIS   I O    1 
ATOM   6633 C  CB   . HIS   B 1 286 ? -10.243 -30.443 -34.908 1.00 38.08  ?  288 HIS   I CB   1 
ATOM   6634 C  CG   . HIS   B 1 286 ? -9.838  -31.504 -35.886 1.00 38.74  ?  288 HIS   I CG   1 
ATOM   6635 N  ND1  . HIS   B 1 286 ? -10.710 -32.465 -36.348 1.00 43.86  ?  288 HIS   I ND1  1 
ATOM   6636 C  CD2  . HIS   B 1 286 ? -8.670  -31.708 -36.546 1.00 45.99  ?  288 HIS   I CD2  1 
ATOM   6637 C  CE1  . HIS   B 1 286 ? -10.088 -33.242 -37.219 1.00 43.32  ?  288 HIS   I CE1  1 
ATOM   6638 N  NE2  . HIS   B 1 286 ? -8.846  -32.807 -37.352 1.00 46.45  ?  288 HIS   I NE2  1 
ATOM   6639 N  N    . CYS   B 1 287 ? -7.948  -31.160 -32.869 1.00 26.45  ?  289 CYS   I N    1 
ATOM   6640 C  CA   . CYS   B 1 287 ? -6.749  -31.920 -32.416 1.00 30.08  ?  289 CYS   I CA   1 
ATOM   6641 C  C    . CYS   B 1 287 ? -6.943  -32.609 -31.049 1.00 29.09  ?  289 CYS   I C    1 
ATOM   6642 O  O    . CYS   B 1 287 ? -6.630  -33.815 -30.866 1.00 27.08  ?  289 CYS   I O    1 
ATOM   6643 C  CB   . CYS   B 1 287 ? -5.511  -31.004 -32.311 1.00 33.00  ?  289 CYS   I CB   1 
ATOM   6644 S  SG   . CYS   B 1 287 ? -3.962  -31.893 -32.076 1.00 38.28  ?  289 CYS   I SG   1 
ATOM   6645 N  N    . ILE   B 1 288 ? -7.435  -31.840 -30.083 1.00 26.80  ?  290 ILE   I N    1 
ATOM   6646 C  CA   . ILE   B 1 288 ? -7.666  -32.403 -28.750 1.00 27.66  ?  290 ILE   I CA   1 
ATOM   6647 C  C    . ILE   B 1 288 ? -8.657  -33.579 -28.843 1.00 28.53  ?  290 ILE   I C    1 
ATOM   6648 O  O    . ILE   B 1 288 ? -8.418  -34.608 -28.183 1.00 26.13  ?  290 ILE   I O    1 
ATOM   6649 C  CB   . ILE   B 1 288 ? -8.134  -31.349 -27.741 1.00 27.61  ?  290 ILE   I CB   1 
ATOM   6650 C  CG1  . ILE   B 1 288 ? -7.026  -30.316 -27.533 1.00 26.40  ?  290 ILE   I CG1  1 
ATOM   6651 C  CG2  . ILE   B 1 288 ? -8.524  -31.973 -26.397 1.00 26.44  ?  290 ILE   I CG2  1 
ATOM   6652 C  CD1  . ILE   B 1 288 ? -7.562  -28.968 -27.106 1.00 26.39  ?  290 ILE   I CD1  1 
ATOM   6653 N  N    . ALA   B 1 289 ? -9.697  -33.458 -29.702 1.00 26.05  ?  291 ALA   I N    1 
ATOM   6654 C  CA   . ALA   B 1 289 ? -10.734 -34.507 -29.820 1.00 27.69  ?  291 ALA   I CA   1 
ATOM   6655 C  C    . ALA   B 1 289 ? -10.191 -35.851 -30.303 1.00 28.74  ?  291 ALA   I C    1 
ATOM   6656 O  O    . ALA   B 1 289 ? -10.742 -36.906 -29.971 1.00 29.88  ?  291 ALA   I O    1 
ATOM   6657 C  CB   . ALA   B 1 289 ? -11.895 -34.042 -30.683 1.00 26.62  ?  291 ALA   I CB   1 
ATOM   6658 N  N    . GLU   B 1 290 ? -9.077  -35.780 -31.024 1.00 31.87  ?  292 GLU   I N    1 
ATOM   6659 C  CA   . GLU   B 1 290 ? -8.354  -36.919 -31.597 1.00 36.60  ?  292 GLU   I CA   1 
ATOM   6660 C  C    . GLU   B 1 290 ? -7.064  -37.335 -30.879 1.00 33.31  ?  292 GLU   I C    1 
ATOM   6661 O  O    . GLU   B 1 290 ? -6.448  -38.298 -31.298 1.00 31.74  ?  292 GLU   I O    1 
ATOM   6662 C  CB   . GLU   B 1 290 ? -7.936  -36.573 -33.046 1.00 41.25  ?  292 GLU   I CB   1 
ATOM   6663 C  CG   . GLU   B 1 290 ? -8.832  -37.123 -34.138 1.00 46.99  ?  292 GLU   I CG   1 
ATOM   6664 C  CD   . GLU   B 1 290 ? -8.263  -36.816 -35.502 1.00 48.43  ?  292 GLU   I CD   1 
ATOM   6665 O  OE1  . GLU   B 1 290 ? -7.918  -35.630 -35.736 1.00 55.36  ?  292 GLU   I OE1  1 
ATOM   6666 O  OE2  . GLU   B 1 290 ? -8.133  -37.757 -36.314 1.00 51.91  ?  292 GLU   I OE2  1 
ATOM   6667 N  N    . VAL   B 1 291 ? -6.619  -36.628 -29.848 1.00 29.97  ?  293 VAL   I N    1 
ATOM   6668 C  CA   . VAL   B 1 291 ? -5.313  -36.953 -29.255 1.00 31.34  ?  293 VAL   I CA   1 
ATOM   6669 C  C    . VAL   B 1 291 ? -5.273  -38.411 -28.732 1.00 31.17  ?  293 VAL   I C    1 
ATOM   6670 O  O    . VAL   B 1 291 ? -6.313  -38.971 -28.330 1.00 27.18  ?  293 VAL   I O    1 
ATOM   6671 C  CB   . VAL   B 1 291 ? -4.913  -35.964 -28.140 1.00 33.10  ?  293 VAL   I CB   1 
ATOM   6672 C  CG1  . VAL   B 1 291 ? -5.777  -36.145 -26.885 1.00 34.20  ?  293 VAL   I CG1  1 
ATOM   6673 C  CG2  . VAL   B 1 291 ? -3.432  -36.086 -27.805 1.00 33.94  ?  293 VAL   I CG2  1 
ATOM   6674 N  N    . GLU   B 1 292 ? -4.068  -38.987 -28.761 1.00 32.75  ?  294 GLU   I N    1 
ATOM   6675 C  CA   . GLU   B 1 292 ? -3.793  -40.370 -28.338 1.00 34.67  ?  294 GLU   I CA   1 
ATOM   6676 C  C    . GLU   B 1 292 ? -3.949  -40.405 -26.802 1.00 31.30  ?  294 GLU   I C    1 
ATOM   6677 O  O    . GLU   B 1 292 ? -3.695  -39.412 -26.108 1.00 28.82  ?  294 GLU   I O    1 
ATOM   6678 C  CB   . GLU   B 1 292 ? -2.364  -40.826 -28.807 1.00 38.52  ?  294 GLU   I CB   1 
ATOM   6679 C  CG   . GLU   B 1 292 ? -2.227  -42.264 -29.355 1.00 45.41  ?  294 GLU   I CG   1 
ATOM   6680 C  CD   . GLU   B 1 292 ? -0.851  -42.607 -30.050 1.00 50.75  ?  294 GLU   I CD   1 
ATOM   6681 O  OE1  . GLU   B 1 292 ? -0.161  -41.744 -30.664 1.00 50.12  ?  294 GLU   I OE1  1 
ATOM   6682 O  OE2  . GLU   B 1 292 ? -0.439  -43.791 -30.011 1.00 50.87  ?  294 GLU   I OE2  1 
ATOM   6683 N  N    . ASN   B 1 293 ? -4.422  -41.543 -26.310 1.00 29.66  ?  295 ASN   I N    1 
ATOM   6684 C  CA   . ASN   B 1 293 ? -4.523  -41.849 -24.888 1.00 27.54  ?  295 ASN   I CA   1 
ATOM   6685 C  C    . ASN   B 1 293 ? -3.177  -41.578 -24.218 1.00 27.60  ?  295 ASN   I C    1 
ATOM   6686 O  O    . ASN   B 1 293 ? -2.153  -42.025 -24.747 1.00 29.66  ?  295 ASN   I O    1 
ATOM   6687 C  CB   . ASN   B 1 293 ? -4.818  -43.345 -24.695 1.00 27.44  ?  295 ASN   I CB   1 
ATOM   6688 C  CG   . ASN   B 1 293 ? -6.207  -43.750 -25.109 1.00 27.45  ?  295 ASN   I CG   1 
ATOM   6689 O  OD1  . ASN   B 1 293 ? -7.049  -42.925 -25.486 1.00 25.53  ?  295 ASN   I OD1  1 
ATOM   6690 N  ND2  . ASN   B 1 293 ? -6.469  -45.055 -25.007 1.00 25.98  ?  295 ASN   I ND2  1 
ATOM   6691 N  N    . ASP   B 1 294 ? -3.173  -40.885 -23.075 1.00 25.87  ?  296 ASP   I N    1 
ATOM   6692 C  CA   . ASP   B 1 294 ? -1.970  -40.699 -22.271 1.00 27.20  ?  296 ASP   I CA   1 
ATOM   6693 C  C    . ASP   B 1 294 ? -1.616  -42.089 -21.688 1.00 30.18  ?  296 ASP   I C    1 
ATOM   6694 O  O    . ASP   B 1 294 ? -2.401  -43.017 -21.798 1.00 25.98  ?  296 ASP   I O    1 
ATOM   6695 C  CB   . ASP   B 1 294 ? -2.255  -39.693 -21.161 1.00 27.64  ?  296 ASP   I CB   1 
ATOM   6696 C  CG   . ASP   B 1 294 ? -0.987  -39.102 -20.489 1.00 26.59  ?  296 ASP   I CG   1 
ATOM   6697 O  OD1  . ASP   B 1 294 ? 0.149   -39.425 -20.873 1.00 28.13  ?  296 ASP   I OD1  1 
ATOM   6698 O  OD2  . ASP   B 1 294 ? -1.166  -38.306 -19.532 1.00 23.43  ?  296 ASP   I OD2  1 
ATOM   6699 N  N    . GLU   B 1 295 ? -0.436  -42.248 -21.097 1.00 34.25  ?  297 GLU   I N    1 
ATOM   6700 C  CA   . GLU   B 1 295 ? -0.098  -43.548 -20.492 1.00 36.80  ?  297 GLU   I CA   1 
ATOM   6701 C  C    . GLU   B 1 295 ? -0.733  -43.595 -19.120 1.00 35.12  ?  297 GLU   I C    1 
ATOM   6702 O  O    . GLU   B 1 295 ? -0.816  -42.576 -18.457 1.00 33.15  ?  297 GLU   I O    1 
ATOM   6703 C  CB   . GLU   B 1 295 ? 1.414   -43.756 -20.412 1.00 38.69  ?  297 GLU   I CB   1 
ATOM   6704 C  CG   . GLU   B 1 295 ? 1.831   -45.231 -20.461 1.00 43.61  ?  297 GLU   I CG   1 
ATOM   6705 C  CD   . GLU   B 1 295 ? 3.122   -45.488 -21.252 1.00 50.17  ?  297 GLU   I CD   1 
ATOM   6706 O  OE1  . GLU   B 1 295 ? 3.353   -44.805 -22.308 1.00 49.74  ?  297 GLU   I OE1  1 
ATOM   6707 O  OE2  . GLU   B 1 295 ? 3.887   -46.399 -20.823 1.00 52.13  ?  297 GLU   I OE2  1 
ATOM   6708 N  N    . MET   B 1 296 ? -1.223  -44.758 -18.706 1.00 36.11  ?  298 MET   I N    1 
ATOM   6709 C  CA   . MET   B 1 296 ? -1.827  -44.847 -17.388 1.00 38.74  ?  298 MET   I CA   1 
ATOM   6710 C  C    . MET   B 1 296 ? -0.699  -44.790 -16.358 1.00 38.44  ?  298 MET   I C    1 
ATOM   6711 O  O    . MET   B 1 296 ? 0.407   -45.256 -16.637 1.00 38.47  ?  298 MET   I O    1 
ATOM   6712 C  CB   . MET   B 1 296 ? -2.723  -46.085 -17.233 1.00 39.98  ?  298 MET   I CB   1 
ATOM   6713 C  CG   . MET   B 1 296 ? -2.033  -47.411 -17.067 1.00 41.27  ?  298 MET   I CG   1 
ATOM   6714 S  SD   . MET   B 1 296 ? -3.215  -48.759 -16.784 1.00 46.39  ?  298 MET   I SD   1 
ATOM   6715 C  CE   . MET   B 1 296 ? -2.193  -49.792 -15.701 1.00 50.52  ?  298 MET   I CE   1 
ATOM   6716 N  N    . PRO   B 1 297 ? -0.957  -44.191 -15.181 1.00 40.09  ?  299 PRO   I N    1 
ATOM   6717 C  CA   . PRO   B 1 297 ? 0.092   -44.203 -14.151 1.00 39.79  ?  299 PRO   I CA   1 
ATOM   6718 C  C    . PRO   B 1 297 ? 0.515   -45.639 -13.809 1.00 38.75  ?  299 PRO   I C    1 
ATOM   6719 O  O    . PRO   B 1 297 ? -0.331  -46.530 -13.762 1.00 35.60  ?  299 PRO   I O    1 
ATOM   6720 C  CB   . PRO   B 1 297 ? -0.566  -43.503 -12.937 1.00 40.13  ?  299 PRO   I CB   1 
ATOM   6721 C  CG   . PRO   B 1 297 ? -1.817  -42.872 -13.441 1.00 40.36  ?  299 PRO   I CG   1 
ATOM   6722 C  CD   . PRO   B 1 297 ? -2.211  -43.559 -14.715 1.00 38.99  ?  299 PRO   I CD   1 
ATOM   6723 N  N    . ALA   B 1 298 ? 1.813   -45.850 -13.595 1.00 41.30  ?  300 ALA   I N    1 
ATOM   6724 C  CA   . ALA   B 1 298 ? 2.360   -47.190 -13.401 1.00 48.54  ?  300 ALA   I CA   1 
ATOM   6725 C  C    . ALA   B 1 298 ? 1.683   -47.903 -12.241 1.00 50.28  ?  300 ALA   I C    1 
ATOM   6726 O  O    . ALA   B 1 298 ? 1.090   -48.980 -12.412 1.00 56.70  ?  300 ALA   I O    1 
ATOM   6727 C  CB   . ALA   B 1 298 ? 3.865   -47.123 -13.172 1.00 49.74  ?  300 ALA   I CB   1 
ATOM   6728 N  N    . ASP   B 1 299 ? 1.754   -47.274 -11.075 1.00 49.94  ?  301 ASP   I N    1 
ATOM   6729 C  CA   . ASP   B 1 299 ? 1.158   -47.806 -9.861  1.00 51.98  ?  301 ASP   I CA   1 
ATOM   6730 C  C    . ASP   B 1 299 ? -0.325  -47.525 -9.921  1.00 51.91  ?  301 ASP   I C    1 
ATOM   6731 O  O    . ASP   B 1 299 ? -0.713  -46.349 -9.879  1.00 51.94  ?  301 ASP   I O    1 
ATOM   6732 C  CB   . ASP   B 1 299 ? 1.743   -47.103 -8.634  1.00 56.46  ?  301 ASP   I CB   1 
ATOM   6733 N  N    . LEU   B 1 300 ? -1.137  -48.578 -10.067 1.00 45.13  ?  302 LEU   I N    1 
ATOM   6734 C  CA   . LEU   B 1 300 ? -2.589  -48.455 -9.966  1.00 42.26  ?  302 LEU   I CA   1 
ATOM   6735 C  C    . LEU   B 1 300 ? -3.130  -49.670 -9.227  1.00 43.37  ?  302 LEU   I C    1 
ATOM   6736 O  O    . LEU   B 1 300 ? -2.961  -50.799 -9.700  1.00 44.77  ?  302 LEU   I O    1 
ATOM   6737 C  CB   . LEU   B 1 300 ? -3.275  -48.381 -11.326 1.00 38.68  ?  302 LEU   I CB   1 
ATOM   6738 C  CG   . LEU   B 1 300 ? -3.432  -47.071 -12.110 1.00 37.47  ?  302 LEU   I CG   1 
ATOM   6739 C  CD1  . LEU   B 1 300 ? -4.621  -47.277 -13.051 1.00 37.25  ?  302 LEU   I CD1  1 
ATOM   6740 C  CD2  . LEU   B 1 300 ? -3.593  -45.807 -11.269 1.00 35.71  ?  302 LEU   I CD2  1 
ATOM   6741 N  N    . PRO   B 1 301 ? -3.766  -49.443 -8.069  1.00 41.01  ?  303 PRO   I N    1 
ATOM   6742 C  CA   . PRO   B 1 301 ? -4.358  -50.526 -7.279  1.00 40.96  ?  303 PRO   I CA   1 
ATOM   6743 C  C    . PRO   B 1 301 ? -5.546  -51.229 -7.912  1.00 40.19  ?  303 PRO   I C    1 
ATOM   6744 O  O    . PRO   B 1 301 ? -6.144  -50.722 -8.864  1.00 36.16  ?  303 PRO   I O    1 
ATOM   6745 C  CB   . PRO   B 1 301 ? -4.825  -49.814 -5.994  1.00 42.94  ?  303 PRO   I CB   1 
ATOM   6746 C  CG   . PRO   B 1 301 ? -4.003  -48.569 -5.902  1.00 41.88  ?  303 PRO   I CG   1 
ATOM   6747 C  CD   . PRO   B 1 301 ? -3.657  -48.182 -7.302  1.00 41.14  ?  303 PRO   I CD   1 
ATOM   6748 N  N    . SER   B 1 302 ? -5.886  -52.392 -7.349  1.00 37.79  ?  304 SER   I N    1 
ATOM   6749 C  CA   . SER   B 1 302 ? -7.125  -53.080 -7.678  1.00 35.91  ?  304 SER   I CA   1 
ATOM   6750 C  C    . SER   B 1 302 ? -8.318  -52.200 -7.345  1.00 33.13  ?  304 SER   I C    1 
ATOM   6751 O  O    . SER   B 1 302 ? -8.257  -51.371 -6.449  1.00 36.90  ?  304 SER   I O    1 
ATOM   6752 C  CB   . SER   B 1 302 ? -7.288  -54.399 -6.900  1.00 34.59  ?  304 SER   I CB   1 
ATOM   6753 O  OG   . SER   B 1 302 ? -8.638  -54.910 -7.041  1.00 35.70  ?  304 SER   I OG   1 
ATOM   6754 N  N    . LEU   B 1 303 ? -9.409  -52.413 -8.053  1.00 32.38  ?  305 LEU   I N    1 
ATOM   6755 C  CA   . LEU   B 1 303 ? -10.664 -51.703 -7.771  1.00 32.67  ?  305 LEU   I CA   1 
ATOM   6756 C  C    . LEU   B 1 303 ? -11.473 -52.351 -6.634  1.00 30.88  ?  305 LEU   I C    1 
ATOM   6757 O  O    . LEU   B 1 303 ? -12.462 -51.766 -6.170  1.00 26.42  ?  305 LEU   I O    1 
ATOM   6758 C  CB   . LEU   B 1 303 ? -11.516 -51.689 -9.042  1.00 34.39  ?  305 LEU   I CB   1 
ATOM   6759 C  CG   . LEU   B 1 303 ? -10.902 -50.949 -10.241 1.00 35.69  ?  305 LEU   I CG   1 
ATOM   6760 C  CD1  . LEU   B 1 303 ? -11.219 -51.608 -11.576 1.00 37.16  ?  305 LEU   I CD1  1 
ATOM   6761 C  CD2  . LEU   B 1 303 ? -11.365 -49.527 -10.256 1.00 35.62  ?  305 LEU   I CD2  1 
ATOM   6762 N  N    . ALA   B 1 304 ? -11.094 -53.566 -6.218  1.00 28.10  ?  306 ALA   I N    1 
ATOM   6763 C  CA   . ALA   B 1 304 ? -11.860 -54.295 -5.210  1.00 27.40  ?  306 ALA   I CA   1 
ATOM   6764 C  C    . ALA   B 1 304 ? -11.871 -53.578 -3.877  1.00 26.73  ?  306 ALA   I C    1 
ATOM   6765 O  O    . ALA   B 1 304 ? -12.900 -53.576 -3.197  1.00 31.13  ?  306 ALA   I O    1 
ATOM   6766 C  CB   . ALA   B 1 304 ? -11.364 -55.743 -5.050  1.00 29.43  ?  306 ALA   I CB   1 
ATOM   6767 N  N    . ALA   B 1 305 ? -10.784 -52.916 -3.514  1.00 25.71  ?  307 ALA   I N    1 
ATOM   6768 C  CA   . ALA   B 1 305 ? -10.752 -52.115 -2.267  1.00 27.95  ?  307 ALA   I CA   1 
ATOM   6769 C  C    . ALA   B 1 305 ? -11.931 -51.146 -2.161  1.00 28.82  ?  307 ALA   I C    1 
ATOM   6770 O  O    . ALA   B 1 305 ? -12.701 -51.217 -1.213  1.00 31.99  ?  307 ALA   I O    1 
ATOM   6771 C  CB   . ALA   B 1 305 ? -9.424  -51.340 -2.108  1.00 27.46  ?  307 ALA   I CB   1 
ATOM   6772 N  N    . ASP   B 1 306 ? -12.071 -50.277 -3.154  1.00 31.13  ?  308 ASP   I N    1 
ATOM   6773 C  CA   . ASP   B 1 306 ? -13.077 -49.207 -3.131  1.00 29.92  ?  308 ASP   I CA   1 
ATOM   6774 C  C    . ASP   B 1 306 ? -14.472 -49.651 -3.566  1.00 27.86  ?  308 ASP   I C    1 
ATOM   6775 O  O    . ASP   B 1 306 ? -15.456 -49.152 -3.053  1.00 28.67  ?  308 ASP   I O    1 
ATOM   6776 C  CB   . ASP   B 1 306 ? -12.595 -48.036 -3.987  1.00 33.71  ?  308 ASP   I CB   1 
ATOM   6777 C  CG   . ASP   B 1 306 ? -11.639 -47.129 -3.247  1.00 37.12  ?  308 ASP   I CG   1 
ATOM   6778 O  OD1  . ASP   B 1 306 ? -10.880 -47.588 -2.368  1.00 40.43  ?  308 ASP   I OD1  1 
ATOM   6779 O  OD2  . ASP   B 1 306 ? -11.644 -45.918 -3.543  1.00 43.36  ?  308 ASP   I OD2  1 
ATOM   6780 N  N    . PHE   B 1 307 ? -14.567 -50.616 -4.480  1.00 27.39  ?  309 PHE   I N    1 
ATOM   6781 C  CA   . PHE   B 1 307 ? -15.838 -50.983 -5.113  1.00 24.18  ?  309 PHE   I CA   1 
ATOM   6782 C  C    . PHE   B 1 307 ? -16.459 -52.352 -4.757  1.00 24.40  ?  309 PHE   I C    1 
ATOM   6783 O  O    . PHE   B 1 307 ? -17.636 -52.594 -5.062  1.00 20.96  ?  309 PHE   I O    1 
ATOM   6784 C  CB   . PHE   B 1 307 ? -15.658 -50.781 -6.606  1.00 24.24  ?  309 PHE   I CB   1 
ATOM   6785 C  CG   . PHE   B 1 307 ? -15.338 -49.350 -6.962  1.00 22.54  ?  309 PHE   I CG   1 
ATOM   6786 C  CD1  . PHE   B 1 307 ? -16.328 -48.366 -6.914  1.00 22.85  ?  309 PHE   I CD1  1 
ATOM   6787 C  CD2  . PHE   B 1 307 ? -14.064 -48.975 -7.313  1.00 23.36  ?  309 PHE   I CD2  1 
ATOM   6788 C  CE1  . PHE   B 1 307 ? -16.054 -47.037 -7.245  1.00 21.15  ?  309 PHE   I CE1  1 
ATOM   6789 C  CE2  . PHE   B 1 307 ? -13.777 -47.636 -7.617  1.00 23.01  ?  309 PHE   I CE2  1 
ATOM   6790 C  CZ   . PHE   B 1 307 ? -14.769 -46.674 -7.587  1.00 20.62  ?  309 PHE   I CZ   1 
ATOM   6791 N  N    . VAL   B 1 308 ? -15.702 -53.204 -4.055  1.00 26.25  ?  310 VAL   I N    1 
ATOM   6792 C  CA   . VAL   B 1 308 ? -16.215 -54.505 -3.538  1.00 28.18  ?  310 VAL   I CA   1 
ATOM   6793 C  C    . VAL   B 1 308 ? -15.927 -54.718 -2.038  1.00 30.83  ?  310 VAL   I C    1 
ATOM   6794 O  O    . VAL   B 1 308 ? -16.867 -54.937 -1.241  1.00 26.53  ?  310 VAL   I O    1 
ATOM   6795 C  CB   . VAL   B 1 308 ? -15.616 -55.686 -4.319  1.00 28.67  ?  310 VAL   I CB   1 
ATOM   6796 C  CG1  . VAL   B 1 308 ? -16.227 -57.027 -3.870  1.00 28.36  ?  310 VAL   I CG1  1 
ATOM   6797 C  CG2  . VAL   B 1 308 ? -15.790 -55.483 -5.834  1.00 29.55  ?  310 VAL   I CG2  1 
ATOM   6798 N  N    . GLU   B 1 309 ? -14.633 -54.662 -1.682  1.00 33.70  ?  311 GLU   I N    1 
ATOM   6799 C  CA   . GLU   B 1 309 ? -14.143 -54.941 -0.319  1.00 39.05  ?  311 GLU   I CA   1 
ATOM   6800 C  C    . GLU   B 1 309 ? -14.609 -53.973 0.751   1.00 38.98  ?  311 GLU   I C    1 
ATOM   6801 O  O    . GLU   B 1 309 ? -15.070 -54.395 1.822   1.00 37.21  ?  311 GLU   I O    1 
ATOM   6802 C  CB   . GLU   B 1 309 ? -12.614 -54.973 -0.296  1.00 42.83  ?  311 GLU   I CB   1 
ATOM   6803 C  CG   . GLU   B 1 309 ? -12.032 -56.183 -1.040  1.00 47.78  ?  311 GLU   I CG   1 
ATOM   6804 C  CD   . GLU   B 1 309 ? -10.528 -56.084 -1.301  1.00 48.20  ?  311 GLU   I CD   1 
ATOM   6805 O  OE1  . GLU   B 1 309 ? -9.927  -55.010 -1.111  1.00 53.70  ?  311 GLU   I OE1  1 
ATOM   6806 O  OE2  . GLU   B 1 309 ? -9.931  -57.095 -1.723  1.00 52.27  ?  311 GLU   I OE2  1 
ATOM   6807 N  N    . SER   B 1 310 ? -14.460 -52.681 0.461   1.00 39.98  ?  312 SER   I N    1 
ATOM   6808 C  CA   . SER   B 1 310 ? -14.768 -51.612 1.407   1.00 38.60  ?  312 SER   I CA   1 
ATOM   6809 C  C    . SER   B 1 310 ? -16.128 -51.801 2.037   1.00 39.76  ?  312 SER   I C    1 
ATOM   6810 O  O    . SER   B 1 310 ? -17.113 -52.072 1.335   1.00 37.09  ?  312 SER   I O    1 
ATOM   6811 C  CB   . SER   B 1 310 ? -14.712 -50.244 0.709   1.00 40.45  ?  312 SER   I CB   1 
ATOM   6812 O  OG   . SER   B 1 310 ? -15.417 -49.242 1.393   1.00 37.91  ?  312 SER   I OG   1 
ATOM   6813 N  N    . LYS   B 1 311 ? -16.154 -51.746 3.375   1.00 38.70  ?  313 LYS   I N    1 
ATOM   6814 C  CA   . LYS   B 1 311 ? -17.353 -51.364 4.103   1.00 38.61  ?  313 LYS   I CA   1 
ATOM   6815 C  C    . LYS   B 1 311 ? -17.500 -49.883 3.713   1.00 38.35  ?  313 LYS   I C    1 
ATOM   6816 O  O    . LYS   B 1 311 ? -16.485 -49.186 3.586   1.00 40.72  ?  313 LYS   I O    1 
ATOM   6817 C  CB   . LYS   B 1 311 ? -17.160 -51.528 5.621   1.00 37.56  ?  313 LYS   I CB   1 
ATOM   6818 N  N    . ASP   B 1 312 ? -18.724 -49.422 3.482   1.00 35.65  ?  314 ASP   I N    1 
ATOM   6819 C  CA   . ASP   B 1 312 ? -18.995 -48.062 2.917   1.00 36.22  ?  314 ASP   I CA   1 
ATOM   6820 C  C    . ASP   B 1 312 ? -19.411 -48.071 1.431   1.00 35.72  ?  314 ASP   I C    1 
ATOM   6821 O  O    . ASP   B 1 312 ? -19.665 -47.002 0.860   1.00 37.19  ?  314 ASP   I O    1 
ATOM   6822 C  CB   . ASP   B 1 312 ? -17.800 -47.084 3.092   1.00 33.47  ?  314 ASP   I CB   1 
ATOM   6823 N  N    . VAL   B 1 313 ? -19.487 -49.244 0.799   1.00 32.58  ?  315 VAL   I N    1 
ATOM   6824 C  CA   . VAL   B 1 313 ? -19.750 -49.291 -0.639  1.00 30.38  ?  315 VAL   I CA   1 
ATOM   6825 C  C    . VAL   B 1 313 ? -21.145 -48.724 -0.873  1.00 29.56  ?  315 VAL   I C    1 
ATOM   6826 O  O    . VAL   B 1 313 ? -21.321 -47.821 -1.702  1.00 28.39  ?  315 VAL   I O    1 
ATOM   6827 C  CB   . VAL   B 1 313 ? -19.528 -50.723 -1.234  1.00 29.30  ?  315 VAL   I CB   1 
ATOM   6828 C  CG1  . VAL   B 1 313 ? -20.378 -51.000 -2.458  1.00 28.71  ?  315 VAL   I CG1  1 
ATOM   6829 C  CG2  . VAL   B 1 313 ? -18.044 -50.947 -1.567  1.00 27.40  ?  315 VAL   I CG2  1 
ATOM   6830 N  N    . CYS   B 1 314 ? -22.108 -49.244 -0.110  1.00 28.08  ?  316 CYS   I N    1 
ATOM   6831 C  CA   . CYS   B 1 314 ? -23.507 -48.875 -0.237  1.00 29.75  ?  316 CYS   I CA   1 
ATOM   6832 C  C    . CYS   B 1 314 ? -23.751 -47.479 0.296   1.00 27.89  ?  316 CYS   I C    1 
ATOM   6833 O  O    . CYS   B 1 314 ? -24.611 -46.806 -0.222  1.00 26.36  ?  316 CYS   I O    1 
ATOM   6834 C  CB   . CYS   B 1 314 ? -24.421 -49.883 0.457   1.00 30.78  ?  316 CYS   I CB   1 
ATOM   6835 S  SG   . CYS   B 1 314 ? -24.455 -51.505 -0.379  1.00 37.39  ?  316 CYS   I SG   1 
ATOM   6836 N  N    . LYS   B 1 315 ? -22.997 -47.068 1.320   1.00 28.35  ?  317 LYS   I N    1 
ATOM   6837 C  CA   . LYS   B 1 315 ? -23.122 -45.719 1.902   1.00 29.63  ?  317 LYS   I CA   1 
ATOM   6838 C  C    . LYS   B 1 315 ? -22.596 -44.670 0.903   1.00 28.36  ?  317 LYS   I C    1 
ATOM   6839 O  O    . LYS   B 1 315 ? -23.248 -43.665 0.672   1.00 26.71  ?  317 LYS   I O    1 
ATOM   6840 C  CB   . LYS   B 1 315 ? -22.410 -45.613 3.261   1.00 30.15  ?  317 LYS   I CB   1 
ATOM   6841 N  N    . ASN   B 1 316 ? -21.403 -44.924 0.364   1.00 26.79  ?  318 ASN   I N    1 
ATOM   6842 C  CA   . ASN   B 1 316 ? -20.839 -44.147 -0.713  1.00 28.25  ?  318 ASN   I CA   1 
ATOM   6843 C  C    . ASN   B 1 316 ? -21.678 -44.111 -1.958  1.00 27.26  ?  318 ASN   I C    1 
ATOM   6844 O  O    . ASN   B 1 316 ? -21.793 -43.050 -2.568  1.00 25.43  ?  318 ASN   I O    1 
ATOM   6845 C  CB   . ASN   B 1 316 ? -19.416 -44.586 -1.068  1.00 29.61  ?  318 ASN   I CB   1 
ATOM   6846 C  CG   . ASN   B 1 316 ? -18.431 -44.237 0.027   1.00 30.92  ?  318 ASN   I CG   1 
ATOM   6847 O  OD1  . ASN   B 1 316 ? -18.811 -43.588 1.003   1.00 31.16  ?  318 ASN   I OD1  1 
ATOM   6848 N  ND2  . ASN   B 1 316 ? -17.176 -44.690 -0.102  1.00 32.17  ?  318 ASN   I ND2  1 
ATOM   6849 N  N    . TYR   B 1 317 ? -22.264 -45.241 -2.320  1.00 23.99  ?  319 TYR   I N    1 
ATOM   6850 C  CA   . TYR   B 1 317 ? -23.184 -45.314 -3.445  1.00 24.31  ?  319 TYR   I CA   1 
ATOM   6851 C  C    . TYR   B 1 317 ? -24.414 -44.430 -3.242  1.00 26.35  ?  319 TYR   I C    1 
ATOM   6852 O  O    . TYR   B 1 317 ? -24.618 -43.505 -4.030  1.00 25.43  ?  319 TYR   I O    1 
ATOM   6853 C  CB   . TYR   B 1 317 ? -23.635 -46.760 -3.667  1.00 24.47  ?  319 TYR   I CB   1 
ATOM   6854 C  CG   . TYR   B 1 317 ? -24.613 -46.967 -4.786  1.00 25.39  ?  319 TYR   I CG   1 
ATOM   6855 C  CD1  . TYR   B 1 317 ? -24.315 -46.540 -6.079  1.00 28.16  ?  319 TYR   I CD1  1 
ATOM   6856 C  CD2  . TYR   B 1 317 ? -25.848 -47.581 -4.572  1.00 25.57  ?  319 TYR   I CD2  1 
ATOM   6857 C  CE1  . TYR   B 1 317 ? -25.207 -46.724 -7.124  1.00 24.82  ?  319 TYR   I CE1  1 
ATOM   6858 C  CE2  . TYR   B 1 317 ? -26.743 -47.778 -5.616  1.00 24.97  ?  319 TYR   I CE2  1 
ATOM   6859 C  CZ   . TYR   B 1 317 ? -26.412 -47.341 -6.893  1.00 26.11  ?  319 TYR   I CZ   1 
ATOM   6860 O  OH   . TYR   B 1 317 ? -27.282 -47.516 -7.972  1.00 25.46  ?  319 TYR   I OH   1 
ATOM   6861 N  N    . ALA   B 1 318 ? -25.177 -44.708 -2.165  1.00 26.53  ?  320 ALA   I N    1 
ATOM   6862 C  CA   . ALA   B 1 318 ? -26.473 -44.086 -1.879  1.00 26.05  ?  320 ALA   I CA   1 
ATOM   6863 C  C    . ALA   B 1 318 ? -26.444 -42.563 -1.662  1.00 29.00  ?  320 ALA   I C    1 
ATOM   6864 O  O    . ALA   B 1 318 ? -27.470 -41.908 -1.836  1.00 28.41  ?  320 ALA   I O    1 
ATOM   6865 C  CB   . ALA   B 1 318 ? -27.118 -44.756 -0.685  1.00 25.01  ?  320 ALA   I CB   1 
ATOM   6866 N  N    . GLU   B 1 319 ? -25.293 -42.022 -1.264  1.00 30.47  ?  321 GLU   I N    1 
ATOM   6867 C  CA   . GLU   B 1 319 ? -25.141 -40.573 -1.081  1.00 35.21  ?  321 GLU   I CA   1 
ATOM   6868 C  C    . GLU   B 1 319 ? -25.222 -39.772 -2.397  1.00 32.24  ?  321 GLU   I C    1 
ATOM   6869 O  O    . GLU   B 1 319 ? -25.736 -38.649 -2.409  1.00 32.82  ?  321 GLU   I O    1 
ATOM   6870 C  CB   . GLU   B 1 319 ? -23.837 -40.259 -0.350  1.00 37.38  ?  321 GLU   I CB   1 
ATOM   6871 C  CG   . GLU   B 1 319 ? -23.746 -38.812 0.101   1.00 45.11  ?  321 GLU   I CG   1 
ATOM   6872 C  CD   . GLU   B 1 319 ? -22.334 -38.405 0.482   1.00 52.33  ?  321 GLU   I CD   1 
ATOM   6873 O  OE1  . GLU   B 1 319 ? -21.451 -38.397 -0.427  1.00 54.29  ?  321 GLU   I OE1  1 
ATOM   6874 O  OE2  . GLU   B 1 319 ? -22.126 -38.083 1.680   1.00 50.69  ?  321 GLU   I OE2  1 
ATOM   6875 N  N    . ALA   B 1 320 ? -24.719 -40.356 -3.484  1.00 30.13  ?  322 ALA   I N    1 
ATOM   6876 C  CA   . ALA   B 1 320 ? -24.736 -39.731 -4.818  1.00 30.31  ?  322 ALA   I CA   1 
ATOM   6877 C  C    . ALA   B 1 320 ? -24.409 -40.803 -5.851  1.00 26.40  ?  322 ALA   I C    1 
ATOM   6878 O  O    . ALA   B 1 320 ? -23.265 -40.929 -6.266  1.00 22.53  ?  322 ALA   I O    1 
ATOM   6879 C  CB   . ALA   B 1 320 ? -23.716 -38.576 -4.929  1.00 30.01  ?  322 ALA   I CB   1 
ATOM   6880 N  N    . LYS   B 1 321 ? -25.441 -41.528 -6.275  1.00 26.09  ?  323 LYS   I N    1 
ATOM   6881 C  CA   . LYS   B 1 321 ? -25.289 -42.788 -7.014  1.00 28.75  ?  323 LYS   I CA   1 
ATOM   6882 C  C    . LYS   B 1 321 ? -24.514 -42.544 -8.285  1.00 28.93  ?  323 LYS   I C    1 
ATOM   6883 O  O    . LYS   B 1 321 ? -23.569 -43.281 -8.582  1.00 23.64  ?  323 LYS   I O    1 
ATOM   6884 C  CB   . LYS   B 1 321 ? -26.662 -43.441 -7.305  1.00 28.51  ?  323 LYS   I CB   1 
ATOM   6885 C  CG   . LYS   B 1 321 ? -27.442 -43.752 -6.028  1.00 29.89  ?  323 LYS   I CG   1 
ATOM   6886 C  CD   . LYS   B 1 321 ? -28.712 -44.530 -6.335  1.00 32.73  ?  323 LYS   I CD   1 
ATOM   6887 C  CE   . LYS   B 1 321 ? -29.376 -45.016 -5.061  1.00 32.68  ?  323 LYS   I CE   1 
ATOM   6888 N  NZ   . LYS   B 1 321 ? -30.713 -45.606 -5.378  1.00 32.92  ?  323 LYS   I NZ   1 
ATOM   6889 N  N    . ASP   B 1 322 ? -24.861 -41.461 -8.991  1.00 27.17  ?  324 ASP   I N    1 
ATOM   6890 C  CA   . ASP   B 1 322 ? -24.248 -41.197 -10.269 1.00 29.54  ?  324 ASP   I CA   1 
ATOM   6891 C  C    . ASP   B 1 322 ? -22.779 -40.795 -10.161 1.00 27.24  ?  324 ASP   I C    1 
ATOM   6892 O  O    . ASP   B 1 322 ? -22.024 -41.102 -11.073 1.00 29.07  ?  324 ASP   I O    1 
ATOM   6893 C  CB   . ASP   B 1 322 ? -25.106 -40.215 -11.117 1.00 33.61  ?  324 ASP   I CB   1 
ATOM   6894 C  CG   . ASP   B 1 322 ? -26.285 -40.925 -11.785 1.00 39.30  ?  324 ASP   I CG   1 
ATOM   6895 O  OD1  . ASP   B 1 322 ? -26.462 -42.135 -11.513 1.00 43.02  ?  324 ASP   I OD1  1 
ATOM   6896 O  OD2  . ASP   B 1 322 ? -27.020 -40.324 -12.618 1.00 45.55  ?  324 ASP   I OD2  1 
ATOM   6897 N  N    . VAL   B 1 323 ? -22.370 -40.134 -9.079  1.00 24.13  ?  325 VAL   I N    1 
ATOM   6898 C  CA   . VAL   B 1 323 ? -20.972 -39.763 -8.885  1.00 25.70  ?  325 VAL   I CA   1 
ATOM   6899 C  C    . VAL   B 1 323 ? -20.214 -41.045 -8.498  1.00 24.02  ?  325 VAL   I C    1 
ATOM   6900 O  O    . VAL   B 1 323 ? -19.193 -41.332 -9.066  1.00 24.13  ?  325 VAL   I O    1 
ATOM   6901 C  CB   . VAL   B 1 323 ? -20.789 -38.631 -7.847  1.00 27.97  ?  325 VAL   I CB   1 
ATOM   6902 C  CG1  . VAL   B 1 323 ? -19.364 -38.540 -7.343  1.00 29.11  ?  325 VAL   I CG1  1 
ATOM   6903 C  CG2  . VAL   B 1 323 ? -21.213 -37.278 -8.432  1.00 30.14  ?  325 VAL   I CG2  1 
ATOM   6904 N  N    . PHE   B 1 324 ? -20.752 -41.852 -7.603  1.00 23.26  ?  326 PHE   I N    1 
ATOM   6905 C  CA   . PHE   B 1 324 ? -20.116 -43.164 -7.309  1.00 20.26  ?  326 PHE   I CA   1 
ATOM   6906 C  C    . PHE   B 1 324 ? -20.007 -44.024 -8.550  1.00 18.69  ?  326 PHE   I C    1 
ATOM   6907 O  O    . PHE   B 1 324 ? -18.941 -44.493 -8.882  1.00 20.18  ?  326 PHE   I O    1 
ATOM   6908 C  CB   . PHE   B 1 324 ? -20.834 -43.895 -6.186  1.00 19.22  ?  326 PHE   I CB   1 
ATOM   6909 C  CG   . PHE   B 1 324 ? -20.032 -45.036 -5.592  1.00 19.49  ?  326 PHE   I CG   1 
ATOM   6910 C  CD1  . PHE   B 1 324 ? -18.898 -44.782 -4.834  1.00 20.07  ?  326 PHE   I CD1  1 
ATOM   6911 C  CD2  . PHE   B 1 324 ? -20.400 -46.347 -5.825  1.00 18.99  ?  326 PHE   I CD2  1 
ATOM   6912 C  CE1  . PHE   B 1 324 ? -18.166 -45.829 -4.281  1.00 21.12  ?  326 PHE   I CE1  1 
ATOM   6913 C  CE2  . PHE   B 1 324 ? -19.684 -47.391 -5.265  1.00 19.73  ?  326 PHE   I CE2  1 
ATOM   6914 C  CZ   . PHE   B 1 324 ? -18.560 -47.138 -4.528  1.00 20.12  ?  326 PHE   I CZ   1 
ATOM   6915 N  N    . LEU   B 1 325 ? -21.083 -44.175 -9.304  1.00 20.52  ?  327 LEU   I N    1 
ATOM   6916 C  CA   . LEU   B 1 325 ? -21.034 -44.965 -10.559 1.00 18.15  ?  327 LEU   I CA   1 
ATOM   6917 C  C    . LEU   B 1 325 ? -20.090 -44.338 -11.561 1.00 18.26  ?  327 LEU   I C    1 
ATOM   6918 O  O    . LEU   B 1 325 ? -19.325 -45.041 -12.272 1.00 17.65  ?  327 LEU   I O    1 
ATOM   6919 C  CB   . LEU   B 1 325 ? -22.422 -45.170 -11.145 1.00 18.50  ?  327 LEU   I CB   1 
ATOM   6920 C  CG   . LEU   B 1 325 ? -23.345 -46.062 -10.332 1.00 18.57  ?  327 LEU   I CG   1 
ATOM   6921 C  CD1  . LEU   B 1 325 ? -24.725 -46.052 -10.958 1.00 20.42  ?  327 LEU   I CD1  1 
ATOM   6922 C  CD2  . LEU   B 1 325 ? -22.821 -47.490 -10.243 1.00 18.66  ?  327 LEU   I CD2  1 
ATOM   6923 N  N    . GLY   B 1 326 ? -20.065 -42.998 -11.592 1.00 17.81  ?  328 GLY   I N    1 
ATOM   6924 C  CA   . GLY   B 1 326 ? -19.068 -42.314 -12.422 1.00 16.87  ?  328 GLY   I CA   1 
ATOM   6925 C  C    . GLY   B 1 326 ? -17.658 -42.601 -11.984 1.00 16.75  ?  328 GLY   I C    1 
ATOM   6926 O  O    . GLY   B 1 326 ? -16.743 -42.719 -12.792 1.00 17.40  ?  328 GLY   I O    1 
ATOM   6927 N  N    . MET   B 1 327 ? -17.454 -42.612 -10.677 1.00 16.94  ?  329 MET   I N    1 
ATOM   6928 C  CA   . MET   B 1 327 ? -16.182 -42.935 -10.154 1.00 18.53  ?  329 MET   I CA   1 
ATOM   6929 C  C    . MET   B 1 327 ? -15.749 -44.339 -10.573 1.00 16.10  ?  329 MET   I C    1 
ATOM   6930 O  O    . MET   B 1 327 ? -14.669 -44.518 -11.042 1.00 15.64  ?  329 MET   I O    1 
ATOM   6931 C  CB   . MET   B 1 327 ? -16.169 -42.800 -8.617  1.00 21.63  ?  329 MET   I CB   1 
ATOM   6932 C  CG   . MET   B 1 327 ? -16.014 -41.378 -8.156  1.00 21.68  ?  329 MET   I CG   1 
ATOM   6933 S  SD   . MET   B 1 327 ? -16.479 -41.223 -6.442  1.00 25.94  ?  329 MET   I SD   1 
ATOM   6934 C  CE   . MET   B 1 327 ? -16.262 -39.393 -6.312  1.00 27.45  ?  329 MET   I CE   1 
ATOM   6935 N  N    . PHE   B 1 328 ? -16.614 -45.310 -10.470 1.00 15.35  ?  330 PHE   I N    1 
ATOM   6936 C  CA   . PHE   B 1 328 ? -16.219 -46.659 -10.854 1.00 16.06  ?  330 PHE   I CA   1 
ATOM   6937 C  C    . PHE   B 1 328 ? -15.852 -46.707 -12.339 1.00 17.96  ?  330 PHE   I C    1 
ATOM   6938 O  O    . PHE   B 1 328 ? -14.868 -47.384 -12.738 1.00 16.99  ?  330 PHE   I O    1 
ATOM   6939 C  CB   . PHE   B 1 328 ? -17.365 -47.581 -10.536 1.00 16.15  ?  330 PHE   I CB   1 
ATOM   6940 C  CG   . PHE   B 1 328 ? -17.270 -48.935 -11.142 1.00 17.09  ?  330 PHE   I CG   1 
ATOM   6941 C  CD1  . PHE   B 1 328 ? -17.777 -49.164 -12.444 1.00 17.49  ?  330 PHE   I CD1  1 
ATOM   6942 C  CD2  . PHE   B 1 328 ? -16.790 -49.989 -10.405 1.00 16.28  ?  330 PHE   I CD2  1 
ATOM   6943 C  CE1  . PHE   B 1 328 ? -17.768 -50.437 -12.999 1.00 18.37  ?  330 PHE   I CE1  1 
ATOM   6944 C  CE2  . PHE   B 1 328 ? -16.784 -51.271 -10.948 1.00 17.32  ?  330 PHE   I CE2  1 
ATOM   6945 C  CZ   . PHE   B 1 328 ? -17.250 -51.487 -12.236 1.00 18.04  ?  330 PHE   I CZ   1 
ATOM   6946 N  N    . LEU   B 1 329 ? -16.628 -45.970 -13.151 1.00 18.79  ?  331 LEU   I N    1 
ATOM   6947 C  CA   . LEU   B 1 329 ? -16.426 -45.984 -14.609 1.00 18.03  ?  331 LEU   I CA   1 
ATOM   6948 C  C    . LEU   B 1 329 ? -15.088 -45.354 -14.896 1.00 18.07  ?  331 LEU   I C    1 
ATOM   6949 O  O    . LEU   B 1 329 ? -14.317 -45.842 -15.729 1.00 16.81  ?  331 LEU   I O    1 
ATOM   6950 C  CB   . LEU   B 1 329 ? -17.511 -45.200 -15.333 1.00 19.31  ?  331 LEU   I CB   1 
ATOM   6951 C  CG   . LEU   B 1 329 ? -18.234 -45.714 -16.581 1.00 21.54  ?  331 LEU   I CG   1 
ATOM   6952 C  CD1  . LEU   B 1 329 ? -18.660 -44.495 -17.386 1.00 23.04  ?  331 LEU   I CD1  1 
ATOM   6953 C  CD2  . LEU   B 1 329 ? -17.472 -46.720 -17.446 1.00 21.14  ?  331 LEU   I CD2  1 
ATOM   6954 N  N    . TYR   B 1 330 ? -14.814 -44.255 -14.206 1.00 18.21  ?  332 TYR   I N    1 
ATOM   6955 C  CA   . TYR   B 1 330 ? -13.515 -43.578 -14.373 1.00 19.20  ?  332 TYR   I CA   1 
ATOM   6956 C  C    . TYR   B 1 330 ? -12.389 -44.525 -13.991 1.00 19.69  ?  332 TYR   I C    1 
ATOM   6957 O  O    . TYR   B 1 330 ? -11.480 -44.768 -14.759 1.00 18.17  ?  332 TYR   I O    1 
ATOM   6958 C  CB   . TYR   B 1 330 ? -13.452 -42.327 -13.514 1.00 19.50  ?  332 TYR   I CB   1 
ATOM   6959 C  CG   . TYR   B 1 330 ? -12.066 -41.886 -13.122 1.00 22.06  ?  332 TYR   I CG   1 
ATOM   6960 C  CD1  . TYR   B 1 330 ? -11.321 -41.054 -13.944 1.00 23.48  ?  332 TYR   I CD1  1 
ATOM   6961 C  CD2  . TYR   B 1 330 ? -11.502 -42.283 -11.901 1.00 23.96  ?  332 TYR   I CD2  1 
ATOM   6962 C  CE1  . TYR   B 1 330 ? -10.042 -40.605 -13.572 1.00 24.37  ?  332 TYR   I CE1  1 
ATOM   6963 C  CE2  . TYR   B 1 330 ? -10.226 -41.848 -11.520 1.00 25.68  ?  332 TYR   I CE2  1 
ATOM   6964 C  CZ   . TYR   B 1 330 ? -9.503  -41.009 -12.344 1.00 25.11  ?  332 TYR   I CZ   1 
ATOM   6965 O  OH   . TYR   B 1 330 ? -8.221  -40.628 -11.986 1.00 26.09  ?  332 TYR   I OH   1 
ATOM   6966 N  N    . GLU   B 1 331 ? -12.480 -45.092 -12.801 1.00 19.82  ?  333 GLU   I N    1 
ATOM   6967 C  CA   . GLU   B 1 331 ? -11.402 -45.974 -12.360 1.00 20.30  ?  333 GLU   I CA   1 
ATOM   6968 C  C    . GLU   B 1 331 ? -11.261 -47.163 -13.330 1.00 19.95  ?  333 GLU   I C    1 
ATOM   6969 O  O    . GLU   B 1 331 ? -10.169 -47.477 -13.734 1.00 19.67  ?  333 GLU   I O    1 
ATOM   6970 C  CB   . GLU   B 1 331 ? -11.642 -46.461 -10.930 1.00 19.84  ?  333 GLU   I CB   1 
ATOM   6971 C  CG   . GLU   B 1 331 ? -11.700 -45.401 -9.851  1.00 20.00  ?  333 GLU   I CG   1 
ATOM   6972 C  CD   . GLU   B 1 331 ? -10.376 -44.703 -9.571  1.00 20.27  ?  333 GLU   I CD   1 
ATOM   6973 O  OE1  . GLU   B 1 331 ? -9.343  -44.993 -10.226 1.00 22.62  ?  333 GLU   I OE1  1 
ATOM   6974 O  OE2  . GLU   B 1 331 ? -10.387 -43.796 -8.716  1.00 21.98  ?  333 GLU   I OE2  1 
ATOM   6975 N  N    . TYR   B 1 332 ? -12.355 -47.773 -13.765 1.00 20.36  ?  334 TYR   I N    1 
ATOM   6976 C  CA   . TYR   B 1 332 ? -12.236 -48.928 -14.679 1.00 23.52  ?  334 TYR   I CA   1 
ATOM   6977 C  C    . TYR   B 1 332 ? -11.709 -48.516 -16.049 1.00 23.22  ?  334 TYR   I C    1 
ATOM   6978 O  O    . TYR   B 1 332 ? -10.735 -49.098 -16.562 1.00 20.51  ?  334 TYR   I O    1 
ATOM   6979 C  CB   . TYR   B 1 332 ? -13.564 -49.678 -14.858 1.00 25.38  ?  334 TYR   I CB   1 
ATOM   6980 C  CG   . TYR   B 1 332 ? -13.406 -51.177 -14.904 1.00 29.26  ?  334 TYR   I CG   1 
ATOM   6981 C  CD1  . TYR   B 1 332 ? -12.785 -51.816 -15.988 1.00 31.09  ?  334 TYR   I CD1  1 
ATOM   6982 C  CD2  . TYR   B 1 332 ? -13.875 -51.968 -13.855 1.00 34.02  ?  334 TYR   I CD2  1 
ATOM   6983 C  CE1  . TYR   B 1 332 ? -12.654 -53.202 -16.023 1.00 33.62  ?  334 TYR   I CE1  1 
ATOM   6984 C  CE2  . TYR   B 1 332 ? -13.739 -53.352 -13.869 1.00 35.32  ?  334 TYR   I CE2  1 
ATOM   6985 C  CZ   . TYR   B 1 332 ? -13.118 -53.962 -14.937 1.00 35.91  ?  334 TYR   I CZ   1 
ATOM   6986 O  OH   . TYR   B 1 332 ? -13.019 -55.334 -14.905 1.00 41.50  ?  334 TYR   I OH   1 
ATOM   6987 N  N    . ALA   B 1 333 ? -12.361 -47.510 -16.640 1.00 21.19  ?  335 ALA   I N    1 
ATOM   6988 C  CA   . ALA   B 1 333 ? -11.949 -46.998 -17.931 1.00 19.23  ?  335 ALA   I CA   1 
ATOM   6989 C  C    . ALA   B 1 333 ? -10.469 -46.596 -17.990 1.00 18.95  ?  335 ALA   I C    1 
ATOM   6990 O  O    . ALA   B 1 333 ? -9.777  -46.905 -18.977 1.00 18.66  ?  335 ALA   I O    1 
ATOM   6991 C  CB   . ALA   B 1 333 ? -12.820 -45.795 -18.323 1.00 18.28  ?  335 ALA   I CB   1 
ATOM   6992 N  N    . ARG   B 1 334 ? -9.947  -45.907 -16.973 1.00 20.55  ?  336 ARG   I N    1 
ATOM   6993 C  CA   . ARG   B 1 334 ? -8.531  -45.454 -17.090 1.00 22.66  ?  336 ARG   I CA   1 
ATOM   6994 C  C    . ARG   B 1 334 ? -7.513  -46.630 -17.050 1.00 23.23  ?  336 ARG   I C    1 
ATOM   6995 O  O    . ARG   B 1 334 ? -6.392  -46.536 -17.582 1.00 21.40  ?  336 ARG   I O    1 
ATOM   6996 C  CB   . ARG   B 1 334 ? -8.193  -44.388 -16.088 1.00 22.98  ?  336 ARG   I CB   1 
ATOM   6997 C  CG   . ARG   B 1 334 ? -8.146  -44.752 -14.622 1.00 23.82  ?  336 ARG   I CG   1 
ATOM   6998 C  CD   . ARG   B 1 334 ? -7.451  -43.585 -13.994 1.00 26.43  ?  336 ARG   I CD   1 
ATOM   6999 N  NE   . ARG   B 1 334 ? -7.424  -43.606 -12.560 1.00 29.37  ?  336 ARG   I NE   1 
ATOM   7000 C  CZ   . ARG   B 1 334 ? -6.544  -42.961 -11.807 1.00 28.10  ?  336 ARG   I CZ   1 
ATOM   7001 N  NH1  . ARG   B 1 334 ? -5.560  -42.216 -12.317 1.00 25.81  ?  336 ARG   I NH1  1 
ATOM   7002 N  NH2  . ARG   B 1 334 ? -6.663  -43.077 -10.495 1.00 31.49  ?  336 ARG   I NH2  1 
ATOM   7003 N  N    . ARG   B 1 335 ? -7.951  -47.737 -16.452 1.00 24.29  ?  337 ARG   I N    1 
ATOM   7004 C  CA   . ARG   B 1 335 ? -7.204  -48.986 -16.443 1.00 28.12  ?  337 ARG   I CA   1 
ATOM   7005 C  C    . ARG   B 1 335 ? -7.366  -49.755 -17.736 1.00 28.84  ?  337 ARG   I C    1 
ATOM   7006 O  O    . ARG   B 1 335 ? -6.484  -50.550 -18.043 1.00 30.54  ?  337 ARG   I O    1 
ATOM   7007 C  CB   . ARG   B 1 335 ? -7.657  -49.895 -15.289 1.00 27.65  ?  337 ARG   I CB   1 
ATOM   7008 C  CG   . ARG   B 1 335 ? -7.239  -49.367 -13.941 1.00 27.88  ?  337 ARG   I CG   1 
ATOM   7009 C  CD   . ARG   B 1 335 ? -8.020  -49.991 -12.787 1.00 28.63  ?  337 ARG   I CD   1 
ATOM   7010 N  NE   . ARG   B 1 335 ? -7.419  -49.573 -11.520 1.00 29.31  ?  337 ARG   I NE   1 
ATOM   7011 C  CZ   . ARG   B 1 335 ? -7.518  -48.351 -10.982 1.00 30.18  ?  337 ARG   I CZ   1 
ATOM   7012 N  NH1  . ARG   B 1 335 ? -8.227  -47.388 -11.586 1.00 28.81  ?  337 ARG   I NH1  1 
ATOM   7013 N  NH2  . ARG   B 1 335 ? -6.917  -48.084 -9.810  1.00 26.81  ?  337 ARG   I NH2  1 
ATOM   7014 N  N    . HIS   B 1 336 ? -8.462  -49.539 -18.482 1.00 26.63  ?  338 HIS   I N    1 
ATOM   7015 C  CA   . HIS   B 1 336 ? -8.689  -50.286 -19.712 1.00 26.70  ?  338 HIS   I CA   1 
ATOM   7016 C  C    . HIS   B 1 336 ? -8.914  -49.431 -20.959 1.00 27.86  ?  338 HIS   I C    1 
ATOM   7017 O  O    . HIS   B 1 336 ? -10.064 -49.284 -21.403 1.00 26.75  ?  338 HIS   I O    1 
ATOM   7018 C  CB   . HIS   B 1 336 ? -9.823  -51.307 -19.482 1.00 26.30  ?  338 HIS   I CB   1 
ATOM   7019 C  CG   . HIS   B 1 336 ? -9.453  -52.374 -18.502 1.00 27.94  ?  338 HIS   I CG   1 
ATOM   7020 N  ND1  . HIS   B 1 336 ? -8.863  -53.561 -18.882 1.00 28.03  ?  338 HIS   I ND1  1 
ATOM   7021 C  CD2  . HIS   B 1 336 ? -9.535  -52.410 -17.150 1.00 27.75  ?  338 HIS   I CD2  1 
ATOM   7022 C  CE1  . HIS   B 1 336 ? -8.626  -54.292 -17.808 1.00 29.74  ?  338 HIS   I CE1  1 
ATOM   7023 N  NE2  . HIS   B 1 336 ? -8.997  -53.607 -16.745 1.00 29.02  ?  338 HIS   I NE2  1 
ATOM   7024 N  N    . PRO   B 1 337 ? -7.815  -48.854 -21.531 1.00 29.56  ?  339 PRO   I N    1 
ATOM   7025 C  CA   . PRO   B 1 337 ? -7.884  -48.208 -22.874 1.00 29.87  ?  339 PRO   I CA   1 
ATOM   7026 C  C    . PRO   B 1 337 ? -8.265  -49.182 -23.998 1.00 30.97  ?  339 PRO   I C    1 
ATOM   7027 O  O    . PRO   B 1 337 ? -8.805  -48.767 -25.031 1.00 32.86  ?  339 PRO   I O    1 
ATOM   7028 C  CB   . PRO   B 1 337 ? -6.468  -47.661 -23.096 1.00 29.46  ?  339 PRO   I CB   1 
ATOM   7029 C  CG   . PRO   B 1 337 ? -5.614  -48.240 -21.977 1.00 29.39  ?  339 PRO   I CG   1 
ATOM   7030 C  CD   . PRO   B 1 337 ? -6.545  -48.541 -20.853 1.00 28.45  ?  339 PRO   I CD   1 
ATOM   7031 N  N    . ASP   B 1 338 ? -8.014  -50.464 -23.763 1.00 29.62  ?  340 ASP   I N    1 
ATOM   7032 C  CA   . ASP   B 1 338 ? -8.289  -51.510 -24.717 1.00 30.42  ?  340 ASP   I CA   1 
ATOM   7033 C  C    . ASP   B 1 338 ? -9.734  -51.901 -24.813 1.00 28.91  ?  340 ASP   I C    1 
ATOM   7034 O  O    . ASP   B 1 338 ? -10.066 -52.662 -25.695 1.00 29.84  ?  340 ASP   I O    1 
ATOM   7035 C  CB   . ASP   B 1 338 ? -7.484  -52.781 -24.369 1.00 31.51  ?  340 ASP   I CB   1 
ATOM   7036 C  CG   . ASP   B 1 338 ? -7.769  -53.276 -22.983 1.00 30.75  ?  340 ASP   I CG   1 
ATOM   7037 O  OD1  . ASP   B 1 338 ? -7.862  -52.414 -22.096 1.00 29.10  ?  340 ASP   I OD1  1 
ATOM   7038 O  OD2  . ASP   B 1 338 ? -7.883  -54.495 -22.772 1.00 31.13  ?  340 ASP   I OD2  1 
ATOM   7039 N  N    . TYR   B 1 339 ? -10.580 -51.469 -23.881 1.00 28.02  ?  341 TYR   I N    1 
ATOM   7040 C  CA   . TYR   B 1 339 ? -12.006 -51.793 -23.968 1.00 25.99  ?  341 TYR   I CA   1 
ATOM   7041 C  C    . TYR   B 1 339 ? -12.724 -50.847 -24.933 1.00 25.75  ?  341 TYR   I C    1 
ATOM   7042 O  O    . TYR   B 1 339 ? -12.286 -49.738 -25.159 1.00 23.33  ?  341 TYR   I O    1 
ATOM   7043 C  CB   . TYR   B 1 339 ? -12.657 -51.776 -22.583 1.00 25.84  ?  341 TYR   I CB   1 
ATOM   7044 C  CG   . TYR   B 1 339 ? -12.267 -52.942 -21.712 1.00 26.31  ?  341 TYR   I CG   1 
ATOM   7045 C  CD1  . TYR   B 1 339 ? -11.322 -53.895 -22.134 1.00 26.59  ?  341 TYR   I CD1  1 
ATOM   7046 C  CD2  . TYR   B 1 339 ? -12.834 -53.105 -20.459 1.00 26.12  ?  341 TYR   I CD2  1 
ATOM   7047 C  CE1  . TYR   B 1 339 ? -10.964 -54.947 -21.323 1.00 26.53  ?  341 TYR   I CE1  1 
ATOM   7048 C  CE2  . TYR   B 1 339 ? -12.477 -54.179 -19.655 1.00 26.90  ?  341 TYR   I CE2  1 
ATOM   7049 C  CZ   . TYR   B 1 339 ? -11.528 -55.083 -20.093 1.00 25.48  ?  341 TYR   I CZ   1 
ATOM   7050 O  OH   . TYR   B 1 339 ? -11.141 -56.153 -19.324 1.00 25.54  ?  341 TYR   I OH   1 
ATOM   7051 N  N    . SER   B 1 340 ? -13.814 -51.325 -25.523 1.00 25.35  ?  342 SER   I N    1 
ATOM   7052 C  CA   . SER   B 1 340 ? -14.753 -50.448 -26.137 1.00 24.39  ?  342 SER   I CA   1 
ATOM   7053 C  C    . SER   B 1 340 ? -15.484 -49.705 -25.020 1.00 23.00  ?  342 SER   I C    1 
ATOM   7054 O  O    . SER   B 1 340 ? -15.664 -50.216 -23.893 1.00 24.51  ?  342 SER   I O    1 
ATOM   7055 C  CB   . SER   B 1 340 ? -15.746 -51.204 -27.028 1.00 25.07  ?  342 SER   I CB   1 
ATOM   7056 O  OG   . SER   B 1 340 ? -16.682 -51.889 -26.240 1.00 25.03  ?  342 SER   I OG   1 
ATOM   7057 N  N    . VAL   B 1 341 ? -15.916 -48.493 -25.342 1.00 18.39  ?  343 VAL   I N    1 
ATOM   7058 C  CA   . VAL   B 1 341 ? -16.637 -47.726 -24.440 1.00 17.10  ?  343 VAL   I CA   1 
ATOM   7059 C  C    . VAL   B 1 341 ? -17.915 -48.393 -24.034 1.00 15.25  ?  343 VAL   I C    1 
ATOM   7060 O  O    . VAL   B 1 341 ? -18.284 -48.410 -22.842 1.00 13.67  ?  343 VAL   I O    1 
ATOM   7061 C  CB   . VAL   B 1 341 ? -16.972 -46.335 -25.029 1.00 15.94  ?  343 VAL   I CB   1 
ATOM   7062 C  CG1  . VAL   B 1 341 ? -17.988 -45.642 -24.155 1.00 15.37  ?  343 VAL   I CG1  1 
ATOM   7063 C  CG2  . VAL   B 1 341 ? -15.698 -45.498 -25.107 1.00 15.44  ?  343 VAL   I CG2  1 
ATOM   7064 N  N    . VAL   B 1 342 ? -18.640 -48.870 -25.009 1.00 16.94  ?  344 VAL   I N    1 
ATOM   7065 C  CA   . VAL   B 1 342 ? -19.880 -49.606 -24.713 1.00 18.78  ?  344 VAL   I CA   1 
ATOM   7066 C  C    . VAL   B 1 342 ? -19.634 -50.781 -23.739 1.00 17.09  ?  344 VAL   I C    1 
ATOM   7067 O  O    . VAL   B 1 342 ? -20.521 -51.135 -23.019 1.00 15.27  ?  344 VAL   I O    1 
ATOM   7068 C  CB   . VAL   B 1 342 ? -20.586 -50.138 -25.995 1.00 21.63  ?  344 VAL   I CB   1 
ATOM   7069 C  CG1  . VAL   B 1 342 ? -21.159 -48.994 -26.838 1.00 24.60  ?  344 VAL   I CG1  1 
ATOM   7070 C  CG2  . VAL   B 1 342 ? -19.657 -51.029 -26.816 1.00 23.39  ?  344 VAL   I CG2  1 
ATOM   7071 N  N    . LEU   B 1 343 ? -18.445 -51.410 -23.746 1.00 17.89  ?  345 LEU   I N    1 
ATOM   7072 C  CA   . LEU   B 1 343 ? -18.223 -52.546 -22.829 1.00 17.96  ?  345 LEU   I CA   1 
ATOM   7073 C  C    . LEU   B 1 343 ? -18.071 -52.010 -21.416 1.00 17.42  ?  345 LEU   I C    1 
ATOM   7074 O  O    . LEU   B 1 343 ? -18.571 -52.611 -20.475 1.00 16.14  ?  345 LEU   I O    1 
ATOM   7075 C  CB   . LEU   B 1 343 ? -17.023 -53.399 -23.231 1.00 18.23  ?  345 LEU   I CB   1 
ATOM   7076 C  CG   . LEU   B 1 343 ? -16.520 -54.419 -22.177 1.00 18.47  ?  345 LEU   I CG   1 
ATOM   7077 C  CD1  . LEU   B 1 343 ? -17.481 -55.578 -21.990 1.00 18.58  ?  345 LEU   I CD1  1 
ATOM   7078 C  CD2  . LEU   B 1 343 ? -15.141 -54.947 -22.549 1.00 18.38  ?  345 LEU   I CD2  1 
ATOM   7079 N  N    . LEU   B 1 344 ? -17.409 -50.843 -21.285 1.00 16.33  ?  346 LEU   I N    1 
ATOM   7080 C  CA   . LEU   B 1 344 ? -17.224 -50.211 -19.991 1.00 15.40  ?  346 LEU   I CA   1 
ATOM   7081 C  C    . LEU   B 1 344 ? -18.622 -49.822 -19.462 1.00 15.96  ?  346 LEU   I C    1 
ATOM   7082 O  O    . LEU   B 1 344 ? -18.904 -49.983 -18.276 1.00 15.93  ?  346 LEU   I O    1 
ATOM   7083 C  CB   . LEU   B 1 344 ? -16.289 -49.001 -20.112 1.00 14.41  ?  346 LEU   I CB   1 
ATOM   7084 C  CG   . LEU   B 1 344 ? -14.842 -49.417 -20.287 1.00 14.41  ?  346 LEU   I CG   1 
ATOM   7085 C  CD1  . LEU   B 1 344 ? -14.035 -48.260 -20.795 1.00 15.04  ?  346 LEU   I CD1  1 
ATOM   7086 C  CD2  . LEU   B 1 344 ? -14.233 -49.885 -18.967 1.00 15.23  ?  346 LEU   I CD2  1 
ATOM   7087 N  N    . LEU   B 1 345 ? -19.501 -49.342 -20.349 1.00 17.18  ?  347 LEU   I N    1 
ATOM   7088 C  CA   . LEU   B 1 345 ? -20.886 -49.013 -19.959 1.00 18.12  ?  347 LEU   I CA   1 
ATOM   7089 C  C    . LEU   B 1 345 ? -21.746 -50.214 -19.584 1.00 17.43  ?  347 LEU   I C    1 
ATOM   7090 O  O    . LEU   B 1 345 ? -22.509 -50.132 -18.631 1.00 18.11  ?  347 LEU   I O    1 
ATOM   7091 C  CB   . LEU   B 1 345 ? -21.579 -48.163 -20.998 1.00 19.87  ?  347 LEU   I CB   1 
ATOM   7092 C  CG   . LEU   B 1 345 ? -20.912 -46.801 -21.200 1.00 20.39  ?  347 LEU   I CG   1 
ATOM   7093 C  CD1  . LEU   B 1 345 ? -21.610 -46.057 -22.311 1.00 22.83  ?  347 LEU   I CD1  1 
ATOM   7094 C  CD2  . LEU   B 1 345 ? -20.948 -45.981 -19.961 1.00 22.72  ?  347 LEU   I CD2  1 
ATOM   7095 N  N    . ARG   B 1 346 ? -21.567 -51.340 -20.253 1.00 17.63  ?  348 ARG   I N    1 
ATOM   7096 C  CA   . ARG   B 1 346 ? -22.122 -52.616 -19.709 1.00 18.49  ?  348 ARG   I CA   1 
ATOM   7097 C  C    . ARG   B 1 346 ? -21.625 -52.983 -18.319 1.00 18.76  ?  348 ARG   I C    1 
ATOM   7098 O  O    . ARG   B 1 346 ? -22.427 -53.364 -17.499 1.00 18.66  ?  348 ARG   I O    1 
ATOM   7099 C  CB   . ARG   B 1 346 ? -21.823 -53.769 -20.622 1.00 18.67  ?  348 ARG   I CB   1 
ATOM   7100 C  CG   . ARG   B 1 346 ? -22.586 -53.694 -21.924 1.00 19.02  ?  348 ARG   I CG   1 
ATOM   7101 C  CD   . ARG   B 1 346 ? -22.195 -54.807 -22.870 1.00 20.01  ?  348 ARG   I CD   1 
ATOM   7102 N  NE   . ARG   B 1 346 ? -22.595 -54.394 -24.190 1.00 20.21  ?  348 ARG   I NE   1 
ATOM   7103 C  CZ   . ARG   B 1 346 ? -21.848 -54.412 -25.296 1.00 20.13  ?  348 ARG   I CZ   1 
ATOM   7104 N  NH1  . ARG   B 1 346 ? -20.609 -54.914 -25.306 1.00 20.42  ?  348 ARG   I NH1  1 
ATOM   7105 N  NH2  . ARG   B 1 346 ? -22.378 -53.925 -26.424 1.00 19.48  ?  348 ARG   I NH2  1 
ATOM   7106 N  N    . LEU   B 1 347 ? -20.312 -52.843 -18.073 1.00 20.48  ?  349 LEU   I N    1 
ATOM   7107 C  CA   . LEU   B 1 347 ? -19.707 -53.188 -16.799 1.00 21.78  ?  349 LEU   I CA   1 
ATOM   7108 C  C    . LEU   B 1 347 ? -20.279 -52.306 -15.693 1.00 20.89  ?  349 LEU   I C    1 
ATOM   7109 O  O    . LEU   B 1 347 ? -20.765 -52.798 -14.666 1.00 19.30  ?  349 LEU   I O    1 
ATOM   7110 C  CB   . LEU   B 1 347 ? -18.173 -53.029 -16.845 1.00 23.72  ?  349 LEU   I CB   1 
ATOM   7111 C  CG   . LEU   B 1 347 ? -17.381 -53.892 -17.823 1.00 25.48  ?  349 LEU   I CG   1 
ATOM   7112 C  CD1  . LEU   B 1 347 ? -15.908 -53.546 -17.797 1.00 26.60  ?  349 LEU   I CD1  1 
ATOM   7113 C  CD2  . LEU   B 1 347 ? -17.577 -55.362 -17.526 1.00 26.94  ?  349 LEU   I CD2  1 
ATOM   7114 N  N    . ALA   B 1 348 ? -20.266 -50.997 -15.938 1.00 18.84  ?  350 ALA   I N    1 
ATOM   7115 C  CA   . ALA   B 1 348 ? -20.910 -50.070 -15.041 1.00 19.74  ?  350 ALA   I CA   1 
ATOM   7116 C  C    . ALA   B 1 348 ? -22.393 -50.341 -14.812 1.00 19.79  ?  350 ALA   I C    1 
ATOM   7117 O  O    . ALA   B 1 348 ? -22.856 -50.288 -13.680 1.00 22.58  ?  350 ALA   I O    1 
ATOM   7118 C  CB   . ALA   B 1 348 ? -20.720 -48.643 -15.541 1.00 19.32  ?  350 ALA   I CB   1 
ATOM   7119 N  N    . LYS   B 1 349 ? -23.156 -50.607 -15.860 1.00 20.66  ?  351 LYS   I N    1 
ATOM   7120 C  CA   . LYS   B 1 349 ? -24.569 -50.975 -15.670 1.00 21.84  ?  351 LYS   I CA   1 
ATOM   7121 C  C    . LYS   B 1 349 ? -24.722 -52.242 -14.794 1.00 23.17  ?  351 LYS   I C    1 
ATOM   7122 O  O    . LYS   B 1 349 ? -25.729 -52.381 -14.080 1.00 22.82  ?  351 LYS   I O    1 
ATOM   7123 C  CB   . LYS   B 1 349 ? -25.251 -51.250 -16.996 1.00 21.38  ?  351 LYS   I CB   1 
ATOM   7124 C  CG   . LYS   B 1 349 ? -26.756 -51.382 -16.903 1.00 22.41  ?  351 LYS   I CG   1 
ATOM   7125 C  CD   . LYS   B 1 349 ? -27.391 -51.915 -18.192 1.00 26.38  ?  351 LYS   I CD   1 
ATOM   7126 N  N    . THR   B 1 350 ? -23.755 -53.161 -14.892 1.00 22.18  ?  352 THR   I N    1 
ATOM   7127 C  CA   . THR   B 1 350 ? -23.841 -54.448 -14.164 1.00 22.67  ?  352 THR   I CA   1 
ATOM   7128 C  C    . THR   B 1 350 ? -23.552 -54.143 -12.724 1.00 20.48  ?  352 THR   I C    1 
ATOM   7129 O  O    . THR   B 1 350 ? -24.304 -54.536 -11.838 1.00 19.69  ?  352 THR   I O    1 
ATOM   7130 C  CB   . THR   B 1 350 ? -22.854 -55.481 -14.714 1.00 22.68  ?  352 THR   I CB   1 
ATOM   7131 O  OG1  . THR   B 1 350 ? -23.267 -55.851 -16.033 1.00 23.48  ?  352 THR   I OG1  1 
ATOM   7132 C  CG2  . THR   B 1 350 ? -22.798 -56.727 -13.857 1.00 24.36  ?  352 THR   I CG2  1 
ATOM   7133 N  N    . TYR   B 1 351 ? -22.497 -53.366 -12.521 1.00 19.65  ?  353 TYR   I N    1 
ATOM   7134 C  CA   . TYR   B 1 351 ? -22.175 -52.886 -11.205 1.00 18.23  ?  353 TYR   I CA   1 
ATOM   7135 C  C    . TYR   B 1 351 ? -23.349 -52.122 -10.538 1.00 19.71  ?  353 TYR   I C    1 
ATOM   7136 O  O    . TYR   B 1 351 ? -23.563 -52.304 -9.324  1.00 18.50  ?  353 TYR   I O    1 
ATOM   7137 C  CB   . TYR   B 1 351 ? -20.865 -52.098 -11.243 1.00 17.08  ?  353 TYR   I CB   1 
ATOM   7138 C  CG   . TYR   B 1 351 ? -20.345 -51.710 -9.903  1.00 16.34  ?  353 TYR   I CG   1 
ATOM   7139 C  CD1  . TYR   B 1 351 ? -19.908 -52.675 -9.009  1.00 17.03  ?  353 TYR   I CD1  1 
ATOM   7140 C  CD2  . TYR   B 1 351 ? -20.295 -50.370 -9.508  1.00 15.71  ?  353 TYR   I CD2  1 
ATOM   7141 C  CE1  . TYR   B 1 351 ? -19.437 -52.337 -7.762  1.00 16.60  ?  353 TYR   I CE1  1 
ATOM   7142 C  CE2  . TYR   B 1 351 ? -19.848 -50.019 -8.267  1.00 15.83  ?  353 TYR   I CE2  1 
ATOM   7143 C  CZ   . TYR   B 1 351 ? -19.396 -50.998 -7.395  1.00 16.42  ?  353 TYR   I CZ   1 
ATOM   7144 O  OH   . TYR   B 1 351 ? -18.913 -50.648 -6.144  1.00 16.53  ?  353 TYR   I OH   1 
ATOM   7145 N  N    . GLU   B 1 352 ? -24.109 -51.333 -11.328 1.00 19.09  ?  354 GLU   I N    1 
ATOM   7146 C  CA   . GLU   B 1 352 ? -25.252 -50.531 -10.851 1.00 20.72  ?  354 GLU   I CA   1 
ATOM   7147 C  C    . GLU   B 1 352 ? -26.421 -51.429 -10.498 1.00 21.36  ?  354 GLU   I C    1 
ATOM   7148 O  O    . GLU   B 1 352 ? -27.081 -51.239 -9.467  1.00 21.87  ?  354 GLU   I O    1 
ATOM   7149 C  CB   . GLU   B 1 352 ? -25.719 -49.512 -11.927 1.00 22.05  ?  354 GLU   I CB   1 
ATOM   7150 C  CG   . GLU   B 1 352 ? -27.004 -48.698 -11.618 1.00 23.90  ?  354 GLU   I CG   1 
ATOM   7151 C  CD   . GLU   B 1 352 ? -27.619 -47.923 -12.822 1.00 26.16  ?  354 GLU   I CD   1 
ATOM   7152 O  OE1  . GLU   B 1 352 ? -27.679 -48.453 -13.967 1.00 26.32  ?  354 GLU   I OE1  1 
ATOM   7153 O  OE2  . GLU   B 1 352 ? -28.093 -46.762 -12.622 1.00 29.20  ?  354 GLU   I OE2  1 
ATOM   7154 N  N    . THR   B 1 353 ? -26.724 -52.361 -11.395 1.00 22.22  ?  355 THR   I N    1 
ATOM   7155 C  CA   . THR   B 1 353 ? -27.798 -53.335 -11.145 1.00 23.96  ?  355 THR   I CA   1 
ATOM   7156 C  C    . THR   B 1 353 ? -27.405 -54.120 -9.876  1.00 24.42  ?  355 THR   I C    1 
ATOM   7157 O  O    . THR   B 1 353 ? -28.201 -54.239 -8.981  1.00 25.01  ?  355 THR   I O    1 
ATOM   7158 C  CB   . THR   B 1 353 ? -28.056 -54.263 -12.365 1.00 23.43  ?  355 THR   I CB   1 
ATOM   7159 O  OG1  . THR   B 1 353 ? -28.386 -53.492 -13.531 1.00 20.78  ?  355 THR   I OG1  1 
ATOM   7160 C  CG2  . THR   B 1 353 ? -29.211 -55.221 -12.113 1.00 23.41  ?  355 THR   I CG2  1 
ATOM   7161 N  N    . THR   B 1 354 ? -26.159 -54.563 -9.746  1.00 26.95  ?  356 THR   I N    1 
ATOM   7162 C  CA   . THR   B 1 354 ? -25.802 -55.338 -8.572  1.00 28.91  ?  356 THR   I CA   1 
ATOM   7163 C  C    . THR   B 1 354 ? -26.032 -54.534 -7.309  1.00 29.90  ?  356 THR   I C    1 
ATOM   7164 O  O    . THR   B 1 354 ? -26.589 -55.072 -6.345  1.00 31.14  ?  356 THR   I O    1 
ATOM   7165 C  CB   . THR   B 1 354 ? -24.335 -55.843 -8.554  1.00 30.86  ?  356 THR   I CB   1 
ATOM   7166 O  OG1  . THR   B 1 354 ? -23.437 -54.764 -8.885  1.00 33.48  ?  356 THR   I OG1  1 
ATOM   7167 C  CG2  . THR   B 1 354 ? -24.143 -56.969 -9.519  1.00 29.63  ?  356 THR   I CG2  1 
ATOM   7168 N  N    . LEU   B 1 355 ? -25.617 -53.261 -7.292  1.00 27.30  ?  357 LEU   I N    1 
ATOM   7169 C  CA   . LEU   B 1 355 ? -25.696 -52.512 -6.057  1.00 27.52  ?  357 LEU   I CA   1 
ATOM   7170 C  C    . LEU   B 1 355 ? -27.149 -52.172 -5.756  1.00 27.29  ?  357 LEU   I C    1 
ATOM   7171 O  O    . LEU   B 1 355 ? -27.546 -52.226 -4.605  1.00 27.14  ?  357 LEU   I O    1 
ATOM   7172 C  CB   . LEU   B 1 355 ? -24.796 -51.275 -6.053  1.00 27.87  ?  357 LEU   I CB   1 
ATOM   7173 C  CG   . LEU   B 1 355 ? -23.260 -51.415 -6.073  1.00 27.44  ?  357 LEU   I CG   1 
ATOM   7174 C  CD1  . LEU   B 1 355 ? -22.641 -50.105 -5.624  1.00 25.82  ?  357 LEU   I CD1  1 
ATOM   7175 C  CD2  . LEU   B 1 355 ? -22.725 -52.537 -5.203  1.00 27.02  ?  357 LEU   I CD2  1 
ATOM   7176 N  N    . GLU   B 1 356 ? -27.952 -51.872 -6.781  1.00 29.04  ?  358 GLU   I N    1 
ATOM   7177 C  CA   . GLU   B 1 356 ? -29.386 -51.632 -6.577  1.00 31.74  ?  358 GLU   I CA   1 
ATOM   7178 C  C    . GLU   B 1 356 ? -30.099 -52.809 -5.897  1.00 32.21  ?  358 GLU   I C    1 
ATOM   7179 O  O    . GLU   B 1 356 ? -30.931 -52.609 -5.008  1.00 34.63  ?  358 GLU   I O    1 
ATOM   7180 C  CB   . GLU   B 1 356 ? -30.079 -51.305 -7.897  1.00 31.09  ?  358 GLU   I CB   1 
ATOM   7181 C  CG   . GLU   B 1 356 ? -29.802 -49.878 -8.368  1.00 32.89  ?  358 GLU   I CG   1 
ATOM   7182 C  CD   . GLU   B 1 356 ? -30.387 -48.827 -7.454  1.00 34.21  ?  358 GLU   I CD   1 
ATOM   7183 O  OE1  . GLU   B 1 356 ? -31.432 -49.117 -6.837  1.00 34.81  ?  358 GLU   I OE1  1 
ATOM   7184 O  OE2  . GLU   B 1 356 ? -29.809 -47.707 -7.352  1.00 35.10  ?  358 GLU   I OE2  1 
ATOM   7185 N  N    . LYS   B 1 357 ? -29.753 -54.018 -6.322  1.00 33.20  ?  359 LYS   I N    1 
ATOM   7186 C  CA   . LYS   B 1 357 ? -30.201 -55.271 -5.673  1.00 32.53  ?  359 LYS   I CA   1 
ATOM   7187 C  C    . LYS   B 1 357 ? -29.499 -55.494 -4.314  1.00 31.34  ?  359 LYS   I C    1 
ATOM   7188 O  O    . LYS   B 1 357 ? -30.151 -55.739 -3.310  1.00 31.36  ?  359 LYS   I O    1 
ATOM   7189 C  CB   . LYS   B 1 357 ? -29.972 -56.450 -6.637  1.00 34.00  ?  359 LYS   I CB   1 
ATOM   7190 C  CG   . LYS   B 1 357 ? -30.146 -57.862 -6.046  1.00 38.45  ?  359 LYS   I CG   1 
ATOM   7191 C  CD   . LYS   B 1 357 ? -29.822 -58.952 -7.077  1.00 41.73  ?  359 LYS   I CD   1 
ATOM   7192 C  CE   . LYS   B 1 357 ? -28.385 -58.840 -7.617  1.00 45.99  ?  359 LYS   I CE   1 
ATOM   7193 N  NZ   . LYS   B 1 357 ? -27.744 -60.137 -7.990  1.00 46.20  ?  359 LYS   I NZ   1 
ATOM   7194 N  N    . CYS   B 1 358 ? -28.177 -55.375 -4.276  1.00 32.90  ?  360 CYS   I N    1 
ATOM   7195 C  CA   . CYS   B 1 358 ? -27.413 -55.766 -3.108  1.00 34.68  ?  360 CYS   I CA   1 
ATOM   7196 C  C    . CYS   B 1 358 ? -27.422 -54.808 -1.925  1.00 36.97  ?  360 CYS   I C    1 
ATOM   7197 O  O    . CYS   B 1 358 ? -27.391 -55.251 -0.774  1.00 36.07  ?  360 CYS   I O    1 
ATOM   7198 C  CB   . CYS   B 1 358 ? -25.987 -56.117 -3.496  1.00 36.40  ?  360 CYS   I CB   1 
ATOM   7199 S  SG   . CYS   B 1 358 ? -25.970 -57.603 -4.507  1.00 41.36  ?  360 CYS   I SG   1 
ATOM   7200 N  N    . CYS   B 1 359 ? -27.495 -53.508 -2.185  1.00 34.17  ?  361 CYS   I N    1 
ATOM   7201 C  CA   . CYS   B 1 359 ? -27.652 -52.557 -1.110  1.00 36.03  ?  361 CYS   I CA   1 
ATOM   7202 C  C    . CYS   B 1 359 ? -29.057 -52.680 -0.421  1.00 36.61  ?  361 CYS   I C    1 
ATOM   7203 O  O    . CYS   B 1 359 ? -29.216 -52.324 0.746   1.00 35.75  ?  361 CYS   I O    1 
ATOM   7204 C  CB   . CYS   B 1 359 ? -27.253 -51.145 -1.627  1.00 35.53  ?  361 CYS   I CB   1 
ATOM   7205 S  SG   . CYS   B 1 359 ? -25.488 -51.124 -2.158  1.00 35.18  ?  361 CYS   I SG   1 
ATOM   7206 N  N    . ALA   B 1 360 ? -30.044 -53.256 -1.113  1.00 39.62  ?  362 ALA   I N    1 
ATOM   7207 C  CA   . ALA   B 1 360 ? -31.356 -53.560 -0.514  1.00 41.77  ?  362 ALA   I CA   1 
ATOM   7208 C  C    . ALA   B 1 360 ? -31.455 -54.943 0.157   1.00 45.56  ?  362 ALA   I C    1 
ATOM   7209 O  O    . ALA   B 1 360 ? -32.336 -55.156 0.991   1.00 45.42  ?  362 ALA   I O    1 
ATOM   7210 C  CB   . ALA   B 1 360 ? -32.458 -53.413 -1.557  1.00 43.80  ?  362 ALA   I CB   1 
ATOM   7211 N  N    . ALA   B 1 361 ? -30.551 -55.862 -0.186  1.00 49.85  ?  363 ALA   I N    1 
ATOM   7212 C  CA   . ALA   B 1 361 ? -30.569 -57.245 0.335   1.00 50.63  ?  363 ALA   I CA   1 
ATOM   7213 C  C    . ALA   B 1 361 ? -30.151 -57.338 1.806   1.00 49.86  ?  363 ALA   I C    1 
ATOM   7214 O  O    . ALA   B 1 361 ? -29.651 -56.366 2.399   1.00 49.46  ?  363 ALA   I O    1 
ATOM   7215 C  CB   . ALA   B 1 361 ? -29.671 -58.144 -0.523  1.00 52.57  ?  363 ALA   I CB   1 
ATOM   7216 N  N    . ALA   B 1 362 ? -30.347 -58.527 2.378   1.00 48.13  ?  364 ALA   I N    1 
ATOM   7217 C  CA   . ALA   B 1 362 ? -30.104 -58.760 3.813   1.00 48.31  ?  364 ALA   I CA   1 
ATOM   7218 C  C    . ALA   B 1 362 ? -28.639 -58.540 4.225   1.00 43.95  ?  364 ALA   I C    1 
ATOM   7219 O  O    . ALA   B 1 362 ? -28.387 -57.870 5.238   1.00 45.50  ?  364 ALA   I O    1 
ATOM   7220 C  CB   . ALA   B 1 362 ? -30.583 -60.153 4.220   1.00 49.73  ?  364 ALA   I CB   1 
ATOM   7221 N  N    . ASP   B 1 363 ? -27.702 -59.074 3.432   1.00 38.58  ?  365 ASP   I N    1 
ATOM   7222 C  CA   . ASP   B 1 363 ? -26.253 -58.872 3.646   1.00 38.60  ?  365 ASP   I CA   1 
ATOM   7223 C  C    . ASP   B 1 363 ? -25.559 -58.348 2.391   1.00 35.68  ?  365 ASP   I C    1 
ATOM   7224 O  O    . ASP   B 1 363 ? -25.032 -59.150 1.598   1.00 33.50  ?  365 ASP   I O    1 
ATOM   7225 C  CB   . ASP   B 1 363 ? -25.583 -60.182 4.106   1.00 39.02  ?  365 ASP   I CB   1 
ATOM   7226 C  CG   . ASP   B 1 363 ? -24.108 -59.994 4.547   1.00 40.10  ?  365 ASP   I CG   1 
ATOM   7227 O  OD1  . ASP   B 1 363 ? -23.498 -58.922 4.312   1.00 42.59  ?  365 ASP   I OD1  1 
ATOM   7228 O  OD2  . ASP   B 1 363 ? -23.560 -60.948 5.151   1.00 43.06  ?  365 ASP   I OD2  1 
ATOM   7229 N  N    . PRO   B 1 364 ? -25.499 -56.997 2.227   1.00 34.76  ?  366 PRO   I N    1 
ATOM   7230 C  CA   . PRO   B 1 364 ? -24.954 -56.408 0.980   1.00 31.76  ?  366 PRO   I CA   1 
ATOM   7231 C  C    . PRO   B 1 364 ? -23.544 -56.866 0.593   1.00 28.49  ?  366 PRO   I C    1 
ATOM   7232 O  O    . PRO   B 1 364 ? -23.305 -57.294 -0.544  1.00 22.04  ?  366 PRO   I O    1 
ATOM   7233 C  CB   . PRO   B 1 364 ? -24.999 -54.888 1.254   1.00 34.03  ?  366 PRO   I CB   1 
ATOM   7234 C  CG   . PRO   B 1 364 ? -26.080 -54.713 2.247   1.00 35.01  ?  366 PRO   I CG   1 
ATOM   7235 C  CD   . PRO   B 1 364 ? -26.105 -55.968 3.091   1.00 36.67  ?  366 PRO   I CD   1 
ATOM   7236 N  N    . HIS   B 1 365 ? -22.625 -56.796 1.554   1.00 30.69  ?  367 HIS   I N    1 
ATOM   7237 C  CA   . HIS   B 1 365 ? -21.227 -57.122 1.332   1.00 32.77  ?  367 HIS   I CA   1 
ATOM   7238 C  C    . HIS   B 1 365 ? -21.035 -58.536 0.799   1.00 35.15  ?  367 HIS   I C    1 
ATOM   7239 O  O    . HIS   B 1 365 ? -20.208 -58.755 -0.086  1.00 38.79  ?  367 HIS   I O    1 
ATOM   7240 C  CB   . HIS   B 1 365 ? -20.462 -56.968 2.632   1.00 34.88  ?  367 HIS   I CB   1 
ATOM   7241 C  CG   . HIS   B 1 365 ? -19.014 -57.253 2.509   1.00 36.24  ?  367 HIS   I CG   1 
ATOM   7242 N  ND1  . HIS   B 1 365 ? -18.511 -58.539 2.491   1.00 41.02  ?  367 HIS   I ND1  1 
ATOM   7243 C  CD2  . HIS   B 1 365 ? -17.953 -56.424 2.414   1.00 36.11  ?  367 HIS   I CD2  1 
ATOM   7244 C  CE1  . HIS   B 1 365 ? -17.194 -58.488 2.391   1.00 41.42  ?  367 HIS   I CE1  1 
ATOM   7245 N  NE2  . HIS   B 1 365 ? -16.833 -57.217 2.318   1.00 41.69  ?  367 HIS   I NE2  1 
ATOM   7246 N  N    . GLU   B 1 366 ? -21.760 -59.495 1.348   1.00 35.06  ?  368 GLU   I N    1 
ATOM   7247 C  CA   . GLU   B 1 366 ? -21.748 -60.848 0.774   1.00 39.93  ?  368 GLU   I CA   1 
ATOM   7248 C  C    . GLU   B 1 366 ? -22.528 -60.930 -0.555  1.00 37.32  ?  368 GLU   I C    1 
ATOM   7249 O  O    . GLU   B 1 366 ? -22.196 -61.730 -1.419  1.00 38.91  ?  368 GLU   I O    1 
ATOM   7250 C  CB   . GLU   B 1 366 ? -22.304 -61.874 1.763   1.00 44.10  ?  368 GLU   I CB   1 
ATOM   7251 C  CG   . GLU   B 1 366 ? -21.549 -61.945 3.079   1.00 49.64  ?  368 GLU   I CG   1 
ATOM   7252 C  CD   . GLU   B 1 366 ? -20.087 -62.306 2.922   1.00 52.63  ?  368 GLU   I CD   1 
ATOM   7253 O  OE1  . GLU   B 1 366 ? -19.803 -63.522 2.754   1.00 53.35  ?  368 GLU   I OE1  1 
ATOM   7254 O  OE2  . GLU   B 1 366 ? -19.239 -61.369 2.996   1.00 55.52  ?  368 GLU   I OE2  1 
ATOM   7255 N  N    . CYS   B 1 367 ? -23.562 -60.115 -0.715  1.00 35.62  ?  369 CYS   I N    1 
ATOM   7256 C  CA   . CYS   B 1 367 ? -24.263 -60.039 -2.003  1.00 38.90  ?  369 CYS   I CA   1 
ATOM   7257 C  C    . CYS   B 1 367 ? -23.352 -59.670 -3.206  1.00 36.30  ?  369 CYS   I C    1 
ATOM   7258 O  O    . CYS   B 1 367 ? -23.350 -60.355 -4.219  1.00 34.18  ?  369 CYS   I O    1 
ATOM   7259 C  CB   . CYS   B 1 367 ? -25.438 -59.074 -1.885  1.00 42.39  ?  369 CYS   I CB   1 
ATOM   7260 S  SG   . CYS   B 1 367 ? -26.626 -59.094 -3.236  1.00 46.78  ?  369 CYS   I SG   1 
ATOM   7261 N  N    . TYR   B 1 368 ? -22.559 -58.607 -3.087  1.00 36.16  ?  370 TYR   I N    1 
ATOM   7262 C  CA   . TYR   B 1 368 ? -21.807 -58.097 -4.244  1.00 33.42  ?  370 TYR   I CA   1 
ATOM   7263 C  C    . TYR   B 1 368 ? -20.333 -58.500 -4.187  1.00 33.49  ?  370 TYR   I C    1 
ATOM   7264 O  O    . TYR   B 1 368 ? -19.519 -58.060 -5.027  1.00 29.63  ?  370 TYR   I O    1 
ATOM   7265 C  CB   . TYR   B 1 368 ? -22.001 -56.577 -4.412  1.00 33.51  ?  370 TYR   I CB   1 
ATOM   7266 C  CG   . TYR   B 1 368 ? -21.655 -55.773 -3.205  1.00 30.91  ?  370 TYR   I CG   1 
ATOM   7267 C  CD1  . TYR   B 1 368 ? -20.344 -55.695 -2.771  1.00 31.24  ?  370 TYR   I CD1  1 
ATOM   7268 C  CD2  . TYR   B 1 368 ? -22.630 -55.095 -2.481  1.00 31.05  ?  370 TYR   I CD2  1 
ATOM   7269 C  CE1  . TYR   B 1 368 ? -19.996 -54.966 -1.666  1.00 31.83  ?  370 TYR   I CE1  1 
ATOM   7270 C  CE2  . TYR   B 1 368 ? -22.288 -54.362 -1.358  1.00 30.43  ?  370 TYR   I CE2  1 
ATOM   7271 C  CZ   . TYR   B 1 368 ? -20.947 -54.300 -0.974  1.00 30.78  ?  370 TYR   I CZ   1 
ATOM   7272 O  OH   . TYR   B 1 368 ? -20.513 -53.639 0.142   1.00 33.50  ?  370 TYR   I OH   1 
ATOM   7273 N  N    . ALA   B 1 369 ? -19.986 -59.368 -3.226  1.00 32.44  ?  371 ALA   I N    1 
ATOM   7274 C  CA   . ALA   B 1 369 ? -18.607 -59.846 -3.089  1.00 32.26  ?  371 ALA   I CA   1 
ATOM   7275 C  C    . ALA   B 1 369 ? -18.017 -60.377 -4.384  1.00 29.17  ?  371 ALA   I C    1 
ATOM   7276 O  O    . ALA   B 1 369 ? -16.837 -60.174 -4.614  1.00 31.84  ?  371 ALA   I O    1 
ATOM   7277 C  CB   . ALA   B 1 369 ? -18.506 -60.908 -1.997  1.00 36.10  ?  371 ALA   I CB   1 
ATOM   7278 N  N    . LYS   B 1 370 ? -18.816 -61.069 -5.195  1.00 28.33  ?  372 LYS   I N    1 
ATOM   7279 C  CA   . LYS   B 1 370 ? -18.394 -61.591 -6.523  1.00 30.80  ?  372 LYS   I CA   1 
ATOM   7280 C  C    . LYS   B 1 370 ? -19.011 -60.853 -7.739  1.00 30.90  ?  372 LYS   I C    1 
ATOM   7281 O  O    . LYS   B 1 370 ? -19.408 -61.477 -8.742  1.00 34.14  ?  372 LYS   I O    1 
ATOM   7282 C  CB   . LYS   B 1 370 ? -18.680 -63.113 -6.647  1.00 31.41  ?  372 LYS   I CB   1 
ATOM   7283 N  N    . VAL   B 1 371 ? -19.108 -59.531 -7.648  1.00 30.24  ?  373 VAL   I N    1 
ATOM   7284 C  CA   . VAL   B 1 371 ? -19.658 -58.737 -8.757  1.00 28.57  ?  373 VAL   I CA   1 
ATOM   7285 C  C    . VAL   B 1 371 ? -18.659 -58.674 -9.931  1.00 28.46  ?  373 VAL   I C    1 
ATOM   7286 O  O    . VAL   B 1 371 ? -19.042 -58.761 -11.109 1.00 26.57  ?  373 VAL   I O    1 
ATOM   7287 C  CB   . VAL   B 1 371 ? -20.092 -57.322 -8.304  1.00 30.55  ?  373 VAL   I CB   1 
ATOM   7288 C  CG1  . VAL   B 1 371 ? -18.924 -56.478 -7.764  1.00 28.76  ?  373 VAL   I CG1  1 
ATOM   7289 C  CG2  . VAL   B 1 371 ? -20.778 -56.605 -9.467  1.00 31.88  ?  373 VAL   I CG2  1 
ATOM   7290 N  N    . PHE   B 1 372 ? -17.380 -58.549 -9.603  1.00 26.46  ?  374 PHE   I N    1 
ATOM   7291 C  CA   . PHE   B 1 372 ? -16.328 -58.675 -10.561 1.00 29.49  ?  374 PHE   I CA   1 
ATOM   7292 C  C    . PHE   B 1 372 ? -16.358 -59.974 -11.382 1.00 33.85  ?  374 PHE   I C    1 
ATOM   7293 O  O    . PHE   B 1 372 ? -15.906 -59.976 -12.536 1.00 36.14  ?  374 PHE   I O    1 
ATOM   7294 C  CB   . PHE   B 1 372 ? -14.971 -58.466 -9.867  1.00 33.29  ?  374 PHE   I CB   1 
ATOM   7295 C  CG   . PHE   B 1 372 ? -14.594 -57.007 -9.670  1.00 34.75  ?  374 PHE   I CG   1 
ATOM   7296 C  CD1  . PHE   B 1 372 ? -15.553 -55.989 -9.683  1.00 37.17  ?  374 PHE   I CD1  1 
ATOM   7297 C  CD2  . PHE   B 1 372 ? -13.263 -56.652 -9.451  1.00 37.70  ?  374 PHE   I CD2  1 
ATOM   7298 C  CE1  . PHE   B 1 372 ? -15.190 -54.664 -9.514  1.00 36.72  ?  374 PHE   I CE1  1 
ATOM   7299 C  CE2  . PHE   B 1 372 ? -12.897 -55.323 -9.262  1.00 37.53  ?  374 PHE   I CE2  1 
ATOM   7300 C  CZ   . PHE   B 1 372 ? -13.865 -54.328 -9.316  1.00 38.13  ?  374 PHE   I CZ   1 
ATOM   7301 N  N    . ASP   B 1 373 ? -16.900 -61.062 -10.838 1.00 33.12  ?  375 ASP   I N    1 
ATOM   7302 C  CA   . ASP   B 1 373 ? -17.160 -62.266 -11.659 1.00 35.76  ?  375 ASP   I CA   1 
ATOM   7303 C  C    . ASP   B 1 373 ? -18.133 -62.045 -12.852 1.00 34.44  ?  375 ASP   I C    1 
ATOM   7304 O  O    . ASP   B 1 373 ? -17.967 -62.656 -13.914 1.00 29.58  ?  375 ASP   I O    1 
ATOM   7305 C  CB   . ASP   B 1 373 ? -17.756 -63.411 -10.800 1.00 34.77  ?  375 ASP   I CB   1 
ATOM   7306 C  CG   . ASP   B 1 373 ? -16.756 -64.077 -9.921  1.00 33.31  ?  375 ASP   I CG   1 
ATOM   7307 O  OD1  . ASP   B 1 373 ? -15.702 -63.485 -9.673  1.00 32.89  ?  375 ASP   I OD1  1 
ATOM   7308 O  OD2  . ASP   B 1 373 ? -17.037 -65.230 -9.468  1.00 39.69  ?  375 ASP   I OD2  1 
ATOM   7309 N  N    . GLU   B 1 374 ? -19.161 -61.224 -12.639 1.00 35.32  ?  376 GLU   I N    1 
ATOM   7310 C  CA   . GLU   B 1 374 ? -20.162 -60.938 -13.673 1.00 37.25  ?  376 GLU   I CA   1 
ATOM   7311 C  C    . GLU   B 1 374 ? -19.566 -60.208 -14.882 1.00 36.06  ?  376 GLU   I C    1 
ATOM   7312 O  O    . GLU   B 1 374 ? -20.156 -60.248 -15.959 1.00 35.76  ?  376 GLU   I O    1 
ATOM   7313 C  CB   . GLU   B 1 374 ? -21.344 -60.159 -13.107 1.00 40.39  ?  376 GLU   I CB   1 
ATOM   7314 C  CG   . GLU   B 1 374 ? -22.082 -60.905 -12.003 1.00 44.68  ?  376 GLU   I CG   1 
ATOM   7315 C  CD   . GLU   B 1 374 ? -23.447 -60.311 -11.689 1.00 54.21  ?  376 GLU   I CD   1 
ATOM   7316 O  OE1  . GLU   B 1 374 ? -23.695 -59.127 -12.010 1.00 58.11  ?  376 GLU   I OE1  1 
ATOM   7317 O  OE2  . GLU   B 1 374 ? -24.288 -61.038 -11.109 1.00 62.82  ?  376 GLU   I OE2  1 
ATOM   7318 N  N    . PHE   B 1 375 ? -18.386 -59.595 -14.713 1.00 34.20  ?  377 PHE   I N    1 
ATOM   7319 C  CA   . PHE   B 1 375 ? -17.710 -58.845 -15.785 1.00 34.32  ?  377 PHE   I CA   1 
ATOM   7320 C  C    . PHE   B 1 375 ? -16.998 -59.727 -16.787 1.00 36.01  ?  377 PHE   I C    1 
ATOM   7321 O  O    . PHE   B 1 375 ? -16.956 -59.392 -17.976 1.00 29.36  ?  377 PHE   I O    1 
ATOM   7322 C  CB   . PHE   B 1 375 ? -16.662 -57.854 -15.221 1.00 31.94  ?  377 PHE   I CB   1 
ATOM   7323 C  CG   . PHE   B 1 375 ? -17.217 -56.802 -14.285 1.00 30.57  ?  377 PHE   I CG   1 
ATOM   7324 C  CD1  . PHE   B 1 375 ? -18.580 -56.488 -14.229 1.00 29.40  ?  377 PHE   I CD1  1 
ATOM   7325 C  CD2  . PHE   B 1 375 ? -16.351 -56.075 -13.483 1.00 29.07  ?  377 PHE   I CD2  1 
ATOM   7326 C  CE1  . PHE   B 1 375 ? -19.064 -55.504 -13.380 1.00 26.49  ?  377 PHE   I CE1  1 
ATOM   7327 C  CE2  . PHE   B 1 375 ? -16.845 -55.098 -12.639 1.00 30.76  ?  377 PHE   I CE2  1 
ATOM   7328 C  CZ   . PHE   B 1 375 ? -18.211 -54.810 -12.593 1.00 26.87  ?  377 PHE   I CZ   1 
ATOM   7329 N  N    . LYS   B 1 376 ? -16.417 -60.835 -16.309 1.00 36.48  ?  378 LYS   I N    1 
ATOM   7330 C  CA   . LYS   B 1 376 ? -15.562 -61.665 -17.150 1.00 37.95  ?  378 LYS   I CA   1 
ATOM   7331 C  C    . LYS   B 1 376 ? -16.245 -62.080 -18.465 1.00 33.81  ?  378 LYS   I C    1 
ATOM   7332 O  O    . LYS   B 1 376 ? -15.651 -61.923 -19.500 1.00 36.34  ?  378 LYS   I O    1 
ATOM   7333 C  CB   . LYS   B 1 376 ? -15.003 -62.881 -16.381 1.00 44.18  ?  378 LYS   I CB   1 
ATOM   7334 C  CG   . LYS   B 1 376 ? -13.719 -63.470 -16.989 1.00 48.69  ?  378 LYS   I CG   1 
ATOM   7335 C  CD   . LYS   B 1 376 ? -12.607 -63.767 -15.948 1.00 52.21  ?  378 LYS   I CD   1 
ATOM   7336 C  CE   . LYS   B 1 376 ? -13.083 -64.649 -14.784 1.00 53.96  ?  378 LYS   I CE   1 
ATOM   7337 N  NZ   . LYS   B 1 376 ? -12.052 -65.479 -14.087 1.00 53.98  ?  378 LYS   I NZ   1 
ATOM   7338 N  N    . PRO   B 1 377 ? -17.490 -62.566 -18.425 1.00 28.91  ?  379 PRO   I N    1 
ATOM   7339 C  CA   . PRO   B 1 377 ? -18.197 -62.922 -19.685 1.00 28.14  ?  379 PRO   I CA   1 
ATOM   7340 C  C    . PRO   B 1 377 ? -18.610 -61.711 -20.526 1.00 27.52  ?  379 PRO   I C    1 
ATOM   7341 O  O    . PRO   B 1 377 ? -18.683 -61.807 -21.757 1.00 24.97  ?  379 PRO   I O    1 
ATOM   7342 C  CB   . PRO   B 1 377 ? -19.449 -63.649 -19.205 1.00 28.38  ?  379 PRO   I CB   1 
ATOM   7343 C  CG   . PRO   B 1 377 ? -19.653 -63.191 -17.796 1.00 28.71  ?  379 PRO   I CG   1 
ATOM   7344 C  CD   . PRO   B 1 377 ? -18.287 -62.905 -17.234 1.00 29.36  ?  379 PRO   I CD   1 
ATOM   7345 N  N    . LEU   B 1 378 ? -18.913 -60.597 -19.870 1.00 26.10  ?  380 LEU   I N    1 
ATOM   7346 C  CA   . LEU   B 1 378 ? -19.081 -59.328 -20.623 1.00 26.86  ?  380 LEU   I CA   1 
ATOM   7347 C  C    . LEU   B 1 378 ? -17.833 -58.967 -21.407 1.00 22.45  ?  380 LEU   I C    1 
ATOM   7348 O  O    . LEU   B 1 378 ? -17.954 -58.627 -22.536 1.00 22.13  ?  380 LEU   I O    1 
ATOM   7349 C  CB   . LEU   B 1 378 ? -19.484 -58.169 -19.723 1.00 26.06  ?  380 LEU   I CB   1 
ATOM   7350 C  CG   . LEU   B 1 378 ? -20.957 -57.949 -19.380 1.00 31.52  ?  380 LEU   I CG   1 
ATOM   7351 C  CD1  . LEU   B 1 378 ? -21.959 -58.990 -19.857 1.00 32.52  ?  380 LEU   I CD1  1 
ATOM   7352 C  CD2  . LEU   B 1 378 ? -21.083 -57.726 -17.866 1.00 34.41  ?  380 LEU   I CD2  1 
ATOM   7353 N  N    . VAL   B 1 379 ? -16.646 -59.036 -20.800 1.00 23.37  ?  381 VAL   I N    1 
ATOM   7354 C  CA   . VAL   B 1 379 ? -15.369 -58.816 -21.513 1.00 21.78  ?  381 VAL   I CA   1 
ATOM   7355 C  C    . VAL   B 1 379 ? -15.116 -59.834 -22.581 1.00 23.20  ?  381 VAL   I C    1 
ATOM   7356 O  O    . VAL   B 1 379 ? -14.818 -59.481 -23.727 1.00 22.07  ?  381 VAL   I O    1 
ATOM   7357 C  CB   . VAL   B 1 379 ? -14.152 -58.830 -20.548 1.00 22.52  ?  381 VAL   I CB   1 
ATOM   7358 C  CG1  . VAL   B 1 379 ? -12.840 -58.764 -21.296 1.00 22.72  ?  381 VAL   I CG1  1 
ATOM   7359 C  CG2  . VAL   B 1 379 ? -14.215 -57.673 -19.582 1.00 24.65  ?  381 VAL   I CG2  1 
ATOM   7360 N  N    . GLU   B 1 380 ? -15.255 -61.115 -22.205 1.00 24.68  ?  382 GLU   I N    1 
ATOM   7361 C  CA   . GLU   B 1 380 ? -14.916 -62.258 -23.072 1.00 25.82  ?  382 GLU   I CA   1 
ATOM   7362 C  C    . GLU   B 1 380 ? -15.617 -62.244 -24.397 1.00 24.64  ?  382 GLU   I C    1 
ATOM   7363 O  O    . GLU   B 1 380 ? -15.040 -62.559 -25.427 1.00 22.48  ?  382 GLU   I O    1 
ATOM   7364 C  CB   . GLU   B 1 380 ? -15.261 -63.575 -22.361 1.00 29.20  ?  382 GLU   I CB   1 
ATOM   7365 C  CG   . GLU   B 1 380 ? -14.394 -63.843 -21.115 1.00 35.50  ?  382 GLU   I CG   1 
ATOM   7366 C  CD   . GLU   B 1 380 ? -13.222 -64.756 -21.381 1.00 42.23  ?  382 GLU   I CD   1 
ATOM   7367 O  OE1  . GLU   B 1 380 ? -13.429 -66.005 -21.417 1.00 47.23  ?  382 GLU   I OE1  1 
ATOM   7368 O  OE2  . GLU   B 1 380 ? -12.103 -64.216 -21.554 1.00 48.18  ?  382 GLU   I OE2  1 
ATOM   7369 N  N    . GLU   B 1 381 ? -16.879 -61.859 -24.346 1.00 27.03  ?  383 GLU   I N    1 
ATOM   7370 C  CA   . GLU   B 1 381 ? -17.754 -62.010 -25.457 1.00 29.30  ?  383 GLU   I CA   1 
ATOM   7371 C  C    . GLU   B 1 381 ? -17.357 -61.108 -26.647 1.00 25.93  ?  383 GLU   I C    1 
ATOM   7372 O  O    . GLU   B 1 381 ? -17.297 -61.596 -27.771 1.00 24.90  ?  383 GLU   I O    1 
ATOM   7373 C  CB   . GLU   B 1 381 ? -19.227 -61.959 -24.949 1.00 34.42  ?  383 GLU   I CB   1 
ATOM   7374 C  CG   . GLU   B 1 381 ? -20.269 -61.186 -25.722 1.00 42.49  ?  383 GLU   I CG   1 
ATOM   7375 C  CD   . GLU   B 1 381 ? -20.340 -61.537 -27.163 1.00 43.17  ?  383 GLU   I CD   1 
ATOM   7376 O  OE1  . GLU   B 1 381 ? -19.999 -62.697 -27.504 1.00 49.64  ?  383 GLU   I OE1  1 
ATOM   7377 O  OE2  . GLU   B 1 381 ? -20.744 -60.630 -27.916 1.00 37.30  ?  383 GLU   I OE2  1 
ATOM   7378 N  N    . PRO   B 1 382 ? -17.034 -59.811 -26.418 1.00 23.85  ?  384 PRO   I N    1 
ATOM   7379 C  CA   . PRO   B 1 382 ? -16.565 -59.061 -27.571 1.00 23.56  ?  384 PRO   I CA   1 
ATOM   7380 C  C    . PRO   B 1 382 ? -15.186 -59.511 -28.006 1.00 24.05  ?  384 PRO   I C    1 
ATOM   7381 O  O    . PRO   B 1 382 ? -14.877 -59.509 -29.246 1.00 23.72  ?  384 PRO   I O    1 
ATOM   7382 C  CB   . PRO   B 1 382 ? -16.587 -57.573 -27.113 1.00 22.81  ?  384 PRO   I CB   1 
ATOM   7383 C  CG   . PRO   B 1 382 ? -16.796 -57.593 -25.677 1.00 22.60  ?  384 PRO   I CG   1 
ATOM   7384 C  CD   . PRO   B 1 382 ? -17.402 -58.934 -25.304 1.00 23.30  ?  384 PRO   I CD   1 
ATOM   7385 N  N    . GLN   B 1 383 ? -14.363 -59.921 -27.038 1.00 23.71  ?  385 GLN   I N    1 
ATOM   7386 C  CA   . GLN   B 1 383 ? -13.007 -60.361 -27.369 1.00 27.03  ?  385 GLN   I CA   1 
ATOM   7387 C  C    . GLN   B 1 383 ? -13.078 -61.637 -28.219 1.00 25.79  ?  385 GLN   I C    1 
ATOM   7388 O  O    . GLN   B 1 383 ? -12.449 -61.743 -29.247 1.00 25.49  ?  385 GLN   I O    1 
ATOM   7389 C  CB   . GLN   B 1 383 ? -12.172 -60.619 -26.116 1.00 31.07  ?  385 GLN   I CB   1 
ATOM   7390 C  CG   . GLN   B 1 383 ? -11.967 -59.376 -25.245 1.00 34.55  ?  385 GLN   I CG   1 
ATOM   7391 C  CD   . GLN   B 1 383 ? -11.148 -59.662 -23.983 1.00 36.57  ?  385 GLN   I CD   1 
ATOM   7392 O  OE1  . GLN   B 1 383 ? -11.317 -60.714 -23.315 1.00 36.86  ?  385 GLN   I OE1  1 
ATOM   7393 N  NE2  . GLN   B 1 383 ? -10.218 -58.751 -23.679 1.00 34.16  ?  385 GLN   I NE2  1 
ATOM   7394 N  N    . ASN   B 1 384 ? -13.892 -62.588 -27.823 1.00 27.86  ?  386 ASN   I N    1 
ATOM   7395 C  CA   . ASN   B 1 384 ? -14.033 -63.823 -28.624 1.00 28.85  ?  386 ASN   I CA   1 
ATOM   7396 C  C    . ASN   B 1 384 ? -14.639 -63.559 -30.023 1.00 31.48  ?  386 ASN   I C    1 
ATOM   7397 O  O    . ASN   B 1 384 ? -14.283 -64.212 -31.004 1.00 29.99  ?  386 ASN   I O    1 
ATOM   7398 C  CB   . ASN   B 1 384 ? -14.883 -64.831 -27.866 1.00 28.83  ?  386 ASN   I CB   1 
ATOM   7399 C  CG   . ASN   B 1 384 ? -14.295 -65.195 -26.510 1.00 27.61  ?  386 ASN   I CG   1 
ATOM   7400 O  OD1  . ASN   B 1 384 ? -13.096 -65.148 -26.312 1.00 29.99  ?  386 ASN   I OD1  1 
ATOM   7401 N  ND2  . ASN   B 1 384 ? -15.157 -65.506 -25.562 1.00 29.66  ?  386 ASN   I ND2  1 
ATOM   7402 N  N    . LEU   B 1 385 ? -15.534 -62.585 -30.129 1.00 31.30  ?  387 LEU   I N    1 
ATOM   7403 C  CA   . LEU   B 1 385 ? -16.098 -62.247 -31.428 1.00 30.35  ?  387 LEU   I CA   1 
ATOM   7404 C  C    . LEU   B 1 385 ? -15.063 -61.686 -32.396 1.00 28.75  ?  387 LEU   I C    1 
ATOM   7405 O  O    . LEU   B 1 385 ? -15.063 -62.027 -33.569 1.00 26.57  ?  387 LEU   I O    1 
ATOM   7406 C  CB   . LEU   B 1 385 ? -17.237 -61.241 -31.312 1.00 32.50  ?  387 LEU   I CB   1 
ATOM   7407 C  CG   . LEU   B 1 385 ? -18.666 -61.636 -30.978 1.00 34.59  ?  387 LEU   I CG   1 
ATOM   7408 C  CD1  . LEU   B 1 385 ? -19.577 -60.618 -31.674 1.00 36.07  ?  387 LEU   I CD1  1 
ATOM   7409 C  CD2  . LEU   B 1 385 ? -19.073 -63.042 -31.397 1.00 36.19  ?  387 LEU   I CD2  1 
ATOM   7410 N  N    . ILE   B 1 386 ? -14.222 -60.790 -31.919 1.00 25.37  ?  388 ILE   I N    1 
ATOM   7411 C  CA   . ILE   B 1 386 ? -13.189 -60.229 -32.744 1.00 28.30  ?  388 ILE   I CA   1 
ATOM   7412 C  C    . ILE   B 1 386 ? -12.092 -61.275 -33.080 1.00 28.64  ?  388 ILE   I C    1 
ATOM   7413 O  O    . ILE   B 1 386 ? -11.674 -61.365 -34.236 1.00 30.21  ?  388 ILE   I O    1 
ATOM   7414 C  CB   . ILE   B 1 386 ? -12.635 -58.905 -32.137 1.00 29.81  ?  388 ILE   I CB   1 
ATOM   7415 C  CG1  . ILE   B 1 386 ? -13.759 -57.849 -32.075 1.00 31.48  ?  388 ILE   I CG1  1 
ATOM   7416 C  CG2  . ILE   B 1 386 ? -11.467 -58.371 -32.941 1.00 27.63  ?  388 ILE   I CG2  1 
ATOM   7417 C  CD1  . ILE   B 1 386 ? -13.552 -56.774 -31.014 1.00 34.78  ?  388 ILE   I CD1  1 
ATOM   7418 N  N    . LYS   B 1 387 ? -11.672 -62.095 -32.132 1.00 29.15  ?  389 LYS   I N    1 
ATOM   7419 C  CA   . LYS   B 1 387 ? -10.809 -63.224 -32.487 1.00 33.34  ?  389 LYS   I CA   1 
ATOM   7420 C  C    . LYS   B 1 387 ? -11.405 -64.052 -33.621 1.00 32.01  ?  389 LYS   I C    1 
ATOM   7421 O  O    . LYS   B 1 387 ? -10.814 -64.169 -34.671 1.00 32.22  ?  389 LYS   I O    1 
ATOM   7422 C  CB   . LYS   B 1 387 ? -10.547 -64.162 -31.311 1.00 34.22  ?  389 LYS   I CB   1 
ATOM   7423 N  N    . GLN   B 1 388 ? -12.601 -64.576 -33.425 1.00 34.96  ?  390 GLN   I N    1 
ATOM   7424 C  CA   . GLN   B 1 388 ? -13.178 -65.507 -34.397 1.00 36.25  ?  390 GLN   I CA   1 
ATOM   7425 C  C    . GLN   B 1 388 ? -13.206 -64.830 -35.777 1.00 37.85  ?  390 GLN   I C    1 
ATOM   7426 O  O    . GLN   B 1 388 ? -12.585 -65.309 -36.721 1.00 35.94  ?  390 GLN   I O    1 
ATOM   7427 C  CB   . GLN   B 1 388 ? -14.577 -65.975 -33.957 1.00 39.17  ?  390 GLN   I CB   1 
ATOM   7428 C  CG   . GLN   B 1 388 ? -14.888 -67.437 -34.223 1.00 42.46  ?  390 GLN   I CG   1 
ATOM   7429 C  CD   . GLN   B 1 388 ? -14.333 -68.364 -33.148 1.00 44.84  ?  390 GLN   I CD   1 
ATOM   7430 O  OE1  . GLN   B 1 388 ? -15.056 -69.203 -32.607 1.00 46.94  ?  390 GLN   I OE1  1 
ATOM   7431 N  NE2  . GLN   B 1 388 ? -13.044 -68.220 -32.838 1.00 48.37  ?  390 GLN   I NE2  1 
ATOM   7432 N  N    . ASN   B 1 389 ? -13.868 -63.677 -35.852 1.00 37.79  ?  391 ASN   I N    1 
ATOM   7433 C  CA   . ASN   B 1 389 ? -14.012 -62.923 -37.101 1.00 36.86  ?  391 ASN   I CA   1 
ATOM   7434 C  C    . ASN   B 1 389 ? -12.661 -62.463 -37.716 1.00 37.16  ?  391 ASN   I C    1 
ATOM   7435 O  O    . ASN   B 1 389 ? -12.537 -62.417 -38.975 1.00 38.52  ?  391 ASN   I O    1 
ATOM   7436 C  CB   . ASN   B 1 389 ? -15.003 -61.732 -36.921 1.00 34.25  ?  391 ASN   I CB   1 
ATOM   7437 C  CG   . ASN   B 1 389 ? -16.478 -62.170 -36.917 1.00 34.73  ?  391 ASN   I CG   1 
ATOM   7438 O  OD1  . ASN   B 1 389 ? -17.029 -62.533 -37.956 1.00 31.27  ?  391 ASN   I OD1  1 
ATOM   7439 N  ND2  . ASN   B 1 389 ? -17.125 -62.102 -35.759 1.00 32.18  ?  391 ASN   I ND2  1 
ATOM   7440 N  N    . CYS   B 1 390 ? -11.669 -62.109 -36.886 1.00 34.93  ?  392 CYS   I N    1 
ATOM   7441 C  CA   . CYS   B 1 390 ? -10.354 -61.700 -37.445 1.00 34.94  ?  392 CYS   I CA   1 
ATOM   7442 C  C    . CYS   B 1 390 ? -9.531  -62.919 -37.869 1.00 32.17  ?  392 CYS   I C    1 
ATOM   7443 O  O    . CYS   B 1 390 ? -8.824  -62.827 -38.848 1.00 28.68  ?  392 CYS   I O    1 
ATOM   7444 C  CB   . CYS   B 1 390 ? -9.537  -60.793 -36.528 1.00 36.75  ?  392 CYS   I CB   1 
ATOM   7445 S  SG   . CYS   B 1 390 ? -10.063 -59.052 -36.428 1.00 39.37  ?  392 CYS   I SG   1 
ATOM   7446 N  N    . GLU   B 1 391 ? -9.620  -64.034 -37.136 1.00 32.04  ?  393 GLU   I N    1 
ATOM   7447 C  CA   . GLU   B 1 391 ? -9.104  -65.338 -37.609 1.00 36.47  ?  393 GLU   I CA   1 
ATOM   7448 C  C    . GLU   B 1 391 ? -9.709  -65.686 -38.968 1.00 36.64  ?  393 GLU   I C    1 
ATOM   7449 O  O    . GLU   B 1 391 ? -8.991  -66.118 -39.866 1.00 37.47  ?  393 GLU   I O    1 
ATOM   7450 C  CB   . GLU   B 1 391 ? -9.387  -66.497 -36.606 1.00 41.24  ?  393 GLU   I CB   1 
ATOM   7451 C  CG   . GLU   B 1 391 ? -8.527  -66.500 -35.313 1.00 46.30  ?  393 GLU   I CG   1 
ATOM   7452 C  CD   . GLU   B 1 391 ? -8.978  -67.505 -34.225 1.00 51.46  ?  393 GLU   I CD   1 
ATOM   7453 O  OE1  . GLU   B 1 391 ? -8.253  -67.670 -33.207 1.00 51.10  ?  393 GLU   I OE1  1 
ATOM   7454 O  OE2  . GLU   B 1 391 ? -10.061 -68.134 -34.360 1.00 55.80  ?  393 GLU   I OE2  1 
ATOM   7455 N  N    . LEU   B 1 392 ? -11.017 -65.447 -39.113 1.00 38.58  ?  394 LEU   I N    1 
ATOM   7456 C  CA   . LEU   B 1 392 ? -11.756 -65.695 -40.356 1.00 40.64  ?  394 LEU   I CA   1 
ATOM   7457 C  C    . LEU   B 1 392 ? -11.293 -64.781 -41.465 1.00 39.81  ?  394 LEU   I C    1 
ATOM   7458 O  O    . LEU   B 1 392 ? -11.061 -65.239 -42.598 1.00 41.01  ?  394 LEU   I O    1 
ATOM   7459 C  CB   . LEU   B 1 392 ? -13.282 -65.533 -40.163 1.00 41.45  ?  394 LEU   I CB   1 
ATOM   7460 C  CG   . LEU   B 1 392 ? -14.270 -66.026 -41.237 1.00 41.50  ?  394 LEU   I CG   1 
ATOM   7461 C  CD1  . LEU   B 1 392 ? -14.034 -67.481 -41.652 1.00 43.84  ?  394 LEU   I CD1  1 
ATOM   7462 C  CD2  . LEU   B 1 392 ? -15.706 -65.856 -40.740 1.00 38.93  ?  394 LEU   I CD2  1 
ATOM   7463 N  N    . PHE   B 1 393 ? -11.164 -63.493 -41.161 1.00 38.01  ?  395 PHE   I N    1 
ATOM   7464 C  CA   . PHE   B 1 393 ? -10.614 -62.549 -42.135 1.00 37.58  ?  395 PHE   I CA   1 
ATOM   7465 C  C    . PHE   B 1 393 ? -9.200  -62.956 -42.582 1.00 38.36  ?  395 PHE   I C    1 
ATOM   7466 O  O    . PHE   B 1 393 ? -8.890  -62.839 -43.753 1.00 38.73  ?  395 PHE   I O    1 
ATOM   7467 C  CB   . PHE   B 1 393 ? -10.631 -61.125 -41.584 1.00 38.51  ?  395 PHE   I CB   1 
ATOM   7468 C  CG   . PHE   B 1 393 ? -9.885  -60.138 -42.429 1.00 38.89  ?  395 PHE   I CG   1 
ATOM   7469 C  CD1  . PHE   B 1 393 ? -8.496  -59.987 -42.290 1.00 39.98  ?  395 PHE   I CD1  1 
ATOM   7470 C  CD2  . PHE   B 1 393 ? -10.554 -59.370 -43.362 1.00 39.25  ?  395 PHE   I CD2  1 
ATOM   7471 C  CE1  . PHE   B 1 393 ? -7.798  -59.088 -43.078 1.00 43.21  ?  395 PHE   I CE1  1 
ATOM   7472 C  CE2  . PHE   B 1 393 ? -9.866  -58.462 -44.157 1.00 42.42  ?  395 PHE   I CE2  1 
ATOM   7473 C  CZ   . PHE   B 1 393 ? -8.482  -58.313 -44.010 1.00 44.40  ?  395 PHE   I CZ   1 
ATOM   7474 N  N    . GLU   B 1 394 ? -8.373  -63.438 -41.649 1.00 39.78  ?  396 GLU   I N    1 
ATOM   7475 C  CA   . GLU   B 1 394 ? -7.015  -63.932 -41.942 1.00 44.77  ?  396 GLU   I CA   1 
ATOM   7476 C  C    . GLU   B 1 394 ? -6.944  -65.067 -42.975 1.00 47.73  ?  396 GLU   I C    1 
ATOM   7477 O  O    . GLU   B 1 394 ? -6.038  -65.089 -43.816 1.00 45.15  ?  396 GLU   I O    1 
ATOM   7478 C  CB   . GLU   B 1 394 ? -6.342  -64.431 -40.654 1.00 45.67  ?  396 GLU   I CB   1 
ATOM   7479 N  N    . GLN   B 1 395 ? -7.873  -66.018 -42.884 1.00 49.72  ?  397 GLN   I N    1 
ATOM   7480 C  CA   . GLN   B 1 395 ? -7.872  -67.189 -43.777 1.00 51.60  ?  397 GLN   I CA   1 
ATOM   7481 C  C    . GLN   B 1 395 ? -8.301  -66.797 -45.183 1.00 50.53  ?  397 GLN   I C    1 
ATOM   7482 O  O    . GLN   B 1 395 ? -7.649  -67.160 -46.162 1.00 48.97  ?  397 GLN   I O    1 
ATOM   7483 C  CB   . GLN   B 1 395 ? -8.804  -68.278 -43.265 1.00 51.84  ?  397 GLN   I CB   1 
ATOM   7484 C  CG   . GLN   B 1 395 ? -8.403  -68.879 -41.934 1.00 52.83  ?  397 GLN   I CG   1 
ATOM   7485 C  CD   . GLN   B 1 395 ? -9.568  -69.564 -41.238 1.00 57.53  ?  397 GLN   I CD   1 
ATOM   7486 O  OE1  . GLN   B 1 395 ? -9.962  -70.669 -41.613 1.00 60.84  ?  397 GLN   I OE1  1 
ATOM   7487 N  NE2  . GLN   B 1 395 ? -10.131 -68.906 -40.219 1.00 58.04  ?  397 GLN   I NE2  1 
ATOM   7488 N  N    . LEU   B 1 396 ? -9.387  -66.032 -45.265 1.00 48.02  ?  398 LEU   I N    1 
ATOM   7489 C  CA   . LEU   B 1 396 ? -9.984  -65.655 -46.542 1.00 45.75  ?  398 LEU   I CA   1 
ATOM   7490 C  C    . LEU   B 1 396 ? -10.237 -64.167 -46.623 1.00 46.01  ?  398 LEU   I C    1 
ATOM   7491 O  O    . LEU   B 1 396 ? -11.356 -63.722 -46.431 1.00 51.24  ?  398 LEU   I O    1 
ATOM   7492 C  CB   . LEU   B 1 396 ? -11.258 -66.455 -46.795 1.00 46.68  ?  398 LEU   I CB   1 
ATOM   7493 C  CG   . LEU   B 1 396 ? -12.203 -66.856 -45.657 1.00 45.63  ?  398 LEU   I CG   1 
ATOM   7494 C  CD1  . LEU   B 1 396 ? -13.419 -65.958 -45.492 1.00 45.72  ?  398 LEU   I CD1  1 
ATOM   7495 C  CD2  . LEU   B 1 396 ? -12.671 -68.275 -45.924 1.00 46.00  ?  398 LEU   I CD2  1 
ATOM   7496 N  N    . GLY   B 1 397 ? -9.165  -63.427 -46.916 1.00 40.80  ?  399 GLY   I N    1 
ATOM   7497 C  CA   . GLY   B 1 397 ? -9.117  -61.978 -47.185 1.00 35.40  ?  399 GLY   I CA   1 
ATOM   7498 C  C    . GLY   B 1 397 ? -10.392 -61.192 -47.251 1.00 35.60  ?  399 GLY   I C    1 
ATOM   7499 O  O    . GLY   B 1 397 ? -11.455 -61.708 -46.949 1.00 37.77  ?  399 GLY   I O    1 
ATOM   7500 N  N    . GLU   B 1 398 ? -10.316 -59.931 -47.648 1.00 31.88  ?  400 GLU   I N    1 
ATOM   7501 C  CA   . GLU   B 1 398 ? -11.479 -59.080 -47.491 1.00 32.38  ?  400 GLU   I CA   1 
ATOM   7502 C  C    . GLU   B 1 398 ? -12.702 -59.560 -48.270 1.00 32.41  ?  400 GLU   I C    1 
ATOM   7503 O  O    . GLU   B 1 398 ? -13.728 -59.820 -47.675 1.00 33.21  ?  400 GLU   I O    1 
ATOM   7504 C  CB   . GLU   B 1 398 ? -11.185 -57.616 -47.854 1.00 31.70  ?  400 GLU   I CB   1 
ATOM   7505 C  CG   . GLU   B 1 398 ? -12.431 -56.728 -47.742 1.00 29.95  ?  400 GLU   I CG   1 
ATOM   7506 C  CD   . GLU   B 1 398 ? -12.158 -55.296 -48.110 1.00 33.01  ?  400 GLU   I CD   1 
ATOM   7507 O  OE1  . GLU   B 1 398 ? -11.439 -54.608 -47.367 1.00 39.12  ?  400 GLU   I OE1  1 
ATOM   7508 O  OE2  . GLU   B 1 398 ? -12.662 -54.844 -49.151 1.00 37.50  ?  400 GLU   I OE2  1 
ATOM   7509 N  N    . TYR   B 1 399 ? -12.574 -59.627 -49.597 1.00 35.18  ?  401 TYR   I N    1 
ATOM   7510 C  CA   . TYR   B 1 399 ? -13.674 -59.924 -50.519 1.00 32.88  ?  401 TYR   I CA   1 
ATOM   7511 C  C    . TYR   B 1 399 ? -14.352 -61.221 -50.138 1.00 31.14  ?  401 TYR   I C    1 
ATOM   7512 O  O    . TYR   B 1 399 ? -15.547 -61.277 -50.027 1.00 29.52  ?  401 TYR   I O    1 
ATOM   7513 C  CB   . TYR   B 1 399 ? -13.183 -59.985 -51.985 1.00 34.01  ?  401 TYR   I CB   1 
ATOM   7514 C  CG   . TYR   B 1 399 ? -14.204 -60.605 -52.920 1.00 34.49  ?  401 TYR   I CG   1 
ATOM   7515 C  CD1  . TYR   B 1 399 ? -15.374 -59.916 -53.248 1.00 32.73  ?  401 TYR   I CD1  1 
ATOM   7516 C  CD2  . TYR   B 1 399 ? -14.033 -61.905 -53.432 1.00 36.24  ?  401 TYR   I CD2  1 
ATOM   7517 C  CE1  . TYR   B 1 399 ? -16.337 -60.469 -54.076 1.00 32.80  ?  401 TYR   I CE1  1 
ATOM   7518 C  CE2  . TYR   B 1 399 ? -15.003 -62.468 -54.269 1.00 37.93  ?  401 TYR   I CE2  1 
ATOM   7519 C  CZ   . TYR   B 1 399 ? -16.151 -61.737 -54.587 1.00 34.92  ?  401 TYR   I CZ   1 
ATOM   7520 O  OH   . TYR   B 1 399 ? -17.130 -62.263 -55.394 1.00 35.46  ?  401 TYR   I OH   1 
ATOM   7521 N  N    . LYS   B 1 400 ? -13.573 -62.256 -49.910 1.00 32.25  ?  402 LYS   I N    1 
ATOM   7522 C  CA   . LYS   B 1 400 ? -14.137 -63.539 -49.535 1.00 33.79  ?  402 LYS   I CA   1 
ATOM   7523 C  C    . LYS   B 1 400 ? -14.537 -63.571 -48.041 1.00 32.51  ?  402 LYS   I C    1 
ATOM   7524 O  O    . LYS   B 1 400 ? -15.290 -64.455 -47.624 1.00 27.38  ?  402 LYS   I O    1 
ATOM   7525 C  CB   . LYS   B 1 400 ? -13.168 -64.663 -49.909 1.00 37.10  ?  402 LYS   I CB   1 
ATOM   7526 C  CG   . LYS   B 1 400 ? -12.834 -64.720 -51.403 1.00 37.28  ?  402 LYS   I CG   1 
ATOM   7527 N  N    . PHE   B 1 401 ? -14.046 -62.612 -47.250 1.00 30.29  ?  403 PHE   I N    1 
ATOM   7528 C  CA   . PHE   B 1 401 ? -14.627 -62.368 -45.911 1.00 31.23  ?  403 PHE   I CA   1 
ATOM   7529 C  C    . PHE   B 1 401 ? -16.026 -61.735 -46.024 1.00 30.05  ?  403 PHE   I C    1 
ATOM   7530 O  O    . PHE   B 1 401 ? -16.958 -62.179 -45.340 1.00 25.90  ?  403 PHE   I O    1 
ATOM   7531 C  CB   . PHE   B 1 401 ? -13.700 -61.479 -45.083 1.00 33.56  ?  403 PHE   I CB   1 
ATOM   7532 C  CG   . PHE   B 1 401 ? -14.169 -61.192 -43.691 1.00 31.01  ?  403 PHE   I CG   1 
ATOM   7533 C  CD1  . PHE   B 1 401 ? -14.384 -62.235 -42.788 1.00 31.10  ?  403 PHE   I CD1  1 
ATOM   7534 C  CD2  . PHE   B 1 401 ? -14.318 -59.877 -43.264 1.00 30.97  ?  403 PHE   I CD2  1 
ATOM   7535 C  CE1  . PHE   B 1 401 ? -14.776 -61.959 -41.486 1.00 32.05  ?  403 PHE   I CE1  1 
ATOM   7536 C  CE2  . PHE   B 1 401 ? -14.732 -59.592 -41.976 1.00 29.94  ?  403 PHE   I CE2  1 
ATOM   7537 C  CZ   . PHE   B 1 401 ? -14.936 -60.631 -41.080 1.00 31.16  ?  403 PHE   I CZ   1 
ATOM   7538 N  N    . GLN   B 1 402 ? -16.159 -60.716 -46.895 1.00 29.94  ?  404 GLN   I N    1 
ATOM   7539 C  CA   . GLN   B 1 402 ? -17.471 -60.109 -47.219 1.00 29.36  ?  404 GLN   I CA   1 
ATOM   7540 C  C    . GLN   B 1 402 ? -18.444 -61.174 -47.621 1.00 28.16  ?  404 GLN   I C    1 
ATOM   7541 O  O    . GLN   B 1 402 ? -19.607 -61.112 -47.268 1.00 28.66  ?  404 GLN   I O    1 
ATOM   7542 C  CB   . GLN   B 1 402 ? -17.407 -59.058 -48.351 1.00 31.54  ?  404 GLN   I CB   1 
ATOM   7543 C  CG   . GLN   B 1 402 ? -16.773 -57.717 -47.981 1.00 33.23  ?  404 GLN   I CG   1 
ATOM   7544 C  CD   . GLN   B 1 402 ? -16.337 -56.874 -49.181 1.00 35.08  ?  404 GLN   I CD   1 
ATOM   7545 O  OE1  . GLN   B 1 402 ? -15.519 -57.288 -49.977 1.00 37.21  ?  404 GLN   I OE1  1 
ATOM   7546 N  NE2  . GLN   B 1 402 ? -16.849 -55.662 -49.273 1.00 40.68  ?  404 GLN   I NE2  1 
ATOM   7547 N  N    . ASN   B 1 403 ? -17.976 -62.155 -48.361 1.00 29.04  ?  405 ASN   I N    1 
ATOM   7548 C  CA   . ASN   B 1 403 ? -18.878 -63.184 -48.859 1.00 31.17  ?  405 ASN   I CA   1 
ATOM   7549 C  C    . ASN   B 1 403 ? -19.329 -64.131 -47.779 1.00 29.90  ?  405 ASN   I C    1 
ATOM   7550 O  O    . ASN   B 1 403 ? -20.493 -64.498 -47.771 1.00 30.37  ?  405 ASN   I O    1 
ATOM   7551 C  CB   . ASN   B 1 403 ? -18.281 -63.914 -50.060 1.00 31.93  ?  405 ASN   I CB   1 
ATOM   7552 C  CG   . ASN   B 1 403 ? -18.320 -63.067 -51.338 1.00 30.24  ?  405 ASN   I CG   1 
ATOM   7553 O  OD1  . ASN   B 1 403 ? -18.943 -62.027 -51.383 1.00 26.17  ?  405 ASN   I OD1  1 
ATOM   7554 N  ND2  . ASN   B 1 403 ? -17.640 -63.535 -52.374 1.00 28.64  ?  405 ASN   I ND2  1 
ATOM   7555 N  N    . ALA   B 1 404 ? -18.427 -64.493 -46.871 1.00 28.83  ?  406 ALA   I N    1 
ATOM   7556 C  CA   . ALA   B 1 404 ? -18.770 -65.213 -45.646 1.00 29.94  ?  406 ALA   I CA   1 
ATOM   7557 C  C    . ALA   B 1 404 ? -19.811 -64.484 -44.808 1.00 31.47  ?  406 ALA   I C    1 
ATOM   7558 O  O    . ALA   B 1 404 ? -20.783 -65.097 -44.334 1.00 32.28  ?  406 ALA   I O    1 
ATOM   7559 C  CB   . ALA   B 1 404 ? -17.523 -65.452 -44.811 1.00 31.82  ?  406 ALA   I CB   1 
ATOM   7560 N  N    . LEU   B 1 405 ? -19.604 -63.173 -44.636 1.00 29.73  ?  407 LEU   I N    1 
ATOM   7561 C  CA   . LEU   B 1 405 ? -20.512 -62.363 -43.850 1.00 28.41  ?  407 LEU   I CA   1 
ATOM   7562 C  C    . LEU   B 1 405 ? -21.901 -62.291 -44.454 1.00 26.89  ?  407 LEU   I C    1 
ATOM   7563 O  O    . LEU   B 1 405 ? -22.911 -62.337 -43.713 1.00 22.56  ?  407 LEU   I O    1 
ATOM   7564 C  CB   . LEU   B 1 405 ? -19.981 -60.940 -43.703 1.00 29.26  ?  407 LEU   I CB   1 
ATOM   7565 C  CG   . LEU   B 1 405 ? -18.771 -60.744 -42.799 1.00 29.68  ?  407 LEU   I CG   1 
ATOM   7566 C  CD1  . LEU   B 1 405 ? -18.435 -59.265 -42.736 1.00 29.49  ?  407 LEU   I CD1  1 
ATOM   7567 C  CD2  . LEU   B 1 405 ? -19.052 -61.273 -41.409 1.00 30.16  ?  407 LEU   I CD2  1 
ATOM   7568 N  N    . LEU   B 1 406 ? -21.919 -62.208 -45.791 1.00 25.38  ?  408 LEU   I N    1 
ATOM   7569 C  CA   . LEU   B 1 406 ? -23.115 -62.040 -46.580 1.00 27.72  ?  408 LEU   I CA   1 
ATOM   7570 C  C    . LEU   B 1 406 ? -23.988 -63.283 -46.533 1.00 24.64  ?  408 LEU   I C    1 
ATOM   7571 O  O    . LEU   B 1 406 ? -25.212 -63.199 -46.431 1.00 23.02  ?  408 LEU   I O    1 
ATOM   7572 C  CB   . LEU   B 1 406 ? -22.691 -61.727 -48.018 1.00 33.48  ?  408 LEU   I CB   1 
ATOM   7573 C  CG   . LEU   B 1 406 ? -23.593 -61.018 -49.007 1.00 38.00  ?  408 LEU   I CG   1 
ATOM   7574 C  CD1  . LEU   B 1 406 ? -24.183 -59.721 -48.479 1.00 40.43  ?  408 LEU   I CD1  1 
ATOM   7575 C  CD2  . LEU   B 1 406 ? -22.790 -60.716 -50.263 1.00 40.89  ?  408 LEU   I CD2  1 
ATOM   7576 N  N    . VAL   B 1 407 ? -23.360 -64.442 -46.578 1.00 24.09  ?  409 VAL   I N    1 
ATOM   7577 C  CA   . VAL   B 1 407 ? -24.106 -65.697 -46.386 1.00 27.58  ?  409 VAL   I CA   1 
ATOM   7578 C  C    . VAL   B 1 407 ? -24.693 -65.703 -44.988 1.00 28.79  ?  409 VAL   I C    1 
ATOM   7579 O  O    . VAL   B 1 407 ? -25.869 -66.029 -44.823 1.00 31.54  ?  409 VAL   I O    1 
ATOM   7580 C  CB   . VAL   B 1 407 ? -23.223 -66.947 -46.598 1.00 28.28  ?  409 VAL   I CB   1 
ATOM   7581 C  CG1  . VAL   B 1 407 ? -23.931 -68.214 -46.130 1.00 30.31  ?  409 VAL   I CG1  1 
ATOM   7582 C  CG2  . VAL   B 1 407 ? -22.806 -67.067 -48.075 1.00 30.77  ?  409 VAL   I CG2  1 
ATOM   7583 N  N    . ARG   B 1 408 ? -23.854 -65.369 -43.995 1.00 29.79  ?  410 ARG   I N    1 
ATOM   7584 C  CA   . ARG   B 1 408 ? -24.248 -65.316 -42.567 1.00 29.91  ?  410 ARG   I CA   1 
ATOM   7585 C  C    . ARG   B 1 408 ? -25.433 -64.425 -42.269 1.00 28.06  ?  410 ARG   I C    1 
ATOM   7586 O  O    . ARG   B 1 408 ? -26.367 -64.861 -41.640 1.00 25.61  ?  410 ARG   I O    1 
ATOM   7587 C  CB   . ARG   B 1 408 ? -23.053 -64.873 -41.717 1.00 31.19  ?  410 ARG   I CB   1 
ATOM   7588 C  CG   . ARG   B 1 408 ? -23.302 -64.810 -40.207 1.00 36.57  ?  410 ARG   I CG   1 
ATOM   7589 C  CD   . ARG   B 1 408 ? -21.997 -64.969 -39.416 1.00 39.23  ?  410 ARG   I CD   1 
ATOM   7590 N  NE   . ARG   B 1 408 ? -21.476 -63.719 -38.858 1.00 41.83  ?  410 ARG   I NE   1 
ATOM   7591 C  CZ   . ARG   B 1 408 ? -20.177 -63.415 -38.666 1.00 42.83  ?  410 ARG   I CZ   1 
ATOM   7592 N  NH1  . ARG   B 1 408 ? -19.185 -64.238 -39.039 1.00 43.29  ?  410 ARG   I NH1  1 
ATOM   7593 N  NH2  . ARG   B 1 408 ? -19.855 -62.246 -38.113 1.00 40.99  ?  410 ARG   I NH2  1 
ATOM   7594 N  N    . TYR   B 1 409 ? -25.401 -63.171 -42.731 1.00 30.20  ?  411 TYR   I N    1 
ATOM   7595 C  CA   . TYR   B 1 409 ? -26.509 -62.237 -42.457 1.00 29.87  ?  411 TYR   I CA   1 
ATOM   7596 C  C    . TYR   B 1 409 ? -27.782 -62.461 -43.287 1.00 30.72  ?  411 TYR   I C    1 
ATOM   7597 O  O    . TYR   B 1 409 ? -28.894 -62.281 -42.776 1.00 30.37  ?  411 TYR   I O    1 
ATOM   7598 C  CB   . TYR   B 1 409 ? -26.034 -60.792 -42.547 1.00 32.09  ?  411 TYR   I CB   1 
ATOM   7599 C  CG   . TYR   B 1 409 ? -24.868 -60.520 -41.637 1.00 33.71  ?  411 TYR   I CG   1 
ATOM   7600 C  CD1  . TYR   B 1 409 ? -24.878 -60.935 -40.292 1.00 34.30  ?  411 TYR   I CD1  1 
ATOM   7601 C  CD2  . TYR   B 1 409 ? -23.749 -59.855 -42.106 1.00 32.90  ?  411 TYR   I CD2  1 
ATOM   7602 C  CE1  . TYR   B 1 409 ? -23.805 -60.673 -39.462 1.00 35.51  ?  411 TYR   I CE1  1 
ATOM   7603 C  CE2  . TYR   B 1 409 ? -22.688 -59.603 -41.279 1.00 33.87  ?  411 TYR   I CE2  1 
ATOM   7604 C  CZ   . TYR   B 1 409 ? -22.716 -60.025 -39.977 1.00 33.11  ?  411 TYR   I CZ   1 
ATOM   7605 O  OH   . TYR   B 1 409 ? -21.646 -59.777 -39.206 1.00 37.95  ?  411 TYR   I OH   1 
ATOM   7606 N  N    . THR   B 1 410 ? -27.622 -62.879 -44.538 1.00 30.95  ?  412 THR   I N    1 
ATOM   7607 C  CA   . THR   B 1 410 ? -28.752 -63.245 -45.369 1.00 31.32  ?  412 THR   I CA   1 
ATOM   7608 C  C    . THR   B 1 410 ? -29.556 -64.394 -44.745 1.00 30.83  ?  412 THR   I C    1 
ATOM   7609 O  O    . THR   B 1 410 ? -30.785 -64.404 -44.828 1.00 28.90  ?  412 THR   I O    1 
ATOM   7610 C  CB   . THR   B 1 410 ? -28.298 -63.691 -46.789 1.00 32.03  ?  412 THR   I CB   1 
ATOM   7611 O  OG1  . THR   B 1 410 ? -27.408 -62.712 -47.363 1.00 31.59  ?  412 THR   I OG1  1 
ATOM   7612 C  CG2  . THR   B 1 410 ? -29.501 -63.876 -47.687 1.00 32.12  ?  412 THR   I CG2  1 
ATOM   7613 N  N    . LYS   B 1 411 ? -28.874 -65.353 -44.142 1.00 30.83  ?  413 LYS   I N    1 
ATOM   7614 C  CA   . LYS   B 1 411 ? -29.576 -66.441 -43.410 1.00 35.89  ?  413 LYS   I CA   1 
ATOM   7615 C  C    . LYS   B 1 411 ? -30.299 -65.936 -42.141 1.00 38.70  ?  413 LYS   I C    1 
ATOM   7616 O  O    . LYS   B 1 411 ? -31.434 -66.358 -41.828 1.00 40.95  ?  413 LYS   I O    1 
ATOM   7617 C  CB   . LYS   B 1 411 ? -28.625 -67.584 -43.075 1.00 37.57  ?  413 LYS   I CB   1 
ATOM   7618 C  CG   . LYS   B 1 411 ? -28.326 -68.501 -44.266 1.00 40.61  ?  413 LYS   I CG   1 
ATOM   7619 C  CD   . LYS   B 1 411 ? -27.284 -69.544 -43.930 1.00 42.03  ?  413 LYS   I CD   1 
ATOM   7620 C  CE   . LYS   B 1 411 ? -26.904 -70.338 -45.168 1.00 46.20  ?  413 LYS   I CE   1 
ATOM   7621 N  NZ   . LYS   B 1 411 ? -25.991 -71.483 -44.872 1.00 50.40  ?  413 LYS   I NZ   1 
ATOM   7622 N  N    . LYS   B 1 412 ? -29.665 -65.005 -41.436 1.00 36.26  ?  414 LYS   I N    1 
ATOM   7623 C  CA   . LYS   B 1 412 ? -30.265 -64.443 -40.215 1.00 34.23  ?  414 LYS   I CA   1 
ATOM   7624 C  C    . LYS   B 1 412 ? -31.490 -63.587 -40.495 1.00 34.21  ?  414 LYS   I C    1 
ATOM   7625 O  O    . LYS   B 1 412 ? -32.449 -63.644 -39.756 1.00 36.46  ?  414 LYS   I O    1 
ATOM   7626 C  CB   . LYS   B 1 412 ? -29.212 -63.652 -39.419 1.00 34.34  ?  414 LYS   I CB   1 
ATOM   7627 C  CG   . LYS   B 1 412 ? -28.087 -64.535 -38.892 1.00 35.58  ?  414 LYS   I CG   1 
ATOM   7628 C  CD   . LYS   B 1 412 ? -26.804 -63.769 -38.658 1.00 37.83  ?  414 LYS   I CD   1 
ATOM   7629 C  CE   . LYS   B 1 412 ? -25.867 -64.522 -37.727 1.00 40.69  ?  414 LYS   I CE   1 
ATOM   7630 N  NZ   . LYS   B 1 412 ? -26.256 -64.453 -36.288 1.00 43.10  ?  414 LYS   I NZ   1 
ATOM   7631 N  N    . VAL   B 1 413 ? -31.446 -62.779 -41.553 1.00 35.86  ?  415 VAL   I N    1 
ATOM   7632 C  CA   . VAL   B 1 413 ? -32.498 -61.807 -41.857 1.00 34.28  ?  415 VAL   I CA   1 
ATOM   7633 C  C    . VAL   B 1 413 ? -32.716 -61.708 -43.380 1.00 33.10  ?  415 VAL   I C    1 
ATOM   7634 O  O    . VAL   B 1 413 ? -32.537 -60.649 -43.976 1.00 29.28  ?  415 VAL   I O    1 
ATOM   7635 C  CB   . VAL   B 1 413 ? -32.157 -60.409 -41.275 1.00 36.30  ?  415 VAL   I CB   1 
ATOM   7636 C  CG1  . VAL   B 1 413 ? -33.414 -59.562 -41.190 1.00 39.75  ?  415 VAL   I CG1  1 
ATOM   7637 C  CG2  . VAL   B 1 413 ? -31.522 -60.522 -39.901 1.00 35.44  ?  415 VAL   I CG2  1 
ATOM   7638 N  N    . PRO   B 1 414 ? -33.153 -62.818 -44.014 1.00 36.62  ?  416 PRO   I N    1 
ATOM   7639 C  CA   . PRO   B 1 414 ? -33.383 -62.854 -45.474 1.00 37.14  ?  416 PRO   I CA   1 
ATOM   7640 C  C    . PRO   B 1 414 ? -34.510 -61.970 -46.009 1.00 34.51  ?  416 PRO   I C    1 
ATOM   7641 O  O    . PRO   B 1 414 ? -34.638 -61.881 -47.217 1.00 36.98  ?  416 PRO   I O    1 
ATOM   7642 C  CB   . PRO   B 1 414 ? -33.688 -64.338 -45.769 1.00 39.26  ?  416 PRO   I CB   1 
ATOM   7643 C  CG   . PRO   B 1 414 ? -34.104 -64.920 -44.468 1.00 39.60  ?  416 PRO   I CG   1 
ATOM   7644 C  CD   . PRO   B 1 414 ? -33.434 -64.118 -43.376 1.00 38.65  ?  416 PRO   I CD   1 
ATOM   7645 N  N    . GLN   B 1 415 ? -35.308 -61.341 -45.145 1.00 36.26  ?  417 GLN   I N    1 
ATOM   7646 C  CA   . GLN   B 1 415 ? -36.341 -60.371 -45.576 1.00 41.18  ?  417 GLN   I CA   1 
ATOM   7647 C  C    . GLN   B 1 415 ? -35.731 -59.023 -45.982 1.00 42.04  ?  417 GLN   I C    1 
ATOM   7648 O  O    . GLN   B 1 415 ? -36.382 -58.214 -46.638 1.00 45.01  ?  417 GLN   I O    1 
ATOM   7649 C  CB   . GLN   B 1 415 ? -37.382 -60.105 -44.461 1.00 42.61  ?  417 GLN   I CB   1 
ATOM   7650 C  CG   . GLN   B 1 415 ? -38.116 -61.335 -43.925 1.00 43.67  ?  417 GLN   I CG   1 
ATOM   7651 C  CD   . GLN   B 1 415 ? -37.372 -62.081 -42.827 1.00 45.32  ?  417 GLN   I CD   1 
ATOM   7652 O  OE1  . GLN   B 1 415 ? -36.409 -61.575 -42.246 1.00 45.46  ?  417 GLN   I OE1  1 
ATOM   7653 N  NE2  . GLN   B 1 415 ? -37.802 -63.307 -42.556 1.00 44.07  ?  417 GLN   I NE2  1 
ATOM   7654 N  N    . VAL   B 1 416 ? -34.503 -58.769 -45.544 1.00 40.08  ?  418 VAL   I N    1 
ATOM   7655 C  CA   . VAL   B 1 416 ? -33.802 -57.525 -45.836 1.00 39.82  ?  418 VAL   I CA   1 
ATOM   7656 C  C    . VAL   B 1 416 ? -33.494 -57.491 -47.324 1.00 41.42  ?  418 VAL   I C    1 
ATOM   7657 O  O    . VAL   B 1 416 ? -33.325 -58.537 -47.959 1.00 41.81  ?  418 VAL   I O    1 
ATOM   7658 C  CB   . VAL   B 1 416 ? -32.540 -57.386 -44.927 1.00 38.19  ?  418 VAL   I CB   1 
ATOM   7659 C  CG1  . VAL   B 1 416 ? -31.595 -56.284 -45.357 1.00 36.94  ?  418 VAL   I CG1  1 
ATOM   7660 C  CG2  . VAL   B 1 416 ? -32.990 -57.102 -43.508 1.00 39.86  ?  418 VAL   I CG2  1 
ATOM   7661 N  N    . SER   B 1 417 ? -33.487 -56.272 -47.865 1.00 42.89  ?  419 SER   I N    1 
ATOM   7662 C  CA   . SER   B 1 417 ? -33.230 -56.006 -49.277 1.00 41.75  ?  419 SER   I CA   1 
ATOM   7663 C  C    . SER   B 1 417 ? -31.830 -56.465 -49.636 1.00 39.14  ?  419 SER   I C    1 
ATOM   7664 O  O    . SER   B 1 417 ? -30.881 -56.240 -48.869 1.00 37.64  ?  419 SER   I O    1 
ATOM   7665 C  CB   . SER   B 1 417 ? -33.342 -54.499 -49.561 1.00 44.54  ?  419 SER   I CB   1 
ATOM   7666 O  OG   . SER   B 1 417 ? -33.297 -54.217 -50.945 1.00 47.53  ?  419 SER   I OG   1 
ATOM   7667 N  N    . THR   B 1 418 ? -31.731 -57.114 -50.796 1.00 37.26  ?  420 THR   I N    1 
ATOM   7668 C  CA   . THR   B 1 418 ? -30.471 -57.598 -51.334 1.00 37.98  ?  420 THR   I CA   1 
ATOM   7669 C  C    . THR   B 1 418 ? -29.427 -56.461 -51.408 1.00 38.72  ?  420 THR   I C    1 
ATOM   7670 O  O    . THR   B 1 418 ? -28.285 -56.677 -51.013 1.00 32.26  ?  420 THR   I O    1 
ATOM   7671 C  CB   . THR   B 1 418 ? -30.642 -58.299 -52.726 1.00 37.58  ?  420 THR   I CB   1 
ATOM   7672 O  OG1  . THR   B 1 418 ? -31.527 -59.434 -52.634 1.00 34.17  ?  420 THR   I OG1  1 
ATOM   7673 C  CG2  . THR   B 1 418 ? -29.281 -58.773 -53.257 1.00 36.36  ?  420 THR   I CG2  1 
ATOM   7674 N  N    . PRO   B 1 419 ? -29.816 -55.263 -51.925 1.00 40.60  ?  421 PRO   I N    1 
ATOM   7675 C  CA   . PRO   B 1 419 ? -28.858 -54.128 -51.991 1.00 40.32  ?  421 PRO   I CA   1 
ATOM   7676 C  C    . PRO   B 1 419 ? -28.237 -53.781 -50.658 1.00 37.86  ?  421 PRO   I C    1 
ATOM   7677 O  O    . PRO   B 1 419 ? -27.012 -53.615 -50.577 1.00 40.63  ?  421 PRO   I O    1 
ATOM   7678 C  CB   . PRO   B 1 419 ? -29.717 -52.939 -52.473 1.00 42.24  ?  421 PRO   I CB   1 
ATOM   7679 C  CG   . PRO   B 1 419 ? -30.957 -53.544 -53.060 1.00 44.52  ?  421 PRO   I CG   1 
ATOM   7680 C  CD   . PRO   B 1 419 ? -30.985 -55.034 -52.797 1.00 40.49  ?  421 PRO   I CD   1 
ATOM   7681 N  N    . THR   B 1 420 ? -29.088 -53.702 -49.635 1.00 34.95  ?  422 THR   I N    1 
ATOM   7682 C  CA   . THR   B 1 420 ? -28.683 -53.382 -48.272 1.00 33.37  ?  422 THR   I CA   1 
ATOM   7683 C  C    . THR   B 1 420 ? -27.840 -54.488 -47.628 1.00 32.79  ?  422 THR   I C    1 
ATOM   7684 O  O    . THR   B 1 420 ? -26.894 -54.193 -46.921 1.00 29.63  ?  422 THR   I O    1 
ATOM   7685 C  CB   . THR   B 1 420 ? -29.924 -53.070 -47.410 1.00 34.60  ?  422 THR   I CB   1 
ATOM   7686 O  OG1  . THR   B 1 420 ? -30.564 -51.888 -47.911 1.00 41.90  ?  422 THR   I OG1  1 
ATOM   7687 C  CG2  . THR   B 1 420 ? -29.574 -52.845 -45.970 1.00 33.38  ?  422 THR   I CG2  1 
ATOM   7688 N  N    . LEU   B 1 421 ? -28.180 -55.754 -47.840 1.00 30.12  ?  423 LEU   I N    1 
ATOM   7689 C  CA   . LEU   B 1 421 ? -27.318 -56.822 -47.333 1.00 32.61  ?  423 LEU   I CA   1 
ATOM   7690 C  C    . LEU   B 1 421 ? -25.909 -56.742 -47.931 1.00 34.11  ?  423 LEU   I C    1 
ATOM   7691 O  O    . LEU   B 1 421 ? -24.914 -56.999 -47.238 1.00 33.72  ?  423 LEU   I O    1 
ATOM   7692 C  CB   . LEU   B 1 421 ? -27.886 -58.212 -47.642 1.00 33.15  ?  423 LEU   I CB   1 
ATOM   7693 C  CG   . LEU   B 1 421 ? -29.012 -58.654 -46.740 1.00 34.45  ?  423 LEU   I CG   1 
ATOM   7694 C  CD1  . LEU   B 1 421 ? -29.840 -59.711 -47.464 1.00 36.39  ?  423 LEU   I CD1  1 
ATOM   7695 C  CD2  . LEU   B 1 421 ? -28.417 -59.176 -45.446 1.00 35.42  ?  423 LEU   I CD2  1 
ATOM   7696 N  N    . VAL   B 1 422 ? -25.846 -56.438 -49.229 1.00 33.60  ?  424 VAL   I N    1 
ATOM   7697 C  CA   . VAL   B 1 422 ? -24.588 -56.338 -49.926 1.00 31.85  ?  424 VAL   I CA   1 
ATOM   7698 C  C    . VAL   B 1 422 ? -23.818 -55.175 -49.315 1.00 32.32  ?  424 VAL   I C    1 
ATOM   7699 O  O    . VAL   B 1 422 ? -22.766 -55.391 -48.745 1.00 35.31  ?  424 VAL   I O    1 
ATOM   7700 C  CB   . VAL   B 1 422 ? -24.786 -56.141 -51.445 1.00 30.98  ?  424 VAL   I CB   1 
ATOM   7701 C  CG1  . VAL   B 1 422 ? -23.464 -55.767 -52.118 1.00 28.41  ?  424 VAL   I CG1  1 
ATOM   7702 C  CG2  . VAL   B 1 422 ? -25.375 -57.418 -52.077 1.00 32.20  ?  424 VAL   I CG2  1 
ATOM   7703 N  N    . GLU   B 1 423 ? -24.357 -53.966 -49.419 1.00 32.55  ?  425 GLU   I N    1 
ATOM   7704 C  CA   . GLU   B 1 423 ? -23.686 -52.796 -48.914 1.00 33.20  ?  425 GLU   I CA   1 
ATOM   7705 C  C    . GLU   B 1 423 ? -23.174 -53.087 -47.500 1.00 33.98  ?  425 GLU   I C    1 
ATOM   7706 O  O    . GLU   B 1 423 ? -21.953 -53.139 -47.291 1.00 32.29  ?  425 GLU   I O    1 
ATOM   7707 C  CB   . GLU   B 1 423 ? -24.609 -51.577 -48.919 1.00 36.86  ?  425 GLU   I CB   1 
ATOM   7708 C  CG   . GLU   B 1 423 ? -23.917 -50.271 -48.497 1.00 36.50  ?  425 GLU   I CG   1 
ATOM   7709 N  N    . VAL   B 1 424 ? -24.066 -53.384 -46.558 1.00 33.92  ?  426 VAL   I N    1 
ATOM   7710 C  CA   . VAL   B 1 424 ? -23.637 -53.518 -45.143 1.00 37.41  ?  426 VAL   I CA   1 
ATOM   7711 C  C    . VAL   B 1 424 ? -22.635 -54.661 -44.851 1.00 34.45  ?  426 VAL   I C    1 
ATOM   7712 O  O    . VAL   B 1 424 ? -21.750 -54.508 -44.005 1.00 29.24  ?  426 VAL   I O    1 
ATOM   7713 C  CB   . VAL   B 1 424 ? -24.841 -53.541 -44.167 1.00 46.05  ?  426 VAL   I CB   1 
ATOM   7714 C  CG1  . VAL   B 1 424 ? -25.733 -52.306 -44.406 1.00 46.26  ?  426 VAL   I CG1  1 
ATOM   7715 C  CG2  . VAL   B 1 424 ? -25.623 -54.849 -44.260 1.00 47.12  ?  426 VAL   I CG2  1 
ATOM   7716 N  N    . SER   B 1 425 ? -22.726 -55.772 -45.594 1.00 34.24  ?  427 SER   I N    1 
ATOM   7717 C  CA   . SER   B 1 425 ? -21.666 -56.809 -45.532 1.00 32.88  ?  427 SER   I CA   1 
ATOM   7718 C  C    . SER   B 1 425 ? -20.354 -56.319 -46.144 1.00 32.08  ?  427 SER   I C    1 
ATOM   7719 O  O    . SER   B 1 425 ? -19.272 -56.693 -45.685 1.00 32.68  ?  427 SER   I O    1 
ATOM   7720 C  CB   . SER   B 1 425 ? -22.091 -58.089 -46.232 1.00 33.76  ?  427 SER   I CB   1 
ATOM   7721 O  OG   . SER   B 1 425 ? -23.347 -58.549 -45.745 1.00 33.88  ?  427 SER   I OG   1 
ATOM   7722 N  N    . ARG   B 1 426 ? -20.449 -55.500 -47.186 1.00 31.18  ?  428 ARG   I N    1 
ATOM   7723 C  CA   . ARG   B 1 426 ? -19.289 -54.856 -47.722 1.00 33.13  ?  428 ARG   I CA   1 
ATOM   7724 C  C    . ARG   B 1 426 ? -18.700 -53.985 -46.624 1.00 32.49  ?  428 ARG   I C    1 
ATOM   7725 O  O    . ARG   B 1 426 ? -17.541 -54.201 -46.240 1.00 36.24  ?  428 ARG   I O    1 
ATOM   7726 C  CB   . ARG   B 1 426 ? -19.568 -54.023 -49.002 1.00 33.83  ?  428 ARG   I CB   1 
ATOM   7727 C  CG   . ARG   B 1 426 ? -20.133 -54.808 -50.172 1.00 35.46  ?  428 ARG   I CG   1 
ATOM   7728 C  CD   . ARG   B 1 426 ? -19.999 -54.096 -51.506 1.00 37.19  ?  428 ARG   I CD   1 
ATOM   7729 N  NE   . ARG   B 1 426 ? -18.865 -54.672 -52.238 1.00 40.21  ?  428 ARG   I NE   1 
ATOM   7730 C  CZ   . ARG   B 1 426 ? -17.825 -54.016 -52.749 1.00 41.41  ?  428 ARG   I CZ   1 
ATOM   7731 N  NH1  . ARG   B 1 426 ? -17.727 -52.691 -52.726 1.00 44.96  ?  428 ARG   I NH1  1 
ATOM   7732 N  NH2  . ARG   B 1 426 ? -16.872 -54.710 -53.342 1.00 43.75  ?  428 ARG   I NH2  1 
ATOM   7733 N  N    . ASN   B 1 427 ? -19.493 -53.041 -46.113 1.00 29.22  ?  429 ASN   I N    1 
ATOM   7734 C  CA   . ASN   B 1 427 ? -19.054 -52.122 -45.007 1.00 31.70  ?  429 ASN   I CA   1 
ATOM   7735 C  C    . ASN   B 1 427 ? -18.447 -52.893 -43.799 1.00 31.67  ?  429 ASN   I C    1 
ATOM   7736 O  O    . ASN   B 1 427 ? -17.318 -52.621 -43.381 1.00 29.55  ?  429 ASN   I O    1 
ATOM   7737 C  CB   . ASN   B 1 427 ? -20.213 -51.201 -44.542 1.00 31.34  ?  429 ASN   I CB   1 
ATOM   7738 C  CG   . ASN   B 1 427 ? -20.635 -50.168 -45.605 1.00 31.98  ?  429 ASN   I CG   1 
ATOM   7739 O  OD1  . ASN   B 1 427 ? -19.924 -49.929 -46.566 1.00 35.10  ?  429 ASN   I OD1  1 
ATOM   7740 N  ND2  . ASN   B 1 427 ? -21.797 -49.565 -45.424 1.00 31.25  ?  429 ASN   I ND2  1 
ATOM   7741 N  N    . LEU   B 1 428 ? -19.155 -53.908 -43.304 1.00 31.43  ?  430 LEU   I N    1 
ATOM   7742 C  CA   . LEU   B 1 428 ? -18.609 -54.743 -42.210 1.00 31.42  ?  430 LEU   I CA   1 
ATOM   7743 C  C    . LEU   B 1 428 ? -17.265 -55.349 -42.544 1.00 32.08  ?  430 LEU   I C    1 
ATOM   7744 O  O    . LEU   B 1 428 ? -16.372 -55.416 -41.685 1.00 33.32  ?  430 LEU   I O    1 
ATOM   7745 C  CB   . LEU   B 1 428 ? -19.597 -55.837 -41.763 1.00 31.04  ?  430 LEU   I CB   1 
ATOM   7746 C  CG   . LEU   B 1 428 ? -20.505 -55.581 -40.543 1.00 31.74  ?  430 LEU   I CG   1 
ATOM   7747 C  CD1  . LEU   B 1 428 ? -20.706 -54.122 -40.213 1.00 31.42  ?  430 LEU   I CD1  1 
ATOM   7748 C  CD2  . LEU   B 1 428 ? -21.850 -56.277 -40.690 1.00 34.09  ?  430 LEU   I CD2  1 
ATOM   7749 N  N    . GLY   B 1 429 ? -17.112 -55.752 -43.793 1.00 32.15  ?  431 GLY   I N    1 
ATOM   7750 C  CA   . GLY   B 1 429 ? -15.886 -56.357 -44.262 1.00 32.76  ?  431 GLY   I CA   1 
ATOM   7751 C  C    . GLY   B 1 429 ? -14.691 -55.445 -44.289 1.00 32.43  ?  431 GLY   I C    1 
ATOM   7752 O  O    . GLY   B 1 429 ? -13.567 -55.864 -43.954 1.00 31.24  ?  431 GLY   I O    1 
ATOM   7753 N  N    . LYS   B 1 430 ? -14.922 -54.202 -44.690 1.00 34.28  ?  432 LYS   I N    1 
ATOM   7754 C  CA   . LYS   B 1 430 ? -13.890 -53.173 -44.633 1.00 35.97  ?  432 LYS   I CA   1 
ATOM   7755 C  C    . LYS   B 1 430 ? -13.404 -53.008 -43.187 1.00 38.52  ?  432 LYS   I C    1 
ATOM   7756 O  O    . LYS   B 1 430 ? -12.195 -52.922 -42.923 1.00 39.87  ?  432 LYS   I O    1 
ATOM   7757 C  CB   . LYS   B 1 430 ? -14.435 -51.834 -45.106 1.00 36.55  ?  432 LYS   I CB   1 
ATOM   7758 C  CG   . LYS   B 1 430 ? -14.902 -51.789 -46.542 1.00 41.07  ?  432 LYS   I CG   1 
ATOM   7759 C  CD   . LYS   B 1 430 ? -14.962 -50.352 -47.020 1.00 42.60  ?  432 LYS   I CD   1 
ATOM   7760 C  CE   . LYS   B 1 430 ? -15.444 -50.279 -48.452 1.00 44.07  ?  432 LYS   I CE   1 
ATOM   7761 N  NZ   . LYS   B 1 430 ? -15.443 -48.846 -48.858 1.00 47.67  ?  432 LYS   I NZ   1 
ATOM   7762 N  N    . VAL   B 1 431 ? -14.352 -52.997 -42.252 1.00 43.82  ?  433 VAL   I N    1 
ATOM   7763 C  CA   . VAL   B 1 431 ? -14.034 -52.778 -40.845 1.00 47.87  ?  433 VAL   I CA   1 
ATOM   7764 C  C    . VAL   B 1 431 ? -13.073 -53.870 -40.368 1.00 49.86  ?  433 VAL   I C    1 
ATOM   7765 O  O    . VAL   B 1 431 ? -12.148 -53.588 -39.618 1.00 50.78  ?  433 VAL   I O    1 
ATOM   7766 C  CB   . VAL   B 1 431 ? -15.310 -52.629 -39.973 1.00 49.41  ?  433 VAL   I CB   1 
ATOM   7767 C  CG1  . VAL   B 1 431 ? -14.958 -52.592 -38.486 1.00 49.60  ?  433 VAL   I CG1  1 
ATOM   7768 C  CG2  . VAL   B 1 431 ? -16.069 -51.359 -40.372 1.00 48.66  ?  433 VAL   I CG2  1 
ATOM   7769 N  N    . GLY   B 1 432 ? -13.248 -55.096 -40.850 1.00 52.56  ?  434 GLY   I N    1 
ATOM   7770 C  CA   . GLY   B 1 432 ? -12.211 -56.126 -40.684 1.00 54.89  ?  434 GLY   I CA   1 
ATOM   7771 C  C    . GLY   B 1 432 ? -10.832 -55.734 -41.222 1.00 52.47  ?  434 GLY   I C    1 
ATOM   7772 O  O    . GLY   B 1 432 ? -9.815  -55.930 -40.545 1.00 49.34  ?  434 GLY   I O    1 
ATOM   7773 N  N    . SER   B 1 433 ? -10.796 -55.188 -42.435 1.00 50.12  ?  435 SER   I N    1 
ATOM   7774 C  CA   . SER   B 1 433 ? -9.523  -54.783 -43.058 1.00 55.96  ?  435 SER   I CA   1 
ATOM   7775 C  C    . SER   B 1 433 ? -8.785  -53.714 -42.258 1.00 57.10  ?  435 SER   I C    1 
ATOM   7776 O  O    . SER   B 1 433 ? -7.560  -53.775 -42.117 1.00 61.58  ?  435 SER   I O    1 
ATOM   7777 C  CB   . SER   B 1 433 ? -9.715  -54.316 -44.517 1.00 56.70  ?  435 SER   I CB   1 
ATOM   7778 O  OG   . SER   B 1 433 ? -9.895  -55.430 -45.377 1.00 54.89  ?  435 SER   I OG   1 
ATOM   7779 N  N    . LYS   B 1 434 ? -9.531  -52.742 -41.742 1.00 55.14  ?  436 LYS   I N    1 
ATOM   7780 C  CA   . LYS   B 1 434 ? -8.955  -51.717 -40.897 1.00 52.75  ?  436 LYS   I CA   1 
ATOM   7781 C  C    . LYS   B 1 434 ? -8.514  -52.297 -39.550 1.00 48.78  ?  436 LYS   I C    1 
ATOM   7782 O  O    . LYS   B 1 434 ? -7.347  -52.196 -39.196 1.00 52.27  ?  436 LYS   I O    1 
ATOM   7783 C  CB   . LYS   B 1 434 ? -9.950  -50.584 -40.686 1.00 55.85  ?  436 LYS   I CB   1 
ATOM   7784 C  CG   . LYS   B 1 434 ? -9.425  -49.431 -39.839 1.00 60.52  ?  436 LYS   I CG   1 
ATOM   7785 C  CD   . LYS   B 1 434 ? -8.244  -48.727 -40.489 1.00 63.13  ?  436 LYS   I CD   1 
ATOM   7786 C  CE   . LYS   B 1 434 ? -7.969  -47.380 -39.827 1.00 63.13  ?  436 LYS   I CE   1 
ATOM   7787 N  NZ   . LYS   B 1 434 ? -7.127  -46.483 -40.667 1.00 61.24  ?  436 LYS   I NZ   1 
ATOM   7788 N  N    . CYS   B 1 435 ? -9.435  -52.922 -38.827 1.00 44.42  ?  437 CYS   I N    1 
ATOM   7789 C  CA   . CYS   B 1 435 ? -9.221  -53.239 -37.407 1.00 41.28  ?  437 CYS   I CA   1 
ATOM   7790 C  C    . CYS   B 1 435 ? -8.497  -54.516 -37.092 1.00 40.68  ?  437 CYS   I C    1 
ATOM   7791 O  O    . CYS   B 1 435 ? -7.927  -54.614 -35.999 1.00 36.15  ?  437 CYS   I O    1 
ATOM   7792 C  CB   . CYS   B 1 435 ? -10.541 -53.295 -36.645 1.00 41.67  ?  437 CYS   I CB   1 
ATOM   7793 S  SG   . CYS   B 1 435 ? -11.481 -51.765 -36.681 1.00 44.39  ?  437 CYS   I SG   1 
ATOM   7794 N  N    . CYS   B 1 436 ? -8.555  -55.517 -37.972 1.00 38.71  ?  438 CYS   I N    1 
ATOM   7795 C  CA   . CYS   B 1 436 ? -7.737  -56.718 -37.760 1.00 39.52  ?  438 CYS   I CA   1 
ATOM   7796 C  C    . CYS   B 1 436 ? -6.211  -56.494 -37.949 1.00 38.35  ?  438 CYS   I C    1 
ATOM   7797 O  O    . CYS   B 1 436 ? -5.416  -57.316 -37.496 1.00 39.16  ?  438 CYS   I O    1 
ATOM   7798 C  CB   . CYS   B 1 436 ? -8.222  -57.895 -38.606 1.00 39.75  ?  438 CYS   I CB   1 
ATOM   7799 S  SG   . CYS   B 1 436 ? -9.951  -58.311 -38.305 1.00 42.98  ?  438 CYS   I SG   1 
ATOM   7800 N  N    . LYS   B 1 437 ? -5.810  -55.404 -38.599 1.00 38.91  ?  439 LYS   I N    1 
ATOM   7801 C  CA   . LYS   B 1 437 ? -4.389  -55.017 -38.668 1.00 42.16  ?  439 LYS   I CA   1 
ATOM   7802 C  C    . LYS   B 1 437 ? -3.813  -54.391 -37.369 1.00 44.64  ?  439 LYS   I C    1 
ATOM   7803 O  O    . LYS   B 1 437 ? -2.617  -54.091 -37.318 1.00 48.22  ?  439 LYS   I O    1 
ATOM   7804 C  CB   . LYS   B 1 437 ? -4.163  -54.040 -39.826 1.00 43.13  ?  439 LYS   I CB   1 
ATOM   7805 N  N    . HIS   B 1 438 ? -4.652  -54.159 -36.350 1.00 45.28  ?  440 HIS   I N    1 
ATOM   7806 C  CA   . HIS   B 1 438 ? -4.201  -53.732 -35.017 1.00 42.16  ?  440 HIS   I CA   1 
ATOM   7807 C  C    . HIS   B 1 438 ? -4.031  -54.939 -34.111 1.00 38.80  ?  440 HIS   I C    1 
ATOM   7808 O  O    . HIS   B 1 438 ? -4.682  -55.953 -34.345 1.00 37.27  ?  440 HIS   I O    1 
ATOM   7809 C  CB   . HIS   B 1 438 ? -5.210  -52.770 -34.387 1.00 45.79  ?  440 HIS   I CB   1 
ATOM   7810 C  CG   . HIS   B 1 438 ? -5.076  -51.361 -34.863 1.00 49.48  ?  440 HIS   I CG   1 
ATOM   7811 N  ND1  . HIS   B 1 438 ? -3.964  -50.592 -34.597 1.00 52.39  ?  440 HIS   I ND1  1 
ATOM   7812 C  CD2  . HIS   B 1 438 ? -5.908  -50.583 -35.594 1.00 53.28  ?  440 HIS   I CD2  1 
ATOM   7813 C  CE1  . HIS   B 1 438 ? -4.115  -49.399 -35.144 1.00 53.13  ?  440 HIS   I CE1  1 
ATOM   7814 N  NE2  . HIS   B 1 438 ? -5.286  -49.368 -35.755 1.00 57.41  ?  440 HIS   I NE2  1 
ATOM   7815 N  N    . PRO   B 1 439 ? -3.166  -54.837 -33.061 1.00 38.15  ?  441 PRO   I N    1 
ATOM   7816 C  CA   . PRO   B 1 439 ? -3.021  -55.940 -32.102 1.00 39.80  ?  441 PRO   I CA   1 
ATOM   7817 C  C    . PRO   B 1 439 ? -4.205  -56.010 -31.133 1.00 41.45  ?  441 PRO   I C    1 
ATOM   7818 O  O    . PRO   B 1 439 ? -4.902  -55.021 -30.956 1.00 43.29  ?  441 PRO   I O    1 
ATOM   7819 C  CB   . PRO   B 1 439 ? -1.722  -55.598 -31.357 1.00 36.95  ?  441 PRO   I CB   1 
ATOM   7820 C  CG   . PRO   B 1 439 ? -1.588  -54.119 -31.475 1.00 35.41  ?  441 PRO   I CG   1 
ATOM   7821 C  CD   . PRO   B 1 439 ? -2.369  -53.664 -32.665 1.00 35.73  ?  441 PRO   I CD   1 
ATOM   7822 N  N    . GLU   B 1 440 ? -4.404  -57.159 -30.484 1.00 48.24  ?  442 GLU   I N    1 
ATOM   7823 C  CA   . GLU   B 1 440 ? -5.557  -57.366 -29.584 1.00 51.23  ?  442 GLU   I CA   1 
ATOM   7824 C  C    . GLU   B 1 440 ? -5.920  -56.117 -28.759 1.00 54.57  ?  442 GLU   I C    1 
ATOM   7825 O  O    . GLU   B 1 440 ? -7.095  -55.796 -28.603 1.00 59.89  ?  442 GLU   I O    1 
ATOM   7826 C  CB   . GLU   B 1 440 ? -5.346  -58.573 -28.658 1.00 49.90  ?  442 GLU   I CB   1 
ATOM   7827 C  CG   . GLU   B 1 440 ? -6.423  -58.724 -27.584 1.00 53.85  ?  442 GLU   I CG   1 
ATOM   7828 C  CD   . GLU   B 1 440 ? -6.575  -60.141 -27.056 1.00 60.41  ?  442 GLU   I CD   1 
ATOM   7829 O  OE1  . GLU   B 1 440 ? -5.543  -60.831 -26.892 1.00 63.07  ?  442 GLU   I OE1  1 
ATOM   7830 O  OE2  . GLU   B 1 440 ? -7.734  -60.561 -26.797 1.00 64.31  ?  442 GLU   I OE2  1 
ATOM   7831 N  N    . ALA   B 1 441 ? -4.922  -55.406 -28.259 1.00 54.48  ?  443 ALA   I N    1 
ATOM   7832 C  CA   . ALA   B 1 441 ? -5.172  -54.265 -27.396 1.00 57.18  ?  443 ALA   I CA   1 
ATOM   7833 C  C    . ALA   B 1 441 ? -5.999  -53.168 -28.073 1.00 51.27  ?  443 ALA   I C    1 
ATOM   7834 O  O    . ALA   B 1 441 ? -6.836  -52.569 -27.429 1.00 51.95  ?  443 ALA   I O    1 
ATOM   7835 C  CB   . ALA   B 1 441 ? -3.856  -53.695 -26.866 1.00 59.89  ?  443 ALA   I CB   1 
ATOM   7836 N  N    . LYS   B 1 442 ? -5.779  -52.913 -29.355 1.00 49.26  ?  444 LYS   I N    1 
ATOM   7837 C  CA   . LYS   B 1 442 ? -6.417  -51.751 -30.021 1.00 46.37  ?  444 LYS   I CA   1 
ATOM   7838 C  C    . LYS   B 1 442 ? -7.662  -52.060 -30.878 1.00 44.16  ?  444 LYS   I C    1 
ATOM   7839 O  O    . LYS   B 1 442 ? -8.259  -51.140 -31.457 1.00 40.68  ?  444 LYS   I O    1 
ATOM   7840 C  CB   . LYS   B 1 442 ? -5.370  -51.017 -30.840 1.00 45.66  ?  444 LYS   I CB   1 
ATOM   7841 C  CG   . LYS   B 1 442 ? -4.152  -50.635 -30.010 1.00 45.98  ?  444 LYS   I CG   1 
ATOM   7842 C  CD   . LYS   B 1 442 ? -3.639  -49.258 -30.376 1.00 48.11  ?  444 LYS   I CD   1 
ATOM   7843 C  CE   . LYS   B 1 442 ? -4.496  -48.164 -29.749 1.00 49.11  ?  444 LYS   I CE   1 
ATOM   7844 N  NZ   . LYS   B 1 442 ? -4.083  -46.824 -30.250 1.00 49.48  ?  444 LYS   I NZ   1 
ATOM   7845 N  N    . ARG   B 1 443 ? -8.063  -53.336 -30.893 1.00 38.75  ?  445 ARG   I N    1 
ATOM   7846 C  CA   . ARG   B 1 443 ? -9.111  -53.833 -31.760 1.00 41.89  ?  445 ARG   I CA   1 
ATOM   7847 C  C    . ARG   B 1 443 ? -10.511 -53.415 -31.337 1.00 41.65  ?  445 ARG   I C    1 
ATOM   7848 O  O    . ARG   B 1 443 ? -11.293 -52.927 -32.165 1.00 42.90  ?  445 ARG   I O    1 
ATOM   7849 C  CB   . ARG   B 1 443 ? -9.050  -55.370 -31.853 1.00 44.06  ?  445 ARG   I CB   1 
ATOM   7850 C  CG   . ARG   B 1 443 ? -7.892  -55.857 -32.696 1.00 46.22  ?  445 ARG   I CG   1 
ATOM   7851 C  CD   . ARG   B 1 443 ? -7.844  -57.373 -32.845 1.00 48.93  ?  445 ARG   I CD   1 
ATOM   7852 N  NE   . ARG   B 1 443 ? -6.624  -57.750 -33.564 1.00 48.73  ?  445 ARG   I NE   1 
ATOM   7853 C  CZ   . ARG   B 1 443 ? -6.340  -58.955 -34.058 1.00 48.67  ?  445 ARG   I CZ   1 
ATOM   7854 N  NH1  . ARG   B 1 443 ? -7.203  -59.970 -33.958 1.00 46.41  ?  445 ARG   I NH1  1 
ATOM   7855 N  NH2  . ARG   B 1 443 ? -5.165  -59.134 -34.681 1.00 48.79  ?  445 ARG   I NH2  1 
ATOM   7856 N  N    . MET   B 1 444 ? -10.834 -53.632 -30.060 1.00 40.63  ?  446 MET   I N    1 
ATOM   7857 C  CA   . MET   B 1 444 ? -12.199 -53.413 -29.585 1.00 35.40  ?  446 MET   I CA   1 
ATOM   7858 C  C    . MET   B 1 444 ? -12.616 -51.951 -29.760 1.00 31.89  ?  446 MET   I C    1 
ATOM   7859 O  O    . MET   B 1 444 ? -13.722 -51.698 -30.217 1.00 31.90  ?  446 MET   I O    1 
ATOM   7860 C  CB   . MET   B 1 444 ? -12.380 -53.910 -28.159 1.00 35.26  ?  446 MET   I CB   1 
ATOM   7861 C  CG   . MET   B 1 444 ? -13.767 -54.499 -27.881 1.00 37.04  ?  446 MET   I CG   1 
ATOM   7862 S  SD   . MET   B 1 444 ? -14.188 -54.738 -26.118 1.00 33.31  ?  446 MET   I SD   1 
ATOM   7863 C  CE   . MET   B 1 444 ? -13.390 -56.304 -25.746 1.00 33.67  ?  446 MET   I CE   1 
ATOM   7864 N  N    . PRO   B 1 445 ? -11.731 -50.987 -29.456 1.00 31.92  ?  447 PRO   I N    1 
ATOM   7865 C  CA   . PRO   B 1 445 ? -12.105 -49.592 -29.764 1.00 33.26  ?  447 PRO   I CA   1 
ATOM   7866 C  C    . PRO   B 1 445 ? -12.306 -49.287 -31.223 1.00 32.93  ?  447 PRO   I C    1 
ATOM   7867 O  O    . PRO   B 1 445 ? -13.274 -48.631 -31.555 1.00 37.21  ?  447 PRO   I O    1 
ATOM   7868 C  CB   . PRO   B 1 445 ? -10.938 -48.756 -29.226 1.00 31.50  ?  447 PRO   I CB   1 
ATOM   7869 C  CG   . PRO   B 1 445 ? -10.014 -49.687 -28.564 1.00 32.36  ?  447 PRO   I CG   1 
ATOM   7870 C  CD   . PRO   B 1 445 ? -10.655 -51.045 -28.456 1.00 32.60  ?  447 PRO   I CD   1 
ATOM   7871 N  N    . CYS   B 1 446 ? -11.384 -49.731 -32.079 1.00 37.36  ?  448 CYS   I N    1 
ATOM   7872 C  CA   . CYS   B 1 446 ? -11.473 -49.559 -33.562 1.00 37.26  ?  448 CYS   I CA   1 
ATOM   7873 C  C    . CYS   B 1 446 ? -12.828 -50.092 -34.047 1.00 34.54  ?  448 CYS   I C    1 
ATOM   7874 O  O    . CYS   B 1 446 ? -13.640 -49.371 -34.612 1.00 31.64  ?  448 CYS   I O    1 
ATOM   7875 C  CB   . CYS   B 1 446 ? -10.304 -50.334 -34.221 1.00 40.18  ?  448 CYS   I CB   1 
ATOM   7876 S  SG   . CYS   B 1 446 ? -10.181 -50.326 -36.044 1.00 47.95  ?  448 CYS   I SG   1 
ATOM   7877 N  N    . ALA   B 1 447 ? -13.085 -51.347 -33.696 1.00 32.44  ?  449 ALA   I N    1 
ATOM   7878 C  CA   . ALA   B 1 447 ? -14.313 -52.026 -34.039 1.00 33.77  ?  449 ALA   I CA   1 
ATOM   7879 C  C    . ALA   B 1 447 ? -15.572 -51.255 -33.601 1.00 35.09  ?  449 ALA   I C    1 
ATOM   7880 O  O    . ALA   B 1 447 ? -16.514 -51.136 -34.377 1.00 36.51  ?  449 ALA   I O    1 
ATOM   7881 C  CB   . ALA   B 1 447 ? -14.305 -53.442 -33.459 1.00 33.30  ?  449 ALA   I CB   1 
ATOM   7882 N  N    . GLU   B 1 448 ? -15.585 -50.739 -32.367 1.00 36.02  ?  450 GLU   I N    1 
ATOM   7883 C  CA   . GLU   B 1 448 ? -16.694 -49.916 -31.868 1.00 34.18  ?  450 GLU   I CA   1 
ATOM   7884 C  C    . GLU   B 1 448 ? -16.867 -48.589 -32.622 1.00 37.73  ?  450 GLU   I C    1 
ATOM   7885 O  O    . GLU   B 1 448 ? -17.989 -48.142 -32.807 1.00 38.07  ?  450 GLU   I O    1 
ATOM   7886 C  CB   . GLU   B 1 448 ? -16.486 -49.578 -30.401 1.00 31.68  ?  450 GLU   I CB   1 
ATOM   7887 C  CG   . GLU   B 1 448 ? -17.363 -48.439 -29.900 1.00 29.85  ?  450 GLU   I CG   1 
ATOM   7888 C  CD   . GLU   B 1 448 ? -17.176 -48.195 -28.428 1.00 25.61  ?  450 GLU   I CD   1 
ATOM   7889 O  OE1  . GLU   B 1 448 ? -16.044 -47.876 -28.031 1.00 21.19  ?  450 GLU   I OE1  1 
ATOM   7890 O  OE2  . GLU   B 1 448 ? -18.160 -48.341 -27.687 1.00 22.60  ?  450 GLU   I OE2  1 
ATOM   7891 N  N    . ASP   B 1 449 ? -15.771 -47.925 -32.965 1.00 41.90  ?  451 ASP   I N    1 
ATOM   7892 C  CA   . ASP   B 1 449 ? -15.855 -46.654 -33.723 1.00 49.00  ?  451 ASP   I CA   1 
ATOM   7893 C  C    . ASP   B 1 449 ? -16.648 -46.849 -35.033 1.00 49.82  ?  451 ASP   I C    1 
ATOM   7894 O  O    . ASP   B 1 449 ? -17.623 -46.135 -35.317 1.00 47.75  ?  451 ASP   I O    1 
ATOM   7895 C  CB   . ASP   B 1 449 ? -14.443 -46.104 -34.069 1.00 54.41  ?  451 ASP   I CB   1 
ATOM   7896 C  CG   . ASP   B 1 449 ? -13.913 -45.127 -33.036 1.00 62.43  ?  451 ASP   I CG   1 
ATOM   7897 O  OD1  . ASP   B 1 449 ? -13.249 -45.569 -32.060 1.00 62.60  ?  451 ASP   I OD1  1 
ATOM   7898 O  OD2  . ASP   B 1 449 ? -14.136 -43.903 -33.227 1.00 72.63  ?  451 ASP   I OD2  1 
ATOM   7899 N  N    . TYR   B 1 450 ? -16.240 -47.850 -35.805 1.00 45.73  ?  452 TYR   I N    1 
ATOM   7900 C  CA   . TYR   B 1 450 ? -16.769 -48.023 -37.154 1.00 48.54  ?  452 TYR   I CA   1 
ATOM   7901 C  C    . TYR   B 1 450 ? -18.107 -48.759 -37.152 1.00 44.31  ?  452 TYR   I C    1 
ATOM   7902 O  O    . TYR   B 1 450 ? -19.024 -48.378 -37.885 1.00 43.16  ?  452 TYR   I O    1 
ATOM   7903 C  CB   . TYR   B 1 450 ? -15.720 -48.699 -38.051 1.00 51.30  ?  452 TYR   I CB   1 
ATOM   7904 C  CG   . TYR   B 1 450 ? -14.471 -47.838 -38.268 1.00 55.89  ?  452 TYR   I CG   1 
ATOM   7905 C  CD1  . TYR   B 1 450 ? -14.553 -46.570 -38.881 1.00 60.88  ?  452 TYR   I CD1  1 
ATOM   7906 C  CD2  . TYR   B 1 450 ? -13.214 -48.281 -37.856 1.00 59.47  ?  452 TYR   I CD2  1 
ATOM   7907 C  CE1  . TYR   B 1 450 ? -13.411 -45.785 -39.073 1.00 66.36  ?  452 TYR   I CE1  1 
ATOM   7908 C  CE2  . TYR   B 1 450 ? -12.070 -47.511 -38.046 1.00 65.12  ?  452 TYR   I CE2  1 
ATOM   7909 C  CZ   . TYR   B 1 450 ? -12.164 -46.266 -38.649 1.00 66.00  ?  452 TYR   I CZ   1 
ATOM   7910 O  OH   . TYR   B 1 450 ? -11.010 -45.528 -38.817 1.00 67.45  ?  452 TYR   I OH   1 
ATOM   7911 N  N    . LEU   B 1 451 ? -18.235 -49.781 -36.307 1.00 37.30  ?  453 LEU   I N    1 
ATOM   7912 C  CA   . LEU   B 1 451 ? -19.487 -50.514 -36.218 1.00 36.28  ?  453 LEU   I CA   1 
ATOM   7913 C  C    . LEU   B 1 451 ? -20.626 -49.617 -35.809 1.00 34.69  ?  453 LEU   I C    1 
ATOM   7914 O  O    . LEU   B 1 451 ? -21.701 -49.720 -36.400 1.00 34.78  ?  453 LEU   I O    1 
ATOM   7915 C  CB   . LEU   B 1 451 ? -19.400 -51.725 -35.276 1.00 36.13  ?  453 LEU   I CB   1 
ATOM   7916 C  CG   . LEU   B 1 451 ? -19.047 -53.110 -35.865 1.00 37.95  ?  453 LEU   I CG   1 
ATOM   7917 C  CD1  . LEU   B 1 451 ? -18.222 -53.081 -37.142 1.00 35.61  ?  453 LEU   I CD1  1 
ATOM   7918 C  CD2  . LEU   B 1 451 ? -18.359 -53.988 -34.813 1.00 38.89  ?  453 LEU   I CD2  1 
ATOM   7919 N  N    . SER   B 1 452 ? -20.402 -48.729 -34.834 1.00 32.37  ?  454 SER   I N    1 
ATOM   7920 C  CA   . SER   B 1 452 ? -21.404 -47.728 -34.477 1.00 34.62  ?  454 SER   I CA   1 
ATOM   7921 C  C    . SER   B 1 452 ? -22.100 -47.152 -35.713 1.00 33.44  ?  454 SER   I C    1 
ATOM   7922 O  O    . SER   B 1 452 ? -23.325 -47.144 -35.776 1.00 33.41  ?  454 SER   I O    1 
ATOM   7923 C  CB   . SER   B 1 452 ? -20.784 -46.550 -33.711 1.00 37.62  ?  454 SER   I CB   1 
ATOM   7924 O  OG   . SER   B 1 452 ? -19.883 -45.794 -34.529 1.00 36.42  ?  454 SER   I OG   1 
ATOM   7925 N  N    . VAL   B 1 453 ? -21.313 -46.673 -36.669 1.00 32.42  ?  455 VAL   I N    1 
ATOM   7926 C  CA   . VAL   B 1 453 ? -21.875 -46.021 -37.864 1.00 38.16  ?  455 VAL   I CA   1 
ATOM   7927 C  C    . VAL   B 1 453 ? -22.435 -47.014 -38.895 1.00 35.60  ?  455 VAL   I C    1 
ATOM   7928 O  O    . VAL   B 1 453 ? -23.428 -46.724 -39.549 1.00 33.49  ?  455 VAL   I O    1 
ATOM   7929 C  CB   . VAL   B 1 453 ? -20.916 -45.008 -38.558 1.00 40.19  ?  455 VAL   I CB   1 
ATOM   7930 C  CG1  . VAL   B 1 453 ? -20.591 -43.861 -37.612 1.00 42.81  ?  455 VAL   I CG1  1 
ATOM   7931 C  CG2  . VAL   B 1 453 ? -19.641 -45.654 -39.108 1.00 43.16  ?  455 VAL   I CG2  1 
ATOM   7932 N  N    . VAL   B 1 454 ? -21.832 -48.190 -39.029 1.00 37.49  ?  456 VAL   I N    1 
ATOM   7933 C  CA   . VAL   B 1 454 ? -22.441 -49.195 -39.909 1.00 37.50  ?  456 VAL   I CA   1 
ATOM   7934 C  C    . VAL   B 1 454 ? -23.810 -49.623 -39.351 1.00 36.09  ?  456 VAL   I C    1 
ATOM   7935 O  O    . VAL   B 1 454 ? -24.759 -49.662 -40.104 1.00 33.49  ?  456 VAL   I O    1 
ATOM   7936 C  CB   . VAL   B 1 454 ? -21.543 -50.401 -40.173 1.00 38.12  ?  456 VAL   I CB   1 
ATOM   7937 C  CG1  . VAL   B 1 454 ? -22.231 -51.378 -41.126 1.00 38.14  ?  456 VAL   I CG1  1 
ATOM   7938 C  CG2  . VAL   B 1 454 ? -20.227 -49.937 -40.760 1.00 38.35  ?  456 VAL   I CG2  1 
ATOM   7939 N  N    . LEU   B 1 455 ? -23.897 -49.866 -38.037 1.00 36.50  ?  457 LEU   I N    1 
ATOM   7940 C  CA   . LEU   B 1 455 ? -25.140 -50.306 -37.338 1.00 35.48  ?  457 LEU   I CA   1 
ATOM   7941 C  C    . LEU   B 1 455 ? -26.203 -49.222 -37.308 1.00 33.28  ?  457 LEU   I C    1 
ATOM   7942 O  O    . LEU   B 1 455 ? -27.380 -49.514 -37.457 1.00 32.61  ?  457 LEU   I O    1 
ATOM   7943 C  CB   . LEU   B 1 455 ? -24.871 -50.772 -35.885 1.00 37.50  ?  457 LEU   I CB   1 
ATOM   7944 C  CG   . LEU   B 1 455 ? -24.375 -52.226 -35.617 1.00 41.90  ?  457 LEU   I CG   1 
ATOM   7945 C  CD1  . LEU   B 1 455 ? -23.328 -52.744 -36.625 1.00 42.44  ?  457 LEU   I CD1  1 
ATOM   7946 C  CD2  . LEU   B 1 455 ? -23.840 -52.364 -34.196 1.00 39.54  ?  457 LEU   I CD2  1 
ATOM   7947 N  N    . ASN   B 1 456 ? -25.809 -47.979 -37.120 1.00 32.35  ?  458 ASN   I N    1 
ATOM   7948 C  CA   . ASN   B 1 456 ? -26.766 -46.875 -37.330 1.00 36.36  ?  458 ASN   I CA   1 
ATOM   7949 C  C    . ASN   B 1 456 ? -27.303 -46.672 -38.784 1.00 37.49  ?  458 ASN   I C    1 
ATOM   7950 O  O    . ASN   B 1 456 ? -28.518 -46.566 -38.960 1.00 41.64  ?  458 ASN   I O    1 
ATOM   7951 C  CB   . ASN   B 1 456 ? -26.216 -45.554 -36.821 1.00 38.30  ?  458 ASN   I CB   1 
ATOM   7952 C  CG   . ASN   B 1 456 ? -27.329 -44.590 -36.461 1.00 39.26  ?  458 ASN   I CG   1 
ATOM   7953 O  OD1  . ASN   B 1 456 ? -28.294 -44.966 -35.782 1.00 42.58  ?  458 ASN   I OD1  1 
ATOM   7954 N  ND2  . ASN   B 1 456 ? -27.202 -43.359 -36.888 1.00 36.62  ?  458 ASN   I ND2  1 
ATOM   7955 N  N    . GLN   B 1 457 ? -26.417 -46.596 -39.786 1.00 37.81  ?  459 GLN   I N    1 
ATOM   7956 C  CA   . GLN   B 1 457 ? -26.780 -46.559 -41.230 1.00 42.30  ?  459 GLN   I CA   1 
ATOM   7957 C  C    . GLN   B 1 457 ? -27.751 -47.677 -41.625 1.00 44.04  ?  459 GLN   I C    1 
ATOM   7958 O  O    . GLN   B 1 457 ? -28.653 -47.490 -42.452 1.00 43.56  ?  459 GLN   I O    1 
ATOM   7959 C  CB   . GLN   B 1 457 ? -25.548 -46.838 -42.098 1.00 51.23  ?  459 GLN   I CB   1 
ATOM   7960 C  CG   . GLN   B 1 457 ? -24.545 -45.720 -42.369 1.00 56.30  ?  459 GLN   I CG   1 
ATOM   7961 C  CD   . GLN   B 1 457 ? -23.349 -46.235 -43.172 1.00 59.20  ?  459 GLN   I CD   1 
ATOM   7962 O  OE1  . GLN   B 1 457 ? -23.212 -47.456 -43.400 1.00 61.11  ?  459 GLN   I OE1  1 
ATOM   7963 N  NE2  . GLN   B 1 457 ? -22.470 -45.308 -43.607 1.00 57.17  ?  459 GLN   I NE2  1 
ATOM   7964 N  N    . LEU   B 1 458 ? -27.469 -48.860 -41.083 1.00 41.09  ?  460 LEU   I N    1 
ATOM   7965 C  CA   . LEU   B 1 458 ? -28.318 -50.040 -41.193 1.00 41.51  ?  460 LEU   I CA   1 
ATOM   7966 C  C    . LEU   B 1 458 ? -29.745 -49.774 -40.662 1.00 40.61  ?  460 LEU   I C    1 
ATOM   7967 O  O    . LEU   B 1 458 ? -30.735 -49.965 -41.384 1.00 38.05  ?  460 LEU   I O    1 
ATOM   7968 C  CB   . LEU   B 1 458 ? -27.645 -51.167 -40.405 1.00 41.90  ?  460 LEU   I CB   1 
ATOM   7969 C  CG   . LEU   B 1 458 ? -28.149 -52.604 -40.431 1.00 43.26  ?  460 LEU   I CG   1 
ATOM   7970 C  CD1  . LEU   B 1 458 ? -27.128 -53.469 -41.170 1.00 49.55  ?  460 LEU   I CD1  1 
ATOM   7971 C  CD2  . LEU   B 1 458 ? -28.333 -53.172 -39.042 1.00 43.81  ?  460 LEU   I CD2  1 
ATOM   7972 N  N    . CYS   B 1 459 ? -29.824 -49.309 -39.415 1.00 39.03  ?  461 CYS   I N    1 
ATOM   7973 C  CA   . CYS   B 1 459 ? -31.088 -48.981 -38.785 1.00 42.49  ?  461 CYS   I CA   1 
ATOM   7974 C  C    . CYS   B 1 459 ? -31.772 -47.743 -39.391 1.00 46.91  ?  461 CYS   I C    1 
ATOM   7975 O  O    . CYS   B 1 459 ? -33.012 -47.637 -39.330 1.00 51.79  ?  461 CYS   I O    1 
ATOM   7976 C  CB   . CYS   B 1 459 ? -30.914 -48.802 -37.269 1.00 42.69  ?  461 CYS   I CB   1 
ATOM   7977 S  SG   . CYS   B 1 459 ? -30.455 -50.343 -36.425 1.00 43.33  ?  461 CYS   I SG   1 
ATOM   7978 N  N    . VAL   B 1 460 ? -30.993 -46.818 -39.954 1.00 45.65  ?  462 VAL   I N    1 
ATOM   7979 C  CA   . VAL   B 1 460 ? -31.573 -45.642 -40.613 1.00 48.54  ?  462 VAL   I CA   1 
ATOM   7980 C  C    . VAL   B 1 460 ? -32.335 -46.106 -41.871 1.00 47.82  ?  462 VAL   I C    1 
ATOM   7981 O  O    . VAL   B 1 460 ? -33.514 -45.784 -42.018 1.00 52.54  ?  462 VAL   I O    1 
ATOM   7982 C  CB   . VAL   B 1 460 ? -30.523 -44.529 -40.925 1.00 45.92  ?  462 VAL   I CB   1 
ATOM   7983 C  CG1  . VAL   B 1 460 ? -31.158 -43.396 -41.732 1.00 45.79  ?  462 VAL   I CG1  1 
ATOM   7984 C  CG2  . VAL   B 1 460 ? -29.896 -43.980 -39.632 1.00 44.02  ?  462 VAL   I CG2  1 
ATOM   7985 N  N    . LEU   B 1 461 ? -31.694 -46.898 -42.733 1.00 47.81  ?  463 LEU   I N    1 
ATOM   7986 C  CA   . LEU   B 1 461 ? -32.398 -47.497 -43.877 1.00 51.25  ?  463 LEU   I CA   1 
ATOM   7987 C  C    . LEU   B 1 461 ? -33.675 -48.213 -43.440 1.00 49.22  ?  463 LEU   I C    1 
ATOM   7988 O  O    . LEU   B 1 461 ? -34.722 -48.043 -44.051 1.00 49.58  ?  463 LEU   I O    1 
ATOM   7989 C  CB   . LEU   B 1 461 ? -31.507 -48.483 -44.646 1.00 53.56  ?  463 LEU   I CB   1 
ATOM   7990 C  CG   . LEU   B 1 461 ? -30.404 -47.855 -45.508 1.00 55.89  ?  463 LEU   I CG   1 
ATOM   7991 C  CD1  . LEU   B 1 461 ? -29.408 -48.911 -45.959 1.00 56.08  ?  463 LEU   I CD1  1 
ATOM   7992 C  CD2  . LEU   B 1 461 ? -30.979 -47.105 -46.706 1.00 56.71  ?  463 LEU   I CD2  1 
ATOM   7993 N  N    . HIS   B 1 462 ? -33.584 -48.969 -42.355 1.00 44.84  ?  464 HIS   I N    1 
ATOM   7994 C  CA   . HIS   B 1 462 ? -34.693 -49.809 -41.904 1.00 45.61  ?  464 HIS   I CA   1 
ATOM   7995 C  C    . HIS   B 1 462 ? -35.918 -49.140 -41.253 1.00 46.79  ?  464 HIS   I C    1 
ATOM   7996 O  O    . HIS   B 1 462 ? -36.981 -49.739 -41.246 1.00 47.48  ?  464 HIS   I O    1 
ATOM   7997 C  CB   . HIS   B 1 462 ? -34.163 -50.844 -40.932 1.00 45.12  ?  464 HIS   I CB   1 
ATOM   7998 C  CG   . HIS   B 1 462 ? -35.119 -51.951 -40.667 1.00 43.15  ?  464 HIS   I CG   1 
ATOM   7999 N  ND1  . HIS   B 1 462 ? -36.125 -51.851 -39.728 1.00 42.07  ?  464 HIS   I ND1  1 
ATOM   8000 C  CD2  . HIS   B 1 462 ? -35.251 -53.167 -41.244 1.00 39.89  ?  464 HIS   I CD2  1 
ATOM   8001 C  CE1  . HIS   B 1 462 ? -36.810 -52.978 -39.710 1.00 42.30  ?  464 HIS   I CE1  1 
ATOM   8002 N  NE2  . HIS   B 1 462 ? -36.297 -53.791 -40.617 1.00 40.32  ?  464 HIS   I NE2  1 
ATOM   8003 N  N    . GLU   B 1 463 ? -35.776 -47.961 -40.651 1.00 52.94  ?  465 GLU   I N    1 
ATOM   8004 C  CA   . GLU   B 1 463 ? -36.955 -47.191 -40.236 1.00 57.11  ?  465 GLU   I CA   1 
ATOM   8005 C  C    . GLU   B 1 463 ? -37.677 -46.664 -41.471 1.00 60.89  ?  465 GLU   I C    1 
ATOM   8006 O  O    . GLU   B 1 463 ? -38.895 -46.667 -41.509 1.00 67.94  ?  465 GLU   I O    1 
ATOM   8007 C  CB   . GLU   B 1 463 ? -36.602 -46.036 -39.271 1.00 59.16  ?  465 GLU   I CB   1 
ATOM   8008 C  CG   . GLU   B 1 463 ? -37.710 -44.992 -38.974 1.00 60.66  ?  465 GLU   I CG   1 
ATOM   8009 C  CD   . GLU   B 1 463 ? -38.869 -45.478 -38.082 1.00 63.30  ?  465 GLU   I CD   1 
ATOM   8010 O  OE1  . GLU   B 1 463 ? -39.129 -46.704 -37.994 1.00 65.88  ?  465 GLU   I OE1  1 
ATOM   8011 O  OE2  . GLU   B 1 463 ? -39.547 -44.615 -37.461 1.00 59.41  ?  465 GLU   I OE2  1 
ATOM   8012 N  N    . LYS   B 1 464 ? -36.935 -46.218 -42.478 1.00 65.94  ?  466 LYS   I N    1 
ATOM   8013 C  CA   . LYS   B 1 464 ? -37.550 -45.587 -43.650 1.00 69.22  ?  466 LYS   I CA   1 
ATOM   8014 C  C    . LYS   B 1 464 ? -38.408 -46.544 -44.512 1.00 64.69  ?  466 LYS   I C    1 
ATOM   8015 O  O    . LYS   B 1 464 ? -39.312 -46.086 -45.206 1.00 67.35  ?  466 LYS   I O    1 
ATOM   8016 C  CB   . LYS   B 1 464 ? -36.492 -44.844 -44.488 1.00 72.41  ?  466 LYS   I CB   1 
ATOM   8017 C  CG   . LYS   B 1 464 ? -35.855 -43.657 -43.760 1.00 70.39  ?  466 LYS   I CG   1 
ATOM   8018 C  CD   . LYS   B 1 464 ? -35.378 -42.571 -44.716 1.00 71.07  ?  466 LYS   I CD   1 
ATOM   8019 N  N    . THR   B 1 465 ? -38.125 -47.846 -44.461 1.00 60.25  ?  467 THR   I N    1 
ATOM   8020 C  CA   . THR   B 1 465 ? -39.044 -48.894 -44.953 1.00 57.27  ?  467 THR   I CA   1 
ATOM   8021 C  C    . THR   B 1 465 ? -38.759 -50.199 -44.196 1.00 53.76  ?  467 THR   I C    1 
ATOM   8022 O  O    . THR   B 1 465 ? -37.906 -50.982 -44.613 1.00 50.08  ?  467 THR   I O    1 
ATOM   8023 C  CB   . THR   B 1 465 ? -38.915 -49.177 -46.465 1.00 57.68  ?  467 THR   I CB   1 
ATOM   8024 O  OG1  . THR   B 1 465 ? -37.554 -49.477 -46.794 1.00 59.76  ?  467 THR   I OG1  1 
ATOM   8025 C  CG2  . THR   B 1 465 ? -39.381 -48.001 -47.312 1.00 59.02  ?  467 THR   I CG2  1 
ATOM   8026 N  N    . PRO   B 1 466 ? -39.458 -50.430 -43.067 1.00 52.98  ?  468 PRO   I N    1 
ATOM   8027 C  CA   . PRO   B 1 466 ? -39.290 -51.653 -42.266 1.00 50.98  ?  468 PRO   I CA   1 
ATOM   8028 C  C    . PRO   B 1 466 ? -39.514 -52.942 -43.049 1.00 50.37  ?  468 PRO   I C    1 
ATOM   8029 O  O    . PRO   B 1 466 ? -40.034 -52.901 -44.162 1.00 49.33  ?  468 PRO   I O    1 
ATOM   8030 C  CB   . PRO   B 1 466 ? -40.347 -51.499 -41.162 1.00 49.88  ?  468 PRO   I CB   1 
ATOM   8031 C  CG   . PRO   B 1 466 ? -40.558 -50.034 -41.044 1.00 49.27  ?  468 PRO   I CG   1 
ATOM   8032 C  CD   . PRO   B 1 466 ? -40.427 -49.510 -42.440 1.00 52.14  ?  468 PRO   I CD   1 
ATOM   8033 N  N    . VAL   B 1 467 ? -39.147 -54.064 -42.428 1.00 49.39  ?  469 VAL   I N    1 
ATOM   8034 C  CA   . VAL   B 1 467 ? -39.025 -55.356 -43.113 1.00 47.69  ?  469 VAL   I CA   1 
ATOM   8035 C  C    . VAL   B 1 467 ? -38.872 -56.563 -42.187 1.00 45.49  ?  469 VAL   I C    1 
ATOM   8036 O  O    . VAL   B 1 467 ? -39.350 -57.649 -42.499 1.00 42.25  ?  469 VAL   I O    1 
ATOM   8037 C  CB   . VAL   B 1 467 ? -37.846 -55.294 -44.134 1.00 51.77  ?  469 VAL   I CB   1 
ATOM   8038 C  CG1  . VAL   B 1 467 ? -36.925 -56.509 -44.065 1.00 51.90  ?  469 VAL   I CG1  1 
ATOM   8039 C  CG2  . VAL   B 1 467 ? -38.364 -55.081 -45.566 1.00 48.85  ?  469 VAL   I CG2  1 
ATOM   8040 N  N    . SER   B 1 468 ? -38.148 -56.393 -41.083 1.00 42.91  ?  470 SER   I N    1 
ATOM   8041 C  CA   . SER   B 1 468 ? -38.060 -57.409 -40.043 1.00 40.91  ?  470 SER   I CA   1 
ATOM   8042 C  C    . SER   B 1 468 ? -38.285 -56.727 -38.693 1.00 39.06  ?  470 SER   I C    1 
ATOM   8043 O  O    . SER   B 1 468 ? -37.631 -55.739 -38.352 1.00 38.86  ?  470 SER   I O    1 
ATOM   8044 C  CB   . SER   B 1 468 ? -36.711 -58.127 -40.083 1.00 37.77  ?  470 SER   I CB   1 
ATOM   8045 O  OG   . SER   B 1 468 ? -36.838 -59.408 -39.519 1.00 42.95  ?  470 SER   I OG   1 
ATOM   8046 N  N    . ASP   B 1 469 ? -39.254 -57.238 -37.963 1.00 36.29  ?  471 ASP   I N    1 
ATOM   8047 C  CA   . ASP   B 1 469 ? -39.450 -56.865 -36.581 1.00 38.09  ?  471 ASP   I CA   1 
ATOM   8048 C  C    . ASP   B 1 469 ? -38.179 -57.067 -35.719 1.00 38.16  ?  471 ASP   I C    1 
ATOM   8049 O  O    . ASP   B 1 469 ? -37.894 -56.260 -34.816 1.00 38.32  ?  471 ASP   I O    1 
ATOM   8050 C  CB   . ASP   B 1 469 ? -40.610 -57.655 -35.992 1.00 39.21  ?  471 ASP   I CB   1 
ATOM   8051 C  CG   . ASP   B 1 469 ? -40.429 -59.178 -36.121 1.00 42.95  ?  471 ASP   I CG   1 
ATOM   8052 O  OD1  . ASP   B 1 469 ? -40.114 -59.682 -37.240 1.00 39.16  ?  471 ASP   I OD1  1 
ATOM   8053 O  OD2  . ASP   B 1 469 ? -40.623 -59.866 -35.091 1.00 46.54  ?  471 ASP   I OD2  1 
ATOM   8054 N  N    . ARG   B 1 470 ? -37.432 -58.131 -36.013 1.00 35.11  ?  472 ARG   I N    1 
ATOM   8055 C  CA   . ARG   B 1 470 ? -36.202 -58.455 -35.306 1.00 35.45  ?  472 ARG   I CA   1 
ATOM   8056 C  C    . ARG   B 1 470 ? -35.162 -57.366 -35.501 1.00 35.15  ?  472 ARG   I C    1 
ATOM   8057 O  O    . ARG   B 1 470 ? -34.501 -56.935 -34.541 1.00 38.37  ?  472 ARG   I O    1 
ATOM   8058 C  CB   . ARG   B 1 470 ? -35.614 -59.772 -35.794 1.00 33.93  ?  472 ARG   I CB   1 
ATOM   8059 C  CG   . ARG   B 1 470 ? -36.484 -60.985 -35.484 1.00 35.34  ?  472 ARG   I CG   1 
ATOM   8060 C  CD   . ARG   B 1 470 ? -36.249 -62.070 -36.516 1.00 33.52  ?  472 ARG   I CD   1 
ATOM   8061 N  NE   . ARG   B 1 470 ? -35.028 -62.776 -36.199 1.00 35.73  ?  472 ARG   I NE   1 
ATOM   8062 C  CZ   . ARG   B 1 470 ? -34.185 -63.320 -37.067 1.00 33.15  ?  472 ARG   I CZ   1 
ATOM   8063 N  NH1  . ARG   B 1 470 ? -34.403 -63.274 -38.383 1.00 34.69  ?  472 ARG   I NH1  1 
ATOM   8064 N  NH2  . ARG   B 1 470 ? -33.109 -63.933 -36.595 1.00 34.64  ?  472 ARG   I NH2  1 
ATOM   8065 N  N    . VAL   B 1 471 ? -34.999 -56.946 -36.741 1.00 30.21  ?  473 VAL   I N    1 
ATOM   8066 C  CA   . VAL   B 1 471 ? -34.073 -55.892 -37.042 1.00 33.99  ?  473 VAL   I CA   1 
ATOM   8067 C  C    . VAL   B 1 471 ? -34.532 -54.657 -36.298 1.00 37.12  ?  473 VAL   I C    1 
ATOM   8068 O  O    . VAL   B 1 471 ? -33.692 -53.929 -35.752 1.00 40.60  ?  473 VAL   I O    1 
ATOM   8069 C  CB   . VAL   B 1 471 ? -33.910 -55.655 -38.561 1.00 30.78  ?  473 VAL   I CB   1 
ATOM   8070 C  CG1  . VAL   B 1 471 ? -33.202 -54.341 -38.854 1.00 32.90  ?  473 VAL   I CG1  1 
ATOM   8071 C  CG2  . VAL   B 1 471 ? -33.125 -56.788 -39.148 1.00 30.18  ?  473 VAL   I CG2  1 
ATOM   8072 N  N    . THR   B 1 472 ? -35.850 -54.452 -36.232 1.00 40.90  ?  474 THR   I N    1 
ATOM   8073 C  CA   . THR   B 1 472 ? -36.391 -53.367 -35.424 1.00 45.27  ?  474 THR   I CA   1 
ATOM   8074 C  C    . THR   B 1 472 ? -36.089 -53.541 -33.935 1.00 42.74  ?  474 THR   I C    1 
ATOM   8075 O  O    . THR   B 1 472 ? -35.759 -52.566 -33.263 1.00 45.26  ?  474 THR   I O    1 
ATOM   8076 C  CB   . THR   B 1 472 ? -37.905 -53.161 -35.602 1.00 46.68  ?  474 THR   I CB   1 
ATOM   8077 O  OG1  . THR   B 1 472 ? -38.300 -53.541 -36.929 1.00 55.56  ?  474 THR   I OG1  1 
ATOM   8078 C  CG2  . THR   B 1 472 ? -38.248 -51.681 -35.368 1.00 47.60  ?  474 THR   I CG2  1 
ATOM   8079 N  N    . LYS   B 1 473 ? -36.211 -54.764 -33.431 1.00 43.67  ?  475 LYS   I N    1 
ATOM   8080 C  CA   . LYS   B 1 473 ? -35.939 -55.050 -32.018 1.00 48.59  ?  475 LYS   I CA   1 
ATOM   8081 C  C    . LYS   B 1 473 ? -34.517 -54.656 -31.599 1.00 48.80  ?  475 LYS   I C    1 
ATOM   8082 O  O    . LYS   B 1 473 ? -34.307 -54.262 -30.447 1.00 58.40  ?  475 LYS   I O    1 
ATOM   8083 C  CB   . LYS   B 1 473 ? -36.237 -56.524 -31.677 1.00 50.60  ?  475 LYS   I CB   1 
ATOM   8084 C  CG   . LYS   B 1 473 ? -36.031 -56.931 -30.211 1.00 57.80  ?  475 LYS   I CG   1 
ATOM   8085 C  CD   . LYS   B 1 473 ? -36.887 -56.136 -29.228 1.00 60.68  ?  475 LYS   I CD   1 
ATOM   8086 C  CE   . LYS   B 1 473 ? -36.608 -56.538 -27.788 1.00 61.94  ?  475 LYS   I CE   1 
ATOM   8087 N  NZ   . LYS   B 1 473 ? -36.979 -57.955 -27.497 1.00 61.44  ?  475 LYS   I NZ   1 
ATOM   8088 N  N    . CYS   B 1 474 ? -33.557 -54.726 -32.521 1.00 43.83  ?  476 CYS   I N    1 
ATOM   8089 C  CA   . CYS   B 1 474 ? -32.189 -54.319 -32.213 1.00 41.68  ?  476 CYS   I CA   1 
ATOM   8090 C  C    . CYS   B 1 474 ? -31.962 -52.829 -32.413 1.00 43.55  ?  476 CYS   I C    1 
ATOM   8091 O  O    . CYS   B 1 474 ? -31.259 -52.208 -31.624 1.00 42.43  ?  476 CYS   I O    1 
ATOM   8092 C  CB   . CYS   B 1 474 ? -31.215 -55.172 -33.002 1.00 41.16  ?  476 CYS   I CB   1 
ATOM   8093 S  SG   . CYS   B 1 474 ? -31.415 -56.926 -32.588 1.00 40.49  ?  476 CYS   I SG   1 
ATOM   8094 N  N    . CYS   B 1 475 ? -32.617 -52.246 -33.413 1.00 44.34  ?  477 CYS   I N    1 
ATOM   8095 C  CA   . CYS   B 1 475 ? -32.463 -50.821 -33.730 1.00 43.82  ?  477 CYS   I CA   1 
ATOM   8096 C  C    . CYS   B 1 475 ? -33.024 -49.828 -32.715 1.00 42.77  ?  477 CYS   I C    1 
ATOM   8097 O  O    . CYS   B 1 475 ? -32.612 -48.674 -32.691 1.00 42.24  ?  477 CYS   I O    1 
ATOM   8098 C  CB   . CYS   B 1 475 ? -33.073 -50.548 -35.101 1.00 45.90  ?  477 CYS   I CB   1 
ATOM   8099 S  SG   . CYS   B 1 475 ? -32.187 -51.398 -36.429 1.00 43.62  ?  477 CYS   I SG   1 
ATOM   8100 N  N    . THR   B 1 476 ? -33.973 -50.283 -31.906 1.00 46.38  ?  478 THR   I N    1 
ATOM   8101 C  CA   . THR   B 1 476 ? -34.615 -49.476 -30.866 1.00 44.37  ?  478 THR   I CA   1 
ATOM   8102 C  C    . THR   B 1 476 ? -34.159 -49.879 -29.470 1.00 45.67  ?  478 THR   I C    1 
ATOM   8103 O  O    . THR   B 1 476 ? -34.649 -49.339 -28.485 1.00 46.88  ?  478 THR   I O    1 
ATOM   8104 C  CB   . THR   B 1 476 ? -36.153 -49.607 -30.947 1.00 41.61  ?  478 THR   I CB   1 
ATOM   8105 O  OG1  . THR   B 1 476 ? -36.533 -50.993 -31.009 1.00 37.13  ?  478 THR   I OG1  1 
ATOM   8106 C  CG2  . THR   B 1 476 ? -36.661 -48.861 -32.155 1.00 43.20  ?  478 THR   I CG2  1 
ATOM   8107 N  N    . GLU   B 1 477 ? -33.211 -50.815 -29.391 1.00 50.48  ?  479 GLU   I N    1 
ATOM   8108 C  CA   . GLU   B 1 477 ? -32.702 -51.339 -28.119 1.00 47.88  ?  479 GLU   I CA   1 
ATOM   8109 C  C    . GLU   B 1 477 ? -31.783 -50.300 -27.512 1.00 45.30  ?  479 GLU   I C    1 
ATOM   8110 O  O    . GLU   B 1 477 ? -31.334 -49.395 -28.214 1.00 47.87  ?  479 GLU   I O    1 
ATOM   8111 C  CB   . GLU   B 1 477 ? -31.947 -52.643 -28.361 1.00 50.13  ?  479 GLU   I CB   1 
ATOM   8112 C  CG   . GLU   B 1 477 ? -31.858 -53.585 -27.173 1.00 54.99  ?  479 GLU   I CG   1 
ATOM   8113 C  CD   . GLU   B 1 477 ? -33.084 -54.440 -26.966 1.00 54.42  ?  479 GLU   I CD   1 
ATOM   8114 O  OE1  . GLU   B 1 477 ? -34.192 -53.884 -26.910 1.00 58.33  ?  479 GLU   I OE1  1 
ATOM   8115 O  OE2  . GLU   B 1 477 ? -32.933 -55.682 -26.843 1.00 63.02  ?  479 GLU   I OE2  1 
ATOM   8116 N  N    . SER   B 1 478 ? -31.513 -50.410 -26.211 1.00 43.62  ?  480 SER   I N    1 
ATOM   8117 C  CA   . SER   B 1 478 ? -30.544 -49.529 -25.554 1.00 44.18  ?  480 SER   I CA   1 
ATOM   8118 C  C    . SER   B 1 478 ? -29.202 -49.498 -26.304 1.00 44.57  ?  480 SER   I C    1 
ATOM   8119 O  O    . SER   B 1 478 ? -28.857 -50.471 -26.994 1.00 43.66  ?  480 SER   I O    1 
ATOM   8120 C  CB   . SER   B 1 478 ? -30.342 -49.960 -24.093 1.00 45.64  ?  480 SER   I CB   1 
ATOM   8121 O  OG   . SER   B 1 478 ? -30.049 -51.342 -23.983 1.00 42.58  ?  480 SER   I OG   1 
ATOM   8122 N  N    . LEU   B 1 479 ? -28.459 -48.392 -26.182 1.00 42.22  ?  481 LEU   I N    1 
ATOM   8123 C  CA   . LEU   B 1 479 ? -27.113 -48.271 -26.798 1.00 44.99  ?  481 LEU   I CA   1 
ATOM   8124 C  C    . LEU   B 1 479 ? -26.161 -49.414 -26.419 1.00 40.40  ?  481 LEU   I C    1 
ATOM   8125 O  O    . LEU   B 1 479 ? -25.291 -49.803 -27.191 1.00 44.39  ?  481 LEU   I O    1 
ATOM   8126 C  CB   . LEU   B 1 479 ? -26.430 -46.916 -26.482 1.00 48.95  ?  481 LEU   I CB   1 
ATOM   8127 C  CG   . LEU   B 1 479 ? -26.660 -45.680 -27.396 1.00 53.25  ?  481 LEU   I CG   1 
ATOM   8128 C  CD1  . LEU   B 1 479 ? -25.432 -44.773 -27.370 1.00 56.70  ?  481 LEU   I CD1  1 
ATOM   8129 C  CD2  . LEU   B 1 479 ? -27.010 -46.006 -28.853 1.00 54.27  ?  481 LEU   I CD2  1 
ATOM   8130 N  N    . VAL   B 1 480 ? -26.344 -49.919 -25.217 1.00 37.18  ?  482 VAL   I N    1 
ATOM   8131 C  CA   . VAL   B 1 480 ? -25.551 -50.996 -24.660 1.00 36.43  ?  482 VAL   I CA   1 
ATOM   8132 C  C    . VAL   B 1 480 ? -25.855 -52.378 -25.329 1.00 34.43  ?  482 VAL   I C    1 
ATOM   8133 O  O    . VAL   B 1 480 ? -24.955 -53.219 -25.505 1.00 35.39  ?  482 VAL   I O    1 
ATOM   8134 C  CB   . VAL   B 1 480 ? -25.705 -50.915 -23.092 1.00 33.57  ?  482 VAL   I CB   1 
ATOM   8135 C  CG1  . VAL   B 1 480 ? -25.863 -52.245 -22.392 1.00 33.42  ?  482 VAL   I CG1  1 
ATOM   8136 C  CG2  . VAL   B 1 480 ? -24.538 -50.141 -22.509 1.00 34.66  ?  482 VAL   I CG2  1 
ATOM   8137 N  N    . ASN   B 1 481 ? -27.118 -52.603 -25.675 1.00 33.80  ?  483 ASN   I N    1 
ATOM   8138 C  CA   . ASN   B 1 481 ? -27.603 -53.882 -26.245 1.00 33.73  ?  483 ASN   I CA   1 
ATOM   8139 C  C    . ASN   B 1 481 ? -27.719 -53.947 -27.817 1.00 30.74  ?  483 ASN   I C    1 
ATOM   8140 O  O    . ASN   B 1 481 ? -27.987 -55.005 -28.360 1.00 24.25  ?  483 ASN   I O    1 
ATOM   8141 C  CB   . ASN   B 1 481 ? -28.964 -54.225 -25.601 1.00 35.96  ?  483 ASN   I CB   1 
ATOM   8142 C  CG   . ASN   B 1 481 ? -28.847 -54.664 -24.143 1.00 37.02  ?  483 ASN   I CG   1 
ATOM   8143 O  OD1  . ASN   B 1 481 ? -27.784 -55.072 -23.689 1.00 37.30  ?  483 ASN   I OD1  1 
ATOM   8144 N  ND2  . ASN   B 1 481 ? -29.966 -54.611 -23.415 1.00 36.51  ?  483 ASN   I ND2  1 
ATOM   8145 N  N    . ARG   B 1 482 ? -27.468 -52.845 -28.517 1.00 28.17  ?  484 ARG   I N    1 
ATOM   8146 C  CA   . ARG   B 1 482 ? -27.621 -52.794 -29.966 1.00 30.34  ?  484 ARG   I CA   1 
ATOM   8147 C  C    . ARG   B 1 482 ? -26.831 -53.862 -30.731 1.00 28.16  ?  484 ARG   I C    1 
ATOM   8148 O  O    . ARG   B 1 482 ? -27.440 -54.652 -31.473 1.00 28.80  ?  484 ARG   I O    1 
ATOM   8149 C  CB   . ARG   B 1 482 ? -27.269 -51.402 -30.485 1.00 32.76  ?  484 ARG   I CB   1 
ATOM   8150 C  CG   . ARG   B 1 482 ? -27.256 -51.230 -32.001 1.00 34.93  ?  484 ARG   I CG   1 
ATOM   8151 C  CD   . ARG   B 1 482 ? -27.152 -49.739 -32.340 1.00 39.08  ?  484 ARG   I CD   1 
ATOM   8152 N  NE   . ARG   B 1 482 ? -28.471 -49.125 -32.465 1.00 41.04  ?  484 ARG   I NE   1 
ATOM   8153 C  CZ   . ARG   B 1 482 ? -28.702 -47.882 -32.876 1.00 46.88  ?  484 ARG   I CZ   1 
ATOM   8154 N  NH1  . ARG   B 1 482 ? -27.706 -47.044 -33.170 1.00 51.00  ?  484 ARG   I NH1  1 
ATOM   8155 N  NH2  . ARG   B 1 482 ? -29.953 -47.458 -32.969 1.00 47.98  ?  484 ARG   I NH2  1 
ATOM   8156 N  N    . ARG   B 1 483 ? -25.502 -53.895 -30.579 1.00 22.67  ?  485 ARG   I N    1 
ATOM   8157 C  CA   . ARG   B 1 483 ? -24.704 -54.891 -31.266 1.00 20.82  ?  485 ARG   I CA   1 
ATOM   8158 C  C    . ARG   B 1 483 ? -24.926 -56.361 -30.714 1.00 22.12  ?  485 ARG   I C    1 
ATOM   8159 O  O    . ARG   B 1 483 ? -25.146 -57.299 -31.492 1.00 21.82  ?  485 ARG   I O    1 
ATOM   8160 C  CB   . ARG   B 1 483 ? -23.258 -54.423 -31.288 1.00 19.57  ?  485 ARG   I CB   1 
ATOM   8161 C  CG   . ARG   B 1 483 ? -22.337 -55.202 -32.169 1.00 20.03  ?  485 ARG   I CG   1 
ATOM   8162 C  CD   . ARG   B 1 483 ? -21.958 -56.582 -31.605 1.00 19.96  ?  485 ARG   I CD   1 
ATOM   8163 N  NE   . ARG   B 1 483 ? -21.408 -56.507 -30.256 1.00 19.31  ?  485 ARG   I NE   1 
ATOM   8164 C  CZ   . ARG   B 1 483 ? -21.303 -57.525 -29.413 1.00 20.42  ?  485 ARG   I CZ   1 
ATOM   8165 N  NH1  . ARG   B 1 483 ? -21.738 -58.746 -29.762 1.00 19.13  ?  485 ARG   I NH1  1 
ATOM   8166 N  NH2  . ARG   B 1 483 ? -20.774 -57.328 -28.207 1.00 19.82  ?  485 ARG   I NH2  1 
ATOM   8167 N  N    . PRO   B 1 484 ? -24.877 -56.552 -29.387 1.00 24.40  ?  486 PRO   I N    1 
ATOM   8168 C  CA   . PRO   B 1 484 ? -25.197 -57.860 -28.849 1.00 26.95  ?  486 PRO   I CA   1 
ATOM   8169 C  C    . PRO   B 1 484 ? -26.562 -58.421 -29.304 1.00 27.96  ?  486 PRO   I C    1 
ATOM   8170 O  O    . PRO   B 1 484 ? -26.644 -59.619 -29.556 1.00 30.64  ?  486 PRO   I O    1 
ATOM   8171 C  CB   . PRO   B 1 484 ? -25.205 -57.643 -27.324 1.00 27.13  ?  486 PRO   I CB   1 
ATOM   8172 C  CG   . PRO   B 1 484 ? -24.445 -56.398 -27.067 1.00 27.54  ?  486 PRO   I CG   1 
ATOM   8173 C  CD   . PRO   B 1 484 ? -24.346 -55.627 -28.362 1.00 25.52  ?  486 PRO   I CD   1 
ATOM   8174 N  N    . CYS   B 1 485 ? -27.595 -57.572 -29.355 1.00 29.95  ?  487 CYS   I N    1 
ATOM   8175 C  CA   . CYS   B 1 485 ? -28.930 -57.928 -29.920 1.00 32.94  ?  487 CYS   I CA   1 
ATOM   8176 C  C    . CYS   B 1 485 ? -28.834 -58.439 -31.366 1.00 32.02  ?  487 CYS   I C    1 
ATOM   8177 O  O    . CYS   B 1 485 ? -29.452 -59.423 -31.721 1.00 31.49  ?  487 CYS   I O    1 
ATOM   8178 C  CB   . CYS   B 1 485 ? -29.889 -56.712 -29.864 1.00 35.56  ?  487 CYS   I CB   1 
ATOM   8179 S  SG   . CYS   B 1 485 ? -31.576 -56.942 -30.492 1.00 39.56  ?  487 CYS   I SG   1 
ATOM   8180 N  N    . PHE   B 1 486 ? -28.062 -57.754 -32.196 1.00 30.71  ?  488 PHE   I N    1 
ATOM   8181 C  CA   . PHE   B 1 486 ? -27.771 -58.267 -33.561 1.00 34.37  ?  488 PHE   I CA   1 
ATOM   8182 C  C    . PHE   B 1 486 ? -26.961 -59.560 -33.543 1.00 33.01  ?  488 PHE   I C    1 
ATOM   8183 O  O    . PHE   B 1 486 ? -27.321 -60.521 -34.234 1.00 28.67  ?  488 PHE   I O    1 
ATOM   8184 C  CB   . PHE   B 1 486 ? -27.041 -57.236 -34.400 1.00 32.77  ?  488 PHE   I CB   1 
ATOM   8185 C  CG   . PHE   B 1 486 ? -27.941 -56.255 -35.054 1.00 33.24  ?  488 PHE   I CG   1 
ATOM   8186 C  CD1  . PHE   B 1 486 ? -28.810 -56.667 -36.064 1.00 35.48  ?  488 PHE   I CD1  1 
ATOM   8187 C  CD2  . PHE   B 1 486 ? -27.890 -54.922 -34.724 1.00 32.64  ?  488 PHE   I CD2  1 
ATOM   8188 C  CE1  . PHE   B 1 486 ? -29.628 -55.751 -36.707 1.00 34.62  ?  488 PHE   I CE1  1 
ATOM   8189 C  CE2  . PHE   B 1 486 ? -28.694 -53.999 -35.362 1.00 34.16  ?  488 PHE   I CE2  1 
ATOM   8190 C  CZ   . PHE   B 1 486 ? -29.566 -54.418 -36.358 1.00 34.81  ?  488 PHE   I CZ   1 
ATOM   8191 N  N    . SER   B 1 487 ? -25.907 -59.591 -32.724 1.00 32.01  ?  489 SER   I N    1 
ATOM   8192 C  CA   . SER   B 1 487 ? -25.109 -60.798 -32.545 1.00 31.72  ?  489 SER   I CA   1 
ATOM   8193 C  C    . SER   B 1 487 ? -25.884 -62.007 -31.980 1.00 35.96  ?  489 SER   I C    1 
ATOM   8194 O  O    . SER   B 1 487 ? -25.385 -63.130 -32.031 1.00 32.74  ?  489 SER   I O    1 
ATOM   8195 C  CB   . SER   B 1 487 ? -23.931 -60.500 -31.633 1.00 30.63  ?  489 SER   I CB   1 
ATOM   8196 O  OG   . SER   B 1 487 ? -22.982 -59.677 -32.258 1.00 27.83  ?  489 SER   I OG   1 
ATOM   8197 N  N    . ALA   B 1 488 ? -27.063 -61.768 -31.390 1.00 40.56  ?  490 ALA   I N    1 
ATOM   8198 C  CA   . ALA   B 1 488 ? -27.961 -62.845 -30.915 1.00 41.11  ?  490 ALA   I CA   1 
ATOM   8199 C  C    . ALA   B 1 488 ? -28.966 -63.356 -31.957 1.00 39.07  ?  490 ALA   I C    1 
ATOM   8200 O  O    . ALA   B 1 488 ? -29.667 -64.335 -31.709 1.00 37.60  ?  490 ALA   I O    1 
ATOM   8201 C  CB   . ALA   B 1 488 ? -28.712 -62.383 -29.677 1.00 42.97  ?  490 ALA   I CB   1 
ATOM   8202 N  N    . LEU   B 1 489 ? -29.065 -62.683 -33.097 1.00 42.54  ?  491 LEU   I N    1 
ATOM   8203 C  CA   . LEU   B 1 489 ? -29.991 -63.103 -34.140 1.00 43.50  ?  491 LEU   I CA   1 
ATOM   8204 C  C    . LEU   B 1 489 ? -29.456 -64.419 -34.694 1.00 39.78  ?  491 LEU   I C    1 
ATOM   8205 O  O    . LEU   B 1 489 ? -28.325 -64.477 -35.154 1.00 37.57  ?  491 LEU   I O    1 
ATOM   8206 C  CB   . LEU   B 1 489 ? -30.138 -62.041 -35.240 1.00 43.87  ?  491 LEU   I CB   1 
ATOM   8207 C  CG   . LEU   B 1 489 ? -30.793 -60.682 -34.914 1.00 46.07  ?  491 LEU   I CG   1 
ATOM   8208 C  CD1  . LEU   B 1 489 ? -30.914 -59.863 -36.183 1.00 45.73  ?  491 LEU   I CD1  1 
ATOM   8209 C  CD2  . LEU   B 1 489 ? -32.162 -60.768 -34.228 1.00 46.47  ?  491 LEU   I CD2  1 
ATOM   8210 N  N    . GLU   B 1 490 ? -30.246 -65.477 -34.529 1.00 43.62  ?  492 GLU   I N    1 
ATOM   8211 C  CA   . GLU   B 1 490 ? -30.013 -66.793 -35.162 1.00 47.10  ?  492 GLU   I CA   1 
ATOM   8212 C  C    . GLU   B 1 490 ? -30.719 -66.842 -36.516 1.00 42.17  ?  492 GLU   I C    1 
ATOM   8213 O  O    . GLU   B 1 490 ? -31.472 -65.921 -36.874 1.00 39.63  ?  492 GLU   I O    1 
ATOM   8214 C  CB   . GLU   B 1 490 ? -30.549 -67.925 -34.276 1.00 50.21  ?  492 GLU   I CB   1 
ATOM   8215 C  CG   . GLU   B 1 490 ? -29.898 -68.045 -32.902 1.00 55.06  ?  492 GLU   I CG   1 
ATOM   8216 C  CD   . GLU   B 1 490 ? -30.889 -68.459 -31.828 1.00 60.41  ?  492 GLU   I CD   1 
ATOM   8217 O  OE1  . GLU   B 1 490 ? -31.788 -67.645 -31.507 1.00 63.46  ?  492 GLU   I OE1  1 
ATOM   8218 O  OE2  . GLU   B 1 490 ? -30.774 -69.592 -31.305 1.00 62.61  ?  492 GLU   I OE2  1 
ATOM   8219 N  N    . VAL   B 1 491 ? -30.494 -67.933 -37.251 1.00 45.26  ?  493 VAL   I N    1 
ATOM   8220 C  CA   . VAL   B 1 491 ? -31.063 -68.124 -38.611 1.00 43.83  ?  493 VAL   I CA   1 
ATOM   8221 C  C    . VAL   B 1 491 ? -32.599 -68.115 -38.563 1.00 43.23  ?  493 VAL   I C    1 
ATOM   8222 O  O    . VAL   B 1 491 ? -33.191 -68.642 -37.627 1.00 42.07  ?  493 VAL   I O    1 
ATOM   8223 C  CB   . VAL   B 1 491 ? -30.542 -69.424 -39.290 1.00 44.11  ?  493 VAL   I CB   1 
ATOM   8224 C  CG1  . VAL   B 1 491 ? -31.081 -69.560 -40.716 1.00 42.49  ?  493 VAL   I CG1  1 
ATOM   8225 C  CG2  . VAL   B 1 491 ? -29.003 -69.479 -39.289 1.00 44.18  ?  493 VAL   I CG2  1 
ATOM   8226 N  N    . ASP   B 1 492 ? -33.228 -67.468 -39.545 1.00 47.61  ?  494 ASP   I N    1 
ATOM   8227 C  CA   . ASP   B 1 492 ? -34.688 -67.461 -39.648 1.00 50.87  ?  494 ASP   I CA   1 
ATOM   8228 C  C    . ASP   B 1 492 ? -35.162 -68.779 -40.278 1.00 52.67  ?  494 ASP   I C    1 
ATOM   8229 O  O    . ASP   B 1 492 ? -35.308 -68.859 -41.491 1.00 52.56  ?  494 ASP   I O    1 
ATOM   8230 C  CB   . ASP   B 1 492 ? -35.163 -66.255 -40.471 1.00 52.06  ?  494 ASP   I CB   1 
ATOM   8231 C  CG   . ASP   B 1 492 ? -36.697 -66.060 -40.444 1.00 60.13  ?  494 ASP   I CG   1 
ATOM   8232 O  OD1  . ASP   B 1 492 ? -37.408 -66.635 -39.584 1.00 67.65  ?  494 ASP   I OD1  1 
ATOM   8233 O  OD2  . ASP   B 1 492 ? -37.201 -65.293 -41.291 1.00 63.03  ?  494 ASP   I OD2  1 
ATOM   8234 N  N    . GLU   B 1 493 ? -35.405 -69.798 -39.444 1.00 55.30  ?  495 GLU   I N    1 
ATOM   8235 C  CA   . GLU   B 1 493 ? -36.047 -71.078 -39.873 1.00 54.07  ?  495 GLU   I CA   1 
ATOM   8236 C  C    . GLU   B 1 493 ? -37.538 -70.934 -40.284 1.00 52.78  ?  495 GLU   I C    1 
ATOM   8237 O  O    . GLU   B 1 493 ? -38.131 -71.855 -40.859 1.00 53.30  ?  495 GLU   I O    1 
ATOM   8238 C  CB   . GLU   B 1 493 ? -35.912 -72.144 -38.772 1.00 51.39  ?  495 GLU   I CB   1 
ATOM   8239 N  N    . THR   B 1 494 ? -38.126 -69.784 -39.963 1.00 52.47  ?  496 THR   I N    1 
ATOM   8240 C  CA   . THR   B 1 494 ? -39.465 -69.384 -40.405 1.00 54.31  ?  496 THR   I CA   1 
ATOM   8241 C  C    . THR   B 1 494 ? -39.478 -68.831 -41.845 1.00 58.58  ?  496 THR   I C    1 
ATOM   8242 O  O    . THR   B 1 494 ? -40.554 -68.659 -42.442 1.00 60.08  ?  496 THR   I O    1 
ATOM   8243 C  CB   . THR   B 1 494 ? -40.087 -68.399 -39.355 1.00 54.71  ?  496 THR   I CB   1 
ATOM   8244 O  OG1  . THR   B 1 494 ? -41.184 -69.052 -38.695 1.00 55.55  ?  496 THR   I OG1  1 
ATOM   8245 C  CG2  . THR   B 1 494 ? -40.563 -67.046 -39.938 1.00 50.88  ?  496 THR   I CG2  1 
ATOM   8246 N  N    . TYR   B 1 495 ? -38.295 -68.553 -42.402 1.00 58.15  ?  497 TYR   I N    1 
ATOM   8247 C  CA   . TYR   B 1 495 ? -38.188 -68.048 -43.767 1.00 54.32  ?  497 TYR   I CA   1 
ATOM   8248 C  C    . TYR   B 1 495 ? -38.608 -69.090 -44.795 1.00 56.51  ?  497 TYR   I C    1 
ATOM   8249 O  O    . TYR   B 1 495 ? -37.946 -70.130 -44.961 1.00 52.31  ?  497 TYR   I O    1 
ATOM   8250 C  CB   . TYR   B 1 495 ? -36.757 -67.570 -44.100 1.00 50.51  ?  497 TYR   I CB   1 
ATOM   8251 C  CG   . TYR   B 1 495 ? -36.671 -66.886 -45.459 1.00 46.00  ?  497 TYR   I CG   1 
ATOM   8252 C  CD1  . TYR   B 1 495 ? -37.408 -65.734 -45.718 1.00 43.91  ?  497 TYR   I CD1  1 
ATOM   8253 C  CD2  . TYR   B 1 495 ? -35.864 -67.388 -46.479 1.00 45.64  ?  497 TYR   I CD2  1 
ATOM   8254 C  CE1  . TYR   B 1 495 ? -37.356 -65.108 -46.949 1.00 44.27  ?  497 TYR   I CE1  1 
ATOM   8255 C  CE2  . TYR   B 1 495 ? -35.805 -66.758 -47.714 1.00 45.18  ?  497 TYR   I CE2  1 
ATOM   8256 C  CZ   . TYR   B 1 495 ? -36.565 -65.626 -47.936 1.00 44.28  ?  497 TYR   I CZ   1 
ATOM   8257 O  OH   . TYR   B 1 495 ? -36.533 -64.968 -49.128 1.00 46.44  ?  497 TYR   I OH   1 
ATOM   8258 N  N    . VAL   B 1 496 ? -39.718 -68.793 -45.467 1.00 59.35  ?  498 VAL   I N    1 
ATOM   8259 C  CA   . VAL   B 1 496 ? -40.080 -69.475 -46.714 1.00 61.87  ?  498 VAL   I CA   1 
ATOM   8260 C  C    . VAL   B 1 496 ? -39.060 -69.143 -47.829 1.00 59.80  ?  498 VAL   I C    1 
ATOM   8261 O  O    . VAL   B 1 496 ? -38.699 -67.978 -48.004 1.00 55.16  ?  498 VAL   I O    1 
ATOM   8262 C  CB   . VAL   B 1 496 ? -41.523 -69.128 -47.175 1.00 61.88  ?  498 VAL   I CB   1 
ATOM   8263 C  CG1  . VAL   B 1 496 ? -42.539 -69.861 -46.313 1.00 60.18  ?  498 VAL   I CG1  1 
ATOM   8264 C  CG2  . VAL   B 1 496 ? -41.799 -67.618 -47.174 1.00 63.03  ?  498 VAL   I CG2  1 
ATOM   8265 N  N    . PRO   B 1 497 ? -38.584 -70.159 -48.580 1.00 64.79  ?  499 PRO   I N    1 
ATOM   8266 C  CA   . PRO   B 1 497 ? -37.578 -69.837 -49.593 1.00 68.65  ?  499 PRO   I CA   1 
ATOM   8267 C  C    . PRO   B 1 497 ? -38.203 -69.103 -50.767 1.00 68.38  ?  499 PRO   I C    1 
ATOM   8268 O  O    . PRO   B 1 497 ? -39.367 -69.356 -51.095 1.00 70.21  ?  499 PRO   I O    1 
ATOM   8269 C  CB   . PRO   B 1 497 ? -37.036 -71.214 -50.026 1.00 70.72  ?  499 PRO   I CB   1 
ATOM   8270 C  CG   . PRO   B 1 497 ? -37.710 -72.230 -49.160 1.00 69.17  ?  499 PRO   I CG   1 
ATOM   8271 C  CD   . PRO   B 1 497 ? -38.956 -71.584 -48.640 1.00 68.48  ?  499 PRO   I CD   1 
ATOM   8272 N  N    . LYS   B 1 498 ? -37.439 -68.203 -51.390 1.00 68.73  ?  500 LYS   I N    1 
ATOM   8273 C  CA   . LYS   B 1 498 ? -37.991 -67.348 -52.443 1.00 64.54  ?  500 LYS   I CA   1 
ATOM   8274 C  C    . LYS   B 1 498 ? -37.962 -67.981 -53.834 1.00 63.75  ?  500 LYS   I C    1 
ATOM   8275 O  O    . LYS   B 1 498 ? -37.158 -68.868 -54.126 1.00 60.14  ?  500 LYS   I O    1 
ATOM   8276 C  CB   . LYS   B 1 498 ? -37.359 -65.946 -52.438 1.00 61.14  ?  500 LYS   I CB   1 
ATOM   8277 C  CG   . LYS   B 1 498 ? -36.184 -65.680 -53.373 1.00 56.63  ?  500 LYS   I CG   1 
ATOM   8278 C  CD   . LYS   B 1 498 ? -36.445 -64.460 -54.248 1.00 54.70  ?  500 LYS   I CD   1 
ATOM   8279 C  CE   . LYS   B 1 498 ? -36.680 -63.184 -53.458 1.00 51.68  ?  500 LYS   I CE   1 
ATOM   8280 N  NZ   . LYS   B 1 498 ? -36.506 -61.994 -54.332 1.00 50.59  ?  500 LYS   I NZ   1 
ATOM   8281 N  N    . GLU   B 1 499 ? -38.858 -67.471 -54.674 1.00 66.35  ?  501 GLU   I N    1 
ATOM   8282 C  CA   . GLU   B 1 499 ? -39.077 -67.932 -56.038 1.00 73.05  ?  501 GLU   I CA   1 
ATOM   8283 C  C    . GLU   B 1 499 ? -37.761 -68.005 -56.816 1.00 74.11  ?  501 GLU   I C    1 
ATOM   8284 O  O    . GLU   B 1 499 ? -36.911 -67.119 -56.696 1.00 75.60  ?  501 GLU   I O    1 
ATOM   8285 C  CB   . GLU   B 1 499 ? -40.060 -66.961 -56.720 1.00 80.39  ?  501 GLU   I CB   1 
ATOM   8286 C  CG   . GLU   B 1 499 ? -40.410 -67.214 -58.186 1.00 87.29  ?  501 GLU   I CG   1 
ATOM   8287 C  CD   . GLU   B 1 499 ? -41.339 -68.396 -58.416 1.00 91.97  ?  501 GLU   I CD   1 
ATOM   8288 O  OE1  . GLU   B 1 499 ? -42.312 -68.566 -57.648 1.00 99.44  ?  501 GLU   I OE1  1 
ATOM   8289 O  OE2  . GLU   B 1 499 ? -41.108 -69.146 -59.394 1.00 93.09  ?  501 GLU   I OE2  1 
ATOM   8290 N  N    . PHE   B 1 500 ? -37.586 -69.079 -57.583 1.00 71.41  ?  502 PHE   I N    1 
ATOM   8291 C  CA   . PHE   B 1 500 ? -36.499 -69.154 -58.546 1.00 66.74  ?  502 PHE   I CA   1 
ATOM   8292 C  C    . PHE   B 1 500 ? -36.783 -68.187 -59.697 1.00 63.43  ?  502 PHE   I C    1 
ATOM   8293 O  O    . PHE   B 1 500 ? -37.844 -68.230 -60.312 1.00 61.11  ?  502 PHE   I O    1 
ATOM   8294 C  CB   . PHE   B 1 500 ? -36.328 -70.568 -59.110 1.00 67.27  ?  502 PHE   I CB   1 
ATOM   8295 C  CG   . PHE   B 1 500 ? -35.227 -70.669 -60.127 1.00 66.51  ?  502 PHE   I CG   1 
ATOM   8296 C  CD1  . PHE   B 1 500 ? -33.899 -70.503 -59.747 1.00 68.33  ?  502 PHE   I CD1  1 
ATOM   8297 C  CD2  . PHE   B 1 500 ? -35.512 -70.893 -61.466 1.00 65.85  ?  502 PHE   I CD2  1 
ATOM   8298 C  CE1  . PHE   B 1 500 ? -32.875 -70.572 -60.681 1.00 66.91  ?  502 PHE   I CE1  1 
ATOM   8299 C  CE2  . PHE   B 1 500 ? -34.493 -70.962 -62.407 1.00 66.86  ?  502 PHE   I CE2  1 
ATOM   8300 C  CZ   . PHE   B 1 500 ? -33.175 -70.800 -62.014 1.00 66.97  ?  502 PHE   I CZ   1 
ATOM   8301 N  N    . ASN   B 1 501 ? -35.826 -67.311 -59.974 1.00 61.69  ?  503 ASN   I N    1 
ATOM   8302 C  CA   . ASN   B 1 501 ? -35.886 -66.441 -61.141 1.00 61.05  ?  503 ASN   I CA   1 
ATOM   8303 C  C    . ASN   B 1 501 ? -34.617 -66.662 -61.970 1.00 55.36  ?  503 ASN   I C    1 
ATOM   8304 O  O    . ASN   B 1 501 ? -33.507 -66.685 -61.432 1.00 51.96  ?  503 ASN   I O    1 
ATOM   8305 C  CB   . ASN   B 1 501 ? -36.023 -64.983 -60.718 1.00 60.93  ?  503 ASN   I CB   1 
ATOM   8306 C  CG   . ASN   B 1 501 ? -35.975 -64.036 -61.895 1.00 61.02  ?  503 ASN   I CG   1 
ATOM   8307 O  OD1  . ASN   B 1 501 ? -34.936 -63.460 -62.187 1.00 59.33  ?  503 ASN   I OD1  1 
ATOM   8308 N  ND2  . ASN   B 1 501 ? -37.096 -63.897 -62.595 1.00 62.44  ?  503 ASN   I ND2  1 
ATOM   8309 N  N    . ALA   B 1 502 ? -34.803 -66.829 -63.278 1.00 49.46  ?  504 ALA   I N    1 
ATOM   8310 C  CA   . ALA   B 1 502 ? -33.724 -67.212 -64.183 1.00 44.23  ?  504 ALA   I CA   1 
ATOM   8311 C  C    . ALA   B 1 502 ? -32.810 -66.036 -64.521 1.00 41.66  ?  504 ALA   I C    1 
ATOM   8312 O  O    . ALA   B 1 502 ? -31.591 -66.226 -64.544 1.00 41.69  ?  504 ALA   I O    1 
ATOM   8313 C  CB   . ALA   B 1 502 ? -34.295 -67.833 -65.447 1.00 45.41  ?  504 ALA   I CB   1 
ATOM   8314 N  N    . GLU   B 1 503 ? -33.382 -64.841 -64.746 1.00 40.41  ?  505 GLU   I N    1 
ATOM   8315 C  CA   . GLU   B 1 503 ? -32.597 -63.596 -65.026 1.00 43.82  ?  505 GLU   I CA   1 
ATOM   8316 C  C    . GLU   B 1 503 ? -31.596 -63.321 -63.921 1.00 44.48  ?  505 GLU   I C    1 
ATOM   8317 O  O    . GLU   B 1 503 ? -30.409 -63.074 -64.193 1.00 47.96  ?  505 GLU   I O    1 
ATOM   8318 C  CB   . GLU   B 1 503 ? -33.485 -62.351 -65.173 1.00 39.93  ?  505 GLU   I CB   1 
ATOM   8319 N  N    . THR   B 1 504 ? -32.090 -63.392 -62.678 1.00 45.55  ?  506 THR   I N    1 
ATOM   8320 C  CA   . THR   B 1 504 ? -31.272 -63.283 -61.466 1.00 44.93  ?  506 THR   I CA   1 
ATOM   8321 C  C    . THR   B 1 504 ? -29.955 -64.049 -61.619 1.00 45.42  ?  506 THR   I C    1 
ATOM   8322 O  O    . THR   B 1 504 ? -28.889 -63.522 -61.306 1.00 45.46  ?  506 THR   I O    1 
ATOM   8323 C  CB   . THR   B 1 504 ? -32.036 -63.808 -60.227 1.00 44.23  ?  506 THR   I CB   1 
ATOM   8324 O  OG1  . THR   B 1 504 ? -33.297 -63.142 -60.115 1.00 42.89  ?  506 THR   I OG1  1 
ATOM   8325 C  CG2  . THR   B 1 504 ? -31.227 -63.592 -58.926 1.00 43.72  ?  506 THR   I CG2  1 
ATOM   8326 N  N    . PHE   B 1 505 ? -30.048 -65.274 -62.133 1.00 41.87  ?  507 PHE   I N    1 
ATOM   8327 C  CA   . PHE   B 1 505 ? -28.887 -66.116 -62.376 1.00 44.33  ?  507 PHE   I CA   1 
ATOM   8328 C  C    . PHE   B 1 505 ? -28.499 -66.220 -63.870 1.00 47.52  ?  507 PHE   I C    1 
ATOM   8329 O  O    . PHE   B 1 505 ? -28.083 -67.289 -64.351 1.00 49.88  ?  507 PHE   I O    1 
ATOM   8330 C  CB   . PHE   B 1 505 ? -29.154 -67.491 -61.761 1.00 42.86  ?  507 PHE   I CB   1 
ATOM   8331 C  CG   . PHE   B 1 505 ? -29.616 -67.413 -60.342 1.00 44.02  ?  507 PHE   I CG   1 
ATOM   8332 C  CD1  . PHE   B 1 505 ? -28.778 -66.895 -59.359 1.00 43.54  ?  507 PHE   I CD1  1 
ATOM   8333 C  CD2  . PHE   B 1 505 ? -30.903 -67.811 -59.986 1.00 43.98  ?  507 PHE   I CD2  1 
ATOM   8334 C  CE1  . PHE   B 1 505 ? -29.217 -66.800 -58.040 1.00 45.69  ?  507 PHE   I CE1  1 
ATOM   8335 C  CE2  . PHE   B 1 505 ? -31.344 -67.720 -58.668 1.00 44.67  ?  507 PHE   I CE2  1 
ATOM   8336 C  CZ   . PHE   B 1 505 ? -30.509 -67.208 -57.695 1.00 44.73  ?  507 PHE   I CZ   1 
ATOM   8337 N  N    . THR   B 1 506 ? -28.620 -65.110 -64.597 1.00 48.39  ?  508 THR   I N    1 
ATOM   8338 C  CA   . THR   B 1 506 ? -28.064 -65.007 -65.944 1.00 50.44  ?  508 THR   I CA   1 
ATOM   8339 C  C    . THR   B 1 506 ? -27.106 -63.840 -65.943 1.00 47.06  ?  508 THR   I C    1 
ATOM   8340 O  O    . THR   B 1 506 ? -27.438 -62.762 -65.463 1.00 44.80  ?  508 THR   I O    1 
ATOM   8341 C  CB   . THR   B 1 506 ? -29.120 -64.744 -67.041 1.00 52.63  ?  508 THR   I CB   1 
ATOM   8342 O  OG1  . THR   B 1 506 ? -30.348 -65.388 -66.713 1.00 53.06  ?  508 THR   I OG1  1 
ATOM   8343 C  CG2  . THR   B 1 506 ? -28.617 -65.259 -68.394 1.00 50.89  ?  508 THR   I CG2  1 
ATOM   8344 N  N    . PHE   B 1 507 ? -25.923 -64.079 -66.482 1.00 47.90  ?  509 PHE   I N    1 
ATOM   8345 C  CA   . PHE   B 1 507 ? -24.873 -63.089 -66.547 1.00 53.33  ?  509 PHE   I CA   1 
ATOM   8346 C  C    . PHE   B 1 507 ? -24.458 -62.992 -68.004 1.00 52.10  ?  509 PHE   I C    1 
ATOM   8347 O  O    . PHE   B 1 507 ? -24.538 -63.979 -68.742 1.00 50.34  ?  509 PHE   I O    1 
ATOM   8348 C  CB   . PHE   B 1 507 ? -23.723 -63.516 -65.638 1.00 55.39  ?  509 PHE   I CB   1 
ATOM   8349 C  CG   . PHE   B 1 507 ? -24.201 -64.053 -64.331 1.00 63.92  ?  509 PHE   I CG   1 
ATOM   8350 C  CD1  . PHE   B 1 507 ? -24.622 -65.383 -64.226 1.00 64.98  ?  509 PHE   I CD1  1 
ATOM   8351 C  CD2  . PHE   B 1 507 ? -24.328 -63.216 -63.228 1.00 69.14  ?  509 PHE   I CD2  1 
ATOM   8352 C  CE1  . PHE   B 1 507 ? -25.126 -65.873 -63.036 1.00 66.73  ?  509 PHE   I CE1  1 
ATOM   8353 C  CE2  . PHE   B 1 507 ? -24.825 -63.706 -62.027 1.00 68.99  ?  509 PHE   I CE2  1 
ATOM   8354 C  CZ   . PHE   B 1 507 ? -25.220 -65.035 -61.931 1.00 69.83  ?  509 PHE   I CZ   1 
ATOM   8355 N  N    . HIS   B 1 508 ? -24.064 -61.790 -68.417 1.00 50.56  ?  510 HIS   I N    1 
ATOM   8356 C  CA   . HIS   B 1 508 ? -23.648 -61.538 -69.796 1.00 48.99  ?  510 HIS   I CA   1 
ATOM   8357 C  C    . HIS   B 1 508 ? -22.148 -61.255 -69.815 1.00 49.38  ?  510 HIS   I C    1 
ATOM   8358 O  O    . HIS   B 1 508 ? -21.518 -61.131 -68.759 1.00 49.90  ?  510 HIS   I O    1 
ATOM   8359 C  CB   . HIS   B 1 508 ? -24.468 -60.394 -70.372 1.00 46.03  ?  510 HIS   I CB   1 
ATOM   8360 C  CG   . HIS   B 1 508 ? -25.943 -60.564 -70.187 1.00 44.18  ?  510 HIS   I CG   1 
ATOM   8361 N  ND1  . HIS   B 1 508 ? -26.586 -61.755 -70.427 1.00 45.13  ?  510 HIS   I ND1  1 
ATOM   8362 C  CD2  . HIS   B 1 508 ? -26.906 -59.694 -69.794 1.00 47.54  ?  510 HIS   I CD2  1 
ATOM   8363 C  CE1  . HIS   B 1 508 ? -27.880 -61.616 -70.194 1.00 43.20  ?  510 HIS   I CE1  1 
ATOM   8364 N  NE2  . HIS   B 1 508 ? -28.100 -60.376 -69.807 1.00 45.17  ?  510 HIS   I NE2  1 
ATOM   8365 N  N    . ALA   B 1 509 ? -21.569 -61.158 -71.005 1.00 52.04  ?  511 ALA   I N    1 
ATOM   8366 C  CA   . ALA   B 1 509 ? -20.116 -60.968 -71.143 1.00 55.34  ?  511 ALA   I CA   1 
ATOM   8367 C  C    . ALA   B 1 509 ? -19.623 -59.601 -70.663 1.00 54.59  ?  511 ALA   I C    1 
ATOM   8368 O  O    . ALA   B 1 509 ? -18.401 -59.413 -70.507 1.00 56.36  ?  511 ALA   I O    1 
ATOM   8369 C  CB   . ALA   B 1 509 ? -19.665 -61.217 -72.583 1.00 58.82  ?  511 ALA   I CB   1 
ATOM   8370 N  N    . ASP   B 1 510 ? -20.556 -58.669 -70.415 1.00 54.67  ?  512 ASP   I N    1 
ATOM   8371 C  CA   . ASP   B 1 510 ? -20.218 -57.348 -69.856 1.00 57.16  ?  512 ASP   I CA   1 
ATOM   8372 C  C    . ASP   B 1 510 ? -19.669 -57.343 -68.417 1.00 54.13  ?  512 ASP   I C    1 
ATOM   8373 O  O    . ASP   B 1 510 ? -19.155 -56.306 -67.994 1.00 48.82  ?  512 ASP   I O    1 
ATOM   8374 C  CB   . ASP   B 1 510 ? -21.384 -56.338 -70.008 1.00 60.99  ?  512 ASP   I CB   1 
ATOM   8375 C  CG   . ASP   B 1 510 ? -22.535 -56.565 -69.015 1.00 66.77  ?  512 ASP   I CG   1 
ATOM   8376 O  OD1  . ASP   B 1 510 ? -22.810 -57.727 -68.620 1.00 72.91  ?  512 ASP   I OD1  1 
ATOM   8377 O  OD2  . ASP   B 1 510 ? -23.185 -55.557 -68.648 1.00 65.78  ?  512 ASP   I OD2  1 
ATOM   8378 N  N    . ILE   B 1 511 ? -19.752 -58.465 -67.680 1.00 52.39  ?  513 ILE   I N    1 
ATOM   8379 C  CA   . ILE   B 1 511 ? -19.087 -58.559 -66.347 1.00 55.13  ?  513 ILE   I CA   1 
ATOM   8380 C  C    . ILE   B 1 511 ? -17.570 -58.820 -66.365 1.00 52.00  ?  513 ILE   I C    1 
ATOM   8381 O  O    . ILE   B 1 511 ? -16.883 -58.560 -65.381 1.00 54.09  ?  513 ILE   I O    1 
ATOM   8382 C  CB   . ILE   B 1 511 ? -19.771 -59.557 -65.376 1.00 58.98  ?  513 ILE   I CB   1 
ATOM   8383 C  CG1  . ILE   B 1 511 ? -19.640 -61.006 -65.844 1.00 57.19  ?  513 ILE   I CG1  1 
ATOM   8384 C  CG2  . ILE   B 1 511 ? -21.230 -59.163 -65.150 1.00 62.52  ?  513 ILE   I CG2  1 
ATOM   8385 C  CD1  . ILE   B 1 511 ? -20.071 -61.990 -64.774 1.00 60.93  ?  513 ILE   I CD1  1 
ATOM   8386 N  N    . CYS   B 1 512 ? -17.044 -59.321 -67.472 1.00 50.89  ?  514 CYS   I N    1 
ATOM   8387 C  CA   . CYS   B 1 512 ? -15.595 -59.355 -67.678 1.00 52.23  ?  514 CYS   I CA   1 
ATOM   8388 C  C    . CYS   B 1 512 ? -15.034 -57.944 -67.898 1.00 50.40  ?  514 CYS   I C    1 
ATOM   8389 O  O    . CYS   B 1 512 ? -13.841 -57.725 -67.693 1.00 55.15  ?  514 CYS   I O    1 
ATOM   8390 C  CB   . CYS   B 1 512 ? -15.245 -60.255 -68.865 1.00 55.93  ?  514 CYS   I CB   1 
ATOM   8391 S  SG   . CYS   B 1 512 ? -16.134 -61.843 -68.856 1.00 62.69  ?  514 CYS   I SG   1 
ATOM   8392 N  N    . THR   B 1 513 ? -15.903 -57.011 -68.311 1.00 48.27  ?  515 THR   I N    1 
ATOM   8393 C  CA   . THR   B 1 513 ? -15.573 -55.602 -68.596 1.00 48.85  ?  515 THR   I CA   1 
ATOM   8394 C  C    . THR   B 1 513 ? -15.909 -54.618 -67.455 1.00 47.78  ?  515 THR   I C    1 
ATOM   8395 O  O    . THR   B 1 513 ? -15.671 -53.417 -67.594 1.00 46.95  ?  515 THR   I O    1 
ATOM   8396 C  CB   . THR   B 1 513 ? -16.309 -55.061 -69.873 1.00 43.77  ?  515 THR   I CB   1 
ATOM   8397 O  OG1  . THR   B 1 513 ? -17.620 -54.565 -69.538 1.00 40.20  ?  515 THR   I OG1  1 
ATOM   8398 C  CG2  . THR   B 1 513 ? -16.429 -56.116 -70.966 1.00 45.13  ?  515 THR   I CG2  1 
ATOM   8399 N  N    . LEU   B 1 514 ? -16.503 -55.084 -66.363 1.00 49.49  ?  516 LEU   I N    1 
ATOM   8400 C  CA   . LEU   B 1 514 ? -16.789 -54.170 -65.255 1.00 54.48  ?  516 LEU   I CA   1 
ATOM   8401 C  C    . LEU   B 1 514 ? -15.540 -54.046 -64.405 1.00 47.33  ?  516 LEU   I C    1 
ATOM   8402 O  O    . LEU   B 1 514 ? -14.691 -54.927 -64.410 1.00 43.28  ?  516 LEU   I O    1 
ATOM   8403 C  CB   . LEU   B 1 514 ? -18.008 -54.628 -64.431 1.00 61.14  ?  516 LEU   I CB   1 
ATOM   8404 C  CG   . LEU   B 1 514 ? -19.394 -54.300 -65.038 1.00 67.73  ?  516 LEU   I CG   1 
ATOM   8405 C  CD1  . LEU   B 1 514 ? -20.529 -55.071 -64.356 1.00 68.07  ?  516 LEU   I CD1  1 
ATOM   8406 C  CD2  . LEU   B 1 514 ? -19.687 -52.800 -65.014 1.00 68.96  ?  516 LEU   I CD2  1 
ATOM   8407 N  N    . SER   B 1 515 ? -15.436 -52.933 -63.689 1.00 50.55  ?  517 SER   I N    1 
ATOM   8408 C  CA   . SER   B 1 515 ? -14.371 -52.730 -62.701 1.00 50.73  ?  517 SER   I CA   1 
ATOM   8409 C  C    . SER   B 1 515 ? -14.375 -53.837 -61.647 1.00 54.28  ?  517 SER   I C    1 
ATOM   8410 O  O    . SER   B 1 515 ? -15.410 -54.477 -61.424 1.00 55.13  ?  517 SER   I O    1 
ATOM   8411 C  CB   . SER   B 1 515 ? -14.536 -51.377 -62.020 1.00 51.11  ?  517 SER   I CB   1 
ATOM   8412 O  OG   . SER   B 1 515 ? -15.826 -51.230 -61.438 1.00 51.33  ?  517 SER   I OG   1 
ATOM   8413 N  N    . GLU   B 1 516 ? -13.218 -54.063 -61.015 1.00 53.31  ?  518 GLU   I N    1 
ATOM   8414 C  CA   . GLU   B 1 516 ? -13.070 -55.085 -59.976 1.00 49.56  ?  518 GLU   I CA   1 
ATOM   8415 C  C    . GLU   B 1 516 ? -14.177 -54.920 -58.945 1.00 50.73  ?  518 GLU   I C    1 
ATOM   8416 O  O    . GLU   B 1 516 ? -14.817 -55.897 -58.550 1.00 45.73  ?  518 GLU   I O    1 
ATOM   8417 C  CB   . GLU   B 1 516 ? -11.708 -54.973 -59.297 1.00 47.40  ?  518 GLU   I CB   1 
ATOM   8418 N  N    . LYS   B 1 517 ? -14.421 -53.661 -58.575 1.00 49.08  ?  519 LYS   I N    1 
ATOM   8419 C  CA   . LYS   B 1 517 ? -15.419 -53.283 -57.575 1.00 48.72  ?  519 LYS   I CA   1 
ATOM   8420 C  C    . LYS   B 1 517 ? -16.856 -53.615 -58.033 1.00 48.12  ?  519 LYS   I C    1 
ATOM   8421 O  O    . LYS   B 1 517 ? -17.615 -54.237 -57.294 1.00 48.32  ?  519 LYS   I O    1 
ATOM   8422 C  CB   . LYS   B 1 517 ? -15.279 -51.788 -57.230 1.00 47.77  ?  519 LYS   I CB   1 
ATOM   8423 C  CG   . LYS   B 1 517 ? -15.309 -51.467 -55.741 1.00 50.24  ?  519 LYS   I CG   1 
ATOM   8424 C  CD   . LYS   B 1 517 ? -13.951 -51.663 -55.060 1.00 50.83  ?  519 LYS   I CD   1 
ATOM   8425 N  N    . GLU   B 1 518 ? -17.203 -53.220 -59.252 1.00 45.69  ?  520 GLU   I N    1 
ATOM   8426 C  CA   . GLU   B 1 518 ? -18.516 -53.517 -59.848 1.00 44.37  ?  520 GLU   I CA   1 
ATOM   8427 C  C    . GLU   B 1 518 ? -18.779 -55.004 -60.067 1.00 39.97  ?  520 GLU   I C    1 
ATOM   8428 O  O    . GLU   B 1 518 ? -19.907 -55.438 -60.010 1.00 36.95  ?  520 GLU   I O    1 
ATOM   8429 C  CB   . GLU   B 1 518 ? -18.647 -52.821 -61.197 1.00 50.97  ?  520 GLU   I CB   1 
ATOM   8430 C  CG   . GLU   B 1 518 ? -19.131 -51.378 -61.144 1.00 55.14  ?  520 GLU   I CG   1 
ATOM   8431 C  CD   . GLU   B 1 518 ? -20.519 -51.190 -61.735 1.00 65.61  ?  520 GLU   I CD   1 
ATOM   8432 O  OE1  . GLU   B 1 518 ? -21.120 -52.184 -62.231 1.00 65.06  ?  520 GLU   I OE1  1 
ATOM   8433 O  OE2  . GLU   B 1 518 ? -21.009 -50.029 -61.717 1.00 71.74  ?  520 GLU   I OE2  1 
ATOM   8434 N  N    . ARG   B 1 519 ? -17.726 -55.748 -60.360 1.00 40.07  ?  521 ARG   I N    1 
ATOM   8435 C  CA   . ARG   B 1 519 ? -17.786 -57.194 -60.621 1.00 42.07  ?  521 ARG   I CA   1 
ATOM   8436 C  C    . ARG   B 1 519 ? -18.101 -57.903 -59.295 1.00 40.12  ?  521 ARG   I C    1 
ATOM   8437 O  O    . ARG   B 1 519 ? -18.864 -58.857 -59.250 1.00 36.87  ?  521 ARG   I O    1 
ATOM   8438 C  CB   . ARG   B 1 519 ? -16.424 -57.681 -61.197 1.00 41.33  ?  521 ARG   I CB   1 
ATOM   8439 C  CG   . ARG   B 1 519 ? -16.445 -58.835 -62.214 1.00 43.77  ?  521 ARG   I CG   1 
ATOM   8440 C  CD   . ARG   B 1 519 ? -15.135 -58.894 -63.022 1.00 43.55  ?  521 ARG   I CD   1 
ATOM   8441 N  NE   . ARG   B 1 519 ? -14.932 -57.694 -63.861 1.00 40.74  ?  521 ARG   I NE   1 
ATOM   8442 N  N    . GLN   B 1 520 ? -17.495 -57.414 -58.214 1.00 41.82  ?  522 GLN   I N    1 
ATOM   8443 C  CA   . GLN   B 1 520 ? -17.738 -57.954 -56.866 1.00 38.42  ?  522 GLN   I CA   1 
ATOM   8444 C  C    . GLN   B 1 520 ? -19.182 -57.730 -56.446 1.00 34.47  ?  522 GLN   I C    1 
ATOM   8445 O  O    . GLN   B 1 520 ? -19.874 -58.695 -56.096 1.00 31.33  ?  522 GLN   I O    1 
ATOM   8446 C  CB   . GLN   B 1 520 ? -16.768 -57.364 -55.856 1.00 38.07  ?  522 GLN   I CB   1 
ATOM   8447 C  CG   . GLN   B 1 520 ? -15.339 -57.876 -56.028 1.00 40.27  ?  522 GLN   I CG   1 
ATOM   8448 C  CD   . GLN   B 1 520 ? -14.350 -57.090 -55.196 1.00 42.30  ?  522 GLN   I CD   1 
ATOM   8449 O  OE1  . GLN   B 1 520 ? -14.425 -55.861 -55.129 1.00 49.64  ?  522 GLN   I OE1  1 
ATOM   8450 N  NE2  . GLN   B 1 520 ? -13.418 -57.781 -54.565 1.00 41.45  ?  522 GLN   I NE2  1 
ATOM   8451 N  N    . ILE   B 1 521 ? -19.649 -56.492 -56.560 1.00 30.28  ?  523 ILE   I N    1 
ATOM   8452 C  CA   . ILE   B 1 521 ? -21.023 -56.162 -56.231 1.00 33.56  ?  523 ILE   I CA   1 
ATOM   8453 C  C    . ILE   B 1 521 ? -22.026 -57.095 -56.937 1.00 36.79  ?  523 ILE   I C    1 
ATOM   8454 O  O    . ILE   B 1 521 ? -23.053 -57.478 -56.340 1.00 34.63  ?  523 ILE   I O    1 
ATOM   8455 C  CB   . ILE   B 1 521 ? -21.411 -54.717 -56.627 1.00 36.03  ?  523 ILE   I CB   1 
ATOM   8456 C  CG1  . ILE   B 1 521 ? -20.513 -53.651 -55.960 1.00 40.67  ?  523 ILE   I CG1  1 
ATOM   8457 C  CG2  . ILE   B 1 521 ? -22.892 -54.438 -56.307 1.00 35.05  ?  523 ILE   I CG2  1 
ATOM   8458 C  CD1  . ILE   B 1 521 ? -20.974 -53.146 -54.612 1.00 42.33  ?  523 ILE   I CD1  1 
ATOM   8459 N  N    . LYS   B 1 522 ? -21.772 -57.402 -58.221 1.00 38.02  ?  524 LYS   I N    1 
ATOM   8460 C  CA   . LYS   B 1 522 ? -22.715 -58.217 -59.005 1.00 36.91  ?  524 LYS   I CA   1 
ATOM   8461 C  C    . LYS   B 1 522 ? -22.664 -59.703 -58.608 1.00 33.73  ?  524 LYS   I C    1 
ATOM   8462 O  O    . LYS   B 1 522 ? -23.709 -60.345 -58.558 1.00 30.04  ?  524 LYS   I O    1 
ATOM   8463 C  CB   . LYS   B 1 522 ? -22.513 -58.046 -60.521 1.00 40.35  ?  524 LYS   I CB   1 
ATOM   8464 C  CG   . LYS   B 1 522 ? -23.618 -57.276 -61.236 1.00 42.33  ?  524 LYS   I CG   1 
ATOM   8465 C  CD   . LYS   B 1 522 ? -24.834 -58.143 -61.519 1.00 40.65  ?  524 LYS   I CD   1 
ATOM   8466 N  N    . LYS   B 1 523 ? -21.471 -60.238 -58.347 1.00 31.78  ?  525 LYS   I N    1 
ATOM   8467 C  CA   . LYS   B 1 523 ? -21.321 -61.615 -57.842 1.00 34.04  ?  525 LYS   I CA   1 
ATOM   8468 C  C    . LYS   B 1 523 ? -21.965 -61.760 -56.482 1.00 35.01  ?  525 LYS   I C    1 
ATOM   8469 O  O    . LYS   B 1 523 ? -22.627 -62.763 -56.210 1.00 42.59  ?  525 LYS   I O    1 
ATOM   8470 C  CB   . LYS   B 1 523 ? -19.864 -62.006 -57.651 1.00 37.02  ?  525 LYS   I CB   1 
ATOM   8471 C  CG   . LYS   B 1 523 ? -19.004 -62.046 -58.907 1.00 41.57  ?  525 LYS   I CG   1 
ATOM   8472 C  CD   . LYS   B 1 523 ? -17.553 -61.595 -58.648 1.00 40.70  ?  525 LYS   I CD   1 
ATOM   8473 C  CE   . LYS   B 1 523 ? -16.572 -62.738 -58.742 1.00 41.53  ?  525 LYS   I CE   1 
ATOM   8474 N  NZ   . LYS   B 1 523 ? -15.183 -62.239 -58.555 1.00 44.87  ?  525 LYS   I NZ   1 
ATOM   8475 N  N    . GLN   B 1 524 ? -21.728 -60.778 -55.618 1.00 32.40  ?  526 GLN   I N    1 
ATOM   8476 C  CA   . GLN   B 1 524 ? -22.252 -60.769 -54.242 1.00 29.04  ?  526 GLN   I CA   1 
ATOM   8477 C  C    . GLN   B 1 524 ? -23.762 -60.674 -54.250 1.00 28.99  ?  526 GLN   I C    1 
ATOM   8478 O  O    . GLN   B 1 524 ? -24.435 -61.368 -53.465 1.00 29.35  ?  526 GLN   I O    1 
ATOM   8479 C  CB   . GLN   B 1 524 ? -21.620 -59.642 -53.427 1.00 26.22  ?  526 GLN   I CB   1 
ATOM   8480 C  CG   . GLN   B 1 524 ? -20.163 -59.928 -53.183 1.00 24.76  ?  526 GLN   I CG   1 
ATOM   8481 C  CD   . GLN   B 1 524 ? -19.423 -58.848 -52.425 1.00 24.64  ?  526 GLN   I CD   1 
ATOM   8482 O  OE1  . GLN   B 1 524 ? -19.627 -57.625 -52.617 1.00 23.00  ?  526 GLN   I OE1  1 
ATOM   8483 N  NE2  . GLN   B 1 524 ? -18.525 -59.296 -51.575 1.00 22.55  ?  526 GLN   I NE2  1 
ATOM   8484 N  N    . THR   B 1 525 ? -24.290 -59.899 -55.190 1.00 28.04  ?  527 THR   I N    1 
ATOM   8485 C  CA   . THR   B 1 525 ? -25.733 -59.810 -55.414 1.00 28.79  ?  527 THR   I CA   1 
ATOM   8486 C  C    . THR   B 1 525 ? -26.344 -61.181 -55.762 1.00 28.63  ?  527 THR   I C    1 
ATOM   8487 O  O    . THR   B 1 525 ? -27.369 -61.554 -55.232 1.00 31.51  ?  527 THR   I O    1 
ATOM   8488 C  CB   . THR   B 1 525 ? -26.083 -58.770 -56.501 1.00 27.36  ?  527 THR   I CB   1 
ATOM   8489 O  OG1  . THR   B 1 525 ? -25.452 -57.520 -56.199 1.00 28.64  ?  527 THR   I OG1  1 
ATOM   8490 C  CG2  . THR   B 1 525 ? -27.566 -58.561 -56.575 1.00 28.27  ?  527 THR   I CG2  1 
ATOM   8491 N  N    . ALA   B 1 526 ? -25.689 -61.930 -56.620 1.00 29.42  ?  528 ALA   I N    1 
ATOM   8492 C  CA   . ALA   B 1 526 ? -26.120 -63.306 -56.914 1.00 31.71  ?  528 ALA   I CA   1 
ATOM   8493 C  C    . ALA   B 1 526 ? -25.876 -64.295 -55.764 1.00 30.28  ?  528 ALA   I C    1 
ATOM   8494 O  O    . ALA   B 1 526 ? -26.494 -65.361 -55.714 1.00 34.30  ?  528 ALA   I O    1 
ATOM   8495 C  CB   . ALA   B 1 526 ? -25.433 -63.798 -58.184 1.00 30.73  ?  528 ALA   I CB   1 
ATOM   8496 N  N    . LEU   B 1 527 ? -24.942 -63.974 -54.876 1.00 30.16  ?  529 LEU   I N    1 
ATOM   8497 C  CA   . LEU   B 1 527 ? -24.663 -64.810 -53.716 1.00 29.10  ?  529 LEU   I CA   1 
ATOM   8498 C  C    . LEU   B 1 527 ? -25.816 -64.688 -52.792 1.00 28.29  ?  529 LEU   I C    1 
ATOM   8499 O  O    . LEU   B 1 527 ? -26.322 -65.704 -52.342 1.00 27.52  ?  529 LEU   I O    1 
ATOM   8500 C  CB   . LEU   B 1 527 ? -23.348 -64.420 -53.000 1.00 28.65  ?  529 LEU   I CB   1 
ATOM   8501 C  CG   . LEU   B 1 527 ? -22.959 -65.241 -51.757 1.00 28.15  ?  529 LEU   I CG   1 
ATOM   8502 C  CD1  . LEU   B 1 527 ? -23.167 -66.754 -51.919 1.00 28.73  ?  529 LEU   I CD1  1 
ATOM   8503 C  CD2  . LEU   B 1 527 ? -21.519 -64.961 -51.392 1.00 28.08  ?  529 LEU   I CD2  1 
ATOM   8504 N  N    . VAL   B 1 528 ? -26.235 -63.443 -52.531 1.00 27.68  ?  530 VAL   I N    1 
ATOM   8505 C  CA   . VAL   B 1 528 ? -27.348 -63.147 -51.615 1.00 28.85  ?  530 VAL   I CA   1 
ATOM   8506 C  C    . VAL   B 1 528 ? -28.631 -63.798 -52.101 1.00 30.13  ?  530 VAL   I C    1 
ATOM   8507 O  O    . VAL   B 1 528 ? -29.408 -64.356 -51.277 1.00 30.89  ?  530 VAL   I O    1 
ATOM   8508 C  CB   . VAL   B 1 528 ? -27.606 -61.631 -51.452 1.00 27.97  ?  530 VAL   I CB   1 
ATOM   8509 C  CG1  . VAL   B 1 528 ? -28.955 -61.370 -50.818 1.00 26.29  ?  530 VAL   I CG1  1 
ATOM   8510 C  CG2  . VAL   B 1 528 ? -26.503 -60.989 -50.612 1.00 27.22  ?  530 VAL   I CG2  1 
ATOM   8511 N  N    . GLU   B 1 529 ? -28.854 -63.666 -53.412 1.00 29.05  ?  531 GLU   I N    1 
ATOM   8512 C  CA   . GLU   B 1 529 ? -30.046 -64.182 -54.073 1.00 29.23  ?  531 GLU   I CA   1 
ATOM   8513 C  C    . GLU   B 1 529 ? -30.037 -65.718 -54.119 1.00 29.42  ?  531 GLU   I C    1 
ATOM   8514 O  O    . GLU   B 1 529 ? -31.092 -66.349 -53.991 1.00 31.34  ?  531 GLU   I O    1 
ATOM   8515 C  CB   . GLU   B 1 529 ? -30.199 -63.556 -55.457 1.00 29.62  ?  531 GLU   I CB   1 
ATOM   8516 C  CG   . GLU   B 1 529 ? -30.579 -62.064 -55.435 1.00 28.83  ?  531 GLU   I CG   1 
ATOM   8517 C  CD   . GLU   B 1 529 ? -32.066 -61.806 -55.237 1.00 30.00  ?  531 GLU   I CD   1 
ATOM   8518 O  OE1  . GLU   B 1 529 ? -32.839 -62.787 -55.144 1.00 26.51  ?  531 GLU   I OE1  1 
ATOM   8519 O  OE2  . GLU   B 1 529 ? -32.482 -60.612 -55.198 1.00 32.46  ?  531 GLU   I OE2  1 
ATOM   8520 N  N    . LEU   B 1 530 ? -28.855 -66.309 -54.238 1.00 29.00  ?  532 LEU   I N    1 
ATOM   8521 C  CA   . LEU   B 1 530 ? -28.672 -67.762 -54.139 1.00 29.60  ?  532 LEU   I CA   1 
ATOM   8522 C  C    . LEU   B 1 530 ? -29.009 -68.293 -52.744 1.00 30.57  ?  532 LEU   I C    1 
ATOM   8523 O  O    . LEU   B 1 530 ? -29.564 -69.403 -52.611 1.00 33.77  ?  532 LEU   I O    1 
ATOM   8524 C  CB   . LEU   B 1 530 ? -27.225 -68.164 -54.539 1.00 31.15  ?  532 LEU   I CB   1 
ATOM   8525 C  CG   . LEU   B 1 530 ? -26.697 -69.574 -54.161 1.00 33.27  ?  532 LEU   I CG   1 
ATOM   8526 C  CD1  . LEU   B 1 530 ? -27.596 -70.704 -54.680 1.00 34.49  ?  532 LEU   I CD1  1 
ATOM   8527 C  CD2  . LEU   B 1 530 ? -25.274 -69.799 -54.646 1.00 30.18  ?  532 LEU   I CD2  1 
ATOM   8528 N  N    . VAL   B 1 531 ? -28.662 -67.515 -51.718 1.00 28.45  ?  533 VAL   I N    1 
ATOM   8529 C  CA   . VAL   B 1 531 ? -28.886 -67.893 -50.324 1.00 27.66  ?  533 VAL   I CA   1 
ATOM   8530 C  C    . VAL   B 1 531 ? -30.343 -67.691 -49.983 1.00 27.09  ?  533 VAL   I C    1 
ATOM   8531 O  O    . VAL   B 1 531 ? -30.929 -68.564 -49.376 1.00 25.61  ?  533 VAL   I O    1 
ATOM   8532 C  CB   . VAL   B 1 531 ? -27.951 -67.144 -49.350 1.00 25.25  ?  533 VAL   I CB   1 
ATOM   8533 C  CG1  . VAL   B 1 531 ? -28.279 -67.452 -47.907 1.00 26.28  ?  533 VAL   I CG1  1 
ATOM   8534 C  CG2  . VAL   B 1 531 ? -26.537 -67.555 -49.607 1.00 26.36  ?  533 VAL   I CG2  1 
ATOM   8535 N  N    . LYS   B 1 532 ? -30.924 -66.572 -50.391 1.00 28.17  ?  534 LYS   I N    1 
ATOM   8536 C  CA   . LYS   B 1 532 ? -32.385 -66.396 -50.314 1.00 31.77  ?  534 LYS   I CA   1 
ATOM   8537 C  C    . LYS   B 1 532 ? -33.236 -67.460 -51.011 1.00 36.09  ?  534 LYS   I C    1 
ATOM   8538 O  O    . LYS   B 1 532 ? -34.340 -67.770 -50.549 1.00 40.99  ?  534 LYS   I O    1 
ATOM   8539 C  CB   . LYS   B 1 532 ? -32.799 -65.036 -50.863 1.00 32.31  ?  534 LYS   I CB   1 
ATOM   8540 C  CG   . LYS   B 1 532 ? -32.434 -63.890 -49.927 1.00 32.25  ?  534 LYS   I CG   1 
ATOM   8541 C  CD   . LYS   B 1 532 ? -32.956 -62.569 -50.429 1.00 32.11  ?  534 LYS   I CD   1 
ATOM   8542 C  CE   . LYS   B 1 532 ? -32.411 -61.439 -49.581 1.00 33.95  ?  534 LYS   I CE   1 
ATOM   8543 N  NZ   . LYS   B 1 532 ? -32.967 -60.153 -50.064 1.00 34.62  ?  534 LYS   I NZ   1 
ATOM   8544 N  N    . HIS   B 1 533 ? -32.754 -67.990 -52.127 1.00 39.32  ?  535 HIS   I N    1 
ATOM   8545 C  CA   . HIS   B 1 533 ? -33.500 -69.003 -52.848 1.00 42.79  ?  535 HIS   I CA   1 
ATOM   8546 C  C    . HIS   B 1 533 ? -33.272 -70.406 -52.268 1.00 41.55  ?  535 HIS   I C    1 
ATOM   8547 O  O    . HIS   B 1 533 ? -34.211 -71.208 -52.220 1.00 43.57  ?  535 HIS   I O    1 
ATOM   8548 C  CB   . HIS   B 1 533 ? -33.207 -68.979 -54.350 1.00 44.41  ?  535 HIS   I CB   1 
ATOM   8549 C  CG   . HIS   B 1 533 ? -33.818 -70.134 -55.083 1.00 46.74  ?  535 HIS   I CG   1 
ATOM   8550 N  ND1  . HIS   B 1 533 ? -35.181 -70.291 -55.217 1.00 48.40  ?  535 HIS   I ND1  1 
ATOM   8551 C  CD2  . HIS   B 1 533 ? -33.254 -71.208 -55.683 1.00 49.04  ?  535 HIS   I CD2  1 
ATOM   8552 C  CE1  . HIS   B 1 533 ? -35.431 -71.403 -55.885 1.00 51.31  ?  535 HIS   I CE1  1 
ATOM   8553 N  NE2  . HIS   B 1 533 ? -34.279 -71.979 -56.179 1.00 50.56  ?  535 HIS   I NE2  1 
ATOM   8554 N  N    . LYS   B 1 534 ? -32.051 -70.706 -51.842 1.00 39.08  ?  536 LYS   I N    1 
ATOM   8555 C  CA   . LYS   B 1 534 ? -31.784 -71.953 -51.101 1.00 41.60  ?  536 LYS   I CA   1 
ATOM   8556 C  C    . LYS   B 1 534 ? -31.038 -71.768 -49.747 1.00 39.31  ?  536 LYS   I C    1 
ATOM   8557 O  O    . LYS   B 1 534 ? -29.843 -72.050 -49.623 1.00 36.11  ?  536 LYS   I O    1 
ATOM   8558 C  CB   . LYS   B 1 534 ? -31.124 -72.978 -52.020 1.00 43.05  ?  536 LYS   I CB   1 
ATOM   8559 C  CG   . LYS   B 1 534 ? -32.120 -73.545 -53.051 1.00 44.85  ?  536 LYS   I CG   1 
ATOM   8560 C  CD   . LYS   B 1 534 ? -31.941 -75.040 -53.298 1.00 47.03  ?  536 LYS   I CD   1 
ATOM   8561 C  CE   . LYS   B 1 534 ? -33.218 -75.725 -53.797 1.00 48.82  ?  536 LYS   I CE   1 
ATOM   8562 N  NZ   . LYS   B 1 534 ? -33.770 -75.059 -55.009 1.00 47.27  ?  536 LYS   I NZ   1 
ATOM   8563 N  N    . PRO   B 1 535 ? -31.775 -71.321 -48.719 1.00 43.41  ?  537 PRO   I N    1 
ATOM   8564 C  CA   . PRO   B 1 535 ? -31.168 -71.066 -47.401 1.00 46.16  ?  537 PRO   I CA   1 
ATOM   8565 C  C    . PRO   B 1 535 ? -30.629 -72.318 -46.690 1.00 46.62  ?  537 PRO   I C    1 
ATOM   8566 O  O    . PRO   B 1 535 ? -29.581 -72.242 -46.042 1.00 49.20  ?  537 PRO   I O    1 
ATOM   8567 C  CB   . PRO   B 1 535 ? -32.289 -70.389 -46.604 1.00 47.49  ?  537 PRO   I CB   1 
ATOM   8568 C  CG   . PRO   B 1 535 ? -33.561 -70.657 -47.346 1.00 48.88  ?  537 PRO   I CG   1 
ATOM   8569 C  CD   . PRO   B 1 535 ? -33.221 -70.994 -48.762 1.00 46.07  ?  537 PRO   I CD   1 
ATOM   8570 N  N    . LYS   B 1 536 ? -31.279 -73.473 -46.847 1.00 45.58  ?  538 LYS   I N    1 
ATOM   8571 C  CA   . LYS   B 1 536 ? -30.740 -74.732 -46.265 1.00 42.78  ?  538 LYS   I CA   1 
ATOM   8572 C  C    . LYS   B 1 536 ? -29.422 -75.202 -46.924 1.00 41.98  ?  538 LYS   I C    1 
ATOM   8573 O  O    . LYS   B 1 536 ? -28.880 -76.228 -46.537 1.00 38.80  ?  538 LYS   I O    1 
ATOM   8574 C  CB   . LYS   B 1 536 ? -31.769 -75.866 -46.323 1.00 37.57  ?  538 LYS   I CB   1 
ATOM   8575 N  N    . ALA   B 1 537 ? -28.923 -74.477 -47.926 1.00 45.30  ?  539 ALA   I N    1 
ATOM   8576 C  CA   . ALA   B 1 537 ? -27.618 -74.778 -48.532 1.00 47.29  ?  539 ALA   I CA   1 
ATOM   8577 C  C    . ALA   B 1 537 ? -26.455 -74.731 -47.520 1.00 49.70  ?  539 ALA   I C    1 
ATOM   8578 O  O    . ALA   B 1 537 ? -26.134 -73.692 -46.954 1.00 52.85  ?  539 ALA   I O    1 
ATOM   8579 C  CB   . ALA   B 1 537 ? -27.350 -73.846 -49.704 1.00 44.50  ?  539 ALA   I CB   1 
ATOM   8580 N  N    . THR   B 1 538 ? -25.840 -75.887 -47.305 1.00 54.23  ?  540 THR   I N    1 
ATOM   8581 C  CA   . THR   B 1 538 ? -24.716 -76.048 -46.387 1.00 54.01  ?  540 THR   I CA   1 
ATOM   8582 C  C    . THR   B 1 538 ? -23.496 -75.293 -46.936 1.00 50.72  ?  540 THR   I C    1 
ATOM   8583 O  O    . THR   B 1 538 ? -23.485 -74.930 -48.116 1.00 41.76  ?  540 THR   I O    1 
ATOM   8584 C  CB   . THR   B 1 538 ? -24.411 -77.567 -46.214 1.00 57.30  ?  540 THR   I CB   1 
ATOM   8585 O  OG1  . THR   B 1 538 ? -25.614 -78.269 -45.864 1.00 53.14  ?  540 THR   I OG1  1 
ATOM   8586 C  CG2  . THR   B 1 538 ? -23.370 -77.834 -45.124 1.00 64.40  ?  540 THR   I CG2  1 
ATOM   8587 N  N    . LYS   B 1 539 ? -22.483 -75.049 -46.094 1.00 49.05  ?  541 LYS   I N    1 
ATOM   8588 C  CA   . LYS   B 1 539 ? -21.221 -74.461 -46.579 1.00 49.43  ?  541 LYS   I CA   1 
ATOM   8589 C  C    . LYS   B 1 539 ? -20.654 -75.257 -47.752 1.00 46.77  ?  541 LYS   I C    1 
ATOM   8590 O  O    . LYS   B 1 539 ? -20.295 -74.673 -48.767 1.00 42.79  ?  541 LYS   I O    1 
ATOM   8591 C  CB   . LYS   B 1 539 ? -20.142 -74.300 -45.473 1.00 49.74  ?  541 LYS   I CB   1 
ATOM   8592 C  CG   . LYS   B 1 539 ? -19.786 -72.840 -45.167 1.00 52.76  ?  541 LYS   I CG   1 
ATOM   8593 C  CD   . LYS   B 1 539 ? -18.502 -72.675 -44.355 1.00 56.18  ?  541 LYS   I CD   1 
ATOM   8594 N  N    . GLU   B 1 540 ? -20.598 -76.581 -47.587 1.00 47.55  ?  542 GLU   I N    1 
ATOM   8595 C  CA   . GLU   B 1 540 ? -20.063 -77.523 -48.586 1.00 48.02  ?  542 GLU   I CA   1 
ATOM   8596 C  C    . GLU   B 1 540 ? -20.568 -77.243 -50.008 1.00 41.62  ?  542 GLU   I C    1 
ATOM   8597 O  O    . GLU   B 1 540 ? -19.794 -77.033 -50.946 1.00 33.12  ?  542 GLU   I O    1 
ATOM   8598 C  CB   . GLU   B 1 540 ? -20.436 -78.994 -48.235 1.00 53.98  ?  542 GLU   I CB   1 
ATOM   8599 C  CG   . GLU   B 1 540 ? -20.153 -79.526 -46.822 1.00 59.35  ?  542 GLU   I CG   1 
ATOM   8600 C  CD   . GLU   B 1 540 ? -18.911 -78.960 -46.161 1.00 60.88  ?  542 GLU   I CD   1 
ATOM   8601 O  OE1  . GLU   B 1 540 ? -19.024 -77.890 -45.532 1.00 63.27  ?  542 GLU   I OE1  1 
ATOM   8602 O  OE2  . GLU   B 1 540 ? -17.839 -79.594 -46.253 1.00 62.73  ?  542 GLU   I OE2  1 
ATOM   8603 N  N    . GLN   B 1 541 ? -21.890 -77.228 -50.126 1.00 43.26  ?  543 GLN   I N    1 
ATOM   8604 C  CA   . GLN   B 1 541 ? -22.576 -77.107 -51.399 1.00 41.10  ?  543 GLN   I CA   1 
ATOM   8605 C  C    . GLN   B 1 541 ? -22.348 -75.714 -51.971 1.00 41.80  ?  543 GLN   I C    1 
ATOM   8606 O  O    . GLN   B 1 541 ? -21.849 -75.559 -53.085 1.00 36.93  ?  543 GLN   I O    1 
ATOM   8607 C  CB   . GLN   B 1 541 ? -24.063 -77.390 -51.191 1.00 45.49  ?  543 GLN   I CB   1 
ATOM   8608 C  CG   . GLN   B 1 541 ? -24.363 -78.833 -50.774 1.00 49.39  ?  543 GLN   I CG   1 
ATOM   8609 C  CD   . GLN   B 1 541 ? -25.821 -79.054 -50.409 1.00 51.97  ?  543 GLN   I CD   1 
ATOM   8610 O  OE1  . GLN   B 1 541 ? -26.329 -78.460 -49.457 1.00 57.95  ?  543 GLN   I OE1  1 
ATOM   8611 N  NE2  . GLN   B 1 541 ? -26.498 -79.921 -51.157 1.00 57.33  ?  543 GLN   I NE2  1 
ATOM   8612 N  N    . LEU   B 1 542 ? -22.660 -74.703 -51.161 1.00 43.29  ?  544 LEU   I N    1 
ATOM   8613 C  CA   . LEU   B 1 542 ? -22.462 -73.311 -51.541 1.00 42.73  ?  544 LEU   I CA   1 
ATOM   8614 C  C    . LEU   B 1 542 ? -21.062 -73.078 -52.074 1.00 39.78  ?  544 LEU   I C    1 
ATOM   8615 O  O    . LEU   B 1 542 ? -20.912 -72.477 -53.135 1.00 40.60  ?  544 LEU   I O    1 
ATOM   8616 C  CB   . LEU   B 1 542 ? -22.757 -72.366 -50.373 1.00 42.95  ?  544 LEU   I CB   1 
ATOM   8617 C  CG   . LEU   B 1 542 ? -23.361 -71.031 -50.761 1.00 44.80  ?  544 LEU   I CG   1 
ATOM   8618 C  CD1  . LEU   B 1 542 ? -24.821 -71.201 -51.156 1.00 44.99  ?  544 LEU   I CD1  1 
ATOM   8619 C  CD2  . LEU   B 1 542 ? -23.233 -70.071 -49.581 1.00 48.31  ?  544 LEU   I CD2  1 
ATOM   8620 N  N    . LYS   B 1 543 ? -20.047 -73.592 -51.379 1.00 39.73  ?  545 LYS   I N    1 
ATOM   8621 C  CA   . LYS   B 1 543 ? -18.663 -73.495 -51.865 1.00 39.07  ?  545 LYS   I CA   1 
ATOM   8622 C  C    . LYS   B 1 543 ? -18.591 -74.083 -53.285 1.00 42.00  ?  545 LYS   I C    1 
ATOM   8623 O  O    . LYS   B 1 543 ? -18.234 -73.375 -54.230 1.00 42.33  ?  545 LYS   I O    1 
ATOM   8624 C  CB   . LYS   B 1 543 ? -17.657 -74.169 -50.911 1.00 39.57  ?  545 LYS   I CB   1 
ATOM   8625 C  CG   . LYS   B 1 543 ? -16.180 -73.841 -51.161 1.00 41.58  ?  545 LYS   I CG   1 
ATOM   8626 N  N    . ALA   B 1 544 ? -19.009 -75.340 -53.449 1.00 40.48  ?  546 ALA   I N    1 
ATOM   8627 C  CA   . ALA   B 1 544 ? -18.974 -76.004 -54.762 1.00 40.69  ?  546 ALA   I CA   1 
ATOM   8628 C  C    . ALA   B 1 544 ? -19.693 -75.221 -55.909 1.00 41.24  ?  546 ALA   I C    1 
ATOM   8629 O  O    . ALA   B 1 544 ? -19.272 -75.286 -57.060 1.00 40.90  ?  546 ALA   I O    1 
ATOM   8630 C  CB   . ALA   B 1 544 ? -19.524 -77.424 -54.646 1.00 41.79  ?  546 ALA   I CB   1 
ATOM   8631 N  N    . VAL   B 1 545 ? -20.753 -74.478 -55.591 1.00 40.56  ?  547 VAL   I N    1 
ATOM   8632 C  CA   . VAL   B 1 545 ? -21.448 -73.642 -56.583 1.00 41.36  ?  547 VAL   I CA   1 
ATOM   8633 C  C    . VAL   B 1 545 ? -20.579 -72.414 -56.914 1.00 41.79  ?  547 VAL   I C    1 
ATOM   8634 O  O    . VAL   B 1 545 ? -20.232 -72.190 -58.064 1.00 44.28  ?  547 VAL   I O    1 
ATOM   8635 C  CB   . VAL   B 1 545 ? -22.861 -73.231 -56.094 1.00 40.21  ?  547 VAL   I CB   1 
ATOM   8636 C  CG1  . VAL   B 1 545 ? -23.536 -72.292 -57.088 1.00 39.45  ?  547 VAL   I CG1  1 
ATOM   8637 C  CG2  . VAL   B 1 545 ? -23.736 -74.471 -55.859 1.00 39.85  ?  547 VAL   I CG2  1 
ATOM   8638 N  N    . MET   B 1 546 ? -20.195 -71.662 -55.889 1.00 42.61  ?  548 MET   I N    1 
ATOM   8639 C  CA   . MET   B 1 546 ? -19.317 -70.498 -56.035 1.00 45.57  ?  548 MET   I CA   1 
ATOM   8640 C  C    . MET   B 1 546 ? -18.044 -70.799 -56.829 1.00 47.47  ?  548 MET   I C    1 
ATOM   8641 O  O    . MET   B 1 546 ? -17.590 -69.982 -57.634 1.00 47.99  ?  548 MET   I O    1 
ATOM   8642 C  CB   . MET   B 1 546 ? -18.889 -69.971 -54.657 1.00 44.25  ?  548 MET   I CB   1 
ATOM   8643 C  CG   . MET   B 1 546 ? -19.993 -69.358 -53.828 1.00 44.91  ?  548 MET   I CG   1 
ATOM   8644 S  SD   . MET   B 1 546 ? -19.375 -68.504 -52.362 1.00 55.28  ?  548 MET   I SD   1 
ATOM   8645 C  CE   . MET   B 1 546 ? -17.796 -69.269 -51.962 1.00 53.22  ?  548 MET   I CE   1 
ATOM   8646 N  N    . ASP   B 1 547 ? -17.474 -71.966 -56.569 1.00 47.64  ?  549 ASP   I N    1 
ATOM   8647 C  CA   . ASP   B 1 547 ? -16.230 -72.390 -57.181 1.00 51.92  ?  549 ASP   I CA   1 
ATOM   8648 C  C    . ASP   B 1 547 ? -16.430 -72.680 -58.682 1.00 52.17  ?  549 ASP   I C    1 
ATOM   8649 O  O    . ASP   B 1 547 ? -15.533 -72.402 -59.493 1.00 52.20  ?  549 ASP   I O    1 
ATOM   8650 C  CB   . ASP   B 1 547 ? -15.696 -73.645 -56.464 1.00 55.59  ?  549 ASP   I CB   1 
ATOM   8651 C  CG   . ASP   B 1 547 ? -15.472 -73.435 -54.946 1.00 58.87  ?  549 ASP   I CG   1 
ATOM   8652 O  OD1  . ASP   B 1 547 ? -15.302 -72.268 -54.492 1.00 56.12  ?  549 ASP   I OD1  1 
ATOM   8653 O  OD2  . ASP   B 1 547 ? -15.485 -74.462 -54.214 1.00 58.77  ?  549 ASP   I OD2  1 
ATOM   8654 N  N    . ASP   B 1 548 ? -17.594 -73.242 -59.033 1.00 50.09  ?  550 ASP   I N    1 
ATOM   8655 C  CA   . ASP   B 1 548 ? -17.982 -73.460 -60.436 1.00 47.57  ?  550 ASP   I CA   1 
ATOM   8656 C  C    . ASP   B 1 548 ? -18.296 -72.138 -61.100 1.00 46.91  ?  550 ASP   I C    1 
ATOM   8657 O  O    . ASP   B 1 548 ? -17.887 -71.914 -62.234 1.00 44.55  ?  550 ASP   I O    1 
ATOM   8658 C  CB   . ASP   B 1 548 ? -19.195 -74.390 -60.561 1.00 45.46  ?  550 ASP   I CB   1 
ATOM   8659 C  CG   . ASP   B 1 548 ? -18.897 -75.829 -60.126 1.00 46.89  ?  550 ASP   I CG   1 
ATOM   8660 O  OD1  . ASP   B 1 548 ? -17.716 -76.249 -60.056 1.00 48.33  ?  550 ASP   I OD1  1 
ATOM   8661 O  OD2  . ASP   B 1 548 ? -19.875 -76.555 -59.842 1.00 49.36  ?  550 ASP   I OD2  1 
ATOM   8662 N  N    . PHE   B 1 549 ? -19.026 -71.260 -60.405 1.00 48.01  ?  551 PHE   I N    1 
ATOM   8663 C  CA   . PHE   B 1 549 ? -19.228 -69.899 -60.902 1.00 48.32  ?  551 PHE   I CA   1 
ATOM   8664 C  C    . PHE   B 1 549 ? -17.886 -69.255 -61.188 1.00 49.02  ?  551 PHE   I C    1 
ATOM   8665 O  O    . PHE   B 1 549 ? -17.705 -68.670 -62.246 1.00 48.98  ?  551 PHE   I O    1 
ATOM   8666 C  CB   . PHE   B 1 549 ? -20.023 -69.023 -59.941 1.00 44.57  ?  551 PHE   I CB   1 
ATOM   8667 C  CG   . PHE   B 1 549 ? -20.385 -67.684 -60.515 1.00 45.75  ?  551 PHE   I CG   1 
ATOM   8668 C  CD1  . PHE   B 1 549 ? -21.485 -67.545 -61.356 1.00 47.43  ?  551 PHE   I CD1  1 
ATOM   8669 C  CD2  . PHE   B 1 549 ? -19.602 -66.555 -60.246 1.00 47.72  ?  551 PHE   I CD2  1 
ATOM   8670 C  CE1  . PHE   B 1 549 ? -21.818 -66.303 -61.892 1.00 47.58  ?  551 PHE   I CE1  1 
ATOM   8671 C  CE2  . PHE   B 1 549 ? -19.926 -65.315 -60.782 1.00 45.37  ?  551 PHE   I CE2  1 
ATOM   8672 C  CZ   . PHE   B 1 549 ? -21.038 -65.186 -61.608 1.00 47.48  ?  551 PHE   I CZ   1 
ATOM   8673 N  N    . ALA   B 1 550 ? -16.947 -69.380 -60.252 1.00 53.95  ?  552 ALA   I N    1 
ATOM   8674 C  CA   . ALA   B 1 550 ? -15.580 -68.849 -60.439 1.00 57.30  ?  552 ALA   I CA   1 
ATOM   8675 C  C    . ALA   B 1 550 ? -14.849 -69.475 -61.649 1.00 55.00  ?  552 ALA   I C    1 
ATOM   8676 O  O    . ALA   B 1 550 ? -14.116 -68.782 -62.347 1.00 54.18  ?  552 ALA   I O    1 
ATOM   8677 C  CB   . ALA   B 1 550 ? -14.748 -69.017 -59.161 1.00 59.59  ?  552 ALA   I CB   1 
ATOM   8678 N  N    . ALA   B 1 551 ? -15.047 -70.777 -61.865 1.00 55.42  ?  553 ALA   I N    1 
ATOM   8679 C  CA   . ALA   B 1 551 ? -14.549 -71.496 -63.055 1.00 53.26  ?  553 ALA   I CA   1 
ATOM   8680 C  C    . ALA   B 1 551 ? -15.217 -70.989 -64.332 1.00 52.00  ?  553 ALA   I C    1 
ATOM   8681 O  O    . ALA   B 1 551 ? -14.548 -70.460 -65.226 1.00 53.78  ?  553 ALA   I O    1 
ATOM   8682 C  CB   . ALA   B 1 551 ? -14.766 -73.010 -62.903 1.00 53.90  ?  553 ALA   I CB   1 
ATOM   8683 N  N    . PHE   B 1 552 ? -16.537 -71.167 -64.396 1.00 47.13  ?  554 PHE   I N    1 
ATOM   8684 C  CA   . PHE   B 1 552 ? -17.393 -70.537 -65.385 1.00 43.66  ?  554 PHE   I CA   1 
ATOM   8685 C  C    . PHE   B 1 552 ? -16.892 -69.144 -65.820 1.00 47.34  ?  554 PHE   I C    1 
ATOM   8686 O  O    . PHE   B 1 552 ? -16.521 -68.956 -66.981 1.00 48.92  ?  554 PHE   I O    1 
ATOM   8687 C  CB   . PHE   B 1 552 ? -18.834 -70.474 -64.833 1.00 42.21  ?  554 PHE   I CB   1 
ATOM   8688 C  CG   . PHE   B 1 552 ? -19.749 -69.596 -65.620 1.00 43.25  ?  554 PHE   I CG   1 
ATOM   8689 C  CD1  . PHE   B 1 552 ? -20.314 -70.041 -66.807 1.00 42.53  ?  554 PHE   I CD1  1 
ATOM   8690 C  CD2  . PHE   B 1 552 ? -20.011 -68.299 -65.201 1.00 42.91  ?  554 PHE   I CD2  1 
ATOM   8691 C  CE1  . PHE   B 1 552 ? -21.132 -69.214 -67.547 1.00 41.53  ?  554 PHE   I CE1  1 
ATOM   8692 C  CE2  . PHE   B 1 552 ? -20.829 -67.470 -65.943 1.00 42.68  ?  554 PHE   I CE2  1 
ATOM   8693 C  CZ   . PHE   B 1 552 ? -21.384 -67.927 -67.119 1.00 43.66  ?  554 PHE   I CZ   1 
ATOM   8694 N  N    . VAL   B 1 553 ? -16.857 -68.186 -64.894 1.00 49.70  ?  555 VAL   I N    1 
ATOM   8695 C  CA   . VAL   B 1 553 ? -16.496 -66.798 -65.228 1.00 48.86  ?  555 VAL   I CA   1 
ATOM   8696 C  C    . VAL   B 1 553 ? -15.141 -66.741 -65.920 1.00 49.60  ?  555 VAL   I C    1 
ATOM   8697 O  O    . VAL   B 1 553 ? -15.049 -66.179 -67.000 1.00 47.34  ?  555 VAL   I O    1 
ATOM   8698 C  CB   . VAL   B 1 553 ? -16.494 -65.853 -63.995 1.00 48.39  ?  555 VAL   I CB   1 
ATOM   8699 C  CG1  . VAL   B 1 553 ? -15.938 -64.478 -64.350 1.00 45.48  ?  555 VAL   I CG1  1 
ATOM   8700 C  CG2  . VAL   B 1 553 ? -17.901 -65.671 -63.460 1.00 50.40  ?  555 VAL   I CG2  1 
ATOM   8701 N  N    . GLU   B 1 554 ? -14.113 -67.340 -65.309 1.00 57.27  ?  556 GLU   I N    1 
ATOM   8702 C  CA   . GLU   B 1 554 ? -12.734 -67.293 -65.841 1.00 64.21  ?  556 GLU   I CA   1 
ATOM   8703 C  C    . GLU   B 1 554 ? -12.646 -67.971 -67.205 1.00 65.69  ?  556 GLU   I C    1 
ATOM   8704 O  O    . GLU   B 1 554 ? -11.932 -67.490 -68.077 1.00 64.25  ?  556 GLU   I O    1 
ATOM   8705 C  CB   . GLU   B 1 554 ? -11.717 -67.937 -64.880 1.00 70.90  ?  556 GLU   I CB   1 
ATOM   8706 C  CG   . GLU   B 1 554 ? -10.249 -67.568 -65.167 1.00 77.39  ?  556 GLU   I CG   1 
ATOM   8707 C  CD   . GLU   B 1 554 ? -9.241  -68.689 -64.876 1.00 82.83  ?  556 GLU   I CD   1 
ATOM   8708 O  OE1  . GLU   B 1 554 ? -9.453  -69.480 -63.923 1.00 86.49  ?  556 GLU   I OE1  1 
ATOM   8709 O  OE2  . GLU   B 1 554 ? -8.218  -68.775 -65.600 1.00 81.85  ?  556 GLU   I OE2  1 
ATOM   8710 N  N    . LYS   B 1 555 ? -13.371 -69.083 -67.366 1.00 68.84  ?  557 LYS   I N    1 
ATOM   8711 C  CA   . LYS   B 1 555 ? -13.516 -69.765 -68.655 1.00 66.90  ?  557 LYS   I CA   1 
ATOM   8712 C  C    . LYS   B 1 555 ? -14.069 -68.812 -69.721 1.00 66.05  ?  557 LYS   I C    1 
ATOM   8713 O  O    . LYS   B 1 555 ? -13.401 -68.571 -70.722 1.00 72.23  ?  557 LYS   I O    1 
ATOM   8714 C  CB   . LYS   B 1 555 ? -14.417 -71.004 -68.524 1.00 65.15  ?  557 LYS   I CB   1 
ATOM   8715 C  CG   . LYS   B 1 555 ? -14.472 -71.883 -69.763 1.00 64.85  ?  557 LYS   I CG   1 
ATOM   8716 N  N    . CYS   B 1 556 ? -15.250 -68.243 -69.491 1.00 62.32  ?  558 CYS   I N    1 
ATOM   8717 C  CA   . CYS   B 1 556 ? -15.912 -67.424 -70.518 1.00 66.51  ?  558 CYS   I CA   1 
ATOM   8718 C  C    . CYS   B 1 556 ? -15.294 -66.049 -70.801 1.00 65.18  ?  558 CYS   I C    1 
ATOM   8719 O  O    . CYS   B 1 556 ? -15.523 -65.494 -71.877 1.00 65.24  ?  558 CYS   I O    1 
ATOM   8720 C  CB   . CYS   B 1 556 ? -17.403 -67.259 -70.218 1.00 69.34  ?  558 CYS   I CB   1 
ATOM   8721 S  SG   . CYS   B 1 556 ? -18.316 -68.812 -70.159 1.00 75.13  ?  558 CYS   I SG   1 
ATOM   8722 N  N    . CYS   B 1 557 ? -14.543 -65.490 -69.855 1.00 66.35  ?  559 CYS   I N    1 
ATOM   8723 C  CA   . CYS   B 1 557 ? -13.835 -64.220 -70.090 1.00 67.20  ?  559 CYS   I CA   1 
ATOM   8724 C  C    . CYS   B 1 557 ? -12.519 -64.424 -70.856 1.00 68.97  ?  559 CYS   I C    1 
ATOM   8725 O  O    . CYS   B 1 557 ? -12.022 -63.491 -71.498 1.00 67.53  ?  559 CYS   I O    1 
ATOM   8726 C  CB   . CYS   B 1 557 ? -13.529 -63.512 -68.765 1.00 65.77  ?  559 CYS   I CB   1 
ATOM   8727 S  SG   . CYS   B 1 557 ? -14.949 -63.084 -67.729 1.00 61.01  ?  559 CYS   I SG   1 
ATOM   8728 N  N    . LYS   B 1 558 ? -11.956 -65.629 -70.741 1.00 70.49  ?  560 LYS   I N    1 
ATOM   8729 C  CA   . LYS   B 1 558 ? -10.670 -65.995 -71.337 1.00 73.70  ?  560 LYS   I CA   1 
ATOM   8730 C  C    . LYS   B 1 558 ? -10.855 -66.648 -72.704 1.00 75.73  ?  560 LYS   I C    1 
ATOM   8731 O  O    . LYS   B 1 558 ? -9.918  -66.659 -73.503 1.00 75.02  ?  560 LYS   I O    1 
ATOM   8732 C  CB   . LYS   B 1 558 ? -9.922  -66.960 -70.394 1.00 72.30  ?  560 LYS   I CB   1 
ATOM   8733 C  CG   . LYS   B 1 558 ? -8.476  -67.254 -70.758 1.00 71.69  ?  560 LYS   I CG   1 
ATOM   8734 N  N    . ALA   B 1 559 ? -12.053 -67.181 -72.967 1.00 80.49  ?  561 ALA   I N    1 
ATOM   8735 C  CA   . ALA   B 1 559 ? -12.327 -67.973 -74.173 1.00 83.08  ?  561 ALA   I CA   1 
ATOM   8736 C  C    . ALA   B 1 559 ? -12.506 -67.089 -75.406 1.00 85.85  ?  561 ALA   I C    1 
ATOM   8737 O  O    . ALA   B 1 559 ? -12.849 -65.906 -75.293 1.00 91.13  ?  561 ALA   I O    1 
ATOM   8738 C  CB   . ALA   B 1 559 ? -13.561 -68.855 -73.973 1.00 79.82  ?  561 ALA   I CB   1 
ATOM   8739 N  N    . ASP   B 1 560 ? -12.249 -67.675 -76.577 1.00 82.06  ?  562 ASP   I N    1 
ATOM   8740 C  CA   . ASP   B 1 560 ? -12.582 -67.052 -77.863 1.00 79.79  ?  562 ASP   I CA   1 
ATOM   8741 C  C    . ASP   B 1 560 ? -14.093 -66.993 -77.963 1.00 73.92  ?  562 ASP   I C    1 
ATOM   8742 O  O    . ASP   B 1 560 ? -14.765 -68.016 -77.780 1.00 68.43  ?  562 ASP   I O    1 
ATOM   8743 C  CB   . ASP   B 1 560 ? -12.024 -67.853 -79.049 1.00 77.97  ?  562 ASP   I CB   1 
ATOM   8744 C  CG   . ASP   B 1 560 ? -10.531 -67.716 -79.190 1.00 75.24  ?  562 ASP   I CG   1 
ATOM   8745 O  OD1  . ASP   B 1 560 ? -10.065 -66.591 -79.483 1.00 72.69  ?  562 ASP   I OD1  1 
ATOM   8746 O  OD2  . ASP   B 1 560 ? -9.828  -68.734 -79.018 1.00 69.78  ?  562 ASP   I OD2  1 
ATOM   8747 N  N    . ASP   B 1 561 ? -14.609 -65.796 -78.246 1.00 69.82  ?  563 ASP   I N    1 
ATOM   8748 C  CA   . ASP   B 1 561 ? -16.038 -65.503 -78.198 1.00 70.06  ?  563 ASP   I CA   1 
ATOM   8749 C  C    . ASP   B 1 561 ? -16.560 -65.562 -76.727 1.00 73.37  ?  563 ASP   I C    1 
ATOM   8750 O  O    . ASP   B 1 561 ? -16.404 -66.570 -76.027 1.00 76.91  ?  563 ASP   I O    1 
ATOM   8751 C  CB   . ASP   B 1 561 ? -16.804 -66.397 -79.195 1.00 67.09  ?  563 ASP   I CB   1 
ATOM   8752 C  CG   . ASP   B 1 561 ? -18.225 -66.604 -78.819 1.00 66.78  ?  563 ASP   I CG   1 
ATOM   8753 O  OD1  . ASP   B 1 561 ? -18.944 -65.598 -78.741 1.00 64.49  ?  563 ASP   I OD1  1 
ATOM   8754 O  OD2  . ASP   B 1 561 ? -18.625 -67.776 -78.617 1.00 72.05  ?  563 ASP   I OD2  1 
ATOM   8755 N  N    . LYS   B 1 562 ? -17.154 -64.452 -76.278 1.00 72.20  ?  564 LYS   I N    1 
ATOM   8756 C  CA   . LYS   B 1 562 ? -17.607 -64.271 -74.899 1.00 68.24  ?  564 LYS   I CA   1 
ATOM   8757 C  C    . LYS   B 1 562 ? -19.085 -64.628 -74.727 1.00 66.80  ?  564 LYS   I C    1 
ATOM   8758 O  O    . LYS   B 1 562 ? -19.407 -65.565 -74.003 1.00 68.78  ?  564 LYS   I O    1 
ATOM   8759 C  CB   . LYS   B 1 562 ? -17.369 -62.827 -74.444 1.00 64.58  ?  564 LYS   I CB   1 
ATOM   8760 N  N    . GLU   B 1 563 ? -19.974 -63.906 -75.408 1.00 66.22  ?  565 GLU   I N    1 
ATOM   8761 C  CA   . GLU   B 1 563 ? -21.413 -63.959 -75.094 1.00 67.02  ?  565 GLU   I CA   1 
ATOM   8762 C  C    . GLU   B 1 563 ? -22.101 -65.309 -75.288 1.00 68.95  ?  565 GLU   I C    1 
ATOM   8763 O  O    . GLU   B 1 563 ? -23.048 -65.634 -74.545 1.00 67.44  ?  565 GLU   I O    1 
ATOM   8764 C  CB   . GLU   B 1 563 ? -22.197 -62.890 -75.862 1.00 67.12  ?  565 GLU   I CB   1 
ATOM   8765 C  CG   . GLU   B 1 563 ? -23.626 -62.686 -75.352 1.00 67.44  ?  565 GLU   I CG   1 
ATOM   8766 C  CD   . GLU   B 1 563 ? -23.700 -62.512 -73.833 1.00 67.94  ?  565 GLU   I CD   1 
ATOM   8767 O  OE1  . GLU   B 1 563 ? -22.940 -61.684 -73.291 1.00 63.15  ?  565 GLU   I OE1  1 
ATOM   8768 O  OE2  . GLU   B 1 563 ? -24.508 -63.203 -73.177 1.00 65.74  ?  565 GLU   I OE2  1 
ATOM   8769 N  N    . THR   B 1 564 ? -21.645 -66.078 -76.277 1.00 64.22  ?  566 THR   I N    1 
ATOM   8770 C  CA   . THR   B 1 564 ? -22.146 -67.436 -76.486 1.00 63.74  ?  566 THR   I CA   1 
ATOM   8771 C  C    . THR   B 1 564 ? -21.809 -68.329 -75.287 1.00 62.45  ?  566 THR   I C    1 
ATOM   8772 O  O    . THR   B 1 564 ? -22.680 -69.042 -74.799 1.00 61.15  ?  566 THR   I O    1 
ATOM   8773 C  CB   . THR   B 1 564 ? -21.585 -68.067 -77.776 1.00 63.25  ?  566 THR   I CB   1 
ATOM   8774 N  N    . CYS   B 1 565 ? -20.559 -68.260 -74.810 1.00 63.44  ?  567 CYS   I N    1 
ATOM   8775 C  CA   . CYS   B 1 565 ? -20.116 -68.997 -73.615 1.00 64.53  ?  567 CYS   I CA   1 
ATOM   8776 C  C    . CYS   B 1 565 ? -21.005 -68.718 -72.412 1.00 66.58  ?  567 CYS   I C    1 
ATOM   8777 O  O    . CYS   B 1 565 ? -21.505 -69.643 -71.781 1.00 70.54  ?  567 CYS   I O    1 
ATOM   8778 C  CB   . CYS   B 1 565 ? -18.682 -68.628 -73.240 1.00 67.16  ?  567 CYS   I CB   1 
ATOM   8779 S  SG   . CYS   B 1 565 ? -17.980 -69.705 -71.970 1.00 74.74  ?  567 CYS   I SG   1 
ATOM   8780 N  N    . PHE   B 1 566 ? -21.191 -67.436 -72.107 1.00 67.39  ?  568 PHE   I N    1 
ATOM   8781 C  CA   . PHE   B 1 566 ? -22.057 -67.000 -71.008 1.00 68.24  ?  568 PHE   I CA   1 
ATOM   8782 C  C    . PHE   B 1 566 ? -23.478 -67.555 -71.106 1.00 67.67  ?  568 PHE   I C    1 
ATOM   8783 O  O    . PHE   B 1 566 ? -24.091 -67.848 -70.084 1.00 68.81  ?  568 PHE   I O    1 
ATOM   8784 C  CB   . PHE   B 1 566 ? -22.104 -65.463 -70.920 1.00 72.12  ?  568 PHE   I CB   1 
ATOM   8785 C  CG   . PHE   B 1 566 ? -21.000 -64.877 -70.102 1.00 75.15  ?  568 PHE   I CG   1 
ATOM   8786 C  CD1  . PHE   B 1 566 ? -19.717 -64.746 -70.622 1.00 77.06  ?  568 PHE   I CD1  1 
ATOM   8787 C  CD2  . PHE   B 1 566 ? -21.233 -64.475 -68.798 1.00 75.90  ?  568 PHE   I CD2  1 
ATOM   8788 C  CE1  . PHE   B 1 566 ? -18.689 -64.211 -69.859 1.00 73.45  ?  568 PHE   I CE1  1 
ATOM   8789 C  CE2  . PHE   B 1 566 ? -20.214 -63.946 -68.031 1.00 75.49  ?  568 PHE   I CE2  1 
ATOM   8790 C  CZ   . PHE   B 1 566 ? -18.942 -63.810 -68.563 1.00 75.07  ?  568 PHE   I CZ   1 
ATOM   8791 N  N    . ALA   B 1 567 ? -24.009 -67.678 -72.320 1.00 65.70  ?  569 ALA   I N    1 
ATOM   8792 C  CA   . ALA   B 1 567 ? -25.331 -68.286 -72.517 1.00 67.99  ?  569 ALA   I CA   1 
ATOM   8793 C  C    . ALA   B 1 567 ? -25.306 -69.821 -72.386 1.00 67.06  ?  569 ALA   I C    1 
ATOM   8794 O  O    . ALA   B 1 567 ? -26.163 -70.397 -71.718 1.00 71.63  ?  569 ALA   I O    1 
ATOM   8795 C  CB   . ALA   B 1 567 ? -25.910 -67.876 -73.863 1.00 69.99  ?  569 ALA   I CB   1 
ATOM   8796 N  N    . GLU   B 1 568 ? -24.323 -70.474 -73.012 1.00 61.90  ?  570 GLU   I N    1 
ATOM   8797 C  CA   . GLU   B 1 568 ? -24.277 -71.944 -73.077 1.00 58.84  ?  570 GLU   I CA   1 
ATOM   8798 C  C    . GLU   B 1 568 ? -23.829 -72.555 -71.761 1.00 55.58  ?  570 GLU   I C    1 
ATOM   8799 O  O    . GLU   B 1 568 ? -24.456 -73.473 -71.255 1.00 49.31  ?  570 GLU   I O    1 
ATOM   8800 C  CB   . GLU   B 1 568 ? -23.341 -72.427 -74.198 1.00 56.94  ?  570 GLU   I CB   1 
ATOM   8801 N  N    . GLU   B 1 569 ? -22.728 -72.040 -71.228 1.00 56.86  ?  571 GLU   I N    1 
ATOM   8802 C  CA   . GLU   B 1 569 ? -22.194 -72.510 -69.959 1.00 59.78  ?  571 GLU   I CA   1 
ATOM   8803 C  C    . GLU   B 1 569 ? -23.096 -72.051 -68.799 1.00 60.23  ?  571 GLU   I C    1 
ATOM   8804 O  O    . GLU   B 1 569 ? -23.207 -72.745 -67.785 1.00 56.76  ?  571 GLU   I O    1 
ATOM   8805 C  CB   . GLU   B 1 569 ? -20.777 -71.995 -69.745 1.00 62.21  ?  571 GLU   I CB   1 
ATOM   8806 C  CG   . GLU   B 1 569 ? -19.794 -72.318 -70.849 1.00 62.92  ?  571 GLU   I CG   1 
ATOM   8807 C  CD   . GLU   B 1 569 ? -19.108 -73.645 -70.660 1.00 64.62  ?  571 GLU   I CD   1 
ATOM   8808 O  OE1  . GLU   B 1 569 ? -19.811 -74.656 -70.437 1.00 64.90  ?  571 GLU   I OE1  1 
ATOM   8809 O  OE2  . GLU   B 1 569 ? -17.861 -73.657 -70.741 1.00 66.54  ?  571 GLU   I OE2  1 
ATOM   8810 N  N    . GLY   B 1 570 ? -23.746 -70.896 -68.965 1.00 57.28  ?  572 GLY   I N    1 
ATOM   8811 C  CA   . GLY   B 1 570 ? -24.693 -70.393 -67.987 1.00 54.50  ?  572 GLY   I CA   1 
ATOM   8812 C  C    . GLY   B 1 570 ? -25.811 -71.377 -67.778 1.00 52.22  ?  572 GLY   I C    1 
ATOM   8813 O  O    . GLY   B 1 570 ? -26.035 -71.829 -66.657 1.00 53.72  ?  572 GLY   I O    1 
ATOM   8814 N  N    . LYS   B 1 571 ? -26.504 -71.717 -68.865 1.00 51.83  ?  573 LYS   I N    1 
ATOM   8815 C  CA   . LYS   B 1 571 ? -27.598 -72.715 -68.828 1.00 48.62  ?  573 LYS   I CA   1 
ATOM   8816 C  C    . LYS   B 1 571 ? -27.176 -73.948 -68.043 1.00 45.96  ?  573 LYS   I C    1 
ATOM   8817 O  O    . LYS   B 1 571 ? -27.927 -74.404 -67.194 1.00 42.45  ?  573 LYS   I O    1 
ATOM   8818 C  CB   . LYS   B 1 571 ? -28.059 -73.132 -70.242 1.00 45.85  ?  573 LYS   I CB   1 
ATOM   8819 C  CG   . LYS   B 1 571 ? -29.160 -72.273 -70.835 1.00 45.75  ?  573 LYS   I CG   1 
ATOM   8820 N  N    . LYS   B 1 572 ? -25.966 -74.446 -68.329 1.00 50.46  ?  574 LYS   I N    1 
ATOM   8821 C  CA   . LYS   B 1 572 ? -25.387 -75.624 -67.676 1.00 51.45  ?  574 LYS   I CA   1 
ATOM   8822 C  C    . LYS   B 1 572 ? -25.190 -75.416 -66.186 1.00 52.67  ?  574 LYS   I C    1 
ATOM   8823 O  O    . LYS   B 1 572 ? -25.627 -76.241 -65.392 1.00 54.76  ?  574 LYS   I O    1 
ATOM   8824 C  CB   . LYS   B 1 572 ? -24.014 -75.963 -68.251 1.00 51.59  ?  574 LYS   I CB   1 
ATOM   8825 C  CG   . LYS   B 1 572 ? -23.998 -76.581 -69.629 1.00 55.01  ?  574 LYS   I CG   1 
ATOM   8826 C  CD   . LYS   B 1 572 ? -22.574 -76.986 -70.027 1.00 51.27  ?  574 LYS   I CD   1 
ATOM   8827 C  CE   . LYS   B 1 572 ? -22.154 -78.271 -69.329 1.00 48.17  ?  574 LYS   I CE   1 
ATOM   8828 N  NZ   . LYS   B 1 572 ? -20.830 -78.750 -69.773 1.00 47.88  ?  574 LYS   I NZ   1 
ATOM   8829 N  N    . LEU   B 1 573 ? -24.494 -74.335 -65.822 1.00 51.88  ?  575 LEU   I N    1 
ATOM   8830 C  CA   . LEU   B 1 573 ? -24.227 -73.982 -64.404 1.00 46.91  ?  575 LEU   I CA   1 
ATOM   8831 C  C    . LEU   B 1 573 ? -25.494 -73.857 -63.545 1.00 44.02  ?  575 LEU   I C    1 
ATOM   8832 O  O    . LEU   B 1 573 ? -25.584 -74.432 -62.454 1.00 44.46  ?  575 LEU   I O    1 
ATOM   8833 C  CB   . LEU   B 1 573 ? -23.447 -72.677 -64.321 1.00 44.37  ?  575 LEU   I CB   1 
ATOM   8834 C  CG   . LEU   B 1 573 ? -23.092 -72.204 -62.912 1.00 44.07  ?  575 LEU   I CG   1 
ATOM   8835 C  CD1  . LEU   B 1 573 ? -22.219 -73.221 -62.194 1.00 41.36  ?  575 LEU   I CD1  1 
ATOM   8836 C  CD2  . LEU   B 1 573 ? -22.409 -70.854 -62.991 1.00 45.82  ?  575 LEU   I CD2  1 
ATOM   8837 N  N    . VAL   B 1 574 ? -26.465 -73.112 -64.050 1.00 43.48  ?  576 VAL   I N    1 
ATOM   8838 C  CA   . VAL   B 1 574 ? -27.747 -72.929 -63.364 1.00 43.57  ?  576 VAL   I CA   1 
ATOM   8839 C  C    . VAL   B 1 574 ? -28.417 -74.286 -63.141 1.00 43.67  ?  576 VAL   I C    1 
ATOM   8840 O  O    . VAL   B 1 574 ? -28.812 -74.622 -62.027 1.00 40.77  ?  576 VAL   I O    1 
ATOM   8841 C  CB   . VAL   B 1 574 ? -28.673 -71.996 -64.174 1.00 43.94  ?  576 VAL   I CB   1 
ATOM   8842 C  CG1  . VAL   B 1 574 ? -30.104 -72.016 -63.643 1.00 45.91  ?  576 VAL   I CG1  1 
ATOM   8843 C  CG2  . VAL   B 1 574 ? -28.100 -70.581 -64.178 1.00 41.50  ?  576 VAL   I CG2  1 
ATOM   8844 N  N    . ALA   B 1 575 ? -28.527 -75.066 -64.210 1.00 42.53  ?  577 ALA   I N    1 
ATOM   8845 C  CA   . ALA   B 1 575 ? -29.137 -76.390 -64.124 1.00 41.45  ?  577 ALA   I CA   1 
ATOM   8846 C  C    . ALA   B 1 575 ? -28.436 -77.275 -63.095 1.00 39.42  ?  577 ALA   I C    1 
ATOM   8847 O  O    . ALA   B 1 575 ? -29.112 -77.896 -62.291 1.00 37.87  ?  577 ALA   I O    1 
ATOM   8848 C  CB   . ALA   B 1 575 ? -29.135 -77.069 -65.483 1.00 42.34  ?  577 ALA   I CB   1 
ATOM   8849 N  N    . ALA   B 1 576 ? -27.093 -77.303 -63.120 1.00 36.55  ?  578 ALA   I N    1 
ATOM   8850 C  CA   . ALA   B 1 576 ? -26.297 -78.186 -62.252 1.00 37.66  ?  578 ALA   I CA   1 
ATOM   8851 C  C    . ALA   B 1 576 ? -26.306 -77.751 -60.786 1.00 39.17  ?  578 ALA   I C    1 
ATOM   8852 O  O    . ALA   B 1 576 ? -26.175 -78.590 -59.871 1.00 38.97  ?  578 ALA   I O    1 
ATOM   8853 C  CB   . ALA   B 1 576 ? -24.854 -78.305 -62.756 1.00 38.85  ?  578 ALA   I CB   1 
ATOM   8854 N  N    . SER   B 1 577 ? -26.440 -76.448 -60.569 1.00 38.72  ?  579 SER   I N    1 
ATOM   8855 C  CA   . SER   B 1 577 ? -26.562 -75.912 -59.227 1.00 40.87  ?  579 SER   I CA   1 
ATOM   8856 C  C    . SER   B 1 577 ? -27.936 -76.258 -58.640 1.00 42.64  ?  579 SER   I C    1 
ATOM   8857 O  O    . SER   B 1 577 ? -27.992 -76.726 -57.512 1.00 37.57  ?  579 SER   I O    1 
ATOM   8858 C  CB   . SER   B 1 577 ? -26.271 -74.415 -59.198 1.00 39.49  ?  579 SER   I CB   1 
ATOM   8859 O  OG   . SER   B 1 577 ? -24.886 -74.181 -59.447 1.00 41.11  ?  579 SER   I OG   1 
ATOM   8860 N  N    . GLN   B 1 578 ? -29.022 -76.084 -59.396 1.00 45.97  ?  580 GLN   I N    1 
ATOM   8861 C  CA   . GLN   B 1 578 ? -30.369 -76.398 -58.868 1.00 47.90  ?  580 GLN   I CA   1 
ATOM   8862 C  C    . GLN   B 1 578 ? -30.476 -77.827 -58.303 1.00 48.13  ?  580 GLN   I C    1 
ATOM   8863 O  O    . GLN   B 1 578 ? -30.993 -78.031 -57.211 1.00 53.94  ?  580 GLN   I O    1 
ATOM   8864 C  CB   . GLN   B 1 578 ? -31.466 -76.180 -59.928 1.00 49.95  ?  580 GLN   I CB   1 
ATOM   8865 C  CG   . GLN   B 1 578 ? -31.998 -74.749 -60.013 1.00 50.32  ?  580 GLN   I CG   1 
ATOM   8866 C  CD   . GLN   B 1 578 ? -32.607 -74.428 -61.367 1.00 49.78  ?  580 GLN   I CD   1 
ATOM   8867 O  OE1  . GLN   B 1 578 ? -31.994 -74.694 -62.403 1.00 53.24  ?  580 GLN   I OE1  1 
ATOM   8868 N  NE2  . GLN   B 1 578 ? -33.806 -73.849 -61.370 1.00 45.43  ?  580 GLN   I NE2  1 
ATOM   8869 N  N    . ALA   B 1 579 ? -29.967 -78.800 -59.045 1.00 48.19  ?  581 ALA   I N    1 
ATOM   8870 C  CA   . ALA   B 1 579 ? -30.088 -80.208 -58.666 1.00 45.41  ?  581 ALA   I CA   1 
ATOM   8871 C  C    . ALA   B 1 579 ? -29.161 -80.572 -57.506 1.00 45.42  ?  581 ALA   I C    1 
ATOM   8872 O  O    . ALA   B 1 579 ? -29.585 -81.265 -56.598 1.00 43.83  ?  581 ALA   I O    1 
ATOM   8873 C  CB   . ALA   B 1 579 ? -29.818 -81.101 -59.855 1.00 42.79  ?  581 ALA   I CB   1 
ATOM   8874 N  N    . ALA   B 1 580 ? -27.910 -80.104 -57.542 1.00 45.59  ?  582 ALA   I N    1 
ATOM   8875 C  CA   . ALA   B 1 580 ? -26.950 -80.319 -56.442 1.00 48.02  ?  582 ALA   I CA   1 
ATOM   8876 C  C    . ALA   B 1 580 ? -27.559 -79.942 -55.091 1.00 51.69  ?  582 ALA   I C    1 
ATOM   8877 O  O    . ALA   B 1 580 ? -27.508 -80.731 -54.138 1.00 52.94  ?  582 ALA   I O    1 
ATOM   8878 C  CB   . ALA   B 1 580 ? -25.660 -79.535 -56.675 1.00 44.62  ?  582 ALA   I CB   1 
ATOM   8879 N  N    . LEU   B 1 581 ? -28.154 -78.747 -55.041 1.00 54.68  ?  583 LEU   I N    1 
ATOM   8880 C  CA   . LEU   B 1 581 ? -28.934 -78.276 -53.883 1.00 56.89  ?  583 LEU   I CA   1 
ATOM   8881 C  C    . LEU   B 1 581 ? -30.290 -78.992 -53.800 1.00 57.53  ?  583 LEU   I C    1 
ATOM   8882 O  O    . LEU   B 1 581 ? -31.324 -78.380 -53.499 1.00 60.56  ?  583 LEU   I O    1 
ATOM   8883 C  CB   . LEU   B 1 581 ? -29.150 -76.756 -53.958 1.00 56.77  ?  583 LEU   I CB   1 
ATOM   8884 C  CG   . LEU   B 1 581 ? -27.961 -75.810 -54.175 1.00 56.64  ?  583 LEU   I CG   1 
ATOM   8885 C  CD1  . LEU   B 1 581 ? -28.425 -74.363 -54.100 1.00 56.70  ?  583 LEU   I CD1  1 
ATOM   8886 C  CD2  . LEU   B 1 581 ? -26.839 -76.065 -53.186 1.00 55.77  ?  583 LEU   I CD2  1 
HETATM 8887 CU CU01 . A1D6U C 2 .   ? -1.538  -5.901  11.262  1.00 100.46 ?  601 A1D6U A CU01 1 
HETATM 8888 S  S003 . A1D6U C 2 .   ? -3.065  -5.420  12.492  1.00 105.26 ?  601 A1D6U A S003 1 
HETATM 8889 N  N007 . A1D6U C 2 .   ? -0.434  -5.580  12.798  1.00 93.11  ?  601 A1D6U A N007 1 
HETATM 8890 N  N008 . A1D6U C 2 .   ? 0.332   -6.266  10.502  1.00 85.66  ?  601 A1D6U A N008 1 
HETATM 8891 N  N00C . A1D6U C 2 .   ? -0.901  -5.215  13.980  1.00 94.82  ?  601 A1D6U A N00C 1 
HETATM 8892 N  N00E . A1D6U C 2 .   ? -2.989  -4.663  15.311  1.00 95.37  ?  601 A1D6U A N00E 1 
HETATM 8893 C  C00F . A1D6U C 2 .   ? 0.846   -5.746  12.631  1.00 84.51  ?  601 A1D6U A C00F 1 
HETATM 8894 C  C00G . A1D6U C 2 .   ? 1.312   -6.105  11.416  1.00 82.85  ?  601 A1D6U A C00G 1 
HETATM 8895 C  C00J . A1D6U C 2 .   ? -2.268  -5.067  14.087  1.00 97.52  ?  601 A1D6U A C00J 1 
HETATM 8896 C  C00L . A1D6U C 2 .   ? 0.600   -6.642  9.218   1.00 76.38  ?  601 A1D6U A C00L 1 
HETATM 8897 C  C00O . A1D6U C 2 .   ? 1.793   -5.478  13.872  1.00 78.49  ?  601 A1D6U A C00O 1 
HETATM 8898 C  C00Q . A1D6U C 2 .   ? 1.907   -6.876  8.800   1.00 74.52  ?  601 A1D6U A C00Q 1 
HETATM 8899 C  C00T . A1D6U C 2 .   ? 2.641   -6.340  11.001  1.00 77.91  ?  601 A1D6U A C00T 1 
HETATM 8900 C  C00U . A1D6U C 2 .   ? -4.405  -5.012  15.518  1.00 93.12  ?  601 A1D6U A C00U 1 
HETATM 8901 C  C00V . A1D6U C 2 .   ? 2.921   -6.725  9.708   1.00 76.68  ?  601 A1D6U A C00V 1 
HETATM 8902 C  C00Y . A1D6U C 2 .   ? 2.562   -4.162  13.636  1.00 76.15  ?  601 A1D6U A C00Y 1 
HETATM 8903 C  C00Z . A1D6U C 2 .   ? -2.289  -3.883  16.341  1.00 92.25  ?  601 A1D6U A C00Z 1 
HETATM 8904 C  C012 . A1D6U C 2 .   ? 2.779   -6.616  14.239  1.00 78.95  ?  601 A1D6U A C012 1 
HETATM 8905 C  C    . IMN   D 3 .   ? 4.135   -9.885  -9.165  1.00 69.98  ?  602 IMN   A C    1 
HETATM 8906 C  C1   . IMN   D 3 .   ? 5.197   -9.232  -9.743  1.00 70.57  ?  602 IMN   A C1   1 
HETATM 8907 C  C2   . IMN   D 3 .   ? 6.277   -10.005 -10.210 1.00 66.95  ?  602 IMN   A C2   1 
HETATM 8908 C  C3   . IMN   D 3 .   ? 6.247   -11.388 -10.080 1.00 68.71  ?  602 IMN   A C3   1 
HETATM 8909 C  C4   . IMN   D 3 .   ? 5.170   -12.035 -9.499  1.00 67.74  ?  602 IMN   A C4   1 
HETATM 8910 C  C5   . IMN   D 3 .   ? 4.122   -11.290 -9.046  1.00 66.74  ?  602 IMN   A C5   1 
HETATM 8911 C  C6   . IMN   D 3 .   ? 8.542   -11.682 -10.472 1.00 68.86  ?  602 IMN   A C6   1 
HETATM 8912 C  C7   . IMN   D 3 .   ? 4.891   -7.832  -9.700  1.00 73.73  ?  602 IMN   A C7   1 
HETATM 8913 C  C8   . IMN   D 3 .   ? 3.645   -7.732  -9.092  1.00 76.33  ?  602 IMN   A C8   1 
HETATM 8914 C  C9   . IMN   D 3 .   ? 1.952   -9.447  -8.101  1.00 90.26  ?  602 IMN   A C9   1 
HETATM 8915 C  C10  . IMN   D 3 .   ? 0.928   -8.388  -7.740  1.00 100.17 ?  602 IMN   A C10  1 
HETATM 8916 C  C11  . IMN   D 3 .   ? 0.630   -7.892  -6.470  1.00 106.97 ?  602 IMN   A C11  1 
HETATM 8917 C  C12  . IMN   D 3 .   ? -0.329  -6.895  -6.397  1.00 114.05 ?  602 IMN   A C12  1 
HETATM 8918 C  C13  . IMN   D 3 .   ? -0.917  -6.445  -7.599  1.00 115.62 ?  602 IMN   A C13  1 
HETATM 8919 C  C14  . IMN   D 3 .   ? -0.583  -6.956  -8.816  1.00 108.35 ?  602 IMN   A C14  1 
HETATM 8920 C  C15  . IMN   D 3 .   ? 0.330   -7.942  -8.905  1.00 101.01 ?  602 IMN   A C15  1 
HETATM 8921 C  C16  . IMN   D 3 .   ? 3.018   -6.331  -8.893  1.00 74.63  ?  602 IMN   A C16  1 
HETATM 8922 C  C17  . IMN   D 3 .   ? 5.679   -6.547  -10.195 1.00 72.80  ?  602 IMN   A C17  1 
HETATM 8923 C  C18  . IMN   D 3 .   ? 7.057   -6.700  -10.904 1.00 74.21  ?  602 IMN   A C18  1 
HETATM 8924 N  N    . IMN   D 3 .   ? 3.212   -8.996  -8.787  1.00 76.63  ?  602 IMN   A N    1 
HETATM 8925 O  O    . IMN   D 3 .   ? 7.265   -12.224 -10.529 1.00 66.47  ?  602 IMN   A O    1 
HETATM 8926 O  O1   . IMN   D 3 .   ? 1.647   -10.565 -7.897  1.00 94.65  ?  602 IMN   A O1   1 
HETATM 8927 O  O2   . IMN   D 3 .   ? 7.314   -7.728  -11.618 1.00 73.61  -1 602 IMN   A O2   1 
HETATM 8928 O  O3   . IMN   D 3 .   ? 7.908   -5.772  -10.784 1.00 68.47  ?  602 IMN   A O3   1 
HETATM 8929 CL CL   . IMN   D 3 .   ? -2.163  -5.187  -7.753  1.00 129.80 ?  602 IMN   A CL   1 
HETATM 8930 C  C1   . PLM   E 4 .   ? 4.064   -4.160  18.262  1.00 43.81  ?  603 PLM   A C1   1 
HETATM 8931 O  O1   . PLM   E 4 .   ? 5.021   -3.991  19.053  1.00 43.50  ?  603 PLM   A O1   1 
HETATM 8932 O  O2   . PLM   E 4 .   ? 3.640   -3.208  17.539  1.00 43.91  ?  603 PLM   A O2   1 
HETATM 8933 C  C2   . PLM   E 4 .   ? 3.462   -5.562  18.193  1.00 43.34  ?  603 PLM   A C2   1 
HETATM 8934 C  C3   . PLM   E 4 .   ? 4.196   -6.569  19.111  1.00 44.00  ?  603 PLM   A C3   1 
HETATM 8935 C  C4   . PLM   E 4 .   ? 5.717   -6.693  18.849  1.00 40.68  ?  603 PLM   A C4   1 
HETATM 8936 C  C5   . PLM   E 4 .   ? 6.267   -8.110  18.777  1.00 39.66  ?  603 PLM   A C5   1 
HETATM 8937 C  C6   . PLM   E 4 .   ? 5.720   -8.992  17.638  1.00 40.55  ?  603 PLM   A C6   1 
HETATM 8938 C  C7   . PLM   E 4 .   ? 6.674   -9.246  16.473  1.00 38.25  ?  603 PLM   A C7   1 
HETATM 8939 C  C8   . PLM   E 4 .   ? 6.548   -10.618 15.805  1.00 37.02  ?  603 PLM   A C8   1 
HETATM 8940 C  C9   . PLM   E 4 .   ? 5.551   -10.595 14.637  1.00 38.31  ?  603 PLM   A C9   1 
HETATM 8941 C  CA   . PLM   E 4 .   ? 5.733   -11.708 13.596  1.00 38.47  ?  603 PLM   A CA   1 
HETATM 8942 C  CB   . PLM   E 4 .   ? 5.335   -11.253 12.175  1.00 35.91  ?  603 PLM   A CB   1 
HETATM 8943 C  C1   . PLM   F 4 .   ? 5.902   -16.793 -4.603  1.00 41.74  ?  604 PLM   A C1   1 
HETATM 8944 O  O1   . PLM   F 4 .   ? 5.179   -15.926 -3.997  1.00 34.83  ?  604 PLM   A O1   1 
HETATM 8945 O  O2   . PLM   F 4 .   ? 6.887   -16.500 -5.347  1.00 37.94  ?  604 PLM   A O2   1 
HETATM 8946 C  C2   . PLM   F 4 .   ? 5.575   -18.267 -4.433  1.00 40.32  ?  604 PLM   A C2   1 
HETATM 8947 C  C3   . PLM   F 4 .   ? 6.322   -18.840 -3.240  1.00 45.62  ?  604 PLM   A C3   1 
HETATM 8948 C  C4   . PLM   F 4 .   ? 5.713   -20.141 -2.697  1.00 44.45  ?  604 PLM   A C4   1 
HETATM 8949 C  C5   . PLM   F 4 .   ? 4.990   -19.887 -1.365  1.00 44.16  ?  604 PLM   A C5   1 
HETATM 8950 C  C6   . PLM   F 4 .   ? 4.569   -21.195 -0.697  1.00 43.94  ?  604 PLM   A C6   1 
HETATM 8951 C  C7   . PLM   F 4 .   ? 3.210   -21.127 -0.003  1.00 42.48  ?  604 PLM   A C7   1 
HETATM 8952 C  C8   . PLM   F 4 .   ? 2.544   -22.507 -0.034  1.00 44.96  ?  604 PLM   A C8   1 
HETATM 8953 C  C9   . PLM   F 4 .   ? 2.425   -23.195 1.324   1.00 46.92  ?  604 PLM   A C9   1 
HETATM 8954 C  CA   . PLM   F 4 .   ? 1.021   -23.065 1.946   1.00 46.25  ?  604 PLM   A CA   1 
HETATM 8955 C  CB   . PLM   F 4 .   ? 0.749   -24.008 3.107   1.00 40.99  ?  604 PLM   A CB   1 
HETATM 8956 C  CC   . PLM   F 4 .   ? 0.569   -25.466 2.685   1.00 40.67  ?  604 PLM   A CC   1 
HETATM 8957 C  CD   . PLM   F 4 .   ? -0.436  -26.169 3.597   1.00 38.83  ?  604 PLM   A CD   1 
HETATM 8958 C  CE   . PLM   F 4 .   ? -0.218  -27.677 3.768   1.00 36.90  ?  604 PLM   A CE   1 
HETATM 8959 C  CF   . PLM   F 4 .   ? -1.569  -28.373 3.995   1.00 37.58  ?  604 PLM   A CF   1 
HETATM 8960 C  CG   . PLM   F 4 .   ? -1.467  -29.747 4.637   1.00 38.30  ?  604 PLM   A CG   1 
HETATM 8961 C  C1   . PLM   G 4 .   ? -0.328  12.356  -8.450  1.00 31.82  ?  605 PLM   A C1   1 
HETATM 8962 O  O1   . PLM   G 4 .   ? -1.585  12.457  -8.392  1.00 25.82  ?  605 PLM   A O1   1 
HETATM 8963 O  O2   . PLM   G 4 .   ? 0.335   12.694  -9.435  1.00 34.42  ?  605 PLM   A O2   1 
HETATM 8964 C  C2   . PLM   G 4 .   ? 0.486   11.827  -7.307  1.00 34.68  ?  605 PLM   A C2   1 
HETATM 8965 C  C3   . PLM   G 4 .   ? 1.460   12.905  -6.806  1.00 38.75  ?  605 PLM   A C3   1 
HETATM 8966 C  C4   . PLM   G 4 .   ? 1.167   13.404  -5.394  1.00 42.44  ?  605 PLM   A C4   1 
HETATM 8967 C  C5   . PLM   G 4 .   ? 1.445   14.908  -5.223  1.00 45.21  ?  605 PLM   A C5   1 
HETATM 8968 C  C6   . PLM   G 4 .   ? 1.843   15.319  -3.794  1.00 49.40  ?  605 PLM   A C6   1 
HETATM 8969 C  C7   . PLM   G 4 .   ? 0.730   16.021  -2.996  1.00 48.90  ?  605 PLM   A C7   1 
HETATM 8970 C  C8   . PLM   G 4 .   ? 0.782   15.694  -1.500  1.00 50.46  ?  605 PLM   A C8   1 
HETATM 8971 C  C9   . PLM   G 4 .   ? 1.060   16.913  -0.615  1.00 49.87  ?  605 PLM   A C9   1 
HETATM 8972 C  CA   . PLM   G 4 .   ? 0.921   16.605  0.877   1.00 47.15  ?  605 PLM   A CA   1 
HETATM 8973 C  CB   . PLM   G 4 .   ? 1.871   15.521  1.384   1.00 45.39  ?  605 PLM   A CB   1 
HETATM 8974 C  CC   . PLM   G 4 .   ? 3.338   15.931  1.259   1.00 45.86  ?  605 PLM   A CC   1 
HETATM 8975 C  CD   . PLM   G 4 .   ? 4.067   15.238  0.116   1.00 45.88  ?  605 PLM   A CD   1 
HETATM 8976 C  CE   . PLM   G 4 .   ? 5.507   15.711  0.032   1.00 46.29  ?  605 PLM   A CE   1 
HETATM 8977 C  CF   . PLM   G 4 .   ? 6.238   14.931  -1.056  1.00 48.66  ?  605 PLM   A CF   1 
HETATM 8978 C  C1   . PLM   H 4 .   ? -3.087  18.282  -1.764  1.00 39.38  ?  606 PLM   A C1   1 
HETATM 8979 O  O1   . PLM   H 4 .   ? -3.070  19.080  -2.725  1.00 36.12  ?  606 PLM   A O1   1 
HETATM 8980 O  O2   . PLM   H 4 .   ? -3.152  18.648  -0.574  1.00 34.85  ?  606 PLM   A O2   1 
HETATM 8981 C  C2   . PLM   H 4 .   ? -2.990  16.785  -2.058  1.00 44.26  ?  606 PLM   A C2   1 
HETATM 8982 C  C3   . PLM   H 4 .   ? -4.289  16.004  -1.832  1.00 42.86  ?  606 PLM   A C3   1 
HETATM 8983 C  C4   . PLM   H 4 .   ? -4.279  15.184  -0.518  1.00 42.66  ?  606 PLM   A C4   1 
HETATM 8984 C  C5   . PLM   H 4 .   ? -5.661  14.974  0.104   1.00 40.15  ?  606 PLM   A C5   1 
HETATM 8985 C  C6   . PLM   H 4 .   ? -6.122  16.326  0.618   1.00 39.17  ?  606 PLM   A C6   1 
HETATM 8986 C  C7   . PLM   H 4 .   ? -7.579  16.464  1.004   1.00 39.08  ?  606 PLM   A C7   1 
HETATM 8987 C  C8   . PLM   H 4 .   ? -7.962  15.499  2.106   1.00 42.34  ?  606 PLM   A C8   1 
HETATM 8988 C  C9   . PLM   H 4 .   ? -7.442  15.976  3.453   1.00 42.37  ?  606 PLM   A C9   1 
HETATM 8989 C  CA   . PLM   H 4 .   ? -7.810  15.049  4.601   1.00 45.33  ?  606 PLM   A CA   1 
HETATM 8990 C  CB   . PLM   H 4 .   ? -9.284  15.177  4.978   1.00 46.47  ?  606 PLM   A CB   1 
HETATM 8991 C  CC   . PLM   H 4 .   ? -9.798  13.961  5.722   1.00 46.67  ?  606 PLM   A CC   1 
HETATM 8992 C  CD   . PLM   H 4 .   ? -10.797 13.190  4.838   1.00 51.64  ?  606 PLM   A CD   1 
HETATM 8993 C  CE   . PLM   H 4 .   ? -11.316 11.892  5.481   1.00 54.85  ?  606 PLM   A CE   1 
HETATM 8994 C  CF   . PLM   H 4 .   ? -12.771 11.500  5.181   1.00 58.10  ?  606 PLM   A CF   1 
HETATM 8995 C  CG   . PLM   H 4 .   ? -13.345 10.728  6.368   1.00 60.97  ?  606 PLM   A CG   1 
HETATM 8996 C  C1   . PLM   I 4 .   ? 3.200   24.194  18.998  1.00 53.56  ?  607 PLM   A C1   1 
HETATM 8997 O  O1   . PLM   I 4 .   ? 4.068   25.116  19.034  1.00 50.81  ?  607 PLM   A O1   1 
HETATM 8998 O  O2   . PLM   I 4 .   ? 3.345   23.125  19.639  1.00 49.63  ?  607 PLM   A O2   1 
HETATM 8999 C  C2   . PLM   I 4 .   ? 1.954   24.425  18.134  1.00 47.06  ?  607 PLM   A C2   1 
HETATM 9000 C  C3   . PLM   I 4 .   ? 0.721   23.543  18.426  1.00 43.73  ?  607 PLM   A C3   1 
HETATM 9001 C  C4   . PLM   I 4 .   ? -0.258  24.088  19.485  1.00 40.32  ?  607 PLM   A C4   1 
HETATM 9002 C  C5   . PLM   I 4 .   ? -1.751  23.766  19.239  1.00 38.63  ?  607 PLM   A C5   1 
HETATM 9003 C  C6   . PLM   I 4 .   ? -2.587  24.850  19.932  1.00 35.82  ?  607 PLM   A C6   1 
HETATM 9004 C  C7   . PLM   I 4 .   ? -4.072  24.592  20.190  1.00 33.90  ?  607 PLM   A C7   1 
HETATM 9005 C  C8   . PLM   I 4 .   ? -4.685  25.945  20.611  1.00 35.40  ?  607 PLM   A C8   1 
HETATM 9006 C  C9   . PLM   I 4 .   ? -5.918  25.896  21.510  1.00 35.00  ?  607 PLM   A C9   1 
HETATM 9007 C  CA   . PLM   I 4 .   ? -6.117  27.229  22.245  1.00 35.58  ?  607 PLM   A CA   1 
HETATM 9008 C  CB   . PLM   I 4 .   ? -7.508  27.417  22.869  1.00 34.71  ?  607 PLM   A CB   1 
HETATM 9009 C  CC   . PLM   I 4 .   ? -8.360  28.590  22.376  1.00 34.77  ?  607 PLM   A CC   1 
HETATM 9010 C  CD   . PLM   I 4 .   ? -9.846  28.221  22.162  1.00 35.75  ?  607 PLM   A CD   1 
HETATM 9011 C  CE   . PLM   I 4 .   ? -10.604 29.383  21.519  1.00 36.65  ?  607 PLM   A CE   1 
HETATM 9012 C  CF   . PLM   I 4 .   ? -12.060 29.068  21.232  1.00 35.95  ?  607 PLM   A CF   1 
HETATM 9013 C  C1   . PLM   J 4 .   ? -9.259  5.110   -17.932 1.00 59.78  ?  608 PLM   A C1   1 
HETATM 9014 O  O1   . PLM   J 4 .   ? -10.380 4.535   -18.011 1.00 60.81  ?  608 PLM   A O1   1 
HETATM 9015 O  O2   . PLM   J 4 .   ? -8.748  5.744   -18.887 1.00 53.76  ?  608 PLM   A O2   1 
HETATM 9016 C  C2   . PLM   J 4 .   ? -8.497  5.049   -16.618 1.00 54.95  ?  608 PLM   A C2   1 
HETATM 9017 C  C3   . PLM   J 4 .   ? -7.193  4.269   -16.776 1.00 51.73  ?  608 PLM   A C3   1 
HETATM 9018 C  C4   . PLM   J 4 .   ? -6.161  5.038   -17.615 1.00 51.20  ?  608 PLM   A C4   1 
HETATM 9019 C  C5   . PLM   J 4 .   ? -5.934  4.397   -18.977 1.00 48.97  ?  608 PLM   A C5   1 
HETATM 9020 C  C6   . PLM   J 4 .   ? -5.360  5.329   -20.042 1.00 46.94  ?  608 PLM   A C6   1 
HETATM 9021 C  C7   . PLM   J 4 .   ? -5.433  4.687   -21.435 1.00 41.84  ?  608 PLM   A C7   1 
HETATM 9022 C  C8   . PLM   J 4 .   ? -4.484  3.506   -21.640 1.00 39.25  ?  608 PLM   A C8   1 
HETATM 9023 C  C9   . PLM   J 4 .   ? -5.279  2.200   -21.598 1.00 38.18  ?  608 PLM   A C9   1 
HETATM 9024 C  CA   . PLM   J 4 .   ? -4.443  0.964   -21.886 1.00 39.04  ?  608 PLM   A CA   1 
HETATM 9025 C  CB   . PLM   J 4 .   ? -5.108  -0.305  -21.315 1.00 39.77  ?  608 PLM   A CB   1 
HETATM 9026 C  CC   . PLM   J 4 .   ? -4.238  -1.579  -21.294 1.00 40.72  ?  608 PLM   A CC   1 
HETATM 9027 C  CD   . PLM   J 4 .   ? -3.555  -1.875  -22.646 1.00 43.34  ?  608 PLM   A CD   1 
HETATM 9028 C  CE   . PLM   J 4 .   ? -2.682  -3.132  -22.658 1.00 43.98  ?  608 PLM   A CE   1 
HETATM 9029 C  CF   . PLM   J 4 .   ? -1.614  -3.022  -23.740 1.00 44.91  ?  608 PLM   A CF   1 
HETATM 9030 C  CG   . PLM   J 4 .   ? -0.736  -4.249  -23.734 1.00 45.50  ?  608 PLM   A CG   1 
HETATM 9031 CU CU01 . A1D6U K 2 .   ? -21.190 -35.845 -48.902 1.00 114.99 ?  601 A1D6U I CU01 1 
HETATM 9032 S  S003 . A1D6U K 2 .   ? -22.729 -36.226 -50.148 1.00 102.11 ?  601 A1D6U I S003 1 
HETATM 9033 N  N007 . A1D6U K 2 .   ? -20.093 -36.212 -50.431 1.00 99.61  ?  601 A1D6U I N007 1 
HETATM 9034 N  N008 . A1D6U K 2 .   ? -19.316 -35.585 -48.114 1.00 88.17  ?  601 A1D6U I N008 1 
HETATM 9035 N  N00C . A1D6U K 2 .   ? -20.557 -36.536 -51.624 1.00 99.19  ?  601 A1D6U I N00C 1 
HETATM 9036 N  N00E . A1D6U K 2 .   ? -22.663 -36.970 -52.971 1.00 101.12 ?  601 A1D6U I N00E 1 
HETATM 9037 C  C00F . A1D6U K 2 .   ? -18.815 -36.113 -50.249 1.00 91.62  ?  601 A1D6U I C00F 1 
HETATM 9038 C  C00G . A1D6U K 2 .   ? -18.337 -35.789 -49.022 1.00 91.01  ?  601 A1D6U I C00G 1 
HETATM 9039 C  C00J . A1D6U K 2 .   ? -21.930 -36.610 -51.741 1.00 104.09 ?  601 A1D6U I C00J 1 
HETATM 9040 C  C00L . A1D6U K 2 .   ? -19.046 -35.237 -46.818 1.00 81.97  ?  601 A1D6U I C00L 1 
HETATM 9041 C  C00O . A1D6U K 2 .   ? -17.912 -36.421 -51.508 1.00 84.45  ?  601 A1D6U I C00O 1 
HETATM 9042 C  C00Q . A1D6U K 2 .   ? -17.738 -35.068 -46.370 1.00 77.24  ?  601 A1D6U I C00Q 1 
HETATM 9043 C  C00T . A1D6U K 2 .   ? -17.001 -35.629 -48.583 1.00 83.32  ?  601 A1D6U I C00T 1 
HETATM 9044 C  C00U . A1D6U K 2 .   ? -23.988 -36.403 -53.254 1.00 99.55  ?  601 A1D6U I C00U 1 
HETATM 9045 C  C00V . A1D6U K 2 .   ? -16.723 -35.265 -47.278 1.00 83.49  ?  601 A1D6U I C00V 1 
HETATM 9046 C  C00Y . A1D6U K 2 .   ? -17.263 -37.808 -51.336 1.00 81.83  ?  601 A1D6U I C00Y 1 
HETATM 9047 C  C00Z . A1D6U K 2 .   ? -22.088 -37.934 -53.926 1.00 102.28 ?  601 A1D6U I C00Z 1 
HETATM 9048 C  C012 . A1D6U K 2 .   ? -16.907 -35.310 -51.916 1.00 84.87  ?  601 A1D6U I C012 1 
HETATM 9049 C  C    . IMN   L 3 .   ? -20.914 -41.345 -29.397 1.00 72.39  ?  602 IMN   I C    1 
HETATM 9050 C  C1   . IMN   L 3 .   ? -22.291 -41.522 -29.301 1.00 72.75  ?  602 IMN   I C1   1 
HETATM 9051 C  C2   . IMN   L 3 .   ? -22.997 -42.515 -30.053 1.00 79.82  ?  602 IMN   I C2   1 
HETATM 9052 C  C3   . IMN   L 3 .   ? -22.320 -43.361 -30.924 1.00 80.86  ?  602 IMN   I C3   1 
HETATM 9053 C  C4   . IMN   L 3 .   ? -20.935 -43.202 -31.039 1.00 80.60  ?  602 IMN   I C4   1 
HETATM 9054 C  C5   . IMN   L 3 .   ? -20.253 -42.229 -30.296 1.00 74.92  ?  602 IMN   I C5   1 
HETATM 9055 C  C6   . IMN   L 3 .   ? -22.955 -45.666 -31.143 1.00 73.55  ?  602 IMN   I C6   1 
HETATM 9056 C  C7   . IMN   L 3 .   ? -22.785 -40.601 -28.356 1.00 68.21  ?  602 IMN   I C7   1 
HETATM 9057 C  C8   . IMN   L 3 .   ? -21.677 -39.893 -27.960 1.00 72.60  ?  602 IMN   I C8   1 
HETATM 9058 C  C9   . IMN   L 3 .   ? -19.179 -39.669 -28.247 1.00 74.66  ?  602 IMN   I C9   1 
HETATM 9059 C  C10  . IMN   L 3 .   ? -17.724 -39.998 -28.760 1.00 78.06  ?  602 IMN   I C10  1 
HETATM 9060 C  C11  . IMN   L 3 .   ? -17.426 -40.647 -29.955 1.00 80.92  ?  602 IMN   I C11  1 
HETATM 9061 C  C12  . IMN   L 3 .   ? -16.131 -40.933 -30.326 1.00 80.92  ?  602 IMN   I C12  1 
HETATM 9062 C  C13  . IMN   L 3 .   ? -15.082 -40.562 -29.493 1.00 82.72  ?  602 IMN   I C13  1 
HETATM 9063 C  C14  . IMN   L 3 .   ? -15.334 -39.910 -28.305 1.00 79.63  ?  602 IMN   I C14  1 
HETATM 9064 C  C15  . IMN   L 3 .   ? -16.641 -39.622 -27.935 1.00 75.94  ?  602 IMN   I C15  1 
HETATM 9065 C  C16  . IMN   L 3 .   ? -21.889 -38.796 -26.951 1.00 74.95  ?  602 IMN   I C16  1 
HETATM 9066 C  C17  . IMN   L 3 .   ? -24.320 -40.454 -27.970 1.00 62.16  ?  602 IMN   I C17  1 
HETATM 9067 C  C18  . IMN   L 3 .   ? -24.970 -40.087 -26.570 1.00 57.90  ?  602 IMN   I C18  1 
HETATM 9068 N  N    . IMN   L 3 .   ? -20.530 -40.326 -28.556 1.00 72.44  ?  602 IMN   I N    1 
HETATM 9069 O  O    . IMN   L 3 .   ? -23.003 -44.347 -31.671 1.00 76.22  ?  602 IMN   I O    1 
HETATM 9070 O  O1   . IMN   L 3 .   ? -19.163 -38.803 -27.440 1.00 74.24  ?  602 IMN   I O1   1 
HETATM 9071 O  O2   . IMN   L 3 .   ? -25.118 -38.883 -26.266 1.00 58.48  ?  602 IMN   I O2   1 
HETATM 9072 O  O3   . IMN   L 3 .   ? -25.456 -40.946 -25.748 1.00 39.92  -1 602 IMN   I O3   1 
HETATM 9073 CL CL   . IMN   L 3 .   ? -13.410 -40.944 -29.984 1.00 91.84  ?  602 IMN   I CL   1 
HETATM 9074 C  C1   . PLM   M 4 .   ? -16.232 -38.538 -54.784 1.00 51.06  ?  603 PLM   I C1   1 
HETATM 9075 O  O1   . PLM   M 4 .   ? -15.109 -38.697 -54.247 1.00 51.71  ?  603 PLM   I O1   1 
HETATM 9076 O  O2   . PLM   M 4 .   ? -17.008 -39.518 -54.923 1.00 49.57  ?  603 PLM   I O2   1 
HETATM 9077 C  C2   . PLM   M 4 .   ? -16.695 -37.158 -55.248 1.00 51.53  ?  603 PLM   I C2   1 
HETATM 9078 C  C3   . PLM   M 4 .   ? -15.705 -36.412 -56.162 1.00 53.90  ?  603 PLM   I C3   1 
HETATM 9079 C  C4   . PLM   M 4 .   ? -14.617 -35.656 -55.388 1.00 53.30  ?  603 PLM   I C4   1 
HETATM 9080 C  C5   . PLM   M 4 .   ? -13.790 -34.689 -56.239 1.00 50.00  ?  603 PLM   I C5   1 
HETATM 9081 C  C6   . PLM   M 4 .   ? -13.832 -33.238 -55.722 1.00 50.32  ?  603 PLM   I C6   1 
HETATM 9082 C  C7   . PLM   M 4 .   ? -13.074 -33.020 -54.404 1.00 49.93  ?  603 PLM   I C7   1 
HETATM 9083 C  C8   . PLM   M 4 .   ? -12.998 -31.552 -53.938 1.00 46.79  ?  603 PLM   I C8   1 
HETATM 9084 C  C9   . PLM   M 4 .   ? -13.854 -31.348 -52.687 1.00 46.51  ?  603 PLM   I C9   1 
HETATM 9085 C  CA   . PLM   M 4 .   ? -13.635 -30.057 -51.896 1.00 45.12  ?  603 PLM   I CA   1 
HETATM 9086 C  CB   . PLM   M 4 .   ? -14.047 -30.269 -50.424 1.00 44.22  ?  603 PLM   I CB   1 
HETATM 9087 C  C1   . PLM   N 4 .   ? -13.859 -25.227 -33.297 1.00 50.15  ?  604 PLM   I C1   1 
HETATM 9088 O  O1   . PLM   N 4 .   ? -14.220 -26.316 -33.771 1.00 39.27  ?  604 PLM   I O1   1 
HETATM 9089 O  O2   . PLM   N 4 .   ? -13.143 -25.141 -32.263 1.00 53.57  ?  604 PLM   I O2   1 
HETATM 9090 C  C2   . PLM   N 4 .   ? -14.322 -23.971 -34.006 1.00 50.19  ?  604 PLM   I C2   1 
HETATM 9091 C  C3   . PLM   N 4 .   ? -13.183 -23.037 -34.420 1.00 50.06  ?  604 PLM   I C3   1 
HETATM 9092 C  C4   . PLM   N 4 .   ? -13.693 -21.626 -34.770 1.00 46.78  ?  604 PLM   I C4   1 
HETATM 9093 C  C5   . PLM   N 4 .   ? -14.729 -21.613 -35.893 1.00 43.04  ?  604 PLM   I C5   1 
HETATM 9094 C  C6   . PLM   N 4 .   ? -15.309 -20.224 -36.105 1.00 41.60  ?  604 PLM   I C6   1 
HETATM 9095 C  C7   . PLM   N 4 .   ? -16.572 -20.352 -36.955 1.00 39.94  ?  604 PLM   I C7   1 
HETATM 9096 C  C8   . PLM   N 4 .   ? -16.913 -19.032 -37.656 1.00 37.44  ?  604 PLM   I C8   1 
HETATM 9097 C  C9   . PLM   N 4 .   ? -17.195 -19.257 -39.130 1.00 36.79  ?  604 PLM   I C9   1 
HETATM 9098 C  CA   . PLM   N 4 .   ? -18.615 -18.943 -39.620 1.00 35.60  ?  604 PLM   I CA   1 
HETATM 9099 C  CB   . PLM   N 4 .   ? -18.686 -17.684 -40.469 1.00 34.78  ?  604 PLM   I CB   1 
HETATM 9100 C  CC   . PLM   N 4 .   ? -18.508 -16.405 -39.652 1.00 38.64  ?  604 PLM   I CC   1 
HETATM 9101 C  CD   . PLM   N 4 .   ? -19.761 -15.526 -39.597 1.00 40.22  ?  604 PLM   I CD   1 
HETATM 9102 C  CE   . PLM   N 4 .   ? -19.736 -14.298 -40.520 1.00 39.55  ?  604 PLM   I CE   1 
HETATM 9103 C  CF   . PLM   N 4 .   ? -21.181 -13.895 -40.899 1.00 38.56  ?  604 PLM   I CF   1 
HETATM 9104 C  CG   . PLM   N 4 .   ? -21.314 -12.560 -41.610 1.00 38.05  ?  604 PLM   I CG   1 
HETATM 9105 C  C1   . PLM   O 4 .   ? -19.126 -54.227 -28.906 1.00 34.82  ?  605 PLM   I C1   1 
HETATM 9106 O  O1   . PLM   O 4 .   ? -20.387 -54.194 -28.973 1.00 33.51  ?  605 PLM   I O1   1 
HETATM 9107 O  O2   . PLM   O 4 .   ? -18.562 -54.405 -27.817 1.00 37.76  ?  605 PLM   I O2   1 
HETATM 9108 C  C2   . PLM   O 4 .   ? -18.241 -54.080 -30.139 1.00 33.60  ?  605 PLM   I C2   1 
HETATM 9109 C  C3   . PLM   O 4 .   ? -17.325 -55.298 -30.283 1.00 33.19  ?  605 PLM   I C3   1 
HETATM 9110 C  C4   . PLM   O 4 .   ? -17.073 -55.753 -31.718 1.00 33.44  ?  605 PLM   I C4   1 
HETATM 9111 C  C5   . PLM   O 4 .   ? -18.246 -56.472 -32.355 1.00 36.82  ?  605 PLM   I C5   1 
HETATM 9112 C  C6   . PLM   O 4 .   ? -17.776 -57.288 -33.567 1.00 40.01  ?  605 PLM   I C6   1 
HETATM 9113 C  C7   . PLM   O 4 .   ? -18.930 -57.832 -34.407 1.00 43.94  ?  605 PLM   I C7   1 
HETATM 9114 C  C8   . PLM   O 4 .   ? -18.767 -57.578 -35.914 1.00 46.66  ?  605 PLM   I C8   1 
HETATM 9115 C  C9   . PLM   O 4 .   ? -18.264 -58.825 -36.649 1.00 48.11  ?  605 PLM   I C9   1 
HETATM 9116 C  CA   . PLM   O 4 .   ? -18.167 -58.669 -38.170 1.00 45.44  ?  605 PLM   I CA   1 
HETATM 9117 C  CB   . PLM   O 4 .   ? -17.184 -57.595 -38.611 1.00 46.64  ?  605 PLM   I CB   1 
HETATM 9118 C  CC   . PLM   O 4 .   ? -15.745 -57.862 -38.163 1.00 44.89  ?  605 PLM   I CC   1 
HETATM 9119 C  CD   . PLM   O 4 .   ? -15.227 -56.814 -37.193 1.00 43.42  ?  605 PLM   I CD   1 
HETATM 9120 C  CE   . PLM   O 4 .   ? -13.919 -57.256 -36.568 1.00 42.67  ?  605 PLM   I CE   1 
HETATM 9121 C  CF   . PLM   O 4 .   ? -13.133 -56.037 -36.079 1.00 45.07  ?  605 PLM   I CF   1 
HETATM 9122 C  C1   . PLM   P 4 .   ? -22.221 -60.581 -35.400 1.00 46.37  ?  606 PLM   I C1   1 
HETATM 9123 O  O1   . PLM   P 4 .   ? -21.757 -60.960 -34.290 1.00 47.13  ?  606 PLM   I O1   1 
HETATM 9124 O  O2   . PLM   P 4 .   ? -22.862 -61.300 -36.191 1.00 49.79  ?  606 PLM   I O2   1 
HETATM 9125 C  C2   . PLM   P 4 .   ? -21.973 -59.166 -35.819 1.00 46.74  ?  606 PLM   I C2   1 
HETATM 9126 C  C3   . PLM   P 4 .   ? -23.219 -58.390 -36.245 1.00 44.73  ?  606 PLM   I C3   1 
HETATM 9127 C  C4   . PLM   P 4 .   ? -22.761 -56.931 -36.343 1.00 45.80  ?  606 PLM   I C4   1 
HETATM 9128 C  C5   . PLM   P 4 .   ? -23.578 -55.935 -37.131 1.00 48.85  ?  606 PLM   I C5   1 
HETATM 9129 C  C6   . PLM   P 4 .   ? -24.430 -56.540 -38.228 1.00 50.46  ?  606 PLM   I C6   1 
HETATM 9130 C  C7   . PLM   P 4 .   ? -25.785 -57.007 -37.717 1.00 51.77  ?  606 PLM   I C7   1 
HETATM 9131 C  C8   . PLM   P 4 .   ? -26.845 -56.981 -38.818 1.00 54.35  ?  606 PLM   I C8   1 
HETATM 9132 C  C9   . PLM   P 4 .   ? -26.565 -57.952 -39.962 1.00 51.25  ?  606 PLM   I C9   1 
HETATM 9133 C  CA   . PLM   P 4 .   ? -26.744 -57.323 -41.342 1.00 51.56  ?  606 PLM   I CA   1 
HETATM 9134 C  CB   . PLM   P 4 .   ? -28.217 -57.324 -41.741 1.00 53.77  ?  606 PLM   I CB   1 
HETATM 9135 C  CC   . PLM   P 4 .   ? -28.603 -56.168 -42.660 1.00 53.32  ?  606 PLM   I CC   1 
HETATM 9136 C  CD   . PLM   P 4 .   ? -29.741 -55.374 -42.011 1.00 59.64  ?  606 PLM   I CD   1 
HETATM 9137 C  CE   . PLM   P 4 .   ? -30.160 -54.149 -42.819 1.00 63.84  ?  606 PLM   I CE   1 
HETATM 9138 C  CF   . PLM   P 4 .   ? -31.460 -53.505 -42.325 1.00 68.81  ?  606 PLM   I CF   1 
HETATM 9139 C  CG   . PLM   P 4 .   ? -32.131 -52.682 -43.415 1.00 70.07  ?  606 PLM   I CG   1 
HETATM 9140 C  C1   . PLM   Q 4 .   ? -16.671 -65.812 -56.611 1.00 61.07  ?  607 PLM   I C1   1 
HETATM 9141 O  O1   . PLM   Q 4 .   ? -17.121 -66.339 -57.653 1.00 61.70  ?  607 PLM   I O1   1 
HETATM 9142 O  O2   . PLM   Q 4 .   ? -15.522 -65.293 -56.601 1.00 54.67  ?  607 PLM   I O2   1 
HETATM 9143 C  C2   . PLM   Q 4 .   ? -17.525 -65.841 -55.331 1.00 56.43  ?  607 PLM   I C2   1 
HETATM 9144 C  C3   . PLM   Q 4 .   ? -18.971 -65.308 -55.450 1.00 51.26  ?  607 PLM   I C3   1 
HETATM 9145 C  C4   . PLM   Q 4 .   ? -19.793 -65.885 -56.620 1.00 44.38  ?  607 PLM   I C4   1 
HETATM 9146 C  C5   . PLM   Q 4 .   ? -21.299 -65.568 -56.564 1.00 41.61  ?  607 PLM   I C5   1 
HETATM 9147 C  C6   . PLM   Q 4 .   ? -22.196 -66.791 -56.758 1.00 41.20  ?  607 PLM   I C6   1 
HETATM 9148 C  C7   . PLM   Q 4 .   ? -23.317 -66.686 -57.803 1.00 40.64  ?  607 PLM   I C7   1 
HETATM 9149 C  C8   . PLM   Q 4 .   ? -23.603 -68.094 -58.340 1.00 40.50  ?  607 PLM   I C8   1 
HETATM 9150 C  C9   . PLM   Q 4 .   ? -24.874 -68.236 -59.184 1.00 42.03  ?  607 PLM   I C9   1 
HETATM 9151 C  CA   . PLM   Q 4 .   ? -25.122 -69.705 -59.554 1.00 42.04  ?  607 PLM   I CA   1 
HETATM 9152 C  CB   . PLM   Q 4 .   ? -26.591 -69.988 -59.914 1.00 44.52  ?  607 PLM   I CB   1 
HETATM 9153 C  CC   . PLM   Q 4 .   ? -27.369 -70.751 -58.826 1.00 45.80  ?  607 PLM   I CC   1 
HETATM 9154 C  CD   . PLM   Q 4 .   ? -28.816 -71.091 -59.237 1.00 45.71  ?  607 PLM   I CD   1 
HETATM 9155 C  CE   . PLM   Q 4 .   ? -29.461 -72.139 -58.320 1.00 46.01  ?  607 PLM   I CE   1 
HETATM 9156 C  CF   . PLM   Q 4 .   ? -30.958 -71.924 -58.123 1.00 46.03  ?  607 PLM   I CF   1 
HETATM 9157 C  C1   . PLM   R 4 .   ? -28.126 -48.315 -19.523 1.00 74.96  ?  608 PLM   I C1   1 
HETATM 9158 O  O1   . PLM   R 4 .   ? -29.370 -48.438 -19.422 1.00 72.65  ?  608 PLM   I O1   1 
HETATM 9159 O  O2   . PLM   R 4 .   ? -27.329 -48.754 -18.648 1.00 77.44  ?  608 PLM   I O2   1 
HETATM 9160 C  C2   . PLM   R 4 .   ? -27.585 -47.633 -20.773 1.00 70.23  ?  608 PLM   I C2   1 
HETATM 9161 C  C3   . PLM   R 4 .   ? -26.929 -46.271 -20.499 1.00 66.36  ?  608 PLM   I C3   1 
HETATM 9162 C  C4   . PLM   R 4 .   ? -25.567 -46.392 -19.802 1.00 61.91  ?  608 PLM   I C4   1 
HETATM 9163 C  C5   . PLM   R 4 .   ? -25.632 -45.960 -18.335 1.00 57.04  ?  608 PLM   I C5   1 
HETATM 9164 C  C6   . PLM   R 4 .   ? -24.484 -46.525 -17.503 1.00 52.55  ?  608 PLM   I C6   1 
HETATM 9165 C  C7   . PLM   R 4 .   ? -24.688 -46.288 -16.009 1.00 47.60  ?  608 PLM   I C7   1 
HETATM 9166 C  C8   . PLM   R 4 .   ? -23.516 -45.561 -15.356 1.00 45.75  ?  608 PLM   I C8   1 
HETATM 9167 C  C9   . PLM   R 4 .   ? -23.784 -44.073 -15.362 1.00 46.29  ?  608 PLM   I C9   1 
HETATM 9168 C  CA   . PLM   R 4 .   ? -22.509 -43.299 -15.102 1.00 48.74  ?  608 PLM   I CA   1 
HETATM 9169 C  CB   . PLM   R 4 .   ? -22.856 -41.829 -15.229 1.00 54.31  ?  608 PLM   I CB   1 
HETATM 9170 C  CC   . PLM   R 4 .   ? -21.630 -40.948 -15.024 1.00 55.71  ?  608 PLM   I CC   1 
HETATM 9171 C  CD   . PLM   R 4 .   ? -21.949 -39.505 -15.373 1.00 56.88  ?  608 PLM   I CD   1 
HETATM 9172 C  CE   . PLM   R 4 .   ? -21.072 -38.518 -14.613 1.00 61.14  ?  608 PLM   I CE   1 
HETATM 9173 C  CF   . PLM   R 4 .   ? -21.670 -38.109 -13.275 1.00 64.36  ?  608 PLM   I CF   1 
HETATM 9174 C  CG   . PLM   R 4 .   ? -20.719 -37.179 -12.548 1.00 65.08  ?  608 PLM   I CG   1 
HETATM 9175 O  O    . HOH   S 5 .   ? -5.988  20.888  7.477   1.00 30.20  ?  701 HOH   A O    1 
HETATM 9176 O  O    . HOH   S 5 .   ? -1.955  21.717  -7.681  1.00 19.20  ?  702 HOH   A O    1 
HETATM 9177 O  O    . HOH   S 5 .   ? 5.804   -5.185  1.519   1.00 38.20  ?  703 HOH   A O    1 
HETATM 9178 O  O    . HOH   S 5 .   ? -17.600 19.083  2.496   1.00 31.77  ?  704 HOH   A O    1 
HETATM 9179 O  O    . HOH   S 5 .   ? -8.938  5.295   -21.083 1.00 23.73  ?  705 HOH   A O    1 
HETATM 9180 O  O    . HOH   S 5 .   ? -0.221  12.244  -38.871 1.00 33.53  ?  706 HOH   A O    1 
HETATM 9181 O  O    . HOH   S 5 .   ? 2.511   12.708  -10.555 1.00 24.83  ?  707 HOH   A O    1 
HETATM 9182 O  O    . HOH   S 5 .   ? -7.332  -4.403  -36.428 1.00 36.77  ?  708 HOH   A O    1 
HETATM 9183 O  O    . HOH   S 5 .   ? 4.255   -26.680 15.555  1.00 28.98  ?  709 HOH   A O    1 
HETATM 9184 O  O    . HOH   S 5 .   ? -12.760 5.136   -6.590  1.00 33.68  ?  710 HOH   A O    1 
HETATM 9185 O  O    . HOH   S 5 .   ? 17.747  7.372   -23.615 1.00 38.81  ?  711 HOH   A O    1 
HETATM 9186 O  O    . HOH   S 5 .   ? 0.780   -36.195 10.862  1.00 23.81  ?  712 HOH   A O    1 
HETATM 9187 O  O    . HOH   S 5 .   ? 21.859  9.767   -25.413 1.00 39.73  ?  713 HOH   A O    1 
HETATM 9188 O  O    . HOH   S 5 .   ? -6.608  -19.076 0.810   1.00 29.53  ?  714 HOH   A O    1 
HETATM 9189 O  O    . HOH   S 5 .   ? -8.887  -36.864 1.518   1.00 27.81  ?  715 HOH   A O    1 
HETATM 9190 O  O    . HOH   S 5 .   ? -3.342  -8.774  -22.291 1.00 42.61  ?  716 HOH   A O    1 
HETATM 9191 O  O    . HOH   S 5 .   ? 2.926   -31.280 18.654  1.00 42.23  ?  717 HOH   A O    1 
HETATM 9192 O  O    . HOH   S 5 .   ? 6.212   -14.451 -2.337  1.00 48.04  ?  718 HOH   A O    1 
HETATM 9193 O  O    . HOH   S 5 .   ? 4.416   14.251  15.068  1.00 34.98  ?  719 HOH   A O    1 
HETATM 9194 O  O    . HOH   S 5 .   ? -7.849  -22.876 -0.031  1.00 36.29  ?  720 HOH   A O    1 
HETATM 9195 O  O    . HOH   S 5 .   ? -6.056  -34.774 -3.955  1.00 31.15  ?  721 HOH   A O    1 
HETATM 9196 O  O    . HOH   S 5 .   ? -4.251  14.538  -41.424 1.00 34.53  ?  722 HOH   A O    1 
HETATM 9197 O  O    . HOH   S 5 .   ? 1.870   16.124  35.028  1.00 34.89  ?  723 HOH   A O    1 
HETATM 9198 O  O    . HOH   S 5 .   ? -12.058 4.215   -28.403 1.00 30.07  ?  724 HOH   A O    1 
HETATM 9199 O  O    . HOH   S 5 .   ? -1.110  23.304  -9.101  1.00 25.77  ?  725 HOH   A O    1 
HETATM 9200 O  O    . HOH   S 5 .   ? 9.193   -17.871 -6.529  1.00 31.02  ?  726 HOH   A O    1 
HETATM 9201 O  O    . HOH   S 5 .   ? -6.850  17.725  22.324  1.00 32.16  ?  727 HOH   A O    1 
HETATM 9202 O  O    . HOH   S 5 .   ? 3.501   -18.182 -20.767 1.00 36.09  ?  728 HOH   A O    1 
HETATM 9203 O  O    . HOH   S 5 .   ? -5.559  -33.563 5.411   1.00 29.46  ?  729 HOH   A O    1 
HETATM 9204 O  O    . HOH   S 5 .   ? 13.017  -42.852 2.569   1.00 24.82  ?  730 HOH   A O    1 
HETATM 9205 O  O    . HOH   S 5 .   ? -8.830  -1.184  -31.048 1.00 30.04  ?  731 HOH   A O    1 
HETATM 9206 O  O    . HOH   S 5 .   ? 12.798  -7.737  -24.652 1.00 19.32  ?  732 HOH   A O    1 
HETATM 9207 O  O    . HOH   S 5 .   ? 8.037   20.216  -15.677 1.00 34.66  ?  733 HOH   A O    1 
HETATM 9208 O  O    . HOH   S 5 .   ? -13.609 10.447  -12.323 1.00 40.55  ?  734 HOH   A O    1 
HETATM 9209 O  O    . HOH   S 5 .   ? -9.829  -2.576  9.129   1.00 35.82  ?  735 HOH   A O    1 
HETATM 9210 O  O    . HOH   S 5 .   ? 12.256  -1.513  11.292  1.00 45.26  ?  736 HOH   A O    1 
HETATM 9211 O  O    . HOH   S 5 .   ? 21.165  2.046   -12.374 1.00 34.96  ?  737 HOH   A O    1 
HETATM 9212 O  O    . HOH   S 5 .   ? 2.347   17.646  -29.929 1.00 33.10  ?  738 HOH   A O    1 
HETATM 9213 O  O    . HOH   S 5 .   ? 8.670   -14.110 -2.974  1.00 26.73  ?  739 HOH   A O    1 
HETATM 9214 O  O    . HOH   S 5 .   ? -17.541 28.663  8.313   1.00 31.46  ?  740 HOH   A O    1 
HETATM 9215 O  O    . HOH   S 5 .   ? 6.201   -3.296  15.468  1.00 33.66  ?  741 HOH   A O    1 
HETATM 9216 O  O    . HOH   S 5 .   ? 11.370  -37.270 5.836   1.00 17.17  ?  742 HOH   A O    1 
HETATM 9217 O  O    . HOH   S 5 .   ? -10.082 -11.811 -8.561  1.00 29.46  ?  743 HOH   A O    1 
HETATM 9218 O  O    . HOH   S 5 .   ? -7.128  -17.683 -6.161  1.00 24.54  ?  744 HOH   A O    1 
HETATM 9219 O  O    . HOH   S 5 .   ? 0.304   -22.064 -12.051 1.00 31.83  ?  745 HOH   A O    1 
HETATM 9220 O  O    . HOH   S 5 .   ? -17.782 -29.092 14.091  1.00 29.52  ?  746 HOH   A O    1 
HETATM 9221 O  O    . HOH   S 5 .   ? 9.658   12.618  -9.212  1.00 21.81  ?  747 HOH   A O    1 
HETATM 9222 O  O    . HOH   S 5 .   ? 14.972  -19.068 22.828  1.00 40.81  ?  748 HOH   A O    1 
HETATM 9223 O  O    . HOH   S 5 .   ? -8.311  -1.376  -28.247 1.00 30.03  ?  749 HOH   A O    1 
HETATM 9224 O  O    . HOH   S 5 .   ? -7.901  33.994  28.216  1.00 37.16  ?  750 HOH   A O    1 
HETATM 9225 O  O    . HOH   S 5 .   ? 9.243   -12.149 28.975  1.00 27.73  ?  751 HOH   A O    1 
HETATM 9226 O  O    . HOH   S 5 .   ? -18.869 -28.072 16.586  1.00 42.58  ?  752 HOH   A O    1 
HETATM 9227 O  O    . HOH   S 5 .   ? -15.521 5.455   8.980   1.00 49.46  ?  753 HOH   A O    1 
HETATM 9228 O  O    . HOH   S 5 .   ? -14.602 10.775  -32.500 1.00 37.18  ?  754 HOH   A O    1 
HETATM 9229 O  O    . HOH   S 5 .   ? 7.232   -42.704 4.425   1.00 33.02  ?  755 HOH   A O    1 
HETATM 9230 O  O    . HOH   S 5 .   ? 14.241  1.470   -28.285 1.00 38.65  ?  756 HOH   A O    1 
HETATM 9231 O  O    . HOH   S 5 .   ? 1.065   23.812  -22.937 1.00 13.84  ?  757 HOH   A O    1 
HETATM 9232 O  O    . HOH   S 5 .   ? 12.573  25.136  2.847   1.00 37.21  ?  758 HOH   A O    1 
HETATM 9233 O  O    . HOH   S 5 .   ? 15.576  4.014   -15.709 1.00 23.64  ?  759 HOH   A O    1 
HETATM 9234 O  O    . HOH   S 5 .   ? -6.364  13.479  -13.875 1.00 31.74  ?  760 HOH   A O    1 
HETATM 9235 O  O    . HOH   S 5 .   ? -1.858  -15.890 2.560   1.00 27.81  ?  761 HOH   A O    1 
HETATM 9236 O  O    . HOH   S 5 .   ? 19.725  -9.561  -14.747 1.00 27.04  ?  762 HOH   A O    1 
HETATM 9237 O  O    . HOH   S 5 .   ? 7.983   10.622  24.794  1.00 38.13  ?  763 HOH   A O    1 
HETATM 9238 O  O    . HOH   S 5 .   ? 0.199   -34.662 -4.650  1.00 25.26  ?  764 HOH   A O    1 
HETATM 9239 O  O    . HOH   S 5 .   ? 10.494  18.551  -5.741  1.00 34.19  ?  765 HOH   A O    1 
HETATM 9240 O  O    . HOH   S 5 .   ? 3.241   24.178  -29.912 1.00 29.31  ?  766 HOH   A O    1 
HETATM 9241 O  O    . HOH   S 5 .   ? 0.682   -34.141 -1.179  1.00 18.51  ?  767 HOH   A O    1 
HETATM 9242 O  O    . HOH   S 5 .   ? 13.158  -29.561 2.790   1.00 29.35  ?  768 HOH   A O    1 
HETATM 9243 O  O    . HOH   S 5 .   ? -1.071  15.485  -13.516 1.00 21.54  ?  769 HOH   A O    1 
HETATM 9244 O  O    . HOH   S 5 .   ? -22.766 -28.563 2.320   1.00 25.33  ?  770 HOH   A O    1 
HETATM 9245 O  O    . HOH   S 5 .   ? 14.756  -3.734  -13.236 1.00 19.39  ?  771 HOH   A O    1 
HETATM 9246 O  O    . HOH   S 5 .   ? 2.117   24.549  -17.125 1.00 33.34  ?  772 HOH   A O    1 
HETATM 9247 O  O    . HOH   S 5 .   ? 12.098  -21.835 -1.193  1.00 32.38  ?  773 HOH   A O    1 
HETATM 9248 O  O    . HOH   S 5 .   ? -3.073  16.931  35.496  1.00 45.37  ?  774 HOH   A O    1 
HETATM 9249 O  O    . HOH   S 5 .   ? -5.845  5.431   -3.571  1.00 33.87  ?  775 HOH   A O    1 
HETATM 9250 O  O    . HOH   S 5 .   ? -12.337 12.927  -27.550 1.00 39.80  ?  776 HOH   A O    1 
HETATM 9251 O  O    . HOH   S 5 .   ? 6.434   28.428  24.176  1.00 40.50  ?  777 HOH   A O    1 
HETATM 9252 O  O    . HOH   S 5 .   ? -5.157  -11.500 21.340  1.00 28.15  ?  778 HOH   A O    1 
HETATM 9253 O  O    . HOH   S 5 .   ? 9.369   -22.483 11.697  1.00 29.90  ?  779 HOH   A O    1 
HETATM 9254 O  O    . HOH   S 5 .   ? 6.644   -23.008 -10.711 1.00 38.86  ?  780 HOH   A O    1 
HETATM 9255 O  O    . HOH   S 5 .   ? 7.881   21.551  -13.174 1.00 51.32  ?  781 HOH   A O    1 
HETATM 9256 O  O    . HOH   S 5 .   ? -13.324 28.609  6.570   1.00 33.30  ?  782 HOH   A O    1 
HETATM 9257 O  O    . HOH   S 5 .   ? 15.419  -3.174  -18.470 1.00 21.82  ?  783 HOH   A O    1 
HETATM 9258 O  O    . HOH   S 5 .   ? 12.901  4.055   -16.335 1.00 35.02  ?  784 HOH   A O    1 
HETATM 9259 O  O    . HOH   S 5 .   ? -4.889  -2.912  6.351   1.00 34.61  ?  785 HOH   A O    1 
HETATM 9260 O  O    . HOH   S 5 .   ? 19.841  -8.271  12.727  1.00 32.94  ?  786 HOH   A O    1 
HETATM 9261 O  O    . HOH   S 5 .   ? 9.006   -0.519  26.856  1.00 29.90  ?  787 HOH   A O    1 
HETATM 9262 O  O    . HOH   S 5 .   ? -21.823 -30.728 -7.324  1.00 35.92  ?  788 HOH   A O    1 
HETATM 9263 O  O    . HOH   S 5 .   ? 0.826   22.567  -7.932  1.00 33.32  ?  789 HOH   A O    1 
HETATM 9264 O  O    . HOH   S 5 .   ? 2.517   23.519  -0.101  1.00 35.85  ?  790 HOH   A O    1 
HETATM 9265 O  O    . HOH   S 5 .   ? -5.817  -11.707 -16.739 1.00 52.38  ?  791 HOH   A O    1 
HETATM 9266 O  O    . HOH   S 5 .   ? 5.094   -23.216 12.656  1.00 25.43  ?  792 HOH   A O    1 
HETATM 9267 O  O    . HOH   S 5 .   ? 10.063  4.621   -11.172 1.00 18.60  ?  793 HOH   A O    1 
HETATM 9268 O  O    . HOH   S 5 .   ? 15.304  -0.974  -25.011 1.00 44.55  ?  794 HOH   A O    1 
HETATM 9269 O  O    . HOH   S 5 .   ? 14.178  13.372  5.442   1.00 39.09  ?  795 HOH   A O    1 
HETATM 9270 O  O    . HOH   S 5 .   ? -1.702  -6.844  -22.455 1.00 44.97  ?  796 HOH   A O    1 
HETATM 9271 O  O    . HOH   S 5 .   ? 8.836   17.779  -7.721  1.00 29.06  ?  797 HOH   A O    1 
HETATM 9272 O  O    . HOH   S 5 .   ? -3.615  10.117  -38.655 1.00 38.54  ?  798 HOH   A O    1 
HETATM 9273 O  O    . HOH   S 5 .   ? 6.275   -45.238 3.935   1.00 35.20  ?  799 HOH   A O    1 
HETATM 9274 O  O    . HOH   S 5 .   ? 0.281   22.527  -1.320  1.00 34.37  ?  800 HOH   A O    1 
HETATM 9275 O  O    . HOH   S 5 .   ? -23.838 -28.973 5.440   1.00 26.53  ?  801 HOH   A O    1 
HETATM 9276 O  O    . HOH   S 5 .   ? -14.631 25.813  6.392   1.00 31.30  ?  802 HOH   A O    1 
HETATM 9277 O  O    . HOH   S 5 .   ? 8.059   -46.783 -2.375  1.00 40.48  ?  803 HOH   A O    1 
HETATM 9278 O  O    . HOH   S 5 .   ? 0.384   -9.629  -24.708 1.00 27.44  ?  804 HOH   A O    1 
HETATM 9279 O  O    . HOH   S 5 .   ? 9.221   -14.908 2.379   1.00 38.74  ?  805 HOH   A O    1 
HETATM 9280 O  O    . HOH   S 5 .   ? -12.006 4.644   -24.110 1.00 38.06  ?  806 HOH   A O    1 
HETATM 9281 O  O    . HOH   S 5 .   ? -15.339 9.493   -30.259 1.00 36.44  ?  807 HOH   A O    1 
HETATM 9282 O  O    . HOH   S 5 .   ? -10.112 -25.679 18.129  1.00 44.32  ?  808 HOH   A O    1 
HETATM 9283 O  O    . HOH   S 5 .   ? 15.230  4.946   -12.970 1.00 37.05  ?  809 HOH   A O    1 
HETATM 9284 O  O    . HOH   S 5 .   ? 5.276   23.971  -28.588 1.00 33.34  ?  810 HOH   A O    1 
HETATM 9285 O  O    . HOH   S 5 .   ? 8.116   -5.143  -29.519 1.00 31.40  ?  811 HOH   A O    1 
HETATM 9286 O  O    . HOH   S 5 .   ? -7.796  -12.903 -15.670 1.00 38.71  ?  812 HOH   A O    1 
HETATM 9287 O  O    . HOH   S 5 .   ? 9.598   -28.251 -9.688  1.00 37.71  ?  813 HOH   A O    1 
HETATM 9288 O  O    . HOH   S 5 .   ? 5.727   -43.857 6.178   1.00 48.51  ?  814 HOH   A O    1 
HETATM 9289 O  O    . HOH   S 5 .   ? -5.933  -35.743 4.622   1.00 26.63  ?  815 HOH   A O    1 
HETATM 9290 O  O    . HOH   S 5 .   ? 14.968  15.014  3.762   1.00 64.26  ?  816 HOH   A O    1 
HETATM 9291 O  O    . HOH   S 5 .   ? 9.098   -30.954 -9.321  1.00 35.80  ?  817 HOH   A O    1 
HETATM 9292 O  O    . HOH   S 5 .   ? -13.915 12.050  -29.342 1.00 64.24  ?  818 HOH   A O    1 
HETATM 9293 O  O    . HOH   S 5 .   ? -18.345 4.213   -2.582  1.00 40.19  ?  819 HOH   A O    1 
HETATM 9294 O  O    . HOH   S 5 .   ? 3.918   -4.106  -0.013  1.00 36.82  ?  820 HOH   A O    1 
HETATM 9295 O  O    . HOH   S 5 .   ? 13.521  -38.526 4.521   1.00 36.76  ?  821 HOH   A O    1 
HETATM 9296 O  O    . HOH   S 5 .   ? 9.918   -12.379 0.848   1.00 37.18  ?  822 HOH   A O    1 
HETATM 9297 O  O    . HOH   S 5 .   ? 4.525   -24.558 15.170  1.00 24.45  ?  823 HOH   A O    1 
HETATM 9298 O  O    . HOH   S 5 .   ? 0.995   4.924   -43.855 1.00 58.45  ?  824 HOH   A O    1 
HETATM 9299 O  O    . HOH   S 5 .   ? 12.238  -34.909 6.062   1.00 25.68  ?  825 HOH   A O    1 
HETATM 9300 O  O    . HOH   S 5 .   ? -1.558  -24.041 -12.647 1.00 38.53  ?  826 HOH   A O    1 
HETATM 9301 O  O    . HOH   S 5 .   ? 5.314   16.632  -30.762 1.00 40.50  ?  827 HOH   A O    1 
HETATM 9302 O  O    . HOH   S 5 .   ? -4.135  11.544  -41.095 1.00 27.47  ?  828 HOH   A O    1 
HETATM 9303 O  O    . HOH   S 5 .   ? 1.003   2.430   -43.617 1.00 38.22  ?  829 HOH   A O    1 
HETATM 9304 O  O    . HOH   T 5 .   ? -36.046 -55.652 -40.936 1.00 36.72  ?  701 HOH   I O    1 
HETATM 9305 O  O    . HOH   T 5 .   ? -20.742 -16.354 -56.007 1.00 41.04  ?  702 HOH   I O    1 
HETATM 9306 O  O    . HOH   T 5 .   ? -12.060 -56.585 -16.512 1.00 26.99  ?  703 HOH   I O    1 
HETATM 9307 O  O    . HOH   T 5 .   ? -12.495 -47.611 -26.288 1.00 30.01  ?  704 HOH   I O    1 
HETATM 9308 O  O    . HOH   T 5 .   ? 2.001   -33.235 -26.098 1.00 38.26  ?  705 HOH   I O    1 
HETATM 9309 O  O    . HOH   T 5 .   ? -8.695  -49.799 -4.816  1.00 34.31  ?  706 HOH   I O    1 
HETATM 9310 O  O    . HOH   T 5 .   ? -37.691 -23.477 -53.842 1.00 30.88  ?  707 HOH   I O    1 
HETATM 9311 O  O    . HOH   T 5 .   ? -13.904 -47.042 -28.446 1.00 31.37  ?  708 HOH   I O    1 
HETATM 9312 O  O    . HOH   T 5 .   ? -27.654 -15.835 -36.600 1.00 40.87  ?  709 HOH   I O    1 
HETATM 9313 O  O    . HOH   T 5 .   ? -23.440 -13.016 -32.608 1.00 37.38  ?  710 HOH   I O    1 
HETATM 9314 O  O    . HOH   T 5 .   ? -10.559 -15.693 -29.626 1.00 41.57  ?  711 HOH   I O    1 
HETATM 9315 O  O    . HOH   T 5 .   ? -8.475  -4.194  -42.653 1.00 20.05  ?  712 HOH   I O    1 
HETATM 9316 O  O    . HOH   T 5 .   ? -24.145 -25.948 -59.002 1.00 35.30  ?  713 HOH   I O    1 
HETATM 9317 O  O    . HOH   T 5 .   ? -9.864  -63.998 -49.156 1.00 34.92  ?  714 HOH   I O    1 
HETATM 9318 O  O    . HOH   T 5 .   ? -4.048  -43.290 -53.252 1.00 40.67  ?  715 HOH   I O    1 
HETATM 9319 O  O    . HOH   T 5 .   ? -25.436 -2.720  -38.788 1.00 32.46  ?  716 HOH   I O    1 
HETATM 9320 O  O    . HOH   T 5 .   ? -6.492  -45.467 -10.036 1.00 35.94  ?  717 HOH   I O    1 
HETATM 9321 O  O    . HOH   T 5 .   ? -16.522 -54.413 -26.453 1.00 26.54  ?  718 HOH   I O    1 
HETATM 9322 O  O    . HOH   T 5 .   ? -45.300 -18.214 -42.912 1.00 31.63  ?  719 HOH   I O    1 
HETATM 9323 O  O    . HOH   T 5 .   ? -13.752 -59.577 -13.661 1.00 28.10  ?  720 HOH   I O    1 
HETATM 9324 O  O    . HOH   T 5 .   ? -28.055 -39.503 -1.791  1.00 30.59  ?  721 HOH   I O    1 
HETATM 9325 O  O    . HOH   T 5 .   ? 0.145   -31.971 -22.530 1.00 26.27  ?  722 HOH   I O    1 
HETATM 9326 O  O    . HOH   T 5 .   ? -18.442 -0.651  -42.042 1.00 26.75  ?  723 HOH   I O    1 
HETATM 9327 O  O    . HOH   T 5 .   ? -34.243 -47.569 -46.460 1.00 39.36  ?  724 HOH   I O    1 
HETATM 9328 O  O    . HOH   T 5 .   ? -10.999 -47.630 -52.779 1.00 31.86  ?  725 HOH   I O    1 
HETATM 9329 O  O    . HOH   T 5 .   ? -27.144 -18.869 -36.137 1.00 26.53  ?  726 HOH   I O    1 
HETATM 9330 O  O    . HOH   T 5 .   ? -17.293 -8.780  -30.059 1.00 43.07  ?  727 HOH   I O    1 
HETATM 9331 O  O    . HOH   T 5 .   ? -19.065 -7.267  -35.943 1.00 19.95  ?  728 HOH   I O    1 
HETATM 9332 O  O    . HOH   T 5 .   ? -21.755 -20.055 -26.349 1.00 46.42  ?  729 HOH   I O    1 
HETATM 9333 O  O    . HOH   T 5 .   ? -33.357 -65.247 -54.958 1.00 27.73  ?  730 HOH   I O    1 
HETATM 9334 O  O    . HOH   T 5 .   ? -6.397  -33.706 -12.658 1.00 16.04  ?  731 HOH   I O    1 
HETATM 9335 O  O    . HOH   T 5 .   ? -22.902 -55.890 3.904   1.00 41.15  ?  732 HOH   I O    1 
HETATM 9336 O  O    . HOH   T 5 .   ? -28.050 -46.805 -15.868 1.00 31.86  ?  733 HOH   I O    1 
HETATM 9337 O  O    . HOH   T 5 .   ? 3.446   -27.623 -58.241 1.00 54.03  ?  734 HOH   I O    1 
HETATM 9338 O  O    . HOH   T 5 .   ? -28.392 -50.983 -14.004 1.00 18.75  ?  735 HOH   I O    1 
HETATM 9339 O  O    . HOH   T 5 .   ? -11.118 -27.517 -34.491 1.00 28.75  ?  736 HOH   I O    1 
HETATM 9340 O  O    . HOH   T 5 .   ? -17.996 -57.498 -0.334  1.00 26.36  ?  737 HOH   I O    1 
HETATM 9341 O  O    . HOH   T 5 .   ? -10.745 -19.225 -48.557 1.00 22.63  ?  738 HOH   I O    1 
HETATM 9342 O  O    . HOH   T 5 .   ? -21.337 -61.097 -5.683  1.00 41.10  ?  739 HOH   I O    1 
HETATM 9343 O  O    . HOH   T 5 .   ? -26.314 -56.940 6.440   1.00 42.43  ?  740 HOH   I O    1 
HETATM 9344 O  O    . HOH   T 5 .   ? -11.816 -52.426 -48.852 1.00 43.03  ?  741 HOH   I O    1 
HETATM 9345 O  O    . HOH   T 5 .   ? -19.234 0.112   -35.445 1.00 34.68  ?  742 HOH   I O    1 
HETATM 9346 O  O    . HOH   T 5 .   ? -22.648 -60.919 -16.143 1.00 36.02  ?  743 HOH   I O    1 
HETATM 9347 O  O    . HOH   T 5 .   ? -25.197 -55.196 -23.481 1.00 36.45  ?  744 HOH   I O    1 
HETATM 9348 O  O    . HOH   T 5 .   ? -24.899 -48.120 -45.263 1.00 46.47  ?  745 HOH   I O    1 
HETATM 9349 O  O    . HOH   T 5 .   ? -3.916  -44.469 -65.036 1.00 35.27  ?  746 HOH   I O    1 
HETATM 9350 O  O    . HOH   T 5 .   ? -14.007 -71.808 -52.272 1.00 48.35  ?  747 HOH   I O    1 
HETATM 9351 O  O    . HOH   T 5 .   ? -37.221 -61.987 -39.663 1.00 87.62  ?  748 HOH   I O    1 
HETATM 9352 O  O    . HOH   T 5 .   ? -2.493  -22.059 -29.144 1.00 42.99  ?  749 HOH   I O    1 
HETATM 9353 O  O    . HOH   T 5 .   ? -15.850 -45.358 -29.064 1.00 34.43  ?  750 HOH   I O    1 
HETATM 9354 O  O    . HOH   T 5 .   ? -24.841 -8.775  -54.324 1.00 42.70  ?  751 HOH   I O    1 
HETATM 9355 O  O    . HOH   T 5 .   ? -25.114 -47.495 -33.530 1.00 38.88  ?  752 HOH   I O    1 
HETATM 9356 O  O    . HOH   T 5 .   ? -6.456  1.316   -39.485 1.00 18.90  ?  753 HOH   I O    1 
HETATM 9357 O  O    . HOH   T 5 .   ? -41.830 -58.692 -39.021 1.00 30.08  ?  754 HOH   I O    1 
HETATM 9358 O  O    . HOH   T 5 .   ? -17.054 -9.968  -55.481 1.00 37.79  ?  755 HOH   I O    1 
HETATM 9359 O  O    . HOH   T 5 .   ? -19.298 -5.279  -48.458 1.00 40.43  ?  756 HOH   I O    1 
HETATM 9360 O  O    . HOH   T 5 .   ? -44.088 -22.827 -40.145 1.00 28.83  ?  757 HOH   I O    1 
HETATM 9361 O  O    . HOH   T 5 .   ? -21.646 -7.350  -45.906 1.00 29.62  ?  758 HOH   I O    1 
HETATM 9362 O  O    . HOH   T 5 .   ? -14.787 -18.705 -49.943 1.00 19.59  ?  759 HOH   I O    1 
HETATM 9363 O  O    . HOH   T 5 .   ? -11.808 -69.615 -61.266 1.00 31.15  ?  760 HOH   I O    1 
HETATM 9364 O  O    . HOH   T 5 .   ? -42.496 -13.430 -39.405 1.00 30.13  ?  761 HOH   I O    1 
HETATM 9365 O  O    . HOH   T 5 .   ? -10.932 -5.973  -27.379 1.00 45.71  ?  762 HOH   I O    1 
HETATM 9366 O  O    . HOH   T 5 .   ? -3.805  -38.258 -18.476 1.00 26.63  ?  763 HOH   I O    1 
HETATM 9367 O  O    . HOH   T 5 .   ? -21.040 -34.413 -15.243 1.00 40.73  ?  764 HOH   I O    1 
HETATM 9368 O  O    . HOH   T 5 .   ? -7.768  -59.395 -22.738 1.00 42.04  ?  765 HOH   I O    1 
HETATM 9369 O  O    . HOH   T 5 .   ? -25.989 -5.899  -41.458 1.00 30.81  ?  766 HOH   I O    1 
HETATM 9370 O  O    . HOH   T 5 .   ? -25.145 -57.721 -16.613 1.00 27.99  ?  767 HOH   I O    1 
HETATM 9371 O  O    . HOH   T 5 .   ? -25.065 -8.032  -42.835 1.00 34.39  ?  768 HOH   I O    1 
HETATM 9372 O  O    . HOH   T 5 .   ? -31.445 -79.280 -62.584 1.00 43.62  ?  769 HOH   I O    1 
HETATM 9373 O  O    . HOH   T 5 .   ? -34.300 -66.506 -57.213 1.00 32.37  ?  770 HOH   I O    1 
HETATM 9374 O  O    . HOH   T 5 .   ? -25.245 -65.346 -71.003 1.00 38.59  ?  771 HOH   I O    1 
HETATM 9375 O  O    . HOH   T 5 .   ? -9.214  -54.267 -27.761 1.00 27.55  ?  772 HOH   I O    1 
HETATM 9376 O  O    . HOH   T 5 .   ? -32.823 -74.540 -48.854 1.00 38.28  ?  773 HOH   I O    1 
HETATM 9377 O  O    . HOH   T 5 .   ? -10.900 -62.383 -50.549 1.00 34.60  ?  774 HOH   I O    1 
HETATM 9378 O  O    . HOH   T 5 .   ? -14.004 -36.540 -39.116 1.00 41.68  ?  775 HOH   I O    1 
HETATM 9379 O  O    . HOH   T 5 .   ? -27.185 -40.033 -8.581  1.00 32.51  ?  776 HOH   I O    1 
HETATM 9380 O  O    . HOH   T 5 .   ? -9.127  -46.213 -26.054 1.00 19.54  ?  777 HOH   I O    1 
HETATM 9381 O  O    . HOH   T 5 .   ? -4.633  -51.658 -16.292 1.00 26.60  ?  778 HOH   I O    1 
HETATM 9382 O  O    . HOH   T 5 .   ? -21.858 -25.799 -39.812 1.00 27.17  ?  779 HOH   I O    1 
HETATM 9383 O  O    . HOH   T 5 .   ? -9.428  -38.750 -8.679  1.00 35.38  ?  780 HOH   I O    1 
HETATM 9384 O  O    . HOH   T 5 .   ? -24.649 -59.665 -8.694  1.00 34.37  ?  781 HOH   I O    1 
HETATM 9385 O  O    . HOH   T 5 .   ? -20.144 -57.183 -23.697 1.00 23.61  ?  782 HOH   I O    1 
HETATM 9386 O  O    . HOH   T 5 .   ? -28.649 -45.807 -9.770  1.00 27.64  ?  783 HOH   I O    1 
HETATM 9387 O  O    . HOH   T 5 .   ? -19.629 -6.895  -32.523 1.00 28.31  ?  784 HOH   I O    1 
HETATM 9388 O  O    . HOH   T 5 .   ? -14.403 -31.249 -35.223 1.00 35.80  ?  785 HOH   I O    1 
HETATM 9389 O  O    . HOH   T 5 .   ? -27.241 -23.834 -30.990 1.00 30.52  ?  786 HOH   I O    1 
HETATM 9390 O  O    . HOH   T 5 .   ? -12.075 -6.743  -24.897 1.00 42.17  ?  787 HOH   I O    1 
HETATM 9391 O  O    . HOH   T 5 .   ? -12.813 -19.027 -26.508 1.00 32.22  ?  788 HOH   I O    1 
HETATM 9392 O  O    . HOH   T 5 .   ? -6.347  -12.011 -39.834 1.00 23.25  ?  789 HOH   I O    1 
HETATM 9393 O  O    . HOH   T 5 .   ? -38.547 -13.261 -53.863 1.00 25.46  ?  790 HOH   I O    1 
HETATM 9394 O  O    . HOH   T 5 .   ? -34.912 -41.669 -22.801 1.00 36.08  ?  791 HOH   I O    1 
HETATM 9395 O  O    . HOH   T 5 .   ? -10.232 -42.631 -27.079 1.00 33.58  ?  792 HOH   I O    1 
HETATM 9396 O  O    . HOH   T 5 .   ? -11.291 -24.582 -62.323 1.00 32.41  ?  793 HOH   I O    1 
HETATM 9397 O  O    . HOH   T 5 .   ? -9.619  -22.765 -28.703 1.00 35.06  ?  794 HOH   I O    1 
HETATM 9398 O  O    . HOH   T 5 .   ? -34.397 -54.075 -45.869 1.00 45.78  ?  795 HOH   I O    1 
HETATM 9399 O  O    . HOH   T 5 .   ? -30.578 -16.378 -54.905 1.00 36.51  ?  796 HOH   I O    1 
HETATM 9400 O  O    . HOH   T 5 .   ? -10.704 -64.846 -28.282 1.00 31.60  ?  797 HOH   I O    1 
HETATM 9401 O  O    . HOH   T 5 .   ? -40.864 -15.403 -29.629 1.00 40.50  ?  798 HOH   I O    1 
HETATM 9402 O  O    . HOH   T 5 .   ? -13.208 -63.923 -11.595 1.00 55.15  ?  799 HOH   I O    1 
HETATM 9403 O  O    . HOH   T 5 .   ? -17.512 -75.785 -47.363 1.00 46.77  ?  800 HOH   I O    1 
HETATM 9404 O  O    . HOH   T 5 .   ? -30.819 -56.158 6.381   1.00 35.52  ?  801 HOH   I O    1 
HETATM 9405 O  O    . HOH   T 5 .   ? -7.193  -19.768 -16.213 1.00 32.22  ?  802 HOH   I O    1 
HETATM 9406 O  O    . HOH   T 5 .   ? -8.593  -40.613 -30.809 1.00 44.07  ?  803 HOH   I O    1 
HETATM 9407 O  O    . HOH   T 5 .   ? -9.054  -21.270 -48.779 1.00 33.05  ?  804 HOH   I O    1 
HETATM 9408 O  O    . HOH   T 5 .   ? -23.905 -23.489 -59.123 1.00 18.63  ?  805 HOH   I O    1 
HETATM 9409 O  O    . HOH   T 5 .   ? -9.281  -66.983 -13.119 1.00 47.60  ?  806 HOH   I O    1 
HETATM 9410 O  O    . HOH   T 5 .   ? -9.570  -60.269 -50.895 1.00 40.46  ?  807 HOH   I O    1 
HETATM 9411 O  O    . HOH   T 5 .   ? -20.128 -64.400 -1.676  1.00 30.86  ?  808 HOH   I O    1 
HETATM 9412 O  O    . HOH   T 5 .   ? -31.396 -45.319 -9.279  1.00 40.41  ?  809 HOH   I O    1 
HETATM 9413 O  O    . HOH   T 5 .   ? -29.840 -50.741 -11.705 1.00 34.95  ?  810 HOH   I O    1 
HETATM 9414 O  O    . HOH   T 5 .   ? -6.353  -3.351  -41.482 1.00 29.70  ?  811 HOH   I O    1 
HETATM 9415 O  O    . HOH   T 5 .   ? -22.076 -61.352 -23.083 1.00 33.66  ?  812 HOH   I O    1 
HETATM 9416 O  O    . HOH   T 5 .   ? -26.901 -2.026  -37.069 1.00 39.68  ?  813 HOH   I O    1 
HETATM 9417 O  O    . HOH   T 5 .   ? -12.647 -59.129 -16.189 1.00 32.03  ?  814 HOH   I O    1 
HETATM 9418 O  O    . HOH   T 5 .   ? -21.970 -59.003 -24.168 1.00 21.74  ?  815 HOH   I O    1 
HETATM 9419 O  O    . HOH   T 5 .   ? -6.395  -9.493  -39.865 1.00 19.27  ?  816 HOH   I O    1 
HETATM 9420 O  O    . HOH   T 5 .   ? -2.026  -51.498 -18.502 1.00 41.67  ?  817 HOH   I O    1 
# 
