data_8XVQ
# 
_entry.id   8XVQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XVQ         pdb_00008xvq 10.2210/pdb8xvq/pdb 
WWPDB D_1300042949 ?            ?                   
# 
_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       2025-01-22 
# 
_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                        8XVQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-15 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wmmu@jiangnan.edu.cn 
_pdbx_contact_author.name_first         Wanmeng 
_pdbx_contact_author.name_last          Mu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6597-527X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, D.'    1 0000-0001-7429-4089 
'Hou, X.'   2 0000-0002-3526-8248 
'Cheng, M.' 3 0000-0003-1758-9491 
'Xu, W.'    4 0000-0001-5053-2441 
'Rao, Y.'   5 0000-0003-2481-0588 
'Mu, W.'    6 0000-0001-6597-527X 
# 
_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                     
'Structure-guided tunnel engineering to reveal the molecular basis of sugar chain extension of inulosucrase' 
_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 'Ni, D.'    1 0000-0001-7429-4089 
primary 'Hou, X.'   2 0000-0002-3526-8248 
primary 'Cheng, M.' 3 0000-0003-1758-9491 
primary 'Xu, W.'    4 0000-0001-5053-2441 
primary 'Rao, Y.'   5 0000-0003-2481-0588 
primary 'Mu, W.'    6 0000-0001-6597-527X 
# 
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 Inulosucrase          86774.883 2   2.4.1.9 ? ? ? 
2 non-polymer syn beta-D-fructofuranose 180.156   2   ?       ? ? ? 
3 non-polymer syn 'CALCIUM ION'         40.078    4   ?       ? ? ? 
4 water       nat water                 18.015    335 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Levansucrase 
# 
_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       
;MLERKEHKKMYKSGKNWAVVTLSTAALVFGATTVNASADTNIENNDSSTVQVTTGDNDIAVKSVTLGSGQVSAASDTTIR
TSANANSASSAANTQNSNSQVASSAAITSSTSSAASSNNTDSKAAQENTNTAKNDDTQKAAPANESSEAKNEPAVNVNDS
SAAKNDDQQSSKKNTTAKLNKDAENVVKKAGIDPNSLTDDQIKALNKMNFSKAAKSGTQMTYNDFQKIADTLIKQDGRYT
VPFFKASEIKNMPAATTKDAQTNTIEPLDVWDSWPVQDVRTGQVANWNGYQLVIAMMGIPNQNDNHIYLLYNKYGDNELS
HWKNVGPIFGYNSTAVSQEWSGSAVLNSDNSIQLFYTRVDTSDNNTNHQKIASATLYLTDNNGNVSLAQVANDHIVFEGD
GYYYQTYDQWKATNKGADNIAMRDAHVIEDDNGDRYLVFEASTGLENYQGEDQIYNWLNYGGDDAFNIKSLFRILSNDDI
KSRATWANAAIGILKLNKDEKNPKVAELYSPLISAPMVSDEIERPNVVKLGNKYYLFAATRLNRGSNDDAWMNANYAVGD
NVAMVGYVADSLTGSYKPLNDSGVVLTASVPANWRTATYSYYAVPVAGKDDQVLVTSYMTNRNGVAGKGMDSTWAPSFLL
QINPDNTTTVLAKMTNQGDWIWDDSSENLDMIGDLDSAALPGERDKPVDWDLIGYGLKPHDPATPNDPETPTTPETPETP
NTPKTPKTPENPGTPQTPNTPNTPEIPLTPETPKQPETQTNNRLPQTGNNANKAMIGLGMGTLLSMFGLAEINKRRFN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLERKEHKKMYKSGKNWAVVTLSTAALVFGATTVNASADTNIENNDSSTVQVTTGDNDIAVKSVTLGSGQVSAASDTTIR
TSANANSASSAANTQNSNSQVASSAAITSSTSSAASSNNTDSKAAQENTNTAKNDDTQKAAPANESSEAKNEPAVNVNDS
SAAKNDDQQSSKKNTTAKLNKDAENVVKKAGIDPNSLTDDQIKALNKMNFSKAAKSGTQMTYNDFQKIADTLIKQDGRYT
VPFFKASEIKNMPAATTKDAQTNTIEPLDVWDSWPVQDVRTGQVANWNGYQLVIAMMGIPNQNDNHIYLLYNKYGDNELS
HWKNVGPIFGYNSTAVSQEWSGSAVLNSDNSIQLFYTRVDTSDNNTNHQKIASATLYLTDNNGNVSLAQVANDHIVFEGD
GYYYQTYDQWKATNKGADNIAMRDAHVIEDDNGDRYLVFEASTGLENYQGEDQIYNWLNYGGDDAFNIKSLFRILSNDDI
KSRATWANAAIGILKLNKDEKNPKVAELYSPLISAPMVSDEIERPNVVKLGNKYYLFAATRLNRGSNDDAWMNANYAVGD
NVAMVGYVADSLTGSYKPLNDSGVVLTASVPANWRTATYSYYAVPVAGKDDQVLVTSYMTNRNGVAGKGMDSTWAPSFLL
QINPDNTTTVLAKMTNQGDWIWDDSSENLDMIGDLDSAALPGERDKPVDWDLIGYGLKPHDPATPNDPETPTTPETPETP
NTPKTPKTPENPGTPQTPNTPNTPEIPLTPETPKQPETQTNNRLPQTGNNANKAMIGLGMGTLLSMFGLAEINKRRFN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 beta-D-fructofuranose FRU 
3 'CALCIUM ION'         CA  
4 water                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LEU n 
1 3   GLU n 
1 4   ARG n 
1 5   LYS n 
1 6   GLU n 
1 7   HIS n 
1 8   LYS n 
1 9   LYS n 
1 10  MET n 
1 11  TYR n 
1 12  LYS n 
1 13  SER n 
1 14  GLY n 
1 15  LYS n 
1 16  ASN n 
1 17  TRP n 
1 18  ALA n 
1 19  VAL n 
1 20  VAL n 
1 21  THR n 
1 22  LEU n 
1 23  SER n 
1 24  THR n 
1 25  ALA n 
1 26  ALA n 
1 27  LEU n 
1 28  VAL n 
1 29  PHE n 
1 30  GLY n 
1 31  ALA n 
1 32  THR n 
1 33  THR n 
1 34  VAL n 
1 35  ASN n 
1 36  ALA n 
1 37  SER n 
1 38  ALA n 
1 39  ASP n 
1 40  THR n 
1 41  ASN n 
1 42  ILE n 
1 43  GLU n 
1 44  ASN n 
1 45  ASN n 
1 46  ASP n 
1 47  SER n 
1 48  SER n 
1 49  THR n 
1 50  VAL n 
1 51  GLN n 
1 52  VAL n 
1 53  THR n 
1 54  THR n 
1 55  GLY n 
1 56  ASP n 
1 57  ASN n 
1 58  ASP n 
1 59  ILE n 
1 60  ALA n 
1 61  VAL n 
1 62  LYS n 
1 63  SER n 
1 64  VAL n 
1 65  THR n 
1 66  LEU n 
1 67  GLY n 
1 68  SER n 
1 69  GLY n 
1 70  GLN n 
1 71  VAL n 
1 72  SER n 
1 73  ALA n 
1 74  ALA n 
1 75  SER n 
1 76  ASP n 
1 77  THR n 
1 78  THR n 
1 79  ILE n 
1 80  ARG n 
1 81  THR n 
1 82  SER n 
1 83  ALA n 
1 84  ASN n 
1 85  ALA n 
1 86  ASN n 
1 87  SER n 
1 88  ALA n 
1 89  SER n 
1 90  SER n 
1 91  ALA n 
1 92  ALA n 
1 93  ASN n 
1 94  THR n 
1 95  GLN n 
1 96  ASN n 
1 97  SER n 
1 98  ASN n 
1 99  SER n 
1 100 GLN n 
1 101 VAL n 
1 102 ALA n 
1 103 SER n 
1 104 SER n 
1 105 ALA n 
1 106 ALA n 
1 107 ILE n 
1 108 THR n 
1 109 SER n 
1 110 SER n 
1 111 THR n 
1 112 SER n 
1 113 SER n 
1 114 ALA n 
1 115 ALA n 
1 116 SER n 
1 117 SER n 
1 118 ASN n 
1 119 ASN n 
1 120 THR n 
1 121 ASP n 
1 122 SER n 
1 123 LYS n 
1 124 ALA n 
1 125 ALA n 
1 126 GLN n 
1 127 GLU n 
1 128 ASN n 
1 129 THR n 
1 130 ASN n 
1 131 THR n 
1 132 ALA n 
1 133 LYS n 
1 134 ASN n 
1 135 ASP n 
1 136 ASP n 
1 137 THR n 
1 138 GLN n 
1 139 LYS n 
1 140 ALA n 
1 141 ALA n 
1 142 PRO n 
1 143 ALA n 
1 144 ASN n 
1 145 GLU n 
1 146 SER n 
1 147 SER n 
1 148 GLU n 
1 149 ALA n 
1 150 LYS n 
1 151 ASN n 
1 152 GLU n 
1 153 PRO n 
1 154 ALA n 
1 155 VAL n 
1 156 ASN n 
1 157 VAL n 
1 158 ASN n 
1 159 ASP n 
1 160 SER n 
1 161 SER n 
1 162 ALA n 
1 163 ALA n 
1 164 LYS n 
1 165 ASN n 
1 166 ASP n 
1 167 ASP n 
1 168 GLN n 
1 169 GLN n 
1 170 SER n 
1 171 SER n 
1 172 LYS n 
1 173 LYS n 
1 174 ASN n 
1 175 THR n 
1 176 THR n 
1 177 ALA n 
1 178 LYS n 
1 179 LEU n 
1 180 ASN n 
1 181 LYS n 
1 182 ASP n 
1 183 ALA n 
1 184 GLU n 
1 185 ASN n 
1 186 VAL n 
1 187 VAL n 
1 188 LYS n 
1 189 LYS n 
1 190 ALA n 
1 191 GLY n 
1 192 ILE n 
1 193 ASP n 
1 194 PRO n 
1 195 ASN n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 ASP n 
1 200 ASP n 
1 201 GLN n 
1 202 ILE n 
1 203 LYS n 
1 204 ALA n 
1 205 LEU n 
1 206 ASN n 
1 207 LYS n 
1 208 MET n 
1 209 ASN n 
1 210 PHE n 
1 211 SER n 
1 212 LYS n 
1 213 ALA n 
1 214 ALA n 
1 215 LYS n 
1 216 SER n 
1 217 GLY n 
1 218 THR n 
1 219 GLN n 
1 220 MET n 
1 221 THR n 
1 222 TYR n 
1 223 ASN n 
1 224 ASP n 
1 225 PHE n 
1 226 GLN n 
1 227 LYS n 
1 228 ILE n 
1 229 ALA n 
1 230 ASP n 
1 231 THR n 
1 232 LEU n 
1 233 ILE n 
1 234 LYS n 
1 235 GLN n 
1 236 ASP n 
1 237 GLY n 
1 238 ARG n 
1 239 TYR n 
1 240 THR n 
1 241 VAL n 
1 242 PRO n 
1 243 PHE n 
1 244 PHE n 
1 245 LYS n 
1 246 ALA n 
1 247 SER n 
1 248 GLU n 
1 249 ILE n 
1 250 LYS n 
1 251 ASN n 
1 252 MET n 
1 253 PRO n 
1 254 ALA n 
1 255 ALA n 
1 256 THR n 
1 257 THR n 
1 258 LYS n 
1 259 ASP n 
1 260 ALA n 
1 261 GLN n 
1 262 THR n 
1 263 ASN n 
1 264 THR n 
1 265 ILE n 
1 266 GLU n 
1 267 PRO n 
1 268 LEU n 
1 269 ASP n 
1 270 VAL n 
1 271 TRP n 
1 272 ASP n 
1 273 SER n 
1 274 TRP n 
1 275 PRO n 
1 276 VAL n 
1 277 GLN n 
1 278 ASP n 
1 279 VAL n 
1 280 ARG n 
1 281 THR n 
1 282 GLY n 
1 283 GLN n 
1 284 VAL n 
1 285 ALA n 
1 286 ASN n 
1 287 TRP n 
1 288 ASN n 
1 289 GLY n 
1 290 TYR n 
1 291 GLN n 
1 292 LEU n 
1 293 VAL n 
1 294 ILE n 
1 295 ALA n 
1 296 MET n 
1 297 MET n 
1 298 GLY n 
1 299 ILE n 
1 300 PRO n 
1 301 ASN n 
1 302 GLN n 
1 303 ASN n 
1 304 ASP n 
1 305 ASN n 
1 306 HIS n 
1 307 ILE n 
1 308 TYR n 
1 309 LEU n 
1 310 LEU n 
1 311 TYR n 
1 312 ASN n 
1 313 LYS n 
1 314 TYR n 
1 315 GLY n 
1 316 ASP n 
1 317 ASN n 
1 318 GLU n 
1 319 LEU n 
1 320 SER n 
1 321 HIS n 
1 322 TRP n 
1 323 LYS n 
1 324 ASN n 
1 325 VAL n 
1 326 GLY n 
1 327 PRO n 
1 328 ILE n 
1 329 PHE n 
1 330 GLY n 
1 331 TYR n 
1 332 ASN n 
1 333 SER n 
1 334 THR n 
1 335 ALA n 
1 336 VAL n 
1 337 SER n 
1 338 GLN n 
1 339 GLU n 
1 340 TRP n 
1 341 SER n 
1 342 GLY n 
1 343 SER n 
1 344 ALA n 
1 345 VAL n 
1 346 LEU n 
1 347 ASN n 
1 348 SER n 
1 349 ASP n 
1 350 ASN n 
1 351 SER n 
1 352 ILE n 
1 353 GLN n 
1 354 LEU n 
1 355 PHE n 
1 356 TYR n 
1 357 THR n 
1 358 ARG n 
1 359 VAL n 
1 360 ASP n 
1 361 THR n 
1 362 SER n 
1 363 ASP n 
1 364 ASN n 
1 365 ASN n 
1 366 THR n 
1 367 ASN n 
1 368 HIS n 
1 369 GLN n 
1 370 LYS n 
1 371 ILE n 
1 372 ALA n 
1 373 SER n 
1 374 ALA n 
1 375 THR n 
1 376 LEU n 
1 377 TYR n 
1 378 LEU n 
1 379 THR n 
1 380 ASP n 
1 381 ASN n 
1 382 ASN n 
1 383 GLY n 
1 384 ASN n 
1 385 VAL n 
1 386 SER n 
1 387 LEU n 
1 388 ALA n 
1 389 GLN n 
1 390 VAL n 
1 391 ALA n 
1 392 ASN n 
1 393 ASP n 
1 394 HIS n 
1 395 ILE n 
1 396 VAL n 
1 397 PHE n 
1 398 GLU n 
1 399 GLY n 
1 400 ASP n 
1 401 GLY n 
1 402 TYR n 
1 403 TYR n 
1 404 TYR n 
1 405 GLN n 
1 406 THR n 
1 407 TYR n 
1 408 ASP n 
1 409 GLN n 
1 410 TRP n 
1 411 LYS n 
1 412 ALA n 
1 413 THR n 
1 414 ASN n 
1 415 LYS n 
1 416 GLY n 
1 417 ALA n 
1 418 ASP n 
1 419 ASN n 
1 420 ILE n 
1 421 ALA n 
1 422 MET n 
1 423 ARG n 
1 424 ASP n 
1 425 ALA n 
1 426 HIS n 
1 427 VAL n 
1 428 ILE n 
1 429 GLU n 
1 430 ASP n 
1 431 ASP n 
1 432 ASN n 
1 433 GLY n 
1 434 ASP n 
1 435 ARG n 
1 436 TYR n 
1 437 LEU n 
1 438 VAL n 
1 439 PHE n 
1 440 GLU n 
1 441 ALA n 
1 442 SER n 
1 443 THR n 
1 444 GLY n 
1 445 LEU n 
1 446 GLU n 
1 447 ASN n 
1 448 TYR n 
1 449 GLN n 
1 450 GLY n 
1 451 GLU n 
1 452 ASP n 
1 453 GLN n 
1 454 ILE n 
1 455 TYR n 
1 456 ASN n 
1 457 TRP n 
1 458 LEU n 
1 459 ASN n 
1 460 TYR n 
1 461 GLY n 
1 462 GLY n 
1 463 ASP n 
1 464 ASP n 
1 465 ALA n 
1 466 PHE n 
1 467 ASN n 
1 468 ILE n 
1 469 LYS n 
1 470 SER n 
1 471 LEU n 
1 472 PHE n 
1 473 ARG n 
1 474 ILE n 
1 475 LEU n 
1 476 SER n 
1 477 ASN n 
1 478 ASP n 
1 479 ASP n 
1 480 ILE n 
1 481 LYS n 
1 482 SER n 
1 483 ARG n 
1 484 ALA n 
1 485 THR n 
1 486 TRP n 
1 487 ALA n 
1 488 ASN n 
1 489 ALA n 
1 490 ALA n 
1 491 ILE n 
1 492 GLY n 
1 493 ILE n 
1 494 LEU n 
1 495 LYS n 
1 496 LEU n 
1 497 ASN n 
1 498 LYS n 
1 499 ASP n 
1 500 GLU n 
1 501 LYS n 
1 502 ASN n 
1 503 PRO n 
1 504 LYS n 
1 505 VAL n 
1 506 ALA n 
1 507 GLU n 
1 508 LEU n 
1 509 TYR n 
1 510 SER n 
1 511 PRO n 
1 512 LEU n 
1 513 ILE n 
1 514 SER n 
1 515 ALA n 
1 516 PRO n 
1 517 MET n 
1 518 VAL n 
1 519 SER n 
1 520 ASP n 
1 521 GLU n 
1 522 ILE n 
1 523 GLU n 
1 524 ARG n 
1 525 PRO n 
1 526 ASN n 
1 527 VAL n 
1 528 VAL n 
1 529 LYS n 
1 530 LEU n 
1 531 GLY n 
1 532 ASN n 
1 533 LYS n 
1 534 TYR n 
1 535 TYR n 
1 536 LEU n 
1 537 PHE n 
1 538 ALA n 
1 539 ALA n 
1 540 THR n 
1 541 ARG n 
1 542 LEU n 
1 543 ASN n 
1 544 ARG n 
1 545 GLY n 
1 546 SER n 
1 547 ASN n 
1 548 ASP n 
1 549 ASP n 
1 550 ALA n 
1 551 TRP n 
1 552 MET n 
1 553 ASN n 
1 554 ALA n 
1 555 ASN n 
1 556 TYR n 
1 557 ALA n 
1 558 VAL n 
1 559 GLY n 
1 560 ASP n 
1 561 ASN n 
1 562 VAL n 
1 563 ALA n 
1 564 MET n 
1 565 VAL n 
1 566 GLY n 
1 567 TYR n 
1 568 VAL n 
1 569 ALA n 
1 570 ASP n 
1 571 SER n 
1 572 LEU n 
1 573 THR n 
1 574 GLY n 
1 575 SER n 
1 576 TYR n 
1 577 LYS n 
1 578 PRO n 
1 579 LEU n 
1 580 ASN n 
1 581 ASP n 
1 582 SER n 
1 583 GLY n 
1 584 VAL n 
1 585 VAL n 
1 586 LEU n 
1 587 THR n 
1 588 ALA n 
1 589 SER n 
1 590 VAL n 
1 591 PRO n 
1 592 ALA n 
1 593 ASN n 
1 594 TRP n 
1 595 ARG n 
1 596 THR n 
1 597 ALA n 
1 598 THR n 
1 599 TYR n 
1 600 SER n 
1 601 TYR n 
1 602 TYR n 
1 603 ALA n 
1 604 VAL n 
1 605 PRO n 
1 606 VAL n 
1 607 ALA n 
1 608 GLY n 
1 609 LYS n 
1 610 ASP n 
1 611 ASP n 
1 612 GLN n 
1 613 VAL n 
1 614 LEU n 
1 615 VAL n 
1 616 THR n 
1 617 SER n 
1 618 TYR n 
1 619 MET n 
1 620 THR n 
1 621 ASN n 
1 622 ARG n 
1 623 ASN n 
1 624 GLY n 
1 625 VAL n 
1 626 ALA n 
1 627 GLY n 
1 628 LYS n 
1 629 GLY n 
1 630 MET n 
1 631 ASP n 
1 632 SER n 
1 633 THR n 
1 634 TRP n 
1 635 ALA n 
1 636 PRO n 
1 637 SER n 
1 638 PHE n 
1 639 LEU n 
1 640 LEU n 
1 641 GLN n 
1 642 ILE n 
1 643 ASN n 
1 644 PRO n 
1 645 ASP n 
1 646 ASN n 
1 647 THR n 
1 648 THR n 
1 649 THR n 
1 650 VAL n 
1 651 LEU n 
1 652 ALA n 
1 653 LYS n 
1 654 MET n 
1 655 THR n 
1 656 ASN n 
1 657 GLN n 
1 658 GLY n 
1 659 ASP n 
1 660 TRP n 
1 661 ILE n 
1 662 TRP n 
1 663 ASP n 
1 664 ASP n 
1 665 SER n 
1 666 SER n 
1 667 GLU n 
1 668 ASN n 
1 669 LEU n 
1 670 ASP n 
1 671 MET n 
1 672 ILE n 
1 673 GLY n 
1 674 ASP n 
1 675 LEU n 
1 676 ASP n 
1 677 SER n 
1 678 ALA n 
1 679 ALA n 
1 680 LEU n 
1 681 PRO n 
1 682 GLY n 
1 683 GLU n 
1 684 ARG n 
1 685 ASP n 
1 686 LYS n 
1 687 PRO n 
1 688 VAL n 
1 689 ASP n 
1 690 TRP n 
1 691 ASP n 
1 692 LEU n 
1 693 ILE n 
1 694 GLY n 
1 695 TYR n 
1 696 GLY n 
1 697 LEU n 
1 698 LYS n 
1 699 PRO n 
1 700 HIS n 
1 701 ASP n 
1 702 PRO n 
1 703 ALA n 
1 704 THR n 
1 705 PRO n 
1 706 ASN n 
1 707 ASP n 
1 708 PRO n 
1 709 GLU n 
1 710 THR n 
1 711 PRO n 
1 712 THR n 
1 713 THR n 
1 714 PRO n 
1 715 GLU n 
1 716 THR n 
1 717 PRO n 
1 718 GLU n 
1 719 THR n 
1 720 PRO n 
1 721 ASN n 
1 722 THR n 
1 723 PRO n 
1 724 LYS n 
1 725 THR n 
1 726 PRO n 
1 727 LYS n 
1 728 THR n 
1 729 PRO n 
1 730 GLU n 
1 731 ASN n 
1 732 PRO n 
1 733 GLY n 
1 734 THR n 
1 735 PRO n 
1 736 GLN n 
1 737 THR n 
1 738 PRO n 
1 739 ASN n 
1 740 THR n 
1 741 PRO n 
1 742 ASN n 
1 743 THR n 
1 744 PRO n 
1 745 GLU n 
1 746 ILE n 
1 747 PRO n 
1 748 LEU n 
1 749 THR n 
1 750 PRO n 
1 751 GLU n 
1 752 THR n 
1 753 PRO n 
1 754 LYS n 
1 755 GLN n 
1 756 PRO n 
1 757 GLU n 
1 758 THR n 
1 759 GLN n 
1 760 THR n 
1 761 ASN n 
1 762 ASN n 
1 763 ARG n 
1 764 LEU n 
1 765 PRO n 
1 766 GLN n 
1 767 THR n 
1 768 GLY n 
1 769 ASN n 
1 770 ASN n 
1 771 ALA n 
1 772 ASN n 
1 773 LYS n 
1 774 ALA n 
1 775 MET n 
1 776 ILE n 
1 777 GLY n 
1 778 LEU n 
1 779 GLY n 
1 780 MET n 
1 781 GLY n 
1 782 THR n 
1 783 LEU n 
1 784 LEU n 
1 785 SER n 
1 786 MET n 
1 787 PHE n 
1 788 GLY n 
1 789 LEU n 
1 790 ALA n 
1 791 GLU n 
1 792 ILE n 
1 793 ASN n 
1 794 LYS n 
1 795 ARG n 
1 796 ARG n 
1 797 PHE n 
1 798 ASN 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                   798 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'inu, DPH67_05265' 
_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      'Limosilactobacillus reuteri' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1598 
_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 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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 
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 
CA  non-polymer                  . 'CALCIUM ION'         ?                                       'Ca 2'           40.078  
FRU 'D-saccharide, beta linking' . beta-D-fructofuranose 'beta-D-fructose; D-fructose; fructose' 'C6 H12 O6'      180.156 
GLN 'L-peptide linking'          y GLUTAMINE             ?                                       'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'       ?                                       'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE               ?                                       'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE             ?                                       'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                 ?                                       'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE            ?                                       'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE               ?                                       'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                ?                                       'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE            ?                                       'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'          y PHENYLALANINE         ?                                       'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE               ?                                       'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                ?                                       'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE             ?                                       'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN            ?                                       'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE              ?                                       'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                ?                                       'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
FRU 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DFrufb             
FRU 'COMMON NAME'                         GMML     1.0 b-D-fructofuranose 
FRU 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Fruf           
FRU 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fru                
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LEU 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   LYS 5   5   ?   ?   ?   A . n 
A 1 6   GLU 6   6   ?   ?   ?   A . n 
A 1 7   HIS 7   7   ?   ?   ?   A . n 
A 1 8   LYS 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   ?   ?   ?   A . n 
A 1 10  MET 10  10  ?   ?   ?   A . n 
A 1 11  TYR 11  11  ?   ?   ?   A . n 
A 1 12  LYS 12  12  ?   ?   ?   A . n 
A 1 13  SER 13  13  ?   ?   ?   A . n 
A 1 14  GLY 14  14  ?   ?   ?   A . n 
A 1 15  LYS 15  15  ?   ?   ?   A . n 
A 1 16  ASN 16  16  ?   ?   ?   A . n 
A 1 17  TRP 17  17  ?   ?   ?   A . n 
A 1 18  ALA 18  18  ?   ?   ?   A . n 
A 1 19  VAL 19  19  ?   ?   ?   A . n 
A 1 20  VAL 20  20  ?   ?   ?   A . n 
A 1 21  THR 21  21  ?   ?   ?   A . n 
A 1 22  LEU 22  22  ?   ?   ?   A . n 
A 1 23  SER 23  23  ?   ?   ?   A . n 
A 1 24  THR 24  24  ?   ?   ?   A . n 
A 1 25  ALA 25  25  ?   ?   ?   A . n 
A 1 26  ALA 26  26  ?   ?   ?   A . n 
A 1 27  LEU 27  27  ?   ?   ?   A . n 
A 1 28  VAL 28  28  ?   ?   ?   A . n 
A 1 29  PHE 29  29  ?   ?   ?   A . n 
A 1 30  GLY 30  30  ?   ?   ?   A . n 
A 1 31  ALA 31  31  ?   ?   ?   A . n 
A 1 32  THR 32  32  ?   ?   ?   A . n 
A 1 33  THR 33  33  ?   ?   ?   A . n 
A 1 34  VAL 34  34  ?   ?   ?   A . n 
A 1 35  ASN 35  35  ?   ?   ?   A . n 
A 1 36  ALA 36  36  ?   ?   ?   A . n 
A 1 37  SER 37  37  ?   ?   ?   A . n 
A 1 38  ALA 38  38  ?   ?   ?   A . n 
A 1 39  ASP 39  39  ?   ?   ?   A . n 
A 1 40  THR 40  40  ?   ?   ?   A . n 
A 1 41  ASN 41  41  ?   ?   ?   A . n 
A 1 42  ILE 42  42  ?   ?   ?   A . n 
A 1 43  GLU 43  43  ?   ?   ?   A . n 
A 1 44  ASN 44  44  ?   ?   ?   A . n 
A 1 45  ASN 45  45  ?   ?   ?   A . n 
A 1 46  ASP 46  46  ?   ?   ?   A . n 
A 1 47  SER 47  47  ?   ?   ?   A . n 
A 1 48  SER 48  48  ?   ?   ?   A . n 
A 1 49  THR 49  49  ?   ?   ?   A . n 
A 1 50  VAL 50  50  ?   ?   ?   A . n 
A 1 51  GLN 51  51  ?   ?   ?   A . n 
A 1 52  VAL 52  52  ?   ?   ?   A . n 
A 1 53  THR 53  53  ?   ?   ?   A . n 
A 1 54  THR 54  54  ?   ?   ?   A . n 
A 1 55  GLY 55  55  ?   ?   ?   A . n 
A 1 56  ASP 56  56  ?   ?   ?   A . n 
A 1 57  ASN 57  57  ?   ?   ?   A . n 
A 1 58  ASP 58  58  ?   ?   ?   A . n 
A 1 59  ILE 59  59  ?   ?   ?   A . n 
A 1 60  ALA 60  60  ?   ?   ?   A . n 
A 1 61  VAL 61  61  ?   ?   ?   A . n 
A 1 62  LYS 62  62  ?   ?   ?   A . n 
A 1 63  SER 63  63  ?   ?   ?   A . n 
A 1 64  VAL 64  64  ?   ?   ?   A . n 
A 1 65  THR 65  65  ?   ?   ?   A . n 
A 1 66  LEU 66  66  ?   ?   ?   A . n 
A 1 67  GLY 67  67  ?   ?   ?   A . n 
A 1 68  SER 68  68  ?   ?   ?   A . n 
A 1 69  GLY 69  69  ?   ?   ?   A . n 
A 1 70  GLN 70  70  ?   ?   ?   A . n 
A 1 71  VAL 71  71  ?   ?   ?   A . n 
A 1 72  SER 72  72  ?   ?   ?   A . n 
A 1 73  ALA 73  73  ?   ?   ?   A . n 
A 1 74  ALA 74  74  ?   ?   ?   A . n 
A 1 75  SER 75  75  ?   ?   ?   A . n 
A 1 76  ASP 76  76  ?   ?   ?   A . n 
A 1 77  THR 77  77  ?   ?   ?   A . n 
A 1 78  THR 78  78  ?   ?   ?   A . n 
A 1 79  ILE 79  79  ?   ?   ?   A . n 
A 1 80  ARG 80  80  ?   ?   ?   A . n 
A 1 81  THR 81  81  ?   ?   ?   A . n 
A 1 82  SER 82  82  ?   ?   ?   A . n 
A 1 83  ALA 83  83  ?   ?   ?   A . n 
A 1 84  ASN 84  84  ?   ?   ?   A . n 
A 1 85  ALA 85  85  ?   ?   ?   A . n 
A 1 86  ASN 86  86  ?   ?   ?   A . n 
A 1 87  SER 87  87  ?   ?   ?   A . n 
A 1 88  ALA 88  88  ?   ?   ?   A . n 
A 1 89  SER 89  89  ?   ?   ?   A . n 
A 1 90  SER 90  90  ?   ?   ?   A . n 
A 1 91  ALA 91  91  ?   ?   ?   A . n 
A 1 92  ALA 92  92  ?   ?   ?   A . n 
A 1 93  ASN 93  93  ?   ?   ?   A . n 
A 1 94  THR 94  94  ?   ?   ?   A . n 
A 1 95  GLN 95  95  ?   ?   ?   A . n 
A 1 96  ASN 96  96  ?   ?   ?   A . n 
A 1 97  SER 97  97  ?   ?   ?   A . n 
A 1 98  ASN 98  98  ?   ?   ?   A . n 
A 1 99  SER 99  99  ?   ?   ?   A . n 
A 1 100 GLN 100 100 ?   ?   ?   A . n 
A 1 101 VAL 101 101 ?   ?   ?   A . n 
A 1 102 ALA 102 102 ?   ?   ?   A . n 
A 1 103 SER 103 103 ?   ?   ?   A . n 
A 1 104 SER 104 104 ?   ?   ?   A . n 
A 1 105 ALA 105 105 ?   ?   ?   A . n 
A 1 106 ALA 106 106 ?   ?   ?   A . n 
A 1 107 ILE 107 107 ?   ?   ?   A . n 
A 1 108 THR 108 108 ?   ?   ?   A . n 
A 1 109 SER 109 109 ?   ?   ?   A . n 
A 1 110 SER 110 110 ?   ?   ?   A . n 
A 1 111 THR 111 111 ?   ?   ?   A . n 
A 1 112 SER 112 112 ?   ?   ?   A . n 
A 1 113 SER 113 113 ?   ?   ?   A . n 
A 1 114 ALA 114 114 ?   ?   ?   A . n 
A 1 115 ALA 115 115 ?   ?   ?   A . n 
A 1 116 SER 116 116 ?   ?   ?   A . n 
A 1 117 SER 117 117 ?   ?   ?   A . n 
A 1 118 ASN 118 118 ?   ?   ?   A . n 
A 1 119 ASN 119 119 ?   ?   ?   A . n 
A 1 120 THR 120 120 ?   ?   ?   A . n 
A 1 121 ASP 121 121 ?   ?   ?   A . n 
A 1 122 SER 122 122 ?   ?   ?   A . n 
A 1 123 LYS 123 123 ?   ?   ?   A . n 
A 1 124 ALA 124 124 ?   ?   ?   A . n 
A 1 125 ALA 125 125 ?   ?   ?   A . n 
A 1 126 GLN 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
A 1 128 ASN 128 128 ?   ?   ?   A . n 
A 1 129 THR 129 129 ?   ?   ?   A . n 
A 1 130 ASN 130 130 ?   ?   ?   A . n 
A 1 131 THR 131 131 ?   ?   ?   A . n 
A 1 132 ALA 132 132 ?   ?   ?   A . n 
A 1 133 LYS 133 133 ?   ?   ?   A . n 
A 1 134 ASN 134 134 ?   ?   ?   A . n 
A 1 135 ASP 135 135 ?   ?   ?   A . n 
A 1 136 ASP 136 136 ?   ?   ?   A . n 
A 1 137 THR 137 137 ?   ?   ?   A . n 
A 1 138 GLN 138 138 ?   ?   ?   A . n 
A 1 139 LYS 139 139 ?   ?   ?   A . n 
A 1 140 ALA 140 140 ?   ?   ?   A . n 
A 1 141 ALA 141 141 ?   ?   ?   A . n 
A 1 142 PRO 142 142 ?   ?   ?   A . n 
A 1 143 ALA 143 143 ?   ?   ?   A . n 
A 1 144 ASN 144 144 ?   ?   ?   A . n 
A 1 145 GLU 145 145 ?   ?   ?   A . n 
A 1 146 SER 146 146 ?   ?   ?   A . n 
A 1 147 SER 147 147 ?   ?   ?   A . n 
A 1 148 GLU 148 148 ?   ?   ?   A . n 
A 1 149 ALA 149 149 ?   ?   ?   A . n 
A 1 150 LYS 150 150 ?   ?   ?   A . n 
A 1 151 ASN 151 151 ?   ?   ?   A . n 
A 1 152 GLU 152 152 ?   ?   ?   A . n 
A 1 153 PRO 153 153 ?   ?   ?   A . n 
A 1 154 ALA 154 154 ?   ?   ?   A . n 
A 1 155 VAL 155 155 ?   ?   ?   A . n 
A 1 156 ASN 156 156 ?   ?   ?   A . n 
A 1 157 VAL 157 157 ?   ?   ?   A . n 
A 1 158 ASN 158 158 ?   ?   ?   A . n 
A 1 159 ASP 159 159 ?   ?   ?   A . n 
A 1 160 SER 160 160 ?   ?   ?   A . n 
A 1 161 SER 161 161 ?   ?   ?   A . n 
A 1 162 ALA 162 162 ?   ?   ?   A . n 
A 1 163 ALA 163 163 ?   ?   ?   A . n 
A 1 164 LYS 164 164 ?   ?   ?   A . n 
A 1 165 ASN 165 165 ?   ?   ?   A . n 
A 1 166 ASP 166 166 ?   ?   ?   A . n 
A 1 167 ASP 167 167 ?   ?   ?   A . n 
A 1 168 GLN 168 168 ?   ?   ?   A . n 
A 1 169 GLN 169 169 ?   ?   ?   A . n 
A 1 170 SER 170 170 ?   ?   ?   A . n 
A 1 171 SER 171 171 ?   ?   ?   A . n 
A 1 172 LYS 172 172 ?   ?   ?   A . n 
A 1 173 LYS 173 173 ?   ?   ?   A . n 
A 1 174 ASN 174 174 ?   ?   ?   A . n 
A 1 175 THR 175 175 ?   ?   ?   A . n 
A 1 176 THR 176 176 ?   ?   ?   A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 GLN 201 201 201 GLN GLN A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 MET 208 208 208 MET MET A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 MET 220 220 220 MET MET A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 TYR 222 222 222 TYR TYR A . n 
A 1 223 ASN 223 223 223 ASN ASN A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 GLN 226 226 226 GLN GLN A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 ILE 228 228 228 ILE ILE A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 ILE 233 233 233 ILE ILE A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 GLN 235 235 235 GLN GLN A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 THR 256 256 256 THR THR A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 GLN 261 261 261 GLN GLN A . n 
A 1 262 THR 262 262 262 THR THR A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 PRO 267 267 267 PRO PRO A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 ASP 269 269 269 ASP ASP A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 TRP 271 271 271 TRP TRP A . n 
A 1 272 ASP 272 272 272 ASP ASP A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 TRP 274 274 274 TRP TRP A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 GLN 283 283 283 GLN GLN A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 ASN 286 286 286 ASN ASN A . n 
A 1 287 TRP 287 287 287 TRP TRP A . n 
A 1 288 ASN 288 288 288 ASN ASN A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 MET 296 296 296 MET MET A . n 
A 1 297 MET 297 297 297 MET MET A . n 
A 1 298 GLY 298 298 298 GLY GLY A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 GLN 302 302 302 GLN GLN A . n 
A 1 303 ASN 303 303 303 ASN ASN A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 ASN 305 305 305 ASN ASN A . n 
A 1 306 HIS 306 306 306 HIS HIS A . n 
A 1 307 ILE 307 307 307 ILE ILE A . n 
A 1 308 TYR 308 308 308 TYR TYR A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 ASN 312 312 312 ASN ASN A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 TYR 314 314 314 TYR TYR A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ASP 316 316 316 ASP ASP A . n 
A 1 317 ASN 317 317 317 ASN ASN A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 SER 320 320 320 SER SER A . n 
A 1 321 HIS 321 321 321 HIS HIS A . n 
A 1 322 TRP 322 322 322 TRP TRP A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 PHE 329 329 329 PHE PHE A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 TYR 331 331 331 TYR TYR A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 THR 334 334 334 THR THR A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 VAL 336 336 336 VAL VAL A . n 
A 1 337 SER 337 337 337 SER SER A . n 
A 1 338 GLN 338 338 338 GLN GLN A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 TRP 340 340 340 TRP TRP A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 VAL 345 345 345 VAL VAL A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ASN 347 347 347 ASN ASN A . n 
A 1 348 SER 348 348 348 SER SER A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 ASN 350 350 350 ASN ASN A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 GLN 353 353 353 GLN GLN A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 TYR 356 356 356 TYR TYR A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 ARG 358 358 358 ARG ARG A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 ASP 360 360 360 ASP ASP A . n 
A 1 361 THR 361 361 361 THR THR A . n 
A 1 362 SER 362 362 362 SER SER A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 ASN 367 367 367 ASN ASN A . n 
A 1 368 HIS 368 368 368 HIS HIS A . n 
A 1 369 GLN 369 369 369 GLN GLN A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 ILE 371 371 371 ILE ILE A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 THR 379 379 379 THR THR A . n 
A 1 380 ASP 380 380 380 ASP ASP A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 ASN 382 382 382 ASN ASN A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 GLN 389 389 389 GLN GLN A . n 
A 1 390 VAL 390 390 390 VAL VAL A . n 
A 1 391 ALA 391 391 391 ALA ALA A . n 
A 1 392 ASN 392 392 392 ASN ASN A . n 
A 1 393 ASP 393 393 393 ASP ASP A . n 
A 1 394 HIS 394 394 394 HIS HIS A . n 
A 1 395 ILE 395 395 395 ILE ILE A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 GLY 399 399 399 GLY GLY A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 TYR 402 402 402 TYR TYR A . n 
A 1 403 TYR 403 403 403 TYR TYR A . n 
A 1 404 TYR 404 404 404 TYR TYR A . n 
A 1 405 GLN 405 405 405 GLN GLN A . n 
A 1 406 THR 406 406 406 THR THR A . n 
A 1 407 TYR 407 407 407 TYR TYR A . n 
A 1 408 ASP 408 408 408 ASP ASP A . n 
A 1 409 GLN 409 409 409 GLN GLN A . n 
A 1 410 TRP 410 410 410 TRP TRP A . n 
A 1 411 LYS 411 411 411 LYS LYS A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 THR 413 413 413 THR THR A . n 
A 1 414 ASN 414 414 414 ASN ASN A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 ALA 417 417 417 ALA ALA A . n 
A 1 418 ASP 418 418 418 ASP ASP A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 ILE 420 420 420 ILE ILE A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 MET 422 422 422 MET MET A . n 
A 1 423 ARG 423 423 423 ARG ARG A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 ALA 425 425 425 ALA ALA A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 ASP 430 430 430 ASP ASP A . n 
A 1 431 ASP 431 431 431 ASP ASP A . n 
A 1 432 ASN 432 432 432 ASN ASN A . n 
A 1 433 GLY 433 433 433 GLY GLY A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 ARG 435 435 435 ARG ARG A . n 
A 1 436 TYR 436 436 436 TYR TYR A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 VAL 438 438 438 VAL VAL A . n 
A 1 439 PHE 439 439 439 PHE PHE A . n 
A 1 440 GLU 440 440 440 GLU GLU A . n 
A 1 441 ALA 441 441 441 ALA ALA A . n 
A 1 442 SER 442 442 442 SER SER A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 GLY 444 444 444 GLY GLY A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 TYR 448 448 448 TYR TYR A . n 
A 1 449 GLN 449 449 449 GLN GLN A . n 
A 1 450 GLY 450 450 450 GLY GLY A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 ASP 452 452 452 ASP ASP A . n 
A 1 453 GLN 453 453 453 GLN GLN A . n 
A 1 454 ILE 454 454 454 ILE ILE A . n 
A 1 455 TYR 455 455 455 TYR TYR A . n 
A 1 456 ASN 456 456 456 ASN ASN A . n 
A 1 457 TRP 457 457 457 TRP TRP A . n 
A 1 458 LEU 458 458 458 LEU LEU A . n 
A 1 459 ASN 459 459 459 ASN ASN A . n 
A 1 460 TYR 460 460 460 TYR TYR A . n 
A 1 461 GLY 461 461 461 GLY GLY A . n 
A 1 462 GLY 462 462 462 GLY GLY A . n 
A 1 463 ASP 463 463 463 ASP ASP A . n 
A 1 464 ASP 464 464 464 ASP ASP A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 PHE 466 466 466 PHE PHE A . n 
A 1 467 ASN 467 467 467 ASN ASN A . n 
A 1 468 ILE 468 468 468 ILE ILE A . n 
A 1 469 LYS 469 469 469 LYS LYS A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 LEU 471 471 471 LEU LEU A . n 
A 1 472 PHE 472 472 472 PHE PHE A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 ILE 474 474 474 ILE ILE A . n 
A 1 475 LEU 475 475 475 LEU LEU A . n 
A 1 476 SER 476 476 476 SER SER A . n 
A 1 477 ASN 477 477 477 ASN ASN A . n 
A 1 478 ASP 478 478 478 ASP ASP A . n 
A 1 479 ASP 479 479 479 ASP ASP A . n 
A 1 480 ILE 480 480 480 ILE ILE A . n 
A 1 481 LYS 481 481 481 LYS LYS A . n 
A 1 482 SER 482 482 482 SER SER A . n 
A 1 483 ARG 483 483 483 ARG ARG A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 THR 485 485 485 THR THR A . n 
A 1 486 TRP 486 486 486 TRP TRP A . n 
A 1 487 ALA 487 487 487 ALA ALA A . n 
A 1 488 ASN 488 488 488 ASN ASN A . n 
A 1 489 ALA 489 489 489 ALA ALA A . n 
A 1 490 ALA 490 490 490 ALA ALA A . n 
A 1 491 ILE 491 491 491 ILE ILE A . n 
A 1 492 GLY 492 492 492 GLY GLY A . n 
A 1 493 ILE 493 493 493 ILE ILE A . n 
A 1 494 LEU 494 494 494 LEU LEU A . n 
A 1 495 LYS 495 495 495 LYS LYS A . n 
A 1 496 LEU 496 496 496 LEU LEU A . n 
A 1 497 ASN 497 497 497 ASN ASN A . n 
A 1 498 LYS 498 498 498 LYS LYS A . n 
A 1 499 ASP 499 499 499 ASP ASP A . n 
A 1 500 GLU 500 500 500 GLU GLU A . n 
A 1 501 LYS 501 501 501 LYS LYS A . n 
A 1 502 ASN 502 502 502 ASN ASN A . n 
A 1 503 PRO 503 503 503 PRO PRO A . n 
A 1 504 LYS 504 504 504 LYS LYS A . n 
A 1 505 VAL 505 505 505 VAL VAL A . n 
A 1 506 ALA 506 506 506 ALA ALA A . n 
A 1 507 GLU 507 507 507 GLU GLU A . n 
A 1 508 LEU 508 508 508 LEU LEU A . n 
A 1 509 TYR 509 509 509 TYR TYR A . n 
A 1 510 SER 510 510 510 SER SER A . n 
A 1 511 PRO 511 511 511 PRO PRO A . n 
A 1 512 LEU 512 512 512 LEU LEU A . n 
A 1 513 ILE 513 513 513 ILE ILE A . n 
A 1 514 SER 514 514 514 SER SER A . n 
A 1 515 ALA 515 515 515 ALA ALA A . n 
A 1 516 PRO 516 516 516 PRO PRO A . n 
A 1 517 MET 517 517 517 MET MET A . n 
A 1 518 VAL 518 518 518 VAL VAL A . n 
A 1 519 SER 519 519 519 SER SER A . n 
A 1 520 ASP 520 520 520 ASP ASP A . n 
A 1 521 GLU 521 521 521 GLU GLU A . n 
A 1 522 ILE 522 522 522 ILE ILE A . n 
A 1 523 GLU 523 523 523 GLU GLU A . n 
A 1 524 ARG 524 524 524 ARG ARG A . n 
A 1 525 PRO 525 525 525 PRO PRO A . n 
A 1 526 ASN 526 526 526 ASN ASN A . n 
A 1 527 VAL 527 527 527 VAL VAL A . n 
A 1 528 VAL 528 528 528 VAL VAL A . n 
A 1 529 LYS 529 529 529 LYS LYS A . n 
A 1 530 LEU 530 530 530 LEU LEU A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 ASN 532 532 532 ASN ASN A . n 
A 1 533 LYS 533 533 533 LYS LYS A . n 
A 1 534 TYR 534 534 534 TYR TYR A . n 
A 1 535 TYR 535 535 535 TYR TYR A . n 
A 1 536 LEU 536 536 536 LEU LEU A . n 
A 1 537 PHE 537 537 537 PHE PHE A . n 
A 1 538 ALA 538 538 538 ALA ALA A . n 
A 1 539 ALA 539 539 539 ALA ALA A . n 
A 1 540 THR 540 540 540 THR THR A . n 
A 1 541 ARG 541 541 541 ARG ARG A . n 
A 1 542 LEU 542 542 542 LEU LEU A . n 
A 1 543 ASN 543 543 543 ASN ASN A . n 
A 1 544 ARG 544 544 544 ARG ARG A . n 
A 1 545 GLY 545 545 545 GLY GLY A . n 
A 1 546 SER 546 546 546 SER SER A . n 
A 1 547 ASN 547 547 547 ASN ASN A . n 
A 1 548 ASP 548 548 548 ASP ASP A . n 
A 1 549 ASP 549 549 549 ASP ASP A . n 
A 1 550 ALA 550 550 550 ALA ALA A . n 
A 1 551 TRP 551 551 551 TRP TRP A . n 
A 1 552 MET 552 552 552 MET MET A . n 
A 1 553 ASN 553 553 553 ASN ASN A . n 
A 1 554 ALA 554 554 554 ALA ALA A . n 
A 1 555 ASN 555 555 555 ASN ASN A . n 
A 1 556 TYR 556 556 556 TYR TYR A . n 
A 1 557 ALA 557 557 557 ALA ALA A . n 
A 1 558 VAL 558 558 558 VAL VAL A . n 
A 1 559 GLY 559 559 559 GLY GLY A . n 
A 1 560 ASP 560 560 560 ASP ASP A . n 
A 1 561 ASN 561 561 561 ASN ASN A . n 
A 1 562 VAL 562 562 562 VAL VAL A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 MET 564 564 564 MET MET A . n 
A 1 565 VAL 565 565 565 VAL VAL A . n 
A 1 566 GLY 566 566 566 GLY GLY A . n 
A 1 567 TYR 567 567 567 TYR TYR A . n 
A 1 568 VAL 568 568 568 VAL VAL A . n 
A 1 569 ALA 569 569 569 ALA ALA A . n 
A 1 570 ASP 570 570 570 ASP ASP A . n 
A 1 571 SER 571 571 571 SER SER A . n 
A 1 572 LEU 572 572 572 LEU LEU A . n 
A 1 573 THR 573 573 573 THR THR A . n 
A 1 574 GLY 574 574 574 GLY GLY A . n 
A 1 575 SER 575 575 575 SER SER A . n 
A 1 576 TYR 576 576 576 TYR TYR A . n 
A 1 577 LYS 577 577 577 LYS LYS A . n 
A 1 578 PRO 578 578 578 PRO PRO A . n 
A 1 579 LEU 579 579 579 LEU LEU A . n 
A 1 580 ASN 580 580 580 ASN ASN A . n 
A 1 581 ASP 581 581 581 ASP ASP A . n 
A 1 582 SER 582 582 582 SER SER A . n 
A 1 583 GLY 583 583 583 GLY GLY A . n 
A 1 584 VAL 584 584 584 VAL VAL A . n 
A 1 585 VAL 585 585 585 VAL VAL A . n 
A 1 586 LEU 586 586 586 LEU LEU A . n 
A 1 587 THR 587 587 587 THR THR A . n 
A 1 588 ALA 588 588 588 ALA ALA A . n 
A 1 589 SER 589 589 589 SER SER A . n 
A 1 590 VAL 590 590 590 VAL VAL A . n 
A 1 591 PRO 591 591 591 PRO PRO A . n 
A 1 592 ALA 592 592 592 ALA ALA A . n 
A 1 593 ASN 593 593 593 ASN ASN A . n 
A 1 594 TRP 594 594 594 TRP TRP A . n 
A 1 595 ARG 595 595 595 ARG ARG A . n 
A 1 596 THR 596 596 596 THR THR A . n 
A 1 597 ALA 597 597 597 ALA ALA A . n 
A 1 598 THR 598 598 598 THR THR A . n 
A 1 599 TYR 599 599 599 TYR TYR A . n 
A 1 600 SER 600 600 600 SER SER A . n 
A 1 601 TYR 601 601 601 TYR TYR A . n 
A 1 602 TYR 602 602 602 TYR TYR A . n 
A 1 603 ALA 603 603 603 ALA ALA A . n 
A 1 604 VAL 604 604 604 VAL VAL A . n 
A 1 605 PRO 605 605 605 PRO PRO A . n 
A 1 606 VAL 606 606 606 VAL VAL A . n 
A 1 607 ALA 607 607 607 ALA ALA A . n 
A 1 608 GLY 608 608 608 GLY GLY A . n 
A 1 609 LYS 609 609 609 LYS LYS A . n 
A 1 610 ASP 610 610 610 ASP ASP A . n 
A 1 611 ASP 611 611 611 ASP ASP A . n 
A 1 612 GLN 612 612 612 GLN GLN A . n 
A 1 613 VAL 613 613 613 VAL VAL A . n 
A 1 614 LEU 614 614 614 LEU LEU A . n 
A 1 615 VAL 615 615 615 VAL VAL A . n 
A 1 616 THR 616 616 616 THR THR A . n 
A 1 617 SER 617 617 617 SER SER A . n 
A 1 618 TYR 618 618 618 TYR TYR A . n 
A 1 619 MET 619 619 619 MET MET A . n 
A 1 620 THR 620 620 620 THR THR A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 ARG 622 622 622 ARG ARG A . n 
A 1 623 ASN 623 623 623 ASN ASN A . n 
A 1 624 GLY 624 624 624 GLY GLY A . n 
A 1 625 VAL 625 625 625 VAL VAL A . n 
A 1 626 ALA 626 626 626 ALA ALA A . n 
A 1 627 GLY 627 627 627 GLY GLY A . n 
A 1 628 LYS 628 628 628 LYS LYS A . n 
A 1 629 GLY 629 629 629 GLY GLY A . n 
A 1 630 MET 630 630 630 MET MET A . n 
A 1 631 ASP 631 631 631 ASP ASP A . n 
A 1 632 SER 632 632 632 SER SER A . n 
A 1 633 THR 633 633 633 THR THR A . n 
A 1 634 TRP 634 634 634 TRP TRP A . n 
A 1 635 ALA 635 635 635 ALA ALA A . n 
A 1 636 PRO 636 636 636 PRO PRO A . n 
A 1 637 SER 637 637 637 SER SER A . n 
A 1 638 PHE 638 638 638 PHE PHE A . n 
A 1 639 LEU 639 639 639 LEU LEU A . n 
A 1 640 LEU 640 640 640 LEU LEU A . n 
A 1 641 GLN 641 641 641 GLN GLN A . n 
A 1 642 ILE 642 642 642 ILE ILE A . n 
A 1 643 ASN 643 643 643 ASN ASN A . n 
A 1 644 PRO 644 644 644 PRO PRO A . n 
A 1 645 ASP 645 645 645 ASP ASP A . n 
A 1 646 ASN 646 646 646 ASN ASN A . n 
A 1 647 THR 647 647 647 THR THR A . n 
A 1 648 THR 648 648 648 THR THR A . n 
A 1 649 THR 649 649 649 THR THR A . n 
A 1 650 VAL 650 650 650 VAL VAL A . n 
A 1 651 LEU 651 651 651 LEU LEU A . n 
A 1 652 ALA 652 652 652 ALA ALA A . n 
A 1 653 LYS 653 653 653 LYS LYS A . n 
A 1 654 MET 654 654 654 MET MET A . n 
A 1 655 THR 655 655 655 THR THR A . n 
A 1 656 ASN 656 656 656 ASN ASN A . n 
A 1 657 GLN 657 657 657 GLN GLN A . n 
A 1 658 GLY 658 658 658 GLY GLY A . n 
A 1 659 ASP 659 659 659 ASP ASP A . n 
A 1 660 TRP 660 660 660 TRP TRP A . n 
A 1 661 ILE 661 661 661 ILE ILE A . n 
A 1 662 TRP 662 662 662 TRP TRP A . n 
A 1 663 ASP 663 663 663 ASP ASP A . n 
A 1 664 ASP 664 664 664 ASP ASP A . n 
A 1 665 SER 665 665 665 SER SER A . n 
A 1 666 SER 666 666 666 SER SER A . n 
A 1 667 GLU 667 667 667 GLU GLU A . n 
A 1 668 ASN 668 668 668 ASN ASN A . n 
A 1 669 LEU 669 669 669 LEU LEU A . n 
A 1 670 ASP 670 670 670 ASP ASP A . n 
A 1 671 MET 671 671 671 MET MET A . n 
A 1 672 ILE 672 672 672 ILE ILE A . n 
A 1 673 GLY 673 673 673 GLY GLY A . n 
A 1 674 ASP 674 674 674 ASP ASP A . n 
A 1 675 LEU 675 675 675 LEU LEU A . n 
A 1 676 ASP 676 676 676 ASP ASP A . n 
A 1 677 SER 677 677 677 SER SER A . n 
A 1 678 ALA 678 678 678 ALA ALA A . n 
A 1 679 ALA 679 679 679 ALA ALA A . n 
A 1 680 LEU 680 680 680 LEU LEU A . n 
A 1 681 PRO 681 681 681 PRO PRO A . n 
A 1 682 GLY 682 682 682 GLY GLY A . n 
A 1 683 GLU 683 683 683 GLU GLU A . n 
A 1 684 ARG 684 684 684 ARG ARG A . n 
A 1 685 ASP 685 685 685 ASP ASP A . n 
A 1 686 LYS 686 686 686 LYS LYS A . n 
A 1 687 PRO 687 687 687 PRO PRO A . n 
A 1 688 VAL 688 688 688 VAL VAL A . n 
A 1 689 ASP 689 689 689 ASP ASP A . n 
A 1 690 TRP 690 690 690 TRP TRP A . n 
A 1 691 ASP 691 691 691 ASP ASP A . n 
A 1 692 LEU 692 692 692 LEU LEU A . n 
A 1 693 ILE 693 693 693 ILE ILE A . n 
A 1 694 GLY 694 694 694 GLY GLY A . n 
A 1 695 TYR 695 695 695 TYR TYR A . n 
A 1 696 GLY 696 696 696 GLY GLY A . n 
A 1 697 LEU 697 697 ?   ?   ?   A . n 
A 1 698 LYS 698 698 ?   ?   ?   A . n 
A 1 699 PRO 699 699 ?   ?   ?   A . n 
A 1 700 HIS 700 700 ?   ?   ?   A . n 
A 1 701 ASP 701 701 ?   ?   ?   A . n 
A 1 702 PRO 702 702 ?   ?   ?   A . n 
A 1 703 ALA 703 703 ?   ?   ?   A . n 
A 1 704 THR 704 704 ?   ?   ?   A . n 
A 1 705 PRO 705 705 ?   ?   ?   A . n 
A 1 706 ASN 706 706 ?   ?   ?   A . n 
A 1 707 ASP 707 707 ?   ?   ?   A . n 
A 1 708 PRO 708 708 ?   ?   ?   A . n 
A 1 709 GLU 709 709 ?   ?   ?   A . n 
A 1 710 THR 710 710 ?   ?   ?   A . n 
A 1 711 PRO 711 711 ?   ?   ?   A . n 
A 1 712 THR 712 712 ?   ?   ?   A . n 
A 1 713 THR 713 713 ?   ?   ?   A . n 
A 1 714 PRO 714 714 ?   ?   ?   A . n 
A 1 715 GLU 715 715 ?   ?   ?   A . n 
A 1 716 THR 716 716 ?   ?   ?   A . n 
A 1 717 PRO 717 717 ?   ?   ?   A . n 
A 1 718 GLU 718 718 ?   ?   ?   A . n 
A 1 719 THR 719 719 ?   ?   ?   A . n 
A 1 720 PRO 720 720 ?   ?   ?   A . n 
A 1 721 ASN 721 721 ?   ?   ?   A . n 
A 1 722 THR 722 722 ?   ?   ?   A . n 
A 1 723 PRO 723 723 ?   ?   ?   A . n 
A 1 724 LYS 724 724 ?   ?   ?   A . n 
A 1 725 THR 725 725 ?   ?   ?   A . n 
A 1 726 PRO 726 726 ?   ?   ?   A . n 
A 1 727 LYS 727 727 ?   ?   ?   A . n 
A 1 728 THR 728 728 ?   ?   ?   A . n 
A 1 729 PRO 729 729 ?   ?   ?   A . n 
A 1 730 GLU 730 730 ?   ?   ?   A . n 
A 1 731 ASN 731 731 ?   ?   ?   A . n 
A 1 732 PRO 732 732 ?   ?   ?   A . n 
A 1 733 GLY 733 733 ?   ?   ?   A . n 
A 1 734 THR 734 734 ?   ?   ?   A . n 
A 1 735 PRO 735 735 ?   ?   ?   A . n 
A 1 736 GLN 736 736 ?   ?   ?   A . n 
A 1 737 THR 737 737 ?   ?   ?   A . n 
A 1 738 PRO 738 738 ?   ?   ?   A . n 
A 1 739 ASN 739 739 ?   ?   ?   A . n 
A 1 740 THR 740 740 ?   ?   ?   A . n 
A 1 741 PRO 741 741 ?   ?   ?   A . n 
A 1 742 ASN 742 742 ?   ?   ?   A . n 
A 1 743 THR 743 743 ?   ?   ?   A . n 
A 1 744 PRO 744 744 ?   ?   ?   A . n 
A 1 745 GLU 745 745 ?   ?   ?   A . n 
A 1 746 ILE 746 746 ?   ?   ?   A . n 
A 1 747 PRO 747 747 ?   ?   ?   A . n 
A 1 748 LEU 748 748 ?   ?   ?   A . n 
A 1 749 THR 749 749 ?   ?   ?   A . n 
A 1 750 PRO 750 750 ?   ?   ?   A . n 
A 1 751 GLU 751 751 ?   ?   ?   A . n 
A 1 752 THR 752 752 ?   ?   ?   A . n 
A 1 753 PRO 753 753 ?   ?   ?   A . n 
A 1 754 LYS 754 754 ?   ?   ?   A . n 
A 1 755 GLN 755 755 ?   ?   ?   A . n 
A 1 756 PRO 756 756 ?   ?   ?   A . n 
A 1 757 GLU 757 757 ?   ?   ?   A . n 
A 1 758 THR 758 758 ?   ?   ?   A . n 
A 1 759 GLN 759 759 ?   ?   ?   A . n 
A 1 760 THR 760 760 ?   ?   ?   A . n 
A 1 761 ASN 761 761 ?   ?   ?   A . n 
A 1 762 ASN 762 762 ?   ?   ?   A . n 
A 1 763 ARG 763 763 ?   ?   ?   A . n 
A 1 764 LEU 764 764 ?   ?   ?   A . n 
A 1 765 PRO 765 765 ?   ?   ?   A . n 
A 1 766 GLN 766 766 ?   ?   ?   A . n 
A 1 767 THR 767 767 ?   ?   ?   A . n 
A 1 768 GLY 768 768 ?   ?   ?   A . n 
A 1 769 ASN 769 769 ?   ?   ?   A . n 
A 1 770 ASN 770 770 ?   ?   ?   A . n 
A 1 771 ALA 771 771 ?   ?   ?   A . n 
A 1 772 ASN 772 772 ?   ?   ?   A . n 
A 1 773 LYS 773 773 ?   ?   ?   A . n 
A 1 774 ALA 774 774 ?   ?   ?   A . n 
A 1 775 MET 775 775 ?   ?   ?   A . n 
A 1 776 ILE 776 776 ?   ?   ?   A . n 
A 1 777 GLY 777 777 ?   ?   ?   A . n 
A 1 778 LEU 778 778 ?   ?   ?   A . n 
A 1 779 GLY 779 779 ?   ?   ?   A . n 
A 1 780 MET 780 780 ?   ?   ?   A . n 
A 1 781 GLY 781 781 ?   ?   ?   A . n 
A 1 782 THR 782 782 ?   ?   ?   A . n 
A 1 783 LEU 783 783 ?   ?   ?   A . n 
A 1 784 LEU 784 784 ?   ?   ?   A . n 
A 1 785 SER 785 785 ?   ?   ?   A . n 
A 1 786 MET 786 786 ?   ?   ?   A . n 
A 1 787 PHE 787 787 ?   ?   ?   A . n 
A 1 788 GLY 788 788 ?   ?   ?   A . n 
A 1 789 LEU 789 789 ?   ?   ?   A . n 
A 1 790 ALA 790 790 ?   ?   ?   A . n 
A 1 791 GLU 791 791 ?   ?   ?   A . n 
A 1 792 ILE 792 792 ?   ?   ?   A . n 
A 1 793 ASN 793 793 ?   ?   ?   A . n 
A 1 794 LYS 794 794 ?   ?   ?   A . n 
A 1 795 ARG 795 795 ?   ?   ?   A . n 
A 1 796 ARG 796 796 ?   ?   ?   A . n 
A 1 797 PHE 797 797 ?   ?   ?   A . n 
A 1 798 ASN 798 798 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LEU 2   2   ?   ?   ?   B . n 
B 1 3   GLU 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   ?   ?   ?   B . n 
B 1 5   LYS 5   5   ?   ?   ?   B . n 
B 1 6   GLU 6   6   ?   ?   ?   B . n 
B 1 7   HIS 7   7   ?   ?   ?   B . n 
B 1 8   LYS 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   ?   ?   ?   B . n 
B 1 10  MET 10  10  ?   ?   ?   B . n 
B 1 11  TYR 11  11  ?   ?   ?   B . n 
B 1 12  LYS 12  12  ?   ?   ?   B . n 
B 1 13  SER 13  13  ?   ?   ?   B . n 
B 1 14  GLY 14  14  ?   ?   ?   B . n 
B 1 15  LYS 15  15  ?   ?   ?   B . n 
B 1 16  ASN 16  16  ?   ?   ?   B . n 
B 1 17  TRP 17  17  ?   ?   ?   B . n 
B 1 18  ALA 18  18  ?   ?   ?   B . n 
B 1 19  VAL 19  19  ?   ?   ?   B . n 
B 1 20  VAL 20  20  ?   ?   ?   B . n 
B 1 21  THR 21  21  ?   ?   ?   B . n 
B 1 22  LEU 22  22  ?   ?   ?   B . n 
B 1 23  SER 23  23  ?   ?   ?   B . n 
B 1 24  THR 24  24  ?   ?   ?   B . n 
B 1 25  ALA 25  25  ?   ?   ?   B . n 
B 1 26  ALA 26  26  ?   ?   ?   B . n 
B 1 27  LEU 27  27  ?   ?   ?   B . n 
B 1 28  VAL 28  28  ?   ?   ?   B . n 
B 1 29  PHE 29  29  ?   ?   ?   B . n 
B 1 30  GLY 30  30  ?   ?   ?   B . n 
B 1 31  ALA 31  31  ?   ?   ?   B . n 
B 1 32  THR 32  32  ?   ?   ?   B . n 
B 1 33  THR 33  33  ?   ?   ?   B . n 
B 1 34  VAL 34  34  ?   ?   ?   B . n 
B 1 35  ASN 35  35  ?   ?   ?   B . n 
B 1 36  ALA 36  36  ?   ?   ?   B . n 
B 1 37  SER 37  37  ?   ?   ?   B . n 
B 1 38  ALA 38  38  ?   ?   ?   B . n 
B 1 39  ASP 39  39  ?   ?   ?   B . n 
B 1 40  THR 40  40  ?   ?   ?   B . n 
B 1 41  ASN 41  41  ?   ?   ?   B . n 
B 1 42  ILE 42  42  ?   ?   ?   B . n 
B 1 43  GLU 43  43  ?   ?   ?   B . n 
B 1 44  ASN 44  44  ?   ?   ?   B . n 
B 1 45  ASN 45  45  ?   ?   ?   B . n 
B 1 46  ASP 46  46  ?   ?   ?   B . n 
B 1 47  SER 47  47  ?   ?   ?   B . n 
B 1 48  SER 48  48  ?   ?   ?   B . n 
B 1 49  THR 49  49  ?   ?   ?   B . n 
B 1 50  VAL 50  50  ?   ?   ?   B . n 
B 1 51  GLN 51  51  ?   ?   ?   B . n 
B 1 52  VAL 52  52  ?   ?   ?   B . n 
B 1 53  THR 53  53  ?   ?   ?   B . n 
B 1 54  THR 54  54  ?   ?   ?   B . n 
B 1 55  GLY 55  55  ?   ?   ?   B . n 
B 1 56  ASP 56  56  ?   ?   ?   B . n 
B 1 57  ASN 57  57  ?   ?   ?   B . n 
B 1 58  ASP 58  58  ?   ?   ?   B . n 
B 1 59  ILE 59  59  ?   ?   ?   B . n 
B 1 60  ALA 60  60  ?   ?   ?   B . n 
B 1 61  VAL 61  61  ?   ?   ?   B . n 
B 1 62  LYS 62  62  ?   ?   ?   B . n 
B 1 63  SER 63  63  ?   ?   ?   B . n 
B 1 64  VAL 64  64  ?   ?   ?   B . n 
B 1 65  THR 65  65  ?   ?   ?   B . n 
B 1 66  LEU 66  66  ?   ?   ?   B . n 
B 1 67  GLY 67  67  ?   ?   ?   B . n 
B 1 68  SER 68  68  ?   ?   ?   B . n 
B 1 69  GLY 69  69  ?   ?   ?   B . n 
B 1 70  GLN 70  70  ?   ?   ?   B . n 
B 1 71  VAL 71  71  ?   ?   ?   B . n 
B 1 72  SER 72  72  ?   ?   ?   B . n 
B 1 73  ALA 73  73  ?   ?   ?   B . n 
B 1 74  ALA 74  74  ?   ?   ?   B . n 
B 1 75  SER 75  75  ?   ?   ?   B . n 
B 1 76  ASP 76  76  ?   ?   ?   B . n 
B 1 77  THR 77  77  ?   ?   ?   B . n 
B 1 78  THR 78  78  ?   ?   ?   B . n 
B 1 79  ILE 79  79  ?   ?   ?   B . n 
B 1 80  ARG 80  80  ?   ?   ?   B . n 
B 1 81  THR 81  81  ?   ?   ?   B . n 
B 1 82  SER 82  82  ?   ?   ?   B . n 
B 1 83  ALA 83  83  ?   ?   ?   B . n 
B 1 84  ASN 84  84  ?   ?   ?   B . n 
B 1 85  ALA 85  85  ?   ?   ?   B . n 
B 1 86  ASN 86  86  ?   ?   ?   B . n 
B 1 87  SER 87  87  ?   ?   ?   B . n 
B 1 88  ALA 88  88  ?   ?   ?   B . n 
B 1 89  SER 89  89  ?   ?   ?   B . n 
B 1 90  SER 90  90  ?   ?   ?   B . n 
B 1 91  ALA 91  91  ?   ?   ?   B . n 
B 1 92  ALA 92  92  ?   ?   ?   B . n 
B 1 93  ASN 93  93  ?   ?   ?   B . n 
B 1 94  THR 94  94  ?   ?   ?   B . n 
B 1 95  GLN 95  95  ?   ?   ?   B . n 
B 1 96  ASN 96  96  ?   ?   ?   B . n 
B 1 97  SER 97  97  ?   ?   ?   B . n 
B 1 98  ASN 98  98  ?   ?   ?   B . n 
B 1 99  SER 99  99  ?   ?   ?   B . n 
B 1 100 GLN 100 100 ?   ?   ?   B . n 
B 1 101 VAL 101 101 ?   ?   ?   B . n 
B 1 102 ALA 102 102 ?   ?   ?   B . n 
B 1 103 SER 103 103 ?   ?   ?   B . n 
B 1 104 SER 104 104 ?   ?   ?   B . n 
B 1 105 ALA 105 105 ?   ?   ?   B . n 
B 1 106 ALA 106 106 ?   ?   ?   B . n 
B 1 107 ILE 107 107 ?   ?   ?   B . n 
B 1 108 THR 108 108 ?   ?   ?   B . n 
B 1 109 SER 109 109 ?   ?   ?   B . n 
B 1 110 SER 110 110 ?   ?   ?   B . n 
B 1 111 THR 111 111 ?   ?   ?   B . n 
B 1 112 SER 112 112 ?   ?   ?   B . n 
B 1 113 SER 113 113 ?   ?   ?   B . n 
B 1 114 ALA 114 114 ?   ?   ?   B . n 
B 1 115 ALA 115 115 ?   ?   ?   B . n 
B 1 116 SER 116 116 ?   ?   ?   B . n 
B 1 117 SER 117 117 ?   ?   ?   B . n 
B 1 118 ASN 118 118 ?   ?   ?   B . n 
B 1 119 ASN 119 119 ?   ?   ?   B . n 
B 1 120 THR 120 120 ?   ?   ?   B . n 
B 1 121 ASP 121 121 ?   ?   ?   B . n 
B 1 122 SER 122 122 ?   ?   ?   B . n 
B 1 123 LYS 123 123 ?   ?   ?   B . n 
B 1 124 ALA 124 124 ?   ?   ?   B . n 
B 1 125 ALA 125 125 ?   ?   ?   B . n 
B 1 126 GLN 126 126 ?   ?   ?   B . n 
B 1 127 GLU 127 127 ?   ?   ?   B . n 
B 1 128 ASN 128 128 ?   ?   ?   B . n 
B 1 129 THR 129 129 ?   ?   ?   B . n 
B 1 130 ASN 130 130 ?   ?   ?   B . n 
B 1 131 THR 131 131 ?   ?   ?   B . n 
B 1 132 ALA 132 132 ?   ?   ?   B . n 
B 1 133 LYS 133 133 ?   ?   ?   B . n 
B 1 134 ASN 134 134 ?   ?   ?   B . n 
B 1 135 ASP 135 135 ?   ?   ?   B . n 
B 1 136 ASP 136 136 ?   ?   ?   B . n 
B 1 137 THR 137 137 ?   ?   ?   B . n 
B 1 138 GLN 138 138 ?   ?   ?   B . n 
B 1 139 LYS 139 139 ?   ?   ?   B . n 
B 1 140 ALA 140 140 ?   ?   ?   B . n 
B 1 141 ALA 141 141 ?   ?   ?   B . n 
B 1 142 PRO 142 142 ?   ?   ?   B . n 
B 1 143 ALA 143 143 ?   ?   ?   B . n 
B 1 144 ASN 144 144 ?   ?   ?   B . n 
B 1 145 GLU 145 145 ?   ?   ?   B . n 
B 1 146 SER 146 146 ?   ?   ?   B . n 
B 1 147 SER 147 147 ?   ?   ?   B . n 
B 1 148 GLU 148 148 ?   ?   ?   B . n 
B 1 149 ALA 149 149 ?   ?   ?   B . n 
B 1 150 LYS 150 150 ?   ?   ?   B . n 
B 1 151 ASN 151 151 ?   ?   ?   B . n 
B 1 152 GLU 152 152 ?   ?   ?   B . n 
B 1 153 PRO 153 153 ?   ?   ?   B . n 
B 1 154 ALA 154 154 ?   ?   ?   B . n 
B 1 155 VAL 155 155 ?   ?   ?   B . n 
B 1 156 ASN 156 156 ?   ?   ?   B . n 
B 1 157 VAL 157 157 ?   ?   ?   B . n 
B 1 158 ASN 158 158 ?   ?   ?   B . n 
B 1 159 ASP 159 159 ?   ?   ?   B . n 
B 1 160 SER 160 160 ?   ?   ?   B . n 
B 1 161 SER 161 161 ?   ?   ?   B . n 
B 1 162 ALA 162 162 ?   ?   ?   B . n 
B 1 163 ALA 163 163 ?   ?   ?   B . n 
B 1 164 LYS 164 164 ?   ?   ?   B . n 
B 1 165 ASN 165 165 ?   ?   ?   B . n 
B 1 166 ASP 166 166 ?   ?   ?   B . n 
B 1 167 ASP 167 167 ?   ?   ?   B . n 
B 1 168 GLN 168 168 ?   ?   ?   B . n 
B 1 169 GLN 169 169 ?   ?   ?   B . n 
B 1 170 SER 170 170 ?   ?   ?   B . n 
B 1 171 SER 171 171 ?   ?   ?   B . n 
B 1 172 LYS 172 172 ?   ?   ?   B . n 
B 1 173 LYS 173 173 ?   ?   ?   B . n 
B 1 174 ASN 174 174 ?   ?   ?   B . n 
B 1 175 THR 175 175 ?   ?   ?   B . n 
B 1 176 THR 176 176 ?   ?   ?   B . n 
B 1 177 ALA 177 177 ?   ?   ?   B . n 
B 1 178 LYS 178 178 178 LYS LYS B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 LYS 181 181 181 LYS LYS B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 ASN 185 185 185 ASN ASN B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 LYS 189 189 189 LYS LYS B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 GLY 191 191 191 GLY GLY B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 ASP 193 193 193 ASP ASP B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 ASN 195 195 195 ASN ASN B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 GLN 201 201 201 GLN GLN B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 LYS 203 203 203 LYS LYS B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 MET 208 208 208 MET MET B . n 
B 1 209 ASN 209 209 209 ASN ASN B . n 
B 1 210 PHE 210 210 210 PHE PHE B . n 
B 1 211 SER 211 211 211 SER SER B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 ALA 213 213 213 ALA ALA B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 SER 216 216 ?   ?   ?   B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 THR 218 218 218 THR THR B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 MET 220 220 220 MET MET B . n 
B 1 221 THR 221 221 221 THR THR B . n 
B 1 222 TYR 222 222 222 TYR TYR B . n 
B 1 223 ASN 223 223 223 ASN ASN B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 PHE 225 225 225 PHE PHE B . n 
B 1 226 GLN 226 226 226 GLN GLN B . n 
B 1 227 LYS 227 227 227 LYS LYS B . n 
B 1 228 ILE 228 228 228 ILE ILE B . n 
B 1 229 ALA 229 229 229 ALA ALA B . n 
B 1 230 ASP 230 230 230 ASP ASP B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 ILE 233 233 233 ILE ILE B . n 
B 1 234 LYS 234 234 234 LYS LYS B . n 
B 1 235 GLN 235 235 235 GLN GLN B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 GLY 237 237 237 GLY GLY B . n 
B 1 238 ARG 238 238 238 ARG ARG B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 THR 240 240 240 THR THR B . n 
B 1 241 VAL 241 241 241 VAL VAL B . n 
B 1 242 PRO 242 242 242 PRO PRO B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 PHE 244 244 244 PHE PHE B . n 
B 1 245 LYS 245 245 245 LYS LYS B . n 
B 1 246 ALA 246 246 246 ALA ALA B . n 
B 1 247 SER 247 247 247 SER SER B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LYS 250 250 250 LYS LYS B . n 
B 1 251 ASN 251 251 251 ASN ASN B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 PRO 253 253 253 PRO PRO B . n 
B 1 254 ALA 254 254 254 ALA ALA B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 THR 256 256 256 THR THR B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 LYS 258 258 258 LYS LYS B . n 
B 1 259 ASP 259 259 259 ASP ASP B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 GLN 261 261 261 GLN GLN B . n 
B 1 262 THR 262 262 262 THR THR B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 ILE 265 265 265 ILE ILE B . n 
B 1 266 GLU 266 266 266 GLU GLU B . n 
B 1 267 PRO 267 267 267 PRO PRO B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 ASP 269 269 269 ASP ASP B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 TRP 271 271 271 TRP TRP B . n 
B 1 272 ASP 272 272 272 ASP ASP B . n 
B 1 273 SER 273 273 273 SER SER B . n 
B 1 274 TRP 274 274 274 TRP TRP B . n 
B 1 275 PRO 275 275 275 PRO PRO B . n 
B 1 276 VAL 276 276 276 VAL VAL B . n 
B 1 277 GLN 277 277 277 GLN GLN B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 THR 281 281 281 THR THR B . n 
B 1 282 GLY 282 282 282 GLY GLY B . n 
B 1 283 GLN 283 283 283 GLN GLN B . n 
B 1 284 VAL 284 284 284 VAL VAL B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 ASN 286 286 286 ASN ASN B . n 
B 1 287 TRP 287 287 287 TRP TRP B . n 
B 1 288 ASN 288 288 288 ASN ASN B . n 
B 1 289 GLY 289 289 289 GLY GLY B . n 
B 1 290 TYR 290 290 290 TYR TYR B . n 
B 1 291 GLN 291 291 291 GLN GLN B . n 
B 1 292 LEU 292 292 292 LEU LEU B . n 
B 1 293 VAL 293 293 293 VAL VAL B . n 
B 1 294 ILE 294 294 294 ILE ILE B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 MET 296 296 296 MET MET B . n 
B 1 297 MET 297 297 297 MET MET B . n 
B 1 298 GLY 298 298 298 GLY GLY B . n 
B 1 299 ILE 299 299 299 ILE ILE B . n 
B 1 300 PRO 300 300 300 PRO PRO B . n 
B 1 301 ASN 301 301 301 ASN ASN B . n 
B 1 302 GLN 302 302 302 GLN GLN B . n 
B 1 303 ASN 303 303 303 ASN ASN B . n 
B 1 304 ASP 304 304 304 ASP ASP B . n 
B 1 305 ASN 305 305 305 ASN ASN B . n 
B 1 306 HIS 306 306 306 HIS HIS B . n 
B 1 307 ILE 307 307 307 ILE ILE B . n 
B 1 308 TYR 308 308 308 TYR TYR B . n 
B 1 309 LEU 309 309 309 LEU LEU B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 ASN 312 312 312 ASN ASN B . n 
B 1 313 LYS 313 313 313 LYS LYS B . n 
B 1 314 TYR 314 314 314 TYR TYR B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 ASP 316 316 316 ASP ASP B . n 
B 1 317 ASN 317 317 317 ASN ASN B . n 
B 1 318 GLU 318 318 318 GLU GLU B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 SER 320 320 320 SER SER B . n 
B 1 321 HIS 321 321 321 HIS HIS B . n 
B 1 322 TRP 322 322 322 TRP TRP B . n 
B 1 323 LYS 323 323 323 LYS LYS B . n 
B 1 324 ASN 324 324 324 ASN ASN B . n 
B 1 325 VAL 325 325 325 VAL VAL B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 PRO 327 327 327 PRO PRO B . n 
B 1 328 ILE 328 328 328 ILE ILE B . n 
B 1 329 PHE 329 329 329 PHE PHE B . n 
B 1 330 GLY 330 330 330 GLY GLY B . n 
B 1 331 TYR 331 331 331 TYR TYR B . n 
B 1 332 ASN 332 332 332 ASN ASN B . n 
B 1 333 SER 333 333 333 SER SER B . n 
B 1 334 THR 334 334 334 THR THR B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 VAL 336 336 336 VAL VAL B . n 
B 1 337 SER 337 337 337 SER SER B . n 
B 1 338 GLN 338 338 338 GLN GLN B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 TRP 340 340 340 TRP TRP B . n 
B 1 341 SER 341 341 341 SER SER B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 SER 343 343 343 SER SER B . n 
B 1 344 ALA 344 344 344 ALA ALA B . n 
B 1 345 VAL 345 345 345 VAL VAL B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 ASN 347 347 347 ASN ASN B . n 
B 1 348 SER 348 348 348 SER SER B . n 
B 1 349 ASP 349 349 349 ASP ASP B . n 
B 1 350 ASN 350 350 350 ASN ASN B . n 
B 1 351 SER 351 351 351 SER SER B . n 
B 1 352 ILE 352 352 352 ILE ILE B . n 
B 1 353 GLN 353 353 353 GLN GLN B . n 
B 1 354 LEU 354 354 354 LEU LEU B . n 
B 1 355 PHE 355 355 355 PHE PHE B . n 
B 1 356 TYR 356 356 356 TYR TYR B . n 
B 1 357 THR 357 357 357 THR THR B . n 
B 1 358 ARG 358 358 358 ARG ARG B . n 
B 1 359 VAL 359 359 359 VAL VAL B . n 
B 1 360 ASP 360 360 360 ASP ASP B . n 
B 1 361 THR 361 361 361 THR THR B . n 
B 1 362 SER 362 362 362 SER SER B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 ASN 364 364 364 ASN ASN B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 THR 366 366 366 THR THR B . n 
B 1 367 ASN 367 367 367 ASN ASN B . n 
B 1 368 HIS 368 368 368 HIS HIS B . n 
B 1 369 GLN 369 369 369 GLN GLN B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 ILE 371 371 371 ILE ILE B . n 
B 1 372 ALA 372 372 372 ALA ALA B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 ALA 374 374 374 ALA ALA B . n 
B 1 375 THR 375 375 375 THR THR B . n 
B 1 376 LEU 376 376 376 LEU LEU B . n 
B 1 377 TYR 377 377 377 TYR TYR B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 THR 379 379 379 THR THR B . n 
B 1 380 ASP 380 380 380 ASP ASP B . n 
B 1 381 ASN 381 381 381 ASN ASN B . n 
B 1 382 ASN 382 382 382 ASN ASN B . n 
B 1 383 GLY 383 383 383 GLY GLY B . n 
B 1 384 ASN 384 384 384 ASN ASN B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 SER 386 386 386 SER SER B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 GLN 389 389 389 GLN GLN B . n 
B 1 390 VAL 390 390 390 VAL VAL B . n 
B 1 391 ALA 391 391 391 ALA ALA B . n 
B 1 392 ASN 392 392 392 ASN ASN B . n 
B 1 393 ASP 393 393 393 ASP ASP B . n 
B 1 394 HIS 394 394 394 HIS HIS B . n 
B 1 395 ILE 395 395 395 ILE ILE B . n 
B 1 396 VAL 396 396 396 VAL VAL B . n 
B 1 397 PHE 397 397 397 PHE PHE B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 GLY 399 399 399 GLY GLY B . n 
B 1 400 ASP 400 400 400 ASP ASP B . n 
B 1 401 GLY 401 401 401 GLY GLY B . n 
B 1 402 TYR 402 402 402 TYR TYR B . n 
B 1 403 TYR 403 403 403 TYR TYR B . n 
B 1 404 TYR 404 404 404 TYR TYR B . n 
B 1 405 GLN 405 405 405 GLN GLN B . n 
B 1 406 THR 406 406 406 THR THR B . n 
B 1 407 TYR 407 407 407 TYR TYR B . n 
B 1 408 ASP 408 408 408 ASP ASP B . n 
B 1 409 GLN 409 409 409 GLN GLN B . n 
B 1 410 TRP 410 410 410 TRP TRP B . n 
B 1 411 LYS 411 411 411 LYS LYS B . n 
B 1 412 ALA 412 412 412 ALA ALA B . n 
B 1 413 THR 413 413 413 THR THR B . n 
B 1 414 ASN 414 414 414 ASN ASN B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 GLY 416 416 416 GLY GLY B . n 
B 1 417 ALA 417 417 417 ALA ALA B . n 
B 1 418 ASP 418 418 418 ASP ASP B . n 
B 1 419 ASN 419 419 419 ASN ASN B . n 
B 1 420 ILE 420 420 420 ILE ILE B . n 
B 1 421 ALA 421 421 421 ALA ALA B . n 
B 1 422 MET 422 422 422 MET MET B . n 
B 1 423 ARG 423 423 423 ARG ARG B . n 
B 1 424 ASP 424 424 424 ASP ASP B . n 
B 1 425 ALA 425 425 425 ALA ALA B . n 
B 1 426 HIS 426 426 426 HIS HIS B . n 
B 1 427 VAL 427 427 427 VAL VAL B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 GLU 429 429 429 GLU GLU B . n 
B 1 430 ASP 430 430 430 ASP ASP B . n 
B 1 431 ASP 431 431 431 ASP ASP B . n 
B 1 432 ASN 432 432 432 ASN ASN B . n 
B 1 433 GLY 433 433 433 GLY GLY B . n 
B 1 434 ASP 434 434 434 ASP ASP B . n 
B 1 435 ARG 435 435 435 ARG ARG B . n 
B 1 436 TYR 436 436 436 TYR TYR B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 VAL 438 438 438 VAL VAL B . n 
B 1 439 PHE 439 439 439 PHE PHE B . n 
B 1 440 GLU 440 440 440 GLU GLU B . n 
B 1 441 ALA 441 441 441 ALA ALA B . n 
B 1 442 SER 442 442 442 SER SER B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 GLY 444 444 444 GLY GLY B . n 
B 1 445 LEU 445 445 445 LEU LEU B . n 
B 1 446 GLU 446 446 446 GLU GLU B . n 
B 1 447 ASN 447 447 447 ASN ASN B . n 
B 1 448 TYR 448 448 448 TYR TYR B . n 
B 1 449 GLN 449 449 449 GLN GLN B . n 
B 1 450 GLY 450 450 450 GLY GLY B . n 
B 1 451 GLU 451 451 451 GLU GLU B . n 
B 1 452 ASP 452 452 452 ASP ASP B . n 
B 1 453 GLN 453 453 453 GLN GLN B . n 
B 1 454 ILE 454 454 454 ILE ILE B . n 
B 1 455 TYR 455 455 455 TYR TYR B . n 
B 1 456 ASN 456 456 456 ASN ASN B . n 
B 1 457 TRP 457 457 457 TRP TRP B . n 
B 1 458 LEU 458 458 458 LEU LEU B . n 
B 1 459 ASN 459 459 459 ASN ASN B . n 
B 1 460 TYR 460 460 460 TYR TYR B . n 
B 1 461 GLY 461 461 461 GLY GLY B . n 
B 1 462 GLY 462 462 462 GLY GLY B . n 
B 1 463 ASP 463 463 463 ASP ASP B . n 
B 1 464 ASP 464 464 464 ASP ASP B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 PHE 466 466 466 PHE PHE B . n 
B 1 467 ASN 467 467 467 ASN ASN B . n 
B 1 468 ILE 468 468 468 ILE ILE B . n 
B 1 469 LYS 469 469 469 LYS LYS B . n 
B 1 470 SER 470 470 470 SER SER B . n 
B 1 471 LEU 471 471 471 LEU LEU B . n 
B 1 472 PHE 472 472 472 PHE PHE B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 ILE 474 474 474 ILE ILE B . n 
B 1 475 LEU 475 475 475 LEU LEU B . n 
B 1 476 SER 476 476 476 SER SER B . n 
B 1 477 ASN 477 477 477 ASN ASN B . n 
B 1 478 ASP 478 478 478 ASP ASP B . n 
B 1 479 ASP 479 479 479 ASP ASP B . n 
B 1 480 ILE 480 480 480 ILE ILE B . n 
B 1 481 LYS 481 481 481 LYS LYS B . n 
B 1 482 SER 482 482 482 SER SER B . n 
B 1 483 ARG 483 483 483 ARG ARG B . n 
B 1 484 ALA 484 484 484 ALA ALA B . n 
B 1 485 THR 485 485 485 THR THR B . n 
B 1 486 TRP 486 486 486 TRP TRP B . n 
B 1 487 ALA 487 487 487 ALA ALA B . n 
B 1 488 ASN 488 488 488 ASN ASN B . n 
B 1 489 ALA 489 489 489 ALA ALA B . n 
B 1 490 ALA 490 490 490 ALA ALA B . n 
B 1 491 ILE 491 491 491 ILE ILE B . n 
B 1 492 GLY 492 492 492 GLY GLY B . n 
B 1 493 ILE 493 493 493 ILE ILE B . n 
B 1 494 LEU 494 494 494 LEU LEU B . n 
B 1 495 LYS 495 495 495 LYS LYS B . n 
B 1 496 LEU 496 496 496 LEU LEU B . n 
B 1 497 ASN 497 497 497 ASN ASN B . n 
B 1 498 LYS 498 498 498 LYS LYS B . n 
B 1 499 ASP 499 499 499 ASP ASP B . n 
B 1 500 GLU 500 500 500 GLU GLU B . n 
B 1 501 LYS 501 501 501 LYS LYS B . n 
B 1 502 ASN 502 502 502 ASN ASN B . n 
B 1 503 PRO 503 503 503 PRO PRO B . n 
B 1 504 LYS 504 504 504 LYS LYS B . n 
B 1 505 VAL 505 505 505 VAL VAL B . n 
B 1 506 ALA 506 506 506 ALA ALA B . n 
B 1 507 GLU 507 507 507 GLU GLU B . n 
B 1 508 LEU 508 508 508 LEU LEU B . n 
B 1 509 TYR 509 509 509 TYR TYR B . n 
B 1 510 SER 510 510 510 SER SER B . n 
B 1 511 PRO 511 511 511 PRO PRO B . n 
B 1 512 LEU 512 512 512 LEU LEU B . n 
B 1 513 ILE 513 513 513 ILE ILE B . n 
B 1 514 SER 514 514 514 SER SER B . n 
B 1 515 ALA 515 515 515 ALA ALA B . n 
B 1 516 PRO 516 516 516 PRO PRO B . n 
B 1 517 MET 517 517 517 MET MET B . n 
B 1 518 VAL 518 518 518 VAL VAL B . n 
B 1 519 SER 519 519 519 SER SER B . n 
B 1 520 ASP 520 520 520 ASP ASP B . n 
B 1 521 GLU 521 521 521 GLU GLU B . n 
B 1 522 ILE 522 522 522 ILE ILE B . n 
B 1 523 GLU 523 523 523 GLU GLU B . n 
B 1 524 ARG 524 524 524 ARG ARG B . n 
B 1 525 PRO 525 525 525 PRO PRO B . n 
B 1 526 ASN 526 526 526 ASN ASN B . n 
B 1 527 VAL 527 527 527 VAL VAL B . n 
B 1 528 VAL 528 528 528 VAL VAL B . n 
B 1 529 LYS 529 529 529 LYS LYS B . n 
B 1 530 LEU 530 530 530 LEU LEU B . n 
B 1 531 GLY 531 531 531 GLY GLY B . n 
B 1 532 ASN 532 532 532 ASN ASN B . n 
B 1 533 LYS 533 533 533 LYS LYS B . n 
B 1 534 TYR 534 534 534 TYR TYR B . n 
B 1 535 TYR 535 535 535 TYR TYR B . n 
B 1 536 LEU 536 536 536 LEU LEU B . n 
B 1 537 PHE 537 537 537 PHE PHE B . n 
B 1 538 ALA 538 538 538 ALA ALA B . n 
B 1 539 ALA 539 539 539 ALA ALA B . n 
B 1 540 THR 540 540 540 THR THR B . n 
B 1 541 ARG 541 541 541 ARG ARG B . n 
B 1 542 LEU 542 542 542 LEU LEU B . n 
B 1 543 ASN 543 543 543 ASN ASN B . n 
B 1 544 ARG 544 544 544 ARG ARG B . n 
B 1 545 GLY 545 545 545 GLY GLY B . n 
B 1 546 SER 546 546 546 SER SER B . n 
B 1 547 ASN 547 547 547 ASN ASN B . n 
B 1 548 ASP 548 548 548 ASP ASP B . n 
B 1 549 ASP 549 549 549 ASP ASP B . n 
B 1 550 ALA 550 550 550 ALA ALA B . n 
B 1 551 TRP 551 551 551 TRP TRP B . n 
B 1 552 MET 552 552 552 MET MET B . n 
B 1 553 ASN 553 553 553 ASN ASN B . n 
B 1 554 ALA 554 554 554 ALA ALA B . n 
B 1 555 ASN 555 555 555 ASN ASN B . n 
B 1 556 TYR 556 556 556 TYR TYR B . n 
B 1 557 ALA 557 557 557 ALA ALA B . n 
B 1 558 VAL 558 558 558 VAL VAL B . n 
B 1 559 GLY 559 559 559 GLY GLY B . n 
B 1 560 ASP 560 560 560 ASP ASP B . n 
B 1 561 ASN 561 561 561 ASN ASN B . n 
B 1 562 VAL 562 562 562 VAL VAL B . n 
B 1 563 ALA 563 563 563 ALA ALA B . n 
B 1 564 MET 564 564 564 MET MET B . n 
B 1 565 VAL 565 565 565 VAL VAL B . n 
B 1 566 GLY 566 566 566 GLY GLY B . n 
B 1 567 TYR 567 567 567 TYR TYR B . n 
B 1 568 VAL 568 568 568 VAL VAL B . n 
B 1 569 ALA 569 569 569 ALA ALA B . n 
B 1 570 ASP 570 570 570 ASP ASP B . n 
B 1 571 SER 571 571 571 SER SER B . n 
B 1 572 LEU 572 572 572 LEU LEU B . n 
B 1 573 THR 573 573 573 THR THR B . n 
B 1 574 GLY 574 574 574 GLY GLY B . n 
B 1 575 SER 575 575 575 SER SER B . n 
B 1 576 TYR 576 576 576 TYR TYR B . n 
B 1 577 LYS 577 577 577 LYS LYS B . n 
B 1 578 PRO 578 578 578 PRO PRO B . n 
B 1 579 LEU 579 579 579 LEU LEU B . n 
B 1 580 ASN 580 580 580 ASN ASN B . n 
B 1 581 ASP 581 581 581 ASP ASP B . n 
B 1 582 SER 582 582 582 SER SER B . n 
B 1 583 GLY 583 583 583 GLY GLY B . n 
B 1 584 VAL 584 584 584 VAL VAL B . n 
B 1 585 VAL 585 585 585 VAL VAL B . n 
B 1 586 LEU 586 586 586 LEU LEU B . n 
B 1 587 THR 587 587 587 THR THR B . n 
B 1 588 ALA 588 588 588 ALA ALA B . n 
B 1 589 SER 589 589 589 SER SER B . n 
B 1 590 VAL 590 590 590 VAL VAL B . n 
B 1 591 PRO 591 591 591 PRO PRO B . n 
B 1 592 ALA 592 592 592 ALA ALA B . n 
B 1 593 ASN 593 593 593 ASN ASN B . n 
B 1 594 TRP 594 594 594 TRP TRP B . n 
B 1 595 ARG 595 595 595 ARG ARG B . n 
B 1 596 THR 596 596 596 THR THR B . n 
B 1 597 ALA 597 597 597 ALA ALA B . n 
B 1 598 THR 598 598 598 THR THR B . n 
B 1 599 TYR 599 599 599 TYR TYR B . n 
B 1 600 SER 600 600 600 SER SER B . n 
B 1 601 TYR 601 601 601 TYR TYR B . n 
B 1 602 TYR 602 602 602 TYR TYR B . n 
B 1 603 ALA 603 603 603 ALA ALA B . n 
B 1 604 VAL 604 604 604 VAL VAL B . n 
B 1 605 PRO 605 605 605 PRO PRO B . n 
B 1 606 VAL 606 606 606 VAL VAL B . n 
B 1 607 ALA 607 607 607 ALA ALA B . n 
B 1 608 GLY 608 608 608 GLY GLY B . n 
B 1 609 LYS 609 609 609 LYS LYS B . n 
B 1 610 ASP 610 610 610 ASP ASP B . n 
B 1 611 ASP 611 611 611 ASP ASP B . n 
B 1 612 GLN 612 612 612 GLN GLN B . n 
B 1 613 VAL 613 613 613 VAL VAL B . n 
B 1 614 LEU 614 614 614 LEU LEU B . n 
B 1 615 VAL 615 615 615 VAL VAL B . n 
B 1 616 THR 616 616 616 THR THR B . n 
B 1 617 SER 617 617 617 SER SER B . n 
B 1 618 TYR 618 618 618 TYR TYR B . n 
B 1 619 MET 619 619 619 MET MET B . n 
B 1 620 THR 620 620 620 THR THR B . n 
B 1 621 ASN 621 621 621 ASN ASN B . n 
B 1 622 ARG 622 622 622 ARG ARG B . n 
B 1 623 ASN 623 623 623 ASN ASN B . n 
B 1 624 GLY 624 624 624 GLY GLY B . n 
B 1 625 VAL 625 625 625 VAL VAL B . n 
B 1 626 ALA 626 626 626 ALA ALA B . n 
B 1 627 GLY 627 627 627 GLY GLY B . n 
B 1 628 LYS 628 628 628 LYS LYS B . n 
B 1 629 GLY 629 629 629 GLY GLY B . n 
B 1 630 MET 630 630 630 MET MET B . n 
B 1 631 ASP 631 631 631 ASP ASP B . n 
B 1 632 SER 632 632 632 SER SER B . n 
B 1 633 THR 633 633 633 THR THR B . n 
B 1 634 TRP 634 634 634 TRP TRP B . n 
B 1 635 ALA 635 635 635 ALA ALA B . n 
B 1 636 PRO 636 636 636 PRO PRO B . n 
B 1 637 SER 637 637 637 SER SER B . n 
B 1 638 PHE 638 638 638 PHE PHE B . n 
B 1 639 LEU 639 639 639 LEU LEU B . n 
B 1 640 LEU 640 640 640 LEU LEU B . n 
B 1 641 GLN 641 641 641 GLN GLN B . n 
B 1 642 ILE 642 642 642 ILE ILE B . n 
B 1 643 ASN 643 643 643 ASN ASN B . n 
B 1 644 PRO 644 644 644 PRO PRO B . n 
B 1 645 ASP 645 645 645 ASP ASP B . n 
B 1 646 ASN 646 646 646 ASN ASN B . n 
B 1 647 THR 647 647 647 THR THR B . n 
B 1 648 THR 648 648 648 THR THR B . n 
B 1 649 THR 649 649 649 THR THR B . n 
B 1 650 VAL 650 650 650 VAL VAL B . n 
B 1 651 LEU 651 651 651 LEU LEU B . n 
B 1 652 ALA 652 652 652 ALA ALA B . n 
B 1 653 LYS 653 653 653 LYS LYS B . n 
B 1 654 MET 654 654 654 MET MET B . n 
B 1 655 THR 655 655 655 THR THR B . n 
B 1 656 ASN 656 656 656 ASN ASN B . n 
B 1 657 GLN 657 657 657 GLN GLN B . n 
B 1 658 GLY 658 658 658 GLY GLY B . n 
B 1 659 ASP 659 659 659 ASP ASP B . n 
B 1 660 TRP 660 660 660 TRP TRP B . n 
B 1 661 ILE 661 661 661 ILE ILE B . n 
B 1 662 TRP 662 662 662 TRP TRP B . n 
B 1 663 ASP 663 663 663 ASP ASP B . n 
B 1 664 ASP 664 664 664 ASP ASP B . n 
B 1 665 SER 665 665 665 SER SER B . n 
B 1 666 SER 666 666 666 SER SER B . n 
B 1 667 GLU 667 667 667 GLU GLU B . n 
B 1 668 ASN 668 668 668 ASN ASN B . n 
B 1 669 LEU 669 669 669 LEU LEU B . n 
B 1 670 ASP 670 670 670 ASP ASP B . n 
B 1 671 MET 671 671 671 MET MET B . n 
B 1 672 ILE 672 672 672 ILE ILE B . n 
B 1 673 GLY 673 673 673 GLY GLY B . n 
B 1 674 ASP 674 674 674 ASP ASP B . n 
B 1 675 LEU 675 675 675 LEU LEU B . n 
B 1 676 ASP 676 676 676 ASP ASP B . n 
B 1 677 SER 677 677 677 SER SER B . n 
B 1 678 ALA 678 678 678 ALA ALA B . n 
B 1 679 ALA 679 679 679 ALA ALA B . n 
B 1 680 LEU 680 680 680 LEU LEU B . n 
B 1 681 PRO 681 681 681 PRO PRO B . n 
B 1 682 GLY 682 682 682 GLY GLY B . n 
B 1 683 GLU 683 683 683 GLU GLU B . n 
B 1 684 ARG 684 684 684 ARG ARG B . n 
B 1 685 ASP 685 685 685 ASP ASP B . n 
B 1 686 LYS 686 686 686 LYS LYS B . n 
B 1 687 PRO 687 687 687 PRO PRO B . n 
B 1 688 VAL 688 688 688 VAL VAL B . n 
B 1 689 ASP 689 689 689 ASP ASP B . n 
B 1 690 TRP 690 690 690 TRP TRP B . n 
B 1 691 ASP 691 691 691 ASP ASP B . n 
B 1 692 LEU 692 692 692 LEU LEU B . n 
B 1 693 ILE 693 693 693 ILE ILE B . n 
B 1 694 GLY 694 694 694 GLY GLY B . n 
B 1 695 TYR 695 695 ?   ?   ?   B . n 
B 1 696 GLY 696 696 ?   ?   ?   B . n 
B 1 697 LEU 697 697 ?   ?   ?   B . n 
B 1 698 LYS 698 698 ?   ?   ?   B . n 
B 1 699 PRO 699 699 ?   ?   ?   B . n 
B 1 700 HIS 700 700 ?   ?   ?   B . n 
B 1 701 ASP 701 701 ?   ?   ?   B . n 
B 1 702 PRO 702 702 ?   ?   ?   B . n 
B 1 703 ALA 703 703 ?   ?   ?   B . n 
B 1 704 THR 704 704 ?   ?   ?   B . n 
B 1 705 PRO 705 705 ?   ?   ?   B . n 
B 1 706 ASN 706 706 ?   ?   ?   B . n 
B 1 707 ASP 707 707 ?   ?   ?   B . n 
B 1 708 PRO 708 708 ?   ?   ?   B . n 
B 1 709 GLU 709 709 ?   ?   ?   B . n 
B 1 710 THR 710 710 ?   ?   ?   B . n 
B 1 711 PRO 711 711 ?   ?   ?   B . n 
B 1 712 THR 712 712 ?   ?   ?   B . n 
B 1 713 THR 713 713 ?   ?   ?   B . n 
B 1 714 PRO 714 714 ?   ?   ?   B . n 
B 1 715 GLU 715 715 ?   ?   ?   B . n 
B 1 716 THR 716 716 ?   ?   ?   B . n 
B 1 717 PRO 717 717 ?   ?   ?   B . n 
B 1 718 GLU 718 718 ?   ?   ?   B . n 
B 1 719 THR 719 719 ?   ?   ?   B . n 
B 1 720 PRO 720 720 ?   ?   ?   B . n 
B 1 721 ASN 721 721 ?   ?   ?   B . n 
B 1 722 THR 722 722 ?   ?   ?   B . n 
B 1 723 PRO 723 723 ?   ?   ?   B . n 
B 1 724 LYS 724 724 ?   ?   ?   B . n 
B 1 725 THR 725 725 ?   ?   ?   B . n 
B 1 726 PRO 726 726 ?   ?   ?   B . n 
B 1 727 LYS 727 727 ?   ?   ?   B . n 
B 1 728 THR 728 728 ?   ?   ?   B . n 
B 1 729 PRO 729 729 ?   ?   ?   B . n 
B 1 730 GLU 730 730 ?   ?   ?   B . n 
B 1 731 ASN 731 731 ?   ?   ?   B . n 
B 1 732 PRO 732 732 ?   ?   ?   B . n 
B 1 733 GLY 733 733 ?   ?   ?   B . n 
B 1 734 THR 734 734 ?   ?   ?   B . n 
B 1 735 PRO 735 735 ?   ?   ?   B . n 
B 1 736 GLN 736 736 ?   ?   ?   B . n 
B 1 737 THR 737 737 ?   ?   ?   B . n 
B 1 738 PRO 738 738 ?   ?   ?   B . n 
B 1 739 ASN 739 739 ?   ?   ?   B . n 
B 1 740 THR 740 740 ?   ?   ?   B . n 
B 1 741 PRO 741 741 ?   ?   ?   B . n 
B 1 742 ASN 742 742 ?   ?   ?   B . n 
B 1 743 THR 743 743 ?   ?   ?   B . n 
B 1 744 PRO 744 744 ?   ?   ?   B . n 
B 1 745 GLU 745 745 ?   ?   ?   B . n 
B 1 746 ILE 746 746 ?   ?   ?   B . n 
B 1 747 PRO 747 747 ?   ?   ?   B . n 
B 1 748 LEU 748 748 ?   ?   ?   B . n 
B 1 749 THR 749 749 ?   ?   ?   B . n 
B 1 750 PRO 750 750 ?   ?   ?   B . n 
B 1 751 GLU 751 751 ?   ?   ?   B . n 
B 1 752 THR 752 752 ?   ?   ?   B . n 
B 1 753 PRO 753 753 ?   ?   ?   B . n 
B 1 754 LYS 754 754 ?   ?   ?   B . n 
B 1 755 GLN 755 755 ?   ?   ?   B . n 
B 1 756 PRO 756 756 ?   ?   ?   B . n 
B 1 757 GLU 757 757 ?   ?   ?   B . n 
B 1 758 THR 758 758 ?   ?   ?   B . n 
B 1 759 GLN 759 759 ?   ?   ?   B . n 
B 1 760 THR 760 760 ?   ?   ?   B . n 
B 1 761 ASN 761 761 ?   ?   ?   B . n 
B 1 762 ASN 762 762 ?   ?   ?   B . n 
B 1 763 ARG 763 763 ?   ?   ?   B . n 
B 1 764 LEU 764 764 ?   ?   ?   B . n 
B 1 765 PRO 765 765 ?   ?   ?   B . n 
B 1 766 GLN 766 766 ?   ?   ?   B . n 
B 1 767 THR 767 767 ?   ?   ?   B . n 
B 1 768 GLY 768 768 ?   ?   ?   B . n 
B 1 769 ASN 769 769 ?   ?   ?   B . n 
B 1 770 ASN 770 770 ?   ?   ?   B . n 
B 1 771 ALA 771 771 ?   ?   ?   B . n 
B 1 772 ASN 772 772 ?   ?   ?   B . n 
B 1 773 LYS 773 773 ?   ?   ?   B . n 
B 1 774 ALA 774 774 ?   ?   ?   B . n 
B 1 775 MET 775 775 ?   ?   ?   B . n 
B 1 776 ILE 776 776 ?   ?   ?   B . n 
B 1 777 GLY 777 777 ?   ?   ?   B . n 
B 1 778 LEU 778 778 ?   ?   ?   B . n 
B 1 779 GLY 779 779 ?   ?   ?   B . n 
B 1 780 MET 780 780 ?   ?   ?   B . n 
B 1 781 GLY 781 781 ?   ?   ?   B . n 
B 1 782 THR 782 782 ?   ?   ?   B . n 
B 1 783 LEU 783 783 ?   ?   ?   B . n 
B 1 784 LEU 784 784 ?   ?   ?   B . n 
B 1 785 SER 785 785 ?   ?   ?   B . n 
B 1 786 MET 786 786 ?   ?   ?   B . n 
B 1 787 PHE 787 787 ?   ?   ?   B . n 
B 1 788 GLY 788 788 ?   ?   ?   B . n 
B 1 789 LEU 789 789 ?   ?   ?   B . n 
B 1 790 ALA 790 790 ?   ?   ?   B . n 
B 1 791 GLU 791 791 ?   ?   ?   B . n 
B 1 792 ILE 792 792 ?   ?   ?   B . n 
B 1 793 ASN 793 793 ?   ?   ?   B . n 
B 1 794 LYS 794 794 ?   ?   ?   B . n 
B 1 795 ARG 795 795 ?   ?   ?   B . n 
B 1 796 ARG 796 796 ?   ?   ?   B . n 
B 1 797 PHE 797 797 ?   ?   ?   B . n 
B 1 798 ASN 798 798 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CA  ? ? CA  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FRU ? ? FRU ? ? '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 FRU 1   801  1   FRU FRU A . 
D 3 CA  1   802  1   CA  CA  A . 
E 3 CA  1   803  3   CA  CA  A . 
F 2 FRU 1   801  2   FRU FRU B . 
G 3 CA  1   802  2   CA  CA  B . 
H 3 CA  1   803  4   CA  CA  B . 
I 4 HOH 1   901  10  HOH HOH A . 
I 4 HOH 2   902  263 HOH HOH A . 
I 4 HOH 3   903  336 HOH HOH A . 
I 4 HOH 4   904  129 HOH HOH A . 
I 4 HOH 5   905  47  HOH HOH A . 
I 4 HOH 6   906  25  HOH HOH A . 
I 4 HOH 7   907  97  HOH HOH A . 
I 4 HOH 8   908  66  HOH HOH A . 
I 4 HOH 9   909  50  HOH HOH A . 
I 4 HOH 10  910  29  HOH HOH A . 
I 4 HOH 11  911  78  HOH HOH A . 
I 4 HOH 12  912  39  HOH HOH A . 
I 4 HOH 13  913  35  HOH HOH A . 
I 4 HOH 14  914  88  HOH HOH A . 
I 4 HOH 15  915  79  HOH HOH A . 
I 4 HOH 16  916  28  HOH HOH A . 
I 4 HOH 17  917  329 HOH HOH A . 
I 4 HOH 18  918  37  HOH HOH A . 
I 4 HOH 19  919  18  HOH HOH A . 
I 4 HOH 20  920  296 HOH HOH A . 
I 4 HOH 21  921  100 HOH HOH A . 
I 4 HOH 22  922  83  HOH HOH A . 
I 4 HOH 23  923  81  HOH HOH A . 
I 4 HOH 24  924  121 HOH HOH A . 
I 4 HOH 25  925  61  HOH HOH A . 
I 4 HOH 26  926  139 HOH HOH A . 
I 4 HOH 27  927  116 HOH HOH A . 
I 4 HOH 28  928  21  HOH HOH A . 
I 4 HOH 29  929  110 HOH HOH A . 
I 4 HOH 30  930  106 HOH HOH A . 
I 4 HOH 31  931  311 HOH HOH A . 
I 4 HOH 32  932  102 HOH HOH A . 
I 4 HOH 33  933  301 HOH HOH A . 
I 4 HOH 34  934  43  HOH HOH A . 
I 4 HOH 35  935  265 HOH HOH A . 
I 4 HOH 36  936  111 HOH HOH A . 
I 4 HOH 37  937  92  HOH HOH A . 
I 4 HOH 38  938  109 HOH HOH A . 
I 4 HOH 39  939  135 HOH HOH A . 
I 4 HOH 40  940  112 HOH HOH A . 
I 4 HOH 41  941  67  HOH HOH A . 
I 4 HOH 42  942  76  HOH HOH A . 
I 4 HOH 43  943  8   HOH HOH A . 
I 4 HOH 44  944  1   HOH HOH A . 
I 4 HOH 45  945  93  HOH HOH A . 
I 4 HOH 46  946  14  HOH HOH A . 
I 4 HOH 47  947  87  HOH HOH A . 
I 4 HOH 48  948  63  HOH HOH A . 
I 4 HOH 49  949  255 HOH HOH A . 
I 4 HOH 50  950  11  HOH HOH A . 
I 4 HOH 51  951  90  HOH HOH A . 
I 4 HOH 52  952  55  HOH HOH A . 
I 4 HOH 53  953  98  HOH HOH A . 
I 4 HOH 54  954  95  HOH HOH A . 
I 4 HOH 55  955  77  HOH HOH A . 
I 4 HOH 56  956  69  HOH HOH A . 
I 4 HOH 57  957  308 HOH HOH A . 
I 4 HOH 58  958  33  HOH HOH A . 
I 4 HOH 59  959  94  HOH HOH A . 
I 4 HOH 60  960  335 HOH HOH A . 
I 4 HOH 61  961  30  HOH HOH A . 
I 4 HOH 62  962  56  HOH HOH A . 
I 4 HOH 63  963  51  HOH HOH A . 
I 4 HOH 64  964  136 HOH HOH A . 
I 4 HOH 65  965  104 HOH HOH A . 
I 4 HOH 66  966  48  HOH HOH A . 
I 4 HOH 67  967  13  HOH HOH A . 
I 4 HOH 68  968  290 HOH HOH A . 
I 4 HOH 69  969  289 HOH HOH A . 
I 4 HOH 70  970  132 HOH HOH A . 
I 4 HOH 71  971  31  HOH HOH A . 
I 4 HOH 72  972  57  HOH HOH A . 
I 4 HOH 73  973  96  HOH HOH A . 
I 4 HOH 74  974  20  HOH HOH A . 
I 4 HOH 75  975  60  HOH HOH A . 
I 4 HOH 76  976  38  HOH HOH A . 
I 4 HOH 77  977  58  HOH HOH A . 
I 4 HOH 78  978  128 HOH HOH A . 
I 4 HOH 79  979  123 HOH HOH A . 
I 4 HOH 80  980  19  HOH HOH A . 
I 4 HOH 81  981  22  HOH HOH A . 
I 4 HOH 82  982  23  HOH HOH A . 
I 4 HOH 83  983  80  HOH HOH A . 
I 4 HOH 84  984  53  HOH HOH A . 
I 4 HOH 85  985  72  HOH HOH A . 
I 4 HOH 86  986  65  HOH HOH A . 
I 4 HOH 87  987  17  HOH HOH A . 
I 4 HOH 88  988  131 HOH HOH A . 
I 4 HOH 89  989  7   HOH HOH A . 
I 4 HOH 90  990  15  HOH HOH A . 
I 4 HOH 91  991  274 HOH HOH A . 
I 4 HOH 92  992  251 HOH HOH A . 
I 4 HOH 93  993  273 HOH HOH A . 
I 4 HOH 94  994  119 HOH HOH A . 
I 4 HOH 95  995  91  HOH HOH A . 
I 4 HOH 96  996  64  HOH HOH A . 
I 4 HOH 97  997  52  HOH HOH A . 
I 4 HOH 98  998  27  HOH HOH A . 
I 4 HOH 99  999  89  HOH HOH A . 
I 4 HOH 100 1000 99  HOH HOH A . 
I 4 HOH 101 1001 122 HOH HOH A . 
I 4 HOH 102 1002 253 HOH HOH A . 
I 4 HOH 103 1003 16  HOH HOH A . 
I 4 HOH 104 1004 74  HOH HOH A . 
I 4 HOH 105 1005 75  HOH HOH A . 
I 4 HOH 106 1006 254 HOH HOH A . 
I 4 HOH 107 1007 24  HOH HOH A . 
I 4 HOH 108 1008 45  HOH HOH A . 
I 4 HOH 109 1009 73  HOH HOH A . 
I 4 HOH 110 1010 140 HOH HOH A . 
I 4 HOH 111 1011 62  HOH HOH A . 
I 4 HOH 112 1012 292 HOH HOH A . 
I 4 HOH 113 1013 6   HOH HOH A . 
I 4 HOH 114 1014 130 HOH HOH A . 
I 4 HOH 115 1015 42  HOH HOH A . 
I 4 HOH 116 1016 32  HOH HOH A . 
I 4 HOH 117 1017 113 HOH HOH A . 
I 4 HOH 118 1018 49  HOH HOH A . 
I 4 HOH 119 1019 258 HOH HOH A . 
I 4 HOH 120 1020 309 HOH HOH A . 
I 4 HOH 121 1021 59  HOH HOH A . 
I 4 HOH 122 1022 134 HOH HOH A . 
I 4 HOH 123 1023 82  HOH HOH A . 
I 4 HOH 124 1024 34  HOH HOH A . 
I 4 HOH 125 1025 41  HOH HOH A . 
I 4 HOH 126 1026 54  HOH HOH A . 
I 4 HOH 127 1027 86  HOH HOH A . 
I 4 HOH 128 1028 70  HOH HOH A . 
I 4 HOH 129 1029 248 HOH HOH A . 
I 4 HOH 130 1030 275 HOH HOH A . 
I 4 HOH 131 1031 261 HOH HOH A . 
I 4 HOH 132 1032 120 HOH HOH A . 
I 4 HOH 133 1033 71  HOH HOH A . 
I 4 HOH 134 1034 126 HOH HOH A . 
I 4 HOH 135 1035 141 HOH HOH A . 
I 4 HOH 136 1036 26  HOH HOH A . 
I 4 HOH 137 1037 46  HOH HOH A . 
I 4 HOH 138 1038 68  HOH HOH A . 
I 4 HOH 139 1039 317 HOH HOH A . 
I 4 HOH 140 1040 300 HOH HOH A . 
I 4 HOH 141 1041 118 HOH HOH A . 
I 4 HOH 142 1042 40  HOH HOH A . 
I 4 HOH 143 1043 125 HOH HOH A . 
I 4 HOH 144 1044 318 HOH HOH A . 
I 4 HOH 145 1045 291 HOH HOH A . 
I 4 HOH 146 1046 107 HOH HOH A . 
I 4 HOH 147 1047 117 HOH HOH A . 
I 4 HOH 148 1048 103 HOH HOH A . 
I 4 HOH 149 1049 264 HOH HOH A . 
I 4 HOH 150 1050 114 HOH HOH A . 
I 4 HOH 151 1051 101 HOH HOH A . 
I 4 HOH 152 1052 108 HOH HOH A . 
I 4 HOH 153 1053 262 HOH HOH A . 
I 4 HOH 154 1054 138 HOH HOH A . 
I 4 HOH 155 1055 252 HOH HOH A . 
I 4 HOH 156 1056 330 HOH HOH A . 
I 4 HOH 157 1057 85  HOH HOH A . 
I 4 HOH 158 1058 124 HOH HOH A . 
I 4 HOH 159 1059 266 HOH HOH A . 
I 4 HOH 160 1060 306 HOH HOH A . 
I 4 HOH 161 1061 302 HOH HOH A . 
I 4 HOH 162 1062 84  HOH HOH A . 
I 4 HOH 163 1063 307 HOH HOH A . 
I 4 HOH 164 1064 319 HOH HOH A . 
I 4 HOH 165 1065 36  HOH HOH A . 
I 4 HOH 166 1066 310 HOH HOH A . 
I 4 HOH 167 1067 44  HOH HOH A . 
I 4 HOH 168 1068 115 HOH HOH A . 
I 4 HOH 169 1069 105 HOH HOH A . 
J 4 HOH 1   901  228 HOH HOH B . 
J 4 HOH 2   902  295 HOH HOH B . 
J 4 HOH 3   903  4   HOH HOH B . 
J 4 HOH 4   904  215 HOH HOH B . 
J 4 HOH 5   905  260 HOH HOH B . 
J 4 HOH 6   906  250 HOH HOH B . 
J 4 HOH 7   907  165 HOH HOH B . 
J 4 HOH 8   908  323 HOH HOH B . 
J 4 HOH 9   909  267 HOH HOH B . 
J 4 HOH 10  910  190 HOH HOH B . 
J 4 HOH 11  911  159 HOH HOH B . 
J 4 HOH 12  912  172 HOH HOH B . 
J 4 HOH 13  913  235 HOH HOH B . 
J 4 HOH 14  914  225 HOH HOH B . 
J 4 HOH 15  915  153 HOH HOH B . 
J 4 HOH 16  916  160 HOH HOH B . 
J 4 HOH 17  917  222 HOH HOH B . 
J 4 HOH 18  918  170 HOH HOH B . 
J 4 HOH 19  919  151 HOH HOH B . 
J 4 HOH 20  920  185 HOH HOH B . 
J 4 HOH 21  921  281 HOH HOH B . 
J 4 HOH 22  922  236 HOH HOH B . 
J 4 HOH 23  923  315 HOH HOH B . 
J 4 HOH 24  924  163 HOH HOH B . 
J 4 HOH 25  925  146 HOH HOH B . 
J 4 HOH 26  926  174 HOH HOH B . 
J 4 HOH 27  927  196 HOH HOH B . 
J 4 HOH 28  928  168 HOH HOH B . 
J 4 HOH 29  929  244 HOH HOH B . 
J 4 HOH 30  930  211 HOH HOH B . 
J 4 HOH 31  931  158 HOH HOH B . 
J 4 HOH 32  932  181 HOH HOH B . 
J 4 HOH 33  933  271 HOH HOH B . 
J 4 HOH 34  934  231 HOH HOH B . 
J 4 HOH 35  935  206 HOH HOH B . 
J 4 HOH 36  936  204 HOH HOH B . 
J 4 HOH 37  937  12  HOH HOH B . 
J 4 HOH 38  938  325 HOH HOH B . 
J 4 HOH 39  939  166 HOH HOH B . 
J 4 HOH 40  940  322 HOH HOH B . 
J 4 HOH 41  941  182 HOH HOH B . 
J 4 HOH 42  942  191 HOH HOH B . 
J 4 HOH 43  943  242 HOH HOH B . 
J 4 HOH 44  944  230 HOH HOH B . 
J 4 HOH 45  945  164 HOH HOH B . 
J 4 HOH 46  946  149 HOH HOH B . 
J 4 HOH 47  947  205 HOH HOH B . 
J 4 HOH 48  948  143 HOH HOH B . 
J 4 HOH 49  949  223 HOH HOH B . 
J 4 HOH 50  950  286 HOH HOH B . 
J 4 HOH 51  951  217 HOH HOH B . 
J 4 HOH 52  952  155 HOH HOH B . 
J 4 HOH 53  953  259 HOH HOH B . 
J 4 HOH 54  954  194 HOH HOH B . 
J 4 HOH 55  955  278 HOH HOH B . 
J 4 HOH 56  956  229 HOH HOH B . 
J 4 HOH 57  957  221 HOH HOH B . 
J 4 HOH 58  958  173 HOH HOH B . 
J 4 HOH 59  959  320 HOH HOH B . 
J 4 HOH 60  960  148 HOH HOH B . 
J 4 HOH 61  961  142 HOH HOH B . 
J 4 HOH 62  962  9   HOH HOH B . 
J 4 HOH 63  963  202 HOH HOH B . 
J 4 HOH 64  964  188 HOH HOH B . 
J 4 HOH 65  965  169 HOH HOH B . 
J 4 HOH 66  966  201 HOH HOH B . 
J 4 HOH 67  967  240 HOH HOH B . 
J 4 HOH 68  968  212 HOH HOH B . 
J 4 HOH 69  969  186 HOH HOH B . 
J 4 HOH 70  970  232 HOH HOH B . 
J 4 HOH 71  971  293 HOH HOH B . 
J 4 HOH 72  972  210 HOH HOH B . 
J 4 HOH 73  973  154 HOH HOH B . 
J 4 HOH 74  974  246 HOH HOH B . 
J 4 HOH 75  975  133 HOH HOH B . 
J 4 HOH 76  976  179 HOH HOH B . 
J 4 HOH 77  977  209 HOH HOH B . 
J 4 HOH 78  978  200 HOH HOH B . 
J 4 HOH 79  979  150 HOH HOH B . 
J 4 HOH 80  980  233 HOH HOH B . 
J 4 HOH 81  981  218 HOH HOH B . 
J 4 HOH 82  982  157 HOH HOH B . 
J 4 HOH 83  983  208 HOH HOH B . 
J 4 HOH 84  984  184 HOH HOH B . 
J 4 HOH 85  985  257 HOH HOH B . 
J 4 HOH 86  986  226 HOH HOH B . 
J 4 HOH 87  987  237 HOH HOH B . 
J 4 HOH 88  988  333 HOH HOH B . 
J 4 HOH 89  989  2   HOH HOH B . 
J 4 HOH 90  990  334 HOH HOH B . 
J 4 HOH 91  991  214 HOH HOH B . 
J 4 HOH 92  992  305 HOH HOH B . 
J 4 HOH 93  993  285 HOH HOH B . 
J 4 HOH 94  994  203 HOH HOH B . 
J 4 HOH 95  995  127 HOH HOH B . 
J 4 HOH 96  996  180 HOH HOH B . 
J 4 HOH 97  997  193 HOH HOH B . 
J 4 HOH 98  998  238 HOH HOH B . 
J 4 HOH 99  999  3   HOH HOH B . 
J 4 HOH 100 1000 299 HOH HOH B . 
J 4 HOH 101 1001 279 HOH HOH B . 
J 4 HOH 102 1002 145 HOH HOH B . 
J 4 HOH 103 1003 175 HOH HOH B . 
J 4 HOH 104 1004 147 HOH HOH B . 
J 4 HOH 105 1005 331 HOH HOH B . 
J 4 HOH 106 1006 152 HOH HOH B . 
J 4 HOH 107 1007 192 HOH HOH B . 
J 4 HOH 108 1008 161 HOH HOH B . 
J 4 HOH 109 1009 227 HOH HOH B . 
J 4 HOH 110 1010 272 HOH HOH B . 
J 4 HOH 111 1011 316 HOH HOH B . 
J 4 HOH 112 1012 284 HOH HOH B . 
J 4 HOH 113 1013 280 HOH HOH B . 
J 4 HOH 114 1014 326 HOH HOH B . 
J 4 HOH 115 1015 276 HOH HOH B . 
J 4 HOH 116 1016 167 HOH HOH B . 
J 4 HOH 117 1017 224 HOH HOH B . 
J 4 HOH 118 1018 187 HOH HOH B . 
J 4 HOH 119 1019 298 HOH HOH B . 
J 4 HOH 120 1020 283 HOH HOH B . 
J 4 HOH 121 1021 245 HOH HOH B . 
J 4 HOH 122 1022 189 HOH HOH B . 
J 4 HOH 123 1023 321 HOH HOH B . 
J 4 HOH 124 1024 198 HOH HOH B . 
J 4 HOH 125 1025 216 HOH HOH B . 
J 4 HOH 126 1026 247 HOH HOH B . 
J 4 HOH 127 1027 207 HOH HOH B . 
J 4 HOH 128 1028 195 HOH HOH B . 
J 4 HOH 129 1029 324 HOH HOH B . 
J 4 HOH 130 1030 219 HOH HOH B . 
J 4 HOH 131 1031 294 HOH HOH B . 
J 4 HOH 132 1032 213 HOH HOH B . 
J 4 HOH 133 1033 314 HOH HOH B . 
J 4 HOH 134 1034 137 HOH HOH B . 
J 4 HOH 135 1035 282 HOH HOH B . 
J 4 HOH 136 1036 304 HOH HOH B . 
J 4 HOH 137 1037 297 HOH HOH B . 
J 4 HOH 138 1038 243 HOH HOH B . 
J 4 HOH 139 1039 176 HOH HOH B . 
J 4 HOH 140 1040 220 HOH HOH B . 
J 4 HOH 141 1041 313 HOH HOH B . 
J 4 HOH 142 1042 332 HOH HOH B . 
J 4 HOH 143 1043 144 HOH HOH B . 
J 4 HOH 144 1044 249 HOH HOH B . 
J 4 HOH 145 1045 303 HOH HOH B . 
J 4 HOH 146 1046 327 HOH HOH B . 
J 4 HOH 147 1047 234 HOH HOH B . 
J 4 HOH 148 1048 5   HOH HOH B . 
J 4 HOH 149 1049 177 HOH HOH B . 
J 4 HOH 150 1050 183 HOH HOH B . 
J 4 HOH 151 1051 156 HOH HOH B . 
J 4 HOH 152 1052 241 HOH HOH B . 
J 4 HOH 153 1053 269 HOH HOH B . 
J 4 HOH 154 1054 287 HOH HOH B . 
J 4 HOH 155 1055 162 HOH HOH B . 
J 4 HOH 156 1056 328 HOH HOH B . 
J 4 HOH 157 1057 178 HOH HOH B . 
J 4 HOH 158 1058 268 HOH HOH B . 
J 4 HOH 159 1059 288 HOH HOH B . 
J 4 HOH 160 1060 197 HOH HOH B . 
J 4 HOH 161 1061 239 HOH HOH B . 
J 4 HOH 162 1062 199 HOH HOH B . 
J 4 HOH 163 1063 171 HOH HOH B . 
J 4 HOH 164 1064 312 HOH HOH B . 
J 4 HOH 165 1065 256 HOH HOH B . 
J 4 HOH 166 1066 270 HOH HOH B . 
# 
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  ? ? ? 5.8.0267 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XVQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     70.240 
_cell.length_a_esd                 ? 
_cell.length_b                     99.920 
_cell.length_b_esd                 ? 
_cell.length_c                     153.030 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XVQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8XVQ 
_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             1.55 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          20.50 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_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    
;0.1 M HEPES pH 7.5
25% w/v Polyethylene glycol 3,350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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         2023-11-02 
_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   0.97854 
_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 BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97854 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XVQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.14 
_reflns.d_resolution_low                               50 
_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                                     59439 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.94 
_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                                0.123 
_reflns.pdbx_Rpim_I_all                                0.035 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.118 
_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                                    2.14 
_reflns_shell.d_res_low                                     2.20 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           25239 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4085 
_reflns_shell.percent_possible_obs                          89.4 
_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                               6.2 
_reflns_shell.pdbx_chi_squared                              0.68 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     5.7 
_reflns_shell.pdbx_Rrim_I_all                               0.375 
_reflns_shell.pdbx_Rpim_I_all                               0.143 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.944 
_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                                  0.346 
_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]                            -0.89 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.60 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            1.49 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.801 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.912 
_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                                 8XVQ 
_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                            2.14 
_refine.ls_d_res_low                             47.54 
_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                     56361 
_refine.ls_number_reflns_R_free                  3015 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.67 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18010 
_refine.ls_R_factor_R_free                       0.22713 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17762 
_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                       0.239 
_refine.pdbx_overall_ESU_R_Free                  0.193 
_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                             4.494 
_refine.overall_SU_ML                            0.119 
_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                       2.14 
_refine_hist.d_res_low                        47.54 
_refine_hist.number_atoms_solvent             335 
_refine_hist.number_atoms_total               8478 
_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        8115 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_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' ? 0.008  0.020  8354  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  7563  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.276  1.933  11356 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.745  3.000  17385 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.611  5.000  1037  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 36.863 25.976 420   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.146 15.000 1328  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.307 15.000 26    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.075  0.200  1239  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  9762  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1920  ? 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' ? 1.225  2.393  4158  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.223  2.394  4151  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.003  3.585  5182  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.003  3.585  5183  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.442  2.537  4196  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.442  2.537  4196  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.341  3.732  6174  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.725  28.095 9757  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.662  27.971 9662  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.140 
_refine_ls_shell.d_res_low                        2.196 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             223 
_refine_ls_shell.number_reflns_R_work             3621 
_refine_ls_shell.percent_reflns_obs               87.80 
_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                  0.195 
_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                  0.249 
# 
_struct.entry_id                     8XVQ 
_struct.title                        'Crystal structure of inulosucrase from Lactobacillus reuteri 121 in complex with fructose' 
_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        8XVQ 
_struct_keywords.text            'Glycoside hydrolase 68 enzyme, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8GP32_LIMRT 
_struct_ref.pdbx_db_accession          Q8GP32 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLERKEHKKMYKSGKNWAVVTLSTAALVFGATTVNASADTNIENNDSSTVQVTTGDNDIAVKSVTLGSGQVSAASDTTIR
TSANANSASSAANTQNSNSQVASSAAITSSTSSAASSNNTDSKAAQENTNTAKNDDTQKAAPANESSEAKNEPAVNVNDS
SAAKNDDQQSSKKNTTAKLNKDAENVVKKAGIDPNSLTDDQIKALNKMNFSKAAKSGTQMTYNDFQKIADTLIKQDGRYT
VPFFKASEIKNMPAATTKDAQTNTIEPLDVWDSWPVQDVRTGQVANWNGYQLVIAMMGIPNQNDNHIYLLYNKYGDNELS
HWKNVGPIFGYNSTAVSQEWSGSAVLNSDNSIQLFYTRVDTSDNNTNHQKIASATLYLTDNNGNVSLAQVANDHIVFEGD
GYYYQTYDQWKATNKGADNIAMRDAHVIEDDNGDRYLVFEASTGLENYQGEDQIYNWLNYGGDDAFNIKSLFRILSNDDI
KSRATWANAAIGILKLNKDEKNPKVAELYSPLISAPMVSDEIERPNVVKLGNKYYLFAATRLNRGSNDDAWMNANYAVGD
NVAMVGYVADSLTGSYKPLNDSGVVLTASVPANWRTATYSYYAVPVAGKDDQVLVTSYMTNRNGVAGKGMDSTWAPSFLL
QINPDNTTTVLAKMTNQGDWIWDDSSENLDMIGDLDSAALPGERDKPVDWDLIGYGLKPHDPATPNDPETPTTPETPETP
NTPKTPKTPENPGTPQTPNTPNTPEIPLTPETPKQPETQTNNRLPQTGNNANKAMIGLGMGTLLSMFGLAEINKRRFN
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8XVQ A 1 ? 798 ? Q8GP32 1 ? 798 ? 1 798 
2 1 8XVQ B 1 ? 798 ? Q8GP32 1 ? 798 ? 1 798 
# 
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_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 90    ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  19620 ? 
2 'ABSA (A^2)' 90    ? 
2 MORE         -13   ? 
2 'SSA (A^2)'  19530 ? 
# 
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,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 180 ? ALA A 190 ? ASN A 180 ALA A 190 1 ? 11 
HELX_P HELX_P2  AA2 ASP A 193 ? LEU A 197 ? ASP A 193 LEU A 197 5 ? 5  
HELX_P HELX_P3  AA3 THR A 198 ? LYS A 207 ? THR A 198 LYS A 207 1 ? 10 
HELX_P HELX_P4  AA4 THR A 221 ? GLN A 235 ? THR A 221 GLN A 235 1 ? 15 
HELX_P HELX_P5  AA5 LYS A 245 ? ILE A 249 ? LYS A 245 ILE A 249 5 ? 5  
HELX_P HELX_P6  AA6 MET A 252 ? ALA A 254 ? MET A 252 ALA A 254 5 ? 3  
HELX_P HELX_P7  AA7 GLU A 318 ? TRP A 322 ? GLU A 318 TRP A 322 5 ? 5  
HELX_P HELX_P8  AA8 THR A 406 ? ASN A 414 ? THR A 406 ASN A 414 1 ? 9  
HELX_P HELX_P9  AA9 GLY A 450 ? TYR A 460 ? GLY A 450 TYR A 460 5 ? 11 
HELX_P HELX_P10 AB1 ASP A 463 ? ASN A 477 ? ASP A 463 ASN A 477 1 ? 15 
HELX_P HELX_P11 AB2 ASN A 477 ? ALA A 487 ? ASN A 477 ALA A 487 1 ? 11 
HELX_P HELX_P12 AB3 ASN A 543 ? GLY A 545 ? ASN A 543 GLY A 545 5 ? 3  
HELX_P HELX_P13 AB4 ASN A 547 ? GLY A 559 ? ASN A 547 GLY A 559 1 ? 13 
HELX_P HELX_P14 AB5 ASP A 663 ? GLU A 667 ? ASP A 663 GLU A 667 5 ? 5  
HELX_P HELX_P15 AB6 ASN A 668 ? ILE A 672 ? ASN A 668 ILE A 672 5 ? 5  
HELX_P HELX_P16 AB7 GLY A 682 ? LYS A 686 ? GLY A 682 LYS A 686 5 ? 5  
HELX_P HELX_P17 AB8 ASP A 689 ? GLY A 694 ? ASP A 689 GLY A 694 1 ? 6  
HELX_P HELX_P18 AB9 ASN B 180 ? ALA B 190 ? ASN B 180 ALA B 190 1 ? 11 
HELX_P HELX_P19 AC1 ASP B 193 ? LEU B 197 ? ASP B 193 LEU B 197 5 ? 5  
HELX_P HELX_P20 AC2 THR B 198 ? MET B 208 ? THR B 198 MET B 208 1 ? 11 
HELX_P HELX_P21 AC3 THR B 221 ? GLN B 235 ? THR B 221 GLN B 235 1 ? 15 
HELX_P HELX_P22 AC4 LYS B 245 ? ILE B 249 ? LYS B 245 ILE B 249 5 ? 5  
HELX_P HELX_P23 AC5 MET B 252 ? ALA B 254 ? MET B 252 ALA B 254 5 ? 3  
HELX_P HELX_P24 AC6 GLU B 318 ? TRP B 322 ? GLU B 318 TRP B 322 5 ? 5  
HELX_P HELX_P25 AC7 THR B 406 ? ASN B 414 ? THR B 406 ASN B 414 1 ? 9  
HELX_P HELX_P26 AC8 GLY B 450 ? TYR B 460 ? GLY B 450 TYR B 460 5 ? 11 
HELX_P HELX_P27 AC9 ASP B 463 ? ASN B 477 ? ASP B 463 ASN B 477 1 ? 15 
HELX_P HELX_P28 AD1 ASN B 477 ? ALA B 487 ? ASN B 477 ALA B 487 1 ? 11 
HELX_P HELX_P29 AD2 ASN B 543 ? GLY B 545 ? ASN B 543 GLY B 545 5 ? 3  
HELX_P HELX_P30 AD3 ASN B 547 ? GLY B 559 ? ASN B 547 GLY B 559 1 ? 13 
HELX_P HELX_P31 AD4 ASP B 663 ? GLU B 667 ? ASP B 663 GLU B 667 5 ? 5  
HELX_P HELX_P32 AD5 ASN B 668 ? ILE B 672 ? ASN B 668 ILE B 672 5 ? 5  
HELX_P HELX_P33 AD6 GLY B 682 ? LYS B 686 ? GLY B 682 LYS B 686 5 ? 5  
HELX_P HELX_P34 AD7 ASP B 689 ? GLY B 694 ? ASP B 689 GLY B 694 1 ? 6  
# 
_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 
metalc1  metalc ? ? A ASN 317 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASN 317 A CA  803  1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc2  metalc ? ? A ASP 418 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 418 A CA  802  1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc3  metalc ? ? A GLN 449 OE1 ? ? ? 1_555 D CA  . CA ? ? A GLN 449 A CA  802  1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc4  metalc ? ? A TRP 486 O   ? ? ? 1_555 D CA  . CA ? ? A TRP 486 A CA  802  1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc5  metalc ? ? A ASN 488 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASN 488 A CA  802  1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc6  metalc ? ? A ASP 520 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 520 A CA  802  1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc7  metalc ? ? A ASP 520 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 520 A CA  802  1_555 ? ? ? ? ? ? ? 2.562 ? ? 
metalc8  metalc ? ? A ASP 659 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 659 A CA  803  1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc9  metalc ? ? A ASP 659 OD2 ? ? ? 1_555 E CA  . CA ? ? A ASP 659 A CA  803  1_555 ? ? ? ? ? ? ? 2.681 ? ? 
metalc10 metalc ? ? A ILE 661 O   ? ? ? 1_555 E CA  . CA ? ? A ILE 661 A CA  803  1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc11 metalc ? ? A SER 666 OG  ? ? ? 1_555 E CA  . CA ? ? A SER 666 A CA  803  1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc12 metalc ? ? D CA  .   CA  ? ? ? 1_555 I HOH . O  ? ? A CA  802 A HOH 944  1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc13 metalc ? ? E CA  .   CA  ? ? ? 1_555 I HOH . O  ? ? A CA  803 A HOH 989  1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc14 metalc ? ? E CA  .   CA  ? ? ? 1_555 I HOH . O  ? ? A CA  803 A HOH 1013 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc15 metalc ? ? B ASN 317 OD1 ? ? ? 1_555 G CA  . CA ? ? B ASN 317 B CA  802  1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc16 metalc ? ? B ASP 418 OD1 ? ? ? 1_555 H CA  . CA ? ? B ASP 418 B CA  803  1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc17 metalc ? ? B GLN 449 OE1 ? ? ? 1_555 H CA  . CA ? ? B GLN 449 B CA  803  1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc18 metalc ? ? B TRP 486 O   ? ? ? 1_555 H CA  . CA ? ? B TRP 486 B CA  803  1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc19 metalc ? ? B ASN 488 OD1 ? ? ? 1_555 H CA  . CA ? ? B ASN 488 B CA  803  1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc20 metalc ? ? B ASP 520 OD1 ? ? ? 1_555 H CA  . CA ? ? B ASP 520 B CA  803  1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc21 metalc ? ? B ASP 520 OD2 ? ? ? 1_555 H CA  . CA ? ? B ASP 520 B CA  803  1_555 ? ? ? ? ? ? ? 2.604 ? ? 
metalc22 metalc ? ? B ASP 659 OD1 ? ? ? 1_555 G CA  . CA ? ? B ASP 659 B CA  802  1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc23 metalc ? ? B ASP 659 OD2 ? ? ? 1_555 G CA  . CA ? ? B ASP 659 B CA  802  1_555 ? ? ? ? ? ? ? 2.527 ? ? 
metalc24 metalc ? ? B ILE 661 O   ? ? ? 1_555 G CA  . CA ? ? B ILE 661 B CA  802  1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc25 metalc ? ? B SER 666 OG  ? ? ? 1_555 G CA  . CA ? ? B SER 666 B CA  802  1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc26 metalc ? ? G CA  .   CA  ? ? ? 1_555 J HOH . O  ? ? B CA  802 B HOH 989  1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc27 metalc ? ? G CA  .   CA  ? ? ? 1_555 J HOH . O  ? ? B CA  802 B HOH 999  1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc28 metalc ? ? H CA  .   CA  ? ? ? 1_555 J HOH . O  ? ? B CA  803 B HOH 962  1_555 ? ? ? ? ? ? ? 2.335 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  OD1 ? A ASN 317 ? A ASN 317 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OD1 ? A ASP 659 ? A ASP 659  ? 1_555 105.5 ? 
2  OD1 ? A ASN 317 ? A ASN 317 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OD2 ? A ASP 659 ? A ASP 659  ? 1_555 80.2  ? 
3  OD1 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OD2 ? A ASP 659 ? A ASP 659  ? 1_555 50.8  ? 
4  OD1 ? A ASN 317 ? A ASN 317 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? A ILE 661 ? A ILE 661  ? 1_555 173.2 ? 
5  OD1 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? A ILE 661 ? A ILE 661  ? 1_555 81.2  ? 
6  OD2 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? A ILE 661 ? A ILE 661  ? 1_555 105.6 ? 
7  OD1 ? A ASN 317 ? A ASN 317 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OG  ? A SER 666 ? A SER 666  ? 1_555 94.4  ? 
8  OD1 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OG  ? A SER 666 ? A SER 666  ? 1_555 124.2 ? 
9  OD2 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OG  ? A SER 666 ? A SER 666  ? 1_555 83.7  ? 
10 O   ? A ILE 661 ? A ILE 661 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OG  ? A SER 666 ? A SER 666  ? 1_555 82.7  ? 
11 OD1 ? A ASN 317 ? A ASN 317 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 989  ? 1_555 83.2  ? 
12 OD1 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 989  ? 1_555 151.6 ? 
13 OD2 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 989  ? 1_555 156.4 ? 
14 O   ? A ILE 661 ? A ILE 661 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 989  ? 1_555 90.2  ? 
15 OG  ? A SER 666 ? A SER 666 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 989  ? 1_555 80.9  ? 
16 OD1 ? A ASN 317 ? A ASN 317 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 1013 ? 1_555 76.8  ? 
17 OD1 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 1013 ? 1_555 74.6  ? 
18 OD2 ? A ASP 659 ? A ASP 659 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 1013 ? 1_555 110.7 ? 
19 O   ? A ILE 661 ? A ILE 661 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 1013 ? 1_555 104.0 ? 
20 OG  ? A SER 666 ? A SER 666 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 1013 ? 1_555 161.1 ? 
21 O   ? I HOH .   ? A HOH 989 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? I HOH .   ? A HOH 1013 ? 1_555 81.4  ? 
22 OD1 ? A ASP 418 ? A ASP 418 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OE1 ? A GLN 449 ? A GLN 449  ? 1_555 83.1  ? 
23 OD1 ? A ASP 418 ? A ASP 418 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? A TRP 486 ? A TRP 486  ? 1_555 98.9  ? 
24 OE1 ? A GLN 449 ? A GLN 449 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? A TRP 486 ? A TRP 486  ? 1_555 86.9  ? 
25 OD1 ? A ASP 418 ? A ASP 418 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASN 488 ? A ASN 488  ? 1_555 152.5 ? 
26 OE1 ? A GLN 449 ? A GLN 449 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASN 488 ? A ASN 488  ? 1_555 75.8  ? 
27 O   ? A TRP 486 ? A TRP 486 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASN 488 ? A ASN 488  ? 1_555 97.4  ? 
28 OD1 ? A ASP 418 ? A ASP 418 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 520 ? A ASP 520  ? 1_555 129.5 ? 
29 OE1 ? A GLN 449 ? A GLN 449 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 520 ? A ASP 520  ? 1_555 146.8 ? 
30 O   ? A TRP 486 ? A TRP 486 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 520 ? A ASP 520  ? 1_555 82.0  ? 
31 OD1 ? A ASN 488 ? A ASN 488 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 520 ? A ASP 520  ? 1_555 74.7  ? 
32 OD1 ? A ASP 418 ? A ASP 418 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD2 ? A ASP 520 ? A ASP 520  ? 1_555 77.3  ? 
33 OE1 ? A GLN 449 ? A GLN 449 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD2 ? A ASP 520 ? A ASP 520  ? 1_555 152.8 ? 
34 O   ? A TRP 486 ? A TRP 486 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD2 ? A ASP 520 ? A ASP 520  ? 1_555 77.9  ? 
35 OD1 ? A ASN 488 ? A ASN 488 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD2 ? A ASP 520 ? A ASP 520  ? 1_555 128.1 ? 
36 OD1 ? A ASP 520 ? A ASP 520 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD2 ? A ASP 520 ? A ASP 520  ? 1_555 53.3  ? 
37 OD1 ? A ASP 418 ? A ASP 418 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? I HOH .   ? A HOH 944  ? 1_555 77.5  ? 
38 OE1 ? A GLN 449 ? A GLN 449 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? I HOH .   ? A HOH 944  ? 1_555 99.4  ? 
39 O   ? A TRP 486 ? A TRP 486 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? I HOH .   ? A HOH 944  ? 1_555 172.3 ? 
40 OD1 ? A ASN 488 ? A ASN 488 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? I HOH .   ? A HOH 944  ? 1_555 88.6  ? 
41 OD1 ? A ASP 520 ? A ASP 520 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? I HOH .   ? A HOH 944  ? 1_555 94.9  ? 
42 OD2 ? A ASP 520 ? A ASP 520 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? I HOH .   ? A HOH 944  ? 1_555 94.6  ? 
43 OD1 ? B ASN 317 ? B ASN 317 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 OD1 ? B ASP 659 ? B ASP 659  ? 1_555 112.2 ? 
44 OD1 ? B ASN 317 ? B ASN 317 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 OD2 ? B ASP 659 ? B ASP 659  ? 1_555 81.2  ? 
45 OD1 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 OD2 ? B ASP 659 ? B ASP 659  ? 1_555 53.9  ? 
46 OD1 ? B ASN 317 ? B ASN 317 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? B ILE 661 ? B ILE 661  ? 1_555 167.7 ? 
47 OD1 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? B ILE 661 ? B ILE 661  ? 1_555 79.7  ? 
48 OD2 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? B ILE 661 ? B ILE 661  ? 1_555 104.5 ? 
49 OD1 ? B ASN 317 ? B ASN 317 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 OG  ? B SER 666 ? B SER 666  ? 1_555 89.0  ? 
50 OD1 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 OG  ? B SER 666 ? B SER 666  ? 1_555 126.3 ? 
51 OD2 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 OG  ? B SER 666 ? B SER 666  ? 1_555 84.1  ? 
52 O   ? B ILE 661 ? B ILE 661 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 OG  ? B SER 666 ? B SER 666  ? 1_555 80.9  ? 
53 OD1 ? B ASN 317 ? B ASN 317 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 989  ? 1_555 79.8  ? 
54 OD1 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 989  ? 1_555 150.0 ? 
55 OD2 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 989  ? 1_555 155.0 ? 
56 O   ? B ILE 661 ? B ILE 661 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 989  ? 1_555 91.4  ? 
57 OG  ? B SER 666 ? B SER 666 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 989  ? 1_555 79.4  ? 
58 OD1 ? B ASN 317 ? B ASN 317 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 999  ? 1_555 77.8  ? 
59 OD1 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 999  ? 1_555 73.9  ? 
60 OD2 ? B ASP 659 ? B ASP 659 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 999  ? 1_555 109.0 ? 
61 O   ? B ILE 661 ? B ILE 661 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 999  ? 1_555 109.8 ? 
62 OG  ? B SER 666 ? B SER 666 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 999  ? 1_555 159.3 ? 
63 O   ? J HOH .   ? B HOH 989 ? 1_555 CA ? G CA . ? B CA 802 ? 1_555 O   ? J HOH .   ? B HOH 999  ? 1_555 82.6  ? 
64 OD1 ? B ASP 418 ? B ASP 418 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OE1 ? B GLN 449 ? B GLN 449  ? 1_555 78.0  ? 
65 OD1 ? B ASP 418 ? B ASP 418 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? B TRP 486 ? B TRP 486  ? 1_555 96.5  ? 
66 OE1 ? B GLN 449 ? B GLN 449 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? B TRP 486 ? B TRP 486  ? 1_555 82.4  ? 
67 OD1 ? B ASP 418 ? B ASP 418 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD1 ? B ASN 488 ? B ASN 488  ? 1_555 152.3 ? 
68 OE1 ? B GLN 449 ? B GLN 449 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD1 ? B ASN 488 ? B ASN 488  ? 1_555 77.5  ? 
69 O   ? B TRP 486 ? B TRP 486 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD1 ? B ASN 488 ? B ASN 488  ? 1_555 92.8  ? 
70 OD1 ? B ASP 418 ? B ASP 418 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD1 ? B ASP 520 ? B ASP 520  ? 1_555 129.1 ? 
71 OE1 ? B GLN 449 ? B GLN 449 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD1 ? B ASP 520 ? B ASP 520  ? 1_555 151.3 ? 
72 O   ? B TRP 486 ? B TRP 486 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD1 ? B ASP 520 ? B ASP 520  ? 1_555 84.7  ? 
73 OD1 ? B ASN 488 ? B ASN 488 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD1 ? B ASP 520 ? B ASP 520  ? 1_555 77.6  ? 
74 OD1 ? B ASP 418 ? B ASP 418 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD2 ? B ASP 520 ? B ASP 520  ? 1_555 78.0  ? 
75 OE1 ? B GLN 449 ? B GLN 449 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD2 ? B ASP 520 ? B ASP 520  ? 1_555 150.0 ? 
76 O   ? B TRP 486 ? B TRP 486 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD2 ? B ASP 520 ? B ASP 520  ? 1_555 82.7  ? 
77 OD1 ? B ASN 488 ? B ASN 488 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD2 ? B ASP 520 ? B ASP 520  ? 1_555 129.2 ? 
78 OD1 ? B ASP 520 ? B ASP 520 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 OD2 ? B ASP 520 ? B ASP 520  ? 1_555 51.6  ? 
79 OD1 ? B ASP 418 ? B ASP 418 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? J HOH .   ? B HOH 962  ? 1_555 82.1  ? 
80 OE1 ? B GLN 449 ? B GLN 449 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? J HOH .   ? B HOH 962  ? 1_555 102.4 ? 
81 O   ? B TRP 486 ? B TRP 486 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? J HOH .   ? B HOH 962  ? 1_555 174.6 ? 
82 OD1 ? B ASN 488 ? B ASN 488 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? J HOH .   ? B HOH 962  ? 1_555 90.8  ? 
83 OD1 ? B ASP 520 ? B ASP 520 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? J HOH .   ? B HOH 962  ? 1_555 92.1  ? 
84 OD2 ? B ASP 520 ? B ASP 520 ? 1_555 CA ? H CA . ? B CA 803 ? 1_555 O   ? J HOH .   ? B HOH 962  ? 1_555 91.9  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 8 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 3 ? 
AA8 ? 4 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 2 ? 
AB3 ? 8 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 3 ? 
AB7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? parallel      
AB3 5 6 ? anti-parallel 
AB3 6 7 ? anti-parallel 
AB3 7 8 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 218 ? GLN A 219 ? THR A 218 GLN A 219 
AA1 2 ILE A 513 ? SER A 514 ? ILE A 513 SER A 514 
AA1 3 ALA A 489 ? LEU A 496 ? ALA A 489 LEU A 496 
AA1 4 ARG A 435 ? SER A 442 ? ARG A 435 SER A 442 
AA1 5 ARG A 423 ? GLU A 429 ? ARG A 423 GLU A 429 
AA2 1 THR A 218 ? GLN A 219 ? THR A 218 GLN A 219 
AA2 2 ILE A 513 ? SER A 514 ? ILE A 513 SER A 514 
AA2 3 ALA A 489 ? LEU A 496 ? ALA A 489 LEU A 496 
AA2 4 VAL A 505 ? LEU A 508 ? VAL A 505 LEU A 508 
AA3 1 THR A 256 ? LYS A 258 ? THR A 256 LYS A 258 
AA3 2 ILE A 265 ? PRO A 267 ? ILE A 265 PRO A 267 
AA4 1 LYS A 323 ? PRO A 327 ? LYS A 323 PRO A 327 
AA4 2 HIS A 306 ? LYS A 313 ? HIS A 306 LYS A 313 
AA4 3 TYR A 290 ? GLY A 298 ? TYR A 290 GLY A 298 
AA4 4 ASP A 269 ? GLN A 277 ? ASP A 269 GLN A 277 
AA4 5 SER A 337 ? LEU A 346 ? SER A 337 LEU A 346 
AA4 6 ILE A 352 ? ASP A 360 ? ILE A 352 ASP A 360 
AA4 7 HIS A 368 ? ASN A 381 ? HIS A 368 ASN A 381 
AA4 8 ASN A 384 ? PHE A 397 ? ASN A 384 PHE A 397 
AA5 1 GLU A 523 ? LEU A 530 ? GLU A 523 LEU A 530 
AA5 2 LYS A 533 ? ARG A 541 ? LYS A 533 ARG A 541 
AA5 3 VAL A 562 ? ALA A 569 ? VAL A 562 ALA A 569 
AA5 4 LYS A 577 ? PRO A 578 ? LYS A 577 PRO A 578 
AA6 1 GLU A 523 ? LEU A 530 ? GLU A 523 LEU A 530 
AA6 2 LYS A 533 ? ARG A 541 ? LYS A 533 ARG A 541 
AA6 3 VAL A 562 ? ALA A 569 ? VAL A 562 ALA A 569 
AA6 4 VAL A 584 ? THR A 587 ? VAL A 584 THR A 587 
AA7 1 THR A 598 ? PRO A 605 ? THR A 598 PRO A 605 
AA7 2 GLN A 612 ? MET A 619 ? GLN A 612 MET A 619 
AA7 3 THR A 633 ? TRP A 634 ? THR A 633 TRP A 634 
AA8 1 THR A 598 ? PRO A 605 ? THR A 598 PRO A 605 
AA8 2 GLN A 612 ? MET A 619 ? GLN A 612 MET A 619 
AA8 3 PRO A 636 ? ASN A 643 ? PRO A 636 ASN A 643 
AA8 4 THR A 647 ? GLN A 657 ? THR A 647 GLN A 657 
AA9 1 THR B 218 ? GLN B 219 ? THR B 218 GLN B 219 
AA9 2 ILE B 513 ? SER B 514 ? ILE B 513 SER B 514 
AA9 3 ALA B 489 ? LEU B 496 ? ALA B 489 LEU B 496 
AA9 4 ARG B 435 ? SER B 442 ? ARG B 435 SER B 442 
AA9 5 ARG B 423 ? GLU B 429 ? ARG B 423 GLU B 429 
AB1 1 THR B 218 ? GLN B 219 ? THR B 218 GLN B 219 
AB1 2 ILE B 513 ? SER B 514 ? ILE B 513 SER B 514 
AB1 3 ALA B 489 ? LEU B 496 ? ALA B 489 LEU B 496 
AB1 4 VAL B 505 ? LEU B 508 ? VAL B 505 LEU B 508 
AB2 1 THR B 256 ? LYS B 258 ? THR B 256 LYS B 258 
AB2 2 ILE B 265 ? PRO B 267 ? ILE B 265 PRO B 267 
AB3 1 LYS B 323 ? PRO B 327 ? LYS B 323 PRO B 327 
AB3 2 HIS B 306 ? LYS B 313 ? HIS B 306 LYS B 313 
AB3 3 TYR B 290 ? GLY B 298 ? TYR B 290 GLY B 298 
AB3 4 ASP B 269 ? GLN B 277 ? ASP B 269 GLN B 277 
AB3 5 SER B 337 ? LEU B 346 ? SER B 337 LEU B 346 
AB3 6 ILE B 352 ? ASP B 360 ? ILE B 352 ASP B 360 
AB3 7 HIS B 368 ? ASN B 381 ? HIS B 368 ASN B 381 
AB3 8 ASN B 384 ? PHE B 397 ? ASN B 384 PHE B 397 
AB4 1 GLU B 523 ? LEU B 530 ? GLU B 523 LEU B 530 
AB4 2 LYS B 533 ? ARG B 541 ? LYS B 533 ARG B 541 
AB4 3 VAL B 562 ? ALA B 569 ? VAL B 562 ALA B 569 
AB4 4 LYS B 577 ? PRO B 578 ? LYS B 577 PRO B 578 
AB5 1 GLU B 523 ? LEU B 530 ? GLU B 523 LEU B 530 
AB5 2 LYS B 533 ? ARG B 541 ? LYS B 533 ARG B 541 
AB5 3 VAL B 562 ? ALA B 569 ? VAL B 562 ALA B 569 
AB5 4 VAL B 584 ? THR B 587 ? VAL B 584 THR B 587 
AB6 1 THR B 598 ? VAL B 606 ? THR B 598 VAL B 606 
AB6 2 LYS B 609 ? MET B 619 ? LYS B 609 MET B 619 
AB6 3 THR B 633 ? TRP B 634 ? THR B 633 TRP B 634 
AB7 1 THR B 598 ? VAL B 606 ? THR B 598 VAL B 606 
AB7 2 LYS B 609 ? MET B 619 ? LYS B 609 MET B 619 
AB7 3 PRO B 636 ? ILE B 642 ? PRO B 636 ILE B 642 
AB7 4 THR B 648 ? GLN B 657 ? THR B 648 GLN B 657 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 218 ? N THR A 218 O SER A 514 ? O SER A 514 
AA1 2 3 O ILE A 513 ? O ILE A 513 N ILE A 491 ? N ILE A 491 
AA1 3 4 O LEU A 496 ? O LEU A 496 N ARG A 435 ? N ARG A 435 
AA1 4 5 O VAL A 438 ? O VAL A 438 N HIS A 426 ? N HIS A 426 
AA2 1 2 N THR A 218 ? N THR A 218 O SER A 514 ? O SER A 514 
AA2 2 3 O ILE A 513 ? O ILE A 513 N ILE A 491 ? N ILE A 491 
AA2 3 4 N LYS A 495 ? N LYS A 495 O ALA A 506 ? O ALA A 506 
AA3 1 2 N THR A 257 ? N THR A 257 O GLU A 266 ? O GLU A 266 
AA4 1 2 O VAL A 325 ? O VAL A 325 N LEU A 309 ? N LEU A 309 
AA4 2 3 O LEU A 310 ? O LEU A 310 N VAL A 293 ? N VAL A 293 
AA4 3 4 O ILE A 294 ? O ILE A 294 N TRP A 274 ? N TRP A 274 
AA4 4 5 N GLN A 277 ? N GLN A 277 O ALA A 344 ? O ALA A 344 
AA4 5 6 N SER A 343 ? N SER A 343 O PHE A 355 ? O PHE A 355 
AA4 6 7 N ILE A 352 ? N ILE A 352 O LEU A 376 ? O LEU A 376 
AA4 7 8 N ILE A 371 ? N ILE A 371 O PHE A 397 ? O PHE A 397 
AA5 1 2 N VAL A 528 ? N VAL A 528 O TYR A 535 ? O TYR A 535 
AA5 2 3 N TYR A 534 ? N TYR A 534 O ALA A 569 ? O ALA A 569 
AA5 3 4 N VAL A 568 ? N VAL A 568 O LYS A 577 ? O LYS A 577 
AA6 1 2 N VAL A 528 ? N VAL A 528 O TYR A 535 ? O TYR A 535 
AA6 2 3 N TYR A 534 ? N TYR A 534 O ALA A 569 ? O ALA A 569 
AA6 3 4 N MET A 564 ? N MET A 564 O VAL A 585 ? O VAL A 585 
AA7 1 2 N VAL A 604 ? N VAL A 604 O LEU A 614 ? O LEU A 614 
AA7 2 3 N MET A 619 ? N MET A 619 O THR A 633 ? O THR A 633 
AA8 1 2 N VAL A 604 ? N VAL A 604 O LEU A 614 ? O LEU A 614 
AA8 2 3 N VAL A 615 ? N VAL A 615 O PHE A 638 ? O PHE A 638 
AA8 3 4 N GLN A 641 ? N GLN A 641 O THR A 649 ? O THR A 649 
AA9 1 2 N THR B 218 ? N THR B 218 O SER B 514 ? O SER B 514 
AA9 2 3 O ILE B 513 ? O ILE B 513 N ILE B 491 ? N ILE B 491 
AA9 3 4 O LEU B 496 ? O LEU B 496 N ARG B 435 ? N ARG B 435 
AA9 4 5 O VAL B 438 ? O VAL B 438 N HIS B 426 ? N HIS B 426 
AB1 1 2 N THR B 218 ? N THR B 218 O SER B 514 ? O SER B 514 
AB1 2 3 O ILE B 513 ? O ILE B 513 N ILE B 491 ? N ILE B 491 
AB1 3 4 N LYS B 495 ? N LYS B 495 O ALA B 506 ? O ALA B 506 
AB2 1 2 N THR B 257 ? N THR B 257 O GLU B 266 ? O GLU B 266 
AB3 1 2 O VAL B 325 ? O VAL B 325 N LEU B 309 ? N LEU B 309 
AB3 2 3 O LEU B 310 ? O LEU B 310 N VAL B 293 ? N VAL B 293 
AB3 3 4 O ILE B 294 ? O ILE B 294 N TRP B 274 ? N TRP B 274 
AB3 4 5 N GLN B 277 ? N GLN B 277 O ALA B 344 ? O ALA B 344 
AB3 5 6 N SER B 343 ? N SER B 343 O PHE B 355 ? O PHE B 355 
AB3 6 7 N ILE B 352 ? N ILE B 352 O LEU B 376 ? O LEU B 376 
AB3 7 8 N ASN B 381 ? N ASN B 381 O ASN B 384 ? O ASN B 384 
AB4 1 2 N GLU B 523 ? N GLU B 523 O ALA B 539 ? O ALA B 539 
AB4 2 3 N TYR B 534 ? N TYR B 534 O ALA B 569 ? O ALA B 569 
AB4 3 4 N VAL B 568 ? N VAL B 568 O LYS B 577 ? O LYS B 577 
AB5 1 2 N GLU B 523 ? N GLU B 523 O ALA B 539 ? O ALA B 539 
AB5 2 3 N TYR B 534 ? N TYR B 534 O ALA B 569 ? O ALA B 569 
AB5 3 4 N MET B 564 ? N MET B 564 O LEU B 586 ? O LEU B 586 
AB6 1 2 N VAL B 604 ? N VAL B 604 O LEU B 614 ? O LEU B 614 
AB6 2 3 N MET B 619 ? N MET B 619 O THR B 633 ? O THR B 633 
AB7 1 2 N VAL B 604 ? N VAL B 604 O LEU B 614 ? O LEU B 614 
AB7 2 3 N VAL B 615 ? N VAL B 615 O PHE B 638 ? O PHE B 638 
AB7 3 4 N GLN B 641 ? N GLN B 641 O THR B 649 ? O THR B 649 
# 
_pdbx_entry_details.entry_id                   8XVQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TRP A 271 ? ? -123.79 -118.86 
2  1 ASP A 304 ? ? -153.67 76.25   
3  1 TYR A 402 ? ? -94.85  -62.93  
4  1 MET A 422 ? ? -160.81 78.74   
5  1 ASN A 447 ? ? -155.34 79.55   
6  1 ASN A 488 ? ? -165.81 45.77   
7  1 ASN A 497 ? ? -67.92  -174.49 
8  1 ASP A 499 ? ? -58.71  97.01   
9  1 MET A 517 ? ? 75.74   -13.76  
10 1 ASP A 581 ? ? 67.45   -63.95  
11 1 VAL A 585 ? ? -130.79 -51.72  
12 1 THR A 620 ? ? 74.68   122.81  
13 1 TYR A 695 ? ? -160.34 117.72  
14 1 LYS B 212 ? ? -38.90  117.03  
15 1 TRP B 271 ? ? -121.81 -116.77 
16 1 ASP B 304 ? ? -151.19 75.64   
17 1 TRP B 340 ? ? -114.70 -167.92 
18 1 TYR B 402 ? ? -98.05  -65.44  
19 1 MET B 422 ? ? -159.34 79.81   
20 1 ASN B 447 ? ? -165.86 73.24   
21 1 ASP B 463 ? ? -69.79  -162.74 
22 1 ASN B 488 ? ? -163.98 45.25   
23 1 MET B 517 ? ? 81.14   -16.21  
24 1 ASN B 561 ? ? -145.19 22.55   
25 1 ASP B 581 ? ? 73.78   -56.81  
26 1 ASP B 581 ? ? 77.18   -60.03  
27 1 VAL B 585 ? ? -130.58 -52.53  
28 1 THR B 620 ? ? 76.38   123.76  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A LEU 2   ? A LEU 2   
3   1 Y 1 A GLU 3   ? A GLU 3   
4   1 Y 1 A ARG 4   ? A ARG 4   
5   1 Y 1 A LYS 5   ? A LYS 5   
6   1 Y 1 A GLU 6   ? A GLU 6   
7   1 Y 1 A HIS 7   ? A HIS 7   
8   1 Y 1 A LYS 8   ? A LYS 8   
9   1 Y 1 A LYS 9   ? A LYS 9   
10  1 Y 1 A MET 10  ? A MET 10  
11  1 Y 1 A TYR 11  ? A TYR 11  
12  1 Y 1 A LYS 12  ? A LYS 12  
13  1 Y 1 A SER 13  ? A SER 13  
14  1 Y 1 A GLY 14  ? A GLY 14  
15  1 Y 1 A LYS 15  ? A LYS 15  
16  1 Y 1 A ASN 16  ? A ASN 16  
17  1 Y 1 A TRP 17  ? A TRP 17  
18  1 Y 1 A ALA 18  ? A ALA 18  
19  1 Y 1 A VAL 19  ? A VAL 19  
20  1 Y 1 A VAL 20  ? A VAL 20  
21  1 Y 1 A THR 21  ? A THR 21  
22  1 Y 1 A LEU 22  ? A LEU 22  
23  1 Y 1 A SER 23  ? A SER 23  
24  1 Y 1 A THR 24  ? A THR 24  
25  1 Y 1 A ALA 25  ? A ALA 25  
26  1 Y 1 A ALA 26  ? A ALA 26  
27  1 Y 1 A LEU 27  ? A LEU 27  
28  1 Y 1 A VAL 28  ? A VAL 28  
29  1 Y 1 A PHE 29  ? A PHE 29  
30  1 Y 1 A GLY 30  ? A GLY 30  
31  1 Y 1 A ALA 31  ? A ALA 31  
32  1 Y 1 A THR 32  ? A THR 32  
33  1 Y 1 A THR 33  ? A THR 33  
34  1 Y 1 A VAL 34  ? A VAL 34  
35  1 Y 1 A ASN 35  ? A ASN 35  
36  1 Y 1 A ALA 36  ? A ALA 36  
37  1 Y 1 A SER 37  ? A SER 37  
38  1 Y 1 A ALA 38  ? A ALA 38  
39  1 Y 1 A ASP 39  ? A ASP 39  
40  1 Y 1 A THR 40  ? A THR 40  
41  1 Y 1 A ASN 41  ? A ASN 41  
42  1 Y 1 A ILE 42  ? A ILE 42  
43  1 Y 1 A GLU 43  ? A GLU 43  
44  1 Y 1 A ASN 44  ? A ASN 44  
45  1 Y 1 A ASN 45  ? A ASN 45  
46  1 Y 1 A ASP 46  ? A ASP 46  
47  1 Y 1 A SER 47  ? A SER 47  
48  1 Y 1 A SER 48  ? A SER 48  
49  1 Y 1 A THR 49  ? A THR 49  
50  1 Y 1 A VAL 50  ? A VAL 50  
51  1 Y 1 A GLN 51  ? A GLN 51  
52  1 Y 1 A VAL 52  ? A VAL 52  
53  1 Y 1 A THR 53  ? A THR 53  
54  1 Y 1 A THR 54  ? A THR 54  
55  1 Y 1 A GLY 55  ? A GLY 55  
56  1 Y 1 A ASP 56  ? A ASP 56  
57  1 Y 1 A ASN 57  ? A ASN 57  
58  1 Y 1 A ASP 58  ? A ASP 58  
59  1 Y 1 A ILE 59  ? A ILE 59  
60  1 Y 1 A ALA 60  ? A ALA 60  
61  1 Y 1 A VAL 61  ? A VAL 61  
62  1 Y 1 A LYS 62  ? A LYS 62  
63  1 Y 1 A SER 63  ? A SER 63  
64  1 Y 1 A VAL 64  ? A VAL 64  
65  1 Y 1 A THR 65  ? A THR 65  
66  1 Y 1 A LEU 66  ? A LEU 66  
67  1 Y 1 A GLY 67  ? A GLY 67  
68  1 Y 1 A SER 68  ? A SER 68  
69  1 Y 1 A GLY 69  ? A GLY 69  
70  1 Y 1 A GLN 70  ? A GLN 70  
71  1 Y 1 A VAL 71  ? A VAL 71  
72  1 Y 1 A SER 72  ? A SER 72  
73  1 Y 1 A ALA 73  ? A ALA 73  
74  1 Y 1 A ALA 74  ? A ALA 74  
75  1 Y 1 A SER 75  ? A SER 75  
76  1 Y 1 A ASP 76  ? A ASP 76  
77  1 Y 1 A THR 77  ? A THR 77  
78  1 Y 1 A THR 78  ? A THR 78  
79  1 Y 1 A ILE 79  ? A ILE 79  
80  1 Y 1 A ARG 80  ? A ARG 80  
81  1 Y 1 A THR 81  ? A THR 81  
82  1 Y 1 A SER 82  ? A SER 82  
83  1 Y 1 A ALA 83  ? A ALA 83  
84  1 Y 1 A ASN 84  ? A ASN 84  
85  1 Y 1 A ALA 85  ? A ALA 85  
86  1 Y 1 A ASN 86  ? A ASN 86  
87  1 Y 1 A SER 87  ? A SER 87  
88  1 Y 1 A ALA 88  ? A ALA 88  
89  1 Y 1 A SER 89  ? A SER 89  
90  1 Y 1 A SER 90  ? A SER 90  
91  1 Y 1 A ALA 91  ? A ALA 91  
92  1 Y 1 A ALA 92  ? A ALA 92  
93  1 Y 1 A ASN 93  ? A ASN 93  
94  1 Y 1 A THR 94  ? A THR 94  
95  1 Y 1 A GLN 95  ? A GLN 95  
96  1 Y 1 A ASN 96  ? A ASN 96  
97  1 Y 1 A SER 97  ? A SER 97  
98  1 Y 1 A ASN 98  ? A ASN 98  
99  1 Y 1 A SER 99  ? A SER 99  
100 1 Y 1 A GLN 100 ? A GLN 100 
101 1 Y 1 A VAL 101 ? A VAL 101 
102 1 Y 1 A ALA 102 ? A ALA 102 
103 1 Y 1 A SER 103 ? A SER 103 
104 1 Y 1 A SER 104 ? A SER 104 
105 1 Y 1 A ALA 105 ? A ALA 105 
106 1 Y 1 A ALA 106 ? A ALA 106 
107 1 Y 1 A ILE 107 ? A ILE 107 
108 1 Y 1 A THR 108 ? A THR 108 
109 1 Y 1 A SER 109 ? A SER 109 
110 1 Y 1 A SER 110 ? A SER 110 
111 1 Y 1 A THR 111 ? A THR 111 
112 1 Y 1 A SER 112 ? A SER 112 
113 1 Y 1 A SER 113 ? A SER 113 
114 1 Y 1 A ALA 114 ? A ALA 114 
115 1 Y 1 A ALA 115 ? A ALA 115 
116 1 Y 1 A SER 116 ? A SER 116 
117 1 Y 1 A SER 117 ? A SER 117 
118 1 Y 1 A ASN 118 ? A ASN 118 
119 1 Y 1 A ASN 119 ? A ASN 119 
120 1 Y 1 A THR 120 ? A THR 120 
121 1 Y 1 A ASP 121 ? A ASP 121 
122 1 Y 1 A SER 122 ? A SER 122 
123 1 Y 1 A LYS 123 ? A LYS 123 
124 1 Y 1 A ALA 124 ? A ALA 124 
125 1 Y 1 A ALA 125 ? A ALA 125 
126 1 Y 1 A GLN 126 ? A GLN 126 
127 1 Y 1 A GLU 127 ? A GLU 127 
128 1 Y 1 A ASN 128 ? A ASN 128 
129 1 Y 1 A THR 129 ? A THR 129 
130 1 Y 1 A ASN 130 ? A ASN 130 
131 1 Y 1 A THR 131 ? A THR 131 
132 1 Y 1 A ALA 132 ? A ALA 132 
133 1 Y 1 A LYS 133 ? A LYS 133 
134 1 Y 1 A ASN 134 ? A ASN 134 
135 1 Y 1 A ASP 135 ? A ASP 135 
136 1 Y 1 A ASP 136 ? A ASP 136 
137 1 Y 1 A THR 137 ? A THR 137 
138 1 Y 1 A GLN 138 ? A GLN 138 
139 1 Y 1 A LYS 139 ? A LYS 139 
140 1 Y 1 A ALA 140 ? A ALA 140 
141 1 Y 1 A ALA 141 ? A ALA 141 
142 1 Y 1 A PRO 142 ? A PRO 142 
143 1 Y 1 A ALA 143 ? A ALA 143 
144 1 Y 1 A ASN 144 ? A ASN 144 
145 1 Y 1 A GLU 145 ? A GLU 145 
146 1 Y 1 A SER 146 ? A SER 146 
147 1 Y 1 A SER 147 ? A SER 147 
148 1 Y 1 A GLU 148 ? A GLU 148 
149 1 Y 1 A ALA 149 ? A ALA 149 
150 1 Y 1 A LYS 150 ? A LYS 150 
151 1 Y 1 A ASN 151 ? A ASN 151 
152 1 Y 1 A GLU 152 ? A GLU 152 
153 1 Y 1 A PRO 153 ? A PRO 153 
154 1 Y 1 A ALA 154 ? A ALA 154 
155 1 Y 1 A VAL 155 ? A VAL 155 
156 1 Y 1 A ASN 156 ? A ASN 156 
157 1 Y 1 A VAL 157 ? A VAL 157 
158 1 Y 1 A ASN 158 ? A ASN 158 
159 1 Y 1 A ASP 159 ? A ASP 159 
160 1 Y 1 A SER 160 ? A SER 160 
161 1 Y 1 A SER 161 ? A SER 161 
162 1 Y 1 A ALA 162 ? A ALA 162 
163 1 Y 1 A ALA 163 ? A ALA 163 
164 1 Y 1 A LYS 164 ? A LYS 164 
165 1 Y 1 A ASN 165 ? A ASN 165 
166 1 Y 1 A ASP 166 ? A ASP 166 
167 1 Y 1 A ASP 167 ? A ASP 167 
168 1 Y 1 A GLN 168 ? A GLN 168 
169 1 Y 1 A GLN 169 ? A GLN 169 
170 1 Y 1 A SER 170 ? A SER 170 
171 1 Y 1 A SER 171 ? A SER 171 
172 1 Y 1 A LYS 172 ? A LYS 172 
173 1 Y 1 A LYS 173 ? A LYS 173 
174 1 Y 1 A ASN 174 ? A ASN 174 
175 1 Y 1 A THR 175 ? A THR 175 
176 1 Y 1 A THR 176 ? A THR 176 
177 1 Y 1 A LEU 697 ? A LEU 697 
178 1 Y 1 A LYS 698 ? A LYS 698 
179 1 Y 1 A PRO 699 ? A PRO 699 
180 1 Y 1 A HIS 700 ? A HIS 700 
181 1 Y 1 A ASP 701 ? A ASP 701 
182 1 Y 1 A PRO 702 ? A PRO 702 
183 1 Y 1 A ALA 703 ? A ALA 703 
184 1 Y 1 A THR 704 ? A THR 704 
185 1 Y 1 A PRO 705 ? A PRO 705 
186 1 Y 1 A ASN 706 ? A ASN 706 
187 1 Y 1 A ASP 707 ? A ASP 707 
188 1 Y 1 A PRO 708 ? A PRO 708 
189 1 Y 1 A GLU 709 ? A GLU 709 
190 1 Y 1 A THR 710 ? A THR 710 
191 1 Y 1 A PRO 711 ? A PRO 711 
192 1 Y 1 A THR 712 ? A THR 712 
193 1 Y 1 A THR 713 ? A THR 713 
194 1 Y 1 A PRO 714 ? A PRO 714 
195 1 Y 1 A GLU 715 ? A GLU 715 
196 1 Y 1 A THR 716 ? A THR 716 
197 1 Y 1 A PRO 717 ? A PRO 717 
198 1 Y 1 A GLU 718 ? A GLU 718 
199 1 Y 1 A THR 719 ? A THR 719 
200 1 Y 1 A PRO 720 ? A PRO 720 
201 1 Y 1 A ASN 721 ? A ASN 721 
202 1 Y 1 A THR 722 ? A THR 722 
203 1 Y 1 A PRO 723 ? A PRO 723 
204 1 Y 1 A LYS 724 ? A LYS 724 
205 1 Y 1 A THR 725 ? A THR 725 
206 1 Y 1 A PRO 726 ? A PRO 726 
207 1 Y 1 A LYS 727 ? A LYS 727 
208 1 Y 1 A THR 728 ? A THR 728 
209 1 Y 1 A PRO 729 ? A PRO 729 
210 1 Y 1 A GLU 730 ? A GLU 730 
211 1 Y 1 A ASN 731 ? A ASN 731 
212 1 Y 1 A PRO 732 ? A PRO 732 
213 1 Y 1 A GLY 733 ? A GLY 733 
214 1 Y 1 A THR 734 ? A THR 734 
215 1 Y 1 A PRO 735 ? A PRO 735 
216 1 Y 1 A GLN 736 ? A GLN 736 
217 1 Y 1 A THR 737 ? A THR 737 
218 1 Y 1 A PRO 738 ? A PRO 738 
219 1 Y 1 A ASN 739 ? A ASN 739 
220 1 Y 1 A THR 740 ? A THR 740 
221 1 Y 1 A PRO 741 ? A PRO 741 
222 1 Y 1 A ASN 742 ? A ASN 742 
223 1 Y 1 A THR 743 ? A THR 743 
224 1 Y 1 A PRO 744 ? A PRO 744 
225 1 Y 1 A GLU 745 ? A GLU 745 
226 1 Y 1 A ILE 746 ? A ILE 746 
227 1 Y 1 A PRO 747 ? A PRO 747 
228 1 Y 1 A LEU 748 ? A LEU 748 
229 1 Y 1 A THR 749 ? A THR 749 
230 1 Y 1 A PRO 750 ? A PRO 750 
231 1 Y 1 A GLU 751 ? A GLU 751 
232 1 Y 1 A THR 752 ? A THR 752 
233 1 Y 1 A PRO 753 ? A PRO 753 
234 1 Y 1 A LYS 754 ? A LYS 754 
235 1 Y 1 A GLN 755 ? A GLN 755 
236 1 Y 1 A PRO 756 ? A PRO 756 
237 1 Y 1 A GLU 757 ? A GLU 757 
238 1 Y 1 A THR 758 ? A THR 758 
239 1 Y 1 A GLN 759 ? A GLN 759 
240 1 Y 1 A THR 760 ? A THR 760 
241 1 Y 1 A ASN 761 ? A ASN 761 
242 1 Y 1 A ASN 762 ? A ASN 762 
243 1 Y 1 A ARG 763 ? A ARG 763 
244 1 Y 1 A LEU 764 ? A LEU 764 
245 1 Y 1 A PRO 765 ? A PRO 765 
246 1 Y 1 A GLN 766 ? A GLN 766 
247 1 Y 1 A THR 767 ? A THR 767 
248 1 Y 1 A GLY 768 ? A GLY 768 
249 1 Y 1 A ASN 769 ? A ASN 769 
250 1 Y 1 A ASN 770 ? A ASN 770 
251 1 Y 1 A ALA 771 ? A ALA 771 
252 1 Y 1 A ASN 772 ? A ASN 772 
253 1 Y 1 A LYS 773 ? A LYS 773 
254 1 Y 1 A ALA 774 ? A ALA 774 
255 1 Y 1 A MET 775 ? A MET 775 
256 1 Y 1 A ILE 776 ? A ILE 776 
257 1 Y 1 A GLY 777 ? A GLY 777 
258 1 Y 1 A LEU 778 ? A LEU 778 
259 1 Y 1 A GLY 779 ? A GLY 779 
260 1 Y 1 A MET 780 ? A MET 780 
261 1 Y 1 A GLY 781 ? A GLY 781 
262 1 Y 1 A THR 782 ? A THR 782 
263 1 Y 1 A LEU 783 ? A LEU 783 
264 1 Y 1 A LEU 784 ? A LEU 784 
265 1 Y 1 A SER 785 ? A SER 785 
266 1 Y 1 A MET 786 ? A MET 786 
267 1 Y 1 A PHE 787 ? A PHE 787 
268 1 Y 1 A GLY 788 ? A GLY 788 
269 1 Y 1 A LEU 789 ? A LEU 789 
270 1 Y 1 A ALA 790 ? A ALA 790 
271 1 Y 1 A GLU 791 ? A GLU 791 
272 1 Y 1 A ILE 792 ? A ILE 792 
273 1 Y 1 A ASN 793 ? A ASN 793 
274 1 Y 1 A LYS 794 ? A LYS 794 
275 1 Y 1 A ARG 795 ? A ARG 795 
276 1 Y 1 A ARG 796 ? A ARG 796 
277 1 Y 1 A PHE 797 ? A PHE 797 
278 1 Y 1 A ASN 798 ? A ASN 798 
279 1 Y 1 B MET 1   ? B MET 1   
280 1 Y 1 B LEU 2   ? B LEU 2   
281 1 Y 1 B GLU 3   ? B GLU 3   
282 1 Y 1 B ARG 4   ? B ARG 4   
283 1 Y 1 B LYS 5   ? B LYS 5   
284 1 Y 1 B GLU 6   ? B GLU 6   
285 1 Y 1 B HIS 7   ? B HIS 7   
286 1 Y 1 B LYS 8   ? B LYS 8   
287 1 Y 1 B LYS 9   ? B LYS 9   
288 1 Y 1 B MET 10  ? B MET 10  
289 1 Y 1 B TYR 11  ? B TYR 11  
290 1 Y 1 B LYS 12  ? B LYS 12  
291 1 Y 1 B SER 13  ? B SER 13  
292 1 Y 1 B GLY 14  ? B GLY 14  
293 1 Y 1 B LYS 15  ? B LYS 15  
294 1 Y 1 B ASN 16  ? B ASN 16  
295 1 Y 1 B TRP 17  ? B TRP 17  
296 1 Y 1 B ALA 18  ? B ALA 18  
297 1 Y 1 B VAL 19  ? B VAL 19  
298 1 Y 1 B VAL 20  ? B VAL 20  
299 1 Y 1 B THR 21  ? B THR 21  
300 1 Y 1 B LEU 22  ? B LEU 22  
301 1 Y 1 B SER 23  ? B SER 23  
302 1 Y 1 B THR 24  ? B THR 24  
303 1 Y 1 B ALA 25  ? B ALA 25  
304 1 Y 1 B ALA 26  ? B ALA 26  
305 1 Y 1 B LEU 27  ? B LEU 27  
306 1 Y 1 B VAL 28  ? B VAL 28  
307 1 Y 1 B PHE 29  ? B PHE 29  
308 1 Y 1 B GLY 30  ? B GLY 30  
309 1 Y 1 B ALA 31  ? B ALA 31  
310 1 Y 1 B THR 32  ? B THR 32  
311 1 Y 1 B THR 33  ? B THR 33  
312 1 Y 1 B VAL 34  ? B VAL 34  
313 1 Y 1 B ASN 35  ? B ASN 35  
314 1 Y 1 B ALA 36  ? B ALA 36  
315 1 Y 1 B SER 37  ? B SER 37  
316 1 Y 1 B ALA 38  ? B ALA 38  
317 1 Y 1 B ASP 39  ? B ASP 39  
318 1 Y 1 B THR 40  ? B THR 40  
319 1 Y 1 B ASN 41  ? B ASN 41  
320 1 Y 1 B ILE 42  ? B ILE 42  
321 1 Y 1 B GLU 43  ? B GLU 43  
322 1 Y 1 B ASN 44  ? B ASN 44  
323 1 Y 1 B ASN 45  ? B ASN 45  
324 1 Y 1 B ASP 46  ? B ASP 46  
325 1 Y 1 B SER 47  ? B SER 47  
326 1 Y 1 B SER 48  ? B SER 48  
327 1 Y 1 B THR 49  ? B THR 49  
328 1 Y 1 B VAL 50  ? B VAL 50  
329 1 Y 1 B GLN 51  ? B GLN 51  
330 1 Y 1 B VAL 52  ? B VAL 52  
331 1 Y 1 B THR 53  ? B THR 53  
332 1 Y 1 B THR 54  ? B THR 54  
333 1 Y 1 B GLY 55  ? B GLY 55  
334 1 Y 1 B ASP 56  ? B ASP 56  
335 1 Y 1 B ASN 57  ? B ASN 57  
336 1 Y 1 B ASP 58  ? B ASP 58  
337 1 Y 1 B ILE 59  ? B ILE 59  
338 1 Y 1 B ALA 60  ? B ALA 60  
339 1 Y 1 B VAL 61  ? B VAL 61  
340 1 Y 1 B LYS 62  ? B LYS 62  
341 1 Y 1 B SER 63  ? B SER 63  
342 1 Y 1 B VAL 64  ? B VAL 64  
343 1 Y 1 B THR 65  ? B THR 65  
344 1 Y 1 B LEU 66  ? B LEU 66  
345 1 Y 1 B GLY 67  ? B GLY 67  
346 1 Y 1 B SER 68  ? B SER 68  
347 1 Y 1 B GLY 69  ? B GLY 69  
348 1 Y 1 B GLN 70  ? B GLN 70  
349 1 Y 1 B VAL 71  ? B VAL 71  
350 1 Y 1 B SER 72  ? B SER 72  
351 1 Y 1 B ALA 73  ? B ALA 73  
352 1 Y 1 B ALA 74  ? B ALA 74  
353 1 Y 1 B SER 75  ? B SER 75  
354 1 Y 1 B ASP 76  ? B ASP 76  
355 1 Y 1 B THR 77  ? B THR 77  
356 1 Y 1 B THR 78  ? B THR 78  
357 1 Y 1 B ILE 79  ? B ILE 79  
358 1 Y 1 B ARG 80  ? B ARG 80  
359 1 Y 1 B THR 81  ? B THR 81  
360 1 Y 1 B SER 82  ? B SER 82  
361 1 Y 1 B ALA 83  ? B ALA 83  
362 1 Y 1 B ASN 84  ? B ASN 84  
363 1 Y 1 B ALA 85  ? B ALA 85  
364 1 Y 1 B ASN 86  ? B ASN 86  
365 1 Y 1 B SER 87  ? B SER 87  
366 1 Y 1 B ALA 88  ? B ALA 88  
367 1 Y 1 B SER 89  ? B SER 89  
368 1 Y 1 B SER 90  ? B SER 90  
369 1 Y 1 B ALA 91  ? B ALA 91  
370 1 Y 1 B ALA 92  ? B ALA 92  
371 1 Y 1 B ASN 93  ? B ASN 93  
372 1 Y 1 B THR 94  ? B THR 94  
373 1 Y 1 B GLN 95  ? B GLN 95  
374 1 Y 1 B ASN 96  ? B ASN 96  
375 1 Y 1 B SER 97  ? B SER 97  
376 1 Y 1 B ASN 98  ? B ASN 98  
377 1 Y 1 B SER 99  ? B SER 99  
378 1 Y 1 B GLN 100 ? B GLN 100 
379 1 Y 1 B VAL 101 ? B VAL 101 
380 1 Y 1 B ALA 102 ? B ALA 102 
381 1 Y 1 B SER 103 ? B SER 103 
382 1 Y 1 B SER 104 ? B SER 104 
383 1 Y 1 B ALA 105 ? B ALA 105 
384 1 Y 1 B ALA 106 ? B ALA 106 
385 1 Y 1 B ILE 107 ? B ILE 107 
386 1 Y 1 B THR 108 ? B THR 108 
387 1 Y 1 B SER 109 ? B SER 109 
388 1 Y 1 B SER 110 ? B SER 110 
389 1 Y 1 B THR 111 ? B THR 111 
390 1 Y 1 B SER 112 ? B SER 112 
391 1 Y 1 B SER 113 ? B SER 113 
392 1 Y 1 B ALA 114 ? B ALA 114 
393 1 Y 1 B ALA 115 ? B ALA 115 
394 1 Y 1 B SER 116 ? B SER 116 
395 1 Y 1 B SER 117 ? B SER 117 
396 1 Y 1 B ASN 118 ? B ASN 118 
397 1 Y 1 B ASN 119 ? B ASN 119 
398 1 Y 1 B THR 120 ? B THR 120 
399 1 Y 1 B ASP 121 ? B ASP 121 
400 1 Y 1 B SER 122 ? B SER 122 
401 1 Y 1 B LYS 123 ? B LYS 123 
402 1 Y 1 B ALA 124 ? B ALA 124 
403 1 Y 1 B ALA 125 ? B ALA 125 
404 1 Y 1 B GLN 126 ? B GLN 126 
405 1 Y 1 B GLU 127 ? B GLU 127 
406 1 Y 1 B ASN 128 ? B ASN 128 
407 1 Y 1 B THR 129 ? B THR 129 
408 1 Y 1 B ASN 130 ? B ASN 130 
409 1 Y 1 B THR 131 ? B THR 131 
410 1 Y 1 B ALA 132 ? B ALA 132 
411 1 Y 1 B LYS 133 ? B LYS 133 
412 1 Y 1 B ASN 134 ? B ASN 134 
413 1 Y 1 B ASP 135 ? B ASP 135 
414 1 Y 1 B ASP 136 ? B ASP 136 
415 1 Y 1 B THR 137 ? B THR 137 
416 1 Y 1 B GLN 138 ? B GLN 138 
417 1 Y 1 B LYS 139 ? B LYS 139 
418 1 Y 1 B ALA 140 ? B ALA 140 
419 1 Y 1 B ALA 141 ? B ALA 141 
420 1 Y 1 B PRO 142 ? B PRO 142 
421 1 Y 1 B ALA 143 ? B ALA 143 
422 1 Y 1 B ASN 144 ? B ASN 144 
423 1 Y 1 B GLU 145 ? B GLU 145 
424 1 Y 1 B SER 146 ? B SER 146 
425 1 Y 1 B SER 147 ? B SER 147 
426 1 Y 1 B GLU 148 ? B GLU 148 
427 1 Y 1 B ALA 149 ? B ALA 149 
428 1 Y 1 B LYS 150 ? B LYS 150 
429 1 Y 1 B ASN 151 ? B ASN 151 
430 1 Y 1 B GLU 152 ? B GLU 152 
431 1 Y 1 B PRO 153 ? B PRO 153 
432 1 Y 1 B ALA 154 ? B ALA 154 
433 1 Y 1 B VAL 155 ? B VAL 155 
434 1 Y 1 B ASN 156 ? B ASN 156 
435 1 Y 1 B VAL 157 ? B VAL 157 
436 1 Y 1 B ASN 158 ? B ASN 158 
437 1 Y 1 B ASP 159 ? B ASP 159 
438 1 Y 1 B SER 160 ? B SER 160 
439 1 Y 1 B SER 161 ? B SER 161 
440 1 Y 1 B ALA 162 ? B ALA 162 
441 1 Y 1 B ALA 163 ? B ALA 163 
442 1 Y 1 B LYS 164 ? B LYS 164 
443 1 Y 1 B ASN 165 ? B ASN 165 
444 1 Y 1 B ASP 166 ? B ASP 166 
445 1 Y 1 B ASP 167 ? B ASP 167 
446 1 Y 1 B GLN 168 ? B GLN 168 
447 1 Y 1 B GLN 169 ? B GLN 169 
448 1 Y 1 B SER 170 ? B SER 170 
449 1 Y 1 B SER 171 ? B SER 171 
450 1 Y 1 B LYS 172 ? B LYS 172 
451 1 Y 1 B LYS 173 ? B LYS 173 
452 1 Y 1 B ASN 174 ? B ASN 174 
453 1 Y 1 B THR 175 ? B THR 175 
454 1 Y 1 B THR 176 ? B THR 176 
455 1 Y 1 B ALA 177 ? B ALA 177 
456 1 Y 1 B SER 216 ? B SER 216 
457 1 Y 1 B TYR 695 ? B TYR 695 
458 1 Y 1 B GLY 696 ? B GLY 696 
459 1 Y 1 B LEU 697 ? B LEU 697 
460 1 Y 1 B LYS 698 ? B LYS 698 
461 1 Y 1 B PRO 699 ? B PRO 699 
462 1 Y 1 B HIS 700 ? B HIS 700 
463 1 Y 1 B ASP 701 ? B ASP 701 
464 1 Y 1 B PRO 702 ? B PRO 702 
465 1 Y 1 B ALA 703 ? B ALA 703 
466 1 Y 1 B THR 704 ? B THR 704 
467 1 Y 1 B PRO 705 ? B PRO 705 
468 1 Y 1 B ASN 706 ? B ASN 706 
469 1 Y 1 B ASP 707 ? B ASP 707 
470 1 Y 1 B PRO 708 ? B PRO 708 
471 1 Y 1 B GLU 709 ? B GLU 709 
472 1 Y 1 B THR 710 ? B THR 710 
473 1 Y 1 B PRO 711 ? B PRO 711 
474 1 Y 1 B THR 712 ? B THR 712 
475 1 Y 1 B THR 713 ? B THR 713 
476 1 Y 1 B PRO 714 ? B PRO 714 
477 1 Y 1 B GLU 715 ? B GLU 715 
478 1 Y 1 B THR 716 ? B THR 716 
479 1 Y 1 B PRO 717 ? B PRO 717 
480 1 Y 1 B GLU 718 ? B GLU 718 
481 1 Y 1 B THR 719 ? B THR 719 
482 1 Y 1 B PRO 720 ? B PRO 720 
483 1 Y 1 B ASN 721 ? B ASN 721 
484 1 Y 1 B THR 722 ? B THR 722 
485 1 Y 1 B PRO 723 ? B PRO 723 
486 1 Y 1 B LYS 724 ? B LYS 724 
487 1 Y 1 B THR 725 ? B THR 725 
488 1 Y 1 B PRO 726 ? B PRO 726 
489 1 Y 1 B LYS 727 ? B LYS 727 
490 1 Y 1 B THR 728 ? B THR 728 
491 1 Y 1 B PRO 729 ? B PRO 729 
492 1 Y 1 B GLU 730 ? B GLU 730 
493 1 Y 1 B ASN 731 ? B ASN 731 
494 1 Y 1 B PRO 732 ? B PRO 732 
495 1 Y 1 B GLY 733 ? B GLY 733 
496 1 Y 1 B THR 734 ? B THR 734 
497 1 Y 1 B PRO 735 ? B PRO 735 
498 1 Y 1 B GLN 736 ? B GLN 736 
499 1 Y 1 B THR 737 ? B THR 737 
500 1 Y 1 B PRO 738 ? B PRO 738 
501 1 Y 1 B ASN 739 ? B ASN 739 
502 1 Y 1 B THR 740 ? B THR 740 
503 1 Y 1 B PRO 741 ? B PRO 741 
504 1 Y 1 B ASN 742 ? B ASN 742 
505 1 Y 1 B THR 743 ? B THR 743 
506 1 Y 1 B PRO 744 ? B PRO 744 
507 1 Y 1 B GLU 745 ? B GLU 745 
508 1 Y 1 B ILE 746 ? B ILE 746 
509 1 Y 1 B PRO 747 ? B PRO 747 
510 1 Y 1 B LEU 748 ? B LEU 748 
511 1 Y 1 B THR 749 ? B THR 749 
512 1 Y 1 B PRO 750 ? B PRO 750 
513 1 Y 1 B GLU 751 ? B GLU 751 
514 1 Y 1 B THR 752 ? B THR 752 
515 1 Y 1 B PRO 753 ? B PRO 753 
516 1 Y 1 B LYS 754 ? B LYS 754 
517 1 Y 1 B GLN 755 ? B GLN 755 
518 1 Y 1 B PRO 756 ? B PRO 756 
519 1 Y 1 B GLU 757 ? B GLU 757 
520 1 Y 1 B THR 758 ? B THR 758 
521 1 Y 1 B GLN 759 ? B GLN 759 
522 1 Y 1 B THR 760 ? B THR 760 
523 1 Y 1 B ASN 761 ? B ASN 761 
524 1 Y 1 B ASN 762 ? B ASN 762 
525 1 Y 1 B ARG 763 ? B ARG 763 
526 1 Y 1 B LEU 764 ? B LEU 764 
527 1 Y 1 B PRO 765 ? B PRO 765 
528 1 Y 1 B GLN 766 ? B GLN 766 
529 1 Y 1 B THR 767 ? B THR 767 
530 1 Y 1 B GLY 768 ? B GLY 768 
531 1 Y 1 B ASN 769 ? B ASN 769 
532 1 Y 1 B ASN 770 ? B ASN 770 
533 1 Y 1 B ALA 771 ? B ALA 771 
534 1 Y 1 B ASN 772 ? B ASN 772 
535 1 Y 1 B LYS 773 ? B LYS 773 
536 1 Y 1 B ALA 774 ? B ALA 774 
537 1 Y 1 B MET 775 ? B MET 775 
538 1 Y 1 B ILE 776 ? B ILE 776 
539 1 Y 1 B GLY 777 ? B GLY 777 
540 1 Y 1 B LEU 778 ? B LEU 778 
541 1 Y 1 B GLY 779 ? B GLY 779 
542 1 Y 1 B MET 780 ? B MET 780 
543 1 Y 1 B GLY 781 ? B GLY 781 
544 1 Y 1 B THR 782 ? B THR 782 
545 1 Y 1 B LEU 783 ? B LEU 783 
546 1 Y 1 B LEU 784 ? B LEU 784 
547 1 Y 1 B SER 785 ? B SER 785 
548 1 Y 1 B MET 786 ? B MET 786 
549 1 Y 1 B PHE 787 ? B PHE 787 
550 1 Y 1 B GLY 788 ? B GLY 788 
551 1 Y 1 B LEU 789 ? B LEU 789 
552 1 Y 1 B ALA 790 ? B ALA 790 
553 1 Y 1 B GLU 791 ? B GLU 791 
554 1 Y 1 B ILE 792 ? B ILE 792 
555 1 Y 1 B ASN 793 ? B ASN 793 
556 1 Y 1 B LYS 794 ? B LYS 794 
557 1 Y 1 B ARG 795 ? B ARG 795 
558 1 Y 1 B ARG 796 ? B ARG 796 
559 1 Y 1 B PHE 797 ? B PHE 797 
560 1 Y 1 B ASN 798 ? B ASN 798 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
FRU C1   C  N N 75  
FRU C2   C  N R 76  
FRU C3   C  N S 77  
FRU C4   C  N S 78  
FRU C5   C  N R 79  
FRU C6   C  N N 80  
FRU O1   O  N N 81  
FRU O2   O  N N 82  
FRU O3   O  N N 83  
FRU O4   O  N N 84  
FRU O5   O  N N 85  
FRU O6   O  N N 86  
FRU H11  H  N N 87  
FRU H12  H  N N 88  
FRU H3   H  N N 89  
FRU H4   H  N N 90  
FRU H5   H  N N 91  
FRU H61  H  N N 92  
FRU H62  H  N N 93  
FRU HO1  H  N N 94  
FRU HO2  H  N N 95  
FRU HO3  H  N N 96  
FRU HO4  H  N N 97  
FRU HO6  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
FRU C1  C2   sing N N 70  
FRU C1  O1   sing N N 71  
FRU C1  H11  sing N N 72  
FRU C1  H12  sing N N 73  
FRU C2  C3   sing N N 74  
FRU C2  O2   sing N N 75  
FRU C2  O5   sing N N 76  
FRU C3  C4   sing N N 77  
FRU C3  O3   sing N N 78  
FRU C3  H3   sing N N 79  
FRU C4  C5   sing N N 80  
FRU C4  O4   sing N N 81  
FRU C4  H4   sing N N 82  
FRU C5  C6   sing N N 83  
FRU C5  O5   sing N N 84  
FRU C5  H5   sing N N 85  
FRU C6  O6   sing N N 86  
FRU C6  H61  sing N N 87  
FRU C6  H62  sing N N 88  
FRU O1  HO1  sing N N 89  
FRU O2  HO2  sing N N 90  
FRU O3  HO3  sing N N 91  
FRU O4  HO4  sing N N 92  
FRU O6  HO6  sing N N 93  
GLN N   CA   sing N N 94  
GLN N   H    sing N N 95  
GLN N   H2   sing N N 96  
GLN CA  C    sing N N 97  
GLN CA  CB   sing N N 98  
GLN CA  HA   sing N N 99  
GLN C   O    doub N N 100 
GLN C   OXT  sing N N 101 
GLN CB  CG   sing N N 102 
GLN CB  HB2  sing N N 103 
GLN CB  HB3  sing N N 104 
GLN CG  CD   sing N N 105 
GLN CG  HG2  sing N N 106 
GLN CG  HG3  sing N N 107 
GLN CD  OE1  doub N N 108 
GLN CD  NE2  sing N N 109 
GLN NE2 HE21 sing N N 110 
GLN NE2 HE22 sing N N 111 
GLN OXT HXT  sing N N 112 
GLU N   CA   sing N N 113 
GLU N   H    sing N N 114 
GLU N   H2   sing N N 115 
GLU CA  C    sing N N 116 
GLU CA  CB   sing N N 117 
GLU CA  HA   sing N N 118 
GLU C   O    doub N N 119 
GLU C   OXT  sing N N 120 
GLU CB  CG   sing N N 121 
GLU CB  HB2  sing N N 122 
GLU CB  HB3  sing N N 123 
GLU CG  CD   sing N N 124 
GLU CG  HG2  sing N N 125 
GLU CG  HG3  sing N N 126 
GLU CD  OE1  doub N N 127 
GLU CD  OE2  sing N N 128 
GLU OE2 HE2  sing N N 129 
GLU OXT HXT  sing N N 130 
GLY N   CA   sing N N 131 
GLY N   H    sing N N 132 
GLY N   H2   sing N N 133 
GLY CA  C    sing N N 134 
GLY CA  HA2  sing N N 135 
GLY CA  HA3  sing N N 136 
GLY C   O    doub N N 137 
GLY C   OXT  sing N N 138 
GLY OXT HXT  sing N N 139 
HIS N   CA   sing N N 140 
HIS N   H    sing N N 141 
HIS N   H2   sing N N 142 
HIS CA  C    sing N N 143 
HIS CA  CB   sing N N 144 
HIS CA  HA   sing N N 145 
HIS C   O    doub N N 146 
HIS C   OXT  sing N N 147 
HIS CB  CG   sing N N 148 
HIS CB  HB2  sing N N 149 
HIS CB  HB3  sing N N 150 
HIS CG  ND1  sing Y N 151 
HIS CG  CD2  doub Y N 152 
HIS ND1 CE1  doub Y N 153 
HIS ND1 HD1  sing N N 154 
HIS CD2 NE2  sing Y N 155 
HIS CD2 HD2  sing N N 156 
HIS CE1 NE2  sing Y N 157 
HIS CE1 HE1  sing N N 158 
HIS NE2 HE2  sing N N 159 
HIS OXT HXT  sing N N 160 
HOH O   H1   sing N N 161 
HOH O   H2   sing N N 162 
ILE N   CA   sing N N 163 
ILE N   H    sing N N 164 
ILE N   H2   sing N N 165 
ILE CA  C    sing N N 166 
ILE CA  CB   sing N N 167 
ILE CA  HA   sing N N 168 
ILE C   O    doub N N 169 
ILE C   OXT  sing N N 170 
ILE CB  CG1  sing N N 171 
ILE CB  CG2  sing N N 172 
ILE CB  HB   sing N N 173 
ILE CG1 CD1  sing N N 174 
ILE CG1 HG12 sing N N 175 
ILE CG1 HG13 sing N N 176 
ILE CG2 HG21 sing N N 177 
ILE CG2 HG22 sing N N 178 
ILE CG2 HG23 sing N N 179 
ILE CD1 HD11 sing N N 180 
ILE CD1 HD12 sing N N 181 
ILE CD1 HD13 sing N N 182 
ILE OXT HXT  sing N N 183 
LEU N   CA   sing N N 184 
LEU N   H    sing N N 185 
LEU N   H2   sing N N 186 
LEU CA  C    sing N N 187 
LEU CA  CB   sing N N 188 
LEU CA  HA   sing N N 189 
LEU C   O    doub N N 190 
LEU C   OXT  sing N N 191 
LEU CB  CG   sing N N 192 
LEU CB  HB2  sing N N 193 
LEU CB  HB3  sing N N 194 
LEU CG  CD1  sing N N 195 
LEU CG  CD2  sing N N 196 
LEU CG  HG   sing N N 197 
LEU CD1 HD11 sing N N 198 
LEU CD1 HD12 sing N N 199 
LEU CD1 HD13 sing N N 200 
LEU CD2 HD21 sing N N 201 
LEU CD2 HD22 sing N N 202 
LEU CD2 HD23 sing N N 203 
LEU OXT HXT  sing N N 204 
LYS N   CA   sing N N 205 
LYS N   H    sing N N 206 
LYS N   H2   sing N N 207 
LYS CA  C    sing N N 208 
LYS CA  CB   sing N N 209 
LYS CA  HA   sing N N 210 
LYS C   O    doub N N 211 
LYS C   OXT  sing N N 212 
LYS CB  CG   sing N N 213 
LYS CB  HB2  sing N N 214 
LYS CB  HB3  sing N N 215 
LYS CG  CD   sing N N 216 
LYS CG  HG2  sing N N 217 
LYS CG  HG3  sing N N 218 
LYS CD  CE   sing N N 219 
LYS CD  HD2  sing N N 220 
LYS CD  HD3  sing N N 221 
LYS CE  NZ   sing N N 222 
LYS CE  HE2  sing N N 223 
LYS CE  HE3  sing N N 224 
LYS NZ  HZ1  sing N N 225 
LYS NZ  HZ2  sing N N 226 
LYS NZ  HZ3  sing N N 227 
LYS OXT HXT  sing N N 228 
MET N   CA   sing N N 229 
MET N   H    sing N N 230 
MET N   H2   sing N N 231 
MET CA  C    sing N N 232 
MET CA  CB   sing N N 233 
MET CA  HA   sing N N 234 
MET C   O    doub N N 235 
MET C   OXT  sing N N 236 
MET CB  CG   sing N N 237 
MET CB  HB2  sing N N 238 
MET CB  HB3  sing N N 239 
MET CG  SD   sing N N 240 
MET CG  HG2  sing N N 241 
MET CG  HG3  sing N N 242 
MET SD  CE   sing N N 243 
MET CE  HE1  sing N N 244 
MET CE  HE2  sing N N 245 
MET CE  HE3  sing N N 246 
MET OXT HXT  sing N N 247 
PHE N   CA   sing N N 248 
PHE N   H    sing N N 249 
PHE N   H2   sing N N 250 
PHE CA  C    sing N N 251 
PHE CA  CB   sing N N 252 
PHE CA  HA   sing N N 253 
PHE C   O    doub N N 254 
PHE C   OXT  sing N N 255 
PHE CB  CG   sing N N 256 
PHE CB  HB2  sing N N 257 
PHE CB  HB3  sing N N 258 
PHE CG  CD1  doub Y N 259 
PHE CG  CD2  sing Y N 260 
PHE CD1 CE1  sing Y N 261 
PHE CD1 HD1  sing N N 262 
PHE CD2 CE2  doub Y N 263 
PHE CD2 HD2  sing N N 264 
PHE CE1 CZ   doub Y N 265 
PHE CE1 HE1  sing N N 266 
PHE CE2 CZ   sing Y N 267 
PHE CE2 HE2  sing N N 268 
PHE CZ  HZ   sing N N 269 
PHE OXT HXT  sing N N 270 
PRO N   CA   sing N N 271 
PRO N   CD   sing N N 272 
PRO N   H    sing N N 273 
PRO CA  C    sing N N 274 
PRO CA  CB   sing N N 275 
PRO CA  HA   sing N N 276 
PRO C   O    doub N N 277 
PRO C   OXT  sing N N 278 
PRO CB  CG   sing N N 279 
PRO CB  HB2  sing N N 280 
PRO CB  HB3  sing N N 281 
PRO CG  CD   sing N N 282 
PRO CG  HG2  sing N N 283 
PRO CG  HG3  sing N N 284 
PRO CD  HD2  sing N N 285 
PRO CD  HD3  sing N N 286 
PRO OXT HXT  sing N N 287 
SER N   CA   sing N N 288 
SER N   H    sing N N 289 
SER N   H2   sing N N 290 
SER CA  C    sing N N 291 
SER CA  CB   sing N N 292 
SER CA  HA   sing N N 293 
SER C   O    doub N N 294 
SER C   OXT  sing N N 295 
SER CB  OG   sing N N 296 
SER CB  HB2  sing N N 297 
SER CB  HB3  sing N N 298 
SER OG  HG   sing N N 299 
SER OXT HXT  sing N N 300 
THR N   CA   sing N N 301 
THR N   H    sing N N 302 
THR N   H2   sing N N 303 
THR CA  C    sing N N 304 
THR CA  CB   sing N N 305 
THR CA  HA   sing N N 306 
THR C   O    doub N N 307 
THR C   OXT  sing N N 308 
THR CB  OG1  sing N N 309 
THR CB  CG2  sing N N 310 
THR CB  HB   sing N N 311 
THR OG1 HG1  sing N N 312 
THR CG2 HG21 sing N N 313 
THR CG2 HG22 sing N N 314 
THR CG2 HG23 sing N N 315 
THR OXT HXT  sing N N 316 
TRP N   CA   sing N N 317 
TRP N   H    sing N N 318 
TRP N   H2   sing N N 319 
TRP CA  C    sing N N 320 
TRP CA  CB   sing N N 321 
TRP CA  HA   sing N N 322 
TRP C   O    doub N N 323 
TRP C   OXT  sing N N 324 
TRP CB  CG   sing N N 325 
TRP CB  HB2  sing N N 326 
TRP CB  HB3  sing N N 327 
TRP CG  CD1  doub Y N 328 
TRP CG  CD2  sing Y N 329 
TRP CD1 NE1  sing Y N 330 
TRP CD1 HD1  sing N N 331 
TRP CD2 CE2  doub Y N 332 
TRP CD2 CE3  sing Y N 333 
TRP NE1 CE2  sing Y N 334 
TRP NE1 HE1  sing N N 335 
TRP CE2 CZ2  sing Y N 336 
TRP CE3 CZ3  doub Y N 337 
TRP CE3 HE3  sing N N 338 
TRP CZ2 CH2  doub Y N 339 
TRP CZ2 HZ2  sing N N 340 
TRP CZ3 CH2  sing Y N 341 
TRP CZ3 HZ3  sing N N 342 
TRP CH2 HH2  sing N N 343 
TRP OXT HXT  sing N N 344 
TYR N   CA   sing N N 345 
TYR N   H    sing N N 346 
TYR N   H2   sing N N 347 
TYR CA  C    sing N N 348 
TYR CA  CB   sing N N 349 
TYR CA  HA   sing N N 350 
TYR C   O    doub N N 351 
TYR C   OXT  sing N N 352 
TYR CB  CG   sing N N 353 
TYR CB  HB2  sing N N 354 
TYR CB  HB3  sing N N 355 
TYR CG  CD1  doub Y N 356 
TYR CG  CD2  sing Y N 357 
TYR CD1 CE1  sing Y N 358 
TYR CD1 HD1  sing N N 359 
TYR CD2 CE2  doub Y N 360 
TYR CD2 HD2  sing N N 361 
TYR CE1 CZ   doub Y N 362 
TYR CE1 HE1  sing N N 363 
TYR CE2 CZ   sing Y N 364 
TYR CE2 HE2  sing N N 365 
TYR CZ  OH   sing N N 366 
TYR OH  HH   sing N N 367 
TYR OXT HXT  sing N N 368 
VAL N   CA   sing N N 369 
VAL N   H    sing N N 370 
VAL N   H2   sing N N 371 
VAL CA  C    sing N N 372 
VAL CA  CB   sing N N 373 
VAL CA  HA   sing N N 374 
VAL C   O    doub N N 375 
VAL C   OXT  sing N N 376 
VAL CB  CG1  sing N N 377 
VAL CB  CG2  sing N N 378 
VAL CB  HB   sing N N 379 
VAL CG1 HG11 sing N N 380 
VAL CG1 HG12 sing N N 381 
VAL CG1 HG13 sing N N 382 
VAL CG2 HG21 sing N N 383 
VAL CG2 HG22 sing N N 384 
VAL CG2 HG23 sing N N 385 
VAL OXT HXT  sing N N 386 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other private'                                       China 2023YFF1103600 1 
'National Natural Science Foundation of China (NSFC)' China 22308118       2 
'Other private'                                       China BK20231045     3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   2YFR 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2YFR 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XVQ 
_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]   0.014237 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010008 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006535 
_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  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 177 ? 28.149  13.665  -52.700 1.00 48.83 ? 177  ALA A N   1 
ATOM   2    C  CA  . ALA A 1 177 ? 26.946  14.448  -53.083 1.00 48.30 ? 177  ALA A CA  1 
ATOM   3    C  C   . ALA A 1 177 ? 25.973  13.664  -53.983 1.00 49.19 ? 177  ALA A C   1 
ATOM   4    O  O   . ALA A 1 177 ? 24.871  14.134  -54.216 1.00 53.02 ? 177  ALA A O   1 
ATOM   5    C  CB  . ALA A 1 177 ? 27.368  15.750  -53.765 1.00 47.47 ? 177  ALA A CB  1 
ATOM   6    N  N   . LYS A 1 178 ? 26.362  12.487  -54.480 1.00 49.93 ? 178  LYS A N   1 
ATOM   7    C  CA  . LYS A 1 178 ? 25.534  11.735  -55.444 1.00 50.63 ? 178  LYS A CA  1 
ATOM   8    C  C   . LYS A 1 178 ? 25.282  10.277  -55.036 1.00 47.28 ? 178  LYS A C   1 
ATOM   9    O  O   . LYS A 1 178 ? 26.218  9.505   -54.842 1.00 46.19 ? 178  LYS A O   1 
ATOM   10   C  CB  . LYS A 1 178 ? 26.176  11.774  -56.833 1.00 54.36 ? 178  LYS A CB  1 
ATOM   11   C  CG  . LYS A 1 178 ? 26.529  13.177  -57.327 1.00 58.10 ? 178  LYS A CG  1 
ATOM   12   C  CD  . LYS A 1 178 ? 25.296  14.059  -57.516 1.00 62.00 ? 178  LYS A CD  1 
ATOM   13   C  CE  . LYS A 1 178 ? 25.660  15.501  -57.851 1.00 65.15 ? 178  LYS A CE  1 
ATOM   14   N  NZ  . LYS A 1 178 ? 26.243  15.633  -59.216 1.00 66.19 ? 178  LYS A NZ  1 
ATOM   15   N  N   . LEU A 1 179 ? 24.002  9.920   -54.929 1.00 44.70 ? 179  LEU A N   1 
ATOM   16   C  CA  . LEU A 1 179 ? 23.567  8.593   -54.514 1.00 43.82 ? 179  LEU A CA  1 
ATOM   17   C  C   . LEU A 1 179 ? 23.949  7.519   -55.526 1.00 43.16 ? 179  LEU A C   1 
ATOM   18   O  O   . LEU A 1 179 ? 23.835  7.732   -56.731 1.00 41.03 ? 179  LEU A O   1 
ATOM   19   C  CB  . LEU A 1 179 ? 22.042  8.567   -54.368 1.00 44.11 ? 179  LEU A CB  1 
ATOM   20   C  CG  . LEU A 1 179 ? 21.368  9.393   -53.266 1.00 45.62 ? 179  LEU A CG  1 
ATOM   21   C  CD1 . LEU A 1 179 ? 19.959  9.795   -53.683 1.00 44.04 ? 179  LEU A CD1 1 
ATOM   22   C  CD2 . LEU A 1 179 ? 21.335  8.617   -51.952 1.00 45.58 ? 179  LEU A CD2 1 
ATOM   23   N  N   . ASN A 1 180 ? 24.371  6.355   -55.041 1.00 42.15 ? 180  ASN A N   1 
ATOM   24   C  CA  . ASN A 1 180 ? 24.500  5.193   -55.906 1.00 41.68 ? 180  ASN A CA  1 
ATOM   25   C  C   . ASN A 1 180 ? 23.097  4.755   -56.291 1.00 43.26 ? 180  ASN A C   1 
ATOM   26   O  O   . ASN A 1 180 ? 22.120  5.252   -55.716 1.00 42.59 ? 180  ASN A O   1 
ATOM   27   C  CB  . ASN A 1 180 ? 25.318  4.069   -55.243 1.00 43.34 ? 180  ASN A CB  1 
ATOM   28   C  CG  . ASN A 1 180 ? 24.586  3.365   -54.097 1.00 44.23 ? 180  ASN A CG  1 
ATOM   29   O  OD1 . ASN A 1 180 ? 23.365  3.216   -54.105 1.00 45.07 ? 180  ASN A OD1 1 
ATOM   30   N  ND2 . ASN A 1 180 ? 25.353  2.886   -53.124 1.00 43.07 ? 180  ASN A ND2 1 
ATOM   31   N  N   . LYS A 1 181 ? 22.986  3.842   -57.253 1.00 44.87 ? 181  LYS A N   1 
ATOM   32   C  CA  . LYS A 1 181 ? 21.680  3.529   -57.847 1.00 46.82 ? 181  LYS A CA  1 
ATOM   33   C  C   . LYS A 1 181 ? 20.743  2.790   -56.893 1.00 46.92 ? 181  LYS A C   1 
ATOM   34   O  O   . LYS A 1 181 ? 19.539  3.065   -56.873 1.00 45.99 ? 181  LYS A O   1 
ATOM   35   C  CB  . LYS A 1 181 ? 21.817  2.768   -59.178 1.00 49.77 ? 181  LYS A CB  1 
ATOM   36   C  CG  . LYS A 1 181 ? 22.429  1.375   -59.114 1.00 52.74 ? 181  LYS A CG  1 
ATOM   37   C  CD  . LYS A 1 181 ? 22.160  0.602   -60.403 1.00 56.13 ? 181  LYS A CD  1 
ATOM   38   C  CE  . LYS A 1 181 ? 23.090  -0.592  -60.567 1.00 58.60 ? 181  LYS A CE  1 
ATOM   39   N  NZ  . LYS A 1 181 ? 23.307  -1.342  -59.296 1.00 61.06 ? 181  LYS A NZ  1 
ATOM   40   N  N   . ASP A 1 182 ? 21.294  1.859   -56.113 1.00 44.88 ? 182  ASP A N   1 
ATOM   41   C  CA  . ASP A 1 182 ? 20.523  1.159   -55.085 1.00 44.64 ? 182  ASP A CA  1 
ATOM   42   C  C   . ASP A 1 182 ? 19.887  2.154   -54.128 1.00 40.16 ? 182  ASP A C   1 
ATOM   43   O  O   . ASP A 1 182 ? 18.684  2.110   -53.889 1.00 40.13 ? 182  ASP A O   1 
ATOM   44   C  CB  . ASP A 1 182 ? 21.418  0.208   -54.286 1.00 47.28 ? 182  ASP A CB  1 
ATOM   45   C  CG  . ASP A 1 182 ? 21.688  -1.080  -55.006 1.00 48.92 ? 182  ASP A CG  1 
ATOM   46   O  OD1 . ASP A 1 182 ? 20.801  -1.542  -55.752 1.00 51.34 ? 182  ASP A OD1 1 
ATOM   47   O  OD2 . ASP A 1 182 ? 22.784  -1.644  -54.804 1.00 55.67 ? 182  ASP A OD2 1 
ATOM   48   N  N   . ALA A 1 183 ? 20.717  3.047   -53.602 1.00 36.49 ? 183  ALA A N   1 
ATOM   49   C  CA  . ALA A 1 183 ? 20.295  4.091   -52.675 1.00 36.05 ? 183  ALA A CA  1 
ATOM   50   C  C   . ALA A 1 183 ? 19.256  5.036   -53.288 1.00 35.99 ? 183  ALA A C   1 
ATOM   51   O  O   . ALA A 1 183 ? 18.278  5.388   -52.637 1.00 33.99 ? 183  ALA A O   1 
ATOM   52   C  CB  . ALA A 1 183 ? 21.512  4.880   -52.199 1.00 34.84 ? 183  ALA A CB  1 
ATOM   53   N  N   . GLU A 1 184 ? 19.470  5.447   -54.539 1.00 39.00 ? 184  GLU A N   1 
ATOM   54   C  CA  . GLU A 1 184 ? 18.479  6.271   -55.246 1.00 40.09 ? 184  GLU A CA  1 
ATOM   55   C  C   . GLU A 1 184 ? 17.167  5.493   -55.441 1.00 39.38 ? 184  GLU A C   1 
ATOM   56   O  O   . GLU A 1 184 ? 16.081  6.070   -55.378 1.00 39.17 ? 184  GLU A O   1 
ATOM   57   C  CB  . GLU A 1 184 ? 19.035  6.774   -56.589 1.00 43.10 ? 184  GLU A CB  1 
ATOM   58   C  CG  . GLU A 1 184 ? 18.091  7.711   -57.352 1.00 44.86 ? 184  GLU A CG  1 
ATOM   59   C  CD  . GLU A 1 184 ? 18.629  8.180   -58.702 1.00 46.22 ? 184  GLU A CD  1 
ATOM   60   O  OE1 . GLU A 1 184 ? 19.546  7.543   -59.257 1.00 48.48 ? 184  GLU A OE1 1 
ATOM   61   O  OE2 . GLU A 1 184 ? 18.118  9.192   -59.224 1.00 49.19 ? 184  GLU A OE2 1 
ATOM   62   N  N   . ASN A 1 185 ? 17.257  4.184   -55.662 1.00 40.70 ? 185  ASN A N   1 
ATOM   63   C  CA  . ASN A 1 185 ? 16.055  3.366   -55.783 1.00 41.36 ? 185  ASN A CA  1 
ATOM   64   C  C   . ASN A 1 185 ? 15.193  3.428   -54.516 1.00 40.57 ? 185  ASN A C   1 
ATOM   65   O  O   . ASN A 1 185 ? 14.005  3.763   -54.596 1.00 41.05 ? 185  ASN A O   1 
ATOM   66   C  CB  . ASN A 1 185 ? 16.394  1.912   -56.139 1.00 45.14 ? 185  ASN A CB  1 
ATOM   67   C  CG  . ASN A 1 185 ? 16.800  1.730   -57.603 1.00 49.48 ? 185  ASN A CG  1 
ATOM   68   O  OD1 . ASN A 1 185 ? 16.835  0.604   -58.107 1.00 53.03 ? 185  ASN A OD1 1 
ATOM   69   N  ND2 . ASN A 1 185 ? 17.116  2.829   -58.290 1.00 50.91 ? 185  ASN A ND2 1 
ATOM   70   N  N   . VAL A 1 186 ? 15.785  3.148   -53.351 1.00 37.87 ? 186  VAL A N   1 
ATOM   71   C  CA  . VAL A 1 186 ? 15.014  3.146   -52.090 1.00 35.28 ? 186  VAL A CA  1 
ATOM   72   C  C   . VAL A 1 186 ? 14.524  4.542   -51.720 1.00 34.58 ? 186  VAL A C   1 
ATOM   73   O  O   . VAL A 1 186 ? 13.409  4.707   -51.206 1.00 31.80 ? 186  VAL A O   1 
ATOM   74   C  CB  . VAL A 1 186 ? 15.787  2.520   -50.890 1.00 34.05 ? 186  VAL A CB  1 
ATOM   75   C  CG1 . VAL A 1 186 ? 16.211  1.089   -51.204 1.00 33.70 ? 186  VAL A CG1 1 
ATOM   76   C  CG2 . VAL A 1 186 ? 16.998  3.344   -50.485 1.00 32.94 ? 186  VAL A CG2 1 
ATOM   77   N  N   . VAL A 1 187 ? 15.358  5.545   -51.974 1.00 34.73 ? 187  VAL A N   1 
ATOM   78   C  CA  . VAL A 1 187 ? 14.949  6.925   -51.746 1.00 37.52 ? 187  VAL A CA  1 
ATOM   79   C  C   . VAL A 1 187 ? 13.660  7.190   -52.533 1.00 38.15 ? 187  VAL A C   1 
ATOM   80   O  O   . VAL A 1 187 ? 12.683  7.712   -51.986 1.00 36.03 ? 187  VAL A O   1 
ATOM   81   C  CB  . VAL A 1 187 ? 16.052  7.928   -52.142 1.00 37.70 ? 187  VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 187 ? 15.504  9.351   -52.217 1.00 39.13 ? 187  VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 187 ? 17.207  7.862   -51.155 1.00 37.37 ? 187  VAL A CG2 1 
ATOM   84   N  N   . LYS A 1 188 ? 13.648  6.775   -53.797 1.00 39.31 ? 188  LYS A N   1 
ATOM   85   C  CA  . LYS A 1 188 ? 12.501  7.021   -54.665 1.00 41.10 ? 188  LYS A CA  1 
ATOM   86   C  C   . LYS A 1 188 ? 11.294  6.128   -54.327 1.00 41.40 ? 188  LYS A C   1 
ATOM   87   O  O   . LYS A 1 188 ? 10.160  6.605   -54.331 1.00 39.51 ? 188  LYS A O   1 
ATOM   88   C  CB  . LYS A 1 188 ? 12.896  6.909   -56.141 1.00 42.04 ? 188  LYS A CB  1 
ATOM   89   C  CG  . LYS A 1 188 ? 13.503  8.198   -56.693 1.00 44.09 ? 188  LYS A CG  1 
ATOM   90   C  CD  . LYS A 1 188 ? 13.502  8.248   -58.220 1.00 45.25 ? 188  LYS A CD  1 
ATOM   91   C  CE  . LYS A 1 188 ? 14.833  7.821   -58.809 1.00 45.55 ? 188  LYS A CE  1 
ATOM   92   N  NZ  . LYS A 1 188 ? 14.818  7.914   -60.294 1.00 46.24 ? 188  LYS A NZ  1 
ATOM   93   N  N   . LYS A 1 189 ? 11.532  4.856   -54.018 1.00 41.36 ? 189  LYS A N   1 
ATOM   94   C  CA  . LYS A 1 189 ? 10.474  4.003   -53.487 1.00 42.13 ? 189  LYS A CA  1 
ATOM   95   C  C   . LYS A 1 189 ? 9.843   4.629   -52.240 1.00 40.87 ? 189  LYS A C   1 
ATOM   96   O  O   . LYS A 1 189 ? 8.645   4.461   -51.995 1.00 40.10 ? 189  LYS A O   1 
ATOM   97   C  CB  . LYS A 1 189 ? 11.012  2.605   -53.165 1.00 45.24 ? 189  LYS A CB  1 
ATOM   98   C  CG  . LYS A 1 189 ? 11.260  1.738   -54.396 1.00 47.50 ? 189  LYS A CG  1 
ATOM   99   C  CD  . LYS A 1 189 ? 11.523  0.276   -54.038 1.00 50.87 ? 189  LYS A CD  1 
ATOM   100  C  CE  . LYS A 1 189 ? 13.008  -0.012  -53.828 1.00 52.95 ? 189  LYS A CE  1 
ATOM   101  N  NZ  . LYS A 1 189 ? 13.241  -1.104  -52.831 1.00 54.70 ? 189  LYS A NZ  1 
ATOM   102  N  N   . ALA A 1 190 ? 10.651  5.360   -51.468 1.00 39.18 ? 190  ALA A N   1 
ATOM   103  C  CA  . ALA A 1 190 ? 10.187  6.050   -50.249 1.00 39.59 ? 190  ALA A CA  1 
ATOM   104  C  C   . ALA A 1 190 ? 9.394   7.352   -50.473 1.00 39.44 ? 190  ALA A C   1 
ATOM   105  O  O   . ALA A 1 190 ? 8.814   7.882   -49.519 1.00 39.43 ? 190  ALA A O   1 
ATOM   106  C  CB  . ALA A 1 190 ? 11.372  6.328   -49.319 1.00 37.85 ? 190  ALA A CB  1 
ATOM   107  N  N   . GLY A 1 191 ? 9.371   7.872   -51.701 1.00 39.49 ? 191  GLY A N   1 
ATOM   108  C  CA  . GLY A 1 191 ? 8.723   9.154   -51.986 1.00 39.54 ? 191  GLY A CA  1 
ATOM   109  C  C   . GLY A 1 191 ? 9.515   10.373  -51.525 1.00 40.40 ? 191  GLY A C   1 
ATOM   110  O  O   . GLY A 1 191 ? 8.960   11.460  -51.373 1.00 39.30 ? 191  GLY A O   1 
ATOM   111  N  N   . ILE A 1 192 ? 10.815  10.193  -51.303 1.00 40.74 ? 192  ILE A N   1 
ATOM   112  C  CA  . ILE A 1 192 ? 11.700  11.288  -50.917 1.00 40.14 ? 192  ILE A CA  1 
ATOM   113  C  C   . ILE A 1 192 ? 12.367  11.839  -52.177 1.00 40.44 ? 192  ILE A C   1 
ATOM   114  O  O   . ILE A 1 192 ? 12.867  11.081  -53.004 1.00 39.47 ? 192  ILE A O   1 
ATOM   115  C  CB  . ILE A 1 192 ? 12.774  10.802  -49.912 1.00 40.18 ? 192  ILE A CB  1 
ATOM   116  C  CG1 . ILE A 1 192 ? 12.122  10.433  -48.575 1.00 39.52 ? 192  ILE A CG1 1 
ATOM   117  C  CG2 . ILE A 1 192 ? 13.841  11.869  -49.697 1.00 40.86 ? 192  ILE A CG2 1 
ATOM   118  C  CD1 . ILE A 1 192 ? 12.948  9.499   -47.717 1.00 38.99 ? 192  ILE A CD1 1 
ATOM   119  N  N   . ASP A 1 193 ? 12.356  13.160  -52.321 1.00 43.72 ? 193  ASP A N   1 
ATOM   120  C  CA  . ASP A 1 193 ? 13.073  13.839  -53.407 1.00 44.06 ? 193  ASP A CA  1 
ATOM   121  C  C   . ASP A 1 193 ? 14.582  13.795  -53.126 1.00 41.71 ? 193  ASP A C   1 
ATOM   122  O  O   . ASP A 1 193 ? 15.039  14.355  -52.133 1.00 39.05 ? 193  ASP A O   1 
ATOM   123  C  CB  . ASP A 1 193 ? 12.589  15.300  -53.542 1.00 45.74 ? 193  ASP A CB  1 
ATOM   124  C  CG  . ASP A 1 193 ? 13.533  16.177  -54.376 1.00 47.24 ? 193  ASP A CG  1 
ATOM   125  O  OD1 . ASP A 1 193 ? 14.044  15.709  -55.412 1.00 47.38 ? 193  ASP A OD1 1 
ATOM   126  O  OD2 . ASP A 1 193 ? 13.753  17.349  -53.992 1.00 49.74 ? 193  ASP A OD2 1 
ATOM   127  N  N   . PRO A 1 194 ? 15.359  13.136  -54.003 1.00 40.88 ? 194  PRO A N   1 
ATOM   128  C  CA  . PRO A 1 194 ? 16.799  13.034  -53.779 1.00 41.40 ? 194  PRO A CA  1 
ATOM   129  C  C   . PRO A 1 194 ? 17.494  14.374  -53.548 1.00 44.73 ? 194  PRO A C   1 
ATOM   130  O  O   . PRO A 1 194 ? 18.458  14.444  -52.787 1.00 43.28 ? 194  PRO A O   1 
ATOM   131  C  CB  . PRO A 1 194 ? 17.298  12.380  -55.065 1.00 41.68 ? 194  PRO A CB  1 
ATOM   132  C  CG  . PRO A 1 194 ? 16.154  11.539  -55.509 1.00 41.15 ? 194  PRO A CG  1 
ATOM   133  C  CD  . PRO A 1 194 ? 14.939  12.360  -55.185 1.00 40.57 ? 194  PRO A CD  1 
ATOM   134  N  N   . ASN A 1 195 ? 17.000  15.429  -54.191 1.00 47.89 ? 195  ASN A N   1 
ATOM   135  C  CA  . ASN A 1 195 ? 17.549  16.771  -54.003 1.00 49.42 ? 195  ASN A CA  1 
ATOM   136  C  C   . ASN A 1 195 ? 17.391  17.332  -52.594 1.00 50.13 ? 195  ASN A C   1 
ATOM   137  O  O   . ASN A 1 195 ? 18.117  18.251  -52.220 1.00 53.48 ? 195  ASN A O   1 
ATOM   138  C  CB  . ASN A 1 195 ? 16.936  17.753  -55.009 1.00 51.56 ? 195  ASN A CB  1 
ATOM   139  C  CG  . ASN A 1 195 ? 17.718  17.819  -56.299 1.00 52.63 ? 195  ASN A CG  1 
ATOM   140  O  OD1 . ASN A 1 195 ? 18.422  18.800  -56.554 1.00 59.21 ? 195  ASN A OD1 1 
ATOM   141  N  ND2 . ASN A 1 195 ? 17.619  16.774  -57.114 1.00 50.10 ? 195  ASN A ND2 1 
ATOM   142  N  N   . SER A 1 196 ? 16.454  16.793  -51.815 1.00 49.96 ? 196  SER A N   1 
ATOM   143  C  CA  . SER A 1 196 ? 16.198  17.300  -50.462 1.00 49.47 ? 196  SER A CA  1 
ATOM   144  C  C   . SER A 1 196 ? 17.247  16.837  -49.441 1.00 48.56 ? 196  SER A C   1 
ATOM   145  O  O   . SER A 1 196 ? 17.373  17.422  -48.361 1.00 47.95 ? 196  SER A O   1 
ATOM   146  C  CB  . SER A 1 196 ? 14.798  16.881  -49.997 1.00 49.85 ? 196  SER A CB  1 
ATOM   147  O  OG  . SER A 1 196 ? 14.650  15.472  -50.000 1.00 48.97 ? 196  SER A OG  1 
ATOM   148  N  N   . LEU A 1 197 ? 17.995  15.792  -49.792 1.00 44.90 ? 197  LEU A N   1 
ATOM   149  C  CA  . LEU A 1 197 ? 18.939  15.173  -48.875 1.00 43.56 ? 197  LEU A CA  1 
ATOM   150  C  C   . LEU A 1 197 ? 20.207  16.002  -48.721 1.00 41.90 ? 197  LEU A C   1 
ATOM   151  O  O   . LEU A 1 197 ? 20.645  16.666  -49.652 1.00 43.23 ? 197  LEU A O   1 
ATOM   152  C  CB  . LEU A 1 197 ? 19.310  13.770  -49.371 1.00 44.24 ? 197  LEU A CB  1 
ATOM   153  C  CG  . LEU A 1 197 ? 18.155  12.773  -49.486 1.00 44.51 ? 197  LEU A CG  1 
ATOM   154  C  CD1 . LEU A 1 197 ? 18.618  11.467  -50.124 1.00 43.85 ? 197  LEU A CD1 1 
ATOM   155  C  CD2 . LEU A 1 197 ? 17.549  12.525  -48.113 1.00 44.99 ? 197  LEU A CD2 1 
ATOM   156  N  N   . THR A 1 198 ? 20.795  15.948  -47.536 1.00 40.30 ? 198  THR A N   1 
ATOM   157  C  CA  . THR A 1 198 ? 22.080  16.584  -47.273 1.00 39.04 ? 198  THR A CA  1 
ATOM   158  C  C   . THR A 1 198 ? 23.229  15.682  -47.738 1.00 39.81 ? 198  THR A C   1 
ATOM   159  O  O   . THR A 1 198 ? 23.009  14.508  -48.049 1.00 39.91 ? 198  THR A O   1 
ATOM   160  C  CB  . THR A 1 198 ? 22.259  16.799  -45.775 1.00 38.38 ? 198  THR A CB  1 
ATOM   161  O  OG1 . THR A 1 198 ? 22.269  15.523  -45.126 1.00 37.55 ? 198  THR A OG1 1 
ATOM   162  C  CG2 . THR A 1 198 ? 21.121  17.662  -45.211 1.00 38.49 ? 198  THR A CG2 1 
ATOM   163  N  N   . ASP A 1 199 ? 24.447  16.223  -47.759 1.00 38.78 ? 199  ASP A N   1 
ATOM   164  C  CA  . ASP A 1 199 ? 25.646  15.443  -48.090 1.00 40.29 ? 199  ASP A CA  1 
ATOM   165  C  C   . ASP A 1 199 ? 25.872  14.269  -47.117 1.00 38.33 ? 199  ASP A C   1 
ATOM   166  O  O   . ASP A 1 199 ? 26.261  13.185  -47.547 1.00 35.11 ? 199  ASP A O   1 
ATOM   167  C  CB  . ASP A 1 199 ? 26.905  16.334  -48.131 1.00 42.91 ? 199  ASP A CB  1 
ATOM   168  C  CG  . ASP A 1 199 ? 27.120  17.024  -49.495 1.00 46.73 ? 199  ASP A CG  1 
ATOM   169  O  OD1 . ASP A 1 199 ? 26.288  16.899  -50.423 1.00 49.32 ? 199  ASP A OD1 1 
ATOM   170  O  OD2 . ASP A 1 199 ? 28.154  17.703  -49.641 1.00 51.01 ? 199  ASP A OD2 1 
ATOM   171  N  N   . ASP A 1 200 ? 25.629  14.491  -45.824 1.00 36.51 ? 200  ASP A N   1 
ATOM   172  C  CA  . ASP A 1 200 ? 25.744  13.431  -44.811 1.00 38.18 ? 200  ASP A CA  1 
ATOM   173  C  C   . ASP A 1 200 ? 24.694  12.326  -44.945 1.00 35.95 ? 200  ASP A C   1 
ATOM   174  O  O   . ASP A 1 200 ? 24.986  11.169  -44.664 1.00 37.31 ? 200  ASP A O   1 
ATOM   175  C  CB  . ASP A 1 200 ? 25.666  14.010  -43.393 1.00 40.39 ? 200  ASP A CB  1 
ATOM   176  C  CG  . ASP A 1 200 ? 26.931  14.758  -42.987 1.00 44.12 ? 200  ASP A CG  1 
ATOM   177  O  OD1 . ASP A 1 200 ? 27.991  14.586  -43.642 1.00 46.60 ? 200  ASP A OD1 1 
ATOM   178  O  OD2 . ASP A 1 200 ? 26.860  15.518  -41.997 1.00 45.81 ? 200  ASP A OD2 1 
ATOM   179  N  N   . GLN A 1 201 ? 23.483  12.684  -45.354 1.00 33.44 ? 201  GLN A N   1 
ATOM   180  C  CA  . GLN A 1 201 ? 22.414  11.704  -45.570 1.00 32.83 ? 201  GLN A CA  1 
ATOM   181  C  C   . GLN A 1 201 ? 22.694  10.813  -46.779 1.00 31.12 ? 201  GLN A C   1 
ATOM   182  O  O   . GLN A 1 201 ? 22.433  9.619   -46.748 1.00 27.72 ? 201  GLN A O   1 
ATOM   183  C  CB  . GLN A 1 201 ? 21.069  12.412  -45.752 1.00 32.63 ? 201  GLN A CB  1 
ATOM   184  C  CG  . GLN A 1 201 ? 20.524  12.996  -44.463 1.00 33.79 ? 201  GLN A CG  1 
ATOM   185  C  CD  . GLN A 1 201 ? 19.388  13.990  -44.677 1.00 34.72 ? 201  GLN A CD  1 
ATOM   186  O  OE1 . GLN A 1 201 ? 19.208  14.537  -45.766 1.00 34.23 ? 201  GLN A OE1 1 
ATOM   187  N  NE2 . GLN A 1 201 ? 18.631  14.243  -43.623 1.00 36.08 ? 201  GLN A NE2 1 
ATOM   188  N  N   . ILE A 1 202 ? 23.210  11.423  -47.845 1.00 29.74 ? 202  ILE A N   1 
ATOM   189  C  CA  . ILE A 1 202 ? 23.615  10.705  -49.037 1.00 30.21 ? 202  ILE A CA  1 
ATOM   190  C  C   . ILE A 1 202 ? 24.742  9.745   -48.695 1.00 29.31 ? 202  ILE A C   1 
ATOM   191  O  O   . ILE A 1 202 ? 24.681  8.588   -49.082 1.00 30.28 ? 202  ILE A O   1 
ATOM   192  C  CB  . ILE A 1 202 ? 24.060  11.681  -50.163 1.00 31.03 ? 202  ILE A CB  1 
ATOM   193  C  CG1 . ILE A 1 202 ? 22.836  12.423  -50.720 1.00 31.36 ? 202  ILE A CG1 1 
ATOM   194  C  CG2 . ILE A 1 202 ? 24.790  10.942  -51.277 1.00 29.56 ? 202  ILE A CG2 1 
ATOM   195  C  CD1 . ILE A 1 202 ? 23.182  13.645  -51.547 1.00 31.91 ? 202  ILE A CD1 1 
ATOM   196  N  N   . LYS A 1 203 ? 25.746  10.224  -47.960 1.00 29.15 ? 203  LYS A N   1 
ATOM   197  C  CA  . LYS A 1 203 ? 26.865  9.383   -47.518 1.00 31.08 ? 203  LYS A CA  1 
ATOM   198  C  C   . LYS A 1 203 ? 26.404  8.212   -46.644 1.00 29.45 ? 203  LYS A C   1 
ATOM   199  O  O   . LYS A 1 203 ? 26.954  7.116   -46.727 1.00 27.80 ? 203  LYS A O   1 
ATOM   200  C  CB  . LYS A 1 203 ? 27.902  10.209  -46.755 1.00 34.13 ? 203  LYS A CB  1 
ATOM   201  C  CG  . LYS A 1 203 ? 28.678  11.167  -47.654 1.00 39.58 ? 203  LYS A CG  1 
ATOM   202  C  CD  . LYS A 1 203 ? 29.528  12.164  -46.872 1.00 42.08 ? 203  LYS A CD  1 
ATOM   203  C  CE  . LYS A 1 203 ? 30.743  11.503  -46.240 1.00 45.54 ? 203  LYS A CE  1 
ATOM   204  N  NZ  . LYS A 1 203 ? 31.594  10.801  -47.248 1.00 48.79 ? 203  LYS A NZ  1 
ATOM   205  N  N   . ALA A 1 204 ? 25.406  8.447   -45.797 1.00 27.00 ? 204  ALA A N   1 
ATOM   206  C  CA  . ALA A 1 204 ? 24.878  7.373   -44.977 1.00 26.05 ? 204  ALA A CA  1 
ATOM   207  C  C   . ALA A 1 204 ? 24.243  6.336   -45.901 1.00 25.58 ? 204  ALA A C   1 
ATOM   208  O  O   . ALA A 1 204 ? 24.567  5.149   -45.823 1.00 24.89 ? 204  ALA A O   1 
ATOM   209  C  CB  . ALA A 1 204 ? 23.870  7.901   -43.966 1.00 25.78 ? 204  ALA A CB  1 
ATOM   210  N  N   . LEU A 1 205 ? 23.381  6.799   -46.806 1.00 24.96 ? 205  LEU A N   1 
ATOM   211  C  CA  . LEU A 1 205 ? 22.645  5.903   -47.692 1.00 25.40 ? 205  LEU A CA  1 
ATOM   212  C  C   . LEU A 1 205 ? 23.570  5.096   -48.623 1.00 25.81 ? 205  LEU A C   1 
ATOM   213  O  O   . LEU A 1 205 ? 23.271  3.940   -48.936 1.00 24.04 ? 205  LEU A O   1 
ATOM   214  C  CB  . LEU A 1 205 ? 21.590  6.670   -48.507 1.00 24.98 ? 205  LEU A CB  1 
ATOM   215  C  CG  . LEU A 1 205 ? 20.313  7.107   -47.768 1.00 25.14 ? 205  LEU A CG  1 
ATOM   216  C  CD1 . LEU A 1 205 ? 19.614  8.205   -48.540 1.00 25.52 ? 205  LEU A CD1 1 
ATOM   217  C  CD2 . LEU A 1 205 ? 19.352  5.950   -47.528 1.00 25.09 ? 205  LEU A CD2 1 
ATOM   218  N  N   . ASN A 1 206 ? 24.680  5.698   -49.050 1.00 25.57 ? 206  ASN A N   1 
ATOM   219  C  CA  . ASN A 1 206 ? 25.630  5.016   -49.942 1.00 26.82 ? 206  ASN A CA  1 
ATOM   220  C  C   . ASN A 1 206 ? 26.401  3.888   -49.241 1.00 26.66 ? 206  ASN A C   1 
ATOM   221  O  O   . ASN A 1 206 ? 26.942  3.021   -49.899 1.00 26.74 ? 206  ASN A O   1 
ATOM   222  C  CB  . ASN A 1 206 ? 26.627  6.008   -50.554 1.00 25.92 ? 206  ASN A CB  1 
ATOM   223  C  CG  . ASN A 1 206 ? 26.029  6.827   -51.696 1.00 27.32 ? 206  ASN A CG  1 
ATOM   224  O  OD1 . ASN A 1 206 ? 24.948  6.526   -52.215 1.00 27.98 ? 206  ASN A OD1 1 
ATOM   225  N  ND2 . ASN A 1 206 ? 26.747  7.861   -52.104 1.00 27.11 ? 206  ASN A ND2 1 
ATOM   226  N  N   . LYS A 1 207 ? 26.462  3.915   -47.918 1.00 26.50 ? 207  LYS A N   1 
ATOM   227  C  CA  . LYS A 1 207 ? 27.052  2.813   -47.160 1.00 27.16 ? 207  LYS A CA  1 
ATOM   228  C  C   . LYS A 1 207 ? 26.090  1.647   -46.955 1.00 26.49 ? 207  LYS A C   1 
ATOM   229  O  O   . LYS A 1 207 ? 26.509  0.579   -46.517 1.00 26.91 ? 207  LYS A O   1 
ATOM   230  C  CB  . LYS A 1 207 ? 27.508  3.300   -45.794 1.00 27.75 ? 207  LYS A CB  1 
ATOM   231  C  CG  . LYS A 1 207 ? 28.572  4.378   -45.862 1.00 29.88 ? 207  LYS A CG  1 
ATOM   232  C  CD  . LYS A 1 207 ? 28.872  4.921   -44.477 1.00 31.07 ? 207  LYS A CD  1 
ATOM   233  C  CE  . LYS A 1 207 ? 29.953  5.974   -44.529 1.00 31.55 ? 207  LYS A CE  1 
ATOM   234  N  NZ  . LYS A 1 207 ? 30.490  6.226   -43.168 1.00 34.39 ? 207  LYS A NZ  1 
ATOM   235  N  N   . MET A 1 208 ? 24.807  1.837   -47.252 1.00 25.50 ? 208  MET A N   1 
ATOM   236  C  CA  . MET A 1 208 ? 23.820  0.839   -46.879 1.00 26.11 ? 208  MET A CA  1 
ATOM   237  C  C   . MET A 1 208 ? 24.078  -0.452  -47.640 1.00 27.37 ? 208  MET A C   1 
ATOM   238  O  O   . MET A 1 208 ? 24.215  -0.445  -48.864 1.00 27.56 ? 208  MET A O   1 
ATOM   239  C  CB  . MET A 1 208 ? 22.387  1.329   -47.131 1.00 25.27 ? 208  MET A CB  1 
ATOM   240  C  CG  . MET A 1 208 ? 21.299  0.381   -46.617 1.00 25.49 ? 208  MET A CG  1 
ATOM   241  S  SD  . MET A 1 208 ? 21.307  0.097   -44.823 1.00 24.99 ? 208  MET A SD  1 
ATOM   242  C  CE  . MET A 1 208 ? 21.229  1.781   -44.201 1.00 25.57 ? 208  MET A CE  1 
ATOM   243  N  N   . ASN A 1 209 ? 24.129  -1.555  -46.902 1.00 27.20 ? 209  ASN A N   1 
ATOM   244  C  CA  . ASN A 1 209 ? 24.245  -2.879  -47.494 1.00 28.68 ? 209  ASN A CA  1 
ATOM   245  C  C   . ASN A 1 209 ? 22.845  -3.486  -47.655 1.00 29.45 ? 209  ASN A C   1 
ATOM   246  O  O   . ASN A 1 209 ? 22.132  -3.672  -46.667 1.00 27.63 ? 209  ASN A O   1 
ATOM   247  C  CB  . ASN A 1 209 ? 25.137  -3.754  -46.604 1.00 28.56 ? 209  ASN A CB  1 
ATOM   248  C  CG  . ASN A 1 209 ? 25.405  -5.118  -47.199 1.00 29.36 ? 209  ASN A CG  1 
ATOM   249  O  OD1 . ASN A 1 209 ? 24.744  -5.544  -48.136 1.00 30.36 ? 209  ASN A OD1 1 
ATOM   250  N  ND2 . ASN A 1 209 ? 26.398  -5.811  -46.653 1.00 31.53 ? 209  ASN A ND2 1 
ATOM   251  N  N   . PHE A 1 210 ? 22.454  -3.775  -48.893 1.00 30.93 ? 210  PHE A N   1 
ATOM   252  C  CA  . PHE A 1 210 ? 21.102  -4.266  -49.192 1.00 34.26 ? 210  PHE A CA  1 
ATOM   253  C  C   . PHE A 1 210 ? 20.930  -5.788  -49.264 1.00 36.24 ? 210  PHE A C   1 
ATOM   254  O  O   . PHE A 1 210 ? 19.867  -6.246  -49.667 1.00 36.36 ? 210  PHE A O   1 
ATOM   255  C  CB  . PHE A 1 210 ? 20.572  -3.608  -50.479 1.00 33.16 ? 210  PHE A CB  1 
ATOM   256  C  CG  . PHE A 1 210 ? 20.375  -2.133  -50.336 1.00 33.27 ? 210  PHE A CG  1 
ATOM   257  C  CD1 . PHE A 1 210 ? 19.293  -1.636  -49.612 1.00 33.33 ? 210  PHE A CD1 1 
ATOM   258  C  CD2 . PHE A 1 210 ? 21.296  -1.240  -50.857 1.00 33.17 ? 210  PHE A CD2 1 
ATOM   259  C  CE1 . PHE A 1 210 ? 19.111  -0.277  -49.441 1.00 32.33 ? 210  PHE A CE1 1 
ATOM   260  C  CE2 . PHE A 1 210 ? 21.118  0.128   -50.689 1.00 33.25 ? 210  PHE A CE2 1 
ATOM   261  C  CZ  . PHE A 1 210 ? 20.028  0.609   -49.975 1.00 32.94 ? 210  PHE A CZ  1 
ATOM   262  N  N   . SER A 1 211 ? 21.926  -6.574  -48.848 1.00 39.51 ? 211  SER A N   1 
ATOM   263  C  CA  . SER A 1 211 ? 21.790  -8.042  -48.908 1.00 43.11 ? 211  SER A CA  1 
ATOM   264  C  C   . SER A 1 211 ? 20.701  -8.549  -47.947 1.00 47.49 ? 211  SER A C   1 
ATOM   265  O  O   . SER A 1 211 ? 20.573  -8.063  -46.819 1.00 48.26 ? 211  SER A O   1 
ATOM   266  C  CB  . SER A 1 211 ? 23.114  -8.738  -48.611 1.00 41.99 ? 211  SER A CB  1 
ATOM   267  O  OG  . SER A 1 211 ? 23.421  -8.627  -47.242 1.00 42.88 ? 211  SER A OG  1 
ATOM   268  N  N   . LYS A 1 212 ? 19.915  -9.522  -48.404 1.00 50.06 ? 212  LYS A N   1 
ATOM   269  C  CA  . LYS A 1 212 ? 18.760  -9.988  -47.648 1.00 51.67 ? 212  LYS A CA  1 
ATOM   270  C  C   . LYS A 1 212 ? 19.003  -11.351 -46.981 1.00 51.77 ? 212  LYS A C   1 
ATOM   271  O  O   . LYS A 1 212 ? 18.054  -11.981 -46.507 1.00 50.19 ? 212  LYS A O   1 
ATOM   272  C  CB  . LYS A 1 212 ? 17.525  -10.038 -48.558 1.00 53.84 ? 212  LYS A CB  1 
ATOM   273  C  CG  . LYS A 1 212 ? 16.234  -9.697  -47.828 1.00 57.41 ? 212  LYS A CG  1 
ATOM   274  C  CD  . LYS A 1 212 ? 14.997  -9.916  -48.686 1.00 59.64 ? 212  LYS A CD  1 
ATOM   275  C  CE  . LYS A 1 212 ? 13.730  -9.780  -47.847 1.00 59.90 ? 212  LYS A CE  1 
ATOM   276  N  NZ  . LYS A 1 212 ? 12.491  -10.020 -48.634 1.00 60.45 ? 212  LYS A NZ  1 
ATOM   277  N  N   . ALA A 1 213 ? 20.267  -11.783 -46.916 1.00 50.18 ? 213  ALA A N   1 
ATOM   278  C  CA  . ALA A 1 213 ? 20.621  -13.094 -46.347 1.00 49.21 ? 213  ALA A CA  1 
ATOM   279  C  C   . ALA A 1 213 ? 20.685  -13.071 -44.812 1.00 47.56 ? 213  ALA A C   1 
ATOM   280  O  O   . ALA A 1 213 ? 21.409  -12.273 -44.223 1.00 47.11 ? 213  ALA A O   1 
ATOM   281  C  CB  . ALA A 1 213 ? 21.945  -13.577 -46.922 1.00 47.56 ? 213  ALA A CB  1 
ATOM   282  N  N   . ALA A 1 214 ? 19.931  -13.967 -44.179 1.00 48.91 ? 214  ALA A N   1 
ATOM   283  C  CA  . ALA A 1 214 ? 19.895  -14.078 -42.720 1.00 47.84 ? 214  ALA A CA  1 
ATOM   284  C  C   . ALA A 1 214 ? 21.163  -14.758 -42.205 1.00 46.36 ? 214  ALA A C   1 
ATOM   285  O  O   . ALA A 1 214 ? 21.633  -15.724 -42.795 1.00 46.66 ? 214  ALA A O   1 
ATOM   286  C  CB  . ALA A 1 214 ? 18.660  -14.851 -42.281 1.00 48.13 ? 214  ALA A CB  1 
ATOM   287  N  N   . LYS A 1 215 ? 21.703  -14.242 -41.102 1.00 45.96 ? 215  LYS A N   1 
ATOM   288  C  CA  . LYS A 1 215 ? 22.991  -14.696 -40.552 1.00 46.57 ? 215  LYS A CA  1 
ATOM   289  C  C   . LYS A 1 215 ? 22.872  -15.377 -39.183 1.00 44.83 ? 215  LYS A C   1 
ATOM   290  O  O   . LYS A 1 215 ? 23.562  -16.356 -38.929 1.00 46.67 ? 215  LYS A O   1 
ATOM   291  C  CB  . LYS A 1 215 ? 23.953  -13.506 -40.425 1.00 46.94 ? 215  LYS A CB  1 
ATOM   292  C  CG  . LYS A 1 215 ? 24.466  -12.957 -41.748 1.00 48.01 ? 215  LYS A CG  1 
ATOM   293  C  CD  . LYS A 1 215 ? 25.010  -11.548 -41.584 1.00 48.16 ? 215  LYS A CD  1 
ATOM   294  C  CE  . LYS A 1 215 ? 25.905  -11.157 -42.748 1.00 50.08 ? 215  LYS A CE  1 
ATOM   295  N  NZ  . LYS A 1 215 ? 26.597  -9.871  -42.480 1.00 52.32 ? 215  LYS A NZ  1 
ATOM   296  N  N   . SER A 1 216 ? 22.026  -14.837 -38.301 1.00 42.20 ? 216  SER A N   1 
ATOM   297  C  CA  . SER A 1 216 ? 21.850  -15.358 -36.935 1.00 41.22 ? 216  SER A CA  1 
ATOM   298  C  C   . SER A 1 216 ? 20.344  -15.540 -36.624 1.00 40.81 ? 216  SER A C   1 
ATOM   299  O  O   . SER A 1 216 ? 19.773  -14.863 -35.745 1.00 39.99 ? 216  SER A O   1 
ATOM   300  C  CB  . SER A 1 216 ? 22.576  -14.448 -35.902 1.00 39.04 ? 216  SER A CB  1 
ATOM   301  O  OG  . SER A 1 216 ? 22.399  -13.050 -36.170 1.00 36.73 ? 216  SER A OG  1 
ATOM   302  N  N   . GLY A 1 217 ? 19.718  -16.450 -37.381 1.00 38.29 ? 217  GLY A N   1 
ATOM   303  C  CA  . GLY A 1 217 ? 18.278  -16.779 -37.265 1.00 35.41 ? 217  GLY A CA  1 
ATOM   304  C  C   . GLY A 1 217 ? 17.299  -15.656 -37.602 1.00 31.64 ? 217  GLY A C   1 
ATOM   305  O  O   . GLY A 1 217 ? 17.614  -14.730 -38.359 1.00 33.50 ? 217  GLY A O   1 
ATOM   306  N  N   . THR A 1 218 ? 16.115  -15.741 -37.008 1.00 26.13 ? 218  THR A N   1 
ATOM   307  C  CA  . THR A 1 218 ? 15.076  -14.717 -37.126 1.00 21.81 ? 218  THR A CA  1 
ATOM   308  C  C   . THR A 1 218 ? 15.460  -13.524 -36.281 1.00 20.20 ? 218  THR A C   1 
ATOM   309  O  O   . THR A 1 218 ? 15.871  -13.675 -35.138 1.00 19.38 ? 218  THR A O   1 
ATOM   310  C  CB  . THR A 1 218 ? 13.741  -15.260 -36.601 1.00 21.43 ? 218  THR A CB  1 
ATOM   311  O  OG1 . THR A 1 218 ? 13.346  -16.380 -37.390 1.00 20.87 ? 218  THR A OG1 1 
ATOM   312  C  CG2 . THR A 1 218 ? 12.629  -14.188 -36.589 1.00 21.16 ? 218  THR A CG2 1 
ATOM   313  N  N   . GLN A 1 219 ? 15.319  -12.334 -36.833 1.00 18.57 ? 219  GLN A N   1 
ATOM   314  C  CA  . GLN A 1 219 ? 15.728  -11.135 -36.138 1.00 18.57 ? 219  GLN A CA  1 
ATOM   315  C  C   . GLN A 1 219 ? 14.547  -10.366 -35.593 1.00 18.49 ? 219  GLN A C   1 
ATOM   316  O  O   . GLN A 1 219 ? 13.515  -10.275 -36.256 1.00 18.14 ? 219  GLN A O   1 
ATOM   317  C  CB  . GLN A 1 219 ? 16.525  -10.226 -37.080 1.00 18.99 ? 219  GLN A CB  1 
ATOM   318  C  CG  . GLN A 1 219 ? 17.879  -10.786 -37.468 1.00 18.28 ? 219  GLN A CG  1 
ATOM   319  C  CD  . GLN A 1 219 ? 18.696  -9.827  -38.314 1.00 18.67 ? 219  GLN A CD  1 
ATOM   320  O  OE1 . GLN A 1 219 ? 18.587  -8.606  -38.193 1.00 20.34 ? 219  GLN A OE1 1 
ATOM   321  N  NE2 . GLN A 1 219 ? 19.509  -10.371 -39.173 1.00 18.70 ? 219  GLN A NE2 1 
ATOM   322  N  N   . MET A 1 220 ? 14.695  -9.804  -34.385 1.00 18.10 ? 220  MET A N   1 
ATOM   323  C  CA  . MET A 1 220 ? 13.828  -8.710  -33.965 1.00 17.39 ? 220  MET A CA  1 
ATOM   324  C  C   . MET A 1 220 ? 14.363  -7.465  -34.664 1.00 17.32 ? 220  MET A C   1 
ATOM   325  O  O   . MET A 1 220 ? 15.447  -6.998  -34.342 1.00 17.61 ? 220  MET A O   1 
ATOM   326  C  CB  . MET A 1 220 ? 13.849  -8.530  -32.441 1.00 17.60 ? 220  MET A CB  1 
ATOM   327  C  CG  . MET A 1 220 ? 13.053  -7.326  -31.936 1.00 17.67 ? 220  MET A CG  1 
ATOM   328  S  SD  . MET A 1 220 ? 13.289  -6.991  -30.175 1.00 19.14 ? 220  MET A SD  1 
ATOM   329  C  CE  . MET A 1 220 ? 12.482  -8.438  -29.490 1.00 18.62 ? 220  MET A CE  1 
ATOM   330  N  N   . THR A 1 221 ? 13.613  -6.944  -35.628 1.00 17.75 ? 221  THR A N   1 
ATOM   331  C  CA  . THR A 1 221 ? 14.076  -5.843  -36.473 1.00 18.30 ? 221  THR A CA  1 
ATOM   332  C  C   . THR A 1 221 ? 13.804  -4.525  -35.779 1.00 17.29 ? 221  THR A C   1 
ATOM   333  O  O   . THR A 1 221 ? 13.074  -4.483  -34.799 1.00 17.96 ? 221  THR A O   1 
ATOM   334  C  CB  . THR A 1 221 ? 13.360  -5.802  -37.837 1.00 18.49 ? 221  THR A CB  1 
ATOM   335  O  OG1 . THR A 1 221 ? 11.950  -5.671  -37.618 1.00 18.97 ? 221  THR A OG1 1 
ATOM   336  C  CG2 . THR A 1 221 ? 13.638  -7.075  -38.673 1.00 19.49 ? 221  THR A CG2 1 
ATOM   337  N  N   . TYR A 1 222 ? 14.379  -3.439  -36.297 1.00 17.07 ? 222  TYR A N   1 
ATOM   338  C  CA  . TYR A 1 222 ? 14.144  -2.116  -35.728 1.00 16.51 ? 222  TYR A CA  1 
ATOM   339  C  C   . TYR A 1 222 ? 12.637  -1.823  -35.804 1.00 16.18 ? 222  TYR A C   1 
ATOM   340  O  O   . TYR A 1 222 ? 12.070  -1.243  -34.888 1.00 15.43 ? 222  TYR A O   1 
ATOM   341  C  CB  . TYR A 1 222 ? 14.966  -1.045  -36.467 1.00 16.70 ? 222  TYR A CB  1 
ATOM   342  C  CG  . TYR A 1 222 ? 15.136  0.269   -35.716 1.00 16.38 ? 222  TYR A CG  1 
ATOM   343  C  CD1 . TYR A 1 222 ? 16.074  0.381   -34.690 1.00 16.18 ? 222  TYR A CD1 1 
ATOM   344  C  CD2 . TYR A 1 222 ? 14.380  1.384   -36.035 1.00 16.63 ? 222  TYR A CD2 1 
ATOM   345  C  CE1 . TYR A 1 222 ? 16.269  1.557   -34.018 1.00 16.43 ? 222  TYR A CE1 1 
ATOM   346  C  CE2 . TYR A 1 222 ? 14.552  2.592   -35.346 1.00 16.99 ? 222  TYR A CE2 1 
ATOM   347  C  CZ  . TYR A 1 222 ? 15.507  2.673   -34.336 1.00 16.39 ? 222  TYR A CZ  1 
ATOM   348  O  OH  . TYR A 1 222 ? 15.719  3.830   -33.610 1.00 15.67 ? 222  TYR A OH  1 
ATOM   349  N  N   . ASN A 1 223 ? 12.000  -2.256  -36.890 1.00 16.68 ? 223  ASN A N   1 
ATOM   350  C  CA  . ASN A 1 223 ? 10.543  -2.106  -37.069 1.00 17.20 ? 223  ASN A CA  1 
ATOM   351  C  C   . ASN A 1 223 ? 9.678   -2.912  -36.069 1.00 17.32 ? 223  ASN A C   1 
ATOM   352  O  O   . ASN A 1 223 ? 8.689   -2.384  -35.514 1.00 17.48 ? 223  ASN A O   1 
ATOM   353  C  CB  . ASN A 1 223 ? 10.138  -2.471  -38.508 1.00 17.58 ? 223  ASN A CB  1 
ATOM   354  C  CG  . ASN A 1 223 ? 8.699   -2.080  -38.825 1.00 18.12 ? 223  ASN A CG  1 
ATOM   355  O  OD1 . ASN A 1 223 ? 7.862   -2.926  -39.091 1.00 19.57 ? 223  ASN A OD1 1 
ATOM   356  N  ND2 . ASN A 1 223 ? 8.415   -0.802  -38.790 1.00 18.07 ? 223  ASN A ND2 1 
ATOM   357  N  N   . ASP A 1 224 ? 10.039  -4.178  -35.853 1.00 16.58 ? 224  ASP A N   1 
ATOM   358  C  CA  . ASP A 1 224 ? 9.411   -5.003  -34.817 1.00 16.21 ? 224  ASP A CA  1 
ATOM   359  C  C   . ASP A 1 224 ? 9.431   -4.309  -33.447 1.00 15.87 ? 224  ASP A C   1 
ATOM   360  O  O   . ASP A 1 224 ? 8.418   -4.268  -32.753 1.00 15.94 ? 224  ASP A O   1 
ATOM   361  C  CB  . ASP A 1 224 ? 10.137  -6.337  -34.669 1.00 16.90 ? 224  ASP A CB  1 
ATOM   362  C  CG  . ASP A 1 224 ? 9.977   -7.249  -35.878 1.00 17.84 ? 224  ASP A CG  1 
ATOM   363  O  OD1 . ASP A 1 224 ? 8.986   -7.136  -36.620 1.00 17.47 ? 224  ASP A OD1 1 
ATOM   364  O  OD2 . ASP A 1 224 ? 10.858  -8.120  -36.054 1.00 19.64 ? 224  ASP A OD2 1 
ATOM   365  N  N   . PHE A 1 225 ? 10.601  -3.801  -33.062 1.00 15.39 ? 225  PHE A N   1 
ATOM   366  C  CA  . PHE A 1 225 ? 10.820  -3.224  -31.737 1.00 15.23 ? 225  PHE A CA  1 
ATOM   367  C  C   . PHE A 1 225 ? 9.946   -1.997  -31.594 1.00 15.51 ? 225  PHE A C   1 
ATOM   368  O  O   . PHE A 1 225 ? 9.319   -1.796  -30.561 1.00 14.36 ? 225  PHE A O   1 
ATOM   369  C  CB  . PHE A 1 225 ? 12.306  -2.863  -31.540 1.00 14.36 ? 225  PHE A CB  1 
ATOM   370  C  CG  . PHE A 1 225 ? 12.617  -2.250  -30.204 1.00 14.24 ? 225  PHE A CG  1 
ATOM   371  C  CD1 . PHE A 1 225 ? 12.371  -0.900  -29.965 1.00 13.79 ? 225  PHE A CD1 1 
ATOM   372  C  CD2 . PHE A 1 225 ? 13.159  -3.008  -29.190 1.00 13.65 ? 225  PHE A CD2 1 
ATOM   373  C  CE1 . PHE A 1 225 ? 12.657  -0.333  -28.745 1.00 13.81 ? 225  PHE A CE1 1 
ATOM   374  C  CE2 . PHE A 1 225 ? 13.464  -2.442  -27.974 1.00 13.70 ? 225  PHE A CE2 1 
ATOM   375  C  CZ  . PHE A 1 225 ? 13.198  -1.098  -27.742 1.00 13.39 ? 225  PHE A CZ  1 
ATOM   376  N  N   . GLN A 1 226 ? 9.910   -1.193  -32.650 1.00 16.96 ? 226  GLN A N   1 
ATOM   377  C  CA  . GLN A 1 226 ? 9.060   -0.017  -32.685 1.00 18.91 ? 226  GLN A CA  1 
ATOM   378  C  C   . GLN A 1 226 ? 7.598   -0.424  -32.519 1.00 17.95 ? 226  GLN A C   1 
ATOM   379  O  O   . GLN A 1 226 ? 6.886   0.161   -31.715 1.00 18.12 ? 226  GLN A O   1 
ATOM   380  C  CB  . GLN A 1 226 ? 9.234   0.744   -33.990 1.00 21.37 ? 226  GLN A CB  1 
ATOM   381  C  CG  . GLN A 1 226 ? 8.250   1.883   -34.175 1.00 23.51 ? 226  GLN A CG  1 
ATOM   382  C  CD  . GLN A 1 226 ? 8.741   3.143   -33.518 1.00 27.51 ? 226  GLN A CD  1 
ATOM   383  O  OE1 . GLN A 1 226 ? 9.799   3.654   -33.882 1.00 32.40 ? 226  GLN A OE1 1 
ATOM   384  N  NE2 . GLN A 1 226 ? 7.993   3.648   -32.534 1.00 29.80 ? 226  GLN A NE2 1 
ATOM   385  N  N   . LYS A 1 227 ? 7.158   -1.431  -33.258 1.00 17.37 ? 227  LYS A N   1 
ATOM   386  C  CA  . LYS A 1 227 ? 5.780   -1.944  -33.108 1.00 17.72 ? 227  LYS A CA  1 
ATOM   387  C  C   . LYS A 1 227 ? 5.459   -2.493  -31.703 1.00 17.48 ? 227  LYS A C   1 
ATOM   388  O  O   . LYS A 1 227 ? 4.341   -2.322  -31.208 1.00 17.23 ? 227  LYS A O   1 
ATOM   389  C  CB  . LYS A 1 227 ? 5.497   -3.040  -34.120 1.00 17.61 ? 227  LYS A CB  1 
ATOM   390  C  CG  . LYS A 1 227 ? 5.419   -2.548  -35.549 1.00 18.30 ? 227  LYS A CG  1 
ATOM   391  C  CD  . LYS A 1 227 ? 5.194   -3.733  -36.462 1.00 18.42 ? 227  LYS A CD  1 
ATOM   392  C  CE  . LYS A 1 227 ? 4.803   -3.297  -37.849 1.00 19.24 ? 227  LYS A CE  1 
ATOM   393  N  NZ  . LYS A 1 227 ? 4.819   -4.508  -38.715 1.00 20.99 ? 227  LYS A NZ  1 
ATOM   394  N  N   . ILE A 1 228 ? 6.425   -3.161  -31.080 1.00 17.13 ? 228  ILE A N   1 
ATOM   395  C  CA  . ILE A 1 228 ? 6.215   -3.691  -29.733 1.00 17.25 ? 228  ILE A CA  1 
ATOM   396  C  C   . ILE A 1 228 ? 5.953   -2.503  -28.811 1.00 17.21 ? 228  ILE A C   1 
ATOM   397  O  O   . ILE A 1 228 ? 5.008   -2.515  -28.035 1.00 17.43 ? 228  ILE A O   1 
ATOM   398  C  CB  . ILE A 1 228 ? 7.413   -4.531  -29.256 1.00 16.78 ? 228  ILE A CB  1 
ATOM   399  C  CG1 . ILE A 1 228 ? 7.514   -5.820  -30.069 1.00 17.39 ? 228  ILE A CG1 1 
ATOM   400  C  CG2 . ILE A 1 228 ? 7.298   -4.881  -27.778 1.00 16.88 ? 228  ILE A CG2 1 
ATOM   401  C  CD1 . ILE A 1 228 ? 8.896   -6.453  -30.053 1.00 17.48 ? 228  ILE A CD1 1 
ATOM   402  N  N   . ALA A 1 229 ? 6.766   -1.462  -28.953 1.00 17.91 ? 229  ALA A N   1 
ATOM   403  C  CA  . ALA A 1 229 ? 6.641   -0.262  -28.135 1.00 18.20 ? 229  ALA A CA  1 
ATOM   404  C  C   . ALA A 1 229 ? 5.319   0.445   -28.392 1.00 18.58 ? 229  ALA A C   1 
ATOM   405  O  O   . ALA A 1 229 ? 4.642   0.838   -27.437 1.00 18.61 ? 229  ALA A O   1 
ATOM   406  C  CB  . ALA A 1 229 ? 7.822   0.675   -28.374 1.00 18.09 ? 229  ALA A CB  1 
ATOM   407  N  N   . ASP A 1 230 ? 4.947   0.601   -29.667 1.00 18.80 ? 230  ASP A N   1 
ATOM   408  C  CA  . ASP A 1 230 ? 3.664   1.209   -30.021 1.00 19.87 ? 230  ASP A CA  1 
ATOM   409  C  C   . ASP A 1 230 ? 2.523   0.421   -29.385 1.00 19.41 ? 230  ASP A C   1 
ATOM   410  O  O   . ASP A 1 230 ? 1.571   0.999   -28.867 1.00 18.31 ? 230  ASP A O   1 
ATOM   411  C  CB  . ASP A 1 230 ? 3.446   1.239   -31.537 1.00 21.54 ? 230  ASP A CB  1 
ATOM   412  C  CG  . ASP A 1 230 ? 4.369   2.222   -32.254 1.00 22.89 ? 230  ASP A CG  1 
ATOM   413  O  OD1 . ASP A 1 230 ? 4.977   3.087   -31.593 1.00 25.00 ? 230  ASP A OD1 1 
ATOM   414  O  OD2 . ASP A 1 230 ? 4.489   2.111   -33.492 1.00 25.43 ? 230  ASP A OD2 1 
ATOM   415  N  N   . THR A 1 231 ? 2.618   -0.904  -29.419 1.00 19.05 ? 231  THR A N   1 
ATOM   416  C  CA  . THR A 1 231 ? 1.569   -1.723  -28.827 1.00 19.05 ? 231  THR A CA  1 
ATOM   417  C  C   . THR A 1 231 ? 1.488   -1.467  -27.315 1.00 18.68 ? 231  THR A C   1 
ATOM   418  O  O   . THR A 1 231 ? 0.391   -1.263  -26.756 1.00 18.48 ? 231  THR A O   1 
ATOM   419  C  CB  . THR A 1 231 ? 1.776   -3.208  -29.163 1.00 19.11 ? 231  THR A CB  1 
ATOM   420  O  OG1 . THR A 1 231 ? 1.637   -3.386  -30.586 1.00 18.85 ? 231  THR A OG1 1 
ATOM   421  C  CG2 . THR A 1 231 ? 0.745   -4.074  -28.442 1.00 19.25 ? 231  THR A CG2 1 
ATOM   422  N  N   . LEU A 1 232 ? 2.643   -1.420  -26.659 1.00 18.25 ? 232  LEU A N   1 
ATOM   423  C  CA  . LEU A 1 232 ? 2.675   -1.119  -25.230 1.00 18.94 ? 232  LEU A CA  1 
ATOM   424  C  C   . LEU A 1 232 ? 2.016   0.236   -24.964 1.00 20.09 ? 232  LEU A C   1 
ATOM   425  O  O   . LEU A 1 232 ? 1.198   0.362   -24.062 1.00 19.77 ? 232  LEU A O   1 
ATOM   426  C  CB  . LEU A 1 232 ? 4.107   -1.170  -24.690 1.00 19.31 ? 232  LEU A CB  1 
ATOM   427  C  CG  . LEU A 1 232 ? 4.384   -0.832  -23.212 1.00 19.28 ? 232  LEU A CG  1 
ATOM   428  C  CD1 . LEU A 1 232 ? 5.731   -1.410  -22.825 1.00 19.27 ? 232  LEU A CD1 1 
ATOM   429  C  CD2 . LEU A 1 232 ? 4.352   0.671   -22.930 1.00 19.34 ? 232  LEU A CD2 1 
ATOM   430  N  N   . ILE A 1 233 ? 2.340   1.235   -25.781 1.00 20.77 ? 233  ILE A N   1 
ATOM   431  C  CA  . ILE A 1 233 ? 1.753   2.564   -25.620 1.00 21.94 ? 233  ILE A CA  1 
ATOM   432  C  C   . ILE A 1 233 ? 0.228   2.538   -25.805 1.00 22.52 ? 233  ILE A C   1 
ATOM   433  O  O   . ILE A 1 233 ? -0.480  3.197   -25.069 1.00 24.21 ? 233  ILE A O   1 
ATOM   434  C  CB  . ILE A 1 233 ? 2.454   3.587   -26.548 1.00 21.68 ? 233  ILE A CB  1 
ATOM   435  C  CG1 . ILE A 1 233 ? 3.903   3.790   -26.050 1.00 21.53 ? 233  ILE A CG1 1 
ATOM   436  C  CG2 . ILE A 1 233 ? 1.692   4.919   -26.603 1.00 20.97 ? 233  ILE A CG2 1 
ATOM   437  C  CD1 . ILE A 1 233 ? 4.833   4.376   -27.095 1.00 22.41 ? 233  ILE A CD1 1 
ATOM   438  N  N   . LYS A 1 234 ? -0.269  1.751   -26.750 1.00 23.47 ? 234  LYS A N   1 
ATOM   439  C  CA  . LYS A 1 234 ? -1.705  1.629   -26.975 1.00 25.96 ? 234  LYS A CA  1 
ATOM   440  C  C   . LYS A 1 234 ? -2.451  0.977   -25.819 1.00 25.11 ? 234  LYS A C   1 
ATOM   441  O  O   . LYS A 1 234 ? -3.654  1.173   -25.696 1.00 23.81 ? 234  LYS A O   1 
ATOM   442  C  CB  . LYS A 1 234 ? -1.993  0.850   -28.261 1.00 28.27 ? 234  LYS A CB  1 
ATOM   443  C  CG  . LYS A 1 234 ? -1.653  1.644   -29.513 1.00 32.15 ? 234  LYS A CG  1 
ATOM   444  C  CD  . LYS A 1 234 ? -1.662  0.775   -30.763 1.00 34.79 ? 234  LYS A CD  1 
ATOM   445  C  CE  . LYS A 1 234 ? -1.026  1.512   -31.933 1.00 37.99 ? 234  LYS A CE  1 
ATOM   446  N  NZ  . LYS A 1 234 ? -0.902  0.616   -33.115 1.00 40.53 ? 234  LYS A NZ  1 
ATOM   447  N  N   . GLN A 1 235 ? -1.748  0.203   -24.986 1.00 24.77 ? 235  GLN A N   1 
ATOM   448  C  CA  . GLN A 1 235 ? -2.361  -0.447  -23.831 1.00 25.55 ? 235  GLN A CA  1 
ATOM   449  C  C   . GLN A 1 235 ? -3.629  -1.191  -24.254 1.00 26.11 ? 235  GLN A C   1 
ATOM   450  O  O   . GLN A 1 235 ? -4.708  -0.972  -23.719 1.00 26.22 ? 235  GLN A O   1 
ATOM   451  C  CB  . GLN A 1 235 ? -2.642  0.579   -22.728 1.00 26.14 ? 235  GLN A CB  1 
ATOM   452  C  CG  . GLN A 1 235 ? -1.363  1.185   -22.162 1.00 27.26 ? 235  GLN A CG  1 
ATOM   453  C  CD  . GLN A 1 235 ? -1.567  2.552   -21.521 1.00 28.09 ? 235  GLN A CD  1 
ATOM   454  O  OE1 . GLN A 1 235 ? -1.974  2.656   -20.359 1.00 28.40 ? 235  GLN A OE1 1 
ATOM   455  N  NE2 . GLN A 1 235 ? -1.247  3.614   -22.270 1.00 27.60 ? 235  GLN A NE2 1 
ATOM   456  N  N   . ASP A 1 236 ? -3.462  -2.050  -25.253 1.00 25.98 ? 236  ASP A N   1 
ATOM   457  C  CA  . ASP A 1 236 ? -4.518  -2.895  -25.784 1.00 26.90 ? 236  ASP A CA  1 
ATOM   458  C  C   . ASP A 1 236 ? -4.704  -4.146  -24.905 1.00 25.90 ? 236  ASP A C   1 
ATOM   459  O  O   . ASP A 1 236 ? -3.772  -4.942  -24.757 1.00 24.56 ? 236  ASP A O   1 
ATOM   460  C  CB  . ASP A 1 236 ? -4.136  -3.313  -27.209 1.00 27.79 ? 236  ASP A CB  1 
ATOM   461  C  CG  . ASP A 1 236 ? -5.165  -4.214  -27.855 1.00 29.71 ? 236  ASP A CG  1 
ATOM   462  O  OD1 . ASP A 1 236 ? -5.892  -4.935  -27.136 1.00 30.16 ? 236  ASP A OD1 1 
ATOM   463  O  OD2 . ASP A 1 236 ? -5.249  -4.202  -29.097 1.00 31.20 ? 236  ASP A OD2 1 
ATOM   464  N  N   . GLY A 1 237 ? -5.916  -4.315  -24.364 1.00 25.28 ? 237  GLY A N   1 
ATOM   465  C  CA  . GLY A 1 237 ? -6.281  -5.435  -23.487 1.00 25.05 ? 237  GLY A CA  1 
ATOM   466  C  C   . GLY A 1 237 ? -5.897  -6.842  -23.943 1.00 25.48 ? 237  GLY A C   1 
ATOM   467  O  O   . GLY A 1 237 ? -5.749  -7.738  -23.099 1.00 26.02 ? 237  GLY A O   1 
ATOM   468  N  N   . ARG A 1 238 ? -5.731  -7.051  -25.249 1.00 25.05 ? 238  ARG A N   1 
ATOM   469  C  CA  . ARG A 1 238 ? -5.263  -8.339  -25.760 1.00 26.97 ? 238  ARG A CA  1 
ATOM   470  C  C   . ARG A 1 238 ? -3.848  -8.679  -25.309 1.00 25.54 ? 238  ARG A C   1 
ATOM   471  O  O   . ARG A 1 238 ? -3.493  -9.856  -25.277 1.00 23.83 ? 238  ARG A O   1 
ATOM   472  C  CB  . ARG A 1 238 ? -5.270  -8.383  -27.287 1.00 30.54 ? 238  ARG A CB  1 
ATOM   473  C  CG  . ARG A 1 238 ? -6.641  -8.608  -27.913 1.00 34.34 ? 238  ARG A CG  1 
ATOM   474  C  CD  . ARG A 1 238 ? -6.609  -8.467  -29.429 1.00 37.24 ? 238  ARG A CD  1 
ATOM   475  N  NE  . ARG A 1 238 ? -6.235  -7.107  -29.831 1.00 41.86 ? 238  ARG A NE  1 
ATOM   476  C  CZ  . ARG A 1 238 ? -6.455  -6.568  -31.032 1.00 44.02 ? 238  ARG A CZ  1 
ATOM   477  N  NH1 . ARG A 1 238 ? -7.079  -7.242  -31.996 1.00 43.39 ? 238  ARG A NH1 1 
ATOM   478  N  NH2 . ARG A 1 238 ? -6.056  -5.322  -31.262 1.00 45.59 ? 238  ARG A NH2 1 
ATOM   479  N  N   . TYR A 1 239 ? -3.043  -7.653  -25.017 1.00 22.62 ? 239  TYR A N   1 
ATOM   480  C  CA  . TYR A 1 239 ? -1.633  -7.839  -24.694 1.00 21.41 ? 239  TYR A CA  1 
ATOM   481  C  C   . TYR A 1 239 ? -1.216  -7.290  -23.327 1.00 20.85 ? 239  TYR A C   1 
ATOM   482  O  O   . TYR A 1 239 ? -0.177  -7.681  -22.822 1.00 20.93 ? 239  TYR A O   1 
ATOM   483  C  CB  . TYR A 1 239 ? -0.748  -7.191  -25.763 1.00 21.20 ? 239  TYR A CB  1 
ATOM   484  C  CG  . TYR A 1 239 ? -1.220  -7.400  -27.174 1.00 20.98 ? 239  TYR A CG  1 
ATOM   485  C  CD1 . TYR A 1 239 ? -1.075  -8.628  -27.806 1.00 21.13 ? 239  TYR A CD1 1 
ATOM   486  C  CD2 . TYR A 1 239 ? -1.821  -6.365  -27.884 1.00 21.36 ? 239  TYR A CD2 1 
ATOM   487  C  CE1 . TYR A 1 239 ? -1.529  -8.823  -29.108 1.00 21.03 ? 239  TYR A CE1 1 
ATOM   488  C  CE2 . TYR A 1 239 ? -2.259  -6.542  -29.189 1.00 20.84 ? 239  TYR A CE2 1 
ATOM   489  C  CZ  . TYR A 1 239 ? -2.115  -7.774  -29.794 1.00 21.01 ? 239  TYR A CZ  1 
ATOM   490  O  OH  . TYR A 1 239 ? -2.564  -7.953  -31.082 1.00 20.69 ? 239  TYR A OH  1 
ATOM   491  N  N   . THR A 1 240 ? -1.989  -6.388  -22.733 1.00 20.44 ? 240  THR A N   1 
ATOM   492  C  CA  . THR A 1 240 ? -1.577  -5.790  -21.461 1.00 21.08 ? 240  THR A CA  1 
ATOM   493  C  C   . THR A 1 240 ? -1.591  -6.828  -20.354 1.00 20.10 ? 240  THR A C   1 
ATOM   494  O  O   . THR A 1 240 ? -2.517  -7.631  -20.259 1.00 20.30 ? 240  THR A O   1 
ATOM   495  C  CB  . THR A 1 240 ? -2.481  -4.609  -21.014 1.00 21.84 ? 240  THR A CB  1 
ATOM   496  O  OG1 . THR A 1 240 ? -3.865  -4.987  -21.105 1.00 21.79 ? 240  THR A OG1 1 
ATOM   497  C  CG2 . THR A 1 240 ? -2.210  -3.373  -21.868 1.00 21.83 ? 240  THR A CG2 1 
ATOM   498  N  N   . VAL A 1 241 ? -0.540  -6.821  -19.540 1.00 19.75 ? 241  VAL A N   1 
ATOM   499  C  CA  . VAL A 1 241 ? -0.529  -7.580  -18.303 1.00 19.97 ? 241  VAL A CA  1 
ATOM   500  C  C   . VAL A 1 241 ? -1.754  -7.095  -17.520 1.00 19.81 ? 241  VAL A C   1 
ATOM   501  O  O   . VAL A 1 241 ? -2.009  -5.893  -17.445 1.00 18.72 ? 241  VAL A O   1 
ATOM   502  C  CB  . VAL A 1 241 ? 0.761   -7.344  -17.491 1.00 19.74 ? 241  VAL A CB  1 
ATOM   503  C  CG1 . VAL A 1 241 ? 0.679   -8.019  -16.126 1.00 19.92 ? 241  VAL A CG1 1 
ATOM   504  C  CG2 . VAL A 1 241 ? 1.982   -7.832  -18.261 1.00 20.05 ? 241  VAL A CG2 1 
ATOM   505  N  N   . PRO A 1 242 ? -2.537  -8.026  -16.980 1.00 20.80 ? 242  PRO A N   1 
ATOM   506  C  CA  . PRO A 1 242 ? -3.759  -7.591  -16.328 1.00 22.19 ? 242  PRO A CA  1 
ATOM   507  C  C   . PRO A 1 242 ? -3.471  -6.712  -15.107 1.00 22.17 ? 242  PRO A C   1 
ATOM   508  O  O   . PRO A 1 242 ? -2.399  -6.820  -14.504 1.00 22.80 ? 242  PRO A O   1 
ATOM   509  C  CB  . PRO A 1 242 ? -4.439  -8.902  -15.894 1.00 21.60 ? 242  PRO A CB  1 
ATOM   510  C  CG  . PRO A 1 242 ? -3.721  -9.999  -16.567 1.00 21.93 ? 242  PRO A CG  1 
ATOM   511  C  CD  . PRO A 1 242 ? -2.419  -9.492  -17.078 1.00 21.58 ? 242  PRO A CD  1 
ATOM   512  N  N   . PHE A 1 243 ? -4.409  -5.827  -14.781 1.00 22.75 ? 243  PHE A N   1 
ATOM   513  C  CA  . PHE A 1 243 ? -4.353  -5.081  -13.519 1.00 23.85 ? 243  PHE A CA  1 
ATOM   514  C  C   . PHE A 1 243 ? -4.525  -6.055  -12.340 1.00 23.80 ? 243  PHE A C   1 
ATOM   515  O  O   . PHE A 1 243 ? -5.399  -6.927  -12.376 1.00 25.63 ? 243  PHE A O   1 
ATOM   516  C  CB  . PHE A 1 243 ? -5.426  -3.987  -13.477 1.00 23.41 ? 243  PHE A CB  1 
ATOM   517  C  CG  . PHE A 1 243 ? -5.188  -2.862  -14.459 1.00 23.84 ? 243  PHE A CG  1 
ATOM   518  C  CD1 . PHE A 1 243 ? -4.002  -2.122  -14.422 1.00 23.57 ? 243  PHE A CD1 1 
ATOM   519  C  CD2 . PHE A 1 243 ? -6.146  -2.536  -15.420 1.00 23.41 ? 243  PHE A CD2 1 
ATOM   520  C  CE1 . PHE A 1 243 ? -3.767  -1.093  -15.340 1.00 23.18 ? 243  PHE A CE1 1 
ATOM   521  C  CE2 . PHE A 1 243 ? -5.923  -1.496  -16.323 1.00 23.37 ? 243  PHE A CE2 1 
ATOM   522  C  CZ  . PHE A 1 243 ? -4.729  -0.783  -16.284 1.00 22.78 ? 243  PHE A CZ  1 
ATOM   523  N  N   . PHE A 1 244 ? -3.670  -5.914  -11.329 1.00 24.12 ? 244  PHE A N   1 
ATOM   524  C  CA  . PHE A 1 244 ? -3.730  -6.715  -10.099 1.00 24.28 ? 244  PHE A CA  1 
ATOM   525  C  C   . PHE A 1 244 ? -4.250  -5.818  -8.965  1.00 24.84 ? 244  PHE A C   1 
ATOM   526  O  O   . PHE A 1 244 ? -3.848  -4.650  -8.843  1.00 24.08 ? 244  PHE A O   1 
ATOM   527  C  CB  . PHE A 1 244 ? -2.338  -7.257  -9.735  1.00 24.02 ? 244  PHE A CB  1 
ATOM   528  C  CG  . PHE A 1 244 ? -1.674  -8.071  -10.830 1.00 24.26 ? 244  PHE A CG  1 
ATOM   529  C  CD1 . PHE A 1 244 ? -2.076  -9.376  -11.094 1.00 23.78 ? 244  PHE A CD1 1 
ATOM   530  C  CD2 . PHE A 1 244 ? -0.636  -7.531  -11.593 1.00 24.18 ? 244  PHE A CD2 1 
ATOM   531  C  CE1 . PHE A 1 244 ? -1.479  -10.130 -12.088 1.00 23.69 ? 244  PHE A CE1 1 
ATOM   532  C  CE2 . PHE A 1 244 ? -0.025  -8.285  -12.591 1.00 24.30 ? 244  PHE A CE2 1 
ATOM   533  C  CZ  . PHE A 1 244 ? -0.446  -9.586  -12.835 1.00 23.96 ? 244  PHE A CZ  1 
ATOM   534  N  N   . LYS A 1 245 ? -5.150  -6.353  -8.142  1.00 27.30 ? 245  LYS A N   1 
ATOM   535  C  CA  . LYS A 1 245 ? -5.688  -5.612  -6.975  1.00 27.80 ? 245  LYS A CA  1 
ATOM   536  C  C   . LYS A 1 245 ? -4.594  -5.444  -5.920  1.00 25.77 ? 245  LYS A C   1 
ATOM   537  O  O   . LYS A 1 245 ? -4.224  -6.394  -5.233  1.00 23.39 ? 245  LYS A O   1 
ATOM   538  C  CB  . LYS A 1 245 ? -6.916  -6.316  -6.369  1.00 28.92 ? 245  LYS A CB  1 
ATOM   539  C  CG  . LYS A 1 245 ? -7.720  -5.425  -5.429  1.00 30.89 ? 245  LYS A CG  1 
ATOM   540  C  CD  . LYS A 1 245 ? -8.976  -6.104  -4.903  1.00 31.82 ? 245  LYS A CD  1 
ATOM   541  C  CE  . LYS A 1 245 ? -10.071 -6.176  -5.955  1.00 32.40 ? 245  LYS A CE  1 
ATOM   542  N  NZ  . LYS A 1 245 ? -10.948 -7.352  -5.717  1.00 33.92 ? 245  LYS A NZ  1 
ATOM   543  N  N   . ALA A 1 246 ? -4.085  -4.222  -5.816  1.00 25.70 ? 246  ALA A N   1 
ATOM   544  C  CA  . ALA A 1 246 ? -2.893  -3.938  -5.036  1.00 27.23 ? 246  ALA A CA  1 
ATOM   545  C  C   . ALA A 1 246 ? -3.065  -4.263  -3.557  1.00 28.88 ? 246  ALA A C   1 
ATOM   546  O  O   . ALA A 1 246 ? -2.100  -4.649  -2.894  1.00 29.33 ? 246  ALA A O   1 
ATOM   547  C  CB  . ALA A 1 246 ? -2.495  -2.488  -5.204  1.00 27.44 ? 246  ALA A CB  1 
ATOM   548  N  N   . SER A 1 247 ? -4.294  -4.121  -3.062  1.00 29.06 ? 247  SER A N   1 
ATOM   549  C  CA  . SER A 1 247 ? -4.605  -4.377  -1.658  1.00 30.41 ? 247  SER A CA  1 
ATOM   550  C  C   . SER A 1 247 ? -4.409  -5.842  -1.289  1.00 30.22 ? 247  SER A C   1 
ATOM   551  O  O   . SER A 1 247 ? -4.232  -6.160  -0.122  1.00 31.36 ? 247  SER A O   1 
ATOM   552  C  CB  . SER A 1 247 ? -6.047  -3.951  -1.342  1.00 30.18 ? 247  SER A CB  1 
ATOM   553  O  OG  . SER A 1 247 ? -6.981  -4.839  -1.938  1.00 31.18 ? 247  SER A OG  1 
ATOM   554  N  N   . GLU A 1 248 ? -4.435  -6.733  -2.272  1.00 29.69 ? 248  GLU A N   1 
ATOM   555  C  CA  . GLU A 1 248 ? -4.296  -8.164  -1.997  1.00 30.98 ? 248  GLU A CA  1 
ATOM   556  C  C   . GLU A 1 248 ? -2.861  -8.684  -1.981  1.00 30.14 ? 248  GLU A C   1 
ATOM   557  O  O   . GLU A 1 248 ? -2.627  -9.832  -1.599  1.00 28.49 ? 248  GLU A O   1 
ATOM   558  C  CB  . GLU A 1 248 ? -5.123  -8.964  -2.997  1.00 33.21 ? 248  GLU A CB  1 
ATOM   559  C  CG  . GLU A 1 248 ? -6.597  -8.593  -2.978  1.00 35.62 ? 248  GLU A CG  1 
ATOM   560  C  CD  . GLU A 1 248 ? -7.160  -8.608  -1.574  1.00 38.15 ? 248  GLU A CD  1 
ATOM   561  O  OE1 . GLU A 1 248 ? -7.269  -9.712  -1.003  1.00 40.54 ? 248  GLU A OE1 1 
ATOM   562  O  OE2 . GLU A 1 248 ? -7.472  -7.517  -1.040  1.00 42.09 ? 248  GLU A OE2 1 
ATOM   563  N  N   . ILE A 1 249 ? -1.904  -7.835  -2.342  1.00 29.37 ? 249  ILE A N   1 
ATOM   564  C  CA  . ILE A 1 249 ? -0.538  -8.274  -2.558  1.00 30.25 ? 249  ILE A CA  1 
ATOM   565  C  C   . ILE A 1 249 ? 0.263   -8.269  -1.267  1.00 29.93 ? 249  ILE A C   1 
ATOM   566  O  O   . ILE A 1 249 ? 0.265   -7.278  -0.544  1.00 30.27 ? 249  ILE A O   1 
ATOM   567  C  CB  . ILE A 1 249 ? 0.169   -7.381  -3.602  1.00 30.42 ? 249  ILE A CB  1 
ATOM   568  C  CG1 . ILE A 1 249 ? -0.605  -7.393  -4.937  1.00 30.09 ? 249  ILE A CG1 1 
ATOM   569  C  CG2 . ILE A 1 249 ? 1.610   -7.830  -3.805  1.00 31.05 ? 249  ILE A CG2 1 
ATOM   570  C  CD1 . ILE A 1 249 ? -0.867  -8.772  -5.521  1.00 30.14 ? 249  ILE A CD1 1 
ATOM   571  N  N   . LYS A 1 250 ? 0.958   -9.370  -0.993  1.00 29.80 ? 250  LYS A N   1 
ATOM   572  C  CA  . LYS A 1 250 ? 1.816   -9.455  0.186   1.00 31.08 ? 250  LYS A CA  1 
ATOM   573  C  C   . LYS A 1 250 ? 3.145   -10.122 -0.103  1.00 29.80 ? 250  LYS A C   1 
ATOM   574  O  O   . LYS A 1 250 ? 3.318   -10.850 -1.088  1.00 28.59 ? 250  LYS A O   1 
ATOM   575  C  CB  . LYS A 1 250 ? 1.127   -10.177 1.370   1.00 34.20 ? 250  LYS A CB  1 
ATOM   576  C  CG  . LYS A 1 250 ? -0.194  -10.871 1.077   1.00 35.70 ? 250  LYS A CG  1 
ATOM   577  C  CD  . LYS A 1 250 ? -0.523  -11.903 2.147   1.00 38.21 ? 250  LYS A CD  1 
ATOM   578  C  CE  . LYS A 1 250 ? 0.230   -13.216 1.910   1.00 40.56 ? 250  LYS A CE  1 
ATOM   579  N  NZ  . LYS A 1 250 ? 0.625   -13.913 3.174   1.00 40.65 ? 250  LYS A NZ  1 
ATOM   580  N  N   . ASN A 1 251 ? 4.085   -9.864  0.789   1.00 29.13 ? 251  ASN A N   1 
ATOM   581  C  CA  . ASN A 1 251 ? 5.394   -10.467 0.707   1.00 28.24 ? 251  ASN A CA  1 
ATOM   582  C  C   . ASN A 1 251 ? 5.253   -11.967 0.870   1.00 28.14 ? 251  ASN A C   1 
ATOM   583  O  O   . ASN A 1 251 ? 4.273   -12.451 1.431   1.00 27.50 ? 251  ASN A O   1 
ATOM   584  C  CB  . ASN A 1 251 ? 6.308   -9.899  1.788   1.00 28.10 ? 251  ASN A CB  1 
ATOM   585  C  CG  . ASN A 1 251 ? 6.611   -8.423  1.588   1.00 28.92 ? 251  ASN A CG  1 
ATOM   586  O  OD1 . ASN A 1 251 ? 6.591   -7.907  0.462   1.00 29.95 ? 251  ASN A OD1 1 
ATOM   587  N  ND2 . ASN A 1 251 ? 6.907   -7.733  2.684   1.00 27.46 ? 251  ASN A ND2 1 
ATOM   588  N  N   . MET A 1 252 ? 6.219   -12.700 0.344   1.00 27.98 ? 252  MET A N   1 
ATOM   589  C  CA  . MET A 1 252 ? 6.212   -14.145 0.449   1.00 28.14 ? 252  MET A CA  1 
ATOM   590  C  C   . MET A 1 252 ? 6.853   -14.533 1.786   1.00 26.41 ? 252  MET A C   1 
ATOM   591  O  O   . MET A 1 252 ? 8.014   -14.224 2.027   1.00 23.63 ? 252  MET A O   1 
ATOM   592  C  CB  . MET A 1 252 ? 6.998   -14.750 -0.708  1.00 29.35 ? 252  MET A CB  1 
ATOM   593  C  CG  . MET A 1 252 ? 6.886   -16.252 -0.812  1.00 32.00 ? 252  MET A CG  1 
ATOM   594  S  SD  . MET A 1 252 ? 7.860   -16.901 -2.194  1.00 36.31 ? 252  MET A SD  1 
ATOM   595  C  CE  . MET A 1 252 ? 7.229   -18.571 -2.177  1.00 36.31 ? 252  MET A CE  1 
ATOM   596  N  N   . PRO A 1 253 ? 6.106   -15.224 2.653   1.00 26.78 ? 253  PRO A N   1 
ATOM   597  C  CA  . PRO A 1 253 ? 6.695   -15.638 3.942   1.00 26.95 ? 253  PRO A CA  1 
ATOM   598  C  C   . PRO A 1 253 ? 7.995   -16.451 3.802   1.00 27.44 ? 253  PRO A C   1 
ATOM   599  O  O   . PRO A 1 253 ? 8.952   -16.220 4.542   1.00 28.07 ? 253  PRO A O   1 
ATOM   600  C  CB  . PRO A 1 253 ? 5.579   -16.487 4.581   1.00 26.91 ? 253  PRO A CB  1 
ATOM   601  C  CG  . PRO A 1 253 ? 4.318   -15.940 3.994   1.00 27.29 ? 253  PRO A CG  1 
ATOM   602  C  CD  . PRO A 1 253 ? 4.667   -15.549 2.570   1.00 26.45 ? 253  PRO A CD  1 
ATOM   603  N  N   . ALA A 1 254 ? 8.045   -17.366 2.841   1.00 26.81 ? 254  ALA A N   1 
ATOM   604  C  CA  . ALA A 1 254 ? 9.253   -18.154 2.590   1.00 26.30 ? 254  ALA A CA  1 
ATOM   605  C  C   . ALA A 1 254 ? 10.443  -17.302 2.134   1.00 25.67 ? 254  ALA A C   1 
ATOM   606  O  O   . ALA A 1 254 ? 11.579  -17.775 2.123   1.00 25.74 ? 254  ALA A O   1 
ATOM   607  C  CB  . ALA A 1 254 ? 8.962   -19.239 1.565   1.00 26.56 ? 254  ALA A CB  1 
ATOM   608  N  N   . ALA A 1 255 ? 10.191  -16.055 1.751   1.00 26.29 ? 255  ALA A N   1 
ATOM   609  C  CA  . ALA A 1 255 ? 11.277  -15.124 1.419   1.00 26.86 ? 255  ALA A CA  1 
ATOM   610  C  C   . ALA A 1 255 ? 11.868  -14.447 2.656   1.00 26.90 ? 255  ALA A C   1 
ATOM   611  O  O   . ALA A 1 255 ? 12.875  -13.738 2.543   1.00 27.65 ? 255  ALA A O   1 
ATOM   612  C  CB  . ALA A 1 255 ? 10.797  -14.076 0.432   1.00 26.69 ? 255  ALA A CB  1 
ATOM   613  N  N   . THR A 1 256 ? 11.233  -14.607 3.818   1.00 27.02 ? 256  THR A N   1 
ATOM   614  C  CA  . THR A 1 256 ? 11.908  -14.291 5.097   1.00 27.89 ? 256  THR A CA  1 
ATOM   615  C  C   . THR A 1 256 ? 12.628  -15.558 5.511   1.00 27.41 ? 256  THR A C   1 
ATOM   616  O  O   . THR A 1 256 ? 11.985  -16.556 5.825   1.00 27.26 ? 256  THR A O   1 
ATOM   617  C  CB  . THR A 1 256 ? 10.928  -13.855 6.200   1.00 28.67 ? 256  THR A CB  1 
ATOM   618  O  OG1 . THR A 1 256 ? 10.370  -12.585 5.856   1.00 30.83 ? 256  THR A OG1 1 
ATOM   619  C  CG2 . THR A 1 256 ? 11.637  -13.718 7.560   1.00 29.00 ? 256  THR A CG2 1 
ATOM   620  N  N   . THR A 1 257 ? 13.958  -15.529 5.496   1.00 26.84 ? 257  THR A N   1 
ATOM   621  C  CA  . THR A 1 257 ? 14.728  -16.764 5.617   1.00 28.01 ? 257  THR A CA  1 
ATOM   622  C  C   . THR A 1 257 ? 16.197  -16.458 5.903   1.00 27.61 ? 257  THR A C   1 
ATOM   623  O  O   . THR A 1 257 ? 16.645  -15.315 5.776   1.00 27.19 ? 257  THR A O   1 
ATOM   624  C  CB  . THR A 1 257 ? 14.584  -17.616 4.324   1.00 27.34 ? 257  THR A CB  1 
ATOM   625  O  OG1 . THR A 1 257 ? 15.058  -18.948 4.537   1.00 28.19 ? 257  THR A OG1 1 
ATOM   626  C  CG2 . THR A 1 257 ? 15.359  -17.007 3.170   1.00 28.62 ? 257  THR A CG2 1 
ATOM   627  N  N   . LYS A 1 258 ? 16.945  -17.482 6.292   1.00 28.68 ? 258  LYS A N   1 
ATOM   628  C  CA  . LYS A 1 258 ? 18.385  -17.333 6.477   1.00 29.67 ? 258  LYS A CA  1 
ATOM   629  C  C   . LYS A 1 258 ? 19.098  -17.012 5.143   1.00 29.13 ? 258  LYS A C   1 
ATOM   630  O  O   . LYS A 1 258 ? 19.049  -17.799 4.188   1.00 28.22 ? 258  LYS A O   1 
ATOM   631  C  CB  . LYS A 1 258 ? 18.961  -18.590 7.113   1.00 30.63 ? 258  LYS A CB  1 
ATOM   632  C  CG  . LYS A 1 258 ? 20.349  -18.414 7.701   1.00 31.56 ? 258  LYS A CG  1 
ATOM   633  C  CD  . LYS A 1 258 ? 20.821  -19.722 8.329   1.00 33.52 ? 258  LYS A CD  1 
ATOM   634  C  CE  . LYS A 1 258 ? 22.298  -19.696 8.693   1.00 35.95 ? 258  LYS A CE  1 
ATOM   635  N  NZ  . LYS A 1 258 ? 22.802  -21.061 9.023   1.00 37.03 ? 258  LYS A NZ  1 
ATOM   636  N  N   . ASP A 1 259 ? 19.753  -15.852 5.112   1.00 28.02 ? 259  ASP A N   1 
ATOM   637  C  CA  . ASP A 1 259 ? 20.392  -15.308 3.923   1.00 28.77 ? 259  ASP A CA  1 
ATOM   638  C  C   . ASP A 1 259 ? 21.718  -16.004 3.664   1.00 30.30 ? 259  ASP A C   1 
ATOM   639  O  O   . ASP A 1 259 ? 22.531  -16.178 4.589   1.00 30.04 ? 259  ASP A O   1 
ATOM   640  C  CB  . ASP A 1 259 ? 20.626  -13.798 4.105   1.00 28.41 ? 259  ASP A CB  1 
ATOM   641  C  CG  . ASP A 1 259 ? 21.275  -13.144 2.891   1.00 29.93 ? 259  ASP A CG  1 
ATOM   642  O  OD1 . ASP A 1 259 ? 20.578  -12.981 1.870   1.00 29.21 ? 259  ASP A OD1 1 
ATOM   643  O  OD2 . ASP A 1 259 ? 22.469  -12.763 2.960   1.00 29.06 ? 259  ASP A OD2 1 
ATOM   644  N  N   . ALA A 1 260 ? 21.925  -16.390 2.401   1.00 28.56 ? 260  ALA A N   1 
ATOM   645  C  CA  . ALA A 1 260 ? 23.129  -17.086 1.944   1.00 28.27 ? 260  ALA A CA  1 
ATOM   646  C  C   . ALA A 1 260 ? 24.461  -16.394 2.274   1.00 28.52 ? 260  ALA A C   1 
ATOM   647  O  O   . ALA A 1 260 ? 25.479  -17.071 2.436   1.00 28.79 ? 260  ALA A O   1 
ATOM   648  C  CB  . ALA A 1 260 ? 23.052  -17.324 0.434   1.00 28.31 ? 260  ALA A CB  1 
ATOM   649  N  N   . GLN A 1 261 ? 24.465  -15.066 2.349   1.00 27.97 ? 261  GLN A N   1 
ATOM   650  C  CA  . GLN A 1 261 ? 25.701  -14.322 2.591   1.00 29.66 ? 261  GLN A CA  1 
ATOM   651  C  C   . GLN A 1 261 ? 25.859  -13.850 4.044   1.00 31.23 ? 261  GLN A C   1 
ATOM   652  O  O   . GLN A 1 261 ? 26.956  -13.928 4.575   1.00 32.36 ? 261  GLN A O   1 
ATOM   653  C  CB  . GLN A 1 261 ? 25.830  -13.128 1.632   1.00 29.26 ? 261  GLN A CB  1 
ATOM   654  C  CG  . GLN A 1 261 ? 25.896  -13.532 0.162   1.00 28.75 ? 261  GLN A CG  1 
ATOM   655  C  CD  . GLN A 1 261 ? 26.073  -12.368 -0.800  1.00 28.39 ? 261  GLN A CD  1 
ATOM   656  O  OE1 . GLN A 1 261 ? 26.465  -12.568 -1.939  1.00 28.54 ? 261  GLN A OE1 1 
ATOM   657  N  NE2 . GLN A 1 261 ? 25.769  -11.156 -0.355  1.00 28.90 ? 261  GLN A NE2 1 
ATOM   658  N  N   . THR A 1 262 ? 24.794  -13.369 4.683   1.00 33.63 ? 262  THR A N   1 
ATOM   659  C  CA  . THR A 1 262 ? 24.898  -12.900 6.070   1.00 35.95 ? 262  THR A CA  1 
ATOM   660  C  C   . THR A 1 262 ? 24.681  -13.989 7.127   1.00 37.55 ? 262  THR A C   1 
ATOM   661  O  O   . THR A 1 262 ? 25.045  -13.787 8.284   1.00 38.15 ? 262  THR A O   1 
ATOM   662  C  CB  . THR A 1 262 ? 23.922  -11.750 6.373   1.00 35.95 ? 262  THR A CB  1 
ATOM   663  O  OG1 . THR A 1 262 ? 22.574  -12.230 6.336   1.00 36.87 ? 262  THR A OG1 1 
ATOM   664  C  CG2 . THR A 1 262 ? 24.110  -10.589 5.379   1.00 35.75 ? 262  THR A CG2 1 
ATOM   665  N  N   . ASN A 1 263 ? 24.079  -15.117 6.735   1.00 37.92 ? 263  ASN A N   1 
ATOM   666  C  CA  . ASN A 1 263 ? 23.766  -16.228 7.656   1.00 38.41 ? 263  ASN A CA  1 
ATOM   667  C  C   . ASN A 1 263 ? 22.746  -15.861 8.736   1.00 37.86 ? 263  ASN A C   1 
ATOM   668  O  O   . ASN A 1 263 ? 22.638  -16.542 9.749   1.00 35.91 ? 263  ASN A O   1 
ATOM   669  C  CB  . ASN A 1 263 ? 25.046  -16.773 8.308   1.00 38.84 ? 263  ASN A CB  1 
ATOM   670  C  CG  . ASN A 1 263 ? 26.111  -17.115 7.286   1.00 38.97 ? 263  ASN A CG  1 
ATOM   671  O  OD1 . ASN A 1 263 ? 25.837  -17.792 6.299   1.00 39.15 ? 263  ASN A OD1 1 
ATOM   672  N  ND2 . ASN A 1 263 ? 27.328  -16.635 7.506   1.00 38.80 ? 263  ASN A ND2 1 
ATOM   673  N  N   . THR A 1 264 ? 21.998  -14.788 8.489   1.00 38.11 ? 264  THR A N   1 
ATOM   674  C  CA  . THR A 1 264 ? 21.019  -14.258 9.412   1.00 37.06 ? 264  THR A CA  1 
ATOM   675  C  C   . THR A 1 264 ? 19.678  -14.233 8.694   1.00 36.82 ? 264  THR A C   1 
ATOM   676  O  O   . THR A 1 264 ? 19.632  -14.006 7.480   1.00 36.84 ? 264  THR A O   1 
ATOM   677  C  CB  . THR A 1 264 ? 21.380  -12.820 9.815   1.00 38.30 ? 264  THR A CB  1 
ATOM   678  O  OG1 . THR A 1 264 ? 21.377  -11.983 8.653   1.00 41.36 ? 264  THR A OG1 1 
ATOM   679  C  CG2 . THR A 1 264 ? 22.754  -12.764 10.448  1.00 38.96 ? 264  THR A CG2 1 
ATOM   680  N  N   . ILE A 1 265 ? 18.598  -14.442 9.443   1.00 34.05 ? 265  ILE A N   1 
ATOM   681  C  CA  . ILE A 1 265 ? 17.249  -14.453 8.892   1.00 33.16 ? 265  ILE A CA  1 
ATOM   682  C  C   . ILE A 1 265 ? 16.793  -13.031 8.532   1.00 35.00 ? 265  ILE A C   1 
ATOM   683  O  O   . ILE A 1 265 ? 16.776  -12.145 9.396   1.00 36.11 ? 265  ILE A O   1 
ATOM   684  C  CB  . ILE A 1 265 ? 16.253  -15.094 9.878   1.00 32.47 ? 265  ILE A CB  1 
ATOM   685  C  CG1 . ILE A 1 265 ? 16.694  -16.534 10.184  1.00 33.28 ? 265  ILE A CG1 1 
ATOM   686  C  CG2 . ILE A 1 265 ? 14.835  -15.080 9.317   1.00 31.97 ? 265  ILE A CG2 1 
ATOM   687  C  CD1 . ILE A 1 265 ? 15.669  -17.361 10.928  1.00 32.47 ? 265  ILE A CD1 1 
ATOM   688  N  N   . GLU A 1 266 ? 16.430  -12.810 7.266   1.00 32.39 ? 266  GLU A N   1 
ATOM   689  C  CA  . GLU A 1 266 ? 16.022  -11.472 6.812   1.00 33.06 ? 266  GLU A CA  1 
ATOM   690  C  C   . GLU A 1 266 ? 14.832  -11.547 5.858   1.00 31.09 ? 266  GLU A C   1 
ATOM   691  O  O   . GLU A 1 266 ? 14.640  -12.561 5.199   1.00 31.35 ? 266  GLU A O   1 
ATOM   692  C  CB  . GLU A 1 266 ? 17.172  -10.756 6.092   1.00 33.87 ? 266  GLU A CB  1 
ATOM   693  C  CG  . GLU A 1 266 ? 18.507  -10.738 6.820   1.00 36.26 ? 266  GLU A CG  1 
ATOM   694  C  CD  . GLU A 1 266 ? 18.476  -9.999  8.150   1.00 38.20 ? 266  GLU A CD  1 
ATOM   695  O  OE1 . GLU A 1 266 ? 17.574  -9.157  8.376   1.00 39.13 ? 266  GLU A OE1 1 
ATOM   696  O  OE2 . GLU A 1 266 ? 19.378  -10.266 8.970   1.00 40.18 ? 266  GLU A OE2 1 
ATOM   697  N  N   . PRO A 1 267 ? 14.037  -10.466 5.776   1.00 29.82 ? 267  PRO A N   1 
ATOM   698  C  CA  . PRO A 1 267 ? 13.040  -10.368 4.710   1.00 29.87 ? 267  PRO A CA  1 
ATOM   699  C  C   . PRO A 1 267 ? 13.729  -10.076 3.367   1.00 29.56 ? 267  PRO A C   1 
ATOM   700  O  O   . PRO A 1 267 ? 14.245  -8.978  3.164   1.00 29.69 ? 267  PRO A O   1 
ATOM   701  C  CB  . PRO A 1 267 ? 12.158  -9.188  5.145   1.00 30.16 ? 267  PRO A CB  1 
ATOM   702  C  CG  . PRO A 1 267 ? 12.991  -8.378  6.077   1.00 29.63 ? 267  PRO A CG  1 
ATOM   703  C  CD  . PRO A 1 267 ? 14.128  -9.231  6.575   1.00 30.13 ? 267  PRO A CD  1 
ATOM   704  N  N   . LEU A 1 268 ? 13.759  -11.063 2.473   1.00 27.83 ? 268  LEU A N   1 
ATOM   705  C  CA  . LEU A 1 268 ? 14.451  -10.905 1.194   1.00 26.74 ? 268  LEU A CA  1 
ATOM   706  C  C   . LEU A 1 268 ? 13.514  -10.549 0.045   1.00 26.04 ? 268  LEU A C   1 
ATOM   707  O  O   . LEU A 1 268 ? 12.318  -10.912 0.046   1.00 25.48 ? 268  LEU A O   1 
ATOM   708  C  CB  . LEU A 1 268 ? 15.222  -12.177 0.843   1.00 26.94 ? 268  LEU A CB  1 
ATOM   709  C  CG  . LEU A 1 268 ? 16.180  -12.736 1.921   1.00 27.28 ? 268  LEU A CG  1 
ATOM   710  C  CD1 . LEU A 1 268 ? 16.806  -14.033 1.443   1.00 26.64 ? 268  LEU A CD1 1 
ATOM   711  C  CD2 . LEU A 1 268 ? 17.275  -11.751 2.295   1.00 27.30 ? 268  LEU A CD2 1 
ATOM   712  N  N   . ASP A 1 269 ? 14.075  -9.831  -0.933  1.00 23.87 ? 269  ASP A N   1 
ATOM   713  C  CA  . ASP A 1 269 ? 13.490  -9.748  -2.260  1.00 22.43 ? 269  ASP A CA  1 
ATOM   714  C  C   . ASP A 1 269 ? 13.540  -11.158 -2.838  1.00 21.14 ? 269  ASP A C   1 
ATOM   715  O  O   . ASP A 1 269 ? 14.553  -11.837 -2.710  1.00 20.80 ? 269  ASP A O   1 
ATOM   716  C  CB  . ASP A 1 269 ? 14.299  -8.800  -3.163  1.00 22.40 ? 269  ASP A CB  1 
ATOM   717  C  CG  . ASP A 1 269 ? 13.942  -7.325  -2.973  1.00 22.15 ? 269  ASP A CG  1 
ATOM   718  O  OD1 . ASP A 1 269 ? 12.805  -7.034  -2.557  1.00 21.83 ? 269  ASP A OD1 1 
ATOM   719  O  OD2 . ASP A 1 269 ? 14.801  -6.444  -3.287  1.00 23.12 ? 269  ASP A OD2 1 
ATOM   720  N  N   . VAL A 1 270 ? 12.447  -11.608 -3.445  1.00 20.63 ? 270  VAL A N   1 
ATOM   721  C  CA  . VAL A 1 270 ? 12.481  -12.789 -4.311  1.00 20.23 ? 270  VAL A CA  1 
ATOM   722  C  C   . VAL A 1 270 ? 12.078  -12.360 -5.728  1.00 20.91 ? 270  VAL A C   1 
ATOM   723  O  O   . VAL A 1 270 ? 11.045  -11.709 -5.932  1.00 21.81 ? 270  VAL A O   1 
ATOM   724  C  CB  . VAL A 1 270 ? 11.587  -13.948 -3.804  1.00 20.28 ? 270  VAL A CB  1 
ATOM   725  C  CG1 . VAL A 1 270 ? 10.144  -13.506 -3.569  1.00 20.57 ? 270  VAL A CG1 1 
ATOM   726  C  CG2 . VAL A 1 270 ? 11.627  -15.124 -4.769  1.00 20.12 ? 270  VAL A CG2 1 
ATOM   727  N  N   . TRP A 1 271 ? 12.904  -12.688 -6.707  1.00 20.84 ? 271  TRP A N   1 
ATOM   728  C  CA  . TRP A 1 271 ? 12.603  -12.290 -8.074  1.00 21.63 ? 271  TRP A CA  1 
ATOM   729  C  C   . TRP A 1 271 ? 12.562  -13.520 -9.001  1.00 21.72 ? 271  TRP A C   1 
ATOM   730  O  O   . TRP A 1 271 ? 11.740  -14.411 -8.794  1.00 22.07 ? 271  TRP A O   1 
ATOM   731  C  CB  . TRP A 1 271 ? 13.477  -11.092 -8.550  1.00 21.50 ? 271  TRP A CB  1 
ATOM   732  C  CG  . TRP A 1 271 ? 14.989  -11.221 -8.548  1.00 21.50 ? 271  TRP A CG  1 
ATOM   733  C  CD1 . TRP A 1 271 ? 15.793  -11.387 -9.647  1.00 21.33 ? 271  TRP A CD1 1 
ATOM   734  C  CD2 . TRP A 1 271 ? 15.881  -11.121 -7.421  1.00 22.07 ? 271  TRP A CD2 1 
ATOM   735  N  NE1 . TRP A 1 271 ? 17.106  -11.435 -9.277  1.00 22.05 ? 271  TRP A NE1 1 
ATOM   736  C  CE2 . TRP A 1 271 ? 17.197  -11.270 -7.918  1.00 21.90 ? 271  TRP A CE2 1 
ATOM   737  C  CE3 . TRP A 1 271 ? 15.699  -10.921 -6.046  1.00 21.93 ? 271  TRP A CE3 1 
ATOM   738  C  CZ2 . TRP A 1 271 ? 18.325  -11.233 -7.087  1.00 22.32 ? 271  TRP A CZ2 1 
ATOM   739  C  CZ3 . TRP A 1 271 ? 16.826  -10.883 -5.216  1.00 21.63 ? 271  TRP A CZ3 1 
ATOM   740  C  CH2 . TRP A 1 271 ? 18.117  -11.047 -5.738  1.00 22.12 ? 271  TRP A CH2 1 
ATOM   741  N  N   . ASP A 1 272 ? 13.418  -13.584 -10.001 1.00 22.58 ? 272  ASP A N   1 
ATOM   742  C  CA  . ASP A 1 272 ? 13.370  -14.650 -10.987 1.00 22.60 ? 272  ASP A CA  1 
ATOM   743  C  C   . ASP A 1 272 ? 13.217  -16.030 -10.376 1.00 21.76 ? 272  ASP A C   1 
ATOM   744  O  O   . ASP A 1 272 ? 13.988  -16.420 -9.512  1.00 20.74 ? 272  ASP A O   1 
ATOM   745  C  CB  . ASP A 1 272 ? 14.627  -14.603 -11.844 1.00 24.24 ? 272  ASP A CB  1 
ATOM   746  C  CG  . ASP A 1 272 ? 14.595  -13.460 -12.840 1.00 27.78 ? 272  ASP A CG  1 
ATOM   747  O  OD1 . ASP A 1 272 ? 14.353  -12.303 -12.443 1.00 27.47 ? 272  ASP A OD1 1 
ATOM   748  O  OD2 . ASP A 1 272 ? 14.784  -13.732 -14.038 1.00 34.13 ? 272  ASP A OD2 1 
ATOM   749  N  N   . SER A 1 273 ? 12.210  -16.765 -10.840 1.00 21.21 ? 273  SER A N   1 
ATOM   750  C  CA  . SER A 1 273 ? 11.911  -18.084 -10.302 1.00 20.85 ? 273  SER A CA  1 
ATOM   751  C  C   . SER A 1 273 ? 11.482  -19.014 -11.411 1.00 21.05 ? 273  SER A C   1 
ATOM   752  O  O   . SER A 1 273 ? 10.999  -18.584 -12.467 1.00 21.14 ? 273  SER A O   1 
ATOM   753  C  CB  . SER A 1 273 ? 10.808  -18.005 -9.246  1.00 20.86 ? 273  SER A CB  1 
ATOM   754  O  OG  . SER A 1 273 ? 11.098  -17.024 -8.251  1.00 21.61 ? 273  SER A OG  1 
ATOM   755  N  N   . TRP A 1 274 ? 11.677  -20.294 -11.169 1.00 20.06 ? 274  TRP A N   1 
ATOM   756  C  CA  . TRP A 1 274 ? 11.294  -21.316 -12.123 1.00 20.68 ? 274  TRP A CA  1 
ATOM   757  C  C   . TRP A 1 274 ? 10.974  -22.630 -11.410 1.00 20.28 ? 274  TRP A C   1 
ATOM   758  O  O   . TRP A 1 274 ? 11.542  -22.940 -10.345 1.00 19.63 ? 274  TRP A O   1 
ATOM   759  C  CB  . TRP A 1 274 ? 12.374  -21.517 -13.166 1.00 19.96 ? 274  TRP A CB  1 
ATOM   760  C  CG  . TRP A 1 274 ? 13.692  -21.918 -12.612 1.00 19.96 ? 274  TRP A CG  1 
ATOM   761  C  CD1 . TRP A 1 274 ? 14.186  -23.194 -12.489 1.00 20.10 ? 274  TRP A CD1 1 
ATOM   762  C  CD2 . TRP A 1 274 ? 14.706  -21.046 -12.122 1.00 19.77 ? 274  TRP A CD2 1 
ATOM   763  N  NE1 . TRP A 1 274 ? 15.461  -23.160 -11.949 1.00 20.14 ? 274  TRP A NE1 1 
ATOM   764  C  CE2 . TRP A 1 274 ? 15.800  -21.855 -11.711 1.00 20.09 ? 274  TRP A CE2 1 
ATOM   765  C  CE3 . TRP A 1 274 ? 14.793  -19.665 -11.960 1.00 19.19 ? 274  TRP A CE3 1 
ATOM   766  C  CZ2 . TRP A 1 274 ? 16.955  -21.318 -11.162 1.00 19.56 ? 274  TRP A CZ2 1 
ATOM   767  C  CZ3 . TRP A 1 274 ? 15.938  -19.140 -11.414 1.00 19.34 ? 274  TRP A CZ3 1 
ATOM   768  C  CH2 . TRP A 1 274 ? 17.002  -19.963 -11.019 1.00 19.48 ? 274  TRP A CH2 1 
ATOM   769  N  N   . PRO A 1 275 ? 10.018  -23.378 -11.960 1.00 20.79 ? 275  PRO A N   1 
ATOM   770  C  CA  . PRO A 1 275 ? 9.582   -24.573 -11.282 1.00 20.84 ? 275  PRO A CA  1 
ATOM   771  C  C   . PRO A 1 275 ? 10.397  -25.733 -11.784 1.00 20.70 ? 275  PRO A C   1 
ATOM   772  O  O   . PRO A 1 275 ? 10.997  -25.658 -12.869 1.00 21.18 ? 275  PRO A O   1 
ATOM   773  C  CB  . PRO A 1 275 ? 8.135   -24.689 -11.727 1.00 21.27 ? 275  PRO A CB  1 
ATOM   774  C  CG  . PRO A 1 275 ? 8.174   -24.225 -13.140 1.00 21.66 ? 275  PRO A CG  1 
ATOM   775  C  CD  . PRO A 1 275 ? 9.256   -23.164 -13.204 1.00 21.42 ? 275  PRO A CD  1 
ATOM   776  N  N   . VAL A 1 276 ? 10.447  -26.794 -10.995 1.00 20.59 ? 276  VAL A N   1 
ATOM   777  C  CA  . VAL A 1 276 ? 10.994  -28.032 -11.482 1.00 20.49 ? 276  VAL A CA  1 
ATOM   778  C  C   . VAL A 1 276 ? 9.935   -28.561 -12.428 1.00 20.57 ? 276  VAL A C   1 
ATOM   779  O  O   . VAL A 1 276 ? 8.781   -28.758 -12.028 1.00 20.78 ? 276  VAL A O   1 
ATOM   780  C  CB  . VAL A 1 276 ? 11.282  -29.047 -10.357 1.00 20.85 ? 276  VAL A CB  1 
ATOM   781  C  CG1 . VAL A 1 276 ? 11.742  -30.363 -10.957 1.00 20.62 ? 276  VAL A CG1 1 
ATOM   782  C  CG2 . VAL A 1 276 ? 12.334  -28.483 -9.406  1.00 21.08 ? 276  VAL A CG2 1 
ATOM   783  N  N   . GLN A 1 277 ? 10.356  -28.787 -13.669 1.00 20.35 ? 277  GLN A N   1 
ATOM   784  C  CA  . GLN A 1 277 ? 9.485   -29.090 -14.780 1.00 21.61 ? 277  GLN A CA  1 
ATOM   785  C  C   . GLN A 1 277 ? 9.815   -30.429 -15.362 1.00 21.09 ? 277  GLN A C   1 
ATOM   786  O  O   . GLN A 1 277 ? 10.931  -30.913 -15.236 1.00 21.75 ? 277  GLN A O   1 
ATOM   787  C  CB  . GLN A 1 277 ? 9.696   -28.063 -15.911 1.00 22.18 ? 277  GLN A CB  1 
ATOM   788  C  CG  . GLN A 1 277 ? 9.203   -26.687 -15.577 1.00 23.56 ? 277  GLN A CG  1 
ATOM   789  C  CD  . GLN A 1 277 ? 9.383   -25.694 -16.713 1.00 23.75 ? 277  GLN A CD  1 
ATOM   790  O  OE1 . GLN A 1 277 ? 10.442  -25.074 -16.845 1.00 25.67 ? 277  GLN A OE1 1 
ATOM   791  N  NE2 . GLN A 1 277 ? 8.335   -25.516 -17.522 1.00 23.62 ? 277  GLN A NE2 1 
ATOM   792  N  N   . ASP A 1 278 ? 8.841   -31.016 -16.041 1.00 22.00 ? 278  ASP A N   1 
ATOM   793  C  CA  . ASP A 1 278 ? 9.085   -32.206 -16.848 1.00 23.09 ? 278  ASP A CA  1 
ATOM   794  C  C   . ASP A 1 278 ? 9.873   -31.783 -18.083 1.00 23.20 ? 278  ASP A C   1 
ATOM   795  O  O   . ASP A 1 278 ? 9.470   -30.862 -18.810 1.00 23.90 ? 278  ASP A O   1 
ATOM   796  C  CB  . ASP A 1 278 ? 7.764   -32.855 -17.237 1.00 23.72 ? 278  ASP A CB  1 
ATOM   797  C  CG  . ASP A 1 278 ? 7.949   -34.096 -18.062 1.00 24.49 ? 278  ASP A CG  1 
ATOM   798  O  OD1 . ASP A 1 278 ? 8.368   -34.010 -19.232 1.00 24.72 ? 278  ASP A OD1 1 
ATOM   799  O  OD2 . ASP A 1 278 ? 7.644   -35.168 -17.534 1.00 27.20 ? 278  ASP A OD2 1 
ATOM   800  N  N   . VAL A 1 279 ? 10.988  -32.465 -18.312 1.00 24.20 ? 279  VAL A N   1 
ATOM   801  C  CA  . VAL A 1 279 ? 11.951  -32.076 -19.336 1.00 24.36 ? 279  VAL A CA  1 
ATOM   802  C  C   . VAL A 1 279 ? 11.345  -32.091 -20.746 1.00 24.84 ? 279  VAL A C   1 
ATOM   803  O  O   . VAL A 1 279 ? 11.769  -31.321 -21.605 1.00 23.27 ? 279  VAL A O   1 
ATOM   804  C  CB  . VAL A 1 279 ? 13.246  -32.926 -19.260 1.00 24.48 ? 279  VAL A CB  1 
ATOM   805  C  CG1 . VAL A 1 279 ? 13.011  -34.346 -19.753 1.00 25.10 ? 279  VAL A CG1 1 
ATOM   806  C  CG2 . VAL A 1 279 ? 14.377  -32.284 -20.054 1.00 25.28 ? 279  VAL A CG2 1 
ATOM   807  N  N   . ARG A 1 280 ? 10.347  -32.935 -20.986 1.00 27.66 ? 280  ARG A N   1 
ATOM   808  C  CA  . ARG A 1 280 ? 9.693   -32.962 -22.312 1.00 30.97 ? 280  ARG A CA  1 
ATOM   809  C  C   . ARG A 1 280 ? 8.476   -32.051 -22.447 1.00 28.59 ? 280  ARG A C   1 
ATOM   810  O  O   . ARG A 1 280 ? 8.358   -31.334 -23.429 1.00 28.35 ? 280  ARG A O   1 
ATOM   811  C  CB  . ARG A 1 280 ? 9.310   -34.384 -22.716 1.00 35.41 ? 280  ARG A CB  1 
ATOM   812  C  CG  . ARG A 1 280 ? 10.497  -35.221 -23.139 1.00 39.20 ? 280  ARG A CG  1 
ATOM   813  C  CD  . ARG A 1 280 ? 10.128  -36.682 -23.288 1.00 43.47 ? 280  ARG A CD  1 
ATOM   814  N  NE  . ARG A 1 280 ? 11.203  -37.527 -22.774 1.00 48.68 ? 280  ARG A NE  1 
ATOM   815  C  CZ  . ARG A 1 280 ? 11.434  -37.775 -21.483 1.00 50.74 ? 280  ARG A CZ  1 
ATOM   816  N  NH1 . ARG A 1 280 ? 10.660  -37.255 -20.533 1.00 53.50 ? 280  ARG A NH1 1 
ATOM   817  N  NH2 . ARG A 1 280 ? 12.458  -38.549 -21.139 1.00 53.79 ? 280  ARG A NH2 1 
ATOM   818  N  N   . THR A 1 281 ? 7.569   -32.087 -21.479 1.00 27.42 ? 281  THR A N   1 
ATOM   819  C  CA  . THR A 1 281 ? 6.275   -31.409 -21.633 1.00 26.16 ? 281  THR A CA  1 
ATOM   820  C  C   . THR A 1 281 ? 6.246   -29.998 -21.071 1.00 25.73 ? 281  THR A C   1 
ATOM   821  O  O   . THR A 1 281 ? 5.311   -29.258 -21.365 1.00 25.33 ? 281  THR A O   1 
ATOM   822  C  CB  . THR A 1 281 ? 5.155   -32.158 -20.918 1.00 25.69 ? 281  THR A CB  1 
ATOM   823  O  OG1 . THR A 1 281 ? 5.351   -32.060 -19.498 1.00 24.87 ? 281  THR A OG1 1 
ATOM   824  C  CG2 . THR A 1 281 ? 5.113   -33.617 -21.354 1.00 25.85 ? 281  THR A CG2 1 
ATOM   825  N  N   . GLY A 1 282 ? 7.226   -29.664 -20.223 1.00 24.70 ? 282  GLY A N   1 
ATOM   826  C  CA  . GLY A 1 282 ? 7.217   -28.436 -19.439 1.00 24.57 ? 282  GLY A CA  1 
ATOM   827  C  C   . GLY A 1 282 ? 6.284   -28.382 -18.220 1.00 24.57 ? 282  GLY A C   1 
ATOM   828  O  O   . GLY A 1 282 ? 6.290   -27.385 -17.479 1.00 24.18 ? 282  GLY A O   1 
ATOM   829  N  N   . GLN A 1 283 ? 5.484   -29.424 -17.988 1.00 24.40 ? 283  GLN A N   1 
ATOM   830  C  CA  . GLN A 1 283 ? 4.499   -29.390 -16.885 1.00 26.09 ? 283  GLN A CA  1 
ATOM   831  C  C   . GLN A 1 283 ? 5.244   -29.282 -15.546 1.00 24.32 ? 283  GLN A C   1 
ATOM   832  O  O   . GLN A 1 283 ? 6.315   -29.865 -15.397 1.00 22.28 ? 283  GLN A O   1 
ATOM   833  C  CB  . GLN A 1 283 ? 3.644   -30.660 -16.842 1.00 28.74 ? 283  GLN A CB  1 
ATOM   834  C  CG  . GLN A 1 283 ? 2.880   -30.985 -18.110 1.00 31.78 ? 283  GLN A CG  1 
ATOM   835  C  CD  . GLN A 1 283 ? 1.634   -30.160 -18.288 1.00 34.47 ? 283  GLN A CD  1 
ATOM   836  O  OE1 . GLN A 1 283 ? 1.328   -29.273 -17.494 1.00 35.22 ? 283  GLN A OE1 1 
ATOM   837  N  NE2 . GLN A 1 283 ? 0.900   -30.450 -19.352 1.00 38.73 ? 283  GLN A NE2 1 
ATOM   838  N  N   . VAL A 1 284 ? 4.679   -28.550 -14.596 1.00 23.00 ? 284  VAL A N   1 
ATOM   839  C  CA  . VAL A 1 284 ? 5.224   -28.477 -13.244 1.00 24.58 ? 284  VAL A CA  1 
ATOM   840  C  C   . VAL A 1 284 ? 5.271   -29.893 -12.667 1.00 25.13 ? 284  VAL A C   1 
ATOM   841  O  O   . VAL A 1 284 ? 4.256   -30.552 -12.593 1.00 27.66 ? 284  VAL A O   1 
ATOM   842  C  CB  . VAL A 1 284 ? 4.358   -27.587 -12.340 1.00 24.48 ? 284  VAL A CB  1 
ATOM   843  C  CG1 . VAL A 1 284 ? 4.842   -27.650 -10.887 1.00 23.71 ? 284  VAL A CG1 1 
ATOM   844  C  CG2 . VAL A 1 284 ? 4.354   -26.153 -12.871 1.00 24.85 ? 284  VAL A CG2 1 
ATOM   845  N  N   . ALA A 1 285 ? 6.450   -30.372 -12.304 1.00 26.00 ? 285  ALA A N   1 
ATOM   846  C  CA  . ALA A 1 285 ? 6.597   -31.773 -11.890 1.00 27.99 ? 285  ALA A CA  1 
ATOM   847  C  C   . ALA A 1 285 ? 5.952   -32.042 -10.539 1.00 27.99 ? 285  ALA A C   1 
ATOM   848  O  O   . ALA A 1 285 ? 5.990   -31.191 -9.644  1.00 25.80 ? 285  ALA A O   1 
ATOM   849  C  CB  . ALA A 1 285 ? 8.066   -32.165 -11.844 1.00 28.02 ? 285  ALA A CB  1 
ATOM   850  N  N   . ASN A 1 286 ? 5.323   -33.215 -10.422 1.00 29.74 ? 286  ASN A N   1 
ATOM   851  C  CA  . ASN A 1 286 ? 4.864   -33.740 -9.134  1.00 29.53 ? 286  ASN A CA  1 
ATOM   852  C  C   . ASN A 1 286 ? 5.966   -34.625 -8.558  1.00 30.48 ? 286  ASN A C   1 
ATOM   853  O  O   . ASN A 1 286 ? 6.206   -35.728 -9.062  1.00 31.89 ? 286  ASN A O   1 
ATOM   854  C  CB  . ASN A 1 286 ? 3.558   -34.532 -9.283  1.00 29.47 ? 286  ASN A CB  1 
ATOM   855  C  CG  . ASN A 1 286 ? 2.973   -34.968 -7.936  1.00 29.54 ? 286  ASN A CG  1 
ATOM   856  O  OD1 . ASN A 1 286 ? 3.701   -35.304 -7.003  1.00 30.02 ? 286  ASN A OD1 1 
ATOM   857  N  ND2 . ASN A 1 286 ? 1.659   -34.975 -7.840  1.00 28.88 ? 286  ASN A ND2 1 
ATOM   858  N  N   . TRP A 1 287 ? 6.662   -34.123 -7.536  1.00 29.51 ? 287  TRP A N   1 
ATOM   859  C  CA  . TRP A 1 287 ? 7.759   -34.866 -6.909  1.00 29.94 ? 287  TRP A CA  1 
ATOM   860  C  C   . TRP A 1 287 ? 7.308   -35.348 -5.532  1.00 29.79 ? 287  TRP A C   1 
ATOM   861  O  O   . TRP A 1 287 ? 7.156   -34.546 -4.598  1.00 27.85 ? 287  TRP A O   1 
ATOM   862  C  CB  . TRP A 1 287 ? 9.007   -33.988 -6.790  1.00 29.16 ? 287  TRP A CB  1 
ATOM   863  C  CG  . TRP A 1 287 ? 10.214  -34.728 -6.338  1.00 29.77 ? 287  TRP A CG  1 
ATOM   864  C  CD1 . TRP A 1 287 ? 11.094  -35.410 -7.118  1.00 31.11 ? 287  TRP A CD1 1 
ATOM   865  C  CD2 . TRP A 1 287 ? 10.679  -34.869 -4.992  1.00 30.67 ? 287  TRP A CD2 1 
ATOM   866  N  NE1 . TRP A 1 287 ? 12.087  -35.963 -6.347  1.00 30.79 ? 287  TRP A NE1 1 
ATOM   867  C  CE2 . TRP A 1 287 ? 11.851  -35.650 -5.036  1.00 30.80 ? 287  TRP A CE2 1 
ATOM   868  C  CE3 . TRP A 1 287 ? 10.214  -34.416 -3.749  1.00 31.02 ? 287  TRP A CE3 1 
ATOM   869  C  CZ2 . TRP A 1 287 ? 12.570  -35.985 -3.886  1.00 31.06 ? 287  TRP A CZ2 1 
ATOM   870  C  CZ3 . TRP A 1 287 ? 10.932  -34.741 -2.610  1.00 31.68 ? 287  TRP A CZ3 1 
ATOM   871  C  CH2 . TRP A 1 287 ? 12.096  -35.522 -2.686  1.00 31.74 ? 287  TRP A CH2 1 
ATOM   872  N  N   . ASN A 1 288 ? 7.052   -36.649 -5.425  1.00 30.76 ? 288  ASN A N   1 
ATOM   873  C  CA  . ASN A 1 288 ? 6.544   -37.255 -4.183  1.00 30.27 ? 288  ASN A CA  1 
ATOM   874  C  C   . ASN A 1 288 ? 5.402   -36.449 -3.565  1.00 31.13 ? 288  ASN A C   1 
ATOM   875  O  O   . ASN A 1 288 ? 5.383   -36.225 -2.350  1.00 33.60 ? 288  ASN A O   1 
ATOM   876  C  CB  . ASN A 1 288 ? 7.682   -37.389 -3.155  1.00 31.03 ? 288  ASN A CB  1 
ATOM   877  C  CG  . ASN A 1 288 ? 8.842   -38.233 -3.658  1.00 31.24 ? 288  ASN A CG  1 
ATOM   878  O  OD1 . ASN A 1 288 ? 10.000  -37.843 -3.540  1.00 34.60 ? 288  ASN A OD1 1 
ATOM   879  N  ND2 . ASN A 1 288 ? 8.538   -39.389 -4.217  1.00 30.78 ? 288  ASN A ND2 1 
ATOM   880  N  N   . GLY A 1 289 ? 4.463   -35.993 -4.394  1.00 30.00 ? 289  GLY A N   1 
ATOM   881  C  CA  . GLY A 1 289 ? 3.366   -35.152 -3.925  1.00 28.97 ? 289  GLY A CA  1 
ATOM   882  C  C   . GLY A 1 289 ? 3.707   -33.685 -3.652  1.00 28.47 ? 289  GLY A C   1 
ATOM   883  O  O   . GLY A 1 289 ? 2.861   -32.944 -3.151  1.00 28.02 ? 289  GLY A O   1 
ATOM   884  N  N   . TYR A 1 290 ? 4.925   -33.255 -3.977  1.00 27.21 ? 290  TYR A N   1 
ATOM   885  C  CA  . TYR A 1 290 ? 5.295   -31.842 -3.851  1.00 28.28 ? 290  TYR A CA  1 
ATOM   886  C  C   . TYR A 1 290 ? 5.483   -31.162 -5.215  1.00 26.53 ? 290  TYR A C   1 
ATOM   887  O  O   . TYR A 1 290 ? 5.829   -31.799 -6.219  1.00 25.16 ? 290  TYR A O   1 
ATOM   888  C  CB  . TYR A 1 290 ? 6.596   -31.660 -3.065  1.00 29.64 ? 290  TYR A CB  1 
ATOM   889  C  CG  . TYR A 1 290 ? 6.636   -32.236 -1.664  1.00 30.96 ? 290  TYR A CG  1 
ATOM   890  C  CD1 . TYR A 1 290 ? 6.234   -31.479 -0.563  1.00 31.91 ? 290  TYR A CD1 1 
ATOM   891  C  CD2 . TYR A 1 290 ? 7.127   -33.517 -1.439  1.00 32.69 ? 290  TYR A CD2 1 
ATOM   892  C  CE1 . TYR A 1 290 ? 6.295   -31.996 0.725   1.00 34.81 ? 290  TYR A CE1 1 
ATOM   893  C  CE2 . TYR A 1 290 ? 7.212   -34.040 -0.161  1.00 34.67 ? 290  TYR A CE2 1 
ATOM   894  C  CZ  . TYR A 1 290 ? 6.792   -33.282 0.918   1.00 36.20 ? 290  TYR A CZ  1 
ATOM   895  O  OH  . TYR A 1 290 ? 6.862   -33.814 2.186   1.00 40.01 ? 290  TYR A OH  1 
ATOM   896  N  N   . GLN A 1 291 ? 5.255   -29.856 -5.227  1.00 25.57 ? 291  GLN A N   1 
ATOM   897  C  CA  . GLN A 1 291 ? 5.768   -28.995 -6.300  1.00 25.89 ? 291  GLN A CA  1 
ATOM   898  C  C   . GLN A 1 291 ? 7.020   -28.272 -5.774  1.00 24.66 ? 291  GLN A C   1 
ATOM   899  O  O   . GLN A 1 291 ? 7.079   -27.896 -4.600  1.00 25.05 ? 291  GLN A O   1 
ATOM   900  C  CB  . GLN A 1 291 ? 4.701   -27.993 -6.757  1.00 25.16 ? 291  GLN A CB  1 
ATOM   901  C  CG  . GLN A 1 291 ? 4.138   -27.155 -5.627  1.00 25.33 ? 291  GLN A CG  1 
ATOM   902  C  CD  . GLN A 1 291 ? 3.088   -26.177 -6.090  1.00 25.41 ? 291  GLN A CD  1 
ATOM   903  O  OE1 . GLN A 1 291 ? 3.270   -25.464 -7.088  1.00 24.39 ? 291  GLN A OE1 1 
ATOM   904  N  NE2 . GLN A 1 291 ? 1.968   -26.137 -5.369  1.00 24.58 ? 291  GLN A NE2 1 
ATOM   905  N  N   . LEU A 1 292 ? 8.010   -28.093 -6.645  1.00 23.83 ? 292  LEU A N   1 
ATOM   906  C  CA  . LEU A 1 292 ? 9.295   -27.490 -6.294  1.00 23.59 ? 292  LEU A CA  1 
ATOM   907  C  C   . LEU A 1 292 ? 9.617   -26.319 -7.222  1.00 23.69 ? 292  LEU A C   1 
ATOM   908  O  O   . LEU A 1 292 ? 9.444   -26.418 -8.446  1.00 23.36 ? 292  LEU A O   1 
ATOM   909  C  CB  . LEU A 1 292 ? 10.414  -28.520 -6.423  1.00 24.12 ? 292  LEU A CB  1 
ATOM   910  C  CG  . LEU A 1 292 ? 10.147  -29.870 -5.749  1.00 24.84 ? 292  LEU A CG  1 
ATOM   911  C  CD1 . LEU A 1 292 ? 11.178  -30.880 -6.193  1.00 25.39 ? 292  LEU A CD1 1 
ATOM   912  C  CD2 . LEU A 1 292 ? 10.152  -29.694 -4.241  1.00 25.27 ? 292  LEU A CD2 1 
ATOM   913  N  N   . VAL A 1 293 ? 10.116  -25.239 -6.633  1.00 22.76 ? 293  VAL A N   1 
ATOM   914  C  CA  . VAL A 1 293 ? 10.470  -24.026 -7.353  1.00 22.45 ? 293  VAL A CA  1 
ATOM   915  C  C   . VAL A 1 293 ? 11.840  -23.556 -6.868  1.00 22.31 ? 293  VAL A C   1 
ATOM   916  O  O   . VAL A 1 293 ? 12.163  -23.646 -5.676  1.00 22.92 ? 293  VAL A O   1 
ATOM   917  C  CB  . VAL A 1 293 ? 9.383   -22.937 -7.162  1.00 22.64 ? 293  VAL A CB  1 
ATOM   918  C  CG1 . VAL A 1 293 ? 9.843   -21.562 -7.632  1.00 23.28 ? 293  VAL A CG1 1 
ATOM   919  C  CG2 . VAL A 1 293 ? 8.117   -23.317 -7.899  1.00 22.79 ? 293  VAL A CG2 1 
ATOM   920  N  N   . ILE A 1 294 ? 12.659  -23.088 -7.805  1.00 21.56 ? 294  ILE A N   1 
ATOM   921  C  CA  . ILE A 1 294 ? 13.941  -22.505 -7.478  1.00 20.96 ? 294  ILE A CA  1 
ATOM   922  C  C   . ILE A 1 294 ? 13.905  -21.020 -7.817  1.00 22.23 ? 294  ILE A C   1 
ATOM   923  O  O   . ILE A 1 294 ? 13.424  -20.626 -8.893  1.00 21.80 ? 294  ILE A O   1 
ATOM   924  C  CB  . ILE A 1 294 ? 15.078  -23.224 -8.197  1.00 21.02 ? 294  ILE A CB  1 
ATOM   925  C  CG1 . ILE A 1 294 ? 15.194  -24.652 -7.639  1.00 21.90 ? 294  ILE A CG1 1 
ATOM   926  C  CG2 . ILE A 1 294 ? 16.377  -22.456 -7.985  1.00 21.15 ? 294  ILE A CG2 1 
ATOM   927  C  CD1 . ILE A 1 294 ? 15.656  -25.680 -8.625  1.00 23.16 ? 294  ILE A CD1 1 
ATOM   928  N  N   . ALA A 1 295 ? 14.413  -20.208 -6.893  1.00 21.44 ? 295  ALA A N   1 
ATOM   929  C  CA  . ALA A 1 295 ? 14.186  -18.775 -6.925  1.00 23.42 ? 295  ALA A CA  1 
ATOM   930  C  C   . ALA A 1 295 ? 15.422  -17.989 -6.521  1.00 23.47 ? 295  ALA A C   1 
ATOM   931  O  O   . ALA A 1 295 ? 16.144  -18.381 -5.612  1.00 23.78 ? 295  ALA A O   1 
ATOM   932  C  CB  . ALA A 1 295 ? 13.021  -18.418 -6.013  1.00 23.10 ? 295  ALA A CB  1 
ATOM   933  N  N   . MET A 1 296 ? 15.654  -16.883 -7.218  1.00 23.42 ? 296  MET A N   1 
ATOM   934  C  CA  . MET A 1 296 ? 16.648  -15.916 -6.808  1.00 23.61 ? 296  MET A CA  1 
ATOM   935  C  C   . MET A 1 296 ? 16.110  -15.101 -5.632  1.00 24.17 ? 296  MET A C   1 
ATOM   936  O  O   . MET A 1 296 ? 14.986  -14.569 -5.685  1.00 22.27 ? 296  MET A O   1 
ATOM   937  C  CB  . MET A 1 296 ? 17.006  -14.995 -7.975  1.00 25.42 ? 296  MET A CB  1 
ATOM   938  C  CG  . MET A 1 296 ? 17.828  -15.682 -9.059  1.00 26.09 ? 296  MET A CG  1 
ATOM   939  S  SD  . MET A 1 296 ? 18.499  -14.518 -10.248 1.00 29.69 ? 296  MET A SD  1 
ATOM   940  C  CE  . MET A 1 296 ? 19.788  -13.738 -9.277  1.00 28.42 ? 296  MET A CE  1 
ATOM   941  N  N   . MET A 1 297 ? 16.899  -15.027 -4.560  1.00 23.55 ? 297  MET A N   1 
ATOM   942  C  CA  . MET A 1 297 ? 16.565  -14.165 -3.443  1.00 25.02 ? 297  MET A CA  1 
ATOM   943  C  C   . MET A 1 297 ? 17.787  -13.377 -2.934  1.00 23.66 ? 297  MET A C   1 
ATOM   944  O  O   . MET A 1 297 ? 18.923  -13.768 -3.130  1.00 22.34 ? 297  MET A O   1 
ATOM   945  C  CB  . MET A 1 297 ? 15.951  -14.986 -2.292  1.00 25.82 ? 297  MET A CB  1 
ATOM   946  C  CG  . MET A 1 297 ? 14.776  -15.886 -2.668  1.00 26.36 ? 297  MET A CG  1 
ATOM   947  S  SD  . MET A 1 297 ? 14.014  -16.538 -1.157  1.00 26.32 ? 297  MET A SD  1 
ATOM   948  C  CE  . MET A 1 297 ? 12.486  -17.242 -1.766  1.00 26.40 ? 297  MET A CE  1 
ATOM   949  N  N   . GLY A 1 298 ? 17.528  -12.261 -2.270  1.00 24.65 ? 298  GLY A N   1 
ATOM   950  C  CA  . GLY A 1 298 ? 18.592  -11.485 -1.641  1.00 25.04 ? 298  GLY A CA  1 
ATOM   951  C  C   . GLY A 1 298 ? 18.056  -10.310 -0.855  1.00 25.46 ? 298  GLY A C   1 
ATOM   952  O  O   . GLY A 1 298 ? 16.914  -9.894  -1.043  1.00 25.29 ? 298  GLY A O   1 
ATOM   953  N  N   . ILE A 1 299 ? 18.891  -9.774  0.028   1.00 26.57 ? 299  ILE A N   1 
ATOM   954  C  CA  . ILE A 1 299 ? 18.525  -8.613  0.829   1.00 27.73 ? 299  ILE A CA  1 
ATOM   955  C  C   . ILE A 1 299 ? 18.406  -7.380  -0.070  1.00 27.16 ? 299  ILE A C   1 
ATOM   956  O  O   . ILE A 1 299 ? 19.339  -7.061  -0.797  1.00 25.79 ? 299  ILE A O   1 
ATOM   957  C  CB  . ILE A 1 299 ? 19.570  -8.335  1.930   1.00 28.54 ? 299  ILE A CB  1 
ATOM   958  C  CG1 . ILE A 1 299 ? 19.581  -9.475  2.964   1.00 29.66 ? 299  ILE A CG1 1 
ATOM   959  C  CG2 . ILE A 1 299 ? 19.274  -7.003  2.619   1.00 28.83 ? 299  ILE A CG2 1 
ATOM   960  C  CD1 . ILE A 1 299 ? 20.862  -9.556  3.779   1.00 30.30 ? 299  ILE A CD1 1 
ATOM   961  N  N   . PRO A 1 300 ? 17.262  -6.677  -0.013  1.00 28.57 ? 300  PRO A N   1 
ATOM   962  C  CA  . PRO A 1 300 ? 17.155  -5.437  -0.788  1.00 29.78 ? 300  PRO A CA  1 
ATOM   963  C  C   . PRO A 1 300 ? 18.363  -4.501  -0.595  1.00 31.02 ? 300  PRO A C   1 
ATOM   964  O  O   . PRO A 1 300 ? 18.833  -4.326  0.529   1.00 30.73 ? 300  PRO A O   1 
ATOM   965  C  CB  . PRO A 1 300 ? 15.876  -4.787  -0.247  1.00 29.22 ? 300  PRO A CB  1 
ATOM   966  C  CG  . PRO A 1 300 ? 15.076  -5.908  0.304   1.00 28.79 ? 300  PRO A CG  1 
ATOM   967  C  CD  . PRO A 1 300 ? 16.052  -6.940  0.791   1.00 28.44 ? 300  PRO A CD  1 
ATOM   968  N  N   . ASN A 1 301 ? 18.861  -3.954  -1.706  1.00 32.00 ? 301  ASN A N   1 
ATOM   969  C  CA  . ASN A 1 301 ? 19.974  -2.988  -1.749  1.00 33.02 ? 301  ASN A CA  1 
ATOM   970  C  C   . ASN A 1 301 ? 21.367  -3.553  -1.458  1.00 34.04 ? 301  ASN A C   1 
ATOM   971  O  O   . ASN A 1 301 ? 22.315  -2.792  -1.340  1.00 37.09 ? 301  ASN A O   1 
ATOM   972  C  CB  . ASN A 1 301 ? 19.709  -1.771  -0.849  1.00 33.99 ? 301  ASN A CB  1 
ATOM   973  C  CG  . ASN A 1 301 ? 18.529  -0.946  -1.316  1.00 34.86 ? 301  ASN A CG  1 
ATOM   974  O  OD1 . ASN A 1 301 ? 17.546  -0.789  -0.597  1.00 37.51 ? 301  ASN A OD1 1 
ATOM   975  N  ND2 . ASN A 1 301 ? 18.623  -0.408  -2.510  1.00 35.04 ? 301  ASN A ND2 1 
ATOM   976  N  N   . GLN A 1 302 ? 21.499  -4.871  -1.359  1.00 32.89 ? 302  GLN A N   1 
ATOM   977  C  CA  . GLN A 1 302 ? 22.806  -5.489  -1.287  1.00 33.98 ? 302  GLN A CA  1 
ATOM   978  C  C   . GLN A 1 302 ? 23.065  -6.245  -2.580  1.00 32.26 ? 302  GLN A C   1 
ATOM   979  O  O   . GLN A 1 302 ? 22.124  -6.633  -3.249  1.00 32.57 ? 302  GLN A O   1 
ATOM   980  C  CB  . GLN A 1 302 ? 22.872  -6.443  -0.097  1.00 35.06 ? 302  GLN A CB  1 
ATOM   981  C  CG  . GLN A 1 302 ? 22.483  -5.759  1.206   1.00 37.47 ? 302  GLN A CG  1 
ATOM   982  C  CD  . GLN A 1 302 ? 22.926  -6.501  2.451   1.00 39.31 ? 302  GLN A CD  1 
ATOM   983  O  OE1 . GLN A 1 302 ? 23.340  -7.659  2.404   1.00 40.06 ? 302  GLN A OE1 1 
ATOM   984  N  NE2 . GLN A 1 302 ? 22.843  -5.821  3.586   1.00 41.56 ? 302  GLN A NE2 1 
ATOM   985  N  N   . ASN A 1 303 ? 24.336  -6.435  -2.930  1.00 31.01 ? 303  ASN A N   1 
ATOM   986  C  CA  . ASN A 1 303 ? 24.705  -7.439  -3.919  1.00 32.82 ? 303  ASN A CA  1 
ATOM   987  C  C   . ASN A 1 303 ? 24.683  -8.820  -3.283  1.00 30.55 ? 303  ASN A C   1 
ATOM   988  O  O   . ASN A 1 303 ? 25.611  -9.211  -2.600  1.00 30.63 ? 303  ASN A O   1 
ATOM   989  C  CB  . ASN A 1 303 ? 26.079  -7.177  -4.528  1.00 34.25 ? 303  ASN A CB  1 
ATOM   990  C  CG  . ASN A 1 303 ? 26.268  -7.924  -5.827  1.00 34.24 ? 303  ASN A CG  1 
ATOM   991  O  OD1 . ASN A 1 303 ? 26.218  -9.150  -5.862  1.00 34.59 ? 303  ASN A OD1 1 
ATOM   992  N  ND2 . ASN A 1 303 ? 26.440  -7.183  -6.917  1.00 35.39 ? 303  ASN A ND2 1 
ATOM   993  N  N   . ASP A 1 304 ? 23.611  -9.557  -3.544  1.00 28.27 ? 304  ASP A N   1 
ATOM   994  C  CA  . ASP A 1 304 ? 23.312  -10.773 -2.820  1.00 25.65 ? 304  ASP A CA  1 
ATOM   995  C  C   . ASP A 1 304 ? 22.480  -11.649 -3.752  1.00 24.64 ? 304  ASP A C   1 
ATOM   996  O  O   . ASP A 1 304 ? 21.261  -11.736 -3.625  1.00 24.28 ? 304  ASP A O   1 
ATOM   997  C  CB  . ASP A 1 304 ? 22.561  -10.393 -1.532  1.00 25.09 ? 304  ASP A CB  1 
ATOM   998  C  CG  . ASP A 1 304 ? 22.181  -11.587 -0.681  1.00 24.69 ? 304  ASP A CG  1 
ATOM   999  O  OD1 . ASP A 1 304 ? 22.744  -12.679 -0.881  1.00 24.99 ? 304  ASP A OD1 1 
ATOM   1000 O  OD2 . ASP A 1 304 ? 21.326  -11.412 0.209   1.00 22.90 ? 304  ASP A OD2 1 
ATOM   1001 N  N   . ASN A 1 305 ? 23.148  -12.266 -4.719  1.00 24.33 ? 305  ASN A N   1 
ATOM   1002 C  CA  . ASN A 1 305 ? 22.452  -12.964 -5.790  1.00 23.72 ? 305  ASN A CA  1 
ATOM   1003 C  C   . ASN A 1 305 ? 22.696  -14.448 -5.667  1.00 22.62 ? 305  ASN A C   1 
ATOM   1004 O  O   . ASN A 1 305 ? 23.712  -14.943 -6.124  1.00 22.96 ? 305  ASN A O   1 
ATOM   1005 C  CB  . ASN A 1 305 ? 22.921  -12.458 -7.151  1.00 24.00 ? 305  ASN A CB  1 
ATOM   1006 C  CG  . ASN A 1 305 ? 22.616  -10.986 -7.360  1.00 24.28 ? 305  ASN A CG  1 
ATOM   1007 O  OD1 . ASN A 1 305 ? 21.466  -10.568 -7.310  1.00 25.18 ? 305  ASN A OD1 1 
ATOM   1008 N  ND2 . ASN A 1 305 ? 23.650  -10.197 -7.598  1.00 23.36 ? 305  ASN A ND2 1 
ATOM   1009 N  N   . HIS A 1 306 ? 21.754  -15.157 -5.048  1.00 21.71 ? 306  HIS A N   1 
ATOM   1010 C  CA  . HIS A 1 306 ? 21.873  -16.600 -4.875  1.00 21.12 ? 306  HIS A CA  1 
ATOM   1011 C  C   . HIS A 1 306 ? 20.520  -17.280 -5.030  1.00 21.10 ? 306  HIS A C   1 
ATOM   1012 O  O   . HIS A 1 306 ? 19.466  -16.622 -4.976  1.00 20.18 ? 306  HIS A O   1 
ATOM   1013 C  CB  . HIS A 1 306 ? 22.528  -16.904 -3.516  1.00 20.75 ? 306  HIS A CB  1 
ATOM   1014 C  CG  . HIS A 1 306 ? 23.891  -16.299 -3.381  1.00 19.93 ? 306  HIS A CG  1 
ATOM   1015 N  ND1 . HIS A 1 306 ? 25.016  -16.878 -3.924  1.00 20.14 ? 306  HIS A ND1 1 
ATOM   1016 C  CD2 . HIS A 1 306 ? 24.296  -15.128 -2.835  1.00 19.74 ? 306  HIS A CD2 1 
ATOM   1017 C  CE1 . HIS A 1 306 ? 26.060  -16.102 -3.693  1.00 20.22 ? 306  HIS A CE1 1 
ATOM   1018 N  NE2 . HIS A 1 306 ? 25.653  -15.038 -3.023  1.00 19.44 ? 306  HIS A NE2 1 
ATOM   1019 N  N   . ILE A 1 307 ? 20.548  -18.588 -5.253  1.00 21.45 ? 307  ILE A N   1 
ATOM   1020 C  CA  . ILE A 1 307 ? 19.307  -19.324 -5.519  1.00 23.25 ? 307  ILE A CA  1 
ATOM   1021 C  C   . ILE A 1 307 ? 18.950  -20.221 -4.352  1.00 24.67 ? 307  ILE A C   1 
ATOM   1022 O  O   . ILE A 1 307 ? 19.836  -20.813 -3.714  1.00 25.51 ? 307  ILE A O   1 
ATOM   1023 C  CB  . ILE A 1 307 ? 19.342  -20.164 -6.827  1.00 22.55 ? 307  ILE A CB  1 
ATOM   1024 C  CG1 . ILE A 1 307 ? 20.499  -21.172 -6.819  1.00 23.68 ? 307  ILE A CG1 1 
ATOM   1025 C  CG2 . ILE A 1 307 ? 19.431  -19.234 -8.027  1.00 23.04 ? 307  ILE A CG2 1 
ATOM   1026 C  CD1 . ILE A 1 307 ? 20.593  -22.023 -8.074  1.00 24.00 ? 307  ILE A CD1 1 
ATOM   1027 N  N   . TYR A 1 308 ? 17.648  -20.322 -4.111  1.00 24.30 ? 308  TYR A N   1 
ATOM   1028 C  CA  . TYR A 1 308 ? 17.107  -21.064 -2.991  1.00 24.95 ? 308  TYR A CA  1 
ATOM   1029 C  C   . TYR A 1 308 ? 16.093  -22.045 -3.533  1.00 24.72 ? 308  TYR A C   1 
ATOM   1030 O  O   . TYR A 1 308 ? 15.421  -21.756 -4.523  1.00 25.72 ? 308  TYR A O   1 
ATOM   1031 C  CB  . TYR A 1 308 ? 16.425  -20.108 -2.009  1.00 26.14 ? 308  TYR A CB  1 
ATOM   1032 C  CG  . TYR A 1 308 ? 17.348  -19.084 -1.372  1.00 26.57 ? 308  TYR A CG  1 
ATOM   1033 C  CD1 . TYR A 1 308 ? 17.881  -18.033 -2.124  1.00 26.68 ? 308  TYR A CD1 1 
ATOM   1034 C  CD2 . TYR A 1 308 ? 17.678  -19.154 -0.008  1.00 26.95 ? 308  TYR A CD2 1 
ATOM   1035 C  CE1 . TYR A 1 308 ? 18.730  -17.098 -1.551  1.00 26.28 ? 308  TYR A CE1 1 
ATOM   1036 C  CE2 . TYR A 1 308 ? 18.518  -18.214 0.580   1.00 26.12 ? 308  TYR A CE2 1 
ATOM   1037 C  CZ  . TYR A 1 308 ? 19.034  -17.184 -0.193  1.00 27.13 ? 308  TYR A CZ  1 
ATOM   1038 O  OH  . TYR A 1 308 ? 19.865  -16.227 0.366   1.00 26.89 ? 308  TYR A OH  1 
ATOM   1039 N  N   . LEU A 1 309 ? 15.998  -23.207 -2.904  1.00 24.09 ? 309  LEU A N   1 
ATOM   1040 C  CA  . LEU A 1 309 ? 14.990  -24.193 -3.252  1.00 24.21 ? 309  LEU A CA  1 
ATOM   1041 C  C   . LEU A 1 309 ? 13.752  -24.051 -2.369  1.00 25.38 ? 309  LEU A C   1 
ATOM   1042 O  O   . LEU A 1 309 ? 13.867  -23.991 -1.136  1.00 26.24 ? 309  LEU A O   1 
ATOM   1043 C  CB  . LEU A 1 309 ? 15.568  -25.590 -3.114  1.00 24.36 ? 309  LEU A CB  1 
ATOM   1044 C  CG  . LEU A 1 309 ? 14.608  -26.744 -3.356  1.00 25.36 ? 309  LEU A CG  1 
ATOM   1045 C  CD1 . LEU A 1 309 ? 14.141  -26.791 -4.805  1.00 25.51 ? 309  LEU A CD1 1 
ATOM   1046 C  CD2 . LEU A 1 309 ? 15.290  -28.041 -2.949  1.00 25.91 ? 309  LEU A CD2 1 
ATOM   1047 N  N   . LEU A 1 310 ? 12.578  -24.009 -3.006  1.00 25.40 ? 310  LEU A N   1 
ATOM   1048 C  CA  . LEU A 1 310 ? 11.290  -23.860 -2.324  1.00 26.80 ? 310  LEU A CA  1 
ATOM   1049 C  C   . LEU A 1 310 ? 10.386  -25.051 -2.634  1.00 27.62 ? 310  LEU A C   1 
ATOM   1050 O  O   . LEU A 1 310 ? 10.509  -25.681 -3.695  1.00 26.46 ? 310  LEU A O   1 
ATOM   1051 C  CB  . LEU A 1 310 ? 10.580  -22.595 -2.792  1.00 28.13 ? 310  LEU A CB  1 
ATOM   1052 C  CG  . LEU A 1 310 ? 10.960  -21.226 -2.231  1.00 30.65 ? 310  LEU A CG  1 
ATOM   1053 C  CD1 . LEU A 1 310 ? 12.450  -21.048 -2.021  1.00 30.03 ? 310  LEU A CD1 1 
ATOM   1054 C  CD2 . LEU A 1 310 ? 10.407  -20.153 -3.160  1.00 31.62 ? 310  LEU A CD2 1 
ATOM   1055 N  N   . TYR A 1 311 ? 9.465   -25.348 -1.723  1.00 27.58 ? 311  TYR A N   1 
ATOM   1056 C  CA  . TYR A 1 311 ? 8.520   -26.437 -1.933  1.00 29.49 ? 311  TYR A CA  1 
ATOM   1057 C  C   . TYR A 1 311 ? 7.151   -26.149 -1.352  1.00 28.13 ? 311  TYR A C   1 
ATOM   1058 O  O   . TYR A 1 311 ? 6.979   -25.236 -0.573  1.00 28.75 ? 311  TYR A O   1 
ATOM   1059 C  CB  . TYR A 1 311 ? 9.060   -27.750 -1.357  1.00 31.90 ? 311  TYR A CB  1 
ATOM   1060 C  CG  . TYR A 1 311 ? 9.176   -27.810 0.161   1.00 34.08 ? 311  TYR A CG  1 
ATOM   1061 C  CD1 . TYR A 1 311 ? 10.274  -27.263 0.815   1.00 35.34 ? 311  TYR A CD1 1 
ATOM   1062 C  CD2 . TYR A 1 311 ? 8.204   -28.456 0.932   1.00 36.17 ? 311  TYR A CD2 1 
ATOM   1063 C  CE1 . TYR A 1 311 ? 10.403  -27.340 2.196   1.00 37.71 ? 311  TYR A CE1 1 
ATOM   1064 C  CE2 . TYR A 1 311 ? 8.323   -28.543 2.311   1.00 37.45 ? 311  TYR A CE2 1 
ATOM   1065 C  CZ  . TYR A 1 311 ? 9.421   -27.982 2.938   1.00 38.32 ? 311  TYR A CZ  1 
ATOM   1066 O  OH  . TYR A 1 311 ? 9.544   -28.055 4.304   1.00 42.43 ? 311  TYR A OH  1 
ATOM   1067 N  N   . ASN A 1 312 ? 6.183   -26.942 -1.778  1.00 29.32 ? 312  ASN A N   1 
ATOM   1068 C  CA  . ASN A 1 312 ? 4.800   -26.846 -1.329  1.00 29.40 ? 312  ASN A CA  1 
ATOM   1069 C  C   . ASN A 1 312 ? 4.129   -28.164 -1.712  1.00 30.72 ? 312  ASN A C   1 
ATOM   1070 O  O   . ASN A 1 312 ? 4.688   -28.928 -2.498  1.00 29.44 ? 312  ASN A O   1 
ATOM   1071 C  CB  . ASN A 1 312 ? 4.102   -25.665 -2.015  1.00 29.62 ? 312  ASN A CB  1 
ATOM   1072 C  CG  . ASN A 1 312 ? 2.767   -25.325 -1.390  1.00 27.53 ? 312  ASN A CG  1 
ATOM   1073 O  OD1 . ASN A 1 312 ? 2.244   -26.070 -0.572  1.00 25.08 ? 312  ASN A OD1 1 
ATOM   1074 N  ND2 . ASN A 1 312 ? 2.210   -24.189 -1.778  1.00 27.36 ? 312  ASN A ND2 1 
ATOM   1075 N  N   . LYS A 1 313 ? 2.963   -28.450 -1.133  1.00 32.66 ? 313  LYS A N   1 
ATOM   1076 C  CA  . LYS A 1 313 ? 2.176   -29.612 -1.539  1.00 35.40 ? 313  LYS A CA  1 
ATOM   1077 C  C   . LYS A 1 313 ? 1.702   -29.356 -2.967  1.00 33.99 ? 313  LYS A C   1 
ATOM   1078 O  O   . LYS A 1 313 ? 1.253   -28.250 -3.293  1.00 31.52 ? 313  LYS A O   1 
ATOM   1079 C  CB  . LYS A 1 313 ? 0.976   -29.849 -0.608  1.00 37.86 ? 313  LYS A CB  1 
ATOM   1080 C  CG  . LYS A 1 313 ? 1.313   -30.564 0.700   1.00 41.29 ? 313  LYS A CG  1 
ATOM   1081 C  CD  . LYS A 1 313 ? 1.411   -32.074 0.495   1.00 44.25 ? 313  LYS A CD  1 
ATOM   1082 C  CE  . LYS A 1 313 ? 2.163   -32.778 1.617   1.00 46.45 ? 313  LYS A CE  1 
ATOM   1083 N  NZ  . LYS A 1 313 ? 2.952   -33.932 1.086   1.00 47.21 ? 313  LYS A NZ  1 
ATOM   1084 N  N   . TYR A 1 314 ? 1.821   -30.371 -3.813  1.00 31.96 ? 314  TYR A N   1 
ATOM   1085 C  CA  . TYR A 1 314 ? 1.386   -30.244 -5.182  1.00 31.59 ? 314  TYR A CA  1 
ATOM   1086 C  C   . TYR A 1 314 ? -0.098  -29.838 -5.267  1.00 31.62 ? 314  TYR A C   1 
ATOM   1087 O  O   . TYR A 1 314 ? -0.974  -30.480 -4.673  1.00 28.64 ? 314  TYR A O   1 
ATOM   1088 C  CB  . TYR A 1 314 ? 1.647   -31.537 -5.941  1.00 33.05 ? 314  TYR A CB  1 
ATOM   1089 C  CG  . TYR A 1 314 ? 1.392   -31.400 -7.415  1.00 34.30 ? 314  TYR A CG  1 
ATOM   1090 C  CD1 . TYR A 1 314 ? 0.111   -31.533 -7.921  1.00 35.50 ? 314  TYR A CD1 1 
ATOM   1091 C  CD2 . TYR A 1 314 ? 2.423   -31.102 -8.299  1.00 34.26 ? 314  TYR A CD2 1 
ATOM   1092 C  CE1 . TYR A 1 314 ? -0.142  -31.406 -9.270  1.00 37.32 ? 314  TYR A CE1 1 
ATOM   1093 C  CE2 . TYR A 1 314 ? 2.179   -30.970 -9.659  1.00 35.36 ? 314  TYR A CE2 1 
ATOM   1094 C  CZ  . TYR A 1 314 ? 0.891   -31.124 -10.131 1.00 35.39 ? 314  TYR A CZ  1 
ATOM   1095 O  OH  . TYR A 1 314 ? 0.595   -31.000 -11.457 1.00 38.26 ? 314  TYR A OH  1 
ATOM   1096 N  N   . GLY A 1 315 ? -0.364  -28.751 -5.992  1.00 29.48 ? 315  GLY A N   1 
ATOM   1097 C  CA  . GLY A 1 315 ? -1.725  -28.262 -6.197  1.00 29.15 ? 315  GLY A CA  1 
ATOM   1098 C  C   . GLY A 1 315 ? -2.152  -27.203 -5.202  1.00 28.64 ? 315  GLY A C   1 
ATOM   1099 O  O   . GLY A 1 315 ? -3.176  -26.555 -5.390  1.00 31.80 ? 315  GLY A O   1 
ATOM   1100 N  N   . ASP A 1 316 ? -1.369  -27.003 -4.151  1.00 28.41 ? 316  ASP A N   1 
ATOM   1101 C  CA  . ASP A 1 316 ? -1.720  -26.055 -3.100  1.00 28.63 ? 316  ASP A CA  1 
ATOM   1102 C  C   . ASP A 1 316 ? -1.624  -24.637 -3.638  1.00 28.63 ? 316  ASP A C   1 
ATOM   1103 O  O   . ASP A 1 316 ? -0.636  -24.288 -4.275  1.00 28.72 ? 316  ASP A O   1 
ATOM   1104 C  CB  . ASP A 1 316 ? -0.763  -26.218 -1.928  1.00 29.00 ? 316  ASP A CB  1 
ATOM   1105 C  CG  . ASP A 1 316 ? -1.026  -25.244 -0.819  1.00 29.85 ? 316  ASP A CG  1 
ATOM   1106 O  OD1 . ASP A 1 316 ? -0.707  -24.038 -0.963  1.00 28.61 ? 316  ASP A OD1 1 
ATOM   1107 O  OD2 . ASP A 1 316 ? -1.538  -25.695 0.229   1.00 32.89 ? 316  ASP A OD2 1 
ATOM   1108 N  N   . ASN A 1 317 ? -2.625  -23.817 -3.343  1.00 28.11 ? 317  ASN A N   1 
ATOM   1109 C  CA  . ASN A 1 317 ? -2.709  -22.476 -3.907  1.00 28.56 ? 317  ASN A CA  1 
ATOM   1110 C  C   . ASN A 1 317 ? -2.354  -21.341 -2.984  1.00 27.54 ? 317  ASN A C   1 
ATOM   1111 O  O   . ASN A 1 317 ? -2.602  -20.187 -3.327  1.00 28.31 ? 317  ASN A O   1 
ATOM   1112 C  CB  . ASN A 1 317 ? -4.123  -22.245 -4.438  1.00 28.55 ? 317  ASN A CB  1 
ATOM   1113 C  CG  . ASN A 1 317 ? -4.477  -23.209 -5.526  1.00 27.06 ? 317  ASN A CG  1 
ATOM   1114 O  OD1 . ASN A 1 317 ? -3.603  -23.658 -6.269  1.00 28.16 ? 317  ASN A OD1 1 
ATOM   1115 N  ND2 . ASN A 1 317 ? -5.738  -23.566 -5.610  1.00 25.67 ? 317  ASN A ND2 1 
ATOM   1116 N  N   . GLU A 1 318 ? -1.776  -21.634 -1.827  1.00 28.00 ? 318  GLU A N   1 
ATOM   1117 C  CA  . GLU A 1 318 ? -1.531  -20.580 -0.853  1.00 29.77 ? 318  GLU A CA  1 
ATOM   1118 C  C   . GLU A 1 318 ? -0.078  -20.137 -0.904  1.00 28.68 ? 318  GLU A C   1 
ATOM   1119 O  O   . GLU A 1 318 ? 0.832   -20.946 -0.734  1.00 27.83 ? 318  GLU A O   1 
ATOM   1120 C  CB  . GLU A 1 318 ? -1.931  -21.019 0.570   1.00 32.45 ? 318  GLU A CB  1 
ATOM   1121 C  CG  . GLU A 1 318 ? -3.381  -21.490 0.720   1.00 35.02 ? 318  GLU A CG  1 
ATOM   1122 C  CD  . GLU A 1 318 ? -4.417  -20.462 0.277   1.00 37.64 ? 318  GLU A CD  1 
ATOM   1123 O  OE1 . GLU A 1 318 ? -4.201  -19.245 0.494   1.00 40.40 ? 318  GLU A OE1 1 
ATOM   1124 O  OE2 . GLU A 1 318 ? -5.458  -20.875 -0.292  1.00 41.05 ? 318  GLU A OE2 1 
ATOM   1125 N  N   . LEU A 1 319 ? 0.135   -18.845 -1.139  1.00 27.31 ? 319  LEU A N   1 
ATOM   1126 C  CA  . LEU A 1 319 ? 1.469   -18.298 -1.143  1.00 27.77 ? 319  LEU A CA  1 
ATOM   1127 C  C   . LEU A 1 319 ? 2.191   -18.641 0.157   1.00 27.89 ? 319  LEU A C   1 
ATOM   1128 O  O   . LEU A 1 319 ? 3.352   -19.029 0.150   1.00 29.23 ? 319  LEU A O   1 
ATOM   1129 C  CB  . LEU A 1 319 ? 1.425   -16.780 -1.309  1.00 27.65 ? 319  LEU A CB  1 
ATOM   1130 C  CG  . LEU A 1 319 ? 2.803   -16.098 -1.338  1.00 28.21 ? 319  LEU A CG  1 
ATOM   1131 C  CD1 . LEU A 1 319 ? 3.576   -16.553 -2.568  1.00 28.26 ? 319  LEU A CD1 1 
ATOM   1132 C  CD2 . LEU A 1 319 ? 2.663   -14.578 -1.309  1.00 28.09 ? 319  LEU A CD2 1 
ATOM   1133 N  N   . SER A 1 320 ? 1.496   -18.491 1.275   1.00 28.53 ? 320  SER A N   1 
ATOM   1134 C  CA  . SER A 1 320 ? 2.117   -18.699 2.579   1.00 29.02 ? 320  SER A CA  1 
ATOM   1135 C  C   . SER A 1 320 ? 2.445   -20.158 2.899   1.00 29.22 ? 320  SER A C   1 
ATOM   1136 O  O   . SER A 1 320 ? 3.119   -20.409 3.894   1.00 31.40 ? 320  SER A O   1 
ATOM   1137 C  CB  . SER A 1 320 ? 1.242   -18.097 3.695   1.00 28.44 ? 320  SER A CB  1 
ATOM   1138 O  OG  . SER A 1 320 ? -0.027  -18.722 3.725   1.00 29.44 ? 320  SER A OG  1 
ATOM   1139 N  N   . HIS A 1 321 ? 1.982   -21.117 2.090   1.00 29.20 ? 321  HIS A N   1 
ATOM   1140 C  CA  . HIS A 1 321 ? 2.317   -22.535 2.322   1.00 29.24 ? 321  HIS A CA  1 
ATOM   1141 C  C   . HIS A 1 321 ? 3.650   -22.945 1.723   1.00 29.69 ? 321  HIS A C   1 
ATOM   1142 O  O   . HIS A 1 321 ? 4.151   -24.028 2.021   1.00 28.37 ? 321  HIS A O   1 
ATOM   1143 C  CB  . HIS A 1 321 ? 1.241   -23.469 1.779   1.00 29.90 ? 321  HIS A CB  1 
ATOM   1144 C  CG  . HIS A 1 321 ? -0.025  -23.468 2.578   1.00 30.24 ? 321  HIS A CG  1 
ATOM   1145 N  ND1 . HIS A 1 321 ? -1.140  -24.181 2.199   1.00 30.59 ? 321  HIS A ND1 1 
ATOM   1146 C  CD2 . HIS A 1 321 ? -0.360  -22.831 3.724   1.00 31.54 ? 321  HIS A CD2 1 
ATOM   1147 C  CE1 . HIS A 1 321 ? -2.103  -23.996 3.084   1.00 31.74 ? 321  HIS A CE1 1 
ATOM   1148 N  NE2 . HIS A 1 321 ? -1.657  -23.176 4.016   1.00 32.33 ? 321  HIS A NE2 1 
ATOM   1149 N  N   . TRP A 1 322 ? 4.214   -22.106 0.853   1.00 28.34 ? 322  TRP A N   1 
ATOM   1150 C  CA  . TRP A 1 322 ? 5.534   -22.388 0.316   1.00 27.52 ? 322  TRP A CA  1 
ATOM   1151 C  C   . TRP A 1 322 ? 6.572   -22.359 1.442   1.00 28.19 ? 322  TRP A C   1 
ATOM   1152 O  O   . TRP A 1 322 ? 6.477   -21.536 2.353   1.00 26.94 ? 322  TRP A O   1 
ATOM   1153 C  CB  . TRP A 1 322 ? 5.881   -21.390 -0.794  1.00 26.87 ? 322  TRP A CB  1 
ATOM   1154 C  CG  . TRP A 1 322 ? 5.166   -21.706 -2.084  1.00 25.57 ? 322  TRP A CG  1 
ATOM   1155 C  CD1 . TRP A 1 322 ? 3.952   -21.226 -2.502  1.00 25.36 ? 322  TRP A CD1 1 
ATOM   1156 C  CD2 . TRP A 1 322 ? 5.612   -22.605 -3.098  1.00 25.98 ? 322  TRP A CD2 1 
ATOM   1157 N  NE1 . TRP A 1 322 ? 3.622   -21.765 -3.724  1.00 25.08 ? 322  TRP A NE1 1 
ATOM   1158 C  CE2 . TRP A 1 322 ? 4.627   -22.613 -4.115  1.00 25.81 ? 322  TRP A CE2 1 
ATOM   1159 C  CE3 . TRP A 1 322 ? 6.753   -23.402 -3.253  1.00 24.94 ? 322  TRP A CE3 1 
ATOM   1160 C  CZ2 . TRP A 1 322 ? 4.761   -23.371 -5.269  1.00 25.47 ? 322  TRP A CZ2 1 
ATOM   1161 C  CZ3 . TRP A 1 322 ? 6.873   -24.173 -4.392  1.00 24.82 ? 322  TRP A CZ3 1 
ATOM   1162 C  CH2 . TRP A 1 322 ? 5.888   -24.148 -5.390  1.00 25.45 ? 322  TRP A CH2 1 
ATOM   1163 N  N   . LYS A 1 323 ? 7.548   -23.267 1.379   1.00 29.35 ? 323  LYS A N   1 
ATOM   1164 C  CA  . LYS A 1 323 ? 8.605   -23.354 2.393   1.00 30.75 ? 323  LYS A CA  1 
ATOM   1165 C  C   . LYS A 1 323 ? 9.994   -23.273 1.774   1.00 28.59 ? 323  LYS A C   1 
ATOM   1166 O  O   . LYS A 1 323 ? 10.269  -23.869 0.732   1.00 26.20 ? 323  LYS A O   1 
ATOM   1167 C  CB  . LYS A 1 323 ? 8.455   -24.641 3.226   1.00 32.90 ? 323  LYS A CB  1 
ATOM   1168 C  CG  . LYS A 1 323 ? 7.398   -24.488 4.313   1.00 36.30 ? 323  LYS A CG  1 
ATOM   1169 C  CD  . LYS A 1 323 ? 7.300   -25.704 5.233   1.00 39.94 ? 323  LYS A CD  1 
ATOM   1170 C  CE  . LYS A 1 323 ? 6.338   -26.750 4.680   1.00 43.21 ? 323  LYS A CE  1 
ATOM   1171 N  NZ  . LYS A 1 323 ? 6.251   -27.990 5.516   1.00 45.64 ? 323  LYS A NZ  1 
ATOM   1172 N  N   . ASN A 1 324 ? 10.863  -22.511 2.423   1.00 26.94 ? 324  ASN A N   1 
ATOM   1173 C  CA  . ASN A 1 324 ? 12.205  -22.320 1.924   1.00 26.94 ? 324  ASN A CA  1 
ATOM   1174 C  C   . ASN A 1 324 ? 13.140  -23.358 2.519   1.00 27.44 ? 324  ASN A C   1 
ATOM   1175 O  O   . ASN A 1 324 ? 13.353  -23.376 3.730   1.00 28.38 ? 324  ASN A O   1 
ATOM   1176 C  CB  . ASN A 1 324 ? 12.687  -20.907 2.224   1.00 25.96 ? 324  ASN A CB  1 
ATOM   1177 C  CG  . ASN A 1 324 ? 13.778  -20.450 1.265   1.00 25.70 ? 324  ASN A CG  1 
ATOM   1178 O  OD1 . ASN A 1 324 ? 14.659  -21.229 0.904   1.00 24.93 ? 324  ASN A OD1 1 
ATOM   1179 N  ND2 . ASN A 1 324 ? 13.727  -19.175 0.853   1.00 25.21 ? 324  ASN A ND2 1 
ATOM   1180 N  N   . VAL A 1 325 ? 13.664  -24.234 1.665   1.00 26.87 ? 325  VAL A N   1 
ATOM   1181 C  CA  . VAL A 1 325 ? 14.636  -25.235 2.071   1.00 27.90 ? 325  VAL A CA  1 
ATOM   1182 C  C   . VAL A 1 325 ? 15.966  -24.574 2.427   1.00 29.17 ? 325  VAL A C   1 
ATOM   1183 O  O   . VAL A 1 325 ? 16.674  -25.040 3.320   1.00 29.07 ? 325  VAL A O   1 
ATOM   1184 C  CB  . VAL A 1 325 ? 14.916  -26.255 0.953   1.00 28.10 ? 325  VAL A CB  1 
ATOM   1185 C  CG1 . VAL A 1 325 ? 16.024  -27.223 1.379   1.00 29.40 ? 325  VAL A CG1 1 
ATOM   1186 C  CG2 . VAL A 1 325 ? 13.646  -26.987 0.571   1.00 27.46 ? 325  VAL A CG2 1 
ATOM   1187 N  N   . GLY A 1 326 ? 16.303  -23.497 1.727   1.00 28.73 ? 326  GLY A N   1 
ATOM   1188 C  CA  . GLY A 1 326 ? 17.581  -22.818 1.921   1.00 29.13 ? 326  GLY A CA  1 
ATOM   1189 C  C   . GLY A 1 326 ? 18.330  -22.614 0.606   1.00 28.99 ? 326  GLY A C   1 
ATOM   1190 O  O   . GLY A 1 326 ? 17.884  -23.078 -0.456  1.00 27.19 ? 326  GLY A O   1 
ATOM   1191 N  N   . PRO A 1 327 ? 19.473  -21.914 0.667   1.00 28.28 ? 327  PRO A N   1 
ATOM   1192 C  CA  . PRO A 1 327 ? 20.284  -21.654 -0.528  1.00 27.70 ? 327  PRO A CA  1 
ATOM   1193 C  C   . PRO A 1 327 ? 20.912  -22.921 -1.038  1.00 27.54 ? 327  PRO A C   1 
ATOM   1194 O  O   . PRO A 1 327 ? 21.593  -23.594 -0.275  1.00 27.62 ? 327  PRO A O   1 
ATOM   1195 C  CB  . PRO A 1 327 ? 21.359  -20.684 -0.037  1.00 27.62 ? 327  PRO A CB  1 
ATOM   1196 C  CG  . PRO A 1 327 ? 21.398  -20.855 1.453   1.00 28.08 ? 327  PRO A CG  1 
ATOM   1197 C  CD  . PRO A 1 327 ? 20.040  -21.300 1.881   1.00 27.72 ? 327  PRO A CD  1 
ATOM   1198 N  N   . ILE A 1 328 ? 20.697  -23.241 -2.314  1.00 26.08 ? 328  ILE A N   1 
ATOM   1199 C  CA  . ILE A 1 328 ? 21.190  -24.490 -2.894  1.00 26.42 ? 328  ILE A CA  1 
ATOM   1200 C  C   . ILE A 1 328 ? 22.710  -24.659 -2.741  1.00 26.71 ? 328  ILE A C   1 
ATOM   1201 O  O   . ILE A 1 328 ? 23.185  -25.770 -2.508  1.00 27.50 ? 328  ILE A O   1 
ATOM   1202 C  CB  . ILE A 1 328 ? 20.775  -24.617 -4.389  1.00 26.74 ? 328  ILE A CB  1 
ATOM   1203 C  CG1 . ILE A 1 328 ? 19.267  -24.863 -4.493  1.00 27.11 ? 328  ILE A CG1 1 
ATOM   1204 C  CG2 . ILE A 1 328 ? 21.522  -25.745 -5.093  1.00 25.86 ? 328  ILE A CG2 1 
ATOM   1205 C  CD1 . ILE A 1 328 ? 18.640  -24.362 -5.779  1.00 27.42 ? 328  ILE A CD1 1 
ATOM   1206 N  N   . PHE A 1 329 ? 23.473  -23.575 -2.876  1.00 26.36 ? 329  PHE A N   1 
ATOM   1207 C  CA  . PHE A 1 329 ? 24.926  -23.664 -2.779  1.00 26.37 ? 329  PHE A CA  1 
ATOM   1208 C  C   . PHE A 1 329 ? 25.462  -23.234 -1.409  1.00 26.95 ? 329  PHE A C   1 
ATOM   1209 O  O   . PHE A 1 329 ? 26.656  -23.039 -1.240  1.00 28.04 ? 329  PHE A O   1 
ATOM   1210 C  CB  . PHE A 1 329 ? 25.578  -22.893 -3.928  1.00 26.80 ? 329  PHE A CB  1 
ATOM   1211 C  CG  . PHE A 1 329 ? 25.443  -23.598 -5.243  1.00 27.07 ? 329  PHE A CG  1 
ATOM   1212 C  CD1 . PHE A 1 329 ? 26.297  -24.641 -5.570  1.00 26.57 ? 329  PHE A CD1 1 
ATOM   1213 C  CD2 . PHE A 1 329 ? 24.427  -23.269 -6.123  1.00 26.25 ? 329  PHE A CD2 1 
ATOM   1214 C  CE1 . PHE A 1 329 ? 26.161  -25.325 -6.762  1.00 26.47 ? 329  PHE A CE1 1 
ATOM   1215 C  CE2 . PHE A 1 329 ? 24.288  -23.953 -7.320  1.00 26.38 ? 329  PHE A CE2 1 
ATOM   1216 C  CZ  . PHE A 1 329 ? 25.158  -24.980 -7.640  1.00 26.36 ? 329  PHE A CZ  1 
ATOM   1217 N  N   . GLY A 1 330 ? 24.563  -23.106 -0.442  1.00 26.74 ? 330  GLY A N   1 
ATOM   1218 C  CA  . GLY A 1 330 ? 24.937  -23.074 0.961   1.00 27.71 ? 330  GLY A CA  1 
ATOM   1219 C  C   . GLY A 1 330 ? 25.054  -21.683 1.545   1.00 28.54 ? 330  GLY A C   1 
ATOM   1220 O  O   . GLY A 1 330 ? 24.917  -20.652 0.850   1.00 25.34 ? 330  GLY A O   1 
ATOM   1221 N  N   . TYR A 1 331 ? 25.314  -21.672 2.846   1.00 28.78 ? 331  TYR A N   1 
ATOM   1222 C  CA  . TYR A 1 331 ? 25.549  -20.455 3.586   1.00 30.85 ? 331  TYR A CA  1 
ATOM   1223 C  C   . TYR A 1 331 ? 27.023  -20.110 3.465   1.00 31.63 ? 331  TYR A C   1 
ATOM   1224 O  O   . TYR A 1 331 ? 27.768  -20.815 2.791   1.00 33.62 ? 331  TYR A O   1 
ATOM   1225 C  CB  . TYR A 1 331 ? 25.082  -20.642 5.029   1.00 31.21 ? 331  TYR A CB  1 
ATOM   1226 C  CG  . TYR A 1 331 ? 23.609  -20.955 5.084   1.00 30.74 ? 331  TYR A CG  1 
ATOM   1227 C  CD1 . TYR A 1 331 ? 22.671  -19.949 4.909   1.00 30.83 ? 331  TYR A CD1 1 
ATOM   1228 C  CD2 . TYR A 1 331 ? 23.148  -22.263 5.274   1.00 31.32 ? 331  TYR A CD2 1 
ATOM   1229 C  CE1 . TYR A 1 331 ? 21.316  -20.218 4.940   1.00 29.88 ? 331  TYR A CE1 1 
ATOM   1230 C  CE2 . TYR A 1 331 ? 21.790  -22.539 5.311   1.00 31.32 ? 331  TYR A CE2 1 
ATOM   1231 C  CZ  . TYR A 1 331 ? 20.879  -21.506 5.135   1.00 31.10 ? 331  TYR A CZ  1 
ATOM   1232 O  OH  . TYR A 1 331 ? 19.514  -21.745 5.166   1.00 33.41 ? 331  TYR A OH  1 
ATOM   1233 N  N   . ASN A 1 332 ? 27.440  -19.006 4.067   1.00 33.56 ? 332  ASN A N   1 
ATOM   1234 C  CA  . ASN A 1 332 ? 28.814  -18.513 3.892   1.00 34.24 ? 332  ASN A CA  1 
ATOM   1235 C  C   . ASN A 1 332 ? 29.177  -18.252 2.434   1.00 35.91 ? 332  ASN A C   1 
ATOM   1236 O  O   . ASN A 1 332 ? 30.330  -18.412 2.040   1.00 38.49 ? 332  ASN A O   1 
ATOM   1237 C  CB  . ASN A 1 332 ? 29.814  -19.494 4.498   1.00 34.51 ? 332  ASN A CB  1 
ATOM   1238 C  CG  . ASN A 1 332 ? 29.590  -19.696 5.971   1.00 32.73 ? 332  ASN A CG  1 
ATOM   1239 O  OD1 . ASN A 1 332 ? 29.509  -18.736 6.716   1.00 33.65 ? 332  ASN A OD1 1 
ATOM   1240 N  ND2 . ASN A 1 332 ? 29.491  -20.944 6.397   1.00 32.50 ? 332  ASN A ND2 1 
ATOM   1241 N  N   . SER A 1 333 ? 28.194  -17.842 1.638   1.00 35.18 ? 333  SER A N   1 
ATOM   1242 C  CA  . SER A 1 333 ? 28.428  -17.476 0.237   1.00 34.72 ? 333  SER A CA  1 
ATOM   1243 C  C   . SER A 1 333 ? 28.828  -16.012 0.200   1.00 34.14 ? 333  SER A C   1 
ATOM   1244 O  O   . SER A 1 333 ? 28.649  -15.301 1.184   1.00 33.69 ? 333  SER A O   1 
ATOM   1245 C  CB  . SER A 1 333 ? 27.148  -17.663 -0.583  1.00 34.89 ? 333  SER A CB  1 
ATOM   1246 O  OG  . SER A 1 333 ? 26.661  -18.985 -0.458  1.00 37.26 ? 333  SER A OG  1 
ATOM   1247 N  N   . THR A 1 334 ? 29.357  -15.565 -0.936  1.00 33.68 ? 334  THR A N   1 
ATOM   1248 C  CA  . THR A 1 334 ? 29.772  -14.166 -1.123  1.00 32.76 ? 334  THR A CA  1 
ATOM   1249 C  C   . THR A 1 334 ? 29.407  -13.714 -2.525  1.00 31.72 ? 334  THR A C   1 
ATOM   1250 O  O   . THR A 1 334 ? 29.030  -14.528 -3.369  1.00 31.30 ? 334  THR A O   1 
ATOM   1251 C  CB  . THR A 1 334 ? 31.304  -13.966 -0.937  1.00 32.19 ? 334  THR A CB  1 
ATOM   1252 O  OG1 . THR A 1 334 ? 32.024  -14.667 -1.959  1.00 31.45 ? 334  THR A OG1 1 
ATOM   1253 C  CG2 . THR A 1 334 ? 31.761  -14.457 0.424   1.00 32.25 ? 334  THR A CG2 1 
ATOM   1254 N  N   . ALA A 1 335 ? 29.548  -12.415 -2.769  1.00 31.43 ? 335  ALA A N   1 
ATOM   1255 C  CA  . ALA A 1 335 ? 29.228  -11.819 -4.066  1.00 31.71 ? 335  ALA A CA  1 
ATOM   1256 C  C   . ALA A 1 335 ? 30.267  -12.157 -5.149  1.00 30.56 ? 335  ALA A C   1 
ATOM   1257 O  O   . ALA A 1 335 ? 30.072  -11.847 -6.321  1.00 31.48 ? 335  ALA A O   1 
ATOM   1258 C  CB  . ALA A 1 335 ? 29.066  -10.303 -3.920  1.00 30.84 ? 335  ALA A CB  1 
ATOM   1259 N  N   . VAL A 1 336 ? 31.365  -12.784 -4.746  1.00 31.04 ? 336  VAL A N   1 
ATOM   1260 C  CA  . VAL A 1 336 ? 32.444  -13.155 -5.654  1.00 32.12 ? 336  VAL A CA  1 
ATOM   1261 C  C   . VAL A 1 336 ? 32.032  -14.330 -6.544  1.00 30.17 ? 336  VAL A C   1 
ATOM   1262 O  O   . VAL A 1 336 ? 32.556  -14.491 -7.645  1.00 30.22 ? 336  VAL A O   1 
ATOM   1263 C  CB  . VAL A 1 336 ? 33.749  -13.459 -4.863  1.00 33.37 ? 336  VAL A CB  1 
ATOM   1264 C  CG1 . VAL A 1 336 ? 34.862  -13.933 -5.786  1.00 34.07 ? 336  VAL A CG1 1 
ATOM   1265 C  CG2 . VAL A 1 336 ? 34.194  -12.208 -4.112  1.00 34.67 ? 336  VAL A CG2 1 
ATOM   1266 N  N   . SER A 1 337 ? 31.107  -15.154 -6.062  1.00 29.45 ? 337  SER A N   1 
ATOM   1267 C  CA  . SER A 1 337 ? 30.573  -16.265 -6.855  1.00 29.55 ? 337  SER A CA  1 
ATOM   1268 C  C   . SER A 1 337 ? 29.062  -16.312 -6.642  1.00 28.55 ? 337  SER A C   1 
ATOM   1269 O  O   . SER A 1 337 ? 28.596  -16.622 -5.552  1.00 27.11 ? 337  SER A O   1 
ATOM   1270 C  CB  . SER A 1 337 ? 31.234  -17.589 -6.462  1.00 31.21 ? 337  SER A CB  1 
ATOM   1271 O  OG  . SER A 1 337 ? 30.819  -18.653 -7.314  1.00 31.76 ? 337  SER A OG  1 
ATOM   1272 N  N   . GLN A 1 338 ? 28.308  -15.965 -7.686  1.00 26.87 ? 338  GLN A N   1 
ATOM   1273 C  CA  . GLN A 1 338 ? 26.851  -15.798 -7.598  1.00 25.23 ? 338  GLN A CA  1 
ATOM   1274 C  C   . GLN A 1 338 ? 26.114  -16.823 -8.455  1.00 24.23 ? 338  GLN A C   1 
ATOM   1275 O  O   . GLN A 1 338 ? 26.699  -17.424 -9.366  1.00 23.18 ? 338  GLN A O   1 
ATOM   1276 C  CB  . GLN A 1 338 ? 26.449  -14.390 -8.049  1.00 24.69 ? 338  GLN A CB  1 
ATOM   1277 C  CG  . GLN A 1 338 ? 27.060  -13.270 -7.228  1.00 24.87 ? 338  GLN A CG  1 
ATOM   1278 C  CD  . GLN A 1 338 ? 26.839  -11.906 -7.847  1.00 24.23 ? 338  GLN A CD  1 
ATOM   1279 O  OE1 . GLN A 1 338 ? 25.805  -11.649 -8.473  1.00 23.66 ? 338  GLN A OE1 1 
ATOM   1280 N  NE2 . GLN A 1 338 ? 27.804  -11.018 -7.666  1.00 23.59 ? 338  GLN A NE2 1 
ATOM   1281 N  N   . GLU A 1 339 ? 24.832  -17.015 -8.152  1.00 23.53 ? 339  GLU A N   1 
ATOM   1282 C  CA  . GLU A 1 339 ? 23.960  -17.848 -8.979  1.00 23.74 ? 339  GLU A CA  1 
ATOM   1283 C  C   . GLU A 1 339 ? 22.832  -17.001 -9.535  1.00 22.43 ? 339  GLU A C   1 
ATOM   1284 O  O   . GLU A 1 339 ? 22.098  -16.384 -8.768  1.00 20.95 ? 339  GLU A O   1 
ATOM   1285 C  CB  . GLU A 1 339 ? 23.341  -18.990 -8.182  1.00 24.54 ? 339  GLU A CB  1 
ATOM   1286 C  CG  . GLU A 1 339 ? 24.338  -19.942 -7.548  1.00 24.85 ? 339  GLU A CG  1 
ATOM   1287 C  CD  . GLU A 1 339 ? 24.779  -19.518 -6.167  1.00 25.03 ? 339  GLU A CD  1 
ATOM   1288 O  OE1 . GLU A 1 339 ? 23.977  -18.971 -5.379  1.00 26.35 ? 339  GLU A OE1 1 
ATOM   1289 O  OE2 . GLU A 1 339 ? 25.950  -19.761 -5.855  1.00 27.61 ? 339  GLU A OE2 1 
ATOM   1290 N  N   . TRP A 1 340 ? 22.713  -16.965 -10.865 1.00 21.92 ? 340  TRP A N   1 
ATOM   1291 C  CA  . TRP A 1 340 ? 21.603  -16.300 -11.528 1.00 22.21 ? 340  TRP A CA  1 
ATOM   1292 C  C   . TRP A 1 340 ? 20.686  -17.354 -12.172 1.00 22.34 ? 340  TRP A C   1 
ATOM   1293 O  O   . TRP A 1 340 ? 20.844  -18.548 -11.920 1.00 22.65 ? 340  TRP A O   1 
ATOM   1294 C  CB  . TRP A 1 340 ? 22.115  -15.285 -12.544 1.00 22.87 ? 340  TRP A CB  1 
ATOM   1295 C  CG  . TRP A 1 340 ? 22.903  -14.149 -11.974 1.00 22.43 ? 340  TRP A CG  1 
ATOM   1296 C  CD1 . TRP A 1 340 ? 23.325  -13.972 -10.679 1.00 22.55 ? 340  TRP A CD1 1 
ATOM   1297 C  CD2 . TRP A 1 340 ? 23.411  -13.044 -12.711 1.00 22.64 ? 340  TRP A CD2 1 
ATOM   1298 N  NE1 . TRP A 1 340 ? 24.036  -12.800 -10.573 1.00 22.23 ? 340  TRP A NE1 1 
ATOM   1299 C  CE2 . TRP A 1 340 ? 24.113  -12.217 -11.806 1.00 22.00 ? 340  TRP A CE2 1 
ATOM   1300 C  CE3 . TRP A 1 340 ? 23.335  -12.664 -14.056 1.00 23.28 ? 340  TRP A CE3 1 
ATOM   1301 C  CZ2 . TRP A 1 340 ? 24.739  -11.039 -12.204 1.00 22.25 ? 340  TRP A CZ2 1 
ATOM   1302 C  CZ3 . TRP A 1 340 ? 23.956  -11.485 -14.450 1.00 23.14 ? 340  TRP A CZ3 1 
ATOM   1303 C  CH2 . TRP A 1 340 ? 24.649  -10.690 -13.525 1.00 23.30 ? 340  TRP A CH2 1 
ATOM   1304 N  N   . SER A 1 341 ? 19.714  -16.931 -12.978 1.00 21.78 ? 341  SER A N   1 
ATOM   1305 C  CA  . SER A 1 341 ? 18.633  -17.841 -13.390 1.00 21.18 ? 341  SER A CA  1 
ATOM   1306 C  C   . SER A 1 341 ? 19.011  -18.948 -14.371 1.00 20.13 ? 341  SER A C   1 
ATOM   1307 O  O   . SER A 1 341 ? 20.026  -18.896 -15.080 1.00 18.14 ? 341  SER A O   1 
ATOM   1308 C  CB  . SER A 1 341 ? 17.469  -17.057 -13.984 1.00 21.96 ? 341  SER A CB  1 
ATOM   1309 O  OG  . SER A 1 341 ? 17.077  -16.033 -13.109 1.00 24.08 ? 341  SER A OG  1 
ATOM   1310 N  N   . GLY A 1 342 ? 18.128  -19.935 -14.408 1.00 20.53 ? 342  GLY A N   1 
ATOM   1311 C  CA  . GLY A 1 342 ? 18.212  -21.045 -15.346 1.00 20.54 ? 342  GLY A CA  1 
ATOM   1312 C  C   . GLY A 1 342 ? 16.919  -21.827 -15.336 1.00 20.47 ? 342  GLY A C   1 
ATOM   1313 O  O   . GLY A 1 342 ? 15.828  -21.250 -15.476 1.00 21.39 ? 342  GLY A O   1 
ATOM   1314 N  N   . SER A 1 343 ? 17.030  -23.143 -15.162 1.00 20.27 ? 343  SER A N   1 
ATOM   1315 C  CA  . SER A 1 343 ? 15.874  -24.037 -15.215 1.00 19.51 ? 343  SER A CA  1 
ATOM   1316 C  C   . SER A 1 343 ? 16.124  -25.318 -14.404 1.00 20.35 ? 343  SER A C   1 
ATOM   1317 O  O   . SER A 1 343 ? 17.239  -25.543 -13.923 1.00 20.62 ? 343  SER A O   1 
ATOM   1318 C  CB  . SER A 1 343 ? 15.530  -24.366 -16.678 1.00 18.93 ? 343  SER A CB  1 
ATOM   1319 O  OG  . SER A 1 343 ? 16.619  -24.938 -17.371 1.00 17.57 ? 343  SER A OG  1 
ATOM   1320 N  N   . ALA A 1 344 ? 15.088  -26.148 -14.258 1.00 20.77 ? 344  ALA A N   1 
ATOM   1321 C  CA  . ALA A 1 344 ? 15.196  -27.409 -13.509 1.00 20.69 ? 344  ALA A CA  1 
ATOM   1322 C  C   . ALA A 1 344 ? 14.135  -28.432 -13.903 1.00 20.84 ? 344  ALA A C   1 
ATOM   1323 O  O   . ALA A 1 344 ? 12.957  -28.109 -14.060 1.00 20.22 ? 344  ALA A O   1 
ATOM   1324 C  CB  . ALA A 1 344 ? 15.137  -27.151 -12.016 1.00 21.28 ? 344  ALA A CB  1 
ATOM   1325 N  N   . VAL A 1 345 ? 14.590  -29.670 -14.057 1.00 21.08 ? 345  VAL A N   1 
ATOM   1326 C  CA  . VAL A 1 345 ? 13.762  -30.793 -14.471 1.00 21.52 ? 345  VAL A CA  1 
ATOM   1327 C  C   . VAL A 1 345 ? 14.074  -32.048 -13.641 1.00 21.73 ? 345  VAL A C   1 
ATOM   1328 O  O   . VAL A 1 345 ? 15.069  -32.102 -12.952 1.00 20.37 ? 345  VAL A O   1 
ATOM   1329 C  CB  . VAL A 1 345 ? 13.974  -31.132 -15.952 1.00 21.25 ? 345  VAL A CB  1 
ATOM   1330 C  CG1 . VAL A 1 345 ? 13.665  -29.913 -16.829 1.00 21.95 ? 345  VAL A CG1 1 
ATOM   1331 C  CG2 . VAL A 1 345 ? 15.397  -31.595 -16.199 1.00 21.33 ? 345  VAL A CG2 1 
ATOM   1332 N  N   . LEU A 1 346 ? 13.206  -33.047 -13.715 1.00 23.56 ? 346  LEU A N   1 
ATOM   1333 C  CA  . LEU A 1 346 ? 13.481  -34.333 -13.085 1.00 24.74 ? 346  LEU A CA  1 
ATOM   1334 C  C   . LEU A 1 346 ? 14.375  -35.199 -13.973 1.00 25.03 ? 346  LEU A C   1 
ATOM   1335 O  O   . LEU A 1 346 ? 14.182  -35.273 -15.191 1.00 23.52 ? 346  LEU A O   1 
ATOM   1336 C  CB  . LEU A 1 346 ? 12.173  -35.067 -12.798 1.00 24.88 ? 346  LEU A CB  1 
ATOM   1337 C  CG  . LEU A 1 346 ? 11.206  -34.362 -11.851 1.00 26.70 ? 346  LEU A CG  1 
ATOM   1338 C  CD1 . LEU A 1 346 ? 9.986   -35.256 -11.585 1.00 27.22 ? 346  LEU A CD1 1 
ATOM   1339 C  CD2 . LEU A 1 346 ? 11.921  -33.991 -10.556 1.00 26.45 ? 346  LEU A CD2 1 
ATOM   1340 N  N   . ASN A 1 347 ? 15.364  -35.836 -13.350 1.00 26.54 ? 347  ASN A N   1 
ATOM   1341 C  CA  . ASN A 1 347 ? 16.102  -36.930 -13.971 1.00 28.61 ? 347  ASN A CA  1 
ATOM   1342 C  C   . ASN A 1 347 ? 15.280  -38.241 -13.847 1.00 30.69 ? 347  ASN A C   1 
ATOM   1343 O  O   . ASN A 1 347 ? 14.254  -38.269 -13.161 1.00 30.83 ? 347  ASN A O   1 
ATOM   1344 C  CB  . ASN A 1 347 ? 17.482  -37.101 -13.307 1.00 28.08 ? 347  ASN A CB  1 
ATOM   1345 C  CG  . ASN A 1 347 ? 18.448  -35.949 -13.619 1.00 28.54 ? 347  ASN A CG  1 
ATOM   1346 O  OD1 . ASN A 1 347 ? 18.490  -35.438 -14.742 1.00 28.73 ? 347  ASN A OD1 1 
ATOM   1347 N  ND2 . ASN A 1 347 ? 19.245  -35.556 -12.628 1.00 26.12 ? 347  ASN A ND2 1 
ATOM   1348 N  N   . SER A 1 348 ? 15.750  -39.309 -14.491 1.00 31.68 ? 348  SER A N   1 
ATOM   1349 C  CA  . SER A 1 348 ? 15.087  -40.628 -14.487 1.00 32.68 ? 348  SER A CA  1 
ATOM   1350 C  C   . SER A 1 348 ? 14.880  -41.263 -13.112 1.00 31.36 ? 348  SER A C   1 
ATOM   1351 O  O   . SER A 1 348 ? 13.888  -41.936 -12.886 1.00 30.04 ? 348  SER A O   1 
ATOM   1352 C  CB  . SER A 1 348 ? 15.878  -41.617 -15.343 1.00 33.52 ? 348  SER A CB  1 
ATOM   1353 O  OG  . SER A 1 348 ? 15.578  -41.431 -16.710 1.00 37.84 ? 348  SER A OG  1 
ATOM   1354 N  N   . ASP A 1 349 ? 15.831  -41.062 -12.215 1.00 31.77 ? 349  ASP A N   1 
ATOM   1355 C  CA  . ASP A 1 349 ? 15.751  -41.588 -10.853 1.00 32.12 ? 349  ASP A CA  1 
ATOM   1356 C  C   . ASP A 1 349 ? 15.095  -40.597 -9.870  1.00 32.77 ? 349  ASP A C   1 
ATOM   1357 O  O   . ASP A 1 349 ? 15.249  -40.734 -8.655  1.00 33.75 ? 349  ASP A O   1 
ATOM   1358 C  CB  . ASP A 1 349 ? 17.161  -41.924 -10.361 1.00 33.79 ? 349  ASP A CB  1 
ATOM   1359 C  CG  . ASP A 1 349 ? 18.043  -40.680 -10.202 1.00 35.85 ? 349  ASP A CG  1 
ATOM   1360 O  OD1 . ASP A 1 349 ? 17.662  -39.586 -10.704 1.00 37.01 ? 349  ASP A OD1 1 
ATOM   1361 O  OD2 . ASP A 1 349 ? 19.118  -40.795 -9.583  1.00 34.11 ? 349  ASP A OD2 1 
ATOM   1362 N  N   . ASN A 1 350 ? 14.401  -39.580 -10.387 1.00 32.06 ? 350  ASN A N   1 
ATOM   1363 C  CA  . ASN A 1 350 ? 13.707  -38.598 -9.553  1.00 29.92 ? 350  ASN A CA  1 
ATOM   1364 C  C   . ASN A 1 350 ? 14.647  -37.664 -8.753  1.00 28.70 ? 350  ASN A C   1 
ATOM   1365 O  O   . ASN A 1 350 ? 14.193  -36.968 -7.848  1.00 29.29 ? 350  ASN A O   1 
ATOM   1366 C  CB  . ASN A 1 350 ? 12.676  -39.309 -8.635  1.00 31.60 ? 350  ASN A CB  1 
ATOM   1367 C  CG  . ASN A 1 350 ? 11.261  -38.722 -8.748  1.00 32.30 ? 350  ASN A CG  1 
ATOM   1368 O  OD1 . ASN A 1 350 ? 10.847  -38.239 -9.803  1.00 32.07 ? 350  ASN A OD1 1 
ATOM   1369 N  ND2 . ASN A 1 350 ? 10.507  -38.793 -7.659  1.00 31.98 ? 350  ASN A ND2 1 
ATOM   1370 N  N   . SER A 1 351 ? 15.943  -37.639 -9.079  1.00 27.85 ? 351  SER A N   1 
ATOM   1371 C  CA  . SER A 1 351 ? 16.799  -36.528 -8.672  1.00 27.52 ? 351  SER A CA  1 
ATOM   1372 C  C   . SER A 1 351 ? 16.486  -35.342 -9.603  1.00 27.46 ? 351  SER A C   1 
ATOM   1373 O  O   . SER A 1 351 ? 15.775  -35.510 -10.583 1.00 25.35 ? 351  SER A O   1 
ATOM   1374 C  CB  . SER A 1 351 ? 18.282  -36.883 -8.748  1.00 27.33 ? 351  SER A CB  1 
ATOM   1375 O  OG  . SER A 1 351 ? 18.700  -37.178 -10.068 1.00 27.09 ? 351  SER A OG  1 
ATOM   1376 N  N   . ILE A 1 352 ? 17.018  -34.164 -9.284  1.00 29.37 ? 352  ILE A N   1 
ATOM   1377 C  CA  . ILE A 1 352 ? 16.735  -32.927 -10.027 1.00 30.12 ? 352  ILE A CA  1 
ATOM   1378 C  C   . ILE A 1 352 ? 17.980  -32.427 -10.740 1.00 28.90 ? 352  ILE A C   1 
ATOM   1379 O  O   . ILE A 1 352 ? 19.028  -32.244 -10.111 1.00 28.47 ? 352  ILE A O   1 
ATOM   1380 C  CB  . ILE A 1 352 ? 16.232  -31.839 -9.071  1.00 32.88 ? 352  ILE A CB  1 
ATOM   1381 C  CG1 . ILE A 1 352 ? 14.784  -32.133 -8.691  1.00 35.78 ? 352  ILE A CG1 1 
ATOM   1382 C  CG2 . ILE A 1 352 ? 16.339  -30.448 -9.688  1.00 33.72 ? 352  ILE A CG2 1 
ATOM   1383 C  CD1 . ILE A 1 352 ? 14.395  -31.580 -7.342  1.00 38.26 ? 352  ILE A CD1 1 
ATOM   1384 N  N   . GLN A 1 353 ? 17.880  -32.214 -12.051 1.00 26.16 ? 353  GLN A N   1 
ATOM   1385 C  CA  . GLN A 1 353 ? 18.971  -31.583 -12.767 1.00 24.56 ? 353  GLN A CA  1 
ATOM   1386 C  C   . GLN A 1 353 ? 18.709  -30.073 -12.863 1.00 23.63 ? 353  GLN A C   1 
ATOM   1387 O  O   . GLN A 1 353 ? 17.724  -29.638 -13.471 1.00 22.81 ? 353  GLN A O   1 
ATOM   1388 C  CB  . GLN A 1 353 ? 19.201  -32.205 -14.144 1.00 24.05 ? 353  GLN A CB  1 
ATOM   1389 C  CG  . GLN A 1 353 ? 20.610  -31.956 -14.655 1.00 24.40 ? 353  GLN A CG  1 
ATOM   1390 C  CD  . GLN A 1 353 ? 21.689  -32.568 -13.755 1.00 24.28 ? 353  GLN A CD  1 
ATOM   1391 O  OE1 . GLN A 1 353 ? 21.463  -33.587 -13.097 1.00 22.48 ? 353  GLN A OE1 1 
ATOM   1392 N  NE2 . GLN A 1 353 ? 22.868  -31.949 -13.729 1.00 24.27 ? 353  GLN A NE2 1 
ATOM   1393 N  N   . LEU A 1 354 ? 19.604  -29.311 -12.235 1.00 22.20 ? 354  LEU A N   1 
ATOM   1394 C  CA  . LEU A 1 354 ? 19.542  -27.871 -12.180 1.00 21.65 ? 354  LEU A CA  1 
ATOM   1395 C  C   . LEU A 1 354 ? 20.440  -27.316 -13.252 1.00 21.42 ? 354  LEU A C   1 
ATOM   1396 O  O   . LEU A 1 354 ? 21.581  -27.749 -13.384 1.00 21.90 ? 354  LEU A O   1 
ATOM   1397 C  CB  . LEU A 1 354 ? 20.029  -27.364 -10.816 1.00 22.22 ? 354  LEU A CB  1 
ATOM   1398 C  CG  . LEU A 1 354 ? 20.191  -25.836 -10.663 1.00 21.85 ? 354  LEU A CG  1 
ATOM   1399 C  CD1 . LEU A 1 354 ? 18.844  -25.141 -10.751 1.00 21.45 ? 354  LEU A CD1 1 
ATOM   1400 C  CD2 . LEU A 1 354 ? 20.907  -25.483 -9.365  1.00 22.36 ? 354  LEU A CD2 1 
ATOM   1401 N  N   . PHE A 1 355 ? 19.906  -26.381 -14.039 1.00 20.66 ? 355  PHE A N   1 
ATOM   1402 C  CA  . PHE A 1 355 ? 20.715  -25.519 -14.888 1.00 20.30 ? 355  PHE A CA  1 
ATOM   1403 C  C   . PHE A 1 355 ? 20.586  -24.113 -14.338 1.00 19.35 ? 355  PHE A C   1 
ATOM   1404 O  O   . PHE A 1 355 ? 19.487  -23.676 -13.982 1.00 18.86 ? 355  PHE A O   1 
ATOM   1405 C  CB  . PHE A 1 355 ? 20.261  -25.591 -16.347 1.00 19.88 ? 355  PHE A CB  1 
ATOM   1406 C  CG  . PHE A 1 355 ? 20.536  -26.910 -16.967 1.00 19.98 ? 355  PHE A CG  1 
ATOM   1407 C  CD1 . PHE A 1 355 ? 19.648  -27.961 -16.798 1.00 19.85 ? 355  PHE A CD1 1 
ATOM   1408 C  CD2 . PHE A 1 355 ? 21.718  -27.131 -17.668 1.00 19.83 ? 355  PHE A CD2 1 
ATOM   1409 C  CE1 . PHE A 1 355 ? 19.925  -29.204 -17.334 1.00 19.39 ? 355  PHE A CE1 1 
ATOM   1410 C  CE2 . PHE A 1 355 ? 21.991  -28.369 -18.212 1.00 19.28 ? 355  PHE A CE2 1 
ATOM   1411 C  CZ  . PHE A 1 355 ? 21.097  -29.401 -18.045 1.00 19.65 ? 355  PHE A CZ  1 
ATOM   1412 N  N   . TYR A 1 356 ? 21.714  -23.423 -14.248 1.00 18.76 ? 356  TYR A N   1 
ATOM   1413 C  CA  . TYR A 1 356 ? 21.748  -22.094 -13.671 1.00 19.33 ? 356  TYR A CA  1 
ATOM   1414 C  C   . TYR A 1 356 ? 22.937  -21.333 -14.255 1.00 18.70 ? 356  TYR A C   1 
ATOM   1415 O  O   . TYR A 1 356 ? 23.715  -21.856 -15.075 1.00 17.25 ? 356  TYR A O   1 
ATOM   1416 C  CB  . TYR A 1 356 ? 21.809  -22.164 -12.119 1.00 19.98 ? 356  TYR A CB  1 
ATOM   1417 C  CG  . TYR A 1 356 ? 23.169  -22.581 -11.586 1.00 20.32 ? 356  TYR A CG  1 
ATOM   1418 C  CD1 . TYR A 1 356 ? 23.541  -23.925 -11.533 1.00 20.95 ? 356  TYR A CD1 1 
ATOM   1419 C  CD2 . TYR A 1 356 ? 24.093  -21.629 -11.160 1.00 20.87 ? 356  TYR A CD2 1 
ATOM   1420 C  CE1 . TYR A 1 356 ? 24.792  -24.307 -11.067 1.00 20.85 ? 356  TYR A CE1 1 
ATOM   1421 C  CE2 . TYR A 1 356 ? 25.351  -21.996 -10.700 1.00 21.16 ? 356  TYR A CE2 1 
ATOM   1422 C  CZ  . TYR A 1 356 ? 25.697  -23.339 -10.648 1.00 21.31 ? 356  TYR A CZ  1 
ATOM   1423 O  OH  . TYR A 1 356 ? 26.954  -23.702 -10.183 1.00 21.58 ? 356  TYR A OH  1 
ATOM   1424 N  N   . THR A 1 357 ? 23.053  -20.086 -13.831 1.00 18.36 ? 357  THR A N   1 
ATOM   1425 C  CA  . THR A 1 357 ? 24.112  -19.217 -14.271 1.00 18.63 ? 357  THR A CA  1 
ATOM   1426 C  C   . THR A 1 357 ? 25.082  -18.995 -13.118 1.00 19.29 ? 357  THR A C   1 
ATOM   1427 O  O   . THR A 1 357 ? 24.708  -18.374 -12.112 1.00 19.00 ? 357  THR A O   1 
ATOM   1428 C  CB  . THR A 1 357 ? 23.547  -17.844 -14.705 1.00 18.17 ? 357  THR A CB  1 
ATOM   1429 O  OG1 . THR A 1 357 ? 22.452  -18.034 -15.604 1.00 17.81 ? 357  THR A OG1 1 
ATOM   1430 C  CG2 . THR A 1 357 ? 24.624  -16.975 -15.351 1.00 17.80 ? 357  THR A CG2 1 
ATOM   1431 N  N   . ARG A 1 358 ? 26.318  -19.487 -13.294 1.00 20.42 ? 358  ARG A N   1 
ATOM   1432 C  CA  . ARG A 1 358 ? 27.443  -19.236 -12.377 1.00 20.51 ? 358  ARG A CA  1 
ATOM   1433 C  C   . ARG A 1 358 ? 28.102  -17.934 -12.796 1.00 21.45 ? 358  ARG A C   1 
ATOM   1434 O  O   . ARG A 1 358 ? 28.571  -17.817 -13.927 1.00 21.61 ? 358  ARG A O   1 
ATOM   1435 C  CB  . ARG A 1 358 ? 28.456  -20.394 -12.418 1.00 20.81 ? 358  ARG A CB  1 
ATOM   1436 C  CG  . ARG A 1 358 ? 29.762  -20.197 -11.643 1.00 21.22 ? 358  ARG A CG  1 
ATOM   1437 C  CD  . ARG A 1 358 ? 29.544  -19.939 -10.167 1.00 21.71 ? 358  ARG A CD  1 
ATOM   1438 N  NE  . ARG A 1 358 ? 28.877  -21.058 -9.522  1.00 21.84 ? 358  ARG A NE  1 
ATOM   1439 C  CZ  . ARG A 1 358 ? 28.201  -20.986 -8.381  1.00 21.88 ? 358  ARG A CZ  1 
ATOM   1440 N  NH1 . ARG A 1 358 ? 28.098  -19.853 -7.711  1.00 22.86 ? 358  ARG A NH1 1 
ATOM   1441 N  NH2 . ARG A 1 358 ? 27.623  -22.073 -7.894  1.00 22.93 ? 358  ARG A NH2 1 
ATOM   1442 N  N   . VAL A 1 359 ? 28.118  -16.965 -11.880 1.00 22.13 ? 359  VAL A N   1 
ATOM   1443 C  CA  . VAL A 1 359 ? 28.687  -15.644 -12.117 1.00 22.57 ? 359  VAL A CA  1 
ATOM   1444 C  C   . VAL A 1 359 ? 29.905  -15.402 -11.212 1.00 22.77 ? 359  VAL A C   1 
ATOM   1445 O  O   . VAL A 1 359 ? 29.783  -15.355 -9.991  1.00 24.63 ? 359  VAL A O   1 
ATOM   1446 C  CB  . VAL A 1 359 ? 27.635  -14.547 -11.875 1.00 21.74 ? 359  VAL A CB  1 
ATOM   1447 C  CG1 . VAL A 1 359 ? 28.203  -13.170 -12.202 1.00 22.28 ? 359  VAL A CG1 1 
ATOM   1448 C  CG2 . VAL A 1 359 ? 26.388  -14.833 -12.700 1.00 22.32 ? 359  VAL A CG2 1 
ATOM   1449 N  N   . ASP A 1 360 ? 31.071  -15.262 -11.821 1.00 23.82 ? 360  ASP A N   1 
ATOM   1450 C  CA  . ASP A 1 360 ? 32.331  -15.014 -11.103 1.00 25.81 ? 360  ASP A CA  1 
ATOM   1451 C  C   . ASP A 1 360 ? 32.645  -13.531 -11.208 1.00 25.35 ? 360  ASP A C   1 
ATOM   1452 O  O   . ASP A 1 360 ? 32.771  -13.020 -12.305 1.00 24.32 ? 360  ASP A O   1 
ATOM   1453 C  CB  . ASP A 1 360 ? 33.453  -15.856 -11.732 1.00 26.84 ? 360  ASP A CB  1 
ATOM   1454 C  CG  . ASP A 1 360 ? 34.838  -15.542 -11.168 1.00 28.64 ? 360  ASP A CG  1 
ATOM   1455 O  OD1 . ASP A 1 360 ? 35.021  -14.575 -10.405 1.00 30.10 ? 360  ASP A OD1 1 
ATOM   1456 O  OD2 . ASP A 1 360 ? 35.770  -16.276 -11.519 1.00 32.35 ? 360  ASP A OD2 1 
ATOM   1457 N  N   . THR A 1 361 ? 32.763  -12.836 -10.081 1.00 26.75 ? 361  THR A N   1 
ATOM   1458 C  CA  . THR A 1 361 ? 33.013  -11.392 -10.115 1.00 28.24 ? 361  THR A CA  1 
ATOM   1459 C  C   . THR A 1 361 ? 34.434  -10.973 -9.699  1.00 28.96 ? 361  THR A C   1 
ATOM   1460 O  O   . THR A 1 361 ? 34.670  -9.795  -9.436  1.00 27.35 ? 361  THR A O   1 
ATOM   1461 C  CB  . THR A 1 361 ? 31.990  -10.628 -9.251  1.00 28.12 ? 361  THR A CB  1 
ATOM   1462 O  OG1 . THR A 1 361 ? 32.099  -11.065 -7.897  1.00 30.07 ? 361  THR A OG1 1 
ATOM   1463 C  CG2 . THR A 1 361 ? 30.579  -10.874 -9.736  1.00 28.37 ? 361  THR A CG2 1 
ATOM   1464 N  N   . SER A 1 362 ? 35.371  -11.918 -9.681  1.00 30.09 ? 362  SER A N   1 
ATOM   1465 C  CA  . SER A 1 362 ? 36.746  -11.649 -9.228  1.00 32.63 ? 362  SER A CA  1 
ATOM   1466 C  C   . SER A 1 362 ? 37.587  -10.829 -10.209 1.00 33.95 ? 362  SER A C   1 
ATOM   1467 O  O   . SER A 1 362 ? 38.573  -10.225 -9.805  1.00 32.32 ? 362  SER A O   1 
ATOM   1468 C  CB  . SER A 1 362 ? 37.479  -12.958 -8.927  1.00 33.11 ? 362  SER A CB  1 
ATOM   1469 O  OG  . SER A 1 362 ? 37.549  -13.775 -10.077 1.00 32.77 ? 362  SER A OG  1 
ATOM   1470 N  N   . ASP A 1 363 ? 37.216  -10.799 -11.489 1.00 34.86 ? 363  ASP A N   1 
ATOM   1471 C  CA  . ASP A 1 363 ? 37.939  -9.956  -12.447 1.00 34.31 ? 363  ASP A CA  1 
ATOM   1472 C  C   . ASP A 1 363 ? 37.350  -8.553  -12.400 1.00 35.31 ? 363  ASP A C   1 
ATOM   1473 O  O   . ASP A 1 363 ? 36.489  -8.190  -13.209 1.00 31.92 ? 363  ASP A O   1 
ATOM   1474 C  CB  . ASP A 1 363 ? 37.884  -10.539 -13.859 1.00 34.82 ? 363  ASP A CB  1 
ATOM   1475 C  CG  . ASP A 1 363 ? 38.665  -9.708  -14.874 1.00 35.49 ? 363  ASP A CG  1 
ATOM   1476 O  OD1 . ASP A 1 363 ? 39.539  -8.903  -14.483 1.00 37.70 ? 363  ASP A OD1 1 
ATOM   1477 O  OD2 . ASP A 1 363 ? 38.410  -9.859  -16.079 1.00 36.42 ? 363  ASP A OD2 1 
ATOM   1478 N  N   . ASN A 1 364 ? 37.802  -7.768  -11.421 1.00 36.63 ? 364  ASN A N   1 
ATOM   1479 C  CA  . ASN A 1 364 ? 37.372  -6.378  -11.293 1.00 35.83 ? 364  ASN A CA  1 
ATOM   1480 C  C   . ASN A 1 364 ? 35.866  -6.192  -11.162 1.00 33.46 ? 364  ASN A C   1 
ATOM   1481 O  O   . ASN A 1 364 ? 35.316  -5.234  -11.698 1.00 30.86 ? 364  ASN A O   1 
ATOM   1482 C  CB  . ASN A 1 364 ? 37.855  -5.589  -12.507 1.00 39.11 ? 364  ASN A CB  1 
ATOM   1483 C  CG  . ASN A 1 364 ? 38.895  -4.568  -12.154 1.00 42.89 ? 364  ASN A CG  1 
ATOM   1484 O  OD1 . ASN A 1 364 ? 39.971  -4.898  -11.642 1.00 43.40 ? 364  ASN A OD1 1 
ATOM   1485 N  ND2 . ASN A 1 364 ? 38.584  -3.306  -12.433 1.00 46.25 ? 364  ASN A ND2 1 
ATOM   1486 N  N   . ASN A 1 365 ? 35.202  -7.115  -10.472 1.00 32.57 ? 365  ASN A N   1 
ATOM   1487 C  CA  . ASN A 1 365 ? 33.758  -7.029  -10.215 1.00 32.34 ? 365  ASN A CA  1 
ATOM   1488 C  C   . ASN A 1 365 ? 32.848  -7.190  -11.448 1.00 30.80 ? 365  ASN A C   1 
ATOM   1489 O  O   . ASN A 1 365 ? 31.669  -6.850  -11.379 1.00 32.00 ? 365  ASN A O   1 
ATOM   1490 C  CB  . ASN A 1 365 ? 33.424  -5.713  -9.498  1.00 33.93 ? 365  ASN A CB  1 
ATOM   1491 C  CG  . ASN A 1 365 ? 34.349  -5.439  -8.320  1.00 37.10 ? 365  ASN A CG  1 
ATOM   1492 O  OD1 . ASN A 1 365 ? 34.520  -6.286  -7.436  1.00 35.84 ? 365  ASN A OD1 1 
ATOM   1493 N  ND2 . ASN A 1 365 ? 34.947  -4.247  -8.297  1.00 40.27 ? 365  ASN A ND2 1 
ATOM   1494 N  N   . THR A 1 366 ? 33.376  -7.689  -12.564 1.00 28.19 ? 366  THR A N   1 
ATOM   1495 C  CA  . THR A 1 366 ? 32.554  -7.903  -13.757 1.00 27.20 ? 366  THR A CA  1 
ATOM   1496 C  C   . THR A 1 366 ? 31.641  -9.111  -13.542 1.00 25.80 ? 366  THR A C   1 
ATOM   1497 O  O   . THR A 1 366 ? 31.988  -10.057 -12.847 1.00 24.33 ? 366  THR A O   1 
ATOM   1498 C  CB  . THR A 1 366 ? 33.382  -8.180  -15.040 1.00 27.32 ? 366  THR A CB  1 
ATOM   1499 O  OG1 . THR A 1 366 ? 34.160  -9.377  -14.878 1.00 26.47 ? 366  THR A OG1 1 
ATOM   1500 C  CG2 . THR A 1 366 ? 34.302  -6.994  -15.401 1.00 27.69 ? 366  THR A CG2 1 
ATOM   1501 N  N   . ASN A 1 367 ? 30.473  -9.071  -14.161 1.00 24.90 ? 367  ASN A N   1 
ATOM   1502 C  CA  . ASN A 1 367 ? 29.544  -10.199 -14.118 1.00 23.07 ? 367  ASN A CA  1 
ATOM   1503 C  C   . ASN A 1 367 ? 29.901  -11.252 -15.179 1.00 22.77 ? 367  ASN A C   1 
ATOM   1504 O  O   . ASN A 1 367 ? 29.217  -11.418 -16.182 1.00 22.08 ? 367  ASN A O   1 
ATOM   1505 C  CB  . ASN A 1 367 ? 28.108  -9.673  -14.233 1.00 22.14 ? 367  ASN A CB  1 
ATOM   1506 C  CG  . ASN A 1 367 ? 27.677  -8.917  -12.986 1.00 22.73 ? 367  ASN A CG  1 
ATOM   1507 O  OD1 . ASN A 1 367 ? 28.036  -9.293  -11.872 1.00 23.50 ? 367  ASN A OD1 1 
ATOM   1508 N  ND2 . ASN A 1 367 ? 26.921  -7.848  -13.162 1.00 22.10 ? 367  ASN A ND2 1 
ATOM   1509 N  N   . HIS A 1 368 ? 31.011  -11.950 -14.939 1.00 23.42 ? 368  HIS A N   1 
ATOM   1510 C  CA  . HIS A 1 368 ? 31.485  -13.029 -15.805 1.00 22.60 ? 368  HIS A CA  1 
ATOM   1511 C  C   . HIS A 1 368 ? 30.516  -14.194 -15.645 1.00 22.26 ? 368  HIS A C   1 
ATOM   1512 O  O   . HIS A 1 368 ? 30.602  -14.948 -14.663 1.00 21.45 ? 368  HIS A O   1 
ATOM   1513 C  CB  . HIS A 1 368 ? 32.907  -13.444 -15.409 1.00 23.08 ? 368  HIS A CB  1 
ATOM   1514 C  CG  . HIS A 1 368 ? 33.569  -14.394 -16.365 1.00 23.81 ? 368  HIS A CG  1 
ATOM   1515 N  ND1 . HIS A 1 368 ? 34.933  -14.598 -16.372 1.00 23.99 ? 368  HIS A ND1 1 
ATOM   1516 C  CD2 . HIS A 1 368 ? 33.063  -15.190 -17.346 1.00 24.29 ? 368  HIS A CD2 1 
ATOM   1517 C  CE1 . HIS A 1 368 ? 35.243  -15.488 -17.302 1.00 24.25 ? 368  HIS A CE1 1 
ATOM   1518 N  NE2 . HIS A 1 368 ? 34.126  -15.862 -17.909 1.00 25.47 ? 368  HIS A NE2 1 
ATOM   1519 N  N   . GLN A 1 369 ? 29.598  -14.318 -16.607 1.00 20.85 ? 369  GLN A N   1 
ATOM   1520 C  CA  . GLN A 1 369 ? 28.515  -15.317 -16.568 1.00 21.00 ? 369  GLN A CA  1 
ATOM   1521 C  C   . GLN A 1 369 ? 28.830  -16.599 -17.326 1.00 20.59 ? 369  GLN A C   1 
ATOM   1522 O  O   . GLN A 1 369 ? 29.466  -16.565 -18.382 1.00 21.19 ? 369  GLN A O   1 
ATOM   1523 C  CB  . GLN A 1 369 ? 27.243  -14.727 -17.163 1.00 20.31 ? 369  GLN A CB  1 
ATOM   1524 C  CG  . GLN A 1 369 ? 26.670  -13.579 -16.363 1.00 19.64 ? 369  GLN A CG  1 
ATOM   1525 C  CD  . GLN A 1 369 ? 25.914  -12.633 -17.250 1.00 20.04 ? 369  GLN A CD  1 
ATOM   1526 O  OE1 . GLN A 1 369 ? 24.885  -13.005 -17.842 1.00 19.11 ? 369  GLN A OE1 1 
ATOM   1527 N  NE2 . GLN A 1 369 ? 26.421  -11.398 -17.366 1.00 19.30 ? 369  GLN A NE2 1 
ATOM   1528 N  N   . LYS A 1 370 ? 28.336  -17.715 -16.795 1.00 20.67 ? 370  LYS A N   1 
ATOM   1529 C  CA  . LYS A 1 370 ? 28.591  -19.037 -17.349 1.00 20.67 ? 370  LYS A CA  1 
ATOM   1530 C  C   . LYS A 1 370 ? 27.400  -19.926 -17.126 1.00 20.93 ? 370  LYS A C   1 
ATOM   1531 O  O   . LYS A 1 370 ? 26.809  -19.924 -16.029 1.00 21.05 ? 370  LYS A O   1 
ATOM   1532 C  CB  . LYS A 1 370 ? 29.765  -19.689 -16.635 1.00 22.70 ? 370  LYS A CB  1 
ATOM   1533 C  CG  . LYS A 1 370 ? 31.084  -18.948 -16.746 1.00 23.22 ? 370  LYS A CG  1 
ATOM   1534 C  CD  . LYS A 1 370 ? 32.091  -19.616 -15.835 1.00 24.81 ? 370  LYS A CD  1 
ATOM   1535 C  CE  . LYS A 1 370 ? 33.477  -19.031 -16.036 1.00 25.77 ? 370  LYS A CE  1 
ATOM   1536 N  NZ  . LYS A 1 370 ? 34.223  -19.050 -14.767 1.00 25.29 ? 370  LYS A NZ  1 
ATOM   1537 N  N   . ILE A 1 371 ? 27.041  -20.710 -18.139 1.00 20.88 ? 371  ILE A N   1 
ATOM   1538 C  CA  . ILE A 1 371 ? 25.943  -21.666 -17.955 1.00 20.87 ? 371  ILE A CA  1 
ATOM   1539 C  C   . ILE A 1 371 ? 26.539  -22.871 -17.239 1.00 21.11 ? 371  ILE A C   1 
ATOM   1540 O  O   . ILE A 1 371 ? 27.501  -23.458 -17.728 1.00 21.99 ? 371  ILE A O   1 
ATOM   1541 C  CB  . ILE A 1 371 ? 25.301  -22.113 -19.270 1.00 20.21 ? 371  ILE A CB  1 
ATOM   1542 C  CG1 . ILE A 1 371 ? 24.691  -20.910 -20.004 1.00 20.72 ? 371  ILE A CG1 1 
ATOM   1543 C  CG2 . ILE A 1 371 ? 24.234  -23.170 -18.983 1.00 20.42 ? 371  ILE A CG2 1 
ATOM   1544 C  CD1 . ILE A 1 371 ? 24.490  -21.135 -21.483 1.00 20.75 ? 371  ILE A CD1 1 
ATOM   1545 N  N   . ALA A 1 372 ? 25.966  -23.212 -16.092 1.00 21.52 ? 372  ALA A N   1 
ATOM   1546 C  CA  . ALA A 1 372 ? 26.431  -24.323 -15.272 1.00 22.65 ? 372  ALA A CA  1 
ATOM   1547 C  C   . ALA A 1 372 ? 25.282  -25.275 -14.934 1.00 23.48 ? 372  ALA A C   1 
ATOM   1548 O  O   . ALA A 1 372 ? 24.101  -24.939 -15.076 1.00 24.36 ? 372  ALA A O   1 
ATOM   1549 C  CB  . ALA A 1 372 ? 27.068  -23.805 -13.986 1.00 22.99 ? 372  ALA A CB  1 
ATOM   1550 N  N   . SER A 1 373 ? 25.649  -26.473 -14.500 1.00 23.19 ? 373  SER A N   1 
ATOM   1551 C  CA  . SER A 1 373 ? 24.683  -27.497 -14.129 1.00 23.75 ? 373  SER A CA  1 
ATOM   1552 C  C   . SER A 1 373 ? 25.131  -28.270 -12.889 1.00 23.00 ? 373  SER A C   1 
ATOM   1553 O  O   . SER A 1 373 ? 26.318  -28.448 -12.659 1.00 22.63 ? 373  SER A O   1 
ATOM   1554 C  CB  . SER A 1 373 ? 24.476  -28.494 -15.273 1.00 23.51 ? 373  SER A CB  1 
ATOM   1555 O  OG  . SER A 1 373 ? 23.323  -29.294 -15.014 1.00 23.11 ? 373  SER A OG  1 
ATOM   1556 N  N   . ALA A 1 374 ? 24.164  -28.730 -12.108 1.00 23.67 ? 374  ALA A N   1 
ATOM   1557 C  CA  . ALA A 1 374 ? 24.433  -29.643 -10.995 1.00 23.88 ? 374  ALA A CA  1 
ATOM   1558 C  C   . ALA A 1 374 ? 23.190  -30.457 -10.708 1.00 25.91 ? 374  ALA A C   1 
ATOM   1559 O  O   . ALA A 1 374 ? 22.059  -30.038 -11.029 1.00 24.36 ? 374  ALA A O   1 
ATOM   1560 C  CB  . ALA A 1 374 ? 24.848  -28.870 -9.758  1.00 24.21 ? 374  ALA A CB  1 
ATOM   1561 N  N   . THR A 1 375 ? 23.406  -31.617 -10.089 1.00 27.21 ? 375  THR A N   1 
ATOM   1562 C  CA  . THR A 1 375 ? 22.337  -32.533 -9.735  1.00 27.28 ? 375  THR A CA  1 
ATOM   1563 C  C   . THR A 1 375 ? 21.980  -32.336 -8.267  1.00 29.24 ? 375  THR A C   1 
ATOM   1564 O  O   . THR A 1 375 ? 22.869  -32.298 -7.395  1.00 31.10 ? 375  THR A O   1 
ATOM   1565 C  CB  . THR A 1 375 ? 22.768  -33.996 -9.968  1.00 28.32 ? 375  THR A CB  1 
ATOM   1566 O  OG1 . THR A 1 375 ? 23.291  -34.142 -11.298 1.00 26.98 ? 375  THR A OG1 1 
ATOM   1567 C  CG2 . THR A 1 375 ? 21.591  -34.949 -9.785  1.00 28.89 ? 375  THR A CG2 1 
ATOM   1568 N  N   . LEU A 1 376 ? 20.683  -32.202 -7.998  1.00 27.47 ? 376  LEU A N   1 
ATOM   1569 C  CA  . LEU A 1 376 ? 20.178  -32.053 -6.652  1.00 27.35 ? 376  LEU A CA  1 
ATOM   1570 C  C   . LEU A 1 376 ? 19.537  -33.376 -6.234  1.00 27.62 ? 376  LEU A C   1 
ATOM   1571 O  O   . LEU A 1 376 ? 18.689  -33.908 -6.955  1.00 27.73 ? 376  LEU A O   1 
ATOM   1572 C  CB  . LEU A 1 376 ? 19.130  -30.939 -6.587  1.00 27.80 ? 376  LEU A CB  1 
ATOM   1573 C  CG  . LEU A 1 376 ? 19.492  -29.555 -7.151  1.00 28.48 ? 376  LEU A CG  1 
ATOM   1574 C  CD1 . LEU A 1 376 ? 18.528  -28.512 -6.607  1.00 28.20 ? 376  LEU A CD1 1 
ATOM   1575 C  CD2 . LEU A 1 376 ? 20.923  -29.150 -6.842  1.00 28.76 ? 376  LEU A CD2 1 
ATOM   1576 N  N   . TYR A 1 377 ? 19.970  -33.908 -5.091  1.00 27.60 ? 377  TYR A N   1 
ATOM   1577 C  CA  . TYR A 1 377 ? 19.324  -35.062 -4.450  1.00 27.82 ? 377  TYR A CA  1 
ATOM   1578 C  C   . TYR A 1 377 ? 18.602  -34.549 -3.226  1.00 27.66 ? 377  TYR A C   1 
ATOM   1579 O  O   . TYR A 1 377 ? 19.208  -33.927 -2.342  1.00 26.10 ? 377  TYR A O   1 
ATOM   1580 C  CB  . TYR A 1 377 ? 20.349  -36.117 -4.045  1.00 27.46 ? 377  TYR A CB  1 
ATOM   1581 C  CG  . TYR A 1 377 ? 21.038  -36.748 -5.223  1.00 27.00 ? 377  TYR A CG  1 
ATOM   1582 C  CD1 . TYR A 1 377 ? 20.427  -37.770 -5.952  1.00 28.00 ? 377  TYR A CD1 1 
ATOM   1583 C  CD2 . TYR A 1 377 ? 22.296  -36.326 -5.618  1.00 26.72 ? 377  TYR A CD2 1 
ATOM   1584 C  CE1 . TYR A 1 377 ? 21.058  -38.342 -7.051  1.00 27.12 ? 377  TYR A CE1 1 
ATOM   1585 C  CE2 . TYR A 1 377 ? 22.934  -36.896 -6.706  1.00 26.38 ? 377  TYR A CE2 1 
ATOM   1586 C  CZ  . TYR A 1 377 ? 22.309  -37.897 -7.416  1.00 26.45 ? 377  TYR A CZ  1 
ATOM   1587 O  OH  . TYR A 1 377 ? 22.953  -38.450 -8.493  1.00 26.66 ? 377  TYR A OH  1 
ATOM   1588 N  N   . LEU A 1 378 ? 17.298  -34.781 -3.200  1.00 28.03 ? 378  LEU A N   1 
ATOM   1589 C  CA  . LEU A 1 378 ? 16.455  -34.323 -2.118  1.00 31.04 ? 378  LEU A CA  1 
ATOM   1590 C  C   . LEU A 1 378 ? 15.995  -35.519 -1.298  1.00 33.17 ? 378  LEU A C   1 
ATOM   1591 O  O   . LEU A 1 378 ? 16.124  -36.668 -1.723  1.00 31.74 ? 378  LEU A O   1 
ATOM   1592 C  CB  . LEU A 1 378 ? 15.222  -33.601 -2.664  1.00 30.75 ? 378  LEU A CB  1 
ATOM   1593 C  CG  . LEU A 1 378 ? 15.420  -32.556 -3.765  1.00 31.28 ? 378  LEU A CG  1 
ATOM   1594 C  CD1 . LEU A 1 378 ? 14.117  -31.810 -4.014  1.00 31.20 ? 378  LEU A CD1 1 
ATOM   1595 C  CD2 . LEU A 1 378 ? 16.521  -31.580 -3.408  1.00 31.55 ? 378  LEU A CD2 1 
ATOM   1596 N  N   . THR A 1 379 ? 15.433  -35.229 -0.131  1.00 35.73 ? 379  THR A N   1 
ATOM   1597 C  CA  . THR A 1 379 ? 14.757  -36.244 0.658   1.00 37.73 ? 379  THR A CA  1 
ATOM   1598 C  C   . THR A 1 379 ? 13.481  -35.690 1.257   1.00 37.43 ? 379  THR A C   1 
ATOM   1599 O  O   . THR A 1 379 ? 13.360  -34.498 1.544   1.00 35.34 ? 379  THR A O   1 
ATOM   1600 C  CB  . THR A 1 379 ? 15.649  -36.810 1.778   1.00 38.52 ? 379  THR A CB  1 
ATOM   1601 O  OG1 . THR A 1 379 ? 16.172  -35.731 2.556   1.00 39.78 ? 379  THR A OG1 1 
ATOM   1602 C  CG2 . THR A 1 379 ? 16.802  -37.613 1.187   1.00 39.44 ? 379  THR A CG2 1 
ATOM   1603 N  N   . ASP A 1 380 ? 12.548  -36.612 1.442   1.00 39.52 ? 380  ASP A N   1 
ATOM   1604 C  CA  . ASP A 1 380 ? 11.195  -36.346 1.840   1.00 41.57 ? 380  ASP A CA  1 
ATOM   1605 C  C   . ASP A 1 380 ? 11.012  -36.974 3.222   1.00 44.21 ? 380  ASP A C   1 
ATOM   1606 O  O   . ASP A 1 380 ? 10.965  -38.194 3.347   1.00 40.54 ? 380  ASP A O   1 
ATOM   1607 C  CB  . ASP A 1 380 ? 10.282  -37.002 0.800   1.00 40.26 ? 380  ASP A CB  1 
ATOM   1608 C  CG  . ASP A 1 380 ? 8.834   -37.002 1.189   1.00 38.75 ? 380  ASP A CG  1 
ATOM   1609 O  OD1 . ASP A 1 380 ? 8.436   -36.202 2.058   1.00 38.54 ? 380  ASP A OD1 1 
ATOM   1610 O  OD2 . ASP A 1 380 ? 8.091   -37.813 0.599   1.00 40.38 ? 380  ASP A OD2 1 
ATOM   1611 N  N   . ASN A 1 381 ? 10.929  -36.144 4.257   1.00 48.84 ? 381  ASN A N   1 
ATOM   1612 C  CA  . ASN A 1 381 ? 10.757  -36.657 5.616   1.00 54.22 ? 381  ASN A CA  1 
ATOM   1613 C  C   . ASN A 1 381 ? 9.669   -35.937 6.393   1.00 54.55 ? 381  ASN A C   1 
ATOM   1614 O  O   . ASN A 1 381 ? 9.872   -34.828 6.887   1.00 55.70 ? 381  ASN A O   1 
ATOM   1615 C  CB  . ASN A 1 381 ? 12.077  -36.615 6.389   1.00 56.17 ? 381  ASN A CB  1 
ATOM   1616 C  CG  . ASN A 1 381 ? 12.103  -37.614 7.533   1.00 59.92 ? 381  ASN A CG  1 
ATOM   1617 O  OD1 . ASN A 1 381 ? 11.106  -37.804 8.233   1.00 61.26 ? 381  ASN A OD1 1 
ATOM   1618 N  ND2 . ASN A 1 381 ? 13.241  -38.271 7.719   1.00 62.65 ? 381  ASN A ND2 1 
ATOM   1619 N  N   . ASN A 1 382 ? 8.513   -36.589 6.485   1.00 56.94 ? 382  ASN A N   1 
ATOM   1620 C  CA  . ASN A 1 382 ? 7.385   -36.099 7.266   1.00 56.81 ? 382  ASN A CA  1 
ATOM   1621 C  C   . ASN A 1 382 ? 6.997   -34.671 6.880   1.00 53.82 ? 382  ASN A C   1 
ATOM   1622 O  O   . ASN A 1 382 ? 7.077   -33.739 7.694   1.00 50.46 ? 382  ASN A O   1 
ATOM   1623 C  CB  . ASN A 1 382 ? 7.700   -36.203 8.765   1.00 59.10 ? 382  ASN A CB  1 
ATOM   1624 C  CG  . ASN A 1 382 ? 6.457   -36.105 9.638   1.00 60.36 ? 382  ASN A CG  1 
ATOM   1625 O  OD1 . ASN A 1 382 ? 5.375   -35.745 9.171   1.00 62.36 ? 382  ASN A OD1 1 
ATOM   1626 N  ND2 . ASN A 1 382 ? 6.609   -36.427 10.915  1.00 61.21 ? 382  ASN A ND2 1 
ATOM   1627 N  N   . GLY A 1 383 ? 6.602   -34.508 5.622   1.00 50.01 ? 383  GLY A N   1 
ATOM   1628 C  CA  . GLY A 1 383 ? 6.101   -33.226 5.133   1.00 49.56 ? 383  GLY A CA  1 
ATOM   1629 C  C   . GLY A 1 383 ? 7.168   -32.196 4.804   1.00 48.11 ? 383  GLY A C   1 
ATOM   1630 O  O   . GLY A 1 383 ? 6.844   -31.116 4.309   1.00 51.43 ? 383  GLY A O   1 
ATOM   1631 N  N   . ASN A 1 384 ? 8.436   -32.511 5.064   1.00 45.61 ? 384  ASN A N   1 
ATOM   1632 C  CA  . ASN A 1 384 ? 9.527   -31.581 4.770   1.00 44.59 ? 384  ASN A CA  1 
ATOM   1633 C  C   . ASN A 1 384 ? 10.450  -32.133 3.697   1.00 42.87 ? 384  ASN A C   1 
ATOM   1634 O  O   . ASN A 1 384 ? 10.772  -33.330 3.674   1.00 42.35 ? 384  ASN A O   1 
ATOM   1635 C  CB  . ASN A 1 384 ? 10.342  -31.247 6.022   1.00 45.94 ? 384  ASN A CB  1 
ATOM   1636 C  CG  . ASN A 1 384 ? 9.606   -30.309 6.973   1.00 48.10 ? 384  ASN A CG  1 
ATOM   1637 O  OD1 . ASN A 1 384 ? 9.798   -29.088 6.948   1.00 49.65 ? 384  ASN A OD1 1 
ATOM   1638 N  ND2 . ASN A 1 384 ? 8.761   -30.878 7.820   1.00 48.38 ? 384  ASN A ND2 1 
ATOM   1639 N  N   . VAL A 1 385 ? 10.865  -31.244 2.801   1.00 38.56 ? 385  VAL A N   1 
ATOM   1640 C  CA  . VAL A 1 385 ? 11.844  -31.569 1.789   1.00 35.35 ? 385  VAL A CA  1 
ATOM   1641 C  C   . VAL A 1 385 ? 13.165  -30.975 2.234   1.00 31.52 ? 385  VAL A C   1 
ATOM   1642 O  O   . VAL A 1 385 ? 13.227  -29.818 2.654   1.00 31.30 ? 385  VAL A O   1 
ATOM   1643 C  CB  . VAL A 1 385 ? 11.429  -31.008 0.410   1.00 35.68 ? 385  VAL A CB  1 
ATOM   1644 C  CG1 . VAL A 1 385 ? 12.551  -31.167 -0.606  1.00 34.72 ? 385  VAL A CG1 1 
ATOM   1645 C  CG2 . VAL A 1 385 ? 10.161  -31.697 -0.064  1.00 35.91 ? 385  VAL A CG2 1 
ATOM   1646 N  N   . SER A 1 386 ? 14.216  -31.777 2.142   1.00 30.03 ? 386  SER A N   1 
ATOM   1647 C  CA  . SER A 1 386 ? 15.563  -31.327 2.452   1.00 31.45 ? 386  SER A CA  1 
ATOM   1648 C  C   . SER A 1 386 ? 16.444  -31.505 1.253   1.00 29.16 ? 386  SER A C   1 
ATOM   1649 O  O   . SER A 1 386 ? 16.215  -32.397 0.438   1.00 28.13 ? 386  SER A O   1 
ATOM   1650 C  CB  . SER A 1 386 ? 16.144  -32.157 3.595   1.00 31.79 ? 386  SER A CB  1 
ATOM   1651 O  OG  . SER A 1 386 ? 15.218  -32.178 4.650   1.00 35.34 ? 386  SER A OG  1 
ATOM   1652 N  N   . LEU A 1 387 ? 17.472  -30.673 1.177   1.00 29.05 ? 387  LEU A N   1 
ATOM   1653 C  CA  . LEU A 1 387 ? 18.507  -30.830 0.183   1.00 31.40 ? 387  LEU A CA  1 
ATOM   1654 C  C   . LEU A 1 387 ? 19.617  -31.711 0.750   1.00 31.83 ? 387  LEU A C   1 
ATOM   1655 O  O   . LEU A 1 387 ? 20.367  -31.270 1.611   1.00 30.10 ? 387  LEU A O   1 
ATOM   1656 C  CB  . LEU A 1 387 ? 19.080  -29.471 -0.232  1.00 31.35 ? 387  LEU A CB  1 
ATOM   1657 C  CG  . LEU A 1 387 ? 20.279  -29.566 -1.189  1.00 31.96 ? 387  LEU A CG  1 
ATOM   1658 C  CD1 . LEU A 1 387 ? 19.893  -30.219 -2.518  1.00 32.04 ? 387  LEU A CD1 1 
ATOM   1659 C  CD2 . LEU A 1 387 ? 20.896  -28.196 -1.410  1.00 32.49 ? 387  LEU A CD2 1 
ATOM   1660 N  N   . ALA A 1 388 ? 19.719  -32.945 0.248   1.00 33.12 ? 388  ALA A N   1 
ATOM   1661 C  CA  . ALA A 1 388 ? 20.704  -33.911 0.741   1.00 32.67 ? 388  ALA A CA  1 
ATOM   1662 C  C   . ALA A 1 388 ? 22.078  -33.653 0.144   1.00 35.87 ? 388  ALA A C   1 
ATOM   1663 O  O   . ALA A 1 388 ? 23.088  -33.687 0.857   1.00 34.82 ? 388  ALA A O   1 
ATOM   1664 C  CB  . ALA A 1 388 ? 20.264  -35.334 0.423   1.00 32.85 ? 388  ALA A CB  1 
ATOM   1665 N  N   . GLN A 1 389 ? 22.127  -33.400 -1.167  1.00 35.85 ? 389  GLN A N   1 
ATOM   1666 C  CA  . GLN A 1 389 ? 23.404  -33.277 -1.856  1.00 34.44 ? 389  GLN A CA  1 
ATOM   1667 C  C   . GLN A 1 389 ? 23.312  -32.512 -3.177  1.00 33.31 ? 389  GLN A C   1 
ATOM   1668 O  O   . GLN A 1 389 ? 22.345  -32.637 -3.924  1.00 31.26 ? 389  GLN A O   1 
ATOM   1669 C  CB  . GLN A 1 389 ? 23.957  -34.672 -2.129  1.00 36.72 ? 389  GLN A CB  1 
ATOM   1670 C  CG  . GLN A 1 389 ? 25.356  -34.700 -2.729  1.00 39.36 ? 389  GLN A CG  1 
ATOM   1671 C  CD  . GLN A 1 389 ? 25.830  -36.111 -3.017  1.00 42.14 ? 389  GLN A CD  1 
ATOM   1672 O  OE1 . GLN A 1 389 ? 25.161  -37.079 -2.672  1.00 46.86 ? 389  GLN A OE1 1 
ATOM   1673 N  NE2 . GLN A 1 389 ? 26.984  -36.233 -3.656  1.00 43.85 ? 389  GLN A NE2 1 
ATOM   1674 N  N   . VAL A 1 390 ? 24.354  -31.731 -3.433  1.00 31.60 ? 390  VAL A N   1 
ATOM   1675 C  CA  . VAL A 1 390 ? 24.601  -31.097 -4.709  1.00 31.25 ? 390  VAL A CA  1 
ATOM   1676 C  C   . VAL A 1 390 ? 25.816  -31.792 -5.300  1.00 31.61 ? 390  VAL A C   1 
ATOM   1677 O  O   . VAL A 1 390 ? 26.903  -31.714 -4.718  1.00 31.07 ? 390  VAL A O   1 
ATOM   1678 C  CB  . VAL A 1 390 ? 24.944  -29.603 -4.542  1.00 30.16 ? 390  VAL A CB  1 
ATOM   1679 C  CG1 . VAL A 1 390 ? 25.138  -28.948 -5.910  1.00 29.72 ? 390  VAL A CG1 1 
ATOM   1680 C  CG2 . VAL A 1 390 ? 23.865  -28.898 -3.735  1.00 30.06 ? 390  VAL A CG2 1 
ATOM   1681 N  N   . ALA A 1 391 ? 25.622  -32.449 -6.448  1.00 28.77 ? 391  ALA A N   1 
ATOM   1682 C  CA  . ALA A 1 391 ? 26.655  -33.210 -7.136  1.00 27.82 ? 391  ALA A CA  1 
ATOM   1683 C  C   . ALA A 1 391 ? 26.878  -32.699 -8.549  1.00 27.43 ? 391  ALA A C   1 
ATOM   1684 O  O   . ALA A 1 391 ? 26.000  -32.058 -9.145  1.00 25.14 ? 391  ALA A O   1 
ATOM   1685 C  CB  . ALA A 1 391 ? 26.249  -34.677 -7.212  1.00 28.59 ? 391  ALA A CB  1 
ATOM   1686 N  N   . ASN A 1 392 ? 28.058  -33.014 -9.082  1.00 27.92 ? 392  ASN A N   1 
ATOM   1687 C  CA  . ASN A 1 392 ? 28.399  -32.795 -10.493 1.00 28.50 ? 392  ASN A CA  1 
ATOM   1688 C  C   . ASN A 1 392 ? 28.344  -31.334 -10.923 1.00 26.99 ? 392  ASN A C   1 
ATOM   1689 O  O   . ASN A 1 392 ? 28.035  -31.055 -12.074 1.00 26.88 ? 392  ASN A O   1 
ATOM   1690 C  CB  . ASN A 1 392 ? 27.453  -33.594 -11.388 1.00 30.73 ? 392  ASN A CB  1 
ATOM   1691 C  CG  . ASN A 1 392 ? 27.311  -35.034 -10.952 1.00 32.22 ? 392  ASN A CG  1 
ATOM   1692 O  OD1 . ASN A 1 392 ? 28.307  -35.738 -10.822 1.00 33.75 ? 392  ASN A OD1 1 
ATOM   1693 N  ND2 . ASN A 1 392 ? 26.065  -35.489 -10.753 1.00 30.81 ? 392  ASN A ND2 1 
ATOM   1694 N  N   . ASP A 1 393 ? 28.619  -30.403 -10.011 1.00 26.47 ? 393  ASP A N   1 
ATOM   1695 C  CA  . ASP A 1 393 ? 28.537  -28.987 -10.354 1.00 26.50 ? 393  ASP A CA  1 
ATOM   1696 C  C   . ASP A 1 393 ? 29.655  -28.632 -11.317 1.00 27.01 ? 393  ASP A C   1 
ATOM   1697 O  O   . ASP A 1 393 ? 30.827  -28.840 -11.020 1.00 27.84 ? 393  ASP A O   1 
ATOM   1698 C  CB  . ASP A 1 393 ? 28.582  -28.084 -9.124  1.00 26.25 ? 393  ASP A CB  1 
ATOM   1699 C  CG  . ASP A 1 393 ? 28.358  -26.609 -9.472  1.00 26.99 ? 393  ASP A CG  1 
ATOM   1700 O  OD1 . ASP A 1 393 ? 27.349  -26.277 -10.141 1.00 26.20 ? 393  ASP A OD1 1 
ATOM   1701 O  OD2 . ASP A 1 393 ? 29.192  -25.779 -9.065  1.00 26.56 ? 393  ASP A OD2 1 
ATOM   1702 N  N   . HIS A 1 394 ? 29.293  -28.106 -12.483 1.00 26.07 ? 394  HIS A N   1 
ATOM   1703 C  CA  . HIS A 1 394 ? 30.290  -27.781 -13.489 1.00 25.59 ? 394  HIS A CA  1 
ATOM   1704 C  C   . HIS A 1 394 ? 29.771  -26.784 -14.505 1.00 24.64 ? 394  HIS A C   1 
ATOM   1705 O  O   . HIS A 1 394 ? 28.577  -26.566 -14.618 1.00 24.61 ? 394  HIS A O   1 
ATOM   1706 C  CB  . HIS A 1 394 ? 30.788  -29.056 -14.196 1.00 26.91 ? 394  HIS A CB  1 
ATOM   1707 C  CG  . HIS A 1 394 ? 29.785  -29.685 -15.115 1.00 28.05 ? 394  HIS A CG  1 
ATOM   1708 N  ND1 . HIS A 1 394 ? 28.607  -30.247 -14.665 1.00 28.70 ? 394  HIS A ND1 1 
ATOM   1709 C  CD2 . HIS A 1 394 ? 29.805  -29.874 -16.459 1.00 27.74 ? 394  HIS A CD2 1 
ATOM   1710 C  CE1 . HIS A 1 394 ? 27.937  -30.735 -15.698 1.00 28.83 ? 394  HIS A CE1 1 
ATOM   1711 N  NE2 . HIS A 1 394 ? 28.645  -30.528 -16.795 1.00 26.89 ? 394  HIS A NE2 1 
ATOM   1712 N  N   . ILE A 1 395 ? 30.703  -26.200 -15.242 1.00 24.21 ? 395  ILE A N   1 
ATOM   1713 C  CA  . ILE A 1 395 ? 30.396  -25.278 -16.311 1.00 24.14 ? 395  ILE A CA  1 
ATOM   1714 C  C   . ILE A 1 395 ? 30.052  -26.067 -17.576 1.00 23.64 ? 395  ILE A C   1 
ATOM   1715 O  O   . ILE A 1 395 ? 30.828  -26.915 -18.012 1.00 23.90 ? 395  ILE A O   1 
ATOM   1716 C  CB  . ILE A 1 395 ? 31.587  -24.349 -16.598 1.00 22.10 ? 395  ILE A CB  1 
ATOM   1717 C  CG1 . ILE A 1 395 ? 31.962  -23.550 -15.348 1.00 22.49 ? 395  ILE A CG1 1 
ATOM   1718 C  CG2 . ILE A 1 395 ? 31.274  -23.434 -17.773 1.00 22.71 ? 395  ILE A CG2 1 
ATOM   1719 C  CD1 . ILE A 1 395 ? 30.817  -22.805 -14.679 1.00 21.96 ? 395  ILE A CD1 1 
ATOM   1720 N  N   . VAL A 1 396 ? 28.896  -25.761 -18.159 1.00 22.16 ? 396  VAL A N   1 
ATOM   1721 C  CA  . VAL A 1 396 ? 28.460  -26.373 -19.403 1.00 21.09 ? 396  VAL A CA  1 
ATOM   1722 C  C   . VAL A 1 396 ? 28.939  -25.565 -20.601 1.00 21.73 ? 396  VAL A C   1 
ATOM   1723 O  O   . VAL A 1 396 ? 29.457  -26.129 -21.567 1.00 21.21 ? 396  VAL A O   1 
ATOM   1724 C  CB  . VAL A 1 396 ? 26.924  -26.480 -19.454 1.00 21.50 ? 396  VAL A CB  1 
ATOM   1725 C  CG1 . VAL A 1 396 ? 26.468  -26.990 -20.817 1.00 21.51 ? 396  VAL A CG1 1 
ATOM   1726 C  CG2 . VAL A 1 396 ? 26.408  -27.391 -18.335 1.00 21.40 ? 396  VAL A CG2 1 
ATOM   1727 N  N   . PHE A 1 397 ? 28.735  -24.247 -20.563 1.00 21.31 ? 397  PHE A N   1 
ATOM   1728 C  CA  . PHE A 1 397 ? 29.065  -23.409 -21.711 1.00 20.91 ? 397  PHE A CA  1 
ATOM   1729 C  C   . PHE A 1 397 ? 29.191  -21.958 -21.289 1.00 20.82 ? 397  PHE A C   1 
ATOM   1730 O  O   . PHE A 1 397 ? 28.445  -21.486 -20.423 1.00 20.27 ? 397  PHE A O   1 
ATOM   1731 C  CB  . PHE A 1 397 ? 27.976  -23.567 -22.778 1.00 21.17 ? 397  PHE A CB  1 
ATOM   1732 C  CG  . PHE A 1 397 ? 28.253  -22.842 -24.076 1.00 20.91 ? 397  PHE A CG  1 
ATOM   1733 C  CD1 . PHE A 1 397 ? 29.299  -23.234 -24.895 1.00 20.33 ? 397  PHE A CD1 1 
ATOM   1734 C  CD2 . PHE A 1 397 ? 27.409  -21.803 -24.510 1.00 20.73 ? 397  PHE A CD2 1 
ATOM   1735 C  CE1 . PHE A 1 397 ? 29.532  -22.587 -26.099 1.00 21.16 ? 397  PHE A CE1 1 
ATOM   1736 C  CE2 . PHE A 1 397 ? 27.639  -21.149 -25.710 1.00 20.43 ? 397  PHE A CE2 1 
ATOM   1737 C  CZ  . PHE A 1 397 ? 28.707  -21.536 -26.509 1.00 20.99 ? 397  PHE A CZ  1 
ATOM   1738 N  N   . GLU A 1 398 ? 30.140  -21.245 -21.883 1.00 21.49 ? 398  GLU A N   1 
ATOM   1739 C  CA  . GLU A 1 398 ? 30.220  -19.802 -21.667 1.00 23.08 ? 398  GLU A CA  1 
ATOM   1740 C  C   . GLU A 1 398 ? 30.510  -18.993 -22.938 1.00 22.44 ? 398  GLU A C   1 
ATOM   1741 O  O   . GLU A 1 398 ? 30.965  -17.859 -22.864 1.00 22.66 ? 398  GLU A O   1 
ATOM   1742 C  CB  . GLU A 1 398 ? 31.219  -19.473 -20.558 1.00 24.49 ? 398  GLU A CB  1 
ATOM   1743 C  CG  . GLU A 1 398 ? 32.658  -19.877 -20.829 1.00 25.69 ? 398  GLU A CG  1 
ATOM   1744 C  CD  . GLU A 1 398 ? 33.604  -19.228 -19.827 1.00 27.90 ? 398  GLU A CD  1 
ATOM   1745 O  OE1 . GLU A 1 398 ? 33.741  -17.980 -19.852 1.00 28.05 ? 398  GLU A OE1 1 
ATOM   1746 O  OE2 . GLU A 1 398 ? 34.187  -19.962 -19.002 1.00 27.24 ? 398  GLU A OE2 1 
ATOM   1747 N  N   . GLY A 1 399 ? 30.182  -19.554 -24.095 1.00 21.38 ? 399  GLY A N   1 
ATOM   1748 C  CA  . GLY A 1 399 ? 30.329  -18.838 -25.355 1.00 21.44 ? 399  GLY A CA  1 
ATOM   1749 C  C   . GLY A 1 399 ? 31.469  -19.404 -26.168 1.00 21.05 ? 399  GLY A C   1 
ATOM   1750 O  O   . GLY A 1 399 ? 32.436  -19.909 -25.615 1.00 21.07 ? 399  GLY A O   1 
ATOM   1751 N  N   . ASP A 1 400 ? 31.352  -19.316 -27.489 1.00 21.29 ? 400  ASP A N   1 
ATOM   1752 C  CA  . ASP A 1 400 ? 32.373  -19.864 -28.399 1.00 20.97 ? 400  ASP A CA  1 
ATOM   1753 C  C   . ASP A 1 400 ? 33.123  -18.784 -29.218 1.00 20.58 ? 400  ASP A C   1 
ATOM   1754 O  O   . ASP A 1 400 ? 34.210  -19.059 -29.722 1.00 19.58 ? 400  ASP A O   1 
ATOM   1755 C  CB  . ASP A 1 400 ? 31.716  -20.827 -29.375 1.00 20.35 ? 400  ASP A CB  1 
ATOM   1756 C  CG  . ASP A 1 400 ? 30.728  -20.123 -30.284 1.00 19.98 ? 400  ASP A CG  1 
ATOM   1757 O  OD1 . ASP A 1 400 ? 29.754  -19.548 -29.746 1.00 19.06 ? 400  ASP A OD1 1 
ATOM   1758 O  OD2 . ASP A 1 400 ? 30.936  -20.119 -31.516 1.00 19.33 ? 400  ASP A OD2 1 
ATOM   1759 N  N   . GLY A 1 401 ? 32.526  -17.593 -29.385 1.00 18.66 ? 401  GLY A N   1 
ATOM   1760 C  CA  . GLY A 1 401 ? 33.178  -16.485 -30.110 1.00 17.69 ? 401  GLY A CA  1 
ATOM   1761 C  C   . GLY A 1 401 ? 32.685  -16.289 -31.537 1.00 16.82 ? 401  GLY A C   1 
ATOM   1762 O  O   . GLY A 1 401 ? 32.752  -15.190 -32.084 1.00 16.39 ? 401  GLY A O   1 
ATOM   1763 N  N   . TYR A 1 402 ? 32.182  -17.357 -32.139 1.00 16.98 ? 402  TYR A N   1 
ATOM   1764 C  CA  . TYR A 1 402 ? 31.566  -17.281 -33.462 1.00 16.79 ? 402  TYR A CA  1 
ATOM   1765 C  C   . TYR A 1 402 ? 30.033  -17.114 -33.355 1.00 16.87 ? 402  TYR A C   1 
ATOM   1766 O  O   . TYR A 1 402 ? 29.486  -16.097 -33.791 1.00 18.33 ? 402  TYR A O   1 
ATOM   1767 C  CB  . TYR A 1 402 ? 31.934  -18.509 -34.286 1.00 16.20 ? 402  TYR A CB  1 
ATOM   1768 C  CG  . TYR A 1 402 ? 31.356  -18.463 -35.668 1.00 16.73 ? 402  TYR A CG  1 
ATOM   1769 C  CD1 . TYR A 1 402 ? 31.832  -17.549 -36.609 1.00 16.29 ? 402  TYR A CD1 1 
ATOM   1770 C  CD2 . TYR A 1 402 ? 30.309  -19.317 -36.038 1.00 16.54 ? 402  TYR A CD2 1 
ATOM   1771 C  CE1 . TYR A 1 402 ? 31.300  -17.498 -37.881 1.00 16.57 ? 402  TYR A CE1 1 
ATOM   1772 C  CE2 . TYR A 1 402 ? 29.767  -19.262 -37.309 1.00 16.50 ? 402  TYR A CE2 1 
ATOM   1773 C  CZ  . TYR A 1 402 ? 30.272  -18.354 -38.224 1.00 16.75 ? 402  TYR A CZ  1 
ATOM   1774 O  OH  . TYR A 1 402 ? 29.745  -18.286 -39.488 1.00 16.49 ? 402  TYR A OH  1 
ATOM   1775 N  N   . TYR A 1 403 ? 29.344  -18.094 -32.786 1.00 17.03 ? 403  TYR A N   1 
ATOM   1776 C  CA  . TYR A 1 403 ? 27.883  -18.005 -32.578 1.00 17.42 ? 403  TYR A CA  1 
ATOM   1777 C  C   . TYR A 1 403 ? 27.527  -17.068 -31.442 1.00 17.21 ? 403  TYR A C   1 
ATOM   1778 O  O   . TYR A 1 403 ? 26.598  -16.251 -31.579 1.00 16.15 ? 403  TYR A O   1 
ATOM   1779 C  CB  . TYR A 1 403 ? 27.271  -19.383 -32.281 1.00 17.83 ? 403  TYR A CB  1 
ATOM   1780 C  CG  . TYR A 1 403 ? 27.409  -20.340 -33.434 1.00 18.46 ? 403  TYR A CG  1 
ATOM   1781 C  CD1 . TYR A 1 403 ? 26.823  -20.061 -34.662 1.00 18.49 ? 403  TYR A CD1 1 
ATOM   1782 C  CD2 . TYR A 1 403 ? 28.144  -21.516 -33.298 1.00 19.51 ? 403  TYR A CD2 1 
ATOM   1783 C  CE1 . TYR A 1 403 ? 26.963  -20.925 -35.735 1.00 19.28 ? 403  TYR A CE1 1 
ATOM   1784 C  CE2 . TYR A 1 403 ? 28.289  -22.396 -34.353 1.00 20.07 ? 403  TYR A CE2 1 
ATOM   1785 C  CZ  . TYR A 1 403 ? 27.701  -22.098 -35.570 1.00 20.40 ? 403  TYR A CZ  1 
ATOM   1786 O  OH  . TYR A 1 403 ? 27.867  -22.980 -36.614 1.00 21.44 ? 403  TYR A OH  1 
ATOM   1787 N  N   . TYR A 1 404 ? 28.257  -17.199 -30.330 1.00 16.69 ? 404  TYR A N   1 
ATOM   1788 C  CA  . TYR A 1 404 ? 27.957  -16.472 -29.110 1.00 17.61 ? 404  TYR A CA  1 
ATOM   1789 C  C   . TYR A 1 404 ? 29.181  -15.725 -28.605 1.00 18.54 ? 404  TYR A C   1 
ATOM   1790 O  O   . TYR A 1 404 ? 30.295  -16.202 -28.749 1.00 20.87 ? 404  TYR A O   1 
ATOM   1791 C  CB  . TYR A 1 404 ? 27.380  -17.425 -28.072 1.00 17.49 ? 404  TYR A CB  1 
ATOM   1792 C  CG  . TYR A 1 404 ? 26.187  -18.135 -28.661 1.00 17.75 ? 404  TYR A CG  1 
ATOM   1793 C  CD1 . TYR A 1 404 ? 24.975  -17.455 -28.865 1.00 17.01 ? 404  TYR A CD1 1 
ATOM   1794 C  CD2 . TYR A 1 404 ? 26.282  -19.459 -29.093 1.00 17.64 ? 404  TYR A CD2 1 
ATOM   1795 C  CE1 . TYR A 1 404 ? 23.909  -18.083 -29.447 1.00 16.82 ? 404  TYR A CE1 1 
ATOM   1796 C  CE2 . TYR A 1 404 ? 25.202  -20.097 -29.663 1.00 17.25 ? 404  TYR A CE2 1 
ATOM   1797 C  CZ  . TYR A 1 404 ? 24.028  -19.407 -29.853 1.00 16.67 ? 404  TYR A CZ  1 
ATOM   1798 O  OH  . TYR A 1 404 ? 22.977  -20.054 -30.445 1.00 15.73 ? 404  TYR A OH  1 
ATOM   1799 N  N   . GLN A 1 405 ? 28.955  -14.522 -28.075 1.00 18.35 ? 405  GLN A N   1 
ATOM   1800 C  CA  . GLN A 1 405 ? 30.016  -13.666 -27.538 1.00 17.97 ? 405  GLN A CA  1 
ATOM   1801 C  C   . GLN A 1 405 ? 30.633  -14.281 -26.281 1.00 17.59 ? 405  GLN A C   1 
ATOM   1802 O  O   . GLN A 1 405 ? 29.916  -14.769 -25.401 1.00 15.88 ? 405  GLN A O   1 
ATOM   1803 C  CB  . GLN A 1 405 ? 29.456  -12.288 -27.184 1.00 17.88 ? 405  GLN A CB  1 
ATOM   1804 C  CG  . GLN A 1 405 ? 30.510  -11.226 -26.951 1.00 18.35 ? 405  GLN A CG  1 
ATOM   1805 C  CD  . GLN A 1 405 ? 29.930  -9.944  -26.367 1.00 18.74 ? 405  GLN A CD  1 
ATOM   1806 O  OE1 . GLN A 1 405 ? 29.068  -9.981  -25.499 1.00 18.87 ? 405  GLN A OE1 1 
ATOM   1807 N  NE2 . GLN A 1 405 ? 30.438  -8.803  -26.813 1.00 19.80 ? 405  GLN A NE2 1 
ATOM   1808 N  N   . THR A 1 406 ? 31.962  -14.221 -26.199 1.00 17.56 ? 406  THR A N   1 
ATOM   1809 C  CA  . THR A 1 406 ? 32.694  -14.742 -25.070 1.00 18.68 ? 406  THR A CA  1 
ATOM   1810 C  C   . THR A 1 406 ? 32.952  -13.627 -24.096 1.00 19.42 ? 406  THR A C   1 
ATOM   1811 O  O   . THR A 1 406 ? 32.863  -12.439 -24.450 1.00 19.57 ? 406  THR A O   1 
ATOM   1812 C  CB  . THR A 1 406 ? 34.062  -15.345 -25.465 1.00 18.82 ? 406  THR A CB  1 
ATOM   1813 O  OG1 . THR A 1 406 ? 34.909  -14.328 -26.018 1.00 19.49 ? 406  THR A OG1 1 
ATOM   1814 C  CG2 . THR A 1 406 ? 33.887  -16.496 -26.459 1.00 18.09 ? 406  THR A CG2 1 
ATOM   1815 N  N   . TYR A 1 407 ? 33.276  -14.010 -22.868 1.00 19.81 ? 407  TYR A N   1 
ATOM   1816 C  CA  . TYR A 1 407 ? 33.713  -13.039 -21.877 1.00 21.25 ? 407  TYR A CA  1 
ATOM   1817 C  C   . TYR A 1 407 ? 34.889  -12.211 -22.399 1.00 20.91 ? 407  TYR A C   1 
ATOM   1818 O  O   . TYR A 1 407 ? 34.866  -10.982 -22.311 1.00 20.23 ? 407  TYR A O   1 
ATOM   1819 C  CB  . TYR A 1 407 ? 34.121  -13.708 -20.568 1.00 22.29 ? 407  TYR A CB  1 
ATOM   1820 C  CG  . TYR A 1 407 ? 34.622  -12.698 -19.547 1.00 22.95 ? 407  TYR A CG  1 
ATOM   1821 C  CD1 . TYR A 1 407 ? 33.726  -11.888 -18.856 1.00 23.56 ? 407  TYR A CD1 1 
ATOM   1822 C  CD2 . TYR A 1 407 ? 35.981  -12.531 -19.306 1.00 23.88 ? 407  TYR A CD2 1 
ATOM   1823 C  CE1 . TYR A 1 407 ? 34.160  -10.957 -17.935 1.00 24.43 ? 407  TYR A CE1 1 
ATOM   1824 C  CE2 . TYR A 1 407 ? 36.435  -11.593 -18.388 1.00 24.55 ? 407  TYR A CE2 1 
ATOM   1825 C  CZ  . TYR A 1 407 ? 35.517  -10.815 -17.702 1.00 25.69 ? 407  TYR A CZ  1 
ATOM   1826 O  OH  . TYR A 1 407 ? 35.934  -9.885  -16.786 1.00 27.20 ? 407  TYR A OH  1 
ATOM   1827 N  N   . ASP A 1 408 ? 35.911  -12.891 -22.911 1.00 21.50 ? 408  ASP A N   1 
ATOM   1828 C  CA  . ASP A 1 408 ? 37.127  -12.221 -23.408 1.00 23.15 ? 408  ASP A CA  1 
ATOM   1829 C  C   . ASP A 1 408 ? 36.828  -11.248 -24.535 1.00 22.25 ? 408  ASP A C   1 
ATOM   1830 O  O   . ASP A 1 408 ? 37.472  -10.211 -24.641 1.00 23.15 ? 408  ASP A O   1 
ATOM   1831 C  CB  . ASP A 1 408 ? 38.173  -13.234 -23.913 1.00 24.35 ? 408  ASP A CB  1 
ATOM   1832 C  CG  . ASP A 1 408 ? 38.824  -14.021 -22.799 1.00 25.97 ? 408  ASP A CG  1 
ATOM   1833 O  OD1 . ASP A 1 408 ? 38.810  -13.565 -21.641 1.00 29.07 ? 408  ASP A OD1 1 
ATOM   1834 O  OD2 . ASP A 1 408 ? 39.366  -15.104 -23.084 1.00 27.48 ? 408  ASP A OD2 1 
ATOM   1835 N  N   . GLN A 1 409 ? 35.880  -11.582 -25.402 1.00 21.85 ? 409  GLN A N   1 
ATOM   1836 C  CA  . GLN A 1 409 ? 35.501  -10.637 -26.462 1.00 21.76 ? 409  GLN A CA  1 
ATOM   1837 C  C   . GLN A 1 409 ? 34.884  -9.373  -25.860 1.00 21.23 ? 409  GLN A C   1 
ATOM   1838 O  O   . GLN A 1 409 ? 35.249  -8.257  -26.236 1.00 20.95 ? 409  GLN A O   1 
ATOM   1839 C  CB  . GLN A 1 409 ? 34.532  -11.267 -27.447 1.00 21.33 ? 409  GLN A CB  1 
ATOM   1840 C  CG  . GLN A 1 409 ? 35.181  -12.246 -28.404 1.00 21.51 ? 409  GLN A CG  1 
ATOM   1841 C  CD  . GLN A 1 409 ? 34.148  -13.033 -29.187 1.00 21.47 ? 409  GLN A CD  1 
ATOM   1842 O  OE1 . GLN A 1 409 ? 33.093  -13.393 -28.658 1.00 20.54 ? 409  GLN A OE1 1 
ATOM   1843 N  NE2 . GLN A 1 409 ? 34.440  -13.304 -30.452 1.00 21.21 ? 409  GLN A NE2 1 
ATOM   1844 N  N   . TRP A 1 410 ? 33.952  -9.554  -24.932 1.00 20.59 ? 410  TRP A N   1 
ATOM   1845 C  CA  . TRP A 1 410 ? 33.303  -8.421  -24.271 1.00 21.73 ? 410  TRP A CA  1 
ATOM   1846 C  C   . TRP A 1 410 ? 34.323  -7.543  -23.515 1.00 23.37 ? 410  TRP A C   1 
ATOM   1847 O  O   . TRP A 1 410 ? 34.266  -6.316  -23.592 1.00 22.15 ? 410  TRP A O   1 
ATOM   1848 C  CB  . TRP A 1 410 ? 32.221  -8.910  -23.304 1.00 21.41 ? 410  TRP A CB  1 
ATOM   1849 C  CG  . TRP A 1 410 ? 31.663  -7.841  -22.418 1.00 21.60 ? 410  TRP A CG  1 
ATOM   1850 C  CD1 . TRP A 1 410 ? 30.681  -6.944  -22.728 1.00 20.64 ? 410  TRP A CD1 1 
ATOM   1851 C  CD2 . TRP A 1 410 ? 32.053  -7.558  -21.064 1.00 21.25 ? 410  TRP A CD2 1 
ATOM   1852 N  NE1 . TRP A 1 410 ? 30.442  -6.118  -21.658 1.00 20.80 ? 410  TRP A NE1 1 
ATOM   1853 C  CE2 . TRP A 1 410 ? 31.271  -6.470  -20.625 1.00 21.50 ? 410  TRP A CE2 1 
ATOM   1854 C  CE3 . TRP A 1 410 ? 32.978  -8.122  -20.187 1.00 21.53 ? 410  TRP A CE3 1 
ATOM   1855 C  CZ2 . TRP A 1 410 ? 31.382  -5.935  -19.339 1.00 22.21 ? 410  TRP A CZ2 1 
ATOM   1856 C  CZ3 . TRP A 1 410 ? 33.100  -7.585  -18.911 1.00 22.81 ? 410  TRP A CZ3 1 
ATOM   1857 C  CH2 . TRP A 1 410 ? 32.303  -6.506  -18.496 1.00 22.72 ? 410  TRP A CH2 1 
ATOM   1858 N  N   . LYS A 1 411 ? 35.227  -8.185  -22.778 1.00 23.59 ? 411  LYS A N   1 
ATOM   1859 C  CA  . LYS A 1 411 ? 36.207  -7.476  -21.965 1.00 25.23 ? 411  LYS A CA  1 
ATOM   1860 C  C   . LYS A 1 411 ? 37.156  -6.660  -22.832 1.00 25.41 ? 411  LYS A C   1 
ATOM   1861 O  O   . LYS A 1 411 ? 37.529  -5.562  -22.470 1.00 25.86 ? 411  LYS A O   1 
ATOM   1862 C  CB  . LYS A 1 411 ? 37.028  -8.454  -21.133 1.00 26.91 ? 411  LYS A CB  1 
ATOM   1863 C  CG  . LYS A 1 411 ? 38.009  -7.778  -20.185 1.00 28.62 ? 411  LYS A CG  1 
ATOM   1864 C  CD  . LYS A 1 411 ? 38.765  -8.816  -19.379 1.00 30.40 ? 411  LYS A CD  1 
ATOM   1865 C  CE  . LYS A 1 411 ? 40.060  -8.270  -18.806 1.00 31.77 ? 411  LYS A CE  1 
ATOM   1866 N  NZ  . LYS A 1 411 ? 40.745  -9.329  -18.002 1.00 33.25 ? 411  LYS A NZ  1 
ATOM   1867 N  N   . ALA A 1 412 ? 37.524  -7.205  -23.980 1.00 25.27 ? 412  ALA A N   1 
ATOM   1868 C  CA  . ALA A 1 412 ? 38.446  -6.544  -24.885 1.00 26.45 ? 412  ALA A CA  1 
ATOM   1869 C  C   . ALA A 1 412 ? 37.978  -5.167  -25.367 1.00 26.73 ? 412  ALA A C   1 
ATOM   1870 O  O   . ALA A 1 412 ? 38.788  -4.249  -25.465 1.00 26.05 ? 412  ALA A O   1 
ATOM   1871 C  CB  . ALA A 1 412 ? 38.745  -7.452  -26.069 1.00 26.20 ? 412  ALA A CB  1 
ATOM   1872 N  N   . THR A 1 413 ? 36.686  -5.012  -25.663 1.00 27.84 ? 413  THR A N   1 
ATOM   1873 C  CA  . THR A 1 413 ? 36.185  -3.748  -26.224 1.00 27.33 ? 413  THR A CA  1 
ATOM   1874 C  C   . THR A 1 413 ? 35.274  -2.953  -25.295 1.00 27.77 ? 413  THR A C   1 
ATOM   1875 O  O   . THR A 1 413 ? 34.894  -1.843  -25.632 1.00 29.20 ? 413  THR A O   1 
ATOM   1876 C  CB  . THR A 1 413 ? 35.424  -3.981  -27.540 1.00 27.62 ? 413  THR A CB  1 
ATOM   1877 O  OG1 . THR A 1 413 ? 34.403  -4.954  -27.331 1.00 27.52 ? 413  THR A OG1 1 
ATOM   1878 C  CG2 . THR A 1 413 ? 36.358  -4.472  -28.632 1.00 27.47 ? 413  THR A CG2 1 
ATOM   1879 N  N   . ASN A 1 414 ? 34.909  -3.485  -24.131 1.00 27.79 ? 414  ASN A N   1 
ATOM   1880 C  CA  . ASN A 1 414 ? 33.939  -2.774  -23.311 1.00 28.57 ? 414  ASN A CA  1 
ATOM   1881 C  C   . ASN A 1 414 ? 34.492  -1.497  -22.657 1.00 30.49 ? 414  ASN A C   1 
ATOM   1882 O  O   . ASN A 1 414 ? 35.436  -1.550  -21.886 1.00 29.46 ? 414  ASN A O   1 
ATOM   1883 C  CB  . ASN A 1 414 ? 33.314  -3.664  -22.241 1.00 27.61 ? 414  ASN A CB  1 
ATOM   1884 C  CG  . ASN A 1 414 ? 32.202  -2.946  -21.480 1.00 27.65 ? 414  ASN A CG  1 
ATOM   1885 O  OD1 . ASN A 1 414 ? 31.431  -2.178  -22.071 1.00 27.45 ? 414  ASN A OD1 1 
ATOM   1886 N  ND2 . ASN A 1 414 ? 32.132  -3.162  -20.177 1.00 26.12 ? 414  ASN A ND2 1 
ATOM   1887 N  N   . LYS A 1 415 ? 33.883  -0.359  -22.976 1.00 32.10 ? 415  LYS A N   1 
ATOM   1888 C  CA  . LYS A 1 415 ? 34.144  0.886   -22.256 1.00 33.93 ? 415  LYS A CA  1 
ATOM   1889 C  C   . LYS A 1 415 ? 32.924  1.333   -21.451 1.00 34.71 ? 415  LYS A C   1 
ATOM   1890 O  O   . LYS A 1 415 ? 32.873  2.475   -20.987 1.00 34.16 ? 415  LYS A O   1 
ATOM   1891 C  CB  . LYS A 1 415 ? 34.559  1.976   -23.236 1.00 34.72 ? 415  LYS A CB  1 
ATOM   1892 C  CG  . LYS A 1 415 ? 35.830  1.649   -23.992 1.00 36.63 ? 415  LYS A CG  1 
ATOM   1893 C  CD  . LYS A 1 415 ? 36.316  2.860   -24.776 1.00 39.31 ? 415  LYS A CD  1 
ATOM   1894 C  CE  . LYS A 1 415 ? 37.612  2.569   -25.515 1.00 40.38 ? 415  LYS A CE  1 
ATOM   1895 N  NZ  . LYS A 1 415 ? 38.731  2.251   -24.583 1.00 41.38 ? 415  LYS A NZ  1 
ATOM   1896 N  N   . GLY A 1 416 ? 31.945  0.434   -21.305 1.00 33.14 ? 416  GLY A N   1 
ATOM   1897 C  CA  . GLY A 1 416 ? 30.754  0.659   -20.475 1.00 32.64 ? 416  GLY A CA  1 
ATOM   1898 C  C   . GLY A 1 416 ? 29.436  0.678   -21.244 1.00 31.35 ? 416  GLY A C   1 
ATOM   1899 O  O   . GLY A 1 416 ? 28.382  0.857   -20.655 1.00 32.32 ? 416  GLY A O   1 
ATOM   1900 N  N   . ALA A 1 417 ? 29.492  0.517   -22.559 1.00 28.38 ? 417  ALA A N   1 
ATOM   1901 C  CA  . ALA A 1 417 ? 28.299  0.576   -23.394 1.00 26.42 ? 417  ALA A CA  1 
ATOM   1902 C  C   . ALA A 1 417 ? 27.810  -0.801  -23.819 1.00 24.24 ? 417  ALA A C   1 
ATOM   1903 O  O   . ALA A 1 417 ? 26.748  -0.911  -24.411 1.00 24.61 ? 417  ALA A O   1 
ATOM   1904 C  CB  . ALA A 1 417 ? 28.557  1.443   -24.624 1.00 26.49 ? 417  ALA A CB  1 
ATOM   1905 N  N   . ASP A 1 418 ? 28.563  -1.848  -23.504 1.00 22.74 ? 418  ASP A N   1 
ATOM   1906 C  CA  . ASP A 1 418 ? 28.250  -3.172  -23.997 1.00 20.83 ? 418  ASP A CA  1 
ATOM   1907 C  C   . ASP A 1 418 ? 27.787  -4.062  -22.870 1.00 20.55 ? 418  ASP A C   1 
ATOM   1908 O  O   . ASP A 1 418 ? 28.414  -4.129  -21.825 1.00 18.42 ? 418  ASP A O   1 
ATOM   1909 C  CB  . ASP A 1 418 ? 29.463  -3.793  -24.673 1.00 21.04 ? 418  ASP A CB  1 
ATOM   1910 C  CG  . ASP A 1 418 ? 29.104  -4.988  -25.548 1.00 20.66 ? 418  ASP A CG  1 
ATOM   1911 O  OD1 . ASP A 1 418 ? 27.933  -5.118  -25.951 1.00 19.58 ? 418  ASP A OD1 1 
ATOM   1912 O  OD2 . ASP A 1 418 ? 30.002  -5.803  -25.834 1.00 20.17 ? 418  ASP A OD2 1 
ATOM   1913 N  N   . ASN A 1 419 ? 26.670  -4.739  -23.109 1.00 19.94 ? 419  ASN A N   1 
ATOM   1914 C  CA  . ASN A 1 419 ? 26.128  -5.691  -22.182 1.00 19.70 ? 419  ASN A CA  1 
ATOM   1915 C  C   . ASN A 1 419 ? 26.895  -6.998  -22.308 1.00 19.78 ? 419  ASN A C   1 
ATOM   1916 O  O   . ASN A 1 419 ? 27.564  -7.254  -23.316 1.00 20.15 ? 419  ASN A O   1 
ATOM   1917 C  CB  . ASN A 1 419 ? 24.646  -5.904  -22.481 1.00 19.76 ? 419  ASN A CB  1 
ATOM   1918 C  CG  . ASN A 1 419 ? 23.871  -6.492  -21.312 1.00 20.23 ? 419  ASN A CG  1 
ATOM   1919 O  OD1 . ASN A 1 419 ? 24.318  -6.490  -20.154 1.00 18.90 ? 419  ASN A OD1 1 
ATOM   1920 N  ND2 . ASN A 1 419 ? 22.679  -6.995  -21.615 1.00 19.85 ? 419  ASN A ND2 1 
ATOM   1921 N  N   . ILE A 1 420 ? 26.831  -7.801  -21.257 1.00 19.77 ? 420  ILE A N   1 
ATOM   1922 C  CA  . ILE A 1 420 ? 27.440  -9.119  -21.251 1.00 20.58 ? 420  ILE A CA  1 
ATOM   1923 C  C   . ILE A 1 420 ? 26.382  -10.091 -20.742 1.00 19.90 ? 420  ILE A C   1 
ATOM   1924 O  O   . ILE A 1 420 ? 25.767  -9.851  -19.700 1.00 20.32 ? 420  ILE A O   1 
ATOM   1925 C  CB  . ILE A 1 420 ? 28.716  -9.200  -20.384 1.00 21.74 ? 420  ILE A CB  1 
ATOM   1926 C  CG1 . ILE A 1 420 ? 29.136  -10.664 -20.253 1.00 23.21 ? 420  ILE A CG1 1 
ATOM   1927 C  CG2 . ILE A 1 420 ? 28.510  -8.564  -19.012 1.00 21.66 ? 420  ILE A CG2 1 
ATOM   1928 C  CD1 . ILE A 1 420 ? 30.410  -10.873 -19.487 1.00 25.08 ? 420  ILE A CD1 1 
ATOM   1929 N  N   . ALA A 1 421 ? 26.157  -11.168 -21.480 1.00 18.94 ? 421  ALA A N   1 
ATOM   1930 C  CA  . ALA A 1 421 ? 25.066  -12.085 -21.150 1.00 19.67 ? 421  ALA A CA  1 
ATOM   1931 C  C   . ALA A 1 421 ? 25.432  -13.495 -21.580 1.00 19.30 ? 421  ALA A C   1 
ATOM   1932 O  O   . ALA A 1 421 ? 25.843  -13.718 -22.718 1.00 18.46 ? 421  ALA A O   1 
ATOM   1933 C  CB  . ALA A 1 421 ? 23.771  -11.648 -21.794 1.00 18.96 ? 421  ALA A CB  1 
ATOM   1934 N  N   . MET A 1 422 ? 25.297  -14.422 -20.632 1.00 18.66 ? 422  MET A N   1 
ATOM   1935 C  CA  . MET A 1 422 ? 25.526  -15.832 -20.873 1.00 18.66 ? 422  MET A CA  1 
ATOM   1936 C  C   . MET A 1 422 ? 24.825  -16.545 -19.750 1.00 17.84 ? 422  MET A C   1 
ATOM   1937 O  O   . MET A 1 422 ? 25.434  -16.965 -18.767 1.00 17.68 ? 422  MET A O   1 
ATOM   1938 C  CB  . MET A 1 422 ? 27.021  -16.134 -20.903 1.00 19.31 ? 422  MET A CB  1 
ATOM   1939 C  CG  . MET A 1 422 ? 27.399  -17.602 -21.061 1.00 19.39 ? 422  MET A CG  1 
ATOM   1940 S  SD  . MET A 1 422 ? 26.661  -18.416 -22.489 1.00 19.17 ? 422  MET A SD  1 
ATOM   1941 C  CE  . MET A 1 422 ? 27.113  -17.307 -23.831 1.00 19.84 ? 422  MET A CE  1 
ATOM   1942 N  N   . ARG A 1 423 ? 23.511  -16.656 -19.885 1.00 18.05 ? 423  ARG A N   1 
ATOM   1943 C  CA  . ARG A 1 423 ? 22.681  -16.982 -18.735 1.00 17.19 ? 423  ARG A CA  1 
ATOM   1944 C  C   . ARG A 1 423 ? 21.312  -17.514 -19.123 1.00 17.60 ? 423  ARG A C   1 
ATOM   1945 O  O   . ARG A 1 423 ? 21.012  -17.710 -20.312 1.00 17.31 ? 423  ARG A O   1 
ATOM   1946 C  CB  . ARG A 1 423 ? 22.541  -15.733 -17.853 1.00 16.97 ? 423  ARG A CB  1 
ATOM   1947 C  CG  . ARG A 1 423 ? 21.900  -14.506 -18.501 1.00 16.83 ? 423  ARG A CG  1 
ATOM   1948 C  CD  . ARG A 1 423 ? 21.623  -13.489 -17.403 1.00 16.64 ? 423  ARG A CD  1 
ATOM   1949 N  NE  . ARG A 1 423 ? 20.927  -12.272 -17.799 1.00 16.51 ? 423  ARG A NE  1 
ATOM   1950 C  CZ  . ARG A 1 423 ? 21.516  -11.130 -18.176 1.00 17.37 ? 423  ARG A CZ  1 
ATOM   1951 N  NH1 . ARG A 1 423 ? 22.836  -11.029 -18.273 1.00 17.45 ? 423  ARG A NH1 1 
ATOM   1952 N  NH2 . ARG A 1 423 ? 20.771  -10.067 -18.461 1.00 17.55 ? 423  ARG A NH2 1 
ATOM   1953 N  N   . ASP A 1 424 ? 20.500  -17.758 -18.096 1.00 17.44 ? 424  ASP A N   1 
ATOM   1954 C  CA  . ASP A 1 424 ? 19.077  -18.051 -18.229 1.00 17.65 ? 424  ASP A CA  1 
ATOM   1955 C  C   . ASP A 1 424 ? 18.866  -19.275 -19.121 1.00 18.21 ? 424  ASP A C   1 
ATOM   1956 O  O   . ASP A 1 424 ? 18.063  -19.255 -20.040 1.00 17.99 ? 424  ASP A O   1 
ATOM   1957 C  CB  . ASP A 1 424 ? 18.301  -16.840 -18.781 1.00 17.67 ? 424  ASP A CB  1 
ATOM   1958 C  CG  . ASP A 1 424 ? 18.285  -15.647 -17.831 1.00 18.07 ? 424  ASP A CG  1 
ATOM   1959 O  OD1 . ASP A 1 424 ? 19.049  -15.627 -16.828 1.00 17.27 ? 424  ASP A OD1 1 
ATOM   1960 O  OD2 . ASP A 1 424 ? 17.487  -14.712 -18.107 1.00 17.81 ? 424  ASP A OD2 1 
ATOM   1961 N  N   . ALA A 1 425 ? 19.595  -20.347 -18.841 1.00 18.54 ? 425  ALA A N   1 
ATOM   1962 C  CA  . ALA A 1 425 ? 19.543  -21.527 -19.676 1.00 18.01 ? 425  ALA A CA  1 
ATOM   1963 C  C   . ALA A 1 425 ? 18.273  -22.302 -19.378 1.00 18.34 ? 425  ALA A C   1 
ATOM   1964 O  O   . ALA A 1 425 ? 17.981  -22.620 -18.218 1.00 18.21 ? 425  ALA A O   1 
ATOM   1965 C  CB  . ALA A 1 425 ? 20.770  -22.398 -19.444 1.00 18.64 ? 425  ALA A CB  1 
ATOM   1966 N  N   . HIS A 1 426 ? 17.524  -22.595 -20.439 1.00 18.22 ? 426  HIS A N   1 
ATOM   1967 C  CA  . HIS A 1 426 ? 16.298  -23.358 -20.361 1.00 18.28 ? 426  HIS A CA  1 
ATOM   1968 C  C   . HIS A 1 426 ? 16.469  -24.712 -21.029 1.00 18.07 ? 426  HIS A C   1 
ATOM   1969 O  O   . HIS A 1 426 ? 16.692  -24.792 -22.245 1.00 17.18 ? 426  HIS A O   1 
ATOM   1970 C  CB  . HIS A 1 426 ? 15.153  -22.621 -21.042 1.00 18.69 ? 426  HIS A CB  1 
ATOM   1971 C  CG  . HIS A 1 426 ? 13.853  -23.350 -20.941 1.00 18.59 ? 426  HIS A CG  1 
ATOM   1972 N  ND1 . HIS A 1 426 ? 13.014  -23.216 -19.861 1.00 18.16 ? 426  HIS A ND1 1 
ATOM   1973 C  CD2 . HIS A 1 426 ? 13.279  -24.268 -21.754 1.00 18.60 ? 426  HIS A CD2 1 
ATOM   1974 C  CE1 . HIS A 1 426 ? 11.963  -23.997 -20.024 1.00 18.58 ? 426  HIS A CE1 1 
ATOM   1975 N  NE2 . HIS A 1 426 ? 12.100  -24.648 -21.165 1.00 18.65 ? 426  HIS A NE2 1 
ATOM   1976 N  N   . VAL A 1 427 ? 16.346  -25.775 -20.240 1.00 17.74 ? 427  VAL A N   1 
ATOM   1977 C  CA  . VAL A 1 427 ? 16.540  -27.126 -20.773 1.00 18.13 ? 427  VAL A CA  1 
ATOM   1978 C  C   . VAL A 1 427 ? 15.223  -27.694 -21.299 1.00 18.83 ? 427  VAL A C   1 
ATOM   1979 O  O   . VAL A 1 427 ? 14.166  -27.546 -20.681 1.00 16.96 ? 427  VAL A O   1 
ATOM   1980 C  CB  . VAL A 1 427 ? 17.139  -28.107 -19.740 1.00 18.34 ? 427  VAL A CB  1 
ATOM   1981 C  CG1 . VAL A 1 427 ? 16.200  -28.337 -18.563 1.00 18.30 ? 427  VAL A CG1 1 
ATOM   1982 C  CG2 . VAL A 1 427 ? 17.483  -29.423 -20.408 1.00 18.35 ? 427  VAL A CG2 1 
ATOM   1983 N  N   . ILE A 1 428 ? 15.307  -28.340 -22.453 1.00 19.16 ? 428  ILE A N   1 
ATOM   1984 C  CA  . ILE A 1 428 ? 14.154  -28.969 -23.057 1.00 20.75 ? 428  ILE A CA  1 
ATOM   1985 C  C   . ILE A 1 428 ? 14.635  -30.140 -23.897 1.00 21.43 ? 428  ILE A C   1 
ATOM   1986 O  O   . ILE A 1 428 ? 15.675  -30.053 -24.562 1.00 21.25 ? 428  ILE A O   1 
ATOM   1987 C  CB  . ILE A 1 428 ? 13.325  -27.975 -23.911 1.00 21.25 ? 428  ILE A CB  1 
ATOM   1988 C  CG1 . ILE A 1 428 ? 12.151  -28.695 -24.594 1.00 22.44 ? 428  ILE A CG1 1 
ATOM   1989 C  CG2 . ILE A 1 428 ? 14.191  -27.245 -24.935 1.00 20.51 ? 428  ILE A CG2 1 
ATOM   1990 C  CD1 . ILE A 1 428 ? 11.098  -27.757 -25.153 1.00 22.60 ? 428  ILE A CD1 1 
ATOM   1991 N  N   . GLU A 1 429 ? 13.874  -31.231 -23.857 1.00 22.77 ? 429  GLU A N   1 
ATOM   1992 C  CA  . GLU A 1 429 ? 14.170  -32.412 -24.655 1.00 24.47 ? 429  GLU A CA  1 
ATOM   1993 C  C   . GLU A 1 429 ? 13.034  -32.623 -25.634 1.00 24.99 ? 429  GLU A C   1 
ATOM   1994 O  O   . GLU A 1 429 ? 11.868  -32.492 -25.267 1.00 23.71 ? 429  GLU A O   1 
ATOM   1995 C  CB  . GLU A 1 429 ? 14.340  -33.632 -23.744 1.00 26.35 ? 429  GLU A CB  1 
ATOM   1996 C  CG  . GLU A 1 429 ? 14.767  -34.912 -24.456 1.00 28.15 ? 429  GLU A CG  1 
ATOM   1997 C  CD  . GLU A 1 429 ? 14.986  -36.076 -23.493 1.00 30.16 ? 429  GLU A CD  1 
ATOM   1998 O  OE1 . GLU A 1 429 ? 15.832  -35.969 -22.574 1.00 32.92 ? 429  GLU A OE1 1 
ATOM   1999 O  OE2 . GLU A 1 429 ? 14.314  -37.100 -23.666 1.00 30.98 ? 429  GLU A OE2 1 
ATOM   2000 N  N   . ASP A 1 430 ? 13.372  -32.948 -26.877 1.00 27.11 ? 430  ASP A N   1 
ATOM   2001 C  CA  . ASP A 1 430 ? 12.362  -33.236 -27.892 1.00 28.44 ? 430  ASP A CA  1 
ATOM   2002 C  C   . ASP A 1 430 ? 12.128  -34.743 -28.034 1.00 30.23 ? 430  ASP A C   1 
ATOM   2003 O  O   . ASP A 1 430 ? 12.703  -35.550 -27.292 1.00 28.57 ? 430  ASP A O   1 
ATOM   2004 C  CB  . ASP A 1 430 ? 12.758  -32.599 -29.236 1.00 30.20 ? 430  ASP A CB  1 
ATOM   2005 C  CG  . ASP A 1 430 ? 13.992  -33.237 -29.873 1.00 30.87 ? 430  ASP A CG  1 
ATOM   2006 O  OD1 . ASP A 1 430 ? 14.420  -34.361 -29.493 1.00 30.15 ? 430  ASP A OD1 1 
ATOM   2007 O  OD2 . ASP A 1 430 ? 14.520  -32.601 -30.801 1.00 33.35 ? 430  ASP A OD2 1 
ATOM   2008 N  N   . ASP A 1 431 ? 11.313  -35.114 -29.016 1.00 31.83 ? 431  ASP A N   1 
ATOM   2009 C  CA  . ASP A 1 431 ? 10.853  -36.496 -29.189 1.00 33.23 ? 431  ASP A CA  1 
ATOM   2010 C  C   . ASP A 1 431 ? 11.885  -37.405 -29.836 1.00 30.73 ? 431  ASP A C   1 
ATOM   2011 O  O   . ASP A 1 431 ? 11.671  -38.610 -29.950 1.00 27.96 ? 431  ASP A O   1 
ATOM   2012 C  CB  . ASP A 1 431 ? 9.569   -36.513 -30.015 1.00 35.42 ? 431  ASP A CB  1 
ATOM   2013 C  CG  . ASP A 1 431 ? 8.416   -35.871 -29.281 1.00 39.11 ? 431  ASP A CG  1 
ATOM   2014 O  OD1 . ASP A 1 431 ? 8.187   -36.256 -28.112 1.00 39.03 ? 431  ASP A OD1 1 
ATOM   2015 O  OD2 . ASP A 1 431 ? 7.752   -34.985 -29.865 1.00 42.48 ? 431  ASP A OD2 1 
ATOM   2016 N  N   . ASN A 1 432 ? 12.991  -36.819 -30.272 1.00 30.70 ? 432  ASN A N   1 
ATOM   2017 C  CA  . ASN A 1 432 ? 14.111  -37.582 -30.787 1.00 30.61 ? 432  ASN A CA  1 
ATOM   2018 C  C   . ASN A 1 432 ? 15.130  -37.911 -29.722 1.00 28.22 ? 432  ASN A C   1 
ATOM   2019 O  O   . ASN A 1 432 ? 16.203  -38.389 -30.048 1.00 29.16 ? 432  ASN A O   1 
ATOM   2020 C  CB  . ASN A 1 432 ? 14.768  -36.833 -31.946 1.00 32.04 ? 432  ASN A CB  1 
ATOM   2021 C  CG  . ASN A 1 432 ? 14.013  -37.020 -33.248 1.00 34.71 ? 432  ASN A CG  1 
ATOM   2022 O  OD1 . ASN A 1 432 ? 12.882  -37.484 -33.252 1.00 34.82 ? 432  ASN A OD1 1 
ATOM   2023 N  ND2 . ASN A 1 432 ? 14.643  -36.666 -34.362 1.00 38.65 ? 432  ASN A ND2 1 
ATOM   2024 N  N   . GLY A 1 433 ? 14.803  -37.652 -28.456 1.00 27.13 ? 433  GLY A N   1 
ATOM   2025 C  CA  . GLY A 1 433 ? 15.725  -37.906 -27.358 1.00 26.77 ? 433  GLY A CA  1 
ATOM   2026 C  C   . GLY A 1 433 ? 16.875  -36.914 -27.239 1.00 26.39 ? 433  GLY A C   1 
ATOM   2027 O  O   . GLY A 1 433 ? 17.782  -37.109 -26.436 1.00 25.05 ? 433  GLY A O   1 
ATOM   2028 N  N   . ASP A 1 434 ? 16.849  -35.847 -28.030 1.00 26.29 ? 434  ASP A N   1 
ATOM   2029 C  CA  . ASP A 1 434 ? 17.867  -34.802 -27.937 1.00 26.60 ? 434  ASP A CA  1 
ATOM   2030 C  C   . ASP A 1 434 ? 17.493  -33.750 -26.890 1.00 25.28 ? 434  ASP A C   1 
ATOM   2031 O  O   . ASP A 1 434 ? 16.448  -33.116 -26.983 1.00 24.35 ? 434  ASP A O   1 
ATOM   2032 C  CB  . ASP A 1 434 ? 17.998  -34.103 -29.282 1.00 27.59 ? 434  ASP A CB  1 
ATOM   2033 C  CG  . ASP A 1 434 ? 18.422  -35.046 -30.387 1.00 27.47 ? 434  ASP A CG  1 
ATOM   2034 O  OD1 . ASP A 1 434 ? 19.326  -35.888 -30.144 1.00 24.81 ? 434  ASP A OD1 1 
ATOM   2035 O  OD2 . ASP A 1 434 ? 17.857  -34.903 -31.494 1.00 26.66 ? 434  ASP A OD2 1 
ATOM   2036 N  N   . ARG A 1 435 ? 18.372  -33.556 -25.918 1.00 25.19 ? 435  ARG A N   1 
ATOM   2037 C  CA  . ARG A 1 435 ? 18.232  -32.503 -24.930 1.00 24.31 ? 435  ARG A CA  1 
ATOM   2038 C  C   . ARG A 1 435 ? 18.989  -31.239 -25.345 1.00 21.49 ? 435  ARG A C   1 
ATOM   2039 O  O   . ARG A 1 435 ? 20.142  -31.336 -25.717 1.00 20.30 ? 435  ARG A O   1 
ATOM   2040 C  CB  . ARG A 1 435 ? 18.786  -33.003 -23.618 1.00 24.67 ? 435  ARG A CB  1 
ATOM   2041 C  CG  . ARG A 1 435 ? 18.453  -32.100 -22.464 1.00 25.84 ? 435  ARG A CG  1 
ATOM   2042 C  CD  . ARG A 1 435 ? 18.840  -32.763 -21.168 1.00 26.27 ? 435  ARG A CD  1 
ATOM   2043 N  NE  . ARG A 1 435 ? 17.920  -33.847 -20.888 1.00 26.35 ? 435  ARG A NE  1 
ATOM   2044 C  CZ  . ARG A 1 435 ? 17.724  -34.368 -19.687 1.00 26.64 ? 435  ARG A CZ  1 
ATOM   2045 N  NH1 . ARG A 1 435 ? 18.416  -33.939 -18.631 1.00 28.22 ? 435  ARG A NH1 1 
ATOM   2046 N  NH2 . ARG A 1 435 ? 16.837  -35.335 -19.549 1.00 26.93 ? 435  ARG A NH2 1 
ATOM   2047 N  N   . TYR A 1 436 ? 18.339  -30.071 -25.237 1.00 19.90 ? 436  TYR A N   1 
ATOM   2048 C  CA  . TYR A 1 436 ? 18.906  -28.781 -25.646 1.00 18.97 ? 436  TYR A CA  1 
ATOM   2049 C  C   . TYR A 1 436 ? 18.883  -27.740 -24.538 1.00 18.17 ? 436  TYR A C   1 
ATOM   2050 O  O   . TYR A 1 436 ? 18.056  -27.821 -23.643 1.00 18.80 ? 436  TYR A O   1 
ATOM   2051 C  CB  . TYR A 1 436 ? 18.101  -28.190 -26.800 1.00 19.94 ? 436  TYR A CB  1 
ATOM   2052 C  CG  . TYR A 1 436 ? 18.118  -28.984 -28.082 1.00 20.42 ? 436  TYR A CG  1 
ATOM   2053 C  CD1 . TYR A 1 436 ? 17.267  -30.076 -28.257 1.00 20.72 ? 436  TYR A CD1 1 
ATOM   2054 C  CD2 . TYR A 1 436 ? 18.960  -28.632 -29.124 1.00 20.21 ? 436  TYR A CD2 1 
ATOM   2055 C  CE1 . TYR A 1 436 ? 17.277  -30.796 -29.432 1.00 22.21 ? 436  TYR A CE1 1 
ATOM   2056 C  CE2 . TYR A 1 436 ? 18.970  -29.338 -30.306 1.00 20.59 ? 436  TYR A CE2 1 
ATOM   2057 C  CZ  . TYR A 1 436 ? 18.129  -30.410 -30.456 1.00 22.24 ? 436  TYR A CZ  1 
ATOM   2058 O  OH  . TYR A 1 436 ? 18.143  -31.105 -31.624 1.00 23.56 ? 436  TYR A OH  1 
ATOM   2059 N  N   . LEU A 1 437 ? 19.778  -26.750 -24.601 1.00 16.66 ? 437  LEU A N   1 
ATOM   2060 C  CA  . LEU A 1 437 ? 19.618  -25.533 -23.798 1.00 16.35 ? 437  LEU A CA  1 
ATOM   2061 C  C   . LEU A 1 437 ? 19.307  -24.365 -24.695 1.00 15.96 ? 437  LEU A C   1 
ATOM   2062 O  O   . LEU A 1 437 ? 19.958  -24.168 -25.716 1.00 14.48 ? 437  LEU A O   1 
ATOM   2063 C  CB  . LEU A 1 437 ? 20.864  -25.191 -22.978 1.00 16.39 ? 437  LEU A CB  1 
ATOM   2064 C  CG  . LEU A 1 437 ? 21.339  -26.258 -21.988 1.00 15.84 ? 437  LEU A CG  1 
ATOM   2065 C  CD1 . LEU A 1 437 ? 22.604  -25.784 -21.282 1.00 15.67 ? 437  LEU A CD1 1 
ATOM   2066 C  CD2 . LEU A 1 437 ? 20.235  -26.560 -21.002 1.00 15.59 ? 437  LEU A CD2 1 
ATOM   2067 N  N   . VAL A 1 438 ? 18.289  -23.611 -24.299 1.00 16.30 ? 438  VAL A N   1 
ATOM   2068 C  CA  . VAL A 1 438 ? 17.924  -22.370 -24.943 1.00 16.50 ? 438  VAL A CA  1 
ATOM   2069 C  C   . VAL A 1 438 ? 18.292  -21.312 -23.898 1.00 16.43 ? 438  VAL A C   1 
ATOM   2070 O  O   . VAL A 1 438 ? 17.889  -21.413 -22.745 1.00 16.59 ? 438  VAL A O   1 
ATOM   2071 C  CB  . VAL A 1 438 ? 16.437  -22.394 -25.350 1.00 16.54 ? 438  VAL A CB  1 
ATOM   2072 C  CG1 . VAL A 1 438 ? 15.981  -21.067 -25.924 1.00 17.19 ? 438  VAL A CG1 1 
ATOM   2073 C  CG2 . VAL A 1 438 ? 16.210  -23.487 -26.382 1.00 16.89 ? 438  VAL A CG2 1 
ATOM   2074 N  N   . PHE A 1 439 ? 19.120  -20.347 -24.281 1.00 16.04 ? 439  PHE A N   1 
ATOM   2075 C  CA  . PHE A 1 439 ? 19.764  -19.456 -23.326 1.00 15.53 ? 439  PHE A CA  1 
ATOM   2076 C  C   . PHE A 1 439 ? 19.895  -18.042 -23.851 1.00 15.45 ? 439  PHE A C   1 
ATOM   2077 O  O   . PHE A 1 439 ? 19.760  -17.797 -25.048 1.00 14.72 ? 439  PHE A O   1 
ATOM   2078 C  CB  . PHE A 1 439 ? 21.160  -19.976 -22.952 1.00 16.05 ? 439  PHE A CB  1 
ATOM   2079 C  CG  . PHE A 1 439 ? 22.081  -20.162 -24.123 1.00 15.55 ? 439  PHE A CG  1 
ATOM   2080 C  CD1 . PHE A 1 439 ? 22.032  -21.328 -24.887 1.00 15.91 ? 439  PHE A CD1 1 
ATOM   2081 C  CD2 . PHE A 1 439 ? 23.024  -19.189 -24.442 1.00 15.57 ? 439  PHE A CD2 1 
ATOM   2082 C  CE1 . PHE A 1 439 ? 22.897  -21.502 -25.962 1.00 15.77 ? 439  PHE A CE1 1 
ATOM   2083 C  CE2 . PHE A 1 439 ? 23.881  -19.355 -25.507 1.00 15.09 ? 439  PHE A CE2 1 
ATOM   2084 C  CZ  . PHE A 1 439 ? 23.826  -20.514 -26.268 1.00 15.33 ? 439  PHE A CZ  1 
ATOM   2085 N  N   . GLU A 1 440 ? 20.133  -17.124 -22.919 1.00 15.39 ? 440  GLU A N   1 
ATOM   2086 C  CA  . GLU A 1 440 ? 20.377  -15.719 -23.223 1.00 15.37 ? 440  GLU A CA  1 
ATOM   2087 C  C   . GLU A 1 440 ? 21.870  -15.464 -23.471 1.00 14.87 ? 440  GLU A C   1 
ATOM   2088 O  O   . GLU A 1 440 ? 22.709  -15.839 -22.661 1.00 14.89 ? 440  GLU A O   1 
ATOM   2089 C  CB  . GLU A 1 440 ? 19.903  -14.810 -22.090 1.00 15.84 ? 440  GLU A CB  1 
ATOM   2090 C  CG  . GLU A 1 440 ? 20.318  -13.370 -22.333 1.00 16.02 ? 440  GLU A CG  1 
ATOM   2091 C  CD  . GLU A 1 440 ? 19.882  -12.403 -21.274 1.00 16.77 ? 440  GLU A CD  1 
ATOM   2092 O  OE1 . GLU A 1 440 ? 19.302  -12.834 -20.249 1.00 16.41 ? 440  GLU A OE1 1 
ATOM   2093 O  OE2 . GLU A 1 440 ? 20.138  -11.188 -21.497 1.00 17.27 ? 440  GLU A OE2 1 
ATOM   2094 N  N   . ALA A 1 441 ? 22.177  -14.796 -24.582 1.00 14.48 ? 441  ALA A N   1 
ATOM   2095 C  CA  . ALA A 1 441 ? 23.551  -14.480 -24.962 1.00 14.38 ? 441  ALA A CA  1 
ATOM   2096 C  C   . ALA A 1 441 ? 23.592  -13.253 -25.875 1.00 14.37 ? 441  ALA A C   1 
ATOM   2097 O  O   . ALA A 1 441 ? 22.578  -12.601 -26.081 1.00 13.96 ? 441  ALA A O   1 
ATOM   2098 C  CB  . ALA A 1 441 ? 24.189  -15.682 -25.646 1.00 14.56 ? 441  ALA A CB  1 
ATOM   2099 N  N   . SER A 1 442 ? 24.776  -12.926 -26.392 1.00 15.02 ? 442  SER A N   1 
ATOM   2100 C  CA  . SER A 1 442 ? 24.914  -11.975 -27.489 1.00 15.12 ? 442  SER A CA  1 
ATOM   2101 C  C   . SER A 1 442 ? 25.501  -12.710 -28.675 1.00 15.00 ? 442  SER A C   1 
ATOM   2102 O  O   . SER A 1 442 ? 26.168  -13.718 -28.495 1.00 14.08 ? 442  SER A O   1 
ATOM   2103 C  CB  . SER A 1 442 ? 25.828  -10.842 -27.076 1.00 15.85 ? 442  SER A CB  1 
ATOM   2104 O  OG  . SER A 1 442 ? 25.383  -10.279 -25.855 1.00 16.61 ? 442  SER A OG  1 
ATOM   2105 N  N   . THR A 1 443 ? 25.247  -12.234 -29.894 1.00 15.57 ? 443  THR A N   1 
ATOM   2106 C  CA  . THR A 1 443 ? 25.894  -12.848 -31.067 1.00 15.45 ? 443  THR A CA  1 
ATOM   2107 C  C   . THR A 1 443 ? 27.436  -12.723 -30.987 1.00 16.06 ? 443  THR A C   1 
ATOM   2108 O  O   . THR A 1 443 ? 27.989  -11.797 -30.370 1.00 15.40 ? 443  THR A O   1 
ATOM   2109 C  CB  . THR A 1 443 ? 25.467  -12.222 -32.417 1.00 15.16 ? 443  THR A CB  1 
ATOM   2110 O  OG1 . THR A 1 443 ? 25.944  -10.865 -32.485 1.00 15.71 ? 443  THR A OG1 1 
ATOM   2111 C  CG2 . THR A 1 443 ? 23.979  -12.266 -32.617 1.00 14.67 ? 443  THR A CG2 1 
ATOM   2112 N  N   . GLY A 1 444 ? 28.110  -13.680 -31.609 1.00 16.36 ? 444  GLY A N   1 
ATOM   2113 C  CA  . GLY A 1 444 ? 29.533  -13.587 -31.850 1.00 17.35 ? 444  GLY A CA  1 
ATOM   2114 C  C   . GLY A 1 444 ? 29.843  -13.117 -33.268 1.00 17.62 ? 444  GLY A C   1 
ATOM   2115 O  O   . GLY A 1 444 ? 29.019  -12.463 -33.945 1.00 16.92 ? 444  GLY A O   1 
ATOM   2116 N  N   . LEU A 1 445 ? 31.025  -13.504 -33.735 1.00 17.81 ? 445  LEU A N   1 
ATOM   2117 C  CA  . LEU A 1 445 ? 31.554  -13.000 -34.983 1.00 17.99 ? 445  LEU A CA  1 
ATOM   2118 C  C   . LEU A 1 445 ? 30.789  -13.508 -36.209 1.00 17.92 ? 445  LEU A C   1 
ATOM   2119 O  O   . LEU A 1 445 ? 31.033  -13.039 -37.315 1.00 17.91 ? 445  LEU A O   1 
ATOM   2120 C  CB  . LEU A 1 445 ? 33.060  -13.303 -35.078 1.00 18.82 ? 445  LEU A CB  1 
ATOM   2121 C  CG  . LEU A 1 445 ? 33.878  -12.522 -34.054 1.00 19.05 ? 445  LEU A CG  1 
ATOM   2122 C  CD1 . LEU A 1 445 ? 35.290  -13.078 -33.948 1.00 19.52 ? 445  LEU A CD1 1 
ATOM   2123 C  CD2 . LEU A 1 445 ? 33.912  -11.045 -34.405 1.00 19.55 ? 445  LEU A CD2 1 
ATOM   2124 N  N   . GLU A 1 446 ? 29.840  -14.420 -36.008 1.00 17.47 ? 446  GLU A N   1 
ATOM   2125 C  CA  . GLU A 1 446 ? 28.918  -14.816 -37.074 1.00 17.81 ? 446  GLU A CA  1 
ATOM   2126 C  C   . GLU A 1 446 ? 28.100  -13.629 -37.585 1.00 17.98 ? 446  GLU A C   1 
ATOM   2127 O  O   . GLU A 1 446 ? 27.860  -13.485 -38.789 1.00 17.37 ? 446  GLU A O   1 
ATOM   2128 C  CB  . GLU A 1 446 ? 27.977  -15.936 -36.603 1.00 17.72 ? 446  GLU A CB  1 
ATOM   2129 C  CG  . GLU A 1 446 ? 27.061  -16.457 -37.705 1.00 17.80 ? 446  GLU A CG  1 
ATOM   2130 C  CD  . GLU A 1 446 ? 25.962  -17.380 -37.214 1.00 17.40 ? 446  GLU A CD  1 
ATOM   2131 O  OE1 . GLU A 1 446 ? 25.449  -17.210 -36.080 1.00 18.14 ? 446  GLU A OE1 1 
ATOM   2132 O  OE2 . GLU A 1 446 ? 25.567  -18.255 -38.000 1.00 16.94 ? 446  GLU A OE2 1 
ATOM   2133 N  N   . ASN A 1 447 ? 27.643  -12.793 -36.666 1.00 17.61 ? 447  ASN A N   1 
ATOM   2134 C  CA  . ASN A 1 447 ? 27.013  -11.543 -37.037 1.00 17.47 ? 447  ASN A CA  1 
ATOM   2135 C  C   . ASN A 1 447 ? 27.168  -10.588 -35.863 1.00 17.92 ? 447  ASN A C   1 
ATOM   2136 O  O   . ASN A 1 447 ? 26.242  -10.430 -35.033 1.00 17.58 ? 447  ASN A O   1 
ATOM   2137 C  CB  . ASN A 1 447 ? 25.539  -11.759 -37.367 1.00 17.86 ? 447  ASN A CB  1 
ATOM   2138 C  CG  . ASN A 1 447 ? 24.899  -10.522 -37.970 1.00 18.19 ? 447  ASN A CG  1 
ATOM   2139 O  OD1 . ASN A 1 447 ? 25.587  -9.699  -38.571 1.00 19.17 ? 447  ASN A OD1 1 
ATOM   2140 N  ND2 . ASN A 1 447 ? 23.592  -10.364 -37.783 1.00 17.65 ? 447  ASN A ND2 1 
ATOM   2141 N  N   . TYR A 1 448 ? 28.360  -10.001 -35.761 1.00 17.00 ? 448  TYR A N   1 
ATOM   2142 C  CA  . TYR A 1 448 ? 28.753  -9.313  -34.539 1.00 17.25 ? 448  TYR A CA  1 
ATOM   2143 C  C   . TYR A 1 448 ? 28.216  -7.889  -34.445 1.00 16.86 ? 448  TYR A C   1 
ATOM   2144 O  O   . TYR A 1 448 ? 27.920  -7.232  -35.443 1.00 16.94 ? 448  TYR A O   1 
ATOM   2145 C  CB  . TYR A 1 448 ? 30.280  -9.315  -34.394 1.00 17.42 ? 448  TYR A CB  1 
ATOM   2146 C  CG  . TYR A 1 448 ? 30.803  -9.179  -32.969 1.00 17.95 ? 448  TYR A CG  1 
ATOM   2147 C  CD1 . TYR A 1 448 ? 30.254  -9.924  -31.924 1.00 17.78 ? 448  TYR A CD1 1 
ATOM   2148 C  CD2 . TYR A 1 448 ? 31.870  -8.319  -32.674 1.00 17.41 ? 448  TYR A CD2 1 
ATOM   2149 C  CE1 . TYR A 1 448 ? 30.750  -9.826  -30.628 1.00 17.68 ? 448  TYR A CE1 1 
ATOM   2150 C  CE2 . TYR A 1 448 ? 32.371  -8.205  -31.382 1.00 17.14 ? 448  TYR A CE2 1 
ATOM   2151 C  CZ  . TYR A 1 448 ? 31.815  -8.954  -30.363 1.00 17.61 ? 448  TYR A CZ  1 
ATOM   2152 O  OH  . TYR A 1 448 ? 32.297  -8.842  -29.074 1.00 17.14 ? 448  TYR A OH  1 
ATOM   2153 N  N   . GLN A 1 449 ? 28.081  -7.420  -33.220 1.00 17.18 ? 449  GLN A N   1 
ATOM   2154 C  CA  . GLN A 1 449 ? 27.795  -6.021  -32.970 1.00 17.80 ? 449  GLN A CA  1 
ATOM   2155 C  C   . GLN A 1 449 ? 28.840  -5.122  -33.641 1.00 17.95 ? 449  GLN A C   1 
ATOM   2156 O  O   . GLN A 1 449 ? 29.977  -5.525  -33.836 1.00 18.41 ? 449  GLN A O   1 
ATOM   2157 C  CB  . GLN A 1 449 ? 27.825  -5.754  -31.475 1.00 17.86 ? 449  GLN A CB  1 
ATOM   2158 C  CG  . GLN A 1 449 ? 29.202  -5.950  -30.847 1.00 18.25 ? 449  GLN A CG  1 
ATOM   2159 C  CD  . GLN A 1 449 ? 29.153  -6.032  -29.341 1.00 18.37 ? 449  GLN A CD  1 
ATOM   2160 O  OE1 . GLN A 1 449 ? 28.107  -6.299  -28.765 1.00 18.07 ? 449  GLN A OE1 1 
ATOM   2161 N  NE2 . GLN A 1 449 ? 30.289  -5.803  -28.693 1.00 18.93 ? 449  GLN A NE2 1 
ATOM   2162 N  N   . GLY A 1 450 ? 28.440  -3.903  -33.971 1.00 18.27 ? 450  GLY A N   1 
ATOM   2163 C  CA  . GLY A 1 450 ? 29.372  -2.887  -34.451 1.00 18.85 ? 450  GLY A CA  1 
ATOM   2164 C  C   . GLY A 1 450 ? 28.617  -1.786  -35.178 1.00 19.22 ? 450  GLY A C   1 
ATOM   2165 O  O   . GLY A 1 450 ? 27.431  -1.952  -35.523 1.00 17.70 ? 450  GLY A O   1 
ATOM   2166 N  N   . GLU A 1 451 ? 29.301  -0.660  -35.397 1.00 19.54 ? 451  GLU A N   1 
ATOM   2167 C  CA  . GLU A 1 451 ? 28.727  0.482   -36.128 1.00 19.82 ? 451  GLU A CA  1 
ATOM   2168 C  C   . GLU A 1 451 ? 28.254  0.106   -37.527 1.00 18.25 ? 451  GLU A C   1 
ATOM   2169 O  O   . GLU A 1 451 ? 27.263  0.641   -38.034 1.00 17.36 ? 451  GLU A O   1 
ATOM   2170 C  CB  . GLU A 1 451 ? 29.747  1.631   -36.227 1.00 21.32 ? 451  GLU A CB  1 
ATOM   2171 C  CG  . GLU A 1 451 ? 29.110  2.905   -36.766 1.00 22.47 ? 451  GLU A CG  1 
ATOM   2172 C  CD  . GLU A 1 451 ? 30.045  4.089   -36.779 1.00 23.56 ? 451  GLU A CD  1 
ATOM   2173 O  OE1 . GLU A 1 451 ? 31.099  4.060   -36.135 1.00 24.48 ? 451  GLU A OE1 1 
ATOM   2174 O  OE2 . GLU A 1 451 ? 29.700  5.065   -37.447 1.00 27.88 ? 451  GLU A OE2 1 
ATOM   2175 N  N   . ASP A 1 452 ? 28.963  -0.829  -38.150 1.00 18.27 ? 452  ASP A N   1 
ATOM   2176 C  CA  . ASP A 1 452 ? 28.539  -1.393  -39.447 1.00 18.13 ? 452  ASP A CA  1 
ATOM   2177 C  C   . ASP A 1 452 ? 27.095  -1.862  -39.494 1.00 16.80 ? 452  ASP A C   1 
ATOM   2178 O  O   . ASP A 1 452 ? 26.484  -1.829  -40.554 1.00 16.09 ? 452  ASP A O   1 
ATOM   2179 C  CB  . ASP A 1 452 ? 29.447  -2.559  -39.850 1.00 18.14 ? 452  ASP A CB  1 
ATOM   2180 C  CG  . ASP A 1 452 ? 30.772  -2.091  -40.417 1.00 19.14 ? 452  ASP A CG  1 
ATOM   2181 O  OD1 . ASP A 1 452 ? 31.091  -0.893  -40.308 1.00 20.36 ? 452  ASP A OD1 1 
ATOM   2182 O  OD2 . ASP A 1 452 ? 31.519  -2.913  -40.968 1.00 19.45 ? 452  ASP A OD2 1 
ATOM   2183 N  N   . GLN A 1 453 ? 26.561  -2.326  -38.364 1.00 16.88 ? 453  GLN A N   1 
ATOM   2184 C  CA  . GLN A 1 453 ? 25.185  -2.858  -38.321 1.00 17.37 ? 453  GLN A CA  1 
ATOM   2185 C  C   . GLN A 1 453 ? 24.117  -1.794  -38.644 1.00 17.12 ? 453  GLN A C   1 
ATOM   2186 O  O   . GLN A 1 453 ? 23.062  -2.103  -39.181 1.00 16.49 ? 453  GLN A O   1 
ATOM   2187 C  CB  . GLN A 1 453 ? 24.905  -3.490  -36.957 1.00 17.96 ? 453  GLN A CB  1 
ATOM   2188 C  CG  . GLN A 1 453 ? 25.678  -4.775  -36.710 1.00 18.24 ? 453  GLN A CG  1 
ATOM   2189 C  CD  . GLN A 1 453 ? 25.137  -5.961  -37.509 1.00 19.09 ? 453  GLN A CD  1 
ATOM   2190 O  OE1 . GLN A 1 453 ? 24.189  -5.837  -38.280 1.00 18.16 ? 453  GLN A OE1 1 
ATOM   2191 N  NE2 . GLN A 1 453 ? 25.747  -7.130  -37.311 1.00 19.88 ? 453  GLN A NE2 1 
ATOM   2192 N  N   . ILE A 1 454 ? 24.424  -0.532  -38.352 1.00 17.63 ? 454  ILE A N   1 
ATOM   2193 C  CA  . ILE A 1 454 ? 23.557  0.584   -38.714 1.00 18.31 ? 454  ILE A CA  1 
ATOM   2194 C  C   . ILE A 1 454 ? 23.375  0.630   -40.232 1.00 19.50 ? 454  ILE A C   1 
ATOM   2195 O  O   . ILE A 1 454 ? 22.356  1.125   -40.725 1.00 20.36 ? 454  ILE A O   1 
ATOM   2196 C  CB  . ILE A 1 454 ? 24.138  1.922   -38.203 1.00 18.85 ? 454  ILE A CB  1 
ATOM   2197 C  CG1 . ILE A 1 454 ? 24.227  1.911   -36.665 1.00 18.73 ? 454  ILE A CG1 1 
ATOM   2198 C  CG2 . ILE A 1 454 ? 23.319  3.109   -38.716 1.00 18.70 ? 454  ILE A CG2 1 
ATOM   2199 C  CD1 . ILE A 1 454 ? 25.030  3.045   -36.069 1.00 18.49 ? 454  ILE A CD1 1 
ATOM   2200 N  N   . TYR A 1 455 ? 24.337  0.074   -40.973 1.00 20.24 ? 455  TYR A N   1 
ATOM   2201 C  CA  . TYR A 1 455 ? 24.271  0.064   -42.434 1.00 21.22 ? 455  TYR A CA  1 
ATOM   2202 C  C   . TYR A 1 455 ? 23.916  -1.301  -43.031 1.00 22.10 ? 455  TYR A C   1 
ATOM   2203 O  O   . TYR A 1 455 ? 24.299  -1.587  -44.172 1.00 22.95 ? 455  TYR A O   1 
ATOM   2204 C  CB  . TYR A 1 455 ? 25.606  0.569   -43.000 1.00 21.91 ? 455  TYR A CB  1 
ATOM   2205 C  CG  . TYR A 1 455 ? 25.986  1.916   -42.417 1.00 21.99 ? 455  TYR A CG  1 
ATOM   2206 C  CD1 . TYR A 1 455 ? 25.394  3.081   -42.890 1.00 22.12 ? 455  TYR A CD1 1 
ATOM   2207 C  CD2 . TYR A 1 455 ? 26.881  2.020   -41.361 1.00 21.48 ? 455  TYR A CD2 1 
ATOM   2208 C  CE1 . TYR A 1 455 ? 25.718  4.317   -42.354 1.00 22.75 ? 455  TYR A CE1 1 
ATOM   2209 C  CE2 . TYR A 1 455 ? 27.210  3.258   -40.820 1.00 22.05 ? 455  TYR A CE2 1 
ATOM   2210 C  CZ  . TYR A 1 455 ? 26.619  4.397   -41.317 1.00 22.37 ? 455  TYR A CZ  1 
ATOM   2211 O  OH  . TYR A 1 455 ? 26.913  5.632   -40.797 1.00 24.49 ? 455  TYR A OH  1 
ATOM   2212 N  N   . ASN A 1 456 ? 23.209  -2.146  -42.277 1.00 20.75 ? 456  ASN A N   1 
ATOM   2213 C  CA  . ASN A 1 456 ? 22.636  -3.371  -42.850 1.00 21.43 ? 456  ASN A CA  1 
ATOM   2214 C  C   . ASN A 1 456 ? 21.134  -3.265  -42.889 1.00 20.18 ? 456  ASN A C   1 
ATOM   2215 O  O   . ASN A 1 456 ? 20.482  -3.258  -41.854 1.00 17.46 ? 456  ASN A O   1 
ATOM   2216 C  CB  . ASN A 1 456 ? 23.053  -4.614  -42.078 1.00 22.37 ? 456  ASN A CB  1 
ATOM   2217 C  CG  . ASN A 1 456 ? 24.525  -4.894  -42.219 1.00 24.49 ? 456  ASN A CG  1 
ATOM   2218 O  OD1 . ASN A 1 456 ? 25.129  -4.586  -43.258 1.00 26.63 ? 456  ASN A OD1 1 
ATOM   2219 N  ND2 . ASN A 1 456 ? 25.119  -5.473  -41.186 1.00 23.72 ? 456  ASN A ND2 1 
ATOM   2220 N  N   . TRP A 1 457 ? 20.617  -3.185  -44.110 1.00 19.77 ? 457  TRP A N   1 
ATOM   2221 C  CA  . TRP A 1 457 ? 19.206  -2.929  -44.386 1.00 21.21 ? 457  TRP A CA  1 
ATOM   2222 C  C   . TRP A 1 457 ? 18.304  -3.972  -43.748 1.00 20.91 ? 457  TRP A C   1 
ATOM   2223 O  O   . TRP A 1 457 ? 17.182  -3.655  -43.343 1.00 20.46 ? 457  TRP A O   1 
ATOM   2224 C  CB  . TRP A 1 457 ? 19.025  -2.908  -45.908 1.00 21.73 ? 457  TRP A CB  1 
ATOM   2225 C  CG  . TRP A 1 457 ? 17.715  -2.469  -46.465 1.00 22.16 ? 457  TRP A CG  1 
ATOM   2226 C  CD1 . TRP A 1 457 ? 16.778  -3.267  -47.065 1.00 22.39 ? 457  TRP A CD1 1 
ATOM   2227 C  CD2 . TRP A 1 457 ? 17.235  -1.119  -46.600 1.00 22.29 ? 457  TRP A CD2 1 
ATOM   2228 N  NE1 . TRP A 1 457 ? 15.727  -2.501  -47.525 1.00 22.41 ? 457  TRP A NE1 1 
ATOM   2229 C  CE2 . TRP A 1 457 ? 15.985  -1.182  -47.257 1.00 22.35 ? 457  TRP A CE2 1 
ATOM   2230 C  CE3 . TRP A 1 457 ? 17.732  0.129   -46.220 1.00 22.88 ? 457  TRP A CE3 1 
ATOM   2231 C  CZ2 . TRP A 1 457 ? 15.220  -0.039  -47.531 1.00 22.31 ? 457  TRP A CZ2 1 
ATOM   2232 C  CZ3 . TRP A 1 457 ? 16.973  1.264   -46.492 1.00 22.83 ? 457  TRP A CZ3 1 
ATOM   2233 C  CH2 . TRP A 1 457 ? 15.725  1.166   -47.137 1.00 22.27 ? 457  TRP A CH2 1 
ATOM   2234 N  N   . LEU A 1 458 ? 18.808  -5.200  -43.650 1.00 21.70 ? 458  LEU A N   1 
ATOM   2235 C  CA  . LEU A 1 458 ? 18.104  -6.324  -43.022 1.00 23.12 ? 458  LEU A CA  1 
ATOM   2236 C  C   . LEU A 1 458 ? 17.684  -6.027  -41.579 1.00 20.68 ? 458  LEU A C   1 
ATOM   2237 O  O   . LEU A 1 458 ? 16.693  -6.554  -41.101 1.00 20.31 ? 458  LEU A O   1 
ATOM   2238 C  CB  . LEU A 1 458 ? 19.020  -7.557  -42.974 1.00 26.53 ? 458  LEU A CB  1 
ATOM   2239 C  CG  . LEU A 1 458 ? 18.424  -8.933  -43.280 1.00 30.27 ? 458  LEU A CG  1 
ATOM   2240 C  CD1 . LEU A 1 458 ? 19.421  -10.007 -42.853 1.00 31.50 ? 458  LEU A CD1 1 
ATOM   2241 C  CD2 . LEU A 1 458 ? 17.079  -9.189  -42.621 1.00 31.90 ? 458  LEU A CD2 1 
ATOM   2242 N  N   . ASN A 1 459 ? 18.459  -5.215  -40.871 1.00 18.68 ? 459  ASN A N   1 
ATOM   2243 C  CA  . ASN A 1 459 ? 18.162  -4.929  -39.466 1.00 18.17 ? 459  ASN A CA  1 
ATOM   2244 C  C   . ASN A 1 459 ? 16.938  -4.044  -39.261 1.00 17.32 ? 459  ASN A C   1 
ATOM   2245 O  O   . ASN A 1 459 ? 16.362  -4.026  -38.177 1.00 16.08 ? 459  ASN A O   1 
ATOM   2246 C  CB  . ASN A 1 459 ? 19.359  -4.286  -38.775 1.00 18.30 ? 459  ASN A CB  1 
ATOM   2247 C  CG  . ASN A 1 459 ? 20.568  -5.221  -38.691 1.00 18.40 ? 459  ASN A CG  1 
ATOM   2248 O  OD1 . ASN A 1 459 ? 20.441  -6.453  -38.742 1.00 17.75 ? 459  ASN A OD1 1 
ATOM   2249 N  ND2 . ASN A 1 459 ? 21.744  -4.630  -38.562 1.00 17.52 ? 459  ASN A ND2 1 
ATOM   2250 N  N   . TYR A 1 460 ? 16.558  -3.298  -40.292 1.00 17.96 ? 460  TYR A N   1 
ATOM   2251 C  CA  . TYR A 1 460 ? 15.524  -2.280  -40.155 1.00 17.70 ? 460  TYR A CA  1 
ATOM   2252 C  C   . TYR A 1 460 ? 14.128  -2.899  -40.241 1.00 17.70 ? 460  TYR A C   1 
ATOM   2253 O  O   . TYR A 1 460 ? 13.299  -2.710  -39.346 1.00 16.73 ? 460  TYR A O   1 
ATOM   2254 C  CB  . TYR A 1 460 ? 15.745  -1.162  -41.169 1.00 17.75 ? 460  TYR A CB  1 
ATOM   2255 C  CG  . TYR A 1 460 ? 16.943  -0.299  -40.840 1.00 18.09 ? 460  TYR A CG  1 
ATOM   2256 C  CD1 . TYR A 1 460 ? 18.245  -0.714  -41.150 1.00 18.61 ? 460  TYR A CD1 1 
ATOM   2257 C  CD2 . TYR A 1 460 ? 16.789  0.926   -40.204 1.00 17.59 ? 460  TYR A CD2 1 
ATOM   2258 C  CE1 . TYR A 1 460 ? 19.347  0.070   -40.833 1.00 17.59 ? 460  TYR A CE1 1 
ATOM   2259 C  CE2 . TYR A 1 460 ? 17.879  1.718   -39.897 1.00 17.39 ? 460  TYR A CE2 1 
ATOM   2260 C  CZ  . TYR A 1 460 ? 19.153  1.294   -40.208 1.00 17.83 ? 460  TYR A CZ  1 
ATOM   2261 O  OH  . TYR A 1 460 ? 20.240  2.096   -39.885 1.00 16.75 ? 460  TYR A OH  1 
ATOM   2262 N  N   . GLY A 1 461 ? 13.870  -3.639  -41.313 1.00 18.97 ? 461  GLY A N   1 
ATOM   2263 C  CA  . GLY A 1 461 ? 12.676  -4.481  -41.415 1.00 19.02 ? 461  GLY A CA  1 
ATOM   2264 C  C   . GLY A 1 461 ? 11.352  -3.776  -41.667 1.00 19.62 ? 461  GLY A C   1 
ATOM   2265 O  O   . GLY A 1 461 ? 10.301  -4.388  -41.509 1.00 19.61 ? 461  GLY A O   1 
ATOM   2266 N  N   . GLY A 1 462 ? 11.392  -2.494  -42.021 1.00 19.89 ? 462  GLY A N   1 
ATOM   2267 C  CA  . GLY A 1 462 ? 10.183  -1.743  -42.329 1.00 20.51 ? 462  GLY A CA  1 
ATOM   2268 C  C   . GLY A 1 462 ? 10.069  -1.519  -43.826 1.00 21.53 ? 462  GLY A C   1 
ATOM   2269 O  O   . GLY A 1 462 ? 10.816  -2.093  -44.610 1.00 22.21 ? 462  GLY A O   1 
ATOM   2270 N  N   . ASP A 1 463 ? 9.143   -0.668  -44.233 1.00 22.72 ? 463  ASP A N   1 
ATOM   2271 C  CA  . ASP A 1 463 ? 9.131   -0.207  -45.608 1.00 24.79 ? 463  ASP A CA  1 
ATOM   2272 C  C   . ASP A 1 463 ? 10.264  0.801   -45.828 1.00 24.64 ? 463  ASP A C   1 
ATOM   2273 O  O   . ASP A 1 463 ? 10.931  1.239   -44.884 1.00 23.95 ? 463  ASP A O   1 
ATOM   2274 C  CB  . ASP A 1 463 ? 7.750   0.345   -46.001 1.00 25.28 ? 463  ASP A CB  1 
ATOM   2275 C  CG  . ASP A 1 463 ? 7.400   1.641   -45.304 1.00 26.29 ? 463  ASP A CG  1 
ATOM   2276 O  OD1 . ASP A 1 463 ? 8.282   2.352   -44.788 1.00 27.31 ? 463  ASP A OD1 1 
ATOM   2277 O  OD2 . ASP A 1 463 ? 6.209   1.963   -45.288 1.00 29.79 ? 463  ASP A OD2 1 
ATOM   2278 N  N   . ASP A 1 464 ? 10.471  1.175   -47.082 1.00 25.09 ? 464  ASP A N   1 
ATOM   2279 C  CA  . ASP A 1 464 ? 11.589  2.037   -47.437 1.00 23.86 ? 464  ASP A CA  1 
ATOM   2280 C  C   . ASP A 1 464 ? 11.601  3.357   -46.696 1.00 22.29 ? 464  ASP A C   1 
ATOM   2281 O  O   . ASP A 1 464 ? 12.660  3.777   -46.232 1.00 20.52 ? 464  ASP A O   1 
ATOM   2282 C  CB  . ASP A 1 464 ? 11.609  2.283   -48.937 1.00 26.13 ? 464  ASP A CB  1 
ATOM   2283 C  CG  . ASP A 1 464 ? 11.809  1.002   -49.718 1.00 27.68 ? 464  ASP A CG  1 
ATOM   2284 O  OD1 . ASP A 1 464 ? 12.927  0.471   -49.709 1.00 30.38 ? 464  ASP A OD1 1 
ATOM   2285 O  OD2 . ASP A 1 464 ? 10.836  0.517   -50.315 1.00 30.22 ? 464  ASP A OD2 1 
ATOM   2286 N  N   . ALA A 1 465 ? 10.447  4.014   -46.585 1.00 21.01 ? 465  ALA A N   1 
ATOM   2287 C  CA  . ALA A 1 465 ? 10.388  5.283   -45.853 1.00 20.96 ? 465  ALA A CA  1 
ATOM   2288 C  C   . ALA A 1 465 ? 10.767  5.083   -44.379 1.00 20.37 ? 465  ALA A C   1 
ATOM   2289 O  O   . ALA A 1 465 ? 11.506  5.885   -43.803 1.00 19.71 ? 465  ALA A O   1 
ATOM   2290 C  CB  . ALA A 1 465 ? 9.007   5.914   -45.954 1.00 21.18 ? 465  ALA A CB  1 
ATOM   2291 N  N   . PHE A 1 466 ? 10.268  4.005   -43.778 1.00 19.57 ? 466  PHE A N   1 
ATOM   2292 C  CA  . PHE A 1 466 ? 10.564  3.727   -42.380 1.00 19.10 ? 466  PHE A CA  1 
ATOM   2293 C  C   . PHE A 1 466 ? 12.042  3.497   -42.191 1.00 18.93 ? 466  PHE A C   1 
ATOM   2294 O  O   . PHE A 1 466 ? 12.644  4.015   -41.247 1.00 18.92 ? 466  PHE A O   1 
ATOM   2295 C  CB  . PHE A 1 466 ? 9.815   2.496   -41.859 1.00 18.89 ? 466  PHE A CB  1 
ATOM   2296 C  CG  . PHE A 1 466 ? 10.176  2.145   -40.437 1.00 18.04 ? 466  PHE A CG  1 
ATOM   2297 C  CD1 . PHE A 1 466 ? 9.558   2.792   -39.372 1.00 18.09 ? 466  PHE A CD1 1 
ATOM   2298 C  CD2 . PHE A 1 466 ? 11.133  1.180   -40.165 1.00 17.74 ? 466  PHE A CD2 1 
ATOM   2299 C  CE1 . PHE A 1 466 ? 9.885   2.473   -38.061 1.00 17.49 ? 466  PHE A CE1 1 
ATOM   2300 C  CE2 . PHE A 1 466 ? 11.474  0.862   -38.854 1.00 17.74 ? 466  PHE A CE2 1 
ATOM   2301 C  CZ  . PHE A 1 466 ? 10.850  1.519   -37.803 1.00 17.03 ? 466  PHE A CZ  1 
ATOM   2302 N  N   . ASN A 1 467 ? 12.623  2.711   -43.085 1.00 18.57 ? 467  ASN A N   1 
ATOM   2303 C  CA  . ASN A 1 467 ? 14.012  2.351   -42.946 1.00 19.62 ? 467  ASN A CA  1 
ATOM   2304 C  C   . ASN A 1 467 ? 14.882  3.598   -43.071 1.00 19.49 ? 467  ASN A C   1 
ATOM   2305 O  O   . ASN A 1 467 ? 15.768  3.818   -42.257 1.00 19.48 ? 467  ASN A O   1 
ATOM   2306 C  CB  . ASN A 1 467 ? 14.416  1.292   -43.976 1.00 19.74 ? 467  ASN A CB  1 
ATOM   2307 C  CG  . ASN A 1 467 ? 13.731  -0.047  -43.759 1.00 20.08 ? 467  ASN A CG  1 
ATOM   2308 O  OD1 . ASN A 1 467 ? 12.981  -0.263  -42.786 1.00 19.34 ? 467  ASN A OD1 1 
ATOM   2309 N  ND2 . ASN A 1 467 ? 13.990  -0.965  -44.675 1.00 20.46 ? 467  ASN A ND2 1 
ATOM   2310 N  N   . ILE A 1 468 ? 14.604  4.436   -44.067 1.00 21.18 ? 468  ILE A N   1 
ATOM   2311 C  CA  . ILE A 1 468 ? 15.392  5.652   -44.265 1.00 22.15 ? 468  ILE A CA  1 
ATOM   2312 C  C   . ILE A 1 468 ? 15.236  6.598   -43.083 1.00 21.92 ? 468  ILE A C   1 
ATOM   2313 O  O   . ILE A 1 468 ? 16.227  7.056   -42.528 1.00 21.87 ? 468  ILE A O   1 
ATOM   2314 C  CB  . ILE A 1 468 ? 15.043  6.387   -45.574 1.00 23.39 ? 468  ILE A CB  1 
ATOM   2315 C  CG1 . ILE A 1 468 ? 15.417  5.513   -46.775 1.00 24.00 ? 468  ILE A CG1 1 
ATOM   2316 C  CG2 . ILE A 1 468 ? 15.796  7.724   -45.638 1.00 23.21 ? 468  ILE A CG2 1 
ATOM   2317 C  CD1 . ILE A 1 468 ? 14.990  6.073   -48.115 1.00 24.51 ? 468  ILE A CD1 1 
ATOM   2318 N  N   . LYS A 1 469 ? 13.998  6.884   -42.706 1.00 23.18 ? 469  LYS A N   1 
ATOM   2319 C  CA  . LYS A 1 469 ? 13.715  7.700   -41.508 1.00 25.01 ? 469  LYS A CA  1 
ATOM   2320 C  C   . LYS A 1 469 ? 14.479  7.165   -40.293 1.00 22.87 ? 469  LYS A C   1 
ATOM   2321 O  O   . LYS A 1 469 ? 15.086  7.914   -39.527 1.00 22.53 ? 469  LYS A O   1 
ATOM   2322 C  CB  . LYS A 1 469 ? 12.211  7.706   -41.211 1.00 28.49 ? 469  LYS A CB  1 
ATOM   2323 C  CG  . LYS A 1 469 ? 11.852  8.229   -39.821 1.00 32.91 ? 469  LYS A CG  1 
ATOM   2324 C  CD  . LYS A 1 469 ? 10.357  8.492   -39.660 1.00 35.99 ? 469  LYS A CD  1 
ATOM   2325 C  CE  . LYS A 1 469 ? 10.070  9.277   -38.381 1.00 38.98 ? 469  LYS A CE  1 
ATOM   2326 N  NZ  . LYS A 1 469 ? 10.364  10.736  -38.539 1.00 40.60 ? 469  LYS A NZ  1 
ATOM   2327 N  N   . SER A 1 470 ? 14.462  5.857   -40.133 1.00 20.64 ? 470  SER A N   1 
ATOM   2328 C  CA  . SER A 1 470 ? 15.127  5.240   -39.009 1.00 20.10 ? 470  SER A CA  1 
ATOM   2329 C  C   . SER A 1 470 ? 16.639  5.444   -39.073 1.00 19.52 ? 470  SER A C   1 
ATOM   2330 O  O   . SER A 1 470 ? 17.255  5.803   -38.061 1.00 18.05 ? 470  SER A O   1 
ATOM   2331 C  CB  . SER A 1 470 ? 14.754  3.749   -38.928 1.00 20.60 ? 470  SER A CB  1 
ATOM   2332 O  OG  . SER A 1 470 ? 13.353  3.600   -38.671 1.00 19.64 ? 470  SER A OG  1 
ATOM   2333 N  N   . LEU A 1 471 ? 17.238  5.251   -40.252 1.00 19.51 ? 471  LEU A N   1 
ATOM   2334 C  CA  . LEU A 1 471 ? 18.686  5.427   -40.388 1.00 20.39 ? 471  LEU A CA  1 
ATOM   2335 C  C   . LEU A 1 471 ? 19.131  6.834   -39.982 1.00 20.05 ? 471  LEU A C   1 
ATOM   2336 O  O   . LEU A 1 471 ? 20.105  7.006   -39.243 1.00 19.82 ? 471  LEU A O   1 
ATOM   2337 C  CB  . LEU A 1 471 ? 19.134  5.158   -41.823 1.00 21.39 ? 471  LEU A CB  1 
ATOM   2338 C  CG  . LEU A 1 471 ? 20.562  5.580   -42.184 1.00 22.05 ? 471  LEU A CG  1 
ATOM   2339 C  CD1 . LEU A 1 471 ? 21.591  4.712   -41.472 1.00 21.74 ? 471  LEU A CD1 1 
ATOM   2340 C  CD2 . LEU A 1 471 ? 20.752  5.510   -43.693 1.00 22.86 ? 471  LEU A CD2 1 
ATOM   2341 N  N   . PHE A 1 472 ? 18.421  7.841   -40.467 1.00 19.59 ? 472  PHE A N   1 
ATOM   2342 C  CA  . PHE A 1 472 ? 18.789  9.211   -40.160 1.00 20.11 ? 472  PHE A CA  1 
ATOM   2343 C  C   . PHE A 1 472 ? 18.601  9.493   -38.674 1.00 19.82 ? 472  PHE A C   1 
ATOM   2344 O  O   . PHE A 1 472 ? 19.394  10.215  -38.081 1.00 19.69 ? 472  PHE A O   1 
ATOM   2345 C  CB  . PHE A 1 472 ? 17.991  10.212  -40.996 1.00 20.71 ? 472  PHE A CB  1 
ATOM   2346 C  CG  . PHE A 1 472 ? 18.192  10.081  -42.485 1.00 21.32 ? 472  PHE A CG  1 
ATOM   2347 C  CD1 . PHE A 1 472 ? 19.309  9.445   -43.023 1.00 21.80 ? 472  PHE A CD1 1 
ATOM   2348 C  CD2 . PHE A 1 472 ? 17.235  10.610  -43.367 1.00 22.20 ? 472  PHE A CD2 1 
ATOM   2349 C  CE1 . PHE A 1 472 ? 19.467  9.330   -44.399 1.00 21.42 ? 472  PHE A CE1 1 
ATOM   2350 C  CE2 . PHE A 1 472 ? 17.397  10.499  -44.738 1.00 21.47 ? 472  PHE A CE2 1 
ATOM   2351 C  CZ  . PHE A 1 472 ? 18.516  9.858   -45.249 1.00 21.62 ? 472  PHE A CZ  1 
ATOM   2352 N  N   . ARG A 1 473 ? 17.582  8.896   -38.061 1.00 19.56 ? 473  ARG A N   1 
ATOM   2353 C  CA  . ARG A 1 473 ? 17.335  9.141   -36.645 1.00 20.38 ? 473  ARG A CA  1 
ATOM   2354 C  C   . ARG A 1 473 ? 18.480  8.604   -35.828 1.00 19.65 ? 473  ARG A C   1 
ATOM   2355 O  O   . ARG A 1 473 ? 19.007  9.297   -34.959 1.00 19.80 ? 473  ARG A O   1 
ATOM   2356 C  CB  . ARG A 1 473 ? 16.007  8.520   -36.179 1.00 20.21 ? 473  ARG A CB  1 
ATOM   2357 C  CG  . ARG A 1 473 ? 15.671  8.769   -34.711 1.00 20.02 ? 473  ARG A CG  1 
ATOM   2358 C  CD  . ARG A 1 473 ? 15.751  10.249  -34.323 1.00 21.19 ? 473  ARG A CD  1 
ATOM   2359 N  NE  . ARG A 1 473 ? 15.421  10.455  -32.911 1.00 21.40 ? 473  ARG A NE  1 
ATOM   2360 C  CZ  . ARG A 1 473 ? 16.023  11.315  -32.093 1.00 22.34 ? 473  ARG A CZ  1 
ATOM   2361 N  NH1 . ARG A 1 473 ? 17.033  12.077  -32.508 1.00 23.46 ? 473  ARG A NH1 1 
ATOM   2362 N  NH2 . ARG A 1 473 ? 15.626  11.404  -30.827 1.00 22.35 ? 473  ARG A NH2 1 
ATOM   2363 N  N   . ILE A 1 474 ? 18.872  7.368   -36.118 1.00 20.60 ? 474  ILE A N   1 
ATOM   2364 C  CA  . ILE A 1 474 ? 20.005  6.725   -35.423 1.00 20.97 ? 474  ILE A CA  1 
ATOM   2365 C  C   . ILE A 1 474 ? 21.297  7.591   -35.511 1.00 21.54 ? 474  ILE A C   1 
ATOM   2366 O  O   . ILE A 1 474 ? 21.952  7.854   -34.508 1.00 20.96 ? 474  ILE A O   1 
ATOM   2367 C  CB  . ILE A 1 474 ? 20.243  5.308   -35.977 1.00 20.76 ? 474  ILE A CB  1 
ATOM   2368 C  CG1 . ILE A 1 474 ? 19.084  4.379   -35.561 1.00 20.82 ? 474  ILE A CG1 1 
ATOM   2369 C  CG2 . ILE A 1 474 ? 21.573  4.738   -35.482 1.00 21.06 ? 474  ILE A CG2 1 
ATOM   2370 C  CD1 . ILE A 1 474 ? 18.960  3.108   -36.377 1.00 20.61 ? 474  ILE A CD1 1 
ATOM   2371 N  N   . LEU A 1 475 ? 21.627  8.056   -36.708 1.00 22.31 ? 475  LEU A N   1 
ATOM   2372 C  CA  . LEU A 1 475 ? 22.815  8.881   -36.908 1.00 23.90 ? 475  LEU A CA  1 
ATOM   2373 C  C   . LEU A 1 475 ? 22.690  10.311  -36.348 1.00 24.22 ? 475  LEU A C   1 
ATOM   2374 O  O   . LEU A 1 475 ? 23.698  10.987  -36.208 1.00 25.11 ? 475  LEU A O   1 
ATOM   2375 C  CB  . LEU A 1 475 ? 23.162  8.959   -38.399 1.00 25.23 ? 475  LEU A CB  1 
ATOM   2376 C  CG  . LEU A 1 475 ? 23.542  7.639   -39.094 1.00 25.96 ? 475  LEU A CG  1 
ATOM   2377 C  CD1 . LEU A 1 475 ? 23.868  7.911   -40.550 1.00 26.47 ? 475  LEU A CD1 1 
ATOM   2378 C  CD2 . LEU A 1 475 ? 24.720  6.944   -38.421 1.00 26.04 ? 475  LEU A CD2 1 
ATOM   2379 N  N   . SER A 1 476 ? 21.476  10.773  -36.046 1.00 23.89 ? 476  SER A N   1 
ATOM   2380 C  CA  . SER A 1 476 ? 21.264  12.131  -35.501 1.00 23.85 ? 476  SER A CA  1 
ATOM   2381 C  C   . SER A 1 476 ? 21.495  12.269  -33.992 1.00 23.45 ? 476  SER A C   1 
ATOM   2382 O  O   . SER A 1 476 ? 21.528  13.381  -33.485 1.00 22.49 ? 476  SER A O   1 
ATOM   2383 C  CB  . SER A 1 476 ? 19.842  12.602  -35.812 1.00 24.46 ? 476  SER A CB  1 
ATOM   2384 O  OG  . SER A 1 476 ? 18.889  11.883  -35.019 1.00 25.95 ? 476  SER A OG  1 
ATOM   2385 N  N   . ASN A 1 477 ? 21.646  11.155  -33.274 1.00 23.46 ? 477  ASN A N   1 
ATOM   2386 C  CA  . ASN A 1 477 ? 21.691  11.152  -31.803 1.00 23.22 ? 477  ASN A CA  1 
ATOM   2387 C  C   . ASN A 1 477 ? 22.781  10.176  -31.344 1.00 24.34 ? 477  ASN A C   1 
ATOM   2388 O  O   . ASN A 1 477 ? 22.732  8.990   -31.685 1.00 23.67 ? 477  ASN A O   1 
ATOM   2389 C  CB  . ASN A 1 477 ? 20.301  10.740  -31.270 1.00 22.95 ? 477  ASN A CB  1 
ATOM   2390 C  CG  . ASN A 1 477 ? 20.237  10.580  -29.739 1.00 23.18 ? 477  ASN A CG  1 
ATOM   2391 O  OD1 . ASN A 1 477 ? 20.833  9.687   -29.149 1.00 22.49 ? 477  ASN A OD1 1 
ATOM   2392 N  ND2 . ASN A 1 477 ? 19.433  11.417  -29.108 1.00 23.68 ? 477  ASN A ND2 1 
ATOM   2393 N  N   . ASP A 1 478 ? 23.754  10.678  -30.582 1.00 25.15 ? 478  ASP A N   1 
ATOM   2394 C  CA  . ASP A 1 478 ? 24.915  9.882   -30.157 1.00 26.40 ? 478  ASP A CA  1 
ATOM   2395 C  C   . ASP A 1 478 ? 24.540  8.654   -29.341 1.00 23.97 ? 478  ASP A C   1 
ATOM   2396 O  O   . ASP A 1 478 ? 25.234  7.624   -29.408 1.00 21.71 ? 478  ASP A O   1 
ATOM   2397 C  CB  . ASP A 1 478 ? 25.885  10.706  -29.302 1.00 29.84 ? 478  ASP A CB  1 
ATOM   2398 C  CG  . ASP A 1 478 ? 26.706  11.695  -30.106 1.00 33.62 ? 478  ASP A CG  1 
ATOM   2399 O  OD1 . ASP A 1 478 ? 26.874  11.509  -31.327 1.00 35.53 ? 478  ASP A OD1 1 
ATOM   2400 O  OD2 . ASP A 1 478 ? 27.203  12.671  -29.492 1.00 39.17 ? 478  ASP A OD2 1 
ATOM   2401 N  N   . ASP A 1 479 ? 23.491  8.777   -28.529 1.00 20.78 ? 479  ASP A N   1 
ATOM   2402 C  CA  . ASP A 1 479 ? 23.089  7.669   -27.669 1.00 19.94 ? 479  ASP A CA  1 
ATOM   2403 C  C   . ASP A 1 479 ? 22.399  6.579   -28.470 1.00 18.76 ? 479  ASP A C   1 
ATOM   2404 O  O   . ASP A 1 479 ? 22.618  5.403   -28.212 1.00 18.47 ? 479  ASP A O   1 
ATOM   2405 C  CB  . ASP A 1 479 ? 22.160  8.115   -26.542 1.00 20.02 ? 479  ASP A CB  1 
ATOM   2406 C  CG  . ASP A 1 479 ? 22.041  7.072   -25.467 1.00 19.79 ? 479  ASP A CG  1 
ATOM   2407 O  OD1 . ASP A 1 479 ? 23.037  6.864   -24.767 1.00 21.51 ? 479  ASP A OD1 1 
ATOM   2408 O  OD2 . ASP A 1 479 ? 20.974  6.438   -25.326 1.00 19.92 ? 479  ASP A OD2 1 
ATOM   2409 N  N   . ILE A 1 480 ? 21.565  6.961   -29.435 1.00 17.72 ? 480  ILE A N   1 
ATOM   2410 C  CA  . ILE A 1 480 ? 20.927  5.960   -30.300 1.00 18.11 ? 480  ILE A CA  1 
ATOM   2411 C  C   . ILE A 1 480 ? 21.984  5.267   -31.177 1.00 18.66 ? 480  ILE A C   1 
ATOM   2412 O  O   . ILE A 1 480 ? 21.994  4.036   -31.297 1.00 16.85 ? 480  ILE A O   1 
ATOM   2413 C  CB  . ILE A 1 480 ? 19.797  6.539   -31.158 1.00 17.23 ? 480  ILE A CB  1 
ATOM   2414 C  CG1 . ILE A 1 480 ? 18.690  7.086   -30.249 1.00 17.78 ? 480  ILE A CG1 1 
ATOM   2415 C  CG2 . ILE A 1 480 ? 19.243  5.448   -32.054 1.00 17.37 ? 480  ILE A CG2 1 
ATOM   2416 C  CD1 . ILE A 1 480 ? 17.547  7.782   -30.965 1.00 17.95 ? 480  ILE A CD1 1 
ATOM   2417 N  N   . LYS A 1 481 ? 22.855  6.072   -31.782 1.00 18.82 ? 481  LYS A N   1 
ATOM   2418 C  CA  . LYS A 1 481 ? 23.992  5.550   -32.550 1.00 20.96 ? 481  LYS A CA  1 
ATOM   2419 C  C   . LYS A 1 481 ? 24.858  4.585   -31.738 1.00 20.02 ? 481  LYS A C   1 
ATOM   2420 O  O   . LYS A 1 481 ? 25.212  3.502   -32.207 1.00 20.31 ? 481  LYS A O   1 
ATOM   2421 C  CB  . LYS A 1 481 ? 24.865  6.702   -33.062 1.00 22.36 ? 481  LYS A CB  1 
ATOM   2422 C  CG  . LYS A 1 481 ? 25.935  6.260   -34.041 1.00 24.41 ? 481  LYS A CG  1 
ATOM   2423 C  CD  . LYS A 1 481 ? 26.601  7.451   -34.714 1.00 26.00 ? 481  LYS A CD  1 
ATOM   2424 C  CE  . LYS A 1 481 ? 27.838  7.013   -35.474 1.00 27.65 ? 481  LYS A CE  1 
ATOM   2425 N  NZ  . LYS A 1 481 ? 28.602  8.192   -35.950 1.00 29.40 ? 481  LYS A NZ  1 
ATOM   2426 N  N   . SER A 1 482 ? 25.231  4.995   -30.533 1.00 19.72 ? 482  SER A N   1 
ATOM   2427 C  CA  . SER A 1 482 ? 25.982  4.126   -29.633 1.00 19.20 ? 482  SER A CA  1 
ATOM   2428 C  C   . SER A 1 482 ? 25.232  2.805   -29.300 1.00 18.50 ? 482  SER A C   1 
ATOM   2429 O  O   . SER A 1 482 ? 25.799  1.731   -29.407 1.00 18.35 ? 482  SER A O   1 
ATOM   2430 C  CB  . SER A 1 482 ? 26.327  4.879   -28.354 1.00 19.71 ? 482  SER A CB  1 
ATOM   2431 O  OG  . SER A 1 482 ? 26.893  4.005   -27.399 1.00 20.73 ? 482  SER A OG  1 
ATOM   2432 N  N   . ARG A 1 483 ? 23.970  2.886   -28.885 1.00 18.29 ? 483  ARG A N   1 
ATOM   2433 C  CA  . ARG A 1 483 ? 23.189  1.673   -28.585 1.00 17.77 ? 483  ARG A CA  1 
ATOM   2434 C  C   . ARG A 1 483 ? 23.110  0.761   -29.793 1.00 16.92 ? 483  ARG A C   1 
ATOM   2435 O  O   . ARG A 1 483 ? 23.314  -0.440  -29.668 1.00 16.15 ? 483  ARG A O   1 
ATOM   2436 C  CB  . ARG A 1 483 ? 21.785  2.006   -28.096 1.00 17.29 ? 483  ARG A CB  1 
ATOM   2437 C  CG  . ARG A 1 483 ? 21.764  2.543   -26.686 1.00 17.67 ? 483  ARG A CG  1 
ATOM   2438 C  CD  . ARG A 1 483 ? 20.460  3.253   -26.367 1.00 17.65 ? 483  ARG A CD  1 
ATOM   2439 N  NE  . ARG A 1 483 ? 20.431  3.748   -24.990 1.00 17.55 ? 483  ARG A NE  1 
ATOM   2440 C  CZ  . ARG A 1 483 ? 19.829  3.136   -23.967 1.00 18.92 ? 483  ARG A CZ  1 
ATOM   2441 N  NH1 . ARG A 1 483 ? 19.160  1.994   -24.128 1.00 19.90 ? 483  ARG A NH1 1 
ATOM   2442 N  NH2 . ARG A 1 483 ? 19.890  3.668   -22.755 1.00 18.79 ? 483  ARG A NH2 1 
ATOM   2443 N  N   . ALA A 1 484 ? 22.848  1.336   -30.962 1.00 16.44 ? 484  ALA A N   1 
ATOM   2444 C  CA  . ALA A 1 484 ? 22.797  0.557   -32.203 1.00 17.10 ? 484  ALA A CA  1 
ATOM   2445 C  C   . ALA A 1 484 ? 24.120  -0.155  -32.538 1.00 17.92 ? 484  ALA A C   1 
ATOM   2446 O  O   . ALA A 1 484 ? 24.126  -1.286  -33.078 1.00 17.34 ? 484  ALA A O   1 
ATOM   2447 C  CB  . ALA A 1 484 ? 22.396  1.449   -33.350 1.00 16.88 ? 484  ALA A CB  1 
ATOM   2448 N  N   . THR A 1 485 ? 25.215  0.549   -32.260 1.00 17.90 ? 485  THR A N   1 
ATOM   2449 C  CA  . THR A 1 485 ? 26.580  0.064   -32.439 1.00 18.49 ? 485  THR A CA  1 
ATOM   2450 C  C   . THR A 1 485 ? 26.889  -1.120  -31.530 1.00 17.63 ? 485  THR A C   1 
ATOM   2451 O  O   . THR A 1 485 ? 27.585  -2.034  -31.931 1.00 17.40 ? 485  THR A O   1 
ATOM   2452 C  CB  . THR A 1 485 ? 27.599  1.193   -32.149 1.00 18.62 ? 485  THR A CB  1 
ATOM   2453 O  OG1 . THR A 1 485 ? 27.447  2.224   -33.127 1.00 19.18 ? 485  THR A OG1 1 
ATOM   2454 C  CG2 . THR A 1 485 ? 29.041  0.683   -32.158 1.00 18.79 ? 485  THR A CG2 1 
ATOM   2455 N  N   . TRP A 1 486 ? 26.341  -1.111  -30.327 1.00 17.36 ? 486  TRP A N   1 
ATOM   2456 C  CA  . TRP A 1 486 ? 26.603  -2.165  -29.359 1.00 17.70 ? 486  TRP A CA  1 
ATOM   2457 C  C   . TRP A 1 486 ? 25.491  -3.257  -29.223 1.00 17.18 ? 486  TRP A C   1 
ATOM   2458 O  O   . TRP A 1 486 ? 25.700  -4.254  -28.534 1.00 17.46 ? 486  TRP A O   1 
ATOM   2459 C  CB  . TRP A 1 486 ? 26.908  -1.517  -28.007 1.00 18.93 ? 486  TRP A CB  1 
ATOM   2460 C  CG  . TRP A 1 486 ? 28.221  -0.722  -28.001 1.00 20.47 ? 486  TRP A CG  1 
ATOM   2461 C  CD1 . TRP A 1 486 ? 28.348  0.635   -28.032 1.00 21.35 ? 486  TRP A CD1 1 
ATOM   2462 C  CD2 . TRP A 1 486 ? 29.567  -1.244  -27.955 1.00 21.00 ? 486  TRP A CD2 1 
ATOM   2463 N  NE1 . TRP A 1 486 ? 29.671  0.994   -28.001 1.00 21.95 ? 486  TRP A NE1 1 
ATOM   2464 C  CE2 . TRP A 1 486 ? 30.444  -0.135  -27.960 1.00 22.76 ? 486  TRP A CE2 1 
ATOM   2465 C  CE3 . TRP A 1 486 ? 30.112  -2.535  -27.901 1.00 21.12 ? 486  TRP A CE3 1 
ATOM   2466 C  CZ2 . TRP A 1 486 ? 31.845  -0.274  -27.918 1.00 22.48 ? 486  TRP A CZ2 1 
ATOM   2467 C  CZ3 . TRP A 1 486 ? 31.501  -2.676  -27.856 1.00 21.57 ? 486  TRP A CZ3 1 
ATOM   2468 C  CH2 . TRP A 1 486 ? 32.351  -1.546  -27.873 1.00 22.04 ? 486  TRP A CH2 1 
ATOM   2469 N  N   . ALA A 1 487 ? 24.344  -3.093  -29.885 1.00 15.96 ? 487  ALA A N   1 
ATOM   2470 C  CA  . ALA A 1 487 ? 23.214  -4.040  -29.724 1.00 15.91 ? 487  ALA A CA  1 
ATOM   2471 C  C   . ALA A 1 487 ? 23.408  -5.332  -30.528 1.00 15.08 ? 487  ALA A C   1 
ATOM   2472 O  O   . ALA A 1 487 ? 23.592  -5.305  -31.750 1.00 14.76 ? 487  ALA A O   1 
ATOM   2473 C  CB  . ALA A 1 487 ? 21.883  -3.385  -30.111 1.00 15.21 ? 487  ALA A CB  1 
ATOM   2474 N  N   . ASN A 1 488 ? 23.330  -6.465  -29.842 1.00 15.18 ? 488  ASN A N   1 
ATOM   2475 C  CA  . ASN A 1 488 ? 23.358  -7.771  -30.520 1.00 14.77 ? 488  ASN A CA  1 
ATOM   2476 C  C   . ASN A 1 488 ? 22.915  -8.917  -29.611 1.00 14.55 ? 488  ASN A C   1 
ATOM   2477 O  O   . ASN A 1 488 ? 23.539  -9.990  -29.564 1.00 14.67 ? 488  ASN A O   1 
ATOM   2478 C  CB  . ASN A 1 488 ? 24.764  -8.046  -31.049 1.00 15.07 ? 488  ASN A CB  1 
ATOM   2479 C  CG  . ASN A 1 488 ? 25.775  -8.272  -29.945 1.00 15.11 ? 488  ASN A CG  1 
ATOM   2480 O  OD1 . ASN A 1 488 ? 25.657  -7.724  -28.841 1.00 15.71 ? 488  ASN A OD1 1 
ATOM   2481 N  ND2 . ASN A 1 488 ? 26.789  -9.098  -30.234 1.00 15.17 ? 488  ASN A ND2 1 
ATOM   2482 N  N   . ALA A 1 489 ? 21.823  -8.694  -28.900 1.00 14.24 ? 489  ALA A N   1 
ATOM   2483 C  CA  . ALA A 1 489 ? 21.235  -9.725  -28.064 1.00 14.16 ? 489  ALA A CA  1 
ATOM   2484 C  C   . ALA A 1 489 ? 20.863  -10.951 -28.880 1.00 14.04 ? 489  ALA A C   1 
ATOM   2485 O  O   . ALA A 1 489 ? 20.448  -10.841 -30.030 1.00 13.53 ? 489  ALA A O   1 
ATOM   2486 C  CB  . ALA A 1 489 ? 20.017  -9.181  -27.335 1.00 14.39 ? 489  ALA A CB  1 
ATOM   2487 N  N   . ALA A 1 490 ? 21.023  -12.120 -28.276 1.00 14.40 ? 490  ALA A N   1 
ATOM   2488 C  CA  . ALA A 1 490 ? 20.688  -13.369 -28.926 1.00 14.81 ? 490  ALA A CA  1 
ATOM   2489 C  C   . ALA A 1 490 ? 19.986  -14.305 -27.937 1.00 15.27 ? 490  ALA A C   1 
ATOM   2490 O  O   . ALA A 1 490 ? 20.254  -14.290 -26.736 1.00 14.54 ? 490  ALA A O   1 
ATOM   2491 C  CB  . ALA A 1 490 ? 21.958  -14.022 -29.481 1.00 15.69 ? 490  ALA A CB  1 
ATOM   2492 N  N   . ILE A 1 491 ? 19.031  -15.069 -28.454 1.00 15.76 ? 491  ILE A N   1 
ATOM   2493 C  CA  . ILE A 1 491 ? 18.536  -16.244 -27.776 1.00 16.30 ? 491  ILE A CA  1 
ATOM   2494 C  C   . ILE A 1 491 ? 19.230  -17.427 -28.453 1.00 16.31 ? 491  ILE A C   1 
ATOM   2495 O  O   . ILE A 1 491 ? 18.996  -17.715 -29.640 1.00 16.26 ? 491  ILE A O   1 
ATOM   2496 C  CB  . ILE A 1 491 ? 17.014  -16.393 -27.903 1.00 16.96 ? 491  ILE A CB  1 
ATOM   2497 C  CG1 . ILE A 1 491 ? 16.307  -15.220 -27.221 1.00 16.53 ? 491  ILE A CG1 1 
ATOM   2498 C  CG2 . ILE A 1 491 ? 16.573  -17.741 -27.317 1.00 17.17 ? 491  ILE A CG2 1 
ATOM   2499 C  CD1 . ILE A 1 491 ? 14.793  -15.275 -27.319 1.00 16.88 ? 491  ILE A CD1 1 
ATOM   2500 N  N   . GLY A 1 492 ? 20.099  -18.087 -27.707 1.00 15.25 ? 492  GLY A N   1 
ATOM   2501 C  CA  . GLY A 1 492 ? 20.903  -19.149 -28.255 1.00 15.88 ? 492  GLY A CA  1 
ATOM   2502 C  C   . GLY A 1 492 ? 20.283  -20.517 -28.079 1.00 15.97 ? 492  GLY A C   1 
ATOM   2503 O  O   . GLY A 1 492 ? 19.342  -20.699 -27.294 1.00 15.59 ? 492  GLY A O   1 
ATOM   2504 N  N   . ILE A 1 493 ? 20.822  -21.484 -28.818 1.00 15.61 ? 493  ILE A N   1 
ATOM   2505 C  CA  . ILE A 1 493 ? 20.456  -22.873 -28.614 1.00 16.05 ? 493  ILE A CA  1 
ATOM   2506 C  C   . ILE A 1 493 ? 21.687  -23.767 -28.851 1.00 16.83 ? 493  ILE A C   1 
ATOM   2507 O  O   . ILE A 1 493 ? 22.513  -23.511 -29.734 1.00 16.33 ? 493  ILE A O   1 
ATOM   2508 C  CB  . ILE A 1 493 ? 19.249  -23.311 -29.496 1.00 16.51 ? 493  ILE A CB  1 
ATOM   2509 C  CG1 . ILE A 1 493 ? 18.822  -24.746 -29.153 1.00 16.55 ? 493  ILE A CG1 1 
ATOM   2510 C  CG2 . ILE A 1 493 ? 19.591  -23.194 -30.968 1.00 16.73 ? 493  ILE A CG2 1 
ATOM   2511 C  CD1 . ILE A 1 493 ? 17.566  -25.222 -29.848 1.00 17.09 ? 493  ILE A CD1 1 
ATOM   2512 N  N   . LEU A 1 494 ? 21.812  -24.783 -28.011 1.00 17.13 ? 494  LEU A N   1 
ATOM   2513 C  CA  . LEU A 1 494 ? 22.804  -25.823 -28.178 1.00 17.48 ? 494  LEU A CA  1 
ATOM   2514 C  C   . LEU A 1 494 ? 22.182  -27.145 -27.777 1.00 17.74 ? 494  LEU A C   1 
ATOM   2515 O  O   . LEU A 1 494 ? 21.242  -27.178 -26.980 1.00 15.85 ? 494  LEU A O   1 
ATOM   2516 C  CB  . LEU A 1 494 ? 24.038  -25.553 -27.324 1.00 17.25 ? 494  LEU A CB  1 
ATOM   2517 C  CG  . LEU A 1 494 ? 23.867  -25.350 -25.811 1.00 17.27 ? 494  LEU A CG  1 
ATOM   2518 C  CD1 . LEU A 1 494 ? 23.864  -26.667 -25.027 1.00 17.37 ? 494  LEU A CD1 1 
ATOM   2519 C  CD2 . LEU A 1 494 ? 25.004  -24.455 -25.325 1.00 16.89 ? 494  LEU A CD2 1 
ATOM   2520 N  N   . LYS A 1 495 ? 22.726  -28.208 -28.354 1.00 18.29 ? 495  LYS A N   1 
ATOM   2521 C  CA  . LYS A 1 495 ? 22.386  -29.563 -27.997 1.00 19.85 ? 495  LYS A CA  1 
ATOM   2522 C  C   . LYS A 1 495 ? 23.388  -30.117 -26.978 1.00 20.51 ? 495  LYS A C   1 
ATOM   2523 O  O   . LYS A 1 495 ? 24.599  -29.944 -27.121 1.00 20.92 ? 495  LYS A O   1 
ATOM   2524 C  CB  . LYS A 1 495 ? 22.398  -30.443 -29.241 1.00 20.69 ? 495  LYS A CB  1 
ATOM   2525 C  CG  . LYS A 1 495 ? 22.019  -31.892 -28.943 1.00 22.04 ? 495  LYS A CG  1 
ATOM   2526 C  CD  . LYS A 1 495 ? 21.478  -32.601 -30.173 1.00 22.68 ? 495  LYS A CD  1 
ATOM   2527 C  CE  . LYS A 1 495 ? 22.560  -32.934 -31.164 1.00 24.27 ? 495  LYS A CE  1 
ATOM   2528 N  NZ  . LYS A 1 495 ? 21.905  -33.447 -32.398 1.00 25.44 ? 495  LYS A NZ  1 
ATOM   2529 N  N   . LEU A 1 496 ? 22.859  -30.768 -25.949 1.00 21.25 ? 496  LEU A N   1 
ATOM   2530 C  CA  . LEU A 1 496 ? 23.665  -31.456 -24.954 1.00 22.60 ? 496  LEU A CA  1 
ATOM   2531 C  C   . LEU A 1 496 ? 23.871  -32.910 -25.358 1.00 24.38 ? 496  LEU A C   1 
ATOM   2532 O  O   . LEU A 1 496 ? 23.104  -33.461 -26.162 1.00 22.26 ? 496  LEU A O   1 
ATOM   2533 C  CB  . LEU A 1 496 ? 22.964  -31.439 -23.591 1.00 21.76 ? 496  LEU A CB  1 
ATOM   2534 C  CG  . LEU A 1 496 ? 22.690  -30.086 -22.933 1.00 21.23 ? 496  LEU A CG  1 
ATOM   2535 C  CD1 . LEU A 1 496 ? 21.829  -30.305 -21.700 1.00 21.87 ? 496  LEU A CD1 1 
ATOM   2536 C  CD2 . LEU A 1 496 ? 23.966  -29.341 -22.563 1.00 20.42 ? 496  LEU A CD2 1 
ATOM   2537 N  N   . ASN A 1 497 ? 24.894  -33.530 -24.766 1.00 28.64 ? 497  ASN A N   1 
ATOM   2538 C  CA  . ASN A 1 497 ? 25.062  -34.988 -24.807 1.00 31.43 ? 497  ASN A CA  1 
ATOM   2539 C  C   . ASN A 1 497 ? 23.954  -35.669 -23.997 1.00 31.45 ? 497  ASN A C   1 
ATOM   2540 O  O   . ASN A 1 497 ? 23.040  -34.994 -23.508 1.00 27.86 ? 497  ASN A O   1 
ATOM   2541 C  CB  . ASN A 1 497 ? 26.465  -35.394 -24.327 1.00 34.04 ? 497  ASN A CB  1 
ATOM   2542 C  CG  . ASN A 1 497 ? 26.697  -35.133 -22.836 1.00 35.41 ? 497  ASN A CG  1 
ATOM   2543 O  OD1 . ASN A 1 497 ? 25.831  -34.646 -22.110 1.00 33.50 ? 497  ASN A OD1 1 
ATOM   2544 N  ND2 . ASN A 1 497 ? 27.898  -35.445 -22.385 1.00 38.26 ? 497  ASN A ND2 1 
ATOM   2545 N  N   . LYS A 1 498 ? 24.036  -36.991 -23.846 1.00 35.15 ? 498  LYS A N   1 
ATOM   2546 C  CA  . LYS A 1 498 ? 22.930  -37.784 -23.261 1.00 38.65 ? 498  LYS A CA  1 
ATOM   2547 C  C   . LYS A 1 498 ? 22.946  -37.854 -21.720 1.00 39.95 ? 498  LYS A C   1 
ATOM   2548 O  O   . LYS A 1 498 ? 21.912  -38.077 -21.071 1.00 37.86 ? 498  LYS A O   1 
ATOM   2549 C  CB  . LYS A 1 498 ? 22.977  -39.206 -23.827 1.00 40.96 ? 498  LYS A CB  1 
ATOM   2550 C  CG  . LYS A 1 498 ? 23.116  -39.248 -25.346 1.00 41.03 ? 498  LYS A CG  1 
ATOM   2551 C  CD  . LYS A 1 498 ? 21.815  -38.833 -26.017 1.00 38.68 ? 498  LYS A CD  1 
ATOM   2552 C  CE  . LYS A 1 498 ? 20.948  -40.039 -26.297 1.00 38.18 ? 498  LYS A CE  1 
ATOM   2553 N  NZ  . LYS A 1 498 ? 19.862  -39.708 -27.253 1.00 37.65 ? 498  LYS A NZ  1 
ATOM   2554 N  N   . ASP A 1 499 ? 24.136  -37.674 -21.163 1.00 40.39 ? 499  ASP A N   1 
ATOM   2555 C  CA  . ASP A 1 499 ? 24.402  -37.786 -19.732 1.00 38.70 ? 499  ASP A CA  1 
ATOM   2556 C  C   . ASP A 1 499 ? 23.542  -36.799 -18.928 1.00 37.56 ? 499  ASP A C   1 
ATOM   2557 O  O   . ASP A 1 499 ? 23.890  -35.630 -18.806 1.00 39.08 ? 499  ASP A O   1 
ATOM   2558 C  CB  . ASP A 1 499 ? 25.899  -37.502 -19.517 1.00 38.65 ? 499  ASP A CB  1 
ATOM   2559 C  CG  . ASP A 1 499 ? 26.436  -38.075 -18.220 1.00 40.46 ? 499  ASP A CG  1 
ATOM   2560 O  OD1 . ASP A 1 499 ? 25.653  -38.242 -17.253 1.00 39.28 ? 499  ASP A OD1 1 
ATOM   2561 O  OD2 . ASP A 1 499 ? 27.660  -38.356 -18.193 1.00 39.79 ? 499  ASP A OD2 1 
ATOM   2562 N  N   . GLU A 1 500 ? 22.419  -37.271 -18.396 1.00 35.68 ? 500  GLU A N   1 
ATOM   2563 C  CA  . GLU A 1 500 ? 21.516  -36.422 -17.618 1.00 37.60 ? 500  GLU A CA  1 
ATOM   2564 C  C   . GLU A 1 500 ? 22.199  -35.601 -16.507 1.00 36.20 ? 500  GLU A C   1 
ATOM   2565 O  O   . GLU A 1 500 ? 21.860  -34.437 -16.274 1.00 33.46 ? 500  GLU A O   1 
ATOM   2566 C  CB  . GLU A 1 500 ? 20.457  -37.275 -16.943 1.00 40.19 ? 500  GLU A CB  1 
ATOM   2567 C  CG  . GLU A 1 500 ? 19.354  -37.783 -17.841 1.00 42.90 ? 500  GLU A CG  1 
ATOM   2568 C  CD  . GLU A 1 500 ? 18.314  -38.530 -17.037 1.00 45.37 ? 500  GLU A CD  1 
ATOM   2569 O  OE1 . GLU A 1 500 ? 18.644  -38.943 -15.905 1.00 47.41 ? 500  GLU A OE1 1 
ATOM   2570 O  OE2 . GLU A 1 500 ? 17.176  -38.691 -17.525 1.00 49.93 ? 500  GLU A OE2 1 
ATOM   2571 N  N   . LYS A 1 501 ? 23.123  -36.236 -15.795 1.00 33.76 ? 501  LYS A N   1 
ATOM   2572 C  CA  . LYS A 1 501 ? 23.671  -35.667 -14.570 1.00 32.14 ? 501  LYS A CA  1 
ATOM   2573 C  C   . LYS A 1 501 ? 24.993  -34.975 -14.800 1.00 29.91 ? 501  LYS A C   1 
ATOM   2574 O  O   . LYS A 1 501 ? 25.450  -34.225 -13.944 1.00 30.82 ? 501  LYS A O   1 
ATOM   2575 C  CB  . LYS A 1 501 ? 23.822  -36.750 -13.507 1.00 31.60 ? 501  LYS A CB  1 
ATOM   2576 C  CG  . LYS A 1 501 ? 22.503  -37.371 -13.081 1.00 31.64 ? 501  LYS A CG  1 
ATOM   2577 C  CD  . LYS A 1 501 ? 22.740  -38.431 -12.018 1.00 31.95 ? 501  LYS A CD  1 
ATOM   2578 C  CE  . LYS A 1 501 ? 21.470  -39.191 -11.699 1.00 32.12 ? 501  LYS A CE  1 
ATOM   2579 N  NZ  . LYS A 1 501 ? 21.635  -40.000 -10.461 1.00 32.67 ? 501  LYS A NZ  1 
ATOM   2580 N  N   . ASN A 1 502 ? 25.620  -35.233 -15.941 1.00 28.76 ? 502  ASN A N   1 
ATOM   2581 C  CA  . ASN A 1 502 ? 26.826  -34.513 -16.310 1.00 28.99 ? 502  ASN A CA  1 
ATOM   2582 C  C   . ASN A 1 502 ? 26.764  -33.981 -17.757 1.00 27.73 ? 502  ASN A C   1 
ATOM   2583 O  O   . ASN A 1 502 ? 27.603  -34.296 -18.584 1.00 26.34 ? 502  ASN A O   1 
ATOM   2584 C  CB  . ASN A 1 502 ? 28.043  -35.394 -16.069 1.00 31.18 ? 502  ASN A CB  1 
ATOM   2585 C  CG  . ASN A 1 502 ? 29.349  -34.611 -16.055 1.00 33.24 ? 502  ASN A CG  1 
ATOM   2586 O  OD1 . ASN A 1 502 ? 29.388  -33.401 -15.796 1.00 33.78 ? 502  ASN A OD1 1 
ATOM   2587 N  ND2 . ASN A 1 502 ? 30.433  -35.308 -16.334 1.00 35.54 ? 502  ASN A ND2 1 
ATOM   2588 N  N   . PRO A 1 503 ? 25.780  -33.119 -18.047 1.00 27.52 ? 503  PRO A N   1 
ATOM   2589 C  CA  . PRO A 1 503 ? 25.667  -32.574 -19.406 1.00 28.59 ? 503  PRO A CA  1 
ATOM   2590 C  C   . PRO A 1 503 ? 26.898  -31.786 -19.877 1.00 27.85 ? 503  PRO A C   1 
ATOM   2591 O  O   . PRO A 1 503 ? 27.443  -30.973 -19.131 1.00 27.04 ? 503  PRO A O   1 
ATOM   2592 C  CB  . PRO A 1 503 ? 24.431  -31.661 -19.320 1.00 28.15 ? 503  PRO A CB  1 
ATOM   2593 C  CG  . PRO A 1 503 ? 24.313  -31.323 -17.875 1.00 28.18 ? 503  PRO A CG  1 
ATOM   2594 C  CD  . PRO A 1 503 ? 24.774  -32.546 -17.141 1.00 27.11 ? 503  PRO A CD  1 
ATOM   2595 N  N   . LYS A 1 504 ? 27.345  -32.084 -21.090 1.00 27.65 ? 504  LYS A N   1 
ATOM   2596 C  CA  . LYS A 1 504 ? 28.283  -31.254 -21.809 1.00 28.97 ? 504  LYS A CA  1 
ATOM   2597 C  C   . LYS A 1 504 ? 27.732  -30.918 -23.201 1.00 26.17 ? 504  LYS A C   1 
ATOM   2598 O  O   . LYS A 1 504 ? 26.836  -31.588 -23.721 1.00 22.83 ? 504  LYS A O   1 
ATOM   2599 C  CB  . LYS A 1 504 ? 29.629  -31.951 -21.935 1.00 33.54 ? 504  LYS A CB  1 
ATOM   2600 C  CG  . LYS A 1 504 ? 30.393  -32.075 -20.624 1.00 37.51 ? 504  LYS A CG  1 
ATOM   2601 C  CD  . LYS A 1 504 ? 31.886  -32.215 -20.907 1.00 41.48 ? 504  LYS A CD  1 
ATOM   2602 C  CE  . LYS A 1 504 ? 32.695  -32.399 -19.636 1.00 44.10 ? 504  LYS A CE  1 
ATOM   2603 N  NZ  . LYS A 1 504 ? 32.398  -33.716 -19.012 1.00 45.66 ? 504  LYS A NZ  1 
ATOM   2604 N  N   . VAL A 1 505 ? 28.302  -29.890 -23.802 1.00 23.61 ? 505  VAL A N   1 
ATOM   2605 C  CA  . VAL A 1 505 ? 27.873  -29.428 -25.111 1.00 24.08 ? 505  VAL A CA  1 
ATOM   2606 C  C   . VAL A 1 505 ? 28.164  -30.489 -26.153 1.00 23.11 ? 505  VAL A C   1 
ATOM   2607 O  O   . VAL A 1 505 ? 29.304  -30.873 -26.297 1.00 22.99 ? 505  VAL A O   1 
ATOM   2608 C  CB  . VAL A 1 505 ? 28.614  -28.137 -25.523 1.00 23.98 ? 505  VAL A CB  1 
ATOM   2609 C  CG1 . VAL A 1 505 ? 28.271  -27.737 -26.954 1.00 24.69 ? 505  VAL A CG1 1 
ATOM   2610 C  CG2 . VAL A 1 505 ? 28.276  -27.001 -24.568 1.00 24.10 ? 505  VAL A CG2 1 
ATOM   2611 N  N   . ALA A 1 506 ? 27.135  -30.944 -26.878 1.00 22.38 ? 506  ALA A N   1 
ATOM   2612 C  CA  . ALA A 1 506 ? 27.326  -31.816 -28.031 1.00 21.79 ? 506  ALA A CA  1 
ATOM   2613 C  C   . ALA A 1 506 ? 27.368  -31.025 -29.344 1.00 22.38 ? 506  ALA A C   1 
ATOM   2614 O  O   . ALA A 1 506 ? 28.145  -31.360 -30.231 1.00 21.90 ? 506  ALA A O   1 
ATOM   2615 C  CB  . ALA A 1 506 ? 26.247  -32.904 -28.092 1.00 22.08 ? 506  ALA A CB  1 
ATOM   2616 N  N   . GLU A 1 507 ? 26.533  -29.997 -29.494 1.00 22.98 ? 507  GLU A N   1 
ATOM   2617 C  CA  . GLU A 1 507 ? 26.580  -29.183 -30.711 1.00 23.28 ? 507  GLU A CA  1 
ATOM   2618 C  C   . GLU A 1 507 ? 26.051  -27.750 -30.513 1.00 21.92 ? 507  GLU A C   1 
ATOM   2619 O  O   . GLU A 1 507 ? 25.104  -27.544 -29.774 1.00 21.46 ? 507  GLU A O   1 
ATOM   2620 C  CB  . GLU A 1 507 ? 25.785  -29.887 -31.801 1.00 25.12 ? 507  GLU A CB  1 
ATOM   2621 C  CG  . GLU A 1 507 ? 26.116  -29.423 -33.196 1.00 28.12 ? 507  GLU A CG  1 
ATOM   2622 C  CD  . GLU A 1 507 ? 25.427  -30.275 -34.247 1.00 31.03 ? 507  GLU A CD  1 
ATOM   2623 O  OE1 . GLU A 1 507 ? 24.626  -31.166 -33.890 1.00 33.23 ? 507  GLU A OE1 1 
ATOM   2624 O  OE2 . GLU A 1 507 ? 25.685  -30.042 -35.433 1.00 35.38 ? 507  GLU A OE2 1 
ATOM   2625 N  N   . LEU A 1 508 ? 26.695  -26.778 -31.155 1.00 20.58 ? 508  LEU A N   1 
ATOM   2626 C  CA  . LEU A 1 508 ? 26.251  -25.381 -31.139 1.00 21.00 ? 508  LEU A CA  1 
ATOM   2627 C  C   . LEU A 1 508 ? 25.514  -25.031 -32.415 1.00 19.90 ? 508  LEU A C   1 
ATOM   2628 O  O   . LEU A 1 508 ? 25.846  -25.544 -33.481 1.00 18.21 ? 508  LEU A O   1 
ATOM   2629 C  CB  . LEU A 1 508 ? 27.436  -24.426 -31.026 1.00 20.56 ? 508  LEU A CB  1 
ATOM   2630 C  CG  . LEU A 1 508 ? 28.232  -24.463 -29.744 1.00 21.45 ? 508  LEU A CG  1 
ATOM   2631 C  CD1 . LEU A 1 508 ? 29.392  -23.467 -29.840 1.00 22.46 ? 508  LEU A CD1 1 
ATOM   2632 C  CD2 . LEU A 1 508 ? 27.359  -24.185 -28.537 1.00 21.00 ? 508  LEU A CD2 1 
ATOM   2633 N  N   . TYR A 1 509 ? 24.531  -24.145 -32.295 1.00 19.41 ? 509  TYR A N   1 
ATOM   2634 C  CA  . TYR A 1 509 ? 23.827  -23.626 -33.461 1.00 19.94 ? 509  TYR A CA  1 
ATOM   2635 C  C   . TYR A 1 509 ? 23.843  -22.102 -33.490 1.00 19.68 ? 509  TYR A C   1 
ATOM   2636 O  O   . TYR A 1 509 ? 24.143  -21.454 -32.485 1.00 20.11 ? 509  TYR A O   1 
ATOM   2637 C  CB  . TYR A 1 509 ? 22.393  -24.152 -33.471 1.00 20.65 ? 509  TYR A CB  1 
ATOM   2638 C  CG  . TYR A 1 509 ? 22.310  -25.660 -33.318 1.00 21.32 ? 509  TYR A CG  1 
ATOM   2639 C  CD1 . TYR A 1 509 ? 22.433  -26.506 -34.428 1.00 21.98 ? 509  TYR A CD1 1 
ATOM   2640 C  CD2 . TYR A 1 509 ? 22.136  -26.238 -32.073 1.00 21.61 ? 509  TYR A CD2 1 
ATOM   2641 C  CE1 . TYR A 1 509 ? 22.364  -27.877 -34.293 1.00 22.27 ? 509  TYR A CE1 1 
ATOM   2642 C  CE2 . TYR A 1 509 ? 22.070  -27.613 -31.922 1.00 21.97 ? 509  TYR A CE2 1 
ATOM   2643 C  CZ  . TYR A 1 509 ? 22.180  -28.429 -33.034 1.00 22.78 ? 509  TYR A CZ  1 
ATOM   2644 O  OH  . TYR A 1 509 ? 22.109  -29.799 -32.883 1.00 22.04 ? 509  TYR A OH  1 
ATOM   2645 N  N   . SER A 1 510 ? 23.538  -21.540 -34.656 1.00 19.15 ? 510  SER A N   1 
ATOM   2646 C  CA  . SER A 1 510 ? 23.195  -20.133 -34.762 1.00 19.53 ? 510  SER A CA  1 
ATOM   2647 C  C   . SER A 1 510 ? 22.006  -19.797 -33.856 1.00 18.22 ? 510  SER A C   1 
ATOM   2648 O  O   . SER A 1 510 ? 21.147  -20.646 -33.604 1.00 18.96 ? 510  SER A O   1 
ATOM   2649 C  CB  . SER A 1 510 ? 22.817  -19.766 -36.191 1.00 20.12 ? 510  SER A CB  1 
ATOM   2650 O  OG  . SER A 1 510 ? 23.890  -20.012 -37.062 1.00 22.83 ? 510  SER A OG  1 
ATOM   2651 N  N   . PRO A 1 511 ? 21.953  -18.553 -33.373 1.00 17.48 ? 511  PRO A N   1 
ATOM   2652 C  CA  . PRO A 1 511 ? 20.853  -18.103 -32.519 1.00 17.36 ? 511  PRO A CA  1 
ATOM   2653 C  C   . PRO A 1 511 ? 19.493  -18.365 -33.130 1.00 16.54 ? 511  PRO A C   1 
ATOM   2654 O  O   . PRO A 1 511 ? 19.321  -18.255 -34.346 1.00 16.40 ? 511  PRO A O   1 
ATOM   2655 C  CB  . PRO A 1 511 ? 21.076  -16.594 -32.416 1.00 17.57 ? 511  PRO A CB  1 
ATOM   2656 C  CG  . PRO A 1 511 ? 22.512  -16.398 -32.644 1.00 17.59 ? 511  PRO A CG  1 
ATOM   2657 C  CD  . PRO A 1 511 ? 23.041  -17.567 -33.436 1.00 17.18 ? 511  PRO A CD  1 
ATOM   2658 N  N   . LEU A 1 512 ? 18.536  -18.714 -32.286 1.00 15.92 ? 512  LEU A N   1 
ATOM   2659 C  CA  . LEU A 1 512 ? 17.163  -18.805 -32.722 1.00 16.18 ? 512  LEU A CA  1 
ATOM   2660 C  C   . LEU A 1 512 ? 16.625  -17.405 -33.038 1.00 15.70 ? 512  LEU A C   1 
ATOM   2661 O  O   . LEU A 1 512 ? 15.992  -17.209 -34.046 1.00 15.84 ? 512  LEU A O   1 
ATOM   2662 C  CB  . LEU A 1 512 ? 16.316  -19.455 -31.642 1.00 16.41 ? 512  LEU A CB  1 
ATOM   2663 C  CG  . LEU A 1 512 ? 16.702  -20.893 -31.268 1.00 16.60 ? 512  LEU A CG  1 
ATOM   2664 C  CD1 . LEU A 1 512 ? 15.746  -21.386 -30.190 1.00 16.64 ? 512  LEU A CD1 1 
ATOM   2665 C  CD2 . LEU A 1 512 ? 16.674  -21.798 -32.491 1.00 16.25 ? 512  LEU A CD2 1 
ATOM   2666 N  N   . ILE A 1 513 ? 16.881  -16.446 -32.151 1.00 15.80 ? 513  ILE A N   1 
ATOM   2667 C  CA  . ILE A 1 513 ? 16.453  -15.059 -32.317 1.00 15.60 ? 513  ILE A CA  1 
ATOM   2668 C  C   . ILE A 1 513 ? 17.721  -14.218 -32.110 1.00 15.14 ? 513  ILE A C   1 
ATOM   2669 O  O   . ILE A 1 513 ? 18.567  -14.578 -31.295 1.00 15.16 ? 513  ILE A O   1 
ATOM   2670 C  CB  . ILE A 1 513 ? 15.354  -14.669 -31.274 1.00 16.51 ? 513  ILE A CB  1 
ATOM   2671 C  CG1 . ILE A 1 513 ? 14.106  -15.551 -31.398 1.00 17.02 ? 513  ILE A CG1 1 
ATOM   2672 C  CG2 . ILE A 1 513 ? 14.961  -13.185 -31.345 1.00 16.54 ? 513  ILE A CG2 1 
ATOM   2673 C  CD1 . ILE A 1 513 ? 13.288  -15.323 -32.651 1.00 18.28 ? 513  ILE A CD1 1 
ATOM   2674 N  N   . SER A 1 514 ? 17.882  -13.134 -32.867 1.00 14.30 ? 514  SER A N   1 
ATOM   2675 C  CA  . SER A 1 514 ? 18.924  -12.144 -32.584 1.00 14.73 ? 514  SER A CA  1 
ATOM   2676 C  C   . SER A 1 514 ? 18.374  -10.738 -32.800 1.00 14.92 ? 514  SER A C   1 
ATOM   2677 O  O   . SER A 1 514 ? 17.399  -10.568 -33.527 1.00 14.98 ? 514  SER A O   1 
ATOM   2678 C  CB  . SER A 1 514 ? 20.157  -12.390 -33.448 1.00 14.84 ? 514  SER A CB  1 
ATOM   2679 O  OG  . SER A 1 514 ? 19.880  -12.186 -34.836 1.00 15.24 ? 514  SER A OG  1 
ATOM   2680 N  N   . ALA A 1 515 ? 18.975  -9.734  -32.161 1.00 15.28 ? 515  ALA A N   1 
ATOM   2681 C  CA  . ALA A 1 515 ? 18.521  -8.348  -32.328 1.00 15.41 ? 515  ALA A CA  1 
ATOM   2682 C  C   . ALA A 1 515 ? 19.682  -7.382  -32.605 1.00 15.86 ? 515  ALA A C   1 
ATOM   2683 O  O   . ALA A 1 515 ? 19.813  -6.340  -31.951 1.00 15.30 ? 515  ALA A O   1 
ATOM   2684 C  CB  . ALA A 1 515 ? 17.724  -7.900  -31.117 1.00 15.66 ? 515  ALA A CB  1 
ATOM   2685 N  N   . PRO A 1 516 ? 20.508  -7.702  -33.618 1.00 16.23 ? 516  PRO A N   1 
ATOM   2686 C  CA  . PRO A 1 516 ? 21.574  -6.765  -33.942 1.00 16.14 ? 516  PRO A CA  1 
ATOM   2687 C  C   . PRO A 1 516 ? 21.010  -5.392  -34.339 1.00 16.16 ? 516  PRO A C   1 
ATOM   2688 O  O   . PRO A 1 516 ? 19.985  -5.321  -35.025 1.00 15.69 ? 516  PRO A O   1 
ATOM   2689 C  CB  . PRO A 1 516 ? 22.322  -7.445  -35.096 1.00 16.15 ? 516  PRO A CB  1 
ATOM   2690 C  CG  . PRO A 1 516 ? 21.333  -8.349  -35.713 1.00 17.05 ? 516  PRO A CG  1 
ATOM   2691 C  CD  . PRO A 1 516 ? 20.412  -8.804  -34.593 1.00 16.62 ? 516  PRO A CD  1 
ATOM   2692 N  N   . MET A 1 517 ? 21.667  -4.328  -33.859 1.00 16.49 ? 517  MET A N   1 
ATOM   2693 C  CA  . MET A 1 517 ? 21.237  -2.936  -34.053 1.00 15.79 ? 517  MET A CA  1 
ATOM   2694 C  C   . MET A 1 517 ? 20.056  -2.504  -33.182 1.00 15.65 ? 517  MET A C   1 
ATOM   2695 O  O   . MET A 1 517 ? 19.803  -1.292  -33.055 1.00 15.15 ? 517  MET A O   1 
ATOM   2696 C  CB  . MET A 1 517 ? 20.895  -2.664  -35.514 1.00 16.24 ? 517  MET A CB  1 
ATOM   2697 C  CG  . MET A 1 517 ? 21.050  -1.206  -35.935 1.00 16.40 ? 517  MET A CG  1 
ATOM   2698 S  SD  . MET A 1 517 ? 20.370  -0.910  -37.566 1.00 17.15 ? 517  MET A SD  1 
ATOM   2699 C  CE  . MET A 1 517 ? 18.629  -0.768  -37.128 1.00 17.56 ? 517  MET A CE  1 
ATOM   2700 N  N   . VAL A 1 518 ? 19.362  -3.472  -32.562 1.00 15.66 ? 518  VAL A N   1 
ATOM   2701 C  CA  . VAL A 1 518 ? 18.006  -3.269  -32.012 1.00 15.44 ? 518  VAL A CA  1 
ATOM   2702 C  C   . VAL A 1 518 ? 17.912  -3.339  -30.475 1.00 15.68 ? 518  VAL A C   1 
ATOM   2703 O  O   . VAL A 1 518 ? 17.289  -2.473  -29.862 1.00 16.40 ? 518  VAL A O   1 
ATOM   2704 C  CB  . VAL A 1 518 ? 17.017  -4.260  -32.672 1.00 15.63 ? 518  VAL A CB  1 
ATOM   2705 C  CG1 . VAL A 1 518 ? 15.608  -4.105  -32.120 1.00 15.80 ? 518  VAL A CG1 1 
ATOM   2706 C  CG2 . VAL A 1 518 ? 17.007  -4.061  -34.184 1.00 15.82 ? 518  VAL A CG2 1 
ATOM   2707 N  N   . SER A 1 519 ? 18.508  -4.366  -29.865 1.00 15.37 ? 519  SER A N   1 
ATOM   2708 C  CA  . SER A 1 519 ? 18.531  -4.524  -28.414 1.00 15.74 ? 519  SER A CA  1 
ATOM   2709 C  C   . SER A 1 519 ? 19.740  -5.328  -27.949 1.00 15.91 ? 519  SER A C   1 
ATOM   2710 O  O   . SER A 1 519 ? 20.193  -6.249  -28.641 1.00 14.57 ? 519  SER A O   1 
ATOM   2711 C  CB  . SER A 1 519 ? 17.264  -5.220  -27.915 1.00 16.80 ? 519  SER A CB  1 
ATOM   2712 O  OG  . SER A 1 519 ? 17.295  -5.363  -26.493 1.00 18.20 ? 519  SER A OG  1 
ATOM   2713 N  N   . ASP A 1 520 ? 20.247  -4.992  -26.763 1.00 16.08 ? 520  ASP A N   1 
ATOM   2714 C  CA  . ASP A 1 520 ? 21.344  -5.742  -26.183 1.00 16.47 ? 520  ASP A CA  1 
ATOM   2715 C  C   . ASP A 1 520 ? 20.895  -6.544  -24.948 1.00 16.62 ? 520  ASP A C   1 
ATOM   2716 O  O   . ASP A 1 520 ? 21.738  -7.016  -24.191 1.00 16.39 ? 520  ASP A O   1 
ATOM   2717 C  CB  . ASP A 1 520 ? 22.523  -4.791  -25.835 1.00 16.86 ? 520  ASP A CB  1 
ATOM   2718 C  CG  . ASP A 1 520 ? 23.911  -5.373  -26.175 1.00 17.30 ? 520  ASP A CG  1 
ATOM   2719 O  OD1 . ASP A 1 520 ? 24.029  -6.308  -27.008 1.00 16.38 ? 520  ASP A OD1 1 
ATOM   2720 O  OD2 . ASP A 1 520 ? 24.912  -4.830  -25.621 1.00 17.59 ? 520  ASP A OD2 1 
ATOM   2721 N  N   . GLU A 1 521 ? 19.592  -6.736  -24.749 1.00 17.22 ? 521  GLU A N   1 
ATOM   2722 C  CA  . GLU A 1 521 ? 19.129  -7.616  -23.654 1.00 17.28 ? 521  GLU A CA  1 
ATOM   2723 C  C   . GLU A 1 521 ? 17.725  -8.183  -23.851 1.00 17.79 ? 521  GLU A C   1 
ATOM   2724 O  O   . GLU A 1 521 ? 16.727  -7.448  -23.831 1.00 16.96 ? 521  GLU A O   1 
ATOM   2725 C  CB  . GLU A 1 521 ? 19.180  -6.878  -22.318 1.00 17.58 ? 521  GLU A CB  1 
ATOM   2726 C  CG  . GLU A 1 521 ? 19.125  -7.795  -21.115 1.00 17.58 ? 521  GLU A CG  1 
ATOM   2727 C  CD  . GLU A 1 521 ? 19.347  -7.034  -19.827 1.00 18.26 ? 521  GLU A CD  1 
ATOM   2728 O  OE1 . GLU A 1 521 ? 18.384  -6.370  -19.376 1.00 19.09 ? 521  GLU A OE1 1 
ATOM   2729 O  OE2 . GLU A 1 521 ? 20.483  -7.087  -19.294 1.00 18.61 ? 521  GLU A OE2 1 
ATOM   2730 N  N   . ILE A 1 522 ? 17.668  -9.510  -24.011 1.00 17.55 ? 522  ILE A N   1 
ATOM   2731 C  CA  . ILE A 1 522 ? 16.423  -10.252 -24.078 1.00 16.99 ? 522  ILE A CA  1 
ATOM   2732 C  C   . ILE A 1 522 ? 16.603  -11.467 -23.154 1.00 17.20 ? 522  ILE A C   1 
ATOM   2733 O  O   . ILE A 1 522 ? 17.490  -12.294 -23.370 1.00 16.93 ? 522  ILE A O   1 
ATOM   2734 C  CB  . ILE A 1 522 ? 16.119  -10.704 -25.520 1.00 16.27 ? 522  ILE A CB  1 
ATOM   2735 C  CG1 . ILE A 1 522 ? 15.844  -9.497  -26.428 1.00 16.24 ? 522  ILE A CG1 1 
ATOM   2736 C  CG2 . ILE A 1 522 ? 14.928  -11.639 -25.552 1.00 16.45 ? 522  ILE A CG2 1 
ATOM   2737 C  CD1 . ILE A 1 522 ? 15.951  -9.827  -27.909 1.00 15.68 ? 522  ILE A CD1 1 
ATOM   2738 N  N   . GLU A 1 523 ? 15.748  -11.583 -22.148 1.00 17.90 ? 523  GLU A N   1 
ATOM   2739 C  CA  . GLU A 1 523 ? 16.016  -12.454 -21.005 1.00 18.66 ? 523  GLU A CA  1 
ATOM   2740 C  C   . GLU A 1 523 ? 15.015  -13.581 -20.829 1.00 18.91 ? 523  GLU A C   1 
ATOM   2741 O  O   . GLU A 1 523 ? 13.927  -13.579 -21.420 1.00 18.17 ? 523  GLU A O   1 
ATOM   2742 C  CB  . GLU A 1 523 ? 16.027  -11.614 -19.732 1.00 19.61 ? 523  GLU A CB  1 
ATOM   2743 C  CG  . GLU A 1 523 ? 16.805  -10.313 -19.865 1.00 20.61 ? 523  GLU A CG  1 
ATOM   2744 C  CD  . GLU A 1 523 ? 16.976  -9.642  -18.519 1.00 22.39 ? 523  GLU A CD  1 
ATOM   2745 O  OE1 . GLU A 1 523 ? 15.991  -9.045  -18.037 1.00 22.57 ? 523  GLU A OE1 1 
ATOM   2746 O  OE2 . GLU A 1 523 ? 18.101  -9.707  -17.964 1.00 24.09 ? 523  GLU A OE2 1 
ATOM   2747 N  N   . ARG A 1 524 ? 15.395  -14.535 -19.982 1.00 19.54 ? 524  ARG A N   1 
ATOM   2748 C  CA  . ARG A 1 524 ? 14.505  -15.619 -19.565 1.00 20.78 ? 524  ARG A CA  1 
ATOM   2749 C  C   . ARG A 1 524 ? 13.821  -16.293 -20.740 1.00 19.36 ? 524  ARG A C   1 
ATOM   2750 O  O   . ARG A 1 524 ? 12.619  -16.456 -20.743 1.00 20.47 ? 524  ARG A O   1 
ATOM   2751 C  CB  . ARG A 1 524 ? 13.479  -15.085 -18.582 1.00 22.69 ? 524  ARG A CB  1 
ATOM   2752 C  CG  . ARG A 1 524 ? 14.150  -14.596 -17.313 1.00 26.12 ? 524  ARG A CG  1 
ATOM   2753 C  CD  . ARG A 1 524 ? 14.307  -15.737 -16.320 1.00 27.99 ? 524  ARG A CD  1 
ATOM   2754 N  NE  . ARG A 1 524 ? 13.181  -15.633 -15.406 1.00 31.72 ? 524  ARG A NE  1 
ATOM   2755 C  CZ  . ARG A 1 524 ? 12.497  -16.638 -14.884 1.00 30.84 ? 524  ARG A CZ  1 
ATOM   2756 N  NH1 . ARG A 1 524 ? 11.477  -16.346 -14.080 1.00 32.35 ? 524  ARG A NH1 1 
ATOM   2757 N  NH2 . ARG A 1 524 ? 12.808  -17.901 -15.140 1.00 29.86 ? 524  ARG A NH2 1 
ATOM   2758 N  N   . PRO A 1 525 ? 14.599  -16.711 -21.733 1.00 18.52 ? 525  PRO A N   1 
ATOM   2759 C  CA  . PRO A 1 525 ? 13.983  -17.452 -22.818 1.00 19.63 ? 525  PRO A CA  1 
ATOM   2760 C  C   . PRO A 1 525 ? 13.379  -18.757 -22.303 1.00 20.07 ? 525  PRO A C   1 
ATOM   2761 O  O   . PRO A 1 525 ? 13.932  -19.413 -21.412 1.00 19.51 ? 525  PRO A O   1 
ATOM   2762 C  CB  . PRO A 1 525 ? 15.148  -17.722 -23.768 1.00 19.12 ? 525  PRO A CB  1 
ATOM   2763 C  CG  . PRO A 1 525 ? 16.354  -17.716 -22.884 1.00 18.64 ? 525  PRO A CG  1 
ATOM   2764 C  CD  . PRO A 1 525 ? 16.062  -16.671 -21.854 1.00 18.46 ? 525  PRO A CD  1 
ATOM   2765 N  N   . ASN A 1 526 ? 12.242  -19.106 -22.871 1.00 20.68 ? 526  ASN A N   1 
ATOM   2766 C  CA  . ASN A 1 526 ? 11.452  -20.206 -22.390 1.00 21.40 ? 526  ASN A CA  1 
ATOM   2767 C  C   . ASN A 1 526 ? 10.764  -20.871 -23.584 1.00 21.15 ? 526  ASN A C   1 
ATOM   2768 O  O   . ASN A 1 526 ? 10.227  -20.187 -24.431 1.00 21.07 ? 526  ASN A O   1 
ATOM   2769 C  CB  . ASN A 1 526 ? 10.440  -19.664 -21.389 1.00 21.15 ? 526  ASN A CB  1 
ATOM   2770 C  CG  . ASN A 1 526 ? 9.474   -20.721 -20.906 1.00 22.10 ? 526  ASN A CG  1 
ATOM   2771 O  OD1 . ASN A 1 526 ? 9.829   -21.900 -20.754 1.00 21.51 ? 526  ASN A OD1 1 
ATOM   2772 N  ND2 . ASN A 1 526 ? 8.231   -20.309 -20.682 1.00 21.86 ? 526  ASN A ND2 1 
ATOM   2773 N  N   . VAL A 1 527 ? 10.828  -22.193 -23.665 1.00 20.86 ? 527  VAL A N   1 
ATOM   2774 C  CA  . VAL A 1 527 ? 10.152  -22.925 -24.722 1.00 21.28 ? 527  VAL A CA  1 
ATOM   2775 C  C   . VAL A 1 527 ? 9.011   -23.782 -24.156 1.00 22.53 ? 527  VAL A C   1 
ATOM   2776 O  O   . VAL A 1 527 ? 9.210   -24.616 -23.267 1.00 23.23 ? 527  VAL A O   1 
ATOM   2777 C  CB  . VAL A 1 527 ? 11.121  -23.803 -25.511 1.00 21.71 ? 527  VAL A CB  1 
ATOM   2778 C  CG1 . VAL A 1 527 ? 10.374  -24.546 -26.622 1.00 22.44 ? 527  VAL A CG1 1 
ATOM   2779 C  CG2 . VAL A 1 527 ? 12.233  -22.951 -26.088 1.00 21.77 ? 527  VAL A CG2 1 
ATOM   2780 N  N   . VAL A 1 528 ? 7.806   -23.541 -24.668 1.00 23.13 ? 528  VAL A N   1 
ATOM   2781 C  CA  . VAL A 1 528 ? 6.637   -24.337 -24.338 1.00 23.49 ? 528  VAL A CA  1 
ATOM   2782 C  C   . VAL A 1 528 ? 6.182   -25.069 -25.594 1.00 24.12 ? 528  VAL A C   1 
ATOM   2783 O  O   . VAL A 1 528 ? 5.938   -24.444 -26.633 1.00 21.53 ? 528  VAL A O   1 
ATOM   2784 C  CB  . VAL A 1 528 ? 5.491   -23.439 -23.825 1.00 23.99 ? 528  VAL A CB  1 
ATOM   2785 C  CG1 . VAL A 1 528 ? 4.272   -24.276 -23.479 1.00 25.08 ? 528  VAL A CG1 1 
ATOM   2786 C  CG2 . VAL A 1 528 ? 5.942   -22.645 -22.612 1.00 24.21 ? 528  VAL A CG2 1 
ATOM   2787 N  N   . LYS A 1 529 ? 6.099   -26.394 -25.507 1.00 25.67 ? 529  LYS A N   1 
ATOM   2788 C  CA  . LYS A 1 529 ? 5.518   -27.202 -26.576 1.00 27.32 ? 529  LYS A CA  1 
ATOM   2789 C  C   . LYS A 1 529 ? 3.990   -27.269 -26.399 1.00 28.17 ? 529  LYS A C   1 
ATOM   2790 O  O   . LYS A 1 529 ? 3.490   -27.640 -25.337 1.00 28.20 ? 529  LYS A O   1 
ATOM   2791 C  CB  . LYS A 1 529 ? 6.125   -28.601 -26.565 1.00 28.83 ? 529  LYS A CB  1 
ATOM   2792 C  CG  . LYS A 1 529 ? 5.699   -29.507 -27.718 1.00 30.55 ? 529  LYS A CG  1 
ATOM   2793 C  CD  . LYS A 1 529 ? 6.380   -30.871 -27.607 1.00 31.05 ? 529  LYS A CD  1 
ATOM   2794 C  CE  . LYS A 1 529 ? 5.552   -31.991 -28.222 1.00 31.82 ? 529  LYS A CE  1 
ATOM   2795 N  NZ  . LYS A 1 529 ? 5.713   -32.042 -29.693 1.00 32.53 ? 529  LYS A NZ  1 
ATOM   2796 N  N   . LEU A 1 530 ? 3.254   -26.891 -27.434 1.00 27.45 ? 530  LEU A N   1 
ATOM   2797 C  CA  . LEU A 1 530 ? 1.791   -26.932 -27.410 1.00 27.04 ? 530  LEU A CA  1 
ATOM   2798 C  C   . LEU A 1 530 ? 1.341   -27.550 -28.717 1.00 27.99 ? 530  LEU A C   1 
ATOM   2799 O  O   . LEU A 1 530 ? 1.595   -26.982 -29.787 1.00 26.81 ? 530  LEU A O   1 
ATOM   2800 C  CB  . LEU A 1 530 ? 1.204   -25.533 -27.295 1.00 25.52 ? 530  LEU A CB  1 
ATOM   2801 C  CG  . LEU A 1 530 ? 1.577   -24.715 -26.065 1.00 25.89 ? 530  LEU A CG  1 
ATOM   2802 C  CD1 . LEU A 1 530 ? 1.026   -23.306 -26.215 1.00 25.10 ? 530  LEU A CD1 1 
ATOM   2803 C  CD2 . LEU A 1 530 ? 1.092   -25.363 -24.772 1.00 25.49 ? 530  LEU A CD2 1 
ATOM   2804 N  N   . GLY A 1 531 ? 0.665   -28.694 -28.625 1.00 29.08 ? 531  GLY A N   1 
ATOM   2805 C  CA  . GLY A 1 531 ? 0.416   -29.541 -29.788 1.00 29.13 ? 531  GLY A CA  1 
ATOM   2806 C  C   . GLY A 1 531 ? 1.742   -30.028 -30.348 1.00 29.84 ? 531  GLY A C   1 
ATOM   2807 O  O   . GLY A 1 531 ? 2.531   -30.672 -29.649 1.00 31.83 ? 531  GLY A O   1 
ATOM   2808 N  N   . ASN A 1 532 ? 1.997   -29.709 -31.606 1.00 29.84 ? 532  ASN A N   1 
ATOM   2809 C  CA  . ASN A 1 532 ? 3.255   -30.056 -32.243 1.00 32.35 ? 532  ASN A CA  1 
ATOM   2810 C  C   . ASN A 1 532 ? 4.001   -28.799 -32.685 1.00 30.77 ? 532  ASN A C   1 
ATOM   2811 O  O   . ASN A 1 532 ? 4.738   -28.816 -33.668 1.00 30.65 ? 532  ASN A O   1 
ATOM   2812 C  CB  . ASN A 1 532 ? 2.990   -30.957 -33.443 1.00 36.69 ? 532  ASN A CB  1 
ATOM   2813 C  CG  . ASN A 1 532 ? 2.089   -30.300 -34.458 1.00 41.24 ? 532  ASN A CG  1 
ATOM   2814 O  OD1 . ASN A 1 532 ? 1.318   -29.395 -34.118 1.00 47.51 ? 532  ASN A OD1 1 
ATOM   2815 N  ND2 . ASN A 1 532 ? 2.174   -30.742 -35.710 1.00 44.46 ? 532  ASN A ND2 1 
ATOM   2816 N  N   . LYS A 1 533 ? 3.796   -27.698 -31.972 1.00 29.33 ? 533  LYS A N   1 
ATOM   2817 C  CA  . LYS A 1 533 ? 4.561   -26.488 -32.224 1.00 28.64 ? 533  LYS A CA  1 
ATOM   2818 C  C   . LYS A 1 533 ? 5.391   -26.140 -30.999 1.00 26.06 ? 533  LYS A C   1 
ATOM   2819 O  O   . LYS A 1 533 ? 5.051   -26.514 -29.878 1.00 24.14 ? 533  LYS A O   1 
ATOM   2820 C  CB  . LYS A 1 533 ? 3.630   -25.356 -32.586 1.00 30.12 ? 533  LYS A CB  1 
ATOM   2821 C  CG  . LYS A 1 533 ? 3.023   -25.549 -33.954 1.00 33.05 ? 533  LYS A CG  1 
ATOM   2822 C  CD  . LYS A 1 533 ? 1.868   -24.604 -34.174 1.00 34.63 ? 533  LYS A CD  1 
ATOM   2823 C  CE  . LYS A 1 533 ? 1.434   -24.634 -35.625 1.00 37.77 ? 533  LYS A CE  1 
ATOM   2824 N  NZ  . LYS A 1 533 ? 0.345   -23.641 -35.832 1.00 40.32 ? 533  LYS A NZ  1 
ATOM   2825 N  N   . TYR A 1 534 ? 6.491   -25.438 -31.235 1.00 23.95 ? 534  TYR A N   1 
ATOM   2826 C  CA  . TYR A 1 534 ? 7.342   -24.970 -30.168 1.00 23.85 ? 534  TYR A CA  1 
ATOM   2827 C  C   . TYR A 1 534 ? 7.223   -23.451 -30.026 1.00 22.13 ? 534  TYR A C   1 
ATOM   2828 O  O   . TYR A 1 534 ? 7.570   -22.706 -30.939 1.00 20.34 ? 534  TYR A O   1 
ATOM   2829 C  CB  . TYR A 1 534 ? 8.785   -25.403 -30.437 1.00 25.35 ? 534  TYR A CB  1 
ATOM   2830 C  CG  . TYR A 1 534 ? 8.966   -26.888 -30.287 1.00 26.94 ? 534  TYR A CG  1 
ATOM   2831 C  CD1 . TYR A 1 534 ? 9.104   -27.456 -29.031 1.00 28.17 ? 534  TYR A CD1 1 
ATOM   2832 C  CD2 . TYR A 1 534 ? 8.937   -27.737 -31.394 1.00 29.06 ? 534  TYR A CD2 1 
ATOM   2833 C  CE1 . TYR A 1 534 ? 9.257   -28.824 -28.873 1.00 29.95 ? 534  TYR A CE1 1 
ATOM   2834 C  CE2 . TYR A 1 534 ? 9.076   -29.112 -31.246 1.00 29.79 ? 534  TYR A CE2 1 
ATOM   2835 C  CZ  . TYR A 1 534 ? 9.247   -29.643 -29.981 1.00 31.03 ? 534  TYR A CZ  1 
ATOM   2836 O  OH  . TYR A 1 534 ? 9.388   -31.001 -29.802 1.00 36.67 ? 534  TYR A OH  1 
ATOM   2837 N  N   . TYR A 1 535 ? 6.739   -23.006 -28.869 1.00 20.06 ? 535  TYR A N   1 
ATOM   2838 C  CA  . TYR A 1 535 ? 6.599   -21.578 -28.586 1.00 19.93 ? 535  TYR A CA  1 
ATOM   2839 C  C   . TYR A 1 535 ? 7.741   -21.062 -27.740 1.00 18.88 ? 535  TYR A C   1 
ATOM   2840 O  O   . TYR A 1 535 ? 7.968   -21.531 -26.622 1.00 19.22 ? 535  TYR A O   1 
ATOM   2841 C  CB  . TYR A 1 535 ? 5.256   -21.285 -27.910 1.00 19.56 ? 535  TYR A CB  1 
ATOM   2842 C  CG  . TYR A 1 535 ? 4.108   -21.531 -28.846 1.00 19.88 ? 535  TYR A CG  1 
ATOM   2843 C  CD1 . TYR A 1 535 ? 3.668   -22.814 -29.089 1.00 19.89 ? 535  TYR A CD1 1 
ATOM   2844 C  CD2 . TYR A 1 535 ? 3.479   -20.474 -29.511 1.00 20.59 ? 535  TYR A CD2 1 
ATOM   2845 C  CE1 . TYR A 1 535 ? 2.630   -23.053 -29.971 1.00 20.77 ? 535  TYR A CE1 1 
ATOM   2846 C  CE2 . TYR A 1 535 ? 2.433   -20.698 -30.386 1.00 20.28 ? 535  TYR A CE2 1 
ATOM   2847 C  CZ  . TYR A 1 535 ? 2.017   -22.002 -30.601 1.00 20.66 ? 535  TYR A CZ  1 
ATOM   2848 O  OH  . TYR A 1 535 ? 1.009   -22.287 -31.462 1.00 21.67 ? 535  TYR A OH  1 
ATOM   2849 N  N   . LEU A 1 536 ? 8.448   -20.079 -28.283 1.00 17.76 ? 536  LEU A N   1 
ATOM   2850 C  CA  . LEU A 1 536 ? 9.591   -19.486 -27.635 1.00 16.46 ? 536  LEU A CA  1 
ATOM   2851 C  C   . LEU A 1 536 ? 9.202   -18.108 -27.119 1.00 16.86 ? 536  LEU A C   1 
ATOM   2852 O  O   . LEU A 1 536 ? 8.899   -17.224 -27.925 1.00 16.02 ? 536  LEU A O   1 
ATOM   2853 C  CB  . LEU A 1 536 ? 10.728  -19.345 -28.649 1.00 16.39 ? 536  LEU A CB  1 
ATOM   2854 C  CG  . LEU A 1 536 ? 11.949  -18.524 -28.238 1.00 15.55 ? 536  LEU A CG  1 
ATOM   2855 C  CD1 . LEU A 1 536 ? 12.509  -19.055 -26.947 1.00 15.75 ? 536  LEU A CD1 1 
ATOM   2856 C  CD2 . LEU A 1 536 ? 12.994  -18.537 -29.337 1.00 15.73 ? 536  LEU A CD2 1 
ATOM   2857 N  N   . PHE A 1 537 ? 9.232   -17.941 -25.796 1.00 16.32 ? 537  PHE A N   1 
ATOM   2858 C  CA  . PHE A 1 537 ? 8.892   -16.688 -25.136 1.00 17.21 ? 537  PHE A CA  1 
ATOM   2859 C  C   . PHE A 1 537 ? 10.114  -16.125 -24.446 1.00 16.79 ? 537  PHE A C   1 
ATOM   2860 O  O   . PHE A 1 537 ? 11.048  -16.859 -24.123 1.00 16.94 ? 537  PHE A O   1 
ATOM   2861 C  CB  . PHE A 1 537 ? 7.800   -16.880 -24.067 1.00 17.95 ? 537  PHE A CB  1 
ATOM   2862 C  CG  . PHE A 1 537 ? 6.525   -17.451 -24.593 1.00 17.80 ? 537  PHE A CG  1 
ATOM   2863 C  CD1 . PHE A 1 537 ? 5.662   -16.668 -25.347 1.00 18.34 ? 537  PHE A CD1 1 
ATOM   2864 C  CD2 . PHE A 1 537 ? 6.187   -18.774 -24.346 1.00 18.47 ? 537  PHE A CD2 1 
ATOM   2865 C  CE1 . PHE A 1 537 ? 4.477   -17.199 -25.842 1.00 18.60 ? 537  PHE A CE1 1 
ATOM   2866 C  CE2 . PHE A 1 537 ? 5.002   -19.312 -24.831 1.00 18.18 ? 537  PHE A CE2 1 
ATOM   2867 C  CZ  . PHE A 1 537 ? 4.151   -18.525 -25.586 1.00 18.95 ? 537  PHE A CZ  1 
ATOM   2868 N  N   . ALA A 1 538 ? 10.088  -14.818 -24.198 1.00 16.48 ? 538  ALA A N   1 
ATOM   2869 C  CA  . ALA A 1 538 ? 11.176  -14.151 -23.464 1.00 16.31 ? 538  ALA A CA  1 
ATOM   2870 C  C   . ALA A 1 538 ? 10.726  -12.817 -22.861 1.00 16.41 ? 538  ALA A C   1 
ATOM   2871 O  O   . ALA A 1 538 ? 9.820   -12.158 -23.374 1.00 16.08 ? 538  ALA A O   1 
ATOM   2872 C  CB  . ALA A 1 538 ? 12.364  -13.933 -24.392 1.00 16.09 ? 538  ALA A CB  1 
ATOM   2873 N  N   . ALA A 1 539 ? 11.373  -12.419 -21.776 1.00 16.19 ? 539  ALA A N   1 
ATOM   2874 C  CA  . ALA A 1 539 ? 11.101  -11.128 -21.170 1.00 16.57 ? 539  ALA A CA  1 
ATOM   2875 C  C   . ALA A 1 539 ? 12.147  -10.141 -21.669 1.00 16.92 ? 539  ALA A C   1 
ATOM   2876 O  O   . ALA A 1 539 ? 13.284  -10.530 -21.960 1.00 16.55 ? 539  ALA A O   1 
ATOM   2877 C  CB  . ALA A 1 539 ? 11.167  -11.247 -19.663 1.00 16.60 ? 539  ALA A CB  1 
ATOM   2878 N  N   . THR A 1 540 ? 11.769  -8.869  -21.780 1.00 17.26 ? 540  THR A N   1 
ATOM   2879 C  CA  . THR A 1 540 ? 12.723  -7.851  -22.146 1.00 18.18 ? 540  THR A CA  1 
ATOM   2880 C  C   . THR A 1 540 ? 12.302  -6.508  -21.570 1.00 19.28 ? 540  THR A C   1 
ATOM   2881 O  O   . THR A 1 540 ? 11.120  -6.273  -21.302 1.00 19.79 ? 540  THR A O   1 
ATOM   2882 C  CB  . THR A 1 540 ? 12.951  -7.771  -23.687 1.00 17.99 ? 540  THR A CB  1 
ATOM   2883 O  OG1 . THR A 1 540 ? 14.096  -6.941  -23.973 1.00 18.31 ? 540  THR A OG1 1 
ATOM   2884 C  CG2 . THR A 1 540 ? 11.737  -7.225  -24.408 1.00 17.99 ? 540  THR A CG2 1 
ATOM   2885 N  N   . ARG A 1 541 ? 13.301  -5.671  -21.330 1.00 19.25 ? 541  ARG A N   1 
ATOM   2886 C  CA  . ARG A 1 541 ? 13.099  -4.296  -20.918 1.00 21.04 ? 541  ARG A CA  1 
ATOM   2887 C  C   . ARG A 1 541 ? 13.391  -3.459  -22.160 1.00 19.70 ? 541  ARG A C   1 
ATOM   2888 O  O   . ARG A 1 541 ? 14.504  -3.476  -22.665 1.00 19.43 ? 541  ARG A O   1 
ATOM   2889 C  CB  . ARG A 1 541 ? 14.030  -3.947  -19.747 1.00 22.22 ? 541  ARG A CB  1 
ATOM   2890 C  CG  . ARG A 1 541 ? 13.754  -4.764  -18.482 1.00 24.07 ? 541  ARG A CG  1 
ATOM   2891 C  CD  . ARG A 1 541 ? 14.340  -4.133  -17.226 1.00 27.15 ? 541  ARG A CD  1 
ATOM   2892 N  NE  . ARG A 1 541 ? 14.084  -4.889  -15.982 1.00 29.82 ? 541  ARG A NE  1 
ATOM   2893 C  CZ  . ARG A 1 541 ? 13.073  -4.687  -15.129 1.00 32.03 ? 541  ARG A CZ  1 
ATOM   2894 N  NH1 . ARG A 1 541 ? 12.152  -3.760  -15.345 1.00 33.82 ? 541  ARG A NH1 1 
ATOM   2895 N  NH2 . ARG A 1 541 ? 12.971  -5.435  -14.031 1.00 33.77 ? 541  ARG A NH2 1 
ATOM   2896 N  N   . LEU A 1 542 ? 12.385  -2.775  -22.685 1.00 19.14 ? 542  LEU A N   1 
ATOM   2897 C  CA  . LEU A 1 542 ? 12.562  -2.029  -23.936 1.00 18.95 ? 542  LEU A CA  1 
ATOM   2898 C  C   . LEU A 1 542 ? 13.610  -0.931  -23.790 1.00 18.03 ? 542  LEU A C   1 
ATOM   2899 O  O   . LEU A 1 542 ? 14.182  -0.475  -24.784 1.00 17.19 ? 542  LEU A O   1 
ATOM   2900 C  CB  . LEU A 1 542 ? 11.227  -1.462  -24.452 1.00 19.76 ? 542  LEU A CB  1 
ATOM   2901 C  CG  . LEU A 1 542 ? 10.144  -2.457  -24.871 1.00 20.76 ? 542  LEU A CG  1 
ATOM   2902 C  CD1 . LEU A 1 542 ? 8.908   -1.703  -25.309 1.00 21.33 ? 542  LEU A CD1 1 
ATOM   2903 C  CD2 . LEU A 1 542 ? 10.593  -3.438  -25.959 1.00 20.73 ? 542  LEU A CD2 1 
ATOM   2904 N  N   . ASN A 1 543 ? 13.895  -0.500  -22.563 1.00 17.49 ? 543  ASN A N   1 
ATOM   2905 C  CA  . ASN A 1 543 ? 14.941  0.503   -22.382 1.00 18.35 ? 543  ASN A CA  1 
ATOM   2906 C  C   . ASN A 1 543 ? 16.388  -0.046  -22.553 1.00 19.64 ? 543  ASN A C   1 
ATOM   2907 O  O   . ASN A 1 543 ? 17.354  0.711   -22.399 1.00 18.19 ? 543  ASN A O   1 
ATOM   2908 C  CB  . ASN A 1 543 ? 14.755  1.268   -21.068 1.00 18.59 ? 543  ASN A CB  1 
ATOM   2909 C  CG  . ASN A 1 543 ? 14.978  0.410   -19.828 1.00 18.55 ? 543  ASN A CG  1 
ATOM   2910 O  OD1 . ASN A 1 543 ? 15.323  -0.774  -19.904 1.00 17.96 ? 543  ASN A OD1 1 
ATOM   2911 N  ND2 . ASN A 1 543 ? 14.814  1.028   -18.674 1.00 17.90 ? 543  ASN A ND2 1 
ATOM   2912 N  N   . ARG A 1 544 ? 16.514  -1.341  -22.894 1.00 19.72 ? 544  ARG A N   1 
ATOM   2913 C  CA  . ARG A 1 544 ? 17.796  -1.934  -23.304 1.00 21.57 ? 544  ARG A CA  1 
ATOM   2914 C  C   . ARG A 1 544 ? 17.904  -1.959  -24.832 1.00 21.28 ? 544  ARG A C   1 
ATOM   2915 O  O   . ARG A 1 544 ? 18.849  -2.515  -25.393 1.00 20.68 ? 544  ARG A O   1 
ATOM   2916 C  CB  . ARG A 1 544 ? 17.944  -3.360  -22.758 1.00 22.61 ? 544  ARG A CB  1 
ATOM   2917 C  CG  . ARG A 1 544 ? 17.633  -3.535  -21.267 1.00 24.91 ? 544  ARG A CG  1 
ATOM   2918 C  CD  . ARG A 1 544 ? 18.518  -2.689  -20.371 1.00 27.18 ? 544  ARG A CD  1 
ATOM   2919 N  NE  . ARG A 1 544 ? 18.612  -3.223  -18.999 1.00 29.51 ? 544  ARG A NE  1 
ATOM   2920 C  CZ  . ARG A 1 544 ? 17.966  -2.770  -17.914 1.00 30.40 ? 544  ARG A CZ  1 
ATOM   2921 N  NH1 . ARG A 1 544 ? 17.104  -1.765  -17.968 1.00 29.62 ? 544  ARG A NH1 1 
ATOM   2922 N  NH2 . ARG A 1 544 ? 18.171  -3.358  -16.739 1.00 32.47 ? 544  ARG A NH2 1 
ATOM   2923 N  N   . GLY A 1 545 ? 16.924  -1.351  -25.493 1.00 20.01 ? 545  GLY A N   1 
ATOM   2924 C  CA  . GLY A 1 545 ? 16.900  -1.244  -26.937 1.00 18.95 ? 545  GLY A CA  1 
ATOM   2925 C  C   . GLY A 1 545 ? 17.487  0.068   -27.407 1.00 18.19 ? 545  GLY A C   1 
ATOM   2926 O  O   . GLY A 1 545 ? 17.680  1.007   -26.638 1.00 17.46 ? 545  GLY A O   1 
ATOM   2927 N  N   . SER A 1 546 ? 17.770  0.119   -28.696 1.00 17.31 ? 546  SER A N   1 
ATOM   2928 C  CA  . SER A 1 546 ? 18.481  1.230   -29.263 1.00 16.91 ? 546  SER A CA  1 
ATOM   2929 C  C   . SER A 1 546 ? 17.553  2.405   -29.557 1.00 16.22 ? 546  SER A C   1 
ATOM   2930 O  O   . SER A 1 546 ? 17.983  3.535   -29.536 1.00 15.65 ? 546  SER A O   1 
ATOM   2931 C  CB  . SER A 1 546 ? 19.215  0.789   -30.525 1.00 16.53 ? 546  SER A CB  1 
ATOM   2932 O  OG  . SER A 1 546 ? 18.320  0.302   -31.498 1.00 16.23 ? 546  SER A OG  1 
ATOM   2933 N  N   . ASN A 1 547 ? 16.277  2.139   -29.798 1.00 16.79 ? 547  ASN A N   1 
ATOM   2934 C  CA  . ASN A 1 547 ? 15.341  3.197   -30.179 1.00 17.26 ? 547  ASN A CA  1 
ATOM   2935 C  C   . ASN A 1 547 ? 14.885  3.998   -28.929 1.00 17.90 ? 547  ASN A C   1 
ATOM   2936 O  O   . ASN A 1 547 ? 13.844  3.701   -28.346 1.00 17.11 ? 547  ASN A O   1 
ATOM   2937 C  CB  . ASN A 1 547 ? 14.178  2.566   -30.947 1.00 17.24 ? 547  ASN A CB  1 
ATOM   2938 C  CG  . ASN A 1 547 ? 13.208  3.586   -31.531 1.00 17.49 ? 547  ASN A CG  1 
ATOM   2939 O  OD1 . ASN A 1 547 ? 13.114  4.717   -31.074 1.00 17.79 ? 547  ASN A OD1 1 
ATOM   2940 N  ND2 . ASN A 1 547 ? 12.460  3.165   -32.547 1.00 18.07 ? 547  ASN A ND2 1 
ATOM   2941 N  N   . ASP A 1 548 ? 15.672  5.001   -28.527 1.00 17.64 ? 548  ASP A N   1 
ATOM   2942 C  CA  . ASP A 1 548 ? 15.364  5.784   -27.309 1.00 18.51 ? 548  ASP A CA  1 
ATOM   2943 C  C   . ASP A 1 548 ? 13.968  6.414   -27.342 1.00 18.57 ? 548  ASP A C   1 
ATOM   2944 O  O   . ASP A 1 548 ? 13.258  6.377   -26.346 1.00 19.13 ? 548  ASP A O   1 
ATOM   2945 C  CB  . ASP A 1 548 ? 16.421  6.875   -27.042 1.00 18.76 ? 548  ASP A CB  1 
ATOM   2946 C  CG  . ASP A 1 548 ? 17.732  6.309   -26.490 1.00 19.29 ? 548  ASP A CG  1 
ATOM   2947 O  OD1 . ASP A 1 548 ? 17.843  5.065   -26.283 1.00 17.58 ? 548  ASP A OD1 1 
ATOM   2948 O  OD2 . ASP A 1 548 ? 18.647  7.129   -26.241 1.00 19.27 ? 548  ASP A OD2 1 
ATOM   2949 N  N   . ASP A 1 549 ? 13.574  6.963   -28.484 1.00 19.10 ? 549  ASP A N   1 
ATOM   2950 C  CA  . ASP A 1 549 ? 12.248  7.570   -28.628 1.00 19.84 ? 549  ASP A CA  1 
ATOM   2951 C  C   . ASP A 1 549 ? 11.155  6.568   -28.268 1.00 19.87 ? 549  ASP A C   1 
ATOM   2952 O  O   . ASP A 1 549 ? 10.274  6.871   -27.492 1.00 19.26 ? 549  ASP A O   1 
ATOM   2953 C  CB  . ASP A 1 549 ? 11.986  8.049   -30.053 1.00 20.14 ? 549  ASP A CB  1 
ATOM   2954 C  CG  . ASP A 1 549 ? 12.994  9.084   -30.534 1.00 21.23 ? 549  ASP A CG  1 
ATOM   2955 O  OD1 . ASP A 1 549 ? 13.426  9.954   -29.753 1.00 21.20 ? 549  ASP A OD1 1 
ATOM   2956 O  OD2 . ASP A 1 549 ? 13.339  9.021   -31.724 1.00 21.59 ? 549  ASP A OD2 1 
ATOM   2957 N  N   . ALA A 1 550 ? 11.214  5.380   -28.864 1.00 19.87 ? 550  ALA A N   1 
ATOM   2958 C  CA  . ALA A 1 550 ? 10.207  4.354   -28.617 1.00 19.73 ? 550  ALA A CA  1 
ATOM   2959 C  C   . ALA A 1 550 ? 10.064  4.010   -27.136 1.00 19.37 ? 550  ALA A C   1 
ATOM   2960 O  O   . ALA A 1 550 ? 8.954   4.025   -26.602 1.00 19.69 ? 550  ALA A O   1 
ATOM   2961 C  CB  . ALA A 1 550 ? 10.501  3.107   -29.445 1.00 19.97 ? 550  ALA A CB  1 
ATOM   2962 N  N   . TRP A 1 551 ? 11.166  3.728   -26.447 1.00 19.82 ? 551  TRP A N   1 
ATOM   2963 C  CA  . TRP A 1 551 ? 11.055  3.333   -25.041 1.00 19.04 ? 551  TRP A CA  1 
ATOM   2964 C  C   . TRP A 1 551 ? 10.840  4.476   -24.065 1.00 19.92 ? 551  TRP A C   1 
ATOM   2965 O  O   . TRP A 1 551 ? 10.260  4.270   -22.998 1.00 19.21 ? 551  TRP A O   1 
ATOM   2966 C  CB  . TRP A 1 551 ? 12.210  2.403   -24.592 1.00 19.86 ? 551  TRP A CB  1 
ATOM   2967 C  CG  . TRP A 1 551 ? 13.645  2.926   -24.570 1.00 19.17 ? 551  TRP A CG  1 
ATOM   2968 C  CD1 . TRP A 1 551 ? 14.639  2.635   -25.475 1.00 19.02 ? 551  TRP A CD1 1 
ATOM   2969 C  CD2 . TRP A 1 551 ? 14.257  3.710   -23.552 1.00 18.73 ? 551  TRP A CD2 1 
ATOM   2970 N  NE1 . TRP A 1 551 ? 15.807  3.232   -25.100 1.00 18.27 ? 551  TRP A NE1 1 
ATOM   2971 C  CE2 . TRP A 1 551 ? 15.605  3.894   -23.920 1.00 18.53 ? 551  TRP A CE2 1 
ATOM   2972 C  CE3 . TRP A 1 551 ? 13.797  4.284   -22.360 1.00 19.41 ? 551  TRP A CE3 1 
ATOM   2973 C  CZ2 . TRP A 1 551 ? 16.496  4.640   -23.150 1.00 18.65 ? 551  TRP A CZ2 1 
ATOM   2974 C  CZ3 . TRP A 1 551 ? 14.685  5.025   -21.593 1.00 19.61 ? 551  TRP A CZ3 1 
ATOM   2975 C  CH2 . TRP A 1 551 ? 16.020  5.198   -21.993 1.00 19.00 ? 551  TRP A CH2 1 
ATOM   2976 N  N   . MET A 1 552 ? 11.298  5.679   -24.417 1.00 20.08 ? 552  MET A N   1 
ATOM   2977 C  CA  . MET A 1 552 ? 11.035  6.855   -23.587 1.00 20.09 ? 552  MET A CA  1 
ATOM   2978 C  C   . MET A 1 552 ? 9.558   7.222   -23.723 1.00 18.76 ? 552  MET A C   1 
ATOM   2979 O  O   . MET A 1 552 ? 8.935   7.646   -22.748 1.00 17.71 ? 552  MET A O   1 
ATOM   2980 C  CB  . MET A 1 552 ? 11.961  8.039   -23.950 1.00 20.45 ? 552  MET A CB  1 
ATOM   2981 C  CG  . MET A 1 552 ? 13.422  7.772   -23.613 1.00 21.27 ? 552  MET A CG  1 
ATOM   2982 S  SD  . MET A 1 552 ? 14.519  9.160   -23.991 1.00 23.11 ? 552  MET A SD  1 
ATOM   2983 C  CE  . MET A 1 552 ? 14.059  10.249  -22.646 1.00 24.72 ? 552  MET A CE  1 
ATOM   2984 N  N   . ASN A 1 553 ? 8.999   7.022   -24.919 1.00 18.33 ? 553  ASN A N   1 
ATOM   2985 C  CA  . ASN A 1 553 ? 7.553   7.130   -25.116 1.00 18.90 ? 553  ASN A CA  1 
ATOM   2986 C  C   . ASN A 1 553 ? 6.752   6.060   -24.357 1.00 18.57 ? 553  ASN A C   1 
ATOM   2987 O  O   . ASN A 1 553 ? 5.664   6.338   -23.857 1.00 18.37 ? 553  ASN A O   1 
ATOM   2988 C  CB  . ASN A 1 553 ? 7.202   7.137   -26.616 1.00 19.59 ? 553  ASN A CB  1 
ATOM   2989 C  CG  . ASN A 1 553 ? 7.490   8.476   -27.265 1.00 19.67 ? 553  ASN A CG  1 
ATOM   2990 O  OD1 . ASN A 1 553 ? 7.464   9.508   -26.596 1.00 19.44 ? 553  ASN A OD1 1 
ATOM   2991 N  ND2 . ASN A 1 553 ? 7.793   8.465   -28.558 1.00 18.81 ? 553  ASN A ND2 1 
ATOM   2992 N  N   . ALA A 1 554 ? 7.289   4.848   -24.253 1.00 19.03 ? 554  ALA A N   1 
ATOM   2993 C  CA  . ALA A 1 554 ? 6.671   3.818   -23.408 1.00 19.23 ? 554  ALA A CA  1 
ATOM   2994 C  C   . ALA A 1 554 ? 6.608   4.291   -21.962 1.00 19.90 ? 554  ALA A C   1 
ATOM   2995 O  O   . ALA A 1 554 ? 5.570   4.180   -21.320 1.00 20.29 ? 554  ALA A O   1 
ATOM   2996 C  CB  . ALA A 1 554 ? 7.440   2.507   -23.487 1.00 19.41 ? 554  ALA A CB  1 
ATOM   2997 N  N   . ASN A 1 555 ? 7.722   4.815   -21.457 1.00 19.87 ? 555  ASN A N   1 
ATOM   2998 C  CA  . ASN A 1 555 ? 7.782   5.297   -20.080 1.00 21.35 ? 555  ASN A CA  1 
ATOM   2999 C  C   . ASN A 1 555 ? 6.760   6.424   -19.817 1.00 22.52 ? 555  ASN A C   1 
ATOM   3000 O  O   . ASN A 1 555 ? 5.983   6.367   -18.864 1.00 22.97 ? 555  ASN A O   1 
ATOM   3001 C  CB  . ASN A 1 555 ? 9.203   5.754   -19.736 1.00 20.81 ? 555  ASN A CB  1 
ATOM   3002 C  CG  . ASN A 1 555 ? 10.168  4.587   -19.525 1.00 20.07 ? 555  ASN A CG  1 
ATOM   3003 O  OD1 . ASN A 1 555 ? 9.756   3.443   -19.331 1.00 19.03 ? 555  ASN A OD1 1 
ATOM   3004 N  ND2 . ASN A 1 555 ? 11.461  4.885   -19.536 1.00 19.40 ? 555  ASN A ND2 1 
ATOM   3005 N  N   . TYR A 1 556 ? 6.752   7.419   -20.691 1.00 23.90 ? 556  TYR A N   1 
ATOM   3006 C  CA  . TYR A 1 556 ? 5.827   8.537   -20.611 1.00 24.81 ? 556  TYR A CA  1 
ATOM   3007 C  C   . TYR A 1 556 ? 4.352   8.075   -20.609 1.00 23.26 ? 556  TYR A C   1 
ATOM   3008 O  O   . TYR A 1 556 ? 3.558   8.531   -19.800 1.00 20.23 ? 556  TYR A O   1 
ATOM   3009 C  CB  . TYR A 1 556 ? 6.096   9.463   -21.795 1.00 28.15 ? 556  TYR A CB  1 
ATOM   3010 C  CG  . TYR A 1 556 ? 5.358   10.763  -21.757 1.00 31.93 ? 556  TYR A CG  1 
ATOM   3011 C  CD1 . TYR A 1 556 ? 5.741   11.760  -20.874 1.00 35.29 ? 556  TYR A CD1 1 
ATOM   3012 C  CD2 . TYR A 1 556 ? 4.293   11.010  -22.619 1.00 35.22 ? 556  TYR A CD2 1 
ATOM   3013 C  CE1 . TYR A 1 556 ? 5.076   12.964  -20.830 1.00 38.43 ? 556  TYR A CE1 1 
ATOM   3014 C  CE2 . TYR A 1 556 ? 3.615   12.216  -22.587 1.00 37.75 ? 556  TYR A CE2 1 
ATOM   3015 C  CZ  . TYR A 1 556 ? 4.014   13.190  -21.688 1.00 40.10 ? 556  TYR A CZ  1 
ATOM   3016 O  OH  . TYR A 1 556 ? 3.368   14.403  -21.635 1.00 47.31 ? 556  TYR A OH  1 
ATOM   3017 N  N   . ALA A 1 557 ? 3.995   7.168   -21.518 1.00 21.97 ? 557  ALA A N   1 
ATOM   3018 C  CA  . ALA A 1 557 ? 2.630   6.649   -21.577 1.00 21.85 ? 557  ALA A CA  1 
ATOM   3019 C  C   . ALA A 1 557 ? 2.227   5.780   -20.348 1.00 21.04 ? 557  ALA A C   1 
ATOM   3020 O  O   . ALA A 1 557 ? 1.160   5.990   -19.781 1.00 20.99 ? 557  ALA A O   1 
ATOM   3021 C  CB  . ALA A 1 557 ? 2.410   5.875   -22.876 1.00 22.35 ? 557  ALA A CB  1 
ATOM   3022 N  N   . VAL A 1 558 ? 3.070   4.829   -19.941 1.00 20.45 ? 558  VAL A N   1 
ATOM   3023 C  CA  . VAL A 1 558 ? 2.690   3.807   -18.911 1.00 20.04 ? 558  VAL A CA  1 
ATOM   3024 C  C   . VAL A 1 558 ? 3.457   3.894   -17.578 1.00 19.15 ? 558  VAL A C   1 
ATOM   3025 O  O   . VAL A 1 558 ? 2.975   3.419   -16.537 1.00 19.61 ? 558  VAL A O   1 
ATOM   3026 C  CB  . VAL A 1 558 ? 2.851   2.373   -19.487 1.00 19.82 ? 558  VAL A CB  1 
ATOM   3027 C  CG1 . VAL A 1 558 ? 2.661   1.295   -18.429 1.00 19.65 ? 558  VAL A CG1 1 
ATOM   3028 C  CG2 . VAL A 1 558 ? 1.880   2.142   -20.637 1.00 20.40 ? 558  VAL A CG2 1 
ATOM   3029 N  N   . GLY A 1 559 ? 4.651   4.471   -17.594 1.00 17.89 ? 559  GLY A N   1 
ATOM   3030 C  CA  . GLY A 1 559 ? 5.515   4.427   -16.420 1.00 17.72 ? 559  GLY A CA  1 
ATOM   3031 C  C   . GLY A 1 559 ? 6.403   3.192   -16.377 1.00 17.47 ? 559  GLY A C   1 
ATOM   3032 O  O   . GLY A 1 559 ? 7.129   2.991   -15.414 1.00 16.77 ? 559  GLY A O   1 
ATOM   3033 N  N   . ASP A 1 560 ? 6.360   2.365   -17.423 1.00 17.83 ? 560  ASP A N   1 
ATOM   3034 C  CA  . ASP A 1 560 ? 7.275   1.218   -17.526 1.00 18.68 ? 560  ASP A CA  1 
ATOM   3035 C  C   . ASP A 1 560 ? 7.427   0.794   -18.974 1.00 17.69 ? 560  ASP A C   1 
ATOM   3036 O  O   . ASP A 1 560 ? 6.732   1.280   -19.870 1.00 19.00 ? 560  ASP A O   1 
ATOM   3037 C  CB  . ASP A 1 560 ? 6.798   0.035   -16.661 1.00 19.42 ? 560  ASP A CB  1 
ATOM   3038 C  CG  . ASP A 1 560 ? 7.938   -0.917  -16.248 1.00 20.69 ? 560  ASP A CG  1 
ATOM   3039 O  OD1 . ASP A 1 560 ? 9.070   -0.785  -16.751 1.00 20.69 ? 560  ASP A OD1 1 
ATOM   3040 O  OD2 . ASP A 1 560 ? 7.687   -1.825  -15.421 1.00 22.25 ? 560  ASP A OD2 1 
ATOM   3041 N  N   . ASN A 1 561 ? 8.368   -0.098  -19.211 1.00 17.85 ? 561  ASN A N   1 
ATOM   3042 C  CA  . ASN A 1 561 ? 8.727   -0.462  -20.564 1.00 17.68 ? 561  ASN A CA  1 
ATOM   3043 C  C   . ASN A 1 561 ? 8.977   -1.935  -20.741 1.00 17.63 ? 561  ASN A C   1 
ATOM   3044 O  O   . ASN A 1 561 ? 9.550   -2.345  -21.757 1.00 17.89 ? 561  ASN A O   1 
ATOM   3045 C  CB  . ASN A 1 561 ? 9.963   0.338   -20.990 1.00 17.38 ? 561  ASN A CB  1 
ATOM   3046 C  CG  . ASN A 1 561 ? 11.137  0.147   -20.052 1.00 17.30 ? 561  ASN A CG  1 
ATOM   3047 O  OD1 . ASN A 1 561 ? 11.879  -0.842  -20.144 1.00 16.95 ? 561  ASN A OD1 1 
ATOM   3048 N  ND2 . ASN A 1 561 ? 11.327  1.107   -19.155 1.00 17.18 ? 561  ASN A ND2 1 
ATOM   3049 N  N   . VAL A 1 562 ? 8.532   -2.743  -19.779 1.00 17.03 ? 562  VAL A N   1 
ATOM   3050 C  CA  . VAL A 1 562 ? 8.742   -4.189  -19.888 1.00 16.42 ? 562  VAL A CA  1 
ATOM   3051 C  C   . VAL A 1 562 ? 7.730   -4.860  -20.807 1.00 15.40 ? 562  VAL A C   1 
ATOM   3052 O  O   . VAL A 1 562 ? 6.638   -4.353  -21.041 1.00 14.45 ? 562  VAL A O   1 
ATOM   3053 C  CB  . VAL A 1 562 ? 8.717   -4.918  -18.537 1.00 16.55 ? 562  VAL A CB  1 
ATOM   3054 C  CG1 . VAL A 1 562 ? 9.808   -4.364  -17.644 1.00 17.25 ? 562  VAL A CG1 1 
ATOM   3055 C  CG2 . VAL A 1 562 ? 7.347   -4.852  -17.875 1.00 16.37 ? 562  VAL A CG2 1 
ATOM   3056 N  N   . ALA A 1 563 ? 8.140   -5.999  -21.332 1.00 14.71 ? 563  ALA A N   1 
ATOM   3057 C  CA  . ALA A 1 563 ? 7.320   -6.783  -22.219 1.00 15.16 ? 563  ALA A CA  1 
ATOM   3058 C  C   . ALA A 1 563 ? 7.734   -8.255  -22.168 1.00 14.86 ? 563  ALA A C   1 
ATOM   3059 O  O   . ALA A 1 563 ? 8.809   -8.586  -21.694 1.00 14.62 ? 563  ALA A O   1 
ATOM   3060 C  CB  . ALA A 1 563 ? 7.446   -6.259  -23.638 1.00 15.18 ? 563  ALA A CB  1 
ATOM   3061 N  N   . MET A 1 564 ? 6.835   -9.117  -22.632 1.00 15.35 ? 564  MET A N   1 
ATOM   3062 C  CA  . MET A 1 564 ? 7.166   -10.466 -23.025 1.00 15.68 ? 564  MET A CA  1 
ATOM   3063 C  C   . MET A 1 564 ? 6.966   -10.566 -24.536 1.00 15.13 ? 564  MET A C   1 
ATOM   3064 O  O   . MET A 1 564 ? 5.996   -10.074 -25.074 1.00 15.22 ? 564  MET A O   1 
ATOM   3065 C  CB  . MET A 1 564 ? 6.284   -11.485 -22.312 1.00 16.03 ? 564  MET A CB  1 
ATOM   3066 C  CG  . MET A 1 564 ? 6.815   -12.895 -22.425 1.00 16.90 ? 564  MET A CG  1 
ATOM   3067 S  SD  . MET A 1 564 ? 5.877   -14.184 -21.577 1.00 17.79 ? 564  MET A SD  1 
ATOM   3068 C  CE  . MET A 1 564 ? 4.497   -14.398 -22.672 1.00 18.10 ? 564  MET A CE  1 
ATOM   3069 N  N   . VAL A 1 565 ? 7.906   -11.192 -25.212 1.00 15.31 ? 565  VAL A N   1 
ATOM   3070 C  CA  . VAL A 1 565 ? 7.813   -11.404 -26.629 1.00 15.43 ? 565  VAL A CA  1 
ATOM   3071 C  C   . VAL A 1 565 ? 7.671   -12.897 -26.866 1.00 15.85 ? 565  VAL A C   1 
ATOM   3072 O  O   . VAL A 1 565 ? 7.920   -13.705 -25.969 1.00 15.40 ? 565  VAL A O   1 
ATOM   3073 C  CB  . VAL A 1 565 ? 9.032   -10.822 -27.374 1.00 16.02 ? 565  VAL A CB  1 
ATOM   3074 C  CG1 . VAL A 1 565 ? 9.058   -9.306  -27.220 1.00 15.87 ? 565  VAL A CG1 1 
ATOM   3075 C  CG2 . VAL A 1 565 ? 10.352  -11.426 -26.877 1.00 16.20 ? 565  VAL A CG2 1 
ATOM   3076 N  N   . GLY A 1 566 ? 7.254   -13.264 -28.069 1.00 15.61 ? 566  GLY A N   1 
ATOM   3077 C  CA  . GLY A 1 566 ? 7.054   -14.661 -28.376 1.00 15.95 ? 566  GLY A CA  1 
ATOM   3078 C  C   . GLY A 1 566 ? 7.188   -14.938 -29.856 1.00 16.31 ? 566  GLY A C   1 
ATOM   3079 O  O   . GLY A 1 566 ? 6.908   -14.063 -30.689 1.00 15.10 ? 566  GLY A O   1 
ATOM   3080 N  N   . TYR A 1 567 ? 7.599   -16.176 -30.140 1.00 16.79 ? 567  TYR A N   1 
ATOM   3081 C  CA  . TYR A 1 567 ? 7.863   -16.697 -31.480 1.00 17.17 ? 567  TYR A CA  1 
ATOM   3082 C  C   . TYR A 1 567 ? 7.397   -18.146 -31.506 1.00 18.04 ? 567  TYR A C   1 
ATOM   3083 O  O   . TYR A 1 567 ? 7.118   -18.734 -30.451 1.00 17.29 ? 567  TYR A O   1 
ATOM   3084 C  CB  . TYR A 1 567 ? 9.366   -16.622 -31.827 1.00 16.98 ? 567  TYR A CB  1 
ATOM   3085 C  CG  . TYR A 1 567 ? 9.910   -15.234 -31.614 1.00 16.95 ? 567  TYR A CG  1 
ATOM   3086 C  CD1 . TYR A 1 567 ? 10.242  -14.799 -30.341 1.00 17.18 ? 567  TYR A CD1 1 
ATOM   3087 C  CD2 . TYR A 1 567 ? 10.028  -14.341 -32.669 1.00 17.34 ? 567  TYR A CD2 1 
ATOM   3088 C  CE1 . TYR A 1 567 ? 10.710  -13.521 -30.129 1.00 17.75 ? 567  TYR A CE1 1 
ATOM   3089 C  CE2 . TYR A 1 567 ? 10.478  -13.043 -32.464 1.00 17.80 ? 567  TYR A CE2 1 
ATOM   3090 C  CZ  . TYR A 1 567 ? 10.818  -12.641 -31.185 1.00 17.87 ? 567  TYR A CZ  1 
ATOM   3091 O  OH  . TYR A 1 567 ? 11.274  -11.353 -30.954 1.00 19.56 ? 567  TYR A OH  1 
ATOM   3092 N  N   . VAL A 1 568 ? 7.300   -18.721 -32.701 1.00 18.29 ? 568  VAL A N   1 
ATOM   3093 C  CA  . VAL A 1 568 ? 6.811   -20.083 -32.814 1.00 20.06 ? 568  VAL A CA  1 
ATOM   3094 C  C   . VAL A 1 568 ? 7.492   -20.801 -33.960 1.00 20.34 ? 568  VAL A C   1 
ATOM   3095 O  O   . VAL A 1 568 ? 7.775   -20.202 -34.988 1.00 19.41 ? 568  VAL A O   1 
ATOM   3096 C  CB  . VAL A 1 568 ? 5.271   -20.134 -32.965 1.00 20.87 ? 568  VAL A CB  1 
ATOM   3097 C  CG1 . VAL A 1 568 ? 4.825   -19.462 -34.260 1.00 21.69 ? 568  VAL A CG1 1 
ATOM   3098 C  CG2 . VAL A 1 568 ? 4.784   -21.573 -32.901 1.00 21.98 ? 568  VAL A CG2 1 
ATOM   3099 N  N   . ALA A 1 569 ? 7.799   -22.071 -33.738 1.00 20.58 ? 569  ALA A N   1 
ATOM   3100 C  CA  . ALA A 1 569 ? 8.450   -22.900 -34.739 1.00 22.84 ? 569  ALA A CA  1 
ATOM   3101 C  C   . ALA A 1 569 ? 7.787   -24.261 -34.779 1.00 23.74 ? 569  ALA A C   1 
ATOM   3102 O  O   . ALA A 1 569 ? 7.142   -24.673 -33.829 1.00 21.63 ? 569  ALA A O   1 
ATOM   3103 C  CB  . ALA A 1 569 ? 9.936   -23.048 -34.436 1.00 21.64 ? 569  ALA A CB  1 
ATOM   3104 N  N   . ASP A 1 570 ? 7.968   -24.947 -35.896 1.00 27.06 ? 570  ASP A N   1 
ATOM   3105 C  CA  . ASP A 1 570 ? 7.461   -26.309 -36.067 1.00 30.29 ? 570  ASP A CA  1 
ATOM   3106 C  C   . ASP A 1 570 ? 8.443   -27.357 -35.560 1.00 31.07 ? 570  ASP A C   1 
ATOM   3107 O  O   . ASP A 1 570 ? 8.102   -28.526 -35.444 1.00 31.26 ? 570  ASP A O   1 
ATOM   3108 C  CB  . ASP A 1 570 ? 7.142   -26.533 -37.531 1.00 31.49 ? 570  ASP A CB  1 
ATOM   3109 C  CG  . ASP A 1 570 ? 6.084   -25.597 -38.004 1.00 32.36 ? 570  ASP A CG  1 
ATOM   3110 O  OD1 . ASP A 1 570 ? 4.925   -25.769 -37.586 1.00 34.85 ? 570  ASP A OD1 1 
ATOM   3111 O  OD2 . ASP A 1 570 ? 6.416   -24.648 -38.733 1.00 36.82 ? 570  ASP A OD2 1 
ATOM   3112 N  N   . SER A 1 571 ? 9.663   -26.936 -35.250 1.00 30.08 ? 571  SER A N   1 
ATOM   3113 C  CA  . SER A 1 571 ? 10.617  -27.826 -34.625 1.00 30.31 ? 571  SER A CA  1 
ATOM   3114 C  C   . SER A 1 571 ? 11.492  -27.006 -33.703 1.00 30.52 ? 571  SER A C   1 
ATOM   3115 O  O   . SER A 1 571 ? 11.553  -25.777 -33.802 1.00 28.67 ? 571  SER A O   1 
ATOM   3116 C  CB  . SER A 1 571 ? 11.458  -28.554 -35.668 1.00 30.21 ? 571  SER A CB  1 
ATOM   3117 O  OG  . SER A 1 571 ? 12.503  -27.729 -36.132 1.00 33.06 ? 571  SER A OG  1 
ATOM   3118 N  N   . LEU A 1 572 ? 12.188  -27.699 -32.820 1.00 30.11 ? 572  LEU A N   1 
ATOM   3119 C  CA  . LEU A 1 572 ? 12.894  -27.057 -31.736 1.00 30.69 ? 572  LEU A CA  1 
ATOM   3120 C  C   . LEU A 1 572 ? 14.028  -26.161 -32.240 1.00 30.11 ? 572  LEU A C   1 
ATOM   3121 O  O   . LEU A 1 572 ? 14.179  -25.037 -31.763 1.00 28.52 ? 572  LEU A O   1 
ATOM   3122 C  CB  . LEU A 1 572 ? 13.402  -28.122 -30.770 1.00 31.36 ? 572  LEU A CB  1 
ATOM   3123 C  CG  . LEU A 1 572 ? 13.720  -27.761 -29.328 1.00 32.45 ? 572  LEU A CG  1 
ATOM   3124 C  CD1 . LEU A 1 572 ? 12.713  -26.807 -28.709 1.00 33.39 ? 572  LEU A CD1 1 
ATOM   3125 C  CD2 . LEU A 1 572 ? 13.759  -29.053 -28.539 1.00 32.59 ? 572  LEU A CD2 1 
ATOM   3126 N  N   . THR A 1 573 ? 14.805  -26.641 -33.211 1.00 30.27 ? 573  THR A N   1 
ATOM   3127 C  CA  . THR A 1 573 ? 15.850  -25.830 -33.836 1.00 29.92 ? 573  THR A CA  1 
ATOM   3128 C  C   . THR A 1 573 ? 15.400  -25.233 -35.177 1.00 29.67 ? 573  THR A C   1 
ATOM   3129 O  O   . THR A 1 573 ? 16.234  -24.803 -35.973 1.00 28.98 ? 573  THR A O   1 
ATOM   3130 C  CB  . THR A 1 573 ? 17.139  -26.642 -34.103 1.00 31.02 ? 573  THR A CB  1 
ATOM   3131 O  OG1 . THR A 1 573 ? 16.897  -27.575 -35.155 1.00 29.52 ? 573  THR A OG1 1 
ATOM   3132 C  CG2 . THR A 1 573 ? 17.618  -27.384 -32.844 1.00 31.53 ? 573  THR A CG2 1 
ATOM   3133 N  N   . GLY A 1 574 ? 14.096  -25.205 -35.438 1.00 29.06 ? 574  GLY A N   1 
ATOM   3134 C  CA  . GLY A 1 574 ? 13.589  -24.729 -36.731 1.00 26.50 ? 574  GLY A CA  1 
ATOM   3135 C  C   . GLY A 1 574 ? 13.584  -23.220 -36.748 1.00 25.47 ? 574  GLY A C   1 
ATOM   3136 O  O   . GLY A 1 574 ? 14.072  -22.574 -35.815 1.00 23.93 ? 574  GLY A O   1 
ATOM   3137 N  N   . SER A 1 575 ? 13.016  -22.657 -37.805 1.00 24.09 ? 575  SER A N   1 
ATOM   3138 C  CA  . SER A 1 575 ? 12.878  -21.221 -37.936 1.00 23.67 ? 575  SER A CA  1 
ATOM   3139 C  C   . SER A 1 575 ? 11.721  -20.718 -37.071 1.00 23.15 ? 575  SER A C   1 
ATOM   3140 O  O   . SER A 1 575 ? 10.593  -21.169 -37.212 1.00 23.92 ? 575  SER A O   1 
ATOM   3141 C  CB  . SER A 1 575 ? 12.638  -20.866 -39.405 1.00 23.53 ? 575  SER A CB  1 
ATOM   3142 O  OG  . SER A 1 575 ? 12.671  -19.467 -39.561 1.00 24.46 ? 575  SER A OG  1 
ATOM   3143 N  N   . TYR A 1 576 ? 12.010  -19.795 -36.163 1.00 22.92 ? 576  TYR A N   1 
ATOM   3144 C  CA  . TYR A 1 576 ? 10.997  -19.215 -35.293 1.00 22.38 ? 576  TYR A CA  1 
ATOM   3145 C  C   . TYR A 1 576 ? 10.400  -17.947 -35.921 1.00 22.85 ? 576  TYR A C   1 
ATOM   3146 O  O   . TYR A 1 576 ? 11.123  -17.093 -36.429 1.00 23.25 ? 576  TYR A O   1 
ATOM   3147 C  CB  . TYR A 1 576 ? 11.589  -18.925 -33.910 1.00 22.65 ? 576  TYR A CB  1 
ATOM   3148 C  CG  . TYR A 1 576 ? 11.729  -20.161 -33.068 1.00 22.63 ? 576  TYR A CG  1 
ATOM   3149 C  CD1 . TYR A 1 576 ? 12.818  -21.013 -33.234 1.00 22.48 ? 576  TYR A CD1 1 
ATOM   3150 C  CD2 . TYR A 1 576 ? 10.762  -20.501 -32.126 1.00 22.24 ? 576  TYR A CD2 1 
ATOM   3151 C  CE1 . TYR A 1 576 ? 12.944  -22.164 -32.484 1.00 22.61 ? 576  TYR A CE1 1 
ATOM   3152 C  CE2 . TYR A 1 576 ? 10.891  -21.645 -31.354 1.00 22.58 ? 576  TYR A CE2 1 
ATOM   3153 C  CZ  . TYR A 1 576 ? 11.981  -22.476 -31.542 1.00 22.82 ? 576  TYR A CZ  1 
ATOM   3154 O  OH  . TYR A 1 576 ? 12.107  -23.620 -30.788 1.00 23.48 ? 576  TYR A OH  1 
ATOM   3155 N  N   . LYS A 1 577 ? 9.074   -17.854 -35.912 1.00 23.01 ? 577  LYS A N   1 
ATOM   3156 C  CA  . LYS A 1 577 ? 8.362   -16.710 -36.483 1.00 23.39 ? 577  LYS A CA  1 
ATOM   3157 C  C   . LYS A 1 577 ? 7.603   -15.950 -35.409 1.00 20.61 ? 577  LYS A C   1 
ATOM   3158 O  O   . LYS A 1 577 ? 6.980   -16.554 -34.542 1.00 19.20 ? 577  LYS A O   1 
ATOM   3159 C  CB  . LYS A 1 577 ? 7.398   -17.195 -37.570 1.00 25.83 ? 577  LYS A CB  1 
ATOM   3160 C  CG  . LYS A 1 577 ? 8.062   -18.111 -38.599 1.00 28.44 ? 577  LYS A CG  1 
ATOM   3161 C  CD  . LYS A 1 577 ? 9.219   -17.421 -39.303 1.00 31.32 ? 577  LYS A CD  1 
ATOM   3162 C  CE  . LYS A 1 577 ? 10.061  -18.395 -40.106 1.00 35.46 ? 577  LYS A CE  1 
ATOM   3163 N  NZ  . LYS A 1 577 ? 9.427   -18.795 -41.394 1.00 39.16 ? 577  LYS A NZ  1 
ATOM   3164 N  N   . PRO A 1 578 ? 7.640   -14.618 -35.471 1.00 19.42 ? 578  PRO A N   1 
ATOM   3165 C  CA  . PRO A 1 578 ? 7.079   -13.822 -34.371 1.00 19.11 ? 578  PRO A CA  1 
ATOM   3166 C  C   . PRO A 1 578 ? 5.580   -14.026 -34.237 1.00 18.30 ? 578  PRO A C   1 
ATOM   3167 O  O   . PRO A 1 578 ? 4.893   -14.305 -35.242 1.00 18.42 ? 578  PRO A O   1 
ATOM   3168 C  CB  . PRO A 1 578 ? 7.415   -12.378 -34.765 1.00 19.40 ? 578  PRO A CB  1 
ATOM   3169 C  CG  . PRO A 1 578 ? 7.680   -12.419 -36.241 1.00 19.23 ? 578  PRO A CG  1 
ATOM   3170 C  CD  . PRO A 1 578 ? 8.223   -13.780 -36.531 1.00 19.26 ? 578  PRO A CD  1 
ATOM   3171 N  N   . LEU A 1 579 ? 5.088   -13.954 -33.003 1.00 17.32 ? 579  LEU A N   1 
ATOM   3172 C  CA  . LEU A 1 579 ? 3.650   -13.975 -32.748 1.00 17.22 ? 579  LEU A CA  1 
ATOM   3173 C  C   . LEU A 1 579 ? 3.130   -12.555 -32.824 1.00 16.88 ? 579  LEU A C   1 
ATOM   3174 O  O   . LEU A 1 579 ? 3.889   -11.597 -32.635 1.00 15.93 ? 579  LEU A O   1 
ATOM   3175 C  CB  . LEU A 1 579 ? 3.331   -14.592 -31.382 1.00 17.43 ? 579  LEU A CB  1 
ATOM   3176 C  CG  . LEU A 1 579 ? 3.853   -16.022 -31.156 1.00 17.23 ? 579  LEU A CG  1 
ATOM   3177 C  CD1 . LEU A 1 579 ? 3.771   -16.401 -29.690 1.00 16.87 ? 579  LEU A CD1 1 
ATOM   3178 C  CD2 . LEU A 1 579 ? 3.096   -17.030 -31.999 1.00 18.02 ? 579  LEU A CD2 1 
ATOM   3179 N  N   . ASN A 1 580 ? 1.838   -12.421 -33.117 1.00 16.96 ? 580  ASN A N   1 
ATOM   3180 C  CA  . ASN A 1 580 ? 1.167   -11.111 -33.177 1.00 16.61 ? 580  ASN A CA  1 
ATOM   3181 C  C   . ASN A 1 580 ? 1.922   -10.094 -34.037 1.00 17.56 ? 580  ASN A C   1 
ATOM   3182 O  O   . ASN A 1 580 ? 2.133   -8.951  -33.623 1.00 16.42 ? 580  ASN A O   1 
ATOM   3183 C  CB  . ASN A 1 580 ? 0.951   -10.557 -31.764 1.00 16.45 ? 580  ASN A CB  1 
ATOM   3184 C  CG  . ASN A 1 580 ? 0.176   -11.521 -30.870 1.00 16.72 ? 580  ASN A CG  1 
ATOM   3185 O  OD1 . ASN A 1 580 ? -0.928  -11.932 -31.207 1.00 17.50 ? 580  ASN A OD1 1 
ATOM   3186 N  ND2 . ASN A 1 580 ? 0.745   -11.873 -29.729 1.00 16.19 ? 580  ASN A ND2 1 
ATOM   3187 N  N   . ASP A 1 581 ? 2.339   -10.526 -35.226 1.00 18.60 ? 581  ASP A N   1 
ATOM   3188 C  CA  . ASP A 1 581 ? 3.139   -9.703  -36.161 1.00 19.99 ? 581  ASP A CA  1 
ATOM   3189 C  C   . ASP A 1 581 ? 4.570   -9.357  -35.715 1.00 18.51 ? 581  ASP A C   1 
ATOM   3190 O  O   . ASP A 1 581 ? 5.527   -9.764  -36.347 1.00 18.10 ? 581  ASP A O   1 
ATOM   3191 C  CB  . ASP A 1 581 ? 2.414   -8.403  -36.540 1.00 22.38 ? 581  ASP A CB  1 
ATOM   3192 C  CG  . ASP A 1 581 ? 3.155   -7.630  -37.608 1.00 25.07 ? 581  ASP A CG  1 
ATOM   3193 O  OD1 . ASP A 1 581 ? 3.442   -8.230  -38.665 1.00 30.69 ? 581  ASP A OD1 1 
ATOM   3194 O  OD2 . ASP A 1 581 ? 3.490   -6.439  -37.395 1.00 27.51 ? 581  ASP A OD2 1 
ATOM   3195 N  N   . SER A 1 582 ? 4.695   -8.603  -34.630 1.00 17.48 ? 582  SER A N   1 
ATOM   3196 C  CA  . SER A 1 582 ? 5.956   -8.023  -34.202 1.00 16.59 ? 582  SER A CA  1 
ATOM   3197 C  C   . SER A 1 582 ? 6.719   -8.855  -33.172 1.00 16.33 ? 582  SER A C   1 
ATOM   3198 O  O   . SER A 1 582 ? 7.888   -8.548  -32.862 1.00 14.68 ? 582  SER A O   1 
ATOM   3199 C  CB  . SER A 1 582 ? 5.662   -6.696  -33.545 1.00 16.81 ? 582  SER A CB  1 
ATOM   3200 O  OG  . SER A 1 582 ? 4.790   -6.898  -32.436 1.00 17.17 ? 582  SER A OG  1 
ATOM   3201 N  N   . GLY A 1 583 ? 6.044   -9.854  -32.599 1.00 15.25 ? 583  GLY A N   1 
ATOM   3202 C  CA  . GLY A 1 583 ? 6.634   -10.671 -31.558 1.00 15.24 ? 583  GLY A CA  1 
ATOM   3203 C  C   . GLY A 1 583 ? 6.110   -10.267 -30.195 1.00 15.47 ? 583  GLY A C   1 
ATOM   3204 O  O   . GLY A 1 583 ? 6.393   -10.940 -29.220 1.00 15.18 ? 583  GLY A O   1 
ATOM   3205 N  N   . VAL A 1 584 ? 5.356   -9.164  -30.118 1.00 15.55 ? 584  VAL A N   1 
ATOM   3206 C  CA  . VAL A 1 584 ? 4.740   -8.756  -28.848 1.00 15.29 ? 584  VAL A CA  1 
ATOM   3207 C  C   . VAL A 1 584 ? 3.761   -9.821  -28.322 1.00 14.94 ? 584  VAL A C   1 
ATOM   3208 O  O   . VAL A 1 584 ? 3.011   -10.406 -29.091 1.00 14.01 ? 584  VAL A O   1 
ATOM   3209 C  CB  . VAL A 1 584 ? 4.006   -7.396  -28.962 1.00 15.54 ? 584  VAL A CB  1 
ATOM   3210 C  CG1 . VAL A 1 584 ? 2.763   -7.483  -29.850 1.00 15.65 ? 584  VAL A CG1 1 
ATOM   3211 C  CG2 . VAL A 1 584 ? 3.639   -6.861  -27.576 1.00 16.18 ? 584  VAL A CG2 1 
ATOM   3212 N  N   . VAL A 1 585 ? 3.795   -10.064 -27.009 1.00 14.75 ? 585  VAL A N   1 
ATOM   3213 C  CA  . VAL A 1 585 ? 2.842   -10.958 -26.352 1.00 14.91 ? 585  VAL A CA  1 
ATOM   3214 C  C   . VAL A 1 585 ? 2.243   -10.289 -25.120 1.00 15.10 ? 585  VAL A C   1 
ATOM   3215 O  O   . VAL A 1 585 ? 1.027   -10.235 -24.987 1.00 15.00 ? 585  VAL A O   1 
ATOM   3216 C  CB  . VAL A 1 585 ? 3.487   -12.318 -25.996 1.00 14.99 ? 585  VAL A CB  1 
ATOM   3217 C  CG1 . VAL A 1 585 ? 2.492   -13.214 -25.260 1.00 15.20 ? 585  VAL A CG1 1 
ATOM   3218 C  CG2 . VAL A 1 585 ? 3.970   -13.000 -27.267 1.00 14.71 ? 585  VAL A CG2 1 
ATOM   3219 N  N   . LEU A 1 586 ? 3.096   -9.770  -24.236 1.00 15.41 ? 586  LEU A N   1 
ATOM   3220 C  CA  . LEU A 1 586 ? 2.648   -8.999  -23.074 1.00 16.31 ? 586  LEU A CA  1 
ATOM   3221 C  C   . LEU A 1 586 ? 3.290   -7.620  -23.035 1.00 16.71 ? 586  LEU A C   1 
ATOM   3222 O  O   . LEU A 1 586 ? 4.464   -7.481  -23.380 1.00 16.53 ? 586  LEU A O   1 
ATOM   3223 C  CB  . LEU A 1 586 ? 2.982   -9.735  -21.785 1.00 15.99 ? 586  LEU A CB  1 
ATOM   3224 C  CG  . LEU A 1 586 ? 2.360   -11.130 -21.672 1.00 16.21 ? 586  LEU A CG  1 
ATOM   3225 C  CD1 . LEU A 1 586 ? 2.887   -11.852 -20.452 1.00 16.81 ? 586  LEU A CD1 1 
ATOM   3226 C  CD2 . LEU A 1 586 ? 0.843   -11.051 -21.622 1.00 16.95 ? 586  LEU A CD2 1 
ATOM   3227 N  N   . THR A 1 587 ? 2.526   -6.611  -22.611 1.00 17.18 ? 587  THR A N   1 
ATOM   3228 C  CA  . THR A 1 587 ? 3.081   -5.267  -22.416 1.00 18.41 ? 587  THR A CA  1 
ATOM   3229 C  C   . THR A 1 587 ? 2.769   -4.732  -21.019 1.00 18.74 ? 587  THR A C   1 
ATOM   3230 O  O   . THR A 1 587 ? 1.713   -5.004  -20.458 1.00 18.54 ? 587  THR A O   1 
ATOM   3231 C  CB  . THR A 1 587 ? 2.577   -4.271  -23.480 1.00 19.18 ? 587  THR A CB  1 
ATOM   3232 O  OG1 . THR A 1 587 ? 1.155   -4.146  -23.405 1.00 19.19 ? 587  THR A OG1 1 
ATOM   3233 C  CG2 . THR A 1 587 ? 2.963   -4.748  -24.889 1.00 19.39 ? 587  THR A CG2 1 
ATOM   3234 N  N   . ALA A 1 588 ? 3.702   -3.974  -20.466 1.00 18.64 ? 588  ALA A N   1 
ATOM   3235 C  CA  . ALA A 1 588 ? 3.520   -3.350  -19.165 1.00 18.88 ? 588  ALA A CA  1 
ATOM   3236 C  C   . ALA A 1 588 ? 2.229   -2.535  -19.108 1.00 19.28 ? 588  ALA A C   1 
ATOM   3237 O  O   . ALA A 1 588 ? 1.837   -1.905  -20.087 1.00 18.86 ? 588  ALA A O   1 
ATOM   3238 C  CB  . ALA A 1 588 ? 4.713   -2.458  -18.864 1.00 19.35 ? 588  ALA A CB  1 
ATOM   3239 N  N   . SER A 1 589 ? 1.568   -2.555  -17.958 1.00 19.08 ? 589  SER A N   1 
ATOM   3240 C  CA  . SER A 1 589 ? 0.321   -1.812  -17.763 1.00 19.23 ? 589  SER A CA  1 
ATOM   3241 C  C   . SER A 1 589 ? 0.369   -0.809  -16.596 1.00 19.85 ? 589  SER A C   1 
ATOM   3242 O  O   . SER A 1 589 ? -0.524  0.023   -16.495 1.00 20.57 ? 589  SER A O   1 
ATOM   3243 C  CB  . SER A 1 589 ? -0.848  -2.787  -17.551 1.00 18.71 ? 589  SER A CB  1 
ATOM   3244 O  OG  . SER A 1 589 ? -0.542  -3.754  -16.549 1.00 18.24 ? 589  SER A OG  1 
ATOM   3245 N  N   . VAL A 1 590 ? 1.372   -0.896  -15.714 1.00 19.51 ? 590  VAL A N   1 
ATOM   3246 C  CA  . VAL A 1 590 ? 1.489   0.036   -14.585 1.00 20.31 ? 590  VAL A CA  1 
ATOM   3247 C  C   . VAL A 1 590 ? 2.904   0.571   -14.432 1.00 20.53 ? 590  VAL A C   1 
ATOM   3248 O  O   . VAL A 1 590 ? 3.865   -0.037  -14.930 1.00 20.54 ? 590  VAL A O   1 
ATOM   3249 C  CB  . VAL A 1 590 ? 1.063   -0.601  -13.230 1.00 20.23 ? 590  VAL A CB  1 
ATOM   3250 C  CG1 . VAL A 1 590 ? -0.425  -0.890  -13.229 1.00 20.27 ? 590  VAL A CG1 1 
ATOM   3251 C  CG2 . VAL A 1 590 ? 1.880   -1.858  -12.907 1.00 19.88 ? 590  VAL A CG2 1 
ATOM   3252 N  N   . PRO A 1 591 ? 3.049   1.708   -13.730 1.00 21.51 ? 591  PRO A N   1 
ATOM   3253 C  CA  . PRO A 1 591 ? 4.403   2.241   -13.513 1.00 21.67 ? 591  PRO A CA  1 
ATOM   3254 C  C   . PRO A 1 591 ? 5.329   1.278   -12.772 1.00 22.44 ? 591  PRO A C   1 
ATOM   3255 O  O   . PRO A 1 591 ? 4.873   0.482   -11.924 1.00 22.36 ? 591  PRO A O   1 
ATOM   3256 C  CB  . PRO A 1 591 ? 4.167   3.530   -12.711 1.00 21.16 ? 591  PRO A CB  1 
ATOM   3257 C  CG  . PRO A 1 591 ? 2.777   3.932   -13.021 1.00 21.31 ? 591  PRO A CG  1 
ATOM   3258 C  CD  . PRO A 1 591 ? 2.008   2.654   -13.285 1.00 21.87 ? 591  PRO A CD  1 
ATOM   3259 N  N   . ALA A 1 592 ? 6.619   1.352   -13.113 1.00 22.81 ? 592  ALA A N   1 
ATOM   3260 C  CA  . ALA A 1 592 ? 7.608   0.386   -12.627 1.00 23.01 ? 592  ALA A CA  1 
ATOM   3261 C  C   . ALA A 1 592 ? 7.822   0.457   -11.109 1.00 23.73 ? 592  ALA A C   1 
ATOM   3262 O  O   . ALA A 1 592 ? 8.293   -0.505  -10.518 1.00 22.57 ? 592  ALA A O   1 
ATOM   3263 C  CB  . ALA A 1 592 ? 8.935   0.582   -13.337 1.00 22.87 ? 592  ALA A CB  1 
ATOM   3264 N  N   . ASN A 1 593 ? 7.493   1.592   -10.489 1.00 23.55 ? 593  ASN A N   1 
ATOM   3265 C  CA  . ASN A 1 593 ? 7.681   1.738   -9.046  1.00 24.60 ? 593  ASN A CA  1 
ATOM   3266 C  C   . ASN A 1 593 ? 6.447   1.438   -8.209  1.00 23.59 ? 593  ASN A C   1 
ATOM   3267 O  O   . ASN A 1 593 ? 6.466   1.641   -7.002  1.00 24.79 ? 593  ASN A O   1 
ATOM   3268 C  CB  . ASN A 1 593 ? 8.237   3.132   -8.696  1.00 25.19 ? 593  ASN A CB  1 
ATOM   3269 C  CG  . ASN A 1 593 ? 7.303   4.253   -9.084  1.00 24.99 ? 593  ASN A CG  1 
ATOM   3270 O  OD1 . ASN A 1 593 ? 6.447   4.098   -9.939  1.00 25.06 ? 593  ASN A OD1 1 
ATOM   3271 N  ND2 . ASN A 1 593 ? 7.493   5.409   -8.469  1.00 27.01 ? 593  ASN A ND2 1 
ATOM   3272 N  N   . TRP A 1 594 ? 5.380   0.936   -8.830  1.00 23.35 ? 594  TRP A N   1 
ATOM   3273 C  CA  . TRP A 1 594 ? 4.195   0.561   -8.081  1.00 22.59 ? 594  TRP A CA  1 
ATOM   3274 C  C   . TRP A 1 594 ? 4.347   -0.836  -7.523  1.00 22.47 ? 594  TRP A C   1 
ATOM   3275 O  O   . TRP A 1 594 ? 5.042   -1.687  -8.096  1.00 21.34 ? 594  TRP A O   1 
ATOM   3276 C  CB  . TRP A 1 594 ? 2.956   0.588   -8.953  1.00 23.54 ? 594  TRP A CB  1 
ATOM   3277 C  CG  . TRP A 1 594 ? 2.416   1.943   -9.279  1.00 23.26 ? 594  TRP A CG  1 
ATOM   3278 C  CD1 . TRP A 1 594 ? 3.037   3.155   -9.132  1.00 23.77 ? 594  TRP A CD1 1 
ATOM   3279 C  CD2 . TRP A 1 594 ? 1.138   2.211   -9.843  1.00 23.07 ? 594  TRP A CD2 1 
ATOM   3280 N  NE1 . TRP A 1 594 ? 2.209   4.164   -9.567  1.00 23.19 ? 594  TRP A NE1 1 
ATOM   3281 C  CE2 . TRP A 1 594 ? 1.040   3.610   -10.018 1.00 23.30 ? 594  TRP A CE2 1 
ATOM   3282 C  CE3 . TRP A 1 594 ? 0.063   1.403   -10.225 1.00 22.75 ? 594  TRP A CE3 1 
ATOM   3283 C  CZ2 . TRP A 1 594 ? -0.087  4.215   -10.562 1.00 23.43 ? 594  TRP A CZ2 1 
ATOM   3284 C  CZ3 . TRP A 1 594 ? -1.063  2.004   -10.754 1.00 23.20 ? 594  TRP A CZ3 1 
ATOM   3285 C  CH2 . TRP A 1 594 ? -1.127  3.400   -10.923 1.00 24.10 ? 594  TRP A CH2 1 
ATOM   3286 N  N   . ARG A 1 595 ? 3.671   -1.070  -6.402  1.00 23.39 ? 595  ARG A N   1 
ATOM   3287 C  CA  . ARG A 1 595 ? 3.572   -2.406  -5.796  1.00 22.60 ? 595  ARG A CA  1 
ATOM   3288 C  C   . ARG A 1 595 ? 3.241   -3.502  -6.816  1.00 21.62 ? 595  ARG A C   1 
ATOM   3289 O  O   . ARG A 1 595 ? 3.872   -4.560  -6.810  1.00 21.26 ? 595  ARG A O   1 
ATOM   3290 C  CB  . ARG A 1 595 ? 2.494   -2.398  -4.694  1.00 23.22 ? 595  ARG A CB  1 
ATOM   3291 C  CG  . ARG A 1 595 ? 2.375   -3.683  -3.872  1.00 22.26 ? 595  ARG A CG  1 
ATOM   3292 C  CD  . ARG A 1 595 ? 3.703   -4.034  -3.250  1.00 22.39 ? 595  ARG A CD  1 
ATOM   3293 N  NE  . ARG A 1 595 ? 3.593   -4.870  -2.051  1.00 23.13 ? 595  ARG A NE  1 
ATOM   3294 C  CZ  . ARG A 1 595 ? 4.430   -5.853  -1.716  1.00 23.52 ? 595  ARG A CZ  1 
ATOM   3295 N  NH1 . ARG A 1 595 ? 5.446   -6.189  -2.502  1.00 23.12 ? 595  ARG A NH1 1 
ATOM   3296 N  NH2 . ARG A 1 595 ? 4.242   -6.534  -0.583  1.00 24.63 ? 595  ARG A NH2 1 
ATOM   3297 N  N   . THR A 1 596 ? 2.250   -3.255  -7.676  1.00 21.91 ? 596  THR A N   1 
ATOM   3298 C  CA  . THR A 1 596 ? 1.802   -4.270  -8.651  1.00 21.58 ? 596  THR A CA  1 
ATOM   3299 C  C   . THR A 1 596 ? 2.590   -4.311  -9.988  1.00 20.19 ? 596  THR A C   1 
ATOM   3300 O  O   . THR A 1 596 ? 2.150   -4.947  -10.941 1.00 20.09 ? 596  THR A O   1 
ATOM   3301 C  CB  . THR A 1 596 ? 0.288   -4.141  -8.953  1.00 22.84 ? 596  THR A CB  1 
ATOM   3302 O  OG1 . THR A 1 596 ? 0.015   -2.884  -9.595  1.00 22.12 ? 596  THR A OG1 1 
ATOM   3303 C  CG2 . THR A 1 596 ? -0.553  -4.275  -7.656  1.00 22.63 ? 596  THR A CG2 1 
ATOM   3304 N  N   . ALA A 1 597 ? 3.736   -3.641  -10.066 1.00 19.29 ? 597  ALA A N   1 
ATOM   3305 C  CA  . ALA A 1 597 ? 4.626   -3.769  -11.244 1.00 19.71 ? 597  ALA A CA  1 
ATOM   3306 C  C   . ALA A 1 597 ? 5.136   -5.205  -11.333 1.00 19.04 ? 597  ALA A C   1 
ATOM   3307 O  O   . ALA A 1 597 ? 5.336   -5.858  -10.305 1.00 18.85 ? 597  ALA A O   1 
ATOM   3308 C  CB  . ALA A 1 597 ? 5.803   -2.806  -11.146 1.00 19.70 ? 597  ALA A CB  1 
ATOM   3309 N  N   . THR A 1 598 ? 5.321   -5.696  -12.552 1.00 18.77 ? 598  THR A N   1 
ATOM   3310 C  CA  . THR A 1 598 ? 5.791   -7.051  -12.762 1.00 18.64 ? 598  THR A CA  1 
ATOM   3311 C  C   . THR A 1 598 ? 6.973   -7.109  -13.719 1.00 18.61 ? 598  THR A C   1 
ATOM   3312 O  O   . THR A 1 598 ? 7.273   -6.152  -14.441 1.00 17.96 ? 598  THR A O   1 
ATOM   3313 C  CB  . THR A 1 598 ? 4.672   -7.985  -13.282 1.00 18.80 ? 598  THR A CB  1 
ATOM   3314 O  OG1 . THR A 1 598 ? 3.988   -7.374  -14.372 1.00 17.00 ? 598  THR A OG1 1 
ATOM   3315 C  CG2 . THR A 1 598 ? 3.666   -8.282  -12.173 1.00 19.11 ? 598  THR A CG2 1 
ATOM   3316 N  N   . TYR A 1 599 ? 7.669   -8.240  -13.664 1.00 18.73 ? 599  TYR A N   1 
ATOM   3317 C  CA  . TYR A 1 599 ? 8.685   -8.564  -14.637 1.00 19.63 ? 599  TYR A CA  1 
ATOM   3318 C  C   . TYR A 1 599 ? 9.055   -10.053 -14.603 1.00 20.19 ? 599  TYR A C   1 
ATOM   3319 O  O   . TYR A 1 599 ? 8.560   -10.820 -13.769 1.00 20.07 ? 599  TYR A O   1 
ATOM   3320 C  CB  . TYR A 1 599 ? 9.937   -7.668  -14.489 1.00 18.87 ? 599  TYR A CB  1 
ATOM   3321 C  CG  . TYR A 1 599 ? 10.898  -7.842  -15.651 1.00 18.40 ? 599  TYR A CG  1 
ATOM   3322 C  CD1 . TYR A 1 599 ? 10.522  -7.495  -16.936 1.00 18.08 ? 599  TYR A CD1 1 
ATOM   3323 C  CD2 . TYR A 1 599 ? 12.163  -8.400  -15.464 1.00 18.79 ? 599  TYR A CD2 1 
ATOM   3324 C  CE1 . TYR A 1 599 ? 11.374  -7.687  -18.008 1.00 18.33 ? 599  TYR A CE1 1 
ATOM   3325 C  CE2 . TYR A 1 599 ? 13.036  -8.589  -16.525 1.00 18.90 ? 599  TYR A CE2 1 
ATOM   3326 C  CZ  . TYR A 1 599 ? 12.632  -8.236  -17.801 1.00 18.76 ? 599  TYR A CZ  1 
ATOM   3327 O  OH  . TYR A 1 599 ? 13.495  -8.434  -18.853 1.00 18.58 ? 599  TYR A OH  1 
ATOM   3328 N  N   . SER A 1 600 ? 9.867   -10.453 -15.579 1.00 21.27 ? 600  SER A N   1 
ATOM   3329 C  CA  . SER A 1 600 ? 10.408  -11.786 -15.662 1.00 22.30 ? 600  SER A CA  1 
ATOM   3330 C  C   . SER A 1 600 ? 9.294   -12.820 -15.832 1.00 20.64 ? 600  SER A C   1 
ATOM   3331 O  O   . SER A 1 600 ? 9.281   -13.877 -15.202 1.00 20.37 ? 600  SER A O   1 
ATOM   3332 C  CB  . SER A 1 600 ? 11.302  -12.059 -14.461 1.00 23.50 ? 600  SER A CB  1 
ATOM   3333 O  OG  . SER A 1 600 ? 12.319  -12.948 -14.844 1.00 28.99 ? 600  SER A OG  1 
ATOM   3334 N  N   . TYR A 1 601 ? 8.389   -12.482 -16.745 1.00 20.30 ? 601  TYR A N   1 
ATOM   3335 C  CA  . TYR A 1 601 ? 7.253   -13.304 -17.155 1.00 19.86 ? 601  TYR A CA  1 
ATOM   3336 C  C   . TYR A 1 601 ? 7.761   -14.667 -17.581 1.00 19.77 ? 601  TYR A C   1 
ATOM   3337 O  O   . TYR A 1 601 ? 8.759   -14.761 -18.285 1.00 19.62 ? 601  TYR A O   1 
ATOM   3338 C  CB  . TYR A 1 601 ? 6.500   -12.618 -18.310 1.00 19.51 ? 601  TYR A CB  1 
ATOM   3339 C  CG  . TYR A 1 601 ? 6.153   -11.199 -17.950 1.00 19.91 ? 601  TYR A CG  1 
ATOM   3340 C  CD1 . TYR A 1 601 ? 5.166   -10.939 -17.015 1.00 20.17 ? 601  TYR A CD1 1 
ATOM   3341 C  CD2 . TYR A 1 601 ? 6.827   -10.111 -18.509 1.00 19.74 ? 601  TYR A CD2 1 
ATOM   3342 C  CE1 . TYR A 1 601 ? 4.856   -9.652  -16.642 1.00 19.87 ? 601  TYR A CE1 1 
ATOM   3343 C  CE2 . TYR A 1 601 ? 6.497   -8.814  -18.148 1.00 19.96 ? 601  TYR A CE2 1 
ATOM   3344 C  CZ  . TYR A 1 601 ? 5.514   -8.596  -17.206 1.00 20.11 ? 601  TYR A CZ  1 
ATOM   3345 O  OH  . TYR A 1 601 ? 5.166   -7.313  -16.791 1.00 21.64 ? 601  TYR A OH  1 
ATOM   3346 N  N   . TYR A 1 602 ? 7.112   -15.714 -17.095 1.00 19.34 ? 602  TYR A N   1 
ATOM   3347 C  CA  . TYR A 1 602 ? 7.525   -17.068 -17.394 1.00 19.50 ? 602  TYR A CA  1 
ATOM   3348 C  C   . TYR A 1 602 ? 6.314   -17.962 -17.585 1.00 19.61 ? 602  TYR A C   1 
ATOM   3349 O  O   . TYR A 1 602 ? 5.576   -18.276 -16.625 1.00 19.97 ? 602  TYR A O   1 
ATOM   3350 C  CB  . TYR A 1 602 ? 8.414   -17.592 -16.281 1.00 19.77 ? 602  TYR A CB  1 
ATOM   3351 C  CG  . TYR A 1 602 ? 9.083   -18.894 -16.602 1.00 20.45 ? 602  TYR A CG  1 
ATOM   3352 C  CD1 . TYR A 1 602 ? 10.237  -18.933 -17.386 1.00 21.35 ? 602  TYR A CD1 1 
ATOM   3353 C  CD2 . TYR A 1 602 ? 8.583   -20.086 -16.110 1.00 20.52 ? 602  TYR A CD2 1 
ATOM   3354 C  CE1 . TYR A 1 602 ? 10.865  -20.124 -17.663 1.00 22.32 ? 602  TYR A CE1 1 
ATOM   3355 C  CE2 . TYR A 1 602 ? 9.203   -21.282 -16.387 1.00 21.52 ? 602  TYR A CE2 1 
ATOM   3356 C  CZ  . TYR A 1 602 ? 10.332  -21.301 -17.171 1.00 21.70 ? 602  TYR A CZ  1 
ATOM   3357 O  OH  . TYR A 1 602 ? 10.936  -22.496 -17.447 1.00 23.65 ? 602  TYR A OH  1 
ATOM   3358 N  N   . ALA A 1 603 ? 6.137   -18.388 -18.823 1.00 18.67 ? 603  ALA A N   1 
ATOM   3359 C  CA  . ALA A 1 603 ? 4.978   -19.158 -19.235 1.00 18.87 ? 603  ALA A CA  1 
ATOM   3360 C  C   . ALA A 1 603 ? 5.164   -20.645 -18.891 1.00 19.01 ? 603  ALA A C   1 
ATOM   3361 O  O   . ALA A 1 603 ? 6.222   -21.219 -19.146 1.00 18.35 ? 603  ALA A O   1 
ATOM   3362 C  CB  . ALA A 1 603 ? 4.748   -18.983 -20.728 1.00 18.42 ? 603  ALA A CB  1 
ATOM   3363 N  N   . VAL A 1 604 ? 4.129   -21.245 -18.306 1.00 19.08 ? 604  VAL A N   1 
ATOM   3364 C  CA  . VAL A 1 604 ? 4.141   -22.645 -17.901 1.00 20.90 ? 604  VAL A CA  1 
ATOM   3365 C  C   . VAL A 1 604 ? 2.914   -23.321 -18.504 1.00 20.88 ? 604  VAL A C   1 
ATOM   3366 O  O   . VAL A 1 604 ? 1.835   -22.721 -18.528 1.00 20.02 ? 604  VAL A O   1 
ATOM   3367 C  CB  . VAL A 1 604 ? 4.145   -22.721 -16.354 1.00 23.90 ? 604  VAL A CB  1 
ATOM   3368 C  CG1 . VAL A 1 604 ? 3.484   -23.978 -15.829 1.00 26.19 ? 604  VAL A CG1 1 
ATOM   3369 C  CG2 . VAL A 1 604 ? 5.568   -22.589 -15.824 1.00 24.10 ? 604  VAL A CG2 1 
ATOM   3370 N  N   . PRO A 1 605 ? 3.059   -24.563 -19.009 1.00 21.57 ? 605  PRO A N   1 
ATOM   3371 C  CA  . PRO A 1 605 ? 1.876   -25.188 -19.617 1.00 22.95 ? 605  PRO A CA  1 
ATOM   3372 C  C   . PRO A 1 605 ? 0.777   -25.525 -18.617 1.00 23.47 ? 605  PRO A C   1 
ATOM   3373 O  O   . PRO A 1 605 ? 0.968   -25.432 -17.405 1.00 24.49 ? 605  PRO A O   1 
ATOM   3374 C  CB  . PRO A 1 605 ? 2.420   -26.464 -20.274 1.00 22.62 ? 605  PRO A CB  1 
ATOM   3375 C  CG  . PRO A 1 605 ? 3.771   -26.682 -19.698 1.00 22.79 ? 605  PRO A CG  1 
ATOM   3376 C  CD  . PRO A 1 605 ? 4.274   -25.378 -19.169 1.00 22.16 ? 605  PRO A CD  1 
ATOM   3377 N  N   . VAL A 1 606 ? -0.383  -25.864 -19.139 1.00 24.55 ? 606  VAL A N   1 
ATOM   3378 C  CA  . VAL A 1 606 ? -1.536  -26.114 -18.304 1.00 25.83 ? 606  VAL A CA  1 
ATOM   3379 C  C   . VAL A 1 606 ? -1.975  -27.533 -18.616 1.00 27.29 ? 606  VAL A C   1 
ATOM   3380 O  O   . VAL A 1 606 ? -2.105  -27.885 -19.785 1.00 27.95 ? 606  VAL A O   1 
ATOM   3381 C  CB  . VAL A 1 606 ? -2.639  -25.096 -18.608 1.00 26.43 ? 606  VAL A CB  1 
ATOM   3382 C  CG1 . VAL A 1 606 ? -3.950  -25.473 -17.928 1.00 27.46 ? 606  VAL A CG1 1 
ATOM   3383 C  CG2 . VAL A 1 606 ? -2.196  -23.699 -18.185 1.00 25.42 ? 606  VAL A CG2 1 
ATOM   3384 N  N   . ALA A 1 607 ? -2.161  -28.354 -17.582 1.00 28.19 ? 607  ALA A N   1 
ATOM   3385 C  CA  . ALA A 1 607 ? -2.528  -29.767 -17.773 1.00 30.42 ? 607  ALA A CA  1 
ATOM   3386 C  C   . ALA A 1 607 ? -3.845  -29.906 -18.555 1.00 31.25 ? 607  ALA A C   1 
ATOM   3387 O  O   . ALA A 1 607 ? -4.856  -29.321 -18.172 1.00 30.28 ? 607  ALA A O   1 
ATOM   3388 C  CB  . ALA A 1 607 ? -2.651  -30.466 -16.419 1.00 30.67 ? 607  ALA A CB  1 
ATOM   3389 N  N   . GLY A 1 608 ? -3.822  -30.657 -19.653 1.00 33.40 ? 608  GLY A N   1 
ATOM   3390 C  CA  . GLY A 1 608 ? -5.038  -30.943 -20.425 1.00 36.59 ? 608  GLY A CA  1 
ATOM   3391 C  C   . GLY A 1 608 ? -5.378  -29.945 -21.531 1.00 41.47 ? 608  GLY A C   1 
ATOM   3392 O  O   . GLY A 1 608 ? -6.349  -30.140 -22.276 1.00 42.30 ? 608  GLY A O   1 
ATOM   3393 N  N   . LYS A 1 609 ? -4.592  -28.876 -21.660 1.00 41.64 ? 609  LYS A N   1 
ATOM   3394 C  CA  . LYS A 1 609 ? -4.880  -27.859 -22.666 1.00 41.21 ? 609  LYS A CA  1 
ATOM   3395 C  C   . LYS A 1 609 ? -3.684  -27.613 -23.570 1.00 38.59 ? 609  LYS A C   1 
ATOM   3396 O  O   . LYS A 1 609 ? -2.546  -27.586 -23.117 1.00 38.96 ? 609  LYS A O   1 
ATOM   3397 C  CB  . LYS A 1 609 ? -5.360  -26.582 -21.987 1.00 44.19 ? 609  LYS A CB  1 
ATOM   3398 C  CG  . LYS A 1 609 ? -6.649  -26.811 -21.205 1.00 47.82 ? 609  LYS A CG  1 
ATOM   3399 C  CD  . LYS A 1 609 ? -7.419  -25.532 -20.956 1.00 50.68 ? 609  LYS A CD  1 
ATOM   3400 C  CE  . LYS A 1 609 ? -8.212  -25.083 -22.177 1.00 53.13 ? 609  LYS A CE  1 
ATOM   3401 N  NZ  . LYS A 1 609 ? -9.549  -25.729 -22.238 1.00 55.26 ? 609  LYS A NZ  1 
ATOM   3402 N  N   . ASP A 1 610 ? -3.944  -27.457 -24.860 1.00 35.25 ? 610  ASP A N   1 
ATOM   3403 C  CA  . ASP A 1 610 ? -2.870  -27.200 -25.818 1.00 34.57 ? 610  ASP A CA  1 
ATOM   3404 C  C   . ASP A 1 610 ? -2.934  -25.778 -26.390 1.00 31.59 ? 610  ASP A C   1 
ATOM   3405 O  O   . ASP A 1 610 ? -2.224  -25.461 -27.336 1.00 31.72 ? 610  ASP A O   1 
ATOM   3406 C  CB  . ASP A 1 610 ? -2.913  -28.244 -26.935 1.00 35.03 ? 610  ASP A CB  1 
ATOM   3407 C  CG  . ASP A 1 610 ? -4.193  -28.189 -27.733 1.00 36.52 ? 610  ASP A CG  1 
ATOM   3408 O  OD1 . ASP A 1 610 ? -5.055  -27.336 -27.437 1.00 37.71 ? 610  ASP A OD1 1 
ATOM   3409 O  OD2 . ASP A 1 610 ? -4.332  -28.992 -28.668 1.00 40.45 ? 610  ASP A OD2 1 
ATOM   3410 N  N   . ASP A 1 611 ? -3.782  -24.933 -25.812 1.00 30.24 ? 611  ASP A N   1 
ATOM   3411 C  CA  . ASP A 1 611 ? -4.009  -23.583 -26.328 1.00 29.99 ? 611  ASP A CA  1 
ATOM   3412 C  C   . ASP A 1 611 ? -3.994  -22.494 -25.246 1.00 27.56 ? 611  ASP A C   1 
ATOM   3413 O  O   . ASP A 1 611 ? -4.426  -21.366 -25.495 1.00 27.44 ? 611  ASP A O   1 
ATOM   3414 C  CB  . ASP A 1 611 ? -5.330  -23.545 -27.105 1.00 32.10 ? 611  ASP A CB  1 
ATOM   3415 C  CG  . ASP A 1 611 ? -6.558  -23.673 -26.202 1.00 34.20 ? 611  ASP A CG  1 
ATOM   3416 O  OD1 . ASP A 1 611 ? -6.479  -24.295 -25.119 1.00 33.39 ? 611  ASP A OD1 1 
ATOM   3417 O  OD2 . ASP A 1 611 ? -7.613  -23.131 -26.583 1.00 38.84 ? 611  ASP A OD2 1 
ATOM   3418 N  N   . GLN A 1 612 ? -3.494  -22.827 -24.060 1.00 25.46 ? 612  GLN A N   1 
ATOM   3419 C  CA  . GLN A 1 612 ? -3.326  -21.867 -22.978 1.00 25.53 ? 612  GLN A CA  1 
ATOM   3420 C  C   . GLN A 1 612 ? -1.994  -22.101 -22.297 1.00 24.36 ? 612  GLN A C   1 
ATOM   3421 O  O   . GLN A 1 612 ? -1.525  -23.241 -22.215 1.00 23.38 ? 612  GLN A O   1 
ATOM   3422 C  CB  . GLN A 1 612 ? -4.394  -22.043 -21.909 1.00 26.68 ? 612  GLN A CB  1 
ATOM   3423 C  CG  . GLN A 1 612 ? -5.809  -21.752 -22.344 1.00 28.05 ? 612  GLN A CG  1 
ATOM   3424 C  CD  . GLN A 1 612 ? -6.809  -21.990 -21.227 1.00 30.26 ? 612  GLN A CD  1 
ATOM   3425 O  OE1 . GLN A 1 612 ? -6.507  -22.649 -20.206 1.00 32.35 ? 612  GLN A OE1 1 
ATOM   3426 N  NE2 . GLN A 1 612 ? -8.015  -21.469 -21.413 1.00 29.85 ? 612  GLN A NE2 1 
ATOM   3427 N  N   . VAL A 1 613 ? -1.406  -21.026 -21.780 1.00 22.06 ? 613  VAL A N   1 
ATOM   3428 C  CA  . VAL A 1 613 ? -0.324  -21.152 -20.829 1.00 21.23 ? 613  VAL A CA  1 
ATOM   3429 C  C   . VAL A 1 613 ? -0.658  -20.305 -19.622 1.00 20.58 ? 613  VAL A C   1 
ATOM   3430 O  O   . VAL A 1 613 ? -1.506  -19.409 -19.707 1.00 20.13 ? 613  VAL A O   1 
ATOM   3431 C  CB  . VAL A 1 613 ? 1.052   -20.760 -21.416 1.00 21.24 ? 613  VAL A CB  1 
ATOM   3432 C  CG1 . VAL A 1 613 ? 1.452   -21.730 -22.517 1.00 21.39 ? 613  VAL A CG1 1 
ATOM   3433 C  CG2 . VAL A 1 613 ? 1.069   -19.317 -21.905 1.00 21.82 ? 613  VAL A CG2 1 
ATOM   3434 N  N   . LEU A 1 614 ? -0.026  -20.631 -18.497 1.00 19.89 ? 614  LEU A N   1 
ATOM   3435 C  CA  . LEU A 1 614 ? -0.141  -19.842 -17.264 1.00 19.98 ? 614  LEU A CA  1 
ATOM   3436 C  C   . LEU A 1 614 ? 1.107   -18.955 -17.117 1.00 19.36 ? 614  LEU A C   1 
ATOM   3437 O  O   . LEU A 1 614 ? 2.227   -19.459 -16.993 1.00 19.69 ? 614  LEU A O   1 
ATOM   3438 C  CB  . LEU A 1 614 ? -0.286  -20.759 -16.052 1.00 19.91 ? 614  LEU A CB  1 
ATOM   3439 C  CG  . LEU A 1 614 ? -0.530  -20.049 -14.711 1.00 20.82 ? 614  LEU A CG  1 
ATOM   3440 C  CD1 . LEU A 1 614 ? -1.925  -19.439 -14.690 1.00 21.37 ? 614  LEU A CD1 1 
ATOM   3441 C  CD2 . LEU A 1 614 ? -0.323  -20.995 -13.530 1.00 20.85 ? 614  LEU A CD2 1 
ATOM   3442 N  N   . VAL A 1 615 ? 0.914   -17.640 -17.131 1.00 18.38 ? 615  VAL A N   1 
ATOM   3443 C  CA  . VAL A 1 615 ? 2.038   -16.719 -17.040 1.00 17.90 ? 615  VAL A CA  1 
ATOM   3444 C  C   . VAL A 1 615 ? 2.324   -16.388 -15.584 1.00 17.43 ? 615  VAL A C   1 
ATOM   3445 O  O   . VAL A 1 615 ? 1.493   -15.810 -14.882 1.00 16.21 ? 615  VAL A O   1 
ATOM   3446 C  CB  . VAL A 1 615 ? 1.809   -15.422 -17.840 1.00 18.38 ? 615  VAL A CB  1 
ATOM   3447 C  CG1 . VAL A 1 615 ? 3.018   -14.493 -17.704 1.00 18.56 ? 615  VAL A CG1 1 
ATOM   3448 C  CG2 . VAL A 1 615 ? 1.557   -15.764 -19.303 1.00 18.74 ? 615  VAL A CG2 1 
ATOM   3449 N  N   . THR A 1 616 ? 3.516   -16.766 -15.145 1.00 17.57 ? 616  THR A N   1 
ATOM   3450 C  CA  . THR A 1 616 ? 3.989   -16.416 -13.822 1.00 18.26 ? 616  THR A CA  1 
ATOM   3451 C  C   . THR A 1 616 ? 4.933   -15.226 -13.936 1.00 18.27 ? 616  THR A C   1 
ATOM   3452 O  O   . THR A 1 616 ? 5.443   -14.934 -15.005 1.00 17.88 ? 616  THR A O   1 
ATOM   3453 C  CB  . THR A 1 616 ? 4.721   -17.591 -13.154 1.00 18.29 ? 616  THR A CB  1 
ATOM   3454 O  OG1 . THR A 1 616 ? 5.980   -17.799 -13.795 1.00 19.05 ? 616  THR A OG1 1 
ATOM   3455 C  CG2 . THR A 1 616 ? 3.891   -18.861 -13.260 1.00 19.22 ? 616  THR A CG2 1 
ATOM   3456 N  N   . SER A 1 617 ? 5.143   -14.545 -12.823 1.00 18.56 ? 617  SER A N   1 
ATOM   3457 C  CA  . SER A 1 617 ? 6.088   -13.450 -12.762 1.00 19.31 ? 617  SER A CA  1 
ATOM   3458 C  C   . SER A 1 617 ? 6.385   -13.081 -11.328 1.00 20.10 ? 617  SER A C   1 
ATOM   3459 O  O   . SER A 1 617 ? 5.671   -13.487 -10.390 1.00 20.93 ? 617  SER A O   1 
ATOM   3460 C  CB  . SER A 1 617 ? 5.551   -12.203 -13.509 1.00 19.54 ? 617  SER A CB  1 
ATOM   3461 O  OG  . SER A 1 617 ? 4.351   -11.708 -12.950 1.00 18.54 ? 617  SER A OG  1 
ATOM   3462 N  N   . TYR A 1 618 ? 7.439   -12.299 -11.143 1.00 20.93 ? 618  TYR A N   1 
ATOM   3463 C  CA  . TYR A 1 618 ? 7.661   -11.713 -9.852  1.00 21.11 ? 618  TYR A CA  1 
ATOM   3464 C  C   . TYR A 1 618 ? 7.020   -10.344 -9.866  1.00 22.23 ? 618  TYR A C   1 
ATOM   3465 O  O   . TYR A 1 618 ? 6.883   -9.724  -10.927 1.00 21.01 ? 618  TYR A O   1 
ATOM   3466 C  CB  . TYR A 1 618 ? 9.139   -11.731 -9.456  1.00 21.03 ? 618  TYR A CB  1 
ATOM   3467 C  CG  . TYR A 1 618 ? 10.084  -10.732 -10.076 1.00 21.57 ? 618  TYR A CG  1 
ATOM   3468 C  CD1 . TYR A 1 618 ? 10.201  -9.445  -9.552  1.00 22.78 ? 618  TYR A CD1 1 
ATOM   3469 C  CD2 . TYR A 1 618 ? 10.928  -11.096 -11.126 1.00 21.02 ? 618  TYR A CD2 1 
ATOM   3470 C  CE1 . TYR A 1 618 ? 11.107  -8.530  -10.071 1.00 22.69 ? 618  TYR A CE1 1 
ATOM   3471 C  CE2 . TYR A 1 618 ? 11.837  -10.184 -11.658 1.00 22.19 ? 618  TYR A CE2 1 
ATOM   3472 C  CZ  . TYR A 1 618 ? 11.923  -8.906  -11.126 1.00 22.63 ? 618  TYR A CZ  1 
ATOM   3473 O  OH  . TYR A 1 618 ? 12.821  -8.002  -11.635 1.00 22.80 ? 618  TYR A OH  1 
ATOM   3474 N  N   . MET A 1 619 ? 6.588   -9.907  -8.685  1.00 23.07 ? 619  MET A N   1 
ATOM   3475 C  CA  . MET A 1 619 ? 5.884   -8.633  -8.524  1.00 23.44 ? 619  MET A CA  1 
ATOM   3476 C  C   . MET A 1 619 ? 6.663   -7.724  -7.585  1.00 22.78 ? 619  MET A C   1 
ATOM   3477 O  O   . MET A 1 619 ? 7.273   -8.188  -6.633  1.00 21.69 ? 619  MET A O   1 
ATOM   3478 C  CB  . MET A 1 619 ? 4.476   -8.869  -7.978  1.00 23.55 ? 619  MET A CB  1 
ATOM   3479 C  CG  . MET A 1 619 ? 3.653   -7.614  -7.728  1.00 23.01 ? 619  MET A CG  1 
ATOM   3480 S  SD  . MET A 1 619 ? 1.914   -8.000  -7.405  1.00 24.52 ? 619  MET A SD  1 
ATOM   3481 C  CE  . MET A 1 619 ? 1.200   -8.132  -9.036  1.00 25.10 ? 619  MET A CE  1 
ATOM   3482 N  N   . THR A 1 620 ? 6.619   -6.429  -7.884  1.00 22.55 ? 620  THR A N   1 
ATOM   3483 C  CA  . THR A 1 620 ? 7.343   -5.401  -7.167  1.00 22.25 ? 620  THR A CA  1 
ATOM   3484 C  C   . THR A 1 620 ? 8.813   -5.439  -7.517  1.00 23.14 ? 620  THR A C   1 
ATOM   3485 O  O   . THR A 1 620 ? 9.499   -6.452  -7.333  1.00 21.57 ? 620  THR A O   1 
ATOM   3486 C  CB  . THR A 1 620 ? 7.181   -5.474  -5.633  1.00 22.58 ? 620  THR A CB  1 
ATOM   3487 O  OG1 . THR A 1 620 ? 5.787   -5.575  -5.306  1.00 22.80 ? 620  THR A OG1 1 
ATOM   3488 C  CG2 . THR A 1 620 ? 7.774   -4.229  -4.991  1.00 23.01 ? 620  THR A CG2 1 
ATOM   3489 N  N   . ASN A 1 621 ? 9.303   -4.302  -8.006  1.00 22.66 ? 621  ASN A N   1 
ATOM   3490 C  CA  . ASN A 1 621 ? 10.666  -4.234  -8.426  1.00 23.06 ? 621  ASN A CA  1 
ATOM   3491 C  C   . ASN A 1 621 ? 11.583  -4.211  -7.235  1.00 23.44 ? 621  ASN A C   1 
ATOM   3492 O  O   . ASN A 1 621 ? 11.188  -3.793  -6.149  1.00 22.56 ? 621  ASN A O   1 
ATOM   3493 C  CB  . ASN A 1 621 ? 10.886  -3.069  -9.378  1.00 23.29 ? 621  ASN A CB  1 
ATOM   3494 C  CG  . ASN A 1 621 ? 10.627  -3.483  -10.811 1.00 23.14 ? 621  ASN A CG  1 
ATOM   3495 O  OD1 . ASN A 1 621 ? 11.316  -4.356  -11.328 1.00 23.30 ? 621  ASN A OD1 1 
ATOM   3496 N  ND2 . ASN A 1 621 ? 9.588   -2.943  -11.415 1.00 22.12 ? 621  ASN A ND2 1 
ATOM   3497 N  N   . ARG A 1 622 ? 12.793  -4.717  -7.451  1.00 24.08 ? 622  ARG A N   1 
ATOM   3498 C  CA  . ARG A 1 622 ? 13.739  -4.978  -6.363  1.00 25.66 ? 622  ARG A CA  1 
ATOM   3499 C  C   . ARG A 1 622 ? 14.156  -3.731  -5.590  1.00 26.36 ? 622  ARG A C   1 
ATOM   3500 O  O   . ARG A 1 622 ? 13.877  -2.600  -5.989  1.00 24.95 ? 622  ARG A O   1 
ATOM   3501 C  CB  . ARG A 1 622 ? 14.975  -5.675  -6.921  1.00 24.51 ? 622  ARG A CB  1 
ATOM   3502 C  CG  . ARG A 1 622 ? 14.681  -7.098  -7.354  1.00 24.71 ? 622  ARG A CG  1 
ATOM   3503 C  CD  . ARG A 1 622 ? 15.803  -7.666  -8.190  1.00 24.28 ? 622  ARG A CD  1 
ATOM   3504 N  NE  . ARG A 1 622 ? 17.085  -7.713  -7.483  1.00 24.49 ? 622  ARG A NE  1 
ATOM   3505 C  CZ  . ARG A 1 622 ? 18.263  -7.984  -8.062  1.00 24.31 ? 622  ARG A CZ  1 
ATOM   3506 N  NH1 . ARG A 1 622 ? 18.344  -8.259  -9.362  1.00 23.94 ? 622  ARG A NH1 1 
ATOM   3507 N  NH2 . ARG A 1 622 ? 19.372  -8.015  -7.334  1.00 24.02 ? 622  ARG A NH2 1 
ATOM   3508 N  N   . ASN A 1 623 ? 14.791  -3.968  -4.449  1.00 28.28 ? 623  ASN A N   1 
ATOM   3509 C  CA  . ASN A 1 623 ? 15.521  -2.935  -3.730  1.00 28.27 ? 623  ASN A CA  1 
ATOM   3510 C  C   . ASN A 1 623 ? 14.672  -1.804  -3.171  1.00 28.04 ? 623  ASN A C   1 
ATOM   3511 O  O   . ASN A 1 623 ? 15.134  -0.670  -3.076  1.00 31.38 ? 623  ASN A O   1 
ATOM   3512 C  CB  . ASN A 1 623 ? 16.621  -2.380  -4.638  1.00 27.83 ? 623  ASN A CB  1 
ATOM   3513 C  CG  . ASN A 1 623 ? 17.575  -3.457  -5.104  1.00 27.77 ? 623  ASN A CG  1 
ATOM   3514 O  OD1 . ASN A 1 623 ? 18.006  -4.310  -4.319  1.00 26.68 ? 623  ASN A OD1 1 
ATOM   3515 N  ND2 . ASN A 1 623 ? 17.918  -3.423  -6.382  1.00 26.38 ? 623  ASN A ND2 1 
ATOM   3516 N  N   . GLY A 1 624 ? 13.439  -2.114  -2.792  1.00 27.62 ? 624  GLY A N   1 
ATOM   3517 C  CA  . GLY A 1 624 ? 12.591  -1.175  -2.062  1.00 26.24 ? 624  GLY A CA  1 
ATOM   3518 C  C   . GLY A 1 624 ? 12.105  0.033   -2.848  1.00 27.70 ? 624  GLY A C   1 
ATOM   3519 O  O   . GLY A 1 624 ? 11.710  1.035   -2.248  1.00 28.15 ? 624  GLY A O   1 
ATOM   3520 N  N   . VAL A 1 625 ? 12.084  -0.052  -4.176  1.00 26.27 ? 625  VAL A N   1 
ATOM   3521 C  CA  . VAL A 1 625 ? 11.652  1.087   -4.994  1.00 27.23 ? 625  VAL A CA  1 
ATOM   3522 C  C   . VAL A 1 625 ? 10.166  1.423   -4.834  1.00 26.36 ? 625  VAL A C   1 
ATOM   3523 O  O   . VAL A 1 625 ? 9.752   2.545   -5.091  1.00 24.82 ? 625  VAL A O   1 
ATOM   3524 C  CB  . VAL A 1 625 ? 11.964  0.906   -6.500  1.00 27.79 ? 625  VAL A CB  1 
ATOM   3525 C  CG1 . VAL A 1 625 ? 13.460  0.779   -6.727  1.00 27.49 ? 625  VAL A CG1 1 
ATOM   3526 C  CG2 . VAL A 1 625 ? 11.203  -0.272  -7.102  1.00 28.34 ? 625  VAL A CG2 1 
ATOM   3527 N  N   . ALA A 1 626 ? 9.368   0.447   -4.412  1.00 27.01 ? 626  ALA A N   1 
ATOM   3528 C  CA  . ALA A 1 626 ? 7.949   0.665   -4.180  1.00 27.43 ? 626  ALA A CA  1 
ATOM   3529 C  C   . ALA A 1 626 ? 7.668   1.118   -2.739  1.00 29.83 ? 626  ALA A C   1 
ATOM   3530 O  O   . ALA A 1 626 ? 6.500   1.302   -2.362  1.00 28.57 ? 626  ALA A O   1 
ATOM   3531 C  CB  . ALA A 1 626 ? 7.179   -0.598  -4.498  1.00 27.63 ? 626  ALA A CB  1 
ATOM   3532 N  N   . GLY A 1 627 ? 8.730   1.277   -1.945  1.00 31.32 ? 627  GLY A N   1 
ATOM   3533 C  CA  . GLY A 1 627 ? 8.630   1.812   -0.590  1.00 34.23 ? 627  GLY A CA  1 
ATOM   3534 C  C   . GLY A 1 627 ? 9.064   0.843   0.497   1.00 36.64 ? 627  GLY A C   1 
ATOM   3535 O  O   . GLY A 1 627 ? 9.391   -0.318  0.232   1.00 37.82 ? 627  GLY A O   1 
ATOM   3536 N  N   . LYS A 1 628 ? 9.064   1.360   1.722   1.00 39.33 ? 628  LYS A N   1 
ATOM   3537 C  CA  . LYS A 1 628 ? 9.411   0.641   2.955   1.00 42.71 ? 628  LYS A CA  1 
ATOM   3538 C  C   . LYS A 1 628 ? 8.841   -0.782  3.024   1.00 41.31 ? 628  LYS A C   1 
ATOM   3539 O  O   . LYS A 1 628 ? 7.623   -0.961  3.070   1.00 43.82 ? 628  LYS A O   1 
ATOM   3540 C  CB  . LYS A 1 628 ? 8.861   1.464   4.135   1.00 47.76 ? 628  LYS A CB  1 
ATOM   3541 C  CG  . LYS A 1 628 ? 9.239   1.036   5.551   1.00 51.08 ? 628  LYS A CG  1 
ATOM   3542 C  CD  . LYS A 1 628 ? 8.268   1.672   6.555   1.00 54.32 ? 628  LYS A CD  1 
ATOM   3543 C  CE  . LYS A 1 628 ? 8.945   2.265   7.787   1.00 57.44 ? 628  LYS A CE  1 
ATOM   3544 N  NZ  . LYS A 1 628 ? 8.961   1.326   8.944   1.00 59.06 ? 628  LYS A NZ  1 
ATOM   3545 N  N   . GLY A 1 629 ? 9.721   -1.783  3.026   1.00 40.24 ? 629  GLY A N   1 
ATOM   3546 C  CA  . GLY A 1 629 ? 9.322   -3.193  3.201   1.00 39.31 ? 629  GLY A CA  1 
ATOM   3547 C  C   . GLY A 1 629 ? 8.378   -3.779  2.157   1.00 36.78 ? 629  GLY A C   1 
ATOM   3548 O  O   . GLY A 1 629 ? 7.691   -4.775  2.412   1.00 35.12 ? 629  GLY A O   1 
ATOM   3549 N  N   . MET A 1 630 ? 8.336   -3.164  0.981   1.00 36.29 ? 630  MET A N   1 
ATOM   3550 C  CA  . MET A 1 630 ? 7.609   -3.724  -0.155  1.00 35.68 ? 630  MET A CA  1 
ATOM   3551 C  C   . MET A 1 630 ? 8.616   -4.573  -0.906  1.00 33.05 ? 630  MET A C   1 
ATOM   3552 O  O   . MET A 1 630 ? 9.320   -4.099  -1.790  1.00 32.37 ? 630  MET A O   1 
ATOM   3553 C  CB  . MET A 1 630 ? 7.065   -2.614  -1.062  1.00 37.87 ? 630  MET A CB  1 
ATOM   3554 C  CG  . MET A 1 630 ? 6.115   -1.635  -0.392  1.00 39.70 ? 630  MET A CG  1 
ATOM   3555 S  SD  . MET A 1 630 ? 4.620   -2.433  0.206   1.00 43.97 ? 630  MET A SD  1 
ATOM   3556 C  CE  . MET A 1 630 ? 3.540   -1.009  0.395   1.00 42.89 ? 630  MET A CE  1 
ATOM   3557 N  N   . ASP A 1 631 ? 8.719   -5.827  -0.518  1.00 31.26 ? 631  ASP A N   1 
ATOM   3558 C  CA  . ASP A 1 631 ? 9.722   -6.692  -1.104  1.00 30.04 ? 631  ASP A CA  1 
ATOM   3559 C  C   . ASP A 1 631 ? 9.195   -7.219  -2.429  1.00 28.02 ? 631  ASP A C   1 
ATOM   3560 O  O   . ASP A 1 631 ? 7.989   -7.256  -2.654  1.00 27.23 ? 631  ASP A O   1 
ATOM   3561 C  CB  . ASP A 1 631 ? 10.057  -7.857  -0.165  1.00 30.27 ? 631  ASP A CB  1 
ATOM   3562 C  CG  . ASP A 1 631 ? 10.520  -7.389  1.220   1.00 30.90 ? 631  ASP A CG  1 
ATOM   3563 O  OD1 . ASP A 1 631 ? 10.974  -6.222  1.357   1.00 31.92 ? 631  ASP A OD1 1 
ATOM   3564 O  OD2 . ASP A 1 631 ? 10.431  -8.200  2.170   1.00 28.81 ? 631  ASP A OD2 1 
ATOM   3565 N  N   . SER A 1 632 ? 10.115  -7.624  -3.301  1.00 27.72 ? 632  SER A N   1 
ATOM   3566 C  CA  . SER A 1 632 ? 9.767   -8.396  -4.477  1.00 25.94 ? 632  SER A CA  1 
ATOM   3567 C  C   . SER A 1 632 ? 9.212   -9.719  -3.999  1.00 25.82 ? 632  SER A C   1 
ATOM   3568 O  O   . SER A 1 632 ? 9.815   -10.379 -3.167  1.00 27.29 ? 632  SER A O   1 
ATOM   3569 C  CB  . SER A 1 632 ? 10.988  -8.632  -5.369  1.00 25.52 ? 632  SER A CB  1 
ATOM   3570 O  OG  . SER A 1 632 ? 11.482  -7.399  -5.838  1.00 25.14 ? 632  SER A OG  1 
ATOM   3571 N  N   . THR A 1 633 ? 8.061   -10.082 -4.552  1.00 24.56 ? 633  THR A N   1 
ATOM   3572 C  CA  . THR A 1 633 ? 7.286   -11.235 -4.147  1.00 23.04 ? 633  THR A CA  1 
ATOM   3573 C  C   . THR A 1 633 ? 6.815   -11.941 -5.427  1.00 22.80 ? 633  THR A C   1 
ATOM   3574 O  O   . THR A 1 633 ? 7.210   -11.549 -6.535  1.00 22.39 ? 633  THR A O   1 
ATOM   3575 C  CB  . THR A 1 633 ? 6.105   -10.786 -3.250  1.00 21.86 ? 633  THR A CB  1 
ATOM   3576 O  OG1 . THR A 1 633 ? 5.405   -11.924 -2.739  1.00 22.59 ? 633  THR A OG1 1 
ATOM   3577 C  CG2 . THR A 1 633 ? 5.146   -9.862  -4.002  1.00 21.90 ? 633  THR A CG2 1 
ATOM   3578 N  N   . TRP A 1 634 ? 5.998   -12.978 -5.285  1.00 22.56 ? 634  TRP A N   1 
ATOM   3579 C  CA  . TRP A 1 634 ? 5.448   -13.687 -6.451  1.00 22.89 ? 634  TRP A CA  1 
ATOM   3580 C  C   . TRP A 1 634 ? 4.105   -13.097 -6.855  1.00 22.79 ? 634  TRP A C   1 
ATOM   3581 O  O   . TRP A 1 634 ? 3.261   -12.844 -5.997  1.00 23.96 ? 634  TRP A O   1 
ATOM   3582 C  CB  . TRP A 1 634 ? 5.270   -15.179 -6.147  1.00 23.17 ? 634  TRP A CB  1 
ATOM   3583 C  CG  . TRP A 1 634 ? 6.526   -15.967 -6.210  1.00 22.82 ? 634  TRP A CG  1 
ATOM   3584 C  CD1 . TRP A 1 634 ? 7.754   -15.537 -6.633  1.00 23.08 ? 634  TRP A CD1 1 
ATOM   3585 C  CD2 . TRP A 1 634 ? 6.678   -17.347 -5.876  1.00 23.20 ? 634  TRP A CD2 1 
ATOM   3586 N  NE1 . TRP A 1 634 ? 8.665   -16.557 -6.562  1.00 23.64 ? 634  TRP A NE1 1 
ATOM   3587 C  CE2 . TRP A 1 634 ? 8.033   -17.685 -6.106  1.00 23.76 ? 634  TRP A CE2 1 
ATOM   3588 C  CE3 . TRP A 1 634 ? 5.803   -18.333 -5.399  1.00 23.13 ? 634  TRP A CE3 1 
ATOM   3589 C  CZ2 . TRP A 1 634 ? 8.537   -18.966 -5.869  1.00 23.75 ? 634  TRP A CZ2 1 
ATOM   3590 C  CZ3 . TRP A 1 634 ? 6.304   -19.612 -5.158  1.00 23.98 ? 634  TRP A CZ3 1 
ATOM   3591 C  CH2 . TRP A 1 634 ? 7.662   -19.917 -5.401  1.00 24.01 ? 634  TRP A CH2 1 
ATOM   3592 N  N   . ALA A 1 635 ? 3.927   -12.855 -8.156  1.00 21.87 ? 635  ALA A N   1 
ATOM   3593 C  CA  . ALA A 1 635 ? 2.719   -12.269 -8.676  1.00 21.17 ? 635  ALA A CA  1 
ATOM   3594 C  C   . ALA A 1 635 ? 1.611   -13.302 -8.705  1.00 21.46 ? 635  ALA A C   1 
ATOM   3595 O  O   . ALA A 1 635 ? 1.888   -14.505 -8.785  1.00 20.98 ? 635  ALA A O   1 
ATOM   3596 C  CB  . ALA A 1 635 ? 2.944   -11.738 -10.089 1.00 21.82 ? 635  ALA A CB  1 
ATOM   3597 N  N   . PRO A 1 636 ? 0.348   -12.835 -8.662  1.00 20.70 ? 636  PRO A N   1 
ATOM   3598 C  CA  . PRO A 1 636 ? -0.719  -13.713 -9.110  1.00 21.42 ? 636  PRO A CA  1 
ATOM   3599 C  C   . PRO A 1 636 ? -0.403  -14.127 -10.548 1.00 21.51 ? 636  PRO A C   1 
ATOM   3600 O  O   . PRO A 1 636 ? 0.255   -13.380 -11.262 1.00 21.80 ? 636  PRO A O   1 
ATOM   3601 C  CB  . PRO A 1 636 ? -1.982  -12.825 -9.066  1.00 21.22 ? 636  PRO A CB  1 
ATOM   3602 C  CG  . PRO A 1 636 ? -1.593  -11.576 -8.372  1.00 21.38 ? 636  PRO A CG  1 
ATOM   3603 C  CD  . PRO A 1 636 ? -0.102  -11.443 -8.498  1.00 21.16 ? 636  PRO A CD  1 
ATOM   3604 N  N   . SER A 1 637 ? -0.847  -15.306 -10.950 1.00 20.79 ? 637  SER A N   1 
ATOM   3605 C  CA  . SER A 1 637 ? -0.570  -15.801 -12.270 1.00 20.60 ? 637  SER A CA  1 
ATOM   3606 C  C   . SER A 1 637 ? -1.809  -15.598 -13.094 1.00 20.63 ? 637  SER A C   1 
ATOM   3607 O  O   . SER A 1 637 ? -2.902  -15.433 -12.535 1.00 20.93 ? 637  SER A O   1 
ATOM   3608 C  CB  . SER A 1 637 ? -0.179  -17.267 -12.213 1.00 20.70 ? 637  SER A CB  1 
ATOM   3609 O  OG  . SER A 1 637 ? 0.948   -17.412 -11.380 1.00 20.70 ? 637  SER A OG  1 
ATOM   3610 N  N   . PHE A 1 638 ? -1.652  -15.563 -14.414 1.00 19.47 ? 638  PHE A N   1 
ATOM   3611 C  CA  . PHE A 1 638 ? -2.811  -15.400 -15.283 1.00 19.72 ? 638  PHE A CA  1 
ATOM   3612 C  C   . PHE A 1 638 ? -2.707  -16.220 -16.548 1.00 18.98 ? 638  PHE A C   1 
ATOM   3613 O  O   . PHE A 1 638 ? -1.612  -16.530 -16.993 1.00 19.22 ? 638  PHE A O   1 
ATOM   3614 C  CB  . PHE A 1 638 ? -3.047  -13.912 -15.595 1.00 20.23 ? 638  PHE A CB  1 
ATOM   3615 C  CG  . PHE A 1 638 ? -1.924  -13.251 -16.345 1.00 21.23 ? 638  PHE A CG  1 
ATOM   3616 C  CD1 . PHE A 1 638 ? -0.890  -12.626 -15.667 1.00 20.73 ? 638  PHE A CD1 1 
ATOM   3617 C  CD2 . PHE A 1 638 ? -1.923  -13.229 -17.739 1.00 21.53 ? 638  PHE A CD2 1 
ATOM   3618 C  CE1 . PHE A 1 638 ? 0.135   -12.005 -16.358 1.00 21.85 ? 638  PHE A CE1 1 
ATOM   3619 C  CE2 . PHE A 1 638 ? -0.902  -12.601 -18.431 1.00 21.47 ? 638  PHE A CE2 1 
ATOM   3620 C  CZ  . PHE A 1 638 ? 0.121   -11.987 -17.744 1.00 21.50 ? 638  PHE A CZ  1 
ATOM   3621 N  N   . LEU A 1 639 ? -3.853  -16.565 -17.133 1.00 18.73 ? 639  LEU A N   1 
ATOM   3622 C  CA  . LEU A 1 639 ? -3.863  -17.374 -18.354 1.00 19.01 ? 639  LEU A CA  1 
ATOM   3623 C  C   . LEU A 1 639 ? -3.667  -16.515 -19.602 1.00 18.80 ? 639  LEU A C   1 
ATOM   3624 O  O   . LEU A 1 639 ? -4.160  -15.381 -19.685 1.00 19.12 ? 639  LEU A O   1 
ATOM   3625 C  CB  . LEU A 1 639 ? -5.156  -18.194 -18.480 1.00 18.60 ? 639  LEU A CB  1 
ATOM   3626 C  CG  . LEU A 1 639 ? -5.326  -19.385 -17.533 1.00 18.55 ? 639  LEU A CG  1 
ATOM   3627 C  CD1 . LEU A 1 639 ? -6.689  -20.028 -17.770 1.00 19.31 ? 639  LEU A CD1 1 
ATOM   3628 C  CD2 . LEU A 1 639 ? -4.215  -20.409 -17.709 1.00 18.77 ? 639  LEU A CD2 1 
ATOM   3629 N  N   . LEU A 1 640 ? -2.929  -17.079 -20.548 1.00 19.14 ? 640  LEU A N   1 
ATOM   3630 C  CA  . LEU A 1 640 ? -2.665  -16.479 -21.845 1.00 20.00 ? 640  LEU A CA  1 
ATOM   3631 C  C   . LEU A 1 640 ? -3.117  -17.493 -22.875 1.00 19.83 ? 640  LEU A C   1 
ATOM   3632 O  O   . LEU A 1 640 ? -2.643  -18.624 -22.882 1.00 20.24 ? 640  LEU A O   1 
ATOM   3633 C  CB  . LEU A 1 640 ? -1.166  -16.202 -22.021 1.00 19.74 ? 640  LEU A CB  1 
ATOM   3634 C  CG  . LEU A 1 640 ? -0.662  -15.746 -23.396 1.00 19.58 ? 640  LEU A CG  1 
ATOM   3635 C  CD1 . LEU A 1 640 ? -1.226  -14.380 -23.767 1.00 19.94 ? 640  LEU A CD1 1 
ATOM   3636 C  CD2 . LEU A 1 640 ? 0.855   -15.682 -23.389 1.00 19.95 ? 640  LEU A CD2 1 
ATOM   3637 N  N   . GLN A 1 641 ? -4.023  -17.088 -23.753 1.00 20.19 ? 641  GLN A N   1 
ATOM   3638 C  CA  . GLN A 1 641 ? -4.533  -17.996 -24.773 1.00 20.82 ? 641  GLN A CA  1 
ATOM   3639 C  C   . GLN A 1 641 ? -3.615  -17.933 -25.959 1.00 20.33 ? 641  GLN A C   1 
ATOM   3640 O  O   . GLN A 1 641 ? -3.277  -16.844 -26.419 1.00 19.81 ? 641  GLN A O   1 
ATOM   3641 C  CB  . GLN A 1 641 ? -5.956  -17.605 -25.185 1.00 21.39 ? 641  GLN A CB  1 
ATOM   3642 C  CG  . GLN A 1 641 ? -6.618  -18.530 -26.185 1.00 22.12 ? 641  GLN A CG  1 
ATOM   3643 C  CD  . GLN A 1 641 ? -8.094  -18.187 -26.370 1.00 23.63 ? 641  GLN A CD  1 
ATOM   3644 O  OE1 . GLN A 1 641 ? -8.925  -18.517 -25.529 1.00 24.43 ? 641  GLN A OE1 1 
ATOM   3645 N  NE2 . GLN A 1 641 ? -8.416  -17.501 -27.460 1.00 24.77 ? 641  GLN A NE2 1 
ATOM   3646 N  N   . ILE A 1 642 ? -3.237  -19.101 -26.455 1.00 20.42 ? 642  ILE A N   1 
ATOM   3647 C  CA  . ILE A 1 642 ? -2.466  -19.217 -27.678 1.00 21.73 ? 642  ILE A CA  1 
ATOM   3648 C  C   . ILE A 1 642 ? -3.388  -19.659 -28.814 1.00 22.28 ? 642  ILE A C   1 
ATOM   3649 O  O   . ILE A 1 642 ? -3.995  -20.735 -28.754 1.00 20.99 ? 642  ILE A O   1 
ATOM   3650 C  CB  . ILE A 1 642 ? -1.315  -20.247 -27.529 1.00 22.30 ? 642  ILE A CB  1 
ATOM   3651 C  CG1 . ILE A 1 642 ? -0.492  -19.992 -26.258 1.00 21.85 ? 642  ILE A CG1 1 
ATOM   3652 C  CG2 . ILE A 1 642 ? -0.423  -20.230 -28.760 1.00 22.90 ? 642  ILE A CG2 1 
ATOM   3653 C  CD1 . ILE A 1 642 ? 0.108   -18.613 -26.178 1.00 22.21 ? 642  ILE A CD1 1 
ATOM   3654 N  N   . ASN A 1 643 ? -3.476  -18.821 -29.847 1.00 22.89 ? 643  ASN A N   1 
ATOM   3655 C  CA  . ASN A 1 643 ? -4.373  -19.060 -30.969 1.00 23.21 ? 643  ASN A CA  1 
ATOM   3656 C  C   . ASN A 1 643 ? -3.644  -19.732 -32.098 1.00 22.88 ? 643  ASN A C   1 
ATOM   3657 O  O   . ASN A 1 643 ? -2.447  -19.523 -32.279 1.00 23.77 ? 643  ASN A O   1 
ATOM   3658 C  CB  . ASN A 1 643 ? -4.978  -17.741 -31.458 1.00 23.44 ? 643  ASN A CB  1 
ATOM   3659 C  CG  . ASN A 1 643 ? -5.665  -16.994 -30.348 1.00 23.73 ? 643  ASN A CG  1 
ATOM   3660 O  OD1 . ASN A 1 643 ? -6.300  -17.612 -29.490 1.00 25.28 ? 643  ASN A OD1 1 
ATOM   3661 N  ND2 . ASN A 1 643 ? -5.509  -15.673 -30.318 1.00 22.95 ? 643  ASN A ND2 1 
ATOM   3662 N  N   . PRO A 1 644 ? -4.368  -20.520 -32.900 1.00 22.21 ? 644  PRO A N   1 
ATOM   3663 C  CA  . PRO A 1 644 ? -3.676  -21.296 -33.931 1.00 21.15 ? 644  PRO A CA  1 
ATOM   3664 C  C   . PRO A 1 644 ? -3.095  -20.479 -35.092 1.00 19.67 ? 644  PRO A C   1 
ATOM   3665 O  O   . PRO A 1 644 ? -2.387  -21.035 -35.903 1.00 19.61 ? 644  PRO A O   1 
ATOM   3666 C  CB  . PRO A 1 644 ? -4.752  -22.276 -34.441 1.00 22.11 ? 644  PRO A CB  1 
ATOM   3667 C  CG  . PRO A 1 644 ? -6.026  -21.880 -33.823 1.00 22.95 ? 644  PRO A CG  1 
ATOM   3668 C  CD  . PRO A 1 644 ? -5.826  -20.719 -32.901 1.00 22.73 ? 644  PRO A CD  1 
ATOM   3669 N  N   . ASP A 1 645 ? -3.386  -19.185 -35.171 1.00 18.94 ? 645  ASP A N   1 
ATOM   3670 C  CA  . ASP A 1 645 ? -2.919  -18.354 -36.281 1.00 18.00 ? 645  ASP A CA  1 
ATOM   3671 C  C   . ASP A 1 645 ? -1.727  -17.490 -35.836 1.00 17.59 ? 645  ASP A C   1 
ATOM   3672 O  O   . ASP A 1 645 ? -1.509  -16.395 -36.368 1.00 16.88 ? 645  ASP A O   1 
ATOM   3673 C  CB  . ASP A 1 645 ? -4.083  -17.492 -36.825 1.00 18.23 ? 645  ASP A CB  1 
ATOM   3674 C  CG  . ASP A 1 645 ? -4.496  -16.400 -35.871 1.00 17.74 ? 645  ASP A CG  1 
ATOM   3675 O  OD1 . ASP A 1 645 ? -4.280  -16.570 -34.657 1.00 18.82 ? 645  ASP A OD1 1 
ATOM   3676 O  OD2 . ASP A 1 645 ? -5.000  -15.363 -36.322 1.00 17.17 ? 645  ASP A OD2 1 
ATOM   3677 N  N   . ASN A 1 646 ? -0.937  -18.004 -34.886 1.00 17.47 ? 646  ASN A N   1 
ATOM   3678 C  CA  . ASN A 1 646 ? 0.259   -17.324 -34.414 1.00 18.30 ? 646  ASN A CA  1 
ATOM   3679 C  C   . ASN A 1 646 ? -0.070  -15.955 -33.801 1.00 17.85 ? 646  ASN A C   1 
ATOM   3680 O  O   . ASN A 1 646 ? 0.627   -14.955 -34.041 1.00 16.99 ? 646  ASN A O   1 
ATOM   3681 C  CB  . ASN A 1 646 ? 1.293   -17.177 -35.555 1.00 20.02 ? 646  ASN A CB  1 
ATOM   3682 C  CG  . ASN A 1 646 ? 1.728   -18.521 -36.134 1.00 21.29 ? 646  ASN A CG  1 
ATOM   3683 O  OD1 . ASN A 1 646 ? 1.603   -19.541 -35.509 1.00 22.62 ? 646  ASN A OD1 1 
ATOM   3684 N  ND2 . ASN A 1 646 ? 2.233   -18.504 -37.328 1.00 23.56 ? 646  ASN A ND2 1 
ATOM   3685 N  N   . THR A 1 647 ? -1.166  -15.923 -33.052 1.00 17.51 ? 647  THR A N   1 
ATOM   3686 C  CA  . THR A 1 647 ? -1.502  -14.803 -32.184 1.00 17.58 ? 647  THR A CA  1 
ATOM   3687 C  C   . THR A 1 647 ? -1.797  -15.313 -30.799 1.00 17.56 ? 647  THR A C   1 
ATOM   3688 O  O   . THR A 1 647 ? -1.936  -16.519 -30.567 1.00 17.05 ? 647  THR A O   1 
ATOM   3689 C  CB  . THR A 1 647 ? -2.744  -13.998 -32.662 1.00 16.64 ? 647  THR A CB  1 
ATOM   3690 O  OG1 . THR A 1 647 ? -3.900  -14.835 -32.662 1.00 16.29 ? 647  THR A OG1 1 
ATOM   3691 C  CG2 . THR A 1 647 ? -2.524  -13.434 -34.061 1.00 17.06 ? 647  THR A CG2 1 
ATOM   3692 N  N   . THR A 1 648 ? -1.915  -14.368 -29.877 1.00 18.78 ? 648  THR A N   1 
ATOM   3693 C  CA  . THR A 1 648 ? -2.214  -14.673 -28.495 1.00 20.13 ? 648  THR A CA  1 
ATOM   3694 C  C   . THR A 1 648 ? -3.202  -13.651 -27.966 1.00 20.06 ? 648  THR A C   1 
ATOM   3695 O  O   . THR A 1 648 ? -3.345  -12.559 -28.518 1.00 20.31 ? 648  THR A O   1 
ATOM   3696 C  CB  . THR A 1 648 ? -0.937  -14.605 -27.614 1.00 20.27 ? 648  THR A CB  1 
ATOM   3697 O  OG1 . THR A 1 648 ? -0.440  -13.256 -27.588 1.00 19.51 ? 648  THR A OG1 1 
ATOM   3698 C  CG2 . THR A 1 648 ? 0.135   -15.526 -28.151 1.00 20.46 ? 648  THR A CG2 1 
ATOM   3699 N  N   . THR A 1 649 ? -3.841  -14.011 -26.869 1.00 20.48 ? 649  THR A N   1 
ATOM   3700 C  CA  . THR A 1 649 ? -4.810  -13.159 -26.206 1.00 21.75 ? 649  THR A CA  1 
ATOM   3701 C  C   . THR A 1 649 ? -4.742  -13.363 -24.710 1.00 21.17 ? 649  THR A C   1 
ATOM   3702 O  O   . THR A 1 649 ? -4.891  -14.476 -24.228 1.00 21.80 ? 649  THR A O   1 
ATOM   3703 C  CB  . THR A 1 649 ? -6.248  -13.487 -26.648 1.00 22.84 ? 649  THR A CB  1 
ATOM   3704 O  OG1 . THR A 1 649 ? -6.304  -13.549 -28.076 1.00 23.94 ? 649  THR A OG1 1 
ATOM   3705 C  CG2 . THR A 1 649 ? -7.230  -12.412 -26.127 1.00 22.97 ? 649  THR A CG2 1 
ATOM   3706 N  N   . VAL A 1 650 ? -4.546  -12.280 -23.976 1.00 21.34 ? 650  VAL A N   1 
ATOM   3707 C  CA  . VAL A 1 650 ? -4.593  -12.323 -22.527 1.00 21.76 ? 650  VAL A CA  1 
ATOM   3708 C  C   . VAL A 1 650 ? -6.027  -12.634 -22.048 1.00 22.73 ? 650  VAL A C   1 
ATOM   3709 O  O   . VAL A 1 650 ? -6.993  -12.055 -22.547 1.00 20.91 ? 650  VAL A O   1 
ATOM   3710 C  CB  . VAL A 1 650 ? -4.114  -10.992 -21.940 1.00 22.22 ? 650  VAL A CB  1 
ATOM   3711 C  CG1 . VAL A 1 650 ? -4.385  -10.916 -20.440 1.00 21.99 ? 650  VAL A CG1 1 
ATOM   3712 C  CG2 . VAL A 1 650 ? -2.629  -10.787 -22.248 1.00 22.34 ? 650  VAL A CG2 1 
ATOM   3713 N  N   . LEU A 1 651 ? -6.151  -13.564 -21.099 1.00 23.08 ? 651  LEU A N   1 
ATOM   3714 C  CA  . LEU A 1 651 ? -7.446  -13.900 -20.522 1.00 23.98 ? 651  LEU A CA  1 
ATOM   3715 C  C   . LEU A 1 651 ? -7.598  -13.277 -19.134 1.00 24.88 ? 651  LEU A C   1 
ATOM   3716 O  O   . LEU A 1 651 ? -6.618  -13.108 -18.399 1.00 25.04 ? 651  LEU A O   1 
ATOM   3717 C  CB  . LEU A 1 651 ? -7.632  -15.419 -20.439 1.00 24.10 ? 651  LEU A CB  1 
ATOM   3718 C  CG  . LEU A 1 651 ? -7.509  -16.191 -21.754 1.00 24.07 ? 651  LEU A CG  1 
ATOM   3719 C  CD1 . LEU A 1 651 ? -7.762  -17.677 -21.526 1.00 24.57 ? 651  LEU A CD1 1 
ATOM   3720 C  CD2 . LEU A 1 651 ? -8.468  -15.655 -22.812 1.00 24.23 ? 651  LEU A CD2 1 
ATOM   3721 N  N   . ALA A 1 652 ? -8.839  -12.944 -18.795 1.00 25.50 ? 652  ALA A N   1 
ATOM   3722 C  CA  . ALA A 1 652 ? -9.208  -12.425 -17.479 1.00 27.85 ? 652  ALA A CA  1 
ATOM   3723 C  C   . ALA A 1 652 ? -9.421  -13.590 -16.500 1.00 28.37 ? 652  ALA A C   1 
ATOM   3724 O  O   . ALA A 1 652 ? -10.499 -13.743 -15.928 1.00 28.86 ? 652  ALA A O   1 
ATOM   3725 C  CB  . ALA A 1 652 ? -10.478 -11.586 -17.592 1.00 27.75 ? 652  ALA A CB  1 
ATOM   3726 N  N   . LYS A 1 653 ? -8.376  -14.392 -16.334 1.00 27.54 ? 653  LYS A N   1 
ATOM   3727 C  CA  . LYS A 1 653 ? -8.389  -15.589 -15.518 1.00 28.20 ? 653  LYS A CA  1 
ATOM   3728 C  C   . LYS A 1 653 ? -7.115  -15.542 -14.682 1.00 26.40 ? 653  LYS A C   1 
ATOM   3729 O  O   . LYS A 1 653 ? -6.022  -15.647 -15.233 1.00 25.98 ? 653  LYS A O   1 
ATOM   3730 C  CB  . LYS A 1 653 ? -8.344  -16.830 -16.403 1.00 31.22 ? 653  LYS A CB  1 
ATOM   3731 C  CG  . LYS A 1 653 ? -9.516  -17.014 -17.347 1.00 33.56 ? 653  LYS A CG  1 
ATOM   3732 C  CD  . LYS A 1 653 ? -10.795 -17.292 -16.589 1.00 36.79 ? 653  LYS A CD  1 
ATOM   3733 C  CE  . LYS A 1 653 ? -11.489 -18.550 -17.082 1.00 39.46 ? 653  LYS A CE  1 
ATOM   3734 N  NZ  . LYS A 1 653 ? -12.917 -18.530 -16.656 1.00 40.88 ? 653  LYS A NZ  1 
ATOM   3735 N  N   . MET A 1 654 ? -7.255  -15.384 -13.369 1.00 24.19 ? 654  MET A N   1 
ATOM   3736 C  CA  . MET A 1 654 ? -6.136  -15.085 -12.486 1.00 23.80 ? 654  MET A CA  1 
ATOM   3737 C  C   . MET A 1 654 ? -6.128  -16.014 -11.269 1.00 23.37 ? 654  MET A C   1 
ATOM   3738 O  O   . MET A 1 654 ? -7.192  -16.495 -10.834 1.00 21.35 ? 654  MET A O   1 
ATOM   3739 C  CB  . MET A 1 654 ? -6.231  -13.623 -12.038 1.00 24.59 ? 654  MET A CB  1 
ATOM   3740 C  CG  . MET A 1 654 ? -4.999  -13.100 -11.311 1.00 25.12 ? 654  MET A CG  1 
ATOM   3741 S  SD  . MET A 1 654 ? -5.034  -11.331 -10.978 1.00 26.34 ? 654  MET A SD  1 
ATOM   3742 C  CE  . MET A 1 654 ? -4.964  -10.686 -12.651 1.00 26.39 ? 654  MET A CE  1 
ATOM   3743 N  N   . THR A 1 655 ? -4.936  -16.249 -10.711 1.00 22.86 ? 655  THR A N   1 
ATOM   3744 C  CA  . THR A 1 655 ? -4.786  -17.101 -9.537  1.00 23.04 ? 655  THR A CA  1 
ATOM   3745 C  C   . THR A 1 655 ? -4.429  -16.258 -8.325  1.00 24.26 ? 655  THR A C   1 
ATOM   3746 O  O   . THR A 1 655 ? -4.293  -15.029 -8.431  1.00 22.45 ? 655  THR A O   1 
ATOM   3747 C  CB  . THR A 1 655 ? -3.653  -18.116 -9.727  1.00 22.94 ? 655  THR A CB  1 
ATOM   3748 O  OG1 . THR A 1 655 ? -2.396  -17.423 -9.777  1.00 22.19 ? 655  THR A OG1 1 
ATOM   3749 C  CG2 . THR A 1 655 ? -3.853  -18.912 -10.989 1.00 23.15 ? 655  THR A CG2 1 
ATOM   3750 N  N   . ASN A 1 656 ? -4.272  -16.932 -7.178  1.00 24.30 ? 656  ASN A N   1 
ATOM   3751 C  CA  . ASN A 1 656 ? -3.535  -16.385 -6.028  1.00 25.06 ? 656  ASN A CA  1 
ATOM   3752 C  C   . ASN A 1 656 ? -2.095  -16.080 -6.413  1.00 24.81 ? 656  ASN A C   1 
ATOM   3753 O  O   . ASN A 1 656 ? -1.599  -16.584 -7.425  1.00 23.68 ? 656  ASN A O   1 
ATOM   3754 C  CB  . ASN A 1 656 ? -3.453  -17.405 -4.872  1.00 26.72 ? 656  ASN A CB  1 
ATOM   3755 C  CG  . ASN A 1 656 ? -4.783  -17.632 -4.174  1.00 27.12 ? 656  ASN A CG  1 
ATOM   3756 O  OD1 . ASN A 1 656 ? -5.674  -16.796 -4.198  1.00 26.57 ? 656  ASN A OD1 1 
ATOM   3757 N  ND2 . ASN A 1 656 ? -4.905  -18.780 -3.532  1.00 28.93 ? 656  ASN A ND2 1 
ATOM   3758 N  N   . GLN A 1 657 ? -1.418  -15.292 -5.579  1.00 24.23 ? 657  GLN A N   1 
ATOM   3759 C  CA  . GLN A 1 657 ? -0.003  -15.029 -5.758  1.00 24.61 ? 657  GLN A CA  1 
ATOM   3760 C  C   . GLN A 1 657 ? 0.752   -16.359 -5.734  1.00 24.97 ? 657  GLN A C   1 
ATOM   3761 O  O   . GLN A 1 657 ? 0.536   -17.198 -4.854  1.00 23.66 ? 657  GLN A O   1 
ATOM   3762 C  CB  . GLN A 1 657 ? 0.543   -14.149 -4.635  1.00 24.99 ? 657  GLN A CB  1 
ATOM   3763 C  CG  . GLN A 1 657 ? 0.018   -12.725 -4.579  1.00 24.55 ? 657  GLN A CG  1 
ATOM   3764 C  CD  . GLN A 1 657 ? 0.692   -11.925 -3.486  1.00 24.97 ? 657  GLN A CD  1 
ATOM   3765 O  OE1 . GLN A 1 657 ? 0.062   -11.539 -2.499  1.00 27.34 ? 657  GLN A OE1 1 
ATOM   3766 N  NE2 . GLN A 1 657 ? 1.985   -11.671 -3.646  1.00 25.49 ? 657  GLN A NE2 1 
ATOM   3767 N  N   . GLY A 1 658 ? 1.619   -16.565 -6.712  1.00 24.06 ? 658  GLY A N   1 
ATOM   3768 C  CA  . GLY A 1 658 ? 2.595   -17.634 -6.607  1.00 23.69 ? 658  GLY A CA  1 
ATOM   3769 C  C   . GLY A 1 658 ? 2.076   -18.993 -6.985  1.00 23.72 ? 658  GLY A C   1 
ATOM   3770 O  O   . GLY A 1 658 ? 2.646   -20.005 -6.583  1.00 23.19 ? 658  GLY A O   1 
ATOM   3771 N  N   . ASP A 1 659 ? 1.005   -19.019 -7.777  1.00 24.19 ? 659  ASP A N   1 
ATOM   3772 C  CA  . ASP A 1 659 ? 0.407   -20.275 -8.244  1.00 23.22 ? 659  ASP A CA  1 
ATOM   3773 C  C   . ASP A 1 659 ? 1.047   -20.687 -9.583  1.00 23.60 ? 659  ASP A C   1 
ATOM   3774 O  O   . ASP A 1 659 ? 0.999   -19.929 -10.570 1.00 23.38 ? 659  ASP A O   1 
ATOM   3775 C  CB  . ASP A 1 659 ? -1.095  -20.057 -8.378  1.00 22.95 ? 659  ASP A CB  1 
ATOM   3776 C  CG  . ASP A 1 659 ? -1.881  -21.338 -8.561  1.00 22.65 ? 659  ASP A CG  1 
ATOM   3777 O  OD1 . ASP A 1 659 ? -1.314  -22.385 -8.887  1.00 22.49 ? 659  ASP A OD1 1 
ATOM   3778 O  OD2 . ASP A 1 659 ? -3.120  -21.277 -8.397  1.00 24.03 ? 659  ASP A OD2 1 
ATOM   3779 N  N   . TRP A 1 660 ? 1.636   -21.880 -9.610  1.00 22.31 ? 660  TRP A N   1 
ATOM   3780 C  CA  . TRP A 1 660 ? 2.346   -22.392 -10.779 1.00 23.23 ? 660  TRP A CA  1 
ATOM   3781 C  C   . TRP A 1 660 ? 1.563   -23.459 -11.529 1.00 24.48 ? 660  TRP A C   1 
ATOM   3782 O  O   . TRP A 1 660 ? 2.012   -23.929 -12.573 1.00 25.85 ? 660  TRP A O   1 
ATOM   3783 C  CB  . TRP A 1 660 ? 3.693   -22.995 -10.356 1.00 24.03 ? 660  TRP A CB  1 
ATOM   3784 C  CG  . TRP A 1 660 ? 4.622   -21.993 -9.765  1.00 23.68 ? 660  TRP A CG  1 
ATOM   3785 C  CD1 . TRP A 1 660 ? 4.629   -21.553 -8.480  1.00 23.10 ? 660  TRP A CD1 1 
ATOM   3786 C  CD2 . TRP A 1 660 ? 5.678   -21.300 -10.433 1.00 23.64 ? 660  TRP A CD2 1 
ATOM   3787 N  NE1 . TRP A 1 660 ? 5.613   -20.621 -8.303  1.00 23.54 ? 660  TRP A NE1 1 
ATOM   3788 C  CE2 . TRP A 1 660 ? 6.277   -20.444 -9.485  1.00 23.64 ? 660  TRP A CE2 1 
ATOM   3789 C  CE3 . TRP A 1 660 ? 6.161   -21.298 -11.742 1.00 23.98 ? 660  TRP A CE3 1 
ATOM   3790 C  CZ2 . TRP A 1 660 ? 7.339   -19.602 -9.800  1.00 23.30 ? 660  TRP A CZ2 1 
ATOM   3791 C  CZ3 . TRP A 1 660 ? 7.228   -20.465 -12.051 1.00 23.52 ? 660  TRP A CZ3 1 
ATOM   3792 C  CH2 . TRP A 1 660 ? 7.800   -19.630 -11.084 1.00 23.47 ? 660  TRP A CH2 1 
ATOM   3793 N  N   . ILE A 1 661 ? 0.405   -23.851 -10.994 1.00 24.86 ? 661  ILE A N   1 
ATOM   3794 C  CA  . ILE A 1 661 ? -0.363  -24.968 -11.523 1.00 24.08 ? 661  ILE A CA  1 
ATOM   3795 C  C   . ILE A 1 661 ? -1.814  -24.541 -11.666 1.00 24.25 ? 661  ILE A C   1 
ATOM   3796 O  O   . ILE A 1 661 ? -2.543  -24.480 -10.678 1.00 23.24 ? 661  ILE A O   1 
ATOM   3797 C  CB  . ILE A 1 661 ? -0.316  -26.201 -10.568 1.00 23.63 ? 661  ILE A CB  1 
ATOM   3798 C  CG1 . ILE A 1 661 ? 1.127   -26.618 -10.270 1.00 24.04 ? 661  ILE A CG1 1 
ATOM   3799 C  CG2 . ILE A 1 661 ? -1.094  -27.376 -11.172 1.00 22.91 ? 661  ILE A CG2 1 
ATOM   3800 C  CD1 . ILE A 1 661 ? 1.274   -27.454 -9.016  1.00 24.41 ? 661  ILE A CD1 1 
ATOM   3801 N  N   . TRP A 1 662 ? -2.246  -24.259 -12.889 1.00 24.06 ? 662  TRP A N   1 
ATOM   3802 C  CA  . TRP A 1 662 ? -3.622  -23.860 -13.104 1.00 24.70 ? 662  TRP A CA  1 
ATOM   3803 C  C   . TRP A 1 662 ? -4.515  -25.100 -13.103 1.00 25.47 ? 662  TRP A C   1 
ATOM   3804 O  O   . TRP A 1 662 ? -4.176  -26.114 -13.702 1.00 23.20 ? 662  TRP A O   1 
ATOM   3805 C  CB  . TRP A 1 662 ? -3.810  -23.115 -14.424 1.00 25.04 ? 662  TRP A CB  1 
ATOM   3806 C  CG  . TRP A 1 662 ? -5.271  -22.882 -14.718 1.00 24.47 ? 662  TRP A CG  1 
ATOM   3807 C  CD1 . TRP A 1 662 ? -6.129  -23.743 -15.355 1.00 23.91 ? 662  TRP A CD1 1 
ATOM   3808 C  CD2 . TRP A 1 662 ? -6.055  -21.748 -14.336 1.00 23.91 ? 662  TRP A CD2 1 
ATOM   3809 N  NE1 . TRP A 1 662 ? -7.391  -23.203 -15.393 1.00 24.05 ? 662  TRP A NE1 1 
ATOM   3810 C  CE2 . TRP A 1 662 ? -7.375  -21.983 -14.778 1.00 23.60 ? 662  TRP A CE2 1 
ATOM   3811 C  CE3 . TRP A 1 662 ? -5.771  -20.556 -13.670 1.00 23.89 ? 662  TRP A CE3 1 
ATOM   3812 C  CZ2 . TRP A 1 662 ? -8.401  -21.067 -14.589 1.00 23.98 ? 662  TRP A CZ2 1 
ATOM   3813 C  CZ3 . TRP A 1 662 ? -6.790  -19.649 -13.474 1.00 23.90 ? 662  TRP A CZ3 1 
ATOM   3814 C  CH2 . TRP A 1 662 ? -8.096  -19.912 -13.934 1.00 23.94 ? 662  TRP A CH2 1 
ATOM   3815 N  N   . ASP A 1 663 ? -5.645  -25.001 -12.411 1.00 27.42 ? 663  ASP A N   1 
ATOM   3816 C  CA  . ASP A 1 663 ? -6.768  -25.935 -12.590 1.00 30.10 ? 663  ASP A CA  1 
ATOM   3817 C  C   . ASP A 1 663 ? -8.040  -25.162 -12.275 1.00 33.08 ? 663  ASP A C   1 
ATOM   3818 O  O   . ASP A 1 663 ? -7.978  -23.947 -12.004 1.00 35.27 ? 663  ASP A O   1 
ATOM   3819 C  CB  . ASP A 1 663 ? -6.598  -27.199 -11.732 1.00 29.19 ? 663  ASP A CB  1 
ATOM   3820 C  CG  . ASP A 1 663 ? -6.309  -26.889 -10.277 1.00 28.62 ? 663  ASP A CG  1 
ATOM   3821 O  OD1 . ASP A 1 663 ? -6.900  -25.937 -9.730  1.00 27.64 ? 663  ASP A OD1 1 
ATOM   3822 O  OD2 . ASP A 1 663 ? -5.475  -27.596 -9.680  1.00 29.83 ? 663  ASP A OD2 1 
ATOM   3823 N  N   . ASP A 1 664 ? -9.186  -25.833 -12.325 1.00 37.43 ? 664  ASP A N   1 
ATOM   3824 C  CA  . ASP A 1 664 ? -10.478 -25.178 -12.062 1.00 40.99 ? 664  ASP A CA  1 
ATOM   3825 C  C   . ASP A 1 664 ? -10.546 -24.512 -10.692 1.00 40.39 ? 664  ASP A C   1 
ATOM   3826 O  O   . ASP A 1 664 ? -11.096 -23.418 -10.543 1.00 43.44 ? 664  ASP A O   1 
ATOM   3827 C  CB  . ASP A 1 664 ? -11.618 -26.196 -12.166 1.00 44.97 ? 664  ASP A CB  1 
ATOM   3828 C  CG  . ASP A 1 664 ? -11.902 -26.614 -13.596 1.00 45.97 ? 664  ASP A CG  1 
ATOM   3829 O  OD1 . ASP A 1 664 ? -11.499 -25.892 -14.536 1.00 45.09 ? 664  ASP A OD1 1 
ATOM   3830 O  OD2 . ASP A 1 664 ? -12.540 -27.674 -13.771 1.00 48.33 ? 664  ASP A OD2 1 
ATOM   3831 N  N   . SER A 1 665 ? -9.961  -25.163 -9.697  1.00 36.70 ? 665  SER A N   1 
ATOM   3832 C  CA  . SER A 1 665 ? -10.017 -24.656 -8.338  1.00 36.12 ? 665  SER A CA  1 
ATOM   3833 C  C   . SER A 1 665 ? -9.017  -23.525 -8.059  1.00 34.08 ? 665  SER A C   1 
ATOM   3834 O  O   . SER A 1 665 ? -9.055  -22.934 -6.986  1.00 32.91 ? 665  SER A O   1 
ATOM   3835 C  CB  . SER A 1 665 ? -9.774  -25.803 -7.361  1.00 34.82 ? 665  SER A CB  1 
ATOM   3836 O  OG  . SER A 1 665 ? -8.432  -26.238 -7.438  1.00 37.95 ? 665  SER A OG  1 
ATOM   3837 N  N   . SER A 1 666 ? -8.114  -23.236 -8.997  1.00 31.65 ? 666  SER A N   1 
ATOM   3838 C  CA  . SER A 1 666 ? -7.056  -22.252 -8.743  1.00 29.47 ? 666  SER A CA  1 
ATOM   3839 C  C   . SER A 1 666 ? -7.507  -20.815 -8.994  1.00 29.22 ? 666  SER A C   1 
ATOM   3840 O  O   . SER A 1 666 ? -6.845  -19.879 -8.551  1.00 28.03 ? 666  SER A O   1 
ATOM   3841 C  CB  . SER A 1 666 ? -5.820  -22.538 -9.609  1.00 29.56 ? 666  SER A CB  1 
ATOM   3842 O  OG  . SER A 1 666 ? -5.186  -23.771 -9.295  1.00 27.78 ? 666  SER A OG  1 
ATOM   3843 N  N   . GLU A 1 667 ? -8.622  -20.622 -9.696  1.00 30.38 ? 667  GLU A N   1 
ATOM   3844 C  CA  . GLU A 1 667 ? -9.046  -19.272 -10.063 1.00 31.37 ? 667  GLU A CA  1 
ATOM   3845 C  C   . GLU A 1 667 ? -9.455  -18.427 -8.867  1.00 32.51 ? 667  GLU A C   1 
ATOM   3846 O  O   . GLU A 1 667 ? -10.193 -18.891 -8.009  1.00 32.94 ? 667  GLU A O   1 
ATOM   3847 C  CB  . GLU A 1 667 ? -10.213 -19.313 -11.033 1.00 32.76 ? 667  GLU A CB  1 
ATOM   3848 C  CG  . GLU A 1 667 ? -10.640 -17.931 -11.506 1.00 33.15 ? 667  GLU A CG  1 
ATOM   3849 C  CD  . GLU A 1 667 ? -11.454 -17.988 -12.777 1.00 34.64 ? 667  GLU A CD  1 
ATOM   3850 O  OE1 . GLU A 1 667 ? -12.431 -18.748 -12.821 1.00 34.04 ? 667  GLU A OE1 1 
ATOM   3851 O  OE2 . GLU A 1 667 ? -11.110 -17.276 -13.739 1.00 38.57 ? 667  GLU A OE2 1 
ATOM   3852 N  N   . ASN A 1 668 ? -8.977  -17.184 -8.824  1.00 33.14 ? 668  ASN A N   1 
ATOM   3853 C  CA  . ASN A 1 668 ? -9.409  -16.211 -7.822  1.00 34.23 ? 668  ASN A CA  1 
ATOM   3854 C  C   . ASN A 1 668 ? -9.633  -14.855 -8.470  1.00 36.41 ? 668  ASN A C   1 
ATOM   3855 O  O   . ASN A 1 668 ? -8.734  -14.004 -8.525  1.00 36.75 ? 668  ASN A O   1 
ATOM   3856 C  CB  . ASN A 1 668 ? -8.412  -16.116 -6.659  1.00 33.49 ? 668  ASN A CB  1 
ATOM   3857 C  CG  . ASN A 1 668 ? -8.897  -15.196 -5.548  1.00 33.44 ? 668  ASN A CG  1 
ATOM   3858 O  OD1 . ASN A 1 668 ? -9.948  -14.582 -5.652  1.00 32.84 ? 668  ASN A OD1 1 
ATOM   3859 N  ND2 . ASN A 1 668 ? -8.124  -15.102 -4.479  1.00 34.27 ? 668  ASN A ND2 1 
ATOM   3860 N  N   . LEU A 1 669 ? -10.859 -14.656 -8.947  1.00 40.43 ? 669  LEU A N   1 
ATOM   3861 C  CA  . LEU A 1 669 ? -11.218 -13.439 -9.655  1.00 41.09 ? 669  LEU A CA  1 
ATOM   3862 C  C   . LEU A 1 669 ? -11.151 -12.208 -8.740  1.00 40.95 ? 669  LEU A C   1 
ATOM   3863 O  O   . LEU A 1 669 ? -11.106 -11.083 -9.227  1.00 39.43 ? 669  LEU A O   1 
ATOM   3864 C  CB  . LEU A 1 669 ? -12.600 -13.583 -10.317 1.00 43.04 ? 669  LEU A CB  1 
ATOM   3865 C  CG  . LEU A 1 669 ? -12.759 -14.727 -11.342 1.00 44.63 ? 669  LEU A CG  1 
ATOM   3866 C  CD1 . LEU A 1 669 ? -14.176 -14.769 -11.907 1.00 44.98 ? 669  LEU A CD1 1 
ATOM   3867 C  CD2 . LEU A 1 669 ? -11.737 -14.647 -12.474 1.00 45.48 ? 669  LEU A CD2 1 
ATOM   3868 N  N   . ASP A 1 670 ? -11.115 -12.416 -7.425  1.00 41.43 ? 670  ASP A N   1 
ATOM   3869 C  CA  . ASP A 1 670 ? -10.918 -11.312 -6.484  1.00 40.45 ? 670  ASP A CA  1 
ATOM   3870 C  C   . ASP A 1 670 ? -9.541  -10.665 -6.622  1.00 39.23 ? 670  ASP A C   1 
ATOM   3871 O  O   . ASP A 1 670 ? -9.366  -9.530  -6.206  1.00 39.83 ? 670  ASP A O   1 
ATOM   3872 C  CB  . ASP A 1 670 ? -11.113 -11.777 -5.036  1.00 43.23 ? 670  ASP A CB  1 
ATOM   3873 C  CG  . ASP A 1 670 ? -11.198 -10.615 -4.052  1.00 47.14 ? 670  ASP A CG  1 
ATOM   3874 O  OD1 . ASP A 1 670 ? -12.188 -9.857  -4.114  1.00 47.78 ? 670  ASP A OD1 1 
ATOM   3875 O  OD2 . ASP A 1 670 ? -10.275 -10.452 -3.221  1.00 50.24 ? 670  ASP A OD2 1 
ATOM   3876 N  N   . MET A 1 671 ? -8.560  -11.380 -7.180  1.00 38.39 ? 671  MET A N   1 
ATOM   3877 C  CA  . MET A 1 671 ? -7.226  -10.802 -7.395  1.00 36.15 ? 671  MET A CA  1 
ATOM   3878 C  C   . MET A 1 671 ? -7.183  -9.810  -8.571  1.00 34.94 ? 671  MET A C   1 
ATOM   3879 O  O   . MET A 1 671 ? -6.243  -9.013  -8.669  1.00 32.73 ? 671  MET A O   1 
ATOM   3880 C  CB  . MET A 1 671 ? -6.173  -11.896 -7.584  1.00 35.65 ? 671  MET A CB  1 
ATOM   3881 C  CG  . MET A 1 671 ? -6.024  -12.820 -6.377  1.00 37.34 ? 671  MET A CG  1 
ATOM   3882 S  SD  . MET A 1 671 ? -5.459  -11.992 -4.871  1.00 37.79 ? 671  MET A SD  1 
ATOM   3883 C  CE  . MET A 1 671 ? -3.707  -11.814 -5.222  1.00 39.70 ? 671  MET A CE  1 
ATOM   3884 N  N   . ILE A 1 672 ? -8.196  -9.838  -9.438  1.00 32.38 ? 672  ILE A N   1 
ATOM   3885 C  CA  . ILE A 1 672 ? -8.237  -8.937  -10.589 1.00 32.38 ? 672  ILE A CA  1 
ATOM   3886 C  C   . ILE A 1 672 ? -8.539  -7.521  -10.150 1.00 30.46 ? 672  ILE A C   1 
ATOM   3887 O  O   . ILE A 1 672 ? -9.497  -7.282  -9.429  1.00 31.01 ? 672  ILE A O   1 
ATOM   3888 C  CB  . ILE A 1 672 ? -9.272  -9.366  -11.644 1.00 32.41 ? 672  ILE A CB  1 
ATOM   3889 C  CG1 . ILE A 1 672 ? -8.870  -10.712 -12.249 1.00 33.31 ? 672  ILE A CG1 1 
ATOM   3890 C  CG2 . ILE A 1 672 ? -9.378  -8.312  -12.756 1.00 32.64 ? 672  ILE A CG2 1 
ATOM   3891 C  CD1 . ILE A 1 672 ? -9.994  -11.405 -12.990 1.00 34.26 ? 672  ILE A CD1 1 
ATOM   3892 N  N   . GLY A 1 673 ? -7.704  -6.586  -10.587 1.00 29.01 ? 673  GLY A N   1 
ATOM   3893 C  CA  . GLY A 1 673 ? -7.902  -5.177  -10.286 1.00 28.43 ? 673  GLY A CA  1 
ATOM   3894 C  C   . GLY A 1 673 ? -8.388  -4.424  -11.504 1.00 28.73 ? 673  GLY A C   1 
ATOM   3895 O  O   . GLY A 1 673 ? -8.764  -5.007  -12.517 1.00 25.82 ? 673  GLY A O   1 
ATOM   3896 N  N   . ASP A 1 674 ? -8.405  -3.107  -11.385 1.00 30.22 ? 674  ASP A N   1 
ATOM   3897 C  CA  . ASP A 1 674 ? -8.555  -2.238  -12.545 1.00 31.31 ? 674  ASP A CA  1 
ATOM   3898 C  C   . ASP A 1 674 ? -7.568  -1.099  -12.384 1.00 30.41 ? 674  ASP A C   1 
ATOM   3899 O  O   . ASP A 1 674 ? -6.806  -1.075  -11.418 1.00 28.46 ? 674  ASP A O   1 
ATOM   3900 C  CB  . ASP A 1 674 ? -10.014 -1.761  -12.709 1.00 31.01 ? 674  ASP A CB  1 
ATOM   3901 C  CG  . ASP A 1 674 ? -10.556 -1.007  -11.488 1.00 31.82 ? 674  ASP A CG  1 
ATOM   3902 O  OD1 . ASP A 1 674 ? -9.813  -0.772  -10.511 1.00 32.08 ? 674  ASP A OD1 1 
ATOM   3903 O  OD2 . ASP A 1 674 ? -11.760 -0.647  -11.512 1.00 32.25 ? 674  ASP A OD2 1 
ATOM   3904 N  N   . LEU A 1 675 ? -7.573  -0.171  -13.333 1.00 34.67 ? 675  LEU A N   1 
ATOM   3905 C  CA  . LEU A 1 675 ? -6.678  0.987   -13.317 1.00 37.23 ? 675  LEU A CA  1 
ATOM   3906 C  C   . LEU A 1 675 ? -6.585  1.586   -11.923 1.00 37.13 ? 675  LEU A C   1 
ATOM   3907 O  O   . LEU A 1 675 ? -5.497  1.870   -11.420 1.00 37.53 ? 675  LEU A O   1 
ATOM   3908 C  CB  . LEU A 1 675 ? -7.199  2.041   -14.307 1.00 41.34 ? 675  LEU A CB  1 
ATOM   3909 C  CG  . LEU A 1 675 ? -6.449  3.367   -14.462 1.00 42.97 ? 675  LEU A CG  1 
ATOM   3910 C  CD1 . LEU A 1 675 ? -4.990  3.141   -14.828 1.00 44.94 ? 675  LEU A CD1 1 
ATOM   3911 C  CD2 . LEU A 1 675 ? -7.142  4.218   -15.510 1.00 43.76 ? 675  LEU A CD2 1 
ATOM   3912 N  N   . ASP A 1 676 ? -7.737  1.746   -11.285 1.00 38.19 ? 676  ASP A N   1 
ATOM   3913 C  CA  . ASP A 1 676 ? -7.805  2.427   -9.996  1.00 39.25 ? 676  ASP A CA  1 
ATOM   3914 C  C   . ASP A 1 676 ? -7.192  1.587   -8.892  1.00 33.44 ? 676  ASP A C   1 
ATOM   3915 O  O   . ASP A 1 676 ? -6.306  2.055   -8.186  1.00 31.55 ? 676  ASP A O   1 
ATOM   3916 C  CB  . ASP A 1 676 ? -9.254  2.784   -9.648  1.00 43.77 ? 676  ASP A CB  1 
ATOM   3917 C  CG  . ASP A 1 676 ? -9.362  4.098   -8.907  1.00 49.55 ? 676  ASP A CG  1 
ATOM   3918 O  OD1 . ASP A 1 676 ? -9.099  5.155   -9.529  1.00 54.40 ? 676  ASP A OD1 1 
ATOM   3919 O  OD2 . ASP A 1 676 ? -9.717  4.075   -7.708  1.00 55.41 ? 676  ASP A OD2 1 
ATOM   3920 N  N   . SER A 1 677 ? -7.649  0.340   -8.782  1.00 30.29 ? 677  SER A N   1 
ATOM   3921 C  CA  . SER A 1 677 ? -7.260  -0.548  -7.697  1.00 29.50 ? 677  SER A CA  1 
ATOM   3922 C  C   . SER A 1 677 ? -5.894  -1.216  -7.903  1.00 29.59 ? 677  SER A C   1 
ATOM   3923 O  O   . SER A 1 677 ? -5.416  -1.920  -7.015  1.00 27.01 ? 677  SER A O   1 
ATOM   3924 C  CB  . SER A 1 677 ? -8.336  -1.623  -7.487  1.00 30.71 ? 677  SER A CB  1 
ATOM   3925 O  OG  . SER A 1 677 ? -8.448  -2.483  -8.610  1.00 29.76 ? 677  SER A OG  1 
ATOM   3926 N  N   . ALA A 1 678 ? -5.267  -1.008  -9.064  1.00 29.72 ? 678  ALA A N   1 
ATOM   3927 C  CA  . ALA A 1 678 ? -3.879  -1.449  -9.269  1.00 30.53 ? 678  ALA A CA  1 
ATOM   3928 C  C   . ALA A 1 678 ? -2.870  -0.635  -8.466  1.00 30.15 ? 678  ALA A C   1 
ATOM   3929 O  O   . ALA A 1 678 ? -1.734  -1.070  -8.291  1.00 30.96 ? 678  ALA A O   1 
ATOM   3930 C  CB  . ALA A 1 678 ? -3.512  -1.415  -10.746 1.00 30.54 ? 678  ALA A CB  1 
ATOM   3931 N  N   . ALA A 1 679 ? -3.269  0.549   -8.001  1.00 30.16 ? 679  ALA A N   1 
ATOM   3932 C  CA  . ALA A 1 679 ? -2.413  1.389   -7.147  1.00 31.63 ? 679  ALA A CA  1 
ATOM   3933 C  C   . ALA A 1 679 ? -2.829  1.321   -5.670  1.00 32.53 ? 679  ALA A C   1 
ATOM   3934 O  O   . ALA A 1 679 ? -4.015  1.267   -5.363  1.00 32.68 ? 679  ALA A O   1 
ATOM   3935 C  CB  . ALA A 1 679 ? -2.476  2.833   -7.619  1.00 32.39 ? 679  ALA A CB  1 
ATOM   3936 N  N   . LEU A 1 680 ? -1.856  1.325   -4.761  1.00 33.67 ? 680  LEU A N   1 
ATOM   3937 C  CA  . LEU A 1 680 ? -2.139  1.566   -3.339  1.00 35.78 ? 680  LEU A CA  1 
ATOM   3938 C  C   . LEU A 1 680 ? -2.356  3.072   -3.159  1.00 37.40 ? 680  LEU A C   1 
ATOM   3939 O  O   . LEU A 1 680 ? -1.844  3.859   -3.964  1.00 37.85 ? 680  LEU A O   1 
ATOM   3940 C  CB  . LEU A 1 680 ? -0.976  1.112   -2.453  1.00 34.47 ? 680  LEU A CB  1 
ATOM   3941 C  CG  . LEU A 1 680 ? -0.613  -0.370  -2.479  1.00 34.10 ? 680  LEU A CG  1 
ATOM   3942 C  CD1 . LEU A 1 680 ? 0.686   -0.609  -1.746  1.00 34.19 ? 680  LEU A CD1 1 
ATOM   3943 C  CD2 . LEU A 1 680 ? -1.704  -1.214  -1.848  1.00 35.36 ? 680  LEU A CD2 1 
ATOM   3944 N  N   . PRO A 1 681 ? -3.104  3.485   -2.108  1.00 39.40 ? 681  PRO A N   1 
ATOM   3945 C  CA  . PRO A 1 681 ? -3.294  4.928   -1.917  1.00 39.11 ? 681  PRO A CA  1 
ATOM   3946 C  C   . PRO A 1 681 ? -1.953  5.669   -1.887  1.00 39.54 ? 681  PRO A C   1 
ATOM   3947 O  O   . PRO A 1 681 ? -0.998  5.194   -1.270  1.00 38.76 ? 681  PRO A O   1 
ATOM   3948 C  CB  . PRO A 1 681 ? -4.018  5.021   -0.565  1.00 39.98 ? 681  PRO A CB  1 
ATOM   3949 C  CG  . PRO A 1 681 ? -4.664  3.692   -0.374  1.00 39.43 ? 681  PRO A CG  1 
ATOM   3950 C  CD  . PRO A 1 681 ? -3.776  2.694   -1.057  1.00 39.51 ? 681  PRO A CD  1 
ATOM   3951 N  N   . GLY A 1 682 ? -1.872  6.795   -2.593  1.00 39.63 ? 682  GLY A N   1 
ATOM   3952 C  CA  . GLY A 1 682 ? -0.660  7.604   -2.612  1.00 38.85 ? 682  GLY A CA  1 
ATOM   3953 C  C   . GLY A 1 682 ? 0.266   7.316   -3.776  1.00 40.47 ? 682  GLY A C   1 
ATOM   3954 O  O   . GLY A 1 682 ? 1.001   8.208   -4.225  1.00 40.98 ? 682  GLY A O   1 
ATOM   3955 N  N   . GLU A 1 683 ? 0.240   6.084   -4.283  1.00 39.50 ? 683  GLU A N   1 
ATOM   3956 C  CA  . GLU A 1 683 ? 1.190   5.688   -5.332  1.00 38.96 ? 683  GLU A CA  1 
ATOM   3957 C  C   . GLU A 1 683 ? 1.118   6.552   -6.582  1.00 38.29 ? 683  GLU A C   1 
ATOM   3958 O  O   . GLU A 1 683 ? 2.149   6.818   -7.197  1.00 37.74 ? 683  GLU A O   1 
ATOM   3959 C  CB  . GLU A 1 683 ? 1.037   4.212   -5.699  1.00 37.05 ? 683  GLU A CB  1 
ATOM   3960 C  CG  . GLU A 1 683 ? 1.744   3.298   -4.720  1.00 36.71 ? 683  GLU A CG  1 
ATOM   3961 C  CD  . GLU A 1 683 ? 1.795   1.863   -5.189  1.00 36.58 ? 683  GLU A CD  1 
ATOM   3962 O  OE1 . GLU A 1 683 ? 0.754   1.370   -5.663  1.00 38.65 ? 683  GLU A OE1 1 
ATOM   3963 O  OE2 . GLU A 1 683 ? 2.867   1.227   -5.077  1.00 34.24 ? 683  GLU A OE2 1 
ATOM   3964 N  N   . ARG A 1 684 ? -0.086  6.992   -6.943  1.00 40.50 ? 684  ARG A N   1 
ATOM   3965 C  CA  . ARG A 1 684 ? -0.272  7.889   -8.088  1.00 42.68 ? 684  ARG A CA  1 
ATOM   3966 C  C   . ARG A 1 684 ? 0.458   9.217   -7.948  1.00 43.60 ? 684  ARG A C   1 
ATOM   3967 O  O   . ARG A 1 684 ? 0.913   9.772   -8.939  1.00 45.89 ? 684  ARG A O   1 
ATOM   3968 C  CB  . ARG A 1 684 ? -1.753  8.152   -8.334  1.00 45.60 ? 684  ARG A CB  1 
ATOM   3969 C  CG  . ARG A 1 684 ? -2.416  7.030   -9.102  1.00 47.90 ? 684  ARG A CG  1 
ATOM   3970 C  CD  . ARG A 1 684 ? -3.853  7.325   -9.468  1.00 48.97 ? 684  ARG A CD  1 
ATOM   3971 N  NE  . ARG A 1 684 ? -4.203  6.583   -10.675 1.00 52.13 ? 684  ARG A NE  1 
ATOM   3972 C  CZ  . ARG A 1 684 ? -4.425  5.269   -10.735 1.00 53.49 ? 684  ARG A CZ  1 
ATOM   3973 N  NH1 . ARG A 1 684 ? -4.360  4.504   -9.650  1.00 55.55 ? 684  ARG A NH1 1 
ATOM   3974 N  NH2 . ARG A 1 684 ? -4.718  4.706   -11.901 1.00 54.94 ? 684  ARG A NH2 1 
ATOM   3975 N  N   . ASP A 1 685 ? 0.575   9.723   -6.724  1.00 44.87 ? 685  ASP A N   1 
ATOM   3976 C  CA  . ASP A 1 685 ? 1.274   10.988  -6.468  1.00 46.21 ? 685  ASP A CA  1 
ATOM   3977 C  C   . ASP A 1 685 ? 2.760   10.785  -6.134  1.00 44.82 ? 685  ASP A C   1 
ATOM   3978 O  O   . ASP A 1 685 ? 3.440   11.720  -5.742  1.00 44.50 ? 685  ASP A O   1 
ATOM   3979 C  CB  . ASP A 1 685 ? 0.574   11.749  -5.328  1.00 47.72 ? 685  ASP A CB  1 
ATOM   3980 C  CG  . ASP A 1 685 ? -0.836  12.200  -5.698  1.00 48.65 ? 685  ASP A CG  1 
ATOM   3981 O  OD1 . ASP A 1 685 ? -1.097  12.482  -6.887  1.00 52.37 ? 685  ASP A OD1 1 
ATOM   3982 O  OD2 . ASP A 1 685 ? -1.686  12.289  -4.793  1.00 50.30 ? 685  ASP A OD2 1 
ATOM   3983 N  N   . LYS A 1 686 ? 3.258   9.566   -6.314  1.00 44.79 ? 686  LYS A N   1 
ATOM   3984 C  CA  . LYS A 1 686 ? 4.618   9.209   -5.939  1.00 43.22 ? 686  LYS A CA  1 
ATOM   3985 C  C   . LYS A 1 686 ? 5.572   9.659   -7.043  1.00 38.78 ? 686  LYS A C   1 
ATOM   3986 O  O   . LYS A 1 686 ? 5.199   9.652   -8.206  1.00 38.03 ? 686  LYS A O   1 
ATOM   3987 C  CB  . LYS A 1 686 ? 4.700   7.692   -5.752  1.00 46.25 ? 686  LYS A CB  1 
ATOM   3988 C  CG  . LYS A 1 686 ? 5.821   7.206   -4.858  1.00 48.16 ? 686  LYS A CG  1 
ATOM   3989 C  CD  . LYS A 1 686 ? 5.535   5.801   -4.336  1.00 49.89 ? 686  LYS A CD  1 
ATOM   3990 C  CE  . LYS A 1 686 ? 5.379   4.797   -5.479  1.00 50.82 ? 686  LYS A CE  1 
ATOM   3991 N  NZ  . LYS A 1 686 ? 5.447   3.381   -5.007  1.00 49.91 ? 686  LYS A NZ  1 
ATOM   3992 N  N   . PRO A 1 687 ? 6.809   10.045  -6.691  1.00 36.14 ? 687  PRO A N   1 
ATOM   3993 C  CA  . PRO A 1 687 ? 7.713   10.491  -7.756  1.00 34.81 ? 687  PRO A CA  1 
ATOM   3994 C  C   . PRO A 1 687 ? 8.185   9.332   -8.642  1.00 32.27 ? 687  PRO A C   1 
ATOM   3995 O  O   . PRO A 1 687 ? 8.286   8.201   -8.181  1.00 29.02 ? 687  PRO A O   1 
ATOM   3996 C  CB  . PRO A 1 687 ? 8.907   11.100  -6.996  1.00 35.21 ? 687  PRO A CB  1 
ATOM   3997 C  CG  . PRO A 1 687 ? 8.545   11.077  -5.545  1.00 36.88 ? 687  PRO A CG  1 
ATOM   3998 C  CD  . PRO A 1 687 ? 7.461   10.058  -5.372  1.00 35.67 ? 687  PRO A CD  1 
ATOM   3999 N  N   . VAL A 1 688 ? 8.478   9.632   -9.902  1.00 29.31 ? 688  VAL A N   1 
ATOM   4000 C  CA  . VAL A 1 688 ? 9.067   8.658   -10.794 1.00 27.48 ? 688  VAL A CA  1 
ATOM   4001 C  C   . VAL A 1 688 ? 10.429  8.242   -10.265 1.00 27.70 ? 688  VAL A C   1 
ATOM   4002 O  O   . VAL A 1 688 ? 11.184  9.072   -9.743  1.00 27.16 ? 688  VAL A O   1 
ATOM   4003 C  CB  . VAL A 1 688 ? 9.252   9.229   -12.216 1.00 27.39 ? 688  VAL A CB  1 
ATOM   4004 C  CG1 . VAL A 1 688 ? 9.942   8.211   -13.129 1.00 27.21 ? 688  VAL A CG1 1 
ATOM   4005 C  CG2 . VAL A 1 688 ? 7.917   9.655   -12.795 1.00 26.95 ? 688  VAL A CG2 1 
ATOM   4006 N  N   . ASP A 1 689 ? 10.735  6.951   -10.409 1.00 26.57 ? 689  ASP A N   1 
ATOM   4007 C  CA  . ASP A 1 689 ? 12.075  6.428   -10.161 1.00 26.74 ? 689  ASP A CA  1 
ATOM   4008 C  C   . ASP A 1 689 ? 12.810  6.316   -11.506 1.00 25.96 ? 689  ASP A C   1 
ATOM   4009 O  O   . ASP A 1 689 ? 12.584  5.368   -12.266 1.00 24.17 ? 689  ASP A O   1 
ATOM   4010 C  CB  . ASP A 1 689 ? 11.969  5.066   -9.477  1.00 27.54 ? 689  ASP A CB  1 
ATOM   4011 C  CG  . ASP A 1 689 ? 13.288  4.559   -8.989  1.00 28.87 ? 689  ASP A CG  1 
ATOM   4012 O  OD1 . ASP A 1 689 ? 14.315  4.847   -9.643  1.00 28.43 ? 689  ASP A OD1 1 
ATOM   4013 O  OD2 . ASP A 1 689 ? 13.289  3.855   -7.950  1.00 31.48 ? 689  ASP A OD2 1 
ATOM   4014 N  N   . TRP A 1 690 ? 13.691  7.277   -11.799 1.00 24.80 ? 690  TRP A N   1 
ATOM   4015 C  CA  . TRP A 1 690 ? 14.235  7.417   -13.161 1.00 24.23 ? 690  TRP A CA  1 
ATOM   4016 C  C   . TRP A 1 690 ? 15.328  6.418   -13.475 1.00 24.42 ? 690  TRP A C   1 
ATOM   4017 O  O   . TRP A 1 690 ? 15.499  6.033   -14.636 1.00 25.06 ? 690  TRP A O   1 
ATOM   4018 C  CB  . TRP A 1 690 ? 14.753  8.830   -13.411 1.00 23.81 ? 690  TRP A CB  1 
ATOM   4019 C  CG  . TRP A 1 690 ? 13.666  9.844   -13.396 1.00 23.81 ? 690  TRP A CG  1 
ATOM   4020 C  CD1 . TRP A 1 690 ? 13.356  10.689  -12.377 1.00 23.73 ? 690  TRP A CD1 1 
ATOM   4021 C  CD2 . TRP A 1 690 ? 12.710  10.096  -14.433 1.00 23.99 ? 690  TRP A CD2 1 
ATOM   4022 N  NE1 . TRP A 1 690 ? 12.281  11.465  -12.716 1.00 24.13 ? 690  TRP A NE1 1 
ATOM   4023 C  CE2 . TRP A 1 690 ? 11.860  11.116  -13.974 1.00 23.83 ? 690  TRP A CE2 1 
ATOM   4024 C  CE3 . TRP A 1 690 ? 12.484  9.548   -15.702 1.00 24.65 ? 690  TRP A CE3 1 
ATOM   4025 C  CZ2 . TRP A 1 690 ? 10.807  11.613  -14.740 1.00 23.77 ? 690  TRP A CZ2 1 
ATOM   4026 C  CZ3 . TRP A 1 690 ? 11.435  10.046  -16.463 1.00 24.17 ? 690  TRP A CZ3 1 
ATOM   4027 C  CH2 . TRP A 1 690 ? 10.613  11.070  -15.978 1.00 23.91 ? 690  TRP A CH2 1 
ATOM   4028 N  N   . ASP A 1 691 ? 16.087  6.015   -12.462 1.00 24.65 ? 691  ASP A N   1 
ATOM   4029 C  CA  . ASP A 1 691 ? 17.106  4.990   -12.659 1.00 25.87 ? 691  ASP A CA  1 
ATOM   4030 C  C   . ASP A 1 691 ? 16.434  3.663   -13.059 1.00 25.42 ? 691  ASP A C   1 
ATOM   4031 O  O   . ASP A 1 691 ? 16.959  2.922   -13.892 1.00 24.20 ? 691  ASP A O   1 
ATOM   4032 C  CB  . ASP A 1 691 ? 17.979  4.817   -11.407 1.00 27.07 ? 691  ASP A CB  1 
ATOM   4033 C  CG  . ASP A 1 691 ? 18.822  6.066   -11.087 1.00 29.37 ? 691  ASP A CG  1 
ATOM   4034 O  OD1 . ASP A 1 691 ? 18.592  7.143   -11.681 1.00 30.29 ? 691  ASP A OD1 1 
ATOM   4035 O  OD2 . ASP A 1 691 ? 19.709  5.987   -10.218 1.00 29.68 ? 691  ASP A OD2 1 
ATOM   4036 N  N   . LEU A 1 692 ? 15.269  3.391   -12.472 1.00 25.47 ? 692  LEU A N   1 
ATOM   4037 C  CA  . LEU A 1 692 ? 14.512  2.170   -12.732 1.00 25.40 ? 692  LEU A CA  1 
ATOM   4038 C  C   . LEU A 1 692 ? 13.988  2.105   -14.175 1.00 26.08 ? 692  LEU A C   1 
ATOM   4039 O  O   . LEU A 1 692 ? 14.161  1.100   -14.856 1.00 26.23 ? 692  LEU A O   1 
ATOM   4040 C  CB  . LEU A 1 692 ? 13.354  2.069   -11.739 1.00 26.01 ? 692  LEU A CB  1 
ATOM   4041 C  CG  . LEU A 1 692 ? 12.420  0.846   -11.770 1.00 27.32 ? 692  LEU A CG  1 
ATOM   4042 C  CD1 . LEU A 1 692 ? 13.185  -0.448  -11.515 1.00 26.57 ? 692  LEU A CD1 1 
ATOM   4043 C  CD2 . LEU A 1 692 ? 11.322  1.032   -10.730 1.00 26.54 ? 692  LEU A CD2 1 
ATOM   4044 N  N   . ILE A 1 693 ? 13.363  3.175   -14.651 1.00 24.30 ? 693  ILE A N   1 
ATOM   4045 C  CA  . ILE A 1 693 ? 12.767  3.149   -15.991 1.00 24.19 ? 693  ILE A CA  1 
ATOM   4046 C  C   . ILE A 1 693 ? 13.704  3.633   -17.114 1.00 23.48 ? 693  ILE A C   1 
ATOM   4047 O  O   . ILE A 1 693 ? 13.429  3.382   -18.270 1.00 22.01 ? 693  ILE A O   1 
ATOM   4048 C  CB  . ILE A 1 693 ? 11.450  3.944   -16.054 1.00 23.51 ? 693  ILE A CB  1 
ATOM   4049 C  CG1 . ILE A 1 693 ? 11.693  5.449   -15.854 1.00 23.74 ? 693  ILE A CG1 1 
ATOM   4050 C  CG2 . ILE A 1 693 ? 10.465  3.416   -15.022 1.00 23.94 ? 693  ILE A CG2 1 
ATOM   4051 C  CD1 . ILE A 1 693 ? 10.478  6.299   -16.149 1.00 24.10 ? 693  ILE A CD1 1 
ATOM   4052 N  N   . GLY A 1 694 ? 14.778  4.341   -16.768 1.00 25.05 ? 694  GLY A N   1 
ATOM   4053 C  CA  . GLY A 1 694 ? 15.719  4.898   -17.752 1.00 26.33 ? 694  GLY A CA  1 
ATOM   4054 C  C   . GLY A 1 694 ? 15.326  6.274   -18.295 1.00 29.73 ? 694  GLY A C   1 
ATOM   4055 O  O   . GLY A 1 694 ? 14.164  6.724   -18.168 1.00 28.98 ? 694  GLY A O   1 
ATOM   4056 N  N   . TYR A 1 695 ? 16.311  6.948   -18.893 1.00 31.77 ? 695  TYR A N   1 
ATOM   4057 C  CA  . TYR A 1 695 ? 16.100  8.196   -19.651 1.00 34.48 ? 695  TYR A CA  1 
ATOM   4058 C  C   . TYR A 1 695 ? 17.287  8.435   -20.588 1.00 35.28 ? 695  TYR A C   1 
ATOM   4059 O  O   . TYR A 1 695 ? 18.428  8.616   -20.133 1.00 33.53 ? 695  TYR A O   1 
ATOM   4060 C  CB  . TYR A 1 695 ? 15.957  9.391   -18.709 1.00 35.75 ? 695  TYR A CB  1 
ATOM   4061 C  CG  . TYR A 1 695 ? 15.437  10.662  -19.348 1.00 36.70 ? 695  TYR A CG  1 
ATOM   4062 C  CD1 . TYR A 1 695 ? 16.283  11.521  -20.062 1.00 35.81 ? 695  TYR A CD1 1 
ATOM   4063 C  CD2 . TYR A 1 695 ? 14.099  11.032  -19.198 1.00 36.77 ? 695  TYR A CD2 1 
ATOM   4064 C  CE1 . TYR A 1 695 ? 15.806  12.697  -20.618 1.00 35.50 ? 695  TYR A CE1 1 
ATOM   4065 C  CE2 . TYR A 1 695 ? 13.614  12.201  -19.754 1.00 36.79 ? 695  TYR A CE2 1 
ATOM   4066 C  CZ  . TYR A 1 695 ? 14.459  13.032  -20.460 1.00 37.41 ? 695  TYR A CZ  1 
ATOM   4067 O  OH  . TYR A 1 695 ? 13.937  14.192  -20.999 1.00 36.48 ? 695  TYR A OH  1 
ATOM   4068 N  N   . GLY A 1 696 ? 17.012  8.449   -21.890 1.00 40.11 ? 696  GLY A N   1 
ATOM   4069 C  CA  . GLY A 1 696 ? 18.053  8.612   -22.925 1.00 42.61 ? 696  GLY A CA  1 
ATOM   4070 C  C   . GLY A 1 696 ? 18.917  9.855   -22.802 1.00 41.39 ? 696  GLY A C   1 
ATOM   4071 O  O   . GLY A 1 696 ? 20.143  9.750   -22.794 1.00 44.43 ? 696  GLY A O   1 
ATOM   4072 N  N   . LYS B 1 178 ? 31.580  3.868   12.050  1.00 37.50 ? 178  LYS B N   1 
ATOM   4073 C  CA  . LYS B 1 178 ? 32.771  4.712   12.330  1.00 36.09 ? 178  LYS B CA  1 
ATOM   4074 C  C   . LYS B 1 178 ? 32.634  6.050   11.593  1.00 31.40 ? 178  LYS B C   1 
ATOM   4075 O  O   . LYS B 1 178 ? 33.104  6.210   10.475  1.00 29.74 ? 178  LYS B O   1 
ATOM   4076 C  CB  . LYS B 1 178 ? 34.071  4.002   11.926  1.00 38.42 ? 178  LYS B CB  1 
ATOM   4077 C  CG  . LYS B 1 178 ? 34.151  2.510   12.235  1.00 42.54 ? 178  LYS B CG  1 
ATOM   4078 C  CD  . LYS B 1 178 ? 34.036  2.192   13.719  1.00 44.17 ? 178  LYS B CD  1 
ATOM   4079 C  CE  . LYS B 1 178 ? 33.808  0.694   13.914  1.00 46.55 ? 178  LYS B CE  1 
ATOM   4080 N  NZ  . LYS B 1 178 ? 33.557  0.320   15.330  1.00 45.74 ? 178  LYS B NZ  1 
ATOM   4081 N  N   . LEU B 1 179 ? 31.993  7.002   12.247  1.00 29.43 ? 179  LEU B N   1 
ATOM   4082 C  CA  . LEU B 1 179 ? 31.736  8.324   11.691  1.00 29.85 ? 179  LEU B CA  1 
ATOM   4083 C  C   . LEU B 1 179 ? 32.541  9.382   12.430  1.00 28.81 ? 179  LEU B C   1 
ATOM   4084 O  O   . LEU B 1 179 ? 32.723  9.280   13.639  1.00 29.09 ? 179  LEU B O   1 
ATOM   4085 C  CB  . LEU B 1 179 ? 30.256  8.657   11.872  1.00 30.77 ? 179  LEU B CB  1 
ATOM   4086 C  CG  . LEU B 1 179 ? 29.225  7.881   11.055  1.00 32.27 ? 179  LEU B CG  1 
ATOM   4087 C  CD1 . LEU B 1 179 ? 27.827  8.217   11.552  1.00 32.09 ? 179  LEU B CD1 1 
ATOM   4088 C  CD2 . LEU B 1 179 ? 29.348  8.220   9.580   1.00 32.94 ? 179  LEU B CD2 1 
ATOM   4089 N  N   . ASN B 1 180 ? 32.987  10.428  11.742  1.00 29.03 ? 180  ASN B N   1 
ATOM   4090 C  CA  . ASN B 1 180 ? 33.539  11.572  12.467  1.00 29.68 ? 180  ASN B CA  1 
ATOM   4091 C  C   . ASN B 1 180 ? 32.385  12.289  13.151  1.00 29.22 ? 180  ASN B C   1 
ATOM   4092 O  O   . ASN B 1 180 ? 31.235  11.876  12.996  1.00 27.41 ? 180  ASN B O   1 
ATOM   4093 C  CB  . ASN B 1 180 ? 34.422  12.481  11.596  1.00 30.76 ? 180  ASN B CB  1 
ATOM   4094 C  CG  . ASN B 1 180 ? 33.691  13.115  10.438  1.00 31.81 ? 180  ASN B CG  1 
ATOM   4095 O  OD1 . ASN B 1 180 ? 32.535  13.529  10.556  1.00 32.97 ? 180  ASN B OD1 1 
ATOM   4096 N  ND2 . ASN B 1 180 ? 34.392  13.231  9.299   1.00 31.62 ? 180  ASN B ND2 1 
ATOM   4097 N  N   . LYS B 1 181 ? 32.665  13.327  13.927  1.00 30.51 ? 181  LYS B N   1 
ATOM   4098 C  CA  . LYS B 1 181 ? 31.592  13.907  14.743  1.00 32.77 ? 181  LYS B CA  1 
ATOM   4099 C  C   . LYS B 1 181 ? 30.578  14.711  13.937  1.00 30.24 ? 181  LYS B C   1 
ATOM   4100 O  O   . LYS B 1 181 ? 29.388  14.604  14.194  1.00 28.04 ? 181  LYS B O   1 
ATOM   4101 C  CB  . LYS B 1 181 ? 32.108  14.706  15.945  1.00 35.28 ? 181  LYS B CB  1 
ATOM   4102 C  CG  . LYS B 1 181 ? 33.058  15.850  15.658  1.00 39.66 ? 181  LYS B CG  1 
ATOM   4103 C  CD  . LYS B 1 181 ? 33.584  16.378  16.990  1.00 44.64 ? 181  LYS B CD  1 
ATOM   4104 C  CE  . LYS B 1 181 ? 34.769  17.319  16.857  1.00 46.04 ? 181  LYS B CE  1 
ATOM   4105 N  NZ  . LYS B 1 181 ? 34.627  18.340  15.783  1.00 47.30 ? 181  LYS B NZ  1 
ATOM   4106 N  N   . ASP B 1 182 ? 31.034  15.492  12.963  1.00 29.38 ? 182  ASP B N   1 
ATOM   4107 C  CA  . ASP B 1 182 ? 30.102  16.217  12.091  1.00 28.27 ? 182  ASP B CA  1 
ATOM   4108 C  C   . ASP B 1 182 ? 29.143  15.248  11.398  1.00 27.64 ? 182  ASP B C   1 
ATOM   4109 O  O   . ASP B 1 182 ? 27.925  15.481  11.358  1.00 27.26 ? 182  ASP B O   1 
ATOM   4110 C  CB  . ASP B 1 182 ? 30.856  17.025  11.043  1.00 28.85 ? 182  ASP B CB  1 
ATOM   4111 C  CG  . ASP B 1 182 ? 31.634  18.173  11.639  1.00 29.86 ? 182  ASP B CG  1 
ATOM   4112 O  OD1 . ASP B 1 182 ? 31.154  18.790  12.605  1.00 33.09 ? 182  ASP B OD1 1 
ATOM   4113 O  OD2 . ASP B 1 182 ? 32.720  18.485  11.127  1.00 30.56 ? 182  ASP B OD2 1 
ATOM   4114 N  N   . ALA B 1 183 ? 29.691  14.158  10.869  1.00 27.01 ? 183  ALA B N   1 
ATOM   4115 C  CA  . ALA B 1 183 ? 28.896  13.174  10.139  1.00 27.96 ? 183  ALA B CA  1 
ATOM   4116 C  C   . ALA B 1 183 ? 27.815  12.593  11.025  1.00 29.37 ? 183  ALA B C   1 
ATOM   4117 O  O   . ALA B 1 183 ? 26.648  12.515  10.634  1.00 29.01 ? 183  ALA B O   1 
ATOM   4118 C  CB  . ALA B 1 183 ? 29.774  12.050  9.610   1.00 27.93 ? 183  ALA B CB  1 
ATOM   4119 N  N   . GLU B 1 184 ? 28.218  12.172  12.217  1.00 31.44 ? 184  GLU B N   1 
ATOM   4120 C  CA  . GLU B 1 184 ? 27.277  11.646  13.181  1.00 33.10 ? 184  GLU B CA  1 
ATOM   4121 C  C   . GLU B 1 184 ? 26.203  12.665  13.555  1.00 30.31 ? 184  GLU B C   1 
ATOM   4122 O  O   . GLU B 1 184 ? 25.034  12.316  13.625  1.00 29.06 ? 184  GLU B O   1 
ATOM   4123 C  CB  . GLU B 1 184 ? 28.001  11.168  14.428  1.00 36.38 ? 184  GLU B CB  1 
ATOM   4124 C  CG  . GLU B 1 184 ? 27.121  10.286  15.293  1.00 40.44 ? 184  GLU B CG  1 
ATOM   4125 C  CD  . GLU B 1 184 ? 27.930  9.374   16.175  1.00 43.01 ? 184  GLU B CD  1 
ATOM   4126 O  OE1 . GLU B 1 184 ? 28.713  9.901   16.986  1.00 45.00 ? 184  GLU B OE1 1 
ATOM   4127 O  OE2 . GLU B 1 184 ? 27.776  8.140   16.042  1.00 48.46 ? 184  GLU B OE2 1 
ATOM   4128 N  N   . ASN B 1 185 ? 26.609  13.914  13.782  1.00 31.00 ? 185  ASN B N   1 
ATOM   4129 C  CA  . ASN B 1 185 ? 25.681  15.010  14.075  1.00 31.79 ? 185  ASN B CA  1 
ATOM   4130 C  C   . ASN B 1 185 ? 24.591  15.181  13.019  1.00 31.70 ? 185  ASN B C   1 
ATOM   4131 O  O   . ASN B 1 185 ? 23.409  15.221  13.349  1.00 31.96 ? 185  ASN B O   1 
ATOM   4132 C  CB  . ASN B 1 185 ? 26.429  16.346  14.204  1.00 33.52 ? 185  ASN B CB  1 
ATOM   4133 C  CG  . ASN B 1 185 ? 27.130  16.507  15.539  1.00 36.44 ? 185  ASN B CG  1 
ATOM   4134 O  OD1 . ASN B 1 185 ? 27.891  17.456  15.738  1.00 39.06 ? 185  ASN B OD1 1 
ATOM   4135 N  ND2 . ASN B 1 185 ? 26.879  15.592  16.461  1.00 37.25 ? 185  ASN B ND2 1 
ATOM   4136 N  N   . VAL B 1 186 ? 24.989  15.302  11.756  1.00 30.08 ? 186  VAL B N   1 
ATOM   4137 C  CA  . VAL B 1 186 ? 24.012  15.544  10.696  1.00 29.19 ? 186  VAL B CA  1 
ATOM   4138 C  C   . VAL B 1 186 ? 23.145  14.311  10.475  1.00 29.35 ? 186  VAL B C   1 
ATOM   4139 O  O   . VAL B 1 186 ? 21.962  14.441  10.179  1.00 28.90 ? 186  VAL B O   1 
ATOM   4140 C  CB  . VAL B 1 186 ? 24.642  16.043  9.377   1.00 28.76 ? 186  VAL B CB  1 
ATOM   4141 C  CG1 . VAL B 1 186 ? 25.389  17.351  9.619   1.00 28.84 ? 186  VAL B CG1 1 
ATOM   4142 C  CG2 . VAL B 1 186 ? 25.535  14.992  8.720   1.00 29.51 ? 186  VAL B CG2 1 
ATOM   4143 N  N   . VAL B 1 187 ? 23.722  13.128  10.653  1.00 29.60 ? 187  VAL B N   1 
ATOM   4144 C  CA  . VAL B 1 187 ? 22.961  11.887  10.570  1.00 32.08 ? 187  VAL B CA  1 
ATOM   4145 C  C   . VAL B 1 187 ? 21.849  11.841  11.634  1.00 33.69 ? 187  VAL B C   1 
ATOM   4146 O  O   . VAL B 1 187 ? 20.713  11.504  11.325  1.00 31.87 ? 187  VAL B O   1 
ATOM   4147 C  CB  . VAL B 1 187 ? 23.887  10.637  10.644  1.00 32.94 ? 187  VAL B CB  1 
ATOM   4148 C  CG1 . VAL B 1 187 ? 23.104  9.366   10.954  1.00 32.47 ? 187  VAL B CG1 1 
ATOM   4149 C  CG2 . VAL B 1 187 ? 24.643  10.455  9.332   1.00 32.00 ? 187  VAL B CG2 1 
ATOM   4150 N  N   . LYS B 1 188 ? 22.160  12.198  12.877  1.00 38.23 ? 188  LYS B N   1 
ATOM   4151 C  CA  . LYS B 1 188 ? 21.128  12.175  13.916  1.00 39.99 ? 188  LYS B CA  1 
ATOM   4152 C  C   . LYS B 1 188 ? 20.106  13.295  13.711  1.00 39.28 ? 188  LYS B C   1 
ATOM   4153 O  O   . LYS B 1 188 ? 18.911  13.043  13.808  1.00 36.68 ? 188  LYS B O   1 
ATOM   4154 C  CB  . LYS B 1 188 ? 21.706  12.186  15.331  1.00 42.44 ? 188  LYS B CB  1 
ATOM   4155 C  CG  . LYS B 1 188 ? 22.445  13.443  15.759  1.00 48.02 ? 188  LYS B CG  1 
ATOM   4156 C  CD  . LYS B 1 188 ? 22.813  13.358  17.243  1.00 51.53 ? 188  LYS B CD  1 
ATOM   4157 C  CE  . LYS B 1 188 ? 23.991  14.257  17.599  1.00 52.93 ? 188  LYS B CE  1 
ATOM   4158 N  NZ  . LYS B 1 188 ? 24.456  14.035  18.997  1.00 54.70 ? 188  LYS B NZ  1 
ATOM   4159 N  N   . LYS B 1 189 ? 20.565  14.508  13.393  1.00 37.63 ? 189  LYS B N   1 
ATOM   4160 C  CA  . LYS B 1 189 ? 19.646  15.609  13.091  1.00 39.33 ? 189  LYS B CA  1 
ATOM   4161 C  C   . LYS B 1 189 ? 18.699  15.268  11.935  1.00 37.32 ? 189  LYS B C   1 
ATOM   4162 O  O   . LYS B 1 189 ? 17.570  15.749  11.900  1.00 38.85 ? 189  LYS B O   1 
ATOM   4163 C  CB  . LYS B 1 189 ? 20.390  16.918  12.811  1.00 41.53 ? 189  LYS B CB  1 
ATOM   4164 C  CG  . LYS B 1 189 ? 20.686  17.723  14.072  1.00 45.12 ? 189  LYS B CG  1 
ATOM   4165 C  CD  . LYS B 1 189 ? 21.202  19.122  13.763  1.00 48.20 ? 189  LYS B CD  1 
ATOM   4166 C  CE  . LYS B 1 189 ? 22.703  19.123  13.513  1.00 50.49 ? 189  LYS B CE  1 
ATOM   4167 N  NZ  . LYS B 1 189 ? 23.118  20.212  12.582  1.00 52.44 ? 189  LYS B NZ  1 
ATOM   4168 N  N   . ALA B 1 190 ? 19.146  14.422  11.014  1.00 34.06 ? 190  ALA B N   1 
ATOM   4169 C  CA  . ALA B 1 190 ? 18.296  13.959  9.920   1.00 34.56 ? 190  ALA B CA  1 
ATOM   4170 C  C   . ALA B 1 190 ? 17.386  12.780  10.303  1.00 35.12 ? 190  ALA B C   1 
ATOM   4171 O  O   . ALA B 1 190 ? 16.637  12.286  9.462   1.00 35.58 ? 190  ALA B O   1 
ATOM   4172 C  CB  . ALA B 1 190 ? 19.149  13.592  8.710   1.00 33.34 ? 190  ALA B CB  1 
ATOM   4173 N  N   . GLY B 1 191 ? 17.440  12.330  11.557  1.00 35.75 ? 191  GLY B N   1 
ATOM   4174 C  CA  . GLY B 1 191 ? 16.621  11.206  12.005  1.00 34.66 ? 191  GLY B CA  1 
ATOM   4175 C  C   . GLY B 1 191 ? 17.049  9.900   11.371  1.00 34.46 ? 191  GLY B C   1 
ATOM   4176 O  O   . GLY B 1 191 ? 16.238  9.006   11.187  1.00 35.24 ? 191  GLY B O   1 
ATOM   4177 N  N   . ILE B 1 192 ? 18.326  9.778   11.030  1.00 36.08 ? 192  ILE B N   1 
ATOM   4178 C  CA  . ILE B 1 192 ? 18.820  8.565   10.382  1.00 36.43 ? 192  ILE B CA  1 
ATOM   4179 C  C   . ILE B 1 192 ? 19.565  7.727   11.409  1.00 36.91 ? 192  ILE B C   1 
ATOM   4180 O  O   . ILE B 1 192 ? 20.344  8.251   12.189  1.00 36.93 ? 192  ILE B O   1 
ATOM   4181 C  CB  . ILE B 1 192 ? 19.731  8.888   9.179   1.00 36.82 ? 192  ILE B CB  1 
ATOM   4182 C  CG1 . ILE B 1 192 ? 18.915  9.569   8.074   1.00 38.63 ? 192  ILE B CG1 1 
ATOM   4183 C  CG2 . ILE B 1 192 ? 20.392  7.620   8.642   1.00 35.54 ? 192  ILE B CG2 1 
ATOM   4184 C  CD1 . ILE B 1 192 ? 19.744  10.340  7.072   1.00 38.67 ? 192  ILE B CD1 1 
ATOM   4185 N  N   . ASP B 1 193 ? 19.299  6.428   11.407  1.00 39.17 ? 193  ASP B N   1 
ATOM   4186 C  CA  . ASP B 1 193 ? 20.002  5.485   12.263  1.00 40.98 ? 193  ASP B CA  1 
ATOM   4187 C  C   . ASP B 1 193 ? 21.386  5.220   11.674  1.00 41.76 ? 193  ASP B C   1 
ATOM   4188 O  O   . ASP B 1 193 ? 21.496  4.606   10.608  1.00 43.12 ? 193  ASP B O   1 
ATOM   4189 C  CB  . ASP B 1 193 ? 19.210  4.177   12.356  1.00 42.48 ? 193  ASP B CB  1 
ATOM   4190 C  CG  . ASP B 1 193 ? 19.896  3.125   13.211  1.00 43.17 ? 193  ASP B CG  1 
ATOM   4191 O  OD1 . ASP B 1 193 ? 20.837  3.460   13.964  1.00 43.43 ? 193  ASP B OD1 1 
ATOM   4192 O  OD2 . ASP B 1 193 ? 19.485  1.952   13.120  1.00 45.18 ? 193  ASP B OD2 1 
ATOM   4193 N  N   . PRO B 1 194 ? 22.448  5.666   12.367  1.00 41.73 ? 194  PRO B N   1 
ATOM   4194 C  CA  . PRO B 1 194 ? 23.812  5.481   11.859  1.00 43.38 ? 194  PRO B CA  1 
ATOM   4195 C  C   . PRO B 1 194 ? 24.134  4.060   11.405  1.00 43.29 ? 194  PRO B C   1 
ATOM   4196 O  O   . PRO B 1 194 ? 24.950  3.879   10.511  1.00 42.36 ? 194  PRO B O   1 
ATOM   4197 C  CB  . PRO B 1 194 ? 24.696  5.849   13.058  1.00 43.59 ? 194  PRO B CB  1 
ATOM   4198 C  CG  . PRO B 1 194 ? 23.863  6.748   13.897  1.00 43.61 ? 194  PRO B CG  1 
ATOM   4199 C  CD  . PRO B 1 194 ? 22.435  6.325   13.688  1.00 42.75 ? 194  PRO B CD  1 
ATOM   4200 N  N   . ASN B 1 195 ? 23.493  3.066   12.008  1.00 46.35 ? 195  ASN B N   1 
ATOM   4201 C  CA  . ASN B 1 195 ? 23.771  1.665   11.686  1.00 46.51 ? 195  ASN B CA  1 
ATOM   4202 C  C   . ASN B 1 195 ? 23.086  1.156   10.409  1.00 44.10 ? 195  ASN B C   1 
ATOM   4203 O  O   . ASN B 1 195 ? 23.403  0.068   9.933   1.00 43.74 ? 195  ASN B O   1 
ATOM   4204 C  CB  . ASN B 1 195 ? 23.405  0.770   12.881  1.00 49.79 ? 195  ASN B CB  1 
ATOM   4205 C  CG  . ASN B 1 195 ? 24.078  1.211   14.181  1.00 51.96 ? 195  ASN B CG  1 
ATOM   4206 O  OD1 . ASN B 1 195 ? 23.594  0.908   15.270  1.00 54.98 ? 195  ASN B OD1 1 
ATOM   4207 N  ND2 . ASN B 1 195 ? 25.187  1.938   14.070  1.00 53.32 ? 195  ASN B ND2 1 
ATOM   4208 N  N   . SER B 1 196 ? 22.149  1.923   9.855   1.00 42.39 ? 196  SER B N   1 
ATOM   4209 C  CA  . SER B 1 196 ? 21.535  1.560   8.570   1.00 42.18 ? 196  SER B CA  1 
ATOM   4210 C  C   . SER B 1 196 ? 22.398  2.013   7.383   1.00 40.67 ? 196  SER B C   1 
ATOM   4211 O  O   . SER B 1 196 ? 22.145  1.621   6.245   1.00 41.04 ? 196  SER B O   1 
ATOM   4212 C  CB  . SER B 1 196 ? 20.143  2.173   8.450   1.00 42.67 ? 196  SER B CB  1 
ATOM   4213 O  OG  . SER B 1 196 ? 20.210  3.588   8.548   1.00 45.12 ? 196  SER B OG  1 
ATOM   4214 N  N   . LEU B 1 197 ? 23.412  2.833   7.656   1.00 37.63 ? 197  LEU B N   1 
ATOM   4215 C  CA  . LEU B 1 197 ? 24.289  3.376   6.621   1.00 36.53 ? 197  LEU B CA  1 
ATOM   4216 C  C   . LEU B 1 197 ? 25.174  2.293   6.048   1.00 36.96 ? 197  LEU B C   1 
ATOM   4217 O  O   . LEU B 1 197 ? 25.691  1.464   6.793   1.00 42.07 ? 197  LEU B O   1 
ATOM   4218 C  CB  . LEU B 1 197 ? 25.184  4.474   7.215   1.00 35.29 ? 197  LEU B CB  1 
ATOM   4219 C  CG  . LEU B 1 197 ? 24.453  5.663   7.828   1.00 33.72 ? 197  LEU B CG  1 
ATOM   4220 C  CD1 . LEU B 1 197 ? 25.442  6.627   8.448   1.00 33.59 ? 197  LEU B CD1 1 
ATOM   4221 C  CD2 . LEU B 1 197 ? 23.605  6.360   6.775   1.00 35.02 ? 197  LEU B CD2 1 
ATOM   4222 N  N   . THR B 1 198 ? 25.369  2.306   4.735   1.00 35.82 ? 198  THR B N   1 
ATOM   4223 C  CA  . THR B 1 198 ? 26.304  1.384   4.093   1.00 34.76 ? 198  THR B CA  1 
ATOM   4224 C  C   . THR B 1 198 ? 27.727  1.862   4.365   1.00 37.16 ? 198  THR B C   1 
ATOM   4225 O  O   . THR B 1 198 ? 27.919  2.940   4.949   1.00 34.56 ? 198  THR B O   1 
ATOM   4226 C  CB  . THR B 1 198 ? 26.101  1.344   2.574   1.00 35.61 ? 198  THR B CB  1 
ATOM   4227 O  OG1 . THR B 1 198 ? 26.426  2.624   2.007   1.00 35.68 ? 198  THR B OG1 1 
ATOM   4228 C  CG2 . THR B 1 198 ? 24.653  0.967   2.231   1.00 35.59 ? 198  THR B CG2 1 
ATOM   4229 N  N   . ASP B 1 199 ? 28.719  1.076   3.934   1.00 37.02 ? 199  ASP B N   1 
ATOM   4230 C  CA  . ASP B 1 199 ? 30.121  1.482   4.058   1.00 37.40 ? 199  ASP B CA  1 
ATOM   4231 C  C   . ASP B 1 199 ? 30.456  2.653   3.130   1.00 35.05 ? 199  ASP B C   1 
ATOM   4232 O  O   . ASP B 1 199 ? 31.129  3.584   3.543   1.00 35.14 ? 199  ASP B O   1 
ATOM   4233 C  CB  . ASP B 1 199 ? 31.081  0.315   3.802   1.00 37.50 ? 199  ASP B CB  1 
ATOM   4234 C  CG  . ASP B 1 199 ? 31.183  -0.644  4.996   1.00 39.02 ? 199  ASP B CG  1 
ATOM   4235 O  OD1 . ASP B 1 199 ? 30.972  -0.237  6.156   1.00 39.07 ? 199  ASP B OD1 1 
ATOM   4236 O  OD2 . ASP B 1 199 ? 31.486  -1.824  4.767   1.00 42.13 ? 199  ASP B OD2 1 
ATOM   4237 N  N   . ASP B 1 200 ? 29.970  2.611   1.895   1.00 33.31 ? 200  ASP B N   1 
ATOM   4238 C  CA  . ASP B 1 200 ? 30.194  3.707   0.941   1.00 33.14 ? 200  ASP B CA  1 
ATOM   4239 C  C   . ASP B 1 200 ? 29.609  5.011   1.447   1.00 29.57 ? 200  ASP B C   1 
ATOM   4240 O  O   . ASP B 1 200 ? 30.194  6.067   1.261   1.00 28.42 ? 200  ASP B O   1 
ATOM   4241 C  CB  . ASP B 1 200 ? 29.590  3.390   -0.433  1.00 33.63 ? 200  ASP B CB  1 
ATOM   4242 C  CG  . ASP B 1 200 ? 30.358  2.313   -1.172  1.00 36.90 ? 200  ASP B CG  1 
ATOM   4243 O  OD1 . ASP B 1 200 ? 31.501  2.010   -0.766  1.00 37.36 ? 200  ASP B OD1 1 
ATOM   4244 O  OD2 . ASP B 1 200 ? 29.819  1.766   -2.164  1.00 38.68 ? 200  ASP B OD2 1 
ATOM   4245 N  N   . GLN B 1 201 ? 28.449  4.918   2.080   1.00 29.82 ? 201  GLN B N   1 
ATOM   4246 C  CA  . GLN B 1 201 ? 27.771  6.080   2.632   1.00 30.84 ? 201  GLN B CA  1 
ATOM   4247 C  C   . GLN B 1 201 ? 28.546  6.660   3.806   1.00 30.39 ? 201  GLN B C   1 
ATOM   4248 O  O   . GLN B 1 201 ? 28.652  7.874   3.928   1.00 28.96 ? 201  GLN B O   1 
ATOM   4249 C  CB  . GLN B 1 201 ? 26.339  5.722   3.040   1.00 31.76 ? 201  GLN B CB  1 
ATOM   4250 C  CG  . GLN B 1 201 ? 25.425  5.541   1.836   1.00 32.54 ? 201  GLN B CG  1 
ATOM   4251 C  CD  . GLN B 1 201 ? 24.075  4.934   2.184   1.00 33.35 ? 201  GLN B CD  1 
ATOM   4252 O  OE1 . GLN B 1 201 ? 23.799  4.574   3.329   1.00 34.28 ? 201  GLN B OE1 1 
ATOM   4253 N  NE2 . GLN B 1 201 ? 23.228  4.808   1.181   1.00 34.37 ? 201  GLN B NE2 1 
ATOM   4254 N  N   . ILE B 1 202 ? 29.114  5.789   4.644   1.00 31.36 ? 202  ILE B N   1 
ATOM   4255 C  CA  . ILE B 1 202 ? 29.941  6.239   5.771   1.00 30.35 ? 202  ILE B CA  1 
ATOM   4256 C  C   . ILE B 1 202 ? 31.172  6.968   5.253   1.00 28.53 ? 202  ILE B C   1 
ATOM   4257 O  O   . ILE B 1 202 ? 31.455  8.071   5.720   1.00 26.70 ? 202  ILE B O   1 
ATOM   4258 C  CB  . ILE B 1 202 ? 30.352  5.074   6.711   1.00 31.90 ? 202  ILE B CB  1 
ATOM   4259 C  CG1 . ILE B 1 202 ? 29.128  4.556   7.476   1.00 32.68 ? 202  ILE B CG1 1 
ATOM   4260 C  CG2 . ILE B 1 202 ? 31.438  5.522   7.706   1.00 31.98 ? 202  ILE B CG2 1 
ATOM   4261 C  CD1 . ILE B 1 202 ? 29.280  3.135   7.999   1.00 32.53 ? 202  ILE B CD1 1 
ATOM   4262 N  N   . LYS B 1 203 ? 31.886  6.389   4.283   1.00 27.95 ? 203  LYS B N   1 
ATOM   4263 C  CA  . LYS B 1 203 ? 33.103  7.050   3.789   1.00 30.26 ? 203  LYS B CA  1 
ATOM   4264 C  C   . LYS B 1 203 ? 32.841  8.381   3.053   1.00 26.72 ? 203  LYS B C   1 
ATOM   4265 O  O   . LYS B 1 203 ? 33.660  9.301   3.134   1.00 24.14 ? 203  LYS B O   1 
ATOM   4266 C  CB  . LYS B 1 203 ? 34.003  6.106   2.977   1.00 34.18 ? 203  LYS B CB  1 
ATOM   4267 C  CG  . LYS B 1 203 ? 33.512  5.724   1.604   1.00 38.82 ? 203  LYS B CG  1 
ATOM   4268 C  CD  . LYS B 1 203 ? 34.646  5.082   0.816   1.00 42.00 ? 203  LYS B CD  1 
ATOM   4269 C  CE  . LYS B 1 203 ? 34.141  4.227   -0.342  1.00 44.40 ? 203  LYS B CE  1 
ATOM   4270 N  NZ  . LYS B 1 203 ? 33.785  5.017   -1.553  1.00 45.50 ? 203  LYS B NZ  1 
ATOM   4271 N  N   . ALA B 1 204 ? 31.683  8.487   2.392   1.00 24.97 ? 204  ALA B N   1 
ATOM   4272 C  CA  . ALA B 1 204 ? 31.241  9.745   1.780   1.00 24.32 ? 204  ALA B CA  1 
ATOM   4273 C  C   . ALA B 1 204 ? 30.979  10.837  2.831   1.00 23.51 ? 204  ALA B C   1 
ATOM   4274 O  O   . ALA B 1 204 ? 31.426  11.970  2.692   1.00 23.12 ? 204  ALA B O   1 
ATOM   4275 C  CB  . ALA B 1 204 ? 29.994  9.506   0.932   1.00 24.01 ? 204  ALA B CB  1 
ATOM   4276 N  N   . LEU B 1 205 ? 30.268  10.488  3.893   1.00 24.31 ? 205  LEU B N   1 
ATOM   4277 C  CA  . LEU B 1 205 ? 30.019  11.442  4.980   1.00 24.56 ? 205  LEU B CA  1 
ATOM   4278 C  C   . LEU B 1 205 ? 31.310  11.883  5.667   1.00 23.30 ? 205  LEU B C   1 
ATOM   4279 O  O   . LEU B 1 205 ? 31.482  13.056  5.966   1.00 22.19 ? 205  LEU B O   1 
ATOM   4280 C  CB  . LEU B 1 205 ? 29.045  10.848  6.002   1.00 25.37 ? 205  LEU B CB  1 
ATOM   4281 C  CG  . LEU B 1 205 ? 27.610  10.733  5.475   1.00 27.02 ? 205  LEU B CG  1 
ATOM   4282 C  CD1 . LEU B 1 205 ? 26.816  9.748   6.331   1.00 27.91 ? 205  LEU B CD1 1 
ATOM   4283 C  CD2 . LEU B 1 205 ? 26.914  12.101  5.397   1.00 27.17 ? 205  LEU B CD2 1 
ATOM   4284 N  N   . ASN B 1 206 ? 32.228  10.941  5.874   1.00 22.76 ? 206  ASN B N   1 
ATOM   4285 C  CA  . ASN B 1 206 ? 33.523  11.224  6.501   1.00 23.35 ? 206  ASN B CA  1 
ATOM   4286 C  C   . ASN B 1 206 ? 34.468  12.080  5.652   1.00 23.43 ? 206  ASN B C   1 
ATOM   4287 O  O   . ASN B 1 206 ? 35.360  12.711  6.181   1.00 23.81 ? 206  ASN B O   1 
ATOM   4288 C  CB  . ASN B 1 206 ? 34.219  9.912   6.895   1.00 22.74 ? 206  ASN B CB  1 
ATOM   4289 C  CG  . ASN B 1 206 ? 33.629  9.292   8.145   1.00 21.63 ? 206  ASN B CG  1 
ATOM   4290 O  OD1 . ASN B 1 206 ? 32.946  9.956   8.906   1.00 21.01 ? 206  ASN B OD1 1 
ATOM   4291 N  ND2 . ASN B 1 206 ? 33.893  8.001   8.359   1.00 22.71 ? 206  ASN B ND2 1 
ATOM   4292 N  N   . LYS B 1 207 ? 34.254  12.095  4.344   1.00 25.03 ? 207  LYS B N   1 
ATOM   4293 C  CA  . LYS B 1 207 ? 34.985  12.959  3.440   1.00 26.68 ? 207  LYS B CA  1 
ATOM   4294 C  C   . LYS B 1 207 ? 34.367  14.350  3.315   1.00 25.60 ? 207  LYS B C   1 
ATOM   4295 O  O   . LYS B 1 207 ? 35.002  15.245  2.797   1.00 26.37 ? 207  LYS B O   1 
ATOM   4296 C  CB  . LYS B 1 207 ? 35.005  12.359  2.039   1.00 31.20 ? 207  LYS B CB  1 
ATOM   4297 C  CG  . LYS B 1 207 ? 36.082  11.323  1.806   1.00 34.73 ? 207  LYS B CG  1 
ATOM   4298 C  CD  . LYS B 1 207 ? 36.028  10.829  0.367   1.00 36.70 ? 207  LYS B CD  1 
ATOM   4299 C  CE  . LYS B 1 207 ? 36.284  11.959  -0.609  1.00 37.70 ? 207  LYS B CE  1 
ATOM   4300 N  NZ  . LYS B 1 207 ? 36.681  11.417  -1.931  1.00 41.22 ? 207  LYS B NZ  1 
ATOM   4301 N  N   . MET B 1 208 ? 33.130  14.525  3.767   1.00 24.68 ? 208  MET B N   1 
ATOM   4302 C  CA  . MET B 1 208 ? 32.439  15.782  3.608   1.00 23.32 ? 208  MET B CA  1 
ATOM   4303 C  C   . MET B 1 208 ? 33.209  16.890  4.334   1.00 23.67 ? 208  MET B C   1 
ATOM   4304 O  O   . MET B 1 208 ? 33.612  16.741  5.499   1.00 22.22 ? 208  MET B O   1 
ATOM   4305 C  CB  . MET B 1 208 ? 31.000  15.664  4.140   1.00 23.07 ? 208  MET B CB  1 
ATOM   4306 C  CG  . MET B 1 208 ? 30.154  16.917  3.982   1.00 23.80 ? 208  MET B CG  1 
ATOM   4307 S  SD  . MET B 1 208 ? 29.922  17.462  2.265   1.00 22.23 ? 208  MET B SD  1 
ATOM   4308 C  CE  . MET B 1 208 ? 29.013  16.070  1.601   1.00 23.19 ? 208  MET B CE  1 
ATOM   4309 N  N   . ASN B 1 209 ? 33.441  17.985  3.624   1.00 23.27 ? 209  ASN B N   1 
ATOM   4310 C  CA  . ASN B 1 209 ? 33.983  19.185  4.222   1.00 23.96 ? 209  ASN B CA  1 
ATOM   4311 C  C   . ASN B 1 209 ? 32.816  20.066  4.661   1.00 25.04 ? 209  ASN B C   1 
ATOM   4312 O  O   . ASN B 1 209 ? 32.173  20.730  3.836   1.00 23.77 ? 209  ASN B O   1 
ATOM   4313 C  CB  . ASN B 1 209 ? 34.901  19.904  3.221   1.00 24.61 ? 209  ASN B CB  1 
ATOM   4314 C  CG  . ASN B 1 209 ? 35.470  21.203  3.760   1.00 26.73 ? 209  ASN B CG  1 
ATOM   4315 O  OD1 . ASN B 1 209 ? 35.066  21.694  4.811   1.00 28.71 ? 209  ASN B OD1 1 
ATOM   4316 N  ND2 . ASN B 1 209 ? 36.409  21.775  3.029   1.00 28.74 ? 209  ASN B ND2 1 
ATOM   4317 N  N   . PHE B 1 210 ? 32.547  20.057  5.966   1.00 27.25 ? 210  PHE B N   1 
ATOM   4318 C  CA  . PHE B 1 210 ? 31.497  20.885  6.578   1.00 28.73 ? 210  PHE B CA  1 
ATOM   4319 C  C   . PHE B 1 210 ? 31.965  22.309  6.939   1.00 33.32 ? 210  PHE B C   1 
ATOM   4320 O  O   . PHE B 1 210 ? 31.166  23.115  7.418   1.00 31.72 ? 210  PHE B O   1 
ATOM   4321 C  CB  . PHE B 1 210 ? 30.988  20.212  7.855   1.00 27.18 ? 210  PHE B CB  1 
ATOM   4322 C  CG  . PHE B 1 210 ? 30.301  18.888  7.627   1.00 26.67 ? 210  PHE B CG  1 
ATOM   4323 C  CD1 . PHE B 1 210 ? 28.933  18.836  7.376   1.00 25.54 ? 210  PHE B CD1 1 
ATOM   4324 C  CD2 . PHE B 1 210 ? 31.008  17.698  7.701   1.00 25.93 ? 210  PHE B CD2 1 
ATOM   4325 C  CE1 . PHE B 1 210 ? 28.294  17.627  7.178   1.00 26.07 ? 210  PHE B CE1 1 
ATOM   4326 C  CE2 . PHE B 1 210 ? 30.369  16.482  7.512   1.00 26.65 ? 210  PHE B CE2 1 
ATOM   4327 C  CZ  . PHE B 1 210 ? 29.008  16.444  7.259   1.00 26.40 ? 210  PHE B CZ  1 
ATOM   4328 N  N   . SER B 1 211 ? 33.240  22.608  6.746   1.00 37.81 ? 211  SER B N   1 
ATOM   4329 C  CA  . SER B 1 211 ? 33.789  23.899  7.171   1.00 41.51 ? 211  SER B CA  1 
ATOM   4330 C  C   . SER B 1 211 ? 33.859  25.033  6.183   1.00 47.02 ? 211  SER B C   1 
ATOM   4331 O  O   . SER B 1 211 ? 33.611  26.176  6.557   1.00 50.82 ? 211  SER B O   1 
ATOM   4332 C  CB  . SER B 1 211 ? 35.169  23.722  7.755   1.00 39.96 ? 211  SER B CB  1 
ATOM   4333 O  OG  . SER B 1 211 ? 36.079  23.378  6.760   1.00 37.41 ? 211  SER B OG  1 
ATOM   4334 N  N   . LYS B 1 212 ? 34.261  24.700  4.968   1.00 51.27 ? 212  LYS B N   1 
ATOM   4335 C  CA  . LYS B 1 212 ? 34.427  25.617  3.864   1.00 54.28 ? 212  LYS B CA  1 
ATOM   4336 C  C   . LYS B 1 212 ? 33.338  26.680  3.816   1.00 56.98 ? 212  LYS B C   1 
ATOM   4337 O  O   . LYS B 1 212 ? 32.183  26.368  3.756   1.00 61.66 ? 212  LYS B O   1 
ATOM   4338 C  CB  . LYS B 1 212 ? 34.449  24.817  2.580   1.00 55.67 ? 212  LYS B CB  1 
ATOM   4339 C  CG  . LYS B 1 212 ? 35.050  25.540  1.394   1.00 57.01 ? 212  LYS B CG  1 
ATOM   4340 C  CD  . LYS B 1 212 ? 34.289  25.243  0.133   1.00 59.68 ? 212  LYS B CD  1 
ATOM   4341 C  CE  . LYS B 1 212 ? 35.189  25.068  -1.071  1.00 61.77 ? 212  LYS B CE  1 
ATOM   4342 N  NZ  . LYS B 1 212 ? 36.002  26.225  -1.519  1.00 62.39 ? 212  LYS B NZ  1 
ATOM   4343 N  N   . ALA B 1 213 ? 33.725  27.924  3.968   1.00 57.99 ? 213  ALA B N   1 
ATOM   4344 C  CA  . ALA B 1 213 ? 32.825  29.061  3.945   1.00 58.43 ? 213  ALA B CA  1 
ATOM   4345 C  C   . ALA B 1 213 ? 32.732  29.585  2.533   1.00 59.83 ? 213  ALA B C   1 
ATOM   4346 O  O   . ALA B 1 213 ? 33.576  29.287  1.724   1.00 59.53 ? 213  ALA B O   1 
ATOM   4347 C  CB  . ALA B 1 213 ? 33.381  30.149  4.829   1.00 57.40 ? 213  ALA B CB  1 
ATOM   4348 N  N   . ALA B 1 214 ? 31.721  30.369  2.222   1.00 61.60 ? 214  ALA B N   1 
ATOM   4349 C  CA  . ALA B 1 214 ? 31.648  30.874  0.874   1.00 65.95 ? 214  ALA B CA  1 
ATOM   4350 C  C   . ALA B 1 214 ? 32.533  32.090  0.718   1.00 69.52 ? 214  ALA B C   1 
ATOM   4351 O  O   . ALA B 1 214 ? 32.680  32.900  1.625   1.00 69.59 ? 214  ALA B O   1 
ATOM   4352 C  CB  . ALA B 1 214 ? 30.225  31.183  0.459   1.00 65.46 ? 214  ALA B CB  1 
ATOM   4353 N  N   . LYS B 1 215 ? 33.144  32.187  -0.440  1.00 74.18 ? 215  LYS B N   1 
ATOM   4354 C  CA  . LYS B 1 215 ? 34.037  33.290  -0.763  1.00 77.77 ? 215  LYS B CA  1 
ATOM   4355 C  C   . LYS B 1 215 ? 33.431  34.711  -0.820  1.00 79.02 ? 215  LYS B C   1 
ATOM   4356 O  O   . LYS B 1 215 ? 33.436  35.445  0.174   1.00 84.17 ? 215  LYS B O   1 
ATOM   4357 C  CB  . LYS B 1 215 ? 34.853  32.951  -2.020  1.00 77.73 ? 215  LYS B CB  1 
ATOM   4358 C  CG  . LYS B 1 215 ? 36.279  32.446  -1.698  1.00 76.54 ? 215  LYS B CG  1 
ATOM   4359 C  CD  . LYS B 1 215 ? 37.369  33.468  -2.018  1.00 76.23 ? 215  LYS B CD  1 
ATOM   4360 C  CE  . LYS B 1 215 ? 38.583  33.429  -1.090  1.00 75.56 ? 215  LYS B CE  1 
ATOM   4361 N  NZ  . LYS B 1 215 ? 39.132  34.762  -0.633  1.00 74.41 ? 215  LYS B NZ  1 
ATOM   4362 N  N   . GLY B 1 217 ? 30.339  35.759  -3.057  1.00 56.48 ? 217  GLY B N   1 
ATOM   4363 C  CA  . GLY B 1 217 ? 29.253  35.756  -3.982  1.00 48.63 ? 217  GLY B CA  1 
ATOM   4364 C  C   . GLY B 1 217 ? 28.289  34.741  -3.444  1.00 42.54 ? 217  GLY B C   1 
ATOM   4365 O  O   . GLY B 1 217 ? 28.637  33.790  -2.776  1.00 48.71 ? 217  GLY B O   1 
ATOM   4366 N  N   . THR B 1 218 ? 27.067  34.914  -3.799  1.00 33.81 ? 218  THR B N   1 
ATOM   4367 C  CA  . THR B 1 218 ? 26.027  34.036  -3.416  1.00 28.71 ? 218  THR B CA  1 
ATOM   4368 C  C   . THR B 1 218 ? 26.104  32.801  -4.303  1.00 25.11 ? 218  THR B C   1 
ATOM   4369 O  O   . THR B 1 218 ? 26.553  32.870  -5.386  1.00 24.05 ? 218  THR B O   1 
ATOM   4370 C  CB  . THR B 1 218 ? 24.747  34.809  -3.660  1.00 27.49 ? 218  THR B CB  1 
ATOM   4371 O  OG1 . THR B 1 218 ? 24.752  35.937  -2.820  1.00 27.45 ? 218  THR B OG1 1 
ATOM   4372 C  CG2 . THR B 1 218 ? 23.504  34.029  -3.458  1.00 27.75 ? 218  THR B CG2 1 
ATOM   4373 N  N   . GLN B 1 219 ? 25.679  31.668  -3.821  1.00 23.04 ? 219  GLN B N   1 
ATOM   4374 C  CA  . GLN B 1 219 ? 25.642  30.509  -4.648  1.00 22.88 ? 219  GLN B CA  1 
ATOM   4375 C  C   . GLN B 1 219 ? 24.218  30.024  -4.921  1.00 21.51 ? 219  GLN B C   1 
ATOM   4376 O  O   . GLN B 1 219 ? 23.351  30.227  -4.140  1.00 20.27 ? 219  GLN B O   1 
ATOM   4377 C  CB  . GLN B 1 219 ? 26.391  29.357  -3.995  1.00 23.26 ? 219  GLN B CB  1 
ATOM   4378 C  CG  . GLN B 1 219 ? 27.897  29.360  -4.072  1.00 23.44 ? 219  GLN B CG  1 
ATOM   4379 C  CD  . GLN B 1 219 ? 28.524  28.226  -3.291  1.00 25.05 ? 219  GLN B CD  1 
ATOM   4380 O  OE1 . GLN B 1 219 ? 28.111  27.111  -3.361  1.00 26.51 ? 219  GLN B OE1 1 
ATOM   4381 N  NE2 . GLN B 1 219 ? 29.498  28.538  -2.533  1.00 25.50 ? 219  GLN B NE2 1 
ATOM   4382 N  N   . MET B 1 220 ? 24.004  29.475  -6.097  1.00 20.44 ? 220  MET B N   1 
ATOM   4383 C  CA  . MET B 1 220 ? 22.796  28.707  -6.338  1.00 19.86 ? 220  MET B CA  1 
ATOM   4384 C  C   . MET B 1 220 ? 23.099  27.328  -5.793  1.00 18.83 ? 220  MET B C   1 
ATOM   4385 O  O   . MET B 1 220 ? 23.850  26.579  -6.409  1.00 17.86 ? 220  MET B O   1 
ATOM   4386 C  CB  . MET B 1 220 ? 22.466  28.617  -7.833  1.00 19.69 ? 220  MET B CB  1 
ATOM   4387 C  CG  . MET B 1 220 ? 21.205  27.799  -8.105  1.00 19.90 ? 220  MET B CG  1 
ATOM   4388 S  SD  . MET B 1 220 ? 20.918  27.507  -9.854  1.00 20.05 ? 220  MET B SD  1 
ATOM   4389 C  CE  . MET B 1 220 ? 20.301  29.115  -10.370 1.00 19.65 ? 220  MET B CE  1 
ATOM   4390 N  N   . THR B 1 221 ? 22.520  26.999  -4.639  1.00 19.14 ? 221  THR B N   1 
ATOM   4391 C  CA  . THR B 1 221 ? 22.769  25.705  -3.989  1.00 19.22 ? 221  THR B CA  1 
ATOM   4392 C  C   . THR B 1 221 ? 21.963  24.587  -4.653  1.00 18.60 ? 221  THR B C   1 
ATOM   4393 O  O   . THR B 1 221 ? 21.135  24.831  -5.533  1.00 18.02 ? 221  THR B O   1 
ATOM   4394 C  CB  . THR B 1 221 ? 22.447  25.759  -2.478  1.00 20.52 ? 221  THR B CB  1 
ATOM   4395 O  OG1 . THR B 1 221 ? 21.042  25.989  -2.263  1.00 20.67 ? 221  THR B OG1 1 
ATOM   4396 C  CG2 . THR B 1 221 ? 23.237  26.896  -1.807  1.00 20.75 ? 221  THR B CG2 1 
ATOM   4397 N  N   . TYR B 1 222 ? 22.216  23.357  -4.224  1.00 18.19 ? 222  TYR B N   1 
ATOM   4398 C  CA  . TYR B 1 222 ? 21.527  22.207  -4.772  1.00 17.49 ? 222  TYR B CA  1 
ATOM   4399 C  C   . TYR B 1 222 ? 20.058  22.280  -4.362  1.00 17.71 ? 222  TYR B C   1 
ATOM   4400 O  O   . TYR B 1 222 ? 19.156  21.935  -5.124  1.00 17.13 ? 222  TYR B O   1 
ATOM   4401 C  CB  . TYR B 1 222 ? 22.187  20.933  -4.261  1.00 17.62 ? 222  TYR B CB  1 
ATOM   4402 C  CG  . TYR B 1 222 ? 21.873  19.703  -5.059  1.00 17.93 ? 222  TYR B CG  1 
ATOM   4403 C  CD1 . TYR B 1 222 ? 22.527  19.454  -6.271  1.00 17.95 ? 222  TYR B CD1 1 
ATOM   4404 C  CD2 . TYR B 1 222 ? 20.947  18.764  -4.603  1.00 18.38 ? 222  TYR B CD2 1 
ATOM   4405 C  CE1 . TYR B 1 222 ? 22.255  18.314  -7.006  1.00 17.92 ? 222  TYR B CE1 1 
ATOM   4406 C  CE2 . TYR B 1 222 ? 20.673  17.610  -5.344  1.00 18.33 ? 222  TYR B CE2 1 
ATOM   4407 C  CZ  . TYR B 1 222 ? 21.329  17.398  -6.542  1.00 17.73 ? 222  TYR B CZ  1 
ATOM   4408 O  OH  . TYR B 1 222 ? 21.066  16.269  -7.295  1.00 18.54 ? 222  TYR B OH  1 
ATOM   4409 N  N   . ASN B 1 223 ? 19.833  22.776  -3.158  1.00 18.15 ? 223  ASN B N   1 
ATOM   4410 C  CA  . ASN B 1 223 ? 18.490  22.987  -2.636  1.00 19.08 ? 223  ASN B CA  1 
ATOM   4411 C  C   . ASN B 1 223 ? 17.742  24.081  -3.425  1.00 18.67 ? 223  ASN B C   1 
ATOM   4412 O  O   . ASN B 1 223 ? 16.604  23.870  -3.819  1.00 17.99 ? 223  ASN B O   1 
ATOM   4413 C  CB  . ASN B 1 223 ? 18.571  23.326  -1.136  1.00 19.77 ? 223  ASN B CB  1 
ATOM   4414 C  CG  . ASN B 1 223 ? 17.210  23.315  -0.449  1.00 20.64 ? 223  ASN B CG  1 
ATOM   4415 O  OD1 . ASN B 1 223 ? 16.781  24.317  0.038   1.00 24.92 ? 223  ASN B OD1 1 
ATOM   4416 N  ND2 . ASN B 1 223 ? 16.549  22.183  -0.410  1.00 20.75 ? 223  ASN B ND2 1 
ATOM   4417 N  N   . ASP B 1 224 ? 18.397  25.220  -3.682  1.00 18.45 ? 224  ASP B N   1 
ATOM   4418 C  CA  . ASP B 1 224 ? 17.801  26.279  -4.518  1.00 18.74 ? 224  ASP B CA  1 
ATOM   4419 C  C   . ASP B 1 224 ? 17.330  25.723  -5.849  1.00 18.41 ? 224  ASP B C   1 
ATOM   4420 O  O   . ASP B 1 224 ? 16.210  25.974  -6.268  1.00 17.46 ? 224  ASP B O   1 
ATOM   4421 C  CB  . ASP B 1 224 ? 18.787  27.407  -4.816  1.00 18.92 ? 224  ASP B CB  1 
ATOM   4422 C  CG  . ASP B 1 224 ? 19.146  28.215  -3.595  1.00 19.80 ? 224  ASP B CG  1 
ATOM   4423 O  OD1 . ASP B 1 224 ? 18.322  28.324  -2.668  1.00 21.08 ? 224  ASP B OD1 1 
ATOM   4424 O  OD2 . ASP B 1 224 ? 20.261  28.754  -3.574  1.00 20.30 ? 224  ASP B OD2 1 
ATOM   4425 N  N   . PHE B 1 225 ? 18.210  24.980  -6.508  1.00 18.56 ? 225  PHE B N   1 
ATOM   4426 C  CA  . PHE B 1 225 ? 17.941  24.411  -7.829  1.00 18.70 ? 225  PHE B CA  1 
ATOM   4427 C  C   . PHE B 1 225 ? 16.695  23.508  -7.749  1.00 20.30 ? 225  PHE B C   1 
ATOM   4428 O  O   . PHE B 1 225 ? 15.788  23.585  -8.577  1.00 20.24 ? 225  PHE B O   1 
ATOM   4429 C  CB  . PHE B 1 225 ? 19.192  23.643  -8.327  1.00 17.96 ? 225  PHE B CB  1 
ATOM   4430 C  CG  . PHE B 1 225 ? 19.073  23.093  -9.727  1.00 17.29 ? 225  PHE B CG  1 
ATOM   4431 C  CD1 . PHE B 1 225 ? 18.437  21.892  -9.960  1.00 17.15 ? 225  PHE B CD1 1 
ATOM   4432 C  CD2 . PHE B 1 225 ? 19.585  23.792  -10.811 1.00 17.29 ? 225  PHE B CD2 1 
ATOM   4433 C  CE1 . PHE B 1 225 ? 18.308  21.395  -11.244 1.00 16.94 ? 225  PHE B CE1 1 
ATOM   4434 C  CE2 . PHE B 1 225 ? 19.467  23.306  -12.094 1.00 16.89 ? 225  PHE B CE2 1 
ATOM   4435 C  CZ  . PHE B 1 225 ? 18.824  22.099  -12.312 1.00 16.88 ? 225  PHE B CZ  1 
ATOM   4436 N  N   . GLN B 1 226 ? 16.654  22.660  -6.732  1.00 21.58 ? 226  GLN B N   1 
ATOM   4437 C  CA  . GLN B 1 226 ? 15.546  21.755  -6.536  1.00 21.93 ? 226  GLN B CA  1 
ATOM   4438 C  C   . GLN B 1 226 ? 14.236  22.535  -6.368  1.00 21.39 ? 226  GLN B C   1 
ATOM   4439 O  O   . GLN B 1 226 ? 13.199  22.151  -6.903  1.00 20.39 ? 226  GLN B O   1 
ATOM   4440 C  CB  . GLN B 1 226 ? 15.823  20.916  -5.300  1.00 23.89 ? 226  GLN B CB  1 
ATOM   4441 C  CG  . GLN B 1 226 ? 14.694  20.007  -4.876  1.00 26.32 ? 226  GLN B CG  1 
ATOM   4442 C  CD  . GLN B 1 226 ? 14.777  18.692  -5.583  1.00 27.98 ? 226  GLN B CD  1 
ATOM   4443 O  OE1 . GLN B 1 226 ? 15.607  17.850  -5.237  1.00 30.69 ? 226  GLN B OE1 1 
ATOM   4444 N  NE2 . GLN B 1 226 ? 13.951  18.518  -6.604  1.00 28.99 ? 226  GLN B NE2 1 
ATOM   4445 N  N   . LYS B 1 227 ? 14.291  23.632  -5.622  1.00 20.56 ? 227  LYS B N   1 
ATOM   4446 C  CA  . LYS B 1 227 ? 13.102  24.439  -5.382  1.00 20.78 ? 227  LYS B CA  1 
ATOM   4447 C  C   . LYS B 1 227 ? 12.667  25.163  -6.636  1.00 19.93 ? 227  LYS B C   1 
ATOM   4448 O  O   . LYS B 1 227 ? 11.468  25.324  -6.883  1.00 19.81 ? 227  LYS B O   1 
ATOM   4449 C  CB  . LYS B 1 227 ? 13.340  25.456  -4.278  1.00 21.45 ? 227  LYS B CB  1 
ATOM   4450 C  CG  . LYS B 1 227 ? 13.426  24.867  -2.878  1.00 22.86 ? 227  LYS B CG  1 
ATOM   4451 C  CD  . LYS B 1 227 ? 13.585  26.005  -1.903  1.00 24.30 ? 227  LYS B CD  1 
ATOM   4452 C  CE  . LYS B 1 227 ? 13.470  25.574  -0.477  1.00 26.75 ? 227  LYS B CE  1 
ATOM   4453 N  NZ  . LYS B 1 227 ? 13.704  26.762  0.391   1.00 28.47 ? 227  LYS B NZ  1 
ATOM   4454 N  N   . ILE B 1 228 ? 13.632  25.612  -7.422  1.00 19.49 ? 228  ILE B N   1 
ATOM   4455 C  CA  . ILE B 1 228 ? 13.306  26.266  -8.688  1.00 18.75 ? 228  ILE B CA  1 
ATOM   4456 C  C   . ILE B 1 228 ? 12.574  25.257  -9.558  1.00 18.43 ? 228  ILE B C   1 
ATOM   4457 O  O   . ILE B 1 228 ? 11.523  25.556  -10.115 1.00 17.73 ? 228  ILE B O   1 
ATOM   4458 C  CB  . ILE B 1 228 ? 14.556  26.827  -9.396  1.00 18.92 ? 228  ILE B CB  1 
ATOM   4459 C  CG1 . ILE B 1 228 ? 15.158  27.982  -8.581  1.00 19.04 ? 228  ILE B CG1 1 
ATOM   4460 C  CG2 . ILE B 1 228 ? 14.197  27.335  -10.795 1.00 19.01 ? 228  ILE B CG2 1 
ATOM   4461 C  CD1 . ILE B 1 228 ? 16.602  28.300  -8.943  1.00 19.47 ? 228  ILE B CD1 1 
ATOM   4462 N  N   . ALA B 1 229 ? 13.096  24.040  -9.644  1.00 18.80 ? 229  ALA B N   1 
ATOM   4463 C  CA  . ALA B 1 229 ? 12.432  23.015  -10.449 1.00 18.55 ? 229  ALA B CA  1 
ATOM   4464 C  C   . ALA B 1 229 ? 11.043  22.650  -9.916  1.00 19.77 ? 229  ALA B C   1 
ATOM   4465 O  O   . ALA B 1 229 ? 10.121  22.435  -10.701 1.00 18.26 ? 229  ALA B O   1 
ATOM   4466 C  CB  . ALA B 1 229 ? 13.293  21.775  -10.548 1.00 18.35 ? 229  ALA B CB  1 
ATOM   4467 N  N   . ASP B 1 230 ? 10.915  22.529  -8.593  1.00 20.53 ? 230  ASP B N   1 
ATOM   4468 C  CA  . ASP B 1 230 ? 9.637   22.227  -7.959  1.00 20.78 ? 230  ASP B CA  1 
ATOM   4469 C  C   . ASP B 1 230 ? 8.601   23.315  -8.262  1.00 20.19 ? 230  ASP B C   1 
ATOM   4470 O  O   . ASP B 1 230 ? 7.447   23.013  -8.562  1.00 19.09 ? 230  ASP B O   1 
ATOM   4471 C  CB  . ASP B 1 230 ? 9.796   22.097  -6.437  1.00 23.04 ? 230  ASP B CB  1 
ATOM   4472 C  CG  . ASP B 1 230 ? 10.465  20.777  -6.007  1.00 26.03 ? 230  ASP B CG  1 
ATOM   4473 O  OD1 . ASP B 1 230 ? 10.528  19.812  -6.797  1.00 27.58 ? 230  ASP B OD1 1 
ATOM   4474 O  OD2 . ASP B 1 230 ? 10.935  20.714  -4.851  1.00 29.28 ? 230  ASP B OD2 1 
ATOM   4475 N  N   . THR B 1 231 ? 9.016   24.575  -8.171  1.00 19.28 ? 231  THR B N   1 
ATOM   4476 C  CA  . THR B 1 231 ? 8.148   25.690  -8.552  1.00 19.69 ? 231  THR B CA  1 
ATOM   4477 C  C   . THR B 1 231 ? 7.711   25.560  -10.013 1.00 19.41 ? 231  THR B C   1 
ATOM   4478 O  O   . THR B 1 231 ? 6.522   25.678  -10.311 1.00 19.58 ? 231  THR B O   1 
ATOM   4479 C  CB  . THR B 1 231 ? 8.824   27.039  -8.270  1.00 19.35 ? 231  THR B CB  1 
ATOM   4480 O  OG1 . THR B 1 231 ? 9.149   27.104  -6.876  1.00 19.09 ? 231  THR B OG1 1 
ATOM   4481 C  CG2 . THR B 1 231 ? 7.905   28.199  -8.604  1.00 19.83 ? 231  THR B CG2 1 
ATOM   4482 N  N   . LEU B 1 232 ? 8.648   25.257  -10.908 1.00 19.33 ? 232  LEU B N   1 
ATOM   4483 C  CA  . LEU B 1 232 ? 8.294   25.055  -12.317 1.00 20.58 ? 232  LEU B CA  1 
ATOM   4484 C  C   . LEU B 1 232 ? 7.202   23.968  -12.451 1.00 21.22 ? 232  LEU B C   1 
ATOM   4485 O  O   . LEU B 1 232 ? 6.205   24.145  -13.171 1.00 19.31 ? 232  LEU B O   1 
ATOM   4486 C  CB  . LEU B 1 232 ? 9.539   24.707  -13.136 1.00 20.22 ? 232  LEU B CB  1 
ATOM   4487 C  CG  . LEU B 1 232 ? 9.426   24.511  -14.657 1.00 20.64 ? 232  LEU B CG  1 
ATOM   4488 C  CD1 . LEU B 1 232 ? 10.737  24.867  -15.347 1.00 19.53 ? 232  LEU B CD1 1 
ATOM   4489 C  CD2 . LEU B 1 232 ? 9.026   23.089  -15.021 1.00 21.02 ? 232  LEU B CD2 1 
ATOM   4490 N  N   . ILE B 1 233 ? 7.404   22.871  -11.721 1.00 20.91 ? 233  ILE B N   1 
ATOM   4491 C  CA  . ILE B 1 233 ? 6.545   21.701  -11.788 1.00 21.86 ? 233  ILE B CA  1 
ATOM   4492 C  C   . ILE B 1 233 ? 5.128   22.068  -11.325 1.00 21.66 ? 233  ILE B C   1 
ATOM   4493 O  O   . ILE B 1 233 ? 4.152   21.695  -11.956 1.00 20.69 ? 233  ILE B O   1 
ATOM   4494 C  CB  . ILE B 1 233 ? 7.167   20.520  -10.971 1.00 21.57 ? 233  ILE B CB  1 
ATOM   4495 C  CG1 . ILE B 1 233 ? 8.398   19.988  -11.716 1.00 21.43 ? 233  ILE B CG1 1 
ATOM   4496 C  CG2 . ILE B 1 233 ? 6.148   19.397  -10.738 1.00 20.79 ? 233  ILE B CG2 1 
ATOM   4497 C  CD1 . ILE B 1 233 ? 9.305   19.100  -10.890 1.00 22.30 ? 233  ILE B CD1 1 
ATOM   4498 N  N   . LYS B 1 234 ? 5.033   22.835  -10.251 1.00 22.45 ? 234  LYS B N   1 
ATOM   4499 C  CA  . LYS B 1 234 ? 3.731   23.290  -9.737  1.00 24.18 ? 234  LYS B CA  1 
ATOM   4500 C  C   . LYS B 1 234 ? 2.947   24.253  -10.638 1.00 23.43 ? 234  LYS B C   1 
ATOM   4501 O  O   . LYS B 1 234 ? 1.745   24.373  -10.487 1.00 23.43 ? 234  LYS B O   1 
ATOM   4502 C  CB  . LYS B 1 234 ? 3.891   23.891  -8.347  1.00 25.63 ? 234  LYS B CB  1 
ATOM   4503 C  CG  . LYS B 1 234 ? 4.002   22.817  -7.290  1.00 28.54 ? 234  LYS B CG  1 
ATOM   4504 C  CD  . LYS B 1 234 ? 4.622   23.319  -6.002  1.00 30.02 ? 234  LYS B CD  1 
ATOM   4505 C  CE  . LYS B 1 234 ? 4.606   22.204  -4.974  1.00 31.18 ? 234  LYS B CE  1 
ATOM   4506 N  NZ  . LYS B 1 234 ? 5.981   21.873  -4.526  1.00 32.22 ? 234  LYS B NZ  1 
ATOM   4507 N  N   . GLN B 1 235 ? 3.610   24.917  -11.578 1.00 23.51 ? 235  GLN B N   1 
ATOM   4508 C  CA  . GLN B 1 235 ? 2.919   25.765  -12.551 1.00 24.28 ? 235  GLN B CA  1 
ATOM   4509 C  C   . GLN B 1 235 ? 2.076   26.811  -11.831 1.00 23.90 ? 235  GLN B C   1 
ATOM   4510 O  O   . GLN B 1 235 ? 0.857   26.905  -11.984 1.00 24.14 ? 235  GLN B O   1 
ATOM   4511 C  CB  . GLN B 1 235 ? 2.111   24.908  -13.537 1.00 24.59 ? 235  GLN B CB  1 
ATOM   4512 C  CG  . GLN B 1 235 ? 3.022   24.189  -14.523 1.00 24.79 ? 235  GLN B CG  1 
ATOM   4513 C  CD  . GLN B 1 235 ? 2.391   22.973  -15.184 1.00 25.67 ? 235  GLN B CD  1 
ATOM   4514 O  OE1 . GLN B 1 235 ? 1.819   23.071  -16.255 1.00 25.66 ? 235  GLN B OE1 1 
ATOM   4515 N  NE2 . GLN B 1 235 ? 2.531   21.810  -14.558 1.00 26.34 ? 235  GLN B NE2 1 
ATOM   4516 N  N   . ASP B 1 236 ? 2.772   27.590  -11.026 1.00 23.60 ? 236  ASP B N   1 
ATOM   4517 C  CA  . ASP B 1 236 ? 2.169   28.600  -10.188 1.00 24.00 ? 236  ASP B CA  1 
ATOM   4518 C  C   . ASP B 1 236 ? 2.148   29.905  -10.987 1.00 22.50 ? 236  ASP B C   1 
ATOM   4519 O  O   . ASP B 1 236 ? 3.193   30.380  -11.449 1.00 21.58 ? 236  ASP B O   1 
ATOM   4520 C  CB  . ASP B 1 236 ? 2.993   28.689  -8.898  1.00 24.77 ? 236  ASP B CB  1 
ATOM   4521 C  CG  . ASP B 1 236 ? 2.575   29.816  -7.978  1.00 25.24 ? 236  ASP B CG  1 
ATOM   4522 O  OD1 . ASP B 1 236 ? 2.052   30.852  -8.422  1.00 25.41 ? 236  ASP B OD1 1 
ATOM   4523 O  OD2 . ASP B 1 236 ? 2.856   29.687  -6.766  1.00 29.18 ? 236  ASP B OD2 1 
ATOM   4524 N  N   . GLY B 1 237 ? 0.951   30.463  -11.147 1.00 20.75 ? 237  GLY B N   1 
ATOM   4525 C  CA  . GLY B 1 237 ? 0.718   31.655  -11.966 1.00 21.23 ? 237  GLY B CA  1 
ATOM   4526 C  C   . GLY B 1 237 ? 1.511   32.894  -11.597 1.00 20.19 ? 237  GLY B C   1 
ATOM   4527 O  O   . GLY B 1 237 ? 1.567   33.838  -12.370 1.00 19.97 ? 237  GLY B O   1 
ATOM   4528 N  N   . ARG B 1 238 ? 2.124   32.899  -10.422 1.00 20.98 ? 238  ARG B N   1 
ATOM   4529 C  CA  . ARG B 1 238 ? 2.964   34.026  -10.007 1.00 21.36 ? 238  ARG B CA  1 
ATOM   4530 C  C   . ARG B 1 238 ? 4.285   34.035  -10.755 1.00 20.61 ? 238  ARG B C   1 
ATOM   4531 O  O   . ARG B 1 238 ? 4.931   35.075  -10.862 1.00 20.22 ? 238  ARG B O   1 
ATOM   4532 C  CB  . ARG B 1 238 ? 3.212   34.005  -8.491  1.00 21.00 ? 238  ARG B CB  1 
ATOM   4533 C  CG  . ARG B 1 238 ? 1.930   34.276  -7.693  1.00 22.12 ? 238  ARG B CG  1 
ATOM   4534 C  CD  . ARG B 1 238 ? 2.106   34.058  -6.197  1.00 21.80 ? 238  ARG B CD  1 
ATOM   4535 N  NE  . ARG B 1 238 ? 2.362   32.645  -5.875  1.00 23.09 ? 238  ARG B NE  1 
ATOM   4536 C  CZ  . ARG B 1 238 ? 2.720   32.208  -4.669  1.00 23.25 ? 238  ARG B CZ  1 
ATOM   4537 N  NH1 . ARG B 1 238 ? 2.853   33.050  -3.658  1.00 24.62 ? 238  ARG B NH1 1 
ATOM   4538 N  NH2 . ARG B 1 238 ? 2.944   30.926  -4.467  1.00 23.01 ? 238  ARG B NH2 1 
ATOM   4539 N  N   . TYR B 1 239 ? 4.674   32.876  -11.273 1.00 20.20 ? 239  TYR B N   1 
ATOM   4540 C  CA  . TYR B 1 239 ? 5.979   32.710  -11.878 1.00 19.91 ? 239  TYR B CA  1 
ATOM   4541 C  C   . TYR B 1 239 ? 5.949   32.153  -13.285 1.00 19.11 ? 239  TYR B C   1 
ATOM   4542 O  O   . TYR B 1 239 ? 6.955   32.227  -13.972 1.00 18.92 ? 239  TYR B O   1 
ATOM   4543 C  CB  . TYR B 1 239 ? 6.830   31.776  -11.024 1.00 20.25 ? 239  TYR B CB  1 
ATOM   4544 C  CG  . TYR B 1 239 ? 6.682   32.013  -9.539  1.00 20.88 ? 239  TYR B CG  1 
ATOM   4545 C  CD1 . TYR B 1 239 ? 7.256   33.118  -8.934  1.00 20.78 ? 239  TYR B CD1 1 
ATOM   4546 C  CD2 . TYR B 1 239 ? 5.980   31.112  -8.739  1.00 20.88 ? 239  TYR B CD2 1 
ATOM   4547 C  CE1 . TYR B 1 239 ? 7.126   33.330  -7.570  1.00 21.39 ? 239  TYR B CE1 1 
ATOM   4548 C  CE2 . TYR B 1 239 ? 5.859   31.306  -7.379  1.00 20.94 ? 239  TYR B CE2 1 
ATOM   4549 C  CZ  . TYR B 1 239 ? 6.422   32.416  -6.807  1.00 21.46 ? 239  TYR B CZ  1 
ATOM   4550 O  OH  . TYR B 1 239 ? 6.287   32.615  -5.468  1.00 23.46 ? 239  TYR B OH  1 
ATOM   4551 N  N   . THR B 1 240 ? 4.841   31.566  -13.715 1.00 18.35 ? 240  THR B N   1 
ATOM   4552 C  CA  . THR B 1 240 ? 4.815   30.956  -15.025 1.00 17.86 ? 240  THR B CA  1 
ATOM   4553 C  C   . THR B 1 240 ? 4.849   32.032  -16.089 1.00 18.43 ? 240  THR B C   1 
ATOM   4554 O  O   . THR B 1 240 ? 4.148   33.069  -15.990 1.00 17.34 ? 240  THR B O   1 
ATOM   4555 C  CB  . THR B 1 240 ? 3.565   30.108  -15.279 1.00 18.15 ? 240  THR B CB  1 
ATOM   4556 O  OG1 . THR B 1 240 ? 2.396   30.864  -14.947 1.00 18.35 ? 240  THR B OG1 1 
ATOM   4557 C  CG2 . THR B 1 240 ? 3.605   28.812  -14.451 1.00 18.83 ? 240  THR B CG2 1 
ATOM   4558 N  N   . VAL B 1 241 ? 5.648   31.771  -17.117 1.00 18.25 ? 241  VAL B N   1 
ATOM   4559 C  CA  . VAL B 1 241 ? 5.559   32.558  -18.330 1.00 18.78 ? 241  VAL B CA  1 
ATOM   4560 C  C   . VAL B 1 241 ? 4.101   32.470  -18.779 1.00 18.70 ? 241  VAL B C   1 
ATOM   4561 O  O   . VAL B 1 241 ? 3.530   31.382  -18.831 1.00 18.08 ? 241  VAL B O   1 
ATOM   4562 C  CB  . VAL B 1 241 ? 6.507   32.053  -19.425 1.00 19.33 ? 241  VAL B CB  1 
ATOM   4563 C  CG1 . VAL B 1 241 ? 6.398   32.942  -20.654 1.00 20.02 ? 241  VAL B CG1 1 
ATOM   4564 C  CG2 . VAL B 1 241 ? 7.958   32.020  -18.911 1.00 20.16 ? 241  VAL B CG2 1 
ATOM   4565 N  N   . PRO B 1 242 ? 3.497   33.621  -19.096 1.00 19.91 ? 242  PRO B N   1 
ATOM   4566 C  CA  . PRO B 1 242 ? 2.087   33.639  -19.484 1.00 19.40 ? 242  PRO B CA  1 
ATOM   4567 C  C   . PRO B 1 242 ? 1.851   32.866  -20.748 1.00 19.19 ? 242  PRO B C   1 
ATOM   4568 O  O   . PRO B 1 242 ? 2.774   32.726  -21.572 1.00 19.07 ? 242  PRO B O   1 
ATOM   4569 C  CB  . PRO B 1 242 ? 1.771   35.123  -19.718 1.00 20.27 ? 242  PRO B CB  1 
ATOM   4570 C  CG  . PRO B 1 242 ? 3.014   35.886  -19.472 1.00 20.74 ? 242  PRO B CG  1 
ATOM   4571 C  CD  . PRO B 1 242 ? 4.114   34.963  -19.063 1.00 19.98 ? 242  PRO B CD  1 
ATOM   4572 N  N   . PHE B 1 243 ? 0.631   32.353  -20.896 1.00 18.12 ? 243  PHE B N   1 
ATOM   4573 C  CA  . PHE B 1 243 ? 0.229   31.692  -22.119 1.00 18.56 ? 243  PHE B CA  1 
ATOM   4574 C  C   . PHE B 1 243 ? 0.074   32.731  -23.232 1.00 17.97 ? 243  PHE B C   1 
ATOM   4575 O  O   . PHE B 1 243 ? -0.534  33.774  -23.030 1.00 17.52 ? 243  PHE B O   1 
ATOM   4576 C  CB  . PHE B 1 243 ? -1.075  30.919  -21.933 1.00 18.76 ? 243  PHE B CB  1 
ATOM   4577 C  CG  . PHE B 1 243 ? -0.959  29.744  -20.999 1.00 19.54 ? 243  PHE B CG  1 
ATOM   4578 C  CD1 . PHE B 1 243 ? -0.006  28.755  -21.224 1.00 19.93 ? 243  PHE B CD1 1 
ATOM   4579 C  CD2 . PHE B 1 243 ? -1.798  29.629  -19.902 1.00 19.90 ? 243  PHE B CD2 1 
ATOM   4580 C  CE1 . PHE B 1 243 ? 0.107   27.669  -20.371 1.00 21.16 ? 243  PHE B CE1 1 
ATOM   4581 C  CE2 . PHE B 1 243 ? -1.703  28.535  -19.041 1.00 20.63 ? 243  PHE B CE2 1 
ATOM   4582 C  CZ  . PHE B 1 243 ? -0.743  27.557  -19.273 1.00 21.05 ? 243  PHE B CZ  1 
ATOM   4583 N  N   . PHE B 1 244 ? 0.624   32.427  -24.396 1.00 18.00 ? 244  PHE B N   1 
ATOM   4584 C  CA  . PHE B 1 244 ? 0.529   33.310  -25.566 1.00 19.14 ? 244  PHE B CA  1 
ATOM   4585 C  C   . PHE B 1 244 ? -0.445  32.700  -26.553 1.00 19.77 ? 244  PHE B C   1 
ATOM   4586 O  O   . PHE B 1 244 ? -0.480  31.478  -26.697 1.00 20.45 ? 244  PHE B O   1 
ATOM   4587 C  CB  . PHE B 1 244 ? 1.895   33.462  -26.238 1.00 18.43 ? 244  PHE B CB  1 
ATOM   4588 C  CG  . PHE B 1 244 ? 2.958   33.990  -25.327 1.00 18.12 ? 244  PHE B CG  1 
ATOM   4589 C  CD1 . PHE B 1 244 ? 3.023   35.340  -25.040 1.00 17.88 ? 244  PHE B CD1 1 
ATOM   4590 C  CD2 . PHE B 1 244 ? 3.895   33.135  -24.766 1.00 18.35 ? 244  PHE B CD2 1 
ATOM   4591 C  CE1 . PHE B 1 244 ? 4.003   35.844  -24.201 1.00 18.26 ? 244  PHE B CE1 1 
ATOM   4592 C  CE2 . PHE B 1 244 ? 4.875   33.630  -23.921 1.00 18.60 ? 244  PHE B CE2 1 
ATOM   4593 C  CZ  . PHE B 1 244 ? 4.933   34.984  -23.641 1.00 18.15 ? 244  PHE B CZ  1 
ATOM   4594 N  N   . LYS B 1 245 ? -1.227  33.539  -27.233 1.00 20.42 ? 245  LYS B N   1 
ATOM   4595 C  CA  . LYS B 1 245 ? -2.195  33.036  -28.213 1.00 20.72 ? 245  LYS B CA  1 
ATOM   4596 C  C   . LYS B 1 245 ? -1.458  32.642  -29.496 1.00 20.05 ? 245  LYS B C   1 
ATOM   4597 O  O   . LYS B 1 245 ? -1.025  33.493  -30.287 1.00 20.43 ? 245  LYS B O   1 
ATOM   4598 C  CB  . LYS B 1 245 ? -3.292  34.066  -28.480 1.00 21.89 ? 245  LYS B CB  1 
ATOM   4599 C  CG  . LYS B 1 245 ? -4.575  33.453  -29.017 1.00 22.15 ? 245  LYS B CG  1 
ATOM   4600 C  CD  . LYS B 1 245 ? -5.626  34.494  -29.382 1.00 23.31 ? 245  LYS B CD  1 
ATOM   4601 C  CE  . LYS B 1 245 ? -6.236  35.174  -28.159 1.00 23.99 ? 245  LYS B CE  1 
ATOM   4602 N  NZ  . LYS B 1 245 ? -7.151  36.295  -28.530 1.00 23.83 ? 245  LYS B NZ  1 
ATOM   4603 N  N   . ALA B 1 246 ? -1.318  31.342  -29.688 1.00 19.42 ? 246  ALA B N   1 
ATOM   4604 C  CA  . ALA B 1 246 ? -0.473  30.790  -30.737 1.00 19.66 ? 246  ALA B CA  1 
ATOM   4605 C  C   . ALA B 1 246 ? -0.859  31.283  -32.119 1.00 20.60 ? 246  ALA B C   1 
ATOM   4606 O  O   . ALA B 1 246 ? 0.005   31.589  -32.934 1.00 19.82 ? 246  ALA B O   1 
ATOM   4607 C  CB  . ALA B 1 246 ? -0.529  29.274  -30.708 1.00 19.16 ? 246  ALA B CB  1 
ATOM   4608 N  N   . SER B 1 247 ? -2.162  31.361  -32.374 1.00 20.92 ? 247  SER B N   1 
ATOM   4609 C  CA  . SER B 1 247 ? -2.666  31.758  -33.682 1.00 21.59 ? 247  SER B CA  1 
ATOM   4610 C  C   . SER B 1 247 ? -2.175  33.151  -34.091 1.00 21.51 ? 247  SER B C   1 
ATOM   4611 O  O   . SER B 1 247 ? -2.157  33.450  -35.259 1.00 21.52 ? 247  SER B O   1 
ATOM   4612 C  CB  . SER B 1 247 ? -4.201  31.719  -33.688 1.00 21.52 ? 247  SER B CB  1 
ATOM   4613 O  OG  . SER B 1 247 ? -4.725  32.681  -32.782 1.00 22.28 ? 247  SER B OG  1 
ATOM   4614 N  N   . GLU B 1 248 ? -1.798  34.002  -33.137 1.00 22.03 ? 248  GLU B N   1 
ATOM   4615 C  CA  . GLU B 1 248 ? -1.337  35.361  -33.454 1.00 22.86 ? 248  GLU B CA  1 
ATOM   4616 C  C   . GLU B 1 248 ? 0.144   35.446  -33.785 1.00 21.45 ? 248  GLU B C   1 
ATOM   4617 O  O   . GLU B 1 248 ? 0.619   36.506  -34.168 1.00 21.46 ? 248  GLU B O   1 
ATOM   4618 C  CB  . GLU B 1 248 ? -1.604  36.324  -32.289 1.00 25.15 ? 248  GLU B CB  1 
ATOM   4619 C  CG  . GLU B 1 248 ? -3.042  36.379  -31.803 1.00 28.88 ? 248  GLU B CG  1 
ATOM   4620 C  CD  . GLU B 1 248 ? -4.007  36.693  -32.920 1.00 32.62 ? 248  GLU B CD  1 
ATOM   4621 O  OE1 . GLU B 1 248 ? -3.975  37.846  -33.402 1.00 34.70 ? 248  GLU B OE1 1 
ATOM   4622 O  OE2 . GLU B 1 248 ? -4.767  35.770  -33.321 1.00 37.92 ? 248  GLU B OE2 1 
ATOM   4623 N  N   . ILE B 1 249 ? 0.889   34.358  -33.622 1.00 20.19 ? 249  ILE B N   1 
ATOM   4624 C  CA  . ILE B 1 249 ? 2.350   34.456  -33.665 1.00 19.55 ? 249  ILE B CA  1 
ATOM   4625 C  C   . ILE B 1 249 ? 2.861   34.458  -35.107 1.00 19.45 ? 249  ILE B C   1 
ATOM   4626 O  O   . ILE B 1 249 ? 2.473   33.608  -35.915 1.00 18.69 ? 249  ILE B O   1 
ATOM   4627 C  CB  . ILE B 1 249 ? 3.007   33.328  -32.859 1.00 18.96 ? 249  ILE B CB  1 
ATOM   4628 C  CG1 . ILE B 1 249 ? 2.551   33.393  -31.402 1.00 18.16 ? 249  ILE B CG1 1 
ATOM   4629 C  CG2 . ILE B 1 249 ? 4.530   33.408  -32.955 1.00 19.36 ? 249  ILE B CG2 1 
ATOM   4630 C  CD1 . ILE B 1 249 ? 2.774   34.727  -30.729 1.00 18.39 ? 249  ILE B CD1 1 
ATOM   4631 N  N   . LYS B 1 250 ? 3.723   35.430  -35.403 1.00 18.15 ? 250  LYS B N   1 
ATOM   4632 C  CA  . LYS B 1 250 ? 4.337   35.597  -36.717 1.00 18.31 ? 250  LYS B CA  1 
ATOM   4633 C  C   . LYS B 1 250 ? 5.858   35.464  -36.656 1.00 17.16 ? 250  LYS B C   1 
ATOM   4634 O  O   . LYS B 1 250 ? 6.484   35.852  -35.653 1.00 15.76 ? 250  LYS B O   1 
ATOM   4635 C  CB  . LYS B 1 250 ? 4.038   37.009  -37.262 1.00 19.10 ? 250  LYS B CB  1 
ATOM   4636 C  CG  . LYS B 1 250 ? 2.572   37.363  -37.371 1.00 20.39 ? 250  LYS B CG  1 
ATOM   4637 C  CD  . LYS B 1 250 ? 1.859   36.398  -38.298 1.00 21.07 ? 250  LYS B CD  1 
ATOM   4638 C  CE  . LYS B 1 250 ? 0.432   36.841  -38.578 1.00 21.71 ? 250  LYS B CE  1 
ATOM   4639 N  NZ  . LYS B 1 250 ? -0.150  35.803  -39.472 1.00 23.02 ? 250  LYS B NZ  1 
ATOM   4640 N  N   . ASN B 1 251 ? 6.440   34.947  -37.745 1.00 15.92 ? 251  ASN B N   1 
ATOM   4641 C  CA  . ASN B 1 251 ? 7.863   35.134  -38.025 1.00 16.07 ? 251  ASN B CA  1 
ATOM   4642 C  C   . ASN B 1 251 ? 8.133   36.634  -38.182 1.00 16.38 ? 251  ASN B C   1 
ATOM   4643 O  O   . ASN B 1 251 ? 7.289   37.359  -38.700 1.00 16.58 ? 251  ASN B O   1 
ATOM   4644 C  CB  . ASN B 1 251 ? 8.254   34.397  -39.311 1.00 15.42 ? 251  ASN B CB  1 
ATOM   4645 C  CG  . ASN B 1 251 ? 8.101   32.891  -39.170 1.00 15.42 ? 251  ASN B CG  1 
ATOM   4646 O  OD1 . ASN B 1 251 ? 8.179   32.356  -38.057 1.00 16.60 ? 251  ASN B OD1 1 
ATOM   4647 N  ND2 . ASN B 1 251 ? 7.862   32.213  -40.265 1.00 14.45 ? 251  ASN B ND2 1 
ATOM   4648 N  N   . MET B 1 252 ? 9.276   37.104  -37.718 1.00 17.22 ? 252  MET B N   1 
ATOM   4649 C  CA  . MET B 1 252 ? 9.597   38.518  -37.814 1.00 18.69 ? 252  MET B CA  1 
ATOM   4650 C  C   . MET B 1 252 ? 9.918   38.860  -39.263 1.00 17.60 ? 252  MET B C   1 
ATOM   4651 O  O   . MET B 1 252 ? 10.831  38.275  -39.831 1.00 17.70 ? 252  MET B O   1 
ATOM   4652 C  CB  . MET B 1 252 ? 10.787  38.876  -36.925 1.00 20.73 ? 252  MET B CB  1 
ATOM   4653 C  CG  . MET B 1 252 ? 11.039  40.379  -36.829 1.00 23.68 ? 252  MET B CG  1 
ATOM   4654 S  SD  . MET B 1 252 ? 12.530  40.838  -35.908 1.00 28.34 ? 252  MET B SD  1 
ATOM   4655 C  CE  . MET B 1 252 ? 13.744  40.221  -37.018 1.00 26.45 ? 252  MET B CE  1 
ATOM   4656 N  N   . PRO B 1 253 ? 9.199   39.827  -39.862 1.00 16.81 ? 253  PRO B N   1 
ATOM   4657 C  CA  . PRO B 1 253 ? 9.510   40.043  -41.289 1.00 16.99 ? 253  PRO B CA  1 
ATOM   4658 C  C   . PRO B 1 253 ? 10.967  40.455  -41.572 1.00 16.41 ? 253  PRO B C   1 
ATOM   4659 O  O   . PRO B 1 253 ? 11.520  40.038  -42.578 1.00 16.02 ? 253  PRO B O   1 
ATOM   4660 C  CB  . PRO B 1 253 ? 8.500   41.122  -41.702 1.00 16.81 ? 253  PRO B CB  1 
ATOM   4661 C  CG  . PRO B 1 253 ? 7.315   40.829  -40.817 1.00 16.35 ? 253  PRO B CG  1 
ATOM   4662 C  CD  . PRO B 1 253 ? 7.943   40.497  -39.482 1.00 16.43 ? 253  PRO B CD  1 
ATOM   4663 N  N   . ALA B 1 254 ? 11.580  41.217  -40.670 1.00 16.04 ? 254  ALA B N   1 
ATOM   4664 C  CA  . ALA B 1 254 ? 12.971  41.627  -40.816 1.00 16.58 ? 254  ALA B CA  1 
ATOM   4665 C  C   . ALA B 1 254 ? 13.994  40.478  -40.652 1.00 16.62 ? 254  ALA B C   1 
ATOM   4666 O  O   . ALA B 1 254 ? 15.181  40.664  -40.966 1.00 16.20 ? 254  ALA B O   1 
ATOM   4667 C  CB  . ALA B 1 254 ? 13.291  42.752  -39.840 1.00 16.73 ? 254  ALA B CB  1 
ATOM   4668 N  N   . ALA B 1 255 ? 13.535  39.316  -40.179 1.00 16.18 ? 255  ALA B N   1 
ATOM   4669 C  CA  . ALA B 1 255 ? 14.348  38.101  -40.162 1.00 17.39 ? 255  ALA B CA  1 
ATOM   4670 C  C   . ALA B 1 255 ? 14.363  37.363  -41.501 1.00 18.28 ? 255  ALA B C   1 
ATOM   4671 O  O   . ALA B 1 255 ? 15.040  36.336  -41.642 1.00 20.20 ? 255  ALA B O   1 
ATOM   4672 C  CB  . ALA B 1 255 ? 13.893  37.167  -39.061 1.00 16.82 ? 255  ALA B CB  1 
ATOM   4673 N  N   . THR B 1 256 ? 13.614  37.858  -42.481 1.00 18.30 ? 256  THR B N   1 
ATOM   4674 C  CA  . THR B 1 256 ? 13.798  37.408  -43.853 1.00 18.63 ? 256  THR B CA  1 
ATOM   4675 C  C   . THR B 1 256 ? 14.719  38.434  -44.483 1.00 19.61 ? 256  THR B C   1 
ATOM   4676 O  O   . THR B 1 256 ? 14.305  39.533  -44.818 1.00 19.96 ? 256  THR B O   1 
ATOM   4677 C  CB  . THR B 1 256 ? 12.470  37.276  -44.605 1.00 18.74 ? 256  THR B CB  1 
ATOM   4678 O  OG1 . THR B 1 256 ? 11.702  36.248  -43.979 1.00 18.06 ? 256  THR B OG1 1 
ATOM   4679 C  CG2 . THR B 1 256 ? 12.701  36.892  -46.061 1.00 19.27 ? 256  THR B CG2 1 
ATOM   4680 N  N   . THR B 1 257 ? 15.993  38.077  -44.585 1.00 18.95 ? 257  THR B N   1 
ATOM   4681 C  CA  . THR B 1 257 ? 17.031  39.045  -44.854 1.00 18.87 ? 257  THR B CA  1 
ATOM   4682 C  C   . THR B 1 257 ? 18.204  38.316  -45.483 1.00 19.61 ? 257  THR B C   1 
ATOM   4683 O  O   . THR B 1 257 ? 18.280  37.069  -45.457 1.00 18.86 ? 257  THR B O   1 
ATOM   4684 C  CB  . THR B 1 257 ? 17.461  39.737  -43.538 1.00 18.36 ? 257  THR B CB  1 
ATOM   4685 O  OG1 . THR B 1 257 ? 18.215  40.932  -43.807 1.00 17.89 ? 257  THR B OG1 1 
ATOM   4686 C  CG2 . THR B 1 257 ? 18.270  38.781  -42.663 1.00 18.33 ? 257  THR B CG2 1 
ATOM   4687 N  N   . LYS B 1 258 ? 19.135  39.079  -46.027 1.00 19.94 ? 258  LYS B N   1 
ATOM   4688 C  CA  . LYS B 1 258 ? 20.326  38.475  -46.618 1.00 21.24 ? 258  LYS B CA  1 
ATOM   4689 C  C   . LYS B 1 258 ? 21.172  37.894  -45.503 1.00 20.19 ? 258  LYS B C   1 
ATOM   4690 O  O   . LYS B 1 258 ? 21.568  38.602  -44.581 1.00 19.89 ? 258  LYS B O   1 
ATOM   4691 C  CB  . LYS B 1 258 ? 21.124  39.517  -47.401 1.00 23.64 ? 258  LYS B CB  1 
ATOM   4692 C  CG  . LYS B 1 258 ? 22.256  38.953  -48.244 1.00 25.88 ? 258  LYS B CG  1 
ATOM   4693 C  CD  . LYS B 1 258 ? 23.059  40.092  -48.860 1.00 28.15 ? 258  LYS B CD  1 
ATOM   4694 C  CE  . LYS B 1 258 ? 23.120  39.964  -50.361 1.00 31.16 ? 258  LYS B CE  1 
ATOM   4695 N  NZ  . LYS B 1 258 ? 23.662  41.236  -50.913 1.00 33.54 ? 258  LYS B NZ  1 
ATOM   4696 N  N   . ASP B 1 259 ? 21.424  36.598  -45.594 1.00 19.17 ? 259  ASP B N   1 
ATOM   4697 C  CA  . ASP B 1 259 ? 22.170  35.874  -44.584 1.00 18.89 ? 259  ASP B CA  1 
ATOM   4698 C  C   . ASP B 1 259 ? 23.650  36.247  -44.656 1.00 19.09 ? 259  ASP B C   1 
ATOM   4699 O  O   . ASP B 1 259 ? 24.203  36.398  -45.743 1.00 19.48 ? 259  ASP B O   1 
ATOM   4700 C  CB  . ASP B 1 259 ? 22.007  34.371  -44.805 1.00 18.18 ? 259  ASP B CB  1 
ATOM   4701 C  CG  . ASP B 1 259 ? 22.751  33.551  -43.784 1.00 17.85 ? 259  ASP B CG  1 
ATOM   4702 O  OD1 . ASP B 1 259 ? 22.362  33.620  -42.611 1.00 18.53 ? 259  ASP B OD1 1 
ATOM   4703 O  OD2 . ASP B 1 259 ? 23.727  32.854  -44.138 1.00 17.17 ? 259  ASP B OD2 1 
ATOM   4704 N  N   . ALA B 1 260 ? 24.284  36.363  -43.499 1.00 18.70 ? 260  ALA B N   1 
ATOM   4705 C  CA  . ALA B 1 260 ? 25.673  36.818  -43.415 1.00 19.96 ? 260  ALA B CA  1 
ATOM   4706 C  C   . ALA B 1 260 ? 26.658  35.809  -44.020 1.00 20.58 ? 260  ALA B C   1 
ATOM   4707 O  O   . ALA B 1 260 ? 27.719  36.210  -44.489 1.00 20.10 ? 260  ALA B O   1 
ATOM   4708 C  CB  . ALA B 1 260 ? 26.045  37.107  -41.969 1.00 19.60 ? 260  ALA B CB  1 
ATOM   4709 N  N   . GLN B 1 261 ? 26.302  34.517  -44.001 1.00 20.67 ? 261  GLN B N   1 
ATOM   4710 C  CA  . GLN B 1 261 ? 27.182  33.466  -44.536 1.00 21.53 ? 261  GLN B CA  1 
ATOM   4711 C  C   . GLN B 1 261 ? 26.914  33.120  -46.003 1.00 22.76 ? 261  GLN B C   1 
ATOM   4712 O  O   . GLN B 1 261 ? 27.858  32.950  -46.768 1.00 23.10 ? 261  GLN B O   1 
ATOM   4713 C  CB  . GLN B 1 261 ? 27.131  32.209  -43.659 1.00 20.99 ? 261  GLN B CB  1 
ATOM   4714 C  CG  . GLN B 1 261 ? 27.815  32.437  -42.306 1.00 20.53 ? 261  GLN B CG  1 
ATOM   4715 C  CD  . GLN B 1 261 ? 27.857  31.220  -41.394 1.00 20.93 ? 261  GLN B CD  1 
ATOM   4716 O  OE1 . GLN B 1 261 ? 28.449  31.276  -40.302 1.00 20.88 ? 261  GLN B OE1 1 
ATOM   4717 N  NE2 . GLN B 1 261 ? 27.205  30.124  -41.807 1.00 19.57 ? 261  GLN B NE2 1 
ATOM   4718 N  N   . THR B 1 262 ? 25.650  33.024  -46.403 1.00 22.61 ? 262  THR B N   1 
ATOM   4719 C  CA  . THR B 1 262 ? 25.318  32.579  -47.760 1.00 23.41 ? 262  THR B CA  1 
ATOM   4720 C  C   . THR B 1 262 ? 25.167  33.723  -48.750 1.00 24.59 ? 262  THR B C   1 
ATOM   4721 O  O   . THR B 1 262 ? 25.266  33.500  -49.952 1.00 24.39 ? 262  THR B O   1 
ATOM   4722 C  CB  . THR B 1 262 ? 24.013  31.760  -47.787 1.00 22.67 ? 262  THR B CB  1 
ATOM   4723 O  OG1 . THR B 1 262 ? 22.910  32.620  -47.470 1.00 22.39 ? 262  THR B OG1 1 
ATOM   4724 C  CG2 . THR B 1 262 ? 24.084  30.618  -46.787 1.00 22.19 ? 262  THR B CG2 1 
ATOM   4725 N  N   . ASN B 1 263 ? 24.892  34.927  -48.244 1.00 25.87 ? 263  ASN B N   1 
ATOM   4726 C  CA  . ASN B 1 263 ? 24.572  36.103  -49.064 1.00 28.89 ? 263  ASN B CA  1 
ATOM   4727 C  C   . ASN B 1 263 ? 23.315  35.944  -49.902 1.00 29.42 ? 263  ASN B C   1 
ATOM   4728 O  O   . ASN B 1 263 ? 23.163  36.601  -50.927 1.00 30.88 ? 263  ASN B O   1 
ATOM   4729 C  CB  . ASN B 1 263 ? 25.746  36.493  -49.965 1.00 31.41 ? 263  ASN B CB  1 
ATOM   4730 C  CG  . ASN B 1 263 ? 27.063  36.500  -49.221 1.00 34.30 ? 263  ASN B CG  1 
ATOM   4731 O  OD1 . ASN B 1 263 ? 27.135  36.875  -48.046 1.00 36.01 ? 263  ASN B OD1 1 
ATOM   4732 N  ND2 . ASN B 1 263 ? 28.112  36.067  -49.896 1.00 36.59 ? 263  ASN B ND2 1 
ATOM   4733 N  N   . THR B 1 264 ? 22.416  35.074  -49.455 1.00 29.94 ? 264  THR B N   1 
ATOM   4734 C  CA  . THR B 1 264 ? 21.124  34.882  -50.087 1.00 28.98 ? 264  THR B CA  1 
ATOM   4735 C  C   . THR B 1 264 ? 20.056  35.308  -49.093 1.00 27.87 ? 264  THR B C   1 
ATOM   4736 O  O   . THR B 1 264 ? 20.243  35.176  -47.878 1.00 25.46 ? 264  THR B O   1 
ATOM   4737 C  CB  . THR B 1 264 ? 20.904  33.407  -50.455 1.00 29.55 ? 264  THR B CB  1 
ATOM   4738 O  OG1 . THR B 1 264 ? 21.000  32.588  -49.280 1.00 30.41 ? 264  THR B OG1 1 
ATOM   4739 C  CG2 . THR B 1 264 ? 21.952  32.948  -51.472 1.00 30.71 ? 264  THR B CG2 1 
ATOM   4740 N  N   . ILE B 1 265 ? 18.940  35.802  -49.618 1.00 27.39 ? 265  ILE B N   1 
ATOM   4741 C  CA  . ILE B 1 265 ? 17.792  36.187  -48.802 1.00 28.52 ? 265  ILE B CA  1 
ATOM   4742 C  C   . ILE B 1 265 ? 17.075  34.924  -48.344 1.00 27.37 ? 265  ILE B C   1 
ATOM   4743 O  O   . ILE B 1 265 ? 16.651  34.129  -49.171 1.00 27.46 ? 265  ILE B O   1 
ATOM   4744 C  CB  . ILE B 1 265 ? 16.812  37.105  -49.578 1.00 30.26 ? 265  ILE B CB  1 
ATOM   4745 C  CG1 . ILE B 1 265 ? 17.345  38.541  -49.623 1.00 32.36 ? 265  ILE B CG1 1 
ATOM   4746 C  CG2 . ILE B 1 265 ? 15.461  37.164  -48.892 1.00 29.82 ? 265  ILE B CG2 1 
ATOM   4747 C  CD1 . ILE B 1 265 ? 18.746  38.695  -50.175 1.00 33.57 ? 265  ILE B CD1 1 
ATOM   4748 N  N   . GLU B 1 266 ? 16.982  34.741  -47.026 1.00 26.00 ? 266  GLU B N   1 
ATOM   4749 C  CA  . GLU B 1 266 ? 16.370  33.555  -46.416 1.00 26.68 ? 266  GLU B CA  1 
ATOM   4750 C  C   . GLU B 1 266 ? 15.548  33.985  -45.215 1.00 24.33 ? 266  GLU B C   1 
ATOM   4751 O  O   . GLU B 1 266 ? 15.875  34.989  -44.577 1.00 22.29 ? 266  GLU B O   1 
ATOM   4752 C  CB  . GLU B 1 266 ? 17.432  32.562  -45.891 1.00 28.52 ? 266  GLU B CB  1 
ATOM   4753 C  CG  . GLU B 1 266 ? 18.522  32.164  -46.869 1.00 31.00 ? 266  GLU B CG  1 
ATOM   4754 C  CD  . GLU B 1 266 ? 18.009  31.376  -48.057 1.00 33.47 ? 266  GLU B CD  1 
ATOM   4755 O  OE1 . GLU B 1 266 ? 16.958  30.727  -47.931 1.00 37.98 ? 266  GLU B OE1 1 
ATOM   4756 O  OE2 . GLU B 1 266 ? 18.662  31.409  -49.121 1.00 35.14 ? 266  GLU B OE2 1 
ATOM   4757 N  N   . PRO B 1 267 ? 14.504  33.206  -44.883 1.00 23.36 ? 267  PRO B N   1 
ATOM   4758 C  CA  . PRO B 1 267 ? 13.839  33.407  -43.611 1.00 22.55 ? 267  PRO B CA  1 
ATOM   4759 C  C   . PRO B 1 267 ? 14.703  32.804  -42.513 1.00 21.23 ? 267  PRO B C   1 
ATOM   4760 O  O   . PRO B 1 267 ? 14.906  31.585  -42.483 1.00 21.20 ? 267  PRO B O   1 
ATOM   4761 C  CB  . PRO B 1 267 ? 12.524  32.637  -43.760 1.00 23.23 ? 267  PRO B CB  1 
ATOM   4762 C  CG  . PRO B 1 267 ? 12.713  31.686  -44.904 1.00 23.29 ? 267  PRO B CG  1 
ATOM   4763 C  CD  . PRO B 1 267 ? 14.004  32.010  -45.593 1.00 23.37 ? 267  PRO B CD  1 
ATOM   4764 N  N   . LEU B 1 268 ? 15.212  33.651  -41.629 1.00 19.29 ? 268  LEU B N   1 
ATOM   4765 C  CA  . LEU B 1 268 ? 16.118  33.207  -40.576 1.00 19.07 ? 268  LEU B CA  1 
ATOM   4766 C  C   . LEU B 1 268 ? 15.404  33.017  -39.241 1.00 17.56 ? 268  LEU B C   1 
ATOM   4767 O  O   . LEU B 1 268 ? 14.405  33.666  -38.967 1.00 17.13 ? 268  LEU B O   1 
ATOM   4768 C  CB  . LEU B 1 268 ? 17.261  34.231  -40.405 1.00 19.62 ? 268  LEU B CB  1 
ATOM   4769 C  CG  . LEU B 1 268 ? 18.011  34.621  -41.683 1.00 20.68 ? 268  LEU B CG  1 
ATOM   4770 C  CD1 . LEU B 1 268 ? 19.096  35.672  -41.428 1.00 20.99 ? 268  LEU B CD1 1 
ATOM   4771 C  CD2 . LEU B 1 268 ? 18.619  33.395  -42.350 1.00 21.17 ? 268  LEU B CD2 1 
ATOM   4772 N  N   . ASP B 1 269 ? 15.941  32.139  -38.406 1.00 16.81 ? 269  ASP B N   1 
ATOM   4773 C  CA  . ASP B 1 269 ? 15.646  32.163  -36.972 1.00 16.30 ? 269  ASP B CA  1 
ATOM   4774 C  C   . ASP B 1 269 ? 16.240  33.455  -36.399 1.00 16.62 ? 269  ASP B C   1 
ATOM   4775 O  O   . ASP B 1 269 ? 17.372  33.810  -36.744 1.00 16.04 ? 269  ASP B O   1 
ATOM   4776 C  CB  . ASP B 1 269 ? 16.318  30.995  -36.241 1.00 15.87 ? 269  ASP B CB  1 
ATOM   4777 C  CG  . ASP B 1 269 ? 15.613  29.652  -36.442 1.00 16.48 ? 269  ASP B CG  1 
ATOM   4778 O  OD1 . ASP B 1 269 ? 14.385  29.613  -36.727 1.00 16.82 ? 269  ASP B OD1 1 
ATOM   4779 O  OD2 . ASP B 1 269 ? 16.303  28.621  -36.294 1.00 16.00 ? 269  ASP B OD2 1 
ATOM   4780 N  N   . VAL B 1 270 ? 15.496  34.128  -35.526 1.00 16.34 ? 270  VAL B N   1 
ATOM   4781 C  CA  . VAL B 1 270 ? 16.046  35.190  -34.695 1.00 16.82 ? 270  VAL B CA  1 
ATOM   4782 C  C   . VAL B 1 270 ? 15.886  34.765  -33.243 1.00 16.50 ? 270  VAL B C   1 
ATOM   4783 O  O   . VAL B 1 270 ? 14.807  34.408  -32.814 1.00 16.21 ? 270  VAL B O   1 
ATOM   4784 C  CB  . VAL B 1 270 ? 15.409  36.585  -34.978 1.00 18.01 ? 270  VAL B CB  1 
ATOM   4785 C  CG1 . VAL B 1 270 ? 13.892  36.546  -34.881 1.00 17.96 ? 270  VAL B CG1 1 
ATOM   4786 C  CG2 . VAL B 1 270 ? 15.985  37.642  -34.033 1.00 18.60 ? 270  VAL B CG2 1 
ATOM   4787 N  N   . TRP B 1 271 ? 16.984  34.742  -32.495 1.00 17.08 ? 271  TRP B N   1 
ATOM   4788 C  CA  . TRP B 1 271 ? 16.915  34.305  -31.117 1.00 17.21 ? 271  TRP B CA  1 
ATOM   4789 C  C   . TRP B 1 271 ? 17.411  35.390  -30.161 1.00 18.01 ? 271  TRP B C   1 
ATOM   4790 O  O   . TRP B 1 271 ? 16.791  36.467  -30.108 1.00 18.86 ? 271  TRP B O   1 
ATOM   4791 C  CB  . TRP B 1 271 ? 17.498  32.880  -30.906 1.00 16.78 ? 271  TRP B CB  1 
ATOM   4792 C  CG  . TRP B 1 271 ? 18.939  32.583  -31.275 1.00 16.84 ? 271  TRP B CG  1 
ATOM   4793 C  CD1 . TRP B 1 271 ? 19.992  32.421  -30.409 1.00 16.68 ? 271  TRP B CD1 1 
ATOM   4794 C  CD2 . TRP B 1 271 ? 19.446  32.289  -32.574 1.00 16.97 ? 271  TRP B CD2 1 
ATOM   4795 N  NE1 . TRP B 1 271 ? 21.131  32.121  -31.098 1.00 16.95 ? 271  TRP B NE1 1 
ATOM   4796 C  CE2 . TRP B 1 271 ? 20.829  32.027  -32.431 1.00 17.37 ? 271  TRP B CE2 1 
ATOM   4797 C  CE3 . TRP B 1 271 ? 18.881  32.264  -33.853 1.00 17.25 ? 271  TRP B CE3 1 
ATOM   4798 C  CZ2 . TRP B 1 271 ? 21.653  31.730  -33.518 1.00 17.45 ? 271  TRP B CZ2 1 
ATOM   4799 C  CZ3 . TRP B 1 271 ? 19.704  31.962  -34.943 1.00 18.14 ? 271  TRP B CZ3 1 
ATOM   4800 C  CH2 . TRP B 1 271 ? 21.080  31.700  -34.765 1.00 17.64 ? 271  TRP B CH2 1 
ATOM   4801 N  N   . ASP B 1 272 ? 18.488  35.159  -29.422 1.00 18.30 ? 272  ASP B N   1 
ATOM   4802 C  CA  . ASP B 1 272 ? 18.933  36.119  -28.400 1.00 18.94 ? 272  ASP B CA  1 
ATOM   4803 C  C   . ASP B 1 272 ? 19.060  37.506  -29.011 1.00 18.68 ? 272  ASP B C   1 
ATOM   4804 O  O   . ASP B 1 272 ? 19.720  37.667  -30.039 1.00 18.38 ? 272  ASP B O   1 
ATOM   4805 C  CB  . ASP B 1 272 ? 20.292  35.718  -27.832 1.00 19.96 ? 272  ASP B CB  1 
ATOM   4806 C  CG  . ASP B 1 272 ? 20.225  34.457  -26.971 1.00 21.58 ? 272  ASP B CG  1 
ATOM   4807 O  OD1 . ASP B 1 272 ? 19.526  33.488  -27.314 1.00 22.31 ? 272  ASP B OD1 1 
ATOM   4808 O  OD2 . ASP B 1 272 ? 20.888  34.453  -25.930 1.00 25.74 ? 272  ASP B OD2 1 
ATOM   4809 N  N   . SER B 1 273 ? 18.462  38.485  -28.338 1.00 18.14 ? 273  SER B N   1 
ATOM   4810 C  CA  . SER B 1 273 ? 18.310  39.837  -28.848 1.00 18.10 ? 273  SER B CA  1 
ATOM   4811 C  C   . SER B 1 273 ? 18.405  40.793  -27.661 1.00 18.16 ? 273  SER B C   1 
ATOM   4812 O  O   . SER B 1 273 ? 18.006  40.441  -26.542 1.00 17.45 ? 273  SER B O   1 
ATOM   4813 C  CB  . SER B 1 273 ? 16.945  39.983  -29.541 1.00 18.61 ? 273  SER B CB  1 
ATOM   4814 O  OG  . SER B 1 273 ? 16.853  39.238  -30.773 1.00 18.31 ? 273  SER B OG  1 
ATOM   4815 N  N   . TRP B 1 274 ? 18.974  41.974  -27.894 1.00 17.32 ? 274  TRP B N   1 
ATOM   4816 C  CA  . TRP B 1 274 ? 19.084  42.997  -26.863 1.00 17.80 ? 274  TRP B CA  1 
ATOM   4817 C  C   . TRP B 1 274 ? 19.021  44.414  -27.450 1.00 17.98 ? 274  TRP B C   1 
ATOM   4818 O  O   . TRP B 1 274 ? 19.535  44.673  -28.547 1.00 17.67 ? 274  TRP B O   1 
ATOM   4819 C  CB  . TRP B 1 274 ? 20.364  42.827  -26.053 1.00 17.68 ? 274  TRP B CB  1 
ATOM   4820 C  CG  . TRP B 1 274 ? 21.618  42.869  -26.853 1.00 17.42 ? 274  TRP B CG  1 
ATOM   4821 C  CD1 . TRP B 1 274 ? 22.437  43.946  -27.047 1.00 17.34 ? 274  TRP B CD1 1 
ATOM   4822 C  CD2 . TRP B 1 274 ? 22.204  41.783  -27.579 1.00 17.19 ? 274  TRP B CD2 1 
ATOM   4823 N  NE1 . TRP B 1 274 ? 23.504  43.596  -27.848 1.00 17.02 ? 274  TRP B NE1 1 
ATOM   4824 C  CE2 . TRP B 1 274 ? 23.380  42.275  -28.195 1.00 17.32 ? 274  TRP B CE2 1 
ATOM   4825 C  CE3 . TRP B 1 274 ? 21.849  40.451  -27.776 1.00 17.55 ? 274  TRP B CE3 1 
ATOM   4826 C  CZ2 . TRP B 1 274 ? 24.204  41.473  -28.974 1.00 17.46 ? 274  TRP B CZ2 1 
ATOM   4827 C  CZ3 . TRP B 1 274 ? 22.670  39.652  -28.562 1.00 17.91 ? 274  TRP B CZ3 1 
ATOM   4828 C  CH2 . TRP B 1 274 ? 23.832  40.168  -29.148 1.00 17.76 ? 274  TRP B CH2 1 
ATOM   4829 N  N   . PRO B 1 275 ? 18.392  45.343  -26.709 1.00 18.57 ? 275  PRO B N   1 
ATOM   4830 C  CA  . PRO B 1 275 ? 18.269  46.697  -27.231 1.00 18.08 ? 275  PRO B CA  1 
ATOM   4831 C  C   . PRO B 1 275 ? 19.527  47.506  -26.945 1.00 17.42 ? 275  PRO B C   1 
ATOM   4832 O  O   . PRO B 1 275 ? 20.286  47.176  -26.023 1.00 16.75 ? 275  PRO B O   1 
ATOM   4833 C  CB  . PRO B 1 275 ? 17.070  47.258  -26.445 1.00 18.28 ? 275  PRO B CB  1 
ATOM   4834 C  CG  . PRO B 1 275 ? 17.058  46.480  -25.155 1.00 18.47 ? 275  PRO B CG  1 
ATOM   4835 C  CD  . PRO B 1 275 ? 17.964  45.278  -25.298 1.00 18.05 ? 275  PRO B CD  1 
ATOM   4836 N  N   . VAL B 1 276 ? 19.756  48.549  -27.738 1.00 17.08 ? 276  VAL B N   1 
ATOM   4837 C  CA  . VAL B 1 276 ? 20.736  49.537  -27.371 1.00 16.77 ? 276  VAL B CA  1 
ATOM   4838 C  C   . VAL B 1 276 ? 20.120  50.271  -26.189 1.00 17.74 ? 276  VAL B C   1 
ATOM   4839 O  O   . VAL B 1 276 ? 19.032  50.837  -26.297 1.00 17.64 ? 276  VAL B O   1 
ATOM   4840 C  CB  . VAL B 1 276 ? 21.056  50.503  -28.510 1.00 16.90 ? 276  VAL B CB  1 
ATOM   4841 C  CG1 . VAL B 1 276 ? 21.951  51.645  -28.018 1.00 16.62 ? 276  VAL B CG1 1 
ATOM   4842 C  CG2 . VAL B 1 276 ? 21.708  49.751  -29.659 1.00 16.46 ? 276  VAL B CG2 1 
ATOM   4843 N  N   . GLN B 1 277 ? 20.822  50.238  -25.064 1.00 18.59 ? 277  GLN B N   1 
ATOM   4844 C  CA  . GLN B 1 277 ? 20.304  50.729  -23.787 1.00 19.98 ? 277  GLN B CA  1 
ATOM   4845 C  C   . GLN B 1 277 ? 21.103  51.918  -23.285 1.00 20.16 ? 277  GLN B C   1 
ATOM   4846 O  O   . GLN B 1 277 ? 22.267  52.097  -23.639 1.00 19.53 ? 277  GLN B O   1 
ATOM   4847 C  CB  . GLN B 1 277 ? 20.376  49.618  -22.740 1.00 20.15 ? 277  GLN B CB  1 
ATOM   4848 C  CG  . GLN B 1 277 ? 19.284  48.594  -22.908 1.00 21.61 ? 277  GLN B CG  1 
ATOM   4849 C  CD  . GLN B 1 277 ? 19.435  47.417  -21.953 1.00 21.97 ? 277  GLN B CD  1 
ATOM   4850 O  OE1 . GLN B 1 277 ? 20.260  46.524  -22.186 1.00 23.83 ? 277  GLN B OE1 1 
ATOM   4851 N  NE2 . GLN B 1 277 ? 18.648  47.414  -20.875 1.00 20.18 ? 277  GLN B NE2 1 
ATOM   4852 N  N   . ASP B 1 278 ? 20.461  52.731  -22.456 1.00 20.97 ? 278  ASP B N   1 
ATOM   4853 C  CA  . ASP B 1 278 ? 21.171  53.733  -21.666 1.00 21.01 ? 278  ASP B CA  1 
ATOM   4854 C  C   . ASP B 1 278 ? 22.038  52.996  -20.643 1.00 20.13 ? 278  ASP B C   1 
ATOM   4855 O  O   . ASP B 1 278 ? 21.523  52.188  -19.854 1.00 20.08 ? 278  ASP B O   1 
ATOM   4856 C  CB  . ASP B 1 278 ? 20.186  54.623  -20.932 1.00 21.43 ? 278  ASP B CB  1 
ATOM   4857 C  CG  . ASP B 1 278 ? 20.857  55.783  -20.265 1.00 22.37 ? 278  ASP B CG  1 
ATOM   4858 O  OD1 . ASP B 1 278 ? 21.553  55.587  -19.241 1.00 23.40 ? 278  ASP B OD1 1 
ATOM   4859 O  OD2 . ASP B 1 278 ? 20.683  56.903  -20.774 1.00 25.15 ? 278  ASP B OD2 1 
ATOM   4860 N  N   . VAL B 1 279 ? 23.328  53.293  -20.647 1.00 19.42 ? 279  VAL B N   1 
ATOM   4861 C  CA  . VAL B 1 279 ? 24.301  52.575  -19.819 1.00 21.30 ? 279  VAL B CA  1 
ATOM   4862 C  C   . VAL B 1 279 ? 24.078  52.761  -18.310 1.00 22.72 ? 279  VAL B C   1 
ATOM   4863 O  O   . VAL B 1 279 ? 24.505  51.928  -17.520 1.00 22.63 ? 279  VAL B O   1 
ATOM   4864 C  CB  . VAL B 1 279 ? 25.760  52.959  -20.205 1.00 21.25 ? 279  VAL B CB  1 
ATOM   4865 C  CG1 . VAL B 1 279 ? 26.105  54.374  -19.778 1.00 21.60 ? 279  VAL B CG1 1 
ATOM   4866 C  CG2 . VAL B 1 279 ? 26.770  51.967  -19.631 1.00 22.38 ? 279  VAL B CG2 1 
ATOM   4867 N  N   . ARG B 1 280 ? 23.403  53.837  -17.912 1.00 25.38 ? 280  ARG B N   1 
ATOM   4868 C  CA  . ARG B 1 280 ? 23.146  54.100  -16.490 1.00 27.03 ? 280  ARG B CA  1 
ATOM   4869 C  C   . ARG B 1 280 ? 21.784  53.600  -16.027 1.00 25.77 ? 280  ARG B C   1 
ATOM   4870 O  O   . ARG B 1 280 ? 21.679  53.049  -14.944 1.00 27.28 ? 280  ARG B O   1 
ATOM   4871 C  CB  . ARG B 1 280 ? 23.270  55.591  -16.195 1.00 30.54 ? 280  ARG B CB  1 
ATOM   4872 C  CG  . ARG B 1 280 ? 24.703  56.092  -16.242 1.00 33.95 ? 280  ARG B CG  1 
ATOM   4873 C  CD  . ARG B 1 280 ? 24.822  57.511  -16.787 1.00 38.25 ? 280  ARG B CD  1 
ATOM   4874 N  NE  . ARG B 1 280 ? 25.941  57.569  -17.716 1.00 44.33 ? 280  ARG B NE  1 
ATOM   4875 C  CZ  . ARG B 1 280 ? 25.873  57.861  -19.015 1.00 46.23 ? 280  ARG B CZ  1 
ATOM   4876 N  NH1 . ARG B 1 280 ? 24.737  58.222  -19.607 1.00 48.40 ? 280  ARG B NH1 1 
ATOM   4877 N  NH2 . ARG B 1 280 ? 26.991  57.827  -19.724 1.00 47.36 ? 280  ARG B NH2 1 
ATOM   4878 N  N   . THR B 1 281 ? 20.743  53.788  -16.833 1.00 24.73 ? 281  THR B N   1 
ATOM   4879 C  CA  . THR B 1 281 ? 19.376  53.417  -16.415 1.00 23.07 ? 281  THR B CA  1 
ATOM   4880 C  C   . THR B 1 281 ? 18.886  52.089  -16.980 1.00 21.90 ? 281  THR B C   1 
ATOM   4881 O  O   . THR B 1 281 ? 17.898  51.545  -16.494 1.00 18.94 ? 281  THR B O   1 
ATOM   4882 C  CB  . THR B 1 281 ? 18.355  54.479  -16.827 1.00 23.58 ? 281  THR B CB  1 
ATOM   4883 O  OG1 . THR B 1 281 ? 18.245  54.513  -18.253 1.00 23.23 ? 281  THR B OG1 1 
ATOM   4884 C  CG2 . THR B 1 281 ? 18.766  55.852  -16.316 1.00 24.63 ? 281  THR B CG2 1 
ATOM   4885 N  N   . GLY B 1 282 ? 19.545  51.587  -18.028 1.00 21.78 ? 282  GLY B N   1 
ATOM   4886 C  CA  . GLY B 1 282 ? 19.063  50.388  -18.732 1.00 21.56 ? 282  GLY B CA  1 
ATOM   4887 C  C   . GLY B 1 282 ? 17.819  50.613  -19.597 1.00 20.64 ? 282  GLY B C   1 
ATOM   4888 O  O   . GLY B 1 282 ? 17.352  49.685  -20.265 1.00 20.79 ? 282  GLY B O   1 
ATOM   4889 N  N   . GLN B 1 283 ? 17.277  51.829  -19.628 1.00 21.09 ? 283  GLN B N   1 
ATOM   4890 C  CA  . GLN B 1 283 ? 16.104  52.093  -20.494 1.00 22.09 ? 283  GLN B CA  1 
ATOM   4891 C  C   . GLN B 1 283 ? 16.510  52.004  -21.977 1.00 20.41 ? 283  GLN B C   1 
ATOM   4892 O  O   . GLN B 1 283 ? 17.645  52.315  -22.330 1.00 19.16 ? 283  GLN B O   1 
ATOM   4893 C  CB  . GLN B 1 283 ? 15.482  53.455  -20.193 1.00 24.02 ? 283  GLN B CB  1 
ATOM   4894 C  CG  . GLN B 1 283 ? 14.860  53.519  -18.806 1.00 26.88 ? 283  GLN B CG  1 
ATOM   4895 C  CD  . GLN B 1 283 ? 14.085  54.798  -18.545 1.00 30.29 ? 283  GLN B CD  1 
ATOM   4896 O  OE1 . GLN B 1 283 ? 13.572  55.436  -19.463 1.00 35.32 ? 283  GLN B OE1 1 
ATOM   4897 N  NE2 . GLN B 1 283 ? 13.978  55.168  -17.280 1.00 31.67 ? 283  GLN B NE2 1 
ATOM   4898 N  N   . VAL B 1 284 ? 15.584  51.582  -22.826 1.00 19.22 ? 284  VAL B N   1 
ATOM   4899 C  CA  . VAL B 1 284 ? 15.838  51.501  -24.258 1.00 19.73 ? 284  VAL B CA  1 
ATOM   4900 C  C   . VAL B 1 284 ? 16.172  52.918  -24.725 1.00 20.27 ? 284  VAL B C   1 
ATOM   4901 O  O   . VAL B 1 284 ? 15.425  53.843  -24.455 1.00 22.51 ? 284  VAL B O   1 
ATOM   4902 C  CB  . VAL B 1 284 ? 14.638  50.918  -25.036 1.00 18.82 ? 284  VAL B CB  1 
ATOM   4903 C  CG1 . VAL B 1 284 ? 14.913  50.911  -26.531 1.00 18.45 ? 284  VAL B CG1 1 
ATOM   4904 C  CG2 . VAL B 1 284 ? 14.325  49.499  -24.559 1.00 18.96 ? 284  VAL B CG2 1 
ATOM   4905 N  N   . ALA B 1 285 ? 17.314  53.083  -25.377 1.00 20.32 ? 285  ALA B N   1 
ATOM   4906 C  CA  . ALA B 1 285 ? 17.771  54.396  -25.798 1.00 20.16 ? 285  ALA B CA  1 
ATOM   4907 C  C   . ALA B 1 285 ? 16.988  54.896  -26.995 1.00 20.59 ? 285  ALA B C   1 
ATOM   4908 O  O   . ALA B 1 285 ? 16.653  54.133  -27.908 1.00 19.58 ? 285  ALA B O   1 
ATOM   4909 C  CB  . ALA B 1 285 ? 19.254  54.366  -26.137 1.00 20.72 ? 285  ALA B CB  1 
ATOM   4910 N  N   . ASN B 1 286 ? 16.715  56.200  -26.982 1.00 20.59 ? 286  ASN B N   1 
ATOM   4911 C  CA  . ASN B 1 286 ? 16.178  56.881  -28.130 1.00 20.27 ? 286  ASN B CA  1 
ATOM   4912 C  C   . ASN B 1 286 ? 17.340  57.486  -28.936 1.00 19.92 ? 286  ASN B C   1 
ATOM   4913 O  O   . ASN B 1 286 ? 17.937  58.494  -28.541 1.00 18.44 ? 286  ASN B O   1 
ATOM   4914 C  CB  . ASN B 1 286 ? 15.159  57.943  -27.681 1.00 20.49 ? 286  ASN B CB  1 
ATOM   4915 C  CG  . ASN B 1 286 ? 14.410  58.558  -28.835 1.00 20.88 ? 286  ASN B CG  1 
ATOM   4916 O  OD1 . ASN B 1 286 ? 14.794  58.406  -29.992 1.00 21.14 ? 286  ASN B OD1 1 
ATOM   4917 N  ND2 . ASN B 1 286 ? 13.318  59.255  -28.528 1.00 21.17 ? 286  ASN B ND2 1 
ATOM   4918 N  N   . TRP B 1 287 ? 17.646  56.861  -30.074 1.00 19.50 ? 287  TRP B N   1 
ATOM   4919 C  CA  . TRP B 1 287 ? 18.729  57.318  -30.937 1.00 19.94 ? 287  TRP B CA  1 
ATOM   4920 C  C   . TRP B 1 287 ? 18.135  58.066  -32.128 1.00 19.36 ? 287  TRP B C   1 
ATOM   4921 O  O   . TRP B 1 287 ? 17.661  57.445  -33.067 1.00 17.47 ? 287  TRP B O   1 
ATOM   4922 C  CB  . TRP B 1 287 ? 19.624  56.137  -31.396 1.00 20.47 ? 287  TRP B CB  1 
ATOM   4923 C  CG  . TRP B 1 287 ? 20.826  56.586  -32.138 1.00 20.17 ? 287  TRP B CG  1 
ATOM   4924 C  CD1 . TRP B 1 287 ? 21.994  57.014  -31.607 1.00 20.34 ? 287  TRP B CD1 1 
ATOM   4925 C  CD2 . TRP B 1 287 ? 20.965  56.696  -33.561 1.00 21.49 ? 287  TRP B CD2 1 
ATOM   4926 N  NE1 . TRP B 1 287 ? 22.859  57.388  -32.605 1.00 20.85 ? 287  TRP B NE1 1 
ATOM   4927 C  CE2 . TRP B 1 287 ? 22.256  57.192  -33.814 1.00 20.99 ? 287  TRP B CE2 1 
ATOM   4928 C  CE3 . TRP B 1 287 ? 20.119  56.419  -34.647 1.00 21.41 ? 287  TRP B CE3 1 
ATOM   4929 C  CZ2 . TRP B 1 287 ? 22.724  57.429  -35.101 1.00 21.74 ? 287  TRP B CZ2 1 
ATOM   4930 C  CZ3 . TRP B 1 287 ? 20.570  56.663  -35.913 1.00 22.03 ? 287  TRP B CZ3 1 
ATOM   4931 C  CH2 . TRP B 1 287 ? 21.870  57.158  -36.140 1.00 22.54 ? 287  TRP B CH2 1 
ATOM   4932 N  N   . ASN B 1 288 ? 18.152  59.401  -32.068 1.00 18.78 ? 288  ASN B N   1 
ATOM   4933 C  CA  . ASN B 1 288 ? 17.591  60.246  -33.119 1.00 19.46 ? 288  ASN B CA  1 
ATOM   4934 C  C   . ASN B 1 288 ? 16.179  59.839  -33.528 1.00 18.70 ? 288  ASN B C   1 
ATOM   4935 O  O   . ASN B 1 288 ? 15.844  59.816  -34.704 1.00 17.85 ? 288  ASN B O   1 
ATOM   4936 C  CB  . ASN B 1 288 ? 18.512  60.256  -34.358 1.00 20.70 ? 288  ASN B CB  1 
ATOM   4937 C  CG  . ASN B 1 288 ? 19.900  60.787  -34.043 1.00 21.54 ? 288  ASN B CG  1 
ATOM   4938 O  OD1 . ASN B 1 288 ? 20.902  60.125  -34.292 1.00 24.08 ? 288  ASN B OD1 1 
ATOM   4939 N  ND2 . ASN B 1 288 ? 19.959  61.970  -33.468 1.00 21.51 ? 288  ASN B ND2 1 
ATOM   4940 N  N   . GLY B 1 289 ? 15.352  59.499  -32.556 1.00 18.04 ? 289  GLY B N   1 
ATOM   4941 C  CA  . GLY B 1 289 ? 13.983  59.111  -32.860 1.00 18.38 ? 289  GLY B CA  1 
ATOM   4942 C  C   . GLY B 1 289 ? 13.812  57.634  -33.148 1.00 17.67 ? 289  GLY B C   1 
ATOM   4943 O  O   . GLY B 1 289 ? 12.696  57.186  -33.385 1.00 16.83 ? 289  GLY B O   1 
ATOM   4944 N  N   . TYR B 1 290 ? 14.905  56.870  -33.133 1.00 17.74 ? 290  TYR B N   1 
ATOM   4945 C  CA  . TYR B 1 290 ? 14.829  55.413  -33.356 1.00 17.99 ? 290  TYR B CA  1 
ATOM   4946 C  C   . TYR B 1 290 ? 15.097  54.597  -32.095 1.00 17.34 ? 290  TYR B C   1 
ATOM   4947 O  O   . TYR B 1 290 ? 15.824  55.034  -31.205 1.00 17.43 ? 290  TYR B O   1 
ATOM   4948 C  CB  . TYR B 1 290 ? 15.846  54.977  -34.391 1.00 18.86 ? 290  TYR B CB  1 
ATOM   4949 C  CG  . TYR B 1 290 ? 15.730  55.637  -35.745 1.00 20.56 ? 290  TYR B CG  1 
ATOM   4950 C  CD1 . TYR B 1 290 ? 16.446  56.788  -36.043 1.00 20.95 ? 290  TYR B CD1 1 
ATOM   4951 C  CD2 . TYR B 1 290 ? 14.941  55.082  -36.745 1.00 21.63 ? 290  TYR B CD2 1 
ATOM   4952 C  CE1 . TYR B 1 290 ? 16.352  57.385  -37.291 1.00 22.23 ? 290  TYR B CE1 1 
ATOM   4953 C  CE2 . TYR B 1 290 ? 14.852  55.668  -38.006 1.00 22.13 ? 290  TYR B CE2 1 
ATOM   4954 C  CZ  . TYR B 1 290 ? 15.561  56.819  -38.273 1.00 22.33 ? 290  TYR B CZ  1 
ATOM   4955 O  OH  . TYR B 1 290 ? 15.485  57.404  -39.522 1.00 22.73 ? 290  TYR B OH  1 
ATOM   4956 N  N   . GLN B 1 291 ? 14.525  53.397  -32.056 1.00 16.20 ? 291  GLN B N   1 
ATOM   4957 C  CA  . GLN B 1 291 ? 14.937  52.354  -31.116 1.00 15.44 ? 291  GLN B CA  1 
ATOM   4958 C  C   . GLN B 1 291 ? 15.750  51.338  -31.917 1.00 15.19 ? 291  GLN B C   1 
ATOM   4959 O  O   . GLN B 1 291 ? 15.414  51.032  -33.072 1.00 14.65 ? 291  GLN B O   1 
ATOM   4960 C  CB  . GLN B 1 291 ? 13.738  51.682  -30.449 1.00 15.46 ? 291  GLN B CB  1 
ATOM   4961 C  CG  . GLN B 1 291 ? 12.722  51.075  -31.407 1.00 15.18 ? 291  GLN B CG  1 
ATOM   4962 C  CD  . GLN B 1 291 ? 11.537  50.464  -30.688 1.00 14.89 ? 291  GLN B CD  1 
ATOM   4963 O  OE1 . GLN B 1 291 ? 11.705  49.664  -29.767 1.00 14.23 ? 291  GLN B OE1 1 
ATOM   4964 N  NE2 . GLN B 1 291 ? 10.325  50.840  -31.112 1.00 14.46 ? 291  GLN B NE2 1 
ATOM   4965 N  N   . LEU B 1 292 ? 16.836  50.863  -31.318 1.00 14.80 ? 292  LEU B N   1 
ATOM   4966 C  CA  . LEU B 1 292 ? 17.803  50.005  -31.998 1.00 15.43 ? 292  LEU B CA  1 
ATOM   4967 C  C   . LEU B 1 292 ? 17.921  48.683  -31.245 1.00 15.72 ? 292  LEU B C   1 
ATOM   4968 O  O   . LEU B 1 292 ? 17.929  48.676  -30.005 1.00 16.39 ? 292  LEU B O   1 
ATOM   4969 C  CB  . LEU B 1 292 ? 19.173  50.687  -32.047 1.00 15.49 ? 292  LEU B CB  1 
ATOM   4970 C  CG  . LEU B 1 292 ? 19.201  52.102  -32.637 1.00 15.68 ? 292  LEU B CG  1 
ATOM   4971 C  CD1 . LEU B 1 292 ? 20.550  52.738  -32.369 1.00 16.23 ? 292  LEU B CD1 1 
ATOM   4972 C  CD2 . LEU B 1 292 ? 18.917  52.058  -34.125 1.00 15.76 ? 292  LEU B CD2 1 
ATOM   4973 N  N   . VAL B 1 293 ? 18.002  47.577  -31.977 1.00 15.02 ? 293  VAL B N   1 
ATOM   4974 C  CA  . VAL B 1 293 ? 18.166  46.248  -31.353 1.00 15.36 ? 293  VAL B CA  1 
ATOM   4975 C  C   . VAL B 1 293 ? 19.216  45.439  -32.109 1.00 15.21 ? 293  VAL B C   1 
ATOM   4976 O  O   . VAL B 1 293 ? 19.340  45.537  -33.341 1.00 14.49 ? 293  VAL B O   1 
ATOM   4977 C  CB  . VAL B 1 293 ? 16.819  45.466  -31.288 1.00 15.56 ? 293  VAL B CB  1 
ATOM   4978 C  CG1 . VAL B 1 293 ? 17.005  43.996  -30.932 1.00 15.91 ? 293  VAL B CG1 1 
ATOM   4979 C  CG2 . VAL B 1 293 ? 15.902  46.106  -30.278 1.00 15.92 ? 293  VAL B CG2 1 
ATOM   4980 N  N   . ILE B 1 294 ? 20.001  44.681  -31.358 1.00 15.66 ? 294  ILE B N   1 
ATOM   4981 C  CA  . ILE B 1 294 ? 20.968  43.765  -31.943 1.00 17.07 ? 294  ILE B CA  1 
ATOM   4982 C  C   . ILE B 1 294 ? 20.474  42.362  -31.637 1.00 16.67 ? 294  ILE B C   1 
ATOM   4983 O  O   . ILE B 1 294 ? 20.025  42.083  -30.519 1.00 15.58 ? 294  ILE B O   1 
ATOM   4984 C  CB  . ILE B 1 294 ? 22.380  44.014  -31.402 1.00 18.94 ? 294  ILE B CB  1 
ATOM   4985 C  CG1 . ILE B 1 294 ? 22.833  45.421  -31.806 1.00 20.78 ? 294  ILE B CG1 1 
ATOM   4986 C  CG2 . ILE B 1 294 ? 23.367  42.985  -31.948 1.00 19.41 ? 294  ILE B CG2 1 
ATOM   4987 C  CD1 . ILE B 1 294 ? 23.547  46.148  -30.700 1.00 22.65 ? 294  ILE B CD1 1 
ATOM   4988 N  N   . ALA B 1 295 ? 20.523  41.506  -32.651 1.00 16.97 ? 295  ALA B N   1 
ATOM   4989 C  CA  . ALA B 1 295 ? 19.915  40.177  -32.578 1.00 17.47 ? 295  ALA B CA  1 
ATOM   4990 C  C   . ALA B 1 295 ? 20.795  39.136  -33.236 1.00 17.58 ? 295  ALA B C   1 
ATOM   4991 O  O   . ALA B 1 295 ? 21.372  39.392  -34.288 1.00 17.57 ? 295  ALA B O   1 
ATOM   4992 C  CB  . ALA B 1 295 ? 18.564  40.207  -33.275 1.00 17.97 ? 295  ALA B CB  1 
ATOM   4993 N  N   . MET B 1 296 ? 20.881  37.958  -32.629 1.00 17.92 ? 296  MET B N   1 
ATOM   4994 C  CA  . MET B 1 296 ? 21.407  36.781  -33.326 1.00 18.60 ? 296  MET B CA  1 
ATOM   4995 C  C   . MET B 1 296 ? 20.372  36.238  -34.319 1.00 18.04 ? 296  MET B C   1 
ATOM   4996 O  O   . MET B 1 296 ? 19.194  36.110  -33.990 1.00 18.29 ? 296  MET B O   1 
ATOM   4997 C  CB  . MET B 1 296 ? 21.800  35.683  -32.323 1.00 19.72 ? 296  MET B CB  1 
ATOM   4998 C  CG  . MET B 1 296 ? 23.051  36.044  -31.518 1.00 20.63 ? 296  MET B CG  1 
ATOM   4999 S  SD  . MET B 1 296 ? 23.482  34.736  -30.363 1.00 24.98 ? 296  MET B SD  1 
ATOM   5000 C  CE  . MET B 1 296 ? 24.249  33.590  -31.514 1.00 22.89 ? 296  MET B CE  1 
ATOM   5001 N  N   . MET B 1 297 ? 20.815  35.911  -35.527 1.00 17.84 ? 297  MET B N   1 
ATOM   5002 C  CA  . MET B 1 297 ? 19.973  35.265  -36.525 1.00 17.77 ? 297  MET B CA  1 
ATOM   5003 C  C   . MET B 1 297 ? 20.829  34.324  -37.350 1.00 17.62 ? 297  MET B C   1 
ATOM   5004 O  O   . MET B 1 297 ? 22.064  34.484  -37.438 1.00 17.32 ? 297  MET B O   1 
ATOM   5005 C  CB  . MET B 1 297 ? 19.341  36.280  -37.499 1.00 18.12 ? 297  MET B CB  1 
ATOM   5006 C  CG  . MET B 1 297 ? 18.661  37.493  -36.892 1.00 18.35 ? 297  MET B CG  1 
ATOM   5007 S  SD  . MET B 1 297 ? 17.883  38.455  -38.208 1.00 19.05 ? 297  MET B SD  1 
ATOM   5008 C  CE  . MET B 1 297 ? 16.951  39.603  -37.173 1.00 20.45 ? 297  MET B CE  1 
ATOM   5009 N  N   . GLY B 1 298 ? 20.166  33.368  -37.979 1.00 16.93 ? 298  GLY B N   1 
ATOM   5010 C  CA  . GLY B 1 298 ? 20.826  32.443  -38.866 1.00 17.69 ? 298  GLY B CA  1 
ATOM   5011 C  C   . GLY B 1 298 ? 19.859  31.431  -39.439 1.00 17.90 ? 298  GLY B C   1 
ATOM   5012 O  O   . GLY B 1 298 ? 18.761  31.258  -38.913 1.00 19.14 ? 298  GLY B O   1 
ATOM   5013 N  N   . ILE B 1 299 ? 20.286  30.750  -40.501 1.00 17.79 ? 299  ILE B N   1 
ATOM   5014 C  CA  . ILE B 1 299 ? 19.435  29.813  -41.243 1.00 18.31 ? 299  ILE B CA  1 
ATOM   5015 C  C   . ILE B 1 299 ? 19.137  28.648  -40.311 1.00 18.42 ? 299  ILE B C   1 
ATOM   5016 O  O   . ILE B 1 299 ? 20.053  28.135  -39.680 1.00 17.77 ? 299  ILE B O   1 
ATOM   5017 C  CB  . ILE B 1 299 ? 20.152  29.296  -42.531 1.00 18.34 ? 299  ILE B CB  1 
ATOM   5018 C  CG1 . ILE B 1 299 ? 20.335  30.439  -43.527 1.00 19.20 ? 299  ILE B CG1 1 
ATOM   5019 C  CG2 . ILE B 1 299 ? 19.370  28.160  -43.211 1.00 18.51 ? 299  ILE B CG2 1 
ATOM   5020 C  CD1 . ILE B 1 299 ? 21.193  30.100  -44.746 1.00 18.88 ? 299  ILE B CD1 1 
ATOM   5021 N  N   . PRO B 1 300 ? 17.859  28.238  -40.203 1.00 20.00 ? 300  PRO B N   1 
ATOM   5022 C  CA  . PRO B 1 300 ? 17.565  27.030  -39.436 1.00 20.73 ? 300  PRO B CA  1 
ATOM   5023 C  C   . PRO B 1 300 ? 18.369  25.823  -39.891 1.00 22.13 ? 300  PRO B C   1 
ATOM   5024 O  O   . PRO B 1 300 ? 18.605  25.656  -41.082 1.00 23.06 ? 300  PRO B O   1 
ATOM   5025 C  CB  . PRO B 1 300 ? 16.066  26.818  -39.674 1.00 19.92 ? 300  PRO B CB  1 
ATOM   5026 C  CG  . PRO B 1 300 ? 15.554  28.200  -39.837 1.00 19.95 ? 300  PRO B CG  1 
ATOM   5027 C  CD  . PRO B 1 300 ? 16.616  28.910  -40.636 1.00 20.01 ? 300  PRO B CD  1 
ATOM   5028 N  N   . ASN B 1 301 ? 18.837  25.039  -38.924 1.00 23.74 ? 301  ASN B N   1 
ATOM   5029 C  CA  . ASN B 1 301 ? 19.610  23.824  -39.179 1.00 25.74 ? 301  ASN B CA  1 
ATOM   5030 C  C   . ASN B 1 301 ? 20.972  24.019  -39.825 1.00 26.39 ? 301  ASN B C   1 
ATOM   5031 O  O   . ASN B 1 301 ? 21.560  23.058  -40.287 1.00 28.01 ? 301  ASN B O   1 
ATOM   5032 C  CB  . ASN B 1 301 ? 18.786  22.809  -39.994 1.00 26.92 ? 301  ASN B CB  1 
ATOM   5033 C  CG  . ASN B 1 301 ? 17.585  22.308  -39.231 1.00 27.73 ? 301  ASN B CG  1 
ATOM   5034 O  OD1 . ASN B 1 301 ? 16.447  22.576  -39.605 1.00 29.07 ? 301  ASN B OD1 1 
ATOM   5035 N  ND2 . ASN B 1 301 ? 17.834  21.602  -38.131 1.00 27.31 ? 301  ASN B ND2 1 
ATOM   5036 N  N   . GLN B 1 302 ? 21.490  25.242  -39.849 1.00 26.57 ? 302  GLN B N   1 
ATOM   5037 C  CA  . GLN B 1 302 ? 22.867  25.462  -40.267 1.00 26.07 ? 302  GLN B CA  1 
ATOM   5038 C  C   . GLN B 1 302 ? 23.665  26.101  -39.127 1.00 25.75 ? 302  GLN B C   1 
ATOM   5039 O  O   . GLN B 1 302 ? 23.109  26.777  -38.251 1.00 22.85 ? 302  GLN B O   1 
ATOM   5040 C  CB  . GLN B 1 302 ? 22.920  26.339  -41.510 1.00 29.38 ? 302  GLN B CB  1 
ATOM   5041 C  CG  . GLN B 1 302 ? 22.395  25.657  -42.778 1.00 33.49 ? 302  GLN B CG  1 
ATOM   5042 C  CD  . GLN B 1 302 ? 22.795  26.374  -44.062 1.00 39.01 ? 302  GLN B CD  1 
ATOM   5043 O  OE1 . GLN B 1 302 ? 21.965  26.590  -44.945 1.00 45.46 ? 302  GLN B OE1 1 
ATOM   5044 N  NE2 . GLN B 1 302 ? 24.076  26.726  -44.184 1.00 42.49 ? 302  GLN B NE2 1 
ATOM   5045 N  N   . ASN B 1 303 ? 24.977  25.881  -39.148 1.00 24.69 ? 303  ASN B N   1 
ATOM   5046 C  CA  . ASN B 1 303 ? 25.881  26.554  -38.243 1.00 24.36 ? 303  ASN B CA  1 
ATOM   5047 C  C   . ASN B 1 303 ? 26.081  27.963  -38.773 1.00 21.74 ? 303  ASN B C   1 
ATOM   5048 O  O   . ASN B 1 303 ? 26.897  28.197  -39.672 1.00 19.33 ? 303  ASN B O   1 
ATOM   5049 C  CB  . ASN B 1 303 ? 27.196  25.793  -38.196 1.00 26.96 ? 303  ASN B CB  1 
ATOM   5050 C  CG  . ASN B 1 303 ? 28.151  26.314  -37.147 1.00 29.63 ? 303  ASN B CG  1 
ATOM   5051 O  OD1 . ASN B 1 303 ? 27.982  27.389  -36.564 1.00 28.74 ? 303  ASN B OD1 1 
ATOM   5052 N  ND2 . ASN B 1 303 ? 29.185  25.528  -36.901 1.00 34.25 ? 303  ASN B ND2 1 
ATOM   5053 N  N   . ASP B 1 304 ? 25.308  28.899  -38.220 1.00 19.44 ? 304  ASP B N   1 
ATOM   5054 C  CA  . ASP B 1 304 ? 25.214  30.230  -38.787 1.00 18.14 ? 304  ASP B CA  1 
ATOM   5055 C  C   . ASP B 1 304 ? 24.908  31.234  -37.685 1.00 17.88 ? 304  ASP B C   1 
ATOM   5056 O  O   . ASP B 1 304 ? 23.774  31.697  -37.549 1.00 18.03 ? 304  ASP B O   1 
ATOM   5057 C  CB  . ASP B 1 304 ? 24.131  30.218  -39.861 1.00 17.35 ? 304  ASP B CB  1 
ATOM   5058 C  CG  . ASP B 1 304 ? 24.011  31.528  -40.604 1.00 17.38 ? 304  ASP B CG  1 
ATOM   5059 O  OD1 . ASP B 1 304 ? 24.968  32.338  -40.600 1.00 17.68 ? 304  ASP B OD1 1 
ATOM   5060 O  OD2 . ASP B 1 304 ? 22.947  31.730  -41.222 1.00 17.39 ? 304  ASP B OD2 1 
ATOM   5061 N  N   . ASN B 1 305 ? 25.918  31.554  -36.891 1.00 17.46 ? 305  ASN B N   1 
ATOM   5062 C  CA  . ASN B 1 305 ? 25.724  32.379  -35.692 1.00 17.77 ? 305  ASN B CA  1 
ATOM   5063 C  C   . ASN B 1 305 ? 26.367  33.761  -35.843 1.00 17.11 ? 305  ASN B C   1 
ATOM   5064 O  O   . ASN B 1 305 ? 27.589  33.912  -35.666 1.00 16.93 ? 305  ASN B O   1 
ATOM   5065 C  CB  . ASN B 1 305 ? 26.264  31.651  -34.456 1.00 17.73 ? 305  ASN B CB  1 
ATOM   5066 C  CG  . ASN B 1 305 ? 25.578  30.318  -34.219 1.00 19.13 ? 305  ASN B CG  1 
ATOM   5067 O  OD1 . ASN B 1 305 ? 24.359  30.254  -34.047 1.00 19.62 ? 305  ASN B OD1 1 
ATOM   5068 N  ND2 . ASN B 1 305 ? 26.359  29.232  -34.229 1.00 20.27 ? 305  ASN B ND2 1 
ATOM   5069 N  N   . HIS B 1 306 ? 25.543  34.749  -36.204 1.00 16.59 ? 306  HIS B N   1 
ATOM   5070 C  CA  . HIS B 1 306 ? 25.993  36.140  -36.406 1.00 16.35 ? 306  HIS B CA  1 
ATOM   5071 C  C   . HIS B 1 306 ? 24.962  37.145  -35.916 1.00 16.45 ? 306  HIS B C   1 
ATOM   5072 O  O   . HIS B 1 306 ? 23.777  36.813  -35.745 1.00 16.99 ? 306  HIS B O   1 
ATOM   5073 C  CB  . HIS B 1 306 ? 26.336  36.398  -37.874 1.00 16.50 ? 306  HIS B CB  1 
ATOM   5074 C  CG  . HIS B 1 306 ? 27.413  35.501  -38.387 1.00 16.35 ? 306  HIS B CG  1 
ATOM   5075 N  ND1 . HIS B 1 306 ? 28.752  35.772  -38.213 1.00 15.97 ? 306  HIS B ND1 1 
ATOM   5076 C  CD2 . HIS B 1 306 ? 27.345  34.290  -38.990 1.00 16.79 ? 306  HIS B CD2 1 
ATOM   5077 C  CE1 . HIS B 1 306 ? 29.462  34.790  -38.735 1.00 16.92 ? 306  HIS B CE1 1 
ATOM   5078 N  NE2 . HIS B 1 306 ? 28.631  33.876  -39.211 1.00 16.95 ? 306  HIS B NE2 1 
ATOM   5079 N  N   . ILE B 1 307 ? 25.428  38.368  -35.667 1.00 15.42 ? 307  ILE B N   1 
ATOM   5080 C  CA  . ILE B 1 307 ? 24.589  39.404  -35.115 1.00 15.44 ? 307  ILE B CA  1 
ATOM   5081 C  C   . ILE B 1 307 ? 24.256  40.487  -36.147 1.00 15.92 ? 307  ILE B C   1 
ATOM   5082 O  O   . ILE B 1 307 ? 25.075  40.839  -37.016 1.00 15.46 ? 307  ILE B O   1 
ATOM   5083 C  CB  . ILE B 1 307 ? 25.169  40.016  -33.821 1.00 15.68 ? 307  ILE B CB  1 
ATOM   5084 C  CG1 . ILE B 1 307 ? 26.571  40.590  -34.055 1.00 15.49 ? 307  ILE B CG1 1 
ATOM   5085 C  CG2 . ILE B 1 307 ? 25.174  38.974  -32.688 1.00 15.28 ? 307  ILE B CG2 1 
ATOM   5086 C  CD1 . ILE B 1 307 ? 27.132  41.295  -32.843 1.00 15.80 ? 307  ILE B CD1 1 
ATOM   5087 N  N   . TYR B 1 308 ? 23.013  40.973  -36.031 1.00 15.95 ? 308  TYR B N   1 
ATOM   5088 C  CA  . TYR B 1 308 ? 22.361  41.847  -36.986 1.00 16.15 ? 308  TYR B CA  1 
ATOM   5089 C  C   . TYR B 1 308 ? 21.881  43.098  -36.253 1.00 16.63 ? 308  TYR B C   1 
ATOM   5090 O  O   . TYR B 1 308 ? 21.546  43.045  -35.075 1.00 17.08 ? 308  TYR B O   1 
ATOM   5091 C  CB  . TYR B 1 308 ? 21.155  41.126  -37.606 1.00 15.69 ? 308  TYR B CB  1 
ATOM   5092 C  CG  . TYR B 1 308 ? 21.547  39.983  -38.517 1.00 14.98 ? 308  TYR B CG  1 
ATOM   5093 C  CD1 . TYR B 1 308 ? 22.066  38.812  -38.000 1.00 14.66 ? 308  TYR B CD1 1 
ATOM   5094 C  CD2 . TYR B 1 308 ? 21.444  40.099  -39.900 1.00 14.79 ? 308  TYR B CD2 1 
ATOM   5095 C  CE1 . TYR B 1 308 ? 22.460  37.773  -38.826 1.00 14.47 ? 308  TYR B CE1 1 
ATOM   5096 C  CE2 . TYR B 1 308 ? 21.836  39.064  -40.739 1.00 14.69 ? 308  TYR B CE2 1 
ATOM   5097 C  CZ  . TYR B 1 308 ? 22.337  37.901  -40.190 1.00 14.53 ? 308  TYR B CZ  1 
ATOM   5098 O  OH  . TYR B 1 308 ? 22.721  36.872  -40.996 1.00 14.01 ? 308  TYR B OH  1 
ATOM   5099 N  N   . LEU B 1 309 ? 21.870  44.223  -36.946 1.00 16.92 ? 309  LEU B N   1 
ATOM   5100 C  CA  . LEU B 1 309 ? 21.355  45.464  -36.377 1.00 17.41 ? 309  LEU B CA  1 
ATOM   5101 C  C   . LEU B 1 309 ? 19.957  45.756  -36.932 1.00 17.15 ? 309  LEU B C   1 
ATOM   5102 O  O   . LEU B 1 309 ? 19.743  45.822  -38.154 1.00 16.21 ? 309  LEU B O   1 
ATOM   5103 C  CB  . LEU B 1 309 ? 22.300  46.635  -36.674 1.00 17.72 ? 309  LEU B CB  1 
ATOM   5104 C  CG  . LEU B 1 309 ? 21.811  48.033  -36.247 1.00 18.00 ? 309  LEU B CG  1 
ATOM   5105 C  CD1 . LEU B 1 309 ? 21.574  48.072  -34.754 1.00 18.78 ? 309  LEU B CD1 1 
ATOM   5106 C  CD2 . LEU B 1 309 ? 22.832  49.095  -36.640 1.00 18.18 ? 309  LEU B CD2 1 
ATOM   5107 N  N   . LEU B 1 310 ? 19.015  45.962  -36.027 1.00 17.42 ? 310  LEU B N   1 
ATOM   5108 C  CA  . LEU B 1 310 ? 17.669  46.334  -36.424 1.00 18.51 ? 310  LEU B CA  1 
ATOM   5109 C  C   . LEU B 1 310 ? 17.251  47.665  -35.853 1.00 18.57 ? 310  LEU B C   1 
ATOM   5110 O  O   . LEU B 1 310 ? 17.766  48.109  -34.821 1.00 17.71 ? 310  LEU B O   1 
ATOM   5111 C  CB  . LEU B 1 310 ? 16.660  45.274  -35.991 1.00 19.38 ? 310  LEU B CB  1 
ATOM   5112 C  CG  . LEU B 1 310 ? 16.993  43.875  -36.488 1.00 20.71 ? 310  LEU B CG  1 
ATOM   5113 C  CD1 . LEU B 1 310 ? 17.358  43.011  -35.302 1.00 20.73 ? 310  LEU B CD1 1 
ATOM   5114 C  CD2 . LEU B 1 310 ? 15.805  43.306  -37.244 1.00 21.61 ? 310  LEU B CD2 1 
ATOM   5115 N  N   . TYR B 1 311 ? 16.277  48.285  -36.515 1.00 19.06 ? 311  TYR B N   1 
ATOM   5116 C  CA  . TYR B 1 311 ? 15.729  49.547  -36.028 1.00 18.88 ? 311  TYR B CA  1 
ATOM   5117 C  C   . TYR B 1 311 ? 14.254  49.673  -36.315 1.00 18.59 ? 311  TYR B C   1 
ATOM   5118 O  O   . TYR B 1 311 ? 13.705  48.947  -37.125 1.00 18.42 ? 311  TYR B O   1 
ATOM   5119 C  CB  . TYR B 1 311 ? 16.478  50.739  -36.635 1.00 19.57 ? 311  TYR B CB  1 
ATOM   5120 C  CG  . TYR B 1 311 ? 16.322  50.909  -38.133 1.00 19.99 ? 311  TYR B CG  1 
ATOM   5121 C  CD1 . TYR B 1 311 ? 17.009  50.096  -39.019 1.00 20.82 ? 311  TYR B CD1 1 
ATOM   5122 C  CD2 . TYR B 1 311 ? 15.507  51.911  -38.663 1.00 20.94 ? 311  TYR B CD2 1 
ATOM   5123 C  CE1 . TYR B 1 311 ? 16.882  50.257  -40.399 1.00 21.96 ? 311  TYR B CE1 1 
ATOM   5124 C  CE2 . TYR B 1 311 ? 15.367  52.073  -40.035 1.00 21.77 ? 311  TYR B CE2 1 
ATOM   5125 C  CZ  . TYR B 1 311 ? 16.064  51.249  -40.899 1.00 21.68 ? 311  TYR B CZ  1 
ATOM   5126 O  OH  . TYR B 1 311 ? 15.934  51.409  -42.263 1.00 22.91 ? 311  TYR B OH  1 
ATOM   5127 N  N   . ASN B 1 312 ? 13.637  50.626  -35.625 1.00 18.80 ? 312  ASN B N   1 
ATOM   5128 C  CA  . ASN B 1 312 ? 12.241  50.981  -35.772 1.00 18.96 ? 312  ASN B CA  1 
ATOM   5129 C  C   . ASN B 1 312 ? 12.137  52.373  -35.157 1.00 19.81 ? 312  ASN B C   1 
ATOM   5130 O  O   . ASN B 1 312 ? 13.022  52.776  -34.396 1.00 19.15 ? 312  ASN B O   1 
ATOM   5131 C  CB  . ASN B 1 312 ? 11.373  49.975  -34.994 1.00 19.02 ? 312  ASN B CB  1 
ATOM   5132 C  CG  . ASN B 1 312 ? 9.885   50.084  -35.291 1.00 18.29 ? 312  ASN B CG  1 
ATOM   5133 O  OD1 . ASN B 1 312 ? 9.431   50.916  -36.085 1.00 17.07 ? 312  ASN B OD1 1 
ATOM   5134 N  ND2 . ASN B 1 312 ? 9.107   49.212  -34.643 1.00 18.38 ? 312  ASN B ND2 1 
ATOM   5135 N  N   . LYS B 1 313 ? 11.083  53.116  -35.475 1.00 21.61 ? 313  LYS B N   1 
ATOM   5136 C  CA  . LYS B 1 313 ? 10.876  54.411  -34.828 1.00 23.38 ? 313  LYS B CA  1 
ATOM   5137 C  C   . LYS B 1 313 ? 10.658  54.162  -33.336 1.00 21.52 ? 313  LYS B C   1 
ATOM   5138 O  O   . LYS B 1 313 ? 10.038  53.165  -32.961 1.00 19.23 ? 313  LYS B O   1 
ATOM   5139 C  CB  . LYS B 1 313 ? 9.694   55.165  -35.452 1.00 26.58 ? 313  LYS B CB  1 
ATOM   5140 C  CG  . LYS B 1 313 ? 9.947   55.627  -36.893 1.00 31.23 ? 313  LYS B CG  1 
ATOM   5141 C  CD  . LYS B 1 313 ? 11.116  56.619  -37.009 1.00 33.93 ? 313  LYS B CD  1 
ATOM   5142 C  CE  . LYS B 1 313 ? 11.119  57.363  -38.341 1.00 36.54 ? 313  LYS B CE  1 
ATOM   5143 N  NZ  . LYS B 1 313 ? 12.191  58.406  -38.401 1.00 38.15 ? 313  LYS B NZ  1 
ATOM   5144 N  N   . TYR B 1 314 ? 11.195  55.051  -32.494 1.00 21.01 ? 314  TYR B N   1 
ATOM   5145 C  CA  . TYR B 1 314 ? 11.071  54.889  -31.038 1.00 21.13 ? 314  TYR B CA  1 
ATOM   5146 C  C   . TYR B 1 314 ? 9.600   54.823  -30.657 1.00 20.40 ? 314  TYR B C   1 
ATOM   5147 O  O   . TYR B 1 314 ? 8.785   55.601  -31.154 1.00 19.70 ? 314  TYR B O   1 
ATOM   5148 C  CB  . TYR B 1 314 ? 11.761  56.015  -30.268 1.00 21.31 ? 314  TYR B CB  1 
ATOM   5149 C  CG  . TYR B 1 314 ? 11.961  55.704  -28.805 1.00 22.16 ? 314  TYR B CG  1 
ATOM   5150 C  CD1 . TYR B 1 314 ? 13.078  55.013  -28.388 1.00 22.99 ? 314  TYR B CD1 1 
ATOM   5151 C  CD2 . TYR B 1 314 ? 11.022  56.091  -27.829 1.00 22.94 ? 314  TYR B CD2 1 
ATOM   5152 C  CE1 . TYR B 1 314 ? 13.277  54.701  -27.056 1.00 23.47 ? 314  TYR B CE1 1 
ATOM   5153 C  CE2 . TYR B 1 314 ? 11.222  55.780  -26.486 1.00 23.50 ? 314  TYR B CE2 1 
ATOM   5154 C  CZ  . TYR B 1 314 ? 12.358  55.087  -26.115 1.00 24.68 ? 314  TYR B CZ  1 
ATOM   5155 O  OH  . TYR B 1 314 ? 12.621  54.744  -24.801 1.00 29.23 ? 314  TYR B OH  1 
ATOM   5156 N  N   . GLY B 1 315 ? 9.265   53.844  -29.831 1.00 19.88 ? 315  GLY B N   1 
ATOM   5157 C  CA  . GLY B 1 315 ? 7.905   53.668  -29.345 1.00 20.33 ? 315  GLY B CA  1 
ATOM   5158 C  C   . GLY B 1 315 ? 6.929   52.956  -30.270 1.00 19.97 ? 315  GLY B C   1 
ATOM   5159 O  O   . GLY B 1 315 ? 5.838   52.582  -29.829 1.00 21.15 ? 315  GLY B O   1 
ATOM   5160 N  N   . ASP B 1 316 ? 7.296   52.766  -31.539 1.00 19.36 ? 316  ASP B N   1 
ATOM   5161 C  CA  . ASP B 1 316 ? 6.454   52.035  -32.490 1.00 18.74 ? 316  ASP B CA  1 
ATOM   5162 C  C   . ASP B 1 316 ? 6.286   50.617  -31.950 1.00 18.60 ? 316  ASP B C   1 
ATOM   5163 O  O   . ASP B 1 316 ? 7.219   50.065  -31.356 1.00 19.19 ? 316  ASP B O   1 
ATOM   5164 C  CB  . ASP B 1 316 ? 7.093   52.046  -33.887 1.00 18.43 ? 316  ASP B CB  1 
ATOM   5165 C  CG  . ASP B 1 316 ? 6.319   51.228  -34.907 1.00 18.46 ? 316  ASP B CG  1 
ATOM   5166 O  OD1 . ASP B 1 316 ? 6.195   49.988  -34.745 1.00 17.37 ? 316  ASP B OD1 1 
ATOM   5167 O  OD2 . ASP B 1 316 ? 5.848   51.827  -35.911 1.00 19.44 ? 316  ASP B OD2 1 
ATOM   5168 N  N   . ASN B 1 317 ? 5.101   50.050  -32.147 1.00 18.59 ? 317  ASN B N   1 
ATOM   5169 C  CA  . ASN B 1 317 ? 4.702   48.791  -31.506 1.00 18.77 ? 317  ASN B CA  1 
ATOM   5170 C  C   . ASN B 1 317 ? 4.493   47.614  -32.444 1.00 18.32 ? 317  ASN B C   1 
ATOM   5171 O  O   . ASN B 1 317 ? 4.084   46.551  -31.985 1.00 17.57 ? 317  ASN B O   1 
ATOM   5172 C  CB  . ASN B 1 317 ? 3.400   48.985  -30.718 1.00 18.42 ? 317  ASN B CB  1 
ATOM   5173 C  CG  . ASN B 1 317 ? 3.558   49.906  -29.526 1.00 19.17 ? 317  ASN B CG  1 
ATOM   5174 O  OD1 . ASN B 1 317 ? 4.595   49.924  -28.863 1.00 19.84 ? 317  ASN B OD1 1 
ATOM   5175 N  ND2 . ASN B 1 317 ? 2.521   50.675  -29.241 1.00 19.13 ? 317  ASN B ND2 1 
ATOM   5176 N  N   . GLU B 1 318 ? 4.744   47.790  -33.741 1.00 19.21 ? 318  GLU B N   1 
ATOM   5177 C  CA  . GLU B 1 318 ? 4.537   46.719  -34.722 1.00 20.59 ? 318  GLU B CA  1 
ATOM   5178 C  C   . GLU B 1 318 ? 5.815   45.944  -35.023 1.00 20.65 ? 318  GLU B C   1 
ATOM   5179 O  O   . GLU B 1 318 ? 6.842   46.540  -35.388 1.00 19.60 ? 318  GLU B O   1 
ATOM   5180 C  CB  . GLU B 1 318 ? 4.009   47.285  -36.040 1.00 22.89 ? 318  GLU B CB  1 
ATOM   5181 C  CG  . GLU B 1 318 ? 2.670   48.005  -35.936 1.00 25.63 ? 318  GLU B CG  1 
ATOM   5182 C  CD  . GLU B 1 318 ? 1.593   47.153  -35.275 1.00 28.98 ? 318  GLU B CD  1 
ATOM   5183 O  OE1 . GLU B 1 318 ? 1.531   45.912  -35.515 1.00 30.71 ? 318  GLU B OE1 1 
ATOM   5184 O  OE2 . GLU B 1 318 ? 0.804   47.734  -34.503 1.00 33.24 ? 318  GLU B OE2 1 
ATOM   5185 N  N   . LEU B 1 319 ? 5.725   44.612  -34.914 1.00 19.88 ? 319  LEU B N   1 
ATOM   5186 C  CA  . LEU B 1 319 ? 6.818   43.709  -35.269 1.00 19.25 ? 319  LEU B CA  1 
ATOM   5187 C  C   . LEU B 1 319 ? 7.286   43.934  -36.687 1.00 19.66 ? 319  LEU B C   1 
ATOM   5188 O  O   . LEU B 1 319 ? 8.504   43.879  -36.967 1.00 18.92 ? 319  LEU B O   1 
ATOM   5189 C  CB  . LEU B 1 319 ? 6.385   42.247  -35.127 1.00 19.25 ? 319  LEU B CB  1 
ATOM   5190 C  CG  . LEU B 1 319 ? 7.462   41.175  -35.331 1.00 19.03 ? 319  LEU B CG  1 
ATOM   5191 C  CD1 . LEU B 1 319 ? 8.494   41.207  -34.215 1.00 18.76 ? 319  LEU B CD1 1 
ATOM   5192 C  CD2 . LEU B 1 319 ? 6.810   39.798  -35.418 1.00 19.40 ? 319  LEU B CD2 1 
ATOM   5193 N  N   . SER B 1 320 ? 6.325   44.153  -37.587 1.00 19.40 ? 320  SER B N   1 
ATOM   5194 C  CA  . SER B 1 320 ? 6.628   44.279  -39.012 1.00 19.87 ? 320  SER B CA  1 
ATOM   5195 C  C   . SER B 1 320 ? 7.199   45.657  -39.377 1.00 20.15 ? 320  SER B C   1 
ATOM   5196 O  O   . SER B 1 320 ? 7.612   45.861  -40.514 1.00 20.07 ? 320  SER B O   1 
ATOM   5197 C  CB  . SER B 1 320 ? 5.387   43.951  -39.875 1.00 20.58 ? 320  SER B CB  1 
ATOM   5198 O  OG  . SER B 1 320 ? 4.427   44.983  -39.772 1.00 21.55 ? 320  SER B OG  1 
ATOM   5199 N  N   . HIS B 1 321 ? 7.240   46.610  -38.443 1.00 20.04 ? 321  HIS B N   1 
ATOM   5200 C  CA  . HIS B 1 321 ? 7.931   47.884  -38.724 1.00 20.09 ? 321  HIS B CA  1 
ATOM   5201 C  C   . HIS B 1 321 ? 9.451   47.824  -38.456 1.00 19.46 ? 321  HIS B C   1 
ATOM   5202 O  O   . HIS B 1 321 ? 10.174  48.727  -38.839 1.00 18.24 ? 321  HIS B O   1 
ATOM   5203 C  CB  . HIS B 1 321 ? 7.271   49.054  -37.980 1.00 21.40 ? 321  HIS B CB  1 
ATOM   5204 C  CG  . HIS B 1 321 ? 5.886   49.366  -38.463 1.00 22.82 ? 321  HIS B CG  1 
ATOM   5205 N  ND1 . HIS B 1 321 ? 5.110   50.368  -37.912 1.00 23.66 ? 321  HIS B ND1 1 
ATOM   5206 C  CD2 . HIS B 1 321 ? 5.132   48.797  -39.438 1.00 22.94 ? 321  HIS B CD2 1 
ATOM   5207 C  CE1 . HIS B 1 321 ? 3.944   50.409  -38.539 1.00 23.93 ? 321  HIS B CE1 1 
ATOM   5208 N  NE2 . HIS B 1 321 ? 3.930   49.464  -39.465 1.00 23.70 ? 321  HIS B NE2 1 
ATOM   5209 N  N   . TRP B 1 322 ? 9.940   46.758  -37.816 1.00 18.65 ? 322  TRP B N   1 
ATOM   5210 C  CA  . TRP B 1 322 ? 11.378  46.590  -37.633 1.00 18.17 ? 322  TRP B CA  1 
ATOM   5211 C  C   . TRP B 1 322 ? 12.060  46.344  -38.986 1.00 18.95 ? 322  TRP B C   1 
ATOM   5212 O  O   . TRP B 1 322 ? 11.546  45.592  -39.804 1.00 17.20 ? 322  TRP B O   1 
ATOM   5213 C  CB  . TRP B 1 322 ? 11.665  45.445  -36.655 1.00 17.89 ? 322  TRP B CB  1 
ATOM   5214 C  CG  . TRP B 1 322 ? 11.379  45.846  -35.261 1.00 18.11 ? 322  TRP B CG  1 
ATOM   5215 C  CD1 . TRP B 1 322 ? 10.204  45.713  -34.592 1.00 18.43 ? 322  TRP B CD1 1 
ATOM   5216 C  CD2 . TRP B 1 322 ? 12.270  46.533  -34.386 1.00 18.90 ? 322  TRP B CD2 1 
ATOM   5217 N  NE1 . TRP B 1 322 ? 10.319  46.248  -33.321 1.00 19.15 ? 322  TRP B NE1 1 
ATOM   5218 C  CE2 . TRP B 1 322 ? 11.585  46.753  -33.175 1.00 19.40 ? 322  TRP B CE2 1 
ATOM   5219 C  CE3 . TRP B 1 322 ? 13.604  46.947  -34.491 1.00 19.46 ? 322  TRP B CE3 1 
ATOM   5220 C  CZ2 . TRP B 1 322 ? 12.182  47.381  -32.086 1.00 18.88 ? 322  TRP B CZ2 1 
ATOM   5221 C  CZ3 . TRP B 1 322 ? 14.193  47.580  -33.402 1.00 19.37 ? 322  TRP B CZ3 1 
ATOM   5222 C  CH2 . TRP B 1 322 ? 13.482  47.778  -32.216 1.00 19.19 ? 322  TRP B CH2 1 
ATOM   5223 N  N   . LYS B 1 323 ? 13.199  47.000  -39.206 1.00 19.32 ? 323  LYS B N   1 
ATOM   5224 C  CA  . LYS B 1 323 ? 13.989  46.818  -40.415 1.00 20.80 ? 323  LYS B CA  1 
ATOM   5225 C  C   . LYS B 1 323 ? 15.399  46.357  -40.052 1.00 18.97 ? 323  LYS B C   1 
ATOM   5226 O  O   . LYS B 1 323 ? 15.965  46.773  -39.042 1.00 18.12 ? 323  LYS B O   1 
ATOM   5227 C  CB  . LYS B 1 323 ? 14.022  48.124  -41.224 1.00 23.92 ? 323  LYS B CB  1 
ATOM   5228 C  CG  . LYS B 1 323 ? 12.740  48.369  -41.999 1.00 27.44 ? 323  LYS B CG  1 
ATOM   5229 C  CD  . LYS B 1 323 ? 12.768  49.680  -42.774 1.00 32.25 ? 323  LYS B CD  1 
ATOM   5230 C  CE  . LYS B 1 323 ? 12.405  50.843  -41.872 1.00 36.24 ? 323  LYS B CE  1 
ATOM   5231 N  NZ  . LYS B 1 323 ? 12.405  52.150  -42.592 1.00 40.03 ? 323  LYS B NZ  1 
ATOM   5232 N  N   . ASN B 1 324 ? 15.943  45.466  -40.869 1.00 18.23 ? 324  ASN B N   1 
ATOM   5233 C  CA  . ASN B 1 324 ? 17.253  44.868  -40.628 1.00 17.59 ? 324  ASN B CA  1 
ATOM   5234 C  C   . ASN B 1 324 ? 18.314  45.636  -41.413 1.00 17.19 ? 324  ASN B C   1 
ATOM   5235 O  O   . ASN B 1 324 ? 18.262  45.684  -42.625 1.00 16.21 ? 324  ASN B O   1 
ATOM   5236 C  CB  . ASN B 1 324 ? 17.228  43.384  -41.042 1.00 17.49 ? 324  ASN B CB  1 
ATOM   5237 C  CG  . ASN B 1 324 ? 18.361  42.577  -40.425 1.00 17.68 ? 324  ASN B CG  1 
ATOM   5238 O  OD1 . ASN B 1 324 ? 19.490  43.059  -40.292 1.00 15.86 ? 324  ASN B OD1 1 
ATOM   5239 N  ND2 . ASN B 1 324 ? 18.050  41.334  -40.016 1.00 17.58 ? 324  ASN B ND2 1 
ATOM   5240 N  N   . VAL B 1 325 ? 19.260  46.249  -40.714 1.00 17.44 ? 325  VAL B N   1 
ATOM   5241 C  CA  . VAL B 1 325 ? 20.335  47.002  -41.362 1.00 17.76 ? 325  VAL B CA  1 
ATOM   5242 C  C   . VAL B 1 325 ? 21.297  45.996  -41.985 1.00 18.20 ? 325  VAL B C   1 
ATOM   5243 O  O   . VAL B 1 325 ? 21.969  46.297  -42.961 1.00 18.05 ? 325  VAL B O   1 
ATOM   5244 C  CB  . VAL B 1 325 ? 21.109  47.875  -40.345 1.00 18.25 ? 325  VAL B CB  1 
ATOM   5245 C  CG1 . VAL B 1 325 ? 22.285  48.584  -41.001 1.00 18.28 ? 325  VAL B CG1 1 
ATOM   5246 C  CG2 . VAL B 1 325 ? 20.169  48.874  -39.674 1.00 18.10 ? 325  VAL B CG2 1 
ATOM   5247 N  N   . GLY B 1 326 ? 21.355  44.804  -41.394 1.00 17.72 ? 326  GLY B N   1 
ATOM   5248 C  CA  . GLY B 1 326 ? 22.158  43.692  -41.908 1.00 17.88 ? 326  GLY B CA  1 
ATOM   5249 C  C   . GLY B 1 326 ? 23.069  43.187  -40.800 1.00 17.84 ? 326  GLY B C   1 
ATOM   5250 O  O   . GLY B 1 326 ? 22.962  43.635  -39.655 1.00 17.21 ? 326  GLY B O   1 
ATOM   5251 N  N   . PRO B 1 327 ? 23.986  42.274  -41.139 1.00 18.22 ? 327  PRO B N   1 
ATOM   5252 C  CA  . PRO B 1 327 ? 24.947  41.771  -40.178 1.00 18.57 ? 327  PRO B CA  1 
ATOM   5253 C  C   . PRO B 1 327 ? 26.026  42.811  -39.837 1.00 18.69 ? 327  PRO B C   1 
ATOM   5254 O  O   . PRO B 1 327 ? 26.589  43.435  -40.732 1.00 18.93 ? 327  PRO B O   1 
ATOM   5255 C  CB  . PRO B 1 327 ? 25.520  40.536  -40.882 1.00 19.09 ? 327  PRO B CB  1 
ATOM   5256 C  CG  . PRO B 1 327 ? 25.405  40.863  -42.327 1.00 19.19 ? 327  PRO B CG  1 
ATOM   5257 C  CD  . PRO B 1 327 ? 24.126  41.623  -42.455 1.00 18.65 ? 327  PRO B CD  1 
ATOM   5258 N  N   . ILE B 1 328 ? 26.287  42.999  -38.543 1.00 18.74 ? 328  ILE B N   1 
ATOM   5259 C  CA  . ILE B 1 328 ? 27.221  44.015  -38.067 1.00 19.39 ? 328  ILE B CA  1 
ATOM   5260 C  C   . ILE B 1 328 ? 28.650  43.822  -38.598 1.00 19.52 ? 328  ILE B C   1 
ATOM   5261 O  O   . ILE B 1 328 ? 29.317  44.793  -38.951 1.00 17.17 ? 328  ILE B O   1 
ATOM   5262 C  CB  . ILE B 1 328 ? 27.225  44.084  -36.521 1.00 20.14 ? 328  ILE B CB  1 
ATOM   5263 C  CG1 . ILE B 1 328 ? 25.890  44.651  -36.026 1.00 20.33 ? 328  ILE B CG1 1 
ATOM   5264 C  CG2 . ILE B 1 328 ? 28.387  44.928  -36.002 1.00 20.42 ? 328  ILE B CG2 1 
ATOM   5265 C  CD1 . ILE B 1 328 ? 25.569  44.301  -34.587 1.00 20.52 ? 328  ILE B CD1 1 
ATOM   5266 N  N   . PHE B 1 329 ? 29.111  42.575  -38.662 1.00 20.32 ? 329  PHE B N   1 
ATOM   5267 C  CA  . PHE B 1 329 ? 30.456  42.290  -39.133 1.00 20.33 ? 329  PHE B CA  1 
ATOM   5268 C  C   . PHE B 1 329 ? 30.459  41.816  -40.589 1.00 21.43 ? 329  PHE B C   1 
ATOM   5269 O  O   . PHE B 1 329 ? 31.403  41.153  -41.026 1.00 22.62 ? 329  PHE B O   1 
ATOM   5270 C  CB  . PHE B 1 329 ? 31.144  41.286  -38.192 1.00 20.59 ? 329  PHE B CB  1 
ATOM   5271 C  CG  . PHE B 1 329 ? 31.431  41.861  -36.835 1.00 20.21 ? 329  PHE B CG  1 
ATOM   5272 C  CD1 . PHE B 1 329 ? 32.563  42.652  -36.631 1.00 19.77 ? 329  PHE B CD1 1 
ATOM   5273 C  CD2 . PHE B 1 329 ? 30.556  41.664  -35.785 1.00 19.46 ? 329  PHE B CD2 1 
ATOM   5274 C  CE1 . PHE B 1 329 ? 32.814  43.218  -35.407 1.00 20.10 ? 329  PHE B CE1 1 
ATOM   5275 C  CE2 . PHE B 1 329 ? 30.803  42.227  -34.542 1.00 19.94 ? 329  PHE B CE2 1 
ATOM   5276 C  CZ  . PHE B 1 329 ? 31.939  42.999  -34.352 1.00 20.13 ? 329  PHE B CZ  1 
ATOM   5277 N  N   . GLY B 1 330 ? 29.398  42.150  -41.327 1.00 21.26 ? 330  GLY B N   1 
ATOM   5278 C  CA  . GLY B 1 330 ? 29.398  42.055  -42.782 1.00 21.44 ? 330  GLY B CA  1 
ATOM   5279 C  C   . GLY B 1 330 ? 28.889  40.752  -43.372 1.00 21.79 ? 330  GLY B C   1 
ATOM   5280 O  O   . GLY B 1 330 ? 28.624  39.765  -42.666 1.00 19.73 ? 330  GLY B O   1 
ATOM   5281 N  N   . TYR B 1 331 ? 28.740  40.791  -44.695 1.00 21.80 ? 331  TYR B N   1 
ATOM   5282 C  CA  . TYR B 1 331 ? 28.365  39.651  -45.491 1.00 22.66 ? 331  TYR B CA  1 
ATOM   5283 C  C   . TYR B 1 331 ? 29.613  38.824  -45.769 1.00 23.65 ? 331  TYR B C   1 
ATOM   5284 O  O   . TYR B 1 331 ? 30.721  39.213  -45.384 1.00 20.64 ? 331  TYR B O   1 
ATOM   5285 C  CB  . TYR B 1 331 ? 27.685  40.138  -46.776 1.00 22.92 ? 331  TYR B CB  1 
ATOM   5286 C  CG  . TYR B 1 331 ? 26.349  40.800  -46.461 1.00 23.13 ? 331  TYR B CG  1 
ATOM   5287 C  CD1 . TYR B 1 331 ? 25.274  40.039  -45.995 1.00 23.67 ? 331  TYR B CD1 1 
ATOM   5288 C  CD2 . TYR B 1 331 ? 26.178  42.187  -46.560 1.00 23.61 ? 331  TYR B CD2 1 
ATOM   5289 C  CE1 . TYR B 1 331 ? 24.065  40.635  -45.672 1.00 23.19 ? 331  TYR B CE1 1 
ATOM   5290 C  CE2 . TYR B 1 331 ? 24.969  42.787  -46.242 1.00 23.26 ? 331  TYR B CE2 1 
ATOM   5291 C  CZ  . TYR B 1 331 ? 23.916  42.005  -45.803 1.00 23.95 ? 331  TYR B CZ  1 
ATOM   5292 O  OH  . TYR B 1 331 ? 22.711  42.578  -45.467 1.00 22.95 ? 331  TYR B OH  1 
ATOM   5293 N  N   . ASN B 1 332 ? 29.430  37.677  -46.415 1.00 23.87 ? 332  ASN B N   1 
ATOM   5294 C  CA  . ASN B 1 332 ? 30.547  36.774  -46.723 1.00 24.14 ? 332  ASN B CA  1 
ATOM   5295 C  C   . ASN B 1 332 ? 31.330  36.337  -45.501 1.00 23.38 ? 332  ASN B C   1 
ATOM   5296 O  O   . ASN B 1 332 ? 32.534  36.147  -45.579 1.00 21.96 ? 332  ASN B O   1 
ATOM   5297 C  CB  . ASN B 1 332 ? 31.510  37.427  -47.713 1.00 25.19 ? 332  ASN B CB  1 
ATOM   5298 C  CG  . ASN B 1 332 ? 30.830  37.819  -48.999 1.00 27.02 ? 332  ASN B CG  1 
ATOM   5299 O  OD1 . ASN B 1 332 ? 30.471  36.963  -49.802 1.00 29.39 ? 332  ASN B OD1 1 
ATOM   5300 N  ND2 . ASN B 1 332 ? 30.662  39.111  -49.211 1.00 26.93 ? 332  ASN B ND2 1 
ATOM   5301 N  N   . SER B 1 333 ? 30.660  36.186  -44.366 1.00 23.79 ? 333  SER B N   1 
ATOM   5302 C  CA  . SER B 1 333 ? 31.353  35.774  -43.145 1.00 24.09 ? 333  SER B CA  1 
ATOM   5303 C  C   . SER B 1 333 ? 31.380  34.242  -43.137 1.00 23.41 ? 333  SER B C   1 
ATOM   5304 O  O   . SER B 1 333 ? 30.880  33.615  -44.073 1.00 23.01 ? 333  SER B O   1 
ATOM   5305 C  CB  . SER B 1 333 ? 30.669  36.356  -41.910 1.00 24.63 ? 333  SER B CB  1 
ATOM   5306 O  OG  . SER B 1 333 ? 29.423  35.726  -41.692 1.00 27.96 ? 333  SER B OG  1 
ATOM   5307 N  N   . THR B 1 334 ? 31.991  33.648  -42.114 1.00 21.70 ? 334  THR B N   1 
ATOM   5308 C  CA  . THR B 1 334 ? 32.152  32.196  -42.020 1.00 21.42 ? 334  THR B CA  1 
ATOM   5309 C  C   . THR B 1 334 ? 31.732  31.682  -40.657 1.00 19.93 ? 334  THR B C   1 
ATOM   5310 O  O   . THR B 1 334 ? 31.601  32.439  -39.693 1.00 19.21 ? 334  THR B O   1 
ATOM   5311 C  CB  . THR B 1 334 ? 33.621  31.736  -42.253 1.00 22.35 ? 334  THR B CB  1 
ATOM   5312 O  OG1 . THR B 1 334 ? 34.422  32.026  -41.100 1.00 24.21 ? 334  THR B OG1 1 
ATOM   5313 C  CG2 . THR B 1 334 ? 34.238  32.440  -43.445 1.00 23.74 ? 334  THR B CG2 1 
ATOM   5314 N  N   . ALA B 1 335 ? 31.548  30.370  -40.592 1.00 19.00 ? 335  ALA B N   1 
ATOM   5315 C  CA  . ALA B 1 335 ? 31.226  29.681  -39.352 1.00 19.01 ? 335  ALA B CA  1 
ATOM   5316 C  C   . ALA B 1 335 ? 32.426  29.558  -38.449 1.00 19.99 ? 335  ALA B C   1 
ATOM   5317 O  O   . ALA B 1 335 ? 32.285  29.188  -37.272 1.00 20.11 ? 335  ALA B O   1 
ATOM   5318 C  CB  . ALA B 1 335 ? 30.667  28.294  -39.658 1.00 18.82 ? 335  ALA B CB  1 
ATOM   5319 N  N   . VAL B 1 336 ? 33.616  29.864  -38.974 1.00 20.04 ? 336  VAL B N   1 
ATOM   5320 C  CA  . VAL B 1 336 ? 34.813  29.758  -38.173 1.00 20.06 ? 336  VAL B CA  1 
ATOM   5321 C  C   . VAL B 1 336 ? 34.907  30.907  -37.169 1.00 19.63 ? 336  VAL B C   1 
ATOM   5322 O  O   . VAL B 1 336 ? 35.479  30.742  -36.104 1.00 19.76 ? 336  VAL B O   1 
ATOM   5323 C  CB  . VAL B 1 336 ? 36.083  29.659  -39.045 1.00 20.34 ? 336  VAL B CB  1 
ATOM   5324 C  CG1 . VAL B 1 336 ? 37.298  29.361  -38.175 1.00 20.27 ? 336  VAL B CG1 1 
ATOM   5325 C  CG2 . VAL B 1 336 ? 35.910  28.558  -40.094 1.00 20.66 ? 336  VAL B CG2 1 
ATOM   5326 N  N   . SER B 1 337 ? 34.353  32.066  -37.518 1.00 18.96 ? 337  SER B N   1 
ATOM   5327 C  CA  . SER B 1 337 ? 34.394  33.231  -36.644 1.00 18.58 ? 337  SER B CA  1 
ATOM   5328 C  C   . SER B 1 337 ? 32.979  33.753  -36.465 1.00 17.25 ? 337  SER B C   1 
ATOM   5329 O  O   . SER B 1 337 ? 32.370  34.228  -37.416 1.00 16.50 ? 337  SER B O   1 
ATOM   5330 C  CB  . SER B 1 337 ? 35.306  34.328  -37.209 1.00 19.01 ? 337  SER B CB  1 
ATOM   5331 O  OG  . SER B 1 337 ? 35.524  35.330  -36.224 1.00 18.96 ? 337  SER B OG  1 
ATOM   5332 N  N   . GLN B 1 338 ? 32.462  33.650  -35.242 1.00 15.48 ? 338  GLN B N   1 
ATOM   5333 C  CA  . GLN B 1 338 ? 31.031  33.813  -35.002 1.00 15.24 ? 338  GLN B CA  1 
ATOM   5334 C  C   . GLN B 1 338 ? 30.805  34.880  -33.964 1.00 15.25 ? 338  GLN B C   1 
ATOM   5335 O  O   . GLN B 1 338 ? 31.695  35.209  -33.193 1.00 15.33 ? 338  GLN B O   1 
ATOM   5336 C  CB  . GLN B 1 338 ? 30.420  32.499  -34.486 1.00 15.00 ? 338  GLN B CB  1 
ATOM   5337 C  CG  . GLN B 1 338 ? 30.539  31.296  -35.405 1.00 14.79 ? 338  GLN B CG  1 
ATOM   5338 C  CD  . GLN B 1 338 ? 29.975  29.998  -34.775 1.00 15.28 ? 338  GLN B CD  1 
ATOM   5339 O  OE1 . GLN B 1 338 ? 29.162  30.025  -33.828 1.00 13.42 ? 338  GLN B OE1 1 
ATOM   5340 N  NE2 . GLN B 1 338 ? 30.417  28.846  -35.311 1.00 15.11 ? 338  GLN B NE2 1 
ATOM   5341 N  N   . GLU B 1 339 ? 29.600  35.418  -33.922 1.00 15.62 ? 339  GLU B N   1 
ATOM   5342 C  CA  . GLU B 1 339 ? 29.233  36.329  -32.841 1.00 15.60 ? 339  GLU B CA  1 
ATOM   5343 C  C   . GLU B 1 339 ? 28.042  35.792  -32.058 1.00 15.26 ? 339  GLU B C   1 
ATOM   5344 O  O   . GLU B 1 339 ? 27.005  35.489  -32.644 1.00 14.21 ? 339  GLU B O   1 
ATOM   5345 C  CB  . GLU B 1 339 ? 28.858  37.709  -33.391 1.00 15.97 ? 339  GLU B CB  1 
ATOM   5346 C  CG  . GLU B 1 339 ? 29.917  38.368  -34.236 1.00 16.33 ? 339  GLU B CG  1 
ATOM   5347 C  CD  . GLU B 1 339 ? 29.769  38.083  -35.709 1.00 16.86 ? 339  GLU B CD  1 
ATOM   5348 O  OE1 . GLU B 1 339 ? 28.624  38.078  -36.232 1.00 17.46 ? 339  GLU B OE1 1 
ATOM   5349 O  OE2 . GLU B 1 339 ? 30.822  37.893  -36.352 1.00 18.39 ? 339  GLU B OE2 1 
ATOM   5350 N  N   . TRP B 1 340 ? 28.190  35.702  -30.741 1.00 15.59 ? 340  TRP B N   1 
ATOM   5351 C  CA  . TRP B 1 340 ? 27.067  35.400  -29.852 1.00 15.72 ? 340  TRP B CA  1 
ATOM   5352 C  C   . TRP B 1 340 ? 26.783  36.613  -28.938 1.00 16.34 ? 340  TRP B C   1 
ATOM   5353 O  O   . TRP B 1 340 ? 27.310  37.717  -29.158 1.00 15.42 ? 340  TRP B O   1 
ATOM   5354 C  CB  . TRP B 1 340 ? 27.312  34.133  -28.997 1.00 15.93 ? 340  TRP B CB  1 
ATOM   5355 C  CG  . TRP B 1 340 ? 27.757  32.872  -29.702 1.00 15.38 ? 340  TRP B CG  1 
ATOM   5356 C  CD1 . TRP B 1 340 ? 27.928  32.663  -31.047 1.00 15.57 ? 340  TRP B CD1 1 
ATOM   5357 C  CD2 . TRP B 1 340 ? 28.018  31.618  -29.069 1.00 15.39 ? 340  TRP B CD2 1 
ATOM   5358 N  NE1 . TRP B 1 340 ? 28.338  31.359  -31.279 1.00 15.65 ? 340  TRP B NE1 1 
ATOM   5359 C  CE2 . TRP B 1 340 ? 28.399  30.702  -30.077 1.00 15.82 ? 340  TRP B CE2 1 
ATOM   5360 C  CE3 . TRP B 1 340 ? 28.008  31.191  -27.738 1.00 15.62 ? 340  TRP B CE3 1 
ATOM   5361 C  CZ2 . TRP B 1 340 ? 28.738  29.370  -29.790 1.00 15.89 ? 340  TRP B CZ2 1 
ATOM   5362 C  CZ3 . TRP B 1 340 ? 28.356  29.873  -27.455 1.00 15.93 ? 340  TRP B CZ3 1 
ATOM   5363 C  CH2 . TRP B 1 340 ? 28.704  28.981  -28.475 1.00 15.69 ? 340  TRP B CH2 1 
ATOM   5364 N  N   . SER B 1 341 ? 25.957  36.405  -27.909 1.00 16.77 ? 341  SER B N   1 
ATOM   5365 C  CA  . SER B 1 341 ? 25.251  37.500  -27.284 1.00 17.85 ? 341  SER B CA  1 
ATOM   5366 C  C   . SER B 1 341 ? 26.103  38.449  -26.454 1.00 17.20 ? 341  SER B C   1 
ATOM   5367 O  O   . SER B 1 341 ? 27.189  38.129  -26.026 1.00 17.46 ? 341  SER B O   1 
ATOM   5368 C  CB  . SER B 1 341 ? 24.106  36.960  -26.419 1.00 18.74 ? 341  SER B CB  1 
ATOM   5369 O  OG  . SER B 1 341 ? 23.305  36.082  -27.185 1.00 20.62 ? 341  SER B OG  1 
ATOM   5370 N  N   . GLY B 1 342 ? 25.551  39.629  -26.225 1.00 17.97 ? 342  GLY B N   1 
ATOM   5371 C  CA  . GLY B 1 342 ? 26.171  40.628  -25.382 1.00 17.84 ? 342  GLY B CA  1 
ATOM   5372 C  C   . GLY B 1 342 ? 25.200  41.725  -25.005 1.00 17.61 ? 342  GLY B C   1 
ATOM   5373 O  O   . GLY B 1 342 ? 24.111  41.445  -24.530 1.00 17.18 ? 342  GLY B O   1 
ATOM   5374 N  N   . SER B 1 343 ? 25.619  42.976  -25.197 1.00 16.73 ? 343  SER B N   1 
ATOM   5375 C  CA  . SER B 1 343 ? 24.805  44.124  -24.877 1.00 16.35 ? 343  SER B CA  1 
ATOM   5376 C  C   . SER B 1 343 ? 25.300  45.314  -25.702 1.00 16.76 ? 343  SER B C   1 
ATOM   5377 O  O   . SER B 1 343 ? 26.308  45.207  -26.427 1.00 16.35 ? 343  SER B O   1 
ATOM   5378 C  CB  . SER B 1 343 ? 24.866  44.418  -23.381 1.00 16.70 ? 343  SER B CB  1 
ATOM   5379 O  OG  . SER B 1 343 ? 26.206  44.544  -22.917 1.00 16.27 ? 343  SER B OG  1 
ATOM   5380 N  N   . ALA B 1 344 ? 24.598  46.437  -25.602 1.00 15.98 ? 344  ALA B N   1 
ATOM   5381 C  CA  . ALA B 1 344 ? 24.978  47.625  -26.333 1.00 16.81 ? 344  ALA B CA  1 
ATOM   5382 C  C   . ALA B 1 344 ? 24.388  48.866  -25.692 1.00 17.59 ? 344  ALA B C   1 
ATOM   5383 O  O   . ALA B 1 344 ? 23.243  48.866  -25.267 1.00 18.48 ? 344  ALA B O   1 
ATOM   5384 C  CB  . ALA B 1 344 ? 24.543  47.522  -27.780 1.00 17.25 ? 344  ALA B CB  1 
ATOM   5385 N  N   . VAL B 1 345 ? 25.194  49.913  -25.608 1.00 17.98 ? 345  VAL B N   1 
ATOM   5386 C  CA  . VAL B 1 345 ? 24.765  51.164  -25.025 1.00 18.61 ? 345  VAL B CA  1 
ATOM   5387 C  C   . VAL B 1 345 ? 25.188  52.326  -25.904 1.00 18.97 ? 345  VAL B C   1 
ATOM   5388 O  O   . VAL B 1 345 ? 25.948  52.142  -26.850 1.00 18.09 ? 345  VAL B O   1 
ATOM   5389 C  CB  . VAL B 1 345 ? 25.350  51.361  -23.611 1.00 19.43 ? 345  VAL B CB  1 
ATOM   5390 C  CG1 . VAL B 1 345 ? 24.781  50.323  -22.663 1.00 19.07 ? 345  VAL B CG1 1 
ATOM   5391 C  CG2 . VAL B 1 345 ? 26.883  51.309  -23.628 1.00 19.68 ? 345  VAL B CG2 1 
ATOM   5392 N  N   . LEU B 1 346 ? 24.666  53.513  -25.607 1.00 20.25 ? 346  LEU B N   1 
ATOM   5393 C  CA  . LEU B 1 346 ? 25.145  54.732  -26.253 1.00 21.44 ? 346  LEU B CA  1 
ATOM   5394 C  C   . LEU B 1 346 ? 26.382  55.239  -25.544 1.00 21.39 ? 346  LEU B C   1 
ATOM   5395 O  O   . LEU B 1 346 ? 26.463  55.191  -24.320 1.00 22.23 ? 346  LEU B O   1 
ATOM   5396 C  CB  . LEU B 1 346 ? 24.066  55.830  -26.271 1.00 22.15 ? 346  LEU B CB  1 
ATOM   5397 C  CG  . LEU B 1 346 ? 22.839  55.511  -27.125 1.00 22.95 ? 346  LEU B CG  1 
ATOM   5398 C  CD1 . LEU B 1 346 ? 21.897  56.704  -27.199 1.00 23.97 ? 346  LEU B CD1 1 
ATOM   5399 C  CD2 . LEU B 1 346 ? 23.239  55.079  -28.521 1.00 23.16 ? 346  LEU B CD2 1 
ATOM   5400 N  N   . ASN B 1 347 ? 27.342  55.717  -26.329 1.00 21.11 ? 347  ASN B N   1 
ATOM   5401 C  CA  . ASN B 1 347 ? 28.431  56.540  -25.825 1.00 21.16 ? 347  ASN B CA  1 
ATOM   5402 C  C   . ASN B 1 347 ? 28.023  58.027  -25.796 1.00 22.50 ? 347  ASN B C   1 
ATOM   5403 O  O   . ASN B 1 347 ? 26.971  58.403  -26.333 1.00 22.80 ? 347  ASN B O   1 
ATOM   5404 C  CB  . ASN B 1 347 ? 29.667  56.353  -26.715 1.00 20.69 ? 347  ASN B CB  1 
ATOM   5405 C  CG  . ASN B 1 347 ? 30.253  54.949  -26.622 1.00 19.62 ? 347  ASN B CG  1 
ATOM   5406 O  OD1 . ASN B 1 347 ? 30.338  54.391  -25.546 1.00 19.86 ? 347  ASN B OD1 1 
ATOM   5407 N  ND2 . ASN B 1 347 ? 30.661  54.382  -27.757 1.00 18.90 ? 347  ASN B ND2 1 
ATOM   5408 N  N   . SER B 1 348 ? 28.851  58.855  -25.157 1.00 23.88 ? 348  SER B N   1 
ATOM   5409 C  CA  . SER B 1 348 ? 28.609  60.307  -25.008 1.00 25.67 ? 348  SER B CA  1 
ATOM   5410 C  C   . SER B 1 348 ? 28.232  61.014  -26.289 1.00 24.20 ? 348  SER B C   1 
ATOM   5411 O  O   . SER B 1 348 ? 27.368  61.870  -26.276 1.00 24.78 ? 348  SER B O   1 
ATOM   5412 C  CB  . SER B 1 348 ? 29.858  61.007  -24.458 1.00 27.63 ? 348  SER B CB  1 
ATOM   5413 O  OG  . SER B 1 348 ? 29.976  60.777  -23.064 1.00 34.90 ? 348  SER B OG  1 
ATOM   5414 N  N   . ASP B 1 349 ? 28.901  60.643  -27.379 1.00 23.54 ? 349  ASP B N   1 
ATOM   5415 C  CA  . ASP B 1 349 ? 28.725  61.255  -28.692 1.00 22.59 ? 349  ASP B CA  1 
ATOM   5416 C  C   . ASP B 1 349 ? 27.664  60.565  -29.549 1.00 22.50 ? 349  ASP B C   1 
ATOM   5417 O  O   . ASP B 1 349 ? 27.601  60.794  -30.755 1.00 20.32 ? 349  ASP B O   1 
ATOM   5418 C  CB  . ASP B 1 349 ? 30.055  61.227  -29.451 1.00 22.40 ? 349  ASP B CB  1 
ATOM   5419 C  CG  . ASP B 1 349 ? 30.451  59.819  -29.889 1.00 22.13 ? 349  ASP B CG  1 
ATOM   5420 O  OD1 . ASP B 1 349 ? 29.995  58.847  -29.263 1.00 20.54 ? 349  ASP B OD1 1 
ATOM   5421 O  OD2 . ASP B 1 349 ? 31.226  59.679  -30.857 1.00 22.69 ? 349  ASP B OD2 1 
ATOM   5422 N  N   . ASN B 1 350 ? 26.853  59.700  -28.940 1.00 23.51 ? 350  ASN B N   1 
ATOM   5423 C  CA  . ASN B 1 350 ? 25.826  58.945  -29.668 1.00 24.60 ? 350  ASN B CA  1 
ATOM   5424 C  C   . ASN B 1 350 ? 26.290  57.850  -30.629 1.00 22.91 ? 350  ASN B C   1 
ATOM   5425 O  O   . ASN B 1 350 ? 25.482  57.352  -31.411 1.00 20.93 ? 350  ASN B O   1 
ATOM   5426 C  CB  . ASN B 1 350 ? 24.865  59.887  -30.410 1.00 27.85 ? 350  ASN B CB  1 
ATOM   5427 C  CG  . ASN B 1 350 ? 23.693  60.279  -29.562 1.00 31.75 ? 350  ASN B CG  1 
ATOM   5428 O  OD1 . ASN B 1 350 ? 23.795  60.352  -28.329 1.00 34.59 ? 350  ASN B OD1 1 
ATOM   5429 N  ND2 . ASN B 1 350 ? 22.560  60.528  -30.209 1.00 34.31 ? 350  ASN B ND2 1 
ATOM   5430 N  N   . SER B 1 351 ? 27.560  57.467  -30.580 1.00 21.86 ? 351  SER B N   1 
ATOM   5431 C  CA  . SER B 1 351 ? 27.955  56.203  -31.171 1.00 21.69 ? 351  SER B CA  1 
ATOM   5432 C  C   . SER B 1 351 ? 27.453  55.093  -30.228 1.00 21.64 ? 351  SER B C   1 
ATOM   5433 O  O   . SER B 1 351 ? 27.071  55.365  -29.082 1.00 20.59 ? 351  SER B O   1 
ATOM   5434 C  CB  . SER B 1 351 ? 29.476  56.121  -31.377 1.00 22.67 ? 351  SER B CB  1 
ATOM   5435 O  OG  . SER B 1 351 ? 30.226  56.234  -30.167 1.00 22.81 ? 351  SER B OG  1 
ATOM   5436 N  N   . ILE B 1 352 ? 27.444  53.860  -30.725 1.00 20.47 ? 352  ILE B N   1 
ATOM   5437 C  CA  . ILE B 1 352 ? 27.033  52.708  -29.945 1.00 20.54 ? 352  ILE B CA  1 
ATOM   5438 C  C   . ILE B 1 352 ? 28.290  51.902  -29.567 1.00 19.73 ? 352  ILE B C   1 
ATOM   5439 O  O   . ILE B 1 352 ? 29.122  51.607  -30.416 1.00 19.09 ? 352  ILE B O   1 
ATOM   5440 C  CB  . ILE B 1 352 ? 26.051  51.819  -30.736 1.00 21.36 ? 352  ILE B CB  1 
ATOM   5441 C  CG1 . ILE B 1 352 ? 24.692  52.506  -30.906 1.00 23.49 ? 352  ILE B CG1 1 
ATOM   5442 C  CG2 . ILE B 1 352 ? 25.839  50.477  -30.045 1.00 21.66 ? 352  ILE B CG2 1 
ATOM   5443 C  CD1 . ILE B 1 352 ? 24.689  53.753  -31.769 1.00 23.59 ? 352  ILE B CD1 1 
ATOM   5444 N  N   . GLN B 1 353 ? 28.428  51.563  -28.291 1.00 18.75 ? 353  GLN B N   1 
ATOM   5445 C  CA  . GLN B 1 353 ? 29.453  50.637  -27.866 1.00 17.98 ? 353  GLN B CA  1 
ATOM   5446 C  C   . GLN B 1 353 ? 28.832  49.247  -27.766 1.00 18.02 ? 353  GLN B C   1 
ATOM   5447 O  O   . GLN B 1 353 ? 28.026  48.978  -26.891 1.00 18.91 ? 353  GLN B O   1 
ATOM   5448 C  CB  . GLN B 1 353 ? 30.085  51.087  -26.547 1.00 17.47 ? 353  GLN B CB  1 
ATOM   5449 C  CG  . GLN B 1 353 ? 31.476  50.513  -26.296 1.00 17.39 ? 353  GLN B CG  1 
ATOM   5450 C  CD  . GLN B 1 353 ? 32.441  50.815  -27.426 1.00 17.79 ? 353  GLN B CD  1 
ATOM   5451 O  OE1 . GLN B 1 353 ? 32.341  51.853  -28.080 1.00 17.45 ? 353  GLN B OE1 1 
ATOM   5452 N  NE2 . GLN B 1 353 ? 33.354  49.889  -27.687 1.00 17.39 ? 353  GLN B NE2 1 
ATOM   5453 N  N   . LEU B 1 354 ? 29.190  48.382  -28.704 1.00 17.59 ? 354  LEU B N   1 
ATOM   5454 C  CA  . LEU B 1 354 ? 28.744  47.004  -28.701 1.00 17.16 ? 354  LEU B CA  1 
ATOM   5455 C  C   . LEU B 1 354 ? 29.649  46.138  -27.837 1.00 17.63 ? 354  LEU B C   1 
ATOM   5456 O  O   . LEU B 1 354 ? 30.869  46.195  -27.945 1.00 17.58 ? 354  LEU B O   1 
ATOM   5457 C  CB  . LEU B 1 354 ? 28.753  46.471  -30.129 1.00 17.05 ? 354  LEU B CB  1 
ATOM   5458 C  CG  . LEU B 1 354 ? 28.431  45.000  -30.397 1.00 16.43 ? 354  LEU B CG  1 
ATOM   5459 C  CD1 . LEU B 1 354 ? 26.996  44.641  -30.039 1.00 16.26 ? 354  LEU B CD1 1 
ATOM   5460 C  CD2 . LEU B 1 354 ? 28.737  44.709  -31.862 1.00 16.08 ? 354  LEU B CD2 1 
ATOM   5461 N  N   . PHE B 1 355 ? 29.039  45.350  -26.965 1.00 17.43 ? 355  PHE B N   1 
ATOM   5462 C  CA  . PHE B 1 355 ? 29.719  44.246  -26.306 1.00 17.01 ? 355  PHE B CA  1 
ATOM   5463 C  C   . PHE B 1 355 ? 29.105  42.959  -26.827 1.00 16.36 ? 355  PHE B C   1 
ATOM   5464 O  O   . PHE B 1 355 ? 27.883  42.821  -26.880 1.00 16.25 ? 355  PHE B O   1 
ATOM   5465 C  CB  . PHE B 1 355 ? 29.569  44.353  -24.786 1.00 17.05 ? 355  PHE B CB  1 
ATOM   5466 C  CG  . PHE B 1 355 ? 30.351  45.481  -24.211 1.00 17.49 ? 355  PHE B CG  1 
ATOM   5467 C  CD1 . PHE B 1 355 ? 29.787  46.747  -24.095 1.00 17.87 ? 355  PHE B CD1 1 
ATOM   5468 C  CD2 . PHE B 1 355 ? 31.678  45.305  -23.868 1.00 17.49 ? 355  PHE B CD2 1 
ATOM   5469 C  CE1 . PHE B 1 355 ? 30.535  47.811  -23.611 1.00 17.81 ? 355  PHE B CE1 1 
ATOM   5470 C  CE2 . PHE B 1 355 ? 32.427  46.355  -23.382 1.00 17.94 ? 355  PHE B CE2 1 
ATOM   5471 C  CZ  . PHE B 1 355 ? 31.855  47.613  -23.253 1.00 18.19 ? 355  PHE B CZ  1 
ATOM   5472 N  N   . TYR B 1 356 ? 29.947  42.016  -27.232 1.00 16.20 ? 356  TYR B N   1 
ATOM   5473 C  CA  . TYR B 1 356 ? 29.446  40.770  -27.753 1.00 16.04 ? 356  TYR B CA  1 
ATOM   5474 C  C   . TYR B 1 356 ? 30.426  39.646  -27.477 1.00 16.56 ? 356  TYR B C   1 
ATOM   5475 O  O   . TYR B 1 356 ? 31.475  39.866  -26.852 1.00 16.81 ? 356  TYR B O   1 
ATOM   5476 C  CB  . TYR B 1 356 ? 29.158  40.907  -29.240 1.00 16.08 ? 356  TYR B CB  1 
ATOM   5477 C  CG  . TYR B 1 356 ? 30.403  41.023  -30.079 1.00 16.36 ? 356  TYR B CG  1 
ATOM   5478 C  CD1 . TYR B 1 356 ? 31.140  42.200  -30.117 1.00 16.48 ? 356  TYR B CD1 1 
ATOM   5479 C  CD2 . TYR B 1 356 ? 30.857  39.935  -30.818 1.00 16.24 ? 356  TYR B CD2 1 
ATOM   5480 C  CE1 . TYR B 1 356 ? 32.297  42.290  -30.885 1.00 16.76 ? 356  TYR B CE1 1 
ATOM   5481 C  CE2 . TYR B 1 356 ? 32.006  40.012  -31.572 1.00 16.69 ? 356  TYR B CE2 1 
ATOM   5482 C  CZ  . TYR B 1 356 ? 32.716  41.190  -31.620 1.00 17.01 ? 356  TYR B CZ  1 
ATOM   5483 O  OH  . TYR B 1 356 ? 33.862  41.235  -32.385 1.00 17.53 ? 356  TYR B OH  1 
ATOM   5484 N  N   . THR B 1 357 ? 30.066  38.443  -27.927 1.00 16.19 ? 357  THR B N   1 
ATOM   5485 C  CA  . THR B 1 357 ? 30.935  37.271  -27.766 1.00 15.86 ? 357  THR B CA  1 
ATOM   5486 C  C   . THR B 1 357 ? 31.549  36.868  -29.105 1.00 16.02 ? 357  THR B C   1 
ATOM   5487 O  O   . THR B 1 357 ? 30.841  36.437  -30.004 1.00 16.68 ? 357  THR B O   1 
ATOM   5488 C  CB  . THR B 1 357 ? 30.141  36.084  -27.198 1.00 15.15 ? 357  THR B CB  1 
ATOM   5489 O  OG1 . THR B 1 357 ? 29.382  36.514  -26.059 1.00 14.27 ? 357  THR B OG1 1 
ATOM   5490 C  CG2 . THR B 1 357 ? 31.067  34.940  -26.796 1.00 14.70 ? 357  THR B CG2 1 
ATOM   5491 N  N   . ARG B 1 358 ? 32.866  37.008  -29.235 1.00 15.98 ? 358  ARG B N   1 
ATOM   5492 C  CA  . ARG B 1 358 ? 33.577  36.522  -30.416 1.00 16.10 ? 358  ARG B CA  1 
ATOM   5493 C  C   . ARG B 1 358 ? 33.871  35.052  -30.152 1.00 16.11 ? 358  ARG B C   1 
ATOM   5494 O  O   . ARG B 1 358 ? 34.343  34.703  -29.074 1.00 16.99 ? 358  ARG B O   1 
ATOM   5495 C  CB  . ARG B 1 358 ? 34.866  37.302  -30.652 1.00 15.48 ? 358  ARG B CB  1 
ATOM   5496 C  CG  . ARG B 1 358 ? 35.771  36.765  -31.761 1.00 15.52 ? 358  ARG B CG  1 
ATOM   5497 C  CD  . ARG B 1 358 ? 35.103  36.727  -33.128 1.00 15.41 ? 358  ARG B CD  1 
ATOM   5498 N  NE  . ARG B 1 358 ? 34.642  38.053  -33.533 1.00 15.04 ? 358  ARG B NE  1 
ATOM   5499 C  CZ  . ARG B 1 358 ? 33.811  38.293  -34.541 1.00 14.64 ? 358  ARG B CZ  1 
ATOM   5500 N  NH1 . ARG B 1 358 ? 33.298  37.303  -35.268 1.00 14.30 ? 358  ARG B NH1 1 
ATOM   5501 N  NH2 . ARG B 1 358 ? 33.450  39.543  -34.789 1.00 14.82 ? 358  ARG B NH2 1 
ATOM   5502 N  N   . VAL B 1 359 ? 33.525  34.201  -31.104 1.00 15.73 ? 359  VAL B N   1 
ATOM   5503 C  CA  . VAL B 1 359 ? 33.654  32.764  -30.943 1.00 16.59 ? 359  VAL B CA  1 
ATOM   5504 C  C   . VAL B 1 359 ? 34.433  32.250  -32.150 1.00 17.76 ? 359  VAL B C   1 
ATOM   5505 O  O   . VAL B 1 359 ? 33.986  32.387  -33.291 1.00 18.27 ? 359  VAL B O   1 
ATOM   5506 C  CB  . VAL B 1 359 ? 32.300  32.034  -30.889 1.00 16.67 ? 359  VAL B CB  1 
ATOM   5507 C  CG1 . VAL B 1 359 ? 32.526  30.527  -30.726 1.00 16.77 ? 359  VAL B CG1 1 
ATOM   5508 C  CG2 . VAL B 1 359 ? 31.422  32.590  -29.774 1.00 16.45 ? 359  VAL B CG2 1 
ATOM   5509 N  N   . ASP B 1 360 ? 35.601  31.686  -31.876 1.00 18.14 ? 360  ASP B N   1 
ATOM   5510 C  CA  . ASP B 1 360 ? 36.530  31.228  -32.901 1.00 20.06 ? 360  ASP B CA  1 
ATOM   5511 C  C   . ASP B 1 360 ? 36.491  29.689  -32.837 1.00 18.97 ? 360  ASP B C   1 
ATOM   5512 O  O   . ASP B 1 360 ? 36.716  29.109  -31.785 1.00 17.88 ? 360  ASP B O   1 
ATOM   5513 C  CB  . ASP B 1 360 ? 37.915  31.857  -32.587 1.00 21.92 ? 360  ASP B CB  1 
ATOM   5514 C  CG  . ASP B 1 360 ? 39.105  31.083  -33.152 1.00 24.82 ? 360  ASP B CG  1 
ATOM   5515 O  OD1 . ASP B 1 360 ? 39.002  30.349  -34.162 1.00 23.47 ? 360  ASP B OD1 1 
ATOM   5516 O  OD2 . ASP B 1 360 ? 40.200  31.262  -32.558 1.00 30.72 ? 360  ASP B OD2 1 
ATOM   5517 N  N   . THR B 1 361 ? 36.143  29.035  -33.941 1.00 18.97 ? 361  THR B N   1 
ATOM   5518 C  CA  . THR B 1 361 ? 36.011  27.582  -33.922 1.00 19.79 ? 361  THR B CA  1 
ATOM   5519 C  C   . THR B 1 361 ? 37.135  26.864  -34.679 1.00 20.20 ? 361  THR B C   1 
ATOM   5520 O  O   . THR B 1 361 ? 36.992  25.689  -34.993 1.00 20.59 ? 361  THR B O   1 
ATOM   5521 C  CB  . THR B 1 361 ? 34.655  27.117  -34.476 1.00 19.39 ? 361  THR B CB  1 
ATOM   5522 O  OG1 . THR B 1 361 ? 34.557  27.489  -35.848 1.00 18.99 ? 361  THR B OG1 1 
ATOM   5523 C  CG2 . THR B 1 361 ? 33.507  27.738  -33.689 1.00 19.55 ? 361  THR B CG2 1 
ATOM   5524 N  N   . SER B 1 362 ? 38.249  27.554  -34.937 1.00 19.70 ? 362  SER B N   1 
ATOM   5525 C  CA  . SER B 1 362 ? 39.360  26.971  -35.695 1.00 20.65 ? 362  SER B CA  1 
ATOM   5526 C  C   . SER B 1 362 ? 40.126  25.857  -34.964 1.00 22.10 ? 362  SER B C   1 
ATOM   5527 O  O   . SER B 1 362 ? 40.759  25.046  -35.624 1.00 22.28 ? 362  SER B O   1 
ATOM   5528 C  CB  . SER B 1 362 ? 40.354  28.048  -36.147 1.00 19.84 ? 362  SER B CB  1 
ATOM   5529 O  OG  . SER B 1 362 ? 41.023  28.604  -35.045 1.00 18.41 ? 362  SER B OG  1 
ATOM   5530 N  N   . ASP B 1 363 ? 40.073  25.809  -33.629 1.00 22.97 ? 363  ASP B N   1 
ATOM   5531 C  CA  . ASP B 1 363 ? 40.717  24.714  -32.881 1.00 24.44 ? 363  ASP B CA  1 
ATOM   5532 C  C   . ASP B 1 363 ? 39.779  23.502  -32.772 1.00 24.53 ? 363  ASP B C   1 
ATOM   5533 O  O   . ASP B 1 363 ? 39.077  23.316  -31.769 1.00 23.01 ? 363  ASP B O   1 
ATOM   5534 C  CB  . ASP B 1 363 ? 41.178  25.153  -31.483 1.00 25.37 ? 363  ASP B CB  1 
ATOM   5535 C  CG  . ASP B 1 363 ? 41.859  24.008  -30.701 1.00 26.77 ? 363  ASP B CG  1 
ATOM   5536 O  OD1 . ASP B 1 363 ? 42.140  22.957  -31.327 1.00 29.06 ? 363  ASP B OD1 1 
ATOM   5537 O  OD2 . ASP B 1 363 ? 42.095  24.151  -29.480 1.00 24.81 ? 363  ASP B OD2 1 
ATOM   5538 N  N   . ASN B 1 364 ? 39.757  22.703  -33.828 1.00 24.62 ? 364  ASN B N   1 
ATOM   5539 C  CA  . ASN B 1 364 ? 38.975  21.497  -33.849 1.00 26.50 ? 364  ASN B CA  1 
ATOM   5540 C  C   . ASN B 1 364 ? 37.504  21.735  -33.501 1.00 25.77 ? 364  ASN B C   1 
ATOM   5541 O  O   . ASN B 1 364 ? 36.907  20.970  -32.749 1.00 24.84 ? 364  ASN B O   1 
ATOM   5542 C  CB  . ASN B 1 364 ? 39.586  20.476  -32.889 1.00 29.71 ? 364  ASN B CB  1 
ATOM   5543 C  CG  . ASN B 1 364 ? 39.368  19.059  -33.360 1.00 34.34 ? 364  ASN B CG  1 
ATOM   5544 O  OD1 . ASN B 1 364 ? 39.895  18.665  -34.401 1.00 43.02 ? 364  ASN B OD1 1 
ATOM   5545 N  ND2 . ASN B 1 364 ? 38.583  18.292  -32.622 1.00 35.81 ? 364  ASN B ND2 1 
ATOM   5546 N  N   . ASN B 1 365 ? 36.941  22.819  -34.033 1.00 24.52 ? 365  ASN B N   1 
ATOM   5547 C  CA  . ASN B 1 365 ? 35.528  23.130  -33.894 1.00 25.15 ? 365  ASN B CA  1 
ATOM   5548 C  C   . ASN B 1 365 ? 35.036  23.402  -32.473 1.00 22.94 ? 365  ASN B C   1 
ATOM   5549 O  O   . ASN B 1 365 ? 33.845  23.288  -32.213 1.00 23.93 ? 365  ASN B O   1 
ATOM   5550 C  CB  . ASN B 1 365 ? 34.674  22.012  -34.519 1.00 27.88 ? 365  ASN B CB  1 
ATOM   5551 C  CG  . ASN B 1 365 ? 34.966  21.811  -35.992 1.00 30.12 ? 365  ASN B CG  1 
ATOM   5552 O  OD1 . ASN B 1 365 ? 35.087  22.762  -36.748 1.00 33.13 ? 365  ASN B OD1 1 
ATOM   5553 N  ND2 . ASN B 1 365 ? 35.072  20.565  -36.405 1.00 32.88 ? 365  ASN B ND2 1 
ATOM   5554 N  N   . THR B 1 366 ? 35.920  23.764  -31.553 1.00 21.13 ? 366  THR B N   1 
ATOM   5555 C  CA  . THR B 1 366 ? 35.474  24.098  -30.214 1.00 20.54 ? 366  THR B CA  1 
ATOM   5556 C  C   . THR B 1 366 ? 34.866  25.491  -30.227 1.00 20.13 ? 366  THR B C   1 
ATOM   5557 O  O   . THR B 1 366 ? 35.217  26.305  -31.079 1.00 20.01 ? 366  THR B O   1 
ATOM   5558 C  CB  . THR B 1 366 ? 36.612  24.072  -29.194 1.00 20.92 ? 366  THR B CB  1 
ATOM   5559 O  OG1 . THR B 1 366 ? 37.624  25.017  -29.588 1.00 21.45 ? 366  THR B OG1 1 
ATOM   5560 C  CG2 . THR B 1 366 ? 37.174  22.648  -29.092 1.00 20.60 ? 366  THR B CG2 1 
ATOM   5561 N  N   . ASN B 1 367 ? 33.966  25.758  -29.277 1.00 19.14 ? 367  ASN B N   1 
ATOM   5562 C  CA  . ASN B 1 367 ? 33.390  27.084  -29.115 1.00 18.67 ? 367  ASN B CA  1 
ATOM   5563 C  C   . ASN B 1 367 ? 34.237  27.961  -28.184 1.00 18.53 ? 367  ASN B C   1 
ATOM   5564 O  O   . ASN B 1 367 ? 33.879  28.249  -27.042 1.00 17.28 ? 367  ASN B O   1 
ATOM   5565 C  CB  . ASN B 1 367 ? 31.931  26.976  -28.674 1.00 18.95 ? 367  ASN B CB  1 
ATOM   5566 C  CG  . ASN B 1 367 ? 31.028  26.456  -29.787 1.00 18.85 ? 367  ASN B CG  1 
ATOM   5567 O  OD1 . ASN B 1 367 ? 31.134  26.865  -30.934 1.00 19.03 ? 367  ASN B OD1 1 
ATOM   5568 N  ND2 . ASN B 1 367 ? 30.155  25.553  -29.453 1.00 19.15 ? 367  ASN B ND2 1 
ATOM   5569 N  N   . HIS B 1 368 ? 35.378  28.400  -28.711 1.00 19.04 ? 368  HIS B N   1 
ATOM   5570 C  CA  . HIS B 1 368 ? 36.302  29.248  -27.963 1.00 18.90 ? 368  HIS B CA  1 
ATOM   5571 C  C   . HIS B 1 368 ? 35.723  30.663  -27.923 1.00 18.95 ? 368  HIS B C   1 
ATOM   5572 O  O   . HIS B 1 368 ? 35.843  31.424  -28.882 1.00 17.96 ? 368  HIS B O   1 
ATOM   5573 C  CB  . HIS B 1 368 ? 37.683  29.228  -28.631 1.00 19.70 ? 368  HIS B CB  1 
ATOM   5574 C  CG  . HIS B 1 368 ? 38.747  29.960  -27.870 1.00 19.83 ? 368  HIS B CG  1 
ATOM   5575 N  ND1 . HIS B 1 368 ? 40.081  29.883  -28.212 1.00 20.05 ? 368  HIS B ND1 1 
ATOM   5576 C  CD2 . HIS B 1 368 ? 38.680  30.771  -26.785 1.00 20.60 ? 368  HIS B CD2 1 
ATOM   5577 C  CE1 . HIS B 1 368 ? 40.791  30.622  -27.377 1.00 20.79 ? 368  HIS B CE1 1 
ATOM   5578 N  NE2 . HIS B 1 368 ? 39.965  31.169  -26.498 1.00 21.27 ? 368  HIS B NE2 1 
ATOM   5579 N  N   . GLN B 1 369 ? 35.088  30.985  -26.803 1.00 18.63 ? 369  GLN B N   1 
ATOM   5580 C  CA  . GLN B 1 369 ? 34.395  32.246  -26.620 1.00 18.79 ? 369  GLN B CA  1 
ATOM   5581 C  C   . GLN B 1 369 ? 35.270  33.319  -25.990 1.00 18.55 ? 369  GLN B C   1 
ATOM   5582 O  O   . GLN B 1 369 ? 36.050  33.048  -25.091 1.00 17.83 ? 369  GLN B O   1 
ATOM   5583 C  CB  . GLN B 1 369 ? 33.187  32.034  -25.711 1.00 18.58 ? 369  GLN B CB  1 
ATOM   5584 C  CG  . GLN B 1 369 ? 32.140  31.106  -26.296 1.00 18.26 ? 369  GLN B CG  1 
ATOM   5585 C  CD  . GLN B 1 369 ? 31.457  30.306  -25.213 1.00 18.55 ? 369  GLN B CD  1 
ATOM   5586 O  OE1 . GLN B 1 369 ? 30.859  30.870  -24.283 1.00 16.71 ? 369  GLN B OE1 1 
ATOM   5587 N  NE2 . GLN B 1 369 ? 31.536  28.976  -25.324 1.00 18.56 ? 369  GLN B NE2 1 
ATOM   5588 N  N   . LYS B 1 370 ? 35.087  34.549  -26.449 1.00 18.97 ? 370  LYS B N   1 
ATOM   5589 C  CA  . LYS B 1 370 ? 35.780  35.702  -25.903 1.00 19.43 ? 370  LYS B CA  1 
ATOM   5590 C  C   . LYS B 1 370 ? 34.828  36.893  -25.832 1.00 18.82 ? 370  LYS B C   1 
ATOM   5591 O  O   . LYS B 1 370 ? 34.067  37.148  -26.756 1.00 18.84 ? 370  LYS B O   1 
ATOM   5592 C  CB  . LYS B 1 370 ? 36.972  36.052  -26.795 1.00 20.55 ? 370  LYS B CB  1 
ATOM   5593 C  CG  . LYS B 1 370 ? 38.025  34.955  -26.907 1.00 21.11 ? 370  LYS B CG  1 
ATOM   5594 C  CD  . LYS B 1 370 ? 38.873  35.175  -28.136 1.00 23.22 ? 370  LYS B CD  1 
ATOM   5595 C  CE  . LYS B 1 370 ? 39.944  34.104  -28.280 1.00 24.82 ? 370  LYS B CE  1 
ATOM   5596 N  NZ  . LYS B 1 370 ? 40.535  34.149  -29.643 1.00 24.66 ? 370  LYS B NZ  1 
ATOM   5597 N  N   . ILE B 1 371 ? 34.867  37.625  -24.734 1.00 18.60 ? 371  ILE B N   1 
ATOM   5598 C  CA  . ILE B 1 371 ? 34.129  38.870  -24.650 1.00 18.03 ? 371  ILE B CA  1 
ATOM   5599 C  C   . ILE B 1 371 ? 34.872  39.923  -25.452 1.00 18.29 ? 371  ILE B C   1 
ATOM   5600 O  O   . ILE B 1 371 ? 36.034  40.189  -25.187 1.00 18.34 ? 371  ILE B O   1 
ATOM   5601 C  CB  . ILE B 1 371 ? 33.992  39.359  -23.215 1.00 17.80 ? 371  ILE B CB  1 
ATOM   5602 C  CG1 . ILE B 1 371 ? 33.149  38.371  -22.402 1.00 17.84 ? 371  ILE B CG1 1 
ATOM   5603 C  CG2 . ILE B 1 371 ? 33.363  40.748  -23.196 1.00 17.70 ? 371  ILE B CG2 1 
ATOM   5604 C  CD1 . ILE B 1 371 ? 33.166  38.671  -20.927 1.00 18.45 ? 371  ILE B CD1 1 
ATOM   5605 N  N   . ALA B 1 372 ? 34.182  40.491  -26.436 1.00 17.95 ? 372  ALA B N   1 
ATOM   5606 C  CA  . ALA B 1 372 ? 34.735  41.490  -27.333 1.00 18.29 ? 372  ALA B CA  1 
ATOM   5607 C  C   . ALA B 1 372 ? 33.889  42.760  -27.306 1.00 18.32 ? 372  ALA B C   1 
ATOM   5608 O  O   . ALA B 1 372 ? 32.729  42.756  -26.836 1.00 17.06 ? 372  ALA B O   1 
ATOM   5609 C  CB  . ALA B 1 372 ? 34.798  40.942  -28.753 1.00 18.37 ? 372  ALA B CB  1 
ATOM   5610 N  N   . SER B 1 373 ? 34.478  43.851  -27.798 1.00 18.39 ? 373  SER B N   1 
ATOM   5611 C  CA  . SER B 1 373 ? 33.737  45.091  -27.980 1.00 18.58 ? 373  SER B CA  1 
ATOM   5612 C  C   . SER B 1 373 ? 34.188  45.849  -29.228 1.00 19.26 ? 373  SER B C   1 
ATOM   5613 O  O   . SER B 1 373 ? 35.380  45.806  -29.603 1.00 19.17 ? 373  SER B O   1 
ATOM   5614 C  CB  . SER B 1 373 ? 33.875  45.983  -26.749 1.00 18.76 ? 373  SER B CB  1 
ATOM   5615 O  OG  . SER B 1 373 ? 32.989  47.094  -26.814 1.00 19.09 ? 373  SER B OG  1 
ATOM   5616 N  N   . ALA B 1 374 ? 33.225  46.548  -29.840 1.00 18.04 ? 374  ALA B N   1 
ATOM   5617 C  CA  . ALA B 1 374 ? 33.448  47.413  -30.991 1.00 18.34 ? 374  ALA B CA  1 
ATOM   5618 C  C   . ALA B 1 374 ? 32.561  48.645  -30.876 1.00 18.77 ? 374  ALA B C   1 
ATOM   5619 O  O   . ALA B 1 374 ? 31.497  48.593  -30.258 1.00 19.07 ? 374  ALA B O   1 
ATOM   5620 C  CB  . ALA B 1 374 ? 33.148  46.686  -32.294 1.00 17.85 ? 374  ALA B CB  1 
ATOM   5621 N  N   . THR B 1 375 ? 33.016  49.755  -31.455 1.00 18.51 ? 375  THR B N   1 
ATOM   5622 C  CA  . THR B 1 375 ? 32.231  50.969  -31.512 1.00 18.19 ? 375  THR B CA  1 
ATOM   5623 C  C   . THR B 1 375 ? 31.469  50.973  -32.849 1.00 18.38 ? 375  THR B C   1 
ATOM   5624 O  O   . THR B 1 375 ? 32.052  50.669  -33.916 1.00 17.44 ? 375  THR B O   1 
ATOM   5625 C  CB  . THR B 1 375 ? 33.118  52.233  -31.369 1.00 18.36 ? 375  THR B CB  1 
ATOM   5626 O  OG1 . THR B 1 375 ? 33.901  52.166  -30.168 1.00 17.80 ? 375  THR B OG1 1 
ATOM   5627 C  CG2 . THR B 1 375 ? 32.254  53.485  -31.267 1.00 18.78 ? 375  THR B CG2 1 
ATOM   5628 N  N   . LEU B 1 376 ? 30.171  51.292  -32.800 1.00 17.51 ? 376  LEU B N   1 
ATOM   5629 C  CA  . LEU B 1 376 ? 29.362  51.395  -34.017 1.00 17.56 ? 376  LEU B CA  1 
ATOM   5630 C  C   . LEU B 1 376 ? 28.930  52.830  -34.295 1.00 17.64 ? 376  LEU B C   1 
ATOM   5631 O  O   . LEU B 1 376 ? 28.327  53.489  -33.432 1.00 16.23 ? 376  LEU B O   1 
ATOM   5632 C  CB  . LEU B 1 376 ? 28.091  50.544  -33.928 1.00 17.83 ? 376  LEU B CB  1 
ATOM   5633 C  CG  . LEU B 1 376 ? 28.134  49.114  -33.431 1.00 17.84 ? 376  LEU B CG  1 
ATOM   5634 C  CD1 . LEU B 1 376 ? 26.741  48.520  -33.528 1.00 17.66 ? 376  LEU B CD1 1 
ATOM   5635 C  CD2 . LEU B 1 376 ? 29.126  48.288  -34.222 1.00 18.42 ? 376  LEU B CD2 1 
ATOM   5636 N  N   . TYR B 1 377 ? 29.181  53.280  -35.519 1.00 18.16 ? 377  TYR B N   1 
ATOM   5637 C  CA  . TYR B 1 377 ? 28.768  54.618  -35.957 1.00 19.70 ? 377  TYR B CA  1 
ATOM   5638 C  C   . TYR B 1 377 ? 27.660  54.463  -36.965 1.00 20.65 ? 377  TYR B C   1 
ATOM   5639 O  O   . TYR B 1 377 ? 27.845  53.797  -37.994 1.00 20.57 ? 377  TYR B O   1 
ATOM   5640 C  CB  . TYR B 1 377 ? 29.943  55.373  -36.592 1.00 19.24 ? 377  TYR B CB  1 
ATOM   5641 C  CG  . TYR B 1 377 ? 31.017  55.728  -35.612 1.00 18.66 ? 377  TYR B CG  1 
ATOM   5642 C  CD1 . TYR B 1 377 ? 30.916  56.878  -34.824 1.00 19.47 ? 377  TYR B CD1 1 
ATOM   5643 C  CD2 . TYR B 1 377 ? 32.122  54.916  -35.443 1.00 18.11 ? 377  TYR B CD2 1 
ATOM   5644 C  CE1 . TYR B 1 377 ? 31.907  57.211  -33.913 1.00 18.72 ? 377  TYR B CE1 1 
ATOM   5645 C  CE2 . TYR B 1 377 ? 33.117  55.239  -34.533 1.00 18.32 ? 377  TYR B CE2 1 
ATOM   5646 C  CZ  . TYR B 1 377 ? 33.013  56.381  -33.777 1.00 18.21 ? 377  TYR B CZ  1 
ATOM   5647 O  OH  . TYR B 1 377 ? 34.008  56.693  -32.874 1.00 18.93 ? 377  TYR B OH  1 
ATOM   5648 N  N   . LEU B 1 378 ? 26.500  55.050  -36.665 1.00 21.19 ? 378  LEU B N   1 
ATOM   5649 C  CA  . LEU B 1 378 ? 25.344  54.905  -37.526 1.00 22.14 ? 378  LEU B CA  1 
ATOM   5650 C  C   . LEU B 1 378 ? 25.019  56.206  -38.230 1.00 22.72 ? 378  LEU B C   1 
ATOM   5651 O  O   . LEU B 1 378 ? 25.320  57.282  -37.721 1.00 22.35 ? 378  LEU B O   1 
ATOM   5652 C  CB  . LEU B 1 378 ? 24.126  54.471  -36.715 1.00 22.88 ? 378  LEU B CB  1 
ATOM   5653 C  CG  . LEU B 1 378 ? 24.297  53.254  -35.788 1.00 24.03 ? 378  LEU B CG  1 
ATOM   5654 C  CD1 . LEU B 1 378 ? 22.953  52.859  -35.212 1.00 23.33 ? 378  LEU B CD1 1 
ATOM   5655 C  CD2 . LEU B 1 378 ? 24.955  52.076  -36.486 1.00 23.14 ? 378  LEU B CD2 1 
ATOM   5656 N  N   . THR B 1 379 ? 24.358  56.103  -39.376 1.00 24.26 ? 379  THR B N   1 
ATOM   5657 C  CA  . THR B 1 379 ? 23.843  57.280  -40.053 1.00 26.63 ? 379  THR B CA  1 
ATOM   5658 C  C   . THR B 1 379 ? 22.345  57.159  -40.284 1.00 26.74 ? 379  THR B C   1 
ATOM   5659 O  O   . THR B 1 379 ? 21.819  56.084  -40.544 1.00 26.23 ? 379  THR B O   1 
ATOM   5660 C  CB  . THR B 1 379 ? 24.569  57.536  -41.393 1.00 28.57 ? 379  THR B CB  1 
ATOM   5661 O  OG1 . THR B 1 379 ? 24.486  56.365  -42.205 1.00 30.11 ? 379  THR B OG1 1 
ATOM   5662 C  CG2 . THR B 1 379 ? 26.048  57.891  -41.155 1.00 29.52 ? 379  THR B CG2 1 
ATOM   5663 N  N   . ASP B 1 380 ? 21.685  58.301  -40.189 1.00 27.72 ? 380  ASP B N   1 
ATOM   5664 C  CA  . ASP B 1 380 ? 20.248  58.445  -40.303 1.00 29.76 ? 380  ASP B CA  1 
ATOM   5665 C  C   . ASP B 1 380 ? 19.996  59.236  -41.577 1.00 33.74 ? 380  ASP B C   1 
ATOM   5666 O  O   . ASP B 1 380 ? 20.333  60.429  -41.650 1.00 33.49 ? 380  ASP B O   1 
ATOM   5667 C  CB  . ASP B 1 380 ? 19.751  59.235  -39.095 1.00 29.78 ? 380  ASP B CB  1 
ATOM   5668 C  CG  . ASP B 1 380 ? 18.303  59.667  -39.209 1.00 29.88 ? 380  ASP B CG  1 
ATOM   5669 O  OD1 . ASP B 1 380 ? 17.534  59.130  -40.030 1.00 30.35 ? 380  ASP B OD1 1 
ATOM   5670 O  OD2 . ASP B 1 380 ? 17.928  60.552  -38.427 1.00 29.97 ? 380  ASP B OD2 1 
ATOM   5671 N  N   . ASN B 1 381 ? 19.429  58.579  -42.577 1.00 35.04 ? 381  ASN B N   1 
ATOM   5672 C  CA  . ASN B 1 381 ? 19.109  59.241  -43.832 1.00 40.59 ? 381  ASN B CA  1 
ATOM   5673 C  C   . ASN B 1 381 ? 17.694  58.891  -44.255 1.00 40.18 ? 381  ASN B C   1 
ATOM   5674 O  O   . ASN B 1 381 ? 17.389  57.722  -44.494 1.00 39.30 ? 381  ASN B O   1 
ATOM   5675 C  CB  . ASN B 1 381 ? 20.098  58.824  -44.926 1.00 43.87 ? 381  ASN B CB  1 
ATOM   5676 C  CG  . ASN B 1 381 ? 19.780  59.456  -46.265 1.00 49.06 ? 381  ASN B CG  1 
ATOM   5677 O  OD1 . ASN B 1 381 ? 19.808  60.678  -46.405 1.00 55.50 ? 381  ASN B OD1 1 
ATOM   5678 N  ND2 . ASN B 1 381 ? 19.464  58.627  -47.257 1.00 52.63 ? 381  ASN B ND2 1 
ATOM   5679 N  N   . ASN B 1 382 ? 16.824  59.897  -44.310 1.00 40.60 ? 382  ASN B N   1 
ATOM   5680 C  CA  . ASN B 1 382 ? 15.513  59.739  -44.931 1.00 42.46 ? 382  ASN B CA  1 
ATOM   5681 C  C   . ASN B 1 382 ? 14.643  58.643  -44.308 1.00 39.04 ? 382  ASN B C   1 
ATOM   5682 O  O   . ASN B 1 382 ? 13.962  57.915  -45.029 1.00 39.49 ? 382  ASN B O   1 
ATOM   5683 C  CB  . ASN B 1 382 ? 15.697  59.457  -46.437 1.00 46.11 ? 382  ASN B CB  1 
ATOM   5684 C  CG  . ASN B 1 382 ? 15.152  60.565  -47.317 1.00 50.38 ? 382  ASN B CG  1 
ATOM   5685 O  OD1 . ASN B 1 382 ? 15.519  61.737  -47.173 1.00 51.67 ? 382  ASN B OD1 1 
ATOM   5686 N  ND2 . ASN B 1 382 ? 14.283  60.195  -48.254 1.00 53.61 ? 382  ASN B ND2 1 
ATOM   5687 N  N   . GLY B 1 383 ? 14.674  58.515  -42.982 1.00 36.41 ? 383  GLY B N   1 
ATOM   5688 C  CA  . GLY B 1 383 ? 13.907  57.463  -42.288 1.00 34.21 ? 383  GLY B CA  1 
ATOM   5689 C  C   . GLY B 1 383 ? 14.618  56.121  -42.198 1.00 32.58 ? 383  GLY B C   1 
ATOM   5690 O  O   . GLY B 1 383 ? 14.134  55.200  -41.540 1.00 33.42 ? 383  GLY B O   1 
ATOM   5691 N  N   . ASN B 1 384 ? 15.784  56.025  -42.829 1.00 33.01 ? 384  ASN B N   1 
ATOM   5692 C  CA  . ASN B 1 384 ? 16.573  54.791  -42.870 1.00 33.27 ? 384  ASN B CA  1 
ATOM   5693 C  C   . ASN B 1 384 ? 17.858  54.935  -42.090 1.00 30.40 ? 384  ASN B C   1 
ATOM   5694 O  O   . ASN B 1 384 ? 18.593  55.904  -42.272 1.00 30.60 ? 384  ASN B O   1 
ATOM   5695 C  CB  . ASN B 1 384 ? 16.930  54.428  -44.307 1.00 34.13 ? 384  ASN B CB  1 
ATOM   5696 C  CG  . ASN B 1 384 ? 15.726  54.012  -45.107 1.00 36.74 ? 384  ASN B CG  1 
ATOM   5697 O  OD1 . ASN B 1 384 ? 14.900  53.220  -44.644 1.00 39.36 ? 384  ASN B OD1 1 
ATOM   5698 N  ND2 . ASN B 1 384 ? 15.610  54.544  -46.313 1.00 38.82 ? 384  ASN B ND2 1 
ATOM   5699 N  N   . VAL B 1 385 ? 18.116  53.955  -41.232 1.00 27.92 ? 385  VAL B N   1 
ATOM   5700 C  CA  . VAL B 1 385 ? 19.336  53.882  -40.452 1.00 26.16 ? 385  VAL B CA  1 
ATOM   5701 C  C   . VAL B 1 385 ? 20.338  53.007  -41.197 1.00 25.01 ? 385  VAL B C   1 
ATOM   5702 O  O   . VAL B 1 385 ? 19.989  51.927  -41.683 1.00 23.71 ? 385  VAL B O   1 
ATOM   5703 C  CB  . VAL B 1 385 ? 19.048  53.299  -39.053 1.00 26.42 ? 385  VAL B CB  1 
ATOM   5704 C  CG1 . VAL B 1 385 ? 20.333  52.896  -38.339 1.00 25.95 ? 385  VAL B CG1 1 
ATOM   5705 C  CG2 . VAL B 1 385 ? 18.251  54.300  -38.227 1.00 26.90 ? 385  VAL B CG2 1 
ATOM   5706 N  N   . SER B 1 386 ? 21.584  53.471  -41.270 1.00 24.16 ? 386  SER B N   1 
ATOM   5707 C  CA  . SER B 1 386 ? 22.676  52.691  -41.861 1.00 24.03 ? 386  SER B CA  1 
ATOM   5708 C  C   . SER B 1 386 ? 23.816  52.542  -40.901 1.00 22.96 ? 386  SER B C   1 
ATOM   5709 O  O   . SER B 1 386 ? 24.024  53.397  -40.036 1.00 20.85 ? 386  SER B O   1 
ATOM   5710 C  CB  . SER B 1 386 ? 23.207  53.369  -43.124 1.00 24.88 ? 386  SER B CB  1 
ATOM   5711 O  OG  . SER B 1 386 ? 22.322  53.105  -44.182 1.00 28.67 ? 386  SER B OG  1 
ATOM   5712 N  N   . LEU B 1 387 ? 24.578  51.465  -41.097 1.00 22.87 ? 387  LEU B N   1 
ATOM   5713 C  CA  . LEU B 1 387 ? 25.797  51.232  -40.347 1.00 23.34 ? 387  LEU B CA  1 
ATOM   5714 C  C   . LEU B 1 387 ? 26.958  51.840  -41.130 1.00 22.92 ? 387  LEU B C   1 
ATOM   5715 O  O   . LEU B 1 387 ? 27.366  51.309  -42.146 1.00 23.48 ? 387  LEU B O   1 
ATOM   5716 C  CB  . LEU B 1 387 ? 25.982  49.731  -40.100 1.00 24.14 ? 387  LEU B CB  1 
ATOM   5717 C  CG  . LEU B 1 387 ? 27.214  49.243  -39.332 1.00 25.34 ? 387  LEU B CG  1 
ATOM   5718 C  CD1 . LEU B 1 387 ? 27.389  49.933  -37.984 1.00 25.57 ? 387  LEU B CD1 1 
ATOM   5719 C  CD2 . LEU B 1 387 ? 27.092  47.737  -39.145 1.00 24.99 ? 387  LEU B CD2 1 
ATOM   5720 N  N   . ALA B 1 388 ? 27.487  52.966  -40.657 1.00 22.72 ? 388  ALA B N   1 
ATOM   5721 C  CA  . ALA B 1 388 ? 28.552  53.670  -41.373 1.00 21.98 ? 388  ALA B CA  1 
ATOM   5722 C  C   . ALA B 1 388 ? 29.916  53.075  -41.066 1.00 22.51 ? 388  ALA B C   1 
ATOM   5723 O  O   . ALA B 1 388 ? 30.747  52.950  -41.962 1.00 20.94 ? 388  ALA B O   1 
ATOM   5724 C  CB  . ALA B 1 388 ? 28.541  55.152  -41.044 1.00 21.24 ? 388  ALA B CB  1 
ATOM   5725 N  N   . GLN B 1 389 ? 30.162  52.702  -39.809 1.00 22.73 ? 389  GLN B N   1 
ATOM   5726 C  CA  . GLN B 1 389 ? 31.459  52.128  -39.462 1.00 22.66 ? 389  GLN B CA  1 
ATOM   5727 C  C   . GLN B 1 389 ? 31.420  51.285  -38.189 1.00 21.58 ? 389  GLN B C   1 
ATOM   5728 O  O   . GLN B 1 389 ? 30.677  51.584  -37.249 1.00 20.49 ? 389  GLN B O   1 
ATOM   5729 C  CB  . GLN B 1 389 ? 32.498  53.251  -39.309 1.00 23.72 ? 389  GLN B CB  1 
ATOM   5730 C  CG  . GLN B 1 389 ? 33.951  52.805  -39.129 1.00 24.77 ? 389  GLN B CG  1 
ATOM   5731 C  CD  . GLN B 1 389 ? 34.875  53.970  -38.778 1.00 27.76 ? 389  GLN B CD  1 
ATOM   5732 O  OE1 . GLN B 1 389 ? 34.429  55.099  -38.617 1.00 30.81 ? 389  GLN B OE1 1 
ATOM   5733 N  NE2 . GLN B 1 389 ? 36.166  53.696  -38.659 1.00 29.36 ? 389  GLN B NE2 1 
ATOM   5734 N  N   . VAL B 1 390 ? 32.258  50.254  -38.188 1.00 20.20 ? 390  VAL B N   1 
ATOM   5735 C  CA  . VAL B 1 390 ? 32.526  49.409  -37.033 1.00 20.12 ? 390  VAL B CA  1 
ATOM   5736 C  C   . VAL B 1 390 ? 33.985  49.597  -36.743 1.00 19.83 ? 390  VAL B C   1 
ATOM   5737 O  O   . VAL B 1 390 ? 34.821  49.345  -37.602 1.00 19.74 ? 390  VAL B O   1 
ATOM   5738 C  CB  . VAL B 1 390 ? 32.246  47.922  -37.349 1.00 20.89 ? 390  VAL B CB  1 
ATOM   5739 C  CG1 . VAL B 1 390 ? 32.514  47.037  -36.134 1.00 20.50 ? 390  VAL B CG1 1 
ATOM   5740 C  CG2 . VAL B 1 390 ? 30.803  47.761  -37.821 1.00 21.36 ? 390  VAL B CG2 1 
ATOM   5741 N  N   . ALA B 1 391 ? 34.311  50.053  -35.545 1.00 19.81 ? 391  ALA B N   1 
ATOM   5742 C  CA  . ALA B 1 391 ? 35.658  50.490  -35.273 1.00 19.42 ? 391  ALA B CA  1 
ATOM   5743 C  C   . ALA B 1 391 ? 36.205  49.944  -33.968 1.00 19.61 ? 391  ALA B C   1 
ATOM   5744 O  O   . ALA B 1 391 ? 35.483  49.822  -32.980 1.00 19.04 ? 391  ALA B O   1 
ATOM   5745 C  CB  . ALA B 1 391 ? 35.701  52.024  -35.251 1.00 19.85 ? 391  ALA B CB  1 
ATOM   5746 N  N   . ASN B 1 392 ? 37.517  49.703  -33.948 1.00 19.77 ? 392  ASN B N   1 
ATOM   5747 C  CA  . ASN B 1 392 ? 38.216  49.313  -32.723 1.00 20.78 ? 392  ASN B CA  1 
ATOM   5748 C  C   . ASN B 1 392 ? 37.673  47.972  -32.153 1.00 19.30 ? 392  ASN B C   1 
ATOM   5749 O  O   . ASN B 1 392 ? 37.560  47.821  -30.943 1.00 19.58 ? 392  ASN B O   1 
ATOM   5750 C  CB  . ASN B 1 392 ? 38.172  50.413  -31.620 1.00 22.18 ? 392  ASN B CB  1 
ATOM   5751 C  CG  . ASN B 1 392 ? 38.019  51.850  -32.162 1.00 25.77 ? 392  ASN B CG  1 
ATOM   5752 O  OD1 . ASN B 1 392 ? 38.827  52.299  -32.960 1.00 26.08 ? 392  ASN B OD1 1 
ATOM   5753 N  ND2 . ASN B 1 392 ? 36.968  52.588  -31.688 1.00 25.94 ? 392  ASN B ND2 1 
ATOM   5754 N  N   . ASP B 1 393 ? 37.360  47.016  -33.024 1.00 18.67 ? 393  ASP B N   1 
ATOM   5755 C  CA  . ASP B 1 393 ? 36.932  45.673  -32.594 1.00 18.76 ? 393  ASP B CA  1 
ATOM   5756 C  C   . ASP B 1 393 ? 38.088  44.947  -31.928 1.00 18.22 ? 393  ASP B C   1 
ATOM   5757 O  O   . ASP B 1 393 ? 39.143  44.768  -32.538 1.00 18.08 ? 393  ASP B O   1 
ATOM   5758 C  CB  . ASP B 1 393 ? 36.444  44.822  -33.774 1.00 18.53 ? 393  ASP B CB  1 
ATOM   5759 C  CG  . ASP B 1 393 ? 35.902  43.428  -33.325 1.00 18.85 ? 393  ASP B CG  1 
ATOM   5760 O  OD1 . ASP B 1 393 ? 35.174  43.342  -32.323 1.00 18.98 ? 393  ASP B OD1 1 
ATOM   5761 O  OD2 . ASP B 1 393 ? 36.147  42.416  -34.009 1.00 18.78 ? 393  ASP B OD2 1 
ATOM   5762 N  N   . HIS B 1 394 ? 37.895  44.519  -30.685 1.00 17.17 ? 394  HIS B N   1 
ATOM   5763 C  CA  . HIS B 1 394 ? 38.959  43.862  -29.960 1.00 17.01 ? 394  HIS B CA  1 
ATOM   5764 C  C   . HIS B 1 394 ? 38.416  43.009  -28.814 1.00 17.92 ? 394  HIS B C   1 
ATOM   5765 O  O   . HIS B 1 394 ? 37.266  43.164  -28.381 1.00 17.70 ? 394  HIS B O   1 
ATOM   5766 C  CB  . HIS B 1 394 ? 39.948  44.904  -29.396 1.00 16.28 ? 394  HIS B CB  1 
ATOM   5767 C  CG  . HIS B 1 394 ? 39.358  45.764  -28.319 1.00 15.92 ? 394  HIS B CG  1 
ATOM   5768 N  ND1 . HIS B 1 394 ? 38.427  46.749  -28.581 1.00 15.13 ? 394  HIS B ND1 1 
ATOM   5769 C  CD2 . HIS B 1 394 ? 39.536  45.761  -26.976 1.00 15.91 ? 394  HIS B CD2 1 
ATOM   5770 C  CE1 . HIS B 1 394 ? 38.067  47.321  -27.445 1.00 15.57 ? 394  HIS B CE1 1 
ATOM   5771 N  NE2 . HIS B 1 394 ? 38.723  46.741  -26.456 1.00 15.80 ? 394  HIS B NE2 1 
ATOM   5772 N  N   . ILE B 1 395 ? 39.287  42.134  -28.317 1.00 18.21 ? 395  ILE B N   1 
ATOM   5773 C  CA  . ILE B 1 395 ? 38.976  41.252  -27.218 1.00 18.33 ? 395  ILE B CA  1 
ATOM   5774 C  C   . ILE B 1 395 ? 39.142  42.022  -25.915 1.00 18.64 ? 395  ILE B C   1 
ATOM   5775 O  O   . ILE B 1 395 ? 40.147  42.669  -25.703 1.00 18.96 ? 395  ILE B O   1 
ATOM   5776 C  CB  . ILE B 1 395 ? 39.909  40.026  -27.187 1.00 18.75 ? 395  ILE B CB  1 
ATOM   5777 C  CG1 . ILE B 1 395 ? 39.841  39.220  -28.507 1.00 18.55 ? 395  ILE B CG1 1 
ATOM   5778 C  CG2 . ILE B 1 395 ? 39.589  39.163  -25.966 1.00 18.57 ? 395  ILE B CG2 1 
ATOM   5779 C  CD1 . ILE B 1 395 ? 38.440  38.829  -28.939 1.00 19.10 ? 395  ILE B CD1 1 
ATOM   5780 N  N   . VAL B 1 396 ? 38.143  41.946  -25.049 1.00 18.31 ? 396  VAL B N   1 
ATOM   5781 C  CA  . VAL B 1 396 ? 38.186  42.614  -23.757 1.00 18.94 ? 396  VAL B CA  1 
ATOM   5782 C  C   . VAL B 1 396 ? 38.622  41.627  -22.680 1.00 19.38 ? 396  VAL B C   1 
ATOM   5783 O  O   . VAL B 1 396 ? 39.499  41.935  -21.892 1.00 19.62 ? 396  VAL B O   1 
ATOM   5784 C  CB  . VAL B 1 396 ? 36.802  43.197  -23.415 1.00 19.16 ? 396  VAL B CB  1 
ATOM   5785 C  CG1 . VAL B 1 396 ? 36.805  43.853  -22.043 1.00 19.48 ? 396  VAL B CG1 1 
ATOM   5786 C  CG2 . VAL B 1 396 ? 36.391  44.187  -24.495 1.00 19.42 ? 396  VAL B CG2 1 
ATOM   5787 N  N   . PHE B 1 397 ? 38.014  40.437  -22.664 1.00 19.31 ? 397  PHE B N   1 
ATOM   5788 C  CA  . PHE B 1 397 ? 38.281  39.463  -21.617 1.00 19.83 ? 397  PHE B CA  1 
ATOM   5789 C  C   . PHE B 1 397 ? 37.967  38.065  -22.109 1.00 20.86 ? 397  PHE B C   1 
ATOM   5790 O  O   . PHE B 1 397 ? 36.995  37.852  -22.841 1.00 19.22 ? 397  PHE B O   1 
ATOM   5791 C  CB  . PHE B 1 397 ? 37.430  39.783  -20.372 1.00 19.69 ? 397  PHE B CB  1 
ATOM   5792 C  CG  . PHE B 1 397 ? 37.803  38.981  -19.157 1.00 19.28 ? 397  PHE B CG  1 
ATOM   5793 C  CD1 . PHE B 1 397 ? 39.094  39.044  -18.632 1.00 18.87 ? 397  PHE B CD1 1 
ATOM   5794 C  CD2 . PHE B 1 397 ? 36.870  38.158  -18.542 1.00 19.18 ? 397  PHE B CD2 1 
ATOM   5795 C  CE1 . PHE B 1 397 ? 39.443  38.303  -17.524 1.00 19.23 ? 397  PHE B CE1 1 
ATOM   5796 C  CE2 . PHE B 1 397 ? 37.218  37.411  -17.427 1.00 19.55 ? 397  PHE B CE2 1 
ATOM   5797 C  CZ  . PHE B 1 397 ? 38.504  37.485  -16.915 1.00 19.15 ? 397  PHE B CZ  1 
ATOM   5798 N  N   . GLU B 1 398 ? 38.808  37.109  -21.739 1.00 21.89 ? 398  GLU B N   1 
ATOM   5799 C  CA  . GLU B 1 398 ? 38.470  35.710  -21.966 1.00 23.16 ? 398  GLU B CA  1 
ATOM   5800 C  C   . GLU B 1 398 ? 38.831  34.798  -20.817 1.00 21.76 ? 398  GLU B C   1 
ATOM   5801 O  O   . GLU B 1 398 ? 38.976  33.605  -21.012 1.00 22.35 ? 398  GLU B O   1 
ATOM   5802 C  CB  . GLU B 1 398 ? 39.077  35.201  -23.271 1.00 25.75 ? 398  GLU B CB  1 
ATOM   5803 C  CG  . GLU B 1 398 ? 40.588  35.288  -23.357 1.00 27.38 ? 398  GLU B CG  1 
ATOM   5804 C  CD  . GLU B 1 398 ? 41.096  34.606  -24.606 1.00 30.03 ? 398  GLU B CD  1 
ATOM   5805 O  OE1 . GLU B 1 398 ? 40.773  33.409  -24.790 1.00 30.93 ? 398  GLU B OE1 1 
ATOM   5806 O  OE2 . GLU B 1 398 ? 41.806  35.269  -25.398 1.00 34.14 ? 398  GLU B OE2 1 
ATOM   5807 N  N   . GLY B 1 399 ? 38.934  35.359  -19.623 1.00 20.84 ? 399  GLY B N   1 
ATOM   5808 C  CA  . GLY B 1 399 ? 39.181  34.576  -18.412 1.00 21.71 ? 399  GLY B CA  1 
ATOM   5809 C  C   . GLY B 1 399 ? 40.594  34.769  -17.900 1.00 20.97 ? 399  GLY B C   1 
ATOM   5810 O  O   . GLY B 1 399 ? 41.520  35.000  -18.686 1.00 21.99 ? 399  GLY B O   1 
ATOM   5811 N  N   . ASP B 1 400 ? 40.757  34.652  -16.586 1.00 21.11 ? 400  ASP B N   1 
ATOM   5812 C  CA  . ASP B 1 400 ? 42.058  34.843  -15.938 1.00 20.95 ? 400  ASP B CA  1 
ATOM   5813 C  C   . ASP B 1 400 ? 42.649  33.550  -15.385 1.00 21.59 ? 400  ASP B C   1 
ATOM   5814 O  O   . ASP B 1 400 ? 43.866  33.458  -15.204 1.00 21.49 ? 400  ASP B O   1 
ATOM   5815 C  CB  . ASP B 1 400 ? 41.931  35.842  -14.794 1.00 21.23 ? 400  ASP B CB  1 
ATOM   5816 C  CG  . ASP B 1 400 ? 40.949  35.384  -13.743 1.00 21.65 ? 400  ASP B CG  1 
ATOM   5817 O  OD1 . ASP B 1 400 ? 39.784  35.114  -14.103 1.00 22.31 ? 400  ASP B OD1 1 
ATOM   5818 O  OD2 . ASP B 1 400 ? 41.340  35.264  -12.564 1.00 21.59 ? 400  ASP B OD2 1 
ATOM   5819 N  N   . GLY B 1 401 ? 41.796  32.575  -15.064 1.00 21.43 ? 401  GLY B N   1 
ATOM   5820 C  CA  . GLY B 1 401 ? 42.257  31.304  -14.506 1.00 21.11 ? 401  GLY B CA  1 
ATOM   5821 C  C   . GLY B 1 401 ? 41.998  31.156  -13.021 1.00 20.63 ? 401  GLY B C   1 
ATOM   5822 O  O   . GLY B 1 401 ? 41.875  30.049  -12.524 1.00 20.87 ? 401  GLY B O   1 
ATOM   5823 N  N   . TYR B 1 402 ? 41.889  32.266  -12.307 1.00 21.45 ? 402  TYR B N   1 
ATOM   5824 C  CA  . TYR B 1 402 ? 41.546  32.230  -10.878 1.00 21.87 ? 402  TYR B CA  1 
ATOM   5825 C  C   . TYR B 1 402 ? 40.047  32.490  -10.616 1.00 21.53 ? 402  TYR B C   1 
ATOM   5826 O  O   . TYR B 1 402 ? 39.320  31.614  -10.139 1.00 20.05 ? 402  TYR B O   1 
ATOM   5827 C  CB  . TYR B 1 402 ? 42.409  33.242  -10.125 1.00 21.97 ? 402  TYR B CB  1 
ATOM   5828 C  CG  . TYR B 1 402 ? 42.166  33.253  -8.648  1.00 22.12 ? 402  TYR B CG  1 
ATOM   5829 C  CD1 . TYR B 1 402 ? 42.631  32.227  -7.848  1.00 22.82 ? 402  TYR B CD1 1 
ATOM   5830 C  CD2 . TYR B 1 402 ? 41.478  34.295  -8.049  1.00 22.73 ? 402  TYR B CD2 1 
ATOM   5831 C  CE1 . TYR B 1 402 ? 42.414  32.237  -6.481  1.00 23.36 ? 402  TYR B CE1 1 
ATOM   5832 C  CE2 . TYR B 1 402 ? 41.250  34.308  -6.690  1.00 23.22 ? 402  TYR B CE2 1 
ATOM   5833 C  CZ  . TYR B 1 402 ? 41.726  33.280  -5.916  1.00 23.81 ? 402  TYR B CZ  1 
ATOM   5834 O  OH  . TYR B 1 402 ? 41.490  33.299  -4.566  1.00 26.36 ? 402  TYR B OH  1 
ATOM   5835 N  N   . TYR B 1 403 ? 39.589  33.697  -10.926 1.00 21.63 ? 403  TYR B N   1 
ATOM   5836 C  CA  . TYR B 1 403 ? 38.183  34.035  -10.775 1.00 21.45 ? 403  TYR B CA  1 
ATOM   5837 C  C   . TYR B 1 403 ? 37.360  33.268  -11.796 1.00 20.58 ? 403  TYR B C   1 
ATOM   5838 O  O   . TYR B 1 403 ? 36.293  32.734  -11.465 1.00 19.14 ? 403  TYR B O   1 
ATOM   5839 C  CB  . TYR B 1 403 ? 37.958  35.551  -10.938 1.00 22.45 ? 403  TYR B CB  1 
ATOM   5840 C  CG  . TYR B 1 403 ? 38.683  36.353  -9.891  1.00 24.07 ? 403  TYR B CG  1 
ATOM   5841 C  CD1 . TYR B 1 403 ? 38.390  36.180  -8.550  1.00 25.06 ? 403  TYR B CD1 1 
ATOM   5842 C  CD2 . TYR B 1 403 ? 39.704  37.244  -10.234 1.00 25.48 ? 403  TYR B CD2 1 
ATOM   5843 C  CE1 . TYR B 1 403 ? 39.057  36.886  -7.573  1.00 25.63 ? 403  TYR B CE1 1 
ATOM   5844 C  CE2 . TYR B 1 403 ? 40.377  37.965  -9.258  1.00 26.05 ? 403  TYR B CE2 1 
ATOM   5845 C  CZ  . TYR B 1 403 ? 40.047  37.776  -7.933  1.00 26.52 ? 403  TYR B CZ  1 
ATOM   5846 O  OH  . TYR B 1 403 ? 40.690  38.471  -6.947  1.00 28.76 ? 403  TYR B OH  1 
ATOM   5847 N  N   . TYR B 1 404 ? 37.868  33.196  -13.027 1.00 19.90 ? 404  TYR B N   1 
ATOM   5848 C  CA  . TYR B 1 404 ? 37.114  32.602  -14.135 1.00 19.62 ? 404  TYR B CA  1 
ATOM   5849 C  C   . TYR B 1 404 ? 37.956  31.663  -14.978 1.00 19.78 ? 404  TYR B C   1 
ATOM   5850 O  O   . TYR B 1 404 ? 39.122  31.939  -15.263 1.00 19.76 ? 404  TYR B O   1 
ATOM   5851 C  CB  . TYR B 1 404 ? 36.514  33.700  -14.999 1.00 19.10 ? 404  TYR B CB  1 
ATOM   5852 C  CG  . TYR B 1 404 ? 35.751  34.691  -14.159 1.00 19.28 ? 404  TYR B CG  1 
ATOM   5853 C  CD1 . TYR B 1 404 ? 34.493  34.374  -13.661 1.00 19.49 ? 404  TYR B CD1 1 
ATOM   5854 C  CD2 . TYR B 1 404 ? 36.297  35.928  -13.829 1.00 19.36 ? 404  TYR B CD2 1 
ATOM   5855 C  CE1 . TYR B 1 404 ? 33.790  35.252  -12.872 1.00 19.08 ? 404  TYR B CE1 1 
ATOM   5856 C  CE2 . TYR B 1 404 ? 35.598  36.829  -13.029 1.00 19.03 ? 404  TYR B CE2 1 
ATOM   5857 C  CZ  . TYR B 1 404 ? 34.348  36.481  -12.544 1.00 19.24 ? 404  TYR B CZ  1 
ATOM   5858 O  OH  . TYR B 1 404 ? 33.640  37.348  -11.735 1.00 18.80 ? 404  TYR B OH  1 
ATOM   5859 N  N   . GLN B 1 405 ? 37.335  30.556  -15.380 1.00 19.76 ? 405  GLN B N   1 
ATOM   5860 C  CA  . GLN B 1 405 ? 37.979  29.527  -16.186 1.00 19.43 ? 405  GLN B CA  1 
ATOM   5861 C  C   . GLN B 1 405 ? 38.378  30.059  -17.559 1.00 19.95 ? 405  GLN B C   1 
ATOM   5862 O  O   . GLN B 1 405 ? 37.586  30.772  -18.193 1.00 18.88 ? 405  GLN B O   1 
ATOM   5863 C  CB  . GLN B 1 405 ? 37.029  28.349  -16.383 1.00 19.92 ? 405  GLN B CB  1 
ATOM   5864 C  CG  . GLN B 1 405 ? 37.670  27.128  -17.038 1.00 20.78 ? 405  GLN B CG  1 
ATOM   5865 C  CD  . GLN B 1 405 ? 36.649  26.053  -17.362 1.00 21.76 ? 405  GLN B CD  1 
ATOM   5866 O  OE1 . GLN B 1 405 ? 35.631  26.316  -18.022 1.00 22.04 ? 405  GLN B OE1 1 
ATOM   5867 N  NE2 . GLN B 1 405 ? 36.915  24.837  -16.912 1.00 20.36 ? 405  GLN B NE2 1 
ATOM   5868 N  N   . THR B 1 406 ? 39.596  29.709  -17.995 1.00 18.82 ? 406  THR B N   1 
ATOM   5869 C  CA  . THR B 1 406 ? 40.112  30.070  -19.320 1.00 19.09 ? 406  THR B CA  1 
ATOM   5870 C  C   . THR B 1 406 ? 39.878  28.936  -20.316 1.00 18.73 ? 406  THR B C   1 
ATOM   5871 O  O   . THR B 1 406 ? 39.611  27.793  -19.933 1.00 18.96 ? 406  THR B O   1 
ATOM   5872 C  CB  . THR B 1 406 ? 41.639  30.365  -19.299 1.00 18.99 ? 406  THR B CB  1 
ATOM   5873 O  OG1 . THR B 1 406 ? 42.364  29.147  -19.099 1.00 18.30 ? 406  THR B OG1 1 
ATOM   5874 C  CG2 . THR B 1 406 ? 42.005  31.366  -18.189 1.00 19.11 ? 406  THR B CG2 1 
ATOM   5875 N  N   . TYR B 1 407 ? 39.997  29.259  -21.594 1.00 18.53 ? 407  TYR B N   1 
ATOM   5876 C  CA  . TYR B 1 407 ? 39.952  28.257  -22.649 1.00 19.76 ? 407  TYR B CA  1 
ATOM   5877 C  C   . TYR B 1 407 ? 41.021  27.174  -22.454 1.00 20.71 ? 407  TYR B C   1 
ATOM   5878 O  O   . TYR B 1 407 ? 40.725  25.999  -22.635 1.00 20.66 ? 407  TYR B O   1 
ATOM   5879 C  CB  . TYR B 1 407 ? 40.132  28.891  -24.028 1.00 19.83 ? 407  TYR B CB  1 
ATOM   5880 C  CG  . TYR B 1 407 ? 40.102  27.869  -25.158 1.00 20.85 ? 407  TYR B CG  1 
ATOM   5881 C  CD1 . TYR B 1 407 ? 38.899  27.295  -25.563 1.00 20.73 ? 407  TYR B CD1 1 
ATOM   5882 C  CD2 . TYR B 1 407 ? 41.277  27.469  -25.819 1.00 21.35 ? 407  TYR B CD2 1 
ATOM   5883 C  CE1 . TYR B 1 407 ? 38.855  26.364  -26.584 1.00 21.28 ? 407  TYR B CE1 1 
ATOM   5884 C  CE2 . TYR B 1 407 ? 41.243  26.529  -26.842 1.00 20.71 ? 407  TYR B CE2 1 
ATOM   5885 C  CZ  . TYR B 1 407 ? 40.025  25.970  -27.209 1.00 20.95 ? 407  TYR B CZ  1 
ATOM   5886 O  OH  . TYR B 1 407 ? 39.943  25.053  -28.220 1.00 20.36 ? 407  TYR B OH  1 
ATOM   5887 N  N   . ASP B 1 408 ? 42.250  27.572  -22.109 1.00 22.61 ? 408  ASP B N   1 
ATOM   5888 C  CA  . ASP B 1 408 ? 43.354  26.610  -21.917 1.00 24.34 ? 408  ASP B CA  1 
ATOM   5889 C  C   . ASP B 1 408 ? 43.022  25.626  -20.791 1.00 23.76 ? 408  ASP B C   1 
ATOM   5890 O  O   . ASP B 1 408 ? 43.285  24.440  -20.924 1.00 23.71 ? 408  ASP B O   1 
ATOM   5891 C  CB  . ASP B 1 408 ? 44.695  27.310  -21.611 1.00 25.43 ? 408  ASP B CB  1 
ATOM   5892 C  CG  . ASP B 1 408 ? 45.330  27.960  -22.849 1.00 28.60 ? 408  ASP B CG  1 
ATOM   5893 O  OD1 . ASP B 1 408 ? 44.985  27.579  -23.983 1.00 28.69 ? 408  ASP B OD1 1 
ATOM   5894 O  OD2 . ASP B 1 408 ? 46.189  28.855  -22.686 1.00 31.41 ? 408  ASP B OD2 1 
ATOM   5895 N  N   . GLN B 1 409 ? 42.448  26.122  -19.695 1.00 23.68 ? 409  GLN B N   1 
ATOM   5896 C  CA  . GLN B 1 409 ? 42.070  25.257  -18.558 1.00 24.00 ? 409  GLN B CA  1 
ATOM   5897 C  C   . GLN B 1 409 ? 41.011  24.254  -18.980 1.00 24.59 ? 409  GLN B C   1 
ATOM   5898 O  O   . GLN B 1 409 ? 41.104  23.057  -18.675 1.00 24.55 ? 409  GLN B O   1 
ATOM   5899 C  CB  . GLN B 1 409 ? 41.536  26.066  -17.382 1.00 22.89 ? 409  GLN B CB  1 
ATOM   5900 C  CG  . GLN B 1 409 ? 42.589  26.850  -16.631 1.00 23.22 ? 409  GLN B CG  1 
ATOM   5901 C  CD  . GLN B 1 409 ? 41.977  27.786  -15.608 1.00 24.36 ? 409  GLN B CD  1 
ATOM   5902 O  OE1 . GLN B 1 409 ? 40.955  28.432  -15.875 1.00 22.95 ? 409  GLN B OE1 1 
ATOM   5903 N  NE2 . GLN B 1 409 ? 42.581  27.852  -14.419 1.00 24.13 ? 409  GLN B NE2 1 
ATOM   5904 N  N   . TRP B 1 410 ? 40.004  24.755  -19.689 1.00 24.12 ? 410  TRP B N   1 
ATOM   5905 C  CA  . TRP B 1 410 ? 38.937  23.908  -20.189 1.00 23.36 ? 410  TRP B CA  1 
ATOM   5906 C  C   . TRP B 1 410 ? 39.535  22.822  -21.079 1.00 24.18 ? 410  TRP B C   1 
ATOM   5907 O  O   . TRP B 1 410 ? 39.235  21.635  -20.923 1.00 24.56 ? 410  TRP B O   1 
ATOM   5908 C  CB  . TRP B 1 410 ? 37.926  24.747  -20.971 1.00 22.13 ? 410  TRP B CB  1 
ATOM   5909 C  CG  . TRP B 1 410 ? 36.894  23.921  -21.647 1.00 22.31 ? 410  TRP B CG  1 
ATOM   5910 C  CD1 . TRP B 1 410 ? 35.776  23.380  -21.083 1.00 21.93 ? 410  TRP B CD1 1 
ATOM   5911 C  CD2 . TRP B 1 410 ? 36.881  23.536  -23.015 1.00 22.29 ? 410  TRP B CD2 1 
ATOM   5912 N  NE1 . TRP B 1 410 ? 35.065  22.686  -22.021 1.00 22.71 ? 410  TRP B NE1 1 
ATOM   5913 C  CE2 . TRP B 1 410 ? 35.722  22.763  -23.218 1.00 22.94 ? 410  TRP B CE2 1 
ATOM   5914 C  CE3 . TRP B 1 410 ? 37.728  23.784  -24.096 1.00 22.51 ? 410  TRP B CE3 1 
ATOM   5915 C  CZ2 . TRP B 1 410 ? 35.393  22.222  -24.457 1.00 23.85 ? 410  TRP B CZ2 1 
ATOM   5916 C  CZ3 . TRP B 1 410 ? 37.415  23.242  -25.322 1.00 23.60 ? 410  TRP B CZ3 1 
ATOM   5917 C  CH2 . TRP B 1 410 ? 36.256  22.469  -25.498 1.00 24.59 ? 410  TRP B CH2 1 
ATOM   5918 N  N   . LYS B 1 411 ? 40.381  23.246  -22.005 1.00 24.33 ? 411  LYS B N   1 
ATOM   5919 C  CA  . LYS B 1 411 ? 40.993  22.337  -22.969 1.00 26.14 ? 411  LYS B CA  1 
ATOM   5920 C  C   . LYS B 1 411 ? 41.809  21.252  -22.279 1.00 25.84 ? 411  LYS B C   1 
ATOM   5921 O  O   . LYS B 1 411 ? 41.721  20.080  -22.637 1.00 23.30 ? 411  LYS B O   1 
ATOM   5922 C  CB  . LYS B 1 411 ? 41.897  23.102  -23.945 1.00 27.13 ? 411  LYS B CB  1 
ATOM   5923 C  CG  . LYS B 1 411 ? 42.248  22.287  -25.172 1.00 29.28 ? 411  LYS B CG  1 
ATOM   5924 C  CD  . LYS B 1 411 ? 42.957  23.095  -26.240 1.00 31.39 ? 411  LYS B CD  1 
ATOM   5925 C  CE  . LYS B 1 411 ? 43.415  22.176  -27.370 1.00 33.42 ? 411  LYS B CE  1 
ATOM   5926 N  NZ  . LYS B 1 411 ? 44.294  22.867  -28.349 1.00 34.33 ? 411  LYS B NZ  1 
ATOM   5927 N  N   . ALA B 1 412 ? 42.590  21.661  -21.284 1.00 26.01 ? 412  ALA B N   1 
ATOM   5928 C  CA  . ALA B 1 412 ? 43.468  20.748  -20.576 1.00 27.74 ? 412  ALA B CA  1 
ATOM   5929 C  C   . ALA B 1 412 ? 42.709  19.527  -20.051 1.00 28.79 ? 412  ALA B C   1 
ATOM   5930 O  O   . ALA B 1 412 ? 43.191  18.422  -20.193 1.00 30.45 ? 412  ALA B O   1 
ATOM   5931 C  CB  . ALA B 1 412 ? 44.175  21.466  -19.434 1.00 28.15 ? 412  ALA B CB  1 
ATOM   5932 N  N   . THR B 1 413 ? 41.518  19.720  -19.474 1.00 29.96 ? 413  THR B N   1 
ATOM   5933 C  CA  . THR B 1 413 ? 40.801  18.620  -18.807 1.00 29.92 ? 413  THR B CA  1 
ATOM   5934 C  C   . THR B 1 413 ? 39.615  18.040  -19.578 1.00 30.45 ? 413  THR B C   1 
ATOM   5935 O  O   . THR B 1 413 ? 39.157  16.958  -19.246 1.00 31.59 ? 413  THR B O   1 
ATOM   5936 C  CB  . THR B 1 413 ? 40.335  19.020  -17.384 1.00 30.93 ? 413  THR B CB  1 
ATOM   5937 O  OG1 . THR B 1 413 ? 39.768  20.336  -17.395 1.00 30.34 ? 413  THR B OG1 1 
ATOM   5938 C  CG2 . THR B 1 413 ? 41.528  18.994  -16.394 1.00 31.26 ? 413  THR B CG2 1 
ATOM   5939 N  N   . ASN B 1 414 ? 39.123  18.714  -20.614 1.00 30.36 ? 414  ASN B N   1 
ATOM   5940 C  CA  . ASN B 1 414 ? 37.856  18.294  -21.194 1.00 31.73 ? 414  ASN B CA  1 
ATOM   5941 C  C   . ASN B 1 414 ? 37.934  16.941  -21.912 1.00 32.51 ? 414  ASN B C   1 
ATOM   5942 O  O   . ASN B 1 414 ? 38.773  16.742  -22.782 1.00 32.69 ? 414  ASN B O   1 
ATOM   5943 C  CB  . ASN B 1 414 ? 37.302  19.342  -22.154 1.00 31.05 ? 414  ASN B CB  1 
ATOM   5944 C  CG  . ASN B 1 414 ? 35.906  18.992  -22.639 1.00 30.53 ? 414  ASN B CG  1 
ATOM   5945 O  OD1 . ASN B 1 414 ? 35.024  18.651  -21.845 1.00 28.31 ? 414  ASN B OD1 1 
ATOM   5946 N  ND2 . ASN B 1 414 ? 35.707  19.036  -23.948 1.00 31.85 ? 414  ASN B ND2 1 
ATOM   5947 N  N   . LYS B 1 415 ? 37.055  16.029  -21.518 1.00 33.42 ? 415  LYS B N   1 
ATOM   5948 C  CA  . LYS B 1 415 ? 36.858  14.764  -22.208 1.00 35.74 ? 415  LYS B CA  1 
ATOM   5949 C  C   . LYS B 1 415 ? 35.426  14.650  -22.747 1.00 34.45 ? 415  LYS B C   1 
ATOM   5950 O  O   . LYS B 1 415 ? 35.007  13.573  -23.178 1.00 35.10 ? 415  LYS B O   1 
ATOM   5951 C  CB  . LYS B 1 415 ? 37.196  13.599  -21.270 1.00 39.30 ? 415  LYS B CB  1 
ATOM   5952 C  CG  . LYS B 1 415 ? 38.693  13.456  -21.023 1.00 42.21 ? 415  LYS B CG  1 
ATOM   5953 C  CD  . LYS B 1 415 ? 39.386  12.755  -22.187 1.00 46.25 ? 415  LYS B CD  1 
ATOM   5954 C  CE  . LYS B 1 415 ? 40.737  13.377  -22.532 1.00 49.11 ? 415  LYS B CE  1 
ATOM   5955 N  NZ  . LYS B 1 415 ? 41.646  13.483  -21.352 1.00 51.66 ? 415  LYS B NZ  1 
ATOM   5956 N  N   . GLY B 1 416 ? 34.692  15.767  -22.745 1.00 30.81 ? 416  GLY B N   1 
ATOM   5957 C  CA  . GLY B 1 416 ? 33.352  15.827  -23.328 1.00 28.85 ? 416  GLY B CA  1 
ATOM   5958 C  C   . GLY B 1 416 ? 32.263  16.220  -22.340 1.00 28.08 ? 416  GLY B C   1 
ATOM   5959 O  O   . GLY B 1 416 ? 31.115  16.434  -22.739 1.00 28.76 ? 416  GLY B O   1 
ATOM   5960 N  N   . ALA B 1 417 ? 32.598  16.318  -21.055 1.00 25.94 ? 417  ALA B N   1 
ATOM   5961 C  CA  . ALA B 1 417 ? 31.587  16.643  -20.037 1.00 25.38 ? 417  ALA B CA  1 
ATOM   5962 C  C   . ALA B 1 417 ? 31.642  18.094  -19.536 1.00 23.78 ? 417  ALA B C   1 
ATOM   5963 O  O   . ALA B 1 417 ? 30.764  18.518  -18.773 1.00 23.75 ? 417  ALA B O   1 
ATOM   5964 C  CB  . ALA B 1 417 ? 31.682  15.674  -18.868 1.00 25.25 ? 417  ALA B CB  1 
ATOM   5965 N  N   . ASP B 1 418 ? 32.632  18.871  -19.962 1.00 21.30 ? 418  ASP B N   1 
ATOM   5966 C  CA  . ASP B 1 418 ? 32.773  20.195  -19.376 1.00 20.89 ? 418  ASP B CA  1 
ATOM   5967 C  C   . ASP B 1 418 ? 32.269  21.269  -20.331 1.00 20.30 ? 418  ASP B C   1 
ATOM   5968 O  O   . ASP B 1 418 ? 32.611  21.271  -21.515 1.00 19.09 ? 418  ASP B O   1 
ATOM   5969 C  CB  . ASP B 1 418 ? 34.217  20.475  -18.979 1.00 19.98 ? 418  ASP B CB  1 
ATOM   5970 C  CG  . ASP B 1 418 ? 34.348  21.641  -17.991 1.00 19.86 ? 418  ASP B CG  1 
ATOM   5971 O  OD1 . ASP B 1 418 ? 33.358  22.005  -17.298 1.00 19.28 ? 418  ASP B OD1 1 
ATOM   5972 O  OD2 . ASP B 1 418 ? 35.469  22.176  -17.881 1.00 18.77 ? 418  ASP B OD2 1 
ATOM   5973 N  N   . ASN B 1 419 ? 31.480  22.195  -19.802 1.00 18.82 ? 419  ASN B N   1 
ATOM   5974 C  CA  . ASN B 1 419 ? 30.984  23.292  -20.610 1.00 19.04 ? 419  ASN B CA  1 
ATOM   5975 C  C   . ASN B 1 419 ? 32.089  24.328  -20.722 1.00 19.19 ? 419  ASN B C   1 
ATOM   5976 O  O   . ASN B 1 419 ? 32.938  24.429  -19.856 1.00 19.77 ? 419  ASN B O   1 
ATOM   5977 C  CB  . ASN B 1 419 ? 29.729  23.919  -19.985 1.00 18.77 ? 419  ASN B CB  1 
ATOM   5978 C  CG  . ASN B 1 419 ? 28.909  24.747  -20.984 1.00 19.39 ? 419  ASN B CG  1 
ATOM   5979 O  OD1 . ASN B 1 419 ? 28.985  24.547  -22.194 1.00 19.67 ? 419  ASN B OD1 1 
ATOM   5980 N  ND2 . ASN B 1 419 ? 28.112  25.674  -20.471 1.00 18.81 ? 419  ASN B ND2 1 
ATOM   5981 N  N   . ILE B 1 420 ? 32.060  25.101  -21.790 1.00 19.36 ? 420  ILE B N   1 
ATOM   5982 C  CA  . ILE B 1 420 ? 32.889  26.270  -21.902 1.00 20.92 ? 420  ILE B CA  1 
ATOM   5983 C  C   . ILE B 1 420 ? 31.976  27.494  -22.026 1.00 20.20 ? 420  ILE B C   1 
ATOM   5984 O  O   . ILE B 1 420 ? 31.005  27.494  -22.799 1.00 19.22 ? 420  ILE B O   1 
ATOM   5985 C  CB  . ILE B 1 420 ? 33.886  26.173  -23.080 1.00 23.15 ? 420  ILE B CB  1 
ATOM   5986 C  CG1 . ILE B 1 420 ? 34.451  27.558  -23.404 1.00 24.14 ? 420  ILE B CG1 1 
ATOM   5987 C  CG2 . ILE B 1 420 ? 33.244  25.536  -24.305 1.00 23.47 ? 420  ILE B CG2 1 
ATOM   5988 C  CD1 . ILE B 1 420 ? 35.962  27.553  -23.481 1.00 26.87 ? 420  ILE B CD1 1 
ATOM   5989 N  N   . ALA B 1 421 ? 32.285  28.521  -21.236 1.00 19.66 ? 421  ALA B N   1 
ATOM   5990 C  CA  . ALA B 1 421 ? 31.449  29.716  -21.172 1.00 19.47 ? 421  ALA B CA  1 
ATOM   5991 C  C   . ALA B 1 421 ? 32.286  30.945  -20.870 1.00 19.11 ? 421  ALA B C   1 
ATOM   5992 O  O   . ALA B 1 421 ? 32.989  31.002  -19.867 1.00 19.42 ? 421  ALA B O   1 
ATOM   5993 C  CB  . ALA B 1 421 ? 30.373  29.543  -20.111 1.00 19.31 ? 421  ALA B CB  1 
ATOM   5994 N  N   . MET B 1 422 ? 32.220  31.923  -21.761 1.00 18.52 ? 422  MET B N   1 
ATOM   5995 C  CA  . MET B 1 422 ? 32.880  33.203  -21.549 1.00 17.75 ? 422  MET B CA  1 
ATOM   5996 C  C   . MET B 1 422 ? 32.137  34.148  -22.490 1.00 17.42 ? 422  MET B C   1 
ATOM   5997 O  O   . MET B 1 422 ? 32.574  34.394  -23.618 1.00 17.40 ? 422  MET B O   1 
ATOM   5998 C  CB  . MET B 1 422 ? 34.369  33.073  -21.876 1.00 18.09 ? 422  MET B CB  1 
ATOM   5999 C  CG  . MET B 1 422 ? 35.177  34.365  -21.805 1.00 18.19 ? 422  MET B CG  1 
ATOM   6000 S  SD  . MET B 1 422 ? 35.110  35.266  -20.232 1.00 18.90 ? 422  MET B SD  1 
ATOM   6001 C  CE  . MET B 1 422 ? 35.560  33.947  -19.106 1.00 18.88 ? 422  MET B CE  1 
ATOM   6002 N  N   . ARG B 1 423 ? 30.960  34.606  -22.058 1.00 15.92 ? 423  ARG B N   1 
ATOM   6003 C  CA  . ARG B 1 423 ? 30.025  35.206  -23.006 1.00 15.47 ? 423  ARG B CA  1 
ATOM   6004 C  C   . ARG B 1 423 ? 28.974  36.087  -22.349 1.00 14.71 ? 423  ARG B C   1 
ATOM   6005 O  O   . ARG B 1 423 ? 29.001  36.304  -21.131 1.00 14.34 ? 423  ARG B O   1 
ATOM   6006 C  CB  . ARG B 1 423 ? 29.365  34.102  -23.856 1.00 15.38 ? 423  ARG B CB  1 
ATOM   6007 C  CG  . ARG B 1 423 ? 28.411  33.176  -23.121 1.00 15.27 ? 423  ARG B CG  1 
ATOM   6008 C  CD  . ARG B 1 423 ? 27.759  32.234  -24.113 1.00 14.91 ? 423  ARG B CD  1 
ATOM   6009 N  NE  . ARG B 1 423 ? 26.901  31.230  -23.489 1.00 15.59 ? 423  ARG B NE  1 
ATOM   6010 C  CZ  . ARG B 1 423 ? 27.221  29.949  -23.292 1.00 16.80 ? 423  ARG B CZ  1 
ATOM   6011 N  NH1 . ARG B 1 423 ? 28.418  29.471  -23.637 1.00 16.75 ? 423  ARG B NH1 1 
ATOM   6012 N  NH2 . ARG B 1 423 ? 26.325  29.126  -22.752 1.00 17.61 ? 423  ARG B NH2 1 
ATOM   6013 N  N   . ASP B 1 424 ? 28.070  36.615  -23.171 1.00 14.59 ? 424  ASP B N   1 
ATOM   6014 C  CA  . ASP B 1 424 ? 26.859  37.278  -22.688 1.00 14.88 ? 424  ASP B CA  1 
ATOM   6015 C  C   . ASP B 1 424 ? 27.176  38.459  -21.763 1.00 15.15 ? 424  ASP B C   1 
ATOM   6016 O  O   . ASP B 1 424 ? 26.603  38.595  -20.680 1.00 16.29 ? 424  ASP B O   1 
ATOM   6017 C  CB  . ASP B 1 424 ? 25.947  36.261  -21.981 1.00 15.45 ? 424  ASP B CB  1 
ATOM   6018 C  CG  . ASP B 1 424 ? 25.327  35.239  -22.935 1.00 15.65 ? 424  ASP B CG  1 
ATOM   6019 O  OD1 . ASP B 1 424 ? 25.739  35.155  -24.101 1.00 15.47 ? 424  ASP B OD1 1 
ATOM   6020 O  OD2 . ASP B 1 424 ? 24.384  34.527  -22.512 1.00 16.67 ? 424  ASP B OD2 1 
ATOM   6021 N  N   . ALA B 1 425 ? 28.089  39.315  -22.197 1.00 14.93 ? 425  ALA B N   1 
ATOM   6022 C  CA  . ALA B 1 425 ? 28.559  40.405  -21.370 1.00 15.14 ? 425  ALA B CA  1 
ATOM   6023 C  C   . ALA B 1 425 ? 27.518  41.513  -21.347 1.00 14.71 ? 425  ALA B C   1 
ATOM   6024 O  O   . ALA B 1 425 ? 27.169  42.025  -22.399 1.00 13.74 ? 425  ALA B O   1 
ATOM   6025 C  CB  . ALA B 1 425 ? 29.890  40.941  -21.884 1.00 14.76 ? 425  ALA B CB  1 
ATOM   6026 N  N   . HIS B 1 426 ? 27.036  41.842  -20.145 1.00 15.48 ? 426  HIS B N   1 
ATOM   6027 C  CA  . HIS B 1 426 ? 26.111  42.969  -19.896 1.00 16.69 ? 426  HIS B CA  1 
ATOM   6028 C  C   . HIS B 1 426 ? 26.855  44.200  -19.342 1.00 17.52 ? 426  HIS B C   1 
ATOM   6029 O  O   . HIS B 1 426 ? 27.391  44.161  -18.226 1.00 18.16 ? 426  HIS B O   1 
ATOM   6030 C  CB  . HIS B 1 426 ? 25.006  42.578  -18.910 1.00 16.92 ? 426  HIS B CB  1 
ATOM   6031 C  CG  . HIS B 1 426 ? 23.975  43.654  -18.708 1.00 16.90 ? 426  HIS B CG  1 
ATOM   6032 N  ND1 . HIS B 1 426 ? 22.976  43.912  -19.621 1.00 16.41 ? 426  HIS B ND1 1 
ATOM   6033 C  CD2 . HIS B 1 426 ? 23.815  44.559  -17.714 1.00 17.13 ? 426  HIS B CD2 1 
ATOM   6034 C  CE1 . HIS B 1 426 ? 22.254  44.934  -19.202 1.00 16.69 ? 426  HIS B CE1 1 
ATOM   6035 N  NE2 . HIS B 1 426 ? 22.739  45.343  -18.047 1.00 16.49 ? 426  HIS B NE2 1 
ATOM   6036 N  N   . VAL B 1 427 ? 26.889  45.285  -20.114 1.00 17.53 ? 427  VAL B N   1 
ATOM   6037 C  CA  . VAL B 1 427 ? 27.567  46.500  -19.654 1.00 18.46 ? 427  VAL B CA  1 
ATOM   6038 C  C   . VAL B 1 427 ? 26.617  47.405  -18.850 1.00 19.23 ? 427  VAL B C   1 
ATOM   6039 O  O   . VAL B 1 427 ? 25.460  47.592  -19.217 1.00 18.12 ? 427  VAL B O   1 
ATOM   6040 C  CB  . VAL B 1 427 ? 28.244  47.269  -20.814 1.00 18.30 ? 427  VAL B CB  1 
ATOM   6041 C  CG1 . VAL B 1 427 ? 27.223  47.882  -21.759 1.00 18.24 ? 427  VAL B CG1 1 
ATOM   6042 C  CG2 . VAL B 1 427 ? 29.194  48.332  -20.273 1.00 18.49 ? 427  VAL B CG2 1 
ATOM   6043 N  N   . ILE B 1 428 ? 27.117  47.955  -17.747 1.00 20.61 ? 428  ILE B N   1 
ATOM   6044 C  CA  . ILE B 1 428 ? 26.318  48.849  -16.888 1.00 22.12 ? 428  ILE B CA  1 
ATOM   6045 C  C   . ILE B 1 428 ? 27.257  49.805  -16.148 1.00 23.26 ? 428  ILE B C   1 
ATOM   6046 O  O   . ILE B 1 428 ? 28.332  49.395  -15.728 1.00 22.36 ? 428  ILE B O   1 
ATOM   6047 C  CB  . ILE B 1 428 ? 25.448  48.053  -15.888 1.00 22.45 ? 428  ILE B CB  1 
ATOM   6048 C  CG1 . ILE B 1 428 ? 24.716  49.005  -14.929 1.00 23.97 ? 428  ILE B CG1 1 
ATOM   6049 C  CG2 . ILE B 1 428 ? 26.293  47.063  -15.097 1.00 22.85 ? 428  ILE B CG2 1 
ATOM   6050 C  CD1 . ILE B 1 428 ? 23.743  48.342  -13.981 1.00 23.93 ? 428  ILE B CD1 1 
ATOM   6051 N  N   . GLU B 1 429 ? 26.856  51.075  -16.025 1.00 25.09 ? 429  GLU B N   1 
ATOM   6052 C  CA  . GLU B 1 429 ? 27.645  52.095  -15.314 1.00 27.68 ? 429  GLU B CA  1 
ATOM   6053 C  C   . GLU B 1 429 ? 26.986  52.408  -13.970 1.00 28.86 ? 429  GLU B C   1 
ATOM   6054 O  O   . GLU B 1 429 ? 25.777  52.678  -13.911 1.00 29.82 ? 429  GLU B O   1 
ATOM   6055 C  CB  . GLU B 1 429 ? 27.767  53.374  -16.161 1.00 29.59 ? 429  GLU B CB  1 
ATOM   6056 C  CG  . GLU B 1 429 ? 28.628  54.492  -15.568 1.00 30.68 ? 429  GLU B CG  1 
ATOM   6057 C  CD  . GLU B 1 429 ? 28.456  55.829  -16.298 1.00 31.70 ? 429  GLU B CD  1 
ATOM   6058 O  OE1 . GLU B 1 429 ? 28.537  55.872  -17.540 1.00 33.36 ? 429  GLU B OE1 1 
ATOM   6059 O  OE2 . GLU B 1 429 ? 28.231  56.855  -15.631 1.00 34.78 ? 429  GLU B OE2 1 
ATOM   6060 N  N   . ASP B 1 430 ? 27.770  52.376  -12.898 1.00 29.88 ? 430  ASP B N   1 
ATOM   6061 C  CA  . ASP B 1 430 ? 27.249  52.658  -11.554 1.00 32.05 ? 430  ASP B CA  1 
ATOM   6062 C  C   . ASP B 1 430 ? 27.145  54.161  -11.330 1.00 33.26 ? 430  ASP B C   1 
ATOM   6063 O  O   . ASP B 1 430 ? 27.414  54.945  -12.239 1.00 29.98 ? 430  ASP B O   1 
ATOM   6064 C  CB  . ASP B 1 430 ? 28.123  51.986  -10.476 1.00 33.73 ? 430  ASP B CB  1 
ATOM   6065 C  CG  . ASP B 1 430 ? 29.475  52.697  -10.246 1.00 34.44 ? 430  ASP B CG  1 
ATOM   6066 O  OD1 . ASP B 1 430 ? 29.946  53.517  -11.076 1.00 34.84 ? 430  ASP B OD1 1 
ATOM   6067 O  OD2 . ASP B 1 430 ? 30.081  52.421  -9.197  1.00 37.35 ? 430  ASP B OD2 1 
ATOM   6068 N  N   . ASP B 1 431 ? 26.787  54.559  -10.113 1.00 37.68 ? 431  ASP B N   1 
ATOM   6069 C  CA  . ASP B 1 431 ? 26.652  55.984  -9.768  1.00 41.88 ? 431  ASP B CA  1 
ATOM   6070 C  C   . ASP B 1 431 ? 27.991  56.744  -9.719  1.00 41.34 ? 431  ASP B C   1 
ATOM   6071 O  O   . ASP B 1 431 ? 28.013  57.971  -9.828  1.00 38.70 ? 431  ASP B O   1 
ATOM   6072 C  CB  . ASP B 1 431 ? 25.939  56.134  -8.423  1.00 47.56 ? 431  ASP B CB  1 
ATOM   6073 C  CG  . ASP B 1 431 ? 24.577  55.461  -8.405  1.00 52.36 ? 431  ASP B CG  1 
ATOM   6074 O  OD1 . ASP B 1 431 ? 23.973  55.294  -9.489  1.00 58.89 ? 431  ASP B OD1 1 
ATOM   6075 O  OD2 . ASP B 1 431 ? 24.111  55.101  -7.303  1.00 58.29 ? 431  ASP B OD2 1 
ATOM   6076 N  N   . ASN B 1 432 ? 29.100  56.022  -9.568  1.00 39.64 ? 432  ASN B N   1 
ATOM   6077 C  CA  . ASN B 1 432 ? 30.432  56.646  -9.524  1.00 39.68 ? 432  ASN B CA  1 
ATOM   6078 C  C   . ASN B 1 432 ? 31.085  56.937  -10.869 1.00 36.75 ? 432  ASN B C   1 
ATOM   6079 O  O   . ASN B 1 432 ? 32.176  57.484  -10.898 1.00 38.17 ? 432  ASN B O   1 
ATOM   6080 C  CB  . ASN B 1 432 ? 31.366  55.776  -8.702  1.00 42.12 ? 432  ASN B CB  1 
ATOM   6081 C  CG  . ASN B 1 432 ? 30.875  55.609  -7.288  1.00 45.45 ? 432  ASN B CG  1 
ATOM   6082 O  OD1 . ASN B 1 432 ? 30.865  56.567  -6.515  1.00 46.53 ? 432  ASN B OD1 1 
ATOM   6083 N  ND2 . ASN B 1 432 ? 30.427  54.402  -6.950  1.00 46.80 ? 432  ASN B ND2 1 
ATOM   6084 N  N   . GLY B 1 433 ? 30.423  56.581  -11.969 1.00 36.65 ? 433  GLY B N   1 
ATOM   6085 C  CA  . GLY B 1 433 ? 30.982  56.744  -13.319 1.00 35.50 ? 433  GLY B CA  1 
ATOM   6086 C  C   . GLY B 1 433 ? 31.759  55.546  -13.861 1.00 34.28 ? 433  GLY B C   1 
ATOM   6087 O  O   . GLY B 1 433 ? 32.300  55.616  -14.952 1.00 37.00 ? 433  GLY B O   1 
ATOM   6088 N  N   . ASP B 1 434 ? 31.825  54.457  -13.106 1.00 33.88 ? 434  ASP B N   1 
ATOM   6089 C  CA  . ASP B 1 434 ? 32.555  53.244  -13.515 1.00 33.91 ? 434  ASP B CA  1 
ATOM   6090 C  C   . ASP B 1 434 ? 31.654  52.324  -14.362 1.00 31.74 ? 434  ASP B C   1 
ATOM   6091 O  O   . ASP B 1 434 ? 30.585  51.936  -13.894 1.00 30.40 ? 434  ASP B O   1 
ATOM   6092 C  CB  . ASP B 1 434 ? 32.973  52.440  -12.265 1.00 34.41 ? 434  ASP B CB  1 
ATOM   6093 C  CG  . ASP B 1 434 ? 33.928  53.201  -11.338 1.00 36.14 ? 434  ASP B CG  1 
ATOM   6094 O  OD1 . ASP B 1 434 ? 34.790  53.933  -11.846 1.00 36.73 ? 434  ASP B OD1 1 
ATOM   6095 O  OD2 . ASP B 1 434 ? 33.822  53.035  -10.097 1.00 37.40 ? 434  ASP B OD2 1 
ATOM   6096 N  N   . ARG B 1 435 ? 32.074  51.968  -15.579 1.00 29.11 ? 435  ARG B N   1 
ATOM   6097 C  CA  . ARG B 1 435 ? 31.432  50.874  -16.308 1.00 26.93 ? 435  ARG B CA  1 
ATOM   6098 C  C   . ARG B 1 435 ? 31.942  49.504  -15.828 1.00 24.78 ? 435  ARG B C   1 
ATOM   6099 O  O   . ARG B 1 435 ? 33.142  49.293  -15.644 1.00 22.99 ? 435  ARG B O   1 
ATOM   6100 C  CB  . ARG B 1 435 ? 31.625  50.986  -17.820 1.00 27.66 ? 435  ARG B CB  1 
ATOM   6101 C  CG  . ARG B 1 435 ? 30.834  52.103  -18.470 1.00 28.19 ? 435  ARG B CG  1 
ATOM   6102 C  CD  . ARG B 1 435 ? 31.079  52.121  -19.956 1.00 28.42 ? 435  ARG B CD  1 
ATOM   6103 N  NE  . ARG B 1 435 ? 30.301  53.141  -20.658 1.00 29.08 ? 435  ARG B NE  1 
ATOM   6104 C  CZ  . ARG B 1 435 ? 30.251  53.252  -21.985 1.00 31.65 ? 435  ARG B CZ  1 
ATOM   6105 N  NH1 . ARG B 1 435 ? 30.944  52.416  -22.753 1.00 32.03 ? 435  ARG B NH1 1 
ATOM   6106 N  NH2 . ARG B 1 435 ? 29.514  54.206  -22.566 1.00 32.84 ? 435  ARG B NH2 1 
ATOM   6107 N  N   . TYR B 1 436 ? 31.002  48.585  -15.642 1.00 22.78 ? 436  TYR B N   1 
ATOM   6108 C  CA  . TYR B 1 436 ? 31.294  47.175  -15.381 1.00 21.82 ? 436  TYR B CA  1 
ATOM   6109 C  C   . TYR B 1 436 ? 30.691  46.299  -16.477 1.00 20.67 ? 436  TYR B C   1 
ATOM   6110 O  O   . TYR B 1 436 ? 29.709  46.701  -17.113 1.00 19.60 ? 436  TYR B O   1 
ATOM   6111 C  CB  . TYR B 1 436 ? 30.661  46.741  -14.059 1.00 22.09 ? 436  TYR B CB  1 
ATOM   6112 C  CG  . TYR B 1 436 ? 31.186  47.455  -12.840 1.00 23.18 ? 436  TYR B CG  1 
ATOM   6113 C  CD1 . TYR B 1 436 ? 30.884  48.787  -12.608 1.00 23.74 ? 436  TYR B CD1 1 
ATOM   6114 C  CD2 . TYR B 1 436 ? 31.967  46.787  -11.902 1.00 23.65 ? 436  TYR B CD2 1 
ATOM   6115 C  CE1 . TYR B 1 436 ? 31.359  49.442  -11.483 1.00 24.11 ? 436  TYR B CE1 1 
ATOM   6116 C  CE2 . TYR B 1 436 ? 32.449  47.435  -10.775 1.00 24.23 ? 436  TYR B CE2 1 
ATOM   6117 C  CZ  . TYR B 1 436 ? 32.134  48.757  -10.571 1.00 23.76 ? 436  TYR B CZ  1 
ATOM   6118 O  OH  . TYR B 1 436 ? 32.604  49.397  -9.468  1.00 24.35 ? 436  TYR B OH  1 
ATOM   6119 N  N   . LEU B 1 437 ? 31.276  45.107  -16.664 1.00 19.22 ? 437  LEU B N   1 
ATOM   6120 C  CA  . LEU B 1 437 ? 30.653  44.011  -17.386 1.00 19.19 ? 437  LEU B CA  1 
ATOM   6121 C  C   . LEU B 1 437 ? 30.278  42.917  -16.395 1.00 18.96 ? 437  LEU B C   1 
ATOM   6122 O  O   . LEU B 1 437 ? 31.092  42.502  -15.556 1.00 19.13 ? 437  LEU B O   1 
ATOM   6123 C  CB  . LEU B 1 437 ? 31.574  43.385  -18.442 1.00 18.63 ? 437  LEU B CB  1 
ATOM   6124 C  CG  . LEU B 1 437 ? 32.153  44.283  -19.534 1.00 18.80 ? 437  LEU B CG  1 
ATOM   6125 C  CD1 . LEU B 1 437 ? 32.994  43.463  -20.504 1.00 18.25 ? 437  LEU B CD1 1 
ATOM   6126 C  CD2 . LEU B 1 437 ? 31.044  45.032  -20.247 1.00 18.09 ? 437  LEU B CD2 1 
ATOM   6127 N  N   . VAL B 1 438 ? 29.036  42.464  -16.508 1.00 18.30 ? 438  VAL B N   1 
ATOM   6128 C  CA  . VAL B 1 438 ? 28.530  41.314  -15.780 1.00 16.90 ? 438  VAL B CA  1 
ATOM   6129 C  C   . VAL B 1 438 ? 28.270  40.276  -16.871 1.00 16.30 ? 438  VAL B C   1 
ATOM   6130 O  O   . VAL B 1 438 ? 27.609  40.576  -17.866 1.00 15.78 ? 438  VAL B O   1 
ATOM   6131 C  CB  . VAL B 1 438 ? 27.263  41.706  -15.016 1.00 16.75 ? 438  VAL B CB  1 
ATOM   6132 C  CG1 . VAL B 1 438 ? 26.589  40.488  -14.408 1.00 16.50 ? 438  VAL B CG1 1 
ATOM   6133 C  CG2 . VAL B 1 438 ? 27.606  42.733  -13.942 1.00 16.58 ? 438  VAL B CG2 1 
ATOM   6134 N  N   . PHE B 1 439 ? 28.824  39.076  -16.710 1.00 16.52 ? 439  PHE B N   1 
ATOM   6135 C  CA  . PHE B 1 439 ? 28.914  38.110  -17.805 1.00 15.89 ? 439  PHE B CA  1 
ATOM   6136 C  C   . PHE B 1 439 ? 28.781  36.641  -17.362 1.00 15.83 ? 439  PHE B C   1 
ATOM   6137 O  O   . PHE B 1 439 ? 28.884  36.300  -16.175 1.00 15.35 ? 439  PHE B O   1 
ATOM   6138 C  CB  . PHE B 1 439 ? 30.239  38.321  -18.548 1.00 16.17 ? 439  PHE B CB  1 
ATOM   6139 C  CG  . PHE B 1 439 ? 31.450  38.198  -17.664 1.00 16.56 ? 439  PHE B CG  1 
ATOM   6140 C  CD1 . PHE B 1 439 ? 31.897  39.292  -16.919 1.00 16.73 ? 439  PHE B CD1 1 
ATOM   6141 C  CD2 . PHE B 1 439 ? 32.116  37.001  -17.545 1.00 16.44 ? 439  PHE B CD2 1 
ATOM   6142 C  CE1 . PHE B 1 439 ? 33.003  39.187  -16.100 1.00 16.59 ? 439  PHE B CE1 1 
ATOM   6143 C  CE2 . PHE B 1 439 ? 33.232  36.896  -16.731 1.00 16.51 ? 439  PHE B CE2 1 
ATOM   6144 C  CZ  . PHE B 1 439 ? 33.669  37.982  -16.002 1.00 16.14 ? 439  PHE B CZ  1 
ATOM   6145 N  N   . GLU B 1 440 ? 28.531  35.784  -18.339 1.00 15.46 ? 440  GLU B N   1 
ATOM   6146 C  CA  . GLU B 1 440 ? 28.456  34.362  -18.110 1.00 16.47 ? 440  GLU B CA  1 
ATOM   6147 C  C   . GLU B 1 440 ? 29.865  33.756  -18.210 1.00 16.28 ? 440  GLU B C   1 
ATOM   6148 O  O   . GLU B 1 440 ? 30.562  33.931  -19.204 1.00 16.52 ? 440  GLU B O   1 
ATOM   6149 C  CB  . GLU B 1 440 ? 27.521  33.683  -19.122 1.00 16.89 ? 440  GLU B CB  1 
ATOM   6150 C  CG  . GLU B 1 440 ? 27.575  32.167  -19.051 1.00 17.36 ? 440  GLU B CG  1 
ATOM   6151 C  CD  . GLU B 1 440 ? 26.589  31.458  -19.956 1.00 17.94 ? 440  GLU B CD  1 
ATOM   6152 O  OE1 . GLU B 1 440 ? 25.887  32.140  -20.725 1.00 18.22 ? 440  GLU B OE1 1 
ATOM   6153 O  OE2 . GLU B 1 440 ? 26.513  30.199  -19.883 1.00 17.97 ? 440  GLU B OE2 1 
ATOM   6154 N  N   . ALA B 1 441 ? 30.282  33.077  -17.156 1.00 16.25 ? 441  ALA B N   1 
ATOM   6155 C  CA  . ALA B 1 441 ? 31.541  32.324  -17.173 1.00 17.37 ? 441  ALA B CA  1 
ATOM   6156 C  C   . ALA B 1 441 ? 31.400  31.036  -16.349 1.00 16.75 ? 441  ALA B C   1 
ATOM   6157 O  O   . ALA B 1 441 ? 30.288  30.629  -16.000 1.00 16.00 ? 441  ALA B O   1 
ATOM   6158 C  CB  . ALA B 1 441 ? 32.684  33.190  -16.646 1.00 17.29 ? 441  ALA B CB  1 
ATOM   6159 N  N   . SER B 1 442 ? 32.534  30.396  -16.100 1.00 17.28 ? 442  SER B N   1 
ATOM   6160 C  CA  . SER B 1 442 ? 32.665  29.326  -15.115 1.00 17.49 ? 442  SER B CA  1 
ATOM   6161 C  C   . SER B 1 442 ? 33.725  29.770  -14.120 1.00 17.77 ? 442  SER B C   1 
ATOM   6162 O  O   . SER B 1 442 ? 34.587  30.579  -14.460 1.00 18.03 ? 442  SER B O   1 
ATOM   6163 C  CB  . SER B 1 442 ? 33.124  28.027  -15.773 1.00 17.46 ? 442  SER B CB  1 
ATOM   6164 O  OG  . SER B 1 442 ? 32.336  27.668  -16.881 1.00 16.26 ? 442  SER B OG  1 
ATOM   6165 N  N   . THR B 1 443 ? 33.678  29.247  -12.895 1.00 18.22 ? 443  THR B N   1 
ATOM   6166 C  CA  . THR B 1 443 ? 34.670  29.633  -11.884 1.00 18.94 ? 443  THR B CA  1 
ATOM   6167 C  C   . THR B 1 443 ? 36.055  29.119  -12.261 1.00 19.27 ? 443  THR B C   1 
ATOM   6168 O  O   . THR B 1 443 ? 36.183  28.147  -12.999 1.00 19.18 ? 443  THR B O   1 
ATOM   6169 C  CB  . THR B 1 443 ? 34.325  29.114  -10.479 1.00 19.08 ? 443  THR B CB  1 
ATOM   6170 O  OG1 . THR B 1 443 ? 34.431  27.681  -10.443 1.00 18.25 ? 443  THR B OG1 1 
ATOM   6171 C  CG2 . THR B 1 443 ? 32.934  29.560  -10.085 1.00 19.74 ? 443  THR B CG2 1 
ATOM   6172 N  N   . GLY B 1 444 ? 37.083  29.799  -11.762 1.00 20.21 ? 444  GLY B N   1 
ATOM   6173 C  CA  . GLY B 1 444 ? 38.463  29.377  -11.948 1.00 20.50 ? 444  GLY B CA  1 
ATOM   6174 C  C   . GLY B 1 444 ? 38.979  28.773  -10.653 1.00 21.49 ? 444  GLY B C   1 
ATOM   6175 O  O   . GLY B 1 444 ? 38.193  28.343  -9.812  1.00 20.68 ? 444  GLY B O   1 
ATOM   6176 N  N   . LEU B 1 445 ? 40.302  28.780  -10.477 1.00 23.45 ? 445  LEU B N   1 
ATOM   6177 C  CA  . LEU B 1 445 ? 40.939  28.113  -9.331  1.00 23.58 ? 445  LEU B CA  1 
ATOM   6178 C  C   . LEU B 1 445 ? 40.550  28.704  -7.976  1.00 23.24 ? 445  LEU B C   1 
ATOM   6179 O  O   . LEU B 1 445 ? 40.862  28.117  -6.955  1.00 21.65 ? 445  LEU B O   1 
ATOM   6180 C  CB  . LEU B 1 445 ? 42.467  28.087  -9.494  1.00 24.56 ? 445  LEU B CB  1 
ATOM   6181 C  CG  . LEU B 1 445 ? 43.011  27.270  -10.680 1.00 25.80 ? 445  LEU B CG  1 
ATOM   6182 C  CD1 . LEU B 1 445 ? 44.514  27.442  -10.854 1.00 26.32 ? 445  LEU B CD1 1 
ATOM   6183 C  CD2 . LEU B 1 445 ? 42.672  25.804  -10.521 1.00 26.30 ? 445  LEU B CD2 1 
ATOM   6184 N  N   . GLU B 1 446 ? 39.876  29.857  -7.961  1.00 22.70 ? 446  GLU B N   1 
ATOM   6185 C  CA  . GLU B 1 446 ? 39.295  30.392  -6.721  1.00 22.35 ? 446  GLU B CA  1 
ATOM   6186 C  C   . GLU B 1 446 ? 38.336  29.406  -6.040  1.00 22.10 ? 446  GLU B C   1 
ATOM   6187 O  O   . GLU B 1 446 ? 38.271  29.360  -4.815  1.00 22.41 ? 446  GLU B O   1 
ATOM   6188 C  CB  . GLU B 1 446 ? 38.561  31.708  -6.981  1.00 22.57 ? 446  GLU B CB  1 
ATOM   6189 C  CG  . GLU B 1 446 ? 37.925  32.312  -5.725  1.00 22.79 ? 446  GLU B CG  1 
ATOM   6190 C  CD  . GLU B 1 446 ? 37.230  33.631  -5.975  1.00 22.84 ? 446  GLU B CD  1 
ATOM   6191 O  OE1 . GLU B 1 446 ? 36.528  33.757  -6.994  1.00 22.47 ? 446  GLU B OE1 1 
ATOM   6192 O  OE2 . GLU B 1 446 ? 37.376  34.547  -5.138  1.00 24.44 ? 446  GLU B OE2 1 
ATOM   6193 N  N   . ASN B 1 447 ? 37.575  28.656  -6.834  1.00 20.54 ? 447  ASN B N   1 
ATOM   6194 C  CA  . ASN B 1 447 ? 36.639  27.645  -6.317  1.00 20.76 ? 447  ASN B CA  1 
ATOM   6195 C  C   . ASN B 1 447 ? 36.228  26.772  -7.484  1.00 20.30 ? 447  ASN B C   1 
ATOM   6196 O  O   . ASN B 1 447 ? 35.107  26.858  -8.008  1.00 20.55 ? 447  ASN B O   1 
ATOM   6197 C  CB  . ASN B 1 447 ? 35.403  28.274  -5.652  1.00 20.44 ? 447  ASN B CB  1 
ATOM   6198 C  CG  . ASN B 1 447 ? 34.501  27.238  -4.979  1.00 20.65 ? 447  ASN B CG  1 
ATOM   6199 O  OD1 . ASN B 1 447 ? 34.949  26.169  -4.568  1.00 21.38 ? 447  ASN B OD1 1 
ATOM   6200 N  ND2 . ASN B 1 447 ? 33.221  27.553  -4.866  1.00 20.06 ? 447  ASN B ND2 1 
ATOM   6201 N  N   . TYR B 1 448 ? 37.163  25.940  -7.897  1.00 19.46 ? 448  TYR B N   1 
ATOM   6202 C  CA  . TYR B 1 448 ? 37.082  25.306  -9.179  1.00 20.36 ? 448  TYR B CA  1 
ATOM   6203 C  C   . TYR B 1 448 ? 36.187  24.074  -9.157  1.00 20.58 ? 448  TYR B C   1 
ATOM   6204 O  O   . TYR B 1 448 ? 35.905  23.520  -8.103  1.00 21.04 ? 448  TYR B O   1 
ATOM   6205 C  CB  . TYR B 1 448 ? 38.489  24.948  -9.612  1.00 20.94 ? 448  TYR B CB  1 
ATOM   6206 C  CG  . TYR B 1 448 ? 38.648  24.765  -11.089 1.00 21.76 ? 448  TYR B CG  1 
ATOM   6207 C  CD1 . TYR B 1 448 ? 38.153  25.711  -11.984 1.00 22.12 ? 448  TYR B CD1 1 
ATOM   6208 C  CD2 . TYR B 1 448 ? 39.310  23.652  -11.599 1.00 21.91 ? 448  TYR B CD2 1 
ATOM   6209 C  CE1 . TYR B 1 448 ? 38.320  25.548  -13.344 1.00 22.29 ? 448  TYR B CE1 1 
ATOM   6210 C  CE2 . TYR B 1 448 ? 39.490  23.491  -12.957 1.00 22.74 ? 448  TYR B CE2 1 
ATOM   6211 C  CZ  . TYR B 1 448 ? 38.983  24.441  -13.823 1.00 22.20 ? 448  TYR B CZ  1 
ATOM   6212 O  OH  . TYR B 1 448 ? 39.147  24.286  -15.177 1.00 22.51 ? 448  TYR B OH  1 
ATOM   6213 N  N   . GLN B 1 449 ? 35.705  23.681  -10.329 1.00 20.88 ? 449  GLN B N   1 
ATOM   6214 C  CA  . GLN B 1 449 ? 35.024  22.406  -10.501 1.00 20.81 ? 449  GLN B CA  1 
ATOM   6215 C  C   . GLN B 1 449 ? 35.882  21.233  -10.064 1.00 21.39 ? 449  GLN B C   1 
ATOM   6216 O  O   . GLN B 1 449 ? 37.089  21.343  -9.993  1.00 21.06 ? 449  GLN B O   1 
ATOM   6217 C  CB  . GLN B 1 449 ? 34.675  22.194  -11.961 1.00 20.59 ? 449  GLN B CB  1 
ATOM   6218 C  CG  . GLN B 1 449 ? 35.888  22.109  -12.877 1.00 20.86 ? 449  GLN B CG  1 
ATOM   6219 C  CD  . GLN B 1 449 ? 35.541  22.257  -14.347 1.00 20.71 ? 449  GLN B CD  1 
ATOM   6220 O  OE1 . GLN B 1 449 ? 34.510  22.855  -14.734 1.00 20.71 ? 449  GLN B OE1 1 
ATOM   6221 N  NE2 . GLN B 1 449 ? 36.413  21.738  -15.182 1.00 21.31 ? 449  GLN B NE2 1 
ATOM   6222 N  N   . GLY B 1 450 ? 35.236  20.102  -9.818  1.00 22.25 ? 450  GLY B N   1 
ATOM   6223 C  CA  . GLY B 1 450 ? 35.920  18.876  -9.419  1.00 22.68 ? 450  GLY B CA  1 
ATOM   6224 C  C   . GLY B 1 450 ? 34.996  17.982  -8.612  1.00 23.14 ? 450  GLY B C   1 
ATOM   6225 O  O   . GLY B 1 450 ? 33.964  18.443  -8.088  1.00 22.40 ? 450  GLY B O   1 
ATOM   6226 N  N   . GLU B 1 451 ? 35.365  16.703  -8.509  1.00 23.67 ? 451  GLU B N   1 
ATOM   6227 C  CA  . GLU B 1 451 ? 34.643  15.758  -7.663  1.00 25.35 ? 451  GLU B CA  1 
ATOM   6228 C  C   . GLU B 1 451 ? 34.612  16.240  -6.211  1.00 24.04 ? 451  GLU B C   1 
ATOM   6229 O  O   . GLU B 1 451 ? 33.669  15.951  -5.472  1.00 25.43 ? 451  GLU B O   1 
ATOM   6230 C  CB  . GLU B 1 451 ? 35.259  14.339  -7.768  1.00 28.31 ? 451  GLU B CB  1 
ATOM   6231 C  CG  . GLU B 1 451 ? 34.454  13.239  -7.072  1.00 29.64 ? 451  GLU B CG  1 
ATOM   6232 C  CD  . GLU B 1 451 ? 35.109  11.855  -7.155  1.00 33.03 ? 451  GLU B CD  1 
ATOM   6233 O  OE1 . GLU B 1 451 ? 35.991  11.660  -8.014  1.00 36.26 ? 451  GLU B OE1 1 
ATOM   6234 O  OE2 . GLU B 1 451 ? 34.737  10.956  -6.364  1.00 33.60 ? 451  GLU B OE2 1 
ATOM   6235 N  N   . ASP B 1 452 ? 35.626  16.990  -5.801  1.00 23.44 ? 452  ASP B N   1 
ATOM   6236 C  CA  . ASP B 1 452 ? 35.642  17.549  -4.445  1.00 24.20 ? 452  ASP B CA  1 
ATOM   6237 C  C   . ASP B 1 452 ? 34.452  18.429  -4.127  1.00 21.95 ? 452  ASP B C   1 
ATOM   6238 O  O   . ASP B 1 452 ? 34.062  18.535  -2.966  1.00 20.10 ? 452  ASP B O   1 
ATOM   6239 C  CB  . ASP B 1 452 ? 36.908  18.352  -4.203  1.00 26.18 ? 452  ASP B CB  1 
ATOM   6240 C  CG  . ASP B 1 452 ? 38.112  17.478  -3.943  1.00 28.91 ? 452  ASP B CG  1 
ATOM   6241 O  OD1 . ASP B 1 452 ? 37.968  16.257  -3.660  1.00 31.45 ? 452  ASP B OD1 1 
ATOM   6242 O  OD2 . ASP B 1 452 ? 39.217  18.038  -4.016  1.00 32.11 ? 452  ASP B OD2 1 
ATOM   6243 N  N   . GLN B 1 453 ? 33.878  19.075  -5.144  1.00 20.11 ? 453  GLN B N   1 
ATOM   6244 C  CA  . GLN B 1 453 ? 32.708  19.906  -4.912  1.00 19.09 ? 453  GLN B CA  1 
ATOM   6245 C  C   . GLN B 1 453 ? 31.529  19.093  -4.380  1.00 18.70 ? 453  GLN B C   1 
ATOM   6246 O  O   . GLN B 1 453 ? 30.680  19.647  -3.669  1.00 18.34 ? 453  GLN B O   1 
ATOM   6247 C  CB  . GLN B 1 453 ? 32.311  20.679  -6.169  1.00 18.58 ? 453  GLN B CB  1 
ATOM   6248 C  CG  . GLN B 1 453 ? 33.319  21.743  -6.573  1.00 18.49 ? 453  GLN B CG  1 
ATOM   6249 C  CD  . GLN B 1 453 ? 33.410  22.892  -5.587  1.00 18.78 ? 453  GLN B CD  1 
ATOM   6250 O  OE1 . GLN B 1 453 ? 32.630  22.989  -4.641  1.00 18.27 ? 453  GLN B OE1 1 
ATOM   6251 N  NE2 . GLN B 1 453 ? 34.369  23.778  -5.806  1.00 19.52 ? 453  GLN B NE2 1 
ATOM   6252 N  N   . ILE B 1 454 ? 31.474  17.797  -4.700  1.00 17.92 ? 454  ILE B N   1 
ATOM   6253 C  CA  . ILE B 1 454 ? 30.448  16.924  -4.123  1.00 19.35 ? 454  ILE B CA  1 
ATOM   6254 C  C   . ILE B 1 454 ? 30.599  16.843  -2.601  1.00 20.11 ? 454  ILE B C   1 
ATOM   6255 O  O   . ILE B 1 454 ? 29.624  16.682  -1.875  1.00 21.17 ? 454  ILE B O   1 
ATOM   6256 C  CB  . ILE B 1 454 ? 30.494  15.505  -4.714  1.00 19.58 ? 454  ILE B CB  1 
ATOM   6257 C  CG1 . ILE B 1 454 ? 30.175  15.545  -6.208  1.00 19.94 ? 454  ILE B CG1 1 
ATOM   6258 C  CG2 . ILE B 1 454 ? 29.504  14.590  -4.008  1.00 19.86 ? 454  ILE B CG2 1 
ATOM   6259 C  CD1 . ILE B 1 454 ? 30.368  14.212  -6.892  1.00 20.13 ? 454  ILE B CD1 1 
ATOM   6260 N  N   . TYR B 1 455 ? 31.827  16.975  -2.127  1.00 20.38 ? 455  TYR B N   1 
ATOM   6261 C  CA  . TYR B 1 455 ? 32.112  16.872  -0.713  1.00 22.21 ? 455  TYR B CA  1 
ATOM   6262 C  C   . TYR B 1 455 ? 32.318  18.225  -0.044  1.00 21.58 ? 455  TYR B C   1 
ATOM   6263 O  O   . TYR B 1 455 ? 33.025  18.317  0.951   1.00 21.34 ? 455  TYR B O   1 
ATOM   6264 C  CB  . TYR B 1 455 ? 33.324  15.966  -0.524  1.00 22.23 ? 455  TYR B CB  1 
ATOM   6265 C  CG  . TYR B 1 455 ? 33.104  14.588  -1.116  1.00 22.34 ? 455  TYR B CG  1 
ATOM   6266 C  CD1 . TYR B 1 455 ? 32.391  13.620  -0.418  1.00 21.99 ? 455  TYR B CD1 1 
ATOM   6267 C  CD2 . TYR B 1 455 ? 33.601  14.253  -2.373  1.00 22.86 ? 455  TYR B CD2 1 
ATOM   6268 C  CE1 . TYR B 1 455 ? 32.188  12.352  -0.946  1.00 21.30 ? 455  TYR B CE1 1 
ATOM   6269 C  CE2 . TYR B 1 455 ? 33.412  12.983  -2.910  1.00 22.60 ? 455  TYR B CE2 1 
ATOM   6270 C  CZ  . TYR B 1 455 ? 32.699  12.037  -2.183  1.00 22.06 ? 455  TYR B CZ  1 
ATOM   6271 O  OH  . TYR B 1 455 ? 32.502  10.778  -2.694  1.00 21.79 ? 455  TYR B OH  1 
ATOM   6272 N  N   . ASN B 1 456 ? 31.692  19.270  -0.593  1.00 22.10 ? 456  ASN B N   1 
ATOM   6273 C  CA  . ASN B 1 456 ? 31.637  20.575  0.058   1.00 22.94 ? 456  ASN B CA  1 
ATOM   6274 C  C   . ASN B 1 456 ? 30.220  20.889  0.493   1.00 22.33 ? 456  ASN B C   1 
ATOM   6275 O  O   . ASN B 1 456 ? 29.360  21.159  -0.340  1.00 22.06 ? 456  ASN B O   1 
ATOM   6276 C  CB  . ASN B 1 456 ? 32.142  21.672  -0.860  1.00 24.16 ? 456  ASN B CB  1 
ATOM   6277 C  CG  . ASN B 1 456 ? 33.643  21.682  -0.978  1.00 26.54 ? 456  ASN B CG  1 
ATOM   6278 O  OD1 . ASN B 1 456 ? 34.361  21.331  -0.029  1.00 29.79 ? 456  ASN B OD1 1 
ATOM   6279 N  ND2 . ASN B 1 456 ? 34.134  22.089  -2.142  1.00 25.89 ? 456  ASN B ND2 1 
ATOM   6280 N  N   . TRP B 1 457 ? 29.997  20.890  1.807   1.00 21.36 ? 457  TRP B N   1 
ATOM   6281 C  CA  . TRP B 1 457 ? 28.659  20.951  2.378   1.00 21.21 ? 457  TRP B CA  1 
ATOM   6282 C  C   . TRP B 1 457 ? 27.861  22.200  1.989   1.00 21.25 ? 457  TRP B C   1 
ATOM   6283 O  O   . TRP B 1 457 ? 26.655  22.107  1.766   1.00 20.36 ? 457  TRP B O   1 
ATOM   6284 C  CB  . TRP B 1 457 ? 28.774  20.852  3.890   1.00 21.31 ? 457  TRP B CB  1 
ATOM   6285 C  CG  . TRP B 1 457 ? 27.525  20.669  4.688   1.00 21.06 ? 457  TRP B CG  1 
ATOM   6286 C  CD1 . TRP B 1 457 ? 26.968  21.578  5.558   1.00 21.47 ? 457  TRP B CD1 1 
ATOM   6287 C  CD2 . TRP B 1 457 ? 26.731  19.483  4.791   1.00 21.13 ? 457  TRP B CD2 1 
ATOM   6288 N  NE1 . TRP B 1 457 ? 25.876  21.027  6.177   1.00 21.35 ? 457  TRP B NE1 1 
ATOM   6289 C  CE2 . TRP B 1 457 ? 25.707  19.744  5.723   1.00 21.49 ? 457  TRP B CE2 1 
ATOM   6290 C  CE3 . TRP B 1 457 ? 26.781  18.228  4.181   1.00 21.77 ? 457  TRP B CE3 1 
ATOM   6291 C  CZ2 . TRP B 1 457 ? 24.737  18.800  6.051   1.00 22.15 ? 457  TRP B CZ2 1 
ATOM   6292 C  CZ3 . TRP B 1 457 ? 25.809  17.285  4.514   1.00 22.10 ? 457  TRP B CZ3 1 
ATOM   6293 C  CH2 . TRP B 1 457 ? 24.813  17.574  5.448   1.00 21.47 ? 457  TRP B CH2 1 
ATOM   6294 N  N   . LEU B 1 458 ? 28.512  23.356  1.877   1.00 21.51 ? 458  LEU B N   1 
ATOM   6295 C  CA  . LEU B 1 458 ? 27.771  24.586  1.562   1.00 23.07 ? 458  LEU B CA  1 
ATOM   6296 C  C   . LEU B 1 458 ? 27.158  24.624  0.144   1.00 21.02 ? 458  LEU B C   1 
ATOM   6297 O  O   . LEU B 1 458 ? 26.405  25.541  -0.176  1.00 19.95 ? 458  LEU B O   1 
ATOM   6298 C  CB  . LEU B 1 458 ? 28.617  25.844  1.802   1.00 26.64 ? 458  LEU B CB  1 
ATOM   6299 C  CG  . LEU B 1 458 ? 30.008  26.036  1.189   1.00 29.97 ? 458  LEU B CG  1 
ATOM   6300 C  CD1 . LEU B 1 458 ? 30.161  25.523  -0.229  1.00 31.16 ? 458  LEU B CD1 1 
ATOM   6301 C  CD2 . LEU B 1 458 ? 30.382  27.517  1.254   1.00 31.99 ? 458  LEU B CD2 1 
ATOM   6302 N  N   . ASN B 1 459 ? 27.492  23.652  -0.705  1.00 19.47 ? 459  ASN B N   1 
ATOM   6303 C  CA  . ASN B 1 459 ? 26.894  23.581  -2.034  1.00 19.40 ? 459  ASN B CA  1 
ATOM   6304 C  C   . ASN B 1 459 ? 25.468  23.069  -1.967  1.00 19.30 ? 459  ASN B C   1 
ATOM   6305 O  O   . ASN B 1 459 ? 24.699  23.268  -2.907  1.00 19.78 ? 459  ASN B O   1 
ATOM   6306 C  CB  . ASN B 1 459 ? 27.721  22.689  -2.957  1.00 19.20 ? 459  ASN B CB  1 
ATOM   6307 C  CG  . ASN B 1 459 ? 29.084  23.260  -3.249  1.00 19.66 ? 459  ASN B CG  1 
ATOM   6308 O  OD1 . ASN B 1 459 ? 29.286  24.467  -3.177  1.00 21.12 ? 459  ASN B OD1 1 
ATOM   6309 N  ND2 . ASN B 1 459 ? 30.032  22.397  -3.581  1.00 19.54 ? 459  ASN B ND2 1 
ATOM   6310 N  N   . TYR B 1 460 ? 25.116  22.432  -0.843  1.00 19.16 ? 460  TYR B N   1 
ATOM   6311 C  CA  . TYR B 1 460 ? 23.859  21.718  -0.717  1.00 18.70 ? 460  TYR B CA  1 
ATOM   6312 C  C   . TYR B 1 460 ? 22.747  22.657  -0.321  1.00 19.26 ? 460  TYR B C   1 
ATOM   6313 O  O   . TYR B 1 460 ? 21.741  22.736  -1.019  1.00 19.54 ? 460  TYR B O   1 
ATOM   6314 C  CB  . TYR B 1 460 ? 24.000  20.533  0.250   1.00 18.44 ? 460  TYR B CB  1 
ATOM   6315 C  CG  . TYR B 1 460 ? 24.785  19.392  -0.365  1.00 17.83 ? 460  TYR B CG  1 
ATOM   6316 C  CD1 . TYR B 1 460 ? 26.168  19.405  -0.392  1.00 17.62 ? 460  TYR B CD1 1 
ATOM   6317 C  CD2 . TYR B 1 460 ? 24.136  18.318  -0.959  1.00 17.65 ? 460  TYR B CD2 1 
ATOM   6318 C  CE1 . TYR B 1 460 ? 26.882  18.373  -0.979  1.00 17.08 ? 460  TYR B CE1 1 
ATOM   6319 C  CE2 . TYR B 1 460 ? 24.843  17.282  -1.553  1.00 16.86 ? 460  TYR B CE2 1 
ATOM   6320 C  CZ  . TYR B 1 460 ? 26.213  17.312  -1.560  1.00 16.83 ? 460  TYR B CZ  1 
ATOM   6321 O  OH  . TYR B 1 460 ? 26.926  16.280  -2.148  1.00 16.54 ? 460  TYR B OH  1 
ATOM   6322 N  N   . GLY B 1 461 ? 22.931  23.356  0.795   1.00 19.78 ? 461  GLY B N   1 
ATOM   6323 C  CA  . GLY B 1 461 ? 22.056  24.457  1.206   1.00 19.49 ? 461  GLY B CA  1 
ATOM   6324 C  C   . GLY B 1 461 ? 20.677  24.095  1.729   1.00 20.59 ? 461  GLY B C   1 
ATOM   6325 O  O   . GLY B 1 461 ? 19.859  24.985  1.928   1.00 20.80 ? 461  GLY B O   1 
ATOM   6326 N  N   . GLY B 1 462 ? 20.390  22.805  1.932   1.00 20.33 ? 462  GLY B N   1 
ATOM   6327 C  CA  . GLY B 1 462 ? 19.116  22.391  2.546   1.00 20.66 ? 462  GLY B CA  1 
ATOM   6328 C  C   . GLY B 1 462 ? 19.309  22.062  4.016   1.00 21.57 ? 462  GLY B C   1 
ATOM   6329 O  O   . GLY B 1 462 ? 20.371  22.307  4.566   1.00 22.19 ? 462  GLY B O   1 
ATOM   6330 N  N   . ASP B 1 463 ? 18.316  21.447  4.644   1.00 22.09 ? 463  ASP B N   1 
ATOM   6331 C  CA  . ASP B 1 463 ? 18.504  21.028  6.025   1.00 23.24 ? 463  ASP B CA  1 
ATOM   6332 C  C   . ASP B 1 463 ? 19.513  19.870  6.001   1.00 23.66 ? 463  ASP B C   1 
ATOM   6333 O  O   . ASP B 1 463 ? 20.233  19.682  5.016   1.00 22.33 ? 463  ASP B O   1 
ATOM   6334 C  CB  . ASP B 1 463 ? 17.181  20.572  6.639   1.00 24.32 ? 463  ASP B CB  1 
ATOM   6335 C  CG  . ASP B 1 463 ? 16.483  19.519  5.801   1.00 24.50 ? 463  ASP B CG  1 
ATOM   6336 O  OD1 . ASP B 1 463 ? 17.123  18.968  4.882   1.00 24.99 ? 463  ASP B OD1 1 
ATOM   6337 O  OD2 . ASP B 1 463 ? 15.293  19.242  6.062   1.00 29.08 ? 463  ASP B OD2 1 
ATOM   6338 N  N   . ASP B 1 464 ? 19.582  19.097  7.078   1.00 23.54 ? 464  ASP B N   1 
ATOM   6339 C  CA  . ASP B 1 464 ? 20.494  17.951  7.119   1.00 24.46 ? 464  ASP B CA  1 
ATOM   6340 C  C   . ASP B 1 464 ? 19.965  16.756  6.330   1.00 22.96 ? 464  ASP B C   1 
ATOM   6341 O  O   . ASP B 1 464 ? 20.716  16.116  5.607   1.00 22.58 ? 464  ASP B O   1 
ATOM   6342 C  CB  . ASP B 1 464 ? 20.807  17.557  8.562   1.00 26.46 ? 464  ASP B CB  1 
ATOM   6343 C  CG  . ASP B 1 464 ? 21.555  18.645  9.313   1.00 28.39 ? 464  ASP B CG  1 
ATOM   6344 O  OD1 . ASP B 1 464 ? 22.294  19.425  8.692   1.00 32.38 ? 464  ASP B OD1 1 
ATOM   6345 O  OD2 . ASP B 1 464 ? 21.421  18.724  10.540  1.00 33.01 ? 464  ASP B OD2 1 
ATOM   6346 N  N   . ALA B 1 465 ? 18.666  16.492  6.443   1.00 22.32 ? 465  ALA B N   1 
ATOM   6347 C  CA  . ALA B 1 465 ? 18.026  15.393  5.727   1.00 22.38 ? 465  ALA B CA  1 
ATOM   6348 C  C   . ALA B 1 465 ? 18.095  15.586  4.210   1.00 21.03 ? 465  ALA B C   1 
ATOM   6349 O  O   . ALA B 1 465 ? 18.437  14.658  3.465   1.00 19.02 ? 465  ALA B O   1 
ATOM   6350 C  CB  . ALA B 1 465 ? 16.571  15.243  6.171   1.00 22.89 ? 465  ALA B CB  1 
ATOM   6351 N  N   . PHE B 1 466 ? 17.791  16.792  3.752   1.00 20.67 ? 466  PHE B N   1 
ATOM   6352 C  CA  . PHE B 1 466 ? 17.911  17.079  2.322   1.00 21.18 ? 466  PHE B CA  1 
ATOM   6353 C  C   . PHE B 1 466 ? 19.363  16.916  1.846   1.00 20.07 ? 466  PHE B C   1 
ATOM   6354 O  O   . PHE B 1 466 ? 19.627  16.277  0.827   1.00 19.19 ? 466  PHE B O   1 
ATOM   6355 C  CB  . PHE B 1 466 ? 17.427  18.487  1.995   1.00 21.65 ? 466  PHE B CB  1 
ATOM   6356 C  CG  . PHE B 1 466 ? 17.681  18.876  0.569   1.00 22.87 ? 466  PHE B CG  1 
ATOM   6357 C  CD1 . PHE B 1 466 ? 16.755  18.560  -0.426  1.00 23.22 ? 466  PHE B CD1 1 
ATOM   6358 C  CD2 . PHE B 1 466 ? 18.865  19.504  0.208   1.00 22.76 ? 466  PHE B CD2 1 
ATOM   6359 C  CE1 . PHE B 1 466 ? 16.994  18.892  -1.754  1.00 23.21 ? 466  PHE B CE1 1 
ATOM   6360 C  CE2 . PHE B 1 466 ? 19.106  19.844  -1.114  1.00 24.12 ? 466  PHE B CE2 1 
ATOM   6361 C  CZ  . PHE B 1 466 ? 18.172  19.537  -2.100  1.00 23.69 ? 466  PHE B CZ  1 
ATOM   6362 N  N   . ASN B 1 467 ? 20.301  17.499  2.583   1.00 19.89 ? 467  ASN B N   1 
ATOM   6363 C  CA  . ASN B 1 467 ? 21.709  17.430  2.187   1.00 20.84 ? 467  ASN B CA  1 
ATOM   6364 C  C   . ASN B 1 467 ? 22.227  15.991  2.079   1.00 21.51 ? 467  ASN B C   1 
ATOM   6365 O  O   . ASN B 1 467 ? 22.887  15.639  1.085   1.00 21.73 ? 467  ASN B O   1 
ATOM   6366 C  CB  . ASN B 1 467 ? 22.586  18.222  3.150   1.00 20.69 ? 467  ASN B CB  1 
ATOM   6367 C  CG  . ASN B 1 467 ? 22.321  19.707  3.092   1.00 21.44 ? 467  ASN B CG  1 
ATOM   6368 O  OD1 . ASN B 1 467 ? 21.528  20.178  2.284   1.00 21.26 ? 467  ASN B OD1 1 
ATOM   6369 N  ND2 . ASN B 1 467 ? 23.011  20.461  3.944   1.00 22.20 ? 467  ASN B ND2 1 
ATOM   6370 N  N   . ILE B 1 468 ? 21.923  15.163  3.083   1.00 21.38 ? 468  ILE B N   1 
ATOM   6371 C  CA  . ILE B 1 468 ? 22.419  13.776  3.096   1.00 22.67 ? 468  ILE B CA  1 
ATOM   6372 C  C   . ILE B 1 468 ? 21.804  12.985  1.952   1.00 23.15 ? 468  ILE B C   1 
ATOM   6373 O  O   . ILE B 1 468 ? 22.518  12.344  1.181   1.00 24.14 ? 468  ILE B O   1 
ATOM   6374 C  CB  . ILE B 1 468 ? 22.165  13.080  4.459   1.00 22.93 ? 468  ILE B CB  1 
ATOM   6375 C  CG1 . ILE B 1 468 ? 23.036  13.741  5.544   1.00 23.55 ? 468  ILE B CG1 1 
ATOM   6376 C  CG2 . ILE B 1 468 ? 22.437  11.580  4.360   1.00 22.53 ? 468  ILE B CG2 1 
ATOM   6377 C  CD1 . ILE B 1 468 ? 22.757  13.254  6.960   1.00 24.21 ? 468  ILE B CD1 1 
ATOM   6378 N  N   . LYS B 1 469 ? 20.480  13.047  1.848   1.00 24.39 ? 469  LYS B N   1 
ATOM   6379 C  CA  . LYS B 1 469 ? 19.715  12.447  0.735   1.00 26.15 ? 469  LYS B CA  1 
ATOM   6380 C  C   . LYS B 1 469 ? 20.307  12.836  -0.636  1.00 23.97 ? 469  LYS B C   1 
ATOM   6381 O  O   . LYS B 1 469 ? 20.505  11.980  -1.513  1.00 20.99 ? 469  LYS B O   1 
ATOM   6382 C  CB  . LYS B 1 469 ? 18.244  12.899  0.835   1.00 29.06 ? 469  LYS B CB  1 
ATOM   6383 C  CG  . LYS B 1 469 ? 17.315  12.376  -0.255  1.00 33.74 ? 469  LYS B CG  1 
ATOM   6384 C  CD  . LYS B 1 469 ? 15.904  12.948  -0.117  1.00 36.68 ? 469  LYS B CD  1 
ATOM   6385 C  CE  . LYS B 1 469 ? 15.820  14.370  -0.675  1.00 39.47 ? 469  LYS B CE  1 
ATOM   6386 N  NZ  . LYS B 1 469 ? 14.504  15.012  -0.394  1.00 41.28 ? 469  LYS B NZ  1 
ATOM   6387 N  N   . SER B 1 470 ? 20.595  14.129  -0.792  1.00 22.58 ? 470  SER B N   1 
ATOM   6388 C  CA  . SER B 1 470 ? 21.203  14.645  -2.006  1.00 22.42 ? 470  SER B CA  1 
ATOM   6389 C  C   . SER B 1 470 ? 22.580  14.037  -2.249  1.00 22.42 ? 470  SER B C   1 
ATOM   6390 O  O   . SER B 1 470 ? 22.873  13.561  -3.345  1.00 23.00 ? 470  SER B O   1 
ATOM   6391 C  CB  . SER B 1 470 ? 21.284  16.176  -1.953  1.00 22.16 ? 470  SER B CB  1 
ATOM   6392 O  OG  . SER B 1 470 ? 19.982  16.738  -1.857  1.00 21.26 ? 470  SER B OG  1 
ATOM   6393 N  N   . LEU B 1 471 ? 23.421  14.034  -1.224  1.00 23.12 ? 471  LEU B N   1 
ATOM   6394 C  CA  . LEU B 1 471 ? 24.757  13.467  -1.347  1.00 23.13 ? 471  LEU B CA  1 
ATOM   6395 C  C   . LEU B 1 471 ? 24.711  12.021  -1.840  1.00 23.05 ? 471  LEU B C   1 
ATOM   6396 O  O   . LEU B 1 471 ? 25.430  11.647  -2.783  1.00 22.95 ? 471  LEU B O   1 
ATOM   6397 C  CB  . LEU B 1 471 ? 25.497  13.540  -0.004  1.00 22.45 ? 471  LEU B CB  1 
ATOM   6398 C  CG  . LEU B 1 471 ? 26.778  12.703  0.124   1.00 21.98 ? 471  LEU B CG  1 
ATOM   6399 C  CD1 . LEU B 1 471 ? 27.900  13.283  -0.711  1.00 21.69 ? 471  LEU B CD1 1 
ATOM   6400 C  CD2 . LEU B 1 471 ? 27.200  12.579  1.586   1.00 21.72 ? 471  LEU B CD2 1 
ATOM   6401 N  N   . PHE B 1 472 ? 23.873  11.209  -1.198  1.00 23.99 ? 472  PHE B N   1 
ATOM   6402 C  CA  . PHE B 1 472 ? 23.800  9.779   -1.530  1.00 24.23 ? 472  PHE B CA  1 
ATOM   6403 C  C   . PHE B 1 472 ? 23.244  9.549   -2.945  1.00 23.71 ? 472  PHE B C   1 
ATOM   6404 O  O   . PHE B 1 472 ? 23.655  8.623   -3.645  1.00 23.67 ? 472  PHE B O   1 
ATOM   6405 C  CB  . PHE B 1 472 ? 22.953  9.002   -0.507  1.00 24.78 ? 472  PHE B CB  1 
ATOM   6406 C  CG  . PHE B 1 472 ? 23.517  8.978   0.907   1.00 25.14 ? 472  PHE B CG  1 
ATOM   6407 C  CD1 . PHE B 1 472 ? 24.837  9.323   1.188   1.00 26.42 ? 472  PHE B CD1 1 
ATOM   6408 C  CD2 . PHE B 1 472 ? 22.713  8.573   1.960   1.00 25.24 ? 472  PHE B CD2 1 
ATOM   6409 C  CE1 . PHE B 1 472 ? 25.324  9.279   2.487   1.00 25.59 ? 472  PHE B CE1 1 
ATOM   6410 C  CE2 . PHE B 1 472 ? 23.197  8.524   3.255   1.00 25.19 ? 472  PHE B CE2 1 
ATOM   6411 C  CZ  . PHE B 1 472 ? 24.498  8.883   3.518   1.00 25.83 ? 472  PHE B CZ  1 
ATOM   6412 N  N   . ARG B 1 473 ? 22.318  10.400  -3.361  1.00 23.09 ? 473  ARG B N   1 
ATOM   6413 C  CA  . ARG B 1 473 ? 21.752  10.315  -4.704  1.00 22.81 ? 473  ARG B CA  1 
ATOM   6414 C  C   . ARG B 1 473 ? 22.797  10.673  -5.750  1.00 21.77 ? 473  ARG B C   1 
ATOM   6415 O  O   . ARG B 1 473 ? 22.974  9.950   -6.745  1.00 20.94 ? 473  ARG B O   1 
ATOM   6416 C  CB  . ARG B 1 473 ? 20.524  11.240  -4.805  1.00 23.91 ? 473  ARG B CB  1 
ATOM   6417 C  CG  . ARG B 1 473 ? 19.873  11.273  -6.170  1.00 24.46 ? 473  ARG B CG  1 
ATOM   6418 C  CD  . ARG B 1 473 ? 19.184  9.960   -6.469  1.00 24.62 ? 473  ARG B CD  1 
ATOM   6419 N  NE  . ARG B 1 473 ? 18.602  9.977   -7.806  1.00 25.13 ? 473  ARG B NE  1 
ATOM   6420 C  CZ  . ARG B 1 473 ? 18.844  9.097   -8.776  1.00 24.30 ? 473  ARG B CZ  1 
ATOM   6421 N  NH1 . ARG B 1 473 ? 19.675  8.077   -8.596  1.00 24.76 ? 473  ARG B NH1 1 
ATOM   6422 N  NH2 . ARG B 1 473 ? 18.226  9.239   -9.944  1.00 24.08 ? 473  ARG B NH2 1 
ATOM   6423 N  N   . ILE B 1 474 ? 23.508  11.774  -5.521  1.00 21.50 ? 474  ILE B N   1 
ATOM   6424 C  CA  . ILE B 1 474 ? 24.595  12.169  -6.421  1.00 22.16 ? 474  ILE B CA  1 
ATOM   6425 C  C   . ILE B 1 474 ? 25.605  11.025  -6.565  1.00 22.95 ? 474  ILE B C   1 
ATOM   6426 O  O   . ILE B 1 474 ? 25.989  10.661  -7.677  1.00 22.01 ? 474  ILE B O   1 
ATOM   6427 C  CB  . ILE B 1 474 ? 25.298  13.461  -5.943  1.00 22.52 ? 474  ILE B CB  1 
ATOM   6428 C  CG1 . ILE B 1 474 ? 24.365  14.670  -6.090  1.00 22.54 ? 474  ILE B CG1 1 
ATOM   6429 C  CG2 . ILE B 1 474 ? 26.555  13.717  -6.747  1.00 22.50 ? 474  ILE B CG2 1 
ATOM   6430 C  CD1 . ILE B 1 474 ? 24.853  15.907  -5.362  1.00 22.83 ? 474  ILE B CD1 1 
ATOM   6431 N  N   . LEU B 1 475 ? 26.008  10.425  -5.448  1.00 24.20 ? 475  LEU B N   1 
ATOM   6432 C  CA  . LEU B 1 475 ? 26.958  9.310   -5.517  1.00 25.63 ? 475  LEU B CA  1 
ATOM   6433 C  C   . LEU B 1 475 ? 26.388  8.027   -6.116  1.00 25.90 ? 475  LEU B C   1 
ATOM   6434 O  O   . LEU B 1 475 ? 27.140  7.228   -6.640  1.00 26.66 ? 475  LEU B O   1 
ATOM   6435 C  CB  . LEU B 1 475 ? 27.572  9.025   -4.141  1.00 26.22 ? 475  LEU B CB  1 
ATOM   6436 C  CG  . LEU B 1 475 ? 28.449  10.179  -3.638  1.00 25.82 ? 475  LEU B CG  1 
ATOM   6437 C  CD1 . LEU B 1 475 ? 28.857  9.952   -2.205  1.00 26.15 ? 475  LEU B CD1 1 
ATOM   6438 C  CD2 . LEU B 1 475 ? 29.680  10.371  -4.521  1.00 26.53 ? 475  LEU B CD2 1 
ATOM   6439 N  N   . SER B 1 476 ? 25.075  7.829   -6.069  1.00 26.75 ? 476  SER B N   1 
ATOM   6440 C  CA  . SER B 1 476 ? 24.479  6.581   -6.580  1.00 26.71 ? 476  SER B CA  1 
ATOM   6441 C  C   . SER B 1 476 ? 24.244  6.562   -8.107  1.00 27.12 ? 476  SER B C   1 
ATOM   6442 O  O   . SER B 1 476 ? 23.789  5.550   -8.649  1.00 28.47 ? 476  SER B O   1 
ATOM   6443 C  CB  . SER B 1 476 ? 23.154  6.311   -5.861  1.00 27.48 ? 476  SER B CB  1 
ATOM   6444 O  OG  . SER B 1 476 ? 22.139  7.226   -6.277  1.00 30.04 ? 476  SER B OG  1 
ATOM   6445 N  N   . ASN B 1 477 ? 24.541  7.664   -8.796  1.00 25.58 ? 477  ASN B N   1 
ATOM   6446 C  CA  . ASN B 1 477 ? 24.177  7.830   -10.207 1.00 25.01 ? 477  ASN B CA  1 
ATOM   6447 C  C   . ASN B 1 477 ? 25.336  8.447   -10.960 1.00 24.88 ? 477  ASN B C   1 
ATOM   6448 O  O   . ASN B 1 477 ? 25.738  9.575   -10.673 1.00 23.05 ? 477  ASN B O   1 
ATOM   6449 C  CB  . ASN B 1 477 ? 22.938  8.731   -10.351 1.00 23.76 ? 477  ASN B CB  1 
ATOM   6450 C  CG  . ASN B 1 477 ? 22.482  8.885   -11.802 1.00 23.99 ? 477  ASN B CG  1 
ATOM   6451 O  OD1 . ASN B 1 477 ? 23.165  9.488   -12.631 1.00 21.76 ? 477  ASN B OD1 1 
ATOM   6452 N  ND2 . ASN B 1 477 ? 21.315  8.330   -12.110 1.00 24.61 ? 477  ASN B ND2 1 
ATOM   6453 N  N   . ASP B 1 478 ? 25.857  7.712   -11.932 1.00 25.37 ? 478  ASP B N   1 
ATOM   6454 C  CA  . ASP B 1 478 ? 27.053  8.147   -12.642 1.00 27.95 ? 478  ASP B CA  1 
ATOM   6455 C  C   . ASP B 1 478 ? 26.845  9.443   -13.430 1.00 26.27 ? 478  ASP B C   1 
ATOM   6456 O  O   . ASP B 1 478 ? 27.778  10.233  -13.581 1.00 24.37 ? 478  ASP B O   1 
ATOM   6457 C  CB  . ASP B 1 478 ? 27.544  7.042   -13.581 1.00 31.40 ? 478  ASP B CB  1 
ATOM   6458 C  CG  . ASP B 1 478 ? 28.202  5.887   -12.829 1.00 35.46 ? 478  ASP B CG  1 
ATOM   6459 O  OD1 . ASP B 1 478 ? 28.633  6.085   -11.665 1.00 36.63 ? 478  ASP B OD1 1 
ATOM   6460 O  OD2 . ASP B 1 478 ? 28.294  4.788   -13.414 1.00 38.28 ? 478  ASP B OD2 1 
ATOM   6461 N  N   . ASP B 1 479 ? 25.637  9.660   -13.942 1.00 24.37 ? 479  ASP B N   1 
ATOM   6462 C  CA  . ASP B 1 479 ? 25.397  10.873  -14.706 1.00 23.73 ? 479  ASP B CA  1 
ATOM   6463 C  C   . ASP B 1 479 ? 25.386  12.082  -13.773 1.00 21.81 ? 479  ASP B C   1 
ATOM   6464 O  O   . ASP B 1 479 ? 26.006  13.102  -14.066 1.00 19.53 ? 479  ASP B O   1 
ATOM   6465 C  CB  . ASP B 1 479 ? 24.111  10.803  -15.505 1.00 24.23 ? 479  ASP B CB  1 
ATOM   6466 C  CG  . ASP B 1 479 ? 23.995  11.956  -16.482 1.00 25.16 ? 479  ASP B CG  1 
ATOM   6467 O  OD1 . ASP B 1 479 ? 24.847  12.038  -17.379 1.00 25.18 ? 479  ASP B OD1 1 
ATOM   6468 O  OD2 . ASP B 1 479 ? 23.092  12.798  -16.330 1.00 25.03 ? 479  ASP B OD2 1 
ATOM   6469 N  N   . ILE B 1 480 ? 24.686  11.943  -12.649 1.00 21.85 ? 480  ILE B N   1 
ATOM   6470 C  CA  . ILE B 1 480 ? 24.552  13.024  -11.670 1.00 21.84 ? 480  ILE B CA  1 
ATOM   6471 C  C   . ILE B 1 480 ? 25.928  13.331  -11.080 1.00 21.94 ? 480  ILE B C   1 
ATOM   6472 O  O   . ILE B 1 480 ? 26.318  14.498  -10.992 1.00 21.11 ? 480  ILE B O   1 
ATOM   6473 C  CB  . ILE B 1 480 ? 23.526  12.690  -10.570 1.00 21.97 ? 480  ILE B CB  1 
ATOM   6474 C  CG1 . ILE B 1 480 ? 22.125  12.515  -11.184 1.00 22.09 ? 480  ILE B CG1 1 
ATOM   6475 C  CG2 . ILE B 1 480 ? 23.497  13.782  -9.496  1.00 21.67 ? 480  ILE B CG2 1 
ATOM   6476 C  CD1 . ILE B 1 480 ? 21.036  12.212  -10.171 1.00 22.17 ? 480  ILE B CD1 1 
ATOM   6477 N  N   . LYS B 1 481 ? 26.664  12.281  -10.713 1.00 22.41 ? 481  LYS B N   1 
ATOM   6478 C  CA  . LYS B 1 481 ? 28.018  12.427  -10.167 1.00 22.81 ? 481  LYS B CA  1 
ATOM   6479 C  C   . LYS B 1 481 ? 28.931  13.174  -11.146 1.00 21.37 ? 481  LYS B C   1 
ATOM   6480 O  O   . LYS B 1 481 ? 29.658  14.097  -10.761 1.00 20.59 ? 481  LYS B O   1 
ATOM   6481 C  CB  . LYS B 1 481 ? 28.625  11.058  -9.843  1.00 24.39 ? 481  LYS B CB  1 
ATOM   6482 C  CG  . LYS B 1 481 ? 30.034  11.114  -9.252  1.00 26.16 ? 481  LYS B CG  1 
ATOM   6483 C  CD  . LYS B 1 481 ? 30.535  9.727   -8.828  1.00 27.39 ? 481  LYS B CD  1 
ATOM   6484 C  CE  . LYS B 1 481 ? 31.864  9.818   -8.093  1.00 28.66 ? 481  LYS B CE  1 
ATOM   6485 N  NZ  . LYS B 1 481 ? 32.590  8.521   -8.125  1.00 30.73 ? 481  LYS B NZ  1 
ATOM   6486 N  N   . SER B 1 482 ? 28.897  12.762  -12.401 1.00 19.96 ? 482  SER B N   1 
ATOM   6487 C  CA  . SER B 1 482 ? 29.679  13.420  -13.432 1.00 21.04 ? 482  SER B CA  1 
ATOM   6488 C  C   . SER B 1 482 ? 29.312  14.913  -13.581 1.00 20.26 ? 482  SER B C   1 
ATOM   6489 O  O   . SER B 1 482 ? 30.186  15.786  -13.501 1.00 19.52 ? 482  SER B O   1 
ATOM   6490 C  CB  . SER B 1 482 ? 29.507  12.701  -14.762 1.00 22.08 ? 482  SER B CB  1 
ATOM   6491 O  OG  . SER B 1 482 ? 30.301  13.328  -15.749 1.00 24.21 ? 482  SER B OG  1 
ATOM   6492 N  N   . ARG B 1 483 ? 28.025  15.204  -13.762 1.00 18.80 ? 483  ARG B N   1 
ATOM   6493 C  CA  . ARG B 1 483 ? 27.576  16.594  -13.844 1.00 18.33 ? 483  ARG B CA  1 
ATOM   6494 C  C   . ARG B 1 483 ? 28.035  17.415  -12.646 1.00 18.11 ? 483  ARG B C   1 
ATOM   6495 O  O   . ARG B 1 483 ? 28.530  18.537  -12.807 1.00 17.96 ? 483  ARG B O   1 
ATOM   6496 C  CB  . ARG B 1 483 ? 26.048  16.682  -13.950 1.00 18.13 ? 483  ARG B CB  1 
ATOM   6497 C  CG  . ARG B 1 483 ? 25.509  16.380  -15.338 1.00 18.29 ? 483  ARG B CG  1 
ATOM   6498 C  CD  . ARG B 1 483 ? 24.019  16.135  -15.294 1.00 18.45 ? 483  ARG B CD  1 
ATOM   6499 N  NE  . ARG B 1 483 ? 23.518  15.716  -16.588 1.00 18.71 ? 483  ARG B NE  1 
ATOM   6500 C  CZ  . ARG B 1 483 ? 22.769  16.461  -17.409 1.00 18.64 ? 483  ARG B CZ  1 
ATOM   6501 N  NH1 . ARG B 1 483 ? 22.384  17.703  -17.107 1.00 18.33 ? 483  ARG B NH1 1 
ATOM   6502 N  NH2 . ARG B 1 483 ? 22.421  15.951  -18.569 1.00 17.93 ? 483  ARG B NH2 1 
ATOM   6503 N  N   . ALA B 1 484 ? 27.853  16.865  -11.446 1.00 17.56 ? 484  ALA B N   1 
ATOM   6504 C  CA  . ALA B 1 484 ? 28.252  17.553  -10.224 1.00 18.12 ? 484  ALA B CA  1 
ATOM   6505 C  C   . ALA B 1 484 ? 29.753  17.874  -10.208 1.00 18.03 ? 484  ALA B C   1 
ATOM   6506 O  O   . ALA B 1 484 ? 30.178  18.943  -9.731  1.00 16.37 ? 484  ALA B O   1 
ATOM   6507 C  CB  . ALA B 1 484 ? 27.879  16.719  -9.002  1.00 17.96 ? 484  ALA B CB  1 
ATOM   6508 N  N   . THR B 1 485 ? 30.524  16.920  -10.732 1.00 18.27 ? 485  THR B N   1 
ATOM   6509 C  CA  . THR B 1 485 ? 31.976  16.978  -10.828 1.00 19.25 ? 485  THR B CA  1 
ATOM   6510 C  C   . THR B 1 485 ? 32.471  18.074  -11.772 1.00 19.66 ? 485  THR B C   1 
ATOM   6511 O  O   . THR B 1 485 ? 33.535  18.621  -11.568 1.00 19.72 ? 485  THR B O   1 
ATOM   6512 C  CB  . THR B 1 485 ? 32.496  15.601  -11.311 1.00 19.46 ? 485  THR B CB  1 
ATOM   6513 O  OG1 . THR B 1 485 ? 32.226  14.627  -10.306 1.00 19.99 ? 485  THR B OG1 1 
ATOM   6514 C  CG2 . THR B 1 485 ? 33.964  15.607  -11.620 1.00 19.69 ? 485  THR B CG2 1 
ATOM   6515 N  N   . TRP B 1 486 ? 31.678  18.389  -12.790 1.00 20.28 ? 486  TRP B N   1 
ATOM   6516 C  CA  . TRP B 1 486 ? 32.034  19.390  -13.790 1.00 20.12 ? 486  TRP B CA  1 
ATOM   6517 C  C   . TRP B 1 486 ? 31.288  20.740  -13.649 1.00 18.73 ? 486  TRP B C   1 
ATOM   6518 O  O   . TRP B 1 486 ? 31.693  21.718  -14.265 1.00 17.62 ? 486  TRP B O   1 
ATOM   6519 C  CB  . TRP B 1 486 ? 31.835  18.793  -15.187 1.00 20.96 ? 486  TRP B CB  1 
ATOM   6520 C  CG  . TRP B 1 486 ? 32.812  17.675  -15.456 1.00 21.67 ? 486  TRP B CG  1 
ATOM   6521 C  CD1 . TRP B 1 486 ? 32.559  16.323  -15.418 1.00 21.98 ? 486  TRP B CD1 1 
ATOM   6522 C  CD2 . TRP B 1 486 ? 34.205  17.813  -15.755 1.00 21.46 ? 486  TRP B CD2 1 
ATOM   6523 N  NE1 . TRP B 1 486 ? 33.710  15.621  -15.690 1.00 22.61 ? 486  TRP B NE1 1 
ATOM   6524 C  CE2 . TRP B 1 486 ? 34.735  16.508  -15.895 1.00 22.01 ? 486  TRP B CE2 1 
ATOM   6525 C  CE3 . TRP B 1 486 ? 35.056  18.913  -15.931 1.00 21.84 ? 486  TRP B CE3 1 
ATOM   6526 C  CZ2 . TRP B 1 486 ? 36.075  16.274  -16.200 1.00 22.47 ? 486  TRP B CZ2 1 
ATOM   6527 C  CZ3 . TRP B 1 486 ? 36.399  18.680  -16.230 1.00 22.11 ? 486  TRP B CZ3 1 
ATOM   6528 C  CH2 . TRP B 1 486 ? 36.892  17.372  -16.368 1.00 22.66 ? 486  TRP B CH2 1 
ATOM   6529 N  N   . ALA B 1 487 ? 30.251  20.804  -12.813 1.00 17.89 ? 487  ALA B N   1 
ATOM   6530 C  CA  . ALA B 1 487 ? 29.413  22.019  -12.701 1.00 17.39 ? 487  ALA B CA  1 
ATOM   6531 C  C   . ALA B 1 487 ? 30.057  23.157  -11.894 1.00 17.06 ? 487  ALA B C   1 
ATOM   6532 O  O   . ALA B 1 487 ? 30.426  22.979  -10.730 1.00 16.53 ? 487  ALA B O   1 
ATOM   6533 C  CB  . ALA B 1 487 ? 28.057  21.673  -12.112 1.00 16.91 ? 487  ALA B CB  1 
ATOM   6534 N  N   . ASN B 1 488 ? 30.182  24.322  -12.522 1.00 16.99 ? 488  ASN B N   1 
ATOM   6535 C  CA  . ASN B 1 488 ? 30.743  25.501  -11.862 1.00 16.64 ? 488  ASN B CA  1 
ATOM   6536 C  C   . ASN B 1 488 ? 30.436  26.808  -12.620 1.00 17.06 ? 488  ASN B C   1 
ATOM   6537 O  O   . ASN B 1 488 ? 31.306  27.683  -12.784 1.00 15.77 ? 488  ASN B O   1 
ATOM   6538 C  CB  . ASN B 1 488 ? 32.263  25.339  -11.624 1.00 16.46 ? 488  ASN B CB  1 
ATOM   6539 C  CG  . ASN B 1 488 ? 33.070  25.385  -12.902 1.00 16.76 ? 488  ASN B CG  1 
ATOM   6540 O  OD1 . ASN B 1 488 ? 32.622  24.927  -13.957 1.00 17.25 ? 488  ASN B OD1 1 
ATOM   6541 N  ND2 . ASN B 1 488 ? 34.270  25.943  -12.817 1.00 16.38 ? 488  ASN B ND2 1 
ATOM   6542 N  N   . ALA B 1 489 ? 29.180  26.944  -13.039 1.00 17.29 ? 489  ALA B N   1 
ATOM   6543 C  CA  . ALA B 1 489 ? 28.718  28.174  -13.671 1.00 16.91 ? 489  ALA B CA  1 
ATOM   6544 C  C   . ALA B 1 489 ? 28.911  29.343  -12.726 1.00 17.14 ? 489  ALA B C   1 
ATOM   6545 O  O   . ALA B 1 489 ? 28.796  29.218  -11.499 1.00 15.98 ? 489  ALA B O   1 
ATOM   6546 C  CB  . ALA B 1 489 ? 27.263  28.061  -14.051 1.00 16.89 ? 489  ALA B CB  1 
ATOM   6547 N  N   . ALA B 1 490 ? 29.204  30.484  -13.329 1.00 17.75 ? 490  ALA B N   1 
ATOM   6548 C  CA  . ALA B 1 490 ? 29.381  31.726  -12.610 1.00 17.76 ? 490  ALA B CA  1 
ATOM   6549 C  C   . ALA B 1 490 ? 28.726  32.890  -13.382 1.00 17.93 ? 490  ALA B C   1 
ATOM   6550 O  O   . ALA B 1 490 ? 28.749  32.911  -14.609 1.00 17.07 ? 490  ALA B O   1 
ATOM   6551 C  CB  . ALA B 1 490 ? 30.864  31.982  -12.451 1.00 17.38 ? 490  ALA B CB  1 
ATOM   6552 N  N   . ILE B 1 491 ? 28.148  33.845  -12.653 1.00 17.82 ? 491  ILE B N   1 
ATOM   6553 C  CA  . ILE B 1 491 ? 27.850  35.147  -13.211 1.00 17.57 ? 491  ILE B CA  1 
ATOM   6554 C  C   . ILE B 1 491 ? 28.946  36.071  -12.713 1.00 18.09 ? 491  ILE B C   1 
ATOM   6555 O  O   . ILE B 1 491 ? 28.982  36.434  -11.530 1.00 17.82 ? 491  ILE B O   1 
ATOM   6556 C  CB  . ILE B 1 491 ? 26.488  35.708  -12.792 1.00 17.32 ? 491  ILE B CB  1 
ATOM   6557 C  CG1 . ILE B 1 491 ? 25.366  34.812  -13.334 1.00 17.64 ? 491  ILE B CG1 1 
ATOM   6558 C  CG2 . ILE B 1 491 ? 26.343  37.142  -13.323 1.00 16.92 ? 491  ILE B CG2 1 
ATOM   6559 C  CD1 . ILE B 1 491 ? 23.974  35.264  -12.936 1.00 17.80 ? 491  ILE B CD1 1 
ATOM   6560 N  N   . GLY B 1 492 ? 29.844  36.432  -13.620 1.00 17.61 ? 492  GLY B N   1 
ATOM   6561 C  CA  . GLY B 1 492 ? 31.029  37.174  -13.257 1.00 17.84 ? 492  GLY B CA  1 
ATOM   6562 C  C   . GLY B 1 492 ? 30.827  38.672  -13.374 1.00 18.18 ? 492  GLY B C   1 
ATOM   6563 O  O   . GLY B 1 492 ? 29.861  39.129  -13.966 1.00 17.26 ? 492  GLY B O   1 
ATOM   6564 N  N   . ILE B 1 493 ? 31.757  39.424  -12.791 1.00 18.97 ? 493  ILE B N   1 
ATOM   6565 C  CA  . ILE B 1 493 ? 31.733  40.875  -12.838 1.00 19.11 ? 493  ILE B CA  1 
ATOM   6566 C  C   . ILE B 1 493 ? 33.173  41.369  -12.922 1.00 19.68 ? 493  ILE B C   1 
ATOM   6567 O  O   . ILE B 1 493 ? 34.081  40.792  -12.294 1.00 19.74 ? 493  ILE B O   1 
ATOM   6568 C  CB  . ILE B 1 493 ? 30.945  41.498  -11.653 1.00 18.39 ? 493  ILE B CB  1 
ATOM   6569 C  CG1 . ILE B 1 493 ? 30.837  43.022  -11.824 1.00 18.91 ? 493  ILE B CG1 1 
ATOM   6570 C  CG2 . ILE B 1 493 ? 31.572  41.128  -10.320 1.00 18.56 ? 493  ILE B CG2 1 
ATOM   6571 C  CD1 . ILE B 1 493 ? 29.777  43.696  -10.962 1.00 18.72 ? 493  ILE B CD1 1 
ATOM   6572 N  N   . LEU B 1 494 ? 33.379  42.382  -13.764 1.00 19.27 ? 494  LEU B N   1 
ATOM   6573 C  CA  . LEU B 1 494 ? 34.646  43.089  -13.836 1.00 20.40 ? 494  LEU B CA  1 
ATOM   6574 C  C   . LEU B 1 494 ? 34.391  44.582  -14.041 1.00 21.63 ? 494  LEU B C   1 
ATOM   6575 O  O   . LEU B 1 494 ? 33.325  44.985  -14.523 1.00 21.89 ? 494  LEU B O   1 
ATOM   6576 C  CB  . LEU B 1 494 ? 35.537  42.523  -14.948 1.00 19.61 ? 494  LEU B CB  1 
ATOM   6577 C  CG  . LEU B 1 494 ? 35.038  42.561  -16.397 1.00 19.95 ? 494  LEU B CG  1 
ATOM   6578 C  CD1 . LEU B 1 494 ? 35.364  43.878  -17.080 1.00 20.74 ? 494  LEU B CD1 1 
ATOM   6579 C  CD2 . LEU B 1 494 ? 35.657  41.420  -17.201 1.00 19.95 ? 494  LEU B CD2 1 
ATOM   6580 N  N   . LYS B 1 495 ? 35.359  45.394  -13.640 1.00 22.46 ? 495  LYS B N   1 
ATOM   6581 C  CA  . LYS B 1 495 ? 35.305  46.825  -13.896 1.00 23.19 ? 495  LYS B CA  1 
ATOM   6582 C  C   . LYS B 1 495 ? 36.167  47.142  -15.103 1.00 22.10 ? 495  LYS B C   1 
ATOM   6583 O  O   . LYS B 1 495 ? 37.293  46.649  -15.207 1.00 21.36 ? 495  LYS B O   1 
ATOM   6584 C  CB  . LYS B 1 495 ? 35.805  47.608  -12.694 1.00 24.93 ? 495  LYS B CB  1 
ATOM   6585 C  CG  . LYS B 1 495 ? 35.447  49.079  -12.773 1.00 26.61 ? 495  LYS B CG  1 
ATOM   6586 C  CD  . LYS B 1 495 ? 35.707  49.784  -11.450 1.00 28.05 ? 495  LYS B CD  1 
ATOM   6587 C  CE  . LYS B 1 495 ? 37.164  50.163  -11.329 1.00 29.77 ? 495  LYS B CE  1 
ATOM   6588 N  NZ  . LYS B 1 495 ? 37.411  50.813  -10.019 1.00 32.30 ? 495  LYS B NZ  1 
ATOM   6589 N  N   . LEU B 1 496 ? 35.635  47.969  -15.999 1.00 21.21 ? 496  LEU B N   1 
ATOM   6590 C  CA  . LEU B 1 496 ? 36.368  48.426  -17.184 1.00 21.52 ? 496  LEU B CA  1 
ATOM   6591 C  C   . LEU B 1 496 ? 37.119  49.703  -16.866 1.00 21.93 ? 496  LEU B C   1 
ATOM   6592 O  O   . LEU B 1 496 ? 36.832  50.347  -15.871 1.00 20.92 ? 496  LEU B O   1 
ATOM   6593 C  CB  . LEU B 1 496 ? 35.403  48.728  -18.336 1.00 21.09 ? 496  LEU B CB  1 
ATOM   6594 C  CG  . LEU B 1 496 ? 34.594  47.562  -18.894 1.00 20.69 ? 496  LEU B CG  1 
ATOM   6595 C  CD1 . LEU B 1 496 ? 33.518  48.092  -19.844 1.00 20.93 ? 496  LEU B CD1 1 
ATOM   6596 C  CD2 . LEU B 1 496 ? 35.496  46.561  -19.589 1.00 20.36 ? 496  LEU B CD2 1 
ATOM   6597 N  N   . ASN B 1 497 ? 38.064  50.075  -17.723 1.00 23.61 ? 497  ASN B N   1 
ATOM   6598 C  CA  . ASN B 1 497 ? 38.746  51.374  -17.596 1.00 24.97 ? 497  ASN B CA  1 
ATOM   6599 C  C   . ASN B 1 497 ? 37.799  52.514  -17.997 1.00 25.41 ? 497  ASN B C   1 
ATOM   6600 O  O   . ASN B 1 497 ? 36.647  52.258  -18.368 1.00 25.54 ? 497  ASN B O   1 
ATOM   6601 C  CB  . ASN B 1 497 ? 40.027  51.381  -18.438 1.00 25.98 ? 497  ASN B CB  1 
ATOM   6602 C  CG  . ASN B 1 497 ? 39.759  51.383  -19.940 1.00 27.28 ? 497  ASN B CG  1 
ATOM   6603 O  OD1 . ASN B 1 497 ? 38.674  51.031  -20.416 1.00 28.94 ? 497  ASN B OD1 1 
ATOM   6604 N  ND2 . ASN B 1 497 ? 40.765  51.760  -20.693 1.00 29.83 ? 497  ASN B ND2 1 
ATOM   6605 N  N   . LYS B 1 498 ? 38.267  53.758  -17.942 1.00 27.70 ? 498  LYS B N   1 
ATOM   6606 C  CA  . LYS B 1 498 ? 37.393  54.921  -18.180 1.00 30.40 ? 498  LYS B CA  1 
ATOM   6607 C  C   . LYS B 1 498 ? 37.171  55.304  -19.655 1.00 29.85 ? 498  LYS B C   1 
ATOM   6608 O  O   . LYS B 1 498 ? 36.417  56.229  -19.940 1.00 29.71 ? 498  LYS B O   1 
ATOM   6609 C  CB  . LYS B 1 498 ? 37.922  56.145  -17.420 1.00 34.30 ? 498  LYS B CB  1 
ATOM   6610 C  CG  . LYS B 1 498 ? 38.007  55.949  -15.911 1.00 37.61 ? 498  LYS B CG  1 
ATOM   6611 C  CD  . LYS B 1 498 ? 36.657  56.071  -15.222 1.00 39.90 ? 498  LYS B CD  1 
ATOM   6612 C  CE  . LYS B 1 498 ? 36.413  57.484  -14.710 1.00 42.87 ? 498  LYS B CE  1 
ATOM   6613 N  NZ  . LYS B 1 498 ? 35.018  57.647  -14.199 1.00 44.50 ? 498  LYS B NZ  1 
ATOM   6614 N  N   . ASP B 1 499 ? 37.811  54.605  -20.586 1.00 29.68 ? 499  ASP B N   1 
ATOM   6615 C  CA  . ASP B 1 499 ? 37.708  54.931  -22.007 1.00 29.23 ? 499  ASP B CA  1 
ATOM   6616 C  C   . ASP B 1 499 ? 36.517  54.192  -22.642 1.00 27.90 ? 499  ASP B C   1 
ATOM   6617 O  O   . ASP B 1 499 ? 36.576  52.967  -22.872 1.00 23.97 ? 499  ASP B O   1 
ATOM   6618 C  CB  . ASP B 1 499 ? 39.008  54.549  -22.712 1.00 31.53 ? 499  ASP B CB  1 
ATOM   6619 C  CG  . ASP B 1 499 ? 39.123  55.155  -24.100 1.00 35.25 ? 499  ASP B CG  1 
ATOM   6620 O  OD1 . ASP B 1 499 ? 38.097  55.196  -24.819 1.00 37.61 ? 499  ASP B OD1 1 
ATOM   6621 O  OD2 . ASP B 1 499 ? 40.251  55.573  -24.476 1.00 35.34 ? 499  ASP B OD2 1 
ATOM   6622 N  N   . GLU B 1 500 ? 35.452  54.943  -22.933 1.00 25.71 ? 500  GLU B N   1 
ATOM   6623 C  CA  . GLU B 1 500 ? 34.209  54.355  -23.424 1.00 27.45 ? 500  GLU B CA  1 
ATOM   6624 C  C   . GLU B 1 500 ? 34.347  53.572  -24.734 1.00 24.76 ? 500  GLU B C   1 
ATOM   6625 O  O   . GLU B 1 500 ? 33.721  52.523  -24.876 1.00 24.16 ? 500  GLU B O   1 
ATOM   6626 C  CB  . GLU B 1 500 ? 33.047  55.382  -23.511 1.00 29.35 ? 500  GLU B CB  1 
ATOM   6627 C  CG  . GLU B 1 500 ? 33.412  56.782  -23.956 1.00 31.26 ? 500  GLU B CG  1 
ATOM   6628 C  CD  . GLU B 1 500 ? 32.213  57.601  -24.439 1.00 32.58 ? 500  GLU B CD  1 
ATOM   6629 O  OE1 . GLU B 1 500 ? 31.130  57.535  -23.817 1.00 30.99 ? 500  GLU B OE1 1 
ATOM   6630 O  OE2 . GLU B 1 500 ? 32.372  58.329  -25.449 1.00 34.19 ? 500  GLU B OE2 1 
ATOM   6631 N  N   . LYS B 1 501 ? 35.166  54.058  -25.668 1.00 24.10 ? 501  LYS B N   1 
ATOM   6632 C  CA  . LYS B 1 501 ? 35.321  53.417  -26.984 1.00 24.19 ? 501  LYS B CA  1 
ATOM   6633 C  C   . LYS B 1 501 ? 36.474  52.406  -27.062 1.00 24.05 ? 501  LYS B C   1 
ATOM   6634 O  O   . LYS B 1 501 ? 36.602  51.698  -28.057 1.00 22.53 ? 501  LYS B O   1 
ATOM   6635 C  CB  . LYS B 1 501 ? 35.482  54.474  -28.068 1.00 24.85 ? 501  LYS B CB  1 
ATOM   6636 C  CG  . LYS B 1 501 ? 34.273  55.379  -28.205 1.00 25.90 ? 501  LYS B CG  1 
ATOM   6637 C  CD  . LYS B 1 501 ? 34.571  56.533  -29.145 1.00 26.77 ? 501  LYS B CD  1 
ATOM   6638 C  CE  . LYS B 1 501 ? 33.321  57.358  -29.387 1.00 26.53 ? 501  LYS B CE  1 
ATOM   6639 N  NZ  . LYS B 1 501 ? 33.487  58.302  -30.527 1.00 26.78 ? 501  LYS B NZ  1 
ATOM   6640 N  N   . ASN B 1 502 ? 37.288  52.323  -26.006 1.00 24.92 ? 502  ASN B N   1 
ATOM   6641 C  CA  . ASN B 1 502 ? 38.424  51.386  -25.968 1.00 26.21 ? 502  ASN B CA  1 
ATOM   6642 C  C   . ASN B 1 502 ? 38.381  50.529  -24.714 1.00 24.91 ? 502  ASN B C   1 
ATOM   6643 O  O   . ASN B 1 502 ? 39.347  50.499  -23.967 1.00 26.37 ? 502  ASN B O   1 
ATOM   6644 C  CB  . ASN B 1 502 ? 39.764  52.154  -25.996 1.00 27.70 ? 502  ASN B CB  1 
ATOM   6645 C  CG  . ASN B 1 502 ? 39.894  53.051  -27.205 1.00 29.55 ? 502  ASN B CG  1 
ATOM   6646 O  OD1 . ASN B 1 502 ? 40.107  54.272  -27.094 1.00 32.80 ? 502  ASN B OD1 1 
ATOM   6647 N  ND2 . ASN B 1 502 ? 39.717  52.465  -28.369 1.00 29.99 ? 502  ASN B ND2 1 
ATOM   6648 N  N   . PRO B 1 503 ? 37.260  49.836  -24.469 1.00 23.54 ? 503  PRO B N   1 
ATOM   6649 C  CA  . PRO B 1 503 ? 37.155  49.146  -23.199 1.00 23.20 ? 503  PRO B CA  1 
ATOM   6650 C  C   . PRO B 1 503 ? 38.262  48.110  -22.988 1.00 24.18 ? 503  PRO B C   1 
ATOM   6651 O  O   . PRO B 1 503 ? 38.617  47.358  -23.906 1.00 23.74 ? 503  PRO B O   1 
ATOM   6652 C  CB  . PRO B 1 503 ? 35.773  48.478  -23.276 1.00 22.85 ? 503  PRO B CB  1 
ATOM   6653 C  CG  . PRO B 1 503 ? 35.420  48.459  -24.718 1.00 21.73 ? 503  PRO B CG  1 
ATOM   6654 C  CD  . PRO B 1 503 ? 36.025  49.702  -25.264 1.00 22.54 ? 503  PRO B CD  1 
ATOM   6655 N  N   . LYS B 1 504 ? 38.808  48.121  -21.782 1.00 25.13 ? 504  LYS B N   1 
ATOM   6656 C  CA  . LYS B 1 504 ? 39.791  47.160  -21.325 1.00 27.17 ? 504  LYS B CA  1 
ATOM   6657 C  C   . LYS B 1 504 ? 39.489  46.915  -19.859 1.00 25.24 ? 504  LYS B C   1 
ATOM   6658 O  O   . LYS B 1 504 ? 38.903  47.771  -19.194 1.00 25.57 ? 504  LYS B O   1 
ATOM   6659 C  CB  . LYS B 1 504 ? 41.221  47.708  -21.466 1.00 30.30 ? 504  LYS B CB  1 
ATOM   6660 C  CG  . LYS B 1 504 ? 41.661  47.969  -22.911 1.00 34.04 ? 504  LYS B CG  1 
ATOM   6661 C  CD  . LYS B 1 504 ? 43.185  47.921  -23.034 1.00 36.79 ? 504  LYS B CD  1 
ATOM   6662 C  CE  . LYS B 1 504 ? 43.659  47.589  -24.443 1.00 40.18 ? 504  LYS B CE  1 
ATOM   6663 N  NZ  . LYS B 1 504 ? 44.340  48.736  -25.112 1.00 42.17 ? 504  LYS B NZ  1 
ATOM   6664 N  N   . VAL B 1 505 ? 39.887  45.753  -19.362 1.00 23.09 ? 505  VAL B N   1 
ATOM   6665 C  CA  . VAL B 1 505 ? 39.668  45.403  -17.971 1.00 23.05 ? 505  VAL B CA  1 
ATOM   6666 C  C   . VAL B 1 505 ? 40.545  46.299  -17.086 1.00 23.67 ? 505  VAL B C   1 
ATOM   6667 O  O   . VAL B 1 505 ? 41.741  46.452  -17.342 1.00 23.37 ? 505  VAL B O   1 
ATOM   6668 C  CB  . VAL B 1 505 ? 39.986  43.914  -17.695 1.00 22.22 ? 505  VAL B CB  1 
ATOM   6669 C  CG1 . VAL B 1 505 ? 39.790  43.593  -16.221 1.00 22.68 ? 505  VAL B CG1 1 
ATOM   6670 C  CG2 . VAL B 1 505 ? 39.109  42.990  -18.542 1.00 22.47 ? 505  VAL B CG2 1 
ATOM   6671 N  N   . ALA B 1 506 ? 39.928  46.896  -16.073 1.00 23.65 ? 506  ALA B N   1 
ATOM   6672 C  CA  . ALA B 1 506 ? 40.632  47.630  -15.030 1.00 25.36 ? 506  ALA B CA  1 
ATOM   6673 C  C   . ALA B 1 506 ? 40.789  46.740  -13.791 1.00 26.29 ? 506  ALA B C   1 
ATOM   6674 O  O   . ALA B 1 506 ? 41.858  46.697  -13.191 1.00 26.05 ? 506  ALA B O   1 
ATOM   6675 C  CB  . ALA B 1 506 ? 39.880  48.903  -14.668 1.00 25.45 ? 506  ALA B CB  1 
ATOM   6676 N  N   . GLU B 1 507 ? 39.728  46.029  -13.416 1.00 26.79 ? 507  GLU B N   1 
ATOM   6677 C  CA  . GLU B 1 507 ? 39.774  45.153  -12.257 1.00 27.16 ? 507  GLU B CA  1 
ATOM   6678 C  C   . GLU B 1 507 ? 38.822  43.964  -12.398 1.00 27.03 ? 507  GLU B C   1 
ATOM   6679 O  O   . GLU B 1 507 ? 37.723  44.097  -12.946 1.00 25.36 ? 507  GLU B O   1 
ATOM   6680 C  CB  . GLU B 1 507 ? 39.432  45.953  -11.004 1.00 30.25 ? 507  GLU B CB  1 
ATOM   6681 C  CG  . GLU B 1 507 ? 40.015  45.368  -9.735  1.00 33.91 ? 507  GLU B CG  1 
ATOM   6682 C  CD  . GLU B 1 507 ? 39.724  46.219  -8.509  1.00 38.60 ? 507  GLU B CD  1 
ATOM   6683 O  OE1 . GLU B 1 507 ? 39.239  47.365  -8.676  1.00 44.06 ? 507  GLU B OE1 1 
ATOM   6684 O  OE2 . GLU B 1 507 ? 39.977  45.740  -7.376  1.00 40.17 ? 507  GLU B OE2 1 
ATOM   6685 N  N   . LEU B 1 508 ? 39.259  42.809  -11.896 1.00 26.00 ? 508  LEU B N   1 
ATOM   6686 C  CA  . LEU B 1 508 ? 38.446  41.601  -11.834 1.00 26.16 ? 508  LEU B CA  1 
ATOM   6687 C  C   . LEU B 1 508 ? 37.961  41.362  -10.418 1.00 25.27 ? 508  LEU B C   1 
ATOM   6688 O  O   . LEU B 1 508 ? 38.607  41.752  -9.465  1.00 25.97 ? 508  LEU B O   1 
ATOM   6689 C  CB  . LEU B 1 508 ? 39.267  40.382  -12.256 1.00 26.56 ? 508  LEU B CB  1 
ATOM   6690 C  CG  . LEU B 1 508 ? 39.871  40.372  -13.657 1.00 26.79 ? 508  LEU B CG  1 
ATOM   6691 C  CD1 . LEU B 1 508 ? 40.723  39.120  -13.802 1.00 27.76 ? 508  LEU B CD1 1 
ATOM   6692 C  CD2 . LEU B 1 508 ? 38.782  40.422  -14.713 1.00 26.73 ? 508  LEU B CD2 1 
ATOM   6693 N  N   . TYR B 1 509 ? 36.833  40.684  -10.285 1.00 25.10 ? 509  TYR B N   1 
ATOM   6694 C  CA  . TYR B 1 509 ? 36.318  40.307  -8.977  1.00 24.41 ? 509  TYR B CA  1 
ATOM   6695 C  C   . TYR B 1 509 ? 35.833  38.875  -9.006  1.00 23.53 ? 509  TYR B C   1 
ATOM   6696 O  O   . TYR B 1 509 ? 35.654  38.277  -10.080 1.00 21.57 ? 509  TYR B O   1 
ATOM   6697 C  CB  . TYR B 1 509 ? 35.136  41.186  -8.581  1.00 25.69 ? 509  TYR B CB  1 
ATOM   6698 C  CG  . TYR B 1 509 ? 35.383  42.662  -8.706  1.00 25.81 ? 509  TYR B CG  1 
ATOM   6699 C  CD1 . TYR B 1 509 ? 35.111  43.325  -9.905  1.00 26.10 ? 509  TYR B CD1 1 
ATOM   6700 C  CD2 . TYR B 1 509 ? 35.879  43.404  -7.630  1.00 26.50 ? 509  TYR B CD2 1 
ATOM   6701 C  CE1 . TYR B 1 509 ? 35.340  44.680  -10.049 1.00 27.04 ? 509  TYR B CE1 1 
ATOM   6702 C  CE2 . TYR B 1 509 ? 36.111  44.771  -7.755  1.00 27.99 ? 509  TYR B CE2 1 
ATOM   6703 C  CZ  . TYR B 1 509 ? 35.829  45.406  -8.975  1.00 28.56 ? 509  TYR B CZ  1 
ATOM   6704 O  OH  . TYR B 1 509 ? 36.041  46.750  -9.137  1.00 28.19 ? 509  TYR B OH  1 
ATOM   6705 N  N   . SER B 1 510 ? 35.588  38.363  -7.807  1.00 22.49 ? 510  SER B N   1 
ATOM   6706 C  CA  . SER B 1 510 ? 34.868  37.115  -7.595  1.00 23.06 ? 510  SER B CA  1 
ATOM   6707 C  C   . SER B 1 510 ? 33.458  37.171  -8.175  1.00 21.59 ? 510  SER B C   1 
ATOM   6708 O  O   . SER B 1 510 ? 32.845  38.229  -8.173  1.00 22.44 ? 510  SER B O   1 
ATOM   6709 C  CB  . SER B 1 510 ? 34.734  36.852  -6.093  1.00 23.24 ? 510  SER B CB  1 
ATOM   6710 O  OG  . SER B 1 510 ? 35.993  36.578  -5.520  1.00 24.22 ? 510  SER B OG  1 
ATOM   6711 N  N   . PRO B 1 511 ? 32.938  36.030  -8.650  1.00 20.98 ? 511  PRO B N   1 
ATOM   6712 C  CA  . PRO B 1 511 ? 31.562  35.950  -9.176  1.00 20.68 ? 511  PRO B CA  1 
ATOM   6713 C  C   . PRO B 1 511 ? 30.515  36.521  -8.246  1.00 19.87 ? 511  PRO B C   1 
ATOM   6714 O  O   . PRO B 1 511 ? 30.611  36.361  -7.025  1.00 19.92 ? 511  PRO B O   1 
ATOM   6715 C  CB  . PRO B 1 511 ? 31.318  34.447  -9.326  1.00 21.18 ? 511  PRO B CB  1 
ATOM   6716 C  CG  . PRO B 1 511 ? 32.671  33.806  -9.378  1.00 20.64 ? 511  PRO B CG  1 
ATOM   6717 C  CD  . PRO B 1 511 ? 33.672  34.754  -8.792  1.00 20.53 ? 511  PRO B CD  1 
ATOM   6718 N  N   . LEU B 1 512 ? 29.525  37.189  -8.823  1.00 18.64 ? 512  LEU B N   1 
ATOM   6719 C  CA  . LEU B 1 512 ? 28.370  37.657  -8.070  1.00 18.56 ? 512  LEU B CA  1 
ATOM   6720 C  C   . LEU B 1 512 ? 27.508  36.455  -7.674  1.00 18.76 ? 512  LEU B C   1 
ATOM   6721 O  O   . LEU B 1 512 ? 26.949  36.410  -6.575  1.00 18.56 ? 512  LEU B O   1 
ATOM   6722 C  CB  . LEU B 1 512 ? 27.529  38.609  -8.923  1.00 18.61 ? 512  LEU B CB  1 
ATOM   6723 C  CG  . LEU B 1 512 ? 28.182  39.886  -9.445  1.00 19.05 ? 512  LEU B CG  1 
ATOM   6724 C  CD1 . LEU B 1 512 ? 27.234  40.621  -10.385 1.00 19.76 ? 512  LEU B CD1 1 
ATOM   6725 C  CD2 . LEU B 1 512 ? 28.563  40.773  -8.282  1.00 19.57 ? 512  LEU B CD2 1 
ATOM   6726 N  N   . ILE B 1 513 ? 27.405  35.498  -8.597  1.00 17.75 ? 513  ILE B N   1 
ATOM   6727 C  CA  . ILE B 1 513 ? 26.666  34.264  -8.380  1.00 18.85 ? 513  ILE B CA  1 
ATOM   6728 C  C   . ILE B 1 513 ? 27.504  33.135  -8.949  1.00 18.05 ? 513  ILE B C   1 
ATOM   6729 O  O   . ILE B 1 513 ? 28.151  33.296  -9.997  1.00 17.05 ? 513  ILE B O   1 
ATOM   6730 C  CB  . ILE B 1 513 ? 25.299  34.275  -9.120  1.00 19.30 ? 513  ILE B CB  1 
ATOM   6731 C  CG1 . ILE B 1 513 ? 24.401  35.402  -8.615  1.00 20.15 ? 513  ILE B CG1 1 
ATOM   6732 C  CG2 . ILE B 1 513 ? 24.594  32.934  -8.993  1.00 20.00 ? 513  ILE B CG2 1 
ATOM   6733 C  CD1 . ILE B 1 513 ? 23.822  35.171  -7.237  1.00 20.23 ? 513  ILE B CD1 1 
ATOM   6734 N  N   . SER B 1 514 ? 27.495  31.995  -8.263  1.00 17.79 ? 514  SER B N   1 
ATOM   6735 C  CA  . SER B 1 514 ? 28.094  30.794  -8.812  1.00 17.53 ? 514  SER B CA  1 
ATOM   6736 C  C   . SER B 1 514 ? 27.323  29.530  -8.418  1.00 17.87 ? 514  SER B C   1 
ATOM   6737 O  O   . SER B 1 514 ? 26.580  29.503  -7.436  1.00 17.18 ? 514  SER B O   1 
ATOM   6738 C  CB  . SER B 1 514 ? 29.563  30.717  -8.415  1.00 17.66 ? 514  SER B CB  1 
ATOM   6739 O  OG  . SER B 1 514 ? 29.727  30.375  -7.058  1.00 18.11 ? 514  SER B OG  1 
ATOM   6740 N  N   . ALA B 1 515 ? 27.483  28.475  -9.203  1.00 17.71 ? 515  ALA B N   1 
ATOM   6741 C  CA  . ALA B 1 515 ? 26.766  27.244  -8.902  1.00 17.47 ? 515  ALA B CA  1 
ATOM   6742 C  C   . ALA B 1 515 ? 27.672  26.015  -8.944  1.00 16.91 ? 515  ALA B C   1 
ATOM   6743 O  O   . ALA B 1 515 ? 27.343  25.039  -9.610  1.00 15.88 ? 515  ALA B O   1 
ATOM   6744 C  CB  . ALA B 1 515 ? 25.571  27.088  -9.832  1.00 17.51 ? 515  ALA B CB  1 
ATOM   6745 N  N   . PRO B 1 516 ? 28.786  26.033  -8.166  1.00 17.42 ? 516  PRO B N   1 
ATOM   6746 C  CA  . PRO B 1 516 ? 29.577  24.819  -8.013  1.00 17.52 ? 516  PRO B CA  1 
ATOM   6747 C  C   . PRO B 1 516 ? 28.694  23.637  -7.605  1.00 17.61 ? 516  PRO B C   1 
ATOM   6748 O  O   . PRO B 1 516 ? 27.848  23.783  -6.711  1.00 17.15 ? 516  PRO B O   1 
ATOM   6749 C  CB  . PRO B 1 516 ? 30.563  25.170  -6.887  1.00 17.92 ? 516  PRO B CB  1 
ATOM   6750 C  CG  . PRO B 1 516 ? 29.916  26.254  -6.133  1.00 17.84 ? 516  PRO B CG  1 
ATOM   6751 C  CD  . PRO B 1 516 ? 29.198  27.054  -7.190  1.00 17.91 ? 516  PRO B CD  1 
ATOM   6752 N  N   . MET B 1 517 ? 28.875  22.505  -8.292  1.00 18.27 ? 517  MET B N   1 
ATOM   6753 C  CA  . MET B 1 517 ? 28.148  21.241  -8.029  1.00 18.66 ? 517  MET B CA  1 
ATOM   6754 C  C   . MET B 1 517 ? 26.743  21.157  -8.636  1.00 18.86 ? 517  MET B C   1 
ATOM   6755 O  O   . MET B 1 517 ? 26.176  20.063  -8.730  1.00 19.35 ? 517  MET B O   1 
ATOM   6756 C  CB  . MET B 1 517 ? 28.028  20.963  -6.517  1.00 19.06 ? 517  MET B CB  1 
ATOM   6757 C  CG  . MET B 1 517 ? 27.773  19.490  -6.175  1.00 19.00 ? 517  MET B CG  1 
ATOM   6758 S  SD  . MET B 1 517 ? 27.509  19.241  -4.417  1.00 18.57 ? 517  MET B SD  1 
ATOM   6759 C  CE  . MET B 1 517 ? 25.774  19.679  -4.260  1.00 19.60 ? 517  MET B CE  1 
ATOM   6760 N  N   . VAL B 1 518 ? 26.190  22.300  -9.034  1.00 18.51 ? 518  VAL B N   1 
ATOM   6761 C  CA  . VAL B 1 518 ? 24.760  22.452  -9.270  1.00 18.17 ? 518  VAL B CA  1 
ATOM   6762 C  C   . VAL B 1 518 ? 24.406  22.664  -10.752 1.00 17.99 ? 518  VAL B C   1 
ATOM   6763 O  O   . VAL B 1 518 ? 23.531  21.997  -11.268 1.00 18.35 ? 518  VAL B O   1 
ATOM   6764 C  CB  . VAL B 1 518 ? 24.220  23.614  -8.404  1.00 18.59 ? 518  VAL B CB  1 
ATOM   6765 C  CG1 . VAL B 1 518 ? 22.724  23.819  -8.629  1.00 18.47 ? 518  VAL B CG1 1 
ATOM   6766 C  CG2 . VAL B 1 518 ? 24.523  23.351  -6.925  1.00 18.33 ? 518  VAL B CG2 1 
ATOM   6767 N  N   . SER B 1 519 ? 25.053  23.607  -11.425 1.00 17.62 ? 519  SER B N   1 
ATOM   6768 C  CA  . SER B 1 519 ? 24.807  23.824  -12.862 1.00 17.49 ? 519  SER B CA  1 
ATOM   6769 C  C   . SER B 1 519 ? 26.090  24.252  -13.538 1.00 16.66 ? 519  SER B C   1 
ATOM   6770 O  O   . SER B 1 519 ? 26.921  24.924  -12.928 1.00 15.82 ? 519  SER B O   1 
ATOM   6771 C  CB  . SER B 1 519 ? 23.724  24.895  -13.093 1.00 18.17 ? 519  SER B CB  1 
ATOM   6772 O  OG  . SER B 1 519 ? 23.436  25.069  -14.481 1.00 17.88 ? 519  SER B OG  1 
ATOM   6773 N  N   . ASP B 1 520 ? 26.263  23.833  -14.785 1.00 15.89 ? 520  ASP B N   1 
ATOM   6774 C  CA  . ASP B 1 520 ? 27.351  24.346  -15.590 1.00 16.79 ? 520  ASP B CA  1 
ATOM   6775 C  C   . ASP B 1 520 ? 26.872  25.333  -16.657 1.00 16.95 ? 520  ASP B C   1 
ATOM   6776 O  O   . ASP B 1 520 ? 27.613  25.620  -17.597 1.00 16.71 ? 520  ASP B O   1 
ATOM   6777 C  CB  . ASP B 1 520 ? 28.139  23.182  -16.229 1.00 16.95 ? 520  ASP B CB  1 
ATOM   6778 C  CG  . ASP B 1 520 ? 29.666  23.418  -16.261 1.00 17.12 ? 520  ASP B CG  1 
ATOM   6779 O  OD1 . ASP B 1 520 ? 30.225  24.238  -15.502 1.00 17.28 ? 520  ASP B OD1 1 
ATOM   6780 O  OD2 . ASP B 1 520 ? 30.341  22.722  -17.059 1.00 17.75 ? 520  ASP B OD2 1 
ATOM   6781 N  N   . GLU B 1 521 ? 25.668  25.889  -16.524 1.00 18.14 ? 521  GLU B N   1 
ATOM   6782 C  CA  . GLU B 1 521 ? 25.215  26.903  -17.516 1.00 18.81 ? 521  GLU B CA  1 
ATOM   6783 C  C   . GLU B 1 521 ? 24.104  27.811  -17.032 1.00 17.97 ? 521  GLU B C   1 
ATOM   6784 O  O   . GLU B 1 521 ? 22.980  27.374  -16.851 1.00 17.77 ? 521  GLU B O   1 
ATOM   6785 C  CB  . GLU B 1 521 ? 24.769  26.218  -18.821 1.00 20.35 ? 521  GLU B CB  1 
ATOM   6786 C  CG  . GLU B 1 521 ? 24.671  27.181  -20.005 1.00 21.02 ? 521  GLU B CG  1 
ATOM   6787 C  CD  . GLU B 1 521 ? 24.571  26.451  -21.320 1.00 21.88 ? 521  GLU B CD  1 
ATOM   6788 O  OE1 . GLU B 1 521 ? 23.448  26.056  -21.681 1.00 24.40 ? 521  GLU B OE1 1 
ATOM   6789 O  OE2 . GLU B 1 521 ? 25.610  26.286  -21.984 1.00 22.08 ? 521  GLU B OE2 1 
ATOM   6790 N  N   . ILE B 1 522 ? 24.434  29.084  -16.850 1.00 18.23 ? 522  ILE B N   1 
ATOM   6791 C  CA  . ILE B 1 522 ? 23.482  30.128  -16.476 1.00 17.87 ? 522  ILE B CA  1 
ATOM   6792 C  C   . ILE B 1 522 ? 23.778  31.335  -17.358 1.00 17.83 ? 522  ILE B C   1 
ATOM   6793 O  O   . ILE B 1 522 ? 24.899  31.868  -17.356 1.00 17.46 ? 522  ILE B O   1 
ATOM   6794 C  CB  . ILE B 1 522 ? 23.611  30.522  -15.001 1.00 18.32 ? 522  ILE B CB  1 
ATOM   6795 C  CG1 . ILE B 1 522 ? 23.327  29.313  -14.097 1.00 18.62 ? 522  ILE B CG1 1 
ATOM   6796 C  CG2 . ILE B 1 522 ? 22.675  31.677  -14.678 1.00 18.80 ? 522  ILE B CG2 1 
ATOM   6797 C  CD1 . ILE B 1 522 ? 23.624  29.535  -12.633 1.00 18.02 ? 522  ILE B CD1 1 
ATOM   6798 N  N   . GLU B 1 523 ? 22.764  31.757  -18.106 1.00 17.19 ? 523  GLU B N   1 
ATOM   6799 C  CA  . GLU B 1 523 ? 22.966  32.554  -19.299 1.00 17.46 ? 523  GLU B CA  1 
ATOM   6800 C  C   . GLU B 1 523 ? 22.339  33.956  -19.198 1.00 16.84 ? 523  GLU B C   1 
ATOM   6801 O  O   . GLU B 1 523 ? 21.469  34.214  -18.346 1.00 16.78 ? 523  GLU B O   1 
ATOM   6802 C  CB  . GLU B 1 523 ? 22.397  31.785  -20.509 1.00 17.45 ? 523  GLU B CB  1 
ATOM   6803 C  CG  . GLU B 1 523 ? 23.010  30.394  -20.705 1.00 18.36 ? 523  GLU B CG  1 
ATOM   6804 C  CD  . GLU B 1 523 ? 22.548  29.678  -21.979 1.00 18.75 ? 523  GLU B CD  1 
ATOM   6805 O  OE1 . GLU B 1 523 ? 21.334  29.446  -22.158 1.00 19.06 ? 523  GLU B OE1 1 
ATOM   6806 O  OE2 . GLU B 1 523 ? 23.408  29.303  -22.786 1.00 18.71 ? 523  GLU B OE2 1 
ATOM   6807 N  N   . ARG B 1 524 ? 22.787  34.840  -20.079 1.00 16.91 ? 524  ARG B N   1 
ATOM   6808 C  CA  . ARG B 1 524 ? 22.182  36.162  -20.283 1.00 18.41 ? 524  ARG B CA  1 
ATOM   6809 C  C   . ARG B 1 524 ? 22.004  36.953  -18.978 1.00 17.71 ? 524  ARG B C   1 
ATOM   6810 O  O   . ARG B 1 524 ? 20.928  37.440  -18.685 1.00 17.83 ? 524  ARG B O   1 
ATOM   6811 C  CB  . ARG B 1 524 ? 20.849  35.993  -21.023 1.00 20.66 ? 524  ARG B CB  1 
ATOM   6812 C  CG  . ARG B 1 524 ? 21.019  35.491  -22.469 1.00 22.59 ? 524  ARG B CG  1 
ATOM   6813 C  CD  . ARG B 1 524 ? 21.290  36.646  -23.440 1.00 24.90 ? 524  ARG B CD  1 
ATOM   6814 N  NE  . ARG B 1 524 ? 20.014  36.991  -24.090 1.00 28.48 ? 524  ARG B NE  1 
ATOM   6815 C  CZ  . ARG B 1 524 ? 19.574  38.205  -24.379 1.00 27.64 ? 524  ARG B CZ  1 
ATOM   6816 N  NH1 . ARG B 1 524 ? 20.287  39.280  -24.116 1.00 28.05 ? 524  ARG B NH1 1 
ATOM   6817 N  NH2 . ARG B 1 524 ? 18.377  38.326  -24.941 1.00 30.17 ? 524  ARG B NH2 1 
ATOM   6818 N  N   . PRO B 1 525 ? 23.077  37.076  -18.185 1.00 17.43 ? 525  PRO B N   1 
ATOM   6819 C  CA  . PRO B 1 525 ? 22.948  37.845  -16.953 1.00 17.41 ? 525  PRO B CA  1 
ATOM   6820 C  C   . PRO B 1 525 ? 22.598  39.284  -17.278 1.00 17.37 ? 525  PRO B C   1 
ATOM   6821 O  O   . PRO B 1 525 ? 23.010  39.812  -18.314 1.00 16.65 ? 525  PRO B O   1 
ATOM   6822 C  CB  . PRO B 1 525 ? 24.337  37.751  -16.318 1.00 17.48 ? 525  PRO B CB  1 
ATOM   6823 C  CG  . PRO B 1 525 ? 25.255  37.397  -17.433 1.00 17.49 ? 525  PRO B CG  1 
ATOM   6824 C  CD  . PRO B 1 525 ? 24.446  36.586  -18.391 1.00 17.50 ? 525  PRO B CD  1 
ATOM   6825 N  N   . ASN B 1 526 ? 21.846  39.901  -16.387 1.00 16.99 ? 526  ASN B N   1 
ATOM   6826 C  CA  . ASN B 1 526 ? 21.226  41.164  -16.665 1.00 17.88 ? 526  ASN B CA  1 
ATOM   6827 C  C   . ASN B 1 526 ? 21.025  41.876  -15.340 1.00 18.56 ? 526  ASN B C   1 
ATOM   6828 O  O   . ASN B 1 526 ? 20.496  41.297  -14.408 1.00 19.51 ? 526  ASN B O   1 
ATOM   6829 C  CB  . ASN B 1 526 ? 19.893  40.915  -17.347 1.00 17.48 ? 526  ASN B CB  1 
ATOM   6830 C  CG  . ASN B 1 526 ? 19.138  42.186  -17.649 1.00 17.55 ? 526  ASN B CG  1 
ATOM   6831 O  OD1 . ASN B 1 526 ? 19.736  43.241  -17.929 1.00 17.27 ? 526  ASN B OD1 1 
ATOM   6832 N  ND2 . ASN B 1 526 ? 17.813  42.096  -17.602 1.00 16.65 ? 526  ASN B ND2 1 
ATOM   6833 N  N   . VAL B 1 527 ? 21.469  43.115  -15.258 1.00 18.58 ? 527  VAL B N   1 
ATOM   6834 C  CA  . VAL B 1 527 ? 21.320  43.899  -14.046 1.00 19.74 ? 527  VAL B CA  1 
ATOM   6835 C  C   . VAL B 1 527 ? 20.350  45.016  -14.359 1.00 20.04 ? 527  VAL B C   1 
ATOM   6836 O  O   . VAL B 1 527 ? 20.519  45.738  -15.350 1.00 19.90 ? 527  VAL B O   1 
ATOM   6837 C  CB  . VAL B 1 527 ? 22.662  44.473  -13.539 1.00 19.96 ? 527  VAL B CB  1 
ATOM   6838 C  CG1 . VAL B 1 527 ? 22.447  45.328  -12.296 1.00 20.89 ? 527  VAL B CG1 1 
ATOM   6839 C  CG2 . VAL B 1 527 ? 23.642  43.359  -13.213 1.00 19.93 ? 527  VAL B CG2 1 
ATOM   6840 N  N   . VAL B 1 528 ? 19.298  45.128  -13.555 1.00 21.67 ? 528  VAL B N   1 
ATOM   6841 C  CA  . VAL B 1 528 ? 18.421  46.296  -13.643 1.00 22.62 ? 528  VAL B CA  1 
ATOM   6842 C  C   . VAL B 1 528 ? 18.305  47.010  -12.305 1.00 24.22 ? 528  VAL B C   1 
ATOM   6843 O  O   . VAL B 1 528 ? 18.013  46.412  -11.252 1.00 22.68 ? 528  VAL B O   1 
ATOM   6844 C  CB  . VAL B 1 528 ? 17.061  46.040  -14.381 1.00 23.68 ? 528  VAL B CB  1 
ATOM   6845 C  CG1 . VAL B 1 528 ? 16.775  44.568  -14.619 1.00 24.29 ? 528  VAL B CG1 1 
ATOM   6846 C  CG2 . VAL B 1 528 ? 15.882  46.759  -13.739 1.00 23.49 ? 528  VAL B CG2 1 
ATOM   6847 N  N   . LYS B 1 529 ? 18.585  48.310  -12.381 1.00 25.37 ? 529  LYS B N   1 
ATOM   6848 C  CA  . LYS B 1 529 ? 18.534  49.213  -11.254 1.00 27.39 ? 529  LYS B CA  1 
ATOM   6849 C  C   . LYS B 1 529 ? 17.066  49.601  -11.079 1.00 26.15 ? 529  LYS B C   1 
ATOM   6850 O  O   . LYS B 1 529 ? 16.430  50.079  -12.009 1.00 26.09 ? 529  LYS B O   1 
ATOM   6851 C  CB  . LYS B 1 529 ? 19.410  50.433  -11.552 1.00 29.42 ? 529  LYS B CB  1 
ATOM   6852 C  CG  . LYS B 1 529 ? 19.680  51.341  -10.363 1.00 33.46 ? 529  LYS B CG  1 
ATOM   6853 C  CD  . LYS B 1 529 ? 20.252  52.679  -10.817 1.00 34.83 ? 529  LYS B CD  1 
ATOM   6854 C  CE  . LYS B 1 529 ? 20.417  53.647  -9.657  1.00 36.86 ? 529  LYS B CE  1 
ATOM   6855 N  NZ  . LYS B 1 529 ? 21.270  53.081  -8.572  1.00 39.13 ? 529  LYS B NZ  1 
ATOM   6856 N  N   . LEU B 1 530 ? 16.514  49.337  -9.905  1.00 25.42 ? 530  LEU B N   1 
ATOM   6857 C  CA  . LEU B 1 530 ? 15.139  49.728  -9.593  1.00 25.95 ? 530  LEU B CA  1 
ATOM   6858 C  C   . LEU B 1 530 ? 15.169  50.355  -8.222  1.00 26.50 ? 530  LEU B C   1 
ATOM   6859 O  O   . LEU B 1 530 ? 15.626  49.720  -7.265  1.00 26.18 ? 530  LEU B O   1 
ATOM   6860 C  CB  . LEU B 1 530 ? 14.218  48.514  -9.544  1.00 26.09 ? 530  LEU B CB  1 
ATOM   6861 C  CG  . LEU B 1 530 ? 13.866  47.823  -10.851 1.00 26.68 ? 530  LEU B CG  1 
ATOM   6862 C  CD1 . LEU B 1 530 ? 12.987  46.607  -10.553 1.00 26.16 ? 530  LEU B CD1 1 
ATOM   6863 C  CD2 . LEU B 1 530 ? 13.184  48.801  -11.797 1.00 26.22 ? 530  LEU B CD2 1 
ATOM   6864 N  N   . GLY B 1 531 ? 14.679  51.587  -8.129  1.00 28.28 ? 531  GLY B N   1 
ATOM   6865 C  CA  . GLY B 1 531 ? 14.916  52.431  -6.968  1.00 28.99 ? 531  GLY B CA  1 
ATOM   6866 C  C   . GLY B 1 531 ? 16.404  52.527  -6.684  1.00 30.11 ? 531  GLY B C   1 
ATOM   6867 O  O   . GLY B 1 531 ? 17.194  52.905  -7.543  1.00 31.21 ? 531  GLY B O   1 
ATOM   6868 N  N   . ASN B 1 532 ? 16.782  52.132  -5.480  1.00 32.93 ? 532  ASN B N   1 
ATOM   6869 C  CA  . ASN B 1 532 ? 18.163  52.181  -5.045  1.00 35.66 ? 532  ASN B CA  1 
ATOM   6870 C  C   . ASN B 1 532 ? 18.801  50.787  -4.976  1.00 34.43 ? 532  ASN B C   1 
ATOM   6871 O  O   . ASN B 1 532 ? 19.910  50.640  -4.464  1.00 35.95 ? 532  ASN B O   1 
ATOM   6872 C  CB  . ASN B 1 532 ? 18.258  52.906  -3.693  1.00 39.98 ? 532  ASN B CB  1 
ATOM   6873 C  CG  . ASN B 1 532 ? 17.293  52.353  -2.644  1.00 45.04 ? 532  ASN B CG  1 
ATOM   6874 O  OD1 . ASN B 1 532 ? 16.957  51.166  -2.637  1.00 45.73 ? 532  ASN B OD1 1 
ATOM   6875 N  ND2 . ASN B 1 532 ? 16.850  53.225  -1.737  1.00 49.23 ? 532  ASN B ND2 1 
ATOM   6876 N  N   . LYS B 1 533 ? 18.110  49.782  -5.515  1.00 30.93 ? 533  LYS B N   1 
ATOM   6877 C  CA  . LYS B 1 533 ? 18.576  48.401  -5.491  1.00 30.17 ? 533  LYS B CA  1 
ATOM   6878 C  C   . LYS B 1 533 ? 18.981  47.907  -6.877  1.00 27.66 ? 533  LYS B C   1 
ATOM   6879 O  O   . LYS B 1 533 ? 18.599  48.490  -7.883  1.00 25.16 ? 533  LYS B O   1 
ATOM   6880 C  CB  . LYS B 1 533 ? 17.481  47.507  -4.912  1.00 31.65 ? 533  LYS B CB  1 
ATOM   6881 C  CG  . LYS B 1 533 ? 17.217  47.837  -3.449  1.00 33.93 ? 533  LYS B CG  1 
ATOM   6882 C  CD  . LYS B 1 533 ? 16.376  46.805  -2.736  1.00 35.47 ? 533  LYS B CD  1 
ATOM   6883 C  CE  . LYS B 1 533 ? 16.332  47.131  -1.253  1.00 38.77 ? 533  LYS B CE  1 
ATOM   6884 N  NZ  . LYS B 1 533 ? 15.237  46.395  -0.565  1.00 40.53 ? 533  LYS B NZ  1 
ATOM   6885 N  N   . TYR B 1 534 ? 19.758  46.827  -6.900  1.00 25.66 ? 534  TYR B N   1 
ATOM   6886 C  CA  . TYR B 1 534 ? 20.257  46.222  -8.133  1.00 25.47 ? 534  TYR B CA  1 
ATOM   6887 C  C   . TYR B 1 534 ? 19.737  44.793  -8.230  1.00 24.74 ? 534  TYR B C   1 
ATOM   6888 O  O   . TYR B 1 534 ? 19.970  43.966  -7.335  1.00 23.57 ? 534  TYR B O   1 
ATOM   6889 C  CB  . TYR B 1 534 ? 21.791  46.224  -8.159  1.00 25.98 ? 534  TYR B CB  1 
ATOM   6890 C  CG  . TYR B 1 534 ? 22.382  47.612  -8.216  1.00 27.51 ? 534  TYR B CG  1 
ATOM   6891 C  CD1 . TYR B 1 534 ? 22.545  48.358  -7.058  1.00 28.57 ? 534  TYR B CD1 1 
ATOM   6892 C  CD2 . TYR B 1 534 ? 22.739  48.193  -9.431  1.00 27.86 ? 534  TYR B CD2 1 
ATOM   6893 C  CE1 . TYR B 1 534 ? 23.069  49.635  -7.098  1.00 30.30 ? 534  TYR B CE1 1 
ATOM   6894 C  CE2 . TYR B 1 534 ? 23.263  49.470  -9.479  1.00 29.65 ? 534  TYR B CE2 1 
ATOM   6895 C  CZ  . TYR B 1 534 ? 23.425  50.184  -8.310  1.00 30.33 ? 534  TYR B CZ  1 
ATOM   6896 O  OH  . TYR B 1 534 ? 23.947  51.451  -8.338  1.00 34.06 ? 534  TYR B OH  1 
ATOM   6897 N  N   . TYR B 1 535 ? 19.029  44.523  -9.320  1.00 24.13 ? 535  TYR B N   1 
ATOM   6898 C  CA  . TYR B 1 535 ? 18.445  43.219  -9.578  1.00 23.44 ? 535  TYR B CA  1 
ATOM   6899 C  C   . TYR B 1 535 ? 19.247  42.500  -10.645 1.00 23.42 ? 535  TYR B C   1 
ATOM   6900 O  O   . TYR B 1 535 ? 19.470  43.032  -11.740 1.00 22.11 ? 535  TYR B O   1 
ATOM   6901 C  CB  . TYR B 1 535 ? 16.976  43.366  -9.994  1.00 23.98 ? 535  TYR B CB  1 
ATOM   6902 C  CG  . TYR B 1 535 ? 16.127  43.827  -8.833  1.00 24.21 ? 535  TYR B CG  1 
ATOM   6903 C  CD1 . TYR B 1 535 ? 16.056  45.175  -8.494  1.00 24.81 ? 535  TYR B CD1 1 
ATOM   6904 C  CD2 . TYR B 1 535 ? 15.449  42.912  -8.038  1.00 24.03 ? 535  TYR B CD2 1 
ATOM   6905 C  CE1 . TYR B 1 535 ? 15.307  45.603  -7.407  1.00 25.17 ? 535  TYR B CE1 1 
ATOM   6906 C  CE2 . TYR B 1 535 ? 14.694  43.326  -6.953  1.00 24.36 ? 535  TYR B CE2 1 
ATOM   6907 C  CZ  . TYR B 1 535 ? 14.628  44.674  -6.636  1.00 25.00 ? 535  TYR B CZ  1 
ATOM   6908 O  OH  . TYR B 1 535 ? 13.887  45.101  -5.548  1.00 24.96 ? 535  TYR B OH  1 
ATOM   6909 N  N   . LEU B 1 536 ? 19.681  41.289  -10.308 1.00 21.56 ? 536  LEU B N   1 
ATOM   6910 C  CA  . LEU B 1 536 ? 20.433  40.448  -11.216 1.00 20.62 ? 536  LEU B CA  1 
ATOM   6911 C  C   . LEU B 1 536 ? 19.525  39.317  -11.684 1.00 19.66 ? 536  LEU B C   1 
ATOM   6912 O  O   . LEU B 1 536 ? 19.018  38.556  -10.868 1.00 19.36 ? 536  LEU B O   1 
ATOM   6913 C  CB  . LEU B 1 536 ? 21.655  39.891  -10.479 1.00 20.85 ? 536  LEU B CB  1 
ATOM   6914 C  CG  . LEU B 1 536 ? 22.551  38.907  -11.219 1.00 20.28 ? 536  LEU B CG  1 
ATOM   6915 C  CD1 . LEU B 1 536 ? 23.083  39.498  -12.505 1.00 20.31 ? 536  LEU B CD1 1 
ATOM   6916 C  CD2 . LEU B 1 536 ? 23.682  38.496  -10.305 1.00 20.25 ? 536  LEU B CD2 1 
ATOM   6917 N  N   . PHE B 1 537 ? 19.291  39.246  -12.986 1.00 18.47 ? 537  PHE B N   1 
ATOM   6918 C  CA  . PHE B 1 537 ? 18.467  38.209  -13.569 1.00 18.53 ? 537  PHE B CA  1 
ATOM   6919 C  C   . PHE B 1 537 ? 19.315  37.376  -14.522 1.00 18.81 ? 537  PHE B C   1 
ATOM   6920 O  O   . PHE B 1 537 ? 20.307  37.852  -15.064 1.00 17.96 ? 537  PHE B O   1 
ATOM   6921 C  CB  . PHE B 1 537 ? 17.293  38.788  -14.354 1.00 18.71 ? 537  PHE B CB  1 
ATOM   6922 C  CG  . PHE B 1 537 ? 16.350  39.622  -13.537 1.00 18.77 ? 537  PHE B CG  1 
ATOM   6923 C  CD1 . PHE B 1 537 ? 15.505  39.034  -12.629 1.00 19.49 ? 537  PHE B CD1 1 
ATOM   6924 C  CD2 . PHE B 1 537 ? 16.275  40.994  -13.719 1.00 20.02 ? 537  PHE B CD2 1 
ATOM   6925 C  CE1 . PHE B 1 537 ? 14.626  39.790  -11.881 1.00 19.90 ? 537  PHE B CE1 1 
ATOM   6926 C  CE2 . PHE B 1 537 ? 15.388  41.767  -12.983 1.00 20.25 ? 537  PHE B CE2 1 
ATOM   6927 C  CZ  . PHE B 1 537 ? 14.566  41.160  -12.054 1.00 20.83 ? 537  PHE B CZ  1 
ATOM   6928 N  N   . ALA B 1 538 ? 18.937  36.116  -14.708 1.00 17.74 ? 538  ALA B N   1 
ATOM   6929 C  CA  . ALA B 1 538 ? 19.606  35.284  -15.679 1.00 16.58 ? 538  ALA B CA  1 
ATOM   6930 C  C   . ALA B 1 538 ? 18.650  34.215  -16.157 1.00 16.31 ? 538  ALA B C   1 
ATOM   6931 O  O   . ALA B 1 538 ? 17.716  33.841  -15.446 1.00 16.79 ? 538  ALA B O   1 
ATOM   6932 C  CB  . ALA B 1 538 ? 20.847  34.653  -15.069 1.00 16.63 ? 538  ALA B CB  1 
ATOM   6933 N  N   . ALA B 1 539 ? 18.877  33.731  -17.369 1.00 16.03 ? 539  ALA B N   1 
ATOM   6934 C  CA  . ALA B 1 539 ? 18.122  32.621  -17.888 1.00 15.98 ? 539  ALA B CA  1 
ATOM   6935 C  C   . ALA B 1 539 ? 18.925  31.359  -17.703 1.00 16.31 ? 539  ALA B C   1 
ATOM   6936 O  O   . ALA B 1 539 ? 20.163  31.371  -17.771 1.00 15.73 ? 539  ALA B O   1 
ATOM   6937 C  CB  . ALA B 1 539 ? 17.812  32.824  -19.355 1.00 15.83 ? 539  ALA B CB  1 
ATOM   6938 N  N   . THR B 1 540 ? 18.221  30.256  -17.490 1.00 16.65 ? 540  THR B N   1 
ATOM   6939 C  CA  . THR B 1 540 ? 18.874  28.963  -17.446 1.00 17.46 ? 540  THR B CA  1 
ATOM   6940 C  C   . THR B 1 540 ? 17.938  27.855  -17.945 1.00 18.34 ? 540  THR B C   1 
ATOM   6941 O  O   . THR B 1 540 ? 16.707  27.923  -17.785 1.00 16.87 ? 540  THR B O   1 
ATOM   6942 C  CB  . THR B 1 540 ? 19.387  28.657  -16.009 1.00 17.84 ? 540  THR B CB  1 
ATOM   6943 O  OG1 . THR B 1 540 ? 20.302  27.552  -16.031 1.00 18.00 ? 540  THR B OG1 1 
ATOM   6944 C  CG2 . THR B 1 540 ? 18.234  28.348  -15.058 1.00 17.76 ? 540  THR B CG2 1 
ATOM   6945 N  N   . ARG B 1 541 ? 18.534  26.850  -18.575 1.00 19.29 ? 541  ARG B N   1 
ATOM   6946 C  CA  . ARG B 1 541 ? 17.836  25.618  -18.901 1.00 19.70 ? 541  ARG B CA  1 
ATOM   6947 C  C   . ARG B 1 541 ? 18.150  24.641  -17.772 1.00 18.48 ? 541  ARG B C   1 
ATOM   6948 O  O   . ARG B 1 541 ? 19.305  24.278  -17.543 1.00 16.95 ? 541  ARG B O   1 
ATOM   6949 C  CB  . ARG B 1 541 ? 18.289  25.064  -20.268 1.00 21.00 ? 541  ARG B CB  1 
ATOM   6950 C  CG  . ARG B 1 541 ? 17.994  25.988  -21.434 1.00 23.34 ? 541  ARG B CG  1 
ATOM   6951 C  CD  . ARG B 1 541 ? 17.840  25.236  -22.763 1.00 25.36 ? 541  ARG B CD  1 
ATOM   6952 N  NE  . ARG B 1 541 ? 17.633  26.143  -23.896 1.00 26.49 ? 541  ARG B NE  1 
ATOM   6953 C  CZ  . ARG B 1 541 ? 16.459  26.417  -24.483 1.00 30.11 ? 541  ARG B CZ  1 
ATOM   6954 N  NH1 . ARG B 1 541 ? 15.315  25.857  -24.092 1.00 31.14 ? 541  ARG B NH1 1 
ATOM   6955 N  NH2 . ARG B 1 541 ? 16.417  27.273  -25.501 1.00 32.06 ? 541  ARG B NH2 1 
ATOM   6956 N  N   . LEU B 1 542 ? 17.131  24.197  -17.050 1.00 18.85 ? 542  LEU B N   1 
ATOM   6957 C  CA  . LEU B 1 542 ? 17.398  23.321  -15.894 1.00 18.10 ? 542  LEU B CA  1 
ATOM   6958 C  C   . LEU B 1 542 ? 18.029  21.973  -16.283 1.00 17.55 ? 542  LEU B C   1 
ATOM   6959 O  O   . LEU B 1 542 ? 18.603  21.304  -15.430 1.00 16.94 ? 542  LEU B O   1 
ATOM   6960 C  CB  . LEU B 1 542 ? 16.162  23.137  -15.027 1.00 17.44 ? 542  LEU B CB  1 
ATOM   6961 C  CG  . LEU B 1 542 ? 15.640  24.430  -14.405 1.00 18.03 ? 542  LEU B CG  1 
ATOM   6962 C  CD1 . LEU B 1 542 ? 14.242  24.189  -13.844 1.00 18.36 ? 542  LEU B CD1 1 
ATOM   6963 C  CD2 . LEU B 1 542 ? 16.560  25.007  -13.326 1.00 17.92 ? 542  LEU B CD2 1 
ATOM   6964 N  N   . ASN B 1 543 ? 17.970  21.581  -17.557 1.00 17.77 ? 543  ASN B N   1 
ATOM   6965 C  CA  . ASN B 1 543 ? 18.651  20.360  -17.978 1.00 18.54 ? 543  ASN B CA  1 
ATOM   6966 C  C   . ASN B 1 543 ? 20.165  20.503  -18.133 1.00 19.66 ? 543  ASN B C   1 
ATOM   6967 O  O   . ASN B 1 543 ? 20.847  19.550  -18.496 1.00 20.13 ? 543  ASN B O   1 
ATOM   6968 C  CB  . ASN B 1 543 ? 18.012  19.747  -19.215 1.00 18.66 ? 543  ASN B CB  1 
ATOM   6969 C  CG  . ASN B 1 543 ? 18.177  20.593  -20.456 1.00 19.47 ? 543  ASN B CG  1 
ATOM   6970 O  OD1 . ASN B 1 543 ? 18.808  21.655  -20.438 1.00 19.10 ? 543  ASN B OD1 1 
ATOM   6971 N  ND2 . ASN B 1 543 ? 17.595  20.122  -21.555 1.00 20.10 ? 543  ASN B ND2 1 
ATOM   6972 N  N   . ARG B 1 544 ? 20.697  21.692  -17.853 1.00 20.55 ? 544  ARG B N   1 
ATOM   6973 C  CA  . ARG B 1 544 ? 22.127  21.864  -17.719 1.00 21.75 ? 544  ARG B CA  1 
ATOM   6974 C  C   . ARG B 1 544 ? 22.580  21.707  -16.258 1.00 21.69 ? 544  ARG B C   1 
ATOM   6975 O  O   . ARG B 1 544 ? 23.761  21.877  -15.963 1.00 21.78 ? 544  ARG B O   1 
ATOM   6976 C  CB  . ARG B 1 544 ? 22.563  23.233  -18.249 1.00 24.43 ? 544  ARG B CB  1 
ATOM   6977 C  CG  . ARG B 1 544 ? 22.035  23.601  -19.623 1.00 27.27 ? 544  ARG B CG  1 
ATOM   6978 C  CD  . ARG B 1 544 ? 22.219  22.501  -20.639 1.00 29.98 ? 544  ARG B CD  1 
ATOM   6979 N  NE  . ARG B 1 544 ? 22.288  23.063  -21.985 1.00 32.53 ? 544  ARG B NE  1 
ATOM   6980 C  CZ  . ARG B 1 544 ? 21.329  23.023  -22.914 1.00 32.98 ? 544  ARG B CZ  1 
ATOM   6981 N  NH1 . ARG B 1 544 ? 20.150  22.445  -22.695 1.00 34.16 ? 544  ARG B NH1 1 
ATOM   6982 N  NH2 . ARG B 1 544 ? 21.558  23.592  -24.089 1.00 33.20 ? 544  ARG B NH2 1 
ATOM   6983 N  N   . GLY B 1 545 ? 21.642  21.399  -15.358 1.00 21.25 ? 545  GLY B N   1 
ATOM   6984 C  CA  . GLY B 1 545 ? 21.929  21.140  -13.945 1.00 20.52 ? 545  GLY B CA  1 
ATOM   6985 C  C   . GLY B 1 545 ? 22.305  19.688  -13.642 1.00 20.36 ? 545  GLY B C   1 
ATOM   6986 O  O   . GLY B 1 545 ? 22.035  18.782  -14.431 1.00 18.36 ? 545  GLY B O   1 
ATOM   6987 N  N   . SER B 1 546 ? 22.941  19.473  -12.491 1.00 19.50 ? 546  SER B N   1 
ATOM   6988 C  CA  . SER B 1 546 ? 23.345  18.116  -12.084 1.00 19.81 ? 546  SER B CA  1 
ATOM   6989 C  C   . SER B 1 546 ? 22.172  17.273  -11.587 1.00 18.77 ? 546  SER B C   1 
ATOM   6990 O  O   . SER B 1 546 ? 22.190  16.057  -11.690 1.00 21.20 ? 546  SER B O   1 
ATOM   6991 C  CB  . SER B 1 546 ? 24.436  18.195  -11.005 1.00 18.70 ? 546  SER B CB  1 
ATOM   6992 O  OG  . SER B 1 546 ? 24.014  19.006  -9.939  1.00 18.04 ? 546  SER B OG  1 
ATOM   6993 N  N   . ASN B 1 547 ? 21.154  17.917  -11.048 1.00 19.03 ? 547  ASN B N   1 
ATOM   6994 C  CA  . ASN B 1 547 ? 20.002  17.201  -10.496 1.00 19.48 ? 547  ASN B CA  1 
ATOM   6995 C  C   . ASN B 1 547 ? 19.067  16.677  -11.599 1.00 19.37 ? 547  ASN B C   1 
ATOM   6996 O  O   . ASN B 1 547 ? 18.051  17.292  -11.937 1.00 17.52 ? 547  ASN B O   1 
ATOM   6997 C  CB  . ASN B 1 547 ? 19.272  18.097  -9.499  1.00 19.31 ? 547  ASN B CB  1 
ATOM   6998 C  CG  . ASN B 1 547 ? 18.213  17.360  -8.695  1.00 18.89 ? 547  ASN B CG  1 
ATOM   6999 O  OD1 . ASN B 1 547 ? 17.698  16.325  -9.101  1.00 18.25 ? 547  ASN B OD1 1 
ATOM   7000 N  ND2 . ASN B 1 547 ? 17.842  17.938  -7.566  1.00 19.30 ? 547  ASN B ND2 1 
ATOM   7001 N  N   . ASP B 1 548 ? 19.447  15.525  -12.149 1.00 19.74 ? 548  ASP B N   1 
ATOM   7002 C  CA  . ASP B 1 548 ? 18.700  14.882  -13.225 1.00 20.17 ? 548  ASP B CA  1 
ATOM   7003 C  C   . ASP B 1 548 ? 17.244  14.625  -12.863 1.00 20.95 ? 548  ASP B C   1 
ATOM   7004 O  O   . ASP B 1 548 ? 16.367  14.806  -13.721 1.00 20.21 ? 548  ASP B O   1 
ATOM   7005 C  CB  . ASP B 1 548 ? 19.352  13.564  -13.642 1.00 20.83 ? 548  ASP B CB  1 
ATOM   7006 C  CG  . ASP B 1 548 ? 20.614  13.760  -14.473 1.00 21.23 ? 548  ASP B CG  1 
ATOM   7007 O  OD1 . ASP B 1 548 ? 20.999  14.923  -14.789 1.00 21.92 ? 548  ASP B OD1 1 
ATOM   7008 O  OD2 . ASP B 1 548 ? 21.217  12.725  -14.815 1.00 19.96 ? 548  ASP B OD2 1 
ATOM   7009 N  N   . ASP B 1 549 ? 16.983  14.214  -11.616 1.00 20.73 ? 549  ASP B N   1 
ATOM   7010 C  CA  . ASP B 1 549 ? 15.612  13.948  -11.183 1.00 21.70 ? 549  ASP B CA  1 
ATOM   7011 C  C   . ASP B 1 549 ? 14.759  15.207  -11.331 1.00 21.17 ? 549  ASP B C   1 
ATOM   7012 O  O   . ASP B 1 549 ? 13.666  15.155  -11.872 1.00 20.82 ? 549  ASP B O   1 
ATOM   7013 C  CB  . ASP B 1 549 ? 15.558  13.448  -9.732  1.00 22.81 ? 549  ASP B CB  1 
ATOM   7014 C  CG  . ASP B 1 549 ? 16.291  12.113  -9.541  1.00 23.98 ? 549  ASP B CG  1 
ATOM   7015 O  OD1 . ASP B 1 549 ? 16.383  11.322  -10.497 1.00 24.30 ? 549  ASP B OD1 1 
ATOM   7016 O  OD2 . ASP B 1 549 ? 16.806  11.862  -8.436  1.00 24.75 ? 549  ASP B OD2 1 
ATOM   7017 N  N   . ALA B 1 550 ? 15.293  16.336  -10.882 1.00 20.79 ? 550  ALA B N   1 
ATOM   7018 C  CA  . ALA B 1 550 ? 14.576  17.597  -10.909 1.00 20.11 ? 550  ALA B CA  1 
ATOM   7019 C  C   . ALA B 1 550 ? 14.205  18.015  -12.327 1.00 19.69 ? 550  ALA B C   1 
ATOM   7020 O  O   . ALA B 1 550 ? 13.053  18.369  -12.595 1.00 19.10 ? 550  ALA B O   1 
ATOM   7021 C  CB  . ALA B 1 550 ? 15.390  18.683  -10.219 1.00 20.03 ? 550  ALA B CB  1 
ATOM   7022 N  N   . TRP B 1 551 ? 15.156  17.962  -13.250 1.00 20.22 ? 551  TRP B N   1 
ATOM   7023 C  CA  . TRP B 1 551 ? 14.840  18.432  -14.609 1.00 20.38 ? 551  TRP B CA  1 
ATOM   7024 C  C   . TRP B 1 551 ? 14.072  17.437  -15.448 1.00 19.74 ? 551  TRP B C   1 
ATOM   7025 O  O   . TRP B 1 551 ? 13.301  17.839  -16.325 1.00 19.99 ? 551  TRP B O   1 
ATOM   7026 C  CB  . TRP B 1 551 ? 16.057  18.980  -15.363 1.00 20.34 ? 551  TRP B CB  1 
ATOM   7027 C  CG  . TRP B 1 551 ? 17.195  18.053  -15.704 1.00 20.44 ? 551  TRP B CG  1 
ATOM   7028 C  CD1 . TRP B 1 551 ? 18.406  17.985  -15.067 1.00 20.51 ? 551  TRP B CD1 1 
ATOM   7029 C  CD2 . TRP B 1 551 ? 17.290  17.170  -16.835 1.00 20.09 ? 551  TRP B CD2 1 
ATOM   7030 N  NE1 . TRP B 1 551 ? 19.224  17.079  -15.699 1.00 20.12 ? 551  TRP B NE1 1 
ATOM   7031 C  CE2 . TRP B 1 551 ? 18.566  16.565  -16.787 1.00 19.83 ? 551  TRP B CE2 1 
ATOM   7032 C  CE3 . TRP B 1 551 ? 16.410  16.810  -17.864 1.00 19.79 ? 551  TRP B CE3 1 
ATOM   7033 C  CZ2 . TRP B 1 551 ? 18.987  15.617  -17.728 1.00 19.62 ? 551  TRP B CZ2 1 
ATOM   7034 C  CZ3 . TRP B 1 551 ? 16.822  15.867  -18.793 1.00 19.50 ? 551  TRP B CZ3 1 
ATOM   7035 C  CH2 . TRP B 1 551 ? 18.107  15.283  -18.720 1.00 19.92 ? 551  TRP B CH2 1 
ATOM   7036 N  N   . MET B 1 552 ? 14.259  16.148  -15.190 1.00 19.85 ? 552  MET B N   1 
ATOM   7037 C  CA  . MET B 1 552 ? 13.453  15.137  -15.871 1.00 20.53 ? 552  MET B CA  1 
ATOM   7038 C  C   . MET B 1 552 ? 11.987  15.249  -15.429 1.00 20.38 ? 552  MET B C   1 
ATOM   7039 O  O   . MET B 1 552 ? 11.078  15.164  -16.258 1.00 20.33 ? 552  MET B O   1 
ATOM   7040 C  CB  . MET B 1 552 ? 13.996  13.723  -15.634 1.00 21.86 ? 552  MET B CB  1 
ATOM   7041 C  CG  . MET B 1 552 ? 15.292  13.426  -16.365 1.00 22.70 ? 552  MET B CG  1 
ATOM   7042 S  SD  . MET B 1 552 ? 16.026  11.836  -15.917 1.00 23.47 ? 552  MET B SD  1 
ATOM   7043 C  CE  . MET B 1 552 ? 17.575  11.905  -16.805 1.00 25.75 ? 552  MET B CE  1 
ATOM   7044 N  N   . ASN B 1 553 ? 11.762  15.458  -14.131 1.00 21.23 ? 553  ASN B N   1 
ATOM   7045 C  CA  . ASN B 1 553 ? 10.421  15.741  -13.618 1.00 21.47 ? 553  ASN B CA  1 
ATOM   7046 C  C   . ASN B 1 553 ? 9.826   17.022  -14.209 1.00 21.10 ? 553  ASN B C   1 
ATOM   7047 O  O   . ASN B 1 553 ? 8.628   17.091  -14.471 1.00 19.66 ? 553  ASN B O   1 
ATOM   7048 C  CB  . ASN B 1 553 ? 10.429  15.850  -12.099 1.00 22.52 ? 553  ASN B CB  1 
ATOM   7049 C  CG  . ASN B 1 553 ? 10.580  14.503  -11.416 1.00 23.48 ? 553  ASN B CG  1 
ATOM   7050 O  OD1 . ASN B 1 553 ? 10.250  13.478  -11.988 1.00 24.41 ? 553  ASN B OD1 1 
ATOM   7051 N  ND2 . ASN B 1 553 ? 11.079  14.509  -10.178 1.00 23.67 ? 553  ASN B ND2 1 
ATOM   7052 N  N   . ALA B 1 554 ? 10.661  18.032  -14.415 1.00 20.41 ? 554  ALA B N   1 
ATOM   7053 C  CA  . ALA B 1 554 ? 10.201  19.259  -15.044 1.00 20.03 ? 554  ALA B CA  1 
ATOM   7054 C  C   . ALA B 1 554 ? 9.681   18.950  -16.443 1.00 19.73 ? 554  ALA B C   1 
ATOM   7055 O  O   . ALA B 1 554 ? 8.621   19.439  -16.840 1.00 18.88 ? 554  ALA B O   1 
ATOM   7056 C  CB  . ALA B 1 554 ? 11.323  20.281  -15.101 1.00 19.78 ? 554  ALA B CB  1 
ATOM   7057 N  N   . ASN B 1 555 ? 10.441  18.134  -17.176 1.00 20.50 ? 555  ASN B N   1 
ATOM   7058 C  CA  . ASN B 1 555 ? 10.091  17.739  -18.529 1.00 21.51 ? 555  ASN B CA  1 
ATOM   7059 C  C   . ASN B 1 555 ? 8.787   16.941  -18.564 1.00 24.33 ? 555  ASN B C   1 
ATOM   7060 O  O   . ASN B 1 555 ? 7.954   17.134  -19.449 1.00 25.36 ? 555  ASN B O   1 
ATOM   7061 C  CB  . ASN B 1 555 ? 11.237  16.943  -19.174 1.00 21.05 ? 555  ASN B CB  1 
ATOM   7062 C  CG  . ASN B 1 555 ? 12.373  17.838  -19.653 1.00 19.69 ? 555  ASN B CG  1 
ATOM   7063 O  OD1 . ASN B 1 555 ? 12.257  19.066  -19.663 1.00 19.05 ? 555  ASN B OD1 1 
ATOM   7064 N  ND2 . ASN B 1 555 ? 13.467  17.232  -20.043 1.00 19.12 ? 555  ASN B ND2 1 
ATOM   7065 N  N   . TYR B 1 556 ? 8.608   16.080  -17.573 1.00 26.88 ? 556  TYR B N   1 
ATOM   7066 C  CA  . TYR B 1 556 ? 7.403   15.275  -17.435 1.00 29.37 ? 556  TYR B CA  1 
ATOM   7067 C  C   . TYR B 1 556 ? 6.204   16.192  -17.205 1.00 27.37 ? 556  TYR B C   1 
ATOM   7068 O  O   . TYR B 1 556 ? 5.184   16.089  -17.894 1.00 25.97 ? 556  TYR B O   1 
ATOM   7069 C  CB  . TYR B 1 556 ? 7.591   14.299  -16.261 1.00 34.66 ? 556  TYR B CB  1 
ATOM   7070 C  CG  . TYR B 1 556 ? 6.566   13.189  -16.141 1.00 41.30 ? 556  TYR B CG  1 
ATOM   7071 C  CD1 . TYR B 1 556 ? 6.500   12.172  -17.090 1.00 44.29 ? 556  TYR B CD1 1 
ATOM   7072 C  CD2 . TYR B 1 556 ? 5.690   13.127  -15.044 1.00 47.08 ? 556  TYR B CD2 1 
ATOM   7073 C  CE1 . TYR B 1 556 ? 5.562   11.150  -16.981 1.00 47.80 ? 556  TYR B CE1 1 
ATOM   7074 C  CE2 . TYR B 1 556 ? 4.757   12.100  -14.919 1.00 48.90 ? 556  TYR B CE2 1 
ATOM   7075 C  CZ  . TYR B 1 556 ? 4.695   11.114  -15.895 1.00 48.38 ? 556  TYR B CZ  1 
ATOM   7076 O  OH  . TYR B 1 556 ? 3.780   10.090  -15.799 1.00 49.19 ? 556  TYR B OH  1 
ATOM   7077 N  N   . ALA B 1 557 ? 6.350   17.126  -16.273 1.00 25.04 ? 557  ALA B N   1 
ATOM   7078 C  CA  . ALA B 1 557 ? 5.226   17.940  -15.841 1.00 25.56 ? 557  ALA B CA  1 
ATOM   7079 C  C   . ALA B 1 557 ? 4.804   18.995  -16.872 1.00 25.34 ? 557  ALA B C   1 
ATOM   7080 O  O   . ALA B 1 557 ? 3.630   19.252  -17.031 1.00 24.88 ? 557  ALA B O   1 
ATOM   7081 C  CB  . ALA B 1 557 ? 5.549   18.598  -14.515 1.00 25.71 ? 557  ALA B CB  1 
ATOM   7082 N  N   . VAL B 1 558 ? 5.770   19.602  -17.561 1.00 24.83 ? 558  VAL B N   1 
ATOM   7083 C  CA  . VAL B 1 558 ? 5.512   20.782  -18.404 1.00 23.25 ? 558  VAL B CA  1 
ATOM   7084 C  C   . VAL B 1 558 ? 5.914   20.586  -19.862 1.00 21.72 ? 558  VAL B C   1 
ATOM   7085 O  O   . VAL B 1 558 ? 5.331   21.222  -20.752 1.00 22.02 ? 558  VAL B O   1 
ATOM   7086 C  CB  . VAL B 1 558 ? 6.270   21.996  -17.831 1.00 23.66 ? 558  VAL B CB  1 
ATOM   7087 C  CG1 . VAL B 1 558 ? 6.203   23.197  -18.757 1.00 24.48 ? 558  VAL B CG1 1 
ATOM   7088 C  CG2 . VAL B 1 558 ? 5.713   22.337  -16.465 1.00 24.22 ? 558  VAL B CG2 1 
ATOM   7089 N  N   . GLY B 1 559 ? 6.910   19.727  -20.096 1.00 19.94 ? 559  GLY B N   1 
ATOM   7090 C  CA  . GLY B 1 559 ? 7.473   19.502  -21.423 1.00 18.92 ? 559  GLY B CA  1 
ATOM   7091 C  C   . GLY B 1 559 ? 8.625   20.441  -21.743 1.00 18.61 ? 559  GLY B C   1 
ATOM   7092 O  O   . GLY B 1 559 ? 9.084   20.524  -22.897 1.00 18.49 ? 559  GLY B O   1 
ATOM   7093 N  N   . ASP B 1 560 ? 9.063   21.195  -20.741 1.00 17.84 ? 560  ASP B N   1 
ATOM   7094 C  CA  . ASP B 1 560 ? 10.241  22.037  -20.869 1.00 17.94 ? 560  ASP B CA  1 
ATOM   7095 C  C   . ASP B 1 560 ? 10.804  22.262  -19.464 1.00 17.61 ? 560  ASP B C   1 
ATOM   7096 O  O   . ASP B 1 560 ? 10.184  21.849  -18.471 1.00 17.23 ? 560  ASP B O   1 
ATOM   7097 C  CB  . ASP B 1 560 ? 9.899   23.368  -21.560 1.00 18.02 ? 560  ASP B CB  1 
ATOM   7098 C  CG  . ASP B 1 560 ? 11.116  24.025  -22.237 1.00 18.69 ? 560  ASP B CG  1 
ATOM   7099 O  OD1 . ASP B 1 560 ? 12.260  23.551  -22.029 1.00 18.93 ? 560  ASP B OD1 1 
ATOM   7100 O  OD2 . ASP B 1 560 ? 10.925  25.011  -22.980 1.00 17.95 ? 560  ASP B OD2 1 
ATOM   7101 N  N   . ASN B 1 561 ? 11.963  22.920  -19.399 1.00 16.58 ? 561  ASN B N   1 
ATOM   7102 C  CA  . ASN B 1 561 ? 12.723  23.069  -18.159 1.00 16.62 ? 561  ASN B CA  1 
ATOM   7103 C  C   . ASN B 1 561 ? 13.456  24.426  -18.050 1.00 16.73 ? 561  ASN B C   1 
ATOM   7104 O  O   . ASN B 1 561 ? 14.422  24.563  -17.279 1.00 15.27 ? 561  ASN B O   1 
ATOM   7105 C  CB  . ASN B 1 561 ? 13.734  21.915  -18.057 1.00 16.31 ? 561  ASN B CB  1 
ATOM   7106 C  CG  . ASN B 1 561 ? 14.682  21.876  -19.242 1.00 16.40 ? 561  ASN B CG  1 
ATOM   7107 O  OD1 . ASN B 1 561 ? 15.583  22.722  -19.361 1.00 17.46 ? 561  ASN B OD1 1 
ATOM   7108 N  ND2 . ASN B 1 561 ? 14.471  20.925  -20.143 1.00 16.01 ? 561  ASN B ND2 1 
ATOM   7109 N  N   . VAL B 1 562 ? 12.975  25.431  -18.789 1.00 16.83 ? 562  VAL B N   1 
ATOM   7110 C  CA  . VAL B 1 562 ? 13.607  26.738  -18.791 1.00 16.70 ? 562  VAL B CA  1 
ATOM   7111 C  C   . VAL B 1 562 ? 13.048  27.611  -17.671 1.00 16.02 ? 562  VAL B C   1 
ATOM   7112 O  O   . VAL B 1 562 ? 11.912  27.412  -17.195 1.00 15.96 ? 562  VAL B O   1 
ATOM   7113 C  CB  . VAL B 1 562 ? 13.501  27.450  -20.173 1.00 18.22 ? 562  VAL B CB  1 
ATOM   7114 C  CG1 . VAL B 1 562 ? 14.091  26.568  -21.260 1.00 18.12 ? 562  VAL B CG1 1 
ATOM   7115 C  CG2 . VAL B 1 562 ? 12.073  27.878  -20.519 1.00 18.53 ? 562  VAL B CG2 1 
ATOM   7116 N  N   . ALA B 1 563 ? 13.877  28.554  -17.242 1.00 15.00 ? 563  ALA B N   1 
ATOM   7117 C  CA  . ALA B 1 563 ? 13.565  29.461  -16.156 1.00 14.50 ? 563  ALA B CA  1 
ATOM   7118 C  C   . ALA B 1 563 ? 14.339  30.768  -16.277 1.00 14.18 ? 563  ALA B C   1 
ATOM   7119 O  O   . ALA B 1 563 ? 15.363  30.819  -16.932 1.00 14.17 ? 563  ALA B O   1 
ATOM   7120 C  CB  . ALA B 1 563 ? 13.893  28.792  -14.828 1.00 14.67 ? 563  ALA B CB  1 
ATOM   7121 N  N   . MET B 1 564 ? 13.831  31.820  -15.639 1.00 14.49 ? 564  MET B N   1 
ATOM   7122 C  CA  . MET B 1 564 ? 14.621  32.995  -15.318 1.00 15.01 ? 564  MET B CA  1 
ATOM   7123 C  C   . MET B 1 564 ? 14.739  33.027  -13.801 1.00 15.01 ? 564  MET B C   1 
ATOM   7124 O  O   . MET B 1 564 ? 13.749  32.858  -13.086 1.00 15.88 ? 564  MET B O   1 
ATOM   7125 C  CB  . MET B 1 564 ? 13.976  34.310  -15.830 1.00 15.91 ? 564  MET B CB  1 
ATOM   7126 C  CG  . MET B 1 564 ? 14.936  35.507  -15.859 1.00 16.14 ? 564  MET B CG  1 
ATOM   7127 S  SD  . MET B 1 564 ? 14.162  37.080  -16.352 1.00 17.42 ? 564  MET B SD  1 
ATOM   7128 C  CE  . MET B 1 564 ? 13.124  37.483  -14.950 1.00 17.58 ? 564  MET B CE  1 
ATOM   7129 N  N   . VAL B 1 565 ? 15.953  33.237  -13.321 1.00 14.66 ? 565  VAL B N   1 
ATOM   7130 C  CA  . VAL B 1 565 ? 16.205  33.405  -11.903 1.00 14.83 ? 565  VAL B CA  1 
ATOM   7131 C  C   . VAL B 1 565 ? 16.558  34.859  -11.615 1.00 15.08 ? 565  VAL B C   1 
ATOM   7132 O  O   . VAL B 1 565 ? 16.855  35.650  -12.526 1.00 15.12 ? 565  VAL B O   1 
ATOM   7133 C  CB  . VAL B 1 565 ? 17.336  32.484  -11.405 1.00 14.68 ? 565  VAL B CB  1 
ATOM   7134 C  CG1 . VAL B 1 565 ? 16.910  31.037  -11.539 1.00 15.06 ? 565  VAL B CG1 1 
ATOM   7135 C  CG2 . VAL B 1 565 ? 18.633  32.731  -12.167 1.00 14.82 ? 565  VAL B CG2 1 
ATOM   7136 N  N   . GLY B 1 566 ? 16.527  35.219  -10.344 1.00 15.55 ? 566  GLY B N   1 
ATOM   7137 C  CA  . GLY B 1 566 ? 16.794  36.592  -9.973  1.00 16.46 ? 566  GLY B CA  1 
ATOM   7138 C  C   . GLY B 1 566 ? 17.218  36.790  -8.541  1.00 16.42 ? 566  GLY B C   1 
ATOM   7139 O  O   . GLY B 1 566 ? 16.841  36.006  -7.653  1.00 15.40 ? 566  GLY B O   1 
ATOM   7140 N  N   . TYR B 1 567 ? 18.010  37.846  -8.349  1.00 16.81 ? 567  TYR B N   1 
ATOM   7141 C  CA  . TYR B 1 567 ? 18.623  38.186  -7.074  1.00 17.78 ? 567  TYR B CA  1 
ATOM   7142 C  C   . TYR B 1 567 ? 18.619  39.710  -6.894  1.00 19.23 ? 567  TYR B C   1 
ATOM   7143 O  O   . TYR B 1 567 ? 18.502  40.457  -7.873  1.00 19.02 ? 567  TYR B O   1 
ATOM   7144 C  CB  . TYR B 1 567 ? 20.065  37.657  -7.034  1.00 18.28 ? 567  TYR B CB  1 
ATOM   7145 C  CG  . TYR B 1 567 ? 20.196  36.181  -7.395  1.00 18.47 ? 567  TYR B CG  1 
ATOM   7146 C  CD1 . TYR B 1 567 ? 20.179  35.780  -8.716  1.00 18.41 ? 567  TYR B CD1 1 
ATOM   7147 C  CD2 . TYR B 1 567 ? 20.310  35.199  -6.411  1.00 18.95 ? 567  TYR B CD2 1 
ATOM   7148 C  CE1 . TYR B 1 567 ? 20.265  34.454  -9.062  1.00 19.83 ? 567  TYR B CE1 1 
ATOM   7149 C  CE2 . TYR B 1 567 ? 20.401  33.849  -6.747  1.00 19.22 ? 567  TYR B CE2 1 
ATOM   7150 C  CZ  . TYR B 1 567 ? 20.389  33.485  -8.083  1.00 19.48 ? 567  TYR B CZ  1 
ATOM   7151 O  OH  . TYR B 1 567 ? 20.497  32.178  -8.479  1.00 19.21 ? 567  TYR B OH  1 
ATOM   7152 N  N   . VAL B 1 568 ? 18.747  40.161  -5.649  1.00 19.92 ? 568  VAL B N   1 
ATOM   7153 C  CA  . VAL B 1 568 ? 18.778  41.592  -5.343  1.00 21.12 ? 568  VAL B CA  1 
ATOM   7154 C  C   . VAL B 1 568 ? 19.942  41.920  -4.406  1.00 21.01 ? 568  VAL B C   1 
ATOM   7155 O  O   . VAL B 1 568 ? 20.276  41.133  -3.515  1.00 19.67 ? 568  VAL B O   1 
ATOM   7156 C  CB  . VAL B 1 568 ? 17.435  42.085  -4.743  1.00 21.45 ? 568  VAL B CB  1 
ATOM   7157 C  CG1 . VAL B 1 568 ? 17.194  41.505  -3.363  1.00 21.59 ? 568  VAL B CG1 1 
ATOM   7158 C  CG2 . VAL B 1 568 ? 17.385  43.605  -4.679  1.00 22.47 ? 568  VAL B CG2 1 
ATOM   7159 N  N   . ALA B 1 569 ? 20.566  43.072  -4.644  1.00 21.72 ? 569  ALA B N   1 
ATOM   7160 C  CA  . ALA B 1 569 ? 21.627  43.612  -3.782  1.00 21.60 ? 569  ALA B CA  1 
ATOM   7161 C  C   . ALA B 1 569 ? 21.449  45.126  -3.625  1.00 22.73 ? 569  ALA B C   1 
ATOM   7162 O  O   . ALA B 1 569 ? 20.807  45.771  -4.456  1.00 21.84 ? 569  ALA B O   1 
ATOM   7163 C  CB  . ALA B 1 569 ? 22.996  43.296  -4.356  1.00 21.39 ? 569  ALA B CB  1 
ATOM   7164 N  N   . ASP B 1 570 ? 22.015  45.668  -2.546  1.00 24.55 ? 570  ASP B N   1 
ATOM   7165 C  CA  . ASP B 1 570 ? 22.006  47.095  -2.239  1.00 26.42 ? 570  ASP B CA  1 
ATOM   7166 C  C   . ASP B 1 570 ? 23.034  47.878  -3.033  1.00 27.60 ? 570  ASP B C   1 
ATOM   7167 O  O   . ASP B 1 570 ? 23.049  49.095  -2.966  1.00 26.32 ? 570  ASP B O   1 
ATOM   7168 C  CB  . ASP B 1 570 ? 22.324  47.334  -0.754  1.00 28.35 ? 570  ASP B CB  1 
ATOM   7169 C  CG  . ASP B 1 570 ? 21.228  46.866  0.170   1.00 29.83 ? 570  ASP B CG  1 
ATOM   7170 O  OD1 . ASP B 1 570 ? 20.051  46.808  -0.248  1.00 32.07 ? 570  ASP B OD1 1 
ATOM   7171 O  OD2 . ASP B 1 570 ? 21.547  46.589  1.345   1.00 33.48 ? 570  ASP B OD2 1 
ATOM   7172 N  N   . SER B 1 571 ? 23.935  47.188  -3.726  1.00 29.10 ? 571  SER B N   1 
ATOM   7173 C  CA  . SER B 1 571 ? 24.928  47.850  -4.570  1.00 29.72 ? 571  SER B CA  1 
ATOM   7174 C  C   . SER B 1 571 ? 25.326  46.921  -5.721  1.00 30.21 ? 571  SER B C   1 
ATOM   7175 O  O   . SER B 1 571 ? 25.223  45.691  -5.602  1.00 29.93 ? 571  SER B O   1 
ATOM   7176 C  CB  . SER B 1 571 ? 26.150  48.231  -3.740  1.00 28.91 ? 571  SER B CB  1 
ATOM   7177 O  OG  . SER B 1 571 ? 26.862  47.075  -3.354  1.00 31.26 ? 571  SER B OG  1 
ATOM   7178 N  N   . LEU B 1 572 ? 25.779  47.511  -6.823  1.00 30.30 ? 572  LEU B N   1 
ATOM   7179 C  CA  . LEU B 1 572 ? 26.127  46.753  -8.024  1.00 31.46 ? 572  LEU B CA  1 
ATOM   7180 C  C   . LEU B 1 572 ? 27.015  45.533  -7.737  1.00 32.08 ? 572  LEU B C   1 
ATOM   7181 O  O   . LEU B 1 572 ? 26.729  44.436  -8.217  1.00 32.27 ? 572  LEU B O   1 
ATOM   7182 C  CB  . LEU B 1 572 ? 26.800  47.663  -9.061  1.00 31.42 ? 572  LEU B CB  1 
ATOM   7183 C  CG  . LEU B 1 572 ? 27.174  46.995  -10.394 1.00 31.54 ? 572  LEU B CG  1 
ATOM   7184 C  CD1 . LEU B 1 572 ? 26.008  46.209  -10.970 1.00 30.94 ? 572  LEU B CD1 1 
ATOM   7185 C  CD2 . LEU B 1 572 ? 27.648  48.043  -11.398 1.00 34.04 ? 572  LEU B CD2 1 
ATOM   7186 N  N   . THR B 1 573 ? 28.075  45.738  -6.954  1.00 33.72 ? 573  THR B N   1 
ATOM   7187 C  CA  . THR B 1 573 ? 29.042  44.680  -6.595  1.00 34.14 ? 573  THR B CA  1 
ATOM   7188 C  C   . THR B 1 573 ? 28.755  43.993  -5.240  1.00 33.45 ? 573  THR B C   1 
ATOM   7189 O  O   . THR B 1 573 ? 29.547  43.170  -4.781  1.00 33.27 ? 573  THR B O   1 
ATOM   7190 C  CB  . THR B 1 573 ? 30.484  45.241  -6.563  1.00 34.87 ? 573  THR B CB  1 
ATOM   7191 O  OG1 . THR B 1 573 ? 30.588  46.257  -5.562  1.00 37.14 ? 573  THR B OG1 1 
ATOM   7192 C  CG2 . THR B 1 573 ? 30.858  45.852  -7.905  1.00 36.02 ? 573  THR B CG2 1 
ATOM   7193 N  N   . GLY B 1 574 ? 27.614  44.300  -4.627  1.00 33.81 ? 574  GLY B N   1 
ATOM   7194 C  CA  . GLY B 1 574 ? 27.334  43.891  -3.242  1.00 32.28 ? 574  GLY B CA  1 
ATOM   7195 C  C   . GLY B 1 574 ? 26.925  42.439  -3.177  1.00 31.25 ? 574  GLY B C   1 
ATOM   7196 O  O   . GLY B 1 574 ? 27.080  41.699  -4.147  1.00 31.83 ? 574  GLY B O   1 
ATOM   7197 N  N   . SER B 1 575 ? 26.391  42.027  -2.039  1.00 28.19 ? 575  SER B N   1 
ATOM   7198 C  CA  . SER B 1 575 ? 25.925  40.668  -1.881  1.00 27.66 ? 575  SER B CA  1 
ATOM   7199 C  C   . SER B 1 575 ? 24.514  40.525  -2.469  1.00 26.52 ? 575  SER B C   1 
ATOM   7200 O  O   . SER B 1 575 ? 23.595  41.184  -2.013  1.00 23.47 ? 575  SER B O   1 
ATOM   7201 C  CB  . SER B 1 575 ? 25.925  40.298  -0.407  1.00 28.50 ? 575  SER B CB  1 
ATOM   7202 O  OG  . SER B 1 575 ? 25.818  38.904  -0.262  1.00 29.45 ? 575  SER B OG  1 
ATOM   7203 N  N   . TYR B 1 576 ? 24.358  39.673  -3.489  1.00 25.56 ? 576  TYR B N   1 
ATOM   7204 C  CA  . TYR B 1 576 ? 23.040  39.381  -4.081  1.00 24.30 ? 576  TYR B CA  1 
ATOM   7205 C  C   . TYR B 1 576 ? 22.301  38.286  -3.316  1.00 23.64 ? 576  TYR B C   1 
ATOM   7206 O  O   . TYR B 1 576 ? 22.870  37.244  -2.998  1.00 24.03 ? 576  TYR B O   1 
ATOM   7207 C  CB  . TYR B 1 576 ? 23.169  39.015  -5.576  1.00 24.91 ? 576  TYR B CB  1 
ATOM   7208 C  CG  . TYR B 1 576 ? 23.471  40.230  -6.422  1.00 24.34 ? 576  TYR B CG  1 
ATOM   7209 C  CD1 . TYR B 1 576 ? 24.779  40.681  -6.594  1.00 24.12 ? 576  TYR B CD1 1 
ATOM   7210 C  CD2 . TYR B 1 576 ? 22.443  40.958  -7.009  1.00 23.42 ? 576  TYR B CD2 1 
ATOM   7211 C  CE1 . TYR B 1 576 ? 25.047  41.822  -7.346  1.00 24.17 ? 576  TYR B CE1 1 
ATOM   7212 C  CE2 . TYR B 1 576 ? 22.692  42.089  -7.752  1.00 23.68 ? 576  TYR B CE2 1 
ATOM   7213 C  CZ  . TYR B 1 576 ? 23.993  42.526  -7.917  1.00 24.34 ? 576  TYR B CZ  1 
ATOM   7214 O  OH  . TYR B 1 576 ? 24.216  43.658  -8.660  1.00 23.93 ? 576  TYR B OH  1 
ATOM   7215 N  N   . LYS B 1 577 ? 21.030  38.533  -3.026  1.00 22.63 ? 577  LYS B N   1 
ATOM   7216 C  CA  . LYS B 1 577 ? 20.179  37.570  -2.321  1.00 24.13 ? 577  LYS B CA  1 
ATOM   7217 C  C   . LYS B 1 577 ? 19.044  37.131  -3.220  1.00 21.06 ? 577  LYS B C   1 
ATOM   7218 O  O   . LYS B 1 577 ? 18.444  37.955  -3.896  1.00 21.47 ? 577  LYS B O   1 
ATOM   7219 C  CB  . LYS B 1 577 ? 19.606  38.194  -1.037  1.00 25.77 ? 577  LYS B CB  1 
ATOM   7220 C  CG  . LYS B 1 577 ? 20.673  38.782  -0.112  1.00 29.32 ? 577  LYS B CG  1 
ATOM   7221 C  CD  . LYS B 1 577 ? 21.545  37.686  0.502   1.00 31.70 ? 577  LYS B CD  1 
ATOM   7222 C  CE  . LYS B 1 577 ? 22.812  38.226  1.147   1.00 33.23 ? 577  LYS B CE  1 
ATOM   7223 N  NZ  . LYS B 1 577 ? 22.546  39.419  1.991   1.00 36.26 ? 577  LYS B NZ  1 
ATOM   7224 N  N   . PRO B 1 578 ? 18.720  35.835  -3.209  1.00 19.80 ? 578  PRO B N   1 
ATOM   7225 C  CA  . PRO B 1 578 ? 17.756  35.331  -4.188  1.00 18.65 ? 578  PRO B CA  1 
ATOM   7226 C  C   . PRO B 1 578 ? 16.371  35.913  -3.978  1.00 18.34 ? 578  PRO B C   1 
ATOM   7227 O  O   . PRO B 1 578 ? 15.996  36.221  -2.861  1.00 18.22 ? 578  PRO B O   1 
ATOM   7228 C  CB  . PRO B 1 578 ? 17.776  33.824  -3.962  1.00 18.38 ? 578  PRO B CB  1 
ATOM   7229 C  CG  . PRO B 1 578 ? 18.237  33.650  -2.553  1.00 18.88 ? 578  PRO B CG  1 
ATOM   7230 C  CD  . PRO B 1 578 ? 19.210  34.770  -2.314  1.00 19.65 ? 578  PRO B CD  1 
ATOM   7231 N  N   . LEU B 1 579 ? 15.646  36.103  -5.067  1.00 18.08 ? 579  LEU B N   1 
ATOM   7232 C  CA  . LEU B 1 579 ? 14.239  36.468  -5.010  1.00 18.50 ? 579  LEU B CA  1 
ATOM   7233 C  C   . LEU B 1 579 ? 13.362  35.227  -4.794  1.00 18.47 ? 579  LEU B C   1 
ATOM   7234 O  O   . LEU B 1 579 ? 13.757  34.110  -5.157  1.00 18.77 ? 579  LEU B O   1 
ATOM   7235 C  CB  . LEU B 1 579 ? 13.828  37.141  -6.322  1.00 18.81 ? 579  LEU B CB  1 
ATOM   7236 C  CG  . LEU B 1 579 ? 14.573  38.434  -6.648  1.00 19.02 ? 579  LEU B CG  1 
ATOM   7237 C  CD1 . LEU B 1 579 ? 14.141  38.944  -8.010  1.00 19.73 ? 579  LEU B CD1 1 
ATOM   7238 C  CD2 . LEU B 1 579 ? 14.333  39.465  -5.561  1.00 19.34 ? 579  LEU B CD2 1 
ATOM   7239 N  N   . ASN B 1 580 ? 12.178  35.436  -4.218  1.00 18.34 ? 580  ASN B N   1 
ATOM   7240 C  CA  . ASN B 1 580 ? 11.209  34.353  -3.980  1.00 19.42 ? 580  ASN B CA  1 
ATOM   7241 C  C   . ASN B 1 580 ? 11.886  33.147  -3.323  1.00 19.78 ? 580  ASN B C   1 
ATOM   7242 O  O   . ASN B 1 580 ? 11.622  32.010  -3.703  1.00 19.98 ? 580  ASN B O   1 
ATOM   7243 C  CB  . ASN B 1 580 ? 10.544  33.931  -5.299  1.00 18.72 ? 580  ASN B CB  1 
ATOM   7244 C  CG  . ASN B 1 580 ? 9.850   35.088  -5.995  1.00 18.36 ? 580  ASN B CG  1 
ATOM   7245 O  OD1 . ASN B 1 580 ? 8.892   35.642  -5.481  1.00 19.31 ? 580  ASN B OD1 1 
ATOM   7246 N  ND2 . ASN B 1 580 ? 10.330  35.453  -7.166  1.00 18.33 ? 580  ASN B ND2 1 
ATOM   7247 N  N   . ASP B 1 581 ? 12.804  33.427  -2.393  1.00 21.23 ? 581  ASP B N   1 
ATOM   7248 C  CA  A ASP B 1 581 ? 13.524  32.412  -1.601  0.50 21.32 ? 581  ASP B CA  1 
ATOM   7249 C  CA  B ASP B 1 581 ? 13.483  32.386  -1.595  0.50 21.32 ? 581  ASP B CA  1 
ATOM   7250 C  C   . ASP B 1 581 ? 14.593  31.644  -2.358  1.00 20.41 ? 581  ASP B C   1 
ATOM   7251 O  O   . ASP B 1 581 ? 15.745  31.646  -1.950  1.00 20.01 ? 581  ASP B O   1 
ATOM   7252 C  CB  A ASP B 1 581 ? 12.556  31.433  -0.932  0.50 22.33 ? 581  ASP B CB  1 
ATOM   7253 C  CB  B ASP B 1 581 ? 12.443  31.385  -1.042  0.50 22.35 ? 581  ASP B CB  1 
ATOM   7254 C  CG  A ASP B 1 581 ? 11.675  32.111  0.067   0.50 22.80 ? 581  ASP B CG  1 
ATOM   7255 C  CG  B ASP B 1 581 ? 13.056  30.322  -0.163  0.50 22.74 ? 581  ASP B CG  1 
ATOM   7256 O  OD1 A ASP B 1 581 ? 12.120  33.136  0.619   0.50 23.51 ? 581  ASP B OD1 1 
ATOM   7257 O  OD1 B ASP B 1 581 ? 13.773  30.679  0.798   0.50 25.15 ? 581  ASP B OD1 1 
ATOM   7258 O  OD2 A ASP B 1 581 ? 10.556  31.621  0.304   0.50 24.19 ? 581  ASP B OD2 1 
ATOM   7259 O  OD2 B ASP B 1 581 ? 12.811  29.128  -0.432  0.50 23.18 ? 581  ASP B OD2 1 
ATOM   7260 N  N   . SER B 1 582 ? 14.227  30.992  -3.457  1.00 20.17 ? 582  SER B N   1 
ATOM   7261 C  CA  . SER B 1 582 ? 15.152  30.091  -4.170  1.00 19.12 ? 582  SER B CA  1 
ATOM   7262 C  C   . SER B 1 582 ? 15.891  30.725  -5.333  1.00 18.82 ? 582  SER B C   1 
ATOM   7263 O  O   . SER B 1 582 ? 16.835  30.118  -5.874  1.00 17.89 ? 582  SER B O   1 
ATOM   7264 C  CB  . SER B 1 582 ? 14.377  28.916  -4.743  1.00 18.78 ? 582  SER B CB  1 
ATOM   7265 O  OG  . SER B 1 582 ? 13.502  29.362  -5.784  1.00 17.87 ? 582  SER B OG  1 
ATOM   7266 N  N   . GLY B 1 583 ? 15.415  31.889  -5.764  1.00 17.91 ? 583  GLY B N   1 
ATOM   7267 C  CA  . GLY B 1 583 ? 15.922  32.512  -6.985  1.00 17.37 ? 583  GLY B CA  1 
ATOM   7268 C  C   . GLY B 1 583 ? 14.968  32.430  -8.168  1.00 17.00 ? 583  GLY B C   1 
ATOM   7269 O  O   . GLY B 1 583 ? 15.150  33.157  -9.145  1.00 16.84 ? 583  GLY B O   1 
ATOM   7270 N  N   . VAL B 1 584 ? 13.944  31.576  -8.090  1.00 16.24 ? 584  VAL B N   1 
ATOM   7271 C  CA  . VAL B 1 584 ? 12.965  31.447  -9.165  1.00 15.95 ? 584  VAL B CA  1 
ATOM   7272 C  C   . VAL B 1 584 ? 12.228  32.772  -9.410  1.00 16.19 ? 584  VAL B C   1 
ATOM   7273 O  O   . VAL B 1 584 ? 11.824  33.446  -8.468  1.00 15.27 ? 584  VAL B O   1 
ATOM   7274 C  CB  . VAL B 1 584 ? 11.926  30.330  -8.893  1.00 16.03 ? 584  VAL B CB  1 
ATOM   7275 C  CG1 . VAL B 1 584 ? 10.902  30.754  -7.849  1.00 16.17 ? 584  VAL B CG1 1 
ATOM   7276 C  CG2 . VAL B 1 584 ? 11.205  29.923  -10.174 1.00 15.97 ? 584  VAL B CG2 1 
ATOM   7277 N  N   . VAL B 1 585 ? 12.067  33.128  -10.682 1.00 15.93 ? 585  VAL B N   1 
ATOM   7278 C  CA  . VAL B 1 585 ? 11.294  34.319  -11.069 1.00 16.60 ? 585  VAL B CA  1 
ATOM   7279 C  C   . VAL B 1 585 ? 10.299  33.941  -12.156 1.00 16.55 ? 585  VAL B C   1 
ATOM   7280 O  O   . VAL B 1 585 ? 9.107   34.200  -12.012 1.00 16.99 ? 585  VAL B O   1 
ATOM   7281 C  CB  . VAL B 1 585 ? 12.209  35.485  -11.522 1.00 16.82 ? 585  VAL B CB  1 
ATOM   7282 C  CG1 . VAL B 1 585 ? 11.374  36.697  -11.942 1.00 16.93 ? 585  VAL B CG1 1 
ATOM   7283 C  CG2 . VAL B 1 585 ? 13.173  35.884  -10.403 1.00 16.76 ? 585  VAL B CG2 1 
ATOM   7284 N  N   . LEU B 1 586 ? 10.787  33.311  -13.226 1.00 16.49 ? 586  LEU B N   1 
ATOM   7285 C  CA  . LEU B 1 586 ? 9.931   32.793  -14.301 1.00 16.77 ? 586  LEU B CA  1 
ATOM   7286 C  C   . LEU B 1 586 ? 10.110  31.305  -14.525 1.00 17.55 ? 586  LEU B C   1 
ATOM   7287 O  O   . LEU B 1 586 ? 11.227  30.783  -14.455 1.00 17.00 ? 586  LEU B O   1 
ATOM   7288 C  CB  . LEU B 1 586 ? 10.255  33.486  -15.612 1.00 16.55 ? 586  LEU B CB  1 
ATOM   7289 C  CG  . LEU B 1 586 ? 10.102  35.000  -15.603 1.00 16.71 ? 586  LEU B CG  1 
ATOM   7290 C  CD1 . LEU B 1 586 ? 10.623  35.584  -16.905 1.00 16.58 ? 586  LEU B CD1 1 
ATOM   7291 C  CD2 . LEU B 1 586 ? 8.645   35.375  -15.361 1.00 17.13 ? 586  LEU B CD2 1 
ATOM   7292 N  N   . THR B 1 587 ? 9.019   30.613  -14.844 1.00 18.07 ? 587  THR B N   1 
ATOM   7293 C  CA  . THR B 1 587 ? 9.137   29.189  -15.180 1.00 18.19 ? 587  THR B CA  1 
ATOM   7294 C  C   . THR B 1 587 ? 8.413   28.885  -16.479 1.00 17.72 ? 587  THR B C   1 
ATOM   7295 O  O   . THR B 1 587 ? 7.400   29.514  -16.803 1.00 17.19 ? 587  THR B O   1 
ATOM   7296 C  CB  . THR B 1 587 ? 8.585   28.298  -14.062 1.00 18.75 ? 587  THR B CB  1 
ATOM   7297 O  OG1 . THR B 1 587 ? 7.226   28.641  -13.804 1.00 18.92 ? 587  THR B OG1 1 
ATOM   7298 C  CG2 . THR B 1 587 ? 9.373   28.492  -12.793 1.00 19.20 ? 587  THR B CG2 1 
ATOM   7299 N  N   . ALA B 1 588 ? 8.947   27.910  -17.208 1.00 17.16 ? 588  ALA B N   1 
ATOM   7300 C  CA  . ALA B 1 588 ? 8.353   27.432  -18.436 1.00 17.12 ? 588  ALA B CA  1 
ATOM   7301 C  C   . ALA B 1 588 ? 6.899   27.023  -18.212 1.00 17.19 ? 588  ALA B C   1 
ATOM   7302 O  O   . ALA B 1 588 ? 6.538   26.462  -17.177 1.00 17.32 ? 588  ALA B O   1 
ATOM   7303 C  CB  . ALA B 1 588 ? 9.149   26.249  -18.972 1.00 17.72 ? 588  ALA B CB  1 
ATOM   7304 N  N   . SER B 1 589 ? 6.055   27.299  -19.193 1.00 16.86 ? 589  SER B N   1 
ATOM   7305 C  CA  . SER B 1 589 ? 4.640   26.962  -19.056 1.00 16.45 ? 589  SER B CA  1 
ATOM   7306 C  C   . SER B 1 589 ? 4.105   26.074  -20.167 1.00 16.15 ? 589  SER B C   1 
ATOM   7307 O  O   . SER B 1 589 ? 3.012   25.572  -20.027 1.00 16.29 ? 589  SER B O   1 
ATOM   7308 C  CB  . SER B 1 589 ? 3.806   28.242  -18.949 1.00 15.83 ? 589  SER B CB  1 
ATOM   7309 O  OG  . SER B 1 589 ? 4.029   29.080  -20.064 1.00 15.71 ? 589  SER B OG  1 
ATOM   7310 N  N   . VAL B 1 590 ? 4.860   25.896  -21.254 1.00 16.11 ? 590  VAL B N   1 
ATOM   7311 C  CA  . VAL B 1 590 ? 4.464   25.056  -22.372 1.00 16.36 ? 590  VAL B CA  1 
ATOM   7312 C  C   . VAL B 1 590 ? 5.627   24.196  -22.882 1.00 16.78 ? 590  VAL B C   1 
ATOM   7313 O  O   . VAL B 1 590 ? 6.798   24.498  -22.622 1.00 16.52 ? 590  VAL B O   1 
ATOM   7314 C  CB  . VAL B 1 590 ? 3.900   25.870  -23.569 1.00 17.02 ? 590  VAL B CB  1 
ATOM   7315 C  CG1 . VAL B 1 590 ? 2.633   26.615  -23.169 1.00 16.70 ? 590  VAL B CG1 1 
ATOM   7316 C  CG2 . VAL B 1 590 ? 4.951   26.815  -24.161 1.00 17.21 ? 590  VAL B CG2 1 
ATOM   7317 N  N   . PRO B 1 591 ? 5.304   23.116  -23.618 1.00 16.98 ? 591  PRO B N   1 
ATOM   7318 C  CA  . PRO B 1 591 ? 6.355   22.235  -24.112 1.00 17.17 ? 591  PRO B CA  1 
ATOM   7319 C  C   . PRO B 1 591 ? 7.336   22.940  -25.033 1.00 17.54 ? 591  PRO B C   1 
ATOM   7320 O  O   . PRO B 1 591 ? 6.938   23.811  -25.811 1.00 19.19 ? 591  PRO B O   1 
ATOM   7321 C  CB  . PRO B 1 591 ? 5.575   21.137  -24.859 1.00 16.92 ? 591  PRO B CB  1 
ATOM   7322 C  CG  . PRO B 1 591 ? 4.265   21.070  -24.126 1.00 17.15 ? 591  PRO B CG  1 
ATOM   7323 C  CD  . PRO B 1 591 ? 3.965   22.500  -23.743 1.00 16.99 ? 591  PRO B CD  1 
ATOM   7324 N  N   . ALA B 1 592 ? 8.598   22.528  -24.956 1.00 17.04 ? 592  ALA B N   1 
ATOM   7325 C  CA  . ALA B 1 592 ? 9.688   23.196  -25.660 1.00 17.05 ? 592  ALA B CA  1 
ATOM   7326 C  C   . ALA B 1 592 ? 9.534   23.145  -27.178 1.00 17.50 ? 592  ALA B C   1 
ATOM   7327 O  O   . ALA B 1 592 ? 10.077  24.008  -27.872 1.00 16.35 ? 592  ALA B O   1 
ATOM   7328 C  CB  . ALA B 1 592 ? 11.026  22.594  -25.240 1.00 17.18 ? 592  ALA B CB  1 
ATOM   7329 N  N   . ASN B 1 593 ? 8.799   22.145  -27.691 1.00 17.97 ? 593  ASN B N   1 
ATOM   7330 C  CA  . ASN B 1 593 ? 8.530   22.053  -29.131 1.00 18.42 ? 593  ASN B CA  1 
ATOM   7331 C  C   . ASN B 1 593 ? 7.266   22.771  -29.654 1.00 18.59 ? 593  ASN B C   1 
ATOM   7332 O  O   . ASN B 1 593 ? 6.937   22.651  -30.837 1.00 19.44 ? 593  ASN B O   1 
ATOM   7333 C  CB  . ASN B 1 593 ? 8.543   20.596  -29.612 1.00 18.93 ? 593  ASN B CB  1 
ATOM   7334 C  CG  . ASN B 1 593 ? 7.449   19.745  -28.994 1.00 19.51 ? 593  ASN B CG  1 
ATOM   7335 O  OD1 . ASN B 1 593 ? 6.845   20.103  -27.988 1.00 20.03 ? 593  ASN B OD1 1 
ATOM   7336 N  ND2 . ASN B 1 593 ? 7.210   18.583  -29.594 1.00 19.82 ? 593  ASN B ND2 1 
ATOM   7337 N  N   . TRP B 1 594 ? 6.567   23.522  -28.811 1.00 18.13 ? 594  TRP B N   1 
ATOM   7338 C  CA  . TRP B 1 594 ? 5.398   24.251  -29.287 1.00 17.65 ? 594  TRP B CA  1 
ATOM   7339 C  C   . TRP B 1 594 ? 5.811   25.583  -29.873 1.00 17.22 ? 594  TRP B C   1 
ATOM   7340 O  O   . TRP B 1 594 ? 6.873   26.120  -29.546 1.00 16.57 ? 594  TRP B O   1 
ATOM   7341 C  CB  . TRP B 1 594 ? 4.409   24.490  -28.154 1.00 18.28 ? 594  TRP B CB  1 
ATOM   7342 C  CG  . TRP B 1 594 ? 3.633   23.292  -27.744 1.00 18.52 ? 594  TRP B CG  1 
ATOM   7343 C  CD1 . TRP B 1 594 ? 3.875   21.974  -28.068 1.00 18.66 ? 594  TRP B CD1 1 
ATOM   7344 C  CD2 . TRP B 1 594 ? 2.488   23.290  -26.893 1.00 18.90 ? 594  TRP B CD2 1 
ATOM   7345 N  NE1 . TRP B 1 594 ? 2.930   21.162  -27.474 1.00 18.79 ? 594  TRP B NE1 1 
ATOM   7346 C  CE2 . TRP B 1 594 ? 2.074   21.947  -26.743 1.00 18.68 ? 594  TRP B CE2 1 
ATOM   7347 C  CE3 . TRP B 1 594 ? 1.768   24.296  -26.244 1.00 19.21 ? 594  TRP B CE3 1 
ATOM   7348 C  CZ2 . TRP B 1 594 ? 0.979   21.593  -25.975 1.00 19.04 ? 594  TRP B CZ2 1 
ATOM   7349 C  CZ3 . TRP B 1 594 ? 0.680   23.936  -25.472 1.00 19.99 ? 594  TRP B CZ3 1 
ATOM   7350 C  CH2 . TRP B 1 594 ? 0.295   22.594  -25.349 1.00 19.43 ? 594  TRP B CH2 1 
ATOM   7351 N  N   . ARG B 1 595 ? 4.963   26.115  -30.745 1.00 17.41 ? 595  ARG B N   1 
ATOM   7352 C  CA  . ARG B 1 595 ? 5.177   27.426  -31.344 1.00 17.57 ? 595  ARG B CA  1 
ATOM   7353 C  C   . ARG B 1 595 ? 5.454   28.502  -30.280 1.00 17.16 ? 595  ARG B C   1 
ATOM   7354 O  O   . ARG B 1 595 ? 6.348   29.337  -30.456 1.00 19.29 ? 595  ARG B O   1 
ATOM   7355 C  CB  . ARG B 1 595 ? 3.957   27.828  -32.183 1.00 17.66 ? 595  ARG B CB  1 
ATOM   7356 C  CG  . ARG B 1 595 ? 4.051   29.198  -32.835 1.00 17.43 ? 595  ARG B CG  1 
ATOM   7357 C  CD  . ARG B 1 595 ? 5.324   29.326  -33.647 1.00 17.95 ? 595  ARG B CD  1 
ATOM   7358 N  NE  . ARG B 1 595 ? 5.174   30.183  -34.813 1.00 18.56 ? 595  ARG B NE  1 
ATOM   7359 C  CZ  . ARG B 1 595 ? 6.144   30.883  -35.403 1.00 18.75 ? 595  ARG B CZ  1 
ATOM   7360 N  NH1 . ARG B 1 595 ? 7.403   30.863  -34.967 1.00 18.56 ? 595  ARG B NH1 1 
ATOM   7361 N  NH2 . ARG B 1 595 ? 5.845   31.600  -36.484 1.00 19.09 ? 595  ARG B NH2 1 
ATOM   7362 N  N   . THR B 1 596 ? 4.692   28.468  -29.190 1.00 16.81 ? 596  THR B N   1 
ATOM   7363 C  CA  . THR B 1 596 ? 4.746   29.502  -28.145 1.00 16.39 ? 596  THR B CA  1 
ATOM   7364 C  C   . THR B 1 596 ? 5.766   29.278  -27.027 1.00 15.60 ? 596  THR B C   1 
ATOM   7365 O  O   . THR B 1 596 ? 5.783   30.040  -26.048 1.00 15.38 ? 596  THR B O   1 
ATOM   7366 C  CB  . THR B 1 596 ? 3.348   29.794  -27.526 1.00 16.31 ? 596  THR B CB  1 
ATOM   7367 O  OG1 . THR B 1 596 ? 2.846   28.656  -26.792 1.00 15.26 ? 596  THR B OG1 1 
ATOM   7368 C  CG2 . THR B 1 596 ? 2.370   30.177  -28.618 1.00 16.85 ? 596  THR B CG2 1 
ATOM   7369 N  N   . ALA B 1 597 ? 6.635   28.280  -27.176 1.00 15.81 ? 597  ALA B N   1 
ATOM   7370 C  CA  . ALA B 1 597 ? 7.797   28.121  -26.267 1.00 15.75 ? 597  ALA B CA  1 
ATOM   7371 C  C   . ALA B 1 597 ? 8.693   29.351  -26.334 1.00 15.99 ? 597  ALA B C   1 
ATOM   7372 O  O   . ALA B 1 597 ? 8.780   30.024  -27.378 1.00 15.77 ? 597  ALA B O   1 
ATOM   7373 C  CB  . ALA B 1 597 ? 8.605   26.889  -26.624 1.00 16.38 ? 597  ALA B CB  1 
ATOM   7374 N  N   . THR B 1 598 ? 9.352   29.646  -25.218 1.00 15.82 ? 598  THR B N   1 
ATOM   7375 C  CA  . THR B 1 598 ? 10.194  30.826  -25.109 1.00 15.62 ? 598  THR B CA  1 
ATOM   7376 C  C   . THR B 1 598 ? 11.493  30.502  -24.397 1.00 15.63 ? 598  THR B C   1 
ATOM   7377 O  O   . THR B 1 598 ? 11.596  29.489  -23.695 1.00 15.71 ? 598  THR B O   1 
ATOM   7378 C  CB  . THR B 1 598 ? 9.464   31.968  -24.350 1.00 15.48 ? 598  THR B CB  1 
ATOM   7379 O  OG1 . THR B 1 598 ? 8.912   31.466  -23.127 1.00 15.27 ? 598  THR B OG1 1 
ATOM   7380 C  CG2 . THR B 1 598 ? 8.367   32.548  -25.184 1.00 15.00 ? 598  THR B CG2 1 
ATOM   7381 N  N   . TYR B 1 599 ? 12.483  31.359  -24.605 1.00 15.85 ? 599  TYR B N   1 
ATOM   7382 C  CA  . TYR B 1 599 ? 13.729  31.348  -23.844 1.00 16.65 ? 599  TYR B CA  1 
ATOM   7383 C  C   . TYR B 1 599 ? 14.444  32.705  -23.984 1.00 17.34 ? 599  TYR B C   1 
ATOM   7384 O  O   . TYR B 1 599 ? 14.015  33.564  -24.773 1.00 15.57 ? 599  TYR B O   1 
ATOM   7385 C  CB  . TYR B 1 599 ? 14.653  30.216  -24.314 1.00 17.18 ? 599  TYR B CB  1 
ATOM   7386 C  CG  . TYR B 1 599 ? 15.872  30.027  -23.438 1.00 16.89 ? 599  TYR B CG  1 
ATOM   7387 C  CD1 . TYR B 1 599 ? 15.728  29.702  -22.103 1.00 16.93 ? 599  TYR B CD1 1 
ATOM   7388 C  CD2 . TYR B 1 599 ? 17.163  30.169  -23.947 1.00 17.42 ? 599  TYR B CD2 1 
ATOM   7389 C  CE1 . TYR B 1 599 ? 16.823  29.534  -21.281 1.00 17.36 ? 599  TYR B CE1 1 
ATOM   7390 C  CE2 . TYR B 1 599 ? 18.277  29.999  -23.136 1.00 17.42 ? 599  TYR B CE2 1 
ATOM   7391 C  CZ  . TYR B 1 599 ? 18.095  29.679  -21.798 1.00 17.41 ? 599  TYR B CZ  1 
ATOM   7392 O  OH  . TYR B 1 599 ? 19.154  29.523  -20.954 1.00 18.04 ? 599  TYR B OH  1 
ATOM   7393 N  N   . SER B 1 600 ? 15.518  32.879  -23.205 1.00 18.02 ? 600  SER B N   1 
ATOM   7394 C  CA  . SER B 1 600 ? 16.340  34.082  -23.181 1.00 19.63 ? 600  SER B CA  1 
ATOM   7395 C  C   . SER B 1 600 ? 15.564  35.300  -22.728 1.00 18.59 ? 600  SER B C   1 
ATOM   7396 O  O   . SER B 1 600 ? 15.668  36.376  -23.304 1.00 19.04 ? 600  SER B O   1 
ATOM   7397 C  CB  . SER B 1 600 ? 17.040  34.335  -24.514 1.00 21.94 ? 600  SER B CB  1 
ATOM   7398 O  OG  . SER B 1 600 ? 18.135  33.451  -24.646 1.00 27.10 ? 600  SER B OG  1 
ATOM   7399 N  N   . TYR B 1 601 ? 14.818  35.101  -21.655 1.00 18.23 ? 601  TYR B N   1 
ATOM   7400 C  CA  . TYR B 1 601 ? 14.133  36.159  -20.942 1.00 17.82 ? 601  TYR B CA  1 
ATOM   7401 C  C   . TYR B 1 601 ? 15.148  37.252  -20.615 1.00 17.99 ? 601  TYR B C   1 
ATOM   7402 O  O   . TYR B 1 601 ? 16.259  36.970  -20.141 1.00 17.42 ? 601  TYR B O   1 
ATOM   7403 C  CB  . TYR B 1 601 ? 13.484  35.595  -19.665 1.00 17.97 ? 601  TYR B CB  1 
ATOM   7404 C  CG  . TYR B 1 601 ? 12.708  34.347  -19.972 1.00 17.71 ? 601  TYR B CG  1 
ATOM   7405 C  CD1 . TYR B 1 601 ? 11.513  34.425  -20.675 1.00 17.80 ? 601  TYR B CD1 1 
ATOM   7406 C  CD2 . TYR B 1 601 ? 13.193  33.083  -19.639 1.00 18.05 ? 601  TYR B CD2 1 
ATOM   7407 C  CE1 . TYR B 1 601 ? 10.803  33.300  -21.009 1.00 17.81 ? 601  TYR B CE1 1 
ATOM   7408 C  CE2 . TYR B 1 601 ? 12.473  31.931  -19.975 1.00 18.06 ? 601  TYR B CE2 1 
ATOM   7409 C  CZ  . TYR B 1 601 ? 11.281  32.051  -20.669 1.00 18.16 ? 601  TYR B CZ  1 
ATOM   7410 O  OH  . TYR B 1 601 ? 10.529  30.940  -21.047 1.00 19.39 ? 601  TYR B OH  1 
ATOM   7411 N  N   . TYR B 1 602 ? 14.782  38.482  -20.953 1.00 17.72 ? 602  TYR B N   1 
ATOM   7412 C  CA  . TYR B 1 602 ? 15.625  39.634  -20.744 1.00 18.19 ? 602  TYR B CA  1 
ATOM   7413 C  C   . TYR B 1 602 ? 14.747  40.806  -20.333 1.00 18.03 ? 602  TYR B C   1 
ATOM   7414 O  O   . TYR B 1 602 ? 13.991  41.354  -21.125 1.00 17.44 ? 602  TYR B O   1 
ATOM   7415 C  CB  . TYR B 1 602 ? 16.400  39.941  -22.012 1.00 19.22 ? 602  TYR B CB  1 
ATOM   7416 C  CG  . TYR B 1 602 ? 17.459  40.990  -21.851 1.00 19.59 ? 602  TYR B CG  1 
ATOM   7417 C  CD1 . TYR B 1 602 ? 18.687  40.677  -21.286 1.00 20.06 ? 602  TYR B CD1 1 
ATOM   7418 C  CD2 . TYR B 1 602 ? 17.237  42.292  -22.262 1.00 19.76 ? 602  TYR B CD2 1 
ATOM   7419 C  CE1 . TYR B 1 602 ? 19.671  41.636  -21.141 1.00 20.34 ? 602  TYR B CE1 1 
ATOM   7420 C  CE2 . TYR B 1 602 ? 18.209  43.259  -22.114 1.00 20.10 ? 602  TYR B CE2 1 
ATOM   7421 C  CZ  . TYR B 1 602 ? 19.422  42.922  -21.558 1.00 19.86 ? 602  TYR B CZ  1 
ATOM   7422 O  OH  . TYR B 1 602 ? 20.390  43.864  -21.414 1.00 20.61 ? 602  TYR B OH  1 
ATOM   7423 N  N   . ALA B 1 603 ? 14.860  41.160  -19.064 1.00 18.90 ? 603  ALA B N   1 
ATOM   7424 C  CA  . ALA B 1 603 ? 14.089  42.230  -18.457 1.00 18.32 ? 603  ALA B CA  1 
ATOM   7425 C  C   . ALA B 1 603 ? 14.624  43.626  -18.818 1.00 18.31 ? 603  ALA B C   1 
ATOM   7426 O  O   . ALA B 1 603 ? 15.829  43.907  -18.706 1.00 17.32 ? 603  ALA B O   1 
ATOM   7427 C  CB  . ALA B 1 603 ? 14.107  42.060  -16.952 1.00 18.53 ? 603  ALA B CB  1 
ATOM   7428 N  N   . VAL B 1 604 ? 13.701  44.499  -19.206 1.00 18.42 ? 604  VAL B N   1 
ATOM   7429 C  CA  . VAL B 1 604 ? 13.999  45.890  -19.497 1.00 19.03 ? 604  VAL B CA  1 
ATOM   7430 C  C   . VAL B 1 604 ? 13.220  46.788  -18.530 1.00 18.59 ? 604  VAL B C   1 
ATOM   7431 O  O   . VAL B 1 604 ? 12.040  46.531  -18.232 1.00 16.06 ? 604  VAL B O   1 
ATOM   7432 C  CB  . VAL B 1 604 ? 13.646  46.220  -20.975 1.00 20.51 ? 604  VAL B CB  1 
ATOM   7433 C  CG1 . VAL B 1 604 ? 13.814  47.694  -21.282 1.00 22.00 ? 604  VAL B CG1 1 
ATOM   7434 C  CG2 . VAL B 1 604 ? 14.558  45.447  -21.904 1.00 21.44 ? 604  VAL B CG2 1 
ATOM   7435 N  N   . PRO B 1 605 ? 13.864  47.861  -18.042 1.00 20.13 ? 605  PRO B N   1 
ATOM   7436 C  CA  . PRO B 1 605 ? 13.138  48.743  -17.136 1.00 20.98 ? 605  PRO B CA  1 
ATOM   7437 C  C   . PRO B 1 605 ? 11.992  49.461  -17.837 1.00 21.75 ? 605  PRO B C   1 
ATOM   7438 O  O   . PRO B 1 605 ? 11.942  49.513  -19.070 1.00 21.18 ? 605  PRO B O   1 
ATOM   7439 C  CB  . PRO B 1 605 ? 14.198  49.743  -16.662 1.00 21.56 ? 605  PRO B CB  1 
ATOM   7440 C  CG  . PRO B 1 605 ? 15.503  49.217  -17.135 1.00 21.72 ? 605  PRO B CG  1 
ATOM   7441 C  CD  . PRO B 1 605 ? 15.235  48.326  -18.291 1.00 20.84 ? 605  PRO B CD  1 
ATOM   7442 N  N   . VAL B 1 606 ? 11.082  49.996  -17.032 1.00 22.13 ? 606  VAL B N   1 
ATOM   7443 C  CA  . VAL B 1 606 ? 9.892   50.684  -17.512 1.00 23.32 ? 606  VAL B CA  1 
ATOM   7444 C  C   . VAL B 1 606 ? 9.984   52.115  -17.013 1.00 24.02 ? 606  VAL B C   1 
ATOM   7445 O  O   . VAL B 1 606 ? 10.115  52.351  -15.814 1.00 23.91 ? 606  VAL B O   1 
ATOM   7446 C  CB  . VAL B 1 606 ? 8.608   49.997  -16.980 1.00 23.88 ? 606  VAL B CB  1 
ATOM   7447 C  CG1 . VAL B 1 606 ? 7.358   50.796  -17.342 1.00 25.24 ? 606  VAL B CG1 1 
ATOM   7448 C  CG2 . VAL B 1 606 ? 8.514   48.576  -17.529 1.00 24.20 ? 606  VAL B CG2 1 
ATOM   7449 N  N   . ALA B 1 607 ? 9.944   53.066  -17.930 1.00 25.39 ? 607  ALA B N   1 
ATOM   7450 C  CA  . ALA B 1 607 ? 10.036  54.476  -17.576 1.00 27.77 ? 607  ALA B CA  1 
ATOM   7451 C  C   . ALA B 1 607 ? 9.021   54.858  -16.486 1.00 27.82 ? 607  ALA B C   1 
ATOM   7452 O  O   . ALA B 1 607 ? 7.836   54.572  -16.603 1.00 28.85 ? 607  ALA B O   1 
ATOM   7453 C  CB  . ALA B 1 607 ? 9.834   55.332  -18.821 1.00 28.76 ? 607  ALA B CB  1 
ATOM   7454 N  N   . GLY B 1 608 ? 9.508   55.461  -15.412 1.00 29.43 ? 608  GLY B N   1 
ATOM   7455 C  CA  . GLY B 1 608 ? 8.641   55.971  -14.355 1.00 33.26 ? 608  GLY B CA  1 
ATOM   7456 C  C   . GLY B 1 608 ? 8.193   54.970  -13.297 1.00 36.00 ? 608  GLY B C   1 
ATOM   7457 O  O   . GLY B 1 608 ? 7.486   55.352  -12.368 1.00 35.96 ? 608  GLY B O   1 
ATOM   7458 N  N   . LYS B 1 609 ? 8.610   53.704  -13.408 1.00 36.46 ? 609  LYS B N   1 
ATOM   7459 C  CA  . LYS B 1 609 ? 8.174   52.666  -12.474 1.00 35.41 ? 609  LYS B CA  1 
ATOM   7460 C  C   . LYS B 1 609 ? 9.384   52.018  -11.825 1.00 34.75 ? 609  LYS B C   1 
ATOM   7461 O  O   . LYS B 1 609 ? 10.254  51.501  -12.520 1.00 37.77 ? 609  LYS B O   1 
ATOM   7462 C  CB  . LYS B 1 609 ? 7.355   51.603  -13.206 1.00 37.23 ? 609  LYS B CB  1 
ATOM   7463 C  CG  . LYS B 1 609 ? 6.237   52.144  -14.080 1.00 39.90 ? 609  LYS B CG  1 
ATOM   7464 C  CD  . LYS B 1 609 ? 5.262   53.048  -13.335 1.00 43.03 ? 609  LYS B CD  1 
ATOM   7465 C  CE  . LYS B 1 609 ? 4.423   52.304  -12.308 1.00 45.28 ? 609  LYS B CE  1 
ATOM   7466 N  NZ  . LYS B 1 609 ? 3.237   51.669  -12.951 1.00 47.72 ? 609  LYS B NZ  1 
ATOM   7467 N  N   . ASP B 1 610 ? 9.447   52.030  -10.498 1.00 31.47 ? 610  ASP B N   1 
ATOM   7468 C  CA  . ASP B 1 610 ? 10.551  51.377  -9.795  1.00 31.14 ? 610  ASP B CA  1 
ATOM   7469 C  C   . ASP B 1 610 ? 10.230  49.937  -9.348  1.00 27.61 ? 610  ASP B C   1 
ATOM   7470 O  O   . ASP B 1 610 ? 11.045  49.307  -8.690  1.00 27.55 ? 610  ASP B O   1 
ATOM   7471 C  CB  . ASP B 1 610 ? 11.038  52.232  -8.611  1.00 33.72 ? 610  ASP B CB  1 
ATOM   7472 C  CG  . ASP B 1 610 ? 9.918   52.632  -7.647  1.00 36.23 ? 610  ASP B CG  1 
ATOM   7473 O  OD1 . ASP B 1 610 ? 8.804   52.054  -7.690  1.00 38.40 ? 610  ASP B OD1 1 
ATOM   7474 O  OD2 . ASP B 1 610 ? 10.164  53.543  -6.832  1.00 40.20 ? 610  ASP B OD2 1 
ATOM   7475 N  N   . ASP B 1 611 ? 9.065   49.419  -9.729  1.00 25.81 ? 611  ASP B N   1 
ATOM   7476 C  CA  . ASP B 1 611 ? 8.603   48.099  -9.283  1.00 26.31 ? 611  ASP B CA  1 
ATOM   7477 C  C   . ASP B 1 611 ? 8.096   47.221  -10.437 1.00 25.00 ? 611  ASP B C   1 
ATOM   7478 O  O   . ASP B 1 611 ? 7.309   46.311  -10.215 1.00 26.22 ? 611  ASP B O   1 
ATOM   7479 C  CB  . ASP B 1 611 ? 7.483   48.279  -8.239  1.00 26.86 ? 611  ASP B CB  1 
ATOM   7480 C  CG  . ASP B 1 611 ? 6.207   48.825  -8.848  1.00 27.66 ? 611  ASP B CG  1 
ATOM   7481 O  OD1 . ASP B 1 611 ? 6.269   49.433  -9.946  1.00 27.40 ? 611  ASP B OD1 1 
ATOM   7482 O  OD2 . ASP B 1 611 ? 5.134   48.618  -8.248  1.00 30.64 ? 611  ASP B OD2 1 
ATOM   7483 N  N   . GLN B 1 612 ? 8.526   47.517  -11.661 1.00 23.86 ? 612  GLN B N   1 
ATOM   7484 C  CA  . GLN B 1 612 ? 8.090   46.797  -12.851 1.00 23.88 ? 612  GLN B CA  1 
ATOM   7485 C  C   . GLN B 1 612 ? 9.244   46.657  -13.816 1.00 21.78 ? 612  GLN B C   1 
ATOM   7486 O  O   . GLN B 1 612 ? 10.038  47.584  -13.982 1.00 21.84 ? 612  GLN B O   1 
ATOM   7487 C  CB  . GLN B 1 612 ? 6.992   47.561  -13.603 1.00 26.20 ? 612  GLN B CB  1 
ATOM   7488 C  CG  . GLN B 1 612 ? 5.598   47.466  -13.018 1.00 28.47 ? 612  GLN B CG  1 
ATOM   7489 C  CD  . GLN B 1 612 ? 4.580   48.283  -13.802 1.00 30.40 ? 612  GLN B CD  1 
ATOM   7490 O  OE1 . GLN B 1 612 ? 4.865   48.807  -14.890 1.00 33.48 ? 612  GLN B OE1 1 
ATOM   7491 N  NE2 . GLN B 1 612 ? 3.389   48.392  -13.258 1.00 31.47 ? 612  GLN B NE2 1 
ATOM   7492 N  N   . VAL B 1 613 ? 9.308   45.517  -14.489 1.00 19.34 ? 613  VAL B N   1 
ATOM   7493 C  CA  . VAL B 1 613 ? 10.175  45.379  -15.641 1.00 18.36 ? 613  VAL B CA  1 
ATOM   7494 C  C   . VAL B 1 613 ? 9.385   44.736  -16.755 1.00 17.40 ? 613  VAL B C   1 
ATOM   7495 O  O   . VAL B 1 613 ? 8.388   44.062  -16.506 1.00 17.63 ? 613  VAL B O   1 
ATOM   7496 C  CB  . VAL B 1 613 ? 11.446  44.566  -15.322 1.00 18.41 ? 613  VAL B CB  1 
ATOM   7497 C  CG1 . VAL B 1 613 ? 12.293  45.309  -14.301 1.00 18.47 ? 613  VAL B CG1 1 
ATOM   7498 C  CG2 . VAL B 1 613 ? 11.101  43.155  -14.839 1.00 18.67 ? 613  VAL B CG2 1 
ATOM   7499 N  N   . LEU B 1 614 ? 9.824   44.974  -17.983 1.00 17.25 ? 614  LEU B N   1 
ATOM   7500 C  CA  . LEU B 1 614 ? 9.240   44.348  -19.150 1.00 17.06 ? 614  LEU B CA  1 
ATOM   7501 C  C   . LEU B 1 614 ? 10.127  43.173  -19.543 1.00 16.74 ? 614  LEU B C   1 
ATOM   7502 O  O   . LEU B 1 614 ? 11.305  43.347  -19.848 1.00 16.18 ? 614  LEU B O   1 
ATOM   7503 C  CB  . LEU B 1 614 ? 9.162   45.347  -20.297 1.00 17.52 ? 614  LEU B CB  1 
ATOM   7504 C  CG  . LEU B 1 614 ? 8.551   44.835  -21.604 1.00 18.04 ? 614  LEU B CG  1 
ATOM   7505 C  CD1 . LEU B 1 614 ? 7.084   44.482  -21.412 1.00 18.19 ? 614  LEU B CD1 1 
ATOM   7506 C  CD2 . LEU B 1 614 ? 8.730   45.872  -22.707 1.00 18.46 ? 614  LEU B CD2 1 
ATOM   7507 N  N   . VAL B 1 615 ? 9.546   41.982  -19.531 1.00 17.10 ? 615  VAL B N   1 
ATOM   7508 C  CA  . VAL B 1 615 ? 10.254  40.760  -19.900 1.00 16.29 ? 615  VAL B CA  1 
ATOM   7509 C  C   . VAL B 1 615 ? 10.116  40.491  -21.401 1.00 15.91 ? 615  VAL B C   1 
ATOM   7510 O  O   . VAL B 1 615 ? 9.015   40.204  -21.905 1.00 15.43 ? 615  VAL B O   1 
ATOM   7511 C  CB  . VAL B 1 615 ? 9.723   39.544  -19.122 1.00 16.04 ? 615  VAL B CB  1 
ATOM   7512 C  CG1 . VAL B 1 615 ? 10.471  38.292  -19.544 1.00 16.78 ? 615  VAL B CG1 1 
ATOM   7513 C  CG2 . VAL B 1 615 ? 9.869   39.764  -17.623 1.00 16.31 ? 615  VAL B CG2 1 
ATOM   7514 N  N   . THR B 1 616 ? 11.248  40.580  -22.095 1.00 14.90 ? 616  THR B N   1 
ATOM   7515 C  CA  . THR B 1 616 ? 11.330  40.260  -23.498 1.00 14.87 ? 616  THR B CA  1 
ATOM   7516 C  C   . THR B 1 616 ? 11.876  38.831  -23.642 1.00 14.72 ? 616  THR B C   1 
ATOM   7517 O  O   . THR B 1 616 ? 12.520  38.314  -22.731 1.00 14.28 ? 616  THR B O   1 
ATOM   7518 C  CB  . THR B 1 616 ? 12.252  41.260  -24.231 1.00 14.94 ? 616  THR B CB  1 
ATOM   7519 O  OG1 . THR B 1 616 ? 13.611  41.107  -23.780 1.00 15.19 ? 616  THR B OG1 1 
ATOM   7520 C  CG2 . THR B 1 616 ? 11.801  42.710  -23.973 1.00 14.52 ? 616  THR B CG2 1 
ATOM   7521 N  N   . SER B 1 617 ? 11.639  38.195  -24.781 1.00 14.41 ? 617  SER B N   1 
ATOM   7522 C  CA  . SER B 1 617 ? 12.231  36.883  -25.028 1.00 14.88 ? 617  SER B CA  1 
ATOM   7523 C  C   . SER B 1 617 ? 12.143  36.538  -26.501 1.00 15.55 ? 617  SER B C   1 
ATOM   7524 O  O   . SER B 1 617 ? 11.539  37.276  -27.283 1.00 15.26 ? 617  SER B O   1 
ATOM   7525 C  CB  . SER B 1 617 ? 11.537  35.800  -24.188 1.00 15.26 ? 617  SER B CB  1 
ATOM   7526 O  OG  . SER B 1 617 ? 10.133  35.690  -24.473 1.00 15.49 ? 617  SER B OG  1 
ATOM   7527 N  N   . TYR B 1 618 ? 12.757  35.423  -26.896 1.00 15.97 ? 618  TYR B N   1 
ATOM   7528 C  CA  . TYR B 1 618 ? 12.481  34.885  -28.213 1.00 15.77 ? 618  TYR B CA  1 
ATOM   7529 C  C   . TYR B 1 618 ? 11.537  33.739  -28.040 1.00 16.09 ? 618  TYR B C   1 
ATOM   7530 O  O   . TYR B 1 618 ? 11.489  33.108  -26.975 1.00 15.47 ? 618  TYR B O   1 
ATOM   7531 C  CB  . TYR B 1 618 ? 13.731  34.520  -29.004 1.00 15.99 ? 618  TYR B CB  1 
ATOM   7532 C  CG  . TYR B 1 618 ? 14.468  33.231  -28.649 1.00 16.26 ? 618  TYR B CG  1 
ATOM   7533 C  CD1 . TYR B 1 618 ? 14.118  32.013  -29.232 1.00 16.13 ? 618  TYR B CD1 1 
ATOM   7534 C  CD2 . TYR B 1 618 ? 15.563  33.255  -27.805 1.00 15.86 ? 618  TYR B CD2 1 
ATOM   7535 C  CE1 . TYR B 1 618 ? 14.827  30.846  -28.945 1.00 16.37 ? 618  TYR B CE1 1 
ATOM   7536 C  CE2 . TYR B 1 618 ? 16.265  32.093  -27.495 1.00 16.00 ? 618  TYR B CE2 1 
ATOM   7537 C  CZ  . TYR B 1 618 ? 15.895  30.897  -28.064 1.00 16.15 ? 618  TYR B CZ  1 
ATOM   7538 O  OH  . TYR B 1 618 ? 16.610  29.772  -27.786 1.00 16.04 ? 618  TYR B OH  1 
ATOM   7539 N  N   . MET B 1 619 ? 10.755  33.523  -29.089 1.00 15.58 ? 619  MET B N   1 
ATOM   7540 C  CA  . MET B 1 619 ? 9.686   32.554  -29.102 1.00 16.17 ? 619  MET B CA  1 
ATOM   7541 C  C   . MET B 1 619 ? 9.961   31.544  -30.202 1.00 15.56 ? 619  MET B C   1 
ATOM   7542 O  O   . MET B 1 619 ? 10.445  31.906  -31.265 1.00 15.27 ? 619  MET B O   1 
ATOM   7543 C  CB  . MET B 1 619 ? 8.338   33.243  -29.362 1.00 15.99 ? 619  MET B CB  1 
ATOM   7544 C  CG  . MET B 1 619 ? 7.174   32.292  -29.607 1.00 16.25 ? 619  MET B CG  1 
ATOM   7545 S  SD  . MET B 1 619 ? 5.575   33.121  -29.383 1.00 15.75 ? 619  MET B SD  1 
ATOM   7546 C  CE  . MET B 1 619 ? 5.498   33.325  -27.605 1.00 15.35 ? 619  MET B CE  1 
ATOM   7547 N  N   . THR B 1 620 ? 9.617   30.291  -29.919 1.00 15.84 ? 620  THR B N   1 
ATOM   7548 C  CA  . THR B 1 620 ? 9.801   29.156  -30.809 1.00 16.06 ? 620  THR B CA  1 
ATOM   7549 C  C   . THR B 1 620 ? 11.265  28.757  -30.792 1.00 16.76 ? 620  THR B C   1 
ATOM   7550 O  O   . THR B 1 620 ? 12.169  29.585  -31.072 1.00 16.39 ? 620  THR B O   1 
ATOM   7551 C  CB  . THR B 1 620 ? 9.366   29.419  -32.256 1.00 16.39 ? 620  THR B CB  1 
ATOM   7552 O  OG1 . THR B 1 620 ? 8.069   30.036  -32.283 1.00 16.04 ? 620  THR B OG1 1 
ATOM   7553 C  CG2 . THR B 1 620 ? 9.352   28.106  -33.030 1.00 16.78 ? 620  THR B CG2 1 
ATOM   7554 N  N   . ASN B 1 621 ? 11.523  27.494  -30.462 1.00 16.66 ? 621  ASN B N   1 
ATOM   7555 C  CA  . ASN B 1 621 ? 12.909  27.045  -30.437 1.00 17.03 ? 621  ASN B CA  1 
ATOM   7556 C  C   . ASN B 1 621 ? 13.437  26.886  -31.825 1.00 17.11 ? 621  ASN B C   1 
ATOM   7557 O  O   . ASN B 1 621 ? 12.677  26.703  -32.772 1.00 18.03 ? 621  ASN B O   1 
ATOM   7558 C  CB  . ASN B 1 621 ? 13.089  25.811  -29.573 1.00 17.10 ? 621  ASN B CB  1 
ATOM   7559 C  CG  . ASN B 1 621 ? 13.140  26.172  -28.104 1.00 17.68 ? 621  ASN B CG  1 
ATOM   7560 O  OD1 . ASN B 1 621 ? 14.112  26.763  -27.654 1.00 18.58 ? 621  ASN B OD1 1 
ATOM   7561 N  ND2 . ASN B 1 621 ? 12.088  25.865  -27.363 1.00 17.99 ? 621  ASN B ND2 1 
ATOM   7562 N  N   . ARG B 1 622 ? 14.752  27.002  -31.931 1.00 17.46 ? 622  ARG B N   1 
ATOM   7563 C  CA  . ARG B 1 622 ? 15.447  27.057  -33.199 1.00 17.78 ? 622  ARG B CA  1 
ATOM   7564 C  C   . ARG B 1 622 ? 15.398  25.756  -33.999 1.00 18.40 ? 622  ARG B C   1 
ATOM   7565 O  O   . ARG B 1 622 ? 15.100  24.688  -33.455 1.00 18.08 ? 622  ARG B O   1 
ATOM   7566 C  CB  . ARG B 1 622 ? 16.912  27.429  -32.957 1.00 17.73 ? 622  ARG B CB  1 
ATOM   7567 C  CG  . ARG B 1 622 ? 17.135  28.825  -32.397 1.00 18.87 ? 622  ARG B CG  1 
ATOM   7568 C  CD  . ARG B 1 622 ? 18.528  28.925  -31.793 1.00 19.73 ? 622  ARG B CD  1 
ATOM   7569 N  NE  . ARG B 1 622 ? 19.564  28.650  -32.784 1.00 20.45 ? 622  ARG B NE  1 
ATOM   7570 C  CZ  . ARG B 1 622 ? 20.862  28.561  -32.504 1.00 20.48 ? 622  ARG B CZ  1 
ATOM   7571 N  NH1 . ARG B 1 622 ? 21.281  28.726  -31.265 1.00 19.71 ? 622  ARG B NH1 1 
ATOM   7572 N  NH2 . ARG B 1 622 ? 21.743  28.307  -33.474 1.00 20.42 ? 622  ARG B NH2 1 
ATOM   7573 N  N   . ASN B 1 623 ? 15.706  25.881  -35.293 1.00 17.75 ? 623  ASN B N   1 
ATOM   7574 C  CA  . ASN B 1 623 ? 15.990  24.738  -36.159 1.00 18.75 ? 623  ASN B CA  1 
ATOM   7575 C  C   . ASN B 1 623 ? 14.762  23.941  -36.561 1.00 19.38 ? 623  ASN B C   1 
ATOM   7576 O  O   . ASN B 1 623 ? 14.861  22.753  -36.818 1.00 20.02 ? 623  ASN B O   1 
ATOM   7577 C  CB  . ASN B 1 623 ? 17.057  23.826  -35.530 1.00 18.29 ? 623  ASN B CB  1 
ATOM   7578 C  CG  . ASN B 1 623 ? 18.359  24.567  -35.257 1.00 18.32 ? 623  ASN B CG  1 
ATOM   7579 O  OD1 . ASN B 1 623 ? 18.835  25.324  -36.097 1.00 18.05 ? 623  ASN B OD1 1 
ATOM   7580 N  ND2 . ASN B 1 623 ? 18.929  24.359  -34.087 1.00 18.07 ? 623  ASN B ND2 1 
ATOM   7581 N  N   . GLY B 1 624 ? 13.607  24.605  -36.628 1.00 19.25 ? 624  GLY B N   1 
ATOM   7582 C  CA  . GLY B 1 624 ? 12.397  23.963  -37.095 1.00 19.54 ? 624  GLY B CA  1 
ATOM   7583 C  C   . GLY B 1 624 ? 11.820  22.888  -36.191 1.00 19.46 ? 624  GLY B C   1 
ATOM   7584 O  O   . GLY B 1 624 ? 11.067  22.040  -36.668 1.00 19.88 ? 624  GLY B O   1 
ATOM   7585 N  N   . VAL B 1 625 ? 12.129  22.930  -34.890 1.00 19.61 ? 625  VAL B N   1 
ATOM   7586 C  CA  . VAL B 1 625 ? 11.595  21.934  -33.947 1.00 19.15 ? 625  VAL B CA  1 
ATOM   7587 C  C   . VAL B 1 625 ? 10.086  22.075  -33.733 1.00 19.53 ? 625  VAL B C   1 
ATOM   7588 O  O   . VAL B 1 625 ? 9.459   21.137  -33.272 1.00 19.38 ? 625  VAL B O   1 
ATOM   7589 C  CB  . VAL B 1 625 ? 12.281  21.961  -32.556 1.00 18.65 ? 625  VAL B CB  1 
ATOM   7590 C  CG1 . VAL B 1 625 ? 13.757  21.573  -32.663 1.00 18.95 ? 625  VAL B CG1 1 
ATOM   7591 C  CG2 . VAL B 1 625 ? 12.095  23.305  -31.863 1.00 18.29 ? 625  VAL B CG2 1 
ATOM   7592 N  N   . ALA B 1 626 ? 9.512   23.245  -34.032 1.00 19.28 ? 626  ALA B N   1 
ATOM   7593 C  CA  . ALA B 1 626 ? 8.059   23.419  -33.970 1.00 19.76 ? 626  ALA B CA  1 
ATOM   7594 C  C   . ALA B 1 626 ? 7.376   23.233  -35.326 1.00 20.44 ? 626  ALA B C   1 
ATOM   7595 O  O   . ALA B 1 626 ? 6.170   23.471  -35.453 1.00 20.17 ? 626  ALA B O   1 
ATOM   7596 C  CB  . ALA B 1 626 ? 7.710   24.778  -33.389 1.00 19.58 ? 626  ALA B CB  1 
ATOM   7597 N  N   . GLY B 1 627 ? 8.138   22.798  -36.329 1.00 20.26 ? 627  GLY B N   1 
ATOM   7598 C  CA  . GLY B 1 627 ? 7.615   22.598  -37.689 1.00 20.67 ? 627  GLY B CA  1 
ATOM   7599 C  C   . GLY B 1 627 ? 8.437   23.415  -38.665 1.00 21.26 ? 627  GLY B C   1 
ATOM   7600 O  O   . GLY B 1 627 ? 9.011   24.447  -38.285 1.00 21.93 ? 627  GLY B O   1 
ATOM   7601 N  N   . LYS B 1 628 ? 8.507   22.966  -39.916 1.00 22.86 ? 628  LYS B N   1 
ATOM   7602 C  CA  . LYS B 1 628 ? 9.321   23.637  -40.910 1.00 25.00 ? 628  LYS B CA  1 
ATOM   7603 C  C   . LYS B 1 628 ? 8.833   25.066  -41.168 1.00 23.25 ? 628  LYS B C   1 
ATOM   7604 O  O   . LYS B 1 628 ? 7.645   25.308  -41.336 1.00 22.67 ? 628  LYS B O   1 
ATOM   7605 C  CB  . LYS B 1 628 ? 9.448   22.822  -42.211 1.00 29.59 ? 628  LYS B CB  1 
ATOM   7606 C  CG  . LYS B 1 628 ? 8.290   22.862  -43.200 1.00 34.87 ? 628  LYS B CG  1 
ATOM   7607 C  CD  . LYS B 1 628 ? 7.264   21.761  -42.925 1.00 39.06 ? 628  LYS B CD  1 
ATOM   7608 C  CE  . LYS B 1 628 ? 6.328   21.497  -44.103 1.00 42.27 ? 628  LYS B CE  1 
ATOM   7609 N  NZ  . LYS B 1 628 ? 5.245   22.517  -44.232 1.00 42.88 ? 628  LYS B NZ  1 
ATOM   7610 N  N   . GLY B 1 629 ? 9.754   26.021  -41.159 1.00 21.78 ? 629  GLY B N   1 
ATOM   7611 C  CA  . GLY B 1 629 ? 9.384   27.419  -41.369 1.00 21.62 ? 629  GLY B CA  1 
ATOM   7612 C  C   . GLY B 1 629 ? 8.748   28.117  -40.163 1.00 21.72 ? 629  GLY B C   1 
ATOM   7613 O  O   . GLY B 1 629 ? 8.421   29.312  -40.243 1.00 21.32 ? 629  GLY B O   1 
ATOM   7614 N  N   . MET B 1 630 ? 8.586   27.401  -39.048 1.00 20.81 ? 630  MET B N   1 
ATOM   7615 C  CA  . MET B 1 630 ? 8.207   28.024  -37.792 1.00 20.84 ? 630  MET B CA  1 
ATOM   7616 C  C   . MET B 1 630 ? 9.498   28.552  -37.153 1.00 19.54 ? 630  MET B C   1 
ATOM   7617 O  O   . MET B 1 630 ? 10.151  27.887  -36.356 1.00 18.92 ? 630  MET B O   1 
ATOM   7618 C  CB  . MET B 1 630 ? 7.440   27.049  -36.880 1.00 22.32 ? 630  MET B CB  1 
ATOM   7619 C  CG  . MET B 1 630 ? 6.100   26.531  -37.432 1.00 24.02 ? 630  MET B CG  1 
ATOM   7620 S  SD  . MET B 1 630 ? 4.866   27.822  -37.765 1.00 26.38 ? 630  MET B SD  1 
ATOM   7621 C  CE  . MET B 1 630 ? 3.334   26.923  -37.486 1.00 28.77 ? 630  MET B CE  1 
ATOM   7622 N  N   . ASP B 1 631 ? 9.872   29.767  -37.528 1.00 18.94 ? 631  ASP B N   1 
ATOM   7623 C  CA  . ASP B 1 631 ? 11.171  30.296  -37.160 1.00 18.01 ? 631  ASP B CA  1 
ATOM   7624 C  C   . ASP B 1 631 ? 11.155  30.849  -35.755 1.00 17.46 ? 631  ASP B C   1 
ATOM   7625 O  O   . ASP B 1 631 ? 10.114  31.275  -35.259 1.00 17.83 ? 631  ASP B O   1 
ATOM   7626 C  CB  . ASP B 1 631 ? 11.590  31.387  -38.133 1.00 19.06 ? 631  ASP B CB  1 
ATOM   7627 C  CG  . ASP B 1 631 ? 11.657  30.896  -39.556 1.00 19.62 ? 631  ASP B CG  1 
ATOM   7628 O  OD1 . ASP B 1 631 ? 11.912  29.699  -39.766 1.00 20.33 ? 631  ASP B OD1 1 
ATOM   7629 O  OD2 . ASP B 1 631 ? 11.445  31.710  -40.465 1.00 20.17 ? 631  ASP B OD2 1 
ATOM   7630 N  N   . SER B 1 632 ? 12.319  30.847  -35.113 1.00 16.69 ? 632  SER B N   1 
ATOM   7631 C  CA  . SER B 1 632 ? 12.496  31.616  -33.890 1.00 16.09 ? 632  SER B CA  1 
ATOM   7632 C  C   . SER B 1 632 ? 12.193  33.069  -34.200 1.00 15.83 ? 632  SER B C   1 
ATOM   7633 O  O   . SER B 1 632 ? 12.582  33.579  -35.256 1.00 15.20 ? 632  SER B O   1 
ATOM   7634 C  CB  . SER B 1 632 ? 13.905  31.433  -33.326 1.00 16.22 ? 632  SER B CB  1 
ATOM   7635 O  OG  . SER B 1 632 ? 14.163  30.045  -33.075 1.00 15.64 ? 632  SER B OG  1 
ATOM   7636 N  N   . THR B 1 633 ? 11.443  33.702  -33.303 1.00 15.73 ? 633  THR B N   1 
ATOM   7637 C  CA  . THR B 1 633 ? 10.917  35.046  -33.528 1.00 15.95 ? 633  THR B CA  1 
ATOM   7638 C  C   . THR B 1 633 ? 10.901  35.791  -32.194 1.00 16.49 ? 633  THR B C   1 
ATOM   7639 O  O   . THR B 1 633 ? 11.331  35.225  -31.174 1.00 15.75 ? 633  THR B O   1 
ATOM   7640 C  CB  . THR B 1 633 ? 9.513   34.992  -34.168 1.00 15.92 ? 633  THR B CB  1 
ATOM   7641 O  OG1 . THR B 1 633 ? 9.098   36.318  -34.538 1.00 15.84 ? 633  THR B OG1 1 
ATOM   7642 C  CG2 . THR B 1 633 ? 8.493   34.331  -33.256 1.00 15.56 ? 633  THR B CG2 1 
ATOM   7643 N  N   . TRP B 1 634 ? 10.428  37.035  -32.196 1.00 16.37 ? 634  TRP B N   1 
ATOM   7644 C  CA  . TRP B 1 634 ? 10.348  37.829  -30.967 1.00 17.23 ? 634  TRP B CA  1 
ATOM   7645 C  C   . TRP B 1 634 ? 9.004   37.589  -30.299 1.00 17.30 ? 634  TRP B C   1 
ATOM   7646 O  O   . TRP B 1 634 ? 7.962   37.788  -30.912 1.00 18.11 ? 634  TRP B O   1 
ATOM   7647 C  CB  . TRP B 1 634 ? 10.531  39.328  -31.249 1.00 17.31 ? 634  TRP B CB  1 
ATOM   7648 C  CG  . TRP B 1 634 ? 11.920  39.712  -31.526 1.00 17.65 ? 634  TRP B CG  1 
ATOM   7649 C  CD1 . TRP B 1 634 ? 13.035  38.922  -31.385 1.00 17.65 ? 634  TRP B CD1 1 
ATOM   7650 C  CD2 . TRP B 1 634 ? 12.391  40.995  -31.945 1.00 17.65 ? 634  TRP B CD2 1 
ATOM   7651 N  NE1 . TRP B 1 634 ? 14.154  39.624  -31.705 1.00 17.76 ? 634  TRP B NE1 1 
ATOM   7652 C  CE2 . TRP B 1 634 ? 13.802  40.899  -32.062 1.00 18.09 ? 634  TRP B CE2 1 
ATOM   7653 C  CE3 . TRP B 1 634 ? 11.769  42.213  -32.242 1.00 17.46 ? 634  TRP B CE3 1 
ATOM   7654 C  CZ2 . TRP B 1 634 ? 14.609  41.984  -32.462 1.00 17.84 ? 634  TRP B CZ2 1 
ATOM   7655 C  CZ3 . TRP B 1 634 ? 12.578  43.303  -32.661 1.00 18.11 ? 634  TRP B CZ3 1 
ATOM   7656 C  CH2 . TRP B 1 634 ? 13.981  43.177  -32.751 1.00 17.73 ? 634  TRP B CH2 1 
ATOM   7657 N  N   . ALA B 1 635 ? 9.040   37.154  -29.042 1.00 16.67 ? 635  ALA B N   1 
ATOM   7658 C  CA  . ALA B 1 635 ? 7.840   36.892  -28.295 1.00 16.33 ? 635  ALA B CA  1 
ATOM   7659 C  C   . ALA B 1 635 ? 7.114   38.197  -27.977 1.00 16.61 ? 635  ALA B C   1 
ATOM   7660 O  O   . ALA B 1 635 ? 7.720   39.269  -27.976 1.00 16.84 ? 635  ALA B O   1 
ATOM   7661 C  CB  . ALA B 1 635 ? 8.189   36.188  -26.997 1.00 16.57 ? 635  ALA B CB  1 
ATOM   7662 N  N   . PRO B 1 636 ? 5.814   38.108  -27.681 1.00 16.71 ? 636  PRO B N   1 
ATOM   7663 C  CA  . PRO B 1 636 ? 5.200   39.232  -26.988 1.00 16.61 ? 636  PRO B CA  1 
ATOM   7664 C  C   . PRO B 1 636 ? 5.923   39.462  -25.658 1.00 16.37 ? 636  PRO B C   1 
ATOM   7665 O  O   . PRO B 1 636 ? 6.432   38.520  -25.036 1.00 15.69 ? 636  PRO B O   1 
ATOM   7666 C  CB  . PRO B 1 636 ? 3.757   38.762  -26.745 1.00 16.44 ? 636  PRO B CB  1 
ATOM   7667 C  CG  . PRO B 1 636 ? 3.544   37.638  -27.688 1.00 16.84 ? 636  PRO B CG  1 
ATOM   7668 C  CD  . PRO B 1 636 ? 4.887   36.970  -27.802 1.00 17.01 ? 636  PRO B CD  1 
ATOM   7669 N  N   . SER B 1 637 ? 6.000   40.713  -25.246 1.00 16.17 ? 637  SER B N   1 
ATOM   7670 C  CA  . SER B 1 637 ? 6.640   41.034  -23.992 1.00 16.75 ? 637  SER B CA  1 
ATOM   7671 C  C   . SER B 1 637 ? 5.561   41.133  -22.914 1.00 17.42 ? 637  SER B C   1 
ATOM   7672 O  O   . SER B 1 637 ? 4.407   41.411  -23.211 1.00 17.93 ? 637  SER B O   1 
ATOM   7673 C  CB  . SER B 1 637 ? 7.425   42.323  -24.133 1.00 16.85 ? 637  SER B CB  1 
ATOM   7674 O  OG  . SER B 1 637 ? 8.226   42.270  -25.301 1.00 16.99 ? 637  SER B OG  1 
ATOM   7675 N  N   . PHE B 1 638 ? 5.934   40.879  -21.671 1.00 17.73 ? 638  PHE B N   1 
ATOM   7676 C  CA  . PHE B 1 638 ? 4.992   40.964  -20.575 1.00 17.70 ? 638  PHE B CA  1 
ATOM   7677 C  C   . PHE B 1 638 ? 5.611   41.645  -19.356 1.00 18.16 ? 638  PHE B C   1 
ATOM   7678 O  O   . PHE B 1 638 ? 6.844   41.617  -19.157 1.00 18.09 ? 638  PHE B O   1 
ATOM   7679 C  CB  . PHE B 1 638 ? 4.438   39.577  -20.233 1.00 17.73 ? 638  PHE B CB  1 
ATOM   7680 C  CG  . PHE B 1 638 ? 5.487   38.570  -19.843 1.00 18.46 ? 638  PHE B CG  1 
ATOM   7681 C  CD1 . PHE B 1 638 ? 6.112   37.778  -20.809 1.00 18.13 ? 638  PHE B CD1 1 
ATOM   7682 C  CD2 . PHE B 1 638 ? 5.826   38.379  -18.502 1.00 18.00 ? 638  PHE B CD2 1 
ATOM   7683 C  CE1 . PHE B 1 638 ? 7.060   36.827  -20.438 1.00 18.13 ? 638  PHE B CE1 1 
ATOM   7684 C  CE2 . PHE B 1 638 ? 6.777   37.435  -18.136 1.00 18.08 ? 638  PHE B CE2 1 
ATOM   7685 C  CZ  . PHE B 1 638 ? 7.397   36.664  -19.104 1.00 17.97 ? 638  PHE B CZ  1 
ATOM   7686 N  N   . LEU B 1 639 ? 4.750   42.289  -18.564 1.00 18.64 ? 639  LEU B N   1 
ATOM   7687 C  CA  . LEU B 1 639 ? 5.170   42.935  -17.324 1.00 19.23 ? 639  LEU B CA  1 
ATOM   7688 C  C   . LEU B 1 639 ? 5.408   41.946  -16.178 1.00 18.56 ? 639  LEU B C   1 
ATOM   7689 O  O   . LEU B 1 639 ? 4.716   40.947  -16.035 1.00 18.39 ? 639  LEU B O   1 
ATOM   7690 C  CB  . LEU B 1 639 ? 4.150   43.986  -16.869 1.00 20.04 ? 639  LEU B CB  1 
ATOM   7691 C  CG  . LEU B 1 639 ? 4.082   45.296  -17.651 1.00 20.90 ? 639  LEU B CG  1 
ATOM   7692 C  CD1 . LEU B 1 639 ? 3.083   46.199  -16.954 1.00 22.12 ? 639  LEU B CD1 1 
ATOM   7693 C  CD2 . LEU B 1 639 ? 5.435   45.987  -17.766 1.00 21.03 ? 639  LEU B CD2 1 
ATOM   7694 N  N   . LEU B 1 640 ? 6.411   42.266  -15.374 1.00 18.68 ? 640  LEU B N   1 
ATOM   7695 C  CA  . LEU B 1 640 ? 6.793   41.500  -14.216 1.00 19.22 ? 640  LEU B CA  1 
ATOM   7696 C  C   . LEU B 1 640 ? 6.874   42.518  -13.079 1.00 19.82 ? 640  LEU B C   1 
ATOM   7697 O  O   . LEU B 1 640 ? 7.568   43.542  -13.186 1.00 17.94 ? 640  LEU B O   1 
ATOM   7698 C  CB  . LEU B 1 640 ? 8.156   40.827  -14.438 1.00 19.02 ? 640  LEU B CB  1 
ATOM   7699 C  CG  . LEU B 1 640 ? 8.797   40.187  -13.202 1.00 19.42 ? 640  LEU B CG  1 
ATOM   7700 C  CD1 . LEU B 1 640 ? 8.000   38.967  -12.775 1.00 19.35 ? 640  LEU B CD1 1 
ATOM   7701 C  CD2 . LEU B 1 640 ? 10.246  39.813  -13.463 1.00 19.81 ? 640  LEU B CD2 1 
ATOM   7702 N  N   . GLN B 1 641 ? 6.153   42.232  -12.003 1.00 20.80 ? 641  GLN B N   1 
ATOM   7703 C  CA  . GLN B 1 641 ? 6.145   43.107  -10.847 1.00 21.28 ? 641  GLN B CA  1 
ATOM   7704 C  C   . GLN B 1 641 ? 7.143   42.631  -9.832  1.00 21.37 ? 641  GLN B C   1 
ATOM   7705 O  O   . GLN B 1 641 ? 7.200   41.433  -9.507  1.00 20.07 ? 641  GLN B O   1 
ATOM   7706 C  CB  . GLN B 1 641 ? 4.782   43.128  -10.213 1.00 21.59 ? 641  GLN B CB  1 
ATOM   7707 C  CG  . GLN B 1 641 ? 4.696   44.054  -9.018  1.00 22.44 ? 641  GLN B CG  1 
ATOM   7708 C  CD  . GLN B 1 641 ? 3.265   44.289  -8.649  1.00 23.22 ? 641  GLN B CD  1 
ATOM   7709 O  OE1 . GLN B 1 641 ? 2.542   44.956  -9.371  1.00 24.23 ? 641  GLN B OE1 1 
ATOM   7710 N  NE2 . GLN B 1 641 ? 2.826   43.678  -7.561  1.00 24.77 ? 641  GLN B NE2 1 
ATOM   7711 N  N   . ILE B 1 642 ? 7.910   43.585  -9.320  1.00 22.00 ? 642  ILE B N   1 
ATOM   7712 C  CA  . ILE B 1 642 ? 8.917   43.318  -8.325  1.00 23.75 ? 642  ILE B CA  1 
ATOM   7713 C  C   . ILE B 1 642 ? 8.406   43.937  -7.034  1.00 24.90 ? 642  ILE B C   1 
ATOM   7714 O  O   . ILE B 1 642 ? 8.112   45.124  -6.991  1.00 25.70 ? 642  ILE B O   1 
ATOM   7715 C  CB  . ILE B 1 642 ? 10.266  43.953  -8.718  1.00 24.65 ? 642  ILE B CB  1 
ATOM   7716 C  CG1 . ILE B 1 642 ? 10.653  43.587  -10.158 1.00 25.12 ? 642  ILE B CG1 1 
ATOM   7717 C  CG2 . ILE B 1 642 ? 11.368  43.528  -7.754  1.00 25.44 ? 642  ILE B CG2 1 
ATOM   7718 C  CD1 . ILE B 1 642 ? 10.687  42.100  -10.438 1.00 24.85 ? 642  ILE B CD1 1 
ATOM   7719 N  N   . ASN B 1 643 ? 8.299   43.130  -5.986  1.00 25.79 ? 643  ASN B N   1 
ATOM   7720 C  CA  . ASN B 1 643 ? 7.691   43.574  -4.728  1.00 26.18 ? 643  ASN B CA  1 
ATOM   7721 C  C   . ASN B 1 643 ? 8.743   43.936  -3.701  1.00 27.22 ? 643  ASN B C   1 
ATOM   7722 O  O   . ASN B 1 643 ? 9.842   43.391  -3.734  1.00 29.94 ? 643  ASN B O   1 
ATOM   7723 C  CB  . ASN B 1 643 ? 6.790   42.482  -4.162  1.00 24.78 ? 643  ASN B CB  1 
ATOM   7724 C  CG  . ASN B 1 643 ? 5.674   42.111  -5.105  1.00 24.81 ? 643  ASN B CG  1 
ATOM   7725 O  OD1 . ASN B 1 643 ? 5.034   42.990  -5.703  1.00 24.58 ? 643  ASN B OD1 1 
ATOM   7726 N  ND2 . ASN B 1 643 ? 5.432   40.798  -5.261  1.00 24.44 ? 643  ASN B ND2 1 
ATOM   7727 N  N   . PRO B 1 644 ? 8.413   44.848  -2.770  1.00 28.71 ? 644  PRO B N   1 
ATOM   7728 C  CA  . PRO B 1 644 ? 9.398   45.269  -1.758  1.00 28.70 ? 644  PRO B CA  1 
ATOM   7729 C  C   . PRO B 1 644 ? 9.942   44.132  -0.869  1.00 28.09 ? 644  PRO B C   1 
ATOM   7730 O  O   . PRO B 1 644 ? 11.062  44.236  -0.360  1.00 29.19 ? 644  PRO B O   1 
ATOM   7731 C  CB  . PRO B 1 644 ? 8.614   46.274  -0.900  1.00 29.31 ? 644  PRO B CB  1 
ATOM   7732 C  CG  . PRO B 1 644 ? 7.498   46.736  -1.762  1.00 29.31 ? 644  PRO B CG  1 
ATOM   7733 C  CD  . PRO B 1 644 ? 7.136   45.579  -2.637  1.00 28.65 ? 644  PRO B CD  1 
ATOM   7734 N  N   . ASP B 1 645 ? 9.164   43.063  -0.696  1.00 27.26 ? 645  ASP B N   1 
ATOM   7735 C  CA  . ASP B 1 645 ? 9.583   41.914  0.116   1.00 27.39 ? 645  ASP B CA  1 
ATOM   7736 C  C   . ASP B 1 645 ? 10.399  40.862  -0.653  1.00 26.87 ? 645  ASP B C   1 
ATOM   7737 O  O   . ASP B 1 645 ? 10.469  39.711  -0.232  1.00 26.23 ? 645  ASP B O   1 
ATOM   7738 C  CB  . ASP B 1 645 ? 8.358   41.240  0.735   1.00 27.87 ? 645  ASP B CB  1 
ATOM   7739 C  CG  . ASP B 1 645 ? 7.463   40.569  -0.296  1.00 28.40 ? 645  ASP B CG  1 
ATOM   7740 O  OD1 . ASP B 1 645 ? 7.638   40.769  -1.526  1.00 27.04 ? 645  ASP B OD1 1 
ATOM   7741 O  OD2 . ASP B 1 645 ? 6.555   39.844  0.138   1.00 28.78 ? 645  ASP B OD2 1 
ATOM   7742 N  N   . ASN B 1 646 ? 11.002  41.258  -1.775  1.00 25.68 ? 646  ASN B N   1 
ATOM   7743 C  CA  . ASN B 1 646 ? 11.810  40.366  -2.619  1.00 24.31 ? 646  ASN B CA  1 
ATOM   7744 C  C   . ASN B 1 646 ? 11.041  39.167  -3.153  1.00 22.93 ? 646  ASN B C   1 
ATOM   7745 O  O   . ASN B 1 646 ? 11.611  38.094  -3.375  1.00 21.49 ? 646  ASN B O   1 
ATOM   7746 C  CB  . ASN B 1 646 ? 13.090  39.923  -1.898  1.00 24.21 ? 646  ASN B CB  1 
ATOM   7747 C  CG  . ASN B 1 646 ? 13.981  41.088  -1.532  1.00 24.22 ? 646  ASN B CG  1 
ATOM   7748 O  OD1 . ASN B 1 646 ? 13.955  42.130  -2.164  1.00 23.58 ? 646  ASN B OD1 1 
ATOM   7749 N  ND2 . ASN B 1 646 ? 14.788  40.903  -0.510  1.00 25.47 ? 646  ASN B ND2 1 
ATOM   7750 N  N   . THR B 1 647 ? 9.743   39.350  -3.361  1.00 22.26 ? 647  THR B N   1 
ATOM   7751 C  CA  . THR B 1 647 ? 8.968   38.412  -4.157  1.00 22.35 ? 647  THR B CA  1 
ATOM   7752 C  C   . THR B 1 647 ? 8.676   39.109  -5.481  1.00 22.89 ? 647  THR B C   1 
ATOM   7753 O  O   . THR B 1 647 ? 8.888   40.332  -5.620  1.00 22.60 ? 647  THR B O   1 
ATOM   7754 C  CB  . THR B 1 647 ? 7.648   37.992  -3.478  1.00 22.83 ? 647  THR B CB  1 
ATOM   7755 O  OG1 . THR B 1 647 ? 6.821   39.141  -3.254  1.00 22.03 ? 647  THR B OG1 1 
ATOM   7756 C  CG2 . THR B 1 647 ? 7.917   37.264  -2.145  1.00 22.87 ? 647  THR B CG2 1 
ATOM   7757 N  N   . THR B 1 648 ? 8.204   38.336  -6.454  1.00 21.90 ? 648  THR B N   1 
ATOM   7758 C  CA  . THR B 1 648 ? 7.794   38.890  -7.742  1.00 20.60 ? 648  THR B CA  1 
ATOM   7759 C  C   . THR B 1 648 ? 6.483   38.269  -8.185  1.00 20.55 ? 648  THR B C   1 
ATOM   7760 O  O   . THR B 1 648 ? 6.106   37.182  -7.730  1.00 20.14 ? 648  THR B O   1 
ATOM   7761 C  CB  . THR B 1 648 ? 8.865   38.632  -8.838  1.00 20.57 ? 648  THR B CB  1 
ATOM   7762 O  OG1 . THR B 1 648 ? 8.998   37.223  -9.092  1.00 19.38 ? 648  THR B OG1 1 
ATOM   7763 C  CG2 . THR B 1 648 ? 10.233  39.192  -8.430  1.00 20.26 ? 648  THR B CG2 1 
ATOM   7764 N  N   . THR B 1 649 ? 5.773   38.948  -9.076  1.00 20.81 ? 649  THR B N   1 
ATOM   7765 C  CA  . THR B 1 649 ? 4.670   38.294  -9.767  1.00 20.90 ? 649  THR B CA  1 
ATOM   7766 C  C   . THR B 1 649 ? 4.551   38.721  -11.232 1.00 20.32 ? 649  THR B C   1 
ATOM   7767 O  O   . THR B 1 649 ? 4.689   39.895  -11.582 1.00 18.09 ? 649  THR B O   1 
ATOM   7768 C  CB  . THR B 1 649 ? 3.311   38.452  -9.038  1.00 22.52 ? 649  THR B CB  1 
ATOM   7769 O  OG1 . THR B 1 649 ? 2.299   37.721  -9.759  1.00 22.62 ? 649  THR B OG1 1 
ATOM   7770 C  CG2 . THR B 1 649 ? 2.899   39.905  -8.927  1.00 22.83 ? 649  THR B CG2 1 
ATOM   7771 N  N   . VAL B 1 650 ? 4.308   37.736  -12.080 1.00 19.85 ? 650  VAL B N   1 
ATOM   7772 C  CA  . VAL B 1 650 ? 4.013   38.003  -13.467 1.00 21.25 ? 650  VAL B CA  1 
ATOM   7773 C  C   . VAL B 1 650 ? 2.654   38.688  -13.560 1.00 21.71 ? 650  VAL B C   1 
ATOM   7774 O  O   . VAL B 1 650 ? 1.718   38.252  -12.912 1.00 24.12 ? 650  VAL B O   1 
ATOM   7775 C  CB  . VAL B 1 650 ? 3.975   36.701  -14.268 1.00 20.90 ? 650  VAL B CB  1 
ATOM   7776 C  CG1 . VAL B 1 650 ? 3.511   36.968  -15.696 1.00 21.17 ? 650  VAL B CG1 1 
ATOM   7777 C  CG2 . VAL B 1 650 ? 5.345   36.029  -14.235 1.00 20.88 ? 650  VAL B CG2 1 
ATOM   7778 N  N   . LEU B 1 651 ? 2.555   39.767  -14.337 1.00 21.37 ? 651  LEU B N   1 
ATOM   7779 C  CA  . LEU B 1 651 ? 1.282   40.467  -14.526 1.00 21.46 ? 651  LEU B CA  1 
ATOM   7780 C  C   . LEU B 1 651 ? 0.672   40.037  -15.853 1.00 21.93 ? 651  LEU B C   1 
ATOM   7781 O  O   . LEU B 1 651 ? 1.395   39.610  -16.752 1.00 22.35 ? 651  LEU B O   1 
ATOM   7782 C  CB  . LEU B 1 651 ? 1.479   41.989  -14.486 1.00 21.09 ? 651  LEU B CB  1 
ATOM   7783 C  CG  . LEU B 1 651 ? 2.031   42.529  -13.170 1.00 20.70 ? 651  LEU B CG  1 
ATOM   7784 C  CD1 . LEU B 1 651 ? 2.331   44.020  -13.270 1.00 21.22 ? 651  LEU B CD1 1 
ATOM   7785 C  CD2 . LEU B 1 651 ? 1.073   42.260  -12.014 1.00 20.99 ? 651  LEU B CD2 1 
ATOM   7786 N  N   . ALA B 1 652 ? -0.655  40.113  -15.954 1.00 22.36 ? 652  ALA B N   1 
ATOM   7787 C  CA  . ALA B 1 652 ? -1.365  39.835  -17.209 1.00 24.24 ? 652  ALA B CA  1 
ATOM   7788 C  C   . ALA B 1 652 ? -1.448  41.106  -18.067 1.00 25.04 ? 652  ALA B C   1 
ATOM   7789 O  O   . ALA B 1 652 ? -2.529  41.530  -18.490 1.00 27.56 ? 652  ALA B O   1 
ATOM   7790 C  CB  . ALA B 1 652 ? -2.758  39.284  -16.928 1.00 24.45 ? 652  ALA B CB  1 
ATOM   7791 N  N   . LYS B 1 653 ? -0.296  41.735  -18.253 1.00 24.61 ? 653  LYS B N   1 
ATOM   7792 C  CA  . LYS B 1 653 ? -0.138  42.857  -19.143 1.00 25.71 ? 653  LYS B CA  1 
ATOM   7793 C  C   . LYS B 1 653 ? 0.853   42.362  -20.178 1.00 23.88 ? 653  LYS B C   1 
ATOM   7794 O  O   . LYS B 1 653 ? 1.954   41.931  -19.839 1.00 22.77 ? 653  LYS B O   1 
ATOM   7795 C  CB  . LYS B 1 653 ? 0.414   44.061  -18.396 1.00 28.28 ? 653  LYS B CB  1 
ATOM   7796 C  CG  . LYS B 1 653 ? -0.537  44.641  -17.353 1.00 31.01 ? 653  LYS B CG  1 
ATOM   7797 C  CD  . LYS B 1 653 ? -1.759  45.239  -18.013 1.00 33.82 ? 653  LYS B CD  1 
ATOM   7798 C  CE  . LYS B 1 653 ? -2.689  45.904  -17.015 1.00 35.90 ? 653  LYS B CE  1 
ATOM   7799 N  NZ  . LYS B 1 653 ? -4.016  46.136  -17.645 1.00 37.78 ? 653  LYS B NZ  1 
ATOM   7800 N  N   . MET B 1 654 ? 0.435   42.388  -21.432 1.00 21.99 ? 654  MET B N   1 
ATOM   7801 C  CA  . MET B 1 654 ? 1.194   41.805  -22.527 1.00 20.54 ? 654  MET B CA  1 
ATOM   7802 C  C   . MET B 1 654 ? 1.157   42.774  -23.724 1.00 20.40 ? 654  MET B C   1 
ATOM   7803 O  O   . MET B 1 654 ? 0.141   43.469  -23.951 1.00 18.59 ? 654  MET B O   1 
ATOM   7804 C  CB  . MET B 1 654 ? 0.580   40.456  -22.889 1.00 20.28 ? 654  MET B CB  1 
ATOM   7805 C  CG  . MET B 1 654 ? 1.289   39.709  -24.002 1.00 21.07 ? 654  MET B CG  1 
ATOM   7806 S  SD  . MET B 1 654 ? 0.633   38.056  -24.323 1.00 20.34 ? 654  MET B SD  1 
ATOM   7807 C  CE  . MET B 1 654 ? 0.968   37.260  -22.756 1.00 20.95 ? 654  MET B CE  1 
ATOM   7808 N  N   . THR B 1 655 ? 2.266   42.806  -24.470 1.00 19.10 ? 655  THR B N   1 
ATOM   7809 C  CA  . THR B 1 655 ? 2.419   43.662  -25.638 1.00 18.95 ? 655  THR B CA  1 
ATOM   7810 C  C   . THR B 1 655 ? 2.265   42.876  -26.945 1.00 18.52 ? 655  THR B C   1 
ATOM   7811 O  O   . THR B 1 655 ? 2.051   41.654  -26.937 1.00 17.65 ? 655  THR B O   1 
ATOM   7812 C  CB  . THR B 1 655 ? 3.827   44.290  -25.672 1.00 18.72 ? 655  THR B CB  1 
ATOM   7813 O  OG1 . THR B 1 655 ? 4.785   43.261  -25.905 1.00 18.51 ? 655  THR B OG1 1 
ATOM   7814 C  CG2 . THR B 1 655 ? 4.165   45.015  -24.383 1.00 18.81 ? 655  THR B CG2 1 
ATOM   7815 N  N   . ASN B 1 656 ? 2.409   43.580  -28.067 1.00 17.98 ? 656  ASN B N   1 
ATOM   7816 C  CA  . ASN B 1 656 ? 2.709   42.923  -29.339 1.00 19.36 ? 656  ASN B CA  1 
ATOM   7817 C  C   . ASN B 1 656 ? 4.054   42.196  -29.297 1.00 18.38 ? 656  ASN B C   1 
ATOM   7818 O  O   . ASN B 1 656 ? 4.892   42.492  -28.449 1.00 18.28 ? 656  ASN B O   1 
ATOM   7819 C  CB  . ASN B 1 656 ? 2.761   43.942  -30.474 1.00 21.37 ? 656  ASN B CB  1 
ATOM   7820 C  CG  . ASN B 1 656 ? 1.389   44.386  -30.926 1.00 22.94 ? 656  ASN B CG  1 
ATOM   7821 O  OD1 . ASN B 1 656 ? 0.400   43.668  -30.775 1.00 26.00 ? 656  ASN B OD1 1 
ATOM   7822 N  ND2 . ASN B 1 656 ? 1.329   45.558  -31.515 1.00 24.03 ? 656  ASN B ND2 1 
ATOM   7823 N  N   . GLN B 1 657 ? 4.245   41.234  -30.192 1.00 17.45 ? 657  GLN B N   1 
ATOM   7824 C  CA  . GLN B 1 657 ? 5.565   40.628  -30.394 1.00 17.56 ? 657  GLN B CA  1 
ATOM   7825 C  C   . GLN B 1 657 ? 6.609   41.710  -30.577 1.00 17.50 ? 657  GLN B C   1 
ATOM   7826 O  O   . GLN B 1 657 ? 6.397   42.650  -31.351 1.00 17.26 ? 657  GLN B O   1 
ATOM   7827 C  CB  . GLN B 1 657 ? 5.589   39.762  -31.642 1.00 17.31 ? 657  GLN B CB  1 
ATOM   7828 C  CG  . GLN B 1 657 ? 4.870   38.435  -31.497 1.00 18.32 ? 657  GLN B CG  1 
ATOM   7829 C  CD  . GLN B 1 657 ? 4.970   37.616  -32.768 1.00 17.75 ? 657  GLN B CD  1 
ATOM   7830 O  OE1 . GLN B 1 657 ? 4.043   37.586  -33.543 1.00 18.48 ? 657  GLN B OE1 1 
ATOM   7831 N  NE2 . GLN B 1 657 ? 6.117   36.977  -32.998 1.00 17.93 ? 657  GLN B NE2 1 
ATOM   7832 N  N   . GLY B 1 658 ? 7.726   41.582  -29.870 1.00 17.20 ? 658  GLY B N   1 
ATOM   7833 C  CA  . GLY B 1 658 ? 8.896   42.391  -30.167 1.00 17.60 ? 658  GLY B CA  1 
ATOM   7834 C  C   . GLY B 1 658 ? 8.845   43.817  -29.659 1.00 17.73 ? 658  GLY B C   1 
ATOM   7835 O  O   . GLY B 1 658 ? 9.488   44.701  -30.225 1.00 18.04 ? 658  GLY B O   1 
ATOM   7836 N  N   . ASP B 1 659 ? 8.072   44.044  -28.603 1.00 17.92 ? 659  ASP B N   1 
ATOM   7837 C  CA  . ASP B 1 659 ? 7.953   45.369  -28.005 1.00 17.77 ? 659  ASP B CA  1 
ATOM   7838 C  C   . ASP B 1 659 ? 8.959   45.451  -26.859 1.00 17.71 ? 659  ASP B C   1 
ATOM   7839 O  O   . ASP B 1 659 ? 8.924   44.634  -25.932 1.00 17.36 ? 659  ASP B O   1 
ATOM   7840 C  CB  . ASP B 1 659 ? 6.526   45.579  -27.504 1.00 18.35 ? 659  ASP B CB  1 
ATOM   7841 C  CG  . ASP B 1 659 ? 6.216   47.029  -27.164 1.00 18.24 ? 659  ASP B CG  1 
ATOM   7842 O  OD1 . ASP B 1 659 ? 7.160   47.819  -26.946 1.00 18.57 ? 659  ASP B OD1 1 
ATOM   7843 O  OD2 . ASP B 1 659 ? 5.011   47.355  -27.095 1.00 17.84 ? 659  ASP B OD2 1 
ATOM   7844 N  N   . TRP B 1 660 ? 9.862   46.423  -26.946 1.00 17.44 ? 660  TRP B N   1 
ATOM   7845 C  CA  . TRP B 1 660 ? 10.903  46.641  -25.940 1.00 17.84 ? 660  TRP B CA  1 
ATOM   7846 C  C   . TRP B 1 660 ? 10.621  47.839  -25.035 1.00 18.03 ? 660  TRP B C   1 
ATOM   7847 O  O   . TRP B 1 660 ? 11.383  48.100  -24.098 1.00 17.57 ? 660  TRP B O   1 
ATOM   7848 C  CB  . TRP B 1 660 ? 12.237  46.863  -26.639 1.00 18.32 ? 660  TRP B CB  1 
ATOM   7849 C  CG  . TRP B 1 660 ? 12.606  45.742  -27.552 1.00 18.15 ? 660  TRP B CG  1 
ATOM   7850 C  CD1 . TRP B 1 660 ? 12.204  45.570  -28.836 1.00 18.90 ? 660  TRP B CD1 1 
ATOM   7851 C  CD2 . TRP B 1 660 ? 13.444  44.642  -27.242 1.00 18.50 ? 660  TRP B CD2 1 
ATOM   7852 N  NE1 . TRP B 1 660 ? 12.738  44.414  -29.351 1.00 19.13 ? 660  TRP B NE1 1 
ATOM   7853 C  CE2 . TRP B 1 660 ? 13.517  43.832  -28.390 1.00 19.32 ? 660  TRP B CE2 1 
ATOM   7854 C  CE3 . TRP B 1 660 ? 14.153  44.262  -26.107 1.00 18.97 ? 660  TRP B CE3 1 
ATOM   7855 C  CZ2 . TRP B 1 660 ? 14.254  42.647  -28.426 1.00 19.63 ? 660  TRP B CZ2 1 
ATOM   7856 C  CZ3 . TRP B 1 660 ? 14.897  43.089  -26.149 1.00 19.56 ? 660  TRP B CZ3 1 
ATOM   7857 C  CH2 . TRP B 1 660 ? 14.936  42.299  -27.301 1.00 19.50 ? 660  TRP B CH2 1 
ATOM   7858 N  N   . ILE B 1 661 ? 9.528   48.552  -25.313 1.00 18.20 ? 661  ILE B N   1 
ATOM   7859 C  CA  . ILE B 1 661 ? 9.205   49.806  -24.626 1.00 19.46 ? 661  ILE B CA  1 
ATOM   7860 C  C   . ILE B 1 661 ? 7.768   49.750  -24.086 1.00 19.77 ? 661  ILE B C   1 
ATOM   7861 O  O   . ILE B 1 661 ? 6.804   49.882  -24.843 1.00 19.25 ? 661  ILE B O   1 
ATOM   7862 C  CB  . ILE B 1 661 ? 9.352   51.017  -25.585 1.00 20.00 ? 661  ILE B CB  1 
ATOM   7863 C  CG1 . ILE B 1 661 ? 10.786  51.096  -26.117 1.00 20.39 ? 661  ILE B CG1 1 
ATOM   7864 C  CG2 . ILE B 1 661 ? 8.928   52.321  -24.892 1.00 20.44 ? 661  ILE B CG2 1 
ATOM   7865 C  CD1 . ILE B 1 661 ? 10.936  52.013  -27.309 1.00 21.48 ? 661  ILE B CD1 1 
ATOM   7866 N  N   . TRP B 1 662 ? 7.618   49.548  -22.784 1.00 20.93 ? 662  TRP B N   1 
ATOM   7867 C  CA  . TRP B 1 662 ? 6.293   49.540  -22.203 1.00 21.13 ? 662  TRP B CA  1 
ATOM   7868 C  C   . TRP B 1 662 ? 5.773   50.954  -21.997 1.00 22.15 ? 662  TRP B C   1 
ATOM   7869 O  O   . TRP B 1 662 ? 6.454   51.795  -21.426 1.00 21.80 ? 662  TRP B O   1 
ATOM   7870 C  CB  . TRP B 1 662 ? 6.243   48.841  -20.860 1.00 20.86 ? 662  TRP B CB  1 
ATOM   7871 C  CG  . TRP B 1 662 ? 4.855   48.914  -20.318 1.00 21.08 ? 662  TRP B CG  1 
ATOM   7872 C  CD1 . TRP B 1 662 ? 4.354   49.849  -19.449 1.00 21.48 ? 662  TRP B CD1 1 
ATOM   7873 C  CD2 . TRP B 1 662 ? 3.761   48.054  -20.659 1.00 21.27 ? 662  TRP B CD2 1 
ATOM   7874 N  NE1 . TRP B 1 662 ? 3.015   49.617  -19.223 1.00 21.50 ? 662  TRP B NE1 1 
ATOM   7875 C  CE2 . TRP B 1 662 ? 2.624   48.517  -19.943 1.00 21.81 ? 662  TRP B CE2 1 
ATOM   7876 C  CE3 . TRP B 1 662 ? 3.635   46.927  -21.478 1.00 21.22 ? 662  TRP B CE3 1 
ATOM   7877 C  CZ2 . TRP B 1 662 ? 1.370   47.901  -20.039 1.00 21.61 ? 662  TRP B CZ2 1 
ATOM   7878 C  CZ3 . TRP B 1 662 ? 2.395   46.311  -21.575 1.00 22.28 ? 662  TRP B CZ3 1 
ATOM   7879 C  CH2 . TRP B 1 662 ? 1.274   46.797  -20.846 1.00 22.37 ? 662  TRP B CH2 1 
ATOM   7880 N  N   . ASP B 1 663 ? 4.543   51.170  -22.443 1.00 22.82 ? 663  ASP B N   1 
ATOM   7881 C  CA  . ASP B 1 663 ? 3.711   52.284  -22.013 1.00 24.50 ? 663  ASP B CA  1 
ATOM   7882 C  C   . ASP B 1 663 ? 2.250   51.811  -22.108 1.00 26.47 ? 663  ASP B C   1 
ATOM   7883 O  O   . ASP B 1 663 ? 1.991   50.660  -22.471 1.00 25.22 ? 663  ASP B O   1 
ATOM   7884 C  CB  . ASP B 1 663 ? 3.990   53.528  -22.867 1.00 24.10 ? 663  ASP B CB  1 
ATOM   7885 C  CG  . ASP B 1 663 ? 3.978   53.233  -24.367 1.00 23.04 ? 663  ASP B CG  1 
ATOM   7886 O  OD1 . ASP B 1 663 ? 3.093   52.489  -24.840 1.00 23.05 ? 663  ASP B OD1 1 
ATOM   7887 O  OD2 . ASP B 1 663 ? 4.850   53.756  -25.072 1.00 22.47 ? 663  ASP B OD2 1 
ATOM   7888 N  N   . ASP B 1 664 ? 1.299   52.675  -21.771 1.00 30.40 ? 664  ASP B N   1 
ATOM   7889 C  CA  . ASP B 1 664 ? -0.127  52.310  -21.834 1.00 32.56 ? 664  ASP B CA  1 
ATOM   7890 C  C   . ASP B 1 664 ? -0.598  51.958  -23.253 1.00 31.80 ? 664  ASP B C   1 
ATOM   7891 O  O   . ASP B 1 664 ? -1.311  50.961  -23.424 1.00 36.17 ? 664  ASP B O   1 
ATOM   7892 C  CB  . ASP B 1 664 ? -0.997  53.397  -21.191 1.00 34.77 ? 664  ASP B CB  1 
ATOM   7893 C  CG  . ASP B 1 664 ? -0.868  53.416  -19.663 1.00 38.69 ? 664  ASP B CG  1 
ATOM   7894 O  OD1 . ASP B 1 664 ? -0.709  52.338  -19.062 1.00 41.75 ? 664  ASP B OD1 1 
ATOM   7895 O  OD2 . ASP B 1 664 ? -0.919  54.501  -19.054 1.00 43.49 ? 664  ASP B OD2 1 
ATOM   7896 N  N   . SER B 1 665 ? -0.137  52.711  -24.256 1.00 29.92 ? 665  SER B N   1 
ATOM   7897 C  CA  . SER B 1 665 ? -0.368  52.390  -25.696 1.00 29.45 ? 665  SER B CA  1 
ATOM   7898 C  C   . SER B 1 665 ? 0.071   50.979  -26.118 1.00 26.01 ? 665  SER B C   1 
ATOM   7899 O  O   . SER B 1 665 ? -0.407  50.463  -27.120 1.00 24.95 ? 665  SER B O   1 
ATOM   7900 C  CB  . SER B 1 665 ? 0.357   53.410  -26.631 1.00 31.44 ? 665  SER B CB  1 
ATOM   7901 O  OG  . SER B 1 665 ? 1.692   52.979  -27.051 1.00 31.91 ? 665  SER B OG  1 
ATOM   7902 N  N   . SER B 1 666 ? 1.004   50.378  -25.382 1.00 23.56 ? 666  SER B N   1 
ATOM   7903 C  CA  . SER B 1 666 ? 1.659   49.146  -25.828 1.00 23.51 ? 666  SER B CA  1 
ATOM   7904 C  C   . SER B 1 666 ? 0.866   47.875  -25.537 1.00 23.54 ? 666  SER B C   1 
ATOM   7905 O  O   . SER B 1 666 ? 1.114   46.819  -26.133 1.00 22.85 ? 666  SER B O   1 
ATOM   7906 C  CB  . SER B 1 666 ? 3.067   49.043  -25.215 1.00 22.80 ? 666  SER B CB  1 
ATOM   7907 O  OG  . SER B 1 666 ? 3.914   50.088  -25.690 1.00 21.11 ? 666  SER B OG  1 
ATOM   7908 N  N   . GLU B 1 667 ? -0.094  47.956  -24.630 1.00 25.78 ? 667  GLU B N   1 
ATOM   7909 C  CA  . GLU B 1 667 ? -0.825  46.758  -24.224 1.00 27.88 ? 667  GLU B CA  1 
ATOM   7910 C  C   . GLU B 1 667 ? -1.658  46.215  -25.370 1.00 27.57 ? 667  GLU B C   1 
ATOM   7911 O  O   . GLU B 1 667 ? -2.376  46.965  -26.013 1.00 26.32 ? 667  GLU B O   1 
ATOM   7912 C  CB  . GLU B 1 667 ? -1.712  47.083  -23.033 1.00 30.55 ? 667  GLU B CB  1 
ATOM   7913 C  CG  . GLU B 1 667 ? -2.293  45.883  -22.331 1.00 33.82 ? 667  GLU B CG  1 
ATOM   7914 C  CD  . GLU B 1 667 ? -3.079  46.284  -21.092 1.00 36.80 ? 667  GLU B CD  1 
ATOM   7915 O  OE1 . GLU B 1 667 ? -2.792  47.351  -20.482 1.00 41.49 ? 667  GLU B OE1 1 
ATOM   7916 O  OE2 . GLU B 1 667 ? -3.983  45.532  -20.732 1.00 36.46 ? 667  GLU B OE2 1 
ATOM   7917 N  N   . ASN B 1 668 ? -1.529  44.920  -25.652 1.00 28.06 ? 668  ASN B N   1 
ATOM   7918 C  CA  . ASN B 1 668 ? -2.400  44.259  -26.617 1.00 30.47 ? 668  ASN B CA  1 
ATOM   7919 C  C   . ASN B 1 668 ? -2.977  42.990  -25.994 1.00 32.33 ? 668  ASN B C   1 
ATOM   7920 O  O   . ASN B 1 668 ? -2.311  41.962  -25.934 1.00 33.01 ? 668  ASN B O   1 
ATOM   7921 C  CB  . ASN B 1 668 ? -1.651  43.913  -27.917 1.00 29.46 ? 668  ASN B CB  1 
ATOM   7922 C  CG  . ASN B 1 668 ? -2.568  43.311  -28.974 1.00 30.55 ? 668  ASN B CG  1 
ATOM   7923 O  OD1 . ASN B 1 668 ? -3.716  42.987  -28.698 1.00 31.59 ? 668  ASN B OD1 1 
ATOM   7924 N  ND2 . ASN B 1 668 ? -2.063  43.162  -30.197 1.00 30.91 ? 668  ASN B ND2 1 
ATOM   7925 N  N   . LEU B 1 669 ? -4.229  43.055  -25.565 1.00 34.60 ? 669  LEU B N   1 
ATOM   7926 C  CA  . LEU B 1 669 ? -4.861  41.914  -24.902 1.00 36.91 ? 669  LEU B CA  1 
ATOM   7927 C  C   . LEU B 1 669 ? -5.259  40.778  -25.849 1.00 33.81 ? 669  LEU B C   1 
ATOM   7928 O  O   . LEU B 1 669 ? -5.541  39.687  -25.393 1.00 34.82 ? 669  LEU B O   1 
ATOM   7929 C  CB  . LEU B 1 669 ? -6.044  42.390  -24.047 1.00 40.41 ? 669  LEU B CB  1 
ATOM   7930 C  CG  . LEU B 1 669 ? -5.638  43.382  -22.933 1.00 42.41 ? 669  LEU B CG  1 
ATOM   7931 C  CD1 . LEU B 1 669 ? -6.827  43.792  -22.087 1.00 44.26 ? 669  LEU B CD1 1 
ATOM   7932 C  CD2 . LEU B 1 669 ? -4.539  42.842  -22.020 1.00 45.64 ? 669  LEU B CD2 1 
ATOM   7933 N  N   . ASP B 1 670 ? -5.230  40.999  -27.159 1.00 33.60 ? 670  ASP B N   1 
ATOM   7934 C  CA  . ASP B 1 670 ? -5.484  39.916  -28.116 1.00 33.36 ? 670  ASP B CA  1 
ATOM   7935 C  C   . ASP B 1 670 ? -4.354  38.874  -28.138 1.00 31.26 ? 670  ASP B C   1 
ATOM   7936 O  O   . ASP B 1 670 ? -4.554  37.765  -28.604 1.00 28.67 ? 670  ASP B O   1 
ATOM   7937 C  CB  . ASP B 1 670 ? -5.685  40.454  -29.541 1.00 37.67 ? 670  ASP B CB  1 
ATOM   7938 C  CG  . ASP B 1 670 ? -6.955  41.303  -29.691 1.00 43.31 ? 670  ASP B CG  1 
ATOM   7939 O  OD1 . ASP B 1 670 ? -7.922  41.114  -28.919 1.00 45.91 ? 670  ASP B OD1 1 
ATOM   7940 O  OD2 . ASP B 1 670 ? -6.989  42.161  -30.601 1.00 47.51 ? 670  ASP B OD2 1 
ATOM   7941 N  N   . MET B 1 671 ? -3.169  39.237  -27.650 1.00 29.24 ? 671  MET B N   1 
ATOM   7942 C  CA  . MET B 1 671 ? -2.034  38.319  -27.656 1.00 28.48 ? 671  MET B CA  1 
ATOM   7943 C  C   . MET B 1 671 ? -2.127  37.289  -26.524 1.00 28.29 ? 671  MET B C   1 
ATOM   7944 O  O   . MET B 1 671 ? -1.471  36.249  -26.574 1.00 27.67 ? 671  MET B O   1 
ATOM   7945 C  CB  . MET B 1 671 ? -0.721  39.105  -27.547 1.00 28.02 ? 671  MET B CB  1 
ATOM   7946 C  CG  . MET B 1 671 ? -0.545  40.169  -28.621 1.00 28.18 ? 671  MET B CG  1 
ATOM   7947 S  SD  . MET B 1 671 ? -0.650  39.577  -30.325 1.00 28.58 ? 671  MET B SD  1 
ATOM   7948 C  CE  . MET B 1 671 ? 0.853   38.613  -30.454 1.00 27.80 ? 671  MET B CE  1 
ATOM   7949 N  N   . ILE B 1 672 ? -2.930  37.574  -25.504 1.00 28.37 ? 672  ILE B N   1 
ATOM   7950 C  CA  . ILE B 1 672 ? -2.973  36.720  -24.324 1.00 30.55 ? 672  ILE B CA  1 
ATOM   7951 C  C   . ILE B 1 672 ? -3.737  35.436  -24.639 1.00 28.53 ? 672  ILE B C   1 
ATOM   7952 O  O   . ILE B 1 672 ? -4.856  35.465  -25.129 1.00 28.57 ? 672  ILE B O   1 
ATOM   7953 C  CB  . ILE B 1 672 ? -3.566  37.455  -23.093 1.00 33.49 ? 672  ILE B CB  1 
ATOM   7954 C  CG1 . ILE B 1 672 ? -2.810  38.792  -22.884 1.00 35.62 ? 672  ILE B CG1 1 
ATOM   7955 C  CG2 . ILE B 1 672 ? -3.525  36.551  -21.855 1.00 33.59 ? 672  ILE B CG2 1 
ATOM   7956 C  CD1 . ILE B 1 672 ? -2.347  39.108  -21.470 1.00 37.46 ? 672  ILE B CD1 1 
ATOM   7957 N  N   . GLY B 1 673 ? -3.098  34.307  -24.382 1.00 27.68 ? 673  GLY B N   1 
ATOM   7958 C  CA  . GLY B 1 673 ? -3.705  33.008  -24.627 1.00 27.48 ? 673  GLY B CA  1 
ATOM   7959 C  C   . GLY B 1 673 ? -4.075  32.377  -23.310 1.00 26.60 ? 673  GLY B C   1 
ATOM   7960 O  O   . GLY B 1 673 ? -3.955  33.001  -22.279 1.00 25.28 ? 673  GLY B O   1 
ATOM   7961 N  N   . ASP B 1 674 ? -4.566  31.147  -23.369 1.00 28.24 ? 674  ASP B N   1 
ATOM   7962 C  CA  . ASP B 1 674 ? -4.717  30.301  -22.188 1.00 29.09 ? 674  ASP B CA  1 
ATOM   7963 C  C   . ASP B 1 674 ? -4.189  28.919  -22.547 1.00 28.07 ? 674  ASP B C   1 
ATOM   7964 O  O   . ASP B 1 674 ? -3.645  28.718  -23.642 1.00 25.45 ? 674  ASP B O   1 
ATOM   7965 C  CB  . ASP B 1 674 ? -6.178  30.247  -21.712 1.00 29.93 ? 674  ASP B CB  1 
ATOM   7966 C  CG  . ASP B 1 674 ? -7.148  29.782  -22.798 1.00 30.02 ? 674  ASP B CG  1 
ATOM   7967 O  OD1 . ASP B 1 674 ? -6.751  29.084  -23.756 1.00 29.57 ? 674  ASP B OD1 1 
ATOM   7968 O  OD2 . ASP B 1 674 ? -8.329  30.134  -22.681 1.00 32.21 ? 674  ASP B OD2 1 
ATOM   7969 N  N   . LEU B 1 675 ? -4.345  27.968  -21.638 1.00 28.77 ? 675  LEU B N   1 
ATOM   7970 C  CA  . LEU B 1 675 ? -3.752  26.657  -21.845 1.00 32.21 ? 675  LEU B CA  1 
ATOM   7971 C  C   . LEU B 1 675 ? -4.178  26.078  -23.184 1.00 30.56 ? 675  LEU B C   1 
ATOM   7972 O  O   . LEU B 1 675 ? -3.368  25.472  -23.876 1.00 31.51 ? 675  LEU B O   1 
ATOM   7973 C  CB  . LEU B 1 675 ? -4.099  25.695  -20.705 1.00 34.60 ? 675  LEU B CB  1 
ATOM   7974 C  CG  . LEU B 1 675 ? -3.428  24.314  -20.780 1.00 37.23 ? 675  LEU B CG  1 
ATOM   7975 C  CD1 . LEU B 1 675 ? -1.948  24.355  -21.180 1.00 36.97 ? 675  LEU B CD1 1 
ATOM   7976 C  CD2 . LEU B 1 675 ? -3.602  23.599  -19.447 1.00 38.71 ? 675  LEU B CD2 1 
ATOM   7977 N  N   . ASP B 1 676 ? -5.425  26.318  -23.571 1.00 28.83 ? 676  ASP B N   1 
ATOM   7978 C  CA  . ASP B 1 676 ? -5.924  25.811  -24.841 1.00 30.04 ? 676  ASP B CA  1 
ATOM   7979 C  C   . ASP B 1 676 ? -5.354  26.551  -26.058 1.00 27.31 ? 676  ASP B C   1 
ATOM   7980 O  O   . ASP B 1 676 ? -4.785  25.941  -26.941 1.00 25.57 ? 676  ASP B O   1 
ATOM   7981 C  CB  . ASP B 1 676 ? -7.454  25.881  -24.881 1.00 32.88 ? 676  ASP B CB  1 
ATOM   7982 C  CG  . ASP B 1 676 ? -8.024  25.183  -26.099 1.00 35.49 ? 676  ASP B CG  1 
ATOM   7983 O  OD1 . ASP B 1 676 ? -7.796  23.961  -26.247 1.00 38.51 ? 676  ASP B OD1 1 
ATOM   7984 O  OD2 . ASP B 1 676 ? -8.679  25.854  -26.920 1.00 38.86 ? 676  ASP B OD2 1 
ATOM   7985 N  N   . SER B 1 677 ? -5.536  27.869  -26.110 1.00 26.08 ? 677  SER B N   1 
ATOM   7986 C  CA  . SER B 1 677 ? -5.077  28.660  -27.255 1.00 25.04 ? 677  SER B CA  1 
ATOM   7987 C  C   . SER B 1 677 ? -3.537  28.770  -27.344 1.00 24.22 ? 677  SER B C   1 
ATOM   7988 O  O   . SER B 1 677 ? -3.017  29.206  -28.371 1.00 23.35 ? 677  SER B O   1 
ATOM   7989 C  CB  . SER B 1 677 ? -5.684  30.066  -27.201 1.00 24.96 ? 677  SER B CB  1 
ATOM   7990 O  OG  . SER B 1 677 ? -5.318  30.713  -25.990 1.00 25.59 ? 677  SER B OG  1 
ATOM   7991 N  N   . ALA B 1 678 ? -2.818  28.381  -26.292 1.00 22.65 ? 678  ALA B N   1 
ATOM   7992 C  CA  . ALA B 1 678 ? -1.347  28.375  -26.342 1.00 22.82 ? 678  ALA B CA  1 
ATOM   7993 C  C   . ALA B 1 678 ? -0.752  27.369  -27.349 1.00 22.49 ? 678  ALA B C   1 
ATOM   7994 O  O   . ALA B 1 678 ? 0.391   27.521  -27.768 1.00 21.26 ? 678  ALA B O   1 
ATOM   7995 C  CB  . ALA B 1 678 ? -0.766  28.156  -24.959 1.00 23.00 ? 678  ALA B CB  1 
ATOM   7996 N  N   . ALA B 1 679 ? -1.527  26.356  -27.728 1.00 21.63 ? 679  ALA B N   1 
ATOM   7997 C  CA  . ALA B 1 679 ? -1.108  25.363  -28.712 1.00 22.69 ? 679  ALA B CA  1 
ATOM   7998 C  C   . ALA B 1 679 ? -1.766  25.643  -30.051 1.00 23.49 ? 679  ALA B C   1 
ATOM   7999 O  O   . ALA B 1 679 ? -2.940  25.984  -30.078 1.00 22.86 ? 679  ALA B O   1 
ATOM   8000 C  CB  . ALA B 1 679 ? -1.546  23.981  -28.257 1.00 22.90 ? 679  ALA B CB  1 
ATOM   8001 N  N   . LEU B 1 680 ? -1.035  25.476  -31.152 1.00 24.12 ? 680  LEU B N   1 
ATOM   8002 C  CA  . LEU B 1 680 ? -1.679  25.372  -32.456 1.00 24.47 ? 680  LEU B CA  1 
ATOM   8003 C  C   . LEU B 1 680 ? -2.351  24.007  -32.591 1.00 26.76 ? 680  LEU B C   1 
ATOM   8004 O  O   . LEU B 1 680 ? -1.927  23.029  -31.954 1.00 24.34 ? 680  LEU B O   1 
ATOM   8005 C  CB  . LEU B 1 680 ? -0.676  25.534  -33.587 1.00 24.47 ? 680  LEU B CB  1 
ATOM   8006 C  CG  . LEU B 1 680 ? 0.058   26.866  -33.667 1.00 24.38 ? 680  LEU B CG  1 
ATOM   8007 C  CD1 . LEU B 1 680 ? 1.223   26.737  -34.624 1.00 25.51 ? 680  LEU B CD1 1 
ATOM   8008 C  CD2 . LEU B 1 680 ? -0.883  27.993  -34.067 1.00 24.06 ? 680  LEU B CD2 1 
ATOM   8009 N  N   . PRO B 1 681 ? -3.397  23.931  -33.436 1.00 30.37 ? 681  PRO B N   1 
ATOM   8010 C  CA  . PRO B 1 681 ? -4.009  22.648  -33.782 1.00 31.11 ? 681  PRO B CA  1 
ATOM   8011 C  C   . PRO B 1 681 ? -2.965  21.593  -34.135 1.00 32.50 ? 681  PRO B C   1 
ATOM   8012 O  O   . PRO B 1 681 ? -2.047  21.861  -34.915 1.00 35.57 ? 681  PRO B O   1 
ATOM   8013 C  CB  . PRO B 1 681 ? -4.867  22.988  -35.012 1.00 31.81 ? 681  PRO B CB  1 
ATOM   8014 C  CG  . PRO B 1 681 ? -5.197  24.429  -34.865 1.00 31.78 ? 681  PRO B CG  1 
ATOM   8015 C  CD  . PRO B 1 681 ? -4.032  25.060  -34.151 1.00 31.27 ? 681  PRO B CD  1 
ATOM   8016 N  N   . GLY B 1 682 ? -3.089  20.412  -33.540 1.00 32.33 ? 682  GLY B N   1 
ATOM   8017 C  CA  . GLY B 1 682 ? -2.155  19.319  -33.768 1.00 31.12 ? 682  GLY B CA  1 
ATOM   8018 C  C   . GLY B 1 682 ? -0.975  19.282  -32.803 1.00 31.55 ? 682  GLY B C   1 
ATOM   8019 O  O   . GLY B 1 682 ? -0.367  18.231  -32.613 1.00 30.16 ? 682  GLY B O   1 
ATOM   8020 N  N   . GLU B 1 683 ? -0.638  20.408  -32.171 1.00 29.50 ? 683  GLU B N   1 
ATOM   8021 C  CA  . GLU B 1 683 ? 0.562   20.414  -31.329 1.00 29.24 ? 683  GLU B CA  1 
ATOM   8022 C  C   . GLU B 1 683 ? 0.438   19.494  -30.128 1.00 30.03 ? 683  GLU B C   1 
ATOM   8023 O  O   . GLU B 1 683 ? 1.412   18.844  -29.758 1.00 29.45 ? 683  GLU B O   1 
ATOM   8024 C  CB  . GLU B 1 683 ? 0.951   21.824  -30.891 1.00 26.82 ? 683  GLU B CB  1 
ATOM   8025 C  CG  . GLU B 1 683 ? 1.537   22.652  -32.021 1.00 24.90 ? 683  GLU B CG  1 
ATOM   8026 C  CD  . GLU B 1 683 ? 2.144   23.939  -31.512 1.00 24.35 ? 683  GLU B CD  1 
ATOM   8027 O  OE1 . GLU B 1 683 ? 1.444   24.676  -30.789 1.00 25.09 ? 683  GLU B OE1 1 
ATOM   8028 O  OE2 . GLU B 1 683 ? 3.311   24.214  -31.833 1.00 21.50 ? 683  GLU B OE2 1 
ATOM   8029 N  N   . ARG B 1 684 ? -0.755  19.406  -29.546 1.00 32.93 ? 684  ARG B N   1 
ATOM   8030 C  CA  . ARG B 1 684 ? -0.959  18.553  -28.373 1.00 35.61 ? 684  ARG B CA  1 
ATOM   8031 C  C   . ARG B 1 684 ? -0.823  17.061  -28.687 1.00 35.47 ? 684  ARG B C   1 
ATOM   8032 O  O   . ARG B 1 684 ? -0.590  16.263  -27.782 1.00 36.63 ? 684  ARG B O   1 
ATOM   8033 C  CB  . ARG B 1 684 ? -2.323  18.812  -27.741 1.00 37.78 ? 684  ARG B CB  1 
ATOM   8034 C  CG  . ARG B 1 684 ? -2.522  20.236  -27.269 1.00 40.48 ? 684  ARG B CG  1 
ATOM   8035 C  CD  . ARG B 1 684 ? -3.749  20.363  -26.383 1.00 42.42 ? 684  ARG B CD  1 
ATOM   8036 N  NE  . ARG B 1 684 ? -3.351  20.494  -24.986 1.00 44.43 ? 684  ARG B NE  1 
ATOM   8037 C  CZ  . ARG B 1 684 ? -3.234  21.646  -24.324 1.00 45.51 ? 684  ARG B CZ  1 
ATOM   8038 N  NH1 . ARG B 1 684 ? -3.508  22.813  -24.907 1.00 43.89 ? 684  ARG B NH1 1 
ATOM   8039 N  NH2 . ARG B 1 684 ? -2.850  21.626  -23.053 1.00 46.19 ? 684  ARG B NH2 1 
ATOM   8040 N  N   . ASP B 1 685 ? -0.971  16.691  -29.954 1.00 36.08 ? 685  ASP B N   1 
ATOM   8041 C  CA  . ASP B 1 685 ? -0.817  15.300  -30.389 1.00 38.53 ? 685  ASP B CA  1 
ATOM   8042 C  C   . ASP B 1 685 ? 0.590   14.996  -30.938 1.00 37.74 ? 685  ASP B C   1 
ATOM   8043 O  O   . ASP B 1 685 ? 0.945   13.835  -31.115 1.00 37.00 ? 685  ASP B O   1 
ATOM   8044 C  CB  . ASP B 1 685 ? -1.891  14.958  -31.443 1.00 40.85 ? 685  ASP B CB  1 
ATOM   8045 C  CG  . ASP B 1 685 ? -3.315  14.992  -30.873 1.00 44.08 ? 685  ASP B CG  1 
ATOM   8046 O  OD1 . ASP B 1 685 ? -3.501  14.737  -29.664 1.00 49.35 ? 685  ASP B OD1 1 
ATOM   8047 O  OD2 . ASP B 1 685 ? -4.257  15.280  -31.636 1.00 48.33 ? 685  ASP B OD2 1 
ATOM   8048 N  N   . LYS B 1 686 ? 1.374   16.041  -31.210 1.00 36.40 ? 686  LYS B N   1 
ATOM   8049 C  CA  . LYS B 1 686 ? 2.772   15.921  -31.660 1.00 34.04 ? 686  LYS B CA  1 
ATOM   8050 C  C   . LYS B 1 686 ? 3.562   15.028  -30.695 1.00 30.76 ? 686  LYS B C   1 
ATOM   8051 O  O   . LYS B 1 686 ? 3.408   15.143  -29.489 1.00 26.94 ? 686  LYS B O   1 
ATOM   8052 C  CB  . LYS B 1 686 ? 3.408   17.323  -31.694 1.00 35.52 ? 686  LYS B CB  1 
ATOM   8053 C  CG  . LYS B 1 686 ? 4.394   17.589  -32.813 1.00 37.41 ? 686  LYS B CG  1 
ATOM   8054 C  CD  . LYS B 1 686 ? 4.414   19.067  -33.219 1.00 37.79 ? 686  LYS B CD  1 
ATOM   8055 C  CE  . LYS B 1 686 ? 4.735   19.996  -32.043 1.00 39.83 ? 686  LYS B CE  1 
ATOM   8056 N  NZ  . LYS B 1 686 ? 5.020   21.428  -32.430 1.00 38.63 ? 686  LYS B NZ  1 
ATOM   8057 N  N   . PRO B 1 687 ? 4.408   14.129  -31.218 1.00 29.42 ? 687  PRO B N   1 
ATOM   8058 C  CA  . PRO B 1 687 ? 5.264   13.420  -30.272 1.00 28.04 ? 687  PRO B CA  1 
ATOM   8059 C  C   . PRO B 1 687 ? 6.205   14.386  -29.543 1.00 27.66 ? 687  PRO B C   1 
ATOM   8060 O  O   . PRO B 1 687 ? 6.488   15.484  -30.036 1.00 26.22 ? 687  PRO B O   1 
ATOM   8061 C  CB  . PRO B 1 687 ? 6.054   12.438  -31.153 1.00 28.14 ? 687  PRO B CB  1 
ATOM   8062 C  CG  . PRO B 1 687 ? 5.923   12.944  -32.543 1.00 30.10 ? 687  PRO B CG  1 
ATOM   8063 C  CD  . PRO B 1 687 ? 4.619   13.696  -32.610 1.00 29.70 ? 687  PRO B CD  1 
ATOM   8064 N  N   . VAL B 1 688 ? 6.656   13.984  -28.359 1.00 26.41 ? 688  VAL B N   1 
ATOM   8065 C  CA  . VAL B 1 688 ? 7.711   14.711  -27.645 1.00 25.34 ? 688  VAL B CA  1 
ATOM   8066 C  C   . VAL B 1 688 ? 9.014   14.747  -28.464 1.00 23.66 ? 688  VAL B C   1 
ATOM   8067 O  O   . VAL B 1 688 ? 9.410   13.747  -29.044 1.00 22.88 ? 688  VAL B O   1 
ATOM   8068 C  CB  . VAL B 1 688 ? 8.000   14.079  -26.266 1.00 25.72 ? 688  VAL B CB  1 
ATOM   8069 C  CG1 . VAL B 1 688 ? 9.175   14.784  -25.584 1.00 26.05 ? 688  VAL B CG1 1 
ATOM   8070 C  CG2 . VAL B 1 688 ? 6.757   14.139  -25.389 1.00 25.93 ? 688  VAL B CG2 1 
ATOM   8071 N  N   . ASP B 1 689 ? 9.664   15.907  -28.524 1.00 22.76 ? 689  ASP B N   1 
ATOM   8072 C  CA  . ASP B 1 689 ? 11.023  16.007  -29.087 1.00 22.26 ? 689  ASP B CA  1 
ATOM   8073 C  C   . ASP B 1 689 ? 12.003  15.835  -27.931 1.00 21.60 ? 689  ASP B C   1 
ATOM   8074 O  O   . ASP B 1 689 ? 12.352  16.792  -27.236 1.00 22.30 ? 689  ASP B O   1 
ATOM   8075 C  CB  . ASP B 1 689 ? 11.211  17.361  -29.802 1.00 22.74 ? 689  ASP B CB  1 
ATOM   8076 C  CG  . ASP B 1 689 ? 12.559  17.495  -30.496 1.00 22.76 ? 689  ASP B CG  1 
ATOM   8077 O  OD1 . ASP B 1 689 ? 13.554  16.887  -30.056 1.00 21.82 ? 689  ASP B OD1 1 
ATOM   8078 O  OD2 . ASP B 1 689 ? 12.620  18.254  -31.484 1.00 22.71 ? 689  ASP B OD2 1 
ATOM   8079 N  N   . TRP B 1 690 ? 12.444  14.599  -27.722 1.00 21.26 ? 690  TRP B N   1 
ATOM   8080 C  CA  . TRP B 1 690 ? 13.252  14.261  -26.548 1.00 20.57 ? 690  TRP B CA  1 
ATOM   8081 C  C   . TRP B 1 690 ? 14.652  14.876  -26.600 1.00 19.90 ? 690  TRP B C   1 
ATOM   8082 O  O   . TRP B 1 690 ? 15.156  15.298  -25.564 1.00 20.69 ? 690  TRP B O   1 
ATOM   8083 C  CB  . TRP B 1 690 ? 13.344  12.743  -26.344 1.00 20.44 ? 690  TRP B CB  1 
ATOM   8084 C  CG  . TRP B 1 690 ? 12.040  12.108  -26.001 1.00 21.03 ? 690  TRP B CG  1 
ATOM   8085 C  CD1 . TRP B 1 690 ? 11.267  11.335  -26.820 1.00 20.57 ? 690  TRP B CD1 1 
ATOM   8086 C  CD2 . TRP B 1 690 ? 11.347  12.177  -24.746 1.00 21.17 ? 690  TRP B CD2 1 
ATOM   8087 N  NE1 . TRP B 1 690 ? 10.147  10.928  -26.158 1.00 21.15 ? 690  TRP B NE1 1 
ATOM   8088 C  CE2 . TRP B 1 690 ? 10.164  11.432  -24.886 1.00 20.89 ? 690  TRP B CE2 1 
ATOM   8089 C  CE3 . TRP B 1 690 ? 11.605  12.813  -23.527 1.00 21.36 ? 690  TRP B CE3 1 
ATOM   8090 C  CZ2 . TRP B 1 690 ? 9.245   11.289  -23.853 1.00 21.73 ? 690  TRP B CZ2 1 
ATOM   8091 C  CZ3 . TRP B 1 690 ? 10.691  12.677  -22.499 1.00 21.02 ? 690  TRP B CZ3 1 
ATOM   8092 C  CH2 . TRP B 1 690 ? 9.520   11.929  -22.670 1.00 21.97 ? 690  TRP B CH2 1 
ATOM   8093 N  N   . ASP B 1 691 ? 15.265  14.946  -27.784 1.00 19.58 ? 691  ASP B N   1 
ATOM   8094 C  CA  . ASP B 1 691 ? 16.566  15.620  -27.951 1.00 20.51 ? 691  ASP B CA  1 
ATOM   8095 C  C   . ASP B 1 691 ? 16.491  17.087  -27.523 1.00 20.77 ? 691  ASP B C   1 
ATOM   8096 O  O   . ASP B 1 691 ? 17.411  17.596  -26.889 1.00 19.90 ? 691  ASP B O   1 
ATOM   8097 C  CB  . ASP B 1 691 ? 17.067  15.576  -29.408 1.00 21.52 ? 691  ASP B CB  1 
ATOM   8098 C  CG  . ASP B 1 691 ? 17.483  14.171  -29.848 1.00 22.69 ? 691  ASP B CG  1 
ATOM   8099 O  OD1 . ASP B 1 691 ? 17.228  13.205  -29.112 1.00 22.55 ? 691  ASP B OD1 1 
ATOM   8100 O  OD2 . ASP B 1 691 ? 18.046  14.020  -30.948 1.00 25.40 ? 691  ASP B OD2 1 
ATOM   8101 N  N   . LEU B 1 692 ? 15.411  17.759  -27.908 1.00 20.26 ? 692  LEU B N   1 
ATOM   8102 C  CA  . LEU B 1 692 ? 15.232  19.158  -27.573 1.00 20.33 ? 692  LEU B CA  1 
ATOM   8103 C  C   . LEU B 1 692 ? 15.265  19.379  -26.057 1.00 21.50 ? 692  LEU B C   1 
ATOM   8104 O  O   . LEU B 1 692 ? 15.908  20.306  -25.608 1.00 22.36 ? 692  LEU B O   1 
ATOM   8105 C  CB  . LEU B 1 692 ? 13.943  19.689  -28.181 1.00 20.17 ? 692  LEU B CB  1 
ATOM   8106 C  CG  . LEU B 1 692 ? 13.543  21.141  -27.898 1.00 20.75 ? 692  LEU B CG  1 
ATOM   8107 C  CD1 . LEU B 1 692 ? 14.658  22.118  -28.280 1.00 21.52 ? 692  LEU B CD1 1 
ATOM   8108 C  CD2 . LEU B 1 692 ? 12.264  21.440  -28.648 1.00 20.39 ? 692  LEU B CD2 1 
ATOM   8109 N  N   . ILE B 1 693 ? 14.642  18.502  -25.273 1.00 21.13 ? 693  ILE B N   1 
ATOM   8110 C  CA  . ILE B 1 693 ? 14.511  18.736  -23.831 1.00 21.36 ? 693  ILE B CA  1 
ATOM   8111 C  C   . ILE B 1 693 ? 15.495  17.971  -22.936 1.00 22.17 ? 693  ILE B C   1 
ATOM   8112 O  O   . ILE B 1 693 ? 15.584  18.262  -21.738 1.00 22.81 ? 693  ILE B O   1 
ATOM   8113 C  CB  . ILE B 1 693 ? 13.058  18.513  -23.344 1.00 21.16 ? 693  ILE B CB  1 
ATOM   8114 C  CG1 . ILE B 1 693 ? 12.653  17.045  -23.448 1.00 21.53 ? 693  ILE B CG1 1 
ATOM   8115 C  CG2 . ILE B 1 693 ? 12.103  19.383  -24.148 1.00 21.52 ? 693  ILE B CG2 1 
ATOM   8116 C  CD1 . ILE B 1 693 ? 11.191  16.815  -23.161 1.00 22.02 ? 693  ILE B CD1 1 
ATOM   8117 N  N   . GLY B 1 694 ? 16.245  17.028  -23.508 1.00 23.47 ? 694  GLY B N   1 
ATOM   8118 C  CA  . GLY B 1 694 ? 17.266  16.264  -22.778 1.00 25.87 ? 694  GLY B CA  1 
ATOM   8119 C  C   . GLY B 1 694 ? 18.700  16.814  -22.800 1.00 28.79 ? 694  GLY B C   1 
ATOM   8120 O  O   . GLY B 1 694 ? 19.126  17.473  -23.755 1.00 31.75 ? 694  GLY B O   1 
HETATM 8121 C  C1  . FRU C 2 .   ? 15.821  -10.917 -15.100 1.00 36.21 ? 801  FRU A C1  1 
HETATM 8122 C  C2  . FRU C 2 .   ? 17.325  -11.198 -14.939 1.00 35.13 ? 801  FRU A C2  1 
HETATM 8123 C  C3  . FRU C 2 .   ? 17.823  -12.530 -15.539 1.00 33.90 ? 801  FRU A C3  1 
HETATM 8124 C  C4  . FRU C 2 .   ? 18.971  -12.916 -14.608 1.00 33.51 ? 801  FRU A C4  1 
HETATM 8125 C  C5  . FRU C 2 .   ? 18.658  -12.234 -13.270 1.00 34.82 ? 801  FRU A C5  1 
HETATM 8126 C  C6  . FRU C 2 .   ? 19.864  -11.556 -12.608 1.00 35.63 ? 801  FRU A C6  1 
HETATM 8127 O  O1  . FRU C 2 .   ? 15.310  -10.228 -13.931 1.00 36.24 ? 801  FRU A O1  1 
HETATM 8128 O  O2  . FRU C 2 .   ? 18.062  -10.092 -15.499 1.00 36.73 ? 801  FRU A O2  1 
HETATM 8129 O  O3  . FRU C 2 .   ? 18.295  -12.453 -16.898 1.00 30.30 ? 801  FRU A O3  1 
HETATM 8130 O  O4  . FRU C 2 .   ? 19.083  -14.329 -14.467 1.00 31.01 ? 801  FRU A O4  1 
HETATM 8131 O  O5  . FRU C 2 .   ? 17.647  -11.256 -13.537 1.00 34.00 ? 801  FRU A O5  1 
HETATM 8132 O  O6  . FRU C 2 .   ? 19.516  -11.001 -11.324 1.00 35.51 ? 801  FRU A O6  1 
HETATM 8133 CA CA  . CA  D 3 .   ? 26.344  -6.114  -27.314 1.00 18.99 ? 802  CA  A CA  1 
HETATM 8134 CA CA  . CA  E 3 .   ? -2.999  -23.954 -8.485  1.00 23.22 ? 803  CA  A CA  1 
HETATM 8135 C  C1  . FRU F 2 .   ? 21.189  31.513  -24.981 1.00 41.41 ? 801  FRU B C1  1 
HETATM 8136 C  C2  . FRU F 2 .   ? 22.622  31.363  -25.509 1.00 38.46 ? 801  FRU B C2  1 
HETATM 8137 C  C3  . FRU F 2 .   ? 23.559  32.484  -25.054 1.00 35.67 ? 801  FRU B C3  1 
HETATM 8138 C  C4  . FRU F 2 .   ? 24.544  32.598  -26.215 1.00 35.49 ? 801  FRU B C4  1 
HETATM 8139 C  C5  . FRU F 2 .   ? 23.750  32.159  -27.457 1.00 36.43 ? 801  FRU B C5  1 
HETATM 8140 C  C6  . FRU F 2 .   ? 24.519  31.356  -28.522 1.00 36.24 ? 801  FRU B C6  1 
HETATM 8141 O  O1  . FRU F 2 .   ? 20.215  31.283  -26.016 1.00 42.54 ? 801  FRU B O1  1 
HETATM 8142 O  O2  . FRU F 2 .   ? 23.136  30.086  -25.085 1.00 40.15 ? 801  FRU B O2  1 
HETATM 8143 O  O3  . FRU F 2 .   ? 24.226  32.257  -23.801 1.00 32.33 ? 801  FRU B O3  1 
HETATM 8144 O  O4  . FRU F 2 .   ? 25.012  33.951  -26.279 1.00 32.22 ? 801  FRU B O4  1 
HETATM 8145 O  O5  . FRU F 2 .   ? 22.644  31.387  -26.950 1.00 37.35 ? 801  FRU B O5  1 
HETATM 8146 O  O6  . FRU F 2 .   ? 23.678  30.932  -29.628 1.00 33.50 ? 801  FRU B O6  1 
HETATM 8147 CA CA  . CA  G 3 .   ? 5.853   49.733  -26.948 1.00 17.15 ? 802  CA  B CA  1 
HETATM 8148 CA CA  . CA  H 3 .   ? 32.442  23.405  -15.681 1.00 17.76 ? 803  CA  B CA  1 
HETATM 8149 O  O   . HOH I 4 .   ? 26.279  10.336  -42.920 1.00 34.61 ? 901  HOH A O   1 
HETATM 8150 O  O   . HOH I 4 .   ? 21.400  -9.591  -10.642 1.00 41.62 ? 902  HOH A O   1 
HETATM 8151 O  O   . HOH I 4 .   ? 25.496  3.027   -25.634 1.00 33.65 ? 903  HOH A O   1 
HETATM 8152 O  O   . HOH I 4 .   ? 5.944   11.326  -27.296 1.00 22.14 ? 904  HOH A O   1 
HETATM 8153 O  O   . HOH I 4 .   ? 10.125  -10.574 1.548   1.00 24.49 ? 905  HOH A O   1 
HETATM 8154 O  O   . HOH I 4 .   ? 3.044   -5.140  -32.251 1.00 22.23 ? 906  HOH A O   1 
HETATM 8155 O  O   . HOH I 4 .   ? 24.612  -2.395  -25.128 1.00 31.16 ? 907  HOH A O   1 
HETATM 8156 O  O   . HOH I 4 .   ? 3.758   -29.321 -23.327 1.00 23.56 ? 908  HOH A O   1 
HETATM 8157 O  O   . HOH I 4 .   ? 20.869  -14.564 -1.235  1.00 26.14 ? 909  HOH A O   1 
HETATM 8158 O  O   . HOH I 4 .   ? 0.642   -1.698  -22.296 1.00 15.13 ? 910  HOH A O   1 
HETATM 8159 O  O   . HOH I 4 .   ? -4.842  -20.061 -7.010  1.00 21.83 ? 911  HOH A O   1 
HETATM 8160 O  O   . HOH I 4 .   ? 0.611   -0.887  -6.817  1.00 26.79 ? 912  HOH A O   1 
HETATM 8161 O  O   . HOH I 4 .   ? 8.692   -3.824  -14.185 1.00 21.42 ? 913  HOH A O   1 
HETATM 8162 O  O   . HOH I 4 .   ? 34.650  -11.210 -13.165 1.00 21.34 ? 914  HOH A O   1 
HETATM 8163 O  O   . HOH I 4 .   ? 17.013  -35.197 -16.903 1.00 32.22 ? 915  HOH A O   1 
HETATM 8164 O  O   . HOH I 4 .   ? -1.308  -11.715 -25.740 1.00 14.09 ? 916  HOH A O   1 
HETATM 8165 O  O   . HOH I 4 .   ? 19.399  -19.987 -36.228 1.00 37.36 ? 917  HOH A O   1 
HETATM 8166 O  O   . HOH I 4 .   ? 13.266  -5.467  -10.089 1.00 22.14 ? 918  HOH A O   1 
HETATM 8167 O  O   . HOH I 4 .   ? 15.073  -4.703  -25.391 1.00 17.19 ? 919  HOH A O   1 
HETATM 8168 O  O   . HOH I 4 .   ? 5.349   -2.649  -14.725 1.00 27.46 ? 920  HOH A O   1 
HETATM 8169 O  O   . HOH I 4 .   ? 30.070  -28.586 -22.062 1.00 23.85 ? 921  HOH A O   1 
HETATM 8170 O  O   . HOH I 4 .   ? 30.009  -23.573 -10.142 1.00 24.92 ? 922  HOH A O   1 
HETATM 8171 O  O   . HOH I 4 .   ? 25.727  -31.666 -13.641 1.00 33.08 ? 923  HOH A O   1 
HETATM 8172 O  O   . HOH I 4 .   ? 12.219  5.115   -36.898 1.00 23.28 ? 924  HOH A O   1 
HETATM 8173 O  O   . HOH I 4 .   ? 15.430  -19.114 -19.309 1.00 21.30 ? 925  HOH A O   1 
HETATM 8174 O  O   . HOH I 4 .   ? -5.644  -12.912 -35.743 1.00 16.65 ? 926  HOH A O   1 
HETATM 8175 O  O   . HOH I 4 .   ? 29.149  4.173   -33.437 1.00 22.55 ? 927  HOH A O   1 
HETATM 8176 O  O   . HOH I 4 .   ? 23.551  -19.282 -39.541 1.00 33.57 ? 928  HOH A O   1 
HETATM 8177 O  O   . HOH I 4 .   ? 21.353  -35.973 -31.784 1.00 24.22 ? 929  HOH A O   1 
HETATM 8178 O  O   . HOH I 4 .   ? 32.641  -4.929  -25.406 1.00 25.50 ? 930  HOH A O   1 
HETATM 8179 O  O   . HOH I 4 .   ? 24.023  1.675   -50.381 1.00 32.05 ? 931  HOH A O   1 
HETATM 8180 O  O   . HOH I 4 .   ? 33.161  -16.523 -22.151 1.00 25.95 ? 932  HOH A O   1 
HETATM 8181 O  O   . HOH I 4 .   ? 23.553  -35.250 -28.021 1.00 27.77 ? 933  HOH A O   1 
HETATM 8182 O  O   . HOH I 4 .   ? -5.138  -7.584  -20.344 1.00 20.35 ? 934  HOH A O   1 
HETATM 8183 O  O   . HOH I 4 .   ? 9.930   -14.895 -12.532 1.00 41.40 ? 935  HOH A O   1 
HETATM 8184 O  O   . HOH I 4 .   ? 17.809  -36.190 -33.790 1.00 29.36 ? 936  HOH A O   1 
HETATM 8185 O  O   . HOH I 4 .   ? 27.486  -11.474 -24.003 1.00 19.34 ? 937  HOH A O   1 
HETATM 8186 O  O   . HOH I 4 .   ? 23.482  -8.023  -18.168 1.00 24.78 ? 938  HOH A O   1 
HETATM 8187 O  O   . HOH I 4 .   ? 10.771  4.722   -6.215  1.00 33.88 ? 939  HOH A O   1 
HETATM 8188 O  O   . HOH I 4 .   ? 30.475  -10.465 -37.671 1.00 21.47 ? 940  HOH A O   1 
HETATM 8189 O  O   . HOH I 4 .   ? 1.786   -30.112 -21.835 1.00 40.91 ? 941  HOH A O   1 
HETATM 8190 O  O   . HOH I 4 .   ? -4.515  -24.642 -1.664  1.00 29.42 ? 942  HOH A O   1 
HETATM 8191 O  O   . HOH I 4 .   ? 1.468   -23.508 -7.208  1.00 19.10 ? 943  HOH A O   1 
HETATM 8192 O  O   . HOH I 4 .   ? 26.889  -7.841  -25.828 1.00 16.03 ? 944  HOH A O   1 
HETATM 8193 O  O   . HOH I 4 .   ? 27.142  -14.037 -25.025 1.00 17.65 ? 945  HOH A O   1 
HETATM 8194 O  O   . HOH I 4 .   ? 22.279  -8.343  -39.145 1.00 23.30 ? 946  HOH A O   1 
HETATM 8195 O  O   . HOH I 4 .   ? 30.275  -25.888 -6.630  1.00 32.34 ? 947  HOH A O   1 
HETATM 8196 O  O   . HOH I 4 .   ? 7.756   -29.250 -9.163  1.00 23.11 ? 948  HOH A O   1 
HETATM 8197 O  O   . HOH I 4 .   ? 10.334  9.176   -21.065 1.00 30.54 ? 949  HOH A O   1 
HETATM 8198 O  O   . HOH I 4 .   ? 27.338  7.760   -42.355 1.00 32.76 ? 950  HOH A O   1 
HETATM 8199 O  O   . HOH I 4 .   ? 30.277  -14.400 -19.724 1.00 26.94 ? 951  HOH A O   1 
HETATM 8200 O  O   . HOH I 4 .   ? 9.973   -15.907 -20.378 1.00 19.71 ? 952  HOH A O   1 
HETATM 8201 O  O   . HOH I 4 .   ? 23.131  -1.582  -27.252 1.00 17.79 ? 953  HOH A O   1 
HETATM 8202 O  O   . HOH I 4 .   ? 20.883  -10.590 -24.004 1.00 19.89 ? 954  HOH A O   1 
HETATM 8203 O  O   . HOH I 4 .   ? -0.265  -19.758 -4.918  1.00 25.45 ? 955  HOH A O   1 
HETATM 8204 O  O   . HOH I 4 .   ? 4.245   -33.961 -17.952 1.00 30.63 ? 956  HOH A O   1 
HETATM 8205 O  O   . HOH I 4 .   ? 10.652  -10.738 -35.460 1.00 33.84 ? 957  HOH A O   1 
HETATM 8206 O  O   . HOH I 4 .   ? 2.113   -5.403  -13.595 1.00 17.52 ? 958  HOH A O   1 
HETATM 8207 O  O   . HOH I 4 .   ? 23.063  -9.263  -24.874 1.00 20.75 ? 959  HOH A O   1 
HETATM 8208 O  O   . HOH I 4 .   ? 24.637  0.548   -25.240 1.00 32.79 ? 960  HOH A O   1 
HETATM 8209 O  O   . HOH I 4 .   ? -2.105  0.438   -18.661 1.00 29.45 ? 961  HOH A O   1 
HETATM 8210 O  O   . HOH I 4 .   ? 7.513   -17.262 -20.877 1.00 17.39 ? 962  HOH A O   1 
HETATM 8211 O  O   . HOH I 4 .   ? 25.990  -11.518 -4.550  1.00 24.37 ? 963  HOH A O   1 
HETATM 8212 O  O   . HOH I 4 .   ? 16.225  6.753   -9.287  1.00 30.29 ? 964  HOH A O   1 
HETATM 8213 O  O   . HOH I 4 .   ? 32.299  -22.031 -32.894 1.00 26.17 ? 965  HOH A O   1 
HETATM 8214 O  O   . HOH I 4 .   ? 5.503   -18.945 1.822   1.00 29.72 ? 966  HOH A O   1 
HETATM 8215 O  O   . HOH I 4 .   ? 20.014  -13.051 -39.001 1.00 30.02 ? 967  HOH A O   1 
HETATM 8216 O  O   . HOH I 4 .   ? -1.073  -17.556 1.295   1.00 34.12 ? 968  HOH A O   1 
HETATM 8217 O  O   . HOH I 4 .   ? 0.966   -22.144 -4.834  1.00 29.19 ? 969  HOH A O   1 
HETATM 8218 O  O   . HOH I 4 .   ? 10.476  -9.705  -32.988 1.00 26.19 ? 970  HOH A O   1 
HETATM 8219 O  O   . HOH I 4 .   ? -0.526  -4.824  -14.030 1.00 20.12 ? 971  HOH A O   1 
HETATM 8220 O  O   . HOH I 4 .   ? 7.978   -23.318 -19.236 1.00 17.85 ? 972  HOH A O   1 
HETATM 8221 O  O   . HOH I 4 .   ? 19.268  -12.059 -25.441 1.00 25.08 ? 973  HOH A O   1 
HETATM 8222 O  O   . HOH I 4 .   ? 25.467  -15.418 -34.007 1.00 20.39 ? 974  HOH A O   1 
HETATM 8223 O  O   . HOH I 4 .   ? 14.108  -21.366 -18.157 1.00 20.42 ? 975  HOH A O   1 
HETATM 8224 O  O   . HOH I 4 .   ? 7.791   -1.792  -8.148  1.00 18.73 ? 976  HOH A O   1 
HETATM 8225 O  O   . HOH I 4 .   ? -0.756  -25.884 -21.917 1.00 16.38 ? 977  HOH A O   1 
HETATM 8226 O  O   . HOH I 4 .   ? 12.613  12.568  -29.977 1.00 25.68 ? 978  HOH A O   1 
HETATM 8227 O  O   . HOH I 4 .   ? 14.708  10.609  -39.149 1.00 26.05 ? 979  HOH A O   1 
HETATM 8228 O  O   . HOH I 4 .   ? 15.885  -6.582  -21.112 1.00 30.94 ? 980  HOH A O   1 
HETATM 8229 O  O   . HOH I 4 .   ? 10.356  -6.533  -39.688 1.00 25.04 ? 981  HOH A O   1 
HETATM 8230 O  O   . HOH I 4 .   ? 14.545  -4.175  -43.933 1.00 23.83 ? 982  HOH A O   1 
HETATM 8231 O  O   . HOH I 4 .   ? 20.986  -32.952 -18.563 1.00 25.45 ? 983  HOH A O   1 
HETATM 8232 O  O   . HOH I 4 .   ? 3.273   -15.894 -10.720 1.00 21.06 ? 984  HOH A O   1 
HETATM 8233 O  O   . HOH I 4 .   ? 21.294  -8.958  -4.913  1.00 24.56 ? 985  HOH A O   1 
HETATM 8234 O  O   . HOH I 4 .   ? 10.441  -26.833 -21.506 1.00 26.55 ? 986  HOH A O   1 
HETATM 8235 O  O   . HOH I 4 .   ? 13.013  0.468   -32.924 1.00 16.28 ? 987  HOH A O   1 
HETATM 8236 O  O   . HOH I 4 .   ? 14.701  -18.967 -35.767 1.00 17.16 ? 988  HOH A O   1 
HETATM 8237 O  O   . HOH I 4 .   ? -3.714  -26.128 -8.104  1.00 21.51 ? 989  HOH A O   1 
HETATM 8238 O  O   . HOH I 4 .   ? 17.877  -7.050  -35.706 1.00 15.49 ? 990  HOH A O   1 
HETATM 8239 O  O   . HOH I 4 .   ? 10.377  -2.229  -3.834  1.00 29.28 ? 991  HOH A O   1 
HETATM 8240 O  O   . HOH I 4 .   ? 18.602  2.178   -20.381 1.00 29.52 ? 992  HOH A O   1 
HETATM 8241 O  O   . HOH I 4 .   ? 17.060  -7.353  -4.654  1.00 28.18 ? 993  HOH A O   1 
HETATM 8242 O  O   . HOH I 4 .   ? 6.969   4.322   -43.306 1.00 33.49 ? 994  HOH A O   1 
HETATM 8243 O  O   . HOH I 4 .   ? 29.833  -14.700 -22.609 1.00 28.53 ? 995  HOH A O   1 
HETATM 8244 O  O   . HOH I 4 .   ? 11.806  -34.327 -16.395 1.00 21.27 ? 996  HOH A O   1 
HETATM 8245 O  O   . HOH I 4 .   ? 7.878   -16.361 -12.326 1.00 23.18 ? 997  HOH A O   1 
HETATM 8246 O  O   . HOH I 4 .   ? -0.843  -3.278  -25.161 1.00 21.93 ? 998  HOH A O   1 
HETATM 8247 O  O   . HOH I 4 .   ? 29.761  -6.757  -15.564 1.00 25.30 ? 999  HOH A O   1 
HETATM 8248 O  O   . HOH I 4 .   ? 25.421  -3.744  -33.443 1.00 12.70 ? 1000 HOH A O   1 
HETATM 8249 O  O   . HOH I 4 .   ? 14.249  5.890   -34.818 1.00 23.54 ? 1001 HOH A O   1 
HETATM 8250 O  O   . HOH I 4 .   ? 31.634  0.186   -24.563 1.00 27.16 ? 1002 HOH A O   1 
HETATM 8251 O  O   . HOH I 4 .   ? 15.668  -0.465  -30.991 1.00 16.52 ? 1003 HOH A O   1 
HETATM 8252 O  O   . HOH I 4 .   ? 26.900  -19.414 -3.234  1.00 37.09 ? 1004 HOH A O   1 
HETATM 8253 O  O   . HOH I 4 .   ? 29.412  -17.491 -3.007  1.00 22.03 ? 1005 HOH A O   1 
HETATM 8254 O  O   . HOH I 4 .   ? 12.322  7.487   -20.180 1.00 27.34 ? 1006 HOH A O   1 
HETATM 8255 O  O   . HOH I 4 .   ? 2.333   -1.705  -33.085 1.00 30.46 ? 1007 HOH A O   1 
HETATM 8256 O  O   . HOH I 4 .   ? -6.163  -2.343  -4.329  1.00 24.47 ? 1008 HOH A O   1 
HETATM 8257 O  O   . HOH I 4 .   ? 22.694  -20.804 -3.661  1.00 15.48 ? 1009 HOH A O   1 
HETATM 8258 O  O   . HOH I 4 .   ? 3.915   6.417   -9.566  1.00 47.49 ? 1010 HOH A O   1 
HETATM 8259 O  O   . HOH I 4 .   ? 15.716  -18.646 -16.569 1.00 17.78 ? 1011 HOH A O   1 
HETATM 8260 O  O   . HOH I 4 .   ? -1.951  -16.956 -1.417  1.00 29.60 ? 1012 HOH A O   1 
HETATM 8261 O  O   . HOH I 4 .   ? -1.137  -24.733 -7.319  1.00 24.07 ? 1013 HOH A O   1 
HETATM 8262 O  O   . HOH I 4 .   ? 9.500   -23.673 -37.949 1.00 27.34 ? 1014 HOH A O   1 
HETATM 8263 O  O   . HOH I 4 .   ? -4.210  -4.145  -17.783 1.00 25.92 ? 1015 HOH A O   1 
HETATM 8264 O  O   . HOH I 4 .   ? -1.628  -3.981  -11.708 1.00 20.00 ? 1016 HOH A O   1 
HETATM 8265 O  O   . HOH I 4 .   ? 31.975  -0.520  -34.455 1.00 22.15 ? 1017 HOH A O   1 
HETATM 8266 O  O   . HOH I 4 .   ? 10.572  -21.067 4.864   1.00 28.23 ? 1018 HOH A O   1 
HETATM 8267 O  O   . HOH I 4 .   ? 11.947  11.790  -9.326  1.00 24.70 ? 1019 HOH A O   1 
HETATM 8268 O  O   . HOH I 4 .   ? 19.621  -22.563 -35.068 1.00 41.06 ? 1020 HOH A O   1 
HETATM 8269 O  O   . HOH I 4 .   ? 12.699  -24.799 -15.064 1.00 22.12 ? 1021 HOH A O   1 
HETATM 8270 O  O   . HOH I 4 .   ? 9.744   4.591   -11.687 1.00 26.49 ? 1022 HOH A O   1 
HETATM 8271 O  O   . HOH I 4 .   ? 22.224  -20.348 -17.275 1.00 26.41 ? 1023 HOH A O   1 
HETATM 8272 O  O   . HOH I 4 .   ? 2.931   -3.832  -15.787 1.00 21.72 ? 1024 HOH A O   1 
HETATM 8273 O  O   . HOH I 4 .   ? -6.875  -6.189  -16.195 1.00 27.39 ? 1025 HOH A O   1 
HETATM 8274 O  O   . HOH I 4 .   ? 2.041   -13.295 -13.561 1.00 22.54 ? 1026 HOH A O   1 
HETATM 8275 O  O   . HOH I 4 .   ? 33.434  -26.982 -14.843 1.00 29.70 ? 1027 HOH A O   1 
HETATM 8276 O  O   . HOH I 4 .   ? 0.116   -24.466 -14.840 1.00 25.04 ? 1028 HOH A O   1 
HETATM 8277 O  O   . HOH I 4 .   ? 15.021  9.911   -27.366 1.00 21.95 ? 1029 HOH A O   1 
HETATM 8278 O  O   . HOH I 4 .   ? 8.488   -11.267 -0.684  1.00 24.70 ? 1030 HOH A O   1 
HETATM 8279 O  O   . HOH I 4 .   ? 16.274  -7.854  -15.251 1.00 42.08 ? 1031 HOH A O   1 
HETATM 8280 O  O   . HOH I 4 .   ? 8.178   3.368   -48.230 1.00 27.11 ? 1032 HOH A O   1 
HETATM 8281 O  O   . HOH I 4 .   ? 19.318  -8.583  -3.250  1.00 25.78 ? 1033 HOH A O   1 
HETATM 8282 O  O   . HOH I 4 .   ? 12.379  -1.482  -17.368 1.00 45.01 ? 1034 HOH A O   1 
HETATM 8283 O  O   . HOH I 4 .   ? 5.933   6.642   -11.234 1.00 35.30 ? 1035 HOH A O   1 
HETATM 8284 O  O   . HOH I 4 .   ? 0.750   -6.559  -32.737 1.00 29.15 ? 1036 HOH A O   1 
HETATM 8285 O  O   . HOH I 4 .   ? -3.886  -8.870  -6.969  1.00 35.74 ? 1037 HOH A O   1 
HETATM 8286 O  O   . HOH I 4 .   ? -0.682  -29.828 -22.937 1.00 41.63 ? 1038 HOH A O   1 
HETATM 8287 O  O   . HOH I 4 .   ? 7.817   -25.489 -20.849 1.00 26.14 ? 1039 HOH A O   1 
HETATM 8288 O  O   . HOH I 4 .   ? 22.273  -34.133 -20.806 1.00 31.78 ? 1040 HOH A O   1 
HETATM 8289 O  O   . HOH I 4 .   ? 27.968  -4.148  -43.890 1.00 23.50 ? 1041 HOH A O   1 
HETATM 8290 O  O   . HOH I 4 .   ? -8.260  -2.662  -25.073 1.00 37.83 ? 1042 HOH A O   1 
HETATM 8291 O  O   . HOH I 4 .   ? 23.361  -23.457 -36.944 1.00 21.88 ? 1043 HOH A O   1 
HETATM 8292 O  O   . HOH I 4 .   ? 7.428   -27.839 -23.218 1.00 33.81 ? 1044 HOH A O   1 
HETATM 8293 O  O   . HOH I 4 .   ? -2.779  -14.792 -2.928  1.00 27.06 ? 1045 HOH A O   1 
HETATM 8294 O  O   . HOH I 4 .   ? 33.018  -5.016  -30.016 1.00 26.74 ? 1046 HOH A O   1 
HETATM 8295 O  O   . HOH I 4 .   ? 28.018  -6.085  -40.372 1.00 28.68 ? 1047 HOH A O   1 
HETATM 8296 O  O   . HOH I 4 .   ? 36.079  -15.954 -22.545 1.00 27.99 ? 1048 HOH A O   1 
HETATM 8297 O  O   . HOH I 4 .   ? 7.146   -16.132 -9.661  1.00 29.32 ? 1049 HOH A O   1 
HETATM 8298 O  O   . HOH I 4 .   ? 31.551  -2.184  -37.001 1.00 24.22 ? 1050 HOH A O   1 
HETATM 8299 O  O   . HOH I 4 .   ? 31.950  -30.506 -24.593 1.00 49.51 ? 1051 HOH A O   1 
HETATM 8300 O  O   . HOH I 4 .   ? 21.840  0.355   -23.420 1.00 41.20 ? 1052 HOH A O   1 
HETATM 8301 O  O   . HOH I 4 .   ? 19.173  -6.770  -16.269 1.00 45.71 ? 1053 HOH A O   1 
HETATM 8302 O  O   . HOH I 4 .   ? 4.591   -17.550 -8.993  1.00 26.14 ? 1054 HOH A O   1 
HETATM 8303 O  O   . HOH I 4 .   ? 25.055  0.725   -20.674 1.00 41.88 ? 1055 HOH A O   1 
HETATM 8304 O  O   . HOH I 4 .   ? 28.821  -1.644  -45.338 1.00 32.53 ? 1056 HOH A O   1 
HETATM 8305 O  O   . HOH I 4 .   ? 32.791  -25.892 -10.878 1.00 37.83 ? 1057 HOH A O   1 
HETATM 8306 O  O   . HOH I 4 .   ? 16.402  12.260  -37.743 1.00 41.01 ? 1058 HOH A O   1 
HETATM 8307 O  O   . HOH I 4 .   ? 20.528  10.833  -18.200 1.00 35.16 ? 1059 HOH A O   1 
HETATM 8308 O  O   . HOH I 4 .   ? -1.274  -10.339 -35.396 1.00 23.96 ? 1060 HOH A O   1 
HETATM 8309 O  O   . HOH I 4 .   ? -8.723  -17.795 -32.219 1.00 23.82 ? 1061 HOH A O   1 
HETATM 8310 O  O   . HOH I 4 .   ? 31.362  -24.366 -11.709 1.00 54.32 ? 1062 HOH A O   1 
HETATM 8311 O  O   . HOH I 4 .   ? -1.176  -6.033  -33.960 1.00 48.18 ? 1063 HOH A O   1 
HETATM 8312 O  O   . HOH I 4 .   ? 15.017  -9.964  -41.188 1.00 43.60 ? 1064 HOH A O   1 
HETATM 8313 O  O   . HOH I 4 .   ? 15.565  -3.841  -10.335 1.00 34.63 ? 1065 HOH A O   1 
HETATM 8314 O  O   . HOH I 4 .   ? 20.249  -24.608 -36.771 1.00 46.05 ? 1066 HOH A O   1 
HETATM 8315 O  O   . HOH I 4 .   ? -7.280  -9.078  -19.156 1.00 32.29 ? 1067 HOH A O   1 
HETATM 8316 O  O   . HOH I 4 .   ? 32.360  -0.502  -31.582 1.00 31.99 ? 1068 HOH A O   1 
HETATM 8317 O  O   . HOH I 4 .   ? 32.066  -23.929 -34.490 1.00 29.77 ? 1069 HOH A O   1 
HETATM 8318 O  O   . HOH J 4 .   ? 38.894  32.508  -35.109 1.00 23.23 ? 901  HOH B O   1 
HETATM 8319 O  O   . HOH J 4 .   ? 16.397  37.362  -26.097 1.00 28.92 ? 902  HOH B O   1 
HETATM 8320 O  O   . HOH J 4 .   ? 9.715   48.236  -29.236 1.00 12.66 ? 903  HOH B O   1 
HETATM 8321 O  O   . HOH J 4 .   ? 31.137  37.674  -38.834 1.00 17.88 ? 904  HOH B O   1 
HETATM 8322 O  O   . HOH J 4 .   ? 19.756  6.641   -5.665  1.00 36.27 ? 905  HOH B O   1 
HETATM 8323 O  O   . HOH J 4 .   ? 15.139  14.284  -23.245 1.00 30.04 ? 906  HOH B O   1 
HETATM 8324 O  O   . HOH J 4 .   ? 3.938   30.355  -22.251 1.00 16.44 ? 907  HOH B O   1 
HETATM 8325 O  O   . HOH J 4 .   ? 39.532  34.824  -3.831  1.00 34.64 ? 908  HOH B O   1 
HETATM 8326 O  O   . HOH J 4 .   ? 24.026  13.674  -19.149 1.00 29.09 ? 909  HOH B O   1 
HETATM 8327 O  O   . HOH J 4 .   ? 21.022  41.027  -44.018 1.00 18.09 ? 910  HOH B O   1 
HETATM 8328 O  O   . HOH J 4 .   ? 7.493   36.112  -10.835 1.00 16.28 ? 911  HOH B O   1 
HETATM 8329 O  O   . HOH J 4 .   ? 15.978  23.863  -31.197 1.00 24.75 ? 912  HOH B O   1 
HETATM 8330 O  O   . HOH J 4 .   ? 37.716  20.644  -18.912 1.00 19.94 ? 913  HOH B O   1 
HETATM 8331 O  O   . HOH J 4 .   ? 36.853  40.129  -33.060 1.00 23.95 ? 914  HOH B O   1 
HETATM 8332 O  O   . HOH J 4 .   ? 19.702  30.604  -6.592  1.00 19.55 ? 915  HOH B O   1 
HETATM 8333 O  O   . HOH J 4 .   ? 12.619  43.383  -4.094  1.00 27.60 ? 916  HOH B O   1 
HETATM 8334 O  O   . HOH J 4 .   ? 33.063  50.941  -22.641 1.00 18.71 ? 917  HOH B O   1 
HETATM 8335 O  O   . HOH J 4 .   ? 16.113  27.703  -29.270 1.00 19.01 ? 918  HOH B O   1 
HETATM 8336 O  O   . HOH J 4 .   ? 35.948  8.566   4.121   1.00 23.44 ? 919  HOH B O   1 
HETATM 8337 O  O   . HOH J 4 .   ? 10.947  36.180  -41.490 1.00 17.50 ? 920  HOH B O   1 
HETATM 8338 O  O   . HOH J 4 .   ? 10.582  18.725  -33.032 1.00 34.90 ? 921  HOH B O   1 
HETATM 8339 O  O   . HOH J 4 .   ? 29.278  20.386  -17.534 1.00 22.60 ? 922  HOH B O   1 
HETATM 8340 O  O   . HOH J 4 .   ? 40.944  44.065  -21.458 1.00 26.02 ? 923  HOH B O   1 
HETATM 8341 O  O   . HOH J 4 .   ? 1.691   33.783  -14.977 1.00 22.26 ? 924  HOH B O   1 
HETATM 8342 O  O   . HOH J 4 .   ? 20.892  25.172  -15.063 1.00 16.30 ? 925  HOH B O   1 
HETATM 8343 O  O   . HOH J 4 .   ? 2.191   26.917  -29.565 1.00 15.63 ? 926  HOH B O   1 
HETATM 8344 O  O   . HOH J 4 .   ? 23.367  28.913  -36.060 1.00 21.73 ? 927  HOH B O   1 
HETATM 8345 O  O   . HOH J 4 .   ? 8.715   26.396  -23.189 1.00 19.08 ? 928  HOH B O   1 
HETATM 8346 O  O   . HOH J 4 .   ? 13.851  35.570  -1.313  1.00 28.78 ? 929  HOH B O   1 
HETATM 8347 O  O   . HOH J 4 .   ? 11.447  49.761  -14.350 1.00 16.70 ? 930  HOH B O   1 
HETATM 8348 O  O   . HOH J 4 .   ? 5.894   26.367  -14.523 1.00 25.19 ? 931  HOH B O   1 
HETATM 8349 O  O   . HOH J 4 .   ? 11.999  34.224  -39.961 1.00 12.30 ? 932  HOH B O   1 
HETATM 8350 O  O   . HOH J 4 .   ? -0.003  44.908  -8.737  1.00 30.40 ? 933  HOH B O   1 
HETATM 8351 O  O   . HOH J 4 .   ? 34.966  30.772  -18.005 1.00 14.44 ? 934  HOH B O   1 
HETATM 8352 O  O   . HOH J 4 .   ? 18.317  37.576  -18.367 1.00 20.13 ? 935  HOH B O   1 
HETATM 8353 O  O   . HOH J 4 .   ? 23.947  39.256  -20.713 1.00 14.69 ? 936  HOH B O   1 
HETATM 8354 O  O   . HOH J 4 .   ? 42.315  54.441  -23.290 1.00 33.31 ? 937  HOH B O   1 
HETATM 8355 O  O   . HOH J 4 .   ? 32.141  29.812  -6.159  1.00 25.14 ? 938  HOH B O   1 
HETATM 8356 O  O   . HOH J 4 .   ? 6.464   30.282  -23.508 1.00 16.23 ? 939  HOH B O   1 
HETATM 8357 O  O   . HOH J 4 .   ? 5.035   35.975  -5.636  1.00 21.63 ? 940  HOH B O   1 
HETATM 8358 O  O   . HOH J 4 .   ? 13.257  29.551  -42.096 1.00 20.78 ? 941  HOH B O   1 
HETATM 8359 O  O   . HOH J 4 .   ? 23.570  34.731  -39.688 1.00 19.28 ? 942  HOH B O   1 
HETATM 8360 O  O   . HOH J 4 .   ? 8.436   18.490  -24.466 1.00 24.34 ? 943  HOH B O   1 
HETATM 8361 O  O   . HOH J 4 .   ? 34.246  28.330  -19.045 1.00 17.30 ? 944  HOH B O   1 
HETATM 8362 O  O   . HOH J 4 .   ? 1.178   30.417  -18.072 1.00 22.53 ? 945  HOH B O   1 
HETATM 8363 O  O   . HOH J 4 .   ? 33.240  14.884  7.358   1.00 17.38 ? 946  HOH B O   1 
HETATM 8364 O  O   . HOH J 4 .   ? 23.571  39.099  -23.412 1.00 19.52 ? 947  HOH B O   1 
HETATM 8365 O  O   . HOH J 4 .   ? 19.350  20.395  -7.282  1.00 17.54 ? 948  HOH B O   1 
HETATM 8366 O  O   . HOH J 4 .   ? 24.314  55.073  -22.755 1.00 17.33 ? 949  HOH B O   1 
HETATM 8367 O  O   . HOH J 4 .   ? 40.812  22.347  -15.920 1.00 25.05 ? 950  HOH B O   1 
HETATM 8368 O  O   . HOH J 4 .   ? 2.754   46.430  -28.194 1.00 17.50 ? 951  HOH B O   1 
HETATM 8369 O  O   . HOH J 4 .   ? 11.180  28.112  -5.400  1.00 17.88 ? 952  HOH B O   1 
HETATM 8370 O  O   . HOH J 4 .   ? 19.432  9.539   -1.607  1.00 29.80 ? 953  HOH B O   1 
HETATM 8371 O  O   . HOH J 4 .   ? 27.687  40.022  -37.804 1.00 12.78 ? 954  HOH B O   1 
HETATM 8372 O  O   . HOH J 4 .   ? 13.132  27.313  -36.205 1.00 23.98 ? 955  HOH B O   1 
HETATM 8373 O  O   . HOH J 4 .   ? 36.563  30.659  -24.004 1.00 16.10 ? 956  HOH B O   1 
HETATM 8374 O  O   . HOH J 4 .   ? 36.045  49.253  -29.000 1.00 20.99 ? 957  HOH B O   1 
HETATM 8375 O  O   . HOH J 4 .   ? 9.467   25.389  -30.089 1.00 18.25 ? 958  HOH B O   1 
HETATM 8376 O  O   . HOH J 4 .   ? 9.844   30.027  -4.050  1.00 31.64 ? 959  HOH B O   1 
HETATM 8377 O  O   . HOH J 4 .   ? 27.004  31.112  -15.592 1.00 22.94 ? 960  HOH B O   1 
HETATM 8378 O  O   . HOH J 4 .   ? 17.082  11.096  -13.087 1.00 28.02 ? 961  HOH B O   1 
HETATM 8379 O  O   . HOH J 4 .   ? 33.025  25.046  -17.236 1.00 18.08 ? 962  HOH B O   1 
HETATM 8380 O  O   . HOH J 4 .   ? 21.982  45.915  -24.172 1.00 18.84 ? 963  HOH B O   1 
HETATM 8381 O  O   . HOH J 4 .   ? 17.145  49.745  -44.016 1.00 31.24 ? 964  HOH B O   1 
HETATM 8382 O  O   . HOH J 4 .   ? 12.240  26.848  -24.465 1.00 20.05 ? 965  HOH B O   1 
HETATM 8383 O  O   . HOH J 4 .   ? 8.583   37.573  -23.301 1.00 18.09 ? 966  HOH B O   1 
HETATM 8384 O  O   . HOH J 4 .   ? 32.153  20.794  -9.668  1.00 18.38 ? 967  HOH B O   1 
HETATM 8385 O  O   . HOH J 4 .   ? 17.669  51.767  -28.752 1.00 18.15 ? 968  HOH B O   1 
HETATM 8386 O  O   . HOH J 4 .   ? 10.001  43.244  -39.138 1.00 19.20 ? 969  HOH B O   1 
HETATM 8387 O  O   . HOH J 4 .   ? 35.628  32.064  -8.915  1.00 16.78 ? 970  HOH B O   1 
HETATM 8388 O  O   . HOH J 4 .   ? 6.380   45.389  -31.108 1.00 23.86 ? 971  HOH B O   1 
HETATM 8389 O  O   . HOH J 4 .   ? 21.860  47.757  -17.148 1.00 30.60 ? 972  HOH B O   1 
HETATM 8390 O  O   . HOH J 4 .   ? 19.924  27.055  -0.021  1.00 27.87 ? 973  HOH B O   1 
HETATM 8391 O  O   . HOH J 4 .   ? -3.005  21.160  -30.285 1.00 27.86 ? 974  HOH B O   1 
HETATM 8392 O  O   . HOH J 4 .   ? -2.548  36.849  -40.267 1.00 16.31 ? 975  HOH B O   1 
HETATM 8393 O  O   . HOH J 4 .   ? -4.155  30.076  -30.709 1.00 17.80 ? 976  HOH B O   1 
HETATM 8394 O  O   . HOH J 4 .   ? 18.925  47.179  -17.057 1.00 27.18 ? 977  HOH B O   1 
HETATM 8395 O  O   . HOH J 4 .   ? 9.682   40.124  -26.206 1.00 18.47 ? 978  HOH B O   1 
HETATM 8396 O  O   . HOH J 4 .   ? 35.299  13.602  14.661  1.00 26.29 ? 979  HOH B O   1 
HETATM 8397 O  O   . HOH J 4 .   ? 11.369  53.452  -40.402 1.00 41.33 ? 980  HOH B O   1 
HETATM 8398 O  O   . HOH J 4 .   ? 22.021  48.529  -44.569 1.00 28.49 ? 981  HOH B O   1 
HETATM 8399 O  O   . HOH J 4 .   ? 5.582   27.997  -11.462 1.00 17.61 ? 982  HOH B O   1 
HETATM 8400 O  O   . HOH J 4 .   ? 18.262  45.390  -18.827 1.00 19.19 ? 983  HOH B O   1 
HETATM 8401 O  O   . HOH J 4 .   ? 10.829  25.653  -34.888 1.00 16.41 ? 984  HOH B O   1 
HETATM 8402 O  O   . HOH J 4 .   ? 8.169   12.331  -10.581 1.00 29.30 ? 985  HOH B O   1 
HETATM 8403 O  O   . HOH J 4 .   ? 40.643  28.528  -30.552 1.00 22.41 ? 986  HOH B O   1 
HETATM 8404 O  O   . HOH J 4 .   ? 28.055  19.939  -15.143 1.00 18.63 ? 987  HOH B O   1 
HETATM 8405 O  O   . HOH J 4 .   ? 28.124  26.719  -23.723 1.00 28.21 ? 988  HOH B O   1 
HETATM 8406 O  O   . HOH J 4 .   ? 5.669   52.044  -27.090 1.00 16.92 ? 989  HOH B O   1 
HETATM 8407 O  O   . HOH J 4 .   ? 32.888  23.751  -27.697 1.00 25.13 ? 990  HOH B O   1 
HETATM 8408 O  O   . HOH J 4 .   ? 13.861  23.201  -40.389 1.00 27.86 ? 991  HOH B O   1 
HETATM 8409 O  O   . HOH J 4 .   ? -1.434  33.990  -20.030 1.00 46.81 ? 992  HOH B O   1 
HETATM 8410 O  O   . HOH J 4 .   ? 29.568  27.487  -16.877 1.00 26.77 ? 993  HOH B O   1 
HETATM 8411 O  O   . HOH J 4 .   ? 23.185  41.775  -21.384 1.00 19.99 ? 994  HOH B O   1 
HETATM 8412 O  O   . HOH J 4 .   ? 9.290   10.994  -29.402 1.00 19.87 ? 995  HOH B O   1 
HETATM 8413 O  O   . HOH J 4 .   ? 11.187  35.003  -37.193 1.00 18.50 ? 996  HOH B O   1 
HETATM 8414 O  O   . HOH J 4 .   ? 28.820  38.833  -40.052 1.00 17.44 ? 997  HOH B O   1 
HETATM 8415 O  O   . HOH J 4 .   ? 28.910  17.194  -17.176 1.00 28.82 ? 998  HOH B O   1 
HETATM 8416 O  O   . HOH J 4 .   ? 7.492   50.064  -28.584 1.00 15.92 ? 999  HOH B O   1 
HETATM 8417 O  O   . HOH J 4 .   ? 23.114  51.909  -12.845 1.00 36.16 ? 1000 HOH B O   1 
HETATM 8418 O  O   . HOH J 4 .   ? 12.389  27.149  -38.748 1.00 26.97 ? 1001 HOH B O   1 
HETATM 8419 O  O   . HOH J 4 .   ? 26.394  25.882  -5.508  1.00 16.18 ? 1002 HOH B O   1 
HETATM 8420 O  O   . HOH J 4 .   ? 2.148   30.033  -24.460 1.00 16.60 ? 1003 HOH B O   1 
HETATM 8421 O  O   . HOH J 4 .   ? 27.657  29.275  -17.495 1.00 21.14 ? 1004 HOH B O   1 
HETATM 8422 O  O   . HOH J 4 .   ? 19.038  28.353  -35.710 1.00 22.77 ? 1005 HOH B O   1 
HETATM 8423 O  O   . HOH J 4 .   ? 24.618  23.466  3.147   1.00 21.64 ? 1006 HOH B O   1 
HETATM 8424 O  O   . HOH J 4 .   ? 28.427  30.248  -37.683 1.00 15.79 ? 1007 HOH B O   1 
HETATM 8425 O  O   . HOH J 4 .   ? 20.308  42.081  -0.866  1.00 34.53 ? 1008 HOH B O   1 
HETATM 8426 O  O   . HOH J 4 .   ? 38.529  26.979  -31.471 1.00 18.62 ? 1009 HOH B O   1 
HETATM 8427 O  O   . HOH J 4 .   ? 0.357   43.331  -6.252  1.00 38.39 ? 1010 HOH B O   1 
HETATM 8428 O  O   . HOH J 4 .   ? 35.186  51.446  -20.939 1.00 25.20 ? 1011 HOH B O   1 
HETATM 8429 O  O   . HOH J 4 .   ? 25.215  19.531  -15.359 1.00 34.20 ? 1012 HOH B O   1 
HETATM 8430 O  O   . HOH J 4 .   ? 3.077   30.897  -36.576 1.00 22.12 ? 1013 HOH B O   1 
HETATM 8431 O  O   . HOH J 4 .   ? 31.319  23.400  3.432   1.00 28.91 ? 1014 HOH B O   1 
HETATM 8432 O  O   . HOH J 4 .   ? 24.879  28.801  -31.062 1.00 31.88 ? 1015 HOH B O   1 
HETATM 8433 O  O   . HOH J 4 .   ? 7.262   28.234  -21.591 1.00 19.58 ? 1016 HOH B O   1 
HETATM 8434 O  O   . HOH J 4 .   ? 29.873  38.968  -24.383 1.00 17.11 ? 1017 HOH B O   1 
HETATM 8435 O  O   . HOH J 4 .   ? 14.376  44.632  -43.107 1.00 16.72 ? 1018 HOH B O   1 
HETATM 8436 O  O   . HOH J 4 .   ? 19.269  49.482  -14.896 1.00 25.32 ? 1019 HOH B O   1 
HETATM 8437 O  O   . HOH J 4 .   ? 21.229  27.057  -19.512 1.00 28.90 ? 1020 HOH B O   1 
HETATM 8438 O  O   . HOH J 4 .   ? 9.689   30.529  -42.508 1.00 22.86 ? 1021 HOH B O   1 
HETATM 8439 O  O   . HOH J 4 .   ? 19.194  44.527  -45.079 1.00 35.97 ? 1022 HOH B O   1 
HETATM 8440 O  O   . HOH J 4 .   ? 6.741   27.720  -5.442  1.00 34.53 ? 1023 HOH B O   1 
HETATM 8441 O  O   . HOH J 4 .   ? 14.721  39.224  -25.654 1.00 32.14 ? 1024 HOH B O   1 
HETATM 8442 O  O   . HOH J 4 .   ? 2.876   51.599  -33.139 1.00 20.56 ? 1025 HOH B O   1 
HETATM 8443 O  O   . HOH J 4 .   ? -3.880  18.116  -31.233 1.00 41.33 ? 1026 HOH B O   1 
HETATM 8444 O  O   . HOH J 4 .   ? 16.511  39.530  -17.333 1.00 14.04 ? 1027 HOH B O   1 
HETATM 8445 O  O   . HOH J 4 .   ? 21.135  29.226  -37.232 1.00 16.74 ? 1028 HOH B O   1 
HETATM 8446 O  O   . HOH J 4 .   ? 26.814  38.515  -4.513  1.00 25.00 ? 1029 HOH B O   1 
HETATM 8447 O  O   . HOH J 4 .   ? 24.395  49.754  -43.439 1.00 19.63 ? 1030 HOH B O   1 
HETATM 8448 O  O   . HOH J 4 .   ? 13.167  39.520  -28.155 1.00 28.79 ? 1031 HOH B O   1 
HETATM 8449 O  O   . HOH J 4 .   ? 13.188  51.081  -21.176 1.00 33.48 ? 1032 HOH B O   1 
HETATM 8450 O  O   . HOH J 4 .   ? 33.521  49.848  -40.776 1.00 32.31 ? 1033 HOH B O   1 
HETATM 8451 O  O   . HOH J 4 .   ? 14.857  8.987   -9.673  1.00 25.66 ? 1034 HOH B O   1 
HETATM 8452 O  O   . HOH J 4 .   ? 14.366  14.280  -31.085 1.00 34.09 ? 1035 HOH B O   1 
HETATM 8453 O  O   . HOH J 4 .   ? 2.644   22.304  -20.376 1.00 34.56 ? 1036 HOH B O   1 
HETATM 8454 O  O   . HOH J 4 .   ? 10.285  49.115  -21.452 1.00 31.76 ? 1037 HOH B O   1 
HETATM 8455 O  O   . HOH J 4 .   ? 9.903   18.395  -26.978 1.00 21.58 ? 1038 HOH B O   1 
HETATM 8456 O  O   . HOH J 4 .   ? 0.450   35.824  -28.764 1.00 34.99 ? 1039 HOH B O   1 
HETATM 8457 O  O   . HOH J 4 .   ? 26.181  56.772  -34.292 1.00 18.68 ? 1040 HOH B O   1 
HETATM 8458 O  O   . HOH J 4 .   ? 18.408  41.759  -47.034 1.00 28.88 ? 1041 HOH B O   1 
HETATM 8459 O  O   . HOH J 4 .   ? 25.729  26.018  -24.929 1.00 32.78 ? 1042 HOH B O   1 
HETATM 8460 O  O   . HOH J 4 .   ? 21.389  20.705  -9.683  1.00 18.04 ? 1043 HOH B O   1 
HETATM 8461 O  O   . HOH J 4 .   ? 38.854  20.246  -14.398 1.00 30.91 ? 1044 HOH B O   1 
HETATM 8462 O  O   . HOH J 4 .   ? 6.970   20.447  -40.296 1.00 31.32 ? 1045 HOH B O   1 
HETATM 8463 O  O   . HOH J 4 .   ? 18.591  20.029  9.727   1.00 41.91 ? 1046 HOH B O   1 
HETATM 8464 O  O   . HOH J 4 .   ? 43.143  30.368  -22.620 1.00 23.11 ? 1047 HOH B O   1 
HETATM 8465 O  O   . HOH J 4 .   ? 8.351   47.264  -31.317 1.00 18.43 ? 1048 HOH B O   1 
HETATM 8466 O  O   . HOH J 4 .   ? 2.196   41.425  -32.379 1.00 22.95 ? 1049 HOH B O   1 
HETATM 8467 O  O   . HOH J 4 .   ? 12.615  25.309  -40.557 1.00 22.82 ? 1050 HOH B O   1 
HETATM 8468 O  O   . HOH J 4 .   ? 9.679   25.211  -4.453  1.00 34.93 ? 1051 HOH B O   1 
HETATM 8469 O  O   . HOH J 4 .   ? 36.383  40.155  -5.508  1.00 25.65 ? 1052 HOH B O   1 
HETATM 8470 O  O   . HOH J 4 .   ? 35.066  16.134  -19.243 1.00 28.46 ? 1053 HOH B O   1 
HETATM 8471 O  O   . HOH J 4 .   ? 37.934  15.876  -9.896  1.00 28.89 ? 1054 HOH B O   1 
HETATM 8472 O  O   . HOH J 4 .   ? 12.451  16.563  -8.406  1.00 26.20 ? 1055 HOH B O   1 
HETATM 8473 O  O   . HOH J 4 .   ? 17.010  17.549  8.772   1.00 38.26 ? 1056 HOH B O   1 
HETATM 8474 O  O   . HOH J 4 .   ? 2.979   43.454  -34.154 1.00 19.21 ? 1057 HOH B O   1 
HETATM 8475 O  O   . HOH J 4 .   ? 27.226  10.072  -17.687 1.00 49.17 ? 1058 HOH B O   1 
HETATM 8476 O  O   . HOH J 4 .   ? 38.395  17.416  -7.249  1.00 32.88 ? 1059 HOH B O   1 
HETATM 8477 O  O   . HOH J 4 .   ? 24.302  26.683  -34.685 1.00 36.58 ? 1060 HOH B O   1 
HETATM 8478 O  O   . HOH J 4 .   ? 25.303  19.028  -18.218 1.00 34.48 ? 1061 HOH B O   1 
HETATM 8479 O  O   . HOH J 4 .   ? 11.226  41.474  -28.254 1.00 23.09 ? 1062 HOH B O   1 
HETATM 8480 O  O   . HOH J 4 .   ? 17.886  25.586  -29.633 1.00 32.15 ? 1063 HOH B O   1 
HETATM 8481 O  O   . HOH J 4 .   ? 3.984   39.311  -40.481 1.00 23.86 ? 1064 HOH B O   1 
HETATM 8482 O  O   . HOH J 4 .   ? 9.011   12.064  -19.020 1.00 32.72 ? 1065 HOH B O   1 
HETATM 8483 O  O   . HOH J 4 .   ? 40.084  20.031  -28.469 1.00 45.67 ? 1066 HOH B O   1 
# 
