data_9JSG
# 
_entry.id   9JSG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9JSG         pdb_00009jsg 10.2210/pdb9jsg/pdb 
WWPDB D_1300051722 ?            ?                   
EMDB  EMD-61772    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'EM metadata'     1 0 2025-05-14 ? 
3 'Additional map'  1 0 2025-05-14 1 
4 'Half map'        1 0 2025-05-14 1 
5 'Half map'        1 0 2025-05-14 2 
6 Image             1 0 2025-05-14 ? 
7 'Primary map'     1 0 2025-05-14 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JSG 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Clostridium perfringens iota toxin pore Ib in pore state' 
_pdbx_database_related.db_id          EMD-61772 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 6 
_pdbx_contact_author.email              tsuge@cc.kyoto-su.ac.jp 
_pdbx_contact_author.name_first         Hideaki 
_pdbx_contact_author.name_last          Tsuge 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0166-9163 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yamada, T.'  1 0000-0002-5828-3993 
'Sugita, Y.'  2 0000-0001-6861-4840 
'Yoshida, T.' 3 0000-0002-1384-2210 
'Noda, T.'    4 0000-0002-0658-4663 
'Tsuge, H.'   5 0000-0003-0166-9163 
# 
_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                     'Step-by-Step Maturation Mechanism of Binary Toxin Pore Revealed by Cryo-EM Analysis' 
_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 'Yamada, T.'  1 0000-0002-5828-3993 
primary 'Sugita, Y.'  2 0000-0001-6861-4840 
primary 'Yoshida, T.' 3 0000-0002-1384-2210 
primary 'Noda, T.'    4 0000-0002-0658-4663 
primary 'Tsuge, H.'   5 0000-0003-0166-9163 
# 
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 'Iota toxin component Ib' 76638.297 1 ? ? ? ? 
2 non-polymer syn 'CALCIUM ION'             40.078    3 ? ? ? ? 
# 
_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       
;NNFFDVRFFSAAWEDEDLDTDNDNIPDAYEKNGYTIKDSIAVKWNDSFAEQGYKKYVSSYLESNTAGDPYTDYQKASGSI
DKAIKLEARDPLVAAYPVVGVGMENLIISTNEHASSDQGKTVSRATTNSKTDANTVGVSISAGYQNGFTGNITTSYSHTT
DNSTAVQDSNGESWNTGLSINKGESAYINANVRYYNTGTAPMYKVTPTTNLVLDGETLATIKAQDNQIGNNLSPNETYPK
KGLSPLALNTMDQFNARLIPINYDQLKKLDSGKQIKLETTQVSGNYGTKNSQGQIITEGNSWSNYISQIDSVSASIILDT
GSQTFERRVAAKEQGNPEDKTPEITIGEAIKKAFSATKNGELLYFNGIPIDESCVELIFDDNTSEIIKEQLKYLDDKKIY
NVKLERGMNILIKVPSYFTNFDEYNNFPASWSNIDTKNQDGLQSVANKLSGETKIIIPMSKLKPYKRYVFSGYSKDPSTS
NSITVNIKSKEQKTDYLVPEKDYTKFSYEFETTGKDSSDIEITLTSSGVIFLDNLSITELNSTPEILKEPEIKVPSDQEI
LDAHNKYYADIKLDTNTGNTYIDGIYFEPTQTNKEALDYIQKYRVEATLQYSGFKDIGTKDKEIRNYLGDQNQPKTNYIN
FRSYFTSGENVMTYKKLRIYAVTPDNRELLVLSVNLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;NNFFDVRFFSAAWEDEDLDTDNDNIPDAYEKNGYTIKDSIAVKWNDSFAEQGYKKYVSSYLESNTAGDPYTDYQKASGSI
DKAIKLEARDPLVAAYPVVGVGMENLIISTNEHASSDQGKTVSRATTNSKTDANTVGVSISAGYQNGFTGNITTSYSHTT
DNSTAVQDSNGESWNTGLSINKGESAYINANVRYYNTGTAPMYKVTPTTNLVLDGETLATIKAQDNQIGNNLSPNETYPK
KGLSPLALNTMDQFNARLIPINYDQLKKLDSGKQIKLETTQVSGNYGTKNSQGQIITEGNSWSNYISQIDSVSASIILDT
GSQTFERRVAAKEQGNPEDKTPEITIGEAIKKAFSATKNGELLYFNGIPIDESCVELIFDDNTSEIIKEQLKYLDDKKIY
NVKLERGMNILIKVPSYFTNFDEYNNFPASWSNIDTKNQDGLQSVANKLSGETKIIIPMSKLKPYKRYVFSGYSKDPSTS
NSITVNIKSKEQKTDYLVPEKDYTKFSYEFETTGKDSSDIEITLTSSGVIFLDNLSITELNSTPEILKEPEIKVPSDQEI
LDAHNKYYADIKLDTNTGNTYIDGIYFEPTQTNKEALDYIQKYRVEATLQYSGFKDIGTKDKEIRNYLGDQNQPKTNYIN
FRSYFTSGENVMTYKKLRIYAVTPDNRELLVLSVNLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'CALCIUM ION' 
_pdbx_entity_nonpoly.comp_id     CA 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASN n 
1 2   ASN n 
1 3   PHE n 
1 4   PHE n 
1 5   ASP n 
1 6   VAL n 
1 7   ARG n 
1 8   PHE n 
1 9   PHE n 
1 10  SER n 
1 11  ALA n 
1 12  ALA n 
1 13  TRP n 
1 14  GLU n 
1 15  ASP n 
1 16  GLU n 
1 17  ASP n 
1 18  LEU n 
1 19  ASP n 
1 20  THR n 
1 21  ASP n 
1 22  ASN n 
1 23  ASP n 
1 24  ASN n 
1 25  ILE n 
1 26  PRO n 
1 27  ASP n 
1 28  ALA n 
1 29  TYR n 
1 30  GLU n 
1 31  LYS n 
1 32  ASN n 
1 33  GLY n 
1 34  TYR n 
1 35  THR n 
1 36  ILE n 
1 37  LYS n 
1 38  ASP n 
1 39  SER n 
1 40  ILE n 
1 41  ALA n 
1 42  VAL n 
1 43  LYS n 
1 44  TRP n 
1 45  ASN n 
1 46  ASP n 
1 47  SER n 
1 48  PHE n 
1 49  ALA n 
1 50  GLU n 
1 51  GLN n 
1 52  GLY n 
1 53  TYR n 
1 54  LYS n 
1 55  LYS n 
1 56  TYR n 
1 57  VAL n 
1 58  SER n 
1 59  SER n 
1 60  TYR n 
1 61  LEU n 
1 62  GLU n 
1 63  SER n 
1 64  ASN n 
1 65  THR n 
1 66  ALA n 
1 67  GLY n 
1 68  ASP n 
1 69  PRO n 
1 70  TYR n 
1 71  THR n 
1 72  ASP n 
1 73  TYR n 
1 74  GLN n 
1 75  LYS n 
1 76  ALA n 
1 77  SER n 
1 78  GLY n 
1 79  SER n 
1 80  ILE n 
1 81  ASP n 
1 82  LYS n 
1 83  ALA n 
1 84  ILE n 
1 85  LYS n 
1 86  LEU n 
1 87  GLU n 
1 88  ALA n 
1 89  ARG n 
1 90  ASP n 
1 91  PRO n 
1 92  LEU n 
1 93  VAL n 
1 94  ALA n 
1 95  ALA n 
1 96  TYR n 
1 97  PRO n 
1 98  VAL n 
1 99  VAL n 
1 100 GLY n 
1 101 VAL n 
1 102 GLY n 
1 103 MET n 
1 104 GLU n 
1 105 ASN n 
1 106 LEU n 
1 107 ILE n 
1 108 ILE n 
1 109 SER n 
1 110 THR n 
1 111 ASN n 
1 112 GLU n 
1 113 HIS n 
1 114 ALA n 
1 115 SER n 
1 116 SER n 
1 117 ASP n 
1 118 GLN n 
1 119 GLY n 
1 120 LYS n 
1 121 THR n 
1 122 VAL n 
1 123 SER n 
1 124 ARG n 
1 125 ALA n 
1 126 THR n 
1 127 THR n 
1 128 ASN n 
1 129 SER n 
1 130 LYS n 
1 131 THR n 
1 132 ASP n 
1 133 ALA n 
1 134 ASN n 
1 135 THR n 
1 136 VAL n 
1 137 GLY n 
1 138 VAL n 
1 139 SER n 
1 140 ILE n 
1 141 SER n 
1 142 ALA n 
1 143 GLY n 
1 144 TYR n 
1 145 GLN n 
1 146 ASN n 
1 147 GLY n 
1 148 PHE n 
1 149 THR n 
1 150 GLY n 
1 151 ASN n 
1 152 ILE n 
1 153 THR n 
1 154 THR n 
1 155 SER n 
1 156 TYR n 
1 157 SER n 
1 158 HIS n 
1 159 THR n 
1 160 THR n 
1 161 ASP n 
1 162 ASN n 
1 163 SER n 
1 164 THR n 
1 165 ALA n 
1 166 VAL n 
1 167 GLN n 
1 168 ASP n 
1 169 SER n 
1 170 ASN n 
1 171 GLY n 
1 172 GLU n 
1 173 SER n 
1 174 TRP n 
1 175 ASN n 
1 176 THR n 
1 177 GLY n 
1 178 LEU n 
1 179 SER n 
1 180 ILE n 
1 181 ASN n 
1 182 LYS n 
1 183 GLY n 
1 184 GLU n 
1 185 SER n 
1 186 ALA n 
1 187 TYR n 
1 188 ILE n 
1 189 ASN n 
1 190 ALA n 
1 191 ASN n 
1 192 VAL n 
1 193 ARG n 
1 194 TYR n 
1 195 TYR n 
1 196 ASN n 
1 197 THR n 
1 198 GLY n 
1 199 THR n 
1 200 ALA n 
1 201 PRO n 
1 202 MET n 
1 203 TYR n 
1 204 LYS n 
1 205 VAL n 
1 206 THR n 
1 207 PRO n 
1 208 THR n 
1 209 THR n 
1 210 ASN n 
1 211 LEU n 
1 212 VAL n 
1 213 LEU n 
1 214 ASP n 
1 215 GLY n 
1 216 GLU n 
1 217 THR n 
1 218 LEU n 
1 219 ALA n 
1 220 THR n 
1 221 ILE n 
1 222 LYS n 
1 223 ALA n 
1 224 GLN n 
1 225 ASP n 
1 226 ASN n 
1 227 GLN n 
1 228 ILE n 
1 229 GLY n 
1 230 ASN n 
1 231 ASN n 
1 232 LEU n 
1 233 SER n 
1 234 PRO n 
1 235 ASN n 
1 236 GLU n 
1 237 THR n 
1 238 TYR n 
1 239 PRO n 
1 240 LYS n 
1 241 LYS n 
1 242 GLY n 
1 243 LEU n 
1 244 SER n 
1 245 PRO n 
1 246 LEU n 
1 247 ALA n 
1 248 LEU n 
1 249 ASN n 
1 250 THR n 
1 251 MET n 
1 252 ASP n 
1 253 GLN n 
1 254 PHE n 
1 255 ASN n 
1 256 ALA n 
1 257 ARG n 
1 258 LEU n 
1 259 ILE n 
1 260 PRO n 
1 261 ILE n 
1 262 ASN n 
1 263 TYR n 
1 264 ASP n 
1 265 GLN n 
1 266 LEU n 
1 267 LYS n 
1 268 LYS n 
1 269 LEU n 
1 270 ASP n 
1 271 SER n 
1 272 GLY n 
1 273 LYS n 
1 274 GLN n 
1 275 ILE n 
1 276 LYS n 
1 277 LEU n 
1 278 GLU n 
1 279 THR n 
1 280 THR n 
1 281 GLN n 
1 282 VAL n 
1 283 SER n 
1 284 GLY n 
1 285 ASN n 
1 286 TYR n 
1 287 GLY n 
1 288 THR n 
1 289 LYS n 
1 290 ASN n 
1 291 SER n 
1 292 GLN n 
1 293 GLY n 
1 294 GLN n 
1 295 ILE n 
1 296 ILE n 
1 297 THR n 
1 298 GLU n 
1 299 GLY n 
1 300 ASN n 
1 301 SER n 
1 302 TRP n 
1 303 SER n 
1 304 ASN n 
1 305 TYR n 
1 306 ILE n 
1 307 SER n 
1 308 GLN n 
1 309 ILE n 
1 310 ASP n 
1 311 SER n 
1 312 VAL n 
1 313 SER n 
1 314 ALA n 
1 315 SER n 
1 316 ILE n 
1 317 ILE n 
1 318 LEU n 
1 319 ASP n 
1 320 THR n 
1 321 GLY n 
1 322 SER n 
1 323 GLN n 
1 324 THR n 
1 325 PHE n 
1 326 GLU n 
1 327 ARG n 
1 328 ARG n 
1 329 VAL n 
1 330 ALA n 
1 331 ALA n 
1 332 LYS n 
1 333 GLU n 
1 334 GLN n 
1 335 GLY n 
1 336 ASN n 
1 337 PRO n 
1 338 GLU n 
1 339 ASP n 
1 340 LYS n 
1 341 THR n 
1 342 PRO n 
1 343 GLU n 
1 344 ILE n 
1 345 THR n 
1 346 ILE n 
1 347 GLY n 
1 348 GLU n 
1 349 ALA n 
1 350 ILE n 
1 351 LYS n 
1 352 LYS n 
1 353 ALA n 
1 354 PHE n 
1 355 SER n 
1 356 ALA n 
1 357 THR n 
1 358 LYS n 
1 359 ASN n 
1 360 GLY n 
1 361 GLU n 
1 362 LEU n 
1 363 LEU n 
1 364 TYR n 
1 365 PHE n 
1 366 ASN n 
1 367 GLY n 
1 368 ILE n 
1 369 PRO n 
1 370 ILE n 
1 371 ASP n 
1 372 GLU n 
1 373 SER n 
1 374 CYS n 
1 375 VAL n 
1 376 GLU n 
1 377 LEU n 
1 378 ILE n 
1 379 PHE n 
1 380 ASP n 
1 381 ASP n 
1 382 ASN n 
1 383 THR n 
1 384 SER n 
1 385 GLU n 
1 386 ILE n 
1 387 ILE n 
1 388 LYS n 
1 389 GLU n 
1 390 GLN n 
1 391 LEU n 
1 392 LYS n 
1 393 TYR n 
1 394 LEU n 
1 395 ASP n 
1 396 ASP n 
1 397 LYS n 
1 398 LYS n 
1 399 ILE n 
1 400 TYR n 
1 401 ASN n 
1 402 VAL n 
1 403 LYS n 
1 404 LEU n 
1 405 GLU n 
1 406 ARG n 
1 407 GLY n 
1 408 MET n 
1 409 ASN n 
1 410 ILE n 
1 411 LEU n 
1 412 ILE n 
1 413 LYS n 
1 414 VAL n 
1 415 PRO n 
1 416 SER n 
1 417 TYR n 
1 418 PHE n 
1 419 THR n 
1 420 ASN n 
1 421 PHE n 
1 422 ASP n 
1 423 GLU n 
1 424 TYR n 
1 425 ASN n 
1 426 ASN n 
1 427 PHE n 
1 428 PRO n 
1 429 ALA n 
1 430 SER n 
1 431 TRP n 
1 432 SER n 
1 433 ASN n 
1 434 ILE n 
1 435 ASP n 
1 436 THR n 
1 437 LYS n 
1 438 ASN n 
1 439 GLN n 
1 440 ASP n 
1 441 GLY n 
1 442 LEU n 
1 443 GLN n 
1 444 SER n 
1 445 VAL n 
1 446 ALA n 
1 447 ASN n 
1 448 LYS n 
1 449 LEU n 
1 450 SER n 
1 451 GLY n 
1 452 GLU n 
1 453 THR n 
1 454 LYS n 
1 455 ILE n 
1 456 ILE n 
1 457 ILE n 
1 458 PRO n 
1 459 MET n 
1 460 SER n 
1 461 LYS n 
1 462 LEU n 
1 463 LYS n 
1 464 PRO n 
1 465 TYR n 
1 466 LYS n 
1 467 ARG n 
1 468 TYR n 
1 469 VAL n 
1 470 PHE n 
1 471 SER n 
1 472 GLY n 
1 473 TYR n 
1 474 SER n 
1 475 LYS n 
1 476 ASP n 
1 477 PRO n 
1 478 SER n 
1 479 THR n 
1 480 SER n 
1 481 ASN n 
1 482 SER n 
1 483 ILE n 
1 484 THR n 
1 485 VAL n 
1 486 ASN n 
1 487 ILE n 
1 488 LYS n 
1 489 SER n 
1 490 LYS n 
1 491 GLU n 
1 492 GLN n 
1 493 LYS n 
1 494 THR n 
1 495 ASP n 
1 496 TYR n 
1 497 LEU n 
1 498 VAL n 
1 499 PRO n 
1 500 GLU n 
1 501 LYS n 
1 502 ASP n 
1 503 TYR n 
1 504 THR n 
1 505 LYS n 
1 506 PHE n 
1 507 SER n 
1 508 TYR n 
1 509 GLU n 
1 510 PHE n 
1 511 GLU n 
1 512 THR n 
1 513 THR n 
1 514 GLY n 
1 515 LYS n 
1 516 ASP n 
1 517 SER n 
1 518 SER n 
1 519 ASP n 
1 520 ILE n 
1 521 GLU n 
1 522 ILE n 
1 523 THR n 
1 524 LEU n 
1 525 THR n 
1 526 SER n 
1 527 SER n 
1 528 GLY n 
1 529 VAL n 
1 530 ILE n 
1 531 PHE n 
1 532 LEU n 
1 533 ASP n 
1 534 ASN n 
1 535 LEU n 
1 536 SER n 
1 537 ILE n 
1 538 THR n 
1 539 GLU n 
1 540 LEU n 
1 541 ASN n 
1 542 SER n 
1 543 THR n 
1 544 PRO n 
1 545 GLU n 
1 546 ILE n 
1 547 LEU n 
1 548 LYS n 
1 549 GLU n 
1 550 PRO n 
1 551 GLU n 
1 552 ILE n 
1 553 LYS n 
1 554 VAL n 
1 555 PRO n 
1 556 SER n 
1 557 ASP n 
1 558 GLN n 
1 559 GLU n 
1 560 ILE n 
1 561 LEU n 
1 562 ASP n 
1 563 ALA n 
1 564 HIS n 
1 565 ASN n 
1 566 LYS n 
1 567 TYR n 
1 568 TYR n 
1 569 ALA n 
1 570 ASP n 
1 571 ILE n 
1 572 LYS n 
1 573 LEU n 
1 574 ASP n 
1 575 THR n 
1 576 ASN n 
1 577 THR n 
1 578 GLY n 
1 579 ASN n 
1 580 THR n 
1 581 TYR n 
1 582 ILE n 
1 583 ASP n 
1 584 GLY n 
1 585 ILE n 
1 586 TYR n 
1 587 PHE n 
1 588 GLU n 
1 589 PRO n 
1 590 THR n 
1 591 GLN n 
1 592 THR n 
1 593 ASN n 
1 594 LYS n 
1 595 GLU n 
1 596 ALA n 
1 597 LEU n 
1 598 ASP n 
1 599 TYR n 
1 600 ILE n 
1 601 GLN n 
1 602 LYS n 
1 603 TYR n 
1 604 ARG n 
1 605 VAL n 
1 606 GLU n 
1 607 ALA n 
1 608 THR n 
1 609 LEU n 
1 610 GLN n 
1 611 TYR n 
1 612 SER n 
1 613 GLY n 
1 614 PHE n 
1 615 LYS n 
1 616 ASP n 
1 617 ILE n 
1 618 GLY n 
1 619 THR n 
1 620 LYS n 
1 621 ASP n 
1 622 LYS n 
1 623 GLU n 
1 624 ILE n 
1 625 ARG n 
1 626 ASN n 
1 627 TYR n 
1 628 LEU n 
1 629 GLY n 
1 630 ASP n 
1 631 GLN n 
1 632 ASN n 
1 633 GLN n 
1 634 PRO n 
1 635 LYS n 
1 636 THR n 
1 637 ASN n 
1 638 TYR n 
1 639 ILE n 
1 640 ASN n 
1 641 PHE n 
1 642 ARG n 
1 643 SER n 
1 644 TYR n 
1 645 PHE n 
1 646 THR n 
1 647 SER n 
1 648 GLY n 
1 649 GLU n 
1 650 ASN n 
1 651 VAL n 
1 652 MET n 
1 653 THR n 
1 654 TYR n 
1 655 LYS n 
1 656 LYS n 
1 657 LEU n 
1 658 ARG n 
1 659 ILE n 
1 660 TYR n 
1 661 ALA n 
1 662 VAL n 
1 663 THR n 
1 664 PRO n 
1 665 ASP n 
1 666 ASN n 
1 667 ARG n 
1 668 GLU n 
1 669 LEU n 
1 670 LEU n 
1 671 VAL n 
1 672 LEU n 
1 673 SER n 
1 674 VAL n 
1 675 ASN n 
1 676 LEU n 
1 677 GLU n 
1 678 HIS n 
1 679 HIS n 
1 680 HIS n 
1 681 HIS n 
1 682 HIS n 
1 683 HIS 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                   683 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'NCIB 10748' 
_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      'Clostridium perfringens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1502 
_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(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                       pET23a 
_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  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASN 1   201 ?   ?   ?   A . n 
A 1 2   ASN 2   202 ?   ?   ?   A . n 
A 1 3   PHE 3   203 ?   ?   ?   A . n 
A 1 4   PHE 4   204 ?   ?   ?   A . n 
A 1 5   ASP 5   205 ?   ?   ?   A . n 
A 1 6   VAL 6   206 ?   ?   ?   A . n 
A 1 7   ARG 7   207 ?   ?   ?   A . n 
A 1 8   PHE 8   208 ?   ?   ?   A . n 
A 1 9   PHE 9   209 ?   ?   ?   A . n 
A 1 10  SER 10  210 ?   ?   ?   A . n 
A 1 11  ALA 11  211 ?   ?   ?   A . n 
A 1 12  ALA 12  212 ?   ?   ?   A . n 
A 1 13  TRP 13  213 ?   ?   ?   A . n 
A 1 14  GLU 14  214 ?   ?   ?   A . n 
A 1 15  ASP 15  215 ?   ?   ?   A . n 
A 1 16  GLU 16  216 216 GLU GLU A . n 
A 1 17  ASP 17  217 217 ASP ASP A . n 
A 1 18  LEU 18  218 218 LEU LEU A . n 
A 1 19  ASP 19  219 219 ASP ASP A . n 
A 1 20  THR 20  220 220 THR THR A . n 
A 1 21  ASP 21  221 221 ASP ASP A . n 
A 1 22  ASN 22  222 222 ASN ASN A . n 
A 1 23  ASP 23  223 223 ASP ASP A . n 
A 1 24  ASN 24  224 224 ASN ASN A . n 
A 1 25  ILE 25  225 225 ILE ILE A . n 
A 1 26  PRO 26  226 226 PRO PRO A . n 
A 1 27  ASP 27  227 227 ASP ASP A . n 
A 1 28  ALA 28  228 228 ALA ALA A . n 
A 1 29  TYR 29  229 229 TYR TYR A . n 
A 1 30  GLU 30  230 230 GLU GLU A . n 
A 1 31  LYS 31  231 231 LYS LYS A . n 
A 1 32  ASN 32  232 232 ASN ASN A . n 
A 1 33  GLY 33  233 233 GLY GLY A . n 
A 1 34  TYR 34  234 234 TYR TYR A . n 
A 1 35  THR 35  235 235 THR THR A . n 
A 1 36  ILE 36  236 236 ILE ILE A . n 
A 1 37  LYS 37  237 237 LYS LYS A . n 
A 1 38  ASP 38  238 238 ASP ASP A . n 
A 1 39  SER 39  239 239 SER SER A . n 
A 1 40  ILE 40  240 240 ILE ILE A . n 
A 1 41  ALA 41  241 241 ALA ALA A . n 
A 1 42  VAL 42  242 242 VAL VAL A . n 
A 1 43  LYS 43  243 243 LYS LYS A . n 
A 1 44  TRP 44  244 244 TRP TRP A . n 
A 1 45  ASN 45  245 245 ASN ASN A . n 
A 1 46  ASP 46  246 246 ASP ASP A . n 
A 1 47  SER 47  247 247 SER SER A . n 
A 1 48  PHE 48  248 248 PHE PHE A . n 
A 1 49  ALA 49  249 249 ALA ALA A . n 
A 1 50  GLU 50  250 250 GLU GLU A . n 
A 1 51  GLN 51  251 251 GLN GLN A . n 
A 1 52  GLY 52  252 252 GLY GLY A . n 
A 1 53  TYR 53  253 253 TYR TYR A . n 
A 1 54  LYS 54  254 254 LYS LYS A . n 
A 1 55  LYS 55  255 255 LYS LYS A . n 
A 1 56  TYR 56  256 256 TYR TYR A . n 
A 1 57  VAL 57  257 257 VAL VAL A . n 
A 1 58  SER 58  258 258 SER SER A . n 
A 1 59  SER 59  259 259 SER SER A . n 
A 1 60  TYR 60  260 260 TYR TYR A . n 
A 1 61  LEU 61  261 261 LEU LEU A . n 
A 1 62  GLU 62  262 262 GLU GLU A . n 
A 1 63  SER 63  263 263 SER SER A . n 
A 1 64  ASN 64  264 264 ASN ASN A . n 
A 1 65  THR 65  265 265 THR THR A . n 
A 1 66  ALA 66  266 266 ALA ALA A . n 
A 1 67  GLY 67  267 267 GLY GLY A . n 
A 1 68  ASP 68  268 268 ASP ASP A . n 
A 1 69  PRO 69  269 269 PRO PRO A . n 
A 1 70  TYR 70  270 270 TYR TYR A . n 
A 1 71  THR 71  271 271 THR THR A . n 
A 1 72  ASP 72  272 272 ASP ASP A . n 
A 1 73  TYR 73  273 273 TYR TYR A . n 
A 1 74  GLN 74  274 274 GLN GLN A . n 
A 1 75  LYS 75  275 275 LYS LYS A . n 
A 1 76  ALA 76  276 276 ALA ALA A . n 
A 1 77  SER 77  277 277 SER SER A . n 
A 1 78  GLY 78  278 278 GLY GLY A . n 
A 1 79  SER 79  279 279 SER SER A . n 
A 1 80  ILE 80  280 280 ILE ILE A . n 
A 1 81  ASP 81  281 281 ASP ASP A . n 
A 1 82  LYS 82  282 282 LYS LYS A . n 
A 1 83  ALA 83  283 283 ALA ALA A . n 
A 1 84  ILE 84  284 284 ILE ILE A . n 
A 1 85  LYS 85  285 285 LYS LYS A . n 
A 1 86  LEU 86  286 286 LEU LEU A . n 
A 1 87  GLU 87  287 287 GLU GLU A . n 
A 1 88  ALA 88  288 288 ALA ALA A . n 
A 1 89  ARG 89  289 289 ARG ARG A . n 
A 1 90  ASP 90  290 290 ASP ASP A . n 
A 1 91  PRO 91  291 291 PRO PRO A . n 
A 1 92  LEU 92  292 292 LEU LEU A . n 
A 1 93  VAL 93  293 293 VAL VAL A . n 
A 1 94  ALA 94  294 294 ALA ALA A . n 
A 1 95  ALA 95  295 295 ALA ALA A . n 
A 1 96  TYR 96  296 296 TYR TYR A . n 
A 1 97  PRO 97  297 297 PRO PRO A . n 
A 1 98  VAL 98  298 298 VAL VAL A . n 
A 1 99  VAL 99  299 299 VAL VAL A . n 
A 1 100 GLY 100 300 300 GLY GLY A . n 
A 1 101 VAL 101 301 301 VAL VAL A . n 
A 1 102 GLY 102 302 302 GLY GLY A . n 
A 1 103 MET 103 303 303 MET MET A . n 
A 1 104 GLU 104 304 304 GLU GLU A . n 
A 1 105 ASN 105 305 305 ASN ASN A . n 
A 1 106 LEU 106 306 306 LEU LEU A . n 
A 1 107 ILE 107 307 307 ILE ILE A . n 
A 1 108 ILE 108 308 308 ILE ILE A . n 
A 1 109 SER 109 309 309 SER SER A . n 
A 1 110 THR 110 310 310 THR THR A . n 
A 1 111 ASN 111 311 311 ASN ASN A . n 
A 1 112 GLU 112 312 312 GLU GLU A . n 
A 1 113 HIS 113 313 313 HIS HIS A . n 
A 1 114 ALA 114 314 314 ALA ALA A . n 
A 1 115 SER 115 315 315 SER SER A . n 
A 1 116 SER 116 316 316 SER SER A . n 
A 1 117 ASP 117 317 317 ASP ASP A . n 
A 1 118 GLN 118 318 318 GLN GLN A . n 
A 1 119 GLY 119 319 319 GLY GLY A . n 
A 1 120 LYS 120 320 320 LYS LYS A . n 
A 1 121 THR 121 321 321 THR THR A . n 
A 1 122 VAL 122 322 322 VAL VAL A . n 
A 1 123 SER 123 323 323 SER SER A . n 
A 1 124 ARG 124 324 324 ARG ARG A . n 
A 1 125 ALA 125 325 325 ALA ALA A . n 
A 1 126 THR 126 326 326 THR THR A . n 
A 1 127 THR 127 327 327 THR THR A . n 
A 1 128 ASN 128 328 328 ASN ASN A . n 
A 1 129 SER 129 329 329 SER SER A . n 
A 1 130 LYS 130 330 330 LYS LYS A . n 
A 1 131 THR 131 331 331 THR THR A . n 
A 1 132 ASP 132 332 332 ASP ASP A . n 
A 1 133 ALA 133 333 333 ALA ALA A . n 
A 1 134 ASN 134 334 334 ASN ASN A . n 
A 1 135 THR 135 335 335 THR THR A . n 
A 1 136 VAL 136 336 336 VAL VAL A . n 
A 1 137 GLY 137 337 337 GLY GLY A . n 
A 1 138 VAL 138 338 338 VAL VAL A . n 
A 1 139 SER 139 339 339 SER SER A . n 
A 1 140 ILE 140 340 340 ILE ILE A . n 
A 1 141 SER 141 341 341 SER SER A . n 
A 1 142 ALA 142 342 342 ALA ALA A . n 
A 1 143 GLY 143 343 343 GLY GLY A . n 
A 1 144 TYR 144 344 344 TYR TYR A . n 
A 1 145 GLN 145 345 345 GLN GLN A . n 
A 1 146 ASN 146 346 346 ASN ASN A . n 
A 1 147 GLY 147 347 347 GLY GLY A . n 
A 1 148 PHE 148 348 348 PHE PHE A . n 
A 1 149 THR 149 349 349 THR THR A . n 
A 1 150 GLY 150 350 350 GLY GLY A . n 
A 1 151 ASN 151 351 351 ASN ASN A . n 
A 1 152 ILE 152 352 352 ILE ILE A . n 
A 1 153 THR 153 353 353 THR THR A . n 
A 1 154 THR 154 354 354 THR THR A . n 
A 1 155 SER 155 355 355 SER SER A . n 
A 1 156 TYR 156 356 356 TYR TYR A . n 
A 1 157 SER 157 357 357 SER SER A . n 
A 1 158 HIS 158 358 358 HIS HIS A . n 
A 1 159 THR 159 359 359 THR THR A . n 
A 1 160 THR 160 360 360 THR THR A . n 
A 1 161 ASP 161 361 361 ASP ASP A . n 
A 1 162 ASN 162 362 362 ASN ASN A . n 
A 1 163 SER 163 363 363 SER SER A . n 
A 1 164 THR 164 364 364 THR THR A . n 
A 1 165 ALA 165 365 365 ALA ALA A . n 
A 1 166 VAL 166 366 366 VAL VAL A . n 
A 1 167 GLN 167 367 367 GLN GLN A . n 
A 1 168 ASP 168 368 368 ASP ASP A . n 
A 1 169 SER 169 369 369 SER SER A . n 
A 1 170 ASN 170 370 370 ASN ASN A . n 
A 1 171 GLY 171 371 371 GLY GLY A . n 
A 1 172 GLU 172 372 372 GLU GLU A . n 
A 1 173 SER 173 373 373 SER SER A . n 
A 1 174 TRP 174 374 374 TRP TRP A . n 
A 1 175 ASN 175 375 375 ASN ASN A . n 
A 1 176 THR 176 376 376 THR THR A . n 
A 1 177 GLY 177 377 377 GLY GLY A . n 
A 1 178 LEU 178 378 378 LEU LEU A . n 
A 1 179 SER 179 379 379 SER SER A . n 
A 1 180 ILE 180 380 380 ILE ILE A . n 
A 1 181 ASN 181 381 381 ASN ASN A . n 
A 1 182 LYS 182 382 382 LYS LYS A . n 
A 1 183 GLY 183 383 383 GLY GLY A . n 
A 1 184 GLU 184 384 384 GLU GLU A . n 
A 1 185 SER 185 385 385 SER SER A . n 
A 1 186 ALA 186 386 386 ALA ALA A . n 
A 1 187 TYR 187 387 387 TYR TYR A . n 
A 1 188 ILE 188 388 388 ILE ILE A . n 
A 1 189 ASN 189 389 389 ASN ASN A . n 
A 1 190 ALA 190 390 390 ALA ALA A . n 
A 1 191 ASN 191 391 391 ASN ASN A . n 
A 1 192 VAL 192 392 392 VAL VAL A . n 
A 1 193 ARG 193 393 393 ARG ARG A . n 
A 1 194 TYR 194 394 394 TYR TYR A . n 
A 1 195 TYR 195 395 395 TYR TYR A . n 
A 1 196 ASN 196 396 396 ASN ASN A . n 
A 1 197 THR 197 397 397 THR THR A . n 
A 1 198 GLY 198 398 398 GLY GLY A . n 
A 1 199 THR 199 399 399 THR THR A . n 
A 1 200 ALA 200 400 400 ALA ALA A . n 
A 1 201 PRO 201 401 401 PRO PRO A . n 
A 1 202 MET 202 402 402 MET MET A . n 
A 1 203 TYR 203 403 403 TYR TYR A . n 
A 1 204 LYS 204 404 404 LYS LYS A . n 
A 1 205 VAL 205 405 405 VAL VAL A . n 
A 1 206 THR 206 406 406 THR THR A . n 
A 1 207 PRO 207 407 407 PRO PRO A . n 
A 1 208 THR 208 408 408 THR THR A . n 
A 1 209 THR 209 409 409 THR THR A . n 
A 1 210 ASN 210 410 410 ASN ASN A . n 
A 1 211 LEU 211 411 411 LEU LEU A . n 
A 1 212 VAL 212 412 412 VAL VAL A . n 
A 1 213 LEU 213 413 413 LEU LEU A . n 
A 1 214 ASP 214 414 414 ASP ASP A . n 
A 1 215 GLY 215 415 415 GLY GLY A . n 
A 1 216 GLU 216 416 416 GLU GLU A . n 
A 1 217 THR 217 417 417 THR THR A . n 
A 1 218 LEU 218 418 418 LEU LEU A . n 
A 1 219 ALA 219 419 419 ALA ALA A . n 
A 1 220 THR 220 420 420 THR THR A . n 
A 1 221 ILE 221 421 421 ILE ILE A . n 
A 1 222 LYS 222 422 422 LYS LYS A . n 
A 1 223 ALA 223 423 423 ALA ALA A . n 
A 1 224 GLN 224 424 424 GLN GLN A . n 
A 1 225 ASP 225 425 425 ASP ASP A . n 
A 1 226 ASN 226 426 426 ASN ASN A . n 
A 1 227 GLN 227 427 427 GLN GLN A . n 
A 1 228 ILE 228 428 428 ILE ILE A . n 
A 1 229 GLY 229 429 429 GLY GLY A . n 
A 1 230 ASN 230 430 430 ASN ASN A . n 
A 1 231 ASN 231 431 431 ASN ASN A . n 
A 1 232 LEU 232 432 432 LEU LEU A . n 
A 1 233 SER 233 433 433 SER SER A . n 
A 1 234 PRO 234 434 434 PRO PRO A . n 
A 1 235 ASN 235 435 435 ASN ASN A . n 
A 1 236 GLU 236 436 436 GLU GLU A . n 
A 1 237 THR 237 437 437 THR THR A . n 
A 1 238 TYR 238 438 438 TYR TYR A . n 
A 1 239 PRO 239 439 439 PRO PRO A . n 
A 1 240 LYS 240 440 440 LYS LYS A . n 
A 1 241 LYS 241 441 441 LYS LYS A . n 
A 1 242 GLY 242 442 442 GLY GLY A . n 
A 1 243 LEU 243 443 443 LEU LEU A . n 
A 1 244 SER 244 444 444 SER SER A . n 
A 1 245 PRO 245 445 445 PRO PRO A . n 
A 1 246 LEU 246 446 446 LEU LEU A . n 
A 1 247 ALA 247 447 447 ALA ALA A . n 
A 1 248 LEU 248 448 448 LEU LEU A . n 
A 1 249 ASN 249 449 449 ASN ASN A . n 
A 1 250 THR 250 450 450 THR THR A . n 
A 1 251 MET 251 451 451 MET MET A . n 
A 1 252 ASP 252 452 452 ASP ASP A . n 
A 1 253 GLN 253 453 453 GLN GLN A . n 
A 1 254 PHE 254 454 454 PHE PHE A . n 
A 1 255 ASN 255 455 455 ASN ASN A . n 
A 1 256 ALA 256 456 456 ALA ALA A . n 
A 1 257 ARG 257 457 457 ARG ARG A . n 
A 1 258 LEU 258 458 458 LEU LEU A . n 
A 1 259 ILE 259 459 459 ILE ILE A . n 
A 1 260 PRO 260 460 460 PRO PRO A . n 
A 1 261 ILE 261 461 461 ILE ILE A . n 
A 1 262 ASN 262 462 462 ASN ASN A . n 
A 1 263 TYR 263 463 463 TYR TYR A . n 
A 1 264 ASP 264 464 464 ASP ASP A . n 
A 1 265 GLN 265 465 465 GLN GLN A . n 
A 1 266 LEU 266 466 466 LEU LEU A . n 
A 1 267 LYS 267 467 467 LYS LYS A . n 
A 1 268 LYS 268 468 468 LYS LYS A . n 
A 1 269 LEU 269 469 469 LEU LEU A . n 
A 1 270 ASP 270 470 470 ASP ASP A . n 
A 1 271 SER 271 471 471 SER SER A . n 
A 1 272 GLY 272 472 472 GLY GLY A . n 
A 1 273 LYS 273 473 473 LYS LYS A . n 
A 1 274 GLN 274 474 474 GLN GLN A . n 
A 1 275 ILE 275 475 475 ILE ILE A . n 
A 1 276 LYS 276 476 476 LYS LYS A . n 
A 1 277 LEU 277 477 477 LEU LEU A . n 
A 1 278 GLU 278 478 478 GLU GLU A . n 
A 1 279 THR 279 479 479 THR THR A . n 
A 1 280 THR 280 480 480 THR THR A . n 
A 1 281 GLN 281 481 481 GLN GLN A . n 
A 1 282 VAL 282 482 482 VAL VAL A . n 
A 1 283 SER 283 483 483 SER SER A . n 
A 1 284 GLY 284 484 484 GLY GLY A . n 
A 1 285 ASN 285 485 485 ASN ASN A . n 
A 1 286 TYR 286 486 486 TYR TYR A . n 
A 1 287 GLY 287 487 487 GLY GLY A . n 
A 1 288 THR 288 488 488 THR THR A . n 
A 1 289 LYS 289 489 489 LYS LYS A . n 
A 1 290 ASN 290 490 490 ASN ASN A . n 
A 1 291 SER 291 491 491 SER SER A . n 
A 1 292 GLN 292 492 492 GLN GLN A . n 
A 1 293 GLY 293 493 493 GLY GLY A . n 
A 1 294 GLN 294 494 494 GLN GLN A . n 
A 1 295 ILE 295 495 495 ILE ILE A . n 
A 1 296 ILE 296 496 496 ILE ILE A . n 
A 1 297 THR 297 497 497 THR THR A . n 
A 1 298 GLU 298 498 498 GLU GLU A . n 
A 1 299 GLY 299 499 499 GLY GLY A . n 
A 1 300 ASN 300 500 500 ASN ASN A . n 
A 1 301 SER 301 501 501 SER SER A . n 
A 1 302 TRP 302 502 502 TRP TRP A . n 
A 1 303 SER 303 503 503 SER SER A . n 
A 1 304 ASN 304 504 504 ASN ASN A . n 
A 1 305 TYR 305 505 505 TYR TYR A . n 
A 1 306 ILE 306 506 506 ILE ILE A . n 
A 1 307 SER 307 507 507 SER SER A . n 
A 1 308 GLN 308 508 508 GLN GLN A . n 
A 1 309 ILE 309 509 509 ILE ILE A . n 
A 1 310 ASP 310 510 510 ASP ASP A . n 
A 1 311 SER 311 511 511 SER SER A . n 
A 1 312 VAL 312 512 512 VAL VAL A . n 
A 1 313 SER 313 513 513 SER SER A . n 
A 1 314 ALA 314 514 514 ALA ALA A . n 
A 1 315 SER 315 515 515 SER SER A . n 
A 1 316 ILE 316 516 516 ILE ILE A . n 
A 1 317 ILE 317 517 517 ILE ILE A . n 
A 1 318 LEU 318 518 518 LEU LEU A . n 
A 1 319 ASP 319 519 519 ASP ASP A . n 
A 1 320 THR 320 520 520 THR THR A . n 
A 1 321 GLY 321 521 521 GLY GLY A . n 
A 1 322 SER 322 522 522 SER SER A . n 
A 1 323 GLN 323 523 523 GLN GLN A . n 
A 1 324 THR 324 524 524 THR THR A . n 
A 1 325 PHE 325 525 525 PHE PHE A . n 
A 1 326 GLU 326 526 526 GLU GLU A . n 
A 1 327 ARG 327 527 527 ARG ARG A . n 
A 1 328 ARG 328 528 528 ARG ARG A . n 
A 1 329 VAL 329 529 529 VAL VAL A . n 
A 1 330 ALA 330 530 530 ALA ALA A . n 
A 1 331 ALA 331 531 531 ALA ALA A . n 
A 1 332 LYS 332 532 532 LYS LYS A . n 
A 1 333 GLU 333 533 533 GLU GLU A . n 
A 1 334 GLN 334 534 534 GLN GLN A . n 
A 1 335 GLY 335 535 535 GLY GLY A . n 
A 1 336 ASN 336 536 536 ASN ASN A . n 
A 1 337 PRO 337 537 537 PRO PRO A . n 
A 1 338 GLU 338 538 538 GLU GLU A . n 
A 1 339 ASP 339 539 539 ASP ASP A . n 
A 1 340 LYS 340 540 540 LYS LYS A . n 
A 1 341 THR 341 541 541 THR THR A . n 
A 1 342 PRO 342 542 542 PRO PRO A . n 
A 1 343 GLU 343 543 543 GLU GLU A . n 
A 1 344 ILE 344 544 544 ILE ILE A . n 
A 1 345 THR 345 545 545 THR THR A . n 
A 1 346 ILE 346 546 546 ILE ILE A . n 
A 1 347 GLY 347 547 547 GLY GLY A . n 
A 1 348 GLU 348 548 548 GLU GLU A . n 
A 1 349 ALA 349 549 549 ALA ALA A . n 
A 1 350 ILE 350 550 550 ILE ILE A . n 
A 1 351 LYS 351 551 551 LYS LYS A . n 
A 1 352 LYS 352 552 552 LYS LYS A . n 
A 1 353 ALA 353 553 553 ALA ALA A . n 
A 1 354 PHE 354 554 554 PHE PHE A . n 
A 1 355 SER 355 555 555 SER SER A . n 
A 1 356 ALA 356 556 556 ALA ALA A . n 
A 1 357 THR 357 557 557 THR THR A . n 
A 1 358 LYS 358 558 558 LYS LYS A . n 
A 1 359 ASN 359 559 559 ASN ASN A . n 
A 1 360 GLY 360 560 560 GLY GLY A . n 
A 1 361 GLU 361 561 561 GLU GLU A . n 
A 1 362 LEU 362 562 562 LEU LEU A . n 
A 1 363 LEU 363 563 563 LEU LEU A . n 
A 1 364 TYR 364 564 564 TYR TYR A . n 
A 1 365 PHE 365 565 565 PHE PHE A . n 
A 1 366 ASN 366 566 566 ASN ASN A . n 
A 1 367 GLY 367 567 567 GLY GLY A . n 
A 1 368 ILE 368 568 568 ILE ILE A . n 
A 1 369 PRO 369 569 569 PRO PRO A . n 
A 1 370 ILE 370 570 570 ILE ILE A . n 
A 1 371 ASP 371 571 571 ASP ASP A . n 
A 1 372 GLU 372 572 572 GLU GLU A . n 
A 1 373 SER 373 573 573 SER SER A . n 
A 1 374 CYS 374 574 574 CYS CYS A . n 
A 1 375 VAL 375 575 575 VAL VAL A . n 
A 1 376 GLU 376 576 576 GLU GLU A . n 
A 1 377 LEU 377 577 577 LEU LEU A . n 
A 1 378 ILE 378 578 578 ILE ILE A . n 
A 1 379 PHE 379 579 579 PHE PHE A . n 
A 1 380 ASP 380 580 580 ASP ASP A . n 
A 1 381 ASP 381 581 581 ASP ASP A . n 
A 1 382 ASN 382 582 582 ASN ASN A . n 
A 1 383 THR 383 583 583 THR THR A . n 
A 1 384 SER 384 584 584 SER SER A . n 
A 1 385 GLU 385 585 585 GLU GLU A . n 
A 1 386 ILE 386 586 586 ILE ILE A . n 
A 1 387 ILE 387 587 587 ILE ILE A . n 
A 1 388 LYS 388 588 588 LYS LYS A . n 
A 1 389 GLU 389 589 589 GLU GLU A . n 
A 1 390 GLN 390 590 590 GLN GLN A . n 
A 1 391 LEU 391 591 591 LEU LEU A . n 
A 1 392 LYS 392 592 592 LYS LYS A . n 
A 1 393 TYR 393 593 593 TYR TYR A . n 
A 1 394 LEU 394 594 594 LEU LEU A . n 
A 1 395 ASP 395 595 595 ASP ASP A . n 
A 1 396 ASP 396 596 596 ASP ASP A . n 
A 1 397 LYS 397 597 597 LYS LYS A . n 
A 1 398 LYS 398 598 598 LYS LYS A . n 
A 1 399 ILE 399 599 599 ILE ILE A . n 
A 1 400 TYR 400 600 600 TYR TYR A . n 
A 1 401 ASN 401 601 601 ASN ASN A . n 
A 1 402 VAL 402 602 602 VAL VAL A . n 
A 1 403 LYS 403 603 603 LYS LYS A . n 
A 1 404 LEU 404 604 604 LEU LEU A . n 
A 1 405 GLU 405 605 605 GLU GLU A . n 
A 1 406 ARG 406 606 606 ARG ARG A . n 
A 1 407 GLY 407 607 607 GLY GLY A . n 
A 1 408 MET 408 608 608 MET MET A . n 
A 1 409 ASN 409 609 609 ASN ASN A . n 
A 1 410 ILE 410 610 610 ILE ILE A . n 
A 1 411 LEU 411 611 611 LEU LEU A . n 
A 1 412 ILE 412 612 612 ILE ILE A . n 
A 1 413 LYS 413 613 613 LYS LYS A . n 
A 1 414 VAL 414 614 614 VAL VAL A . n 
A 1 415 PRO 415 615 615 PRO PRO A . n 
A 1 416 SER 416 616 616 SER SER A . n 
A 1 417 TYR 417 617 617 TYR TYR A . n 
A 1 418 PHE 418 618 618 PHE PHE A . n 
A 1 419 THR 419 619 619 THR THR A . n 
A 1 420 ASN 420 620 620 ASN ASN A . n 
A 1 421 PHE 421 621 621 PHE PHE A . n 
A 1 422 ASP 422 622 622 ASP ASP A . n 
A 1 423 GLU 423 623 623 GLU GLU A . n 
A 1 424 TYR 424 624 624 TYR TYR A . n 
A 1 425 ASN 425 625 625 ASN ASN A . n 
A 1 426 ASN 426 626 626 ASN ASN A . n 
A 1 427 PHE 427 627 627 PHE PHE A . n 
A 1 428 PRO 428 628 628 PRO PRO A . n 
A 1 429 ALA 429 629 629 ALA ALA A . n 
A 1 430 SER 430 630 630 SER SER A . n 
A 1 431 TRP 431 631 631 TRP TRP A . n 
A 1 432 SER 432 632 632 SER SER A . n 
A 1 433 ASN 433 633 633 ASN ASN A . n 
A 1 434 ILE 434 634 634 ILE ILE A . n 
A 1 435 ASP 435 635 635 ASP ASP A . n 
A 1 436 THR 436 636 636 THR THR A . n 
A 1 437 LYS 437 637 637 LYS LYS A . n 
A 1 438 ASN 438 638 638 ASN ASN A . n 
A 1 439 GLN 439 639 639 GLN GLN A . n 
A 1 440 ASP 440 640 640 ASP ASP A . n 
A 1 441 GLY 441 641 641 GLY GLY A . n 
A 1 442 LEU 442 642 642 LEU LEU A . n 
A 1 443 GLN 443 643 643 GLN GLN A . n 
A 1 444 SER 444 644 644 SER SER A . n 
A 1 445 VAL 445 645 645 VAL VAL A . n 
A 1 446 ALA 446 646 646 ALA ALA A . n 
A 1 447 ASN 447 647 647 ASN ASN A . n 
A 1 448 LYS 448 648 648 LYS LYS A . n 
A 1 449 LEU 449 649 649 LEU LEU A . n 
A 1 450 SER 450 650 650 SER SER A . n 
A 1 451 GLY 451 651 651 GLY GLY A . n 
A 1 452 GLU 452 652 652 GLU GLU A . n 
A 1 453 THR 453 653 653 THR THR A . n 
A 1 454 LYS 454 654 654 LYS LYS A . n 
A 1 455 ILE 455 655 655 ILE ILE A . n 
A 1 456 ILE 456 656 656 ILE ILE A . n 
A 1 457 ILE 457 657 657 ILE ILE A . n 
A 1 458 PRO 458 658 658 PRO PRO A . n 
A 1 459 MET 459 659 659 MET MET A . n 
A 1 460 SER 460 660 660 SER SER A . n 
A 1 461 LYS 461 661 661 LYS LYS A . n 
A 1 462 LEU 462 662 662 LEU LEU A . n 
A 1 463 LYS 463 663 663 LYS LYS A . n 
A 1 464 PRO 464 664 664 PRO PRO A . n 
A 1 465 TYR 465 665 665 TYR TYR A . n 
A 1 466 LYS 466 666 666 LYS LYS A . n 
A 1 467 ARG 467 667 667 ARG ARG A . n 
A 1 468 TYR 468 668 668 TYR TYR A . n 
A 1 469 VAL 469 669 669 VAL VAL A . n 
A 1 470 PHE 470 670 670 PHE PHE A . n 
A 1 471 SER 471 671 671 SER SER A . n 
A 1 472 GLY 472 672 672 GLY GLY A . n 
A 1 473 TYR 473 673 673 TYR TYR A . n 
A 1 474 SER 474 674 674 SER SER A . n 
A 1 475 LYS 475 675 675 LYS LYS A . n 
A 1 476 ASP 476 676 676 ASP ASP A . n 
A 1 477 PRO 477 677 677 PRO PRO A . n 
A 1 478 SER 478 678 678 SER SER A . n 
A 1 479 THR 479 679 679 THR THR A . n 
A 1 480 SER 480 680 680 SER SER A . n 
A 1 481 ASN 481 681 681 ASN ASN A . n 
A 1 482 SER 482 682 682 SER SER A . n 
A 1 483 ILE 483 683 683 ILE ILE A . n 
A 1 484 THR 484 684 684 THR THR A . n 
A 1 485 VAL 485 685 685 VAL VAL A . n 
A 1 486 ASN 486 686 686 ASN ASN A . n 
A 1 487 ILE 487 687 687 ILE ILE A . n 
A 1 488 LYS 488 688 688 LYS LYS A . n 
A 1 489 SER 489 689 689 SER SER A . n 
A 1 490 LYS 490 690 690 LYS LYS A . n 
A 1 491 GLU 491 691 691 GLU GLU A . n 
A 1 492 GLN 492 692 692 GLN GLN A . n 
A 1 493 LYS 493 693 693 LYS LYS A . n 
A 1 494 THR 494 694 694 THR THR A . n 
A 1 495 ASP 495 695 695 ASP ASP A . n 
A 1 496 TYR 496 696 696 TYR TYR A . n 
A 1 497 LEU 497 697 697 LEU LEU A . n 
A 1 498 VAL 498 698 698 VAL VAL A . n 
A 1 499 PRO 499 699 699 PRO PRO A . n 
A 1 500 GLU 500 700 700 GLU GLU A . n 
A 1 501 LYS 501 701 701 LYS LYS A . n 
A 1 502 ASP 502 702 702 ASP ASP A . n 
A 1 503 TYR 503 703 703 TYR TYR A . n 
A 1 504 THR 504 704 704 THR THR A . n 
A 1 505 LYS 505 705 705 LYS LYS A . n 
A 1 506 PHE 506 706 706 PHE PHE A . n 
A 1 507 SER 507 707 707 SER SER A . n 
A 1 508 TYR 508 708 708 TYR TYR A . n 
A 1 509 GLU 509 709 709 GLU GLU A . n 
A 1 510 PHE 510 710 710 PHE PHE A . n 
A 1 511 GLU 511 711 711 GLU GLU A . n 
A 1 512 THR 512 712 712 THR THR A . n 
A 1 513 THR 513 713 713 THR THR A . n 
A 1 514 GLY 514 714 714 GLY GLY A . n 
A 1 515 LYS 515 715 715 LYS LYS A . n 
A 1 516 ASP 516 716 716 ASP ASP A . n 
A 1 517 SER 517 717 717 SER SER A . n 
A 1 518 SER 518 718 718 SER SER A . n 
A 1 519 ASP 519 719 719 ASP ASP A . n 
A 1 520 ILE 520 720 720 ILE ILE A . n 
A 1 521 GLU 521 721 721 GLU GLU A . n 
A 1 522 ILE 522 722 722 ILE ILE A . n 
A 1 523 THR 523 723 723 THR THR A . n 
A 1 524 LEU 524 724 724 LEU LEU A . n 
A 1 525 THR 525 725 725 THR THR A . n 
A 1 526 SER 526 726 726 SER SER A . n 
A 1 527 SER 527 727 727 SER SER A . n 
A 1 528 GLY 528 728 728 GLY GLY A . n 
A 1 529 VAL 529 729 729 VAL VAL A . n 
A 1 530 ILE 530 730 730 ILE ILE A . n 
A 1 531 PHE 531 731 731 PHE PHE A . n 
A 1 532 LEU 532 732 732 LEU LEU A . n 
A 1 533 ASP 533 733 733 ASP ASP A . n 
A 1 534 ASN 534 734 734 ASN ASN A . n 
A 1 535 LEU 535 735 735 LEU LEU A . n 
A 1 536 SER 536 736 736 SER SER A . n 
A 1 537 ILE 537 737 737 ILE ILE A . n 
A 1 538 THR 538 738 738 THR THR A . n 
A 1 539 GLU 539 739 739 GLU GLU A . n 
A 1 540 LEU 540 740 740 LEU LEU A . n 
A 1 541 ASN 541 741 741 ASN ASN A . n 
A 1 542 SER 542 742 742 SER SER A . n 
A 1 543 THR 543 743 743 THR THR A . n 
A 1 544 PRO 544 744 744 PRO PRO A . n 
A 1 545 GLU 545 745 745 GLU GLU A . n 
A 1 546 ILE 546 746 ?   ?   ?   A . n 
A 1 547 LEU 547 747 ?   ?   ?   A . n 
A 1 548 LYS 548 748 ?   ?   ?   A . n 
A 1 549 GLU 549 749 ?   ?   ?   A . n 
A 1 550 PRO 550 750 ?   ?   ?   A . n 
A 1 551 GLU 551 751 ?   ?   ?   A . n 
A 1 552 ILE 552 752 ?   ?   ?   A . n 
A 1 553 LYS 553 753 ?   ?   ?   A . n 
A 1 554 VAL 554 754 ?   ?   ?   A . n 
A 1 555 PRO 555 755 ?   ?   ?   A . n 
A 1 556 SER 556 756 ?   ?   ?   A . n 
A 1 557 ASP 557 757 ?   ?   ?   A . n 
A 1 558 GLN 558 758 ?   ?   ?   A . n 
A 1 559 GLU 559 759 ?   ?   ?   A . n 
A 1 560 ILE 560 760 ?   ?   ?   A . n 
A 1 561 LEU 561 761 ?   ?   ?   A . n 
A 1 562 ASP 562 762 ?   ?   ?   A . n 
A 1 563 ALA 563 763 ?   ?   ?   A . n 
A 1 564 HIS 564 764 ?   ?   ?   A . n 
A 1 565 ASN 565 765 ?   ?   ?   A . n 
A 1 566 LYS 566 766 ?   ?   ?   A . n 
A 1 567 TYR 567 767 ?   ?   ?   A . n 
A 1 568 TYR 568 768 ?   ?   ?   A . n 
A 1 569 ALA 569 769 ?   ?   ?   A . n 
A 1 570 ASP 570 770 ?   ?   ?   A . n 
A 1 571 ILE 571 771 ?   ?   ?   A . n 
A 1 572 LYS 572 772 ?   ?   ?   A . n 
A 1 573 LEU 573 773 ?   ?   ?   A . n 
A 1 574 ASP 574 774 ?   ?   ?   A . n 
A 1 575 THR 575 775 ?   ?   ?   A . n 
A 1 576 ASN 576 776 ?   ?   ?   A . n 
A 1 577 THR 577 777 ?   ?   ?   A . n 
A 1 578 GLY 578 778 ?   ?   ?   A . n 
A 1 579 ASN 579 779 ?   ?   ?   A . n 
A 1 580 THR 580 780 ?   ?   ?   A . n 
A 1 581 TYR 581 781 ?   ?   ?   A . n 
A 1 582 ILE 582 782 ?   ?   ?   A . n 
A 1 583 ASP 583 783 ?   ?   ?   A . n 
A 1 584 GLY 584 784 ?   ?   ?   A . n 
A 1 585 ILE 585 785 ?   ?   ?   A . n 
A 1 586 TYR 586 786 ?   ?   ?   A . n 
A 1 587 PHE 587 787 ?   ?   ?   A . n 
A 1 588 GLU 588 788 ?   ?   ?   A . n 
A 1 589 PRO 589 789 ?   ?   ?   A . n 
A 1 590 THR 590 790 ?   ?   ?   A . n 
A 1 591 GLN 591 791 ?   ?   ?   A . n 
A 1 592 THR 592 792 ?   ?   ?   A . n 
A 1 593 ASN 593 793 ?   ?   ?   A . n 
A 1 594 LYS 594 794 ?   ?   ?   A . n 
A 1 595 GLU 595 795 ?   ?   ?   A . n 
A 1 596 ALA 596 796 ?   ?   ?   A . n 
A 1 597 LEU 597 797 ?   ?   ?   A . n 
A 1 598 ASP 598 798 ?   ?   ?   A . n 
A 1 599 TYR 599 799 ?   ?   ?   A . n 
A 1 600 ILE 600 800 ?   ?   ?   A . n 
A 1 601 GLN 601 801 ?   ?   ?   A . n 
A 1 602 LYS 602 802 ?   ?   ?   A . n 
A 1 603 TYR 603 803 ?   ?   ?   A . n 
A 1 604 ARG 604 804 ?   ?   ?   A . n 
A 1 605 VAL 605 805 ?   ?   ?   A . n 
A 1 606 GLU 606 806 ?   ?   ?   A . n 
A 1 607 ALA 607 807 ?   ?   ?   A . n 
A 1 608 THR 608 808 ?   ?   ?   A . n 
A 1 609 LEU 609 809 ?   ?   ?   A . n 
A 1 610 GLN 610 810 ?   ?   ?   A . n 
A 1 611 TYR 611 811 ?   ?   ?   A . n 
A 1 612 SER 612 812 ?   ?   ?   A . n 
A 1 613 GLY 613 813 ?   ?   ?   A . n 
A 1 614 PHE 614 814 ?   ?   ?   A . n 
A 1 615 LYS 615 815 ?   ?   ?   A . n 
A 1 616 ASP 616 816 ?   ?   ?   A . n 
A 1 617 ILE 617 817 ?   ?   ?   A . n 
A 1 618 GLY 618 818 ?   ?   ?   A . n 
A 1 619 THR 619 819 ?   ?   ?   A . n 
A 1 620 LYS 620 820 ?   ?   ?   A . n 
A 1 621 ASP 621 821 ?   ?   ?   A . n 
A 1 622 LYS 622 822 ?   ?   ?   A . n 
A 1 623 GLU 623 823 ?   ?   ?   A . n 
A 1 624 ILE 624 824 ?   ?   ?   A . n 
A 1 625 ARG 625 825 ?   ?   ?   A . n 
A 1 626 ASN 626 826 ?   ?   ?   A . n 
A 1 627 TYR 627 827 ?   ?   ?   A . n 
A 1 628 LEU 628 828 ?   ?   ?   A . n 
A 1 629 GLY 629 829 ?   ?   ?   A . n 
A 1 630 ASP 630 830 ?   ?   ?   A . n 
A 1 631 GLN 631 831 ?   ?   ?   A . n 
A 1 632 ASN 632 832 ?   ?   ?   A . n 
A 1 633 GLN 633 833 ?   ?   ?   A . n 
A 1 634 PRO 634 834 ?   ?   ?   A . n 
A 1 635 LYS 635 835 ?   ?   ?   A . n 
A 1 636 THR 636 836 ?   ?   ?   A . n 
A 1 637 ASN 637 837 ?   ?   ?   A . n 
A 1 638 TYR 638 838 ?   ?   ?   A . n 
A 1 639 ILE 639 839 ?   ?   ?   A . n 
A 1 640 ASN 640 840 ?   ?   ?   A . n 
A 1 641 PHE 641 841 ?   ?   ?   A . n 
A 1 642 ARG 642 842 ?   ?   ?   A . n 
A 1 643 SER 643 843 ?   ?   ?   A . n 
A 1 644 TYR 644 844 ?   ?   ?   A . n 
A 1 645 PHE 645 845 ?   ?   ?   A . n 
A 1 646 THR 646 846 ?   ?   ?   A . n 
A 1 647 SER 647 847 ?   ?   ?   A . n 
A 1 648 GLY 648 848 ?   ?   ?   A . n 
A 1 649 GLU 649 849 ?   ?   ?   A . n 
A 1 650 ASN 650 850 ?   ?   ?   A . n 
A 1 651 VAL 651 851 ?   ?   ?   A . n 
A 1 652 MET 652 852 ?   ?   ?   A . n 
A 1 653 THR 653 853 ?   ?   ?   A . n 
A 1 654 TYR 654 854 ?   ?   ?   A . n 
A 1 655 LYS 655 855 ?   ?   ?   A . n 
A 1 656 LYS 656 856 ?   ?   ?   A . n 
A 1 657 LEU 657 857 ?   ?   ?   A . n 
A 1 658 ARG 658 858 ?   ?   ?   A . n 
A 1 659 ILE 659 859 ?   ?   ?   A . n 
A 1 660 TYR 660 860 ?   ?   ?   A . n 
A 1 661 ALA 661 861 ?   ?   ?   A . n 
A 1 662 VAL 662 862 ?   ?   ?   A . n 
A 1 663 THR 663 863 ?   ?   ?   A . n 
A 1 664 PRO 664 864 ?   ?   ?   A . n 
A 1 665 ASP 665 865 ?   ?   ?   A . n 
A 1 666 ASN 666 866 ?   ?   ?   A . n 
A 1 667 ARG 667 867 ?   ?   ?   A . n 
A 1 668 GLU 668 868 ?   ?   ?   A . n 
A 1 669 LEU 669 869 ?   ?   ?   A . n 
A 1 670 LEU 670 870 ?   ?   ?   A . n 
A 1 671 VAL 671 871 ?   ?   ?   A . n 
A 1 672 LEU 672 872 ?   ?   ?   A . n 
A 1 673 SER 673 873 ?   ?   ?   A . n 
A 1 674 VAL 674 874 ?   ?   ?   A . n 
A 1 675 ASN 675 875 ?   ?   ?   A . n 
A 1 676 LEU 676 876 ?   ?   ?   A . n 
A 1 677 GLU 677 877 ?   ?   ?   A . n 
A 1 678 HIS 678 878 ?   ?   ?   A . n 
A 1 679 HIS 679 879 ?   ?   ?   A . n 
A 1 680 HIS 680 880 ?   ?   ?   A . n 
A 1 681 HIS 681 881 ?   ?   ?   A . n 
A 1 682 HIS 682 882 ?   ?   ?   A . n 
A 1 683 HIS 683 883 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CA 1 901 1 CA CA A . 
C 2 CA 1 902 2 CA CA A . 
D 2 CA 1 903 3 CA CA A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A TYR 229 ? OH  ? A TYR 29  OH  
2  1 Y 1 A TYR 234 ? OH  ? A TYR 34  OH  
3  1 Y 1 A TYR 253 ? OH  ? A TYR 53  OH  
4  1 Y 1 A TYR 256 ? OH  ? A TYR 56  OH  
5  1 Y 1 A TYR 260 ? OH  ? A TYR 60  OH  
6  1 Y 1 A TYR 270 ? OH  ? A TYR 70  OH  
7  1 Y 1 A TYR 273 ? OH  ? A TYR 73  OH  
8  1 Y 1 A ARG 289 ? NH1 ? A ARG 89  NH1 
9  1 Y 1 A ARG 289 ? NH2 ? A ARG 89  NH2 
10 1 Y 1 A TYR 296 ? OH  ? A TYR 96  OH  
11 1 Y 1 A ARG 324 ? NH1 ? A ARG 124 NH1 
12 1 Y 1 A ARG 324 ? NH2 ? A ARG 124 NH2 
13 1 Y 1 A TYR 344 ? OH  ? A TYR 144 OH  
14 1 Y 1 A TYR 356 ? OH  ? A TYR 156 OH  
15 1 Y 1 A TYR 387 ? OH  ? A TYR 187 OH  
16 1 Y 1 A ARG 393 ? NH1 ? A ARG 193 NH1 
17 1 Y 1 A ARG 393 ? NH2 ? A ARG 193 NH2 
18 1 Y 1 A TYR 394 ? OH  ? A TYR 194 OH  
19 1 Y 1 A TYR 395 ? OH  ? A TYR 195 OH  
20 1 Y 1 A TYR 403 ? OH  ? A TYR 203 OH  
21 1 Y 1 A TYR 438 ? OH  ? A TYR 238 OH  
22 1 Y 1 A ARG 457 ? NH1 ? A ARG 257 NH1 
23 1 Y 1 A ARG 457 ? NH2 ? A ARG 257 NH2 
24 1 Y 1 A TYR 463 ? OH  ? A TYR 263 OH  
25 1 Y 1 A TYR 486 ? OH  ? A TYR 286 OH  
26 1 Y 1 A TYR 505 ? OH  ? A TYR 305 OH  
27 1 Y 1 A ARG 527 ? NH1 ? A ARG 327 NH1 
28 1 Y 1 A ARG 527 ? NH2 ? A ARG 327 NH2 
29 1 Y 1 A ARG 528 ? NH1 ? A ARG 328 NH1 
30 1 Y 1 A ARG 528 ? NH2 ? A ARG 328 NH2 
31 1 Y 1 A TYR 564 ? OH  ? A TYR 364 OH  
32 1 Y 1 A TYR 593 ? OH  ? A TYR 393 OH  
33 1 Y 1 A TYR 600 ? OH  ? A TYR 400 OH  
34 1 Y 1 A ARG 606 ? NH1 ? A ARG 406 NH1 
35 1 Y 1 A ARG 606 ? NH2 ? A ARG 406 NH2 
36 1 Y 1 A TYR 617 ? OH  ? A TYR 417 OH  
37 1 Y 1 A TYR 624 ? OH  ? A TYR 424 OH  
38 1 Y 1 A TYR 665 ? OH  ? A TYR 465 OH  
39 1 Y 1 A ARG 667 ? NH1 ? A ARG 467 NH1 
40 1 Y 1 A ARG 667 ? NH2 ? A ARG 467 NH2 
41 1 Y 1 A TYR 668 ? OH  ? A TYR 468 OH  
42 1 Y 1 A TYR 673 ? OH  ? A TYR 473 OH  
43 1 Y 1 A TYR 696 ? OH  ? A TYR 496 OH  
44 1 Y 1 A TYR 703 ? OH  ? A TYR 503 OH  
45 1 Y 1 A TYR 708 ? OH  ? A TYR 508 OH  
# 
_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                   9JSG 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given    ? 1.000000  0.000000  0.000000 0.000000  1.000000  0.000000 0.000000 0.000000 1.000000 0.00000   0.00000   0.00000 
2 generate ? 0.623490  -0.781832 0.000000 0.781832  0.623490  0.000000 0.000000 0.000000 1.000000 135.57231 -47.43880 0.00000 
3 generate ? -0.222521 -0.974928 0.000000 0.974928  -0.222521 0.000000 0.000000 0.000000 1.000000 257.18939 28.97829  0.00000 
4 generate ? -0.900969 -0.433884 0.000000 0.433884  -0.900969 0.000000 0.000000 0.000000 1.000000 273.27115 171.70764 0.00000 
5 generate ? -0.900969 0.433884  0.000000 -0.433884 -0.900969 0.000000 0.000000 0.000000 1.000000 171.70764 273.27115 0.00000 
6 generate ? -0.222521 0.974928  0.000000 -0.974928 -0.222521 0.000000 0.000000 0.000000 1.000000 28.97829  257.18939 0.00000 
7 generate ? 0.623490  0.781832  0.000000 -0.781832 0.623490  0.000000 0.000000 0.000000 1.000000 -47.43880 135.57231 0.00000 
# 
_struct.entry_id                     9JSG 
_struct.title                        'Clostridium perfringens iota toxin pore Ib in pore state' 
_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        9JSG 
_struct_keywords.text            'Toxin, Prepore, Pre-pore, Pore, Translocation' 
_struct_keywords.pdbx_keywords   TOXIN 
# 
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 2 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q46221_CLOPF 
_struct_ref.pdbx_db_accession          Q46221 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NNFFDVRFFSAAWEDEDLDTDNDNIPDAYEKNGYTIKDSIAVKWNDSFAEQGYKKYVSSYLESNTAGDPYTDYQKASGSI
DKAIKLEARDPLVAAYPVVGVGMENLIISTNEHASSDQGKTVSRATTNSKTDANTVGVSISAGYQNGFTGNITTSYSHTT
DNSTAVQDSNGESWNTGLSINKGESAYINANVRYYNTGTAPMYKVTPTTNLVLDGETLATIKAQDNQIGNNLSPNETYPK
KGLSPLALNTMDQFNARLIPINYDQLKKLDSGKQIKLETTQVSGNYGTKNSQGQIITEGNSWSNYISQIDSVSASIILDT
GSQTFERRVAAKEQGNPEDKTPEITIGEAIKKAFSATKNGELLYFNGIPIDESCVELIFDDNTSEIIKEQLKYLDDKKIY
NVKLERGMNILIKVPSYFTNFDEYNNFPASWSNIDTKNQDGLQSVANKLSGETKIIIPMSKLKPYKRYVFSGYSKDPSTS
NSITVNIKSKEQKTDYLVPEKDYTKFSYEFETTGKDSSDIEITLTSSGVIFLDNLSITELNSTPEILKEPEIKVPSDQEI
LDAHNKYYADIKLDTNTGNTYIDGIYFEPTQTNKEALDYIQKYRVEATLQYSGFKDIGTKDKEIRNYLGDQNQPKTNYIN
FRSYFTSGENVMTYKKLRIYAVTPDNRELLVLSVN
;
_struct_ref.pdbx_align_begin           201 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JSG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 675 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q46221 
_struct_ref_seq.db_align_beg                  201 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  875 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       201 
_struct_ref_seq.pdbx_auth_seq_align_end       875 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JSG LEU A 676 ? UNP Q46221 ? ? 'expression tag' 876 1 
1 9JSG GLU A 677 ? UNP Q46221 ? ? 'expression tag' 877 2 
1 9JSG HIS A 678 ? UNP Q46221 ? ? 'expression tag' 878 3 
1 9JSG HIS A 679 ? UNP Q46221 ? ? 'expression tag' 879 4 
1 9JSG HIS A 680 ? UNP Q46221 ? ? 'expression tag' 880 5 
1 9JSG HIS A 681 ? UNP Q46221 ? ? 'expression tag' 881 6 
1 9JSG HIS A 682 ? UNP Q46221 ? ? 'expression tag' 882 7 
1 9JSG HIS A 683 ? UNP Q46221 ? ? 'expression tag' 883 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D 
1 2 A,B,C,D 
1 3 A,B,C,D 
1 4 A,B,C,D 
1 5 A,B,C,D 
1 6 A,B,C,D 
1 7 A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'       1_555 x,y,z 1.0       0.0       0.0       0.0       0.0       1.0       0.0       0.0       0.0      
0.0       1.0      0.0      
2 'point symmetry operation' ?     ?     0.624122  -0.781327 -0.000175 135.48299 0.781327  0.624122  0.000032  -47.51727 0.000084 
-0.000157 1.000000 0.03192  
3 'point symmetry operation' ?     ?     -0.222292 -0.974980 0.000019  257.17497 0.974980  -0.222292 -0.000043 28.97494  0.000046 
0.000009  1.000000 0.00580  
4 'point symmetry operation' ?     ?     -0.900814 -0.434205 0.000074  273.29890 0.434205  -0.900814 -0.000169 171.66445 0.000140 
-0.000120 1.000000 -0.00176 
5 'point symmetry operation' ?     ?     -0.900909 0.434008  0.000160  171.69103 -0.434008 -0.900909 0.000145  273.28075 0.000207 
0.000061  1.000000 -0.00940 
6 'point symmetry operation' ?     ?     -0.222602 0.974909  0.000179  28.97282  -0.974909 -0.222602 0.000100  257.19623 0.000138 
-0.000152 1.000000 0.01148  
7 'point symmetry operation' ?     ?     0.623464  0.781852  0.000079  -47.49351 -0.781852 0.623464  0.000158  135.60687 0.000074 
-0.000161 1.000000 0.02242  
# 
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 PRO A 26  ? ASN A 32  ? PRO A 226 ASN A 232 1 ? 7  
HELX_P HELX_P2  AA2 ASN A 45  ? GLY A 52  ? ASN A 245 GLY A 252 5 ? 8  
HELX_P HELX_P3  AA3 THR A 71  ? GLY A 78  ? THR A 271 GLY A 278 1 ? 8  
HELX_P HELX_P4  AA4 LYS A 85  ? ASP A 90  ? LYS A 285 ASP A 290 5 ? 6  
HELX_P HELX_P5  AA5 GLN A 224 ? ILE A 228 ? GLN A 424 ILE A 428 5 ? 5  
HELX_P HELX_P6  AA6 ASN A 262 ? SER A 271 ? ASN A 462 SER A 471 1 ? 10 
HELX_P HELX_P7  AA7 TRP A 302 ? VAL A 312 ? TRP A 502 VAL A 512 1 ? 11 
HELX_P HELX_P8  AA8 THR A 345 ? SER A 355 ? THR A 545 SER A 555 1 ? 11 
HELX_P HELX_P9  AA9 ASP A 380 ? LYS A 392 ? ASP A 580 LYS A 592 1 ? 13 
HELX_P HELX_P10 AB1 LYS A 398 ? VAL A 402 ? LYS A 598 VAL A 602 5 ? 5  
HELX_P HELX_P11 AB2 PRO A 458 ? LEU A 462 ? PRO A 658 LEU A 662 5 ? 5  
# 
_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 ASP 19  OD1 ? ? ? 1_555 C CA . CA ? ? A ASP 219 A CA 902 1_555 ? ? ? ? ? ? ? 2.532 ? ? 
metalc2  metalc ? ? A ASP 21  OD2 ? ? ? 1_555 B CA . CA ? ? A ASP 221 A CA 901 1_555 ? ? ? ? ? ? ? 2.566 ? ? 
metalc3  metalc ? ? A ASP 21  OD1 ? ? ? 1_555 C CA . CA ? ? A ASP 221 A CA 902 1_555 ? ? ? ? ? ? ? 2.450 ? ? 
metalc4  metalc ? ? A ASP 23  OD2 ? ? ? 1_555 B CA . CA ? ? A ASP 223 A CA 901 1_555 ? ? ? ? ? ? ? 2.673 ? ? 
metalc5  metalc ? ? A ASP 23  OD1 ? ? ? 1_555 C CA . CA ? ? A ASP 223 A CA 902 1_555 ? ? ? ? ? ? ? 2.695 ? ? 
metalc6  metalc ? ? A ILE 25  O   ? ? ? 1_555 C CA . CA ? ? A ILE 225 A CA 902 1_555 ? ? ? ? ? ? ? 2.474 ? ? 
metalc7  metalc ? ? A ASP 27  OD1 ? ? ? 1_555 C CA . CA ? ? A ASP 227 A CA 902 1_555 ? ? ? ? ? ? ? 2.853 ? ? 
metalc8  metalc ? ? A GLU 30  OE1 ? ? ? 1_555 B CA . CA ? ? A GLU 230 A CA 901 1_555 ? ? ? ? ? ? ? 2.544 ? ? 
metalc9  metalc ? ? A GLU 30  OE2 ? ? ? 1_555 B CA . CA ? ? A GLU 230 A CA 901 1_555 ? ? ? ? ? ? ? 2.892 ? ? 
metalc10 metalc ? ? A GLU 30  OE2 ? ? ? 1_555 C CA . CA ? ? A GLU 230 A CA 902 1_555 ? ? ? ? ? ? ? 2.465 ? ? 
metalc11 metalc ? ? A SER 59  O   ? ? ? 1_555 B CA . CA ? ? A SER 259 A CA 901 1_555 ? ? ? ? ? ? ? 2.515 ? ? 
metalc12 metalc ? ? A GLU 62  O   ? ? ? 1_555 B CA . CA ? ? A GLU 262 A CA 901 1_555 ? ? ? ? ? ? ? 2.499 ? ? 
metalc13 metalc ? ? A ASP 72  OD2 ? ? ? 1_555 B CA . CA ? ? A ASP 272 A CA 901 1_555 ? ? ? ? ? ? ? 2.634 ? ? 
metalc14 metalc ? ? A ASN 420 O   ? ? ? 1_555 D CA . CA ? ? A ASN 620 A CA 903 1_555 ? ? ? ? ? ? ? 2.591 ? ? 
metalc15 metalc ? ? A ASP 422 OD2 ? ? ? 1_555 D CA . CA ? ? A ASP 622 A CA 903 1_555 ? ? ? ? ? ? ? 2.927 ? ? 
metalc16 metalc ? ? A VAL 445 O   ? ? ? 1_555 D CA . CA ? ? A VAL 645 A CA 903 1_555 ? ? ? ? ? ? ? 2.607 ? ? 
metalc17 metalc ? ? A ASP 533 OD1 ? ? ? 1_555 D CA . CA ? ? A ASP 733 A CA 903 1_555 ? ? ? ? ? ? ? 2.988 ? ? 
metalc18 metalc ? ? A ASP 533 OD2 ? ? ? 1_555 D CA . CA ? ? A ASP 733 A CA 903 1_555 ? ? ? ? ? ? ? 2.741 ? ? 
# 
_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 ASP 19  ? A ASP 219 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OD1 ? A ASP 21  ? A ASP 221 ? 1_555 73.8  ? 
2  OD1 ? A ASP 19  ? A ASP 219 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OD1 ? A ASP 23  ? A ASP 223 ? 1_555 70.0  ? 
3  OD1 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OD1 ? A ASP 23  ? A ASP 223 ? 1_555 67.3  ? 
4  OD1 ? A ASP 19  ? A ASP 219 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 O   ? A ILE 25  ? A ILE 225 ? 1_555 69.4  ? 
5  OD1 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 O   ? A ILE 25  ? A ILE 225 ? 1_555 133.4 ? 
6  OD1 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 O   ? A ILE 25  ? A ILE 225 ? 1_555 73.8  ? 
7  OD1 ? A ASP 19  ? A ASP 219 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OD1 ? A ASP 27  ? A ASP 227 ? 1_555 95.1  ? 
8  OD1 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OD1 ? A ASP 27  ? A ASP 227 ? 1_555 106.0 ? 
9  OD1 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OD1 ? A ASP 27  ? A ASP 227 ? 1_555 164.8 ? 
10 O   ? A ILE 25  ? A ILE 225 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OD1 ? A ASP 27  ? A ASP 227 ? 1_555 104.8 ? 
11 OD1 ? A ASP 19  ? A ASP 219 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 135.2 ? 
12 OD1 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 101.4 ? 
13 OD1 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 67.3  ? 
14 O   ? A ILE 25  ? A ILE 225 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 85.9  ? 
15 OD1 ? A ASP 27  ? A ASP 227 ? 1_555 CA ? C CA . ? A CA 902 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 127.9 ? 
16 OD2 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OD2 ? A ASP 23  ? A ASP 223 ? 1_555 94.6  ? 
17 OD2 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OE1 ? A GLU 30  ? A GLU 230 ? 1_555 123.8 ? 
18 OD2 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OE1 ? A GLU 30  ? A GLU 230 ? 1_555 84.6  ? 
19 OD2 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 81.0  ? 
20 OD2 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 67.1  ? 
21 OE1 ? A GLU 30  ? A GLU 230 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 47.1  ? 
22 OD2 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A SER 59  ? A SER 259 ? 1_555 88.2  ? 
23 OD2 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A SER 59  ? A SER 259 ? 1_555 152.4 ? 
24 OE1 ? A GLU 30  ? A GLU 230 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A SER 59  ? A SER 259 ? 1_555 71.3  ? 
25 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A SER 59  ? A SER 259 ? 1_555 86.3  ? 
26 OD2 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A GLU 62  ? A GLU 262 ? 1_555 71.4  ? 
27 OD2 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A GLU 62  ? A GLU 262 ? 1_555 133.5 ? 
28 OE1 ? A GLU 30  ? A GLU 230 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A GLU 62  ? A GLU 262 ? 1_555 140.4 ? 
29 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A GLU 62  ? A GLU 262 ? 1_555 145.9 ? 
30 O   ? A SER 59  ? A SER 259 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 O   ? A GLU 62  ? A GLU 262 ? 1_555 73.3  ? 
31 OD2 ? A ASP 21  ? A ASP 221 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OD2 ? A ASP 72  ? A ASP 272 ? 1_555 146.1 ? 
32 OD2 ? A ASP 23  ? A ASP 223 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OD2 ? A ASP 72  ? A ASP 272 ? 1_555 93.5  ? 
33 OE1 ? A GLU 30  ? A GLU 230 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OD2 ? A ASP 72  ? A ASP 272 ? 1_555 89.6  ? 
34 OE2 ? A GLU 30  ? A GLU 230 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OD2 ? A ASP 72  ? A ASP 272 ? 1_555 132.1 ? 
35 O   ? A SER 59  ? A SER 259 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OD2 ? A ASP 72  ? A ASP 272 ? 1_555 99.4  ? 
36 O   ? A GLU 62  ? A GLU 262 ? 1_555 CA ? B CA . ? A CA 901 ? 1_555 OD2 ? A ASP 72  ? A ASP 272 ? 1_555 79.2  ? 
37 O   ? A ASN 420 ? A ASN 620 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD2 ? A ASP 422 ? A ASP 622 ? 1_555 77.2  ? 
38 O   ? A ASN 420 ? A ASN 620 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 O   ? A VAL 445 ? A VAL 645 ? 1_555 94.7  ? 
39 OD2 ? A ASP 422 ? A ASP 622 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 O   ? A VAL 445 ? A VAL 645 ? 1_555 121.1 ? 
40 O   ? A ASN 420 ? A ASN 620 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD1 ? A ASP 533 ? A ASP 733 ? 1_555 70.8  ? 
41 OD2 ? A ASP 422 ? A ASP 622 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD1 ? A ASP 533 ? A ASP 733 ? 1_555 146.6 ? 
42 O   ? A VAL 445 ? A VAL 645 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD1 ? A ASP 533 ? A ASP 733 ? 1_555 72.0  ? 
43 O   ? A ASN 420 ? A ASN 620 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD2 ? A ASP 533 ? A ASP 733 ? 1_555 115.6 ? 
44 OD2 ? A ASP 422 ? A ASP 622 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD2 ? A ASP 533 ? A ASP 733 ? 1_555 165.4 ? 
45 O   ? A VAL 445 ? A VAL 645 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD2 ? A ASP 533 ? A ASP 733 ? 1_555 67.0  ? 
46 OD1 ? A ASP 533 ? A ASP 733 ? 1_555 CA ? D CA . ? A CA 903 ? 1_555 OD2 ? A ASP 533 ? A ASP 733 ? 1_555 44.8  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           238 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            438 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    239 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     439 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -2.35 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 4 ? 
AB3 ? 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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 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 TYR A 34  ? LYS A 37  ? TYR A 234 LYS A 237 
AA1 2 ILE A 40  ? LYS A 43  ? ILE A 240 LYS A 243 
AA2 1 VAL A 99  ? THR A 110 ? VAL A 299 THR A 310 
AA2 2 ALA A 186 ? ASN A 196 ? ALA A 386 ASN A 396 
AA2 3 LEU A 246 ? LEU A 248 ? LEU A 446 LEU A 448 
AA3 1 THR A 237 ? TYR A 238 ? THR A 437 TYR A 438 
AA3 2 ALA A 186 ? ASN A 196 ? ALA A 386 ASN A 396 
AA3 3 PRO A 260 ? ILE A 261 ? PRO A 460 ILE A 461 
AA4 1 GLU A 112 ? TYR A 144 ? GLU A 312 TYR A 344 
AA4 2 PHE A 148 ? ILE A 180 ? PHE A 348 ILE A 380 
AA5 1 GLU A 216 ? LYS A 222 ? GLU A 416 LYS A 422 
AA5 2 MET A 202 ? LEU A 213 ? MET A 402 LEU A 413 
AA5 3 GLY A 229 ? LEU A 232 ? GLY A 429 LEU A 432 
AA6 1 GLU A 216 ? LYS A 222 ? GLU A 416 LYS A 422 
AA6 2 MET A 202 ? LEU A 213 ? MET A 402 LEU A 413 
AA6 3 LYS A 276 ? ASN A 285 ? LYS A 476 ASN A 485 
AA7 1 THR A 288 ? LYS A 289 ? THR A 488 LYS A 489 
AA7 2 ILE A 295 ? ILE A 296 ? ILE A 495 ILE A 496 
AA8 1 THR A 324 ? ALA A 330 ? THR A 524 ALA A 530 
AA8 2 SER A 313 ? ASP A 319 ? SER A 513 ASP A 519 
AA8 3 ASN A 409 ? LYS A 413 ? ASN A 609 LYS A 613 
AA8 4 GLU A 376 ? PHE A 379 ? GLU A 576 PHE A 579 
AA9 1 THR A 357 ? LYS A 358 ? THR A 557 LYS A 558 
AA9 2 LEU A 363 ? TYR A 364 ? LEU A 563 TYR A 564 
AB1 1 TYR A 417 ? THR A 419 ? TYR A 617 THR A 619 
AB1 2 ILE A 530 ? GLU A 539 ? ILE A 730 GLU A 739 
AB1 3 ASN A 447 ? LEU A 449 ? ASN A 647 LEU A 649 
AB2 1 TYR A 417 ? THR A 419 ? TYR A 617 THR A 619 
AB2 2 ILE A 530 ? GLU A 539 ? ILE A 730 GLU A 739 
AB2 3 ARG A 467 ? LYS A 475 ? ARG A 667 LYS A 675 
AB2 4 THR A 504 ? GLU A 511 ? THR A 704 GLU A 711 
AB3 1 GLU A 452 ? ILE A 457 ? GLU A 652 ILE A 657 
AB3 2 ILE A 520 ? SER A 526 ? ILE A 720 SER A 726 
AB3 3 ILE A 483 ? LYS A 488 ? ILE A 683 LYS A 688 
AB3 4 LYS A 493 ? LEU A 497 ? LYS A 693 LEU A 697 
# 
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 LYS A 37  ? N LYS A 237 O ILE A 40  ? O ILE A 240 
AA2 1 2 N GLU A 104 ? N GLU A 304 O ASN A 191 ? O ASN A 391 
AA2 2 3 N ALA A 190 ? N ALA A 390 O LEU A 248 ? O LEU A 448 
AA3 1 2 O TYR A 238 ? O TYR A 438 N TYR A 194 ? N TYR A 394 
AA3 2 3 N ALA A 186 ? N ALA A 386 O ILE A 261 ? O ILE A 461 
AA4 1 2 N SER A 123 ? N SER A 323 O SER A 169 ? O SER A 369 
AA5 1 2 O GLU A 216 ? O GLU A 416 N LEU A 213 ? N LEU A 413 
AA5 2 3 N VAL A 205 ? N VAL A 405 O GLY A 229 ? O GLY A 429 
AA6 1 2 O GLU A 216 ? O GLU A 416 N LEU A 213 ? N LEU A 413 
AA6 2 3 N THR A 206 ? N THR A 406 O SER A 283 ? O SER A 483 
AA7 1 2 N THR A 288 ? N THR A 488 O ILE A 296 ? O ILE A 496 
AA8 1 2 O ARG A 327 ? O ARG A 527 N ILE A 316 ? N ILE A 516 
AA8 2 3 N ILE A 317 ? N ILE A 517 O ILE A 412 ? O ILE A 612 
AA8 3 4 O LYS A 413 ? O LYS A 613 N GLU A 376 ? N GLU A 576 
AA9 1 2 N THR A 357 ? N THR A 557 O TYR A 364 ? O TYR A 564 
AB1 1 2 N TYR A 417 ? N TYR A 617 O ILE A 537 ? O ILE A 737 
AB1 2 3 O LEU A 532 ? O LEU A 732 N ASN A 447 ? N ASN A 647 
AB2 1 2 N TYR A 417 ? N TYR A 617 O ILE A 537 ? O ILE A 737 
AB2 2 3 O SER A 536 ? O SER A 736 N SER A 471 ? N SER A 671 
AB2 3 4 N PHE A 470 ? N PHE A 670 O TYR A 508 ? O TYR A 708 
AB3 1 2 N ILE A 457 ? N ILE A 657 O ILE A 520 ? O ILE A 720 
AB3 2 3 O THR A 523 ? O THR A 723 N ASN A 486 ? N ASN A 686 
AB3 3 4 N VAL A 485 ? N VAL A 685 O ASP A 495 ? O ASP A 695 
# 
_pdbx_entry_details.entry_id                   9JSG 
_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_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C A TRP 374 ? ? O A TRP 374 ? ? 0.974 1.229 -0.255 0.019 N 
2 1 C A ASN 375 ? ? O A ASN 375 ? ? 1.001 1.229 -0.228 0.019 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 269 ? ? -63.39  1.18    
2 1 ASN A 633 ? ? 63.01   63.73   
3 1 ASP A 640 ? ? -98.57  31.58   
4 1 SER A 644 ? ? -121.40 -56.44  
5 1 SER A 689 ? ? -149.34 -158.39 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9JSG 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  6klx 
_em_3d_fitting_list.pdb_chain_id                  A 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      A 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                6klx 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9JSG 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.47 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               161249 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 'ORGANELLE OR CELLULAR COMPONENT' 
_em_entity_assembly.name                 'Clostridium perfringens iota toxin component Ib' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9JSG 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      0.01 
_em_imaging.nominal_defocus_min             600 
_em_imaging.nominal_defocus_max             1600 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9JSG 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277.15 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9JSG 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9JSG 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C7 
# 
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 ASN 201 ? A ASN 1   
2   1 Y 1 A ASN 202 ? A ASN 2   
3   1 Y 1 A PHE 203 ? A PHE 3   
4   1 Y 1 A PHE 204 ? A PHE 4   
5   1 Y 1 A ASP 205 ? A ASP 5   
6   1 Y 1 A VAL 206 ? A VAL 6   
7   1 Y 1 A ARG 207 ? A ARG 7   
8   1 Y 1 A PHE 208 ? A PHE 8   
9   1 Y 1 A PHE 209 ? A PHE 9   
10  1 Y 1 A SER 210 ? A SER 10  
11  1 Y 1 A ALA 211 ? A ALA 11  
12  1 Y 1 A ALA 212 ? A ALA 12  
13  1 Y 1 A TRP 213 ? A TRP 13  
14  1 Y 1 A GLU 214 ? A GLU 14  
15  1 Y 1 A ASP 215 ? A ASP 15  
16  1 Y 1 A ILE 746 ? A ILE 546 
17  1 Y 1 A LEU 747 ? A LEU 547 
18  1 Y 1 A LYS 748 ? A LYS 548 
19  1 Y 1 A GLU 749 ? A GLU 549 
20  1 Y 1 A PRO 750 ? A PRO 550 
21  1 Y 1 A GLU 751 ? A GLU 551 
22  1 Y 1 A ILE 752 ? A ILE 552 
23  1 Y 1 A LYS 753 ? A LYS 553 
24  1 Y 1 A VAL 754 ? A VAL 554 
25  1 Y 1 A PRO 755 ? A PRO 555 
26  1 Y 1 A SER 756 ? A SER 556 
27  1 Y 1 A ASP 757 ? A ASP 557 
28  1 Y 1 A GLN 758 ? A GLN 558 
29  1 Y 1 A GLU 759 ? A GLU 559 
30  1 Y 1 A ILE 760 ? A ILE 560 
31  1 Y 1 A LEU 761 ? A LEU 561 
32  1 Y 1 A ASP 762 ? A ASP 562 
33  1 Y 1 A ALA 763 ? A ALA 563 
34  1 Y 1 A HIS 764 ? A HIS 564 
35  1 Y 1 A ASN 765 ? A ASN 565 
36  1 Y 1 A LYS 766 ? A LYS 566 
37  1 Y 1 A TYR 767 ? A TYR 567 
38  1 Y 1 A TYR 768 ? A TYR 568 
39  1 Y 1 A ALA 769 ? A ALA 569 
40  1 Y 1 A ASP 770 ? A ASP 570 
41  1 Y 1 A ILE 771 ? A ILE 571 
42  1 Y 1 A LYS 772 ? A LYS 572 
43  1 Y 1 A LEU 773 ? A LEU 573 
44  1 Y 1 A ASP 774 ? A ASP 574 
45  1 Y 1 A THR 775 ? A THR 575 
46  1 Y 1 A ASN 776 ? A ASN 576 
47  1 Y 1 A THR 777 ? A THR 577 
48  1 Y 1 A GLY 778 ? A GLY 578 
49  1 Y 1 A ASN 779 ? A ASN 579 
50  1 Y 1 A THR 780 ? A THR 580 
51  1 Y 1 A TYR 781 ? A TYR 581 
52  1 Y 1 A ILE 782 ? A ILE 582 
53  1 Y 1 A ASP 783 ? A ASP 583 
54  1 Y 1 A GLY 784 ? A GLY 584 
55  1 Y 1 A ILE 785 ? A ILE 585 
56  1 Y 1 A TYR 786 ? A TYR 586 
57  1 Y 1 A PHE 787 ? A PHE 587 
58  1 Y 1 A GLU 788 ? A GLU 588 
59  1 Y 1 A PRO 789 ? A PRO 589 
60  1 Y 1 A THR 790 ? A THR 590 
61  1 Y 1 A GLN 791 ? A GLN 591 
62  1 Y 1 A THR 792 ? A THR 592 
63  1 Y 1 A ASN 793 ? A ASN 593 
64  1 Y 1 A LYS 794 ? A LYS 594 
65  1 Y 1 A GLU 795 ? A GLU 595 
66  1 Y 1 A ALA 796 ? A ALA 596 
67  1 Y 1 A LEU 797 ? A LEU 597 
68  1 Y 1 A ASP 798 ? A ASP 598 
69  1 Y 1 A TYR 799 ? A TYR 599 
70  1 Y 1 A ILE 800 ? A ILE 600 
71  1 Y 1 A GLN 801 ? A GLN 601 
72  1 Y 1 A LYS 802 ? A LYS 602 
73  1 Y 1 A TYR 803 ? A TYR 603 
74  1 Y 1 A ARG 804 ? A ARG 604 
75  1 Y 1 A VAL 805 ? A VAL 605 
76  1 Y 1 A GLU 806 ? A GLU 606 
77  1 Y 1 A ALA 807 ? A ALA 607 
78  1 Y 1 A THR 808 ? A THR 608 
79  1 Y 1 A LEU 809 ? A LEU 609 
80  1 Y 1 A GLN 810 ? A GLN 610 
81  1 Y 1 A TYR 811 ? A TYR 611 
82  1 Y 1 A SER 812 ? A SER 612 
83  1 Y 1 A GLY 813 ? A GLY 613 
84  1 Y 1 A PHE 814 ? A PHE 614 
85  1 Y 1 A LYS 815 ? A LYS 615 
86  1 Y 1 A ASP 816 ? A ASP 616 
87  1 Y 1 A ILE 817 ? A ILE 617 
88  1 Y 1 A GLY 818 ? A GLY 618 
89  1 Y 1 A THR 819 ? A THR 619 
90  1 Y 1 A LYS 820 ? A LYS 620 
91  1 Y 1 A ASP 821 ? A ASP 621 
92  1 Y 1 A LYS 822 ? A LYS 622 
93  1 Y 1 A GLU 823 ? A GLU 623 
94  1 Y 1 A ILE 824 ? A ILE 624 
95  1 Y 1 A ARG 825 ? A ARG 625 
96  1 Y 1 A ASN 826 ? A ASN 626 
97  1 Y 1 A TYR 827 ? A TYR 627 
98  1 Y 1 A LEU 828 ? A LEU 628 
99  1 Y 1 A GLY 829 ? A GLY 629 
100 1 Y 1 A ASP 830 ? A ASP 630 
101 1 Y 1 A GLN 831 ? A GLN 631 
102 1 Y 1 A ASN 832 ? A ASN 632 
103 1 Y 1 A GLN 833 ? A GLN 633 
104 1 Y 1 A PRO 834 ? A PRO 634 
105 1 Y 1 A LYS 835 ? A LYS 635 
106 1 Y 1 A THR 836 ? A THR 636 
107 1 Y 1 A ASN 837 ? A ASN 637 
108 1 Y 1 A TYR 838 ? A TYR 638 
109 1 Y 1 A ILE 839 ? A ILE 639 
110 1 Y 1 A ASN 840 ? A ASN 640 
111 1 Y 1 A PHE 841 ? A PHE 641 
112 1 Y 1 A ARG 842 ? A ARG 642 
113 1 Y 1 A SER 843 ? A SER 643 
114 1 Y 1 A TYR 844 ? A TYR 644 
115 1 Y 1 A PHE 845 ? A PHE 645 
116 1 Y 1 A THR 846 ? A THR 646 
117 1 Y 1 A SER 847 ? A SER 647 
118 1 Y 1 A GLY 848 ? A GLY 648 
119 1 Y 1 A GLU 849 ? A GLU 649 
120 1 Y 1 A ASN 850 ? A ASN 650 
121 1 Y 1 A VAL 851 ? A VAL 651 
122 1 Y 1 A MET 852 ? A MET 652 
123 1 Y 1 A THR 853 ? A THR 653 
124 1 Y 1 A TYR 854 ? A TYR 654 
125 1 Y 1 A LYS 855 ? A LYS 655 
126 1 Y 1 A LYS 856 ? A LYS 656 
127 1 Y 1 A LEU 857 ? A LEU 657 
128 1 Y 1 A ARG 858 ? A ARG 658 
129 1 Y 1 A ILE 859 ? A ILE 659 
130 1 Y 1 A TYR 860 ? A TYR 660 
131 1 Y 1 A ALA 861 ? A ALA 661 
132 1 Y 1 A VAL 862 ? A VAL 662 
133 1 Y 1 A THR 863 ? A THR 663 
134 1 Y 1 A PRO 864 ? A PRO 664 
135 1 Y 1 A ASP 865 ? A ASP 665 
136 1 Y 1 A ASN 866 ? A ASN 666 
137 1 Y 1 A ARG 867 ? A ARG 667 
138 1 Y 1 A GLU 868 ? A GLU 668 
139 1 Y 1 A LEU 869 ? A LEU 669 
140 1 Y 1 A LEU 870 ? A LEU 670 
141 1 Y 1 A VAL 871 ? A VAL 671 
142 1 Y 1 A LEU 872 ? A LEU 672 
143 1 Y 1 A SER 873 ? A SER 673 
144 1 Y 1 A VAL 874 ? A VAL 674 
145 1 Y 1 A ASN 875 ? A ASN 675 
146 1 Y 1 A LEU 876 ? A LEU 676 
147 1 Y 1 A GLU 877 ? A GLU 677 
148 1 Y 1 A HIS 878 ? A HIS 678 
149 1 Y 1 A HIS 879 ? A HIS 679 
150 1 Y 1 A HIS 880 ? A HIS 680 
151 1 Y 1 A HIS 881 ? A HIS 681 
152 1 Y 1 A HIS 882 ? A HIS 682 
153 1 Y 1 A HIS 883 ? A HIS 683 
# 
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  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
ILE N    N  N N 159 
ILE CA   C  N S 160 
ILE C    C  N N 161 
ILE O    O  N N 162 
ILE CB   C  N S 163 
ILE CG1  C  N N 164 
ILE CG2  C  N N 165 
ILE CD1  C  N N 166 
ILE OXT  O  N N 167 
ILE H    H  N N 168 
ILE H2   H  N N 169 
ILE HA   H  N N 170 
ILE HB   H  N N 171 
ILE HG12 H  N N 172 
ILE HG13 H  N N 173 
ILE HG21 H  N N 174 
ILE HG22 H  N N 175 
ILE HG23 H  N N 176 
ILE HD11 H  N N 177 
ILE HD12 H  N N 178 
ILE HD13 H  N N 179 
ILE HXT  H  N N 180 
LEU N    N  N N 181 
LEU CA   C  N S 182 
LEU C    C  N N 183 
LEU O    O  N N 184 
LEU CB   C  N N 185 
LEU CG   C  N N 186 
LEU CD1  C  N N 187 
LEU CD2  C  N N 188 
LEU OXT  O  N N 189 
LEU H    H  N N 190 
LEU H2   H  N N 191 
LEU HA   H  N N 192 
LEU HB2  H  N N 193 
LEU HB3  H  N N 194 
LEU HG   H  N N 195 
LEU HD11 H  N N 196 
LEU HD12 H  N N 197 
LEU HD13 H  N N 198 
LEU HD21 H  N N 199 
LEU HD22 H  N N 200 
LEU HD23 H  N N 201 
LEU HXT  H  N N 202 
LYS N    N  N N 203 
LYS CA   C  N S 204 
LYS C    C  N N 205 
LYS O    O  N N 206 
LYS CB   C  N N 207 
LYS CG   C  N N 208 
LYS CD   C  N N 209 
LYS CE   C  N N 210 
LYS NZ   N  N N 211 
LYS OXT  O  N N 212 
LYS H    H  N N 213 
LYS H2   H  N N 214 
LYS HA   H  N N 215 
LYS HB2  H  N N 216 
LYS HB3  H  N N 217 
LYS HG2  H  N N 218 
LYS HG3  H  N N 219 
LYS HD2  H  N N 220 
LYS HD3  H  N N 221 
LYS HE2  H  N N 222 
LYS HE3  H  N N 223 
LYS HZ1  H  N N 224 
LYS HZ2  H  N N 225 
LYS HZ3  H  N N 226 
LYS HXT  H  N N 227 
MET N    N  N N 228 
MET CA   C  N S 229 
MET C    C  N N 230 
MET O    O  N N 231 
MET CB   C  N N 232 
MET CG   C  N N 233 
MET SD   S  N N 234 
MET CE   C  N N 235 
MET OXT  O  N N 236 
MET H    H  N N 237 
MET H2   H  N N 238 
MET HA   H  N N 239 
MET HB2  H  N N 240 
MET HB3  H  N N 241 
MET HG2  H  N N 242 
MET HG3  H  N N 243 
MET HE1  H  N N 244 
MET HE2  H  N N 245 
MET HE3  H  N N 246 
MET HXT  H  N N 247 
PHE N    N  N N 248 
PHE CA   C  N S 249 
PHE C    C  N N 250 
PHE O    O  N N 251 
PHE CB   C  N N 252 
PHE CG   C  Y N 253 
PHE CD1  C  Y N 254 
PHE CD2  C  Y N 255 
PHE CE1  C  Y N 256 
PHE CE2  C  Y N 257 
PHE CZ   C  Y N 258 
PHE OXT  O  N N 259 
PHE H    H  N N 260 
PHE H2   H  N N 261 
PHE HA   H  N N 262 
PHE HB2  H  N N 263 
PHE HB3  H  N N 264 
PHE HD1  H  N N 265 
PHE HD2  H  N N 266 
PHE HE1  H  N N 267 
PHE HE2  H  N N 268 
PHE HZ   H  N N 269 
PHE HXT  H  N N 270 
PRO N    N  N N 271 
PRO CA   C  N S 272 
PRO C    C  N N 273 
PRO O    O  N N 274 
PRO CB   C  N N 275 
PRO CG   C  N N 276 
PRO CD   C  N N 277 
PRO OXT  O  N N 278 
PRO H    H  N N 279 
PRO HA   H  N N 280 
PRO HB2  H  N N 281 
PRO HB3  H  N N 282 
PRO HG2  H  N N 283 
PRO HG3  H  N N 284 
PRO HD2  H  N N 285 
PRO HD3  H  N N 286 
PRO HXT  H  N N 287 
SER N    N  N N 288 
SER CA   C  N S 289 
SER C    C  N N 290 
SER O    O  N N 291 
SER CB   C  N N 292 
SER OG   O  N N 293 
SER OXT  O  N N 294 
SER H    H  N N 295 
SER H2   H  N N 296 
SER HA   H  N N 297 
SER HB2  H  N N 298 
SER HB3  H  N N 299 
SER HG   H  N N 300 
SER HXT  H  N N 301 
THR N    N  N N 302 
THR CA   C  N S 303 
THR C    C  N N 304 
THR O    O  N N 305 
THR CB   C  N R 306 
THR OG1  O  N N 307 
THR CG2  C  N N 308 
THR OXT  O  N N 309 
THR H    H  N N 310 
THR H2   H  N N 311 
THR HA   H  N N 312 
THR HB   H  N N 313 
THR HG1  H  N N 314 
THR HG21 H  N N 315 
THR HG22 H  N N 316 
THR HG23 H  N N 317 
THR HXT  H  N N 318 
TRP N    N  N N 319 
TRP CA   C  N S 320 
TRP C    C  N N 321 
TRP O    O  N N 322 
TRP CB   C  N N 323 
TRP CG   C  Y N 324 
TRP CD1  C  Y N 325 
TRP CD2  C  Y N 326 
TRP NE1  N  Y N 327 
TRP CE2  C  Y N 328 
TRP CE3  C  Y N 329 
TRP CZ2  C  Y N 330 
TRP CZ3  C  Y N 331 
TRP CH2  C  Y N 332 
TRP OXT  O  N N 333 
TRP H    H  N N 334 
TRP H2   H  N N 335 
TRP HA   H  N N 336 
TRP HB2  H  N N 337 
TRP HB3  H  N N 338 
TRP HD1  H  N N 339 
TRP HE1  H  N N 340 
TRP HE3  H  N N 341 
TRP HZ2  H  N N 342 
TRP HZ3  H  N N 343 
TRP HH2  H  N N 344 
TRP HXT  H  N N 345 
TYR N    N  N N 346 
TYR CA   C  N S 347 
TYR C    C  N N 348 
TYR O    O  N N 349 
TYR CB   C  N N 350 
TYR CG   C  Y N 351 
TYR CD1  C  Y N 352 
TYR CD2  C  Y N 353 
TYR CE1  C  Y N 354 
TYR CE2  C  Y N 355 
TYR CZ   C  Y N 356 
TYR OH   O  N N 357 
TYR OXT  O  N N 358 
TYR H    H  N N 359 
TYR H2   H  N N 360 
TYR HA   H  N N 361 
TYR HB2  H  N N 362 
TYR HB3  H  N N 363 
TYR HD1  H  N N 364 
TYR HD2  H  N N 365 
TYR HE1  H  N N 366 
TYR HE2  H  N N 367 
TYR HH   H  N N 368 
TYR HXT  H  N N 369 
VAL N    N  N N 370 
VAL CA   C  N S 371 
VAL C    C  N N 372 
VAL O    O  N N 373 
VAL CB   C  N N 374 
VAL CG1  C  N N 375 
VAL CG2  C  N N 376 
VAL OXT  O  N N 377 
VAL H    H  N N 378 
VAL H2   H  N N 379 
VAL HA   H  N N 380 
VAL HB   H  N N 381 
VAL HG11 H  N N 382 
VAL HG12 H  N N 383 
VAL HG13 H  N N 384 
VAL HG21 H  N N 385 
VAL HG22 H  N N 386 
VAL HG23 H  N N 387 
VAL HXT  H  N N 388 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-30 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9JSG 
_em_admin.last_update        2025-05-14 
_em_admin.map_release_date   2025-05-14 
_em_admin.title              'Clostridium perfringens iota toxin pore Ib in pore state' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20  mM C4H11NO3 1 'tris hydroxymethyl aminomethane' 
1 100 mM NaCl     2 'Sodium Chloride'                 
1 1.0 mM CaCl2    3 'Calcium Chloride'                
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                ? 
_em_entity_assembly_molwt.value                ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1502 
_em_entity_assembly_naturalsource.organism             'Clostridium perfringens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               'NCIB 10748' 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              pet23a 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50.0 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    1 
_em_image_recording.num_real_images                     11549 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   6223563 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            'template picker'      1  1 ? ? cryoSPARC       3.3.2  
'IMAGE ACQUISITION'             ?                      2  ? ? 1 ?               ?      
MASKING                         ?                      3  ? ? ? ?               ?      
'CTF CORRECTION'                'patch CTF estimation' 4  1 ? ? cryoSPARC       3.3.2  
'LAYERLINE INDEXING'            ?                      5  ? ? ? ?               ?      
'DIFFRACTION INDEXING'          ?                      6  ? ? ? ?               ?      
'MODEL FITTING'                 ?                      7  ? 1 ? 'UCSF ChimeraX' 1.2.4  
OTHER                           ?                      8  ? ? ? ?               ?      
'MODEL REFINEMENT'              ?                      9  ? 1 ? PHENIX          1.19.2 
'MODEL REFINEMENT'              ?                      10 ? 1 ? Coot            0.9.5  
'INITIAL EULER ASSIGNMENT'      ?                      11 1 ? ? ?               ?      
'FINAL EULER ASSIGNMENT'        ?                      12 1 ? ? cryoSPARC       3.3.2  
CLASSIFICATION                  ?                      13 1 ? ? cryoSPARC       3.3.2  
RECONSTRUCTION                  ?                      14 1 ? ? cryoSPARC       3.3.2  
'VOLUME SELECTION'              ?                      15 1 1 1 ?               ?      
'SERIES ALIGNMENT'              ?                      16 1 1 1 ?               ?      
'MOLECULAR REPLACEMENT'         ?                      17 1 1 1 ?               ?      
'LATTICE DISTORTION CORRECTION' ?                      18 1 1 1 ?               ?      
'SYMMETRY DETERMINATION'        ?                      19 1 1 1 ?               ?      
'CRYSTALLOGRAPHY MERGING'       ?                      20 1 1 1 ?               ?      
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)'        Japan 21J13410 1 
'Japan Society for the Promotion of Science (JSPS)'        Japan 21H02452 2 
'Japan Society for the Promotion of Science (JSPS)'        Japan 24K01993 3 
'Japan Agency for Medical Research and Development (AMED)' Japan 2366     4 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB       6klx   ? 
2 ? 'in silico model'    AlphaFold Q46221 ? 
# 
_atom_sites.entry_id                    9JSG 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
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   . GLU A 1 16  ? 93.248  142.706 49.358  1.00 51.31  ? 216 GLU A N   1 
ATOM   2    C  CA  . GLU A 1 16  ? 92.657  142.080 50.536  1.00 51.31  ? 216 GLU A CA  1 
ATOM   3    C  C   . GLU A 1 16  ? 93.344  140.757 50.863  1.00 51.31  ? 216 GLU A C   1 
ATOM   4    O  O   . GLU A 1 16  ? 92.772  139.897 51.533  1.00 51.31  ? 216 GLU A O   1 
ATOM   5    C  CB  . GLU A 1 16  ? 91.153  141.854 50.335  1.00 51.31  ? 216 GLU A CB  1 
ATOM   6    C  CG  . GLU A 1 16  ? 90.383  143.047 49.776  1.00 51.31  ? 216 GLU A CG  1 
ATOM   7    C  CD  . GLU A 1 16  ? 89.360  142.643 48.726  1.00 51.31  ? 216 GLU A CD  1 
ATOM   8    O  OE1 . GLU A 1 16  ? 88.590  141.690 48.972  1.00 51.31  ? 216 GLU A OE1 1 
ATOM   9    O  OE2 . GLU A 1 16  ? 89.315  143.286 47.656  1.00 51.31  ? 216 GLU A OE2 1 
ATOM   10   N  N   . ASP A 1 17  ? 94.574  140.592 50.379  1.00 49.04  ? 217 ASP A N   1 
ATOM   11   C  CA  . ASP A 1 17  ? 95.353  139.390 50.634  1.00 49.04  ? 217 ASP A CA  1 
ATOM   12   C  C   . ASP A 1 17  ? 96.657  139.668 51.367  1.00 49.04  ? 217 ASP A C   1 
ATOM   13   O  O   . ASP A 1 17  ? 97.472  138.748 51.519  1.00 49.04  ? 217 ASP A O   1 
ATOM   14   C  CB  . ASP A 1 17  ? 95.652  138.649 49.322  1.00 49.04  ? 217 ASP A CB  1 
ATOM   15   C  CG  . ASP A 1 17  ? 94.413  137.991 48.730  1.00 49.04  ? 217 ASP A CG  1 
ATOM   16   O  OD1 . ASP A 1 17  ? 93.406  137.861 49.453  1.00 49.04  ? 217 ASP A OD1 1 
ATOM   17   O  OD2 . ASP A 1 17  ? 94.457  137.596 47.547  1.00 49.04  ? 217 ASP A OD2 1 
ATOM   18   N  N   . LEU A 1 18  ? 96.879  140.897 51.827  1.00 40.04  ? 218 LEU A N   1 
ATOM   19   C  CA  . LEU A 1 18  ? 98.103  141.234 52.538  1.00 40.04  ? 218 LEU A CA  1 
ATOM   20   C  C   . LEU A 1 18  ? 97.949  140.928 54.021  1.00 40.04  ? 218 LEU A C   1 
ATOM   21   O  O   . LEU A 1 18  ? 96.945  141.298 54.640  1.00 40.04  ? 218 LEU A O   1 
ATOM   22   C  CB  . LEU A 1 18  ? 98.445  142.709 52.332  1.00 40.04  ? 218 LEU A CB  1 
ATOM   23   C  CG  . LEU A 1 18  ? 99.874  143.130 52.685  1.00 40.04  ? 218 LEU A CG  1 
ATOM   24   C  CD1 . LEU A 1 18  ? 100.884 142.447 51.769  1.00 40.04  ? 218 LEU A CD1 1 
ATOM   25   C  CD2 . LEU A 1 18  ? 100.010 144.643 52.627  1.00 40.04  ? 218 LEU A CD2 1 
ATOM   26   N  N   . ASP A 1 19  ? 98.945  140.249 54.587  1.00 34.08  ? 219 ASP A N   1 
ATOM   27   C  CA  . ASP A 1 19  ? 98.970  139.882 56.003  1.00 34.08  ? 219 ASP A CA  1 
ATOM   28   C  C   . ASP A 1 19  ? 100.333 140.290 56.555  1.00 34.08  ? 219 ASP A C   1 
ATOM   29   O  O   . ASP A 1 19  ? 101.300 139.528 56.470  1.00 34.08  ? 219 ASP A O   1 
ATOM   30   C  CB  . ASP A 1 19  ? 98.704  138.393 56.190  1.00 34.08  ? 219 ASP A CB  1 
ATOM   31   C  CG  . ASP A 1 19  ? 98.321  138.047 57.613  1.00 34.08  ? 219 ASP A CG  1 
ATOM   32   O  OD1 . ASP A 1 19  ? 98.111  138.977 58.419  1.00 34.08  ? 219 ASP A OD1 1 
ATOM   33   O  OD2 . ASP A 1 19  ? 98.225  136.844 57.929  1.00 34.08  ? 219 ASP A OD2 1 
ATOM   34   N  N   . THR A 1 20  ? 100.403 141.496 57.124  1.00 32.73  ? 220 THR A N   1 
ATOM   35   C  CA  . THR A 1 20  ? 101.684 142.032 57.577  1.00 32.73  ? 220 THR A CA  1 
ATOM   36   C  C   . THR A 1 20  ? 102.204 141.280 58.798  1.00 32.73  ? 220 THR A C   1 
ATOM   37   O  O   . THR A 1 20  ? 103.385 140.920 58.859  1.00 32.73  ? 220 THR A O   1 
ATOM   38   C  CB  . THR A 1 20  ? 101.548 143.524 57.883  1.00 32.73  ? 220 THR A CB  1 
ATOM   39   O  OG1 . THR A 1 20  ? 100.849 144.174 56.814  1.00 32.73  ? 220 THR A OG1 1 
ATOM   40   C  CG2 . THR A 1 20  ? 102.920 144.161 58.048  1.00 32.73  ? 220 THR A CG2 1 
ATOM   41   N  N   . ASP A 1 21  ? 101.340 141.030 59.777  1.00 31.04  ? 221 ASP A N   1 
ATOM   42   C  CA  . ASP A 1 21  ? 101.750 140.390 61.021  1.00 31.04  ? 221 ASP A CA  1 
ATOM   43   C  C   . ASP A 1 21  ? 101.665 138.871 60.967  1.00 31.04  ? 221 ASP A C   1 
ATOM   44   O  O   . ASP A 1 21  ? 101.997 138.213 61.960  1.00 31.04  ? 221 ASP A O   1 
ATOM   45   C  CB  . ASP A 1 21  ? 100.899 140.908 62.186  1.00 31.04  ? 221 ASP A CB  1 
ATOM   46   C  CG  . ASP A 1 21  ? 99.422  140.945 61.855  1.00 31.04  ? 221 ASP A CG  1 
ATOM   47   O  OD1 . ASP A 1 21  ? 99.070  140.670 60.690  1.00 31.04  ? 221 ASP A OD1 1 
ATOM   48   O  OD2 . ASP A 1 21  ? 98.612  141.244 62.757  1.00 31.04  ? 221 ASP A OD2 1 
ATOM   49   N  N   . ASN A 1 22  ? 101.246 138.302 59.834  1.00 32.54  ? 222 ASN A N   1 
ATOM   50   C  CA  . ASN A 1 22  ? 101.102 136.853 59.671  1.00 32.54  ? 222 ASN A CA  1 
ATOM   51   C  C   . ASN A 1 22  ? 100.233 136.254 60.776  1.00 32.54  ? 222 ASN A C   1 
ATOM   52   O  O   . ASN A 1 22  ? 100.532 135.191 61.321  1.00 32.54  ? 222 ASN A O   1 
ATOM   53   C  CB  . ASN A 1 22  ? 102.463 136.151 59.606  1.00 32.54  ? 222 ASN A CB  1 
ATOM   54   C  CG  . ASN A 1 22  ? 103.504 136.954 58.847  1.00 32.54  ? 222 ASN A CG  1 
ATOM   55   O  OD1 . ASN A 1 22  ? 104.112 137.873 59.395  1.00 32.54  ? 222 ASN A OD1 1 
ATOM   56   N  ND2 . ASN A 1 22  ? 103.687 136.636 57.571  1.00 32.54  ? 222 ASN A ND2 1 
ATOM   57   N  N   . ASP A 1 23  ? 99.143  136.944 61.101  1.00 31.01  ? 223 ASP A N   1 
ATOM   58   C  CA  . ASP A 1 23  ? 98.189  136.486 62.100  1.00 31.01  ? 223 ASP A CA  1 
ATOM   59   C  C   . ASP A 1 23  ? 96.983  135.796 61.471  1.00 31.01  ? 223 ASP A C   1 
ATOM   60   O  O   . ASP A 1 23  ? 95.965  135.612 62.145  1.00 31.01  ? 223 ASP A O   1 
ATOM   61   C  CB  . ASP A 1 23  ? 97.743  137.660 62.976  1.00 31.01  ? 223 ASP A CB  1 
ATOM   62   C  CG  . ASP A 1 23  ? 96.675  138.509 62.318  1.00 31.01  ? 223 ASP A CG  1 
ATOM   63   O  OD1 . ASP A 1 23  ? 96.866  138.907 61.150  1.00 31.01  ? 223 ASP A OD1 1 
ATOM   64   O  OD2 . ASP A 1 23  ? 95.652  138.790 62.975  1.00 31.01  ? 223 ASP A OD2 1 
ATOM   65   N  N   . ASN A 1 24  ? 97.079  135.431 60.190  1.00 31.32  ? 224 ASN A N   1 
ATOM   66   C  CA  . ASN A 1 24  ? 96.093  134.678 59.406  1.00 31.32  ? 224 ASN A CA  1 
ATOM   67   C  C   . ASN A 1 24  ? 94.855  135.496 59.062  1.00 31.32  ? 224 ASN A C   1 
ATOM   68   O  O   . ASN A 1 24  ? 93.878  134.932 58.543  1.00 31.32  ? 224 ASN A O   1 
ATOM   69   C  CB  . ASN A 1 24  ? 95.666  133.382 60.104  1.00 31.32  ? 224 ASN A CB  1 
ATOM   70   C  CG  . ASN A 1 24  ? 95.981  132.151 59.281  1.00 31.32  ? 224 ASN A CG  1 
ATOM   71   O  OD1 . ASN A 1 24  ? 96.931  132.138 58.497  1.00 31.32  ? 224 ASN A OD1 1 
ATOM   72   N  ND2 . ASN A 1 24  ? 95.185  131.102 59.457  1.00 31.32  ? 224 ASN A ND2 1 
ATOM   73   N  N   . ILE A 1 25  ? 94.852  136.800 59.324  1.00 30.83  ? 225 ILE A N   1 
ATOM   74   C  CA  . ILE A 1 25  ? 93.750  137.684 58.968  1.00 30.83  ? 225 ILE A CA  1 
ATOM   75   C  C   . ILE A 1 25  ? 94.312  138.817 58.122  1.00 30.83  ? 225 ILE A C   1 
ATOM   76   O  O   . ILE A 1 25  ? 95.299  139.439 58.519  1.00 30.83  ? 225 ILE A O   1 
ATOM   77   C  CB  . ILE A 1 25  ? 93.019  138.245 60.203  1.00 30.83  ? 225 ILE A CB  1 
ATOM   78   C  CG1 . ILE A 1 25  ? 92.742  137.129 61.212  1.00 30.83  ? 225 ILE A CG1 1 
ATOM   79   C  CG2 . ILE A 1 25  ? 91.722  138.926 59.789  1.00 30.83  ? 225 ILE A CG2 1 
ATOM   80   C  CD1 . ILE A 1 25  ? 92.648  137.598 62.646  1.00 30.83  ? 225 ILE A CD1 1 
ATOM   81   N  N   . PRO A 1 26  ? 93.735  139.111 56.957  1.00 33.46  ? 226 PRO A N   1 
ATOM   82   C  CA  . PRO A 1 26  ? 94.277  140.184 56.114  1.00 33.46  ? 226 PRO A CA  1 
ATOM   83   C  C   . PRO A 1 26  ? 94.167  141.548 56.783  1.00 33.46  ? 226 PRO A C   1 
ATOM   84   O  O   . PRO A 1 26  ? 93.303  141.784 57.630  1.00 33.46  ? 226 PRO A O   1 
ATOM   85   C  CB  . PRO A 1 26  ? 93.417  140.113 54.846  1.00 33.46  ? 226 PRO A CB  1 
ATOM   86   C  CG  . PRO A 1 26  ? 92.860  138.725 54.837  1.00 33.46  ? 226 PRO A CG  1 
ATOM   87   C  CD  . PRO A 1 26  ? 92.664  138.362 56.278  1.00 33.46  ? 226 PRO A CD  1 
ATOM   88   N  N   . ASP A 1 27  ? 95.070  142.450 56.388  1.00 33.50  ? 227 ASP A N   1 
ATOM   89   C  CA  . ASP A 1 27  ? 95.107  143.784 56.980  1.00 33.50  ? 227 ASP A CA  1 
ATOM   90   C  C   . ASP A 1 27  ? 93.816  144.551 56.713  1.00 33.50  ? 227 ASP A C   1 
ATOM   91   O  O   . ASP A 1 27  ? 93.306  145.249 57.597  1.00 33.50  ? 227 ASP A O   1 
ATOM   92   C  CB  . ASP A 1 27  ? 96.307  144.561 56.439  1.00 33.50  ? 227 ASP A CB  1 
ATOM   93   C  CG  . ASP A 1 27  ? 97.620  143.838 56.666  1.00 33.50  ? 227 ASP A CG  1 
ATOM   94   O  OD1 . ASP A 1 27  ? 97.609  142.763 57.300  1.00 33.50  ? 227 ASP A OD1 1 
ATOM   95   O  OD2 . ASP A 1 27  ? 98.663  144.345 56.202  1.00 33.50  ? 227 ASP A OD2 1 
ATOM   96   N  N   . ALA A 1 28  ? 93.285  144.448 55.493  1.00 32.85  ? 228 ALA A N   1 
ATOM   97   C  CA  . ALA A 1 28  ? 92.033  145.127 55.175  1.00 32.85  ? 228 ALA A CA  1 
ATOM   98   C  C   . ALA A 1 28  ? 90.883  144.576 56.007  1.00 32.85  ? 228 ALA A C   1 
ATOM   99   O  O   . ALA A 1 28  ? 89.971  145.317 56.393  1.00 32.85  ? 228 ALA A O   1 
ATOM   100  C  CB  . ALA A 1 28  ? 91.730  145.000 53.682  1.00 32.85  ? 228 ALA A CB  1 
ATOM   101  N  N   . TYR A 1 29  ? 90.911  143.273 56.295  1.00 32.76  ? 229 TYR A N   1 
ATOM   102  C  CA  . TYR A 1 29  ? 89.869  142.677 57.126  1.00 32.76  ? 229 TYR A CA  1 
ATOM   103  C  C   . TYR A 1 29  ? 89.963  143.164 58.565  1.00 32.76  ? 229 TYR A C   1 
ATOM   104  O  O   . TYR A 1 29  ? 88.939  143.326 59.238  1.00 32.76  ? 229 TYR A O   1 
ATOM   105  C  CB  . TYR A 1 29  ? 89.956  141.151 57.068  1.00 32.76  ? 229 TYR A CB  1 
ATOM   106  C  CG  . TYR A 1 29  ? 89.451  140.540 55.777  1.00 32.76  ? 229 TYR A CG  1 
ATOM   107  C  CD1 . TYR A 1 29  ? 89.119  141.335 54.687  1.00 32.76  ? 229 TYR A CD1 1 
ATOM   108  C  CD2 . TYR A 1 29  ? 89.309  139.165 55.649  1.00 32.76  ? 229 TYR A CD2 1 
ATOM   109  C  CE1 . TYR A 1 29  ? 88.661  140.778 53.509  1.00 32.76  ? 229 TYR A CE1 1 
ATOM   110  C  CE2 . TYR A 1 29  ? 88.852  138.600 54.475  1.00 32.76  ? 229 TYR A CE2 1 
ATOM   111  C  CZ  . TYR A 1 29  ? 88.528  139.411 53.409  1.00 32.76  ? 229 TYR A CZ  1 
ATOM   112  N  N   . GLU A 1 30  ? 91.181  143.391 59.064  1.00 30.70  ? 230 GLU A N   1 
ATOM   113  C  CA  . GLU A 1 30  ? 91.346  143.858 60.436  1.00 30.70  ? 230 GLU A CA  1 
ATOM   114  C  C   . GLU A 1 30  ? 91.017  145.341 60.575  1.00 30.70  ? 230 GLU A C   1 
ATOM   115  O  O   . GLU A 1 30  ? 90.455  145.758 61.594  1.00 30.70  ? 230 GLU A O   1 
ATOM   116  C  CB  . GLU A 1 30  ? 92.767  143.581 60.926  1.00 30.70  ? 230 GLU A CB  1 
ATOM   117  C  CG  . GLU A 1 30  ? 93.167  142.120 60.860  1.00 30.70  ? 230 GLU A CG  1 
ATOM   118  C  CD  . GLU A 1 30  ? 94.320  141.791 61.785  1.00 30.70  ? 230 GLU A CD  1 
ATOM   119  O  OE1 . GLU A 1 30  ? 94.170  141.973 63.011  1.00 30.70  ? 230 GLU A OE1 1 
ATOM   120  O  OE2 . GLU A 1 30  ? 95.377  141.352 61.287  1.00 30.70  ? 230 GLU A OE2 1 
ATOM   121  N  N   . LYS A 1 31  ? 91.370  146.153 59.575  1.00 32.18  ? 231 LYS A N   1 
ATOM   122  C  CA  . LYS A 1 31  ? 91.049  147.576 59.632  1.00 32.18  ? 231 LYS A CA  1 
ATOM   123  C  C   . LYS A 1 31  ? 89.541  147.791 59.667  1.00 32.18  ? 231 LYS A C   1 
ATOM   124  O  O   . LYS A 1 31  ? 89.031  148.595 60.455  1.00 32.18  ? 231 LYS A O   1 
ATOM   125  C  CB  . LYS A 1 31  ? 91.671  148.306 58.442  1.00 32.18  ? 231 LYS A CB  1 
ATOM   126  C  CG  . LYS A 1 31  ? 93.185  148.399 58.488  1.00 32.18  ? 231 LYS A CG  1 
ATOM   127  C  CD  . LYS A 1 31  ? 93.739  148.948 57.184  1.00 32.18  ? 231 LYS A CD  1 
ATOM   128  C  CE  . LYS A 1 31  ? 95.082  148.323 56.844  1.00 32.18  ? 231 LYS A CE  1 
ATOM   129  N  NZ  . LYS A 1 31  ? 95.845  149.148 55.868  1.00 32.18  ? 231 LYS A NZ  1 
ATOM   130  N  N   . ASN A 1 32  ? 88.812  147.076 58.817  1.00 33.45  ? 232 ASN A N   1 
ATOM   131  C  CA  . ASN A 1 32  ? 87.360  147.058 58.849  1.00 33.45  ? 232 ASN A CA  1 
ATOM   132  C  C   . ASN A 1 32  ? 86.902  145.901 59.734  1.00 33.45  ? 232 ASN A C   1 
ATOM   133  O  O   . ASN A 1 32  ? 87.681  145.333 60.503  1.00 33.45  ? 232 ASN A O   1 
ATOM   134  C  CB  . ASN A 1 32  ? 86.800  146.966 57.431  1.00 33.45  ? 232 ASN A CB  1 
ATOM   135  C  CG  . ASN A 1 32  ? 87.465  147.941 56.479  1.00 33.45  ? 232 ASN A CG  1 
ATOM   136  O  OD1 . ASN A 1 32  ? 87.645  149.115 56.801  1.00 33.45  ? 232 ASN A OD1 1 
ATOM   137  N  ND2 . ASN A 1 32  ? 87.833  147.458 55.299  1.00 33.45  ? 232 ASN A ND2 1 
ATOM   138  N  N   . GLY A 1 33  ? 85.620  145.556 59.661  1.00 31.73  ? 233 GLY A N   1 
ATOM   139  C  CA  . GLY A 1 33  ? 85.136  144.397 60.377  1.00 31.73  ? 233 GLY A CA  1 
ATOM   140  C  C   . GLY A 1 33  ? 85.423  143.098 59.647  1.00 31.73  ? 233 GLY A C   1 
ATOM   141  O  O   . GLY A 1 33  ? 85.683  143.066 58.445  1.00 31.73  ? 233 GLY A O   1 
ATOM   142  N  N   . TYR A 1 34  ? 85.369  142.003 60.402  1.00 30.30  ? 234 TYR A N   1 
ATOM   143  C  CA  . TYR A 1 34  ? 85.524  140.671 59.835  1.00 30.30  ? 234 TYR A CA  1 
ATOM   144  C  C   . TYR A 1 34  ? 84.864  139.670 60.769  1.00 30.30  ? 234 TYR A C   1 
ATOM   145  O  O   . TYR A 1 34  ? 84.603  139.964 61.938  1.00 30.30  ? 234 TYR A O   1 
ATOM   146  C  CB  . TYR A 1 34  ? 87.001  140.318 59.611  1.00 30.30  ? 234 TYR A CB  1 
ATOM   147  C  CG  . TYR A 1 34  ? 87.809  140.152 60.881  1.00 30.30  ? 234 TYR A CG  1 
ATOM   148  C  CD1 . TYR A 1 34  ? 88.402  141.246 61.497  1.00 30.30  ? 234 TYR A CD1 1 
ATOM   149  C  CD2 . TYR A 1 34  ? 87.989  138.900 61.456  1.00 30.30  ? 234 TYR A CD2 1 
ATOM   150  C  CE1 . TYR A 1 34  ? 89.144  141.100 62.654  1.00 30.30  ? 234 TYR A CE1 1 
ATOM   151  C  CE2 . TYR A 1 34  ? 88.729  138.744 62.614  1.00 30.30  ? 234 TYR A CE2 1 
ATOM   152  C  CZ  . TYR A 1 34  ? 89.304  139.848 63.208  1.00 30.30  ? 234 TYR A CZ  1 
ATOM   153  N  N   . THR A 1 35  ? 84.596  138.480 60.235  1.00 32.20  ? 235 THR A N   1 
ATOM   154  C  CA  . THR A 1 35  ? 84.015  137.411 61.037  1.00 32.20  ? 235 THR A CA  1 
ATOM   155  C  C   . THR A 1 35  ? 84.660  136.093 60.638  1.00 32.20  ? 235 THR A C   1 
ATOM   156  O  O   . THR A 1 35  ? 85.444  136.025 59.689  1.00 32.20  ? 235 THR A O   1 
ATOM   157  C  CB  . THR A 1 35  ? 82.488  137.359 60.890  1.00 32.20  ? 235 THR A CB  1 
ATOM   158  O  OG1 . THR A 1 35  ? 81.915  136.730 62.043  1.00 32.20  ? 235 THR A OG1 1 
ATOM   159  C  CG2 . THR A 1 35  ? 82.087  136.588 59.644  1.00 32.20  ? 235 THR A CG2 1 
ATOM   160  N  N   . ILE A 1 36  ? 84.342  135.042 61.389  1.00 31.61  ? 236 ILE A N   1 
ATOM   161  C  CA  . ILE A 1 36  ? 84.901  133.713 61.162  1.00 31.61  ? 236 ILE A CA  1 
ATOM   162  C  C   . ILE A 1 36  ? 83.763  132.772 60.798  1.00 31.61  ? 236 ILE A C   1 
ATOM   163  O  O   . ILE A 1 36  ? 82.809  132.611 61.570  1.00 31.61  ? 236 ILE A O   1 
ATOM   164  C  CB  . ILE A 1 36  ? 85.667  133.197 62.390  1.00 31.61  ? 236 ILE A CB  1 
ATOM   165  C  CG1 . ILE A 1 36  ? 86.658  134.254 62.886  1.00 31.61  ? 236 ILE A CG1 1 
ATOM   166  C  CG2 . ILE A 1 36  ? 86.371  131.886 62.066  1.00 31.61  ? 236 ILE A CG2 1 
ATOM   167  C  CD1 . ILE A 1 36  ? 88.007  134.208 62.198  1.00 31.61  ? 236 ILE A CD1 1 
ATOM   168  N  N   . LYS A 1 37  ? 83.865  132.151 59.624  1.00 34.42  ? 237 LYS A N   1 
ATOM   169  C  CA  . LYS A 1 37  ? 82.916  131.140 59.173  1.00 34.42  ? 237 LYS A CA  1 
ATOM   170  C  C   . LYS A 1 37  ? 83.702  129.939 58.674  1.00 34.42  ? 237 LYS A C   1 
ATOM   171  O  O   . LYS A 1 37  ? 84.594  130.088 57.833  1.00 34.42  ? 237 LYS A O   1 
ATOM   172  C  CB  . LYS A 1 37  ? 82.004  131.684 58.069  1.00 34.42  ? 237 LYS A CB  1 
ATOM   173  C  CG  . LYS A 1 37  ? 81.041  132.764 58.532  1.00 34.42  ? 237 LYS A CG  1 
ATOM   174  C  CD  . LYS A 1 37  ? 80.171  133.254 57.386  1.00 34.42  ? 237 LYS A CD  1 
ATOM   175  C  CE  . LYS A 1 37  ? 79.135  134.254 57.870  1.00 34.42  ? 237 LYS A CE  1 
ATOM   176  N  NZ  . LYS A 1 37  ? 77.823  134.063 57.192  1.00 34.42  ? 237 LYS A NZ  1 
ATOM   177  N  N   . ASP A 1 38  ? 83.370  128.754 59.193  1.00 35.48  ? 238 ASP A N   1 
ATOM   178  C  CA  . ASP A 1 38  ? 84.047  127.509 58.821  1.00 35.48  ? 238 ASP A CA  1 
ATOM   179  C  C   . ASP A 1 38  ? 85.559  127.626 59.000  1.00 35.48  ? 238 ASP A C   1 
ATOM   180  O  O   . ASP A 1 38  ? 86.341  127.172 58.162  1.00 35.48  ? 238 ASP A O   1 
ATOM   181  C  CB  . ASP A 1 38  ? 83.693  127.098 57.392  1.00 35.48  ? 238 ASP A CB  1 
ATOM   182  C  CG  . ASP A 1 38  ? 82.351  126.396 57.302  1.00 35.48  ? 238 ASP A CG  1 
ATOM   183  O  OD1 . ASP A 1 38  ? 81.699  126.221 58.352  1.00 35.48  ? 238 ASP A OD1 1 
ATOM   184  O  OD2 . ASP A 1 38  ? 81.950  126.020 56.181  1.00 35.48  ? 238 ASP A OD2 1 
ATOM   185  N  N   . SER A 1 39  ? 85.968  128.254 60.105  1.00 34.63  ? 239 SER A N   1 
ATOM   186  C  CA  . SER A 1 39  ? 87.378  128.471 60.434  1.00 34.63  ? 239 SER A CA  1 
ATOM   187  C  C   . SER A 1 39  ? 88.098  129.277 59.357  1.00 34.63  ? 239 SER A C   1 
ATOM   188  O  O   . SER A 1 39  ? 89.298  129.100 59.131  1.00 34.63  ? 239 SER A O   1 
ATOM   189  C  CB  . SER A 1 39  ? 88.104  127.145 60.684  1.00 34.63  ? 239 SER A CB  1 
ATOM   190  O  OG  . SER A 1 39  ? 87.491  126.417 61.735  1.00 34.63  ? 239 SER A OG  1 
ATOM   191  N  N   . ILE A 1 40  ? 87.374  130.169 58.683  1.00 34.02  ? 240 ILE A N   1 
ATOM   192  C  CA  . ILE A 1 40  ? 87.939  131.039 57.657  1.00 34.02  ? 240 ILE A CA  1 
ATOM   193  C  C   . ILE A 1 40  ? 87.499  132.466 57.946  1.00 34.02  ? 240 ILE A C   1 
ATOM   194  O  O   . ILE A 1 40  ? 86.314  132.716 58.195  1.00 34.02  ? 240 ILE A O   1 
ATOM   195  C  CB  . ILE A 1 40  ? 87.505  130.614 56.240  1.00 34.02  ? 240 ILE A CB  1 
ATOM   196  C  CG1 . ILE A 1 40  ? 88.012  129.204 55.924  1.00 34.02  ? 240 ILE A CG1 1 
ATOM   197  C  CG2 . ILE A 1 40  ? 87.996  131.616 55.203  1.00 34.02  ? 240 ILE A CG2 1 
ATOM   198  C  CD1 . ILE A 1 40  ? 89.443  129.159 55.428  1.00 34.02  ? 240 ILE A CD1 1 
ATOM   199  N  N   . ALA A 1 41  ? 88.449  133.398 57.925  1.00 33.66  ? 241 ALA A N   1 
ATOM   200  C  CA  . ALA A 1 41  ? 88.138  134.802 58.142  1.00 33.66  ? 241 ALA A CA  1 
ATOM   201  C  C   . ALA A 1 41  ? 87.572  135.412 56.866  1.00 33.66  ? 241 ALA A C   1 
ATOM   202  O  O   . ALA A 1 41  ? 88.202  135.348 55.805  1.00 33.66  ? 241 ALA A O   1 
ATOM   203  C  CB  . ALA A 1 41  ? 89.384  135.565 58.590  1.00 33.66  ? 241 ALA A CB  1 
ATOM   204  N  N   . VAL A 1 42  ? 86.382  136.004 56.970  1.00 33.46  ? 242 VAL A N   1 
ATOM   205  C  CA  . VAL A 1 42  ? 85.702  136.604 55.832  1.00 33.46  ? 242 VAL A CA  1 
ATOM   206  C  C   . VAL A 1 42  ? 85.305  138.032 56.180  1.00 33.46  ? 242 VAL A C   1 
ATOM   207  O  O   . VAL A 1 42  ? 85.190  138.412 57.350  1.00 33.46  ? 242 VAL A O   1 
ATOM   208  C  CB  . VAL A 1 42  ? 84.461  135.794 55.385  1.00 33.46  ? 242 VAL A CB  1 
ATOM   209  C  CG1 . VAL A 1 42  ? 84.786  134.309 55.299  1.00 33.46  ? 242 VAL A CG1 1 
ATOM   210  C  CG2 . VAL A 1 42  ? 83.292  136.037 56.322  1.00 33.46  ? 242 VAL A CG2 1 
ATOM   211  N  N   . LYS A 1 43  ? 85.103  138.826 55.129  1.00 34.82  ? 243 LYS A N   1 
ATOM   212  C  CA  . LYS A 1 43  ? 84.751  140.231 55.286  1.00 34.82  ? 243 LYS A CA  1 
ATOM   213  C  C   . LYS A 1 43  ? 83.377  140.372 55.931  1.00 34.82  ? 243 LYS A C   1 
ATOM   214  O  O   . LYS A 1 43  ? 82.444  139.626 55.619  1.00 34.82  ? 243 LYS A O   1 
ATOM   215  C  CB  . LYS A 1 43  ? 84.777  140.925 53.923  1.00 34.82  ? 243 LYS A CB  1 
ATOM   216  C  CG  . LYS A 1 43  ? 84.313  142.372 53.928  1.00 34.82  ? 243 LYS A CG  1 
ATOM   217  C  CD  . LYS A 1 43  ? 85.091  143.194 52.912  1.00 34.82  ? 243 LYS A CD  1 
ATOM   218  C  CE  . LYS A 1 43  ? 84.170  143.816 51.876  1.00 34.82  ? 243 LYS A CE  1 
ATOM   219  N  NZ  . LYS A 1 43  ? 83.390  144.956 52.432  1.00 34.82  ? 243 LYS A NZ  1 
ATOM   220  N  N   . TRP A 1 44  ? 83.097  141.234 56.794  1.00 35.00  ? 244 TRP A N   1 
ATOM   221  C  CA  . TRP A 1 44  ? 81.829  141.565 57.403  1.00 35.00  ? 244 TRP A CA  1 
ATOM   222  C  C   . TRP A 1 44  ? 80.698  142.171 56.557  1.00 35.00  ? 244 TRP A C   1 
ATOM   223  O  O   . TRP A 1 44  ? 80.847  143.174 55.979  1.00 35.00  ? 244 TRP A O   1 
ATOM   224  C  CB  . TRP A 1 44  ? 82.122  142.424 58.564  1.00 30.00  ? 244 TRP A CB  1 
ATOM   225  C  CG  . TRP A 1 44  ? 80.914  142.798 59.361  1.00 30.00  ? 244 TRP A CG  1 
ATOM   226  C  CD1 . TRP A 1 44  ? 80.201  143.956 59.336  1.00 30.00  ? 244 TRP A CD1 1 
ATOM   227  C  CD2 . TRP A 1 44  ? 80.219  141.930 60.262  1.00 30.00  ? 244 TRP A CD2 1 
ATOM   228  N  NE1 . TRP A 1 44  ? 79.125  143.869 60.153  1.00 30.00  ? 244 TRP A NE1 1 
ATOM   229  C  CE2 . TRP A 1 44  ? 79.112  142.647 60.744  1.00 30.00  ? 244 TRP A CE2 1 
ATOM   230  C  CE3 . TRP A 1 44  ? 80.442  140.632 60.712  1.00 30.00  ? 244 TRP A CE3 1 
ATOM   231  C  CZ2 . TRP A 1 44  ? 78.229  142.102 61.659  1.00 30.00  ? 244 TRP A CZ2 1 
ATOM   232  C  CZ3 . TRP A 1 44  ? 79.551  140.096 61.604  1.00 30.00  ? 244 TRP A CZ3 1 
ATOM   233  C  CH2 . TRP A 1 44  ? 78.461  140.819 62.060  1.00 30.00  ? 244 TRP A CH2 1 
ATOM   234  N  N   . ASN A 1 45  ? 79.541  141.578 56.627  1.00 40.00  ? 245 ASN A N   1 
ATOM   235  C  CA  . ASN A 1 45  ? 78.316  142.112 56.069  1.00 40.00  ? 245 ASN A CA  1 
ATOM   236  C  C   . ASN A 1 45  ? 77.496  142.249 57.276  1.00 40.00  ? 245 ASN A C   1 
ATOM   237  O  O   . ASN A 1 45  ? 77.597  141.453 58.092  1.00 40.00  ? 245 ASN A O   1 
ATOM   238  C  CB  . ASN A 1 45  ? 77.597  141.231 55.033  1.00 40.00  ? 245 ASN A CB  1 
ATOM   239  C  CG  . ASN A 1 45  ? 76.654  141.896 54.081  1.00 40.00  ? 245 ASN A CG  1 
ATOM   240  O  OD1 . ASN A 1 45  ? 75.862  142.744 54.459  1.00 40.00  ? 245 ASN A OD1 1 
ATOM   241  N  ND2 . ASN A 1 45  ? 76.720  141.472 52.842  1.00 40.00  ? 245 ASN A ND2 1 
ATOM   242  N  N   . ASP A 1 46  ? 76.625  143.193 57.275  1.00 43.40  ? 246 ASP A N   1 
ATOM   243  C  CA  . ASP A 1 46  ? 75.641  143.521 58.301  1.00 43.40  ? 246 ASP A CA  1 
ATOM   244  C  C   . ASP A 1 46  ? 74.611  142.415 58.497  1.00 43.40  ? 246 ASP A C   1 
ATOM   245  O  O   . ASP A 1 46  ? 74.261  142.109 59.643  1.00 43.40  ? 246 ASP A O   1 
ATOM   246  C  CB  . ASP A 1 46  ? 74.939  144.835 57.956  1.00 43.40  ? 246 ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 46  ? 75.762  146.052 58.340  1.00 43.40  ? 246 ASP A CG  1 
ATOM   248  O  OD1 . ASP A 1 46  ? 76.574  146.508 57.509  1.00 43.40  ? 246 ASP A OD1 1 
ATOM   249  O  OD2 . ASP A 1 46  ? 75.597  146.549 59.473  1.00 43.40  ? 246 ASP A OD2 1 
ATOM   250  N  N   . SER A 1 47  ? 74.132  141.804 57.411  1.00 43.72  ? 247 SER A N   1 
ATOM   251  C  CA  . SER A 1 47  ? 73.161  140.721 57.507  1.00 43.72  ? 247 SER A CA  1 
ATOM   252  C  C   . SER A 1 47  ? 73.654  139.560 58.360  1.00 43.72  ? 247 SER A C   1 
ATOM   253  O  O   . SER A 1 47  ? 72.830  138.884 58.989  1.00 43.72  ? 247 SER A O   1 
ATOM   254  C  CB  . SER A 1 47  ? 72.801  140.214 56.109  1.00 43.72  ? 247 SER A CB  1 
ATOM   255  O  OG  . SER A 1 47  ? 73.951  139.743 55.429  1.00 43.72  ? 247 SER A OG  1 
ATOM   256  N  N   . PHE A 1 48  ? 74.969  139.326 58.408  1.00 40.71  ? 248 PHE A N   1 
ATOM   257  C  CA  . PHE A 1 48  ? 75.522  138.282 59.261  1.00 40.71  ? 248 PHE A CA  1 
ATOM   258  C  C   . PHE A 1 48  ? 75.117  138.458 60.716  1.00 40.71  ? 248 PHE A C   1 
ATOM   259  O  O   . PHE A 1 48  ? 74.951  137.459 61.426  1.00 40.71  ? 248 PHE A O   1 
ATOM   260  C  CB  . PHE A 1 48  ? 77.050  138.264 59.162  1.00 40.71  ? 248 PHE A CB  1 
ATOM   261  C  CG  . PHE A 1 48  ? 77.571  137.858 57.815  1.00 40.71  ? 248 PHE A CG  1 
ATOM   262  C  CD1 . PHE A 1 48  ? 76.730  137.310 56.861  1.00 40.71  ? 248 PHE A CD1 1 
ATOM   263  C  CD2 . PHE A 1 48  ? 78.910  138.022 57.504  1.00 40.71  ? 248 PHE A CD2 1 
ATOM   264  C  CE1 . PHE A 1 48  ? 77.214  136.937 55.625  1.00 40.71  ? 248 PHE A CE1 1 
ATOM   265  C  CE2 . PHE A 1 48  ? 79.399  137.650 56.269  1.00 40.71  ? 248 PHE A CE2 1 
ATOM   266  C  CZ  . PHE A 1 48  ? 78.550  137.107 55.328  1.00 40.71  ? 248 PHE A CZ  1 
ATOM   267  N  N   . ALA A 1 49  ? 74.947  139.703 61.170  1.00 43.33  ? 249 ALA A N   1 
ATOM   268  C  CA  . ALA A 1 49  ? 74.568  139.942 62.557  1.00 43.33  ? 249 ALA A CA  1 
ATOM   269  C  C   . ALA A 1 49  ? 73.210  139.336 62.881  1.00 43.33  ? 249 ALA A C   1 
ATOM   270  O  O   . ALA A 1 49  ? 72.928  139.040 64.048  1.00 43.33  ? 249 ALA A O   1 
ATOM   271  C  CB  . ALA A 1 49  ? 74.562  141.442 62.849  1.00 43.33  ? 249 ALA A CB  1 
ATOM   272  N  N   . GLU A 1 50  ? 72.358  139.141 61.869  1.00 46.59  ? 250 GLU A N   1 
ATOM   273  C  CA  . GLU A 1 50  ? 71.065  138.517 62.119  1.00 46.59  ? 250 GLU A CA  1 
ATOM   274  C  C   . GLU A 1 50  ? 71.205  137.026 62.398  1.00 46.59  ? 250 GLU A C   1 
ATOM   275  O  O   . GLU A 1 50  ? 70.342  136.441 63.063  1.00 46.59  ? 250 GLU A O   1 
ATOM   276  C  CB  . GLU A 1 50  ? 70.119  138.761 60.941  1.00 46.59  ? 250 GLU A CB  1 
ATOM   277  C  CG  . GLU A 1 50  ? 68.673  138.225 61.074  1.00 46.59  ? 250 GLU A CG  1 
ATOM   278  C  CD  . GLU A 1 50  ? 67.747  138.532 59.894  1.00 46.59  ? 250 GLU A CD  1 
ATOM   279  O  OE1 . GLU A 1 50  ? 68.184  139.144 58.895  1.00 46.59  ? 250 GLU A OE1 1 
ATOM   280  O  OE2 . GLU A 1 50  ? 66.556  138.158 59.981  1.00 46.59  ? 250 GLU A OE2 1 
ATOM   281  N  N   . GLN A 1 51  ? 72.275  136.400 61.917  1.00 43.71  ? 251 GLN A N   1 
ATOM   282  C  CA  . GLN A 1 51  ? 72.498  134.980 62.150  1.00 43.71  ? 251 GLN A CA  1 
ATOM   283  C  C   . GLN A 1 51  ? 73.288  134.702 63.422  1.00 43.71  ? 251 GLN A C   1 
ATOM   284  O  O   . GLN A 1 51  ? 73.578  133.536 63.710  1.00 43.71  ? 251 GLN A O   1 
ATOM   285  C  CB  . GLN A 1 51  ? 73.217  134.348 60.955  1.00 43.71  ? 251 GLN A CB  1 
ATOM   286  C  CG  . GLN A 1 51  ? 72.821  134.922 59.607  1.00 43.71  ? 251 GLN A CG  1 
ATOM   287  C  CD  . GLN A 1 51  ? 73.789  134.527 58.510  1.00 43.71  ? 251 GLN A CD  1 
ATOM   288  O  OE1 . GLN A 1 51  ? 74.330  135.377 57.806  1.00 43.71  ? 251 GLN A OE1 1 
ATOM   289  N  NE2 . GLN A 1 51  ? 74.010  133.226 58.361  1.00 43.71  ? 251 GLN A NE2 1 
ATOM   290  N  N   . GLY A 1 52  ? 73.641  135.733 64.182  1.00 39.69  ? 252 GLY A N   1 
ATOM   291  C  CA  . GLY A 1 52  ? 74.361  135.563 65.425  1.00 39.69  ? 252 GLY A CA  1 
ATOM   292  C  C   . GLY A 1 52  ? 75.851  135.810 65.361  1.00 39.69  ? 252 GLY A C   1 
ATOM   293  O  O   . GLY A 1 52  ? 76.531  135.633 66.378  1.00 39.69  ? 252 GLY A O   1 
ATOM   294  N  N   . TYR A 1 53  ? 76.379  136.210 64.208  1.00 36.18  ? 253 TYR A N   1 
ATOM   295  C  CA  . TYR A 1 53  ? 77.803  136.473 64.080  1.00 36.18  ? 253 TYR A CA  1 
ATOM   296  C  C   . TYR A 1 53  ? 78.157  137.822 64.696  1.00 36.18  ? 253 TYR A C   1 
ATOM   297  O  O   . TYR A 1 53  ? 77.329  138.735 64.764  1.00 36.18  ? 253 TYR A O   1 
ATOM   298  C  CB  . TYR A 1 53  ? 78.223  136.437 62.610  1.00 36.18  ? 253 TYR A CB  1 
ATOM   299  C  CG  . TYR A 1 53  ? 78.185  135.053 62.007  1.00 36.18  ? 253 TYR A CG  1 
ATOM   300  C  CD1 . TYR A 1 53  ? 79.254  134.179 62.161  1.00 36.18  ? 253 TYR A CD1 1 
ATOM   301  C  CD2 . TYR A 1 53  ? 77.081  134.618 61.287  1.00 36.18  ? 253 TYR A CD2 1 
ATOM   302  C  CE1 . TYR A 1 53  ? 79.223  132.912 61.611  1.00 36.18  ? 253 TYR A CE1 1 
ATOM   303  C  CE2 . TYR A 1 53  ? 77.042  133.353 60.734  1.00 36.18  ? 253 TYR A CE2 1 
ATOM   304  C  CZ  . TYR A 1 53  ? 78.115  132.504 60.899  1.00 36.18  ? 253 TYR A CZ  1 
ATOM   305  N  N   . LYS A 1 54  ? 79.403  137.938 65.146  1.00 33.96  ? 254 LYS A N   1 
ATOM   306  C  CA  . LYS A 1 54  ? 79.888  139.133 65.822  1.00 33.96  ? 254 LYS A CA  1 
ATOM   307  C  C   . LYS A 1 54  ? 80.960  139.808 64.981  1.00 33.96  ? 254 LYS A C   1 
ATOM   308  O  O   . LYS A 1 54  ? 81.823  139.142 64.401  1.00 33.96  ? 254 LYS A O   1 
ATOM   309  C  CB  . LYS A 1 54  ? 80.450  138.793 67.207  1.00 33.96  ? 254 LYS A CB  1 
ATOM   310  C  CG  . LYS A 1 54  ? 79.387  138.559 68.267  1.00 33.96  ? 254 LYS A CG  1 
ATOM   311  C  CD  . LYS A 1 54  ? 79.957  137.818 69.465  1.00 33.96  ? 254 LYS A CD  1 
ATOM   312  C  CE  . LYS A 1 54  ? 79.004  137.864 70.648  1.00 33.96  ? 254 LYS A CE  1 
ATOM   313  N  NZ  . LYS A 1 54  ? 77.661  137.327 70.298  1.00 33.96  ? 254 LYS A NZ  1 
ATOM   314  N  N   . LYS A 1 55  ? 80.897  141.137 64.919  1.00 31.24  ? 255 LYS A N   1 
ATOM   315  C  CA  . LYS A 1 55  ? 81.882  141.917 64.187  1.00 31.24  ? 255 LYS A CA  1 
ATOM   316  C  C   . LYS A 1 55  ? 83.145  142.087 65.023  1.00 31.24  ? 255 LYS A C   1 
ATOM   317  O  O   . LYS A 1 55  ? 83.080  142.396 66.216  1.00 31.24  ? 255 LYS A O   1 
ATOM   318  C  CB  . LYS A 1 55  ? 81.305  143.282 63.815  1.00 31.24  ? 255 LYS A CB  1 
ATOM   319  C  CG  . LYS A 1 55  ? 82.140  144.083 62.833  1.00 31.24  ? 255 LYS A CG  1 
ATOM   320  C  CD  . LYS A 1 55  ? 81.596  145.496 62.692  1.00 31.24  ? 255 LYS A CD  1 
ATOM   321  C  CE  . LYS A 1 55  ? 82.300  146.260 61.585  1.00 31.24  ? 255 LYS A CE  1 
ATOM   322  N  NZ  . LYS A 1 55  ? 82.933  147.509 62.087  1.00 31.24  ? 255 LYS A NZ  1 
ATOM   323  N  N   . TYR A 1 56  ? 84.297  141.885 64.389  1.00 30.14  ? 256 TYR A N   1 
ATOM   324  C  CA  . TYR A 1 56  ? 85.585  141.932 65.066  1.00 30.14  ? 256 TYR A CA  1 
ATOM   325  C  C   . TYR A 1 56  ? 86.503  142.938 64.387  1.00 30.14  ? 256 TYR A C   1 
ATOM   326  O  O   . TYR A 1 56  ? 86.495  143.074 63.160  1.00 30.14  ? 256 TYR A O   1 
ATOM   327  C  CB  . TYR A 1 56  ? 86.257  140.554 65.081  1.00 30.14  ? 256 TYR A CB  1 
ATOM   328  C  CG  . TYR A 1 56  ? 85.533  139.522 65.915  1.00 30.14  ? 256 TYR A CG  1 
ATOM   329  C  CD1 . TYR A 1 56  ? 85.200  139.778 67.239  1.00 30.14  ? 256 TYR A CD1 1 
ATOM   330  C  CD2 . TYR A 1 56  ? 85.189  138.288 65.381  1.00 30.14  ? 256 TYR A CD2 1 
ATOM   331  C  CE1 . TYR A 1 56  ? 84.541  138.837 68.005  1.00 30.14  ? 256 TYR A CE1 1 
ATOM   332  C  CE2 . TYR A 1 56  ? 84.529  137.340 66.139  1.00 30.14  ? 256 TYR A CE2 1 
ATOM   333  C  CZ  . TYR A 1 56  ? 84.208  137.619 67.450  1.00 30.14  ? 256 TYR A CZ  1 
ATOM   334  N  N   . VAL A 1 57  ? 87.286  143.646 65.198  1.00 29.04  ? 257 VAL A N   1 
ATOM   335  C  CA  . VAL A 1 57  ? 88.314  144.559 64.718  1.00 29.04  ? 257 VAL A CA  1 
ATOM   336  C  C   . VAL A 1 57  ? 89.568  144.347 65.553  1.00 29.04  ? 257 VAL A C   1 
ATOM   337  O  O   . VAL A 1 57  ? 89.497  144.075 66.756  1.00 29.04  ? 257 VAL A O   1 
ATOM   338  C  CB  . VAL A 1 57  ? 87.862  146.036 64.778  1.00 29.04  ? 257 VAL A CB  1 
ATOM   339  C  CG1 . VAL A 1 57  ? 86.883  146.341 63.655  1.00 29.04  ? 257 VAL A CG1 1 
ATOM   340  C  CG2 . VAL A 1 57  ? 87.245  146.350 66.131  1.00 29.04  ? 257 VAL A CG2 1 
ATOM   341  N  N   . SER A 1 58  ? 90.723  144.467 64.905  1.00 29.06  ? 258 SER A N   1 
ATOM   342  C  CA  . SER A 1 58  ? 92.000  144.260 65.577  1.00 29.06  ? 258 SER A CA  1 
ATOM   343  C  C   . SER A 1 58  ? 93.075  145.028 64.822  1.00 29.06  ? 258 SER A C   1 
ATOM   344  O  O   . SER A 1 58  ? 92.830  145.596 63.754  1.00 29.06  ? 258 SER A O   1 
ATOM   345  C  CB  . SER A 1 58  ? 92.339  142.769 65.675  1.00 29.06  ? 258 SER A CB  1 
ATOM   346  O  OG  . SER A 1 58  ? 91.865  142.063 64.542  1.00 29.06  ? 258 SER A OG  1 
ATOM   347  N  N   . SER A 1 59  ? 94.278  145.044 65.393  1.00 29.02  ? 259 SER A N   1 
ATOM   348  C  CA  . SER A 1 59  ? 95.416  145.729 64.795  1.00 29.02  ? 259 SER A CA  1 
ATOM   349  C  C   . SER A 1 59  ? 96.059  144.836 63.743  1.00 29.02  ? 259 SER A C   1 
ATOM   350  O  O   . SER A 1 59  ? 96.364  143.669 64.010  1.00 29.02  ? 259 SER A O   1 
ATOM   351  C  CB  . SER A 1 59  ? 96.438  146.108 65.866  1.00 29.02  ? 259 SER A CB  1 
ATOM   352  O  OG  . SER A 1 59  ? 97.580  146.714 65.290  1.00 29.02  ? 259 SER A OG  1 
ATOM   353  N  N   . TYR A 1 60  ? 96.267  145.389 62.548  1.00 30.81  ? 260 TYR A N   1 
ATOM   354  C  CA  . TYR A 1 60  ? 96.894  144.641 61.467  1.00 30.81  ? 260 TYR A CA  1 
ATOM   355  C  C   . TYR A 1 60  ? 98.412  144.604 61.576  1.00 30.81  ? 260 TYR A C   1 
ATOM   356  O  O   . TYR A 1 60  ? 99.057  143.913 60.779  1.00 30.81  ? 260 TYR A O   1 
ATOM   357  C  CB  . TYR A 1 60  ? 96.476  145.224 60.112  1.00 30.81  ? 260 TYR A CB  1 
ATOM   358  C  CG  . TYR A 1 60  ? 97.125  146.545 59.763  1.00 30.81  ? 260 TYR A CG  1 
ATOM   359  C  CD1 . TYR A 1 60  ? 96.586  147.743 60.213  1.00 30.81  ? 260 TYR A CD1 1 
ATOM   360  C  CD2 . TYR A 1 60  ? 98.261  146.598 58.965  1.00 30.81  ? 260 TYR A CD2 1 
ATOM   361  C  CE1 . TYR A 1 60  ? 97.170  148.954 59.893  1.00 30.81  ? 260 TYR A CE1 1 
ATOM   362  C  CE2 . TYR A 1 60  ? 98.851  147.804 58.640  1.00 30.81  ? 260 TYR A CE2 1 
ATOM   363  C  CZ  . TYR A 1 60  ? 98.301  148.979 59.105  1.00 30.81  ? 260 TYR A CZ  1 
ATOM   364  N  N   . LEU A 1 61  ? 98.995  145.324 62.534  1.00 30.65  ? 261 LEU A N   1 
ATOM   365  C  CA  . LEU A 1 61  ? 100.431 145.286 62.773  1.00 30.65  ? 261 LEU A CA  1 
ATOM   366  C  C   . LEU A 1 61  ? 100.808 144.477 64.006  1.00 30.65  ? 261 LEU A C   1 
ATOM   367  O  O   . LEU A 1 61  ? 102.003 144.296 64.264  1.00 30.65  ? 261 LEU A O   1 
ATOM   368  C  CB  . LEU A 1 61  ? 100.984 146.710 62.915  1.00 30.65  ? 261 LEU A CB  1 
ATOM   369  C  CG  . LEU A 1 61  ? 101.200 147.495 61.618  1.00 30.65  ? 261 LEU A CG  1 
ATOM   370  C  CD1 . LEU A 1 61  ? 101.706 148.896 61.917  1.00 30.65  ? 261 LEU A CD1 1 
ATOM   371  C  CD2 . LEU A 1 61  ? 102.161 146.759 60.697  1.00 30.65  ? 261 LEU A CD2 1 
ATOM   372  N  N   . GLU A 1 62  ? 99.831  143.989 64.768  1.00 28.05  ? 262 GLU A N   1 
ATOM   373  C  CA  . GLU A 1 62  ? 100.082 143.214 65.977  1.00 28.05  ? 262 GLU A CA  1 
ATOM   374  C  C   . GLU A 1 62  ? 99.346  141.887 65.869  1.00 28.05  ? 262 GLU A C   1 
ATOM   375  O  O   . GLU A 1 62  ? 98.138  141.867 65.609  1.00 28.05  ? 262 GLU A O   1 
ATOM   376  C  CB  . GLU A 1 62  ? 99.631  143.977 67.226  1.00 28.05  ? 262 GLU A CB  1 
ATOM   377  C  CG  . GLU A 1 62  ? 100.590 143.879 68.399  1.00 28.05  ? 262 GLU A CG  1 
ATOM   378  C  CD  . GLU A 1 62  ? 101.978 144.388 68.062  1.00 28.05  ? 262 GLU A CD  1 
ATOM   379  O  OE1 . GLU A 1 62  ? 102.091 145.540 67.594  1.00 28.05  ? 262 GLU A OE1 1 
ATOM   380  O  OE2 . GLU A 1 62  ? 102.954 143.637 68.266  1.00 28.05  ? 262 GLU A OE2 1 
ATOM   381  N  N   . SER A 1 63  ? 100.071 140.786 66.071  1.00 24.37  ? 263 SER A N   1 
ATOM   382  C  CA  . SER A 1 63  ? 99.435  139.473 66.049  1.00 24.37  ? 263 SER A CA  1 
ATOM   383  C  C   . SER A 1 63  ? 98.621  139.226 67.312  1.00 24.37  ? 263 SER A C   1 
ATOM   384  O  O   . SER A 1 63  ? 97.605  138.523 67.266  1.00 24.37  ? 263 SER A O   1 
ATOM   385  C  CB  . SER A 1 63  ? 100.488 138.380 65.870  1.00 24.37  ? 263 SER A CB  1 
ATOM   386  O  OG  . SER A 1 63  ? 101.211 138.165 67.069  1.00 24.37  ? 263 SER A OG  1 
ATOM   387  N  N   . ASN A 1 64  ? 99.045  139.790 68.440  1.00 22.96  ? 264 ASN A N   1 
ATOM   388  C  CA  . ASN A 1 64  ? 98.338  139.687 69.714  1.00 22.96  ? 264 ASN A CA  1 
ATOM   389  C  C   . ASN A 1 64  ? 97.987  141.109 70.146  1.00 22.96  ? 264 ASN A C   1 
ATOM   390  O  O   . ASN A 1 64  ? 98.773  141.775 70.822  1.00 22.96  ? 264 ASN A O   1 
ATOM   391  C  CB  . ASN A 1 64  ? 99.183  138.967 70.767  1.00 22.96  ? 264 ASN A CB  1 
ATOM   392  C  CG  . ASN A 1 64  ? 99.616  137.584 70.322  1.00 22.96  ? 264 ASN A CG  1 
ATOM   393  O  OD1 . ASN A 1 64  ? 100.192 137.416 69.248  1.00 22.96  ? 264 ASN A OD1 1 
ATOM   394  N  ND2 . ASN A 1 64  ? 99.340  136.583 71.151  1.00 22.96  ? 264 ASN A ND2 1 
ATOM   395  N  N   . THR A 1 65  ? 96.800  141.570 69.742  1.00 23.53  ? 265 THR A N   1 
ATOM   396  C  CA  . THR A 1 65  ? 96.402  142.946 70.027  1.00 23.53  ? 265 THR A CA  1 
ATOM   397  C  C   . THR A 1 65  ? 96.251  143.188 71.525  1.00 23.53  ? 265 THR A C   1 
ATOM   398  O  O   . THR A 1 65  ? 96.694  144.220 72.041  1.00 23.53  ? 265 THR A O   1 
ATOM   399  C  CB  . THR A 1 65  ? 95.098  143.273 69.298  1.00 23.53  ? 265 THR A CB  1 
ATOM   400  O  OG1 . THR A 1 65  ? 95.277  143.090 67.888  1.00 23.53  ? 265 THR A OG1 1 
ATOM   401  C  CG2 . THR A 1 65  ? 94.678  144.709 69.566  1.00 23.53  ? 265 THR A CG2 1 
ATOM   402  N  N   . ALA A 1 66  ? 95.638  142.246 72.239  1.00 21.90  ? 266 ALA A N   1 
ATOM   403  C  CA  . ALA A 1 66  ? 95.381  142.414 73.664  1.00 21.90  ? 266 ALA A CA  1 
ATOM   404  C  C   . ALA A 1 66  ? 96.570  142.036 74.539  1.00 21.90  ? 266 ALA A C   1 
ATOM   405  O  O   . ALA A 1 66  ? 96.504  142.228 75.758  1.00 21.90  ? 266 ALA A O   1 
ATOM   406  C  CB  . ALA A 1 66  ? 94.157  141.593 74.075  1.00 21.90  ? 266 ALA A CB  1 
ATOM   407  N  N   . GLY A 1 67  ? 97.646  141.507 73.958  1.00 21.07  ? 267 GLY A N   1 
ATOM   408  C  CA  . GLY A 1 67  ? 98.831  141.175 74.721  1.00 21.07  ? 267 GLY A CA  1 
ATOM   409  C  C   . GLY A 1 67  ? 98.770  139.874 75.489  1.00 21.07  ? 267 GLY A C   1 
ATOM   410  O  O   . GLY A 1 67  ? 99.649  139.627 76.324  1.00 21.07  ? 267 GLY A O   1 
ATOM   411  N  N   . ASP A 1 68  ? 97.774  139.041 75.243  1.00 21.57  ? 268 ASP A N   1 
ATOM   412  C  CA  . ASP A 1 68  ? 97.630  137.743 75.880  1.00 21.57  ? 268 ASP A CA  1 
ATOM   413  C  C   . ASP A 1 68  ? 98.269  136.660 75.019  1.00 21.57  ? 268 ASP A C   1 
ATOM   414  O  O   . ASP A 1 68  ? 98.526  136.863 73.829  1.00 21.57  ? 268 ASP A O   1 
ATOM   415  C  CB  . ASP A 1 68  ? 96.147  137.449 76.130  1.00 21.57  ? 268 ASP A CB  1 
ATOM   416  C  CG  . ASP A 1 68  ? 95.325  137.477 74.864  1.00 21.57  ? 268 ASP A CG  1 
ATOM   417  O  OD1 . ASP A 1 68  ? 95.385  136.503 74.087  1.00 21.57  ? 268 ASP A OD1 1 
ATOM   418  O  OD2 . ASP A 1 68  ? 94.617  138.481 74.645  1.00 21.57  ? 268 ASP A OD2 1 
ATOM   419  N  N   . PRO A 1 69  ? 98.555  135.479 75.598  1.00 19.90  ? 269 PRO A N   1 
ATOM   420  C  CA  . PRO A 1 69  ? 99.283  134.443 74.843  1.00 19.90  ? 269 PRO A CA  1 
ATOM   421  C  C   . PRO A 1 69  ? 98.558  133.904 73.616  1.00 19.90  ? 269 PRO A C   1 
ATOM   422  O  O   . PRO A 1 69  ? 99.085  133.017 72.936  1.00 19.90  ? 269 PRO A O   1 
ATOM   423  C  CB  . PRO A 1 69  ? 99.488  133.328 75.881  1.00 19.90  ? 269 PRO A CB  1 
ATOM   424  C  CG  . PRO A 1 69  ? 98.588  133.660 77.025  1.00 19.90  ? 269 PRO A CG  1 
ATOM   425  C  CD  . PRO A 1 69  ? 98.445  135.138 77.026  1.00 19.90  ? 269 PRO A CD  1 
ATOM   426  N  N   . TYR A 1 70  ? 97.368  134.413 73.315  1.00 21.09  ? 270 TYR A N   1 
ATOM   427  C  CA  . TYR A 1 70  ? 96.587  133.950 72.177  1.00 21.09  ? 270 TYR A CA  1 
ATOM   428  C  C   . TYR A 1 70  ? 96.490  135.047 71.126  1.00 21.09  ? 270 TYR A C   1 
ATOM   429  O  O   . TYR A 1 70  ? 96.301  136.223 71.456  1.00 21.09  ? 270 TYR A O   1 
ATOM   430  C  CB  . TYR A 1 70  ? 95.189  133.506 72.616  1.00 21.09  ? 270 TYR A CB  1 
ATOM   431  C  CG  . TYR A 1 70  ? 95.207  132.505 73.748  1.00 21.09  ? 270 TYR A CG  1 
ATOM   432  C  CD1 . TYR A 1 70  ? 95.644  131.204 73.539  1.00 21.09  ? 270 TYR A CD1 1 
ATOM   433  C  CD2 . TYR A 1 70  ? 94.797  132.862 75.025  1.00 21.09  ? 270 TYR A CD2 1 
ATOM   434  C  CE1 . TYR A 1 70  ? 95.667  130.285 74.570  1.00 21.09  ? 270 TYR A CE1 1 
ATOM   435  C  CE2 . TYR A 1 70  ? 94.817  131.950 76.063  1.00 21.09  ? 270 TYR A CE2 1 
ATOM   436  C  CZ  . TYR A 1 70  ? 95.253  130.662 75.828  1.00 21.09  ? 270 TYR A CZ  1 
ATOM   437  N  N   . THR A 1 71  ? 96.625  134.657 69.862  1.00 22.80  ? 271 THR A N   1 
ATOM   438  C  CA  . THR A 1 71  ? 96.591  135.603 68.758  1.00 22.80  ? 271 THR A CA  1 
ATOM   439  C  C   . THR A 1 71  ? 95.151  136.005 68.438  1.00 22.80  ? 271 THR A C   1 
ATOM   440  O  O   . THR A 1 71  ? 94.186  135.445 68.964  1.00 22.80  ? 271 THR A O   1 
ATOM   441  C  CB  . THR A 1 71  ? 97.263  135.012 67.520  1.00 22.80  ? 271 THR A CB  1 
ATOM   442  O  OG1 . THR A 1 71  ? 96.373  134.085 66.885  1.00 22.80  ? 271 THR A OG1 1 
ATOM   443  C  CG2 . THR A 1 71  ? 98.547  134.292 67.903  1.00 22.80  ? 271 THR A CG2 1 
ATOM   444  N  N   . ASP A 1 72  ? 95.020  137.000 67.557  1.00 25.05  ? 272 ASP A N   1 
ATOM   445  C  CA  . ASP A 1 72  ? 93.698  137.506 67.197  1.00 25.05  ? 272 ASP A CA  1 
ATOM   446  C  C   . ASP A 1 72  ? 92.858  136.432 66.515  1.00 25.05  ? 272 ASP A C   1 
ATOM   447  O  O   . ASP A 1 72  ? 91.672  136.272 66.827  1.00 25.05  ? 272 ASP A O   1 
ATOM   448  C  CB  . ASP A 1 72  ? 93.836  138.730 66.293  1.00 25.05  ? 272 ASP A CB  1 
ATOM   449  C  CG  . ASP A 1 72  ? 94.515  139.893 66.988  1.00 25.05  ? 272 ASP A CG  1 
ATOM   450  O  OD1 . ASP A 1 72  ? 94.413  139.990 68.228  1.00 25.05  ? 272 ASP A OD1 1 
ATOM   451  O  OD2 . ASP A 1 72  ? 95.152  140.711 66.292  1.00 25.05  ? 272 ASP A OD2 1 
ATOM   452  N  N   . TYR A 1 73  ? 93.454  135.687 65.580  1.00 26.32  ? 273 TYR A N   1 
ATOM   453  C  CA  . TYR A 1 73  ? 92.712  134.638 64.888  1.00 26.32  ? 273 TYR A CA  1 
ATOM   454  C  C   . TYR A 1 73  ? 92.322  133.515 65.839  1.00 26.32  ? 273 TYR A C   1 
ATOM   455  O  O   . TYR A 1 73  ? 91.220  132.965 65.736  1.00 26.32  ? 273 TYR A O   1 
ATOM   456  C  CB  . TYR A 1 73  ? 93.533  134.091 63.721  1.00 26.32  ? 273 TYR A CB  1 
ATOM   457  C  CG  . TYR A 1 73  ? 92.871  132.931 63.010  1.00 26.32  ? 273 TYR A CG  1 
ATOM   458  C  CD1 . TYR A 1 73  ? 91.838  133.145 62.106  1.00 26.32  ? 273 TYR A CD1 1 
ATOM   459  C  CD2 . TYR A 1 73  ? 93.274  131.623 63.248  1.00 26.32  ? 273 TYR A CD2 1 
ATOM   460  C  CE1 . TYR A 1 73  ? 91.228  132.088 61.456  1.00 26.32  ? 273 TYR A CE1 1 
ATOM   461  C  CE2 . TYR A 1 73  ? 92.669  130.562 62.603  1.00 26.32  ? 273 TYR A CE2 1 
ATOM   462  C  CZ  . TYR A 1 73  ? 91.647  130.801 61.709  1.00 26.32  ? 273 TYR A CZ  1 
ATOM   463  N  N   . GLN A 1 74  ? 93.213  133.159 66.767  1.00 23.96  ? 274 GLN A N   1 
ATOM   464  C  CA  . GLN A 1 74  ? 92.910  132.093 67.717  1.00 23.96  ? 274 GLN A CA  1 
ATOM   465  C  C   . GLN A 1 74  ? 91.716  132.457 68.589  1.00 23.96  ? 274 GLN A C   1 
ATOM   466  O  O   . GLN A 1 74  ? 90.860  131.610 68.869  1.00 23.96  ? 274 GLN A O   1 
ATOM   467  C  CB  . GLN A 1 74  ? 94.135  131.797 68.581  1.00 23.96  ? 274 GLN A CB  1 
ATOM   468  C  CG  . GLN A 1 74  ? 95.135  130.850 67.940  1.00 23.96  ? 274 GLN A CG  1 
ATOM   469  C  CD  . GLN A 1 74  ? 96.382  130.665 68.781  1.00 23.96  ? 274 GLN A CD  1 
ATOM   470  O  OE1 . GLN A 1 74  ? 96.867  131.608 69.407  1.00 23.96  ? 274 GLN A OE1 1 
ATOM   471  N  NE2 . GLN A 1 74  ? 96.909  129.448 68.800  1.00 23.96  ? 274 GLN A NE2 1 
ATOM   472  N  N   . LYS A 1 75  ? 91.643  133.714 69.030  1.00 24.87  ? 275 LYS A N   1 
ATOM   473  C  CA  . LYS A 1 75  ? 90.523  134.145 69.858  1.00 24.87  ? 275 LYS A CA  1 
ATOM   474  C  C   . LYS A 1 75  ? 89.245  134.266 69.039  1.00 24.87  ? 275 LYS A C   1 
ATOM   475  O  O   . LYS A 1 75  ? 88.172  133.828 69.476  1.00 24.87  ? 275 LYS A O   1 
ATOM   476  C  CB  . LYS A 1 75  ? 90.858  135.476 70.533  1.00 24.87  ? 275 LYS A CB  1 
ATOM   477  C  CG  . LYS A 1 75  ? 92.088  135.423 71.421  1.00 24.87  ? 275 LYS A CG  1 
ATOM   478  C  CD  . LYS A 1 75  ? 92.500  136.812 71.869  1.00 24.87  ? 275 LYS A CD  1 
ATOM   479  C  CE  . LYS A 1 75  ? 92.166  137.035 73.331  1.00 24.87  ? 275 LYS A CE  1 
ATOM   480  N  NZ  . LYS A 1 75  ? 91.704  138.427 73.582  1.00 24.87  ? 275 LYS A NZ  1 
ATOM   481  N  N   . ALA A 1 76  ? 89.335  134.861 67.848  1.00 26.16  ? 276 ALA A N   1 
ATOM   482  C  CA  . ALA A 1 76  ? 88.142  135.079 67.035  1.00 26.16  ? 276 ALA A CA  1 
ATOM   483  C  C   . ALA A 1 76  ? 87.528  133.763 66.570  1.00 26.16  ? 276 ALA A C   1 
ATOM   484  O  O   . ALA A 1 76  ? 86.304  133.595 66.614  1.00 26.16  ? 276 ALA A O   1 
ATOM   485  C  CB  . ALA A 1 76  ? 88.479  135.967 65.838  1.00 26.16  ? 276 ALA A CB  1 
ATOM   486  N  N   . SER A 1 77  ? 88.358  132.820 66.120  1.00 26.19  ? 277 SER A N   1 
ATOM   487  C  CA  . SER A 1 77  ? 87.854  131.561 65.588  1.00 26.19  ? 277 SER A CA  1 
ATOM   488  C  C   . SER A 1 77  ? 87.378  130.602 66.671  1.00 26.19  ? 277 SER A C   1 
ATOM   489  O  O   . SER A 1 77  ? 86.580  129.707 66.376  1.00 26.19  ? 277 SER A O   1 
ATOM   490  C  CB  . SER A 1 77  ? 88.932  130.880 64.742  1.00 26.19  ? 277 SER A CB  1 
ATOM   491  O  OG  . SER A 1 77  ? 90.118  130.682 65.494  1.00 26.19  ? 277 SER A OG  1 
ATOM   492  N  N   . GLY A 1 78  ? 87.842  130.765 67.906  1.00 26.00  ? 278 GLY A N   1 
ATOM   493  C  CA  . GLY A 1 78  ? 87.482  129.850 68.969  1.00 26.00  ? 278 GLY A CA  1 
ATOM   494  C  C   . GLY A 1 78  ? 88.436  128.697 69.176  1.00 26.00  ? 278 GLY A C   1 
ATOM   495  O  O   . GLY A 1 78  ? 88.070  127.722 69.843  1.00 26.00  ? 278 GLY A O   1 
ATOM   496  N  N   . SER A 1 79  ? 89.648  128.771 68.626  1.00 26.96  ? 279 SER A N   1 
ATOM   497  C  CA  . SER A 1 79  ? 90.649  127.720 68.760  1.00 26.96  ? 279 SER A CA  1 
ATOM   498  C  C   . SER A 1 79  ? 91.368  127.752 70.105  1.00 26.96  ? 279 SER A C   1 
ATOM   499  O  O   . SER A 1 79  ? 92.429  127.132 70.244  1.00 26.96  ? 279 SER A O   1 
ATOM   500  C  CB  . SER A 1 79  ? 91.667  127.816 67.622  1.00 26.96  ? 279 SER A CB  1 
ATOM   501  O  OG  . SER A 1 79  ? 91.022  127.827 66.361  1.00 26.96  ? 279 SER A OG  1 
ATOM   502  N  N   . ILE A 1 80  ? 90.815  128.455 71.085  1.00 24.96  ? 280 ILE A N   1 
ATOM   503  C  CA  . ILE A 1 80  ? 91.413  128.565 72.398  1.00 24.96  ? 280 ILE A CA  1 
ATOM   504  C  C   . ILE A 1 80  ? 90.733  127.570 73.331  1.00 24.96  ? 280 ILE A C   1 
ATOM   505  O  O   . ILE A 1 80  ? 89.735  126.942 72.986  1.00 24.96  ? 280 ILE A O   1 
ATOM   506  C  CB  . ILE A 1 80  ? 91.326  130.006 72.951  1.00 24.96  ? 280 ILE A CB  1 
ATOM   507  C  CG1 . ILE A 1 80  ? 89.900  130.544 72.815  1.00 24.96  ? 280 ILE A CG1 1 
ATOM   508  C  CG2 . ILE A 1 80  ? 92.310  130.912 72.230  1.00 24.96  ? 280 ILE A CG2 1 
ATOM   509  C  CD1 . ILE A 1 80  ? 89.744  131.983 73.256  1.00 24.96  ? 280 ILE A CD1 1 
ATOM   510  N  N   . ASP A 1 81  ? 91.302  127.401 74.525  1.00 22.20  ? 281 ASP A N   1 
ATOM   511  C  CA  . ASP A 1 81  ? 90.750  126.479 75.509  1.00 22.20  ? 281 ASP A CA  1 
ATOM   512  C  C   . ASP A 1 81  ? 89.290  126.820 75.780  1.00 22.20  ? 281 ASP A C   1 
ATOM   513  O  O   . ASP A 1 81  ? 88.934  127.986 75.973  1.00 22.20  ? 281 ASP A O   1 
ATOM   514  C  CB  . ASP A 1 81  ? 91.577  126.549 76.799  1.00 22.20  ? 281 ASP A CB  1 
ATOM   515  C  CG  . ASP A 1 81  ? 90.831  126.031 78.024  1.00 22.20  ? 281 ASP A CG  1 
ATOM   516  O  OD1 . ASP A 1 81  ? 89.966  125.138 77.893  1.00 22.20  ? 281 ASP A OD1 1 
ATOM   517  O  OD2 . ASP A 1 81  ? 91.118  126.525 79.134  1.00 22.20  ? 281 ASP A OD2 1 
ATOM   518  N  N   . LYS A 1 82  ? 88.443  125.789 75.787  1.00 21.95  ? 282 LYS A N   1 
ATOM   519  C  CA  . LYS A 1 82  ? 87.000  125.982 75.847  1.00 21.95  ? 282 LYS A CA  1 
ATOM   520  C  C   . LYS A 1 82  ? 86.517  126.496 77.196  1.00 21.95  ? 282 LYS A C   1 
ATOM   521  O  O   . LYS A 1 82  ? 85.370  126.946 77.289  1.00 21.95  ? 282 LYS A O   1 
ATOM   522  C  CB  . LYS A 1 82  ? 86.289  124.673 75.507  1.00 21.95  ? 282 LYS A CB  1 
ATOM   523  C  CG  . LYS A 1 82  ? 86.617  124.137 74.123  1.00 21.95  ? 282 LYS A CG  1 
ATOM   524  C  CD  . LYS A 1 82  ? 85.825  124.862 73.048  1.00 21.95  ? 282 LYS A CD  1 
ATOM   525  C  CE  . LYS A 1 82  ? 86.462  124.681 71.680  1.00 21.95  ? 282 LYS A CE  1 
ATOM   526  N  NZ  . LYS A 1 82  ? 85.457  124.764 70.585  1.00 21.95  ? 282 LYS A NZ  1 
ATOM   527  N  N   . ALA A 1 83  ? 87.349  126.444 78.235  1.00 20.68  ? 283 ALA A N   1 
ATOM   528  C  CA  . ALA A 1 83  ? 86.970  126.992 79.530  1.00 20.68  ? 283 ALA A CA  1 
ATOM   529  C  C   . ALA A 1 83  ? 87.079  128.509 79.580  1.00 20.68  ? 283 ALA A C   1 
ATOM   530  O  O   . ALA A 1 83  ? 86.592  129.117 80.539  1.00 20.68  ? 283 ALA A O   1 
ATOM   531  C  CB  . ALA A 1 83  ? 87.828  126.375 80.636  1.00 20.68  ? 283 ALA A CB  1 
ATOM   532  N  N   . ILE A 1 84  ? 87.703  129.129 78.578  1.00 20.82  ? 284 ILE A N   1 
ATOM   533  C  CA  . ILE A 1 84  ? 87.799  130.582 78.528  1.00 20.82  ? 284 ILE A CA  1 
ATOM   534  C  C   . ILE A 1 84  ? 86.444  131.168 78.157  1.00 20.82  ? 284 ILE A C   1 
ATOM   535  O  O   . ILE A 1 84  ? 85.735  130.643 77.286  1.00 20.82  ? 284 ILE A O   1 
ATOM   536  C  CB  . ILE A 1 84  ? 88.890  131.008 77.531  1.00 20.82  ? 284 ILE A CB  1 
ATOM   537  C  CG1 . ILE A 1 84  ? 90.236  130.391 77.917  1.00 20.82  ? 284 ILE A CG1 1 
ATOM   538  C  CG2 . ILE A 1 84  ? 89.009  132.521 77.478  1.00 20.82  ? 284 ILE A CG2 1 
ATOM   539  C  CD1 . ILE A 1 84  ? 91.310  130.564 76.866  1.00 20.82  ? 284 ILE A CD1 1 
ATOM   540  N  N   . LYS A 1 85  ? 86.073  132.260 78.823  1.00 24.54  ? 285 LYS A N   1 
ATOM   541  C  CA  . LYS A 1 85  ? 84.791  132.899 78.565  1.00 24.54  ? 285 LYS A CA  1 
ATOM   542  C  C   . LYS A 1 85  ? 84.739  133.457 77.146  1.00 24.54  ? 285 LYS A C   1 
ATOM   543  O  O   . LYS A 1 85  ? 85.762  133.806 76.551  1.00 24.54  ? 285 LYS A O   1 
ATOM   544  C  CB  . LYS A 1 85  ? 84.539  134.018 79.574  1.00 24.54  ? 285 LYS A CB  1 
ATOM   545  C  CG  . LYS A 1 85  ? 84.445  133.548 81.016  1.00 24.54  ? 285 LYS A CG  1 
ATOM   546  C  CD  . LYS A 1 85  ? 83.774  134.593 81.892  1.00 24.54  ? 285 LYS A CD  1 
ATOM   547  C  CE  . LYS A 1 85  ? 82.283  134.326 82.026  1.00 24.54  ? 285 LYS A CE  1 
ATOM   548  N  NZ  . LYS A 1 85  ? 81.955  132.889 81.814  1.00 24.54  ? 285 LYS A NZ  1 
ATOM   549  N  N   . LEU A 1 86  ? 83.520  133.535 76.603  1.00 28.80  ? 286 LEU A N   1 
ATOM   550  C  CA  . LEU A 1 86  ? 83.339  134.006 75.235  1.00 28.80  ? 286 LEU A CA  1 
ATOM   551  C  C   . LEU A 1 86  ? 83.708  135.475 75.071  1.00 28.80  ? 286 LEU A C   1 
ATOM   552  O  O   . LEU A 1 86  ? 84.002  135.905 73.950  1.00 28.80  ? 286 LEU A O   1 
ATOM   553  C  CB  . LEU A 1 86  ? 81.896  133.781 74.781  1.00 28.80  ? 286 LEU A CB  1 
ATOM   554  C  CG  . LEU A 1 86  ? 80.807  134.667 75.391  1.00 28.80  ? 286 LEU A CG  1 
ATOM   555  C  CD1 . LEU A 1 86  ? 79.662  134.845 74.408  1.00 28.80  ? 286 LEU A CD1 1 
ATOM   556  C  CD2 . LEU A 1 86  ? 80.299  134.096 76.706  1.00 28.80  ? 286 LEU A CD2 1 
ATOM   557  N  N   . GLU A 1 87  ? 83.705  136.251 76.159  1.00 29.19  ? 287 GLU A N   1 
ATOM   558  C  CA  . GLU A 1 87  ? 84.096  137.653 76.070  1.00 29.19  ? 287 GLU A CA  1 
ATOM   559  C  C   . GLU A 1 87  ? 85.530  137.790 75.576  1.00 29.19  ? 287 GLU A C   1 
ATOM   560  O  O   . GLU A 1 87  ? 85.848  138.713 74.814  1.00 29.19  ? 287 GLU A O   1 
ATOM   561  C  CB  . GLU A 1 87  ? 83.936  138.336 77.429  1.00 29.19  ? 287 GLU A CB  1 
ATOM   562  C  CG  . GLU A 1 87  ? 82.569  138.154 78.062  1.00 29.19  ? 287 GLU A CG  1 
ATOM   563  C  CD  . GLU A 1 87  ? 82.590  137.187 79.228  1.00 29.19  ? 287 GLU A CD  1 
ATOM   564  O  OE1 . GLU A 1 87  ? 83.353  137.431 80.185  1.00 29.19  ? 287 GLU A OE1 1 
ATOM   565  O  OE2 . GLU A 1 87  ? 81.843  136.188 79.187  1.00 29.19  ? 287 GLU A OE2 1 
ATOM   566  N  N   . ALA A 1 88  ? 86.408  136.882 75.994  1.00 28.29  ? 288 ALA A N   1 
ATOM   567  C  CA  . ALA A 1 88  ? 87.790  136.882 75.541  1.00 28.29  ? 288 ALA A CA  1 
ATOM   568  C  C   . ALA A 1 88  ? 87.938  136.468 74.084  1.00 28.29  ? 288 ALA A C   1 
ATOM   569  O  O   . ALA A 1 88  ? 89.032  136.604 73.530  1.00 28.29  ? 288 ALA A O   1 
ATOM   570  C  CB  . ALA A 1 88  ? 88.635  135.963 76.427  1.00 28.29  ? 288 ALA A CB  1 
ATOM   571  N  N   . ARG A 1 89  ? 86.876  135.963 73.450  1.00 29.81  ? 289 ARG A N   1 
ATOM   572  C  CA  . ARG A 1 89  ? 86.945  135.675 72.023  1.00 29.81  ? 289 ARG A CA  1 
ATOM   573  C  C   . ARG A 1 89  ? 87.102  136.941 71.192  1.00 29.81  ? 289 ARG A C   1 
ATOM   574  O  O   . ARG A 1 89  ? 87.604  136.871 70.065  1.00 29.81  ? 289 ARG A O   1 
ATOM   575  C  CB  . ARG A 1 89  ? 85.705  134.901 71.575  1.00 29.81  ? 289 ARG A CB  1 
ATOM   576  C  CG  . ARG A 1 89  ? 85.536  133.554 72.259  1.00 29.81  ? 289 ARG A CG  1 
ATOM   577  C  CD  . ARG A 1 89  ? 85.101  132.482 71.272  1.00 29.81  ? 289 ARG A CD  1 
ATOM   578  N  NE  . ARG A 1 89  ? 83.669  132.538 70.996  1.00 29.81  ? 289 ARG A NE  1 
ATOM   579  C  CZ  . ARG A 1 89  ? 82.777  131.696 71.497  1.00 29.81  ? 289 ARG A CZ  1 
ATOM   580  N  N   . ASP A 1 90  ? 86.685  138.085 71.718  1.00 28.24  ? 290 ASP A N   1 
ATOM   581  C  CA  . ASP A 1 90  ? 86.934  139.351 71.044  1.00 28.24  ? 290 ASP A CA  1 
ATOM   582  C  C   . ASP A 1 90  ? 88.417  139.693 71.130  1.00 28.24  ? 290 ASP A C   1 
ATOM   583  O  O   . ASP A 1 90  ? 89.010  139.583 72.210  1.00 28.24  ? 290 ASP A O   1 
ATOM   584  C  CB  . ASP A 1 90  ? 86.097  140.464 71.673  1.00 28.24  ? 290 ASP A CB  1 
ATOM   585  C  CG  . ASP A 1 90  ? 85.935  141.660 70.757  1.00 28.24  ? 290 ASP A CG  1 
ATOM   586  O  OD1 . ASP A 1 90  ? 86.880  142.471 70.663  1.00 28.24  ? 290 ASP A OD1 1 
ATOM   587  O  OD2 . ASP A 1 90  ? 84.860  141.792 70.134  1.00 28.24  ? 290 ASP A OD2 1 
ATOM   588  N  N   . PRO A 1 91  ? 89.052  140.094 70.026  1.00 26.38  ? 291 PRO A N   1 
ATOM   589  C  CA  . PRO A 1 91  ? 90.482  140.440 70.086  1.00 26.38  ? 291 PRO A CA  1 
ATOM   590  C  C   . PRO A 1 91  ? 90.796  141.591 71.026  1.00 26.38  ? 291 PRO A C   1 
ATOM   591  O  O   . PRO A 1 91  ? 91.913  141.650 71.555  1.00 26.38  ? 291 PRO A O   1 
ATOM   592  C  CB  . PRO A 1 91  ? 90.817  140.798 68.631  1.00 26.38  ? 291 PRO A CB  1 
ATOM   593  C  CG  . PRO A 1 91  ? 89.768  140.110 67.818  1.00 26.38  ? 291 PRO A CG  1 
ATOM   594  C  CD  . PRO A 1 91  ? 88.525  140.152 68.653  1.00 26.38  ? 291 PRO A CD  1 
ATOM   595  N  N   . LEU A 1 92  ? 89.854  142.507 71.252  1.00 25.85  ? 292 LEU A N   1 
ATOM   596  C  CA  . LEU A 1 92  ? 90.093  143.646 72.127  1.00 25.85  ? 292 LEU A CA  1 
ATOM   597  C  C   . LEU A 1 92  ? 89.963  143.305 73.605  1.00 25.85  ? 292 LEU A C   1 
ATOM   598  O  O   . LEU A 1 92  ? 90.407  144.093 74.448  1.00 25.85  ? 292 LEU A O   1 
ATOM   599  C  CB  . LEU A 1 92  ? 89.129  144.787 71.788  1.00 25.85  ? 292 LEU A CB  1 
ATOM   600  C  CG  . LEU A 1 92  ? 89.343  145.475 70.438  1.00 25.85  ? 292 LEU A CG  1 
ATOM   601  C  CD1 . LEU A 1 92  ? 88.321  146.581 70.231  1.00 25.85  ? 292 LEU A CD1 1 
ATOM   602  C  CD2 . LEU A 1 92  ? 90.758  146.020 70.331  1.00 25.85  ? 292 LEU A CD2 1 
ATOM   603  N  N   . VAL A 1 93  ? 89.374  142.162 73.940  1.00 24.84  ? 293 VAL A N   1 
ATOM   604  C  CA  . VAL A 1 93  ? 89.213  141.730 75.324  1.00 24.84  ? 293 VAL A CA  1 
ATOM   605  C  C   . VAL A 1 93  ? 90.217  140.618 75.591  1.00 24.84  ? 293 VAL A C   1 
ATOM   606  O  O   . VAL A 1 93  ? 90.191  139.573 74.930  1.00 24.84  ? 293 VAL A O   1 
ATOM   607  C  CB  . VAL A 1 93  ? 87.777  141.260 75.605  1.00 24.84  ? 293 VAL A CB  1 
ATOM   608  C  CG1 . VAL A 1 93  ? 87.601  140.948 77.083  1.00 24.84  ? 293 VAL A CG1 1 
ATOM   609  C  CG2 . VAL A 1 93  ? 86.779  142.315 75.155  1.00 24.84  ? 293 VAL A CG2 1 
ATOM   610  N  N   . ALA A 1 94  ? 91.100  140.839 76.559  1.00 23.43  ? 294 ALA A N   1 
ATOM   611  C  CA  . ALA A 1 94  ? 92.164  139.892 76.848  1.00 23.43  ? 294 ALA A CA  1 
ATOM   612  C  C   . ALA A 1 94  ? 91.666  138.752 77.728  1.00 23.43  ? 294 ALA A C   1 
ATOM   613  O  O   . ALA A 1 94  ? 90.800  138.933 78.587  1.00 23.43  ? 294 ALA A O   1 
ATOM   614  C  CB  . ALA A 1 94  ? 93.338  140.596 77.532  1.00 23.43  ? 294 ALA A CB  1 
ATOM   615  N  N   . ALA A 1 95  ? 92.229  137.569 77.501  1.00 21.15  ? 295 ALA A N   1 
ATOM   616  C  CA  . ALA A 1 95  ? 92.006  136.429 78.382  1.00 21.15  ? 295 ALA A CA  1 
ATOM   617  C  C   . ALA A 1 95  ? 92.924  136.583 79.586  1.00 21.15  ? 295 ALA A C   1 
ATOM   618  O  O   . ALA A 1 95  ? 94.144  136.420 79.471  1.00 21.15  ? 295 ALA A O   1 
ATOM   619  C  CB  . ALA A 1 95  ? 92.264  135.117 77.647  1.00 21.15  ? 295 ALA A CB  1 
ATOM   620  N  N   . TYR A 1 96  ? 92.346  136.900 80.740  1.00 19.00  ? 296 TYR A N   1 
ATOM   621  C  CA  . TYR A 1 96  ? 93.146  137.293 81.891  1.00 19.00  ? 296 TYR A CA  1 
ATOM   622  C  C   . TYR A 1 96  ? 92.511  136.800 83.185  1.00 19.00  ? 296 TYR A C   1 
ATOM   623  O  O   . TYR A 1 96  ? 91.413  137.244 83.548  1.00 19.00  ? 296 TYR A O   1 
ATOM   624  C  CB  . TYR A 1 96  ? 93.306  138.814 81.917  1.00 19.00  ? 296 TYR A CB  1 
ATOM   625  C  CG  . TYR A 1 96  ? 94.337  139.324 82.894  1.00 19.00  ? 296 TYR A CG  1 
ATOM   626  C  CD1 . TYR A 1 96  ? 95.674  138.968 82.774  1.00 19.00  ? 296 TYR A CD1 1 
ATOM   627  C  CD2 . TYR A 1 96  ? 93.976  140.173 83.932  1.00 19.00  ? 296 TYR A CD2 1 
ATOM   628  C  CE1 . TYR A 1 96  ? 96.620  139.437 83.664  1.00 19.00  ? 296 TYR A CE1 1 
ATOM   629  C  CE2 . TYR A 1 96  ? 94.915  140.648 84.826  1.00 19.00  ? 296 TYR A CE2 1 
ATOM   630  C  CZ  . TYR A 1 96  ? 96.234  140.278 84.687  1.00 19.00  ? 296 TYR A CZ  1 
ATOM   631  N  N   . PRO A 1 97  ? 93.161  135.889 83.905  1.00 15.19  ? 297 PRO A N   1 
ATOM   632  C  CA  . PRO A 1 97  ? 92.606  135.423 85.179  1.00 15.19  ? 297 PRO A CA  1 
ATOM   633  C  C   . PRO A 1 97  ? 92.980  136.349 86.327  1.00 15.19  ? 297 PRO A C   1 
ATOM   634  O  O   . PRO A 1 97  ? 94.125  136.791 86.451  1.00 15.19  ? 297 PRO A O   1 
ATOM   635  C  CB  . PRO A 1 97  ? 93.237  134.038 85.355  1.00 15.19  ? 297 PRO A CB  1 
ATOM   636  C  CG  . PRO A 1 97  ? 94.517  134.097 84.580  1.00 15.19  ? 297 PRO A CG  1 
ATOM   637  C  CD  . PRO A 1 97  ? 94.418  135.204 83.558  1.00 15.19  ? 297 PRO A CD  1 
ATOM   638  N  N   . VAL A 1 98  ? 91.995  136.638 87.171  1.00 14.60  ? 298 VAL A N   1 
ATOM   639  C  CA  . VAL A 1 98  ? 92.183  137.445 88.373  1.00 14.60  ? 298 VAL A CA  1 
ATOM   640  C  C   . VAL A 1 98  ? 91.938  136.528 89.561  1.00 14.60  ? 298 VAL A C   1 
ATOM   641  O  O   . VAL A 1 98  ? 90.805  136.084 89.789  1.00 14.60  ? 298 VAL A O   1 
ATOM   642  C  CB  . VAL A 1 98  ? 91.248  138.660 88.406  1.00 14.60  ? 298 VAL A CB  1 
ATOM   643  C  CG1 . VAL A 1 98  ? 91.704  139.651 89.466  1.00 14.60  ? 298 VAL A CG1 1 
ATOM   644  C  CG2 . VAL A 1 98  ? 91.189  139.322 87.038  1.00 14.60  ? 298 VAL A CG2 1 
ATOM   645  N  N   . VAL A 1 99  ? 92.991  136.249 90.325  1.00 11.90  ? 299 VAL A N   1 
ATOM   646  C  CA  . VAL A 1 99  ? 92.947  135.269 91.404  1.00 11.90  ? 299 VAL A CA  1 
ATOM   647  C  C   . VAL A 1 99  ? 93.225  135.976 92.723  1.00 11.90  ? 299 VAL A C   1 
ATOM   648  O  O   . VAL A 1 99  ? 94.214  136.708 92.846  1.00 11.90  ? 299 VAL A O   1 
ATOM   649  C  CB  . VAL A 1 99  ? 93.949  134.125 91.171  1.00 11.90  ? 299 VAL A CB  1 
ATOM   650  C  CG1 . VAL A 1 99  ? 93.969  133.184 92.366  1.00 11.90  ? 299 VAL A CG1 1 
ATOM   651  C  CG2 . VAL A 1 99  ? 93.605  133.372 89.896  1.00 11.90  ? 299 VAL A CG2 1 
ATOM   652  N  N   . GLY A 1 100 ? 92.351  135.751 93.705  1.00 11.30  ? 300 GLY A N   1 
ATOM   653  C  CA  . GLY A 1 100 ? 92.550  136.283 95.033  1.00 11.30  ? 300 GLY A CA  1 
ATOM   654  C  C   . GLY A 1 100 ? 92.375  135.197 96.076  1.00 11.30  ? 300 GLY A C   1 
ATOM   655  O  O   . GLY A 1 100 ? 91.794  134.143 95.819  1.00 11.30  ? 300 GLY A O   1 
ATOM   656  N  N   . VAL A 1 101 ? 92.895  135.475 97.268  1.00 11.69  ? 301 VAL A N   1 
ATOM   657  C  CA  . VAL A 1 101 ? 92.872  134.534 98.382  1.00 11.69  ? 301 VAL A CA  1 
ATOM   658  C  C   . VAL A 1 101 ? 92.174  135.194 99.561  1.00 11.69  ? 301 VAL A C   1 
ATOM   659  O  O   . VAL A 1 101 ? 92.496  136.332 99.924  1.00 11.69  ? 301 VAL A O   1 
ATOM   660  C  CB  . VAL A 1 101 ? 94.292  134.083 98.774  1.00 11.69  ? 301 VAL A CB  1 
ATOM   661  C  CG1 . VAL A 1 101 ? 94.232  133.048 99.889  1.00 11.69  ? 301 VAL A CG1 1 
ATOM   662  C  CG2 . VAL A 1 101 ? 95.026  133.528 97.567  1.00 11.69  ? 301 VAL A CG2 1 
ATOM   663  N  N   . GLY A 1 102 ? 91.222  134.486 100.150 1.00 12.35  ? 302 GLY A N   1 
ATOM   664  C  CA  . GLY A 1 102 ? 90.535  134.948 101.347 1.00 12.35  ? 302 GLY A CA  1 
ATOM   665  C  C   . GLY A 1 102 ? 90.680  133.936 102.467 1.00 12.35  ? 302 GLY A C   1 
ATOM   666  O  O   . GLY A 1 102 ? 90.596  132.729 102.235 1.00 12.35  ? 302 GLY A O   1 
ATOM   667  N  N   . MET A 1 103 ? 90.893  134.437 103.680 1.00 16.14  ? 303 MET A N   1 
ATOM   668  C  CA  . MET A 1 103 ? 91.087  133.595 104.851 1.00 16.14  ? 303 MET A CA  1 
ATOM   669  C  C   . MET A 1 103 ? 89.792  133.506 105.648 1.00 16.14  ? 303 MET A C   1 
ATOM   670  O  O   . MET A 1 103 ? 89.115  134.513 105.870 1.00 16.14  ? 303 MET A O   1 
ATOM   671  C  CB  . MET A 1 103 ? 92.213  134.140 105.734 1.00 16.14  ? 303 MET A CB  1 
ATOM   672  C  CG  . MET A 1 103 ? 92.480  133.314 106.981 1.00 16.14  ? 303 MET A CG  1 
ATOM   673  S  SD  . MET A 1 103 ? 93.887  133.924 107.926 1.00 16.14  ? 303 MET A SD  1 
ATOM   674  C  CE  . MET A 1 103 ? 93.464  135.656 108.069 1.00 16.14  ? 303 MET A CE  1 
ATOM   675  N  N   . GLU A 1 104 ? 89.453  132.288 106.079 1.00 17.20  ? 304 GLU A N   1 
ATOM   676  C  CA  . GLU A 1 104 ? 88.205  132.037 106.784 1.00 17.20  ? 304 GLU A CA  1 
ATOM   677  C  C   . GLU A 1 104 ? 88.382  131.667 108.249 1.00 17.20  ? 304 GLU A C   1 
ATOM   678  O  O   . GLU A 1 104 ? 87.434  131.830 109.023 1.00 17.20  ? 304 GLU A O   1 
ATOM   679  C  CB  . GLU A 1 104 ? 87.417  130.918 106.087 1.00 17.20  ? 304 GLU A CB  1 
ATOM   680  C  CG  . GLU A 1 104 ? 87.582  130.892 104.575 1.00 17.20  ? 304 GLU A CG  1 
ATOM   681  C  CD  . GLU A 1 104 ? 86.398  130.262 103.870 1.00 17.20  ? 304 GLU A CD  1 
ATOM   682  O  OE1 . GLU A 1 104 ? 85.708  129.428 104.492 1.00 17.20  ? 304 GLU A OE1 1 
ATOM   683  O  OE2 . GLU A 1 104 ? 86.158  130.598 102.691 1.00 17.20  ? 304 GLU A OE2 1 
ATOM   684  N  N   . ASN A 1 105 ? 89.553  131.178 108.649 1.00 16.30  ? 305 ASN A N   1 
ATOM   685  C  CA  . ASN A 1 105 ? 89.763  130.758 110.027 1.00 16.30  ? 305 ASN A CA  1 
ATOM   686  C  C   . ASN A 1 105 ? 91.251  130.800 110.346 1.00 16.30  ? 305 ASN A C   1 
ATOM   687  O  O   . ASN A 1 105 ? 92.084  130.570 109.468 1.00 16.30  ? 305 ASN A O   1 
ATOM   688  C  CB  . ASN A 1 105 ? 89.210  129.349 110.268 1.00 16.30  ? 305 ASN A CB  1 
ATOM   689  C  CG  . ASN A 1 105 ? 88.691  129.158 111.678 1.00 16.30  ? 305 ASN A CG  1 
ATOM   690  O  OD1 . ASN A 1 105 ? 88.904  130.002 112.548 1.00 16.30  ? 305 ASN A OD1 1 
ATOM   691  N  ND2 . ASN A 1 105 ? 88.008  128.045 111.912 1.00 16.30  ? 305 ASN A ND2 1 
ATOM   692  N  N   . LEU A 1 106 ? 91.571  131.089 111.605 1.00 15.29  ? 306 LEU A N   1 
ATOM   693  C  CA  . LEU A 1 106 ? 92.942  131.077 112.093 1.00 15.29  ? 306 LEU A CA  1 
ATOM   694  C  C   . LEU A 1 106 ? 92.990  130.233 113.357 1.00 15.29  ? 306 LEU A C   1 
ATOM   695  O  O   . LEU A 1 106 ? 92.209  130.461 114.286 1.00 15.29  ? 306 LEU A O   1 
ATOM   696  C  CB  . LEU A 1 106 ? 93.444  132.504 112.361 1.00 15.29  ? 306 LEU A CB  1 
ATOM   697  C  CG  . LEU A 1 106 ? 94.950  132.777 112.468 1.00 15.29  ? 306 LEU A CG  1 
ATOM   698  C  CD1 . LEU A 1 106 ? 95.528  132.339 113.806 1.00 15.29  ? 306 LEU A CD1 1 
ATOM   699  C  CD2 . LEU A 1 106 ? 95.698  132.112 111.320 1.00 15.29  ? 306 LEU A CD2 1 
ATOM   700  N  N   . ILE A 1 107 ? 93.901  129.263 113.390 1.00 15.55  ? 307 ILE A N   1 
ATOM   701  C  CA  . ILE A 1 107 ? 94.021  128.322 114.497 1.00 15.55  ? 307 ILE A CA  1 
ATOM   702  C  C   . ILE A 1 107 ? 95.419  128.451 115.086 1.00 15.55  ? 307 ILE A C   1 
ATOM   703  O  O   . ILE A 1 107 ? 96.413  128.427 114.351 1.00 15.55  ? 307 ILE A O   1 
ATOM   704  C  CB  . ILE A 1 107 ? 93.748  126.875 114.043 1.00 15.55  ? 307 ILE A CB  1 
ATOM   705  C  CG1 . ILE A 1 107 ? 92.306  126.738 113.549 1.00 15.55  ? 307 ILE A CG1 1 
ATOM   706  C  CG2 . ILE A 1 107 ? 94.017  125.899 115.176 1.00 15.55  ? 307 ILE A CG2 1 
ATOM   707  C  CD1 . ILE A 1 107 ? 92.195  126.359 112.090 1.00 15.55  ? 307 ILE A CD1 1 
ATOM   708  N  N   . ILE A 1 108 ? 95.491  128.581 116.408 1.00 16.72  ? 308 ILE A N   1 
ATOM   709  C  CA  . ILE A 1 108 ? 96.749  128.751 117.127 1.00 16.72  ? 308 ILE A CA  1 
ATOM   710  C  C   . ILE A 1 108 ? 96.993  127.511 117.976 1.00 16.72  ? 308 ILE A C   1 
ATOM   711  O  O   . ILE A 1 108 ? 96.117  127.091 118.741 1.00 16.72  ? 308 ILE A O   1 
ATOM   712  C  CB  . ILE A 1 108 ? 96.731  130.017 118.002 1.00 16.72  ? 308 ILE A CB  1 
ATOM   713  C  CG1 . ILE A 1 108 ? 96.431  131.250 117.152 1.00 16.72  ? 308 ILE A CG1 1 
ATOM   714  C  CG2 . ILE A 1 108 ? 98.055  130.181 118.732 1.00 16.72  ? 308 ILE A CG2 1 
ATOM   715  C  CD1 . ILE A 1 108 ? 95.579  132.281 117.856 1.00 16.72  ? 308 ILE A CD1 1 
ATOM   716  N  N   . SER A 1 109 ? 98.183  126.930 117.839 1.00 17.40  ? 309 SER A N   1 
ATOM   717  C  CA  . SER A 1 109 ? 98.615  125.797 118.649 1.00 17.40  ? 309 SER A CA  1 
ATOM   718  C  C   . SER A 1 109 ? 99.808  126.250 119.477 1.00 17.40  ? 309 SER A C   1 
ATOM   719  O  O   . SER A 1 109 ? 100.882 126.515 118.929 1.00 17.40  ? 309 SER A O   1 
ATOM   720  C  CB  . SER A 1 109 ? 98.975  124.596 117.773 1.00 17.40  ? 309 SER A CB  1 
ATOM   721  O  OG  . SER A 1 109 ? 97.998  124.386 116.768 1.00 17.40  ? 309 SER A OG  1 
ATOM   722  N  N   . THR A 1 110 ? 99.617  126.346 120.793 1.00 19.98  ? 310 THR A N   1 
ATOM   723  C  CA  . THR A 1 110 ? 100.676 126.826 121.668 1.00 19.98  ? 310 THR A CA  1 
ATOM   724  C  C   . THR A 1 110 ? 101.668 125.710 121.974 1.00 19.98  ? 310 THR A C   1 
ATOM   725  O  O   . THR A 1 110 ? 101.280 124.615 122.389 1.00 19.98  ? 310 THR A O   1 
ATOM   726  C  CB  . THR A 1 110 ? 100.091 127.381 122.967 1.00 19.98  ? 310 THR A CB  1 
ATOM   727  O  OG1 . THR A 1 110 ? 99.084  128.351 122.659 1.00 19.98  ? 310 THR A OG1 1 
ATOM   728  C  CG2 . THR A 1 110 ? 101.180 128.046 123.797 1.00 19.98  ? 310 THR A CG2 1 
ATOM   729  N  N   . ASN A 1 111 ? 102.951 125.998 121.765 1.00 22.48  ? 311 ASN A N   1 
ATOM   730  C  CA  . ASN A 1 111 ? 104.023 125.022 121.950 1.00 22.48  ? 311 ASN A CA  1 
ATOM   731  C  C   . ASN A 1 111 ? 104.618 125.130 123.355 1.00 22.48  ? 311 ASN A C   1 
ATOM   732  O  O   . ASN A 1 111 ? 105.794 125.436 123.546 1.00 22.48  ? 311 ASN A O   1 
ATOM   733  C  CB  . ASN A 1 111 ? 105.095 125.216 120.882 1.00 22.48  ? 311 ASN A CB  1 
ATOM   734  C  CG  . ASN A 1 111 ? 105.726 123.907 120.437 1.00 22.48  ? 311 ASN A CG  1 
ATOM   735  O  OD1 . ASN A 1 111 ? 105.364 122.832 120.921 1.00 22.48  ? 311 ASN A OD1 1 
ATOM   736  N  ND2 . ASN A 1 111 ? 106.684 123.994 119.523 1.00 22.48  ? 311 ASN A ND2 1 
ATOM   737  N  N   . GLU A 1 112 ? 103.772 124.872 124.349 1.00 23.52  ? 312 GLU A N   1 
ATOM   738  C  CA  . GLU A 1 112 ? 104.198 124.838 125.739 1.00 23.52  ? 312 GLU A CA  1 
ATOM   739  C  C   . GLU A 1 112 ? 104.214 123.397 126.232 1.00 23.52  ? 312 GLU A C   1 
ATOM   740  O  O   . GLU A 1 112 ? 103.374 122.585 125.834 1.00 23.52  ? 312 GLU A O   1 
ATOM   741  C  CB  . GLU A 1 112 ? 103.289 125.694 126.626 1.00 23.52  ? 312 GLU A CB  1 
ATOM   742  C  CG  . GLU A 1 112 ? 101.807 125.405 126.483 1.00 23.52  ? 312 GLU A CG  1 
ATOM   743  C  CD  . GLU A 1 112 ? 100.934 126.463 127.135 1.00 23.52  ? 312 GLU A CD  1 
ATOM   744  O  OE1 . GLU A 1 112 ? 101.266 127.664 127.036 1.00 23.52  ? 312 GLU A OE1 1 
ATOM   745  O  OE2 . GLU A 1 112 ? 99.911  126.094 127.747 1.00 23.52  ? 312 GLU A OE2 1 
ATOM   746  N  N   . HIS A 1 113 ? 105.185 123.082 127.084 1.00 22.18  ? 313 HIS A N   1 
ATOM   747  C  CA  . HIS A 1 113 ? 105.386 121.736 127.605 1.00 22.18  ? 313 HIS A CA  1 
ATOM   748  C  C   . HIS A 1 113 ? 104.899 121.671 129.046 1.00 22.18  ? 313 HIS A C   1 
ATOM   749  O  O   . HIS A 1 113 ? 105.345 122.451 129.891 1.00 22.18  ? 313 HIS A O   1 
ATOM   750  C  CB  . HIS A 1 113 ? 106.864 121.341 127.523 1.00 22.18  ? 313 HIS A CB  1 
ATOM   751  C  CG  . HIS A 1 113 ? 107.117 119.883 127.747 1.00 22.18  ? 313 HIS A CG  1 
ATOM   752  N  ND1 . HIS A 1 113 ? 106.794 118.916 126.818 1.00 22.18  ? 313 HIS A ND1 1 
ATOM   753  C  CD2 . HIS A 1 113 ? 107.667 119.226 128.796 1.00 22.18  ? 313 HIS A CD2 1 
ATOM   754  C  CE1 . HIS A 1 113 ? 107.134 117.729 127.285 1.00 22.18  ? 313 HIS A CE1 1 
ATOM   755  N  NE2 . HIS A 1 113 ? 107.665 117.888 128.483 1.00 22.18  ? 313 HIS A NE2 1 
ATOM   756  N  N   . ALA A 1 114 ? 103.993 120.737 129.322 1.00 20.76  ? 314 ALA A N   1 
ATOM   757  C  CA  . ALA A 1 114 ? 103.423 120.558 130.649 1.00 20.76  ? 314 ALA A CA  1 
ATOM   758  C  C   . ALA A 1 114 ? 103.802 119.186 131.186 1.00 20.76  ? 314 ALA A C   1 
ATOM   759  O  O   . ALA A 1 114 ? 103.750 118.189 130.458 1.00 20.76  ? 314 ALA A O   1 
ATOM   760  C  CB  . ALA A 1 114 ? 101.899 120.710 130.623 1.00 20.76  ? 314 ALA A CB  1 
ATOM   761  N  N   . SER A 1 115 ? 104.185 119.135 132.461 1.00 21.35  ? 315 SER A N   1 
ATOM   762  C  CA  . SER A 1 115 ? 104.627 117.897 133.084 1.00 21.35  ? 315 SER A CA  1 
ATOM   763  C  C   . SER A 1 115 ? 104.034 117.779 134.482 1.00 21.35  ? 315 SER A C   1 
ATOM   764  O  O   . SER A 1 115 ? 103.789 118.779 135.161 1.00 21.35  ? 315 SER A O   1 
ATOM   765  C  CB  . SER A 1 115 ? 106.158 117.817 133.158 1.00 21.35  ? 315 SER A CB  1 
ATOM   766  O  OG  . SER A 1 115 ? 106.723 119.095 133.390 1.00 21.35  ? 315 SER A OG  1 
ATOM   767  N  N   . SER A 1 116 ? 103.817 116.537 134.907 1.00 22.58  ? 316 SER A N   1 
ATOM   768  C  CA  . SER A 1 116 ? 103.312 116.241 136.240 1.00 22.58  ? 316 SER A CA  1 
ATOM   769  C  C   . SER A 1 116 ? 104.097 115.067 136.808 1.00 22.58  ? 316 SER A C   1 
ATOM   770  O  O   . SER A 1 116 ? 104.432 114.129 136.081 1.00 22.58  ? 316 SER A O   1 
ATOM   771  C  CB  . SER A 1 116 ? 101.814 115.917 136.216 1.00 22.58  ? 316 SER A CB  1 
ATOM   772  O  OG  . SER A 1 116 ? 101.520 114.943 135.230 1.00 22.58  ? 316 SER A OG  1 
ATOM   773  N  N   . ASP A 1 117 ? 104.390 115.127 138.106 1.00 25.09  ? 317 ASP A N   1 
ATOM   774  C  CA  . ASP A 1 117 ? 105.180 114.107 138.779 1.00 25.09  ? 317 ASP A CA  1 
ATOM   775  C  C   . ASP A 1 117 ? 104.532 113.734 140.104 1.00 25.09  ? 317 ASP A C   1 
ATOM   776  O  O   . ASP A 1 117 ? 104.014 114.591 140.826 1.00 25.09  ? 317 ASP A O   1 
ATOM   777  C  CB  . ASP A 1 117 ? 106.619 114.579 139.025 1.00 25.09  ? 317 ASP A CB  1 
ATOM   778  C  CG  . ASP A 1 117 ? 107.576 114.125 137.941 1.00 25.09  ? 317 ASP A CG  1 
ATOM   779  O  OD1 . ASP A 1 117 ? 107.868 112.913 137.877 1.00 25.09  ? 317 ASP A OD1 1 
ATOM   780  O  OD2 . ASP A 1 117 ? 108.037 114.979 137.154 1.00 25.09  ? 317 ASP A OD2 1 
ATOM   781  N  N   . GLN A 1 118 ? 104.588 112.442 140.423 1.00 24.60  ? 318 GLN A N   1 
ATOM   782  C  CA  . GLN A 1 118 ? 103.996 111.909 141.644 1.00 24.60  ? 318 GLN A CA  1 
ATOM   783  C  C   . GLN A 1 118 ? 105.012 110.979 142.289 1.00 24.60  ? 318 GLN A C   1 
ATOM   784  O  O   . GLN A 1 118 ? 105.574 110.116 141.609 1.00 24.60  ? 318 GLN A O   1 
ATOM   785  C  CB  . GLN A 1 118 ? 102.696 111.161 141.334 1.00 24.60  ? 318 GLN A CB  1 
ATOM   786  C  CG  . GLN A 1 118 ? 101.753 111.011 142.508 1.00 24.60  ? 318 GLN A CG  1 
ATOM   787  C  CD  . GLN A 1 118 ? 100.303 111.160 142.092 1.00 24.60  ? 318 GLN A CD  1 
ATOM   788  O  OE1 . GLN A 1 118 ? 99.797  112.270 141.945 1.00 24.60  ? 318 GLN A OE1 1 
ATOM   789  N  NE2 . GLN A 1 118 ? 99.629  110.033 141.893 1.00 24.60  ? 318 GLN A NE2 1 
ATOM   790  N  N   . GLY A 1 119 ? 105.251 111.150 143.591 1.00 22.21  ? 319 GLY A N   1 
ATOM   791  C  CA  . GLY A 1 119 ? 106.283 110.400 144.268 1.00 22.21  ? 319 GLY A CA  1 
ATOM   792  C  C   . GLY A 1 119 ? 105.880 109.985 145.669 1.00 22.21  ? 319 GLY A C   1 
ATOM   793  O  O   . GLY A 1 119 ? 105.097 110.653 146.345 1.00 22.21  ? 319 GLY A O   1 
ATOM   794  N  N   . LYS A 1 120 ? 106.453 108.862 146.102 1.00 22.49  ? 320 LYS A N   1 
ATOM   795  C  CA  . LYS A 1 120 ? 106.246 108.323 147.439 1.00 22.49  ? 320 LYS A CA  1 
ATOM   796  C  C   . LYS A 1 120 ? 107.588 107.909 148.025 1.00 22.49  ? 320 LYS A C   1 
ATOM   797  O  O   . LYS A 1 120 ? 108.498 107.500 147.299 1.00 22.49  ? 320 LYS A O   1 
ATOM   798  C  CB  . LYS A 1 120 ? 105.292 107.120 147.427 1.00 22.49  ? 320 LYS A CB  1 
ATOM   799  C  CG  . LYS A 1 120 ? 103.823 107.480 147.560 1.00 22.49  ? 320 LYS A CG  1 
ATOM   800  C  CD  . LYS A 1 120 ? 102.941 106.244 147.467 1.00 22.49  ? 320 LYS A CD  1 
ATOM   801  C  CE  . LYS A 1 120 ? 101.476 106.585 147.701 1.00 22.49  ? 320 LYS A CE  1 
ATOM   802  N  NZ  . LYS A 1 120 ? 101.174 106.817 149.143 1.00 22.49  ? 320 LYS A NZ  1 
ATOM   803  N  N   . THR A 1 121 ? 107.702 108.013 149.349 1.00 22.25  ? 321 THR A N   1 
ATOM   804  C  CA  . THR A 1 121 ? 108.931 107.667 150.051 1.00 22.25  ? 321 THR A CA  1 
ATOM   805  C  C   . THR A 1 121 ? 108.605 106.990 151.373 1.00 22.25  ? 321 THR A C   1 
ATOM   806  O  O   . THR A 1 121 ? 107.657 107.369 152.066 1.00 22.25  ? 321 THR A O   1 
ATOM   807  C  CB  . THR A 1 121 ? 109.802 108.904 150.322 1.00 22.25  ? 321 THR A CB  1 
ATOM   808  O  OG1 . THR A 1 121 ? 108.967 110.014 150.674 1.00 22.25  ? 321 THR A OG1 1 
ATOM   809  C  CG2 . THR A 1 121 ? 110.628 109.264 149.097 1.00 22.25  ? 321 THR A CG2 1 
ATOM   810  N  N   . VAL A 1 122 ? 109.407 105.987 151.723 1.00 23.30  ? 322 VAL A N   1 
ATOM   811  C  CA  . VAL A 1 122 ? 109.333 105.332 153.028 1.00 23.30  ? 322 VAL A CA  1 
ATOM   812  C  C   . VAL A 1 122 ? 110.755 105.133 153.538 1.00 23.30  ? 322 VAL A C   1 
ATOM   813  O  O   . VAL A 1 122 ? 111.646 104.737 152.780 1.00 23.30  ? 322 VAL A O   1 
ATOM   814  C  CB  . VAL A 1 122 ? 108.565 103.993 152.967 1.00 23.30  ? 322 VAL A CB  1 
ATOM   815  C  CG1 . VAL A 1 122 ? 109.170 103.067 151.925 1.00 23.30  ? 322 VAL A CG1 1 
ATOM   816  C  CG2 . VAL A 1 122 ? 108.542 103.323 154.334 1.00 23.30  ? 322 VAL A CG2 1 
ATOM   817  N  N   . SER A 1 123 ? 110.972 105.421 154.820 1.00 24.54  ? 323 SER A N   1 
ATOM   818  C  CA  . SER A 1 123 ? 112.300 105.330 155.409 1.00 24.54  ? 323 SER A CA  1 
ATOM   819  C  C   . SER A 1 123 ? 112.199 104.868 156.855 1.00 24.54  ? 323 SER A C   1 
ATOM   820  O  O   . SER A 1 123 ? 111.171 105.032 157.514 1.00 24.54  ? 323 SER A O   1 
ATOM   821  C  CB  . SER A 1 123 ? 113.041 106.672 155.338 1.00 24.54  ? 323 SER A CB  1 
ATOM   822  O  OG  . SER A 1 123 ? 114.295 106.597 155.994 1.00 24.54  ? 323 SER A OG  1 
ATOM   823  N  N   . ARG A 1 124 ? 113.291 104.280 157.342 1.00 25.46  ? 324 ARG A N   1 
ATOM   824  C  CA  . ARG A 1 124 ? 113.388 103.826 158.723 1.00 25.46  ? 324 ARG A CA  1 
ATOM   825  C  C   . ARG A 1 124 ? 114.783 104.120 159.253 1.00 25.46  ? 324 ARG A C   1 
ATOM   826  O  O   . ARG A 1 124 ? 115.775 103.911 158.546 1.00 25.46  ? 324 ARG A O   1 
ATOM   827  C  CB  . ARG A 1 124 ? 113.074 102.327 158.839 1.00 25.46  ? 324 ARG A CB  1 
ATOM   828  C  CG  . ARG A 1 124 ? 113.206 101.771 160.245 1.00 25.46  ? 324 ARG A CG  1 
ATOM   829  C  CD  . ARG A 1 124 ? 113.081 100.258 160.255 1.00 25.46  ? 324 ARG A CD  1 
ATOM   830  N  NE  . ARG A 1 124 ? 112.137 99.801  161.267 1.00 25.46  ? 324 ARG A NE  1 
ATOM   831  C  CZ  . ARG A 1 124 ? 112.344 98.768  162.074 1.00 25.46  ? 324 ARG A CZ  1 
ATOM   832  N  N   . ALA A 1 125 ? 114.855 104.602 160.492 1.00 25.17  ? 325 ALA A N   1 
ATOM   833  C  CA  . ALA A 1 125 ? 116.115 104.952 161.133 1.00 25.17  ? 325 ALA A CA  1 
ATOM   834  C  C   . ALA A 1 125 ? 116.183 104.303 162.507 1.00 25.17  ? 325 ALA A C   1 
ATOM   835  O  O   . ALA A 1 125 ? 115.164 104.199 163.198 1.00 25.17  ? 325 ALA A O   1 
ATOM   836  C  CB  . ALA A 1 125 ? 116.272 106.470 161.258 1.00 25.17  ? 325 ALA A CB  1 
ATOM   837  N  N   . THR A 1 126 ? 117.377 103.864 162.896 1.00 26.46  ? 326 THR A N   1 
ATOM   838  C  CA  . THR A 1 126 ? 117.620 103.270 164.204 1.00 26.46  ? 326 THR A CA  1 
ATOM   839  C  C   . THR A 1 126 ? 118.822 103.949 164.843 1.00 26.46  ? 326 THR A C   1 
ATOM   840  O  O   . THR A 1 126 ? 119.869 104.091 164.203 1.00 26.46  ? 326 THR A O   1 
ATOM   841  C  CB  . THR A 1 126 ? 117.858 101.761 164.092 1.00 26.46  ? 326 THR A CB  1 
ATOM   842  O  OG1 . THR A 1 126 ? 116.764 101.152 163.395 1.00 26.46  ? 326 THR A OG1 1 
ATOM   843  C  CG2 . THR A 1 126 ? 117.981 101.135 165.473 1.00 26.46  ? 326 THR A CG2 1 
ATOM   844  N  N   . THR A 1 127 ? 118.672 104.367 166.098 1.00 27.02  ? 327 THR A N   1 
ATOM   845  C  CA  . THR A 1 127 ? 119.713 105.086 166.818 1.00 27.02  ? 327 THR A CA  1 
ATOM   846  C  C   . THR A 1 127 ? 119.980 104.425 168.163 1.00 27.02  ? 327 THR A C   1 
ATOM   847  O  O   . THR A 1 127 ? 119.048 103.999 168.853 1.00 27.02  ? 327 THR A O   1 
ATOM   848  C  CB  . THR A 1 127 ? 119.323 106.555 167.035 1.00 27.02  ? 327 THR A CB  1 
ATOM   849  O  OG1 . THR A 1 127 ? 118.663 107.053 165.865 1.00 27.02  ? 327 THR A OG1 1 
ATOM   850  C  CG2 . THR A 1 127 ? 120.556 107.399 167.315 1.00 27.02  ? 327 THR A CG2 1 
ATOM   851  N  N   . ASN A 1 128 ? 121.260 104.342 168.526 1.00 28.23  ? 328 ASN A N   1 
ATOM   852  C  CA  . ASN A 1 128 ? 121.694 103.836 169.822 1.00 28.23  ? 328 ASN A CA  1 
ATOM   853  C  C   . ASN A 1 128 ? 122.614 104.865 170.460 1.00 28.23  ? 328 ASN A C   1 
ATOM   854  O  O   . ASN A 1 128 ? 123.543 105.355 169.810 1.00 28.23  ? 328 ASN A O   1 
ATOM   855  C  CB  . ASN A 1 128 ? 122.413 102.490 169.684 1.00 28.23  ? 328 ASN A CB  1 
ATOM   856  C  CG  . ASN A 1 128 ? 121.476 101.363 169.295 1.00 28.23  ? 328 ASN A CG  1 
ATOM   857  O  OD1 . ASN A 1 128 ? 121.334 101.038 168.116 1.00 28.23  ? 328 ASN A OD1 1 
ATOM   858  N  ND2 . ASN A 1 128 ? 120.830 100.763 170.287 1.00 28.23  ? 328 ASN A ND2 1 
ATOM   859  N  N   . SER A 1 129 ? 122.360 105.190 171.726 1.00 30.65  ? 329 SER A N   1 
ATOM   860  C  CA  . SER A 1 129 ? 123.088 106.235 172.427 1.00 30.65  ? 329 SER A CA  1 
ATOM   861  C  C   . SER A 1 129 ? 123.643 105.713 173.747 1.00 30.65  ? 329 SER A C   1 
ATOM   862  O  O   . SER A 1 129 ? 123.025 104.889 174.426 1.00 30.65  ? 329 SER A O   1 
ATOM   863  C  CB  . SER A 1 129 ? 122.194 107.455 172.686 1.00 30.65  ? 329 SER A CB  1 
ATOM   864  O  OG  . SER A 1 129 ? 121.875 108.120 171.476 1.00 30.65  ? 329 SER A OG  1 
ATOM   865  N  N   . LYS A 1 130 ? 124.813 106.238 174.109 1.00 33.50  ? 330 LYS A N   1 
ATOM   866  C  CA  . LYS A 1 130 ? 125.564 105.799 175.279 1.00 33.50  ? 330 LYS A CA  1 
ATOM   867  C  C   . LYS A 1 130 ? 126.245 107.012 175.895 1.00 33.50  ? 330 LYS A C   1 
ATOM   868  O  O   . LYS A 1 130 ? 127.025 107.688 175.217 1.00 33.50  ? 330 LYS A O   1 
ATOM   869  C  CB  . LYS A 1 130 ? 126.593 104.731 174.876 1.00 33.50  ? 330 LYS A CB  1 
ATOM   870  C  CG  . LYS A 1 130 ? 127.446 104.158 175.996 1.00 33.50  ? 330 LYS A CG  1 
ATOM   871  C  CD  . LYS A 1 130 ? 126.704 104.019 177.306 1.00 33.50  ? 330 LYS A CD  1 
ATOM   872  C  CE  . LYS A 1 130 ? 127.663 103.591 178.397 1.00 33.50  ? 330 LYS A CE  1 
ATOM   873  N  NZ  . LYS A 1 130 ? 127.971 104.727 179.303 1.00 33.50  ? 330 LYS A NZ  1 
ATOM   874  N  N   . THR A 1 131 ? 125.960 107.287 177.169 1.00 34.32  ? 331 THR A N   1 
ATOM   875  C  CA  . THR A 1 131 ? 126.520 108.475 177.799 1.00 34.32  ? 331 THR A CA  1 
ATOM   876  C  C   . THR A 1 131 ? 126.915 108.186 179.242 1.00 34.32  ? 331 THR A C   1 
ATOM   877  O  O   . THR A 1 131 ? 126.342 107.318 179.910 1.00 34.32  ? 331 THR A O   1 
ATOM   878  C  CB  . THR A 1 131 ? 125.542 109.657 177.748 1.00 34.32  ? 331 THR A CB  1 
ATOM   879  O  OG1 . THR A 1 131 ? 126.051 110.734 178.545 1.00 34.32  ? 331 THR A OG1 1 
ATOM   880  C  CG2 . THR A 1 131 ? 124.182 109.251 178.270 1.00 34.32  ? 331 THR A CG2 1 
ATOM   881  N  N   . ASP A 1 132 ? 127.908 108.944 179.709 1.00 37.31  ? 332 ASP A N   1 
ATOM   882  C  CA  . ASP A 1 132 ? 128.403 108.882 181.076 1.00 37.31  ? 332 ASP A CA  1 
ATOM   883  C  C   . ASP A 1 132 ? 128.577 110.299 181.604 1.00 37.31  ? 332 ASP A C   1 
ATOM   884  O  O   . ASP A 1 132 ? 129.036 111.184 180.879 1.00 37.31  ? 332 ASP A O   1 
ATOM   885  C  CB  . ASP A 1 132 ? 129.737 108.129 181.158 1.00 37.31  ? 332 ASP A CB  1 
ATOM   886  C  CG  . ASP A 1 132 ? 129.556 106.628 181.246 1.00 37.31  ? 332 ASP A CG  1 
ATOM   887  O  OD1 . ASP A 1 132 ? 129.088 106.145 182.297 1.00 37.31  ? 332 ASP A OD1 1 
ATOM   888  O  OD2 . ASP A 1 132 ? 129.883 105.930 180.263 1.00 37.31  ? 332 ASP A OD2 1 
ATOM   889  N  N   . ALA A 1 133 ? 128.212 110.506 182.867 1.00 37.46  ? 333 ALA A N   1 
ATOM   890  C  CA  . ALA A 1 133 ? 128.290 111.815 183.495 1.00 37.46  ? 333 ALA A CA  1 
ATOM   891  C  C   . ALA A 1 133 ? 128.905 111.697 184.882 1.00 37.46  ? 333 ALA A C   1 
ATOM   892  O  O   . ALA A 1 133 ? 128.684 110.715 185.596 1.00 37.46  ? 333 ALA A O   1 
ATOM   893  C  CB  . ALA A 1 133 ? 126.906 112.472 183.596 1.00 37.46  ? 333 ALA A CB  1 
ATOM   894  N  N   . ASN A 1 134 ? 129.673 112.719 185.260 1.00 40.37  ? 334 ASN A N   1 
ATOM   895  C  CA  . ASN A 1 134 ? 130.309 112.784 186.569 1.00 40.37  ? 334 ASN A CA  1 
ATOM   896  C  C   . ASN A 1 134 ? 130.051 114.153 187.178 1.00 40.37  ? 334 ASN A C   1 
ATOM   897  O  O   . ASN A 1 134 ? 130.166 115.170 186.488 1.00 40.37  ? 334 ASN A O   1 
ATOM   898  C  CB  . ASN A 1 134 ? 131.817 112.523 186.470 1.00 40.37  ? 334 ASN A CB  1 
ATOM   899  C  CG  . ASN A 1 134 ? 132.148 111.045 186.407 1.00 40.37  ? 334 ASN A CG  1 
ATOM   900  O  OD1 . ASN A 1 134 ? 132.328 110.395 187.436 1.00 40.37  ? 334 ASN A OD1 1 
ATOM   901  N  ND2 . ASN A 1 134 ? 132.230 110.507 185.196 1.00 40.37  ? 334 ASN A ND2 1 
ATOM   902  N  N   . THR A 1 135 ? 129.710 114.175 188.464 1.00 41.49  ? 335 THR A N   1 
ATOM   903  C  CA  . THR A 1 135 ? 129.379 115.408 189.167 1.00 41.49  ? 335 THR A CA  1 
ATOM   904  C  C   . THR A 1 135 ? 130.078 115.431 190.518 1.00 41.49  ? 335 THR A C   1 
ATOM   905  O  O   . THR A 1 135 ? 130.077 114.428 191.239 1.00 41.49  ? 335 THR A O   1 
ATOM   906  C  CB  . THR A 1 135 ? 127.864 115.546 189.358 1.00 41.49  ? 335 THR A CB  1 
ATOM   907  O  OG1 . THR A 1 135 ? 127.207 115.412 188.092 1.00 41.49  ? 335 THR A OG1 1 
ATOM   908  C  CG2 . THR A 1 135 ? 127.521 116.901 189.962 1.00 41.49  ? 335 THR A CG2 1 
ATOM   909  N  N   . VAL A 1 136 ? 130.677 116.572 190.852 1.00 42.89  ? 336 VAL A N   1 
ATOM   910  C  CA  . VAL A 1 136 ? 131.290 116.806 192.154 1.00 42.89  ? 336 VAL A CA  1 
ATOM   911  C  C   . VAL A 1 136 ? 130.649 118.049 192.755 1.00 42.89  ? 336 VAL A C   1 
ATOM   912  O  O   . VAL A 1 136 ? 130.557 119.086 192.089 1.00 42.89  ? 336 VAL A O   1 
ATOM   913  C  CB  . VAL A 1 136 ? 132.817 116.980 192.049 1.00 42.89  ? 336 VAL A CB  1 
ATOM   914  C  CG1 . VAL A 1 136 ? 133.470 116.775 193.408 1.00 42.89  ? 336 VAL A CG1 1 
ATOM   915  C  CG2 . VAL A 1 136 ? 133.397 116.016 191.023 1.00 42.89  ? 336 VAL A CG2 1 
ATOM   916  N  N   . GLY A 1 137 ? 130.210 117.946 194.001 1.00 46.95  ? 337 GLY A N   1 
ATOM   917  C  CA  . GLY A 1 137 ? 129.518 119.046 194.649 1.00 46.95  ? 337 GLY A CA  1 
ATOM   918  C  C   . GLY A 1 137 ? 130.059 119.301 196.038 1.00 46.95  ? 337 GLY A C   1 
ATOM   919  O  O   . GLY A 1 137 ? 130.417 118.376 196.771 1.00 46.95  ? 337 GLY A O   1 
ATOM   920  N  N   . VAL A 1 138 ? 130.102 120.583 196.398 1.00 51.06  ? 338 VAL A N   1 
ATOM   921  C  CA  . VAL A 1 138 ? 130.558 121.032 197.710 1.00 51.06  ? 338 VAL A CA  1 
ATOM   922  C  C   . VAL A 1 138 ? 129.536 122.024 198.248 1.00 51.06  ? 338 VAL A C   1 
ATOM   923  O  O   . VAL A 1 138 ? 129.138 122.956 197.541 1.00 51.06  ? 338 VAL A O   1 
ATOM   924  C  CB  . VAL A 1 138 ? 131.959 121.671 197.639 1.00 51.06  ? 338 VAL A CB  1 
ATOM   925  C  CG1 . VAL A 1 138 ? 132.175 122.635 198.799 1.00 51.06  ? 338 VAL A CG1 1 
ATOM   926  C  CG2 . VAL A 1 138 ? 133.037 120.597 197.614 1.00 51.06  ? 338 VAL A CG2 1 
ATOM   927  N  N   . SER A 1 139 ? 129.106 121.824 199.492 1.00 57.94  ? 339 SER A N   1 
ATOM   928  C  CA  . SER A 1 139 ? 128.103 122.672 200.120 1.00 57.94  ? 339 SER A CA  1 
ATOM   929  C  C   . SER A 1 139 ? 128.580 123.111 201.497 1.00 57.94  ? 339 SER A C   1 
ATOM   930  O  O   . SER A 1 139 ? 129.141 122.314 202.254 1.00 57.94  ? 339 SER A O   1 
ATOM   931  C  CB  . SER A 1 139 ? 126.758 121.945 200.243 1.00 57.94  ? 339 SER A CB  1 
ATOM   932  O  OG  . SER A 1 139 ? 126.069 122.341 201.415 1.00 57.94  ? 339 SER A OG  1 
ATOM   933  N  N   . ILE A 1 140 ? 128.353 124.384 201.812 1.00 62.96  ? 340 ILE A N   1 
ATOM   934  C  CA  . ILE A 1 140 ? 128.692 124.963 203.108 1.00 62.96  ? 340 ILE A CA  1 
ATOM   935  C  C   . ILE A 1 140 ? 127.423 125.559 203.703 1.00 62.96  ? 340 ILE A C   1 
ATOM   936  O  O   . ILE A 1 140 ? 126.717 126.320 203.033 1.00 62.96  ? 340 ILE A O   1 
ATOM   937  C  CB  . ILE A 1 140 ? 129.788 126.037 202.987 1.00 62.96  ? 340 ILE A CB  1 
ATOM   938  C  CG1 . ILE A 1 140 ? 130.911 125.562 202.059 1.00 62.96  ? 340 ILE A CG1 1 
ATOM   939  C  CG2 . ILE A 1 140 ? 130.329 126.404 204.363 1.00 62.96  ? 340 ILE A CG2 1 
ATOM   940  C  CD1 . ILE A 1 140 ? 131.968 124.724 202.745 1.00 62.96  ? 340 ILE A CD1 1 
ATOM   941  N  N   . SER A 1 141 ? 127.134 125.213 204.957 1.00 72.30  ? 341 SER A N   1 
ATOM   942  C  CA  . SER A 1 141 ? 125.952 125.709 205.648 1.00 72.30  ? 341 SER A CA  1 
ATOM   943  C  C   . SER A 1 141 ? 126.339 126.230 207.023 1.00 72.30  ? 341 SER A C   1 
ATOM   944  O  O   . SER A 1 141 ? 127.177 125.638 207.707 1.00 72.30  ? 341 SER A O   1 
ATOM   945  C  CB  . SER A 1 141 ? 124.888 124.612 205.787 1.00 72.30  ? 341 SER A CB  1 
ATOM   946  O  OG  . SER A 1 141 ? 123.861 125.011 206.678 1.00 72.30  ? 341 SER A OG  1 
ATOM   947  N  N   . ALA A 1 142 ? 125.730 127.346 207.418 1.00 79.48  ? 342 ALA A N   1 
ATOM   948  C  CA  . ALA A 1 142 ? 125.943 127.936 208.733 1.00 79.48  ? 342 ALA A CA  1 
ATOM   949  C  C   . ALA A 1 142 ? 124.632 128.524 209.226 1.00 79.48  ? 342 ALA A C   1 
ATOM   950  O  O   . ALA A 1 142 ? 123.902 129.148 208.450 1.00 79.48  ? 342 ALA A O   1 
ATOM   951  C  CB  . ALA A 1 142 ? 127.029 129.019 208.690 1.00 79.48  ? 342 ALA A CB  1 
ATOM   952  N  N   . GLY A 1 143 ? 124.334 128.326 210.508 1.00 91.76  ? 343 GLY A N   1 
ATOM   953  C  CA  . GLY A 1 143 ? 123.082 128.819 211.045 1.00 91.76  ? 343 GLY A CA  1 
ATOM   954  C  C   . GLY A 1 143 ? 123.061 128.802 212.558 1.00 91.76  ? 343 GLY A C   1 
ATOM   955  O  O   . GLY A 1 143 ? 124.058 128.494 213.217 1.00 91.76  ? 343 GLY A O   1 
ATOM   956  N  N   . TYR A 1 144 ? 121.896 129.146 213.101 1.00 101.59 ? 344 TYR A N   1 
ATOM   957  C  CA  . TYR A 1 144 ? 121.660 129.183 214.541 1.00 101.59 ? 344 TYR A CA  1 
ATOM   958  C  C   . TYR A 1 144 ? 120.421 128.357 214.860 1.00 101.59 ? 344 TYR A C   1 
ATOM   959  O  O   . TYR A 1 144 ? 119.294 128.801 214.615 1.00 101.59 ? 344 TYR A O   1 
ATOM   960  C  CB  . TYR A 1 144 ? 121.497 130.621 215.037 1.00 101.59 ? 344 TYR A CB  1 
ATOM   961  C  CG  . TYR A 1 144 ? 121.243 130.731 216.525 1.00 101.59 ? 344 TYR A CG  1 
ATOM   962  C  CD1 . TYR A 1 144 ? 122.295 130.736 217.430 1.00 101.59 ? 344 TYR A CD1 1 
ATOM   963  C  CD2 . TYR A 1 144 ? 119.951 130.836 217.023 1.00 101.59 ? 344 TYR A CD2 1 
ATOM   964  C  CE1 . TYR A 1 144 ? 122.068 130.837 218.790 1.00 101.59 ? 344 TYR A CE1 1 
ATOM   965  C  CE2 . TYR A 1 144 ? 119.713 130.938 218.381 1.00 101.59 ? 344 TYR A CE2 1 
ATOM   966  C  CZ  . TYR A 1 144 ? 120.776 130.937 219.259 1.00 101.59 ? 344 TYR A CZ  1 
ATOM   967  N  N   . GLN A 1 145 ? 120.631 127.157 215.403 1.00 105.95 ? 345 GLN A N   1 
ATOM   968  C  CA  . GLN A 1 145 ? 119.551 126.302 215.893 1.00 105.95 ? 345 GLN A CA  1 
ATOM   969  C  C   . GLN A 1 145 ? 119.934 125.829 217.298 1.00 105.95 ? 345 GLN A C   1 
ATOM   970  O  O   . GLN A 1 145 ? 120.553 124.777 217.468 1.00 105.95 ? 345 GLN A O   1 
ATOM   971  C  CB  . GLN A 1 145 ? 119.295 125.127 214.948 1.00 105.95 ? 345 GLN A CB  1 
ATOM   972  C  CG  . GLN A 1 145 ? 117.975 124.416 215.191 1.00 105.95 ? 345 GLN A CG  1 
ATOM   973  C  CD  . GLN A 1 145 ? 117.670 123.370 214.137 1.00 105.95 ? 345 GLN A CD  1 
ATOM   974  O  OE1 . GLN A 1 145 ? 117.272 122.249 214.454 1.00 105.95 ? 345 GLN A OE1 1 
ATOM   975  N  NE2 . GLN A 1 145 ? 117.858 123.733 212.874 1.00 105.95 ? 345 GLN A NE2 1 
ATOM   976  N  N   . ASN A 1 146 ? 119.553 126.624 218.302 1.00 107.38 ? 346 ASN A N   1 
ATOM   977  C  CA  . ASN A 1 146 ? 119.964 126.406 219.685 1.00 107.38 ? 346 ASN A CA  1 
ATOM   978  C  C   . ASN A 1 146 ? 121.483 126.329 219.780 1.00 107.38 ? 346 ASN A C   1 
ATOM   979  O  O   . ASN A 1 146 ? 122.029 125.464 220.473 1.00 107.38 ? 346 ASN A O   1 
ATOM   980  C  CB  . ASN A 1 146 ? 119.319 125.139 220.254 1.00 107.38 ? 346 ASN A CB  1 
ATOM   981  C  CG  . ASN A 1 146 ? 117.985 125.414 220.921 1.00 107.38 ? 346 ASN A CG  1 
ATOM   982  O  OD1 . ASN A 1 146 ? 117.050 125.901 220.288 1.00 107.38 ? 346 ASN A OD1 1 
ATOM   983  N  ND2 . ASN A 1 146 ? 117.892 125.101 222.209 1.00 107.38 ? 346 ASN A ND2 1 
ATOM   984  N  N   . GLY A 1 147 ? 122.166 127.229 219.087 1.00 105.61 ? 347 GLY A N   1 
ATOM   985  C  CA  . GLY A 1 147 ? 123.613 127.251 219.035 1.00 105.61 ? 347 GLY A CA  1 
ATOM   986  C  C   . GLY A 1 147 ? 124.124 127.573 217.642 1.00 105.61 ? 347 GLY A C   1 
ATOM   987  O  O   . GLY A 1 147 ? 123.403 127.519 216.647 1.00 105.61 ? 347 GLY A O   1 
ATOM   988  N  N   . PHE A 1 148 ? 125.409 127.915 217.597 1.00 104.13 ? 348 PHE A N   1 
ATOM   989  C  CA  . PHE A 1 148 ? 126.079 128.275 216.351 1.00 104.13 ? 348 PHE A CA  1 
ATOM   990  C  C   . PHE A 1 148 ? 126.502 126.991 215.647 1.00 104.13 ? 348 PHE A C   1 
ATOM   991  O  O   . PHE A 1 148 ? 127.506 126.376 216.019 1.00 104.13 ? 348 PHE A O   1 
ATOM   992  C  CB  . PHE A 1 148 ? 127.290 129.173 216.616 1.00 104.13 ? 348 PHE A CB  1 
ATOM   993  C  CG  . PHE A 1 148 ? 126.945 130.564 217.096 1.00 104.13 ? 348 PHE A CG  1 
ATOM   994  C  CD1 . PHE A 1 148 ? 125.687 130.866 217.594 1.00 104.13 ? 348 PHE A CD1 1 
ATOM   995  C  CD2 . PHE A 1 148 ? 127.896 131.570 217.051 1.00 104.13 ? 348 PHE A CD2 1 
ATOM   996  C  CE1 . PHE A 1 148 ? 125.386 132.142 218.034 1.00 104.13 ? 348 PHE A CE1 1 
ATOM   997  C  CE2 . PHE A 1 148 ? 127.601 132.848 217.489 1.00 104.13 ? 348 PHE A CE2 1 
ATOM   998  C  CZ  . PHE A 1 148 ? 126.343 133.134 217.981 1.00 104.13 ? 348 PHE A CZ  1 
ATOM   999  N  N   . THR A 1 149 ? 125.744 126.583 214.633 1.00 97.38  ? 349 THR A N   1 
ATOM   1000 C  CA  . THR A 1 149 ? 125.995 125.329 213.941 1.00 97.38  ? 349 THR A CA  1 
ATOM   1001 C  C   . THR A 1 149 ? 126.532 125.575 212.535 1.00 97.38  ? 349 THR A C   1 
ATOM   1002 O  O   . THR A 1 149 ? 126.193 126.559 211.873 1.00 97.38  ? 349 THR A O   1 
ATOM   1003 C  CB  . THR A 1 149 ? 124.721 124.481 213.868 1.00 97.38  ? 349 THR A CB  1 
ATOM   1004 O  OG1 . THR A 1 149 ? 123.973 124.838 212.700 1.00 97.38  ? 349 THR A OG1 1 
ATOM   1005 C  CG2 . THR A 1 149 ? 123.861 124.697 215.104 1.00 97.38  ? 349 THR A CG2 1 
ATOM   1006 N  N   . GLY A 1 150 ? 127.385 124.652 212.087 1.00 88.14  ? 350 GLY A N   1 
ATOM   1007 C  CA  . GLY A 1 150 ? 127.945 124.702 210.752 1.00 88.14  ? 350 GLY A CA  1 
ATOM   1008 C  C   . GLY A 1 150 ? 128.099 123.302 210.200 1.00 88.14  ? 350 GLY A C   1 
ATOM   1009 O  O   . GLY A 1 150 ? 128.086 122.314 210.938 1.00 88.14  ? 350 GLY A O   1 
ATOM   1010 N  N   . ASN A 1 151 ? 128.247 123.226 208.879 1.00 75.30  ? 351 ASN A N   1 
ATOM   1011 C  CA  . ASN A 1 151 ? 128.327 121.934 208.211 1.00 75.30  ? 351 ASN A CA  1 
ATOM   1012 C  C   . ASN A 1 151 ? 128.988 122.116 206.852 1.00 75.30  ? 351 ASN A C   1 
ATOM   1013 O  O   . ASN A 1 151 ? 128.745 123.111 206.165 1.00 75.30  ? 351 ASN A O   1 
ATOM   1014 C  CB  . ASN A 1 151 ? 126.928 121.309 208.066 1.00 75.30  ? 351 ASN A CB  1 
ATOM   1015 C  CG  . ASN A 1 151 ? 126.906 120.087 207.154 1.00 75.30  ? 351 ASN A CG  1 
ATOM   1016 O  OD1 . ASN A 1 151 ? 127.178 120.173 205.955 1.00 75.30  ? 351 ASN A OD1 1 
ATOM   1017 N  ND2 . ASN A 1 151 ? 126.580 118.936 207.729 1.00 75.30  ? 351 ASN A ND2 1 
ATOM   1018 N  N   . ILE A 1 152 ? 129.823 121.147 206.480 1.00 69.77  ? 352 ILE A N   1 
ATOM   1019 C  CA  . ILE A 1 152 ? 130.456 121.089 205.168 1.00 69.77  ? 352 ILE A CA  1 
ATOM   1020 C  C   . ILE A 1 152 ? 130.181 119.714 204.577 1.00 69.77  ? 352 ILE A C   1 
ATOM   1021 O  O   . ILE A 1 152 ? 130.400 118.695 205.242 1.00 69.77  ? 352 ILE A O   1 
ATOM   1022 C  CB  . ILE A 1 152 ? 131.972 121.351 205.247 1.00 69.77  ? 352 ILE A CB  1 
ATOM   1023 C  CG1 . ILE A 1 152 ? 132.249 122.725 205.857 1.00 69.77  ? 352 ILE A CG1 1 
ATOM   1024 C  CG2 . ILE A 1 152 ? 132.608 121.236 203.868 1.00 69.77  ? 352 ILE A CG2 1 
ATOM   1025 C  CD1 . ILE A 1 152 ? 133.348 122.720 206.897 1.00 69.77  ? 352 ILE A CD1 1 
ATOM   1026 N  N   . THR A 1 153 ? 129.702 119.682 203.336 1.00 62.54  ? 353 THR A N   1 
ATOM   1027 C  CA  . THR A 1 153 ? 129.328 118.439 202.674 1.00 62.54  ? 353 THR A CA  1 
ATOM   1028 C  C   . THR A 1 153 ? 130.027 118.345 201.326 1.00 62.54  ? 353 THR A C   1 
ATOM   1029 O  O   . THR A 1 153 ? 130.055 119.320 200.569 1.00 62.54  ? 353 THR A O   1 
ATOM   1030 C  CB  . THR A 1 153 ? 127.809 118.347 202.485 1.00 62.54  ? 353 THR A CB  1 
ATOM   1031 O  OG1 . THR A 1 153 ? 127.154 118.580 203.738 1.00 62.54  ? 353 THR A OG1 1 
ATOM   1032 C  CG2 . THR A 1 153 ? 127.415 116.973 201.964 1.00 62.54  ? 353 THR A CG2 1 
ATOM   1033 N  N   . THR A 1 154 ? 130.591 117.176 201.033 1.00 55.07  ? 354 THR A N   1 
ATOM   1034 C  CA  . THR A 1 154 ? 131.203 116.887 199.743 1.00 55.07  ? 354 THR A CA  1 
ATOM   1035 C  C   . THR A 1 154 ? 130.552 115.638 199.167 1.00 55.07  ? 354 THR A C   1 
ATOM   1036 O  O   . THR A 1 154 ? 130.446 114.619 199.855 1.00 55.07  ? 354 THR A O   1 
ATOM   1037 C  CB  . THR A 1 154 ? 132.716 116.689 199.878 1.00 55.07  ? 354 THR A CB  1 
ATOM   1038 O  OG1 . THR A 1 154 ? 133.289 117.811 200.562 1.00 55.07  ? 354 THR A OG1 1 
ATOM   1039 C  CG2 . THR A 1 154 ? 133.362 116.556 198.506 1.00 55.07  ? 354 THR A CG2 1 
ATOM   1040 N  N   . SER A 1 155 ? 130.121 115.718 197.909 1.00 48.30  ? 355 SER A N   1 
ATOM   1041 C  CA  . SER A 1 155 ? 129.408 114.623 197.268 1.00 48.30  ? 355 SER A CA  1 
ATOM   1042 C  C   . SER A 1 155 ? 129.957 114.375 195.871 1.00 48.30  ? 355 SER A C   1 
ATOM   1043 O  O   . SER A 1 155 ? 130.408 115.298 195.187 1.00 48.30  ? 355 SER A O   1 
ATOM   1044 C  CB  . SER A 1 155 ? 127.902 114.907 197.187 1.00 48.30  ? 355 SER A CB  1 
ATOM   1045 O  OG  . SER A 1 155 ? 127.598 115.729 196.073 1.00 48.30  ? 355 SER A OG  1 
ATOM   1046 N  N   . TYR A 1 156 ? 129.898 113.113 195.451 1.00 45.18  ? 356 TYR A N   1 
ATOM   1047 C  CA  . TYR A 1 156 ? 130.352 112.692 194.135 1.00 45.18  ? 356 TYR A CA  1 
ATOM   1048 C  C   . TYR A 1 156 ? 129.330 111.732 193.539 1.00 45.18  ? 356 TYR A C   1 
ATOM   1049 O  O   . TYR A 1 156 ? 128.835 110.827 194.217 1.00 45.18  ? 356 TYR A O   1 
ATOM   1050 C  CB  . TYR A 1 156 ? 131.739 112.032 194.218 1.00 45.18  ? 356 TYR A CB  1 
ATOM   1051 C  CG  . TYR A 1 156 ? 132.177 111.311 192.964 1.00 45.18  ? 356 TYR A CG  1 
ATOM   1052 C  CD1 . TYR A 1 156 ? 132.740 112.008 191.903 1.00 45.18  ? 356 TYR A CD1 1 
ATOM   1053 C  CD2 . TYR A 1 156 ? 132.037 109.934 192.843 1.00 45.18  ? 356 TYR A CD2 1 
ATOM   1054 C  CE1 . TYR A 1 156 ? 133.148 111.356 190.756 1.00 45.18  ? 356 TYR A CE1 1 
ATOM   1055 C  CE2 . TYR A 1 156 ? 132.443 109.273 191.700 1.00 45.18  ? 356 TYR A CE2 1 
ATOM   1056 C  CZ  . TYR A 1 156 ? 132.997 109.989 190.660 1.00 45.18  ? 356 TYR A CZ  1 
ATOM   1057 N  N   . SER A 1 157 ? 129.020 111.933 192.259 1.00 42.47  ? 357 SER A N   1 
ATOM   1058 C  CA  . SER A 1 157 ? 127.970 111.172 191.597 1.00 42.47  ? 357 SER A CA  1 
ATOM   1059 C  C   . SER A 1 157 ? 128.427 110.768 190.203 1.00 42.47  ? 357 SER A C   1 
ATOM   1060 O  O   . SER A 1 157 ? 129.071 111.547 189.495 1.00 42.47  ? 357 SER A O   1 
ATOM   1061 C  CB  . SER A 1 157 ? 126.666 111.974 191.511 1.00 42.47  ? 357 SER A CB  1 
ATOM   1062 O  OG  . SER A 1 157 ? 125.540 111.116 191.449 1.00 42.47  ? 357 SER A OG  1 
ATOM   1063 N  N   . HIS A 1 158 ? 128.084 109.541 189.817 1.00 40.01  ? 358 HIS A N   1 
ATOM   1064 C  CA  . HIS A 1 158 ? 128.395 109.016 188.493 1.00 40.01  ? 358 HIS A CA  1 
ATOM   1065 C  C   . HIS A 1 158 ? 127.140 108.397 187.899 1.00 40.01  ? 358 HIS A C   1 
ATOM   1066 O  O   . HIS A 1 158 ? 126.459 107.613 188.566 1.00 40.01  ? 358 HIS A O   1 
ATOM   1067 C  CB  . HIS A 1 158 ? 129.523 107.980 188.558 1.00 40.01  ? 358 HIS A CB  1 
ATOM   1068 C  CG  . HIS A 1 158 ? 129.839 107.344 187.242 1.00 40.01  ? 358 HIS A CG  1 
ATOM   1069 N  ND1 . HIS A 1 158 ? 130.559 107.986 186.258 1.00 40.01  ? 358 HIS A ND1 1 
ATOM   1070 C  CD2 . HIS A 1 158 ? 129.535 106.121 186.747 1.00 40.01  ? 358 HIS A CD2 1 
ATOM   1071 C  CE1 . HIS A 1 158 ? 130.684 107.187 185.214 1.00 40.01  ? 358 HIS A CE1 1 
ATOM   1072 N  NE2 . HIS A 1 158 ? 130.071 106.050 185.484 1.00 40.01  ? 358 HIS A NE2 1 
ATOM   1073 N  N   . THR A 1 159 ? 126.838 108.745 186.649 1.00 38.63  ? 359 THR A N   1 
ATOM   1074 C  CA  . THR A 1 159 ? 125.628 108.299 185.972 1.00 38.63  ? 359 THR A CA  1 
ATOM   1075 C  C   . THR A 1 159 ? 125.987 107.653 184.642 1.00 38.63  ? 359 THR A C   1 
ATOM   1076 O  O   . THR A 1 159 ? 126.784 108.204 183.876 1.00 38.63  ? 359 THR A O   1 
ATOM   1077 C  CB  . THR A 1 159 ? 124.661 109.467 185.745 1.00 38.63  ? 359 THR A CB  1 
ATOM   1078 O  OG1 . THR A 1 159 ? 124.320 110.061 187.004 1.00 38.63  ? 359 THR A OG1 1 
ATOM   1079 C  CG2 . THR A 1 159 ? 123.389 108.986 185.060 1.00 38.63  ? 359 THR A CG2 1 
ATOM   1080 N  N   . THR A 1 160 ? 125.399 106.491 184.374 1.00 38.13  ? 360 THR A N   1 
ATOM   1081 C  CA  . THR A 1 160 ? 125.570 105.767 183.120 1.00 38.13  ? 360 THR A CA  1 
ATOM   1082 C  C   . THR A 1 160 ? 124.207 105.587 182.469 1.00 38.13  ? 360 THR A C   1 
ATOM   1083 O  O   . THR A 1 160 ? 123.263 105.136 183.125 1.00 38.13  ? 360 THR A O   1 
ATOM   1084 C  CB  . THR A 1 160 ? 126.227 104.405 183.361 1.00 38.13  ? 360 THR A CB  1 
ATOM   1085 O  OG1 . THR A 1 160 ? 127.346 104.557 184.243 1.00 38.13  ? 360 THR A OG1 1 
ATOM   1086 C  CG2 . THR A 1 160 ? 126.689 103.788 182.056 1.00 38.13  ? 360 THR A CG2 1 
ATOM   1087 N  N   . ASP A 1 161 ? 124.096 105.934 181.185 1.00 35.44  ? 361 ASP A N   1 
ATOM   1088 C  CA  . ASP A 1 161 ? 122.810 105.864 180.508 1.00 35.44  ? 361 ASP A CA  1 
ATOM   1089 C  C   . ASP A 1 161 ? 122.963 105.260 179.118 1.00 35.44  ? 361 ASP A C   1 
ATOM   1090 O  O   . ASP A 1 161 ? 123.907 105.582 178.388 1.00 35.44  ? 361 ASP A O   1 
ATOM   1091 C  CB  . ASP A 1 161 ? 122.156 107.252 180.412 1.00 35.44  ? 361 ASP A CB  1 
ATOM   1092 C  CG  . ASP A 1 161 ? 121.066 107.317 179.358 1.00 35.44  ? 361 ASP A CG  1 
ATOM   1093 O  OD1 . ASP A 1 161 ? 119.899 107.032 179.695 1.00 35.44  ? 361 ASP A OD1 1 
ATOM   1094 O  OD2 . ASP A 1 161 ? 121.374 107.653 178.195 1.00 35.44  ? 361 ASP A OD2 1 
ATOM   1095 N  N   . ASN A 1 162 ? 122.018 104.388 178.766 1.00 33.45  ? 362 ASN A N   1 
ATOM   1096 C  CA  . ASN A 1 162 ? 121.923 103.772 177.450 1.00 33.45  ? 362 ASN A CA  1 
ATOM   1097 C  C   . ASN A 1 162 ? 120.522 104.001 176.901 1.00 33.45  ? 362 ASN A C   1 
ATOM   1098 O  O   . ASN A 1 162 ? 119.538 103.902 177.638 1.00 33.45  ? 362 ASN A O   1 
ATOM   1099 C  CB  . ASN A 1 162 ? 122.217 102.267 177.511 1.00 33.45  ? 362 ASN A CB  1 
ATOM   1100 C  CG  . ASN A 1 162 ? 123.700 101.962 177.523 1.00 33.45  ? 362 ASN A CG  1 
ATOM   1101 O  OD1 . ASN A 1 162 ? 124.361 102.001 176.487 1.00 33.45  ? 362 ASN A OD1 1 
ATOM   1102 N  ND2 . ASN A 1 162 ? 124.230 101.655 178.701 1.00 33.45  ? 362 ASN A ND2 1 
ATOM   1103 N  N   . SER A 1 163 ? 120.434 104.304 175.607 1.00 31.18  ? 363 SER A N   1 
ATOM   1104 C  CA  . SER A 1 163 ? 119.156 104.612 174.982 1.00 31.18  ? 363 SER A CA  1 
ATOM   1105 C  C   . SER A 1 163 ? 119.097 104.010 173.586 1.00 31.18  ? 363 SER A C   1 
ATOM   1106 O  O   . SER A 1 163 ? 120.122 103.829 172.927 1.00 31.18  ? 363 SER A O   1 
ATOM   1107 C  CB  . SER A 1 163 ? 118.920 106.127 174.900 1.00 31.18  ? 363 SER A CB  1 
ATOM   1108 O  OG  . SER A 1 163 ? 119.265 106.764 176.117 1.00 31.18  ? 363 SER A OG  1 
ATOM   1109 N  N   . THR A 1 164 ? 117.878 103.714 173.138 1.00 30.16  ? 364 THR A N   1 
ATOM   1110 C  CA  . THR A 1 164 ? 117.647 103.236 171.783 1.00 30.16  ? 364 THR A CA  1 
ATOM   1111 C  C   . THR A 1 164 ? 116.397 103.908 171.233 1.00 30.16  ? 364 THR A C   1 
ATOM   1112 O  O   . THR A 1 164 ? 115.508 104.311 171.989 1.00 30.16  ? 364 THR A O   1 
ATOM   1113 C  CB  . THR A 1 164 ? 117.505 101.707 171.732 1.00 30.16  ? 364 THR A CB  1 
ATOM   1114 O  OG1 . THR A 1 164 ? 117.499 101.270 170.367 1.00 30.16  ? 364 THR A OG1 1 
ATOM   1115 C  CG2 . THR A 1 164 ? 116.220 101.258 172.413 1.00 30.16  ? 364 THR A CG2 1 
ATOM   1116 N  N   . ALA A 1 165 ? 116.343 104.041 169.909 1.00 27.47  ? 365 ALA A N   1 
ATOM   1117 C  CA  . ALA A 1 165 ? 115.218 104.708 169.272 1.00 27.47  ? 365 ALA A CA  1 
ATOM   1118 C  C   . ALA A 1 165 ? 115.037 104.174 167.857 1.00 27.47  ? 365 ALA A C   1 
ATOM   1119 O  O   . ALA A 1 165 ? 116.018 103.898 167.163 1.00 27.47  ? 365 ALA A O   1 
ATOM   1120 C  CB  . ALA A 1 165 ? 115.416 106.228 169.242 1.00 27.47  ? 365 ALA A CB  1 
ATOM   1121 N  N   . VAL A 1 166 ? 113.779 104.034 167.444 1.00 25.75  ? 366 VAL A N   1 
ATOM   1122 C  CA  . VAL A 1 166 ? 113.421 103.606 166.097 1.00 25.75  ? 366 VAL A CA  1 
ATOM   1123 C  C   . VAL A 1 166 ? 112.401 104.590 165.539 1.00 25.75  ? 366 VAL A C   1 
ATOM   1124 O  O   . VAL A 1 166 ? 111.400 104.891 166.198 1.00 25.75  ? 366 VAL A O   1 
ATOM   1125 C  CB  . VAL A 1 166 ? 112.852 102.172 166.078 1.00 25.75  ? 366 VAL A CB  1 
ATOM   1126 C  CG1 . VAL A 1 166 ? 112.497 101.761 164.658 1.00 25.75  ? 366 VAL A CG1 1 
ATOM   1127 C  CG2 . VAL A 1 166 ? 113.845 101.194 166.686 1.00 25.75  ? 366 VAL A CG2 1 
ATOM   1128 N  N   . GLN A 1 167 ? 112.655 105.087 164.331 1.00 26.13  ? 367 GLN A N   1 
ATOM   1129 C  CA  . GLN A 1 167 ? 111.777 106.040 163.667 1.00 26.13  ? 367 GLN A CA  1 
ATOM   1130 C  C   . GLN A 1 167 ? 111.365 105.504 162.302 1.00 26.13  ? 367 GLN A C   1 
ATOM   1131 O  O   . GLN A 1 167 ? 112.193 104.960 161.565 1.00 26.13  ? 367 GLN A O   1 
ATOM   1132 C  CB  . GLN A 1 167 ? 112.460 107.403 163.509 1.00 26.13  ? 367 GLN A CB  1 
ATOM   1133 C  CG  . GLN A 1 167 ? 111.609 108.452 162.809 1.00 26.13  ? 367 GLN A CG  1 
ATOM   1134 C  CD  . GLN A 1 167 ? 112.255 109.823 162.809 1.00 26.13  ? 367 GLN A CD  1 
ATOM   1135 O  OE1 . GLN A 1 167 ? 113.247 110.054 162.118 1.00 26.13  ? 367 GLN A OE1 1 
ATOM   1136 N  NE2 . GLN A 1 167 ? 111.693 110.742 163.588 1.00 26.13  ? 367 GLN A NE2 1 
ATOM   1137 N  N   . ASP A 1 168 ? 110.085 105.660 161.972 1.00 26.56  ? 368 ASP A N   1 
ATOM   1138 C  CA  . ASP A 1 168 ? 109.538 105.267 160.680 1.00 26.56  ? 368 ASP A CA  1 
ATOM   1139 C  C   . ASP A 1 168 ? 108.876 106.478 160.038 1.00 26.56  ? 368 ASP A C   1 
ATOM   1140 O  O   . ASP A 1 168 ? 108.103 107.183 160.693 1.00 26.56  ? 368 ASP A O   1 
ATOM   1141 C  CB  . ASP A 1 168 ? 108.528 104.126 160.833 1.00 26.56  ? 368 ASP A CB  1 
ATOM   1142 C  CG  . ASP A 1 168 ? 109.194 102.779 161.035 1.00 26.56  ? 368 ASP A CG  1 
ATOM   1143 O  OD1 . ASP A 1 168 ? 109.804 102.265 160.073 1.00 26.56  ? 368 ASP A OD1 1 
ATOM   1144 O  OD2 . ASP A 1 168 ? 109.110 102.236 162.156 1.00 26.56  ? 368 ASP A OD2 1 
ATOM   1145 N  N   . SER A 1 169 ? 109.176 106.716 158.761 1.00 24.44  ? 369 SER A N   1 
ATOM   1146 C  CA  . SER A 1 169 ? 108.689 107.891 158.058 1.00 24.44  ? 369 SER A CA  1 
ATOM   1147 C  C   . SER A 1 169 ? 108.083 107.497 156.719 1.00 24.44  ? 369 SER A C   1 
ATOM   1148 O  O   . SER A 1 169 ? 108.615 106.645 156.002 1.00 24.44  ? 369 SER A O   1 
ATOM   1149 C  CB  . SER A 1 169 ? 109.813 108.912 157.833 1.00 24.44  ? 369 SER A CB  1 
ATOM   1150 O  OG  . SER A 1 169 ? 110.237 109.482 159.058 1.00 24.44  ? 369 SER A OG  1 
ATOM   1151 N  N   . ASN A 1 170 ? 106.966 108.144 156.386 1.00 24.80  ? 370 ASN A N   1 
ATOM   1152 C  CA  . ASN A 1 170 ? 106.298 107.971 155.102 1.00 24.80  ? 370 ASN A CA  1 
ATOM   1153 C  C   . ASN A 1 170 ? 105.962 109.348 154.554 1.00 24.80  ? 370 ASN A C   1 
ATOM   1154 O  O   . ASN A 1 170 ? 105.554 110.230 155.313 1.00 24.80  ? 370 ASN A O   1 
ATOM   1155 C  CB  . ASN A 1 170 ? 105.026 107.128 155.244 1.00 24.80  ? 370 ASN A CB  1 
ATOM   1156 C  CG  . ASN A 1 170 ? 105.318 105.654 155.437 1.00 24.80  ? 370 ASN A CG  1 
ATOM   1157 O  OD1 . ASN A 1 170 ? 105.402 105.169 156.565 1.00 24.80  ? 370 ASN A OD1 1 
ATOM   1158 N  ND2 . ASN A 1 170 ? 105.471 104.931 154.334 1.00 24.80  ? 370 ASN A ND2 1 
ATOM   1159 N  N   . GLY A 1 171 ? 106.133 109.530 153.251 1.00 22.33  ? 371 GLY A N   1 
ATOM   1160 C  CA  . GLY A 1 171 ? 105.914 110.827 152.638 1.00 22.33  ? 371 GLY A CA  1 
ATOM   1161 C  C   . GLY A 1 171 ? 105.404 110.704 151.219 1.00 22.33  ? 371 GLY A C   1 
ATOM   1162 O  O   . GLY A 1 171 ? 105.667 109.722 150.522 1.00 22.33  ? 371 GLY A O   1 
ATOM   1163 N  N   . GLU A 1 172 ? 104.676 111.738 150.791 1.00 24.42  ? 372 GLU A N   1 
ATOM   1164 C  CA  . GLU A 1 172 ? 104.117 111.821 149.450 1.00 24.42  ? 372 GLU A CA  1 
ATOM   1165 C  C   . GLU A 1 172 ? 104.450 113.185 148.862 1.00 24.42  ? 372 GLU A C   1 
ATOM   1166 O  O   . GLU A 1 172 ? 104.600 114.169 149.590 1.00 24.42  ? 372 GLU A O   1 
ATOM   1167 C  CB  . GLU A 1 172 ? 102.597 111.611 149.461 1.00 24.42  ? 372 GLU A CB  1 
ATOM   1168 C  CG  . GLU A 1 172 ? 102.166 110.162 149.333 1.00 24.42  ? 372 GLU A CG  1 
ATOM   1169 C  CD  . GLU A 1 172 ? 100.671 110.016 149.128 1.00 24.42  ? 372 GLU A CD  1 
ATOM   1170 O  OE1 . GLU A 1 172 ? 99.924  110.079 150.128 1.00 24.42  ? 372 GLU A OE1 1 
ATOM   1171 O  OE2 . GLU A 1 172 ? 100.241 109.835 147.969 1.00 24.42  ? 372 GLU A OE2 1 
ATOM   1172 N  N   . SER A 1 173 ? 104.562 113.237 147.535 1.00 23.07  ? 373 SER A N   1 
ATOM   1173 C  CA  . SER A 1 173 ? 104.933 114.467 146.849 1.00 23.07  ? 373 SER A CA  1 
ATOM   1174 C  C   . SER A 1 173 ? 104.230 114.556 145.502 1.00 23.07  ? 373 SER A C   1 
ATOM   1175 O  O   . SER A 1 173 ? 104.110 113.565 144.776 1.00 23.07  ? 373 SER A O   1 
ATOM   1176 C  CB  . SER A 1 173 ? 106.452 114.556 146.645 1.00 23.07  ? 373 SER A CB  1 
ATOM   1177 O  OG  . SER A 1 173 ? 106.946 113.408 145.978 1.00 23.07  ? 373 SER A OG  1 
ATOM   1178 N  N   . TRP A 1 174 ? 103.860 115.657 145.063 1.00 23.48  ? 374 TRP A N   1 
ATOM   1179 C  CA  . TRP A 1 174 ? 103.130 116.071 143.845 1.00 23.48  ? 374 TRP A CA  1 
ATOM   1180 C  C   . TRP A 1 174 ? 103.679 117.293 143.233 1.00 23.48  ? 374 TRP A C   1 
ATOM   1181 O  O   . TRP A 1 174 ? 103.597 118.158 143.674 1.00 23.48  ? 374 TRP A O   1 
ATOM   1182 C  CB  . TRP A 1 174 ? 101.617 116.305 144.100 1.00 30.00  ? 374 TRP A CB  1 
ATOM   1183 C  CG  . TRP A 1 174 ? 100.802 115.284 144.779 1.00 30.00  ? 374 TRP A CG  1 
ATOM   1184 C  CD1 . TRP A 1 174 ? 100.093 114.303 144.200 1.00 30.00  ? 374 TRP A CD1 1 
ATOM   1185 C  CD2 . TRP A 1 174 ? 100.757 115.067 146.194 1.00 30.00  ? 374 TRP A CD2 1 
ATOM   1186 N  NE1 . TRP A 1 174 ? 99.575  113.508 145.163 1.00 30.00  ? 374 TRP A NE1 1 
ATOM   1187 C  CE2 . TRP A 1 174 ? 99.986  113.925 146.389 1.00 30.00  ? 374 TRP A CE2 1 
ATOM   1188 C  CE3 . TRP A 1 174 ? 101.354 115.678 147.289 1.00 30.00  ? 374 TRP A CE3 1 
ATOM   1189 C  CZ2 . TRP A 1 174 ? 99.709  113.443 147.658 1.00 30.00  ? 374 TRP A CZ2 1 
ATOM   1190 C  CZ3 . TRP A 1 174 ? 101.085 115.219 148.530 1.00 30.00  ? 374 TRP A CZ3 1 
ATOM   1191 C  CH2 . TRP A 1 174 ? 100.246 114.132 148.707 1.00 30.00  ? 374 TRP A CH2 1 
ATOM   1192 N  N   . ASN A 1 175 ? 104.238 117.241 142.147 1.00 23.79  ? 375 ASN A N   1 
ATOM   1193 C  CA  . ASN A 1 175 ? 104.804 118.293 141.269 1.00 23.79  ? 375 ASN A CA  1 
ATOM   1194 C  C   . ASN A 1 175 ? 104.060 118.677 139.953 1.00 23.79  ? 375 ASN A C   1 
ATOM   1195 O  O   . ASN A 1 175 ? 103.708 117.975 139.332 1.00 23.79  ? 375 ASN A O   1 
ATOM   1196 C  CB  . ASN A 1 175 ? 106.275 117.942 141.130 1.00 23.79  ? 375 ASN A CB  1 
ATOM   1197 C  CG  . ASN A 1 175 ? 107.208 118.203 142.287 1.00 23.79  ? 375 ASN A CG  1 
ATOM   1198 O  OD1 . ASN A 1 175 ? 107.510 119.339 142.670 1.00 23.79  ? 375 ASN A OD1 1 
ATOM   1199 N  ND2 . ASN A 1 175 ? 107.742 117.121 142.829 1.00 23.79  ? 375 ASN A ND2 1 
ATOM   1200 N  N   . THR A 1 176 ? 103.973 119.888 139.574 1.00 23.04  ? 376 THR A N   1 
ATOM   1201 C  CA  . THR A 1 176 ? 103.477 120.297 138.267 1.00 23.04  ? 376 THR A CA  1 
ATOM   1202 C  C   . THR A 1 176 ? 104.416 121.346 137.689 1.00 23.04  ? 376 THR A C   1 
ATOM   1203 O  O   . THR A 1 176 ? 104.905 122.218 138.414 1.00 23.04  ? 376 THR A O   1 
ATOM   1204 C  CB  . THR A 1 176 ? 102.051 120.863 138.348 1.00 23.04  ? 376 THR A CB  1 
ATOM   1205 O  OG1 . THR A 1 176 ? 101.973 121.822 139.410 1.00 23.04  ? 376 THR A OG1 1 
ATOM   1206 C  CG2 . THR A 1 176 ? 101.046 119.749 138.598 1.00 23.04  ? 376 THR A CG2 1 
ATOM   1207 N  N   . GLY A 1 177 ? 104.666 121.261 136.383 1.00 21.84  ? 377 GLY A N   1 
ATOM   1208 C  CA  . GLY A 1 177 ? 105.586 122.173 135.739 1.00 21.84  ? 377 GLY A CA  1 
ATOM   1209 C  C   . GLY A 1 177 ? 105.110 122.555 134.353 1.00 21.84  ? 377 GLY A C   1 
ATOM   1210 O  O   . GLY A 1 177 ? 104.462 121.774 133.652 1.00 21.84  ? 377 GLY A O   1 
ATOM   1211 N  N   . LEU A 1 178 ? 105.465 123.777 133.963 1.00 21.25  ? 378 LEU A N   1 
ATOM   1212 C  CA  . LEU A 1 178 ? 105.096 124.313 132.655 1.00 21.25  ? 378 LEU A CA  1 
ATOM   1213 C  C   . LEU A 1 178 ? 106.267 125.115 132.114 1.00 21.25  ? 378 LEU A C   1 
ATOM   1214 O  O   . LEU A 1 178 ? 106.790 125.990 132.811 1.00 21.25  ? 378 LEU A O   1 
ATOM   1215 C  CB  . LEU A 1 178 ? 103.844 125.181 132.752 1.00 21.25  ? 378 LEU A CB  1 
ATOM   1216 C  CG  . LEU A 1 178 ? 103.240 125.641 131.425 1.00 21.25  ? 378 LEU A CG  1 
ATOM   1217 C  CD1 . LEU A 1 178 ? 102.566 124.481 130.709 1.00 21.25  ? 378 LEU A CD1 1 
ATOM   1218 C  CD2 . LEU A 1 178 ? 102.258 126.779 131.651 1.00 21.25  ? 378 LEU A CD2 1 
ATOM   1219 N  N   . SER A 1 179 ? 106.674 124.822 130.882 1.00 21.42  ? 379 SER A N   1 
ATOM   1220 C  CA  . SER A 1 179 ? 107.785 125.506 130.237 1.00 21.42  ? 379 SER A CA  1 
ATOM   1221 C  C   . SER A 1 179 ? 107.350 126.014 128.870 1.00 21.42  ? 379 SER A C   1 
ATOM   1222 O  O   . SER A 1 179 ? 106.477 125.432 128.220 1.00 21.42  ? 379 SER A O   1 
ATOM   1223 C  CB  . SER A 1 179 ? 109.002 124.585 130.086 1.00 21.42  ? 379 SER A CB  1 
ATOM   1224 O  OG  . SER A 1 179 ? 108.625 123.316 129.585 1.00 21.42  ? 379 SER A OG  1 
ATOM   1225 N  N   . ILE A 1 180 ? 107.974 127.111 128.439 1.00 21.32  ? 380 ILE A N   1 
ATOM   1226 C  CA  . ILE A 1 180 ? 107.633 127.762 127.182 1.00 21.32  ? 380 ILE A CA  1 
ATOM   1227 C  C   . ILE A 1 180 ? 108.901 128.313 126.542 1.00 21.32  ? 380 ILE A C   1 
ATOM   1228 O  O   . ILE A 1 180 ? 109.839 128.730 127.229 1.00 21.32  ? 380 ILE A O   1 
ATOM   1229 C  CB  . ILE A 1 180 ? 106.583 128.882 127.389 1.00 21.32  ? 380 ILE A CB  1 
ATOM   1230 C  CG1 . ILE A 1 180 ? 106.055 129.394 126.045 1.00 21.32  ? 380 ILE A CG1 1 
ATOM   1231 C  CG2 . ILE A 1 180 ? 107.161 130.024 128.211 1.00 21.32  ? 380 ILE A CG2 1 
ATOM   1232 C  CD1 . ILE A 1 180 ? 105.509 128.305 125.151 1.00 21.32  ? 380 ILE A CD1 1 
ATOM   1233 N  N   . ASN A 1 181 ? 108.930 128.294 125.213 1.00 21.68  ? 381 ASN A N   1 
ATOM   1234 C  CA  . ASN A 1 181 ? 110.009 128.885 124.434 1.00 21.68  ? 381 ASN A CA  1 
ATOM   1235 C  C   . ASN A 1 181 ? 109.545 130.227 123.886 1.00 21.68  ? 381 ASN A C   1 
ATOM   1236 O  O   . ASN A 1 181 ? 108.501 130.308 123.230 1.00 21.68  ? 381 ASN A O   1 
ATOM   1237 C  CB  . ASN A 1 181 ? 110.427 127.957 123.291 1.00 21.68  ? 381 ASN A CB  1 
ATOM   1238 C  CG  . ASN A 1 181 ? 111.611 128.490 122.506 1.00 21.68  ? 381 ASN A CG  1 
ATOM   1239 O  OD1 . ASN A 1 181 ? 112.305 129.404 122.948 1.00 21.68  ? 381 ASN A OD1 1 
ATOM   1240 N  ND2 . ASN A 1 181 ? 111.845 127.916 121.332 1.00 21.68  ? 381 ASN A ND2 1 
ATOM   1241 N  N   . LYS A 1 182 ? 110.320 131.278 124.157 1.00 21.37  ? 382 LYS A N   1 
ATOM   1242 C  CA  . LYS A 1 182 ? 109.931 132.625 123.758 1.00 21.37  ? 382 LYS A CA  1 
ATOM   1243 C  C   . LYS A 1 182 ? 110.229 132.926 122.295 1.00 21.37  ? 382 LYS A C   1 
ATOM   1244 O  O   . LYS A 1 182 ? 109.748 133.941 121.781 1.00 21.37  ? 382 LYS A O   1 
ATOM   1245 C  CB  . LYS A 1 182 ? 110.628 133.655 124.648 1.00 21.37  ? 382 LYS A CB  1 
ATOM   1246 C  CG  . LYS A 1 182 ? 110.468 133.392 126.136 1.00 21.37  ? 382 LYS A CG  1 
ATOM   1247 C  CD  . LYS A 1 182 ? 109.117 133.864 126.646 1.00 21.37  ? 382 LYS A CD  1 
ATOM   1248 C  CE  . LYS A 1 182 ? 109.260 134.629 127.951 1.00 21.37  ? 382 LYS A CE  1 
ATOM   1249 N  NZ  . LYS A 1 182 ? 108.127 134.357 128.878 1.00 21.37  ? 382 LYS A NZ  1 
ATOM   1250 N  N   . GLY A 1 183 ? 111.001 132.081 121.617 1.00 21.06  ? 383 GLY A N   1 
ATOM   1251 C  CA  . GLY A 1 183 ? 111.280 132.281 120.209 1.00 21.06  ? 383 GLY A CA  1 
ATOM   1252 C  C   . GLY A 1 183 ? 110.216 131.672 119.323 1.00 21.06  ? 383 GLY A C   1 
ATOM   1253 O  O   . GLY A 1 183 ? 109.704 132.326 118.408 1.00 21.06  ? 383 GLY A O   1 
ATOM   1254 N  N   . GLU A 1 184 ? 109.873 130.415 119.590 1.00 20.27  ? 384 GLU A N   1 
ATOM   1255 C  CA  . GLU A 1 184 ? 108.804 129.705 118.892 1.00 20.27  ? 384 GLU A CA  1 
ATOM   1256 C  C   . GLU A 1 184 ? 107.760 129.333 119.941 1.00 20.27  ? 384 GLU A C   1 
ATOM   1257 O  O   . GLU A 1 184 ? 107.788 128.234 120.499 1.00 20.27  ? 384 GLU A O   1 
ATOM   1258 C  CB  . GLU A 1 184 ? 109.337 128.476 118.160 1.00 20.27  ? 384 GLU A CB  1 
ATOM   1259 C  CG  . GLU A 1 184 ? 110.448 128.777 117.168 1.00 20.27  ? 384 GLU A CG  1 
ATOM   1260 C  CD  . GLU A 1 184 ? 110.500 127.775 116.031 1.00 20.27  ? 384 GLU A CD  1 
ATOM   1261 O  OE1 . GLU A 1 184 ? 109.953 126.664 116.188 1.00 20.27  ? 384 GLU A OE1 1 
ATOM   1262 O  OE2 . GLU A 1 184 ? 111.088 128.100 114.977 1.00 20.27  ? 384 GLU A OE2 1 
ATOM   1263 N  N   . SER A 1 185 ? 106.838 130.256 120.206 1.00 18.52  ? 385 SER A N   1 
ATOM   1264 C  CA  . SER A 1 185 ? 105.838 130.054 121.244 1.00 18.52  ? 385 SER A CA  1 
ATOM   1265 C  C   . SER A 1 185 ? 104.588 129.350 120.738 1.00 18.52  ? 385 SER A C   1 
ATOM   1266 O  O   . SER A 1 185 ? 103.956 128.608 121.498 1.00 18.52  ? 385 SER A O   1 
ATOM   1267 C  CB  . SER A 1 185 ? 105.446 131.395 121.868 1.00 18.52  ? 385 SER A CB  1 
ATOM   1268 O  OG  . SER A 1 185 ? 106.593 132.129 122.262 1.00 18.52  ? 385 SER A OG  1 
ATOM   1269 N  N   . ALA A 1 186 ? 104.217 129.556 119.477 1.00 16.15  ? 386 ALA A N   1 
ATOM   1270 C  CA  . ALA A 1 186 ? 103.005 128.952 118.943 1.00 16.15  ? 386 ALA A CA  1 
ATOM   1271 C  C   . ALA A 1 186 ? 103.125 128.831 117.432 1.00 16.15  ? 386 ALA A C   1 
ATOM   1272 O  O   . ALA A 1 186 ? 103.968 129.473 116.801 1.00 16.15  ? 386 ALA A O   1 
ATOM   1273 C  CB  . ALA A 1 186 ? 101.760 129.761 119.323 1.00 16.15  ? 386 ALA A CB  1 
ATOM   1274 N  N   . TYR A 1 187 ? 102.262 127.994 116.865 1.00 15.69  ? 387 TYR A N   1 
ATOM   1275 C  CA  . TYR A 1 187 ? 102.161 127.800 115.426 1.00 15.69  ? 387 TYR A CA  1 
ATOM   1276 C  C   . TYR A 1 187 ? 100.769 128.202 114.964 1.00 15.69  ? 387 TYR A C   1 
ATOM   1277 O  O   . TYR A 1 187 ? 99.788  128.041 115.697 1.00 15.69  ? 387 TYR A O   1 
ATOM   1278 C  CB  . TYR A 1 187 ? 102.448 126.347 115.039 1.00 15.69  ? 387 TYR A CB  1 
ATOM   1279 C  CG  . TYR A 1 187 ? 103.845 125.887 115.392 1.00 15.69  ? 387 TYR A CG  1 
ATOM   1280 C  CD1 . TYR A 1 187 ? 104.960 126.493 114.828 1.00 15.69  ? 387 TYR A CD1 1 
ATOM   1281 C  CD2 . TYR A 1 187 ? 104.048 124.848 116.291 1.00 15.69  ? 387 TYR A CD2 1 
ATOM   1282 C  CE1 . TYR A 1 187 ? 106.238 126.077 115.147 1.00 15.69  ? 387 TYR A CE1 1 
ATOM   1283 C  CE2 . TYR A 1 187 ? 105.323 124.425 116.617 1.00 15.69  ? 387 TYR A CE2 1 
ATOM   1284 C  CZ  . TYR A 1 187 ? 106.413 125.043 116.043 1.00 15.69  ? 387 TYR A CZ  1 
ATOM   1285 N  N   . ILE A 1 188 ? 100.685 128.734 113.746 1.00 13.82  ? 388 ILE A N   1 
ATOM   1286 C  CA  . ILE A 1 188 ? 99.443  129.272 113.205 1.00 13.82  ? 388 ILE A CA  1 
ATOM   1287 C  C   . ILE A 1 188 ? 99.073  128.509 111.941 1.00 13.82  ? 388 ILE A C   1 
ATOM   1288 O  O   . ILE A 1 188 ? 99.935  128.205 111.108 1.00 13.82  ? 388 ILE A O   1 
ATOM   1289 C  CB  . ILE A 1 188 ? 99.553  130.783 112.920 1.00 13.82  ? 388 ILE A CB  1 
ATOM   1290 C  CG1 . ILE A 1 188 ? 100.840 131.097 112.153 1.00 13.82  ? 388 ILE A CG1 1 
ATOM   1291 C  CG2 . ILE A 1 188 ? 99.496  131.575 114.217 1.00 13.82  ? 388 ILE A CG2 1 
ATOM   1292 C  CD1 . ILE A 1 188 ? 100.850 132.469 111.519 1.00 13.82  ? 388 ILE A CD1 1 
ATOM   1293 N  N   . ASN A 1 189 ? 97.788  128.194 111.808 1.00 13.44  ? 389 ASN A N   1 
ATOM   1294 C  CA  . ASN A 1 189 ? 97.237  127.534 110.631 1.00 13.44  ? 389 ASN A CA  1 
ATOM   1295 C  C   . ASN A 1 189 ? 96.104  128.396 110.093 1.00 13.44  ? 389 ASN A C   1 
ATOM   1296 O  O   . ASN A 1 189 ? 95.212  128.794 110.849 1.00 13.44  ? 389 ASN A O   1 
ATOM   1297 C  CB  . ASN A 1 189 ? 96.738  126.128 110.976 1.00 13.44  ? 389 ASN A CB  1 
ATOM   1298 C  CG  . ASN A 1 189 ? 96.151  125.401 109.779 1.00 13.44  ? 389 ASN A CG  1 
ATOM   1299 O  OD1 . ASN A 1 189 ? 96.273  125.847 108.639 1.00 13.44  ? 389 ASN A OD1 1 
ATOM   1300 N  ND2 . ASN A 1 189 ? 95.505  124.270 110.039 1.00 13.44  ? 389 ASN A ND2 1 
ATOM   1301 N  N   . ALA A 1 190 ? 96.139  128.685 108.795 1.00 13.09  ? 390 ALA A N   1 
ATOM   1302 C  CA  . ALA A 1 190 ? 95.153  129.548 108.158 1.00 13.09  ? 390 ALA A CA  1 
ATOM   1303 C  C   . ALA A 1 190 ? 94.298  128.740 107.191 1.00 13.09  ? 390 ALA A C   1 
ATOM   1304 O  O   . ALA A 1 190 ? 94.827  128.048 106.319 1.00 13.09  ? 390 ALA A O   1 
ATOM   1305 C  CB  . ALA A 1 190 ? 95.835  130.704 107.422 1.00 13.09  ? 390 ALA A CB  1 
ATOM   1306 N  N   . ASN A 1 191 ? 92.982  128.833 107.346 1.00 13.70  ? 391 ASN A N   1 
ATOM   1307 C  CA  . ASN A 1 191 ? 92.040  128.208 106.428 1.00 13.70  ? 391 ASN A CA  1 
ATOM   1308 C  C   . ASN A 1 191 ? 91.700  129.212 105.335 1.00 13.70  ? 391 ASN A C   1 
ATOM   1309 O  O   . ASN A 1 191 ? 91.089  130.250 105.609 1.00 13.70  ? 391 ASN A O   1 
ATOM   1310 C  CB  . ASN A 1 191 ? 90.780  127.749 107.162 1.00 13.70  ? 391 ASN A CB  1 
ATOM   1311 C  CG  . ASN A 1 191 ? 91.040  126.570 108.079 1.00 13.70  ? 391 ASN A CG  1 
ATOM   1312 O  OD1 . ASN A 1 191 ? 92.155  126.057 108.149 1.00 13.70  ? 391 ASN A OD1 1 
ATOM   1313 N  ND2 . ASN A 1 191 ? 90.006  126.134 108.789 1.00 13.70  ? 391 ASN A ND2 1 
ATOM   1314 N  N   . VAL A 1 192 ? 92.097  128.902 104.101 1.00 12.64  ? 392 VAL A N   1 
ATOM   1315 C  CA  . VAL A 1 192 ? 92.001  129.842 102.994 1.00 12.64  ? 392 VAL A CA  1 
ATOM   1316 C  C   . VAL A 1 192 ? 91.296  129.186 101.816 1.00 12.64  ? 392 VAL A C   1 
ATOM   1317 O  O   . VAL A 1 192 ? 91.205  127.960 101.711 1.00 12.64  ? 392 VAL A O   1 
ATOM   1318 C  CB  . VAL A 1 192 ? 93.386  130.371 102.556 1.00 12.64  ? 392 VAL A CB  1 
ATOM   1319 C  CG1 . VAL A 1 192 ? 94.073  131.091 103.707 1.00 12.64  ? 392 VAL A CG1 1 
ATOM   1320 C  CG2 . VAL A 1 192 ? 94.249  129.234 102.038 1.00 12.64  ? 392 VAL A CG2 1 
ATOM   1321 N  N   . ARG A 1 193 ? 90.787  130.036 100.925 1.00 12.30  ? 393 ARG A N   1 
ATOM   1322 C  CA  . ARG A 1 193 ? 90.136  129.616 99.694  1.00 12.30  ? 393 ARG A CA  1 
ATOM   1323 C  C   . ARG A 1 193 ? 90.576  130.541 98.570  1.00 12.30  ? 393 ARG A C   1 
ATOM   1324 O  O   . ARG A 1 193 ? 90.842  131.724 98.799  1.00 12.30  ? 393 ARG A O   1 
ATOM   1325 C  CB  . ARG A 1 193 ? 88.608  129.643 99.831  1.00 12.30  ? 393 ARG A CB  1 
ATOM   1326 C  CG  . ARG A 1 193 ? 87.875  128.751 98.844  1.00 12.30  ? 393 ARG A CG  1 
ATOM   1327 C  CD  . ARG A 1 193 ? 86.369  128.922 98.959  1.00 12.30  ? 393 ARG A CD  1 
ATOM   1328 N  NE  . ARG A 1 193 ? 85.874  128.527 100.273 1.00 12.30  ? 393 ARG A NE  1 
ATOM   1329 C  CZ  . ARG A 1 193 ? 85.448  127.309 100.578 1.00 12.30  ? 393 ARG A CZ  1 
ATOM   1330 N  N   . TYR A 1 194 ? 90.650  130.001 97.358  1.00 12.26  ? 394 TYR A N   1 
ATOM   1331 C  CA  . TYR A 1 194 ? 91.041  130.771 96.186  1.00 12.26  ? 394 TYR A CA  1 
ATOM   1332 C  C   . TYR A 1 194 ? 89.809  131.164 95.381  1.00 12.26  ? 394 TYR A C   1 
ATOM   1333 O  O   . TYR A 1 194 ? 88.779  130.486 95.414  1.00 12.26  ? 394 TYR A O   1 
ATOM   1334 C  CB  . TYR A 1 194 ? 92.011  129.981 95.302  1.00 12.26  ? 394 TYR A CB  1 
ATOM   1335 C  CG  . TYR A 1 194 ? 93.227  129.445 96.026  1.00 12.26  ? 394 TYR A CG  1 
ATOM   1336 C  CD1 . TYR A 1 194 ? 93.736  130.089 97.147  1.00 12.26  ? 394 TYR A CD1 1 
ATOM   1337 C  CD2 . TYR A 1 194 ? 93.868  128.295 95.584  1.00 12.26  ? 394 TYR A CD2 1 
ATOM   1338 C  CE1 . TYR A 1 194 ? 94.847  129.600 97.808  1.00 12.26  ? 394 TYR A CE1 1 
ATOM   1339 C  CE2 . TYR A 1 194 ? 94.980  127.801 96.239  1.00 12.26  ? 394 TYR A CE2 1 
ATOM   1340 C  CZ  . TYR A 1 194 ? 95.464  128.456 97.350  1.00 12.26  ? 394 TYR A CZ  1 
ATOM   1341 N  N   . TYR A 1 195 ? 89.922  132.277 94.659  1.00 12.66  ? 395 TYR A N   1 
ATOM   1342 C  CA  . TYR A 1 195 ? 88.829  132.810 93.859  1.00 12.66  ? 395 TYR A CA  1 
ATOM   1343 C  C   . TYR A 1 195 ? 89.343  133.179 92.475  1.00 12.66  ? 395 TYR A C   1 
ATOM   1344 O  O   . TYR A 1 195 ? 90.532  133.447 92.290  1.00 12.66  ? 395 TYR A O   1 
ATOM   1345 C  CB  . TYR A 1 195 ? 88.190  134.042 94.522  1.00 12.66  ? 395 TYR A CB  1 
ATOM   1346 C  CG  . TYR A 1 195 ? 87.576  133.767 95.877  1.00 12.66  ? 395 TYR A CG  1 
ATOM   1347 C  CD1 . TYR A 1 195 ? 88.358  133.728 97.024  1.00 12.66  ? 395 TYR A CD1 1 
ATOM   1348 C  CD2 . TYR A 1 195 ? 86.211  133.552 96.010  1.00 12.66  ? 395 TYR A CD2 1 
ATOM   1349 C  CE1 . TYR A 1 195 ? 87.801  133.478 98.263  1.00 12.66  ? 395 TYR A CE1 1 
ATOM   1350 C  CE2 . TYR A 1 195 ? 85.644  133.300 97.245  1.00 12.66  ? 395 TYR A CE2 1 
ATOM   1351 C  CZ  . TYR A 1 195 ? 86.442  133.265 98.367  1.00 12.66  ? 395 TYR A CZ  1 
ATOM   1352 N  N   . ASN A 1 196 ? 88.436  133.181 91.501  1.00 14.17  ? 396 ASN A N   1 
ATOM   1353 C  CA  . ASN A 1 196 ? 88.766  133.543 90.125  1.00 14.17  ? 396 ASN A CA  1 
ATOM   1354 C  C   . ASN A 1 196 ? 87.651  134.428 89.587  1.00 14.17  ? 396 ASN A C   1 
ATOM   1355 O  O   . ASN A 1 196 ? 86.518  133.969 89.421  1.00 14.17  ? 396 ASN A O   1 
ATOM   1356 C  CB  . ASN A 1 196 ? 88.951  132.302 89.251  1.00 14.17  ? 396 ASN A CB  1 
ATOM   1357 C  CG  . ASN A 1 196 ? 89.682  132.601 87.955  1.00 14.17  ? 396 ASN A CG  1 
ATOM   1358 O  OD1 . ASN A 1 196 ? 89.694  133.736 87.480  1.00 14.17  ? 396 ASN A OD1 1 
ATOM   1359 N  ND2 . ASN A 1 196 ? 90.298  131.578 87.376  1.00 14.17  ? 396 ASN A ND2 1 
ATOM   1360 N  N   . THR A 1 197 ? 87.972  135.693 89.314  1.00 17.95  ? 397 THR A N   1 
ATOM   1361 C  CA  . THR A 1 197 ? 87.008  136.654 88.791  1.00 17.95  ? 397 THR A CA  1 
ATOM   1362 C  C   . THR A 1 197 ? 87.395  137.169 87.408  1.00 17.95  ? 397 THR A C   1 
ATOM   1363 O  O   . THR A 1 197 ? 86.924  138.233 86.993  1.00 17.95  ? 397 THR A O   1 
ATOM   1364 C  CB  . THR A 1 197 ? 86.842  137.823 89.762  1.00 17.95  ? 397 THR A CB  1 
ATOM   1365 O  OG1 . THR A 1 197 ? 88.106  138.470 89.956  1.00 17.95  ? 397 THR A OG1 1 
ATOM   1366 C  CG2 . THR A 1 197 ? 86.318  137.333 91.103  1.00 17.95  ? 397 THR A CG2 1 
ATOM   1367 N  N   . GLY A 1 198 ? 88.240  136.437 86.687  1.00 17.14  ? 398 GLY A N   1 
ATOM   1368 C  CA  . GLY A 1 198 ? 88.697  136.835 85.375  1.00 17.14  ? 398 GLY A CA  1 
ATOM   1369 C  C   . GLY A 1 198 ? 87.931  136.157 84.257  1.00 17.14  ? 398 GLY A C   1 
ATOM   1370 O  O   . GLY A 1 198 ? 86.798  135.694 84.429  1.00 17.14  ? 398 GLY A O   1 
ATOM   1371 N  N   . THR A 1 199 ? 88.566  136.102 83.084  1.00 18.60  ? 399 THR A N   1 
ATOM   1372 C  CA  . THR A 1 199 ? 87.965  135.500 81.902  1.00 18.60  ? 399 THR A CA  1 
ATOM   1373 C  C   . THR A 1 199 ? 88.574  134.163 81.511  1.00 18.60  ? 399 THR A C   1 
ATOM   1374 O  O   . THR A 1 199 ? 87.976  133.449 80.702  1.00 18.60  ? 399 THR A O   1 
ATOM   1375 C  CB  . THR A 1 199 ? 88.074  136.450 80.700  1.00 18.60  ? 399 THR A CB  1 
ATOM   1376 O  OG1 . THR A 1 199 ? 89.420  136.926 80.583  1.00 18.60  ? 399 THR A OG1 1 
ATOM   1377 C  CG2 . THR A 1 199 ? 87.136  137.628 80.866  1.00 18.60  ? 399 THR A CG2 1 
ATOM   1378 N  N   . ALA A 1 200 ? 89.735  133.809 82.055  1.00 15.88  ? 400 ALA A N   1 
ATOM   1379 C  CA  . ALA A 1 200 ? 90.397  132.578 81.670  1.00 15.88  ? 400 ALA A CA  1 
ATOM   1380 C  C   . ALA A 1 200 ? 90.698  131.723 82.896  1.00 15.88  ? 400 ALA A C   1 
ATOM   1381 O  O   . ALA A 1 200 ? 90.934  132.254 83.985  1.00 15.88  ? 400 ALA A O   1 
ATOM   1382 C  CB  . ALA A 1 200 ? 91.702  132.865 80.917  1.00 15.88  ? 400 ALA A CB  1 
ATOM   1383 N  N   . PRO A 1 201 ? 90.688  130.401 82.752  1.00 14.82  ? 401 PRO A N   1 
ATOM   1384 C  CA  . PRO A 1 201 ? 91.051  129.536 83.877  1.00 14.82  ? 401 PRO A CA  1 
ATOM   1385 C  C   . PRO A 1 201 ? 92.547  129.574 84.147  1.00 14.82  ? 401 PRO A C   1 
ATOM   1386 O  O   . PRO A 1 201 ? 93.357  129.938 83.292  1.00 14.82  ? 401 PRO A O   1 
ATOM   1387 C  CB  . PRO A 1 201 ? 90.607  128.146 83.412  1.00 14.82  ? 401 PRO A CB  1 
ATOM   1388 C  CG  . PRO A 1 201 ? 90.682  128.220 81.927  1.00 14.82  ? 401 PRO A CG  1 
ATOM   1389 C  CD  . PRO A 1 201 ? 90.288  129.626 81.565  1.00 14.82  ? 401 PRO A CD  1 
ATOM   1390 N  N   . MET A 1 202 ? 92.906  129.189 85.367  1.00 13.46  ? 402 MET A N   1 
ATOM   1391 C  CA  . MET A 1 202 ? 94.297  129.105 85.786  1.00 13.46  ? 402 MET A CA  1 
ATOM   1392 C  C   . MET A 1 202 ? 94.612  127.681 86.219  1.00 13.46  ? 402 MET A C   1 
ATOM   1393 O  O   . MET A 1 202 ? 93.826  127.047 86.930  1.00 13.46  ? 402 MET A O   1 
ATOM   1394 C  CB  . MET A 1 202 ? 94.594  130.079 86.930  1.00 13.46  ? 402 MET A CB  1 
ATOM   1395 C  CG  . MET A 1 202 ? 96.038  130.550 86.972  1.00 13.46  ? 402 MET A CG  1 
ATOM   1396 S  SD  . MET A 1 202 ? 96.463  131.389 88.509  1.00 13.46  ? 402 MET A SD  1 
ATOM   1397 C  CE  . MET A 1 202 ? 97.226  132.879 87.875  1.00 13.46  ? 402 MET A CE  1 
ATOM   1398 N  N   . TYR A 1 203 ? 95.766  127.184 85.786  1.00 14.22  ? 403 TYR A N   1 
ATOM   1399 C  CA  . TYR A 1 203 ? 96.223  125.842 86.110  1.00 14.22  ? 403 TYR A CA  1 
ATOM   1400 C  C   . TYR A 1 203 ? 97.452  125.927 87.004  1.00 14.22  ? 403 TYR A C   1 
ATOM   1401 O  O   . TYR A 1 203 ? 98.331  126.764 86.784  1.00 14.22  ? 403 TYR A O   1 
ATOM   1402 C  CB  . TYR A 1 203 ? 96.548  125.049 84.841  1.00 14.22  ? 403 TYR A CB  1 
ATOM   1403 C  CG  . TYR A 1 203 ? 95.390  124.940 83.874  1.00 14.22  ? 403 TYR A CG  1 
ATOM   1404 C  CD1 . TYR A 1 203 ? 95.175  125.913 82.905  1.00 14.22  ? 403 TYR A CD1 1 
ATOM   1405 C  CD2 . TYR A 1 203 ? 94.508  123.869 83.932  1.00 14.22  ? 403 TYR A CD2 1 
ATOM   1406 C  CE1 . TYR A 1 203 ? 94.118  125.819 82.021  1.00 14.22  ? 403 TYR A CE1 1 
ATOM   1407 C  CE2 . TYR A 1 203 ? 93.449  123.767 83.052  1.00 14.22  ? 403 TYR A CE2 1 
ATOM   1408 C  CZ  . TYR A 1 203 ? 93.258  124.744 82.098  1.00 14.22  ? 403 TYR A CZ  1 
ATOM   1409 N  N   . LYS A 1 204 ? 97.499  125.058 88.015  1.00 12.12  ? 404 LYS A N   1 
ATOM   1410 C  CA  . LYS A 1 204 ? 98.579  125.040 89.004  1.00 12.12  ? 404 LYS A CA  1 
ATOM   1411 C  C   . LYS A 1 204 ? 98.685  126.393 89.712  1.00 12.12  ? 404 LYS A C   1 
ATOM   1412 O  O   . LYS A 1 204 ? 99.692  127.098 89.629  1.00 12.12  ? 404 LYS A O   1 
ATOM   1413 C  CB  . LYS A 1 204 ? 99.909  124.642 88.357  1.00 12.12  ? 404 LYS A CB  1 
ATOM   1414 C  CG  . LYS A 1 204 ? 100.708 123.621 89.149  1.00 12.12  ? 404 LYS A CG  1 
ATOM   1415 C  CD  . LYS A 1 204 ? 102.160 123.594 88.702  1.00 12.12  ? 404 LYS A CD  1 
ATOM   1416 C  CE  . LYS A 1 204 ? 103.070 123.088 89.808  1.00 12.12  ? 404 LYS A CE  1 
ATOM   1417 N  NZ  . LYS A 1 204 ? 104.333 122.514 89.268  1.00 12.12  ? 404 LYS A NZ  1 
ATOM   1418 N  N   . VAL A 1 205 ? 97.610  126.742 90.419  1.00 11.46  ? 405 VAL A N   1 
ATOM   1419 C  CA  . VAL A 1 205 ? 97.531  128.033 91.095  1.00 11.46  ? 405 VAL A CA  1 
ATOM   1420 C  C   . VAL A 1 205 ? 98.463  128.023 92.299  1.00 11.46  ? 405 VAL A C   1 
ATOM   1421 O  O   . VAL A 1 205 ? 98.347  127.171 93.188  1.00 11.46  ? 405 VAL A O   1 
ATOM   1422 C  CB  . VAL A 1 205 ? 96.088  128.344 91.510  1.00 11.46  ? 405 VAL A CB  1 
ATOM   1423 C  CG1 . VAL A 1 205 ? 95.999  129.727 92.132  1.00 11.46  ? 405 VAL A CG1 1 
ATOM   1424 C  CG2 . VAL A 1 205 ? 95.156  128.230 90.313  1.00 11.46  ? 405 VAL A CG2 1 
ATOM   1425 N  N   . THR A 1 206 ? 99.395  128.977 92.335  1.00 11.30  ? 406 THR A N   1 
ATOM   1426 C  CA  . THR A 1 206 ? 100.398 129.071 93.393  1.00 11.30  ? 406 THR A CA  1 
ATOM   1427 C  C   . THR A 1 206 ? 100.439 130.500 93.921  1.00 11.30  ? 406 THR A C   1 
ATOM   1428 O  O   . THR A 1 206 ? 101.296 131.300 93.520  1.00 11.30  ? 406 THR A O   1 
ATOM   1429 C  CB  . THR A 1 206 ? 101.773 128.639 92.887  1.00 11.30  ? 406 THR A CB  1 
ATOM   1430 O  OG1 . THR A 1 206 ? 101.646 127.426 92.134  1.00 11.30  ? 406 THR A OG1 1 
ATOM   1431 C  CG2 . THR A 1 206 ? 102.720 128.406 94.051  1.00 11.30  ? 406 THR A CG2 1 
ATOM   1432 N  N   . PRO A 1 207 ? 99.526  130.860 94.818  1.00 10.68  ? 407 PRO A N   1 
ATOM   1433 C  CA  . PRO A 1 207 ? 99.522  132.217 95.370  1.00 10.68  ? 407 PRO A CA  1 
ATOM   1434 C  C   . PRO A 1 207 ? 100.589 132.405 96.439  1.00 10.68  ? 407 PRO A C   1 
ATOM   1435 O  O   . PRO A 1 207 ? 101.073 131.457 97.058  1.00 10.68  ? 407 PRO A O   1 
ATOM   1436 C  CB  . PRO A 1 207 ? 98.116  132.358 95.973  1.00 10.68  ? 407 PRO A CB  1 
ATOM   1437 C  CG  . PRO A 1 207 ? 97.368  131.098 95.592  1.00 10.68  ? 407 PRO A CG  1 
ATOM   1438 C  CD  . PRO A 1 207 ? 98.401  130.060 95.322  1.00 10.68  ? 407 PRO A CD  1 
ATOM   1439 N  N   . THR A 1 208 ? 100.951 133.670 96.645  1.00 12.45  ? 408 THR A N   1 
ATOM   1440 C  CA  . THR A 1 208 ? 101.862 134.078 97.707  1.00 12.45  ? 408 THR A CA  1 
ATOM   1441 C  C   . THR A 1 208 ? 101.127 135.033 98.637  1.00 12.45  ? 408 THR A C   1 
ATOM   1442 O  O   . THR A 1 208 ? 100.509 136.000 98.177  1.00 12.45  ? 408 THR A O   1 
ATOM   1443 C  CB  . THR A 1 208 ? 103.120 134.744 97.141  1.00 12.45  ? 408 THR A CB  1 
ATOM   1444 O  OG1 . THR A 1 208 ? 103.675 133.919 96.108  1.00 12.45  ? 408 THR A OG1 1 
ATOM   1445 C  CG2 . THR A 1 208 ? 104.157 134.939 98.236  1.00 12.45  ? 408 THR A CG2 1 
ATOM   1446 N  N   . THR A 1 209 ? 101.196 134.761 99.939  1.00 14.31  ? 409 THR A N   1 
ATOM   1447 C  CA  . THR A 1 209 ? 100.400 135.486 100.919 1.00 14.31  ? 409 THR A CA  1 
ATOM   1448 C  C   . THR A 1 209 ? 101.271 136.018 102.049 1.00 14.31  ? 409 THR A C   1 
ATOM   1449 O  O   . THR A 1 209 ? 102.181 135.341 102.533 1.00 14.31  ? 409 THR A O   1 
ATOM   1450 C  CB  . THR A 1 209 ? 99.288  134.603 101.513 1.00 14.31  ? 409 THR A CB  1 
ATOM   1451 O  OG1 . THR A 1 209 ? 99.873  133.517 102.244 1.00 14.31  ? 409 THR A OG1 1 
ATOM   1452 C  CG2 . THR A 1 209 ? 98.393  134.049 100.413 1.00 14.31  ? 409 THR A CG2 1 
ATOM   1453 N  N   . ASN A 1 210 ? 100.961 137.239 102.468 1.00 14.22  ? 410 ASN A N   1 
ATOM   1454 C  CA  . ASN A 1 210 ? 101.539 137.875 103.642 1.00 14.22  ? 410 ASN A CA  1 
ATOM   1455 C  C   . ASN A 1 210 ? 100.580 137.761 104.819 1.00 14.22  ? 410 ASN A C   1 
ATOM   1456 O  O   . ASN A 1 210 ? 99.378  138.010 104.688 1.00 14.22  ? 410 ASN A O   1 
ATOM   1457 C  CB  . ASN A 1 210 ? 101.844 139.352 103.376 1.00 14.22  ? 410 ASN A CB  1 
ATOM   1458 C  CG  . ASN A 1 210 ? 103.197 139.566 102.735 1.00 14.22  ? 410 ASN A CG  1 
ATOM   1459 O  OD1 . ASN A 1 210 ? 104.063 138.695 102.780 1.00 14.22  ? 410 ASN A OD1 1 
ATOM   1460 N  ND2 . ASN A 1 210 ? 103.389 140.736 102.137 1.00 14.22  ? 410 ASN A ND2 1 
ATOM   1461 N  N   . LEU A 1 211 ? 101.127 137.385 105.976 1.00 14.63  ? 411 LEU A N   1 
ATOM   1462 C  CA  . LEU A 1 211 ? 100.379 137.333 107.228 1.00 14.63  ? 411 LEU A CA  1 
ATOM   1463 C  C   . LEU A 1 211 ? 100.828 138.510 108.085 1.00 14.63  ? 411 LEU A C   1 
ATOM   1464 O  O   . LEU A 1 211 ? 101.993 138.578 108.492 1.00 14.63  ? 411 LEU A O   1 
ATOM   1465 C  CB  . LEU A 1 211 ? 100.603 136.004 107.948 1.00 14.63  ? 411 LEU A CB  1 
ATOM   1466 C  CG  . LEU A 1 211 ? 100.068 134.758 107.238 1.00 14.63  ? 411 LEU A CG  1 
ATOM   1467 C  CD1 . LEU A 1 211 ? 100.518 133.495 107.953 1.00 14.63  ? 411 LEU A CD1 1 
ATOM   1468 C  CD2 . LEU A 1 211 ? 98.551  134.806 107.134 1.00 14.63  ? 411 LEU A CD2 1 
ATOM   1469 N  N   . VAL A 1 212 ? 99.908  139.432 108.361 1.00 16.13  ? 412 VAL A N   1 
ATOM   1470 C  CA  . VAL A 1 212 ? 100.224 140.699 109.014 1.00 16.13  ? 412 VAL A CA  1 
ATOM   1471 C  C   . VAL A 1 212 ? 99.467  140.775 110.332 1.00 16.13  ? 412 VAL A C   1 
ATOM   1472 O  O   . VAL A 1 212 ? 98.260  140.509 110.377 1.00 16.13  ? 412 VAL A O   1 
ATOM   1473 C  CB  . VAL A 1 212 ? 99.877  141.899 108.115 1.00 16.13  ? 412 VAL A CB  1 
ATOM   1474 C  CG1 . VAL A 1 212 ? 100.243 143.205 108.803 1.00 16.13  ? 412 VAL A CG1 1 
ATOM   1475 C  CG2 . VAL A 1 212 ? 100.584 141.779 106.774 1.00 16.13  ? 412 VAL A CG2 1 
ATOM   1476 N  N   . LEU A 1 213 ? 100.178 141.137 111.401 1.00 20.04  ? 413 LEU A N   1 
ATOM   1477 C  CA  . LEU A 1 213 ? 99.578  141.301 112.723 1.00 20.04  ? 413 LEU A CA  1 
ATOM   1478 C  C   . LEU A 1 213 ? 100.099 142.596 113.333 1.00 20.04  ? 413 LEU A C   1 
ATOM   1479 O  O   . LEU A 1 213 ? 101.283 142.693 113.668 1.00 20.04  ? 413 LEU A O   1 
ATOM   1480 C  CB  . LEU A 1 213 ? 99.893  140.110 113.629 1.00 20.04  ? 413 LEU A CB  1 
ATOM   1481 C  CG  . LEU A 1 213 ? 99.518  140.262 115.105 1.00 20.04  ? 413 LEU A CG  1 
ATOM   1482 C  CD1 . LEU A 1 213 ? 98.009  140.229 115.286 1.00 20.04  ? 413 LEU A CD1 1 
ATOM   1483 C  CD2 . LEU A 1 213 ? 100.187 139.183 115.943 1.00 20.04  ? 413 LEU A CD2 1 
ATOM   1484 N  N   . ASP A 1 214 ? 99.210  143.582 113.476 1.00 25.39  ? 414 ASP A N   1 
ATOM   1485 C  CA  . ASP A 1 214 ? 99.516  144.849 114.146 1.00 25.39  ? 414 ASP A CA  1 
ATOM   1486 C  C   . ASP A 1 214 ? 100.710 145.555 113.502 1.00 25.39  ? 414 ASP A C   1 
ATOM   1487 O  O   . ASP A 1 214 ? 101.649 145.983 114.176 1.00 25.39  ? 414 ASP A O   1 
ATOM   1488 C  CB  . ASP A 1 214 ? 99.747  144.634 115.644 1.00 25.39  ? 414 ASP A CB  1 
ATOM   1489 C  CG  . ASP A 1 214 ? 99.581  145.910 116.448 1.00 25.39  ? 414 ASP A CG  1 
ATOM   1490 O  OD1 . ASP A 1 214 ? 98.642  146.678 116.157 1.00 25.39  ? 414 ASP A OD1 1 
ATOM   1491 O  OD2 . ASP A 1 214 ? 100.391 146.144 117.371 1.00 25.39  ? 414 ASP A OD2 1 
ATOM   1492 N  N   . GLY A 1 215 ? 100.668 145.674 112.177 1.00 21.23  ? 415 GLY A N   1 
ATOM   1493 C  CA  . GLY A 1 215 ? 101.685 146.411 111.455 1.00 21.23  ? 415 GLY A CA  1 
ATOM   1494 C  C   . GLY A 1 215 ? 102.971 145.664 111.188 1.00 21.23  ? 415 GLY A C   1 
ATOM   1495 O  O   . GLY A 1 215 ? 103.913 146.262 110.657 1.00 21.23  ? 415 GLY A O   1 
ATOM   1496 N  N   . GLU A 1 216 ? 103.047 144.383 111.536 1.00 19.04  ? 416 GLU A N   1 
ATOM   1497 C  CA  . GLU A 1 216 ? 104.228 143.571 111.282 1.00 19.04  ? 416 GLU A CA  1 
ATOM   1498 C  C   . GLU A 1 216 ? 103.835 142.348 110.468 1.00 19.04  ? 416 GLU A C   1 
ATOM   1499 O  O   . GLU A 1 216 ? 102.820 141.706 110.748 1.00 19.04  ? 416 GLU A O   1 
ATOM   1500 C  CB  . GLU A 1 216 ? 104.904 143.133 112.587 1.00 19.04  ? 416 GLU A CB  1 
ATOM   1501 C  CG  . GLU A 1 216 ? 105.209 144.269 113.548 1.00 19.04  ? 416 GLU A CG  1 
ATOM   1502 C  CD  . GLU A 1 216 ? 105.905 143.793 114.808 1.00 19.04  ? 416 GLU A CD  1 
ATOM   1503 O  OE1 . GLU A 1 216 ? 105.724 142.615 115.181 1.00 19.04  ? 416 GLU A OE1 1 
ATOM   1504 O  OE2 . GLU A 1 216 ? 106.636 144.597 115.425 1.00 19.04  ? 416 GLU A OE2 1 
ATOM   1505 N  N   . THR A 1 217 ? 104.645 142.032 109.461 1.00 15.23  ? 417 THR A N   1 
ATOM   1506 C  CA  . THR A 1 217 ? 104.415 140.868 108.613 1.00 15.23  ? 417 THR A CA  1 
ATOM   1507 C  C   . THR A 1 217 ? 105.024 139.647 109.294 1.00 15.23  ? 417 THR A C   1 
ATOM   1508 O  O   . THR A 1 217 ? 106.248 139.526 109.387 1.00 15.23  ? 417 THR A O   1 
ATOM   1509 C  CB  . THR A 1 217 ? 105.013 141.077 107.225 1.00 15.23  ? 417 THR A CB  1 
ATOM   1510 O  OG1 . THR A 1 217 ? 104.504 142.291 106.659 1.00 15.23  ? 417 THR A OG1 1 
ATOM   1511 C  CG2 . THR A 1 217 ? 104.664 139.912 106.311 1.00 15.23  ? 417 THR A CG2 1 
ATOM   1512 N  N   . LEU A 1 218 ? 104.165 138.746 109.777 1.00 15.40  ? 418 LEU A N   1 
ATOM   1513 C  CA  . LEU A 1 218 ? 104.656 137.547 110.447 1.00 15.40  ? 418 LEU A CA  1 
ATOM   1514 C  C   . LEU A 1 218 ? 105.405 136.641 109.479 1.00 15.40  ? 418 LEU A C   1 
ATOM   1515 O  O   . LEU A 1 218 ? 106.492 136.144 109.800 1.00 15.40  ? 418 LEU A O   1 
ATOM   1516 C  CB  . LEU A 1 218 ? 103.498 136.789 111.093 1.00 15.40  ? 418 LEU A CB  1 
ATOM   1517 C  CG  . LEU A 1 218 ? 102.662 137.529 112.135 1.00 15.40  ? 418 LEU A CG  1 
ATOM   1518 C  CD1 . LEU A 1 218 ? 101.192 137.210 111.940 1.00 15.40  ? 418 LEU A CD1 1 
ATOM   1519 C  CD2 . LEU A 1 218 ? 103.111 137.164 113.538 1.00 15.40  ? 418 LEU A CD2 1 
ATOM   1520 N  N   . ALA A 1 219 ? 104.846 136.416 108.293 1.00 13.63  ? 419 ALA A N   1 
ATOM   1521 C  CA  . ALA A 1 219 ? 105.466 135.514 107.335 1.00 13.63  ? 419 ALA A CA  1 
ATOM   1522 C  C   . ALA A 1 219 ? 104.949 135.815 105.937 1.00 13.63  ? 419 ALA A C   1 
ATOM   1523 O  O   . ALA A 1 219 ? 103.888 136.424 105.756 1.00 13.63  ? 419 ALA A O   1 
ATOM   1524 C  CB  . ALA A 1 219 ? 105.205 134.047 107.697 1.00 13.63  ? 419 ALA A CB  1 
ATOM   1525 N  N   . THR A 1 220 ? 105.729 135.380 104.949 1.00 12.76  ? 420 THR A N   1 
ATOM   1526 C  CA  . THR A 1 220 ? 105.354 135.414 103.540 1.00 12.76  ? 420 THR A CA  1 
ATOM   1527 C  C   . THR A 1 220 ? 105.452 133.987 103.018 1.00 12.76  ? 420 THR A C   1 
ATOM   1528 O  O   . THR A 1 220 ? 106.553 133.436 102.909 1.00 12.76  ? 420 THR A O   1 
ATOM   1529 C  CB  . THR A 1 220 ? 106.256 136.357 102.744 1.00 12.76  ? 420 THR A CB  1 
ATOM   1530 O  OG1 . THR A 1 220 ? 106.171 137.679 103.293 1.00 12.76  ? 420 THR A OG1 1 
ATOM   1531 C  CG2 . THR A 1 220 ? 105.831 136.392 101.285 1.00 12.76  ? 420 THR A CG2 1 
ATOM   1532 N  N   . ILE A 1 221 ? 104.306 133.392 102.698 1.00 12.81  ? 421 ILE A N   1 
ATOM   1533 C  CA  . ILE A 1 221 ? 104.216 131.974 102.370 1.00 12.81  ? 421 ILE A CA  1 
ATOM   1534 C  C   . ILE A 1 221 ? 103.842 131.822 100.904 1.00 12.81  ? 421 ILE A C   1 
ATOM   1535 O  O   . ILE A 1 221 ? 102.877 132.438 100.433 1.00 12.81  ? 421 ILE A O   1 
ATOM   1536 C  CB  . ILE A 1 221 ? 103.199 131.250 103.269 1.00 12.81  ? 421 ILE A CB  1 
ATOM   1537 C  CG1 . ILE A 1 221 ? 103.298 131.760 104.709 1.00 12.81  ? 421 ILE A CG1 1 
ATOM   1538 C  CG2 . ILE A 1 221 ? 103.416 129.746 103.207 1.00 12.81  ? 421 ILE A CG2 1 
ATOM   1539 C  CD1 . ILE A 1 221 ? 104.465 131.187 105.482 1.00 12.81  ? 421 ILE A CD1 1 
ATOM   1540 N  N   . LYS A 1 222 ? 104.607 131.003 100.188 1.00 13.37  ? 422 LYS A N   1 
ATOM   1541 C  CA  . LYS A 1 222 ? 104.280 130.605 98.828  1.00 13.37  ? 422 LYS A CA  1 
ATOM   1542 C  C   . LYS A 1 222 ? 103.677 129.208 98.843  1.00 13.37  ? 422 LYS A C   1 
ATOM   1543 O  O   . LYS A 1 222 ? 104.139 128.329 99.577  1.00 13.37  ? 422 LYS A O   1 
ATOM   1544 C  CB  . LYS A 1 222 ? 105.527 130.637 97.943  1.00 13.37  ? 422 LYS A CB  1 
ATOM   1545 C  CG  . LYS A 1 222 ? 105.295 130.202 96.505  1.00 13.37  ? 422 LYS A CG  1 
ATOM   1546 C  CD  . LYS A 1 222 ? 106.605 129.826 95.831  1.00 13.37  ? 422 LYS A CD  1 
ATOM   1547 C  CE  . LYS A 1 222 ? 106.368 129.094 94.522  1.00 13.37  ? 422 LYS A CE  1 
ATOM   1548 N  NZ  . LYS A 1 222 ? 105.672 129.950 93.524  1.00 13.37  ? 422 LYS A NZ  1 
ATOM   1549 N  N   . ALA A 1 223 ? 102.636 129.011 98.037  1.00 13.99  ? 423 ALA A N   1 
ATOM   1550 C  CA  . ALA A 1 223 ? 101.928 127.736 98.028  1.00 13.99  ? 423 ALA A CA  1 
ATOM   1551 C  C   . ALA A 1 223 ? 102.845 126.608 97.572  1.00 13.99  ? 423 ALA A C   1 
ATOM   1552 O  O   . ALA A 1 223 ? 103.669 126.776 96.669  1.00 13.99  ? 423 ALA A O   1 
ATOM   1553 C  CB  . ALA A 1 223 ? 100.700 127.817 97.123  1.00 13.99  ? 423 ALA A CB  1 
ATOM   1554 N  N   . GLN A 1 224 ? 102.698 125.451 98.208  1.00 14.99  ? 424 GLN A N   1 
ATOM   1555 C  CA  . GLN A 1 224 ? 103.477 124.260 97.907  1.00 14.99  ? 424 GLN A CA  1 
ATOM   1556 C  C   . GLN A 1 224 ? 102.538 123.141 97.457  1.00 14.99  ? 424 GLN A C   1 
ATOM   1557 O  O   . GLN A 1 224 ? 101.351 123.364 97.207  1.00 14.99  ? 424 GLN A O   1 
ATOM   1558 C  CB  . GLN A 1 224 ? 104.325 123.851 99.115  1.00 14.99  ? 424 GLN A CB  1 
ATOM   1559 C  CG  . GLN A 1 224 ? 105.404 124.860 99.483  1.00 14.99  ? 424 GLN A CG  1 
ATOM   1560 C  CD  . GLN A 1 224 ? 106.403 125.090 98.362  1.00 14.99  ? 424 GLN A CD  1 
ATOM   1561 O  OE1 . GLN A 1 224 ? 106.667 124.200 97.554  1.00 14.99  ? 424 GLN A OE1 1 
ATOM   1562 N  NE2 . GLN A 1 224 ? 106.963 126.294 98.308  1.00 14.99  ? 424 GLN A NE2 1 
ATOM   1563 N  N   . ASP A 1 225 ? 103.095 121.930 97.345  1.00 15.86  ? 425 ASP A N   1 
ATOM   1564 C  CA  . ASP A 1 225 ? 102.348 120.792 96.813  1.00 15.86  ? 425 ASP A CA  1 
ATOM   1565 C  C   . ASP A 1 225 ? 101.013 120.601 97.522  1.00 15.86  ? 425 ASP A C   1 
ATOM   1566 O  O   . ASP A 1 225 ? 100.000 120.294 96.883  1.00 15.86  ? 425 ASP A O   1 
ATOM   1567 C  CB  . ASP A 1 225 ? 103.191 119.521 96.925  1.00 15.86  ? 425 ASP A CB  1 
ATOM   1568 C  CG  . ASP A 1 225 ? 103.942 119.204 95.648  1.00 15.86  ? 425 ASP A CG  1 
ATOM   1569 O  OD1 . ASP A 1 225 ? 103.782 119.952 94.661  1.00 15.86  ? 425 ASP A OD1 1 
ATOM   1570 O  OD2 . ASP A 1 225 ? 104.691 118.204 95.631  1.00 15.86  ? 425 ASP A OD2 1 
ATOM   1571 N  N   . ASN A 1 226 ? 100.989 120.775 98.844  1.00 14.54  ? 426 ASN A N   1 
ATOM   1572 C  CA  . ASN A 1 226 ? 99.755  120.584 99.596  1.00 14.54  ? 426 ASN A CA  1 
ATOM   1573 C  C   . ASN A 1 226 ? 98.757  121.716 99.387  1.00 14.54  ? 426 ASN A C   1 
ATOM   1574 O  O   . ASN A 1 226 ? 97.582  121.557 99.735  1.00 14.54  ? 426 ASN A O   1 
ATOM   1575 C  CB  . ASN A 1 226 ? 100.066 120.440 101.087 1.00 14.54  ? 426 ASN A CB  1 
ATOM   1576 C  CG  . ASN A 1 226 ? 100.552 119.052 101.451 1.00 14.54  ? 426 ASN A CG  1 
ATOM   1577 O  OD1 . ASN A 1 226 ? 100.408 118.108 100.675 1.00 14.54  ? 426 ASN A OD1 1 
ATOM   1578 N  ND2 . ASN A 1 226 ? 101.131 118.920 102.638 1.00 14.54  ? 426 ASN A ND2 1 
ATOM   1579 N  N   . GLN A 1 227 ? 99.189  122.849 98.831  1.00 13.52  ? 427 GLN A N   1 
ATOM   1580 C  CA  . GLN A 1 227 ? 98.335  124.026 98.709  1.00 13.52  ? 427 GLN A CA  1 
ATOM   1581 C  C   . GLN A 1 227 ? 98.131  124.478 97.267  1.00 13.52  ? 427 GLN A C   1 
ATOM   1582 O  O   . GLN A 1 227 ? 97.616  125.580 97.045  1.00 13.52  ? 427 GLN A O   1 
ATOM   1583 C  CB  . GLN A 1 227 ? 98.910  125.180 99.536  1.00 13.52  ? 427 GLN A CB  1 
ATOM   1584 C  CG  . GLN A 1 227 ? 98.744  125.010 101.036 1.00 13.52  ? 427 GLN A CG  1 
ATOM   1585 C  CD  . GLN A 1 227 ? 99.909  124.282 101.675 1.00 13.52  ? 427 GLN A CD  1 
ATOM   1586 O  OE1 . GLN A 1 227 ? 101.018 124.275 101.143 1.00 13.52  ? 427 GLN A OE1 1 
ATOM   1587 N  NE2 . GLN A 1 227 ? 99.663  123.661 102.822 1.00 13.52  ? 427 GLN A NE2 1 
ATOM   1588 N  N   . ILE A 1 228 ? 98.512  123.667 96.286  1.00 13.12  ? 428 ILE A N   1 
ATOM   1589 C  CA  . ILE A 1 228 ? 98.395  124.041 94.881  1.00 13.12  ? 428 ILE A CA  1 
ATOM   1590 C  C   . ILE A 1 228 ? 97.074  123.518 94.332  1.00 13.12  ? 428 ILE A C   1 
ATOM   1591 O  O   . ILE A 1 228 ? 96.750  122.334 94.486  1.00 13.12  ? 428 ILE A O   1 
ATOM   1592 C  CB  . ILE A 1 228 ? 99.585  123.504 94.067  1.00 13.12  ? 428 ILE A CB  1 
ATOM   1593 C  CG1 . ILE A 1 228 ? 100.806 124.408 94.249  1.00 13.12  ? 428 ILE A CG1 1 
ATOM   1594 C  CG2 . ILE A 1 228 ? 99.225  123.392 92.593  1.00 13.12  ? 428 ILE A CG2 1 
ATOM   1595 C  CD1 . ILE A 1 228 ? 102.121 123.722 93.955  1.00 13.12  ? 428 ILE A CD1 1 
ATOM   1596 N  N   . GLY A 1 229 ? 96.310  124.401 93.693  1.00 11.63  ? 429 GLY A N   1 
ATOM   1597 C  CA  . GLY A 1 229 ? 95.064  124.014 93.059  1.00 11.63  ? 429 GLY A CA  1 
ATOM   1598 C  C   . GLY A 1 229 ? 95.284  123.668 91.601  1.00 11.63  ? 429 GLY A C   1 
ATOM   1599 O  O   . GLY A 1 229 ? 95.858  124.453 90.844  1.00 11.63  ? 429 GLY A O   1 
ATOM   1600 N  N   . ASN A 1 230 ? 94.824  122.476 91.210  1.00 11.71  ? 430 ASN A N   1 
ATOM   1601 C  CA  . ASN A 1 230 ? 95.044  122.006 89.846  1.00 11.71  ? 430 ASN A CA  1 
ATOM   1602 C  C   . ASN A 1 230 ? 94.265  122.843 88.836  1.00 11.71  ? 430 ASN A C   1 
ATOM   1603 O  O   . ASN A 1 230 ? 94.819  123.285 87.823  1.00 11.71  ? 430 ASN A O   1 
ATOM   1604 C  CB  . ASN A 1 230 ? 94.659  120.531 89.732  1.00 11.71  ? 430 ASN A CB  1 
ATOM   1605 C  CG  . ASN A 1 230 ? 95.558  119.630 90.555  1.00 11.71  ? 430 ASN A CG  1 
ATOM   1606 O  OD1 . ASN A 1 230 ? 96.664  120.014 90.931  1.00 11.71  ? 430 ASN A OD1 1 
ATOM   1607 N  ND2 . ASN A 1 230 ? 95.085  118.422 90.838  1.00 11.71  ? 430 ASN A ND2 1 
ATOM   1608 N  N   . ASN A 1 231 ? 92.980  123.073 89.095  1.00 13.29  ? 431 ASN A N   1 
ATOM   1609 C  CA  . ASN A 1 231 ? 92.115  123.799 88.178  1.00 13.29  ? 431 ASN A CA  1 
ATOM   1610 C  C   . ASN A 1 231 ? 91.383  124.903 88.922  1.00 13.29  ? 431 ASN A C   1 
ATOM   1611 O  O   . ASN A 1 231 ? 90.966  124.722 90.070  1.00 13.29  ? 431 ASN A O   1 
ATOM   1612 C  CB  . ASN A 1 231 ? 91.100  122.863 87.507  1.00 13.29  ? 431 ASN A CB  1 
ATOM   1613 C  CG  . ASN A 1 231 ? 91.762  121.710 86.782  1.00 13.29  ? 431 ASN A CG  1 
ATOM   1614 O  OD1 . ASN A 1 231 ? 92.056  120.674 87.378  1.00 13.29  ? 431 ASN A OD1 1 
ATOM   1615 N  ND2 . ASN A 1 231 ? 91.998  121.882 85.487  1.00 13.29  ? 431 ASN A ND2 1 
ATOM   1616 N  N   . LEU A 1 232 ? 91.227  126.051 88.259  1.00 12.93  ? 432 LEU A N   1 
ATOM   1617 C  CA  . LEU A 1 232 ? 90.477  127.175 88.824  1.00 12.93  ? 432 LEU A CA  1 
ATOM   1618 C  C   . LEU A 1 232 ? 89.801  127.901 87.658  1.00 12.93  ? 432 LEU A C   1 
ATOM   1619 O  O   . LEU A 1 232 ? 90.395  128.777 87.027  1.00 12.93  ? 432 LEU A O   1 
ATOM   1620 C  CB  . LEU A 1 232 ? 91.377  128.107 89.622  1.00 12.93  ? 432 LEU A CB  1 
ATOM   1621 C  CG  . LEU A 1 232 ? 90.676  129.233 90.384  1.00 12.93  ? 432 LEU A CG  1 
ATOM   1622 C  CD1 . LEU A 1 232 ? 89.589  128.678 91.292  1.00 12.93  ? 432 LEU A CD1 1 
ATOM   1623 C  CD2 . LEU A 1 232 ? 91.678  130.051 91.181  1.00 12.93  ? 432 LEU A CD2 1 
ATOM   1624 N  N   . SER A 1 233 ? 88.556  127.523 87.388  1.00 14.28  ? 433 SER A N   1 
ATOM   1625 C  CA  . SER A 1 233 ? 87.782  128.141 86.326  1.00 14.28  ? 433 SER A CA  1 
ATOM   1626 C  C   . SER A 1 233 ? 87.293  129.521 86.753  1.00 14.28  ? 433 SER A C   1 
ATOM   1627 O  O   . SER A 1 233 ? 87.170  129.805 87.947  1.00 14.28  ? 433 SER A O   1 
ATOM   1628 C  CB  . SER A 1 233 ? 86.598  127.252 85.957  1.00 14.28  ? 433 SER A CB  1 
ATOM   1629 O  OG  . SER A 1 233 ? 86.974  126.268 85.010  1.00 14.28  ? 433 SER A OG  1 
ATOM   1630 N  N   . PRO A 1 234 ? 87.019  130.405 85.793  1.00 15.49  ? 434 PRO A N   1 
ATOM   1631 C  CA  . PRO A 1 234 ? 86.456  131.715 86.144  1.00 15.49  ? 434 PRO A CA  1 
ATOM   1632 C  C   . PRO A 1 234 ? 85.118  131.565 86.854  1.00 15.49  ? 434 PRO A C   1 
ATOM   1633 O  O   . PRO A 1 234 ? 84.339  130.655 86.565  1.00 15.49  ? 434 PRO A O   1 
ATOM   1634 C  CB  . PRO A 1 234 ? 86.301  132.419 84.789  1.00 15.49  ? 434 PRO A CB  1 
ATOM   1635 C  CG  . PRO A 1 234 ? 86.518  131.368 83.746  1.00 15.49  ? 434 PRO A CG  1 
ATOM   1636 C  CD  . PRO A 1 234 ? 87.358  130.305 84.364  1.00 15.49  ? 434 PRO A CD  1 
ATOM   1637 N  N   . ASN A 1 235 ? 84.868  132.469 87.802  1.00 16.90  ? 435 ASN A N   1 
ATOM   1638 C  CA  . ASN A 1 235 ? 83.671  132.477 88.639  1.00 16.90  ? 435 ASN A CA  1 
ATOM   1639 C  C   . ASN A 1 235 ? 83.550  131.225 89.500  1.00 16.90  ? 435 ASN A C   1 
ATOM   1640 O  O   . ASN A 1 235 ? 82.440  130.840 89.880  1.00 16.90  ? 435 ASN A O   1 
ATOM   1641 C  CB  . ASN A 1 235 ? 82.399  132.661 87.801  1.00 16.90  ? 435 ASN A CB  1 
ATOM   1642 C  CG  . ASN A 1 235 ? 82.389  133.970 87.039  1.00 16.90  ? 435 ASN A CG  1 
ATOM   1643 O  OD1 . ASN A 1 235 ? 82.807  135.007 87.555  1.00 16.90  ? 435 ASN A OD1 1 
ATOM   1644 N  ND2 . ASN A 1 235 ? 81.912  133.931 85.801  1.00 16.90  ? 435 ASN A ND2 1 
ATOM   1645 N  N   . GLU A 1 236 ? 84.669  130.580 89.819  1.00 15.60  ? 436 GLU A N   1 
ATOM   1646 C  CA  . GLU A 1 236 ? 84.690  129.398 90.663  1.00 15.60  ? 436 GLU A CA  1 
ATOM   1647 C  C   . GLU A 1 236 ? 85.746  129.569 91.747  1.00 15.60  ? 436 GLU A C   1 
ATOM   1648 O  O   . GLU A 1 236 ? 86.528  130.524 91.739  1.00 15.60  ? 436 GLU A O   1 
ATOM   1649 C  CB  . GLU A 1 236 ? 84.961  128.125 89.847  1.00 15.60  ? 436 GLU A CB  1 
ATOM   1650 C  CG  . GLU A 1 236 ? 83.880  127.801 88.829  1.00 15.60  ? 436 GLU A CG  1 
ATOM   1651 C  CD  . GLU A 1 236 ? 84.028  126.409 88.249  1.00 15.60  ? 436 GLU A CD  1 
ATOM   1652 O  OE1 . GLU A 1 236 ? 84.787  125.601 88.825  1.00 15.60  ? 436 GLU A OE1 1 
ATOM   1653 O  OE2 . GLU A 1 236 ? 83.387  126.123 87.217  1.00 15.60  ? 436 GLU A OE2 1 
ATOM   1654 N  N   . THR A 1 237 ? 85.761  128.630 92.689  1.00 13.40  ? 437 THR A N   1 
ATOM   1655 C  CA  . THR A 1 237 ? 86.654  128.687 93.837  1.00 13.40  ? 437 THR A CA  1 
ATOM   1656 C  C   . THR A 1 237 ? 87.363  127.353 94.016  1.00 13.40  ? 437 THR A C   1 
ATOM   1657 O  O   . THR A 1 237 ? 86.867  126.299 93.609  1.00 13.40  ? 437 THR A O   1 
ATOM   1658 C  CB  . THR A 1 237 ? 85.899  129.038 95.129  1.00 13.40  ? 437 THR A CB  1 
ATOM   1659 O  OG1 . THR A 1 237 ? 84.961  127.999 95.435  1.00 13.40  ? 437 THR A OG1 1 
ATOM   1660 C  CG2 . THR A 1 237 ? 85.155  130.357 94.984  1.00 13.40  ? 437 THR A CG2 1 
ATOM   1661 N  N   . TYR A 1 238 ? 88.542  127.411 94.633  1.00 12.75  ? 438 TYR A N   1 
ATOM   1662 C  CA  . TYR A 1 238 ? 89.260  126.216 95.069  1.00 12.75  ? 438 TYR A CA  1 
ATOM   1663 C  C   . TYR A 1 238 ? 89.533  126.352 96.561  1.00 12.75  ? 438 TYR A C   1 
ATOM   1664 O  O   . TYR A 1 238 ? 90.244  127.291 96.974  1.00 12.75  ? 438 TYR A O   1 
ATOM   1665 C  CB  . TYR A 1 238 ? 90.568  126.007 94.303  1.00 12.75  ? 438 TYR A CB  1 
ATOM   1666 C  CG  . TYR A 1 238 ? 91.367  124.843 94.842  1.00 12.75  ? 438 TYR A CG  1 
ATOM   1667 C  CD1 . TYR A 1 238 ? 90.943  123.534 94.644  1.00 12.75  ? 438 TYR A CD1 1 
ATOM   1668 C  CD2 . TYR A 1 238 ? 92.527  125.051 95.575  1.00 12.75  ? 438 TYR A CD2 1 
ATOM   1669 C  CE1 . TYR A 1 238 ? 91.662  122.466 95.144  1.00 12.75  ? 438 TYR A CE1 1 
ATOM   1670 C  CE2 . TYR A 1 238 ? 93.253  123.988 96.081  1.00 12.75  ? 438 TYR A CE2 1 
ATOM   1671 C  CZ  . TYR A 1 238 ? 92.816  122.698 95.862  1.00 12.75  ? 438 TYR A CZ  1 
ATOM   1672 N  N   . PRO A 1 239 ? 89.002  125.456 97.409  1.00 13.12  ? 439 PRO A N   1 
ATOM   1673 C  CA  . PRO A 1 239 ? 88.116  124.347 97.038  1.00 13.12  ? 439 PRO A CA  1 
ATOM   1674 C  C   . PRO A 1 239 ? 86.728  124.824 96.615  1.00 13.12  ? 439 PRO A C   1 
ATOM   1675 O  O   . PRO A 1 239 ? 86.406  125.998 96.792  1.00 13.12  ? 439 PRO A O   1 
ATOM   1676 C  CB  . PRO A 1 239 ? 88.038  123.515 98.322  1.00 13.12  ? 439 PRO A CB  1 
ATOM   1677 C  CG  . PRO A 1 239 ? 89.255  123.903 99.101  1.00 13.12  ? 439 PRO A CG  1 
ATOM   1678 C  CD  . PRO A 1 239 ? 89.429  125.358 98.813  1.00 13.12  ? 439 PRO A CD  1 
ATOM   1679 N  N   . LYS A 1 240 ? 85.925  123.918 96.060  1.00 17.52  ? 440 LYS A N   1 
ATOM   1680 C  CA  . LYS A 1 240 ? 84.646  124.290 95.477  1.00 17.52  ? 440 LYS A CA  1 
ATOM   1681 C  C   . LYS A 1 240 ? 83.677  124.767 96.561  1.00 17.52  ? 440 LYS A C   1 
ATOM   1682 O  O   . LYS A 1 240 ? 83.991  124.800 97.754  1.00 17.52  ? 440 LYS A O   1 
ATOM   1683 C  CB  . LYS A 1 240 ? 84.067  123.119 94.689  1.00 17.52  ? 440 LYS A CB  1 
ATOM   1684 C  CG  . LYS A 1 240 ? 85.011  122.570 93.632  1.00 17.52  ? 440 LYS A CG  1 
ATOM   1685 C  CD  . LYS A 1 240 ? 84.691  123.130 92.256  1.00 17.52  ? 440 LYS A CD  1 
ATOM   1686 C  CE  . LYS A 1 240 ? 85.272  122.258 91.154  1.00 17.52  ? 440 LYS A CE  1 
ATOM   1687 N  NZ  . LYS A 1 240 ? 84.408  122.245 89.941  1.00 17.52  ? 440 LYS A NZ  1 
ATOM   1688 N  N   . LYS A 1 241 ? 82.474  125.144 96.121  1.00 20.32  ? 441 LYS A N   1 
ATOM   1689 C  CA  . LYS A 1 241 ? 81.524  125.816 97.004  1.00 20.32  ? 441 LYS A CA  1 
ATOM   1690 C  C   . LYS A 1 241 ? 81.130  124.938 98.186  1.00 20.32  ? 441 LYS A C   1 
ATOM   1691 O  O   . LYS A 1 241 ? 81.018  125.425 99.318  1.00 20.32  ? 441 LYS A O   1 
ATOM   1692 C  CB  . LYS A 1 241 ? 80.286  126.232 96.208  1.00 20.32  ? 441 LYS A CB  1 
ATOM   1693 C  CG  . LYS A 1 241 ? 79.445  127.304 96.874  1.00 20.32  ? 441 LYS A CG  1 
ATOM   1694 C  CD  . LYS A 1 241 ? 77.978  127.160 96.499  1.00 20.32  ? 441 LYS A CD  1 
ATOM   1695 C  CE  . LYS A 1 241 ? 77.189  128.405 96.867  1.00 20.32  ? 441 LYS A CE  1 
ATOM   1696 N  NZ  . LYS A 1 241 ? 76.952  129.279 95.684  1.00 20.32  ? 441 LYS A NZ  1 
ATOM   1697 N  N   . GLY A 1 242 ? 80.920  123.647 97.950  1.00 18.06  ? 442 GLY A N   1 
ATOM   1698 C  CA  . GLY A 1 242 ? 80.483  122.745 98.992  1.00 18.06  ? 442 GLY A CA  1 
ATOM   1699 C  C   . GLY A 1 242 ? 81.569  122.148 99.855  1.00 18.06  ? 442 GLY A C   1 
ATOM   1700 O  O   . GLY A 1 242 ? 81.270  121.304 100.706 1.00 18.06  ? 442 GLY A O   1 
ATOM   1701 N  N   . LEU A 1 243 ? 82.823  122.551 99.672  1.00 15.95  ? 443 LEU A N   1 
ATOM   1702 C  CA  . LEU A 1 243 ? 83.946  121.982 100.402 1.00 15.95  ? 443 LEU A CA  1 
ATOM   1703 C  C   . LEU A 1 243 ? 84.498  122.986 101.408 1.00 15.95  ? 443 LEU A C   1 
ATOM   1704 O  O   . LEU A 1 243 ? 84.229  124.188 101.345 1.00 15.95  ? 443 LEU A O   1 
ATOM   1705 C  CB  . LEU A 1 243 ? 85.049  121.536 99.434  1.00 15.95  ? 443 LEU A CB  1 
ATOM   1706 C  CG  . LEU A 1 243 ? 84.648  120.488 98.395  1.00 15.95  ? 443 LEU A CG  1 
ATOM   1707 C  CD1 . LEU A 1 243 ? 85.740  120.322 97.350  1.00 15.95  ? 443 LEU A CD1 1 
ATOM   1708 C  CD2 . LEU A 1 243 ? 84.334  119.159 99.064  1.00 15.95  ? 443 LEU A CD2 1 
ATOM   1709 N  N   . SER A 1 244 ? 85.281  122.465 102.348 1.00 13.95  ? 444 SER A N   1 
ATOM   1710 C  CA  . SER A 1 244 ? 85.910  123.275 103.377 1.00 13.95  ? 444 SER A CA  1 
ATOM   1711 C  C   . SER A 1 244 ? 87.167  123.955 102.838 1.00 13.95  ? 444 SER A C   1 
ATOM   1712 O  O   . SER A 1 244 ? 87.791  123.466 101.895 1.00 13.95  ? 444 SER A O   1 
ATOM   1713 C  CB  . SER A 1 244 ? 86.256  122.409 104.584 1.00 13.95  ? 444 SER A CB  1 
ATOM   1714 O  OG  . SER A 1 244 ? 85.087  121.878 105.184 1.00 13.95  ? 444 SER A OG  1 
ATOM   1715 N  N   . PRO A 1 245 ? 87.555  125.090 103.418 1.00 13.08  ? 445 PRO A N   1 
ATOM   1716 C  CA  . PRO A 1 245 ? 88.774  125.767 102.963 1.00 13.08  ? 445 PRO A CA  1 
ATOM   1717 C  C   . PRO A 1 245 ? 90.020  124.943 103.248 1.00 13.08  ? 445 PRO A C   1 
ATOM   1718 O  O   . PRO A 1 245 ? 90.073  124.159 104.198 1.00 13.08  ? 445 PRO A O   1 
ATOM   1719 C  CB  . PRO A 1 245 ? 88.777  127.073 103.766 1.00 13.08  ? 445 PRO A CB  1 
ATOM   1720 C  CG  . PRO A 1 245 ? 87.938  126.782 104.964 1.00 13.08  ? 445 PRO A CG  1 
ATOM   1721 C  CD  . PRO A 1 245 ? 86.875  125.842 104.486 1.00 13.08  ? 445 PRO A CD  1 
ATOM   1722 N  N   . LEU A 1 246 ? 91.031  125.131 102.405 1.00 12.11  ? 446 LEU A N   1 
ATOM   1723 C  CA  . LEU A 1 246 ? 92.275  124.391 102.552 1.00 12.11  ? 446 LEU A CA  1 
ATOM   1724 C  C   . LEU A 1 246 ? 93.119  124.979 103.679 1.00 12.11  ? 446 LEU A C   1 
ATOM   1725 O  O   . LEU A 1 246 ? 92.994  126.151 104.044 1.00 12.11  ? 446 LEU A O   1 
ATOM   1726 C  CB  . LEU A 1 246 ? 93.062  124.388 101.240 1.00 12.11  ? 446 LEU A CB  1 
ATOM   1727 C  CG  . LEU A 1 246 ? 93.646  125.713 100.747 1.00 12.11  ? 446 LEU A CG  1 
ATOM   1728 C  CD1 . LEU A 1 246 ? 95.138  125.783 101.031 1.00 12.11  ? 446 LEU A CD1 1 
ATOM   1729 C  CD2 . LEU A 1 246 ? 93.372  125.901 99.264  1.00 12.11  ? 446 LEU A CD2 1 
ATOM   1730 N  N   . ALA A 1 247 ? 93.998  124.145 104.228 1.00 12.67  ? 447 ALA A N   1 
ATOM   1731 C  CA  . ALA A 1 247 ? 94.805  124.505 105.387 1.00 12.67  ? 447 ALA A CA  1 
ATOM   1732 C  C   . ALA A 1 247 ? 96.213  124.878 104.940 1.00 12.67  ? 447 ALA A C   1 
ATOM   1733 O  O   . ALA A 1 247 ? 96.882  124.093 104.258 1.00 12.67  ? 447 ALA A O   1 
ATOM   1734 C  CB  . ALA A 1 247 ? 94.850  123.359 106.396 1.00 12.67  ? 447 ALA A CB  1 
ATOM   1735 N  N   . LEU A 1 248 ? 96.658  126.071 105.327 1.00 12.70  ? 448 LEU A N   1 
ATOM   1736 C  CA  . LEU A 1 248 ? 98.019  126.543 105.107 1.00 12.70  ? 448 LEU A CA  1 
ATOM   1737 C  C   . LEU A 1 248 ? 98.680  126.610 106.479 1.00 12.70  ? 448 LEU A C   1 
ATOM   1738 O  O   . LEU A 1 248 ? 98.332  127.459 107.305 1.00 12.70  ? 448 LEU A O   1 
ATOM   1739 C  CB  . LEU A 1 248 ? 98.020  127.900 104.407 1.00 12.70  ? 448 LEU A CB  1 
ATOM   1740 C  CG  . LEU A 1 248 ? 99.365  128.609 104.249 1.00 12.70  ? 448 LEU A CG  1 
ATOM   1741 C  CD1 . LEU A 1 248 ? 100.293 127.804 103.354 1.00 12.70  ? 448 LEU A CD1 1 
ATOM   1742 C  CD2 . LEU A 1 248 ? 99.168  130.014 103.702 1.00 12.70  ? 448 LEU A CD2 1 
ATOM   1743 N  N   . ASN A 1 249 ? 99.612  125.688 106.729 1.00 13.55  ? 449 ASN A N   1 
ATOM   1744 C  CA  . ASN A 1 249 ? 100.263 125.580 108.028 1.00 13.55  ? 449 ASN A CA  1 
ATOM   1745 C  C   . ASN A 1 249 ? 101.755 125.296 107.920 1.00 13.55  ? 449 ASN A C   1 
ATOM   1746 O  O   . ASN A 1 249 ? 102.392 125.001 108.939 1.00 13.55  ? 449 ASN A O   1 
ATOM   1747 C  CB  . ASN A 1 249 ? 99.587  124.492 108.873 1.00 13.55  ? 449 ASN A CB  1 
ATOM   1748 C  CG  . ASN A 1 249 ? 99.543  123.150 108.168 1.00 13.55  ? 449 ASN A CG  1 
ATOM   1749 O  OD1 . ASN A 1 249 ? 99.651  123.076 106.944 1.00 13.55  ? 449 ASN A OD1 1 
ATOM   1750 N  ND2 . ASN A 1 249 ? 99.381  122.082 108.938 1.00 13.55  ? 449 ASN A ND2 1 
ATOM   1751 N  N   . THR A 1 250 ? 102.329 125.373 106.723 1.00 15.09  ? 450 THR A N   1 
ATOM   1752 C  CA  . THR A 1 250 ? 103.746 125.120 106.519 1.00 15.09  ? 450 THR A CA  1 
ATOM   1753 C  C   . THR A 1 250 ? 104.375 126.293 105.783 1.00 15.09  ? 450 THR A C   1 
ATOM   1754 O  O   . THR A 1 250 ? 103.717 126.982 105.000 1.00 15.09  ? 450 THR A O   1 
ATOM   1755 C  CB  . THR A 1 250 ? 103.986 123.823 105.732 1.00 15.09  ? 450 THR A CB  1 
ATOM   1756 O  OG1 . THR A 1 250 ? 103.077 123.755 104.627 1.00 15.09  ? 450 THR A OG1 1 
ATOM   1757 C  CG2 . THR A 1 250 ? 103.780 122.611 106.629 1.00 15.09  ? 450 THR A CG2 1 
ATOM   1758 N  N   . MET A 1 251 ? 105.664 126.515 106.046 1.00 17.27  ? 451 MET A N   1 
ATOM   1759 C  CA  . MET A 1 251 ? 106.399 127.618 105.448 1.00 17.27  ? 451 MET A CA  1 
ATOM   1760 C  C   . MET A 1 251 ? 107.596 127.184 104.616 1.00 17.27  ? 451 MET A C   1 
ATOM   1761 O  O   . MET A 1 251 ? 108.199 128.033 103.949 1.00 17.27  ? 451 MET A O   1 
ATOM   1762 C  CB  . MET A 1 251 ? 106.882 128.592 106.535 1.00 17.27  ? 451 MET A CB  1 
ATOM   1763 C  CG  . MET A 1 251 ? 107.919 128.002 107.478 1.00 17.27  ? 451 MET A CG  1 
ATOM   1764 S  SD  . MET A 1 251 ? 109.059 129.234 108.140 1.00 17.27  ? 451 MET A SD  1 
ATOM   1765 C  CE  . MET A 1 251 ? 107.999 130.675 108.225 1.00 17.27  ? 451 MET A CE  1 
ATOM   1766 N  N   . ASP A 1 252 ? 107.957 125.903 104.628 1.00 17.22  ? 452 ASP A N   1 
ATOM   1767 C  CA  . ASP A 1 252 ? 109.116 125.431 103.890 1.00 17.22  ? 452 ASP A CA  1 
ATOM   1768 C  C   . ASP A 1 252 ? 108.698 124.906 102.517 1.00 17.22  ? 452 ASP A C   1 
ATOM   1769 O  O   . ASP A 1 252 ? 107.516 124.873 102.165 1.00 17.22  ? 452 ASP A O   1 
ATOM   1770 C  CB  . ASP A 1 252 ? 109.856 124.360 104.691 1.00 17.22  ? 452 ASP A CB  1 
ATOM   1771 C  CG  . ASP A 1 252 ? 109.092 123.054 104.761 1.00 17.22  ? 452 ASP A CG  1 
ATOM   1772 O  OD1 . ASP A 1 252 ? 107.876 123.092 105.043 1.00 17.22  ? 452 ASP A OD1 1 
ATOM   1773 O  OD2 . ASP A 1 252 ? 109.706 121.991 104.534 1.00 17.22  ? 452 ASP A OD2 1 
ATOM   1774 N  N   . GLN A 1 253 ? 109.689 124.484 101.730 1.00 16.98  ? 453 GLN A N   1 
ATOM   1775 C  CA  . GLN A 1 253 ? 109.441 124.019 100.372 1.00 16.98  ? 453 GLN A CA  1 
ATOM   1776 C  C   . GLN A 1 253 ? 108.846 122.619 100.319 1.00 16.98  ? 453 GLN A C   1 
ATOM   1777 O  O   . GLN A 1 253 ? 108.227 122.262 99.310  1.00 16.98  ? 453 GLN A O   1 
ATOM   1778 C  CB  . GLN A 1 253 ? 110.745 124.051 99.568  1.00 16.98  ? 453 GLN A CB  1 
ATOM   1779 C  CG  . GLN A 1 253 ? 110.557 124.028 98.060  1.00 16.98  ? 453 GLN A CG  1 
ATOM   1780 C  CD  . GLN A 1 253 ? 111.865 124.178 97.310  1.00 16.98  ? 453 GLN A CD  1 
ATOM   1781 O  OE1 . GLN A 1 253 ? 112.558 125.187 97.440  1.00 16.98  ? 453 GLN A OE1 1 
ATOM   1782 N  NE2 . GLN A 1 253 ? 112.212 123.169 96.519  1.00 16.98  ? 453 GLN A NE2 1 
ATOM   1783 N  N   . PHE A 1 254 ? 109.006 121.822 101.376 1.00 16.34  ? 454 PHE A N   1 
ATOM   1784 C  CA  . PHE A 1 254 ? 108.578 120.427 101.366 1.00 16.34  ? 454 PHE A CA  1 
ATOM   1785 C  C   . PHE A 1 254 ? 107.440 120.157 102.344 1.00 16.34  ? 454 PHE A C   1 
ATOM   1786 O  O   . PHE A 1 254 ? 107.180 118.995 102.676 1.00 16.34  ? 454 PHE A O   1 
ATOM   1787 C  CB  . PHE A 1 254 ? 109.766 119.509 101.663 1.00 16.34  ? 454 PHE A CB  1 
ATOM   1788 C  CG  . PHE A 1 254 ? 110.968 119.779 100.805 1.00 16.34  ? 454 PHE A CG  1 
ATOM   1789 C  CD1 . PHE A 1 254 ? 110.907 119.607 99.432  1.00 16.34  ? 454 PHE A CD1 1 
ATOM   1790 C  CD2 . PHE A 1 254 ? 112.157 120.209 101.369 1.00 16.34  ? 454 PHE A CD2 1 
ATOM   1791 C  CE1 . PHE A 1 254 ? 112.010 119.857 98.638  1.00 16.34  ? 454 PHE A CE1 1 
ATOM   1792 C  CE2 . PHE A 1 254 ? 113.263 120.461 100.580 1.00 16.34  ? 454 PHE A CE2 1 
ATOM   1793 C  CZ  . PHE A 1 254 ? 113.189 120.285 99.213  1.00 16.34  ? 454 PHE A CZ  1 
ATOM   1794 N  N   . ASN A 1 255 ? 106.755 121.205 102.807 1.00 15.36  ? 455 ASN A N   1 
ATOM   1795 C  CA  . ASN A 1 255 ? 105.608 121.073 103.708 1.00 15.36  ? 455 ASN A CA  1 
ATOM   1796 C  C   . ASN A 1 255 ? 105.970 120.296 104.972 1.00 15.36  ? 455 ASN A C   1 
ATOM   1797 O  O   . ASN A 1 255 ? 105.219 119.432 105.428 1.00 15.36  ? 455 ASN A O   1 
ATOM   1798 C  CB  . ASN A 1 255 ? 104.417 120.423 102.997 1.00 15.36  ? 455 ASN A CB  1 
ATOM   1799 C  CG  . ASN A 1 255 ? 103.868 121.279 101.875 1.00 15.36  ? 455 ASN A CG  1 
ATOM   1800 O  OD1 . ASN A 1 255 ? 103.438 122.411 102.096 1.00 15.36  ? 455 ASN A OD1 1 
ATOM   1801 N  ND2 . ASN A 1 255 ? 103.876 120.741 100.661 1.00 15.36  ? 455 ASN A ND2 1 
ATOM   1802 N  N   . ALA A 1 256 ? 107.132 120.604 105.547 1.00 16.58  ? 456 ALA A N   1 
ATOM   1803 C  CA  . ALA A 1 256 ? 107.617 119.906 106.728 1.00 16.58  ? 456 ALA A CA  1 
ATOM   1804 C  C   . ALA A 1 256 ? 107.953 120.828 107.893 1.00 16.58  ? 456 ALA A C   1 
ATOM   1805 O  O   . ALA A 1 256 ? 108.340 120.333 108.957 1.00 16.58  ? 456 ALA A O   1 
ATOM   1806 C  CB  . ALA A 1 256 ? 108.850 119.062 106.378 1.00 16.58  ? 456 ALA A CB  1 
ATOM   1807 N  N   . ARG A 1 257 ? 107.808 122.126 107.728 1.00 16.80  ? 457 ARG A N   1 
ATOM   1808 C  CA  . ARG A 1 257 ? 108.145 123.122 108.789 1.00 16.80  ? 457 ARG A CA  1 
ATOM   1809 C  C   . ARG A 1 257 ? 106.931 124.008 109.038 1.00 16.80  ? 457 ARG A C   1 
ATOM   1810 O  O   . ARG A 1 257 ? 106.479 124.669 108.139 1.00 16.80  ? 457 ARG A O   1 
ATOM   1811 C  CB  . ARG A 1 257 ? 109.476 123.844 108.517 1.00 16.80  ? 457 ARG A CB  1 
ATOM   1812 C  CG  . ARG A 1 257 ? 109.759 125.081 109.357 1.00 16.80  ? 457 ARG A CG  1 
ATOM   1813 C  CD  . ARG A 1 257 ? 110.702 124.861 110.520 1.00 16.80  ? 457 ARG A CD  1 
ATOM   1814 N  NE  . ARG A 1 257 ? 111.110 126.087 111.198 1.00 16.80  ? 457 ARG A NE  1 
ATOM   1815 C  CZ  . ARG A 1 257 ? 110.632 126.514 112.358 1.00 16.80  ? 457 ARG A CZ  1 
ATOM   1816 N  N   . LEU A 1 258 ? 106.505 124.080 110.278 1.00 15.63  ? 458 LEU A N   1 
ATOM   1817 C  CA  . LEU A 1 258 ? 105.352 124.887 110.641 1.00 15.63  ? 458 LEU A CA  1 
ATOM   1818 C  C   . LEU A 1 258 ? 105.731 126.367 110.720 1.00 15.63  ? 458 LEU A C   1 
ATOM   1819 O  O   . LEU A 1 258 ? 106.907 126.740 110.708 1.00 15.63  ? 458 LEU A O   1 
ATOM   1820 C  CB  . LEU A 1 258 ? 104.766 124.411 111.969 1.00 15.63  ? 458 LEU A CB  1 
ATOM   1821 C  CG  . LEU A 1 258 ? 104.416 122.923 112.052 1.00 15.63  ? 458 LEU A CG  1 
ATOM   1822 C  CD1 . LEU A 1 258 ? 104.034 122.535 113.471 1.00 15.63  ? 458 LEU A CD1 1 
ATOM   1823 C  CD2 . LEU A 1 258 ? 103.299 122.575 111.080 1.00 15.63  ? 458 LEU A CD2 1 
ATOM   1824 N  N   . ILE A 1 259 ? 104.711 127.216 110.804 1.00 14.95  ? 459 ILE A N   1 
ATOM   1825 C  CA  . ILE A 1 259 ? 104.882 128.665 110.826 1.00 14.95  ? 459 ILE A CA  1 
ATOM   1826 C  C   . ILE A 1 259 ? 104.905 129.110 112.286 1.00 14.95  ? 459 ILE A C   1 
ATOM   1827 O  O   . ILE A 1 259 ? 103.871 129.016 112.967 1.00 14.95  ? 459 ILE A O   1 
ATOM   1828 C  CB  . ILE A 1 259 ? 103.765 129.374 110.049 1.00 14.95  ? 459 ILE A CB  1 
ATOM   1829 C  CG1 . ILE A 1 259 ? 103.582 128.731 108.673 1.00 14.95  ? 459 ILE A CG1 1 
ATOM   1830 C  CG2 . ILE A 1 259 ? 104.071 130.858 109.914 1.00 14.95  ? 459 ILE A CG2 1 
ATOM   1831 C  CD1 . ILE A 1 259 ? 102.238 129.017 108.039 1.00 14.95  ? 459 ILE A CD1 1 
ATOM   1832 N  N   . PRO A 1 260 ? 106.031 129.596 112.802 1.00 15.87  ? 460 PRO A N   1 
ATOM   1833 C  CA  . PRO A 1 260 ? 106.111 129.976 114.213 1.00 15.87  ? 460 PRO A CA  1 
ATOM   1834 C  C   . PRO A 1 260 ? 105.841 131.457 114.455 1.00 15.87  ? 460 PRO A C   1 
ATOM   1835 O  O   . PRO A 1 260 ? 105.973 132.303 113.569 1.00 15.87  ? 460 PRO A O   1 
ATOM   1836 C  CB  . PRO A 1 260 ? 107.563 129.629 114.570 1.00 15.87  ? 460 PRO A CB  1 
ATOM   1837 C  CG  . PRO A 1 260 ? 108.313 129.877 113.291 1.00 15.87  ? 460 PRO A CG  1 
ATOM   1838 C  CD  . PRO A 1 260 ? 107.344 129.675 112.138 1.00 15.87  ? 460 PRO A CD  1 
ATOM   1839 N  N   . ILE A 1 261 ? 105.449 131.752 115.697 1.00 16.81  ? 461 ILE A N   1 
ATOM   1840 C  CA  . ILE A 1 261 ? 105.321 133.113 116.197 1.00 16.81  ? 461 ILE A CA  1 
ATOM   1841 C  C   . ILE A 1 261 ? 105.990 133.183 117.564 1.00 16.81  ? 461 ILE A C   1 
ATOM   1842 O  O   . ILE A 1 261 ? 106.142 132.177 118.257 1.00 16.81  ? 461 ILE A O   1 
ATOM   1843 C  CB  . ILE A 1 261 ? 103.850 133.581 116.287 1.00 16.81  ? 461 ILE A CB  1 
ATOM   1844 C  CG1 . ILE A 1 261 ? 103.051 132.672 117.221 1.00 16.81  ? 461 ILE A CG1 1 
ATOM   1845 C  CG2 . ILE A 1 261 ? 103.216 133.637 114.904 1.00 16.81  ? 461 ILE A CG2 1 
ATOM   1846 C  CD1 . ILE A 1 261 ? 101.819 133.329 117.801 1.00 16.81  ? 461 ILE A CD1 1 
ATOM   1847 N  N   . ASN A 1 262 ? 106.391 134.393 117.948 1.00 18.60  ? 462 ASN A N   1 
ATOM   1848 C  CA  . ASN A 1 262 ? 107.118 134.592 119.193 1.00 18.60  ? 462 ASN A CA  1 
ATOM   1849 C  C   . ASN A 1 262 ? 106.145 134.895 120.334 1.00 18.60  ? 462 ASN A C   1 
ATOM   1850 O  O   . ASN A 1 262 ? 104.922 134.867 120.167 1.00 18.60  ? 462 ASN A O   1 
ATOM   1851 C  CB  . ASN A 1 262 ? 108.183 135.676 119.018 1.00 18.60  ? 462 ASN A CB  1 
ATOM   1852 C  CG  . ASN A 1 262 ? 107.601 137.033 118.658 1.00 18.60  ? 462 ASN A CG  1 
ATOM   1853 O  OD1 . ASN A 1 262 ? 106.704 137.542 119.329 1.00 18.60  ? 462 ASN A OD1 1 
ATOM   1854 N  ND2 . ASN A 1 262 ? 108.122 137.629 117.594 1.00 18.60  ? 462 ASN A ND2 1 
ATOM   1855 N  N   . TYR A 1 263 ? 106.694 135.184 121.518 1.00 20.93  ? 463 TYR A N   1 
ATOM   1856 C  CA  . TYR A 1 263 ? 105.866 135.361 122.708 1.00 20.93  ? 463 TYR A CA  1 
ATOM   1857 C  C   . TYR A 1 263 ? 105.022 136.626 122.627 1.00 20.93  ? 463 TYR A C   1 
ATOM   1858 O  O   . TYR A 1 263 ? 103.839 136.611 122.991 1.00 20.93  ? 463 TYR A O   1 
ATOM   1859 C  CB  . TYR A 1 263 ? 106.750 135.388 123.956 1.00 20.93  ? 463 TYR A CB  1 
ATOM   1860 C  CG  . TYR A 1 263 ? 105.998 135.147 125.245 1.00 20.93  ? 463 TYR A CG  1 
ATOM   1861 C  CD1 . TYR A 1 263 ? 105.099 134.097 125.361 1.00 20.93  ? 463 TYR A CD1 1 
ATOM   1862 C  CD2 . TYR A 1 263 ? 106.186 135.976 126.344 1.00 20.93  ? 463 TYR A CD2 1 
ATOM   1863 C  CE1 . TYR A 1 263 ? 104.408 133.875 126.538 1.00 20.93  ? 463 TYR A CE1 1 
ATOM   1864 C  CE2 . TYR A 1 263 ? 105.500 135.761 127.524 1.00 20.93  ? 463 TYR A CE2 1 
ATOM   1865 C  CZ  . TYR A 1 263 ? 104.612 134.709 127.615 1.00 20.93  ? 463 TYR A CZ  1 
ATOM   1866 N  N   . ASP A 1 264 ? 105.611 137.732 122.166 1.00 21.66  ? 464 ASP A N   1 
ATOM   1867 C  CA  . ASP A 1 264 ? 104.872 138.989 122.088 1.00 21.66  ? 464 ASP A CA  1 
ATOM   1868 C  C   . ASP A 1 264 ? 103.710 138.892 121.107 1.00 21.66  ? 464 ASP A C   1 
ATOM   1869 O  O   . ASP A 1 264 ? 102.620 139.409 121.375 1.00 21.66  ? 464 ASP A O   1 
ATOM   1870 C  CB  . ASP A 1 264 ? 105.814 140.126 121.695 1.00 21.66  ? 464 ASP A CB  1 
ATOM   1871 C  CG  . ASP A 1 264 ? 107.198 139.964 122.289 1.00 21.66  ? 464 ASP A CG  1 
ATOM   1872 O  OD1 . ASP A 1 264 ? 107.340 140.144 123.517 1.00 21.66  ? 464 ASP A OD1 1 
ATOM   1873 O  OD2 . ASP A 1 264 ? 108.142 139.654 121.533 1.00 21.66  ? 464 ASP A OD2 1 
ATOM   1874 N  N   . GLN A 1 265 ? 103.927 138.239 119.963 1.00 19.36  ? 465 GLN A N   1 
ATOM   1875 C  CA  . GLN A 1 265 ? 102.847 138.068 118.997 1.00 19.36  ? 465 GLN A CA  1 
ATOM   1876 C  C   . GLN A 1 265 ? 101.733 137.199 119.566 1.00 19.36  ? 465 GLN A C   1 
ATOM   1877 O  O   . GLN A 1 265 ? 100.547 137.466 119.337 1.00 19.36  ? 465 GLN A O   1 
ATOM   1878 C  CB  . GLN A 1 265 ? 103.397 137.470 117.702 1.00 19.36  ? 465 GLN A CB  1 
ATOM   1879 C  CG  . GLN A 1 265 ? 104.168 138.467 116.852 1.00 19.36  ? 465 GLN A CG  1 
ATOM   1880 C  CD  . GLN A 1 265 ? 105.337 137.836 116.126 1.00 19.36  ? 465 GLN A CD  1 
ATOM   1881 O  OE1 . GLN A 1 265 ? 105.569 136.631 116.226 1.00 19.36  ? 465 GLN A OE1 1 
ATOM   1882 N  NE2 . GLN A 1 265 ? 106.088 138.649 115.393 1.00 19.36  ? 465 GLN A NE2 1 
ATOM   1883 N  N   . LEU A 1 266 ? 102.096 136.153 120.313 1.00 20.56  ? 466 LEU A N   1 
ATOM   1884 C  CA  . LEU A 1 266 ? 101.086 135.317 120.956 1.00 20.56  ? 466 LEU A CA  1 
ATOM   1885 C  C   . LEU A 1 266 ? 100.290 136.108 121.987 1.00 20.56  ? 466 LEU A C   1 
ATOM   1886 O  O   . LEU A 1 266 ? 99.067  135.948 122.094 1.00 20.56  ? 466 LEU A O   1 
ATOM   1887 C  CB  . LEU A 1 266 ? 101.750 134.102 121.604 1.00 20.56  ? 466 LEU A CB  1 
ATOM   1888 C  CG  . LEU A 1 266 ? 100.810 133.093 122.267 1.00 20.56  ? 466 LEU A CG  1 
ATOM   1889 C  CD1 . LEU A 1 266 ? 99.830  132.527 121.251 1.00 20.56  ? 466 LEU A CD1 1 
ATOM   1890 C  CD2 . LEU A 1 266 ? 101.600 131.978 122.931 1.00 20.56  ? 466 LEU A CD2 1 
ATOM   1891 N  N   . LYS A 1 267 ? 100.965 136.960 122.762 1.00 22.54  ? 467 LYS A N   1 
ATOM   1892 C  CA  . LYS A 1 267 ? 100.263 137.798 123.729 1.00 22.54  ? 467 LYS A CA  1 
ATOM   1893 C  C   . LYS A 1 267 ? 99.330  138.781 123.033 1.00 22.54  ? 467 LYS A C   1 
ATOM   1894 O  O   . LYS A 1 267 ? 98.220  139.041 123.513 1.00 22.54  ? 467 LYS A O   1 
ATOM   1895 C  CB  . LYS A 1 267 ? 101.267 138.542 124.609 1.00 22.54  ? 467 LYS A CB  1 
ATOM   1896 C  CG  . LYS A 1 267 ? 102.069 137.642 125.532 1.00 22.54  ? 467 LYS A CG  1 
ATOM   1897 C  CD  . LYS A 1 267 ? 101.208 137.118 126.671 1.00 22.54  ? 467 LYS A CD  1 
ATOM   1898 C  CE  . LYS A 1 267 ? 101.286 135.606 126.775 1.00 22.54  ? 467 LYS A CE  1 
ATOM   1899 N  NZ  . LYS A 1 267 ? 100.421 134.933 125.768 1.00 22.54  ? 467 LYS A NZ  1 
ATOM   1900 N  N   . LYS A 1 268 ? 99.768  139.344 121.905 1.00 22.84  ? 468 LYS A N   1 
ATOM   1901 C  CA  . LYS A 1 268 ? 98.900  140.229 121.134 1.00 22.84  ? 468 LYS A CA  1 
ATOM   1902 C  C   . LYS A 1 268 ? 97.676  139.483 120.618 1.00 22.84  ? 468 LYS A C   1 
ATOM   1903 O  O   . LYS A 1 268 ? 96.560  140.016 120.638 1.00 22.84  ? 468 LYS A O   1 
ATOM   1904 C  CB  . LYS A 1 268 ? 99.680  140.846 119.971 1.00 22.84  ? 468 LYS A CB  1 
ATOM   1905 C  CG  . LYS A 1 268 ? 100.400 142.138 120.312 1.00 22.84  ? 468 LYS A CG  1 
ATOM   1906 C  CD  . LYS A 1 268 ? 101.694 142.266 119.527 1.00 22.84  ? 468 LYS A CD  1 
ATOM   1907 C  CE  . LYS A 1 268 ? 101.849 143.662 118.946 1.00 22.84  ? 468 LYS A CE  1 
ATOM   1908 N  NZ  . LYS A 1 268 ? 103.174 143.850 118.294 1.00 22.84  ? 468 LYS A NZ  1 
ATOM   1909 N  N   . LEU A 1 269 ? 97.870  138.251 120.143 1.00 22.49  ? 469 LEU A N   1 
ATOM   1910 C  CA  . LEU A 1 269 ? 96.743  137.446 119.681 1.00 22.49  ? 469 LEU A CA  1 
ATOM   1911 C  C   . LEU A 1 269 ? 95.778  137.140 120.818 1.00 22.49  ? 469 LEU A C   1 
ATOM   1912 O  O   . LEU A 1 269 ? 94.555  137.185 120.635 1.00 22.49  ? 469 LEU A O   1 
ATOM   1913 C  CB  . LEU A 1 269 ? 97.249  136.151 119.046 1.00 22.49  ? 469 LEU A CB  1 
ATOM   1914 C  CG  . LEU A 1 269 ? 97.831  136.269 117.637 1.00 22.49  ? 469 LEU A CG  1 
ATOM   1915 C  CD1 . LEU A 1 269 ? 98.238  134.902 117.112 1.00 22.49  ? 469 LEU A CD1 1 
ATOM   1916 C  CD2 . LEU A 1 269 ? 96.834  136.933 116.703 1.00 22.49  ? 469 LEU A CD2 1 
ATOM   1917 N  N   . ASP A 1 270 ? 96.307  136.827 122.002 1.00 25.81  ? 470 ASP A N   1 
ATOM   1918 C  CA  . ASP A 1 270 ? 95.453  136.532 123.147 1.00 25.81  ? 470 ASP A CA  1 
ATOM   1919 C  C   . ASP A 1 270 ? 94.770  137.777 123.696 1.00 25.81  ? 470 ASP A C   1 
ATOM   1920 O  O   . ASP A 1 270 ? 93.820  137.653 124.475 1.00 25.81  ? 470 ASP A O   1 
ATOM   1921 C  CB  . ASP A 1 270 ? 96.268  135.855 124.249 1.00 25.81  ? 470 ASP A CB  1 
ATOM   1922 C  CG  . ASP A 1 270 ? 96.783  134.491 123.838 1.00 25.81  ? 470 ASP A CG  1 
ATOM   1923 O  OD1 . ASP A 1 270 ? 96.294  133.951 122.822 1.00 25.81  ? 470 ASP A OD1 1 
ATOM   1924 O  OD2 . ASP A 1 270 ? 97.677  133.956 124.528 1.00 25.81  ? 470 ASP A OD2 1 
ATOM   1925 N  N   . SER A 1 271 ? 95.228  138.966 123.313 1.00 26.80  ? 471 SER A N   1 
ATOM   1926 C  CA  . SER A 1 271 ? 94.629  140.214 123.768 1.00 26.80  ? 471 SER A CA  1 
ATOM   1927 C  C   . SER A 1 271 ? 93.488  140.683 122.875 1.00 26.80  ? 471 SER A C   1 
ATOM   1928 O  O   . SER A 1 271 ? 92.871  141.712 123.173 1.00 26.80  ? 471 SER A O   1 
ATOM   1929 C  CB  . SER A 1 271 ? 95.698  141.307 123.860 1.00 26.80  ? 471 SER A CB  1 
ATOM   1930 O  OG  . SER A 1 271 ? 95.779  142.048 122.654 1.00 26.80  ? 471 SER A OG  1 
ATOM   1931 N  N   . GLY A 1 272 ? 93.186  139.956 121.800 1.00 25.42  ? 472 GLY A N   1 
ATOM   1932 C  CA  . GLY A 1 272 ? 92.089  140.298 120.915 1.00 25.42  ? 472 GLY A CA  1 
ATOM   1933 C  C   . GLY A 1 272 ? 92.496  140.749 119.531 1.00 25.42  ? 472 GLY A C   1 
ATOM   1934 O  O   . GLY A 1 272 ? 91.618  140.944 118.683 1.00 25.42  ? 472 GLY A O   1 
ATOM   1935 N  N   . LYS A 1 273 ? 93.787  140.924 119.268 1.00 24.43  ? 473 LYS A N   1 
ATOM   1936 C  CA  . LYS A 1 273 ? 94.237  141.312 117.941 1.00 24.43  ? 473 LYS A CA  1 
ATOM   1937 C  C   . LYS A 1 273 ? 94.073  140.153 116.966 1.00 24.43  ? 473 LYS A C   1 
ATOM   1938 O  O   . LYS A 1 273 ? 94.142  138.979 117.342 1.00 24.43  ? 473 LYS A O   1 
ATOM   1939 C  CB  . LYS A 1 273 ? 95.691  141.776 117.981 1.00 24.43  ? 473 LYS A CB  1 
ATOM   1940 C  CG  . LYS A 1 273 ? 95.860  143.162 118.592 1.00 24.43  ? 473 LYS A CG  1 
ATOM   1941 C  CD  . LYS A 1 273 ? 97.320  143.497 118.847 1.00 24.43  ? 473 LYS A CD  1 
ATOM   1942 C  CE  . LYS A 1 273 ? 97.481  144.886 119.453 1.00 24.43  ? 473 LYS A CE  1 
ATOM   1943 N  NZ  . LYS A 1 273 ? 96.347  145.251 120.341 1.00 24.43  ? 473 LYS A NZ  1 
ATOM   1944 N  N   . GLN A 1 274 ? 93.853  140.491 115.699 1.00 22.61  ? 474 GLN A N   1 
ATOM   1945 C  CA  . GLN A 1 274 ? 93.558  139.501 114.676 1.00 22.61  ? 474 GLN A CA  1 
ATOM   1946 C  C   . GLN A 1 274 ? 94.591  139.580 113.559 1.00 22.61  ? 474 GLN A C   1 
ATOM   1947 O  O   . GLN A 1 274 ? 95.148  140.647 113.281 1.00 22.61  ? 474 GLN A O   1 
ATOM   1948 C  CB  . GLN A 1 274 ? 92.146  139.702 114.106 1.00 22.61  ? 474 GLN A CB  1 
ATOM   1949 C  CG  . GLN A 1 274 ? 91.065  139.821 115.177 1.00 22.61  ? 474 GLN A CG  1 
ATOM   1950 C  CD  . GLN A 1 274 ? 90.404  138.500 115.500 1.00 22.61  ? 474 GLN A CD  1 
ATOM   1951 O  OE1 . GLN A 1 274 ? 90.902  137.737 116.328 1.00 22.61  ? 474 GLN A OE1 1 
ATOM   1952 N  NE2 . GLN A 1 274 ? 89.277  138.221 114.856 1.00 22.61  ? 474 GLN A NE2 1 
ATOM   1953 N  N   . ILE A 1 275 ? 94.844  138.437 112.928 1.00 18.02  ? 475 ILE A N   1 
ATOM   1954 C  CA  . ILE A 1 275 ? 95.813  138.336 111.841 1.00 18.02  ? 475 ILE A CA  1 
ATOM   1955 C  C   . ILE A 1 275 ? 95.099  138.544 110.513 1.00 18.02  ? 475 ILE A C   1 
ATOM   1956 O  O   . ILE A 1 275 ? 94.039  137.960 110.259 1.00 18.02  ? 475 ILE A O   1 
ATOM   1957 C  CB  . ILE A 1 275 ? 96.538  136.978 111.878 1.00 18.02  ? 475 ILE A CB  1 
ATOM   1958 C  CG1 . ILE A 1 275 ? 97.640  136.987 112.938 1.00 18.02  ? 475 ILE A CG1 1 
ATOM   1959 C  CG2 . ILE A 1 275 ? 97.120  136.636 110.519 1.00 18.02  ? 475 ILE A CG2 1 
ATOM   1960 C  CD1 . ILE A 1 275 ? 98.006  135.609 113.447 1.00 18.02  ? 475 ILE A CD1 1 
ATOM   1961 N  N   . LYS A 1 276 ? 95.682  139.384 109.662 1.00 16.48  ? 476 LYS A N   1 
ATOM   1962 C  CA  . LYS A 1 276 ? 95.159  139.658 108.334 1.00 16.48  ? 476 LYS A CA  1 
ATOM   1963 C  C   . LYS A 1 276 ? 96.010  138.962 107.280 1.00 16.48  ? 476 LYS A C   1 
ATOM   1964 O  O   . LYS A 1 276 ? 97.223  138.797 107.441 1.00 16.48  ? 476 LYS A O   1 
ATOM   1965 C  CB  . LYS A 1 276 ? 95.119  141.165 108.064 1.00 16.48  ? 476 LYS A CB  1 
ATOM   1966 C  CG  . LYS A 1 276 ? 94.575  141.990 109.220 1.00 16.48  ? 476 LYS A CG  1 
ATOM   1967 C  CD  . LYS A 1 276 ? 93.103  141.699 109.460 1.00 16.48  ? 476 LYS A CD  1 
ATOM   1968 C  CE  . LYS A 1 276 ? 92.668  142.150 110.843 1.00 16.48  ? 476 LYS A CE  1 
ATOM   1969 N  NZ  . LYS A 1 276 ? 91.294  141.681 111.173 1.00 16.48  ? 476 LYS A NZ  1 
ATOM   1970 N  N   . LEU A 1 277 ? 95.356  138.551 106.197 1.00 14.67  ? 477 LEU A N   1 
ATOM   1971 C  CA  . LEU A 1 277 ? 96.000  137.863 105.087 1.00 14.67  ? 477 LEU A CA  1 
ATOM   1972 C  C   . LEU A 1 277 ? 95.905  138.727 103.838 1.00 14.67  ? 477 LEU A C   1 
ATOM   1973 O  O   . LEU A 1 277 ? 94.822  139.211 103.496 1.00 14.67  ? 477 LEU A O   1 
ATOM   1974 C  CB  . LEU A 1 277 ? 95.353  136.498 104.836 1.00 14.67  ? 477 LEU A CB  1 
ATOM   1975 C  CG  . LEU A 1 277 ? 95.964  135.637 103.726 1.00 14.67  ? 477 LEU A CG  1 
ATOM   1976 C  CD1 . LEU A 1 277 ? 96.240  134.230 104.229 1.00 14.67  ? 477 LEU A CD1 1 
ATOM   1977 C  CD2 . LEU A 1 277 ? 95.052  135.604 102.507 1.00 14.67  ? 477 LEU A CD2 1 
ATOM   1978 N  N   . GLU A 1 278 ? 97.036  138.915 103.160 1.00 14.78  ? 478 GLU A N   1 
ATOM   1979 C  CA  . GLU A 1 278 ? 97.083  139.672 101.916 1.00 14.78  ? 478 GLU A CA  1 
ATOM   1980 C  C   . GLU A 1 278 ? 97.699  138.811 100.824 1.00 14.78  ? 478 GLU A C   1 
ATOM   1981 O  O   . GLU A 1 278 ? 98.572  137.986 101.097 1.00 14.78  ? 478 GLU A O   1 
ATOM   1982 C  CB  . GLU A 1 278 ? 97.890  140.968 102.071 1.00 14.78  ? 478 GLU A CB  1 
ATOM   1983 C  CG  . GLU A 1 278 ? 97.881  141.552 103.472 1.00 14.78  ? 478 GLU A CG  1 
ATOM   1984 C  CD  . GLU A 1 278 ? 98.479  142.943 103.523 1.00 14.78  ? 478 GLU A CD  1 
ATOM   1985 O  OE1 . GLU A 1 278 ? 99.532  143.162 102.889 1.00 14.78  ? 478 GLU A OE1 1 
ATOM   1986 O  OE2 . GLU A 1 278 ? 97.898  143.818 104.199 1.00 14.78  ? 478 GLU A OE2 1 
ATOM   1987 N  N   . THR A 1 279 ? 97.241  139.001 99.590  1.00 14.46  ? 479 THR A N   1 
ATOM   1988 C  CA  . THR A 1 279 ? 97.774  138.281 98.440  1.00 14.46  ? 479 THR A CA  1 
ATOM   1989 C  C   . THR A 1 279 ? 98.711  139.206 97.670  1.00 14.46  ? 479 THR A C   1 
ATOM   1990 O  O   . THR A 1 279 ? 98.289  140.272 97.206  1.00 14.46  ? 479 THR A O   1 
ATOM   1991 C  CB  . THR A 1 279 ? 96.651  137.781 97.534  1.00 14.46  ? 479 THR A CB  1 
ATOM   1992 O  OG1 . THR A 1 279 ? 95.618  137.188 98.332  1.00 14.46  ? 479 THR A OG1 1 
ATOM   1993 C  CG2 . THR A 1 279 ? 97.180  136.748 96.549  1.00 14.46  ? 479 THR A CG2 1 
ATOM   1994 N  N   . THR A 1 280 ? 99.973  138.799 97.534  1.00 13.94  ? 480 THR A N   1 
ATOM   1995 C  CA  . THR A 1 280 ? 100.959 139.608 96.829  1.00 13.94  ? 480 THR A CA  1 
ATOM   1996 C  C   . THR A 1 280 ? 101.116 139.225 95.365  1.00 13.94  ? 480 THR A C   1 
ATOM   1997 O  O   . THR A 1 280 ? 101.274 140.111 94.520  1.00 13.94  ? 480 THR A O   1 
ATOM   1998 C  CB  . THR A 1 280 ? 102.324 139.507 97.519  1.00 13.94  ? 480 THR A CB  1 
ATOM   1999 O  OG1 . THR A 1 280 ? 102.842 138.179 97.370  1.00 13.94  ? 480 THR A OG1 1 
ATOM   2000 C  CG2 . THR A 1 280 ? 102.199 139.834 98.998  1.00 13.94  ? 480 THR A CG2 1 
ATOM   2001 N  N   . GLN A 1 281 ? 101.074 137.934 95.047  1.00 12.76  ? 481 GLN A N   1 
ATOM   2002 C  CA  . GLN A 1 281 ? 101.198 137.478 93.671  1.00 12.76  ? 481 GLN A CA  1 
ATOM   2003 C  C   . GLN A 1 281 ? 100.630 136.070 93.571  1.00 12.76  ? 481 GLN A C   1 
ATOM   2004 O  O   . GLN A 1 281 ? 100.594 135.326 94.554  1.00 12.76  ? 481 GLN A O   1 
ATOM   2005 C  CB  . GLN A 1 281 ? 102.655 137.511 93.195  1.00 12.76  ? 481 GLN A CB  1 
ATOM   2006 C  CG  . GLN A 1 281 ? 103.598 136.671 94.038  1.00 12.76  ? 481 GLN A CG  1 
ATOM   2007 C  CD  . GLN A 1 281 ? 105.052 136.884 93.676  1.00 12.76  ? 481 GLN A CD  1 
ATOM   2008 O  OE1 . GLN A 1 281 ? 105.399 137.850 92.995  1.00 12.76  ? 481 GLN A OE1 1 
ATOM   2009 N  NE2 . GLN A 1 281 ? 105.914 135.984 94.131  1.00 12.76  ? 481 GLN A NE2 1 
ATOM   2010 N  N   . VAL A 1 282 ? 100.184 135.719 92.368  1.00 9.41   ? 482 VAL A N   1 
ATOM   2011 C  CA  . VAL A 1 282 ? 99.632  134.401 92.081  1.00 9.41   ? 482 VAL A CA  1 
ATOM   2012 C  C   . VAL A 1 282 ? 100.319 133.853 90.838  1.00 9.41   ? 482 VAL A C   1 
ATOM   2013 O  O   . VAL A 1 282 ? 100.416 134.549 89.821  1.00 9.41   ? 482 VAL A O   1 
ATOM   2014 C  CB  . VAL A 1 282 ? 98.105  134.443 91.879  1.00 9.41   ? 482 VAL A CB  1 
ATOM   2015 C  CG1 . VAL A 1 282 ? 97.568  133.044 91.631  1.00 9.41   ? 482 VAL A CG1 1 
ATOM   2016 C  CG2 . VAL A 1 282 ? 97.420  135.072 93.083  1.00 9.41   ? 482 VAL A CG2 1 
ATOM   2017 N  N   . SER A 1 283 ? 100.790 132.614 90.919  1.00 10.97  ? 483 SER A N   1 
ATOM   2018 C  CA  . SER A 1 283 ? 101.397 131.928 89.790  1.00 10.97  ? 483 SER A CA  1 
ATOM   2019 C  C   . SER A 1 283 ? 100.432 130.892 89.229  1.00 10.97  ? 483 SER A C   1 
ATOM   2020 O  O   . SER A 1 283 ? 99.634  130.300 89.959  1.00 10.97  ? 483 SER A O   1 
ATOM   2021 C  CB  . SER A 1 283 ? 102.709 131.254 90.200  1.00 10.97  ? 483 SER A CB  1 
ATOM   2022 O  OG  . SER A 1 283 ? 103.789 132.170 90.154  1.00 10.97  ? 483 SER A OG  1 
ATOM   2023 N  N   . GLY A 1 284 ? 100.513 130.679 87.922  1.00 12.94  ? 484 GLY A N   1 
ATOM   2024 C  CA  . GLY A 1 284 ? 99.620  129.743 87.264  1.00 12.94  ? 484 GLY A CA  1 
ATOM   2025 C  C   . GLY A 1 284 ? 100.050 129.526 85.832  1.00 12.94  ? 484 GLY A C   1 
ATOM   2026 O  O   . GLY A 1 284 ? 100.988 130.159 85.334  1.00 12.94  ? 484 GLY A O   1 
ATOM   2027 N  N   . ASN A 1 285 ? 99.343  128.614 85.171  1.00 13.76  ? 485 ASN A N   1 
ATOM   2028 C  CA  . ASN A 1 285 ? 99.647  128.225 83.805  1.00 13.76  ? 485 ASN A CA  1 
ATOM   2029 C  C   . ASN A 1 285 ? 98.403  128.318 82.932  1.00 13.76  ? 485 ASN A C   1 
ATOM   2030 O  O   . ASN A 1 285 ? 97.269  128.233 83.412  1.00 13.76  ? 485 ASN A O   1 
ATOM   2031 C  CB  . ASN A 1 285 ? 100.216 126.800 83.745  1.00 13.76  ? 485 ASN A CB  1 
ATOM   2032 C  CG  . ASN A 1 285 ? 101.549 126.672 84.454  1.00 13.76  ? 485 ASN A CG  1 
ATOM   2033 O  OD1 . ASN A 1 285 ? 102.411 127.542 84.340  1.00 13.76  ? 485 ASN A OD1 1 
ATOM   2034 N  ND2 . ASN A 1 285 ? 101.724 125.583 85.191  1.00 13.76  ? 485 ASN A ND2 1 
ATOM   2035 N  N   . TYR A 1 286 ? 98.631  128.499 81.636  1.00 16.61  ? 486 TYR A N   1 
ATOM   2036 C  CA  . TYR A 1 286 ? 97.584  128.473 80.627  1.00 16.61  ? 486 TYR A CA  1 
ATOM   2037 C  C   . TYR A 1 286 ? 97.804  127.290 79.691  1.00 16.61  ? 486 TYR A C   1 
ATOM   2038 O  O   . TYR A 1 286 ? 98.871  126.672 79.669  1.00 16.61  ? 486 TYR A O   1 
ATOM   2039 C  CB  . TYR A 1 286 ? 97.538  129.790 79.843  1.00 16.61  ? 486 TYR A CB  1 
ATOM   2040 C  CG  . TYR A 1 286 ? 98.818  130.140 79.117  1.00 16.61  ? 486 TYR A CG  1 
ATOM   2041 C  CD1 . TYR A 1 286 ? 99.040  129.718 77.813  1.00 16.61  ? 486 TYR A CD1 1 
ATOM   2042 C  CD2 . TYR A 1 286 ? 99.802  130.902 79.734  1.00 16.61  ? 486 TYR A CD2 1 
ATOM   2043 C  CE1 . TYR A 1 286 ? 100.208 130.037 77.146  1.00 16.61  ? 486 TYR A CE1 1 
ATOM   2044 C  CE2 . TYR A 1 286 ? 100.973 131.227 79.075  1.00 16.61  ? 486 TYR A CE2 1 
ATOM   2045 C  CZ  . TYR A 1 286 ? 101.170 130.793 77.782  1.00 16.61  ? 486 TYR A CZ  1 
ATOM   2046 N  N   . GLY A 1 287 ? 96.775  126.981 78.910  1.00 17.72  ? 487 GLY A N   1 
ATOM   2047 C  CA  . GLY A 1 287 ? 96.786  125.817 78.038  1.00 17.72  ? 487 GLY A CA  1 
ATOM   2048 C  C   . GLY A 1 287 ? 97.055  126.187 76.592  1.00 17.72  ? 487 GLY A C   1 
ATOM   2049 O  O   . GLY A 1 287 ? 96.564  127.199 76.092  1.00 17.72  ? 487 GLY A O   1 
ATOM   2050 N  N   . THR A 1 288 ? 97.847  125.347 75.924  1.00 22.00  ? 488 THR A N   1 
ATOM   2051 C  CA  . THR A 1 288 ? 98.140  125.484 74.504  1.00 22.00  ? 488 THR A CA  1 
ATOM   2052 C  C   . THR A 1 288 ? 98.049  124.105 73.860  1.00 22.00  ? 488 THR A C   1 
ATOM   2053 O  O   . THR A 1 288 ? 97.746  123.108 74.523  1.00 22.00  ? 488 THR A O   1 
ATOM   2054 C  CB  . THR A 1 288 ? 99.519  126.109 74.265  1.00 22.00  ? 488 THR A CB  1 
ATOM   2055 O  OG1 . THR A 1 288 ? 100.501 125.431 75.060  1.00 22.00  ? 488 THR A OG1 1 
ATOM   2056 C  CG2 . THR A 1 288 ? 99.511  127.587 74.622  1.00 22.00  ? 488 THR A CG2 1 
ATOM   2057 N  N   . LYS A 1 289 ? 98.318  124.049 72.560  1.00 29.52  ? 489 LYS A N   1 
ATOM   2058 C  CA  . LYS A 1 289 ? 98.300  122.803 71.810  1.00 29.52  ? 489 LYS A CA  1 
ATOM   2059 C  C   . LYS A 1 289 ? 99.661  122.555 71.178  1.00 29.52  ? 489 LYS A C   1 
ATOM   2060 O  O   . LYS A 1 289 ? 100.338 123.488 70.732  1.00 29.52  ? 489 LYS A O   1 
ATOM   2061 C  CB  . LYS A 1 289 ? 97.216  122.818 70.724  1.00 29.52  ? 489 LYS A CB  1 
ATOM   2062 C  CG  . LYS A 1 289 ? 95.931  122.107 71.119  1.00 29.52  ? 489 LYS A CG  1 
ATOM   2063 C  CD  . LYS A 1 289 ? 94.753  123.064 71.160  1.00 29.52  ? 489 LYS A CD  1 
ATOM   2064 C  CE  . LYS A 1 289 ? 93.586  122.469 71.932  1.00 29.52  ? 489 LYS A CE  1 
ATOM   2065 N  NZ  . LYS A 1 289 ? 92.611  123.508 72.360  1.00 29.52  ? 489 LYS A NZ  1 
ATOM   2066 N  N   . ASN A 1 290 ? 100.059 121.287 71.143  1.00 33.88  ? 490 ASN A N   1 
ATOM   2067 C  CA  . ASN A 1 290 ? 101.329 120.863 70.574  1.00 33.88  ? 490 ASN A CA  1 
ATOM   2068 C  C   . ASN A 1 290 ? 101.103 120.200 69.217  1.00 33.88  ? 490 ASN A C   1 
ATOM   2069 O  O   . ASN A 1 290 ? 99.983  120.133 68.706  1.00 33.88  ? 490 ASN A O   1 
ATOM   2070 C  CB  . ASN A 1 290 ? 102.072 119.940 71.549  1.00 33.88  ? 490 ASN A CB  1 
ATOM   2071 C  CG  . ASN A 1 290 ? 101.359 118.611 71.780  1.00 33.88  ? 490 ASN A CG  1 
ATOM   2072 O  OD1 . ASN A 1 290 ? 100.345 118.305 71.155  1.00 33.88  ? 490 ASN A OD1 1 
ATOM   2073 N  ND2 . ASN A 1 290 ? 101.902 117.812 72.690  1.00 33.88  ? 490 ASN A ND2 1 
ATOM   2074 N  N   . SER A 1 291 ? 102.198 119.708 68.631  1.00 36.93  ? 491 SER A N   1 
ATOM   2075 C  CA  . SER A 1 291 ? 102.120 119.051 67.330  1.00 36.93  ? 491 SER A CA  1 
ATOM   2076 C  C   . SER A 1 291 ? 101.353 117.736 67.386  1.00 36.93  ? 491 SER A C   1 
ATOM   2077 O  O   . SER A 1 291 ? 100.836 117.291 66.356  1.00 36.93  ? 491 SER A O   1 
ATOM   2078 C  CB  . SER A 1 291 ? 103.524 118.809 66.777  1.00 36.93  ? 491 SER A CB  1 
ATOM   2079 O  OG  . SER A 1 291 ? 103.900 119.837 65.876  1.00 36.93  ? 491 SER A OG  1 
ATOM   2080 N  N   . GLN A 1 292 ? 101.268 117.108 68.556  1.00 37.47  ? 492 GLN A N   1 
ATOM   2081 C  CA  . GLN A 1 292 ? 100.540 115.857 68.719  1.00 37.47  ? 492 GLN A CA  1 
ATOM   2082 C  C   . GLN A 1 292 ? 99.060  116.066 69.012  1.00 37.47  ? 492 GLN A C   1 
ATOM   2083 O  O   . GLN A 1 292 ? 98.320  115.082 69.119  1.00 37.47  ? 492 GLN A O   1 
ATOM   2084 C  CB  . GLN A 1 292 ? 101.172 115.020 69.836  1.00 37.47  ? 492 GLN A CB  1 
ATOM   2085 C  CG  . GLN A 1 292 ? 102.490 114.368 69.452  1.00 37.47  ? 492 GLN A CG  1 
ATOM   2086 C  CD  . GLN A 1 292 ? 103.692 115.145 69.949  1.00 37.47  ? 492 GLN A CD  1 
ATOM   2087 O  OE1 . GLN A 1 292 ? 103.988 116.233 69.455  1.00 37.47  ? 492 GLN A OE1 1 
ATOM   2088 N  NE2 . GLN A 1 292 ? 104.393 114.588 70.930  1.00 37.47  ? 492 GLN A NE2 1 
ATOM   2089 N  N   . GLY A 1 293 ? 98.612  117.313 69.145  1.00 32.23  ? 493 GLY A N   1 
ATOM   2090 C  CA  . GLY A 1 293 ? 97.217  117.593 69.416  1.00 32.23  ? 493 GLY A CA  1 
ATOM   2091 C  C   . GLY A 1 293 ? 96.815  117.526 70.871  1.00 32.23  ? 493 GLY A C   1 
ATOM   2092 O  O   . GLY A 1 293 ? 95.616  117.597 71.167  1.00 32.23  ? 493 GLY A O   1 
ATOM   2093 N  N   . GLN A 1 294 ? 97.768  117.397 71.787  1.00 27.06  ? 494 GLN A N   1 
ATOM   2094 C  CA  . GLN A 1 294 ? 97.479  117.321 73.210  1.00 27.06  ? 494 GLN A CA  1 
ATOM   2095 C  C   . GLN A 1 294 ? 97.626  118.693 73.855  1.00 27.06  ? 494 GLN A C   1 
ATOM   2096 O  O   . GLN A 1 294 ? 98.473  119.500 73.462  1.00 27.06  ? 494 GLN A O   1 
ATOM   2097 C  CB  . GLN A 1 294 ? 98.406  116.321 73.903  1.00 27.06  ? 494 GLN A CB  1 
ATOM   2098 C  CG  . GLN A 1 294 ? 98.600  115.017 73.141  1.00 27.06  ? 494 GLN A CG  1 
ATOM   2099 C  CD  . GLN A 1 294 ? 97.347  114.163 73.107  1.00 27.06  ? 494 GLN A CD  1 
ATOM   2100 O  OE1 . GLN A 1 294 ? 96.472  114.291 73.964  1.00 27.06  ? 494 GLN A OE1 1 
ATOM   2101 N  NE2 . GLN A 1 294 ? 97.256  113.285 72.116  1.00 27.06  ? 494 GLN A NE2 1 
ATOM   2102 N  N   . ILE A 1 295 ? 96.788  118.950 74.855  1.00 21.28  ? 495 ILE A N   1 
ATOM   2103 C  CA  . ILE A 1 295 ? 96.829  120.216 75.578  1.00 21.28  ? 495 ILE A CA  1 
ATOM   2104 C  C   . ILE A 1 295 ? 98.023  120.205 76.521  1.00 21.28  ? 495 ILE A C   1 
ATOM   2105 O  O   . ILE A 1 295 ? 98.199  119.272 77.313  1.00 21.28  ? 495 ILE A O   1 
ATOM   2106 C  CB  . ILE A 1 295 ? 95.516  120.454 76.341  1.00 21.28  ? 495 ILE A CB  1 
ATOM   2107 C  CG1 . ILE A 1 295 ? 94.365  120.698 75.363  1.00 21.28  ? 495 ILE A CG1 1 
ATOM   2108 C  CG2 . ILE A 1 295 ? 95.659  121.630 77.295  1.00 21.28  ? 495 ILE A CG2 1 
ATOM   2109 C  CD1 . ILE A 1 295 ? 93.013  120.815 76.029  1.00 21.28  ? 495 ILE A CD1 1 
ATOM   2110 N  N   . ILE A 1 296 ? 98.847  121.246 76.440  1.00 20.38  ? 496 ILE A N   1 
ATOM   2111 C  CA  . ILE A 1 296 ? 100.048 121.374 77.255  1.00 20.38  ? 496 ILE A CA  1 
ATOM   2112 C  C   . ILE A 1 296 ? 99.930  122.644 78.086  1.00 20.38  ? 496 ILE A C   1 
ATOM   2113 O  O   . ILE A 1 296 ? 99.650  123.720 77.546  1.00 20.38  ? 496 ILE A O   1 
ATOM   2114 C  CB  . ILE A 1 296 ? 101.322 121.404 76.391  1.00 20.38  ? 496 ILE A CB  1 
ATOM   2115 C  CG1 . ILE A 1 296 ? 101.465 120.105 75.596  1.00 20.38  ? 496 ILE A CG1 1 
ATOM   2116 C  CG2 . ILE A 1 296 ? 102.553 121.645 77.255  1.00 20.38  ? 496 ILE A CG2 1 
ATOM   2117 C  CD1 . ILE A 1 296 ? 101.607 118.870 76.459  1.00 20.38  ? 496 ILE A CD1 1 
ATOM   2118 N  N   . THR A 1 297 ? 100.138 122.512 79.399  1.00 18.16  ? 497 THR A N   1 
ATOM   2119 C  CA  . THR A 1 297 ? 100.192 123.651 80.304  1.00 18.16  ? 497 THR A CA  1 
ATOM   2120 C  C   . THR A 1 297 ? 101.557 123.860 80.938  1.00 18.16  ? 497 THR A C   1 
ATOM   2121 O  O   . THR A 1 297 ? 101.803 124.941 81.485  1.00 18.16  ? 497 THR A O   1 
ATOM   2122 C  CB  . THR A 1 297 ? 99.164  123.496 81.436  1.00 18.16  ? 497 THR A CB  1 
ATOM   2123 O  OG1 . THR A 1 297 ? 99.510  122.361 82.235  1.00 18.16  ? 497 THR A OG1 1 
ATOM   2124 C  CG2 . THR A 1 297 ? 97.766  123.279 80.871  1.00 18.16  ? 497 THR A CG2 1 
ATOM   2125 N  N   . GLU A 1 298 ? 102.439 122.865 80.885  1.00 22.75  ? 498 GLU A N   1 
ATOM   2126 C  CA  . GLU A 1 298 ? 103.739 122.964 81.535  1.00 22.75  ? 498 GLU A CA  1 
ATOM   2127 C  C   . GLU A 1 298 ? 104.625 123.942 80.775  1.00 22.75  ? 498 GLU A C   1 
ATOM   2128 O  O   . GLU A 1 298 ? 104.725 123.876 79.545  1.00 22.75  ? 498 GLU A O   1 
ATOM   2129 C  CB  . GLU A 1 298 ? 104.400 121.586 81.606  1.00 22.75  ? 498 GLU A CB  1 
ATOM   2130 C  CG  . GLU A 1 298 ? 104.100 120.838 82.896  1.00 22.75  ? 498 GLU A CG  1 
ATOM   2131 C  CD  . GLU A 1 298 ? 104.730 121.485 84.111  1.00 22.75  ? 498 GLU A CD  1 
ATOM   2132 O  OE1 . GLU A 1 298 ? 105.892 121.157 84.432  1.00 22.75  ? 498 GLU A OE1 1 
ATOM   2133 O  OE2 . GLU A 1 298 ? 104.062 122.327 84.746  1.00 22.75  ? 498 GLU A OE2 1 
ATOM   2134 N  N   . GLY A 1 299 ? 105.261 124.856 81.506  1.00 20.25  ? 499 GLY A N   1 
ATOM   2135 C  CA  . GLY A 1 299 ? 106.106 125.862 80.900  1.00 20.25  ? 499 GLY A CA  1 
ATOM   2136 C  C   . GLY A 1 299 ? 105.380 127.065 80.340  1.00 20.25  ? 499 GLY A C   1 
ATOM   2137 O  O   . GLY A 1 299 ? 106.036 127.958 79.788  1.00 20.25  ? 499 GLY A O   1 
ATOM   2138 N  N   . ASN A 1 300 ? 104.055 127.126 80.465  1.00 16.79  ? 500 ASN A N   1 
ATOM   2139 C  CA  . ASN A 1 300 ? 103.261 128.250 79.971  1.00 16.79  ? 500 ASN A CA  1 
ATOM   2140 C  C   . ASN A 1 300 ? 102.915 129.139 81.162  1.00 16.79  ? 500 ASN A C   1 
ATOM   2141 O  O   . ASN A 1 300 ? 101.836 129.037 81.745  1.00 16.79  ? 500 ASN A O   1 
ATOM   2142 C  CB  . ASN A 1 300 ? 102.008 127.759 79.256  1.00 16.79  ? 500 ASN A CB  1 
ATOM   2143 C  CG  . ASN A 1 300 ? 102.318 127.036 77.962  1.00 16.79  ? 500 ASN A CG  1 
ATOM   2144 O  OD1 . ASN A 1 300 ? 103.383 127.215 77.371  1.00 16.79  ? 500 ASN A OD1 1 
ATOM   2145 N  ND2 . ASN A 1 300 ? 101.371 126.228 77.503  1.00 16.79  ? 500 ASN A ND2 1 
ATOM   2146 N  N   . SER A 1 301 ? 103.835 130.033 81.511  1.00 15.86  ? 501 SER A N   1 
ATOM   2147 C  CA  . SER A 1 301 ? 103.698 130.860 82.703  1.00 15.86  ? 501 SER A CA  1 
ATOM   2148 C  C   . SER A 1 301 ? 102.821 132.074 82.419  1.00 15.86  ? 501 SER A C   1 
ATOM   2149 O  O   . SER A 1 301 ? 103.001 132.756 81.405  1.00 15.86  ? 501 SER A O   1 
ATOM   2150 C  CB  . SER A 1 301 ? 105.072 131.308 83.199  1.00 15.86  ? 501 SER A CB  1 
ATOM   2151 O  OG  . SER A 1 301 ? 104.961 132.038 84.408  1.00 15.86  ? 501 SER A OG  1 
ATOM   2152 N  N   . TRP A 1 302 ? 101.773 132.300 83.240  1.00 16.04  ? 502 TRP A N   1 
ATOM   2153 C  CA  . TRP A 1 302 ? 100.940 133.548 83.192  1.00 16.04  ? 502 TRP A CA  1 
ATOM   2154 C  C   . TRP A 1 302 ? 101.759 134.806 83.586  1.00 16.04  ? 502 TRP A C   1 
ATOM   2155 O  O   . TRP A 1 302 ? 101.404 135.846 83.064  1.00 16.04  ? 502 TRP A O   1 
ATOM   2156 C  CB  . TRP A 1 302 ? 99.620  133.475 84.025  1.00 30.00  ? 502 TRP A CB  1 
ATOM   2157 C  CG  . TRP A 1 302 ? 98.428  132.906 83.326  1.00 30.00  ? 502 TRP A CG  1 
ATOM   2158 C  CD1 . TRP A 1 302 ? 97.823  131.718 83.594  1.00 30.00  ? 502 TRP A CD1 1 
ATOM   2159 C  CD2 . TRP A 1 302 ? 97.670  133.518 82.271  1.00 30.00  ? 502 TRP A CD2 1 
ATOM   2160 N  NE1 . TRP A 1 302 ? 96.760  131.537 82.763  1.00 30.00  ? 502 TRP A NE1 1 
ATOM   2161 C  CE2 . TRP A 1 302 ? 96.646  132.614 81.933  1.00 30.00  ? 502 TRP A CE2 1 
ATOM   2162 C  CE3 . TRP A 1 302 ? 97.773  134.715 81.556  1.00 30.00  ? 502 TRP A CE3 1 
ATOM   2163 C  CZ2 . TRP A 1 302 ? 95.720  132.878 80.928  1.00 30.00  ? 502 TRP A CZ2 1 
ATOM   2164 C  CZ3 . TRP A 1 302 ? 96.854  134.978 80.570  1.00 30.00  ? 502 TRP A CZ3 1 
ATOM   2165 C  CH2 . TRP A 1 302 ? 95.848  134.067 80.254  1.00 30.00  ? 502 TRP A CH2 1 
ATOM   2166 N  N   . SER A 1 303 ? 102.845 134.681 84.390  1.00 16.70  ? 503 SER A N   1 
ATOM   2167 C  CA  . SER A 1 303 ? 103.630 135.849 84.780  1.00 16.70  ? 503 SER A CA  1 
ATOM   2168 C  C   . SER A 1 303 ? 104.360 136.476 83.601  1.00 16.70  ? 503 SER A C   1 
ATOM   2169 O  O   . SER A 1 303 ? 104.716 137.659 83.664  1.00 16.70  ? 503 SER A O   1 
ATOM   2170 C  CB  . SER A 1 303 ? 104.633 135.467 85.869  1.00 16.70  ? 503 SER A CB  1 
ATOM   2171 O  OG  . SER A 1 303 ? 103.974 134.965 87.018  1.00 16.70  ? 503 SER A OG  1 
ATOM   2172 N  N   . ASN A 1 304 ? 104.594 135.716 82.530  1.00 17.39  ? 504 ASN A N   1 
ATOM   2173 C  CA  . ASN A 1 304 ? 105.256 136.259 81.350  1.00 17.39  ? 504 ASN A CA  1 
ATOM   2174 C  C   . ASN A 1 304 ? 104.397 137.283 80.620  1.00 17.39  ? 504 ASN A C   1 
ATOM   2175 O  O   . ASN A 1 304 ? 104.925 138.037 79.795  1.00 17.39  ? 504 ASN A O   1 
ATOM   2176 C  CB  . ASN A 1 304 ? 105.634 135.127 80.394  1.00 17.39  ? 504 ASN A CB  1 
ATOM   2177 C  CG  . ASN A 1 304 ? 106.681 134.198 80.976  1.00 17.39  ? 504 ASN A CG  1 
ATOM   2178 O  OD1 . ASN A 1 304 ? 107.170 134.411 82.084  1.00 17.39  ? 504 ASN A OD1 1 
ATOM   2179 N  ND2 . ASN A 1 304 ? 107.026 133.156 80.229  1.00 17.39  ? 504 ASN A ND2 1 
ATOM   2180 N  N   . TYR A 1 305 ? 103.094 137.330 80.901  1.00 19.59  ? 505 TYR A N   1 
ATOM   2181 C  CA  . TYR A 1 305 ? 102.180 138.215 80.197  1.00 19.59  ? 505 TYR A CA  1 
ATOM   2182 C  C   . TYR A 1 305 ? 101.487 139.236 81.085  1.00 19.59  ? 505 TYR A C   1 
ATOM   2183 O  O   . TYR A 1 305 ? 100.786 140.105 80.555  1.00 19.59  ? 505 TYR A O   1 
ATOM   2184 C  CB  . TYR A 1 305 ? 101.103 137.400 79.462  1.00 19.59  ? 505 TYR A CB  1 
ATOM   2185 C  CG  . TYR A 1 305 ? 101.637 136.524 78.353  1.00 19.59  ? 505 TYR A CG  1 
ATOM   2186 C  CD1 . TYR A 1 305 ? 102.143 135.258 78.624  1.00 19.59  ? 505 TYR A CD1 1 
ATOM   2187 C  CD2 . TYR A 1 305 ? 101.633 136.959 77.035  1.00 19.59  ? 505 TYR A CD2 1 
ATOM   2188 C  CE1 . TYR A 1 305 ? 102.631 134.454 77.614  1.00 19.59  ? 505 TYR A CE1 1 
ATOM   2189 C  CE2 . TYR A 1 305 ? 102.118 136.161 76.019  1.00 19.59  ? 505 TYR A CE2 1 
ATOM   2190 C  CZ  . TYR A 1 305 ? 102.617 134.911 76.314  1.00 19.59  ? 505 TYR A CZ  1 
ATOM   2191 N  N   . ILE A 1 306 ? 101.652 139.160 82.408  1.00 19.74  ? 506 ILE A N   1 
ATOM   2192 C  CA  . ILE A 1 306 ? 100.895 140.031 83.308  1.00 19.74  ? 506 ILE A CA  1 
ATOM   2193 C  C   . ILE A 1 306 ? 101.274 141.490 83.087  1.00 19.74  ? 506 ILE A C   1 
ATOM   2194 O  O   . ILE A 1 306 ? 100.407 142.361 82.931  1.00 19.74  ? 506 ILE A O   1 
ATOM   2195 C  CB  . ILE A 1 306 ? 101.114 139.604 84.771  1.00 19.74  ? 506 ILE A CB  1 
ATOM   2196 C  CG1 . ILE A 1 306 ? 100.268 138.374 85.101  1.00 19.74  ? 506 ILE A CG1 1 
ATOM   2197 C  CG2 . ILE A 1 306 ? 100.783 140.745 85.721  1.00 19.74  ? 506 ILE A CG2 1 
ATOM   2198 C  CD1 . ILE A 1 306 ? 100.682 137.674 86.376  1.00 19.74  ? 506 ILE A CD1 1 
ATOM   2199 N  N   . SER A 1 307 ? 102.578 141.779 83.069  1.00 20.60  ? 507 SER A N   1 
ATOM   2200 C  CA  . SER A 1 307 ? 103.031 143.156 82.896  1.00 20.60  ? 507 SER A CA  1 
ATOM   2201 C  C   . SER A 1 307 ? 102.642 143.698 81.527  1.00 20.60  ? 507 SER A C   1 
ATOM   2202 O  O   . SER A 1 307 ? 102.207 144.850 81.408  1.00 20.60  ? 507 SER A O   1 
ATOM   2203 C  CB  . SER A 1 307 ? 104.544 143.238 83.098  1.00 20.60  ? 507 SER A CB  1 
ATOM   2204 O  OG  . SER A 1 307 ? 104.879 143.188 84.473  1.00 20.60  ? 507 SER A OG  1 
ATOM   2205 N  N   . GLN A 1 308 ? 102.794 142.884 80.481  1.00 21.83  ? 508 GLN A N   1 
ATOM   2206 C  CA  . GLN A 1 308 ? 102.444 143.331 79.137  1.00 21.83  ? 508 GLN A CA  1 
ATOM   2207 C  C   . GLN A 1 308 ? 100.952 143.609 79.015  1.00 21.83  ? 508 GLN A C   1 
ATOM   2208 O  O   . GLN A 1 308 ? 100.548 144.597 78.389  1.00 21.83  ? 508 GLN A O   1 
ATOM   2209 C  CB  . GLN A 1 308 ? 102.890 142.293 78.107  1.00 21.83  ? 508 GLN A CB  1 
ATOM   2210 C  CG  . GLN A 1 308 ? 102.342 142.526 76.709  1.00 21.83  ? 508 GLN A CG  1 
ATOM   2211 C  CD  . GLN A 1 308 ? 102.946 141.589 75.683  1.00 21.83  ? 508 GLN A CD  1 
ATOM   2212 O  OE1 . GLN A 1 308 ? 104.014 141.857 75.133  1.00 21.83  ? 508 GLN A OE1 1 
ATOM   2213 N  NE2 . GLN A 1 308 ? 102.265 140.479 75.421  1.00 21.83  ? 508 GLN A NE2 1 
ATOM   2214 N  N   . ILE A 1 309 ? 100.114 142.751 79.605  1.00 21.76  ? 509 ILE A N   1 
ATOM   2215 C  CA  . ILE A 1 309 ? 98.671  142.971 79.560  1.00 21.76  ? 509 ILE A CA  1 
ATOM   2216 C  C   . ILE A 1 309 ? 98.299  144.232 80.328  1.00 21.76  ? 509 ILE A C   1 
ATOM   2217 O  O   . ILE A 1 309 ? 97.502  145.052 79.853  1.00 21.76  ? 509 ILE A O   1 
ATOM   2218 C  CB  . ILE A 1 309 ? 97.928  141.735 80.101  1.00 21.76  ? 509 ILE A CB  1 
ATOM   2219 C  CG1 . ILE A 1 309 ? 97.906  140.624 79.049  1.00 21.76  ? 509 ILE A CG1 1 
ATOM   2220 C  CG2 . ILE A 1 309 ? 96.511  142.097 80.522  1.00 21.76  ? 509 ILE A CG2 1 
ATOM   2221 C  CD1 . ILE A 1 309 ? 97.663  139.246 79.622  1.00 21.76  ? 509 ILE A CD1 1 
ATOM   2222 N  N   . ASP A 1 310 ? 98.875  144.419 81.519  1.00 22.93  ? 510 ASP A N   1 
ATOM   2223 C  CA  . ASP A 1 310 ? 98.546  145.595 82.316  1.00 22.93  ? 510 ASP A CA  1 
ATOM   2224 C  C   . ASP A 1 310 ? 99.062  146.879 81.676  1.00 22.93  ? 510 ASP A C   1 
ATOM   2225 O  O   . ASP A 1 310 ? 98.506  147.956 81.918  1.00 22.93  ? 510 ASP A O   1 
ATOM   2226 C  CB  . ASP A 1 310 ? 99.110  145.447 83.729  1.00 22.93  ? 510 ASP A CB  1 
ATOM   2227 C  CG  . ASP A 1 310 ? 98.279  144.517 84.592  1.00 22.93  ? 510 ASP A CG  1 
ATOM   2228 O  OD1 . ASP A 1 310 ? 97.105  144.272 84.245  1.00 22.93  ? 510 ASP A OD1 1 
ATOM   2229 O  OD2 . ASP A 1 310 ? 98.801  144.032 85.618  1.00 22.93  ? 510 ASP A OD2 1 
ATOM   2230 N  N   . SER A 1 311 ? 100.113 146.788 80.860  1.00 24.02  ? 511 SER A N   1 
ATOM   2231 C  CA  . SER A 1 311 ? 100.711 147.985 80.277  1.00 24.02  ? 511 SER A CA  1 
ATOM   2232 C  C   . SER A 1 311 ? 99.893  148.550 79.120  1.00 24.02  ? 511 SER A C   1 
ATOM   2233 O  O   . SER A 1 311 ? 99.883  149.769 78.917  1.00 24.02  ? 511 SER A O   1 
ATOM   2234 C  CB  . SER A 1 311 ? 102.134 147.681 79.806  1.00 24.02  ? 511 SER A CB  1 
ATOM   2235 O  OG  . SER A 1 311 ? 102.528 148.562 78.769  1.00 24.02  ? 511 SER A OG  1 
ATOM   2236 N  N   . VAL A 1 312 ? 99.210  147.698 78.355  1.00 24.36  ? 512 VAL A N   1 
ATOM   2237 C  CA  . VAL A 1 312 ? 98.544  148.126 77.128  1.00 24.36  ? 512 VAL A CA  1 
ATOM   2238 C  C   . VAL A 1 312 ? 97.025  148.107 77.256  1.00 24.36  ? 512 VAL A C   1 
ATOM   2239 O  O   . VAL A 1 312 ? 96.323  148.269 76.253  1.00 24.36  ? 512 VAL A O   1 
ATOM   2240 C  CB  . VAL A 1 312 ? 98.995  147.273 75.932  1.00 24.36  ? 512 VAL A CB  1 
ATOM   2241 C  CG1 . VAL A 1 312 ? 100.508 147.281 75.816  1.00 24.36  ? 512 VAL A CG1 1 
ATOM   2242 C  CG2 . VAL A 1 312 ? 98.474  145.849 76.066  1.00 24.36  ? 512 VAL A CG2 1 
ATOM   2243 N  N   . SER A 1 313 ? 96.495  147.923 78.462  1.00 26.32  ? 513 SER A N   1 
ATOM   2244 C  CA  . SER A 1 313 ? 95.059  147.772 78.650  1.00 26.32  ? 513 SER A CA  1 
ATOM   2245 C  C   . SER A 1 313 ? 94.565  148.745 79.715  1.00 26.32  ? 513 SER A C   1 
ATOM   2246 O  O   . SER A 1 313 ? 95.343  149.349 80.459  1.00 26.32  ? 513 SER A O   1 
ATOM   2247 C  CB  . SER A 1 313 ? 94.700  146.331 79.030  1.00 26.32  ? 513 SER A CB  1 
ATOM   2248 O  OG  . SER A 1 313 ? 94.797  145.467 77.912  1.00 26.32  ? 513 SER A OG  1 
ATOM   2249 N  N   . ALA A 1 314 ? 93.243  148.888 79.772  1.00 28.06  ? 514 ALA A N   1 
ATOM   2250 C  CA  . ALA A 1 314 ? 92.547  149.635 80.806  1.00 28.06  ? 514 ALA A CA  1 
ATOM   2251 C  C   . ALA A 1 314 ? 91.675  148.673 81.597  1.00 28.06  ? 514 ALA A C   1 
ATOM   2252 O  O   . ALA A 1 314 ? 91.128  147.714 81.038  1.00 28.06  ? 514 ALA A O   1 
ATOM   2253 C  CB  . ALA A 1 314 ? 91.694  150.757 80.208  1.00 28.06  ? 514 ALA A CB  1 
ATOM   2254 N  N   . SER A 1 315 ? 91.552  148.930 82.897  1.00 30.16  ? 515 SER A N   1 
ATOM   2255 C  CA  . SER A 1 315 ? 90.881  148.027 83.822  1.00 30.16  ? 515 SER A CA  1 
ATOM   2256 C  C   . SER A 1 315 ? 89.444  148.477 84.057  1.00 30.16  ? 515 SER A C   1 
ATOM   2257 O  O   . SER A 1 315 ? 89.195  149.649 84.367  1.00 30.16  ? 515 SER A O   1 
ATOM   2258 C  CB  . SER A 1 315 ? 91.633  147.960 85.151  1.00 30.16  ? 515 SER A CB  1 
ATOM   2259 O  OG  . SER A 1 315 ? 93.035  147.940 84.942  1.00 30.16  ? 515 SER A OG  1 
ATOM   2260 N  N   . ILE A 1 316 ? 88.507  147.542 83.905  1.00 30.26  ? 516 ILE A N   1 
ATOM   2261 C  CA  . ILE A 1 316 ? 87.094  147.777 84.177  1.00 30.26  ? 516 ILE A CA  1 
ATOM   2262 C  C   . ILE A 1 316 ? 86.610  146.708 85.144  1.00 30.26  ? 516 ILE A C   1 
ATOM   2263 O  O   . ILE A 1 316 ? 86.738  145.510 84.868  1.00 30.26  ? 516 ILE A O   1 
ATOM   2264 C  CB  . ILE A 1 316 ? 86.248  147.765 82.889  1.00 30.26  ? 516 ILE A CB  1 
ATOM   2265 C  CG1 . ILE A 1 316 ? 86.863  148.685 81.832  1.00 30.26  ? 516 ILE A CG1 1 
ATOM   2266 C  CG2 . ILE A 1 316 ? 84.818  148.179 83.190  1.00 30.26  ? 516 ILE A CG2 1 
ATOM   2267 C  CD1 . ILE A 1 316 ? 86.233  148.545 80.464  1.00 30.26  ? 516 ILE A CD1 1 
ATOM   2268 N  N   . ILE A 1 317 ? 86.045  147.137 86.267  1.00 33.21  ? 517 ILE A N   1 
ATOM   2269 C  CA  . ILE A 1 317 ? 85.532  146.233 87.290  1.00 33.21  ? 517 ILE A CA  1 
ATOM   2270 C  C   . ILE A 1 317 ? 84.033  146.458 87.410  1.00 33.21  ? 517 ILE A C   1 
ATOM   2271 O  O   . ILE A 1 317 ? 83.571  147.602 87.372  1.00 33.21  ? 517 ILE A O   1 
ATOM   2272 C  CB  . ILE A 1 317 ? 86.234  146.449 88.644  1.00 33.21  ? 517 ILE A CB  1 
ATOM   2273 C  CG1 . ILE A 1 317 ? 87.750  146.314 88.484  1.00 33.21  ? 517 ILE A CG1 1 
ATOM   2274 C  CG2 . ILE A 1 317 ? 85.717  145.464 89.681  1.00 33.21  ? 517 ILE A CG2 1 
ATOM   2275 C  CD1 . ILE A 1 317 ? 88.510  146.356 89.792  1.00 33.21  ? 517 ILE A CD1 1 
ATOM   2276 N  N   . LEU A 1 318 ? 83.279  145.369 87.515  1.00 38.29  ? 518 LEU A N   1 
ATOM   2277 C  CA  . LEU A 1 318 ? 81.837  145.402 87.722  1.00 38.29  ? 518 LEU A CA  1 
ATOM   2278 C  C   . LEU A 1 318 ? 81.503  144.706 89.032  1.00 38.29  ? 518 LEU A C   1 
ATOM   2279 O  O   . LEU A 1 318 ? 81.941  143.572 89.266  1.00 38.29  ? 518 LEU A O   1 
ATOM   2280 C  CB  . LEU A 1 318 ? 81.097  144.735 86.562  1.00 38.29  ? 518 LEU A CB  1 
ATOM   2281 C  CG  . LEU A 1 318 ? 79.583  144.556 86.700  1.00 38.29  ? 518 LEU A CG  1 
ATOM   2282 C  CD1 . LEU A 1 318 ? 78.902  145.878 86.999  1.00 38.29  ? 518 LEU A CD1 1 
ATOM   2283 C  CD2 . LEU A 1 318 ? 79.008  143.938 85.436  1.00 38.29  ? 518 LEU A CD2 1 
ATOM   2284 N  N   . ASP A 1 319 ? 80.729  145.381 89.881  1.00 47.95  ? 519 ASP A N   1 
ATOM   2285 C  CA  . ASP A 1 319 ? 80.334  144.862 91.188  1.00 47.95  ? 519 ASP A CA  1 
ATOM   2286 C  C   . ASP A 1 319 ? 78.813  144.934 91.292  1.00 47.95  ? 519 ASP A C   1 
ATOM   2287 O  O   . ASP A 1 319 ? 78.246  146.015 91.483  1.00 47.95  ? 519 ASP A O   1 
ATOM   2288 C  CB  . ASP A 1 319 ? 81.003  145.643 92.313  1.00 47.95  ? 519 ASP A CB  1 
ATOM   2289 C  CG  . ASP A 1 319 ? 80.856  144.965 93.659  1.00 47.95  ? 519 ASP A CG  1 
ATOM   2290 O  OD1 . ASP A 1 319 ? 81.438  143.878 93.845  1.00 47.95  ? 519 ASP A OD1 1 
ATOM   2291 O  OD2 . ASP A 1 319 ? 80.154  145.523 94.531  1.00 47.95  ? 519 ASP A OD2 1 
ATOM   2292 N  N   . THR A 1 320 ? 78.164  143.778 91.177  1.00 50.20  ? 520 THR A N   1 
ATOM   2293 C  CA  . THR A 1 320 ? 76.715  143.669 91.284  1.00 50.20  ? 520 THR A CA  1 
ATOM   2294 C  C   . THR A 1 320 ? 76.247  143.457 92.718  1.00 50.20  ? 520 THR A C   1 
ATOM   2295 O  O   . THR A 1 320 ? 75.099  143.053 92.928  1.00 50.20  ? 520 THR A O   1 
ATOM   2296 C  CB  . THR A 1 320 ? 76.207  142.526 90.401  1.00 50.20  ? 520 THR A CB  1 
ATOM   2297 O  OG1 . THR A 1 320 ? 76.483  141.271 91.036  1.00 50.20  ? 520 THR A OG1 1 
ATOM   2298 C  CG2 . THR A 1 320 ? 76.890  142.559 89.042  1.00 50.20  ? 520 THR A CG2 1 
ATOM   2299 N  N   . GLY A 1 321 ? 77.097  143.715 93.695  1.00 51.36  ? 521 GLY A N   1 
ATOM   2300 C  CA  . GLY A 1 321 ? 76.752  143.517 95.099  1.00 51.36  ? 521 GLY A CA  1 
ATOM   2301 C  C   . GLY A 1 321 ? 77.136  142.169 95.671  1.00 51.36  ? 521 GLY A C   1 
ATOM   2302 O  O   . GLY A 1 321 ? 77.629  142.088 96.795  1.00 51.36  ? 521 GLY A O   1 
ATOM   2303 N  N   . SER A 1 322 ? 76.910  141.101 94.909  1.00 49.63  ? 522 SER A N   1 
ATOM   2304 C  CA  . SER A 1 322 ? 77.261  139.755 95.344  1.00 49.63  ? 522 SER A CA  1 
ATOM   2305 C  C   . SER A 1 322 ? 78.477  139.188 94.627  1.00 49.63  ? 522 SER A C   1 
ATOM   2306 O  O   . SER A 1 322 ? 79.194  138.366 95.207  1.00 49.63  ? 522 SER A O   1 
ATOM   2307 C  CB  . SER A 1 322 ? 76.077  138.804 95.143  1.00 49.63  ? 522 SER A CB  1 
ATOM   2308 O  OG  . SER A 1 322 ? 75.413  139.064 93.920  1.00 49.63  ? 522 SER A OG  1 
ATOM   2309 N  N   . GLN A 1 323 ? 78.726  139.601 93.389  1.00 42.75  ? 523 GLN A N   1 
ATOM   2310 C  CA  . GLN A 1 323 ? 79.836  139.100 92.594  1.00 42.75  ? 523 GLN A CA  1 
ATOM   2311 C  C   . GLN A 1 323 ? 80.674  140.263 92.074  1.00 42.75  ? 523 GLN A C   1 
ATOM   2312 O  O   . GLN A 1 323 ? 80.254  141.424 92.093  1.00 42.75  ? 523 GLN A O   1 
ATOM   2313 C  CB  . GLN A 1 323 ? 79.335  138.239 91.428  1.00 42.75  ? 523 GLN A CB  1 
ATOM   2314 C  CG  . GLN A 1 323 ? 79.337  136.747 91.716  1.00 42.75  ? 523 GLN A CG  1 
ATOM   2315 C  CD  . GLN A 1 323 ? 78.707  135.938 90.602  1.00 42.75  ? 523 GLN A CD  1 
ATOM   2316 O  OE1 . GLN A 1 323 ? 77.542  136.138 90.255  1.00 42.75  ? 523 GLN A OE1 1 
ATOM   2317 N  NE2 . GLN A 1 323 ? 79.475  135.015 90.032  1.00 42.75  ? 523 GLN A NE2 1 
ATOM   2318 N  N   . THR A 1 324 ? 81.875  139.933 91.604  1.00 34.84  ? 524 THR A N   1 
ATOM   2319 C  CA  . THR A 1 324 ? 82.809  140.915 91.075  1.00 34.84  ? 524 THR A CA  1 
ATOM   2320 C  C   . THR A 1 324 ? 83.459  140.357 89.818  1.00 34.84  ? 524 THR A C   1 
ATOM   2321 O  O   . THR A 1 324 ? 83.880  139.196 89.793  1.00 34.84  ? 524 THR A O   1 
ATOM   2322 C  CB  . THR A 1 324 ? 83.879  141.282 92.117  1.00 34.84  ? 524 THR A CB  1 
ATOM   2323 O  OG1 . THR A 1 324 ? 83.346  142.248 93.032  1.00 34.84  ? 524 THR A OG1 1 
ATOM   2324 C  CG2 . THR A 1 324 ? 85.121  141.858 91.451  1.00 34.84  ? 524 THR A CG2 1 
ATOM   2325 N  N   . PHE A 1 325 ? 83.529  141.182 88.775  1.00 31.86  ? 525 PHE A N   1 
ATOM   2326 C  CA  . PHE A 1 325 ? 84.121  140.790 87.501  1.00 31.86  ? 525 PHE A CA  1 
ATOM   2327 C  C   . PHE A 1 325 ? 85.156  141.825 87.089  1.00 31.86  ? 525 PHE A C   1 
ATOM   2328 O  O   . PHE A 1 325 ? 84.858  143.021 87.051  1.00 31.86  ? 525 PHE A O   1 
ATOM   2329 C  CB  . PHE A 1 325 ? 83.050  140.646 86.413  1.00 31.86  ? 525 PHE A CB  1 
ATOM   2330 C  CG  . PHE A 1 325 ? 81.885  139.787 86.818  1.00 31.86  ? 525 PHE A CG  1 
ATOM   2331 C  CD1 . PHE A 1 325 ? 80.802  140.332 87.490  1.00 31.86  ? 525 PHE A CD1 1 
ATOM   2332 C  CD2 . PHE A 1 325 ? 81.874  138.434 86.527  1.00 31.86  ? 525 PHE A CD2 1 
ATOM   2333 C  CE1 . PHE A 1 325 ? 79.733  139.542 87.865  1.00 31.86  ? 525 PHE A CE1 1 
ATOM   2334 C  CE2 . PHE A 1 325 ? 80.806  137.638 86.898  1.00 31.86  ? 525 PHE A CE2 1 
ATOM   2335 C  CZ  . PHE A 1 325 ? 79.735  138.194 87.567  1.00 31.86  ? 525 PHE A CZ  1 
ATOM   2336 N  N   . GLU A 1 326 ? 86.366  141.367 86.774  1.00 25.41  ? 526 GLU A N   1 
ATOM   2337 C  CA  . GLU A 1 326 ? 87.470  142.242 86.402  1.00 25.41  ? 526 GLU A CA  1 
ATOM   2338 C  C   . GLU A 1 326 ? 87.867  141.964 84.959  1.00 25.41  ? 526 GLU A C   1 
ATOM   2339 O  O   . GLU A 1 326 ? 88.023  140.803 84.569  1.00 25.41  ? 526 GLU A O   1 
ATOM   2340 C  CB  . GLU A 1 326 ? 88.666  142.038 87.338  1.00 25.41  ? 526 GLU A CB  1 
ATOM   2341 C  CG  . GLU A 1 326 ? 89.787  143.043 87.148  1.00 25.41  ? 526 GLU A CG  1 
ATOM   2342 C  CD  . GLU A 1 326 ? 90.497  143.370 88.447  1.00 25.41  ? 526 GLU A CD  1 
ATOM   2343 O  OE1 . GLU A 1 326 ? 90.052  142.884 89.507  1.00 25.41  ? 526 GLU A OE1 1 
ATOM   2344 O  OE2 . GLU A 1 326 ? 91.499  144.113 88.407  1.00 25.41  ? 526 GLU A OE2 1 
ATOM   2345 N  N   . ARG A 1 327 ? 88.032  143.028 84.171  1.00 25.04  ? 527 ARG A N   1 
ATOM   2346 C  CA  . ARG A 1 327 ? 88.320  142.910 82.751  1.00 25.04  ? 527 ARG A CA  1 
ATOM   2347 C  C   . ARG A 1 327 ? 89.404  143.902 82.352  1.00 25.04  ? 527 ARG A C   1 
ATOM   2348 O  O   . ARG A 1 327 ? 89.534  144.986 82.929  1.00 25.04  ? 527 ARG A O   1 
ATOM   2349 C  CB  . ARG A 1 327 ? 87.064  143.160 81.901  1.00 25.04  ? 527 ARG A CB  1 
ATOM   2350 C  CG  . ARG A 1 327 ? 85.876  142.280 82.249  1.00 25.04  ? 527 ARG A CG  1 
ATOM   2351 C  CD  . ARG A 1 327 ? 86.000  140.912 81.610  1.00 25.04  ? 527 ARG A CD  1 
ATOM   2352 N  NE  . ARG A 1 327 ? 84.929  140.015 82.025  1.00 25.04  ? 527 ARG A NE  1 
ATOM   2353 C  CZ  . ARG A 1 327 ? 84.954  139.272 83.124  1.00 25.04  ? 527 ARG A CZ  1 
ATOM   2354 N  N   . ARG A 1 328 ? 90.177  143.515 81.337  1.00 24.18  ? 528 ARG A N   1 
ATOM   2355 C  CA  . ARG A 1 328 ? 91.185  144.369 80.726  1.00 24.18  ? 528 ARG A CA  1 
ATOM   2356 C  C   . ARG A 1 328 ? 90.828  144.563 79.260  1.00 24.18  ? 528 ARG A C   1 
ATOM   2357 O  O   . ARG A 1 328 ? 90.618  143.584 78.538  1.00 24.18  ? 528 ARG A O   1 
ATOM   2358 C  CB  . ARG A 1 328 ? 92.586  143.759 80.852  1.00 24.18  ? 528 ARG A CB  1 
ATOM   2359 C  CG  . ARG A 1 328 ? 93.068  143.568 82.281  1.00 24.18  ? 528 ARG A CG  1 
ATOM   2360 C  CD  . ARG A 1 328 ? 93.481  144.888 82.907  1.00 24.18  ? 528 ARG A CD  1 
ATOM   2361 N  NE  . ARG A 1 328 ? 94.104  144.698 84.212  1.00 24.18  ? 528 ARG A NE  1 
ATOM   2362 C  CZ  . ARG A 1 328 ? 93.433  144.566 85.349  1.00 24.18  ? 528 ARG A CZ  1 
ATOM   2363 N  N   . VAL A 1 329 ? 90.761  145.818 78.824  1.00 25.10  ? 529 VAL A N   1 
ATOM   2364 C  CA  . VAL A 1 329 ? 90.389  146.155 77.453  1.00 25.10  ? 529 VAL A CA  1 
ATOM   2365 C  C   . VAL A 1 329 ? 91.538  146.919 76.811  1.00 25.10  ? 529 VAL A C   1 
ATOM   2366 O  O   . VAL A 1 329 ? 92.022  147.907 77.373  1.00 25.10  ? 529 VAL A O   1 
ATOM   2367 C  CB  . VAL A 1 329 ? 89.087  146.977 77.399  1.00 25.10  ? 529 VAL A CB  1 
ATOM   2368 C  CG1 . VAL A 1 329 ? 88.703  147.264 75.956  1.00 25.10  ? 529 VAL A CG1 1 
ATOM   2369 C  CG2 . VAL A 1 329 ? 87.967  146.239 78.113  1.00 25.10  ? 529 VAL A CG2 1 
ATOM   2370 N  N   . ALA A 1 330 ? 91.971  146.462 75.638  1.00 26.75  ? 530 ALA A N   1 
ATOM   2371 C  CA  . ALA A 1 330 ? 93.124  147.059 74.976  1.00 26.75  ? 530 ALA A CA  1 
ATOM   2372 C  C   . ALA A 1 330 ? 92.794  148.447 74.436  1.00 26.75  ? 530 ALA A C   1 
ATOM   2373 O  O   . ALA A 1 330 ? 91.690  148.698 73.946  1.00 26.75  ? 530 ALA A O   1 
ATOM   2374 C  CB  . ALA A 1 330 ? 93.608  146.158 73.841  1.00 26.75  ? 530 ALA A CB  1 
ATOM   2375 N  N   . ALA A 1 331 ? 93.771  149.349 74.527  1.00 30.38  ? 531 ALA A N   1 
ATOM   2376 C  CA  . ALA A 1 331 ? 93.655  150.695 73.983  1.00 30.38  ? 531 ALA A CA  1 
ATOM   2377 C  C   . ALA A 1 331 ? 95.001  151.109 73.406  1.00 30.38  ? 531 ALA A C   1 
ATOM   2378 O  O   . ALA A 1 331 ? 96.050  150.582 73.785  1.00 30.38  ? 531 ALA A O   1 
ATOM   2379 C  CB  . ALA A 1 331 ? 93.189  151.700 75.043  1.00 30.38  ? 531 ALA A CB  1 
ATOM   2380 N  N   . LYS A 1 332 ? 94.964  152.066 72.482  1.00 36.09  ? 532 LYS A N   1 
ATOM   2381 C  CA  . LYS A 1 332 ? 96.171  152.445 71.764  1.00 36.09  ? 532 LYS A CA  1 
ATOM   2382 C  C   . LYS A 1 332 ? 97.005  153.433 72.578  1.00 36.09  ? 532 LYS A C   1 
ATOM   2383 O  O   . LYS A 1 332 ? 96.522  154.075 73.515  1.00 36.09  ? 532 LYS A O   1 
ATOM   2384 C  CB  . LYS A 1 332 ? 95.827  153.058 70.406  1.00 36.09  ? 532 LYS A CB  1 
ATOM   2385 C  CG  . LYS A 1 332 ? 95.360  154.499 70.459  1.00 36.09  ? 532 LYS A CG  1 
ATOM   2386 C  CD  . LYS A 1 332 ? 95.607  155.192 69.125  1.00 36.09  ? 532 LYS A CD  1 
ATOM   2387 C  CE  . LYS A 1 332 ? 97.036  155.012 68.642  1.00 36.09  ? 532 LYS A CE  1 
ATOM   2388 N  NZ  . LYS A 1 332 ? 97.478  156.144 67.783  1.00 36.09  ? 532 LYS A NZ  1 
ATOM   2389 N  N   . GLU A 1 333 ? 98.276  153.543 72.205  1.00 39.82  ? 533 GLU A N   1 
ATOM   2390 C  CA  . GLU A 1 333 ? 99.169  154.523 72.808  1.00 39.82  ? 533 GLU A CA  1 
ATOM   2391 C  C   . GLU A 1 333 ? 98.842  155.916 72.285  1.00 39.82  ? 533 GLU A C   1 
ATOM   2392 O  O   . GLU A 1 333 ? 98.524  156.094 71.107  1.00 39.82  ? 533 GLU A O   1 
ATOM   2393 C  CB  . GLU A 1 333 ? 100.625 154.172 72.506  1.00 39.82  ? 533 GLU A CB  1 
ATOM   2394 C  CG  . GLU A 1 333 ? 101.571 154.367 73.679  1.00 39.82  ? 533 GLU A CG  1 
ATOM   2395 C  CD  . GLU A 1 333 ? 103.013 154.532 73.240  1.00 39.82  ? 533 GLU A CD  1 
ATOM   2396 O  OE1 . GLU A 1 333 ? 103.606 153.542 72.763  1.00 39.82  ? 533 GLU A OE1 1 
ATOM   2397 O  OE2 . GLU A 1 333 ? 103.553 155.651 73.371  1.00 39.82  ? 533 GLU A OE2 1 
ATOM   2398 N  N   . GLN A 1 334 ? 98.930  156.909 73.171  1.00 45.32  ? 534 GLN A N   1 
ATOM   2399 C  CA  . GLN A 1 334 ? 98.497  158.259 72.818  1.00 45.32  ? 534 GLN A CA  1 
ATOM   2400 C  C   . GLN A 1 334 ? 99.356  158.856 71.707  1.00 45.32  ? 534 GLN A C   1 
ATOM   2401 O  O   . GLN A 1 334 ? 98.831  159.435 70.749  1.00 45.32  ? 534 GLN A O   1 
ATOM   2402 C  CB  . GLN A 1 334 ? 98.522  159.157 74.056  1.00 45.32  ? 534 GLN A CB  1 
ATOM   2403 C  CG  . GLN A 1 334 ? 97.171  159.317 74.736  1.00 45.32  ? 534 GLN A CG  1 
ATOM   2404 C  CD  . GLN A 1 334 ? 96.021  159.376 73.749  1.00 45.32  ? 534 GLN A CD  1 
ATOM   2405 O  OE1 . GLN A 1 334 ? 95.183  158.476 73.701  1.00 45.32  ? 534 GLN A OE1 1 
ATOM   2406 N  NE2 . GLN A 1 334 ? 95.972  160.443 72.960  1.00 45.32  ? 534 GLN A NE2 1 
ATOM   2407 N  N   . GLY A 1 335 ? 100.674 158.724 71.815  1.00 43.95  ? 535 GLY A N   1 
ATOM   2408 C  CA  . GLY A 1 335 ? 101.588 159.390 70.915  1.00 43.95  ? 535 GLY A CA  1 
ATOM   2409 C  C   . GLY A 1 335 ? 102.206 158.560 69.813  1.00 43.95  ? 535 GLY A C   1 
ATOM   2410 O  O   . GLY A 1 335 ? 102.966 159.105 69.008  1.00 43.95  ? 535 GLY A O   1 
ATOM   2411 N  N   . ASN A 1 336 ? 101.914 157.265 69.746  1.00 39.62  ? 536 ASN A N   1 
ATOM   2412 C  CA  . ASN A 1 336 ? 102.567 156.397 68.769  1.00 39.62  ? 536 ASN A CA  1 
ATOM   2413 C  C   . ASN A 1 336 ? 101.807 156.412 67.449  1.00 39.62  ? 536 ASN A C   1 
ATOM   2414 O  O   . ASN A 1 336 ? 100.640 156.006 67.415  1.00 39.62  ? 536 ASN A O   1 
ATOM   2415 C  CB  . ASN A 1 336 ? 102.660 154.974 69.302  1.00 39.62  ? 536 ASN A CB  1 
ATOM   2416 C  CG  . ASN A 1 336 ? 103.703 154.146 68.578  1.00 39.62  ? 536 ASN A CG  1 
ATOM   2417 O  OD1 . ASN A 1 336 ? 104.310 154.600 67.608  1.00 39.62  ? 536 ASN A OD1 1 
ATOM   2418 N  ND2 . ASN A 1 336 ? 103.918 152.923 69.048  1.00 39.62  ? 536 ASN A ND2 1 
ATOM   2419 N  N   . PRO A 1 337 ? 102.418 156.866 66.347  1.00 38.14  ? 537 PRO A N   1 
ATOM   2420 C  CA  . PRO A 1 337 ? 101.727 156.795 65.048  1.00 38.14  ? 537 PRO A CA  1 
ATOM   2421 C  C   . PRO A 1 337 ? 101.610 155.385 64.496  1.00 38.14  ? 537 PRO A C   1 
ATOM   2422 O  O   . PRO A 1 337 ? 100.748 155.147 63.640  1.00 38.14  ? 537 PRO A O   1 
ATOM   2423 C  CB  . PRO A 1 337 ? 102.597 157.659 64.119  1.00 38.14  ? 537 PRO A CB  1 
ATOM   2424 C  CG  . PRO A 1 337 ? 103.813 158.021 64.877  1.00 38.14  ? 537 PRO A CG  1 
ATOM   2425 C  CD  . PRO A 1 337 ? 103.642 157.680 66.313  1.00 38.14  ? 537 PRO A CD  1 
ATOM   2426 N  N   . GLU A 1 338 ? 102.439 154.450 64.953  1.00 36.64  ? 538 GLU A N   1 
ATOM   2427 C  CA  . GLU A 1 338 ? 102.450 153.090 64.435  1.00 36.64  ? 538 GLU A CA  1 
ATOM   2428 C  C   . GLU A 1 338 ? 101.544 152.146 65.213  1.00 36.64  ? 538 GLU A C   1 
ATOM   2429 O  O   . GLU A 1 338 ? 101.478 150.960 64.877  1.00 36.64  ? 538 GLU A O   1 
ATOM   2430 C  CB  . GLU A 1 338 ? 103.880 152.538 64.431  1.00 36.64  ? 538 GLU A CB  1 
ATOM   2431 C  CG  . GLU A 1 338 ? 104.758 153.099 63.327  1.00 36.64  ? 538 GLU A CG  1 
ATOM   2432 C  CD  . GLU A 1 338 ? 104.280 152.699 61.944  1.00 36.64  ? 538 GLU A CD  1 
ATOM   2433 O  OE1 . GLU A 1 338 ? 104.188 151.483 61.677  1.00 36.64  ? 538 GLU A OE1 1 
ATOM   2434 O  OE2 . GLU A 1 338 ? 103.999 153.598 61.126  1.00 36.64  ? 538 GLU A OE2 1 
ATOM   2435 N  N   . ASP A 1 339 ? 100.849 152.633 66.237  1.00 36.83  ? 539 ASP A N   1 
ATOM   2436 C  CA  . ASP A 1 339 ? 99.932  151.793 66.996  1.00 36.83  ? 539 ASP A CA  1 
ATOM   2437 C  C   . ASP A 1 339 ? 98.576  151.790 66.302  1.00 36.83  ? 539 ASP A C   1 
ATOM   2438 O  O   . ASP A 1 339 ? 97.968  152.849 66.110  1.00 36.83  ? 539 ASP A O   1 
ATOM   2439 C  CB  . ASP A 1 339 ? 99.809  152.295 68.432  1.00 36.83  ? 539 ASP A CB  1 
ATOM   2440 C  CG  . ASP A 1 339 ? 99.244  151.245 69.367  1.00 36.83  ? 539 ASP A CG  1 
ATOM   2441 O  OD1 . ASP A 1 339 ? 98.009  151.081 69.404  1.00 36.83  ? 539 ASP A OD1 1 
ATOM   2442 O  OD2 . ASP A 1 339 ? 100.038 150.582 70.067  1.00 36.83  ? 539 ASP A OD2 1 
ATOM   2443 N  N   . LYS A 1 340 ? 98.100  150.604 65.926  1.00 33.38  ? 540 LYS A N   1 
ATOM   2444 C  CA  . LYS A 1 340 ? 96.877  150.456 65.149  1.00 33.38  ? 540 LYS A CA  1 
ATOM   2445 C  C   . LYS A 1 340 ? 95.749  149.819 65.960  1.00 33.38  ? 540 LYS A C   1 
ATOM   2446 O  O   . LYS A 1 340 ? 94.870  149.161 65.398  1.00 33.38  ? 540 LYS A O   1 
ATOM   2447 C  CB  . LYS A 1 340 ? 97.144  149.642 63.885  1.00 33.38  ? 540 LYS A CB  1 
ATOM   2448 C  CG  . LYS A 1 340 ? 98.346  150.119 63.087  1.00 33.38  ? 540 LYS A CG  1 
ATOM   2449 C  CD  . LYS A 1 340 ? 98.119  151.511 62.526  1.00 33.38  ? 540 LYS A CD  1 
ATOM   2450 C  CE  . LYS A 1 340 ? 99.369  152.041 61.843  1.00 33.38  ? 540 LYS A CE  1 
ATOM   2451 N  NZ  . LYS A 1 340 ? 99.175  153.423 61.328  1.00 33.38  ? 540 LYS A NZ  1 
ATOM   2452 N  N   . THR A 1 341 ? 95.765  150.001 67.275  1.00 33.53  ? 541 THR A N   1 
ATOM   2453 C  CA  . THR A 1 341 ? 94.696  149.471 68.109  1.00 33.53  ? 541 THR A CA  1 
ATOM   2454 C  C   . THR A 1 341 ? 93.401  150.229 67.829  1.00 33.53  ? 541 THR A C   1 
ATOM   2455 O  O   . THR A 1 341 ? 93.398  151.467 67.853  1.00 33.53  ? 541 THR A O   1 
ATOM   2456 C  CB  . THR A 1 341 ? 95.057  149.578 69.589  1.00 33.53  ? 541 THR A CB  1 
ATOM   2457 O  OG1 . THR A 1 341 ? 96.378  149.065 69.801  1.00 33.53  ? 541 THR A OG1 1 
ATOM   2458 C  CG2 . THR A 1 341 ? 94.069  148.790 70.438  1.00 33.53  ? 541 THR A CG2 1 
ATOM   2459 N  N   . PRO A 1 342 ? 92.296  149.537 67.550  1.00 32.84  ? 542 PRO A N   1 
ATOM   2460 C  CA  . PRO A 1 342 ? 91.036  150.239 67.284  1.00 32.84  ? 542 PRO A CA  1 
ATOM   2461 C  C   . PRO A 1 342 ? 90.538  150.998 68.505  1.00 32.84  ? 542 PRO A C   1 
ATOM   2462 O  O   . PRO A 1 342 ? 90.772  150.608 69.651  1.00 32.84  ? 542 PRO A O   1 
ATOM   2463 C  CB  . PRO A 1 342 ? 90.073  149.109 66.897  1.00 32.84  ? 542 PRO A CB  1 
ATOM   2464 C  CG  . PRO A 1 342 ? 90.957  147.977 66.476  1.00 32.84  ? 542 PRO A CG  1 
ATOM   2465 C  CD  . PRO A 1 342 ? 92.179  148.085 67.333  1.00 32.84  ? 542 PRO A CD  1 
ATOM   2466 N  N   . GLU A 1 343 ? 89.839  152.099 68.241  1.00 37.44  ? 543 GLU A N   1 
ATOM   2467 C  CA  . GLU A 1 343 ? 89.251  152.939 69.279  1.00 37.44  ? 543 GLU A CA  1 
ATOM   2468 C  C   . GLU A 1 343 ? 87.774  152.608 69.440  1.00 37.44  ? 543 GLU A C   1 
ATOM   2469 O  O   . GLU A 1 343 ? 87.034  152.541 68.453  1.00 37.44  ? 543 GLU A O   1 
ATOM   2470 C  CB  . GLU A 1 343 ? 89.412  154.421 68.942  1.00 37.44  ? 543 GLU A CB  1 
ATOM   2471 C  CG  . GLU A 1 343 ? 90.843  154.941 68.957  1.00 37.44  ? 543 GLU A CG  1 
ATOM   2472 C  CD  . GLU A 1 343 ? 90.959  156.391 68.548  1.00 37.44  ? 543 GLU A CD  1 
ATOM   2473 O  OE1 . GLU A 1 343 ? 89.960  156.967 68.066  1.00 37.44  ? 543 GLU A OE1 1 
ATOM   2474 O  OE2 . GLU A 1 343 ? 92.053  156.964 68.727  1.00 37.44  ? 543 GLU A OE2 1 
ATOM   2475 N  N   . ILE A 1 344 ? 87.353  152.405 70.687  1.00 37.54  ? 544 ILE A N   1 
ATOM   2476 C  CA  . ILE A 1 344 ? 85.954  152.199 71.031  1.00 37.54  ? 544 ILE A CA  1 
ATOM   2477 C  C   . ILE A 1 344 ? 85.621  153.092 72.216  1.00 37.54  ? 544 ILE A C   1 
ATOM   2478 O  O   . ILE A 1 344 ? 86.503  153.570 72.933  1.00 37.54  ? 544 ILE A O   1 
ATOM   2479 C  CB  . ILE A 1 344 ? 85.638  150.721 71.356  1.00 37.54  ? 544 ILE A CB  1 
ATOM   2480 C  CG1 . ILE A 1 344 ? 86.378  150.284 72.622  1.00 37.54  ? 544 ILE A CG1 1 
ATOM   2481 C  CG2 . ILE A 1 344 ? 85.982  149.820 70.177  1.00 37.54  ? 544 ILE A CG2 1 
ATOM   2482 C  CD1 . ILE A 1 344 ? 86.266  148.805 72.910  1.00 37.54  ? 544 ILE A CD1 1 
ATOM   2483 N  N   . THR A 1 345 ? 84.328  153.321 72.412  1.00 40.68  ? 545 THR A N   1 
ATOM   2484 C  CA  . THR A 1 345 ? 83.866  154.138 73.521  1.00 40.68  ? 545 THR A CA  1 
ATOM   2485 C  C   . THR A 1 345 ? 83.845  153.320 74.811  1.00 40.68  ? 545 THR A C   1 
ATOM   2486 O  O   . THR A 1 345 ? 84.071  152.108 74.816  1.00 40.68  ? 545 THR A O   1 
ATOM   2487 C  CB  . THR A 1 345 ? 82.480  154.711 73.228  1.00 40.68  ? 545 THR A CB  1 
ATOM   2488 O  OG1 . THR A 1 345 ? 81.540  153.641 73.080  1.00 40.68  ? 545 THR A OG1 1 
ATOM   2489 C  CG2 . THR A 1 345 ? 82.505  155.537 71.951  1.00 40.68  ? 545 THR A CG2 1 
ATOM   2490 N  N   . ILE A 1 346 ? 83.576  154.009 75.922  1.00 41.89  ? 546 ILE A N   1 
ATOM   2491 C  CA  . ILE A 1 346 ? 83.516  153.335 77.216  1.00 41.89  ? 546 ILE A CA  1 
ATOM   2492 C  C   . ILE A 1 346 ? 82.361  152.341 77.247  1.00 41.89  ? 546 ILE A C   1 
ATOM   2493 O  O   . ILE A 1 346 ? 82.506  151.214 77.736  1.00 41.89  ? 546 ILE A O   1 
ATOM   2494 C  CB  . ILE A 1 346 ? 83.414  154.369 78.351  1.00 41.89  ? 546 ILE A CB  1 
ATOM   2495 C  CG1 . ILE A 1 346 ? 84.746  155.106 78.515  1.00 41.89  ? 546 ILE A CG1 1 
ATOM   2496 C  CG2 . ILE A 1 346 ? 83.012  153.703 79.657  1.00 41.89  ? 546 ILE A CG2 1 
ATOM   2497 C  CD1 . ILE A 1 346 ? 84.769  156.083 79.668  1.00 41.89  ? 546 ILE A CD1 1 
ATOM   2498 N  N   . GLY A 1 347 ? 81.197  152.737 76.723  1.00 39.30  ? 547 GLY A N   1 
ATOM   2499 C  CA  . GLY A 1 347 ? 80.073  151.817 76.667  1.00 39.30  ? 547 GLY A CA  1 
ATOM   2500 C  C   . GLY A 1 347 ? 80.338  150.620 75.775  1.00 39.30  ? 547 GLY A C   1 
ATOM   2501 O  O   . GLY A 1 347 ? 79.972  149.489 76.113  1.00 39.30  ? 547 GLY A O   1 
ATOM   2502 N  N   . GLU A 1 348 ? 80.976  150.848 74.624  1.00 38.10  ? 548 GLU A N   1 
ATOM   2503 C  CA  . GLU A 1 348 ? 81.340  149.739 73.748  1.00 38.10  ? 548 GLU A CA  1 
ATOM   2504 C  C   . GLU A 1 348 ? 82.322  148.798 74.436  1.00 38.10  ? 548 GLU A C   1 
ATOM   2505 O  O   . GLU A 1 348 ? 82.206  147.573 74.318  1.00 38.10  ? 548 GLU A O   1 
ATOM   2506 C  CB  . GLU A 1 348 ? 81.932  150.271 72.443  1.00 38.10  ? 548 GLU A CB  1 
ATOM   2507 C  CG  . GLU A 1 348 ? 80.900  150.764 71.442  1.00 38.10  ? 548 GLU A CG  1 
ATOM   2508 C  CD  . GLU A 1 348 ? 81.448  151.839 70.523  1.00 38.10  ? 548 GLU A CD  1 
ATOM   2509 O  OE1 . GLU A 1 348 ? 82.624  151.733 70.115  1.00 38.10  ? 548 GLU A OE1 1 
ATOM   2510 O  OE2 . GLU A 1 348 ? 80.703  152.792 70.208  1.00 38.10  ? 548 GLU A OE2 1 
ATOM   2511 N  N   . ALA A 1 349 ? 83.296  149.356 75.160  1.00 36.06  ? 549 ALA A N   1 
ATOM   2512 C  CA  . ALA A 1 349 ? 84.246  148.524 75.890  1.00 36.06  ? 549 ALA A CA  1 
ATOM   2513 C  C   . ALA A 1 349 ? 83.547  147.703 76.967  1.00 36.06  ? 549 ALA A C   1 
ATOM   2514 O  O   . ALA A 1 349 ? 83.855  146.521 77.152  1.00 36.06  ? 549 ALA A O   1 
ATOM   2515 C  CB  . ALA A 1 349 ? 85.342  149.393 76.504  1.00 36.06  ? 549 ALA A CB  1 
ATOM   2516 N  N   . ILE A 1 350 ? 82.602  148.315 77.684  1.00 37.56  ? 550 ILE A N   1 
ATOM   2517 C  CA  . ILE A 1 350 ? 81.866  147.595 78.721  1.00 37.56  ? 550 ILE A CA  1 
ATOM   2518 C  C   . ILE A 1 350 ? 81.060  146.458 78.106  1.00 37.56  ? 550 ILE A C   1 
ATOM   2519 O  O   . ILE A 1 350 ? 81.054  145.328 78.614  1.00 37.56  ? 550 ILE A O   1 
ATOM   2520 C  CB  . ILE A 1 350 ? 80.967  148.565 79.509  1.00 37.56  ? 550 ILE A CB  1 
ATOM   2521 C  CG1 . ILE A 1 350 ? 81.808  149.422 80.456  1.00 37.56  ? 550 ILE A CG1 1 
ATOM   2522 C  CG2 . ILE A 1 350 ? 79.901  147.805 80.283  1.00 37.56  ? 550 ILE A CG2 1 
ATOM   2523 C  CD1 . ILE A 1 350 ? 81.120  150.694 80.900  1.00 37.56  ? 550 ILE A CD1 1 
ATOM   2524 N  N   . LYS A 1 351 ? 80.377  146.739 76.993  1.00 40.08  ? 551 LYS A N   1 
ATOM   2525 C  CA  . LYS A 1 351 ? 79.579  145.711 76.331  1.00 40.08  ? 551 LYS A CA  1 
ATOM   2526 C  C   . LYS A 1 351 ? 80.453  144.568 75.830  1.00 40.08  ? 551 LYS A C   1 
ATOM   2527 O  O   . LYS A 1 351 ? 80.081  143.394 75.949  1.00 40.08  ? 551 LYS A O   1 
ATOM   2528 C  CB  . LYS A 1 351 ? 78.787  146.327 75.177  1.00 40.08  ? 551 LYS A CB  1 
ATOM   2529 C  CG  . LYS A 1 351 ? 77.823  145.364 74.503  1.00 40.08  ? 551 LYS A CG  1 
ATOM   2530 C  CD  . LYS A 1 351 ? 77.087  146.035 73.355  1.00 40.08  ? 551 LYS A CD  1 
ATOM   2531 C  CE  . LYS A 1 351 ? 76.822  145.056 72.223  1.00 40.08  ? 551 LYS A CE  1 
ATOM   2532 N  NZ  . LYS A 1 351 ? 75.447  144.491 72.285  1.00 40.08  ? 551 LYS A NZ  1 
ATOM   2533 N  N   . LYS A 1 352 ? 81.616  144.890 75.258  1.00 33.29  ? 552 LYS A N   1 
ATOM   2534 C  CA  . LYS A 1 352 ? 82.524  143.848 74.787  1.00 33.29  ? 552 LYS A CA  1 
ATOM   2535 C  C   . LYS A 1 352 ? 83.066  143.016 75.943  1.00 33.29  ? 552 LYS A C   1 
ATOM   2536 O  O   . LYS A 1 352 ? 83.159  141.786 75.840  1.00 33.29  ? 552 LYS A O   1 
ATOM   2537 C  CB  . LYS A 1 352 ? 83.671  144.471 73.994  1.00 33.29  ? 552 LYS A CB  1 
ATOM   2538 C  CG  . LYS A 1 352 ? 83.359  144.721 72.529  1.00 33.29  ? 552 LYS A CG  1 
ATOM   2539 C  CD  . LYS A 1 352 ? 84.491  145.470 71.847  1.00 33.29  ? 552 LYS A CD  1 
ATOM   2540 C  CE  . LYS A 1 352 ? 84.116  145.871 70.431  1.00 33.29  ? 552 LYS A CE  1 
ATOM   2541 N  NZ  . LYS A 1 352 ? 83.605  144.714 69.644  1.00 33.29  ? 552 LYS A NZ  1 
ATOM   2542 N  N   . ALA A 1 353 ? 83.431  143.666 77.050  1.00 32.21  ? 553 ALA A N   1 
ATOM   2543 C  CA  . ALA A 1 353 ? 84.079  142.964 78.151  1.00 32.21  ? 553 ALA A CA  1 
ATOM   2544 C  C   . ALA A 1 353 ? 83.110  142.105 78.951  1.00 32.21  ? 553 ALA A C   1 
ATOM   2545 O  O   . ALA A 1 353 ? 83.480  141.008 79.385  1.00 32.21  ? 553 ALA A O   1 
ATOM   2546 C  CB  . ALA A 1 353 ? 84.770  143.965 79.076  1.00 32.21  ? 553 ALA A CB  1 
ATOM   2547 N  N   . PHE A 1 354 ? 81.879  142.572 79.163  1.00 35.06  ? 554 PHE A N   1 
ATOM   2548 C  CA  . PHE A 1 354 ? 80.933  141.867 80.017  1.00 35.06  ? 554 PHE A CA  1 
ATOM   2549 C  C   . PHE A 1 354 ? 79.860  141.122 79.233  1.00 35.06  ? 554 PHE A C   1 
ATOM   2550 O  O   . PHE A 1 354 ? 78.937  140.571 79.843  1.00 35.06  ? 554 PHE A O   1 
ATOM   2551 C  CB  . PHE A 1 354 ? 80.289  142.847 81.000  1.00 35.06  ? 554 PHE A CB  1 
ATOM   2552 C  CG  . PHE A 1 354 ? 81.271  143.495 81.932  1.00 35.06  ? 554 PHE A CG  1 
ATOM   2553 C  CD1 . PHE A 1 354 ? 81.900  142.756 82.919  1.00 35.06  ? 554 PHE A CD1 1 
ATOM   2554 C  CD2 . PHE A 1 354 ? 81.572  144.842 81.814  1.00 35.06  ? 554 PHE A CD2 1 
ATOM   2555 C  CE1 . PHE A 1 354 ? 82.809  143.348 83.775  1.00 35.06  ? 554 PHE A CE1 1 
ATOM   2556 C  CE2 . PHE A 1 354 ? 82.480  145.440 82.668  1.00 35.06  ? 554 PHE A CE2 1 
ATOM   2557 C  CZ  . PHE A 1 354 ? 83.099  144.692 83.648  1.00 35.06  ? 554 PHE A CZ  1 
ATOM   2558 N  N   . SER A 1 355 ? 79.966  141.079 77.903  1.00 40.78  ? 555 SER A N   1 
ATOM   2559 C  CA  . SER A 1 355 ? 78.995  140.391 77.049  1.00 40.78  ? 555 SER A CA  1 
ATOM   2560 C  C   . SER A 1 355 ? 77.573  140.868 77.331  1.00 40.78  ? 555 SER A C   1 
ATOM   2561 O  O   . SER A 1 355 ? 76.626  140.080 77.385  1.00 40.78  ? 555 SER A O   1 
ATOM   2562 C  CB  . SER A 1 355 ? 79.099  138.873 77.203  1.00 40.78  ? 555 SER A CB  1 
ATOM   2563 O  OG  . SER A 1 355 ? 79.959  138.320 76.222  1.00 40.78  ? 555 SER A OG  1 
ATOM   2564 N  N   . ALA A 1 356 ? 77.422  142.176 77.518  1.00 50.96  ? 556 ALA A N   1 
ATOM   2565 C  CA  . ALA A 1 356 ? 76.114  142.745 77.800  1.00 50.96  ? 556 ALA A CA  1 
ATOM   2566 C  C   . ALA A 1 356 ? 75.225  142.689 76.562  1.00 50.96  ? 556 ALA A C   1 
ATOM   2567 O  O   . ALA A 1 356 ? 75.701  142.651 75.425  1.00 50.96  ? 556 ALA A O   1 
ATOM   2568 C  CB  . ALA A 1 356 ? 76.252  144.186 78.285  1.00 50.96  ? 556 ALA A CB  1 
ATOM   2569 N  N   . THR A 1 357 ? 73.916  142.683 76.796  1.00 65.56  ? 557 THR A N   1 
ATOM   2570 C  CA  . THR A 1 357 ? 72.929  142.596 75.730  1.00 65.56  ? 557 THR A CA  1 
ATOM   2571 C  C   . THR A 1 357 ? 72.332  143.972 75.471  1.00 65.56  ? 557 THR A C   1 
ATOM   2572 O  O   . THR A 1 357 ? 71.918  144.662 76.409  1.00 65.56  ? 557 THR A O   1 
ATOM   2573 C  CB  . THR A 1 357 ? 71.821  141.602 76.087  1.00 65.56  ? 557 THR A CB  1 
ATOM   2574 O  OG1 . THR A 1 357 ? 72.400  140.433 76.682  1.00 65.56  ? 557 THR A OG1 1 
ATOM   2575 C  CG2 . THR A 1 357 ? 71.044  141.200 74.842  1.00 65.56  ? 557 THR A CG2 1 
ATOM   2576 N  N   . LYS A 1 358 ? 72.289  144.366 74.200  1.00 76.07  ? 558 LYS A N   1 
ATOM   2577 C  CA  . LYS A 1 358 ? 71.739  145.655 73.789  1.00 76.07  ? 558 LYS A CA  1 
ATOM   2578 C  C   . LYS A 1 358 ? 70.350  145.415 73.208  1.00 76.07  ? 558 LYS A C   1 
ATOM   2579 O  O   . LYS A 1 358 ? 70.208  145.024 72.047  1.00 76.07  ? 558 LYS A O   1 
ATOM   2580 C  CB  . LYS A 1 358 ? 72.654  146.339 72.779  1.00 76.07  ? 558 LYS A CB  1 
ATOM   2581 C  CG  . LYS A 1 358 ? 72.539  147.857 72.760  1.00 76.07  ? 558 LYS A CG  1 
ATOM   2582 C  CD  . LYS A 1 358 ? 73.628  148.505 73.599  1.00 76.07  ? 558 LYS A CD  1 
ATOM   2583 C  CE  . LYS A 1 358 ? 73.597  150.019 73.478  1.00 76.07  ? 558 LYS A CE  1 
ATOM   2584 N  NZ  . LYS A 1 358 ? 72.399  150.605 74.138  1.00 76.07  ? 558 LYS A NZ  1 
ATOM   2585 N  N   . ASN A 1 359 ? 69.320  145.654 74.023  1.00 82.95  ? 559 ASN A N   1 
ATOM   2586 C  CA  . ASN A 1 359 ? 67.932  145.551 73.590  1.00 82.95  ? 559 ASN A CA  1 
ATOM   2587 C  C   . ASN A 1 359 ? 67.386  146.876 73.076  1.00 82.95  ? 559 ASN A C   1 
ATOM   2588 O  O   . ASN A 1 359 ? 66.173  147.118 73.149  1.00 82.95  ? 559 ASN A O   1 
ATOM   2589 C  CB  . ASN A 1 359 ? 67.064  145.023 74.734  1.00 82.95  ? 559 ASN A CB  1 
ATOM   2590 C  CG  . ASN A 1 359 ? 67.666  143.805 75.407  1.00 82.95  ? 559 ASN A CG  1 
ATOM   2591 O  OD1 . ASN A 1 359 ? 68.808  143.835 75.866  1.00 82.95  ? 559 ASN A OD1 1 
ATOM   2592 N  ND2 . ASN A 1 359 ? 66.898  142.723 75.470  1.00 82.95  ? 559 ASN A ND2 1 
ATOM   2593 N  N   . GLY A 1 360 ? 68.253  147.740 72.558  1.00 88.83  ? 560 GLY A N   1 
ATOM   2594 C  CA  . GLY A 1 360 ? 67.872  149.084 72.174  1.00 88.83  ? 560 GLY A CA  1 
ATOM   2595 C  C   . GLY A 1 360 ? 68.865  150.090 72.716  1.00 88.83  ? 560 GLY A C   1 
ATOM   2596 O  O   . GLY A 1 360 ? 70.045  150.061 72.358  1.00 88.83  ? 560 GLY A O   1 
ATOM   2597 N  N   . GLU A 1 361 ? 68.399  150.988 73.583  1.00 88.87  ? 561 GLU A N   1 
ATOM   2598 C  CA  . GLU A 1 361 ? 69.272  151.892 74.316  1.00 88.87  ? 561 GLU A CA  1 
ATOM   2599 C  C   . GLU A 1 361 ? 69.518  151.418 75.743  1.00 88.87  ? 561 GLU A C   1 
ATOM   2600 O  O   . GLU A 1 361 ? 69.861  152.228 76.612  1.00 88.87  ? 561 GLU A O   1 
ATOM   2601 C  CB  . GLU A 1 361 ? 68.694  153.308 74.317  1.00 88.87  ? 561 GLU A CB  1 
ATOM   2602 C  CG  . GLU A 1 361 ? 69.692  154.379 73.909  1.00 88.87  ? 561 GLU A CG  1 
ATOM   2603 C  CD  . GLU A 1 361 ? 69.023  155.666 73.468  1.00 88.87  ? 561 GLU A CD  1 
ATOM   2604 O  OE1 . GLU A 1 361 ? 67.961  156.007 74.031  1.00 88.87  ? 561 GLU A OE1 1 
ATOM   2605 O  OE2 . GLU A 1 361 ? 69.559  156.334 72.560  1.00 88.87  ? 561 GLU A OE2 1 
ATOM   2606 N  N   . LEU A 1 362 ? 69.349  150.123 75.999  1.00 80.32  ? 562 LEU A N   1 
ATOM   2607 C  CA  . LEU A 1 362 ? 69.502  149.549 77.327  1.00 80.32  ? 562 LEU A CA  1 
ATOM   2608 C  C   . LEU A 1 362 ? 70.618  148.516 77.324  1.00 80.32  ? 562 LEU A C   1 
ATOM   2609 O  O   . LEU A 1 362 ? 70.850  147.827 76.326  1.00 80.32  ? 562 LEU A O   1 
ATOM   2610 C  CB  . LEU A 1 362 ? 68.196  148.899 77.811  1.00 80.32  ? 562 LEU A CB  1 
ATOM   2611 C  CG  . LEU A 1 362 ? 66.880  149.628 77.521  1.00 80.32  ? 562 LEU A CG  1 
ATOM   2612 C  CD1 . LEU A 1 362 ? 66.266  149.159 76.207  1.00 80.32  ? 562 LEU A CD1 1 
ATOM   2613 C  CD2 . LEU A 1 362 ? 65.900  149.442 78.669  1.00 80.32  ? 562 LEU A CD2 1 
ATOM   2614 N  N   . LEU A 1 363 ? 71.310  148.413 78.456  1.00 68.22  ? 563 LEU A N   1 
ATOM   2615 C  CA  . LEU A 1 363 ? 72.403  147.469 78.637  1.00 68.22  ? 563 LEU A CA  1 
ATOM   2616 C  C   . LEU A 1 363 ? 72.093  146.562 79.819  1.00 68.22  ? 563 LEU A C   1 
ATOM   2617 O  O   . LEU A 1 363 ? 71.850  147.047 80.930  1.00 68.22  ? 563 LEU A O   1 
ATOM   2618 C  CB  . LEU A 1 363 ? 73.731  148.200 78.860  1.00 68.22  ? 563 LEU A CB  1 
ATOM   2619 C  CG  . LEU A 1 363 ? 74.970  147.614 78.178  1.00 68.22  ? 563 LEU A CG  1 
ATOM   2620 C  CD1 . LEU A 1 363 ? 74.642  147.129 76.775  1.00 68.22  ? 563 LEU A CD1 1 
ATOM   2621 C  CD2 . LEU A 1 363 ? 76.095  148.635 78.144  1.00 68.22  ? 563 LEU A CD2 1 
ATOM   2622 N  N   . TYR A 1 364 ? 72.096  145.253 79.577  1.00 66.53  ? 564 TYR A N   1 
ATOM   2623 C  CA  . TYR A 1 364 ? 71.829  144.259 80.607  1.00 66.53  ? 564 TYR A CA  1 
ATOM   2624 C  C   . TYR A 1 364 ? 72.984  143.271 80.659  1.00 66.53  ? 564 TYR A C   1 
ATOM   2625 O  O   . TYR A 1 364 ? 73.383  142.727 79.624  1.00 66.53  ? 564 TYR A O   1 
ATOM   2626 C  CB  . TYR A 1 364 ? 70.514  143.518 80.336  1.00 66.53  ? 564 TYR A CB  1 
ATOM   2627 C  CG  . TYR A 1 364 ? 69.282  144.391 80.431  1.00 66.53  ? 564 TYR A CG  1 
ATOM   2628 C  CD1 . TYR A 1 364 ? 68.734  144.719 81.664  1.00 66.53  ? 564 TYR A CD1 1 
ATOM   2629 C  CD2 . TYR A 1 364 ? 68.671  144.886 79.288  1.00 66.53  ? 564 TYR A CD2 1 
ATOM   2630 C  CE1 . TYR A 1 364 ? 67.608  145.515 81.755  1.00 66.53  ? 564 TYR A CE1 1 
ATOM   2631 C  CE2 . TYR A 1 364 ? 67.545  145.684 79.369  1.00 66.53  ? 564 TYR A CE2 1 
ATOM   2632 C  CZ  . TYR A 1 364 ? 67.018  145.995 80.604  1.00 66.53  ? 564 TYR A CZ  1 
ATOM   2633 N  N   . PHE A 1 365 ? 73.515  143.038 81.859  1.00 56.00  ? 565 PHE A N   1 
ATOM   2634 C  CA  . PHE A 1 365 ? 74.588  142.062 82.020  1.00 56.00  ? 565 PHE A CA  1 
ATOM   2635 C  C   . PHE A 1 365 ? 74.028  140.648 82.144  1.00 56.00  ? 565 PHE A C   1 
ATOM   2636 O  O   . PHE A 1 365 ? 74.296  139.784 81.303  1.00 56.00  ? 565 PHE A O   1 
ATOM   2637 C  CB  . PHE A 1 365 ? 75.440  142.416 83.243  1.00 56.00  ? 565 PHE A CB  1 
ATOM   2638 C  CG  . PHE A 1 365 ? 76.479  141.385 83.580  1.00 56.00  ? 565 PHE A CG  1 
ATOM   2639 C  CD1 . PHE A 1 365 ? 77.300  140.859 82.594  1.00 56.00  ? 565 PHE A CD1 1 
ATOM   2640 C  CD2 . PHE A 1 365 ? 76.634  140.938 84.881  1.00 56.00  ? 565 PHE A CD2 1 
ATOM   2641 C  CE1 . PHE A 1 365 ? 78.255  139.909 82.903  1.00 56.00  ? 565 PHE A CE1 1 
ATOM   2642 C  CE2 . PHE A 1 365 ? 77.587  139.989 85.194  1.00 56.00  ? 565 PHE A CE2 1 
ATOM   2643 C  CZ  . PHE A 1 365 ? 78.399  139.474 84.204  1.00 56.00  ? 565 PHE A CZ  1 
ATOM   2644 N  N   . ASN A 1 366 ? 73.247  140.401 83.191  1.00 60.82  ? 566 ASN A N   1 
ATOM   2645 C  CA  . ASN A 1 366 ? 72.581  139.120 83.405  1.00 60.82  ? 566 ASN A CA  1 
ATOM   2646 C  C   . ASN A 1 366 ? 71.142  139.371 83.843  1.00 60.82  ? 566 ASN A C   1 
ATOM   2647 O  O   . ASN A 1 366 ? 70.633  138.765 84.787  1.00 60.82  ? 566 ASN A O   1 
ATOM   2648 C  CB  . ASN A 1 366 ? 73.331  138.272 84.431  1.00 60.82  ? 566 ASN A CB  1 
ATOM   2649 C  CG  . ASN A 1 366 ? 74.520  137.548 83.830  1.00 60.82  ? 566 ASN A CG  1 
ATOM   2650 O  OD1 . ASN A 1 366 ? 74.502  137.164 82.661  1.00 60.82  ? 566 ASN A OD1 1 
ATOM   2651 N  ND2 . ASN A 1 366 ? 75.562  137.357 84.631  1.00 60.82  ? 566 ASN A ND2 1 
ATOM   2652 N  N   . GLY A 1 367 ? 70.468  140.284 83.144  1.00 65.88  ? 567 GLY A N   1 
ATOM   2653 C  CA  . GLY A 1 367 ? 69.164  140.756 83.545  1.00 65.88  ? 567 GLY A CA  1 
ATOM   2654 C  C   . GLY A 1 367 ? 69.184  141.979 84.436  1.00 65.88  ? 567 GLY A C   1 
ATOM   2655 O  O   . GLY A 1 367 ? 68.119  142.551 84.700  1.00 65.88  ? 567 GLY A O   1 
ATOM   2656 N  N   . ILE A 1 368 ? 70.355  142.395 84.904  1.00 66.34  ? 568 ILE A N   1 
ATOM   2657 C  CA  . ILE A 1 368 ? 70.495  143.590 85.730  1.00 66.34  ? 568 ILE A CA  1 
ATOM   2658 C  C   . ILE A 1 368 ? 70.858  144.753 84.812  1.00 66.34  ? 568 ILE A C   1 
ATOM   2659 O  O   . ILE A 1 368 ? 71.885  144.677 84.117  1.00 66.34  ? 568 ILE A O   1 
ATOM   2660 C  CB  . ILE A 1 368 ? 71.558  143.399 86.818  1.00 66.34  ? 568 ILE A CB  1 
ATOM   2661 C  CG1 . ILE A 1 368 ? 71.300  142.110 87.599  1.00 66.34  ? 568 ILE A CG1 1 
ATOM   2662 C  CG2 . ILE A 1 368 ? 71.581  144.598 87.755  1.00 66.34  ? 568 ILE A CG2 1 
ATOM   2663 C  CD1 . ILE A 1 368 ? 72.552  141.304 87.875  1.00 66.34  ? 568 ILE A CD1 1 
ATOM   2664 N  N   . PRO A 1 369 ? 70.060  145.820 84.766  1.00 68.05  ? 569 PRO A N   1 
ATOM   2665 C  CA  . PRO A 1 369 ? 70.408  146.963 83.906  1.00 68.05  ? 569 PRO A CA  1 
ATOM   2666 C  C   . PRO A 1 369 ? 71.699  147.619 84.373  1.00 68.05  ? 569 PRO A C   1 
ATOM   2667 O  O   . PRO A 1 369 ? 71.844  147.975 85.545  1.00 68.05  ? 569 PRO A O   1 
ATOM   2668 C  CB  . PRO A 1 369 ? 69.211  147.913 84.045  1.00 68.05  ? 569 PRO A CB  1 
ATOM   2669 C  CG  . PRO A 1 369 ? 68.252  147.281 84.977  1.00 68.05  ? 569 PRO A CG  1 
ATOM   2670 C  CD  . PRO A 1 369 ? 68.761  145.966 85.444  1.00 68.05  ? 569 PRO A CD  1 
ATOM   2671 N  N   . ILE A 1 370 ? 72.638  147.779 83.442  1.00 65.72  ? 570 ILE A N   1 
ATOM   2672 C  CA  . ILE A 1 370 ? 73.933  148.378 83.747  1.00 65.72  ? 570 ILE A CA  1 
ATOM   2673 C  C   . ILE A 1 370 ? 74.091  149.670 82.956  1.00 65.72  ? 570 ILE A C   1 
ATOM   2674 O  O   . ILE A 1 370 ? 75.202  150.034 82.556  1.00 65.72  ? 570 ILE A O   1 
ATOM   2675 C  CB  . ILE A 1 370 ? 75.089  147.403 83.456  1.00 65.72  ? 570 ILE A CB  1 
ATOM   2676 C  CG1 . ILE A 1 370 ? 74.834  146.638 82.158  1.00 65.72  ? 570 ILE A CG1 1 
ATOM   2677 C  CG2 . ILE A 1 370 ? 75.275  146.441 84.619  1.00 65.72  ? 570 ILE A CG2 1 
ATOM   2678 C  CD1 . ILE A 1 370 ? 76.097  146.161 81.478  1.00 65.72  ? 570 ILE A CD1 1 
ATOM   2679 N  N   . ASP A 1 371 ? 72.979  150.364 82.723  1.00 70.17  ? 571 ASP A N   1 
ATOM   2680 C  CA  . ASP A 1 371 ? 73.015  151.628 82.003  1.00 70.17  ? 571 ASP A CA  1 
ATOM   2681 C  C   . ASP A 1 371 ? 73.780  152.681 82.801  1.00 70.17  ? 571 ASP A C   1 
ATOM   2682 O  O   . ASP A 1 371 ? 73.971  152.565 84.014  1.00 70.17  ? 571 ASP A O   1 
ATOM   2683 C  CB  . ASP A 1 371 ? 71.598  152.123 81.716  1.00 70.17  ? 571 ASP A CB  1 
ATOM   2684 C  CG  . ASP A 1 371 ? 70.713  151.046 81.129  1.00 70.17  ? 571 ASP A CG  1 
ATOM   2685 O  OD1 . ASP A 1 371 ? 70.341  150.110 81.868  1.00 70.17  ? 571 ASP A OD1 1 
ATOM   2686 O  OD2 . ASP A 1 371 ? 70.387  151.136 79.928  1.00 70.17  ? 571 ASP A OD2 1 
ATOM   2687 N  N   . GLU A 1 372 ? 74.215  153.728 82.095  1.00 66.59  ? 572 GLU A N   1 
ATOM   2688 C  CA  . GLU A 1 372 ? 75.005  154.779 82.726  1.00 66.59  ? 572 GLU A CA  1 
ATOM   2689 C  C   . GLU A 1 372 ? 74.228  155.496 83.822  1.00 66.59  ? 572 GLU A C   1 
ATOM   2690 O  O   . GLU A 1 372 ? 74.814  155.912 84.828  1.00 66.59  ? 572 GLU A O   1 
ATOM   2691 C  CB  . GLU A 1 372 ? 75.476  155.781 81.670  1.00 66.59  ? 572 GLU A CB  1 
ATOM   2692 C  CG  . GLU A 1 372 ? 76.460  156.817 82.183  1.00 66.59  ? 572 GLU A CG  1 
ATOM   2693 C  CD  . GLU A 1 372 ? 76.727  157.916 81.172  1.00 66.59  ? 572 GLU A CD  1 
ATOM   2694 O  OE1 . GLU A 1 372 ? 76.523  157.675 79.964  1.00 66.59  ? 572 GLU A OE1 1 
ATOM   2695 O  OE2 . GLU A 1 372 ? 77.135  159.021 81.585  1.00 66.59  ? 572 GLU A OE2 1 
ATOM   2696 N  N   . SER A 1 373 ? 72.918  155.649 83.653  1.00 82.01  ? 573 SER A N   1 
ATOM   2697 C  CA  . SER A 1 373 ? 72.081  156.332 84.630  1.00 82.01  ? 573 SER A CA  1 
ATOM   2698 C  C   . SER A 1 373 ? 71.544  155.401 85.711  1.00 82.01  ? 573 SER A C   1 
ATOM   2699 O  O   . SER A 1 373 ? 70.858  155.870 86.624  1.00 82.01  ? 573 SER A O   1 
ATOM   2700 C  CB  . SER A 1 373 ? 70.910  157.025 83.926  1.00 82.01  ? 573 SER A CB  1 
ATOM   2701 O  OG  . SER A 1 373 ? 70.168  156.104 83.146  1.00 82.01  ? 573 SER A OG  1 
ATOM   2702 N  N   . CYS A 1 374 ? 71.832  154.102 85.631  1.00 77.28  ? 574 CYS A N   1 
ATOM   2703 C  CA  . CYS A 1 374 ? 71.335  153.134 86.598  1.00 77.28  ? 574 CYS A CA  1 
ATOM   2704 C  C   . CYS A 1 374 ? 72.432  152.542 87.471  1.00 77.28  ? 574 CYS A C   1 
ATOM   2705 O  O   . CYS A 1 374 ? 72.132  151.723 88.346  1.00 77.28  ? 574 CYS A O   1 
ATOM   2706 C  CB  . CYS A 1 374 ? 70.588  152.006 85.879  1.00 77.28  ? 574 CYS A CB  1 
ATOM   2707 S  SG  . CYS A 1 374 ? 69.041  152.511 85.093  1.00 77.28  ? 574 CYS A SG  1 
ATOM   2708 N  N   . VAL A 1 375 ? 73.690  152.928 87.260  1.00 69.18  ? 575 VAL A N   1 
ATOM   2709 C  CA  . VAL A 1 375 ? 74.810  152.395 88.022  1.00 69.18  ? 575 VAL A CA  1 
ATOM   2710 C  C   . VAL A 1 375 ? 75.640  153.555 88.556  1.00 69.18  ? 575 VAL A C   1 
ATOM   2711 O  O   . VAL A 1 375 ? 75.485  154.705 88.142  1.00 69.18  ? 575 VAL A O   1 
ATOM   2712 C  CB  . VAL A 1 375 ? 75.700  151.451 87.186  1.00 69.18  ? 575 VAL A CB  1 
ATOM   2713 C  CG1 . VAL A 1 375 ? 74.887  150.283 86.657  1.00 69.18  ? 575 VAL A CG1 1 
ATOM   2714 C  CG2 . VAL A 1 375 ? 76.365  152.215 86.051  1.00 69.18  ? 575 VAL A CG2 1 
ATOM   2715 N  N   . GLU A 1 376 ? 76.528  153.230 89.490  1.00 68.95  ? 576 GLU A N   1 
ATOM   2716 C  CA  . GLU A 1 376 ? 77.422  154.202 90.102  1.00 68.95  ? 576 GLU A CA  1 
ATOM   2717 C  C   . GLU A 1 376 ? 78.810  154.017 89.504  1.00 68.95  ? 576 GLU A C   1 
ATOM   2718 O  O   . GLU A 1 376 ? 79.345  152.905 89.509  1.00 68.95  ? 576 GLU A O   1 
ATOM   2719 C  CB  . GLU A 1 376 ? 77.442  154.027 91.620  1.00 68.95  ? 576 GLU A CB  1 
ATOM   2720 C  CG  . GLU A 1 376 ? 77.603  155.315 92.408  1.00 68.95  ? 576 GLU A CG  1 
ATOM   2721 C  CD  . GLU A 1 376 ? 76.335  156.154 92.409  1.00 68.95  ? 576 GLU A CD  1 
ATOM   2722 O  OE1 . GLU A 1 376 ? 76.084  156.850 91.412  1.00 68.95  ? 576 GLU A OE1 1 
ATOM   2723 O  OE2 . GLU A 1 376 ? 75.592  156.109 93.416  1.00 68.95  ? 576 GLU A OE2 1 
ATOM   2724 N  N   . LEU A 1 377 ? 79.382  155.098 88.982  1.00 54.54  ? 577 LEU A N   1 
ATOM   2725 C  CA  . LEU A 1 377 ? 80.676  155.055 88.314  1.00 54.54  ? 577 LEU A CA  1 
ATOM   2726 C  C   . LEU A 1 377 ? 81.739  155.669 89.214  1.00 54.54  ? 577 LEU A C   1 
ATOM   2727 O  O   . LEU A 1 377 ? 81.554  156.771 89.742  1.00 54.54  ? 577 LEU A O   1 
ATOM   2728 C  CB  . LEU A 1 377 ? 80.621  155.791 86.975  1.00 54.54  ? 577 LEU A CB  1 
ATOM   2729 C  CG  . LEU A 1 377 ? 79.671  155.192 85.936  1.00 54.54  ? 577 LEU A CG  1 
ATOM   2730 C  CD1 . LEU A 1 377 ? 79.498  156.133 84.757  1.00 54.54  ? 577 LEU A CD1 1 
ATOM   2731 C  CD2 . LEU A 1 377 ? 80.170  153.829 85.470  1.00 54.54  ? 577 LEU A CD2 1 
ATOM   2732 N  N   . ILE A 1 378 ? 82.845  154.951 89.391  1.00 48.60  ? 578 ILE A N   1 
ATOM   2733 C  CA  . ILE A 1 378 ? 83.952  155.383 90.235  1.00 48.60  ? 578 ILE A CA  1 
ATOM   2734 C  C   . ILE A 1 378 ? 85.233  155.334 89.414  1.00 48.60  ? 578 ILE A C   1 
ATOM   2735 O  O   . ILE A 1 378 ? 85.499  154.338 88.727  1.00 48.60  ? 578 ILE A O   1 
ATOM   2736 C  CB  . ILE A 1 378 ? 84.069  154.518 91.503  1.00 48.60  ? 578 ILE A CB  1 
ATOM   2737 C  CG1 . ILE A 1 378 ? 82.856  154.740 92.409  1.00 48.60  ? 578 ILE A CG1 1 
ATOM   2738 C  CG2 . ILE A 1 378 ? 85.354  154.832 92.254  1.00 48.60  ? 578 ILE A CG2 1 
ATOM   2739 C  CD1 . ILE A 1 378 ? 82.418  153.508 93.166  1.00 48.60  ? 578 ILE A CD1 1 
ATOM   2740 N  N   . PHE A 1 379 ? 86.013  156.409 89.476  1.00 51.98  ? 579 PHE A N   1 
ATOM   2741 C  CA  . PHE A 1 379 ? 87.282  156.509 88.773  1.00 51.98  ? 579 PHE A CA  1 
ATOM   2742 C  C   . PHE A 1 379 ? 88.341  157.046 89.727  1.00 51.98  ? 579 PHE A C   1 
ATOM   2743 O  O   . PHE A 1 379 ? 88.038  157.523 90.824  1.00 51.98  ? 579 PHE A O   1 
ATOM   2744 C  CB  . PHE A 1 379 ? 87.178  157.421 87.543  1.00 51.98  ? 579 PHE A CB  1 
ATOM   2745 C  CG  . PHE A 1 379 ? 85.908  157.244 86.758  1.00 51.98  ? 579 PHE A CG  1 
ATOM   2746 C  CD1 . PHE A 1 379 ? 85.659  156.072 86.067  1.00 51.98  ? 579 PHE A CD1 1 
ATOM   2747 C  CD2 . PHE A 1 379 ? 84.966  158.259 86.710  1.00 51.98  ? 579 PHE A CD2 1 
ATOM   2748 C  CE1 . PHE A 1 379 ? 84.491  155.912 85.345  1.00 51.98  ? 579 PHE A CE1 1 
ATOM   2749 C  CE2 . PHE A 1 379 ? 83.797  158.104 85.990  1.00 51.98  ? 579 PHE A CE2 1 
ATOM   2750 C  CZ  . PHE A 1 379 ? 83.559  156.930 85.308  1.00 51.98  ? 579 PHE A CZ  1 
ATOM   2751 N  N   . ASP A 1 380 ? 89.598  156.962 89.300  1.00 58.95  ? 580 ASP A N   1 
ATOM   2752 C  CA  . ASP A 1 380 ? 90.689  157.626 89.993  1.00 58.95  ? 580 ASP A CA  1 
ATOM   2753 C  C   . ASP A 1 380 ? 90.828  159.050 89.461  1.00 58.95  ? 580 ASP A C   1 
ATOM   2754 O  O   . ASP A 1 380 ? 90.005  159.531 88.677  1.00 58.95  ? 580 ASP A O   1 
ATOM   2755 C  CB  . ASP A 1 380 ? 91.992  156.833 89.847  1.00 58.95  ? 580 ASP A CB  1 
ATOM   2756 C  CG  . ASP A 1 380 ? 92.145  156.203 88.480  1.00 58.95  ? 580 ASP A CG  1 
ATOM   2757 O  OD1 . ASP A 1 380 ? 91.205  156.309 87.667  1.00 58.95  ? 580 ASP A OD1 1 
ATOM   2758 O  OD2 . ASP A 1 380 ? 93.207  155.601 88.216  1.00 58.95  ? 580 ASP A OD2 1 
ATOM   2759 N  N   . ASP A 1 381 ? 91.883  159.738 89.901  1.00 66.77  ? 581 ASP A N   1 
ATOM   2760 C  CA  . ASP A 1 381 ? 92.042  161.149 89.556  1.00 66.77  ? 581 ASP A CA  1 
ATOM   2761 C  C   . ASP A 1 381 ? 92.260  161.337 88.058  1.00 66.77  ? 581 ASP A C   1 
ATOM   2762 O  O   . ASP A 1 381 ? 91.599  162.169 87.424  1.00 66.77  ? 581 ASP A O   1 
ATOM   2763 C  CB  . ASP A 1 381 ? 93.201  161.754 90.350  1.00 66.77  ? 581 ASP A CB  1 
ATOM   2764 C  CG  . ASP A 1 381 ? 93.162  161.374 91.818  1.00 66.77  ? 581 ASP A CG  1 
ATOM   2765 O  OD1 . ASP A 1 381 ? 92.113  160.878 92.279  1.00 66.77  ? 581 ASP A OD1 1 
ATOM   2766 O  OD2 . ASP A 1 381 ? 94.183  161.575 92.511  1.00 66.77  ? 581 ASP A OD2 1 
ATOM   2767 N  N   . ASN A 1 382 ? 93.187  160.572 87.475  1.00 66.60  ? 582 ASN A N   1 
ATOM   2768 C  CA  . ASN A 1 382 ? 93.521  160.754 86.065  1.00 66.60  ? 582 ASN A CA  1 
ATOM   2769 C  C   . ASN A 1 382 ? 92.332  160.427 85.169  1.00 66.60  ? 582 ASN A C   1 
ATOM   2770 O  O   . ASN A 1 382 ? 92.032  161.162 84.219  1.00 66.60  ? 582 ASN A O   1 
ATOM   2771 C  CB  . ASN A 1 382 ? 94.726  159.887 85.699  1.00 66.60  ? 582 ASN A CB  1 
ATOM   2772 C  CG  . ASN A 1 382 ? 95.616  160.539 84.659  1.00 66.60  ? 582 ASN A CG  1 
ATOM   2773 O  OD1 . ASN A 1 382 ? 95.143  161.010 83.626  1.00 66.60  ? 582 ASN A OD1 1 
ATOM   2774 N  ND2 . ASN A 1 382 ? 96.916  160.567 84.927  1.00 66.60  ? 582 ASN A ND2 1 
ATOM   2775 N  N   . THR A 1 383 ? 91.643  159.318 85.457  1.00 60.24  ? 583 THR A N   1 
ATOM   2776 C  CA  . THR A 1 383 ? 90.477  158.951 84.661  1.00 60.24  ? 583 THR A CA  1 
ATOM   2777 C  C   . THR A 1 383 ? 89.376  159.995 84.781  1.00 60.24  ? 583 THR A C   1 
ATOM   2778 O  O   . THR A 1 383 ? 88.726  160.332 83.788  1.00 60.24  ? 583 THR A O   1 
ATOM   2779 C  CB  . THR A 1 383 ? 89.954  157.576 85.080  1.00 60.24  ? 583 THR A CB  1 
ATOM   2780 O  OG1 . THR A 1 383 ? 91.056  156.686 85.296  1.00 60.24  ? 583 THR A OG1 1 
ATOM   2781 C  CG2 . THR A 1 383 ? 89.040  157.004 84.004  1.00 60.24  ? 583 THR A CG2 1 
ATOM   2782 N  N   . SER A 1 384 ? 89.152  160.515 85.991  1.00 65.53  ? 584 SER A N   1 
ATOM   2783 C  CA  . SER A 1 384 ? 88.141  161.550 86.175  1.00 65.53  ? 584 SER A CA  1 
ATOM   2784 C  C   . SER A 1 384 ? 88.487  162.803 85.381  1.00 65.53  ? 584 SER A C   1 
ATOM   2785 O  O   . SER A 1 384 ? 87.623  163.393 84.722  1.00 65.53  ? 584 SER A O   1 
ATOM   2786 C  CB  . SER A 1 384 ? 87.983  161.880 87.659  1.00 65.53  ? 584 SER A CB  1 
ATOM   2787 O  OG  . SER A 1 384 ? 87.360  160.814 88.352  1.00 65.53  ? 584 SER A OG  1 
ATOM   2788 N  N   . GLU A 1 385 ? 89.769  163.153 85.429  1.00 69.59  ? 585 GLU A N   1 
ATOM   2789 C  CA  . GLU A 1 385 ? 90.289  164.329 84.689  1.00 69.59  ? 585 GLU A CA  1 
ATOM   2790 C  C   . GLU A 1 385 ? 90.086  164.181 83.183  1.00 69.59  ? 585 GLU A C   1 
ATOM   2791 O  O   . GLU A 1 385 ? 89.503  165.109 82.609  1.00 69.59  ? 585 GLU A O   1 
ATOM   2792 C  CB  . GLU A 1 385 ? 91.773  164.525 84.976  1.00 69.59  ? 585 GLU A CB  1 
ATOM   2793 C  CG  . GLU A 1 385 ? 92.053  165.240 86.286  1.00 69.59  ? 585 GLU A CG  1 
ATOM   2794 C  CD  . GLU A 1 385 ? 93.361  164.846 86.958  1.00 69.59  ? 585 GLU A CD  1 
ATOM   2795 O  OE1 . GLU A 1 385 ? 94.315  164.488 86.235  1.00 69.59  ? 585 GLU A OE1 1 
ATOM   2796 O  OE2 . GLU A 1 385 ? 93.422  164.894 88.204  1.00 69.59  ? 585 GLU A OE2 1 
ATOM   2797 N  N   . ILE A 1 386 ? 90.562  163.100 82.562  1.00 67.59  ? 586 ILE A N   1 
ATOM   2798 C  CA  . ILE A 1 386 ? 90.290  162.902 81.108  1.00 67.59  ? 586 ILE A CA  1 
ATOM   2799 C  C   . ILE A 1 386 ? 88.786  162.850 80.856  1.00 67.59  ? 586 ILE A C   1 
ATOM   2800 O  O   . ILE A 1 386 ? 88.337  163.461 79.883  1.00 67.59  ? 586 ILE A O   1 
ATOM   2801 C  CB  . ILE A 1 386 ? 90.972  161.636 80.539  1.00 67.59  ? 586 ILE A CB  1 
ATOM   2802 C  CG1 . ILE A 1 386 ? 92.422  161.474 81.004  1.00 67.59  ? 586 ILE A CG1 1 
ATOM   2803 C  CG2 . ILE A 1 386 ? 90.860  161.597 79.026  1.00 67.59  ? 586 ILE A CG2 1 
ATOM   2804 C  CD1 . ILE A 1 386 ? 92.878  160.039 81.049  1.00 67.59  ? 586 ILE A CD1 1 
ATOM   2805 N  N   . ILE A 1 387 ? 88.029  162.134 81.673  1.00 68.54  ? 587 ILE A N   1 
ATOM   2806 C  CA  . ILE A 1 387 ? 86.591  161.928 81.327  1.00 68.54  ? 587 ILE A CA  1 
ATOM   2807 C  C   . ILE A 1 387 ? 85.879  163.275 81.302  1.00 68.54  ? 587 ILE A C   1 
ATOM   2808 O  O   . ILE A 1 387 ? 85.195  163.546 80.312  1.00 68.54  ? 587 ILE A O   1 
ATOM   2809 C  CB  . ILE A 1 387 ? 85.932  160.888 82.253  1.00 68.54  ? 587 ILE A CB  1 
ATOM   2810 C  CG1 . ILE A 1 387 ? 86.280  159.467 81.807  1.00 68.54  ? 587 ILE A CG1 1 
ATOM   2811 C  CG2 . ILE A 1 387 ? 84.428  161.096 82.334  1.00 68.54  ? 587 ILE A CG2 1 
ATOM   2812 C  CD1 . ILE A 1 387 ? 85.791  158.394 82.736  1.00 68.54  ? 587 ILE A CD1 1 
ATOM   2813 N  N   . LYS A 1 388 ? 86.085  164.105 82.330  1.00 75.79  ? 588 LYS A N   1 
ATOM   2814 C  CA  . LYS A 1 388 ? 85.368  165.408 82.442  1.00 75.79  ? 588 LYS A CA  1 
ATOM   2815 C  C   . LYS A 1 388 ? 85.776  166.347 81.298  1.00 75.79  ? 588 LYS A C   1 
ATOM   2816 O  O   . LYS A 1 388 ? 84.868  167.004 80.755  1.00 75.79  ? 588 LYS A O   1 
ATOM   2817 C  CB  . LYS A 1 388 ? 85.592  166.010 83.832  1.00 75.79  ? 588 LYS A CB  1 
ATOM   2818 C  CG  . LYS A 1 388 ? 86.900  166.766 84.029  1.00 75.79  ? 588 LYS A CG  1 
ATOM   2819 C  CD  . LYS A 1 388 ? 87.223  167.084 85.471  1.00 75.79  ? 588 LYS A CD  1 
ATOM   2820 C  CE  . LYS A 1 388 ? 88.620  167.643 85.637  1.00 75.79  ? 588 LYS A CE  1 
ATOM   2821 N  NZ  . LYS A 1 388 ? 88.927  167.958 87.052  1.00 75.79  ? 588 LYS A NZ  1 
ATOM   2822 N  N   . GLU A 1 389 ? 87.063  166.396 80.939  1.00 78.74  ? 589 GLU A N   1 
ATOM   2823 C  CA  . GLU A 1 389 ? 87.535  167.216 79.792  1.00 78.74  ? 589 GLU A CA  1 
ATOM   2824 C  C   . GLU A 1 389 ? 86.891  166.769 78.491  1.00 78.74  ? 589 GLU A C   1 
ATOM   2825 O  O   . GLU A 1 389 ? 86.271  167.603 77.838  1.00 78.74  ? 589 GLU A O   1 
ATOM   2826 C  CB  . GLU A 1 389 ? 89.035  167.053 79.573  1.00 78.74  ? 589 GLU A CB  1 
ATOM   2827 C  CG  . GLU A 1 389 ? 89.862  168.032 80.379  1.00 78.74  ? 589 GLU A CG  1 
ATOM   2828 C  CD  . GLU A 1 389 ? 91.166  167.466 80.909  1.00 78.74  ? 589 GLU A CD  1 
ATOM   2829 O  OE1 . GLU A 1 389 ? 91.837  168.167 81.694  1.00 78.74  ? 589 GLU A OE1 1 
ATOM   2830 O  OE2 . GLU A 1 389 ? 91.510  166.326 80.533  1.00 78.74  ? 589 GLU A OE2 1 
ATOM   2831 N  N   . GLN A 1 390 ? 87.059  165.505 78.127  1.00 72.30  ? 590 GLN A N   1 
ATOM   2832 C  CA  . GLN A 1 390 ? 86.531  165.004 76.832  1.00 72.30  ? 590 GLN A CA  1 
ATOM   2833 C  C   . GLN A 1 390 ? 85.066  165.431 76.713  1.00 72.30  ? 590 GLN A C   1 
ATOM   2834 O  O   . GLN A 1 390 ? 84.780  166.111 75.739  1.00 72.30  ? 590 GLN A O   1 
ATOM   2835 C  CB  . GLN A 1 390 ? 86.781  163.503 76.738  1.00 72.30  ? 590 GLN A CB  1 
ATOM   2836 C  CG  . GLN A 1 390 ? 87.921  163.101 75.821  1.00 72.30  ? 590 GLN A CG  1 
ATOM   2837 C  CD  . GLN A 1 390 ? 87.750  161.673 75.365  1.00 72.30  ? 590 GLN A CD  1 
ATOM   2838 O  OE1 . GLN A 1 390 ? 88.447  160.767 75.816  1.00 72.30  ? 590 GLN A OE1 1 
ATOM   2839 N  NE2 . GLN A 1 390 ? 86.805  161.458 74.462  1.00 72.30  ? 590 GLN A NE2 1 
ATOM   2840 N  N   . LEU A 1 391 ? 84.224  165.174 77.721  1.00 78.76  ? 591 LEU A N   1 
ATOM   2841 C  CA  . LEU A 1 391 ? 82.780  165.550 77.727  1.00 78.76  ? 591 LEU A CA  1 
ATOM   2842 C  C   . LEU A 1 391 ? 82.579  167.011 77.307  1.00 78.76  ? 591 LEU A C   1 
ATOM   2843 O  O   . LEU A 1 391 ? 81.625  167.269 76.553  1.00 78.76  ? 591 LEU A O   1 
ATOM   2844 C  CB  . LEU A 1 391 ? 82.195  165.342 79.129  1.00 78.76  ? 591 LEU A CB  1 
ATOM   2845 C  CG  . LEU A 1 391 ? 81.949  163.905 79.568  1.00 78.76  ? 591 LEU A CG  1 
ATOM   2846 C  CD1 . LEU A 1 391 ? 81.354  163.875 80.965  1.00 78.76  ? 591 LEU A CD1 1 
ATOM   2847 C  CD2 . LEU A 1 391 ? 81.042  163.194 78.584  1.00 78.76  ? 591 LEU A CD2 1 
ATOM   2848 N  N   . LYS A 1 392 ? 83.442  167.934 77.747  1.00 85.23  ? 592 LYS A N   1 
ATOM   2849 C  CA  . LYS A 1 392 ? 83.241  169.388 77.451  1.00 85.23  ? 592 LYS A CA  1 
ATOM   2850 C  C   . LYS A 1 392 ? 83.400  169.683 75.947  1.00 85.23  ? 592 LYS A C   1 
ATOM   2851 O  O   . LYS A 1 392 ? 83.186  170.848 75.565  1.00 85.23  ? 592 LYS A O   1 
ATOM   2852 C  CB  . LYS A 1 392 ? 84.145  170.249 78.342  1.00 85.23  ? 592 LYS A CB  1 
ATOM   2853 C  CG  . LYS A 1 392 ? 85.456  170.725 77.730  1.00 85.23  ? 592 LYS A CG  1 
ATOM   2854 C  CD  . LYS A 1 392 ? 86.477  171.141 78.766  1.00 85.23  ? 592 LYS A CD  1 
ATOM   2855 C  CE  . LYS A 1 392 ? 87.899  170.841 78.338  1.00 85.23  ? 592 LYS A CE  1 
ATOM   2856 N  NZ  . LYS A 1 392 ? 88.894  171.335 79.319  1.00 85.23  ? 592 LYS A NZ  1 
ATOM   2857 N  N   . TYR A 1 393 ? 83.703  168.680 75.119  1.00 90.91  ? 593 TYR A N   1 
ATOM   2858 C  CA  . TYR A 1 393 ? 83.784  168.881 73.647  1.00 90.91  ? 593 TYR A CA  1 
ATOM   2859 C  C   . TYR A 1 393 ? 82.778  167.992 72.904  1.00 90.91  ? 593 TYR A C   1 
ATOM   2860 O  O   . TYR A 1 393 ? 82.949  167.841 71.683  1.00 90.91  ? 593 TYR A O   1 
ATOM   2861 C  CB  . TYR A 1 393 ? 85.190  168.562 73.139  1.00 90.91  ? 593 TYR A CB  1 
ATOM   2862 C  CG  . TYR A 1 393 ? 86.288  169.432 73.694  1.00 90.91  ? 593 TYR A CG  1 
ATOM   2863 C  CD1 . TYR A 1 393 ? 86.327  170.789 73.430  1.00 90.91  ? 593 TYR A CD1 1 
ATOM   2864 C  CD2 . TYR A 1 393 ? 87.299  168.892 74.470  1.00 90.91  ? 593 TYR A CD2 1 
ATOM   2865 C  CE1 . TYR A 1 393 ? 87.335  171.594 73.934  1.00 90.91  ? 593 TYR A CE1 1 
ATOM   2866 C  CE2 . TYR A 1 393 ? 88.316  169.681 74.979  1.00 90.91  ? 593 TYR A CE2 1 
ATOM   2867 C  CZ  . TYR A 1 393 ? 88.333  171.037 74.712  1.00 90.91  ? 593 TYR A CZ  1 
ATOM   2868 N  N   . LEU A 1 394 ? 81.801  167.426 73.612  1.00 93.51  ? 594 LEU A N   1 
ATOM   2869 C  CA  . LEU A 1 394 ? 80.854  166.470 72.983  1.00 93.51  ? 594 LEU A CA  1 
ATOM   2870 C  C   . LEU A 1 394 ? 79.439  167.050 73.008  1.00 93.51  ? 594 LEU A C   1 
ATOM   2871 O  O   . LEU A 1 394 ? 79.092  167.723 73.993  1.00 93.51  ? 594 LEU A O   1 
ATOM   2872 C  CB  . LEU A 1 394 ? 80.908  165.157 73.769  1.00 93.51  ? 594 LEU A CB  1 
ATOM   2873 C  CG  . LEU A 1 394 ? 82.005  164.166 73.382  1.00 93.51  ? 594 LEU A CG  1 
ATOM   2874 C  CD1 . LEU A 1 394 ? 83.378  164.736 73.704  1.00 93.51  ? 594 LEU A CD1 1 
ATOM   2875 C  CD2 . LEU A 1 394 ? 81.806  162.838 74.097  1.00 93.51  ? 594 LEU A CD2 1 
ATOM   2876 N  N   . ASP A 1 395 ? 78.655  166.789 71.962  1.00 98.15  ? 595 ASP A N   1 
ATOM   2877 C  CA  . ASP A 1 395 ? 77.240  167.244 71.932  1.00 98.15  ? 595 ASP A CA  1 
ATOM   2878 C  C   . ASP A 1 395 ? 76.517  166.587 73.106  1.00 98.15  ? 595 ASP A C   1 
ATOM   2879 O  O   . ASP A 1 395 ? 75.827  167.315 73.845  1.00 98.15  ? 595 ASP A O   1 
ATOM   2880 C  CB  . ASP A 1 395 ? 76.597  166.947 70.573  1.00 98.15  ? 595 ASP A CB  1 
ATOM   2881 C  CG  . ASP A 1 395 ? 76.699  165.499 70.115  1.00 98.15  ? 595 ASP A CG  1 
ATOM   2882 O  OD1 . ASP A 1 395 ? 75.714  165.004 69.537  1.00 98.15  ? 595 ASP A OD1 1 
ATOM   2883 O  OD2 . ASP A 1 395 ? 77.760  164.879 70.329  1.00 98.15  ? 595 ASP A OD2 1 
ATOM   2884 N  N   . ASP A 1 396 ? 76.667  165.266 73.267  1.00 91.10  ? 596 ASP A N   1 
ATOM   2885 C  CA  . ASP A 1 396 ? 76.107  164.555 74.444  1.00 91.10  ? 596 ASP A CA  1 
ATOM   2886 C  C   . ASP A 1 396 ? 77.088  164.723 75.597  1.00 91.10  ? 596 ASP A C   1 
ATOM   2887 O  O   . ASP A 1 396 ? 78.254  165.048 75.334  1.00 91.10  ? 596 ASP A O   1 
ATOM   2888 C  CB  . ASP A 1 396 ? 75.920  163.065 74.166  1.00 91.10  ? 596 ASP A CB  1 
ATOM   2889 C  CG  . ASP A 1 396 ? 74.793  162.748 73.200  1.00 91.10  ? 596 ASP A CG  1 
ATOM   2890 O  OD1 . ASP A 1 396 ? 73.965  163.644 72.954  1.00 91.10  ? 596 ASP A OD1 1 
ATOM   2891 O  OD2 . ASP A 1 396 ? 74.760  161.610 72.698  1.00 91.10  ? 596 ASP A OD2 1 
ATOM   2892 N  N   . LYS A 1 397 ? 76.644  164.543 76.831  1.00 86.10  ? 597 LYS A N   1 
ATOM   2893 C  CA  . LYS A 1 397 ? 77.619  164.582 77.950  1.00 86.10  ? 597 LYS A CA  1 
ATOM   2894 C  C   . LYS A 1 397 ? 77.619  163.194 78.588  1.00 86.10  ? 597 LYS A C   1 
ATOM   2895 O  O   . LYS A 1 397 ? 77.962  163.099 79.774  1.00 86.10  ? 597 LYS A O   1 
ATOM   2896 C  CB  . LYS A 1 397 ? 77.312  165.729 78.916  1.00 86.10  ? 597 LYS A CB  1 
ATOM   2897 C  CG  . LYS A 1 397 ? 78.277  166.906 78.854  1.00 86.10  ? 597 LYS A CG  1 
ATOM   2898 C  CD  . LYS A 1 397 ? 78.164  167.711 77.579  1.00 86.10  ? 597 LYS A CD  1 
ATOM   2899 C  CE  . LYS A 1 397 ? 78.973  168.989 77.612  1.00 86.10  ? 597 LYS A CE  1 
ATOM   2900 N  NZ  . LYS A 1 397 ? 79.446  169.370 76.261  1.00 86.10  ? 597 LYS A NZ  1 
ATOM   2901 N  N   . LYS A 1 398 ? 77.260  162.169 77.807  1.00 71.33  ? 598 LYS A N   1 
ATOM   2902 C  CA  . LYS A 1 398 ? 77.268  160.766 78.289  1.00 71.33  ? 598 LYS A CA  1 
ATOM   2903 C  C   . LYS A 1 398 ? 78.702  160.240 78.371  1.00 71.33  ? 598 LYS A C   1 
ATOM   2904 O  O   . LYS A 1 398 ? 79.358  160.216 77.338  1.00 71.33  ? 598 LYS A O   1 
ATOM   2905 C  CB  . LYS A 1 398 ? 76.381  159.920 77.373  1.00 71.33  ? 598 LYS A CB  1 
ATOM   2906 C  CG  . LYS A 1 398 ? 74.888  160.066 77.608  1.00 71.33  ? 598 LYS A CG  1 
ATOM   2907 C  CD  . LYS A 1 398 ? 74.103  160.238 76.335  1.00 71.33  ? 598 LYS A CD  1 
ATOM   2908 C  CE  . LYS A 1 398 ? 72.620  160.013 76.531  1.00 71.33  ? 598 LYS A CE  1 
ATOM   2909 N  NZ  . LYS A 1 398 ? 72.306  158.579 76.732  1.00 71.33  ? 598 LYS A NZ  1 
ATOM   2910 N  N   . ILE A 1 399 ? 79.156  159.834 79.555  1.00 59.62  ? 599 ILE A N   1 
ATOM   2911 C  CA  . ILE A 1 399 ? 80.499  159.233 79.804  1.00 59.62  ? 599 ILE A CA  1 
ATOM   2912 C  C   . ILE A 1 399 ? 80.660  157.968 78.976  1.00 59.62  ? 599 ILE A C   1 
ATOM   2913 O  O   . ILE A 1 399 ? 81.780  157.651 78.602  1.00 59.62  ? 599 ILE A O   1 
ATOM   2914 C  CB  . ILE A 1 399 ? 80.600  158.935 81.313  1.00 59.62  ? 599 ILE A CB  1 
ATOM   2915 C  CG1 . ILE A 1 399 ? 80.742  160.224 82.124  1.00 59.62  ? 599 ILE A CG1 1 
ATOM   2916 C  CG2 . ILE A 1 399 ? 81.696  157.934 81.646  1.00 59.62  ? 599 ILE A CG2 1 
ATOM   2917 C  CD1 . ILE A 1 399 ? 80.389  160.066 83.579  1.00 59.62  ? 599 ILE A CD1 1 
ATOM   2918 N  N   . TYR A 1 400 ? 79.559  157.290 78.690  1.00 53.48  ? 600 TYR A N   1 
ATOM   2919 C  CA  . TYR A 1 400 ? 79.607  156.029 77.921  1.00 53.48  ? 600 TYR A CA  1 
ATOM   2920 C  C   . TYR A 1 400 ? 79.999  156.366 76.476  1.00 53.48  ? 600 TYR A C   1 
ATOM   2921 O  O   . TYR A 1 400 ? 80.402  155.454 75.755  1.00 53.48  ? 600 TYR A O   1 
ATOM   2922 C  CB  . TYR A 1 400 ? 78.298  155.262 78.133  1.00 53.48  ? 600 TYR A CB  1 
ATOM   2923 C  CG  . TYR A 1 400 ? 78.213  154.356 79.335  1.00 53.48  ? 600 TYR A CG  1 
ATOM   2924 C  CD1 . TYR A 1 400 ? 78.928  154.609 80.493  1.00 53.48  ? 600 TYR A CD1 1 
ATOM   2925 C  CD2 . TYR A 1 400 ? 77.376  153.252 79.326  1.00 53.48  ? 600 TYR A CD2 1 
ATOM   2926 C  CE1 . TYR A 1 400 ? 78.822  153.786 81.601  1.00 53.48  ? 600 TYR A CE1 1 
ATOM   2927 C  CE2 . TYR A 1 400 ? 77.263  152.413 80.421  1.00 53.48  ? 600 TYR A CE2 1 
ATOM   2928 C  CZ  . TYR A 1 400 ? 77.989  152.682 81.566  1.00 53.48  ? 600 TYR A CZ  1 
ATOM   2929 N  N   . ASN A 1 401 ? 79.889  157.637 76.073  1.00 56.11  ? 601 ASN A N   1 
ATOM   2930 C  CA  . ASN A 1 401 ? 80.322  158.064 74.749  1.00 56.11  ? 601 ASN A CA  1 
ATOM   2931 C  C   . ASN A 1 401 ? 81.772  158.530 74.721  1.00 56.11  ? 601 ASN A C   1 
ATOM   2932 O  O   . ASN A 1 401 ? 82.280  158.859 73.644  1.00 56.11  ? 601 ASN A O   1 
ATOM   2933 C  CB  . ASN A 1 401 ? 79.412  159.181 74.230  1.00 56.11  ? 601 ASN A CB  1 
ATOM   2934 C  CG  . ASN A 1 401 ? 78.167  158.650 73.546  1.00 56.11  ? 601 ASN A CG  1 
ATOM   2935 O  OD1 . ASN A 1 401 ? 77.770  157.505 73.758  1.00 56.11  ? 601 ASN A OD1 1 
ATOM   2936 N  ND2 . ASN A 1 401 ? 77.545  159.482 72.719  1.00 56.11  ? 601 ASN A ND2 1 
ATOM   2937 N  N   . VAL A 1 402 ? 82.443  158.569 75.867  1.00 51.87  ? 602 VAL A N   1 
ATOM   2938 C  CA  . VAL A 1 402 ? 83.837  158.992 75.933  1.00 51.87  ? 602 VAL A CA  1 
ATOM   2939 C  C   . VAL A 1 402 ? 84.725  157.880 75.394  1.00 51.87  ? 602 VAL A C   1 
ATOM   2940 O  O   . VAL A 1 402 ? 84.541  156.701 75.722  1.00 51.87  ? 602 VAL A O   1 
ATOM   2941 C  CB  . VAL A 1 402 ? 84.216  159.367 77.378  1.00 51.87  ? 602 VAL A CB  1 
ATOM   2942 C  CG1 . VAL A 1 402 ? 85.727  159.399 77.554  1.00 51.87  ? 602 VAL A CG1 1 
ATOM   2943 C  CG2 . VAL A 1 402 ? 83.600  160.706 77.757  1.00 51.87  ? 602 VAL A CG2 1 
ATOM   2944 N  N   . LYS A 1 403 ? 85.684  158.250 74.546  1.00 46.37  ? 603 LYS A N   1 
ATOM   2945 C  CA  . LYS A 1 403 ? 86.607  157.271 73.985  1.00 46.37  ? 603 LYS A CA  1 
ATOM   2946 C  C   . LYS A 1 403 ? 87.465  156.651 75.081  1.00 46.37  ? 603 LYS A C   1 
ATOM   2947 O  O   . LYS A 1 403 ? 88.014  157.356 75.932  1.00 46.37  ? 603 LYS A O   1 
ATOM   2948 C  CB  . LYS A 1 403 ? 87.495  157.931 72.929  1.00 46.37  ? 603 LYS A CB  1 
ATOM   2949 C  CG  . LYS A 1 403 ? 86.741  158.484 71.731  1.00 46.37  ? 603 LYS A CG  1 
ATOM   2950 C  CD  . LYS A 1 403 ? 85.694  157.503 71.232  1.00 46.37  ? 603 LYS A CD  1 
ATOM   2951 C  CE  . LYS A 1 403 ? 86.072  156.942 69.871  1.00 46.37  ? 603 LYS A CE  1 
ATOM   2952 N  NZ  . LYS A 1 403 ? 85.009  156.056 69.323  1.00 46.37  ? 603 LYS A NZ  1 
ATOM   2953 N  N   . LEU A 1 404 ? 87.578  155.326 75.056  1.00 39.17  ? 604 LEU A N   1 
ATOM   2954 C  CA  . LEU A 1 404 ? 88.400  154.624 76.030  1.00 39.17  ? 604 LEU A CA  1 
ATOM   2955 C  C   . LEU A 1 404 ? 89.880  154.848 75.739  1.00 39.17  ? 604 LEU A C   1 
ATOM   2956 O  O   . LEU A 1 404 ? 90.304  154.885 74.581  1.00 39.17  ? 604 LEU A O   1 
ATOM   2957 C  CB  . LEU A 1 404 ? 88.077  153.130 76.018  1.00 39.17  ? 604 LEU A CB  1 
ATOM   2958 C  CG  . LEU A 1 404 ? 88.787  152.258 77.054  1.00 39.17  ? 604 LEU A CG  1 
ATOM   2959 C  CD1 . LEU A 1 404 ? 87.901  152.032 78.269  1.00 39.17  ? 604 LEU A CD1 1 
ATOM   2960 C  CD2 . LEU A 1 404 ? 89.207  150.934 76.441  1.00 39.17  ? 604 LEU A CD2 1 
ATOM   2961 N  N   . GLU A 1 405 ? 90.667  155.003 76.803  1.00 39.79  ? 605 GLU A N   1 
ATOM   2962 C  CA  . GLU A 1 405 ? 92.101  155.225 76.685  1.00 39.79  ? 605 GLU A CA  1 
ATOM   2963 C  C   . GLU A 1 405 ? 92.857  154.274 77.601  1.00 39.79  ? 605 GLU A C   1 
ATOM   2964 O  O   . GLU A 1 405 ? 92.324  153.783 78.599  1.00 39.79  ? 605 GLU A O   1 
ATOM   2965 C  CB  . GLU A 1 405 ? 92.481  156.678 77.014  1.00 39.79  ? 605 GLU A CB  1 
ATOM   2966 C  CG  . GLU A 1 405 ? 92.220  157.657 75.881  1.00 39.79  ? 605 GLU A CG  1 
ATOM   2967 C  CD  . GLU A 1 405 ? 91.851  159.040 76.373  1.00 39.79  ? 605 GLU A CD  1 
ATOM   2968 O  OE1 . GLU A 1 405 ? 90.706  159.221 76.834  1.00 39.79  ? 605 GLU A OE1 1 
ATOM   2969 O  OE2 . GLU A 1 405 ? 92.705  159.950 76.292  1.00 39.79  ? 605 GLU A OE2 1 
ATOM   2970 N  N   . ARG A 1 406 ? 94.112  154.020 77.241  1.00 30.86  ? 606 ARG A N   1 
ATOM   2971 C  CA  . ARG A 1 406 ? 94.952  153.102 77.997  1.00 30.86  ? 606 ARG A CA  1 
ATOM   2972 C  C   . ARG A 1 406 ? 95.339  153.718 79.336  1.00 30.86  ? 606 ARG A C   1 
ATOM   2973 O  O   . ARG A 1 406 ? 95.721  154.890 79.406  1.00 30.86  ? 606 ARG A O   1 
ATOM   2974 C  CB  . ARG A 1 406 ? 96.197  152.751 77.181  1.00 30.86  ? 606 ARG A CB  1 
ATOM   2975 C  CG  . ARG A 1 406 ? 97.410  152.337 77.991  1.00 30.86  ? 606 ARG A CG  1 
ATOM   2976 C  CD  . ARG A 1 406 ? 98.643  152.304 77.101  1.00 30.86  ? 606 ARG A CD  1 
ATOM   2977 N  NE  . ARG A 1 406 ? 98.396  151.560 75.872  1.00 30.86  ? 606 ARG A NE  1 
ATOM   2978 C  CZ  . ARG A 1 406 ? 99.338  150.977 75.143  1.00 30.86  ? 606 ARG A CZ  1 
ATOM   2979 N  N   . GLY A 1 407 ? 95.238  152.924 80.400  1.00 33.58  ? 607 GLY A N   1 
ATOM   2980 C  CA  . GLY A 1 407 ? 95.531  153.385 81.740  1.00 33.58  ? 607 GLY A CA  1 
ATOM   2981 C  C   . GLY A 1 407 ? 94.325  153.779 82.563  1.00 33.58  ? 607 GLY A C   1 
ATOM   2982 O  O   . GLY A 1 407 ? 94.486  154.118 83.742  1.00 33.58  ? 607 GLY A O   1 
ATOM   2983 N  N   . MET A 1 408 ? 93.128  153.748 81.985  1.00 37.77  ? 608 MET A N   1 
ATOM   2984 C  CA  . MET A 1 408 ? 91.923  154.093 82.726  1.00 37.77  ? 608 MET A CA  1 
ATOM   2985 C  C   . MET A 1 408 ? 91.575  153.004 83.735  1.00 37.77  ? 608 MET A C   1 
ATOM   2986 O  O   . MET A 1 408 ? 91.839  151.817 83.523  1.00 37.77  ? 608 MET A O   1 
ATOM   2987 C  CB  . MET A 1 408 ? 90.749  154.305 81.770  1.00 37.77  ? 608 MET A CB  1 
ATOM   2988 C  CG  . MET A 1 408 ? 90.812  155.595 80.969  1.00 37.77  ? 608 MET A CG  1 
ATOM   2989 S  SD  . MET A 1 408 ? 89.337  155.839 79.962  1.00 37.77  ? 608 MET A SD  1 
ATOM   2990 C  CE  . MET A 1 408 ? 89.390  157.608 79.702  1.00 37.77  ? 608 MET A CE  1 
ATOM   2991 N  N   . ASN A 1 409 ? 90.975  153.425 84.846  1.00 40.23  ? 609 ASN A N   1 
ATOM   2992 C  CA  . ASN A 1 409 ? 90.460  152.517 85.866  1.00 40.23  ? 609 ASN A CA  1 
ATOM   2993 C  C   . ASN A 1 409 ? 89.005  152.885 86.118  1.00 40.23  ? 609 ASN A C   1 
ATOM   2994 O  O   . ASN A 1 409 ? 88.717  153.973 86.627  1.00 40.23  ? 609 ASN A O   1 
ATOM   2995 C  CB  . ASN A 1 409 ? 91.279  152.601 87.155  1.00 40.23  ? 609 ASN A CB  1 
ATOM   2996 C  CG  . ASN A 1 409 ? 92.633  151.935 87.029  1.00 40.23  ? 609 ASN A CG  1 
ATOM   2997 O  OD1 . ASN A 1 409 ? 92.733  150.708 86.977  1.00 40.23  ? 609 ASN A OD1 1 
ATOM   2998 N  ND2 . ASN A 1 409 ? 93.688  152.740 86.983  1.00 40.23  ? 609 ASN A ND2 1 
ATOM   2999 N  N   . ILE A 1 410 ? 88.089  151.985 85.766  1.00 38.10  ? 610 ILE A N   1 
ATOM   3000 C  CA  . ILE A 1 410 ? 86.656  152.237 85.862  1.00 38.10  ? 610 ILE A CA  1 
ATOM   3001 C  C   . ILE A 1 410 ? 86.043  151.186 86.774  1.00 38.10  ? 610 ILE A C   1 
ATOM   3002 O  O   . ILE A 1 410 ? 86.341  149.994 86.639  1.00 38.10  ? 610 ILE A O   1 
ATOM   3003 C  CB  . ILE A 1 410 ? 85.985  152.224 84.475  1.00 38.10  ? 610 ILE A CB  1 
ATOM   3004 C  CG1 . ILE A 1 410 ? 86.487  153.395 83.628  1.00 38.10  ? 610 ILE A CG1 1 
ATOM   3005 C  CG2 . ILE A 1 410 ? 84.471  152.273 84.606  1.00 38.10  ? 610 ILE A CG2 1 
ATOM   3006 C  CD1 . ILE A 1 410 ? 86.564  153.091 82.148  1.00 38.10  ? 610 ILE A CD1 1 
ATOM   3007 N  N   . LEU A 1 411 ? 85.202  151.627 87.709  1.00 42.07  ? 611 LEU A N   1 
ATOM   3008 C  CA  . LEU A 1 411 ? 84.475  150.729 88.597  1.00 42.07  ? 611 LEU A CA  1 
ATOM   3009 C  C   . LEU A 1 411 ? 82.987  151.020 88.476  1.00 42.07  ? 611 LEU A C   1 
ATOM   3010 O  O   . LEU A 1 411 ? 82.548  152.148 88.718  1.00 42.07  ? 611 LEU A O   1 
ATOM   3011 C  CB  . LEU A 1 411 ? 84.944  150.886 90.045  1.00 42.07  ? 611 LEU A CB  1 
ATOM   3012 C  CG  . LEU A 1 411 ? 84.113  150.166 91.109  1.00 42.07  ? 611 LEU A CG  1 
ATOM   3013 C  CD1 . LEU A 1 411 ? 84.216  148.659 90.942  1.00 42.07  ? 611 LEU A CD1 1 
ATOM   3014 C  CD2 . LEU A 1 411 ? 84.558  150.580 92.501  1.00 42.07  ? 611 LEU A CD2 1 
ATOM   3015 N  N   . ILE A 1 412 ? 82.219  150.003 88.102  1.00 45.87  ? 612 ILE A N   1 
ATOM   3016 C  CA  . ILE A 1 412 ? 80.770  150.087 87.986  1.00 45.87  ? 612 ILE A CA  1 
ATOM   3017 C  C   . ILE A 1 412 ? 80.171  149.368 89.184  1.00 45.87  ? 612 ILE A C   1 
ATOM   3018 O  O   . ILE A 1 412 ? 80.557  148.233 89.491  1.00 45.87  ? 612 ILE A O   1 
ATOM   3019 C  CB  . ILE A 1 412 ? 80.275  149.473 86.667  1.00 45.87  ? 612 ILE A CB  1 
ATOM   3020 C  CG1 . ILE A 1 412 ? 80.953  150.149 85.474  1.00 45.87  ? 612 ILE A CG1 1 
ATOM   3021 C  CG2 . ILE A 1 412 ? 78.765  149.567 86.565  1.00 45.87  ? 612 ILE A CG2 1 
ATOM   3022 C  CD1 . ILE A 1 412 ? 81.276  149.200 84.343  1.00 45.87  ? 612 ILE A CD1 1 
ATOM   3023 N  N   . LYS A 1 413 ? 79.268  150.047 89.895  1.00 59.01  ? 613 LYS A N   1 
ATOM   3024 C  CA  . LYS A 1 413 ? 78.613  149.469 91.095  1.00 59.01  ? 613 LYS A CA  1 
ATOM   3025 C  C   . LYS A 1 413 ? 77.109  149.463 90.894  1.00 59.01  ? 613 LYS A C   1 
ATOM   3026 O  O   . LYS A 1 413 ? 76.573  150.515 90.606  1.00 59.01  ? 613 LYS A O   1 
ATOM   3027 C  CB  . LYS A 1 413 ? 78.959  150.260 92.349  1.00 59.01  ? 613 LYS A CB  1 
ATOM   3028 C  CG  . LYS A 1 413 ? 80.369  150.058 92.879  1.00 59.01  ? 613 LYS A CG  1 
ATOM   3029 C  CD  . LYS A 1 413 ? 80.475  150.269 94.372  1.00 59.01  ? 613 LYS A CD  1 
ATOM   3030 C  CE  . LYS A 1 413 ? 80.506  148.973 95.153  1.00 59.01  ? 613 LYS A CE  1 
ATOM   3031 N  NZ  . LYS A 1 413 ? 79.192  148.285 95.142  1.00 59.01  ? 613 LYS A NZ  1 
ATOM   3032 N  N   . VAL A 1 414 ? 76.518  148.282 90.816  1.00 66.86  ? 614 VAL A N   1 
ATOM   3033 C  CA  . VAL A 1 414 ? 75.047  148.166 90.698  1.00 66.86  ? 614 VAL A CA  1 
ATOM   3034 C  C   . VAL A 1 414 ? 74.462  148.590 92.041  1.00 66.86  ? 614 VAL A C   1 
ATOM   3035 O  O   . VAL A 1 414 ? 74.922  148.089 93.074  1.00 66.86  ? 614 VAL A O   1 
ATOM   3036 C  CB  . VAL A 1 414 ? 74.622  146.750 90.269  1.00 66.86  ? 614 VAL A CB  1 
ATOM   3037 C  CG1 . VAL A 1 414 ? 73.126  146.528 90.400  1.00 66.86  ? 614 VAL A CG1 1 
ATOM   3038 C  CG2 . VAL A 1 414 ? 75.111  146.411 88.871  1.00 66.86  ? 614 VAL A CG2 1 
ATOM   3039 N  N   . PRO A 1 415 ? 73.499  149.531 92.052  1.00 86.76  ? 615 PRO A N   1 
ATOM   3040 C  CA  . PRO A 1 415 ? 72.849  149.998 93.287  1.00 86.76  ? 615 PRO A CA  1 
ATOM   3041 C  C   . PRO A 1 415 ? 72.110  148.978 94.167  1.00 86.76  ? 615 PRO A C   1 
ATOM   3042 O  O   . PRO A 1 415 ? 71.455  148.124 93.632  1.00 86.76  ? 615 PRO A O   1 
ATOM   3043 C  CB  . PRO A 1 415 ? 71.782  150.964 92.749  1.00 30.00  ? 615 PRO A CB  1 
ATOM   3044 C  CG  . PRO A 1 415 ? 71.562  150.534 91.327  1.00 30.00  ? 615 PRO A CG  1 
ATOM   3045 C  CD  . PRO A 1 415 ? 72.956  150.181 90.866  1.00 30.00  ? 615 PRO A CD  1 
ATOM   3046 N  N   . SER A 1 416 ? 72.267  149.083 95.487  1.00 99.40  ? 616 SER A N   1 
ATOM   3047 C  CA  . SER A 1 416 ? 71.527  148.222 96.448  1.00 99.40  ? 616 SER A CA  1 
ATOM   3048 C  C   . SER A 1 416 ? 70.043  148.560 96.347  1.00 99.40  ? 616 SER A C   1 
ATOM   3049 O  O   . SER A 1 416 ? 69.236  147.617 96.288  1.00 99.40  ? 616 SER A O   1 
ATOM   3050 C  CB  . SER A 1 416 ? 72.002  148.417 97.863  1.00 99.40  ? 616 SER A CB  1 
ATOM   3051 O  OG  . SER A 1 416 ? 73.416  148.377 97.950  1.00 99.40  ? 616 SER A OG  1 
ATOM   3052 N  N   . TYR A 1 417 ? 69.699  149.856 96.286  1.00 108.67 ? 617 TYR A N   1 
ATOM   3053 C  CA  . TYR A 1 417 ? 68.297  150.188 96.084  1.00 108.67 ? 617 TYR A CA  1 
ATOM   3054 C  C   . TYR A 1 417 ? 68.176  151.119 94.889  1.00 108.67 ? 617 TYR A C   1 
ATOM   3055 O  O   . TYR A 1 417 ? 69.024  151.993 94.691  1.00 108.67 ? 617 TYR A O   1 
ATOM   3056 C  CB  . TYR A 1 417 ? 67.696  150.850 97.329  1.00 108.67 ? 617 TYR A CB  1 
ATOM   3057 C  CG  . TYR A 1 417 ? 67.719  149.976 98.562  1.00 108.67 ? 617 TYR A CG  1 
ATOM   3058 C  CD1 . TYR A 1 417 ? 67.102  148.732 98.566  1.00 108.67 ? 617 TYR A CD1 1 
ATOM   3059 C  CD2 . TYR A 1 417 ? 68.354  150.397 99.722  1.00 108.67 ? 617 TYR A CD2 1 
ATOM   3060 C  CE1 . TYR A 1 417 ? 67.120  147.930 99.691  1.00 108.67 ? 617 TYR A CE1 1 
ATOM   3061 C  CE2 . TYR A 1 417 ? 68.377  149.602 100.853 1.00 108.67 ? 617 TYR A CE2 1 
ATOM   3062 C  CZ  . TYR A 1 417 ? 67.758  148.370 100.832 1.00 108.67 ? 617 TYR A CZ  1 
ATOM   3063 N  N   . PHE A 1 418 ? 67.121  150.941 94.097  1.00 110.83 ? 618 PHE A N   1 
ATOM   3064 C  CA  . PHE A 1 418 ? 66.928  151.768 92.916  1.00 110.83 ? 618 PHE A CA  1 
ATOM   3065 C  C   . PHE A 1 418 ? 65.444  151.870 92.600  1.00 110.83 ? 618 PHE A C   1 
ATOM   3066 O  O   . PHE A 1 418 ? 64.685  150.916 92.792  1.00 110.83 ? 618 PHE A O   1 
ATOM   3067 C  CB  . PHE A 1 418 ? 67.687  151.208 91.707  1.00 110.83 ? 618 PHE A CB  1 
ATOM   3068 C  CG  . PHE A 1 418 ? 67.540  152.035 90.462  1.00 110.83 ? 618 PHE A CG  1 
ATOM   3069 C  CD1 . PHE A 1 418 ? 68.243  153.220 90.316  1.00 110.83 ? 618 PHE A CD1 1 
ATOM   3070 C  CD2 . PHE A 1 418 ? 66.702  151.628 89.438  1.00 110.83 ? 618 PHE A CD2 1 
ATOM   3071 C  CE1 . PHE A 1 418 ? 68.111  153.983 89.171  1.00 110.83 ? 618 PHE A CE1 1 
ATOM   3072 C  CE2 . PHE A 1 418 ? 66.567  152.387 88.291  1.00 110.83 ? 618 PHE A CE2 1 
ATOM   3073 C  CZ  . PHE A 1 418 ? 67.272  153.566 88.157  1.00 110.83 ? 618 PHE A CZ  1 
ATOM   3074 N  N   . THR A 1 419 ? 65.039  153.042 92.114  1.00 116.61 ? 619 THR A N   1 
ATOM   3075 C  CA  . THR A 1 419 ? 63.668  153.248 91.666  1.00 116.61 ? 619 THR A CA  1 
ATOM   3076 C  C   . THR A 1 419 ? 63.666  154.199 90.477  1.00 116.61 ? 619 THR A C   1 
ATOM   3077 O  O   . THR A 1 419 ? 64.344  155.234 90.496  1.00 116.61 ? 619 THR A O   1 
ATOM   3078 C  CB  . THR A 1 419 ? 62.780  153.797 92.792  1.00 116.61 ? 619 THR A CB  1 
ATOM   3079 O  OG1 . THR A 1 419 ? 61.510  154.187 92.254  1.00 116.61 ? 619 THR A OG1 1 
ATOM   3080 C  CG2 . THR A 1 419 ? 63.429  154.996 93.469  1.00 116.61 ? 619 THR A CG2 1 
ATOM   3081 N  N   . ASN A 1 420 ? 62.911  153.827 89.443  1.00 120.07 ? 620 ASN A N   1 
ATOM   3082 C  CA  . ASN A 1 420 ? 62.701  154.654 88.264  1.00 120.07 ? 620 ASN A CA  1 
ATOM   3083 C  C   . ASN A 1 420 ? 61.232  154.999 88.061  1.00 120.07 ? 620 ASN A C   1 
ATOM   3084 O  O   . ASN A 1 420 ? 60.883  155.628 87.055  1.00 120.07 ? 620 ASN A O   1 
ATOM   3085 C  CB  . ASN A 1 420 ? 63.256  153.954 87.019  1.00 120.07 ? 620 ASN A CB  1 
ATOM   3086 C  CG  . ASN A 1 420 ? 62.655  152.579 86.807  1.00 120.07 ? 620 ASN A CG  1 
ATOM   3087 O  OD1 . ASN A 1 420 ? 61.953  152.054 87.672  1.00 120.07 ? 620 ASN A OD1 1 
ATOM   3088 N  ND2 . ASN A 1 420 ? 62.928  151.986 85.650  1.00 120.07 ? 620 ASN A ND2 1 
ATOM   3089 N  N   . PHE A 1 421 ? 60.363  154.582 88.985  1.00 122.39 ? 621 PHE A N   1 
ATOM   3090 C  CA  . PHE A 1 421 ? 58.936  154.904 88.989  1.00 122.39 ? 621 PHE A CA  1 
ATOM   3091 C  C   . PHE A 1 421 ? 58.190  154.307 87.799  1.00 122.39 ? 621 PHE A C   1 
ATOM   3092 O  O   . PHE A 1 421 ? 57.075  154.738 87.486  1.00 122.39 ? 621 PHE A O   1 
ATOM   3093 C  CB  . PHE A 1 421 ? 58.708  156.420 89.044  1.00 122.39 ? 621 PHE A CB  1 
ATOM   3094 C  CG  . PHE A 1 421 ? 59.495  157.111 90.118  1.00 122.39 ? 621 PHE A CG  1 
ATOM   3095 C  CD1 . PHE A 1 421 ? 59.272  156.827 91.455  1.00 122.39 ? 621 PHE A CD1 1 
ATOM   3096 C  CD2 . PHE A 1 421 ? 60.465  158.045 89.791  1.00 122.39 ? 621 PHE A CD2 1 
ATOM   3097 C  CE1 . PHE A 1 421 ? 59.996  157.462 92.445  1.00 122.39 ? 621 PHE A CE1 1 
ATOM   3098 C  CE2 . PHE A 1 421 ? 61.194  158.684 90.775  1.00 122.39 ? 621 PHE A CE2 1 
ATOM   3099 C  CZ  . PHE A 1 421 ? 60.959  158.392 92.104  1.00 122.39 ? 621 PHE A CZ  1 
ATOM   3100 N  N   . ASP A 1 422 ? 58.771  153.317 87.121  1.00 124.36 ? 622 ASP A N   1 
ATOM   3101 C  CA  . ASP A 1 422 ? 58.116  152.671 85.990  1.00 124.36 ? 622 ASP A CA  1 
ATOM   3102 C  C   . ASP A 1 422 ? 57.766  151.217 86.279  1.00 124.36 ? 622 ASP A C   1 
ATOM   3103 O  O   . ASP A 1 422 ? 56.592  150.840 86.224  1.00 124.36 ? 622 ASP A O   1 
ATOM   3104 C  CB  . ASP A 1 422 ? 59.007  152.765 84.743  1.00 124.36 ? 622 ASP A CB  1 
ATOM   3105 C  CG  . ASP A 1 422 ? 59.531  154.165 84.501  1.00 124.36 ? 622 ASP A CG  1 
ATOM   3106 O  OD1 . ASP A 1 422 ? 58.869  155.133 84.930  1.00 124.36 ? 622 ASP A OD1 1 
ATOM   3107 O  OD2 . ASP A 1 422 ? 60.607  154.299 83.880  1.00 124.36 ? 622 ASP A OD2 1 
ATOM   3108 N  N   . GLU A 1 423 ? 58.761  150.383 86.588  1.00 124.51 ? 623 GLU A N   1 
ATOM   3109 C  CA  . GLU A 1 423 ? 58.509  148.978 86.889  1.00 124.51 ? 623 GLU A CA  1 
ATOM   3110 C  C   . GLU A 1 423 ? 59.293  148.440 88.075  1.00 124.51 ? 623 GLU A C   1 
ATOM   3111 O  O   . GLU A 1 423 ? 58.953  147.357 88.560  1.00 124.51 ? 623 GLU A O   1 
ATOM   3112 C  CB  . GLU A 1 423 ? 58.812  148.099 85.665  1.00 124.51 ? 623 GLU A CB  1 
ATOM   3113 C  CG  . GLU A 1 423 ? 58.006  148.438 84.419  1.00 124.51 ? 623 GLU A CG  1 
ATOM   3114 C  CD  . GLU A 1 423 ? 57.637  147.208 83.612  1.00 124.51 ? 623 GLU A CD  1 
ATOM   3115 O  OE1 . GLU A 1 423 ? 57.466  146.127 84.217  1.00 124.51 ? 623 GLU A OE1 1 
ATOM   3116 O  OE2 . GLU A 1 423 ? 57.520  147.321 82.374  1.00 124.51 ? 623 GLU A OE2 1 
ATOM   3117 N  N   . TYR A 1 424 ? 60.318  149.136 88.560  1.00 118.92 ? 624 TYR A N   1 
ATOM   3118 C  CA  . TYR A 1 424 ? 61.200  148.618 89.597  1.00 118.92 ? 624 TYR A CA  1 
ATOM   3119 C  C   . TYR A 1 424 ? 61.232  149.575 90.779  1.00 118.92 ? 624 TYR A C   1 
ATOM   3120 O  O   . TYR A 1 424 ? 61.496  150.770 90.611  1.00 118.92 ? 624 TYR A O   1 
ATOM   3121 C  CB  . TYR A 1 424 ? 62.613  148.404 89.051  1.00 118.92 ? 624 TYR A CB  1 
ATOM   3122 C  CG  . TYR A 1 424 ? 63.540  147.678 90.002  1.00 118.92 ? 624 TYR A CG  1 
ATOM   3123 C  CD1 . TYR A 1 424 ? 63.510  146.295 90.110  1.00 118.92 ? 624 TYR A CD1 1 
ATOM   3124 C  CD2 . TYR A 1 424 ? 64.447  148.379 90.787  1.00 118.92 ? 624 TYR A CD2 1 
ATOM   3125 C  CE1 . TYR A 1 424 ? 64.357  145.629 90.976  1.00 118.92 ? 624 TYR A CE1 1 
ATOM   3126 C  CE2 . TYR A 1 424 ? 65.295  147.722 91.656  1.00 118.92 ? 624 TYR A CE2 1 
ATOM   3127 C  CZ  . TYR A 1 424 ? 65.247  146.348 91.746  1.00 118.92 ? 624 TYR A CZ  1 
ATOM   3128 N  N   . ASN A 1 425 ? 60.964  149.043 91.971  1.00 117.54 ? 625 ASN A N   1 
ATOM   3129 C  CA  . ASN A 1 425 ? 61.077  149.814 93.206  1.00 117.54 ? 625 ASN A CA  1 
ATOM   3130 C  C   . ASN A 1 425 ? 61.280  148.818 94.340  1.00 117.54 ? 625 ASN A C   1 
ATOM   3131 O  O   . ASN A 1 425 ? 60.333  148.126 94.728  1.00 117.54 ? 625 ASN A O   1 
ATOM   3132 C  CB  . ASN A 1 425 ? 59.836  150.671 93.431  1.00 117.54 ? 625 ASN A CB  1 
ATOM   3133 C  CG  . ASN A 1 425 ? 60.072  151.791 94.429  1.00 117.54 ? 625 ASN A CG  1 
ATOM   3134 O  OD1 . ASN A 1 425 ? 60.960  151.706 95.278  1.00 117.54 ? 625 ASN A OD1 1 
ATOM   3135 N  ND2 . ASN A 1 425 ? 59.277  152.850 94.326  1.00 117.54 ? 625 ASN A ND2 1 
ATOM   3136 N  N   . ASN A 1 426 ? 62.503  148.747 94.866  1.00 115.60 ? 626 ASN A N   1 
ATOM   3137 C  CA  . ASN A 1 426 ? 62.865  147.756 95.873  1.00 115.60 ? 626 ASN A CA  1 
ATOM   3138 C  C   . ASN A 1 426 ? 63.352  148.406 97.165  1.00 115.60 ? 626 ASN A C   1 
ATOM   3139 O  O   . ASN A 1 426 ? 64.109  147.798 97.924  1.00 115.60 ? 626 ASN A O   1 
ATOM   3140 C  CB  . ASN A 1 426 ? 63.920  146.794 95.327  1.00 115.60 ? 626 ASN A CB  1 
ATOM   3141 C  CG  . ASN A 1 426 ? 65.244  147.478 95.047  1.00 115.60 ? 626 ASN A CG  1 
ATOM   3142 O  OD1 . ASN A 1 426 ? 65.306  148.695 94.875  1.00 115.60 ? 626 ASN A OD1 1 
ATOM   3143 N  ND2 . ASN A 1 426 ? 66.315  146.694 95.000  1.00 115.60 ? 626 ASN A ND2 1 
ATOM   3144 N  N   . PHE A 1 427 ? 62.930  149.641 97.424  1.00 118.51 ? 627 PHE A N   1 
ATOM   3145 C  CA  . PHE A 1 427 ? 63.298  150.299 98.666  1.00 118.51 ? 627 PHE A CA  1 
ATOM   3146 C  C   . PHE A 1 427 ? 62.657  149.575 99.850  1.00 118.51 ? 627 PHE A C   1 
ATOM   3147 O  O   . PHE A 1 427 ? 61.569  149.006 99.725  1.00 118.51 ? 627 PHE A O   1 
ATOM   3148 C  CB  . PHE A 1 427 ? 62.866  151.763 98.642  1.00 118.51 ? 627 PHE A CB  1 
ATOM   3149 C  CG  . PHE A 1 427 ? 63.931  152.701 98.150  1.00 118.51 ? 627 PHE A CG  1 
ATOM   3150 C  CD1 . PHE A 1 427 ? 64.087  152.947 96.796  1.00 118.51 ? 627 PHE A CD1 1 
ATOM   3151 C  CD2 . PHE A 1 427 ? 64.779  153.336 99.043  1.00 118.51 ? 627 PHE A CD2 1 
ATOM   3152 C  CE1 . PHE A 1 427 ? 65.067  153.810 96.343  1.00 118.51 ? 627 PHE A CE1 1 
ATOM   3153 C  CE2 . PHE A 1 427 ? 65.761  154.200 98.595  1.00 118.51 ? 627 PHE A CE2 1 
ATOM   3154 C  CZ  . PHE A 1 427 ? 65.905  154.436 97.243  1.00 118.51 ? 627 PHE A CZ  1 
ATOM   3155 N  N   . PRO A 1 428 ? 63.317  149.571 101.012 1.00 120.84 ? 628 PRO A N   1 
ATOM   3156 C  CA  . PRO A 1 428 ? 62.748  148.871 102.176 1.00 120.84 ? 628 PRO A CA  1 
ATOM   3157 C  C   . PRO A 1 428 ? 61.416  149.435 102.633 1.00 120.84 ? 628 PRO A C   1 
ATOM   3158 O  O   . PRO A 1 428 ? 60.646  148.717 103.283 1.00 120.84 ? 628 PRO A O   1 
ATOM   3159 C  CB  . PRO A 1 428 ? 63.830  149.037 103.254 1.00 120.84 ? 628 PRO A CB  1 
ATOM   3160 C  CG  . PRO A 1 428 ? 64.634  150.216 102.817 1.00 120.84 ? 628 PRO A CG  1 
ATOM   3161 C  CD  . PRO A 1 428 ? 64.614  150.197 101.319 1.00 120.84 ? 628 PRO A CD  1 
ATOM   3162 N  N   . ALA A 1 429 ? 61.118  150.695 102.320 1.00 125.56 ? 629 ALA A N   1 
ATOM   3163 C  CA  . ALA A 1 429 ? 59.829  151.283 102.660 1.00 125.56 ? 629 ALA A CA  1 
ATOM   3164 C  C   . ALA A 1 429 ? 59.172  151.872 101.421 1.00 125.56 ? 629 ALA A C   1 
ATOM   3165 O  O   . ALA A 1 429 ? 59.670  151.697 100.304 1.00 125.56 ? 629 ALA A O   1 
ATOM   3166 C  CB  . ALA A 1 429 ? 59.990  152.353 103.742 1.00 125.56 ? 629 ALA A CB  1 
ATOM   3167 N  N   . SER A 1 430 ? 58.056  152.571 101.605 1.00 129.52 ? 630 SER A N   1 
ATOM   3168 C  CA  . SER A 1 430 ? 57.337  153.204 100.508 1.00 129.52 ? 630 SER A CA  1 
ATOM   3169 C  C   . SER A 1 430 ? 57.579  154.707 100.543 1.00 129.52 ? 630 SER A C   1 
ATOM   3170 O  O   . SER A 1 430 ? 57.432  155.340 101.594 1.00 129.52 ? 630 SER A O   1 
ATOM   3171 C  CB  . SER A 1 430 ? 55.840  152.905 100.591 1.00 129.52 ? 630 SER A CB  1 
ATOM   3172 O  OG  . SER A 1 430 ? 55.598  151.509 100.586 1.00 129.52 ? 630 SER A OG  1 
ATOM   3173 N  N   . TRP A 1 431 ? 57.916  155.328 99.408  1.00 131.34 ? 631 TRP A N   1 
ATOM   3174 C  CA  . TRP A 1 431 ? 58.235  156.789 99.387  1.00 131.34 ? 631 TRP A CA  1 
ATOM   3175 C  C   . TRP A 1 431 ? 56.982  157.614 99.683  1.00 131.34 ? 631 TRP A C   1 
ATOM   3176 O  O   . TRP A 1 431 ? 55.934  157.327 99.060  1.00 131.34 ? 631 TRP A O   1 
ATOM   3177 C  CB  . TRP A 1 431 ? 58.810  157.210 98.037  1.00 30.00  ? 631 TRP A CB  1 
ATOM   3178 C  CG  . TRP A 1 431 ? 60.261  156.887 97.836  1.00 30.00  ? 631 TRP A CG  1 
ATOM   3179 C  CD1 . TRP A 1 431 ? 60.769  155.817 97.161  1.00 30.00  ? 631 TRP A CD1 1 
ATOM   3180 C  CD2 . TRP A 1 431 ? 61.397  157.644 98.291  1.00 30.00  ? 631 TRP A CD2 1 
ATOM   3181 N  NE1 . TRP A 1 431 ? 62.135  155.855 97.170  1.00 30.00  ? 631 TRP A NE1 1 
ATOM   3182 C  CE2 . TRP A 1 431 ? 62.550  156.961 97.856  1.00 30.00  ? 631 TRP A CE2 1 
ATOM   3183 C  CE3 . TRP A 1 431 ? 61.560  158.820 99.028  1.00 30.00  ? 631 TRP A CE3 1 
ATOM   3184 C  CZ2 . TRP A 1 431 ? 63.835  157.420 98.131  1.00 30.00  ? 631 TRP A CZ2 1 
ATOM   3185 C  CZ3 . TRP A 1 431 ? 62.830  159.277 99.296  1.00 30.00  ? 631 TRP A CZ3 1 
ATOM   3186 C  CH2 . TRP A 1 431 ? 63.953  158.577 98.860  1.00 30.00  ? 631 TRP A CH2 1 
ATOM   3187 N  N   . SER A 1 432 ? 57.080  158.635 100.540 1.00 135.24 ? 632 SER A N   1 
ATOM   3188 C  CA  . SER A 1 432 ? 55.893  159.507 100.787 1.00 135.24 ? 632 SER A CA  1 
ATOM   3189 C  C   . SER A 1 432 ? 55.708  160.618 99.735  1.00 135.24 ? 632 SER A C   1 
ATOM   3190 O  O   . SER A 1 432 ? 56.735  161.152 99.299  1.00 135.24 ? 632 SER A O   1 
ATOM   3191 C  CB  . SER A 1 432 ? 55.976  160.094 102.176 1.00 135.24 ? 632 SER A CB  1 
ATOM   3192 O  OG  . SER A 1 432 ? 57.075  160.984 102.284 1.00 135.24 ? 632 SER A OG  1 
ATOM   3193 N  N   . ASN A 1 433 ? 54.462  160.906 99.310  1.00 136.13 ? 633 ASN A N   1 
ATOM   3194 C  CA  . ASN A 1 433 ? 54.151  162.043 98.441  1.00 136.13 ? 633 ASN A CA  1 
ATOM   3195 C  C   . ASN A 1 433 ? 54.840  161.903 97.082  1.00 136.13 ? 633 ASN A C   1 
ATOM   3196 O  O   . ASN A 1 433 ? 55.696  162.701 96.697  1.00 136.13 ? 633 ASN A O   1 
ATOM   3197 C  CB  . ASN A 1 433 ? 54.523  163.367 99.119  1.00 136.13 ? 633 ASN A CB  1 
ATOM   3198 C  CG  . ASN A 1 433 ? 53.741  163.608 100.395 1.00 136.13 ? 633 ASN A CG  1 
ATOM   3199 O  OD1 . ASN A 1 433 ? 54.312  163.690 101.482 1.00 136.13 ? 633 ASN A OD1 1 
ATOM   3200 N  ND2 . ASN A 1 433 ? 52.424  163.721 100.270 1.00 136.13 ? 633 ASN A ND2 1 
ATOM   3201 N  N   . ILE A 1 434 ? 54.445  160.859 96.355  1.00 136.05 ? 634 ILE A N   1 
ATOM   3202 C  CA  . ILE A 1 434 ? 55.002  160.549 95.044  1.00 136.05 ? 634 ILE A CA  1 
ATOM   3203 C  C   . ILE A 1 434 ? 53.950  160.834 93.980  1.00 136.05 ? 634 ILE A C   1 
ATOM   3204 O  O   . ILE A 1 434 ? 52.779  160.465 94.131  1.00 136.05 ? 634 ILE A O   1 
ATOM   3205 C  CB  . ILE A 1 434 ? 55.482  159.087 94.962  1.00 136.05 ? 634 ILE A CB  1 
ATOM   3206 C  CG1 . ILE A 1 434 ? 54.445  158.143 95.578  1.00 136.05 ? 634 ILE A CG1 1 
ATOM   3207 C  CG2 . ILE A 1 434 ? 56.830  158.934 95.644  1.00 136.05 ? 634 ILE A CG2 1 
ATOM   3208 C  CD1 . ILE A 1 434 ? 54.674  156.686 95.248  1.00 136.05 ? 634 ILE A CD1 1 
ATOM   3209 N  N   . ASP A 1 435 ? 54.373  161.495 92.905  1.00 136.22 ? 635 ASP A N   1 
ATOM   3210 C  CA  . ASP A 1 435 ? 53.514  161.804 91.767  1.00 136.22 ? 635 ASP A CA  1 
ATOM   3211 C  C   . ASP A 1 435 ? 53.975  160.956 90.588  1.00 136.22 ? 635 ASP A C   1 
ATOM   3212 O  O   . ASP A 1 435 ? 55.084  161.146 90.077  1.00 136.22 ? 635 ASP A O   1 
ATOM   3213 C  CB  . ASP A 1 435 ? 53.564  163.294 91.429  1.00 136.22 ? 635 ASP A CB  1 
ATOM   3214 C  CG  . ASP A 1 435 ? 52.591  163.679 90.329  1.00 136.22 ? 635 ASP A CG  1 
ATOM   3215 O  OD1 . ASP A 1 435 ? 51.735  162.846 89.965  1.00 136.22 ? 635 ASP A OD1 1 
ATOM   3216 O  OD2 . ASP A 1 435 ? 52.685  164.819 89.827  1.00 136.22 ? 635 ASP A OD2 1 
ATOM   3217 N  N   . THR A 1 436 ? 53.126  160.022 90.159  1.00 137.39 ? 636 THR A N   1 
ATOM   3218 C  CA  . THR A 1 436 ? 53.450  159.125 89.060  1.00 137.39 ? 636 THR A CA  1 
ATOM   3219 C  C   . THR A 1 436 ? 52.772  159.505 87.750  1.00 137.39 ? 636 THR A C   1 
ATOM   3220 O  O   . THR A 1 436 ? 53.097  158.920 86.712  1.00 137.39 ? 636 THR A O   1 
ATOM   3221 C  CB  . THR A 1 436 ? 53.072  157.682 89.420  1.00 137.39 ? 636 THR A CB  1 
ATOM   3222 O  OG1 . THR A 1 436 ? 53.562  156.791 88.410  1.00 137.39 ? 636 THR A OG1 1 
ATOM   3223 C  CG2 . THR A 1 436 ? 51.562  157.538 89.528  1.00 137.39 ? 636 THR A CG2 1 
ATOM   3224 N  N   . LYS A 1 437 ? 51.846  160.466 87.771  1.00 136.61 ? 637 LYS A N   1 
ATOM   3225 C  CA  . LYS A 1 437 ? 51.143  160.896 86.562  1.00 136.61 ? 637 LYS A CA  1 
ATOM   3226 C  C   . LYS A 1 437 ? 51.984  161.949 85.839  1.00 136.61 ? 637 LYS A C   1 
ATOM   3227 O  O   . LYS A 1 437 ? 51.709  163.150 85.862  1.00 136.61 ? 637 LYS A O   1 
ATOM   3228 C  CB  . LYS A 1 437 ? 49.758  161.424 86.910  1.00 136.61 ? 637 LYS A CB  1 
ATOM   3229 C  CG  . LYS A 1 437 ? 48.734  161.257 85.800  1.00 136.61 ? 637 LYS A CG  1 
ATOM   3230 C  CD  . LYS A 1 437 ? 48.474  159.788 85.505  1.00 136.61 ? 637 LYS A CD  1 
ATOM   3231 C  CE  . LYS A 1 437 ? 47.740  159.613 84.187  1.00 136.61 ? 637 LYS A CE  1 
ATOM   3232 N  NZ  . LYS A 1 437 ? 48.582  160.009 83.025  1.00 136.61 ? 637 LYS A NZ  1 
ATOM   3233 N  N   . ASN A 1 438 ? 53.039  161.468 85.184  1.00 133.49 ? 638 ASN A N   1 
ATOM   3234 C  CA  . ASN A 1 438 ? 53.965  162.344 84.485  1.00 133.49 ? 638 ASN A CA  1 
ATOM   3235 C  C   . ASN A 1 438 ? 54.516  161.628 83.262  1.00 133.49 ? 638 ASN A C   1 
ATOM   3236 O  O   . ASN A 1 438 ? 54.496  160.397 83.174  1.00 133.49 ? 638 ASN A O   1 
ATOM   3237 C  CB  . ASN A 1 438 ? 55.113  162.794 85.400  1.00 133.49 ? 638 ASN A CB  1 
ATOM   3238 C  CG  . ASN A 1 438 ? 55.584  164.201 85.094  1.00 133.49 ? 638 ASN A CG  1 
ATOM   3239 O  OD1 . ASN A 1 438 ? 55.312  164.741 84.022  1.00 133.49 ? 638 ASN A OD1 1 
ATOM   3240 N  ND2 . ASN A 1 438 ? 56.298  164.803 86.039  1.00 133.49 ? 638 ASN A ND2 1 
ATOM   3241 N  N   . GLN A 1 439 ? 55.008  162.422 82.309  1.00 132.89 ? 639 GLN A N   1 
ATOM   3242 C  CA  . GLN A 1 439 ? 55.639  161.901 81.104  1.00 132.89 ? 639 GLN A CA  1 
ATOM   3243 C  C   . GLN A 1 439 ? 56.979  162.566 80.819  1.00 132.89 ? 639 GLN A C   1 
ATOM   3244 O  O   . GLN A 1 439 ? 57.557  162.336 79.749  1.00 132.89 ? 639 GLN A O   1 
ATOM   3245 C  CB  . GLN A 1 439 ? 54.710  162.063 79.894  1.00 132.89 ? 639 GLN A CB  1 
ATOM   3246 C  CG  . GLN A 1 439 ? 54.556  160.805 79.055  1.00 132.89 ? 639 GLN A CG  1 
ATOM   3247 C  CD  . GLN A 1 439 ? 53.860  159.684 79.803  1.00 132.89 ? 639 GLN A CD  1 
ATOM   3248 O  OE1 . GLN A 1 439 ? 52.939  159.922 80.584  1.00 132.89 ? 639 GLN A OE1 1 
ATOM   3249 N  NE2 . GLN A 1 439 ? 54.298  158.453 79.566  1.00 132.89 ? 639 GLN A NE2 1 
ATOM   3250 N  N   . ASP A 1 440 ? 57.490  163.382 81.742  1.00 131.87 ? 640 ASP A N   1 
ATOM   3251 C  CA  . ASP A 1 440 ? 58.757  164.083 81.573  1.00 131.87 ? 640 ASP A CA  1 
ATOM   3252 C  C   . ASP A 1 440 ? 59.908  163.370 82.276  1.00 131.87 ? 640 ASP A C   1 
ATOM   3253 O  O   . ASP A 1 440 ? 60.849  164.021 82.743  1.00 131.87 ? 640 ASP A O   1 
ATOM   3254 C  CB  . ASP A 1 440 ? 58.637  165.519 82.080  1.00 131.87 ? 640 ASP A CB  1 
ATOM   3255 C  CG  . ASP A 1 440 ? 57.324  166.170 81.687  1.00 131.87 ? 640 ASP A CG  1 
ATOM   3256 O  OD1 . ASP A 1 440 ? 56.617  165.615 80.820  1.00 131.87 ? 640 ASP A OD1 1 
ATOM   3257 O  OD2 . ASP A 1 440 ? 56.998  167.237 82.250  1.00 131.87 ? 640 ASP A OD2 1 
ATOM   3258 N  N   . GLY A 1 441 ? 59.851  162.042 82.362  1.00 128.56 ? 641 GLY A N   1 
ATOM   3259 C  CA  . GLY A 1 441 ? 60.856  161.297 83.084  1.00 128.56 ? 641 GLY A CA  1 
ATOM   3260 C  C   . GLY A 1 441 ? 62.124  161.063 82.291  1.00 128.56 ? 641 GLY A C   1 
ATOM   3261 O  O   . GLY A 1 441 ? 62.210  161.336 81.094  1.00 128.56 ? 641 GLY A O   1 
ATOM   3262 N  N   . LEU A 1 442 ? 63.134  160.547 82.996  1.00 123.03 ? 642 LEU A N   1 
ATOM   3263 C  CA  . LEU A 1 442 ? 64.395  160.213 82.343  1.00 123.03 ? 642 LEU A CA  1 
ATOM   3264 C  C   . LEU A 1 442 ? 64.204  159.106 81.315  1.00 123.03 ? 642 LEU A C   1 
ATOM   3265 O  O   . LEU A 1 442 ? 64.764  159.168 80.215  1.00 123.03 ? 642 LEU A O   1 
ATOM   3266 C  CB  . LEU A 1 442 ? 65.436  159.808 83.387  1.00 123.03 ? 642 LEU A CB  1 
ATOM   3267 C  CG  . LEU A 1 442 ? 66.901  159.896 82.956  1.00 123.03 ? 642 LEU A CG  1 
ATOM   3268 C  CD1 . LEU A 1 442 ? 67.214  161.274 82.395  1.00 123.03 ? 642 LEU A CD1 1 
ATOM   3269 C  CD2 . LEU A 1 442 ? 67.824  159.570 84.120  1.00 123.03 ? 642 LEU A CD2 1 
ATOM   3270 N  N   . GLN A 1 443 ? 63.418  158.082 81.653  1.00 124.57 ? 643 GLN A N   1 
ATOM   3271 C  CA  . GLN A 1 443 ? 63.122  157.001 80.723  1.00 124.57 ? 643 GLN A CA  1 
ATOM   3272 C  C   . GLN A 1 443 ? 61.648  156.958 80.336  1.00 124.57 ? 643 GLN A C   1 
ATOM   3273 O  O   . GLN A 1 443 ? 61.318  157.077 79.153  1.00 124.57 ? 643 GLN A O   1 
ATOM   3274 C  CB  . GLN A 1 443 ? 63.553  155.659 81.328  1.00 124.57 ? 643 GLN A CB  1 
ATOM   3275 C  CG  . GLN A 1 443 ? 65.054  155.411 81.293  1.00 124.57 ? 643 GLN A CG  1 
ATOM   3276 C  CD  . GLN A 1 443 ? 65.778  156.058 82.457  1.00 124.57 ? 643 GLN A CD  1 
ATOM   3277 O  OE1 . GLN A 1 443 ? 65.157  156.491 83.427  1.00 124.57 ? 643 GLN A OE1 1 
ATOM   3278 N  NE2 . GLN A 1 443 ? 67.101  156.126 82.367  1.00 124.57 ? 643 GLN A NE2 1 
ATOM   3279 N  N   . SER A 1 444 ? 60.745  156.794 81.304  1.00 127.88 ? 644 SER A N   1 
ATOM   3280 C  CA  . SER A 1 444 ? 59.314  156.778 81.015  1.00 127.88 ? 644 SER A CA  1 
ATOM   3281 C  C   . SER A 1 444 ? 58.553  157.861 81.771  1.00 127.88 ? 644 SER A C   1 
ATOM   3282 O  O   . SER A 1 444 ? 57.874  158.680 81.143  1.00 127.88 ? 644 SER A O   1 
ATOM   3283 C  CB  . SER A 1 444 ? 58.734  155.393 81.331  1.00 127.88 ? 644 SER A CB  1 
ATOM   3284 O  OG  . SER A 1 444 ? 57.410  155.270 80.841  1.00 127.88 ? 644 SER A OG  1 
ATOM   3285 N  N   . VAL A 1 445 ? 58.646  157.893 83.103  1.00 128.26 ? 645 VAL A N   1 
ATOM   3286 C  CA  . VAL A 1 445 ? 57.909  158.846 83.927  1.00 128.26 ? 645 VAL A CA  1 
ATOM   3287 C  C   . VAL A 1 445 ? 58.851  159.420 84.976  1.00 128.26 ? 645 VAL A C   1 
ATOM   3288 O  O   . VAL A 1 445 ? 59.912  158.865 85.267  1.00 128.26 ? 645 VAL A O   1 
ATOM   3289 C  CB  . VAL A 1 445 ? 56.666  158.222 84.612  1.00 128.26 ? 645 VAL A CB  1 
ATOM   3290 C  CG1 . VAL A 1 445 ? 56.013  157.168 83.725  1.00 128.26 ? 645 VAL A CG1 1 
ATOM   3291 C  CG2 . VAL A 1 445 ? 57.031  157.629 85.964  1.00 128.26 ? 645 VAL A CG2 1 
ATOM   3292 N  N   . ALA A 1 446 ? 58.449  160.555 85.539  1.00 129.69 ? 646 ALA A N   1 
ATOM   3293 C  CA  . ALA A 1 446 ? 59.212  161.248 86.568  1.00 129.69 ? 646 ALA A CA  1 
ATOM   3294 C  C   . ALA A 1 446 ? 58.398  161.304 87.859  1.00 129.69 ? 646 ALA A C   1 
ATOM   3295 O  O   . ALA A 1 446 ? 57.312  160.726 87.965  1.00 129.69 ? 646 ALA A O   1 
ATOM   3296 C  CB  . ALA A 1 446 ? 59.606  162.649 86.096  1.00 129.69 ? 646 ALA A CB  1 
ATOM   3297 N  N   . ASN A 1 447 ? 58.939  162.014 88.850  1.00 130.31 ? 647 ASN A N   1 
ATOM   3298 C  CA  . ASN A 1 447 ? 58.285  162.221 90.141  1.00 130.31 ? 647 ASN A CA  1 
ATOM   3299 C  C   . ASN A 1 447 ? 58.319  163.719 90.431  1.00 130.31 ? 647 ASN A C   1 
ATOM   3300 O  O   . ASN A 1 447 ? 59.267  164.221 91.043  1.00 130.31 ? 647 ASN A O   1 
ATOM   3301 C  CB  . ASN A 1 447 ? 58.965  161.411 91.243  1.00 130.31 ? 647 ASN A CB  1 
ATOM   3302 C  CG  . ASN A 1 447 ? 58.426  161.739 92.621  1.00 130.31 ? 647 ASN A CG  1 
ATOM   3303 O  OD1 . ASN A 1 447 ? 57.246  161.537 92.902  1.00 130.31 ? 647 ASN A OD1 1 
ATOM   3304 N  ND2 . ASN A 1 447 ? 59.292  162.246 93.490  1.00 130.31 ? 647 ASN A ND2 1 
ATOM   3305 N  N   . LYS A 1 448 ? 57.289  164.431 89.981  1.00 129.89 ? 648 LYS A N   1 
ATOM   3306 C  CA  . LYS A 1 448 ? 57.191  165.868 90.218  1.00 129.89 ? 648 LYS A CA  1 
ATOM   3307 C  C   . LYS A 1 448 ? 56.986  166.116 91.707  1.00 129.89 ? 648 LYS A C   1 
ATOM   3308 O  O   . LYS A 1 448 ? 55.927  165.799 92.257  1.00 129.89 ? 648 LYS A O   1 
ATOM   3309 C  CB  . LYS A 1 448 ? 56.051  166.463 89.399  1.00 129.89 ? 648 LYS A CB  1 
ATOM   3310 C  CG  . LYS A 1 448 ? 56.020  167.982 89.388  1.00 129.89 ? 648 LYS A CG  1 
ATOM   3311 C  CD  . LYS A 1 448 ? 54.658  168.504 88.964  1.00 129.89 ? 648 LYS A CD  1 
ATOM   3312 C  CE  . LYS A 1 448 ? 54.358  168.154 87.515  1.00 129.89 ? 648 LYS A CE  1 
ATOM   3313 N  NZ  . LYS A 1 448 ? 55.237  168.898 86.570  1.00 129.89 ? 648 LYS A NZ  1 
ATOM   3314 N  N   . LEU A 1 449 ? 57.997  166.680 92.362  1.00 129.82 ? 649 LEU A N   1 
ATOM   3315 C  CA  . LEU A 1 449 ? 57.972  166.895 93.804  1.00 129.82 ? 649 LEU A CA  1 
ATOM   3316 C  C   . LEU A 1 449 ? 57.237  168.197 94.097  1.00 129.82 ? 649 LEU A C   1 
ATOM   3317 O  O   . LEU A 1 449 ? 57.761  169.288 93.841  1.00 129.82 ? 649 LEU A O   1 
ATOM   3318 C  CB  . LEU A 1 449 ? 59.389  166.921 94.371  1.00 129.82 ? 649 LEU A CB  1 
ATOM   3319 C  CG  . LEU A 1 449 ? 59.541  167.308 95.845  1.00 129.82 ? 649 LEU A CG  1 
ATOM   3320 C  CD1 . LEU A 1 449 ? 58.617  166.481 96.727  1.00 129.82 ? 649 LEU A CD1 1 
ATOM   3321 C  CD2 . LEU A 1 449 ? 60.987  167.158 96.293  1.00 129.82 ? 649 LEU A CD2 1 
ATOM   3322 N  N   . SER A 1 450 ? 56.024  168.085 94.631  1.00 127.89 ? 650 SER A N   1 
ATOM   3323 C  CA  . SER A 1 450 ? 55.224  169.230 95.058  1.00 127.89 ? 650 SER A CA  1 
ATOM   3324 C  C   . SER A 1 450 ? 55.032  169.098 96.566  1.00 127.89 ? 650 SER A C   1 
ATOM   3325 O  O   . SER A 1 450 ? 54.028  168.552 97.031  1.00 127.89 ? 650 SER A O   1 
ATOM   3326 C  CB  . SER A 1 450 ? 53.888  169.285 94.315  1.00 127.89 ? 650 SER A CB  1 
ATOM   3327 O  OG  . SER A 1 450 ? 53.331  170.586 94.360  1.00 127.89 ? 650 SER A OG  1 
ATOM   3328 N  N   . GLY A 1 451 ? 55.999  169.604 97.326  1.00 129.94 ? 651 GLY A N   1 
ATOM   3329 C  CA  . GLY A 1 451 ? 55.958  169.497 98.771  1.00 129.94 ? 651 GLY A CA  1 
ATOM   3330 C  C   . GLY A 1 451 ? 57.211  168.878 99.357  1.00 129.94 ? 651 GLY A C   1 
ATOM   3331 O  O   . GLY A 1 451 ? 58.326  169.184 98.925  1.00 129.94 ? 651 GLY A O   1 
ATOM   3332 N  N   . GLU A 1 452 ? 57.036  168.002 100.344 1.00 132.80 ? 652 GLU A N   1 
ATOM   3333 C  CA  . GLU A 1 452 ? 58.139  167.343 101.029 1.00 132.80 ? 652 GLU A CA  1 
ATOM   3334 C  C   . GLU A 1 452 ? 57.986  165.836 100.891 1.00 132.80 ? 652 GLU A C   1 
ATOM   3335 O  O   . GLU A 1 452 ? 56.872  165.311 101.000 1.00 132.80 ? 652 GLU A O   1 
ATOM   3336 C  CB  . GLU A 1 452 ? 58.178  167.743 102.508 1.00 132.80 ? 652 GLU A CB  1 
ATOM   3337 C  CG  . GLU A 1 452 ? 59.175  166.963 103.348 1.00 132.80 ? 652 GLU A CG  1 
ATOM   3338 C  CD  . GLU A 1 452 ? 58.700  166.755 104.773 1.00 132.80 ? 652 GLU A CD  1 
ATOM   3339 O  OE1 . GLU A 1 452 ? 58.918  167.655 105.611 1.00 132.80 ? 652 GLU A OE1 1 
ATOM   3340 O  OE2 . GLU A 1 452 ? 58.108  165.692 105.054 1.00 132.80 ? 652 GLU A OE2 1 
ATOM   3341 N  N   . THR A 1 453 ? 59.099  165.142 100.652 1.00 134.28 ? 653 THR A N   1 
ATOM   3342 C  CA  . THR A 1 453 ? 59.118  163.692 100.541 1.00 134.28 ? 653 THR A CA  1 
ATOM   3343 C  C   . THR A 1 453 ? 60.103  163.145 101.565 1.00 134.28 ? 653 THR A C   1 
ATOM   3344 O  O   . THR A 1 453 ? 61.192  163.699 101.737 1.00 134.28 ? 653 THR A O   1 
ATOM   3345 C  CB  . THR A 1 453 ? 59.510  163.261 99.123  1.00 134.28 ? 653 THR A CB  1 
ATOM   3346 O  OG1 . THR A 1 453 ? 58.420  163.510 98.227  1.00 134.28 ? 653 THR A OG1 1 
ATOM   3347 C  CG2 . THR A 1 453 ? 59.865  161.786 99.079  1.00 134.28 ? 653 THR A CG2 1 
ATOM   3348 N  N   . LYS A 1 454 ? 59.717  162.077 102.257 1.00 134.71 ? 654 LYS A N   1 
ATOM   3349 C  CA  . LYS A 1 454 ? 60.580  161.472 103.261 1.00 134.71 ? 654 LYS A CA  1 
ATOM   3350 C  C   . LYS A 1 454 ? 60.549  159.959 103.112 1.00 134.71 ? 654 LYS A C   1 
ATOM   3351 O  O   . LYS A 1 454 ? 59.561  159.380 102.652 1.00 134.71 ? 654 LYS A O   1 
ATOM   3352 C  CB  . LYS A 1 454 ? 60.163  161.875 104.682 1.00 134.71 ? 654 LYS A CB  1 
ATOM   3353 C  CG  . LYS A 1 454 ? 61.308  161.901 105.680 1.00 134.71 ? 654 LYS A CG  1 
ATOM   3354 C  CD  . LYS A 1 454 ? 60.871  162.501 107.007 1.00 134.71 ? 654 LYS A CD  1 
ATOM   3355 C  CE  . LYS A 1 454 ? 61.744  162.008 108.149 1.00 134.71 ? 654 LYS A CE  1 
ATOM   3356 N  NZ  . LYS A 1 454 ? 63.129  162.547 108.060 1.00 134.71 ? 654 LYS A NZ  1 
ATOM   3357 N  N   . ILE A 1 455 ? 61.648  159.321 103.508 1.00 133.90 ? 655 ILE A N   1 
ATOM   3358 C  CA  . ILE A 1 455 ? 61.751  157.869 103.489 1.00 133.90 ? 655 ILE A CA  1 
ATOM   3359 C  C   . ILE A 1 455 ? 62.244  157.398 104.850 1.00 133.90 ? 655 ILE A C   1 
ATOM   3360 O  O   . ILE A 1 455 ? 62.944  158.121 105.566 1.00 133.90 ? 655 ILE A O   1 
ATOM   3361 C  CB  . ILE A 1 455 ? 62.677  157.366 102.357 1.00 133.90 ? 655 ILE A CB  1 
ATOM   3362 C  CG1 . ILE A 1 455 ? 62.402  155.892 102.047 1.00 133.90 ? 655 ILE A CG1 1 
ATOM   3363 C  CG2 . ILE A 1 455 ? 64.139  157.565 102.722 1.00 133.90 ? 655 ILE A CG2 1 
ATOM   3364 C  CD1 . ILE A 1 455 ? 61.030  155.635 101.470 1.00 133.90 ? 655 ILE A CD1 1 
ATOM   3365 N  N   . ILE A 1 456 ? 61.853  156.180 105.214 1.00 133.07 ? 656 ILE A N   1 
ATOM   3366 C  CA  . ILE A 1 456 ? 62.255  155.556 106.469 1.00 133.07 ? 656 ILE A CA  1 
ATOM   3367 C  C   . ILE A 1 456 ? 63.059  154.315 106.113 1.00 133.07 ? 656 ILE A C   1 
ATOM   3368 O  O   . ILE A 1 456 ? 62.512  153.347 105.569 1.00 133.07 ? 656 ILE A O   1 
ATOM   3369 C  CB  . ILE A 1 456 ? 61.045  155.196 107.343 1.00 133.07 ? 656 ILE A CB  1 
ATOM   3370 C  CG1 . ILE A 1 456 ? 59.936  156.245 107.202 1.00 133.07 ? 656 ILE A CG1 1 
ATOM   3371 C  CG2 . ILE A 1 456 ? 61.464  155.051 108.799 1.00 133.07 ? 656 ILE A CG2 1 
ATOM   3372 C  CD1 . ILE A 1 456 ? 60.288  157.603 107.763 1.00 133.07 ? 656 ILE A CD1 1 
ATOM   3373 N  N   . ILE A 1 457 ? 64.354  154.328 106.416 1.00 132.56 ? 657 ILE A N   1 
ATOM   3374 C  CA  . ILE A 1 457 ? 65.212  153.177 106.159 1.00 132.56 ? 657 ILE A CA  1 
ATOM   3375 C  C   . ILE A 1 457 ? 65.569  152.548 107.500 1.00 132.56 ? 657 ILE A C   1 
ATOM   3376 O  O   . ILE A 1 457 ? 66.360  153.125 108.264 1.00 132.56 ? 657 ILE A O   1 
ATOM   3377 C  CB  . ILE A 1 457 ? 66.471  153.578 105.375 1.00 132.56 ? 657 ILE A CB  1 
ATOM   3378 C  CG1 . ILE A 1 457 ? 66.103  154.499 104.208 1.00 132.56 ? 657 ILE A CG1 1 
ATOM   3379 C  CG2 . ILE A 1 457 ? 67.205  152.342 104.879 1.00 132.56 ? 657 ILE A CG2 1 
ATOM   3380 C  CD1 . ILE A 1 457 ? 65.467  153.784 103.036 1.00 132.56 ? 657 ILE A CD1 1 
ATOM   3381 N  N   . PRO A 1 458 ? 64.998  151.393 107.839 1.00 130.38 ? 658 PRO A N   1 
ATOM   3382 C  CA  . PRO A 1 458 ? 65.360  150.735 109.100 1.00 130.38 ? 658 PRO A CA  1 
ATOM   3383 C  C   . PRO A 1 458 ? 66.833  150.364 109.125 1.00 130.38 ? 658 PRO A C   1 
ATOM   3384 O  O   . PRO A 1 458 ? 67.425  150.017 108.100 1.00 130.38 ? 658 PRO A O   1 
ATOM   3385 C  CB  . PRO A 1 458 ? 64.464  149.489 109.121 1.00 130.38 ? 658 PRO A CB  1 
ATOM   3386 C  CG  . PRO A 1 458 ? 63.340  149.806 108.188 1.00 130.38 ? 658 PRO A CG  1 
ATOM   3387 C  CD  . PRO A 1 458 ? 63.926  150.682 107.125 1.00 130.38 ? 658 PRO A CD  1 
ATOM   3388 N  N   . MET A 1 459 ? 67.429  150.447 110.317 1.00 130.31 ? 659 MET A N   1 
ATOM   3389 C  CA  . MET A 1 459 ? 68.845  150.135 110.464 1.00 130.31 ? 659 MET A CA  1 
ATOM   3390 C  C   . MET A 1 459 ? 69.141  148.668 110.183 1.00 130.31 ? 659 MET A C   1 
ATOM   3391 O  O   . MET A 1 459 ? 70.278  148.332 109.832 1.00 130.31 ? 659 MET A O   1 
ATOM   3392 C  CB  . MET A 1 459 ? 69.317  150.508 111.870 1.00 130.31 ? 659 MET A CB  1 
ATOM   3393 C  CG  . MET A 1 459 ? 70.823  150.643 112.005 1.00 130.31 ? 659 MET A CG  1 
ATOM   3394 S  SD  . MET A 1 459 ? 71.431  152.097 111.129 1.00 130.31 ? 659 MET A SD  1 
ATOM   3395 C  CE  . MET A 1 459 ? 73.139  152.124 111.657 1.00 130.31 ? 659 MET A CE  1 
ATOM   3396 N  N   . SER A 1 460 ? 68.148  147.788 110.326 1.00 127.45 ? 660 SER A N   1 
ATOM   3397 C  CA  . SER A 1 460 ? 68.343  146.376 110.019 1.00 127.45 ? 660 SER A CA  1 
ATOM   3398 C  C   . SER A 1 460 ? 68.469  146.120 108.523 1.00 127.45 ? 660 SER A C   1 
ATOM   3399 O  O   . SER A 1 460 ? 68.942  145.050 108.129 1.00 127.45 ? 660 SER A O   1 
ATOM   3400 C  CB  . SER A 1 460 ? 67.190  145.550 110.591 1.00 127.45 ? 660 SER A CB  1 
ATOM   3401 O  OG  . SER A 1 460 ? 65.984  145.808 109.893 1.00 127.45 ? 660 SER A OG  1 
ATOM   3402 N  N   . LYS A 1 461 ? 68.060  147.071 107.687 1.00 125.25 ? 661 LYS A N   1 
ATOM   3403 C  CA  . LYS A 1 461 ? 68.139  146.926 106.240 1.00 125.25 ? 661 LYS A CA  1 
ATOM   3404 C  C   . LYS A 1 461 ? 69.444  147.456 105.661 1.00 125.25 ? 661 LYS A C   1 
ATOM   3405 O  O   . LYS A 1 461 ? 69.627  147.406 104.440 1.00 125.25 ? 661 LYS A O   1 
ATOM   3406 C  CB  . LYS A 1 461 ? 66.956  147.639 105.574 1.00 125.25 ? 661 LYS A CB  1 
ATOM   3407 C  CG  . LYS A 1 461 ? 65.594  147.106 105.988 1.00 125.25 ? 661 LYS A CG  1 
ATOM   3408 C  CD  . LYS A 1 461 ? 65.443  145.636 105.629 1.00 125.25 ? 661 LYS A CD  1 
ATOM   3409 C  CE  . LYS A 1 461 ? 64.625  145.461 104.360 1.00 125.25 ? 661 LYS A CE  1 
ATOM   3410 N  NZ  . LYS A 1 461 ? 64.654  144.054 103.869 1.00 125.25 ? 661 LYS A NZ  1 
ATOM   3411 N  N   . LEU A 1 462 ? 70.350  147.957 106.498 1.00 126.48 ? 662 LEU A N   1 
ATOM   3412 C  CA  . LEU A 1 462 ? 71.623  148.495 106.045 1.00 126.48 ? 662 LEU A CA  1 
ATOM   3413 C  C   . LEU A 1 462 ? 72.754  147.889 106.863 1.00 126.48 ? 662 LEU A C   1 
ATOM   3414 O  O   . LEU A 1 462 ? 72.597  147.574 108.046 1.00 126.48 ? 662 LEU A O   1 
ATOM   3415 C  CB  . LEU A 1 462 ? 71.661  150.026 106.155 1.00 126.48 ? 662 LEU A CB  1 
ATOM   3416 C  CG  . LEU A 1 462 ? 70.675  150.812 105.289 1.00 126.48 ? 662 LEU A CG  1 
ATOM   3417 C  CD1 . LEU A 1 462 ? 70.888  152.308 105.462 1.00 126.48 ? 662 LEU A CD1 1 
ATOM   3418 C  CD2 . LEU A 1 462 ? 70.807  150.416 103.827 1.00 126.48 ? 662 LEU A CD2 1 
ATOM   3419 N  N   . LYS A 1 463 ? 73.904  147.727 106.213 1.00 127.11 ? 663 LYS A N   1 
ATOM   3420 C  CA  . LYS A 1 463 ? 75.074  147.173 106.877 1.00 127.11 ? 663 LYS A CA  1 
ATOM   3421 C  C   . LYS A 1 463 ? 75.684  148.207 107.824 1.00 127.11 ? 663 LYS A C   1 
ATOM   3422 O  O   . LYS A 1 463 ? 75.785  149.385 107.475 1.00 127.11 ? 663 LYS A O   1 
ATOM   3423 C  CB  . LYS A 1 463 ? 76.115  146.731 105.851 1.00 127.11 ? 663 LYS A CB  1 
ATOM   3424 C  CG  . LYS A 1 463 ? 75.630  145.647 104.903 1.00 127.11 ? 663 LYS A CG  1 
ATOM   3425 C  CD  . LYS A 1 463 ? 76.759  145.142 104.021 1.00 127.11 ? 663 LYS A CD  1 
ATOM   3426 C  CE  . LYS A 1 463 ? 76.241  144.204 102.943 1.00 127.11 ? 663 LYS A CE  1 
ATOM   3427 N  NZ  . LYS A 1 463 ? 77.328  143.752 102.031 1.00 127.11 ? 663 LYS A NZ  1 
ATOM   3428 N  N   . PRO A 1 464 ? 76.091  147.796 109.022 1.00 131.39 ? 664 PRO A N   1 
ATOM   3429 C  CA  . PRO A 1 464 ? 76.661  148.750 109.976 1.00 131.39 ? 664 PRO A CA  1 
ATOM   3430 C  C   . PRO A 1 464 ? 78.088  149.138 109.620 1.00 131.39 ? 664 PRO A C   1 
ATOM   3431 O  O   . PRO A 1 464 ? 78.831  148.379 108.995 1.00 131.39 ? 664 PRO A O   1 
ATOM   3432 C  CB  . PRO A 1 464 ? 76.617  147.984 111.303 1.00 131.39 ? 664 PRO A CB  1 
ATOM   3433 C  CG  . PRO A 1 464 ? 76.730  146.553 110.901 1.00 131.39 ? 664 PRO A CG  1 
ATOM   3434 C  CD  . PRO A 1 464 ? 76.039  146.427 109.565 1.00 131.39 ? 664 PRO A CD  1 
ATOM   3435 N  N   . TYR A 1 465 ? 78.461  150.345 110.047 1.00 135.40 ? 665 TYR A N   1 
ATOM   3436 C  CA  . TYR A 1 465 ? 79.804  150.891 109.843 1.00 135.40 ? 665 TYR A CA  1 
ATOM   3437 C  C   . TYR A 1 465 ? 80.205  150.850 108.369 1.00 135.40 ? 665 TYR A C   1 
ATOM   3438 O  O   . TYR A 1 465 ? 81.309  150.440 108.006 1.00 135.40 ? 665 TYR A O   1 
ATOM   3439 C  CB  . TYR A 1 465 ? 80.829  150.163 110.714 1.00 135.40 ? 665 TYR A CB  1 
ATOM   3440 C  CG  . TYR A 1 465 ? 81.000  150.775 112.086 1.00 135.40 ? 665 TYR A CG  1 
ATOM   3441 C  CD1 . TYR A 1 465 ? 81.685  151.972 112.251 1.00 135.40 ? 665 TYR A CD1 1 
ATOM   3442 C  CD2 . TYR A 1 465 ? 80.475  150.159 113.214 1.00 135.40 ? 665 TYR A CD2 1 
ATOM   3443 C  CE1 . TYR A 1 465 ? 81.843  152.538 113.502 1.00 135.40 ? 665 TYR A CE1 1 
ATOM   3444 C  CE2 . TYR A 1 465 ? 80.630  150.718 114.470 1.00 135.40 ? 665 TYR A CE2 1 
ATOM   3445 C  CZ  . TYR A 1 465 ? 81.315  151.907 114.607 1.00 135.40 ? 665 TYR A CZ  1 
ATOM   3446 N  N   . LYS A 1 466 ? 79.284  151.286 107.513 1.00 130.33 ? 666 LYS A N   1 
ATOM   3447 C  CA  . LYS A 1 466 ? 79.508  151.341 106.077 1.00 130.33 ? 666 LYS A CA  1 
ATOM   3448 C  C   . LYS A 1 466 ? 79.138  152.722 105.561 1.00 130.33 ? 666 LYS A C   1 
ATOM   3449 O  O   . LYS A 1 466 ? 78.246  153.380 106.106 1.00 130.33 ? 666 LYS A O   1 
ATOM   3450 C  CB  . LYS A 1 466 ? 78.689  150.274 105.342 1.00 130.33 ? 666 LYS A CB  1 
ATOM   3451 C  CG  . LYS A 1 466 ? 79.016  148.846 105.743 1.00 130.33 ? 666 LYS A CG  1 
ATOM   3452 C  CD  . LYS A 1 466 ? 79.834  148.146 104.674 1.00 130.33 ? 666 LYS A CD  1 
ATOM   3453 C  CE  . LYS A 1 466 ? 80.093  146.694 105.042 1.00 130.33 ? 666 LYS A CE  1 
ATOM   3454 N  NZ  . LYS A 1 466 ? 80.772  146.569 106.361 1.00 130.33 ? 666 LYS A NZ  1 
ATOM   3455 N  N   . ARG A 1 467 ? 79.826  153.157 104.511 1.00 125.63 ? 667 ARG A N   1 
ATOM   3456 C  CA  . ARG A 1 467 ? 79.554  154.436 103.871 1.00 125.63 ? 667 ARG A CA  1 
ATOM   3457 C  C   . ARG A 1 467 ? 78.638  154.212 102.675 1.00 125.63 ? 667 ARG A C   1 
ATOM   3458 O  O   . ARG A 1 467 ? 78.964  153.433 101.775 1.00 125.63 ? 667 ARG A O   1 
ATOM   3459 C  CB  . ARG A 1 467 ? 80.852  155.116 103.433 1.00 125.63 ? 667 ARG A CB  1 
ATOM   3460 C  CG  . ARG A 1 467 ? 80.651  156.456 102.741 1.00 125.63 ? 667 ARG A CG  1 
ATOM   3461 C  CD  . ARG A 1 467 ? 81.946  157.252 102.688 1.00 125.63 ? 667 ARG A CD  1 
ATOM   3462 N  NE  . ARG A 1 467 ? 82.901  156.691 101.740 1.00 125.63 ? 667 ARG A NE  1 
ATOM   3463 C  CZ  . ARG A 1 467 ? 83.924  157.360 101.225 1.00 125.63 ? 667 ARG A CZ  1 
ATOM   3464 N  N   . TYR A 1 468 ? 77.496  154.888 102.676 1.00 121.43 ? 668 TYR A N   1 
ATOM   3465 C  CA  . TYR A 1 468 ? 76.503  154.787 101.618 1.00 121.43 ? 668 TYR A CA  1 
ATOM   3466 C  C   . TYR A 1 468 ? 76.407  156.112 100.867 1.00 121.43 ? 668 TYR A C   1 
ATOM   3467 O  O   . TYR A 1 468 ? 76.741  157.181 101.386 1.00 121.43 ? 668 TYR A O   1 
ATOM   3468 C  CB  . TYR A 1 468 ? 75.142  154.383 102.187 1.00 121.43 ? 668 TYR A CB  1 
ATOM   3469 C  CG  . TYR A 1 468 ? 75.044  152.939 102.618 1.00 121.43 ? 668 TYR A CG  1 
ATOM   3470 C  CD1 . TYR A 1 468 ? 75.584  152.515 103.826 1.00 121.43 ? 668 TYR A CD1 1 
ATOM   3471 C  CD2 . TYR A 1 468 ? 74.406  151.998 101.820 1.00 121.43 ? 668 TYR A CD2 1 
ATOM   3472 C  CE1 . TYR A 1 468 ? 75.492  151.195 104.224 1.00 121.43 ? 668 TYR A CE1 1 
ATOM   3473 C  CE2 . TYR A 1 468 ? 74.309  150.676 102.210 1.00 121.43 ? 668 TYR A CE2 1 
ATOM   3474 C  CZ  . TYR A 1 468 ? 74.854  150.280 103.413 1.00 121.43 ? 668 TYR A CZ  1 
ATOM   3475 N  N   . VAL A 1 469 ? 75.937  156.023 99.624  1.00 115.66 ? 669 VAL A N   1 
ATOM   3476 C  CA  . VAL A 1 469 ? 75.760  157.180 98.756  1.00 115.66 ? 669 VAL A CA  1 
ATOM   3477 C  C   . VAL A 1 469 ? 74.327  157.182 98.242  1.00 115.66 ? 669 VAL A C   1 
ATOM   3478 O  O   . VAL A 1 469 ? 73.851  156.175 97.704  1.00 115.66 ? 669 VAL A O   1 
ATOM   3479 C  CB  . VAL A 1 469 ? 76.759  157.176 97.581  1.00 115.66 ? 669 VAL A CB  1 
ATOM   3480 C  CG1 . VAL A 1 469 ? 76.217  157.978 96.407  1.00 115.66 ? 669 VAL A CG1 1 
ATOM   3481 C  CG2 . VAL A 1 469 ? 78.102  157.724 98.028  1.00 115.66 ? 669 VAL A CG2 1 
ATOM   3482 N  N   . PHE A 1 470 ? 73.639  158.306 98.419  1.00 116.62 ? 670 PHE A N   1 
ATOM   3483 C  CA  . PHE A 1 470 ? 72.301  158.515 97.885  1.00 116.62 ? 670 PHE A CA  1 
ATOM   3484 C  C   . PHE A 1 470 ? 72.420  159.375 96.634  1.00 116.62 ? 670 PHE A C   1 
ATOM   3485 O  O   . PHE A 1 470 ? 72.996  160.468 96.683  1.00 116.62 ? 670 PHE A O   1 
ATOM   3486 C  CB  . PHE A 1 470 ? 71.402  159.186 98.923  1.00 116.62 ? 670 PHE A CB  1 
ATOM   3487 C  CG  . PHE A 1 470 ? 70.101  159.688 98.366  1.00 116.62 ? 670 PHE A CG  1 
ATOM   3488 C  CD1 . PHE A 1 470 ? 69.124  158.800 97.945  1.00 116.62 ? 670 PHE A CD1 1 
ATOM   3489 C  CD2 . PHE A 1 470 ? 69.851  161.046 98.270  1.00 116.62 ? 670 PHE A CD2 1 
ATOM   3490 C  CE1 . PHE A 1 470 ? 67.924  159.260 97.435  1.00 116.62 ? 670 PHE A CE1 1 
ATOM   3491 C  CE2 . PHE A 1 470 ? 68.655  161.511 97.761  1.00 116.62 ? 670 PHE A CE2 1 
ATOM   3492 C  CZ  . PHE A 1 470 ? 67.690  160.617 97.343  1.00 116.62 ? 670 PHE A CZ  1 
ATOM   3493 N  N   . SER A 1 471 ? 71.883  158.882 95.520  1.00 112.41 ? 671 SER A N   1 
ATOM   3494 C  CA  . SER A 1 471 ? 72.017  159.544 94.232  1.00 112.41 ? 671 SER A CA  1 
ATOM   3495 C  C   . SER A 1 471 ? 70.652  159.672 93.570  1.00 112.41 ? 671 SER A C   1 
ATOM   3496 O  O   . SER A 1 471 ? 69.724  158.908 93.850  1.00 112.41 ? 671 SER A O   1 
ATOM   3497 C  CB  . SER A 1 471 ? 72.976  158.783 93.306  1.00 112.41 ? 671 SER A CB  1 
ATOM   3498 O  OG  . SER A 1 471 ? 74.286  158.751 93.843  1.00 112.41 ? 671 SER A OG  1 
ATOM   3499 N  N   . GLY A 1 472 ? 70.547  160.650 92.681  1.00 114.04 ? 672 GLY A N   1 
ATOM   3500 C  CA  . GLY A 1 472 ? 69.300  160.872 91.973  1.00 114.04 ? 672 GLY A CA  1 
ATOM   3501 C  C   . GLY A 1 472 ? 69.509  161.788 90.789  1.00 114.04 ? 672 GLY A C   1 
ATOM   3502 O  O   . GLY A 1 472 ? 70.575  162.388 90.615  1.00 114.04 ? 672 GLY A O   1 
ATOM   3503 N  N   . TYR A 1 473 ? 68.466  161.882 89.967  1.00 114.75 ? 673 TYR A N   1 
ATOM   3504 C  CA  . TYR A 1 473 ? 68.454  162.753 88.800  1.00 114.75 ? 673 TYR A CA  1 
ATOM   3505 C  C   . TYR A 1 473 ? 67.351  163.791 88.948  1.00 114.75 ? 673 TYR A C   1 
ATOM   3506 O  O   . TYR A 1 473 ? 66.210  163.454 89.281  1.00 114.75 ? 673 TYR A O   1 
ATOM   3507 C  CB  . TYR A 1 473 ? 68.253  161.953 87.508  1.00 114.75 ? 673 TYR A CB  1 
ATOM   3508 C  CG  . TYR A 1 473 ? 69.506  161.268 87.012  1.00 114.75 ? 673 TYR A CG  1 
ATOM   3509 C  CD1 . TYR A 1 473 ? 69.899  160.038 87.522  1.00 114.75 ? 673 TYR A CD1 1 
ATOM   3510 C  CD2 . TYR A 1 473 ? 70.296  161.854 86.031  1.00 114.75 ? 673 TYR A CD2 1 
ATOM   3511 C  CE1 . TYR A 1 473 ? 71.045  159.411 87.070  1.00 114.75 ? 673 TYR A CE1 1 
ATOM   3512 C  CE2 . TYR A 1 473 ? 71.442  161.234 85.572  1.00 114.75 ? 673 TYR A CE2 1 
ATOM   3513 C  CZ  . TYR A 1 473 ? 71.812  160.012 86.095  1.00 114.75 ? 673 TYR A CZ  1 
ATOM   3514 N  N   . SER A 1 474 ? 67.697  165.051 88.686  1.00 121.44 ? 674 SER A N   1 
ATOM   3515 C  CA  . SER A 1 474 ? 66.778  166.168 88.863  1.00 121.44 ? 674 SER A CA  1 
ATOM   3516 C  C   . SER A 1 474 ? 66.716  167.001 87.591  1.00 121.44 ? 674 SER A C   1 
ATOM   3517 O  O   . SER A 1 474 ? 67.655  167.018 86.793  1.00 121.44 ? 674 SER A O   1 
ATOM   3518 C  CB  . SER A 1 474 ? 67.197  167.056 90.044  1.00 121.44 ? 674 SER A CB  1 
ATOM   3519 O  OG  . SER A 1 474 ? 68.486  167.609 89.835  1.00 121.44 ? 674 SER A OG  1 
ATOM   3520 N  N   . LYS A 1 475 ? 65.592  167.693 87.410  1.00 126.14 ? 675 LYS A N   1 
ATOM   3521 C  CA  . LYS A 1 475 ? 65.388  168.533 86.238  1.00 126.14 ? 675 LYS A CA  1 
ATOM   3522 C  C   . LYS A 1 475 ? 64.414  169.648 86.586  1.00 126.14 ? 675 LYS A C   1 
ATOM   3523 O  O   . LYS A 1 475 ? 63.408  169.415 87.261  1.00 126.14 ? 675 LYS A O   1 
ATOM   3524 C  CB  . LYS A 1 475 ? 64.865  167.712 85.051  1.00 126.14 ? 675 LYS A CB  1 
ATOM   3525 C  CG  . LYS A 1 475 ? 63.958  168.476 84.099  1.00 126.14 ? 675 LYS A CG  1 
ATOM   3526 C  CD  . LYS A 1 475 ? 63.225  167.534 83.159  1.00 126.14 ? 675 LYS A CD  1 
ATOM   3527 C  CE  . LYS A 1 475 ? 62.127  168.255 82.398  1.00 126.14 ? 675 LYS A CE  1 
ATOM   3528 N  NZ  . LYS A 1 475 ? 61.383  167.336 81.495  1.00 126.14 ? 675 LYS A NZ  1 
ATOM   3529 N  N   . ASP A 1 476 ? 64.725  170.862 86.125  1.00 129.27 ? 676 ASP A N   1 
ATOM   3530 C  CA  . ASP A 1 476 ? 63.872  172.028 86.357  1.00 129.27 ? 676 ASP A CA  1 
ATOM   3531 C  C   . ASP A 1 476 ? 64.015  172.970 85.169  1.00 129.27 ? 676 ASP A C   1 
ATOM   3532 O  O   . ASP A 1 476 ? 65.033  173.668 85.036  1.00 129.27 ? 676 ASP A O   1 
ATOM   3533 C  CB  . ASP A 1 476 ? 64.225  172.737 87.661  1.00 129.27 ? 676 ASP A CB  1 
ATOM   3534 C  CG  . ASP A 1 476 ? 63.360  173.955 87.916  1.00 129.27 ? 676 ASP A CG  1 
ATOM   3535 O  OD1 . ASP A 1 476 ? 62.174  173.937 87.522  1.00 129.27 ? 676 ASP A OD1 1 
ATOM   3536 O  OD2 . ASP A 1 476 ? 63.865  174.932 88.507  1.00 129.27 ? 676 ASP A OD2 1 
ATOM   3537 N  N   . PRO A 1 477 ? 63.021  173.015 84.279  1.00 128.76 ? 677 PRO A N   1 
ATOM   3538 C  CA  . PRO A 1 477 ? 63.113  173.928 83.126  1.00 128.76 ? 677 PRO A CA  1 
ATOM   3539 C  C   . PRO A 1 477 ? 63.211  175.393 83.512  1.00 128.76 ? 677 PRO A C   1 
ATOM   3540 O  O   . PRO A 1 477 ? 63.838  176.174 82.784  1.00 128.76 ? 677 PRO A O   1 
ATOM   3541 C  CB  . PRO A 1 477 ? 61.822  173.636 82.345  1.00 128.76 ? 677 PRO A CB  1 
ATOM   3542 C  CG  . PRO A 1 477 ? 61.381  172.283 82.813  1.00 128.76 ? 677 PRO A CG  1 
ATOM   3543 C  CD  . PRO A 1 477 ? 61.798  172.198 84.248  1.00 128.76 ? 677 PRO A CD  1 
ATOM   3544 N  N   . SER A 1 478 ? 62.611  175.793 84.634  1.00 130.07 ? 678 SER A N   1 
ATOM   3545 C  CA  . SER A 1 478 ? 62.637  177.199 85.026  1.00 130.07 ? 678 SER A CA  1 
ATOM   3546 C  C   . SER A 1 478 ? 64.020  177.633 85.496  1.00 130.07 ? 678 SER A C   1 
ATOM   3547 O  O   . SER A 1 478 ? 64.365  178.814 85.382  1.00 130.07 ? 678 SER A O   1 
ATOM   3548 C  CB  . SER A 1 478 ? 61.600  177.460 86.119  1.00 130.07 ? 678 SER A CB  1 
ATOM   3549 O  OG  . SER A 1 478 ? 61.984  176.854 87.340  1.00 130.07 ? 678 SER A OG  1 
ATOM   3550 N  N   . THR A 1 479 ? 64.816  176.697 86.022  1.00 130.63 ? 679 THR A N   1 
ATOM   3551 C  CA  . THR A 1 479 ? 66.164  176.981 86.524  1.00 130.63 ? 679 THR A CA  1 
ATOM   3552 C  C   . THR A 1 479 ? 66.148  178.089 87.575  1.00 130.63 ? 679 THR A C   1 
ATOM   3553 O  O   . THR A 1 479 ? 67.029  178.952 87.611  1.00 130.63 ? 679 THR A O   1 
ATOM   3554 C  CB  . THR A 1 479 ? 67.126  177.333 85.384  1.00 130.63 ? 679 THR A CB  1 
ATOM   3555 O  OG1 . THR A 1 479 ? 66.872  178.671 84.936  1.00 130.63 ? 679 THR A OG1 1 
ATOM   3556 C  CG2 . THR A 1 479 ? 66.952  176.370 84.219  1.00 130.63 ? 679 THR A CG2 1 
ATOM   3557 N  N   . SER A 1 480 ? 65.134  178.069 88.439  1.00 130.76 ? 680 SER A N   1 
ATOM   3558 C  CA  . SER A 1 480 ? 65.000  179.084 89.477  1.00 130.76 ? 680 SER A CA  1 
ATOM   3559 C  C   . SER A 1 480 ? 64.844  178.448 90.853  1.00 130.76 ? 680 SER A C   1 
ATOM   3560 O  O   . SER A 1 480 ? 65.318  178.995 91.854  1.00 130.76 ? 680 SER A O   1 
ATOM   3561 C  CB  . SER A 1 480 ? 63.808  179.997 89.178  1.00 130.76 ? 680 SER A CB  1 
ATOM   3562 O  OG  . SER A 1 480 ? 62.628  179.242 88.963  1.00 130.76 ? 680 SER A OG  1 
ATOM   3563 N  N   . ASN A 1 481 ? 64.183  177.295 90.911  1.00 131.43 ? 681 ASN A N   1 
ATOM   3564 C  CA  . ASN A 1 481 ? 63.913  176.645 92.183  1.00 131.43 ? 681 ASN A CA  1 
ATOM   3565 C  C   . ASN A 1 481 ? 65.181  176.017 92.757  1.00 131.43 ? 681 ASN A C   1 
ATOM   3566 O  O   . ASN A 1 481 ? 66.194  175.849 92.072  1.00 131.43 ? 681 ASN A O   1 
ATOM   3567 C  CB  . ASN A 1 481 ? 62.828  175.580 92.017  1.00 131.43 ? 681 ASN A CB  1 
ATOM   3568 C  CG  . ASN A 1 481 ? 61.533  176.149 91.474  1.00 131.43 ? 681 ASN A CG  1 
ATOM   3569 O  OD1 . ASN A 1 481 ? 60.948  175.606 90.537  1.00 131.43 ? 681 ASN A OD1 1 
ATOM   3570 N  ND2 . ASN A 1 481 ? 61.078  177.250 92.060  1.00 131.43 ? 681 ASN A ND2 1 
ATOM   3571 N  N   . SER A 1 482 ? 65.113  175.674 94.042  1.00 132.91 ? 682 SER A N   1 
ATOM   3572 C  CA  . SER A 1 482 ? 66.209  175.032 94.752  1.00 132.91 ? 682 SER A CA  1 
ATOM   3573 C  C   . SER A 1 482 ? 65.664  173.886 95.592  1.00 132.91 ? 682 SER A C   1 
ATOM   3574 O  O   . SER A 1 482 ? 64.488  173.875 95.964  1.00 132.91 ? 682 SER A O   1 
ATOM   3575 C  CB  . SER A 1 482 ? 66.961  176.030 95.647  1.00 132.91 ? 682 SER A CB  1 
ATOM   3576 O  OG  . SER A 1 482 ? 67.736  175.356 96.623  1.00 132.91 ? 682 SER A OG  1 
ATOM   3577 N  N   . ILE A 1 483 ? 66.530  172.919 95.889  1.00 134.03 ? 683 ILE A N   1 
ATOM   3578 C  CA  . ILE A 1 483 ? 66.158  171.721 96.635  1.00 134.03 ? 683 ILE A CA  1 
ATOM   3579 C  C   . ILE A 1 483 ? 67.004  171.663 97.898  1.00 134.03 ? 683 ILE A C   1 
ATOM   3580 O  O   . ILE A 1 483 ? 68.192  171.997 97.869  1.00 134.03 ? 683 ILE A O   1 
ATOM   3581 C  CB  . ILE A 1 483 ? 66.350  170.448 95.791  1.00 134.03 ? 683 ILE A CB  1 
ATOM   3582 C  CG1 . ILE A 1 483 ? 65.655  170.591 94.436  1.00 134.03 ? 683 ILE A CG1 1 
ATOM   3583 C  CG2 . ILE A 1 483 ? 65.821  169.226 96.528  1.00 134.03 ? 683 ILE A CG2 1 
ATOM   3584 C  CD1 . ILE A 1 483 ? 66.191  169.651 93.379  1.00 134.03 ? 683 ILE A CD1 1 
ATOM   3585 N  N   . THR A 1 484 ? 66.393  171.252 99.006  1.00 136.41 ? 684 THR A N   1 
ATOM   3586 C  CA  . THR A 1 484 ? 67.121  171.031 100.247 1.00 136.41 ? 684 THR A CA  1 
ATOM   3587 C  C   . THR A 1 484 ? 67.271  169.534 100.497 1.00 136.41 ? 684 THR A C   1 
ATOM   3588 O  O   . THR A 1 484 ? 66.311  168.769 100.368 1.00 136.41 ? 684 THR A O   1 
ATOM   3589 C  CB  . THR A 1 484 ? 66.420  171.702 101.433 1.00 136.41 ? 684 THR A CB  1 
ATOM   3590 O  OG1 . THR A 1 484 ? 67.042  171.293 102.657 1.00 136.41 ? 684 THR A OG1 1 
ATOM   3591 C  CG2 . THR A 1 484 ? 64.942  171.352 101.468 1.00 136.41 ? 684 THR A CG2 1 
ATOM   3592 N  N   . VAL A 1 485 ? 68.490  169.121 100.837 1.00 136.96 ? 685 VAL A N   1 
ATOM   3593 C  CA  . VAL A 1 485 ? 68.826  167.720 101.051 1.00 136.96 ? 685 VAL A CA  1 
ATOM   3594 C  C   . VAL A 1 485 ? 69.222  167.540 102.508 1.00 136.96 ? 685 VAL A C   1 
ATOM   3595 O  O   . VAL A 1 485 ? 70.127  168.228 103.001 1.00 136.96 ? 685 VAL A O   1 
ATOM   3596 C  CB  . VAL A 1 485 ? 69.961  167.260 100.118 1.00 136.96 ? 685 VAL A CB  1 
ATOM   3597 C  CG1 . VAL A 1 485 ? 70.228  165.773 100.300 1.00 136.96 ? 685 VAL A CG1 1 
ATOM   3598 C  CG2 . VAL A 1 485 ? 69.622  167.576 98.670  1.00 136.96 ? 685 VAL A CG2 1 
ATOM   3599 N  N   . ASN A 1 486 ? 68.544  166.620 103.192 1.00 138.21 ? 686 ASN A N   1 
ATOM   3600 C  CA  . ASN A 1 486 ? 68.821  166.335 104.594 1.00 138.21 ? 686 ASN A CA  1 
ATOM   3601 C  C   . ASN A 1 486 ? 68.736  164.834 104.826 1.00 138.21 ? 686 ASN A C   1 
ATOM   3602 O  O   . ASN A 1 486 ? 67.812  164.172 104.337 1.00 138.21 ? 686 ASN A O   1 
ATOM   3603 C  CB  . ASN A 1 486 ? 67.845  167.078 105.512 1.00 138.21 ? 686 ASN A CB  1 
ATOM   3604 C  CG  . ASN A 1 486 ? 68.184  166.910 106.979 1.00 138.21 ? 686 ASN A CG  1 
ATOM   3605 O  OD1 . ASN A 1 486 ? 69.350  166.774 107.346 1.00 138.21 ? 686 ASN A OD1 1 
ATOM   3606 N  ND2 . ASN A 1 486 ? 67.162  166.917 107.827 1.00 138.21 ? 686 ASN A ND2 1 
ATOM   3607 N  N   . ILE A 1 487 ? 69.715  164.303 105.556 1.00 138.14 ? 687 ILE A N   1 
ATOM   3608 C  CA  . ILE A 1 487 ? 69.787  162.885 105.881 1.00 138.14 ? 687 ILE A CA  1 
ATOM   3609 C  C   . ILE A 1 487 ? 70.106  162.744 107.363 1.00 138.14 ? 687 ILE A C   1 
ATOM   3610 O  O   . ILE A 1 487 ? 71.128  163.255 107.833 1.00 138.14 ? 687 ILE A O   1 
ATOM   3611 C  CB  . ILE A 1 487 ? 70.844  162.155 105.029 1.00 138.14 ? 687 ILE A CB  1 
ATOM   3612 C  CG1 . ILE A 1 487 ? 70.413  162.111 103.562 1.00 138.14 ? 687 ILE A CG1 1 
ATOM   3613 C  CG2 . ILE A 1 487 ? 71.079  160.749 105.559 1.00 138.14 ? 687 ILE A CG2 1 
ATOM   3614 C  CD1 . ILE A 1 487 ? 71.569  162.036 102.587 1.00 138.14 ? 687 ILE A CD1 1 
ATOM   3615 N  N   . LYS A 1 488 ? 69.233  162.054 108.092 1.00 139.42 ? 688 LYS A N   1 
ATOM   3616 C  CA  . LYS A 1 488 ? 69.464  161.704 109.487 1.00 139.42 ? 688 LYS A CA  1 
ATOM   3617 C  C   . LYS A 1 488 ? 70.106  160.322 109.534 1.00 139.42 ? 688 LYS A C   1 
ATOM   3618 O  O   . LYS A 1 488 ? 69.480  159.326 109.148 1.00 139.42 ? 688 LYS A O   1 
ATOM   3619 C  CB  . LYS A 1 488 ? 68.161  161.729 110.286 1.00 139.42 ? 688 LYS A CB  1 
ATOM   3620 C  CG  . LYS A 1 488 ? 68.251  161.065 111.656 1.00 139.42 ? 688 LYS A CG  1 
ATOM   3621 C  CD  . LYS A 1 488 ? 69.373  161.661 112.497 1.00 139.42 ? 688 LYS A CD  1 
ATOM   3622 C  CE  . LYS A 1 488 ? 69.793  160.714 113.609 1.00 139.42 ? 688 LYS A CE  1 
ATOM   3623 N  NZ  . LYS A 1 488 ? 71.192  160.964 114.053 1.00 139.42 ? 688 LYS A NZ  1 
ATOM   3624 N  N   . SER A 1 489 ? 71.342  160.276 110.012 1.00 140.12 ? 689 SER A N   1 
ATOM   3625 C  CA  . SER A 1 489 ? 72.170  159.077 110.056 1.00 140.12 ? 689 SER A CA  1 
ATOM   3626 C  C   . SER A 1 489 ? 73.086  159.209 111.268 1.00 140.12 ? 689 SER A C   1 
ATOM   3627 O  O   . SER A 1 489 ? 72.771  159.937 112.216 1.00 140.12 ? 689 SER A O   1 
ATOM   3628 C  CB  . SER A 1 489 ? 72.932  158.897 108.732 1.00 140.12 ? 689 SER A CB  1 
ATOM   3629 O  OG  . SER A 1 489 ? 73.759  160.015 108.463 1.00 140.12 ? 689 SER A OG  1 
ATOM   3630 N  N   . LYS A 1 490 ? 74.203  158.475 111.258 1.00 139.49 ? 690 LYS A N   1 
ATOM   3631 C  CA  . LYS A 1 490 ? 75.222  158.662 112.288 1.00 139.49 ? 690 LYS A CA  1 
ATOM   3632 C  C   . LYS A 1 490 ? 75.564  160.137 112.461 1.00 139.49 ? 690 LYS A C   1 
ATOM   3633 O  O   . LYS A 1 490 ? 75.695  160.628 113.588 1.00 139.49 ? 690 LYS A O   1 
ATOM   3634 C  CB  . LYS A 1 490 ? 76.478  157.865 111.934 1.00 139.49 ? 690 LYS A CB  1 
ATOM   3635 C  CG  . LYS A 1 490 ? 77.685  158.200 112.796 1.00 139.49 ? 690 LYS A CG  1 
ATOM   3636 C  CD  . LYS A 1 490 ? 78.982  158.006 112.030 1.00 139.49 ? 690 LYS A CD  1 
ATOM   3637 C  CE  . LYS A 1 490 ? 79.354  159.257 111.250 1.00 139.49 ? 690 LYS A CE  1 
ATOM   3638 N  NZ  . LYS A 1 490 ? 79.757  160.373 112.149 1.00 139.49 ? 690 LYS A NZ  1 
ATOM   3639 N  N   . GLU A 1 491 ? 75.708  160.860 111.352 1.00 140.22 ? 691 GLU A N   1 
ATOM   3640 C  CA  . GLU A 1 491 ? 75.845  162.307 111.364 1.00 140.22 ? 691 GLU A CA  1 
ATOM   3641 C  C   . GLU A 1 491 ? 74.849  162.897 110.378 1.00 140.22 ? 691 GLU A C   1 
ATOM   3642 O  O   . GLU A 1 491 ? 74.675  162.375 109.272 1.00 140.22 ? 691 GLU A O   1 
ATOM   3643 C  CB  . GLU A 1 491 ? 77.272  162.743 111.004 1.00 140.22 ? 691 GLU A CB  1 
ATOM   3644 C  CG  . GLU A 1 491 ? 77.508  164.243 111.093 1.00 140.22 ? 691 GLU A CG  1 
ATOM   3645 C  CD  . GLU A 1 491 ? 77.332  164.945 109.760 1.00 140.22 ? 691 GLU A CD  1 
ATOM   3646 O  OE1 . GLU A 1 491 ? 77.173  164.249 108.736 1.00 140.22 ? 691 GLU A OE1 1 
ATOM   3647 O  OE2 . GLU A 1 491 ? 77.353  166.194 109.738 1.00 140.22 ? 691 GLU A OE2 1 
ATOM   3648 N  N   . GLN A 1 492 ? 74.197  163.984 110.779 1.00 139.63 ? 692 GLN A N   1 
ATOM   3649 C  CA  . GLN A 1 492 ? 73.179  164.631 109.961 1.00 139.63 ? 692 GLN A CA  1 
ATOM   3650 C  C   . GLN A 1 492 ? 73.788  165.819 109.229 1.00 139.63 ? 692 GLN A C   1 
ATOM   3651 O  O   . GLN A 1 492 ? 74.428  166.676 109.847 1.00 139.63 ? 692 GLN A O   1 
ATOM   3652 C  CB  . GLN A 1 492 ? 71.995  165.085 110.817 1.00 139.63 ? 692 GLN A CB  1 
ATOM   3653 C  CG  . GLN A 1 492 ? 70.913  165.812 110.033 1.00 139.63 ? 692 GLN A CG  1 
ATOM   3654 C  CD  . GLN A 1 492 ? 69.537  165.656 110.650 1.00 139.63 ? 692 GLN A CD  1 
ATOM   3655 O  OE1 . GLN A 1 492 ? 68.550  166.177 110.129 1.00 139.63 ? 692 GLN A OE1 1 
ATOM   3656 N  NE2 . GLN A 1 492 ? 69.465  164.937 111.764 1.00 139.63 ? 692 GLN A NE2 1 
ATOM   3657 N  N   . LYS A 1 493 ? 73.583  165.865 107.915 1.00 139.24 ? 693 LYS A N   1 
ATOM   3658 C  CA  . LYS A 1 493 ? 74.121  166.918 107.069 1.00 139.24 ? 693 LYS A CA  1 
ATOM   3659 C  C   . LYS A 1 493 ? 72.991  167.596 106.304 1.00 139.24 ? 693 LYS A C   1 
ATOM   3660 O  O   . LYS A 1 493 ? 71.988  166.966 105.956 1.00 139.24 ? 693 LYS A O   1 
ATOM   3661 C  CB  . LYS A 1 493 ? 75.158  166.363 106.083 1.00 139.24 ? 693 LYS A CB  1 
ATOM   3662 C  CG  . LYS A 1 493 ? 76.163  167.391 105.588 1.00 139.24 ? 693 LYS A CG  1 
ATOM   3663 C  CD  . LYS A 1 493 ? 77.309  167.558 106.572 1.00 139.24 ? 693 LYS A CD  1 
ATOM   3664 C  CE  . LYS A 1 493 ? 77.959  168.925 106.437 1.00 139.24 ? 693 LYS A CE  1 
ATOM   3665 N  NZ  . LYS A 1 493 ? 76.976  170.027 106.638 1.00 139.24 ? 693 LYS A NZ  1 
ATOM   3666 N  N   . THR A 1 494 ? 73.165  168.890 106.046 1.00 139.22 ? 694 THR A N   1 
ATOM   3667 C  CA  . THR A 1 494 ? 72.194  169.688 105.310 1.00 139.22 ? 694 THR A CA  1 
ATOM   3668 C  C   . THR A 1 494 ? 72.888  170.332 104.121 1.00 139.22 ? 694 THR A C   1 
ATOM   3669 O  O   . THR A 1 494 ? 73.964  170.920 104.272 1.00 139.22 ? 694 THR A O   1 
ATOM   3670 C  CB  . THR A 1 494 ? 71.566  170.767 106.202 1.00 139.22 ? 694 THR A CB  1 
ATOM   3671 O  OG1 . THR A 1 494 ? 71.232  170.201 107.476 1.00 139.22 ? 694 THR A OG1 1 
ATOM   3672 C  CG2 . THR A 1 494 ? 70.308  171.327 105.557 1.00 139.22 ? 694 THR A CG2 1 
ATOM   3673 N  N   . ASP A 1 495 ? 72.275  170.223 102.943 1.00 138.08 ? 695 ASP A N   1 
ATOM   3674 C  CA  . ASP A 1 495 ? 72.868  170.763 101.728 1.00 138.08 ? 695 ASP A CA  1 
ATOM   3675 C  C   . ASP A 1 495 ? 71.782  171.360 100.844 1.00 138.08 ? 695 ASP A C   1 
ATOM   3676 O  O   . ASP A 1 495 ? 70.592  171.086 101.012 1.00 138.08 ? 695 ASP A O   1 
ATOM   3677 C  CB  . ASP A 1 495 ? 73.649  169.691 100.956 1.00 138.08 ? 695 ASP A CB  1 
ATOM   3678 C  CG  . ASP A 1 495 ? 74.945  169.306 101.644 1.00 138.08 ? 695 ASP A CG  1 
ATOM   3679 O  OD1 . ASP A 1 495 ? 75.750  170.214 101.948 1.00 138.08 ? 695 ASP A OD1 1 
ATOM   3680 O  OD2 . ASP A 1 495 ? 75.161  168.099 101.880 1.00 138.08 ? 695 ASP A OD2 1 
ATOM   3681 N  N   . TYR A 1 496 ? 72.212  172.188 99.896  1.00 136.51 ? 696 TYR A N   1 
ATOM   3682 C  CA  . TYR A 1 496 ? 71.320  172.818 98.933  1.00 136.51 ? 696 TYR A CA  1 
ATOM   3683 C  C   . TYR A 1 496 ? 71.764  172.471 97.518  1.00 136.51 ? 696 TYR A C   1 
ATOM   3684 O  O   . TYR A 1 496 ? 72.961  172.491 97.209  1.00 136.51 ? 696 TYR A O   1 
ATOM   3685 C  CB  . TYR A 1 496 ? 71.285  174.339 99.118  1.00 136.51 ? 696 TYR A CB  1 
ATOM   3686 C  CG  . TYR A 1 496 ? 70.353  174.795 100.218 1.00 136.51 ? 696 TYR A CG  1 
ATOM   3687 C  CD1 . TYR A 1 496 ? 68.976  174.775 100.039 1.00 136.51 ? 696 TYR A CD1 1 
ATOM   3688 C  CD2 . TYR A 1 496 ? 70.849  175.242 101.435 1.00 136.51 ? 696 TYR A CD2 1 
ATOM   3689 C  CE1 . TYR A 1 496 ? 68.119  175.190 101.041 1.00 136.51 ? 696 TYR A CE1 1 
ATOM   3690 C  CE2 . TYR A 1 496 ? 70.000  175.660 102.443 1.00 136.51 ? 696 TYR A CE2 1 
ATOM   3691 C  CZ  . TYR A 1 496 ? 68.636  175.630 102.240 1.00 136.51 ? 696 TYR A CZ  1 
ATOM   3692 N  N   . LEU A 1 497 ? 70.794  172.154 96.667  1.00 132.11 ? 697 LEU A N   1 
ATOM   3693 C  CA  . LEU A 1 497 ? 71.036  171.754 95.287  1.00 132.11 ? 697 LEU A CA  1 
ATOM   3694 C  C   . LEU A 1 497 ? 70.313  172.711 94.352  1.00 132.11 ? 697 LEU A C   1 
ATOM   3695 O  O   . LEU A 1 497 ? 69.131  173.015 94.555  1.00 132.11 ? 697 LEU A O   1 
ATOM   3696 C  CB  . LEU A 1 497 ? 70.570  170.317 95.043  1.00 132.11 ? 697 LEU A CB  1 
ATOM   3697 C  CG  . LEU A 1 497 ? 70.647  169.797 93.606  1.00 132.11 ? 697 LEU A CG  1 
ATOM   3698 C  CD1 . LEU A 1 497 ? 72.092  169.593 93.184  1.00 132.11 ? 697 LEU A CD1 1 
ATOM   3699 C  CD2 . LEU A 1 497 ? 69.853  168.506 93.460  1.00 132.11 ? 697 LEU A CD2 1 
ATOM   3700 N  N   . VAL A 1 498 ? 71.025  173.186 93.333  1.00 131.59 ? 698 VAL A N   1 
ATOM   3701 C  CA  . VAL A 1 498 ? 70.470  174.081 92.324  1.00 131.59 ? 698 VAL A CA  1 
ATOM   3702 C  C   . VAL A 1 498 ? 70.312  173.281 91.033  1.00 131.59 ? 698 VAL A C   1 
ATOM   3703 O  O   . VAL A 1 498 ? 71.326  172.939 90.401  1.00 131.59 ? 698 VAL A O   1 
ATOM   3704 C  CB  . VAL A 1 498 ? 71.361  175.311 92.109  1.00 131.59 ? 698 VAL A CB  1 
ATOM   3705 C  CG1 . VAL A 1 498 ? 70.712  176.270 91.122  1.00 131.59 ? 698 VAL A CG1 1 
ATOM   3706 C  CG2 . VAL A 1 498 ? 71.635  176.004 93.435  1.00 131.59 ? 698 VAL A CG2 1 
ATOM   3707 N  N   . PRO A 1 499 ? 69.092  172.961 90.610  1.00 129.62 ? 699 PRO A N   1 
ATOM   3708 C  CA  . PRO A 1 499 ? 68.911  172.189 89.375  1.00 129.62 ? 699 PRO A CA  1 
ATOM   3709 C  C   . PRO A 1 499 ? 69.252  173.019 88.146  1.00 129.62 ? 699 PRO A C   1 
ATOM   3710 O  O   . PRO A 1 499 ? 69.370  174.244 88.189  1.00 129.62 ? 699 PRO A O   1 
ATOM   3711 C  CB  . PRO A 1 499 ? 67.426  171.808 89.394  1.00 129.62 ? 699 PRO A CB  1 
ATOM   3712 C  CG  . PRO A 1 499 ? 66.947  172.111 90.785  1.00 129.62 ? 699 PRO A CG  1 
ATOM   3713 C  CD  . PRO A 1 499 ? 67.815  173.211 91.298  1.00 129.62 ? 699 PRO A CD  1 
ATOM   3714 N  N   . GLU A 1 500 ? 69.411  172.317 87.031  1.00 127.12 ? 700 GLU A N   1 
ATOM   3715 C  CA  . GLU A 1 500 ? 69.710  172.920 85.740  1.00 127.12 ? 700 GLU A CA  1 
ATOM   3716 C  C   . GLU A 1 500 ? 68.508  172.764 84.814  1.00 127.12 ? 700 GLU A C   1 
ATOM   3717 O  O   . GLU A 1 500 ? 67.456  172.251 85.205  1.00 127.12 ? 700 GLU A O   1 
ATOM   3718 C  CB  . GLU A 1 500 ? 70.965  172.293 85.123  1.00 127.12 ? 700 GLU A CB  1 
ATOM   3719 C  CG  . GLU A 1 500 ? 72.264  172.724 85.781  1.00 127.12 ? 700 GLU A CG  1 
ATOM   3720 C  CD  . GLU A 1 500 ? 73.468  172.516 84.885  1.00 127.12 ? 700 GLU A CD  1 
ATOM   3721 O  OE1 . GLU A 1 500 ? 73.398  172.890 83.696  1.00 127.12 ? 700 GLU A OE1 1 
ATOM   3722 O  OE2 . GLU A 1 500 ? 74.485  171.975 85.370  1.00 127.12 ? 700 GLU A OE2 1 
ATOM   3723 N  N   . LYS A 1 501 ? 68.676  173.219 83.570  1.00 125.92 ? 701 LYS A N   1 
ATOM   3724 C  CA  . LYS A 1 501 ? 67.587  173.138 82.599  1.00 125.92 ? 701 LYS A CA  1 
ATOM   3725 C  C   . LYS A 1 501 ? 67.227  171.690 82.290  1.00 125.92 ? 701 LYS A C   1 
ATOM   3726 O  O   . LYS A 1 501 ? 66.045  171.347 82.176  1.00 125.92 ? 701 LYS A O   1 
ATOM   3727 C  CB  . LYS A 1 501 ? 67.971  173.880 81.319  1.00 125.92 ? 701 LYS A CB  1 
ATOM   3728 C  CG  . LYS A 1 501 ? 66.882  173.890 80.259  1.00 125.92 ? 701 LYS A CG  1 
ATOM   3729 C  CD  . LYS A 1 501 ? 67.360  174.557 78.980  1.00 125.92 ? 701 LYS A CD  1 
ATOM   3730 C  CE  . LYS A 1 501 ? 66.733  173.914 77.754  1.00 125.92 ? 701 LYS A CE  1 
ATOM   3731 N  NZ  . LYS A 1 501 ? 67.679  172.996 77.062  1.00 125.92 ? 701 LYS A NZ  1 
ATOM   3732 N  N   . ASP A 1 502 ? 68.228  170.827 82.153  1.00 124.39 ? 702 ASP A N   1 
ATOM   3733 C  CA  . ASP A 1 502 ? 68.022  169.421 81.843  1.00 124.39 ? 702 ASP A CA  1 
ATOM   3734 C  C   . ASP A 1 502 ? 68.366  168.572 83.066  1.00 124.39 ? 702 ASP A C   1 
ATOM   3735 O  O   . ASP A 1 502 ? 68.684  169.089 84.142  1.00 124.39 ? 702 ASP A O   1 
ATOM   3736 C  CB  . ASP A 1 502 ? 68.847  169.017 80.618  1.00 124.39 ? 702 ASP A CB  1 
ATOM   3737 C  CG  . ASP A 1 502 ? 68.369  169.692 79.348  1.00 124.39 ? 702 ASP A CG  1 
ATOM   3738 O  OD1 . ASP A 1 502 ? 67.163  170.003 79.257  1.00 124.39 ? 702 ASP A OD1 1 
ATOM   3739 O  OD2 . ASP A 1 502 ? 69.199  169.908 78.439  1.00 124.39 ? 702 ASP A OD2 1 
ATOM   3740 N  N   . TYR A 1 503 ? 68.298  167.255 82.893  1.00 122.64 ? 703 TYR A N   1 
ATOM   3741 C  CA  . TYR A 1 503 ? 68.528  166.327 83.991  1.00 122.64 ? 703 TYR A CA  1 
ATOM   3742 C  C   . TYR A 1 503 ? 69.998  166.318 84.392  1.00 122.64 ? 703 TYR A C   1 
ATOM   3743 O  O   . TYR A 1 503 ? 70.886  166.235 83.538  1.00 122.64 ? 703 TYR A O   1 
ATOM   3744 C  CB  . TYR A 1 503 ? 68.079  164.918 83.599  1.00 122.64 ? 703 TYR A CB  1 
ATOM   3745 C  CG  . TYR A 1 503 ? 66.666  164.585 84.024  1.00 122.64 ? 703 TYR A CG  1 
ATOM   3746 C  CD1 . TYR A 1 503 ? 66.348  164.411 85.364  1.00 122.64 ? 703 TYR A CD1 1 
ATOM   3747 C  CD2 . TYR A 1 503 ? 65.652  164.446 83.086  1.00 122.64 ? 703 TYR A CD2 1 
ATOM   3748 C  CE1 . TYR A 1 503 ? 65.059  164.106 85.758  1.00 122.64 ? 703 TYR A CE1 1 
ATOM   3749 C  CE2 . TYR A 1 503 ? 64.360  164.139 83.470  1.00 122.64 ? 703 TYR A CE2 1 
ATOM   3750 C  CZ  . TYR A 1 503 ? 64.068  163.973 84.807  1.00 122.64 ? 703 TYR A CZ  1 
ATOM   3751 N  N   . THR A 1 504 ? 70.248  166.404 85.697  1.00 118.27 ? 704 THR A N   1 
ATOM   3752 C  CA  . THR A 1 504 ? 71.590  166.333 86.251  1.00 118.27 ? 704 THR A CA  1 
ATOM   3753 C  C   . THR A 1 504 ? 71.570  165.406 87.459  1.00 118.27 ? 704 THR A C   1 
ATOM   3754 O  O   . THR A 1 504 ? 70.546  165.246 88.128  1.00 118.27 ? 704 THR A O   1 
ATOM   3755 C  CB  . THR A 1 504 ? 72.122  167.715 86.652  1.00 118.27 ? 704 THR A CB  1 
ATOM   3756 O  OG1 . THR A 1 504 ? 71.096  168.447 87.332  1.00 118.27 ? 704 THR A OG1 1 
ATOM   3757 C  CG2 . THR A 1 504 ? 72.568  168.495 85.423  1.00 118.27 ? 704 THR A CG2 1 
ATOM   3758 N  N   . LYS A 1 505 ? 72.720  164.799 87.734  1.00 110.61 ? 705 LYS A N   1 
ATOM   3759 C  CA  . LYS A 1 505 ? 72.854  163.806 88.789  1.00 110.61 ? 705 LYS A CA  1 
ATOM   3760 C  C   . LYS A 1 505 ? 73.433  164.440 90.046  1.00 110.61 ? 705 LYS A C   1 
ATOM   3761 O  O   . LYS A 1 505 ? 74.400  165.207 89.980  1.00 110.61 ? 705 LYS A O   1 
ATOM   3762 C  CB  . LYS A 1 505 ? 73.741  162.642 88.339  1.00 110.61 ? 705 LYS A CB  1 
ATOM   3763 C  CG  . LYS A 1 505 ? 73.557  161.376 89.159  1.00 110.61 ? 705 LYS A CG  1 
ATOM   3764 C  CD  . LYS A 1 505 ? 74.508  160.281 88.709  1.00 110.61 ? 705 LYS A CD  1 
ATOM   3765 C  CE  . LYS A 1 505 ? 74.487  159.106 89.672  1.00 110.61 ? 705 LYS A CE  1 
ATOM   3766 N  NZ  . LYS A 1 505 ? 75.746  158.316 89.607  1.00 110.61 ? 705 LYS A NZ  1 
ATOM   3767 N  N   . PHE A 1 506 ? 72.835  164.114 91.189  1.00 115.83 ? 706 PHE A N   1 
ATOM   3768 C  CA  . PHE A 1 506 ? 73.320  164.554 92.487  1.00 115.83 ? 706 PHE A CA  1 
ATOM   3769 C  C   . PHE A 1 506 ? 73.570  163.338 93.368  1.00 115.83 ? 706 PHE A C   1 
ATOM   3770 O  O   . PHE A 1 506 ? 72.817  162.361 93.331  1.00 115.83 ? 706 PHE A O   1 
ATOM   3771 C  CB  . PHE A 1 506 ? 72.331  165.514 93.175  1.00 115.83 ? 706 PHE A CB  1 
ATOM   3772 C  CG  . PHE A 1 506 ? 70.994  164.898 93.485  1.00 115.83 ? 706 PHE A CG  1 
ATOM   3773 C  CD1 . PHE A 1 506 ? 69.976  164.911 92.546  1.00 115.83 ? 706 PHE A CD1 1 
ATOM   3774 C  CD2 . PHE A 1 506 ? 70.751  164.318 94.720  1.00 115.83 ? 706 PHE A CD2 1 
ATOM   3775 C  CE1 . PHE A 1 506 ? 68.744  164.351 92.830  1.00 115.83 ? 706 PHE A CE1 1 
ATOM   3776 C  CE2 . PHE A 1 506 ? 69.522  163.756 95.009  1.00 115.83 ? 706 PHE A CE2 1 
ATOM   3777 C  CZ  . PHE A 1 506 ? 68.518  163.772 94.063  1.00 115.83 ? 706 PHE A CZ  1 
ATOM   3778 N  N   . SER A 1 507 ? 74.642  163.409 94.157  1.00 117.92 ? 707 SER A N   1 
ATOM   3779 C  CA  . SER A 1 507 ? 75.033  162.308 95.031  1.00 117.92 ? 707 SER A CA  1 
ATOM   3780 C  C   . SER A 1 507 ? 75.564  162.868 96.341  1.00 117.92 ? 707 SER A C   1 
ATOM   3781 O  O   . SER A 1 507 ? 76.317  163.846 96.340  1.00 117.92 ? 707 SER A O   1 
ATOM   3782 C  CB  . SER A 1 507 ? 76.092  161.424 94.363  1.00 117.92 ? 707 SER A CB  1 
ATOM   3783 O  OG  . SER A 1 507 ? 75.595  160.841 93.172  1.00 117.92 ? 707 SER A OG  1 
ATOM   3784 N  N   . TYR A 1 508 ? 75.170  162.244 97.451  1.00 122.81 ? 708 TYR A N   1 
ATOM   3785 C  CA  . TYR A 1 508 ? 75.609  162.662 98.777  1.00 122.81 ? 708 TYR A CA  1 
ATOM   3786 C  C   . TYR A 1 508 ? 75.922  161.440 99.627  1.00 122.81 ? 708 TYR A C   1 
ATOM   3787 O  O   . TYR A 1 508 ? 75.213  160.433 99.568  1.00 122.81 ? 708 TYR A O   1 
ATOM   3788 C  CB  . TYR A 1 508 ? 74.549  163.531 99.467  1.00 122.81 ? 708 TYR A CB  1 
ATOM   3789 C  CG  . TYR A 1 508 ? 74.184  164.771 98.685  1.00 122.81 ? 708 TYR A CG  1 
ATOM   3790 C  CD1 . TYR A 1 508 ? 75.055  165.853 98.616  1.00 122.81 ? 708 TYR A CD1 1 
ATOM   3791 C  CD2 . TYR A 1 508 ? 72.974  164.861 98.011  1.00 122.81 ? 708 TYR A CD2 1 
ATOM   3792 C  CE1 . TYR A 1 508 ? 74.728  166.988 97.902  1.00 122.81 ? 708 TYR A CE1 1 
ATOM   3793 C  CE2 . TYR A 1 508 ? 72.638  165.993 97.292  1.00 122.81 ? 708 TYR A CE2 1 
ATOM   3794 C  CZ  . TYR A 1 508 ? 73.519  167.054 97.241  1.00 122.81 ? 708 TYR A CZ  1 
ATOM   3795 N  N   . GLU A 1 509 ? 76.979  161.538 100.428 1.00 125.08 ? 709 GLU A N   1 
ATOM   3796 C  CA  . GLU A 1 509 ? 77.470  160.423 101.225 1.00 125.08 ? 709 GLU A CA  1 
ATOM   3797 C  C   . GLU A 1 509 ? 76.988  160.519 102.668 1.00 125.08 ? 709 GLU A C   1 
ATOM   3798 O  O   . GLU A 1 509 ? 76.670  161.597 103.176 1.00 125.08 ? 709 GLU A O   1 
ATOM   3799 C  CB  . GLU A 1 509 ? 79.001  160.376 101.200 1.00 125.08 ? 709 GLU A CB  1 
ATOM   3800 C  CG  . GLU A 1 509 ? 79.616  160.516 99.818  1.00 125.08 ? 709 GLU A CG  1 
ATOM   3801 C  CD  . GLU A 1 509 ? 81.132  160.544 99.860  1.00 125.08 ? 709 GLU A CD  1 
ATOM   3802 O  OE1 . GLU A 1 509 ? 81.700  160.386 100.961 1.00 125.08 ? 709 GLU A OE1 1 
ATOM   3803 O  OE2 . GLU A 1 509 ? 81.755  160.725 98.793  1.00 125.08 ? 709 GLU A OE2 1 
ATOM   3804 N  N   . PHE A 1 510 ? 76.939  159.362 103.326 1.00 127.41 ? 710 PHE A N   1 
ATOM   3805 C  CA  . PHE A 1 510 ? 76.667  159.299 104.757 1.00 127.41 ? 710 PHE A CA  1 
ATOM   3806 C  C   . PHE A 1 510 ? 77.205  157.980 105.295 1.00 127.41 ? 710 PHE A C   1 
ATOM   3807 O  O   . PHE A 1 510 ? 77.576  157.086 104.533 1.00 127.41 ? 710 PHE A O   1 
ATOM   3808 C  CB  . PHE A 1 510 ? 75.172  159.457 105.066 1.00 127.41 ? 710 PHE A CB  1 
ATOM   3809 C  CG  . PHE A 1 510 ? 74.295  158.419 104.425 1.00 127.41 ? 710 PHE A CG  1 
ATOM   3810 C  CD1 . PHE A 1 510 ? 73.769  158.622 103.161 1.00 127.41 ? 710 PHE A CD1 1 
ATOM   3811 C  CD2 . PHE A 1 510 ? 73.974  157.251 105.099 1.00 127.41 ? 710 PHE A CD2 1 
ATOM   3812 C  CE1 . PHE A 1 510 ? 72.953  157.674 102.573 1.00 127.41 ? 710 PHE A CE1 1 
ATOM   3813 C  CE2 . PHE A 1 510 ? 73.159  156.299 104.517 1.00 127.41 ? 710 PHE A CE2 1 
ATOM   3814 C  CZ  . PHE A 1 510 ? 72.646  156.512 103.252 1.00 127.41 ? 710 PHE A CZ  1 
ATOM   3815 N  N   . GLU A 1 511 ? 77.252  157.875 106.622 1.00 132.63 ? 711 GLU A N   1 
ATOM   3816 C  CA  . GLU A 1 511 ? 77.836  156.720 107.290 1.00 132.63 ? 711 GLU A CA  1 
ATOM   3817 C  C   . GLU A 1 511 ? 76.861  156.157 108.317 1.00 132.63 ? 711 GLU A C   1 
ATOM   3818 O  O   . GLU A 1 511 ? 75.824  156.752 108.621 1.00 132.63 ? 711 GLU A O   1 
ATOM   3819 C  CB  . GLU A 1 511 ? 79.167  157.077 107.967 1.00 132.63 ? 711 GLU A CB  1 
ATOM   3820 C  CG  . GLU A 1 511 ? 80.283  157.429 106.997 1.00 132.63 ? 711 GLU A CG  1 
ATOM   3821 C  CD  . GLU A 1 511 ? 81.564  157.823 107.704 1.00 132.63 ? 711 GLU A CD  1 
ATOM   3822 O  OE1 . GLU A 1 511 ? 81.574  157.847 108.953 1.00 132.63 ? 711 GLU A OE1 1 
ATOM   3823 O  OE2 . GLU A 1 511 ? 82.563  158.111 107.012 1.00 132.63 ? 711 GLU A OE2 1 
ATOM   3824 N  N   . THR A 1 512 ? 77.213  154.988 108.851 1.00 134.10 ? 712 THR A N   1 
ATOM   3825 C  CA  . THR A 1 512 ? 76.407  154.285 109.837 1.00 134.10 ? 712 THR A CA  1 
ATOM   3826 C  C   . THR A 1 512 ? 77.297  153.819 110.982 1.00 134.10 ? 712 THR A C   1 
ATOM   3827 O  O   . THR A 1 512 ? 78.514  153.680 110.833 1.00 134.10 ? 712 THR A O   1 
ATOM   3828 C  CB  . THR A 1 512 ? 75.678  153.079 109.223 1.00 134.10 ? 712 THR A CB  1 
ATOM   3829 O  OG1 . THR A 1 512 ? 76.633  152.195 108.624 1.00 134.10 ? 712 THR A OG1 1 
ATOM   3830 C  CG2 . THR A 1 512 ? 74.677  153.531 108.170 1.00 134.10 ? 712 THR A CG2 1 
ATOM   3831 N  N   . THR A 1 513 ? 76.673  153.575 112.134 1.00 135.50 ? 713 THR A N   1 
ATOM   3832 C  CA  . THR A 1 513 ? 77.391  153.106 113.317 1.00 135.50 ? 713 THR A CA  1 
ATOM   3833 C  C   . THR A 1 513 ? 76.505  152.141 114.089 1.00 135.50 ? 713 THR A C   1 
ATOM   3834 O  O   . THR A 1 513 ? 75.422  152.522 114.541 1.00 135.50 ? 713 THR A O   1 
ATOM   3835 C  CB  . THR A 1 513 ? 77.808  154.274 114.216 1.00 135.50 ? 713 THR A CB  1 
ATOM   3836 O  OG1 . THR A 1 513 ? 76.795  155.288 114.194 1.00 135.50 ? 713 THR A OG1 1 
ATOM   3837 C  CG2 . THR A 1 513 ? 79.134  154.863 113.760 1.00 135.50 ? 713 THR A CG2 1 
ATOM   3838 N  N   . GLY A 1 514 ? 76.965  150.901 114.239 1.00 133.30 ? 714 GLY A N   1 
ATOM   3839 C  CA  . GLY A 1 514 ? 76.276  149.927 115.063 1.00 133.30 ? 714 GLY A CA  1 
ATOM   3840 C  C   . GLY A 1 514 ? 75.069  149.293 114.403 1.00 133.30 ? 714 GLY A C   1 
ATOM   3841 O  O   . GLY A 1 514 ? 74.297  149.973 113.721 1.00 133.30 ? 714 GLY A O   1 
ATOM   3842 N  N   . LYS A 1 515 ? 74.892  147.984 114.604 1.00 131.35 ? 715 LYS A N   1 
ATOM   3843 C  CA  . LYS A 1 515 ? 73.731  147.303 114.041 1.00 131.35 ? 715 LYS A CA  1 
ATOM   3844 C  C   . LYS A 1 515 ? 72.449  147.704 114.763 1.00 131.35 ? 715 LYS A C   1 
ATOM   3845 O  O   . LYS A 1 515 ? 71.430  147.978 114.120 1.00 131.35 ? 715 LYS A O   1 
ATOM   3846 C  CB  . LYS A 1 515 ? 73.931  145.789 114.099 1.00 131.35 ? 715 LYS A CB  1 
ATOM   3847 C  CG  . LYS A 1 515 ? 72.764  144.979 113.554 1.00 131.35 ? 715 LYS A CG  1 
ATOM   3848 C  CD  . LYS A 1 515 ? 72.345  145.451 112.171 1.00 131.35 ? 715 LYS A CD  1 
ATOM   3849 C  CE  . LYS A 1 515 ? 73.040  144.656 111.077 1.00 131.35 ? 715 LYS A CE  1 
ATOM   3850 N  NZ  . LYS A 1 515 ? 72.900  145.309 109.746 1.00 131.35 ? 715 LYS A NZ  1 
ATOM   3851 N  N   . ASP A 1 516 ? 72.482  147.745 116.095 1.00 133.03 ? 716 ASP A N   1 
ATOM   3852 C  CA  . ASP A 1 516 ? 71.314  148.112 116.895 1.00 133.03 ? 716 ASP A CA  1 
ATOM   3853 C  C   . ASP A 1 516 ? 71.425  149.589 117.259 1.00 133.03 ? 716 ASP A C   1 
ATOM   3854 O  O   . ASP A 1 516 ? 71.760  149.964 118.383 1.00 133.03 ? 716 ASP A O   1 
ATOM   3855 C  CB  . ASP A 1 516 ? 71.207  147.222 118.131 1.00 133.03 ? 716 ASP A CB  1 
ATOM   3856 C  CG  . ASP A 1 516 ? 72.557  146.928 118.758 1.00 133.03 ? 716 ASP A CG  1 
ATOM   3857 O  OD1 . ASP A 1 516 ? 73.521  147.672 118.479 1.00 133.03 ? 716 ASP A OD1 1 
ATOM   3858 O  OD2 . ASP A 1 516 ? 72.653  145.952 119.532 1.00 133.03 ? 716 ASP A OD2 1 
ATOM   3859 N  N   . SER A 1 517 ? 71.133  150.439 116.276 1.00 133.60 ? 717 SER A N   1 
ATOM   3860 C  CA  . SER A 1 517 ? 71.209  151.883 116.464 1.00 133.60 ? 717 SER A CA  1 
ATOM   3861 C  C   . SER A 1 517 ? 69.928  152.561 115.994 1.00 133.60 ? 717 SER A C   1 
ATOM   3862 O  O   . SER A 1 517 ? 68.932  151.890 115.704 1.00 133.60 ? 717 SER A O   1 
ATOM   3863 C  CB  . SER A 1 517 ? 72.417  152.457 115.722 1.00 133.60 ? 717 SER A CB  1 
ATOM   3864 O  OG  . SER A 1 517 ? 73.626  152.129 116.386 1.00 133.60 ? 717 SER A OG  1 
ATOM   3865 N  N   . SER A 1 518 ? 69.946  153.888 115.920 1.00 134.83 ? 718 SER A N   1 
ATOM   3866 C  CA  . SER A 1 518 ? 68.779  154.639 115.483 1.00 134.83 ? 718 SER A CA  1 
ATOM   3867 C  C   . SER A 1 518 ? 68.501  154.387 114.002 1.00 134.83 ? 718 SER A C   1 
ATOM   3868 O  O   . SER A 1 518 ? 69.352  153.904 113.249 1.00 134.83 ? 718 SER A O   1 
ATOM   3869 C  CB  . SER A 1 518 ? 68.978  156.133 115.741 1.00 134.83 ? 718 SER A CB  1 
ATOM   3870 O  OG  . SER A 1 518 ? 70.154  156.608 115.109 1.00 134.83 ? 718 SER A OG  1 
ATOM   3871 N  N   . ASP A 1 519 ? 67.282  154.720 113.588 1.00 135.88 ? 719 ASP A N   1 
ATOM   3872 C  CA  . ASP A 1 519 ? 66.849  154.500 112.218 1.00 135.88 ? 719 ASP A CA  1 
ATOM   3873 C  C   . ASP A 1 519 ? 67.499  155.515 111.278 1.00 135.88 ? 719 ASP A C   1 
ATOM   3874 O  O   . ASP A 1 519 ? 68.134  156.485 111.701 1.00 135.88 ? 719 ASP A O   1 
ATOM   3875 C  CB  . ASP A 1 519 ? 65.326  154.581 112.119 1.00 135.88 ? 719 ASP A CB  1 
ATOM   3876 C  CG  . ASP A 1 519 ? 64.636  153.449 112.854 1.00 135.88 ? 719 ASP A CG  1 
ATOM   3877 O  OD1 . ASP A 1 519 ? 65.306  152.442 113.162 1.00 135.88 ? 719 ASP A OD1 1 
ATOM   3878 O  OD2 . ASP A 1 519 ? 63.422  153.568 113.124 1.00 135.88 ? 719 ASP A OD2 1 
ATOM   3879 N  N   . ILE A 1 520 ? 67.330  155.278 109.979 1.00 136.26 ? 720 ILE A N   1 
ATOM   3880 C  CA  . ILE A 1 520 ? 67.893  156.127 108.934 1.00 136.26 ? 720 ILE A CA  1 
ATOM   3881 C  C   . ILE A 1 520 ? 66.753  156.914 108.304 1.00 136.26 ? 720 ILE A C   1 
ATOM   3882 O  O   . ILE A 1 520 ? 65.698  156.348 107.988 1.00 136.26 ? 720 ILE A O   1 
ATOM   3883 C  CB  . ILE A 1 520 ? 68.648  155.300 107.881 1.00 136.26 ? 720 ILE A CB  1 
ATOM   3884 C  CG1 . ILE A 1 520 ? 69.829  154.570 108.524 1.00 136.26 ? 720 ILE A CG1 1 
ATOM   3885 C  CG2 . ILE A 1 520 ? 69.128  156.190 106.743 1.00 136.26 ? 720 ILE A CG2 1 
ATOM   3886 C  CD1 . ILE A 1 520 ? 70.862  155.494 109.129 1.00 136.26 ? 720 ILE A CD1 1 
ATOM   3887 N  N   . GLU A 1 521 ? 66.953  158.218 108.131 1.00 137.50 ? 721 GLU A N   1 
ATOM   3888 C  CA  . GLU A 1 521 ? 65.952  159.087 107.530 1.00 137.50 ? 721 GLU A CA  1 
ATOM   3889 C  C   . GLU A 1 521 ? 66.581  159.849 106.374 1.00 137.50 ? 721 GLU A C   1 
ATOM   3890 O  O   . GLU A 1 521 ? 67.729  160.286 106.472 1.00 137.50 ? 721 GLU A O   1 
ATOM   3891 C  CB  . GLU A 1 521 ? 65.384  160.067 108.562 1.00 137.50 ? 721 GLU A CB  1 
ATOM   3892 C  CG  . GLU A 1 521 ? 65.069  159.443 109.912 1.00 137.50 ? 721 GLU A CG  1 
ATOM   3893 C  CD  . GLU A 1 521 ? 63.901  158.479 109.851 1.00 137.50 ? 721 GLU A CD  1 
ATOM   3894 O  OE1 . GLU A 1 521 ? 62.966  158.732 109.066 1.00 137.50 ? 721 GLU A OE1 1 
ATOM   3895 O  OE2 . GLU A 1 521 ? 63.921  157.470 110.585 1.00 137.50 ? 721 GLU A OE2 1 
ATOM   3896 N  N   . ILE A 1 522 ? 65.840  159.994 105.279 1.00 135.67 ? 722 ILE A N   1 
ATOM   3897 C  CA  . ILE A 1 522 ? 66.259  160.820 104.152 1.00 135.67 ? 722 ILE A CA  1 
ATOM   3898 C  C   . ILE A 1 522 ? 65.060  161.630 103.690 1.00 135.67 ? 722 ILE A C   1 
ATOM   3899 O  O   . ILE A 1 522 ? 63.996  161.063 103.407 1.00 135.67 ? 722 ILE A O   1 
ATOM   3900 C  CB  . ILE A 1 522 ? 66.821  159.975 102.991 1.00 135.67 ? 722 ILE A CB  1 
ATOM   3901 C  CG1 . ILE A 1 522 ? 68.124  159.284 103.403 1.00 135.67 ? 722 ILE A CG1 1 
ATOM   3902 C  CG2 . ILE A 1 522 ? 67.045  160.837 101.759 1.00 135.67 ? 722 ILE A CG2 1 
ATOM   3903 C  CD1 . ILE A 1 522 ? 68.570  158.199 102.449 1.00 135.67 ? 722 ILE A CD1 1 
ATOM   3904 N  N   . THR A 1 523 ? 65.223  162.950 103.604 1.00 135.95 ? 723 THR A N   1 
ATOM   3905 C  CA  . THR A 1 523 ? 64.146  163.820 103.160 1.00 135.95 ? 723 THR A CA  1 
ATOM   3906 C  C   . THR A 1 523 ? 64.610  164.687 101.996 1.00 135.95 ? 723 THR A C   1 
ATOM   3907 O  O   . THR A 1 523 ? 65.791  165.028 101.879 1.00 135.95 ? 723 THR A O   1 
ATOM   3908 C  CB  . THR A 1 523 ? 63.623  164.706 104.306 1.00 135.95 ? 723 THR A CB  1 
ATOM   3909 O  OG1 . THR A 1 523 ? 62.436  165.386 103.882 1.00 135.95 ? 723 THR A OG1 1 
ATOM   3910 C  CG2 . THR A 1 523 ? 64.666  165.726 104.724 1.00 135.95 ? 723 THR A CG2 1 
ATOM   3911 N  N   . LEU A 1 524 ? 63.661  165.021 101.126 1.00 134.15 ? 724 LEU A N   1 
ATOM   3912 C  CA  . LEU A 1 524 ? 63.910  165.852 99.953  1.00 134.15 ? 724 LEU A CA  1 
ATOM   3913 C  C   . LEU A 1 524 ? 62.736  166.811 99.813  1.00 134.15 ? 724 LEU A C   1 
ATOM   3914 O  O   . LEU A 1 524 ? 61.580  166.379 99.734  1.00 134.15 ? 724 LEU A O   1 
ATOM   3915 C  CB  . LEU A 1 524 ? 64.081  165.000 98.696  1.00 134.15 ? 724 LEU A CB  1 
ATOM   3916 C  CG  . LEU A 1 524 ? 65.251  165.360 97.777  1.00 134.15 ? 724 LEU A CG  1 
ATOM   3917 C  CD1 . LEU A 1 524 ? 66.573  165.198 98.509  1.00 134.15 ? 724 LEU A CD1 1 
ATOM   3918 C  CD2 . LEU A 1 524 ? 65.228  164.504 96.521  1.00 134.15 ? 724 LEU A CD2 1 
ATOM   3919 N  N   . THR A 1 525 ? 63.026  168.109 99.793  1.00 134.18 ? 725 THR A N   1 
ATOM   3920 C  CA  . THR A 1 525 ? 61.999  169.133 99.696  1.00 134.18 ? 725 THR A CA  1 
ATOM   3921 C  C   . THR A 1 525 ? 62.423  170.183 98.681  1.00 134.18 ? 725 THR A C   1 
ATOM   3922 O  O   . THR A 1 525 ? 63.609  170.511 98.568  1.00 134.18 ? 725 THR A O   1 
ATOM   3923 C  CB  . THR A 1 525 ? 61.735  169.787 101.061 1.00 134.18 ? 725 THR A CB  1 
ATOM   3924 O  OG1 . THR A 1 525 ? 61.588  168.769 102.059 1.00 134.18 ? 725 THR A OG1 1 
ATOM   3925 C  CG2 . THR A 1 525 ? 60.466  170.626 101.022 1.00 134.18 ? 725 THR A CG2 1 
ATOM   3926 N  N   . SER A 1 526 ? 61.451  170.692 97.931  1.00 131.49 ? 726 SER A N   1 
ATOM   3927 C  CA  . SER A 1 526 ? 61.680  171.738 96.947  1.00 131.49 ? 726 SER A CA  1 
ATOM   3928 C  C   . SER A 1 526 ? 60.692  172.875 97.167  1.00 131.49 ? 726 SER A C   1 
ATOM   3929 O  O   . SER A 1 526 ? 59.509  172.651 97.441  1.00 131.49 ? 726 SER A O   1 
ATOM   3930 C  CB  . SER A 1 526 ? 61.546  171.198 95.518  1.00 131.49 ? 726 SER A CB  1 
ATOM   3931 O  OG  . SER A 1 526 ? 60.193  171.196 95.098  1.00 131.49 ? 726 SER A OG  1 
ATOM   3932 N  N   . SER A 1 527 ? 61.194  174.105 97.045  1.00 129.86 ? 727 SER A N   1 
ATOM   3933 C  CA  . SER A 1 527 ? 60.347  175.276 97.238  1.00 129.86 ? 727 SER A CA  1 
ATOM   3934 C  C   . SER A 1 527 ? 59.339  175.427 96.105  1.00 129.86 ? 727 SER A C   1 
ATOM   3935 O  O   . SER A 1 527 ? 58.173  175.762 96.342  1.00 129.86 ? 727 SER A O   1 
ATOM   3936 C  CB  . SER A 1 527 ? 61.211  176.533 97.360  1.00 129.86 ? 727 SER A CB  1 
ATOM   3937 O  OG  . SER A 1 527 ? 62.001  176.494 98.537  1.00 129.86 ? 727 SER A OG  1 
ATOM   3938 N  N   . GLY A 1 528 ? 59.769  175.183 94.869  1.00 129.99 ? 728 GLY A N   1 
ATOM   3939 C  CA  . GLY A 1 528 ? 58.891  175.332 93.725  1.00 129.99 ? 728 GLY A CA  1 
ATOM   3940 C  C   . GLY A 1 528 ? 58.510  174.021 93.069  1.00 129.99 ? 728 GLY A C   1 
ATOM   3941 O  O   . GLY A 1 528 ? 57.959  173.129 93.720  1.00 129.99 ? 728 GLY A O   1 
ATOM   3942 N  N   . VAL A 1 529 ? 58.800  173.894 91.776  1.00 130.77 ? 729 VAL A N   1 
ATOM   3943 C  CA  . VAL A 1 529 ? 58.461  172.707 90.998  1.00 130.77 ? 729 VAL A CA  1 
ATOM   3944 C  C   . VAL A 1 529 ? 59.750  172.126 90.434  1.00 130.77 ? 729 VAL A C   1 
ATOM   3945 O  O   . VAL A 1 529 ? 60.508  172.832 89.758  1.00 130.77 ? 729 VAL A O   1 
ATOM   3946 C  CB  . VAL A 1 529 ? 57.468  173.025 89.867  1.00 130.77 ? 729 VAL A CB  1 
ATOM   3947 C  CG1 . VAL A 1 529 ? 57.391  171.865 88.884  1.00 130.77 ? 729 VAL A CG1 1 
ATOM   3948 C  CG2 . VAL A 1 529 ? 56.095  173.338 90.440  1.00 130.77 ? 729 VAL A CG2 1 
ATOM   3949 N  N   . ILE A 1 530 ? 59.997  170.847 90.710  1.00 129.72 ? 730 ILE A N   1 
ATOM   3950 C  CA  . ILE A 1 530 ? 61.168  170.132 90.226  1.00 129.72 ? 730 ILE A CA  1 
ATOM   3951 C  C   . ILE A 1 530 ? 60.726  168.758 89.736  1.00 129.72 ? 730 ILE A C   1 
ATOM   3952 O  O   . ILE A 1 530 ? 59.572  168.356 89.901  1.00 129.72 ? 730 ILE A O   1 
ATOM   3953 C  CB  . ILE A 1 530 ? 62.260  169.990 91.308  1.00 129.72 ? 730 ILE A CB  1 
ATOM   3954 C  CG1 . ILE A 1 530 ? 61.709  169.227 92.515  1.00 129.72 ? 730 ILE A CG1 1 
ATOM   3955 C  CG2 . ILE A 1 530 ? 62.799  171.354 91.719  1.00 129.72 ? 730 ILE A CG2 1 
ATOM   3956 C  CD1 . ILE A 1 530 ? 62.748  168.406 93.244  1.00 129.72 ? 730 ILE A CD1 1 
ATOM   3957 N  N   . PHE A 1 531 ? 61.661  168.035 89.125  1.00 128.26 ? 731 PHE A N   1 
ATOM   3958 C  CA  . PHE A 1 531 ? 61.437  166.665 88.691  1.00 128.26 ? 731 PHE A CA  1 
ATOM   3959 C  C   . PHE A 1 531 ? 62.506  165.768 89.297  1.00 128.26 ? 731 PHE A C   1 
ATOM   3960 O  O   . PHE A 1 531 ? 63.665  166.166 89.436  1.00 128.26 ? 731 PHE A O   1 
ATOM   3961 C  CB  . PHE A 1 531 ? 61.455  166.544 87.160  1.00 128.26 ? 731 PHE A CB  1 
ATOM   3962 C  CG  . PHE A 1 531 ? 60.365  167.322 86.478  1.00 128.26 ? 731 PHE A CG  1 
ATOM   3963 C  CD1 . PHE A 1 531 ? 59.110  166.766 86.293  1.00 128.26 ? 731 PHE A CD1 1 
ATOM   3964 C  CD2 . PHE A 1 531 ? 60.596  168.609 86.021  1.00 128.26 ? 731 PHE A CD2 1 
ATOM   3965 C  CE1 . PHE A 1 531 ? 58.107  167.478 85.665  1.00 128.26 ? 731 PHE A CE1 1 
ATOM   3966 C  CE2 . PHE A 1 531 ? 59.596  169.326 85.393  1.00 128.26 ? 731 PHE A CE2 1 
ATOM   3967 C  CZ  . PHE A 1 531 ? 58.349  168.760 85.216  1.00 128.26 ? 731 PHE A CZ  1 
ATOM   3968 N  N   . LEU A 1 532 ? 62.103  164.555 89.667  1.00 125.78 ? 732 LEU A N   1 
ATOM   3969 C  CA  . LEU A 1 532 ? 63.000  163.585 90.276  1.00 125.78 ? 732 LEU A CA  1 
ATOM   3970 C  C   . LEU A 1 532 ? 62.842  162.240 89.585  1.00 125.78 ? 732 LEU A C   1 
ATOM   3971 O  O   . LEU A 1 532 ? 61.720  161.791 89.333  1.00 125.78 ? 732 LEU A O   1 
ATOM   3972 C  CB  . LEU A 1 532 ? 62.725  163.438 91.777  1.00 125.78 ? 732 LEU A CB  1 
ATOM   3973 C  CG  . LEU A 1 532 ? 63.147  164.614 92.661  1.00 125.78 ? 732 LEU A CG  1 
ATOM   3974 C  CD1 . LEU A 1 532 ? 62.512  164.501 94.038  1.00 125.78 ? 732 LEU A CD1 1 
ATOM   3975 C  CD2 . LEU A 1 532 ? 64.663  164.686 92.769  1.00 125.78 ? 732 LEU A CD2 1 
ATOM   3976 N  N   . ASP A 1 533 ? 63.969  161.600 89.282  1.00 120.18 ? 733 ASP A N   1 
ATOM   3977 C  CA  . ASP A 1 533 ? 63.933  160.304 88.622  1.00 120.18 ? 733 ASP A CA  1 
ATOM   3978 C  C   . ASP A 1 533 ? 65.207  159.535 88.939  1.00 120.18 ? 733 ASP A C   1 
ATOM   3979 O  O   . ASP A 1 533 ? 66.256  160.126 89.213  1.00 120.18 ? 733 ASP A O   1 
ATOM   3980 C  CB  . ASP A 1 533 ? 63.763  160.450 87.105  1.00 120.18 ? 733 ASP A CB  1 
ATOM   3981 C  CG  . ASP A 1 533 ? 62.983  159.302 86.494  1.00 120.18 ? 733 ASP A CG  1 
ATOM   3982 O  OD1 . ASP A 1 533 ? 62.515  158.430 87.254  1.00 120.18 ? 733 ASP A OD1 1 
ATOM   3983 O  OD2 . ASP A 1 533 ? 62.836  159.274 85.254  1.00 120.18 ? 733 ASP A OD2 1 
ATOM   3984 N  N   . ASN A 1 534 ? 65.093  158.206 88.893  1.00 115.53 ? 734 ASN A N   1 
ATOM   3985 C  CA  . ASN A 1 534 ? 66.211  157.285 89.100  1.00 115.53 ? 734 ASN A CA  1 
ATOM   3986 C  C   . ASN A 1 534 ? 66.900  157.540 90.443  1.00 115.53 ? 734 ASN A C   1 
ATOM   3987 O  O   . ASN A 1 534 ? 68.070  157.919 90.514  1.00 115.53 ? 734 ASN A O   1 
ATOM   3988 C  CB  . ASN A 1 534 ? 67.209  157.364 87.940  1.00 115.53 ? 734 ASN A CB  1 
ATOM   3989 C  CG  . ASN A 1 534 ? 66.636  156.825 86.643  1.00 115.53 ? 734 ASN A CG  1 
ATOM   3990 O  OD1 . ASN A 1 534 ? 65.431  156.608 86.526  1.00 115.53 ? 734 ASN A OD1 1 
ATOM   3991 N  ND2 . ASN A 1 534 ? 67.504  156.599 85.663  1.00 115.53 ? 734 ASN A ND2 1 
ATOM   3992 N  N   . LEU A 1 535 ? 66.145  157.325 91.516  1.00 114.77 ? 735 LEU A N   1 
ATOM   3993 C  CA  . LEU A 1 535 ? 66.668  157.498 92.864  1.00 114.77 ? 735 LEU A CA  1 
ATOM   3994 C  C   . LEU A 1 535 ? 67.289  156.194 93.345  1.00 114.77 ? 735 LEU A C   1 
ATOM   3995 O  O   . LEU A 1 535 ? 66.659  155.136 93.287  1.00 114.77 ? 735 LEU A O   1 
ATOM   3996 C  CB  . LEU A 1 535 ? 65.562  157.944 93.824  1.00 114.77 ? 735 LEU A CB  1 
ATOM   3997 C  CG  . LEU A 1 535 ? 65.067  159.381 93.653  1.00 114.77 ? 735 LEU A CG  1 
ATOM   3998 C  CD1 . LEU A 1 535 ? 63.745  159.585 94.377  1.00 114.77 ? 735 LEU A CD1 1 
ATOM   3999 C  CD2 . LEU A 1 535 ? 66.111  160.374 94.141  1.00 114.77 ? 735 LEU A CD2 1 
ATOM   4000 N  N   . SER A 1 536 ? 68.530  156.274 93.823  1.00 110.59 ? 736 SER A N   1 
ATOM   4001 C  CA  . SER A 1 536 ? 69.280  155.070 94.143  1.00 110.59 ? 736 SER A CA  1 
ATOM   4002 C  C   . SER A 1 536 ? 70.066  155.253 95.434  1.00 110.59 ? 736 SER A C   1 
ATOM   4003 O  O   . SER A 1 536 ? 70.463  156.365 95.794  1.00 110.59 ? 736 SER A O   1 
ATOM   4004 C  CB  . SER A 1 536 ? 70.233  154.687 93.005  1.00 110.59 ? 736 SER A CB  1 
ATOM   4005 O  OG  . SER A 1 536 ? 71.326  155.586 92.931  1.00 110.59 ? 736 SER A OG  1 
ATOM   4006 N  N   . ILE A 1 537 ? 70.276  154.134 96.122  1.00 108.63 ? 737 ILE A N   1 
ATOM   4007 C  CA  . ILE A 1 537 ? 71.138  154.039 97.293  1.00 108.63 ? 737 ILE A CA  1 
ATOM   4008 C  C   . ILE A 1 537 ? 72.184  152.970 97.002  1.00 108.63 ? 737 ILE A C   1 
ATOM   4009 O  O   . ILE A 1 537 ? 71.835  151.830 96.674  1.00 108.63 ? 737 ILE A O   1 
ATOM   4010 C  CB  . ILE A 1 537 ? 70.339  153.692 98.564  1.00 108.63 ? 737 ILE A CB  1 
ATOM   4011 C  CG1 . ILE A 1 537 ? 69.612  154.927 99.098  1.00 108.63 ? 737 ILE A CG1 1 
ATOM   4012 C  CG2 . ILE A 1 537 ? 71.254  153.101 99.629  1.00 108.63 ? 737 ILE A CG2 1 
ATOM   4013 C  CD1 . ILE A 1 537 ? 70.495  155.859 99.897  1.00 108.63 ? 737 ILE A CD1 1 
ATOM   4014 N  N   . THR A 1 538 ? 73.457  153.339 97.121  1.00 105.17 ? 738 THR A N   1 
ATOM   4015 C  CA  . THR A 1 538 ? 74.568  152.456 96.797  1.00 105.17 ? 738 THR A CA  1 
ATOM   4016 C  C   . THR A 1 538 ? 75.497  152.342 97.997  1.00 105.17 ? 738 THR A C   1 
ATOM   4017 O  O   . THR A 1 538 ? 75.620  153.281 98.790  1.00 105.17 ? 738 THR A O   1 
ATOM   4018 C  CB  . THR A 1 538 ? 75.345  152.970 95.576  1.00 105.17 ? 738 THR A CB  1 
ATOM   4019 O  OG1 . THR A 1 538 ? 74.424  153.450 94.590  1.00 105.17 ? 738 THR A OG1 1 
ATOM   4020 C  CG2 . THR A 1 538 ? 76.184  151.857 94.965  1.00 105.17 ? 738 THR A CG2 1 
ATOM   4021 N  N   . GLU A 1 539 ? 76.146  151.188 98.134  1.00 114.08 ? 739 GLU A N   1 
ATOM   4022 C  CA  . GLU A 1 539 ? 77.036  150.927 99.258  1.00 114.08 ? 739 GLU A CA  1 
ATOM   4023 C  C   . GLU A 1 539 ? 78.486  151.079 98.812  1.00 114.08 ? 739 GLU A C   1 
ATOM   4024 O  O   . GLU A 1 539 ? 78.946  150.359 97.919  1.00 114.08 ? 739 GLU A O   1 
ATOM   4025 C  CB  . GLU A 1 539 ? 76.788  149.528 99.822  1.00 114.08 ? 739 GLU A CB  1 
ATOM   4026 C  CG  . GLU A 1 539 ? 77.869  149.042 100.774 1.00 114.08 ? 739 GLU A CG  1 
ATOM   4027 C  CD  . GLU A 1 539 ? 77.681  147.593 101.175 1.00 114.08 ? 739 GLU A CD  1 
ATOM   4028 O  OE1 . GLU A 1 539 ? 76.619  147.020 100.858 1.00 114.08 ? 739 GLU A OE1 1 
ATOM   4029 O  OE2 . GLU A 1 539 ? 78.598  147.026 101.808 1.00 114.08 ? 739 GLU A OE2 1 
ATOM   4030 N  N   . LEU A 1 540 ? 79.199  152.014 99.433  1.00 119.28 ? 740 LEU A N   1 
ATOM   4031 C  CA  . LEU A 1 540 ? 80.619  152.213 99.174  1.00 119.28 ? 740 LEU A CA  1 
ATOM   4032 C  C   . LEU A 1 540 ? 81.435  151.309 100.098 1.00 119.28 ? 740 LEU A C   1 
ATOM   4033 O  O   . LEU A 1 540 ? 80.914  150.374 100.714 1.00 119.28 ? 740 LEU A O   1 
ATOM   4034 C  CB  . LEU A 1 540 ? 80.993  153.683 99.337  1.00 119.28 ? 740 LEU A CB  1 
ATOM   4035 C  CG  . LEU A 1 540 ? 80.490  154.659 98.272  1.00 119.28 ? 740 LEU A CG  1 
ATOM   4036 C  CD1 . LEU A 1 540 ? 81.274  155.960 98.341  1.00 119.28 ? 740 LEU A CD1 1 
ATOM   4037 C  CD2 . LEU A 1 540 ? 80.587  154.044 96.884  1.00 119.28 ? 740 LEU A CD2 1 
ATOM   4038 N  N   . ASN A 1 541 ? 82.737  151.576 100.191 1.00 127.03 ? 741 ASN A N   1 
ATOM   4039 C  CA  . ASN A 1 541 ? 83.622  150.793 101.039 1.00 127.03 ? 741 ASN A CA  1 
ATOM   4040 C  C   . ASN A 1 541 ? 83.187  150.873 102.503 1.00 127.03 ? 741 ASN A C   1 
ATOM   4041 O  O   . ASN A 1 541 ? 82.401  151.734 102.907 1.00 127.03 ? 741 ASN A O   1 
ATOM   4042 C  CB  . ASN A 1 541 ? 85.065  151.274 100.889 1.00 127.03 ? 741 ASN A CB  1 
ATOM   4043 C  CG  . ASN A 1 541 ? 85.273  152.671 101.441 1.00 127.03 ? 741 ASN A CG  1 
ATOM   4044 O  OD1 . ASN A 1 541 ? 84.402  153.532 101.326 1.00 127.03 ? 741 ASN A OD1 1 
ATOM   4045 N  ND2 . ASN A 1 541 ? 86.432  152.902 102.047 1.00 127.03 ? 741 ASN A ND2 1 
ATOM   4046 N  N   . SER A 1 542 ? 83.723  149.956 103.305 1.00 132.93 ? 742 SER A N   1 
ATOM   4047 C  CA  . SER A 1 542 ? 83.348  149.813 104.706 1.00 132.93 ? 742 SER A CA  1 
ATOM   4048 C  C   . SER A 1 542 ? 84.276  150.655 105.573 1.00 132.93 ? 742 SER A C   1 
ATOM   4049 O  O   . SER A 1 542 ? 85.492  150.433 105.586 1.00 132.93 ? 742 SER A O   1 
ATOM   4050 C  CB  . SER A 1 542 ? 83.402  148.348 105.134 1.00 132.93 ? 742 SER A CB  1 
ATOM   4051 O  OG  . SER A 1 542 ? 84.700  147.809 104.947 1.00 132.93 ? 742 SER A OG  1 
ATOM   4052 N  N   . THR A 1 543 ? 83.702  151.613 106.292 1.00 137.60 ? 743 THR A N   1 
ATOM   4053 C  CA  . THR A 1 543 ? 84.482  152.402 107.232 1.00 137.60 ? 743 THR A CA  1 
ATOM   4054 C  C   . THR A 1 543 ? 84.854  151.550 108.445 1.00 137.60 ? 743 THR A C   1 
ATOM   4055 O  O   . THR A 1 543 ? 84.009  150.818 108.973 1.00 137.60 ? 743 THR A O   1 
ATOM   4056 C  CB  . THR A 1 543 ? 83.703  153.636 107.683 1.00 137.60 ? 743 THR A CB  1 
ATOM   4057 O  OG1 . THR A 1 543 ? 82.627  153.237 108.542 1.00 137.60 ? 743 THR A OG1 1 
ATOM   4058 C  CG2 . THR A 1 543 ? 83.136  154.375 106.481 1.00 137.60 ? 743 THR A CG2 1 
ATOM   4059 N  N   . PRO A 1 544 ? 86.102  151.611 108.903 1.00 141.18 ? 744 PRO A N   1 
ATOM   4060 C  CA  . PRO A 1 544 ? 86.496  150.815 110.071 1.00 141.18 ? 744 PRO A CA  1 
ATOM   4061 C  C   . PRO A 1 544 ? 85.789  151.285 111.333 1.00 141.18 ? 744 PRO A C   1 
ATOM   4062 O  O   . PRO A 1 544 ? 85.465  152.464 111.492 1.00 141.18 ? 744 PRO A O   1 
ATOM   4063 C  CB  . PRO A 1 544 ? 88.011  151.032 110.167 1.00 141.18 ? 744 PRO A CB  1 
ATOM   4064 C  CG  . PRO A 1 544 ? 88.299  152.254 109.376 1.00 141.18 ? 744 PRO A CG  1 
ATOM   4065 C  CD  . PRO A 1 544 ? 87.185  152.473 108.401 1.00 141.18 ? 744 PRO A CD  1 
ATOM   4066 N  N   . GLU A 1 545 ? 85.553  150.338 112.236 1.00 141.98 ? 745 GLU A N   1 
ATOM   4067 C  CA  . GLU A 1 545 ? 84.873  150.632 113.492 1.00 141.98 ? 745 GLU A CA  1 
ATOM   4068 C  C   . GLU A 1 545 ? 85.868  151.015 114.583 1.00 141.98 ? 745 GLU A C   1 
ATOM   4069 O  O   . GLU A 1 545 ? 86.915  150.385 114.732 1.00 141.98 ? 745 GLU A O   1 
ATOM   4070 C  CB  . GLU A 1 545 ? 84.035  149.432 113.942 1.00 141.98 ? 745 GLU A CB  1 
ATOM   4071 C  CG  . GLU A 1 545 ? 84.754  148.097 113.837 1.00 141.98 ? 745 GLU A CG  1 
ATOM   4072 C  CD  . GLU A 1 545 ? 83.973  146.964 114.476 1.00 141.98 ? 745 GLU A CD  1 
ATOM   4073 O  OE1 . GLU A 1 545 ? 82.903  147.233 115.062 1.00 141.98 ? 745 GLU A OE1 1 
ATOM   4074 O  OE2 . GLU A 1 545 ? 84.429  145.804 114.393 1.00 141.98 ? 745 GLU A OE2 1 
HETATM 4075 CA CA  . CA  B 2 .   ? 96.367  141.154 63.997  1.00 26.84  ? 901 CA  A CA  1 
HETATM 4076 CA CA  . CA  C 2 .   ? 96.982  140.995 59.450  1.00 34.97  ? 902 CA  A CA  1 
HETATM 4077 CA CA  . CA  D 2 .   ? 61.556  156.878 84.888  1.00 119.39 ? 903 CA  A CA  1 
# 
