data_2QT9
# 
_entry.id   2QT9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2QT9         
RCSB  RCSB044026   
WWPDB D_1000044026 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          2QTB 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        2QT9 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2007-08-01 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
_audit_author.name           'Scapin, G.' 
_audit_author.pdbx_ordinal   1 
# 
_citation.id                        primary 
_citation.title                     
'4-Arylcyclohexylalanine analogs as potent, selective, and orally active inhibitors of dipeptidyl peptidase IV.' 
_citation.journal_abbrev            Bioorg.Med.Chem.Lett. 
_citation.journal_volume            17 
_citation.page_first                5806 
_citation.page_last                 5811 
_citation.year                      2007 
_citation.journal_id_ASTM           BMCLE8 
_citation.country                   UK 
_citation.journal_id_ISSN           0960-894X 
_citation.journal_id_CSD            1127 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17851076 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2007.08.049 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kaelin, D.E.'     1  
primary 'Smenton, A.L.'    2  
primary 'Eiermann, G.J.'   3  
primary 'He, H.'           4  
primary 'Leiting, B.'      5  
primary 'Lyons, K.A.'      6  
primary 'Patel, R.A.'      7  
primary 'Patel, S.B.'      8  
primary 'Petrov, A.'       9  
primary 'Scapin, G.'       10 
primary 'Wu, J.K.'         11 
primary 'Thornberry, N.A.' 12 
primary 'Weber, A.E.'      13 
primary 'Duffy, J.L.'      14 
# 
_cell.entry_id           2QT9 
_cell.length_a           117.697 
_cell.length_b           126.072 
_cell.length_c           136.970 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2QT9 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
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 'Dipeptidyl peptidase 4' 88381.312 2    3.4.14.5 T39S ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   20   ?        ?    ? ? 
3 non-polymer syn 'SODIUM ION' 22.990    1    ?        ?    ? ? 
4 non-polymer syn 
;(2S,3S)-3-AMINO-4-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-5-YLCYCLOHEXYL)BUTANAMIDE
;
430.519   2    ?        ?    ? ? 
5 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208   4    ?        ?    ? ? 
6 water       nat water 18.015    1304 ?        ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, TP103, Adenosine deaminase complexing protein 2, ADABP' 
# 
_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       
;MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADTRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFN
AEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPV
GHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF
YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQ
NYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKG
TWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY
TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFR
LNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVL
GSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS
KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADTRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFN
AEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPV
GHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF
YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQ
NYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKG
TWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY
TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFR
LNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVL
GSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS
KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   THR n 
1 4   PRO n 
1 5   TRP n 
1 6   LYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LEU n 
1 10  GLY n 
1 11  LEU n 
1 12  LEU n 
1 13  GLY n 
1 14  ALA n 
1 15  ALA n 
1 16  ALA n 
1 17  LEU n 
1 18  VAL n 
1 19  THR n 
1 20  ILE n 
1 21  ILE n 
1 22  THR n 
1 23  VAL n 
1 24  PRO n 
1 25  VAL n 
1 26  VAL n 
1 27  LEU n 
1 28  LEU n 
1 29  ASN n 
1 30  LYS n 
1 31  GLY n 
1 32  THR n 
1 33  ASP n 
1 34  ASP n 
1 35  ALA n 
1 36  THR n 
1 37  ALA n 
1 38  ASP n 
1 39  THR n 
1 40  ARG n 
1 41  LYS n 
1 42  THR n 
1 43  TYR n 
1 44  THR n 
1 45  LEU n 
1 46  THR n 
1 47  ASP n 
1 48  TYR n 
1 49  LEU n 
1 50  LYS n 
1 51  ASN n 
1 52  THR n 
1 53  TYR n 
1 54  ARG n 
1 55  LEU n 
1 56  LYS n 
1 57  LEU n 
1 58  TYR n 
1 59  SER n 
1 60  LEU n 
1 61  ARG n 
1 62  TRP n 
1 63  ILE n 
1 64  SER n 
1 65  ASP n 
1 66  HIS n 
1 67  GLU n 
1 68  TYR n 
1 69  LEU n 
1 70  TYR n 
1 71  LYS n 
1 72  GLN n 
1 73  GLU n 
1 74  ASN n 
1 75  ASN n 
1 76  ILE n 
1 77  LEU n 
1 78  VAL n 
1 79  PHE n 
1 80  ASN n 
1 81  ALA n 
1 82  GLU n 
1 83  TYR n 
1 84  GLY n 
1 85  ASN n 
1 86  SER n 
1 87  SER n 
1 88  VAL n 
1 89  PHE n 
1 90  LEU n 
1 91  GLU n 
1 92  ASN n 
1 93  SER n 
1 94  THR n 
1 95  PHE n 
1 96  ASP n 
1 97  GLU n 
1 98  PHE n 
1 99  GLY n 
1 100 HIS n 
1 101 SER n 
1 102 ILE n 
1 103 ASN n 
1 104 ASP n 
1 105 TYR n 
1 106 SER n 
1 107 ILE n 
1 108 SER n 
1 109 PRO n 
1 110 ASP n 
1 111 GLY n 
1 112 GLN n 
1 113 PHE n 
1 114 ILE n 
1 115 LEU n 
1 116 LEU n 
1 117 GLU n 
1 118 TYR n 
1 119 ASN n 
1 120 TYR n 
1 121 VAL n 
1 122 LYS n 
1 123 GLN n 
1 124 TRP n 
1 125 ARG n 
1 126 HIS n 
1 127 SER n 
1 128 TYR n 
1 129 THR n 
1 130 ALA n 
1 131 SER n 
1 132 TYR n 
1 133 ASP n 
1 134 ILE n 
1 135 TYR n 
1 136 ASP n 
1 137 LEU n 
1 138 ASN n 
1 139 LYS n 
1 140 ARG n 
1 141 GLN n 
1 142 LEU n 
1 143 ILE n 
1 144 THR n 
1 145 GLU n 
1 146 GLU n 
1 147 ARG n 
1 148 ILE n 
1 149 PRO n 
1 150 ASN n 
1 151 ASN n 
1 152 THR n 
1 153 GLN n 
1 154 TRP n 
1 155 VAL n 
1 156 THR n 
1 157 TRP n 
1 158 SER n 
1 159 PRO n 
1 160 VAL n 
1 161 GLY n 
1 162 HIS n 
1 163 LYS n 
1 164 LEU n 
1 165 ALA n 
1 166 TYR n 
1 167 VAL n 
1 168 TRP n 
1 169 ASN n 
1 170 ASN n 
1 171 ASP n 
1 172 ILE n 
1 173 TYR n 
1 174 VAL n 
1 175 LYS n 
1 176 ILE n 
1 177 GLU n 
1 178 PRO n 
1 179 ASN n 
1 180 LEU n 
1 181 PRO n 
1 182 SER n 
1 183 TYR n 
1 184 ARG n 
1 185 ILE n 
1 186 THR n 
1 187 TRP n 
1 188 THR n 
1 189 GLY n 
1 190 LYS n 
1 191 GLU n 
1 192 ASP n 
1 193 ILE n 
1 194 ILE n 
1 195 TYR n 
1 196 ASN n 
1 197 GLY n 
1 198 ILE n 
1 199 THR n 
1 200 ASP n 
1 201 TRP n 
1 202 VAL n 
1 203 TYR n 
1 204 GLU n 
1 205 GLU n 
1 206 GLU n 
1 207 VAL n 
1 208 PHE n 
1 209 SER n 
1 210 ALA n 
1 211 TYR n 
1 212 SER n 
1 213 ALA n 
1 214 LEU n 
1 215 TRP n 
1 216 TRP n 
1 217 SER n 
1 218 PRO n 
1 219 ASN n 
1 220 GLY n 
1 221 THR n 
1 222 PHE n 
1 223 LEU n 
1 224 ALA n 
1 225 TYR n 
1 226 ALA n 
1 227 GLN n 
1 228 PHE n 
1 229 ASN n 
1 230 ASP n 
1 231 THR n 
1 232 GLU n 
1 233 VAL n 
1 234 PRO n 
1 235 LEU n 
1 236 ILE n 
1 237 GLU n 
1 238 TYR n 
1 239 SER n 
1 240 PHE n 
1 241 TYR n 
1 242 SER n 
1 243 ASP n 
1 244 GLU n 
1 245 SER n 
1 246 LEU n 
1 247 GLN n 
1 248 TYR n 
1 249 PRO n 
1 250 LYS n 
1 251 THR n 
1 252 VAL n 
1 253 ARG n 
1 254 VAL n 
1 255 PRO n 
1 256 TYR n 
1 257 PRO n 
1 258 LYS n 
1 259 ALA n 
1 260 GLY n 
1 261 ALA n 
1 262 VAL n 
1 263 ASN n 
1 264 PRO n 
1 265 THR n 
1 266 VAL n 
1 267 LYS n 
1 268 PHE n 
1 269 PHE n 
1 270 VAL n 
1 271 VAL n 
1 272 ASN n 
1 273 THR n 
1 274 ASP n 
1 275 SER n 
1 276 LEU n 
1 277 SER n 
1 278 SER n 
1 279 VAL n 
1 280 THR n 
1 281 ASN n 
1 282 ALA n 
1 283 THR n 
1 284 SER n 
1 285 ILE n 
1 286 GLN n 
1 287 ILE n 
1 288 THR n 
1 289 ALA n 
1 290 PRO n 
1 291 ALA n 
1 292 SER n 
1 293 MET n 
1 294 LEU n 
1 295 ILE n 
1 296 GLY n 
1 297 ASP n 
1 298 HIS n 
1 299 TYR n 
1 300 LEU n 
1 301 CYS n 
1 302 ASP n 
1 303 VAL n 
1 304 THR n 
1 305 TRP n 
1 306 ALA n 
1 307 THR n 
1 308 GLN n 
1 309 GLU n 
1 310 ARG n 
1 311 ILE n 
1 312 SER n 
1 313 LEU n 
1 314 GLN n 
1 315 TRP n 
1 316 LEU n 
1 317 ARG n 
1 318 ARG n 
1 319 ILE n 
1 320 GLN n 
1 321 ASN n 
1 322 TYR n 
1 323 SER n 
1 324 VAL n 
1 325 MET n 
1 326 ASP n 
1 327 ILE n 
1 328 CYS n 
1 329 ASP n 
1 330 TYR n 
1 331 ASP n 
1 332 GLU n 
1 333 SER n 
1 334 SER n 
1 335 GLY n 
1 336 ARG n 
1 337 TRP n 
1 338 ASN n 
1 339 CYS n 
1 340 LEU n 
1 341 VAL n 
1 342 ALA n 
1 343 ARG n 
1 344 GLN n 
1 345 HIS n 
1 346 ILE n 
1 347 GLU n 
1 348 MET n 
1 349 SER n 
1 350 THR n 
1 351 THR n 
1 352 GLY n 
1 353 TRP n 
1 354 VAL n 
1 355 GLY n 
1 356 ARG n 
1 357 PHE n 
1 358 ARG n 
1 359 PRO n 
1 360 SER n 
1 361 GLU n 
1 362 PRO n 
1 363 HIS n 
1 364 PHE n 
1 365 THR n 
1 366 LEU n 
1 367 ASP n 
1 368 GLY n 
1 369 ASN n 
1 370 SER n 
1 371 PHE n 
1 372 TYR n 
1 373 LYS n 
1 374 ILE n 
1 375 ILE n 
1 376 SER n 
1 377 ASN n 
1 378 GLU n 
1 379 GLU n 
1 380 GLY n 
1 381 TYR n 
1 382 ARG n 
1 383 HIS n 
1 384 ILE n 
1 385 CYS n 
1 386 TYR n 
1 387 PHE n 
1 388 GLN n 
1 389 ILE n 
1 390 ASP n 
1 391 LYS n 
1 392 LYS n 
1 393 ASP n 
1 394 CYS n 
1 395 THR n 
1 396 PHE n 
1 397 ILE n 
1 398 THR n 
1 399 LYS n 
1 400 GLY n 
1 401 THR n 
1 402 TRP n 
1 403 GLU n 
1 404 VAL n 
1 405 ILE n 
1 406 GLY n 
1 407 ILE n 
1 408 GLU n 
1 409 ALA n 
1 410 LEU n 
1 411 THR n 
1 412 SER n 
1 413 ASP n 
1 414 TYR n 
1 415 LEU n 
1 416 TYR n 
1 417 TYR n 
1 418 ILE n 
1 419 SER n 
1 420 ASN n 
1 421 GLU n 
1 422 TYR n 
1 423 LYS n 
1 424 GLY n 
1 425 MET n 
1 426 PRO n 
1 427 GLY n 
1 428 GLY n 
1 429 ARG n 
1 430 ASN n 
1 431 LEU n 
1 432 TYR n 
1 433 LYS n 
1 434 ILE n 
1 435 GLN n 
1 436 LEU n 
1 437 SER n 
1 438 ASP n 
1 439 TYR n 
1 440 THR n 
1 441 LYS n 
1 442 VAL n 
1 443 THR n 
1 444 CYS n 
1 445 LEU n 
1 446 SER n 
1 447 CYS n 
1 448 GLU n 
1 449 LEU n 
1 450 ASN n 
1 451 PRO n 
1 452 GLU n 
1 453 ARG n 
1 454 CYS n 
1 455 GLN n 
1 456 TYR n 
1 457 TYR n 
1 458 SER n 
1 459 VAL n 
1 460 SER n 
1 461 PHE n 
1 462 SER n 
1 463 LYS n 
1 464 GLU n 
1 465 ALA n 
1 466 LYS n 
1 467 TYR n 
1 468 TYR n 
1 469 GLN n 
1 470 LEU n 
1 471 ARG n 
1 472 CYS n 
1 473 SER n 
1 474 GLY n 
1 475 PRO n 
1 476 GLY n 
1 477 LEU n 
1 478 PRO n 
1 479 LEU n 
1 480 TYR n 
1 481 THR n 
1 482 LEU n 
1 483 HIS n 
1 484 SER n 
1 485 SER n 
1 486 VAL n 
1 487 ASN n 
1 488 ASP n 
1 489 LYS n 
1 490 GLY n 
1 491 LEU n 
1 492 ARG n 
1 493 VAL n 
1 494 LEU n 
1 495 GLU n 
1 496 ASP n 
1 497 ASN n 
1 498 SER n 
1 499 ALA n 
1 500 LEU n 
1 501 ASP n 
1 502 LYS n 
1 503 MET n 
1 504 LEU n 
1 505 GLN n 
1 506 ASN n 
1 507 VAL n 
1 508 GLN n 
1 509 MET n 
1 510 PRO n 
1 511 SER n 
1 512 LYS n 
1 513 LYS n 
1 514 LEU n 
1 515 ASP n 
1 516 PHE n 
1 517 ILE n 
1 518 ILE n 
1 519 LEU n 
1 520 ASN n 
1 521 GLU n 
1 522 THR n 
1 523 LYS n 
1 524 PHE n 
1 525 TRP n 
1 526 TYR n 
1 527 GLN n 
1 528 MET n 
1 529 ILE n 
1 530 LEU n 
1 531 PRO n 
1 532 PRO n 
1 533 HIS n 
1 534 PHE n 
1 535 ASP n 
1 536 LYS n 
1 537 SER n 
1 538 LYS n 
1 539 LYS n 
1 540 TYR n 
1 541 PRO n 
1 542 LEU n 
1 543 LEU n 
1 544 LEU n 
1 545 ASP n 
1 546 VAL n 
1 547 TYR n 
1 548 ALA n 
1 549 GLY n 
1 550 PRO n 
1 551 CYS n 
1 552 SER n 
1 553 GLN n 
1 554 LYS n 
1 555 ALA n 
1 556 ASP n 
1 557 THR n 
1 558 VAL n 
1 559 PHE n 
1 560 ARG n 
1 561 LEU n 
1 562 ASN n 
1 563 TRP n 
1 564 ALA n 
1 565 THR n 
1 566 TYR n 
1 567 LEU n 
1 568 ALA n 
1 569 SER n 
1 570 THR n 
1 571 GLU n 
1 572 ASN n 
1 573 ILE n 
1 574 ILE n 
1 575 VAL n 
1 576 ALA n 
1 577 SER n 
1 578 PHE n 
1 579 ASP n 
1 580 GLY n 
1 581 ARG n 
1 582 GLY n 
1 583 SER n 
1 584 GLY n 
1 585 TYR n 
1 586 GLN n 
1 587 GLY n 
1 588 ASP n 
1 589 LYS n 
1 590 ILE n 
1 591 MET n 
1 592 HIS n 
1 593 ALA n 
1 594 ILE n 
1 595 ASN n 
1 596 ARG n 
1 597 ARG n 
1 598 LEU n 
1 599 GLY n 
1 600 THR n 
1 601 PHE n 
1 602 GLU n 
1 603 VAL n 
1 604 GLU n 
1 605 ASP n 
1 606 GLN n 
1 607 ILE n 
1 608 GLU n 
1 609 ALA n 
1 610 ALA n 
1 611 ARG n 
1 612 GLN n 
1 613 PHE n 
1 614 SER n 
1 615 LYS n 
1 616 MET n 
1 617 GLY n 
1 618 PHE n 
1 619 VAL n 
1 620 ASP n 
1 621 ASN n 
1 622 LYS n 
1 623 ARG n 
1 624 ILE n 
1 625 ALA n 
1 626 ILE n 
1 627 TRP n 
1 628 GLY n 
1 629 TRP n 
1 630 SER n 
1 631 TYR n 
1 632 GLY n 
1 633 GLY n 
1 634 TYR n 
1 635 VAL n 
1 636 THR n 
1 637 SER n 
1 638 MET n 
1 639 VAL n 
1 640 LEU n 
1 641 GLY n 
1 642 SER n 
1 643 GLY n 
1 644 SER n 
1 645 GLY n 
1 646 VAL n 
1 647 PHE n 
1 648 LYS n 
1 649 CYS n 
1 650 GLY n 
1 651 ILE n 
1 652 ALA n 
1 653 VAL n 
1 654 ALA n 
1 655 PRO n 
1 656 VAL n 
1 657 SER n 
1 658 ARG n 
1 659 TRP n 
1 660 GLU n 
1 661 TYR n 
1 662 TYR n 
1 663 ASP n 
1 664 SER n 
1 665 VAL n 
1 666 TYR n 
1 667 THR n 
1 668 GLU n 
1 669 ARG n 
1 670 TYR n 
1 671 MET n 
1 672 GLY n 
1 673 LEU n 
1 674 PRO n 
1 675 THR n 
1 676 PRO n 
1 677 GLU n 
1 678 ASP n 
1 679 ASN n 
1 680 LEU n 
1 681 ASP n 
1 682 HIS n 
1 683 TYR n 
1 684 ARG n 
1 685 ASN n 
1 686 SER n 
1 687 THR n 
1 688 VAL n 
1 689 MET n 
1 690 SER n 
1 691 ARG n 
1 692 ALA n 
1 693 GLU n 
1 694 ASN n 
1 695 PHE n 
1 696 LYS n 
1 697 GLN n 
1 698 VAL n 
1 699 GLU n 
1 700 TYR n 
1 701 LEU n 
1 702 LEU n 
1 703 ILE n 
1 704 HIS n 
1 705 GLY n 
1 706 THR n 
1 707 ALA n 
1 708 ASP n 
1 709 ASP n 
1 710 ASN n 
1 711 VAL n 
1 712 HIS n 
1 713 PHE n 
1 714 GLN n 
1 715 GLN n 
1 716 SER n 
1 717 ALA n 
1 718 GLN n 
1 719 ILE n 
1 720 SER n 
1 721 LYS n 
1 722 ALA n 
1 723 LEU n 
1 724 VAL n 
1 725 ASP n 
1 726 VAL n 
1 727 GLY n 
1 728 VAL n 
1 729 ASP n 
1 730 PHE n 
1 731 GLN n 
1 732 ALA n 
1 733 MET n 
1 734 TRP n 
1 735 TYR n 
1 736 THR n 
1 737 ASP n 
1 738 GLU n 
1 739 ASP n 
1 740 HIS n 
1 741 GLY n 
1 742 ILE n 
1 743 ALA n 
1 744 SER n 
1 745 SER n 
1 746 THR n 
1 747 ALA n 
1 748 HIS n 
1 749 GLN n 
1 750 HIS n 
1 751 ILE n 
1 752 TYR n 
1 753 THR n 
1 754 HIS n 
1 755 MET n 
1 756 SER n 
1 757 HIS n 
1 758 PHE n 
1 759 ILE n 
1 760 LYS n 
1 761 GLN n 
1 762 CYS n 
1 763 PHE n 
1 764 SER n 
1 765 LEU n 
1 766 PRO 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 'DPP4, ADCP2, CD26' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     Spodoptera 
_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               HI5 
_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          Baculovirus 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PBLUEBAC4.5 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DPP4_HUMAN 
_struct_ref.pdbx_db_accession          P27487 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFN
AEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPV
GHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF
YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQ
NYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKG
TWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY
TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFR
LNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVL
GSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS
KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2QT9 A 1 ? 766 ? P27487 1 ? 766 ? 1 766 
2 1 2QT9 B 1 ? 766 ? P27487 1 ? 766 ? 1 766 
# 
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 2QT9 THR A 39 ? UNP P27487 SER 39 ENGINEERED 39 1 
2 2QT9 THR B 39 ? UNP P27487 SER 39 ENGINEERED 39 2 
# 
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 
524 non-polymer         . 
;(2S,3S)-3-AMINO-4-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-5-YLCYCLOHEXYL)BUTANAMIDE
;
;5-(4-{(1S,2S)-2-AMMONIO-1-[(DIMETHYLAMINO)CARBONYL]-3-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-3-OXOPROPYL}CYCLOHEXYL)[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-1-IUM
;
'C22 H31 F N6 O2' 430.519 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
NA  non-polymer         . 'SODIUM ION' ? 'Na 1'            22.990  
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'     221.208 
NDG D-saccharide        . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? 'C8 H15 N O6'     221.208 
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 
# 
_exptl.crystals_number   1 
_exptl.entry_id          2QT9 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.87 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   57.21 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              8.000000 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    
'PEG4000, Sodium Acetate, TRIS, pH 8.0, vapor diffusion, hanging drop, temperature 293K, pH 8.000000, VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.000000 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   ADSC 
_diffrn_detector.pdbx_collection_date   2003-11-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_wavelength             1.0 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.entry_id                     2QT9 
_reflns.d_resolution_high            2.100 
_reflns.d_resolution_low             30.000 
_reflns.number_obs                   119087 
_reflns.pdbx_Rmerge_I_obs            0.104 
_reflns.pdbx_netI_over_sigmaI        6.600 
_reflns.pdbx_redundancy              7.200 
_reflns.percent_possible_obs         99.900 
_reflns.B_iso_Wilson_estimate        25.100 
_reflns.observed_criterion_sigma_I   0.00 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.10 
_reflns_shell.d_res_low              2.18 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.442 
_reflns_shell.meanI_over_sigI_obs    1.7 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        7.30 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.percent_possible_all   99.80 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2QT9 
_refine.ls_d_res_high                            2.100 
_refine.ls_d_res_low                             30.000 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    99.900 
_refine.ls_number_reflns_obs                     118967 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.ls_R_factor_R_work                       0.190 
_refine.ls_R_factor_R_free                       0.229 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  6004 
_refine.B_iso_mean                               25.300 
_refine.solvent_model_param_bsol                 40.100 
_refine.solvent_model_param_ksol                 0.360 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.aniso_B[1][1]                            5.562 
_refine.aniso_B[2][2]                            -3.148 
_refine.aniso_B[3][3]                            -2.414 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.solvent_model_details                    MASK 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      1X70 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2QT9 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             0.170 
_refine_analyze.Luzzati_d_res_low_obs           5.000 
_refine_analyze.Luzzati_coordinate_error_free   0.280 
_refine_analyze.Luzzati_sigma_a_free            0.210 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11930 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         399 
_refine_hist.number_atoms_solvent             1304 
_refine_hist.number_atoms_total               13633 
_refine_hist.d_res_high                       2.100 
_refine_hist.d_res_low                        30.000 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d           ? 0.010  ?     ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        ? 1.480  ?     ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d ? 24.800 ?     ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d ? 0.861  ?     ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it        ? 0.920  1.500 ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it       ? 1.410  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scbond_it        ? 1.440  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scangle_it       ? 2.100  2.500 ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.180 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.percent_reflns_obs               99.600 
_refine_ls_shell.number_reflns_R_work             11123 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.217 
_refine_ls_shell.R_factor_R_free                  0.255 
_refine_ls_shell.percent_reflns_R_free            5.000 
_refine_ls_shell.number_reflns_R_free             598 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                11721 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PROTEIN_REP.PARAM  ? 'X-RAY DIFFRACTION' 
2 WATER_REP.PARAM    ? 'X-RAY DIFFRACTION' 
3 ION.PARAM          ? 'X-RAY DIFFRACTION' 
4 CARBOHYDRATE.PARAM ? 'X-RAY DIFFRACTION' 
5 ?                  ? 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2QT9 
_struct.title                     'Human dipeptidyl peptidase iv/cd26 in complex with a 4-aryl cyclohexylalanine inhibitor' 
_struct.pdbx_descriptor           'Dipeptidyl peptidase 4 (EC 3.4.14.5)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2QT9 
_struct_keywords.text            
;ALPHA/BETA, BETA-PROPELLER, DIMER, Aminopeptidase, Glycoprotein, Hydrolase, Membrane, Protease, Secreted, Serine protease, Signal-anchor, Transmembrane
;
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 2 ? 
D  N N 2 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 2 ? 
I  N N 2 ? 
J  N N 2 ? 
K  N N 4 ? 
L  N N 2 ? 
M  N N 5 ? 
N  N N 5 ? 
O  N N 2 ? 
P  N N 2 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 5 ? 
T  N N 5 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 2 ? 
Y  N N 2 ? 
Z  N N 2 ? 
AA N N 2 ? 
BA N N 2 ? 
CA N N 2 ? 
DA N N 6 ? 
EA N N 6 ? 
FA N N 6 ? 
GA N N 6 ? 
HA N N 6 ? 
IA N N 6 ? 
JA N N 6 ? 
KA N N 6 ? 
LA N N 6 ? 
# 
_struct_biol.id   1 
# 
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  1  THR A 44  ? ASN A 51  ? THR A 44  ASN A 51  1 ? 8  
HELX_P HELX_P2  2  ASP A 200 ? GLU A 206 ? ASP A 200 GLU A 206 1 ? 7  
HELX_P HELX_P3  3  ASP A 274 ? LEU A 276 ? ASP A 274 LEU A 276 5 ? 3  
HELX_P HELX_P4  4  PRO A 290 ? ILE A 295 ? PRO A 290 ILE A 295 1 ? 6  
HELX_P HELX_P5  5  VAL A 341 ? GLN A 344 ? VAL A 341 GLN A 344 5 ? 4  
HELX_P HELX_P6  6  GLU A 421 ? MET A 425 ? GLU A 421 MET A 425 5 ? 5  
HELX_P HELX_P7  7  ASN A 497 ? GLN A 505 ? ASN A 497 GLN A 505 1 ? 9  
HELX_P HELX_P8  8  ASN A 562 ? THR A 570 ? ASN A 562 THR A 570 1 ? 9  
HELX_P HELX_P9  9  GLY A 587 ? HIS A 592 ? GLY A 587 HIS A 592 1 ? 6  
HELX_P HELX_P10 10 ALA A 593 ? ASN A 595 ? ALA A 593 ASN A 595 5 ? 3  
HELX_P HELX_P11 11 THR A 600 ? SER A 614 ? THR A 600 SER A 614 1 ? 15 
HELX_P HELX_P12 12 SER A 630 ? GLY A 641 ? SER A 630 GLY A 641 1 ? 12 
HELX_P HELX_P13 13 ARG A 658 ? TYR A 662 ? ARG A 658 TYR A 662 5 ? 5  
HELX_P HELX_P14 14 ASP A 663 ? GLY A 672 ? ASP A 663 GLY A 672 1 ? 10 
HELX_P HELX_P15 15 ASN A 679 ? SER A 686 ? ASN A 679 SER A 686 1 ? 8  
HELX_P HELX_P16 16 VAL A 688 ? VAL A 698 ? VAL A 688 VAL A 698 5 ? 11 
HELX_P HELX_P17 17 HIS A 712 ? VAL A 726 ? HIS A 712 VAL A 726 1 ? 15 
HELX_P HELX_P18 18 SER A 744 ? SER A 764 ? SER A 744 SER A 764 1 ? 21 
HELX_P HELX_P19 19 THR B 44  ? ASN B 51  ? THR B 44  ASN B 51  1 ? 8  
HELX_P HELX_P20 20 ASP B 200 ? GLU B 206 ? ASP B 200 GLU B 206 1 ? 7  
HELX_P HELX_P21 21 ASP B 274 ? LEU B 276 ? ASP B 274 LEU B 276 5 ? 3  
HELX_P HELX_P22 22 PRO B 290 ? ILE B 295 ? PRO B 290 ILE B 295 1 ? 6  
HELX_P HELX_P23 23 VAL B 341 ? GLN B 344 ? VAL B 341 GLN B 344 5 ? 4  
HELX_P HELX_P24 24 GLU B 421 ? MET B 425 ? GLU B 421 MET B 425 5 ? 5  
HELX_P HELX_P25 25 ASN B 497 ? GLN B 505 ? ASN B 497 GLN B 505 1 ? 9  
HELX_P HELX_P26 26 ASN B 562 ? THR B 570 ? ASN B 562 THR B 570 1 ? 9  
HELX_P HELX_P27 27 GLY B 587 ? HIS B 592 ? GLY B 587 HIS B 592 1 ? 6  
HELX_P HELX_P28 28 ALA B 593 ? ASN B 595 ? ALA B 593 ASN B 595 5 ? 3  
HELX_P HELX_P29 29 THR B 600 ? LYS B 615 ? THR B 600 LYS B 615 1 ? 16 
HELX_P HELX_P30 30 SER B 630 ? GLY B 641 ? SER B 630 GLY B 641 1 ? 12 
HELX_P HELX_P31 31 ARG B 658 ? TYR B 662 ? ARG B 658 TYR B 662 5 ? 5  
HELX_P HELX_P32 32 ASP B 663 ? GLY B 672 ? ASP B 663 GLY B 672 1 ? 10 
HELX_P HELX_P33 33 ASN B 679 ? SER B 686 ? ASN B 679 SER B 686 1 ? 8  
HELX_P HELX_P34 34 VAL B 688 ? VAL B 698 ? VAL B 688 VAL B 698 5 ? 11 
HELX_P HELX_P35 35 HIS B 712 ? VAL B 726 ? HIS B 712 VAL B 726 1 ? 15 
HELX_P HELX_P36 36 SER B 744 ? PHE B 763 ? SER B 744 PHE B 763 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 328 SG  ? ? ? 1_555 A  CYS 339 SG ? ? A CYS 328  A CYS 339  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf2  disulf ? ? A  CYS 385 SG  ? ? ? 1_555 A  CYS 394 SG ? ? A CYS 385  A CYS 394  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf3  disulf ? ? A  CYS 444 SG  ? ? ? 1_555 A  CYS 447 SG ? ? A CYS 444  A CYS 447  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf4  disulf ? ? A  CYS 454 SG  ? ? ? 1_555 A  CYS 472 SG ? ? A CYS 454  A CYS 472  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf5  disulf ? ? A  CYS 649 SG  ? ? ? 1_555 A  CYS 762 SG ? ? A CYS 649  A CYS 762  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf6  disulf ? ? B  CYS 328 SG  ? ? ? 1_555 B  CYS 339 SG ? ? B CYS 328  B CYS 339  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf7  disulf ? ? B  CYS 385 SG  ? ? ? 1_555 B  CYS 394 SG ? ? B CYS 385  B CYS 394  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf8  disulf ? ? B  CYS 444 SG  ? ? ? 1_555 B  CYS 447 SG ? ? B CYS 444  B CYS 447  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf9  disulf ? ? B  CYS 454 SG  ? ? ? 1_555 B  CYS 472 SG ? ? B CYS 454  B CYS 472  1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf10 disulf ? ? B  CYS 649 SG  ? ? ? 1_555 B  CYS 762 SG ? ? B CYS 649  B CYS 762  1_555 ? ? ? ? ? ? ? 2.053 ? 
covale1  covale ? ? A  ASN 85  ND2 ? ? ? 1_555 L  NAG .   C1 ? ? A ASN 85   L NAG 1085 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale2  covale ? ? A  ASN 92  ND2 ? ? ? 1_555 C  NAG .   C1 ? ? A ASN 92   A NAG 1092 1_555 ? ? ? ? ? ? ? 1.458 ? 
covale3  covale ? ? A  ASN 150 ND2 ? ? ? 1_555 N  NDG .   C1 ? ? A ASN 150  M NDG 1150 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale4  covale ? ? A  ASN 219 ND2 ? ? ? 1_555 P  NAG .   C1 ? ? A ASN 219  N NAG 1219 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale5  covale ? ? A  ASN 229 ND2 ? ? ? 1_555 R  NAG .   C1 ? ? A ASN 229  O NAG 1229 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale6  covale ? ? A  ASN 281 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 281  A NAG 1281 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale7  covale ? ? A  ASN 321 ND2 ? ? ? 1_555 T  NDG .   C1 ? ? A ASN 321  P NDG 1321 1_555 ? ? ? ? ? ? ? 1.460 ? 
metalc1  metalc ? ? A  GLY 490 O   ? ? ? 1_555 F  NA  .   NA ? ? A GLY 490  A NA  1521 1_555 ? ? ? ? ? ? ? 2.434 ? 
metalc2  metalc ? ? A  LEU 491 O   ? ? ? 1_555 F  NA  .   NA ? ? A LEU 491  A NA  1521 1_555 ? ? ? ? ? ? ? 2.442 ? 
covale8  covale ? ? A  ASN 520 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 520  A NAG 1520 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale9  covale ? ? B  ASN 85  ND2 ? ? ? 1_555 V  NAG .   C1 ? ? B ASN 85   Q NAG 2085 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale10 covale ? ? B  ASN 92  ND2 ? ? ? 1_555 H  NAG .   C1 ? ? B ASN 92   B NAG 2092 1_555 ? ? ? ? ? ? ? 1.453 ? 
covale11 covale ? ? B  ASN 150 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? B ASN 150  B NAG 2150 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale12 covale ? ? B  ASN 219 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? B ASN 219  R NAG 2219 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale13 covale ? ? B  ASN 229 ND2 ? ? ? 1_555 Z  NAG .   C1 ? ? B ASN 229  S NAG 2229 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale14 covale ? ? B  ASN 281 ND2 ? ? ? 1_555 BA NAG .   C1 ? ? B ASN 281  T NAG 2281 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale15 covale ? ? B  ASN 321 ND2 ? ? ? 1_555 J  NAG .   C1 ? ? B ASN 321  B NAG 2321 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale16 covale ? ? L  NAG .   O4  ? ? ? 1_555 M  NDG .   C1 ? ? L NAG 1085 L NDG 1086 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale17 covale ? ? N  NDG .   O4  ? ? ? 1_555 O  NAG .   C1 ? ? M NDG 1150 M NAG 1151 1_555 ? ? ? ? ? ? ? 1.392 ? 
covale18 covale ? ? P  NAG .   O4  ? ? ? 1_555 Q  NAG .   C1 ? ? N NAG 1219 N NAG 1220 1_555 ? ? ? ? ? ? ? 1.389 ? 
covale19 covale ? ? R  NAG .   O4  ? ? ? 1_555 S  NDG .   C1 ? ? O NAG 1229 O NDG 1230 1_555 ? ? ? ? ? ? ? 1.384 ? 
covale20 covale ? ? T  NDG .   O4  ? ? ? 1_555 U  NAG .   C1 ? ? P NDG 1321 P NAG 1322 1_555 ? ? ? ? ? ? ? 1.395 ? 
covale21 covale ? ? V  NAG .   O4  ? ? ? 1_555 W  NAG .   C1 ? ? Q NAG 2085 Q NAG 2086 1_555 ? ? ? ? ? ? ? 1.391 ? 
covale22 covale ? ? X  NAG .   O4  ? ? ? 1_555 Y  NAG .   C1 ? ? R NAG 2219 R NAG 2220 1_555 ? ? ? ? ? ? ? 1.386 ? 
covale23 covale ? ? Z  NAG .   O4  ? ? ? 1_555 AA NAG .   C1 ? ? S NAG 2229 S NAG 2230 1_555 ? ? ? ? ? ? ? 1.386 ? 
covale24 covale ? ? BA NAG .   O4  ? ? ? 1_555 CA NAG .   C1 ? ? T NAG 2281 T NAG 2282 1_555 ? ? ? ? ? ? ? 1.379 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 474 A . ? GLY 474 A PRO 475 A ? PRO 475 A 1 1.75 
2 GLY 474 B . ? GLY 474 B PRO 475 B ? PRO 475 B 1 0.29 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 4 ? 
C ? 4 ? 
D ? 4 ? 
E ? 3 ? 
F ? 4 ? 
G ? 2 ? 
H ? 4 ? 
I ? 4 ? 
J ? 4 ? 
K ? 4 ? 
L ? 4 ? 
M ? 8 ? 
N ? 2 ? 
O ? 4 ? 
P ? 4 ? 
Q ? 4 ? 
R ? 3 ? 
S ? 4 ? 
T ? 2 ? 
U ? 4 ? 
V ? 4 ? 
W ? 4 ? 
X ? 4 ? 
Y ? 4 ? 
Z ? 8 ? 
# 
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 
A 1 2 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? parallel      
M 4 5 ? parallel      
M 5 6 ? parallel      
M 6 7 ? parallel      
M 7 8 ? parallel      
N 1 2 ? parallel      
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
S 1 2 ? anti-parallel 
S 2 3 ? anti-parallel 
S 3 4 ? anti-parallel 
T 1 2 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? anti-parallel 
U 3 4 ? anti-parallel 
V 1 2 ? anti-parallel 
V 2 3 ? anti-parallel 
V 3 4 ? anti-parallel 
W 1 2 ? anti-parallel 
W 2 3 ? anti-parallel 
W 3 4 ? anti-parallel 
X 1 2 ? anti-parallel 
X 2 3 ? anti-parallel 
X 3 4 ? anti-parallel 
Y 1 2 ? anti-parallel 
Y 2 3 ? anti-parallel 
Y 3 4 ? anti-parallel 
Z 1 2 ? anti-parallel 
Z 2 3 ? anti-parallel 
Z 3 4 ? parallel      
Z 4 5 ? parallel      
Z 5 6 ? parallel      
Z 6 7 ? parallel      
Z 7 8 ? 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 
A 1 LYS A 41  ? THR A 42  ? LYS A 41  THR A 42  
A 2 VAL A 507 ? GLN A 508 ? VAL A 507 GLN A 508 
B 1 LEU A 60  ? TRP A 62  ? LEU A 60  TRP A 62  
B 2 GLU A 67  ? GLN A 72  ? GLU A 67  GLN A 72  
B 3 ASN A 75  ? ASN A 80  ? ASN A 75  ASN A 80  
B 4 SER A 86  ? LEU A 90  ? SER A 86  LEU A 90  
C 1 ILE A 102 ? ILE A 107 ? ILE A 102 ILE A 107 
C 2 PHE A 113 ? LYS A 122 ? PHE A 113 LYS A 122 
C 3 TYR A 128 ? ASP A 136 ? TYR A 128 ASP A 136 
C 4 GLN A 141 ? LEU A 142 ? GLN A 141 LEU A 142 
D 1 TRP A 154 ? TRP A 157 ? TRP A 154 TRP A 157 
D 2 LEU A 164 ? TRP A 168 ? LEU A 164 TRP A 168 
D 3 ASP A 171 ? LYS A 175 ? ASP A 171 LYS A 175 
D 4 TYR A 183 ? ARG A 184 ? TYR A 183 ARG A 184 
E 1 ILE A 194 ? ASN A 196 ? ILE A 194 ASN A 196 
E 2 PHE A 222 ? ASN A 229 ? PHE A 222 ASN A 229 
E 3 LEU A 214 ? TRP A 216 ? LEU A 214 TRP A 216 
F 1 ILE A 194 ? ASN A 196 ? ILE A 194 ASN A 196 
F 2 PHE A 222 ? ASN A 229 ? PHE A 222 ASN A 229 
F 3 THR A 265 ? ASN A 272 ? THR A 265 ASN A 272 
F 4 SER A 284 ? GLN A 286 ? SER A 284 GLN A 286 
G 1 LEU A 235 ? PHE A 240 ? LEU A 235 PHE A 240 
G 2 LYS A 250 ? PRO A 255 ? LYS A 250 PRO A 255 
H 1 HIS A 298 ? THR A 307 ? HIS A 298 THR A 307 
H 2 ARG A 310 ? ARG A 317 ? ARG A 310 ARG A 317 
H 3 TYR A 322 ? ASP A 331 ? TYR A 322 ASP A 331 
H 4 ARG A 336 ? CYS A 339 ? ARG A 336 CYS A 339 
I 1 HIS A 298 ? THR A 307 ? HIS A 298 THR A 307 
I 2 ARG A 310 ? ARG A 317 ? ARG A 310 ARG A 317 
I 3 TYR A 322 ? ASP A 331 ? TYR A 322 ASP A 331 
I 4 HIS A 345 ? MET A 348 ? HIS A 345 MET A 348 
J 1 HIS A 363 ? PHE A 364 ? HIS A 363 PHE A 364 
J 2 SER A 370 ? SER A 376 ? SER A 370 SER A 376 
J 3 ARG A 382 ? GLN A 388 ? ARG A 382 GLN A 388 
J 4 THR A 395 ? PHE A 396 ? THR A 395 PHE A 396 
K 1 VAL A 404 ? LEU A 410 ? VAL A 404 LEU A 410 
K 2 TYR A 414 ? SER A 419 ? TYR A 414 SER A 419 
K 3 ASN A 430 ? GLN A 435 ? ASN A 430 GLN A 435 
K 4 VAL A 442 ? CYS A 444 ? VAL A 442 CYS A 444 
L 1 TYR A 457 ? PHE A 461 ? TYR A 457 PHE A 461 
L 2 TYR A 467 ? CYS A 472 ? TYR A 467 CYS A 472 
L 3 LEU A 479 ? SER A 484 ? LEU A 479 SER A 484 
L 4 LYS A 489 ? GLU A 495 ? LYS A 489 GLU A 495 
M 1 SER A 511 ? LEU A 519 ? SER A 511 LEU A 519 
M 2 THR A 522 ? LEU A 530 ? THR A 522 LEU A 530 
M 3 ILE A 574 ? PHE A 578 ? ILE A 574 PHE A 578 
M 4 TYR A 540 ? VAL A 546 ? TYR A 540 VAL A 546 
M 5 VAL A 619 ? TRP A 629 ? VAL A 619 TRP A 629 
M 6 CYS A 649 ? VAL A 653 ? CYS A 649 VAL A 653 
M 7 GLU A 699 ? GLY A 705 ? GLU A 699 GLY A 705 
M 8 GLN A 731 ? TYR A 735 ? GLN A 731 TYR A 735 
N 1 LYS B 41  ? THR B 42  ? LYS B 41  THR B 42  
N 2 VAL B 507 ? GLN B 508 ? VAL B 507 GLN B 508 
O 1 ARG B 61  ? TRP B 62  ? ARG B 61  TRP B 62  
O 2 GLU B 67  ? GLN B 72  ? GLU B 67  GLN B 72  
O 3 ASN B 75  ? ASN B 80  ? ASN B 75  ASN B 80  
O 4 SER B 86  ? LEU B 90  ? SER B 86  LEU B 90  
P 1 ASP B 104 ? ILE B 107 ? ASP B 104 ILE B 107 
P 2 PHE B 113 ? LYS B 122 ? PHE B 113 LYS B 122 
P 3 TYR B 128 ? ASP B 136 ? TYR B 128 ASP B 136 
P 4 GLN B 141 ? LEU B 142 ? GLN B 141 LEU B 142 
Q 1 TRP B 154 ? TRP B 157 ? TRP B 154 TRP B 157 
Q 2 LEU B 164 ? TRP B 168 ? LEU B 164 TRP B 168 
Q 3 ASP B 171 ? LYS B 175 ? ASP B 171 LYS B 175 
Q 4 TYR B 183 ? ARG B 184 ? TYR B 183 ARG B 184 
R 1 ILE B 194 ? ASN B 196 ? ILE B 194 ASN B 196 
R 2 PHE B 222 ? ASN B 229 ? PHE B 222 ASN B 229 
R 3 LEU B 214 ? TRP B 216 ? LEU B 214 TRP B 216 
S 1 ILE B 194 ? ASN B 196 ? ILE B 194 ASN B 196 
S 2 PHE B 222 ? ASN B 229 ? PHE B 222 ASN B 229 
S 3 THR B 265 ? ASN B 272 ? THR B 265 ASN B 272 
S 4 ILE B 285 ? GLN B 286 ? ILE B 285 GLN B 286 
T 1 LEU B 235 ? PHE B 240 ? LEU B 235 PHE B 240 
T 2 LYS B 250 ? PRO B 255 ? LYS B 250 PRO B 255 
U 1 HIS B 298 ? THR B 307 ? HIS B 298 THR B 307 
U 2 ARG B 310 ? ARG B 317 ? ARG B 310 ARG B 317 
U 3 TYR B 322 ? TYR B 330 ? TYR B 322 TYR B 330 
U 4 TRP B 337 ? CYS B 339 ? TRP B 337 CYS B 339 
V 1 HIS B 298 ? THR B 307 ? HIS B 298 THR B 307 
V 2 ARG B 310 ? ARG B 317 ? ARG B 310 ARG B 317 
V 3 TYR B 322 ? TYR B 330 ? TYR B 322 TYR B 330 
V 4 HIS B 345 ? MET B 348 ? HIS B 345 MET B 348 
W 1 HIS B 363 ? PHE B 364 ? HIS B 363 PHE B 364 
W 2 SER B 370 ? SER B 376 ? SER B 370 SER B 376 
W 3 ARG B 382 ? GLN B 388 ? ARG B 382 GLN B 388 
W 4 THR B 395 ? PHE B 396 ? THR B 395 PHE B 396 
X 1 VAL B 404 ? LEU B 410 ? VAL B 404 LEU B 410 
X 2 TYR B 414 ? SER B 419 ? TYR B 414 SER B 419 
X 3 ASN B 430 ? GLN B 435 ? ASN B 430 GLN B 435 
X 4 VAL B 442 ? CYS B 444 ? VAL B 442 CYS B 444 
Y 1 TYR B 457 ? PHE B 461 ? TYR B 457 PHE B 461 
Y 2 TYR B 467 ? CYS B 472 ? TYR B 467 CYS B 472 
Y 3 LEU B 479 ? SER B 484 ? LEU B 479 SER B 484 
Y 4 LYS B 489 ? GLU B 495 ? LYS B 489 GLU B 495 
Z 1 SER B 511 ? LEU B 519 ? SER B 511 LEU B 519 
Z 2 THR B 522 ? LEU B 530 ? THR B 522 LEU B 530 
Z 3 ILE B 574 ? PHE B 578 ? ILE B 574 PHE B 578 
Z 4 TYR B 540 ? VAL B 546 ? TYR B 540 VAL B 546 
Z 5 VAL B 619 ? TRP B 629 ? VAL B 619 TRP B 629 
Z 6 CYS B 649 ? VAL B 653 ? CYS B 649 VAL B 653 
Z 7 GLU B 699 ? GLY B 705 ? GLU B 699 GLY B 705 
Z 8 GLN B 731 ? TYR B 735 ? GLN B 731 TYR B 735 
# 
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 
A 1 2 N LYS A 41  ? N LYS A 41  O GLN A 508 ? O GLN A 508 
B 1 2 N ARG A 61  ? N ARG A 61  O LEU A 69  ? O LEU A 69  
B 2 3 N GLN A 72  ? N GLN A 72  O ASN A 75  ? O ASN A 75  
B 3 4 N ILE A 76  ? N ILE A 76  O PHE A 89  ? O PHE A 89  
C 1 2 N SER A 106 ? N SER A 106 O LEU A 115 ? O LEU A 115 
C 2 3 N LEU A 116 ? N LEU A 116 O ASP A 133 ? O ASP A 133 
C 3 4 N ASP A 136 ? N ASP A 136 O GLN A 141 ? O GLN A 141 
D 1 2 N TRP A 154 ? N TRP A 154 O VAL A 167 ? O VAL A 167 
D 2 3 N LEU A 164 ? N LEU A 164 O LYS A 175 ? O LYS A 175 
D 3 4 N VAL A 174 ? N VAL A 174 O TYR A 183 ? O TYR A 183 
E 1 2 N TYR A 195 ? N TYR A 195 O PHE A 228 ? O PHE A 228 
E 2 3 O ALA A 224 ? O ALA A 224 N TRP A 215 ? N TRP A 215 
F 1 2 N TYR A 195 ? N TYR A 195 O PHE A 228 ? O PHE A 228 
F 2 3 N TYR A 225 ? N TYR A 225 O PHE A 269 ? O PHE A 269 
F 3 4 N VAL A 270 ? N VAL A 270 O ILE A 285 ? O ILE A 285 
G 1 2 N PHE A 240 ? N PHE A 240 O LYS A 250 ? O LYS A 250 
H 1 2 N ALA A 306 ? N ALA A 306 O ARG A 310 ? O ARG A 310 
H 2 3 N ILE A 311 ? N ILE A 311 O CYS A 328 ? O CYS A 328 
H 3 4 N ASP A 331 ? N ASP A 331 O ARG A 336 ? O ARG A 336 
I 1 2 N ALA A 306 ? N ALA A 306 O ARG A 310 ? O ARG A 310 
I 2 3 N ILE A 311 ? N ILE A 311 O CYS A 328 ? O CYS A 328 
I 3 4 N MET A 325 ? N MET A 325 O HIS A 345 ? O HIS A 345 
J 1 2 N HIS A 363 ? N HIS A 363 O TYR A 372 ? O TYR A 372 
J 2 3 N PHE A 371 ? N PHE A 371 O PHE A 387 ? O PHE A 387 
J 3 4 N TYR A 386 ? N TYR A 386 O THR A 395 ? O THR A 395 
K 1 2 N ALA A 409 ? N ALA A 409 O TYR A 416 ? O TYR A 416 
K 2 3 N TYR A 417 ? N TYR A 417 O TYR A 432 ? O TYR A 432 
K 3 4 N LYS A 433 ? N LYS A 433 O THR A 443 ? O THR A 443 
L 1 2 N SER A 458 ? N SER A 458 O ARG A 471 ? O ARG A 471 
L 2 3 N CYS A 472 ? N CYS A 472 O LEU A 479 ? O LEU A 479 
L 3 4 N TYR A 480 ? N TYR A 480 O GLU A 495 ? O GLU A 495 
M 1 2 N LEU A 519 ? N LEU A 519 O THR A 522 ? O THR A 522 
M 2 3 N ILE A 529 ? N ILE A 529 O VAL A 575 ? O VAL A 575 
M 3 4 O ILE A 574 ? O ILE A 574 N LEU A 543 ? N LEU A 543 
M 4 5 N LEU A 542 ? N LEU A 542 O ALA A 625 ? O ALA A 625 
M 5 6 N GLY A 628 ? N GLY A 628 O VAL A 653 ? O VAL A 653 
M 6 7 N ALA A 652 ? N ALA A 652 O ILE A 703 ? O ILE A 703 
M 7 8 N TYR A 700 ? N TYR A 700 O GLN A 731 ? O GLN A 731 
N 1 2 N LYS B 41  ? N LYS B 41  O GLN B 508 ? O GLN B 508 
O 1 2 N ARG B 61  ? N ARG B 61  O LEU B 69  ? O LEU B 69  
O 2 3 N TYR B 70  ? N TYR B 70  O LEU B 77  ? O LEU B 77  
O 3 4 N ILE B 76  ? N ILE B 76  O PHE B 89  ? O PHE B 89  
P 1 2 N SER B 106 ? N SER B 106 O LEU B 115 ? O LEU B 115 
P 2 3 N TYR B 118 ? N TYR B 118 O SER B 131 ? O SER B 131 
P 3 4 N ASP B 136 ? N ASP B 136 O GLN B 141 ? O GLN B 141 
Q 1 2 N THR B 156 ? N THR B 156 O ALA B 165 ? O ALA B 165 
Q 2 3 N LEU B 164 ? N LEU B 164 O LYS B 175 ? O LYS B 175 
Q 3 4 N VAL B 174 ? N VAL B 174 O TYR B 183 ? O TYR B 183 
R 1 2 N TYR B 195 ? N TYR B 195 O PHE B 228 ? O PHE B 228 
R 2 3 O ALA B 224 ? O ALA B 224 N TRP B 215 ? N TRP B 215 
S 1 2 N TYR B 195 ? N TYR B 195 O PHE B 228 ? O PHE B 228 
S 2 3 N TYR B 225 ? N TYR B 225 O PHE B 269 ? O PHE B 269 
S 3 4 N VAL B 270 ? N VAL B 270 O ILE B 285 ? O ILE B 285 
T 1 2 N TYR B 238 ? N TYR B 238 O VAL B 252 ? O VAL B 252 
U 1 2 N ALA B 306 ? N ALA B 306 O ARG B 310 ? O ARG B 310 
U 2 3 N ILE B 311 ? N ILE B 311 O CYS B 328 ? O CYS B 328 
U 3 4 N ASP B 329 ? N ASP B 329 O ASN B 338 ? O ASN B 338 
V 1 2 N ALA B 306 ? N ALA B 306 O ARG B 310 ? O ARG B 310 
V 2 3 N ILE B 311 ? N ILE B 311 O CYS B 328 ? O CYS B 328 
V 3 4 N MET B 325 ? N MET B 325 O HIS B 345 ? O HIS B 345 
W 1 2 N HIS B 363 ? N HIS B 363 O TYR B 372 ? O TYR B 372 
W 2 3 N PHE B 371 ? N PHE B 371 O PHE B 387 ? O PHE B 387 
W 3 4 N TYR B 386 ? N TYR B 386 O THR B 395 ? O THR B 395 
X 1 2 N ILE B 405 ? N ILE B 405 O ILE B 418 ? O ILE B 418 
X 2 3 N TYR B 417 ? N TYR B 417 O TYR B 432 ? O TYR B 432 
X 3 4 N LYS B 433 ? N LYS B 433 O THR B 443 ? O THR B 443 
Y 1 2 N SER B 458 ? N SER B 458 O ARG B 471 ? O ARG B 471 
Y 2 3 N LEU B 470 ? N LEU B 470 O THR B 481 ? O THR B 481 
Y 3 4 N TYR B 480 ? N TYR B 480 O LEU B 494 ? O LEU B 494 
Z 1 2 N SER B 511 ? N SER B 511 O LEU B 530 ? O LEU B 530 
Z 2 3 N ILE B 529 ? N ILE B 529 O VAL B 575 ? O VAL B 575 
Z 3 4 O ALA B 576 ? O ALA B 576 N ASP B 545 ? N ASP B 545 
Z 4 5 N LEU B 542 ? N LEU B 542 O ALA B 625 ? O ALA B 625 
Z 5 6 N GLY B 628 ? N GLY B 628 O VAL B 653 ? O VAL B 653 
Z 6 7 N ALA B 652 ? N ALA B 652 O LEU B 701 ? O LEU B 701 
Z 7 8 N TYR B 700 ? N TYR B 700 O GLN B 731 ? O GLN B 731 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG L 1085' 
AC2 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NDG L 1086' 
AC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 1092' 
AC4 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NDG M 1150' 
AC5 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG M 1151' 
AC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG N 1219' 
AC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG N 1220' 
AC8 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE NAG O 1229' 
AC9 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NDG O 1230' 
BC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 1281' 
BC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NDG P 1321' 
BC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG P 1322' 
BC4 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 1520' 
BC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG Q 2085' 
BC6 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG Q 2086' 
BC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 2092' 
BC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 2150' 
BC9 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE NAG R 2219' 
CC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG R 2220' 
CC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG S 2229' 
CC3 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG S 2230' 
CC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG T 2281' 
CC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG T 2282' 
CC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 2321' 
CC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NA A 1521'  
CC8 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE 524 A 1522' 
CC9 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE 524 B 2322' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 7  GLU A  67  ? GLU A 67   . ? 1_555 ? 
2   AC1 7  VAL A  78  ? VAL A 78   . ? 1_555 ? 
3   AC1 7  ASN A  85  ? ASN A 85   . ? 1_555 ? 
4   AC1 7  SER A  86  ? SER A 86   . ? 1_555 ? 
5   AC1 7  SER A  87  ? SER A 87   . ? 1_555 ? 
6   AC1 7  HOH DA .   ? HOH A 1871 . ? 1_555 ? 
7   AC1 7  NDG M  .   ? NDG L 1086 . ? 1_555 ? 
8   AC2 1  NAG L  .   ? NAG L 1085 . ? 1_555 ? 
9   AC3 4  GLU A  73  ? GLU A 73   . ? 1_555 ? 
10  AC3 4  ASN A  74  ? ASN A 74   . ? 1_555 ? 
11  AC3 4  ASN A  75  ? ASN A 75   . ? 1_555 ? 
12  AC3 4  ASN A  92  ? ASN A 92   . ? 1_555 ? 
13  AC4 3  PRO A  149 ? PRO A 149  . ? 1_555 ? 
14  AC4 3  ASN A  150 ? ASN A 150  . ? 1_555 ? 
15  AC4 3  NAG O  .   ? NAG M 1151 . ? 1_555 ? 
16  AC5 2  ARG A  147 ? ARG A 147  . ? 1_555 ? 
17  AC5 2  NDG N  .   ? NDG M 1150 . ? 1_555 ? 
18  AC6 5  ASN A  219 ? ASN A 219  . ? 1_555 ? 
19  AC6 5  THR A  221 ? THR A 221  . ? 1_555 ? 
20  AC6 5  GLN A  308 ? GLN A 308  . ? 1_555 ? 
21  AC6 5  GLU A  309 ? GLU A 309  . ? 1_555 ? 
22  AC6 5  NAG Q  .   ? NAG N 1220 . ? 1_555 ? 
23  AC7 6  PHE A  222 ? PHE A 222  . ? 1_555 ? 
24  AC7 6  ASN A  272 ? ASN A 272  . ? 1_555 ? 
25  AC7 6  TYR A  330 ? TYR A 330  . ? 1_555 ? 
26  AC7 6  GLU A  332 ? GLU A 332  . ? 1_555 ? 
27  AC7 6  NAG P  .   ? NAG N 1219 . ? 1_555 ? 
28  AC7 6  HOH GA .   ? HOH N 2285 . ? 1_555 ? 
29  AC8 9  ILE A  194 ? ILE A 194  . ? 1_555 ? 
30  AC8 9  ASN A  229 ? ASN A 229  . ? 1_555 ? 
31  AC8 9  THR A  231 ? THR A 231  . ? 1_555 ? 
32  AC8 9  GLU A  232 ? GLU A 232  . ? 1_555 ? 
33  AC8 9  HOH DA .   ? HOH A 1553 . ? 1_555 ? 
34  AC8 9  HOH DA .   ? HOH A 1949 . ? 1_555 ? 
35  AC8 9  NDG S  .   ? NDG O 1230 . ? 1_555 ? 
36  AC8 9  HOH HA .   ? HOH O 2294 . ? 1_555 ? 
37  AC8 9  HOH HA .   ? HOH O 2297 . ? 1_555 ? 
38  AC9 1  NAG R  .   ? NAG O 1229 . ? 1_555 ? 
39  BC1 2  VAL A  279 ? VAL A 279  . ? 1_555 ? 
40  BC1 2  ASN A  281 ? ASN A 281  . ? 1_555 ? 
41  BC2 6  ASN A  321 ? ASN A 321  . ? 1_555 ? 
42  BC2 6  MET A  348 ? MET A 348  . ? 1_555 ? 
43  BC2 6  SER A  349 ? SER A 349  . ? 1_555 ? 
44  BC2 6  THR A  350 ? THR A 350  . ? 1_555 ? 
45  BC2 6  ARG A  596 ? ARG A 596  . ? 1_555 ? 
46  BC2 6  NAG U  .   ? NAG P 1322 . ? 1_555 ? 
47  BC3 3  ARG A  596 ? ARG A 596  . ? 1_555 ? 
48  BC3 3  ASP A  678 ? ASP A 678  . ? 1_555 ? 
49  BC3 3  NDG T  .   ? NDG P 1321 . ? 1_555 ? 
50  BC4 2  ASN A  520 ? ASN A 520  . ? 1_555 ? 
51  BC4 2  ARG A  581 ? ARG A 581  . ? 1_555 ? 
52  BC5 7  VAL B  78  ? VAL B 78   . ? 1_555 ? 
53  BC5 7  ASN B  85  ? ASN B 85   . ? 1_555 ? 
54  BC5 7  SER B  86  ? SER B 86   . ? 1_555 ? 
55  BC5 7  SER B  87  ? SER B 87   . ? 1_555 ? 
56  BC5 7  HOH EA .   ? HOH B 2452 . ? 1_555 ? 
57  BC5 7  NAG W  .   ? NAG Q 2086 . ? 1_555 ? 
58  BC5 7  HOH IA .   ? HOH Q 2290 . ? 1_555 ? 
59  BC6 1  NAG V  .   ? NAG Q 2085 . ? 1_555 ? 
60  BC7 5  GLU B  73  ? GLU B 73   . ? 1_555 ? 
61  BC7 5  ASN B  74  ? ASN B 74   . ? 1_555 ? 
62  BC7 5  ASN B  75  ? ASN B 75   . ? 1_555 ? 
63  BC7 5  ASN B  92  ? ASN B 92   . ? 1_555 ? 
64  BC7 5  HOH EA .   ? HOH B 2414 . ? 1_555 ? 
65  BC8 4  ARG B  147 ? ARG B 147  . ? 1_555 ? 
66  BC8 4  ILE B  148 ? ILE B 148  . ? 1_555 ? 
67  BC8 4  ASN B  150 ? ASN B 150  . ? 1_555 ? 
68  BC8 4  HOH EA .   ? HOH B 2367 . ? 1_555 ? 
69  BC9 8  ASN B  219 ? ASN B 219  . ? 1_555 ? 
70  BC9 8  THR B  221 ? THR B 221  . ? 1_555 ? 
71  BC9 8  GLN B  308 ? GLN B 308  . ? 1_555 ? 
72  BC9 8  GLU B  309 ? GLU B 309  . ? 1_555 ? 
73  BC9 8  HOH EA .   ? HOH B 2760 . ? 1_555 ? 
74  BC9 8  NAG Y  .   ? NAG R 2220 . ? 1_555 ? 
75  BC9 8  HOH JA .   ? HOH R 2291 . ? 1_555 ? 
76  BC9 8  HOH JA .   ? HOH R 2293 . ? 1_555 ? 
77  CC1 7  PHE B  222 ? PHE B 222  . ? 1_555 ? 
78  CC1 7  ASN B  272 ? ASN B 272  . ? 1_555 ? 
79  CC1 7  TYR B  330 ? TYR B 330  . ? 1_555 ? 
80  CC1 7  GLU B  332 ? GLU B 332  . ? 1_555 ? 
81  CC1 7  HOH EA .   ? HOH B 2768 . ? 1_555 ? 
82  CC1 7  NAG X  .   ? NAG R 2219 . ? 1_555 ? 
83  CC1 7  HOH JA .   ? HOH R 2289 . ? 1_555 ? 
84  CC2 7  ILE B  194 ? ILE B 194  . ? 1_555 ? 
85  CC2 7  ASN B  229 ? ASN B 229  . ? 1_555 ? 
86  CC2 7  THR B  231 ? THR B 231  . ? 1_555 ? 
87  CC2 7  GLU B  232 ? GLU B 232  . ? 1_555 ? 
88  CC2 7  NAG AA .   ? NAG S 2230 . ? 1_555 ? 
89  CC2 7  HOH KA .   ? HOH S 2284 . ? 1_555 ? 
90  CC2 7  HOH KA .   ? HOH S 2292 . ? 1_555 ? 
91  CC3 2  HOH EA .   ? HOH B 2914 . ? 3_555 ? 
92  CC3 2  NAG Z  .   ? NAG S 2229 . ? 1_555 ? 
93  CC4 7  ASN A  450 ? ASN A 450  . ? 2_564 ? 
94  CC4 7  HOH DA .   ? HOH A 1755 . ? 2_564 ? 
95  CC4 7  TRP B  187 ? TRP B 187  . ? 1_555 ? 
96  CC4 7  ASN B  281 ? ASN B 281  . ? 1_555 ? 
97  CC4 7  NAG CA .   ? NAG T 2282 . ? 1_555 ? 
98  CC4 7  HOH LA .   ? HOH T 2283 . ? 1_555 ? 
99  CC4 7  HOH LA .   ? HOH T 2288 . ? 1_555 ? 
100 CC5 4  THR B  188 ? THR B 188  . ? 1_555 ? 
101 CC5 4  HOH EA .   ? HOH B 2389 . ? 1_555 ? 
102 CC5 4  NAG BA .   ? NAG T 2281 . ? 1_555 ? 
103 CC5 4  HOH LA .   ? HOH T 2283 . ? 1_555 ? 
104 CC6 4  ILE B  319 ? ILE B 319  . ? 1_555 ? 
105 CC6 4  ASN B  321 ? ASN B 321  . ? 1_555 ? 
106 CC6 4  SER B  349 ? SER B 349  . ? 1_555 ? 
107 CC6 4  HOH EA .   ? HOH B 2921 . ? 1_555 ? 
108 CC7 5  GLY A  490 ? GLY A 490  . ? 1_555 ? 
109 CC7 5  LEU A  491 ? LEU A 491  . ? 1_555 ? 
110 CC7 5  LEU B  276 ? LEU B 276  . ? 2_565 ? 
111 CC7 5  VAL B  279 ? VAL B 279  . ? 2_565 ? 
112 CC7 5  HOH EA .   ? HOH B 2444 . ? 2_565 ? 
113 CC8 15 ARG A  125 ? ARG A 125  . ? 1_555 ? 
114 CC8 15 GLU A  205 ? GLU A 205  . ? 1_555 ? 
115 CC8 15 GLU A  206 ? GLU A 206  . ? 1_555 ? 
116 CC8 15 VAL A  207 ? VAL A 207  . ? 1_555 ? 
117 CC8 15 PHE A  357 ? PHE A 357  . ? 1_555 ? 
118 CC8 15 ARG A  358 ? ARG A 358  . ? 1_555 ? 
119 CC8 15 TYR A  547 ? TYR A 547  . ? 1_555 ? 
120 CC8 15 SER A  630 ? SER A 630  . ? 1_555 ? 
121 CC8 15 TYR A  631 ? TYR A 631  . ? 1_555 ? 
122 CC8 15 TYR A  662 ? TYR A 662  . ? 1_555 ? 
123 CC8 15 TYR A  666 ? TYR A 666  . ? 1_555 ? 
124 CC8 15 ASN A  710 ? ASN A 710  . ? 1_555 ? 
125 CC8 15 VAL A  711 ? VAL A 711  . ? 1_555 ? 
126 CC8 15 HOH DA .   ? HOH A 1546 . ? 1_555 ? 
127 CC8 15 HOH DA .   ? HOH A 1775 . ? 1_555 ? 
128 CC9 16 ARG B  125 ? ARG B 125  . ? 1_555 ? 
129 CC9 16 GLU B  205 ? GLU B 205  . ? 1_555 ? 
130 CC9 16 GLU B  206 ? GLU B 206  . ? 1_555 ? 
131 CC9 16 VAL B  207 ? VAL B 207  . ? 1_555 ? 
132 CC9 16 SER B  209 ? SER B 209  . ? 1_555 ? 
133 CC9 16 PHE B  357 ? PHE B 357  . ? 1_555 ? 
134 CC9 16 ARG B  358 ? ARG B 358  . ? 1_555 ? 
135 CC9 16 TYR B  547 ? TYR B 547  . ? 1_555 ? 
136 CC9 16 SER B  630 ? SER B 630  . ? 1_555 ? 
137 CC9 16 TYR B  631 ? TYR B 631  . ? 1_555 ? 
138 CC9 16 TYR B  662 ? TYR B 662  . ? 1_555 ? 
139 CC9 16 TYR B  666 ? TYR B 666  . ? 1_555 ? 
140 CC9 16 ASN B  710 ? ASN B 710  . ? 1_555 ? 
141 CC9 16 VAL B  711 ? VAL B 711  . ? 1_555 ? 
142 CC9 16 HOH EA .   ? HOH B 2343 . ? 1_555 ? 
143 CC9 16 HOH EA .   ? HOH B 2584 . ? 1_555 ? 
# 
_atom_sites.entry_id                    2QT9 
_atom_sites.fract_transf_matrix[1][1]   0.008496 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007932 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007301 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
NA 
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   . THR A  1 39  ? 35.090  46.611 77.477  1.00 47.82 ? 39   THR A N   1 
ATOM   2     C  CA  . THR A  1 39  ? 34.457  47.820 78.087  1.00 47.40 ? 39   THR A CA  1 
ATOM   3     C  C   . THR A  1 39  ? 34.641  49.066 77.223  1.00 46.74 ? 39   THR A C   1 
ATOM   4     O  O   . THR A  1 39  ? 33.705  49.861 77.071  1.00 47.43 ? 39   THR A O   1 
ATOM   5     C  CB  . THR A  1 39  ? 35.044  48.132 79.480  1.00 47.94 ? 39   THR A CB  1 
ATOM   6     O  OG1 . THR A  1 39  ? 34.470  49.353 79.974  1.00 48.78 ? 39   THR A OG1 1 
ATOM   7     C  CG2 . THR A  1 39  ? 36.568  48.292 79.396  1.00 48.13 ? 39   THR A CG2 1 
ATOM   8     N  N   . ARG A  1 40  ? 35.846  49.244 76.678  1.00 45.09 ? 40   ARG A N   1 
ATOM   9     C  CA  . ARG A  1 40  ? 36.132  50.401 75.831  1.00 42.97 ? 40   ARG A CA  1 
ATOM   10    C  C   . ARG A  1 40  ? 35.230  50.403 74.594  1.00 40.49 ? 40   ARG A C   1 
ATOM   11    O  O   . ARG A  1 40  ? 34.605  49.395 74.258  1.00 39.93 ? 40   ARG A O   1 
ATOM   12    C  CB  . ARG A  1 40  ? 37.612  50.413 75.414  1.00 43.75 ? 40   ARG A CB  1 
ATOM   13    C  CG  . ARG A  1 40  ? 38.125  49.076 74.916  1.00 45.52 ? 40   ARG A CG  1 
ATOM   14    C  CD  . ARG A  1 40  ? 39.632  49.087 74.609  1.00 46.34 ? 40   ARG A CD  1 
ATOM   15    N  NE  . ARG A  1 40  ? 40.082  47.723 74.331  1.00 47.52 ? 40   ARG A NE  1 
ATOM   16    C  CZ  . ARG A  1 40  ? 41.107  47.391 73.553  1.00 47.81 ? 40   ARG A CZ  1 
ATOM   17    N  NH1 . ARG A  1 40  ? 41.830  48.326 72.948  1.00 47.59 ? 40   ARG A NH1 1 
ATOM   18    N  NH2 . ARG A  1 40  ? 41.390  46.107 73.362  1.00 48.58 ? 40   ARG A NH2 1 
ATOM   19    N  N   . LYS A  1 41  ? 35.159  51.546 73.928  1.00 37.95 ? 41   LYS A N   1 
ATOM   20    C  CA  . LYS A  1 41  ? 34.326  51.681 72.750  1.00 35.65 ? 41   LYS A CA  1 
ATOM   21    C  C   . LYS A  1 41  ? 34.829  50.878 71.561  1.00 33.15 ? 41   LYS A C   1 
ATOM   22    O  O   . LYS A  1 41  ? 35.975  50.436 71.525  1.00 32.18 ? 41   LYS A O   1 
ATOM   23    C  CB  . LYS A  1 41  ? 34.210  53.156 72.361  1.00 37.37 ? 41   LYS A CB  1 
ATOM   24    C  CG  . LYS A  1 41  ? 35.501  53.971 72.530  1.00 41.11 ? 41   LYS A CG  1 
ATOM   25    C  CD  . LYS A  1 41  ? 35.298  55.435 72.092  1.00 43.24 ? 41   LYS A CD  1 
ATOM   26    C  CE  . LYS A  1 41  ? 36.428  56.356 72.567  1.00 44.89 ? 41   LYS A CE  1 
ATOM   27    N  NZ  . LYS A  1 41  ? 36.471  56.512 74.060  1.00 45.53 ? 41   LYS A NZ  1 
ATOM   28    N  N   . THR A  1 42  ? 33.948  50.661 70.593  1.00 30.11 ? 42   THR A N   1 
ATOM   29    C  CA  . THR A  1 42  ? 34.319  49.947 69.376  1.00 26.46 ? 42   THR A CA  1 
ATOM   30    C  C   . THR A  1 42  ? 34.392  50.995 68.284  1.00 24.58 ? 42   THR A C   1 
ATOM   31    O  O   . THR A  1 42  ? 34.018  52.140 68.507  1.00 24.77 ? 42   THR A O   1 
ATOM   32    C  CB  . THR A  1 42  ? 33.258  48.920 68.979  1.00 26.10 ? 42   THR A CB  1 
ATOM   33    O  OG1 . THR A  1 42  ? 32.007  49.589 68.779  1.00 23.01 ? 42   THR A OG1 1 
ATOM   34    C  CG2 . THR A  1 42  ? 33.109  47.859 70.069  1.00 25.33 ? 42   THR A CG2 1 
ATOM   35    N  N   . TYR A  1 43  ? 34.872  50.602 67.111  1.00 23.00 ? 43   TYR A N   1 
ATOM   36    C  CA  . TYR A  1 43  ? 34.979  51.513 65.980  1.00 20.98 ? 43   TYR A CA  1 
ATOM   37    C  C   . TYR A  1 43  ? 33.602  51.444 65.338  1.00 20.18 ? 43   TYR A C   1 
ATOM   38    O  O   . TYR A  1 43  ? 33.222  50.418 64.760  1.00 19.49 ? 43   TYR A O   1 
ATOM   39    C  CB  . TYR A  1 43  ? 36.066  51.019 65.022  1.00 20.82 ? 43   TYR A CB  1 
ATOM   40    C  CG  . TYR A  1 43  ? 36.318  51.928 63.843  1.00 20.58 ? 43   TYR A CG  1 
ATOM   41    C  CD1 . TYR A  1 43  ? 37.173  53.024 63.939  1.00 19.88 ? 43   TYR A CD1 1 
ATOM   42    C  CD2 . TYR A  1 43  ? 35.698  51.680 62.622  1.00 20.02 ? 43   TYR A CD2 1 
ATOM   43    C  CE1 . TYR A  1 43  ? 37.406  53.858 62.826  1.00 20.06 ? 43   TYR A CE1 1 
ATOM   44    C  CE2 . TYR A  1 43  ? 35.921  52.490 61.521  1.00 20.49 ? 43   TYR A CE2 1 
ATOM   45    C  CZ  . TYR A  1 43  ? 36.772  53.573 61.622  1.00 20.13 ? 43   TYR A CZ  1 
ATOM   46    O  OH  . TYR A  1 43  ? 36.984  54.333 60.497  1.00 19.99 ? 43   TYR A OH  1 
ATOM   47    N  N   . THR A  1 44  ? 32.869  52.547 65.446  1.00 19.59 ? 44   THR A N   1 
ATOM   48    C  CA  . THR A  1 44  ? 31.494  52.633 64.976  1.00 19.41 ? 44   THR A CA  1 
ATOM   49    C  C   . THR A  1 44  ? 31.273  53.112 63.547  1.00 19.63 ? 44   THR A C   1 
ATOM   50    O  O   . THR A  1 44  ? 32.205  53.566 62.870  1.00 19.36 ? 44   THR A O   1 
ATOM   51    C  CB  . THR A  1 44  ? 30.678  53.569 65.892  1.00 19.23 ? 44   THR A CB  1 
ATOM   52    O  OG1 . THR A  1 44  ? 31.088  54.920 65.647  1.00 18.48 ? 44   THR A OG1 1 
ATOM   53    C  CG2 . THR A  1 44  ? 30.896  53.212 67.394  1.00 19.37 ? 44   THR A CG2 1 
ATOM   54    N  N   . LEU A  1 45  ? 30.021  53.023 63.092  1.00 18.68 ? 45   LEU A N   1 
ATOM   55    C  CA  . LEU A  1 45  ? 29.704  53.471 61.740  1.00 19.01 ? 45   LEU A CA  1 
ATOM   56    C  C   . LEU A  1 45  ? 29.921  54.970 61.697  1.00 18.72 ? 45   LEU A C   1 
ATOM   57    O  O   . LEU A  1 45  ? 30.438  55.497 60.721  1.00 20.21 ? 45   LEU A O   1 
ATOM   58    C  CB  . LEU A  1 45  ? 28.255  53.148 61.360  1.00 17.64 ? 45   LEU A CB  1 
ATOM   59    C  CG  . LEU A  1 45  ? 27.889  53.692 59.970  1.00 17.42 ? 45   LEU A CG  1 
ATOM   60    C  CD1 . LEU A  1 45  ? 28.783  53.053 58.901  1.00 15.61 ? 45   LEU A CD1 1 
ATOM   61    C  CD2 . LEU A  1 45  ? 26.399  53.402 59.679  1.00 17.54 ? 45   LEU A CD2 1 
ATOM   62    N  N   . THR A  1 46  ? 29.549  55.662 62.765  1.00 19.38 ? 46   THR A N   1 
ATOM   63    C  CA  . THR A  1 46  ? 29.739  57.109 62.799  1.00 19.67 ? 46   THR A CA  1 
ATOM   64    C  C   . THR A  1 46  ? 31.237  57.451 62.785  1.00 19.56 ? 46   THR A C   1 
ATOM   65    O  O   . THR A  1 46  ? 31.650  58.415 62.142  1.00 20.37 ? 46   THR A O   1 
ATOM   66    C  CB  . THR A  1 46  ? 29.073  57.722 64.034  1.00 20.95 ? 46   THR A CB  1 
ATOM   67    O  OG1 . THR A  1 46  ? 27.710  57.287 64.094  1.00 23.55 ? 46   THR A OG1 1 
ATOM   68    C  CG2 . THR A  1 46  ? 29.101  59.233 63.960  1.00 20.42 ? 46   THR A CG2 1 
ATOM   69    N  N   . ASP A  1 47  ? 32.058  56.678 63.490  1.00 18.92 ? 47   ASP A N   1 
ATOM   70    C  CA  . ASP A  1 47  ? 33.493  56.940 63.465  1.00 18.56 ? 47   ASP A CA  1 
ATOM   71    C  C   . ASP A  1 47  ? 33.991  56.891 62.010  1.00 17.98 ? 47   ASP A C   1 
ATOM   72    O  O   . ASP A  1 47  ? 34.771  57.748 61.585  1.00 17.52 ? 47   ASP A O   1 
ATOM   73    C  CB  . ASP A  1 47  ? 34.238  55.896 64.297  1.00 19.23 ? 47   ASP A CB  1 
ATOM   74    C  CG  . ASP A  1 47  ? 34.042  56.098 65.798  1.00 21.14 ? 47   ASP A CG  1 
ATOM   75    O  OD1 . ASP A  1 47  ? 34.188  55.115 66.543  1.00 21.30 ? 47   ASP A OD1 1 
ATOM   76    O  OD2 . ASP A  1 47  ? 33.748  57.242 66.210  1.00 23.42 ? 47   ASP A OD2 1 
ATOM   77    N  N   . TYR A  1 48  ? 33.561  55.879 61.261  1.00 16.97 ? 48   TYR A N   1 
ATOM   78    C  CA  . TYR A  1 48  ? 33.971  55.746 59.864  1.00 18.60 ? 48   TYR A CA  1 
ATOM   79    C  C   . TYR A  1 48  ? 33.437  56.924 59.030  1.00 19.06 ? 48   TYR A C   1 
ATOM   80    O  O   . TYR A  1 48  ? 34.193  57.588 58.325  1.00 19.98 ? 48   TYR A O   1 
ATOM   81    C  CB  . TYR A  1 48  ? 33.456  54.418 59.277  1.00 18.27 ? 48   TYR A CB  1 
ATOM   82    C  CG  . TYR A  1 48  ? 33.598  54.346 57.772  1.00 19.87 ? 48   TYR A CG  1 
ATOM   83    C  CD1 . TYR A  1 48  ? 34.844  54.514 57.160  1.00 17.83 ? 48   TYR A CD1 1 
ATOM   84    C  CD2 . TYR A  1 48  ? 32.472  54.171 56.949  1.00 19.66 ? 48   TYR A CD2 1 
ATOM   85    C  CE1 . TYR A  1 48  ? 34.968  54.514 55.764  1.00 20.32 ? 48   TYR A CE1 1 
ATOM   86    C  CE2 . TYR A  1 48  ? 32.587  54.167 55.553  1.00 20.30 ? 48   TYR A CE2 1 
ATOM   87    C  CZ  . TYR A  1 48  ? 33.831  54.340 54.967  1.00 20.27 ? 48   TYR A CZ  1 
ATOM   88    O  OH  . TYR A  1 48  ? 33.927  54.353 53.595  1.00 21.73 ? 48   TYR A OH  1 
ATOM   89    N  N   . LEU A  1 49  ? 32.144  57.207 59.147  1.00 20.02 ? 49   LEU A N   1 
ATOM   90    C  CA  . LEU A  1 49  ? 31.519  58.289 58.372  1.00 21.72 ? 49   LEU A CA  1 
ATOM   91    C  C   . LEU A  1 49  ? 31.949  59.716 58.739  1.00 23.26 ? 49   LEU A C   1 
ATOM   92    O  O   . LEU A  1 49  ? 31.970  60.587 57.879  1.00 24.05 ? 49   LEU A O   1 
ATOM   93    C  CB  . LEU A  1 49  ? 29.998  58.183 58.479  1.00 20.20 ? 49   LEU A CB  1 
ATOM   94    C  CG  . LEU A  1 49  ? 29.394  56.874 57.960  1.00 20.48 ? 49   LEU A CG  1 
ATOM   95    C  CD1 . LEU A  1 49  ? 27.878  56.946 58.131  1.00 20.35 ? 49   LEU A CD1 1 
ATOM   96    C  CD2 . LEU A  1 49  ? 29.788  56.641 56.491  1.00 19.55 ? 49   LEU A CD2 1 
ATOM   97    N  N   . LYS A  1 50  ? 32.276  59.953 60.009  1.00 24.21 ? 50   LYS A N   1 
ATOM   98    C  CA  . LYS A  1 50  ? 32.701  61.274 60.458  1.00 25.85 ? 50   LYS A CA  1 
ATOM   99    C  C   . LYS A  1 50  ? 34.222  61.411 60.545  1.00 26.08 ? 50   LYS A C   1 
ATOM   100   O  O   . LYS A  1 50  ? 34.725  62.438 60.987  1.00 24.89 ? 50   LYS A O   1 
ATOM   101   C  CB  . LYS A  1 50  ? 32.105  61.595 61.830  1.00 27.46 ? 50   LYS A CB  1 
ATOM   102   C  CG  . LYS A  1 50  ? 30.596  61.717 61.831  1.00 30.39 ? 50   LYS A CG  1 
ATOM   103   C  CD  . LYS A  1 50  ? 30.156  62.758 60.814  1.00 31.96 ? 50   LYS A CD  1 
ATOM   104   C  CE  . LYS A  1 50  ? 28.687  63.057 60.963  1.00 34.64 ? 50   LYS A CE  1 
ATOM   105   N  NZ  . LYS A  1 50  ? 27.879  61.802 60.898  1.00 35.63 ? 50   LYS A NZ  1 
ATOM   106   N  N   . ASN A  1 51  ? 34.955  60.378 60.143  1.00 26.38 ? 51   ASN A N   1 
ATOM   107   C  CA  . ASN A  1 51  ? 36.420  60.425 60.190  1.00 28.08 ? 51   ASN A CA  1 
ATOM   108   C  C   . ASN A  1 51  ? 36.976  60.806 61.556  1.00 27.93 ? 51   ASN A C   1 
ATOM   109   O  O   . ASN A  1 51  ? 37.865  61.647 61.651  1.00 27.87 ? 51   ASN A O   1 
ATOM   110   C  CB  . ASN A  1 51  ? 36.952  61.420 59.164  1.00 30.18 ? 51   ASN A CB  1 
ATOM   111   C  CG  . ASN A  1 51  ? 36.717  60.967 57.746  1.00 32.90 ? 51   ASN A CG  1 
ATOM   112   O  OD1 . ASN A  1 51  ? 37.122  59.868 57.360  1.00 34.57 ? 51   ASN A OD1 1 
ATOM   113   N  ND2 . ASN A  1 51  ? 36.060  61.813 56.951  1.00 34.74 ? 51   ASN A ND2 1 
ATOM   114   N  N   . THR A  1 52  ? 36.459  60.184 62.606  1.00 27.08 ? 52   THR A N   1 
ATOM   115   C  CA  . THR A  1 52  ? 36.912  60.469 63.956  1.00 28.19 ? 52   THR A CA  1 
ATOM   116   C  C   . THR A  1 52  ? 38.374  60.118 64.136  1.00 27.84 ? 52   THR A C   1 
ATOM   117   O  O   . THR A  1 52  ? 39.113  60.841 64.804  1.00 27.08 ? 52   THR A O   1 
ATOM   118   C  CB  . THR A  1 52  ? 36.135  59.665 64.985  1.00 27.70 ? 52   THR A CB  1 
ATOM   119   O  OG1 . THR A  1 52  ? 34.743  59.938 64.833  1.00 30.91 ? 52   THR A OG1 1 
ATOM   120   C  CG2 . THR A  1 52  ? 36.567  60.049 66.389  1.00 29.46 ? 52   THR A CG2 1 
ATOM   121   N  N   . TYR A  1 53  ? 38.775  58.995 63.545  1.00 27.18 ? 53   TYR A N   1 
ATOM   122   C  CA  . TYR A  1 53  ? 40.148  58.516 63.647  1.00 27.76 ? 53   TYR A CA  1 
ATOM   123   C  C   . TYR A  1 53  ? 40.830  58.731 62.303  1.00 28.58 ? 53   TYR A C   1 
ATOM   124   O  O   . TYR A  1 53  ? 40.556  58.024 61.338  1.00 28.96 ? 53   TYR A O   1 
ATOM   125   C  CB  . TYR A  1 53  ? 40.137  57.043 64.023  1.00 26.75 ? 53   TYR A CB  1 
ATOM   126   C  CG  . TYR A  1 53  ? 39.503  56.803 65.366  1.00 26.85 ? 53   TYR A CG  1 
ATOM   127   C  CD1 . TYR A  1 53  ? 40.089  57.302 66.536  1.00 26.63 ? 53   TYR A CD1 1 
ATOM   128   C  CD2 . TYR A  1 53  ? 38.300  56.105 65.472  1.00 26.67 ? 53   TYR A CD2 1 
ATOM   129   C  CE1 . TYR A  1 53  ? 39.482  57.109 67.784  1.00 28.25 ? 53   TYR A CE1 1 
ATOM   130   C  CE2 . TYR A  1 53  ? 37.686  55.907 66.709  1.00 27.67 ? 53   TYR A CE2 1 
ATOM   131   C  CZ  . TYR A  1 53  ? 38.285  56.414 67.857  1.00 27.30 ? 53   TYR A CZ  1 
ATOM   132   O  OH  . TYR A  1 53  ? 37.673  56.225 69.061  1.00 28.39 ? 53   TYR A OH  1 
ATOM   133   N  N   . ARG A  1 54  ? 41.725  59.708 62.251  1.00 28.84 ? 54   ARG A N   1 
ATOM   134   C  CA  . ARG A  1 54  ? 42.383  60.053 61.006  1.00 29.43 ? 54   ARG A CA  1 
ATOM   135   C  C   . ARG A  1 54  ? 43.851  59.680 60.933  1.00 28.07 ? 54   ARG A C   1 
ATOM   136   O  O   . ARG A  1 54  ? 44.602  59.861 61.896  1.00 26.48 ? 54   ARG A O   1 
ATOM   137   C  CB  . ARG A  1 54  ? 42.228  61.552 60.783  1.00 32.93 ? 54   ARG A CB  1 
ATOM   138   C  CG  . ARG A  1 54  ? 42.455  62.029 59.354  1.00 37.59 ? 54   ARG A CG  1 
ATOM   139   C  CD  . ARG A  1 54  ? 42.293  63.560 59.304  1.00 41.20 ? 54   ARG A CD  1 
ATOM   140   N  NE  . ARG A  1 54  ? 41.265  64.023 60.242  1.00 43.44 ? 54   ARG A NE  1 
ATOM   141   C  CZ  . ARG A  1 54  ? 39.954  63.997 60.011  1.00 45.31 ? 54   ARG A CZ  1 
ATOM   142   N  NH1 . ARG A  1 54  ? 39.486  63.531 58.854  1.00 46.10 ? 54   ARG A NH1 1 
ATOM   143   N  NH2 . ARG A  1 54  ? 39.108  64.445 60.943  1.00 45.89 ? 54   ARG A NH2 1 
ATOM   144   N  N   . LEU A  1 55  ? 44.256  59.157 59.780  1.00 26.98 ? 55   LEU A N   1 
ATOM   145   C  CA  . LEU A  1 55  ? 45.647  58.785 59.562  1.00 26.66 ? 55   LEU A CA  1 
ATOM   146   C  C   . LEU A  1 55  ? 46.377  60.068 59.160  1.00 26.64 ? 55   LEU A C   1 
ATOM   147   O  O   . LEU A  1 55  ? 45.855  60.855 58.375  1.00 26.45 ? 55   LEU A O   1 
ATOM   148   C  CB  . LEU A  1 55  ? 45.740  57.763 58.430  1.00 27.93 ? 55   LEU A CB  1 
ATOM   149   C  CG  . LEU A  1 55  ? 45.039  56.416 58.650  1.00 29.00 ? 55   LEU A CG  1 
ATOM   150   C  CD1 . LEU A  1 55  ? 44.725  55.787 57.312  1.00 30.28 ? 55   LEU A CD1 1 
ATOM   151   C  CD2 . LEU A  1 55  ? 45.922  55.498 59.473  1.00 28.30 ? 55   LEU A CD2 1 
ATOM   152   N  N   . LYS A  1 56  ? 47.555  60.309 59.724  1.00 25.02 ? 56   LYS A N   1 
ATOM   153   C  CA  . LYS A  1 56  ? 48.307  61.498 59.346  1.00 24.80 ? 56   LYS A CA  1 
ATOM   154   C  C   . LYS A  1 56  ? 49.197  61.077 58.201  1.00 23.86 ? 56   LYS A C   1 
ATOM   155   O  O   . LYS A  1 56  ? 49.657  59.932 58.163  1.00 22.89 ? 56   LYS A O   1 
ATOM   156   C  CB  . LYS A  1 56  ? 49.181  62.020 60.487  1.00 25.62 ? 56   LYS A CB  1 
ATOM   157   C  CG  . LYS A  1 56  ? 48.419  62.831 61.524  1.00 27.97 ? 56   LYS A CG  1 
ATOM   158   C  CD  . LYS A  1 56  ? 49.367  63.458 62.549  1.00 29.21 ? 56   LYS A CD  1 
ATOM   159   C  CE  . LYS A  1 56  ? 48.589  64.092 63.701  1.00 30.79 ? 56   LYS A CE  1 
ATOM   160   N  NZ  . LYS A  1 56  ? 49.481  64.364 64.872  1.00 32.16 ? 56   LYS A NZ  1 
ATOM   161   N  N   . LEU A  1 57  ? 49.415  62.007 57.274  1.00 23.05 ? 57   LEU A N   1 
ATOM   162   C  CA  . LEU A  1 57  ? 50.244  61.782 56.100  1.00 23.62 ? 57   LEU A CA  1 
ATOM   163   C  C   . LEU A  1 57  ? 51.418  62.747 56.164  1.00 22.55 ? 57   LEU A C   1 
ATOM   164   O  O   . LEU A  1 57  ? 51.543  63.521 57.107  1.00 22.07 ? 57   LEU A O   1 
ATOM   165   C  CB  . LEU A  1 57  ? 49.440  62.069 54.819  1.00 25.16 ? 57   LEU A CB  1 
ATOM   166   C  CG  . LEU A  1 57  ? 48.310  61.114 54.408  1.00 26.54 ? 57   LEU A CG  1 
ATOM   167   C  CD1 . LEU A  1 57  ? 47.170  61.191 55.399  1.00 28.56 ? 57   LEU A CD1 1 
ATOM   168   C  CD2 . LEU A  1 57  ? 47.821  61.494 53.026  1.00 27.09 ? 57   LEU A CD2 1 
ATOM   169   N  N   . TYR A  1 58  ? 52.279  62.686 55.151  1.00 21.32 ? 58   TYR A N   1 
ATOM   170   C  CA  . TYR A  1 58  ? 53.426  63.588 55.031  1.00 19.10 ? 58   TYR A CA  1 
ATOM   171   C  C   . TYR A  1 58  ? 53.675  63.672 53.528  1.00 19.04 ? 58   TYR A C   1 
ATOM   172   O  O   . TYR A  1 58  ? 54.521  62.973 52.968  1.00 18.15 ? 58   TYR A O   1 
ATOM   173   C  CB  . TYR A  1 58  ? 54.652  63.038 55.761  1.00 18.01 ? 58   TYR A CB  1 
ATOM   174   C  CG  . TYR A  1 58  ? 55.716  64.093 56.021  1.00 16.13 ? 58   TYR A CG  1 
ATOM   175   C  CD1 . TYR A  1 58  ? 55.750  64.808 57.230  1.00 16.10 ? 58   TYR A CD1 1 
ATOM   176   C  CD2 . TYR A  1 58  ? 56.672  64.394 55.056  1.00 15.67 ? 58   TYR A CD2 1 
ATOM   177   C  CE1 . TYR A  1 58  ? 56.713  65.797 57.462  1.00 15.06 ? 58   TYR A CE1 1 
ATOM   178   C  CE2 . TYR A  1 58  ? 57.649  65.376 55.273  1.00 15.87 ? 58   TYR A CE2 1 
ATOM   179   C  CZ  . TYR A  1 58  ? 57.665  66.075 56.467  1.00 16.23 ? 58   TYR A CZ  1 
ATOM   180   O  OH  . TYR A  1 58  ? 58.620  67.044 56.663  1.00 16.72 ? 58   TYR A OH  1 
ATOM   181   N  N   . SER A  1 59  ? 52.881  64.505 52.871  1.00 18.59 ? 59   SER A N   1 
ATOM   182   C  CA  . SER A  1 59  ? 52.990  64.681 51.434  1.00 19.37 ? 59   SER A CA  1 
ATOM   183   C  C   . SER A  1 59  ? 53.979  65.798 51.170  1.00 19.97 ? 59   SER A C   1 
ATOM   184   O  O   . SER A  1 59  ? 53.715  66.950 51.469  1.00 21.22 ? 59   SER A O   1 
ATOM   185   C  CB  . SER A  1 59  ? 51.630  65.052 50.842  1.00 20.47 ? 59   SER A CB  1 
ATOM   186   O  OG  . SER A  1 59  ? 50.656  64.052 51.149  1.00 23.98 ? 59   SER A OG  1 
ATOM   187   N  N   . LEU A  1 60  ? 55.123  65.454 50.611  1.00 20.15 ? 60   LEU A N   1 
ATOM   188   C  CA  . LEU A  1 60  ? 56.128  66.446 50.321  1.00 19.97 ? 60   LEU A CA  1 
ATOM   189   C  C   . LEU A  1 60  ? 56.330  66.556 48.812  1.00 21.18 ? 60   LEU A C   1 
ATOM   190   O  O   . LEU A  1 60  ? 55.933  65.662 48.046  1.00 19.65 ? 60   LEU A O   1 
ATOM   191   C  CB  . LEU A  1 60  ? 57.437  66.066 51.011  1.00 17.96 ? 60   LEU A CB  1 
ATOM   192   C  CG  . LEU A  1 60  ? 58.033  64.706 50.652  1.00 16.94 ? 60   LEU A CG  1 
ATOM   193   C  CD1 . LEU A  1 60  ? 58.737  64.781 49.292  1.00 16.24 ? 60   LEU A CD1 1 
ATOM   194   C  CD2 . LEU A  1 60  ? 59.031  64.308 51.736  1.00 15.92 ? 60   LEU A CD2 1 
ATOM   195   N  N   . ARG A  1 61  ? 56.951  67.652 48.388  1.00 21.78 ? 61   ARG A N   1 
ATOM   196   C  CA  . ARG A  1 61  ? 57.201  67.858 46.971  1.00 22.74 ? 61   ARG A CA  1 
ATOM   197   C  C   . ARG A  1 61  ? 58.684  68.164 46.792  1.00 21.86 ? 61   ARG A C   1 
ATOM   198   O  O   . ARG A  1 61  ? 59.150  69.221 47.215  1.00 21.50 ? 61   ARG A O   1 
ATOM   199   C  CB  . ARG A  1 61  ? 56.380  69.042 46.444  1.00 24.44 ? 61   ARG A CB  1 
ATOM   200   C  CG  . ARG A  1 61  ? 54.938  69.088 46.899  1.00 28.95 ? 61   ARG A CG  1 
ATOM   201   C  CD  . ARG A  1 61  ? 54.210  70.305 46.321  1.00 32.44 ? 61   ARG A CD  1 
ATOM   202   N  NE  . ARG A  1 61  ? 52.756  70.163 46.390  1.00 35.19 ? 61   ARG A NE  1 
ATOM   203   C  CZ  . ARG A  1 61  ? 51.893  70.931 45.722  1.00 36.59 ? 61   ARG A CZ  1 
ATOM   204   N  NH1 . ARG A  1 61  ? 52.340  71.903 44.935  1.00 36.37 ? 61   ARG A NH1 1 
ATOM   205   N  NH2 . ARG A  1 61  ? 50.583  70.713 45.827  1.00 36.63 ? 61   ARG A NH2 1 
ATOM   206   N  N   . TRP A  1 62  ? 59.418  67.246 46.172  1.00 20.12 ? 62   TRP A N   1 
ATOM   207   C  CA  . TRP A  1 62  ? 60.839  67.452 45.918  1.00 20.74 ? 62   TRP A CA  1 
ATOM   208   C  C   . TRP A  1 62  ? 61.001  68.570 44.873  1.00 22.23 ? 62   TRP A C   1 
ATOM   209   O  O   . TRP A  1 62  ? 60.337  68.547 43.832  1.00 21.41 ? 62   TRP A O   1 
ATOM   210   C  CB  . TRP A  1 62  ? 61.481  66.161 45.381  1.00 19.97 ? 62   TRP A CB  1 
ATOM   211   C  CG  . TRP A  1 62  ? 61.633  65.078 46.410  1.00 19.19 ? 62   TRP A CG  1 
ATOM   212   C  CD1 . TRP A  1 62  ? 60.926  63.903 46.491  1.00 18.03 ? 62   TRP A CD1 1 
ATOM   213   C  CD2 . TRP A  1 62  ? 62.568  65.060 47.498  1.00 17.69 ? 62   TRP A CD2 1 
ATOM   214   N  NE1 . TRP A  1 62  ? 61.373  63.159 47.561  1.00 18.61 ? 62   TRP A NE1 1 
ATOM   215   C  CE2 . TRP A  1 62  ? 62.379  63.845 48.193  1.00 17.67 ? 62   TRP A CE2 1 
ATOM   216   C  CE3 . TRP A  1 62  ? 63.550  65.957 47.952  1.00 17.08 ? 62   TRP A CE3 1 
ATOM   217   C  CZ2 . TRP A  1 62  ? 63.137  63.499 49.324  1.00 17.88 ? 62   TRP A CZ2 1 
ATOM   218   C  CZ3 . TRP A  1 62  ? 64.307  65.614 49.083  1.00 18.49 ? 62   TRP A CZ3 1 
ATOM   219   C  CH2 . TRP A  1 62  ? 64.095  64.393 49.752  1.00 18.03 ? 62   TRP A CH2 1 
ATOM   220   N  N   . ILE A  1 63  ? 61.861  69.553 45.143  1.00 22.59 ? 63   ILE A N   1 
ATOM   221   C  CA  . ILE A  1 63  ? 62.072  70.633 44.168  1.00 23.06 ? 63   ILE A CA  1 
ATOM   222   C  C   . ILE A  1 63  ? 63.499  70.600 43.633  1.00 24.19 ? 63   ILE A C   1 
ATOM   223   O  O   . ILE A  1 63  ? 63.872  71.366 42.738  1.00 24.45 ? 63   ILE A O   1 
ATOM   224   C  CB  . ILE A  1 63  ? 61.817  72.021 44.782  1.00 23.29 ? 63   ILE A CB  1 
ATOM   225   C  CG1 . ILE A  1 63  ? 62.752  72.234 45.979  1.00 23.92 ? 63   ILE A CG1 1 
ATOM   226   C  CG2 . ILE A  1 63  ? 60.342  72.157 45.182  1.00 21.41 ? 63   ILE A CG2 1 
ATOM   227   C  CD1 . ILE A  1 63  ? 62.626  73.602 46.608  1.00 25.75 ? 63   ILE A CD1 1 
ATOM   228   N  N   . SER A  1 64  ? 64.306  69.708 44.194  1.00 24.27 ? 64   SER A N   1 
ATOM   229   C  CA  . SER A  1 64  ? 65.686  69.566 43.757  1.00 24.31 ? 64   SER A CA  1 
ATOM   230   C  C   . SER A  1 64  ? 66.173  68.239 44.304  1.00 24.72 ? 64   SER A C   1 
ATOM   231   O  O   . SER A  1 64  ? 65.386  67.419 44.766  1.00 24.51 ? 64   SER A O   1 
ATOM   232   C  CB  . SER A  1 64  ? 66.564  70.708 44.304  1.00 24.29 ? 64   SER A CB  1 
ATOM   233   O  OG  . SER A  1 64  ? 66.763  70.585 45.714  1.00 24.73 ? 64   SER A OG  1 
ATOM   234   N  N   . ASP A  1 65  ? 67.474  68.032 44.257  1.00 24.17 ? 65   ASP A N   1 
ATOM   235   C  CA  . ASP A  1 65  ? 68.038  66.813 44.771  1.00 25.89 ? 65   ASP A CA  1 
ATOM   236   C  C   . ASP A  1 65  ? 68.330  66.940 46.269  1.00 26.14 ? 65   ASP A C   1 
ATOM   237   O  O   . ASP A  1 65  ? 68.710  65.962 46.890  1.00 26.85 ? 65   ASP A O   1 
ATOM   238   C  CB  . ASP A  1 65  ? 69.318  66.513 44.003  1.00 26.49 ? 65   ASP A CB  1 
ATOM   239   C  CG  . ASP A  1 65  ? 69.757  65.069 44.134  1.00 28.26 ? 65   ASP A CG  1 
ATOM   240   O  OD1 . ASP A  1 65  ? 68.894  64.146 44.049  1.00 28.88 ? 65   ASP A OD1 1 
ATOM   241   O  OD2 . ASP A  1 65  ? 70.974  64.857 44.301  1.00 27.61 ? 65   ASP A OD2 1 
ATOM   242   N  N   . HIS A  1 66  ? 68.099  68.124 46.845  1.00 27.28 ? 66   HIS A N   1 
ATOM   243   C  CA  . HIS A  1 66  ? 68.400  68.389 48.264  1.00 28.39 ? 66   HIS A CA  1 
ATOM   244   C  C   . HIS A  1 66  ? 67.249  68.941 49.113  1.00 27.25 ? 66   HIS A C   1 
ATOM   245   O  O   . HIS A  1 66  ? 67.303  68.871 50.343  1.00 27.32 ? 66   HIS A O   1 
ATOM   246   C  CB  . HIS A  1 66  ? 69.560  69.402 48.377  1.00 30.94 ? 66   HIS A CB  1 
ATOM   247   C  CG  . HIS A  1 66  ? 70.698  69.140 47.438  1.00 34.19 ? 66   HIS A CG  1 
ATOM   248   N  ND1 . HIS A  1 66  ? 71.860  68.502 47.827  1.00 36.46 ? 66   HIS A ND1 1 
ATOM   249   C  CD2 . HIS A  1 66  ? 70.837  69.395 46.114  1.00 35.86 ? 66   HIS A CD2 1 
ATOM   250   C  CE1 . HIS A  1 66  ? 72.664  68.374 46.783  1.00 36.93 ? 66   HIS A CE1 1 
ATOM   251   N  NE2 . HIS A  1 66  ? 72.066  68.907 45.730  1.00 37.18 ? 66   HIS A NE2 1 
ATOM   252   N  N   . GLU A  1 67  ? 66.221  69.497 48.480  1.00 26.43 ? 67   GLU A N   1 
ATOM   253   C  CA  . GLU A  1 67  ? 65.115  70.098 49.230  1.00 24.90 ? 67   GLU A CA  1 
ATOM   254   C  C   . GLU A  1 67  ? 63.740  69.695 48.747  1.00 24.98 ? 67   GLU A C   1 
ATOM   255   O  O   . GLU A  1 67  ? 63.550  69.336 47.583  1.00 23.76 ? 67   GLU A O   1 
ATOM   256   C  CB  . GLU A  1 67  ? 65.175  71.634 49.158  1.00 25.23 ? 67   GLU A CB  1 
ATOM   257   C  CG  . GLU A  1 67  ? 66.480  72.275 49.613  1.00 26.30 ? 67   GLU A CG  1 
ATOM   258   C  CD  . GLU A  1 67  ? 66.387  73.799 49.667  1.00 27.81 ? 67   GLU A CD  1 
ATOM   259   O  OE1 . GLU A  1 67  ? 65.980  74.409 48.660  1.00 27.51 ? 67   GLU A OE1 1 
ATOM   260   O  OE2 . GLU A  1 67  ? 66.724  74.389 50.715  1.00 28.82 ? 67   GLU A OE2 1 
ATOM   261   N  N   . TYR A  1 68  ? 62.772  69.796 49.653  1.00 23.83 ? 68   TYR A N   1 
ATOM   262   C  CA  . TYR A  1 68  ? 61.391  69.501 49.329  1.00 23.38 ? 68   TYR A CA  1 
ATOM   263   C  C   . TYR A  1 68  ? 60.471  70.517 49.998  1.00 23.78 ? 68   TYR A C   1 
ATOM   264   O  O   . TYR A  1 68  ? 60.854  71.180 50.976  1.00 23.01 ? 68   TYR A O   1 
ATOM   265   C  CB  . TYR A  1 68  ? 61.029  68.069 49.762  1.00 21.44 ? 68   TYR A CB  1 
ATOM   266   C  CG  . TYR A  1 68  ? 61.032  67.802 51.259  1.00 18.81 ? 68   TYR A CG  1 
ATOM   267   C  CD1 . TYR A  1 68  ? 59.955  68.191 52.068  1.00 19.71 ? 68   TYR A CD1 1 
ATOM   268   C  CD2 . TYR A  1 68  ? 62.077  67.097 51.853  1.00 18.23 ? 68   TYR A CD2 1 
ATOM   269   C  CE1 . TYR A  1 68  ? 59.925  67.875 53.429  1.00 18.70 ? 68   TYR A CE1 1 
ATOM   270   C  CE2 . TYR A  1 68  ? 62.062  66.775 53.201  1.00 18.67 ? 68   TYR A CE2 1 
ATOM   271   C  CZ  . TYR A  1 68  ? 60.984  67.166 53.988  1.00 19.51 ? 68   TYR A CZ  1 
ATOM   272   O  OH  . TYR A  1 68  ? 60.993  66.864 55.335  1.00 19.17 ? 68   TYR A OH  1 
ATOM   273   N  N   . LEU A  1 69  ? 59.268  70.641 49.442  1.00 24.93 ? 69   LEU A N   1 
ATOM   274   C  CA  . LEU A  1 69  ? 58.227  71.536 49.954  1.00 26.27 ? 69   LEU A CA  1 
ATOM   275   C  C   . LEU A  1 69  ? 57.246  70.689 50.748  1.00 27.58 ? 69   LEU A C   1 
ATOM   276   O  O   . LEU A  1 69  ? 56.949  69.549 50.373  1.00 26.69 ? 69   LEU A O   1 
ATOM   277   C  CB  . LEU A  1 69  ? 57.458  72.189 48.810  1.00 26.30 ? 69   LEU A CB  1 
ATOM   278   C  CG  . LEU A  1 69  ? 58.279  73.060 47.856  1.00 27.20 ? 69   LEU A CG  1 
ATOM   279   C  CD1 . LEU A  1 69  ? 57.451  73.447 46.639  1.00 26.64 ? 69   LEU A CD1 1 
ATOM   280   C  CD2 . LEU A  1 69  ? 58.736  74.267 48.620  1.00 26.48 ? 69   LEU A CD2 1 
ATOM   281   N  N   . TYR A  1 70  ? 56.734  71.259 51.829  1.00 28.74 ? 70   TYR A N   1 
ATOM   282   C  CA  . TYR A  1 70  ? 55.787  70.575 52.687  1.00 30.61 ? 70   TYR A CA  1 
ATOM   283   C  C   . TYR A  1 70  ? 54.810  71.623 53.202  1.00 32.73 ? 70   TYR A C   1 
ATOM   284   O  O   . TYR A  1 70  ? 55.226  72.680 53.660  1.00 32.77 ? 70   TYR A O   1 
ATOM   285   C  CB  . TYR A  1 70  ? 56.527  69.922 53.863  1.00 29.63 ? 70   TYR A CB  1 
ATOM   286   C  CG  . TYR A  1 70  ? 55.631  69.192 54.846  1.00 29.46 ? 70   TYR A CG  1 
ATOM   287   C  CD1 . TYR A  1 70  ? 54.900  68.066 54.458  1.00 27.70 ? 70   TYR A CD1 1 
ATOM   288   C  CD2 . TYR A  1 70  ? 55.492  69.645 56.163  1.00 29.21 ? 70   TYR A CD2 1 
ATOM   289   C  CE1 . TYR A  1 70  ? 54.048  67.413 55.349  1.00 28.02 ? 70   TYR A CE1 1 
ATOM   290   C  CE2 . TYR A  1 70  ? 54.636  68.992 57.070  1.00 28.99 ? 70   TYR A CE2 1 
ATOM   291   C  CZ  . TYR A  1 70  ? 53.915  67.883 56.647  1.00 28.54 ? 70   TYR A CZ  1 
ATOM   292   O  OH  . TYR A  1 70  ? 53.021  67.287 57.508  1.00 30.08 ? 70   TYR A OH  1 
ATOM   293   N  N   . LYS A  1 71  ? 53.512  71.352 53.123  1.00 36.16 ? 71   LYS A N   1 
ATOM   294   C  CA  . LYS A  1 71  ? 52.533  72.329 53.611  1.00 39.45 ? 71   LYS A CA  1 
ATOM   295   C  C   . LYS A  1 71  ? 52.181  72.085 55.083  1.00 41.67 ? 71   LYS A C   1 
ATOM   296   O  O   . LYS A  1 71  ? 51.747  70.990 55.452  1.00 42.35 ? 71   LYS A O   1 
ATOM   297   C  CB  . LYS A  1 71  ? 51.265  72.299 52.750  1.00 39.54 ? 71   LYS A CB  1 
ATOM   298   C  CG  . LYS A  1 71  ? 50.218  73.311 53.212  1.00 41.29 ? 71   LYS A CG  1 
ATOM   299   C  CD  . LYS A  1 71  ? 49.194  73.661 52.124  1.00 41.75 ? 71   LYS A CD  1 
ATOM   300   C  CE  . LYS A  1 71  ? 48.134  74.620 52.689  1.00 42.50 ? 71   LYS A CE  1 
ATOM   301   N  NZ  . LYS A  1 71  ? 47.374  75.377 51.640  1.00 41.85 ? 71   LYS A NZ  1 
ATOM   302   N  N   . GLN A  1 72  ? 52.378  73.106 55.918  1.00 43.88 ? 72   GLN A N   1 
ATOM   303   C  CA  . GLN A  1 72  ? 52.103  73.010 57.353  1.00 45.81 ? 72   GLN A CA  1 
ATOM   304   C  C   . GLN A  1 72  ? 51.424  74.283 57.870  1.00 47.55 ? 72   GLN A C   1 
ATOM   305   O  O   . GLN A  1 72  ? 51.925  75.390 57.638  1.00 47.96 ? 72   GLN A O   1 
ATOM   306   C  CB  . GLN A  1 72  ? 53.415  72.802 58.111  1.00 46.37 ? 72   GLN A CB  1 
ATOM   307   C  CG  . GLN A  1 72  ? 53.243  72.190 59.488  1.00 47.88 ? 72   GLN A CG  1 
ATOM   308   C  CD  . GLN A  1 72  ? 54.562  71.836 60.136  1.00 49.39 ? 72   GLN A CD  1 
ATOM   309   O  OE1 . GLN A  1 72  ? 55.341  72.719 60.534  1.00 49.63 ? 72   GLN A OE1 1 
ATOM   310   N  NE2 . GLN A  1 72  ? 54.832  70.531 60.245  1.00 49.94 ? 72   GLN A NE2 1 
ATOM   311   N  N   . GLU A  1 73  ? 50.303  74.137 58.582  1.00 49.01 ? 73   GLU A N   1 
ATOM   312   C  CA  . GLU A  1 73  ? 49.590  75.308 59.115  1.00 50.10 ? 73   GLU A CA  1 
ATOM   313   C  C   . GLU A  1 73  ? 49.145  76.188 57.938  1.00 50.16 ? 73   GLU A C   1 
ATOM   314   O  O   . GLU A  1 73  ? 49.059  77.418 58.054  1.00 50.25 ? 73   GLU A O   1 
ATOM   315   C  CB  . GLU A  1 73  ? 50.523  76.112 60.049  1.00 51.21 ? 73   GLU A CB  1 
ATOM   316   C  CG  . GLU A  1 73  ? 50.865  75.429 61.393  1.00 53.14 ? 73   GLU A CG  1 
ATOM   317   C  CD  . GLU A  1 73  ? 52.223  75.880 61.971  1.00 54.65 ? 73   GLU A CD  1 
ATOM   318   O  OE1 . GLU A  1 73  ? 52.400  75.804 63.214  1.00 54.45 ? 73   GLU A OE1 1 
ATOM   319   O  OE2 . GLU A  1 73  ? 53.117  76.297 61.183  1.00 54.55 ? 73   GLU A OE2 1 
ATOM   320   N  N   . ASN A  1 74  ? 48.865  75.539 56.807  1.00 49.93 ? 74   ASN A N   1 
ATOM   321   C  CA  . ASN A  1 74  ? 48.450  76.224 55.587  1.00 49.36 ? 74   ASN A CA  1 
ATOM   322   C  C   . ASN A  1 74  ? 49.609  77.037 55.019  1.00 48.24 ? 74   ASN A C   1 
ATOM   323   O  O   . ASN A  1 74  ? 49.445  77.781 54.042  1.00 48.37 ? 74   ASN A O   1 
ATOM   324   C  CB  . ASN A  1 74  ? 47.248  77.145 55.844  1.00 50.57 ? 74   ASN A CB  1 
ATOM   325   C  CG  . ASN A  1 74  ? 45.963  76.373 56.096  1.00 51.66 ? 74   ASN A CG  1 
ATOM   326   O  OD1 . ASN A  1 74  ? 45.616  75.456 55.340  1.00 52.31 ? 74   ASN A OD1 1 
ATOM   327   N  ND2 . ASN A  1 74  ? 45.240  76.751 57.153  1.00 52.26 ? 74   ASN A ND2 1 
ATOM   328   N  N   . ASN A  1 75  ? 50.775  76.904 55.649  1.00 46.14 ? 75   ASN A N   1 
ATOM   329   C  CA  . ASN A  1 75  ? 51.985  77.590 55.198  1.00 44.08 ? 75   ASN A CA  1 
ATOM   330   C  C   . ASN A  1 75  ? 52.829  76.592 54.402  1.00 42.31 ? 75   ASN A C   1 
ATOM   331   O  O   . ASN A  1 75  ? 52.784  75.387 54.656  1.00 42.76 ? 75   ASN A O   1 
ATOM   332   C  CB  . ASN A  1 75  ? 52.787  78.094 56.395  1.00 44.62 ? 75   ASN A CB  1 
ATOM   333   C  CG  . ASN A  1 75  ? 52.104  79.240 57.108  1.00 46.65 ? 75   ASN A CG  1 
ATOM   334   O  OD1 . ASN A  1 75  ? 52.184  80.399 56.678  1.00 47.69 ? 75   ASN A OD1 1 
ATOM   335   N  ND2 . ASN A  1 75  ? 51.411  78.925 58.201  1.00 47.17 ? 75   ASN A ND2 1 
ATOM   336   N  N   . ILE A  1 76  ? 53.592  77.090 53.437  1.00 39.19 ? 76   ILE A N   1 
ATOM   337   C  CA  . ILE A  1 76  ? 54.434  76.222 52.634  1.00 36.27 ? 76   ILE A CA  1 
ATOM   338   C  C   . ILE A  1 76  ? 55.852  76.398 53.121  1.00 34.82 ? 76   ILE A C   1 
ATOM   339   O  O   . ILE A  1 76  ? 56.400  77.501 53.063  1.00 35.48 ? 76   ILE A O   1 
ATOM   340   C  CB  . ILE A  1 76  ? 54.358  76.582 51.138  1.00 36.01 ? 76   ILE A CB  1 
ATOM   341   C  CG1 . ILE A  1 76  ? 52.919  76.408 50.643  1.00 35.66 ? 76   ILE A CG1 1 
ATOM   342   C  CG2 . ILE A  1 76  ? 55.307  75.691 50.335  1.00 35.27 ? 76   ILE A CG2 1 
ATOM   343   C  CD1 . ILE A  1 76  ? 52.693  76.809 49.188  1.00 36.13 ? 76   ILE A CD1 1 
ATOM   344   N  N   . LEU A  1 77  ? 56.440  75.316 53.621  1.00 32.55 ? 77   LEU A N   1 
ATOM   345   C  CA  . LEU A  1 77  ? 57.800  75.362 54.136  1.00 31.17 ? 77   LEU A CA  1 
ATOM   346   C  C   . LEU A  1 77  ? 58.758  74.626 53.199  1.00 29.83 ? 77   LEU A C   1 
ATOM   347   O  O   . LEU A  1 77  ? 58.345  73.744 52.436  1.00 29.19 ? 77   LEU A O   1 
ATOM   348   C  CB  . LEU A  1 77  ? 57.840  74.712 55.526  1.00 31.25 ? 77   LEU A CB  1 
ATOM   349   C  CG  . LEU A  1 77  ? 56.894  75.309 56.579  1.00 32.21 ? 77   LEU A CG  1 
ATOM   350   C  CD1 . LEU A  1 77  ? 56.890  74.433 57.820  1.00 31.90 ? 77   LEU A CD1 1 
ATOM   351   C  CD2 . LEU A  1 77  ? 57.338  76.725 56.928  1.00 32.08 ? 77   LEU A CD2 1 
ATOM   352   N  N   . VAL A  1 78  ? 60.029  75.000 53.236  1.00 27.87 ? 78   VAL A N   1 
ATOM   353   C  CA  . VAL A  1 78  ? 61.010  74.310 52.422  1.00 27.76 ? 78   VAL A CA  1 
ATOM   354   C  C   . VAL A  1 78  ? 61.946  73.622 53.404  1.00 27.23 ? 78   VAL A C   1 
ATOM   355   O  O   . VAL A  1 78  ? 62.376  74.221 54.392  1.00 27.29 ? 78   VAL A O   1 
ATOM   356   C  CB  . VAL A  1 78  ? 61.800  75.268 51.479  1.00 27.87 ? 78   VAL A CB  1 
ATOM   357   C  CG1 . VAL A  1 78  ? 62.388  76.449 52.261  1.00 28.70 ? 78   VAL A CG1 1 
ATOM   358   C  CG2 . VAL A  1 78  ? 62.896  74.499 50.798  1.00 26.83 ? 78   VAL A CG2 1 
ATOM   359   N  N   . PHE A  1 79  ? 62.234  72.351 53.145  1.00 26.60 ? 79   PHE A N   1 
ATOM   360   C  CA  . PHE A  1 79  ? 63.094  71.570 54.022  1.00 24.05 ? 79   PHE A CA  1 
ATOM   361   C  C   . PHE A  1 79  ? 64.360  71.138 53.317  1.00 25.71 ? 79   PHE A C   1 
ATOM   362   O  O   . PHE A  1 79  ? 64.364  70.859 52.113  1.00 25.11 ? 79   PHE A O   1 
ATOM   363   C  CB  . PHE A  1 79  ? 62.380  70.293 54.478  1.00 23.78 ? 79   PHE A CB  1 
ATOM   364   C  CG  . PHE A  1 79  ? 61.282  70.522 55.490  1.00 22.21 ? 79   PHE A CG  1 
ATOM   365   C  CD1 . PHE A  1 79  ? 61.469  70.180 56.826  1.00 21.73 ? 79   PHE A CD1 1 
ATOM   366   C  CD2 . PHE A  1 79  ? 60.067  71.068 55.105  1.00 21.46 ? 79   PHE A CD2 1 
ATOM   367   C  CE1 . PHE A  1 79  ? 60.460  70.376 57.774  1.00 19.91 ? 79   PHE A CE1 1 
ATOM   368   C  CE2 . PHE A  1 79  ? 59.044  71.273 56.038  1.00 22.45 ? 79   PHE A CE2 1 
ATOM   369   C  CZ  . PHE A  1 79  ? 59.247  70.924 57.379  1.00 22.69 ? 79   PHE A CZ  1 
ATOM   370   N  N   . ASN A  1 80  ? 65.423  71.057 54.103  1.00 24.72 ? 80   ASN A N   1 
ATOM   371   C  CA  . ASN A  1 80  ? 66.712  70.598 53.652  1.00 25.36 ? 80   ASN A CA  1 
ATOM   372   C  C   . ASN A  1 80  ? 66.703  69.128 54.093  1.00 25.88 ? 80   ASN A C   1 
ATOM   373   O  O   . ASN A  1 80  ? 66.571  68.841 55.287  1.00 25.21 ? 80   ASN A O   1 
ATOM   374   C  CB  . ASN A  1 80  ? 67.793  71.392 54.379  1.00 25.18 ? 80   ASN A CB  1 
ATOM   375   C  CG  . ASN A  1 80  ? 69.177  70.880 54.099  1.00 26.41 ? 80   ASN A CG  1 
ATOM   376   O  OD1 . ASN A  1 80  ? 69.573  69.823 54.598  1.00 26.26 ? 80   ASN A OD1 1 
ATOM   377   N  ND2 . ASN A  1 80  ? 69.931  71.627 53.295  1.00 26.19 ? 80   ASN A ND2 1 
ATOM   378   N  N   . ALA A  1 81  ? 66.826  68.202 53.139  1.00 25.87 ? 81   ALA A N   1 
ATOM   379   C  CA  . ALA A  1 81  ? 66.795  66.764 53.436  1.00 25.49 ? 81   ALA A CA  1 
ATOM   380   C  C   . ALA A  1 81  ? 67.924  66.307 54.362  1.00 26.05 ? 81   ALA A C   1 
ATOM   381   O  O   . ALA A  1 81  ? 67.725  65.519 55.297  1.00 23.19 ? 81   ALA A O   1 
ATOM   382   C  CB  . ALA A  1 81  ? 66.836  65.950 52.111  1.00 25.09 ? 81   ALA A CB  1 
ATOM   383   N  N   . GLU A  1 82  ? 69.116  66.819 54.104  1.00 26.65 ? 82   GLU A N   1 
ATOM   384   C  CA  . GLU A  1 82  ? 70.279  66.447 54.885  1.00 29.20 ? 82   GLU A CA  1 
ATOM   385   C  C   . GLU A  1 82  ? 70.158  66.606 56.412  1.00 29.63 ? 82   GLU A C   1 
ATOM   386   O  O   . GLU A  1 82  ? 70.453  65.676 57.173  1.00 29.42 ? 82   GLU A O   1 
ATOM   387   C  CB  . GLU A  1 82  ? 71.473  67.260 54.391  1.00 31.46 ? 82   GLU A CB  1 
ATOM   388   C  CG  . GLU A  1 82  ? 72.720  67.079 55.207  1.00 35.61 ? 82   GLU A CG  1 
ATOM   389   C  CD  . GLU A  1 82  ? 73.510  65.862 54.811  1.00 38.86 ? 82   GLU A CD  1 
ATOM   390   O  OE1 . GLU A  1 82  ? 72.967  64.729 54.868  1.00 39.67 ? 82   GLU A OE1 1 
ATOM   391   O  OE2 . GLU A  1 82  ? 74.698  66.044 54.435  1.00 41.77 ? 82   GLU A OE2 1 
ATOM   392   N  N   . TYR A  1 83  ? 69.727  67.785 56.847  1.00 29.70 ? 83   TYR A N   1 
ATOM   393   C  CA  . TYR A  1 83  ? 69.640  68.100 58.273  1.00 30.29 ? 83   TYR A CA  1 
ATOM   394   C  C   . TYR A  1 83  ? 68.242  68.229 58.853  1.00 28.93 ? 83   TYR A C   1 
ATOM   395   O  O   . TYR A  1 83  ? 68.077  68.279 60.072  1.00 28.26 ? 83   TYR A O   1 
ATOM   396   C  CB  . TYR A  1 83  ? 70.413  69.398 58.540  1.00 32.05 ? 83   TYR A CB  1 
ATOM   397   C  CG  . TYR A  1 83  ? 71.849  69.332 58.076  1.00 35.22 ? 83   TYR A CG  1 
ATOM   398   C  CD1 . TYR A  1 83  ? 72.276  70.045 56.948  1.00 36.93 ? 83   TYR A CD1 1 
ATOM   399   C  CD2 . TYR A  1 83  ? 72.778  68.534 58.744  1.00 36.74 ? 83   TYR A CD2 1 
ATOM   400   C  CE1 . TYR A  1 83  ? 73.598  69.961 56.504  1.00 38.09 ? 83   TYR A CE1 1 
ATOM   401   C  CE2 . TYR A  1 83  ? 74.100  68.441 58.307  1.00 38.09 ? 83   TYR A CE2 1 
ATOM   402   C  CZ  . TYR A  1 83  ? 74.502  69.153 57.191  1.00 38.63 ? 83   TYR A CZ  1 
ATOM   403   O  OH  . TYR A  1 83  ? 75.805  69.032 56.750  1.00 41.43 ? 83   TYR A OH  1 
ATOM   404   N  N   . GLY A  1 84  ? 67.247  68.318 57.983  1.00 27.36 ? 84   GLY A N   1 
ATOM   405   C  CA  . GLY A  1 84  ? 65.887  68.439 58.445  1.00 27.34 ? 84   GLY A CA  1 
ATOM   406   C  C   . GLY A  1 84  ? 65.487  69.849 58.825  1.00 27.75 ? 84   GLY A C   1 
ATOM   407   O  O   . GLY A  1 84  ? 64.362  70.050 59.275  1.00 26.63 ? 84   GLY A O   1 
ATOM   408   N  N   . ASN A  1 85  ? 66.392  70.820 58.671  1.00 28.45 ? 85   ASN A N   1 
ATOM   409   C  CA  . ASN A  1 85  ? 66.057  72.211 58.995  1.00 30.14 ? 85   ASN A CA  1 
ATOM   410   C  C   . ASN A  1 85  ? 65.214  72.813 57.883  1.00 30.76 ? 85   ASN A C   1 
ATOM   411   O  O   . ASN A  1 85  ? 65.290  72.387 56.729  1.00 29.98 ? 85   ASN A O   1 
ATOM   412   C  CB  . ASN A  1 85  ? 67.318  73.069 59.223  1.00 31.55 ? 85   ASN A CB  1 
ATOM   413   C  CG  . ASN A  1 85  ? 68.240  73.111 58.012  1.00 34.43 ? 85   ASN A CG  1 
ATOM   414   O  OD1 . ASN A  1 85  ? 68.949  72.147 57.722  1.00 34.94 ? 85   ASN A OD1 1 
ATOM   415   N  ND2 . ASN A  1 85  ? 68.230  74.235 57.303  1.00 37.28 ? 85   ASN A ND2 1 
ATOM   416   N  N   . SER A  1 86  ? 64.388  73.790 58.228  1.00 31.25 ? 86   SER A N   1 
ATOM   417   C  CA  . SER A  1 86  ? 63.540  74.400 57.223  1.00 32.44 ? 86   SER A CA  1 
ATOM   418   C  C   . SER A  1 86  ? 63.389  75.906 57.366  1.00 32.94 ? 86   SER A C   1 
ATOM   419   O  O   . SER A  1 86  ? 63.863  76.508 58.333  1.00 33.30 ? 86   SER A O   1 
ATOM   420   C  CB  . SER A  1 86  ? 62.154  73.753 57.244  1.00 33.05 ? 86   SER A CB  1 
ATOM   421   O  OG  . SER A  1 86  ? 61.508  73.958 58.490  1.00 34.65 ? 86   SER A OG  1 
ATOM   422   N  N   . SER A  1 87  ? 62.737  76.498 56.373  1.00 32.82 ? 87   SER A N   1 
ATOM   423   C  CA  . SER A  1 87  ? 62.459  77.928 56.342  1.00 33.43 ? 87   SER A CA  1 
ATOM   424   C  C   . SER A  1 87  ? 61.056  78.031 55.768  1.00 34.40 ? 87   SER A C   1 
ATOM   425   O  O   . SER A  1 87  ? 60.584  77.103 55.101  1.00 34.18 ? 87   SER A O   1 
ATOM   426   C  CB  . SER A  1 87  ? 63.437  78.668 55.417  1.00 33.21 ? 87   SER A CB  1 
ATOM   427   O  OG  . SER A  1 87  ? 64.778  78.599 55.896  1.00 33.69 ? 87   SER A OG  1 
ATOM   428   N  N   . VAL A  1 88  ? 60.385  79.145 56.032  1.00 34.72 ? 88   VAL A N   1 
ATOM   429   C  CA  . VAL A  1 88  ? 59.044  79.358 55.510  1.00 34.91 ? 88   VAL A CA  1 
ATOM   430   C  C   . VAL A  1 88  ? 59.236  79.765 54.062  1.00 36.02 ? 88   VAL A C   1 
ATOM   431   O  O   . VAL A  1 88  ? 60.117  80.573 53.756  1.00 35.74 ? 88   VAL A O   1 
ATOM   432   C  CB  . VAL A  1 88  ? 58.329  80.491 56.264  1.00 35.83 ? 88   VAL A CB  1 
ATOM   433   C  CG1 . VAL A  1 88  ? 56.920  80.689 55.702  1.00 35.63 ? 88   VAL A CG1 1 
ATOM   434   C  CG2 . VAL A  1 88  ? 58.277  80.157 57.766  1.00 35.21 ? 88   VAL A CG2 1 
ATOM   435   N  N   . PHE A  1 89  ? 58.430  79.203 53.168  1.00 35.81 ? 89   PHE A N   1 
ATOM   436   C  CA  . PHE A  1 89  ? 58.567  79.536 51.764  1.00 36.44 ? 89   PHE A CA  1 
ATOM   437   C  C   . PHE A  1 89  ? 57.432  80.440 51.312  1.00 38.11 ? 89   PHE A C   1 
ATOM   438   O  O   . PHE A  1 89  ? 57.621  81.314 50.462  1.00 38.57 ? 89   PHE A O   1 
ATOM   439   C  CB  . PHE A  1 89  ? 58.606  78.256 50.923  1.00 35.35 ? 89   PHE A CB  1 
ATOM   440   C  CG  . PHE A  1 89  ? 58.891  78.500 49.475  1.00 33.97 ? 89   PHE A CG  1 
ATOM   441   C  CD1 . PHE A  1 89  ? 57.867  78.841 48.599  1.00 32.89 ? 89   PHE A CD1 1 
ATOM   442   C  CD2 . PHE A  1 89  ? 60.195  78.442 48.998  1.00 33.78 ? 89   PHE A CD2 1 
ATOM   443   C  CE1 . PHE A  1 89  ? 58.135  79.127 47.262  1.00 33.66 ? 89   PHE A CE1 1 
ATOM   444   C  CE2 . PHE A  1 89  ? 60.483  78.726 47.663  1.00 34.13 ? 89   PHE A CE2 1 
ATOM   445   C  CZ  . PHE A  1 89  ? 59.448  79.070 46.792  1.00 33.89 ? 89   PHE A CZ  1 
ATOM   446   N  N   . LEU A  1 90  ? 56.255  80.231 51.887  1.00 39.79 ? 90   LEU A N   1 
ATOM   447   C  CA  . LEU A  1 90  ? 55.090  81.039 51.546  1.00 42.11 ? 90   LEU A CA  1 
ATOM   448   C  C   . LEU A  1 90  ? 54.141  81.147 52.740  1.00 43.16 ? 90   LEU A C   1 
ATOM   449   O  O   . LEU A  1 90  ? 53.627  80.141 53.242  1.00 42.88 ? 90   LEU A O   1 
ATOM   450   C  CB  . LEU A  1 90  ? 54.349  80.426 50.356  1.00 42.44 ? 90   LEU A CB  1 
ATOM   451   C  CG  . LEU A  1 90  ? 53.276  81.302 49.722  1.00 43.09 ? 90   LEU A CG  1 
ATOM   452   C  CD1 . LEU A  1 90  ? 53.949  82.380 48.873  1.00 43.11 ? 90   LEU A CD1 1 
ATOM   453   C  CD2 . LEU A  1 90  ? 52.360  80.455 48.864  1.00 43.25 ? 90   LEU A CD2 1 
ATOM   454   N  N   . GLU A  1 91  ? 53.918  82.380 53.182  1.00 45.59 ? 91   GLU A N   1 
ATOM   455   C  CA  . GLU A  1 91  ? 53.041  82.673 54.306  1.00 46.84 ? 91   GLU A CA  1 
ATOM   456   C  C   . GLU A  1 91  ? 51.605  82.340 53.965  1.00 47.80 ? 91   GLU A C   1 
ATOM   457   O  O   . GLU A  1 91  ? 51.124  82.639 52.860  1.00 47.56 ? 91   GLU A O   1 
ATOM   458   C  CB  . GLU A  1 91  ? 53.124  84.154 54.662  1.00 48.40 ? 91   GLU A CB  1 
ATOM   459   C  CG  . GLU A  1 91  ? 54.496  84.627 55.066  1.00 49.58 ? 91   GLU A CG  1 
ATOM   460   C  CD  . GLU A  1 91  ? 55.025  83.877 56.267  1.00 51.58 ? 91   GLU A CD  1 
ATOM   461   O  OE1 . GLU A  1 91  ? 54.215  83.518 57.161  1.00 51.87 ? 91   GLU A OE1 1 
ATOM   462   O  OE2 . GLU A  1 91  ? 56.259  83.651 56.325  1.00 52.32 ? 91   GLU A OE2 1 
ATOM   463   N  N   . ASN A  1 92  ? 50.922  81.733 54.930  1.00 48.96 ? 92   ASN A N   1 
ATOM   464   C  CA  . ASN A  1 92  ? 49.518  81.343 54.783  1.00 49.83 ? 92   ASN A CA  1 
ATOM   465   C  C   . ASN A  1 92  ? 48.626  82.578 54.683  1.00 49.77 ? 92   ASN A C   1 
ATOM   466   O  O   . ASN A  1 92  ? 47.501  82.498 54.178  1.00 50.46 ? 92   ASN A O   1 
ATOM   467   C  CB  . ASN A  1 92  ? 49.088  80.500 55.991  1.00 51.24 ? 92   ASN A CB  1 
ATOM   468   C  CG  . ASN A  1 92  ? 49.240  81.257 57.309  1.00 52.75 ? 92   ASN A CG  1 
ATOM   469   O  OD1 . ASN A  1 92  ? 50.297  81.848 57.579  1.00 53.45 ? 92   ASN A OD1 1 
ATOM   470   N  ND2 . ASN A  1 92  ? 48.190  81.254 58.127  1.00 54.30 ? 92   ASN A ND2 1 
ATOM   471   N  N   . SER A  1 93  ? 49.131  83.715 55.164  1.00 48.98 ? 93   SER A N   1 
ATOM   472   C  CA  . SER A  1 93  ? 48.371  84.961 55.141  1.00 47.97 ? 93   SER A CA  1 
ATOM   473   C  C   . SER A  1 93  ? 48.653  85.773 53.883  1.00 47.44 ? 93   SER A C   1 
ATOM   474   O  O   . SER A  1 93  ? 47.893  86.688 53.548  1.00 47.09 ? 93   SER A O   1 
ATOM   475   C  CB  . SER A  1 93  ? 48.700  85.804 56.375  1.00 48.17 ? 93   SER A CB  1 
ATOM   476   O  OG  . SER A  1 93  ? 50.051  86.234 56.343  1.00 49.08 ? 93   SER A OG  1 
ATOM   477   N  N   . THR A  1 94  ? 49.737  85.431 53.185  1.00 46.74 ? 94   THR A N   1 
ATOM   478   C  CA  . THR A  1 94  ? 50.121  86.134 51.959  1.00 45.76 ? 94   THR A CA  1 
ATOM   479   C  C   . THR A  1 94  ? 48.930  86.435 51.052  1.00 45.28 ? 94   THR A C   1 
ATOM   480   O  O   . THR A  1 94  ? 48.914  87.458 50.362  1.00 45.48 ? 94   THR A O   1 
ATOM   481   C  CB  . THR A  1 94  ? 51.152  85.334 51.126  1.00 46.10 ? 94   THR A CB  1 
ATOM   482   O  OG1 . THR A  1 94  ? 52.335  85.114 51.903  1.00 47.08 ? 94   THR A OG1 1 
ATOM   483   C  CG2 . THR A  1 94  ? 51.529  86.103 49.857  1.00 44.94 ? 94   THR A CG2 1 
ATOM   484   N  N   . PHE A  1 95  ? 47.932  85.558 51.046  1.00 44.47 ? 95   PHE A N   1 
ATOM   485   C  CA  . PHE A  1 95  ? 46.763  85.780 50.198  1.00 44.19 ? 95   PHE A CA  1 
ATOM   486   C  C   . PHE A  1 95  ? 45.454  85.991 50.958  1.00 45.05 ? 95   PHE A C   1 
ATOM   487   O  O   . PHE A  1 95  ? 44.385  85.637 50.460  1.00 45.83 ? 95   PHE A O   1 
ATOM   488   C  CB  . PHE A  1 95  ? 46.611  84.614 49.226  1.00 42.58 ? 95   PHE A CB  1 
ATOM   489   C  CG  . PHE A  1 95  ? 47.805  84.413 48.344  1.00 41.29 ? 95   PHE A CG  1 
ATOM   490   C  CD1 . PHE A  1 95  ? 48.087  85.309 47.321  1.00 40.10 ? 95   PHE A CD1 1 
ATOM   491   C  CD2 . PHE A  1 95  ? 48.666  83.340 48.555  1.00 40.72 ? 95   PHE A CD2 1 
ATOM   492   C  CE1 . PHE A  1 95  ? 49.213  85.136 46.519  1.00 40.26 ? 95   PHE A CE1 1 
ATOM   493   C  CE2 . PHE A  1 95  ? 49.793  83.160 47.761  1.00 40.00 ? 95   PHE A CE2 1 
ATOM   494   C  CZ  . PHE A  1 95  ? 50.070  84.059 46.739  1.00 39.74 ? 95   PHE A CZ  1 
ATOM   495   N  N   . ASP A  1 96  ? 45.530  86.578 52.152  1.00 45.36 ? 96   ASP A N   1 
ATOM   496   C  CA  . ASP A  1 96  ? 44.329  86.822 52.954  1.00 45.56 ? 96   ASP A CA  1 
ATOM   497   C  C   . ASP A  1 96  ? 43.267  87.656 52.243  1.00 45.75 ? 96   ASP A C   1 
ATOM   498   O  O   . ASP A  1 96  ? 42.083  87.555 52.557  1.00 45.93 ? 96   ASP A O   1 
ATOM   499   C  CB  . ASP A  1 96  ? 44.687  87.503 54.279  1.00 45.84 ? 96   ASP A CB  1 
ATOM   500   C  CG  . ASP A  1 96  ? 45.223  86.528 55.309  1.00 46.27 ? 96   ASP A CG  1 
ATOM   501   O  OD1 . ASP A  1 96  ? 45.035  85.304 55.122  1.00 47.09 ? 96   ASP A OD1 1 
ATOM   502   O  OD2 . ASP A  1 96  ? 45.820  86.983 56.315  1.00 46.50 ? 96   ASP A OD2 1 
ATOM   503   N  N   . GLU A  1 97  ? 43.682  88.488 51.295  1.00 45.94 ? 97   GLU A N   1 
ATOM   504   C  CA  . GLU A  1 97  ? 42.722  89.317 50.570  1.00 46.29 ? 97   GLU A CA  1 
ATOM   505   C  C   . GLU A  1 97  ? 42.687  88.959 49.102  1.00 45.59 ? 97   GLU A C   1 
ATOM   506   O  O   . GLU A  1 97  ? 42.337  89.789 48.251  1.00 45.91 ? 97   GLU A O   1 
ATOM   507   C  CB  . GLU A  1 97  ? 43.053  90.806 50.730  1.00 47.48 ? 97   GLU A CB  1 
ATOM   508   C  CG  . GLU A  1 97  ? 42.628  91.370 52.080  1.00 49.09 ? 97   GLU A CG  1 
ATOM   509   C  CD  . GLU A  1 97  ? 43.789  91.966 52.842  1.00 50.14 ? 97   GLU A CD  1 
ATOM   510   O  OE1 . GLU A  1 97  ? 43.684  92.084 54.085  1.00 51.03 ? 97   GLU A OE1 1 
ATOM   511   O  OE2 . GLU A  1 97  ? 44.807  92.321 52.197  1.00 50.42 ? 97   GLU A OE2 1 
ATOM   512   N  N   . PHE A  1 98  ? 43.044  87.714 48.809  1.00 44.32 ? 98   PHE A N   1 
ATOM   513   C  CA  . PHE A  1 98  ? 43.059  87.249 47.437  1.00 43.07 ? 98   PHE A CA  1 
ATOM   514   C  C   . PHE A  1 98  ? 41.651  87.300 46.849  1.00 42.81 ? 98   PHE A C   1 
ATOM   515   O  O   . PHE A  1 98  ? 41.475  87.492 45.640  1.00 42.81 ? 98   PHE A O   1 
ATOM   516   C  CB  . PHE A  1 98  ? 43.626  85.829 47.380  1.00 42.69 ? 98   PHE A CB  1 
ATOM   517   C  CG  . PHE A  1 98  ? 43.680  85.265 46.000  1.00 41.88 ? 98   PHE A CG  1 
ATOM   518   C  CD1 . PHE A  1 98  ? 44.379  85.928 44.998  1.00 41.73 ? 98   PHE A CD1 1 
ATOM   519   C  CD2 . PHE A  1 98  ? 43.011  84.081 45.691  1.00 41.64 ? 98   PHE A CD2 1 
ATOM   520   C  CE1 . PHE A  1 98  ? 44.410  85.420 43.700  1.00 41.93 ? 98   PHE A CE1 1 
ATOM   521   C  CE2 . PHE A  1 98  ? 43.032  83.560 44.398  1.00 40.65 ? 98   PHE A CE2 1 
ATOM   522   C  CZ  . PHE A  1 98  ? 43.732  84.229 43.399  1.00 41.59 ? 98   PHE A CZ  1 
ATOM   523   N  N   . GLY A  1 99  ? 40.650  87.124 47.709  1.00 42.12 ? 99   GLY A N   1 
ATOM   524   C  CA  . GLY A  1 99  ? 39.269  87.181 47.265  1.00 41.80 ? 99   GLY A CA  1 
ATOM   525   C  C   . GLY A  1 99  ? 38.686  85.867 46.785  1.00 41.84 ? 99   GLY A C   1 
ATOM   526   O  O   . GLY A  1 99  ? 37.476  85.750 46.558  1.00 42.58 ? 99   GLY A O   1 
ATOM   527   N  N   . HIS A  1 100 ? 39.541  84.867 46.628  1.00 41.51 ? 100  HIS A N   1 
ATOM   528   C  CA  . HIS A  1 100 ? 39.091  83.561 46.161  1.00 40.49 ? 100  HIS A CA  1 
ATOM   529   C  C   . HIS A  1 100 ? 39.637  82.475 47.054  1.00 39.93 ? 100  HIS A C   1 
ATOM   530   O  O   . HIS A  1 100 ? 40.726  82.604 47.616  1.00 39.97 ? 100  HIS A O   1 
ATOM   531   C  CB  . HIS A  1 100 ? 39.583  83.329 44.736  1.00 40.20 ? 100  HIS A CB  1 
ATOM   532   C  CG  . HIS A  1 100 ? 39.022  84.298 43.748  1.00 40.47 ? 100  HIS A CG  1 
ATOM   533   N  ND1 . HIS A  1 100 ? 37.683  84.331 43.425  1.00 40.19 ? 100  HIS A ND1 1 
ATOM   534   C  CD2 . HIS A  1 100 ? 39.612  85.279 43.024  1.00 40.29 ? 100  HIS A CD2 1 
ATOM   535   C  CE1 . HIS A  1 100 ? 37.470  85.293 42.543  1.00 40.52 ? 100  HIS A CE1 1 
ATOM   536   N  NE2 . HIS A  1 100 ? 38.624  85.884 42.283  1.00 40.28 ? 100  HIS A NE2 1 
ATOM   537   N  N   . SER A  1 101 ? 38.880  81.400 47.199  1.00 39.43 ? 101  SER A N   1 
ATOM   538   C  CA  . SER A  1 101 ? 39.361  80.290 48.004  1.00 38.77 ? 101  SER A CA  1 
ATOM   539   C  C   . SER A  1 101 ? 40.340  79.536 47.092  1.00 38.00 ? 101  SER A C   1 
ATOM   540   O  O   . SER A  1 101 ? 39.983  79.146 45.968  1.00 37.75 ? 101  SER A O   1 
ATOM   541   C  CB  . SER A  1 101 ? 38.199  79.394 48.420  1.00 39.35 ? 101  SER A CB  1 
ATOM   542   O  OG  . SER A  1 101 ? 38.623  78.528 49.456  1.00 40.77 ? 101  SER A OG  1 
ATOM   543   N  N   . ILE A  1 102 ? 41.573  79.357 47.558  1.00 36.62 ? 102  ILE A N   1 
ATOM   544   C  CA  . ILE A  1 102 ? 42.589  78.687 46.758  1.00 36.09 ? 102  ILE A CA  1 
ATOM   545   C  C   . ILE A  1 102 ? 42.499  77.173 46.908  1.00 35.62 ? 102  ILE A C   1 
ATOM   546   O  O   . ILE A  1 102 ? 42.638  76.631 48.007  1.00 35.76 ? 102  ILE A O   1 
ATOM   547   C  CB  . ILE A  1 102 ? 44.013  79.144 47.154  1.00 36.20 ? 102  ILE A CB  1 
ATOM   548   C  CG1 . ILE A  1 102 ? 44.084  80.671 47.192  1.00 36.02 ? 102  ILE A CG1 1 
ATOM   549   C  CG2 . ILE A  1 102 ? 45.030  78.648 46.137  1.00 35.54 ? 102  ILE A CG2 1 
ATOM   550   C  CD1 . ILE A  1 102 ? 45.395  81.173 47.753  1.00 36.94 ? 102  ILE A CD1 1 
ATOM   551   N  N   . ASN A  1 103 ? 42.284  76.499 45.785  1.00 35.02 ? 103  ASN A N   1 
ATOM   552   C  CA  . ASN A  1 103 ? 42.163  75.042 45.750  1.00 34.53 ? 103  ASN A CA  1 
ATOM   553   C  C   . ASN A  1 103 ? 43.508  74.344 45.856  1.00 34.31 ? 103  ASN A C   1 
ATOM   554   O  O   . ASN A  1 103 ? 43.659  73.356 46.572  1.00 34.49 ? 103  ASN A O   1 
ATOM   555   C  CB  . ASN A  1 103 ? 41.496  74.602 44.445  1.00 33.75 ? 103  ASN A CB  1 
ATOM   556   C  CG  . ASN A  1 103 ? 41.109  73.150 44.465  1.00 34.61 ? 103  ASN A CG  1 
ATOM   557   O  OD1 . ASN A  1 103 ? 40.279  72.737 45.275  1.00 35.79 ? 103  ASN A OD1 1 
ATOM   558   N  ND2 . ASN A  1 103 ? 41.713  72.358 43.587  1.00 33.29 ? 103  ASN A ND2 1 
ATOM   559   N  N   . ASP A  1 104 ? 44.492  74.849 45.129  1.00 33.90 ? 104  ASP A N   1 
ATOM   560   C  CA  . ASP A  1 104 ? 45.807  74.229 45.153  1.00 34.07 ? 104  ASP A CA  1 
ATOM   561   C  C   . ASP A  1 104 ? 46.829  75.238 44.638  1.00 33.60 ? 104  ASP A C   1 
ATOM   562   O  O   . ASP A  1 104 ? 46.465  76.320 44.166  1.00 32.54 ? 104  ASP A O   1 
ATOM   563   C  CB  . ASP A  1 104 ? 45.770  72.968 44.278  1.00 34.98 ? 104  ASP A CB  1 
ATOM   564   C  CG  . ASP A  1 104 ? 46.957  72.041 44.511  1.00 35.68 ? 104  ASP A CG  1 
ATOM   565   O  OD1 . ASP A  1 104 ? 47.715  72.224 45.494  1.00 36.26 ? 104  ASP A OD1 1 
ATOM   566   O  OD2 . ASP A  1 104 ? 47.124  71.114 43.698  1.00 36.80 ? 104  ASP A OD2 1 
ATOM   567   N  N   . TYR A  1 105 ? 48.102  74.887 44.744  1.00 33.64 ? 105  TYR A N   1 
ATOM   568   C  CA  . TYR A  1 105 ? 49.170  75.762 44.307  1.00 33.66 ? 105  TYR A CA  1 
ATOM   569   C  C   . TYR A  1 105 ? 50.203  74.931 43.578  1.00 33.54 ? 105  TYR A C   1 
ATOM   570   O  O   . TYR A  1 105 ? 50.299  73.728 43.783  1.00 33.61 ? 105  TYR A O   1 
ATOM   571   C  CB  . TYR A  1 105 ? 49.852  76.417 45.502  1.00 35.87 ? 105  TYR A CB  1 
ATOM   572   C  CG  . TYR A  1 105 ? 50.749  75.463 46.275  1.00 38.54 ? 105  TYR A CG  1 
ATOM   573   C  CD1 . TYR A  1 105 ? 50.259  74.717 47.352  1.00 39.82 ? 105  TYR A CD1 1 
ATOM   574   C  CD2 . TYR A  1 105 ? 52.094  75.295 45.916  1.00 39.38 ? 105  TYR A CD2 1 
ATOM   575   C  CE1 . TYR A  1 105 ? 51.096  73.827 48.063  1.00 40.49 ? 105  TYR A CE1 1 
ATOM   576   C  CE2 . TYR A  1 105 ? 52.932  74.413 46.608  1.00 40.20 ? 105  TYR A CE2 1 
ATOM   577   C  CZ  . TYR A  1 105 ? 52.428  73.684 47.683  1.00 41.31 ? 105  TYR A CZ  1 
ATOM   578   O  OH  . TYR A  1 105 ? 53.267  72.831 48.380  1.00 42.17 ? 105  TYR A OH  1 
ATOM   579   N  N   . SER A  1 106 ? 50.989  75.583 42.738  1.00 32.36 ? 106  SER A N   1 
ATOM   580   C  CA  . SER A  1 106 ? 52.034  74.902 42.001  1.00 31.99 ? 106  SER A CA  1 
ATOM   581   C  C   . SER A  1 106 ? 53.166  75.907 41.787  1.00 31.72 ? 106  SER A C   1 
ATOM   582   O  O   . SER A  1 106 ? 53.006  76.895 41.066  1.00 32.34 ? 106  SER A O   1 
ATOM   583   C  CB  . SER A  1 106 ? 51.491  74.413 40.660  1.00 31.19 ? 106  SER A CB  1 
ATOM   584   O  OG  . SER A  1 106 ? 52.552  73.954 39.852  1.00 32.71 ? 106  SER A OG  1 
ATOM   585   N  N   . ILE A  1 107 ? 54.301  75.667 42.426  1.00 31.36 ? 107  ILE A N   1 
ATOM   586   C  CA  . ILE A  1 107 ? 55.447  76.563 42.301  1.00 30.91 ? 107  ILE A CA  1 
ATOM   587   C  C   . ILE A  1 107 ? 56.287  76.188 41.086  1.00 30.31 ? 107  ILE A C   1 
ATOM   588   O  O   . ILE A  1 107 ? 56.501  75.005 40.807  1.00 30.01 ? 107  ILE A O   1 
ATOM   589   C  CB  . ILE A  1 107 ? 56.294  76.497 43.565  1.00 31.73 ? 107  ILE A CB  1 
ATOM   590   C  CG1 . ILE A  1 107 ? 55.432  76.948 44.745  1.00 32.42 ? 107  ILE A CG1 1 
ATOM   591   C  CG2 . ILE A  1 107 ? 57.545  77.354 43.415  1.00 31.70 ? 107  ILE A CG2 1 
ATOM   592   C  CD1 . ILE A  1 107 ? 56.022  76.634 46.098  1.00 34.08 ? 107  ILE A CD1 1 
ATOM   593   N  N   . SER A  1 108 ? 56.743  77.197 40.347  1.00 28.64 ? 108  SER A N   1 
ATOM   594   C  CA  . SER A  1 108 ? 57.538  76.944 39.161  1.00 27.42 ? 108  SER A CA  1 
ATOM   595   C  C   . SER A  1 108 ? 58.818  76.263 39.611  1.00 27.09 ? 108  SER A C   1 
ATOM   596   O  O   . SER A  1 108 ? 59.272  76.450 40.739  1.00 26.88 ? 108  SER A O   1 
ATOM   597   C  CB  . SER A  1 108 ? 57.856  78.254 38.437  1.00 26.15 ? 108  SER A CB  1 
ATOM   598   O  OG  . SER A  1 108 ? 58.696  79.059 39.240  1.00 26.87 ? 108  SER A OG  1 
ATOM   599   N  N   . PRO A  1 109 ? 59.418  75.457 38.728  1.00 27.38 ? 109  PRO A N   1 
ATOM   600   C  CA  . PRO A  1 109 ? 60.653  74.738 39.036  1.00 27.99 ? 109  PRO A CA  1 
ATOM   601   C  C   . PRO A  1 109 ? 61.755  75.647 39.571  1.00 28.91 ? 109  PRO A C   1 
ATOM   602   O  O   . PRO A  1 109 ? 62.495  75.250 40.477  1.00 28.95 ? 109  PRO A O   1 
ATOM   603   C  CB  . PRO A  1 109 ? 61.019  74.099 37.697  1.00 27.86 ? 109  PRO A CB  1 
ATOM   604   C  CG  . PRO A  1 109 ? 59.680  73.821 37.110  1.00 28.00 ? 109  PRO A CG  1 
ATOM   605   C  CD  . PRO A  1 109 ? 58.907  75.075 37.401  1.00 26.97 ? 109  PRO A CD  1 
ATOM   606   N  N   . ASP A  1 110 ? 61.878  76.856 39.027  1.00 29.15 ? 110  ASP A N   1 
ATOM   607   C  CA  . ASP A  1 110 ? 62.930  77.760 39.509  1.00 30.36 ? 110  ASP A CA  1 
ATOM   608   C  C   . ASP A  1 110 ? 62.579  78.510 40.787  1.00 31.11 ? 110  ASP A C   1 
ATOM   609   O  O   . ASP A  1 110 ? 63.360  79.325 41.264  1.00 32.14 ? 110  ASP A O   1 
ATOM   610   C  CB  . ASP A  1 110 ? 63.361  78.740 38.408  1.00 30.20 ? 110  ASP A CB  1 
ATOM   611   C  CG  . ASP A  1 110 ? 62.249  79.688 37.971  1.00 29.82 ? 110  ASP A CG  1 
ATOM   612   O  OD1 . ASP A  1 110 ? 62.378  80.257 36.869  1.00 29.10 ? 110  ASP A OD1 1 
ATOM   613   O  OD2 . ASP A  1 110 ? 61.269  79.875 38.716  1.00 29.96 ? 110  ASP A OD2 1 
ATOM   614   N  N   . GLY A  1 111 ? 61.413  78.208 41.354  1.00 31.73 ? 111  GLY A N   1 
ATOM   615   C  CA  . GLY A  1 111 ? 60.988  78.838 42.595  1.00 32.01 ? 111  GLY A CA  1 
ATOM   616   C  C   . GLY A  1 111 ? 60.595  80.307 42.511  1.00 33.00 ? 111  GLY A C   1 
ATOM   617   O  O   . GLY A  1 111 ? 60.224  80.909 43.522  1.00 32.21 ? 111  GLY A O   1 
ATOM   618   N  N   . GLN A  1 112 ? 60.640  80.875 41.308  1.00 32.75 ? 112  GLN A N   1 
ATOM   619   C  CA  . GLN A  1 112 ? 60.320  82.287 41.107  1.00 33.29 ? 112  GLN A CA  1 
ATOM   620   C  C   . GLN A  1 112 ? 58.840  82.642 41.095  1.00 33.08 ? 112  GLN A C   1 
ATOM   621   O  O   . GLN A  1 112 ? 58.453  83.772 41.437  1.00 33.14 ? 112  GLN A O   1 
ATOM   622   C  CB  . GLN A  1 112 ? 60.964  82.777 39.801  1.00 33.98 ? 112  GLN A CB  1 
ATOM   623   C  CG  . GLN A  1 112 ? 62.481  82.810 39.835  1.00 35.77 ? 112  GLN A CG  1 
ATOM   624   C  CD  . GLN A  1 112 ? 63.095  83.124 38.475  1.00 37.51 ? 112  GLN A CD  1 
ATOM   625   O  OE1 . GLN A  1 112 ? 62.508  83.857 37.665  1.00 37.61 ? 112  GLN A OE1 1 
ATOM   626   N  NE2 . GLN A  1 112 ? 64.287  82.578 38.220  1.00 37.65 ? 112  GLN A NE2 1 
ATOM   627   N  N   . PHE A  1 113 ? 58.008  81.679 40.712  1.00 31.76 ? 113  PHE A N   1 
ATOM   628   C  CA  . PHE A  1 113 ? 56.578  81.922 40.608  1.00 30.91 ? 113  PHE A CA  1 
ATOM   629   C  C   . PHE A  1 113 ? 55.691  80.838 41.225  1.00 31.04 ? 113  PHE A C   1 
ATOM   630   O  O   . PHE A  1 113 ? 56.088  79.680 41.360  1.00 30.01 ? 113  PHE A O   1 
ATOM   631   C  CB  . PHE A  1 113 ? 56.217  82.076 39.125  1.00 30.22 ? 113  PHE A CB  1 
ATOM   632   C  CG  . PHE A  1 113 ? 56.975  83.180 38.425  1.00 31.11 ? 113  PHE A CG  1 
ATOM   633   C  CD1 . PHE A  1 113 ? 56.637  84.518 38.630  1.00 31.23 ? 113  PHE A CD1 1 
ATOM   634   C  CD2 . PHE A  1 113 ? 58.020  82.884 37.555  1.00 30.19 ? 113  PHE A CD2 1 
ATOM   635   C  CE1 . PHE A  1 113 ? 57.325  85.541 37.973  1.00 31.10 ? 113  PHE A CE1 1 
ATOM   636   C  CE2 . PHE A  1 113 ? 58.714  83.898 36.896  1.00 31.77 ? 113  PHE A CE2 1 
ATOM   637   C  CZ  . PHE A  1 113 ? 58.364  85.232 37.105  1.00 30.11 ? 113  PHE A CZ  1 
ATOM   638   N  N   . ILE A  1 114 ? 54.484  81.221 41.604  1.00 30.38 ? 114  ILE A N   1 
ATOM   639   C  CA  . ILE A  1 114 ? 53.558  80.247 42.132  1.00 31.76 ? 114  ILE A CA  1 
ATOM   640   C  C   . ILE A  1 114 ? 52.220  80.434 41.436  1.00 32.08 ? 114  ILE A C   1 
ATOM   641   O  O   . ILE A  1 114 ? 51.713  81.546 41.327  1.00 32.87 ? 114  ILE A O   1 
ATOM   642   C  CB  . ILE A  1 114 ? 53.395  80.358 43.665  1.00 32.69 ? 114  ILE A CB  1 
ATOM   643   C  CG1 . ILE A  1 114 ? 52.381  79.308 44.147  1.00 32.77 ? 114  ILE A CG1 1 
ATOM   644   C  CG2 . ILE A  1 114 ? 52.983  81.765 44.063  1.00 33.22 ? 114  ILE A CG2 1 
ATOM   645   C  CD1 . ILE A  1 114 ? 52.212  79.276 45.656  1.00 33.94 ? 114  ILE A CD1 1 
ATOM   646   N  N   . LEU A  1 115 ? 51.676  79.330 40.939  1.00 31.75 ? 115  LEU A N   1 
ATOM   647   C  CA  . LEU A  1 115 ? 50.404  79.320 40.247  1.00 30.83 ? 115  LEU A CA  1 
ATOM   648   C  C   . LEU A  1 115 ? 49.332  79.060 41.298  1.00 30.97 ? 115  LEU A C   1 
ATOM   649   O  O   . LEU A  1 115 ? 49.451  78.131 42.097  1.00 31.94 ? 115  LEU A O   1 
ATOM   650   C  CB  . LEU A  1 115 ? 50.418  78.208 39.202  1.00 31.05 ? 115  LEU A CB  1 
ATOM   651   C  CG  . LEU A  1 115 ? 49.229  78.061 38.253  1.00 32.20 ? 115  LEU A CG  1 
ATOM   652   C  CD1 . LEU A  1 115 ? 49.127  79.243 37.310  1.00 30.21 ? 115  LEU A CD1 1 
ATOM   653   C  CD2 . LEU A  1 115 ? 49.420  76.785 37.463  1.00 32.61 ? 115  LEU A CD2 1 
ATOM   654   N  N   . LEU A  1 116 ? 48.298  79.892 41.313  1.00 30.00 ? 116  LEU A N   1 
ATOM   655   C  CA  . LEU A  1 116 ? 47.219  79.748 42.279  1.00 29.09 ? 116  LEU A CA  1 
ATOM   656   C  C   . LEU A  1 116 ? 45.973  79.225 41.575  1.00 28.80 ? 116  LEU A C   1 
ATOM   657   O  O   . LEU A  1 116 ? 45.430  79.872 40.677  1.00 28.41 ? 116  LEU A O   1 
ATOM   658   C  CB  . LEU A  1 116 ? 46.919  81.092 42.944  1.00 29.10 ? 116  LEU A CB  1 
ATOM   659   C  CG  . LEU A  1 116 ? 48.072  81.761 43.701  1.00 30.11 ? 116  LEU A CG  1 
ATOM   660   C  CD1 . LEU A  1 116 ? 47.509  82.939 44.500  1.00 30.36 ? 116  LEU A CD1 1 
ATOM   661   C  CD2 . LEU A  1 116 ? 48.745  80.766 44.645  1.00 29.51 ? 116  LEU A CD2 1 
ATOM   662   N  N   . GLU A  1 117 ? 45.526  78.051 42.001  1.00 27.79 ? 117  GLU A N   1 
ATOM   663   C  CA  . GLU A  1 117 ? 44.358  77.400 41.422  1.00 26.82 ? 117  GLU A CA  1 
ATOM   664   C  C   . GLU A  1 117 ? 43.117  77.644 42.265  1.00 26.68 ? 117  GLU A C   1 
ATOM   665   O  O   . GLU A  1 117 ? 43.127  77.390 43.472  1.00 26.54 ? 117  GLU A O   1 
ATOM   666   C  CB  . GLU A  1 117 ? 44.638  75.897 41.314  1.00 25.53 ? 117  GLU A CB  1 
ATOM   667   C  CG  . GLU A  1 117 ? 43.557  75.071 40.633  1.00 25.34 ? 117  GLU A CG  1 
ATOM   668   C  CD  . GLU A  1 117 ? 43.977  73.610 40.498  1.00 24.85 ? 117  GLU A CD  1 
ATOM   669   O  OE1 . GLU A  1 117 ? 44.719  73.274 39.554  1.00 23.89 ? 117  GLU A OE1 1 
ATOM   670   O  OE2 . GLU A  1 117 ? 43.576  72.817 41.363  1.00 25.67 ? 117  GLU A OE2 1 
ATOM   671   N  N   . TYR A  1 118 ? 42.057  78.138 41.623  1.00 26.51 ? 118  TYR A N   1 
ATOM   672   C  CA  . TYR A  1 118 ? 40.794  78.413 42.297  1.00 26.90 ? 118  TYR A CA  1 
ATOM   673   C  C   . TYR A  1 118 ? 39.627  78.216 41.336  1.00 26.90 ? 118  TYR A C   1 
ATOM   674   O  O   . TYR A  1 118 ? 39.835  77.975 40.150  1.00 26.93 ? 118  TYR A O   1 
ATOM   675   C  CB  . TYR A  1 118 ? 40.772  79.834 42.889  1.00 27.48 ? 118  TYR A CB  1 
ATOM   676   C  CG  . TYR A  1 118 ? 40.832  80.968 41.880  1.00 27.66 ? 118  TYR A CG  1 
ATOM   677   C  CD1 . TYR A  1 118 ? 42.009  81.264 41.192  1.00 28.39 ? 118  TYR A CD1 1 
ATOM   678   C  CD2 . TYR A  1 118 ? 39.713  81.762 41.639  1.00 28.37 ? 118  TYR A CD2 1 
ATOM   679   C  CE1 . TYR A  1 118 ? 42.064  82.330 40.298  1.00 28.49 ? 118  TYR A CE1 1 
ATOM   680   C  CE2 . TYR A  1 118 ? 39.754  82.823 40.752  1.00 28.56 ? 118  TYR A CE2 1 
ATOM   681   C  CZ  . TYR A  1 118 ? 40.932  83.106 40.089  1.00 29.42 ? 118  TYR A CZ  1 
ATOM   682   O  OH  . TYR A  1 118 ? 40.976  84.193 39.253  1.00 31.00 ? 118  TYR A OH  1 
ATOM   683   N  N   . ASN A  1 119 ? 38.405  78.328 41.847  1.00 27.03 ? 119  ASN A N   1 
ATOM   684   C  CA  . ASN A  1 119 ? 37.197  78.105 41.046  1.00 27.64 ? 119  ASN A CA  1 
ATOM   685   C  C   . ASN A  1 119 ? 37.268  76.702 40.424  1.00 27.48 ? 119  ASN A C   1 
ATOM   686   O  O   . ASN A  1 119 ? 36.921  76.492 39.256  1.00 26.55 ? 119  ASN A O   1 
ATOM   687   C  CB  . ASN A  1 119 ? 37.040  79.150 39.929  1.00 29.03 ? 119  ASN A CB  1 
ATOM   688   C  CG  . ASN A  1 119 ? 36.565  80.507 40.449  1.00 31.11 ? 119  ASN A CG  1 
ATOM   689   O  OD1 . ASN A  1 119 ? 35.900  80.603 41.495  1.00 30.69 ? 119  ASN A OD1 1 
ATOM   690   N  ND2 . ASN A  1 119 ? 36.889  81.561 39.704  1.00 30.75 ? 119  ASN A ND2 1 
ATOM   691   N  N   . TYR A  1 120 ? 37.736  75.751 41.219  1.00 26.49 ? 120  TYR A N   1 
ATOM   692   C  CA  . TYR A  1 120 ? 37.852  74.370 40.787  1.00 26.31 ? 120  TYR A CA  1 
ATOM   693   C  C   . TYR A  1 120 ? 36.483  73.737 40.512  1.00 25.66 ? 120  TYR A C   1 
ATOM   694   O  O   . TYR A  1 120 ? 35.576  73.803 41.343  1.00 24.64 ? 120  TYR A O   1 
ATOM   695   C  CB  . TYR A  1 120 ? 38.580  73.558 41.871  1.00 27.98 ? 120  TYR A CB  1 
ATOM   696   C  CG  . TYR A  1 120 ? 38.475  72.053 41.706  1.00 29.86 ? 120  TYR A CG  1 
ATOM   697   C  CD1 . TYR A  1 120 ? 39.492  71.314 41.101  1.00 30.22 ? 120  TYR A CD1 1 
ATOM   698   C  CD2 . TYR A  1 120 ? 37.356  71.369 42.177  1.00 31.04 ? 120  TYR A CD2 1 
ATOM   699   C  CE1 . TYR A  1 120 ? 39.392  69.927 40.978  1.00 31.29 ? 120  TYR A CE1 1 
ATOM   700   C  CE2 . TYR A  1 120 ? 37.246  70.003 42.059  1.00 32.25 ? 120  TYR A CE2 1 
ATOM   701   C  CZ  . TYR A  1 120 ? 38.262  69.284 41.464  1.00 31.26 ? 120  TYR A CZ  1 
ATOM   702   O  OH  . TYR A  1 120 ? 38.118  67.922 41.380  1.00 33.21 ? 120  TYR A OH  1 
ATOM   703   N  N   . VAL A  1 121 ? 36.341  73.115 39.350  1.00 24.23 ? 121  VAL A N   1 
ATOM   704   C  CA  . VAL A  1 121 ? 35.094  72.436 39.005  1.00 24.14 ? 121  VAL A CA  1 
ATOM   705   C  C   . VAL A  1 121 ? 35.450  71.054 38.458  1.00 22.79 ? 121  VAL A C   1 
ATOM   706   O  O   . VAL A  1 121 ? 36.003  70.936 37.370  1.00 22.47 ? 121  VAL A O   1 
ATOM   707   C  CB  . VAL A  1 121 ? 34.294  73.184 37.932  1.00 23.62 ? 121  VAL A CB  1 
ATOM   708   C  CG1 . VAL A  1 121 ? 33.004  72.406 37.643  1.00 24.54 ? 121  VAL A CG1 1 
ATOM   709   C  CG2 . VAL A  1 121 ? 33.966  74.612 38.417  1.00 25.24 ? 121  VAL A CG2 1 
ATOM   710   N  N   . LYS A  1 122 ? 35.131  70.014 39.217  1.00 21.93 ? 122  LYS A N   1 
ATOM   711   C  CA  . LYS A  1 122 ? 35.450  68.662 38.804  1.00 20.60 ? 122  LYS A CA  1 
ATOM   712   C  C   . LYS A  1 122 ? 34.749  68.174 37.537  1.00 19.69 ? 122  LYS A C   1 
ATOM   713   O  O   . LYS A  1 122 ? 33.594  68.524 37.264  1.00 17.33 ? 122  LYS A O   1 
ATOM   714   C  CB  . LYS A  1 122 ? 35.144  67.666 39.938  1.00 21.27 ? 122  LYS A CB  1 
ATOM   715   C  CG  . LYS A  1 122 ? 35.551  66.206 39.587  1.00 22.50 ? 122  LYS A CG  1 
ATOM   716   C  CD  . LYS A  1 122 ? 35.234  65.193 40.709  1.00 22.84 ? 122  LYS A CD  1 
ATOM   717   C  CE  . LYS A  1 122 ? 35.345  63.731 40.194  1.00 21.97 ? 122  LYS A CE  1 
ATOM   718   N  NZ  . LYS A  1 122 ? 34.333  63.433 39.129  1.00 20.67 ? 122  LYS A NZ  1 
ATOM   719   N  N   . GLN A  1 123 ? 35.468  67.400 36.728  1.00 18.56 ? 123  GLN A N   1 
ATOM   720   C  CA  . GLN A  1 123 ? 34.809  66.805 35.576  1.00 18.27 ? 123  GLN A CA  1 
ATOM   721   C  C   . GLN A  1 123 ? 34.827  65.287 35.812  1.00 16.88 ? 123  GLN A C   1 
ATOM   722   O  O   . GLN A  1 123 ? 34.075  64.802 36.661  1.00 15.83 ? 123  GLN A O   1 
ATOM   723   C  CB  . GLN A  1 123 ? 35.465  67.159 34.243  1.00 20.15 ? 123  GLN A CB  1 
ATOM   724   C  CG  . GLN A  1 123 ? 34.492  66.800 33.126  1.00 21.96 ? 123  GLN A CG  1 
ATOM   725   C  CD  . GLN A  1 123 ? 35.028  66.993 31.733  1.00 25.16 ? 123  GLN A CD  1 
ATOM   726   O  OE1 . GLN A  1 123 ? 34.265  66.988 30.759  1.00 26.00 ? 123  GLN A OE1 1 
ATOM   727   N  NE2 . GLN A  1 123 ? 36.341  67.146 31.618  1.00 25.79 ? 123  GLN A NE2 1 
ATOM   728   N  N   . TRP A  1 124 ? 35.687  64.540 35.120  1.00 15.69 ? 124  TRP A N   1 
ATOM   729   C  CA  . TRP A  1 124 ? 35.714  63.088 35.324  1.00 14.77 ? 124  TRP A CA  1 
ATOM   730   C  C   . TRP A  1 124 ? 36.650  62.654 36.463  1.00 16.05 ? 124  TRP A C   1 
ATOM   731   O  O   . TRP A  1 124 ? 36.783  63.368 37.463  1.00 16.57 ? 124  TRP A O   1 
ATOM   732   C  CB  . TRP A  1 124 ? 36.061  62.386 34.006  1.00 14.66 ? 124  TRP A CB  1 
ATOM   733   C  CG  . TRP A  1 124 ? 35.195  62.886 32.862  1.00 14.39 ? 124  TRP A CG  1 
ATOM   734   C  CD1 . TRP A  1 124 ? 35.622  63.306 31.627  1.00 14.08 ? 124  TRP A CD1 1 
ATOM   735   C  CD2 . TRP A  1 124 ? 33.769  63.074 32.881  1.00 14.07 ? 124  TRP A CD2 1 
ATOM   736   N  NE1 . TRP A  1 124 ? 34.542  63.750 30.879  1.00 15.65 ? 124  TRP A NE1 1 
ATOM   737   C  CE2 . TRP A  1 124 ? 33.398  63.617 31.624  1.00 15.73 ? 124  TRP A CE2 1 
ATOM   738   C  CE3 . TRP A  1 124 ? 32.770  62.841 33.840  1.00 14.61 ? 124  TRP A CE3 1 
ATOM   739   C  CZ2 . TRP A  1 124 ? 32.070  63.931 31.301  1.00 15.28 ? 124  TRP A CZ2 1 
ATOM   740   C  CZ3 . TRP A  1 124 ? 31.446  63.150 33.527  1.00 16.41 ? 124  TRP A CZ3 1 
ATOM   741   C  CH2 . TRP A  1 124 ? 31.107  63.692 32.262  1.00 16.40 ? 124  TRP A CH2 1 
ATOM   742   N  N   . ARG A  1 125 ? 37.285  61.490 36.340  1.00 15.90 ? 125  ARG A N   1 
ATOM   743   C  CA  . ARG A  1 125 ? 38.169  61.027 37.402  1.00 16.86 ? 125  ARG A CA  1 
ATOM   744   C  C   . ARG A  1 125 ? 39.403  61.916 37.610  1.00 17.93 ? 125  ARG A C   1 
ATOM   745   O  O   . ARG A  1 125 ? 39.803  62.166 38.752  1.00 17.55 ? 125  ARG A O   1 
ATOM   746   C  CB  . ARG A  1 125 ? 38.568  59.553 37.159  1.00 16.15 ? 125  ARG A CB  1 
ATOM   747   C  CG  . ARG A  1 125 ? 39.834  59.111 37.856  1.00 19.74 ? 125  ARG A CG  1 
ATOM   748   C  CD  . ARG A  1 125 ? 39.881  57.661 38.373  1.00 17.76 ? 125  ARG A CD  1 
ATOM   749   N  NE  . ARG A  1 125 ? 38.998  56.678 37.723  1.00 16.82 ? 125  ARG A NE  1 
ATOM   750   C  CZ  . ARG A  1 125 ? 38.368  55.726 38.418  1.00 16.46 ? 125  ARG A CZ  1 
ATOM   751   N  NH1 . ARG A  1 125 ? 38.541  55.681 39.736  1.00 12.93 ? 125  ARG A NH1 1 
ATOM   752   N  NH2 . ARG A  1 125 ? 37.591  54.822 37.826  1.00 13.68 ? 125  ARG A NH2 1 
ATOM   753   N  N   . HIS A  1 126 ? 39.998  62.411 36.526  1.00 17.51 ? 126  HIS A N   1 
ATOM   754   C  CA  . HIS A  1 126 ? 41.180  63.274 36.650  1.00 17.77 ? 126  HIS A CA  1 
ATOM   755   C  C   . HIS A  1 126 ? 40.915  64.716 36.153  1.00 17.19 ? 126  HIS A C   1 
ATOM   756   O  O   . HIS A  1 126 ? 41.514  65.676 36.647  1.00 16.51 ? 126  HIS A O   1 
ATOM   757   C  CB  . HIS A  1 126 ? 42.362  62.678 35.849  1.00 18.68 ? 126  HIS A CB  1 
ATOM   758   C  CG  . HIS A  1 126 ? 42.588  61.214 36.091  1.00 20.00 ? 126  HIS A CG  1 
ATOM   759   N  ND1 . HIS A  1 126 ? 43.129  60.723 37.263  1.00 20.09 ? 126  HIS A ND1 1 
ATOM   760   C  CD2 . HIS A  1 126 ? 42.309  60.131 35.325  1.00 20.53 ? 126  HIS A CD2 1 
ATOM   761   C  CE1 . HIS A  1 126 ? 43.171  59.403 37.209  1.00 21.37 ? 126  HIS A CE1 1 
ATOM   762   N  NE2 . HIS A  1 126 ? 42.677  59.017 36.044  1.00 20.73 ? 126  HIS A NE2 1 
ATOM   763   N  N   . SER A  1 127 ? 40.019  64.855 35.176  1.00 16.58 ? 127  SER A N   1 
ATOM   764   C  CA  . SER A  1 127 ? 39.720  66.165 34.595  1.00 17.93 ? 127  SER A CA  1 
ATOM   765   C  C   . SER A  1 127 ? 38.910  67.118 35.460  1.00 18.49 ? 127  SER A C   1 
ATOM   766   O  O   . SER A  1 127 ? 38.132  66.709 36.334  1.00 18.19 ? 127  SER A O   1 
ATOM   767   C  CB  . SER A  1 127 ? 39.022  66.008 33.236  1.00 17.75 ? 127  SER A CB  1 
ATOM   768   O  OG  . SER A  1 127 ? 37.895  65.149 33.317  1.00 13.62 ? 127  SER A OG  1 
ATOM   769   N  N   . TYR A  1 128 ? 39.133  68.399 35.194  1.00 18.98 ? 128  TYR A N   1 
ATOM   770   C  CA  . TYR A  1 128 ? 38.462  69.507 35.861  1.00 20.41 ? 128  TYR A CA  1 
ATOM   771   C  C   . TYR A  1 128 ? 38.921  70.818 35.225  1.00 21.81 ? 128  TYR A C   1 
ATOM   772   O  O   . TYR A  1 128 ? 39.943  70.861 34.538  1.00 20.99 ? 128  TYR A O   1 
ATOM   773   C  CB  . TYR A  1 128 ? 38.796  69.543 37.354  1.00 19.53 ? 128  TYR A CB  1 
ATOM   774   C  CG  . TYR A  1 128 ? 40.241  69.864 37.679  1.00 21.19 ? 128  TYR A CG  1 
ATOM   775   C  CD1 . TYR A  1 128 ? 40.713  71.185 37.673  1.00 21.40 ? 128  TYR A CD1 1 
ATOM   776   C  CD2 . TYR A  1 128 ? 41.132  68.849 38.031  1.00 21.36 ? 128  TYR A CD2 1 
ATOM   777   C  CE1 . TYR A  1 128 ? 42.031  71.483 38.021  1.00 21.26 ? 128  TYR A CE1 1 
ATOM   778   C  CE2 . TYR A  1 128 ? 42.450  69.131 38.378  1.00 22.07 ? 128  TYR A CE2 1 
ATOM   779   C  CZ  . TYR A  1 128 ? 42.895  70.447 38.376  1.00 22.86 ? 128  TYR A CZ  1 
ATOM   780   O  OH  . TYR A  1 128 ? 44.193  70.715 38.743  1.00 21.56 ? 128  TYR A OH  1 
ATOM   781   N  N   . THR A  1 129 ? 38.145  71.873 35.429  1.00 22.93 ? 129  THR A N   1 
ATOM   782   C  CA  . THR A  1 129 ? 38.532  73.185 34.926  1.00 24.39 ? 129  THR A CA  1 
ATOM   783   C  C   . THR A  1 129 ? 38.703  74.079 36.139  1.00 24.47 ? 129  THR A C   1 
ATOM   784   O  O   . THR A  1 129 ? 38.160  73.800 37.218  1.00 23.16 ? 129  THR A O   1 
ATOM   785   C  CB  . THR A  1 129 ? 37.462  73.824 34.035  1.00 25.71 ? 129  THR A CB  1 
ATOM   786   O  OG1 . THR A  1 129 ? 36.253  73.989 34.788  1.00 27.76 ? 129  THR A OG1 1 
ATOM   787   C  CG2 . THR A  1 129 ? 37.204  72.971 32.815  1.00 25.68 ? 129  THR A CG2 1 
ATOM   788   N  N   . ALA A  1 130 ? 39.472  75.146 35.966  1.00 25.33 ? 130  ALA A N   1 
ATOM   789   C  CA  . ALA A  1 130 ? 39.692  76.085 37.053  1.00 26.15 ? 130  ALA A CA  1 
ATOM   790   C  C   . ALA A  1 130 ? 40.227  77.413 36.545  1.00 27.04 ? 130  ALA A C   1 
ATOM   791   O  O   . ALA A  1 130 ? 40.575  77.557 35.365  1.00 27.58 ? 130  ALA A O   1 
ATOM   792   C  CB  . ALA A  1 130 ? 40.674  75.498 38.050  1.00 25.22 ? 130  ALA A CB  1 
ATOM   793   N  N   . SER A  1 131 ? 40.292  78.375 37.460  1.00 27.56 ? 131  SER A N   1 
ATOM   794   C  CA  . SER A  1 131 ? 40.825  79.692 37.162  1.00 27.71 ? 131  SER A CA  1 
ATOM   795   C  C   . SER A  1 131 ? 42.197  79.702 37.794  1.00 27.68 ? 131  SER A C   1 
ATOM   796   O  O   . SER A  1 131 ? 42.424  79.003 38.777  1.00 27.81 ? 131  SER A O   1 
ATOM   797   C  CB  . SER A  1 131 ? 39.947  80.772 37.781  1.00 28.17 ? 131  SER A CB  1 
ATOM   798   O  OG  . SER A  1 131 ? 38.687  80.776 37.137  1.00 28.97 ? 131  SER A OG  1 
ATOM   799   N  N   . TYR A  1 132 ? 43.112  80.479 37.220  1.00 28.27 ? 132  TYR A N   1 
ATOM   800   C  CA  . TYR A  1 132 ? 44.475  80.555 37.716  1.00 28.79 ? 132  TYR A CA  1 
ATOM   801   C  C   . TYR A  1 132 ? 45.013  81.986 37.775  1.00 29.85 ? 132  TYR A C   1 
ATOM   802   O  O   . TYR A  1 132 ? 44.630  82.846 36.990  1.00 29.26 ? 132  TYR A O   1 
ATOM   803   C  CB  . TYR A  1 132 ? 45.408  79.730 36.817  1.00 28.92 ? 132  TYR A CB  1 
ATOM   804   C  CG  . TYR A  1 132 ? 45.124  78.240 36.799  1.00 29.72 ? 132  TYR A CG  1 
ATOM   805   C  CD1 . TYR A  1 132 ? 44.205  77.685 35.904  1.00 28.74 ? 132  TYR A CD1 1 
ATOM   806   C  CD2 . TYR A  1 132 ? 45.736  77.392 37.725  1.00 29.21 ? 132  TYR A CD2 1 
ATOM   807   C  CE1 . TYR A  1 132 ? 43.898  76.312 35.940  1.00 29.74 ? 132  TYR A CE1 1 
ATOM   808   C  CE2 . TYR A  1 132 ? 45.435  76.030 37.775  1.00 29.32 ? 132  TYR A CE2 1 
ATOM   809   C  CZ  . TYR A  1 132 ? 44.515  75.496 36.887  1.00 29.16 ? 132  TYR A CZ  1 
ATOM   810   O  OH  . TYR A  1 132 ? 44.184  74.166 36.998  1.00 28.89 ? 132  TYR A OH  1 
ATOM   811   N  N   . ASP A  1 133 ? 45.918  82.221 38.713  1.00 30.69 ? 133  ASP A N   1 
ATOM   812   C  CA  . ASP A  1 133 ? 46.572  83.511 38.865  1.00 31.08 ? 133  ASP A CA  1 
ATOM   813   C  C   . ASP A  1 133 ? 48.013  83.133 39.144  1.00 31.59 ? 133  ASP A C   1 
ATOM   814   O  O   . ASP A  1 133 ? 48.294  82.033 39.648  1.00 31.61 ? 133  ASP A O   1 
ATOM   815   C  CB  . ASP A  1 133 ? 45.972  84.296 40.038  1.00 31.86 ? 133  ASP A CB  1 
ATOM   816   C  CG  . ASP A  1 133 ? 44.800  85.177 39.613  1.00 33.36 ? 133  ASP A CG  1 
ATOM   817   O  OD1 . ASP A  1 133 ? 43.903  85.426 40.441  1.00 35.11 ? 133  ASP A OD1 1 
ATOM   818   O  OD2 . ASP A  1 133 ? 44.783  85.630 38.451  1.00 34.00 ? 133  ASP A OD2 1 
ATOM   819   N  N   . ILE A  1 134 ? 48.929  84.020 38.792  1.00 31.41 ? 134  ILE A N   1 
ATOM   820   C  CA  . ILE A  1 134 ? 50.336  83.763 39.009  1.00 31.79 ? 134  ILE A CA  1 
ATOM   821   C  C   . ILE A  1 134 ? 50.852  84.851 39.923  1.00 33.37 ? 134  ILE A C   1 
ATOM   822   O  O   . ILE A  1 134 ? 50.610  86.038 39.691  1.00 33.81 ? 134  ILE A O   1 
ATOM   823   C  CB  . ILE A  1 134 ? 51.129  83.817 37.694  1.00 30.73 ? 134  ILE A CB  1 
ATOM   824   C  CG1 . ILE A  1 134 ? 50.494  82.881 36.670  1.00 29.47 ? 134  ILE A CG1 1 
ATOM   825   C  CG2 . ILE A  1 134 ? 52.597  83.498 37.962  1.00 28.93 ? 134  ILE A CG2 1 
ATOM   826   C  CD1 . ILE A  1 134 ? 51.037  83.052 35.270  1.00 29.88 ? 134  ILE A CD1 1 
ATOM   827   N  N   . TYR A  1 135 ? 51.561  84.435 40.961  1.00 34.01 ? 135  TYR A N   1 
ATOM   828   C  CA  . TYR A  1 135 ? 52.124  85.362 41.911  1.00 35.15 ? 135  TYR A CA  1 
ATOM   829   C  C   . TYR A  1 135 ? 53.642  85.340 41.752  1.00 36.42 ? 135  TYR A C   1 
ATOM   830   O  O   . TYR A  1 135 ? 54.264  84.270 41.751  1.00 35.96 ? 135  TYR A O   1 
ATOM   831   C  CB  . TYR A  1 135 ? 51.730  84.939 43.319  1.00 35.28 ? 135  TYR A CB  1 
ATOM   832   C  CG  . TYR A  1 135 ? 52.242  85.835 44.419  1.00 36.03 ? 135  TYR A CG  1 
ATOM   833   C  CD1 . TYR A  1 135 ? 51.624  87.051 44.705  1.00 34.94 ? 135  TYR A CD1 1 
ATOM   834   C  CD2 . TYR A  1 135 ? 53.337  85.447 45.198  1.00 36.20 ? 135  TYR A CD2 1 
ATOM   835   C  CE1 . TYR A  1 135 ? 52.081  87.855 45.740  1.00 36.53 ? 135  TYR A CE1 1 
ATOM   836   C  CE2 . TYR A  1 135 ? 53.803  86.244 46.235  1.00 36.97 ? 135  TYR A CE2 1 
ATOM   837   C  CZ  . TYR A  1 135 ? 53.171  87.448 46.503  1.00 37.21 ? 135  TYR A CZ  1 
ATOM   838   O  OH  . TYR A  1 135 ? 53.647  88.238 47.529  1.00 38.18 ? 135  TYR A OH  1 
ATOM   839   N  N   . ASP A  1 136 ? 54.228  86.524 41.580  1.00 37.40 ? 136  ASP A N   1 
ATOM   840   C  CA  . ASP A  1 136 ? 55.676  86.664 41.439  1.00 38.13 ? 136  ASP A CA  1 
ATOM   841   C  C   . ASP A  1 136 ? 56.270  86.638 42.849  1.00 39.06 ? 136  ASP A C   1 
ATOM   842   O  O   . ASP A  1 136 ? 55.953  87.493 43.678  1.00 39.39 ? 136  ASP A O   1 
ATOM   843   C  CB  . ASP A  1 136 ? 56.008  88.001 40.774  1.00 38.69 ? 136  ASP A CB  1 
ATOM   844   C  CG  . ASP A  1 136 ? 57.488  88.145 40.461  1.00 38.01 ? 136  ASP A CG  1 
ATOM   845   O  OD1 . ASP A  1 136 ? 58.324  87.990 41.378  1.00 36.70 ? 136  ASP A OD1 1 
ATOM   846   O  OD2 . ASP A  1 136 ? 57.810  88.417 39.285  1.00 40.20 ? 136  ASP A OD2 1 
ATOM   847   N  N   . LEU A  1 137 ? 57.129  85.668 43.130  1.00 39.82 ? 137  LEU A N   1 
ATOM   848   C  CA  . LEU A  1 137 ? 57.708  85.572 44.464  1.00 41.14 ? 137  LEU A CA  1 
ATOM   849   C  C   . LEU A  1 137 ? 58.885  86.514 44.690  1.00 42.86 ? 137  LEU A C   1 
ATOM   850   O  O   . LEU A  1 137 ? 59.254  86.804 45.830  1.00 43.46 ? 137  LEU A O   1 
ATOM   851   C  CB  . LEU A  1 137 ? 58.133  84.131 44.736  1.00 40.69 ? 137  LEU A CB  1 
ATOM   852   C  CG  . LEU A  1 137 ? 56.991  83.129 44.960  1.00 40.71 ? 137  LEU A CG  1 
ATOM   853   C  CD1 . LEU A  1 137 ? 57.347  81.776 44.366  1.00 40.60 ? 137  LEU A CD1 1 
ATOM   854   C  CD2 . LEU A  1 137 ? 56.719  83.010 46.454  1.00 41.67 ? 137  LEU A CD2 1 
ATOM   855   N  N   . ASN A  1 138 ? 59.469  87.012 43.610  1.00 44.03 ? 138  ASN A N   1 
ATOM   856   C  CA  . ASN A  1 138 ? 60.613  87.899 43.754  1.00 45.40 ? 138  ASN A CA  1 
ATOM   857   C  C   . ASN A  1 138 ? 60.155  89.302 44.085  1.00 45.82 ? 138  ASN A C   1 
ATOM   858   O  O   . ASN A  1 138 ? 60.660  89.914 45.027  1.00 47.11 ? 138  ASN A O   1 
ATOM   859   C  CB  . ASN A  1 138 ? 61.448  87.876 42.476  1.00 45.90 ? 138  ASN A CB  1 
ATOM   860   C  CG  . ASN A  1 138 ? 61.899  86.471 42.116  1.00 46.69 ? 138  ASN A CG  1 
ATOM   861   O  OD1 . ASN A  1 138 ? 62.529  85.787 42.933  1.00 45.91 ? 138  ASN A OD1 1 
ATOM   862   N  ND2 . ASN A  1 138 ? 61.571  86.027 40.893  1.00 46.69 ? 138  ASN A ND2 1 
ATOM   863   N  N   . LYS A  1 139 ? 59.186  89.801 43.326  1.00 46.00 ? 139  LYS A N   1 
ATOM   864   C  CA  . LYS A  1 139 ? 58.653  91.132 43.556  1.00 45.71 ? 139  LYS A CA  1 
ATOM   865   C  C   . LYS A  1 139 ? 57.412  91.067 44.455  1.00 46.19 ? 139  LYS A C   1 
ATOM   866   O  O   . LYS A  1 139 ? 56.687  92.061 44.602  1.00 46.56 ? 139  LYS A O   1 
ATOM   867   C  CB  . LYS A  1 139 ? 58.300  91.796 42.224  1.00 45.33 ? 139  LYS A CB  1 
ATOM   868   C  CG  . LYS A  1 139 ? 57.188  91.109 41.462  1.00 46.15 ? 139  LYS A CG  1 
ATOM   869   C  CD  . LYS A  1 139 ? 56.808  91.841 40.177  1.00 45.96 ? 139  LYS A CD  1 
ATOM   870   C  CE  . LYS A  1 139 ? 58.016  92.117 39.274  1.00 46.67 ? 139  LYS A CE  1 
ATOM   871   N  NZ  . LYS A  1 139 ? 58.744  90.895 38.807  1.00 47.70 ? 139  LYS A NZ  1 
ATOM   872   N  N   . ARG A  1 140 ? 57.168  89.901 45.054  1.00 45.77 ? 140  ARG A N   1 
ATOM   873   C  CA  . ARG A  1 140 ? 56.018  89.718 45.938  1.00 45.93 ? 140  ARG A CA  1 
ATOM   874   C  C   . ARG A  1 140 ? 54.771  90.412 45.388  1.00 45.49 ? 140  ARG A C   1 
ATOM   875   O  O   . ARG A  1 140 ? 54.110  91.178 46.095  1.00 45.80 ? 140  ARG A O   1 
ATOM   876   C  CB  . ARG A  1 140 ? 56.316  90.276 47.333  1.00 46.52 ? 140  ARG A CB  1 
ATOM   877   C  CG  . ARG A  1 140 ? 57.525  89.654 48.040  1.00 48.26 ? 140  ARG A CG  1 
ATOM   878   C  CD  . ARG A  1 140 ? 57.355  88.161 48.289  1.00 49.56 ? 140  ARG A CD  1 
ATOM   879   N  NE  . ARG A  1 140 ? 56.151  87.862 49.069  1.00 51.17 ? 140  ARG A NE  1 
ATOM   880   C  CZ  . ARG A  1 140 ? 55.871  86.668 49.591  1.00 51.27 ? 140  ARG A CZ  1 
ATOM   881   N  NH1 . ARG A  1 140 ? 56.715  85.651 49.414  1.00 51.00 ? 140  ARG A NH1 1 
ATOM   882   N  NH2 . ARG A  1 140 ? 54.753  86.494 50.295  1.00 51.19 ? 140  ARG A NH2 1 
ATOM   883   N  N   . GLN A  1 141 ? 54.439  90.131 44.135  1.00 44.49 ? 141  GLN A N   1 
ATOM   884   C  CA  . GLN A  1 141 ? 53.288  90.766 43.502  1.00 43.97 ? 141  GLN A CA  1 
ATOM   885   C  C   . GLN A  1 141 ? 52.479  89.811 42.613  1.00 42.88 ? 141  GLN A C   1 
ATOM   886   O  O   . GLN A  1 141 ? 53.027  88.898 41.990  1.00 42.24 ? 141  GLN A O   1 
ATOM   887   C  CB  . GLN A  1 141 ? 53.784  91.979 42.689  1.00 45.07 ? 141  GLN A CB  1 
ATOM   888   C  CG  . GLN A  1 141 ? 52.795  92.542 41.676  1.00 46.35 ? 141  GLN A CG  1 
ATOM   889   C  CD  . GLN A  1 141 ? 53.390  93.686 40.853  1.00 47.87 ? 141  GLN A CD  1 
ATOM   890   O  OE1 . GLN A  1 141 ? 53.408  94.847 41.293  1.00 47.96 ? 141  GLN A OE1 1 
ATOM   891   N  NE2 . GLN A  1 141 ? 53.893  93.358 39.657  1.00 47.23 ? 141  GLN A NE2 1 
ATOM   892   N  N   . LEU A  1 142 ? 51.171  90.031 42.569  1.00 41.70 ? 142  LEU A N   1 
ATOM   893   C  CA  . LEU A  1 142 ? 50.281  89.223 41.755  1.00 41.15 ? 142  LEU A CA  1 
ATOM   894   C  C   . LEU A  1 142 ? 50.380  89.766 40.325  1.00 40.96 ? 142  LEU A C   1 
ATOM   895   O  O   . LEU A  1 142 ? 50.457  90.981 40.125  1.00 40.99 ? 142  LEU A O   1 
ATOM   896   C  CB  . LEU A  1 142 ? 48.847  89.366 42.267  1.00 40.72 ? 142  LEU A CB  1 
ATOM   897   C  CG  . LEU A  1 142 ? 47.891  88.170 42.161  1.00 41.83 ? 142  LEU A CG  1 
ATOM   898   C  CD1 . LEU A  1 142 ? 48.352  87.029 43.093  1.00 40.47 ? 142  LEU A CD1 1 
ATOM   899   C  CD2 . LEU A  1 142 ? 46.490  88.627 42.533  1.00 40.87 ? 142  LEU A CD2 1 
ATOM   900   N  N   . ILE A  1 143 ? 50.381  88.878 39.335  1.00 40.25 ? 143  ILE A N   1 
ATOM   901   C  CA  . ILE A  1 143 ? 50.469  89.301 37.942  1.00 38.57 ? 143  ILE A CA  1 
ATOM   902   C  C   . ILE A  1 143 ? 49.073  89.578 37.402  1.00 38.82 ? 143  ILE A C   1 
ATOM   903   O  O   . ILE A  1 143 ? 48.180  88.736 37.510  1.00 37.47 ? 143  ILE A O   1 
ATOM   904   C  CB  . ILE A  1 143 ? 51.152  88.224 37.102  1.00 39.07 ? 143  ILE A CB  1 
ATOM   905   C  CG1 . ILE A  1 143 ? 52.569  88.009 37.632  1.00 39.30 ? 143  ILE A CG1 1 
ATOM   906   C  CG2 . ILE A  1 143 ? 51.192  88.633 35.644  1.00 38.30 ? 143  ILE A CG2 1 
ATOM   907   C  CD1 . ILE A  1 143 ? 53.368  86.972 36.868  1.00 39.20 ? 143  ILE A CD1 1 
ATOM   908   N  N   . THR A  1 144 ? 48.886  90.770 36.829  1.00 38.88 ? 144  THR A N   1 
ATOM   909   C  CA  . THR A  1 144 ? 47.587  91.179 36.302  1.00 38.65 ? 144  THR A CA  1 
ATOM   910   C  C   . THR A  1 144 ? 47.519  91.298 34.793  1.00 38.73 ? 144  THR A C   1 
ATOM   911   O  O   . THR A  1 144 ? 46.438  91.457 34.231  1.00 39.32 ? 144  THR A O   1 
ATOM   912   C  CB  . THR A  1 144 ? 47.158  92.534 36.892  1.00 39.22 ? 144  THR A CB  1 
ATOM   913   O  OG1 . THR A  1 144 ? 48.237  93.472 36.757  1.00 39.51 ? 144  THR A OG1 1 
ATOM   914   C  CG2 . THR A  1 144 ? 46.786  92.385 38.363  1.00 38.54 ? 144  THR A CG2 1 
ATOM   915   N  N   . GLU A  1 145 ? 48.663  91.221 34.133  1.00 38.79 ? 145  GLU A N   1 
ATOM   916   C  CA  . GLU A  1 145 ? 48.695  91.323 32.681  1.00 39.44 ? 145  GLU A CA  1 
ATOM   917   C  C   . GLU A  1 145 ? 48.755  89.944 32.009  1.00 38.83 ? 145  GLU A C   1 
ATOM   918   O  O   . GLU A  1 145 ? 49.468  89.048 32.464  1.00 38.17 ? 145  GLU A O   1 
ATOM   919   C  CB  . GLU A  1 145 ? 49.910  92.158 32.250  1.00 41.29 ? 145  GLU A CB  1 
ATOM   920   C  CG  . GLU A  1 145 ? 50.112  93.441 33.077  1.00 44.94 ? 145  GLU A CG  1 
ATOM   921   C  CD  . GLU A  1 145 ? 51.343  94.241 32.666  1.00 47.51 ? 145  GLU A CD  1 
ATOM   922   O  OE1 . GLU A  1 145 ? 51.739  95.174 33.415  1.00 49.62 ? 145  GLU A OE1 1 
ATOM   923   O  OE2 . GLU A  1 145 ? 51.920  93.948 31.588  1.00 49.03 ? 145  GLU A OE2 1 
ATOM   924   N  N   . GLU A  1 146 ? 47.994  89.776 30.933  1.00 37.96 ? 146  GLU A N   1 
ATOM   925   C  CA  . GLU A  1 146 ? 47.999  88.524 30.191  1.00 37.76 ? 146  GLU A CA  1 
ATOM   926   C  C   . GLU A  1 146 ? 47.770  87.295 31.084  1.00 37.12 ? 146  GLU A C   1 
ATOM   927   O  O   . GLU A  1 146 ? 48.503  86.316 30.994  1.00 37.10 ? 146  GLU A O   1 
ATOM   928   C  CB  . GLU A  1 146 ? 49.340  88.369 29.458  1.00 37.57 ? 146  GLU A CB  1 
ATOM   929   C  CG  . GLU A  1 146 ? 49.681  89.502 28.480  1.00 38.78 ? 146  GLU A CG  1 
ATOM   930   C  CD  . GLU A  1 146 ? 48.675  89.623 27.362  1.00 39.08 ? 146  GLU A CD  1 
ATOM   931   O  OE1 . GLU A  1 146 ? 48.357  88.601 26.724  1.00 40.06 ? 146  GLU A OE1 1 
ATOM   932   O  OE2 . GLU A  1 146 ? 48.199  90.744 27.110  1.00 41.16 ? 146  GLU A OE2 1 
ATOM   933   N  N   . ARG A  1 147 ? 46.764  87.338 31.946  1.00 36.60 ? 147  ARG A N   1 
ATOM   934   C  CA  . ARG A  1 147 ? 46.513  86.208 32.826  1.00 36.72 ? 147  ARG A CA  1 
ATOM   935   C  C   . ARG A  1 147 ? 45.829  85.028 32.155  1.00 34.99 ? 147  ARG A C   1 
ATOM   936   O  O   . ARG A  1 147 ? 45.119  85.167 31.158  1.00 34.17 ? 147  ARG A O   1 
ATOM   937   C  CB  . ARG A  1 147 ? 45.699  86.647 34.042  1.00 39.42 ? 147  ARG A CB  1 
ATOM   938   C  CG  . ARG A  1 147 ? 44.982  87.940 33.849  1.00 42.72 ? 147  ARG A CG  1 
ATOM   939   C  CD  . ARG A  1 147 ? 44.089  88.233 35.016  1.00 45.68 ? 147  ARG A CD  1 
ATOM   940   N  NE  . ARG A  1 147 ? 44.810  88.117 36.274  1.00 48.41 ? 147  ARG A NE  1 
ATOM   941   C  CZ  . ARG A  1 147 ? 44.400  88.674 37.407  1.00 50.19 ? 147  ARG A CZ  1 
ATOM   942   N  NH1 . ARG A  1 147 ? 43.276  89.384 37.420  1.00 50.58 ? 147  ARG A NH1 1 
ATOM   943   N  NH2 . ARG A  1 147 ? 45.111  88.525 38.521  1.00 51.19 ? 147  ARG A NH2 1 
ATOM   944   N  N   . ILE A  1 148 ? 46.074  83.854 32.713  1.00 33.62 ? 148  ILE A N   1 
ATOM   945   C  CA  . ILE A  1 148 ? 45.488  82.622 32.213  1.00 31.76 ? 148  ILE A CA  1 
ATOM   946   C  C   . ILE A  1 148 ? 43.968  82.789 32.195  1.00 30.87 ? 148  ILE A C   1 
ATOM   947   O  O   . ILE A  1 148 ? 43.384  83.263 33.161  1.00 29.70 ? 148  ILE A O   1 
ATOM   948   C  CB  . ILE A  1 148 ? 45.902  81.457 33.132  1.00 31.69 ? 148  ILE A CB  1 
ATOM   949   C  CG1 . ILE A  1 148 ? 47.424  81.273 33.050  1.00 31.19 ? 148  ILE A CG1 1 
ATOM   950   C  CG2 . ILE A  1 148 ? 45.156  80.191 32.749  1.00 31.74 ? 148  ILE A CG2 1 
ATOM   951   C  CD1 . ILE A  1 148 ? 48.023  80.470 34.192  1.00 32.20 ? 148  ILE A CD1 1 
ATOM   952   N  N   . PRO A  1 149 ? 43.313  82.395 31.091  1.00 30.67 ? 149  PRO A N   1 
ATOM   953   C  CA  . PRO A  1 149 ? 41.859  82.513 30.958  1.00 30.95 ? 149  PRO A CA  1 
ATOM   954   C  C   . PRO A  1 149 ? 41.111  81.725 32.034  1.00 32.00 ? 149  PRO A C   1 
ATOM   955   O  O   . PRO A  1 149 ? 41.697  80.880 32.726  1.00 32.03 ? 149  PRO A O   1 
ATOM   956   C  CB  . PRO A  1 149 ? 41.581  81.944 29.563  1.00 31.64 ? 149  PRO A CB  1 
ATOM   957   C  CG  . PRO A  1 149 ? 42.932  81.980 28.860  1.00 31.92 ? 149  PRO A CG  1 
ATOM   958   C  CD  . PRO A  1 149 ? 43.885  81.659 29.954  1.00 30.63 ? 149  PRO A CD  1 
ATOM   959   N  N   . ASN A  1 150 ? 39.822  82.017 32.186  1.00 32.61 ? 150  ASN A N   1 
ATOM   960   C  CA  . ASN A  1 150 ? 38.985  81.301 33.150  1.00 32.93 ? 150  ASN A CA  1 
ATOM   961   C  C   . ASN A  1 150 ? 38.545  80.029 32.438  1.00 31.21 ? 150  ASN A C   1 
ATOM   962   O  O   . ASN A  1 150 ? 38.566  79.960 31.208  1.00 30.65 ? 150  ASN A O   1 
ATOM   963   C  CB  . ASN A  1 150 ? 37.765  82.145 33.547  1.00 36.27 ? 150  ASN A CB  1 
ATOM   964   C  CG  . ASN A  1 150 ? 38.049  83.057 34.737  1.00 40.35 ? 150  ASN A CG  1 
ATOM   965   O  OD1 . ASN A  1 150 ? 38.209  82.580 35.857  1.00 41.93 ? 150  ASN A OD1 1 
ATOM   966   N  ND2 . ASN A  1 150 ? 38.147  84.362 34.518  1.00 44.31 ? 150  ASN A ND2 1 
ATOM   967   N  N   . ASN A  1 151 ? 38.159  79.013 33.193  1.00 29.40 ? 151  ASN A N   1 
ATOM   968   C  CA  . ASN A  1 151 ? 37.736  77.767 32.556  1.00 27.90 ? 151  ASN A CA  1 
ATOM   969   C  C   . ASN A  1 151 ? 38.898  77.090 31.824  1.00 25.39 ? 151  ASN A C   1 
ATOM   970   O  O   . ASN A  1 151 ? 38.706  76.448 30.789  1.00 24.71 ? 151  ASN A O   1 
ATOM   971   C  CB  . ASN A  1 151 ? 36.601  78.038 31.573  1.00 29.04 ? 151  ASN A CB  1 
ATOM   972   C  CG  . ASN A  1 151 ? 35.465  78.792 32.215  1.00 31.55 ? 151  ASN A CG  1 
ATOM   973   O  OD1 . ASN A  1 151 ? 34.819  78.298 33.159  1.00 31.79 ? 151  ASN A OD1 1 
ATOM   974   N  ND2 . ASN A  1 151 ? 35.219  80.010 31.727  1.00 31.98 ? 151  ASN A ND2 1 
ATOM   975   N  N   . THR A  1 152 ? 40.103  77.250 32.354  1.00 23.66 ? 152  THR A N   1 
ATOM   976   C  CA  . THR A  1 152 ? 41.274  76.609 31.760  1.00 23.09 ? 152  THR A CA  1 
ATOM   977   C  C   . THR A  1 152 ? 41.166  75.120 32.098  1.00 22.10 ? 152  THR A C   1 
ATOM   978   O  O   . THR A  1 152 ? 40.813  74.762 33.224  1.00 21.41 ? 152  THR A O   1 
ATOM   979   C  CB  . THR A  1 152 ? 42.559  77.226 32.320  1.00 23.58 ? 152  THR A CB  1 
ATOM   980   O  OG1 . THR A  1 152 ? 42.717  78.528 31.742  1.00 25.52 ? 152  THR A OG1 1 
ATOM   981   C  CG2 . THR A  1 152 ? 43.779  76.365 31.992  1.00 23.10 ? 152  THR A CG2 1 
ATOM   982   N  N   . GLN A  1 153 ? 41.455  74.267 31.121  1.00 21.14 ? 153  GLN A N   1 
ATOM   983   C  CA  . GLN A  1 153 ? 41.319  72.823 31.287  1.00 21.62 ? 153  GLN A CA  1 
ATOM   984   C  C   . GLN A  1 153 ? 42.539  72.110 31.853  1.00 22.26 ? 153  GLN A C   1 
ATOM   985   O  O   . GLN A  1 153 ? 42.429  71.059 32.476  1.00 21.50 ? 153  GLN A O   1 
ATOM   986   C  CB  . GLN A  1 153 ? 40.904  72.208 29.942  1.00 20.59 ? 153  GLN A CB  1 
ATOM   987   C  CG  . GLN A  1 153 ? 39.546  72.747 29.455  1.00 22.19 ? 153  GLN A CG  1 
ATOM   988   C  CD  . GLN A  1 153 ? 39.319  72.558 27.961  1.00 23.60 ? 153  GLN A CD  1 
ATOM   989   O  OE1 . GLN A  1 153 ? 40.041  73.121 27.145  1.00 23.11 ? 153  GLN A OE1 1 
ATOM   990   N  NE2 . GLN A  1 153 ? 38.314  71.765 27.600  1.00 22.20 ? 153  GLN A NE2 1 
ATOM   991   N  N   . TRP A  1 154 ? 43.707  72.691 31.642  1.00 22.04 ? 154  TRP A N   1 
ATOM   992   C  CA  . TRP A  1 154 ? 44.934  72.096 32.138  1.00 22.46 ? 154  TRP A CA  1 
ATOM   993   C  C   . TRP A  1 154 ? 46.052  73.115 32.010  1.00 22.02 ? 154  TRP A C   1 
ATOM   994   O  O   . TRP A  1 154 ? 46.122  73.852 31.034  1.00 20.31 ? 154  TRP A O   1 
ATOM   995   C  CB  . TRP A  1 154 ? 45.304  70.863 31.314  1.00 22.11 ? 154  TRP A CB  1 
ATOM   996   C  CG  . TRP A  1 154 ? 46.612  70.276 31.728  1.00 24.24 ? 154  TRP A CG  1 
ATOM   997   C  CD1 . TRP A  1 154 ? 47.802  70.348 31.051  1.00 25.03 ? 154  TRP A CD1 1 
ATOM   998   C  CD2 . TRP A  1 154 ? 46.895  69.615 32.966  1.00 25.14 ? 154  TRP A CD2 1 
ATOM   999   N  NE1 . TRP A  1 154 ? 48.807  69.780 31.801  1.00 25.66 ? 154  TRP A NE1 1 
ATOM   1000  C  CE2 . TRP A  1 154 ? 48.278  69.325 32.980  1.00 25.47 ? 154  TRP A CE2 1 
ATOM   1001  C  CE3 . TRP A  1 154 ? 46.113  69.247 34.071  1.00 25.38 ? 154  TRP A CE3 1 
ATOM   1002  C  CZ2 . TRP A  1 154 ? 48.896  68.683 34.058  1.00 25.72 ? 154  TRP A CZ2 1 
ATOM   1003  C  CZ3 . TRP A  1 154 ? 46.725  68.612 35.138  1.00 25.66 ? 154  TRP A CZ3 1 
ATOM   1004  C  CH2 . TRP A  1 154 ? 48.104  68.337 35.124  1.00 25.72 ? 154  TRP A CH2 1 
ATOM   1005  N  N   . VAL A  1 155 ? 46.927  73.152 33.002  1.00 22.62 ? 155  VAL A N   1 
ATOM   1006  C  CA  . VAL A  1 155 ? 48.062  74.051 32.951  1.00 23.12 ? 155  VAL A CA  1 
ATOM   1007  C  C   . VAL A  1 155 ? 49.242  73.306 33.545  1.00 23.96 ? 155  VAL A C   1 
ATOM   1008  O  O   . VAL A  1 155 ? 49.060  72.412 34.376  1.00 23.17 ? 155  VAL A O   1 
ATOM   1009  C  CB  . VAL A  1 155 ? 47.803  75.346 33.752  1.00 23.25 ? 155  VAL A CB  1 
ATOM   1010  C  CG1 . VAL A  1 155 ? 47.494  74.999 35.208  1.00 23.78 ? 155  VAL A CG1 1 
ATOM   1011  C  CG2 . VAL A  1 155 ? 49.029  76.274 33.658  1.00 22.69 ? 155  VAL A CG2 1 
ATOM   1012  N  N   . THR A  1 156 ? 50.448  73.650 33.094  1.00 24.54 ? 156  THR A N   1 
ATOM   1013  C  CA  . THR A  1 156 ? 51.656  73.016 33.606  1.00 24.64 ? 156  THR A CA  1 
ATOM   1014  C  C   . THR A  1 156 ? 52.908  73.825 33.311  1.00 24.96 ? 156  THR A C   1 
ATOM   1015  O  O   . THR A  1 156 ? 53.091  74.317 32.194  1.00 25.62 ? 156  THR A O   1 
ATOM   1016  C  CB  . THR A  1 156 ? 51.850  71.610 33.002  1.00 26.25 ? 156  THR A CB  1 
ATOM   1017  O  OG1 . THR A  1 156 ? 53.151  71.123 33.345  1.00 27.68 ? 156  THR A OG1 1 
ATOM   1018  C  CG2 . THR A  1 156 ? 51.737  71.653 31.492  1.00 26.47 ? 156  THR A CG2 1 
ATOM   1019  N  N   . TRP A  1 157 ? 53.765  73.956 34.317  1.00 24.11 ? 157  TRP A N   1 
ATOM   1020  C  CA  . TRP A  1 157 ? 55.031  74.662 34.169  1.00 25.00 ? 157  TRP A CA  1 
ATOM   1021  C  C   . TRP A  1 157 ? 55.929  73.768 33.312  1.00 24.52 ? 157  TRP A C   1 
ATOM   1022  O  O   . TRP A  1 157 ? 55.680  72.568 33.204  1.00 23.69 ? 157  TRP A O   1 
ATOM   1023  C  CB  . TRP A  1 157 ? 55.724  74.844 35.527  1.00 24.43 ? 157  TRP A CB  1 
ATOM   1024  C  CG  . TRP A  1 157 ? 55.099  75.823 36.464  1.00 26.65 ? 157  TRP A CG  1 
ATOM   1025  C  CD1 . TRP A  1 157 ? 54.427  75.539 37.625  1.00 26.10 ? 157  TRP A CD1 1 
ATOM   1026  C  CD2 . TRP A  1 157 ? 55.089  77.257 36.338  1.00 26.32 ? 157  TRP A CD2 1 
ATOM   1027  N  NE1 . TRP A  1 157 ? 54.002  76.701 38.221  1.00 26.63 ? 157  TRP A NE1 1 
ATOM   1028  C  CE2 . TRP A  1 157 ? 54.394  77.770 37.455  1.00 27.00 ? 157  TRP A CE2 1 
ATOM   1029  C  CE3 . TRP A  1 157 ? 55.601  78.155 35.392  1.00 26.64 ? 157  TRP A CE3 1 
ATOM   1030  C  CZ2 . TRP A  1 157 ? 54.195  79.148 37.650  1.00 26.96 ? 157  TRP A CZ2 1 
ATOM   1031  C  CZ3 . TRP A  1 157 ? 55.405  79.521 35.586  1.00 26.21 ? 157  TRP A CZ3 1 
ATOM   1032  C  CH2 . TRP A  1 157 ? 54.709  80.004 36.706  1.00 25.39 ? 157  TRP A CH2 1 
ATOM   1033  N  N   . SER A  1 158 ? 56.959  74.350 32.699  1.00 24.02 ? 158  SER A N   1 
ATOM   1034  C  CA  . SER A  1 158 ? 57.913  73.575 31.923  1.00 24.13 ? 158  SER A CA  1 
ATOM   1035  C  C   . SER A  1 158 ? 58.661  72.843 33.042  1.00 25.12 ? 158  SER A C   1 
ATOM   1036  O  O   . SER A  1 158 ? 58.505  73.184 34.216  1.00 25.06 ? 158  SER A O   1 
ATOM   1037  C  CB  . SER A  1 158 ? 58.857  74.504 31.145  1.00 24.08 ? 158  SER A CB  1 
ATOM   1038  O  OG  . SER A  1 158 ? 59.274  75.585 31.965  1.00 24.48 ? 158  SER A OG  1 
ATOM   1039  N  N   . PRO A  1 159 ? 59.454  71.819 32.708  1.00 25.40 ? 159  PRO A N   1 
ATOM   1040  C  CA  . PRO A  1 159 ? 60.186  71.072 33.739  1.00 26.44 ? 159  PRO A CA  1 
ATOM   1041  C  C   . PRO A  1 159 ? 61.313  71.871 34.407  1.00 27.51 ? 159  PRO A C   1 
ATOM   1042  O  O   . PRO A  1 159 ? 61.687  71.626 35.553  1.00 27.51 ? 159  PRO A O   1 
ATOM   1043  C  CB  . PRO A  1 159 ? 60.682  69.838 32.979  1.00 26.50 ? 159  PRO A CB  1 
ATOM   1044  C  CG  . PRO A  1 159 ? 60.776  70.329 31.534  1.00 27.64 ? 159  PRO A CG  1 
ATOM   1045  C  CD  . PRO A  1 159 ? 59.541  71.155 31.397  1.00 25.80 ? 159  PRO A CD  1 
ATOM   1046  N  N   . VAL A  1 160 ? 61.846  72.832 33.673  1.00 28.04 ? 160  VAL A N   1 
ATOM   1047  C  CA  . VAL A  1 160 ? 62.910  73.689 34.167  1.00 28.95 ? 160  VAL A CA  1 
ATOM   1048  C  C   . VAL A  1 160 ? 62.477  75.132 33.922  1.00 28.78 ? 160  VAL A C   1 
ATOM   1049  O  O   . VAL A  1 160 ? 61.743  75.405 32.970  1.00 29.53 ? 160  VAL A O   1 
ATOM   1050  C  CB  . VAL A  1 160 ? 64.232  73.406 33.405  1.00 28.80 ? 160  VAL A CB  1 
ATOM   1051  C  CG1 . VAL A  1 160 ? 65.208  74.565 33.578  1.00 29.31 ? 160  VAL A CG1 1 
ATOM   1052  C  CG2 . VAL A  1 160 ? 64.856  72.117 33.927  1.00 27.77 ? 160  VAL A CG2 1 
ATOM   1053  N  N   . GLY A  1 161 ? 62.914  76.044 34.786  1.00 28.52 ? 161  GLY A N   1 
ATOM   1054  C  CA  . GLY A  1 161 ? 62.571  77.442 34.607  1.00 28.33 ? 161  GLY A CA  1 
ATOM   1055  C  C   . GLY A  1 161 ? 61.144  77.823 34.956  1.00 27.33 ? 161  GLY A C   1 
ATOM   1056  O  O   . GLY A  1 161 ? 60.621  77.410 35.991  1.00 27.42 ? 161  GLY A O   1 
ATOM   1057  N  N   . HIS A  1 162 ? 60.508  78.616 34.098  1.00 27.38 ? 162  HIS A N   1 
ATOM   1058  C  CA  . HIS A  1 162 ? 59.150  79.055 34.374  1.00 26.86 ? 162  HIS A CA  1 
ATOM   1059  C  C   . HIS A  1 162 ? 58.210  79.298 33.197  1.00 26.03 ? 162  HIS A C   1 
ATOM   1060  O  O   . HIS A  1 162 ? 57.347  80.170 33.273  1.00 26.28 ? 162  HIS A O   1 
ATOM   1061  C  CB  . HIS A  1 162 ? 59.182  80.310 35.241  1.00 28.59 ? 162  HIS A CB  1 
ATOM   1062  C  CG  . HIS A  1 162 ? 60.000  81.421 34.663  1.00 30.04 ? 162  HIS A CG  1 
ATOM   1063  N  ND1 . HIS A  1 162 ? 61.029  82.023 35.353  1.00 30.24 ? 162  HIS A ND1 1 
ATOM   1064  C  CD2 . HIS A  1 162 ? 59.941  82.038 33.461  1.00 29.78 ? 162  HIS A CD2 1 
ATOM   1065  C  CE1 . HIS A  1 162 ? 61.570  82.962 34.599  1.00 31.05 ? 162  HIS A CE1 1 
ATOM   1066  N  NE2 . HIS A  1 162 ? 60.928  82.990 33.446  1.00 30.73 ? 162  HIS A NE2 1 
ATOM   1067  N  N   . LYS A  1 163 ? 58.366  78.553 32.112  1.00 25.27 ? 163  LYS A N   1 
ATOM   1068  C  CA  . LYS A  1 163 ? 57.444  78.699 30.989  1.00 25.34 ? 163  LYS A CA  1 
ATOM   1069  C  C   . LYS A  1 163 ? 56.152  78.013 31.421  1.00 25.74 ? 163  LYS A C   1 
ATOM   1070  O  O   . LYS A  1 163 ? 56.158  77.199 32.348  1.00 25.87 ? 163  LYS A O   1 
ATOM   1071  C  CB  . LYS A  1 163 ? 57.938  77.978 29.741  1.00 24.45 ? 163  LYS A CB  1 
ATOM   1072  C  CG  . LYS A  1 163 ? 59.258  78.451 29.171  1.00 25.70 ? 163  LYS A CG  1 
ATOM   1073  C  CD  . LYS A  1 163 ? 59.553  77.660 27.903  1.00 25.07 ? 163  LYS A CD  1 
ATOM   1074  C  CE  . LYS A  1 163 ? 60.918  77.967 27.304  1.00 26.28 ? 163  LYS A CE  1 
ATOM   1075  N  NZ  . LYS A  1 163 ? 61.189  77.087 26.112  1.00 25.18 ? 163  LYS A NZ  1 
ATOM   1076  N  N   . LEU A  1 164 ? 55.058  78.331 30.735  1.00 25.68 ? 164  LEU A N   1 
ATOM   1077  C  CA  . LEU A  1 164 ? 53.752  77.744 31.022  1.00 25.09 ? 164  LEU A CA  1 
ATOM   1078  C  C   . LEU A  1 164 ? 53.104  77.235 29.745  1.00 26.17 ? 164  LEU A C   1 
ATOM   1079  O  O   . LEU A  1 164 ? 53.291  77.806 28.668  1.00 26.28 ? 164  LEU A O   1 
ATOM   1080  C  CB  . LEU A  1 164 ? 52.817  78.784 31.634  1.00 25.20 ? 164  LEU A CB  1 
ATOM   1081  C  CG  . LEU A  1 164 ? 52.954  79.130 33.113  1.00 25.38 ? 164  LEU A CG  1 
ATOM   1082  C  CD1 . LEU A  1 164 ? 52.229  80.436 33.408  1.00 24.00 ? 164  LEU A CD1 1 
ATOM   1083  C  CD2 . LEU A  1 164 ? 52.389  77.980 33.954  1.00 24.25 ? 164  LEU A CD2 1 
ATOM   1084  N  N   . ALA A  1 165 ? 52.351  76.144 29.867  1.00 24.99 ? 165  ALA A N   1 
ATOM   1085  C  CA  . ALA A  1 165 ? 51.614  75.583 28.743  1.00 23.98 ? 165  ALA A CA  1 
ATOM   1086  C  C   . ALA A  1 165 ? 50.263  75.264 29.362  1.00 24.54 ? 165  ALA A C   1 
ATOM   1087  O  O   . ALA A  1 165 ? 50.205  74.675 30.450  1.00 24.68 ? 165  ALA A O   1 
ATOM   1088  C  CB  . ALA A  1 165 ? 52.280  74.318 28.234  1.00 22.63 ? 165  ALA A CB  1 
ATOM   1089  N  N   . TYR A  1 166 ? 49.188  75.701 28.715  1.00 23.51 ? 166  TYR A N   1 
ATOM   1090  C  CA  . TYR A  1 166 ? 47.855  75.428 29.218  1.00 23.96 ? 166  TYR A CA  1 
ATOM   1091  C  C   . TYR A  1 166 ? 46.908  75.173 28.061  1.00 23.19 ? 166  TYR A C   1 
ATOM   1092  O  O   . TYR A  1 166 ? 47.210  75.500 26.914  1.00 23.38 ? 166  TYR A O   1 
ATOM   1093  C  CB  . TYR A  1 166 ? 47.319  76.574 30.097  1.00 25.06 ? 166  TYR A CB  1 
ATOM   1094  C  CG  . TYR A  1 166 ? 47.128  77.901 29.396  1.00 26.48 ? 166  TYR A CG  1 
ATOM   1095  C  CD1 . TYR A  1 166 ? 48.161  78.837 29.338  1.00 27.35 ? 166  TYR A CD1 1 
ATOM   1096  C  CD2 . TYR A  1 166 ? 45.908  78.226 28.794  1.00 26.86 ? 166  TYR A CD2 1 
ATOM   1097  C  CE1 . TYR A  1 166 ? 47.988  80.071 28.698  1.00 27.48 ? 166  TYR A CE1 1 
ATOM   1098  C  CE2 . TYR A  1 166 ? 45.718  79.451 28.151  1.00 27.16 ? 166  TYR A CE2 1 
ATOM   1099  C  CZ  . TYR A  1 166 ? 46.767  80.371 28.112  1.00 28.72 ? 166  TYR A CZ  1 
ATOM   1100  O  OH  . TYR A  1 166 ? 46.584  81.595 27.510  1.00 29.23 ? 166  TYR A OH  1 
ATOM   1101  N  N   . VAL A  1 167 ? 45.773  74.563 28.373  1.00 22.02 ? 167  VAL A N   1 
ATOM   1102  C  CA  . VAL A  1 167 ? 44.766  74.242 27.378  1.00 21.36 ? 167  VAL A CA  1 
ATOM   1103  C  C   . VAL A  1 167 ? 43.493  74.976 27.759  1.00 21.69 ? 167  VAL A C   1 
ATOM   1104  O  O   . VAL A  1 167 ? 43.075  74.969 28.919  1.00 21.74 ? 167  VAL A O   1 
ATOM   1105  C  CB  . VAL A  1 167 ? 44.485  72.726 27.333  1.00 20.30 ? 167  VAL A CB  1 
ATOM   1106  C  CG1 . VAL A  1 167 ? 43.410  72.411 26.303  1.00 20.26 ? 167  VAL A CG1 1 
ATOM   1107  C  CG2 . VAL A  1 167 ? 45.774  71.978 26.996  1.00 20.54 ? 167  VAL A CG2 1 
ATOM   1108  N  N   . TRP A  1 168 ? 42.874  75.601 26.771  1.00 21.95 ? 168  TRP A N   1 
ATOM   1109  C  CA  . TRP A  1 168 ? 41.655  76.364 26.992  1.00 23.17 ? 168  TRP A CA  1 
ATOM   1110  C  C   . TRP A  1 168 ? 40.810  76.179 25.747  1.00 22.04 ? 168  TRP A C   1 
ATOM   1111  O  O   . TRP A  1 168 ? 41.308  76.297 24.632  1.00 21.47 ? 168  TRP A O   1 
ATOM   1112  C  CB  . TRP A  1 168 ? 42.016  77.840 27.216  1.00 25.03 ? 168  TRP A CB  1 
ATOM   1113  C  CG  . TRP A  1 168 ? 40.864  78.734 27.444  1.00 27.79 ? 168  TRP A CG  1 
ATOM   1114  C  CD1 . TRP A  1 168 ? 40.042  78.763 28.542  1.00 29.89 ? 168  TRP A CD1 1 
ATOM   1115  C  CD2 . TRP A  1 168 ? 40.400  79.758 26.569  1.00 29.49 ? 168  TRP A CD2 1 
ATOM   1116  N  NE1 . TRP A  1 168 ? 39.096  79.746 28.397  1.00 30.51 ? 168  TRP A NE1 1 
ATOM   1117  C  CE2 . TRP A  1 168 ? 39.296  80.373 27.193  1.00 30.71 ? 168  TRP A CE2 1 
ATOM   1118  C  CE3 . TRP A  1 168 ? 40.814  80.221 25.313  1.00 30.45 ? 168  TRP A CE3 1 
ATOM   1119  C  CZ2 . TRP A  1 168 ? 38.601  81.434 26.606  1.00 31.77 ? 168  TRP A CZ2 1 
ATOM   1120  C  CZ3 . TRP A  1 168 ? 40.122  81.275 24.731  1.00 31.60 ? 168  TRP A CZ3 1 
ATOM   1121  C  CH2 . TRP A  1 168 ? 39.028  81.869 25.380  1.00 31.82 ? 168  TRP A CH2 1 
ATOM   1122  N  N   . ASN A  1 169 ? 39.536  75.858 25.933  1.00 22.63 ? 169  ASN A N   1 
ATOM   1123  C  CA  . ASN A  1 169 ? 38.644  75.623 24.801  1.00 23.34 ? 169  ASN A CA  1 
ATOM   1124  C  C   . ASN A  1 169 ? 39.242  74.596 23.852  1.00 23.08 ? 169  ASN A C   1 
ATOM   1125  O  O   . ASN A  1 169 ? 39.102  74.698 22.640  1.00 22.83 ? 169  ASN A O   1 
ATOM   1126  C  CB  . ASN A  1 169 ? 38.372  76.923 24.052  1.00 24.01 ? 169  ASN A CB  1 
ATOM   1127  C  CG  . ASN A  1 169 ? 37.473  77.855 24.826  1.00 26.35 ? 169  ASN A CG  1 
ATOM   1128  O  OD1 . ASN A  1 169 ? 37.438  79.061 24.563  1.00 30.79 ? 169  ASN A OD1 1 
ATOM   1129  N  ND2 . ASN A  1 169 ? 36.738  77.311 25.784  1.00 25.97 ? 169  ASN A ND2 1 
ATOM   1130  N  N   . ASN A  1 170 ? 39.930  73.611 24.423  1.00 22.54 ? 170  ASN A N   1 
ATOM   1131  C  CA  . ASN A  1 170 ? 40.539  72.527 23.652  1.00 21.47 ? 170  ASN A CA  1 
ATOM   1132  C  C   . ASN A  1 170 ? 41.747  72.902 22.778  1.00 21.37 ? 170  ASN A C   1 
ATOM   1133  O  O   . ASN A  1 170 ? 42.156  72.126 21.919  1.00 20.25 ? 170  ASN A O   1 
ATOM   1134  C  CB  . ASN A  1 170 ? 39.480  71.840 22.785  1.00 21.24 ? 170  ASN A CB  1 
ATOM   1135  C  CG  . ASN A  1 170 ? 38.435  71.080 23.608  1.00 20.67 ? 170  ASN A CG  1 
ATOM   1136  O  OD1 . ASN A  1 170 ? 37.961  70.028 23.185  1.00 22.27 ? 170  ASN A OD1 1 
ATOM   1137  N  ND2 . ASN A  1 170 ? 38.066  71.615 24.768  1.00 19.09 ? 170  ASN A ND2 1 
ATOM   1138  N  N   . ASP A  1 171 ? 42.315  74.085 22.985  1.00 21.62 ? 171  ASP A N   1 
ATOM   1139  C  CA  . ASP A  1 171 ? 43.492  74.484 22.210  1.00 21.32 ? 171  ASP A CA  1 
ATOM   1140  C  C   . ASP A  1 171 ? 44.658  74.749 23.142  1.00 21.17 ? 171  ASP A C   1 
ATOM   1141  O  O   . ASP A  1 171 ? 44.464  75.154 24.288  1.00 21.50 ? 171  ASP A O   1 
ATOM   1142  C  CB  . ASP A  1 171 ? 43.193  75.724 21.363  1.00 22.65 ? 171  ASP A CB  1 
ATOM   1143  C  CG  . ASP A  1 171 ? 42.518  75.374 20.043  1.00 23.13 ? 171  ASP A CG  1 
ATOM   1144  O  OD1 . ASP A  1 171 ? 41.578  76.085 19.649  1.00 25.38 ? 171  ASP A OD1 1 
ATOM   1145  O  OD2 . ASP A  1 171 ? 42.937  74.393 19.392  1.00 23.82 ? 171  ASP A OD2 1 
ATOM   1146  N  N   . ILE A  1 172 ? 45.872  74.530 22.640  1.00 21.18 ? 172  ILE A N   1 
ATOM   1147  C  CA  . ILE A  1 172 ? 47.084  74.732 23.421  1.00 20.79 ? 172  ILE A CA  1 
ATOM   1148  C  C   . ILE A  1 172 ? 47.679  76.142 23.320  1.00 22.24 ? 172  ILE A C   1 
ATOM   1149  O  O   . ILE A  1 172 ? 47.719  76.720 22.239  1.00 23.24 ? 172  ILE A O   1 
ATOM   1150  C  CB  . ILE A  1 172 ? 48.152  73.723 22.988  1.00 20.47 ? 172  ILE A CB  1 
ATOM   1151  C  CG1 . ILE A  1 172 ? 47.603  72.303 23.159  1.00 17.94 ? 172  ILE A CG1 1 
ATOM   1152  C  CG2 . ILE A  1 172 ? 49.422  73.909 23.824  1.00 19.24 ? 172  ILE A CG2 1 
ATOM   1153  C  CD1 . ILE A  1 172 ? 48.472  71.223 22.560  1.00 17.13 ? 172  ILE A CD1 1 
ATOM   1154  N  N   . TYR A  1 173 ? 48.134  76.677 24.454  1.00 22.63 ? 173  TYR A N   1 
ATOM   1155  C  CA  . TYR A  1 173 ? 48.761  77.999 24.530  1.00 23.55 ? 173  TYR A CA  1 
ATOM   1156  C  C   . TYR A  1 173 ? 50.062  77.879 25.324  1.00 24.11 ? 173  TYR A C   1 
ATOM   1157  O  O   . TYR A  1 173 ? 50.146  77.080 26.258  1.00 22.74 ? 173  TYR A O   1 
ATOM   1158  C  CB  . TYR A  1 173 ? 47.850  79.019 25.238  1.00 22.56 ? 173  TYR A CB  1 
ATOM   1159  C  CG  . TYR A  1 173 ? 46.558  79.324 24.488  1.00 23.50 ? 173  TYR A CG  1 
ATOM   1160  C  CD1 . TYR A  1 173 ? 45.483  78.421 24.507  1.00 22.22 ? 173  TYR A CD1 1 
ATOM   1161  C  CD2 . TYR A  1 173 ? 46.421  80.503 23.732  1.00 22.80 ? 173  TYR A CD2 1 
ATOM   1162  C  CE1 . TYR A  1 173 ? 44.301  78.672 23.794  1.00 22.02 ? 173  TYR A CE1 1 
ATOM   1163  C  CE2 . TYR A  1 173 ? 45.234  80.768 23.009  1.00 22.81 ? 173  TYR A CE2 1 
ATOM   1164  C  CZ  . TYR A  1 173 ? 44.186  79.847 23.048  1.00 22.32 ? 173  TYR A CZ  1 
ATOM   1165  O  OH  . TYR A  1 173 ? 43.031  80.076 22.351  1.00 22.88 ? 173  TYR A OH  1 
ATOM   1166  N  N   . VAL A  1 174 ? 51.069  78.669 24.941  1.00 24.26 ? 174  VAL A N   1 
ATOM   1167  C  CA  . VAL A  1 174 ? 52.360  78.690 25.626  1.00 25.01 ? 174  VAL A CA  1 
ATOM   1168  C  C   . VAL A  1 174 ? 52.742  80.113 26.050  1.00 26.51 ? 174  VAL A C   1 
ATOM   1169  O  O   . VAL A  1 174 ? 52.596  81.056 25.273  1.00 26.73 ? 174  VAL A O   1 
ATOM   1170  C  CB  . VAL A  1 174 ? 53.498  78.142 24.725  1.00 25.10 ? 174  VAL A CB  1 
ATOM   1171  C  CG1 . VAL A  1 174 ? 54.849  78.434 25.372  1.00 23.17 ? 174  VAL A CG1 1 
ATOM   1172  C  CG2 . VAL A  1 174 ? 53.331  76.633 24.515  1.00 22.88 ? 174  VAL A CG2 1 
ATOM   1173  N  N   . LYS A  1 175 ? 53.220  80.258 27.282  1.00 27.47 ? 175  LYS A N   1 
ATOM   1174  C  CA  . LYS A  1 175 ? 53.671  81.550 27.811  1.00 28.91 ? 175  LYS A CA  1 
ATOM   1175  C  C   . LYS A  1 175 ? 55.134  81.437 28.239  1.00 29.65 ? 175  LYS A C   1 
ATOM   1176  O  O   . LYS A  1 175 ? 55.462  80.722 29.198  1.00 29.59 ? 175  LYS A O   1 
ATOM   1177  C  CB  . LYS A  1 175 ? 52.843  81.980 29.027  1.00 30.41 ? 175  LYS A CB  1 
ATOM   1178  C  CG  . LYS A  1 175 ? 51.531  82.658 28.697  1.00 31.99 ? 175  LYS A CG  1 
ATOM   1179  C  CD  . LYS A  1 175 ? 50.704  82.865 29.949  1.00 34.33 ? 175  LYS A CD  1 
ATOM   1180  C  CE  . LYS A  1 175 ? 51.387  83.775 30.941  1.00 36.19 ? 175  LYS A CE  1 
ATOM   1181  N  NZ  . LYS A  1 175 ? 51.277  85.198 30.522  1.00 38.15 ? 175  LYS A NZ  1 
ATOM   1182  N  N   . ILE A  1 176 ? 56.008  82.152 27.538  1.00 29.52 ? 176  ILE A N   1 
ATOM   1183  C  CA  . ILE A  1 176 ? 57.431  82.136 27.842  1.00 29.10 ? 176  ILE A CA  1 
ATOM   1184  C  C   . ILE A  1 176 ? 57.679  82.788 29.187  1.00 29.82 ? 176  ILE A C   1 
ATOM   1185  O  O   . ILE A  1 176 ? 58.570  82.379 29.929  1.00 30.47 ? 176  ILE A O   1 
ATOM   1186  C  CB  . ILE A  1 176 ? 58.218  82.875 26.757  1.00 28.88 ? 176  ILE A CB  1 
ATOM   1187  C  CG1 . ILE A  1 176 ? 57.898  82.256 25.400  1.00 28.64 ? 176  ILE A CG1 1 
ATOM   1188  C  CG2 . ILE A  1 176 ? 59.701  82.798 27.035  1.00 28.38 ? 176  ILE A CG2 1 
ATOM   1189  C  CD1 . ILE A  1 176 ? 58.199  80.767 25.308  1.00 29.51 ? 176  ILE A CD1 1 
ATOM   1190  N  N   . GLU A  1 177 ? 56.887  83.809 29.496  1.00 30.56 ? 177  GLU A N   1 
ATOM   1191  C  CA  . GLU A  1 177 ? 56.992  84.518 30.766  1.00 31.24 ? 177  GLU A CA  1 
ATOM   1192  C  C   . GLU A  1 177 ? 55.577  84.705 31.293  1.00 30.95 ? 177  GLU A C   1 
ATOM   1193  O  O   . GLU A  1 177 ? 54.652  84.974 30.524  1.00 30.52 ? 177  GLU A O   1 
ATOM   1194  C  CB  . GLU A  1 177 ? 57.656  85.881 30.584  1.00 33.27 ? 177  GLU A CB  1 
ATOM   1195  C  CG  . GLU A  1 177 ? 59.004  85.836 29.902  1.00 35.78 ? 177  GLU A CG  1 
ATOM   1196  C  CD  . GLU A  1 177 ? 60.021  85.053 30.690  1.00 37.85 ? 177  GLU A CD  1 
ATOM   1197  O  OE1 . GLU A  1 177 ? 60.137  85.293 31.914  1.00 38.91 ? 177  GLU A OE1 1 
ATOM   1198  O  OE2 . GLU A  1 177 ? 60.715  84.201 30.090  1.00 40.48 ? 177  GLU A OE2 1 
ATOM   1199  N  N   . PRO A  1 178 ? 55.395  84.581 32.615  1.00 30.90 ? 178  PRO A N   1 
ATOM   1200  C  CA  . PRO A  1 178 ? 54.089  84.718 33.273  1.00 31.82 ? 178  PRO A CA  1 
ATOM   1201  C  C   . PRO A  1 178 ? 53.314  85.998 32.949  1.00 33.18 ? 178  PRO A C   1 
ATOM   1202  O  O   . PRO A  1 178 ? 52.088  86.001 32.952  1.00 33.63 ? 178  PRO A O   1 
ATOM   1203  C  CB  . PRO A  1 178 ? 54.436  84.612 34.766  1.00 31.07 ? 178  PRO A CB  1 
ATOM   1204  C  CG  . PRO A  1 178 ? 55.721  83.782 34.772  1.00 30.87 ? 178  PRO A CG  1 
ATOM   1205  C  CD  . PRO A  1 178 ? 56.467  84.399 33.612  1.00 30.67 ? 178  PRO A CD  1 
ATOM   1206  N  N   . ASN A  1 179 ? 54.021  87.084 32.659  1.00 34.24 ? 179  ASN A N   1 
ATOM   1207  C  CA  . ASN A  1 179 ? 53.350  88.349 32.368  1.00 35.20 ? 179  ASN A CA  1 
ATOM   1208  C  C   . ASN A  1 179 ? 53.231  88.672 30.881  1.00 35.10 ? 179  ASN A C   1 
ATOM   1209  O  O   . ASN A  1 179 ? 52.563  89.633 30.518  1.00 35.63 ? 179  ASN A O   1 
ATOM   1210  C  CB  . ASN A  1 179 ? 54.084  89.498 33.057  1.00 36.21 ? 179  ASN A CB  1 
ATOM   1211  C  CG  . ASN A  1 179 ? 55.402  89.816 32.389  1.00 37.99 ? 179  ASN A CG  1 
ATOM   1212  O  OD1 . ASN A  1 179 ? 55.521  90.799 31.655  1.00 40.43 ? 179  ASN A OD1 1 
ATOM   1213  N  ND2 . ASN A  1 179 ? 56.397  88.972 32.620  1.00 38.45 ? 179  ASN A ND2 1 
ATOM   1214  N  N   . LEU A  1 180 ? 53.878  87.886 30.025  1.00 33.91 ? 180  LEU A N   1 
ATOM   1215  C  CA  . LEU A  1 180 ? 53.819  88.133 28.594  1.00 33.21 ? 180  LEU A CA  1 
ATOM   1216  C  C   . LEU A  1 180 ? 52.645  87.431 27.920  1.00 33.63 ? 180  LEU A C   1 
ATOM   1217  O  O   . LEU A  1 180 ? 52.163  86.407 28.396  1.00 33.56 ? 180  LEU A O   1 
ATOM   1218  C  CB  . LEU A  1 180 ? 55.119  87.682 27.928  1.00 32.71 ? 180  LEU A CB  1 
ATOM   1219  C  CG  . LEU A  1 180 ? 56.353  88.468 28.343  1.00 32.72 ? 180  LEU A CG  1 
ATOM   1220  C  CD1 . LEU A  1 180 ? 57.579  87.953 27.606  1.00 32.96 ? 180  LEU A CD1 1 
ATOM   1221  C  CD2 . LEU A  1 180 ? 56.118  89.946 28.043  1.00 33.54 ? 180  LEU A CD2 1 
ATOM   1222  N  N   . PRO A  1 181 ? 52.163  87.984 26.796  1.00 33.56 ? 181  PRO A N   1 
ATOM   1223  C  CA  . PRO A  1 181 ? 51.039  87.370 26.081  1.00 32.79 ? 181  PRO A CA  1 
ATOM   1224  C  C   . PRO A  1 181 ? 51.412  85.969 25.633  1.00 32.12 ? 181  PRO A C   1 
ATOM   1225  O  O   . PRO A  1 181 ? 52.574  85.686 25.367  1.00 30.98 ? 181  PRO A O   1 
ATOM   1226  C  CB  . PRO A  1 181 ? 50.808  88.322 24.902  1.00 33.26 ? 181  PRO A CB  1 
ATOM   1227  C  CG  . PRO A  1 181 ? 52.163  88.955 24.695  1.00 33.86 ? 181  PRO A CG  1 
ATOM   1228  C  CD  . PRO A  1 181 ? 52.623  89.206 26.113  1.00 33.74 ? 181  PRO A CD  1 
ATOM   1229  N  N   . SER A  1 182 ? 50.419  85.096 25.535  1.00 31.63 ? 182  SER A N   1 
ATOM   1230  C  CA  . SER A  1 182 ? 50.681  83.720 25.143  1.00 31.31 ? 182  SER A CA  1 
ATOM   1231  C  C   . SER A  1 182 ? 50.601  83.461 23.644  1.00 30.16 ? 182  SER A C   1 
ATOM   1232  O  O   . SER A  1 182 ? 49.919  84.161 22.912  1.00 29.99 ? 182  SER A O   1 
ATOM   1233  C  CB  . SER A  1 182 ? 49.712  82.793 25.873  1.00 32.27 ? 182  SER A CB  1 
ATOM   1234  O  OG  . SER A  1 182 ? 48.380  83.184 25.637  1.00 32.61 ? 182  SER A OG  1 
ATOM   1235  N  N   . TYR A  1 183 ? 51.326  82.448 23.194  1.00 29.11 ? 183  TYR A N   1 
ATOM   1236  C  CA  . TYR A  1 183 ? 51.309  82.066 21.797  1.00 28.92 ? 183  TYR A CA  1 
ATOM   1237  C  C   . TYR A  1 183 ? 50.264  80.966 21.617  1.00 29.05 ? 183  TYR A C   1 
ATOM   1238  O  O   . TYR A  1 183 ? 50.209  80.014 22.406  1.00 29.43 ? 183  TYR A O   1 
ATOM   1239  C  CB  . TYR A  1 183 ? 52.670  81.523 21.379  1.00 27.31 ? 183  TYR A CB  1 
ATOM   1240  C  CG  . TYR A  1 183 ? 53.801  82.494 21.589  1.00 28.72 ? 183  TYR A CG  1 
ATOM   1241  C  CD1 . TYR A  1 183 ? 54.227  83.348 20.561  1.00 29.32 ? 183  TYR A CD1 1 
ATOM   1242  C  CD2 . TYR A  1 183 ? 54.452  82.561 22.819  1.00 29.21 ? 183  TYR A CD2 1 
ATOM   1243  C  CE1 . TYR A  1 183 ? 55.287  84.242 20.767  1.00 29.99 ? 183  TYR A CE1 1 
ATOM   1244  C  CE2 . TYR A  1 183 ? 55.501  83.443 23.039  1.00 30.04 ? 183  TYR A CE2 1 
ATOM   1245  C  CZ  . TYR A  1 183 ? 55.917  84.277 22.011  1.00 31.13 ? 183  TYR A CZ  1 
ATOM   1246  O  OH  . TYR A  1 183 ? 56.980  85.120 22.247  1.00 32.65 ? 183  TYR A OH  1 
ATOM   1247  N  N   . ARG A  1 184 ? 49.437  81.098 20.589  1.00 28.51 ? 184  ARG A N   1 
ATOM   1248  C  CA  . ARG A  1 184 ? 48.424  80.094 20.295  1.00 29.05 ? 184  ARG A CA  1 
ATOM   1249  C  C   . ARG A  1 184 ? 49.148  79.000 19.537  1.00 28.32 ? 184  ARG A C   1 
ATOM   1250  O  O   . ARG A  1 184 ? 49.775  79.277 18.518  1.00 28.58 ? 184  ARG A O   1 
ATOM   1251  C  CB  . ARG A  1 184 ? 47.357  80.668 19.384  1.00 30.25 ? 184  ARG A CB  1 
ATOM   1252  C  CG  . ARG A  1 184 ? 45.985  80.662 19.978  1.00 33.81 ? 184  ARG A CG  1 
ATOM   1253  C  CD  . ARG A  1 184 ? 44.977  79.833 19.193  1.00 34.18 ? 184  ARG A CD  1 
ATOM   1254  N  NE  . ARG A  1 184 ? 43.659  80.390 19.464  1.00 37.47 ? 184  ARG A NE  1 
ATOM   1255  C  CZ  . ARG A  1 184 ? 42.495  79.838 19.147  1.00 37.48 ? 184  ARG A CZ  1 
ATOM   1256  N  NH1 . ARG A  1 184 ? 42.427  78.670 18.532  1.00 37.86 ? 184  ARG A NH1 1 
ATOM   1257  N  NH2 . ARG A  1 184 ? 41.387  80.484 19.446  1.00 38.44 ? 184  ARG A NH2 1 
ATOM   1258  N  N   . ILE A  1 185 ? 49.058  77.763 20.012  1.00 26.61 ? 185  ILE A N   1 
ATOM   1259  C  CA  . ILE A  1 185 ? 49.741  76.665 19.335  1.00 24.57 ? 185  ILE A CA  1 
ATOM   1260  C  C   . ILE A  1 185 ? 48.825  75.908 18.382  1.00 24.14 ? 185  ILE A C   1 
ATOM   1261  O  O   . ILE A  1 185 ? 49.259  75.452 17.321  1.00 24.73 ? 185  ILE A O   1 
ATOM   1262  C  CB  . ILE A  1 185 ? 50.313  75.655 20.351  1.00 23.81 ? 185  ILE A CB  1 
ATOM   1263  C  CG1 . ILE A  1 185 ? 51.222  76.365 21.356  1.00 23.92 ? 185  ILE A CG1 1 
ATOM   1264  C  CG2 . ILE A  1 185 ? 51.058  74.550 19.625  1.00 23.20 ? 185  ILE A CG2 1 
ATOM   1265  C  CD1 . ILE A  1 185 ? 52.432  77.078 20.719  1.00 23.88 ? 185  ILE A CD1 1 
ATOM   1266  N  N   . THR A  1 186 ? 47.561  75.752 18.769  1.00 23.51 ? 186  THR A N   1 
ATOM   1267  C  CA  . THR A  1 186 ? 46.581  75.033 17.947  1.00 22.14 ? 186  THR A CA  1 
ATOM   1268  C  C   . THR A  1 186 ? 45.315  75.849 17.818  1.00 22.78 ? 186  THR A C   1 
ATOM   1269  O  O   . THR A  1 186 ? 44.966  76.591 18.737  1.00 22.50 ? 186  THR A O   1 
ATOM   1270  C  CB  . THR A  1 186 ? 46.207  73.670 18.584  1.00 21.92 ? 186  THR A CB  1 
ATOM   1271  O  OG1 . THR A  1 186 ? 45.577  73.896 19.861  1.00 19.87 ? 186  THR A OG1 1 
ATOM   1272  C  CG2 . THR A  1 186 ? 47.472  72.813 18.768  1.00 21.12 ? 186  THR A CG2 1 
ATOM   1273  N  N   . TRP A  1 187 ? 44.612  75.672 16.698  1.00 23.75 ? 187  TRP A N   1 
ATOM   1274  C  CA  . TRP A  1 187 ? 43.378  76.414 16.410  1.00 24.17 ? 187  TRP A CA  1 
ATOM   1275  C  C   . TRP A  1 187 ? 42.219  75.490 16.027  1.00 23.89 ? 187  TRP A C   1 
ATOM   1276  O  O   . TRP A  1 187 ? 41.156  75.961 15.645  1.00 23.71 ? 187  TRP A O   1 
ATOM   1277  C  CB  . TRP A  1 187 ? 43.600  77.387 15.231  1.00 24.95 ? 187  TRP A CB  1 
ATOM   1278  C  CG  . TRP A  1 187 ? 44.736  78.346 15.409  1.00 26.41 ? 187  TRP A CG  1 
ATOM   1279  C  CD1 . TRP A  1 187 ? 46.073  78.064 15.344  1.00 26.52 ? 187  TRP A CD1 1 
ATOM   1280  C  CD2 . TRP A  1 187 ? 44.635  79.741 15.740  1.00 27.67 ? 187  TRP A CD2 1 
ATOM   1281  N  NE1 . TRP A  1 187 ? 46.812  79.195 15.619  1.00 27.20 ? 187  TRP A NE1 1 
ATOM   1282  C  CE2 . TRP A  1 187 ? 45.953  80.237 15.867  1.00 28.06 ? 187  TRP A CE2 1 
ATOM   1283  C  CE3 . TRP A  1 187 ? 43.559  80.615 15.946  1.00 28.84 ? 187  TRP A CE3 1 
ATOM   1284  C  CZ2 . TRP A  1 187 ? 46.224  81.572 16.190  1.00 28.72 ? 187  TRP A CZ2 1 
ATOM   1285  C  CZ3 . TRP A  1 187 ? 43.827  81.945 16.271  1.00 30.34 ? 187  TRP A CZ3 1 
ATOM   1286  C  CH2 . TRP A  1 187 ? 45.152  82.407 16.389  1.00 30.21 ? 187  TRP A CH2 1 
ATOM   1287  N  N   . THR A  1 188 ? 42.425  74.182 16.109  1.00 23.29 ? 188  THR A N   1 
ATOM   1288  C  CA  . THR A  1 188 ? 41.387  73.234 15.734  1.00 23.84 ? 188  THR A CA  1 
ATOM   1289  C  C   . THR A  1 188 ? 40.483  72.779 16.891  1.00 23.71 ? 188  THR A C   1 
ATOM   1290  O  O   . THR A  1 188 ? 39.504  72.056 16.679  1.00 23.65 ? 188  THR A O   1 
ATOM   1291  C  CB  . THR A  1 188 ? 42.009  71.990 15.106  1.00 24.51 ? 188  THR A CB  1 
ATOM   1292  O  OG1 . THR A  1 188 ? 43.000  71.471 15.997  1.00 26.25 ? 188  THR A OG1 1 
ATOM   1293  C  CG2 . THR A  1 188 ? 42.672  72.325 13.754  1.00 25.08 ? 188  THR A CG2 1 
ATOM   1294  N  N   . GLY A  1 189 ? 40.815  73.195 18.105  1.00 23.74 ? 189  GLY A N   1 
ATOM   1295  C  CA  . GLY A  1 189 ? 40.039  72.793 19.260  1.00 24.16 ? 189  GLY A CA  1 
ATOM   1296  C  C   . GLY A  1 189 ? 38.537  72.940 19.115  1.00 25.35 ? 189  GLY A C   1 
ATOM   1297  O  O   . GLY A  1 189 ? 38.049  74.008 18.750  1.00 24.64 ? 189  GLY A O   1 
ATOM   1298  N  N   . LYS A  1 190 ? 37.794  71.875 19.415  1.00 25.20 ? 190  LYS A N   1 
ATOM   1299  C  CA  . LYS A  1 190 ? 36.330  71.926 19.327  1.00 26.29 ? 190  LYS A CA  1 
ATOM   1300  C  C   . LYS A  1 190 ? 35.687  71.017 20.377  1.00 25.51 ? 190  LYS A C   1 
ATOM   1301  O  O   . LYS A  1 190 ? 35.882  69.806 20.355  1.00 24.08 ? 190  LYS A O   1 
ATOM   1302  C  CB  . LYS A  1 190 ? 35.879  71.505 17.927  1.00 27.81 ? 190  LYS A CB  1 
ATOM   1303  C  CG  . LYS A  1 190 ? 34.400  71.747 17.652  1.00 31.79 ? 190  LYS A CG  1 
ATOM   1304  C  CD  . LYS A  1 190 ? 34.111  71.630 16.148  1.00 34.16 ? 190  LYS A CD  1 
ATOM   1305  C  CE  . LYS A  1 190 ? 32.637  71.895 15.837  1.00 36.89 ? 190  LYS A CE  1 
ATOM   1306  N  NZ  . LYS A  1 190 ? 32.178  73.220 16.369  1.00 37.85 ? 190  LYS A NZ  1 
ATOM   1307  N  N   . GLU A  1 191 ? 34.926  71.615 21.288  1.00 25.42 ? 191  GLU A N   1 
ATOM   1308  C  CA  . GLU A  1 191 ? 34.261  70.875 22.351  1.00 25.63 ? 191  GLU A CA  1 
ATOM   1309  C  C   . GLU A  1 191 ? 33.642  69.553 21.877  1.00 24.02 ? 191  GLU A C   1 
ATOM   1310  O  O   . GLU A  1 191 ? 32.926  69.514 20.873  1.00 22.79 ? 191  GLU A O   1 
ATOM   1311  C  CB  . GLU A  1 191 ? 33.179  71.743 22.997  1.00 28.23 ? 191  GLU A CB  1 
ATOM   1312  C  CG  . GLU A  1 191 ? 32.480  71.055 24.153  1.00 30.34 ? 191  GLU A CG  1 
ATOM   1313  C  CD  . GLU A  1 191 ? 31.374  71.897 24.738  1.00 33.35 ? 191  GLU A CD  1 
ATOM   1314  O  OE1 . GLU A  1 191 ? 30.613  72.524 23.956  1.00 34.42 ? 191  GLU A OE1 1 
ATOM   1315  O  OE2 . GLU A  1 191 ? 31.257  71.920 25.984  1.00 34.44 ? 191  GLU A OE2 1 
ATOM   1316  N  N   . ASP A  1 192 ? 33.955  68.485 22.608  1.00 23.13 ? 192  ASP A N   1 
ATOM   1317  C  CA  . ASP A  1 192 ? 33.491  67.127 22.335  1.00 23.09 ? 192  ASP A CA  1 
ATOM   1318  C  C   . ASP A  1 192 ? 33.905  66.581 20.988  1.00 22.77 ? 192  ASP A C   1 
ATOM   1319  O  O   . ASP A  1 192 ? 33.414  65.529 20.589  1.00 22.12 ? 192  ASP A O   1 
ATOM   1320  C  CB  . ASP A  1 192 ? 31.966  67.013 22.414  1.00 24.98 ? 192  ASP A CB  1 
ATOM   1321  C  CG  . ASP A  1 192 ? 31.425  67.362 23.775  1.00 26.75 ? 192  ASP A CG  1 
ATOM   1322  O  OD1 . ASP A  1 192 ? 32.130  67.130 24.780  1.00 29.01 ? 192  ASP A OD1 1 
ATOM   1323  O  OD2 . ASP A  1 192 ? 30.287  67.859 23.833  1.00 28.62 ? 192  ASP A OD2 1 
ATOM   1324  N  N   . ILE A  1 193 ? 34.792  67.273 20.277  1.00 21.50 ? 193  ILE A N   1 
ATOM   1325  C  CA  . ILE A  1 193 ? 35.189  66.793 18.963  1.00 21.82 ? 193  ILE A CA  1 
ATOM   1326  C  C   . ILE A  1 193 ? 36.703  66.702 18.764  1.00 21.35 ? 193  ILE A C   1 
ATOM   1327  O  O   . ILE A  1 193 ? 37.220  65.619 18.503  1.00 20.67 ? 193  ILE A O   1 
ATOM   1328  C  CB  . ILE A  1 193 ? 34.590  67.689 17.856  1.00 22.33 ? 193  ILE A CB  1 
ATOM   1329  C  CG1 . ILE A  1 193 ? 33.067  67.730 17.981  1.00 23.22 ? 193  ILE A CG1 1 
ATOM   1330  C  CG2 . ILE A  1 193 ? 34.973  67.136 16.466  1.00 22.30 ? 193  ILE A CG2 1 
ATOM   1331  C  CD1 . ILE A  1 193 ? 32.376  66.416 17.585  1.00 26.22 ? 193  ILE A CD1 1 
ATOM   1332  N  N   . ILE A  1 194 ? 37.392  67.841 18.849  1.00 20.59 ? 194  ILE A N   1 
ATOM   1333  C  CA  . ILE A  1 194 ? 38.847  67.890 18.690  1.00 20.61 ? 194  ILE A CA  1 
ATOM   1334  C  C   . ILE A  1 194 ? 39.490  68.264 20.023  1.00 19.45 ? 194  ILE A C   1 
ATOM   1335  O  O   . ILE A  1 194 ? 39.168  69.301 20.604  1.00 19.82 ? 194  ILE A O   1 
ATOM   1336  C  CB  . ILE A  1 194 ? 39.280  68.944 17.651  1.00 21.53 ? 194  ILE A CB  1 
ATOM   1337  C  CG1 . ILE A  1 194 ? 38.615  68.662 16.301  1.00 21.29 ? 194  ILE A CG1 1 
ATOM   1338  C  CG2 . ILE A  1 194 ? 40.823  68.935 17.501  1.00 20.89 ? 194  ILE A CG2 1 
ATOM   1339  C  CD1 . ILE A  1 194 ? 38.978  67.329 15.690  1.00 19.69 ? 194  ILE A CD1 1 
ATOM   1340  N  N   . TYR A  1 195 ? 40.390  67.421 20.517  1.00 18.16 ? 195  TYR A N   1 
ATOM   1341  C  CA  . TYR A  1 195 ? 41.043  67.701 21.792  1.00 18.43 ? 195  TYR A CA  1 
ATOM   1342  C  C   . TYR A  1 195 ? 42.545  67.882 21.581  1.00 18.76 ? 195  TYR A C   1 
ATOM   1343  O  O   . TYR A  1 195 ? 43.225  66.948 21.180  1.00 20.83 ? 195  TYR A O   1 
ATOM   1344  C  CB  . TYR A  1 195 ? 40.834  66.544 22.780  1.00 18.29 ? 195  TYR A CB  1 
ATOM   1345  C  CG  . TYR A  1 195 ? 39.391  66.184 23.118  1.00 18.57 ? 195  TYR A CG  1 
ATOM   1346  C  CD1 . TYR A  1 195 ? 38.553  65.605 22.165  1.00 18.49 ? 195  TYR A CD1 1 
ATOM   1347  C  CD2 . TYR A  1 195 ? 38.891  66.364 24.411  1.00 17.23 ? 195  TYR A CD2 1 
ATOM   1348  C  CE1 . TYR A  1 195 ? 37.252  65.203 22.492  1.00 19.25 ? 195  TYR A CE1 1 
ATOM   1349  C  CE2 . TYR A  1 195 ? 37.591  65.964 24.753  1.00 18.32 ? 195  TYR A CE2 1 
ATOM   1350  C  CZ  . TYR A  1 195 ? 36.780  65.386 23.794  1.00 19.39 ? 195  TYR A CZ  1 
ATOM   1351  O  OH  . TYR A  1 195 ? 35.501  64.984 24.125  1.00 19.91 ? 195  TYR A OH  1 
ATOM   1352  N  N   . ASN A  1 196 ? 43.061  69.073 21.842  1.00 18.51 ? 196  ASN A N   1 
ATOM   1353  C  CA  . ASN A  1 196 ? 44.492  69.315 21.693  1.00 18.58 ? 196  ASN A CA  1 
ATOM   1354  C  C   . ASN A  1 196 ? 45.116  69.480 23.068  1.00 18.10 ? 196  ASN A C   1 
ATOM   1355  O  O   . ASN A  1 196 ? 44.727  70.371 23.820  1.00 19.55 ? 196  ASN A O   1 
ATOM   1356  C  CB  . ASN A  1 196 ? 44.761  70.606 20.899  1.00 18.60 ? 196  ASN A CB  1 
ATOM   1357  C  CG  . ASN A  1 196 ? 44.251  70.540 19.480  1.00 18.36 ? 196  ASN A CG  1 
ATOM   1358  O  OD1 . ASN A  1 196 ? 44.744  69.763 18.662  1.00 20.74 ? 196  ASN A OD1 1 
ATOM   1359  N  ND2 . ASN A  1 196 ? 43.255  71.356 19.177  1.00 18.70 ? 196  ASN A ND2 1 
ATOM   1360  N  N   . GLY A  1 197 ? 46.094  68.642 23.397  1.00 18.30 ? 197  GLY A N   1 
ATOM   1361  C  CA  . GLY A  1 197 ? 46.762  68.777 24.679  1.00 16.63 ? 197  GLY A CA  1 
ATOM   1362  C  C   . GLY A  1 197 ? 46.037  68.179 25.872  1.00 17.38 ? 197  GLY A C   1 
ATOM   1363  O  O   . GLY A  1 197 ? 46.608  68.138 26.973  1.00 17.84 ? 197  GLY A O   1 
ATOM   1364  N  N   . ILE A  1 198 ? 44.783  67.769 25.673  1.00 16.45 ? 198  ILE A N   1 
ATOM   1365  C  CA  . ILE A  1 198 ? 43.972  67.111 26.717  1.00 16.88 ? 198  ILE A CA  1 
ATOM   1366  C  C   . ILE A  1 198 ? 43.353  65.835 26.138  1.00 16.89 ? 198  ILE A C   1 
ATOM   1367  O  O   . ILE A  1 198 ? 43.205  65.700 24.915  1.00 18.07 ? 198  ILE A O   1 
ATOM   1368  C  CB  . ILE A  1 198 ? 42.821  68.022 27.274  1.00 15.94 ? 198  ILE A CB  1 
ATOM   1369  C  CG1 . ILE A  1 198 ? 41.962  68.575 26.120  1.00 15.68 ? 198  ILE A CG1 1 
ATOM   1370  C  CG2 . ILE A  1 198 ? 43.415  69.138 28.142  1.00 15.58 ? 198  ILE A CG2 1 
ATOM   1371  C  CD1 . ILE A  1 198 ? 40.767  69.423 26.576  1.00 13.02 ? 198  ILE A CD1 1 
ATOM   1372  N  N   . THR A  1 199 ? 42.984  64.901 27.005  1.00 16.10 ? 199  THR A N   1 
ATOM   1373  C  CA  . THR A  1 199 ? 42.421  63.634 26.552  1.00 16.85 ? 199  THR A CA  1 
ATOM   1374  C  C   . THR A  1 199 ? 40.896  63.665 26.532  1.00 17.13 ? 199  THR A C   1 
ATOM   1375  O  O   . THR A  1 199 ? 40.287  64.503 27.197  1.00 17.97 ? 199  THR A O   1 
ATOM   1376  C  CB  . THR A  1 199 ? 42.873  62.503 27.499  1.00 17.19 ? 199  THR A CB  1 
ATOM   1377  O  OG1 . THR A  1 199 ? 42.552  62.861 28.856  1.00 15.74 ? 199  THR A OG1 1 
ATOM   1378  C  CG2 . THR A  1 199 ? 44.385  62.320 27.413  1.00 16.73 ? 199  THR A CG2 1 
ATOM   1379  N  N   . ASP A  1 200 ? 40.288  62.781 25.741  1.00 16.81 ? 200  ASP A N   1 
ATOM   1380  C  CA  . ASP A  1 200 ? 38.838  62.693 25.711  1.00 16.53 ? 200  ASP A CA  1 
ATOM   1381  C  C   . ASP A  1 200 ? 38.507  61.753 26.878  1.00 16.47 ? 200  ASP A C   1 
ATOM   1382  O  O   . ASP A  1 200 ? 39.418  61.342 27.636  1.00 14.82 ? 200  ASP A O   1 
ATOM   1383  C  CB  . ASP A  1 200 ? 38.337  62.121 24.382  1.00 16.56 ? 200  ASP A CB  1 
ATOM   1384  C  CG  . ASP A  1 200 ? 38.704  60.659 24.193  1.00 18.14 ? 200  ASP A CG  1 
ATOM   1385  O  OD1 . ASP A  1 200 ? 39.639  60.159 24.876  1.00 16.82 ? 200  ASP A OD1 1 
ATOM   1386  O  OD2 . ASP A  1 200 ? 38.054  60.015 23.337  1.00 18.30 ? 200  ASP A OD2 1 
ATOM   1387  N  N   . TRP A  1 201 ? 37.233  61.397 27.018  1.00 15.12 ? 201  TRP A N   1 
ATOM   1388  C  CA  . TRP A  1 201 ? 36.810  60.558 28.135  1.00 15.25 ? 201  TRP A CA  1 
ATOM   1389  C  C   . TRP A  1 201 ? 37.571  59.249 28.266  1.00 14.71 ? 201  TRP A C   1 
ATOM   1390  O  O   . TRP A  1 201 ? 38.120  58.960 29.321  1.00 14.48 ? 201  TRP A O   1 
ATOM   1391  C  CB  . TRP A  1 201 ? 35.307  60.226 28.062  1.00 14.41 ? 201  TRP A CB  1 
ATOM   1392  C  CG  . TRP A  1 201 ? 34.823  59.635 29.367  1.00 15.08 ? 201  TRP A CG  1 
ATOM   1393  C  CD1 . TRP A  1 201 ? 34.279  60.313 30.429  1.00 15.10 ? 201  TRP A CD1 1 
ATOM   1394  C  CD2 . TRP A  1 201 ? 34.952  58.268 29.793  1.00 14.05 ? 201  TRP A CD2 1 
ATOM   1395  N  NE1 . TRP A  1 201 ? 34.069  59.455 31.485  1.00 14.31 ? 201  TRP A NE1 1 
ATOM   1396  C  CE2 . TRP A  1 201 ? 34.472  58.196 31.120  1.00 14.59 ? 201  TRP A CE2 1 
ATOM   1397  C  CE3 . TRP A  1 201 ? 35.425  57.100 29.179  1.00 13.90 ? 201  TRP A CE3 1 
ATOM   1398  C  CZ2 . TRP A  1 201 ? 34.451  56.997 31.848  1.00 13.68 ? 201  TRP A CZ2 1 
ATOM   1399  C  CZ3 . TRP A  1 201 ? 35.403  55.897 29.909  1.00 14.77 ? 201  TRP A CZ3 1 
ATOM   1400  C  CH2 . TRP A  1 201 ? 34.919  55.865 31.229  1.00 13.15 ? 201  TRP A CH2 1 
ATOM   1401  N  N   . VAL A  1 202 ? 37.614  58.462 27.198  1.00 14.68 ? 202  VAL A N   1 
ATOM   1402  C  CA  . VAL A  1 202 ? 38.258  57.157 27.299  1.00 13.93 ? 202  VAL A CA  1 
ATOM   1403  C  C   . VAL A  1 202 ? 39.778  57.207 27.479  1.00 14.61 ? 202  VAL A C   1 
ATOM   1404  O  O   . VAL A  1 202 ? 40.336  56.417 28.257  1.00 14.19 ? 202  VAL A O   1 
ATOM   1405  C  CB  . VAL A  1 202 ? 37.818  56.231 26.103  1.00 13.57 ? 202  VAL A CB  1 
ATOM   1406  C  CG1 . VAL A  1 202 ? 38.564  56.579 24.818  1.00 12.21 ? 202  VAL A CG1 1 
ATOM   1407  C  CG2 . VAL A  1 202 ? 37.990  54.760 26.483  1.00 11.69 ? 202  VAL A CG2 1 
ATOM   1408  N  N   . TYR A  1 203 ? 40.464  58.138 26.811  1.00 13.68 ? 203  TYR A N   1 
ATOM   1409  C  CA  . TYR A  1 203 ? 41.915  58.200 26.992  1.00 13.95 ? 203  TYR A CA  1 
ATOM   1410  C  C   . TYR A  1 203 ? 42.236  58.692 28.402  1.00 13.58 ? 203  TYR A C   1 
ATOM   1411  O  O   . TYR A  1 203 ? 43.239  58.291 28.985  1.00 12.95 ? 203  TYR A O   1 
ATOM   1412  C  CB  . TYR A  1 203 ? 42.577  59.122 25.961  1.00 13.58 ? 203  TYR A CB  1 
ATOM   1413  C  CG  . TYR A  1 203 ? 43.068  58.402 24.713  1.00 14.03 ? 203  TYR A CG  1 
ATOM   1414  C  CD1 . TYR A  1 203 ? 42.265  58.292 23.578  1.00 12.50 ? 203  TYR A CD1 1 
ATOM   1415  C  CD2 . TYR A  1 203 ? 44.351  57.862 24.662  1.00 13.93 ? 203  TYR A CD2 1 
ATOM   1416  C  CE1 . TYR A  1 203 ? 42.746  57.668 22.409  1.00 14.47 ? 203  TYR A CE1 1 
ATOM   1417  C  CE2 . TYR A  1 203 ? 44.831  57.240 23.514  1.00 16.20 ? 203  TYR A CE2 1 
ATOM   1418  C  CZ  . TYR A  1 203 ? 44.031  57.153 22.391  1.00 15.82 ? 203  TYR A CZ  1 
ATOM   1419  O  OH  . TYR A  1 203 ? 44.568  56.609 21.244  1.00 17.71 ? 203  TYR A OH  1 
ATOM   1420  N  N   . GLU A  1 204 ? 41.381  59.554 28.953  1.00 13.50 ? 204  GLU A N   1 
ATOM   1421  C  CA  . GLU A  1 204 ? 41.605  60.066 30.294  1.00 13.63 ? 204  GLU A CA  1 
ATOM   1422  C  C   . GLU A  1 204 ? 41.479  58.935 31.317  1.00 14.48 ? 204  GLU A C   1 
ATOM   1423  O  O   . GLU A  1 204 ? 42.339  58.737 32.173  1.00 14.81 ? 204  GLU A O   1 
ATOM   1424  C  CB  . GLU A  1 204 ? 40.569  61.129 30.676  1.00 13.29 ? 204  GLU A CB  1 
ATOM   1425  C  CG  . GLU A  1 204 ? 40.662  61.481 32.150  1.00 12.47 ? 204  GLU A CG  1 
ATOM   1426  C  CD  . GLU A  1 204 ? 39.601  62.451 32.656  1.00 12.82 ? 204  GLU A CD  1 
ATOM   1427  O  OE1 . GLU A  1 204 ? 38.966  63.167 31.834  1.00 13.55 ? 204  GLU A OE1 1 
ATOM   1428  O  OE2 . GLU A  1 204 ? 39.425  62.508 33.899  1.00 12.09 ? 204  GLU A OE2 1 
ATOM   1429  N  N   . GLU A  1 205 ? 40.378  58.202 31.224  1.00 14.23 ? 205  GLU A N   1 
ATOM   1430  C  CA  . GLU A  1 205 ? 40.084  57.141 32.171  1.00 14.08 ? 205  GLU A CA  1 
ATOM   1431  C  C   . GLU A  1 205 ? 40.864  55.837 31.997  1.00 13.95 ? 205  GLU A C   1 
ATOM   1432  O  O   . GLU A  1 205 ? 41.344  55.267 32.975  1.00 13.97 ? 205  GLU A O   1 
ATOM   1433  C  CB  . GLU A  1 205 ? 38.582  56.816 32.120  1.00 14.27 ? 205  GLU A CB  1 
ATOM   1434  C  CG  . GLU A  1 205 ? 38.156  55.546 32.869  1.00 13.53 ? 205  GLU A CG  1 
ATOM   1435  C  CD  . GLU A  1 205 ? 38.286  55.661 34.387  1.00 16.16 ? 205  GLU A CD  1 
ATOM   1436  O  OE1 . GLU A  1 205 ? 38.366  56.795 34.909  1.00 15.80 ? 205  GLU A OE1 1 
ATOM   1437  O  OE2 . GLU A  1 205 ? 38.297  54.610 35.064  1.00 16.37 ? 205  GLU A OE2 1 
ATOM   1438  N  N   . GLU A  1 206 ? 41.026  55.398 30.758  1.00 12.65 ? 206  GLU A N   1 
ATOM   1439  C  CA  . GLU A  1 206 ? 41.631  54.102 30.495  1.00 14.32 ? 206  GLU A CA  1 
ATOM   1440  C  C   . GLU A  1 206 ? 43.065  53.993 30.015  1.00 15.54 ? 206  GLU A C   1 
ATOM   1441  O  O   . GLU A  1 206 ? 43.716  52.989 30.272  1.00 15.20 ? 206  GLU A O   1 
ATOM   1442  C  CB  . GLU A  1 206 ? 40.755  53.349 29.489  1.00 13.09 ? 206  GLU A CB  1 
ATOM   1443  C  CG  . GLU A  1 206 ? 39.277  53.319 29.847  1.00 13.05 ? 206  GLU A CG  1 
ATOM   1444  C  CD  . GLU A  1 206 ? 38.962  52.373 30.999  1.00 14.01 ? 206  GLU A CD  1 
ATOM   1445  O  OE1 . GLU A  1 206 ? 39.901  51.875 31.654  1.00 14.97 ? 206  GLU A OE1 1 
ATOM   1446  O  OE2 . GLU A  1 206 ? 37.763  52.145 31.250  1.00 13.44 ? 206  GLU A OE2 1 
ATOM   1447  N  N   . VAL A  1 207 ? 43.551  55.010 29.314  1.00 17.50 ? 207  VAL A N   1 
ATOM   1448  C  CA  . VAL A  1 207 ? 44.893  54.964 28.745  1.00 17.25 ? 207  VAL A CA  1 
ATOM   1449  C  C   . VAL A  1 207 ? 45.964  55.703 29.539  1.00 18.83 ? 207  VAL A C   1 
ATOM   1450  O  O   . VAL A  1 207 ? 46.913  55.087 30.018  1.00 19.36 ? 207  VAL A O   1 
ATOM   1451  C  CB  . VAL A  1 207 ? 44.868  55.508 27.305  1.00 16.50 ? 207  VAL A CB  1 
ATOM   1452  C  CG1 . VAL A  1 207 ? 46.278  55.439 26.683  1.00 15.22 ? 207  VAL A CG1 1 
ATOM   1453  C  CG2 . VAL A  1 207 ? 43.895  54.689 26.471  1.00 14.83 ? 207  VAL A CG2 1 
ATOM   1454  N  N   . PHE A  1 208 ? 45.799  57.014 29.689  1.00 17.79 ? 208  PHE A N   1 
ATOM   1455  C  CA  . PHE A  1 208 ? 46.765  57.842 30.396  1.00 19.16 ? 208  PHE A CA  1 
ATOM   1456  C  C   . PHE A  1 208 ? 46.507  58.101 31.863  1.00 18.98 ? 208  PHE A C   1 
ATOM   1457  O  O   . PHE A  1 208 ? 47.407  58.555 32.555  1.00 17.74 ? 208  PHE A O   1 
ATOM   1458  C  CB  . PHE A  1 208 ? 46.902  59.202 29.689  1.00 20.70 ? 208  PHE A CB  1 
ATOM   1459  C  CG  . PHE A  1 208 ? 47.545  59.114 28.343  1.00 23.02 ? 208  PHE A CG  1 
ATOM   1460  C  CD1 . PHE A  1 208 ? 48.869  58.707 28.220  1.00 24.47 ? 208  PHE A CD1 1 
ATOM   1461  C  CD2 . PHE A  1 208 ? 46.817  59.379 27.187  1.00 24.62 ? 208  PHE A CD2 1 
ATOM   1462  C  CE1 . PHE A  1 208 ? 49.453  58.556 26.955  1.00 25.69 ? 208  PHE A CE1 1 
ATOM   1463  C  CE2 . PHE A  1 208 ? 47.399  59.228 25.918  1.00 24.27 ? 208  PHE A CE2 1 
ATOM   1464  C  CZ  . PHE A  1 208 ? 48.704  58.818 25.800  1.00 24.19 ? 208  PHE A CZ  1 
ATOM   1465  N  N   . SER A  1 209 ? 45.285  57.839 32.335  1.00 19.40 ? 209  SER A N   1 
ATOM   1466  C  CA  . SER A  1 209 ? 44.938  58.098 33.727  1.00 19.77 ? 209  SER A CA  1 
ATOM   1467  C  C   . SER A  1 209 ? 45.269  59.546 34.041  1.00 19.61 ? 209  SER A C   1 
ATOM   1468  O  O   . SER A  1 209 ? 45.819  59.844 35.098  1.00 19.17 ? 209  SER A O   1 
ATOM   1469  C  CB  . SER A  1 209 ? 45.741  57.203 34.671  1.00 20.08 ? 209  SER A CB  1 
ATOM   1470  O  OG  . SER A  1 209 ? 45.227  55.896 34.650  1.00 22.16 ? 209  SER A OG  1 
ATOM   1471  N  N   . ALA A  1 210 ? 44.930  60.440 33.118  1.00 18.80 ? 210  ALA A N   1 
ATOM   1472  C  CA  . ALA A  1 210 ? 45.216  61.855 33.284  1.00 18.06 ? 210  ALA A CA  1 
ATOM   1473  C  C   . ALA A  1 210 ? 44.454  62.641 32.216  1.00 17.62 ? 210  ALA A C   1 
ATOM   1474  O  O   . ALA A  1 210 ? 44.148  62.111 31.148  1.00 17.70 ? 210  ALA A O   1 
ATOM   1475  C  CB  . ALA A  1 210 ? 46.739  62.110 33.139  1.00 17.85 ? 210  ALA A CB  1 
ATOM   1476  N  N   . TYR A  1 211 ? 44.147  63.898 32.506  1.00 16.83 ? 211  TYR A N   1 
ATOM   1477  C  CA  . TYR A  1 211 ? 43.440  64.759 31.556  1.00 17.64 ? 211  TYR A CA  1 
ATOM   1478  C  C   . TYR A  1 211 ? 44.482  65.319 30.584  1.00 18.33 ? 211  TYR A C   1 
ATOM   1479  O  O   . TYR A  1 211 ? 44.230  65.489 29.391  1.00 18.75 ? 211  TYR A O   1 
ATOM   1480  C  CB  . TYR A  1 211 ? 42.780  65.895 32.319  1.00 16.13 ? 211  TYR A CB  1 
ATOM   1481  C  CG  . TYR A  1 211 ? 41.824  66.779 31.532  1.00 17.61 ? 211  TYR A CG  1 
ATOM   1482  C  CD1 . TYR A  1 211 ? 41.147  66.311 30.398  1.00 15.78 ? 211  TYR A CD1 1 
ATOM   1483  C  CD2 . TYR A  1 211 ? 41.510  68.062 32.003  1.00 15.92 ? 211  TYR A CD2 1 
ATOM   1484  C  CE1 . TYR A  1 211 ? 40.181  67.101 29.766  1.00 16.17 ? 211  TYR A CE1 1 
ATOM   1485  C  CE2 . TYR A  1 211 ? 40.548  68.848 31.381  1.00 15.21 ? 211  TYR A CE2 1 
ATOM   1486  C  CZ  . TYR A  1 211 ? 39.890  68.369 30.276  1.00 15.96 ? 211  TYR A CZ  1 
ATOM   1487  O  OH  . TYR A  1 211 ? 38.913  69.163 29.723  1.00 16.81 ? 211  TYR A OH  1 
ATOM   1488  N  N   . SER A  1 212 ? 45.661  65.584 31.122  1.00 17.65 ? 212  SER A N   1 
ATOM   1489  C  CA  . SER A  1 212 ? 46.768  66.139 30.358  1.00 20.09 ? 212  SER A CA  1 
ATOM   1490  C  C   . SER A  1 212 ? 47.262  65.267 29.204  1.00 19.73 ? 212  SER A C   1 
ATOM   1491  O  O   . SER A  1 212 ? 47.432  64.057 29.354  1.00 19.33 ? 212  SER A O   1 
ATOM   1492  C  CB  . SER A  1 212 ? 47.947  66.392 31.296  1.00 19.57 ? 212  SER A CB  1 
ATOM   1493  O  OG  . SER A  1 212 ? 49.118  66.603 30.543  1.00 27.11 ? 212  SER A OG  1 
ATOM   1494  N  N   . ALA A  1 213 ? 47.497  65.894 28.057  1.00 20.16 ? 213  ALA A N   1 
ATOM   1495  C  CA  . ALA A  1 213 ? 48.043  65.195 26.904  1.00 19.71 ? 213  ALA A CA  1 
ATOM   1496  C  C   . ALA A  1 213 ? 49.156  66.074 26.309  1.00 20.65 ? 213  ALA A C   1 
ATOM   1497  O  O   . ALA A  1 213 ? 49.285  66.202 25.079  1.00 19.61 ? 213  ALA A O   1 
ATOM   1498  C  CB  . ALA A  1 213 ? 46.958  64.918 25.867  1.00 20.29 ? 213  ALA A CB  1 
ATOM   1499  N  N   . LEU A  1 214 ? 49.937  66.678 27.211  1.00 21.19 ? 214  LEU A N   1 
ATOM   1500  C  CA  . LEU A  1 214 ? 51.089  67.553 26.893  1.00 22.40 ? 214  LEU A CA  1 
ATOM   1501  C  C   . LEU A  1 214 ? 52.325  66.986 27.578  1.00 21.91 ? 214  LEU A C   1 
ATOM   1502  O  O   . LEU A  1 214 ? 52.242  66.586 28.737  1.00 22.45 ? 214  LEU A O   1 
ATOM   1503  C  CB  . LEU A  1 214 ? 50.893  68.962 27.455  1.00 22.52 ? 214  LEU A CB  1 
ATOM   1504  C  CG  . LEU A  1 214 ? 49.752  69.793 26.911  1.00 23.90 ? 214  LEU A CG  1 
ATOM   1505  C  CD1 . LEU A  1 214 ? 49.690  71.104 27.670  1.00 24.51 ? 214  LEU A CD1 1 
ATOM   1506  C  CD2 . LEU A  1 214 ? 49.975  70.037 25.429  1.00 25.47 ? 214  LEU A CD2 1 
ATOM   1507  N  N   . TRP A  1 215 ? 53.466  66.998 26.888  1.00 20.93 ? 215  TRP A N   1 
ATOM   1508  C  CA  . TRP A  1 215 ? 54.709  66.476 27.441  1.00 20.33 ? 215  TRP A CA  1 
ATOM   1509  C  C   . TRP A  1 215 ? 55.917  67.377 27.115  1.00 21.08 ? 215  TRP A C   1 
ATOM   1510  O  O   . TRP A  1 215 ? 56.416  67.356 25.989  1.00 21.11 ? 215  TRP A O   1 
ATOM   1511  C  CB  . TRP A  1 215 ? 54.966  65.078 26.878  1.00 18.52 ? 215  TRP A CB  1 
ATOM   1512  C  CG  . TRP A  1 215 ? 53.936  64.061 27.251  1.00 18.90 ? 215  TRP A CG  1 
ATOM   1513  C  CD1 . TRP A  1 215 ? 53.920  63.283 28.384  1.00 19.19 ? 215  TRP A CD1 1 
ATOM   1514  C  CD2 . TRP A  1 215 ? 52.759  63.706 26.509  1.00 17.14 ? 215  TRP A CD2 1 
ATOM   1515  N  NE1 . TRP A  1 215 ? 52.814  62.472 28.386  1.00 18.15 ? 215  TRP A NE1 1 
ATOM   1516  C  CE2 . TRP A  1 215 ? 52.085  62.708 27.248  1.00 18.11 ? 215  TRP A CE2 1 
ATOM   1517  C  CE3 . TRP A  1 215 ? 52.209  64.134 25.295  1.00 17.50 ? 215  TRP A CE3 1 
ATOM   1518  C  CZ2 . TRP A  1 215 ? 50.890  62.134 26.812  1.00 17.62 ? 215  TRP A CZ2 1 
ATOM   1519  C  CZ3 . TRP A  1 215 ? 51.016  63.566 24.854  1.00 18.55 ? 215  TRP A CZ3 1 
ATOM   1520  C  CH2 . TRP A  1 215 ? 50.368  62.573 25.611  1.00 18.89 ? 215  TRP A CH2 1 
ATOM   1521  N  N   . TRP A  1 216 ? 56.373  68.161 28.092  1.00 21.02 ? 216  TRP A N   1 
ATOM   1522  C  CA  . TRP A  1 216 ? 57.526  69.044 27.911  1.00 21.48 ? 216  TRP A CA  1 
ATOM   1523  C  C   . TRP A  1 216 ? 58.815  68.227 27.772  1.00 21.46 ? 216  TRP A C   1 
ATOM   1524  O  O   . TRP A  1 216 ? 58.962  67.182 28.413  1.00 21.31 ? 216  TRP A O   1 
ATOM   1525  C  CB  . TRP A  1 216 ? 57.700  69.962 29.129  1.00 21.35 ? 216  TRP A CB  1 
ATOM   1526  C  CG  . TRP A  1 216 ? 56.799  71.160 29.224  1.00 22.53 ? 216  TRP A CG  1 
ATOM   1527  C  CD1 . TRP A  1 216 ? 55.753  71.337 30.091  1.00 23.19 ? 216  TRP A CD1 1 
ATOM   1528  C  CD2 . TRP A  1 216 ? 56.946  72.396 28.518  1.00 23.07 ? 216  TRP A CD2 1 
ATOM   1529  N  NE1 . TRP A  1 216 ? 55.254  72.610 29.976  1.00 24.05 ? 216  TRP A NE1 1 
ATOM   1530  C  CE2 . TRP A  1 216 ? 55.966  73.284 29.018  1.00 24.57 ? 216  TRP A CE2 1 
ATOM   1531  C  CE3 . TRP A  1 216 ? 57.816  72.843 27.514  1.00 22.78 ? 216  TRP A CE3 1 
ATOM   1532  C  CZ2 . TRP A  1 216 ? 55.832  74.602 28.548  1.00 24.24 ? 216  TRP A CZ2 1 
ATOM   1533  C  CZ3 . TRP A  1 216 ? 57.685  74.147 27.047  1.00 24.06 ? 216  TRP A CZ3 1 
ATOM   1534  C  CH2 . TRP A  1 216 ? 56.697  75.012 27.565  1.00 25.26 ? 216  TRP A CH2 1 
ATOM   1535  N  N   . SER A  1 217 ? 59.753  68.694 26.950  1.00 22.04 ? 217  SER A N   1 
ATOM   1536  C  CA  . SER A  1 217 ? 61.032  67.994 26.829  1.00 21.81 ? 217  SER A CA  1 
ATOM   1537  C  C   . SER A  1 217 ? 61.732  68.294 28.161  1.00 22.28 ? 217  SER A C   1 
ATOM   1538  O  O   . SER A  1 217 ? 61.344  69.224 28.879  1.00 22.01 ? 217  SER A O   1 
ATOM   1539  C  CB  . SER A  1 217 ? 61.855  68.515 25.638  1.00 22.03 ? 217  SER A CB  1 
ATOM   1540  O  OG  . SER A  1 217 ? 62.136  69.902 25.755  1.00 23.27 ? 217  SER A OG  1 
ATOM   1541  N  N   . PRO A  1 218 ? 62.770  67.518 28.510  1.00 22.09 ? 218  PRO A N   1 
ATOM   1542  C  CA  . PRO A  1 218 ? 63.501  67.697 29.766  1.00 23.00 ? 218  PRO A CA  1 
ATOM   1543  C  C   . PRO A  1 218 ? 63.875  69.123 30.159  1.00 23.66 ? 218  PRO A C   1 
ATOM   1544  O  O   . PRO A  1 218 ? 63.719  69.497 31.323  1.00 23.04 ? 218  PRO A O   1 
ATOM   1545  C  CB  . PRO A  1 218 ? 64.718  66.790 29.590  1.00 23.06 ? 218  PRO A CB  1 
ATOM   1546  C  CG  . PRO A  1 218 ? 64.151  65.673 28.734  1.00 24.06 ? 218  PRO A CG  1 
ATOM   1547  C  CD  . PRO A  1 218 ? 63.376  66.446 27.701  1.00 22.84 ? 218  PRO A CD  1 
ATOM   1548  N  N   . ASN A  1 219 ? 64.366  69.926 29.218  1.00 24.23 ? 219  ASN A N   1 
ATOM   1549  C  CA  . ASN A  1 219 ? 64.730  71.291 29.587  1.00 25.34 ? 219  ASN A CA  1 
ATOM   1550  C  C   . ASN A  1 219 ? 63.718  72.350 29.145  1.00 24.98 ? 219  ASN A C   1 
ATOM   1551  O  O   . ASN A  1 219 ? 63.982  73.544 29.249  1.00 24.46 ? 219  ASN A O   1 
ATOM   1552  C  CB  . ASN A  1 219 ? 66.138  71.652 29.076  1.00 26.18 ? 219  ASN A CB  1 
ATOM   1553  C  CG  . ASN A  1 219 ? 66.189  71.839 27.569  1.00 28.11 ? 219  ASN A CG  1 
ATOM   1554  O  OD1 . ASN A  1 219 ? 65.163  71.972 26.901  1.00 26.23 ? 219  ASN A OD1 1 
ATOM   1555  N  ND2 . ASN A  1 219 ? 67.399  71.875 27.025  1.00 30.47 ? 219  ASN A ND2 1 
ATOM   1556  N  N   . GLY A  1 220 ? 62.565  71.913 28.646  1.00 24.66 ? 220  GLY A N   1 
ATOM   1557  C  CA  . GLY A  1 220 ? 61.534  72.857 28.255  1.00 24.37 ? 220  GLY A CA  1 
ATOM   1558  C  C   . GLY A  1 220 ? 61.576  73.420 26.849  1.00 25.15 ? 220  GLY A C   1 
ATOM   1559  O  O   . GLY A  1 220 ? 60.703  74.221 26.465  1.00 24.42 ? 220  GLY A O   1 
ATOM   1560  N  N   . THR A  1 221 ? 62.576  73.022 26.068  1.00 24.13 ? 221  THR A N   1 
ATOM   1561  C  CA  . THR A  1 221 ? 62.672  73.533 24.711  1.00 24.59 ? 221  THR A CA  1 
ATOM   1562  C  C   . THR A  1 221 ? 61.491  73.127 23.844  1.00 24.01 ? 221  THR A C   1 
ATOM   1563  O  O   . THR A  1 221 ? 60.856  73.978 23.202  1.00 23.59 ? 221  THR A O   1 
ATOM   1564  C  CB  . THR A  1 221 ? 63.987  73.081 24.024  1.00 25.80 ? 221  THR A CB  1 
ATOM   1565  O  OG1 . THR A  1 221 ? 65.092  73.760 24.641  1.00 27.07 ? 221  THR A OG1 1 
ATOM   1566  C  CG2 . THR A  1 221 ? 63.949  73.405 22.520  1.00 24.37 ? 221  THR A CG2 1 
ATOM   1567  N  N   . PHE A  1 222 ? 61.200  71.833 23.822  1.00 21.64 ? 222  PHE A N   1 
ATOM   1568  C  CA  . PHE A  1 222 ? 60.103  71.321 23.012  1.00 21.98 ? 222  PHE A CA  1 
ATOM   1569  C  C   . PHE A  1 222 ? 58.862  70.968 23.842  1.00 22.01 ? 222  PHE A C   1 
ATOM   1570  O  O   . PHE A  1 222 ? 58.954  70.636 25.024  1.00 22.84 ? 222  PHE A O   1 
ATOM   1571  C  CB  . PHE A  1 222 ? 60.526  70.048 22.281  1.00 22.09 ? 222  PHE A CB  1 
ATOM   1572  C  CG  . PHE A  1 222 ? 61.663  70.224 21.320  1.00 23.08 ? 222  PHE A CG  1 
ATOM   1573  C  CD1 . PHE A  1 222 ? 61.459  70.833 20.087  1.00 23.48 ? 222  PHE A CD1 1 
ATOM   1574  C  CD2 . PHE A  1 222 ? 62.926  69.707 21.616  1.00 24.51 ? 222  PHE A CD2 1 
ATOM   1575  C  CE1 . PHE A  1 222 ? 62.488  70.918 19.156  1.00 24.37 ? 222  PHE A CE1 1 
ATOM   1576  C  CE2 . PHE A  1 222 ? 63.973  69.789 20.686  1.00 24.76 ? 222  PHE A CE2 1 
ATOM   1577  C  CZ  . PHE A  1 222 ? 63.751  70.396 19.453  1.00 24.03 ? 222  PHE A CZ  1 
ATOM   1578  N  N   . LEU A  1 223 ? 57.702  71.031 23.200  1.00 21.68 ? 223  LEU A N   1 
ATOM   1579  C  CA  . LEU A  1 223 ? 56.455  70.663 23.838  1.00 20.79 ? 223  LEU A CA  1 
ATOM   1580  C  C   . LEU A  1 223 ? 55.777  69.687 22.887  1.00 20.73 ? 223  LEU A C   1 
ATOM   1581  O  O   . LEU A  1 223 ? 55.420  70.054 21.757  1.00 21.32 ? 223  LEU A O   1 
ATOM   1582  C  CB  . LEU A  1 223 ? 55.528  71.873 24.052  1.00 20.62 ? 223  LEU A CB  1 
ATOM   1583  C  CG  . LEU A  1 223 ? 54.131  71.512 24.637  1.00 19.88 ? 223  LEU A CG  1 
ATOM   1584  C  CD1 . LEU A  1 223 ? 54.289  71.153 26.116  1.00 17.86 ? 223  LEU A CD1 1 
ATOM   1585  C  CD2 . LEU A  1 223 ? 53.137  72.684 24.481  1.00 19.17 ? 223  LEU A CD2 1 
ATOM   1586  N  N   . ALA A  1 224 ? 55.636  68.442 23.323  1.00 19.77 ? 224  ALA A N   1 
ATOM   1587  C  CA  . ALA A  1 224 ? 54.952  67.439 22.517  1.00 18.55 ? 224  ALA A CA  1 
ATOM   1588  C  C   . ALA A  1 224 ? 53.503  67.361 23.022  1.00 19.34 ? 224  ALA A C   1 
ATOM   1589  O  O   . ALA A  1 224 ? 53.227  67.623 24.207  1.00 18.51 ? 224  ALA A O   1 
ATOM   1590  C  CB  . ALA A  1 224 ? 55.621  66.102 22.670  1.00 17.14 ? 224  ALA A CB  1 
ATOM   1591  N  N   . TYR A  1 225 ? 52.585  67.006 22.127  1.00 19.25 ? 225  TYR A N   1 
ATOM   1592  C  CA  . TYR A  1 225 ? 51.181  66.888 22.492  1.00 19.59 ? 225  TYR A CA  1 
ATOM   1593  C  C   . TYR A  1 225 ? 50.428  65.958 21.560  1.00 19.46 ? 225  TYR A C   1 
ATOM   1594  O  O   . TYR A  1 225 ? 50.847  65.710 20.422  1.00 19.22 ? 225  TYR A O   1 
ATOM   1595  C  CB  . TYR A  1 225 ? 50.495  68.262 22.504  1.00 20.55 ? 225  TYR A CB  1 
ATOM   1596  C  CG  . TYR A  1 225 ? 50.388  68.945 21.148  1.00 21.94 ? 225  TYR A CG  1 
ATOM   1597  C  CD1 . TYR A  1 225 ? 51.415  69.761 20.669  1.00 22.44 ? 225  TYR A CD1 1 
ATOM   1598  C  CD2 . TYR A  1 225 ? 49.243  68.797 20.357  1.00 22.90 ? 225  TYR A CD2 1 
ATOM   1599  C  CE1 . TYR A  1 225 ? 51.301  70.418 19.435  1.00 22.63 ? 225  TYR A CE1 1 
ATOM   1600  C  CE2 . TYR A  1 225 ? 49.124  69.448 19.124  1.00 23.25 ? 225  TYR A CE2 1 
ATOM   1601  C  CZ  . TYR A  1 225 ? 50.159  70.256 18.678  1.00 23.90 ? 225  TYR A CZ  1 
ATOM   1602  O  OH  . TYR A  1 225 ? 50.033  70.925 17.487  1.00 26.01 ? 225  TYR A OH  1 
ATOM   1603  N  N   . ALA A  1 226 ? 49.314  65.434 22.055  1.00 18.20 ? 226  ALA A N   1 
ATOM   1604  C  CA  . ALA A  1 226 ? 48.500  64.542 21.264  1.00 18.40 ? 226  ALA A CA  1 
ATOM   1605  C  C   . ALA A  1 226 ? 47.224  65.287 20.922  1.00 18.42 ? 226  ALA A C   1 
ATOM   1606  O  O   . ALA A  1 226 ? 46.826  66.206 21.637  1.00 19.91 ? 226  ALA A O   1 
ATOM   1607  C  CB  . ALA A  1 226 ? 48.178  63.275 22.051  1.00 16.77 ? 226  ALA A CB  1 
ATOM   1608  N  N   . GLN A  1 227 ? 46.606  64.896 19.817  1.00 18.40 ? 227  GLN A N   1 
ATOM   1609  C  CA  . GLN A  1 227 ? 45.357  65.486 19.390  1.00 19.09 ? 227  GLN A CA  1 
ATOM   1610  C  C   . GLN A  1 227 ? 44.368  64.356 19.167  1.00 18.96 ? 227  GLN A C   1 
ATOM   1611  O  O   . GLN A  1 227 ? 44.623  63.447 18.372  1.00 19.32 ? 227  GLN A O   1 
ATOM   1612  C  CB  . GLN A  1 227 ? 45.510  66.244 18.085  1.00 19.73 ? 227  GLN A CB  1 
ATOM   1613  C  CG  . GLN A  1 227 ? 44.179  66.799 17.614  1.00 20.52 ? 227  GLN A CG  1 
ATOM   1614  C  CD  . GLN A  1 227 ? 44.234  67.307 16.199  1.00 21.65 ? 227  GLN A CD  1 
ATOM   1615  O  OE1 . GLN A  1 227 ? 44.165  66.531 15.250  1.00 23.56 ? 227  GLN A OE1 1 
ATOM   1616  N  NE2 . GLN A  1 227 ? 44.368  68.614 16.049  1.00 19.95 ? 227  GLN A NE2 1 
ATOM   1617  N  N   . PHE A  1 228 ? 43.224  64.423 19.841  1.00 18.39 ? 228  PHE A N   1 
ATOM   1618  C  CA  . PHE A  1 228 ? 42.231  63.368 19.689  1.00 18.27 ? 228  PHE A CA  1 
ATOM   1619  C  C   . PHE A  1 228 ? 41.043  63.866 18.883  1.00 18.39 ? 228  PHE A C   1 
ATOM   1620  O  O   . PHE A  1 228 ? 40.647  65.014 19.000  1.00 18.93 ? 228  PHE A O   1 
ATOM   1621  C  CB  . PHE A  1 228 ? 41.786  62.886 21.068  1.00 17.33 ? 228  PHE A CB  1 
ATOM   1622  C  CG  . PHE A  1 228 ? 42.931  62.440 21.945  1.00 17.40 ? 228  PHE A CG  1 
ATOM   1623  C  CD1 . PHE A  1 228 ? 43.437  61.144 21.860  1.00 17.08 ? 228  PHE A CD1 1 
ATOM   1624  C  CD2 . PHE A  1 228 ? 43.505  63.324 22.851  1.00 16.97 ? 228  PHE A CD2 1 
ATOM   1625  C  CE1 . PHE A  1 228 ? 44.502  60.731 22.672  1.00 16.43 ? 228  PHE A CE1 1 
ATOM   1626  C  CE2 . PHE A  1 228 ? 44.573  62.927 23.672  1.00 17.05 ? 228  PHE A CE2 1 
ATOM   1627  C  CZ  . PHE A  1 228 ? 45.069  61.627 23.580  1.00 16.83 ? 228  PHE A CZ  1 
ATOM   1628  N  N   . ASN A  1 229 ? 40.484  62.992 18.057  1.00 19.57 ? 229  ASN A N   1 
ATOM   1629  C  CA  . ASN A  1 229 ? 39.345  63.345 17.210  1.00 20.66 ? 229  ASN A CA  1 
ATOM   1630  C  C   . ASN A  1 229 ? 38.217  62.379 17.522  1.00 20.61 ? 229  ASN A C   1 
ATOM   1631  O  O   . ASN A  1 229 ? 38.301  61.192 17.204  1.00 20.40 ? 229  ASN A O   1 
ATOM   1632  C  CB  . ASN A  1 229 ? 39.737  63.221 15.742  1.00 21.98 ? 229  ASN A CB  1 
ATOM   1633  C  CG  . ASN A  1 229 ? 38.717  63.834 14.810  1.00 26.10 ? 229  ASN A CG  1 
ATOM   1634  O  OD1 . ASN A  1 229 ? 37.517  63.867 15.121  1.00 24.61 ? 229  ASN A OD1 1 
ATOM   1635  N  ND2 . ASN A  1 229 ? 39.186  64.306 13.653  1.00 27.81 ? 229  ASN A ND2 1 
ATOM   1636  N  N   . ASP A  1 230 ? 37.158  62.889 18.138  1.00 20.65 ? 230  ASP A N   1 
ATOM   1637  C  CA  . ASP A  1 230 ? 36.026  62.047 18.515  1.00 22.25 ? 230  ASP A CA  1 
ATOM   1638  C  C   . ASP A  1 230 ? 34.827  62.211 17.603  1.00 22.95 ? 230  ASP A C   1 
ATOM   1639  O  O   . ASP A  1 230 ? 33.739  61.707 17.890  1.00 23.25 ? 230  ASP A O   1 
ATOM   1640  C  CB  . ASP A  1 230 ? 35.634  62.350 19.949  1.00 21.20 ? 230  ASP A CB  1 
ATOM   1641  C  CG  . ASP A  1 230 ? 36.636  61.781 20.946  1.00 22.04 ? 230  ASP A CG  1 
ATOM   1642  O  OD1 . ASP A  1 230 ? 37.853  62.025 20.786  1.00 22.26 ? 230  ASP A OD1 1 
ATOM   1643  O  OD2 . ASP A  1 230 ? 36.210  61.097 21.883  1.00 21.47 ? 230  ASP A OD2 1 
ATOM   1644  N  N   . THR A  1 231 ? 35.043  62.894 16.485  1.00 23.64 ? 231  THR A N   1 
ATOM   1645  C  CA  . THR A  1 231 ? 33.982  63.146 15.521  1.00 23.92 ? 231  THR A CA  1 
ATOM   1646  C  C   . THR A  1 231 ? 32.966  62.027 15.377  1.00 24.28 ? 231  THR A C   1 
ATOM   1647  O  O   . THR A  1 231 ? 31.763  62.267 15.464  1.00 25.93 ? 231  THR A O   1 
ATOM   1648  C  CB  . THR A  1 231 ? 34.547  63.467 14.110  1.00 23.59 ? 231  THR A CB  1 
ATOM   1649  O  OG1 . THR A  1 231 ? 35.326  64.672 14.158  1.00 22.42 ? 231  THR A OG1 1 
ATOM   1650  C  CG2 . THR A  1 231 ? 33.403  63.681 13.128  1.00 23.33 ? 231  THR A CG2 1 
ATOM   1651  N  N   . GLU A  1 232 ? 33.411  60.798 15.177  1.00 23.93 ? 232  GLU A N   1 
ATOM   1652  C  CA  . GLU A  1 232 ? 32.427  59.747 14.990  1.00 23.45 ? 232  GLU A CA  1 
ATOM   1653  C  C   . GLU A  1 232 ? 32.183  58.852 16.201  1.00 21.82 ? 232  GLU A C   1 
ATOM   1654  O  O   . GLU A  1 232 ? 31.567  57.808 16.079  1.00 20.40 ? 232  GLU A O   1 
ATOM   1655  C  CB  . GLU A  1 232 ? 32.824  58.891 13.786  1.00 26.46 ? 232  GLU A CB  1 
ATOM   1656  C  CG  . GLU A  1 232 ? 32.705  59.613 12.460  1.00 30.32 ? 232  GLU A CG  1 
ATOM   1657  C  CD  . GLU A  1 232 ? 33.459  58.895 11.355  1.00 32.46 ? 232  GLU A CD  1 
ATOM   1658  O  OE1 . GLU A  1 232 ? 34.704  59.012 11.319  1.00 33.68 ? 232  GLU A OE1 1 
ATOM   1659  O  OE2 . GLU A  1 232 ? 32.807  58.201 10.544  1.00 34.11 ? 232  GLU A OE2 1 
ATOM   1660  N  N   . VAL A  1 233 ? 32.654  59.260 17.371  1.00 19.97 ? 233  VAL A N   1 
ATOM   1661  C  CA  . VAL A  1 233 ? 32.451  58.438 18.558  1.00 18.02 ? 233  VAL A CA  1 
ATOM   1662  C  C   . VAL A  1 233 ? 31.026  58.638 19.058  1.00 17.81 ? 233  VAL A C   1 
ATOM   1663  O  O   . VAL A  1 233 ? 30.582  59.778 19.210  1.00 17.59 ? 233  VAL A O   1 
ATOM   1664  C  CB  . VAL A  1 233 ? 33.457  58.841 19.643  1.00 17.25 ? 233  VAL A CB  1 
ATOM   1665  C  CG1 . VAL A  1 233 ? 33.141  58.125 20.951  1.00 15.89 ? 233  VAL A CG1 1 
ATOM   1666  C  CG2 . VAL A  1 233 ? 34.878  58.507 19.147  1.00 16.87 ? 233  VAL A CG2 1 
ATOM   1667  N  N   . PRO A  1 234 ? 30.280  57.538 19.290  1.00 16.71 ? 234  PRO A N   1 
ATOM   1668  C  CA  . PRO A  1 234 ? 28.906  57.687 19.771  1.00 18.12 ? 234  PRO A CA  1 
ATOM   1669  C  C   . PRO A  1 234 ? 28.906  58.352 21.136  1.00 17.72 ? 234  PRO A C   1 
ATOM   1670  O  O   . PRO A  1 234 ? 29.908  58.294 21.862  1.00 17.53 ? 234  PRO A O   1 
ATOM   1671  C  CB  . PRO A  1 234 ? 28.387  56.251 19.834  1.00 17.72 ? 234  PRO A CB  1 
ATOM   1672  C  CG  . PRO A  1 234 ? 29.227  55.519 18.839  1.00 18.05 ? 234  PRO A CG  1 
ATOM   1673  C  CD  . PRO A  1 234 ? 30.603  56.119 19.072  1.00 17.87 ? 234  PRO A CD  1 
ATOM   1674  N  N   . LEU A  1 235 ? 27.774  58.951 21.489  1.00 17.79 ? 235  LEU A N   1 
ATOM   1675  C  CA  . LEU A  1 235 ? 27.634  59.655 22.761  1.00 17.93 ? 235  LEU A CA  1 
ATOM   1676  C  C   . LEU A  1 235 ? 26.766  58.938 23.798  1.00 17.04 ? 235  LEU A C   1 
ATOM   1677  O  O   . LEU A  1 235 ? 25.672  58.474 23.476  1.00 16.98 ? 235  LEU A O   1 
ATOM   1678  C  CB  . LEU A  1 235 ? 27.026  61.039 22.519  1.00 19.93 ? 235  LEU A CB  1 
ATOM   1679  C  CG  . LEU A  1 235 ? 27.753  62.035 21.597  1.00 21.83 ? 235  LEU A CG  1 
ATOM   1680  C  CD1 . LEU A  1 235 ? 26.708  62.900 20.884  1.00 24.54 ? 235  LEU A CD1 1 
ATOM   1681  C  CD2 . LEU A  1 235 ? 28.702  62.907 22.409  1.00 20.41 ? 235  LEU A CD2 1 
ATOM   1682  N  N   . ILE A  1 236 ? 27.259  58.821 25.029  1.00 14.81 ? 236  ILE A N   1 
ATOM   1683  C  CA  . ILE A  1 236 ? 26.422  58.255 26.077  1.00 13.25 ? 236  ILE A CA  1 
ATOM   1684  C  C   . ILE A  1 236 ? 25.598  59.469 26.545  1.00 14.88 ? 236  ILE A C   1 
ATOM   1685  O  O   . ILE A  1 236 ? 26.115  60.597 26.628  1.00 14.70 ? 236  ILE A O   1 
ATOM   1686  C  CB  . ILE A  1 236 ? 27.236  57.664 27.275  1.00 13.70 ? 236  ILE A CB  1 
ATOM   1687  C  CG1 . ILE A  1 236 ? 26.267  57.221 28.386  1.00 11.47 ? 236  ILE A CG1 1 
ATOM   1688  C  CG2 . ILE A  1 236 ? 28.295  58.670 27.805  1.00 9.39  ? 236  ILE A CG2 1 
ATOM   1689  C  CD1 . ILE A  1 236 ? 25.349  56.055 27.966  1.00 9.91  ? 236  ILE A CD1 1 
ATOM   1690  N  N   . GLU A  1 237 ? 24.316  59.262 26.815  1.00 14.03 ? 237  GLU A N   1 
ATOM   1691  C  CA  . GLU A  1 237 ? 23.453  60.355 27.246  1.00 16.05 ? 237  GLU A CA  1 
ATOM   1692  C  C   . GLU A  1 237 ? 22.712  59.962 28.521  1.00 15.18 ? 237  GLU A C   1 
ATOM   1693  O  O   . GLU A  1 237 ? 22.226  58.843 28.643  1.00 14.34 ? 237  GLU A O   1 
ATOM   1694  C  CB  . GLU A  1 237 ? 22.454  60.707 26.120  1.00 17.19 ? 237  GLU A CB  1 
ATOM   1695  C  CG  . GLU A  1 237 ? 23.134  61.093 24.781  1.00 20.22 ? 237  GLU A CG  1 
ATOM   1696  C  CD  . GLU A  1 237 ? 22.156  61.628 23.724  1.00 22.69 ? 237  GLU A CD  1 
ATOM   1697  O  OE1 . GLU A  1 237 ? 22.600  62.125 22.668  1.00 26.00 ? 237  GLU A OE1 1 
ATOM   1698  O  OE2 . GLU A  1 237 ? 20.939  61.550 23.940  1.00 24.51 ? 237  GLU A OE2 1 
ATOM   1699  N  N   . TYR A  1 238 ? 22.655  60.871 29.486  1.00 15.26 ? 238  TYR A N   1 
ATOM   1700  C  CA  . TYR A  1 238 ? 21.935  60.601 30.734  1.00 15.88 ? 238  TYR A CA  1 
ATOM   1701  C  C   . TYR A  1 238 ? 21.465  61.915 31.351  1.00 15.16 ? 238  TYR A C   1 
ATOM   1702  O  O   . TYR A  1 238 ? 22.042  62.973 31.095  1.00 14.13 ? 238  TYR A O   1 
ATOM   1703  C  CB  . TYR A  1 238 ? 22.808  59.807 31.730  1.00 14.50 ? 238  TYR A CB  1 
ATOM   1704  C  CG  . TYR A  1 238 ? 24.139  60.453 32.085  1.00 16.28 ? 238  TYR A CG  1 
ATOM   1705  C  CD1 . TYR A  1 238 ? 25.306  60.148 31.364  1.00 15.43 ? 238  TYR A CD1 1 
ATOM   1706  C  CD2 . TYR A  1 238 ? 24.244  61.346 33.156  1.00 15.74 ? 238  TYR A CD2 1 
ATOM   1707  C  CE1 . TYR A  1 238 ? 26.552  60.718 31.710  1.00 16.36 ? 238  TYR A CE1 1 
ATOM   1708  C  CE2 . TYR A  1 238 ? 25.500  61.928 33.515  1.00 16.60 ? 238  TYR A CE2 1 
ATOM   1709  C  CZ  . TYR A  1 238 ? 26.640  61.600 32.783  1.00 15.89 ? 238  TYR A CZ  1 
ATOM   1710  O  OH  . TYR A  1 238 ? 27.872  62.124 33.106  1.00 17.73 ? 238  TYR A OH  1 
ATOM   1711  N  N   . SER A  1 239 ? 20.414  61.846 32.153  1.00 15.52 ? 239  SER A N   1 
ATOM   1712  C  CA  . SER A  1 239 ? 19.872  63.045 32.775  1.00 15.96 ? 239  SER A CA  1 
ATOM   1713  C  C   . SER A  1 239 ? 20.644  63.505 34.003  1.00 15.70 ? 239  SER A C   1 
ATOM   1714  O  O   . SER A  1 239 ? 21.186  62.699 34.765  1.00 15.84 ? 239  SER A O   1 
ATOM   1715  C  CB  . SER A  1 239 ? 18.408  62.825 33.176  1.00 16.80 ? 239  SER A CB  1 
ATOM   1716  O  OG  . SER A  1 239 ? 17.601  62.494 32.059  1.00 18.37 ? 239  SER A OG  1 
ATOM   1717  N  N   . PHE A  1 240 ? 20.701  64.816 34.182  1.00 16.09 ? 240  PHE A N   1 
ATOM   1718  C  CA  . PHE A  1 240 ? 21.340  65.386 35.355  1.00 16.63 ? 240  PHE A CA  1 
ATOM   1719  C  C   . PHE A  1 240 ? 20.254  66.283 35.880  1.00 17.18 ? 240  PHE A C   1 
ATOM   1720  O  O   . PHE A  1 240 ? 19.758  67.176 35.155  1.00 15.29 ? 240  PHE A O   1 
ATOM   1721  C  CB  . PHE A  1 240 ? 22.575  66.208 35.008  1.00 17.85 ? 240  PHE A CB  1 
ATOM   1722  C  CG  . PHE A  1 240 ? 23.394  66.549 36.198  1.00 18.02 ? 240  PHE A CG  1 
ATOM   1723  C  CD1 . PHE A  1 240 ? 24.294  65.629 36.710  1.00 18.03 ? 240  PHE A CD1 1 
ATOM   1724  C  CD2 . PHE A  1 240 ? 23.193  67.743 36.874  1.00 18.29 ? 240  PHE A CD2 1 
ATOM   1725  C  CE1 . PHE A  1 240 ? 24.983  65.890 37.895  1.00 19.15 ? 240  PHE A CE1 1 
ATOM   1726  C  CE2 . PHE A  1 240 ? 23.874  68.022 38.059  1.00 18.63 ? 240  PHE A CE2 1 
ATOM   1727  C  CZ  . PHE A  1 240 ? 24.772  67.087 38.572  1.00 18.82 ? 240  PHE A CZ  1 
ATOM   1728  N  N   . TYR A  1 241 ? 19.896  66.078 37.144  1.00 16.26 ? 241  TYR A N   1 
ATOM   1729  C  CA  . TYR A  1 241 ? 18.782  66.828 37.708  1.00 16.81 ? 241  TYR A CA  1 
ATOM   1730  C  C   . TYR A  1 241 ? 19.107  68.161 38.324  1.00 16.63 ? 241  TYR A C   1 
ATOM   1731  O  O   . TYR A  1 241 ? 18.277  69.060 38.299  1.00 16.08 ? 241  TYR A O   1 
ATOM   1732  C  CB  . TYR A  1 241 ? 18.019  65.923 38.688  1.00 16.01 ? 241  TYR A CB  1 
ATOM   1733  C  CG  . TYR A  1 241 ? 17.532  64.683 37.976  1.00 16.63 ? 241  TYR A CG  1 
ATOM   1734  C  CD1 . TYR A  1 241 ? 18.317  63.527 37.948  1.00 16.38 ? 241  TYR A CD1 1 
ATOM   1735  C  CD2 . TYR A  1 241 ? 16.349  64.698 37.235  1.00 15.25 ? 241  TYR A CD2 1 
ATOM   1736  C  CE1 . TYR A  1 241 ? 17.949  62.424 37.204  1.00 16.99 ? 241  TYR A CE1 1 
ATOM   1737  C  CE2 . TYR A  1 241 ? 15.965  63.590 36.469  1.00 16.50 ? 241  TYR A CE2 1 
ATOM   1738  C  CZ  . TYR A  1 241 ? 16.766  62.467 36.457  1.00 17.75 ? 241  TYR A CZ  1 
ATOM   1739  O  OH  . TYR A  1 241 ? 16.437  61.399 35.675  1.00 19.13 ? 241  TYR A OH  1 
ATOM   1740  N  N   . SER A  1 242 ? 20.310  68.274 38.878  1.00 17.62 ? 242  SER A N   1 
ATOM   1741  C  CA  . SER A  1 242 ? 20.779  69.507 39.485  1.00 19.03 ? 242  SER A CA  1 
ATOM   1742  C  C   . SER A  1 242 ? 19.949  69.933 40.685  1.00 19.31 ? 242  SER A C   1 
ATOM   1743  O  O   . SER A  1 242 ? 19.166  69.148 41.223  1.00 19.36 ? 242  SER A O   1 
ATOM   1744  C  CB  . SER A  1 242 ? 20.795  70.621 38.433  1.00 18.42 ? 242  SER A CB  1 
ATOM   1745  O  OG  . SER A  1 242 ? 21.473  71.762 38.919  1.00 19.80 ? 242  SER A OG  1 
ATOM   1746  N  N   . ASP A  1 243 ? 20.129  71.174 41.115  1.00 19.65 ? 243  ASP A N   1 
ATOM   1747  C  CA  . ASP A  1 243 ? 19.379  71.656 42.254  1.00 20.30 ? 243  ASP A CA  1 
ATOM   1748  C  C   . ASP A  1 243 ? 17.896  71.670 41.906  1.00 20.79 ? 243  ASP A C   1 
ATOM   1749  O  O   . ASP A  1 243 ? 17.494  71.684 40.738  1.00 19.76 ? 243  ASP A O   1 
ATOM   1750  C  CB  . ASP A  1 243 ? 19.833  73.060 42.668  1.00 22.92 ? 243  ASP A CB  1 
ATOM   1751  C  CG  . ASP A  1 243 ? 21.324  73.118 43.035  1.00 25.45 ? 243  ASP A CG  1 
ATOM   1752  O  OD1 . ASP A  1 243 ? 21.843  72.168 43.667  1.00 25.24 ? 243  ASP A OD1 1 
ATOM   1753  O  OD2 . ASP A  1 243 ? 21.968  74.133 42.696  1.00 28.39 ? 243  ASP A OD2 1 
ATOM   1754  N  N   . GLU A  1 244 ? 17.094  71.664 42.953  1.00 19.62 ? 244  GLU A N   1 
ATOM   1755  C  CA  . GLU A  1 244 ? 15.653  71.646 42.859  1.00 20.25 ? 244  GLU A CA  1 
ATOM   1756  C  C   . GLU A  1 244 ? 15.098  72.783 41.992  1.00 20.08 ? 244  GLU A C   1 
ATOM   1757  O  O   . GLU A  1 244 ? 14.040  72.662 41.361  1.00 19.36 ? 244  GLU A O   1 
ATOM   1758  C  CB  . GLU A  1 244 ? 15.117  71.728 44.282  1.00 21.26 ? 244  GLU A CB  1 
ATOM   1759  C  CG  . GLU A  1 244 ? 13.662  71.638 44.424  1.00 25.01 ? 244  GLU A CG  1 
ATOM   1760  C  CD  . GLU A  1 244 ? 13.227  71.895 45.857  1.00 24.40 ? 244  GLU A CD  1 
ATOM   1761  O  OE1 . GLU A  1 244 ? 13.996  71.568 46.793  1.00 25.66 ? 244  GLU A OE1 1 
ATOM   1762  O  OE2 . GLU A  1 244 ? 12.112  72.414 46.027  1.00 23.53 ? 244  GLU A OE2 1 
ATOM   1763  N  N   . SER A  1 245 ? 15.815  73.894 41.972  1.00 19.46 ? 245  SER A N   1 
ATOM   1764  C  CA  . SER A  1 245 ? 15.393  75.064 41.217  1.00 19.52 ? 245  SER A CA  1 
ATOM   1765  C  C   . SER A  1 245 ? 15.387  74.851 39.702  1.00 18.43 ? 245  SER A C   1 
ATOM   1766  O  O   . SER A  1 245 ? 14.706  75.583 38.981  1.00 19.12 ? 245  SER A O   1 
ATOM   1767  C  CB  . SER A  1 245 ? 16.290  76.259 41.577  1.00 20.23 ? 245  SER A CB  1 
ATOM   1768  O  OG  . SER A  1 245 ? 17.641  75.987 41.253  1.00 21.14 ? 245  SER A OG  1 
ATOM   1769  N  N   . LEU A  1 246 ? 16.136  73.867 39.212  1.00 16.75 ? 246  LEU A N   1 
ATOM   1770  C  CA  . LEU A  1 246 ? 16.180  73.612 37.762  1.00 16.27 ? 246  LEU A CA  1 
ATOM   1771  C  C   . LEU A  1 246 ? 14.863  72.954 37.305  1.00 15.59 ? 246  LEU A C   1 
ATOM   1772  O  O   . LEU A  1 246 ? 14.579  71.810 37.652  1.00 14.09 ? 246  LEU A O   1 
ATOM   1773  C  CB  . LEU A  1 246 ? 17.367  72.715 37.413  1.00 14.99 ? 246  LEU A CB  1 
ATOM   1774  C  CG  . LEU A  1 246 ? 17.524  72.418 35.920  1.00 16.48 ? 246  LEU A CG  1 
ATOM   1775  C  CD1 . LEU A  1 246 ? 17.752  73.728 35.166  1.00 16.63 ? 246  LEU A CD1 1 
ATOM   1776  C  CD2 . LEU A  1 246 ? 18.717  71.486 35.692  1.00 16.20 ? 246  LEU A CD2 1 
ATOM   1777  N  N   . GLN A  1 247 ? 14.075  73.678 36.517  1.00 16.08 ? 247  GLN A N   1 
ATOM   1778  C  CA  . GLN A  1 247 ? 12.772  73.183 36.087  1.00 15.68 ? 247  GLN A CA  1 
ATOM   1779  C  C   . GLN A  1 247 ? 12.810  71.967 35.168  1.00 15.35 ? 247  GLN A C   1 
ATOM   1780  O  O   . GLN A  1 247 ? 12.015  71.041 35.337  1.00 14.62 ? 247  GLN A O   1 
ATOM   1781  C  CB  . GLN A  1 247 ? 11.961  74.308 35.431  1.00 16.85 ? 247  GLN A CB  1 
ATOM   1782  C  CG  . GLN A  1 247 ? 10.490  73.906 35.181  1.00 16.10 ? 247  GLN A CG  1 
ATOM   1783  C  CD  . GLN A  1 247 ? 9.605   75.081 34.780  1.00 18.59 ? 247  GLN A CD  1 
ATOM   1784  O  OE1 . GLN A  1 247 ? 9.997   75.915 33.957  1.00 19.68 ? 247  GLN A OE1 1 
ATOM   1785  N  NE2 . GLN A  1 247 ? 8.397   75.143 35.353  1.00 17.32 ? 247  GLN A NE2 1 
ATOM   1786  N  N   . TYR A  1 248 ? 13.734  71.962 34.210  1.00 15.86 ? 248  TYR A N   1 
ATOM   1787  C  CA  . TYR A  1 248 ? 13.883  70.847 33.281  1.00 15.93 ? 248  TYR A CA  1 
ATOM   1788  C  C   . TYR A  1 248 ? 15.224  70.157 33.474  1.00 17.37 ? 248  TYR A C   1 
ATOM   1789  O  O   . TYR A  1 248 ? 16.270  70.815 33.446  1.00 16.54 ? 248  TYR A O   1 
ATOM   1790  C  CB  . TYR A  1 248 ? 13.832  71.326 31.822  1.00 16.41 ? 248  TYR A CB  1 
ATOM   1791  C  CG  . TYR A  1 248 ? 12.462  71.738 31.322  1.00 15.97 ? 248  TYR A CG  1 
ATOM   1792  C  CD1 . TYR A  1 248 ? 11.678  70.855 30.579  1.00 15.10 ? 248  TYR A CD1 1 
ATOM   1793  C  CD2 . TYR A  1 248 ? 11.953  73.014 31.586  1.00 14.98 ? 248  TYR A CD2 1 
ATOM   1794  C  CE1 . TYR A  1 248 ? 10.414  71.230 30.105  1.00 13.86 ? 248  TYR A CE1 1 
ATOM   1795  C  CE2 . TYR A  1 248 ? 10.689  73.395 31.115  1.00 15.52 ? 248  TYR A CE2 1 
ATOM   1796  C  CZ  . TYR A  1 248 ? 9.925   72.491 30.367  1.00 14.54 ? 248  TYR A CZ  1 
ATOM   1797  O  OH  . TYR A  1 248 ? 8.695   72.857 29.837  1.00 13.26 ? 248  TYR A OH  1 
ATOM   1798  N  N   . PRO A  1 249 ? 15.215  68.817 33.638  1.00 17.34 ? 249  PRO A N   1 
ATOM   1799  C  CA  . PRO A  1 249 ? 16.466  68.066 33.814  1.00 17.77 ? 249  PRO A CA  1 
ATOM   1800  C  C   . PRO A  1 249 ? 17.349  68.323 32.599  1.00 18.78 ? 249  PRO A C   1 
ATOM   1801  O  O   . PRO A  1 249 ? 16.856  68.518 31.476  1.00 18.63 ? 249  PRO A O   1 
ATOM   1802  C  CB  . PRO A  1 249 ? 16.005  66.605 33.850  1.00 18.71 ? 249  PRO A CB  1 
ATOM   1803  C  CG  . PRO A  1 249 ? 14.592  66.691 34.345  1.00 17.45 ? 249  PRO A CG  1 
ATOM   1804  C  CD  . PRO A  1 249 ? 14.056  67.909 33.622  1.00 16.97 ? 249  PRO A CD  1 
ATOM   1805  N  N   . LYS A  1 250 ? 18.655  68.334 32.834  1.00 17.63 ? 250  LYS A N   1 
ATOM   1806  C  CA  . LYS A  1 250 ? 19.616  68.551 31.783  1.00 18.21 ? 250  LYS A CA  1 
ATOM   1807  C  C   . LYS A  1 250 ? 20.081  67.183 31.252  1.00 17.37 ? 250  LYS A C   1 
ATOM   1808  O  O   . LYS A  1 250 ? 20.126  66.199 32.006  1.00 16.97 ? 250  LYS A O   1 
ATOM   1809  C  CB  . LYS A  1 250 ? 20.793  69.339 32.351  1.00 19.71 ? 250  LYS A CB  1 
ATOM   1810  C  CG  . LYS A  1 250 ? 21.997  69.363 31.455  1.00 25.85 ? 250  LYS A CG  1 
ATOM   1811  C  CD  . LYS A  1 250 ? 23.191  70.041 32.145  1.00 29.08 ? 250  LYS A CD  1 
ATOM   1812  C  CE  . LYS A  1 250 ? 24.479  69.830 31.337  1.00 31.63 ? 250  LYS A CE  1 
ATOM   1813  N  NZ  . LYS A  1 250 ? 25.647  70.608 31.873  1.00 33.79 ? 250  LYS A NZ  1 
ATOM   1814  N  N   . THR A  1 251 ? 20.381  67.104 29.960  1.00 15.29 ? 251  THR A N   1 
ATOM   1815  C  CA  . THR A  1 251 ? 20.867  65.856 29.381  1.00 16.69 ? 251  THR A CA  1 
ATOM   1816  C  C   . THR A  1 251 ? 22.377  65.996 29.152  1.00 17.02 ? 251  THR A C   1 
ATOM   1817  O  O   . THR A  1 251 ? 22.826  66.840 28.374  1.00 17.20 ? 251  THR A O   1 
ATOM   1818  C  CB  . THR A  1 251 ? 20.186  65.516 28.030  1.00 16.61 ? 251  THR A CB  1 
ATOM   1819  O  OG1 . THR A  1 251 ? 18.806  65.211 28.251  1.00 15.23 ? 251  THR A OG1 1 
ATOM   1820  C  CG2 . THR A  1 251 ? 20.846  64.280 27.390  1.00 15.77 ? 251  THR A CG2 1 
ATOM   1821  N  N   . VAL A  1 252 ? 23.159  65.204 29.877  1.00 16.99 ? 252  VAL A N   1 
ATOM   1822  C  CA  . VAL A  1 252 ? 24.613  65.215 29.742  1.00 15.75 ? 252  VAL A CA  1 
ATOM   1823  C  C   . VAL A  1 252 ? 24.938  64.328 28.533  1.00 16.25 ? 252  VAL A C   1 
ATOM   1824  O  O   . VAL A  1 252 ? 24.363  63.235 28.381  1.00 15.65 ? 252  VAL A O   1 
ATOM   1825  C  CB  . VAL A  1 252 ? 25.283  64.638 31.025  1.00 15.68 ? 252  VAL A CB  1 
ATOM   1826  C  CG1 . VAL A  1 252 ? 26.792  64.567 30.858  1.00 15.10 ? 252  VAL A CG1 1 
ATOM   1827  C  CG2 . VAL A  1 252 ? 24.951  65.522 32.231  1.00 17.58 ? 252  VAL A CG2 1 
ATOM   1828  N  N   . ARG A  1 253 ? 25.839  64.790 27.664  1.00 16.25 ? 253  ARG A N   1 
ATOM   1829  C  CA  . ARG A  1 253 ? 26.222  64.017 26.463  1.00 17.89 ? 253  ARG A CA  1 
ATOM   1830  C  C   . ARG A  1 253 ? 27.739  63.858 26.405  1.00 16.82 ? 253  ARG A C   1 
ATOM   1831  O  O   . ARG A  1 253 ? 28.444  64.847 26.303  1.00 17.66 ? 253  ARG A O   1 
ATOM   1832  C  CB  . ARG A  1 253 ? 25.725  64.727 25.191  1.00 18.50 ? 253  ARG A CB  1 
ATOM   1833  C  CG  . ARG A  1 253 ? 24.222  65.021 25.206  1.00 21.04 ? 253  ARG A CG  1 
ATOM   1834  C  CD  . ARG A  1 253 ? 23.683  65.363 23.813  1.00 21.38 ? 253  ARG A CD  1 
ATOM   1835  N  NE  . ARG A  1 253 ? 22.213  65.358 23.812  1.00 24.76 ? 253  ARG A NE  1 
ATOM   1836  C  CZ  . ARG A  1 253 ? 21.439  66.283 24.395  1.00 25.98 ? 253  ARG A CZ  1 
ATOM   1837  N  NH1 . ARG A  1 253 ? 21.978  67.318 25.043  1.00 26.54 ? 253  ARG A NH1 1 
ATOM   1838  N  NH2 . ARG A  1 253 ? 20.112  66.173 24.336  1.00 25.19 ? 253  ARG A NH2 1 
ATOM   1839  N  N   . VAL A  1 254 ? 28.239  62.629 26.445  1.00 15.70 ? 254  VAL A N   1 
ATOM   1840  C  CA  . VAL A  1 254 ? 29.689  62.405 26.454  1.00 16.02 ? 254  VAL A CA  1 
ATOM   1841  C  C   . VAL A  1 254 ? 30.177  61.416 25.391  1.00 16.34 ? 254  VAL A C   1 
ATOM   1842  O  O   . VAL A  1 254 ? 29.699  60.275 25.340  1.00 16.64 ? 254  VAL A O   1 
ATOM   1843  C  CB  . VAL A  1 254 ? 30.154  61.849 27.837  1.00 15.82 ? 254  VAL A CB  1 
ATOM   1844  C  CG1 . VAL A  1 254 ? 31.696  61.755 27.882  1.00 14.83 ? 254  VAL A CG1 1 
ATOM   1845  C  CG2 . VAL A  1 254 ? 29.640  62.737 28.981  1.00 14.65 ? 254  VAL A CG2 1 
ATOM   1846  N  N   . PRO A  1 255 ? 31.122  61.845 24.518  1.00 14.93 ? 255  PRO A N   1 
ATOM   1847  C  CA  . PRO A  1 255 ? 31.618  60.910 23.497  1.00 15.94 ? 255  PRO A CA  1 
ATOM   1848  C  C   . PRO A  1 255 ? 32.244  59.769 24.304  1.00 14.72 ? 255  PRO A C   1 
ATOM   1849  O  O   . PRO A  1 255 ? 33.201  59.957 25.061  1.00 15.11 ? 255  PRO A O   1 
ATOM   1850  C  CB  . PRO A  1 255 ? 32.658  61.732 22.722  1.00 15.84 ? 255  PRO A CB  1 
ATOM   1851  C  CG  . PRO A  1 255 ? 32.208  63.192 22.967  1.00 16.44 ? 255  PRO A CG  1 
ATOM   1852  C  CD  . PRO A  1 255 ? 31.826  63.136 24.441  1.00 15.53 ? 255  PRO A CD  1 
ATOM   1853  N  N   . TYR A  1 256 ? 31.690  58.587 24.135  1.00 14.77 ? 256  TYR A N   1 
ATOM   1854  C  CA  . TYR A  1 256 ? 32.123  57.441 24.901  1.00 15.01 ? 256  TYR A CA  1 
ATOM   1855  C  C   . TYR A  1 256 ? 31.931  56.203 24.045  1.00 14.42 ? 256  TYR A C   1 
ATOM   1856  O  O   . TYR A  1 256 ? 30.796  55.812 23.767  1.00 15.69 ? 256  TYR A O   1 
ATOM   1857  C  CB  . TYR A  1 256 ? 31.245  57.382 26.166  1.00 14.93 ? 256  TYR A CB  1 
ATOM   1858  C  CG  . TYR A  1 256 ? 31.488  56.246 27.142  1.00 15.54 ? 256  TYR A CG  1 
ATOM   1859  C  CD1 . TYR A  1 256 ? 31.324  54.915 26.758  1.00 14.72 ? 256  TYR A CD1 1 
ATOM   1860  C  CD2 . TYR A  1 256 ? 31.869  56.514 28.464  1.00 13.77 ? 256  TYR A CD2 1 
ATOM   1861  C  CE1 . TYR A  1 256 ? 31.530  53.873 27.671  1.00 14.95 ? 256  TYR A CE1 1 
ATOM   1862  C  CE2 . TYR A  1 256 ? 32.084  55.488 29.379  1.00 14.15 ? 256  TYR A CE2 1 
ATOM   1863  C  CZ  . TYR A  1 256 ? 31.908  54.163 28.972  1.00 15.53 ? 256  TYR A CZ  1 
ATOM   1864  O  OH  . TYR A  1 256 ? 32.106  53.137 29.879  1.00 15.52 ? 256  TYR A OH  1 
ATOM   1865  N  N   . PRO A  1 257 ? 33.033  55.559 23.635  1.00 12.97 ? 257  PRO A N   1 
ATOM   1866  C  CA  . PRO A  1 257 ? 32.960  54.352 22.812  1.00 14.23 ? 257  PRO A CA  1 
ATOM   1867  C  C   . PRO A  1 257 ? 32.768  53.092 23.636  1.00 14.95 ? 257  PRO A C   1 
ATOM   1868  O  O   . PRO A  1 257 ? 33.675  52.691 24.389  1.00 14.85 ? 257  PRO A O   1 
ATOM   1869  C  CB  . PRO A  1 257 ? 34.308  54.328 22.090  1.00 12.84 ? 257  PRO A CB  1 
ATOM   1870  C  CG  . PRO A  1 257 ? 35.262  54.878 23.163  1.00 13.55 ? 257  PRO A CG  1 
ATOM   1871  C  CD  . PRO A  1 257 ? 34.432  55.996 23.835  1.00 13.37 ? 257  PRO A CD  1 
ATOM   1872  N  N   . LYS A  1 258 ? 31.593  52.477 23.503  1.00 14.73 ? 258  LYS A N   1 
ATOM   1873  C  CA  . LYS A  1 258 ? 31.325  51.217 24.188  1.00 15.16 ? 258  LYS A CA  1 
ATOM   1874  C  C   . LYS A  1 258 ? 32.004  50.098 23.371  1.00 16.34 ? 258  LYS A C   1 
ATOM   1875  O  O   . LYS A  1 258 ? 32.453  50.335 22.252  1.00 16.18 ? 258  LYS A O   1 
ATOM   1876  C  CB  . LYS A  1 258 ? 29.822  50.988 24.302  1.00 15.00 ? 258  LYS A CB  1 
ATOM   1877  C  CG  . LYS A  1 258 ? 29.205  51.846 25.387  1.00 14.30 ? 258  LYS A CG  1 
ATOM   1878  C  CD  . LYS A  1 258 ? 27.693  51.898 25.295  1.00 14.41 ? 258  LYS A CD  1 
ATOM   1879  C  CE  . LYS A  1 258 ? 27.120  52.821 26.363  1.00 13.69 ? 258  LYS A CE  1 
ATOM   1880  N  NZ  . LYS A  1 258 ? 26.919  52.166 27.700  1.00 13.05 ? 258  LYS A NZ  1 
ATOM   1881  N  N   . ALA A  1 259 ? 32.062  48.887 23.914  1.00 16.73 ? 259  ALA A N   1 
ATOM   1882  C  CA  . ALA A  1 259 ? 32.752  47.790 23.224  1.00 17.41 ? 259  ALA A CA  1 
ATOM   1883  C  C   . ALA A  1 259 ? 32.363  47.619 21.751  1.00 18.01 ? 259  ALA A C   1 
ATOM   1884  O  O   . ALA A  1 259 ? 31.177  47.524 21.408  1.00 17.70 ? 259  ALA A O   1 
ATOM   1885  C  CB  . ALA A  1 259 ? 32.538  46.469 23.986  1.00 15.23 ? 259  ALA A CB  1 
ATOM   1886  N  N   . GLY A  1 260 ? 33.372  47.592 20.883  1.00 17.90 ? 260  GLY A N   1 
ATOM   1887  C  CA  . GLY A  1 260 ? 33.115  47.420 19.457  1.00 18.08 ? 260  GLY A CA  1 
ATOM   1888  C  C   . GLY A  1 260 ? 32.711  48.677 18.700  1.00 18.11 ? 260  GLY A C   1 
ATOM   1889  O  O   . GLY A  1 260 ? 32.672  48.667 17.474  1.00 17.90 ? 260  GLY A O   1 
ATOM   1890  N  N   . ALA A  1 261 ? 32.428  49.765 19.416  1.00 18.10 ? 261  ALA A N   1 
ATOM   1891  C  CA  . ALA A  1 261 ? 32.004  51.007 18.776  1.00 17.30 ? 261  ALA A CA  1 
ATOM   1892  C  C   . ALA A  1 261 ? 33.146  51.788 18.120  1.00 18.24 ? 261  ALA A C   1 
ATOM   1893  O  O   . ALA A  1 261 ? 34.323  51.416 18.229  1.00 18.95 ? 261  ALA A O   1 
ATOM   1894  C  CB  . ALA A  1 261 ? 31.270  51.903 19.791  1.00 15.66 ? 261  ALA A CB  1 
ATOM   1895  N  N   . VAL A  1 262 ? 32.793  52.879 17.445  1.00 17.59 ? 262  VAL A N   1 
ATOM   1896  C  CA  . VAL A  1 262 ? 33.777  53.710 16.788  1.00 17.16 ? 262  VAL A CA  1 
ATOM   1897  C  C   . VAL A  1 262 ? 34.626  54.430 17.833  1.00 18.13 ? 262  VAL A C   1 
ATOM   1898  O  O   . VAL A  1 262 ? 34.101  55.125 18.724  1.00 18.29 ? 262  VAL A O   1 
ATOM   1899  C  CB  . VAL A  1 262 ? 33.093  54.743 15.858  1.00 18.26 ? 262  VAL A CB  1 
ATOM   1900  C  CG1 . VAL A  1 262 ? 34.125  55.728 15.341  1.00 18.23 ? 262  VAL A CG1 1 
ATOM   1901  C  CG2 . VAL A  1 262 ? 32.406  54.019 14.677  1.00 18.65 ? 262  VAL A CG2 1 
ATOM   1902  N  N   . ASN A  1 263 ? 35.940  54.267 17.710  1.00 16.55 ? 263  ASN A N   1 
ATOM   1903  C  CA  . ASN A  1 263 ? 36.908  54.871 18.637  1.00 17.25 ? 263  ASN A CA  1 
ATOM   1904  C  C   . ASN A  1 263 ? 37.424  56.227 18.177  1.00 17.29 ? 263  ASN A C   1 
ATOM   1905  O  O   . ASN A  1 263 ? 37.358  56.569 16.988  1.00 17.74 ? 263  ASN A O   1 
ATOM   1906  C  CB  . ASN A  1 263 ? 38.150  53.965 18.783  1.00 15.71 ? 263  ASN A CB  1 
ATOM   1907  C  CG  . ASN A  1 263 ? 38.032  52.969 19.917  1.00 16.70 ? 263  ASN A CG  1 
ATOM   1908  O  OD1 . ASN A  1 263 ? 37.096  53.043 20.724  1.00 16.36 ? 263  ASN A OD1 1 
ATOM   1909  N  ND2 . ASN A  1 263 ? 38.989  52.034 19.998  1.00 15.21 ? 263  ASN A ND2 1 
ATOM   1910  N  N   . PRO A  1 264 ? 37.948  57.020 19.120  1.00 16.55 ? 264  PRO A N   1 
ATOM   1911  C  CA  . PRO A  1 264 ? 38.486  58.315 18.722  1.00 16.98 ? 264  PRO A CA  1 
ATOM   1912  C  C   . PRO A  1 264 ? 39.788  58.005 17.985  1.00 17.02 ? 264  PRO A C   1 
ATOM   1913  O  O   . PRO A  1 264 ? 40.354  56.929 18.171  1.00 16.97 ? 264  PRO A O   1 
ATOM   1914  C  CB  . PRO A  1 264 ? 38.762  59.004 20.061  1.00 18.29 ? 264  PRO A CB  1 
ATOM   1915  C  CG  . PRO A  1 264 ? 39.104  57.841 20.972  1.00 17.29 ? 264  PRO A CG  1 
ATOM   1916  C  CD  . PRO A  1 264 ? 38.032  56.838 20.583  1.00 17.21 ? 264  PRO A CD  1 
ATOM   1917  N  N   . THR A  1 265 ? 40.245  58.923 17.138  1.00 17.37 ? 265  THR A N   1 
ATOM   1918  C  CA  . THR A  1 265 ? 41.506  58.732 16.425  1.00 17.94 ? 265  THR A CA  1 
ATOM   1919  C  C   . THR A  1 265 ? 42.488  59.684 17.094  1.00 18.32 ? 265  THR A C   1 
ATOM   1920  O  O   . THR A  1 265 ? 42.074  60.594 17.799  1.00 18.30 ? 265  THR A O   1 
ATOM   1921  C  CB  . THR A  1 265 ? 41.396  59.064 14.909  1.00 17.54 ? 265  THR A CB  1 
ATOM   1922  O  OG1 . THR A  1 265 ? 40.900  60.397 14.748  1.00 16.72 ? 265  THR A OG1 1 
ATOM   1923  C  CG2 . THR A  1 265 ? 40.456  58.083 14.207  1.00 18.31 ? 265  THR A CG2 1 
ATOM   1924  N  N   . VAL A  1 266 ? 43.781  59.490 16.855  1.00 19.36 ? 266  VAL A N   1 
ATOM   1925  C  CA  . VAL A  1 266 ? 44.811  60.293 17.508  1.00 20.49 ? 266  VAL A CA  1 
ATOM   1926  C  C   . VAL A  1 266 ? 45.997  60.630 16.599  1.00 21.14 ? 266  VAL A C   1 
ATOM   1927  O  O   . VAL A  1 266 ? 46.359  59.847 15.732  1.00 22.25 ? 266  VAL A O   1 
ATOM   1928  C  CB  . VAL A  1 266 ? 45.364  59.512 18.725  1.00 19.74 ? 266  VAL A CB  1 
ATOM   1929  C  CG1 . VAL A  1 266 ? 45.876  58.135 18.265  1.00 19.69 ? 266  VAL A CG1 1 
ATOM   1930  C  CG2 . VAL A  1 266 ? 46.486  60.279 19.384  1.00 19.84 ? 266  VAL A CG2 1 
ATOM   1931  N  N   . LYS A  1 267 ? 46.592  61.803 16.807  1.00 21.54 ? 267  LYS A N   1 
ATOM   1932  C  CA  . LYS A  1 267 ? 47.773  62.225 16.055  1.00 21.32 ? 267  LYS A CA  1 
ATOM   1933  C  C   . LYS A  1 267 ? 48.734  62.763 17.099  1.00 21.19 ? 267  LYS A C   1 
ATOM   1934  O  O   . LYS A  1 267 ? 48.294  63.208 18.163  1.00 21.28 ? 267  LYS A O   1 
ATOM   1935  C  CB  . LYS A  1 267 ? 47.427  63.330 15.063  1.00 21.63 ? 267  LYS A CB  1 
ATOM   1936  C  CG  . LYS A  1 267 ? 46.557  62.873 13.917  1.00 23.18 ? 267  LYS A CG  1 
ATOM   1937  C  CD  . LYS A  1 267 ? 46.267  64.053 12.989  1.00 25.59 ? 267  LYS A CD  1 
ATOM   1938  C  CE  . LYS A  1 267 ? 45.476  63.624 11.753  1.00 25.95 ? 267  LYS A CE  1 
ATOM   1939  N  NZ  . LYS A  1 267 ? 45.310  64.813 10.873  1.00 27.62 ? 267  LYS A NZ  1 
ATOM   1940  N  N   . PHE A  1 268 ? 50.032  62.722 16.809  1.00 20.86 ? 268  PHE A N   1 
ATOM   1941  C  CA  . PHE A  1 268 ? 51.038  63.203 17.754  1.00 20.87 ? 268  PHE A CA  1 
ATOM   1942  C  C   . PHE A  1 268 ? 51.905  64.297 17.132  1.00 21.64 ? 268  PHE A C   1 
ATOM   1943  O  O   . PHE A  1 268 ? 52.364  64.151 16.001  1.00 21.78 ? 268  PHE A O   1 
ATOM   1944  C  CB  . PHE A  1 268 ? 51.927  62.044 18.201  1.00 20.41 ? 268  PHE A CB  1 
ATOM   1945  C  CG  . PHE A  1 268 ? 52.828  62.386 19.346  1.00 21.84 ? 268  PHE A CG  1 
ATOM   1946  C  CD1 . PHE A  1 268 ? 52.320  62.491 20.641  1.00 21.26 ? 268  PHE A CD1 1 
ATOM   1947  C  CD2 . PHE A  1 268 ? 54.182  62.629 19.135  1.00 22.14 ? 268  PHE A CD2 1 
ATOM   1948  C  CE1 . PHE A  1 268 ? 53.149  62.836 21.713  1.00 21.94 ? 268  PHE A CE1 1 
ATOM   1949  C  CE2 . PHE A  1 268 ? 55.026  62.976 20.207  1.00 22.92 ? 268  PHE A CE2 1 
ATOM   1950  C  CZ  . PHE A  1 268 ? 54.502  63.079 21.498  1.00 22.12 ? 268  PHE A CZ  1 
ATOM   1951  N  N   . PHE A  1 269 ? 52.137  65.379 17.874  1.00 21.94 ? 269  PHE A N   1 
ATOM   1952  C  CA  . PHE A  1 269 ? 52.942  66.498 17.376  1.00 21.96 ? 269  PHE A CA  1 
ATOM   1953  C  C   . PHE A  1 269 ? 53.978  67.000 18.374  1.00 22.05 ? 269  PHE A C   1 
ATOM   1954  O  O   . PHE A  1 269 ? 53.815  66.851 19.588  1.00 22.25 ? 269  PHE A O   1 
ATOM   1955  C  CB  . PHE A  1 269 ? 52.064  67.709 17.036  1.00 21.72 ? 269  PHE A CB  1 
ATOM   1956  C  CG  . PHE A  1 269 ? 50.939  67.426 16.086  1.00 20.60 ? 269  PHE A CG  1 
ATOM   1957  C  CD1 . PHE A  1 269 ? 49.704  66.992 16.556  1.00 20.21 ? 269  PHE A CD1 1 
ATOM   1958  C  CD2 . PHE A  1 269 ? 51.088  67.674 14.724  1.00 21.93 ? 269  PHE A CD2 1 
ATOM   1959  C  CE1 . PHE A  1 269 ? 48.631  66.815 15.690  1.00 19.56 ? 269  PHE A CE1 1 
ATOM   1960  C  CE2 . PHE A  1 269 ? 50.013  67.499 13.831  1.00 20.78 ? 269  PHE A CE2 1 
ATOM   1961  C  CZ  . PHE A  1 269 ? 48.781  67.070 14.320  1.00 21.60 ? 269  PHE A CZ  1 
ATOM   1962  N  N   . VAL A  1 270 ? 55.022  67.643 17.857  1.00 21.53 ? 270  VAL A N   1 
ATOM   1963  C  CA  . VAL A  1 270 ? 56.057  68.215 18.701  1.00 22.31 ? 270  VAL A CA  1 
ATOM   1964  C  C   . VAL A  1 270 ? 56.318  69.622 18.192  1.00 23.42 ? 270  VAL A C   1 
ATOM   1965  O  O   . VAL A  1 270 ? 56.464  69.837 16.986  1.00 22.41 ? 270  VAL A O   1 
ATOM   1966  C  CB  . VAL A  1 270 ? 57.384  67.438 18.635  1.00 22.32 ? 270  VAL A CB  1 
ATOM   1967  C  CG1 . VAL A  1 270 ? 58.396  68.097 19.552  1.00 22.95 ? 270  VAL A CG1 1 
ATOM   1968  C  CG2 . VAL A  1 270 ? 57.173  65.977 19.032  1.00 22.08 ? 270  VAL A CG2 1 
ATOM   1969  N  N   . VAL A  1 271 ? 56.391  70.578 19.112  1.00 24.09 ? 271  VAL A N   1 
ATOM   1970  C  CA  . VAL A  1 271 ? 56.613  71.961 18.724  1.00 25.36 ? 271  VAL A CA  1 
ATOM   1971  C  C   . VAL A  1 271 ? 57.771  72.594 19.479  1.00 25.57 ? 271  VAL A C   1 
ATOM   1972  O  O   . VAL A  1 271 ? 57.955  72.341 20.672  1.00 25.34 ? 271  VAL A O   1 
ATOM   1973  C  CB  . VAL A  1 271 ? 55.322  72.814 18.935  1.00 25.90 ? 271  VAL A CB  1 
ATOM   1974  C  CG1 . VAL A  1 271 ? 54.845  72.718 20.381  1.00 25.77 ? 271  VAL A CG1 1 
ATOM   1975  C  CG2 . VAL A  1 271 ? 55.596  74.269 18.577  1.00 26.75 ? 271  VAL A CG2 1 
ATOM   1976  N  N   . ASN A  1 272 ? 58.560  73.407 18.772  1.00 25.93 ? 272  ASN A N   1 
ATOM   1977  C  CA  . ASN A  1 272 ? 59.697  74.095 19.384  1.00 26.00 ? 272  ASN A CA  1 
ATOM   1978  C  C   . ASN A  1 272 ? 59.204  75.375 20.037  1.00 26.31 ? 272  ASN A C   1 
ATOM   1979  O  O   . ASN A  1 272 ? 58.792  76.307 19.337  1.00 27.43 ? 272  ASN A O   1 
ATOM   1980  C  CB  . ASN A  1 272 ? 60.743  74.468 18.329  1.00 27.00 ? 272  ASN A CB  1 
ATOM   1981  C  CG  . ASN A  1 272 ? 62.041  74.975 18.954  1.00 28.40 ? 272  ASN A CG  1 
ATOM   1982  O  OD1 . ASN A  1 272 ? 62.032  75.664 19.989  1.00 27.23 ? 272  ASN A OD1 1 
ATOM   1983  N  ND2 . ASN A  1 272 ? 63.168  74.634 18.328  1.00 29.58 ? 272  ASN A ND2 1 
ATOM   1984  N  N   . THR A  1 273 ? 59.255  75.449 21.361  1.00 25.91 ? 273  THR A N   1 
ATOM   1985  C  CA  . THR A  1 273 ? 58.782  76.651 22.021  1.00 26.70 ? 273  THR A CA  1 
ATOM   1986  C  C   . THR A  1 273 ? 59.843  77.749 22.101  1.00 28.39 ? 273  THR A C   1 
ATOM   1987  O  O   . THR A  1 273 ? 59.538  78.865 22.519  1.00 28.30 ? 273  THR A O   1 
ATOM   1988  C  CB  . THR A  1 273 ? 58.239  76.359 23.454  1.00 26.21 ? 273  THR A CB  1 
ATOM   1989  O  OG1 . THR A  1 273 ? 59.319  75.982 24.317  1.00 26.51 ? 273  THR A OG1 1 
ATOM   1990  C  CG2 . THR A  1 273 ? 57.209  75.219 23.416  1.00 25.13 ? 273  THR A CG2 1 
ATOM   1991  N  N   . ASP A  1 274 ? 61.081  77.455 21.710  1.00 29.38 ? 274  ASP A N   1 
ATOM   1992  C  CA  . ASP A  1 274 ? 62.114  78.492 21.747  1.00 31.71 ? 274  ASP A CA  1 
ATOM   1993  C  C   . ASP A  1 274 ? 62.056  79.371 20.486  1.00 32.68 ? 274  ASP A C   1 
ATOM   1994  O  O   . ASP A  1 274 ? 62.660  80.436 20.427  1.00 33.16 ? 274  ASP A O   1 
ATOM   1995  C  CB  . ASP A  1 274 ? 63.516  77.875 21.889  1.00 31.67 ? 274  ASP A CB  1 
ATOM   1996  C  CG  . ASP A  1 274 ? 63.841  77.459 23.320  1.00 33.23 ? 274  ASP A CG  1 
ATOM   1997  O  OD1 . ASP A  1 274 ? 63.166  77.919 24.268  1.00 32.54 ? 274  ASP A OD1 1 
ATOM   1998  O  OD2 . ASP A  1 274 ? 64.801  76.674 23.498  1.00 35.13 ? 274  ASP A OD2 1 
ATOM   1999  N  N   . SER A  1 275 ? 61.315  78.931 19.480  1.00 33.24 ? 275  SER A N   1 
ATOM   2000  C  CA  . SER A  1 275 ? 61.222  79.707 18.259  1.00 34.04 ? 275  SER A CA  1 
ATOM   2001  C  C   . SER A  1 275 ? 59.808  80.163 17.941  1.00 34.51 ? 275  SER A C   1 
ATOM   2002  O  O   . SER A  1 275 ? 59.407  80.200 16.779  1.00 34.68 ? 275  SER A O   1 
ATOM   2003  C  CB  . SER A  1 275 ? 61.783  78.896 17.097  1.00 33.62 ? 275  SER A CB  1 
ATOM   2004  O  OG  . SER A  1 275 ? 61.286  77.573 17.148  1.00 35.12 ? 275  SER A OG  1 
ATOM   2005  N  N   . LEU A  1 276 ? 59.044  80.521 18.966  1.00 35.08 ? 276  LEU A N   1 
ATOM   2006  C  CA  . LEU A  1 276 ? 57.683  80.978 18.720  1.00 35.41 ? 276  LEU A CA  1 
ATOM   2007  C  C   . LEU A  1 276 ? 57.712  82.442 18.298  1.00 36.36 ? 276  LEU A C   1 
ATOM   2008  O  O   . LEU A  1 276 ? 58.585  83.197 18.720  1.00 36.86 ? 276  LEU A O   1 
ATOM   2009  C  CB  . LEU A  1 276 ? 56.826  80.805 19.975  1.00 34.59 ? 276  LEU A CB  1 
ATOM   2010  C  CG  . LEU A  1 276 ? 56.679  79.357 20.466  1.00 33.51 ? 276  LEU A CG  1 
ATOM   2011  C  CD1 . LEU A  1 276 ? 56.059  79.348 21.851  1.00 32.98 ? 276  LEU A CD1 1 
ATOM   2012  C  CD2 . LEU A  1 276 ? 55.845  78.564 19.487  1.00 31.87 ? 276  LEU A CD2 1 
ATOM   2013  N  N   . SER A  1 277 ? 56.759  82.826 17.454  1.00 37.37 ? 277  SER A N   1 
ATOM   2014  C  CA  . SER A  1 277 ? 56.652  84.194 16.957  1.00 38.62 ? 277  SER A CA  1 
ATOM   2015  C  C   . SER A  1 277 ? 55.283  84.811 17.200  1.00 39.67 ? 277  SER A C   1 
ATOM   2016  O  O   . SER A  1 277 ? 54.248  84.173 16.986  1.00 39.86 ? 277  SER A O   1 
ATOM   2017  C  CB  . SER A  1 277 ? 56.914  84.251 15.454  1.00 38.38 ? 277  SER A CB  1 
ATOM   2018  O  OG  . SER A  1 277 ? 56.434  85.486 14.941  1.00 37.97 ? 277  SER A OG  1 
ATOM   2019  N  N   . SER A  1 278 ? 55.280  86.071 17.611  1.00 40.64 ? 278  SER A N   1 
ATOM   2020  C  CA  . SER A  1 278 ? 54.031  86.772 17.859  1.00 42.30 ? 278  SER A CA  1 
ATOM   2021  C  C   . SER A  1 278 ? 53.417  87.277 16.551  1.00 42.36 ? 278  SER A C   1 
ATOM   2022  O  O   . SER A  1 278 ? 52.323  87.848 16.552  1.00 42.66 ? 278  SER A O   1 
ATOM   2023  C  CB  . SER A  1 278 ? 54.282  87.939 18.805  1.00 43.17 ? 278  SER A CB  1 
ATOM   2024  O  OG  . SER A  1 278 ? 55.441  88.645 18.399  1.00 45.17 ? 278  SER A OG  1 
ATOM   2025  N  N   . VAL A  1 279 ? 54.116  87.050 15.440  1.00 42.25 ? 279  VAL A N   1 
ATOM   2026  C  CA  . VAL A  1 279 ? 53.647  87.492 14.122  1.00 42.58 ? 279  VAL A CA  1 
ATOM   2027  C  C   . VAL A  1 279 ? 53.264  86.308 13.238  1.00 42.05 ? 279  VAL A C   1 
ATOM   2028  O  O   . VAL A  1 279 ? 52.470  86.437 12.303  1.00 42.54 ? 279  VAL A O   1 
ATOM   2029  C  CB  . VAL A  1 279 ? 54.746  88.308 13.386  1.00 43.19 ? 279  VAL A CB  1 
ATOM   2030  C  CG1 . VAL A  1 279 ? 54.156  88.981 12.150  1.00 43.72 ? 279  VAL A CG1 1 
ATOM   2031  C  CG2 . VAL A  1 279 ? 55.354  89.340 14.329  1.00 43.20 ? 279  VAL A CG2 1 
ATOM   2032  N  N   . THR A  1 280 ? 53.839  85.151 13.534  1.00 41.13 ? 280  THR A N   1 
ATOM   2033  C  CA  . THR A  1 280 ? 53.552  83.957 12.759  1.00 40.32 ? 280  THR A CA  1 
ATOM   2034  C  C   . THR A  1 280 ? 52.991  82.853 13.646  1.00 39.52 ? 280  THR A C   1 
ATOM   2035  O  O   . THR A  1 280 ? 53.316  82.776 14.834  1.00 38.24 ? 280  THR A O   1 
ATOM   2036  C  CB  . THR A  1 280 ? 54.821  83.462 12.066  1.00 41.20 ? 280  THR A CB  1 
ATOM   2037  O  OG1 . THR A  1 280 ? 55.264  84.466 11.140  1.00 42.62 ? 280  THR A OG1 1 
ATOM   2038  C  CG2 . THR A  1 280 ? 54.559  82.151 11.324  1.00 41.00 ? 280  THR A CG2 1 
ATOM   2039  N  N   . ASN A  1 281 ? 52.136  82.009 13.072  1.00 38.51 ? 281  ASN A N   1 
ATOM   2040  C  CA  . ASN A  1 281 ? 51.558  80.913 13.837  1.00 37.88 ? 281  ASN A CA  1 
ATOM   2041  C  C   . ASN A  1 281 ? 52.613  79.836 14.043  1.00 37.56 ? 281  ASN A C   1 
ATOM   2042  O  O   . ASN A  1 281 ? 53.436  79.573 13.160  1.00 37.57 ? 281  ASN A O   1 
ATOM   2043  C  CB  . ASN A  1 281 ? 50.331  80.328 13.131  1.00 37.73 ? 281  ASN A CB  1 
ATOM   2044  C  CG  . ASN A  1 281 ? 49.097  81.196 13.293  1.00 37.42 ? 281  ASN A CG  1 
ATOM   2045  O  OD1 . ASN A  1 281 ? 48.896  81.812 14.350  1.00 37.45 ? 281  ASN A OD1 1 
ATOM   2046  N  ND2 . ASN A  1 281 ? 48.257  81.226 12.259  1.00 38.55 ? 281  ASN A ND2 1 
ATOM   2047  N  N   . ALA A  1 282 ? 52.592  79.225 15.222  1.00 36.85 ? 282  ALA A N   1 
ATOM   2048  C  CA  . ALA A  1 282 ? 53.554  78.183 15.570  1.00 35.35 ? 282  ALA A CA  1 
ATOM   2049  C  C   . ALA A  1 282 ? 53.449  77.024 14.608  1.00 34.56 ? 282  ALA A C   1 
ATOM   2050  O  O   . ALA A  1 282 ? 52.372  76.724 14.107  1.00 34.27 ? 282  ALA A O   1 
ATOM   2051  C  CB  . ALA A  1 282 ? 53.298  77.698 16.993  1.00 35.48 ? 282  ALA A CB  1 
ATOM   2052  N  N   . THR A  1 283 ? 54.569  76.370 14.342  1.00 34.20 ? 283  THR A N   1 
ATOM   2053  C  CA  . THR A  1 283 ? 54.559  75.222 13.451  1.00 34.18 ? 283  THR A CA  1 
ATOM   2054  C  C   . THR A  1 283 ? 54.781  73.953 14.270  1.00 33.47 ? 283  THR A C   1 
ATOM   2055  O  O   . THR A  1 283 ? 55.782  73.830 14.965  1.00 33.73 ? 283  THR A O   1 
ATOM   2056  C  CB  . THR A  1 283 ? 55.656  75.329 12.382  1.00 35.64 ? 283  THR A CB  1 
ATOM   2057  O  OG1 . THR A  1 283 ? 55.413  76.485 11.568  1.00 37.53 ? 283  THR A OG1 1 
ATOM   2058  C  CG2 . THR A  1 283 ? 55.652  74.087 11.506  1.00 35.85 ? 283  THR A CG2 1 
ATOM   2059  N  N   . SER A  1 284 ? 53.838  73.019 14.189  1.00 31.56 ? 284  SER A N   1 
ATOM   2060  C  CA  . SER A  1 284 ? 53.938  71.770 14.922  1.00 30.03 ? 284  SER A CA  1 
ATOM   2061  C  C   . SER A  1 284 ? 54.361  70.672 13.970  1.00 28.72 ? 284  SER A C   1 
ATOM   2062  O  O   . SER A  1 284 ? 53.796  70.535 12.890  1.00 28.20 ? 284  SER A O   1 
ATOM   2063  C  CB  . SER A  1 284 ? 52.589  71.404 15.567  1.00 30.19 ? 284  SER A CB  1 
ATOM   2064  O  OG  . SER A  1 284 ? 52.284  72.251 16.665  1.00 30.29 ? 284  SER A OG  1 
ATOM   2065  N  N   . ILE A  1 285 ? 55.367  69.901 14.376  1.00 27.14 ? 285  ILE A N   1 
ATOM   2066  C  CA  . ILE A  1 285 ? 55.874  68.787 13.576  1.00 26.23 ? 285  ILE A CA  1 
ATOM   2067  C  C   . ILE A  1 285 ? 55.185  67.497 14.027  1.00 25.66 ? 285  ILE A C   1 
ATOM   2068  O  O   . ILE A  1 285 ? 55.260  67.103 15.199  1.00 24.15 ? 285  ILE A O   1 
ATOM   2069  C  CB  . ILE A  1 285 ? 57.398  68.602 13.761  1.00 25.82 ? 285  ILE A CB  1 
ATOM   2070  C  CG1 . ILE A  1 285 ? 58.135  69.915 13.455  1.00 27.03 ? 285  ILE A CG1 1 
ATOM   2071  C  CG2 . ILE A  1 285 ? 57.893  67.507 12.845  1.00 25.37 ? 285  ILE A CG2 1 
ATOM   2072  C  CD1 . ILE A  1 285 ? 58.045  70.336 11.993  1.00 27.98 ? 285  ILE A CD1 1 
ATOM   2073  N  N   . GLN A  1 286 ? 54.528  66.834 13.090  1.00 24.69 ? 286  GLN A N   1 
ATOM   2074  C  CA  . GLN A  1 286 ? 53.838  65.612 13.410  1.00 25.38 ? 286  GLN A CA  1 
ATOM   2075  C  C   . GLN A  1 286 ? 54.765  64.411 13.344  1.00 26.24 ? 286  GLN A C   1 
ATOM   2076  O  O   . GLN A  1 286 ? 55.727  64.397 12.573  1.00 25.95 ? 286  GLN A O   1 
ATOM   2077  C  CB  . GLN A  1 286 ? 52.684  65.408 12.440  1.00 25.65 ? 286  GLN A CB  1 
ATOM   2078  C  CG  . GLN A  1 286 ? 51.971  64.085 12.578  1.00 25.34 ? 286  GLN A CG  1 
ATOM   2079  C  CD  . GLN A  1 286 ? 50.667  64.082 11.810  1.00 26.70 ? 286  GLN A CD  1 
ATOM   2080  O  OE1 . GLN A  1 286 ? 50.369  65.031 11.095  1.00 26.89 ? 286  GLN A OE1 1 
ATOM   2081  N  NE2 . GLN A  1 286 ? 49.881  63.027 11.961  1.00 25.95 ? 286  GLN A NE2 1 
ATOM   2082  N  N   . ILE A  1 287 ? 54.477  63.421 14.186  1.00 25.30 ? 287  ILE A N   1 
ATOM   2083  C  CA  . ILE A  1 287 ? 55.218  62.180 14.190  1.00 25.53 ? 287  ILE A CA  1 
ATOM   2084  C  C   . ILE A  1 287 ? 54.145  61.137 13.975  1.00 26.59 ? 287  ILE A C   1 
ATOM   2085  O  O   . ILE A  1 287 ? 53.346  60.828 14.883  1.00 26.47 ? 287  ILE A O   1 
ATOM   2086  C  CB  . ILE A  1 287 ? 55.927  61.930 15.524  1.00 24.29 ? 287  ILE A CB  1 
ATOM   2087  C  CG1 . ILE A  1 287 ? 56.960  63.032 15.756  1.00 24.33 ? 287  ILE A CG1 1 
ATOM   2088  C  CG2 . ILE A  1 287 ? 56.568  60.557 15.509  1.00 23.23 ? 287  ILE A CG2 1 
ATOM   2089  C  CD1 . ILE A  1 287 ? 57.835  62.839 16.995  1.00 24.23 ? 287  ILE A CD1 1 
ATOM   2090  N  N   . THR A  1 288 ? 54.104  60.618 12.757  1.00 26.81 ? 288  THR A N   1 
ATOM   2091  C  CA  . THR A  1 288 ? 53.107  59.626 12.395  1.00 27.57 ? 288  THR A CA  1 
ATOM   2092  C  C   . THR A  1 288 ? 53.414  58.291 13.051  1.00 28.38 ? 288  THR A C   1 
ATOM   2093  O  O   . THR A  1 288 ? 54.571  57.983 13.353  1.00 27.71 ? 288  THR A O   1 
ATOM   2094  C  CB  . THR A  1 288 ? 53.058  59.466 10.868  1.00 28.19 ? 288  THR A CB  1 
ATOM   2095  O  OG1 . THR A  1 288 ? 54.376  59.202 10.384  1.00 29.47 ? 288  THR A OG1 1 
ATOM   2096  C  CG2 . THR A  1 288 ? 52.580  60.751 10.216  1.00 29.52 ? 288  THR A CG2 1 
ATOM   2097  N  N   . ALA A  1 289 ? 52.371  57.503 13.284  1.00 29.42 ? 289  ALA A N   1 
ATOM   2098  C  CA  . ALA A  1 289 ? 52.528  56.195 13.916  1.00 30.99 ? 289  ALA A CA  1 
ATOM   2099  C  C   . ALA A  1 289 ? 53.119  55.249 12.885  1.00 32.07 ? 289  ALA A C   1 
ATOM   2100  O  O   . ALA A  1 289 ? 53.054  55.524 11.691  1.00 32.77 ? 289  ALA A O   1 
ATOM   2101  C  CB  . ALA A  1 289 ? 51.163  55.675 14.394  1.00 30.35 ? 289  ALA A CB  1 
ATOM   2102  N  N   . PRO A  1 290 ? 53.708  54.130 13.326  1.00 33.09 ? 290  PRO A N   1 
ATOM   2103  C  CA  . PRO A  1 290 ? 54.283  53.197 12.359  1.00 34.14 ? 290  PRO A CA  1 
ATOM   2104  C  C   . PRO A  1 290 ? 53.216  52.568 11.464  1.00 35.49 ? 290  PRO A C   1 
ATOM   2105  O  O   . PRO A  1 290 ? 52.033  52.496 11.835  1.00 35.08 ? 290  PRO A O   1 
ATOM   2106  C  CB  . PRO A  1 290 ? 55.002  52.178 13.245  1.00 33.52 ? 290  PRO A CB  1 
ATOM   2107  C  CG  . PRO A  1 290 ? 54.230  52.210 14.496  1.00 33.93 ? 290  PRO A CG  1 
ATOM   2108  C  CD  . PRO A  1 290 ? 53.977  53.680 14.700  1.00 33.10 ? 290  PRO A CD  1 
ATOM   2109  N  N   . ALA A  1 291 ? 53.648  52.120 10.285  1.00 35.65 ? 291  ALA A N   1 
ATOM   2110  C  CA  . ALA A  1 291 ? 52.763  51.514 9.290   1.00 35.38 ? 291  ALA A CA  1 
ATOM   2111  C  C   . ALA A  1 291 ? 51.959  50.343 9.829   1.00 34.69 ? 291  ALA A C   1 
ATOM   2112  O  O   . ALA A  1 291 ? 50.787  50.185 9.492   1.00 34.97 ? 291  ALA A O   1 
ATOM   2113  C  CB  . ALA A  1 291 ? 53.584  51.070 8.062   1.00 35.76 ? 291  ALA A CB  1 
ATOM   2114  N  N   . SER A  1 292 ? 52.594  49.527 10.661  1.00 34.17 ? 292  SER A N   1 
ATOM   2115  C  CA  . SER A  1 292 ? 51.943  48.364 11.238  1.00 34.45 ? 292  SER A CA  1 
ATOM   2116  C  C   . SER A  1 292 ? 50.822  48.779 12.188  1.00 34.67 ? 292  SER A C   1 
ATOM   2117  O  O   . SER A  1 292 ? 50.022  47.952 12.643  1.00 34.72 ? 292  SER A O   1 
ATOM   2118  C  CB  . SER A  1 292 ? 52.965  47.532 12.005  1.00 34.83 ? 292  SER A CB  1 
ATOM   2119  O  OG  . SER A  1 292 ? 53.516  48.296 13.066  1.00 35.18 ? 292  SER A OG  1 
ATOM   2120  N  N   . MET A  1 293 ? 50.779  50.069 12.486  1.00 34.33 ? 293  MET A N   1 
ATOM   2121  C  CA  . MET A  1 293 ? 49.783  50.617 13.388  1.00 34.33 ? 293  MET A CA  1 
ATOM   2122  C  C   . MET A  1 293 ? 48.733  51.306 12.518  1.00 33.97 ? 293  MET A C   1 
ATOM   2123  O  O   . MET A  1 293 ? 47.538  51.137 12.714  1.00 34.06 ? 293  MET A O   1 
ATOM   2124  C  CB  . MET A  1 293 ? 50.474  51.612 14.332  1.00 33.08 ? 293  MET A CB  1 
ATOM   2125  C  CG  . MET A  1 293 ? 50.041  51.576 15.776  1.00 32.73 ? 293  MET A CG  1 
ATOM   2126  S  SD  . MET A  1 293 ? 49.917  49.977 16.579  1.00 30.55 ? 293  MET A SD  1 
ATOM   2127  C  CE  . MET A  1 293 ? 51.522  49.665 17.174  1.00 31.22 ? 293  MET A CE  1 
ATOM   2128  N  N   . LEU A  1 294 ? 49.183  52.049 11.517  1.00 34.26 ? 294  LEU A N   1 
ATOM   2129  C  CA  . LEU A  1 294 ? 48.259  52.753 10.639  1.00 34.14 ? 294  LEU A CA  1 
ATOM   2130  C  C   . LEU A  1 294 ? 47.361  51.843 9.794   1.00 33.66 ? 294  LEU A C   1 
ATOM   2131  O  O   . LEU A  1 294 ? 46.429  52.319 9.163   1.00 33.49 ? 294  LEU A O   1 
ATOM   2132  C  CB  . LEU A  1 294 ? 49.024  53.726 9.732   1.00 33.84 ? 294  LEU A CB  1 
ATOM   2133  C  CG  . LEU A  1 294 ? 49.571  55.009 10.382  1.00 34.95 ? 294  LEU A CG  1 
ATOM   2134  C  CD1 . LEU A  1 294 ? 50.328  55.832 9.346   1.00 34.90 ? 294  LEU A CD1 1 
ATOM   2135  C  CD2 . LEU A  1 294 ? 48.432  55.838 10.946  1.00 34.42 ? 294  LEU A CD2 1 
ATOM   2136  N  N   . ILE A  1 295 ? 47.613  50.539 9.797   1.00 33.25 ? 295  ILE A N   1 
ATOM   2137  C  CA  . ILE A  1 295 ? 46.784  49.619 9.016   1.00 33.24 ? 295  ILE A CA  1 
ATOM   2138  C  C   . ILE A  1 295 ? 45.346  49.515 9.539   1.00 32.57 ? 295  ILE A C   1 
ATOM   2139  O  O   . ILE A  1 295 ? 44.416  49.259 8.770   1.00 32.71 ? 295  ILE A O   1 
ATOM   2140  C  CB  . ILE A  1 295 ? 47.357  48.186 9.002   1.00 34.00 ? 295  ILE A CB  1 
ATOM   2141  C  CG1 . ILE A  1 295 ? 47.511  47.689 10.438  1.00 34.28 ? 295  ILE A CG1 1 
ATOM   2142  C  CG2 . ILE A  1 295 ? 48.683  48.147 8.230   1.00 34.45 ? 295  ILE A CG2 1 
ATOM   2143  C  CD1 . ILE A  1 295 ? 47.855  46.217 10.551  1.00 35.06 ? 295  ILE A CD1 1 
ATOM   2144  N  N   . GLY A  1 296 ? 45.173  49.681 10.848  1.00 31.21 ? 296  GLY A N   1 
ATOM   2145  C  CA  . GLY A  1 296 ? 43.848  49.603 11.450  1.00 28.99 ? 296  GLY A CA  1 
ATOM   2146  C  C   . GLY A  1 296 ? 43.676  50.581 12.605  1.00 27.75 ? 296  GLY A C   1 
ATOM   2147  O  O   . GLY A  1 296 ? 44.421  51.558 12.725  1.00 27.76 ? 296  GLY A O   1 
ATOM   2148  N  N   . ASP A  1 297 ? 42.677  50.341 13.448  1.00 26.25 ? 297  ASP A N   1 
ATOM   2149  C  CA  . ASP A  1 297 ? 42.455  51.203 14.603  1.00 24.47 ? 297  ASP A CA  1 
ATOM   2150  C  C   . ASP A  1 297 ? 43.607  50.992 15.569  1.00 22.57 ? 297  ASP A C   1 
ATOM   2151  O  O   . ASP A  1 297 ? 44.103  49.870 15.732  1.00 22.01 ? 297  ASP A O   1 
ATOM   2152  C  CB  . ASP A  1 297 ? 41.154  50.850 15.329  1.00 24.33 ? 297  ASP A CB  1 
ATOM   2153  C  CG  . ASP A  1 297 ? 39.924  51.327 14.594  1.00 24.30 ? 297  ASP A CG  1 
ATOM   2154  O  OD1 . ASP A  1 297 ? 40.074  52.067 13.611  1.00 25.90 ? 297  ASP A OD1 1 
ATOM   2155  O  OD2 . ASP A  1 297 ? 38.801  50.969 15.011  1.00 25.20 ? 297  ASP A OD2 1 
ATOM   2156  N  N   . HIS A  1 298 ? 44.026  52.068 16.226  1.00 22.13 ? 298  HIS A N   1 
ATOM   2157  C  CA  . HIS A  1 298 ? 45.114  51.961 17.186  1.00 20.92 ? 298  HIS A CA  1 
ATOM   2158  C  C   . HIS A  1 298 ? 44.985  53.058 18.223  1.00 20.74 ? 298  HIS A C   1 
ATOM   2159  O  O   . HIS A  1 298 ? 44.096  53.915 18.138  1.00 21.07 ? 298  HIS A O   1 
ATOM   2160  C  CB  . HIS A  1 298 ? 46.459  52.091 16.469  1.00 20.47 ? 298  HIS A CB  1 
ATOM   2161  C  CG  . HIS A  1 298 ? 46.567  53.332 15.643  1.00 20.26 ? 298  HIS A CG  1 
ATOM   2162  N  ND1 . HIS A  1 298 ? 45.991  53.444 14.400  1.00 19.96 ? 298  HIS A ND1 1 
ATOM   2163  C  CD2 . HIS A  1 298 ? 47.132  54.534 15.907  1.00 20.92 ? 298  HIS A CD2 1 
ATOM   2164  C  CE1 . HIS A  1 298 ? 46.193  54.663 13.929  1.00 21.67 ? 298  HIS A CE1 1 
ATOM   2165  N  NE2 . HIS A  1 298 ? 46.885  55.345 14.826  1.00 20.25 ? 298  HIS A NE2 1 
ATOM   2166  N  N   . TYR A  1 299 ? 45.894  53.023 19.188  1.00 19.93 ? 299  TYR A N   1 
ATOM   2167  C  CA  . TYR A  1 299 ? 45.934  53.984 20.274  1.00 20.32 ? 299  TYR A CA  1 
ATOM   2168  C  C   . TYR A  1 299 ? 47.378  54.427 20.485  1.00 20.64 ? 299  TYR A C   1 
ATOM   2169  O  O   . TYR A  1 299 ? 48.323  53.721 20.088  1.00 19.60 ? 299  TYR A O   1 
ATOM   2170  C  CB  . TYR A  1 299 ? 45.498  53.347 21.601  1.00 18.91 ? 299  TYR A CB  1 
ATOM   2171  C  CG  . TYR A  1 299 ? 44.168  52.622 21.617  1.00 19.15 ? 299  TYR A CG  1 
ATOM   2172  C  CD1 . TYR A  1 299 ? 42.962  53.325 21.595  1.00 17.66 ? 299  TYR A CD1 1 
ATOM   2173  C  CD2 . TYR A  1 299 ? 44.117  51.231 21.729  1.00 18.78 ? 299  TYR A CD2 1 
ATOM   2174  C  CE1 . TYR A  1 299 ? 41.733  52.662 21.688  1.00 17.60 ? 299  TYR A CE1 1 
ATOM   2175  C  CE2 . TYR A  1 299 ? 42.896  50.552 21.828  1.00 18.72 ? 299  TYR A CE2 1 
ATOM   2176  C  CZ  . TYR A  1 299 ? 41.709  51.273 21.807  1.00 18.74 ? 299  TYR A CZ  1 
ATOM   2177  O  OH  . TYR A  1 299 ? 40.506  50.615 21.911  1.00 17.68 ? 299  TYR A OH  1 
ATOM   2178  N  N   . LEU A  1 300 ? 47.521  55.595 21.115  1.00 19.60 ? 300  LEU A N   1 
ATOM   2179  C  CA  . LEU A  1 300 ? 48.818  56.129 21.516  1.00 19.49 ? 300  LEU A CA  1 
ATOM   2180  C  C   . LEU A  1 300 ? 48.767  55.723 22.989  1.00 19.08 ? 300  LEU A C   1 
ATOM   2181  O  O   . LEU A  1 300 ? 47.808  56.069 23.670  1.00 18.48 ? 300  LEU A O   1 
ATOM   2182  C  CB  . LEU A  1 300 ? 48.840  57.655 21.412  1.00 18.87 ? 300  LEU A CB  1 
ATOM   2183  C  CG  . LEU A  1 300 ? 50.073  58.320 22.044  1.00 18.97 ? 300  LEU A CG  1 
ATOM   2184  C  CD1 . LEU A  1 300 ? 51.314  57.777 21.377  1.00 19.31 ? 300  LEU A CD1 1 
ATOM   2185  C  CD2 . LEU A  1 300 ? 50.006  59.833 21.895  1.00 20.30 ? 300  LEU A CD2 1 
ATOM   2186  N  N   . CYS A  1 301 ? 49.752  54.986 23.493  1.00 19.86 ? 301  CYS A N   1 
ATOM   2187  C  CA  . CYS A  1 301 ? 49.680  54.559 24.893  1.00 19.97 ? 301  CYS A CA  1 
ATOM   2188  C  C   . CYS A  1 301 ? 50.806  55.036 25.808  1.00 20.39 ? 301  CYS A C   1 
ATOM   2189  O  O   . CYS A  1 301 ? 50.746  54.845 27.021  1.00 20.16 ? 301  CYS A O   1 
ATOM   2190  C  CB  . CYS A  1 301 ? 49.560  53.027 24.977  1.00 20.83 ? 301  CYS A CB  1 
ATOM   2191  S  SG  . CYS A  1 301 ? 50.833  52.139 24.036  1.00 24.74 ? 301  CYS A SG  1 
ATOM   2192  N  N   . ASP A  1 302 ? 51.832  55.656 25.242  1.00 20.67 ? 302  ASP A N   1 
ATOM   2193  C  CA  . ASP A  1 302 ? 52.922  56.173 26.059  1.00 20.43 ? 302  ASP A CA  1 
ATOM   2194  C  C   . ASP A  1 302 ? 53.746  57.208 25.332  1.00 20.09 ? 302  ASP A C   1 
ATOM   2195  O  O   . ASP A  1 302 ? 53.931  57.137 24.116  1.00 20.19 ? 302  ASP A O   1 
ATOM   2196  C  CB  . ASP A  1 302 ? 53.880  55.067 26.525  1.00 20.49 ? 302  ASP A CB  1 
ATOM   2197  C  CG  . ASP A  1 302 ? 54.985  55.608 27.428  1.00 20.55 ? 302  ASP A CG  1 
ATOM   2198  O  OD1 . ASP A  1 302 ? 56.001  56.156 26.930  1.00 19.44 ? 302  ASP A OD1 1 
ATOM   2199  O  OD2 . ASP A  1 302 ? 54.824  55.512 28.660  1.00 20.86 ? 302  ASP A OD2 1 
ATOM   2200  N  N   . VAL A  1 303 ? 54.231  58.176 26.099  1.00 19.66 ? 303  VAL A N   1 
ATOM   2201  C  CA  . VAL A  1 303 ? 55.102  59.228 25.580  1.00 20.11 ? 303  VAL A CA  1 
ATOM   2202  C  C   . VAL A  1 303 ? 56.127  59.457 26.669  1.00 19.29 ? 303  VAL A C   1 
ATOM   2203  O  O   . VAL A  1 303 ? 55.771  59.778 27.809  1.00 18.26 ? 303  VAL A O   1 
ATOM   2204  C  CB  . VAL A  1 303 ? 54.372  60.571 25.353  1.00 19.94 ? 303  VAL A CB  1 
ATOM   2205  C  CG1 . VAL A  1 303 ? 55.380  61.618 24.935  1.00 19.79 ? 303  VAL A CG1 1 
ATOM   2206  C  CG2 . VAL A  1 303 ? 53.279  60.423 24.302  1.00 19.72 ? 303  VAL A CG2 1 
ATOM   2207  N  N   . THR A  1 304 ? 57.400  59.283 26.326  1.00 20.00 ? 304  THR A N   1 
ATOM   2208  C  CA  . THR A  1 304 ? 58.463  59.483 27.298  1.00 19.98 ? 304  THR A CA  1 
ATOM   2209  C  C   . THR A  1 304 ? 59.710  60.112 26.669  1.00 21.51 ? 304  THR A C   1 
ATOM   2210  O  O   . THR A  1 304 ? 60.350  59.508 25.798  1.00 21.96 ? 304  THR A O   1 
ATOM   2211  C  CB  . THR A  1 304 ? 58.884  58.152 27.950  1.00 20.21 ? 304  THR A CB  1 
ATOM   2212  O  OG1 . THR A  1 304 ? 57.750  57.522 28.555  1.00 18.02 ? 304  THR A OG1 1 
ATOM   2213  C  CG2 . THR A  1 304 ? 59.945  58.411 29.025  1.00 19.87 ? 304  THR A CG2 1 
ATOM   2214  N  N   . TRP A  1 305 ? 60.060  61.318 27.100  1.00 20.36 ? 305  TRP A N   1 
ATOM   2215  C  CA  . TRP A  1 305 ? 61.247  61.960 26.556  1.00 21.71 ? 305  TRP A CA  1 
ATOM   2216  C  C   . TRP A  1 305 ? 62.477  61.199 27.051  1.00 21.74 ? 305  TRP A C   1 
ATOM   2217  O  O   . TRP A  1 305 ? 62.520  60.784 28.213  1.00 21.24 ? 305  TRP A O   1 
ATOM   2218  C  CB  . TRP A  1 305 ? 61.331  63.414 27.010  1.00 20.75 ? 305  TRP A CB  1 
ATOM   2219  C  CG  . TRP A  1 305 ? 60.465  64.337 26.225  1.00 22.14 ? 305  TRP A CG  1 
ATOM   2220  C  CD1 . TRP A  1 305 ? 59.183  64.704 26.513  1.00 21.92 ? 305  TRP A CD1 1 
ATOM   2221  C  CD2 . TRP A  1 305 ? 60.809  64.997 25.000  1.00 22.97 ? 305  TRP A CD2 1 
ATOM   2222  N  NE1 . TRP A  1 305 ? 58.702  65.553 25.543  1.00 23.17 ? 305  TRP A NE1 1 
ATOM   2223  C  CE2 . TRP A  1 305 ? 59.679  65.747 24.599  1.00 23.06 ? 305  TRP A CE2 1 
ATOM   2224  C  CE3 . TRP A  1 305 ? 61.962  65.023 24.198  1.00 21.78 ? 305  TRP A CE3 1 
ATOM   2225  C  CZ2 . TRP A  1 305 ? 59.666  66.515 23.436  1.00 22.29 ? 305  TRP A CZ2 1 
ATOM   2226  C  CZ3 . TRP A  1 305 ? 61.950  65.786 23.039  1.00 23.21 ? 305  TRP A CZ3 1 
ATOM   2227  C  CH2 . TRP A  1 305 ? 60.809  66.522 22.667  1.00 22.99 ? 305  TRP A CH2 1 
ATOM   2228  N  N   . ALA A  1 306 ? 63.456  60.999 26.174  1.00 21.49 ? 306  ALA A N   1 
ATOM   2229  C  CA  . ALA A  1 306 ? 64.693  60.300 26.541  1.00 22.99 ? 306  ALA A CA  1 
ATOM   2230  C  C   . ALA A  1 306 ? 65.814  61.314 26.809  1.00 23.51 ? 306  ALA A C   1 
ATOM   2231  O  O   . ALA A  1 306 ? 66.598  61.147 27.742  1.00 24.50 ? 306  ALA A O   1 
ATOM   2232  C  CB  . ALA A  1 306 ? 65.111  59.335 25.421  1.00 21.13 ? 306  ALA A CB  1 
ATOM   2233  N  N   . THR A  1 307 ? 65.887  62.353 25.976  1.00 23.11 ? 307  THR A N   1 
ATOM   2234  C  CA  . THR A  1 307 ? 66.892  63.401 26.129  1.00 23.35 ? 307  THR A CA  1 
ATOM   2235  C  C   . THR A  1 307 ? 66.304  64.699 25.595  1.00 23.89 ? 307  THR A C   1 
ATOM   2236  O  O   . THR A  1 307 ? 65.145  64.745 25.194  1.00 23.49 ? 307  THR A O   1 
ATOM   2237  C  CB  . THR A  1 307 ? 68.156  63.126 25.300  1.00 23.21 ? 307  THR A CB  1 
ATOM   2238  O  OG1 . THR A  1 307 ? 67.811  63.182 23.913  1.00 22.56 ? 307  THR A OG1 1 
ATOM   2239  C  CG2 . THR A  1 307 ? 68.740  61.756 25.613  1.00 23.76 ? 307  THR A CG2 1 
ATOM   2240  N  N   . GLN A  1 308 ? 67.125  65.747 25.557  1.00 23.75 ? 308  GLN A N   1 
ATOM   2241  C  CA  . GLN A  1 308 ? 66.677  67.036 25.045  1.00 23.40 ? 308  GLN A CA  1 
ATOM   2242  C  C   . GLN A  1 308 ? 66.238  66.931 23.576  1.00 23.61 ? 308  GLN A C   1 
ATOM   2243  O  O   . GLN A  1 308 ? 65.444  67.742 23.109  1.00 24.28 ? 308  GLN A O   1 
ATOM   2244  C  CB  . GLN A  1 308 ? 67.805  68.076 25.150  1.00 23.26 ? 308  GLN A CB  1 
ATOM   2245  C  CG  . GLN A  1 308 ? 68.410  68.247 26.529  1.00 23.28 ? 308  GLN A CG  1 
ATOM   2246  C  CD  . GLN A  1 308 ? 67.398  68.643 27.577  1.00 24.24 ? 308  GLN A CD  1 
ATOM   2247  O  OE1 . GLN A  1 308 ? 66.262  69.026 27.260  1.00 25.71 ? 308  GLN A OE1 1 
ATOM   2248  N  NE2 . GLN A  1 308 ? 67.804  68.565 28.844  1.00 23.94 ? 308  GLN A NE2 1 
ATOM   2249  N  N   . GLU A  1 309 ? 66.736  65.933 22.854  1.00 23.59 ? 309  GLU A N   1 
ATOM   2250  C  CA  . GLU A  1 309 ? 66.403  65.802 21.439  1.00 24.33 ? 309  GLU A CA  1 
ATOM   2251  C  C   . GLU A  1 309 ? 65.951  64.413 20.985  1.00 24.41 ? 309  GLU A C   1 
ATOM   2252  O  O   . GLU A  1 309 ? 65.942  64.104 19.786  1.00 25.88 ? 309  GLU A O   1 
ATOM   2253  C  CB  . GLU A  1 309 ? 67.603  66.266 20.604  1.00 25.80 ? 309  GLU A CB  1 
ATOM   2254  C  CG  . GLU A  1 309 ? 67.992  67.726 20.884  1.00 27.07 ? 309  GLU A CG  1 
ATOM   2255  C  CD  . GLU A  1 309 ? 69.252  68.176 20.137  1.00 29.16 ? 309  GLU A CD  1 
ATOM   2256  O  OE1 . GLU A  1 309 ? 69.480  67.691 19.010  1.00 30.12 ? 309  GLU A OE1 1 
ATOM   2257  O  OE2 . GLU A  1 309 ? 69.992  69.028 20.678  1.00 29.18 ? 309  GLU A OE2 1 
ATOM   2258  N  N   . ARG A  1 310 ? 65.567  63.575 21.943  1.00 24.17 ? 310  ARG A N   1 
ATOM   2259  C  CA  . ARG A  1 310 ? 65.102  62.227 21.635  1.00 22.84 ? 310  ARG A CA  1 
ATOM   2260  C  C   . ARG A  1 310 ? 63.813  61.964 22.412  1.00 22.76 ? 310  ARG A C   1 
ATOM   2261  O  O   . ARG A  1 310 ? 63.750  62.175 23.633  1.00 21.52 ? 310  ARG A O   1 
ATOM   2262  C  CB  . ARG A  1 310 ? 66.176  61.193 22.019  1.00 21.39 ? 310  ARG A CB  1 
ATOM   2263  C  CG  . ARG A  1 310 ? 65.751  59.730 21.824  1.00 21.08 ? 310  ARG A CG  1 
ATOM   2264  C  CD  . ARG A  1 310 ? 66.943  58.787 22.034  1.00 22.05 ? 310  ARG A CD  1 
ATOM   2265  N  NE  . ARG A  1 310 ? 67.964  59.060 21.024  1.00 22.65 ? 310  ARG A NE  1 
ATOM   2266  C  CZ  . ARG A  1 310 ? 69.261  58.812 21.156  1.00 23.33 ? 310  ARG A CZ  1 
ATOM   2267  N  NH1 . ARG A  1 310 ? 69.736  58.265 22.274  1.00 22.74 ? 310  ARG A NH1 1 
ATOM   2268  N  NH2 . ARG A  1 310 ? 70.092  59.150 20.174  1.00 23.09 ? 310  ARG A NH2 1 
ATOM   2269  N  N   . ILE A  1 311 ? 62.784  61.507 21.709  1.00 23.24 ? 311  ILE A N   1 
ATOM   2270  C  CA  . ILE A  1 311 ? 61.513  61.206 22.367  1.00 23.04 ? 311  ILE A CA  1 
ATOM   2271  C  C   . ILE A  1 311 ? 61.040  59.837 21.923  1.00 23.76 ? 311  ILE A C   1 
ATOM   2272  O  O   . ILE A  1 311 ? 61.267  59.442 20.781  1.00 24.08 ? 311  ILE A O   1 
ATOM   2273  C  CB  . ILE A  1 311 ? 60.425  62.271 22.029  1.00 23.36 ? 311  ILE A CB  1 
ATOM   2274  C  CG1 . ILE A  1 311 ? 59.133  61.969 22.793  1.00 21.93 ? 311  ILE A CG1 1 
ATOM   2275  C  CG2 . ILE A  1 311 ? 60.139  62.295 20.526  1.00 22.73 ? 311  ILE A CG2 1 
ATOM   2276  C  CD1 . ILE A  1 311 ? 58.112  63.085 22.706  1.00 21.42 ? 311  ILE A CD1 1 
ATOM   2277  N  N   . SER A  1 312 ? 60.423  59.090 22.837  1.00 23.45 ? 312  SER A N   1 
ATOM   2278  C  CA  . SER A  1 312 ? 59.900  57.782 22.491  1.00 23.20 ? 312  SER A CA  1 
ATOM   2279  C  C   . SER A  1 312 ? 58.385  57.820 22.606  1.00 24.15 ? 312  SER A C   1 
ATOM   2280  O  O   . SER A  1 312 ? 57.819  58.536 23.449  1.00 24.19 ? 312  SER A O   1 
ATOM   2281  C  CB  . SER A  1 312 ? 60.449  56.686 23.412  1.00 22.73 ? 312  SER A CB  1 
ATOM   2282  O  OG  . SER A  1 312 ? 59.934  56.784 24.730  1.00 23.49 ? 312  SER A OG  1 
ATOM   2283  N  N   . LEU A  1 313 ? 57.742  57.040 21.750  1.00 25.33 ? 313  LEU A N   1 
ATOM   2284  C  CA  . LEU A  1 313 ? 56.292  56.933 21.718  1.00 26.48 ? 313  LEU A CA  1 
ATOM   2285  C  C   . LEU A  1 313 ? 55.963  55.483 21.576  1.00 26.56 ? 313  LEU A C   1 
ATOM   2286  O  O   . LEU A  1 313 ? 56.697  54.726 20.938  1.00 25.83 ? 313  LEU A O   1 
ATOM   2287  C  CB  . LEU A  1 313 ? 55.708  57.606 20.497  1.00 28.34 ? 313  LEU A CB  1 
ATOM   2288  C  CG  . LEU A  1 313 ? 56.125  59.025 20.241  1.00 31.12 ? 313  LEU A CG  1 
ATOM   2289  C  CD1 . LEU A  1 313 ? 55.429  59.506 18.970  1.00 30.89 ? 313  LEU A CD1 1 
ATOM   2290  C  CD2 . LEU A  1 313 ? 55.753  59.876 21.464  1.00 30.76 ? 313  LEU A CD2 1 
ATOM   2291  N  N   . GLN A  1 314 ? 54.850  55.086 22.166  1.00 26.54 ? 314  GLN A N   1 
ATOM   2292  C  CA  . GLN A  1 314 ? 54.434  53.722 22.010  1.00 27.06 ? 314  GLN A CA  1 
ATOM   2293  C  C   . GLN A  1 314 ? 52.983  53.721 21.533  1.00 26.44 ? 314  GLN A C   1 
ATOM   2294  O  O   . GLN A  1 314 ? 52.154  54.502 22.026  1.00 25.52 ? 314  GLN A O   1 
ATOM   2295  C  CB  . GLN A  1 314 ? 54.583  52.959 23.310  1.00 28.96 ? 314  GLN A CB  1 
ATOM   2296  C  CG  . GLN A  1 314 ? 54.259  51.506 23.132  1.00 32.65 ? 314  GLN A CG  1 
ATOM   2297  C  CD  . GLN A  1 314 ? 54.476  50.747 24.392  1.00 35.81 ? 314  GLN A CD  1 
ATOM   2298  O  OE1 . GLN A  1 314 ? 53.931  51.121 25.440  1.00 37.41 ? 314  GLN A OE1 1 
ATOM   2299  N  NE2 . GLN A  1 314 ? 55.274  49.664 24.322  1.00 35.42 ? 314  GLN A NE2 1 
ATOM   2300  N  N   . TRP A  1 315 ? 52.711  52.859 20.557  1.00 24.22 ? 315  TRP A N   1 
ATOM   2301  C  CA  . TRP A  1 315 ? 51.399  52.709 19.965  1.00 23.17 ? 315  TRP A CA  1 
ATOM   2302  C  C   . TRP A  1 315 ? 50.925  51.289 20.200  1.00 23.63 ? 315  TRP A C   1 
ATOM   2303  O  O   . TRP A  1 315 ? 51.716  50.360 20.259  1.00 23.25 ? 315  TRP A O   1 
ATOM   2304  C  CB  . TRP A  1 315 ? 51.457  52.968 18.468  1.00 24.26 ? 315  TRP A CB  1 
ATOM   2305  C  CG  . TRP A  1 315 ? 52.078  54.276 18.100  1.00 24.24 ? 315  TRP A CG  1 
ATOM   2306  C  CD1 . TRP A  1 315 ? 53.408  54.538 17.940  1.00 24.42 ? 315  TRP A CD1 1 
ATOM   2307  C  CD2 . TRP A  1 315 ? 51.390  55.486 17.801  1.00 23.77 ? 315  TRP A CD2 1 
ATOM   2308  N  NE1 . TRP A  1 315 ? 53.592  55.840 17.548  1.00 24.81 ? 315  TRP A NE1 1 
ATOM   2309  C  CE2 . TRP A  1 315 ? 52.369  56.447 17.453  1.00 24.98 ? 315  TRP A CE2 1 
ATOM   2310  C  CE3 . TRP A  1 315 ? 50.040  55.855 17.786  1.00 23.87 ? 315  TRP A CE3 1 
ATOM   2311  C  CZ2 . TRP A  1 315 ? 52.040  57.756 17.090  1.00 23.93 ? 315  TRP A CZ2 1 
ATOM   2312  C  CZ3 . TRP A  1 315 ? 49.707  57.147 17.427  1.00 23.71 ? 315  TRP A CZ3 1 
ATOM   2313  C  CH2 . TRP A  1 315 ? 50.707  58.089 17.082  1.00 24.86 ? 315  TRP A CH2 1 
ATOM   2314  N  N   . LEU A  1 316 ? 49.619  51.126 20.315  1.00 22.77 ? 316  LEU A N   1 
ATOM   2315  C  CA  . LEU A  1 316 ? 49.029  49.829 20.572  1.00 22.10 ? 316  LEU A CA  1 
ATOM   2316  C  C   . LEU A  1 316 ? 47.898  49.635 19.572  1.00 23.44 ? 316  LEU A C   1 
ATOM   2317  O  O   . LEU A  1 316 ? 47.093  50.546 19.358  1.00 22.50 ? 316  LEU A O   1 
ATOM   2318  C  CB  . LEU A  1 316 ? 48.461  49.807 21.995  1.00 21.42 ? 316  LEU A CB  1 
ATOM   2319  C  CG  . LEU A  1 316 ? 47.803  48.545 22.540  1.00 20.87 ? 316  LEU A CG  1 
ATOM   2320  C  CD1 . LEU A  1 316 ? 48.835  47.404 22.630  1.00 22.64 ? 316  LEU A CD1 1 
ATOM   2321  C  CD2 . LEU A  1 316 ? 47.219  48.865 23.915  1.00 20.01 ? 316  LEU A CD2 1 
ATOM   2322  N  N   . ARG A  1 317 ? 47.836  48.457 18.956  1.00 23.66 ? 317  ARG A N   1 
ATOM   2323  C  CA  . ARG A  1 317 ? 46.757  48.170 18.012  1.00 24.73 ? 317  ARG A CA  1 
ATOM   2324  C  C   . ARG A  1 317 ? 45.449  47.990 18.781  1.00 23.14 ? 317  ARG A C   1 
ATOM   2325  O  O   . ARG A  1 317 ? 45.469  47.638 19.952  1.00 22.84 ? 317  ARG A O   1 
ATOM   2326  C  CB  . ARG A  1 317 ? 47.086  46.902 17.218  1.00 26.58 ? 317  ARG A CB  1 
ATOM   2327  C  CG  . ARG A  1 317 ? 48.152  47.121 16.157  1.00 28.55 ? 317  ARG A CG  1 
ATOM   2328  C  CD  . ARG A  1 317 ? 48.472  45.810 15.475  1.00 30.69 ? 317  ARG A CD  1 
ATOM   2329  N  NE  . ARG A  1 317 ? 49.154  46.018 14.207  1.00 31.14 ? 317  ARG A NE  1 
ATOM   2330  C  CZ  . ARG A  1 317 ? 49.762  45.053 13.526  1.00 31.60 ? 317  ARG A CZ  1 
ATOM   2331  N  NH1 . ARG A  1 317 ? 49.773  43.816 14.002  1.00 30.02 ? 317  ARG A NH1 1 
ATOM   2332  N  NH2 . ARG A  1 317 ? 50.351  45.328 12.369  1.00 31.48 ? 317  ARG A NH2 1 
ATOM   2333  N  N   . ARG A  1 318 ? 44.310  48.223 18.137  1.00 23.99 ? 318  ARG A N   1 
ATOM   2334  C  CA  . ARG A  1 318 ? 43.035  48.077 18.847  1.00 24.20 ? 318  ARG A CA  1 
ATOM   2335  C  C   . ARG A  1 318 ? 42.883  46.662 19.430  1.00 25.38 ? 318  ARG A C   1 
ATOM   2336  O  O   . ARG A  1 318 ? 42.273  46.474 20.492  1.00 25.30 ? 318  ARG A O   1 
ATOM   2337  C  CB  . ARG A  1 318 ? 41.853  48.455 17.947  1.00 22.55 ? 318  ARG A CB  1 
ATOM   2338  C  CG  . ARG A  1 318 ? 40.557  48.519 18.742  1.00 22.47 ? 318  ARG A CG  1 
ATOM   2339  C  CD  . ARG A  1 318 ? 39.407  49.198 18.006  1.00 21.61 ? 318  ARG A CD  1 
ATOM   2340  N  NE  . ARG A  1 318 ? 38.177  49.072 18.791  1.00 19.99 ? 318  ARG A NE  1 
ATOM   2341  C  CZ  . ARG A  1 318 ? 37.068  49.767 18.561  1.00 20.67 ? 318  ARG A CZ  1 
ATOM   2342  N  NH1 . ARG A  1 318 ? 37.037  50.635 17.556  1.00 19.31 ? 318  ARG A NH1 1 
ATOM   2343  N  NH2 . ARG A  1 318 ? 36.005  49.616 19.350  1.00 17.79 ? 318  ARG A NH2 1 
ATOM   2344  N  N   . ILE A  1 319 ? 43.439  45.668 18.734  1.00 26.11 ? 319  ILE A N   1 
ATOM   2345  C  CA  . ILE A  1 319 ? 43.470  44.289 19.246  1.00 27.39 ? 319  ILE A CA  1 
ATOM   2346  C  C   . ILE A  1 319 ? 44.742  44.424 20.089  1.00 27.40 ? 319  ILE A C   1 
ATOM   2347  O  O   . ILE A  1 319 ? 45.851  44.279 19.581  1.00 28.40 ? 319  ILE A O   1 
ATOM   2348  C  CB  . ILE A  1 319 ? 43.750  43.271 18.128  1.00 28.36 ? 319  ILE A CB  1 
ATOM   2349  C  CG1 . ILE A  1 319 ? 42.716  43.427 17.023  1.00 29.39 ? 319  ILE A CG1 1 
ATOM   2350  C  CG2 . ILE A  1 319 ? 43.778  41.869 18.694  1.00 27.17 ? 319  ILE A CG2 1 
ATOM   2351  C  CD1 . ILE A  1 319 ? 41.355  43.059 17.456  1.00 30.13 ? 319  ILE A CD1 1 
ATOM   2352  N  N   . GLN A  1 320 ? 44.575  44.711 21.370  1.00 27.84 ? 320  GLN A N   1 
ATOM   2353  C  CA  . GLN A  1 320 ? 45.691  44.991 22.263  1.00 27.78 ? 320  GLN A CA  1 
ATOM   2354  C  C   . GLN A  1 320 ? 46.740  43.926 22.555  1.00 29.04 ? 320  GLN A C   1 
ATOM   2355  O  O   . GLN A  1 320 ? 47.193  43.775 23.693  1.00 29.41 ? 320  GLN A O   1 
ATOM   2356  C  CB  . GLN A  1 320 ? 45.115  45.551 23.558  1.00 26.38 ? 320  GLN A CB  1 
ATOM   2357  C  CG  . GLN A  1 320 ? 44.149  46.719 23.289  1.00 24.05 ? 320  GLN A CG  1 
ATOM   2358  C  CD  . GLN A  1 320 ? 43.613  47.301 24.559  1.00 22.66 ? 320  GLN A CD  1 
ATOM   2359  O  OE1 . GLN A  1 320 ? 44.363  47.499 25.505  1.00 23.14 ? 320  GLN A OE1 1 
ATOM   2360  N  NE2 . GLN A  1 320 ? 42.317  47.583 24.595  1.00 21.21 ? 320  GLN A NE2 1 
ATOM   2361  N  N   . ASN A  1 321 ? 47.172  43.247 21.502  1.00 30.88 ? 321  ASN A N   1 
ATOM   2362  C  CA  . ASN A  1 321 ? 48.173  42.201 21.624  1.00 33.08 ? 321  ASN A CA  1 
ATOM   2363  C  C   . ASN A  1 321 ? 49.438  42.521 20.827  1.00 32.36 ? 321  ASN A C   1 
ATOM   2364  O  O   . ASN A  1 321 ? 50.258  41.644 20.565  1.00 33.20 ? 321  ASN A O   1 
ATOM   2365  C  CB  . ASN A  1 321 ? 47.594  40.862 21.146  1.00 35.11 ? 321  ASN A CB  1 
ATOM   2366  C  CG  . ASN A  1 321 ? 47.317  40.828 19.646  1.00 38.73 ? 321  ASN A CG  1 
ATOM   2367  O  OD1 . ASN A  1 321 ? 47.500  41.825 18.922  1.00 40.09 ? 321  ASN A OD1 1 
ATOM   2368  N  ND2 . ASN A  1 321 ? 46.863  39.671 19.163  1.00 43.58 ? 321  ASN A ND2 1 
ATOM   2369  N  N   . TYR A  1 322 ? 49.604  43.773 20.439  1.00 31.40 ? 322  TYR A N   1 
ATOM   2370  C  CA  . TYR A  1 322 ? 50.775  44.133 19.672  1.00 30.36 ? 322  TYR A CA  1 
ATOM   2371  C  C   . TYR A  1 322 ? 51.061  45.615 19.866  1.00 29.10 ? 322  TYR A C   1 
ATOM   2372  O  O   . TYR A  1 322 ? 50.258  46.471 19.487  1.00 28.81 ? 322  TYR A O   1 
ATOM   2373  C  CB  . TYR A  1 322 ? 50.520  43.791 18.199  1.00 32.03 ? 322  TYR A CB  1 
ATOM   2374  C  CG  . TYR A  1 322 ? 51.692  43.992 17.275  1.00 33.28 ? 322  TYR A CG  1 
ATOM   2375  C  CD1 . TYR A  1 322 ? 51.909  45.221 16.660  1.00 34.81 ? 322  TYR A CD1 1 
ATOM   2376  C  CD2 . TYR A  1 322 ? 52.572  42.947 16.989  1.00 34.86 ? 322  TYR A CD2 1 
ATOM   2377  C  CE1 . TYR A  1 322 ? 52.970  45.413 15.778  1.00 35.16 ? 322  TYR A CE1 1 
ATOM   2378  C  CE2 . TYR A  1 322 ? 53.646  43.130 16.102  1.00 35.03 ? 322  TYR A CE2 1 
ATOM   2379  C  CZ  . TYR A  1 322 ? 53.832  44.366 15.505  1.00 35.61 ? 322  TYR A CZ  1 
ATOM   2380  O  OH  . TYR A  1 322 ? 54.878  44.572 14.631  1.00 37.49 ? 322  TYR A OH  1 
ATOM   2381  N  N   . SER A  1 323 ? 52.198  45.923 20.477  1.00 27.56 ? 323  SER A N   1 
ATOM   2382  C  CA  . SER A  1 323 ? 52.557  47.312 20.722  1.00 27.48 ? 323  SER A CA  1 
ATOM   2383  C  C   . SER A  1 323 ? 53.878  47.592 20.042  1.00 26.93 ? 323  SER A C   1 
ATOM   2384  O  O   . SER A  1 323 ? 54.730  46.697 19.936  1.00 27.06 ? 323  SER A O   1 
ATOM   2385  C  CB  . SER A  1 323 ? 52.705  47.571 22.215  1.00 27.24 ? 323  SER A CB  1 
ATOM   2386  O  OG  . SER A  1 323 ? 53.912  46.998 22.668  1.00 29.45 ? 323  SER A OG  1 
ATOM   2387  N  N   . VAL A  1 324 ? 54.031  48.827 19.573  1.00 25.15 ? 324  VAL A N   1 
ATOM   2388  C  CA  . VAL A  1 324 ? 55.243  49.262 18.892  1.00 25.04 ? 324  VAL A CA  1 
ATOM   2389  C  C   . VAL A  1 324 ? 55.778  50.570 19.469  1.00 24.95 ? 324  VAL A C   1 
ATOM   2390  O  O   . VAL A  1 324 ? 55.088  51.600 19.455  1.00 24.88 ? 324  VAL A O   1 
ATOM   2391  C  CB  . VAL A  1 324 ? 55.005  49.520 17.394  1.00 24.69 ? 324  VAL A CB  1 
ATOM   2392  C  CG1 . VAL A  1 324 ? 56.281  50.085 16.774  1.00 24.18 ? 324  VAL A CG1 1 
ATOM   2393  C  CG2 . VAL A  1 324 ? 54.578  48.242 16.690  1.00 25.10 ? 324  VAL A CG2 1 
ATOM   2394  N  N   . MET A  1 325 ? 57.010  50.524 19.963  1.00 23.42 ? 325  MET A N   1 
ATOM   2395  C  CA  . MET A  1 325 ? 57.652  51.705 20.518  1.00 22.01 ? 325  MET A CA  1 
ATOM   2396  C  C   . MET A  1 325 ? 58.609  52.296 19.482  1.00 22.13 ? 325  MET A C   1 
ATOM   2397  O  O   . MET A  1 325 ? 59.466  51.581 18.937  1.00 21.48 ? 325  MET A O   1 
ATOM   2398  C  CB  . MET A  1 325 ? 58.447  51.344 21.788  1.00 21.13 ? 325  MET A CB  1 
ATOM   2399  C  CG  . MET A  1 325 ? 59.286  52.495 22.355  1.00 19.82 ? 325  MET A CG  1 
ATOM   2400  S  SD  . MET A  1 325 ? 60.558  51.941 23.518  1.00 22.28 ? 325  MET A SD  1 
ATOM   2401  C  CE  . MET A  1 325 ? 61.026  53.444 24.306  1.00 21.46 ? 325  MET A CE  1 
ATOM   2402  N  N   . ASP A  1 326 ? 58.452  53.589 19.211  1.00 21.17 ? 326  ASP A N   1 
ATOM   2403  C  CA  . ASP A  1 326 ? 59.329  54.300 18.289  1.00 22.93 ? 326  ASP A CA  1 
ATOM   2404  C  C   . ASP A  1 326 ? 60.224  55.209 19.129  1.00 23.00 ? 326  ASP A C   1 
ATOM   2405  O  O   . ASP A  1 326 ? 59.801  55.731 20.178  1.00 22.41 ? 326  ASP A O   1 
ATOM   2406  C  CB  . ASP A  1 326 ? 58.536  55.183 17.313  1.00 22.99 ? 326  ASP A CB  1 
ATOM   2407  C  CG  . ASP A  1 326 ? 58.397  54.567 15.931  1.00 25.01 ? 326  ASP A CG  1 
ATOM   2408  O  OD1 . ASP A  1 326 ? 59.129  53.595 15.616  1.00 24.15 ? 326  ASP A OD1 1 
ATOM   2409  O  OD2 . ASP A  1 326 ? 57.556  55.074 15.152  1.00 23.62 ? 326  ASP A OD2 1 
ATOM   2410  N  N   . ILE A  1 327 ? 61.454  55.396 18.670  1.00 22.87 ? 327  ILE A N   1 
ATOM   2411  C  CA  . ILE A  1 327 ? 62.409  56.261 19.350  1.00 23.49 ? 327  ILE A CA  1 
ATOM   2412  C  C   . ILE A  1 327 ? 62.847  57.284 18.323  1.00 24.58 ? 327  ILE A C   1 
ATOM   2413  O  O   . ILE A  1 327 ? 63.546  56.947 17.366  1.00 25.94 ? 327  ILE A O   1 
ATOM   2414  C  CB  . ILE A  1 327 ? 63.593  55.458 19.858  1.00 22.44 ? 327  ILE A CB  1 
ATOM   2415  C  CG1 . ILE A  1 327 ? 63.092  54.499 20.948  1.00 22.87 ? 327  ILE A CG1 1 
ATOM   2416  C  CG2 . ILE A  1 327 ? 64.672  56.394 20.381  1.00 23.60 ? 327  ILE A CG2 1 
ATOM   2417  C  CD1 . ILE A  1 327 ? 64.182  53.722 21.660  1.00 21.14 ? 327  ILE A CD1 1 
ATOM   2418  N  N   . CYS A  1 328 ? 62.441  58.532 18.528  1.00 24.97 ? 328  CYS A N   1 
ATOM   2419  C  CA  . CYS A  1 328 ? 62.711  59.596 17.566  1.00 26.33 ? 328  CYS A CA  1 
ATOM   2420  C  C   . CYS A  1 328 ? 63.705  60.678 17.964  1.00 26.24 ? 328  CYS A C   1 
ATOM   2421  O  O   . CYS A  1 328 ? 63.673  61.185 19.074  1.00 25.95 ? 328  CYS A O   1 
ATOM   2422  C  CB  . CYS A  1 328 ? 61.377  60.241 17.199  1.00 27.66 ? 328  CYS A CB  1 
ATOM   2423  S  SG  . CYS A  1 328 ? 60.027  59.010 17.016  1.00 29.35 ? 328  CYS A SG  1 
ATOM   2424  N  N   . ASP A  1 329 ? 64.579  61.031 17.024  1.00 27.03 ? 329  ASP A N   1 
ATOM   2425  C  CA  . ASP A  1 329 ? 65.603  62.058 17.226  1.00 27.58 ? 329  ASP A CA  1 
ATOM   2426  C  C   . ASP A  1 329 ? 65.328  63.331 16.423  1.00 28.34 ? 329  ASP A C   1 
ATOM   2427  O  O   . ASP A  1 329 ? 64.847  63.271 15.286  1.00 27.68 ? 329  ASP A O   1 
ATOM   2428  C  CB  . ASP A  1 329 ? 66.977  61.494 16.839  1.00 28.33 ? 329  ASP A CB  1 
ATOM   2429  C  CG  . ASP A  1 329 ? 67.552  60.589 17.921  1.00 29.91 ? 329  ASP A CG  1 
ATOM   2430  O  OD1 . ASP A  1 329 ? 66.743  59.985 18.660  1.00 29.96 ? 329  ASP A OD1 1 
ATOM   2431  O  OD2 . ASP A  1 329 ? 68.798  60.479 18.038  1.00 30.87 ? 329  ASP A OD2 1 
ATOM   2432  N  N   . TYR A  1 330 ? 65.619  64.479 17.029  1.00 29.20 ? 330  TYR A N   1 
ATOM   2433  C  CA  . TYR A  1 330 ? 65.432  65.766 16.368  1.00 30.81 ? 330  TYR A CA  1 
ATOM   2434  C  C   . TYR A  1 330 ? 66.594  66.007 15.404  1.00 32.17 ? 330  TYR A C   1 
ATOM   2435  O  O   . TYR A  1 330 ? 67.769  65.904 15.791  1.00 30.45 ? 330  TYR A O   1 
ATOM   2436  C  CB  . TYR A  1 330 ? 65.403  66.902 17.385  1.00 31.68 ? 330  TYR A CB  1 
ATOM   2437  C  CG  . TYR A  1 330 ? 65.293  68.272 16.750  1.00 32.55 ? 330  TYR A CG  1 
ATOM   2438  C  CD1 . TYR A  1 330 ? 64.148  68.642 16.049  1.00 32.63 ? 330  TYR A CD1 1 
ATOM   2439  C  CD2 . TYR A  1 330 ? 66.346  69.193 16.837  1.00 33.19 ? 330  TYR A CD2 1 
ATOM   2440  C  CE1 . TYR A  1 330 ? 64.042  69.892 15.448  1.00 33.03 ? 330  TYR A CE1 1 
ATOM   2441  C  CE2 . TYR A  1 330 ? 66.255  70.452 16.241  1.00 33.36 ? 330  TYR A CE2 1 
ATOM   2442  C  CZ  . TYR A  1 330 ? 65.093  70.791 15.550  1.00 34.10 ? 330  TYR A CZ  1 
ATOM   2443  O  OH  . TYR A  1 330 ? 64.958  72.031 14.978  1.00 35.43 ? 330  TYR A OH  1 
ATOM   2444  N  N   . ASP A  1 331 ? 66.251  66.325 14.159  1.00 33.06 ? 331  ASP A N   1 
ATOM   2445  C  CA  . ASP A  1 331 ? 67.226  66.594 13.102  1.00 35.57 ? 331  ASP A CA  1 
ATOM   2446  C  C   . ASP A  1 331 ? 67.330  68.109 12.903  1.00 36.97 ? 331  ASP A C   1 
ATOM   2447  O  O   . ASP A  1 331 ? 66.440  68.701 12.304  1.00 36.78 ? 331  ASP A O   1 
ATOM   2448  C  CB  . ASP A  1 331 ? 66.742  65.931 11.804  1.00 35.59 ? 331  ASP A CB  1 
ATOM   2449  C  CG  . ASP A  1 331 ? 67.710  66.118 10.636  1.00 36.34 ? 331  ASP A CG  1 
ATOM   2450  O  OD1 . ASP A  1 331 ? 68.215  67.241 10.450  1.00 37.07 ? 331  ASP A OD1 1 
ATOM   2451  O  OD2 . ASP A  1 331 ? 67.944  65.142 9.894   1.00 35.66 ? 331  ASP A OD2 1 
ATOM   2452  N  N   . GLU A  1 332 ? 68.391  68.740 13.407  1.00 39.12 ? 332  GLU A N   1 
ATOM   2453  C  CA  . GLU A  1 332 ? 68.546  70.190 13.243  1.00 42.22 ? 332  GLU A CA  1 
ATOM   2454  C  C   . GLU A  1 332 ? 68.538  70.651 11.779  1.00 43.50 ? 332  GLU A C   1 
ATOM   2455  O  O   . GLU A  1 332 ? 68.128  71.771 11.471  1.00 44.17 ? 332  GLU A O   1 
ATOM   2456  C  CB  . GLU A  1 332 ? 69.852  70.681 13.870  1.00 43.77 ? 332  GLU A CB  1 
ATOM   2457  C  CG  . GLU A  1 332 ? 69.857  70.791 15.371  1.00 46.41 ? 332  GLU A CG  1 
ATOM   2458  C  CD  . GLU A  1 332 ? 71.176  71.324 15.895  1.00 48.25 ? 332  GLU A CD  1 
ATOM   2459  O  OE1 . GLU A  1 332 ? 72.221  70.691 15.618  1.00 49.77 ? 332  GLU A OE1 1 
ATOM   2460  O  OE2 . GLU A  1 332 ? 71.179  72.373 16.583  1.00 49.61 ? 332  GLU A OE2 1 
ATOM   2461  N  N   . SER A  1 333 ? 68.997  69.794 10.876  1.00 44.53 ? 333  SER A N   1 
ATOM   2462  C  CA  . SER A  1 333 ? 69.063  70.155 9.462   1.00 45.41 ? 333  SER A CA  1 
ATOM   2463  C  C   . SER A  1 333 ? 67.689  70.429 8.884   1.00 46.07 ? 333  SER A C   1 
ATOM   2464  O  O   . SER A  1 333 ? 67.441  71.503 8.338   1.00 46.53 ? 333  SER A O   1 
ATOM   2465  C  CB  . SER A  1 333 ? 69.734  69.040 8.662   1.00 45.54 ? 333  SER A CB  1 
ATOM   2466  O  OG  . SER A  1 333 ? 70.920  68.609 9.309   1.00 46.79 ? 333  SER A OG  1 
ATOM   2467  N  N   . SER A  1 334 ? 66.799  69.448 9.003   1.00 46.10 ? 334  SER A N   1 
ATOM   2468  C  CA  . SER A  1 334 ? 65.446  69.567 8.477   1.00 45.68 ? 334  SER A CA  1 
ATOM   2469  C  C   . SER A  1 334 ? 64.432  69.999 9.528   1.00 45.04 ? 334  SER A C   1 
ATOM   2470  O  O   . SER A  1 334 ? 63.257  70.193 9.211   1.00 45.63 ? 334  SER A O   1 
ATOM   2471  C  CB  . SER A  1 334 ? 64.997  68.228 7.885   1.00 46.63 ? 334  SER A CB  1 
ATOM   2472  O  OG  . SER A  1 334 ? 64.939  67.220 8.890   1.00 48.43 ? 334  SER A OG  1 
ATOM   2473  N  N   . GLY A  1 335 ? 64.872  70.141 10.775  1.00 43.71 ? 335  GLY A N   1 
ATOM   2474  C  CA  . GLY A  1 335 ? 63.951  70.527 11.836  1.00 42.13 ? 335  GLY A CA  1 
ATOM   2475  C  C   . GLY A  1 335 ? 62.823  69.510 11.978  1.00 40.80 ? 335  GLY A C   1 
ATOM   2476  O  O   . GLY A  1 335 ? 61.745  69.825 12.470  1.00 41.06 ? 335  GLY A O   1 
ATOM   2477  N  N   . ARG A  1 336 ? 63.079  68.286 11.532  1.00 39.73 ? 336  ARG A N   1 
ATOM   2478  C  CA  . ARG A  1 336 ? 62.103  67.208 11.595  1.00 38.91 ? 336  ARG A CA  1 
ATOM   2479  C  C   . ARG A  1 336 ? 62.520  66.188 12.649  1.00 37.10 ? 336  ARG A C   1 
ATOM   2480  O  O   . ARG A  1 336 ? 63.651  66.218 13.142  1.00 37.11 ? 336  ARG A O   1 
ATOM   2481  C  CB  . ARG A  1 336 ? 62.020  66.495 10.244  1.00 40.36 ? 336  ARG A CB  1 
ATOM   2482  C  CG  . ARG A  1 336 ? 61.819  67.414 9.046   1.00 42.02 ? 336  ARG A CG  1 
ATOM   2483  C  CD  . ARG A  1 336 ? 60.382  67.831 8.923   1.00 43.54 ? 336  ARG A CD  1 
ATOM   2484  N  NE  . ARG A  1 336 ? 59.527  66.668 8.669   1.00 45.57 ? 336  ARG A NE  1 
ATOM   2485  C  CZ  . ARG A  1 336 ? 58.198  66.703 8.700   1.00 45.82 ? 336  ARG A CZ  1 
ATOM   2486  N  NH1 . ARG A  1 336 ? 57.571  67.845 8.975   1.00 46.07 ? 336  ARG A NH1 1 
ATOM   2487  N  NH2 . ARG A  1 336 ? 57.499  65.602 8.458   1.00 46.06 ? 336  ARG A NH2 1 
ATOM   2488  N  N   . TRP A  1 337 ? 61.603  65.286 12.986  1.00 34.30 ? 337  TRP A N   1 
ATOM   2489  C  CA  . TRP A  1 337 ? 61.874  64.230 13.957  1.00 32.14 ? 337  TRP A CA  1 
ATOM   2490  C  C   . TRP A  1 337 ? 61.893  62.907 13.196  1.00 32.51 ? 337  TRP A C   1 
ATOM   2491  O  O   . TRP A  1 337 ? 60.914  62.553 12.548  1.00 32.80 ? 337  TRP A O   1 
ATOM   2492  C  CB  . TRP A  1 337 ? 60.790  64.198 15.042  1.00 29.10 ? 337  TRP A CB  1 
ATOM   2493  C  CG  . TRP A  1 337 ? 60.821  65.386 15.968  1.00 25.55 ? 337  TRP A CG  1 
ATOM   2494  C  CD1 . TRP A  1 337 ? 60.265  66.613 15.752  1.00 25.37 ? 337  TRP A CD1 1 
ATOM   2495  C  CD2 . TRP A  1 337 ? 61.507  65.471 17.224  1.00 24.82 ? 337  TRP A CD2 1 
ATOM   2496  N  NE1 . TRP A  1 337 ? 60.567  67.465 16.798  1.00 24.86 ? 337  TRP A NE1 1 
ATOM   2497  C  CE2 . TRP A  1 337 ? 61.327  66.788 17.714  1.00 23.81 ? 337  TRP A CE2 1 
ATOM   2498  C  CE3 . TRP A  1 337 ? 62.262  64.563 17.984  1.00 24.45 ? 337  TRP A CE3 1 
ATOM   2499  C  CZ2 . TRP A  1 337 ? 61.873  67.221 18.929  1.00 23.86 ? 337  TRP A CZ2 1 
ATOM   2500  C  CZ3 . TRP A  1 337 ? 62.812  65.000 19.199  1.00 24.45 ? 337  TRP A CZ3 1 
ATOM   2501  C  CH2 . TRP A  1 337 ? 62.610  66.318 19.653  1.00 23.23 ? 337  TRP A CH2 1 
ATOM   2502  N  N   . ASN A  1 338 ? 63.011  62.190 13.271  1.00 32.54 ? 338  ASN A N   1 
ATOM   2503  C  CA  . ASN A  1 338 ? 63.172  60.915 12.575  1.00 32.60 ? 338  ASN A CA  1 
ATOM   2504  C  C   . ASN A  1 338 ? 63.200  59.764 13.566  1.00 31.72 ? 338  ASN A C   1 
ATOM   2505  O  O   . ASN A  1 338 ? 63.942  59.802 14.542  1.00 31.30 ? 338  ASN A O   1 
ATOM   2506  C  CB  . ASN A  1 338 ? 64.486  60.902 11.787  1.00 33.82 ? 338  ASN A CB  1 
ATOM   2507  C  CG  . ASN A  1 338 ? 64.526  61.949 10.695  1.00 36.40 ? 338  ASN A CG  1 
ATOM   2508  O  OD1 . ASN A  1 338 ? 63.799  62.939 10.740  1.00 38.71 ? 338  ASN A OD1 1 
ATOM   2509  N  ND2 . ASN A  1 338 ? 65.396  61.746 9.712   1.00 37.90 ? 338  ASN A ND2 1 
ATOM   2510  N  N   . CYS A  1 339 ? 62.398  58.742 13.306  1.00 30.85 ? 339  CYS A N   1 
ATOM   2511  C  CA  . CYS A  1 339 ? 62.346  57.582 14.176  1.00 31.06 ? 339  CYS A CA  1 
ATOM   2512  C  C   . CYS A  1 339 ? 62.895  56.402 13.376  1.00 31.43 ? 339  CYS A C   1 
ATOM   2513  O  O   . CYS A  1 339 ? 62.163  55.771 12.607  1.00 31.53 ? 339  CYS A O   1 
ATOM   2514  C  CB  . CYS A  1 339 ? 60.899  57.293 14.604  1.00 30.52 ? 339  CYS A CB  1 
ATOM   2515  S  SG  . CYS A  1 339 ? 59.865  58.755 14.999  1.00 29.84 ? 339  CYS A SG  1 
ATOM   2516  N  N   . LEU A  1 340 ? 64.185  56.125 13.543  1.00 31.17 ? 340  LEU A N   1 
ATOM   2517  C  CA  . LEU A  1 340 ? 64.836  55.020 12.844  1.00 31.36 ? 340  LEU A CA  1 
ATOM   2518  C  C   . LEU A  1 340 ? 64.159  53.690 13.136  1.00 31.55 ? 340  LEU A C   1 
ATOM   2519  O  O   . LEU A  1 340 ? 63.891  53.357 14.298  1.00 30.32 ? 340  LEU A O   1 
ATOM   2520  C  CB  . LEU A  1 340 ? 66.303  54.929 13.265  1.00 33.10 ? 340  LEU A CB  1 
ATOM   2521  C  CG  . LEU A  1 340 ? 67.254  56.036 12.809  1.00 33.95 ? 340  LEU A CG  1 
ATOM   2522  C  CD1 . LEU A  1 340 ? 68.618  55.855 13.473  1.00 32.92 ? 340  LEU A CD1 1 
ATOM   2523  C  CD2 . LEU A  1 340 ? 67.383  55.984 11.283  1.00 34.93 ? 340  LEU A CD2 1 
ATOM   2524  N  N   . VAL A  1 341 ? 63.898  52.910 12.089  1.00 31.05 ? 341  VAL A N   1 
ATOM   2525  C  CA  . VAL A  1 341 ? 63.254  51.620 12.283  1.00 31.11 ? 341  VAL A CA  1 
ATOM   2526  C  C   . VAL A  1 341 ? 64.163  50.688 13.085  1.00 31.13 ? 341  VAL A C   1 
ATOM   2527  O  O   . VAL A  1 341 ? 63.689  49.790 13.762  1.00 31.45 ? 341  VAL A O   1 
ATOM   2528  C  CB  . VAL A  1 341 ? 62.905  50.946 10.942  1.00 32.15 ? 341  VAL A CB  1 
ATOM   2529  C  CG1 . VAL A  1 341 ? 64.164  50.385 10.290  1.00 31.89 ? 341  VAL A CG1 1 
ATOM   2530  C  CG2 . VAL A  1 341 ? 61.882  49.851 11.182  1.00 33.12 ? 341  VAL A CG2 1 
ATOM   2531  N  N   . ALA A  1 342 ? 65.470  50.901 13.004  1.00 30.53 ? 342  ALA A N   1 
ATOM   2532  C  CA  . ALA A  1 342 ? 66.418  50.087 13.760  1.00 30.27 ? 342  ALA A CA  1 
ATOM   2533  C  C   . ALA A  1 342 ? 66.224  50.291 15.270  1.00 29.43 ? 342  ALA A C   1 
ATOM   2534  O  O   . ALA A  1 342 ? 66.612  49.441 16.065  1.00 30.19 ? 342  ALA A O   1 
ATOM   2535  C  CB  . ALA A  1 342 ? 67.841  50.443 13.375  1.00 29.51 ? 342  ALA A CB  1 
ATOM   2536  N  N   . ARG A  1 343 ? 65.637  51.420 15.654  1.00 28.62 ? 343  ARG A N   1 
ATOM   2537  C  CA  . ARG A  1 343 ? 65.379  51.711 17.058  1.00 27.98 ? 343  ARG A CA  1 
ATOM   2538  C  C   . ARG A  1 343 ? 63.915  51.451 17.437  1.00 28.10 ? 343  ARG A C   1 
ATOM   2539  O  O   . ARG A  1 343 ? 63.399  52.008 18.415  1.00 27.73 ? 343  ARG A O   1 
ATOM   2540  C  CB  . ARG A  1 343 ? 65.748  53.160 17.369  1.00 27.83 ? 343  ARG A CB  1 
ATOM   2541  C  CG  . ARG A  1 343 ? 67.234  53.427 17.249  1.00 29.59 ? 343  ARG A CG  1 
ATOM   2542  C  CD  . ARG A  1 343 ? 67.519  54.891 17.348  1.00 30.78 ? 343  ARG A CD  1 
ATOM   2543  N  NE  . ARG A  1 343 ? 68.957  55.151 17.361  1.00 31.79 ? 343  ARG A NE  1 
ATOM   2544  C  CZ  . ARG A  1 343 ? 69.480  56.366 17.376  1.00 32.43 ? 343  ARG A CZ  1 
ATOM   2545  N  NH1 . ARG A  1 343 ? 68.678  57.429 17.376  1.00 34.08 ? 343  ARG A NH1 1 
ATOM   2546  N  NH2 . ARG A  1 343 ? 70.795  56.523 17.401  1.00 33.86 ? 343  ARG A NH2 1 
ATOM   2547  N  N   . GLN A  1 344 ? 63.251  50.592 16.671  1.00 27.63 ? 344  GLN A N   1 
ATOM   2548  C  CA  . GLN A  1 344 ? 61.854  50.259 16.931  1.00 27.36 ? 344  GLN A CA  1 
ATOM   2549  C  C   . GLN A  1 344 ? 61.797  49.011 17.786  1.00 26.88 ? 344  GLN A C   1 
ATOM   2550  O  O   . GLN A  1 344 ? 62.552  48.066 17.572  1.00 26.10 ? 344  GLN A O   1 
ATOM   2551  C  CB  . GLN A  1 344 ? 61.111  50.024 15.610  1.00 27.70 ? 344  GLN A CB  1 
ATOM   2552  C  CG  . GLN A  1 344 ? 59.661  50.469 15.635  1.00 27.81 ? 344  GLN A CG  1 
ATOM   2553  C  CD  . GLN A  1 344 ? 58.983  50.346 14.277  1.00 28.58 ? 344  GLN A CD  1 
ATOM   2554  O  OE1 . GLN A  1 344 ? 58.800  49.247 13.761  1.00 27.65 ? 344  GLN A OE1 1 
ATOM   2555  N  NE2 . GLN A  1 344 ? 58.605  51.480 13.698  1.00 28.46 ? 344  GLN A NE2 1 
ATOM   2556  N  N   . HIS A  1 345 ? 60.911  49.007 18.778  1.00 26.93 ? 345  HIS A N   1 
ATOM   2557  C  CA  . HIS A  1 345 ? 60.795  47.853 19.661  1.00 26.56 ? 345  HIS A CA  1 
ATOM   2558  C  C   . HIS A  1 345 ? 59.352  47.391 19.694  1.00 27.11 ? 345  HIS A C   1 
ATOM   2559  O  O   . HIS A  1 345 ? 58.431  48.181 19.900  1.00 28.03 ? 345  HIS A O   1 
ATOM   2560  C  CB  . HIS A  1 345 ? 61.284  48.207 21.068  1.00 25.80 ? 345  HIS A CB  1 
ATOM   2561  C  CG  . HIS A  1 345 ? 62.737  48.566 21.124  1.00 25.52 ? 345  HIS A CG  1 
ATOM   2562  N  ND1 . HIS A  1 345 ? 63.202  49.831 20.832  1.00 25.51 ? 345  HIS A ND1 1 
ATOM   2563  C  CD2 . HIS A  1 345 ? 63.829  47.820 21.409  1.00 24.35 ? 345  HIS A CD2 1 
ATOM   2564  C  CE1 . HIS A  1 345 ? 64.518  49.849 20.937  1.00 25.02 ? 345  HIS A CE1 1 
ATOM   2565  N  NE2 . HIS A  1 345 ? 64.924  48.640 21.286  1.00 25.48 ? 345  HIS A NE2 1 
ATOM   2566  N  N   . ILE A  1 346 ? 59.167  46.099 19.494  1.00 27.61 ? 346  ILE A N   1 
ATOM   2567  C  CA  . ILE A  1 346 ? 57.845  45.505 19.438  1.00 28.56 ? 346  ILE A CA  1 
ATOM   2568  C  C   . ILE A  1 346 ? 57.581  44.645 20.651  1.00 28.14 ? 346  ILE A C   1 
ATOM   2569  O  O   . ILE A  1 346 ? 58.505  44.078 21.226  1.00 26.96 ? 346  ILE A O   1 
ATOM   2570  C  CB  . ILE A  1 346 ? 57.729  44.629 18.168  1.00 29.68 ? 346  ILE A CB  1 
ATOM   2571  C  CG1 . ILE A  1 346 ? 57.930  45.511 16.930  1.00 31.17 ? 346  ILE A CG1 1 
ATOM   2572  C  CG2 . ILE A  1 346 ? 56.388  43.917 18.114  1.00 30.37 ? 346  ILE A CG2 1 
ATOM   2573  C  CD1 . ILE A  1 346 ? 57.892  44.745 15.623  1.00 33.19 ? 346  ILE A CD1 1 
ATOM   2574  N  N   . GLU A  1 347 ? 56.312  44.563 21.035  1.00 28.01 ? 347  GLU A N   1 
ATOM   2575  C  CA  . GLU A  1 347 ? 55.879  43.736 22.158  1.00 29.82 ? 347  GLU A CA  1 
ATOM   2576  C  C   . GLU A  1 347 ? 54.625  43.000 21.704  1.00 31.52 ? 347  GLU A C   1 
ATOM   2577  O  O   . GLU A  1 347 ? 53.738  43.589 21.083  1.00 31.11 ? 347  GLU A O   1 
ATOM   2578  C  CB  . GLU A  1 347 ? 55.567  44.588 23.396  1.00 29.12 ? 347  GLU A CB  1 
ATOM   2579  C  CG  . GLU A  1 347 ? 56.700  44.657 24.375  1.00 29.71 ? 347  GLU A CG  1 
ATOM   2580  C  CD  . GLU A  1 347 ? 56.384  45.479 25.612  1.00 29.79 ? 347  GLU A CD  1 
ATOM   2581  O  OE1 . GLU A  1 347 ? 56.825  46.641 25.670  1.00 31.14 ? 347  GLU A OE1 1 
ATOM   2582  O  OE2 . GLU A  1 347 ? 55.698  44.972 26.520  1.00 29.01 ? 347  GLU A OE2 1 
ATOM   2583  N  N   . MET A  1 348 ? 54.568  41.705 21.990  1.00 33.09 ? 348  MET A N   1 
ATOM   2584  C  CA  . MET A  1 348 ? 53.429  40.884 21.596  1.00 34.04 ? 348  MET A CA  1 
ATOM   2585  C  C   . MET A  1 348 ? 52.943  40.105 22.787  1.00 34.40 ? 348  MET A C   1 
ATOM   2586  O  O   . MET A  1 348 ? 53.696  39.800 23.708  1.00 33.37 ? 348  MET A O   1 
ATOM   2587  C  CB  . MET A  1 348 ? 53.817  39.893 20.512  1.00 35.31 ? 348  MET A CB  1 
ATOM   2588  C  CG  . MET A  1 348 ? 54.258  40.519 19.238  1.00 36.88 ? 348  MET A CG  1 
ATOM   2589  S  SD  . MET A  1 348 ? 54.768  39.211 18.126  1.00 41.01 ? 348  MET A SD  1 
ATOM   2590  C  CE  . MET A  1 348 ? 53.267  38.947 17.174  1.00 39.11 ? 348  MET A CE  1 
ATOM   2591  N  N   . SER A  1 349 ? 51.672  39.746 22.740  1.00 36.35 ? 349  SER A N   1 
ATOM   2592  C  CA  . SER A  1 349 ? 51.072  39.022 23.833  1.00 38.06 ? 349  SER A CA  1 
ATOM   2593  C  C   . SER A  1 349 ? 50.631  37.659 23.385  1.00 38.16 ? 349  SER A C   1 
ATOM   2594  O  O   . SER A  1 349 ? 49.856  37.554 22.436  1.00 39.47 ? 349  SER A O   1 
ATOM   2595  C  CB  . SER A  1 349 ? 49.848  39.792 24.339  1.00 39.78 ? 349  SER A CB  1 
ATOM   2596  O  OG  . SER A  1 349 ? 48.870  39.918 23.310  1.00 41.09 ? 349  SER A OG  1 
ATOM   2597  N  N   . THR A  1 350 ? 51.087  36.620 24.081  1.00 38.26 ? 350  THR A N   1 
ATOM   2598  C  CA  . THR A  1 350 ? 50.677  35.259 23.740  1.00 38.02 ? 350  THR A CA  1 
ATOM   2599  C  C   . THR A  1 350 ? 49.560  34.740 24.643  1.00 36.45 ? 350  THR A C   1 
ATOM   2600  O  O   . THR A  1 350 ? 48.520  34.315 24.153  1.00 37.34 ? 350  THR A O   1 
ATOM   2601  C  CB  . THR A  1 350 ? 51.861  34.263 23.802  1.00 39.74 ? 350  THR A CB  1 
ATOM   2602  O  OG1 . THR A  1 350 ? 52.696  34.451 22.651  1.00 41.86 ? 350  THR A OG1 1 
ATOM   2603  C  CG2 . THR A  1 350 ? 51.355  32.810 23.798  1.00 39.56 ? 350  THR A CG2 1 
ATOM   2604  N  N   . THR A  1 351 ? 49.775  34.770 25.956  1.00 34.78 ? 351  THR A N   1 
ATOM   2605  C  CA  . THR A  1 351 ? 48.775  34.273 26.900  1.00 32.87 ? 351  THR A CA  1 
ATOM   2606  C  C   . THR A  1 351 ? 47.592  35.206 27.160  1.00 30.55 ? 351  THR A C   1 
ATOM   2607  O  O   . THR A  1 351 ? 46.498  34.754 27.501  1.00 30.01 ? 351  THR A O   1 
ATOM   2608  C  CB  . THR A  1 351 ? 49.431  33.928 28.244  1.00 33.48 ? 351  THR A CB  1 
ATOM   2609  O  OG1 . THR A  1 351 ? 50.236  35.028 28.683  1.00 35.42 ? 351  THR A OG1 1 
ATOM   2610  C  CG2 . THR A  1 351 ? 50.311  32.710 28.092  1.00 36.16 ? 351  THR A CG2 1 
ATOM   2611  N  N   . GLY A  1 352 ? 47.809  36.506 27.007  1.00 28.75 ? 352  GLY A N   1 
ATOM   2612  C  CA  . GLY A  1 352 ? 46.738  37.452 27.251  1.00 26.23 ? 352  GLY A CA  1 
ATOM   2613  C  C   . GLY A  1 352 ? 46.957  38.772 26.554  1.00 24.68 ? 352  GLY A C   1 
ATOM   2614  O  O   . GLY A  1 352 ? 47.218  38.812 25.349  1.00 24.76 ? 352  GLY A O   1 
ATOM   2615  N  N   . TRP A  1 353 ? 46.878  39.857 27.319  1.00 22.51 ? 353  TRP A N   1 
ATOM   2616  C  CA  . TRP A  1 353 ? 47.059  41.191 26.770  1.00 19.57 ? 353  TRP A CA  1 
ATOM   2617  C  C   . TRP A  1 353 ? 48.484  41.655 27.072  1.00 18.56 ? 353  TRP A C   1 
ATOM   2618  O  O   . TRP A  1 353 ? 49.281  40.878 27.580  1.00 17.85 ? 353  TRP A O   1 
ATOM   2619  C  CB  . TRP A  1 353 ? 45.999  42.120 27.382  1.00 18.98 ? 353  TRP A CB  1 
ATOM   2620  C  CG  . TRP A  1 353 ? 46.013  42.138 28.902  1.00 17.76 ? 353  TRP A CG  1 
ATOM   2621  C  CD1 . TRP A  1 353 ? 46.683  43.016 29.697  1.00 17.32 ? 353  TRP A CD1 1 
ATOM   2622  C  CD2 . TRP A  1 353 ? 45.346  41.220 29.789  1.00 18.02 ? 353  TRP A CD2 1 
ATOM   2623  N  NE1 . TRP A  1 353 ? 46.481  42.709 31.025  1.00 17.97 ? 353  TRP A NE1 1 
ATOM   2624  C  CE2 . TRP A  1 353 ? 45.665  41.610 31.110  1.00 16.91 ? 353  TRP A CE2 1 
ATOM   2625  C  CE3 . TRP A  1 353 ? 44.510  40.105 29.593  1.00 18.21 ? 353  TRP A CE3 1 
ATOM   2626  C  CZ2 . TRP A  1 353 ? 45.182  40.929 32.231  1.00 15.45 ? 353  TRP A CZ2 1 
ATOM   2627  C  CZ3 . TRP A  1 353 ? 44.026  39.428 30.712  1.00 16.17 ? 353  TRP A CZ3 1 
ATOM   2628  C  CH2 . TRP A  1 353 ? 44.367  39.847 32.016  1.00 15.73 ? 353  TRP A CH2 1 
ATOM   2629  N  N   . VAL A  1 354 ? 48.810  42.909 26.765  1.00 17.75 ? 354  VAL A N   1 
ATOM   2630  C  CA  . VAL A  1 354 ? 50.156  43.439 27.008  1.00 17.44 ? 354  VAL A CA  1 
ATOM   2631  C  C   . VAL A  1 354 ? 50.211  44.356 28.247  1.00 17.35 ? 354  VAL A C   1 
ATOM   2632  O  O   . VAL A  1 354 ? 49.457  45.326 28.340  1.00 17.26 ? 354  VAL A O   1 
ATOM   2633  C  CB  . VAL A  1 354 ? 50.645  44.213 25.766  1.00 18.25 ? 354  VAL A CB  1 
ATOM   2634  C  CG1 . VAL A  1 354 ? 52.028  44.828 26.019  1.00 17.69 ? 354  VAL A CG1 1 
ATOM   2635  C  CG2 . VAL A  1 354 ? 50.697  43.262 24.571  1.00 18.54 ? 354  VAL A CG2 1 
ATOM   2636  N  N   . GLY A  1 355 ? 51.102  44.045 29.188  1.00 15.57 ? 355  GLY A N   1 
ATOM   2637  C  CA  . GLY A  1 355 ? 51.218  44.842 30.409  1.00 16.00 ? 355  GLY A CA  1 
ATOM   2638  C  C   . GLY A  1 355 ? 50.109  44.574 31.426  1.00 15.37 ? 355  GLY A C   1 
ATOM   2639  O  O   . GLY A  1 355 ? 49.198  43.792 31.154  1.00 16.85 ? 355  GLY A O   1 
ATOM   2640  N  N   . ARG A  1 356 ? 50.183  45.195 32.600  1.00 13.73 ? 356  ARG A N   1 
ATOM   2641  C  CA  . ARG A  1 356 ? 49.143  45.001 33.620  1.00 13.90 ? 356  ARG A CA  1 
ATOM   2642  C  C   . ARG A  1 356 ? 47.843  45.656 33.162  1.00 14.36 ? 356  ARG A C   1 
ATOM   2643  O  O   . ARG A  1 356 ? 46.831  44.961 33.001  1.00 14.97 ? 356  ARG A O   1 
ATOM   2644  C  CB  . ARG A  1 356 ? 49.617  45.540 34.994  1.00 11.96 ? 356  ARG A CB  1 
ATOM   2645  C  CG  . ARG A  1 356 ? 50.775  44.665 35.567  1.00 12.52 ? 356  ARG A CG  1 
ATOM   2646  C  CD  . ARG A  1 356 ? 51.098  44.928 37.023  1.00 12.85 ? 356  ARG A CD  1 
ATOM   2647  N  NE  . ARG A  1 356 ? 52.025  43.934 37.579  1.00 13.01 ? 356  ARG A NE  1 
ATOM   2648  C  CZ  . ARG A  1 356 ? 53.312  44.159 37.849  1.00 13.18 ? 356  ARG A CZ  1 
ATOM   2649  N  NH1 . ARG A  1 356 ? 53.860  45.347 37.605  1.00 13.76 ? 356  ARG A NH1 1 
ATOM   2650  N  NH2 . ARG A  1 356 ? 54.040  43.213 38.423  1.00 12.36 ? 356  ARG A NH2 1 
ATOM   2651  N  N   . PHE A  1 357 ? 47.877  46.970 32.949  1.00 13.41 ? 357  PHE A N   1 
ATOM   2652  C  CA  . PHE A  1 357 ? 46.721  47.719 32.459  1.00 15.38 ? 357  PHE A CA  1 
ATOM   2653  C  C   . PHE A  1 357 ? 47.089  48.434 31.157  1.00 16.20 ? 357  PHE A C   1 
ATOM   2654  O  O   . PHE A  1 357 ? 46.220  48.979 30.470  1.00 16.56 ? 357  PHE A O   1 
ATOM   2655  C  CB  . PHE A  1 357 ? 46.237  48.735 33.496  1.00 13.97 ? 357  PHE A CB  1 
ATOM   2656  C  CG  . PHE A  1 357 ? 45.537  48.109 34.655  1.00 14.60 ? 357  PHE A CG  1 
ATOM   2657  C  CD1 . PHE A  1 357 ? 44.211  47.727 34.548  1.00 14.87 ? 357  PHE A CD1 1 
ATOM   2658  C  CD2 . PHE A  1 357 ? 46.214  47.856 35.838  1.00 15.03 ? 357  PHE A CD2 1 
ATOM   2659  C  CE1 . PHE A  1 357 ? 43.562  47.103 35.597  1.00 15.03 ? 357  PHE A CE1 1 
ATOM   2660  C  CE2 . PHE A  1 357 ? 45.574  47.222 36.907  1.00 16.21 ? 357  PHE A CE2 1 
ATOM   2661  C  CZ  . PHE A  1 357 ? 44.247  46.849 36.777  1.00 16.48 ? 357  PHE A CZ  1 
ATOM   2662  N  N   . ARG A  1 358 ? 48.379  48.402 30.818  1.00 17.23 ? 358  ARG A N   1 
ATOM   2663  C  CA  . ARG A  1 358 ? 48.910  49.014 29.590  1.00 18.87 ? 358  ARG A CA  1 
ATOM   2664  C  C   . ARG A  1 358 ? 50.382  48.635 29.400  1.00 18.62 ? 358  ARG A C   1 
ATOM   2665  O  O   . ARG A  1 358 ? 51.022  48.161 30.326  1.00 19.01 ? 358  ARG A O   1 
ATOM   2666  C  CB  . ARG A  1 358 ? 48.791  50.535 29.655  1.00 19.19 ? 358  ARG A CB  1 
ATOM   2667  C  CG  . ARG A  1 358 ? 49.680  51.193 30.713  1.00 23.86 ? 358  ARG A CG  1 
ATOM   2668  C  CD  . ARG A  1 358 ? 49.651  52.716 30.495  1.00 28.34 ? 358  ARG A CD  1 
ATOM   2669  N  NE  . ARG A  1 358 ? 50.458  53.456 31.443  1.00 31.51 ? 358  ARG A NE  1 
ATOM   2670  C  CZ  . ARG A  1 358 ? 50.229  54.715 31.816  1.00 33.21 ? 358  ARG A CZ  1 
ATOM   2671  N  NH1 . ARG A  1 358 ? 49.200  55.390 31.325  1.00 31.35 ? 358  ARG A NH1 1 
ATOM   2672  N  NH2 . ARG A  1 358 ? 51.052  55.307 32.680  1.00 34.09 ? 358  ARG A NH2 1 
ATOM   2673  N  N   . PRO A  1 359 ? 50.932  48.811 28.183  1.00 18.84 ? 359  PRO A N   1 
ATOM   2674  C  CA  . PRO A  1 359 ? 52.349  48.458 27.982  1.00 17.71 ? 359  PRO A CA  1 
ATOM   2675  C  C   . PRO A  1 359 ? 53.175  49.251 29.002  1.00 17.71 ? 359  PRO A C   1 
ATOM   2676  O  O   . PRO A  1 359 ? 52.863  50.404 29.277  1.00 17.74 ? 359  PRO A O   1 
ATOM   2677  C  CB  . PRO A  1 359 ? 52.611  48.887 26.533  1.00 17.69 ? 359  PRO A CB  1 
ATOM   2678  C  CG  . PRO A  1 359 ? 51.255  48.649 25.874  1.00 18.07 ? 359  PRO A CG  1 
ATOM   2679  C  CD  . PRO A  1 359 ? 50.313  49.247 26.923  1.00 18.52 ? 359  PRO A CD  1 
ATOM   2680  N  N   . SER A  1 360 ? 54.222  48.652 29.560  1.00 18.33 ? 360  SER A N   1 
ATOM   2681  C  CA  . SER A  1 360 ? 55.001  49.334 30.599  1.00 19.13 ? 360  SER A CA  1 
ATOM   2682  C  C   . SER A  1 360 ? 55.820  50.528 30.086  1.00 18.86 ? 360  SER A C   1 
ATOM   2683  O  O   . SER A  1 360 ? 56.260  50.542 28.938  1.00 18.45 ? 360  SER A O   1 
ATOM   2684  C  CB  . SER A  1 360 ? 55.909  48.328 31.323  1.00 19.59 ? 360  SER A CB  1 
ATOM   2685  O  OG  . SER A  1 360 ? 56.821  47.704 30.435  1.00 21.53 ? 360  SER A OG  1 
ATOM   2686  N  N   . GLU A  1 361 ? 56.035  51.516 30.946  1.00 18.75 ? 361  GLU A N   1 
ATOM   2687  C  CA  . GLU A  1 361 ? 56.767  52.700 30.537  1.00 21.21 ? 361  GLU A CA  1 
ATOM   2688  C  C   . GLU A  1 361 ? 58.269  52.458 30.542  1.00 20.20 ? 361  GLU A C   1 
ATOM   2689  O  O   . GLU A  1 361 ? 58.797  51.690 31.353  1.00 19.58 ? 361  GLU A O   1 
ATOM   2690  C  CB  . GLU A  1 361 ? 56.432  53.901 31.425  1.00 22.71 ? 361  GLU A CB  1 
ATOM   2691  C  CG  . GLU A  1 361 ? 57.098  53.885 32.770  1.00 28.90 ? 361  GLU A CG  1 
ATOM   2692  C  CD  . GLU A  1 361 ? 56.283  53.146 33.818  1.00 32.26 ? 361  GLU A CD  1 
ATOM   2693  O  OE1 . GLU A  1 361 ? 55.619  52.133 33.476  1.00 33.74 ? 361  GLU A OE1 1 
ATOM   2694  O  OE2 . GLU A  1 361 ? 56.322  53.584 34.992  1.00 35.37 ? 361  GLU A OE2 1 
ATOM   2695  N  N   . PRO A  1 362 ? 58.985  53.124 29.630  1.00 19.30 ? 362  PRO A N   1 
ATOM   2696  C  CA  . PRO A  1 362 ? 60.441  52.937 29.573  1.00 18.71 ? 362  PRO A CA  1 
ATOM   2697  C  C   . PRO A  1 362 ? 61.160  53.864 30.539  1.00 18.31 ? 362  PRO A C   1 
ATOM   2698  O  O   . PRO A  1 362 ? 60.680  54.946 30.822  1.00 18.89 ? 362  PRO A O   1 
ATOM   2699  C  CB  . PRO A  1 362 ? 60.763  53.265 28.119  1.00 18.57 ? 362  PRO A CB  1 
ATOM   2700  C  CG  . PRO A  1 362 ? 59.809  54.443 27.852  1.00 18.40 ? 362  PRO A CG  1 
ATOM   2701  C  CD  . PRO A  1 362 ? 58.504  54.018 28.556  1.00 18.45 ? 362  PRO A CD  1 
ATOM   2702  N  N   . HIS A  1 363 ? 62.302  53.434 31.060  1.00 17.46 ? 363  HIS A N   1 
ATOM   2703  C  CA  . HIS A  1 363 ? 63.093  54.274 31.956  1.00 18.34 ? 363  HIS A CA  1 
ATOM   2704  C  C   . HIS A  1 363 ? 64.481  54.426 31.345  1.00 18.07 ? 363  HIS A C   1 
ATOM   2705  O  O   . HIS A  1 363 ? 65.326  53.544 31.466  1.00 17.23 ? 363  HIS A O   1 
ATOM   2706  C  CB  . HIS A  1 363 ? 63.181  53.647 33.340  1.00 18.38 ? 363  HIS A CB  1 
ATOM   2707  C  CG  . HIS A  1 363 ? 61.870  53.629 34.050  1.00 18.87 ? 363  HIS A CG  1 
ATOM   2708  N  ND1 . HIS A  1 363 ? 61.509  54.596 34.961  1.00 18.19 ? 363  HIS A ND1 1 
ATOM   2709  C  CD2 . HIS A  1 363 ? 60.798  52.810 33.921  1.00 18.81 ? 363  HIS A CD2 1 
ATOM   2710  C  CE1 . HIS A  1 363 ? 60.269  54.379 35.362  1.00 18.83 ? 363  HIS A CE1 1 
ATOM   2711  N  NE2 . HIS A  1 363 ? 59.815  53.300 34.748  1.00 19.93 ? 363  HIS A NE2 1 
ATOM   2712  N  N   . PHE A  1 364 ? 64.700  55.558 30.686  1.00 18.34 ? 364  PHE A N   1 
ATOM   2713  C  CA  . PHE A  1 364 ? 65.960  55.827 30.007  1.00 18.94 ? 364  PHE A CA  1 
ATOM   2714  C  C   . PHE A  1 364 ? 67.117  56.242 30.894  1.00 18.95 ? 364  PHE A C   1 
ATOM   2715  O  O   . PHE A  1 364 ? 66.934  56.903 31.919  1.00 17.55 ? 364  PHE A O   1 
ATOM   2716  C  CB  . PHE A  1 364 ? 65.763  56.924 28.951  1.00 19.32 ? 364  PHE A CB  1 
ATOM   2717  C  CG  . PHE A  1 364 ? 64.971  56.482 27.763  1.00 19.41 ? 364  PHE A CG  1 
ATOM   2718  C  CD1 . PHE A  1 364 ? 63.587  56.620 27.743  1.00 19.57 ? 364  PHE A CD1 1 
ATOM   2719  C  CD2 . PHE A  1 364 ? 65.608  55.886 26.673  1.00 18.31 ? 364  PHE A CD2 1 
ATOM   2720  C  CE1 . PHE A  1 364 ? 62.849  56.168 26.652  1.00 20.29 ? 364  PHE A CE1 1 
ATOM   2721  C  CE2 . PHE A  1 364 ? 64.880  55.433 25.587  1.00 19.04 ? 364  PHE A CE2 1 
ATOM   2722  C  CZ  . PHE A  1 364 ? 63.498  55.573 25.575  1.00 20.17 ? 364  PHE A CZ  1 
ATOM   2723  N  N   . THR A  1 365 ? 68.317  55.865 30.471  1.00 19.59 ? 365  THR A N   1 
ATOM   2724  C  CA  . THR A  1 365 ? 69.538  56.249 31.177  1.00 20.44 ? 365  THR A CA  1 
ATOM   2725  C  C   . THR A  1 365 ? 69.802  57.728 30.862  1.00 22.00 ? 365  THR A C   1 
ATOM   2726  O  O   . THR A  1 365 ? 69.100  58.332 30.030  1.00 21.31 ? 365  THR A O   1 
ATOM   2727  C  CB  . THR A  1 365 ? 70.748  55.443 30.672  1.00 20.17 ? 365  THR A CB  1 
ATOM   2728  O  OG1 . THR A  1 365 ? 70.860  55.612 29.248  1.00 18.51 ? 365  THR A OG1 1 
ATOM   2729  C  CG2 . THR A  1 365 ? 70.578  53.953 31.002  1.00 17.71 ? 365  THR A CG2 1 
ATOM   2730  N  N   . LEU A  1 366 ? 70.823  58.300 31.498  1.00 23.06 ? 366  LEU A N   1 
ATOM   2731  C  CA  . LEU A  1 366 ? 71.173  59.707 31.285  1.00 25.58 ? 366  LEU A CA  1 
ATOM   2732  C  C   . LEU A  1 366 ? 71.398  60.063 29.813  1.00 25.41 ? 366  LEU A C   1 
ATOM   2733  O  O   . LEU A  1 366 ? 70.840  61.049 29.324  1.00 26.44 ? 366  LEU A O   1 
ATOM   2734  C  CB  . LEU A  1 366 ? 72.425  60.059 32.090  1.00 27.48 ? 366  LEU A CB  1 
ATOM   2735  C  CG  . LEU A  1 366 ? 72.712  61.548 32.258  1.00 30.35 ? 366  LEU A CG  1 
ATOM   2736  C  CD1 . LEU A  1 366 ? 71.552  62.189 33.018  1.00 31.42 ? 366  LEU A CD1 1 
ATOM   2737  C  CD2 . LEU A  1 366 ? 74.029  61.748 33.023  1.00 32.10 ? 366  LEU A CD2 1 
ATOM   2738  N  N   . ASP A  1 367 ? 72.196  59.267 29.103  1.00 24.31 ? 367  ASP A N   1 
ATOM   2739  C  CA  . ASP A  1 367 ? 72.465  59.547 27.686  1.00 23.86 ? 367  ASP A CA  1 
ATOM   2740  C  C   . ASP A  1 367 ? 71.343  59.097 26.741  1.00 22.86 ? 367  ASP A C   1 
ATOM   2741  O  O   . ASP A  1 367 ? 71.437  59.275 25.529  1.00 22.81 ? 367  ASP A O   1 
ATOM   2742  C  CB  . ASP A  1 367 ? 73.790  58.903 27.236  1.00 24.10 ? 367  ASP A CB  1 
ATOM   2743  C  CG  . ASP A  1 367 ? 73.812  57.373 27.425  1.00 26.01 ? 367  ASP A CG  1 
ATOM   2744  O  OD1 . ASP A  1 367 ? 72.742  56.719 27.389  1.00 24.64 ? 367  ASP A OD1 1 
ATOM   2745  O  OD2 . ASP A  1 367 ? 74.920  56.820 27.586  1.00 26.11 ? 367  ASP A OD2 1 
ATOM   2746  N  N   . GLY A  1 368 ? 70.291  58.500 27.288  1.00 20.96 ? 368  GLY A N   1 
ATOM   2747  C  CA  . GLY A  1 368 ? 69.198  58.060 26.445  1.00 19.05 ? 368  GLY A CA  1 
ATOM   2748  C  C   . GLY A  1 368 ? 69.544  56.976 25.444  1.00 19.88 ? 368  GLY A C   1 
ATOM   2749  O  O   . GLY A  1 368 ? 68.784  56.771 24.500  1.00 18.52 ? 368  GLY A O   1 
ATOM   2750  N  N   . ASN A  1 369 ? 70.666  56.269 25.636  1.00 19.28 ? 369  ASN A N   1 
ATOM   2751  C  CA  . ASN A  1 369 ? 71.048  55.212 24.694  1.00 19.15 ? 369  ASN A CA  1 
ATOM   2752  C  C   . ASN A  1 369 ? 70.528  53.815 25.027  1.00 18.40 ? 369  ASN A C   1 
ATOM   2753  O  O   . ASN A  1 369 ? 70.592  52.913 24.201  1.00 17.28 ? 369  ASN A O   1 
ATOM   2754  C  CB  . ASN A  1 369 ? 72.572  55.154 24.518  1.00 19.12 ? 369  ASN A CB  1 
ATOM   2755  C  CG  . ASN A  1 369 ? 73.112  56.379 23.799  1.00 20.74 ? 369  ASN A CG  1 
ATOM   2756  O  OD1 . ASN A  1 369 ? 72.418  56.973 22.970  1.00 19.82 ? 369  ASN A OD1 1 
ATOM   2757  N  ND2 . ASN A  1 369 ? 74.351  56.758 24.109  1.00 19.86 ? 369  ASN A ND2 1 
ATOM   2758  N  N   . SER A  1 370 ? 69.993  53.644 26.231  1.00 18.09 ? 370  SER A N   1 
ATOM   2759  C  CA  . SER A  1 370 ? 69.456  52.359 26.636  1.00 17.64 ? 370  SER A CA  1 
ATOM   2760  C  C   . SER A  1 370 ? 68.334  52.647 27.637  1.00 17.84 ? 370  SER A C   1 
ATOM   2761  O  O   . SER A  1 370 ? 68.218  53.775 28.114  1.00 18.45 ? 370  SER A O   1 
ATOM   2762  C  CB  . SER A  1 370 ? 70.560  51.493 27.259  1.00 17.17 ? 370  SER A CB  1 
ATOM   2763  O  OG  . SER A  1 370 ? 71.187  52.138 28.348  1.00 18.89 ? 370  SER A OG  1 
ATOM   2764  N  N   . PHE A  1 371 ? 67.496  51.657 27.927  1.00 16.50 ? 371  PHE A N   1 
ATOM   2765  C  CA  . PHE A  1 371 ? 66.398  51.866 28.865  1.00 16.67 ? 371  PHE A CA  1 
ATOM   2766  C  C   . PHE A  1 371 ? 65.960  50.577 29.526  1.00 17.49 ? 371  PHE A C   1 
ATOM   2767  O  O   . PHE A  1 371 ? 66.266  49.487 29.034  1.00 15.79 ? 371  PHE A O   1 
ATOM   2768  C  CB  . PHE A  1 371 ? 65.205  52.513 28.149  1.00 16.80 ? 371  PHE A CB  1 
ATOM   2769  C  CG  . PHE A  1 371 ? 64.619  51.682 27.036  1.00 16.92 ? 371  PHE A CG  1 
ATOM   2770  C  CD1 . PHE A  1 371 ? 63.599  50.769 27.295  1.00 17.53 ? 371  PHE A CD1 1 
ATOM   2771  C  CD2 . PHE A  1 371 ? 65.038  51.861 25.719  1.00 18.00 ? 371  PHE A CD2 1 
ATOM   2772  C  CE1 . PHE A  1 371 ? 62.995  50.046 26.256  1.00 17.22 ? 371  PHE A CE1 1 
ATOM   2773  C  CE2 . PHE A  1 371 ? 64.443  51.148 24.675  1.00 17.59 ? 371  PHE A CE2 1 
ATOM   2774  C  CZ  . PHE A  1 371 ? 63.416  50.237 24.946  1.00 18.09 ? 371  PHE A CZ  1 
ATOM   2775  N  N   . TYR A  1 372 ? 65.237  50.727 30.641  1.00 16.91 ? 372  TYR A N   1 
ATOM   2776  C  CA  . TYR A  1 372 ? 64.732  49.603 31.406  1.00 16.80 ? 372  TYR A CA  1 
ATOM   2777  C  C   . TYR A  1 372 ? 63.214  49.606 31.352  1.00 17.92 ? 372  TYR A C   1 
ATOM   2778  O  O   . TYR A  1 372 ? 62.561  50.656 31.334  1.00 17.71 ? 372  TYR A O   1 
ATOM   2779  C  CB  . TYR A  1 372 ? 65.199  49.672 32.857  1.00 16.42 ? 372  TYR A CB  1 
ATOM   2780  C  CG  . TYR A  1 372 ? 66.700  49.667 33.004  1.00 16.18 ? 372  TYR A CG  1 
ATOM   2781  C  CD1 . TYR A  1 372 ? 67.435  50.853 32.910  1.00 16.50 ? 372  TYR A CD1 1 
ATOM   2782  C  CD2 . TYR A  1 372 ? 67.388  48.478 33.201  1.00 15.78 ? 372  TYR A CD2 1 
ATOM   2783  C  CE1 . TYR A  1 372 ? 68.829  50.851 33.011  1.00 16.92 ? 372  TYR A CE1 1 
ATOM   2784  C  CE2 . TYR A  1 372 ? 68.776  48.456 33.300  1.00 18.22 ? 372  TYR A CE2 1 
ATOM   2785  C  CZ  . TYR A  1 372 ? 69.488  49.637 33.203  1.00 17.98 ? 372  TYR A CZ  1 
ATOM   2786  O  OH  . TYR A  1 372 ? 70.853  49.596 33.271  1.00 17.62 ? 372  TYR A OH  1 
ATOM   2787  N  N   . LYS A  1 373 ? 62.648  48.419 31.307  1.00 18.00 ? 373  LYS A N   1 
ATOM   2788  C  CA  . LYS A  1 373 ? 61.207  48.309 31.228  1.00 18.95 ? 373  LYS A CA  1 
ATOM   2789  C  C   . LYS A  1 373 ? 60.784  46.981 31.861  1.00 18.58 ? 373  LYS A C   1 
ATOM   2790  O  O   . LYS A  1 373 ? 61.489  45.975 31.743  1.00 18.52 ? 373  LYS A O   1 
ATOM   2791  C  CB  . LYS A  1 373 ? 60.817  48.383 29.748  1.00 20.99 ? 373  LYS A CB  1 
ATOM   2792  C  CG  . LYS A  1 373 ? 59.363  48.234 29.449  1.00 22.29 ? 373  LYS A CG  1 
ATOM   2793  C  CD  . LYS A  1 373 ? 59.059  48.325 27.921  1.00 23.25 ? 373  LYS A CD  1 
ATOM   2794  C  CE  . LYS A  1 373 ? 59.298  49.723 27.377  1.00 24.43 ? 373  LYS A CE  1 
ATOM   2795  N  NZ  . LYS A  1 373 ? 58.651  49.964 26.037  1.00 25.35 ? 373  LYS A NZ  1 
ATOM   2796  N  N   . ILE A  1 374 ? 59.658  46.995 32.561  1.00 17.09 ? 374  ILE A N   1 
ATOM   2797  C  CA  . ILE A  1 374 ? 59.137  45.798 33.181  1.00 16.43 ? 374  ILE A CA  1 
ATOM   2798  C  C   . ILE A  1 374 ? 58.410  45.003 32.112  1.00 17.53 ? 374  ILE A C   1 
ATOM   2799  O  O   . ILE A  1 374 ? 57.537  45.533 31.446  1.00 17.53 ? 374  ILE A O   1 
ATOM   2800  C  CB  . ILE A  1 374 ? 58.117  46.143 34.300  1.00 16.00 ? 374  ILE A CB  1 
ATOM   2801  C  CG1 . ILE A  1 374 ? 58.823  46.838 35.454  1.00 14.09 ? 374  ILE A CG1 1 
ATOM   2802  C  CG2 . ILE A  1 374 ? 57.380  44.861 34.763  1.00 14.07 ? 374  ILE A CG2 1 
ATOM   2803  C  CD1 . ILE A  1 374 ? 57.888  47.403 36.498  1.00 15.83 ? 374  ILE A CD1 1 
ATOM   2804  N  N   . ILE A  1 375 ? 58.765  43.739 31.936  1.00 17.58 ? 375  ILE A N   1 
ATOM   2805  C  CA  . ILE A  1 375 ? 58.073  42.925 30.949  1.00 18.80 ? 375  ILE A CA  1 
ATOM   2806  C  C   . ILE A  1 375 ? 57.944  41.503 31.482  1.00 18.41 ? 375  ILE A C   1 
ATOM   2807  O  O   . ILE A  1 375 ? 58.766  41.043 32.277  1.00 16.62 ? 375  ILE A O   1 
ATOM   2808  C  CB  . ILE A  1 375 ? 58.793  42.891 29.555  1.00 21.47 ? 375  ILE A CB  1 
ATOM   2809  C  CG1 . ILE A  1 375 ? 60.124  42.192 29.658  1.00 22.25 ? 375  ILE A CG1 1 
ATOM   2810  C  CG2 . ILE A  1 375 ? 59.006  44.330 28.993  1.00 20.86 ? 375  ILE A CG2 1 
ATOM   2811  C  CD1 . ILE A  1 375 ? 60.858  42.156 28.321  1.00 26.92 ? 375  ILE A CD1 1 
ATOM   2812  N  N   . SER A  1 376 ? 56.901  40.805 31.050  1.00 19.16 ? 376  SER A N   1 
ATOM   2813  C  CA  . SER A  1 376 ? 56.689  39.448 31.509  1.00 20.51 ? 376  SER A CA  1 
ATOM   2814  C  C   . SER A  1 376 ? 57.742  38.536 30.882  1.00 20.42 ? 376  SER A C   1 
ATOM   2815  O  O   . SER A  1 376 ? 57.914  38.526 29.666  1.00 19.77 ? 376  SER A O   1 
ATOM   2816  C  CB  . SER A  1 376 ? 55.282  38.987 31.126  1.00 21.77 ? 376  SER A CB  1 
ATOM   2817  O  OG  . SER A  1 376 ? 55.088  37.645 31.572  1.00 25.78 ? 376  SER A OG  1 
ATOM   2818  N  N   . ASN A  1 377 ? 58.441  37.775 31.718  1.00 21.03 ? 377  ASN A N   1 
ATOM   2819  C  CA  . ASN A  1 377 ? 59.480  36.878 31.236  1.00 21.72 ? 377  ASN A CA  1 
ATOM   2820  C  C   . ASN A  1 377 ? 58.889  35.560 30.725  1.00 23.86 ? 377  ASN A C   1 
ATOM   2821  O  O   . ASN A  1 377 ? 57.663  35.409 30.656  1.00 24.31 ? 377  ASN A O   1 
ATOM   2822  C  CB  . ASN A  1 377 ? 60.513  36.633 32.336  1.00 19.30 ? 377  ASN A CB  1 
ATOM   2823  C  CG  . ASN A  1 377 ? 59.973  35.824 33.495  1.00 17.64 ? 377  ASN A CG  1 
ATOM   2824  O  OD1 . ASN A  1 377 ? 58.879  35.263 33.431  1.00 16.95 ? 377  ASN A OD1 1 
ATOM   2825  N  ND2 . ASN A  1 377 ? 60.761  35.741 34.564  1.00 16.91 ? 377  ASN A ND2 1 
ATOM   2826  N  N   . GLU A  1 378 ? 59.746  34.610 30.372  1.00 26.39 ? 378  GLU A N   1 
ATOM   2827  C  CA  . GLU A  1 378 ? 59.290  33.323 29.836  1.00 29.27 ? 378  GLU A CA  1 
ATOM   2828  C  C   . GLU A  1 378 ? 58.466  32.501 30.817  1.00 28.96 ? 378  GLU A C   1 
ATOM   2829  O  O   . GLU A  1 378 ? 57.730  31.609 30.415  1.00 28.64 ? 378  GLU A O   1 
ATOM   2830  C  CB  . GLU A  1 378 ? 60.489  32.506 29.354  1.00 31.91 ? 378  GLU A CB  1 
ATOM   2831  C  CG  . GLU A  1 378 ? 61.284  33.212 28.268  1.00 37.15 ? 378  GLU A CG  1 
ATOM   2832  C  CD  . GLU A  1 378 ? 60.578  33.213 26.911  1.00 41.13 ? 378  GLU A CD  1 
ATOM   2833  O  OE1 . GLU A  1 378 ? 61.108  33.852 25.964  1.00 42.95 ? 378  GLU A OE1 1 
ATOM   2834  O  OE2 . GLU A  1 378 ? 59.499  32.572 26.778  1.00 43.76 ? 378  GLU A OE2 1 
ATOM   2835  N  N   . GLU A  1 379 ? 58.593  32.807 32.102  1.00 28.84 ? 379  GLU A N   1 
ATOM   2836  C  CA  . GLU A  1 379 ? 57.847  32.104 33.133  1.00 28.55 ? 379  GLU A CA  1 
ATOM   2837  C  C   . GLU A  1 379 ? 56.522  32.819 33.391  1.00 27.19 ? 379  GLU A C   1 
ATOM   2838  O  O   . GLU A  1 379 ? 55.682  32.349 34.164  1.00 26.76 ? 379  GLU A O   1 
ATOM   2839  C  CB  . GLU A  1 379 ? 58.661  32.064 34.422  1.00 31.18 ? 379  GLU A CB  1 
ATOM   2840  C  CG  . GLU A  1 379 ? 59.884  31.202 34.352  1.00 35.16 ? 379  GLU A CG  1 
ATOM   2841  C  CD  . GLU A  1 379 ? 59.528  29.773 34.038  1.00 38.59 ? 379  GLU A CD  1 
ATOM   2842  O  OE1 . GLU A  1 379 ? 58.643  29.210 34.734  1.00 40.06 ? 379  GLU A OE1 1 
ATOM   2843  O  OE2 . GLU A  1 379 ? 60.128  29.205 33.094  1.00 41.54 ? 379  GLU A OE2 1 
ATOM   2844  N  N   . GLY A  1 380 ? 56.332  33.962 32.747  1.00 25.52 ? 380  GLY A N   1 
ATOM   2845  C  CA  . GLY A  1 380 ? 55.101  34.704 32.947  1.00 23.12 ? 380  GLY A CA  1 
ATOM   2846  C  C   . GLY A  1 380 ? 55.183  35.628 34.154  1.00 22.64 ? 380  GLY A C   1 
ATOM   2847  O  O   . GLY A  1 380 ? 54.163  36.104 34.644  1.00 22.20 ? 380  GLY A O   1 
ATOM   2848  N  N   . TYR A  1 381 ? 56.395  35.890 34.643  1.00 21.48 ? 381  TYR A N   1 
ATOM   2849  C  CA  . TYR A  1 381 ? 56.558  36.784 35.780  1.00 19.24 ? 381  TYR A CA  1 
ATOM   2850  C  C   . TYR A  1 381 ? 57.177  38.091 35.319  1.00 19.47 ? 381  TYR A C   1 
ATOM   2851  O  O   . TYR A  1 381 ? 58.185  38.088 34.588  1.00 18.71 ? 381  TYR A O   1 
ATOM   2852  C  CB  . TYR A  1 381 ? 57.433  36.146 36.849  1.00 19.38 ? 381  TYR A CB  1 
ATOM   2853  C  CG  . TYR A  1 381 ? 56.715  35.066 37.606  1.00 19.19 ? 381  TYR A CG  1 
ATOM   2854  C  CD1 . TYR A  1 381 ? 56.760  33.729 37.183  1.00 19.71 ? 381  TYR A CD1 1 
ATOM   2855  C  CD2 . TYR A  1 381 ? 55.968  35.376 38.733  1.00 19.26 ? 381  TYR A CD2 1 
ATOM   2856  C  CE1 . TYR A  1 381 ? 56.072  32.724 37.887  1.00 19.56 ? 381  TYR A CE1 1 
ATOM   2857  C  CE2 . TYR A  1 381 ? 55.275  34.378 39.441  1.00 20.52 ? 381  TYR A CE2 1 
ATOM   2858  C  CZ  . TYR A  1 381 ? 55.340  33.060 39.008  1.00 19.63 ? 381  TYR A CZ  1 
ATOM   2859  O  OH  . TYR A  1 381 ? 54.681  32.088 39.728  1.00 22.95 ? 381  TYR A OH  1 
ATOM   2860  N  N   . ARG A  1 382 ? 56.576  39.199 35.751  1.00 17.52 ? 382  ARG A N   1 
ATOM   2861  C  CA  . ARG A  1 382 ? 57.032  40.527 35.363  1.00 15.80 ? 382  ARG A CA  1 
ATOM   2862  C  C   . ARG A  1 382 ? 58.315  40.962 36.054  1.00 15.63 ? 382  ARG A C   1 
ATOM   2863  O  O   . ARG A  1 382 ? 58.382  41.121 37.281  1.00 14.20 ? 382  ARG A O   1 
ATOM   2864  C  CB  . ARG A  1 382 ? 55.891  41.535 35.565  1.00 16.02 ? 382  ARG A CB  1 
ATOM   2865  C  CG  . ARG A  1 382 ? 54.787  41.336 34.502  1.00 16.15 ? 382  ARG A CG  1 
ATOM   2866  C  CD  . ARG A  1 382 ? 53.402  41.965 34.826  1.00 16.14 ? 382  ARG A CD  1 
ATOM   2867  N  NE  . ARG A  1 382 ? 52.417  41.220 34.043  1.00 16.86 ? 382  ARG A NE  1 
ATOM   2868  C  CZ  . ARG A  1 382 ? 52.161  41.438 32.758  1.00 17.29 ? 382  ARG A CZ  1 
ATOM   2869  N  NH1 . ARG A  1 382 ? 52.776  42.421 32.101  1.00 16.11 ? 382  ARG A NH1 1 
ATOM   2870  N  NH2 . ARG A  1 382 ? 51.389  40.589 32.089  1.00 17.18 ? 382  ARG A NH2 1 
ATOM   2871  N  N   . HIS A  1 383 ? 59.336  41.154 35.227  1.00 15.44 ? 383  HIS A N   1 
ATOM   2872  C  CA  . HIS A  1 383 ? 60.662  41.536 35.689  1.00 14.84 ? 383  HIS A CA  1 
ATOM   2873  C  C   . HIS A  1 383 ? 61.278  42.658 34.856  1.00 14.59 ? 383  HIS A C   1 
ATOM   2874  O  O   . HIS A  1 383 ? 60.782  42.994 33.779  1.00 15.79 ? 383  HIS A O   1 
ATOM   2875  C  CB  . HIS A  1 383 ? 61.547  40.299 35.671  1.00 14.06 ? 383  HIS A CB  1 
ATOM   2876  C  CG  . HIS A  1 383 ? 61.257  39.361 36.796  1.00 15.52 ? 383  HIS A CG  1 
ATOM   2877  N  ND1 . HIS A  1 383 ? 61.735  39.573 38.070  1.00 14.56 ? 383  HIS A ND1 1 
ATOM   2878  C  CD2 . HIS A  1 383 ? 60.457  38.270 36.865  1.00 14.64 ? 383  HIS A CD2 1 
ATOM   2879  C  CE1 . HIS A  1 383 ? 61.241  38.649 38.877  1.00 16.24 ? 383  HIS A CE1 1 
ATOM   2880  N  NE2 . HIS A  1 383 ? 60.461  37.849 38.171  1.00 15.57 ? 383  HIS A NE2 1 
ATOM   2881  N  N   . ILE A  1 384 ? 62.359  43.237 35.362  1.00 13.70 ? 384  ILE A N   1 
ATOM   2882  C  CA  . ILE A  1 384 ? 63.022  44.335 34.674  1.00 13.45 ? 384  ILE A CA  1 
ATOM   2883  C  C   . ILE A  1 384 ? 63.940  43.863 33.548  1.00 15.34 ? 384  ILE A C   1 
ATOM   2884  O  O   . ILE A  1 384 ? 64.856  43.043 33.755  1.00 15.37 ? 384  ILE A O   1 
ATOM   2885  C  CB  . ILE A  1 384 ? 63.826  45.171 35.674  1.00 13.91 ? 384  ILE A CB  1 
ATOM   2886  C  CG1 . ILE A  1 384 ? 62.862  45.774 36.723  1.00 13.90 ? 384  ILE A CG1 1 
ATOM   2887  C  CG2 . ILE A  1 384 ? 64.619  46.254 34.942  1.00 13.01 ? 384  ILE A CG2 1 
ATOM   2888  C  CD1 . ILE A  1 384 ? 63.571  46.168 38.020  1.00 14.36 ? 384  ILE A CD1 1 
ATOM   2889  N  N   . CYS A  1 385 ? 63.711  44.399 32.360  1.00 15.49 ? 385  CYS A N   1 
ATOM   2890  C  CA  . CYS A  1 385 ? 64.509  44.033 31.201  1.00 17.70 ? 385  CYS A CA  1 
ATOM   2891  C  C   . CYS A  1 385 ? 65.292  45.259 30.737  1.00 17.72 ? 385  CYS A C   1 
ATOM   2892  O  O   . CYS A  1 385 ? 64.770  46.385 30.695  1.00 17.19 ? 385  CYS A O   1 
ATOM   2893  C  CB  . CYS A  1 385 ? 63.594  43.478 30.088  1.00 19.28 ? 385  CYS A CB  1 
ATOM   2894  S  SG  . CYS A  1 385 ? 64.340  42.092 29.136  1.00 26.15 ? 385  CYS A SG  1 
ATOM   2895  N  N   . TYR A  1 386 ? 66.555  45.038 30.415  1.00 16.99 ? 386  TYR A N   1 
ATOM   2896  C  CA  . TYR A  1 386 ? 67.443  46.108 29.980  1.00 18.47 ? 386  TYR A CA  1 
ATOM   2897  C  C   . TYR A  1 386 ? 67.522  46.123 28.468  1.00 18.71 ? 386  TYR A C   1 
ATOM   2898  O  O   . TYR A  1 386 ? 67.929  45.133 27.864  1.00 19.28 ? 386  TYR A O   1 
ATOM   2899  C  CB  . TYR A  1 386 ? 68.836  45.882 30.567  1.00 18.18 ? 386  TYR A CB  1 
ATOM   2900  C  CG  . TYR A  1 386 ? 69.848  46.954 30.220  1.00 19.73 ? 386  TYR A CG  1 
ATOM   2901  C  CD1 . TYR A  1 386 ? 69.481  48.292 30.194  1.00 19.57 ? 386  TYR A CD1 1 
ATOM   2902  C  CD2 . TYR A  1 386 ? 71.180  46.631 29.955  1.00 19.60 ? 386  TYR A CD2 1 
ATOM   2903  C  CE1 . TYR A  1 386 ? 70.402  49.285 29.917  1.00 21.07 ? 386  TYR A CE1 1 
ATOM   2904  C  CE2 . TYR A  1 386 ? 72.116  47.624 29.678  1.00 21.27 ? 386  TYR A CE2 1 
ATOM   2905  C  CZ  . TYR A  1 386 ? 71.723  48.944 29.659  1.00 20.39 ? 386  TYR A CZ  1 
ATOM   2906  O  OH  . TYR A  1 386 ? 72.626  49.935 29.354  1.00 21.28 ? 386  TYR A OH  1 
ATOM   2907  N  N   . PHE A  1 387 ? 67.137  47.246 27.866  1.00 18.66 ? 387  PHE A N   1 
ATOM   2908  C  CA  . PHE A  1 387 ? 67.142  47.405 26.409  1.00 18.24 ? 387  PHE A CA  1 
ATOM   2909  C  C   . PHE A  1 387 ? 68.213  48.385 25.924  1.00 19.17 ? 387  PHE A C   1 
ATOM   2910  O  O   . PHE A  1 387 ? 68.534  49.359 26.605  1.00 16.69 ? 387  PHE A O   1 
ATOM   2911  C  CB  . PHE A  1 387 ? 65.806  47.968 25.922  1.00 18.45 ? 387  PHE A CB  1 
ATOM   2912  C  CG  . PHE A  1 387 ? 64.618  47.056 26.125  1.00 17.42 ? 387  PHE A CG  1 
ATOM   2913  C  CD1 . PHE A  1 387 ? 64.031  46.409 25.036  1.00 17.91 ? 387  PHE A CD1 1 
ATOM   2914  C  CD2 . PHE A  1 387 ? 64.022  46.926 27.375  1.00 16.13 ? 387  PHE A CD2 1 
ATOM   2915  C  CE1 . PHE A  1 387 ? 62.851  45.653 25.189  1.00 18.93 ? 387  PHE A CE1 1 
ATOM   2916  C  CE2 . PHE A  1 387 ? 62.846  46.172 27.539  1.00 16.10 ? 387  PHE A CE2 1 
ATOM   2917  C  CZ  . PHE A  1 387 ? 62.263  45.545 26.448  1.00 17.11 ? 387  PHE A CZ  1 
ATOM   2918  N  N   . GLN A  1 388 ? 68.729  48.113 24.722  1.00 20.38 ? 388  GLN A N   1 
ATOM   2919  C  CA  . GLN A  1 388 ? 69.710  48.943 24.008  1.00 21.27 ? 388  GLN A CA  1 
ATOM   2920  C  C   . GLN A  1 388 ? 68.757  49.588 22.987  1.00 21.80 ? 388  GLN A C   1 
ATOM   2921  O  O   . GLN A  1 388 ? 67.948  48.869 22.403  1.00 21.55 ? 388  GLN A O   1 
ATOM   2922  C  CB  . GLN A  1 388 ? 70.689  48.022 23.285  1.00 22.68 ? 388  GLN A CB  1 
ATOM   2923  C  CG  . GLN A  1 388 ? 72.098  47.984 23.801  1.00 23.92 ? 388  GLN A CG  1 
ATOM   2924  C  CD  . GLN A  1 388 ? 72.241  48.327 25.268  1.00 25.00 ? 388  GLN A CD  1 
ATOM   2925  O  OE1 . GLN A  1 388 ? 71.695  47.665 26.155  1.00 27.66 ? 388  GLN A OE1 1 
ATOM   2926  N  NE2 . GLN A  1 388 ? 73.000  49.368 25.532  1.00 26.28 ? 388  GLN A NE2 1 
ATOM   2927  N  N   . ILE A  1 389 ? 68.821  50.898 22.733  1.00 22.22 ? 389  ILE A N   1 
ATOM   2928  C  CA  . ILE A  1 389 ? 67.831  51.466 21.808  1.00 23.93 ? 389  ILE A CA  1 
ATOM   2929  C  C   . ILE A  1 389 ? 67.822  50.922 20.395  1.00 25.44 ? 389  ILE A C   1 
ATOM   2930  O  O   . ILE A  1 389 ? 66.819  51.053 19.700  1.00 25.41 ? 389  ILE A O   1 
ATOM   2931  C  CB  . ILE A  1 389 ? 67.874  53.027 21.691  1.00 23.38 ? 389  ILE A CB  1 
ATOM   2932  C  CG1 . ILE A  1 389 ? 69.173  53.485 21.044  1.00 23.74 ? 389  ILE A CG1 1 
ATOM   2933  C  CG2 . ILE A  1 389 ? 67.624  53.656 23.051  1.00 24.03 ? 389  ILE A CG2 1 
ATOM   2934  C  CD1 . ILE A  1 389 ? 69.263  54.991 20.891  1.00 24.48 ? 389  ILE A CD1 1 
ATOM   2935  N  N   . ASP A  1 390 ? 68.921  50.310 19.972  1.00 26.48 ? 390  ASP A N   1 
ATOM   2936  C  CA  . ASP A  1 390 ? 68.992  49.754 18.632  1.00 28.88 ? 390  ASP A CA  1 
ATOM   2937  C  C   . ASP A  1 390 ? 69.247  48.250 18.686  1.00 29.68 ? 390  ASP A C   1 
ATOM   2938  O  O   . ASP A  1 390 ? 69.952  47.707 17.846  1.00 29.42 ? 390  ASP A O   1 
ATOM   2939  C  CB  . ASP A  1 390 ? 70.113  50.432 17.854  1.00 30.07 ? 390  ASP A CB  1 
ATOM   2940  C  CG  . ASP A  1 390 ? 71.473  50.179 18.475  1.00 31.59 ? 390  ASP A CG  1 
ATOM   2941  O  OD1 . ASP A  1 390 ? 71.524  49.679 19.625  1.00 30.82 ? 390  ASP A OD1 1 
ATOM   2942  O  OD2 . ASP A  1 390 ? 72.483  50.485 17.819  1.00 33.25 ? 390  ASP A OD2 1 
ATOM   2943  N  N   . LYS A  1 391 ? 68.691  47.580 19.688  1.00 29.81 ? 391  LYS A N   1 
ATOM   2944  C  CA  . LYS A  1 391 ? 68.854  46.138 19.811  1.00 30.92 ? 391  LYS A CA  1 
ATOM   2945  C  C   . LYS A  1 391 ? 67.487  45.581 20.133  1.00 31.44 ? 391  LYS A C   1 
ATOM   2946  O  O   . LYS A  1 391 ? 66.776  46.140 20.978  1.00 31.30 ? 391  LYS A O   1 
ATOM   2947  C  CB  . LYS A  1 391 ? 69.837  45.795 20.929  1.00 32.40 ? 391  LYS A CB  1 
ATOM   2948  C  CG  . LYS A  1 391 ? 71.137  45.191 20.436  1.00 34.86 ? 391  LYS A CG  1 
ATOM   2949  C  CD  . LYS A  1 391 ? 71.805  46.075 19.391  1.00 37.01 ? 391  LYS A CD  1 
ATOM   2950  C  CE  . LYS A  1 391 ? 73.029  45.399 18.791  1.00 38.03 ? 391  LYS A CE  1 
ATOM   2951  N  NZ  . LYS A  1 391 ? 73.936  44.902 19.868  1.00 39.40 ? 391  LYS A NZ  1 
ATOM   2952  N  N   . LYS A  1 392 ? 67.115  44.491 19.463  1.00 30.90 ? 392  LYS A N   1 
ATOM   2953  C  CA  . LYS A  1 392 ? 65.799  43.882 19.671  1.00 31.82 ? 392  LYS A CA  1 
ATOM   2954  C  C   . LYS A  1 392 ? 65.636  43.117 20.971  1.00 30.58 ? 392  LYS A C   1 
ATOM   2955  O  O   . LYS A  1 392 ? 64.595  43.199 21.620  1.00 30.95 ? 392  LYS A O   1 
ATOM   2956  C  CB  . LYS A  1 392 ? 65.452  42.926 18.527  1.00 33.61 ? 392  LYS A CB  1 
ATOM   2957  C  CG  . LYS A  1 392 ? 65.323  43.579 17.168  1.00 37.23 ? 392  LYS A CG  1 
ATOM   2958  C  CD  . LYS A  1 392 ? 64.117  44.513 17.093  1.00 40.12 ? 392  LYS A CD  1 
ATOM   2959  C  CE  . LYS A  1 392 ? 63.908  44.991 15.654  1.00 41.51 ? 392  LYS A CE  1 
ATOM   2960  N  NZ  . LYS A  1 392 ? 65.108  45.707 15.116  1.00 41.72 ? 392  LYS A NZ  1 
ATOM   2961  N  N   . ASP A  1 393 ? 66.641  42.338 21.328  1.00 29.47 ? 393  ASP A N   1 
ATOM   2962  C  CA  . ASP A  1 393 ? 66.561  41.556 22.551  1.00 29.33 ? 393  ASP A CA  1 
ATOM   2963  C  C   . ASP A  1 393 ? 66.976  42.387 23.742  1.00 28.05 ? 393  ASP A C   1 
ATOM   2964  O  O   . ASP A  1 393 ? 67.939  43.152 23.670  1.00 28.06 ? 393  ASP A O   1 
ATOM   2965  C  CB  . ASP A  1 393 ? 67.483  40.339 22.500  1.00 31.02 ? 393  ASP A CB  1 
ATOM   2966  C  CG  . ASP A  1 393 ? 67.243  39.469 21.289  1.00 33.75 ? 393  ASP A CG  1 
ATOM   2967  O  OD1 . ASP A  1 393 ? 66.068  39.309 20.862  1.00 32.16 ? 393  ASP A OD1 1 
ATOM   2968  O  OD2 . ASP A  1 393 ? 68.254  38.927 20.777  1.00 35.27 ? 393  ASP A OD2 1 
ATOM   2969  N  N   . CYS A  1 394 ? 66.243  42.223 24.834  1.00 26.61 ? 394  CYS A N   1 
ATOM   2970  C  CA  . CYS A  1 394 ? 66.553  42.918 26.071  1.00 24.74 ? 394  CYS A CA  1 
ATOM   2971  C  C   . CYS A  1 394 ? 67.056  41.843 27.024  1.00 23.43 ? 394  CYS A C   1 
ATOM   2972  O  O   . CYS A  1 394 ? 66.782  40.663 26.821  1.00 23.22 ? 394  CYS A O   1 
ATOM   2973  C  CB  . CYS A  1 394 ? 65.295  43.585 26.649  1.00 24.74 ? 394  CYS A CB  1 
ATOM   2974  S  SG  . CYS A  1 394 ? 63.939  42.471 27.169  1.00 24.20 ? 394  CYS A SG  1 
ATOM   2975  N  N   . THR A  1 395 ? 67.791  42.238 28.055  1.00 22.46 ? 395  THR A N   1 
ATOM   2976  C  CA  . THR A  1 395 ? 68.301  41.277 29.028  1.00 20.86 ? 395  THR A CA  1 
ATOM   2977  C  C   . THR A  1 395 ? 67.585  41.489 30.358  1.00 20.13 ? 395  THR A C   1 
ATOM   2978  O  O   . THR A  1 395 ? 67.520  42.618 30.872  1.00 18.57 ? 395  THR A O   1 
ATOM   2979  C  CB  . THR A  1 395 ? 69.788  41.474 29.275  1.00 22.27 ? 395  THR A CB  1 
ATOM   2980  O  OG1 . THR A  1 395 ? 70.493  41.385 28.029  1.00 23.73 ? 395  THR A OG1 1 
ATOM   2981  C  CG2 . THR A  1 395 ? 70.293  40.411 30.254  1.00 23.48 ? 395  THR A CG2 1 
ATOM   2982  N  N   . PHE A  1 396 ? 67.066  40.406 30.928  1.00 17.63 ? 396  PHE A N   1 
ATOM   2983  C  CA  . PHE A  1 396 ? 66.365  40.500 32.190  1.00 18.26 ? 396  PHE A CA  1 
ATOM   2984  C  C   . PHE A  1 396 ? 67.389  40.704 33.305  1.00 18.60 ? 396  PHE A C   1 
ATOM   2985  O  O   . PHE A  1 396 ? 68.412  40.021 33.348  1.00 19.71 ? 396  PHE A O   1 
ATOM   2986  C  CB  . PHE A  1 396 ? 65.531  39.228 32.425  1.00 18.24 ? 396  PHE A CB  1 
ATOM   2987  C  CG  . PHE A  1 396 ? 64.182  39.261 31.769  1.00 18.76 ? 396  PHE A CG  1 
ATOM   2988  C  CD1 . PHE A  1 396 ? 63.190  40.139 32.217  1.00 18.93 ? 396  PHE A CD1 1 
ATOM   2989  C  CD2 . PHE A  1 396 ? 63.902  38.432 30.691  1.00 19.78 ? 396  PHE A CD2 1 
ATOM   2990  C  CE1 . PHE A  1 396 ? 61.942  40.190 31.598  1.00 17.75 ? 396  PHE A CE1 1 
ATOM   2991  C  CE2 . PHE A  1 396 ? 62.656  38.476 30.061  1.00 19.61 ? 396  PHE A CE2 1 
ATOM   2992  C  CZ  . PHE A  1 396 ? 61.672  39.360 30.516  1.00 19.13 ? 396  PHE A CZ  1 
ATOM   2993  N  N   . ILE A  1 397 ? 67.150  41.650 34.202  1.00 17.74 ? 397  ILE A N   1 
ATOM   2994  C  CA  . ILE A  1 397 ? 68.119  41.855 35.267  1.00 16.70 ? 397  ILE A CA  1 
ATOM   2995  C  C   . ILE A  1 397 ? 67.633  41.351 36.623  1.00 16.28 ? 397  ILE A C   1 
ATOM   2996  O  O   . ILE A  1 397 ? 68.388  41.331 37.596  1.00 14.83 ? 397  ILE A O   1 
ATOM   2997  C  CB  . ILE A  1 397 ? 68.566  43.329 35.352  1.00 16.35 ? 397  ILE A CB  1 
ATOM   2998  C  CG1 . ILE A  1 397 ? 67.462  44.207 35.945  1.00 16.62 ? 397  ILE A CG1 1 
ATOM   2999  C  CG2 . ILE A  1 397 ? 68.933  43.820 33.947  1.00 17.80 ? 397  ILE A CG2 1 
ATOM   3000  C  CD1 . ILE A  1 397 ? 67.942  45.638 36.199  1.00 16.46 ? 397  ILE A CD1 1 
ATOM   3001  N  N   . THR A  1 398 ? 66.367  40.945 36.687  1.00 16.69 ? 398  THR A N   1 
ATOM   3002  C  CA  . THR A  1 398 ? 65.819  40.370 37.909  1.00 16.66 ? 398  THR A CA  1 
ATOM   3003  C  C   . THR A  1 398 ? 65.025  39.163 37.451  1.00 17.93 ? 398  THR A C   1 
ATOM   3004  O  O   . THR A  1 398 ? 64.591  39.096 36.299  1.00 17.15 ? 398  THR A O   1 
ATOM   3005  C  CB  . THR A  1 398 ? 64.864  41.319 38.671  1.00 16.74 ? 398  THR A CB  1 
ATOM   3006  O  OG1 . THR A  1 398 ? 63.750  41.672 37.834  1.00 16.32 ? 398  THR A OG1 1 
ATOM   3007  C  CG2 . THR A  1 398 ? 65.593  42.550 39.124  1.00 15.17 ? 398  THR A CG2 1 
ATOM   3008  N  N   . LYS A  1 399 ? 64.831  38.204 38.347  1.00 18.96 ? 399  LYS A N   1 
ATOM   3009  C  CA  . LYS A  1 399 ? 64.098  37.005 37.978  1.00 20.10 ? 399  LYS A CA  1 
ATOM   3010  C  C   . LYS A  1 399 ? 63.620  36.319 39.243  1.00 19.17 ? 399  LYS A C   1 
ATOM   3011  O  O   . LYS A  1 399 ? 64.122  36.595 40.334  1.00 17.94 ? 399  LYS A O   1 
ATOM   3012  C  CB  . LYS A  1 399 ? 65.009  36.063 37.182  1.00 22.33 ? 399  LYS A CB  1 
ATOM   3013  C  CG  . LYS A  1 399 ? 66.252  35.604 37.948  1.00 25.42 ? 399  LYS A CG  1 
ATOM   3014  C  CD  . LYS A  1 399 ? 67.020  34.505 37.168  1.00 29.19 ? 399  LYS A CD  1 
ATOM   3015  C  CE  . LYS A  1 399 ? 68.354  34.112 37.836  1.00 28.90 ? 399  LYS A CE  1 
ATOM   3016  N  NZ  . LYS A  1 399 ? 68.182  33.587 39.224  1.00 31.90 ? 399  LYS A NZ  1 
ATOM   3017  N  N   . GLY A  1 400 ? 62.637  35.439 39.097  1.00 19.47 ? 400  GLY A N   1 
ATOM   3018  C  CA  . GLY A  1 400 ? 62.107  34.733 40.252  1.00 20.18 ? 400  GLY A CA  1 
ATOM   3019  C  C   . GLY A  1 400 ? 60.587  34.646 40.244  1.00 20.78 ? 400  GLY A C   1 
ATOM   3020  O  O   . GLY A  1 400 ? 59.907  35.306 39.435  1.00 21.42 ? 400  GLY A O   1 
ATOM   3021  N  N   . THR A  1 401 ? 60.043  33.832 41.145  1.00 20.43 ? 401  THR A N   1 
ATOM   3022  C  CA  . THR A  1 401 ? 58.602  33.649 41.210  1.00 20.76 ? 401  THR A CA  1 
ATOM   3023  C  C   . THR A  1 401 ? 57.993  34.727 42.095  1.00 20.82 ? 401  THR A C   1 
ATOM   3024  O  O   . THR A  1 401 ? 57.489  34.461 43.180  1.00 20.92 ? 401  THR A O   1 
ATOM   3025  C  CB  . THR A  1 401 ? 58.244  32.227 41.735  1.00 21.72 ? 401  THR A CB  1 
ATOM   3026  O  OG1 . THR A  1 401 ? 58.897  31.998 42.988  1.00 24.03 ? 401  THR A OG1 1 
ATOM   3027  C  CG2 . THR A  1 401 ? 58.729  31.178 40.766  1.00 21.60 ? 401  THR A CG2 1 
ATOM   3028  N  N   . TRP A  1 402 ? 58.067  35.951 41.594  1.00 19.01 ? 402  TRP A N   1 
ATOM   3029  C  CA  . TRP A  1 402 ? 57.537  37.130 42.247  1.00 18.52 ? 402  TRP A CA  1 
ATOM   3030  C  C   . TRP A  1 402 ? 57.584  38.216 41.166  1.00 17.83 ? 402  TRP A C   1 
ATOM   3031  O  O   . TRP A  1 402 ? 58.056  37.959 40.049  1.00 17.18 ? 402  TRP A O   1 
ATOM   3032  C  CB  . TRP A  1 402 ? 58.387  37.511 43.474  1.00 17.77 ? 402  TRP A CB  1 
ATOM   3033  C  CG  . TRP A  1 402 ? 59.885  37.555 43.232  1.00 17.82 ? 402  TRP A CG  1 
ATOM   3034  C  CD1 . TRP A  1 402 ? 60.780  36.529 43.416  1.00 17.71 ? 402  TRP A CD1 1 
ATOM   3035  C  CD2 . TRP A  1 402 ? 60.658  38.680 42.765  1.00 17.62 ? 402  TRP A CD2 1 
ATOM   3036  N  NE1 . TRP A  1 402 ? 62.052  36.942 43.096  1.00 17.67 ? 402  TRP A NE1 1 
ATOM   3037  C  CE2 . TRP A  1 402 ? 62.014  38.253 42.696  1.00 17.51 ? 402  TRP A CE2 1 
ATOM   3038  C  CE3 . TRP A  1 402 ? 60.341  40.004 42.402  1.00 17.29 ? 402  TRP A CE3 1 
ATOM   3039  C  CZ2 . TRP A  1 402 ? 63.050  39.101 42.279  1.00 17.06 ? 402  TRP A CZ2 1 
ATOM   3040  C  CZ3 . TRP A  1 402 ? 61.377  40.852 41.987  1.00 16.40 ? 402  TRP A CZ3 1 
ATOM   3041  C  CH2 . TRP A  1 402 ? 62.715  40.391 41.931  1.00 17.25 ? 402  TRP A CH2 1 
ATOM   3042  N  N   . GLU A  1 403 ? 57.084  39.411 41.459  1.00 16.53 ? 403  GLU A N   1 
ATOM   3043  C  CA  . GLU A  1 403 ? 57.120  40.442 40.431  1.00 15.23 ? 403  GLU A CA  1 
ATOM   3044  C  C   . GLU A  1 403 ? 57.577  41.823 40.874  1.00 15.52 ? 403  GLU A C   1 
ATOM   3045  O  O   . GLU A  1 403 ? 57.374  42.244 42.017  1.00 15.33 ? 403  GLU A O   1 
ATOM   3046  C  CB  . GLU A  1 403 ? 55.745  40.582 39.764  1.00 13.79 ? 403  GLU A CB  1 
ATOM   3047  C  CG  . GLU A  1 403 ? 55.202  39.289 39.143  1.00 14.50 ? 403  GLU A CG  1 
ATOM   3048  C  CD  . GLU A  1 403 ? 54.041  39.540 38.206  1.00 14.17 ? 403  GLU A CD  1 
ATOM   3049  O  OE1 . GLU A  1 403 ? 53.177  40.385 38.522  1.00 15.74 ? 403  GLU A OE1 1 
ATOM   3050  O  OE2 . GLU A  1 403 ? 53.973  38.886 37.147  1.00 15.94 ? 403  GLU A OE2 1 
ATOM   3051  N  N   . VAL A  1 404 ? 58.190  42.520 39.929  1.00 15.81 ? 404  VAL A N   1 
ATOM   3052  C  CA  . VAL A  1 404 ? 58.627  43.881 40.129  1.00 14.65 ? 404  VAL A CA  1 
ATOM   3053  C  C   . VAL A  1 404 ? 57.337  44.685 39.921  1.00 15.95 ? 404  VAL A C   1 
ATOM   3054  O  O   . VAL A  1 404 ? 56.642  44.513 38.908  1.00 16.12 ? 404  VAL A O   1 
ATOM   3055  C  CB  . VAL A  1 404 ? 59.659  44.255 39.073  1.00 14.87 ? 404  VAL A CB  1 
ATOM   3056  C  CG1 . VAL A  1 404 ? 59.882  45.774 39.077  1.00 14.77 ? 404  VAL A CG1 1 
ATOM   3057  C  CG2 . VAL A  1 404 ? 60.972  43.511 39.361  1.00 12.27 ? 404  VAL A CG2 1 
ATOM   3058  N  N   . ILE A  1 405 ? 56.999  45.538 40.883  1.00 14.67 ? 405  ILE A N   1 
ATOM   3059  C  CA  . ILE A  1 405 ? 55.783  46.341 40.792  1.00 14.73 ? 405  ILE A CA  1 
ATOM   3060  C  C   . ILE A  1 405 ? 56.015  47.608 39.969  1.00 14.64 ? 405  ILE A C   1 
ATOM   3061  O  O   . ILE A  1 405 ? 55.172  48.011 39.160  1.00 14.28 ? 405  ILE A O   1 
ATOM   3062  C  CB  . ILE A  1 405 ? 55.288  46.733 42.193  1.00 14.88 ? 405  ILE A CB  1 
ATOM   3063  C  CG1 . ILE A  1 405 ? 55.114  45.463 43.039  1.00 15.02 ? 405  ILE A CG1 1 
ATOM   3064  C  CG2 . ILE A  1 405 ? 53.964  47.540 42.092  1.00 15.05 ? 405  ILE A CG2 1 
ATOM   3065  C  CD1 . ILE A  1 405 ? 54.095  44.480 42.499  1.00 15.34 ? 405  ILE A CD1 1 
ATOM   3066  N  N   . GLY A  1 406 ? 57.161  48.244 40.171  1.00 14.02 ? 406  GLY A N   1 
ATOM   3067  C  CA  . GLY A  1 406 ? 57.447  49.441 39.405  1.00 13.60 ? 406  GLY A CA  1 
ATOM   3068  C  C   . GLY A  1 406 ? 58.897  49.838 39.546  1.00 13.31 ? 406  GLY A C   1 
ATOM   3069  O  O   . GLY A  1 406 ? 59.542  49.506 40.547  1.00 15.04 ? 406  GLY A O   1 
ATOM   3070  N  N   . ILE A  1 407 ? 59.419  50.504 38.524  1.00 14.04 ? 407  ILE A N   1 
ATOM   3071  C  CA  . ILE A  1 407 ? 60.794  51.014 38.530  1.00 13.82 ? 407  ILE A CA  1 
ATOM   3072  C  C   . ILE A  1 407 ? 60.649  52.436 39.098  1.00 14.53 ? 407  ILE A C   1 
ATOM   3073  O  O   . ILE A  1 407 ? 59.899  53.242 38.541  1.00 13.38 ? 407  ILE A O   1 
ATOM   3074  C  CB  . ILE A  1 407 ? 61.353  51.048 37.097  1.00 12.74 ? 407  ILE A CB  1 
ATOM   3075  C  CG1 . ILE A  1 407 ? 61.619  49.610 36.627  1.00 13.48 ? 407  ILE A CG1 1 
ATOM   3076  C  CG2 . ILE A  1 407 ? 62.619  51.885 37.043  1.00 12.25 ? 407  ILE A CG2 1 
ATOM   3077  C  CD1 . ILE A  1 407 ? 61.864  49.445 35.113  1.00 13.74 ? 407  ILE A CD1 1 
ATOM   3078  N  N   . GLU A  1 408 ? 61.368  52.744 40.180  1.00 13.70 ? 408  GLU A N   1 
ATOM   3079  C  CA  . GLU A  1 408 ? 61.239  54.042 40.857  1.00 13.52 ? 408  GLU A CA  1 
ATOM   3080  C  C   . GLU A  1 408 ? 62.296  55.118 40.620  1.00 14.02 ? 408  GLU A C   1 
ATOM   3081  O  O   . GLU A  1 408 ? 61.998  56.317 40.652  1.00 13.82 ? 408  GLU A O   1 
ATOM   3082  C  CB  . GLU A  1 408 ? 61.129  53.800 42.366  1.00 14.21 ? 408  GLU A CB  1 
ATOM   3083  C  CG  . GLU A  1 408 ? 60.056  52.758 42.745  1.00 15.67 ? 408  GLU A CG  1 
ATOM   3084  C  CD  . GLU A  1 408 ? 58.671  53.217 42.348  1.00 19.87 ? 408  GLU A CD  1 
ATOM   3085  O  OE1 . GLU A  1 408 ? 57.956  52.441 41.677  1.00 21.71 ? 408  GLU A OE1 1 
ATOM   3086  O  OE2 . GLU A  1 408 ? 58.291  54.359 42.701  1.00 19.64 ? 408  GLU A OE2 1 
ATOM   3087  N  N   . ALA A  1 409 ? 63.543  54.708 40.432  1.00 13.75 ? 409  ALA A N   1 
ATOM   3088  C  CA  . ALA A  1 409 ? 64.617  55.668 40.194  1.00 14.41 ? 409  ALA A CA  1 
ATOM   3089  C  C   . ALA A  1 409 ? 65.780  54.932 39.551  1.00 14.35 ? 409  ALA A C   1 
ATOM   3090  O  O   . ALA A  1 409 ? 65.930  53.717 39.718  1.00 13.62 ? 409  ALA A O   1 
ATOM   3091  C  CB  . ALA A  1 409 ? 65.049  56.325 41.523  1.00 14.42 ? 409  ALA A CB  1 
ATOM   3092  N  N   . LEU A  1 410 ? 66.595  55.683 38.825  1.00 14.74 ? 410  LEU A N   1 
ATOM   3093  C  CA  . LEU A  1 410 ? 67.725  55.124 38.116  1.00 15.74 ? 410  LEU A CA  1 
ATOM   3094  C  C   . LEU A  1 410 ? 68.938  56.064 38.179  1.00 15.79 ? 410  LEU A C   1 
ATOM   3095  O  O   . LEU A  1 410 ? 68.806  57.265 37.942  1.00 15.42 ? 410  LEU A O   1 
ATOM   3096  C  CB  . LEU A  1 410 ? 67.337  54.892 36.638  1.00 15.07 ? 410  LEU A CB  1 
ATOM   3097  C  CG  . LEU A  1 410 ? 68.425  54.337 35.692  1.00 17.26 ? 410  LEU A CG  1 
ATOM   3098  C  CD1 . LEU A  1 410 ? 68.793  52.925 36.112  1.00 15.11 ? 410  LEU A CD1 1 
ATOM   3099  C  CD2 . LEU A  1 410 ? 67.942  54.336 34.234  1.00 15.46 ? 410  LEU A CD2 1 
ATOM   3100  N  N   . THR A  1 411 ? 70.101  55.513 38.519  1.00 15.78 ? 411  THR A N   1 
ATOM   3101  C  CA  . THR A  1 411 ? 71.358  56.272 38.526  1.00 17.59 ? 411  THR A CA  1 
ATOM   3102  C  C   . THR A  1 411 ? 72.329  55.415 37.718  1.00 18.07 ? 411  THR A C   1 
ATOM   3103  O  O   . THR A  1 411 ? 71.987  54.292 37.323  1.00 16.67 ? 411  THR A O   1 
ATOM   3104  C  CB  . THR A  1 411 ? 71.971  56.434 39.930  1.00 17.53 ? 411  THR A CB  1 
ATOM   3105  O  OG1 . THR A  1 411 ? 72.444  55.160 40.385  1.00 18.15 ? 411  THR A OG1 1 
ATOM   3106  C  CG2 . THR A  1 411 ? 70.951  56.987 40.892  1.00 17.99 ? 411  THR A CG2 1 
ATOM   3107  N  N   . SER A  1 412 ? 73.542  55.918 37.492  1.00 18.64 ? 412  SER A N   1 
ATOM   3108  C  CA  . SER A  1 412 ? 74.513  55.158 36.710  1.00 18.56 ? 412  SER A CA  1 
ATOM   3109  C  C   . SER A  1 412 ? 74.905  53.895 37.439  1.00 18.87 ? 412  SER A C   1 
ATOM   3110  O  O   . SER A  1 412 ? 75.359  52.930 36.819  1.00 20.30 ? 412  SER A O   1 
ATOM   3111  C  CB  . SER A  1 412 ? 75.773  55.999 36.429  1.00 19.30 ? 412  SER A CB  1 
ATOM   3112  O  OG  . SER A  1 412 ? 76.443  56.337 37.634  1.00 18.72 ? 412  SER A OG  1 
ATOM   3113  N  N   . ASP A  1 413 ? 74.743  53.892 38.760  1.00 18.78 ? 413  ASP A N   1 
ATOM   3114  C  CA  . ASP A  1 413 ? 75.124  52.723 39.545  1.00 18.86 ? 413  ASP A CA  1 
ATOM   3115  C  C   . ASP A  1 413 ? 74.005  51.773 39.988  1.00 18.64 ? 413  ASP A C   1 
ATOM   3116  O  O   . ASP A  1 413 ? 74.225  50.563 40.104  1.00 18.96 ? 413  ASP A O   1 
ATOM   3117  C  CB  . ASP A  1 413 ? 75.911  53.163 40.781  1.00 20.33 ? 413  ASP A CB  1 
ATOM   3118  C  CG  . ASP A  1 413 ? 77.250  53.819 40.421  1.00 22.53 ? 413  ASP A CG  1 
ATOM   3119  O  OD1 . ASP A  1 413 ? 77.885  53.388 39.429  1.00 24.68 ? 413  ASP A OD1 1 
ATOM   3120  O  OD2 . ASP A  1 413 ? 77.661  54.748 41.134  1.00 22.06 ? 413  ASP A OD2 1 
ATOM   3121  N  N   . TYR A  1 414 ? 72.815  52.305 40.231  1.00 17.48 ? 414  TYR A N   1 
ATOM   3122  C  CA  . TYR A  1 414 ? 71.723  51.463 40.704  1.00 17.08 ? 414  TYR A CA  1 
ATOM   3123  C  C   . TYR A  1 414 ? 70.382  51.774 40.051  1.00 15.87 ? 414  TYR A C   1 
ATOM   3124  O  O   . TYR A  1 414 ? 70.150  52.904 39.619  1.00 15.05 ? 414  TYR A O   1 
ATOM   3125  C  CB  . TYR A  1 414 ? 71.536  51.650 42.222  1.00 16.30 ? 414  TYR A CB  1 
ATOM   3126  C  CG  . TYR A  1 414 ? 72.666  51.136 43.096  1.00 18.55 ? 414  TYR A CG  1 
ATOM   3127  C  CD1 . TYR A  1 414 ? 73.670  51.989 43.568  1.00 18.68 ? 414  TYR A CD1 1 
ATOM   3128  C  CD2 . TYR A  1 414 ? 72.719  49.797 43.456  1.00 17.54 ? 414  TYR A CD2 1 
ATOM   3129  C  CE1 . TYR A  1 414 ? 74.700  51.504 44.385  1.00 20.63 ? 414  TYR A CE1 1 
ATOM   3130  C  CE2 . TYR A  1 414 ? 73.731  49.304 44.258  1.00 19.96 ? 414  TYR A CE2 1 
ATOM   3131  C  CZ  . TYR A  1 414 ? 74.718  50.161 44.719  1.00 20.60 ? 414  TYR A CZ  1 
ATOM   3132  O  OH  . TYR A  1 414 ? 75.718  49.649 45.495  1.00 22.44 ? 414  TYR A OH  1 
ATOM   3133  N  N   . LEU A  1 415 ? 69.519  50.760 39.992  1.00 15.20 ? 415  LEU A N   1 
ATOM   3134  C  CA  . LEU A  1 415 ? 68.151  50.914 39.523  1.00 14.91 ? 415  LEU A CA  1 
ATOM   3135  C  C   . LEU A  1 415 ? 67.353  50.583 40.805  1.00 15.42 ? 415  LEU A C   1 
ATOM   3136  O  O   . LEU A  1 415 ? 67.596  49.559 41.457  1.00 14.25 ? 415  LEU A O   1 
ATOM   3137  C  CB  . LEU A  1 415 ? 67.791  49.923 38.407  1.00 14.87 ? 415  LEU A CB  1 
ATOM   3138  C  CG  . LEU A  1 415 ? 66.358  50.138 37.854  1.00 15.39 ? 415  LEU A CG  1 
ATOM   3139  C  CD1 . LEU A  1 415 ? 66.314  49.780 36.395  1.00 14.30 ? 415  LEU A CD1 1 
ATOM   3140  C  CD2 . LEU A  1 415 ? 65.327  49.328 38.664  1.00 13.53 ? 415  LEU A CD2 1 
ATOM   3141  N  N   . TYR A  1 416 ? 66.453  51.476 41.199  1.00 15.16 ? 416  TYR A N   1 
ATOM   3142  C  CA  . TYR A  1 416 ? 65.652  51.255 42.408  1.00 14.44 ? 416  TYR A CA  1 
ATOM   3143  C  C   . TYR A  1 416 ? 64.255  50.816 42.008  1.00 14.88 ? 416  TYR A C   1 
ATOM   3144  O  O   . TYR A  1 416 ? 63.670  51.387 41.080  1.00 14.86 ? 416  TYR A O   1 
ATOM   3145  C  CB  . TYR A  1 416 ? 65.546  52.539 43.230  1.00 14.28 ? 416  TYR A CB  1 
ATOM   3146  C  CG  . TYR A  1 416 ? 66.858  53.007 43.818  1.00 15.24 ? 416  TYR A CG  1 
ATOM   3147  C  CD1 . TYR A  1 416 ? 67.744  53.776 43.058  1.00 16.14 ? 416  TYR A CD1 1 
ATOM   3148  C  CD2 . TYR A  1 416 ? 67.221  52.673 45.123  1.00 14.87 ? 416  TYR A CD2 1 
ATOM   3149  C  CE1 . TYR A  1 416 ? 68.966  54.209 43.577  1.00 15.90 ? 416  TYR A CE1 1 
ATOM   3150  C  CE2 . TYR A  1 416 ? 68.443  53.098 45.667  1.00 15.54 ? 416  TYR A CE2 1 
ATOM   3151  C  CZ  . TYR A  1 416 ? 69.308  53.867 44.879  1.00 16.61 ? 416  TYR A CZ  1 
ATOM   3152  O  OH  . TYR A  1 416 ? 70.508  54.291 45.364  1.00 16.57 ? 416  TYR A OH  1 
ATOM   3153  N  N   . TYR A  1 417 ? 63.705  49.821 42.700  1.00 13.76 ? 417  TYR A N   1 
ATOM   3154  C  CA  . TYR A  1 417 ? 62.367  49.358 42.358  1.00 13.94 ? 417  TYR A CA  1 
ATOM   3155  C  C   . TYR A  1 417 ? 61.617  48.750 43.535  1.00 13.67 ? 417  TYR A C   1 
ATOM   3156  O  O   . TYR A  1 417 ? 62.200  48.424 44.563  1.00 12.86 ? 417  TYR A O   1 
ATOM   3157  C  CB  . TYR A  1 417 ? 62.433  48.336 41.217  1.00 13.80 ? 417  TYR A CB  1 
ATOM   3158  C  CG  . TYR A  1 417 ? 63.079  47.031 41.616  1.00 14.75 ? 417  TYR A CG  1 
ATOM   3159  C  CD1 . TYR A  1 417 ? 62.324  45.983 42.170  1.00 15.04 ? 417  TYR A CD1 1 
ATOM   3160  C  CD2 . TYR A  1 417 ? 64.459  46.852 41.482  1.00 14.09 ? 417  TYR A CD2 1 
ATOM   3161  C  CE1 . TYR A  1 417 ? 62.948  44.780 42.588  1.00 14.26 ? 417  TYR A CE1 1 
ATOM   3162  C  CE2 . TYR A  1 417 ? 65.086  45.662 41.896  1.00 15.30 ? 417  TYR A CE2 1 
ATOM   3163  C  CZ  . TYR A  1 417 ? 64.324  44.640 42.450  1.00 15.51 ? 417  TYR A CZ  1 
ATOM   3164  O  OH  . TYR A  1 417 ? 64.958  43.519 42.925  1.00 15.45 ? 417  TYR A OH  1 
ATOM   3165  N  N   . ILE A  1 418 ? 60.312  48.610 43.368  1.00 13.36 ? 418  ILE A N   1 
ATOM   3166  C  CA  . ILE A  1 418 ? 59.469  48.031 44.401  1.00 13.64 ? 418  ILE A CA  1 
ATOM   3167  C  C   . ILE A  1 418 ? 59.024  46.660 43.853  1.00 14.05 ? 418  ILE A C   1 
ATOM   3168  O  O   . ILE A  1 418 ? 58.699  46.539 42.663  1.00 12.90 ? 418  ILE A O   1 
ATOM   3169  C  CB  . ILE A  1 418 ? 58.258  48.966 44.670  1.00 14.65 ? 418  ILE A CB  1 
ATOM   3170  C  CG1 . ILE A  1 418 ? 58.721  50.149 45.534  1.00 15.07 ? 418  ILE A CG1 1 
ATOM   3171  C  CG2 . ILE A  1 418 ? 57.131  48.208 45.380  1.00 13.58 ? 418  ILE A CG2 1 
ATOM   3172  C  CD1 . ILE A  1 418 ? 57.714  51.216 45.667  1.00 19.75 ? 418  ILE A CD1 1 
ATOM   3173  N  N   . SER A  1 419 ? 59.054  45.630 44.697  1.00 12.53 ? 419  SER A N   1 
ATOM   3174  C  CA  . SER A  1 419 ? 58.642  44.281 44.290  1.00 13.24 ? 419  SER A CA  1 
ATOM   3175  C  C   . SER A  1 419 ? 57.989  43.594 45.471  1.00 13.75 ? 419  SER A C   1 
ATOM   3176  O  O   . SER A  1 419 ? 58.057  44.091 46.595  1.00 12.21 ? 419  SER A O   1 
ATOM   3177  C  CB  . SER A  1 419 ? 59.842  43.431 43.881  1.00 13.42 ? 419  SER A CB  1 
ATOM   3178  O  OG  . SER A  1 419 ? 60.469  42.902 45.051  1.00 12.92 ? 419  SER A OG  1 
ATOM   3179  N  N   . ASN A  1 420 ? 57.356  42.448 45.219  1.00 14.01 ? 420  ASN A N   1 
ATOM   3180  C  CA  . ASN A  1 420 ? 56.734  41.699 46.302  1.00 15.62 ? 420  ASN A CA  1 
ATOM   3181  C  C   . ASN A  1 420 ? 57.548  40.440 46.565  1.00 15.51 ? 420  ASN A C   1 
ATOM   3182  O  O   . ASN A  1 420 ? 56.993  39.404 46.922  1.00 15.80 ? 420  ASN A O   1 
ATOM   3183  C  CB  . ASN A  1 420 ? 55.273  41.324 45.975  1.00 15.43 ? 420  ASN A CB  1 
ATOM   3184  C  CG  . ASN A  1 420 ? 55.113  40.634 44.617  1.00 15.42 ? 420  ASN A CG  1 
ATOM   3185  O  OD1 . ASN A  1 420 ? 56.070  40.132 44.030  1.00 14.49 ? 420  ASN A OD1 1 
ATOM   3186  N  ND2 . ASN A  1 420 ? 53.878  40.598 44.128  1.00 14.88 ? 420  ASN A ND2 1 
ATOM   3187  N  N   . GLU A  1 421 ? 58.865  40.530 46.389  1.00 15.80 ? 421  GLU A N   1 
ATOM   3188  C  CA  . GLU A  1 421 ? 59.726  39.375 46.606  1.00 17.24 ? 421  GLU A CA  1 
ATOM   3189  C  C   . GLU A  1 421 ? 59.867  38.958 48.068  1.00 18.22 ? 421  GLU A C   1 
ATOM   3190  O  O   . GLU A  1 421 ? 59.926  37.770 48.370  1.00 18.27 ? 421  GLU A O   1 
ATOM   3191  C  CB  . GLU A  1 421 ? 61.140  39.616 46.044  1.00 17.72 ? 421  GLU A CB  1 
ATOM   3192  C  CG  . GLU A  1 421 ? 62.116  38.486 46.416  1.00 18.50 ? 421  GLU A CG  1 
ATOM   3193  C  CD  . GLU A  1 421 ? 63.525  38.666 45.873  1.00 19.96 ? 421  GLU A CD  1 
ATOM   3194  O  OE1 . GLU A  1 421 ? 63.862  39.754 45.347  1.00 19.06 ? 421  GLU A OE1 1 
ATOM   3195  O  OE2 . GLU A  1 421 ? 64.313  37.699 45.983  1.00 21.21 ? 421  GLU A OE2 1 
ATOM   3196  N  N   . TYR A  1 422 ? 59.923  39.921 48.978  1.00 18.47 ? 422  TYR A N   1 
ATOM   3197  C  CA  . TYR A  1 422 ? 60.125  39.581 50.377  1.00 19.70 ? 422  TYR A CA  1 
ATOM   3198  C  C   . TYR A  1 422 ? 59.185  38.524 50.960  1.00 19.72 ? 422  TYR A C   1 
ATOM   3199  O  O   . TYR A  1 422 ? 57.970  38.675 50.929  1.00 19.55 ? 422  TYR A O   1 
ATOM   3200  C  CB  . TYR A  1 422 ? 60.047  40.829 51.238  1.00 18.90 ? 422  TYR A CB  1 
ATOM   3201  C  CG  . TYR A  1 422 ? 60.588  40.594 52.623  1.00 20.78 ? 422  TYR A CG  1 
ATOM   3202  C  CD1 . TYR A  1 422 ? 61.897  40.160 52.806  1.00 21.21 ? 422  TYR A CD1 1 
ATOM   3203  C  CD2 . TYR A  1 422 ? 59.813  40.859 53.755  1.00 22.45 ? 422  TYR A CD2 1 
ATOM   3204  C  CE1 . TYR A  1 422 ? 62.434  40.001 54.077  1.00 22.85 ? 422  TYR A CE1 1 
ATOM   3205  C  CE2 . TYR A  1 422 ? 60.343  40.705 55.043  1.00 24.28 ? 422  TYR A CE2 1 
ATOM   3206  C  CZ  . TYR A  1 422 ? 61.660  40.278 55.186  1.00 23.95 ? 422  TYR A CZ  1 
ATOM   3207  O  OH  . TYR A  1 422 ? 62.214  40.159 56.439  1.00 26.91 ? 422  TYR A OH  1 
ATOM   3208  N  N   . LYS A  1 423 ? 59.768  37.471 51.512  1.00 20.42 ? 423  LYS A N   1 
ATOM   3209  C  CA  . LYS A  1 423 ? 59.014  36.385 52.115  1.00 22.82 ? 423  LYS A CA  1 
ATOM   3210  C  C   . LYS A  1 423 ? 57.977  35.770 51.182  1.00 22.89 ? 423  LYS A C   1 
ATOM   3211  O  O   . LYS A  1 423 ? 57.036  35.115 51.633  1.00 23.13 ? 423  LYS A O   1 
ATOM   3212  C  CB  . LYS A  1 423 ? 58.342  36.874 53.405  1.00 24.62 ? 423  LYS A CB  1 
ATOM   3213  C  CG  . LYS A  1 423 ? 59.339  37.166 54.519  1.00 27.91 ? 423  LYS A CG  1 
ATOM   3214  C  CD  . LYS A  1 423 ? 58.660  37.576 55.831  1.00 31.34 ? 423  LYS A CD  1 
ATOM   3215  C  CE  . LYS A  1 423 ? 59.702  37.736 56.955  1.00 34.23 ? 423  LYS A CE  1 
ATOM   3216  N  NZ  . LYS A  1 423 ? 59.256  38.710 58.025  1.00 35.91 ? 423  LYS A NZ  1 
ATOM   3217  N  N   . GLY A  1 424 ? 58.146  35.970 49.878  1.00 22.47 ? 424  GLY A N   1 
ATOM   3218  C  CA  . GLY A  1 424 ? 57.189  35.414 48.936  1.00 21.50 ? 424  GLY A CA  1 
ATOM   3219  C  C   . GLY A  1 424 ? 55.748  35.866 49.163  1.00 20.79 ? 424  GLY A C   1 
ATOM   3220  O  O   . GLY A  1 424 ? 54.809  35.145 48.820  1.00 20.70 ? 424  GLY A O   1 
ATOM   3221  N  N   . MET A  1 425 ? 55.557  37.051 49.736  1.00 20.03 ? 425  MET A N   1 
ATOM   3222  C  CA  . MET A  1 425 ? 54.204  37.571 49.977  1.00 19.40 ? 425  MET A CA  1 
ATOM   3223  C  C   . MET A  1 425 ? 53.792  38.514 48.834  1.00 18.36 ? 425  MET A C   1 
ATOM   3224  O  O   . MET A  1 425 ? 54.251  39.659 48.763  1.00 16.27 ? 425  MET A O   1 
ATOM   3225  C  CB  . MET A  1 425 ? 54.154  38.305 51.322  1.00 20.41 ? 425  MET A CB  1 
ATOM   3226  C  CG  . MET A  1 425 ? 54.463  37.383 52.520  1.00 25.19 ? 425  MET A CG  1 
ATOM   3227  S  SD  . MET A  1 425 ? 54.411  38.215 54.127  1.00 28.27 ? 425  MET A SD  1 
ATOM   3228  C  CE  . MET A  1 425 ? 52.709  38.842 54.128  1.00 27.01 ? 425  MET A CE  1 
ATOM   3229  N  N   . PRO A  1 426 ? 52.908  38.043 47.933  1.00 18.16 ? 426  PRO A N   1 
ATOM   3230  C  CA  . PRO A  1 426 ? 52.473  38.874 46.803  1.00 17.48 ? 426  PRO A CA  1 
ATOM   3231  C  C   . PRO A  1 426 ? 51.741  40.145 47.206  1.00 18.04 ? 426  PRO A C   1 
ATOM   3232  O  O   . PRO A  1 426 ? 51.670  41.104 46.424  1.00 17.79 ? 426  PRO A O   1 
ATOM   3233  C  CB  . PRO A  1 426 ? 51.619  37.918 45.965  1.00 17.58 ? 426  PRO A CB  1 
ATOM   3234  C  CG  . PRO A  1 426 ? 51.087  36.945 46.982  1.00 18.75 ? 426  PRO A CG  1 
ATOM   3235  C  CD  . PRO A  1 426 ? 52.206  36.742 47.958  1.00 17.56 ? 426  PRO A CD  1 
ATOM   3236  N  N   . GLY A  1 427 ? 51.216  40.151 48.428  1.00 17.06 ? 427  GLY A N   1 
ATOM   3237  C  CA  . GLY A  1 427 ? 50.508  41.312 48.940  1.00 16.49 ? 427  GLY A CA  1 
ATOM   3238  C  C   . GLY A  1 427 ? 51.373  42.260 49.778  1.00 16.36 ? 427  GLY A C   1 
ATOM   3239  O  O   . GLY A  1 427 ? 50.841  43.166 50.427  1.00 16.25 ? 427  GLY A O   1 
ATOM   3240  N  N   . GLY A  1 428 ? 52.690  42.036 49.787  1.00 16.52 ? 428  GLY A N   1 
ATOM   3241  C  CA  . GLY A  1 428 ? 53.627  42.906 50.501  1.00 16.49 ? 428  GLY A CA  1 
ATOM   3242  C  C   . GLY A  1 428 ? 54.458  43.661 49.457  1.00 16.58 ? 428  GLY A C   1 
ATOM   3243  O  O   . GLY A  1 428 ? 54.588  43.178 48.330  1.00 16.60 ? 428  GLY A O   1 
ATOM   3244  N  N   . ARG A  1 429 ? 54.996  44.837 49.794  1.00 15.76 ? 429  ARG A N   1 
ATOM   3245  C  CA  . ARG A  1 429 ? 55.789  45.635 48.831  1.00 14.53 ? 429  ARG A CA  1 
ATOM   3246  C  C   . ARG A  1 429 ? 57.016  46.215 49.540  1.00 14.04 ? 429  ARG A C   1 
ATOM   3247  O  O   . ARG A  1 429 ? 56.883  46.794 50.606  1.00 12.89 ? 429  ARG A O   1 
ATOM   3248  C  CB  . ARG A  1 429 ? 54.987  46.844 48.308  1.00 15.00 ? 429  ARG A CB  1 
ATOM   3249  C  CG  . ARG A  1 429 ? 53.610  46.579 47.671  1.00 17.64 ? 429  ARG A CG  1 
ATOM   3250  C  CD  . ARG A  1 429 ? 53.744  46.301 46.178  1.00 19.46 ? 429  ARG A CD  1 
ATOM   3251  N  NE  . ARG A  1 429 ? 52.461  46.197 45.480  1.00 20.90 ? 429  ARG A NE  1 
ATOM   3252  C  CZ  . ARG A  1 429 ? 51.645  45.140 45.534  1.00 23.97 ? 429  ARG A CZ  1 
ATOM   3253  N  NH1 . ARG A  1 429 ? 51.954  44.071 46.265  1.00 21.03 ? 429  ARG A NH1 1 
ATOM   3254  N  NH2 . ARG A  1 429 ? 50.523  45.146 44.823  1.00 23.43 ? 429  ARG A NH2 1 
ATOM   3255  N  N   . ASN A  1 430 ? 58.189  46.080 48.934  1.00 13.91 ? 430  ASN A N   1 
ATOM   3256  C  CA  . ASN A  1 430 ? 59.412  46.626 49.497  1.00 14.03 ? 430  ASN A CA  1 
ATOM   3257  C  C   . ASN A  1 430 ? 60.280  47.268 48.433  1.00 13.99 ? 430  ASN A C   1 
ATOM   3258  O  O   . ASN A  1 430 ? 60.191  46.908 47.261  1.00 13.09 ? 430  ASN A O   1 
ATOM   3259  C  CB  . ASN A  1 430 ? 60.210  45.538 50.202  1.00 14.08 ? 430  ASN A CB  1 
ATOM   3260  C  CG  . ASN A  1 430 ? 59.674  45.258 51.569  1.00 14.42 ? 430  ASN A CG  1 
ATOM   3261  O  OD1 . ASN A  1 430 ? 59.844  46.063 52.481  1.00 15.48 ? 430  ASN A OD1 1 
ATOM   3262  N  ND2 . ASN A  1 430 ? 58.985  44.135 51.716  1.00 12.34 ? 430  ASN A ND2 1 
ATOM   3263  N  N   . LEU A  1 431 ? 61.117  48.214 48.861  1.00 14.65 ? 431  LEU A N   1 
ATOM   3264  C  CA  . LEU A  1 431 ? 62.038  48.931 47.974  1.00 14.85 ? 431  LEU A CA  1 
ATOM   3265  C  C   . LEU A  1 431 ? 63.349  48.162 47.917  1.00 15.97 ? 431  LEU A C   1 
ATOM   3266  O  O   . LEU A  1 431 ? 63.886  47.741 48.962  1.00 15.88 ? 431  LEU A O   1 
ATOM   3267  C  CB  . LEU A  1 431 ? 62.320  50.348 48.507  1.00 13.88 ? 431  LEU A CB  1 
ATOM   3268  C  CG  . LEU A  1 431 ? 63.372  51.180 47.744  1.00 14.38 ? 431  LEU A CG  1 
ATOM   3269  C  CD1 . LEU A  1 431 ? 62.836  51.520 46.337  1.00 12.33 ? 431  LEU A CD1 1 
ATOM   3270  C  CD2 . LEU A  1 431 ? 63.666  52.470 48.514  1.00 13.13 ? 431  LEU A CD2 1 
ATOM   3271  N  N   . TYR A  1 432 ? 63.863  47.993 46.699  1.00 16.02 ? 432  TYR A N   1 
ATOM   3272  C  CA  . TYR A  1 432 ? 65.130  47.289 46.471  1.00 15.66 ? 432  TYR A CA  1 
ATOM   3273  C  C   . TYR A  1 432 ? 66.000  48.108 45.530  1.00 15.60 ? 432  TYR A C   1 
ATOM   3274  O  O   . TYR A  1 432 ? 65.508  48.977 44.805  1.00 15.57 ? 432  TYR A O   1 
ATOM   3275  C  CB  . TYR A  1 432 ? 64.916  45.922 45.785  1.00 15.35 ? 432  TYR A CB  1 
ATOM   3276  C  CG  . TYR A  1 432 ? 64.184  44.871 46.589  1.00 15.50 ? 432  TYR A CG  1 
ATOM   3277  C  CD1 . TYR A  1 432 ? 62.802  44.908 46.734  1.00 14.74 ? 432  TYR A CD1 1 
ATOM   3278  C  CD2 . TYR A  1 432 ? 64.887  43.833 47.222  1.00 16.67 ? 432  TYR A CD2 1 
ATOM   3279  C  CE1 . TYR A  1 432 ? 62.129  43.930 47.495  1.00 16.38 ? 432  TYR A CE1 1 
ATOM   3280  C  CE2 . TYR A  1 432 ? 64.230  42.855 47.977  1.00 15.66 ? 432  TYR A CE2 1 
ATOM   3281  C  CZ  . TYR A  1 432 ? 62.841  42.915 48.111  1.00 16.67 ? 432  TYR A CZ  1 
ATOM   3282  O  OH  . TYR A  1 432 ? 62.185  41.963 48.865  1.00 16.74 ? 432  TYR A OH  1 
ATOM   3283  N  N   . LYS A  1 433 ? 67.295  47.844 45.533  1.00 14.43 ? 433  LYS A N   1 
ATOM   3284  C  CA  . LYS A  1 433 ? 68.150  48.516 44.567  1.00 14.64 ? 433  LYS A CA  1 
ATOM   3285  C  C   . LYS A  1 433 ? 69.001  47.397 43.995  1.00 15.84 ? 433  LYS A C   1 
ATOM   3286  O  O   . LYS A  1 433 ? 69.370  46.458 44.717  1.00 15.51 ? 433  LYS A O   1 
ATOM   3287  C  CB  . LYS A  1 433 ? 69.022  49.621 45.206  1.00 15.13 ? 433  LYS A CB  1 
ATOM   3288  C  CG  . LYS A  1 433 ? 70.175  49.164 46.107  1.00 14.08 ? 433  LYS A CG  1 
ATOM   3289  C  CD  . LYS A  1 433 ? 70.990  50.383 46.576  1.00 14.49 ? 433  LYS A CD  1 
ATOM   3290  C  CE  . LYS A  1 433 ? 72.181  49.979 47.504  1.00 14.58 ? 433  LYS A CE  1 
ATOM   3291  N  NZ  . LYS A  1 433 ? 72.799  51.204 48.121  1.00 14.31 ? 433  LYS A NZ  1 
ATOM   3292  N  N   . ILE A  1 434 ? 69.250  47.443 42.689  1.00 16.36 ? 434  ILE A N   1 
ATOM   3293  C  CA  . ILE A  1 434 ? 70.075  46.423 42.068  1.00 17.59 ? 434  ILE A CA  1 
ATOM   3294  C  C   . ILE A  1 434 ? 71.290  47.118 41.446  1.00 18.96 ? 434  ILE A C   1 
ATOM   3295  O  O   . ILE A  1 434 ? 71.156  48.163 40.784  1.00 18.88 ? 434  ILE A O   1 
ATOM   3296  C  CB  . ILE A  1 434 ? 69.280  45.598 40.995  1.00 16.84 ? 434  ILE A CB  1 
ATOM   3297  C  CG1 . ILE A  1 434 ? 70.218  44.599 40.300  1.00 17.49 ? 434  ILE A CG1 1 
ATOM   3298  C  CG2 . ILE A  1 434 ? 68.630  46.502 39.960  1.00 16.23 ? 434  ILE A CG2 1 
ATOM   3299  C  CD1 . ILE A  1 434 ? 69.500  43.627 39.350  1.00 15.87 ? 434  ILE A CD1 1 
ATOM   3300  N  N   . GLN A  1 435 ? 72.468  46.552 41.689  1.00 18.17 ? 435  GLN A N   1 
ATOM   3301  C  CA  . GLN A  1 435 ? 73.710  47.112 41.175  1.00 18.76 ? 435  GLN A CA  1 
ATOM   3302  C  C   . GLN A  1 435 ? 73.781  46.831 39.691  1.00 18.55 ? 435  GLN A C   1 
ATOM   3303  O  O   . GLN A  1 435 ? 73.826  45.673 39.271  1.00 18.87 ? 435  GLN A O   1 
ATOM   3304  C  CB  . GLN A  1 435 ? 74.930  46.500 41.890  1.00 19.75 ? 435  GLN A CB  1 
ATOM   3305  C  CG  . GLN A  1 435 ? 76.254  47.245 41.618  1.00 21.46 ? 435  GLN A CG  1 
ATOM   3306  C  CD  . GLN A  1 435 ? 77.455  46.633 42.346  1.00 25.34 ? 435  GLN A CD  1 
ATOM   3307  O  OE1 . GLN A  1 435 ? 78.583  46.664 41.837  1.00 27.05 ? 435  GLN A OE1 1 
ATOM   3308  N  NE2 . GLN A  1 435 ? 77.220  46.087 43.543  1.00 23.83 ? 435  GLN A NE2 1 
ATOM   3309  N  N   . LEU A  1 436 ? 73.791  47.895 38.895  1.00 19.01 ? 436  LEU A N   1 
ATOM   3310  C  CA  . LEU A  1 436 ? 73.817  47.754 37.450  1.00 20.59 ? 436  LEU A CA  1 
ATOM   3311  C  C   . LEU A  1 436 ? 75.066  47.054 36.914  1.00 22.29 ? 436  LEU A C   1 
ATOM   3312  O  O   . LEU A  1 436 ? 75.014  46.427 35.861  1.00 23.30 ? 436  LEU A O   1 
ATOM   3313  C  CB  . LEU A  1 436 ? 73.625  49.131 36.800  1.00 19.48 ? 436  LEU A CB  1 
ATOM   3314  C  CG  . LEU A  1 436 ? 72.287  49.746 37.271  1.00 19.30 ? 436  LEU A CG  1 
ATOM   3315  C  CD1 . LEU A  1 436 ? 72.061  51.105 36.610  1.00 18.07 ? 436  LEU A CD1 1 
ATOM   3316  C  CD2 . LEU A  1 436 ? 71.147  48.762 36.957  1.00 18.34 ? 436  LEU A CD2 1 
ATOM   3317  N  N   . SER A  1 437 ? 76.181  47.150 37.629  1.00 23.41 ? 437  SER A N   1 
ATOM   3318  C  CA  . SER A  1 437 ? 77.410  46.486 37.180  1.00 25.49 ? 437  SER A CA  1 
ATOM   3319  C  C   . SER A  1 437 ? 77.435  45.002 37.590  1.00 26.12 ? 437  SER A C   1 
ATOM   3320  O  O   . SER A  1 437 ? 78.249  44.233 37.087  1.00 26.26 ? 437  SER A O   1 
ATOM   3321  C  CB  . SER A  1 437 ? 78.640  47.192 37.759  1.00 26.04 ? 437  SER A CB  1 
ATOM   3322  O  OG  . SER A  1 437 ? 78.789  46.894 39.140  1.00 27.31 ? 437  SER A OG  1 
ATOM   3323  N  N   . ASP A  1 438 ? 76.554  44.601 38.505  1.00 25.84 ? 438  ASP A N   1 
ATOM   3324  C  CA  . ASP A  1 438 ? 76.513  43.204 38.944  1.00 26.36 ? 438  ASP A CA  1 
ATOM   3325  C  C   . ASP A  1 438 ? 75.118  42.853 39.435  1.00 25.33 ? 438  ASP A C   1 
ATOM   3326  O  O   . ASP A  1 438 ? 74.788  43.052 40.611  1.00 25.77 ? 438  ASP A O   1 
ATOM   3327  C  CB  . ASP A  1 438 ? 77.541  42.954 40.067  1.00 26.94 ? 438  ASP A CB  1 
ATOM   3328  C  CG  . ASP A  1 438 ? 77.633  41.475 40.465  1.00 27.17 ? 438  ASP A CG  1 
ATOM   3329  O  OD1 . ASP A  1 438 ? 76.776  40.683 40.043  1.00 28.12 ? 438  ASP A OD1 1 
ATOM   3330  O  OD2 . ASP A  1 438 ? 78.563  41.109 41.212  1.00 29.24 ? 438  ASP A OD2 1 
ATOM   3331  N  N   . TYR A  1 439 ? 74.307  42.308 38.534  1.00 24.87 ? 439  TYR A N   1 
ATOM   3332  C  CA  . TYR A  1 439 ? 72.926  41.963 38.857  1.00 23.78 ? 439  TYR A CA  1 
ATOM   3333  C  C   . TYR A  1 439 ? 72.779  40.963 39.986  1.00 24.18 ? 439  TYR A C   1 
ATOM   3334  O  O   . TYR A  1 439 ? 71.669  40.754 40.466  1.00 24.01 ? 439  TYR A O   1 
ATOM   3335  C  CB  . TYR A  1 439 ? 72.189  41.428 37.624  1.00 23.87 ? 439  TYR A CB  1 
ATOM   3336  C  CG  . TYR A  1 439 ? 72.244  42.337 36.409  1.00 23.26 ? 439  TYR A CG  1 
ATOM   3337  C  CD1 . TYR A  1 439 ? 72.217  43.726 36.548  1.00 22.63 ? 439  TYR A CD1 1 
ATOM   3338  C  CD2 . TYR A  1 439 ? 72.312  41.805 35.122  1.00 22.52 ? 439  TYR A CD2 1 
ATOM   3339  C  CE1 . TYR A  1 439 ? 72.257  44.565 35.435  1.00 22.84 ? 439  TYR A CE1 1 
ATOM   3340  C  CE2 . TYR A  1 439 ? 72.354  42.637 33.997  1.00 22.17 ? 439  TYR A CE2 1 
ATOM   3341  C  CZ  . TYR A  1 439 ? 72.327  44.011 34.158  1.00 22.39 ? 439  TYR A CZ  1 
ATOM   3342  O  OH  . TYR A  1 439 ? 72.374  44.834 33.051  1.00 21.76 ? 439  TYR A OH  1 
ATOM   3343  N  N   . THR A  1 440 ? 73.863  40.327 40.418  1.00 23.60 ? 440  THR A N   1 
ATOM   3344  C  CA  . THR A  1 440 ? 73.708  39.379 41.524  1.00 25.01 ? 440  THR A CA  1 
ATOM   3345  C  C   . THR A  1 440 ? 73.670  40.157 42.833  1.00 23.88 ? 440  THR A C   1 
ATOM   3346  O  O   . THR A  1 440 ? 73.394  39.593 43.884  1.00 24.46 ? 440  THR A O   1 
ATOM   3347  C  CB  . THR A  1 440 ? 74.863  38.365 41.620  1.00 24.60 ? 440  THR A CB  1 
ATOM   3348  O  OG1 . THR A  1 440 ? 76.022  39.030 42.119  1.00 26.10 ? 440  THR A OG1 1 
ATOM   3349  C  CG2 . THR A  1 440 ? 75.183  37.776 40.248  1.00 27.51 ? 440  THR A CG2 1 
ATOM   3350  N  N   . LYS A  1 441 ? 73.952  41.452 42.772  1.00 23.57 ? 441  LYS A N   1 
ATOM   3351  C  CA  . LYS A  1 441 ? 73.934  42.271 43.984  1.00 24.43 ? 441  LYS A CA  1 
ATOM   3352  C  C   . LYS A  1 441 ? 72.633  43.062 44.127  1.00 23.31 ? 441  LYS A C   1 
ATOM   3353  O  O   . LYS A  1 441 ? 72.538  44.190 43.653  1.00 22.82 ? 441  LYS A O   1 
ATOM   3354  C  CB  . LYS A  1 441 ? 75.111  43.250 43.980  1.00 26.11 ? 441  LYS A CB  1 
ATOM   3355  C  CG  . LYS A  1 441 ? 76.450  42.594 43.654  1.00 29.84 ? 441  LYS A CG  1 
ATOM   3356  C  CD  . LYS A  1 441 ? 76.877  41.646 44.746  1.00 31.37 ? 441  LYS A CD  1 
ATOM   3357  C  CE  . LYS A  1 441 ? 77.984  42.273 45.552  1.00 34.46 ? 441  LYS A CE  1 
ATOM   3358  N  NZ  . LYS A  1 441 ? 79.193  42.502 44.705  1.00 35.06 ? 441  LYS A NZ  1 
ATOM   3359  N  N   . VAL A  1 442 ? 71.646  42.464 44.789  1.00 22.50 ? 442  VAL A N   1 
ATOM   3360  C  CA  . VAL A  1 442 ? 70.343  43.093 45.022  1.00 21.12 ? 442  VAL A CA  1 
ATOM   3361  C  C   . VAL A  1 442 ? 70.175  43.343 46.530  1.00 21.66 ? 442  VAL A C   1 
ATOM   3362  O  O   . VAL A  1 442 ? 70.321  42.423 47.325  1.00 22.08 ? 442  VAL A O   1 
ATOM   3363  C  CB  . VAL A  1 442 ? 69.203  42.162 44.544  1.00 21.21 ? 442  VAL A CB  1 
ATOM   3364  C  CG1 . VAL A  1 442 ? 67.835  42.768 44.889  1.00 18.96 ? 442  VAL A CG1 1 
ATOM   3365  C  CG2 . VAL A  1 442 ? 69.334  41.912 43.047  1.00 18.82 ? 442  VAL A CG2 1 
ATOM   3366  N  N   . THR A  1 443 ? 69.867  44.574 46.923  1.00 21.70 ? 443  THR A N   1 
ATOM   3367  C  CA  . THR A  1 443 ? 69.712  44.901 48.338  1.00 21.36 ? 443  THR A CA  1 
ATOM   3368  C  C   . THR A  1 443 ? 68.310  45.390 48.691  1.00 21.22 ? 443  THR A C   1 
ATOM   3369  O  O   . THR A  1 443 ? 67.790  46.316 48.058  1.00 20.81 ? 443  THR A O   1 
ATOM   3370  C  CB  . THR A  1 443 ? 70.696  46.011 48.747  1.00 22.35 ? 443  THR A CB  1 
ATOM   3371  O  OG1 . THR A  1 443 ? 71.996  45.685 48.254  1.00 21.71 ? 443  THR A OG1 1 
ATOM   3372  C  CG2 . THR A  1 443 ? 70.755  46.161 50.269  1.00 22.28 ? 443  THR A CG2 1 
ATOM   3373  N  N   . CYS A  1 444 ? 67.683  44.784 49.698  1.00 21.21 ? 444  CYS A N   1 
ATOM   3374  C  CA  . CYS A  1 444 ? 66.367  45.253 50.091  1.00 20.44 ? 444  CYS A CA  1 
ATOM   3375  C  C   . CYS A  1 444 ? 66.623  46.427 51.018  1.00 20.27 ? 444  CYS A C   1 
ATOM   3376  O  O   . CYS A  1 444 ? 67.369  46.312 51.994  1.00 21.63 ? 444  CYS A O   1 
ATOM   3377  C  CB  . CYS A  1 444 ? 65.561  44.192 50.824  1.00 20.47 ? 444  CYS A CB  1 
ATOM   3378  S  SG  . CYS A  1 444 ? 63.847  44.835 51.038  1.00 21.66 ? 444  CYS A SG  1 
ATOM   3379  N  N   . LEU A  1 445 ? 65.996  47.554 50.723  1.00 18.50 ? 445  LEU A N   1 
ATOM   3380  C  CA  . LEU A  1 445 ? 66.220  48.749 51.512  1.00 17.95 ? 445  LEU A CA  1 
ATOM   3381  C  C   . LEU A  1 445 ? 65.146  49.025 52.564  1.00 17.25 ? 445  LEU A C   1 
ATOM   3382  O  O   . LEU A  1 445 ? 65.353  49.837 53.465  1.00 15.97 ? 445  LEU A O   1 
ATOM   3383  C  CB  . LEU A  1 445 ? 66.351  49.948 50.561  1.00 17.86 ? 445  LEU A CB  1 
ATOM   3384  C  CG  . LEU A  1 445 ? 67.400  49.811 49.433  1.00 18.16 ? 445  LEU A CG  1 
ATOM   3385  C  CD1 . LEU A  1 445 ? 67.346  51.042 48.513  1.00 17.20 ? 445  LEU A CD1 1 
ATOM   3386  C  CD2 . LEU A  1 445 ? 68.804  49.673 50.054  1.00 17.28 ? 445  LEU A CD2 1 
ATOM   3387  N  N   . SER A  1 446 ? 64.004  48.352 52.461  1.00 17.32 ? 446  SER A N   1 
ATOM   3388  C  CA  . SER A  1 446 ? 62.917  48.578 53.414  1.00 17.91 ? 446  SER A CA  1 
ATOM   3389  C  C   . SER A  1 446 ? 62.482  47.345 54.201  1.00 18.87 ? 446  SER A C   1 
ATOM   3390  O  O   . SER A  1 446 ? 61.814  47.479 55.229  1.00 18.99 ? 446  SER A O   1 
ATOM   3391  C  CB  . SER A  1 446 ? 61.692  49.128 52.672  1.00 17.37 ? 446  SER A CB  1 
ATOM   3392  O  OG  . SER A  1 446 ? 61.234  48.173 51.718  1.00 16.13 ? 446  SER A OG  1 
ATOM   3393  N  N   . CYS A  1 447 ? 62.852  46.160 53.724  1.00 18.42 ? 447  CYS A N   1 
ATOM   3394  C  CA  . CYS A  1 447 ? 62.422  44.906 54.354  1.00 20.50 ? 447  CYS A CA  1 
ATOM   3395  C  C   . CYS A  1 447 ? 62.616  44.828 55.859  1.00 20.98 ? 447  CYS A C   1 
ATOM   3396  O  O   . CYS A  1 447 ? 61.709  44.461 56.600  1.00 20.19 ? 447  CYS A O   1 
ATOM   3397  C  CB  . CYS A  1 447 ? 63.146  43.697 53.728  1.00 21.25 ? 447  CYS A CB  1 
ATOM   3398  S  SG  . CYS A  1 447 ? 62.799  43.358 51.961  1.00 23.83 ? 447  CYS A SG  1 
ATOM   3399  N  N   . GLU A  1 448 ? 63.804  45.195 56.308  1.00 21.74 ? 448  GLU A N   1 
ATOM   3400  C  CA  . GLU A  1 448 ? 64.142  45.079 57.715  1.00 23.38 ? 448  GLU A CA  1 
ATOM   3401  C  C   . GLU A  1 448 ? 64.021  46.323 58.592  1.00 22.69 ? 448  GLU A C   1 
ATOM   3402  O  O   . GLU A  1 448 ? 64.397  46.282 59.764  1.00 21.54 ? 448  GLU A O   1 
ATOM   3403  C  CB  . GLU A  1 448 ? 65.557  44.501 57.815  1.00 25.38 ? 448  GLU A CB  1 
ATOM   3404  C  CG  . GLU A  1 448 ? 65.621  43.099 58.387  1.00 30.97 ? 448  GLU A CG  1 
ATOM   3405  C  CD  . GLU A  1 448 ? 64.617  42.157 57.770  1.00 32.28 ? 448  GLU A CD  1 
ATOM   3406  O  OE1 . GLU A  1 448 ? 64.736  41.847 56.565  1.00 33.95 ? 448  GLU A OE1 1 
ATOM   3407  O  OE2 . GLU A  1 448 ? 63.700  41.730 58.501  1.00 35.02 ? 448  GLU A OE2 1 
ATOM   3408  N  N   . LEU A  1 449 ? 63.499  47.418 58.043  1.00 21.61 ? 449  LEU A N   1 
ATOM   3409  C  CA  . LEU A  1 449 ? 63.356  48.639 58.831  1.00 20.99 ? 449  LEU A CA  1 
ATOM   3410  C  C   . LEU A  1 449 ? 62.463  48.392 60.042  1.00 20.59 ? 449  LEU A C   1 
ATOM   3411  O  O   . LEU A  1 449 ? 62.803  48.782 61.153  1.00 20.98 ? 449  LEU A O   1 
ATOM   3412  C  CB  . LEU A  1 449 ? 62.796  49.784 57.970  1.00 19.27 ? 449  LEU A CB  1 
ATOM   3413  C  CG  . LEU A  1 449 ? 63.734  50.244 56.837  1.00 19.75 ? 449  LEU A CG  1 
ATOM   3414  C  CD1 . LEU A  1 449 ? 63.018  51.203 55.937  1.00 18.48 ? 449  LEU A CD1 1 
ATOM   3415  C  CD2 . LEU A  1 449 ? 64.989  50.892 57.421  1.00 20.73 ? 449  LEU A CD2 1 
ATOM   3416  N  N   . ASN A  1 450 ? 61.323  47.744 59.830  1.00 20.59 ? 450  ASN A N   1 
ATOM   3417  C  CA  . ASN A  1 450 ? 60.398  47.434 60.924  1.00 20.60 ? 450  ASN A CA  1 
ATOM   3418  C  C   . ASN A  1 450 ? 59.464  46.380 60.351  1.00 20.66 ? 450  ASN A C   1 
ATOM   3419  O  O   . ASN A  1 450 ? 58.318  46.670 59.987  1.00 18.44 ? 450  ASN A O   1 
ATOM   3420  C  CB  . ASN A  1 450 ? 59.604  48.677 61.340  1.00 20.71 ? 450  ASN A CB  1 
ATOM   3421  C  CG  . ASN A  1 450 ? 58.828  48.459 62.638  1.00 21.56 ? 450  ASN A CG  1 
ATOM   3422  O  OD1 . ASN A  1 450 ? 58.315  47.363 62.900  1.00 22.40 ? 450  ASN A OD1 1 
ATOM   3423  N  ND2 . ASN A  1 450 ? 58.729  49.501 63.444  1.00 21.74 ? 450  ASN A ND2 1 
ATOM   3424  N  N   . PRO A  1 451 ? 59.948  45.132 60.276  1.00 20.66 ? 451  PRO A N   1 
ATOM   3425  C  CA  . PRO A  1 451 ? 59.181  44.014 59.728  1.00 21.32 ? 451  PRO A CA  1 
ATOM   3426  C  C   . PRO A  1 451 ? 57.798  43.749 60.303  1.00 21.67 ? 451  PRO A C   1 
ATOM   3427  O  O   . PRO A  1 451 ? 56.903  43.340 59.568  1.00 21.32 ? 451  PRO A O   1 
ATOM   3428  C  CB  . PRO A  1 451 ? 60.140  42.829 59.869  1.00 22.48 ? 451  PRO A CB  1 
ATOM   3429  C  CG  . PRO A  1 451 ? 60.968  43.185 61.055  1.00 22.95 ? 451  PRO A CG  1 
ATOM   3430  C  CD  . PRO A  1 451 ? 61.212  44.669 60.880  1.00 21.72 ? 451  PRO A CD  1 
ATOM   3431  N  N   . GLU A  1 452 ? 57.612  43.983 61.597  1.00 22.31 ? 452  GLU A N   1 
ATOM   3432  C  CA  . GLU A  1 452 ? 56.313  43.759 62.215  1.00 22.81 ? 452  GLU A CA  1 
ATOM   3433  C  C   . GLU A  1 452 ? 55.307  44.826 61.796  1.00 21.41 ? 452  GLU A C   1 
ATOM   3434  O  O   . GLU A  1 452 ? 54.155  44.533 61.498  1.00 20.66 ? 452  GLU A O   1 
ATOM   3435  C  CB  . GLU A  1 452 ? 56.434  43.777 63.740  1.00 25.67 ? 452  GLU A CB  1 
ATOM   3436  C  CG  . GLU A  1 452 ? 57.294  42.672 64.322  1.00 32.07 ? 452  GLU A CG  1 
ATOM   3437  C  CD  . GLU A  1 452 ? 57.280  42.675 65.852  1.00 36.16 ? 452  GLU A CD  1 
ATOM   3438  O  OE1 . GLU A  1 452 ? 56.237  43.068 66.444  1.00 38.56 ? 452  GLU A OE1 1 
ATOM   3439  O  OE2 . GLU A  1 452 ? 58.304  42.276 66.464  1.00 39.17 ? 452  GLU A OE2 1 
ATOM   3440  N  N   . ARG A  1 453 ? 55.747  46.076 61.777  1.00 20.37 ? 453  ARG A N   1 
ATOM   3441  C  CA  . ARG A  1 453 ? 54.848  47.166 61.424  1.00 19.24 ? 453  ARG A CA  1 
ATOM   3442  C  C   . ARG A  1 453 ? 54.771  47.479 59.932  1.00 18.10 ? 453  ARG A C   1 
ATOM   3443  O  O   . ARG A  1 453 ? 53.739  47.921 59.420  1.00 17.38 ? 453  ARG A O   1 
ATOM   3444  C  CB  . ARG A  1 453 ? 55.282  48.442 62.147  1.00 19.29 ? 453  ARG A CB  1 
ATOM   3445  C  CG  . ARG A  1 453 ? 54.450  49.673 61.801  1.00 18.66 ? 453  ARG A CG  1 
ATOM   3446  C  CD  . ARG A  1 453 ? 54.915  50.879 62.615  1.00 18.61 ? 453  ARG A CD  1 
ATOM   3447  N  NE  . ARG A  1 453 ? 54.158  52.087 62.311  1.00 17.21 ? 453  ARG A NE  1 
ATOM   3448  C  CZ  . ARG A  1 453 ? 54.286  53.223 62.986  1.00 18.42 ? 453  ARG A CZ  1 
ATOM   3449  N  NH1 . ARG A  1 453 ? 55.143  53.286 63.995  1.00 17.56 ? 453  ARG A NH1 1 
ATOM   3450  N  NH2 . ARG A  1 453 ? 53.566  54.291 62.661  1.00 17.24 ? 453  ARG A NH2 1 
ATOM   3451  N  N   . CYS A  1 454 ? 55.866  47.229 59.237  1.00 17.45 ? 454  CYS A N   1 
ATOM   3452  C  CA  . CYS A  1 454 ? 55.952  47.604 57.839  1.00 17.05 ? 454  CYS A CA  1 
ATOM   3453  C  C   . CYS A  1 454 ? 56.307  46.533 56.822  1.00 15.70 ? 454  CYS A C   1 
ATOM   3454  O  O   . CYS A  1 454 ? 57.431  46.045 56.782  1.00 14.96 ? 454  CYS A O   1 
ATOM   3455  C  CB  . CYS A  1 454 ? 56.923  48.794 57.741  1.00 17.65 ? 454  CYS A CB  1 
ATOM   3456  S  SG  . CYS A  1 454 ? 56.316  50.238 58.651  1.00 19.61 ? 454  CYS A SG  1 
ATOM   3457  N  N   . GLN A  1 455 ? 55.326  46.203 55.982  1.00 15.31 ? 455  GLN A N   1 
ATOM   3458  C  CA  . GLN A  1 455 ? 55.497  45.199 54.937  1.00 14.95 ? 455  GLN A CA  1 
ATOM   3459  C  C   . GLN A  1 455 ? 54.951  45.703 53.588  1.00 15.88 ? 455  GLN A C   1 
ATOM   3460  O  O   . GLN A  1 455 ? 54.901  44.957 52.614  1.00 15.84 ? 455  GLN A O   1 
ATOM   3461  C  CB  . GLN A  1 455 ? 54.762  43.917 55.340  1.00 15.26 ? 455  GLN A CB  1 
ATOM   3462  C  CG  . GLN A  1 455 ? 55.278  43.298 56.644  1.00 16.17 ? 455  GLN A CG  1 
ATOM   3463  C  CD  . GLN A  1 455 ? 54.304  42.280 57.252  1.00 19.92 ? 455  GLN A CD  1 
ATOM   3464  O  OE1 . GLN A  1 455 ? 53.320  41.877 56.615  1.00 19.45 ? 455  GLN A OE1 1 
ATOM   3465  N  NE2 . GLN A  1 455 ? 54.582  41.857 58.490  1.00 19.81 ? 455  GLN A NE2 1 
ATOM   3466  N  N   . TYR A  1 456 ? 54.515  46.959 53.546  1.00 14.97 ? 456  TYR A N   1 
ATOM   3467  C  CA  . TYR A  1 456 ? 53.982  47.541 52.323  1.00 15.00 ? 456  TYR A CA  1 
ATOM   3468  C  C   . TYR A  1 456 ? 54.508  48.962 52.180  1.00 14.60 ? 456  TYR A C   1 
ATOM   3469  O  O   . TYR A  1 456 ? 54.117  49.879 52.915  1.00 13.81 ? 456  TYR A O   1 
ATOM   3470  C  CB  . TYR A  1 456 ? 52.457  47.530 52.361  1.00 14.42 ? 456  TYR A CB  1 
ATOM   3471  C  CG  . TYR A  1 456 ? 51.764  47.597 51.003  1.00 13.83 ? 456  TYR A CG  1 
ATOM   3472  C  CD1 . TYR A  1 456 ? 51.627  48.810 50.318  1.00 13.42 ? 456  TYR A CD1 1 
ATOM   3473  C  CD2 . TYR A  1 456 ? 51.182  46.460 50.445  1.00 13.06 ? 456  TYR A CD2 1 
ATOM   3474  C  CE1 . TYR A  1 456 ? 50.915  48.888 49.104  1.00 13.78 ? 456  TYR A CE1 1 
ATOM   3475  C  CE2 . TYR A  1 456 ? 50.467  46.524 49.235  1.00 13.79 ? 456  TYR A CE2 1 
ATOM   3476  C  CZ  . TYR A  1 456 ? 50.334  47.733 48.573  1.00 14.38 ? 456  TYR A CZ  1 
ATOM   3477  O  OH  . TYR A  1 456 ? 49.606  47.780 47.397  1.00 14.35 ? 456  TYR A OH  1 
ATOM   3478  N  N   . TYR A  1 457 ? 55.395  49.149 51.212  1.00 13.33 ? 457  TYR A N   1 
ATOM   3479  C  CA  . TYR A  1 457 ? 56.011  50.453 50.995  1.00 13.03 ? 457  TYR A CA  1 
ATOM   3480  C  C   . TYR A  1 457 ? 55.776  51.060 49.616  1.00 14.19 ? 457  TYR A C   1 
ATOM   3481  O  O   . TYR A  1 457 ? 55.524  50.365 48.624  1.00 13.61 ? 457  TYR A O   1 
ATOM   3482  C  CB  . TYR A  1 457 ? 57.533  50.362 51.200  1.00 12.96 ? 457  TYR A CB  1 
ATOM   3483  C  CG  . TYR A  1 457 ? 58.010  50.160 52.624  1.00 13.75 ? 457  TYR A CG  1 
ATOM   3484  C  CD1 . TYR A  1 457 ? 58.410  51.248 53.405  1.00 14.73 ? 457  TYR A CD1 1 
ATOM   3485  C  CD2 . TYR A  1 457 ? 58.142  48.884 53.165  1.00 15.01 ? 457  TYR A CD2 1 
ATOM   3486  C  CE1 . TYR A  1 457 ? 58.945  51.071 54.681  1.00 13.90 ? 457  TYR A CE1 1 
ATOM   3487  C  CE2 . TYR A  1 457 ? 58.684  48.689 54.466  1.00 14.97 ? 457  TYR A CE2 1 
ATOM   3488  C  CZ  . TYR A  1 457 ? 59.084  49.794 55.209  1.00 15.04 ? 457  TYR A CZ  1 
ATOM   3489  O  OH  . TYR A  1 457 ? 59.641  49.644 56.469  1.00 14.72 ? 457  TYR A OH  1 
ATOM   3490  N  N   . SER A  1 458 ? 55.928  52.373 49.597  1.00 14.04 ? 458  SER A N   1 
ATOM   3491  C  CA  . SER A  1 458 ? 55.842  53.209 48.410  1.00 16.56 ? 458  SER A CA  1 
ATOM   3492  C  C   . SER A  1 458 ? 57.047  54.133 48.648  1.00 16.42 ? 458  SER A C   1 
ATOM   3493  O  O   . SER A  1 458 ? 57.446  54.311 49.803  1.00 15.36 ? 458  SER A O   1 
ATOM   3494  C  CB  . SER A  1 458 ? 54.581  54.054 48.435  1.00 16.15 ? 458  SER A CB  1 
ATOM   3495  O  OG  . SER A  1 458 ? 54.453  54.667 47.203  1.00 25.28 ? 458  SER A OG  1 
ATOM   3496  N  N   . VAL A  1 459 ? 57.595  54.742 47.599  1.00 16.13 ? 459  VAL A N   1 
ATOM   3497  C  CA  . VAL A  1 459 ? 58.746  55.606 47.775  1.00 16.46 ? 459  VAL A CA  1 
ATOM   3498  C  C   . VAL A  1 459 ? 58.706  56.857 46.918  1.00 17.18 ? 459  VAL A C   1 
ATOM   3499  O  O   . VAL A  1 459 ? 58.043  56.886 45.886  1.00 18.84 ? 459  VAL A O   1 
ATOM   3500  C  CB  . VAL A  1 459 ? 60.070  54.834 47.453  1.00 16.27 ? 459  VAL A CB  1 
ATOM   3501  C  CG1 . VAL A  1 459 ? 60.131  54.485 45.970  1.00 14.90 ? 459  VAL A CG1 1 
ATOM   3502  C  CG2 . VAL A  1 459 ? 61.285  55.676 47.850  1.00 16.39 ? 459  VAL A CG2 1 
ATOM   3503  N  N   . SER A  1 460 ? 59.435  57.887 47.341  1.00 16.97 ? 460  SER A N   1 
ATOM   3504  C  CA  . SER A  1 460 ? 59.531  59.141 46.585  1.00 16.85 ? 460  SER A CA  1 
ATOM   3505  C  C   . SER A  1 460 ? 60.983  59.632 46.612  1.00 16.41 ? 460  SER A C   1 
ATOM   3506  O  O   . SER A  1 460 ? 61.467  60.093 47.657  1.00 16.18 ? 460  SER A O   1 
ATOM   3507  C  CB  . SER A  1 460 ? 58.622  60.209 47.203  1.00 17.87 ? 460  SER A CB  1 
ATOM   3508  O  OG  . SER A  1 460 ? 58.687  61.422 46.473  1.00 17.53 ? 460  SER A OG  1 
ATOM   3509  N  N   . PHE A  1 461 ? 61.682  59.535 45.481  1.00 14.74 ? 461  PHE A N   1 
ATOM   3510  C  CA  . PHE A  1 461 ? 63.087  59.971 45.425  1.00 15.12 ? 461  PHE A CA  1 
ATOM   3511  C  C   . PHE A  1 461 ? 63.248  61.443 45.074  1.00 16.10 ? 461  PHE A C   1 
ATOM   3512  O  O   . PHE A  1 461 ? 62.418  61.988 44.359  1.00 16.55 ? 461  PHE A O   1 
ATOM   3513  C  CB  . PHE A  1 461 ? 63.877  59.163 44.385  1.00 13.63 ? 461  PHE A CB  1 
ATOM   3514  C  CG  . PHE A  1 461 ? 64.214  57.763 44.820  1.00 13.47 ? 461  PHE A CG  1 
ATOM   3515  C  CD1 . PHE A  1 461 ? 63.274  56.737 44.728  1.00 12.67 ? 461  PHE A CD1 1 
ATOM   3516  C  CD2 . PHE A  1 461 ? 65.486  57.461 45.300  1.00 13.34 ? 461  PHE A CD2 1 
ATOM   3517  C  CE1 . PHE A  1 461 ? 63.599  55.453 45.100  1.00 12.14 ? 461  PHE A CE1 1 
ATOM   3518  C  CE2 . PHE A  1 461 ? 65.815  56.158 45.679  1.00 13.51 ? 461  PHE A CE2 1 
ATOM   3519  C  CZ  . PHE A  1 461 ? 64.871  55.158 45.577  1.00 12.23 ? 461  PHE A CZ  1 
ATOM   3520  N  N   . SER A  1 462 ? 64.315  62.080 45.568  1.00 16.36 ? 462  SER A N   1 
ATOM   3521  C  CA  . SER A  1 462 ? 64.583  63.479 45.221  1.00 18.38 ? 462  SER A CA  1 
ATOM   3522  C  C   . SER A  1 462 ? 65.050  63.506 43.754  1.00 19.86 ? 462  SER A C   1 
ATOM   3523  O  O   . SER A  1 462 ? 65.316  62.459 43.152  1.00 18.41 ? 462  SER A O   1 
ATOM   3524  C  CB  . SER A  1 462 ? 65.688  64.071 46.109  1.00 16.82 ? 462  SER A CB  1 
ATOM   3525  O  OG  . SER A  1 462 ? 66.909  63.365 45.934  1.00 15.85 ? 462  SER A OG  1 
ATOM   3526  N  N   . LYS A  1 463 ? 65.200  64.704 43.204  1.00 23.49 ? 463  LYS A N   1 
ATOM   3527  C  CA  . LYS A  1 463 ? 65.597  64.882 41.797  1.00 26.60 ? 463  LYS A CA  1 
ATOM   3528  C  C   . LYS A  1 463 ? 66.649  63.954 41.194  1.00 27.34 ? 463  LYS A C   1 
ATOM   3529  O  O   . LYS A  1 463 ? 66.417  63.405 40.120  1.00 29.02 ? 463  LYS A O   1 
ATOM   3530  C  CB  . LYS A  1 463 ? 65.999  66.337 41.557  1.00 28.89 ? 463  LYS A CB  1 
ATOM   3531  C  CG  . LYS A  1 463 ? 64.800  67.271 41.528  1.00 31.86 ? 463  LYS A CG  1 
ATOM   3532  C  CD  . LYS A  1 463 ? 64.209  67.315 40.120  1.00 36.23 ? 463  LYS A CD  1 
ATOM   3533  C  CE  . LYS A  1 463 ? 62.843  67.983 40.066  1.00 37.24 ? 463  LYS A CE  1 
ATOM   3534  N  NZ  . LYS A  1 463 ? 61.785  67.143 40.719  1.00 39.17 ? 463  LYS A NZ  1 
ATOM   3535  N  N   . GLU A  1 464 ? 67.794  63.768 41.848  1.00 27.05 ? 464  GLU A N   1 
ATOM   3536  C  CA  . GLU A  1 464 ? 68.826  62.876 41.300  1.00 26.87 ? 464  GLU A CA  1 
ATOM   3537  C  C   . GLU A  1 464 ? 69.014  61.653 42.193  1.00 25.43 ? 464  GLU A C   1 
ATOM   3538  O  O   . GLU A  1 464 ? 70.116  61.102 42.302  1.00 24.08 ? 464  GLU A O   1 
ATOM   3539  C  CB  . GLU A  1 464 ? 70.178  63.598 41.158  1.00 29.39 ? 464  GLU A CB  1 
ATOM   3540  C  CG  . GLU A  1 464 ? 70.167  64.815 40.242  1.00 33.37 ? 464  GLU A CG  1 
ATOM   3541  C  CD  . GLU A  1 464 ? 69.560  64.512 38.878  1.00 37.48 ? 464  GLU A CD  1 
ATOM   3542  O  OE1 . GLU A  1 464 ? 69.981  63.513 38.244  1.00 40.32 ? 464  GLU A OE1 1 
ATOM   3543  O  OE2 . GLU A  1 464 ? 68.663  65.273 38.429  1.00 38.53 ? 464  GLU A OE2 1 
ATOM   3544  N  N   . ALA A  1 465 ? 67.935  61.247 42.856  1.00 23.89 ? 465  ALA A N   1 
ATOM   3545  C  CA  . ALA A  1 465 ? 67.962  60.081 43.729  1.00 20.94 ? 465  ALA A CA  1 
ATOM   3546  C  C   . ALA A  1 465 ? 68.959  60.177 44.872  1.00 19.60 ? 465  ALA A C   1 
ATOM   3547  O  O   . ALA A  1 465 ? 69.398  59.162 45.394  1.00 18.79 ? 465  ALA A O   1 
ATOM   3548  C  CB  . ALA A  1 465 ? 68.242  58.847 42.916  1.00 19.91 ? 465  ALA A CB  1 
ATOM   3549  N  N   . LYS A  1 466 ? 69.323  61.388 45.265  1.00 19.26 ? 466  LYS A N   1 
ATOM   3550  C  CA  . LYS A  1 466 ? 70.261  61.543 46.370  1.00 19.31 ? 466  LYS A CA  1 
ATOM   3551  C  C   . LYS A  1 466 ? 69.557  61.183 47.683  1.00 18.87 ? 466  LYS A C   1 
ATOM   3552  O  O   . LYS A  1 466 ? 70.184  60.685 48.615  1.00 18.13 ? 466  LYS A O   1 
ATOM   3553  C  CB  . LYS A  1 466 ? 70.785  62.978 46.429  1.00 19.72 ? 466  LYS A CB  1 
ATOM   3554  C  CG  . LYS A  1 466 ? 71.874  63.197 47.488  1.00 23.39 ? 466  LYS A CG  1 
ATOM   3555  C  CD  . LYS A  1 466 ? 72.673  64.487 47.216  1.00 25.83 ? 466  LYS A CD  1 
ATOM   3556  C  CE  . LYS A  1 466 ? 73.859  64.597 48.173  1.00 28.15 ? 466  LYS A CE  1 
ATOM   3557  N  NZ  . LYS A  1 466 ? 74.726  65.767 47.851  1.00 32.46 ? 466  LYS A NZ  1 
ATOM   3558  N  N   . TYR A  1 467 ? 68.247  61.421 47.738  1.00 17.49 ? 467  TYR A N   1 
ATOM   3559  C  CA  . TYR A  1 467 ? 67.456  61.111 48.932  1.00 17.72 ? 467  TYR A CA  1 
ATOM   3560  C  C   . TYR A  1 467 ? 66.148  60.407 48.567  1.00 17.88 ? 467  TYR A C   1 
ATOM   3561  O  O   . TYR A  1 467 ? 65.684  60.502 47.428  1.00 17.29 ? 467  TYR A O   1 
ATOM   3562  C  CB  . TYR A  1 467 ? 67.091  62.398 49.675  1.00 17.55 ? 467  TYR A CB  1 
ATOM   3563  C  CG  . TYR A  1 467 ? 68.277  63.160 50.201  1.00 19.08 ? 467  TYR A CG  1 
ATOM   3564  C  CD1 . TYR A  1 467 ? 68.848  62.829 51.427  1.00 20.13 ? 467  TYR A CD1 1 
ATOM   3565  C  CD2 . TYR A  1 467 ? 68.855  64.187 49.457  1.00 18.82 ? 467  TYR A CD2 1 
ATOM   3566  C  CE1 . TYR A  1 467 ? 69.975  63.502 51.902  1.00 20.74 ? 467  TYR A CE1 1 
ATOM   3567  C  CE2 . TYR A  1 467 ? 69.985  64.864 49.916  1.00 20.82 ? 467  TYR A CE2 1 
ATOM   3568  C  CZ  . TYR A  1 467 ? 70.539  64.515 51.139  1.00 21.64 ? 467  TYR A CZ  1 
ATOM   3569  O  OH  . TYR A  1 467 ? 71.660  65.165 51.592  1.00 22.72 ? 467  TYR A OH  1 
ATOM   3570  N  N   . TYR A  1 468 ? 65.571  59.681 49.526  1.00 17.28 ? 468  TYR A N   1 
ATOM   3571  C  CA  . TYR A  1 468 ? 64.272  59.070 49.305  1.00 16.30 ? 468  TYR A CA  1 
ATOM   3572  C  C   . TYR A  1 468 ? 63.433  59.024 50.560  1.00 17.06 ? 468  TYR A C   1 
ATOM   3573  O  O   . TYR A  1 468 ? 63.940  58.862 51.677  1.00 16.13 ? 468  TYR A O   1 
ATOM   3574  C  CB  . TYR A  1 468 ? 64.351  57.666 48.690  1.00 16.09 ? 468  TYR A CB  1 
ATOM   3575  C  CG  . TYR A  1 468 ? 65.154  56.631 49.442  1.00 16.91 ? 468  TYR A CG  1 
ATOM   3576  C  CD1 . TYR A  1 468 ? 66.536  56.572 49.301  1.00 17.23 ? 468  TYR A CD1 1 
ATOM   3577  C  CD2 . TYR A  1 468 ? 64.531  55.673 50.247  1.00 16.92 ? 468  TYR A CD2 1 
ATOM   3578  C  CE1 . TYR A  1 468 ? 67.289  55.578 49.933  1.00 18.23 ? 468  TYR A CE1 1 
ATOM   3579  C  CE2 . TYR A  1 468 ? 65.278  54.665 50.892  1.00 16.11 ? 468  TYR A CE2 1 
ATOM   3580  C  CZ  . TYR A  1 468 ? 66.660  54.624 50.721  1.00 16.83 ? 468  TYR A CZ  1 
ATOM   3581  O  OH  . TYR A  1 468 ? 67.419  53.613 51.282  1.00 15.28 ? 468  TYR A OH  1 
ATOM   3582  N  N   . GLN A  1 469 ? 62.140  59.224 50.354  1.00 16.46 ? 469  GLN A N   1 
ATOM   3583  C  CA  . GLN A  1 469 ? 61.179  59.172 51.431  1.00 16.38 ? 469  GLN A CA  1 
ATOM   3584  C  C   . GLN A  1 469 ? 60.460  57.849 51.280  1.00 15.99 ? 469  GLN A C   1 
ATOM   3585  O  O   . GLN A  1 469 ? 59.954  57.527 50.198  1.00 14.94 ? 469  GLN A O   1 
ATOM   3586  C  CB  . GLN A  1 469 ? 60.139  60.287 51.310  1.00 15.97 ? 469  GLN A CB  1 
ATOM   3587  C  CG  . GLN A  1 469 ? 59.007  60.118 52.305  1.00 16.41 ? 469  GLN A CG  1 
ATOM   3588  C  CD  . GLN A  1 469 ? 57.773  60.925 51.960  1.00 17.15 ? 469  GLN A CD  1 
ATOM   3589  O  OE1 . GLN A  1 469 ? 57.351  60.981 50.806  1.00 17.60 ? 469  GLN A OE1 1 
ATOM   3590  N  NE2 . GLN A  1 469 ? 57.174  61.545 52.968  1.00 15.73 ? 469  GLN A NE2 1 
ATOM   3591  N  N   . LEU A  1 470 ? 60.442  57.077 52.355  1.00 15.19 ? 470  LEU A N   1 
ATOM   3592  C  CA  . LEU A  1 470 ? 59.727  55.815 52.371  1.00 15.47 ? 470  LEU A CA  1 
ATOM   3593  C  C   . LEU A  1 470 ? 58.380  56.025 53.062  1.00 17.10 ? 470  LEU A C   1 
ATOM   3594  O  O   . LEU A  1 470 ? 58.294  56.705 54.101  1.00 16.29 ? 470  LEU A O   1 
ATOM   3595  C  CB  . LEU A  1 470 ? 60.521  54.751 53.124  1.00 14.35 ? 470  LEU A CB  1 
ATOM   3596  C  CG  . LEU A  1 470 ? 61.652  54.076 52.336  1.00 13.01 ? 470  LEU A CG  1 
ATOM   3597  C  CD1 . LEU A  1 470 ? 62.330  53.057 53.228  1.00 11.90 ? 470  LEU A CD1 1 
ATOM   3598  C  CD2 . LEU A  1 470 ? 61.090  53.393 51.099  1.00 10.48 ? 470  LEU A CD2 1 
ATOM   3599  N  N   . ARG A  1 471 ? 57.331  55.455 52.467  1.00 17.27 ? 471  ARG A N   1 
ATOM   3600  C  CA  . ARG A  1 471 ? 55.989  55.543 53.011  1.00 18.64 ? 471  ARG A CA  1 
ATOM   3601  C  C   . ARG A  1 471 ? 55.516  54.121 53.289  1.00 17.73 ? 471  ARG A C   1 
ATOM   3602  O  O   . ARG A  1 471 ? 55.193  53.360 52.372  1.00 16.23 ? 471  ARG A O   1 
ATOM   3603  C  CB  . ARG A  1 471 ? 55.028  56.209 52.016  1.00 21.30 ? 471  ARG A CB  1 
ATOM   3604  C  CG  . ARG A  1 471 ? 53.594  56.391 52.558  1.00 28.17 ? 471  ARG A CG  1 
ATOM   3605  C  CD  . ARG A  1 471 ? 52.565  56.671 51.443  1.00 32.34 ? 471  ARG A CD  1 
ATOM   3606  N  NE  . ARG A  1 471 ? 52.065  55.398 50.923  1.00 36.96 ? 471  ARG A NE  1 
ATOM   3607  C  CZ  . ARG A  1 471 ? 51.570  55.193 49.708  1.00 38.95 ? 471  ARG A CZ  1 
ATOM   3608  N  NH1 . ARG A  1 471 ? 51.486  56.187 48.821  1.00 39.46 ? 471  ARG A NH1 1 
ATOM   3609  N  NH2 . ARG A  1 471 ? 51.162  53.968 49.383  1.00 40.31 ? 471  ARG A NH2 1 
ATOM   3610  N  N   . CYS A  1 472 ? 55.484  53.764 54.559  1.00 17.26 ? 472  CYS A N   1 
ATOM   3611  C  CA  . CYS A  1 472 ? 55.049  52.441 54.970  1.00 17.24 ? 472  CYS A CA  1 
ATOM   3612  C  C   . CYS A  1 472 ? 53.546  52.556 55.210  1.00 16.38 ? 472  CYS A C   1 
ATOM   3613  O  O   . CYS A  1 472 ? 53.138  53.452 55.926  1.00 16.47 ? 472  CYS A O   1 
ATOM   3614  C  CB  . CYS A  1 472 ? 55.751  52.093 56.291  1.00 17.87 ? 472  CYS A CB  1 
ATOM   3615  S  SG  . CYS A  1 472 ? 54.854  50.892 57.384  1.00 17.48 ? 472  CYS A SG  1 
ATOM   3616  N  N   . SER A  1 473 ? 52.717  51.685 54.628  1.00 17.03 ? 473  SER A N   1 
ATOM   3617  C  CA  . SER A  1 473 ? 51.287  51.804 54.875  1.00 16.54 ? 473  SER A CA  1 
ATOM   3618  C  C   . SER A  1 473 ? 50.611  50.597 55.533  1.00 16.70 ? 473  SER A C   1 
ATOM   3619  O  O   . SER A  1 473 ? 49.373  50.500 55.548  1.00 15.63 ? 473  SER A O   1 
ATOM   3620  C  CB  . SER A  1 473 ? 50.560  52.167 53.580  1.00 16.72 ? 473  SER A CB  1 
ATOM   3621  O  OG  . SER A  1 473 ? 50.843  51.228 52.574  1.00 20.78 ? 473  SER A OG  1 
ATOM   3622  N  N   . GLY A  1 474 ? 51.404  49.681 56.083  1.00 15.00 ? 474  GLY A N   1 
ATOM   3623  C  CA  . GLY A  1 474 ? 50.828  48.527 56.759  1.00 16.32 ? 474  GLY A CA  1 
ATOM   3624  C  C   . GLY A  1 474 ? 51.833  47.413 56.982  1.00 15.51 ? 474  GLY A C   1 
ATOM   3625  O  O   . GLY A  1 474 ? 52.885  47.417 56.361  1.00 16.22 ? 474  GLY A O   1 
ATOM   3626  N  N   . PRO A  1 475 ? 51.505  46.402 57.798  1.00 14.73 ? 475  PRO A N   1 
ATOM   3627  C  CA  . PRO A  1 475 ? 50.232  46.216 58.502  1.00 16.30 ? 475  PRO A CA  1 
ATOM   3628  C  C   . PRO A  1 475 ? 49.942  47.126 59.688  1.00 16.94 ? 475  PRO A C   1 
ATOM   3629  O  O   . PRO A  1 475 ? 48.789  47.236 60.102  1.00 17.15 ? 475  PRO A O   1 
ATOM   3630  C  CB  . PRO A  1 475 ? 50.258  44.736 58.879  1.00 16.16 ? 475  PRO A CB  1 
ATOM   3631  C  CG  . PRO A  1 475 ? 51.698  44.510 59.159  1.00 14.97 ? 475  PRO A CG  1 
ATOM   3632  C  CD  . PRO A  1 475 ? 52.402  45.256 58.024  1.00 14.52 ? 475  PRO A CD  1 
ATOM   3633  N  N   . GLY A  1 476 ? 50.970  47.780 60.224  1.00 16.69 ? 476  GLY A N   1 
ATOM   3634  C  CA  . GLY A  1 476 ? 50.762  48.710 61.320  1.00 16.04 ? 476  GLY A CA  1 
ATOM   3635  C  C   . GLY A  1 476 ? 50.373  50.089 60.778  1.00 16.41 ? 476  GLY A C   1 
ATOM   3636  O  O   . GLY A  1 476 ? 50.069  50.224 59.586  1.00 16.70 ? 476  GLY A O   1 
ATOM   3637  N  N   . LEU A  1 477 ? 50.368  51.107 61.641  1.00 14.97 ? 477  LEU A N   1 
ATOM   3638  C  CA  . LEU A  1 477 ? 50.016  52.470 61.244  1.00 15.16 ? 477  LEU A CA  1 
ATOM   3639  C  C   . LEU A  1 477 ? 51.059  53.056 60.300  1.00 14.46 ? 477  LEU A C   1 
ATOM   3640  O  O   . LEU A  1 477 ? 52.251  52.777 60.430  1.00 15.05 ? 477  LEU A O   1 
ATOM   3641  C  CB  . LEU A  1 477 ? 49.864  53.387 62.473  1.00 14.72 ? 477  LEU A CB  1 
ATOM   3642  C  CG  . LEU A  1 477 ? 48.727  53.041 63.449  1.00 15.23 ? 477  LEU A CG  1 
ATOM   3643  C  CD1 . LEU A  1 477 ? 48.796  53.974 64.680  1.00 14.40 ? 477  LEU A CD1 1 
ATOM   3644  C  CD2 . LEU A  1 477 ? 47.366  53.136 62.741  1.00 15.37 ? 477  LEU A CD2 1 
ATOM   3645  N  N   . PRO A  1 478 ? 50.609  53.861 59.322  1.00 14.40 ? 478  PRO A N   1 
ATOM   3646  C  CA  . PRO A  1 478 ? 51.516  54.483 58.346  1.00 15.48 ? 478  PRO A CA  1 
ATOM   3647  C  C   . PRO A  1 478 ? 52.717  55.136 59.016  1.00 15.25 ? 478  PRO A C   1 
ATOM   3648  O  O   . PRO A  1 478 ? 52.583  55.823 60.037  1.00 14.55 ? 478  PRO A O   1 
ATOM   3649  C  CB  . PRO A  1 478 ? 50.626  55.497 57.636  1.00 14.59 ? 478  PRO A CB  1 
ATOM   3650  C  CG  . PRO A  1 478 ? 49.293  54.784 57.616  1.00 16.47 ? 478  PRO A CG  1 
ATOM   3651  C  CD  . PRO A  1 478 ? 49.203  54.192 59.026  1.00 13.97 ? 478  PRO A CD  1 
ATOM   3652  N  N   . LEU A  1 479 ? 53.888  54.904 58.432  1.00 15.35 ? 479  LEU A N   1 
ATOM   3653  C  CA  . LEU A  1 479 ? 55.140  55.444 58.946  1.00 14.14 ? 479  LEU A CA  1 
ATOM   3654  C  C   . LEU A  1 479 ? 55.892  56.070 57.777  1.00 15.18 ? 479  LEU A C   1 
ATOM   3655  O  O   . LEU A  1 479 ? 56.139  55.398 56.763  1.00 15.65 ? 479  LEU A O   1 
ATOM   3656  C  CB  . LEU A  1 479 ? 55.970  54.306 59.561  1.00 14.62 ? 479  LEU A CB  1 
ATOM   3657  C  CG  . LEU A  1 479 ? 57.364  54.680 60.063  1.00 13.34 ? 479  LEU A CG  1 
ATOM   3658  C  CD1 . LEU A  1 479 ? 57.234  55.850 61.045  1.00 13.29 ? 479  LEU A CD1 1 
ATOM   3659  C  CD2 . LEU A  1 479 ? 58.029  53.482 60.722  1.00 12.48 ? 479  LEU A CD2 1 
ATOM   3660  N  N   . TYR A  1 480 ? 56.257  57.344 57.915  1.00 14.69 ? 480  TYR A N   1 
ATOM   3661  C  CA  . TYR A  1 480 ? 56.974  58.050 56.867  1.00 15.36 ? 480  TYR A CA  1 
ATOM   3662  C  C   . TYR A  1 480 ? 58.373  58.383 57.360  1.00 14.94 ? 480  TYR A C   1 
ATOM   3663  O  O   . TYR A  1 480 ? 58.532  58.987 58.428  1.00 16.11 ? 480  TYR A O   1 
ATOM   3664  C  CB  . TYR A  1 480 ? 56.244  59.352 56.489  1.00 14.05 ? 480  TYR A CB  1 
ATOM   3665  C  CG  . TYR A  1 480 ? 54.838  59.172 55.937  1.00 15.44 ? 480  TYR A CG  1 
ATOM   3666  C  CD1 . TYR A  1 480 ? 53.770  58.824 56.769  1.00 15.36 ? 480  TYR A CD1 1 
ATOM   3667  C  CD2 . TYR A  1 480 ? 54.582  59.354 54.576  1.00 14.99 ? 480  TYR A CD2 1 
ATOM   3668  C  CE1 . TYR A  1 480 ? 52.478  58.660 56.259  1.00 17.46 ? 480  TYR A CE1 1 
ATOM   3669  C  CE2 . TYR A  1 480 ? 53.298  59.191 54.052  1.00 18.52 ? 480  TYR A CE2 1 
ATOM   3670  C  CZ  . TYR A  1 480 ? 52.247  58.841 54.898  1.00 18.60 ? 480  TYR A CZ  1 
ATOM   3671  O  OH  . TYR A  1 480 ? 50.979  58.668 54.369  1.00 23.30 ? 480  TYR A OH  1 
ATOM   3672  N  N   . THR A  1 481 ? 59.379  58.008 56.573  1.00 15.12 ? 481  THR A N   1 
ATOM   3673  C  CA  . THR A  1 481 ? 60.774  58.247 56.931  1.00 15.59 ? 481  THR A CA  1 
ATOM   3674  C  C   . THR A  1 481 ? 61.592  58.811 55.781  1.00 15.25 ? 481  THR A C   1 
ATOM   3675  O  O   . THR A  1 481 ? 61.234  58.621 54.625  1.00 14.82 ? 481  THR A O   1 
ATOM   3676  C  CB  . THR A  1 481 ? 61.445  56.931 57.368  1.00 17.19 ? 481  THR A CB  1 
ATOM   3677  O  OG1 . THR A  1 481 ? 61.124  55.903 56.419  1.00 16.54 ? 481  THR A OG1 1 
ATOM   3678  C  CG2 . THR A  1 481 ? 60.948  56.495 58.753  1.00 17.42 ? 481  THR A CG2 1 
ATOM   3679  N  N   . LEU A  1 482 ? 62.696  59.491 56.093  1.00 14.94 ? 482  LEU A N   1 
ATOM   3680  C  CA  . LEU A  1 482 ? 63.561  60.048 55.058  1.00 15.82 ? 482  LEU A CA  1 
ATOM   3681  C  C   . LEU A  1 482 ? 64.931  59.347 55.109  1.00 16.93 ? 482  LEU A C   1 
ATOM   3682  O  O   . LEU A  1 482 ? 65.455  59.060 56.191  1.00 17.31 ? 482  LEU A O   1 
ATOM   3683  C  CB  . LEU A  1 482 ? 63.718  61.559 55.253  1.00 16.12 ? 482  LEU A CB  1 
ATOM   3684  C  CG  . LEU A  1 482 ? 64.218  62.319 54.016  1.00 16.15 ? 482  LEU A CG  1 
ATOM   3685  C  CD1 . LEU A  1 482 ? 63.142  62.255 52.923  1.00 16.85 ? 482  LEU A CD1 1 
ATOM   3686  C  CD2 . LEU A  1 482 ? 64.532  63.784 54.376  1.00 17.31 ? 482  LEU A CD2 1 
ATOM   3687  N  N   . HIS A  1 483 ? 65.508  59.079 53.940  1.00 16.32 ? 483  HIS A N   1 
ATOM   3688  C  CA  . HIS A  1 483 ? 66.779  58.363 53.847  1.00 15.92 ? 483  HIS A CA  1 
ATOM   3689  C  C   . HIS A  1 483 ? 67.720  58.992 52.824  1.00 16.35 ? 483  HIS A C   1 
ATOM   3690  O  O   . HIS A  1 483 ? 67.254  59.673 51.910  1.00 16.29 ? 483  HIS A O   1 
ATOM   3691  C  CB  . HIS A  1 483 ? 66.508  56.928 53.395  1.00 14.87 ? 483  HIS A CB  1 
ATOM   3692  C  CG  . HIS A  1 483 ? 65.450  56.235 54.189  1.00 15.13 ? 483  HIS A CG  1 
ATOM   3693  N  ND1 . HIS A  1 483 ? 65.736  55.204 55.058  1.00 15.28 ? 483  HIS A ND1 1 
ATOM   3694  C  CD2 . HIS A  1 483 ? 64.114  56.449 54.279  1.00 15.06 ? 483  HIS A CD2 1 
ATOM   3695  C  CE1 . HIS A  1 483 ? 64.623  54.814 55.654  1.00 15.58 ? 483  HIS A CE1 1 
ATOM   3696  N  NE2 . HIS A  1 483 ? 63.624  55.554 55.199  1.00 16.07 ? 483  HIS A NE2 1 
ATOM   3697  N  N   . SER A  1 484 ? 69.028  58.767 52.971  1.00 16.83 ? 484  SER A N   1 
ATOM   3698  C  CA  . SER A  1 484 ? 69.989  59.274 51.982  1.00 20.12 ? 484  SER A CA  1 
ATOM   3699  C  C   . SER A  1 484 ? 70.491  58.043 51.231  1.00 20.04 ? 484  SER A C   1 
ATOM   3700  O  O   . SER A  1 484 ? 70.790  57.015 51.838  1.00 19.55 ? 484  SER A O   1 
ATOM   3701  C  CB  . SER A  1 484 ? 71.169  60.010 52.625  1.00 20.28 ? 484  SER A CB  1 
ATOM   3702  O  OG  . SER A  1 484 ? 71.878  59.148 53.480  1.00 23.72 ? 484  SER A OG  1 
ATOM   3703  N  N   . SER A  1 485 ? 70.583  58.156 49.914  1.00 20.21 ? 485  SER A N   1 
ATOM   3704  C  CA  . SER A  1 485 ? 70.996  57.036 49.089  1.00 21.85 ? 485  SER A CA  1 
ATOM   3705  C  C   . SER A  1 485 ? 72.438  56.587 49.168  1.00 23.12 ? 485  SER A C   1 
ATOM   3706  O  O   . SER A  1 485 ? 72.704  55.392 49.054  1.00 22.00 ? 485  SER A O   1 
ATOM   3707  C  CB  . SER A  1 485 ? 70.676  57.328 47.620  1.00 21.80 ? 485  SER A CB  1 
ATOM   3708  O  OG  . SER A  1 485 ? 69.302  57.628 47.469  1.00 22.40 ? 485  SER A OG  1 
ATOM   3709  N  N   . VAL A  1 486 ? 73.372  57.518 49.359  1.00 24.73 ? 486  VAL A N   1 
ATOM   3710  C  CA  . VAL A  1 486 ? 74.781  57.128 49.355  1.00 26.36 ? 486  VAL A CA  1 
ATOM   3711  C  C   . VAL A  1 486 ? 75.087  55.900 50.218  1.00 27.59 ? 486  VAL A C   1 
ATOM   3712  O  O   . VAL A  1 486 ? 75.750  54.961 49.741  1.00 28.20 ? 486  VAL A O   1 
ATOM   3713  C  CB  . VAL A  1 486 ? 75.705  58.313 49.728  1.00 27.25 ? 486  VAL A CB  1 
ATOM   3714  C  CG1 . VAL A  1 486 ? 75.419  58.795 51.142  1.00 27.24 ? 486  VAL A CG1 1 
ATOM   3715  C  CG2 . VAL A  1 486 ? 77.162  57.882 49.571  1.00 28.04 ? 486  VAL A CG2 1 
ATOM   3716  N  N   . ASN A  1 487 ? 74.624  55.883 51.466  1.00 26.17 ? 487  ASN A N   1 
ATOM   3717  C  CA  . ASN A  1 487 ? 74.843  54.707 52.294  1.00 26.49 ? 487  ASN A CA  1 
ATOM   3718  C  C   . ASN A  1 487 ? 73.537  54.192 52.898  1.00 25.95 ? 487  ASN A C   1 
ATOM   3719  O  O   . ASN A  1 487 ? 73.539  53.457 53.889  1.00 26.12 ? 487  ASN A O   1 
ATOM   3720  C  CB  . ASN A  1 487 ? 75.854  55.003 53.400  1.00 28.91 ? 487  ASN A CB  1 
ATOM   3721  C  CG  . ASN A  1 487 ? 77.263  55.188 52.857  1.00 31.44 ? 487  ASN A CG  1 
ATOM   3722  O  OD1 . ASN A  1 487 ? 77.818  54.289 52.222  1.00 33.19 ? 487  ASN A OD1 1 
ATOM   3723  N  ND2 . ASN A  1 487 ? 77.840  56.359 53.092  1.00 31.29 ? 487  ASN A ND2 1 
ATOM   3724  N  N   . ASP A  1 488 ? 72.426  54.586 52.295  1.00 23.96 ? 488  ASP A N   1 
ATOM   3725  C  CA  . ASP A  1 488 ? 71.118  54.173 52.770  1.00 23.87 ? 488  ASP A CA  1 
ATOM   3726  C  C   . ASP A  1 488 ? 70.898  54.409 54.254  1.00 23.63 ? 488  ASP A C   1 
ATOM   3727  O  O   . ASP A  1 488 ? 70.357  53.556 54.956  1.00 23.40 ? 488  ASP A O   1 
ATOM   3728  C  CB  . ASP A  1 488 ? 70.885  52.707 52.428  1.00 23.39 ? 488  ASP A CB  1 
ATOM   3729  C  CG  . ASP A  1 488 ? 70.801  52.492 50.940  1.00 23.14 ? 488  ASP A CG  1 
ATOM   3730  O  OD1 . ASP A  1 488 ? 71.561  51.667 50.413  1.00 23.91 ? 488  ASP A OD1 1 
ATOM   3731  O  OD2 . ASP A  1 488 ? 69.980  53.179 50.303  1.00 22.42 ? 488  ASP A OD2 1 
ATOM   3732  N  N   . LYS A  1 489 ? 71.309  55.578 54.731  1.00 22.93 ? 489  LYS A N   1 
ATOM   3733  C  CA  . LYS A  1 489 ? 71.105  55.905 56.132  1.00 22.99 ? 489  LYS A CA  1 
ATOM   3734  C  C   . LYS A  1 489 ? 69.652  56.308 56.343  1.00 21.28 ? 489  LYS A C   1 
ATOM   3735  O  O   . LYS A  1 489 ? 69.017  56.872 55.441  1.00 18.38 ? 489  LYS A O   1 
ATOM   3736  C  CB  . LYS A  1 489 ? 72.029  57.048 56.562  1.00 25.20 ? 489  LYS A CB  1 
ATOM   3737  C  CG  . LYS A  1 489 ? 73.490  56.668 56.462  1.00 29.09 ? 489  LYS A CG  1 
ATOM   3738  C  CD  . LYS A  1 489 ? 74.344  57.332 57.524  1.00 32.88 ? 489  LYS A CD  1 
ATOM   3739  C  CE  . LYS A  1 489 ? 74.764  58.719 57.093  1.00 35.54 ? 489  LYS A CE  1 
ATOM   3740  N  NZ  . LYS A  1 489 ? 73.585  59.574 56.779  1.00 36.61 ? 489  LYS A NZ  1 
ATOM   3741  N  N   . GLY A  1 490 ? 69.120  55.960 57.514  1.00 20.34 ? 490  GLY A N   1 
ATOM   3742  C  CA  . GLY A  1 490 ? 67.760  56.335 57.863  1.00 20.15 ? 490  GLY A CA  1 
ATOM   3743  C  C   . GLY A  1 490 ? 67.939  57.640 58.622  1.00 20.78 ? 490  GLY A C   1 
ATOM   3744  O  O   . GLY A  1 490 ? 68.223  57.622 59.831  1.00 20.82 ? 490  GLY A O   1 
ATOM   3745  N  N   . LEU A  1 491 ? 67.792  58.763 57.919  1.00 18.64 ? 491  LEU A N   1 
ATOM   3746  C  CA  . LEU A  1 491 ? 67.976  60.080 58.518  1.00 18.28 ? 491  LEU A CA  1 
ATOM   3747  C  C   . LEU A  1 491 ? 67.039  60.374 59.677  1.00 18.51 ? 491  LEU A C   1 
ATOM   3748  O  O   . LEU A  1 491 ? 67.494  60.612 60.803  1.00 18.50 ? 491  LEU A O   1 
ATOM   3749  C  CB  . LEU A  1 491 ? 67.838  61.178 57.446  1.00 17.51 ? 491  LEU A CB  1 
ATOM   3750  C  CG  . LEU A  1 491 ? 68.743  60.973 56.220  1.00 17.84 ? 491  LEU A CG  1 
ATOM   3751  C  CD1 . LEU A  1 491 ? 68.406  61.973 55.103  1.00 18.48 ? 491  LEU A CD1 1 
ATOM   3752  C  CD2 . LEU A  1 491 ? 70.199  61.135 56.653  1.00 19.04 ? 491  LEU A CD2 1 
ATOM   3753  N  N   . ARG A  1 492 ? 65.736  60.356 59.419  1.00 18.57 ? 492  ARG A N   1 
ATOM   3754  C  CA  . ARG A  1 492 ? 64.787  60.659 60.480  1.00 19.38 ? 492  ARG A CA  1 
ATOM   3755  C  C   . ARG A  1 492 ? 63.369  60.221 60.172  1.00 19.34 ? 492  ARG A C   1 
ATOM   3756  O  O   . ARG A  1 492 ? 63.037  59.874 59.028  1.00 17.55 ? 492  ARG A O   1 
ATOM   3757  C  CB  . ARG A  1 492 ? 64.774  62.170 60.764  1.00 22.32 ? 492  ARG A CB  1 
ATOM   3758  C  CG  . ARG A  1 492 ? 64.207  63.026 59.623  1.00 26.01 ? 492  ARG A CG  1 
ATOM   3759  C  CD  . ARG A  1 492 ? 64.414  64.548 59.862  1.00 29.51 ? 492  ARG A CD  1 
ATOM   3760  N  NE  . ARG A  1 492 ? 65.403  65.098 58.933  1.00 32.34 ? 492  ARG A NE  1 
ATOM   3761  C  CZ  . ARG A  1 492 ? 66.671  64.716 58.913  1.00 33.30 ? 492  ARG A CZ  1 
ATOM   3762  N  NH1 . ARG A  1 492 ? 67.095  63.806 59.779  1.00 37.69 ? 492  ARG A NH1 1 
ATOM   3763  N  NH2 . ARG A  1 492 ? 67.499  65.179 58.004  1.00 32.33 ? 492  ARG A NH2 1 
ATOM   3764  N  N   . VAL A  1 493 ? 62.540  60.248 61.211  1.00 17.23 ? 493  VAL A N   1 
ATOM   3765  C  CA  . VAL A  1 493 ? 61.135  59.894 61.096  1.00 17.43 ? 493  VAL A CA  1 
ATOM   3766  C  C   . VAL A  1 493 ? 60.364  61.181 60.832  1.00 17.19 ? 493  VAL A C   1 
ATOM   3767  O  O   . VAL A  1 493 ? 60.454  62.137 61.617  1.00 18.07 ? 493  VAL A O   1 
ATOM   3768  C  CB  . VAL A  1 493 ? 60.603  59.256 62.393  1.00 17.46 ? 493  VAL A CB  1 
ATOM   3769  C  CG1 . VAL A  1 493 ? 59.087  59.080 62.308  1.00 17.92 ? 493  VAL A CG1 1 
ATOM   3770  C  CG2 . VAL A  1 493 ? 61.288  57.912 62.632  1.00 16.46 ? 493  VAL A CG2 1 
ATOM   3771  N  N   . LEU A  1 494 ? 59.613  61.214 59.735  1.00 15.94 ? 494  LEU A N   1 
ATOM   3772  C  CA  . LEU A  1 494 ? 58.845  62.411 59.380  1.00 15.30 ? 494  LEU A CA  1 
ATOM   3773  C  C   . LEU A  1 494 ? 57.463  62.425 60.034  1.00 15.86 ? 494  LEU A C   1 
ATOM   3774  O  O   . LEU A  1 494 ? 56.983  63.479 60.487  1.00 16.53 ? 494  LEU A O   1 
ATOM   3775  C  CB  . LEU A  1 494 ? 58.718  62.509 57.850  1.00 13.93 ? 494  LEU A CB  1 
ATOM   3776  C  CG  . LEU A  1 494 ? 60.040  62.502 57.045  1.00 13.49 ? 494  LEU A CG  1 
ATOM   3777  C  CD1 . LEU A  1 494 ? 59.753  62.349 55.553  1.00 13.70 ? 494  LEU A CD1 1 
ATOM   3778  C  CD2 . LEU A  1 494 ? 60.804  63.813 57.288  1.00 12.04 ? 494  LEU A CD2 1 
ATOM   3779  N  N   . GLU A  1 495 ? 56.829  61.254 60.100  1.00 15.65 ? 495  GLU A N   1 
ATOM   3780  C  CA  . GLU A  1 495 ? 55.501  61.141 60.708  1.00 15.80 ? 495  GLU A CA  1 
ATOM   3781  C  C   . GLU A  1 495 ? 55.290  59.687 61.097  1.00 15.92 ? 495  GLU A C   1 
ATOM   3782  O  O   . GLU A  1 495 ? 55.425  58.791 60.253  1.00 16.22 ? 495  GLU A O   1 
ATOM   3783  C  CB  . GLU A  1 495 ? 54.429  61.581 59.704  1.00 15.43 ? 495  GLU A CB  1 
ATOM   3784  C  CG  . GLU A  1 495 ? 53.007  61.340 60.153  1.00 16.43 ? 495  GLU A CG  1 
ATOM   3785  C  CD  . GLU A  1 495 ? 52.660  62.083 61.423  1.00 17.21 ? 495  GLU A CD  1 
ATOM   3786  O  OE1 . GLU A  1 495 ? 52.747  63.328 61.427  1.00 20.41 ? 495  GLU A OE1 1 
ATOM   3787  O  OE2 . GLU A  1 495 ? 52.295  61.422 62.411  1.00 18.83 ? 495  GLU A OE2 1 
ATOM   3788  N  N   . ASP A  1 496 ? 54.965  59.442 62.362  1.00 15.34 ? 496  ASP A N   1 
ATOM   3789  C  CA  . ASP A  1 496 ? 54.778  58.071 62.811  1.00 16.21 ? 496  ASP A CA  1 
ATOM   3790  C  C   . ASP A  1 496 ? 53.379  57.761 63.324  1.00 15.79 ? 496  ASP A C   1 
ATOM   3791  O  O   . ASP A  1 496 ? 53.134  56.683 63.864  1.00 16.03 ? 496  ASP A O   1 
ATOM   3792  C  CB  . ASP A  1 496 ? 55.809  57.734 63.903  1.00 16.37 ? 496  ASP A CB  1 
ATOM   3793  C  CG  . ASP A  1 496 ? 55.684  58.634 65.123  1.00 17.67 ? 496  ASP A CG  1 
ATOM   3794  O  OD1 . ASP A  1 496 ? 54.645  59.323 65.259  1.00 17.06 ? 496  ASP A OD1 1 
ATOM   3795  O  OD2 . ASP A  1 496 ? 56.619  58.654 65.957  1.00 18.46 ? 496  ASP A OD2 1 
ATOM   3796  N  N   . ASN A  1 497 ? 52.466  58.713 63.173  1.00 15.98 ? 497  ASN A N   1 
ATOM   3797  C  CA  . ASN A  1 497 ? 51.107  58.526 63.630  1.00 16.32 ? 497  ASN A CA  1 
ATOM   3798  C  C   . ASN A  1 497 ? 50.976  58.123 65.096  1.00 16.72 ? 497  ASN A C   1 
ATOM   3799  O  O   . ASN A  1 497 ? 50.033  57.432 65.470  1.00 14.81 ? 497  ASN A O   1 
ATOM   3800  C  CB  . ASN A  1 497 ? 50.384  57.505 62.727  1.00 15.91 ? 497  ASN A CB  1 
ATOM   3801  C  CG  . ASN A  1 497 ? 49.856  58.143 61.477  1.00 17.42 ? 497  ASN A CG  1 
ATOM   3802  O  OD1 . ASN A  1 497 ? 48.944  58.970 61.534  1.00 19.14 ? 497  ASN A OD1 1 
ATOM   3803  N  ND2 . ASN A  1 497 ? 50.454  57.812 60.337  1.00 16.71 ? 497  ASN A ND2 1 
ATOM   3804  N  N   . SER A  1 498 ? 51.909  58.565 65.936  1.00 17.58 ? 498  SER A N   1 
ATOM   3805  C  CA  . SER A  1 498 ? 51.810  58.207 67.344  1.00 19.07 ? 498  SER A CA  1 
ATOM   3806  C  C   . SER A  1 498 ? 50.511  58.801 67.952  1.00 19.27 ? 498  SER A C   1 
ATOM   3807  O  O   . SER A  1 498 ? 49.914  58.211 68.838  1.00 19.78 ? 498  SER A O   1 
ATOM   3808  C  CB  . SER A  1 498 ? 53.077  58.657 68.110  1.00 19.18 ? 498  SER A CB  1 
ATOM   3809  O  OG  . SER A  1 498 ? 53.368  60.019 67.896  1.00 20.84 ? 498  SER A OG  1 
ATOM   3810  N  N   . ALA A  1 499 ? 50.045  59.941 67.457  1.00 19.82 ? 499  ALA A N   1 
ATOM   3811  C  CA  . ALA A  1 499 ? 48.813  60.505 67.997  1.00 20.15 ? 499  ALA A CA  1 
ATOM   3812  C  C   . ALA A  1 499 ? 47.630  59.555 67.751  1.00 20.73 ? 499  ALA A C   1 
ATOM   3813  O  O   . ALA A  1 499 ? 46.846  59.278 68.662  1.00 21.87 ? 499  ALA A O   1 
ATOM   3814  C  CB  . ALA A  1 499 ? 48.531  61.874 67.380  1.00 20.65 ? 499  ALA A CB  1 
ATOM   3815  N  N   . LEU A  1 500 ? 47.502  59.052 66.527  1.00 19.24 ? 500  LEU A N   1 
ATOM   3816  C  CA  . LEU A  1 500 ? 46.411  58.133 66.204  1.00 18.16 ? 500  LEU A CA  1 
ATOM   3817  C  C   . LEU A  1 500 ? 46.550  56.848 67.017  1.00 18.63 ? 500  LEU A C   1 
ATOM   3818  O  O   . LEU A  1 500 ? 45.558  56.302 67.519  1.00 17.09 ? 500  LEU A O   1 
ATOM   3819  C  CB  . LEU A  1 500 ? 46.413  57.791 64.715  1.00 17.25 ? 500  LEU A CB  1 
ATOM   3820  C  CG  . LEU A  1 500 ? 45.387  56.728 64.305  1.00 17.92 ? 500  LEU A CG  1 
ATOM   3821  C  CD1 . LEU A  1 500 ? 43.982  57.188 64.660  1.00 18.43 ? 500  LEU A CD1 1 
ATOM   3822  C  CD2 . LEU A  1 500 ? 45.510  56.471 62.791  1.00 18.98 ? 500  LEU A CD2 1 
ATOM   3823  N  N   . ASP A  1 501 ? 47.782  56.365 67.142  1.00 19.24 ? 501  ASP A N   1 
ATOM   3824  C  CA  . ASP A  1 501 ? 48.047  55.158 67.915  1.00 21.08 ? 501  ASP A CA  1 
ATOM   3825  C  C   . ASP A  1 501 ? 47.499  55.322 69.346  1.00 22.04 ? 501  ASP A C   1 
ATOM   3826  O  O   . ASP A  1 501 ? 46.832  54.439 69.872  1.00 19.97 ? 501  ASP A O   1 
ATOM   3827  C  CB  . ASP A  1 501 ? 49.556  54.884 67.958  1.00 22.43 ? 501  ASP A CB  1 
ATOM   3828  C  CG  . ASP A  1 501 ? 49.908  53.660 68.803  1.00 25.14 ? 501  ASP A CG  1 
ATOM   3829  O  OD1 . ASP A  1 501 ? 49.528  52.539 68.435  1.00 26.62 ? 501  ASP A OD1 1 
ATOM   3830  O  OD2 . ASP A  1 501 ? 50.560  53.823 69.847  1.00 29.27 ? 501  ASP A OD2 1 
ATOM   3831  N  N   . LYS A  1 502 ? 47.770  56.461 69.975  1.00 24.87 ? 502  LYS A N   1 
ATOM   3832  C  CA  . LYS A  1 502 ? 47.292  56.701 71.337  1.00 27.24 ? 502  LYS A CA  1 
ATOM   3833  C  C   . LYS A  1 502 ? 45.753  56.648 71.384  1.00 27.34 ? 502  LYS A C   1 
ATOM   3834  O  O   . LYS A  1 502 ? 45.171  56.076 72.298  1.00 27.13 ? 502  LYS A O   1 
ATOM   3835  C  CB  . LYS A  1 502 ? 47.796  58.063 71.838  1.00 29.79 ? 502  LYS A CB  1 
ATOM   3836  C  CG  . LYS A  1 502 ? 47.254  58.449 73.220  1.00 34.48 ? 502  LYS A CG  1 
ATOM   3837  C  CD  . LYS A  1 502 ? 47.493  59.931 73.572  1.00 37.13 ? 502  LYS A CD  1 
ATOM   3838  C  CE  . LYS A  1 502 ? 48.938  60.236 73.991  1.00 39.62 ? 502  LYS A CE  1 
ATOM   3839  N  NZ  . LYS A  1 502 ? 49.948  59.998 72.910  1.00 40.99 ? 502  LYS A NZ  1 
ATOM   3840  N  N   . MET A  1 503 ? 45.085  57.226 70.392  1.00 28.10 ? 503  MET A N   1 
ATOM   3841  C  CA  . MET A  1 503 ? 43.623  57.196 70.402  1.00 27.48 ? 503  MET A CA  1 
ATOM   3842  C  C   . MET A  1 503 ? 43.082  55.783 70.224  1.00 26.80 ? 503  MET A C   1 
ATOM   3843  O  O   . MET A  1 503 ? 42.178  55.365 70.949  1.00 25.21 ? 503  MET A O   1 
ATOM   3844  C  CB  . MET A  1 503 ? 43.044  58.094 69.307  1.00 29.81 ? 503  MET A CB  1 
ATOM   3845  C  CG  . MET A  1 503 ? 43.201  59.579 69.537  1.00 31.61 ? 503  MET A CG  1 
ATOM   3846  S  SD  . MET A  1 503 ? 42.526  60.498 68.118  1.00 36.78 ? 503  MET A SD  1 
ATOM   3847  C  CE  . MET A  1 503 ? 40.779  60.411 68.487  1.00 35.15 ? 503  MET A CE  1 
ATOM   3848  N  N   . LEU A  1 504 ? 43.645  55.041 69.273  1.00 25.97 ? 504  LEU A N   1 
ATOM   3849  C  CA  . LEU A  1 504 ? 43.192  53.682 68.997  1.00 25.79 ? 504  LEU A CA  1 
ATOM   3850  C  C   . LEU A  1 504 ? 43.388  52.708 70.147  1.00 26.97 ? 504  LEU A C   1 
ATOM   3851  O  O   . LEU A  1 504 ? 42.810  51.614 70.149  1.00 25.39 ? 504  LEU A O   1 
ATOM   3852  C  CB  . LEU A  1 504 ? 43.874  53.142 67.735  1.00 25.68 ? 504  LEU A CB  1 
ATOM   3853  C  CG  . LEU A  1 504 ? 43.539  53.926 66.461  1.00 25.15 ? 504  LEU A CG  1 
ATOM   3854  C  CD1 . LEU A  1 504 ? 44.176  53.244 65.262  1.00 24.62 ? 504  LEU A CD1 1 
ATOM   3855  C  CD2 . LEU A  1 504 ? 42.016  54.011 66.312  1.00 24.10 ? 504  LEU A CD2 1 
ATOM   3856  N  N   . GLN A  1 505 ? 44.202  53.095 71.126  1.00 28.23 ? 505  GLN A N   1 
ATOM   3857  C  CA  . GLN A  1 505 ? 44.434  52.241 72.291  1.00 30.20 ? 505  GLN A CA  1 
ATOM   3858  C  C   . GLN A  1 505 ? 43.155  52.129 73.131  1.00 29.62 ? 505  GLN A C   1 
ATOM   3859  O  O   . GLN A  1 505 ? 42.975  51.174 73.867  1.00 29.21 ? 505  GLN A O   1 
ATOM   3860  C  CB  . GLN A  1 505 ? 45.573  52.810 73.150  1.00 32.81 ? 505  GLN A CB  1 
ATOM   3861  C  CG  . GLN A  1 505 ? 46.965  52.504 72.596  1.00 36.30 ? 505  GLN A CG  1 
ATOM   3862  C  CD  . GLN A  1 505 ? 48.084  53.193 73.373  1.00 39.81 ? 505  GLN A CD  1 
ATOM   3863  O  OE1 . GLN A  1 505 ? 49.248  53.178 72.950  1.00 42.23 ? 505  GLN A OE1 1 
ATOM   3864  N  NE2 . GLN A  1 505 ? 47.739  53.801 74.512  1.00 40.18 ? 505  GLN A NE2 1 
ATOM   3865  N  N   . ASN A  1 506 ? 42.268  53.111 73.005  1.00 30.10 ? 506  ASN A N   1 
ATOM   3866  C  CA  . ASN A  1 506 ? 41.009  53.111 73.740  1.00 30.64 ? 506  ASN A CA  1 
ATOM   3867  C  C   . ASN A  1 506 ? 39.853  52.553 72.919  1.00 29.11 ? 506  ASN A C   1 
ATOM   3868  O  O   . ASN A  1 506 ? 38.688  52.735 73.275  1.00 28.63 ? 506  ASN A O   1 
ATOM   3869  C  CB  . ASN A  1 506 ? 40.670  54.534 74.191  1.00 32.98 ? 506  ASN A CB  1 
ATOM   3870  C  CG  . ASN A  1 506 ? 41.698  55.086 75.151  1.00 36.12 ? 506  ASN A CG  1 
ATOM   3871  O  OD1 . ASN A  1 506 ? 42.020  54.446 76.161  1.00 37.95 ? 506  ASN A OD1 1 
ATOM   3872  N  ND2 . ASN A  1 506 ? 42.237  56.270 74.840  1.00 36.80 ? 506  ASN A ND2 1 
ATOM   3873  N  N   . VAL A  1 507 ? 40.168  51.864 71.824  1.00 27.33 ? 507  VAL A N   1 
ATOM   3874  C  CA  . VAL A  1 507 ? 39.128  51.312 70.966  1.00 24.24 ? 507  VAL A CA  1 
ATOM   3875  C  C   . VAL A  1 507 ? 39.351  49.827 70.721  1.00 24.47 ? 507  VAL A C   1 
ATOM   3876  O  O   . VAL A  1 507 ? 40.489  49.371 70.587  1.00 23.15 ? 507  VAL A O   1 
ATOM   3877  C  CB  . VAL A  1 507 ? 39.089  52.058 69.594  1.00 23.91 ? 507  VAL A CB  1 
ATOM   3878  C  CG1 . VAL A  1 507 ? 37.944  51.545 68.738  1.00 22.54 ? 507  VAL A CG1 1 
ATOM   3879  C  CG2 . VAL A  1 507 ? 38.931  53.544 69.818  1.00 22.87 ? 507  VAL A CG2 1 
ATOM   3880  N  N   . GLN A  1 508 ? 38.268  49.057 70.686  1.00 23.80 ? 508  GLN A N   1 
ATOM   3881  C  CA  . GLN A  1 508 ? 38.394  47.629 70.414  1.00 24.06 ? 508  GLN A CA  1 
ATOM   3882  C  C   . GLN A  1 508 ? 38.506  47.459 68.901  1.00 23.47 ? 508  GLN A C   1 
ATOM   3883  O  O   . GLN A  1 508 ? 37.508  47.264 68.220  1.00 23.80 ? 508  GLN A O   1 
ATOM   3884  C  CB  . GLN A  1 508 ? 37.168  46.875 70.916  1.00 25.27 ? 508  GLN A CB  1 
ATOM   3885  C  CG  . GLN A  1 508 ? 37.013  46.873 72.421  1.00 27.45 ? 508  GLN A CG  1 
ATOM   3886  C  CD  . GLN A  1 508 ? 35.828  46.048 72.851  1.00 29.00 ? 508  GLN A CD  1 
ATOM   3887  O  OE1 . GLN A  1 508 ? 35.783  44.841 72.606  1.00 30.18 ? 508  GLN A OE1 1 
ATOM   3888  N  NE2 . GLN A  1 508 ? 34.843  46.697 73.476  1.00 30.08 ? 508  GLN A NE2 1 
ATOM   3889  N  N   . MET A  1 509 ? 39.728  47.515 68.391  1.00 22.84 ? 509  MET A N   1 
ATOM   3890  C  CA  . MET A  1 509 ? 39.970  47.410 66.964  1.00 23.35 ? 509  MET A CA  1 
ATOM   3891  C  C   . MET A  1 509 ? 40.042  45.975 66.468  1.00 23.13 ? 509  MET A C   1 
ATOM   3892  O  O   . MET A  1 509 ? 40.434  45.072 67.208  1.00 23.08 ? 509  MET A O   1 
ATOM   3893  C  CB  . MET A  1 509 ? 41.270  48.139 66.605  1.00 22.80 ? 509  MET A CB  1 
ATOM   3894  C  CG  . MET A  1 509 ? 41.233  49.638 66.878  1.00 24.36 ? 509  MET A CG  1 
ATOM   3895  S  SD  . MET A  1 509 ? 39.976  50.485 65.856  1.00 25.33 ? 509  MET A SD  1 
ATOM   3896  C  CE  . MET A  1 509 ? 40.871  50.553 64.282  1.00 24.95 ? 509  MET A CE  1 
ATOM   3897  N  N   . PRO A  1 510 ? 39.655  45.743 65.197  1.00 21.96 ? 510  PRO A N   1 
ATOM   3898  C  CA  . PRO A  1 510 ? 39.706  44.393 64.641  1.00 21.80 ? 510  PRO A CA  1 
ATOM   3899  C  C   . PRO A  1 510 ? 41.139  44.107 64.253  1.00 22.17 ? 510  PRO A C   1 
ATOM   3900  O  O   . PRO A  1 510 ? 41.967  45.017 64.236  1.00 22.51 ? 510  PRO A O   1 
ATOM   3901  C  CB  . PRO A  1 510 ? 38.813  44.493 63.408  1.00 22.03 ? 510  PRO A CB  1 
ATOM   3902  C  CG  . PRO A  1 510 ? 39.080  45.888 62.928  1.00 22.62 ? 510  PRO A CG  1 
ATOM   3903  C  CD  . PRO A  1 510 ? 39.069  46.690 64.229  1.00 22.77 ? 510  PRO A CD  1 
ATOM   3904  N  N   . SER A  1 511 ? 41.419  42.848 63.941  1.00 21.90 ? 511  SER A N   1 
ATOM   3905  C  CA  . SER A  1 511 ? 42.741  42.438 63.492  1.00 23.41 ? 511  SER A CA  1 
ATOM   3906  C  C   . SER A  1 511 ? 42.610  41.963 62.046  1.00 23.75 ? 511  SER A C   1 
ATOM   3907  O  O   . SER A  1 511 ? 41.501  41.776 61.539  1.00 24.07 ? 511  SER A O   1 
ATOM   3908  C  CB  . SER A  1 511 ? 43.280  41.300 64.357  1.00 22.82 ? 511  SER A CB  1 
ATOM   3909  O  OG  . SER A  1 511 ? 42.382  40.208 64.357  1.00 24.78 ? 511  SER A OG  1 
ATOM   3910  N  N   . LYS A  1 512 ? 43.741  41.772 61.382  1.00 24.41 ? 512  LYS A N   1 
ATOM   3911  C  CA  . LYS A  1 512 ? 43.719  41.321 60.008  1.00 24.78 ? 512  LYS A CA  1 
ATOM   3912  C  C   . LYS A  1 512 ? 44.582  40.090 59.842  1.00 25.50 ? 512  LYS A C   1 
ATOM   3913  O  O   . LYS A  1 512 ? 45.756  40.081 60.189  1.00 26.27 ? 512  LYS A O   1 
ATOM   3914  C  CB  . LYS A  1 512 ? 44.200  42.433 59.086  1.00 24.22 ? 512  LYS A CB  1 
ATOM   3915  C  CG  . LYS A  1 512 ? 44.262  42.066 57.625  1.00 25.04 ? 512  LYS A CG  1 
ATOM   3916  C  CD  . LYS A  1 512 ? 44.328  43.348 56.812  1.00 23.80 ? 512  LYS A CD  1 
ATOM   3917  C  CE  . LYS A  1 512 ? 44.743  43.104 55.416  1.00 23.09 ? 512  LYS A CE  1 
ATOM   3918  N  NZ  . LYS A  1 512 ? 45.043  44.409 54.750  1.00 22.98 ? 512  LYS A NZ  1 
ATOM   3919  N  N   . LYS A  1 513 ? 43.979  39.029 59.336  1.00 25.61 ? 513  LYS A N   1 
ATOM   3920  C  CA  . LYS A  1 513 ? 44.714  37.809 59.106  1.00 25.55 ? 513  LYS A CA  1 
ATOM   3921  C  C   . LYS A  1 513 ? 44.902  37.700 57.602  1.00 24.89 ? 513  LYS A C   1 
ATOM   3922  O  O   . LYS A  1 513 ? 43.946  37.824 56.850  1.00 22.65 ? 513  LYS A O   1 
ATOM   3923  C  CB  . LYS A  1 513 ? 43.915  36.617 59.614  1.00 27.14 ? 513  LYS A CB  1 
ATOM   3924  C  CG  . LYS A  1 513 ? 44.551  35.276 59.285  1.00 29.98 ? 513  LYS A CG  1 
ATOM   3925  C  CD  . LYS A  1 513 ? 43.563  34.133 59.522  1.00 32.46 ? 513  LYS A CD  1 
ATOM   3926  C  CE  . LYS A  1 513 ? 44.177  32.794 59.167  1.00 35.33 ? 513  LYS A CE  1 
ATOM   3927  N  NZ  . LYS A  1 513 ? 43.143  31.707 59.126  1.00 38.47 ? 513  LYS A NZ  1 
ATOM   3928  N  N   . LEU A  1 514 ? 46.141  37.504 57.172  1.00 23.95 ? 514  LEU A N   1 
ATOM   3929  C  CA  . LEU A  1 514 ? 46.450  37.352 55.760  1.00 25.57 ? 514  LEU A CA  1 
ATOM   3930  C  C   . LEU A  1 514 ? 47.001  35.934 55.643  1.00 25.73 ? 514  LEU A C   1 
ATOM   3931  O  O   . LEU A  1 514 ? 47.969  35.595 56.313  1.00 25.80 ? 514  LEU A O   1 
ATOM   3932  C  CB  . LEU A  1 514 ? 47.503  38.379 55.340  1.00 25.50 ? 514  LEU A CB  1 
ATOM   3933  C  CG  . LEU A  1 514 ? 48.096  38.259 53.941  1.00 26.43 ? 514  LEU A CG  1 
ATOM   3934  C  CD1 . LEU A  1 514 ? 47.089  38.693 52.887  1.00 25.91 ? 514  LEU A CD1 1 
ATOM   3935  C  CD2 . LEU A  1 514 ? 49.345  39.140 53.869  1.00 28.10 ? 514  LEU A CD2 1 
ATOM   3936  N  N   . ASP A  1 515 ? 46.382  35.104 54.807  1.00 26.56 ? 515  ASP A N   1 
ATOM   3937  C  CA  . ASP A  1 515 ? 46.815  33.717 54.654  1.00 27.34 ? 515  ASP A CA  1 
ATOM   3938  C  C   . ASP A  1 515 ? 46.468  33.228 53.242  1.00 27.99 ? 515  ASP A C   1 
ATOM   3939  O  O   . ASP A  1 515 ? 46.055  34.024 52.395  1.00 26.63 ? 515  ASP A O   1 
ATOM   3940  C  CB  . ASP A  1 515 ? 46.093  32.850 55.686  1.00 28.60 ? 515  ASP A CB  1 
ATOM   3941  C  CG  . ASP A  1 515 ? 46.974  31.744 56.239  1.00 31.49 ? 515  ASP A CG  1 
ATOM   3942  O  OD1 . ASP A  1 515 ? 47.790  31.178 55.477  1.00 31.49 ? 515  ASP A OD1 1 
ATOM   3943  O  OD2 . ASP A  1 515 ? 46.836  31.431 57.437  1.00 32.80 ? 515  ASP A OD2 1 
ATOM   3944  N  N   . PHE A  1 516 ? 46.617  31.925 52.992  1.00 27.96 ? 516  PHE A N   1 
ATOM   3945  C  CA  . PHE A  1 516 ? 46.301  31.374 51.677  1.00 28.48 ? 516  PHE A CA  1 
ATOM   3946  C  C   . PHE A  1 516 ? 45.643  29.999 51.712  1.00 28.92 ? 516  PHE A C   1 
ATOM   3947  O  O   . PHE A  1 516 ? 45.704  29.297 52.722  1.00 28.37 ? 516  PHE A O   1 
ATOM   3948  C  CB  . PHE A  1 516 ? 47.567  31.282 50.823  1.00 29.03 ? 516  PHE A CB  1 
ATOM   3949  C  CG  . PHE A  1 516 ? 48.583  30.287 51.333  1.00 31.26 ? 516  PHE A CG  1 
ATOM   3950  C  CD1 . PHE A  1 516 ? 49.571  30.676 52.236  1.00 31.63 ? 516  PHE A CD1 1 
ATOM   3951  C  CD2 . PHE A  1 516 ? 48.552  28.957 50.912  1.00 31.51 ? 516  PHE A CD2 1 
ATOM   3952  C  CE1 . PHE A  1 516 ? 50.517  29.757 52.711  1.00 32.03 ? 516  PHE A CE1 1 
ATOM   3953  C  CE2 . PHE A  1 516 ? 49.492  28.031 51.382  1.00 31.61 ? 516  PHE A CE2 1 
ATOM   3954  C  CZ  . PHE A  1 516 ? 50.477  28.435 52.283  1.00 31.86 ? 516  PHE A CZ  1 
ATOM   3955  N  N   . ILE A  1 517 ? 44.993  29.636 50.609  1.00 28.55 ? 517  ILE A N   1 
ATOM   3956  C  CA  . ILE A  1 517 ? 44.389  28.323 50.481  1.00 30.04 ? 517  ILE A CA  1 
ATOM   3957  C  C   . ILE A  1 517 ? 44.956  27.764 49.194  1.00 31.64 ? 517  ILE A C   1 
ATOM   3958  O  O   . ILE A  1 517 ? 45.417  28.514 48.334  1.00 31.22 ? 517  ILE A O   1 
ATOM   3959  C  CB  . ILE A  1 517 ? 42.846  28.354 50.391  1.00 29.92 ? 517  ILE A CB  1 
ATOM   3960  C  CG1 . ILE A  1 517 ? 42.389  29.328 49.312  1.00 30.20 ? 517  ILE A CG1 1 
ATOM   3961  C  CG2 . ILE A  1 517 ? 42.261  28.706 51.754  1.00 29.71 ? 517  ILE A CG2 1 
ATOM   3962  C  CD1 . ILE A  1 517 ? 40.868  29.573 49.315  1.00 31.25 ? 517  ILE A CD1 1 
ATOM   3963  N  N   . ILE A  1 518 ? 44.945  26.446 49.058  1.00 33.59 ? 518  ILE A N   1 
ATOM   3964  C  CA  . ILE A  1 518 ? 45.491  25.837 47.857  1.00 35.51 ? 518  ILE A CA  1 
ATOM   3965  C  C   . ILE A  1 518 ? 44.392  25.302 46.969  1.00 36.66 ? 518  ILE A C   1 
ATOM   3966  O  O   . ILE A  1 518 ? 43.537  24.547 47.416  1.00 37.76 ? 518  ILE A O   1 
ATOM   3967  C  CB  . ILE A  1 518 ? 46.451  24.683 48.200  1.00 36.17 ? 518  ILE A CB  1 
ATOM   3968  C  CG1 . ILE A  1 518 ? 47.643  25.215 48.993  1.00 36.39 ? 518  ILE A CG1 1 
ATOM   3969  C  CG2 . ILE A  1 518 ? 46.946  24.014 46.916  1.00 36.21 ? 518  ILE A CG2 1 
ATOM   3970  C  CD1 . ILE A  1 518 ? 48.677  24.144 49.331  1.00 37.48 ? 518  ILE A CD1 1 
ATOM   3971  N  N   . LEU A  1 519 ? 44.397  25.722 45.712  1.00 37.34 ? 519  LEU A N   1 
ATOM   3972  C  CA  . LEU A  1 519 ? 43.412  25.239 44.758  1.00 37.80 ? 519  LEU A CA  1 
ATOM   3973  C  C   . LEU A  1 519 ? 44.203  24.704 43.575  1.00 38.99 ? 519  LEU A C   1 
ATOM   3974  O  O   . LEU A  1 519 ? 44.857  25.477 42.868  1.00 38.11 ? 519  LEU A O   1 
ATOM   3975  C  CB  . LEU A  1 519 ? 42.484  26.366 44.294  1.00 36.81 ? 519  LEU A CB  1 
ATOM   3976  C  CG  . LEU A  1 519 ? 41.566  27.011 45.327  1.00 36.73 ? 519  LEU A CG  1 
ATOM   3977  C  CD1 . LEU A  1 519 ? 40.669  28.047 44.638  1.00 34.74 ? 519  LEU A CD1 1 
ATOM   3978  C  CD2 . LEU A  1 519 ? 40.726  25.922 46.002  1.00 36.46 ? 519  LEU A CD2 1 
ATOM   3979  N  N   . ASN A  1 520 ? 44.178  23.379 43.394  1.00 40.27 ? 520  ASN A N   1 
ATOM   3980  C  CA  . ASN A  1 520 ? 44.871  22.736 42.289  1.00 41.01 ? 520  ASN A CA  1 
ATOM   3981  C  C   . ASN A  1 520 ? 46.353  23.038 42.234  1.00 40.69 ? 520  ASN A C   1 
ATOM   3982  O  O   . ASN A  1 520 ? 46.855  23.557 41.233  1.00 41.00 ? 520  ASN A O   1 
ATOM   3983  C  CB  . ASN A  1 520 ? 44.239  23.164 40.975  1.00 44.12 ? 520  ASN A CB  1 
ATOM   3984  C  CG  . ASN A  1 520 ? 43.692  21.998 40.193  1.00 47.88 ? 520  ASN A CG  1 
ATOM   3985  O  OD1 . ASN A  1 520 ? 43.025  21.116 40.760  1.00 49.00 ? 520  ASN A OD1 1 
ATOM   3986  N  ND2 . ASN A  1 520 ? 43.951  21.999 38.885  1.00 50.72 ? 520  ASN A ND2 1 
ATOM   3987  N  N   . GLU A  1 521 ? 47.055  22.696 43.305  1.00 40.36 ? 521  GLU A N   1 
ATOM   3988  C  CA  . GLU A  1 521 ? 48.493  22.924 43.390  1.00 39.79 ? 521  GLU A CA  1 
ATOM   3989  C  C   . GLU A  1 521 ? 48.863  24.402 43.403  1.00 37.54 ? 521  GLU A C   1 
ATOM   3990  O  O   . GLU A  1 521 ? 50.048  24.737 43.460  1.00 37.38 ? 521  GLU A O   1 
ATOM   3991  C  CB  . GLU A  1 521 ? 49.238  22.234 42.228  1.00 42.20 ? 521  GLU A CB  1 
ATOM   3992  C  CG  . GLU A  1 521 ? 49.376  20.705 42.334  1.00 45.54 ? 521  GLU A CG  1 
ATOM   3993  C  CD  . GLU A  1 521 ? 48.051  19.979 42.204  1.00 48.07 ? 521  GLU A CD  1 
ATOM   3994  O  OE1 . GLU A  1 521 ? 47.283  20.294 41.261  1.00 48.47 ? 521  GLU A OE1 1 
ATOM   3995  O  OE2 . GLU A  1 521 ? 47.775  19.077 43.035  1.00 49.83 ? 521  GLU A OE2 1 
ATOM   3996  N  N   . THR A  1 522 ? 47.877  25.295 43.343  1.00 34.93 ? 522  THR A N   1 
ATOM   3997  C  CA  . THR A  1 522 ? 48.212  26.721 43.368  1.00 31.97 ? 522  THR A CA  1 
ATOM   3998  C  C   . THR A  1 522 ? 47.726  27.401 44.627  1.00 29.92 ? 522  THR A C   1 
ATOM   3999  O  O   . THR A  1 522 ? 46.609  27.171 45.079  1.00 27.84 ? 522  THR A O   1 
ATOM   4000  C  CB  . THR A  1 522 ? 47.634  27.474 42.160  1.00 32.22 ? 522  THR A CB  1 
ATOM   4001  O  OG1 . THR A  1 522 ? 48.193  26.934 40.960  1.00 33.22 ? 522  THR A OG1 1 
ATOM   4002  C  CG2 . THR A  1 522 ? 47.987  28.954 42.231  1.00 31.20 ? 522  THR A CG2 1 
ATOM   4003  N  N   . LYS A  1 523 ? 48.572  28.232 45.219  1.00 28.31 ? 523  LYS A N   1 
ATOM   4004  C  CA  . LYS A  1 523 ? 48.126  28.932 46.402  1.00 28.17 ? 523  LYS A CA  1 
ATOM   4005  C  C   . LYS A  1 523 ? 47.476  30.249 45.993  1.00 25.86 ? 523  LYS A C   1 
ATOM   4006  O  O   . LYS A  1 523 ? 47.950  30.931 45.091  1.00 25.70 ? 523  LYS A O   1 
ATOM   4007  C  CB  . LYS A  1 523 ? 49.283  29.171 47.373  1.00 30.81 ? 523  LYS A CB  1 
ATOM   4008  C  CG  . LYS A  1 523 ? 50.509  29.765 46.760  1.00 34.83 ? 523  LYS A CG  1 
ATOM   4009  C  CD  . LYS A  1 523 ? 51.726  29.494 47.646  1.00 37.14 ? 523  LYS A CD  1 
ATOM   4010  C  CE  . LYS A  1 523 ? 51.587  30.152 49.004  1.00 38.68 ? 523  LYS A CE  1 
ATOM   4011  N  NZ  . LYS A  1 523 ? 52.897  30.108 49.733  1.00 41.02 ? 523  LYS A NZ  1 
ATOM   4012  N  N   . PHE A  1 524 ? 46.368  30.572 46.647  1.00 23.29 ? 524  PHE A N   1 
ATOM   4013  C  CA  . PHE A  1 524 ? 45.633  31.813 46.399  1.00 20.92 ? 524  PHE A CA  1 
ATOM   4014  C  C   . PHE A  1 524 ? 45.467  32.447 47.772  1.00 20.07 ? 524  PHE A C   1 
ATOM   4015  O  O   . PHE A  1 524 ? 45.075  31.770 48.727  1.00 18.60 ? 524  PHE A O   1 
ATOM   4016  C  CB  . PHE A  1 524 ? 44.273  31.529 45.756  1.00 19.11 ? 524  PHE A CB  1 
ATOM   4017  C  CG  . PHE A  1 524 ? 44.376  31.019 44.340  1.00 20.71 ? 524  PHE A CG  1 
ATOM   4018  C  CD1 . PHE A  1 524 ? 44.402  29.647 44.076  1.00 20.31 ? 524  PHE A CD1 1 
ATOM   4019  C  CD2 . PHE A  1 524 ? 44.509  31.914 43.271  1.00 20.20 ? 524  PHE A CD2 1 
ATOM   4020  C  CE1 . PHE A  1 524 ? 44.564  29.171 42.762  1.00 22.12 ? 524  PHE A CE1 1 
ATOM   4021  C  CE2 . PHE A  1 524 ? 44.670  31.457 41.959  1.00 21.79 ? 524  PHE A CE2 1 
ATOM   4022  C  CZ  . PHE A  1 524 ? 44.700  30.079 41.696  1.00 21.60 ? 524  PHE A CZ  1 
ATOM   4023  N  N   . TRP A  1 525 ? 45.785  33.736 47.853  1.00 17.85 ? 525  TRP A N   1 
ATOM   4024  C  CA  . TRP A  1 525 ? 45.743  34.494 49.099  1.00 17.69 ? 525  TRP A CA  1 
ATOM   4025  C  C   . TRP A  1 525 ? 44.412  35.144 49.443  1.00 17.11 ? 525  TRP A C   1 
ATOM   4026  O  O   . TRP A  1 525 ? 43.623  35.518 48.564  1.00 16.04 ? 525  TRP A O   1 
ATOM   4027  C  CB  . TRP A  1 525 ? 46.831  35.594 49.084  1.00 17.25 ? 525  TRP A CB  1 
ATOM   4028  C  CG  . TRP A  1 525 ? 48.226  35.057 49.017  1.00 18.70 ? 525  TRP A CG  1 
ATOM   4029  C  CD1 . TRP A  1 525 ? 48.846  34.488 47.938  1.00 18.34 ? 525  TRP A CD1 1 
ATOM   4030  C  CD2 . TRP A  1 525 ? 49.130  34.924 50.117  1.00 19.03 ? 525  TRP A CD2 1 
ATOM   4031  N  NE1 . TRP A  1 525 ? 50.077  33.994 48.310  1.00 18.49 ? 525  TRP A NE1 1 
ATOM   4032  C  CE2 . TRP A  1 525 ? 50.275  34.253 49.642  1.00 19.08 ? 525  TRP A CE2 1 
ATOM   4033  C  CE3 . TRP A  1 525 ? 49.078  35.307 51.461  1.00 19.95 ? 525  TRP A CE3 1 
ATOM   4034  C  CZ2 . TRP A  1 525 ? 51.365  33.956 50.466  1.00 19.68 ? 525  TRP A CZ2 1 
ATOM   4035  C  CZ3 . TRP A  1 525 ? 50.166  35.011 52.281  1.00 20.91 ? 525  TRP A CZ3 1 
ATOM   4036  C  CH2 . TRP A  1 525 ? 51.290  34.343 51.777  1.00 20.31 ? 525  TRP A CH2 1 
ATOM   4037  N  N   . TYR A  1 526 ? 44.189  35.304 50.740  1.00 16.21 ? 526  TYR A N   1 
ATOM   4038  C  CA  . TYR A  1 526 ? 42.990  35.957 51.228  1.00 17.08 ? 526  TYR A CA  1 
ATOM   4039  C  C   . TYR A  1 526 ? 43.315  36.687 52.520  1.00 15.74 ? 526  TYR A C   1 
ATOM   4040  O  O   . TYR A  1 526 ? 44.354  36.461 53.135  1.00 15.74 ? 526  TYR A O   1 
ATOM   4041  C  CB  . TYR A  1 526 ? 41.871  34.942 51.488  1.00 18.65 ? 526  TYR A CB  1 
ATOM   4042  C  CG  . TYR A  1 526 ? 42.129  34.029 52.662  1.00 21.61 ? 526  TYR A CG  1 
ATOM   4043  C  CD1 . TYR A  1 526 ? 41.741  34.378 53.951  1.00 22.29 ? 526  TYR A CD1 1 
ATOM   4044  C  CD2 . TYR A  1 526 ? 42.752  32.800 52.474  1.00 23.89 ? 526  TYR A CD2 1 
ATOM   4045  C  CE1 . TYR A  1 526 ? 41.964  33.511 55.033  1.00 24.86 ? 526  TYR A CE1 1 
ATOM   4046  C  CE2 . TYR A  1 526 ? 42.979  31.928 53.536  1.00 25.66 ? 526  TYR A CE2 1 
ATOM   4047  C  CZ  . TYR A  1 526 ? 42.581  32.285 54.813  1.00 26.52 ? 526  TYR A CZ  1 
ATOM   4048  O  OH  . TYR A  1 526 ? 42.777  31.388 55.847  1.00 29.23 ? 526  TYR A OH  1 
ATOM   4049  N  N   . GLN A  1 527 ? 42.425  37.586 52.906  1.00 14.77 ? 527  GLN A N   1 
ATOM   4050  C  CA  . GLN A  1 527 ? 42.598  38.310 54.140  1.00 14.95 ? 527  GLN A CA  1 
ATOM   4051  C  C   . GLN A  1 527 ? 41.258  38.290 54.811  1.00 15.08 ? 527  GLN A C   1 
ATOM   4052  O  O   . GLN A  1 527 ? 40.220  38.210 54.149  1.00 14.82 ? 527  GLN A O   1 
ATOM   4053  C  CB  . GLN A  1 527 ? 43.029  39.764 53.903  1.00 14.11 ? 527  GLN A CB  1 
ATOM   4054  C  CG  . GLN A  1 527 ? 42.033  40.638 53.158  1.00 14.26 ? 527  GLN A CG  1 
ATOM   4055  C  CD  . GLN A  1 527 ? 42.474  42.095 53.156  1.00 16.20 ? 527  GLN A CD  1 
ATOM   4056  O  OE1 . GLN A  1 527 ? 43.650  42.405 52.884  1.00 15.03 ? 527  GLN A OE1 1 
ATOM   4057  N  NE2 . GLN A  1 527 ? 41.536  43.000 53.455  1.00 14.46 ? 527  GLN A NE2 1 
ATOM   4058  N  N   . MET A  1 528 ? 41.276  38.333 56.130  1.00 15.98 ? 528  MET A N   1 
ATOM   4059  C  CA  . MET A  1 528 ? 40.035  38.388 56.882  1.00 17.34 ? 528  MET A CA  1 
ATOM   4060  C  C   . MET A  1 528 ? 40.186  39.492 57.903  1.00 18.07 ? 528  MET A C   1 
ATOM   4061  O  O   . MET A  1 528 ? 41.216  39.582 58.576  1.00 18.03 ? 528  MET A O   1 
ATOM   4062  C  CB  . MET A  1 528 ? 39.771  37.076 57.626  1.00 18.18 ? 528  MET A CB  1 
ATOM   4063  C  CG  . MET A  1 528 ? 39.267  35.940 56.760  1.00 19.98 ? 528  MET A CG  1 
ATOM   4064  S  SD  . MET A  1 528 ? 38.804  34.509 57.792  1.00 22.76 ? 528  MET A SD  1 
ATOM   4065  C  CE  . MET A  1 528 ? 40.383  33.724 57.976  1.00 26.10 ? 528  MET A CE  1 
ATOM   4066  N  N   . ILE A  1 529 ? 39.190  40.358 57.986  1.00 17.54 ? 529  ILE A N   1 
ATOM   4067  C  CA  . ILE A  1 529 ? 39.203  41.394 58.994  1.00 17.39 ? 529  ILE A CA  1 
ATOM   4068  C  C   . ILE A  1 529 ? 38.425  40.714 60.119  1.00 18.57 ? 529  ILE A C   1 
ATOM   4069  O  O   . ILE A  1 529 ? 37.215  40.482 60.004  1.00 18.02 ? 529  ILE A O   1 
ATOM   4070  C  CB  . ILE A  1 529 ? 38.470  42.661 58.521  1.00 16.69 ? 529  ILE A CB  1 
ATOM   4071  C  CG1 . ILE A  1 529 ? 39.153  43.205 57.249  1.00 16.16 ? 529  ILE A CG1 1 
ATOM   4072  C  CG2 . ILE A  1 529 ? 38.476  43.708 59.642  1.00 14.42 ? 529  ILE A CG2 1 
ATOM   4073  C  CD1 . ILE A  1 529 ? 40.628  43.501 57.432  1.00 16.19 ? 529  ILE A CD1 1 
ATOM   4074  N  N   . LEU A  1 530 ? 39.137  40.362 61.184  1.00 20.26 ? 530  LEU A N   1 
ATOM   4075  C  CA  . LEU A  1 530 ? 38.556  39.647 62.325  1.00 20.62 ? 530  LEU A CA  1 
ATOM   4076  C  C   . LEU A  1 530 ? 38.105  40.546 63.459  1.00 21.00 ? 530  LEU A C   1 
ATOM   4077  O  O   . LEU A  1 530 ? 38.802  41.496 63.824  1.00 21.22 ? 530  LEU A O   1 
ATOM   4078  C  CB  . LEU A  1 530 ? 39.580  38.643 62.869  1.00 20.41 ? 530  LEU A CB  1 
ATOM   4079  C  CG  . LEU A  1 530 ? 40.092  37.615 61.857  1.00 20.98 ? 530  LEU A CG  1 
ATOM   4080  C  CD1 . LEU A  1 530 ? 41.288  36.835 62.440  1.00 21.31 ? 530  LEU A CD1 1 
ATOM   4081  C  CD2 . LEU A  1 530 ? 38.946  36.686 61.495  1.00 18.80 ? 530  LEU A CD2 1 
ATOM   4082  N  N   . PRO A  1 531 ? 36.929  40.257 64.040  1.00 21.54 ? 531  PRO A N   1 
ATOM   4083  C  CA  . PRO A  1 531 ? 36.398  41.051 65.151  1.00 21.51 ? 531  PRO A CA  1 
ATOM   4084  C  C   . PRO A  1 531 ? 37.324  41.056 66.382  1.00 22.46 ? 531  PRO A C   1 
ATOM   4085  O  O   . PRO A  1 531 ? 38.175  40.178 66.543  1.00 20.05 ? 531  PRO A O   1 
ATOM   4086  C  CB  . PRO A  1 531 ? 35.078  40.354 65.475  1.00 22.08 ? 531  PRO A CB  1 
ATOM   4087  C  CG  . PRO A  1 531 ? 34.626  39.848 64.110  1.00 21.49 ? 531  PRO A CG  1 
ATOM   4088  C  CD  . PRO A  1 531 ? 35.924  39.293 63.546  1.00 21.43 ? 531  PRO A CD  1 
ATOM   4089  N  N   . PRO A  1 532 ? 37.175  42.068 67.251  1.00 23.57 ? 532  PRO A N   1 
ATOM   4090  C  CA  . PRO A  1 532 ? 37.999  42.147 68.469  1.00 25.53 ? 532  PRO A CA  1 
ATOM   4091  C  C   . PRO A  1 532 ? 37.815  40.839 69.265  1.00 26.66 ? 532  PRO A C   1 
ATOM   4092  O  O   . PRO A  1 532 ? 36.766  40.197 69.180  1.00 26.96 ? 532  PRO A O   1 
ATOM   4093  C  CB  . PRO A  1 532 ? 37.395  43.335 69.221  1.00 25.29 ? 532  PRO A CB  1 
ATOM   4094  C  CG  . PRO A  1 532 ? 36.895  44.224 68.129  1.00 24.90 ? 532  PRO A CG  1 
ATOM   4095  C  CD  . PRO A  1 532 ? 36.301  43.251 67.116  1.00 24.06 ? 532  PRO A CD  1 
ATOM   4096  N  N   . HIS A  1 533 ? 38.829  40.439 70.020  1.00 28.33 ? 533  HIS A N   1 
ATOM   4097  C  CA  . HIS A  1 533 ? 38.746  39.225 70.839  1.00 29.45 ? 533  HIS A CA  1 
ATOM   4098  C  C   . HIS A  1 533 ? 38.208  38.038 70.057  1.00 29.78 ? 533  HIS A C   1 
ATOM   4099  O  O   . HIS A  1 533 ? 37.410  37.252 70.577  1.00 29.65 ? 533  HIS A O   1 
ATOM   4100  C  CB  . HIS A  1 533 ? 37.840  39.472 72.047  1.00 30.40 ? 533  HIS A CB  1 
ATOM   4101  C  CG  . HIS A  1 533 ? 38.012  40.827 72.658  1.00 31.97 ? 533  HIS A CG  1 
ATOM   4102  N  ND1 . HIS A  1 533 ? 39.182  41.229 73.270  1.00 33.21 ? 533  HIS A ND1 1 
ATOM   4103  C  CD2 . HIS A  1 533 ? 37.167  41.883 72.730  1.00 32.36 ? 533  HIS A CD2 1 
ATOM   4104  C  CE1 . HIS A  1 533 ? 39.050  42.474 73.695  1.00 33.39 ? 533  HIS A CE1 1 
ATOM   4105  N  NE2 . HIS A  1 533 ? 37.837  42.895 73.380  1.00 33.97 ? 533  HIS A NE2 1 
ATOM   4106  N  N   . PHE A  1 534 ? 38.647  37.901 68.813  1.00 30.10 ? 534  PHE A N   1 
ATOM   4107  C  CA  . PHE A  1 534 ? 38.193  36.801 67.969  1.00 31.13 ? 534  PHE A CA  1 
ATOM   4108  C  C   . PHE A  1 534 ? 38.296  35.454 68.686  1.00 32.02 ? 534  PHE A C   1 
ATOM   4109  O  O   . PHE A  1 534 ? 39.361  35.088 69.182  1.00 32.92 ? 534  PHE A O   1 
ATOM   4110  C  CB  . PHE A  1 534 ? 39.016  36.754 66.679  1.00 30.48 ? 534  PHE A CB  1 
ATOM   4111  C  CG  . PHE A  1 534 ? 38.616  35.649 65.754  1.00 30.59 ? 534  PHE A CG  1 
ATOM   4112  C  CD1 . PHE A  1 534 ? 37.368  35.658 65.133  1.00 29.89 ? 534  PHE A CD1 1 
ATOM   4113  C  CD2 . PHE A  1 534 ? 39.485  34.590 65.498  1.00 31.36 ? 534  PHE A CD2 1 
ATOM   4114  C  CE1 . PHE A  1 534 ? 36.994  34.627 64.273  1.00 29.78 ? 534  PHE A CE1 1 
ATOM   4115  C  CE2 . PHE A  1 534 ? 39.111  33.549 64.632  1.00 31.79 ? 534  PHE A CE2 1 
ATOM   4116  C  CZ  . PHE A  1 534 ? 37.864  33.573 64.024  1.00 29.92 ? 534  PHE A CZ  1 
ATOM   4117  N  N   . ASP A  1 535 ? 37.197  34.707 68.702  1.00 32.53 ? 535  ASP A N   1 
ATOM   4118  C  CA  . ASP A  1 535 ? 37.155  33.405 69.366  1.00 32.73 ? 535  ASP A CA  1 
ATOM   4119  C  C   . ASP A  1 535 ? 36.831  32.301 68.363  1.00 32.66 ? 535  ASP A C   1 
ATOM   4120  O  O   . ASP A  1 535 ? 35.678  32.143 67.963  1.00 32.25 ? 535  ASP A O   1 
ATOM   4121  C  CB  . ASP A  1 535 ? 36.095  33.447 70.464  1.00 32.54 ? 535  ASP A CB  1 
ATOM   4122  C  CG  . ASP A  1 535 ? 36.039  32.161 71.294  1.00 33.61 ? 535  ASP A CG  1 
ATOM   4123  O  OD1 . ASP A  1 535 ? 35.283  32.172 72.285  1.00 34.78 ? 535  ASP A OD1 1 
ATOM   4124  O  OD2 . ASP A  1 535 ? 36.728  31.159 70.970  1.00 32.30 ? 535  ASP A OD2 1 
ATOM   4125  N  N   . LYS A  1 536 ? 37.852  31.540 67.968  1.00 33.31 ? 536  LYS A N   1 
ATOM   4126  C  CA  . LYS A  1 536 ? 37.709  30.457 66.993  1.00 33.97 ? 536  LYS A CA  1 
ATOM   4127  C  C   . LYS A  1 536 ? 36.711  29.377 67.391  1.00 34.24 ? 536  LYS A C   1 
ATOM   4128  O  O   . LYS A  1 536 ? 36.382  28.512 66.581  1.00 33.88 ? 536  LYS A O   1 
ATOM   4129  C  CB  . LYS A  1 536 ? 39.069  29.814 66.728  1.00 35.97 ? 536  LYS A CB  1 
ATOM   4130  C  CG  . LYS A  1 536 ? 39.889  29.593 68.004  1.00 38.81 ? 536  LYS A CG  1 
ATOM   4131  C  CD  . LYS A  1 536 ? 41.274  28.985 67.723  1.00 40.67 ? 536  LYS A CD  1 
ATOM   4132  C  CE  . LYS A  1 536 ? 41.214  27.457 67.597  1.00 41.86 ? 536  LYS A CE  1 
ATOM   4133  N  NZ  . LYS A  1 536 ? 42.523  26.856 67.180  1.00 41.94 ? 536  LYS A NZ  1 
ATOM   4134  N  N   . SER A  1 537 ? 36.226  29.430 68.630  1.00 34.14 ? 537  SER A N   1 
ATOM   4135  C  CA  . SER A  1 537 ? 35.258  28.451 69.103  1.00 34.76 ? 537  SER A CA  1 
ATOM   4136  C  C   . SER A  1 537 ? 33.840  28.943 68.834  1.00 34.88 ? 537  SER A C   1 
ATOM   4137  O  O   . SER A  1 537 ? 32.873  28.244 69.135  1.00 35.19 ? 537  SER A O   1 
ATOM   4138  C  CB  . SER A  1 537 ? 35.429  28.194 70.606  1.00 34.09 ? 537  SER A CB  1 
ATOM   4139  O  OG  . SER A  1 537 ? 34.926  29.283 71.367  1.00 34.91 ? 537  SER A OG  1 
ATOM   4140  N  N   . LYS A  1 538 ? 33.713  30.155 68.291  1.00 34.79 ? 538  LYS A N   1 
ATOM   4141  C  CA  . LYS A  1 538 ? 32.397  30.718 67.974  1.00 34.29 ? 538  LYS A CA  1 
ATOM   4142  C  C   . LYS A  1 538 ? 32.171  30.758 66.466  1.00 33.09 ? 538  LYS A C   1 
ATOM   4143  O  O   . LYS A  1 538 ? 33.110  30.645 65.683  1.00 32.38 ? 538  LYS A O   1 
ATOM   4144  C  CB  . LYS A  1 538 ? 32.267  32.126 68.557  1.00 36.27 ? 538  LYS A CB  1 
ATOM   4145  C  CG  . LYS A  1 538 ? 32.484  32.146 70.059  1.00 39.03 ? 538  LYS A CG  1 
ATOM   4146  C  CD  . LYS A  1 538 ? 32.230  33.517 70.685  1.00 40.82 ? 538  LYS A CD  1 
ATOM   4147  C  CE  . LYS A  1 538 ? 32.414  33.443 72.206  1.00 42.41 ? 538  LYS A CE  1 
ATOM   4148  N  NZ  . LYS A  1 538 ? 31.623  32.316 72.809  1.00 42.87 ? 538  LYS A NZ  1 
ATOM   4149  N  N   . LYS A  1 539 ? 30.916  30.906 66.063  1.00 32.00 ? 539  LYS A N   1 
ATOM   4150  C  CA  . LYS A  1 539 ? 30.580  30.958 64.649  1.00 31.09 ? 539  LYS A CA  1 
ATOM   4151  C  C   . LYS A  1 539 ? 30.212  32.402 64.331  1.00 29.33 ? 539  LYS A C   1 
ATOM   4152  O  O   . LYS A  1 539 ? 29.280  32.956 64.918  1.00 30.09 ? 539  LYS A O   1 
ATOM   4153  C  CB  . LYS A  1 539 ? 29.397  30.033 64.353  1.00 33.21 ? 539  LYS A CB  1 
ATOM   4154  C  CG  . LYS A  1 539 ? 29.575  28.622 64.905  1.00 35.75 ? 539  LYS A CG  1 
ATOM   4155  C  CD  . LYS A  1 539 ? 30.212  27.696 63.895  1.00 37.43 ? 539  LYS A CD  1 
ATOM   4156  C  CE  . LYS A  1 539 ? 29.152  26.828 63.241  1.00 38.56 ? 539  LYS A CE  1 
ATOM   4157  N  NZ  . LYS A  1 539 ? 27.948  27.635 62.844  1.00 40.53 ? 539  LYS A NZ  1 
ATOM   4158  N  N   . TYR A  1 540 ? 30.961  33.029 63.428  1.00 25.92 ? 540  TYR A N   1 
ATOM   4159  C  CA  . TYR A  1 540 ? 30.660  34.412 63.071  1.00 23.17 ? 540  TYR A CA  1 
ATOM   4160  C  C   . TYR A  1 540 ? 30.075  34.491 61.676  1.00 21.12 ? 540  TYR A C   1 
ATOM   4161  O  O   . TYR A  1 540 ? 30.314  33.633 60.836  1.00 20.45 ? 540  TYR A O   1 
ATOM   4162  C  CB  . TYR A  1 540 ? 31.921  35.281 63.059  1.00 22.35 ? 540  TYR A CB  1 
ATOM   4163  C  CG  . TYR A  1 540 ? 32.646  35.407 64.364  1.00 21.82 ? 540  TYR A CG  1 
ATOM   4164  C  CD1 . TYR A  1 540 ? 32.552  36.570 65.123  1.00 22.30 ? 540  TYR A CD1 1 
ATOM   4165  C  CD2 . TYR A  1 540 ? 33.444  34.370 64.838  1.00 22.19 ? 540  TYR A CD2 1 
ATOM   4166  C  CE1 . TYR A  1 540 ? 33.241  36.700 66.334  1.00 23.38 ? 540  TYR A CE1 1 
ATOM   4167  C  CE2 . TYR A  1 540 ? 34.133  34.487 66.044  1.00 23.13 ? 540  TYR A CE2 1 
ATOM   4168  C  CZ  . TYR A  1 540 ? 34.025  35.648 66.781  1.00 23.42 ? 540  TYR A CZ  1 
ATOM   4169  O  OH  . TYR A  1 540 ? 34.680  35.752 67.981  1.00 25.98 ? 540  TYR A OH  1 
ATOM   4170  N  N   . PRO A  1 541 ? 29.254  35.507 61.430  1.00 20.45 ? 541  PRO A N   1 
ATOM   4171  C  CA  . PRO A  1 541 ? 28.689  35.652 60.092  1.00 18.85 ? 541  PRO A CA  1 
ATOM   4172  C  C   . PRO A  1 541 ? 29.877  36.171 59.263  1.00 19.15 ? 541  PRO A C   1 
ATOM   4173  O  O   . PRO A  1 541 ? 30.810  36.758 59.815  1.00 18.53 ? 541  PRO A O   1 
ATOM   4174  C  CB  . PRO A  1 541 ? 27.598  36.700 60.290  1.00 19.89 ? 541  PRO A CB  1 
ATOM   4175  C  CG  . PRO A  1 541 ? 28.048  37.478 61.500  1.00 19.78 ? 541  PRO A CG  1 
ATOM   4176  C  CD  . PRO A  1 541 ? 28.603  36.410 62.394  1.00 19.81 ? 541  PRO A CD  1 
ATOM   4177  N  N   . LEU A  1 542 ? 29.878  35.931 57.961  1.00 18.27 ? 542  LEU A N   1 
ATOM   4178  C  CA  . LEU A  1 542 ? 30.997  36.389 57.145  1.00 17.69 ? 542  LEU A CA  1 
ATOM   4179  C  C   . LEU A  1 542 ? 30.527  37.170 55.915  1.00 16.68 ? 542  LEU A C   1 
ATOM   4180  O  O   . LEU A  1 542 ? 29.584  36.763 55.234  1.00 15.79 ? 542  LEU A O   1 
ATOM   4181  C  CB  . LEU A  1 542 ? 31.865  35.192 56.702  1.00 17.38 ? 542  LEU A CB  1 
ATOM   4182  C  CG  . LEU A  1 542 ? 33.110  35.530 55.859  1.00 18.22 ? 542  LEU A CG  1 
ATOM   4183  C  CD1 . LEU A  1 542 ? 34.210  34.521 56.102  1.00 19.10 ? 542  LEU A CD1 1 
ATOM   4184  C  CD2 . LEU A  1 542 ? 32.743  35.553 54.386  1.00 17.95 ? 542  LEU A CD2 1 
ATOM   4185  N  N   . LEU A  1 543 ? 31.170  38.307 55.669  1.00 15.62 ? 543  LEU A N   1 
ATOM   4186  C  CA  . LEU A  1 543 ? 30.870  39.139 54.507  1.00 14.89 ? 543  LEU A CA  1 
ATOM   4187  C  C   . LEU A  1 543 ? 32.075  39.084 53.564  1.00 15.34 ? 543  LEU A C   1 
ATOM   4188  O  O   . LEU A  1 543 ? 33.189  39.469 53.937  1.00 15.15 ? 543  LEU A O   1 
ATOM   4189  C  CB  . LEU A  1 543 ? 30.592  40.595 54.914  1.00 12.66 ? 543  LEU A CB  1 
ATOM   4190  C  CG  . LEU A  1 543 ? 30.483  41.598 53.747  1.00 13.49 ? 543  LEU A CG  1 
ATOM   4191  C  CD1 . LEU A  1 543 ? 29.271  41.237 52.864  1.00 14.37 ? 543  LEU A CD1 1 
ATOM   4192  C  CD2 . LEU A  1 543 ? 30.352  43.029 54.261  1.00 13.84 ? 543  LEU A CD2 1 
ATOM   4193  N  N   . LEU A  1 544 ? 31.863  38.565 52.358  1.00 14.98 ? 544  LEU A N   1 
ATOM   4194  C  CA  . LEU A  1 544 ? 32.940  38.485 51.378  1.00 15.59 ? 544  LEU A CA  1 
ATOM   4195  C  C   . LEU A  1 544 ? 32.981  39.817 50.604  1.00 15.73 ? 544  LEU A C   1 
ATOM   4196  O  O   . LEU A  1 544 ? 32.065  40.146 49.851  1.00 16.11 ? 544  LEU A O   1 
ATOM   4197  C  CB  . LEU A  1 544 ? 32.705  37.300 50.420  1.00 15.53 ? 544  LEU A CB  1 
ATOM   4198  C  CG  . LEU A  1 544 ? 33.819  36.933 49.423  1.00 16.45 ? 544  LEU A CG  1 
ATOM   4199  C  CD1 . LEU A  1 544 ? 35.097  36.559 50.162  1.00 16.59 ? 544  LEU A CD1 1 
ATOM   4200  C  CD2 . LEU A  1 544 ? 33.367  35.773 48.545  1.00 15.39 ? 544  LEU A CD2 1 
ATOM   4201  N  N   . ASP A  1 545 ? 34.041  40.582 50.822  1.00 15.45 ? 545  ASP A N   1 
ATOM   4202  C  CA  . ASP A  1 545 ? 34.254  41.874 50.165  1.00 15.17 ? 545  ASP A CA  1 
ATOM   4203  C  C   . ASP A  1 545 ? 35.043  41.578 48.884  1.00 14.89 ? 545  ASP A C   1 
ATOM   4204  O  O   . ASP A  1 545 ? 36.198  41.173 48.943  1.00 14.16 ? 545  ASP A O   1 
ATOM   4205  C  CB  . ASP A  1 545 ? 35.063  42.778 51.103  1.00 14.95 ? 545  ASP A CB  1 
ATOM   4206  C  CG  . ASP A  1 545 ? 35.479  44.116 50.452  1.00 16.69 ? 545  ASP A CG  1 
ATOM   4207  O  OD1 . ASP A  1 545 ? 35.345  44.301 49.222  1.00 15.84 ? 545  ASP A OD1 1 
ATOM   4208  O  OD2 . ASP A  1 545 ? 35.956  44.985 51.200  1.00 17.42 ? 545  ASP A OD2 1 
ATOM   4209  N  N   . VAL A  1 546 ? 34.441  41.788 47.723  1.00 15.17 ? 546  VAL A N   1 
ATOM   4210  C  CA  . VAL A  1 546 ? 35.150  41.439 46.492  1.00 15.93 ? 546  VAL A CA  1 
ATOM   4211  C  C   . VAL A  1 546 ? 35.319  42.530 45.448  1.00 14.92 ? 546  VAL A C   1 
ATOM   4212  O  O   . VAL A  1 546 ? 34.524  43.466 45.378  1.00 14.77 ? 546  VAL A O   1 
ATOM   4213  C  CB  . VAL A  1 546 ? 34.419  40.265 45.787  1.00 18.03 ? 546  VAL A CB  1 
ATOM   4214  C  CG1 . VAL A  1 546 ? 33.006  40.678 45.501  1.00 18.47 ? 546  VAL A CG1 1 
ATOM   4215  C  CG2 . VAL A  1 546 ? 35.093  39.887 44.465  1.00 19.48 ? 546  VAL A CG2 1 
ATOM   4216  N  N   . TYR A  1 547 ? 36.395  42.424 44.672  1.00 14.24 ? 547  TYR A N   1 
ATOM   4217  C  CA  . TYR A  1 547 ? 36.597  43.315 43.539  1.00 14.27 ? 547  TYR A CA  1 
ATOM   4218  C  C   . TYR A  1 547 ? 36.823  42.292 42.435  1.00 14.99 ? 547  TYR A C   1 
ATOM   4219  O  O   . TYR A  1 547 ? 35.959  42.110 41.577  1.00 14.79 ? 547  TYR A O   1 
ATOM   4220  C  CB  . TYR A  1 547 ? 37.797  44.242 43.681  1.00 14.28 ? 547  TYR A CB  1 
ATOM   4221  C  CG  . TYR A  1 547 ? 37.855  45.181 42.487  1.00 14.88 ? 547  TYR A CG  1 
ATOM   4222  C  CD1 . TYR A  1 547 ? 38.749  44.960 41.439  1.00 15.23 ? 547  TYR A CD1 1 
ATOM   4223  C  CD2 . TYR A  1 547 ? 36.919  46.222 42.353  1.00 15.49 ? 547  TYR A CD2 1 
ATOM   4224  C  CE1 . TYR A  1 547 ? 38.709  45.738 40.281  1.00 15.51 ? 547  TYR A CE1 1 
ATOM   4225  C  CE2 . TYR A  1 547 ? 36.868  47.009 41.198  1.00 16.49 ? 547  TYR A CE2 1 
ATOM   4226  C  CZ  . TYR A  1 547 ? 37.763  46.752 40.164  1.00 17.57 ? 547  TYR A CZ  1 
ATOM   4227  O  OH  . TYR A  1 547 ? 37.661  47.460 38.994  1.00 17.94 ? 547  TYR A OH  1 
ATOM   4228  N  N   . ALA A  1 548 ? 37.969  41.612 42.473  1.00 14.13 ? 548  ALA A N   1 
ATOM   4229  C  CA  . ALA A  1 548 ? 38.254  40.535 41.536  1.00 14.45 ? 548  ALA A CA  1 
ATOM   4230  C  C   . ALA A  1 548 ? 38.447  40.874 40.061  1.00 15.82 ? 548  ALA A C   1 
ATOM   4231  O  O   . ALA A  1 548 ? 38.419  39.980 39.209  1.00 16.56 ? 548  ALA A O   1 
ATOM   4232  C  CB  . ALA A  1 548 ? 37.157  39.459 41.669  1.00 13.74 ? 548  ALA A CB  1 
ATOM   4233  N  N   . GLY A  1 549 ? 38.635  42.145 39.740  1.00 16.46 ? 549  GLY A N   1 
ATOM   4234  C  CA  . GLY A  1 549 ? 38.844  42.498 38.349  1.00 15.18 ? 549  GLY A CA  1 
ATOM   4235  C  C   . GLY A  1 549 ? 40.220  42.025 37.907  1.00 15.52 ? 549  GLY A C   1 
ATOM   4236  O  O   . GLY A  1 549 ? 41.012  41.577 38.736  1.00 15.06 ? 549  GLY A O   1 
ATOM   4237  N  N   . PRO A  1 550 ? 40.539  42.083 36.603  1.00 14.80 ? 550  PRO A N   1 
ATOM   4238  C  CA  . PRO A  1 550 ? 41.858  41.642 36.137  1.00 15.33 ? 550  PRO A CA  1 
ATOM   4239  C  C   . PRO A  1 550 ? 42.983  42.480 36.724  1.00 15.37 ? 550  PRO A C   1 
ATOM   4240  O  O   . PRO A  1 550 ? 42.954  43.703 36.660  1.00 15.52 ? 550  PRO A O   1 
ATOM   4241  C  CB  . PRO A  1 550 ? 41.767  41.777 34.618  1.00 14.63 ? 550  PRO A CB  1 
ATOM   4242  C  CG  . PRO A  1 550 ? 40.696  42.826 34.421  1.00 15.37 ? 550  PRO A CG  1 
ATOM   4243  C  CD  . PRO A  1 550 ? 39.676  42.458 35.479  1.00 14.38 ? 550  PRO A CD  1 
ATOM   4244  N  N   . CYS A  1 551 ? 43.966  41.774 37.276  1.00 15.45 ? 551  CYS A N   1 
ATOM   4245  C  CA  . CYS A  1 551 ? 45.142  42.326 37.922  1.00 14.92 ? 551  CYS A CA  1 
ATOM   4246  C  C   . CYS A  1 551 ? 44.807  42.999 39.250  1.00 14.23 ? 551  CYS A C   1 
ATOM   4247  O  O   . CYS A  1 551 ? 45.566  43.813 39.752  1.00 14.53 ? 551  CYS A O   1 
ATOM   4248  C  CB  . CYS A  1 551 ? 45.893  43.287 36.985  1.00 14.06 ? 551  CYS A CB  1 
ATOM   4249  S  SG  . CYS A  1 551 ? 47.664  43.527 37.487  1.00 16.97 ? 551  CYS A SG  1 
ATOM   4250  N  N   . SER A  1 552 ? 43.668  42.644 39.828  1.00 14.03 ? 552  SER A N   1 
ATOM   4251  C  CA  . SER A  1 552 ? 43.300  43.210 41.115  1.00 14.10 ? 552  SER A CA  1 
ATOM   4252  C  C   . SER A  1 552 ? 44.037  42.503 42.268  1.00 14.35 ? 552  SER A C   1 
ATOM   4253  O  O   . SER A  1 552 ? 44.623  41.422 42.097  1.00 13.98 ? 552  SER A O   1 
ATOM   4254  C  CB  . SER A  1 552 ? 41.794  43.087 41.333  1.00 14.89 ? 552  SER A CB  1 
ATOM   4255  O  OG  . SER A  1 552 ? 41.413  41.732 41.375  1.00 15.56 ? 552  SER A OG  1 
ATOM   4256  N  N   . GLN A  1 553 ? 44.045  43.139 43.430  1.00 13.30 ? 553  GLN A N   1 
ATOM   4257  C  CA  . GLN A  1 553 ? 44.649  42.534 44.611  1.00 13.78 ? 553  GLN A CA  1 
ATOM   4258  C  C   . GLN A  1 553 ? 43.863  43.091 45.780  1.00 13.79 ? 553  GLN A C   1 
ATOM   4259  O  O   . GLN A  1 553 ? 43.883  44.302 46.005  1.00 12.22 ? 553  GLN A O   1 
ATOM   4260  C  CB  . GLN A  1 553 ? 46.137  42.884 44.770  1.00 14.62 ? 553  GLN A CB  1 
ATOM   4261  C  CG  . GLN A  1 553 ? 46.739  42.181 45.993  1.00 15.35 ? 553  GLN A CG  1 
ATOM   4262  C  CD  . GLN A  1 553 ? 48.248  42.294 46.078  1.00 16.28 ? 553  GLN A CD  1 
ATOM   4263  O  OE1 . GLN A  1 553 ? 48.786  43.351 46.412  1.00 16.09 ? 553  GLN A OE1 1 
ATOM   4264  N  NE2 . GLN A  1 553 ? 48.943  41.192 45.780  1.00 17.83 ? 553  GLN A NE2 1 
ATOM   4265  N  N   . LYS A  1 554 ? 43.143  42.208 46.476  1.00 12.56 ? 554  LYS A N   1 
ATOM   4266  C  CA  . LYS A  1 554 ? 42.319  42.576 47.625  1.00 13.21 ? 554  LYS A CA  1 
ATOM   4267  C  C   . LYS A  1 554 ? 42.822  41.955 48.925  1.00 13.14 ? 554  LYS A C   1 
ATOM   4268  O  O   . LYS A  1 554 ? 42.284  42.228 50.003  1.00 13.74 ? 554  LYS A O   1 
ATOM   4269  C  CB  . LYS A  1 554 ? 40.862  42.165 47.389  1.00 12.50 ? 554  LYS A CB  1 
ATOM   4270  C  CG  . LYS A  1 554 ? 40.122  43.076 46.416  1.00 14.26 ? 554  LYS A CG  1 
ATOM   4271  C  CD  . LYS A  1 554 ? 39.698  44.388 47.105  1.00 14.14 ? 554  LYS A CD  1 
ATOM   4272  C  CE  . LYS A  1 554 ? 38.381  44.199 47.878  1.00 13.20 ? 554  LYS A CE  1 
ATOM   4273  N  NZ  . LYS A  1 554 ? 37.939  45.470 48.538  1.00 15.16 ? 554  LYS A NZ  1 
ATOM   4274  N  N   . ALA A  1 555 ? 43.834  41.098 48.822  1.00 13.48 ? 555  ALA A N   1 
ATOM   4275  C  CA  . ALA A  1 555 ? 44.447  40.501 50.011  1.00 13.69 ? 555  ALA A CA  1 
ATOM   4276  C  C   . ALA A  1 555 ? 45.829  41.137 50.096  1.00 13.45 ? 555  ALA A C   1 
ATOM   4277  O  O   . ALA A  1 555 ? 46.719  40.817 49.294  1.00 13.08 ? 555  ALA A O   1 
ATOM   4278  C  CB  . ALA A  1 555 ? 44.588  38.983 49.854  1.00 11.07 ? 555  ALA A CB  1 
ATOM   4279  N  N   . ASP A  1 556 ? 46.025  42.045 51.039  1.00 13.83 ? 556  ASP A N   1 
ATOM   4280  C  CA  . ASP A  1 556 ? 47.341  42.669 51.158  1.00 15.32 ? 556  ASP A CA  1 
ATOM   4281  C  C   . ASP A  1 556 ? 47.675  43.056 52.595  1.00 15.98 ? 556  ASP A C   1 
ATOM   4282  O  O   . ASP A  1 556 ? 46.916  42.763 53.510  1.00 16.03 ? 556  ASP A O   1 
ATOM   4283  C  CB  . ASP A  1 556 ? 47.451  43.894 50.247  1.00 14.23 ? 556  ASP A CB  1 
ATOM   4284  C  CG  . ASP A  1 556 ? 46.446  44.966 50.580  1.00 16.19 ? 556  ASP A CG  1 
ATOM   4285  O  OD1 . ASP A  1 556 ? 46.135  45.155 51.769  1.00 17.47 ? 556  ASP A OD1 1 
ATOM   4286  O  OD2 . ASP A  1 556 ? 45.987  45.647 49.645  1.00 18.04 ? 556  ASP A OD2 1 
ATOM   4287  N  N   . THR A  1 557 ? 48.807  43.722 52.787  1.00 15.69 ? 557  THR A N   1 
ATOM   4288  C  CA  . THR A  1 557 ? 49.228  44.105 54.129  1.00 16.51 ? 557  THR A CA  1 
ATOM   4289  C  C   . THR A  1 557 ? 48.950  45.560 54.487  1.00 16.19 ? 557  THR A C   1 
ATOM   4290  O  O   . THR A  1 557 ? 49.504  46.093 55.454  1.00 16.04 ? 557  THR A O   1 
ATOM   4291  C  CB  . THR A  1 557 ? 50.734  43.841 54.314  1.00 17.01 ? 557  THR A CB  1 
ATOM   4292  O  OG1 . THR A  1 557 ? 51.459  44.549 53.307  1.00 16.38 ? 557  THR A OG1 1 
ATOM   4293  C  CG2 . THR A  1 557 ? 51.037  42.344 54.184  1.00 16.96 ? 557  THR A CG2 1 
ATOM   4294  N  N   . VAL A  1 558 ? 48.094  46.213 53.715  1.00 15.56 ? 558  VAL A N   1 
ATOM   4295  C  CA  . VAL A  1 558 ? 47.798  47.616 53.972  1.00 14.90 ? 558  VAL A CA  1 
ATOM   4296  C  C   . VAL A  1 558 ? 46.840  47.832 55.150  1.00 15.41 ? 558  VAL A C   1 
ATOM   4297  O  O   . VAL A  1 558 ? 45.852  47.115 55.305  1.00 14.48 ? 558  VAL A O   1 
ATOM   4298  C  CB  . VAL A  1 558 ? 47.208  48.275 52.715  1.00 15.12 ? 558  VAL A CB  1 
ATOM   4299  C  CG1 . VAL A  1 558 ? 46.882  49.743 52.998  1.00 13.66 ? 558  VAL A CG1 1 
ATOM   4300  C  CG2 . VAL A  1 558 ? 48.198  48.148 51.556  1.00 12.21 ? 558  VAL A CG2 1 
ATOM   4301  N  N   . PHE A  1 559 ? 47.142  48.819 55.978  1.00 15.52 ? 559  PHE A N   1 
ATOM   4302  C  CA  . PHE A  1 559 ? 46.291  49.141 57.121  1.00 16.35 ? 559  PHE A CA  1 
ATOM   4303  C  C   . PHE A  1 559 ? 45.173  50.076 56.647  1.00 15.52 ? 559  PHE A C   1 
ATOM   4304  O  O   . PHE A  1 559 ? 45.456  51.109 56.061  1.00 15.05 ? 559  PHE A O   1 
ATOM   4305  C  CB  . PHE A  1 559 ? 47.105  49.843 58.213  1.00 17.64 ? 559  PHE A CB  1 
ATOM   4306  C  CG  . PHE A  1 559 ? 46.266  50.373 59.351  1.00 18.80 ? 559  PHE A CG  1 
ATOM   4307  C  CD1 . PHE A  1 559 ? 45.845  49.530 60.373  1.00 21.28 ? 559  PHE A CD1 1 
ATOM   4308  C  CD2 . PHE A  1 559 ? 45.847  51.699 59.365  1.00 18.77 ? 559  PHE A CD2 1 
ATOM   4309  C  CE1 . PHE A  1 559 ? 45.005  50.007 61.408  1.00 22.42 ? 559  PHE A CE1 1 
ATOM   4310  C  CE2 . PHE A  1 559 ? 45.021  52.178 60.380  1.00 20.68 ? 559  PHE A CE2 1 
ATOM   4311  C  CZ  . PHE A  1 559 ? 44.597  51.328 61.404  1.00 20.29 ? 559  PHE A CZ  1 
ATOM   4312  N  N   . ARG A  1 560 ? 43.914  49.716 56.892  1.00 15.06 ? 560  ARG A N   1 
ATOM   4313  C  CA  . ARG A  1 560 ? 42.797  50.561 56.469  1.00 15.50 ? 560  ARG A CA  1 
ATOM   4314  C  C   . ARG A  1 560 ? 41.748  50.768 57.569  1.00 14.94 ? 560  ARG A C   1 
ATOM   4315  O  O   . ARG A  1 560 ? 41.543  49.898 58.421  1.00 14.92 ? 560  ARG A O   1 
ATOM   4316  C  CB  . ARG A  1 560 ? 42.090  49.951 55.243  1.00 15.95 ? 560  ARG A CB  1 
ATOM   4317  C  CG  . ARG A  1 560 ? 42.996  49.633 54.039  1.00 15.87 ? 560  ARG A CG  1 
ATOM   4318  C  CD  . ARG A  1 560 ? 42.170  49.329 52.775  1.00 16.30 ? 560  ARG A CD  1 
ATOM   4319  N  NE  . ARG A  1 560 ? 43.045  49.197 51.610  1.00 17.20 ? 560  ARG A NE  1 
ATOM   4320  C  CZ  . ARG A  1 560 ? 43.798  48.133 51.340  1.00 17.12 ? 560  ARG A CZ  1 
ATOM   4321  N  NH1 . ARG A  1 560 ? 43.774  47.074 52.140  1.00 18.08 ? 560  ARG A NH1 1 
ATOM   4322  N  NH2 . ARG A  1 560 ? 44.633  48.153 50.303  1.00 15.04 ? 560  ARG A NH2 1 
ATOM   4323  N  N   . LEU A  1 561 ? 41.110  51.936 57.537  1.00 14.89 ? 561  LEU A N   1 
ATOM   4324  C  CA  . LEU A  1 561 ? 40.020  52.296 58.444  1.00 16.40 ? 561  LEU A CA  1 
ATOM   4325  C  C   . LEU A  1 561 ? 38.870  52.508 57.478  1.00 16.67 ? 561  LEU A C   1 
ATOM   4326  O  O   . LEU A  1 561 ? 38.784  53.545 56.809  1.00 16.31 ? 561  LEU A O   1 
ATOM   4327  C  CB  . LEU A  1 561 ? 40.297  53.600 59.195  1.00 16.29 ? 561  LEU A CB  1 
ATOM   4328  C  CG  . LEU A  1 561 ? 41.408  53.491 60.233  1.00 17.42 ? 561  LEU A CG  1 
ATOM   4329  C  CD1 . LEU A  1 561 ? 41.545  54.817 60.973  1.00 19.22 ? 561  LEU A CD1 1 
ATOM   4330  C  CD2 . LEU A  1 561 ? 41.115  52.362 61.187  1.00 17.01 ? 561  LEU A CD2 1 
ATOM   4331  N  N   . ASN A  1 562 ? 38.009  51.507 57.369  1.00 17.51 ? 562  ASN A N   1 
ATOM   4332  C  CA  . ASN A  1 562 ? 36.901  51.597 56.427  1.00 18.22 ? 562  ASN A CA  1 
ATOM   4333  C  C   . ASN A  1 562 ? 35.634  50.906 56.928  1.00 16.88 ? 562  ASN A C   1 
ATOM   4334  O  O   . ASN A  1 562 ? 35.532  50.537 58.100  1.00 16.09 ? 562  ASN A O   1 
ATOM   4335  C  CB  . ASN A  1 562 ? 37.337  50.993 55.096  1.00 18.44 ? 562  ASN A CB  1 
ATOM   4336  C  CG  . ASN A  1 562 ? 37.830  49.582 55.255  1.00 19.90 ? 562  ASN A CG  1 
ATOM   4337  O  OD1 . ASN A  1 562 ? 37.503  48.902 56.249  1.00 20.62 ? 562  ASN A OD1 1 
ATOM   4338  N  ND2 . ASN A  1 562 ? 38.608  49.118 54.289  1.00 18.66 ? 562  ASN A ND2 1 
ATOM   4339  N  N   . TRP A  1 563 ? 34.670  50.721 56.031  1.00 15.31 ? 563  TRP A N   1 
ATOM   4340  C  CA  . TRP A  1 563 ? 33.414  50.106 56.418  1.00 14.64 ? 563  TRP A CA  1 
ATOM   4341  C  C   . TRP A  1 563 ? 33.644  48.750 57.075  1.00 14.35 ? 563  TRP A C   1 
ATOM   4342  O  O   . TRP A  1 563 ? 32.983  48.428 58.064  1.00 13.54 ? 563  TRP A O   1 
ATOM   4343  C  CB  . TRP A  1 563 ? 32.495  49.964 55.211  1.00 13.79 ? 563  TRP A CB  1 
ATOM   4344  C  CG  . TRP A  1 563 ? 31.089  49.507 55.560  1.00 13.68 ? 563  TRP A CG  1 
ATOM   4345  C  CD1 . TRP A  1 563 ? 30.288  49.988 56.571  1.00 13.83 ? 563  TRP A CD1 1 
ATOM   4346  C  CD2 . TRP A  1 563 ? 30.287  48.565 54.831  1.00 11.51 ? 563  TRP A CD2 1 
ATOM   4347  N  NE1 . TRP A  1 563 ? 29.039  49.403 56.506  1.00 13.62 ? 563  TRP A NE1 1 
ATOM   4348  C  CE2 . TRP A  1 563 ? 29.008  48.533 55.449  1.00 12.55 ? 563  TRP A CE2 1 
ATOM   4349  C  CE3 . TRP A  1 563 ? 30.520  47.754 53.714  1.00 10.79 ? 563  TRP A CE3 1 
ATOM   4350  C  CZ2 . TRP A  1 563 ? 27.964  47.718 54.978  1.00 13.18 ? 563  TRP A CZ2 1 
ATOM   4351  C  CZ3 . TRP A  1 563 ? 29.491  46.947 53.245  1.00 12.28 ? 563  TRP A CZ3 1 
ATOM   4352  C  CH2 . TRP A  1 563 ? 28.221  46.936 53.880  1.00 12.28 ? 563  TRP A CH2 1 
ATOM   4353  N  N   . ALA A  1 564 ? 34.585  47.971 56.546  1.00 12.46 ? 564  ALA A N   1 
ATOM   4354  C  CA  . ALA A  1 564 ? 34.880  46.661 57.114  1.00 13.06 ? 564  ALA A CA  1 
ATOM   4355  C  C   . ALA A  1 564 ? 35.376  46.782 58.546  1.00 13.72 ? 564  ALA A C   1 
ATOM   4356  O  O   . ALA A  1 564 ? 35.094  45.908 59.360  1.00 14.11 ? 564  ALA A O   1 
ATOM   4357  C  CB  . ALA A  1 564 ? 35.909  45.910 56.279  1.00 10.43 ? 564  ALA A CB  1 
ATOM   4358  N  N   . THR A  1 565 ? 36.104  47.858 58.856  1.00 14.76 ? 565  THR A N   1 
ATOM   4359  C  CA  . THR A  1 565 ? 36.628  48.061 60.218  1.00 14.92 ? 565  THR A CA  1 
ATOM   4360  C  C   . THR A  1 565 ? 35.456  48.135 61.203  1.00 15.82 ? 565  THR A C   1 
ATOM   4361  O  O   . THR A  1 565 ? 35.491  47.540 62.284  1.00 15.49 ? 565  THR A O   1 
ATOM   4362  C  CB  . THR A  1 565 ? 37.424  49.387 60.354  1.00 15.45 ? 565  THR A CB  1 
ATOM   4363  O  OG1 . THR A  1 565 ? 38.424  49.458 59.330  1.00 13.52 ? 565  THR A OG1 1 
ATOM   4364  C  CG2 . THR A  1 565 ? 38.112  49.461 61.737  1.00 12.09 ? 565  THR A CG2 1 
ATOM   4365  N  N   . TYR A  1 566 ? 34.418  48.868 60.823  1.00 16.14 ? 566  TYR A N   1 
ATOM   4366  C  CA  . TYR A  1 566 ? 33.254  49.009 61.683  1.00 16.77 ? 566  TYR A CA  1 
ATOM   4367  C  C   . TYR A  1 566 ? 32.475  47.706 61.769  1.00 18.06 ? 566  TYR A C   1 
ATOM   4368  O  O   . TYR A  1 566 ? 32.052  47.301 62.863  1.00 17.37 ? 566  TYR A O   1 
ATOM   4369  C  CB  . TYR A  1 566 ? 32.352  50.143 61.172  1.00 17.46 ? 566  TYR A CB  1 
ATOM   4370  C  CG  . TYR A  1 566 ? 30.873  49.847 61.291  1.00 18.89 ? 566  TYR A CG  1 
ATOM   4371  C  CD1 . TYR A  1 566 ? 30.231  49.911 62.526  1.00 19.37 ? 566  TYR A CD1 1 
ATOM   4372  C  CD2 . TYR A  1 566 ? 30.123  49.476 60.171  1.00 18.99 ? 566  TYR A CD2 1 
ATOM   4373  C  CE1 . TYR A  1 566 ? 28.877  49.614 62.658  1.00 21.68 ? 566  TYR A CE1 1 
ATOM   4374  C  CE2 . TYR A  1 566 ? 28.751  49.170 60.287  1.00 21.65 ? 566  TYR A CE2 1 
ATOM   4375  C  CZ  . TYR A  1 566 ? 28.141  49.242 61.535  1.00 22.33 ? 566  TYR A CZ  1 
ATOM   4376  O  OH  . TYR A  1 566 ? 26.819  48.926 61.686  1.00 22.33 ? 566  TYR A OH  1 
ATOM   4377  N  N   . LEU A  1 567 ? 32.287  47.044 60.624  1.00 18.09 ? 567  LEU A N   1 
ATOM   4378  C  CA  . LEU A  1 567 ? 31.549  45.786 60.596  1.00 18.35 ? 567  LEU A CA  1 
ATOM   4379  C  C   . LEU A  1 567 ? 32.171  44.731 61.505  1.00 18.99 ? 567  LEU A C   1 
ATOM   4380  O  O   . LEU A  1 567 ? 31.454  43.960 62.158  1.00 18.78 ? 567  LEU A O   1 
ATOM   4381  C  CB  . LEU A  1 567 ? 31.449  45.241 59.162  1.00 17.48 ? 567  LEU A CB  1 
ATOM   4382  C  CG  . LEU A  1 567 ? 30.540  46.027 58.200  1.00 17.71 ? 567  LEU A CG  1 
ATOM   4383  C  CD1 . LEU A  1 567 ? 30.679  45.459 56.778  1.00 18.60 ? 567  LEU A CD1 1 
ATOM   4384  C  CD2 . LEU A  1 567 ? 29.104  45.944 58.667  1.00 16.75 ? 567  LEU A CD2 1 
ATOM   4385  N  N   . ALA A  1 568 ? 33.498  44.688 61.554  1.00 18.59 ? 568  ALA A N   1 
ATOM   4386  C  CA  . ALA A  1 568 ? 34.169  43.709 62.397  1.00 18.61 ? 568  ALA A CA  1 
ATOM   4387  C  C   . ALA A  1 568 ? 34.218  44.174 63.848  1.00 19.17 ? 568  ALA A C   1 
ATOM   4388  O  O   . ALA A  1 568 ? 33.918  43.407 64.754  1.00 19.56 ? 568  ALA A O   1 
ATOM   4389  C  CB  . ALA A  1 568 ? 35.604  43.436 61.884  1.00 16.66 ? 568  ALA A CB  1 
ATOM   4390  N  N   . SER A  1 569 ? 34.581  45.435 64.059  1.00 18.87 ? 569  SER A N   1 
ATOM   4391  C  CA  . SER A  1 569 ? 34.705  45.963 65.403  1.00 19.13 ? 569  SER A CA  1 
ATOM   4392  C  C   . SER A  1 569 ? 33.378  46.081 66.146  1.00 20.29 ? 569  SER A C   1 
ATOM   4393  O  O   . SER A  1 569 ? 33.258  45.605 67.265  1.00 21.34 ? 569  SER A O   1 
ATOM   4394  C  CB  . SER A  1 569 ? 35.399  47.325 65.369  1.00 18.84 ? 569  SER A CB  1 
ATOM   4395  O  OG  . SER A  1 569 ? 35.421  47.922 66.653  1.00 18.31 ? 569  SER A OG  1 
ATOM   4396  N  N   . THR A  1 570 ? 32.383  46.696 65.522  1.00 19.64 ? 570  THR A N   1 
ATOM   4397  C  CA  . THR A  1 570 ? 31.098  46.881 66.171  1.00 20.59 ? 570  THR A CA  1 
ATOM   4398  C  C   . THR A  1 570 ? 30.072  45.777 65.956  1.00 21.58 ? 570  THR A C   1 
ATOM   4399  O  O   . THR A  1 570 ? 29.359  45.411 66.893  1.00 21.45 ? 570  THR A O   1 
ATOM   4400  C  CB  . THR A  1 570 ? 30.449  48.222 65.756  1.00 20.83 ? 570  THR A CB  1 
ATOM   4401  O  OG1 . THR A  1 570 ? 31.280  49.304 66.190  1.00 20.39 ? 570  THR A OG1 1 
ATOM   4402  C  CG2 . THR A  1 570 ? 29.053  48.365 66.384  1.00 21.07 ? 570  THR A CG2 1 
ATOM   4403  N  N   . GLU A  1 571 ? 29.990  45.228 64.745  1.00 21.34 ? 571  GLU A N   1 
ATOM   4404  C  CA  . GLU A  1 571 ? 28.987  44.194 64.479  1.00 20.42 ? 571  GLU A CA  1 
ATOM   4405  C  C   . GLU A  1 571 ? 29.497  42.755 64.570  1.00 20.06 ? 571  GLU A C   1 
ATOM   4406  O  O   . GLU A  1 571 ? 28.731  41.823 64.374  1.00 19.55 ? 571  GLU A O   1 
ATOM   4407  C  CB  . GLU A  1 571 ? 28.359  44.418 63.097  1.00 20.27 ? 571  GLU A CB  1 
ATOM   4408  C  CG  . GLU A  1 571 ? 27.821  45.829 62.865  1.00 21.58 ? 571  GLU A CG  1 
ATOM   4409  C  CD  . GLU A  1 571 ? 26.655  46.206 63.774  1.00 23.54 ? 571  GLU A CD  1 
ATOM   4410  O  OE1 . GLU A  1 571 ? 26.062  45.296 64.396  1.00 26.11 ? 571  GLU A OE1 1 
ATOM   4411  O  OE2 . GLU A  1 571 ? 26.309  47.413 63.849  1.00 21.79 ? 571  GLU A OE2 1 
ATOM   4412  N  N   . ASN A  1 572 ? 30.780  42.571 64.862  1.00 19.95 ? 572  ASN A N   1 
ATOM   4413  C  CA  . ASN A  1 572 ? 31.366  41.242 64.969  1.00 20.04 ? 572  ASN A CA  1 
ATOM   4414  C  C   . ASN A  1 572 ? 31.185  40.367 63.731  1.00 20.23 ? 572  ASN A C   1 
ATOM   4415  O  O   . ASN A  1 572 ? 30.921  39.164 63.820  1.00 19.62 ? 572  ASN A O   1 
ATOM   4416  C  CB  . ASN A  1 572 ? 30.818  40.536 66.206  1.00 21.75 ? 572  ASN A CB  1 
ATOM   4417  C  CG  . ASN A  1 572 ? 31.228  41.236 67.487  1.00 22.21 ? 572  ASN A CG  1 
ATOM   4418  O  OD1 . ASN A  1 572 ? 30.398  41.785 68.205  1.00 25.13 ? 572  ASN A OD1 1 
ATOM   4419  N  ND2 . ASN A  1 572 ? 32.514  41.238 67.761  1.00 21.83 ? 572  ASN A ND2 1 
ATOM   4420  N  N   . ILE A  1 573 ? 31.367  40.988 62.571  1.00 19.05 ? 573  ILE A N   1 
ATOM   4421  C  CA  . ILE A  1 573 ? 31.251  40.306 61.298  1.00 18.52 ? 573  ILE A CA  1 
ATOM   4422  C  C   . ILE A  1 573 ? 32.642  40.129 60.727  1.00 18.78 ? 573  ILE A C   1 
ATOM   4423  O  O   . ILE A  1 573 ? 33.447  41.057 60.746  1.00 18.13 ? 573  ILE A O   1 
ATOM   4424  C  CB  . ILE A  1 573 ? 30.409  41.156 60.298  1.00 18.88 ? 573  ILE A CB  1 
ATOM   4425  C  CG1 . ILE A  1 573 ? 28.961  41.210 60.753  1.00 18.15 ? 573  ILE A CG1 1 
ATOM   4426  C  CG2 . ILE A  1 573 ? 30.472  40.573 58.888  1.00 18.52 ? 573  ILE A CG2 1 
ATOM   4427  C  CD1 . ILE A  1 573 ? 28.136  42.204 59.966  1.00 18.80 ? 573  ILE A CD1 1 
ATOM   4428  N  N   . ILE A  1 574 ? 32.940  38.935 60.238  1.00 17.91 ? 574  ILE A N   1 
ATOM   4429  C  CA  . ILE A  1 574 ? 34.236  38.717 59.624  1.00 17.58 ? 574  ILE A CA  1 
ATOM   4430  C  C   . ILE A  1 574 ? 34.128  39.212 58.182  1.00 17.31 ? 574  ILE A C   1 
ATOM   4431  O  O   . ILE A  1 574 ? 33.210  38.807 57.449  1.00 17.64 ? 574  ILE A O   1 
ATOM   4432  C  CB  . ILE A  1 574 ? 34.605  37.224 59.567  1.00 17.98 ? 574  ILE A CB  1 
ATOM   4433  C  CG1 . ILE A  1 574 ? 34.869  36.694 60.988  1.00 18.16 ? 574  ILE A CG1 1 
ATOM   4434  C  CG2 . ILE A  1 574 ? 35.830  37.026 58.685  1.00 16.62 ? 574  ILE A CG2 1 
ATOM   4435  C  CD1 . ILE A  1 574 ? 35.080  35.191 61.028  1.00 18.09 ? 574  ILE A CD1 1 
ATOM   4436  N  N   . VAL A  1 575 ? 35.043  40.086 57.768  1.00 15.93 ? 575  VAL A N   1 
ATOM   4437  C  CA  . VAL A  1 575 ? 35.021  40.564 56.385  1.00 14.44 ? 575  VAL A CA  1 
ATOM   4438  C  C   . VAL A  1 575 ? 36.237  40.008 55.673  1.00 14.53 ? 575  VAL A C   1 
ATOM   4439  O  O   . VAL A  1 575 ? 37.374  40.366 55.979  1.00 13.99 ? 575  VAL A O   1 
ATOM   4440  C  CB  . VAL A  1 575 ? 35.037  42.076 56.285  1.00 14.51 ? 575  VAL A CB  1 
ATOM   4441  C  CG1 . VAL A  1 575 ? 34.832  42.472 54.825  1.00 14.74 ? 575  VAL A CG1 1 
ATOM   4442  C  CG2 . VAL A  1 575 ? 33.949  42.663 57.159  1.00 13.32 ? 575  VAL A CG2 1 
ATOM   4443  N  N   . ALA A  1 576 ? 35.986  39.120 54.720  1.00 13.43 ? 576  ALA A N   1 
ATOM   4444  C  CA  . ALA A  1 576 ? 37.062  38.472 53.996  1.00 13.91 ? 576  ALA A CA  1 
ATOM   4445  C  C   . ALA A  1 576 ? 37.172  38.939 52.564  1.00 14.28 ? 576  ALA A C   1 
ATOM   4446  O  O   . ALA A  1 576 ? 36.193  39.389 51.976  1.00 13.79 ? 576  ALA A O   1 
ATOM   4447  C  CB  . ALA A  1 576 ? 36.849  36.956 54.011  1.00 13.31 ? 576  ALA A CB  1 
ATOM   4448  N  N   . SER A  1 577 ? 38.372  38.842 52.005  1.00 14.01 ? 577  SER A N   1 
ATOM   4449  C  CA  . SER A  1 577 ? 38.553  39.175 50.598  1.00 14.88 ? 577  SER A CA  1 
ATOM   4450  C  C   . SER A  1 577 ? 39.495  38.108 50.075  1.00 16.09 ? 577  SER A C   1 
ATOM   4451  O  O   . SER A  1 577 ? 40.376  37.623 50.804  1.00 16.17 ? 577  SER A O   1 
ATOM   4452  C  CB  . SER A  1 577 ? 39.130  40.578 50.423  1.00 15.15 ? 577  SER A CB  1 
ATOM   4453  O  OG  . SER A  1 577 ? 38.144  41.543 50.795  1.00 14.56 ? 577  SER A OG  1 
ATOM   4454  N  N   . PHE A  1 578 ? 39.308  37.741 48.816  1.00 14.50 ? 578  PHE A N   1 
ATOM   4455  C  CA  . PHE A  1 578 ? 40.102  36.679 48.222  1.00 14.87 ? 578  PHE A CA  1 
ATOM   4456  C  C   . PHE A  1 578 ? 40.579  37.053 46.819  1.00 14.04 ? 578  PHE A C   1 
ATOM   4457  O  O   . PHE A  1 578 ? 39.838  37.660 46.036  1.00 12.96 ? 578  PHE A O   1 
ATOM   4458  C  CB  . PHE A  1 578 ? 39.224  35.418 48.164  1.00 14.91 ? 578  PHE A CB  1 
ATOM   4459  C  CG  . PHE A  1 578 ? 39.853  34.247 47.468  1.00 15.86 ? 578  PHE A CG  1 
ATOM   4460  C  CD1 . PHE A  1 578 ? 40.827  33.488 48.102  1.00 16.37 ? 578  PHE A CD1 1 
ATOM   4461  C  CD2 . PHE A  1 578 ? 39.421  33.866 46.197  1.00 14.57 ? 578  PHE A CD2 1 
ATOM   4462  C  CE1 . PHE A  1 578 ? 41.363  32.357 47.481  1.00 16.38 ? 578  PHE A CE1 1 
ATOM   4463  C  CE2 . PHE A  1 578 ? 39.946  32.746 45.572  1.00 15.02 ? 578  PHE A CE2 1 
ATOM   4464  C  CZ  . PHE A  1 578 ? 40.917  31.987 46.213  1.00 15.85 ? 578  PHE A CZ  1 
ATOM   4465  N  N   . ASP A  1 579 ? 41.819  36.705 46.514  1.00 13.75 ? 579  ASP A N   1 
ATOM   4466  C  CA  . ASP A  1 579 ? 42.386  36.945 45.186  1.00 14.63 ? 579  ASP A CA  1 
ATOM   4467  C  C   . ASP A  1 579 ? 42.496  35.619 44.439  1.00 15.50 ? 579  ASP A C   1 
ATOM   4468  O  O   . ASP A  1 579 ? 43.404  34.822 44.703  1.00 15.40 ? 579  ASP A O   1 
ATOM   4469  C  CB  . ASP A  1 579 ? 43.775  37.548 45.288  1.00 13.68 ? 579  ASP A CB  1 
ATOM   4470  C  CG  . ASP A  1 579 ? 43.746  38.964 45.779  1.00 13.95 ? 579  ASP A CG  1 
ATOM   4471  O  OD1 . ASP A  1 579 ? 42.746  39.645 45.475  1.00 14.56 ? 579  ASP A OD1 1 
ATOM   4472  O  OD2 . ASP A  1 579 ? 44.722  39.391 46.427  1.00 13.96 ? 579  ASP A OD2 1 
ATOM   4473  N  N   . GLY A  1 580 ? 41.595  35.388 43.493  1.00 16.30 ? 580  GLY A N   1 
ATOM   4474  C  CA  . GLY A  1 580 ? 41.638  34.138 42.751  1.00 16.57 ? 580  GLY A CA  1 
ATOM   4475  C  C   . GLY A  1 580 ? 42.156  34.314 41.341  1.00 17.90 ? 580  GLY A C   1 
ATOM   4476  O  O   . GLY A  1 580 ? 42.907  35.241 41.061  1.00 17.83 ? 580  GLY A O   1 
ATOM   4477  N  N   . ARG A  1 581 ? 41.757  33.428 40.437  1.00 17.81 ? 581  ARG A N   1 
ATOM   4478  C  CA  . ARG A  1 581 ? 42.222  33.561 39.071  1.00 18.22 ? 581  ARG A CA  1 
ATOM   4479  C  C   . ARG A  1 581 ? 41.878  34.933 38.495  1.00 17.50 ? 581  ARG A C   1 
ATOM   4480  O  O   . ARG A  1 581 ? 40.812  35.489 38.746  1.00 16.44 ? 581  ARG A O   1 
ATOM   4481  C  CB  . ARG A  1 581 ? 41.681  32.417 38.212  1.00 17.72 ? 581  ARG A CB  1 
ATOM   4482  C  CG  . ARG A  1 581 ? 42.553  31.171 38.372  1.00 19.19 ? 581  ARG A CG  1 
ATOM   4483  C  CD  . ARG A  1 581 ? 41.932  29.924 37.755  1.00 19.77 ? 581  ARG A CD  1 
ATOM   4484  N  NE  . ARG A  1 581 ? 40.688  29.544 38.427  1.00 19.39 ? 581  ARG A NE  1 
ATOM   4485  C  CZ  . ARG A  1 581 ? 39.927  28.527 38.042  1.00 21.09 ? 581  ARG A CZ  1 
ATOM   4486  N  NH1 . ARG A  1 581 ? 40.284  27.791 36.991  1.00 20.24 ? 581  ARG A NH1 1 
ATOM   4487  N  NH2 . ARG A  1 581 ? 38.810  28.248 38.701  1.00 21.44 ? 581  ARG A NH2 1 
ATOM   4488  N  N   . GLY A  1 582 ? 42.820  35.482 37.737  1.00 16.88 ? 582  GLY A N   1 
ATOM   4489  C  CA  . GLY A  1 582 ? 42.632  36.798 37.177  1.00 16.37 ? 582  GLY A CA  1 
ATOM   4490  C  C   . GLY A  1 582 ? 43.283  37.878 38.037  1.00 15.80 ? 582  GLY A C   1 
ATOM   4491  O  O   . GLY A  1 582 ? 43.507  38.977 37.535  1.00 16.65 ? 582  GLY A O   1 
ATOM   4492  N  N   . SER A  1 583 ? 43.606  37.588 39.306  1.00 14.97 ? 583  SER A N   1 
ATOM   4493  C  CA  . SER A  1 583 ? 44.201  38.610 40.176  1.00 14.07 ? 583  SER A CA  1 
ATOM   4494  C  C   . SER A  1 583 ? 45.646  38.918 39.774  1.00 13.02 ? 583  SER A C   1 
ATOM   4495  O  O   . SER A  1 583 ? 46.267  38.157 39.034  1.00 13.06 ? 583  SER A O   1 
ATOM   4496  C  CB  . SER A  1 583 ? 44.101  38.199 41.659  1.00 13.44 ? 583  SER A CB  1 
ATOM   4497  O  OG  . SER A  1 583 ? 44.839  37.015 41.936  1.00 13.72 ? 583  SER A OG  1 
ATOM   4498  N  N   . GLY A  1 584 ? 46.194  40.028 40.250  1.00 12.85 ? 584  GLY A N   1 
ATOM   4499  C  CA  . GLY A  1 584 ? 47.534  40.389 39.812  1.00 12.71 ? 584  GLY A CA  1 
ATOM   4500  C  C   . GLY A  1 584 ? 48.734  40.131 40.703  1.00 12.40 ? 584  GLY A C   1 
ATOM   4501  O  O   . GLY A  1 584 ? 48.621  39.555 41.784  1.00 11.34 ? 584  GLY A O   1 
ATOM   4502  N  N   . TYR A  1 585 ? 49.893  40.538 40.190  1.00 12.74 ? 585  TYR A N   1 
ATOM   4503  C  CA  . TYR A  1 585 ? 51.172  40.471 40.893  1.00 14.16 ? 585  TYR A CA  1 
ATOM   4504  C  C   . TYR A  1 585 ? 51.698  39.082 41.276  1.00 15.08 ? 585  TYR A C   1 
ATOM   4505  O  O   . TYR A  1 585 ? 52.611  38.952 42.112  1.00 14.01 ? 585  TYR A O   1 
ATOM   4506  C  CB  . TYR A  1 585 ? 51.062  41.358 42.133  1.00 14.84 ? 585  TYR A CB  1 
ATOM   4507  C  CG  . TYR A  1 585 ? 50.429  42.694 41.810  1.00 14.21 ? 585  TYR A CG  1 
ATOM   4508  C  CD1 . TYR A  1 585 ? 51.070  43.605 40.970  1.00 13.51 ? 585  TYR A CD1 1 
ATOM   4509  C  CD2 . TYR A  1 585 ? 49.167  43.026 42.304  1.00 14.95 ? 585  TYR A CD2 1 
ATOM   4510  C  CE1 . TYR A  1 585 ? 50.473  44.807 40.631  1.00 15.07 ? 585  TYR A CE1 1 
ATOM   4511  C  CE2 . TYR A  1 585 ? 48.555  44.236 41.964  1.00 15.38 ? 585  TYR A CE2 1 
ATOM   4512  C  CZ  . TYR A  1 585 ? 49.221  45.119 41.121  1.00 14.76 ? 585  TYR A CZ  1 
ATOM   4513  O  OH  . TYR A  1 585 ? 48.606  46.293 40.756  1.00 16.97 ? 585  TYR A OH  1 
ATOM   4514  N  N   . GLN A  1 586 ? 51.155  38.060 40.626  1.00 15.57 ? 586  GLN A N   1 
ATOM   4515  C  CA  . GLN A  1 586 ? 51.538  36.690 40.907  1.00 15.57 ? 586  GLN A CA  1 
ATOM   4516  C  C   . GLN A  1 586 ? 51.876  35.919 39.651  1.00 15.86 ? 586  GLN A C   1 
ATOM   4517  O  O   . GLN A  1 586 ? 51.917  34.686 39.680  1.00 16.54 ? 586  GLN A O   1 
ATOM   4518  C  CB  . GLN A  1 586 ? 50.394  35.982 41.604  1.00 15.06 ? 586  GLN A CB  1 
ATOM   4519  C  CG  . GLN A  1 586 ? 49.924  36.641 42.862  1.00 15.32 ? 586  GLN A CG  1 
ATOM   4520  C  CD  . GLN A  1 586 ? 48.486  36.254 43.159  1.00 17.46 ? 586  GLN A CD  1 
ATOM   4521  O  OE1 . GLN A  1 586 ? 48.213  35.171 43.690  1.00 18.61 ? 586  GLN A OE1 1 
ATOM   4522  N  NE2 . GLN A  1 586 ? 47.547  37.128 42.777  1.00 16.09 ? 586  GLN A NE2 1 
ATOM   4523  N  N   . GLY A  1 587 ? 52.091  36.633 38.551  1.00 15.25 ? 587  GLY A N   1 
ATOM   4524  C  CA  . GLY A  1 587 ? 52.420  35.972 37.301  1.00 15.73 ? 587  GLY A CA  1 
ATOM   4525  C  C   . GLY A  1 587 ? 51.226  35.814 36.385  1.00 15.97 ? 587  GLY A C   1 
ATOM   4526  O  O   . GLY A  1 587 ? 50.070  35.798 36.837  1.00 15.87 ? 587  GLY A O   1 
ATOM   4527  N  N   . ASP A  1 588 ? 51.519  35.670 35.098  1.00 16.35 ? 588  ASP A N   1 
ATOM   4528  C  CA  . ASP A  1 588 ? 50.510  35.524 34.045  1.00 17.97 ? 588  ASP A CA  1 
ATOM   4529  C  C   . ASP A  1 588 ? 49.663  34.257 34.097  1.00 18.02 ? 588  ASP A C   1 
ATOM   4530  O  O   . ASP A  1 588 ? 48.549  34.243 33.604  1.00 19.10 ? 588  ASP A O   1 
ATOM   4531  C  CB  . ASP A  1 588 ? 51.175  35.615 32.660  1.00 18.26 ? 588  ASP A CB  1 
ATOM   4532  C  CG  . ASP A  1 588 ? 51.720  36.998 32.371  1.00 19.91 ? 588  ASP A CG  1 
ATOM   4533  O  OD1 . ASP A  1 588 ? 51.384  37.927 33.132  1.00 19.60 ? 588  ASP A OD1 1 
ATOM   4534  O  OD2 . ASP A  1 588 ? 52.464  37.160 31.384  1.00 20.93 ? 588  ASP A OD2 1 
ATOM   4535  N  N   . LYS A  1 589 ? 50.195  33.188 34.661  1.00 18.47 ? 589  LYS A N   1 
ATOM   4536  C  CA  . LYS A  1 589 ? 49.426  31.959 34.736  1.00 20.07 ? 589  LYS A CA  1 
ATOM   4537  C  C   . LYS A  1 589 ? 48.117  32.264 35.462  1.00 18.95 ? 589  LYS A C   1 
ATOM   4538  O  O   . LYS A  1 589 ? 47.029  31.864 35.029  1.00 18.87 ? 589  LYS A O   1 
ATOM   4539  C  CB  . LYS A  1 589 ? 50.204  30.892 35.498  1.00 21.86 ? 589  LYS A CB  1 
ATOM   4540  C  CG  . LYS A  1 589 ? 49.386  29.644 35.757  1.00 27.03 ? 589  LYS A CG  1 
ATOM   4541  C  CD  . LYS A  1 589 ? 48.929  28.989 34.455  1.00 30.94 ? 589  LYS A CD  1 
ATOM   4542  C  CE  . LYS A  1 589 ? 48.034  27.774 34.716  1.00 32.63 ? 589  LYS A CE  1 
ATOM   4543  N  NZ  . LYS A  1 589 ? 48.661  26.851 35.707  1.00 35.73 ? 589  LYS A NZ  1 
ATOM   4544  N  N   . ILE A  1 590 ? 48.241  32.977 36.574  1.00 16.84 ? 590  ILE A N   1 
ATOM   4545  C  CA  . ILE A  1 590 ? 47.091  33.360 37.355  1.00 16.62 ? 590  ILE A CA  1 
ATOM   4546  C  C   . ILE A  1 590 ? 46.352  34.533 36.719  1.00 16.47 ? 590  ILE A C   1 
ATOM   4547  O  O   . ILE A  1 590 ? 45.143  34.441 36.448  1.00 17.43 ? 590  ILE A O   1 
ATOM   4548  C  CB  . ILE A  1 590 ? 47.516  33.711 38.807  1.00 16.53 ? 590  ILE A CB  1 
ATOM   4549  C  CG1 . ILE A  1 590 ? 47.851  32.420 39.557  1.00 16.60 ? 590  ILE A CG1 1 
ATOM   4550  C  CG2 . ILE A  1 590 ? 46.424  34.493 39.498  1.00 14.46 ? 590  ILE A CG2 1 
ATOM   4551  C  CD1 . ILE A  1 590 ? 48.446  32.612 40.953  1.00 18.79 ? 590  ILE A CD1 1 
ATOM   4552  N  N   . MET A  1 591 ? 47.059  35.625 36.437  1.00 15.96 ? 591  MET A N   1 
ATOM   4553  C  CA  . MET A  1 591 ? 46.392  36.798 35.872  1.00 16.24 ? 591  MET A CA  1 
ATOM   4554  C  C   . MET A  1 591 ? 45.678  36.587 34.536  1.00 16.95 ? 591  MET A C   1 
ATOM   4555  O  O   . MET A  1 591 ? 44.556  37.067 34.356  1.00 16.41 ? 591  MET A O   1 
ATOM   4556  C  CB  . MET A  1 591 ? 47.370  37.971 35.735  1.00 17.04 ? 591  MET A CB  1 
ATOM   4557  C  CG  . MET A  1 591 ? 46.668  39.285 35.427  1.00 16.74 ? 591  MET A CG  1 
ATOM   4558  S  SD  . MET A  1 591 ? 47.818  40.700 35.377  1.00 17.42 ? 591  MET A SD  1 
ATOM   4559  C  CE  . MET A  1 591 ? 48.643  40.434 33.769  1.00 17.96 ? 591  MET A CE  1 
ATOM   4560  N  N   . HIS A  1 592 ? 46.306  35.859 33.618  1.00 16.72 ? 592  HIS A N   1 
ATOM   4561  C  CA  . HIS A  1 592 ? 45.709  35.632 32.308  1.00 18.21 ? 592  HIS A CA  1 
ATOM   4562  C  C   . HIS A  1 592 ? 44.671  34.504 32.236  1.00 18.38 ? 592  HIS A C   1 
ATOM   4563  O  O   . HIS A  1 592 ? 44.119  34.249 31.171  1.00 18.61 ? 592  HIS A O   1 
ATOM   4564  C  CB  . HIS A  1 592 ? 46.805  35.381 31.271  1.00 18.05 ? 592  HIS A CB  1 
ATOM   4565  C  CG  . HIS A  1 592 ? 47.594  36.608 30.922  1.00 19.45 ? 592  HIS A CG  1 
ATOM   4566  N  ND1 . HIS A  1 592 ? 48.755  36.560 30.177  1.00 19.12 ? 592  HIS A ND1 1 
ATOM   4567  C  CD2 . HIS A  1 592 ? 47.373  37.920 31.188  1.00 18.44 ? 592  HIS A CD2 1 
ATOM   4568  C  CE1 . HIS A  1 592 ? 49.213  37.787 29.997  1.00 19.14 ? 592  HIS A CE1 1 
ATOM   4569  N  NE2 . HIS A  1 592 ? 48.392  38.631 30.598  1.00 19.47 ? 592  HIS A NE2 1 
ATOM   4570  N  N   . ALA A  1 593 ? 44.397  33.839 33.353  1.00 19.14 ? 593  ALA A N   1 
ATOM   4571  C  CA  . ALA A  1 593 ? 43.420  32.746 33.349  1.00 19.42 ? 593  ALA A CA  1 
ATOM   4572  C  C   . ALA A  1 593 ? 42.059  33.230 32.880  1.00 19.70 ? 593  ALA A C   1 
ATOM   4573  O  O   . ALA A  1 593 ? 41.269  32.439 32.400  1.00 20.58 ? 593  ALA A O   1 
ATOM   4574  C  CB  . ALA A  1 593 ? 43.302  32.136 34.728  1.00 19.08 ? 593  ALA A CB  1 
ATOM   4575  N  N   . ILE A  1 594 ? 41.759  34.520 33.033  1.00 19.44 ? 594  ILE A N   1 
ATOM   4576  C  CA  . ILE A  1 594 ? 40.463  35.014 32.568  1.00 19.76 ? 594  ILE A CA  1 
ATOM   4577  C  C   . ILE A  1 594 ? 40.499  35.761 31.251  1.00 18.58 ? 594  ILE A C   1 
ATOM   4578  O  O   . ILE A  1 594 ? 39.533  36.444 30.900  1.00 19.56 ? 594  ILE A O   1 
ATOM   4579  C  CB  . ILE A  1 594 ? 39.732  35.912 33.601  1.00 20.27 ? 594  ILE A CB  1 
ATOM   4580  C  CG1 . ILE A  1 594 ? 40.589  37.109 34.005  1.00 20.39 ? 594  ILE A CG1 1 
ATOM   4581  C  CG2 . ILE A  1 594 ? 39.349  35.096 34.796  1.00 22.00 ? 594  ILE A CG2 1 
ATOM   4582  C  CD1 . ILE A  1 594 ? 39.906  37.969 35.063  1.00 22.69 ? 594  ILE A CD1 1 
ATOM   4583  N  N   . ASN A  1 595 ? 41.593  35.616 30.512  1.00 18.34 ? 595  ASN A N   1 
ATOM   4584  C  CA  . ASN A  1 595 ? 41.720  36.270 29.211  1.00 18.93 ? 595  ASN A CA  1 
ATOM   4585  C  C   . ASN A  1 595 ? 40.564  35.836 28.312  1.00 19.18 ? 595  ASN A C   1 
ATOM   4586  O  O   . ASN A  1 595 ? 40.256  34.662 28.216  1.00 18.32 ? 595  ASN A O   1 
ATOM   4587  C  CB  . ASN A  1 595 ? 43.043  35.900 28.541  1.00 18.00 ? 595  ASN A CB  1 
ATOM   4588  C  CG  . ASN A  1 595 ? 43.238  36.599 27.187  1.00 18.93 ? 595  ASN A CG  1 
ATOM   4589  O  OD1 . ASN A  1 595 ? 43.635  35.973 26.210  1.00 21.08 ? 595  ASN A OD1 1 
ATOM   4590  N  ND2 . ASN A  1 595 ? 42.978  37.894 27.136  1.00 17.66 ? 595  ASN A ND2 1 
ATOM   4591  N  N   . ARG A  1 596 ? 39.911  36.808 27.690  1.00 19.33 ? 596  ARG A N   1 
ATOM   4592  C  CA  . ARG A  1 596 ? 38.789  36.553 26.802  1.00 19.54 ? 596  ARG A CA  1 
ATOM   4593  C  C   . ARG A  1 596 ? 37.633  35.858 27.497  1.00 18.72 ? 596  ARG A C   1 
ATOM   4594  O  O   . ARG A  1 596 ? 36.675  35.453 26.854  1.00 18.52 ? 596  ARG A O   1 
ATOM   4595  C  CB  . ARG A  1 596 ? 39.247  35.745 25.582  1.00 20.22 ? 596  ARG A CB  1 
ATOM   4596  C  CG  . ARG A  1 596 ? 40.279  36.489 24.726  1.00 21.74 ? 596  ARG A CG  1 
ATOM   4597  C  CD  . ARG A  1 596 ? 40.743  35.649 23.528  1.00 22.58 ? 596  ARG A CD  1 
ATOM   4598  N  NE  . ARG A  1 596 ? 39.629  35.216 22.679  1.00 23.95 ? 596  ARG A NE  1 
ATOM   4599  C  CZ  . ARG A  1 596 ? 39.087  35.933 21.700  1.00 24.28 ? 596  ARG A CZ  1 
ATOM   4600  N  NH1 . ARG A  1 596 ? 39.542  37.150 21.407  1.00 24.47 ? 596  ARG A NH1 1 
ATOM   4601  N  NH2 . ARG A  1 596 ? 38.084  35.418 21.000  1.00 25.20 ? 596  ARG A NH2 1 
ATOM   4602  N  N   . ARG A  1 597 ? 37.700  35.757 28.820  1.00 19.98 ? 597  ARG A N   1 
ATOM   4603  C  CA  . ARG A  1 597 ? 36.642  35.091 29.578  1.00 20.54 ? 597  ARG A CA  1 
ATOM   4604  C  C   . ARG A  1 597 ? 36.266  35.751 30.916  1.00 19.39 ? 597  ARG A C   1 
ATOM   4605  O  O   . ARG A  1 597 ? 36.242  35.093 31.961  1.00 18.40 ? 597  ARG A O   1 
ATOM   4606  C  CB  . ARG A  1 597 ? 37.033  33.627 29.820  1.00 22.97 ? 597  ARG A CB  1 
ATOM   4607  C  CG  . ARG A  1 597 ? 36.437  32.657 28.802  1.00 28.87 ? 597  ARG A CG  1 
ATOM   4608  C  CD  . ARG A  1 597 ? 37.241  32.604 27.514  1.00 34.11 ? 597  ARG A CD  1 
ATOM   4609  N  NE  . ARG A  1 597 ? 36.734  31.591 26.579  1.00 37.44 ? 597  ARG A NE  1 
ATOM   4610  C  CZ  . ARG A  1 597 ? 35.990  31.857 25.509  1.00 38.41 ? 597  ARG A CZ  1 
ATOM   4611  N  NH1 . ARG A  1 597 ? 35.651  33.110 25.220  1.00 38.74 ? 597  ARG A NH1 1 
ATOM   4612  N  NH2 . ARG A  1 597 ? 35.604  30.868 24.717  1.00 38.75 ? 597  ARG A NH2 1 
ATOM   4613  N  N   . LEU A  1 598 ? 35.971  37.045 30.894  1.00 17.16 ? 598  LEU A N   1 
ATOM   4614  C  CA  . LEU A  1 598 ? 35.594  37.718 32.138  1.00 17.12 ? 598  LEU A CA  1 
ATOM   4615  C  C   . LEU A  1 598 ? 34.283  37.110 32.622  1.00 16.75 ? 598  LEU A C   1 
ATOM   4616  O  O   . LEU A  1 598 ? 33.481  36.628 31.819  1.00 16.47 ? 598  LEU A O   1 
ATOM   4617  C  CB  . LEU A  1 598 ? 35.403  39.220 31.915  1.00 16.15 ? 598  LEU A CB  1 
ATOM   4618  C  CG  . LEU A  1 598 ? 36.592  40.020 31.380  1.00 14.91 ? 598  LEU A CG  1 
ATOM   4619  C  CD1 . LEU A  1 598 ? 36.246  41.488 31.502  1.00 15.77 ? 598  LEU A CD1 1 
ATOM   4620  C  CD2 . LEU A  1 598 ? 37.848  39.724 32.178  1.00 13.03 ? 598  LEU A CD2 1 
ATOM   4621  N  N   . GLY A  1 599 ? 34.061  37.115 33.928  1.00 16.09 ? 599  GLY A N   1 
ATOM   4622  C  CA  . GLY A  1 599 ? 32.820  36.561 34.439  1.00 15.68 ? 599  GLY A CA  1 
ATOM   4623  C  C   . GLY A  1 599 ? 32.825  35.044 34.554  1.00 15.68 ? 599  GLY A C   1 
ATOM   4624  O  O   . GLY A  1 599 ? 31.770  34.428 34.638  1.00 16.81 ? 599  GLY A O   1 
ATOM   4625  N  N   . THR A  1 600 ? 33.994  34.422 34.550  1.00 15.82 ? 600  THR A N   1 
ATOM   4626  C  CA  . THR A  1 600 ? 34.020  32.966 34.693  1.00 16.47 ? 600  THR A CA  1 
ATOM   4627  C  C   . THR A  1 600 ? 34.825  32.529 35.913  1.00 15.94 ? 600  THR A C   1 
ATOM   4628  O  O   . THR A  1 600 ? 34.270  32.425 37.003  1.00 16.97 ? 600  THR A O   1 
ATOM   4629  C  CB  . THR A  1 600 ? 34.576  32.236 33.417  1.00 15.83 ? 600  THR A CB  1 
ATOM   4630  O  OG1 . THR A  1 600 ? 35.915  32.673 33.149  1.00 16.52 ? 600  THR A OG1 1 
ATOM   4631  C  CG2 . THR A  1 600 ? 33.695  32.530 32.187  1.00 16.27 ? 600  THR A CG2 1 
ATOM   4632  N  N   . PHE A  1 601 ? 36.130  32.307 35.747  1.00 17.06 ? 601  PHE A N   1 
ATOM   4633  C  CA  . PHE A  1 601 ? 36.961  31.824 36.850  1.00 17.47 ? 601  PHE A CA  1 
ATOM   4634  C  C   . PHE A  1 601 ? 37.069  32.755 38.043  1.00 17.28 ? 601  PHE A C   1 
ATOM   4635  O  O   . PHE A  1 601 ? 37.122  32.284 39.174  1.00 17.83 ? 601  PHE A O   1 
ATOM   4636  C  CB  . PHE A  1 601 ? 38.384  31.476 36.388  1.00 18.68 ? 601  PHE A CB  1 
ATOM   4637  C  CG  . PHE A  1 601 ? 38.445  30.441 35.303  1.00 21.86 ? 601  PHE A CG  1 
ATOM   4638  C  CD1 . PHE A  1 601 ? 37.747  29.246 35.416  1.00 22.84 ? 601  PHE A CD1 1 
ATOM   4639  C  CD2 . PHE A  1 601 ? 39.238  30.650 34.178  1.00 23.34 ? 601  PHE A CD2 1 
ATOM   4640  C  CE1 . PHE A  1 601 ? 37.836  28.269 34.423  1.00 25.83 ? 601  PHE A CE1 1 
ATOM   4641  C  CE2 . PHE A  1 601 ? 39.336  29.685 33.181  1.00 26.13 ? 601  PHE A CE2 1 
ATOM   4642  C  CZ  . PHE A  1 601 ? 38.636  28.490 33.298  1.00 25.52 ? 601  PHE A CZ  1 
ATOM   4643  N  N   . GLU A  1 602 ? 37.118  34.063 37.808  1.00 16.50 ? 602  GLU A N   1 
ATOM   4644  C  CA  . GLU A  1 602 ? 37.232  34.981 38.924  1.00 16.48 ? 602  GLU A CA  1 
ATOM   4645  C  C   . GLU A  1 602 ? 35.938  34.922 39.759  1.00 16.65 ? 602  GLU A C   1 
ATOM   4646  O  O   . GLU A  1 602 ? 35.954  35.096 40.982  1.00 17.04 ? 602  GLU A O   1 
ATOM   4647  C  CB  . GLU A  1 602 ? 37.575  36.408 38.434  1.00 16.13 ? 602  GLU A CB  1 
ATOM   4648  C  CG  . GLU A  1 602 ? 36.414  37.277 37.922  1.00 15.51 ? 602  GLU A CG  1 
ATOM   4649  C  CD  . GLU A  1 602 ? 35.995  36.976 36.492  1.00 17.51 ? 602  GLU A CD  1 
ATOM   4650  O  OE1 . GLU A  1 602 ? 35.455  37.904 35.843  1.00 15.89 ? 602  GLU A OE1 1 
ATOM   4651  O  OE2 . GLU A  1 602 ? 36.182  35.831 36.014  1.00 15.86 ? 602  GLU A OE2 1 
ATOM   4652  N  N   . VAL A  1 603 ? 34.820  34.637 39.104  1.00 16.30 ? 603  VAL A N   1 
ATOM   4653  C  CA  . VAL A  1 603 ? 33.546  34.513 39.816  1.00 17.06 ? 603  VAL A CA  1 
ATOM   4654  C  C   . VAL A  1 603 ? 33.518  33.169 40.560  1.00 18.21 ? 603  VAL A C   1 
ATOM   4655  O  O   . VAL A  1 603 ? 33.213  33.119 41.755  1.00 17.96 ? 603  VAL A O   1 
ATOM   4656  C  CB  . VAL A  1 603 ? 32.346  34.560 38.838  1.00 16.93 ? 603  VAL A CB  1 
ATOM   4657  C  CG1 . VAL A  1 603 ? 31.043  34.271 39.587  1.00 15.42 ? 603  VAL A CG1 1 
ATOM   4658  C  CG2 . VAL A  1 603 ? 32.275  35.941 38.181  1.00 15.21 ? 603  VAL A CG2 1 
ATOM   4659  N  N   . GLU A  1 604 ? 33.851  32.094 39.845  1.00 18.47 ? 604  GLU A N   1 
ATOM   4660  C  CA  . GLU A  1 604 ? 33.872  30.746 40.414  1.00 20.94 ? 604  GLU A CA  1 
ATOM   4661  C  C   . GLU A  1 604 ? 34.797  30.647 41.621  1.00 19.98 ? 604  GLU A C   1 
ATOM   4662  O  O   . GLU A  1 604 ? 34.452  30.016 42.623  1.00 19.41 ? 604  GLU A O   1 
ATOM   4663  C  CB  . GLU A  1 604 ? 34.322  29.723 39.359  1.00 23.42 ? 604  GLU A CB  1 
ATOM   4664  C  CG  . GLU A  1 604 ? 33.331  29.513 38.219  1.00 29.05 ? 604  GLU A CG  1 
ATOM   4665  C  CD  . GLU A  1 604 ? 33.990  28.967 36.951  1.00 32.37 ? 604  GLU A CD  1 
ATOM   4666  O  OE1 . GLU A  1 604 ? 34.797  28.007 37.060  1.00 33.67 ? 604  GLU A OE1 1 
ATOM   4667  O  OE2 . GLU A  1 604 ? 33.698  29.494 35.844  1.00 34.17 ? 604  GLU A OE2 1 
ATOM   4668  N  N   . ASP A  1 605 ? 35.975  31.269 41.531  1.00 19.53 ? 605  ASP A N   1 
ATOM   4669  C  CA  . ASP A  1 605 ? 36.931  31.211 42.638  1.00 18.86 ? 605  ASP A CA  1 
ATOM   4670  C  C   . ASP A  1 605 ? 36.452  31.916 43.906  1.00 17.27 ? 605  ASP A C   1 
ATOM   4671  O  O   . ASP A  1 605 ? 36.829  31.514 45.007  1.00 17.44 ? 605  ASP A O   1 
ATOM   4672  C  CB  . ASP A  1 605 ? 38.307  31.740 42.200  1.00 19.82 ? 605  ASP A CB  1 
ATOM   4673  C  CG  . ASP A  1 605 ? 38.993  30.810 41.200  1.00 21.60 ? 605  ASP A CG  1 
ATOM   4674  O  OD1 . ASP A  1 605 ? 38.474  29.685 40.994  1.00 21.00 ? 605  ASP A OD1 1 
ATOM   4675  O  OD2 . ASP A  1 605 ? 40.049  31.193 40.622  1.00 21.74 ? 605  ASP A OD2 1 
ATOM   4676  N  N   . GLN A  1 606 ? 35.637  32.961 43.767  1.00 15.30 ? 606  GLN A N   1 
ATOM   4677  C  CA  . GLN A  1 606 ? 35.087  33.632 44.940  1.00 15.93 ? 606  GLN A CA  1 
ATOM   4678  C  C   . GLN A  1 606 ? 34.091  32.671 45.628  1.00 16.26 ? 606  GLN A C   1 
ATOM   4679  O  O   . GLN A  1 606 ? 34.015  32.619 46.852  1.00 14.44 ? 606  GLN A O   1 
ATOM   4680  C  CB  . GLN A  1 606 ? 34.350  34.930 44.554  1.00 15.41 ? 606  GLN A CB  1 
ATOM   4681  C  CG  . GLN A  1 606 ? 35.260  36.073 44.044  1.00 14.63 ? 606  GLN A CG  1 
ATOM   4682  C  CD  . GLN A  1 606 ? 36.199  36.562 45.126  1.00 14.57 ? 606  GLN A CD  1 
ATOM   4683  O  OE1 . GLN A  1 606 ? 35.756  36.909 46.222  1.00 14.72 ? 606  GLN A OE1 1 
ATOM   4684  N  NE2 . GLN A  1 606 ? 37.498  36.595 44.829  1.00 13.04 ? 606  GLN A NE2 1 
ATOM   4685  N  N   . ILE A  1 607 ? 33.313  31.929 44.840  1.00 17.02 ? 607  ILE A N   1 
ATOM   4686  C  CA  . ILE A  1 607 ? 32.354  30.999 45.429  1.00 17.32 ? 607  ILE A CA  1 
ATOM   4687  C  C   . ILE A  1 607 ? 33.159  29.906 46.150  1.00 18.22 ? 607  ILE A C   1 
ATOM   4688  O  O   . ILE A  1 607 ? 32.851  29.559 47.280  1.00 18.67 ? 607  ILE A O   1 
ATOM   4689  C  CB  . ILE A  1 607 ? 31.443  30.385 44.351  1.00 17.75 ? 607  ILE A CB  1 
ATOM   4690  C  CG1 . ILE A  1 607 ? 30.665  31.497 43.641  1.00 17.34 ? 607  ILE A CG1 1 
ATOM   4691  C  CG2 . ILE A  1 607 ? 30.448  29.396 44.987  1.00 16.51 ? 607  ILE A CG2 1 
ATOM   4692  C  CD1 . ILE A  1 607 ? 29.805  30.988 42.501  1.00 16.03 ? 607  ILE A CD1 1 
ATOM   4693  N  N   . GLU A  1 608 ? 34.215  29.399 45.511  1.00 20.20 ? 608  GLU A N   1 
ATOM   4694  C  CA  . GLU A  1 608 ? 35.073  28.361 46.119  1.00 20.63 ? 608  GLU A CA  1 
ATOM   4695  C  C   . GLU A  1 608 ? 35.675  28.823 47.444  1.00 20.18 ? 608  GLU A C   1 
ATOM   4696  O  O   . GLU A  1 608 ? 35.698  28.080 48.419  1.00 19.68 ? 608  GLU A O   1 
ATOM   4697  C  CB  . GLU A  1 608 ? 36.246  28.018 45.208  1.00 21.37 ? 608  GLU A CB  1 
ATOM   4698  C  CG  . GLU A  1 608 ? 36.375  26.588 44.724  1.00 24.28 ? 608  GLU A CG  1 
ATOM   4699  C  CD  . GLU A  1 608 ? 36.114  25.513 45.773  1.00 24.98 ? 608  GLU A CD  1 
ATOM   4700  O  OE1 . GLU A  1 608 ? 34.980  25.001 45.773  1.00 26.26 ? 608  GLU A OE1 1 
ATOM   4701  O  OE2 . GLU A  1 608 ? 37.021  25.176 46.569  1.00 24.50 ? 608  GLU A OE2 1 
ATOM   4702  N  N   . ALA A  1 609 ? 36.201  30.042 47.466  1.00 20.12 ? 609  ALA A N   1 
ATOM   4703  C  CA  . ALA A  1 609 ? 36.806  30.572 48.681  1.00 19.43 ? 609  ALA A CA  1 
ATOM   4704  C  C   . ALA A  1 609 ? 35.762  30.652 49.792  1.00 19.21 ? 609  ALA A C   1 
ATOM   4705  O  O   . ALA A  1 609 ? 36.034  30.253 50.927  1.00 18.53 ? 609  ALA A O   1 
ATOM   4706  C  CB  . ALA A  1 609 ? 37.416  31.956 48.418  1.00 19.11 ? 609  ALA A CB  1 
ATOM   4707  N  N   . ALA A  1 610 ? 34.576  31.160 49.473  1.00 18.69 ? 610  ALA A N   1 
ATOM   4708  C  CA  . ALA A  1 610 ? 33.514  31.261 50.483  1.00 20.40 ? 610  ALA A CA  1 
ATOM   4709  C  C   . ALA A  1 610 ? 33.140  29.856 50.945  1.00 22.37 ? 610  ALA A C   1 
ATOM   4710  O  O   . ALA A  1 610 ? 32.904  29.610 52.137  1.00 21.76 ? 610  ALA A O   1 
ATOM   4711  C  CB  . ALA A  1 610 ? 32.296  31.938 49.910  1.00 19.26 ? 610  ALA A CB  1 
ATOM   4712  N  N   . ARG A  1 611 ? 33.087  28.942 49.984  1.00 23.23 ? 611  ARG A N   1 
ATOM   4713  C  CA  . ARG A  1 611 ? 32.757  27.559 50.268  1.00 25.66 ? 611  ARG A CA  1 
ATOM   4714  C  C   . ARG A  1 611 ? 33.757  27.061 51.308  1.00 26.72 ? 611  ARG A C   1 
ATOM   4715  O  O   . ARG A  1 611 ? 33.377  26.483 52.316  1.00 26.53 ? 611  ARG A O   1 
ATOM   4716  C  CB  . ARG A  1 611 ? 32.844  26.746 48.974  1.00 26.47 ? 611  ARG A CB  1 
ATOM   4717  C  CG  . ARG A  1 611 ? 32.253  25.372 49.039  1.00 27.01 ? 611  ARG A CG  1 
ATOM   4718  C  CD  . ARG A  1 611 ? 32.323  24.705 47.678  1.00 26.40 ? 611  ARG A CD  1 
ATOM   4719  N  NE  . ARG A  1 611 ? 31.216  25.070 46.803  1.00 27.22 ? 611  ARG A NE  1 
ATOM   4720  C  CZ  . ARG A  1 611 ? 31.355  25.538 45.565  1.00 27.72 ? 611  ARG A CZ  1 
ATOM   4721  N  NH1 . ARG A  1 611 ? 32.567  25.721 45.040  1.00 26.14 ? 611  ARG A NH1 1 
ATOM   4722  N  NH2 . ARG A  1 611 ? 30.278  25.789 44.836  1.00 27.39 ? 611  ARG A NH2 1 
ATOM   4723  N  N   . GLN A  1 612 ? 35.041  27.302 51.073  1.00 27.64 ? 612  GLN A N   1 
ATOM   4724  C  CA  . GLN A  1 612 ? 36.055  26.871 52.026  1.00 28.65 ? 612  GLN A CA  1 
ATOM   4725  C  C   . GLN A  1 612 ? 35.912  27.581 53.374  1.00 29.27 ? 612  GLN A C   1 
ATOM   4726  O  O   . GLN A  1 612 ? 35.875  26.923 54.418  1.00 29.95 ? 612  GLN A O   1 
ATOM   4727  C  CB  . GLN A  1 612 ? 37.446  27.083 51.442  1.00 28.94 ? 612  GLN A CB  1 
ATOM   4728  C  CG  . GLN A  1 612 ? 37.598  26.317 50.145  1.00 30.41 ? 612  GLN A CG  1 
ATOM   4729  C  CD  . GLN A  1 612 ? 38.966  25.746 49.952  1.00 29.65 ? 612  GLN A CD  1 
ATOM   4730  O  OE1 . GLN A  1 612 ? 39.769  25.712 50.879  1.00 29.49 ? 612  GLN A OE1 1 
ATOM   4731  N  NE2 . GLN A  1 612 ? 39.244  25.274 48.741  1.00 31.27 ? 612  GLN A NE2 1 
ATOM   4732  N  N   . PHE A  1 613 ? 35.809  28.909 53.355  1.00 28.29 ? 613  PHE A N   1 
ATOM   4733  C  CA  . PHE A  1 613 ? 35.648  29.666 54.592  1.00 27.68 ? 613  PHE A CA  1 
ATOM   4734  C  C   . PHE A  1 613 ? 34.470  29.119 55.399  1.00 28.35 ? 613  PHE A C   1 
ATOM   4735  O  O   . PHE A  1 613 ? 34.547  29.016 56.620  1.00 28.60 ? 613  PHE A O   1 
ATOM   4736  C  CB  . PHE A  1 613 ? 35.408  31.156 54.305  1.00 25.49 ? 613  PHE A CB  1 
ATOM   4737  C  CG  . PHE A  1 613 ? 36.523  31.825 53.532  1.00 24.30 ? 613  PHE A CG  1 
ATOM   4738  C  CD1 . PHE A  1 613 ? 37.836  31.382 53.647  1.00 22.71 ? 613  PHE A CD1 1 
ATOM   4739  C  CD2 . PHE A  1 613 ? 36.261  32.928 52.715  1.00 23.43 ? 613  PHE A CD2 1 
ATOM   4740  C  CE1 . PHE A  1 613 ? 38.884  32.025 52.959  1.00 22.42 ? 613  PHE A CE1 1 
ATOM   4741  C  CE2 . PHE A  1 613 ? 37.308  33.578 52.022  1.00 22.53 ? 613  PHE A CE2 1 
ATOM   4742  C  CZ  . PHE A  1 613 ? 38.612  33.125 52.147  1.00 20.28 ? 613  PHE A CZ  1 
ATOM   4743  N  N   . SER A  1 614 ? 33.389  28.766 54.709  1.00 29.79 ? 614  SER A N   1 
ATOM   4744  C  CA  . SER A  1 614 ? 32.191  28.244 55.362  1.00 32.35 ? 614  SER A CA  1 
ATOM   4745  C  C   . SER A  1 614 ? 32.401  26.888 56.016  1.00 33.50 ? 614  SER A C   1 
ATOM   4746  O  O   . SER A  1 614 ? 31.550  26.439 56.774  1.00 35.04 ? 614  SER A O   1 
ATOM   4747  C  CB  . SER A  1 614 ? 31.036  28.110 54.370  1.00 32.70 ? 614  SER A CB  1 
ATOM   4748  O  OG  . SER A  1 614 ? 31.109  26.865 53.700  1.00 33.39 ? 614  SER A OG  1 
ATOM   4749  N  N   . LYS A  1 615 ? 33.521  26.238 55.716  1.00 35.07 ? 615  LYS A N   1 
ATOM   4750  C  CA  . LYS A  1 615 ? 33.828  24.935 56.292  1.00 36.54 ? 615  LYS A CA  1 
ATOM   4751  C  C   . LYS A  1 615 ? 34.588  25.129 57.596  1.00 36.80 ? 615  LYS A C   1 
ATOM   4752  O  O   . LYS A  1 615 ? 34.616  24.239 58.448  1.00 38.52 ? 615  LYS A O   1 
ATOM   4753  C  CB  . LYS A  1 615 ? 34.688  24.097 55.336  1.00 37.42 ? 615  LYS A CB  1 
ATOM   4754  C  CG  . LYS A  1 615 ? 34.034  23.801 53.983  1.00 39.13 ? 615  LYS A CG  1 
ATOM   4755  C  CD  . LYS A  1 615 ? 33.639  22.343 53.829  1.00 38.16 ? 615  LYS A CD  1 
ATOM   4756  C  CE  . LYS A  1 615 ? 32.812  22.103 52.560  1.00 38.42 ? 615  LYS A CE  1 
ATOM   4757  N  NZ  . LYS A  1 615 ? 33.570  22.202 51.268  1.00 37.23 ? 615  LYS A NZ  1 
ATOM   4758  N  N   . MET A  1 616 ? 35.207  26.291 57.761  1.00 36.21 ? 616  MET A N   1 
ATOM   4759  C  CA  . MET A  1 616 ? 35.960  26.547 58.977  1.00 35.02 ? 616  MET A CA  1 
ATOM   4760  C  C   . MET A  1 616 ? 35.048  26.638 60.194  1.00 33.82 ? 616  MET A C   1 
ATOM   4761  O  O   . MET A  1 616 ? 33.912  27.132 60.121  1.00 33.38 ? 616  MET A O   1 
ATOM   4762  C  CB  . MET A  1 616 ? 36.809  27.816 58.827  1.00 36.27 ? 616  MET A CB  1 
ATOM   4763  C  CG  . MET A  1 616 ? 37.968  27.649 57.837  1.00 37.30 ? 616  MET A CG  1 
ATOM   4764  S  SD  . MET A  1 616 ? 38.572  29.235 57.196  1.00 39.61 ? 616  MET A SD  1 
ATOM   4765  C  CE  . MET A  1 616 ? 40.235  28.818 56.676  1.00 37.27 ? 616  MET A CE  1 
ATOM   4766  N  N   . GLY A  1 617 ? 35.571  26.163 61.318  1.00 32.44 ? 617  GLY A N   1 
ATOM   4767  C  CA  . GLY A  1 617 ? 34.805  26.140 62.548  1.00 31.21 ? 617  GLY A CA  1 
ATOM   4768  C  C   . GLY A  1 617 ? 34.278  27.462 63.045  1.00 30.29 ? 617  GLY A C   1 
ATOM   4769  O  O   . GLY A  1 617 ? 33.279  27.493 63.764  1.00 31.37 ? 617  GLY A O   1 
ATOM   4770  N  N   . PHE A  1 618 ? 34.919  28.558 62.654  1.00 28.31 ? 618  PHE A N   1 
ATOM   4771  C  CA  . PHE A  1 618 ? 34.499  29.863 63.137  1.00 26.45 ? 618  PHE A CA  1 
ATOM   4772  C  C   . PHE A  1 618 ? 33.547  30.652 62.232  1.00 24.44 ? 618  PHE A C   1 
ATOM   4773  O  O   . PHE A  1 618 ? 33.251  31.801 62.509  1.00 24.15 ? 618  PHE A O   1 
ATOM   4774  C  CB  . PHE A  1 618 ? 35.751  30.696 63.479  1.00 27.08 ? 618  PHE A CB  1 
ATOM   4775  C  CG  . PHE A  1 618 ? 36.716  30.860 62.326  1.00 27.49 ? 618  PHE A CG  1 
ATOM   4776  C  CD1 . PHE A  1 618 ? 36.521  31.858 61.372  1.00 26.84 ? 618  PHE A CD1 1 
ATOM   4777  C  CD2 . PHE A  1 618 ? 37.819  30.014 62.192  1.00 27.68 ? 618  PHE A CD2 1 
ATOM   4778  C  CE1 . PHE A  1 618 ? 37.415  32.012 60.295  1.00 26.36 ? 618  PHE A CE1 1 
ATOM   4779  C  CE2 . PHE A  1 618 ? 38.718  30.157 61.122  1.00 26.82 ? 618  PHE A CE2 1 
ATOM   4780  C  CZ  . PHE A  1 618 ? 38.510  31.162 60.172  1.00 27.35 ? 618  PHE A CZ  1 
ATOM   4781  N  N   . VAL A  1 619 ? 33.051  30.025 61.173  1.00 23.36 ? 619  VAL A N   1 
ATOM   4782  C  CA  . VAL A  1 619 ? 32.136  30.691 60.243  1.00 22.94 ? 619  VAL A CA  1 
ATOM   4783  C  C   . VAL A  1 619 ? 30.713  30.120 60.316  1.00 22.82 ? 619  VAL A C   1 
ATOM   4784  O  O   . VAL A  1 619 ? 30.530  28.913 60.391  1.00 22.79 ? 619  VAL A O   1 
ATOM   4785  C  CB  . VAL A  1 619 ? 32.671  30.564 58.789  1.00 22.31 ? 619  VAL A CB  1 
ATOM   4786  C  CG1 . VAL A  1 619 ? 31.685  31.150 57.784  1.00 22.09 ? 619  VAL A CG1 1 
ATOM   4787  C  CG2 . VAL A  1 619 ? 34.012  31.295 58.680  1.00 23.49 ? 619  VAL A CG2 1 
ATOM   4788  N  N   . ASP A  1 620 ? 29.707  30.988 60.328  1.00 23.24 ? 620  ASP A N   1 
ATOM   4789  C  CA  . ASP A  1 620 ? 28.321  30.526 60.362  1.00 23.23 ? 620  ASP A CA  1 
ATOM   4790  C  C   . ASP A  1 620 ? 27.838  30.369 58.921  1.00 23.73 ? 620  ASP A C   1 
ATOM   4791  O  O   . ASP A  1 620 ? 27.496  31.357 58.277  1.00 23.14 ? 620  ASP A O   1 
ATOM   4792  C  CB  . ASP A  1 620 ? 27.446  31.546 61.069  1.00 23.88 ? 620  ASP A CB  1 
ATOM   4793  C  CG  . ASP A  1 620 ? 25.994  31.094 61.158  1.00 23.60 ? 620  ASP A CG  1 
ATOM   4794  O  OD1 . ASP A  1 620 ? 25.651  30.038 60.589  1.00 23.81 ? 620  ASP A OD1 1 
ATOM   4795  O  OD2 . ASP A  1 620 ? 25.210  31.806 61.790  1.00 24.03 ? 620  ASP A OD2 1 
ATOM   4796  N  N   . ASN A  1 621 ? 27.787  29.134 58.431  1.00 23.39 ? 621  ASN A N   1 
ATOM   4797  C  CA  . ASN A  1 621 ? 27.401  28.884 57.053  1.00 25.37 ? 621  ASN A CA  1 
ATOM   4798  C  C   . ASN A  1 621 ? 25.983  29.320 56.698  1.00 25.17 ? 621  ASN A C   1 
ATOM   4799  O  O   . ASN A  1 621 ? 25.598  29.276 55.539  1.00 26.12 ? 621  ASN A O   1 
ATOM   4800  C  CB  . ASN A  1 621 ? 27.608  27.400 56.687  1.00 27.40 ? 621  ASN A CB  1 
ATOM   4801  C  CG  . ASN A  1 621 ? 26.634  26.466 57.405  1.00 29.50 ? 621  ASN A CG  1 
ATOM   4802  O  OD1 . ASN A  1 621 ? 26.784  25.254 57.343  1.00 32.63 ? 621  ASN A OD1 1 
ATOM   4803  N  ND2 . ASN A  1 621 ? 25.635  27.027 58.078  1.00 30.36 ? 621  ASN A ND2 1 
ATOM   4804  N  N   . LYS A  1 622 ? 25.210  29.745 57.690  1.00 24.76 ? 622  LYS A N   1 
ATOM   4805  C  CA  . LYS A  1 622 ? 23.846  30.190 57.433  1.00 24.97 ? 622  LYS A CA  1 
ATOM   4806  C  C   . LYS A  1 622 ? 23.846  31.699 57.219  1.00 23.25 ? 622  LYS A C   1 
ATOM   4807  O  O   . LYS A  1 622 ? 22.836  32.279 56.817  1.00 23.09 ? 622  LYS A O   1 
ATOM   4808  C  CB  . LYS A  1 622 ? 22.928  29.846 58.618  1.00 26.60 ? 622  LYS A CB  1 
ATOM   4809  C  CG  . LYS A  1 622 ? 22.897  28.351 58.961  1.00 29.86 ? 622  LYS A CG  1 
ATOM   4810  C  CD  . LYS A  1 622 ? 21.979  28.053 60.171  1.00 33.53 ? 622  LYS A CD  1 
ATOM   4811  C  CE  . LYS A  1 622 ? 22.396  28.802 61.453  1.00 34.59 ? 622  LYS A CE  1 
ATOM   4812  N  NZ  . LYS A  1 622 ? 23.749  28.411 61.989  1.00 35.22 ? 622  LYS A NZ  1 
ATOM   4813  N  N   . ARG A  1 623 ? 24.989  32.324 57.491  1.00 20.86 ? 623  ARG A N   1 
ATOM   4814  C  CA  . ARG A  1 623 ? 25.119  33.765 57.370  1.00 19.64 ? 623  ARG A CA  1 
ATOM   4815  C  C   . ARG A  1 623 ? 26.379  34.204 56.629  1.00 18.48 ? 623  ARG A C   1 
ATOM   4816  O  O   . ARG A  1 623 ? 27.319  34.741 57.211  1.00 18.38 ? 623  ARG A O   1 
ATOM   4817  C  CB  . ARG A  1 623 ? 25.084  34.395 58.759  1.00 19.64 ? 623  ARG A CB  1 
ATOM   4818  C  CG  . ARG A  1 623 ? 23.740  34.271 59.472  1.00 22.58 ? 623  ARG A CG  1 
ATOM   4819  C  CD  . ARG A  1 623 ? 23.984  34.146 60.974  1.00 24.91 ? 623  ARG A CD  1 
ATOM   4820  N  NE  . ARG A  1 623 ? 24.135  35.418 61.642  1.00 26.55 ? 623  ARG A NE  1 
ATOM   4821  C  CZ  . ARG A  1 623 ? 24.793  35.603 62.783  1.00 26.34 ? 623  ARG A CZ  1 
ATOM   4822  N  NH1 . ARG A  1 623 ? 25.389  34.587 63.398  1.00 25.21 ? 623  ARG A NH1 1 
ATOM   4823  N  NH2 . ARG A  1 623 ? 24.830  36.816 63.321  1.00 26.34 ? 623  ARG A NH2 1 
ATOM   4824  N  N   . ILE A  1 624 ? 26.405  33.942 55.339  1.00 18.31 ? 624  ILE A N   1 
ATOM   4825  C  CA  . ILE A  1 624 ? 27.533  34.355 54.531  1.00 18.36 ? 624  ILE A CA  1 
ATOM   4826  C  C   . ILE A  1 624 ? 26.972  35.294 53.486  1.00 18.34 ? 624  ILE A C   1 
ATOM   4827  O  O   . ILE A  1 624 ? 26.021  34.957 52.775  1.00 18.96 ? 624  ILE A O   1 
ATOM   4828  C  CB  . ILE A  1 624 ? 28.191  33.166 53.846  1.00 18.48 ? 624  ILE A CB  1 
ATOM   4829  C  CG1 . ILE A  1 624 ? 28.799  32.247 54.921  1.00 18.46 ? 624  ILE A CG1 1 
ATOM   4830  C  CG2 . ILE A  1 624 ? 29.258  33.665 52.836  1.00 19.05 ? 624  ILE A CG2 1 
ATOM   4831  C  CD1 . ILE A  1 624 ? 29.429  31.011 54.352  1.00 19.50 ? 624  ILE A CD1 1 
ATOM   4832  N  N   . ALA A  1 625 ? 27.553  36.477 53.395  1.00 17.41 ? 625  ALA A N   1 
ATOM   4833  C  CA  . ALA A  1 625 ? 27.083  37.447 52.435  1.00 16.45 ? 625  ALA A CA  1 
ATOM   4834  C  C   . ALA A  1 625 ? 28.220  37.834 51.504  1.00 16.30 ? 625  ALA A C   1 
ATOM   4835  O  O   . ALA A  1 625 ? 29.348  37.362 51.648  1.00 16.62 ? 625  ALA A O   1 
ATOM   4836  C  CB  . ALA A  1 625 ? 26.535  38.669 53.166  1.00 15.65 ? 625  ALA A CB  1 
ATOM   4837  N  N   . ILE A  1 626 ? 27.922  38.688 50.535  1.00 15.55 ? 626  ILE A N   1 
ATOM   4838  C  CA  . ILE A  1 626 ? 28.941  39.116 49.595  1.00 15.33 ? 626  ILE A CA  1 
ATOM   4839  C  C   . ILE A  1 626 ? 28.613  40.503 49.073  1.00 15.51 ? 626  ILE A C   1 
ATOM   4840  O  O   . ILE A  1 626 ? 27.451  40.819 48.879  1.00 16.41 ? 626  ILE A O   1 
ATOM   4841  C  CB  . ILE A  1 626 ? 29.050  38.127 48.407  1.00 15.12 ? 626  ILE A CB  1 
ATOM   4842  C  CG1 . ILE A  1 626 ? 30.081  38.624 47.401  1.00 13.83 ? 626  ILE A CG1 1 
ATOM   4843  C  CG2 . ILE A  1 626 ? 27.693  37.969 47.720  1.00 15.10 ? 626  ILE A CG2 1 
ATOM   4844  C  CD1 . ILE A  1 626 ? 30.446  37.581 46.372  1.00 16.77 ? 626  ILE A CD1 1 
ATOM   4845  N  N   . TRP A  1 627 ? 29.629  41.343 48.869  1.00 15.34 ? 627  TRP A N   1 
ATOM   4846  C  CA  . TRP A  1 627 ? 29.375  42.675 48.328  1.00 14.66 ? 627  TRP A CA  1 
ATOM   4847  C  C   . TRP A  1 627 ? 30.571  43.207 47.524  1.00 15.67 ? 627  TRP A C   1 
ATOM   4848  O  O   . TRP A  1 627 ? 31.721  42.798 47.722  1.00 15.83 ? 627  TRP A O   1 
ATOM   4849  C  CB  . TRP A  1 627 ? 29.003  43.659 49.447  1.00 14.28 ? 627  TRP A CB  1 
ATOM   4850  C  CG  . TRP A  1 627 ? 30.123  44.477 49.994  1.00 14.16 ? 627  TRP A CG  1 
ATOM   4851  C  CD1 . TRP A  1 627 ? 31.065  44.085 50.917  1.00 15.38 ? 627  TRP A CD1 1 
ATOM   4852  C  CD2 . TRP A  1 627 ? 30.413  45.847 49.688  1.00 14.28 ? 627  TRP A CD2 1 
ATOM   4853  N  NE1 . TRP A  1 627 ? 31.917  45.134 51.196  1.00 12.82 ? 627  TRP A NE1 1 
ATOM   4854  C  CE2 . TRP A  1 627 ? 31.539  46.223 50.461  1.00 14.74 ? 627  TRP A CE2 1 
ATOM   4855  C  CE3 . TRP A  1 627 ? 29.830  46.794 48.839  1.00 13.95 ? 627  TRP A CE3 1 
ATOM   4856  C  CZ2 . TRP A  1 627 ? 32.093  47.514 50.415  1.00 16.23 ? 627  TRP A CZ2 1 
ATOM   4857  C  CZ3 . TRP A  1 627 ? 30.374  48.076 48.786  1.00 16.55 ? 627  TRP A CZ3 1 
ATOM   4858  C  CH2 . TRP A  1 627 ? 31.501  48.427 49.577  1.00 15.32 ? 627  TRP A CH2 1 
ATOM   4859  N  N   . GLY A  1 628 ? 30.277  44.123 46.613  1.00 15.39 ? 628  GLY A N   1 
ATOM   4860  C  CA  . GLY A  1 628 ? 31.316  44.692 45.788  1.00 15.64 ? 628  GLY A CA  1 
ATOM   4861  C  C   . GLY A  1 628 ? 30.825  45.932 45.084  1.00 16.13 ? 628  GLY A C   1 
ATOM   4862  O  O   . GLY A  1 628 ? 29.616  46.161 44.938  1.00 14.68 ? 628  GLY A O   1 
ATOM   4863  N  N   . TRP A  1 629 ? 31.785  46.708 44.606  1.00 15.58 ? 629  TRP A N   1 
ATOM   4864  C  CA  . TRP A  1 629 ? 31.502  47.962 43.949  1.00 15.08 ? 629  TRP A CA  1 
ATOM   4865  C  C   . TRP A  1 629 ? 32.188  47.902 42.597  1.00 14.88 ? 629  TRP A C   1 
ATOM   4866  O  O   . TRP A  1 629 ? 33.307  47.386 42.495  1.00 12.57 ? 629  TRP A O   1 
ATOM   4867  C  CB  . TRP A  1 629 ? 32.110  49.088 44.796  1.00 16.60 ? 629  TRP A CB  1 
ATOM   4868  C  CG  . TRP A  1 629 ? 31.621  50.488 44.511  1.00 17.98 ? 629  TRP A CG  1 
ATOM   4869  C  CD1 . TRP A  1 629 ? 31.561  51.109 43.300  1.00 18.11 ? 629  TRP A CD1 1 
ATOM   4870  C  CD2 . TRP A  1 629 ? 31.190  51.455 45.483  1.00 17.79 ? 629  TRP A CD2 1 
ATOM   4871  N  NE1 . TRP A  1 629 ? 31.123  52.403 43.452  1.00 18.81 ? 629  TRP A NE1 1 
ATOM   4872  C  CE2 . TRP A  1 629 ? 30.887  52.644 44.781  1.00 18.69 ? 629  TRP A CE2 1 
ATOM   4873  C  CE3 . TRP A  1 629 ? 31.032  51.431 46.879  1.00 18.34 ? 629  TRP A CE3 1 
ATOM   4874  C  CZ2 . TRP A  1 629 ? 30.432  53.810 45.425  1.00 16.87 ? 629  TRP A CZ2 1 
ATOM   4875  C  CZ3 . TRP A  1 629 ? 30.578  52.597 47.527  1.00 17.93 ? 629  TRP A CZ3 1 
ATOM   4876  C  CH2 . TRP A  1 629 ? 30.284  53.768 46.790  1.00 17.52 ? 629  TRP A CH2 1 
ATOM   4877  N  N   . SER A  1 630 ? 31.525  48.418 41.565  1.00 14.56 ? 630  SER A N   1 
ATOM   4878  C  CA  . SER A  1 630 ? 32.127  48.454 40.231  1.00 15.11 ? 630  SER A CA  1 
ATOM   4879  C  C   . SER A  1 630 ? 32.389  47.015 39.707  1.00 14.45 ? 630  SER A C   1 
ATOM   4880  O  O   . SER A  1 630 ? 31.459  46.212 39.606  1.00 14.49 ? 630  SER A O   1 
ATOM   4881  C  CB  . SER A  1 630 ? 33.431  49.274 40.322  1.00 14.77 ? 630  SER A CB  1 
ATOM   4882  O  OG  . SER A  1 630 ? 33.895  49.666 39.055  1.00 18.32 ? 630  SER A OG  1 
ATOM   4883  N  N   . TYR A  1 631 ? 33.628  46.674 39.355  1.00 13.73 ? 631  TYR A N   1 
ATOM   4884  C  CA  . TYR A  1 631 ? 33.870  45.298 38.909  1.00 13.32 ? 631  TYR A CA  1 
ATOM   4885  C  C   . TYR A  1 631 ? 33.395  44.385 40.041  1.00 13.70 ? 631  TYR A C   1 
ATOM   4886  O  O   . TYR A  1 631 ? 32.862  43.296 39.805  1.00 14.39 ? 631  TYR A O   1 
ATOM   4887  C  CB  . TYR A  1 631 ? 35.353  45.049 38.621  1.00 13.19 ? 631  TYR A CB  1 
ATOM   4888  C  CG  . TYR A  1 631 ? 35.590  43.822 37.762  1.00 14.49 ? 631  TYR A CG  1 
ATOM   4889  C  CD1 . TYR A  1 631 ? 35.411  42.526 38.271  1.00 14.28 ? 631  TYR A CD1 1 
ATOM   4890  C  CD2 . TYR A  1 631 ? 35.944  43.958 36.414  1.00 14.62 ? 631  TYR A CD2 1 
ATOM   4891  C  CE1 . TYR A  1 631 ? 35.574  41.392 37.451  1.00 14.49 ? 631  TYR A CE1 1 
ATOM   4892  C  CE2 . TYR A  1 631 ? 36.110  42.845 35.592  1.00 15.41 ? 631  TYR A CE2 1 
ATOM   4893  C  CZ  . TYR A  1 631 ? 35.922  41.562 36.117  1.00 15.91 ? 631  TYR A CZ  1 
ATOM   4894  O  OH  . TYR A  1 631 ? 36.108  40.477 35.298  1.00 15.76 ? 631  TYR A OH  1 
ATOM   4895  N  N   . GLY A  1 632 ? 33.560  44.850 41.275  1.00 14.10 ? 632  GLY A N   1 
ATOM   4896  C  CA  . GLY A  1 632 ? 33.116  44.075 42.427  1.00 15.61 ? 632  GLY A CA  1 
ATOM   4897  C  C   . GLY A  1 632 ? 31.601  43.868 42.437  1.00 15.39 ? 632  GLY A C   1 
ATOM   4898  O  O   . GLY A  1 632 ? 31.101  42.858 42.951  1.00 15.18 ? 632  GLY A O   1 
ATOM   4899  N  N   . GLY A  1 633 ? 30.867  44.831 41.884  1.00 14.27 ? 633  GLY A N   1 
ATOM   4900  C  CA  . GLY A  1 633 ? 29.419  44.712 41.825  1.00 13.80 ? 633  GLY A CA  1 
ATOM   4901  C  C   . GLY A  1 633 ? 29.032  43.648 40.806  1.00 13.54 ? 633  GLY A C   1 
ATOM   4902  O  O   . GLY A  1 633 ? 28.100  42.880 41.023  1.00 13.78 ? 633  GLY A O   1 
ATOM   4903  N  N   . TYR A  1 634 ? 29.740  43.615 39.681  1.00 13.82 ? 634  TYR A N   1 
ATOM   4904  C  CA  . TYR A  1 634 ? 29.511  42.618 38.626  1.00 13.99 ? 634  TYR A CA  1 
ATOM   4905  C  C   . TYR A  1 634 ? 29.744  41.208 39.192  1.00 14.18 ? 634  TYR A C   1 
ATOM   4906  O  O   . TYR A  1 634 ? 28.889  40.322 39.087  1.00 15.41 ? 634  TYR A O   1 
ATOM   4907  C  CB  . TYR A  1 634 ? 30.480  42.869 37.456  1.00 11.86 ? 634  TYR A CB  1 
ATOM   4908  C  CG  . TYR A  1 634 ? 30.551  41.756 36.405  1.00 12.22 ? 634  TYR A CG  1 
ATOM   4909  C  CD1 . TYR A  1 634 ? 29.449  41.436 35.623  1.00 11.54 ? 634  TYR A CD1 1 
ATOM   4910  C  CD2 . TYR A  1 634 ? 31.750  41.070 36.162  1.00 12.46 ? 634  TYR A CD2 1 
ATOM   4911  C  CE1 . TYR A  1 634 ? 29.544  40.459 34.608  1.00 13.16 ? 634  TYR A CE1 1 
ATOM   4912  C  CE2 . TYR A  1 634 ? 31.858  40.102 35.162  1.00 11.66 ? 634  TYR A CE2 1 
ATOM   4913  C  CZ  . TYR A  1 634 ? 30.742  39.804 34.378  1.00 12.89 ? 634  TYR A CZ  1 
ATOM   4914  O  OH  . TYR A  1 634 ? 30.847  38.914 33.326  1.00 11.69 ? 634  TYR A OH  1 
ATOM   4915  N  N   . VAL A  1 635 ? 30.900  40.999 39.815  1.00 13.77 ? 635  VAL A N   1 
ATOM   4916  C  CA  . VAL A  1 635 ? 31.209  39.690 40.367  1.00 13.61 ? 635  VAL A CA  1 
ATOM   4917  C  C   . VAL A  1 635 ? 30.199  39.269 41.444  1.00 13.55 ? 635  VAL A C   1 
ATOM   4918  O  O   . VAL A  1 635 ? 29.793  38.110 41.487  1.00 13.05 ? 635  VAL A O   1 
ATOM   4919  C  CB  . VAL A  1 635 ? 32.655  39.644 40.941  1.00 13.11 ? 635  VAL A CB  1 
ATOM   4920  C  CG1 . VAL A  1 635 ? 32.921  38.265 41.592  1.00 10.68 ? 635  VAL A CG1 1 
ATOM   4921  C  CG2 . VAL A  1 635 ? 33.656  39.872 39.820  1.00 11.87 ? 635  VAL A CG2 1 
ATOM   4922  N  N   . THR A  1 636 ? 29.791  40.209 42.300  1.00 13.67 ? 636  THR A N   1 
ATOM   4923  C  CA  . THR A  1 636 ? 28.816  39.912 43.352  1.00 13.84 ? 636  THR A CA  1 
ATOM   4924  C  C   . THR A  1 636 ? 27.483  39.468 42.724  1.00 15.51 ? 636  THR A C   1 
ATOM   4925  O  O   . THR A  1 636 ? 26.820  38.546 43.220  1.00 15.00 ? 636  THR A O   1 
ATOM   4926  C  CB  . THR A  1 636 ? 28.515  41.150 44.231  1.00 15.09 ? 636  THR A CB  1 
ATOM   4927  O  OG1 . THR A  1 636 ? 29.670  41.489 45.019  1.00 15.33 ? 636  THR A OG1 1 
ATOM   4928  C  CG2 . THR A  1 636 ? 27.305  40.858 45.150  1.00 13.47 ? 636  THR A CG2 1 
ATOM   4929  N  N   . SER A  1 637 ? 27.087  40.156 41.652  1.00 15.01 ? 637  SER A N   1 
ATOM   4930  C  CA  . SER A  1 637 ? 25.846  39.841 40.958  1.00 16.04 ? 637  SER A CA  1 
ATOM   4931  C  C   . SER A  1 637 ? 25.991  38.496 40.262  1.00 15.84 ? 637  SER A C   1 
ATOM   4932  O  O   . SER A  1 637 ? 25.087  37.674 40.315  1.00 18.19 ? 637  SER A O   1 
ATOM   4933  C  CB  . SER A  1 637 ? 25.495  40.947 39.946  1.00 15.38 ? 637  SER A CB  1 
ATOM   4934  O  OG  . SER A  1 637 ? 25.280  42.196 40.606  1.00 14.70 ? 637  SER A OG  1 
ATOM   4935  N  N   . MET A  1 638 ? 27.119  38.261 39.618  1.00 15.56 ? 638  MET A N   1 
ATOM   4936  C  CA  . MET A  1 638 ? 27.324  36.986 38.950  1.00 15.77 ? 638  MET A CA  1 
ATOM   4937  C  C   . MET A  1 638 ? 27.297  35.856 39.988  1.00 17.51 ? 638  MET A C   1 
ATOM   4938  O  O   . MET A  1 638 ? 26.710  34.785 39.755  1.00 17.39 ? 638  MET A O   1 
ATOM   4939  C  CB  . MET A  1 638 ? 28.648  36.999 38.193  1.00 15.44 ? 638  MET A CB  1 
ATOM   4940  C  CG  . MET A  1 638 ? 28.675  37.947 36.984  1.00 16.27 ? 638  MET A CG  1 
ATOM   4941  S  SD  . MET A  1 638 ? 27.556  37.452 35.637  1.00 16.65 ? 638  MET A SD  1 
ATOM   4942  C  CE  . MET A  1 638 ? 28.535  36.189 34.806  1.00 11.36 ? 638  MET A CE  1 
ATOM   4943  N  N   . VAL A  1 639 ? 27.901  36.105 41.147  1.00 16.72 ? 639  VAL A N   1 
ATOM   4944  C  CA  . VAL A  1 639 ? 27.909  35.102 42.197  1.00 16.37 ? 639  VAL A CA  1 
ATOM   4945  C  C   . VAL A  1 639 ? 26.502  34.842 42.703  1.00 17.30 ? 639  VAL A C   1 
ATOM   4946  O  O   . VAL A  1 639 ? 26.076  33.694 42.781  1.00 17.60 ? 639  VAL A O   1 
ATOM   4947  C  CB  . VAL A  1 639 ? 28.759  35.524 43.407  1.00 15.39 ? 639  VAL A CB  1 
ATOM   4948  C  CG1 . VAL A  1 639 ? 28.509  34.560 44.568  1.00 13.11 ? 639  VAL A CG1 1 
ATOM   4949  C  CG2 . VAL A  1 639 ? 30.225  35.521 43.040  1.00 13.84 ? 639  VAL A CG2 1 
ATOM   4950  N  N   . LEU A  1 640 ? 25.783  35.903 43.058  1.00 16.54 ? 640  LEU A N   1 
ATOM   4951  C  CA  . LEU A  1 640 ? 24.434  35.729 43.566  1.00 16.92 ? 640  LEU A CA  1 
ATOM   4952  C  C   . LEU A  1 640 ? 23.505  35.069 42.550  1.00 17.81 ? 640  LEU A C   1 
ATOM   4953  O  O   . LEU A  1 640 ? 22.484  34.480 42.928  1.00 18.50 ? 640  LEU A O   1 
ATOM   4954  C  CB  . LEU A  1 640 ? 23.845  37.064 44.002  1.00 15.54 ? 640  LEU A CB  1 
ATOM   4955  C  CG  . LEU A  1 640 ? 24.483  37.658 45.257  1.00 16.01 ? 640  LEU A CG  1 
ATOM   4956  C  CD1 . LEU A  1 640 ? 23.946  39.087 45.454  1.00 15.18 ? 640  LEU A CD1 1 
ATOM   4957  C  CD2 . LEU A  1 640 ? 24.163  36.789 46.458  1.00 15.35 ? 640  LEU A CD2 1 
ATOM   4958  N  N   . GLY A  1 641 ? 23.851  35.168 41.269  1.00 17.20 ? 641  GLY A N   1 
ATOM   4959  C  CA  . GLY A  1 641 ? 23.029  34.559 40.231  1.00 17.55 ? 641  GLY A CA  1 
ATOM   4960  C  C   . GLY A  1 641 ? 23.549  33.208 39.754  1.00 18.44 ? 641  GLY A C   1 
ATOM   4961  O  O   . GLY A  1 641 ? 23.043  32.653 38.777  1.00 16.83 ? 641  GLY A O   1 
ATOM   4962  N  N   . SER A  1 642 ? 24.551  32.676 40.454  1.00 18.26 ? 642  SER A N   1 
ATOM   4963  C  CA  . SER A  1 642 ? 25.159  31.410 40.085  1.00 19.59 ? 642  SER A CA  1 
ATOM   4964  C  C   . SER A  1 642 ? 24.381  30.192 40.556  1.00 19.52 ? 642  SER A C   1 
ATOM   4965  O  O   . SER A  1 642 ? 24.603  29.098 40.055  1.00 20.38 ? 642  SER A O   1 
ATOM   4966  C  CB  . SER A  1 642 ? 26.582  31.312 40.659  1.00 20.71 ? 642  SER A CB  1 
ATOM   4967  O  OG  . SER A  1 642 ? 26.527  31.036 42.053  1.00 21.76 ? 642  SER A OG  1 
ATOM   4968  N  N   . GLY A  1 643 ? 23.484  30.374 41.519  1.00 19.94 ? 643  GLY A N   1 
ATOM   4969  C  CA  . GLY A  1 643 ? 22.740  29.247 42.047  1.00 19.79 ? 643  GLY A CA  1 
ATOM   4970  C  C   . GLY A  1 643 ? 23.594  28.361 42.949  1.00 19.87 ? 643  GLY A C   1 
ATOM   4971  O  O   . GLY A  1 643 ? 23.251  27.202 43.176  1.00 19.62 ? 643  GLY A O   1 
ATOM   4972  N  N   . SER A  1 644 ? 24.690  28.899 43.491  1.00 18.51 ? 644  SER A N   1 
ATOM   4973  C  CA  . SER A  1 644 ? 25.571  28.111 44.357  1.00 18.03 ? 644  SER A CA  1 
ATOM   4974  C  C   . SER A  1 644 ? 24.963  27.800 45.727  1.00 18.25 ? 644  SER A C   1 
ATOM   4975  O  O   . SER A  1 644 ? 25.381  26.854 46.386  1.00 18.49 ? 644  SER A O   1 
ATOM   4976  C  CB  . SER A  1 644 ? 26.906  28.829 44.575  1.00 17.98 ? 644  SER A CB  1 
ATOM   4977  O  OG  . SER A  1 644 ? 26.797  29.767 45.640  1.00 18.12 ? 644  SER A OG  1 
ATOM   4978  N  N   . GLY A  1 645 ? 23.999  28.604 46.159  1.00 17.50 ? 645  GLY A N   1 
ATOM   4979  C  CA  . GLY A  1 645 ? 23.373  28.375 47.453  1.00 17.56 ? 645  GLY A CA  1 
ATOM   4980  C  C   . GLY A  1 645 ? 24.234  28.763 48.650  1.00 18.00 ? 645  GLY A C   1 
ATOM   4981  O  O   . GLY A  1 645 ? 23.771  28.748 49.789  1.00 19.23 ? 645  GLY A O   1 
ATOM   4982  N  N   . VAL A  1 646 ? 25.480  29.148 48.409  1.00 18.43 ? 646  VAL A N   1 
ATOM   4983  C  CA  . VAL A  1 646 ? 26.398  29.510 49.497  1.00 17.27 ? 646  VAL A CA  1 
ATOM   4984  C  C   . VAL A  1 646 ? 26.108  30.855 50.163  1.00 17.76 ? 646  VAL A C   1 
ATOM   4985  O  O   . VAL A  1 646 ? 26.387  31.048 51.348  1.00 16.92 ? 646  VAL A O   1 
ATOM   4986  C  CB  . VAL A  1 646 ? 27.848  29.559 48.985  1.00 17.99 ? 646  VAL A CB  1 
ATOM   4987  C  CG1 . VAL A  1 646 ? 28.822  29.891 50.147  1.00 17.71 ? 646  VAL A CG1 1 
ATOM   4988  C  CG2 . VAL A  1 646 ? 28.203  28.238 48.327  1.00 16.72 ? 646  VAL A CG2 1 
ATOM   4989  N  N   . PHE A  1 647 ? 25.535  31.786 49.408  1.00 17.30 ? 647  PHE A N   1 
ATOM   4990  C  CA  . PHE A  1 647 ? 25.297  33.112 49.953  1.00 17.44 ? 647  PHE A CA  1 
ATOM   4991  C  C   . PHE A  1 647 ? 23.856  33.433 50.233  1.00 16.96 ? 647  PHE A C   1 
ATOM   4992  O  O   . PHE A  1 647 ? 22.991  33.222 49.383  1.00 18.07 ? 647  PHE A O   1 
ATOM   4993  C  CB  . PHE A  1 647 ? 25.864  34.174 48.995  1.00 16.32 ? 647  PHE A CB  1 
ATOM   4994  C  CG  . PHE A  1 647 ? 27.329  33.973 48.658  1.00 15.29 ? 647  PHE A CG  1 
ATOM   4995  C  CD1 . PHE A  1 647 ? 28.328  34.616 49.387  1.00 15.25 ? 647  PHE A CD1 1 
ATOM   4996  C  CD2 . PHE A  1 647 ? 27.703  33.101 47.645  1.00 13.87 ? 647  PHE A CD2 1 
ATOM   4997  C  CE1 . PHE A  1 647 ? 29.687  34.383 49.109  1.00 13.37 ? 647  PHE A CE1 1 
ATOM   4998  C  CE2 . PHE A  1 647 ? 29.043  32.861 47.362  1.00 14.86 ? 647  PHE A CE2 1 
ATOM   4999  C  CZ  . PHE A  1 647 ? 30.034  33.505 48.098  1.00 14.15 ? 647  PHE A CZ  1 
ATOM   5000  N  N   . LYS A  1 648 ? 23.605  33.964 51.421  1.00 16.85 ? 648  LYS A N   1 
ATOM   5001  C  CA  . LYS A  1 648 ? 22.251  34.352 51.808  1.00 17.82 ? 648  LYS A CA  1 
ATOM   5002  C  C   . LYS A  1 648 ? 21.811  35.695 51.205  1.00 17.85 ? 648  LYS A C   1 
ATOM   5003  O  O   . LYS A  1 648 ? 20.630  35.903 50.907  1.00 16.42 ? 648  LYS A O   1 
ATOM   5004  C  CB  . LYS A  1 648 ? 22.155  34.462 53.333  1.00 17.13 ? 648  LYS A CB  1 
ATOM   5005  C  CG  . LYS A  1 648 ? 20.773  34.892 53.815  1.00 19.22 ? 648  LYS A CG  1 
ATOM   5006  C  CD  . LYS A  1 648 ? 20.624  34.778 55.324  1.00 20.79 ? 648  LYS A CD  1 
ATOM   5007  C  CE  . LYS A  1 648 ? 19.305  35.405 55.769  1.00 23.28 ? 648  LYS A CE  1 
ATOM   5008  N  NZ  . LYS A  1 648 ? 19.126  35.236 57.225  1.00 25.04 ? 648  LYS A NZ  1 
ATOM   5009  N  N   . CYS A  1 649 ? 22.768  36.608 51.040  1.00 18.11 ? 649  CYS A N   1 
ATOM   5010  C  CA  . CYS A  1 649 ? 22.453  37.935 50.546  1.00 18.74 ? 649  CYS A CA  1 
ATOM   5011  C  C   . CYS A  1 649 ? 23.661  38.640 49.921  1.00 18.69 ? 649  CYS A C   1 
ATOM   5012  O  O   . CYS A  1 649 ? 24.812  38.211 50.091  1.00 18.05 ? 649  CYS A O   1 
ATOM   5013  C  CB  . CYS A  1 649 ? 21.898  38.776 51.709  1.00 20.96 ? 649  CYS A CB  1 
ATOM   5014  S  SG  . CYS A  1 649 ? 23.063  38.926 53.120  1.00 26.69 ? 649  CYS A SG  1 
ATOM   5015  N  N   . GLY A  1 650 ? 23.408  39.722 49.190  1.00 17.55 ? 650  GLY A N   1 
ATOM   5016  C  CA  . GLY A  1 650 ? 24.515  40.432 48.582  1.00 16.69 ? 650  GLY A CA  1 
ATOM   5017  C  C   . GLY A  1 650 ? 24.173  41.848 48.187  1.00 16.17 ? 650  GLY A C   1 
ATOM   5018  O  O   . GLY A  1 650 ? 22.998  42.199 48.015  1.00 16.24 ? 650  GLY A O   1 
ATOM   5019  N  N   . ILE A  1 651 ? 25.208  42.665 48.027  1.00 15.60 ? 651  ILE A N   1 
ATOM   5020  C  CA  . ILE A  1 651 ? 25.015  44.047 47.641  1.00 14.73 ? 651  ILE A CA  1 
ATOM   5021  C  C   . ILE A  1 651 ? 25.943  44.365 46.474  1.00 15.48 ? 651  ILE A C   1 
ATOM   5022  O  O   . ILE A  1 651 ? 27.146  44.088 46.538  1.00 16.05 ? 651  ILE A O   1 
ATOM   5023  C  CB  . ILE A  1 651 ? 25.367  45.029 48.783  1.00 14.95 ? 651  ILE A CB  1 
ATOM   5024  C  CG1 . ILE A  1 651 ? 24.644  44.645 50.084  1.00 14.03 ? 651  ILE A CG1 1 
ATOM   5025  C  CG2 . ILE A  1 651 ? 25.016  46.459 48.348  1.00 15.18 ? 651  ILE A CG2 1 
ATOM   5026  C  CD1 . ILE A  1 651 ? 24.929  45.623 51.252  1.00 11.20 ? 651  ILE A CD1 1 
ATOM   5027  N  N   . ALA A  1 652 ? 25.383  44.956 45.421  1.00 14.61 ? 652  ALA A N   1 
ATOM   5028  C  CA  . ALA A  1 652 ? 26.160  45.345 44.247  1.00 15.45 ? 652  ALA A CA  1 
ATOM   5029  C  C   . ALA A  1 652 ? 25.992  46.842 44.034  1.00 15.49 ? 652  ALA A C   1 
ATOM   5030  O  O   . ALA A  1 652 ? 24.865  47.328 43.848  1.00 16.21 ? 652  ALA A O   1 
ATOM   5031  C  CB  . ALA A  1 652 ? 25.679  44.574 42.995  1.00 13.87 ? 652  ALA A CB  1 
ATOM   5032  N  N   . VAL A  1 653 ? 27.105  47.564 44.090  1.00 14.08 ? 653  VAL A N   1 
ATOM   5033  C  CA  . VAL A  1 653 ? 27.114  49.009 43.894  1.00 14.73 ? 653  VAL A CA  1 
ATOM   5034  C  C   . VAL A  1 653 ? 27.736  49.313 42.524  1.00 14.72 ? 653  VAL A C   1 
ATOM   5035  O  O   . VAL A  1 653 ? 28.849  48.850 42.229  1.00 13.99 ? 653  VAL A O   1 
ATOM   5036  C  CB  . VAL A  1 653 ? 27.949  49.712 44.996  1.00 14.98 ? 653  VAL A CB  1 
ATOM   5037  C  CG1 . VAL A  1 653 ? 27.842  51.218 44.848  1.00 14.28 ? 653  VAL A CG1 1 
ATOM   5038  C  CG2 . VAL A  1 653 ? 27.440  49.284 46.385  1.00 15.46 ? 653  VAL A CG2 1 
ATOM   5039  N  N   . ALA A  1 654 ? 26.998  50.061 41.701  1.00 13.06 ? 654  ALA A N   1 
ATOM   5040  C  CA  . ALA A  1 654 ? 27.415  50.459 40.348  1.00 12.30 ? 654  ALA A CA  1 
ATOM   5041  C  C   . ALA A  1 654 ? 28.078  49.297 39.599  1.00 11.52 ? 654  ALA A C   1 
ATOM   5042  O  O   . ALA A  1 654 ? 29.218  49.385 39.117  1.00 11.11 ? 654  ALA A O   1 
ATOM   5043  C  CB  . ALA A  1 654 ? 28.367  51.667 40.436  1.00 11.29 ? 654  ALA A CB  1 
ATOM   5044  N  N   . PRO A  1 655 ? 27.352  48.184 39.458  1.00 12.48 ? 655  PRO A N   1 
ATOM   5045  C  CA  . PRO A  1 655 ? 27.990  47.071 38.756  1.00 10.96 ? 655  PRO A CA  1 
ATOM   5046  C  C   . PRO A  1 655 ? 27.952  47.147 37.254  1.00 12.43 ? 655  PRO A C   1 
ATOM   5047  O  O   . PRO A  1 655 ? 27.083  47.795 36.674  1.00 10.84 ? 655  PRO A O   1 
ATOM   5048  C  CB  . PRO A  1 655 ? 27.175  45.872 39.221  1.00 11.99 ? 655  PRO A CB  1 
ATOM   5049  C  CG  . PRO A  1 655 ? 25.753  46.449 39.214  1.00 10.83 ? 655  PRO A CG  1 
ATOM   5050  C  CD  . PRO A  1 655 ? 25.996  47.819 39.920  1.00 11.12 ? 655  PRO A CD  1 
ATOM   5051  N  N   . VAL A  1 656 ? 28.900  46.455 36.636  1.00 12.51 ? 656  VAL A N   1 
ATOM   5052  C  CA  . VAL A  1 656 ? 28.898  46.297 35.207  1.00 13.17 ? 656  VAL A CA  1 
ATOM   5053  C  C   . VAL A  1 656 ? 27.893  45.121 35.111  1.00 14.85 ? 656  VAL A C   1 
ATOM   5054  O  O   . VAL A  1 656 ? 27.858  44.267 36.009  1.00 13.81 ? 656  VAL A O   1 
ATOM   5055  C  CB  . VAL A  1 656 ? 30.269  45.854 34.721  1.00 12.50 ? 656  VAL A CB  1 
ATOM   5056  C  CG1 . VAL A  1 656 ? 30.145  45.153 33.334  1.00 12.64 ? 656  VAL A CG1 1 
ATOM   5057  C  CG2 . VAL A  1 656 ? 31.162  47.084 34.610  1.00 10.64 ? 656  VAL A CG2 1 
ATOM   5058  N  N   . SER A  1 657 ? 27.053  45.089 34.081  1.00 15.45 ? 657  SER A N   1 
ATOM   5059  C  CA  . SER A  1 657 ? 26.087  43.995 33.948  1.00 16.09 ? 657  SER A CA  1 
ATOM   5060  C  C   . SER A  1 657 ? 26.226  43.232 32.638  1.00 16.41 ? 657  SER A C   1 
ATOM   5061  O  O   . SER A  1 657 ? 25.787  42.088 32.548  1.00 17.41 ? 657  SER A O   1 
ATOM   5062  C  CB  . SER A  1 657 ? 24.635  44.494 34.100  1.00 16.06 ? 657  SER A CB  1 
ATOM   5063  O  OG  . SER A  1 657 ? 24.215  45.308 33.015  1.00 14.66 ? 657  SER A OG  1 
ATOM   5064  N  N   . ARG A  1 658 ? 26.785  43.867 31.612  1.00 17.09 ? 658  ARG A N   1 
ATOM   5065  C  CA  . ARG A  1 658 ? 27.022  43.193 30.332  1.00 18.15 ? 658  ARG A CA  1 
ATOM   5066  C  C   . ARG A  1 658 ? 28.149  43.977 29.686  1.00 16.77 ? 658  ARG A C   1 
ATOM   5067  O  O   . ARG A  1 658 ? 28.080  45.201 29.564  1.00 15.90 ? 658  ARG A O   1 
ATOM   5068  C  CB  . ARG A  1 658 ? 25.758  43.134 29.446  1.00 20.96 ? 658  ARG A CB  1 
ATOM   5069  C  CG  . ARG A  1 658 ? 25.539  44.285 28.495  1.00 25.18 ? 658  ARG A CG  1 
ATOM   5070  C  CD  . ARG A  1 658 ? 25.142  43.868 27.076  1.00 27.62 ? 658  ARG A CD  1 
ATOM   5071  N  NE  . ARG A  1 658 ? 24.196  42.767 26.991  1.00 27.79 ? 658  ARG A NE  1 
ATOM   5072  C  CZ  . ARG A  1 658 ? 23.677  42.293 25.850  1.00 29.52 ? 658  ARG A CZ  1 
ATOM   5073  N  NH1 . ARG A  1 658 ? 23.988  42.836 24.673  1.00 28.36 ? 658  ARG A NH1 1 
ATOM   5074  N  NH2 . ARG A  1 658 ? 22.882  41.226 25.883  1.00 26.99 ? 658  ARG A NH2 1 
ATOM   5075  N  N   . TRP A  1 659 ? 29.190  43.265 29.276  1.00 16.44 ? 659  TRP A N   1 
ATOM   5076  C  CA  . TRP A  1 659 ? 30.374  43.923 28.748  1.00 16.86 ? 659  TRP A CA  1 
ATOM   5077  C  C   . TRP A  1 659 ? 30.222  44.845 27.544  1.00 18.07 ? 659  TRP A C   1 
ATOM   5078  O  O   . TRP A  1 659 ? 31.029  45.751 27.368  1.00 18.44 ? 659  TRP A O   1 
ATOM   5079  C  CB  . TRP A  1 659 ? 31.477  42.885 28.552  1.00 14.69 ? 659  TRP A CB  1 
ATOM   5080  C  CG  . TRP A  1 659 ? 31.977  42.431 29.921  1.00 16.01 ? 659  TRP A CG  1 
ATOM   5081  C  CD1 . TRP A  1 659 ? 31.747  41.225 30.532  1.00 15.03 ? 659  TRP A CD1 1 
ATOM   5082  C  CD2 . TRP A  1 659 ? 32.656  43.245 30.892  1.00 14.70 ? 659  TRP A CD2 1 
ATOM   5083  N  NE1 . TRP A  1 659 ? 32.232  41.246 31.823  1.00 16.47 ? 659  TRP A NE1 1 
ATOM   5084  C  CE2 . TRP A  1 659 ? 32.796  42.471 32.069  1.00 15.45 ? 659  TRP A CE2 1 
ATOM   5085  C  CE3 . TRP A  1 659 ? 33.156  44.557 30.882  1.00 13.78 ? 659  TRP A CE3 1 
ATOM   5086  C  CZ2 . TRP A  1 659 ? 33.420  42.963 33.230  1.00 14.39 ? 659  TRP A CZ2 1 
ATOM   5087  C  CZ3 . TRP A  1 659 ? 33.777  45.047 32.037  1.00 14.69 ? 659  TRP A CZ3 1 
ATOM   5088  C  CH2 . TRP A  1 659 ? 33.902  44.246 33.196  1.00 14.13 ? 659  TRP A CH2 1 
ATOM   5089  N  N   . GLU A  1 660 ? 29.178  44.662 26.749  1.00 17.00 ? 660  GLU A N   1 
ATOM   5090  C  CA  . GLU A  1 660 ? 28.976  45.539 25.612  1.00 18.42 ? 660  GLU A CA  1 
ATOM   5091  C  C   . GLU A  1 660 ? 28.581  46.947 26.098  1.00 17.97 ? 660  GLU A C   1 
ATOM   5092  O  O   . GLU A  1 660 ? 28.582  47.906 25.324  1.00 18.56 ? 660  GLU A O   1 
ATOM   5093  C  CB  . GLU A  1 660 ? 27.918  44.943 24.659  1.00 18.63 ? 660  GLU A CB  1 
ATOM   5094  C  CG  . GLU A  1 660 ? 28.503  43.897 23.706  1.00 20.92 ? 660  GLU A CG  1 
ATOM   5095  C  CD  . GLU A  1 660 ? 27.473  42.934 23.125  1.00 23.40 ? 660  GLU A CD  1 
ATOM   5096  O  OE1 . GLU A  1 660 ? 27.043  42.006 23.854  1.00 21.09 ? 660  GLU A OE1 1 
ATOM   5097  O  OE2 . GLU A  1 660 ? 27.090  43.108 21.932  1.00 24.77 ? 660  GLU A OE2 1 
ATOM   5098  N  N   . TYR A  1 661 ? 28.249  47.093 27.375  1.00 17.03 ? 661  TYR A N   1 
ATOM   5099  C  CA  . TYR A  1 661 ? 27.884  48.435 27.859  1.00 15.88 ? 661  TYR A CA  1 
ATOM   5100  C  C   . TYR A  1 661 ? 29.097  49.213 28.335  1.00 15.13 ? 661  TYR A C   1 
ATOM   5101  O  O   . TYR A  1 661 ? 29.018  50.424 28.511  1.00 15.76 ? 661  TYR A O   1 
ATOM   5102  C  CB  . TYR A  1 661 ? 26.893  48.387 29.026  1.00 15.03 ? 661  TYR A CB  1 
ATOM   5103  C  CG  . TYR A  1 661 ? 25.549  47.756 28.725  1.00 15.28 ? 661  TYR A CG  1 
ATOM   5104  C  CD1 . TYR A  1 661 ? 25.010  47.760 27.436  1.00 15.18 ? 661  TYR A CD1 1 
ATOM   5105  C  CD2 . TYR A  1 661 ? 24.800  47.170 29.752  1.00 15.98 ? 661  TYR A CD2 1 
ATOM   5106  C  CE1 . TYR A  1 661 ? 23.754  47.191 27.177  1.00 15.72 ? 661  TYR A CE1 1 
ATOM   5107  C  CE2 . TYR A  1 661 ? 23.555  46.607 29.507  1.00 16.08 ? 661  TYR A CE2 1 
ATOM   5108  C  CZ  . TYR A  1 661 ? 23.037  46.617 28.211  1.00 15.56 ? 661  TYR A CZ  1 
ATOM   5109  O  OH  . TYR A  1 661 ? 21.823  46.014 27.977  1.00 14.09 ? 661  TYR A OH  1 
ATOM   5110  N  N   . TYR A  1 662 ? 30.215  48.525 28.542  1.00 14.37 ? 662  TYR A N   1 
ATOM   5111  C  CA  . TYR A  1 662 ? 31.398  49.206 29.025  1.00 14.76 ? 662  TYR A CA  1 
ATOM   5112  C  C   . TYR A  1 662 ? 32.289  49.691 27.885  1.00 15.25 ? 662  TYR A C   1 
ATOM   5113  O  O   . TYR A  1 662 ? 32.066  49.325 26.720  1.00 16.10 ? 662  TYR A O   1 
ATOM   5114  C  CB  . TYR A  1 662 ? 32.172  48.330 30.020  1.00 13.12 ? 662  TYR A CB  1 
ATOM   5115  C  CG  . TYR A  1 662 ? 33.019  49.189 30.925  1.00 13.17 ? 662  TYR A CG  1 
ATOM   5116  C  CD1 . TYR A  1 662 ? 32.440  50.207 31.715  1.00 13.63 ? 662  TYR A CD1 1 
ATOM   5117  C  CD2 . TYR A  1 662 ? 34.407  49.060 30.930  1.00 13.34 ? 662  TYR A CD2 1 
ATOM   5118  C  CE1 . TYR A  1 662 ? 33.247  51.078 32.489  1.00 12.84 ? 662  TYR A CE1 1 
ATOM   5119  C  CE2 . TYR A  1 662 ? 35.214  49.917 31.686  1.00 12.73 ? 662  TYR A CE2 1 
ATOM   5120  C  CZ  . TYR A  1 662 ? 34.641  50.919 32.462  1.00 12.86 ? 662  TYR A CZ  1 
ATOM   5121  O  OH  . TYR A  1 662 ? 35.482  51.733 33.208  1.00 11.66 ? 662  TYR A OH  1 
ATOM   5122  N  N   . ASP A  1 663 ? 33.316  50.481 28.202  1.00 15.28 ? 663  ASP A N   1 
ATOM   5123  C  CA  . ASP A  1 663 ? 34.133  51.051 27.133  1.00 15.36 ? 663  ASP A CA  1 
ATOM   5124  C  C   . ASP A  1 663 ? 35.070  50.119 26.393  1.00 15.75 ? 663  ASP A C   1 
ATOM   5125  O  O   . ASP A  1 663 ? 35.487  49.082 26.894  1.00 16.64 ? 663  ASP A O   1 
ATOM   5126  C  CB  . ASP A  1 663 ? 34.878  52.317 27.620  1.00 13.97 ? 663  ASP A CB  1 
ATOM   5127  C  CG  . ASP A  1 663 ? 35.989  52.024 28.611  1.00 14.58 ? 663  ASP A CG  1 
ATOM   5128  O  OD1 . ASP A  1 663 ? 36.986  51.372 28.236  1.00 14.54 ? 663  ASP A OD1 1 
ATOM   5129  O  OD2 . ASP A  1 663 ? 35.869  52.463 29.771  1.00 12.63 ? 663  ASP A OD2 1 
ATOM   5130  N  N   . SER A  1 664 ? 35.383  50.515 25.170  1.00 15.83 ? 664  SER A N   1 
ATOM   5131  C  CA  . SER A  1 664 ? 36.248  49.750 24.286  1.00 15.99 ? 664  SER A CA  1 
ATOM   5132  C  C   . SER A  1 664 ? 37.660  49.436 24.791  1.00 15.73 ? 664  SER A C   1 
ATOM   5133  O  O   . SER A  1 664 ? 38.066  48.279 24.794  1.00 17.46 ? 664  SER A O   1 
ATOM   5134  C  CB  . SER A  1 664 ? 36.350  50.483 22.947  1.00 15.62 ? 664  SER A CB  1 
ATOM   5135  O  OG  . SER A  1 664 ? 36.882  51.781 23.133  1.00 15.18 ? 664  SER A OG  1 
ATOM   5136  N  N   . VAL A  1 665 ? 38.408  50.457 25.204  1.00 15.47 ? 665  VAL A N   1 
ATOM   5137  C  CA  . VAL A  1 665 ? 39.796  50.250 25.640  1.00 15.17 ? 665  VAL A CA  1 
ATOM   5138  C  C   . VAL A  1 665 ? 39.933  49.215 26.758  1.00 16.02 ? 665  VAL A C   1 
ATOM   5139  O  O   . VAL A  1 665 ? 40.723  48.269 26.653  1.00 15.47 ? 665  VAL A O   1 
ATOM   5140  C  CB  . VAL A  1 665 ? 40.452  51.586 26.062  1.00 14.48 ? 665  VAL A CB  1 
ATOM   5141  C  CG1 . VAL A  1 665 ? 41.900  51.348 26.504  1.00 15.42 ? 665  VAL A CG1 1 
ATOM   5142  C  CG2 . VAL A  1 665 ? 40.407  52.592 24.871  1.00 15.14 ? 665  VAL A CG2 1 
ATOM   5143  N  N   . TYR A  1 666 ? 39.152  49.365 27.822  1.00 15.77 ? 666  TYR A N   1 
ATOM   5144  C  CA  . TYR A  1 666 ? 39.242  48.404 28.912  1.00 16.84 ? 666  TYR A CA  1 
ATOM   5145  C  C   . TYR A  1 666 ? 38.627  47.052 28.527  1.00 16.98 ? 666  TYR A C   1 
ATOM   5146  O  O   . TYR A  1 666 ? 39.280  46.006 28.632  1.00 17.34 ? 666  TYR A O   1 
ATOM   5147  C  CB  . TYR A  1 666 ? 38.539  48.957 30.161  1.00 15.33 ? 666  TYR A CB  1 
ATOM   5148  C  CG  . TYR A  1 666 ? 38.475  48.003 31.349  1.00 14.83 ? 666  TYR A CG  1 
ATOM   5149  C  CD1 . TYR A  1 666 ? 37.500  46.997 31.428  1.00 14.37 ? 666  TYR A CD1 1 
ATOM   5150  C  CD2 . TYR A  1 666 ? 39.374  48.129 32.415  1.00 14.31 ? 666  TYR A CD2 1 
ATOM   5151  C  CE1 . TYR A  1 666 ? 37.422  46.144 32.560  1.00 13.73 ? 666  TYR A CE1 1 
ATOM   5152  C  CE2 . TYR A  1 666 ? 39.310  47.288 33.535  1.00 14.59 ? 666  TYR A CE2 1 
ATOM   5153  C  CZ  . TYR A  1 666 ? 38.339  46.308 33.609  1.00 14.32 ? 666  TYR A CZ  1 
ATOM   5154  O  OH  . TYR A  1 666 ? 38.267  45.523 34.741  1.00 14.31 ? 666  TYR A OH  1 
ATOM   5155  N  N   . THR A  1 667 ? 37.385  47.071 28.054  1.00 15.70 ? 667  THR A N   1 
ATOM   5156  C  CA  . THR A  1 667 ? 36.705  45.824 27.730  1.00 16.21 ? 667  THR A CA  1 
ATOM   5157  C  C   . THR A  1 667 ? 37.390  44.940 26.674  1.00 17.65 ? 667  THR A C   1 
ATOM   5158  O  O   . THR A  1 667 ? 37.616  43.753 26.920  1.00 17.92 ? 667  THR A O   1 
ATOM   5159  C  CB  . THR A  1 667 ? 35.232  46.085 27.312  1.00 15.75 ? 667  THR A CB  1 
ATOM   5160  O  OG1 . THR A  1 667 ? 34.614  46.963 28.260  1.00 14.25 ? 667  THR A OG1 1 
ATOM   5161  C  CG2 . THR A  1 667 ? 34.444  44.773 27.275  1.00 14.20 ? 667  THR A CG2 1 
ATOM   5162  N  N   . GLU A  1 668 ? 37.726  45.509 25.517  1.00 17.40 ? 668  GLU A N   1 
ATOM   5163  C  CA  . GLU A  1 668 ? 38.369  44.743 24.448  1.00 17.69 ? 668  GLU A CA  1 
ATOM   5164  C  C   . GLU A  1 668 ? 39.745  44.219 24.841  1.00 17.91 ? 668  GLU A C   1 
ATOM   5165  O  O   . GLU A  1 668 ? 40.228  43.211 24.297  1.00 18.21 ? 668  GLU A O   1 
ATOM   5166  C  CB  . GLU A  1 668 ? 38.468  45.603 23.181  1.00 16.93 ? 668  GLU A CB  1 
ATOM   5167  C  CG  . GLU A  1 668 ? 37.096  46.026 22.640  1.00 16.47 ? 668  GLU A CG  1 
ATOM   5168  C  CD  . GLU A  1 668 ? 37.163  47.130 21.619  1.00 15.80 ? 668  GLU A CD  1 
ATOM   5169  O  OE1 . GLU A  1 668 ? 38.254  47.376 21.071  1.00 17.20 ? 668  GLU A OE1 1 
ATOM   5170  O  OE2 . GLU A  1 668 ? 36.119  47.762 21.348  1.00 16.55 ? 668  GLU A OE2 1 
ATOM   5171  N  N   . ARG A  1 669 ? 40.373  44.864 25.812  1.00 16.88 ? 669  ARG A N   1 
ATOM   5172  C  CA  . ARG A  1 669 ? 41.699  44.406 26.219  1.00 16.77 ? 669  ARG A CA  1 
ATOM   5173  C  C   . ARG A  1 669 ? 41.589  42.979 26.755  1.00 16.02 ? 669  ARG A C   1 
ATOM   5174  O  O   . ARG A  1 669 ? 42.425  42.119 26.481  1.00 15.52 ? 669  ARG A O   1 
ATOM   5175  C  CB  . ARG A  1 669 ? 42.281  45.326 27.311  1.00 16.78 ? 669  ARG A CB  1 
ATOM   5176  C  CG  . ARG A  1 669 ? 43.624  44.827 27.877  1.00 17.77 ? 669  ARG A CG  1 
ATOM   5177  C  CD  . ARG A  1 669 ? 44.026  45.614 29.116  1.00 18.55 ? 669  ARG A CD  1 
ATOM   5178  N  NE  . ARG A  1 669 ? 44.160  47.018 28.764  1.00 21.33 ? 669  ARG A NE  1 
ATOM   5179  C  CZ  . ARG A  1 669 ? 43.616  48.023 29.439  1.00 20.75 ? 669  ARG A CZ  1 
ATOM   5180  N  NH1 . ARG A  1 669 ? 42.884  47.799 30.526  1.00 16.98 ? 669  ARG A NH1 1 
ATOM   5181  N  NH2 . ARG A  1 669 ? 43.821  49.259 29.017  1.00 21.00 ? 669  ARG A NH2 1 
ATOM   5182  N  N   . TYR A  1 670 ? 40.527  42.741 27.507  1.00 16.60 ? 670  TYR A N   1 
ATOM   5183  C  CA  . TYR A  1 670 ? 40.309  41.456 28.145  1.00 16.92 ? 670  TYR A CA  1 
ATOM   5184  C  C   . TYR A  1 670 ? 39.356  40.541 27.384  1.00 17.52 ? 670  TYR A C   1 
ATOM   5185  O  O   . TYR A  1 670 ? 39.432  39.328 27.530  1.00 18.27 ? 670  TYR A O   1 
ATOM   5186  C  CB  . TYR A  1 670 ? 39.736  41.688 29.548  1.00 15.63 ? 670  TYR A CB  1 
ATOM   5187  C  CG  . TYR A  1 670 ? 40.525  42.704 30.368  1.00 15.53 ? 670  TYR A CG  1 
ATOM   5188  C  CD1 . TYR A  1 670 ? 41.821  42.425 30.788  1.00 15.32 ? 670  TYR A CD1 1 
ATOM   5189  C  CD2 . TYR A  1 670 ? 39.986  43.954 30.685  1.00 15.32 ? 670  TYR A CD2 1 
ATOM   5190  C  CE1 . TYR A  1 670 ? 42.571  43.357 31.502  1.00 16.90 ? 670  TYR A CE1 1 
ATOM   5191  C  CE2 . TYR A  1 670 ? 40.726  44.902 31.405  1.00 16.69 ? 670  TYR A CE2 1 
ATOM   5192  C  CZ  . TYR A  1 670 ? 42.021  44.598 31.811  1.00 15.63 ? 670  TYR A CZ  1 
ATOM   5193  O  OH  . TYR A  1 670 ? 42.764  45.517 32.518  1.00 13.94 ? 670  TYR A OH  1 
ATOM   5194  N  N   . MET A  1 671 ? 38.493  41.132 26.563  1.00 17.24 ? 671  MET A N   1 
ATOM   5195  C  CA  . MET A  1 671 ? 37.457  40.405 25.862  1.00 18.08 ? 671  MET A CA  1 
ATOM   5196  C  C   . MET A  1 671 ? 37.490  40.390 24.334  1.00 20.04 ? 671  MET A C   1 
ATOM   5197  O  O   . MET A  1 671 ? 36.640  39.753 23.707  1.00 19.56 ? 671  MET A O   1 
ATOM   5198  C  CB  . MET A  1 671 ? 36.097  40.976 26.298  1.00 19.40 ? 671  MET A CB  1 
ATOM   5199  C  CG  . MET A  1 671 ? 35.753  40.741 27.765  1.00 19.47 ? 671  MET A CG  1 
ATOM   5200  S  SD  . MET A  1 671 ? 35.150  39.037 28.015  1.00 21.45 ? 671  MET A SD  1 
ATOM   5201  C  CE  . MET A  1 671 ? 33.430  39.223 27.444  1.00 19.06 ? 671  MET A CE  1 
ATOM   5202  N  N   . GLY A  1 672 ? 38.432  41.092 23.723  1.00 20.05 ? 672  GLY A N   1 
ATOM   5203  C  CA  . GLY A  1 672 ? 38.423  41.122 22.276  1.00 21.74 ? 672  GLY A CA  1 
ATOM   5204  C  C   . GLY A  1 672 ? 37.164  41.864 21.824  1.00 22.44 ? 672  GLY A C   1 
ATOM   5205  O  O   . GLY A  1 672 ? 36.569  42.639 22.593  1.00 20.98 ? 672  GLY A O   1 
ATOM   5206  N  N   . LEU A  1 673 ? 36.747  41.618 20.584  1.00 22.43 ? 673  LEU A N   1 
ATOM   5207  C  CA  . LEU A  1 673 ? 35.580  42.285 20.012  1.00 22.95 ? 673  LEU A CA  1 
ATOM   5208  C  C   . LEU A  1 673 ? 34.306  41.455 20.075  1.00 23.73 ? 673  LEU A C   1 
ATOM   5209  O  O   . LEU A  1 673 ? 34.339  40.224 19.965  1.00 24.50 ? 673  LEU A O   1 
ATOM   5210  C  CB  . LEU A  1 673 ? 35.854  42.653 18.557  1.00 23.71 ? 673  LEU A CB  1 
ATOM   5211  C  CG  . LEU A  1 673 ? 36.995  43.629 18.261  1.00 24.77 ? 673  LEU A CG  1 
ATOM   5212  C  CD1 . LEU A  1 673 ? 37.330  43.606 16.775  1.00 25.38 ? 673  LEU A CD1 1 
ATOM   5213  C  CD2 . LEU A  1 673 ? 36.581  45.028 18.694  1.00 25.14 ? 673  LEU A CD2 1 
ATOM   5214  N  N   . PRO A  1 674 ? 33.157  42.129 20.237  1.00 23.28 ? 674  PRO A N   1 
ATOM   5215  C  CA  . PRO A  1 674 ? 31.853  41.470 20.315  1.00 23.35 ? 674  PRO A CA  1 
ATOM   5216  C  C   . PRO A  1 674 ? 31.242  41.215 18.932  1.00 24.59 ? 674  PRO A C   1 
ATOM   5217  O  O   . PRO A  1 674 ? 30.177  41.742 18.605  1.00 23.61 ? 674  PRO A O   1 
ATOM   5218  C  CB  . PRO A  1 674 ? 31.038  42.448 21.149  1.00 23.51 ? 674  PRO A CB  1 
ATOM   5219  C  CG  . PRO A  1 674 ? 31.520  43.770 20.656  1.00 22.81 ? 674  PRO A CG  1 
ATOM   5220  C  CD  . PRO A  1 674 ? 33.042  43.567 20.551  1.00 22.30 ? 674  PRO A CD  1 
ATOM   5221  N  N   . THR A  1 675 ? 31.934  40.411 18.125  1.00 26.10 ? 675  THR A N   1 
ATOM   5222  C  CA  . THR A  1 675 ? 31.479  40.049 16.779  1.00 26.47 ? 675  THR A CA  1 
ATOM   5223  C  C   . THR A  1 675 ? 31.496  38.535 16.713  1.00 28.08 ? 675  THR A C   1 
ATOM   5224  O  O   . THR A  1 675 ? 32.276  37.885 17.417  1.00 27.47 ? 675  THR A O   1 
ATOM   5225  C  CB  . THR A  1 675 ? 32.416  40.590 15.706  1.00 26.00 ? 675  THR A CB  1 
ATOM   5226  O  OG1 . THR A  1 675 ? 33.715  40.009 15.867  1.00 26.79 ? 675  THR A OG1 1 
ATOM   5227  C  CG2 . THR A  1 675 ? 32.532  42.107 15.827  1.00 25.69 ? 675  THR A CG2 1 
ATOM   5228  N  N   . PRO A  1 676 ? 30.640  37.942 15.867  1.00 29.28 ? 676  PRO A N   1 
ATOM   5229  C  CA  . PRO A  1 676 ? 30.635  36.481 15.794  1.00 29.97 ? 676  PRO A CA  1 
ATOM   5230  C  C   . PRO A  1 676 ? 32.000  35.885 15.431  1.00 30.76 ? 676  PRO A C   1 
ATOM   5231  O  O   . PRO A  1 676 ? 32.357  34.808 15.912  1.00 31.94 ? 676  PRO A O   1 
ATOM   5232  C  CB  . PRO A  1 676 ? 29.524  36.182 14.781  1.00 30.16 ? 676  PRO A CB  1 
ATOM   5233  C  CG  . PRO A  1 676 ? 29.477  37.418 13.932  1.00 30.68 ? 676  PRO A CG  1 
ATOM   5234  C  CD  . PRO A  1 676 ? 29.687  38.538 14.919  1.00 29.86 ? 676  PRO A CD  1 
ATOM   5235  N  N   . GLU A  1 677 ? 32.784  36.594 14.628  1.00 31.23 ? 677  GLU A N   1 
ATOM   5236  C  CA  . GLU A  1 677 ? 34.102  36.082 14.255  1.00 31.90 ? 677  GLU A CA  1 
ATOM   5237  C  C   . GLU A  1 677 ? 35.091  36.177 15.409  1.00 30.20 ? 677  GLU A C   1 
ATOM   5238  O  O   . GLU A  1 677 ? 36.103  35.490 15.406  1.00 30.32 ? 677  GLU A O   1 
ATOM   5239  C  CB  . GLU A  1 677 ? 34.703  36.849 13.071  1.00 34.05 ? 677  GLU A CB  1 
ATOM   5240  C  CG  . GLU A  1 677 ? 33.711  37.344 12.043  1.00 38.50 ? 677  GLU A CG  1 
ATOM   5241  C  CD  . GLU A  1 677 ? 32.953  38.562 12.526  1.00 39.65 ? 677  GLU A CD  1 
ATOM   5242  O  OE1 . GLU A  1 677 ? 33.596  39.602 12.803  1.00 41.21 ? 677  GLU A OE1 1 
ATOM   5243  O  OE2 . GLU A  1 677 ? 31.717  38.470 12.626  1.00 41.62 ? 677  GLU A OE2 1 
ATOM   5244  N  N   . ASP A  1 678 ? 34.828  37.046 16.379  1.00 28.48 ? 678  ASP A N   1 
ATOM   5245  C  CA  . ASP A  1 678 ? 35.761  37.165 17.486  1.00 25.90 ? 678  ASP A CA  1 
ATOM   5246  C  C   . ASP A  1 678 ? 35.235  36.575 18.789  1.00 25.00 ? 678  ASP A C   1 
ATOM   5247  O  O   . ASP A  1 678 ? 35.266  35.369 18.962  1.00 24.64 ? 678  ASP A O   1 
ATOM   5248  C  CB  . ASP A  1 678 ? 36.196  38.626 17.696  1.00 26.10 ? 678  ASP A CB  1 
ATOM   5249  C  CG  . ASP A  1 678 ? 37.356  38.758 18.698  1.00 26.65 ? 678  ASP A CG  1 
ATOM   5250  O  OD1 . ASP A  1 678 ? 37.708  37.743 19.324  1.00 26.51 ? 678  ASP A OD1 1 
ATOM   5251  O  OD2 . ASP A  1 678 ? 37.908  39.868 18.867  1.00 26.76 ? 678  ASP A OD2 1 
ATOM   5252  N  N   . ASN A  1 679 ? 34.709  37.393 19.694  1.00 23.54 ? 679  ASN A N   1 
ATOM   5253  C  CA  . ASN A  1 679 ? 34.298  36.841 20.985  1.00 23.17 ? 679  ASN A CA  1 
ATOM   5254  C  C   . ASN A  1 679 ? 32.862  37.129 21.419  1.00 23.15 ? 679  ASN A C   1 
ATOM   5255  O  O   . ASN A  1 679 ? 32.553  37.108 22.615  1.00 21.40 ? 679  ASN A O   1 
ATOM   5256  C  CB  . ASN A  1 679 ? 35.302  37.340 22.046  1.00 21.74 ? 679  ASN A CB  1 
ATOM   5257  C  CG  . ASN A  1 679 ? 35.287  36.516 23.326  1.00 22.94 ? 679  ASN A CG  1 
ATOM   5258  O  OD1 . ASN A  1 679 ? 35.120  35.285 23.299  1.00 21.51 ? 679  ASN A OD1 1 
ATOM   5259  N  ND2 . ASN A  1 679 ? 35.484  37.193 24.460  1.00 20.06 ? 679  ASN A ND2 1 
ATOM   5260  N  N   . LEU A  1 680 ? 31.978  37.374 20.455  1.00 22.97 ? 680  LEU A N   1 
ATOM   5261  C  CA  . LEU A  1 680 ? 30.576  37.673 20.774  1.00 23.41 ? 680  LEU A CA  1 
ATOM   5262  C  C   . LEU A  1 680 ? 29.867  36.658 21.690  1.00 24.20 ? 680  LEU A C   1 
ATOM   5263  O  O   . LEU A  1 680 ? 29.213  37.066 22.658  1.00 24.55 ? 680  LEU A O   1 
ATOM   5264  C  CB  . LEU A  1 680 ? 29.767  37.862 19.485  1.00 23.30 ? 680  LEU A CB  1 
ATOM   5265  C  CG  . LEU A  1 680 ? 28.275  38.187 19.677  1.00 24.34 ? 680  LEU A CG  1 
ATOM   5266  C  CD1 . LEU A  1 680 ? 28.121  39.479 20.469  1.00 23.04 ? 680  LEU A CD1 1 
ATOM   5267  C  CD2 . LEU A  1 680 ? 27.580  38.322 18.323  1.00 23.88 ? 680  LEU A CD2 1 
ATOM   5268  N  N   . ASP A  1 681 ? 29.986  35.357 21.425  1.00 23.71 ? 681  ASP A N   1 
ATOM   5269  C  CA  . ASP A  1 681 ? 29.304  34.394 22.296  1.00 24.51 ? 681  ASP A CA  1 
ATOM   5270  C  C   . ASP A  1 681 ? 29.644  34.582 23.762  1.00 24.40 ? 681  ASP A C   1 
ATOM   5271  O  O   . ASP A  1 681 ? 28.761  34.502 24.619  1.00 23.52 ? 681  ASP A O   1 
ATOM   5272  C  CB  . ASP A  1 681 ? 29.625  32.947 21.939  1.00 25.66 ? 681  ASP A CB  1 
ATOM   5273  C  CG  . ASP A  1 681 ? 29.197  32.586 20.531  1.00 26.51 ? 681  ASP A CG  1 
ATOM   5274  O  OD1 . ASP A  1 681 ? 28.223  33.168 20.029  1.00 27.08 ? 681  ASP A OD1 1 
ATOM   5275  O  OD2 . ASP A  1 681 ? 29.835  31.704 19.940  1.00 29.04 ? 681  ASP A OD2 1 
ATOM   5276  N  N   . HIS A  1 682 ? 30.914  34.810 24.075  1.00 23.93 ? 682  HIS A N   1 
ATOM   5277  C  CA  . HIS A  1 682 ? 31.226  34.988 25.480  1.00 24.11 ? 682  HIS A CA  1 
ATOM   5278  C  C   . HIS A  1 682 ? 30.695  36.313 26.017  1.00 23.47 ? 682  HIS A C   1 
ATOM   5279  O  O   . HIS A  1 682 ? 30.330  36.408 27.190  1.00 22.50 ? 682  HIS A O   1 
ATOM   5280  C  CB  . HIS A  1 682 ? 32.707  34.892 25.778  1.00 25.89 ? 682  HIS A CB  1 
ATOM   5281  C  CG  . HIS A  1 682 ? 32.978  34.953 27.240  1.00 28.47 ? 682  HIS A CG  1 
ATOM   5282  N  ND1 . HIS A  1 682 ? 32.510  33.992 28.112  1.00 29.46 ? 682  HIS A ND1 1 
ATOM   5283  C  CD2 . HIS A  1 682 ? 33.524  35.925 28.008  1.00 28.98 ? 682  HIS A CD2 1 
ATOM   5284  C  CE1 . HIS A  1 682 ? 32.751  34.373 29.354  1.00 30.23 ? 682  HIS A CE1 1 
ATOM   5285  N  NE2 . HIS A  1 682 ? 33.366  35.543 29.318  1.00 28.87 ? 682  HIS A NE2 1 
ATOM   5286  N  N   . TYR A  1 683 ? 30.674  37.343 25.174  1.00 22.03 ? 683  TYR A N   1 
ATOM   5287  C  CA  . TYR A  1 683 ? 30.112  38.622 25.584  1.00 21.75 ? 683  TYR A CA  1 
ATOM   5288  C  C   . TYR A  1 683 ? 28.654  38.373 25.959  1.00 22.03 ? 683  TYR A C   1 
ATOM   5289  O  O   . TYR A  1 683 ? 28.131  38.957 26.908  1.00 22.30 ? 683  TYR A O   1 
ATOM   5290  C  CB  . TYR A  1 683 ? 30.134  39.611 24.430  1.00 19.06 ? 683  TYR A CB  1 
ATOM   5291  C  CG  . TYR A  1 683 ? 31.319  40.540 24.380  1.00 19.17 ? 683  TYR A CG  1 
ATOM   5292  C  CD1 . TYR A  1 683 ? 31.251  41.812 24.955  1.00 18.83 ? 683  TYR A CD1 1 
ATOM   5293  C  CD2 . TYR A  1 683 ? 32.476  40.195 23.675  1.00 17.77 ? 683  TYR A CD2 1 
ATOM   5294  C  CE1 . TYR A  1 683 ? 32.296  42.721 24.817  1.00 18.01 ? 683  TYR A CE1 1 
ATOM   5295  C  CE2 . TYR A  1 683 ? 33.531  41.101 23.530  1.00 18.54 ? 683  TYR A CE2 1 
ATOM   5296  C  CZ  . TYR A  1 683 ? 33.428  42.358 24.102  1.00 18.34 ? 683  TYR A CZ  1 
ATOM   5297  O  OH  . TYR A  1 683 ? 34.451  43.260 23.964  1.00 18.99 ? 683  TYR A OH  1 
ATOM   5298  N  N   . ARG A  1 684 ? 27.990  37.490 25.217  1.00 22.62 ? 684  ARG A N   1 
ATOM   5299  C  CA  . ARG A  1 684 ? 26.579  37.224 25.492  1.00 22.73 ? 684  ARG A CA  1 
ATOM   5300  C  C   . ARG A  1 684 ? 26.303  36.244 26.626  1.00 22.42 ? 684  ARG A C   1 
ATOM   5301  O  O   . ARG A  1 684 ? 25.232  36.271 27.229  1.00 23.07 ? 684  ARG A O   1 
ATOM   5302  C  CB  . ARG A  1 684 ? 25.862  36.779 24.201  1.00 22.95 ? 684  ARG A CB  1 
ATOM   5303  C  CG  . ARG A  1 684 ? 25.816  37.878 23.104  1.00 24.63 ? 684  ARG A CG  1 
ATOM   5304  C  CD  . ARG A  1 684 ? 25.052  39.150 23.559  1.00 25.61 ? 684  ARG A CD  1 
ATOM   5305  N  NE  . ARG A  1 684 ? 25.392  40.316 22.723  1.00 26.84 ? 684  ARG A NE  1 
ATOM   5306  C  CZ  . ARG A  1 684 ? 24.955  40.512 21.478  1.00 28.29 ? 684  ARG A CZ  1 
ATOM   5307  N  NH1 . ARG A  1 684 ? 24.144  39.632 20.901  1.00 29.03 ? 684  ARG A NH1 1 
ATOM   5308  N  NH2 . ARG A  1 684 ? 25.345  41.577 20.799  1.00 27.71 ? 684  ARG A NH2 1 
ATOM   5309  N  N   . ASN A  1 685 ? 27.269  35.402 26.945  1.00 22.43 ? 685  ASN A N   1 
ATOM   5310  C  CA  . ASN A  1 685 ? 27.077  34.420 28.012  1.00 23.33 ? 685  ASN A CA  1 
ATOM   5311  C  C   . ASN A  1 685 ? 27.527  34.945 29.367  1.00 22.09 ? 685  ASN A C   1 
ATOM   5312  O  O   . ASN A  1 685 ? 27.272  34.314 30.391  1.00 21.93 ? 685  ASN A O   1 
ATOM   5313  C  CB  . ASN A  1 685 ? 27.859  33.139 27.704  1.00 26.18 ? 685  ASN A CB  1 
ATOM   5314  C  CG  . ASN A  1 685 ? 27.154  32.254 26.697  1.00 29.99 ? 685  ASN A CG  1 
ATOM   5315  O  OD1 . ASN A  1 685 ? 25.995  31.862 26.893  1.00 33.67 ? 685  ASN A OD1 1 
ATOM   5316  N  ND2 . ASN A  1 685 ? 27.846  31.928 25.608  1.00 32.87 ? 685  ASN A ND2 1 
ATOM   5317  N  N   . SER A  1 686 ? 28.171  36.106 29.380  1.00 19.63 ? 686  SER A N   1 
ATOM   5318  C  CA  . SER A  1 686 ? 28.683  36.644 30.631  1.00 18.43 ? 686  SER A CA  1 
ATOM   5319  C  C   . SER A  1 686 ? 27.912  37.813 31.238  1.00 18.14 ? 686  SER A C   1 
ATOM   5320  O  O   . SER A  1 686 ? 28.482  38.629 31.972  1.00 17.48 ? 686  SER A O   1 
ATOM   5321  C  CB  . SER A  1 686 ? 30.149  37.042 30.442  1.00 17.62 ? 686  SER A CB  1 
ATOM   5322  O  OG  . SER A  1 686 ? 30.288  37.986 29.391  1.00 18.43 ? 686  SER A OG  1 
ATOM   5323  N  N   . THR A  1 687 ? 26.629  37.921 30.936  1.00 17.54 ? 687  THR A N   1 
ATOM   5324  C  CA  . THR A  1 687 ? 25.856  39.019 31.499  1.00 16.77 ? 687  THR A CA  1 
ATOM   5325  C  C   . THR A  1 687 ? 25.187  38.627 32.809  1.00 16.79 ? 687  THR A C   1 
ATOM   5326  O  O   . THR A  1 687 ? 24.953  37.447 33.079  1.00 16.86 ? 687  THR A O   1 
ATOM   5327  C  CB  . THR A  1 687 ? 24.725  39.454 30.559  1.00 18.46 ? 687  THR A CB  1 
ATOM   5328  O  OG1 . THR A  1 687 ? 23.690  38.450 30.562  1.00 16.89 ? 687  THR A OG1 1 
ATOM   5329  C  CG2 . THR A  1 687 ? 25.258  39.659 29.133  1.00 18.05 ? 687  THR A CG2 1 
ATOM   5330  N  N   . VAL A  1 688 ? 24.877  39.629 33.623  1.00 15.93 ? 688  VAL A N   1 
ATOM   5331  C  CA  . VAL A  1 688 ? 24.190  39.396 34.875  1.00 14.73 ? 688  VAL A CA  1 
ATOM   5332  C  C   . VAL A  1 688 ? 22.739  39.047 34.557  1.00 15.56 ? 688  VAL A C   1 
ATOM   5333  O  O   . VAL A  1 688 ? 22.161  38.134 35.161  1.00 16.04 ? 688  VAL A O   1 
ATOM   5334  C  CB  . VAL A  1 688 ? 24.219  40.645 35.758  1.00 13.83 ? 688  VAL A CB  1 
ATOM   5335  C  CG1 . VAL A  1 688 ? 23.335  40.458 36.963  1.00 13.19 ? 688  VAL A CG1 1 
ATOM   5336  C  CG2 . VAL A  1 688 ? 25.670  40.931 36.189  1.00 12.65 ? 688  VAL A CG2 1 
ATOM   5337  N  N   . MET A  1 689 ? 22.156  39.748 33.591  1.00 15.92 ? 689  MET A N   1 
ATOM   5338  C  CA  . MET A  1 689 ? 20.757  39.522 33.223  1.00 16.76 ? 689  MET A CA  1 
ATOM   5339  C  C   . MET A  1 689 ? 20.362  38.072 32.926  1.00 17.71 ? 689  MET A C   1 
ATOM   5340  O  O   . MET A  1 689 ? 19.280  37.640 33.323  1.00 18.18 ? 689  MET A O   1 
ATOM   5341  C  CB  . MET A  1 689 ? 20.368  40.397 32.026  1.00 16.17 ? 689  MET A CB  1 
ATOM   5342  C  CG  . MET A  1 689 ? 20.223  41.896 32.365  1.00 16.62 ? 689  MET A CG  1 
ATOM   5343  S  SD  . MET A  1 689 ? 21.785  42.772 32.749  1.00 14.74 ? 689  MET A SD  1 
ATOM   5344  C  CE  . MET A  1 689 ? 22.420  43.052 31.117  1.00 14.67 ? 689  MET A CE  1 
ATOM   5345  N  N   . SER A  1 690 ? 21.218  37.321 32.236  1.00 17.03 ? 690  SER A N   1 
ATOM   5346  C  CA  . SER A  1 690 ? 20.877  35.933 31.902  1.00 20.03 ? 690  SER A CA  1 
ATOM   5347  C  C   . SER A  1 690 ? 20.734  35.038 33.135  1.00 21.00 ? 690  SER A C   1 
ATOM   5348  O  O   . SER A  1 690 ? 20.178  33.951 33.044  1.00 20.01 ? 690  SER A O   1 
ATOM   5349  C  CB  . SER A  1 690 ? 21.930  35.318 30.972  1.00 20.02 ? 690  SER A CB  1 
ATOM   5350  O  OG  . SER A  1 690 ? 23.164  35.145 31.657  1.00 20.11 ? 690  SER A OG  1 
ATOM   5351  N  N   . ARG A  1 691 ? 21.223  35.495 34.285  1.00 20.88 ? 691  ARG A N   1 
ATOM   5352  C  CA  . ARG A  1 691 ? 21.138  34.699 35.508  1.00 20.39 ? 691  ARG A CA  1 
ATOM   5353  C  C   . ARG A  1 691 ? 20.018  35.158 36.458  1.00 19.97 ? 691  ARG A C   1 
ATOM   5354  O  O   . ARG A  1 691 ? 19.949  34.692 37.601  1.00 17.97 ? 691  ARG A O   1 
ATOM   5355  C  CB  . ARG A  1 691 ? 22.480  34.772 36.245  1.00 20.85 ? 691  ARG A CB  1 
ATOM   5356  C  CG  . ARG A  1 691 ? 23.654  34.373 35.366  1.00 21.08 ? 691  ARG A CG  1 
ATOM   5357  C  CD  . ARG A  1 691 ? 24.948  34.373 36.167  1.00 23.81 ? 691  ARG A CD  1 
ATOM   5358  N  NE  . ARG A  1 691 ? 26.046  33.779 35.422  1.00 22.96 ? 691  ARG A NE  1 
ATOM   5359  C  CZ  . ARG A  1 691 ? 27.123  33.233 35.983  1.00 24.79 ? 691  ARG A CZ  1 
ATOM   5360  N  NH1 . ARG A  1 691 ? 27.255  33.207 37.304  1.00 22.22 ? 691  ARG A NH1 1 
ATOM   5361  N  NH2 . ARG A  1 691 ? 28.057  32.682 35.214  1.00 24.07 ? 691  ARG A NH2 1 
ATOM   5362  N  N   . ALA A  1 692 ? 19.163  36.069 35.994  1.00 17.77 ? 692  ALA A N   1 
ATOM   5363  C  CA  . ALA A  1 692 ? 18.088  36.621 36.829  1.00 18.99 ? 692  ALA A CA  1 
ATOM   5364  C  C   . ALA A  1 692 ? 17.294  35.578 37.639  1.00 19.81 ? 692  ALA A C   1 
ATOM   5365  O  O   . ALA A  1 692 ? 17.096  35.722 38.848  1.00 18.66 ? 692  ALA A O   1 
ATOM   5366  C  CB  . ALA A  1 692 ? 17.126  37.453 35.963  1.00 17.72 ? 692  ALA A CB  1 
ATOM   5367  N  N   . GLU A  1 693 ? 16.840  34.531 36.965  1.00 22.31 ? 693  GLU A N   1 
ATOM   5368  C  CA  . GLU A  1 693 ? 16.070  33.460 37.606  1.00 23.78 ? 693  GLU A CA  1 
ATOM   5369  C  C   . GLU A  1 693 ? 16.725  32.942 38.890  1.00 23.24 ? 693  GLU A C   1 
ATOM   5370  O  O   . GLU A  1 693 ? 16.033  32.670 39.866  1.00 21.97 ? 693  GLU A O   1 
ATOM   5371  C  CB  . GLU A  1 693 ? 15.884  32.305 36.614  1.00 27.77 ? 693  GLU A CB  1 
ATOM   5372  C  CG  . GLU A  1 693 ? 14.874  31.274 37.037  1.00 32.84 ? 693  GLU A CG  1 
ATOM   5373  C  CD  . GLU A  1 693 ? 13.460  31.812 36.993  1.00 36.01 ? 693  GLU A CD  1 
ATOM   5374  O  OE1 . GLU A  1 693 ? 12.808  31.835 38.060  1.00 38.48 ? 693  GLU A OE1 1 
ATOM   5375  O  OE2 . GLU A  1 693 ? 13.006  32.208 35.890  1.00 38.44 ? 693  GLU A OE2 1 
ATOM   5376  N  N   . ASN A  1 694 ? 18.055  32.824 38.897  1.00 22.72 ? 694  ASN A N   1 
ATOM   5377  C  CA  . ASN A  1 694 ? 18.769  32.333 40.080  1.00 22.31 ? 694  ASN A CA  1 
ATOM   5378  C  C   . ASN A  1 694 ? 18.778  33.267 41.283  1.00 22.23 ? 694  ASN A C   1 
ATOM   5379  O  O   . ASN A  1 694 ? 19.278  32.888 42.343  1.00 23.06 ? 694  ASN A O   1 
ATOM   5380  C  CB  . ASN A  1 694 ? 20.218  31.983 39.747  1.00 23.57 ? 694  ASN A CB  1 
ATOM   5381  C  CG  . ASN A  1 694 ? 20.328  30.786 38.842  1.00 23.89 ? 694  ASN A CG  1 
ATOM   5382  O  OD1 . ASN A  1 694 ? 19.588  29.827 38.991  1.00 25.69 ? 694  ASN A OD1 1 
ATOM   5383  N  ND2 . ASN A  1 694 ? 21.254  30.829 37.911  1.00 23.66 ? 694  ASN A ND2 1 
ATOM   5384  N  N   . PHE A  1 695 ? 18.250  34.479 41.144  1.00 20.86 ? 695  PHE A N   1 
ATOM   5385  C  CA  . PHE A  1 695 ? 18.234  35.391 42.282  1.00 20.43 ? 695  PHE A CA  1 
ATOM   5386  C  C   . PHE A  1 695 ? 17.021  35.101 43.183  1.00 21.97 ? 695  PHE A C   1 
ATOM   5387  O  O   . PHE A  1 695 ? 16.825  35.757 44.211  1.00 20.67 ? 695  PHE A O   1 
ATOM   5388  C  CB  . PHE A  1 695 ? 18.191  36.856 41.819  1.00 18.37 ? 695  PHE A CB  1 
ATOM   5389  C  CG  . PHE A  1 695 ? 19.533  37.414 41.373  1.00 17.54 ? 695  PHE A CG  1 
ATOM   5390  C  CD1 . PHE A  1 695 ? 20.213  38.352 42.155  1.00 16.79 ? 695  PHE A CD1 1 
ATOM   5391  C  CD2 . PHE A  1 695 ? 20.082  37.042 40.151  1.00 16.09 ? 695  PHE A CD2 1 
ATOM   5392  C  CE1 . PHE A  1 695 ? 21.433  38.926 41.720  1.00 16.82 ? 695  PHE A CE1 1 
ATOM   5393  C  CE2 . PHE A  1 695 ? 21.287  37.593 39.694  1.00 16.29 ? 695  PHE A CE2 1 
ATOM   5394  C  CZ  . PHE A  1 695 ? 21.970  38.542 40.482  1.00 15.69 ? 695  PHE A CZ  1 
ATOM   5395  N  N   . LYS A  1 696 ? 16.203  34.122 42.801  1.00 24.38 ? 696  LYS A N   1 
ATOM   5396  C  CA  . LYS A  1 696 ? 15.022  33.801 43.606  1.00 26.85 ? 696  LYS A CA  1 
ATOM   5397  C  C   . LYS A  1 696 ? 15.344  33.400 45.025  1.00 26.70 ? 696  LYS A C   1 
ATOM   5398  O  O   . LYS A  1 696 ? 14.570  33.681 45.926  1.00 27.34 ? 696  LYS A O   1 
ATOM   5399  C  CB  . LYS A  1 696 ? 14.180  32.685 42.968  1.00 28.20 ? 696  LYS A CB  1 
ATOM   5400  C  CG  . LYS A  1 696 ? 13.209  33.197 41.923  1.00 32.51 ? 696  LYS A CG  1 
ATOM   5401  C  CD  . LYS A  1 696 ? 11.987  32.308 41.778  1.00 34.74 ? 696  LYS A CD  1 
ATOM   5402  C  CE  . LYS A  1 696 ? 10.891  33.034 40.981  1.00 37.56 ? 696  LYS A CE  1 
ATOM   5403  N  NZ  . LYS A  1 696 ? 11.254  33.272 39.553  1.00 38.92 ? 696  LYS A NZ  1 
ATOM   5404  N  N   . GLN A  1 697 ? 16.478  32.749 45.238  1.00 27.18 ? 697  GLN A N   1 
ATOM   5405  C  CA  . GLN A  1 697 ? 16.799  32.314 46.591  1.00 28.55 ? 697  GLN A CA  1 
ATOM   5406  C  C   . GLN A  1 697 ? 17.802  33.156 47.379  1.00 27.29 ? 697  GLN A C   1 
ATOM   5407  O  O   . GLN A  1 697 ? 18.408  32.647 48.323  1.00 27.12 ? 697  GLN A O   1 
ATOM   5408  C  CB  . GLN A  1 697 ? 17.263  30.846 46.584  1.00 31.26 ? 697  GLN A CB  1 
ATOM   5409  C  CG  . GLN A  1 697 ? 16.156  29.817 46.303  1.00 32.72 ? 697  GLN A CG  1 
ATOM   5410  C  CD  . GLN A  1 697 ? 16.521  28.404 46.773  1.00 35.20 ? 697  GLN A CD  1 
ATOM   5411  O  OE1 . GLN A  1 697 ? 16.411  28.076 47.972  1.00 35.46 ? 697  GLN A OE1 1 
ATOM   5412  N  NE2 . GLN A  1 697 ? 16.975  27.565 45.835  1.00 34.29 ? 697  GLN A NE2 1 
ATOM   5413  N  N   . VAL A  1 698 ? 17.969  34.430 47.012  1.00 25.05 ? 698  VAL A N   1 
ATOM   5414  C  CA  . VAL A  1 698 ? 18.893  35.315 47.721  1.00 23.14 ? 698  VAL A CA  1 
ATOM   5415  C  C   . VAL A  1 698 ? 18.289  36.702 47.903  1.00 23.07 ? 698  VAL A C   1 
ATOM   5416  O  O   . VAL A  1 698 ? 17.392  37.100 47.158  1.00 21.44 ? 698  VAL A O   1 
ATOM   5417  C  CB  . VAL A  1 698 ? 20.236  35.508 46.954  1.00 23.23 ? 698  VAL A CB  1 
ATOM   5418  C  CG1 . VAL A  1 698 ? 20.923  34.176 46.730  1.00 23.36 ? 698  VAL A CG1 1 
ATOM   5419  C  CG2 . VAL A  1 698 ? 19.989  36.203 45.630  1.00 22.37 ? 698  VAL A CG2 1 
ATOM   5420  N  N   . GLU A  1 699 ? 18.774  37.428 48.904  1.00 22.45 ? 699  GLU A N   1 
ATOM   5421  C  CA  . GLU A  1 699 ? 18.329  38.800 49.120  1.00 22.65 ? 699  GLU A CA  1 
ATOM   5422  C  C   . GLU A  1 699 ? 19.411  39.641 48.426  1.00 21.59 ? 699  GLU A C   1 
ATOM   5423  O  O   . GLU A  1 699 ? 20.613  39.498 48.696  1.00 20.66 ? 699  GLU A O   1 
ATOM   5424  C  CB  . GLU A  1 699 ? 18.259  39.138 50.606  1.00 23.86 ? 699  GLU A CB  1 
ATOM   5425  C  CG  . GLU A  1 699 ? 17.279  38.281 51.383  1.00 28.28 ? 699  GLU A CG  1 
ATOM   5426  C  CD  . GLU A  1 699 ? 17.402  38.514 52.871  1.00 31.54 ? 699  GLU A CD  1 
ATOM   5427  O  OE1 . GLU A  1 699 ? 17.304  39.692 53.299  1.00 32.88 ? 699  GLU A OE1 1 
ATOM   5428  O  OE2 . GLU A  1 699 ? 17.609  37.521 53.612  1.00 32.90 ? 699  GLU A OE2 1 
ATOM   5429  N  N   . TYR A  1 700 ? 18.968  40.511 47.531  1.00 19.55 ? 700  TYR A N   1 
ATOM   5430  C  CA  . TYR A  1 700 ? 19.860  41.329 46.730  1.00 17.74 ? 700  TYR A CA  1 
ATOM   5431  C  C   . TYR A  1 700 ? 19.535  42.803 46.865  1.00 17.09 ? 700  TYR A C   1 
ATOM   5432  O  O   . TYR A  1 700 ? 18.366  43.183 46.837  1.00 17.47 ? 700  TYR A O   1 
ATOM   5433  C  CB  . TYR A  1 700 ? 19.710  40.889 45.268  1.00 17.15 ? 700  TYR A CB  1 
ATOM   5434  C  CG  . TYR A  1 700 ? 20.546  41.619 44.228  1.00 16.98 ? 700  TYR A CG  1 
ATOM   5435  C  CD1 . TYR A  1 700 ? 21.937  41.710 44.347  1.00 14.58 ? 700  TYR A CD1 1 
ATOM   5436  C  CD2 . TYR A  1 700 ? 19.960  42.072 43.043  1.00 15.65 ? 700  TYR A CD2 1 
ATOM   5437  C  CE1 . TYR A  1 700 ? 22.726  42.217 43.301  1.00 16.24 ? 700  TYR A CE1 1 
ATOM   5438  C  CE2 . TYR A  1 700 ? 20.737  42.578 41.985  1.00 15.30 ? 700  TYR A CE2 1 
ATOM   5439  C  CZ  . TYR A  1 700 ? 22.118  42.640 42.110  1.00 16.16 ? 700  TYR A CZ  1 
ATOM   5440  O  OH  . TYR A  1 700 ? 22.902  43.022 41.025  1.00 15.58 ? 700  TYR A OH  1 
ATOM   5441  N  N   . LEU A  1 701 ? 20.566  43.630 47.017  1.00 15.88 ? 701  LEU A N   1 
ATOM   5442  C  CA  . LEU A  1 701 ? 20.392  45.080 47.126  1.00 15.69 ? 701  LEU A CA  1 
ATOM   5443  C  C   . LEU A  1 701 ? 21.228  45.655 45.981  1.00 14.75 ? 701  LEU A C   1 
ATOM   5444  O  O   . LEU A  1 701 ? 22.436  45.427 45.923  1.00 15.57 ? 701  LEU A O   1 
ATOM   5445  C  CB  . LEU A  1 701 ? 20.901  45.590 48.484  1.00 14.22 ? 701  LEU A CB  1 
ATOM   5446  C  CG  . LEU A  1 701 ? 21.045  47.117 48.645  1.00 14.91 ? 701  LEU A CG  1 
ATOM   5447  C  CD1 . LEU A  1 701 ? 19.726  47.828 48.349  1.00 12.33 ? 701  LEU A CD1 1 
ATOM   5448  C  CD2 . LEU A  1 701 ? 21.549  47.418 50.083  1.00 13.45 ? 701  LEU A CD2 1 
ATOM   5449  N  N   . LEU A  1 702 ? 20.574  46.365 45.066  1.00 14.30 ? 702  LEU A N   1 
ATOM   5450  C  CA  . LEU A  1 702 ? 21.213  46.956 43.876  1.00 13.38 ? 702  LEU A CA  1 
ATOM   5451  C  C   . LEU A  1 702 ? 21.236  48.478 44.016  1.00 13.26 ? 702  LEU A C   1 
ATOM   5452  O  O   . LEU A  1 702 ? 20.188  49.112 44.155  1.00 13.75 ? 702  LEU A O   1 
ATOM   5453  C  CB  . LEU A  1 702 ? 20.412  46.545 42.627  1.00 13.04 ? 702  LEU A CB  1 
ATOM   5454  C  CG  . LEU A  1 702 ? 20.849  47.015 41.248  1.00 13.01 ? 702  LEU A CG  1 
ATOM   5455  C  CD1 . LEU A  1 702 ? 22.219  46.436 40.893  1.00 12.82 ? 702  LEU A CD1 1 
ATOM   5456  C  CD2 . LEU A  1 702 ? 19.825  46.543 40.226  1.00 12.19 ? 702  LEU A CD2 1 
ATOM   5457  N  N   . ILE A  1 703 ? 22.428  49.064 43.921  1.00 13.63 ? 703  ILE A N   1 
ATOM   5458  C  CA  . ILE A  1 703 ? 22.612  50.501 44.096  1.00 13.55 ? 703  ILE A CA  1 
ATOM   5459  C  C   . ILE A  1 703 ? 23.408  51.097 42.930  1.00 13.98 ? 703  ILE A C   1 
ATOM   5460  O  O   . ILE A  1 703 ? 24.359  50.482 42.450  1.00 12.17 ? 703  ILE A O   1 
ATOM   5461  C  CB  . ILE A  1 703 ? 23.381  50.761 45.426  1.00 13.89 ? 703  ILE A CB  1 
ATOM   5462  C  CG1 . ILE A  1 703 ? 22.638  50.057 46.586  1.00 13.81 ? 703  ILE A CG1 1 
ATOM   5463  C  CG2 . ILE A  1 703 ? 23.557  52.271 45.668  1.00 14.05 ? 703  ILE A CG2 1 
ATOM   5464  C  CD1 . ILE A  1 703 ? 23.336  50.136 47.975  1.00 12.78 ? 703  ILE A CD1 1 
ATOM   5465  N  N   . HIS A  1 704 ? 23.043  52.304 42.501  1.00 13.94 ? 704  HIS A N   1 
ATOM   5466  C  CA  . HIS A  1 704 ? 23.750  52.957 41.383  1.00 14.71 ? 704  HIS A CA  1 
ATOM   5467  C  C   . HIS A  1 704 ? 23.487  54.461 41.339  1.00 14.75 ? 704  HIS A C   1 
ATOM   5468  O  O   . HIS A  1 704 ? 22.372  54.897 41.600  1.00 14.04 ? 704  HIS A O   1 
ATOM   5469  C  CB  . HIS A  1 704 ? 23.296  52.337 40.058  1.00 13.95 ? 704  HIS A CB  1 
ATOM   5470  C  CG  . HIS A  1 704 ? 24.351  52.309 39.000  1.00 14.60 ? 704  HIS A CG  1 
ATOM   5471  N  ND1 . HIS A  1 704 ? 24.702  51.147 38.343  1.00 15.54 ? 704  HIS A ND1 1 
ATOM   5472  C  CD2 . HIS A  1 704 ? 25.122  53.291 38.467  1.00 14.70 ? 704  HIS A CD2 1 
ATOM   5473  C  CE1 . HIS A  1 704 ? 25.640  51.413 37.451  1.00 14.77 ? 704  HIS A CE1 1 
ATOM   5474  N  NE2 . HIS A  1 704 ? 25.913  52.705 37.504  1.00 14.63 ? 704  HIS A NE2 1 
ATOM   5475  N  N   . GLY A  1 705 ? 24.511  55.252 41.015  1.00 15.00 ? 705  GLY A N   1 
ATOM   5476  C  CA  . GLY A  1 705 ? 24.327  56.692 40.923  1.00 14.44 ? 705  GLY A CA  1 
ATOM   5477  C  C   . GLY A  1 705 ? 23.780  57.005 39.534  1.00 14.67 ? 705  GLY A C   1 
ATOM   5478  O  O   . GLY A  1 705 ? 24.257  56.483 38.530  1.00 15.82 ? 705  GLY A O   1 
ATOM   5479  N  N   . THR A  1 706 ? 22.781  57.865 39.454  1.00 14.44 ? 706  THR A N   1 
ATOM   5480  C  CA  . THR A  1 706 ? 22.188  58.184 38.157  1.00 14.81 ? 706  THR A CA  1 
ATOM   5481  C  C   . THR A  1 706 ? 23.090  58.971 37.213  1.00 14.37 ? 706  THR A C   1 
ATOM   5482  O  O   . THR A  1 706 ? 22.888  58.959 36.003  1.00 15.64 ? 706  THR A O   1 
ATOM   5483  C  CB  . THR A  1 706 ? 20.843  58.942 38.332  1.00 15.50 ? 706  THR A CB  1 
ATOM   5484  O  OG1 . THR A  1 706 ? 21.095  60.262 38.817  1.00 14.31 ? 706  THR A OG1 1 
ATOM   5485  C  CG2 . THR A  1 706 ? 19.945  58.205 39.351  1.00 15.91 ? 706  THR A CG2 1 
ATOM   5486  N  N   . ALA A  1 707 ? 24.101  59.638 37.752  1.00 14.12 ? 707  ALA A N   1 
ATOM   5487  C  CA  . ALA A  1 707 ? 25.008  60.408 36.904  1.00 13.65 ? 707  ALA A CA  1 
ATOM   5488  C  C   . ALA A  1 707 ? 26.369  59.696 36.712  1.00 13.23 ? 707  ALA A C   1 
ATOM   5489  O  O   . ALA A  1 707 ? 27.393  60.336 36.481  1.00 13.01 ? 707  ALA A O   1 
ATOM   5490  C  CB  . ALA A  1 707 ? 25.206  61.845 37.503  1.00 11.55 ? 707  ALA A CB  1 
ATOM   5491  N  N   . ASP A  1 708 ? 26.365  58.369 36.778  1.00 12.87 ? 708  ASP A N   1 
ATOM   5492  C  CA  . ASP A  1 708 ? 27.581  57.596 36.599  1.00 13.14 ? 708  ASP A CA  1 
ATOM   5493  C  C   . ASP A  1 708 ? 27.981  57.667 35.124  1.00 14.22 ? 708  ASP A C   1 
ATOM   5494  O  O   . ASP A  1 708 ? 27.297  57.110 34.265  1.00 14.17 ? 708  ASP A O   1 
ATOM   5495  C  CB  . ASP A  1 708 ? 27.338  56.139 37.000  1.00 13.56 ? 708  ASP A CB  1 
ATOM   5496  C  CG  . ASP A  1 708 ? 28.622  55.400 37.317  1.00 12.99 ? 708  ASP A CG  1 
ATOM   5497  O  OD1 . ASP A  1 708 ? 29.650  55.685 36.664  1.00 13.51 ? 708  ASP A OD1 1 
ATOM   5498  O  OD2 . ASP A  1 708 ? 28.604  54.526 38.206  1.00 11.50 ? 708  ASP A OD2 1 
ATOM   5499  N  N   . ASP A  1 709 ? 29.075  58.377 34.843  1.00 13.82 ? 709  ASP A N   1 
ATOM   5500  C  CA  . ASP A  1 709 ? 29.599  58.551 33.485  1.00 14.38 ? 709  ASP A CA  1 
ATOM   5501  C  C   . ASP A  1 709 ? 30.517  57.406 33.098  1.00 14.78 ? 709  ASP A C   1 
ATOM   5502  O  O   . ASP A  1 709 ? 30.868  57.266 31.924  1.00 16.23 ? 709  ASP A O   1 
ATOM   5503  C  CB  . ASP A  1 709 ? 30.439  59.819 33.427  1.00 15.17 ? 709  ASP A CB  1 
ATOM   5504  C  CG  . ASP A  1 709 ? 31.549  59.796 34.460  1.00 14.52 ? 709  ASP A CG  1 
ATOM   5505  O  OD1 . ASP A  1 709 ? 31.247  60.077 35.643  1.00 14.04 ? 709  ASP A OD1 1 
ATOM   5506  O  OD2 . ASP A  1 709 ? 32.704  59.468 34.098  1.00 12.57 ? 709  ASP A OD2 1 
ATOM   5507  N  N   . ASN A  1 710 ? 30.929  56.613 34.086  1.00 14.80 ? 710  ASN A N   1 
ATOM   5508  C  CA  . ASN A  1 710 ? 31.862  55.484 33.891  1.00 14.34 ? 710  ASN A CA  1 
ATOM   5509  C  C   . ASN A  1 710 ? 31.112  54.157 33.590  1.00 14.53 ? 710  ASN A C   1 
ATOM   5510  O  O   . ASN A  1 710 ? 31.158  53.639 32.465  1.00 14.38 ? 710  ASN A O   1 
ATOM   5511  C  CB  . ASN A  1 710 ? 32.713  55.372 35.167  1.00 13.32 ? 710  ASN A CB  1 
ATOM   5512  C  CG  . ASN A  1 710 ? 33.888  54.437 35.004  1.00 13.51 ? 710  ASN A CG  1 
ATOM   5513  O  OD1 . ASN A  1 710 ? 33.919  53.601 34.097  1.00 14.46 ? 710  ASN A OD1 1 
ATOM   5514  N  ND2 . ASN A  1 710 ? 34.854  54.559 35.890  1.00 12.88 ? 710  ASN A ND2 1 
ATOM   5515  N  N   . VAL A  1 711 ? 30.442  53.611 34.611  1.00 14.34 ? 711  VAL A N   1 
ATOM   5516  C  CA  . VAL A  1 711 ? 29.615  52.403 34.473  1.00 13.65 ? 711  VAL A CA  1 
ATOM   5517  C  C   . VAL A  1 711 ? 28.221  53.036 34.487  1.00 14.27 ? 711  VAL A C   1 
ATOM   5518  O  O   . VAL A  1 711 ? 27.677  53.375 35.546  1.00 14.74 ? 711  VAL A O   1 
ATOM   5519  C  CB  . VAL A  1 711 ? 29.773  51.454 35.678  1.00 14.04 ? 711  VAL A CB  1 
ATOM   5520  C  CG1 . VAL A  1 711 ? 28.811  50.262 35.532  1.00 12.09 ? 711  VAL A CG1 1 
ATOM   5521  C  CG2 . VAL A  1 711 ? 31.234  50.969 35.759  1.00 13.07 ? 711  VAL A CG2 1 
ATOM   5522  N  N   . HIS A  1 712 ? 27.656  53.212 33.302  1.00 13.62 ? 712  HIS A N   1 
ATOM   5523  C  CA  . HIS A  1 712 ? 26.383  53.898 33.173  1.00 13.77 ? 712  HIS A CA  1 
ATOM   5524  C  C   . HIS A  1 712 ? 25.223  53.306 33.971  1.00 13.75 ? 712  HIS A C   1 
ATOM   5525  O  O   . HIS A  1 712 ? 25.127  52.091 34.140  1.00 13.35 ? 712  HIS A O   1 
ATOM   5526  C  CB  . HIS A  1 712 ? 26.032  54.022 31.680  1.00 13.73 ? 712  HIS A CB  1 
ATOM   5527  C  CG  . HIS A  1 712 ? 27.163  54.558 30.849  1.00 13.99 ? 712  HIS A CG  1 
ATOM   5528  N  ND1 . HIS A  1 712 ? 27.959  55.606 31.268  1.00 14.69 ? 712  HIS A ND1 1 
ATOM   5529  C  CD2 . HIS A  1 712 ? 27.644  54.180 29.642  1.00 13.63 ? 712  HIS A CD2 1 
ATOM   5530  C  CE1 . HIS A  1 712 ? 28.888  55.844 30.357  1.00 13.99 ? 712  HIS A CE1 1 
ATOM   5531  N  NE2 . HIS A  1 712 ? 28.716  54.993 29.360  1.00 16.34 ? 712  HIS A NE2 1 
ATOM   5532  N  N   . PHE A  1 713 ? 24.348  54.178 34.467  1.00 12.02 ? 713  PHE A N   1 
ATOM   5533  C  CA  . PHE A  1 713 ? 23.194  53.721 35.235  1.00 13.67 ? 713  PHE A CA  1 
ATOM   5534  C  C   . PHE A  1 713 ? 22.491  52.623 34.404  1.00 14.24 ? 713  PHE A C   1 
ATOM   5535  O  O   . PHE A  1 713 ? 21.900  51.696 34.945  1.00 13.58 ? 713  PHE A O   1 
ATOM   5536  C  CB  . PHE A  1 713 ? 22.239  54.893 35.515  1.00 11.69 ? 713  PHE A CB  1 
ATOM   5537  C  CG  . PHE A  1 713 ? 21.071  54.522 36.388  1.00 14.04 ? 713  PHE A CG  1 
ATOM   5538  C  CD1 . PHE A  1 713 ? 21.222  54.439 37.774  1.00 12.78 ? 713  PHE A CD1 1 
ATOM   5539  C  CD2 . PHE A  1 713 ? 19.822  54.222 35.824  1.00 12.56 ? 713  PHE A CD2 1 
ATOM   5540  C  CE1 . PHE A  1 713 ? 20.139  54.060 38.604  1.00 14.62 ? 713  PHE A CE1 1 
ATOM   5541  C  CE2 . PHE A  1 713 ? 18.741  53.841 36.631  1.00 14.43 ? 713  PHE A CE2 1 
ATOM   5542  C  CZ  . PHE A  1 713 ? 18.897  53.757 38.037  1.00 14.55 ? 713  PHE A CZ  1 
ATOM   5543  N  N   . GLN A  1 714 ? 22.558  52.746 33.083  1.00 14.34 ? 714  GLN A N   1 
ATOM   5544  C  CA  . GLN A  1 714 ? 21.992  51.749 32.168  1.00 14.70 ? 714  GLN A CA  1 
ATOM   5545  C  C   . GLN A  1 714 ? 22.257  50.313 32.628  1.00 14.37 ? 714  GLN A C   1 
ATOM   5546  O  O   . GLN A  1 714 ? 21.376  49.460 32.589  1.00 12.49 ? 714  GLN A O   1 
ATOM   5547  C  CB  . GLN A  1 714 ? 22.638  51.912 30.792  1.00 14.39 ? 714  GLN A CB  1 
ATOM   5548  C  CG  . GLN A  1 714 ? 22.492  50.715 29.834  1.00 15.26 ? 714  GLN A CG  1 
ATOM   5549  C  CD  . GLN A  1 714 ? 23.415  50.841 28.615  1.00 14.30 ? 714  GLN A CD  1 
ATOM   5550  O  OE1 . GLN A  1 714 ? 24.581  51.178 28.751  1.00 14.44 ? 714  GLN A OE1 1 
ATOM   5551  N  NE2 . GLN A  1 714 ? 22.900  50.547 27.441  1.00 13.39 ? 714  GLN A NE2 1 
ATOM   5552  N  N   . GLN A  1 715 ? 23.489  50.053 33.047  1.00 13.77 ? 715  GLN A N   1 
ATOM   5553  C  CA  . GLN A  1 715 ? 23.872  48.714 33.442  1.00 13.74 ? 715  GLN A CA  1 
ATOM   5554  C  C   . GLN A  1 715 ? 22.973  48.136 34.555  1.00 14.35 ? 715  GLN A C   1 
ATOM   5555  O  O   . GLN A  1 715 ? 22.571  46.978 34.469  1.00 14.29 ? 715  GLN A O   1 
ATOM   5556  C  CB  . GLN A  1 715 ? 25.367  48.699 33.818  1.00 13.74 ? 715  GLN A CB  1 
ATOM   5557  C  CG  . GLN A  1 715 ? 26.265  49.299 32.714  1.00 13.52 ? 715  GLN A CG  1 
ATOM   5558  C  CD  . GLN A  1 715 ? 27.462  48.423 32.335  1.00 13.47 ? 715  GLN A CD  1 
ATOM   5559  O  OE1 . GLN A  1 715 ? 27.361  47.204 32.358  1.00 13.61 ? 715  GLN A OE1 1 
ATOM   5560  N  NE2 . GLN A  1 715 ? 28.582  49.044 31.955  1.00 10.41 ? 715  GLN A NE2 1 
ATOM   5561  N  N   . SER A  1 716 ? 22.627  48.935 35.566  1.00 13.79 ? 716  SER A N   1 
ATOM   5562  C  CA  . SER A  1 716 ? 21.755  48.461 36.648  1.00 14.71 ? 716  SER A CA  1 
ATOM   5563  C  C   . SER A  1 716 ? 20.299  48.494 36.225  1.00 15.20 ? 716  SER A C   1 
ATOM   5564  O  O   . SER A  1 716 ? 19.495  47.683 36.697  1.00 14.71 ? 716  SER A O   1 
ATOM   5565  C  CB  . SER A  1 716 ? 21.908  49.314 37.916  1.00 15.38 ? 716  SER A CB  1 
ATOM   5566  O  OG  . SER A  1 716 ? 23.091  48.981 38.600  1.00 15.10 ? 716  SER A OG  1 
ATOM   5567  N  N   . ALA A  1 717 ? 19.956  49.440 35.349  1.00 14.39 ? 717  ALA A N   1 
ATOM   5568  C  CA  . ALA A  1 717 ? 18.584  49.553 34.859  1.00 14.46 ? 717  ALA A CA  1 
ATOM   5569  C  C   . ALA A  1 717 ? 18.220  48.274 34.119  1.00 15.03 ? 717  ALA A C   1 
ATOM   5570  O  O   . ALA A  1 717 ? 17.067  47.851 34.148  1.00 14.47 ? 717  ALA A O   1 
ATOM   5571  C  CB  . ALA A  1 717 ? 18.439  50.746 33.934  1.00 14.80 ? 717  ALA A CB  1 
ATOM   5572  N  N   . GLN A  1 718 ? 19.205  47.652 33.466  1.00 13.27 ? 718  GLN A N   1 
ATOM   5573  C  CA  . GLN A  1 718 ? 18.949  46.411 32.736  1.00 13.80 ? 718  GLN A CA  1 
ATOM   5574  C  C   . GLN A  1 718 ? 18.898  45.228 33.717  1.00 14.17 ? 718  GLN A C   1 
ATOM   5575  O  O   . GLN A  1 718 ? 18.179  44.256 33.482  1.00 14.39 ? 718  GLN A O   1 
ATOM   5576  C  CB  . GLN A  1 718 ? 20.001  46.187 31.641  1.00 13.05 ? 718  GLN A CB  1 
ATOM   5577  C  CG  . GLN A  1 718 ? 19.922  47.171 30.474  1.00 13.29 ? 718  GLN A CG  1 
ATOM   5578  C  CD  . GLN A  1 718 ? 18.710  46.957 29.567  1.00 15.18 ? 718  GLN A CD  1 
ATOM   5579  O  OE1 . GLN A  1 718 ? 17.834  46.113 29.843  1.00 14.79 ? 718  GLN A OE1 1 
ATOM   5580  N  NE2 . GLN A  1 718 ? 18.644  47.731 28.478  1.00 13.50 ? 718  GLN A NE2 1 
ATOM   5581  N  N   . ILE A  1 719 ? 19.638  45.310 34.826  1.00 14.22 ? 719  ILE A N   1 
ATOM   5582  C  CA  . ILE A  1 719 ? 19.577  44.241 35.830  1.00 13.81 ? 719  ILE A CA  1 
ATOM   5583  C  C   . ILE A  1 719 ? 18.198  44.228 36.492  1.00 14.21 ? 719  ILE A C   1 
ATOM   5584  O  O   . ILE A  1 719 ? 17.545  43.182 36.597  1.00 14.50 ? 719  ILE A O   1 
ATOM   5585  C  CB  . ILE A  1 719 ? 20.604  44.435 36.975  1.00 14.22 ? 719  ILE A CB  1 
ATOM   5586  C  CG1 . ILE A  1 719 ? 22.031  44.347 36.413  1.00 13.07 ? 719  ILE A CG1 1 
ATOM   5587  C  CG2 . ILE A  1 719 ? 20.372  43.379 38.067  1.00 11.41 ? 719  ILE A CG2 1 
ATOM   5588  C  CD1 . ILE A  1 719 ? 23.154  44.447 37.493  1.00 14.38 ? 719  ILE A CD1 1 
ATOM   5589  N  N   . SER A  1 720 ? 17.753  45.395 36.937  1.00 13.77 ? 720  SER A N   1 
ATOM   5590  C  CA  . SER A  1 720 ? 16.479  45.483 37.615  1.00 13.96 ? 720  SER A CA  1 
ATOM   5591  C  C   . SER A  1 720 ? 15.345  45.012 36.705  1.00 14.74 ? 720  SER A C   1 
ATOM   5592  O  O   . SER A  1 720 ? 14.434  44.329 37.170  1.00 13.93 ? 720  SER A O   1 
ATOM   5593  C  CB  . SER A  1 720 ? 16.220  46.909 38.123  1.00 12.94 ? 720  SER A CB  1 
ATOM   5594  O  OG  . SER A  1 720 ? 16.063  47.822 37.050  1.00 13.91 ? 720  SER A OG  1 
ATOM   5595  N  N   . LYS A  1 721 ? 15.400  45.361 35.418  1.00 15.38 ? 721  LYS A N   1 
ATOM   5596  C  CA  . LYS A  1 721 ? 14.354  44.949 34.474  1.00 16.09 ? 721  LYS A CA  1 
ATOM   5597  C  C   . LYS A  1 721 ? 14.324  43.421 34.311  1.00 16.87 ? 721  LYS A C   1 
ATOM   5598  O  O   . LYS A  1 721 ? 13.237  42.820 34.276  1.00 17.39 ? 721  LYS A O   1 
ATOM   5599  C  CB  . LYS A  1 721 ? 14.541  45.647 33.111  1.00 16.12 ? 721  LYS A CB  1 
ATOM   5600  C  CG  . LYS A  1 721 ? 13.463  45.317 32.069  1.00 16.21 ? 721  LYS A CG  1 
ATOM   5601  C  CD  . LYS A  1 721 ? 13.213  46.470 31.065  1.00 15.17 ? 721  LYS A CD  1 
ATOM   5602  C  CE  . LYS A  1 721 ? 14.443  46.856 30.235  1.00 15.47 ? 721  LYS A CE  1 
ATOM   5603  N  NZ  . LYS A  1 721 ? 15.117  45.743 29.489  1.00 15.96 ? 721  LYS A NZ  1 
ATOM   5604  N  N   . ALA A  1 722 ? 15.497  42.794 34.233  1.00 16.67 ? 722  ALA A N   1 
ATOM   5605  C  CA  . ALA A  1 722 ? 15.558  41.334 34.102  1.00 17.52 ? 722  ALA A CA  1 
ATOM   5606  C  C   . ALA A  1 722 ? 14.970  40.641 35.353  1.00 17.60 ? 722  ALA A C   1 
ATOM   5607  O  O   . ALA A  1 722 ? 14.270  39.630 35.240  1.00 17.55 ? 722  ALA A O   1 
ATOM   5608  C  CB  . ALA A  1 722 ? 17.000  40.872 33.865  1.00 16.93 ? 722  ALA A CB  1 
ATOM   5609  N  N   . LEU A  1 723 ? 15.242  41.188 36.535  1.00 17.50 ? 723  LEU A N   1 
ATOM   5610  C  CA  . LEU A  1 723 ? 14.712  40.621 37.766  1.00 17.62 ? 723  LEU A CA  1 
ATOM   5611  C  C   . LEU A  1 723 ? 13.184  40.795 37.804  1.00 18.51 ? 723  LEU A C   1 
ATOM   5612  O  O   . LEU A  1 723 ? 12.450  39.886 38.224  1.00 18.47 ? 723  LEU A O   1 
ATOM   5613  C  CB  . LEU A  1 723 ? 15.368  41.277 38.983  1.00 15.90 ? 723  LEU A CB  1 
ATOM   5614  C  CG  . LEU A  1 723 ? 16.876  41.009 39.097  1.00 17.72 ? 723  LEU A CG  1 
ATOM   5615  C  CD1 . LEU A  1 723 ? 17.457  41.817 40.253  1.00 14.78 ? 723  LEU A CD1 1 
ATOM   5616  C  CD2 . LEU A  1 723 ? 17.145  39.511 39.301  1.00 15.78 ? 723  LEU A CD2 1 
ATOM   5617  N  N   . VAL A  1 724 ? 12.705  41.955 37.364  1.00 18.54 ? 724  VAL A N   1 
ATOM   5618  C  CA  . VAL A  1 724 ? 11.273  42.188 37.327  1.00 19.16 ? 724  VAL A CA  1 
ATOM   5619  C  C   . VAL A  1 724 ? 10.662  41.188 36.336  1.00 19.55 ? 724  VAL A C   1 
ATOM   5620  O  O   . VAL A  1 724 ? 9.637   40.571 36.620  1.00 20.09 ? 724  VAL A O   1 
ATOM   5621  C  CB  . VAL A  1 724 ? 10.932  43.642 36.873  1.00 18.70 ? 724  VAL A CB  1 
ATOM   5622  C  CG1 . VAL A  1 724 ? 9.422   43.772 36.575  1.00 17.71 ? 724  VAL A CG1 1 
ATOM   5623  C  CG2 . VAL A  1 724 ? 11.307  44.616 37.961  1.00 17.56 ? 724  VAL A CG2 1 
ATOM   5624  N  N   . ASP A  1 725 ? 11.303  41.008 35.187  1.00 20.37 ? 725  ASP A N   1 
ATOM   5625  C  CA  . ASP A  1 725 ? 10.775  40.096 34.189  1.00 22.61 ? 725  ASP A CA  1 
ATOM   5626  C  C   . ASP A  1 725 ? 10.643  38.635 34.632  1.00 23.26 ? 725  ASP A C   1 
ATOM   5627  O  O   . ASP A  1 725 ? 9.825   37.907 34.074  1.00 23.57 ? 725  ASP A O   1 
ATOM   5628  C  CB  . ASP A  1 725 ? 11.587  40.185 32.893  1.00 24.29 ? 725  ASP A CB  1 
ATOM   5629  C  CG  . ASP A  1 725 ? 11.344  41.502 32.134  1.00 26.39 ? 725  ASP A CG  1 
ATOM   5630  O  OD1 . ASP A  1 725 ? 10.471  42.300 32.546  1.00 27.76 ? 725  ASP A OD1 1 
ATOM   5631  O  OD2 . ASP A  1 725 ? 12.024  41.731 31.124  1.00 28.65 ? 725  ASP A OD2 1 
ATOM   5632  N  N   . VAL A  1 726 ? 11.434  38.194 35.613  1.00 22.98 ? 726  VAL A N   1 
ATOM   5633  C  CA  . VAL A  1 726 ? 11.319  36.815 36.096  1.00 22.58 ? 726  VAL A CA  1 
ATOM   5634  C  C   . VAL A  1 726 ? 10.602  36.748 37.444  1.00 21.93 ? 726  VAL A C   1 
ATOM   5635  O  O   . VAL A  1 726 ? 10.532  35.701 38.059  1.00 22.81 ? 726  VAL A O   1 
ATOM   5636  C  CB  . VAL A  1 726 ? 12.695  36.113 36.230  1.00 23.34 ? 726  VAL A CB  1 
ATOM   5637  C  CG1 . VAL A  1 726 ? 13.324  35.947 34.845  1.00 23.82 ? 726  VAL A CG1 1 
ATOM   5638  C  CG2 . VAL A  1 726 ? 13.614  36.902 37.182  1.00 22.57 ? 726  VAL A CG2 1 
ATOM   5639  N  N   . GLY A  1 727 ? 10.074  37.872 37.905  1.00 21.50 ? 727  GLY A N   1 
ATOM   5640  C  CA  . GLY A  1 727 ? 9.360   37.887 39.170  1.00 21.11 ? 727  GLY A CA  1 
ATOM   5641  C  C   . GLY A  1 727 ? 10.192  37.686 40.430  1.00 22.04 ? 727  GLY A C   1 
ATOM   5642  O  O   . GLY A  1 727 ? 9.756   37.005 41.371  1.00 20.86 ? 727  GLY A O   1 
ATOM   5643  N  N   . VAL A  1 728 ? 11.387  38.269 40.469  1.00 20.78 ? 728  VAL A N   1 
ATOM   5644  C  CA  . VAL A  1 728 ? 12.215  38.145 41.661  1.00 20.84 ? 728  VAL A CA  1 
ATOM   5645  C  C   . VAL A  1 728 ? 12.233  39.478 42.403  1.00 20.69 ? 728  VAL A C   1 
ATOM   5646  O  O   . VAL A  1 728 ? 12.515  40.525 41.820  1.00 21.42 ? 728  VAL A O   1 
ATOM   5647  C  CB  . VAL A  1 728 ? 13.671  37.691 41.312  1.00 22.80 ? 728  VAL A CB  1 
ATOM   5648  C  CG1 . VAL A  1 728 ? 14.201  38.507 40.186  1.00 25.24 ? 728  VAL A CG1 1 
ATOM   5649  C  CG2 . VAL A  1 728 ? 14.587  37.875 42.500  1.00 22.31 ? 728  VAL A CG2 1 
ATOM   5650  N  N   . ASP A  1 729 ? 11.895  39.443 43.688  1.00 19.56 ? 729  ASP A N   1 
ATOM   5651  C  CA  . ASP A  1 729 ? 11.901  40.648 44.489  1.00 19.53 ? 729  ASP A CA  1 
ATOM   5652  C  C   . ASP A  1 729 ? 13.338  40.968 44.904  1.00 19.30 ? 729  ASP A C   1 
ATOM   5653  O  O   . ASP A  1 729 ? 14.160  40.065 45.054  1.00 17.90 ? 729  ASP A O   1 
ATOM   5654  C  CB  . ASP A  1 729 ? 11.029  40.482 45.739  1.00 20.98 ? 729  ASP A CB  1 
ATOM   5655  C  CG  . ASP A  1 729 ? 10.858  41.794 46.504  1.00 22.37 ? 729  ASP A CG  1 
ATOM   5656  O  OD1 . ASP A  1 729 ? 10.593  42.814 45.842  1.00 23.07 ? 729  ASP A OD1 1 
ATOM   5657  O  OD2 . ASP A  1 729 ? 10.985  41.817 47.753  1.00 23.21 ? 729  ASP A OD2 1 
ATOM   5658  N  N   . PHE A  1 730 ? 13.642  42.254 45.058  1.00 18.06 ? 730  PHE A N   1 
ATOM   5659  C  CA  . PHE A  1 730 ? 14.984  42.682 45.476  1.00 17.94 ? 730  PHE A CA  1 
ATOM   5660  C  C   . PHE A  1 730 ? 14.891  44.108 46.019  1.00 17.68 ? 730  PHE A C   1 
ATOM   5661  O  O   . PHE A  1 730 ? 13.829  44.748 45.918  1.00 17.31 ? 730  PHE A O   1 
ATOM   5662  C  CB  . PHE A  1 730 ? 15.971  42.598 44.291  1.00 16.92 ? 730  PHE A CB  1 
ATOM   5663  C  CG  . PHE A  1 730 ? 15.652  43.541 43.172  1.00 17.30 ? 730  PHE A CG  1 
ATOM   5664  C  CD1 . PHE A  1 730 ? 16.258  44.792 43.103  1.00 18.23 ? 730  PHE A CD1 1 
ATOM   5665  C  CD2 . PHE A  1 730 ? 14.699  43.208 42.219  1.00 17.87 ? 730  PHE A CD2 1 
ATOM   5666  C  CE1 . PHE A  1 730 ? 15.907  45.705 42.096  1.00 18.28 ? 730  PHE A CE1 1 
ATOM   5667  C  CE2 . PHE A  1 730 ? 14.340  44.114 41.208  1.00 18.26 ? 730  PHE A CE2 1 
ATOM   5668  C  CZ  . PHE A  1 730 ? 14.949  45.368 41.152  1.00 16.82 ? 730  PHE A CZ  1 
ATOM   5669  N  N   . GLN A  1 731 ? 15.985  44.592 46.603  1.00 17.33 ? 731  GLN A N   1 
ATOM   5670  C  CA  . GLN A  1 731 ? 16.045  45.942 47.170  1.00 17.63 ? 731  GLN A CA  1 
ATOM   5671  C  C   . GLN A  1 731 ? 16.862  46.816 46.218  1.00 17.52 ? 731  GLN A C   1 
ATOM   5672  O  O   . GLN A  1 731 ? 17.812  46.342 45.580  1.00 16.02 ? 731  GLN A O   1 
ATOM   5673  C  CB  . GLN A  1 731 ? 16.731  45.912 48.543  1.00 19.01 ? 731  GLN A CB  1 
ATOM   5674  C  CG  . GLN A  1 731 ? 16.277  44.754 49.433  1.00 23.39 ? 731  GLN A CG  1 
ATOM   5675  C  CD  . GLN A  1 731 ? 14.790  44.777 49.682  1.00 25.41 ? 731  GLN A CD  1 
ATOM   5676  O  OE1 . GLN A  1 731 ? 14.112  43.743 49.622  1.00 30.03 ? 731  GLN A OE1 1 
ATOM   5677  N  NE2 . GLN A  1 731 ? 14.265  45.958 49.968  1.00 26.29 ? 731  GLN A NE2 1 
ATOM   5678  N  N   . ALA A  1 732 ? 16.509  48.089 46.136  1.00 16.39 ? 732  ALA A N   1 
ATOM   5679  C  CA  . ALA A  1 732 ? 17.218  48.987 45.246  1.00 16.04 ? 732  ALA A CA  1 
ATOM   5680  C  C   . ALA A  1 732 ? 17.366  50.351 45.846  1.00 15.33 ? 732  ALA A C   1 
ATOM   5681  O  O   . ALA A  1 732 ? 16.638  50.727 46.752  1.00 16.28 ? 732  ALA A O   1 
ATOM   5682  C  CB  . ALA A  1 732 ? 16.468  49.115 43.920  1.00 15.10 ? 732  ALA A CB  1 
ATOM   5683  N  N   . MET A  1 733 ? 18.333  51.088 45.327  1.00 15.66 ? 733  MET A N   1 
ATOM   5684  C  CA  . MET A  1 733 ? 18.561  52.457 45.740  1.00 14.02 ? 733  MET A CA  1 
ATOM   5685  C  C   . MET A  1 733 ? 19.323  53.151 44.615  1.00 14.60 ? 733  MET A C   1 
ATOM   5686  O  O   . MET A  1 733 ? 20.382  52.671 44.195  1.00 16.08 ? 733  MET A O   1 
ATOM   5687  C  CB  . MET A  1 733 ? 19.391  52.528 47.027  1.00 15.30 ? 733  MET A CB  1 
ATOM   5688  C  CG  . MET A  1 733 ? 19.628  53.973 47.521  1.00 13.96 ? 733  MET A CG  1 
ATOM   5689  S  SD  . MET A  1 733 ? 18.098  54.941 47.805  1.00 15.92 ? 733  MET A SD  1 
ATOM   5690  C  CE  . MET A  1 733 ? 17.448  54.174 49.267  1.00 16.96 ? 733  MET A CE  1 
ATOM   5691  N  N   . TRP A  1 734 ? 18.773  54.246 44.104  1.00 12.58 ? 734  TRP A N   1 
ATOM   5692  C  CA  . TRP A  1 734 ? 19.466  55.033 43.079  1.00 13.13 ? 734  TRP A CA  1 
ATOM   5693  C  C   . TRP A  1 734 ? 19.942  56.265 43.839  1.00 13.39 ? 734  TRP A C   1 
ATOM   5694  O  O   . TRP A  1 734 ? 19.340  56.619 44.853  1.00 13.70 ? 734  TRP A O   1 
ATOM   5695  C  CB  . TRP A  1 734 ? 18.519  55.464 41.940  1.00 12.25 ? 734  TRP A CB  1 
ATOM   5696  C  CG  . TRP A  1 734 ? 17.505  56.537 42.325  1.00 11.30 ? 734  TRP A CG  1 
ATOM   5697  C  CD1 . TRP A  1 734 ? 17.732  57.887 42.427  1.00 10.83 ? 734  TRP A CD1 1 
ATOM   5698  C  CD2 . TRP A  1 734 ? 16.125  56.336 42.669  1.00 9.81  ? 734  TRP A CD2 1 
ATOM   5699  N  NE1 . TRP A  1 734 ? 16.573  58.537 42.812  1.00 11.52 ? 734  TRP A NE1 1 
ATOM   5700  C  CE2 . TRP A  1 734 ? 15.575  57.611 42.967  1.00 11.48 ? 734  TRP A CE2 1 
ATOM   5701  C  CE3 . TRP A  1 734 ? 15.299  55.202 42.755  1.00 10.67 ? 734  TRP A CE3 1 
ATOM   5702  C  CZ2 . TRP A  1 734 ? 14.227  57.785 43.350  1.00 11.86 ? 734  TRP A CZ2 1 
ATOM   5703  C  CZ3 . TRP A  1 734 ? 13.959  55.365 43.133  1.00 11.47 ? 734  TRP A CZ3 1 
ATOM   5704  C  CH2 . TRP A  1 734 ? 13.435  56.653 43.427  1.00 11.53 ? 734  TRP A CH2 1 
ATOM   5705  N  N   . TYR A  1 735 ? 21.020  56.900 43.387  1.00 12.82 ? 735  TYR A N   1 
ATOM   5706  C  CA  . TYR A  1 735 ? 21.498  58.119 44.036  1.00 13.81 ? 735  TYR A CA  1 
ATOM   5707  C  C   . TYR A  1 735 ? 21.516  59.217 42.989  1.00 13.78 ? 735  TYR A C   1 
ATOM   5708  O  O   . TYR A  1 735 ? 22.371  59.243 42.097  1.00 13.84 ? 735  TYR A O   1 
ATOM   5709  C  CB  . TYR A  1 735 ? 22.900  57.936 44.653  1.00 13.57 ? 735  TYR A CB  1 
ATOM   5710  C  CG  . TYR A  1 735 ? 22.826  57.298 46.021  1.00 13.38 ? 735  TYR A CG  1 
ATOM   5711  C  CD1 . TYR A  1 735 ? 23.054  55.932 46.197  1.00 12.84 ? 735  TYR A CD1 1 
ATOM   5712  C  CD2 . TYR A  1 735 ? 22.396  58.043 47.120  1.00 13.76 ? 735  TYR A CD2 1 
ATOM   5713  C  CE1 . TYR A  1 735 ? 22.841  55.322 47.434  1.00 13.08 ? 735  TYR A CE1 1 
ATOM   5714  C  CE2 . TYR A  1 735 ? 22.178  57.452 48.358  1.00 14.04 ? 735  TYR A CE2 1 
ATOM   5715  C  CZ  . TYR A  1 735 ? 22.397  56.083 48.511  1.00 14.73 ? 735  TYR A CZ  1 
ATOM   5716  O  OH  . TYR A  1 735 ? 22.123  55.481 49.733  1.00 16.15 ? 735  TYR A OH  1 
ATOM   5717  N  N   . THR A  1 736 ? 20.542  60.104 43.102  1.00 12.78 ? 736  THR A N   1 
ATOM   5718  C  CA  . THR A  1 736 ? 20.397  61.208 42.189  1.00 13.80 ? 736  THR A CA  1 
ATOM   5719  C  C   . THR A  1 736 ? 21.669  62.026 42.036  1.00 14.46 ? 736  THR A C   1 
ATOM   5720  O  O   . THR A  1 736 ? 22.211  62.515 43.031  1.00 14.05 ? 736  THR A O   1 
ATOM   5721  C  CB  . THR A  1 736 ? 19.298  62.172 42.672  1.00 13.39 ? 736  THR A CB  1 
ATOM   5722  O  OG1 . THR A  1 736 ? 18.041  61.478 42.713  1.00 13.27 ? 736  THR A OG1 1 
ATOM   5723  C  CG2 . THR A  1 736 ? 19.219  63.406 41.736  1.00 11.04 ? 736  THR A CG2 1 
ATOM   5724  N  N   . ASP A  1 737 ? 22.099  62.183 40.782  1.00 14.83 ? 737  ASP A N   1 
ATOM   5725  C  CA  . ASP A  1 737 ? 23.262  62.985 40.373  1.00 14.36 ? 737  ASP A CA  1 
ATOM   5726  C  C   . ASP A  1 737 ? 24.638  62.572 40.885  1.00 15.01 ? 737  ASP A C   1 
ATOM   5727  O  O   . ASP A  1 737 ? 25.602  63.348 40.763  1.00 13.91 ? 737  ASP A O   1 
ATOM   5728  C  CB  . ASP A  1 737 ? 23.027  64.462 40.719  1.00 14.78 ? 737  ASP A CB  1 
ATOM   5729  C  CG  . ASP A  1 737 ? 21.933  65.117 39.857  1.00 15.57 ? 737  ASP A CG  1 
ATOM   5730  O  OD1 . ASP A  1 737 ? 21.482  64.506 38.864  1.00 15.25 ? 737  ASP A OD1 1 
ATOM   5731  O  OD2 . ASP A  1 737 ? 21.542  66.261 40.170  1.00 15.99 ? 737  ASP A OD2 1 
ATOM   5732  N  N   . GLU A  1 738 ? 24.736  61.373 41.465  1.00 13.75 ? 738  GLU A N   1 
ATOM   5733  C  CA  . GLU A  1 738 ? 26.028  60.868 41.942  1.00 14.67 ? 738  GLU A CA  1 
ATOM   5734  C  C   . GLU A  1 738 ? 26.671  60.092 40.795  1.00 14.78 ? 738  GLU A C   1 
ATOM   5735  O  O   . GLU A  1 738 ? 25.959  59.476 39.984  1.00 14.27 ? 738  GLU A O   1 
ATOM   5736  C  CB  . GLU A  1 738 ? 25.855  59.919 43.141  1.00 13.54 ? 738  GLU A CB  1 
ATOM   5737  C  CG  . GLU A  1 738 ? 25.471  60.584 44.451  1.00 15.34 ? 738  GLU A CG  1 
ATOM   5738  C  CD  . GLU A  1 738 ? 26.480  61.624 44.886  1.00 18.35 ? 738  GLU A CD  1 
ATOM   5739  O  OE1 . GLU A  1 738 ? 27.641  61.252 45.174  1.00 18.18 ? 738  GLU A OE1 1 
ATOM   5740  O  OE2 . GLU A  1 738 ? 26.116  62.821 44.932  1.00 19.90 ? 738  GLU A OE2 1 
ATOM   5741  N  N   . ASP A  1 739 ? 28.005  60.105 40.731  1.00 14.43 ? 739  ASP A N   1 
ATOM   5742  C  CA  . ASP A  1 739 ? 28.709  59.380 39.681  1.00 14.67 ? 739  ASP A CA  1 
ATOM   5743  C  C   . ASP A  1 739 ? 29.255  58.041 40.217  1.00 14.77 ? 739  ASP A C   1 
ATOM   5744  O  O   . ASP A  1 739 ? 28.789  57.544 41.251  1.00 16.05 ? 739  ASP A O   1 
ATOM   5745  C  CB  . ASP A  1 739 ? 29.819  60.262 39.057  1.00 15.57 ? 739  ASP A CB  1 
ATOM   5746  C  CG  . ASP A  1 739 ? 31.001  60.516 40.003  1.00 17.87 ? 739  ASP A CG  1 
ATOM   5747  O  OD1 . ASP A  1 739 ? 31.065  59.929 41.117  1.00 16.15 ? 739  ASP A OD1 1 
ATOM   5748  O  OD2 . ASP A  1 739 ? 31.889  61.312 39.608  1.00 20.31 ? 739  ASP A OD2 1 
ATOM   5749  N  N   . HIS A  1 740 ? 30.224  57.449 39.537  1.00 13.52 ? 740  HIS A N   1 
ATOM   5750  C  CA  . HIS A  1 740 ? 30.753  56.156 39.964  1.00 15.06 ? 740  HIS A CA  1 
ATOM   5751  C  C   . HIS A  1 740 ? 31.307  56.141 41.405  1.00 15.42 ? 740  HIS A C   1 
ATOM   5752  O  O   . HIS A  1 740 ? 31.354  55.094 42.047  1.00 15.72 ? 740  HIS A O   1 
ATOM   5753  C  CB  . HIS A  1 740 ? 31.840  55.695 38.980  1.00 13.86 ? 740  HIS A CB  1 
ATOM   5754  C  CG  . HIS A  1 740 ? 32.055  54.217 38.963  1.00 14.97 ? 740  HIS A CG  1 
ATOM   5755  N  ND1 . HIS A  1 740 ? 31.016  53.323 38.831  1.00 13.61 ? 740  HIS A ND1 1 
ATOM   5756  C  CD2 . HIS A  1 740 ? 33.185  53.473 39.053  1.00 14.39 ? 740  HIS A CD2 1 
ATOM   5757  C  CE1 . HIS A  1 740 ? 31.494  52.090 38.844  1.00 13.81 ? 740  HIS A CE1 1 
ATOM   5758  N  NE2 . HIS A  1 740 ? 32.805  52.152 38.975  1.00 13.62 ? 740  HIS A NE2 1 
ATOM   5759  N  N   . GLY A  1 741 ? 31.715  57.292 41.925  1.00 16.18 ? 741  GLY A N   1 
ATOM   5760  C  CA  . GLY A  1 741 ? 32.258  57.295 43.277  1.00 16.01 ? 741  GLY A CA  1 
ATOM   5761  C  C   . GLY A  1 741 ? 31.232  57.443 44.398  1.00 16.96 ? 741  GLY A C   1 
ATOM   5762  O  O   . GLY A  1 741 ? 31.556  57.145 45.547  1.00 17.59 ? 741  GLY A O   1 
ATOM   5763  N  N   . ILE A  1 742 ? 30.009  57.867 44.073  1.00 15.14 ? 742  ILE A N   1 
ATOM   5764  C  CA  . ILE A  1 742 ? 28.957  58.114 45.075  1.00 16.15 ? 742  ILE A CA  1 
ATOM   5765  C  C   . ILE A  1 742 ? 29.686  58.648 46.294  1.00 17.49 ? 742  ILE A C   1 
ATOM   5766  O  O   . ILE A  1 742 ? 29.526  58.155 47.415  1.00 18.02 ? 742  ILE A O   1 
ATOM   5767  C  CB  . ILE A  1 742 ? 28.174  56.833 45.445  1.00 14.95 ? 742  ILE A CB  1 
ATOM   5768  C  CG1 . ILE A  1 742 ? 27.782  56.070 44.164  1.00 14.81 ? 742  ILE A CG1 1 
ATOM   5769  C  CG2 . ILE A  1 742 ? 26.915  57.222 46.209  1.00 13.37 ? 742  ILE A CG2 1 
ATOM   5770  C  CD1 . ILE A  1 742 ? 26.784  54.937 44.373  1.00 13.56 ? 742  ILE A CD1 1 
ATOM   5771  N  N   . ALA A  1 743 ? 30.481  59.684 46.038  1.00 17.89 ? 743  ALA A N   1 
ATOM   5772  C  CA  . ALA A  1 743 ? 31.358  60.292 47.023  1.00 18.43 ? 743  ALA A CA  1 
ATOM   5773  C  C   . ALA A  1 743 ? 30.976  61.632 47.626  1.00 19.00 ? 743  ALA A C   1 
ATOM   5774  O  O   . ALA A  1 743 ? 31.695  62.114 48.491  1.00 18.76 ? 743  ALA A O   1 
ATOM   5775  C  CB  . ALA A  1 743 ? 32.786  60.380 46.433  1.00 19.28 ? 743  ALA A CB  1 
ATOM   5776  N  N   . SER A  1 744 ? 29.883  62.260 47.198  1.00 19.23 ? 744  SER A N   1 
ATOM   5777  C  CA  . SER A  1 744 ? 29.551  63.509 47.856  1.00 19.84 ? 744  SER A CA  1 
ATOM   5778  C  C   . SER A  1 744 ? 29.376  63.121 49.340  1.00 20.58 ? 744  SER A C   1 
ATOM   5779  O  O   . SER A  1 744 ? 29.002  61.989 49.668  1.00 20.24 ? 744  SER A O   1 
ATOM   5780  C  CB  . SER A  1 744 ? 28.255  64.114 47.302  1.00 20.85 ? 744  SER A CB  1 
ATOM   5781  O  OG  . SER A  1 744 ? 27.118  63.404 47.753  1.00 23.29 ? 744  SER A OG  1 
ATOM   5782  N  N   . SER A  1 745 ? 29.677  64.050 50.233  1.00 20.61 ? 745  SER A N   1 
ATOM   5783  C  CA  . SER A  1 745 ? 29.556  63.801 51.663  1.00 21.02 ? 745  SER A CA  1 
ATOM   5784  C  C   . SER A  1 745 ? 28.214  63.168 52.090  1.00 19.98 ? 745  SER A C   1 
ATOM   5785  O  O   . SER A  1 745 ? 28.187  62.152 52.798  1.00 19.58 ? 745  SER A O   1 
ATOM   5786  C  CB  . SER A  1 745 ? 29.772  65.115 52.412  1.00 22.37 ? 745  SER A CB  1 
ATOM   5787  O  OG  . SER A  1 745 ? 29.473  64.982 53.782  1.00 26.04 ? 745  SER A OG  1 
ATOM   5788  N  N   . THR A  1 746 ? 27.099  63.748 51.659  1.00 18.46 ? 746  THR A N   1 
ATOM   5789  C  CA  . THR A  1 746 ? 25.803  63.207 52.056  1.00 18.11 ? 746  THR A CA  1 
ATOM   5790  C  C   . THR A  1 746 ? 25.483  61.832 51.440  1.00 17.13 ? 746  THR A C   1 
ATOM   5791  O  O   . THR A  1 746 ? 24.999  60.947 52.136  1.00 17.34 ? 746  THR A O   1 
ATOM   5792  C  CB  . THR A  1 746 ? 24.698  64.229 51.760  1.00 18.37 ? 746  THR A CB  1 
ATOM   5793  O  OG1 . THR A  1 746 ? 24.780  64.654 50.393  1.00 19.92 ? 746  THR A OG1 1 
ATOM   5794  C  CG2 . THR A  1 746 ? 24.889  65.455 52.672  1.00 18.30 ? 746  THR A CG2 1 
ATOM   5795  N  N   . ALA A  1 747 ? 25.774  61.636 50.159  1.00 16.87 ? 747  ALA A N   1 
ATOM   5796  C  CA  . ALA A  1 747 ? 25.508  60.336 49.520  1.00 17.19 ? 747  ALA A CA  1 
ATOM   5797  C  C   . ALA A  1 747 ? 26.375  59.240 50.153  1.00 16.29 ? 747  ALA A C   1 
ATOM   5798  O  O   . ALA A  1 747 ? 25.903  58.137 50.418  1.00 17.08 ? 747  ALA A O   1 
ATOM   5799  C  CB  . ALA A  1 747 ? 25.773  60.418 48.026  1.00 15.68 ? 747  ALA A CB  1 
ATOM   5800  N  N   . HIS A  1 748 ? 27.642  59.553 50.398  1.00 16.43 ? 748  HIS A N   1 
ATOM   5801  C  CA  . HIS A  1 748 ? 28.571  58.599 51.013  1.00 15.49 ? 748  HIS A CA  1 
ATOM   5802  C  C   . HIS A  1 748 ? 28.001  58.072 52.326  1.00 16.40 ? 748  HIS A C   1 
ATOM   5803  O  O   . HIS A  1 748 ? 27.918  56.860 52.546  1.00 15.63 ? 748  HIS A O   1 
ATOM   5804  C  CB  . HIS A  1 748 ? 29.908  59.275 51.288  1.00 16.75 ? 748  HIS A CB  1 
ATOM   5805  C  CG  . HIS A  1 748 ? 30.881  58.419 52.040  1.00 16.93 ? 748  HIS A CG  1 
ATOM   5806  N  ND1 . HIS A  1 748 ? 31.408  57.257 51.520  1.00 15.74 ? 748  HIS A ND1 1 
ATOM   5807  C  CD2 . HIS A  1 748 ? 31.444  58.574 53.264  1.00 15.93 ? 748  HIS A CD2 1 
ATOM   5808  C  CE1 . HIS A  1 748 ? 32.257  56.734 52.388  1.00 17.09 ? 748  HIS A CE1 1 
ATOM   5809  N  NE2 . HIS A  1 748 ? 32.296  57.511 53.456  1.00 15.64 ? 748  HIS A NE2 1 
ATOM   5810  N  N   . GLN A  1 749 ? 27.620  58.987 53.207  1.00 16.23 ? 749  GLN A N   1 
ATOM   5811  C  CA  . GLN A  1 749 ? 27.049  58.598 54.481  1.00 16.50 ? 749  GLN A CA  1 
ATOM   5812  C  C   . GLN A  1 749 ? 25.748  57.823 54.296  1.00 16.15 ? 749  GLN A C   1 
ATOM   5813  O  O   . GLN A  1 749 ? 25.505  56.827 54.978  1.00 15.05 ? 749  GLN A O   1 
ATOM   5814  C  CB  . GLN A  1 749 ? 26.817  59.845 55.325  1.00 18.19 ? 749  GLN A CB  1 
ATOM   5815  C  CG  . GLN A  1 749 ? 28.134  60.550 55.634  1.00 21.09 ? 749  GLN A CG  1 
ATOM   5816  C  CD  . GLN A  1 749 ? 27.942  61.810 56.441  1.00 23.28 ? 749  GLN A CD  1 
ATOM   5817  O  OE1 . GLN A  1 749 ? 27.370  61.781 57.522  1.00 25.80 ? 749  GLN A OE1 1 
ATOM   5818  N  NE2 . GLN A  1 749 ? 28.423  62.924 55.921  1.00 24.96 ? 749  GLN A NE2 1 
ATOM   5819  N  N   . HIS A  1 750 ? 24.912  58.280 53.372  1.00 15.65 ? 750  HIS A N   1 
ATOM   5820  C  CA  . HIS A  1 750 ? 23.634  57.611 53.125  1.00 15.65 ? 750  HIS A CA  1 
ATOM   5821  C  C   . HIS A  1 750 ? 23.773  56.172 52.625  1.00 15.54 ? 750  HIS A C   1 
ATOM   5822  O  O   . HIS A  1 750 ? 23.078  55.268 53.107  1.00 14.07 ? 750  HIS A O   1 
ATOM   5823  C  CB  . HIS A  1 750 ? 22.808  58.414 52.121  1.00 14.90 ? 750  HIS A CB  1 
ATOM   5824  C  CG  . HIS A  1 750 ? 21.355  58.066 52.128  1.00 15.58 ? 750  HIS A CG  1 
ATOM   5825  N  ND1 . HIS A  1 750 ? 20.841  57.003 51.417  1.00 14.31 ? 750  HIS A ND1 1 
ATOM   5826  C  CD2 . HIS A  1 750 ? 20.310  58.625 52.784  1.00 15.48 ? 750  HIS A CD2 1 
ATOM   5827  C  CE1 . HIS A  1 750 ? 19.542  56.922 51.632  1.00 15.05 ? 750  HIS A CE1 1 
ATOM   5828  N  NE2 . HIS A  1 750 ? 19.192  57.894 52.457  1.00 17.15 ? 750  HIS A NE2 1 
ATOM   5829  N  N   . ILE A  1 751 ? 24.674  55.948 51.675  1.00 14.32 ? 751  ILE A N   1 
ATOM   5830  C  CA  . ILE A  1 751 ? 24.826  54.607 51.137  1.00 14.12 ? 751  ILE A CA  1 
ATOM   5831  C  C   . ILE A  1 751 ? 25.349  53.625 52.172  1.00 14.86 ? 751  ILE A C   1 
ATOM   5832  O  O   . ILE A  1 751 ? 24.811  52.519 52.301  1.00 12.31 ? 751  ILE A O   1 
ATOM   5833  C  CB  . ILE A  1 751 ? 25.726  54.582 49.828  1.00 14.00 ? 751  ILE A CB  1 
ATOM   5834  C  CG1 . ILE A  1 751 ? 25.663  53.196 49.186  1.00 13.12 ? 751  ILE A CG1 1 
ATOM   5835  C  CG2 . ILE A  1 751 ? 27.171  55.000 50.140  1.00 13.33 ? 751  ILE A CG2 1 
ATOM   5836  C  CD1 . ILE A  1 751 ? 26.392  53.106 47.788  1.00 10.87 ? 751  ILE A CD1 1 
ATOM   5837  N  N   . TYR A  1 752 ? 26.376  54.020 52.927  1.00 13.87 ? 752  TYR A N   1 
ATOM   5838  C  CA  . TYR A  1 752 ? 26.913  53.107 53.932  1.00 14.72 ? 752  TYR A CA  1 
ATOM   5839  C  C   . TYR A  1 752 ? 25.915  52.857 55.072  1.00 14.38 ? 752  TYR A C   1 
ATOM   5840  O  O   . TYR A  1 752 ? 25.895  51.784 55.667  1.00 14.98 ? 752  TYR A O   1 
ATOM   5841  C  CB  . TYR A  1 752 ? 28.266  53.612 54.445  1.00 12.48 ? 752  TYR A CB  1 
ATOM   5842  C  CG  . TYR A  1 752 ? 29.373  53.231 53.482  1.00 13.29 ? 752  TYR A CG  1 
ATOM   5843  C  CD1 . TYR A  1 752 ? 29.822  51.916 53.407  1.00 11.93 ? 752  TYR A CD1 1 
ATOM   5844  C  CD2 . TYR A  1 752 ? 29.915  54.166 52.593  1.00 12.69 ? 752  TYR A CD2 1 
ATOM   5845  C  CE1 . TYR A  1 752 ? 30.786  51.531 52.473  1.00 14.31 ? 752  TYR A CE1 1 
ATOM   5846  C  CE2 . TYR A  1 752 ? 30.879  53.790 51.657  1.00 13.72 ? 752  TYR A CE2 1 
ATOM   5847  C  CZ  . TYR A  1 752 ? 31.306  52.473 51.605  1.00 12.25 ? 752  TYR A CZ  1 
ATOM   5848  O  OH  . TYR A  1 752 ? 32.225  52.086 50.664  1.00 15.20 ? 752  TYR A OH  1 
ATOM   5849  N  N   . THR A  1 753 ? 25.074  53.839 55.347  1.00 14.74 ? 753  THR A N   1 
ATOM   5850  C  CA  . THR A  1 753 ? 24.050  53.680 56.370  1.00 15.35 ? 753  THR A CA  1 
ATOM   5851  C  C   . THR A  1 753 ? 23.020  52.678 55.842  1.00 15.43 ? 753  THR A C   1 
ATOM   5852  O  O   . THR A  1 753 ? 22.654  51.725 56.544  1.00 17.04 ? 753  THR A O   1 
ATOM   5853  C  CB  . THR A  1 753 ? 23.377  55.035 56.688  1.00 14.57 ? 753  THR A CB  1 
ATOM   5854  O  OG1 . THR A  1 753 ? 24.358  55.907 57.252  1.00 16.82 ? 753  THR A OG1 1 
ATOM   5855  C  CG2 . THR A  1 753 ? 22.216  54.877 57.686  1.00 14.52 ? 753  THR A CG2 1 
ATOM   5856  N  N   . HIS A  1 754 ? 22.599  52.856 54.587  1.00 14.67 ? 754  HIS A N   1 
ATOM   5857  C  CA  . HIS A  1 754 ? 21.612  51.969 53.972  1.00 13.41 ? 754  HIS A CA  1 
ATOM   5858  C  C   . HIS A  1 754 ? 22.158  50.544 53.843  1.00 14.67 ? 754  HIS A C   1 
ATOM   5859  O  O   . HIS A  1 754 ? 21.449  49.563 54.126  1.00 13.69 ? 754  HIS A O   1 
ATOM   5860  C  CB  . HIS A  1 754 ? 21.194  52.501 52.590  1.00 13.18 ? 754  HIS A CB  1 
ATOM   5861  C  CG  . HIS A  1 754 ? 19.911  51.924 52.083  1.00 14.61 ? 754  HIS A CG  1 
ATOM   5862  N  ND1 . HIS A  1 754 ? 18.688  52.213 52.651  1.00 15.43 ? 754  HIS A ND1 1 
ATOM   5863  C  CD2 . HIS A  1 754 ? 19.660  51.059 51.070  1.00 15.33 ? 754  HIS A CD2 1 
ATOM   5864  C  CE1 . HIS A  1 754 ? 17.740  51.550 52.009  1.00 16.30 ? 754  HIS A CE1 1 
ATOM   5865  N  NE2 . HIS A  1 754 ? 18.304  50.842 51.046  1.00 15.14 ? 754  HIS A NE2 1 
ATOM   5866  N  N   . MET A  1 755 ? 23.415  50.409 53.419  1.00 14.45 ? 755  MET A N   1 
ATOM   5867  C  CA  . MET A  1 755 ? 23.992  49.070 53.301  1.00 15.13 ? 755  MET A CA  1 
ATOM   5868  C  C   . MET A  1 755 ? 24.158  48.391 54.679  1.00 15.90 ? 755  MET A C   1 
ATOM   5869  O  O   . MET A  1 755 ? 23.995  47.179 54.792  1.00 16.38 ? 755  MET A O   1 
ATOM   5870  C  CB  . MET A  1 755 ? 25.354  49.115 52.595  1.00 15.15 ? 755  MET A CB  1 
ATOM   5871  C  CG  . MET A  1 755 ? 25.279  49.573 51.135  1.00 14.12 ? 755  MET A CG  1 
ATOM   5872  S  SD  . MET A  1 755 ? 26.821  49.247 50.224  1.00 18.09 ? 755  MET A SD  1 
ATOM   5873  C  CE  . MET A  1 755 ? 27.889  50.372 51.076  1.00 16.76 ? 755  MET A CE  1 
ATOM   5874  N  N   . SER A  1 756 ? 24.509  49.170 55.703  1.00 16.22 ? 756  SER A N   1 
ATOM   5875  C  CA  . SER A  1 756 ? 24.673  48.638 57.052  1.00 16.76 ? 756  SER A CA  1 
ATOM   5876  C  C   . SER A  1 756 ? 23.349  48.059 57.572  1.00 15.96 ? 756  SER A C   1 
ATOM   5877  O  O   . SER A  1 756 ? 23.349  46.997 58.186  1.00 15.13 ? 756  SER A O   1 
ATOM   5878  C  CB  . SER A  1 756 ? 25.184  49.719 58.004  1.00 16.67 ? 756  SER A CB  1 
ATOM   5879  O  OG  . SER A  1 756 ? 26.461  50.189 57.592  1.00 17.95 ? 756  SER A OG  1 
ATOM   5880  N  N   . HIS A  1 757 ? 22.229  48.744 57.327  1.00 16.57 ? 757  HIS A N   1 
ATOM   5881  C  CA  . HIS A  1 757 ? 20.922  48.227 57.759  1.00 17.89 ? 757  HIS A CA  1 
ATOM   5882  C  C   . HIS A  1 757 ? 20.638  46.925 57.001  1.00 17.83 ? 757  HIS A C   1 
ATOM   5883  O  O   . HIS A  1 757 ? 20.099  45.970 57.556  1.00 17.79 ? 757  HIS A O   1 
ATOM   5884  C  CB  . HIS A  1 757 ? 19.766  49.203 57.447  1.00 18.51 ? 757  HIS A CB  1 
ATOM   5885  C  CG  . HIS A  1 757 ? 19.764  50.455 58.269  1.00 20.72 ? 757  HIS A CG  1 
ATOM   5886  N  ND1 . HIS A  1 757 ? 19.877  50.447 59.642  1.00 22.93 ? 757  HIS A ND1 1 
ATOM   5887  C  CD2 . HIS A  1 757 ? 19.642  51.756 57.910  1.00 20.56 ? 757  HIS A CD2 1 
ATOM   5888  C  CE1 . HIS A  1 757 ? 19.831  51.688 60.093  1.00 23.20 ? 757  HIS A CE1 1 
ATOM   5889  N  NE2 . HIS A  1 757 ? 19.689  52.503 59.062  1.00 22.51 ? 757  HIS A NE2 1 
ATOM   5890  N  N   . PHE A  1 758 ? 21.014  46.881 55.729  1.00 17.35 ? 758  PHE A N   1 
ATOM   5891  C  CA  . PHE A  1 758 ? 20.745  45.696 54.916  1.00 17.40 ? 758  PHE A CA  1 
ATOM   5892  C  C   . PHE A  1 758 ? 21.543  44.486 55.411  1.00 18.05 ? 758  PHE A C   1 
ATOM   5893  O  O   . PHE A  1 758 ? 20.997  43.386 55.563  1.00 16.58 ? 758  PHE A O   1 
ATOM   5894  C  CB  . PHE A  1 758 ? 21.059  45.966 53.436  1.00 17.25 ? 758  PHE A CB  1 
ATOM   5895  C  CG  . PHE A  1 758 ? 20.776  44.796 52.546  1.00 16.36 ? 758  PHE A CG  1 
ATOM   5896  C  CD1 . PHE A  1 758 ? 19.484  44.529 52.112  1.00 17.37 ? 758  PHE A CD1 1 
ATOM   5897  C  CD2 . PHE A  1 758 ? 21.793  43.918 52.198  1.00 16.57 ? 758  PHE A CD2 1 
ATOM   5898  C  CE1 . PHE A  1 758 ? 19.209  43.388 51.340  1.00 17.35 ? 758  PHE A CE1 1 
ATOM   5899  C  CE2 . PHE A  1 758 ? 21.534  42.782 51.433  1.00 16.82 ? 758  PHE A CE2 1 
ATOM   5900  C  CZ  . PHE A  1 758 ? 20.238  42.520 51.007  1.00 18.00 ? 758  PHE A CZ  1 
ATOM   5901  N  N   . ILE A  1 759 ? 22.825  44.684 55.678  1.00 17.41 ? 759  ILE A N   1 
ATOM   5902  C  CA  . ILE A  1 759 ? 23.649  43.587 56.170  1.00 18.81 ? 759  ILE A CA  1 
ATOM   5903  C  C   . ILE A  1 759 ? 23.178  43.103 57.562  1.00 19.13 ? 759  ILE A C   1 
ATOM   5904  O  O   . ILE A  1 759 ? 23.007  41.914 57.768  1.00 19.77 ? 759  ILE A O   1 
ATOM   5905  C  CB  . ILE A  1 759 ? 25.136  43.988 56.254  1.00 17.95 ? 759  ILE A CB  1 
ATOM   5906  C  CG1 . ILE A  1 759 ? 25.697  44.190 54.849  1.00 18.93 ? 759  ILE A CG1 1 
ATOM   5907  C  CG2 . ILE A  1 759 ? 25.936  42.891 56.950  1.00 18.97 ? 759  ILE A CG2 1 
ATOM   5908  C  CD1 . ILE A  1 759 ? 25.822  42.903 54.036  1.00 17.43 ? 759  ILE A CD1 1 
ATOM   5909  N  N   . LYS A  1 760 ? 22.972  44.010 58.509  1.00 20.66 ? 760  LYS A N   1 
ATOM   5910  C  CA  . LYS A  1 760 ? 22.527  43.603 59.845  1.00 21.81 ? 760  LYS A CA  1 
ATOM   5911  C  C   . LYS A  1 760 ? 21.219  42.819 59.756  1.00 22.48 ? 760  LYS A C   1 
ATOM   5912  O  O   . LYS A  1 760 ? 21.065  41.773 60.376  1.00 20.95 ? 760  LYS A O   1 
ATOM   5913  C  CB  . LYS A  1 760 ? 22.365  44.826 60.751  1.00 22.48 ? 760  LYS A CB  1 
ATOM   5914  C  CG  . LYS A  1 760 ? 23.716  45.531 61.011  1.00 25.22 ? 760  LYS A CG  1 
ATOM   5915  C  CD  . LYS A  1 760 ? 23.603  46.726 61.952  1.00 26.66 ? 760  LYS A CD  1 
ATOM   5916  C  CE  . LYS A  1 760 ? 23.131  46.307 63.335  1.00 28.23 ? 760  LYS A CE  1 
ATOM   5917  N  NZ  . LYS A  1 760 ? 23.359  47.360 64.367  1.00 31.28 ? 760  LYS A NZ  1 
ATOM   5918  N  N   . GLN A  1 761 ? 20.283  43.328 58.965  1.00 23.06 ? 761  GLN A N   1 
ATOM   5919  C  CA  . GLN A  1 761 ? 18.996  42.674 58.757  1.00 24.30 ? 761  GLN A CA  1 
ATOM   5920  C  C   . GLN A  1 761 ? 19.239  41.251 58.199  1.00 24.16 ? 761  GLN A C   1 
ATOM   5921  O  O   . GLN A  1 761 ? 18.664  40.275 58.689  1.00 25.04 ? 761  GLN A O   1 
ATOM   5922  C  CB  . GLN A  1 761 ? 18.158  43.554 57.807  1.00 25.56 ? 761  GLN A CB  1 
ATOM   5923  C  CG  . GLN A  1 761 ? 17.018  42.888 57.079  1.00 29.85 ? 761  GLN A CG  1 
ATOM   5924  C  CD  . GLN A  1 761 ? 17.487  41.944 55.985  1.00 31.78 ? 761  GLN A CD  1 
ATOM   5925  O  OE1 . GLN A  1 761 ? 18.149  42.353 55.015  1.00 32.67 ? 761  GLN A OE1 1 
ATOM   5926  N  NE2 . GLN A  1 761 ? 17.148  40.664 56.137  1.00 33.07 ? 761  GLN A NE2 1 
ATOM   5927  N  N   . CYS A  1 762 ? 20.099  41.124 57.194  1.00 22.50 ? 762  CYS A N   1 
ATOM   5928  C  CA  . CYS A  1 762 ? 20.405  39.817 56.620  1.00 23.62 ? 762  CYS A CA  1 
ATOM   5929  C  C   . CYS A  1 762 ? 21.030  38.865 57.636  1.00 23.40 ? 762  CYS A C   1 
ATOM   5930  O  O   . CYS A  1 762 ? 20.773  37.667 57.587  1.00 22.93 ? 762  CYS A O   1 
ATOM   5931  C  CB  . CYS A  1 762 ? 21.359  39.958 55.429  1.00 23.67 ? 762  CYS A CB  1 
ATOM   5932  S  SG  . CYS A  1 762 ? 22.015  38.375 54.793  1.00 24.37 ? 762  CYS A SG  1 
ATOM   5933  N  N   . PHE A  1 763 ? 21.851  39.400 58.548  1.00 23.66 ? 763  PHE A N   1 
ATOM   5934  C  CA  . PHE A  1 763 ? 22.525  38.592 59.583  1.00 24.67 ? 763  PHE A CA  1 
ATOM   5935  C  C   . PHE A  1 763 ? 21.755  38.506 60.919  1.00 25.98 ? 763  PHE A C   1 
ATOM   5936  O  O   . PHE A  1 763 ? 22.244  37.905 61.881  1.00 25.01 ? 763  PHE A O   1 
ATOM   5937  C  CB  . PHE A  1 763 ? 23.930  39.153 59.871  1.00 21.55 ? 763  PHE A CB  1 
ATOM   5938  C  CG  . PHE A  1 763 ? 24.927  38.948 58.745  1.00 21.29 ? 763  PHE A CG  1 
ATOM   5939  C  CD1 . PHE A  1 763 ? 24.719  37.972 57.765  1.00 19.01 ? 763  PHE A CD1 1 
ATOM   5940  C  CD2 . PHE A  1 763 ? 26.114  39.688 58.710  1.00 20.38 ? 763  PHE A CD2 1 
ATOM   5941  C  CE1 . PHE A  1 763 ? 25.683  37.736 56.776  1.00 19.35 ? 763  PHE A CE1 1 
ATOM   5942  C  CE2 . PHE A  1 763 ? 27.077  39.459 57.733  1.00 18.92 ? 763  PHE A CE2 1 
ATOM   5943  C  CZ  . PHE A  1 763 ? 26.864  38.478 56.762  1.00 18.83 ? 763  PHE A CZ  1 
ATOM   5944  N  N   . SER A  1 764 ? 20.567  39.108 60.976  1.00 28.32 ? 764  SER A N   1 
ATOM   5945  C  CA  . SER A  1 764 ? 19.750  39.118 62.192  1.00 32.01 ? 764  SER A CA  1 
ATOM   5946  C  C   . SER A  1 764 ? 20.502  39.791 63.329  1.00 35.37 ? 764  SER A C   1 
ATOM   5947  O  O   . SER A  1 764 ? 20.509  39.292 64.468  1.00 36.54 ? 764  SER A O   1 
ATOM   5948  C  CB  . SER A  1 764 ? 19.382  37.698 62.641  1.00 31.50 ? 764  SER A CB  1 
ATOM   5949  O  OG  . SER A  1 764 ? 18.632  37.030 61.657  1.00 31.26 ? 764  SER A OG  1 
ATOM   5950  N  N   . LEU A  1 765 ? 21.151  40.912 63.022  1.00 37.33 ? 765  LEU A N   1 
ATOM   5951  C  CA  . LEU A  1 765 ? 21.900  41.643 64.031  1.00 39.56 ? 765  LEU A CA  1 
ATOM   5952  C  C   . LEU A  1 765 ? 21.093  42.838 64.526  1.00 41.14 ? 765  LEU A C   1 
ATOM   5953  O  O   . LEU A  1 765 ? 20.692  43.704 63.740  1.00 41.22 ? 765  LEU A O   1 
ATOM   5954  C  CB  . LEU A  1 765 ? 23.242  42.111 63.462  1.00 39.18 ? 765  LEU A CB  1 
ATOM   5955  C  CG  . LEU A  1 765 ? 24.109  40.975 62.919  1.00 39.22 ? 765  LEU A CG  1 
ATOM   5956  C  CD1 . LEU A  1 765 ? 25.467  41.544 62.510  1.00 38.16 ? 765  LEU A CD1 1 
ATOM   5957  C  CD2 . LEU A  1 765 ? 24.267  39.867 63.981  1.00 37.76 ? 765  LEU A CD2 1 
ATOM   5958  N  N   . PRO A  1 766 ? 20.843  42.896 65.844  1.00 42.70 ? 766  PRO A N   1 
ATOM   5959  C  CA  . PRO A  1 766 ? 20.076  43.995 66.442  1.00 43.44 ? 766  PRO A CA  1 
ATOM   5960  C  C   . PRO A  1 766 ? 20.641  45.353 66.039  1.00 43.88 ? 766  PRO A C   1 
ATOM   5961  O  O   . PRO A  1 766 ? 19.822  46.248 65.722  1.00 44.46 ? 766  PRO A O   1 
ATOM   5962  C  CB  . PRO A  1 766 ? 20.197  43.728 67.943  1.00 44.13 ? 766  PRO A CB  1 
ATOM   5963  C  CG  . PRO A  1 766 ? 20.310  42.200 67.995  1.00 44.16 ? 766  PRO A CG  1 
ATOM   5964  C  CD  . PRO A  1 766 ? 21.293  41.940 66.874  1.00 43.03 ? 766  PRO A CD  1 
ATOM   5965  O  OXT . PRO A  1 766 ? 21.890  45.496 66.049  1.00 43.69 ? 766  PRO A OXT 1 
ATOM   5966  N  N   . THR B  1 39  ? -12.422 25.438 56.327  1.00 42.09 ? 39   THR B N   1 
ATOM   5967  C  CA  . THR B  1 39  ? -12.364 26.946 56.380  1.00 42.29 ? 39   THR B CA  1 
ATOM   5968  C  C   . THR B  1 39  ? -12.166 27.514 54.971  1.00 41.60 ? 39   THR B C   1 
ATOM   5969  O  O   . THR B  1 39  ? -11.301 27.057 54.226  1.00 42.35 ? 39   THR B O   1 
ATOM   5970  C  CB  . THR B  1 39  ? -11.191 27.426 57.272  1.00 42.49 ? 39   THR B CB  1 
ATOM   5971  O  OG1 . THR B  1 39  ? -11.158 26.656 58.486  1.00 43.93 ? 39   THR B OG1 1 
ATOM   5972  C  CG2 . THR B  1 39  ? -11.362 28.903 57.619  1.00 41.51 ? 39   THR B CG2 1 
ATOM   5973  N  N   . ARG B  1 40  ? -12.966 28.500 54.593  1.00 40.57 ? 40   ARG B N   1 
ATOM   5974  C  CA  . ARG B  1 40  ? -12.830 29.087 53.265  1.00 39.11 ? 40   ARG B CA  1 
ATOM   5975  C  C   . ARG B  1 40  ? -11.516 29.854 53.115  1.00 37.88 ? 40   ARG B C   1 
ATOM   5976  O  O   . ARG B  1 40  ? -11.030 30.497 54.060  1.00 36.50 ? 40   ARG B O   1 
ATOM   5977  C  CB  . ARG B  1 40  ? -13.990 30.045 52.982  1.00 39.81 ? 40   ARG B CB  1 
ATOM   5978  C  CG  . ARG B  1 40  ? -15.368 29.424 53.088  1.00 39.97 ? 40   ARG B CG  1 
ATOM   5979  C  CD  . ARG B  1 40  ? -16.433 30.426 52.695  1.00 39.81 ? 40   ARG B CD  1 
ATOM   5980  N  NE  . ARG B  1 40  ? -16.491 31.552 53.615  1.00 41.05 ? 40   ARG B NE  1 
ATOM   5981  C  CZ  . ARG B  1 40  ? -17.167 32.679 53.383  1.00 41.89 ? 40   ARG B CZ  1 
ATOM   5982  N  NH1 . ARG B  1 40  ? -17.845 32.825 52.249  1.00 41.43 ? 40   ARG B NH1 1 
ATOM   5983  N  NH2 . ARG B  1 40  ? -17.151 33.670 54.278  1.00 41.92 ? 40   ARG B NH2 1 
ATOM   5984  N  N   . LYS B  1 41  ? -10.940 29.785 51.921  1.00 36.77 ? 41   LYS B N   1 
ATOM   5985  C  CA  . LYS B  1 41  ? -9.705  30.508 51.653  1.00 35.77 ? 41   LYS B CA  1 
ATOM   5986  C  C   . LYS B  1 41  ? -10.034 31.998 51.578  1.00 33.73 ? 41   LYS B C   1 
ATOM   5987  O  O   . LYS B  1 41  ? -11.207 32.389 51.549  1.00 33.02 ? 41   LYS B O   1 
ATOM   5988  C  CB  . LYS B  1 41  ? -9.085  30.032 50.340  1.00 37.45 ? 41   LYS B CB  1 
ATOM   5989  C  CG  . LYS B  1 41  ? -9.976  30.189 49.125  1.00 39.87 ? 41   LYS B CG  1 
ATOM   5990  C  CD  . LYS B  1 41  ? -9.408  29.420 47.916  1.00 42.01 ? 41   LYS B CD  1 
ATOM   5991  C  CE  . LYS B  1 41  ? -9.389  27.893 48.163  1.00 43.71 ? 41   LYS B CE  1 
ATOM   5992  N  NZ  . LYS B  1 41  ? -8.858  27.083 47.001  1.00 44.49 ? 41   LYS B NZ  1 
ATOM   5993  N  N   . THR B  1 42  ? -9.000  32.829 51.595  1.00 31.61 ? 42   THR B N   1 
ATOM   5994  C  CA  . THR B  1 42  ? -9.199  34.265 51.517  1.00 30.25 ? 42   THR B CA  1 
ATOM   5995  C  C   . THR B  1 42  ? -8.792  34.752 50.130  1.00 29.01 ? 42   THR B C   1 
ATOM   5996  O  O   . THR B  1 42  ? -8.371  33.956 49.289  1.00 28.23 ? 42   THR B O   1 
ATOM   5997  C  CB  . THR B  1 42  ? -8.356  34.993 52.571  1.00 30.17 ? 42   THR B CB  1 
ATOM   5998  O  OG1 . THR B  1 42  ? -6.978  34.651 52.394  1.00 29.12 ? 42   THR B OG1 1 
ATOM   5999  C  CG2 . THR B  1 42  ? -8.796  34.593 53.969  1.00 30.39 ? 42   THR B CG2 1 
ATOM   6000  N  N   . TYR B  1 43  ? -8.943  36.049 49.877  1.00 27.92 ? 43   TYR B N   1 
ATOM   6001  C  CA  . TYR B  1 43  ? -8.545  36.628 48.582  1.00 26.91 ? 43   TYR B CA  1 
ATOM   6002  C  C   . TYR B  1 43  ? -7.063  36.983 48.758  1.00 26.66 ? 43   TYR B C   1 
ATOM   6003  O  O   . TYR B  1 43  ? -6.728  37.913 49.473  1.00 25.59 ? 43   TYR B O   1 
ATOM   6004  C  CB  . TYR B  1 43  ? -9.343  37.898 48.295  1.00 26.42 ? 43   TYR B CB  1 
ATOM   6005  C  CG  . TYR B  1 43  ? -9.099  38.488 46.920  1.00 25.92 ? 43   TYR B CG  1 
ATOM   6006  C  CD1 . TYR B  1 43  ? -9.757  37.986 45.804  1.00 24.89 ? 43   TYR B CD1 1 
ATOM   6007  C  CD2 . TYR B  1 43  ? -8.222  39.561 46.741  1.00 25.24 ? 43   TYR B CD2 1 
ATOM   6008  C  CE1 . TYR B  1 43  ? -9.559  38.540 44.536  1.00 25.74 ? 43   TYR B CE1 1 
ATOM   6009  C  CE2 . TYR B  1 43  ? -8.012  40.126 45.475  1.00 25.48 ? 43   TYR B CE2 1 
ATOM   6010  C  CZ  . TYR B  1 43  ? -8.686  39.614 44.375  1.00 25.93 ? 43   TYR B CZ  1 
ATOM   6011  O  OH  . TYR B  1 43  ? -8.510  40.169 43.122  1.00 23.17 ? 43   TYR B OH  1 
ATOM   6012  N  N   . THR B  1 44  ? -6.194  36.233 48.096  1.00 26.63 ? 44   THR B N   1 
ATOM   6013  C  CA  . THR B  1 44  ? -4.753  36.402 48.223  1.00 26.73 ? 44   THR B CA  1 
ATOM   6014  C  C   . THR B  1 44  ? -4.120  37.327 47.195  1.00 26.51 ? 44   THR B C   1 
ATOM   6015  O  O   . THR B  1 44  ? -4.727  37.666 46.186  1.00 26.39 ? 44   THR B O   1 
ATOM   6016  C  CB  . THR B  1 44  ? -4.067  35.049 48.092  1.00 27.05 ? 44   THR B CB  1 
ATOM   6017  O  OG1 . THR B  1 44  ? -4.267  34.559 46.759  1.00 26.52 ? 44   THR B OG1 1 
ATOM   6018  C  CG2 . THR B  1 44  ? -4.661  34.051 49.087  1.00 27.07 ? 44   THR B CG2 1 
ATOM   6019  N  N   . LEU B  1 45  ? -2.872  37.703 47.450  1.00 26.31 ? 45   LEU B N   1 
ATOM   6020  C  CA  . LEU B  1 45  ? -2.142  38.574 46.539  1.00 25.03 ? 45   LEU B CA  1 
ATOM   6021  C  C   . LEU B  1 45  ? -2.055  37.892 45.183  1.00 24.84 ? 45   LEU B C   1 
ATOM   6022  O  O   . LEU B  1 45  ? -2.224  38.533 44.151  1.00 24.85 ? 45   LEU B O   1 
ATOM   6023  C  CB  . LEU B  1 45  ? -0.732  38.848 47.081  1.00 24.89 ? 45   LEU B CB  1 
ATOM   6024  C  CG  . LEU B  1 45  ? 0.159   39.801 46.274  1.00 24.36 ? 45   LEU B CG  1 
ATOM   6025  C  CD1 . LEU B  1 45  ? -0.474  41.192 46.224  1.00 21.96 ? 45   LEU B CD1 1 
ATOM   6026  C  CD2 . LEU B  1 45  ? 1.543   39.868 46.946  1.00 23.09 ? 45   LEU B CD2 1 
ATOM   6027  N  N   . THR B  1 46  ? -1.804  36.591 45.169  1.00 24.02 ? 46   THR B N   1 
ATOM   6028  C  CA  . THR B  1 46  ? -1.714  35.898 43.890  1.00 25.17 ? 46   THR B CA  1 
ATOM   6029  C  C   . THR B  1 46  ? -3.042  35.943 43.139  1.00 24.91 ? 46   THR B C   1 
ATOM   6030  O  O   . THR B  1 46  ? -3.069  36.028 41.907  1.00 25.49 ? 46   THR B O   1 
ATOM   6031  C  CB  . THR B  1 46  ? -1.320  34.435 44.056  1.00 25.15 ? 46   THR B CB  1 
ATOM   6032  O  OG1 . THR B  1 46  ? -0.163  34.349 44.882  1.00 30.11 ? 46   THR B OG1 1 
ATOM   6033  C  CG2 . THR B  1 46  ? -0.974  33.841 42.715  1.00 25.19 ? 46   THR B CG2 1 
ATOM   6034  N  N   . ASP B  1 47  ? -4.143  35.869 43.879  1.00 24.95 ? 47   ASP B N   1 
ATOM   6035  C  CA  . ASP B  1 47  ? -5.457  35.923 43.257  1.00 25.22 ? 47   ASP B CA  1 
ATOM   6036  C  C   . ASP B  1 47  ? -5.575  37.241 42.514  1.00 25.54 ? 47   ASP B C   1 
ATOM   6037  O  O   . ASP B  1 47  ? -6.029  37.290 41.361  1.00 25.21 ? 47   ASP B O   1 
ATOM   6038  C  CB  . ASP B  1 47  ? -6.550  35.824 44.317  1.00 25.28 ? 47   ASP B CB  1 
ATOM   6039  C  CG  . ASP B  1 47  ? -6.768  34.393 44.787  1.00 25.41 ? 47   ASP B CG  1 
ATOM   6040  O  OD1 . ASP B  1 47  ? -7.277  34.214 45.903  1.00 25.19 ? 47   ASP B OD1 1 
ATOM   6041  O  OD2 . ASP B  1 47  ? -6.435  33.470 44.024  1.00 25.15 ? 47   ASP B OD2 1 
ATOM   6042  N  N   . TYR B  1 48  ? -5.159  38.310 43.183  1.00 24.75 ? 48   TYR B N   1 
ATOM   6043  C  CA  . TYR B  1 48  ? -5.206  39.631 42.578  1.00 25.03 ? 48   TYR B CA  1 
ATOM   6044  C  C   . TYR B  1 48  ? -4.247  39.742 41.390  1.00 24.88 ? 48   TYR B C   1 
ATOM   6045  O  O   . TYR B  1 48  ? -4.655  40.135 40.301  1.00 24.25 ? 48   TYR B O   1 
ATOM   6046  C  CB  . TYR B  1 48  ? -4.869  40.705 43.620  1.00 25.03 ? 48   TYR B CB  1 
ATOM   6047  C  CG  . TYR B  1 48  ? -4.651  42.079 43.016  1.00 25.83 ? 48   TYR B CG  1 
ATOM   6048  C  CD1 . TYR B  1 48  ? -5.614  42.665 42.185  1.00 26.39 ? 48   TYR B CD1 1 
ATOM   6049  C  CD2 . TYR B  1 48  ? -3.473  42.786 43.265  1.00 25.19 ? 48   TYR B CD2 1 
ATOM   6050  C  CE1 . TYR B  1 48  ? -5.406  43.925 41.617  1.00 26.70 ? 48   TYR B CE1 1 
ATOM   6051  C  CE2 . TYR B  1 48  ? -3.249  44.039 42.710  1.00 25.89 ? 48   TYR B CE2 1 
ATOM   6052  C  CZ  . TYR B  1 48  ? -4.217  44.609 41.889  1.00 26.99 ? 48   TYR B CZ  1 
ATOM   6053  O  OH  . TYR B  1 48  ? -4.010  45.866 41.379  1.00 26.25 ? 48   TYR B OH  1 
ATOM   6054  N  N   . LEU B  1 49  ? -2.982  39.377 41.596  1.00 25.70 ? 49   LEU B N   1 
ATOM   6055  C  CA  . LEU B  1 49  ? -1.974  39.478 40.535  1.00 26.66 ? 49   LEU B CA  1 
ATOM   6056  C  C   . LEU B  1 49  ? -2.179  38.517 39.366  1.00 27.64 ? 49   LEU B C   1 
ATOM   6057  O  O   . LEU B  1 49  ? -1.699  38.760 38.262  1.00 27.96 ? 49   LEU B O   1 
ATOM   6058  C  CB  . LEU B  1 49  ? -0.570  39.294 41.133  1.00 25.52 ? 49   LEU B CB  1 
ATOM   6059  C  CG  . LEU B  1 49  ? -0.190  40.326 42.207  1.00 23.38 ? 49   LEU B CG  1 
ATOM   6060  C  CD1 . LEU B  1 49  ? 1.259   40.127 42.640  1.00 23.78 ? 49   LEU B CD1 1 
ATOM   6061  C  CD2 . LEU B  1 49  ? -0.374  41.725 41.648  1.00 24.40 ? 49   LEU B CD2 1 
ATOM   6062  N  N   . LYS B  1 50  ? -2.892  37.421 39.604  1.00 29.75 ? 50   LYS B N   1 
ATOM   6063  C  CA  . LYS B  1 50  ? -3.147  36.462 38.544  1.00 30.46 ? 50   LYS B CA  1 
ATOM   6064  C  C   . LYS B  1 50  ? -4.569  36.562 38.019  1.00 31.31 ? 50   LYS B C   1 
ATOM   6065  O  O   . LYS B  1 50  ? -4.952  35.814 37.130  1.00 31.41 ? 50   LYS B O   1 
ATOM   6066  C  CB  . LYS B  1 50  ? -2.865  35.048 39.040  1.00 31.63 ? 50   LYS B CB  1 
ATOM   6067  C  CG  . LYS B  1 50  ? -1.395  34.822 39.364  1.00 32.51 ? 50   LYS B CG  1 
ATOM   6068  C  CD  . LYS B  1 50  ? -0.494  35.186 38.174  1.00 34.24 ? 50   LYS B CD  1 
ATOM   6069  C  CE  . LYS B  1 50  ? 0.983   34.922 38.500  1.00 34.81 ? 50   LYS B CE  1 
ATOM   6070  N  NZ  . LYS B  1 50  ? 1.893   35.288 37.374  1.00 34.88 ? 50   LYS B NZ  1 
ATOM   6071  N  N   . ASN B  1 51  ? -5.345  37.495 38.565  1.00 31.94 ? 51   ASN B N   1 
ATOM   6072  C  CA  . ASN B  1 51  ? -6.730  37.691 38.140  1.00 33.18 ? 51   ASN B CA  1 
ATOM   6073  C  C   . ASN B  1 51  ? -7.511  36.381 38.144  1.00 33.20 ? 51   ASN B C   1 
ATOM   6074  O  O   . ASN B  1 51  ? -8.211  36.073 37.187  1.00 32.81 ? 51   ASN B O   1 
ATOM   6075  C  CB  . ASN B  1 51  ? -6.774  38.281 36.727  1.00 34.61 ? 51   ASN B CB  1 
ATOM   6076  C  CG  . ASN B  1 51  ? -8.080  39.043 36.441  1.00 37.56 ? 51   ASN B CG  1 
ATOM   6077  O  OD1 . ASN B  1 51  ? -8.429  39.285 35.284  1.00 39.57 ? 51   ASN B OD1 1 
ATOM   6078  N  ND2 . ASN B  1 51  ? -8.793  39.435 37.498  1.00 37.59 ? 51   ASN B ND2 1 
ATOM   6079  N  N   . THR B  1 52  ? -7.395  35.603 39.211  1.00 32.94 ? 52   THR B N   1 
ATOM   6080  C  CA  . THR B  1 52  ? -8.114  34.349 39.257  1.00 33.96 ? 52   THR B CA  1 
ATOM   6081  C  C   . THR B  1 52  ? -9.632  34.578 39.282  1.00 33.95 ? 52   THR B C   1 
ATOM   6082  O  O   . THR B  1 52  ? -10.392 33.776 38.736  1.00 33.13 ? 52   THR B O   1 
ATOM   6083  C  CB  . THR B  1 52  ? -7.699  33.509 40.477  1.00 34.34 ? 52   THR B CB  1 
ATOM   6084  O  OG1 . THR B  1 52  ? -8.167  34.141 41.662  1.00 36.48 ? 52   THR B OG1 1 
ATOM   6085  C  CG2 . THR B  1 52  ? -6.195  33.394 40.561  1.00 34.58 ? 52   THR B CG2 1 
ATOM   6086  N  N   . TYR B  1 53  ? -10.077 35.662 39.911  1.00 33.63 ? 53   TYR B N   1 
ATOM   6087  C  CA  . TYR B  1 53  ? -11.508 35.960 39.975  1.00 34.26 ? 53   TYR B CA  1 
ATOM   6088  C  C   . TYR B  1 53  ? -11.851 37.068 38.979  1.00 34.89 ? 53   TYR B C   1 
ATOM   6089  O  O   . TYR B  1 53  ? -11.807 38.253 39.297  1.00 35.36 ? 53   TYR B O   1 
ATOM   6090  C  CB  . TYR B  1 53  ? -11.888 36.353 41.398  1.00 33.52 ? 53   TYR B CB  1 
ATOM   6091  C  CG  . TYR B  1 53  ? -11.663 35.221 42.389  1.00 34.09 ? 53   TYR B CG  1 
ATOM   6092  C  CD1 . TYR B  1 53  ? -12.495 34.098 42.403  1.00 34.07 ? 53   TYR B CD1 1 
ATOM   6093  C  CD2 . TYR B  1 53  ? -10.597 35.262 43.291  1.00 34.02 ? 53   TYR B CD2 1 
ATOM   6094  C  CE1 . TYR B  1 53  ? -12.270 33.033 43.299  1.00 34.69 ? 53   TYR B CE1 1 
ATOM   6095  C  CE2 . TYR B  1 53  ? -10.360 34.217 44.183  1.00 34.81 ? 53   TYR B CE2 1 
ATOM   6096  C  CZ  . TYR B  1 53  ? -11.199 33.103 44.186  1.00 35.12 ? 53   TYR B CZ  1 
ATOM   6097  O  OH  . TYR B  1 53  ? -10.950 32.076 45.076  1.00 34.81 ? 53   TYR B OH  1 
ATOM   6098  N  N   . ARG B  1 54  ? -12.211 36.657 37.770  1.00 35.44 ? 54   ARG B N   1 
ATOM   6099  C  CA  . ARG B  1 54  ? -12.497 37.573 36.674  1.00 36.09 ? 54   ARG B CA  1 
ATOM   6100  C  C   . ARG B  1 54  ? -13.881 38.215 36.667  1.00 35.30 ? 54   ARG B C   1 
ATOM   6101  O  O   . ARG B  1 54  ? -14.911 37.539 36.696  1.00 34.01 ? 54   ARG B O   1 
ATOM   6102  C  CB  . ARG B  1 54  ? -12.286 36.830 35.354  1.00 38.43 ? 54   ARG B CB  1 
ATOM   6103  C  CG  . ARG B  1 54  ? -11.847 37.692 34.186  1.00 42.06 ? 54   ARG B CG  1 
ATOM   6104  C  CD  . ARG B  1 54  ? -10.378 37.418 33.864  1.00 44.92 ? 54   ARG B CD  1 
ATOM   6105  N  NE  . ARG B  1 54  ? -10.102 35.983 33.785  1.00 47.12 ? 54   ARG B NE  1 
ATOM   6106  C  CZ  . ARG B  1 54  ? -8.919  35.458 33.480  1.00 48.64 ? 54   ARG B CZ  1 
ATOM   6107  N  NH1 . ARG B  1 54  ? -7.882  36.246 33.221  1.00 48.79 ? 54   ARG B NH1 1 
ATOM   6108  N  NH2 . ARG B  1 54  ? -8.774  34.138 33.423  1.00 49.69 ? 54   ARG B NH2 1 
ATOM   6109  N  N   . LEU B  1 55  ? -13.892 39.536 36.606  1.00 34.81 ? 55   LEU B N   1 
ATOM   6110  C  CA  . LEU B  1 55  ? -15.137 40.277 36.543  1.00 34.29 ? 55   LEU B CA  1 
ATOM   6111  C  C   . LEU B  1 55  ? -15.588 40.215 35.080  1.00 34.03 ? 55   LEU B C   1 
ATOM   6112  O  O   . LEU B  1 55  ? -14.804 40.505 34.183  1.00 33.39 ? 55   LEU B O   1 
ATOM   6113  C  CB  . LEU B  1 55  ? -14.889 41.725 36.947  1.00 35.04 ? 55   LEU B CB  1 
ATOM   6114  C  CG  . LEU B  1 55  ? -16.009 42.434 37.676  1.00 36.05 ? 55   LEU B CG  1 
ATOM   6115  C  CD1 . LEU B  1 55  ? -16.262 41.744 38.989  1.00 37.25 ? 55   LEU B CD1 1 
ATOM   6116  C  CD2 . LEU B  1 55  ? -15.627 43.880 37.925  1.00 37.94 ? 55   LEU B CD2 1 
ATOM   6117  N  N   . LYS B  1 56  ? -16.828 39.810 34.821  1.00 33.33 ? 56   LYS B N   1 
ATOM   6118  C  CA  . LYS B  1 56  ? -17.288 39.767 33.436  1.00 33.17 ? 56   LYS B CA  1 
ATOM   6119  C  C   . LYS B  1 56  ? -17.951 41.083 33.083  1.00 32.61 ? 56   LYS B C   1 
ATOM   6120  O  O   . LYS B  1 56  ? -18.569 41.728 33.922  1.00 32.39 ? 56   LYS B O   1 
ATOM   6121  C  CB  . LYS B  1 56  ? -18.305 38.639 33.206  1.00 34.62 ? 56   LYS B CB  1 
ATOM   6122  C  CG  . LYS B  1 56  ? -17.715 37.246 33.028  1.00 36.61 ? 56   LYS B CG  1 
ATOM   6123  C  CD  . LYS B  1 56  ? -18.737 36.325 32.362  1.00 37.92 ? 56   LYS B CD  1 
ATOM   6124  C  CE  . LYS B  1 56  ? -18.274 34.878 32.334  1.00 38.81 ? 56   LYS B CE  1 
ATOM   6125  N  NZ  . LYS B  1 56  ? -16.990 34.717 31.574  1.00 41.00 ? 56   LYS B NZ  1 
ATOM   6126  N  N   . LEU B  1 57  ? -17.812 41.499 31.838  1.00 32.26 ? 57   LEU B N   1 
ATOM   6127  C  CA  . LEU B  1 57  ? -18.467 42.723 31.413  1.00 32.26 ? 57   LEU B CA  1 
ATOM   6128  C  C   . LEU B  1 57  ? -19.216 42.444 30.120  1.00 31.00 ? 57   LEU B C   1 
ATOM   6129  O  O   . LEU B  1 57  ? -19.239 41.301 29.643  1.00 31.39 ? 57   LEU B O   1 
ATOM   6130  C  CB  . LEU B  1 57  ? -17.453 43.856 31.244  1.00 34.27 ? 57   LEU B CB  1 
ATOM   6131  C  CG  . LEU B  1 57  ? -16.032 43.394 30.983  1.00 35.04 ? 57   LEU B CG  1 
ATOM   6132  C  CD1 . LEU B  1 57  ? -15.976 42.891 29.561  1.00 35.33 ? 57   LEU B CD1 1 
ATOM   6133  C  CD2 . LEU B  1 57  ? -15.040 44.537 31.221  1.00 35.80 ? 57   LEU B CD2 1 
ATOM   6134  N  N   . TYR B  1 58  ? -19.849 43.466 29.563  1.00 28.76 ? 58   TYR B N   1 
ATOM   6135  C  CA  . TYR B  1 58  ? -20.597 43.278 28.334  1.00 27.41 ? 58   TYR B CA  1 
ATOM   6136  C  C   . TYR B  1 58  ? -20.409 44.535 27.502  1.00 27.35 ? 58   TYR B C   1 
ATOM   6137  O  O   . TYR B  1 58  ? -21.228 45.451 27.551  1.00 27.11 ? 58   TYR B O   1 
ATOM   6138  C  CB  . TYR B  1 58  ? -22.084 43.040 28.662  1.00 24.59 ? 58   TYR B CB  1 
ATOM   6139  C  CG  . TYR B  1 58  ? -22.878 42.464 27.503  1.00 24.38 ? 58   TYR B CG  1 
ATOM   6140  C  CD1 . TYR B  1 58  ? -23.320 43.275 26.458  1.00 23.33 ? 58   TYR B CD1 1 
ATOM   6141  C  CD2 . TYR B  1 58  ? -23.180 41.098 27.451  1.00 23.52 ? 58   TYR B CD2 1 
ATOM   6142  C  CE1 . TYR B  1 58  ? -24.051 42.743 25.385  1.00 24.04 ? 58   TYR B CE1 1 
ATOM   6143  C  CE2 . TYR B  1 58  ? -23.905 40.554 26.389  1.00 24.43 ? 58   TYR B CE2 1 
ATOM   6144  C  CZ  . TYR B  1 58  ? -24.337 41.380 25.356  1.00 24.28 ? 58   TYR B CZ  1 
ATOM   6145  O  OH  . TYR B  1 58  ? -25.011 40.833 24.287  1.00 24.88 ? 58   TYR B OH  1 
ATOM   6146  N  N   . SER B  1 59  ? -19.308 44.573 26.761  1.00 26.77 ? 59   SER B N   1 
ATOM   6147  C  CA  . SER B  1 59  ? -18.972 45.711 25.932  1.00 27.04 ? 59   SER B CA  1 
ATOM   6148  C  C   . SER B  1 59  ? -19.584 45.528 24.565  1.00 26.79 ? 59   SER B C   1 
ATOM   6149  O  O   . SER B  1 59  ? -19.185 44.630 23.819  1.00 27.28 ? 59   SER B O   1 
ATOM   6150  C  CB  . SER B  1 59  ? -17.450 45.838 25.773  1.00 28.28 ? 59   SER B CB  1 
ATOM   6151  O  OG  . SER B  1 59  ? -16.792 45.777 27.032  1.00 30.30 ? 59   SER B OG  1 
ATOM   6152  N  N   . LEU B  1 60  ? -20.550 46.377 24.231  1.00 24.79 ? 60   LEU B N   1 
ATOM   6153  C  CA  . LEU B  1 60  ? -21.200 46.295 22.931  1.00 24.71 ? 60   LEU B CA  1 
ATOM   6154  C  C   . LEU B  1 60  ? -20.953 47.588 22.149  1.00 24.84 ? 60   LEU B C   1 
ATOM   6155  O  O   . LEU B  1 60  ? -20.605 48.617 22.727  1.00 23.47 ? 60   LEU B O   1 
ATOM   6156  C  CB  . LEU B  1 60  ? -22.712 46.066 23.121  1.00 22.52 ? 60   LEU B CB  1 
ATOM   6157  C  CG  . LEU B  1 60  ? -23.501 47.037 24.020  1.00 22.48 ? 60   LEU B CG  1 
ATOM   6158  C  CD1 . LEU B  1 60  ? -23.680 48.373 23.288  1.00 21.07 ? 60   LEU B CD1 1 
ATOM   6159  C  CD2 . LEU B  1 60  ? -24.875 46.449 24.385  1.00 19.20 ? 60   LEU B CD2 1 
ATOM   6160  N  N   . ARG B  1 61  ? -21.147 47.536 20.838  1.00 26.10 ? 61   ARG B N   1 
ATOM   6161  C  CA  . ARG B  1 61  ? -20.972 48.722 19.999  1.00 27.38 ? 61   ARG B CA  1 
ATOM   6162  C  C   . ARG B  1 61  ? -22.223 48.927 19.171  1.00 27.35 ? 61   ARG B C   1 
ATOM   6163  O  O   . ARG B  1 61  ? -22.489 48.158 18.263  1.00 27.70 ? 61   ARG B O   1 
ATOM   6164  C  CB  . ARG B  1 61  ? -19.789 48.557 19.042  1.00 29.13 ? 61   ARG B CB  1 
ATOM   6165  C  CG  . ARG B  1 61  ? -18.485 48.187 19.711  1.00 31.72 ? 61   ARG B CG  1 
ATOM   6166  C  CD  . ARG B  1 61  ? -17.390 47.981 18.673  1.00 34.31 ? 61   ARG B CD  1 
ATOM   6167  N  NE  . ARG B  1 61  ? -16.119 47.655 19.309  1.00 35.85 ? 61   ARG B NE  1 
ATOM   6168  C  CZ  . ARG B  1 61  ? -14.953 47.610 18.671  1.00 36.58 ? 61   ARG B CZ  1 
ATOM   6169  N  NH1 . ARG B  1 61  ? -14.901 47.870 17.372  1.00 35.91 ? 61   ARG B NH1 1 
ATOM   6170  N  NH2 . ARG B  1 61  ? -13.843 47.312 19.338  1.00 36.62 ? 61   ARG B NH2 1 
ATOM   6171  N  N   . TRP B  1 62  ? -22.984 49.968 19.482  1.00 27.64 ? 62   TRP B N   1 
ATOM   6172  C  CA  . TRP B  1 62  ? -24.202 50.268 18.739  1.00 28.00 ? 62   TRP B CA  1 
ATOM   6173  C  C   . TRP B  1 62  ? -23.823 50.613 17.304  1.00 29.47 ? 62   TRP B C   1 
ATOM   6174  O  O   . TRP B  1 62  ? -22.965 51.464 17.089  1.00 29.61 ? 62   TRP B O   1 
ATOM   6175  C  CB  . TRP B  1 62  ? -24.923 51.464 19.373  1.00 25.59 ? 62   TRP B CB  1 
ATOM   6176  C  CG  . TRP B  1 62  ? -25.590 51.137 20.670  1.00 25.58 ? 62   TRP B CG  1 
ATOM   6177  C  CD1 . TRP B  1 62  ? -25.217 51.542 21.921  1.00 24.97 ? 62   TRP B CD1 1 
ATOM   6178  C  CD2 . TRP B  1 62  ? -26.756 50.326 20.843  1.00 24.57 ? 62   TRP B CD2 1 
ATOM   6179  N  NE1 . TRP B  1 62  ? -26.084 51.033 22.862  1.00 24.14 ? 62   TRP B NE1 1 
ATOM   6180  C  CE2 . TRP B  1 62  ? -27.037 50.283 22.227  1.00 24.37 ? 62   TRP B CE2 1 
ATOM   6181  C  CE3 . TRP B  1 62  ? -27.591 49.634 19.961  1.00 24.58 ? 62   TRP B CE3 1 
ATOM   6182  C  CZ2 . TRP B  1 62  ? -28.117 49.576 22.750  1.00 24.24 ? 62   TRP B CZ2 1 
ATOM   6183  C  CZ3 . TRP B  1 62  ? -28.671 48.928 20.482  1.00 26.36 ? 62   TRP B CZ3 1 
ATOM   6184  C  CH2 . TRP B  1 62  ? -28.923 48.905 21.868  1.00 25.15 ? 62   TRP B CH2 1 
ATOM   6185  N  N   . ILE B  1 63  ? -24.452 49.972 16.323  1.00 29.81 ? 63   ILE B N   1 
ATOM   6186  C  CA  . ILE B  1 63  ? -24.138 50.283 14.931  1.00 30.30 ? 63   ILE B CA  1 
ATOM   6187  C  C   . ILE B  1 63  ? -25.300 51.018 14.290  1.00 30.09 ? 63   ILE B C   1 
ATOM   6188  O  O   . ILE B  1 63  ? -25.182 51.558 13.193  1.00 29.91 ? 63   ILE B O   1 
ATOM   6189  C  CB  . ILE B  1 63  ? -23.847 49.017 14.091  1.00 30.95 ? 63   ILE B CB  1 
ATOM   6190  C  CG1 . ILE B  1 63  ? -25.126 48.191 13.911  1.00 31.53 ? 63   ILE B CG1 1 
ATOM   6191  C  CG2 . ILE B  1 63  ? -22.772 48.188 14.772  1.00 31.27 ? 63   ILE B CG2 1 
ATOM   6192  C  CD1 . ILE B  1 63  ? -25.000 47.122 12.830  1.00 30.18 ? 63   ILE B CD1 1 
ATOM   6193  N  N   . SER B  1 64  ? -26.428 51.025 14.983  1.00 29.10 ? 64   SER B N   1 
ATOM   6194  C  CA  . SER B  1 64  ? -27.617 51.696 14.491  1.00 28.81 ? 64   SER B CA  1 
ATOM   6195  C  C   . SER B  1 64  ? -28.516 51.950 15.691  1.00 28.88 ? 64   SER B C   1 
ATOM   6196  O  O   . SER B  1 64  ? -28.081 51.828 16.845  1.00 27.40 ? 64   SER B O   1 
ATOM   6197  C  CB  . SER B  1 64  ? -28.350 50.800 13.500  1.00 28.25 ? 64   SER B CB  1 
ATOM   6198  O  OG  . SER B  1 64  ? -28.883 49.669 14.178  1.00 28.50 ? 64   SER B OG  1 
ATOM   6199  N  N   . ASP B  1 65  ? -29.777 52.260 15.423  1.00 28.49 ? 65   ASP B N   1 
ATOM   6200  C  CA  . ASP B  1 65  ? -30.707 52.517 16.503  1.00 29.85 ? 65   ASP B CA  1 
ATOM   6201  C  C   . ASP B  1 65  ? -31.319 51.228 17.084  1.00 30.50 ? 65   ASP B C   1 
ATOM   6202  O  O   . ASP B  1 65  ? -31.961 51.279 18.126  1.00 30.36 ? 65   ASP B O   1 
ATOM   6203  C  CB  . ASP B  1 65  ? -31.802 53.464 16.024  1.00 30.39 ? 65   ASP B CB  1 
ATOM   6204  C  CG  . ASP B  1 65  ? -32.435 54.250 17.169  1.00 32.32 ? 65   ASP B CG  1 
ATOM   6205  O  OD1 . ASP B  1 65  ? -31.718 54.597 18.142  1.00 33.13 ? 65   ASP B OD1 1 
ATOM   6206  O  OD2 . ASP B  1 65  ? -33.647 54.549 17.092  1.00 33.46 ? 65   ASP B OD2 1 
ATOM   6207  N  N   . HIS B  1 66  ? -31.100 50.079 16.439  1.00 30.67 ? 66   HIS B N   1 
ATOM   6208  C  CA  . HIS B  1 66  ? -31.653 48.805 16.931  1.00 32.28 ? 66   HIS B CA  1 
ATOM   6209  C  C   . HIS B  1 66  ? -30.666 47.646 16.968  1.00 30.98 ? 66   HIS B C   1 
ATOM   6210  O  O   . HIS B  1 66  ? -31.023 46.549 17.390  1.00 30.06 ? 66   HIS B O   1 
ATOM   6211  C  CB  . HIS B  1 66  ? -32.842 48.338 16.079  1.00 35.78 ? 66   HIS B CB  1 
ATOM   6212  C  CG  . HIS B  1 66  ? -33.358 49.377 15.146  1.00 39.74 ? 66   HIS B CG  1 
ATOM   6213  N  ND1 . HIS B  1 66  ? -34.465 50.152 15.428  1.00 41.12 ? 66   HIS B ND1 1 
ATOM   6214  C  CD2 . HIS B  1 66  ? -32.864 49.835 13.972  1.00 40.84 ? 66   HIS B CD2 1 
ATOM   6215  C  CE1 . HIS B  1 66  ? -34.624 51.049 14.470  1.00 41.61 ? 66   HIS B CE1 1 
ATOM   6216  N  NE2 . HIS B  1 66  ? -33.665 50.880 13.577  1.00 42.40 ? 66   HIS B NE2 1 
ATOM   6217  N  N   . GLU B  1 67  ? -29.434 47.861 16.523  1.00 30.12 ? 67   GLU B N   1 
ATOM   6218  C  CA  . GLU B  1 67  ? -28.473 46.767 16.527  1.00 28.77 ? 67   GLU B CA  1 
ATOM   6219  C  C   . GLU B  1 67  ? -27.118 47.131 17.105  1.00 28.62 ? 67   GLU B C   1 
ATOM   6220  O  O   . GLU B  1 67  ? -26.660 48.271 16.984  1.00 27.76 ? 67   GLU B O   1 
ATOM   6221  C  CB  . GLU B  1 67  ? -28.252 46.245 15.108  1.00 29.74 ? 67   GLU B CB  1 
ATOM   6222  C  CG  . GLU B  1 67  ? -29.480 45.738 14.396  1.00 31.96 ? 67   GLU B CG  1 
ATOM   6223  C  CD  . GLU B  1 67  ? -29.103 44.900 13.176  1.00 33.59 ? 67   GLU B CD  1 
ATOM   6224  O  OE1 . GLU B  1 67  ? -28.290 45.376 12.356  1.00 34.14 ? 67   GLU B OE1 1 
ATOM   6225  O  OE2 . GLU B  1 67  ? -29.611 43.769 13.051  1.00 34.70 ? 67   GLU B OE2 1 
ATOM   6226  N  N   . TYR B  1 68  ? -26.471 46.151 17.730  1.00 27.65 ? 68   TYR B N   1 
ATOM   6227  C  CA  . TYR B  1 68  ? -25.146 46.372 18.290  1.00 27.76 ? 68   TYR B CA  1 
ATOM   6228  C  C   . TYR B  1 68  ? -24.277 45.174 18.019  1.00 29.42 ? 68   TYR B C   1 
ATOM   6229  O  O   . TYR B  1 68  ? -24.778 44.069 17.772  1.00 29.43 ? 68   TYR B O   1 
ATOM   6230  C  CB  . TYR B  1 68  ? -25.205 46.624 19.798  1.00 25.49 ? 68   TYR B CB  1 
ATOM   6231  C  CG  . TYR B  1 68  ? -25.706 45.468 20.652  1.00 24.13 ? 68   TYR B CG  1 
ATOM   6232  C  CD1 . TYR B  1 68  ? -24.882 44.384 20.970  1.00 23.44 ? 68   TYR B CD1 1 
ATOM   6233  C  CD2 . TYR B  1 68  ? -26.984 45.502 21.207  1.00 22.52 ? 68   TYR B CD2 1 
ATOM   6234  C  CE1 . TYR B  1 68  ? -25.328 43.361 21.836  1.00 22.29 ? 68   TYR B CE1 1 
ATOM   6235  C  CE2 . TYR B  1 68  ? -27.434 44.500 22.058  1.00 20.93 ? 68   TYR B CE2 1 
ATOM   6236  C  CZ  . TYR B  1 68  ? -26.608 43.432 22.374  1.00 22.10 ? 68   TYR B CZ  1 
ATOM   6237  O  OH  . TYR B  1 68  ? -27.067 42.450 23.236  1.00 20.59 ? 68   TYR B OH  1 
ATOM   6238  N  N   . LEU B  1 69  ? -22.968 45.404 18.065  1.00 30.71 ? 69   LEU B N   1 
ATOM   6239  C  CA  . LEU B  1 69  ? -21.997 44.344 17.842  1.00 31.91 ? 69   LEU B CA  1 
ATOM   6240  C  C   . LEU B  1 69  ? -21.505 43.880 19.199  1.00 33.46 ? 69   LEU B C   1 
ATOM   6241  O  O   . LEU B  1 69  ? -21.373 44.677 20.131  1.00 33.55 ? 69   LEU B O   1 
ATOM   6242  C  CB  . LEU B  1 69  ? -20.818 44.860 17.001  1.00 31.02 ? 69   LEU B CB  1 
ATOM   6243  C  CG  . LEU B  1 69  ? -21.157 45.207 15.543  1.00 30.92 ? 69   LEU B CG  1 
ATOM   6244  C  CD1 . LEU B  1 69  ? -19.945 45.822 14.872  1.00 29.50 ? 69   LEU B CD1 1 
ATOM   6245  C  CD2 . LEU B  1 69  ? -21.604 43.937 14.785  1.00 28.70 ? 69   LEU B CD2 1 
ATOM   6246  N  N   . TYR B  1 70  ? -21.259 42.584 19.311  1.00 35.00 ? 70   TYR B N   1 
ATOM   6247  C  CA  . TYR B  1 70  ? -20.769 42.011 20.550  1.00 37.34 ? 70   TYR B CA  1 
ATOM   6248  C  C   . TYR B  1 70  ? -19.797 40.908 20.168  1.00 39.25 ? 70   TYR B C   1 
ATOM   6249  O  O   . TYR B  1 70  ? -20.077 40.123 19.259  1.00 39.96 ? 70   TYR B O   1 
ATOM   6250  C  CB  . TYR B  1 70  ? -21.921 41.434 21.377  1.00 36.71 ? 70   TYR B CB  1 
ATOM   6251  C  CG  . TYR B  1 70  ? -21.473 40.867 22.700  1.00 37.25 ? 70   TYR B CG  1 
ATOM   6252  C  CD1 . TYR B  1 70  ? -20.927 41.689 23.678  1.00 37.08 ? 70   TYR B CD1 1 
ATOM   6253  C  CD2 . TYR B  1 70  ? -21.523 39.497 22.946  1.00 37.70 ? 70   TYR B CD2 1 
ATOM   6254  C  CE1 . TYR B  1 70  ? -20.429 41.162 24.866  1.00 37.91 ? 70   TYR B CE1 1 
ATOM   6255  C  CE2 . TYR B  1 70  ? -21.028 38.962 24.130  1.00 38.69 ? 70   TYR B CE2 1 
ATOM   6256  C  CZ  . TYR B  1 70  ? -20.477 39.805 25.083  1.00 38.03 ? 70   TYR B CZ  1 
ATOM   6257  O  OH  . TYR B  1 70  ? -19.939 39.285 26.236  1.00 39.62 ? 70   TYR B OH  1 
ATOM   6258  N  N   . LYS B  1 71  ? -18.650 40.861 20.840  1.00 41.76 ? 71   LYS B N   1 
ATOM   6259  C  CA  . LYS B  1 71  ? -17.634 39.844 20.549  1.00 44.09 ? 71   LYS B CA  1 
ATOM   6260  C  C   . LYS B  1 71  ? -17.882 38.607 21.419  1.00 45.67 ? 71   LYS B C   1 
ATOM   6261  O  O   . LYS B  1 71  ? -17.936 38.701 22.652  1.00 46.72 ? 71   LYS B O   1 
ATOM   6262  C  CB  . LYS B  1 71  ? -16.238 40.421 20.815  1.00 43.98 ? 71   LYS B CB  1 
ATOM   6263  C  CG  . LYS B  1 71  ? -15.133 39.928 19.863  1.00 44.82 ? 71   LYS B CG  1 
ATOM   6264  C  CD  . LYS B  1 71  ? -13.891 40.845 19.955  1.00 45.46 ? 71   LYS B CD  1 
ATOM   6265  C  CE  . LYS B  1 71  ? -12.775 40.447 18.969  1.00 46.11 ? 71   LYS B CE  1 
ATOM   6266  N  NZ  . LYS B  1 71  ? -11.691 41.490 18.872  1.00 45.56 ? 71   LYS B NZ  1 
ATOM   6267  N  N   . GLN B  1 72  ? -18.046 37.454 20.769  1.00 47.04 ? 72   GLN B N   1 
ATOM   6268  C  CA  . GLN B  1 72  ? -18.297 36.196 21.474  1.00 48.28 ? 72   GLN B CA  1 
ATOM   6269  C  C   . GLN B  1 72  ? -17.552 35.050 20.806  1.00 48.94 ? 72   GLN B C   1 
ATOM   6270  O  O   . GLN B  1 72  ? -17.697 34.826 19.604  1.00 48.91 ? 72   GLN B O   1 
ATOM   6271  C  CB  . GLN B  1 72  ? -19.792 35.885 21.486  1.00 48.66 ? 72   GLN B CB  1 
ATOM   6272  C  CG  . GLN B  1 72  ? -20.199 34.825 22.483  1.00 49.96 ? 72   GLN B CG  1 
ATOM   6273  C  CD  . GLN B  1 72  ? -21.705 34.751 22.658  1.00 51.33 ? 72   GLN B CD  1 
ATOM   6274  O  OE1 . GLN B  1 72  ? -22.424 34.266 21.776  1.00 51.66 ? 72   GLN B OE1 1 
ATOM   6275  N  NE2 . GLN B  1 72  ? -22.197 35.254 23.794  1.00 51.32 ? 72   GLN B NE2 1 
ATOM   6276  N  N   . GLU B  1 73  ? -16.752 34.325 21.585  1.00 50.07 ? 73   GLU B N   1 
ATOM   6277  C  CA  . GLU B  1 73  ? -15.987 33.211 21.035  1.00 50.81 ? 73   GLU B CA  1 
ATOM   6278  C  C   . GLU B  1 73  ? -15.060 33.776 19.946  1.00 50.63 ? 73   GLU B C   1 
ATOM   6279  O  O   . GLU B  1 73  ? -14.786 33.123 18.933  1.00 50.72 ? 73   GLU B O   1 
ATOM   6280  C  CB  . GLU B  1 73  ? -16.947 32.165 20.438  1.00 51.76 ? 73   GLU B CB  1 
ATOM   6281  C  CG  . GLU B  1 73  ? -17.856 31.463 21.463  1.00 53.64 ? 73   GLU B CG  1 
ATOM   6282  C  CD  . GLU B  1 73  ? -19.134 30.881 20.841  1.00 54.90 ? 73   GLU B CD  1 
ATOM   6283  O  OE1 . GLU B  1 73  ? -19.082 30.368 19.697  1.00 56.08 ? 73   GLU B OE1 1 
ATOM   6284  O  OE2 . GLU B  1 73  ? -20.198 30.928 21.505  1.00 55.39 ? 73   GLU B OE2 1 
ATOM   6285  N  N   . ASN B  1 74  ? -14.592 35.005 20.160  1.00 50.11 ? 74   ASN B N   1 
ATOM   6286  C  CA  . ASN B  1 74  ? -13.697 35.661 19.213  1.00 49.68 ? 74   ASN B CA  1 
ATOM   6287  C  C   . ASN B  1 74  ? -14.310 36.060 17.880  1.00 48.88 ? 74   ASN B C   1 
ATOM   6288  O  O   . ASN B  1 74  ? -13.657 36.725 17.072  1.00 49.25 ? 74   ASN B O   1 
ATOM   6289  C  CB  . ASN B  1 74  ? -12.462 34.796 18.963  1.00 50.24 ? 74   ASN B CB  1 
ATOM   6290  C  CG  . ASN B  1 74  ? -11.294 35.209 19.828  1.00 50.65 ? 74   ASN B CG  1 
ATOM   6291  O  OD1 . ASN B  1 74  ? -10.302 34.480 19.957  1.00 51.63 ? 74   ASN B OD1 1 
ATOM   6292  N  ND2 . ASN B  1 74  ? -11.399 36.395 20.425  1.00 49.76 ? 74   ASN B ND2 1 
ATOM   6293  N  N   . ASN B  1 75  ? -15.546 35.648 17.627  1.00 47.99 ? 75   ASN B N   1 
ATOM   6294  C  CA  . ASN B  1 75  ? -16.197 36.046 16.388  1.00 47.04 ? 75   ASN B CA  1 
ATOM   6295  C  C   . ASN B  1 75  ? -17.112 37.221 16.724  1.00 45.68 ? 75   ASN B C   1 
ATOM   6296  O  O   . ASN B  1 75  ? -17.607 37.337 17.852  1.00 45.60 ? 75   ASN B O   1 
ATOM   6297  C  CB  . ASN B  1 75  ? -17.000 34.891 15.778  1.00 49.13 ? 75   ASN B CB  1 
ATOM   6298  C  CG  . ASN B  1 75  ? -17.477 33.897 16.813  1.00 50.68 ? 75   ASN B CG  1 
ATOM   6299  O  OD1 . ASN B  1 75  ? -16.729 33.006 17.238  1.00 51.69 ? 75   ASN B OD1 1 
ATOM   6300  N  ND2 . ASN B  1 75  ? -18.728 34.046 17.236  1.00 51.55 ? 75   ASN B ND2 1 
ATOM   6301  N  N   . ILE B  1 76  ? -17.321 38.102 15.751  1.00 42.94 ? 76   ILE B N   1 
ATOM   6302  C  CA  . ILE B  1 76  ? -18.161 39.269 15.969  1.00 39.88 ? 76   ILE B CA  1 
ATOM   6303  C  C   . ILE B  1 76  ? -19.629 39.003 15.658  1.00 38.20 ? 76   ILE B C   1 
ATOM   6304  O  O   . ILE B  1 76  ? -19.995 38.715 14.520  1.00 38.27 ? 76   ILE B O   1 
ATOM   6305  C  CB  . ILE B  1 76  ? -17.680 40.441 15.118  1.00 39.46 ? 76   ILE B CB  1 
ATOM   6306  C  CG1 . ILE B  1 76  ? -16.260 40.819 15.536  1.00 38.75 ? 76   ILE B CG1 1 
ATOM   6307  C  CG2 . ILE B  1 76  ? -18.624 41.625 15.279  1.00 38.62 ? 76   ILE B CG2 1 
ATOM   6308  C  CD1 . ILE B  1 76  ? -15.646 41.899 14.680  1.00 39.34 ? 76   ILE B CD1 1 
ATOM   6309  N  N   . LEU B  1 77  ? -20.477 39.100 16.674  1.00 36.06 ? 77   LEU B N   1 
ATOM   6310  C  CA  . LEU B  1 77  ? -21.903 38.870 16.469  1.00 33.89 ? 77   LEU B CA  1 
ATOM   6311  C  C   . LEU B  1 77  ? -22.684 40.176 16.407  1.00 32.45 ? 77   LEU B C   1 
ATOM   6312  O  O   . LEU B  1 77  ? -22.266 41.190 16.982  1.00 31.91 ? 77   LEU B O   1 
ATOM   6313  C  CB  . LEU B  1 77  ? -22.474 38.020 17.601  1.00 34.29 ? 77   LEU B CB  1 
ATOM   6314  C  CG  . LEU B  1 77  ? -22.138 36.525 17.682  1.00 34.61 ? 77   LEU B CG  1 
ATOM   6315  C  CD1 . LEU B  1 77  ? -20.659 36.300 17.771  1.00 35.20 ? 77   LEU B CD1 1 
ATOM   6316  C  CD2 . LEU B  1 77  ? -22.827 35.960 18.911  1.00 34.49 ? 77   LEU B CD2 1 
ATOM   6317  N  N   . VAL B  1 78  ? -23.807 40.155 15.695  1.00 31.12 ? 78   VAL B N   1 
ATOM   6318  C  CA  . VAL B  1 78  ? -24.658 41.330 15.618  1.00 30.45 ? 78   VAL B CA  1 
ATOM   6319  C  C   . VAL B  1 78  ? -26.012 40.983 16.248  1.00 30.54 ? 78   VAL B C   1 
ATOM   6320  O  O   . VAL B  1 78  ? -26.680 40.012 15.852  1.00 30.71 ? 78   VAL B O   1 
ATOM   6321  C  CB  . VAL B  1 78  ? -24.855 41.824 14.169  1.00 30.15 ? 78   VAL B CB  1 
ATOM   6322  C  CG1 . VAL B  1 78  ? -25.447 40.735 13.295  1.00 29.69 ? 78   VAL B CG1 1 
ATOM   6323  C  CG2 . VAL B  1 78  ? -25.739 43.062 14.179  1.00 29.59 ? 78   VAL B CG2 1 
ATOM   6324  N  N   . PHE B  1 79  ? -26.401 41.780 17.242  1.00 29.73 ? 79   PHE B N   1 
ATOM   6325  C  CA  . PHE B  1 79  ? -27.652 41.574 17.973  1.00 28.48 ? 79   PHE B CA  1 
ATOM   6326  C  C   . PHE B  1 79  ? -28.788 42.518 17.633  1.00 28.38 ? 79   PHE B C   1 
ATOM   6327  O  O   . PHE B  1 79  ? -28.585 43.690 17.310  1.00 28.12 ? 79   PHE B O   1 
ATOM   6328  C  CB  . PHE B  1 79  ? -27.414 41.698 19.474  1.00 28.94 ? 79   PHE B CB  1 
ATOM   6329  C  CG  . PHE B  1 79  ? -26.695 40.534 20.087  1.00 28.85 ? 79   PHE B CG  1 
ATOM   6330  C  CD1 . PHE B  1 79  ? -27.384 39.628 20.883  1.00 28.95 ? 79   PHE B CD1 1 
ATOM   6331  C  CD2 . PHE B  1 79  ? -25.325 40.373 19.911  1.00 28.56 ? 79   PHE B CD2 1 
ATOM   6332  C  CE1 . PHE B  1 79  ? -26.727 38.582 21.502  1.00 28.45 ? 79   PHE B CE1 1 
ATOM   6333  C  CE2 . PHE B  1 79  ? -24.649 39.329 20.526  1.00 28.51 ? 79   PHE B CE2 1 
ATOM   6334  C  CZ  . PHE B  1 79  ? -25.351 38.429 21.326  1.00 29.92 ? 79   PHE B CZ  1 
ATOM   6335  N  N   . ASN B  1 80  ? -29.998 41.992 17.746  1.00 27.33 ? 80   ASN B N   1 
ATOM   6336  C  CA  . ASN B  1 80  ? -31.190 42.768 17.518  1.00 27.39 ? 80   ASN B CA  1 
ATOM   6337  C  C   . ASN B  1 80  ? -31.619 43.161 18.935  1.00 27.50 ? 80   ASN B C   1 
ATOM   6338  O  O   . ASN B  1 80  ? -32.003 42.302 19.730  1.00 27.36 ? 80   ASN B O   1 
ATOM   6339  C  CB  . ASN B  1 80  ? -32.255 41.899 16.843  1.00 27.36 ? 80   ASN B CB  1 
ATOM   6340  C  CG  . ASN B  1 80  ? -33.566 42.627 16.668  1.00 27.66 ? 80   ASN B CG  1 
ATOM   6341  O  OD1 . ASN B  1 80  ? -34.307 42.839 17.633  1.00 27.90 ? 80   ASN B OD1 1 
ATOM   6342  N  ND2 . ASN B  1 80  ? -33.860 43.028 15.434  1.00 26.65 ? 80   ASN B ND2 1 
ATOM   6343  N  N   . ALA B  1 81  ? -31.533 44.448 19.259  1.00 27.31 ? 81   ALA B N   1 
ATOM   6344  C  CA  . ALA B  1 81  ? -31.886 44.915 20.597  1.00 27.98 ? 81   ALA B CA  1 
ATOM   6345  C  C   . ALA B  1 81  ? -33.300 44.540 21.034  1.00 28.81 ? 81   ALA B C   1 
ATOM   6346  O  O   . ALA B  1 81  ? -33.526 44.144 22.181  1.00 27.82 ? 81   ALA B O   1 
ATOM   6347  C  CB  . ALA B  1 81  ? -31.719 46.425 20.688  1.00 26.74 ? 81   ALA B CB  1 
ATOM   6348  N  N   . GLU B  1 82  ? -34.243 44.687 20.112  1.00 29.30 ? 82   GLU B N   1 
ATOM   6349  C  CA  . GLU B  1 82  ? -35.649 44.424 20.379  1.00 31.67 ? 82   GLU B CA  1 
ATOM   6350  C  C   . GLU B  1 82  ? -35.963 43.024 20.864  1.00 31.74 ? 82   GLU B C   1 
ATOM   6351  O  O   . GLU B  1 82  ? -36.676 42.856 21.850  1.00 30.86 ? 82   GLU B O   1 
ATOM   6352  C  CB  . GLU B  1 82  ? -36.472 44.704 19.124  1.00 33.50 ? 82   GLU B CB  1 
ATOM   6353  C  CG  . GLU B  1 82  ? -37.933 44.984 19.386  1.00 36.73 ? 82   GLU B CG  1 
ATOM   6354  C  CD  . GLU B  1 82  ? -38.709 45.218 18.096  1.00 38.71 ? 82   GLU B CD  1 
ATOM   6355  O  OE1 . GLU B  1 82  ? -38.154 45.843 17.158  1.00 40.06 ? 82   GLU B OE1 1 
ATOM   6356  O  OE2 . GLU B  1 82  ? -39.879 44.786 18.024  1.00 40.11 ? 82   GLU B OE2 1 
ATOM   6357  N  N   . TYR B  1 83  ? -35.418 42.020 20.179  1.00 32.30 ? 83   TYR B N   1 
ATOM   6358  C  CA  . TYR B  1 83  ? -35.693 40.626 20.520  1.00 32.94 ? 83   TYR B CA  1 
ATOM   6359  C  C   . TYR B  1 83  ? -34.536 39.856 21.144  1.00 33.12 ? 83   TYR B C   1 
ATOM   6360  O  O   . TYR B  1 83  ? -34.738 38.803 21.747  1.00 32.70 ? 83   TYR B O   1 
ATOM   6361  C  CB  . TYR B  1 83  ? -36.200 39.901 19.277  1.00 33.82 ? 83   TYR B CB  1 
ATOM   6362  C  CG  . TYR B  1 83  ? -37.406 40.577 18.674  1.00 34.91 ? 83   TYR B CG  1 
ATOM   6363  C  CD1 . TYR B  1 83  ? -37.389 41.024 17.354  1.00 35.74 ? 83   TYR B CD1 1 
ATOM   6364  C  CD2 . TYR B  1 83  ? -38.553 40.800 19.436  1.00 35.69 ? 83   TYR B CD2 1 
ATOM   6365  C  CE1 . TYR B  1 83  ? -38.485 41.679 16.804  1.00 36.92 ? 83   TYR B CE1 1 
ATOM   6366  C  CE2 . TYR B  1 83  ? -39.655 41.455 18.901  1.00 37.35 ? 83   TYR B CE2 1 
ATOM   6367  C  CZ  . TYR B  1 83  ? -39.614 41.892 17.585  1.00 37.22 ? 83   TYR B CZ  1 
ATOM   6368  O  OH  . TYR B  1 83  ? -40.702 42.552 17.063  1.00 39.92 ? 83   TYR B OH  1 
ATOM   6369  N  N   . GLY B  1 84  ? -33.323 40.373 20.998  1.00 32.45 ? 84   GLY B N   1 
ATOM   6370  C  CA  . GLY B  1 84  ? -32.183 39.713 21.600  1.00 31.92 ? 84   GLY B CA  1 
ATOM   6371  C  C   . GLY B  1 84  ? -31.571 38.661 20.709  1.00 32.27 ? 84   GLY B C   1 
ATOM   6372  O  O   . GLY B  1 84  ? -30.589 38.032 21.088  1.00 31.47 ? 84   GLY B O   1 
ATOM   6373  N  N   . ASN B  1 85  ? -32.149 38.462 19.527  1.00 33.65 ? 85   ASN B N   1 
ATOM   6374  C  CA  . ASN B  1 85  ? -31.614 37.475 18.606  1.00 34.33 ? 85   ASN B CA  1 
ATOM   6375  C  C   . ASN B  1 85  ? -30.380 38.048 17.911  1.00 34.87 ? 85   ASN B C   1 
ATOM   6376  O  O   . ASN B  1 85  ? -30.119 39.255 17.959  1.00 33.72 ? 85   ASN B O   1 
ATOM   6377  C  CB  . ASN B  1 85  ? -32.669 37.059 17.580  1.00 35.91 ? 85   ASN B CB  1 
ATOM   6378  C  CG  . ASN B  1 85  ? -33.046 38.174 16.640  1.00 38.28 ? 85   ASN B CG  1 
ATOM   6379  O  OD1 . ASN B  1 85  ? -33.559 39.210 17.057  1.00 39.66 ? 85   ASN B OD1 1 
ATOM   6380  N  ND2 . ASN B  1 85  ? -32.793 37.961 15.352  1.00 40.69 ? 85   ASN B ND2 1 
ATOM   6381  N  N   . SER B  1 86  ? -29.619 37.187 17.254  1.00 34.98 ? 86   SER B N   1 
ATOM   6382  C  CA  . SER B  1 86  ? -28.408 37.649 16.610  1.00 35.38 ? 86   SER B CA  1 
ATOM   6383  C  C   . SER B  1 86  ? -27.976 36.800 15.428  1.00 36.65 ? 86   SER B C   1 
ATOM   6384  O  O   . SER B  1 86  ? -28.668 35.862 15.019  1.00 37.37 ? 86   SER B O   1 
ATOM   6385  C  CB  . SER B  1 86  ? -27.289 37.663 17.642  1.00 34.65 ? 86   SER B CB  1 
ATOM   6386  O  OG  . SER B  1 86  ? -27.079 36.351 18.132  1.00 31.37 ? 86   SER B OG  1 
ATOM   6387  N  N   . SER B  1 87  ? -26.807 37.142 14.897  1.00 37.06 ? 87   SER B N   1 
ATOM   6388  C  CA  . SER B  1 87  ? -26.216 36.442 13.761  1.00 37.65 ? 87   SER B CA  1 
ATOM   6389  C  C   . SER B  1 87  ? -24.720 36.714 13.766  1.00 37.48 ? 87   SER B C   1 
ATOM   6390  O  O   . SER B  1 87  ? -24.241 37.641 14.431  1.00 37.58 ? 87   SER B O   1 
ATOM   6391  C  CB  . SER B  1 87  ? -26.820 36.940 12.444  1.00 37.52 ? 87   SER B CB  1 
ATOM   6392  O  OG  . SER B  1 87  ? -28.230 36.827 12.462  1.00 38.87 ? 87   SER B OG  1 
ATOM   6393  N  N   . VAL B  1 88  ? -23.978 35.897 13.033  1.00 37.95 ? 88   VAL B N   1 
ATOM   6394  C  CA  . VAL B  1 88  ? -22.542 36.072 12.967  1.00 38.17 ? 88   VAL B CA  1 
ATOM   6395  C  C   . VAL B  1 88  ? -22.231 37.203 12.001  1.00 38.67 ? 88   VAL B C   1 
ATOM   6396  O  O   . VAL B  1 88  ? -22.560 37.145 10.819  1.00 38.95 ? 88   VAL B O   1 
ATOM   6397  C  CB  . VAL B  1 88  ? -21.839 34.793 12.498  1.00 38.96 ? 88   VAL B CB  1 
ATOM   6398  C  CG1 . VAL B  1 88  ? -20.353 35.077 12.249  1.00 39.04 ? 88   VAL B CG1 1 
ATOM   6399  C  CG2 . VAL B  1 88  ? -22.004 33.698 13.559  1.00 38.17 ? 88   VAL B CG2 1 
ATOM   6400  N  N   . PHE B  1 89  ? -21.606 38.250 12.514  1.00 38.31 ? 89   PHE B N   1 
ATOM   6401  C  CA  . PHE B  1 89  ? -21.270 39.376 11.669  1.00 38.03 ? 89   PHE B CA  1 
ATOM   6402  C  C   . PHE B  1 89  ? -19.936 39.105 10.996  1.00 38.34 ? 89   PHE B C   1 
ATOM   6403  O  O   . PHE B  1 89  ? -19.778 39.302 9.798   1.00 38.32 ? 89   PHE B O   1 
ATOM   6404  C  CB  . PHE B  1 89  ? -21.196 40.648 12.508  1.00 36.61 ? 89   PHE B CB  1 
ATOM   6405  C  CG  . PHE B  1 89  ? -20.944 41.882 11.701  1.00 35.89 ? 89   PHE B CG  1 
ATOM   6406  C  CD1 . PHE B  1 89  ? -19.654 42.348 11.516  1.00 35.68 ? 89   PHE B CD1 1 
ATOM   6407  C  CD2 . PHE B  1 89  ? -22.000 42.576 11.126  1.00 35.72 ? 89   PHE B CD2 1 
ATOM   6408  C  CE1 . PHE B  1 89  ? -19.412 43.501 10.769  1.00 35.79 ? 89   PHE B CE1 1 
ATOM   6409  C  CE2 . PHE B  1 89  ? -21.775 43.727 10.377  1.00 36.18 ? 89   PHE B CE2 1 
ATOM   6410  C  CZ  . PHE B  1 89  ? -20.472 44.188 10.201  1.00 35.69 ? 89   PHE B CZ  1 
ATOM   6411  N  N   . LEU B  1 90  ? -18.984 38.616 11.772  1.00 39.29 ? 90   LEU B N   1 
ATOM   6412  C  CA  . LEU B  1 90  ? -17.674 38.341 11.235  1.00 40.97 ? 90   LEU B CA  1 
ATOM   6413  C  C   . LEU B  1 90  ? -17.105 37.113 11.915  1.00 42.24 ? 90   LEU B C   1 
ATOM   6414  O  O   . LEU B  1 90  ? -16.704 37.164 13.085  1.00 41.85 ? 90   LEU B O   1 
ATOM   6415  C  CB  . LEU B  1 90  ? -16.762 39.532 11.482  1.00 41.16 ? 90   LEU B CB  1 
ATOM   6416  C  CG  . LEU B  1 90  ? -15.592 39.683 10.525  1.00 41.92 ? 90   LEU B CG  1 
ATOM   6417  C  CD1 . LEU B  1 90  ? -16.117 39.808 9.097   1.00 41.57 ? 90   LEU B CD1 1 
ATOM   6418  C  CD2 . LEU B  1 90  ? -14.779 40.918 10.935  1.00 41.95 ? 90   LEU B CD2 1 
ATOM   6419  N  N   . GLU B  1 91  ? -17.071 36.008 11.170  1.00 43.79 ? 91   GLU B N   1 
ATOM   6420  C  CA  . GLU B  1 91  ? -16.556 34.750 11.692  1.00 45.23 ? 91   GLU B CA  1 
ATOM   6421  C  C   . GLU B  1 91  ? -15.138 34.915 12.210  1.00 45.41 ? 91   GLU B C   1 
ATOM   6422  O  O   . GLU B  1 91  ? -14.298 35.563 11.578  1.00 45.15 ? 91   GLU B O   1 
ATOM   6423  C  CB  . GLU B  1 91  ? -16.595 33.669 10.610  1.00 46.62 ? 91   GLU B CB  1 
ATOM   6424  C  CG  . GLU B  1 91  ? -16.675 32.262 11.187  1.00 48.86 ? 91   GLU B CG  1 
ATOM   6425  C  CD  . GLU B  1 91  ? -17.710 32.169 12.310  1.00 50.20 ? 91   GLU B CD  1 
ATOM   6426  O  OE1 . GLU B  1 91  ? -17.392 32.566 13.461  1.00 51.41 ? 91   GLU B OE1 1 
ATOM   6427  O  OE2 . GLU B  1 91  ? -18.848 31.716 12.037  1.00 50.30 ? 91   GLU B OE2 1 
ATOM   6428  N  N   . ASN B  1 92  ? -14.874 34.322 13.368  1.00 46.05 ? 92   ASN B N   1 
ATOM   6429  C  CA  . ASN B  1 92  ? -13.555 34.409 13.979  1.00 46.92 ? 92   ASN B CA  1 
ATOM   6430  C  C   . ASN B  1 92  ? -12.429 33.810 13.115  1.00 47.10 ? 92   ASN B C   1 
ATOM   6431  O  O   . ASN B  1 92  ? -11.254 33.893 13.482  1.00 47.40 ? 92   ASN B O   1 
ATOM   6432  C  CB  . ASN B  1 92  ? -13.578 33.717 15.345  1.00 47.69 ? 92   ASN B CB  1 
ATOM   6433  C  CG  . ASN B  1 92  ? -13.699 32.208 15.233  1.00 49.17 ? 92   ASN B CG  1 
ATOM   6434  O  OD1 . ASN B  1 92  ? -12.840 31.546 14.650  1.00 50.39 ? 92   ASN B OD1 1 
ATOM   6435  N  ND2 . ASN B  1 92  ? -14.762 31.652 15.802  1.00 50.20 ? 92   ASN B ND2 1 
ATOM   6436  N  N   . SER B  1 93  ? -12.775 33.217 11.975  1.00 46.91 ? 93   SER B N   1 
ATOM   6437  C  CA  . SER B  1 93  ? -11.765 32.606 11.105  1.00 47.15 ? 93   SER B CA  1 
ATOM   6438  C  C   . SER B  1 93  ? -11.460 33.459 9.877   1.00 46.93 ? 93   SER B C   1 
ATOM   6439  O  O   . SER B  1 93  ? -10.544 33.161 9.100   1.00 46.91 ? 93   SER B O   1 
ATOM   6440  C  CB  . SER B  1 93  ? -12.249 31.239 10.633  1.00 47.37 ? 93   SER B CB  1 
ATOM   6441  O  OG  . SER B  1 93  ? -13.310 31.393 9.700   1.00 48.19 ? 93   SER B OG  1 
ATOM   6442  N  N   . THR B  1 94  ? -12.241 34.514 9.701   1.00 46.39 ? 94   THR B N   1 
ATOM   6443  C  CA  . THR B  1 94  ? -12.077 35.396 8.559   1.00 46.27 ? 94   THR B CA  1 
ATOM   6444  C  C   . THR B  1 94  ? -10.635 35.800 8.287   1.00 45.82 ? 94   THR B C   1 
ATOM   6445  O  O   . THR B  1 94  ? -10.186 35.757 7.141   1.00 45.81 ? 94   THR B O   1 
ATOM   6446  C  CB  . THR B  1 94  ? -12.907 36.661 8.737   1.00 46.20 ? 94   THR B CB  1 
ATOM   6447  O  OG1 . THR B  1 94  ? -14.269 36.293 9.000   1.00 47.10 ? 94   THR B OG1 1 
ATOM   6448  C  CG2 . THR B  1 94  ? -12.844 37.515 7.482   1.00 45.73 ? 94   THR B CG2 1 
ATOM   6449  N  N   . PHE B  1 95  ? -9.909  36.176 9.335   1.00 45.38 ? 95   PHE B N   1 
ATOM   6450  C  CA  . PHE B  1 95  ? -8.522  36.615 9.171   1.00 45.07 ? 95   PHE B CA  1 
ATOM   6451  C  C   . PHE B  1 95  ? -7.463  35.710 9.810   1.00 45.44 ? 95   PHE B C   1 
ATOM   6452  O  O   . PHE B  1 95  ? -6.466  36.200 10.340  1.00 45.10 ? 95   PHE B O   1 
ATOM   6453  C  CB  . PHE B  1 95  ? -8.382  38.030 9.729   1.00 43.43 ? 95   PHE B CB  1 
ATOM   6454  C  CG  . PHE B  1 95  ? -9.399  38.985 9.188   1.00 42.31 ? 95   PHE B CG  1 
ATOM   6455  C  CD1 . PHE B  1 95  ? -9.259  39.523 7.906   1.00 41.65 ? 95   PHE B CD1 1 
ATOM   6456  C  CD2 . PHE B  1 95  ? -10.533 39.309 9.935   1.00 41.29 ? 95   PHE B CD2 1 
ATOM   6457  C  CE1 . PHE B  1 95  ? -10.239 40.366 7.372   1.00 40.82 ? 95   PHE B CE1 1 
ATOM   6458  C  CE2 . PHE B  1 95  ? -11.517 40.150 9.410   1.00 41.11 ? 95   PHE B CE2 1 
ATOM   6459  C  CZ  . PHE B  1 95  ? -11.368 40.678 8.125   1.00 40.79 ? 95   PHE B CZ  1 
ATOM   6460  N  N   . ASP B  1 96  ? -7.666  34.396 9.749   1.00 46.19 ? 96   ASP B N   1 
ATOM   6461  C  CA  . ASP B  1 96  ? -6.706  33.463 10.336  1.00 46.87 ? 96   ASP B CA  1 
ATOM   6462  C  C   . ASP B  1 96  ? -5.413  33.386 9.548   1.00 47.34 ? 96   ASP B C   1 
ATOM   6463  O  O   . ASP B  1 96  ? -4.437  32.771 10.000  1.00 47.92 ? 96   ASP B O   1 
ATOM   6464  C  CB  . ASP B  1 96  ? -7.300  32.058 10.451  1.00 47.62 ? 96   ASP B CB  1 
ATOM   6465  C  CG  . ASP B  1 96  ? -8.238  31.927 11.621  1.00 48.34 ? 96   ASP B CG  1 
ATOM   6466  O  OD1 . ASP B  1 96  ? -7.989  32.590 12.651  1.00 48.16 ? 96   ASP B OD1 1 
ATOM   6467  O  OD2 . ASP B  1 96  ? -9.211  31.150 11.519  1.00 49.94 ? 96   ASP B OD2 1 
ATOM   6468  N  N   . GLU B  1 97  ? -5.403  34.001 8.370   1.00 46.89 ? 97   GLU B N   1 
ATOM   6469  C  CA  . GLU B  1 97  ? -4.213  33.995 7.532   1.00 46.56 ? 97   GLU B CA  1 
ATOM   6470  C  C   . GLU B  1 97  ? -3.870  35.417 7.108   1.00 46.09 ? 97   GLU B C   1 
ATOM   6471  O  O   . GLU B  1 97  ? -3.101  35.636 6.160   1.00 45.16 ? 97   GLU B O   1 
ATOM   6472  C  CB  . GLU B  1 97  ? -4.445  33.090 6.318   1.00 47.98 ? 97   GLU B CB  1 
ATOM   6473  C  CG  . GLU B  1 97  ? -4.667  31.629 6.716   1.00 49.48 ? 97   GLU B CG  1 
ATOM   6474  C  CD  . GLU B  1 97  ? -5.580  30.885 5.750   1.00 51.43 ? 97   GLU B CD  1 
ATOM   6475  O  OE1 . GLU B  1 97  ? -6.080  29.786 6.115   1.00 51.50 ? 97   GLU B OE1 1 
ATOM   6476  O  OE2 . GLU B  1 97  ? -5.798  31.399 4.623   1.00 52.19 ? 97   GLU B OE2 1 
ATOM   6477  N  N   . PHE B  1 98  ? -4.449  36.379 7.829   1.00 45.25 ? 98   PHE B N   1 
ATOM   6478  C  CA  . PHE B  1 98  ? -4.210  37.795 7.567   1.00 44.49 ? 98   PHE B CA  1 
ATOM   6479  C  C   . PHE B  1 98  ? -2.706  38.050 7.617   1.00 43.95 ? 98   PHE B C   1 
ATOM   6480  O  O   . PHE B  1 98  ? -2.180  38.887 6.877   1.00 44.20 ? 98   PHE B O   1 
ATOM   6481  C  CB  . PHE B  1 98  ? -4.929  38.676 8.605   1.00 43.95 ? 98   PHE B CB  1 
ATOM   6482  C  CG  . PHE B  1 98  ? -4.747  40.151 8.373   1.00 42.97 ? 98   PHE B CG  1 
ATOM   6483  C  CD1 . PHE B  1 98  ? -5.211  40.748 7.199   1.00 42.50 ? 98   PHE B CD1 1 
ATOM   6484  C  CD2 . PHE B  1 98  ? -4.062  40.935 9.301   1.00 42.75 ? 98   PHE B CD2 1 
ATOM   6485  C  CE1 . PHE B  1 98  ? -4.991  42.106 6.949   1.00 42.10 ? 98   PHE B CE1 1 
ATOM   6486  C  CE2 . PHE B  1 98  ? -3.838  42.291 9.062   1.00 42.33 ? 98   PHE B CE2 1 
ATOM   6487  C  CZ  . PHE B  1 98  ? -4.301  42.881 7.882   1.00 41.88 ? 98   PHE B CZ  1 
ATOM   6488  N  N   . GLY B  1 99  ? -2.014  37.315 8.482   1.00 43.15 ? 99   GLY B N   1 
ATOM   6489  C  CA  . GLY B  1 99  ? -0.577  37.477 8.578   1.00 42.44 ? 99   GLY B CA  1 
ATOM   6490  C  C   . GLY B  1 99  ? -0.168  38.281 9.789   1.00 42.13 ? 99   GLY B C   1 
ATOM   6491  O  O   . GLY B  1 99  ? 1.017   38.390 10.097  1.00 42.50 ? 99   GLY B O   1 
ATOM   6492  N  N   . HIS B  1 100 ? -1.155  38.842 10.479  1.00 41.70 ? 100  HIS B N   1 
ATOM   6493  C  CA  . HIS B  1 100 ? -0.902  39.639 11.675  1.00 41.27 ? 100  HIS B CA  1 
ATOM   6494  C  C   . HIS B  1 100 ? -2.039  39.445 12.656  1.00 41.04 ? 100  HIS B C   1 
ATOM   6495  O  O   . HIS B  1 100 ? -3.130  39.016 12.284  1.00 40.93 ? 100  HIS B O   1 
ATOM   6496  C  CB  . HIS B  1 100 ? -0.818  41.120 11.317  1.00 40.68 ? 100  HIS B CB  1 
ATOM   6497  C  CG  . HIS B  1 100 ? 0.321   41.455 10.409  1.00 40.71 ? 100  HIS B CG  1 
ATOM   6498  N  ND1 . HIS B  1 100 ? 1.615   41.595 10.863  1.00 41.07 ? 100  HIS B ND1 1 
ATOM   6499  C  CD2 . HIS B  1 100 ? 0.364   41.677 9.074   1.00 40.55 ? 100  HIS B CD2 1 
ATOM   6500  C  CE1 . HIS B  1 100 ? 2.406   41.892 9.847   1.00 41.17 ? 100  HIS B CE1 1 
ATOM   6501  N  NE2 . HIS B  1 100 ? 1.672   41.948 8.750   1.00 40.68 ? 100  HIS B NE2 1 
ATOM   6502  N  N   . SER B  1 101 ? -1.789  39.773 13.914  1.00 40.85 ? 101  SER B N   1 
ATOM   6503  C  CA  . SER B  1 101 ? -2.835  39.650 14.906  1.00 41.00 ? 101  SER B CA  1 
ATOM   6504  C  C   . SER B  1 101 ? -3.560  40.994 14.958  1.00 40.24 ? 101  SER B C   1 
ATOM   6505  O  O   . SER B  1 101 ? -2.986  42.006 15.330  1.00 40.65 ? 101  SER B O   1 
ATOM   6506  C  CB  . SER B  1 101 ? -2.231  39.303 16.265  1.00 41.24 ? 101  SER B CB  1 
ATOM   6507  O  OG  . SER B  1 101 ? -3.269  39.040 17.191  1.00 43.01 ? 101  SER B OG  1 
ATOM   6508  N  N   . ILE B  1 102 ? -4.824  41.003 14.564  1.00 39.66 ? 102  ILE B N   1 
ATOM   6509  C  CA  . ILE B  1 102 ? -5.601  42.230 14.555  1.00 38.05 ? 102  ILE B CA  1 
ATOM   6510  C  C   . ILE B  1 102 ? -5.866  42.744 15.968  1.00 37.99 ? 102  ILE B C   1 
ATOM   6511  O  O   . ILE B  1 102 ? -6.524  42.077 16.773  1.00 38.21 ? 102  ILE B O   1 
ATOM   6512  C  CB  . ILE B  1 102 ? -6.920  42.000 13.801  1.00 37.46 ? 102  ILE B CB  1 
ATOM   6513  C  CG1 . ILE B  1 102 ? -6.594  41.638 12.340  1.00 36.46 ? 102  ILE B CG1 1 
ATOM   6514  C  CG2 . ILE B  1 102 ? -7.803  43.246 13.884  1.00 36.05 ? 102  ILE B CG2 1 
ATOM   6515  C  CD1 . ILE B  1 102 ? -7.772  41.150 11.542  1.00 35.48 ? 102  ILE B CD1 1 
ATOM   6516  N  N   . ASN B  1 103 ? -5.341  43.934 16.260  1.00 36.93 ? 103  ASN B N   1 
ATOM   6517  C  CA  . ASN B  1 103 ? -5.492  44.557 17.575  1.00 36.44 ? 103  ASN B CA  1 
ATOM   6518  C  C   . ASN B  1 103 ? -6.904  45.073 17.833  1.00 35.70 ? 103  ASN B C   1 
ATOM   6519  O  O   . ASN B  1 103 ? -7.397  45.016 18.951  1.00 35.40 ? 103  ASN B O   1 
ATOM   6520  C  CB  . ASN B  1 103 ? -4.512  45.723 17.734  1.00 36.46 ? 103  ASN B CB  1 
ATOM   6521  C  CG  . ASN B  1 103 ? -4.655  46.415 19.077  1.00 37.56 ? 103  ASN B CG  1 
ATOM   6522  O  OD1 . ASN B  1 103 ? -4.247  45.875 20.111  1.00 39.00 ? 103  ASN B OD1 1 
ATOM   6523  N  ND2 . ASN B  1 103 ? -5.252  47.597 19.075  1.00 36.30 ? 103  ASN B ND2 1 
ATOM   6524  N  N   . ASP B  1 104 ? -7.547  45.595 16.798  1.00 35.00 ? 104  ASP B N   1 
ATOM   6525  C  CA  . ASP B  1 104 ? -8.892  46.119 16.949  1.00 34.87 ? 104  ASP B CA  1 
ATOM   6526  C  C   . ASP B  1 104 ? -9.503  46.299 15.568  1.00 34.31 ? 104  ASP B C   1 
ATOM   6527  O  O   . ASP B  1 104 ? -8.807  46.245 14.555  1.00 33.78 ? 104  ASP B O   1 
ATOM   6528  C  CB  . ASP B  1 104 ? -8.859  47.465 17.677  1.00 35.76 ? 104  ASP B CB  1 
ATOM   6529  C  CG  . ASP B  1 104 ? -10.160 47.782 18.370  1.00 36.70 ? 104  ASP B CG  1 
ATOM   6530  O  OD1 . ASP B  1 104 ? -11.174 47.129 18.053  1.00 37.99 ? 104  ASP B OD1 1 
ATOM   6531  O  OD2 . ASP B  1 104 ? -10.173 48.689 19.230  1.00 37.08 ? 104  ASP B OD2 1 
ATOM   6532  N  N   . TYR B  1 105 ? -10.806 46.521 15.530  1.00 34.09 ? 105  TYR B N   1 
ATOM   6533  C  CA  . TYR B  1 105 ? -11.489 46.692 14.264  1.00 34.77 ? 105  TYR B CA  1 
ATOM   6534  C  C   . TYR B  1 105 ? -12.436 47.866 14.349  1.00 34.39 ? 105  TYR B C   1 
ATOM   6535  O  O   . TYR B  1 105 ? -12.681 48.407 15.428  1.00 34.87 ? 105  TYR B O   1 
ATOM   6536  C  CB  . TYR B  1 105 ? -12.279 45.433 13.917  1.00 36.98 ? 105  TYR B CB  1 
ATOM   6537  C  CG  . TYR B  1 105 ? -13.429 45.170 14.861  1.00 38.97 ? 105  TYR B CG  1 
ATOM   6538  C  CD1 . TYR B  1 105 ? -13.228 44.529 16.090  1.00 40.10 ? 105  TYR B CD1 1 
ATOM   6539  C  CD2 . TYR B  1 105 ? -14.724 45.574 14.534  1.00 39.19 ? 105  TYR B CD2 1 
ATOM   6540  C  CE1 . TYR B  1 105 ? -14.303 44.296 16.972  1.00 41.03 ? 105  TYR B CE1 1 
ATOM   6541  C  CE2 . TYR B  1 105 ? -15.800 45.348 15.408  1.00 40.32 ? 105  TYR B CE2 1 
ATOM   6542  C  CZ  . TYR B  1 105 ? -15.584 44.711 16.619  1.00 40.71 ? 105  TYR B CZ  1 
ATOM   6543  O  OH  . TYR B  1 105 ? -16.651 44.492 17.470  1.00 42.05 ? 105  TYR B OH  1 
ATOM   6544  N  N   . SER B  1 106 ? -12.982 48.258 13.209  1.00 33.02 ? 106  SER B N   1 
ATOM   6545  C  CA  . SER B  1 106 ? -13.901 49.378 13.183  1.00 31.77 ? 106  SER B CA  1 
ATOM   6546  C  C   . SER B  1 106 ? -14.711 49.362 11.897  1.00 30.55 ? 106  SER B C   1 
ATOM   6547  O  O   . SER B  1 106 ? -14.166 49.473 10.805  1.00 29.75 ? 106  SER B O   1 
ATOM   6548  C  CB  . SER B  1 106 ? -13.108 50.682 13.299  1.00 32.73 ? 106  SER B CB  1 
ATOM   6549  O  OG  . SER B  1 106 ? -13.959 51.793 13.138  1.00 34.06 ? 106  SER B OG  1 
ATOM   6550  N  N   . ILE B  1 107 ? -16.022 49.233 12.031  1.00 30.78 ? 107  ILE B N   1 
ATOM   6551  C  CA  . ILE B  1 107 ? -16.887 49.196 10.870  1.00 29.96 ? 107  ILE B CA  1 
ATOM   6552  C  C   . ILE B  1 107 ? -17.325 50.597 10.487  1.00 29.02 ? 107  ILE B C   1 
ATOM   6553  O  O   . ILE B  1 107 ? -17.671 51.408 11.348  1.00 29.16 ? 107  ILE B O   1 
ATOM   6554  C  CB  . ILE B  1 107 ? -18.137 48.314 11.135  1.00 30.98 ? 107  ILE B CB  1 
ATOM   6555  C  CG1 . ILE B  1 107 ? -17.714 46.856 11.288  1.00 31.83 ? 107  ILE B CG1 1 
ATOM   6556  C  CG2 . ILE B  1 107 ? -19.124 48.418 9.987   1.00 30.43 ? 107  ILE B CG2 1 
ATOM   6557  C  CD1 . ILE B  1 107 ? -17.337 46.492 12.694  1.00 33.49 ? 107  ILE B CD1 1 
ATOM   6558  N  N   . SER B  1 108 ? -17.288 50.885 9.192   1.00 27.29 ? 108  SER B N   1 
ATOM   6559  C  CA  . SER B  1 108 ? -17.701 52.187 8.714   1.00 26.64 ? 108  SER B CA  1 
ATOM   6560  C  C   . SER B  1 108 ? -19.170 52.349 9.085   1.00 27.55 ? 108  SER B C   1 
ATOM   6561  O  O   . SER B  1 108 ? -19.888 51.366 9.267   1.00 28.17 ? 108  SER B O   1 
ATOM   6562  C  CB  . SER B  1 108 ? -17.518 52.291 7.196   1.00 25.82 ? 108  SER B CB  1 
ATOM   6563  O  OG  . SER B  1 108 ? -18.352 51.377 6.489   1.00 24.52 ? 108  SER B OG  1 
ATOM   6564  N  N   . PRO B  1 109 ? -19.633 53.593 9.217   1.00 27.85 ? 109  PRO B N   1 
ATOM   6565  C  CA  . PRO B  1 109 ? -21.022 53.892 9.574   1.00 28.55 ? 109  PRO B CA  1 
ATOM   6566  C  C   . PRO B  1 109 ? -22.083 53.210 8.715   1.00 29.34 ? 109  PRO B C   1 
ATOM   6567  O  O   . PRO B  1 109 ? -23.145 52.852 9.214   1.00 29.72 ? 109  PRO B O   1 
ATOM   6568  C  CB  . PRO B  1 109 ? -21.076 55.410 9.448   1.00 29.07 ? 109  PRO B CB  1 
ATOM   6569  C  CG  . PRO B  1 109 ? -19.724 55.799 9.943   1.00 28.83 ? 109  PRO B CG  1 
ATOM   6570  C  CD  . PRO B  1 109 ? -18.813 54.817 9.240   1.00 27.44 ? 109  PRO B CD  1 
ATOM   6571  N  N   . ASP B  1 110 ? -21.809 53.048 7.426   1.00 29.27 ? 110  ASP B N   1 
ATOM   6572  C  CA  . ASP B  1 110 ? -22.782 52.429 6.540   1.00 29.29 ? 110  ASP B CA  1 
ATOM   6573  C  C   . ASP B  1 110 ? -22.647 50.923 6.462   1.00 29.44 ? 110  ASP B C   1 
ATOM   6574  O  O   . ASP B  1 110 ? -23.263 50.284 5.610   1.00 29.76 ? 110  ASP B O   1 
ATOM   6575  C  CB  . ASP B  1 110 ? -22.693 53.034 5.134   1.00 29.52 ? 110  ASP B CB  1 
ATOM   6576  C  CG  . ASP B  1 110 ? -21.333 52.829 4.481   1.00 29.74 ? 110  ASP B CG  1 
ATOM   6577  O  OD1 . ASP B  1 110 ? -21.117 53.404 3.391   1.00 30.49 ? 110  ASP B OD1 1 
ATOM   6578  O  OD2 . ASP B  1 110 ? -20.487 52.100 5.038   1.00 30.45 ? 110  ASP B OD2 1 
ATOM   6579  N  N   . GLY B  1 111 ? -21.842 50.357 7.354   1.00 29.14 ? 111  GLY B N   1 
ATOM   6580  C  CA  . GLY B  1 111 ? -21.643 48.920 7.365   1.00 28.38 ? 111  GLY B CA  1 
ATOM   6581  C  C   . GLY B  1 111 ? -21.033 48.309 6.108   1.00 29.41 ? 111  GLY B C   1 
ATOM   6582  O  O   . GLY B  1 111 ? -21.051 47.094 5.959   1.00 29.37 ? 111  GLY B O   1 
ATOM   6583  N  N   . GLN B  1 112 ? -20.470 49.113 5.207   1.00 28.86 ? 112  GLN B N   1 
ATOM   6584  C  CA  . GLN B  1 112 ? -19.887 48.544 3.983   1.00 28.61 ? 112  GLN B CA  1 
ATOM   6585  C  C   . GLN B  1 112 ? -18.422 48.117 4.057   1.00 28.58 ? 112  GLN B C   1 
ATOM   6586  O  O   . GLN B  1 112 ? -17.966 47.293 3.258   1.00 28.17 ? 112  GLN B O   1 
ATOM   6587  C  CB  . GLN B  1 112 ? -20.046 49.526 2.823   1.00 29.52 ? 112  GLN B CB  1 
ATOM   6588  C  CG  . GLN B  1 112 ? -21.407 49.479 2.172   1.00 30.79 ? 112  GLN B CG  1 
ATOM   6589  C  CD  . GLN B  1 112 ? -21.653 50.670 1.278   1.00 32.38 ? 112  GLN B CD  1 
ATOM   6590  O  OE1 . GLN B  1 112 ? -20.757 51.118 0.555   1.00 32.18 ? 112  GLN B OE1 1 
ATOM   6591  N  NE2 . GLN B  1 112 ? -22.877 51.190 1.315   1.00 32.62 ? 112  GLN B NE2 1 
ATOM   6592  N  N   . PHE B  1 113 ? -17.686 48.666 5.017   1.00 27.21 ? 113  PHE B N   1 
ATOM   6593  C  CA  . PHE B  1 113 ? -16.267 48.366 5.150   1.00 26.84 ? 113  PHE B CA  1 
ATOM   6594  C  C   . PHE B  1 113 ? -15.874 48.166 6.610   1.00 27.32 ? 113  PHE B C   1 
ATOM   6595  O  O   . PHE B  1 113 ? -16.587 48.591 7.526   1.00 27.07 ? 113  PHE B O   1 
ATOM   6596  C  CB  . PHE B  1 113 ? -15.446 49.524 4.565   1.00 25.77 ? 113  PHE B CB  1 
ATOM   6597  C  CG  . PHE B  1 113 ? -15.670 49.751 3.097   1.00 25.52 ? 113  PHE B CG  1 
ATOM   6598  C  CD1 . PHE B  1 113 ? -14.933 49.050 2.152   1.00 25.57 ? 113  PHE B CD1 1 
ATOM   6599  C  CD2 . PHE B  1 113 ? -16.648 50.632 2.662   1.00 26.12 ? 113  PHE B CD2 1 
ATOM   6600  C  CE1 . PHE B  1 113 ? -15.163 49.223 0.787   1.00 26.78 ? 113  PHE B CE1 1 
ATOM   6601  C  CE2 . PHE B  1 113 ? -16.897 50.815 1.293   1.00 27.03 ? 113  PHE B CE2 1 
ATOM   6602  C  CZ  . PHE B  1 113 ? -16.149 50.106 0.354   1.00 26.50 ? 113  PHE B CZ  1 
ATOM   6603  N  N   . ILE B  1 114 ? -14.745 47.505 6.832   1.00 27.61 ? 114  ILE B N   1 
ATOM   6604  C  CA  . ILE B  1 114 ? -14.276 47.310 8.197   1.00 29.20 ? 114  ILE B CA  1 
ATOM   6605  C  C   . ILE B  1 114 ? -12.808 47.705 8.246   1.00 29.03 ? 114  ILE B C   1 
ATOM   6606  O  O   . ILE B  1 114 ? -12.028 47.325 7.384   1.00 29.72 ? 114  ILE B O   1 
ATOM   6607  C  CB  . ILE B  1 114 ? -14.474 45.846 8.681   1.00 30.74 ? 114  ILE B CB  1 
ATOM   6608  C  CG1 . ILE B  1 114 ? -13.846 45.663 10.063  1.00 31.53 ? 114  ILE B CG1 1 
ATOM   6609  C  CG2 . ILE B  1 114 ? -13.889 44.879 7.687   1.00 30.58 ? 114  ILE B CG2 1 
ATOM   6610  C  CD1 . ILE B  1 114 ? -14.192 44.323 10.708  1.00 34.27 ? 114  ILE B CD1 1 
ATOM   6611  N  N   . LEU B  1 115 ? -12.451 48.506 9.240   1.00 28.67 ? 115  LEU B N   1 
ATOM   6612  C  CA  . LEU B  1 115 ? -11.084 48.979 9.391   1.00 28.76 ? 115  LEU B CA  1 
ATOM   6613  C  C   . LEU B  1 115 ? -10.366 48.020 10.325  1.00 28.67 ? 115  LEU B C   1 
ATOM   6614  O  O   . LEU B  1 115 ? -10.795 47.820 11.459  1.00 28.71 ? 115  LEU B O   1 
ATOM   6615  C  CB  . LEU B  1 115 ? -11.093 50.397 9.983   1.00 27.59 ? 115  LEU B CB  1 
ATOM   6616  C  CG  . LEU B  1 115 ? -9.767  51.150 10.099  1.00 27.94 ? 115  LEU B CG  1 
ATOM   6617  C  CD1 . LEU B  1 115 ? -9.312  51.582 8.721   1.00 28.05 ? 115  LEU B CD1 1 
ATOM   6618  C  CD2 . LEU B  1 115 ? -9.932  52.364 10.986  1.00 26.98 ? 115  LEU B CD2 1 
ATOM   6619  N  N   . LEU B  1 116 ? -9.279  47.426 9.850   1.00 28.34 ? 116  LEU B N   1 
ATOM   6620  C  CA  . LEU B  1 116 ? -8.532  46.479 10.662  1.00 28.15 ? 116  LEU B CA  1 
ATOM   6621  C  C   . LEU B  1 116 ? -7.295  47.169 11.187  1.00 28.23 ? 116  LEU B C   1 
ATOM   6622  O  O   . LEU B  1 116 ? -6.517  47.751 10.425  1.00 28.42 ? 116  LEU B O   1 
ATOM   6623  C  CB  . LEU B  1 116 ? -8.128  45.257 9.831   1.00 27.88 ? 116  LEU B CB  1 
ATOM   6624  C  CG  . LEU B  1 116 ? -9.251  44.435 9.179   1.00 28.81 ? 116  LEU B CG  1 
ATOM   6625  C  CD1 . LEU B  1 116 ? -8.621  43.243 8.462   1.00 30.36 ? 116  LEU B CD1 1 
ATOM   6626  C  CD2 . LEU B  1 116 ? -10.250 43.948 10.237  1.00 27.68 ? 116  LEU B CD2 1 
ATOM   6627  N  N   . GLU B  1 117 ? -7.102  47.098 12.493  1.00 27.68 ? 117  GLU B N   1 
ATOM   6628  C  CA  . GLU B  1 117 ? -5.955  47.746 13.106  1.00 28.21 ? 117  GLU B CA  1 
ATOM   6629  C  C   . GLU B  1 117 ? -4.962  46.721 13.645  1.00 28.57 ? 117  GLU B C   1 
ATOM   6630  O  O   . GLU B  1 117 ? -5.340  45.805 14.370  1.00 29.58 ? 117  GLU B O   1 
ATOM   6631  C  CB  . GLU B  1 117 ? -6.471  48.677 14.216  1.00 27.63 ? 117  GLU B CB  1 
ATOM   6632  C  CG  . GLU B  1 117 ? -5.428  49.346 15.056  1.00 28.13 ? 117  GLU B CG  1 
ATOM   6633  C  CD  . GLU B  1 117 ? -6.054  50.122 16.198  1.00 28.93 ? 117  GLU B CD  1 
ATOM   6634  O  OE1 . GLU B  1 117 ? -6.622  51.198 15.934  1.00 29.54 ? 117  GLU B OE1 1 
ATOM   6635  O  OE2 . GLU B  1 117 ? -5.997  49.652 17.354  1.00 29.57 ? 117  GLU B OE2 1 
ATOM   6636  N  N   . TYR B  1 118 ? -3.692  46.863 13.279  1.00 29.27 ? 118  TYR B N   1 
ATOM   6637  C  CA  . TYR B  1 118 ? -2.664  45.937 13.755  1.00 29.22 ? 118  TYR B CA  1 
ATOM   6638  C  C   . TYR B  1 118 ? -1.313  46.636 13.914  1.00 30.31 ? 118  TYR B C   1 
ATOM   6639  O  O   . TYR B  1 118 ? -1.157  47.789 13.528  1.00 31.11 ? 118  TYR B O   1 
ATOM   6640  C  CB  . TYR B  1 118 ? -2.534  44.734 12.800  1.00 28.09 ? 118  TYR B CB  1 
ATOM   6641  C  CG  . TYR B  1 118 ? -2.154  45.081 11.374  1.00 27.75 ? 118  TYR B CG  1 
ATOM   6642  C  CD1 . TYR B  1 118 ? -3.073  45.672 10.501  1.00 27.43 ? 118  TYR B CD1 1 
ATOM   6643  C  CD2 . TYR B  1 118 ? -0.873  44.804 10.894  1.00 26.92 ? 118  TYR B CD2 1 
ATOM   6644  C  CE1 . TYR B  1 118 ? -2.716  45.975 9.182   1.00 26.93 ? 118  TYR B CE1 1 
ATOM   6645  C  CE2 . TYR B  1 118 ? -0.512  45.097 9.591   1.00 26.71 ? 118  TYR B CE2 1 
ATOM   6646  C  CZ  . TYR B  1 118 ? -1.426  45.677 8.737   1.00 27.85 ? 118  TYR B CZ  1 
ATOM   6647  O  OH  . TYR B  1 118 ? -1.043  45.943 7.438   1.00 28.25 ? 118  TYR B OH  1 
ATOM   6648  N  N   . ASN B  1 119 ? -0.335  45.933 14.472  1.00 31.36 ? 119  ASN B N   1 
ATOM   6649  C  CA  . ASN B  1 119 ? 0.984   46.511 14.690  1.00 32.40 ? 119  ASN B CA  1 
ATOM   6650  C  C   . ASN B  1 119 ? 0.844   47.665 15.676  1.00 31.95 ? 119  ASN B C   1 
ATOM   6651  O  O   . ASN B  1 119 ? 1.569   48.655 15.605  1.00 31.94 ? 119  ASN B O   1 
ATOM   6652  C  CB  . ASN B  1 119 ? 1.592   47.024 13.378  1.00 33.58 ? 119  ASN B CB  1 
ATOM   6653  C  CG  . ASN B  1 119 ? 2.210   45.908 12.541  1.00 35.59 ? 119  ASN B CG  1 
ATOM   6654  O  OD1 . ASN B  1 119 ? 2.677   44.893 13.081  1.00 35.74 ? 119  ASN B OD1 1 
ATOM   6655  N  ND2 . ASN B  1 119 ? 2.243   46.101 11.221  1.00 33.90 ? 119  ASN B ND2 1 
ATOM   6656  N  N   . TYR B  1 120 ? -0.107  47.522 16.588  1.00 31.64 ? 120  TYR B N   1 
ATOM   6657  C  CA  . TYR B  1 120 ? -0.377  48.521 17.604  1.00 31.16 ? 120  TYR B CA  1 
ATOM   6658  C  C   . TYR B  1 120 ? 0.830   48.843 18.463  1.00 30.92 ? 120  TYR B C   1 
ATOM   6659  O  O   . TYR B  1 120 ? 1.407   47.967 19.097  1.00 30.14 ? 120  TYR B O   1 
ATOM   6660  C  CB  . TYR B  1 120 ? -1.504  48.046 18.510  1.00 30.30 ? 120  TYR B CB  1 
ATOM   6661  C  CG  . TYR B  1 120 ? -1.649  48.859 19.772  1.00 31.28 ? 120  TYR B CG  1 
ATOM   6662  C  CD1 . TYR B  1 120 ? -2.442  50.010 19.808  1.00 30.91 ? 120  TYR B CD1 1 
ATOM   6663  C  CD2 . TYR B  1 120 ? -1.016  48.456 20.945  1.00 31.35 ? 120  TYR B CD2 1 
ATOM   6664  C  CE1 . TYR B  1 120 ? -2.607  50.742 21.007  1.00 31.04 ? 120  TYR B CE1 1 
ATOM   6665  C  CE2 . TYR B  1 120 ? -1.168  49.175 22.141  1.00 32.49 ? 120  TYR B CE2 1 
ATOM   6666  C  CZ  . TYR B  1 120 ? -1.965  50.314 22.167  1.00 31.59 ? 120  TYR B CZ  1 
ATOM   6667  O  OH  . TYR B  1 120 ? -2.101  50.999 23.361  1.00 32.19 ? 120  TYR B OH  1 
ATOM   6668  N  N   . VAL B  1 121 ? 1.196   50.115 18.492  1.00 30.41 ? 121  VAL B N   1 
ATOM   6669  C  CA  . VAL B  1 121 ? 2.318   50.559 19.302  1.00 30.31 ? 121  VAL B CA  1 
ATOM   6670  C  C   . VAL B  1 121 ? 1.871   51.747 20.163  1.00 29.04 ? 121  VAL B C   1 
ATOM   6671  O  O   . VAL B  1 121 ? 1.713   52.867 19.671  1.00 28.67 ? 121  VAL B O   1 
ATOM   6672  C  CB  . VAL B  1 121 ? 3.493   51.007 18.420  1.00 31.79 ? 121  VAL B CB  1 
ATOM   6673  C  CG1 . VAL B  1 121 ? 4.717   51.290 19.308  1.00 32.49 ? 121  VAL B CG1 1 
ATOM   6674  C  CG2 . VAL B  1 121 ? 3.802   49.930 17.363  1.00 33.03 ? 121  VAL B CG2 1 
ATOM   6675  N  N   . LYS B  1 122 ? 1.662   51.493 21.444  1.00 27.65 ? 122  LYS B N   1 
ATOM   6676  C  CA  . LYS B  1 122 ? 1.229   52.528 22.362  1.00 26.48 ? 122  LYS B CA  1 
ATOM   6677  C  C   . LYS B  1 122 ? 2.179   53.707 22.470  1.00 25.68 ? 122  LYS B C   1 
ATOM   6678  O  O   . LYS B  1 122 ? 3.405   53.550 22.388  1.00 24.26 ? 122  LYS B O   1 
ATOM   6679  C  CB  . LYS B  1 122 ? 1.049   51.957 23.771  1.00 26.42 ? 122  LYS B CB  1 
ATOM   6680  C  CG  . LYS B  1 122 ? 0.802   53.041 24.829  1.00 25.35 ? 122  LYS B CG  1 
ATOM   6681  C  CD  . LYS B  1 122 ? 0.597   52.467 26.216  1.00 25.18 ? 122  LYS B CD  1 
ATOM   6682  C  CE  . LYS B  1 122 ? 0.231   53.559 27.232  1.00 24.47 ? 122  LYS B CE  1 
ATOM   6683  N  NZ  . LYS B  1 122 ? 1.285   54.615 27.363  1.00 23.83 ? 122  LYS B NZ  1 
ATOM   6684  N  N   . GLN B  1 123 ? 1.608   54.895 22.633  1.00 23.22 ? 123  GLN B N   1 
ATOM   6685  C  CA  . GLN B  1 123 ? 2.434   56.070 22.848  1.00 21.41 ? 123  GLN B CA  1 
ATOM   6686  C  C   . GLN B  1 123 ? 2.068   56.620 24.237  1.00 19.80 ? 123  GLN B C   1 
ATOM   6687  O  O   . GLN B  1 123 ? 2.529   56.082 25.242  1.00 18.79 ? 123  GLN B O   1 
ATOM   6688  C  CB  . GLN B  1 123 ? 2.246   57.147 21.769  1.00 21.81 ? 123  GLN B CB  1 
ATOM   6689  C  CG  . GLN B  1 123 ? 3.014   58.389 22.154  1.00 23.15 ? 123  GLN B CG  1 
ATOM   6690  C  CD  . GLN B  1 123 ? 3.145   59.408 21.046  1.00 26.03 ? 123  GLN B CD  1 
ATOM   6691  O  OE1 . GLN B  1 123 ? 4.165   59.461 20.358  1.00 27.09 ? 123  GLN B OE1 1 
ATOM   6692  N  NE2 . GLN B  1 123 ? 2.124   60.239 20.880  1.00 22.67 ? 123  GLN B NE2 1 
ATOM   6693  N  N   . TRP B  1 124 ? 1.226   57.650 24.327  1.00 17.92 ? 124  TRP B N   1 
ATOM   6694  C  CA  . TRP B  1 124 ? 0.916   58.157 25.658  1.00 16.86 ? 124  TRP B CA  1 
ATOM   6695  C  C   . TRP B  1 124 ? -0.362  57.540 26.232  1.00 17.14 ? 124  TRP B C   1 
ATOM   6696  O  O   . TRP B  1 124 ? -0.612  56.346 26.035  1.00 16.47 ? 124  TRP B O   1 
ATOM   6697  C  CB  . TRP B  1 124 ? 0.871   59.699 25.664  1.00 15.71 ? 124  TRP B CB  1 
ATOM   6698  C  CG  . TRP B  1 124 ? 2.060   60.357 24.967  1.00 13.64 ? 124  TRP B CG  1 
ATOM   6699  C  CD1 . TRP B  1 124 ? 2.005   61.349 24.009  1.00 13.21 ? 124  TRP B CD1 1 
ATOM   6700  C  CD2 . TRP B  1 124 ? 3.458   60.051 25.139  1.00 13.75 ? 124  TRP B CD2 1 
ATOM   6701  N  NE1 . TRP B  1 124 ? 3.276   61.666 23.575  1.00 13.44 ? 124  TRP B NE1 1 
ATOM   6702  C  CE2 . TRP B  1 124 ? 4.185   60.889 24.246  1.00 14.31 ? 124  TRP B CE2 1 
ATOM   6703  C  CE3 . TRP B  1 124 ? 4.165   59.155 25.954  1.00 13.76 ? 124  TRP B CE3 1 
ATOM   6704  C  CZ2 . TRP B  1 124 ? 5.585   60.851 24.147  1.00 14.94 ? 124  TRP B CZ2 1 
ATOM   6705  C  CZ3 . TRP B  1 124 ? 5.565   59.119 25.859  1.00 13.49 ? 124  TRP B CZ3 1 
ATOM   6706  C  CH2 . TRP B  1 124 ? 6.256   59.963 24.959  1.00 14.91 ? 124  TRP B CH2 1 
ATOM   6707  N  N   . ARG B  1 125 ? -1.175  58.322 26.939  1.00 16.97 ? 125  ARG B N   1 
ATOM   6708  C  CA  . ARG B  1 125 ? -2.366  57.748 27.528  1.00 17.05 ? 125  ARG B CA  1 
ATOM   6709  C  C   . ARG B  1 125 ? -3.402  57.334 26.483  1.00 17.30 ? 125  ARG B C   1 
ATOM   6710  O  O   . ARG B  1 125 ? -4.047  56.299 26.632  1.00 17.00 ? 125  ARG B O   1 
ATOM   6711  C  CB  . ARG B  1 125 ? -2.999  58.710 28.534  1.00 15.73 ? 125  ARG B CB  1 
ATOM   6712  C  CG  . ARG B  1 125 ? -4.102  58.068 29.391  1.00 16.17 ? 125  ARG B CG  1 
ATOM   6713  C  CD  . ARG B  1 125 ? -4.846  59.110 30.243  1.00 16.49 ? 125  ARG B CD  1 
ATOM   6714  N  NE  . ARG B  1 125 ? -3.994  59.798 31.223  1.00 15.80 ? 125  ARG B NE  1 
ATOM   6715  C  CZ  . ARG B  1 125 ? -3.769  59.371 32.463  1.00 18.62 ? 125  ARG B CZ  1 
ATOM   6716  N  NH1 . ARG B  1 125 ? -4.324  58.236 32.903  1.00 18.03 ? 125  ARG B NH1 1 
ATOM   6717  N  NH2 . ARG B  1 125 ? -3.024  60.100 33.283  1.00 17.04 ? 125  ARG B NH2 1 
ATOM   6718  N  N   . HIS B  1 126 ? -3.560  58.141 25.439  1.00 17.61 ? 126  HIS B N   1 
ATOM   6719  C  CA  . HIS B  1 126 ? -4.527  57.862 24.392  1.00 17.52 ? 126  HIS B CA  1 
ATOM   6720  C  C   . HIS B  1 126 ? -3.885  57.582 23.036  1.00 18.06 ? 126  HIS B C   1 
ATOM   6721  O  O   . HIS B  1 126 ? -4.403  56.806 22.226  1.00 17.97 ? 126  HIS B O   1 
ATOM   6722  C  CB  . HIS B  1 126 ? -5.462  59.067 24.252  1.00 19.54 ? 126  HIS B CB  1 
ATOM   6723  C  CG  . HIS B  1 126 ? -6.034  59.539 25.554  1.00 21.24 ? 126  HIS B CG  1 
ATOM   6724  N  ND1 . HIS B  1 126 ? -7.000  58.833 26.239  1.00 21.40 ? 126  HIS B ND1 1 
ATOM   6725  C  CD2 . HIS B  1 126 ? -5.767  60.636 26.303  1.00 20.02 ? 126  HIS B CD2 1 
ATOM   6726  C  CE1 . HIS B  1 126 ? -7.304  59.477 27.354  1.00 20.85 ? 126  HIS B CE1 1 
ATOM   6727  N  NE2 . HIS B  1 126 ? -6.570  60.573 27.416  1.00 20.81 ? 126  HIS B NE2 1 
ATOM   6728  N  N   . SER B  1 127 ? -2.762  58.237 22.766  1.00 18.04 ? 127  SER B N   1 
ATOM   6729  C  CA  . SER B  1 127 ? -2.115  58.069 21.473  1.00 17.38 ? 127  SER B CA  1 
ATOM   6730  C  C   . SER B  1 127 ? -1.421  56.723 21.283  1.00 19.17 ? 127  SER B C   1 
ATOM   6731  O  O   . SER B  1 127 ? -1.054  56.050 22.254  1.00 18.24 ? 127  SER B O   1 
ATOM   6732  C  CB  . SER B  1 127 ? -1.097  59.201 21.247  1.00 17.28 ? 127  SER B CB  1 
ATOM   6733  O  OG  . SER B  1 127 ? -0.184  59.290 22.334  1.00 13.42 ? 127  SER B OG  1 
ATOM   6734  N  N   . TYR B  1 128 ? -1.250  56.354 20.012  1.00 19.99 ? 128  TYR B N   1 
ATOM   6735  C  CA  . TYR B  1 128 ? -0.567  55.125 19.609  1.00 21.67 ? 128  TYR B CA  1 
ATOM   6736  C  C   . TYR B  1 128 ? -0.414  55.100 18.083  1.00 22.73 ? 128  TYR B C   1 
ATOM   6737  O  O   . TYR B  1 128 ? -1.068  55.859 17.369  1.00 22.33 ? 128  TYR B O   1 
ATOM   6738  C  CB  . TYR B  1 128 ? -1.345  53.892 20.091  1.00 22.20 ? 128  TYR B CB  1 
ATOM   6739  C  CG  . TYR B  1 128 ? -2.701  53.693 19.446  1.00 23.66 ? 128  TYR B CG  1 
ATOM   6740  C  CD1 . TYR B  1 128 ? -2.817  53.194 18.143  1.00 24.64 ? 128  TYR B CD1 1 
ATOM   6741  C  CD2 . TYR B  1 128 ? -3.869  53.980 20.144  1.00 23.89 ? 128  TYR B CD2 1 
ATOM   6742  C  CE1 . TYR B  1 128 ? -4.074  52.983 17.557  1.00 24.40 ? 128  TYR B CE1 1 
ATOM   6743  C  CE2 . TYR B  1 128 ? -5.128  53.776 19.573  1.00 24.74 ? 128  TYR B CE2 1 
ATOM   6744  C  CZ  . TYR B  1 128 ? -5.223  53.277 18.284  1.00 26.38 ? 128  TYR B CZ  1 
ATOM   6745  O  OH  . TYR B  1 128 ? -6.466  53.070 17.729  1.00 25.70 ? 128  TYR B OH  1 
ATOM   6746  N  N   . THR B  1 129 ? 0.485   54.270 17.580  1.00 23.73 ? 129  THR B N   1 
ATOM   6747  C  CA  . THR B  1 129 ? 0.634   54.160 16.132  1.00 26.35 ? 129  THR B CA  1 
ATOM   6748  C  C   . THR B  1 129 ? 0.271   52.733 15.747  1.00 26.43 ? 129  THR B C   1 
ATOM   6749  O  O   . THR B  1 129 ? 0.353   51.819 16.568  1.00 25.29 ? 129  THR B O   1 
ATOM   6750  C  CB  . THR B  1 129 ? 2.074   54.435 15.646  1.00 26.98 ? 129  THR B CB  1 
ATOM   6751  O  OG1 . THR B  1 129 ? 2.999   53.717 16.473  1.00 28.80 ? 129  THR B OG1 1 
ATOM   6752  C  CG2 . THR B  1 129 ? 2.382   55.934 15.678  1.00 26.70 ? 129  THR B CG2 1 
ATOM   6753  N  N   . ALA B  1 130 ? -0.128  52.545 14.497  1.00 27.51 ? 130  ALA B N   1 
ATOM   6754  C  CA  . ALA B  1 130 ? -0.506  51.218 14.056  1.00 28.86 ? 130  ALA B CA  1 
ATOM   6755  C  C   . ALA B  1 130 ? -0.647  51.153 12.557  1.00 29.07 ? 130  ALA B C   1 
ATOM   6756  O  O   . ALA B  1 130 ? -0.690  52.183 11.879  1.00 29.92 ? 130  ALA B O   1 
ATOM   6757  C  CB  . ALA B  1 130 ? -1.827  50.825 14.707  1.00 28.20 ? 130  ALA B CB  1 
ATOM   6758  N  N   . SER B  1 131 ? -0.709  49.928 12.043  1.00 28.74 ? 131  SER B N   1 
ATOM   6759  C  CA  . SER B  1 131 ? -0.919  49.709 10.613  1.00 29.19 ? 131  SER B CA  1 
ATOM   6760  C  C   . SER B  1 131 ? -2.414  49.463 10.452  1.00 28.67 ? 131  SER B C   1 
ATOM   6761  O  O   . SER B  1 131 ? -3.091  49.037 11.390  1.00 27.98 ? 131  SER B O   1 
ATOM   6762  C  CB  . SER B  1 131 ? -0.139  48.485 10.114  1.00 29.18 ? 131  SER B CB  1 
ATOM   6763  O  OG  . SER B  1 131 ? 1.249   48.712 10.193  1.00 29.57 ? 131  SER B OG  1 
ATOM   6764  N  N   . TYR B  1 132 ? -2.923  49.729 9.263   1.00 28.49 ? 132  TYR B N   1 
ATOM   6765  C  CA  . TYR B  1 132 ? -4.332  49.547 9.012   1.00 29.19 ? 132  TYR B CA  1 
ATOM   6766  C  C   . TYR B  1 132 ? -4.585  48.961 7.629   1.00 30.31 ? 132  TYR B C   1 
ATOM   6767  O  O   . TYR B  1 132 ? -3.847  49.218 6.680   1.00 31.13 ? 132  TYR B O   1 
ATOM   6768  C  CB  . TYR B  1 132 ? -5.077  50.895 9.100   1.00 28.61 ? 132  TYR B CB  1 
ATOM   6769  C  CG  . TYR B  1 132 ? -4.969  51.614 10.431  1.00 28.53 ? 132  TYR B CG  1 
ATOM   6770  C  CD1 . TYR B  1 132 ? -3.845  52.376 10.753  1.00 28.30 ? 132  TYR B CD1 1 
ATOM   6771  C  CD2 . TYR B  1 132 ? -5.978  51.496 11.384  1.00 28.46 ? 132  TYR B CD2 1 
ATOM   6772  C  CE1 . TYR B  1 132 ? -3.731  52.995 11.998  1.00 28.40 ? 132  TYR B CE1 1 
ATOM   6773  C  CE2 . TYR B  1 132 ? -5.874  52.103 12.619  1.00 27.85 ? 132  TYR B CE2 1 
ATOM   6774  C  CZ  . TYR B  1 132 ? -4.752  52.844 12.925  1.00 28.40 ? 132  TYR B CZ  1 
ATOM   6775  O  OH  . TYR B  1 132 ? -4.628  53.397 14.176  1.00 29.12 ? 132  TYR B OH  1 
ATOM   6776  N  N   . ASP B  1 133 ? -5.640  48.173 7.522   1.00 30.47 ? 133  ASP B N   1 
ATOM   6777  C  CA  . ASP B  1 133 ? -6.043  47.630 6.244   1.00 31.06 ? 133  ASP B CA  1 
ATOM   6778  C  C   . ASP B  1 133 ? -7.546  47.756 6.265   1.00 30.33 ? 133  ASP B C   1 
ATOM   6779  O  O   . ASP B  1 133 ? -8.144  47.839 7.330   1.00 29.25 ? 133  ASP B O   1 
ATOM   6780  C  CB  . ASP B  1 133 ? -5.599  46.174 6.084   1.00 33.48 ? 133  ASP B CB  1 
ATOM   6781  C  CG  . ASP B  1 133 ? -4.185  46.062 5.526   1.00 34.09 ? 133  ASP B CG  1 
ATOM   6782  O  OD1 . ASP B  1 133 ? -3.928  46.649 4.460   1.00 35.58 ? 133  ASP B OD1 1 
ATOM   6783  O  OD2 . ASP B  1 133 ? -3.331  45.402 6.149   1.00 37.10 ? 133  ASP B OD2 1 
ATOM   6784  N  N   . ILE B  1 134 ? -8.149  47.808 5.090   1.00 30.11 ? 134  ILE B N   1 
ATOM   6785  C  CA  . ILE B  1 134 ? -9.580  47.946 4.991   1.00 30.07 ? 134  ILE B CA  1 
ATOM   6786  C  C   . ILE B  1 134 ? -10.115 46.702 4.307   1.00 32.05 ? 134  ILE B C   1 
ATOM   6787  O  O   . ILE B  1 134 ? -9.595  46.269 3.275   1.00 32.77 ? 134  ILE B O   1 
ATOM   6788  C  CB  . ILE B  1 134 ? -9.949  49.181 4.154   1.00 29.02 ? 134  ILE B CB  1 
ATOM   6789  C  CG1 . ILE B  1 134 ? -9.435  50.453 4.839   1.00 27.62 ? 134  ILE B CG1 1 
ATOM   6790  C  CG2 . ILE B  1 134 ? -11.450 49.268 3.989   1.00 29.30 ? 134  ILE B CG2 1 
ATOM   6791  C  CD1 . ILE B  1 134 ? -9.537  51.683 3.961   1.00 27.66 ? 134  ILE B CD1 1 
ATOM   6792  N  N   . TYR B  1 135 ? -11.150 46.116 4.893   1.00 33.06 ? 135  TYR B N   1 
ATOM   6793  C  CA  . TYR B  1 135 ? -11.767 44.919 4.333   1.00 34.20 ? 135  TYR B CA  1 
ATOM   6794  C  C   . TYR B  1 135 ? -13.125 45.328 3.760   1.00 34.01 ? 135  TYR B C   1 
ATOM   6795  O  O   . TYR B  1 135 ? -13.913 45.977 4.445   1.00 33.24 ? 135  TYR B O   1 
ATOM   6796  C  CB  . TYR B  1 135 ? -11.947 43.872 5.443   1.00 34.84 ? 135  TYR B CB  1 
ATOM   6797  C  CG  . TYR B  1 135 ? -12.527 42.546 4.990   1.00 36.46 ? 135  TYR B CG  1 
ATOM   6798  C  CD1 . TYR B  1 135 ? -11.757 41.630 4.264   1.00 37.17 ? 135  TYR B CD1 1 
ATOM   6799  C  CD2 . TYR B  1 135 ? -13.845 42.204 5.290   1.00 37.13 ? 135  TYR B CD2 1 
ATOM   6800  C  CE1 . TYR B  1 135 ? -12.289 40.402 3.850   1.00 38.37 ? 135  TYR B CE1 1 
ATOM   6801  C  CE2 . TYR B  1 135 ? -14.391 40.982 4.882   1.00 38.06 ? 135  TYR B CE2 1 
ATOM   6802  C  CZ  . TYR B  1 135 ? -13.611 40.087 4.164   1.00 38.75 ? 135  TYR B CZ  1 
ATOM   6803  O  OH  . TYR B  1 135 ? -14.151 38.882 3.755   1.00 40.23 ? 135  TYR B OH  1 
ATOM   6804  N  N   . ASP B  1 136 ? -13.376 44.979 2.501   1.00 34.51 ? 136  ASP B N   1 
ATOM   6805  C  CA  . ASP B  1 136 ? -14.653 45.285 1.854   1.00 36.33 ? 136  ASP B CA  1 
ATOM   6806  C  C   . ASP B  1 136 ? -15.604 44.156 2.273   1.00 37.64 ? 136  ASP B C   1 
ATOM   6807  O  O   . ASP B  1 136 ? -15.453 43.018 1.826   1.00 37.80 ? 136  ASP B O   1 
ATOM   6808  C  CB  . ASP B  1 136 ? -14.475 45.297 0.333   1.00 36.39 ? 136  ASP B CB  1 
ATOM   6809  C  CG  . ASP B  1 136 ? -15.698 45.798 -0.405  1.00 36.99 ? 136  ASP B CG  1 
ATOM   6810  O  OD1 . ASP B  1 136 ? -16.826 45.383 -0.053  1.00 38.61 ? 136  ASP B OD1 1 
ATOM   6811  O  OD2 . ASP B  1 136 ? -15.526 46.599 -1.357  1.00 37.25 ? 136  ASP B OD2 1 
ATOM   6812  N  N   . LEU B  1 137 ? -16.553 44.477 3.152   1.00 38.66 ? 137  LEU B N   1 
ATOM   6813  C  CA  . LEU B  1 137 ? -17.517 43.514 3.683   1.00 40.20 ? 137  LEU B CA  1 
ATOM   6814  C  C   . LEU B  1 137 ? -18.424 42.912 2.639   1.00 42.02 ? 137  LEU B C   1 
ATOM   6815  O  O   . LEU B  1 137 ? -18.762 41.736 2.707   1.00 42.03 ? 137  LEU B O   1 
ATOM   6816  C  CB  . LEU B  1 137 ? -18.375 44.158 4.773   1.00 39.33 ? 137  LEU B CB  1 
ATOM   6817  C  CG  . LEU B  1 137 ? -17.669 44.373 6.115   1.00 39.65 ? 137  LEU B CG  1 
ATOM   6818  C  CD1 . LEU B  1 137 ? -18.547 45.188 7.071   1.00 37.92 ? 137  LEU B CD1 1 
ATOM   6819  C  CD2 . LEU B  1 137 ? -17.346 43.014 6.710   1.00 39.17 ? 137  LEU B CD2 1 
ATOM   6820  N  N   . ASN B  1 138 ? -18.820 43.712 1.663   1.00 43.97 ? 138  ASN B N   1 
ATOM   6821  C  CA  . ASN B  1 138 ? -19.680 43.186 0.631   1.00 45.29 ? 138  ASN B CA  1 
ATOM   6822  C  C   . ASN B  1 138 ? -18.983 42.092 -0.159  1.00 45.88 ? 138  ASN B C   1 
ATOM   6823  O  O   . ASN B  1 138 ? -19.239 40.896 0.050   1.00 46.98 ? 138  ASN B O   1 
ATOM   6824  C  CB  . ASN B  1 138 ? -20.142 44.302 -0.288  1.00 45.99 ? 138  ASN B CB  1 
ATOM   6825  C  CG  . ASN B  1 138 ? -21.118 45.221 0.397   1.00 47.40 ? 138  ASN B CG  1 
ATOM   6826  O  OD1 . ASN B  1 138 ? -21.846 44.798 1.308   1.00 47.72 ? 138  ASN B OD1 1 
ATOM   6827  N  ND2 . ASN B  1 138 ? -21.155 46.484 -0.034  1.00 48.52 ? 138  ASN B ND2 1 
ATOM   6828  N  N   . LYS B  1 139 ? -18.088 42.490 -1.051  1.00 45.31 ? 139  LYS B N   1 
ATOM   6829  C  CA  . LYS B  1 139 ? -17.379 41.526 -1.865  1.00 44.89 ? 139  LYS B CA  1 
ATOM   6830  C  C   . LYS B  1 139 ? -16.379 40.698 -1.047  1.00 45.22 ? 139  LYS B C   1 
ATOM   6831  O  O   . LYS B  1 139 ? -15.531 39.993 -1.604  1.00 45.39 ? 139  LYS B O   1 
ATOM   6832  C  CB  . LYS B  1 139 ? -16.677 42.255 -3.012  1.00 44.63 ? 139  LYS B CB  1 
ATOM   6833  C  CG  . LYS B  1 139 ? -15.642 43.250 -2.566  1.00 44.12 ? 139  LYS B CG  1 
ATOM   6834  C  CD  . LYS B  1 139 ? -15.095 44.010 -3.758  1.00 43.79 ? 139  LYS B CD  1 
ATOM   6835  C  CE  . LYS B  1 139 ? -16.174 44.842 -4.413  1.00 44.09 ? 139  LYS B CE  1 
ATOM   6836  N  NZ  . LYS B  1 139 ? -15.583 45.700 -5.493  1.00 44.54 ? 139  LYS B NZ  1 
ATOM   6837  N  N   . ARG B  1 140 ? -16.493 40.781 0.275   1.00 45.01 ? 140  ARG B N   1 
ATOM   6838  C  CA  . ARG B  1 140 ? -15.627 40.042 1.187   1.00 45.18 ? 140  ARG B CA  1 
ATOM   6839  C  C   . ARG B  1 140 ? -14.171 39.899 0.734   1.00 44.34 ? 140  ARG B C   1 
ATOM   6840  O  O   . ARG B  1 140 ? -13.650 38.790 0.635   1.00 43.99 ? 140  ARG B O   1 
ATOM   6841  C  CB  . ARG B  1 140 ? -16.207 38.643 1.455   1.00 46.69 ? 140  ARG B CB  1 
ATOM   6842  C  CG  . ARG B  1 140 ? -17.666 38.620 1.934   1.00 48.88 ? 140  ARG B CG  1 
ATOM   6843  C  CD  . ARG B  1 140 ? -18.034 37.236 2.488   1.00 51.30 ? 140  ARG B CD  1 
ATOM   6844  N  NE  . ARG B  1 140 ? -17.293 36.170 1.792   1.00 53.59 ? 140  ARG B NE  1 
ATOM   6845  C  CZ  . ARG B  1 140 ? -17.312 34.878 2.123   1.00 53.86 ? 140  ARG B CZ  1 
ATOM   6846  N  NH1 . ARG B  1 140 ? -18.045 34.453 3.152   1.00 54.23 ? 140  ARG B NH1 1 
ATOM   6847  N  NH2 . ARG B  1 140 ? -16.582 34.013 1.430   1.00 54.00 ? 140  ARG B NH2 1 
ATOM   6848  N  N   . GLN B  1 141 ? -13.518 41.026 0.467   1.00 43.83 ? 141  GLN B N   1 
ATOM   6849  C  CA  . GLN B  1 141 ? -12.118 41.043 0.058   1.00 42.61 ? 141  GLN B CA  1 
ATOM   6850  C  C   . GLN B  1 141 ? -11.390 42.157 0.809   1.00 41.54 ? 141  GLN B C   1 
ATOM   6851  O  O   . GLN B  1 141 ? -12.006 43.094 1.327   1.00 41.17 ? 141  GLN B O   1 
ATOM   6852  C  CB  . GLN B  1 141 ? -11.968 41.327 -1.441  1.00 44.18 ? 141  GLN B CB  1 
ATOM   6853  C  CG  . GLN B  1 141 ? -12.659 40.357 -2.370  1.00 46.41 ? 141  GLN B CG  1 
ATOM   6854  C  CD  . GLN B  1 141 ? -12.443 40.724 -3.830  1.00 47.91 ? 141  GLN B CD  1 
ATOM   6855  O  OE1 . GLN B  1 141 ? -11.302 40.821 -4.294  1.00 49.07 ? 141  GLN B OE1 1 
ATOM   6856  N  NE2 . GLN B  1 141 ? -13.538 40.934 -4.563  1.00 48.84 ? 141  GLN B NE2 1 
ATOM   6857  N  N   . LEU B  1 142 ? -10.070 42.053 0.831   1.00 39.99 ? 142  LEU B N   1 
ATOM   6858  C  CA  . LEU B  1 142 ? -9.215  43.030 1.477   1.00 38.66 ? 142  LEU B CA  1 
ATOM   6859  C  C   . LEU B  1 142 ? -8.777  44.013 0.400   1.00 38.26 ? 142  LEU B C   1 
ATOM   6860  O  O   . LEU B  1 142 ? -8.546  43.624 -0.742  1.00 38.49 ? 142  LEU B O   1 
ATOM   6861  C  CB  . LEU B  1 142 ? -7.999  42.320 2.047   1.00 38.53 ? 142  LEU B CB  1 
ATOM   6862  C  CG  . LEU B  1 142 ? -7.377  42.886 3.311   1.00 38.74 ? 142  LEU B CG  1 
ATOM   6863  C  CD1 . LEU B  1 142 ? -8.357  42.767 4.469   1.00 37.55 ? 142  LEU B CD1 1 
ATOM   6864  C  CD2 . LEU B  1 142 ? -6.107  42.115 3.605   1.00 38.36 ? 142  LEU B CD2 1 
ATOM   6865  N  N   . ILE B  1 143 ? -8.665  45.287 0.747   1.00 36.94 ? 143  ILE B N   1 
ATOM   6866  C  CA  . ILE B  1 143 ? -8.248  46.276 -0.226  1.00 35.62 ? 143  ILE B CA  1 
ATOM   6867  C  C   . ILE B  1 143 ? -6.733  46.296 -0.283  1.00 34.69 ? 143  ILE B C   1 
ATOM   6868  O  O   . ILE B  1 143 ? -6.067  46.455 0.732   1.00 34.50 ? 143  ILE B O   1 
ATOM   6869  C  CB  . ILE B  1 143 ? -8.818  47.648 0.152   1.00 36.41 ? 143  ILE B CB  1 
ATOM   6870  C  CG1 . ILE B  1 143 ? -10.342 47.582 0.052   1.00 36.10 ? 143  ILE B CG1 1 
ATOM   6871  C  CG2 . ILE B  1 143 ? -8.259  48.730 -0.751  1.00 36.23 ? 143  ILE B CG2 1 
ATOM   6872  C  CD1 . ILE B  1 143 ? -11.036 48.827 0.528   1.00 38.86 ? 143  ILE B CD1 1 
ATOM   6873  N  N   . THR B  1 144 ? -6.187  46.127 -1.479  1.00 33.85 ? 144  THR B N   1 
ATOM   6874  C  CA  . THR B  1 144 ? -4.746  46.089 -1.650  1.00 34.35 ? 144  THR B CA  1 
ATOM   6875  C  C   . THR B  1 144 ? -4.137  47.319 -2.323  1.00 34.04 ? 144  THR B C   1 
ATOM   6876  O  O   . THR B  1 144 ? -2.920  47.422 -2.443  1.00 35.51 ? 144  THR B O   1 
ATOM   6877  C  CB  . THR B  1 144 ? -4.348  44.838 -2.444  1.00 35.21 ? 144  THR B CB  1 
ATOM   6878  O  OG1 . THR B  1 144 ? -5.182  44.737 -3.610  1.00 35.93 ? 144  THR B OG1 1 
ATOM   6879  C  CG2 . THR B  1 144 ? -4.535  43.582 -1.579  1.00 35.83 ? 144  THR B CG2 1 
ATOM   6880  N  N   . GLU B  1 145 ? -4.968  48.250 -2.762  1.00 33.00 ? 145  GLU B N   1 
ATOM   6881  C  CA  . GLU B  1 145 ? -4.443  49.453 -3.392  1.00 32.63 ? 145  GLU B CA  1 
ATOM   6882  C  C   . GLU B  1 145 ? -4.750  50.695 -2.571  1.00 30.36 ? 145  GLU B C   1 
ATOM   6883  O  O   . GLU B  1 145 ? -5.724  50.726 -1.812  1.00 28.56 ? 145  GLU B O   1 
ATOM   6884  C  CB  . GLU B  1 145 ? -5.021  49.610 -4.790  1.00 34.80 ? 145  GLU B CB  1 
ATOM   6885  C  CG  . GLU B  1 145 ? -6.511  49.368 -4.863  1.00 39.30 ? 145  GLU B CG  1 
ATOM   6886  C  CD  . GLU B  1 145 ? -6.879  48.585 -6.111  1.00 42.07 ? 145  GLU B CD  1 
ATOM   6887  O  OE1 . GLU B  1 145 ? -6.296  47.488 -6.297  1.00 42.34 ? 145  GLU B OE1 1 
ATOM   6888  O  OE2 . GLU B  1 145 ? -7.737  49.063 -6.896  1.00 43.30 ? 145  GLU B OE2 1 
ATOM   6889  N  N   . GLU B  1 146 ? -3.897  51.703 -2.727  1.00 29.55 ? 146  GLU B N   1 
ATOM   6890  C  CA  . GLU B  1 146 ? -4.047  52.977 -2.034  1.00 29.46 ? 146  GLU B CA  1 
ATOM   6891  C  C   . GLU B  1 146 ? -4.310  52.725 -0.557  1.00 29.08 ? 146  GLU B C   1 
ATOM   6892  O  O   . GLU B  1 146 ? -5.243  53.276 0.036   1.00 29.08 ? 146  GLU B O   1 
ATOM   6893  C  CB  . GLU B  1 146 ? -5.194  53.770 -2.659  1.00 29.17 ? 146  GLU B CB  1 
ATOM   6894  C  CG  . GLU B  1 146 ? -4.961  54.107 -4.129  1.00 30.37 ? 146  GLU B CG  1 
ATOM   6895  C  CD  . GLU B  1 146 ? -3.766  55.036 -4.339  1.00 31.46 ? 146  GLU B CD  1 
ATOM   6896  O  OE1 . GLU B  1 146 ? -3.509  55.886 -3.470  1.00 33.32 ? 146  GLU B OE1 1 
ATOM   6897  O  OE2 . GLU B  1 146 ? -3.091  54.935 -5.378  1.00 33.34 ? 146  GLU B OE2 1 
ATOM   6898  N  N   . ARG B  1 147 ? -3.471  51.877 0.021   1.00 28.18 ? 147  ARG B N   1 
ATOM   6899  C  CA  . ARG B  1 147 ? -3.581  51.500 1.416   1.00 28.94 ? 147  ARG B CA  1 
ATOM   6900  C  C   . ARG B  1 147 ? -3.148  52.592 2.363   1.00 27.63 ? 147  ARG B C   1 
ATOM   6901  O  O   . ARG B  1 147 ? -2.290  53.421 2.035   1.00 27.05 ? 147  ARG B O   1 
ATOM   6902  C  CB  . ARG B  1 147 ? -2.743  50.250 1.666   1.00 30.21 ? 147  ARG B CB  1 
ATOM   6903  C  CG  . ARG B  1 147 ? -3.298  49.031 0.943   1.00 32.68 ? 147  ARG B CG  1 
ATOM   6904  C  CD  . ARG B  1 147 ? -2.300  47.914 0.937   1.00 34.84 ? 147  ARG B CD  1 
ATOM   6905  N  NE  . ARG B  1 147 ? -1.978  47.479 2.283   1.00 37.02 ? 147  ARG B NE  1 
ATOM   6906  C  CZ  . ARG B  1 147 ? -0.863  46.829 2.601   1.00 38.82 ? 147  ARG B CZ  1 
ATOM   6907  N  NH1 . ARG B  1 147 ? 0.030   46.553 1.656   1.00 39.15 ? 147  ARG B NH1 1 
ATOM   6908  N  NH2 . ARG B  1 147 ? -0.643  46.449 3.857   1.00 38.45 ? 147  ARG B NH2 1 
ATOM   6909  N  N   . ILE B  1 148 ? -3.760  52.589 3.540   1.00 27.37 ? 148  ILE B N   1 
ATOM   6910  C  CA  . ILE B  1 148 ? -3.427  53.549 4.577   1.00 26.29 ? 148  ILE B CA  1 
ATOM   6911  C  C   . ILE B  1 148 ? -1.967  53.278 4.890   1.00 26.29 ? 148  ILE B C   1 
ATOM   6912  O  O   . ILE B  1 148 ? -1.585  52.141 5.108   1.00 27.08 ? 148  ILE B O   1 
ATOM   6913  C  CB  . ILE B  1 148 ? -4.331  53.327 5.803   1.00 25.56 ? 148  ILE B CB  1 
ATOM   6914  C  CG1 . ILE B  1 148 ? -5.754  53.759 5.446   1.00 25.22 ? 148  ILE B CG1 1 
ATOM   6915  C  CG2 . ILE B  1 148 ? -3.805  54.101 6.995   1.00 24.84 ? 148  ILE B CG2 1 
ATOM   6916  C  CD1 . ILE B  1 148 ? -6.842  53.188 6.361   1.00 25.99 ? 148  ILE B CD1 1 
ATOM   6917  N  N   . PRO B  1 149 ? -1.131  54.327 4.911   1.00 26.64 ? 149  PRO B N   1 
ATOM   6918  C  CA  . PRO B  1 149 ? 0.308   54.254 5.179   1.00 27.61 ? 149  PRO B CA  1 
ATOM   6919  C  C   . PRO B  1 149 ? 0.664   53.580 6.491   1.00 28.54 ? 149  PRO B C   1 
ATOM   6920  O  O   . PRO B  1 149 ? -0.094  53.648 7.460   1.00 28.86 ? 149  PRO B O   1 
ATOM   6921  C  CB  . PRO B  1 149 ? 0.747   55.727 5.220   1.00 26.96 ? 149  PRO B CB  1 
ATOM   6922  C  CG  . PRO B  1 149 ? -0.350  56.470 4.534   1.00 26.62 ? 149  PRO B CG  1 
ATOM   6923  C  CD  . PRO B  1 149 ? -1.588  55.727 4.919   1.00 26.62 ? 149  PRO B CD  1 
ATOM   6924  N  N   . ASN B  1 150 ? 1.823   52.940 6.530   1.00 29.31 ? 150  ASN B N   1 
ATOM   6925  C  CA  . ASN B  1 150 ? 2.265   52.350 7.779   1.00 31.20 ? 150  ASN B CA  1 
ATOM   6926  C  C   . ASN B  1 150 ? 2.649   53.541 8.670   1.00 30.02 ? 150  ASN B C   1 
ATOM   6927  O  O   . ASN B  1 150 ? 2.999   54.624 8.173   1.00 29.61 ? 150  ASN B O   1 
ATOM   6928  C  CB  . ASN B  1 150 ? 3.474   51.429 7.566   1.00 34.31 ? 150  ASN B CB  1 
ATOM   6929  C  CG  . ASN B  1 150 ? 3.093   50.104 6.901   1.00 38.69 ? 150  ASN B CG  1 
ATOM   6930  O  OD1 . ASN B  1 150 ? 2.079   49.476 7.258   1.00 38.45 ? 150  ASN B OD1 1 
ATOM   6931  N  ND2 . ASN B  1 150 ? 3.911   49.685 5.936   1.00 42.43 ? 150  ASN B ND2 1 
ATOM   6932  N  N   . ASN B  1 151 ? 2.572   53.333 9.977   1.00 28.93 ? 151  ASN B N   1 
ATOM   6933  C  CA  . ASN B  1 151 ? 2.898   54.361 10.955  1.00 28.27 ? 151  ASN B CA  1 
ATOM   6934  C  C   . ASN B  1 151 ? 1.881   55.488 10.934  1.00 26.51 ? 151  ASN B C   1 
ATOM   6935  O  O   . ASN B  1 151 ? 2.235   56.645 11.118  1.00 25.03 ? 151  ASN B O   1 
ATOM   6936  C  CB  . ASN B  1 151 ? 4.293   54.931 10.698  1.00 30.57 ? 151  ASN B CB  1 
ATOM   6937  C  CG  . ASN B  1 151 ? 5.339   53.849 10.537  1.00 32.33 ? 151  ASN B CG  1 
ATOM   6938  O  OD1 . ASN B  1 151 ? 5.442   52.942 11.363  1.00 33.80 ? 151  ASN B OD1 1 
ATOM   6939  N  ND2 . ASN B  1 151 ? 6.125   53.940 9.468   1.00 32.71 ? 151  ASN B ND2 1 
ATOM   6940  N  N   . THR B  1 152 ? 0.619   55.140 10.697  1.00 24.89 ? 152  THR B N   1 
ATOM   6941  C  CA  . THR B  1 152 ? -0.443  56.125 10.690  1.00 23.19 ? 152  THR B CA  1 
ATOM   6942  C  C   . THR B  1 152 ? -0.723  56.419 12.158  1.00 22.62 ? 152  THR B C   1 
ATOM   6943  O  O   . THR B  1 152 ? -0.786  55.517 12.992  1.00 22.33 ? 152  THR B O   1 
ATOM   6944  C  CB  . THR B  1 152 ? -1.673  55.588 9.944   1.00 22.84 ? 152  THR B CB  1 
ATOM   6945  O  OG1 . THR B  1 152 ? -1.429  55.699 8.539   1.00 22.41 ? 152  THR B OG1 1 
ATOM   6946  C  CG2 . THR B  1 152 ? -2.924  56.370 10.289  1.00 21.41 ? 152  THR B CG2 1 
ATOM   6947  N  N   . GLN B  1 153 ? -0.873  57.698 12.460  1.00 22.01 ? 153  GLN B N   1 
ATOM   6948  C  CA  . GLN B  1 153 ? -1.067  58.163 13.822  1.00 21.38 ? 153  GLN B CA  1 
ATOM   6949  C  C   . GLN B  1 153 ? -2.501  58.166 14.299  1.00 21.49 ? 153  GLN B C   1 
ATOM   6950  O  O   . GLN B  1 153 ? -2.771  58.060 15.489  1.00 21.33 ? 153  GLN B O   1 
ATOM   6951  C  CB  . GLN B  1 153 ? -0.453  59.557 13.938  1.00 20.14 ? 153  GLN B CB  1 
ATOM   6952  C  CG  . GLN B  1 153 ? 1.051   59.554 13.607  1.00 20.45 ? 153  GLN B CG  1 
ATOM   6953  C  CD  . GLN B  1 153 ? 1.605   60.933 13.238  1.00 18.83 ? 153  GLN B CD  1 
ATOM   6954  O  OE1 . GLN B  1 153 ? 1.248   61.504 12.203  1.00 16.67 ? 153  GLN B OE1 1 
ATOM   6955  N  NE2 . GLN B  1 153 ? 2.487   61.465 14.082  1.00 18.33 ? 153  GLN B NE2 1 
ATOM   6956  N  N   . TRP B  1 154 ? -3.430  58.287 13.369  1.00 21.61 ? 154  TRP B N   1 
ATOM   6957  C  CA  . TRP B  1 154 ? -4.837  58.304 13.739  1.00 21.57 ? 154  TRP B CA  1 
ATOM   6958  C  C   . TRP B  1 154 ? -5.689  58.147 12.501  1.00 20.51 ? 154  TRP B C   1 
ATOM   6959  O  O   . TRP B  1 154 ? -5.322  58.637 11.434  1.00 19.20 ? 154  TRP B O   1 
ATOM   6960  C  CB  . TRP B  1 154 ? -5.189  59.623 14.425  1.00 23.41 ? 154  TRP B CB  1 
ATOM   6961  C  CG  . TRP B  1 154 ? -6.634  59.712 14.753  1.00 26.80 ? 154  TRP B CG  1 
ATOM   6962  C  CD1 . TRP B  1 154 ? -7.598  60.424 14.084  1.00 28.91 ? 154  TRP B CD1 1 
ATOM   6963  C  CD2 . TRP B  1 154 ? -7.306  59.001 15.794  1.00 27.65 ? 154  TRP B CD2 1 
ATOM   6964  N  NE1 . TRP B  1 154 ? -8.838  60.192 14.650  1.00 29.60 ? 154  TRP B NE1 1 
ATOM   6965  C  CE2 . TRP B  1 154 ? -8.684  59.322 15.700  1.00 29.61 ? 154  TRP B CE2 1 
ATOM   6966  C  CE3 . TRP B  1 154 ? -6.876  58.122 16.797  1.00 27.45 ? 154  TRP B CE3 1 
ATOM   6967  C  CZ2 . TRP B  1 154 ? -9.644  58.789 16.579  1.00 30.16 ? 154  TRP B CZ2 1 
ATOM   6968  C  CZ3 . TRP B  1 154 ? -7.819  57.588 17.669  1.00 29.97 ? 154  TRP B CZ3 1 
ATOM   6969  C  CH2 . TRP B  1 154 ? -9.195  57.926 17.555  1.00 30.95 ? 154  TRP B CH2 1 
ATOM   6970  N  N   . VAL B  1 155 ? -6.815  57.455 12.640  1.00 19.88 ? 155  VAL B N   1 
ATOM   6971  C  CA  . VAL B  1 155 ? -7.727  57.255 11.518  1.00 20.50 ? 155  VAL B CA  1 
ATOM   6972  C  C   . VAL B  1 155 ? -9.140  57.272 12.033  1.00 20.49 ? 155  VAL B C   1 
ATOM   6973  O  O   . VAL B  1 155 ? -9.418  56.712 13.091  1.00 20.19 ? 155  VAL B O   1 
ATOM   6974  C  CB  . VAL B  1 155 ? -7.543  55.882 10.812  1.00 21.00 ? 155  VAL B CB  1 
ATOM   6975  C  CG1 . VAL B  1 155 ? -8.519  55.755 9.659   1.00 20.88 ? 155  VAL B CG1 1 
ATOM   6976  C  CG2 . VAL B  1 155 ? -6.147  55.738 10.299  1.00 23.30 ? 155  VAL B CG2 1 
ATOM   6977  N  N   . THR B  1 156 ? -10.033 57.893 11.273  1.00 20.94 ? 156  THR B N   1 
ATOM   6978  C  CA  . THR B  1 156 ? -11.439 57.946 11.648  1.00 21.69 ? 156  THR B CA  1 
ATOM   6979  C  C   . THR B  1 156 ? -12.355 58.014 10.432  1.00 21.66 ? 156  THR B C   1 
ATOM   6980  O  O   . THR B  1 156 ? -12.112 58.762 9.475   1.00 20.50 ? 156  THR B O   1 
ATOM   6981  C  CB  . THR B  1 156 ? -11.749 59.154 12.567  1.00 23.85 ? 156  THR B CB  1 
ATOM   6982  O  OG1 . THR B  1 156 ? -13.156 59.193 12.842  1.00 25.60 ? 156  THR B OG1 1 
ATOM   6983  C  CG2 . THR B  1 156 ? -11.360 60.441 11.899  1.00 23.82 ? 156  THR B CG2 1 
ATOM   6984  N  N   . TRP B  1 157 ? -13.411 57.210 10.482  1.00 21.14 ? 157  TRP B N   1 
ATOM   6985  C  CA  . TRP B  1 157 ? -14.406 57.163 9.428   1.00 21.25 ? 157  TRP B CA  1 
ATOM   6986  C  C   . TRP B  1 157 ? -15.217 58.449 9.526   1.00 20.85 ? 157  TRP B C   1 
ATOM   6987  O  O   . TRP B  1 157 ? -15.222 59.080 10.574  1.00 19.81 ? 157  TRP B O   1 
ATOM   6988  C  CB  . TRP B  1 157 ? -15.381 55.996 9.664   1.00 22.47 ? 157  TRP B CB  1 
ATOM   6989  C  CG  . TRP B  1 157 ? -14.836 54.609 9.438   1.00 22.88 ? 157  TRP B CG  1 
ATOM   6990  C  CD1 . TRP B  1 157 ? -14.547 53.671 10.394  1.00 22.97 ? 157  TRP B CD1 1 
ATOM   6991  C  CD2 . TRP B  1 157 ? -14.529 53.999 8.175   1.00 22.40 ? 157  TRP B CD2 1 
ATOM   6992  N  NE1 . TRP B  1 157 ? -14.079 52.524 9.804   1.00 22.54 ? 157  TRP B NE1 1 
ATOM   6993  C  CE2 . TRP B  1 157 ? -14.057 52.694 8.445   1.00 22.39 ? 157  TRP B CE2 1 
ATOM   6994  C  CE3 . TRP B  1 157 ? -14.603 54.428 6.845   1.00 21.42 ? 157  TRP B CE3 1 
ATOM   6995  C  CZ2 . TRP B  1 157 ? -13.666 51.815 7.434   1.00 21.89 ? 157  TRP B CZ2 1 
ATOM   6996  C  CZ3 . TRP B  1 157 ? -14.218 53.556 5.840   1.00 22.03 ? 157  TRP B CZ3 1 
ATOM   6997  C  CH2 . TRP B  1 157 ? -13.754 52.264 6.139   1.00 22.16 ? 157  TRP B CH2 1 
ATOM   6998  N  N   . SER B  1 158 ? -15.883 58.844 8.447   1.00 20.28 ? 158  SER B N   1 
ATOM   6999  C  CA  . SER B  1 158 ? -16.763 60.000 8.531   1.00 21.73 ? 158  SER B CA  1 
ATOM   7000  C  C   . SER B  1 158 ? -17.945 59.489 9.382   1.00 22.43 ? 158  SER B C   1 
ATOM   7001  O  O   . SER B  1 158 ? -18.133 58.280 9.524   1.00 20.95 ? 158  SER B O   1 
ATOM   7002  C  CB  . SER B  1 158 ? -17.261 60.419 7.145   1.00 20.52 ? 158  SER B CB  1 
ATOM   7003  O  OG  . SER B  1 158 ? -17.621 59.299 6.344   1.00 21.06 ? 158  SER B OG  1 
ATOM   7004  N  N   . PRO B  1 159 ? -18.747 60.396 9.964   1.00 23.12 ? 159  PRO B N   1 
ATOM   7005  C  CA  . PRO B  1 159 ? -19.887 59.963 10.789  1.00 24.73 ? 159  PRO B CA  1 
ATOM   7006  C  C   . PRO B  1 159 ? -20.973 59.188 10.026  1.00 25.61 ? 159  PRO B C   1 
ATOM   7007  O  O   . PRO B  1 159 ? -21.735 58.428 10.619  1.00 25.79 ? 159  PRO B O   1 
ATOM   7008  C  CB  . PRO B  1 159 ? -20.393 61.278 11.404  1.00 24.71 ? 159  PRO B CB  1 
ATOM   7009  C  CG  . PRO B  1 159 ? -20.005 62.316 10.386  1.00 24.98 ? 159  PRO B CG  1 
ATOM   7010  C  CD  . PRO B  1 159 ? -18.636 61.864 9.929   1.00 24.14 ? 159  PRO B CD  1 
ATOM   7011  N  N   . VAL B  1 160 ? -21.035 59.390 8.713   1.00 25.97 ? 160  VAL B N   1 
ATOM   7012  C  CA  . VAL B  1 160 ? -21.991 58.706 7.850   1.00 26.14 ? 160  VAL B CA  1 
ATOM   7013  C  C   . VAL B  1 160 ? -21.226 58.239 6.608   1.00 26.48 ? 160  VAL B C   1 
ATOM   7014  O  O   . VAL B  1 160 ? -20.208 58.829 6.245   1.00 25.99 ? 160  VAL B O   1 
ATOM   7015  C  CB  . VAL B  1 160 ? -23.131 59.652 7.401   1.00 26.77 ? 160  VAL B CB  1 
ATOM   7016  C  CG1 . VAL B  1 160 ? -24.013 58.941 6.380   1.00 28.27 ? 160  VAL B CG1 1 
ATOM   7017  C  CG2 . VAL B  1 160 ? -23.976 60.072 8.603   1.00 27.27 ? 160  VAL B CG2 1 
ATOM   7018  N  N   . GLY B  1 161 ? -21.714 57.187 5.960   1.00 25.64 ? 161  GLY B N   1 
ATOM   7019  C  CA  . GLY B  1 161 ? -21.052 56.684 4.772   1.00 24.66 ? 161  GLY B CA  1 
ATOM   7020  C  C   . GLY B  1 161 ? -19.776 55.932 5.098   1.00 24.32 ? 161  GLY B C   1 
ATOM   7021  O  O   . GLY B  1 161 ? -19.760 55.094 6.005   1.00 23.42 ? 161  GLY B O   1 
ATOM   7022  N  N   . HIS B  1 162 ? -18.703 56.233 4.363   1.00 23.32 ? 162  HIS B N   1 
ATOM   7023  C  CA  . HIS B  1 162 ? -17.415 55.571 4.582   1.00 23.96 ? 162  HIS B CA  1 
ATOM   7024  C  C   . HIS B  1 162 ? -16.183 56.380 4.152   1.00 23.33 ? 162  HIS B C   1 
ATOM   7025  O  O   . HIS B  1 162 ? -15.214 55.809 3.646   1.00 22.63 ? 162  HIS B O   1 
ATOM   7026  C  CB  . HIS B  1 162 ? -17.387 54.199 3.884   1.00 25.44 ? 162  HIS B CB  1 
ATOM   7027  C  CG  . HIS B  1 162 ? -17.773 54.255 2.443   1.00 27.23 ? 162  HIS B CG  1 
ATOM   7028  N  ND1 . HIS B  1 162 ? -18.958 53.734 1.968   1.00 28.46 ? 162  HIS B ND1 1 
ATOM   7029  C  CD2 . HIS B  1 162 ? -17.160 54.829 1.380   1.00 27.73 ? 162  HIS B CD2 1 
ATOM   7030  C  CE1 . HIS B  1 162 ? -19.059 53.987 0.675   1.00 29.41 ? 162  HIS B CE1 1 
ATOM   7031  N  NE2 . HIS B  1 162 ? -17.981 54.652 0.294   1.00 29.45 ? 162  HIS B NE2 1 
ATOM   7032  N  N   . LYS B  1 163 ? -16.233 57.700 4.327   1.00 21.54 ? 163  LYS B N   1 
ATOM   7033  C  CA  . LYS B  1 163 ? -15.074 58.538 4.024   1.00 21.43 ? 163  LYS B CA  1 
ATOM   7034  C  C   . LYS B  1 163 ? -14.098 58.226 5.150   1.00 20.83 ? 163  LYS B C   1 
ATOM   7035  O  O   . LYS B  1 163 ? -14.503 57.742 6.198   1.00 21.62 ? 163  LYS B O   1 
ATOM   7036  C  CB  . LYS B  1 163 ? -15.414 60.030 4.090   1.00 19.36 ? 163  LYS B CB  1 
ATOM   7037  C  CG  . LYS B  1 163 ? -16.326 60.536 2.991   1.00 21.07 ? 163  LYS B CG  1 
ATOM   7038  C  CD  . LYS B  1 163 ? -16.548 62.042 3.166   1.00 20.60 ? 163  LYS B CD  1 
ATOM   7039  C  CE  . LYS B  1 163 ? -17.428 62.611 2.073   1.00 21.95 ? 163  LYS B CE  1 
ATOM   7040  N  NZ  . LYS B  1 163 ? -17.593 64.074 2.265   1.00 21.22 ? 163  LYS B NZ  1 
ATOM   7041  N  N   . LEU B  1 164 ? -12.823 58.507 4.929   1.00 21.06 ? 164  LEU B N   1 
ATOM   7042  C  CA  . LEU B  1 164 ? -11.799 58.270 5.921   1.00 20.79 ? 164  LEU B CA  1 
ATOM   7043  C  C   . LEU B  1 164 ? -10.901 59.479 6.018   1.00 21.14 ? 164  LEU B C   1 
ATOM   7044  O  O   . LEU B  1 164 ? -10.546 60.078 5.004   1.00 21.96 ? 164  LEU B O   1 
ATOM   7045  C  CB  . LEU B  1 164 ? -10.928 57.084 5.520   1.00 22.00 ? 164  LEU B CB  1 
ATOM   7046  C  CG  . LEU B  1 164 ? -11.391 55.641 5.782   1.00 22.01 ? 164  LEU B CG  1 
ATOM   7047  C  CD1 . LEU B  1 164 ? -10.527 54.675 4.979   1.00 22.23 ? 164  LEU B CD1 1 
ATOM   7048  C  CD2 . LEU B  1 164 ? -11.287 55.343 7.275   1.00 21.22 ? 164  LEU B CD2 1 
ATOM   7049  N  N   . ALA B  1 165 ? -10.541 59.857 7.233   1.00 19.91 ? 165  ALA B N   1 
ATOM   7050  C  CA  . ALA B  1 165 ? -9.604  60.956 7.407   1.00 19.59 ? 165  ALA B CA  1 
ATOM   7051  C  C   . ALA B  1 165 ? -8.531  60.354 8.283   1.00 19.50 ? 165  ALA B C   1 
ATOM   7052  O  O   . ALA B  1 165 ? -8.856  59.650 9.244   1.00 20.75 ? 165  ALA B O   1 
ATOM   7053  C  CB  . ALA B  1 165 ? -10.268 62.142 8.120   1.00 19.34 ? 165  ALA B CB  1 
ATOM   7054  N  N   . TYR B  1 166 ? -7.261  60.586 7.955   1.00 18.15 ? 166  TYR B N   1 
ATOM   7055  C  CA  . TYR B  1 166 ? -6.191  60.059 8.792   1.00 17.62 ? 166  TYR B CA  1 
ATOM   7056  C  C   . TYR B  1 166 ? -5.018  61.003 8.865   1.00 16.96 ? 166  TYR B C   1 
ATOM   7057  O  O   . TYR B  1 166 ? -4.880  61.899 8.030   1.00 17.23 ? 166  TYR B O   1 
ATOM   7058  C  CB  . TYR B  1 166 ? -5.689  58.697 8.305   1.00 17.27 ? 166  TYR B CB  1 
ATOM   7059  C  CG  . TYR B  1 166 ? -5.089  58.671 6.908   1.00 19.05 ? 166  TYR B CG  1 
ATOM   7060  C  CD1 . TYR B  1 166 ? -5.891  58.494 5.790   1.00 19.29 ? 166  TYR B CD1 1 
ATOM   7061  C  CD2 . TYR B  1 166 ? -3.714  58.776 6.715   1.00 19.69 ? 166  TYR B CD2 1 
ATOM   7062  C  CE1 . TYR B  1 166 ? -5.336  58.415 4.506   1.00 20.42 ? 166  TYR B CE1 1 
ATOM   7063  C  CE2 . TYR B  1 166 ? -3.148  58.701 5.431   1.00 20.17 ? 166  TYR B CE2 1 
ATOM   7064  C  CZ  . TYR B  1 166 ? -3.971  58.519 4.336   1.00 20.12 ? 166  TYR B CZ  1 
ATOM   7065  O  OH  . TYR B  1 166 ? -3.427  58.442 3.078   1.00 19.59 ? 166  TYR B OH  1 
ATOM   7066  N  N   . VAL B  1 167 ? -4.185  60.805 9.879   1.00 15.49 ? 167  VAL B N   1 
ATOM   7067  C  CA  . VAL B  1 167 ? -3.008  61.631 10.067  1.00 14.60 ? 167  VAL B CA  1 
ATOM   7068  C  C   . VAL B  1 167 ? -1.793  60.745 9.931   1.00 15.65 ? 167  VAL B C   1 
ATOM   7069  O  O   . VAL B  1 167 ? -1.724  59.679 10.544  1.00 15.83 ? 167  VAL B O   1 
ATOM   7070  C  CB  . VAL B  1 167 ? -2.973  62.292 11.456  1.00 14.00 ? 167  VAL B CB  1 
ATOM   7071  C  CG1 . VAL B  1 167 ? -1.691  63.150 11.591  1.00 11.63 ? 167  VAL B CG1 1 
ATOM   7072  C  CG2 . VAL B  1 167 ? -4.229  63.130 11.653  1.00 14.14 ? 167  VAL B CG2 1 
ATOM   7073  N  N   . TRP B  1 168 ? -0.843  61.199 9.121   1.00 15.42 ? 168  TRP B N   1 
ATOM   7074  C  CA  . TRP B  1 168 ? 0.386   60.466 8.855   1.00 17.37 ? 168  TRP B CA  1 
ATOM   7075  C  C   . TRP B  1 168 ? 1.507   61.501 8.722   1.00 17.43 ? 168  TRP B C   1 
ATOM   7076  O  O   . TRP B  1 168 ? 1.402   62.438 7.922   1.00 17.79 ? 168  TRP B O   1 
ATOM   7077  C  CB  . TRP B  1 168 ? 0.239   59.662 7.555   1.00 17.30 ? 168  TRP B CB  1 
ATOM   7078  C  CG  . TRP B  1 168 ? 1.467   58.900 7.195   1.00 19.22 ? 168  TRP B CG  1 
ATOM   7079  C  CD1 . TRP B  1 168 ? 1.957   57.776 7.808   1.00 19.54 ? 168  TRP B CD1 1 
ATOM   7080  C  CD2 . TRP B  1 168 ? 2.410   59.249 6.184   1.00 20.07 ? 168  TRP B CD2 1 
ATOM   7081  N  NE1 . TRP B  1 168 ? 3.154   57.413 7.234   1.00 20.04 ? 168  TRP B NE1 1 
ATOM   7082  C  CE2 . TRP B  1 168 ? 3.455   58.301 6.238   1.00 19.95 ? 168  TRP B CE2 1 
ATOM   7083  C  CE3 . TRP B  1 168 ? 2.474   60.278 5.236   1.00 20.30 ? 168  TRP B CE3 1 
ATOM   7084  C  CZ2 . TRP B  1 168 ? 4.559   58.350 5.380   1.00 22.82 ? 168  TRP B CZ2 1 
ATOM   7085  C  CZ3 . TRP B  1 168 ? 3.573   60.328 4.374   1.00 21.68 ? 168  TRP B CZ3 1 
ATOM   7086  C  CH2 . TRP B  1 168 ? 4.604   59.364 4.455   1.00 22.20 ? 168  TRP B CH2 1 
ATOM   7087  N  N   . ASN B  1 169 ? 2.573   61.323 9.496   1.00 17.16 ? 169  ASN B N   1 
ATOM   7088  C  CA  . ASN B  1 169 ? 3.690   62.263 9.507   1.00 17.62 ? 169  ASN B CA  1 
ATOM   7089  C  C   . ASN B  1 169 ? 3.181   63.677 9.825   1.00 16.57 ? 169  ASN B C   1 
ATOM   7090  O  O   . ASN B  1 169 ? 3.579   64.664 9.198   1.00 16.62 ? 169  ASN B O   1 
ATOM   7091  C  CB  . ASN B  1 169 ? 4.441   62.254 8.169   1.00 18.92 ? 169  ASN B CB  1 
ATOM   7092  C  CG  . ASN B  1 169 ? 5.346   61.023 7.997   1.00 22.03 ? 169  ASN B CG  1 
ATOM   7093  O  OD1 . ASN B  1 169 ? 5.890   60.796 6.916   1.00 27.53 ? 169  ASN B OD1 1 
ATOM   7094  N  ND2 . ASN B  1 169 ? 5.508   60.236 9.054   1.00 22.09 ? 169  ASN B ND2 1 
ATOM   7095  N  N   . ASN B  1 170 ? 2.266   63.746 10.789  1.00 15.86 ? 170  ASN B N   1 
ATOM   7096  C  CA  . ASN B  1 170 ? 1.707   65.003 11.257  1.00 14.96 ? 170  ASN B CA  1 
ATOM   7097  C  C   . ASN B  1 170 ? 0.841   65.829 10.292  1.00 15.15 ? 170  ASN B C   1 
ATOM   7098  O  O   . ASN B  1 170 ? 0.567   66.999 10.572  1.00 14.49 ? 170  ASN B O   1 
ATOM   7099  C  CB  . ASN B  1 170 ? 2.846   65.867 11.818  1.00 15.78 ? 170  ASN B CB  1 
ATOM   7100  C  CG  . ASN B  1 170 ? 3.440   65.286 13.094  1.00 16.97 ? 170  ASN B CG  1 
ATOM   7101  O  OD1 . ASN B  1 170 ? 3.684   64.087 13.181  1.00 17.86 ? 170  ASN B OD1 1 
ATOM   7102  N  ND2 . ASN B  1 170 ? 3.680   66.143 14.087  1.00 16.93 ? 170  ASN B ND2 1 
ATOM   7103  N  N   . ASP B  1 171 ? 0.423   65.228 9.173   1.00 14.64 ? 171  ASP B N   1 
ATOM   7104  C  CA  . ASP B  1 171 ? -0.464  65.901 8.213   1.00 14.33 ? 171  ASP B CA  1 
ATOM   7105  C  C   . ASP B  1 171 ? -1.765  65.135 8.030   1.00 14.03 ? 171  ASP B C   1 
ATOM   7106  O  O   . ASP B  1 171 ? -1.820  63.923 8.188   1.00 13.76 ? 171  ASP B O   1 
ATOM   7107  C  CB  . ASP B  1 171 ? 0.179   66.044 6.841   1.00 16.51 ? 171  ASP B CB  1 
ATOM   7108  C  CG  . ASP B  1 171 ? 1.180   67.163 6.779   1.00 17.44 ? 171  ASP B CG  1 
ATOM   7109  O  OD1 . ASP B  1 171 ? 2.263   66.919 6.221   1.00 17.46 ? 171  ASP B OD1 1 
ATOM   7110  O  OD2 . ASP B  1 171 ? 0.883   68.273 7.270   1.00 17.42 ? 171  ASP B OD2 1 
ATOM   7111  N  N   . ILE B  1 172 ? -2.814  65.845 7.649   1.00 15.34 ? 172  ILE B N   1 
ATOM   7112  C  CA  . ILE B  1 172 ? -4.107  65.222 7.464   1.00 14.75 ? 172  ILE B CA  1 
ATOM   7113  C  C   . ILE B  1 172 ? -4.301  64.805 6.019   1.00 15.68 ? 172  ILE B C   1 
ATOM   7114  O  O   . ILE B  1 172 ? -3.900  65.511 5.099   1.00 15.27 ? 172  ILE B O   1 
ATOM   7115  C  CB  . ILE B  1 172 ? -5.229  66.201 7.867   1.00 14.73 ? 172  ILE B CB  1 
ATOM   7116  C  CG1 . ILE B  1 172 ? -5.066  66.580 9.335   1.00 14.68 ? 172  ILE B CG1 1 
ATOM   7117  C  CG2 . ILE B  1 172 ? -6.626  65.581 7.566   1.00 13.06 ? 172  ILE B CG2 1 
ATOM   7118  C  CD1 . ILE B  1 172 ? -5.941  67.772 9.754   1.00 14.72 ? 172  ILE B CD1 1 
ATOM   7119  N  N   . TYR B  1 173 ? -4.935  63.650 5.852   1.00 16.16 ? 173  TYR B N   1 
ATOM   7120  C  CA  . TYR B  1 173 ? -5.252  63.093 4.548   1.00 17.13 ? 173  TYR B CA  1 
ATOM   7121  C  C   . TYR B  1 173 ? -6.705  62.609 4.589   1.00 16.53 ? 173  TYR B C   1 
ATOM   7122  O  O   . TYR B  1 173 ? -7.179  62.160 5.638   1.00 15.07 ? 173  TYR B O   1 
ATOM   7123  C  CB  . TYR B  1 173 ? -4.333  61.907 4.220   1.00 16.45 ? 173  TYR B CB  1 
ATOM   7124  C  CG  . TYR B  1 173 ? -2.873  62.272 4.025   1.00 17.41 ? 173  TYR B CG  1 
ATOM   7125  C  CD1 . TYR B  1 173 ? -2.009  62.414 5.115   1.00 16.07 ? 173  TYR B CD1 1 
ATOM   7126  C  CD2 . TYR B  1 173 ? -2.350  62.453 2.741   1.00 17.09 ? 173  TYR B CD2 1 
ATOM   7127  C  CE1 . TYR B  1 173 ? -0.656  62.722 4.931   1.00 15.76 ? 173  TYR B CE1 1 
ATOM   7128  C  CE2 . TYR B  1 173 ? -1.016  62.763 2.548   1.00 17.50 ? 173  TYR B CE2 1 
ATOM   7129  C  CZ  . TYR B  1 173 ? -0.174  62.898 3.646   1.00 17.68 ? 173  TYR B CZ  1 
ATOM   7130  O  OH  . TYR B  1 173 ? 1.138   63.250 3.454   1.00 18.72 ? 173  TYR B OH  1 
ATOM   7131  N  N   . VAL B  1 174 ? -7.410  62.711 3.455   1.00 16.48 ? 174  VAL B N   1 
ATOM   7132  C  CA  . VAL B  1 174 ? -8.797  62.250 3.358   1.00 14.90 ? 174  VAL B CA  1 
ATOM   7133  C  C   . VAL B  1 174 ? -8.986  61.315 2.165   1.00 16.89 ? 174  VAL B C   1 
ATOM   7134  O  O   . VAL B  1 174 ? -8.507  61.586 1.070   1.00 17.22 ? 174  VAL B O   1 
ATOM   7135  C  CB  . VAL B  1 174 ? -9.781  63.422 3.160   1.00 14.85 ? 174  VAL B CB  1 
ATOM   7136  C  CG1 . VAL B  1 174 ? -11.202 62.883 2.867   1.00 13.54 ? 174  VAL B CG1 1 
ATOM   7137  C  CG2 . VAL B  1 174 ? -9.765  64.347 4.400   1.00 14.06 ? 174  VAL B CG2 1 
ATOM   7138  N  N   . LYS B  1 175 ? -9.695  60.220 2.373   1.00 17.75 ? 175  LYS B N   1 
ATOM   7139  C  CA  . LYS B  1 175 ? -9.983  59.296 1.283   1.00 19.40 ? 175  LYS B CA  1 
ATOM   7140  C  C   . LYS B  1 175 ? -11.483 59.277 1.141   1.00 19.71 ? 175  LYS B C   1 
ATOM   7141  O  O   . LYS B  1 175 ? -12.183 58.931 2.098   1.00 20.29 ? 175  LYS B O   1 
ATOM   7142  C  CB  . LYS B  1 175 ? -9.501  57.876 1.602   1.00 20.17 ? 175  LYS B CB  1 
ATOM   7143  C  CG  . LYS B  1 175 ? -7.995  57.686 1.436   1.00 23.54 ? 175  LYS B CG  1 
ATOM   7144  C  CD  . LYS B  1 175 ? -7.497  56.419 2.142   1.00 26.79 ? 175  LYS B CD  1 
ATOM   7145  C  CE  . LYS B  1 175 ? -7.909  55.155 1.409   1.00 26.96 ? 175  LYS B CE  1 
ATOM   7146  N  NZ  . LYS B  1 175 ? -7.129  55.023 0.155   1.00 29.33 ? 175  LYS B NZ  1 
ATOM   7147  N  N   . ILE B  1 176 ? -11.982 59.667 -0.027  1.00 19.93 ? 176  ILE B N   1 
ATOM   7148  C  CA  . ILE B  1 176 ? -13.426 59.645 -0.274  1.00 21.02 ? 176  ILE B CA  1 
ATOM   7149  C  C   . ILE B  1 176 ? -13.893 58.179 -0.409  1.00 22.06 ? 176  ILE B C   1 
ATOM   7150  O  O   . ILE B  1 176 ? -14.991 57.815 0.027   1.00 22.15 ? 176  ILE B O   1 
ATOM   7151  C  CB  . ILE B  1 176 ? -13.784 60.403 -1.573  1.00 20.33 ? 176  ILE B CB  1 
ATOM   7152  C  CG1 . ILE B  1 176 ? -13.238 61.828 -1.498  1.00 20.36 ? 176  ILE B CG1 1 
ATOM   7153  C  CG2 . ILE B  1 176 ? -15.299 60.427 -1.777  1.00 20.17 ? 176  ILE B CG2 1 
ATOM   7154  C  CD1 . ILE B  1 176 ? -13.806 62.652 -0.387  1.00 19.70 ? 176  ILE B CD1 1 
ATOM   7155  N  N   . GLU B  1 177 ? -13.065 57.349 -1.033  1.00 22.76 ? 177  GLU B N   1 
ATOM   7156  C  CA  . GLU B  1 177 ? -13.381 55.926 -1.204  1.00 24.19 ? 177  GLU B CA  1 
ATOM   7157  C  C   . GLU B  1 177 ? -12.171 55.155 -0.718  1.00 23.76 ? 177  GLU B C   1 
ATOM   7158  O  O   . GLU B  1 177 ? -11.039 55.541 -0.986  1.00 23.40 ? 177  GLU B O   1 
ATOM   7159  C  CB  . GLU B  1 177 ? -13.632 55.549 -2.672  1.00 24.63 ? 177  GLU B CB  1 
ATOM   7160  C  CG  . GLU B  1 177 ? -14.828 56.205 -3.330  1.00 28.27 ? 177  GLU B CG  1 
ATOM   7161  C  CD  . GLU B  1 177 ? -16.140 55.897 -2.640  1.00 29.92 ? 177  GLU B CD  1 
ATOM   7162  O  OE1 . GLU B  1 177 ? -16.260 54.814 -2.038  1.00 31.24 ? 177  GLU B OE1 1 
ATOM   7163  O  OE2 . GLU B  1 177 ? -17.064 56.739 -2.712  1.00 33.16 ? 177  GLU B OE2 1 
ATOM   7164  N  N   . PRO B  1 178 ? -12.397 54.047 -0.007  1.00 24.36 ? 178  PRO B N   1 
ATOM   7165  C  CA  . PRO B  1 178 ? -11.355 53.183 0.550   1.00 24.61 ? 178  PRO B CA  1 
ATOM   7166  C  C   . PRO B  1 178 ? -10.235 52.776 -0.396  1.00 25.43 ? 178  PRO B C   1 
ATOM   7167  O  O   . PRO B  1 178 ? -9.073  52.714 0.011   1.00 24.85 ? 178  PRO B O   1 
ATOM   7168  C  CB  . PRO B  1 178 ? -12.148 51.980 1.048   1.00 24.83 ? 178  PRO B CB  1 
ATOM   7169  C  CG  . PRO B  1 178 ? -13.443 52.593 1.471   1.00 24.34 ? 178  PRO B CG  1 
ATOM   7170  C  CD  . PRO B  1 178 ? -13.735 53.518 0.314   1.00 24.09 ? 178  PRO B CD  1 
ATOM   7171  N  N   . ASN B  1 179 ? -10.574 52.511 -1.656  1.00 26.35 ? 179  ASN B N   1 
ATOM   7172  C  CA  . ASN B  1 179 ? -9.575  52.058 -2.630  1.00 28.11 ? 179  ASN B CA  1 
ATOM   7173  C  C   . ASN B  1 179 ? -9.032  53.134 -3.552  1.00 27.63 ? 179  ASN B C   1 
ATOM   7174  O  O   . ASN B  1 179 ? -8.276  52.834 -4.471  1.00 28.61 ? 179  ASN B O   1 
ATOM   7175  C  CB  . ASN B  1 179 ? -10.154 50.939 -3.500  1.00 29.95 ? 179  ASN B CB  1 
ATOM   7176  C  CG  . ASN B  1 179 ? -11.140 51.457 -4.536  1.00 31.95 ? 179  ASN B CG  1 
ATOM   7177  O  OD1 . ASN B  1 179 ? -12.142 52.081 -4.198  1.00 34.31 ? 179  ASN B OD1 1 
ATOM   7178  N  ND2 . ASN B  1 179 ? -10.853 51.202 -5.808  1.00 34.21 ? 179  ASN B ND2 1 
ATOM   7179  N  N   . LEU B  1 180 ? -9.409  54.383 -3.322  1.00 26.51 ? 180  LEU B N   1 
ATOM   7180  C  CA  . LEU B  1 180 ? -8.932  55.463 -4.180  1.00 25.25 ? 180  LEU B CA  1 
ATOM   7181  C  C   . LEU B  1 180 ? -7.819  56.293 -3.525  1.00 24.67 ? 180  LEU B C   1 
ATOM   7182  O  O   . LEU B  1 180 ? -7.605  56.225 -2.310  1.00 23.64 ? 180  LEU B O   1 
ATOM   7183  C  CB  . LEU B  1 180 ? -10.108 56.344 -4.586  1.00 24.91 ? 180  LEU B CB  1 
ATOM   7184  C  CG  . LEU B  1 180 ? -11.200 55.584 -5.351  1.00 25.58 ? 180  LEU B CG  1 
ATOM   7185  C  CD1 . LEU B  1 180 ? -12.312 56.554 -5.723  1.00 25.16 ? 180  LEU B CD1 1 
ATOM   7186  C  CD2 . LEU B  1 180 ? -10.615 54.932 -6.617  1.00 24.70 ? 180  LEU B CD2 1 
ATOM   7187  N  N   . PRO B  1 181 ? -7.079  57.072 -4.328  1.00 23.34 ? 181  PRO B N   1 
ATOM   7188  C  CA  . PRO B  1 181 ? -5.990  57.891 -3.770  1.00 22.24 ? 181  PRO B CA  1 
ATOM   7189  C  C   . PRO B  1 181 ? -6.473  58.903 -2.716  1.00 21.27 ? 181  PRO B C   1 
ATOM   7190  O  O   . PRO B  1 181 ? -7.590  59.403 -2.774  1.00 19.88 ? 181  PRO B O   1 
ATOM   7191  C  CB  . PRO B  1 181 ? -5.406  58.579 -5.004  1.00 22.14 ? 181  PRO B CB  1 
ATOM   7192  C  CG  . PRO B  1 181 ? -5.667  57.577 -6.104  1.00 23.73 ? 181  PRO B CG  1 
ATOM   7193  C  CD  . PRO B  1 181 ? -7.103  57.161 -5.798  1.00 22.96 ? 181  PRO B CD  1 
ATOM   7194  N  N   . SER B  1 182 ? -5.610  59.186 -1.752  1.00 20.07 ? 182  SER B N   1 
ATOM   7195  C  CA  . SER B  1 182 ? -5.913  60.127 -0.688  1.00 19.95 ? 182  SER B CA  1 
ATOM   7196  C  C   . SER B  1 182 ? -5.704  61.550 -1.167  1.00 19.12 ? 182  SER B C   1 
ATOM   7197  O  O   . SER B  1 182 ? -4.903  61.772 -2.069  1.00 16.93 ? 182  SER B O   1 
ATOM   7198  C  CB  . SER B  1 182 ? -4.958  59.893 0.484   1.00 20.54 ? 182  SER B CB  1 
ATOM   7199  O  OG  . SER B  1 182 ? -5.177  58.637 1.080   1.00 22.64 ? 182  SER B OG  1 
ATOM   7200  N  N   . TYR B  1 183 ? -6.428  62.497 -0.563  1.00 18.35 ? 183  TYR B N   1 
ATOM   7201  C  CA  . TYR B  1 183 ? -6.242  63.924 -0.844  1.00 17.72 ? 183  TYR B CA  1 
ATOM   7202  C  C   . TYR B  1 183 ? -5.488  64.465 0.380   1.00 18.28 ? 183  TYR B C   1 
ATOM   7203  O  O   . TYR B  1 183 ? -5.891  64.246 1.525   1.00 15.20 ? 183  TYR B O   1 
ATOM   7204  C  CB  . TYR B  1 183 ? -7.572  64.682 -0.956  1.00 16.68 ? 183  TYR B CB  1 
ATOM   7205  C  CG  . TYR B  1 183 ? -8.432  64.201 -2.088  1.00 17.48 ? 183  TYR B CG  1 
ATOM   7206  C  CD1 . TYR B  1 183 ? -8.289  64.718 -3.379  1.00 16.55 ? 183  TYR B CD1 1 
ATOM   7207  C  CD2 . TYR B  1 183 ? -9.344  63.171 -1.887  1.00 17.62 ? 183  TYR B CD2 1 
ATOM   7208  C  CE1 . TYR B  1 183 ? -9.038  64.209 -4.440  1.00 17.43 ? 183  TYR B CE1 1 
ATOM   7209  C  CE2 . TYR B  1 183 ? -10.091 62.652 -2.939  1.00 18.75 ? 183  TYR B CE2 1 
ATOM   7210  C  CZ  . TYR B  1 183 ? -9.934  63.169 -4.205  1.00 18.42 ? 183  TYR B CZ  1 
ATOM   7211  O  OH  . TYR B  1 183 ? -10.659 62.612 -5.228  1.00 21.50 ? 183  TYR B OH  1 
ATOM   7212  N  N   . ARG B  1 184 ? -4.386  65.155 0.112   1.00 18.45 ? 184  ARG B N   1 
ATOM   7213  C  CA  . ARG B  1 184 ? -3.561  65.764 1.130   1.00 19.66 ? 184  ARG B CA  1 
ATOM   7214  C  C   . ARG B  1 184 ? -4.249  67.036 1.577   1.00 18.74 ? 184  ARG B C   1 
ATOM   7215  O  O   . ARG B  1 184 ? -4.624  67.830 0.735   1.00 19.56 ? 184  ARG B O   1 
ATOM   7216  C  CB  . ARG B  1 184 ? -2.230  66.134 0.522   1.00 23.06 ? 184  ARG B CB  1 
ATOM   7217  C  CG  . ARG B  1 184 ? -1.084  65.426 1.112   1.00 27.72 ? 184  ARG B CG  1 
ATOM   7218  C  CD  . ARG B  1 184 ? -0.289  66.312 2.043   1.00 28.63 ? 184  ARG B CD  1 
ATOM   7219  N  NE  . ARG B  1 184 ? 1.092   66.140 1.664   1.00 29.58 ? 184  ARG B NE  1 
ATOM   7220  C  CZ  . ARG B  1 184 ? 2.159   66.514 2.355   1.00 30.70 ? 184  ARG B CZ  1 
ATOM   7221  N  NH1 . ARG B  1 184 ? 2.054   67.106 3.529   1.00 32.56 ? 184  ARG B NH1 1 
ATOM   7222  N  NH2 . ARG B  1 184 ? 3.355   66.303 1.830   1.00 30.24 ? 184  ARG B NH2 1 
ATOM   7223  N  N   . ILE B  1 185 ? -4.389  67.253 2.885   1.00 18.12 ? 185  ILE B N   1 
ATOM   7224  C  CA  . ILE B  1 185 ? -5.064  68.460 3.393   1.00 18.32 ? 185  ILE B CA  1 
ATOM   7225  C  C   . ILE B  1 185 ? -4.091  69.499 3.960   1.00 18.34 ? 185  ILE B C   1 
ATOM   7226  O  O   . ILE B  1 185 ? -4.357  70.690 3.846   1.00 17.82 ? 185  ILE B O   1 
ATOM   7227  C  CB  . ILE B  1 185 ? -6.108  68.108 4.506   1.00 17.19 ? 185  ILE B CB  1 
ATOM   7228  C  CG1 . ILE B  1 185 ? -7.042  66.991 4.016   1.00 17.90 ? 185  ILE B CG1 1 
ATOM   7229  C  CG2 . ILE B  1 185 ? -6.947  69.350 4.893   1.00 16.56 ? 185  ILE B CG2 1 
ATOM   7230  C  CD1 . ILE B  1 185 ? -7.931  67.359 2.812   1.00 18.30 ? 185  ILE B CD1 1 
ATOM   7231  N  N   . THR B  1 186 ? -2.997  69.053 4.590   1.00 17.70 ? 186  THR B N   1 
ATOM   7232  C  CA  . THR B  1 186 ? -1.987  69.969 5.152   1.00 17.98 ? 186  THR B CA  1 
ATOM   7233  C  C   . THR B  1 186 ? -0.580  69.560 4.699   1.00 18.47 ? 186  THR B C   1 
ATOM   7234  O  O   . THR B  1 186 ? -0.331  68.386 4.408   1.00 17.51 ? 186  THR B O   1 
ATOM   7235  C  CB  . THR B  1 186 ? -1.998  69.989 6.719   1.00 18.73 ? 186  THR B CB  1 
ATOM   7236  O  OG1 . THR B  1 186 ? -1.677  68.685 7.225   1.00 18.19 ? 186  THR B OG1 1 
ATOM   7237  C  CG2 . THR B  1 186 ? -3.360  70.417 7.243   1.00 17.41 ? 186  THR B CG2 1 
ATOM   7238  N  N   . TRP B  1 187 ? 0.336   70.527 4.632   1.00 18.90 ? 187  TRP B N   1 
ATOM   7239  C  CA  . TRP B  1 187 ? 1.722   70.261 4.204   1.00 19.93 ? 187  TRP B CA  1 
ATOM   7240  C  C   . TRP B  1 187 ? 2.730   70.790 5.224   1.00 18.67 ? 187  TRP B C   1 
ATOM   7241  O  O   . TRP B  1 187 ? 3.933   70.765 4.989   1.00 18.80 ? 187  TRP B O   1 
ATOM   7242  C  CB  . TRP B  1 187 ? 2.021   70.930 2.849   1.00 20.67 ? 187  TRP B CB  1 
ATOM   7243  C  CG  . TRP B  1 187 ? 1.495   70.199 1.649   1.00 22.41 ? 187  TRP B CG  1 
ATOM   7244  C  CD1 . TRP B  1 187 ? 2.208   69.414 0.785   1.00 22.15 ? 187  TRP B CD1 1 
ATOM   7245  C  CD2 . TRP B  1 187 ? 0.143   70.193 1.173   1.00 22.44 ? 187  TRP B CD2 1 
ATOM   7246  N  NE1 . TRP B  1 187 ? 1.383   68.924 -0.200  1.00 21.97 ? 187  TRP B NE1 1 
ATOM   7247  C  CE2 . TRP B  1 187 ? 0.112   69.386 0.015   1.00 22.22 ? 187  TRP B CE2 1 
ATOM   7248  C  CE3 . TRP B  1 187 ? -1.043  70.792 1.614   1.00 23.02 ? 187  TRP B CE3 1 
ATOM   7249  C  CZ2 . TRP B  1 187 ? -1.062  69.164 -0.706  1.00 22.11 ? 187  TRP B CZ2 1 
ATOM   7250  C  CZ3 . TRP B  1 187 ? -2.201  70.574 0.902   1.00 22.60 ? 187  TRP B CZ3 1 
ATOM   7251  C  CH2 . TRP B  1 187 ? -2.205  69.767 -0.246  1.00 22.32 ? 187  TRP B CH2 1 
ATOM   7252  N  N   . THR B  1 188 ? 2.232   71.236 6.363   1.00 18.13 ? 188  THR B N   1 
ATOM   7253  C  CA  . THR B  1 188 ? 3.070   71.800 7.405   1.00 17.22 ? 188  THR B CA  1 
ATOM   7254  C  C   . THR B  1 188 ? 3.530   70.834 8.496   1.00 17.11 ? 188  THR B C   1 
ATOM   7255  O  O   . THR B  1 188 ? 4.386   71.179 9.305   1.00 17.10 ? 188  THR B O   1 
ATOM   7256  C  CB  . THR B  1 188 ? 2.317   72.942 8.079   1.00 17.41 ? 188  THR B CB  1 
ATOM   7257  O  OG1 . THR B  1 188 ? 1.032   72.459 8.508   1.00 14.40 ? 188  THR B OG1 1 
ATOM   7258  C  CG2 . THR B  1 188 ? 2.150   74.124 7.098   1.00 17.33 ? 188  THR B CG2 1 
ATOM   7259  N  N   . GLY B  1 189 ? 2.956   69.640 8.526   1.00 17.41 ? 189  GLY B N   1 
ATOM   7260  C  CA  . GLY B  1 189 ? 3.324   68.683 9.546   1.00 18.27 ? 189  GLY B CA  1 
ATOM   7261  C  C   . GLY B  1 189 ? 4.820   68.582 9.747   1.00 18.94 ? 189  GLY B C   1 
ATOM   7262  O  O   . GLY B  1 189 ? 5.575   68.534 8.780   1.00 18.18 ? 189  GLY B O   1 
ATOM   7263  N  N   . LYS B  1 190 ? 5.263   68.535 10.998  1.00 19.56 ? 190  LYS B N   1 
ATOM   7264  C  CA  . LYS B  1 190 ? 6.702   68.433 11.266  1.00 20.10 ? 190  LYS B CA  1 
ATOM   7265  C  C   . LYS B  1 190 ? 6.841   67.753 12.630  1.00 19.47 ? 190  LYS B C   1 
ATOM   7266  O  O   . LYS B  1 190 ? 6.347   68.261 13.641  1.00 17.27 ? 190  LYS B O   1 
ATOM   7267  C  CB  . LYS B  1 190 ? 7.307   69.840 11.286  1.00 21.91 ? 190  LYS B CB  1 
ATOM   7268  C  CG  . LYS B  1 190 ? 8.834   69.928 11.138  1.00 25.59 ? 190  LYS B CG  1 
ATOM   7269  C  CD  . LYS B  1 190 ? 9.210   71.416 11.024  1.00 29.78 ? 190  LYS B CD  1 
ATOM   7270  C  CE  . LYS B  1 190 ? 10.669  71.669 10.659  1.00 32.36 ? 190  LYS B CE  1 
ATOM   7271  N  NZ  . LYS B  1 190 ? 11.606  71.244 11.721  1.00 33.54 ? 190  LYS B NZ  1 
ATOM   7272  N  N   . GLU B  1 191 ? 7.509   66.601 12.638  1.00 19.14 ? 191  GLU B N   1 
ATOM   7273  C  CA  . GLU B  1 191 ? 7.704   65.820 13.857  1.00 19.82 ? 191  GLU B CA  1 
ATOM   7274  C  C   . GLU B  1 191 ? 8.070   66.673 15.069  1.00 18.53 ? 191  GLU B C   1 
ATOM   7275  O  O   . GLU B  1 191 ? 8.990   67.456 14.999  1.00 16.55 ? 191  GLU B O   1 
ATOM   7276  C  CB  . GLU B  1 191 ? 8.789   64.760 13.637  1.00 22.08 ? 191  GLU B CB  1 
ATOM   7277  C  CG  . GLU B  1 191 ? 9.027   63.893 14.876  1.00 26.09 ? 191  GLU B CG  1 
ATOM   7278  C  CD  . GLU B  1 191 ? 9.928   62.679 14.609  1.00 28.76 ? 191  GLU B CD  1 
ATOM   7279  O  OE1 . GLU B  1 191 ? 11.048  62.847 14.088  1.00 30.16 ? 191  GLU B OE1 1 
ATOM   7280  O  OE2 . GLU B  1 191 ? 9.501   61.560 14.938  1.00 31.10 ? 191  GLU B OE2 1 
ATOM   7281  N  N   . ASP B  1 192 ? 7.338   66.501 16.172  1.00 18.54 ? 192  ASP B N   1 
ATOM   7282  C  CA  . ASP B  1 192 ? 7.546   67.254 17.416  1.00 18.80 ? 192  ASP B CA  1 
ATOM   7283  C  C   . ASP B  1 192 ? 7.405   68.765 17.289  1.00 18.66 ? 192  ASP B C   1 
ATOM   7284  O  O   . ASP B  1 192 ? 7.744   69.490 18.233  1.00 18.54 ? 192  ASP B O   1 
ATOM   7285  C  CB  . ASP B  1 192 ? 8.936   66.989 18.036  1.00 20.70 ? 192  ASP B CB  1 
ATOM   7286  C  CG  . ASP B  1 192 ? 9.189   65.533 18.321  1.00 21.53 ? 192  ASP B CG  1 
ATOM   7287  O  OD1 . ASP B  1 192 ? 8.269   64.842 18.794  1.00 22.71 ? 192  ASP B OD1 1 
ATOM   7288  O  OD2 . ASP B  1 192 ? 10.324  65.078 18.075  1.00 23.83 ? 192  ASP B OD2 1 
ATOM   7289  N  N   . ILE B  1 193 ? 6.930   69.254 16.144  1.00 18.11 ? 193  ILE B N   1 
ATOM   7290  C  CA  . ILE B  1 193 ? 6.815   70.697 15.964  1.00 18.18 ? 193  ILE B CA  1 
ATOM   7291  C  C   . ILE B  1 193 ? 5.444   71.197 15.543  1.00 17.16 ? 193  ILE B C   1 
ATOM   7292  O  O   . ILE B  1 193 ? 4.838   72.015 16.244  1.00 17.17 ? 193  ILE B O   1 
ATOM   7293  C  CB  . ILE B  1 193 ? 7.838   71.187 14.948  1.00 19.04 ? 193  ILE B CB  1 
ATOM   7294  C  CG1 . ILE B  1 193 ? 9.249   70.811 15.426  1.00 18.97 ? 193  ILE B CG1 1 
ATOM   7295  C  CG2 . ILE B  1 193 ? 7.695   72.692 14.761  1.00 18.05 ? 193  ILE B CG2 1 
ATOM   7296  C  CD1 . ILE B  1 193 ? 9.752   71.678 16.572  1.00 21.35 ? 193  ILE B CD1 1 
ATOM   7297  N  N   . ILE B  1 194 ? 4.979   70.739 14.385  1.00 15.91 ? 194  ILE B N   1 
ATOM   7298  C  CA  . ILE B  1 194 ? 3.670   71.119 13.892  1.00 14.88 ? 194  ILE B CA  1 
ATOM   7299  C  C   . ILE B  1 194 ? 2.821   69.852 13.845  1.00 15.07 ? 194  ILE B C   1 
ATOM   7300  O  O   . ILE B  1 194 ? 3.203   68.859 13.204  1.00 14.10 ? 194  ILE B O   1 
ATOM   7301  C  CB  . ILE B  1 194 ? 3.729   71.713 12.464  1.00 16.15 ? 194  ILE B CB  1 
ATOM   7302  C  CG1 . ILE B  1 194 ? 4.747   72.872 12.383  1.00 17.07 ? 194  ILE B CG1 1 
ATOM   7303  C  CG2 . ILE B  1 194 ? 2.334   72.169 12.056  1.00 15.40 ? 194  ILE B CG2 1 
ATOM   7304  C  CD1 . ILE B  1 194 ? 4.543   74.025 13.416  1.00 14.84 ? 194  ILE B CD1 1 
ATOM   7305  N  N   . TYR B  1 195 ? 1.686   69.879 14.542  1.00 14.65 ? 195  TYR B N   1 
ATOM   7306  C  CA  . TYR B  1 195 ? 0.763   68.737 14.577  1.00 14.65 ? 195  TYR B CA  1 
ATOM   7307  C  C   . TYR B  1 195 ? -0.557  69.152 13.940  1.00 14.97 ? 195  TYR B C   1 
ATOM   7308  O  O   . TYR B  1 195 ? -1.240  70.033 14.462  1.00 15.36 ? 195  TYR B O   1 
ATOM   7309  C  CB  . TYR B  1 195 ? 0.434   68.303 16.015  1.00 14.75 ? 195  TYR B CB  1 
ATOM   7310  C  CG  . TYR B  1 195 ? 1.618   67.978 16.912  1.00 15.78 ? 195  TYR B CG  1 
ATOM   7311  C  CD1 . TYR B  1 195 ? 2.450   68.989 17.393  1.00 15.06 ? 195  TYR B CD1 1 
ATOM   7312  C  CD2 . TYR B  1 195 ? 1.881   66.660 17.306  1.00 14.07 ? 195  TYR B CD2 1 
ATOM   7313  C  CE1 . TYR B  1 195 ? 3.513   68.702 18.255  1.00 16.53 ? 195  TYR B CE1 1 
ATOM   7314  C  CE2 . TYR B  1 195 ? 2.950   66.364 18.167  1.00 16.38 ? 195  TYR B CE2 1 
ATOM   7315  C  CZ  . TYR B  1 195 ? 3.749   67.387 18.634  1.00 16.15 ? 195  TYR B CZ  1 
ATOM   7316  O  OH  . TYR B  1 195 ? 4.764   67.104 19.496  1.00 17.53 ? 195  TYR B OH  1 
ATOM   7317  N  N   . ASN B  1 196 ? -0.913  68.535 12.820  1.00 13.99 ? 196  ASN B N   1 
ATOM   7318  C  CA  . ASN B  1 196 ? -2.185  68.838 12.185  1.00 13.31 ? 196  ASN B CA  1 
ATOM   7319  C  C   . ASN B  1 196 ? -3.128  67.673 12.424  1.00 14.19 ? 196  ASN B C   1 
ATOM   7320  O  O   . ASN B  1 196 ? -2.790  66.529 12.118  1.00 14.03 ? 196  ASN B O   1 
ATOM   7321  C  CB  . ASN B  1 196 ? -2.011  69.034 10.679  1.00 13.97 ? 196  ASN B CB  1 
ATOM   7322  C  CG  . ASN B  1 196 ? -1.165  70.256 10.350  1.00 14.46 ? 196  ASN B CG  1 
ATOM   7323  O  OD1 . ASN B  1 196 ? -1.593  71.399 10.554  1.00 12.95 ? 196  ASN B OD1 1 
ATOM   7324  N  ND2 . ASN B  1 196 ? 0.053   70.014 9.850   1.00 12.55 ? 196  ASN B ND2 1 
ATOM   7325  N  N   . GLY B  1 197 ? -4.299  67.943 12.990  1.00 14.25 ? 197  GLY B N   1 
ATOM   7326  C  CA  . GLY B  1 197 ? -5.240  66.862 13.188  1.00 14.34 ? 197  GLY B CA  1 
ATOM   7327  C  C   . GLY B  1 197 ? -4.991  65.960 14.381  1.00 14.23 ? 197  GLY B C   1 
ATOM   7328  O  O   . GLY B  1 197 ? -5.823  65.098 14.677  1.00 14.87 ? 197  GLY B O   1 
ATOM   7329  N  N   . ILE B  1 198 ? -3.842  66.114 15.031  1.00 13.23 ? 198  ILE B N   1 
ATOM   7330  C  CA  . ILE B  1 198 ? -3.541  65.346 16.229  1.00 13.47 ? 198  ILE B CA  1 
ATOM   7331  C  C   . ILE B  1 198 ? -3.012  66.323 17.278  1.00 13.28 ? 198  ILE B C   1 
ATOM   7332  O  O   . ILE B  1 198 ? -2.484  67.388 16.942  1.00 14.30 ? 198  ILE B O   1 
ATOM   7333  C  CB  . ILE B  1 198 ? -2.498  64.190 15.987  1.00 13.27 ? 198  ILE B CB  1 
ATOM   7334  C  CG1 . ILE B  1 198 ? -1.232  64.725 15.306  1.00 11.28 ? 198  ILE B CG1 1 
ATOM   7335  C  CG2 . ILE B  1 198 ? -3.161  63.059 15.174  1.00 12.19 ? 198  ILE B CG2 1 
ATOM   7336  C  CD1 . ILE B  1 198 ? -0.116  63.645 15.137  1.00 11.59 ? 198  ILE B CD1 1 
ATOM   7337  N  N   . THR B  1 199 ? -3.154  65.960 18.543  1.00 13.64 ? 199  THR B N   1 
ATOM   7338  C  CA  . THR B  1 199 ? -2.721  66.804 19.658  1.00 13.94 ? 199  THR B CA  1 
ATOM   7339  C  C   . THR B  1 199 ? -1.249  66.600 20.004  1.00 14.55 ? 199  THR B C   1 
ATOM   7340  O  O   . THR B  1 199 ? -0.663  65.585 19.651  1.00 15.04 ? 199  THR B O   1 
ATOM   7341  C  CB  . THR B  1 199 ? -3.520  66.441 20.931  1.00 14.28 ? 199  THR B CB  1 
ATOM   7342  O  OG1 . THR B  1 199 ? -3.529  65.020 21.073  1.00 13.50 ? 199  THR B OG1 1 
ATOM   7343  C  CG2 . THR B  1 199 ? -4.982  66.915 20.849  1.00 11.66 ? 199  THR B CG2 1 
ATOM   7344  N  N   . ASP B  1 200 ? -0.654  67.565 20.691  1.00 14.67 ? 200  ASP B N   1 
ATOM   7345  C  CA  . ASP B  1 200 ? 0.716   67.401 21.147  1.00 15.23 ? 200  ASP B CA  1 
ATOM   7346  C  C   . ASP B  1 200 ? 0.571   66.727 22.515  1.00 14.24 ? 200  ASP B C   1 
ATOM   7347  O  O   . ASP B  1 200 ? -0.538  66.310 22.878  1.00 13.76 ? 200  ASP B O   1 
ATOM   7348  C  CB  . ASP B  1 200 ? 1.471   68.747 21.233  1.00 15.34 ? 200  ASP B CB  1 
ATOM   7349  C  CG  . ASP B  1 200 ? 0.931   69.680 22.313  1.00 16.95 ? 200  ASP B CG  1 
ATOM   7350  O  OD1 . ASP B  1 200 ? -0.218  69.487 22.785  1.00 15.51 ? 200  ASP B OD1 1 
ATOM   7351  O  OD2 . ASP B  1 200 ? 1.672   70.627 22.680  1.00 15.92 ? 200  ASP B OD2 1 
ATOM   7352  N  N   . TRP B  1 201 ? 1.649   66.613 23.289  1.00 13.19 ? 201  TRP B N   1 
ATOM   7353  C  CA  . TRP B  1 201 ? 1.516   65.918 24.559  1.00 13.25 ? 201  TRP B CA  1 
ATOM   7354  C  C   . TRP B  1 201 ? 0.496   66.526 25.512  1.00 13.46 ? 201  TRP B C   1 
ATOM   7355  O  O   . TRP B  1 201 ? -0.407  65.840 26.006  1.00 13.46 ? 201  TRP B O   1 
ATOM   7356  C  CB  . TRP B  1 201 ? 2.861   65.825 25.306  1.00 13.19 ? 201  TRP B CB  1 
ATOM   7357  C  CG  . TRP B  1 201 ? 2.800   64.874 26.489  1.00 13.92 ? 201  TRP B CG  1 
ATOM   7358  C  CD1 . TRP B  1 201 ? 3.107   63.534 26.481  1.00 13.06 ? 201  TRP B CD1 1 
ATOM   7359  C  CD2 . TRP B  1 201 ? 2.308   65.158 27.819  1.00 14.01 ? 201  TRP B CD2 1 
ATOM   7360  N  NE1 . TRP B  1 201 ? 2.832   62.975 27.702  1.00 13.11 ? 201  TRP B NE1 1 
ATOM   7361  C  CE2 . TRP B  1 201 ? 2.341   63.941 28.543  1.00 14.23 ? 201  TRP B CE2 1 
ATOM   7362  C  CE3 . TRP B  1 201 ? 1.845   66.316 28.461  1.00 14.80 ? 201  TRP B CE3 1 
ATOM   7363  C  CZ2 . TRP B  1 201 ? 1.921   63.846 29.880  1.00 13.41 ? 201  TRP B CZ2 1 
ATOM   7364  C  CZ3 . TRP B  1 201 ? 1.428   66.229 29.800  1.00 13.62 ? 201  TRP B CZ3 1 
ATOM   7365  C  CH2 . TRP B  1 201 ? 1.469   64.996 30.491  1.00 14.73 ? 201  TRP B CH2 1 
ATOM   7366  N  N   . VAL B  1 202 ? 0.635   67.813 25.779  1.00 12.44 ? 202  VAL B N   1 
ATOM   7367  C  CA  . VAL B  1 202 ? -0.245  68.428 26.759  1.00 14.20 ? 202  VAL B CA  1 
ATOM   7368  C  C   . VAL B  1 202 ? -1.708  68.544 26.336  1.00 13.80 ? 202  VAL B C   1 
ATOM   7369  O  O   . VAL B  1 202 ? -2.600  68.428 27.180  1.00 14.10 ? 202  VAL B O   1 
ATOM   7370  C  CB  . VAL B  1 202 ? 0.298   69.809 27.231  1.00 13.74 ? 202  VAL B CB  1 
ATOM   7371  C  CG1 . VAL B  1 202 ? 0.011   70.886 26.188  1.00 11.43 ? 202  VAL B CG1 1 
ATOM   7372  C  CG2 . VAL B  1 202 ? -0.299  70.149 28.624  1.00 11.17 ? 202  VAL B CG2 1 
ATOM   7373  N  N   . TYR B  1 203 ? -1.972  68.743 25.051  1.00 12.64 ? 203  TYR B N   1 
ATOM   7374  C  CA  . TYR B  1 203 ? -3.360  68.817 24.614  1.00 14.01 ? 203  TYR B CA  1 
ATOM   7375  C  C   . TYR B  1 203 ? -3.962  67.418 24.703  1.00 14.35 ? 203  TYR B C   1 
ATOM   7376  O  O   . TYR B  1 203 ? -5.143  67.269 25.019  1.00 14.82 ? 203  TYR B O   1 
ATOM   7377  C  CB  . TYR B  1 203 ? -3.483  69.343 23.183  1.00 13.04 ? 203  TYR B CB  1 
ATOM   7378  C  CG  . TYR B  1 203 ? -3.742  70.828 23.112  1.00 13.23 ? 203  TYR B CG  1 
ATOM   7379  C  CD1 . TYR B  1 203 ? -2.694  71.740 23.032  1.00 14.01 ? 203  TYR B CD1 1 
ATOM   7380  C  CD2 . TYR B  1 203 ? -5.049  71.327 23.162  1.00 14.07 ? 203  TYR B CD2 1 
ATOM   7381  C  CE1 . TYR B  1 203 ? -2.941  73.120 23.005  1.00 14.76 ? 203  TYR B CE1 1 
ATOM   7382  C  CE2 . TYR B  1 203 ? -5.306  72.688 23.135  1.00 14.33 ? 203  TYR B CE2 1 
ATOM   7383  C  CZ  . TYR B  1 203 ? -4.253  73.584 23.054  1.00 15.84 ? 203  TYR B CZ  1 
ATOM   7384  O  OH  . TYR B  1 203 ? -4.526  74.935 22.992  1.00 15.61 ? 203  TYR B OH  1 
ATOM   7385  N  N   . GLU B  1 204 ? -3.148  66.393 24.443  1.00 13.00 ? 204  GLU B N   1 
ATOM   7386  C  CA  . GLU B  1 204 ? -3.644  65.025 24.522  1.00 12.94 ? 204  GLU B CA  1 
ATOM   7387  C  C   . GLU B  1 204 ? -4.052  64.677 25.954  1.00 13.17 ? 204  GLU B C   1 
ATOM   7388  O  O   . GLU B  1 204 ? -5.186  64.242 26.229  1.00 12.47 ? 204  GLU B O   1 
ATOM   7389  C  CB  . GLU B  1 204 ? -2.584  63.994 24.082  1.00 10.58 ? 204  GLU B CB  1 
ATOM   7390  C  CG  . GLU B  1 204 ? -3.062  62.570 24.335  1.00 12.81 ? 204  GLU B CG  1 
ATOM   7391  C  CD  . GLU B  1 204 ? -2.070  61.493 23.937  1.00 14.55 ? 204  GLU B CD  1 
ATOM   7392  O  OE1 . GLU B  1 204 ? -1.189  61.751 23.081  1.00 16.01 ? 204  GLU B OE1 1 
ATOM   7393  O  OE2 . GLU B  1 204 ? -2.193  60.373 24.484  1.00 16.19 ? 204  GLU B OE2 1 
ATOM   7394  N  N   . GLU B  1 205 ? -3.111  64.853 26.867  1.00 12.83 ? 205  GLU B N   1 
ATOM   7395  C  CA  . GLU B  1 205 ? -3.336  64.501 28.253  1.00 14.72 ? 205  GLU B CA  1 
ATOM   7396  C  C   . GLU B  1 205 ? -4.238  65.415 29.078  1.00 15.28 ? 205  GLU B C   1 
ATOM   7397  O  O   . GLU B  1 205 ? -5.073  64.937 29.831  1.00 15.85 ? 205  GLU B O   1 
ATOM   7398  C  CB  . GLU B  1 205 ? -1.978  64.371 28.958  1.00 15.67 ? 205  GLU B CB  1 
ATOM   7399  C  CG  . GLU B  1 205 ? -2.050  64.287 30.471  1.00 15.06 ? 205  GLU B CG  1 
ATOM   7400  C  CD  . GLU B  1 205 ? -2.611  62.974 30.970  1.00 16.69 ? 205  GLU B CD  1 
ATOM   7401  O  OE1 . GLU B  1 205 ? -2.705  62.010 30.175  1.00 16.05 ? 205  GLU B OE1 1 
ATOM   7402  O  OE2 . GLU B  1 205 ? -2.946  62.895 32.177  1.00 16.71 ? 205  GLU B OE2 1 
ATOM   7403  N  N   . GLU B  1 206 ? -4.103  66.724 28.921  1.00 14.66 ? 206  GLU B N   1 
ATOM   7404  C  CA  . GLU B  1 206 ? -4.847  67.639 29.762  1.00 14.32 ? 206  GLU B CA  1 
ATOM   7405  C  C   . GLU B  1 206 ? -6.077  68.349 29.204  1.00 16.74 ? 206  GLU B C   1 
ATOM   7406  O  O   . GLU B  1 206 ? -7.020  68.637 29.947  1.00 16.37 ? 206  GLU B O   1 
ATOM   7407  C  CB  . GLU B  1 206 ? -3.887  68.707 30.287  1.00 13.64 ? 206  GLU B CB  1 
ATOM   7408  C  CG  . GLU B  1 206 ? -2.619  68.152 30.911  1.00 14.30 ? 206  GLU B CG  1 
ATOM   7409  C  CD  . GLU B  1 206 ? -2.851  67.481 32.260  1.00 16.60 ? 206  GLU B CD  1 
ATOM   7410  O  OE1 . GLU B  1 206 ? -4.017  67.196 32.619  1.00 17.01 ? 206  GLU B OE1 1 
ATOM   7411  O  OE2 . GLU B  1 206 ? -1.855  67.228 32.972  1.00 16.61 ? 206  GLU B OE2 1 
ATOM   7412  N  N   . VAL B  1 207 ? -6.067  68.650 27.914  1.00 16.70 ? 207  VAL B N   1 
ATOM   7413  C  CA  . VAL B  1 207 ? -7.167  69.394 27.332  1.00 19.00 ? 207  VAL B CA  1 
ATOM   7414  C  C   . VAL B  1 207 ? -8.238  68.545 26.695  1.00 19.58 ? 207  VAL B C   1 
ATOM   7415  O  O   . VAL B  1 207 ? -9.386  68.637 27.087  1.00 19.92 ? 207  VAL B O   1 
ATOM   7416  C  CB  . VAL B  1 207 ? -6.662  70.411 26.285  1.00 19.08 ? 207  VAL B CB  1 
ATOM   7417  C  CG1 . VAL B  1 207 ? -7.833  71.305 25.822  1.00 19.20 ? 207  VAL B CG1 1 
ATOM   7418  C  CG2 . VAL B  1 207 ? -5.564  71.271 26.897  1.00 18.55 ? 207  VAL B CG2 1 
ATOM   7419  N  N   . PHE B  1 208 ? -7.867  67.709 25.731  1.00 20.28 ? 208  PHE B N   1 
ATOM   7420  C  CA  . PHE B  1 208 ? -8.843  66.875 25.030  1.00 21.73 ? 208  PHE B CA  1 
ATOM   7421  C  C   . PHE B  1 208 ? -9.013  65.438 25.509  1.00 22.29 ? 208  PHE B C   1 
ATOM   7422  O  O   . PHE B  1 208 ? -10.003 64.805 25.172  1.00 21.24 ? 208  PHE B O   1 
ATOM   7423  C  CB  . PHE B  1 208 ? -8.520  66.829 23.530  1.00 22.99 ? 208  PHE B CB  1 
ATOM   7424  C  CG  . PHE B  1 208 ? -8.741  68.135 22.824  1.00 26.58 ? 208  PHE B CG  1 
ATOM   7425  C  CD1 . PHE B  1 208 ? -9.990  68.751 22.847  1.00 28.85 ? 208  PHE B CD1 1 
ATOM   7426  C  CD2 . PHE B  1 208 ? -7.707  68.755 22.148  1.00 27.20 ? 208  PHE B CD2 1 
ATOM   7427  C  CE1 . PHE B  1 208 ? -10.201 69.984 22.197  1.00 29.78 ? 208  PHE B CE1 1 
ATOM   7428  C  CE2 . PHE B  1 208 ? -7.906  69.984 21.496  1.00 28.17 ? 208  PHE B CE2 1 
ATOM   7429  C  CZ  . PHE B  1 208 ? -9.143  70.592 21.522  1.00 27.75 ? 208  PHE B CZ  1 
ATOM   7430  N  N   . SER B  1 209 ? -8.058  64.910 26.268  1.00 22.46 ? 209  SER B N   1 
ATOM   7431  C  CA  . SER B  1 209 ? -8.138  63.523 26.718  1.00 23.08 ? 209  SER B CA  1 
ATOM   7432  C  C   . SER B  1 209 ? -8.340  62.631 25.521  1.00 23.65 ? 209  SER B C   1 
ATOM   7433  O  O   . SER B  1 209 ? -9.122  61.682 25.558  1.00 25.10 ? 209  SER B O   1 
ATOM   7434  C  CB  . SER B  1 209 ? -9.292  63.310 27.686  1.00 23.45 ? 209  SER B CB  1 
ATOM   7435  O  OG  . SER B  1 209 ? -8.868  63.515 29.016  1.00 24.60 ? 209  SER B OG  1 
ATOM   7436  N  N   . ALA B  1 210 ? -7.637  62.953 24.446  1.00 23.18 ? 210  ALA B N   1 
ATOM   7437  C  CA  . ALA B  1 210 ? -7.717  62.189 23.214  1.00 21.52 ? 210  ALA B CA  1 
ATOM   7438  C  C   . ALA B  1 210 ? -6.571  62.646 22.353  1.00 21.28 ? 210  ALA B C   1 
ATOM   7439  O  O   . ALA B  1 210 ? -6.045  63.745 22.525  1.00 22.15 ? 210  ALA B O   1 
ATOM   7440  C  CB  . ALA B  1 210 ? -9.041  62.454 22.499  1.00 21.76 ? 210  ALA B CB  1 
ATOM   7441  N  N   . TYR B  1 211 ? -6.206  61.804 21.409  1.00 20.19 ? 211  TYR B N   1 
ATOM   7442  C  CA  . TYR B  1 211 ? -5.116  62.096 20.516  1.00 20.52 ? 211  TYR B CA  1 
ATOM   7443  C  C   . TYR B  1 211 ? -5.572  62.850 19.274  1.00 20.21 ? 211  TYR B C   1 
ATOM   7444  O  O   . TYR B  1 211 ? -4.851  63.716 18.781  1.00 20.20 ? 211  TYR B O   1 
ATOM   7445  C  CB  . TYR B  1 211 ? -4.452  60.784 20.128  1.00 19.84 ? 211  TYR B CB  1 
ATOM   7446  C  CG  . TYR B  1 211 ? -3.211  60.898 19.292  1.00 20.47 ? 211  TYR B CG  1 
ATOM   7447  C  CD1 . TYR B  1 211 ? -2.283  61.916 19.513  1.00 19.57 ? 211  TYR B CD1 1 
ATOM   7448  C  CD2 . TYR B  1 211 ? -2.907  59.921 18.343  1.00 20.26 ? 211  TYR B CD2 1 
ATOM   7449  C  CE1 . TYR B  1 211 ? -1.093  61.950 18.818  1.00 18.32 ? 211  TYR B CE1 1 
ATOM   7450  C  CE2 . TYR B  1 211 ? -1.712  59.945 17.649  1.00 20.44 ? 211  TYR B CE2 1 
ATOM   7451  C  CZ  . TYR B  1 211 ? -0.808  60.956 17.892  1.00 20.21 ? 211  TYR B CZ  1 
ATOM   7452  O  OH  . TYR B  1 211 ? 0.415   60.945 17.253  1.00 20.56 ? 211  TYR B OH  1 
ATOM   7453  N  N   . SER B  1 212 ? -6.763  62.533 18.772  1.00 18.94 ? 212  SER B N   1 
ATOM   7454  C  CA  . SER B  1 212 ? -7.231  63.195 17.569  1.00 19.28 ? 212  SER B CA  1 
ATOM   7455  C  C   . SER B  1 212 ? -7.653  64.630 17.806  1.00 17.75 ? 212  SER B C   1 
ATOM   7456  O  O   . SER B  1 212 ? -8.142  64.991 18.866  1.00 17.89 ? 212  SER B O   1 
ATOM   7457  C  CB  . SER B  1 212 ? -8.376  62.421 16.912  1.00 18.88 ? 212  SER B CB  1 
ATOM   7458  O  OG  . SER B  1 212 ? -9.512  62.399 17.740  1.00 23.30 ? 212  SER B OG  1 
ATOM   7459  N  N   . ALA B  1 213 ? -7.416  65.449 16.795  1.00 17.14 ? 213  ALA B N   1 
ATOM   7460  C  CA  . ALA B  1 213 ? -7.766  66.850 16.831  1.00 16.84 ? 213  ALA B CA  1 
ATOM   7461  C  C   . ALA B  1 213 ? -8.439  67.155 15.505  1.00 16.46 ? 213  ALA B C   1 
ATOM   7462  O  O   . ALA B  1 213 ? -8.082  68.115 14.817  1.00 14.66 ? 213  ALA B O   1 
ATOM   7463  C  CB  . ALA B  1 213 ? -6.517  67.720 17.004  1.00 16.14 ? 213  ALA B CB  1 
ATOM   7464  N  N   . LEU B  1 214 ? -9.363  66.288 15.108  1.00 16.91 ? 214  LEU B N   1 
ATOM   7465  C  CA  . LEU B  1 214 ? -10.149 66.550 13.907  1.00 18.10 ? 214  LEU B CA  1 
ATOM   7466  C  C   . LEU B  1 214 ? -11.582 66.137 14.206  1.00 18.12 ? 214  LEU B C   1 
ATOM   7467  O  O   . LEU B  1 214 ? -11.828 65.198 14.970  1.00 19.30 ? 214  LEU B O   1 
ATOM   7468  C  CB  . LEU B  1 214 ? -9.583  65.855 12.662  1.00 19.26 ? 214  LEU B CB  1 
ATOM   7469  C  CG  . LEU B  1 214 ? -9.183  64.390 12.699  1.00 20.30 ? 214  LEU B CG  1 
ATOM   7470  C  CD1 . LEU B  1 214 ? -10.423 63.541 12.773  1.00 20.33 ? 214  LEU B CD1 1 
ATOM   7471  C  CD2 . LEU B  1 214 ? -8.372  64.070 11.456  1.00 18.38 ? 214  LEU B CD2 1 
ATOM   7472  N  N   . TRP B  1 215 ? -12.520 66.862 13.608  1.00 17.26 ? 215  TRP B N   1 
ATOM   7473  C  CA  . TRP B  1 215 ? -13.939 66.650 13.855  1.00 16.97 ? 215  TRP B CA  1 
ATOM   7474  C  C   . TRP B  1 215 ? -14.772 66.752 12.587  1.00 16.68 ? 215  TRP B C   1 
ATOM   7475  O  O   . TRP B  1 215 ? -14.904 67.838 12.038  1.00 16.69 ? 215  TRP B O   1 
ATOM   7476  C  CB  . TRP B  1 215 ? -14.425 67.722 14.831  1.00 16.37 ? 215  TRP B CB  1 
ATOM   7477  C  CG  . TRP B  1 215 ? -13.707 67.721 16.144  1.00 17.20 ? 215  TRP B CG  1 
ATOM   7478  C  CD1 . TRP B  1 215 ? -14.060 67.025 17.266  1.00 17.21 ? 215  TRP B CD1 1 
ATOM   7479  C  CD2 . TRP B  1 215 ? -12.482 68.401 16.461  1.00 17.62 ? 215  TRP B CD2 1 
ATOM   7480  N  NE1 . TRP B  1 215 ? -13.131 67.226 18.259  1.00 19.26 ? 215  TRP B NE1 1 
ATOM   7481  C  CE2 . TRP B  1 215 ? -12.152 68.064 17.795  1.00 17.53 ? 215  TRP B CE2 1 
ATOM   7482  C  CE3 . TRP B  1 215 ? -11.632 69.258 15.749  1.00 16.72 ? 215  TRP B CE3 1 
ATOM   7483  C  CZ2 . TRP B  1 215 ? -11.009 68.553 18.431  1.00 17.49 ? 215  TRP B CZ2 1 
ATOM   7484  C  CZ3 . TRP B  1 215 ? -10.496 69.744 16.379  1.00 17.70 ? 215  TRP B CZ3 1 
ATOM   7485  C  CH2 . TRP B  1 215 ? -10.193 69.390 17.709  1.00 17.14 ? 215  TRP B CH2 1 
ATOM   7486  N  N   . TRP B  1 216 ? -15.334 65.632 12.144  1.00 16.69 ? 216  TRP B N   1 
ATOM   7487  C  CA  . TRP B  1 216 ? -16.187 65.591 10.956  1.00 17.05 ? 216  TRP B CA  1 
ATOM   7488  C  C   . TRP B  1 216 ? -17.516 66.286 11.250  1.00 18.04 ? 216  TRP B C   1 
ATOM   7489  O  O   . TRP B  1 216 ? -18.034 66.176 12.364  1.00 17.88 ? 216  TRP B O   1 
ATOM   7490  C  CB  . TRP B  1 216 ? -16.526 64.143 10.596  1.00 15.77 ? 216  TRP B CB  1 
ATOM   7491  C  CG  . TRP B  1 216 ? -15.474 63.387 9.890   1.00 15.99 ? 216  TRP B CG  1 
ATOM   7492  C  CD1 . TRP B  1 216 ? -14.673 62.398 10.404  1.00 15.75 ? 216  TRP B CD1 1 
ATOM   7493  C  CD2 . TRP B  1 216 ? -15.169 63.472 8.500   1.00 15.91 ? 216  TRP B CD2 1 
ATOM   7494  N  NE1 . TRP B  1 216 ? -13.895 61.853 9.402   1.00 16.27 ? 216  TRP B NE1 1 
ATOM   7495  C  CE2 . TRP B  1 216 ? -14.179 62.495 8.224   1.00 16.50 ? 216  TRP B CE2 1 
ATOM   7496  C  CE3 . TRP B  1 216 ? -15.637 64.276 7.455   1.00 16.73 ? 216  TRP B CE3 1 
ATOM   7497  C  CZ2 . TRP B  1 216 ? -13.649 62.300 6.934   1.00 15.33 ? 216  TRP B CZ2 1 
ATOM   7498  C  CZ3 . TRP B  1 216 ? -15.107 64.083 6.172   1.00 16.92 ? 216  TRP B CZ3 1 
ATOM   7499  C  CH2 . TRP B  1 216 ? -14.125 63.103 5.930   1.00 15.75 ? 216  TRP B CH2 1 
ATOM   7500  N  N   . SER B  1 217 ? -18.082 66.979 10.264  1.00 17.92 ? 217  SER B N   1 
ATOM   7501  C  CA  . SER B  1 217 ? -19.379 67.598 10.466  1.00 18.42 ? 217  SER B CA  1 
ATOM   7502  C  C   . SER B  1 217 ? -20.364 66.415 10.491  1.00 19.73 ? 217  SER B C   1 
ATOM   7503  O  O   . SER B  1 217 ? -20.018 65.306 10.075  1.00 19.94 ? 217  SER B O   1 
ATOM   7504  C  CB  . SER B  1 217 ? -19.702 68.578 9.328   1.00 18.58 ? 217  SER B CB  1 
ATOM   7505  O  OG  . SER B  1 217 ? -19.881 67.927 8.088   1.00 16.78 ? 217  SER B OG  1 
ATOM   7506  N  N   . PRO B  1 218 ? -21.599 66.633 10.964  1.00 19.79 ? 218  PRO B N   1 
ATOM   7507  C  CA  . PRO B  1 218 ? -22.604 65.564 11.052  1.00 20.90 ? 218  PRO B CA  1 
ATOM   7508  C  C   . PRO B  1 218 ? -22.803 64.620 9.875   1.00 21.06 ? 218  PRO B C   1 
ATOM   7509  O  O   . PRO B  1 218 ? -22.776 63.408 10.056  1.00 21.93 ? 218  PRO B O   1 
ATOM   7510  C  CB  . PRO B  1 218 ? -23.880 66.318 11.439  1.00 20.30 ? 218  PRO B CB  1 
ATOM   7511  C  CG  . PRO B  1 218 ? -23.337 67.423 12.299  1.00 19.79 ? 218  PRO B CG  1 
ATOM   7512  C  CD  . PRO B  1 218 ? -22.148 67.902 11.469  1.00 19.99 ? 218  PRO B CD  1 
ATOM   7513  N  N   . ASN B  1 219 ? -23.013 65.150 8.679   1.00 21.00 ? 219  ASN B N   1 
ATOM   7514  C  CA  . ASN B  1 219 ? -23.201 64.265 7.546   1.00 21.55 ? 219  ASN B CA  1 
ATOM   7515  C  C   . ASN B  1 219 ? -21.884 64.042 6.781   1.00 20.48 ? 219  ASN B C   1 
ATOM   7516  O  O   . ASN B  1 219 ? -21.882 63.478 5.699   1.00 17.96 ? 219  ASN B O   1 
ATOM   7517  C  CB  . ASN B  1 219 ? -24.303 64.801 6.614   1.00 22.51 ? 219  ASN B CB  1 
ATOM   7518  C  CG  . ASN B  1 219 ? -23.879 66.027 5.854   1.00 25.23 ? 219  ASN B CG  1 
ATOM   7519  O  OD1 . ASN B  1 219 ? -22.692 66.350 5.771   1.00 24.79 ? 219  ASN B OD1 1 
ATOM   7520  N  ND2 . ASN B  1 219 ? -24.849 66.714 5.265   1.00 28.22 ? 219  ASN B ND2 1 
ATOM   7521  N  N   . GLY B  1 220 ? -20.773 64.508 7.350   1.00 20.03 ? 220  GLY B N   1 
ATOM   7522  C  CA  . GLY B  1 220 ? -19.473 64.296 6.733   1.00 19.44 ? 220  GLY B CA  1 
ATOM   7523  C  C   . GLY B  1 220 ? -18.971 65.227 5.647   1.00 19.81 ? 220  GLY B C   1 
ATOM   7524  O  O   . GLY B  1 220 ? -17.890 64.996 5.083   1.00 19.14 ? 220  GLY B O   1 
ATOM   7525  N  N   . THR B  1 221 ? -19.722 66.273 5.333   1.00 18.66 ? 221  THR B N   1 
ATOM   7526  C  CA  . THR B  1 221 ? -19.275 67.199 4.300   1.00 18.66 ? 221  THR B CA  1 
ATOM   7527  C  C   . THR B  1 221 ? -18.013 67.967 4.715   1.00 19.13 ? 221  THR B C   1 
ATOM   7528  O  O   . THR B  1 221 ? -17.050 68.054 3.954   1.00 18.47 ? 221  THR B O   1 
ATOM   7529  C  CB  . THR B  1 221 ? -20.376 68.216 3.953   1.00 19.25 ? 221  THR B CB  1 
ATOM   7530  O  OG1 . THR B  1 221 ? -21.450 67.539 3.288   1.00 20.90 ? 221  THR B OG1 1 
ATOM   7531  C  CG2 . THR B  1 221 ? -19.825 69.318 3.034   1.00 18.93 ? 221  THR B CG2 1 
ATOM   7532  N  N   . PHE B  1 222 ? -18.020 68.529 5.920   1.00 18.02 ? 222  PHE B N   1 
ATOM   7533  C  CA  . PHE B  1 222 ? -16.876 69.308 6.384   1.00 16.88 ? 222  PHE B CA  1 
ATOM   7534  C  C   . PHE B  1 222 ? -15.976 68.535 7.337   1.00 15.88 ? 222  PHE B C   1 
ATOM   7535  O  O   . PHE B  1 222 ? -16.429 67.654 8.077   1.00 14.18 ? 222  PHE B O   1 
ATOM   7536  C  CB  . PHE B  1 222 ? -17.341 70.557 7.132   1.00 16.76 ? 222  PHE B CB  1 
ATOM   7537  C  CG  . PHE B  1 222 ? -18.087 71.543 6.291   1.00 16.58 ? 222  PHE B CG  1 
ATOM   7538  C  CD1 . PHE B  1 222 ? -17.421 72.303 5.329   1.00 16.49 ? 222  PHE B CD1 1 
ATOM   7539  C  CD2 . PHE B  1 222 ? -19.447 71.750 6.489   1.00 16.94 ? 222  PHE B CD2 1 
ATOM   7540  C  CE1 . PHE B  1 222 ? -18.095 73.255 4.582   1.00 16.47 ? 222  PHE B CE1 1 
ATOM   7541  C  CE2 . PHE B  1 222 ? -20.142 72.707 5.742   1.00 16.96 ? 222  PHE B CE2 1 
ATOM   7542  C  CZ  . PHE B  1 222 ? -19.469 73.459 4.791   1.00 18.46 ? 222  PHE B CZ  1 
ATOM   7543  N  N   . LEU B  1 223 ? -14.697 68.883 7.317   1.00 15.73 ? 223  LEU B N   1 
ATOM   7544  C  CA  . LEU B  1 223 ? -13.723 68.291 8.225   1.00 15.13 ? 223  LEU B CA  1 
ATOM   7545  C  C   . LEU B  1 223 ? -13.028 69.455 8.928   1.00 15.01 ? 223  LEU B C   1 
ATOM   7546  O  O   . LEU B  1 223 ? -12.340 70.272 8.301   1.00 15.22 ? 223  LEU B O   1 
ATOM   7547  C  CB  . LEU B  1 223 ? -12.687 67.436 7.482   1.00 14.98 ? 223  LEU B CB  1 
ATOM   7548  C  CG  . LEU B  1 223 ? -11.604 66.898 8.427   1.00 15.83 ? 223  LEU B CG  1 
ATOM   7549  C  CD1 . LEU B  1 223 ? -12.239 65.946 9.460   1.00 14.37 ? 223  LEU B CD1 1 
ATOM   7550  C  CD2 . LEU B  1 223 ? -10.519 66.190 7.617   1.00 15.35 ? 223  LEU B CD2 1 
ATOM   7551  N  N   . ALA B  1 224 ? -13.229 69.539 10.233  1.00 14.70 ? 224  ALA B N   1 
ATOM   7552  C  CA  . ALA B  1 224 ? -12.623 70.612 11.008  1.00 14.45 ? 224  ALA B CA  1 
ATOM   7553  C  C   . ALA B  1 224 ? -11.414 70.011 11.697  1.00 13.79 ? 224  ALA B C   1 
ATOM   7554  O  O   . ALA B  1 224 ? -11.387 68.815 11.940  1.00 14.27 ? 224  ALA B O   1 
ATOM   7555  C  CB  . ALA B  1 224 ? -13.625 71.139 12.046  1.00 13.57 ? 224  ALA B CB  1 
ATOM   7556  N  N   . TYR B  1 225 ? -10.404 70.820 11.987  1.00 12.99 ? 225  TYR B N   1 
ATOM   7557  C  CA  . TYR B  1 225 ? -9.244  70.289 12.674  1.00 14.16 ? 225  TYR B CA  1 
ATOM   7558  C  C   . TYR B  1 225 ? -8.445  71.387 13.295  1.00 14.30 ? 225  TYR B C   1 
ATOM   7559  O  O   . TYR B  1 225 ? -8.557  72.541 12.880  1.00 15.40 ? 225  TYR B O   1 
ATOM   7560  C  CB  . TYR B  1 225 ? -8.324  69.507 11.723  1.00 13.36 ? 225  TYR B CB  1 
ATOM   7561  C  CG  . TYR B  1 225 ? -7.755  70.319 10.591  1.00 14.56 ? 225  TYR B CG  1 
ATOM   7562  C  CD1 . TYR B  1 225 ? -8.453  70.446 9.387   1.00 14.99 ? 225  TYR B CD1 1 
ATOM   7563  C  CD2 . TYR B  1 225 ? -6.501  70.925 10.696  1.00 15.39 ? 225  TYR B CD2 1 
ATOM   7564  C  CE1 . TYR B  1 225 ? -7.925  71.141 8.320   1.00 13.72 ? 225  TYR B CE1 1 
ATOM   7565  C  CE2 . TYR B  1 225 ? -5.954  71.636 9.622   1.00 14.38 ? 225  TYR B CE2 1 
ATOM   7566  C  CZ  . TYR B  1 225 ? -6.679  71.736 8.442   1.00 15.90 ? 225  TYR B CZ  1 
ATOM   7567  O  OH  . TYR B  1 225 ? -6.165  72.447 7.388   1.00 16.28 ? 225  TYR B OH  1 
ATOM   7568  N  N   . ALA B  1 226 ? -7.641  71.033 14.289  1.00 13.51 ? 226  ALA B N   1 
ATOM   7569  C  CA  . ALA B  1 226 ? -6.771  72.008 14.942  1.00 13.46 ? 226  ALA B CA  1 
ATOM   7570  C  C   . ALA B  1 226 ? -5.323  71.747 14.517  1.00 13.84 ? 226  ALA B C   1 
ATOM   7571  O  O   . ALA B  1 226 ? -4.969  70.634 14.113  1.00 12.64 ? 226  ALA B O   1 
ATOM   7572  C  CB  . ALA B  1 226 ? -6.872  71.872 16.450  1.00 13.26 ? 226  ALA B CB  1 
ATOM   7573  N  N   . GLN B  1 227 ? -4.498  72.780 14.627  1.00 13.43 ? 227  GLN B N   1 
ATOM   7574  C  CA  . GLN B  1 227 ? -3.086  72.677 14.306  1.00 15.20 ? 227  GLN B CA  1 
ATOM   7575  C  C   . GLN B  1 227 ? -2.321  73.233 15.509  1.00 15.45 ? 227  GLN B C   1 
ATOM   7576  O  O   . GLN B  1 227 ? -2.588  74.357 15.954  1.00 14.24 ? 227  GLN B O   1 
ATOM   7577  C  CB  . GLN B  1 227 ? -2.749  73.513 13.078  1.00 15.48 ? 227  GLN B CB  1 
ATOM   7578  C  CG  . GLN B  1 227 ? -1.274  73.525 12.763  1.00 16.34 ? 227  GLN B CG  1 
ATOM   7579  C  CD  . GLN B  1 227 ? -0.954  74.576 11.729  1.00 19.17 ? 227  GLN B CD  1 
ATOM   7580  O  OE1 . GLN B  1 227 ? -0.799  75.761 12.054  1.00 18.94 ? 227  GLN B OE1 1 
ATOM   7581  N  NE2 . GLN B  1 227 ? -0.884  74.157 10.462  1.00 18.24 ? 227  GLN B NE2 1 
ATOM   7582  N  N   . PHE B  1 228 ? -1.397  72.445 16.055  1.00 15.58 ? 228  PHE B N   1 
ATOM   7583  C  CA  . PHE B  1 228 ? -0.621  72.897 17.202  1.00 15.34 ? 228  PHE B CA  1 
ATOM   7584  C  C   . PHE B  1 228 ? 0.812   73.156 16.779  1.00 16.53 ? 228  PHE B C   1 
ATOM   7585  O  O   . PHE B  1 228 ? 1.388   72.423 15.963  1.00 16.16 ? 228  PHE B O   1 
ATOM   7586  C  CB  . PHE B  1 228 ? -0.676  71.855 18.321  1.00 15.45 ? 228  PHE B CB  1 
ATOM   7587  C  CG  . PHE B  1 228 ? -2.095  71.457 18.698  1.00 15.14 ? 228  PHE B CG  1 
ATOM   7588  C  CD1 . PHE B  1 228 ? -2.874  72.278 19.512  1.00 14.85 ? 228  PHE B CD1 1 
ATOM   7589  C  CD2 . PHE B  1 228 ? -2.663  70.284 18.191  1.00 15.31 ? 228  PHE B CD2 1 
ATOM   7590  C  CE1 . PHE B  1 228 ? -4.208  71.938 19.822  1.00 14.74 ? 228  PHE B CE1 1 
ATOM   7591  C  CE2 . PHE B  1 228 ? -3.993  69.927 18.487  1.00 15.47 ? 228  PHE B CE2 1 
ATOM   7592  C  CZ  . PHE B  1 228 ? -4.766  70.758 19.304  1.00 16.35 ? 228  PHE B CZ  1 
ATOM   7593  N  N   . ASN B  1 229 ? 1.362   74.240 17.309  1.00 16.87 ? 229  ASN B N   1 
ATOM   7594  C  CA  . ASN B  1 229 ? 2.731   74.618 17.015  1.00 18.09 ? 229  ASN B CA  1 
ATOM   7595  C  C   . ASN B  1 229 ? 3.508   74.582 18.319  1.00 16.63 ? 229  ASN B C   1 
ATOM   7596  O  O   . ASN B  1 229 ? 3.261   75.383 19.217  1.00 17.98 ? 229  ASN B O   1 
ATOM   7597  C  CB  . ASN B  1 229 ? 2.768   76.022 16.422  1.00 17.81 ? 229  ASN B CB  1 
ATOM   7598  C  CG  . ASN B  1 229 ? 4.089   76.334 15.781  1.00 20.56 ? 229  ASN B CG  1 
ATOM   7599  O  OD1 . ASN B  1 229 ? 5.129   75.858 16.246  1.00 18.05 ? 229  ASN B OD1 1 
ATOM   7600  N  ND2 . ASN B  1 229 ? 4.065   77.134 14.712  1.00 21.31 ? 229  ASN B ND2 1 
ATOM   7601  N  N   . ASP B  1 230 ? 4.443   73.650 18.421  1.00 16.87 ? 230  ASP B N   1 
ATOM   7602  C  CA  . ASP B  1 230 ? 5.249   73.498 19.629  1.00 16.71 ? 230  ASP B CA  1 
ATOM   7603  C  C   . ASP B  1 230 ? 6.686   73.973 19.443  1.00 17.52 ? 230  ASP B C   1 
ATOM   7604  O  O   . ASP B  1 230 ? 7.560   73.622 20.234  1.00 16.11 ? 230  ASP B O   1 
ATOM   7605  C  CB  . ASP B  1 230 ? 5.270   72.031 20.043  1.00 16.56 ? 230  ASP B CB  1 
ATOM   7606  C  CG  . ASP B  1 230 ? 3.953   71.578 20.628  1.00 17.81 ? 230  ASP B CG  1 
ATOM   7607  O  OD1 . ASP B  1 230 ? 2.918   71.672 19.929  1.00 18.05 ? 230  ASP B OD1 1 
ATOM   7608  O  OD2 . ASP B  1 230 ? 3.963   71.132 21.787  1.00 17.87 ? 230  ASP B OD2 1 
ATOM   7609  N  N   . THR B  1 231 ? 6.927   74.772 18.409  1.00 17.59 ? 231  THR B N   1 
ATOM   7610  C  CA  . THR B  1 231 ? 8.280   75.261 18.099  1.00 19.16 ? 231  THR B CA  1 
ATOM   7611  C  C   . THR B  1 231 ? 9.100   75.721 19.293  1.00 19.94 ? 231  THR B C   1 
ATOM   7612  O  O   . THR B  1 231 ? 10.275  75.361 19.434  1.00 21.96 ? 231  THR B O   1 
ATOM   7613  C  CB  . THR B  1 231 ? 8.239   76.446 17.102  1.00 18.41 ? 231  THR B CB  1 
ATOM   7614  O  OG1 . THR B  1 231 ? 7.625   76.017 15.881  1.00 17.63 ? 231  THR B OG1 1 
ATOM   7615  C  CG2 . THR B  1 231 ? 9.667   76.962 16.809  1.00 19.24 ? 231  THR B CG2 1 
ATOM   7616  N  N   . GLU B  1 232 ? 8.499   76.528 20.150  1.00 19.41 ? 232  GLU B N   1 
ATOM   7617  C  CA  . GLU B  1 232 ? 9.237   77.039 21.293  1.00 20.82 ? 232  GLU B CA  1 
ATOM   7618  C  C   . GLU B  1 232 ? 8.933   76.358 22.624  1.00 18.78 ? 232  GLU B C   1 
ATOM   7619  O  O   . GLU B  1 232 ? 9.343   76.840 23.673  1.00 17.09 ? 232  GLU B O   1 
ATOM   7620  C  CB  . GLU B  1 232 ? 8.993   78.541 21.404  1.00 23.58 ? 232  GLU B CB  1 
ATOM   7621  C  CG  . GLU B  1 232 ? 9.745   79.305 20.327  1.00 29.56 ? 232  GLU B CG  1 
ATOM   7622  C  CD  . GLU B  1 232 ? 9.388   80.773 20.309  1.00 32.57 ? 232  GLU B CD  1 
ATOM   7623  O  OE1 . GLU B  1 232 ? 8.268   81.114 19.859  1.00 34.13 ? 232  GLU B OE1 1 
ATOM   7624  O  OE2 . GLU B  1 232 ? 10.226  81.578 20.764  1.00 35.72 ? 232  GLU B OE2 1 
ATOM   7625  N  N   . VAL B  1 233 ? 8.207   75.247 22.583  1.00 17.51 ? 233  VAL B N   1 
ATOM   7626  C  CA  . VAL B  1 233 ? 7.887   74.544 23.819  1.00 17.35 ? 233  VAL B CA  1 
ATOM   7627  C  C   . VAL B  1 233 ? 9.125   73.769 24.268  1.00 17.08 ? 233  VAL B C   1 
ATOM   7628  O  O   . VAL B  1 233 ? 9.706   73.043 23.479  1.00 16.61 ? 233  VAL B O   1 
ATOM   7629  C  CB  . VAL B  1 233 ? 6.699   73.585 23.588  1.00 17.02 ? 233  VAL B CB  1 
ATOM   7630  C  CG1 . VAL B  1 233 ? 6.460   72.701 24.821  1.00 16.10 ? 233  VAL B CG1 1 
ATOM   7631  C  CG2 . VAL B  1 233 ? 5.447   74.416 23.265  1.00 16.04 ? 233  VAL B CG2 1 
ATOM   7632  N  N   . PRO B  1 234 ? 9.559   73.935 25.536  1.00 16.33 ? 234  PRO B N   1 
ATOM   7633  C  CA  . PRO B  1 234 ? 10.750  73.196 25.993  1.00 17.05 ? 234  PRO B CA  1 
ATOM   7634  C  C   . PRO B  1 234 ? 10.480  71.687 26.014  1.00 17.80 ? 234  PRO B C   1 
ATOM   7635  O  O   . PRO B  1 234 ? 9.323   71.246 26.147  1.00 16.73 ? 234  PRO B O   1 
ATOM   7636  C  CB  . PRO B  1 234 ? 11.007  73.746 27.408  1.00 16.92 ? 234  PRO B CB  1 
ATOM   7637  C  CG  . PRO B  1 234 ? 10.270  75.086 27.431  1.00 16.74 ? 234  PRO B CG  1 
ATOM   7638  C  CD  . PRO B  1 234 ? 9.027   74.799 26.603  1.00 15.75 ? 234  PRO B CD  1 
ATOM   7639  N  N   . LEU B  1 235 ? 11.556  70.907 25.896  1.00 16.50 ? 235  LEU B N   1 
ATOM   7640  C  CA  . LEU B  1 235 ? 11.479  69.446 25.895  1.00 17.99 ? 235  LEU B CA  1 
ATOM   7641  C  C   . LEU B  1 235 ? 11.869  68.782 27.212  1.00 17.51 ? 235  LEU B C   1 
ATOM   7642  O  O   . LEU B  1 235 ? 12.863  69.160 27.837  1.00 17.91 ? 235  LEU B O   1 
ATOM   7643  C  CB  . LEU B  1 235 ? 12.424  68.878 24.837  1.00 18.65 ? 235  LEU B CB  1 
ATOM   7644  C  CG  . LEU B  1 235 ? 12.240  69.449 23.425  1.00 21.28 ? 235  LEU B CG  1 
ATOM   7645  C  CD1 . LEU B  1 235 ? 13.538  69.336 22.631  1.00 22.15 ? 235  LEU B CD1 1 
ATOM   7646  C  CD2 . LEU B  1 235 ? 11.112  68.703 22.770  1.00 19.34 ? 235  LEU B CD2 1 
ATOM   7647  N  N   . ILE B  1 236 ? 11.090  67.792 27.627  1.00 16.30 ? 236  ILE B N   1 
ATOM   7648  C  CA  . ILE B  1 236 ? 11.471  66.999 28.790  1.00 15.19 ? 236  ILE B CA  1 
ATOM   7649  C  C   . ILE B  1 236 ? 12.301  65.912 28.094  1.00 15.56 ? 236  ILE B C   1 
ATOM   7650  O  O   . ILE B  1 236 ? 11.933  65.435 27.008  1.00 14.91 ? 236  ILE B O   1 
ATOM   7651  C  CB  . ILE B  1 236 ? 10.273  66.304 29.509  1.00 15.12 ? 236  ILE B CB  1 
ATOM   7652  C  CG1 . ILE B  1 236 ? 10.806  65.293 30.541  1.00 14.97 ? 236  ILE B CG1 1 
ATOM   7653  C  CG2 . ILE B  1 236 ? 9.384   65.554 28.493  1.00 12.86 ? 236  ILE B CG2 1 
ATOM   7654  C  CD1 . ILE B  1 236 ? 11.699  65.885 31.624  1.00 13.49 ? 236  ILE B CD1 1 
ATOM   7655  N  N   . GLU B  1 237 ? 13.419  65.540 28.695  1.00 14.84 ? 237  GLU B N   1 
ATOM   7656  C  CA  . GLU B  1 237 ? 14.272  64.515 28.112  1.00 15.48 ? 237  GLU B CA  1 
ATOM   7657  C  C   . GLU B  1 237 ? 14.621  63.489 29.181  1.00 14.34 ? 237  GLU B C   1 
ATOM   7658  O  O   . GLU B  1 237 ? 14.970  63.853 30.300  1.00 12.26 ? 237  GLU B O   1 
ATOM   7659  C  CB  . GLU B  1 237 ? 15.570  65.130 27.562  1.00 16.01 ? 237  GLU B CB  1 
ATOM   7660  C  CG  . GLU B  1 237 ? 15.351  66.329 26.673  1.00 19.69 ? 237  GLU B CG  1 
ATOM   7661  C  CD  . GLU B  1 237 ? 16.653  66.870 26.119  1.00 22.61 ? 237  GLU B CD  1 
ATOM   7662  O  OE1 . GLU B  1 237 ? 17.622  66.979 26.889  1.00 25.60 ? 237  GLU B OE1 1 
ATOM   7663  O  OE2 . GLU B  1 237 ? 16.698  67.199 24.927  1.00 24.52 ? 237  GLU B OE2 1 
ATOM   7664  N  N   . TYR B  1 238 ? 14.490  62.209 28.850  1.00 14.62 ? 238  TYR B N   1 
ATOM   7665  C  CA  . TYR B  1 238 ? 14.839  61.151 29.796  1.00 15.49 ? 238  TYR B CA  1 
ATOM   7666  C  C   . TYR B  1 238 ? 15.342  59.958 28.984  1.00 16.11 ? 238  TYR B C   1 
ATOM   7667  O  O   . TYR B  1 238 ? 15.058  59.853 27.788  1.00 15.59 ? 238  TYR B O   1 
ATOM   7668  C  CB  . TYR B  1 238 ? 13.632  60.768 30.679  1.00 14.80 ? 238  TYR B CB  1 
ATOM   7669  C  CG  . TYR B  1 238 ? 12.369  60.374 29.931  1.00 16.90 ? 238  TYR B CG  1 
ATOM   7670  C  CD1 . TYR B  1 238 ? 11.382  61.312 29.652  1.00 16.66 ? 238  TYR B CD1 1 
ATOM   7671  C  CD2 . TYR B  1 238 ? 12.174  59.058 29.476  1.00 17.21 ? 238  TYR B CD2 1 
ATOM   7672  C  CE1 . TYR B  1 238 ? 10.230  60.966 28.931  1.00 16.17 ? 238  TYR B CE1 1 
ATOM   7673  C  CE2 . TYR B  1 238 ? 11.013  58.693 28.750  1.00 15.37 ? 238  TYR B CE2 1 
ATOM   7674  C  CZ  . TYR B  1 238 ? 10.048  59.668 28.480  1.00 17.36 ? 238  TYR B CZ  1 
ATOM   7675  O  OH  . TYR B  1 238 ? 8.916   59.364 27.730  1.00 18.20 ? 238  TYR B OH  1 
ATOM   7676  N  N   . SER B  1 239 ? 16.105  59.071 29.620  1.00 15.69 ? 239  SER B N   1 
ATOM   7677  C  CA  . SER B  1 239 ? 16.633  57.918 28.902  1.00 17.02 ? 239  SER B CA  1 
ATOM   7678  C  C   . SER B  1 239 ? 15.606  56.807 28.832  1.00 17.86 ? 239  SER B C   1 
ATOM   7679  O  O   . SER B  1 239 ? 14.767  56.653 29.737  1.00 16.59 ? 239  SER B O   1 
ATOM   7680  C  CB  . SER B  1 239 ? 17.874  57.347 29.609  1.00 16.88 ? 239  SER B CB  1 
ATOM   7681  O  OG  . SER B  1 239 ? 18.874  58.323 29.758  1.00 18.01 ? 239  SER B OG  1 
ATOM   7682  N  N   . PHE B  1 240 ? 15.674  56.046 27.746  1.00 17.17 ? 240  PHE B N   1 
ATOM   7683  C  CA  . PHE B  1 240 ? 14.838  54.876 27.580  1.00 17.29 ? 240  PHE B CA  1 
ATOM   7684  C  C   . PHE B  1 240 ? 15.871  53.811 27.243  1.00 17.71 ? 240  PHE B C   1 
ATOM   7685  O  O   . PHE B  1 240 ? 16.664  53.961 26.298  1.00 14.96 ? 240  PHE B O   1 
ATOM   7686  C  CB  . PHE B  1 240 ? 13.832  55.035 26.447  1.00 18.78 ? 240  PHE B CB  1 
ATOM   7687  C  CG  . PHE B  1 240 ? 12.799  53.953 26.428  1.00 19.51 ? 240  PHE B CG  1 
ATOM   7688  C  CD1 . PHE B  1 240 ? 11.668  54.043 27.236  1.00 19.96 ? 240  PHE B CD1 1 
ATOM   7689  C  CD2 . PHE B  1 240 ? 12.981  52.815 25.645  1.00 19.97 ? 240  PHE B CD2 1 
ATOM   7690  C  CE1 . PHE B  1 240 ? 10.729  53.017 27.268  1.00 19.98 ? 240  PHE B CE1 1 
ATOM   7691  C  CE2 . PHE B  1 240 ? 12.037  51.773 25.671  1.00 20.31 ? 240  PHE B CE2 1 
ATOM   7692  C  CZ  . PHE B  1 240 ? 10.911  51.882 26.488  1.00 19.86 ? 240  PHE B CZ  1 
ATOM   7693  N  N   . TYR B  1 241 ? 15.871  52.742 28.034  1.00 17.38 ? 241  TYR B N   1 
ATOM   7694  C  CA  . TYR B  1 241 ? 16.860  51.677 27.891  1.00 17.02 ? 241  TYR B CA  1 
ATOM   7695  C  C   . TYR B  1 241 ? 16.536  50.564 26.917  1.00 17.85 ? 241  TYR B C   1 
ATOM   7696  O  O   . TYR B  1 241 ? 17.450  49.996 26.306  1.00 17.03 ? 241  TYR B O   1 
ATOM   7697  C  CB  . TYR B  1 241 ? 17.173  51.127 29.283  1.00 17.04 ? 241  TYR B CB  1 
ATOM   7698  C  CG  . TYR B  1 241 ? 17.587  52.235 30.234  1.00 16.13 ? 241  TYR B CG  1 
ATOM   7699  C  CD1 . TYR B  1 241 ? 16.668  52.822 31.092  1.00 15.55 ? 241  TYR B CD1 1 
ATOM   7700  C  CD2 . TYR B  1 241 ? 18.886  52.747 30.213  1.00 15.82 ? 241  TYR B CD2 1 
ATOM   7701  C  CE1 . TYR B  1 241 ? 17.028  53.900 31.913  1.00 15.91 ? 241  TYR B CE1 1 
ATOM   7702  C  CE2 . TYR B  1 241 ? 19.256  53.828 31.022  1.00 16.37 ? 241  TYR B CE2 1 
ATOM   7703  C  CZ  . TYR B  1 241 ? 18.319  54.396 31.870  1.00 16.40 ? 241  TYR B CZ  1 
ATOM   7704  O  OH  . TYR B  1 241 ? 18.678  55.472 32.658  1.00 18.78 ? 241  TYR B OH  1 
ATOM   7705  N  N   . SER B  1 242 ? 15.247  50.249 26.775  1.00 18.50 ? 242  SER B N   1 
ATOM   7706  C  CA  . SER B  1 242 ? 14.824  49.222 25.824  1.00 19.40 ? 242  SER B CA  1 
ATOM   7707  C  C   . SER B  1 242 ? 15.381  47.831 26.170  1.00 18.76 ? 242  SER B C   1 
ATOM   7708  O  O   . SER B  1 242 ? 15.831  47.588 27.287  1.00 17.20 ? 242  SER B O   1 
ATOM   7709  C  CB  . SER B  1 242 ? 15.278  49.638 24.414  1.00 19.49 ? 242  SER B CB  1 
ATOM   7710  O  OG  . SER B  1 242 ? 14.764  48.790 23.413  1.00 19.21 ? 242  SER B OG  1 
ATOM   7711  N  N   . ASP B  1 243 ? 15.335  46.916 25.208  1.00 18.94 ? 243  ASP B N   1 
ATOM   7712  C  CA  . ASP B  1 243 ? 15.853  45.569 25.428  1.00 19.59 ? 243  ASP B CA  1 
ATOM   7713  C  C   . ASP B  1 243 ? 17.346  45.647 25.682  1.00 18.64 ? 243  ASP B C   1 
ATOM   7714  O  O   . ASP B  1 243 ? 18.019  46.604 25.289  1.00 16.89 ? 243  ASP B O   1 
ATOM   7715  C  CB  . ASP B  1 243 ? 15.605  44.657 24.219  1.00 22.23 ? 243  ASP B CB  1 
ATOM   7716  C  CG  . ASP B  1 243 ? 14.123  44.458 23.923  1.00 26.02 ? 243  ASP B CG  1 
ATOM   7717  O  OD1 . ASP B  1 243 ? 13.279  44.567 24.849  1.00 26.76 ? 243  ASP B OD1 1 
ATOM   7718  O  OD2 . ASP B  1 243 ? 13.809  44.168 22.747  1.00 29.26 ? 243  ASP B OD2 1 
ATOM   7719  N  N   . GLU B  1 244 ? 17.842  44.605 26.332  1.00 18.26 ? 244  GLU B N   1 
ATOM   7720  C  CA  . GLU B  1 244 ? 19.236  44.461 26.703  1.00 19.47 ? 244  GLU B CA  1 
ATOM   7721  C  C   . GLU B  1 244 ? 20.179  44.603 25.501  1.00 19.56 ? 244  GLU B C   1 
ATOM   7722  O  O   . GLU B  1 244 ? 21.321  45.029 25.656  1.00 17.02 ? 244  GLU B O   1 
ATOM   7723  C  CB  . GLU B  1 244 ? 19.407  43.090 27.345  1.00 20.81 ? 244  GLU B CB  1 
ATOM   7724  C  CG  . GLU B  1 244 ? 20.751  42.815 27.939  1.00 25.53 ? 244  GLU B CG  1 
ATOM   7725  C  CD  . GLU B  1 244 ? 20.892  41.345 28.352  1.00 26.46 ? 244  GLU B CD  1 
ATOM   7726  O  OE1 . GLU B  1 244 ? 19.857  40.711 28.669  1.00 26.67 ? 244  GLU B OE1 1 
ATOM   7727  O  OE2 . GLU B  1 244 ? 22.034  40.849 28.368  1.00 28.10 ? 244  GLU B OE2 1 
ATOM   7728  N  N   . SER B  1 245 ? 19.703  44.224 24.310  1.00 19.21 ? 245  SER B N   1 
ATOM   7729  C  CA  . SER B  1 245 ? 20.514  44.312 23.086  1.00 20.47 ? 245  SER B CA  1 
ATOM   7730  C  C   . SER B  1 245 ? 20.891  45.743 22.696  1.00 19.69 ? 245  SER B C   1 
ATOM   7731  O  O   . SER B  1 245 ? 21.871  45.956 21.994  1.00 20.35 ? 245  SER B O   1 
ATOM   7732  C  CB  . SER B  1 245 ? 19.786  43.660 21.900  1.00 20.56 ? 245  SER B CB  1 
ATOM   7733  O  OG  . SER B  1 245 ? 18.497  44.215 21.725  1.00 22.36 ? 245  SER B OG  1 
ATOM   7734  N  N   . LEU B  1 246 ? 20.113  46.730 23.125  1.00 19.13 ? 246  LEU B N   1 
ATOM   7735  C  CA  . LEU B  1 246 ? 20.437  48.116 22.768  1.00 19.12 ? 246  LEU B CA  1 
ATOM   7736  C  C   . LEU B  1 246 ? 21.706  48.522 23.515  1.00 18.98 ? 246  LEU B C   1 
ATOM   7737  O  O   . LEU B  1 246 ? 21.721  48.543 24.759  1.00 18.96 ? 246  LEU B O   1 
ATOM   7738  C  CB  . LEU B  1 246 ? 19.297  49.064 23.148  1.00 17.62 ? 246  LEU B CB  1 
ATOM   7739  C  CG  . LEU B  1 246 ? 19.542  50.501 22.701  1.00 17.07 ? 246  LEU B CG  1 
ATOM   7740  C  CD1 . LEU B  1 246 ? 19.621  50.515 21.166  1.00 17.30 ? 246  LEU B CD1 1 
ATOM   7741  C  CD2 . LEU B  1 246 ? 18.409  51.431 23.206  1.00 15.93 ? 246  LEU B CD2 1 
ATOM   7742  N  N   . GLN B  1 247 ? 22.758  48.864 22.767  1.00 18.12 ? 247  GLN B N   1 
ATOM   7743  C  CA  . GLN B  1 247 ? 24.042  49.213 23.384  1.00 17.15 ? 247  GLN B CA  1 
ATOM   7744  C  C   . GLN B  1 247 ? 24.070  50.591 24.034  1.00 16.64 ? 247  GLN B C   1 
ATOM   7745  O  O   . GLN B  1 247 ? 24.610  50.734 25.124  1.00 15.72 ? 247  GLN B O   1 
ATOM   7746  C  CB  . GLN B  1 247 ? 25.182  49.087 22.361  1.00 16.96 ? 247  GLN B CB  1 
ATOM   7747  C  CG  . GLN B  1 247 ? 26.586  49.337 22.970  1.00 16.63 ? 247  GLN B CG  1 
ATOM   7748  C  CD  . GLN B  1 247 ? 27.705  49.029 21.994  1.00 18.71 ? 247  GLN B CD  1 
ATOM   7749  O  OE1 . GLN B  1 247 ? 27.666  49.461 20.840  1.00 18.70 ? 247  GLN B OE1 1 
ATOM   7750  N  NE2 . GLN B  1 247 ? 28.714  48.288 22.450  1.00 16.27 ? 247  GLN B NE2 1 
ATOM   7751  N  N   . TYR B  1 248 ? 23.513  51.597 23.364  1.00 15.75 ? 248  TYR B N   1 
ATOM   7752  C  CA  . TYR B  1 248 ? 23.446  52.957 23.909  1.00 15.12 ? 248  TYR B CA  1 
ATOM   7753  C  C   . TYR B  1 248 ? 22.002  53.298 24.268  1.00 15.80 ? 248  TYR B C   1 
ATOM   7754  O  O   . TYR B  1 248 ? 21.088  53.102 23.450  1.00 15.72 ? 248  TYR B O   1 
ATOM   7755  C  CB  . TYR B  1 248 ? 23.945  53.995 22.882  1.00 16.16 ? 248  TYR B CB  1 
ATOM   7756  C  CG  . TYR B  1 248 ? 25.443  54.039 22.732  1.00 14.38 ? 248  TYR B CG  1 
ATOM   7757  C  CD1 . TYR B  1 248 ? 26.225  54.854 23.559  1.00 13.80 ? 248  TYR B CD1 1 
ATOM   7758  C  CD2 . TYR B  1 248 ? 26.088  53.240 21.782  1.00 14.84 ? 248  TYR B CD2 1 
ATOM   7759  C  CE1 . TYR B  1 248 ? 27.615  54.869 23.439  1.00 13.15 ? 248  TYR B CE1 1 
ATOM   7760  C  CE2 . TYR B  1 248 ? 27.481  53.249 21.656  1.00 14.39 ? 248  TYR B CE2 1 
ATOM   7761  C  CZ  . TYR B  1 248 ? 28.234  54.059 22.483  1.00 13.96 ? 248  TYR B CZ  1 
ATOM   7762  O  OH  . TYR B  1 248 ? 29.609  54.046 22.350  1.00 15.19 ? 248  TYR B OH  1 
ATOM   7763  N  N   . PRO B  1 249 ? 21.771  53.810 25.487  1.00 15.41 ? 249  PRO B N   1 
ATOM   7764  C  CA  . PRO B  1 249 ? 20.380  54.146 25.817  1.00 15.86 ? 249  PRO B CA  1 
ATOM   7765  C  C   . PRO B  1 249 ? 19.864  55.220 24.856  1.00 17.06 ? 249  PRO B C   1 
ATOM   7766  O  O   . PRO B  1 249 ? 20.632  56.047 24.363  1.00 15.75 ? 249  PRO B O   1 
ATOM   7767  C  CB  . PRO B  1 249 ? 20.478  54.699 27.240  1.00 15.38 ? 249  PRO B CB  1 
ATOM   7768  C  CG  . PRO B  1 249 ? 21.688  53.994 27.812  1.00 13.90 ? 249  PRO B CG  1 
ATOM   7769  C  CD  . PRO B  1 249 ? 22.663  54.043 26.639  1.00 14.61 ? 249  PRO B CD  1 
ATOM   7770  N  N   . LYS B  1 250 ? 18.560  55.217 24.619  1.00 17.63 ? 250  LYS B N   1 
ATOM   7771  C  CA  . LYS B  1 250 ? 17.939  56.216 23.764  1.00 19.90 ? 250  LYS B CA  1 
ATOM   7772  C  C   . LYS B  1 250 ? 17.493  57.389 24.643  1.00 19.76 ? 250  LYS B C   1 
ATOM   7773  O  O   . LYS B  1 250 ? 17.152  57.197 25.815  1.00 20.18 ? 250  LYS B O   1 
ATOM   7774  C  CB  . LYS B  1 250 ? 16.727  55.591 23.070  1.00 23.79 ? 250  LYS B CB  1 
ATOM   7775  C  CG  . LYS B  1 250 ? 15.713  56.547 22.434  1.00 28.99 ? 250  LYS B CG  1 
ATOM   7776  C  CD  . LYS B  1 250 ? 14.795  55.737 21.476  1.00 33.52 ? 250  LYS B CD  1 
ATOM   7777  C  CE  . LYS B  1 250 ? 13.742  56.597 20.739  1.00 36.20 ? 250  LYS B CE  1 
ATOM   7778  N  NZ  . LYS B  1 250 ? 12.429  56.739 21.454  1.00 38.15 ? 250  LYS B NZ  1 
ATOM   7779  N  N   . THR B  1 251 ? 17.545  58.604 24.102  1.00 18.03 ? 251  THR B N   1 
ATOM   7780  C  CA  . THR B  1 251 ? 17.067  59.766 24.836  1.00 17.83 ? 251  THR B CA  1 
ATOM   7781  C  C   . THR B  1 251 ? 15.711  60.159 24.254  1.00 17.86 ? 251  THR B C   1 
ATOM   7782  O  O   . THR B  1 251 ? 15.612  60.531 23.082  1.00 17.25 ? 251  THR B O   1 
ATOM   7783  C  CB  . THR B  1 251 ? 18.002  60.979 24.722  1.00 18.43 ? 251  THR B CB  1 
ATOM   7784  O  OG1 . THR B  1 251 ? 19.210  60.710 25.446  1.00 17.46 ? 251  THR B OG1 1 
ATOM   7785  C  CG2 . THR B  1 251 ? 17.322  62.238 25.344  1.00 18.07 ? 251  THR B CG2 1 
ATOM   7786  N  N   . VAL B  1 252 ? 14.663  60.040 25.064  1.00 16.08 ? 252  VAL B N   1 
ATOM   7787  C  CA  . VAL B  1 252 ? 13.330  60.414 24.616  1.00 16.64 ? 252  VAL B CA  1 
ATOM   7788  C  C   . VAL B  1 252 ? 13.192  61.914 24.830  1.00 16.56 ? 252  VAL B C   1 
ATOM   7789  O  O   . VAL B  1 252 ? 13.578  62.423 25.873  1.00 17.30 ? 252  VAL B O   1 
ATOM   7790  C  CB  . VAL B  1 252 ? 12.242  59.628 25.402  1.00 16.32 ? 252  VAL B CB  1 
ATOM   7791  C  CG1 . VAL B  1 252 ? 10.837  60.127 25.007  1.00 16.09 ? 252  VAL B CG1 1 
ATOM   7792  C  CG2 . VAL B  1 252 ? 12.378  58.125 25.068  1.00 13.96 ? 252  VAL B CG2 1 
ATOM   7793  N  N   . ARG B  1 253 ? 12.692  62.620 23.817  1.00 16.73 ? 253  ARG B N   1 
ATOM   7794  C  CA  . ARG B  1 253 ? 12.540  64.066 23.875  1.00 17.51 ? 253  ARG B CA  1 
ATOM   7795  C  C   . ARG B  1 253 ? 11.121  64.460 23.487  1.00 16.85 ? 253  ARG B C   1 
ATOM   7796  O  O   . ARG B  1 253 ? 10.699  64.237 22.359  1.00 16.12 ? 253  ARG B O   1 
ATOM   7797  C  CB  . ARG B  1 253 ? 13.537  64.745 22.920  1.00 20.41 ? 253  ARG B CB  1 
ATOM   7798  C  CG  . ARG B  1 253 ? 15.000  64.377 23.145  1.00 22.83 ? 253  ARG B CG  1 
ATOM   7799  C  CD  . ARG B  1 253 ? 15.918  65.188 22.207  1.00 27.41 ? 253  ARG B CD  1 
ATOM   7800  N  NE  . ARG B  1 253 ? 17.183  64.484 21.983  1.00 32.67 ? 253  ARG B NE  1 
ATOM   7801  C  CZ  . ARG B  1 253 ? 18.111  64.321 22.919  1.00 33.89 ? 253  ARG B CZ  1 
ATOM   7802  N  NH1 . ARG B  1 253 ? 17.899  64.828 24.127  1.00 36.94 ? 253  ARG B NH1 1 
ATOM   7803  N  NH2 . ARG B  1 253 ? 19.229  63.644 22.663  1.00 32.26 ? 253  ARG B NH2 1 
ATOM   7804  N  N   . VAL B  1 254 ? 10.395  65.064 24.420  1.00 15.46 ? 254  VAL B N   1 
ATOM   7805  C  CA  . VAL B  1 254 ? 9.003   65.427 24.172  1.00 15.21 ? 254  VAL B CA  1 
ATOM   7806  C  C   . VAL B  1 254 ? 8.668   66.860 24.525  1.00 14.73 ? 254  VAL B C   1 
ATOM   7807  O  O   . VAL B  1 254 ? 8.953   67.308 25.645  1.00 13.99 ? 254  VAL B O   1 
ATOM   7808  C  CB  . VAL B  1 254 ? 7.994   64.540 25.037  1.00 15.60 ? 254  VAL B CB  1 
ATOM   7809  C  CG1 . VAL B  1 254 ? 6.541   64.871 24.653  1.00 14.03 ? 254  VAL B CG1 1 
ATOM   7810  C  CG2 . VAL B  1 254 ? 8.257   63.048 24.846  1.00 16.45 ? 254  VAL B CG2 1 
ATOM   7811  N  N   . PRO B  1 255 ? 8.046   67.593 23.583  1.00 13.81 ? 255  PRO B N   1 
ATOM   7812  C  CA  . PRO B  1 255 ? 7.646   68.987 23.820  1.00 14.59 ? 255  PRO B CA  1 
ATOM   7813  C  C   . PRO B  1 255 ? 6.655   68.886 24.991  1.00 13.79 ? 255  PRO B C   1 
ATOM   7814  O  O   . PRO B  1 255 ? 5.591   68.293 24.851  1.00 15.19 ? 255  PRO B O   1 
ATOM   7815  C  CB  . PRO B  1 255 ? 6.941   69.376 22.526  1.00 14.03 ? 255  PRO B CB  1 
ATOM   7816  C  CG  . PRO B  1 255 ? 7.577   68.456 21.499  1.00 15.27 ? 255  PRO B CG  1 
ATOM   7817  C  CD  . PRO B  1 255 ? 7.730   67.165 22.207  1.00 14.39 ? 255  PRO B CD  1 
ATOM   7818  N  N   . TYR B  1 256 ? 7.005   69.474 26.120  1.00 12.77 ? 256  TYR B N   1 
ATOM   7819  C  CA  . TYR B  1 256 ? 6.208   69.386 27.322  1.00 13.73 ? 256  TYR B CA  1 
ATOM   7820  C  C   . TYR B  1 256 ? 6.394   70.694 28.073  1.00 13.91 ? 256  TYR B C   1 
ATOM   7821  O  O   . TYR B  1 256 ? 7.484   71.007 28.547  1.00 14.31 ? 256  TYR B O   1 
ATOM   7822  C  CB  . TYR B  1 256 ? 6.735   68.204 28.172  1.00 13.47 ? 256  TYR B CB  1 
ATOM   7823  C  CG  . TYR B  1 256 ? 6.014   67.898 29.475  1.00 12.78 ? 256  TYR B CG  1 
ATOM   7824  C  CD1 . TYR B  1 256 ? 6.028   68.801 30.539  1.00 13.96 ? 256  TYR B CD1 1 
ATOM   7825  C  CD2 . TYR B  1 256 ? 5.318   66.694 29.645  1.00 13.72 ? 256  TYR B CD2 1 
ATOM   7826  C  CE1 . TYR B  1 256 ? 5.380   68.516 31.735  1.00 13.33 ? 256  TYR B CE1 1 
ATOM   7827  C  CE2 . TYR B  1 256 ? 4.648   66.400 30.847  1.00 12.58 ? 256  TYR B CE2 1 
ATOM   7828  C  CZ  . TYR B  1 256 ? 4.687   67.304 31.876  1.00 13.59 ? 256  TYR B CZ  1 
ATOM   7829  O  OH  . TYR B  1 256 ? 4.049   67.025 33.058  1.00 15.02 ? 256  TYR B OH  1 
ATOM   7830  N  N   . PRO B  1 257 ? 5.324   71.486 28.189  1.00 13.11 ? 257  PRO B N   1 
ATOM   7831  C  CA  . PRO B  1 257 ? 5.414   72.764 28.902  1.00 13.84 ? 257  PRO B CA  1 
ATOM   7832  C  C   . PRO B  1 257 ? 5.191   72.613 30.415  1.00 13.86 ? 257  PRO B C   1 
ATOM   7833  O  O   . PRO B  1 257 ? 4.080   72.288 30.842  1.00 14.48 ? 257  PRO B O   1 
ATOM   7834  C  CB  . PRO B  1 257 ? 4.314   73.605 28.242  1.00 14.13 ? 257  PRO B CB  1 
ATOM   7835  C  CG  . PRO B  1 257 ? 3.230   72.555 27.971  1.00 12.34 ? 257  PRO B CG  1 
ATOM   7836  C  CD  . PRO B  1 257 ? 4.035   71.342 27.482  1.00 13.79 ? 257  PRO B CD  1 
ATOM   7837  N  N   . LYS B  1 258 ? 6.240   72.824 31.211  1.00 13.37 ? 258  LYS B N   1 
ATOM   7838  C  CA  . LYS B  1 258 ? 6.105   72.749 32.664  1.00 14.78 ? 258  LYS B CA  1 
ATOM   7839  C  C   . LYS B  1 258 ? 5.444   74.058 33.104  1.00 16.10 ? 258  LYS B C   1 
ATOM   7840  O  O   . LYS B  1 258 ? 5.293   74.979 32.284  1.00 16.45 ? 258  LYS B O   1 
ATOM   7841  C  CB  . LYS B  1 258 ? 7.468   72.529 33.324  1.00 15.43 ? 258  LYS B CB  1 
ATOM   7842  C  CG  . LYS B  1 258 ? 7.932   71.060 33.226  1.00 14.86 ? 258  LYS B CG  1 
ATOM   7843  C  CD  . LYS B  1 258 ? 9.396   70.875 33.639  1.00 14.87 ? 258  LYS B CD  1 
ATOM   7844  C  CE  . LYS B  1 258 ? 9.873   69.450 33.395  1.00 13.77 ? 258  LYS B CE  1 
ATOM   7845  N  NZ  . LYS B  1 258 ? 9.390   68.496 34.453  1.00 14.35 ? 258  LYS B NZ  1 
ATOM   7846  N  N   . ALA B  1 259 ? 5.028   74.147 34.364  1.00 15.89 ? 259  ALA B N   1 
ATOM   7847  C  CA  . ALA B  1 259 ? 4.320   75.339 34.831  1.00 16.94 ? 259  ALA B CA  1 
ATOM   7848  C  C   . ALA B  1 259 ? 5.008   76.669 34.533  1.00 17.68 ? 259  ALA B C   1 
ATOM   7849  O  O   . ALA B  1 259 ? 6.157   76.883 34.883  1.00 18.94 ? 259  ALA B O   1 
ATOM   7850  C  CB  . ALA B  1 259 ? 4.010   75.216 36.336  1.00 16.09 ? 259  ALA B CB  1 
ATOM   7851  N  N   . GLY B  1 260 ? 4.287   77.571 33.880  1.00 17.51 ? 260  GLY B N   1 
ATOM   7852  C  CA  . GLY B  1 260 ? 4.860   78.862 33.548  1.00 16.92 ? 260  GLY B CA  1 
ATOM   7853  C  C   . GLY B  1 260 ? 5.737   78.913 32.305  1.00 17.28 ? 260  GLY B C   1 
ATOM   7854  O  O   . GLY B  1 260 ? 6.153   80.000 31.909  1.00 17.44 ? 260  GLY B O   1 
ATOM   7855  N  N   . ALA B  1 261 ? 6.030   77.764 31.693  1.00 16.57 ? 261  ALA B N   1 
ATOM   7856  C  CA  . ALA B  1 261 ? 6.874   77.726 30.495  1.00 16.47 ? 261  ALA B CA  1 
ATOM   7857  C  C   . ALA B  1 261 ? 6.115   78.102 29.220  1.00 16.99 ? 261  ALA B C   1 
ATOM   7858  O  O   . ALA B  1 261 ? 4.902   78.344 29.251  1.00 18.35 ? 261  ALA B O   1 
ATOM   7859  C  CB  . ALA B  1 261 ? 7.509   76.322 30.331  1.00 16.21 ? 261  ALA B CB  1 
ATOM   7860  N  N   . VAL B  1 262 ? 6.828   78.166 28.095  1.00 16.61 ? 262  VAL B N   1 
ATOM   7861  C  CA  . VAL B  1 262 ? 6.193   78.491 26.822  1.00 16.10 ? 262  VAL B CA  1 
ATOM   7862  C  C   . VAL B  1 262 ? 5.252   77.368 26.364  1.00 16.86 ? 262  VAL B C   1 
ATOM   7863  O  O   . VAL B  1 262 ? 5.673   76.214 26.245  1.00 15.32 ? 262  VAL B O   1 
ATOM   7864  C  CB  . VAL B  1 262 ? 7.233   78.699 25.698  1.00 15.29 ? 262  VAL B CB  1 
ATOM   7865  C  CG1 . VAL B  1 262 ? 6.498   78.961 24.409  1.00 14.32 ? 262  VAL B CG1 1 
ATOM   7866  C  CG2 . VAL B  1 262 ? 8.190   79.885 26.034  1.00 14.46 ? 262  VAL B CG2 1 
ATOM   7867  N  N   . ASN B  1 263 ? 3.996   77.724 26.083  1.00 16.03 ? 263  ASN B N   1 
ATOM   7868  C  CA  . ASN B  1 263 ? 2.986   76.773 25.638  1.00 16.44 ? 263  ASN B CA  1 
ATOM   7869  C  C   . ASN B  1 263 ? 2.908   76.634 24.128  1.00 16.96 ? 263  ASN B C   1 
ATOM   7870  O  O   . ASN B  1 263 ? 3.416   77.466 23.385  1.00 16.69 ? 263  ASN B O   1 
ATOM   7871  C  CB  . ASN B  1 263 ? 1.575   77.193 26.095  1.00 15.97 ? 263  ASN B CB  1 
ATOM   7872  C  CG  . ASN B  1 263 ? 1.238   76.728 27.513  1.00 17.36 ? 263  ASN B CG  1 
ATOM   7873  O  OD1 . ASN B  1 263 ? 1.893   75.829 28.054  1.00 17.20 ? 263  ASN B OD1 1 
ATOM   7874  N  ND2 . ASN B  1 263 ? 0.197   77.322 28.108  1.00 14.55 ? 263  ASN B ND2 1 
ATOM   7875  N  N   . PRO B  1 264 ? 2.262   75.559 23.658  1.00 16.88 ? 264  PRO B N   1 
ATOM   7876  C  CA  . PRO B  1 264 ? 2.148   75.422 22.213  1.00 15.97 ? 264  PRO B CA  1 
ATOM   7877  C  C   . PRO B  1 264 ? 1.056   76.430 21.837  1.00 16.24 ? 264  PRO B C   1 
ATOM   7878  O  O   . PRO B  1 264 ? 0.247   76.804 22.686  1.00 16.52 ? 264  PRO B O   1 
ATOM   7879  C  CB  . PRO B  1 264 ? 1.671   73.986 22.044  1.00 15.36 ? 264  PRO B CB  1 
ATOM   7880  C  CG  . PRO B  1 264 ? 0.898   73.719 23.304  1.00 16.77 ? 264  PRO B CG  1 
ATOM   7881  C  CD  . PRO B  1 264 ? 1.790   74.343 24.350  1.00 16.84 ? 264  PRO B CD  1 
ATOM   7882  N  N   . THR B  1 265 ? 1.046   76.902 20.600  1.00 15.27 ? 265  THR B N   1 
ATOM   7883  C  CA  . THR B  1 265 ? -0.016  77.815 20.190  1.00 15.60 ? 265  THR B CA  1 
ATOM   7884  C  C   . THR B  1 265 ? -0.909  76.960 19.324  1.00 15.34 ? 265  THR B C   1 
ATOM   7885  O  O   . THR B  1 265 ? -0.517  75.868 18.938  1.00 15.76 ? 265  THR B O   1 
ATOM   7886  C  CB  . THR B  1 265 ? 0.519   79.015 19.406  1.00 14.48 ? 265  THR B CB  1 
ATOM   7887  O  OG1 . THR B  1 265 ? 1.232   78.542 18.258  1.00 14.55 ? 265  THR B OG1 1 
ATOM   7888  C  CG2 . THR B  1 265 ? 1.460   79.838 20.296  1.00 14.22 ? 265  THR B CG2 1 
ATOM   7889  N  N   . VAL B  1 266 ? -2.109  77.434 19.017  1.00 15.96 ? 266  VAL B N   1 
ATOM   7890  C  CA  . VAL B  1 266 ? -3.018  76.621 18.244  1.00 15.29 ? 266  VAL B CA  1 
ATOM   7891  C  C   . VAL B  1 266 ? -3.817  77.393 17.229  1.00 16.12 ? 266  VAL B C   1 
ATOM   7892  O  O   . VAL B  1 266 ? -4.123  78.563 17.446  1.00 17.41 ? 266  VAL B O   1 
ATOM   7893  C  CB  . VAL B  1 266 ? -4.013  75.905 19.184  1.00 14.83 ? 266  VAL B CB  1 
ATOM   7894  C  CG1 . VAL B  1 266 ? -4.762  76.953 20.043  1.00 13.09 ? 266  VAL B CG1 1 
ATOM   7895  C  CG2 . VAL B  1 266 ? -4.991  75.074 18.373  1.00 13.58 ? 266  VAL B CG2 1 
ATOM   7896  N  N   . LYS B  1 267 ? -4.173  76.723 16.134  1.00 16.67 ? 267  LYS B N   1 
ATOM   7897  C  CA  . LYS B  1 267 ? -5.004  77.327 15.091  1.00 16.75 ? 267  LYS B CA  1 
ATOM   7898  C  C   . LYS B  1 267 ? -6.115  76.351 14.730  1.00 16.52 ? 267  LYS B C   1 
ATOM   7899  O  O   . LYS B  1 267 ? -5.963  75.134 14.882  1.00 16.98 ? 267  LYS B O   1 
ATOM   7900  C  CB  . LYS B  1 267 ? -4.171  77.661 13.859  1.00 16.88 ? 267  LYS B CB  1 
ATOM   7901  C  CG  . LYS B  1 267 ? -3.373  78.957 13.980  1.00 18.08 ? 267  LYS B CG  1 
ATOM   7902  C  CD  . LYS B  1 267 ? -2.621  79.207 12.680  1.00 18.92 ? 267  LYS B CD  1 
ATOM   7903  C  CE  . LYS B  1 267 ? -1.573  80.300 12.827  1.00 19.99 ? 267  LYS B CE  1 
ATOM   7904  N  NZ  . LYS B  1 267 ? -0.844  80.388 11.524  1.00 22.85 ? 267  LYS B NZ  1 
ATOM   7905  N  N   . PHE B  1 268 ? -7.231  76.884 14.250  1.00 15.80 ? 268  PHE B N   1 
ATOM   7906  C  CA  . PHE B  1 268 ? -8.373  76.048 13.917  1.00 15.08 ? 268  PHE B CA  1 
ATOM   7907  C  C   . PHE B  1 268 ? -8.807  76.257 12.466  1.00 15.63 ? 268  PHE B C   1 
ATOM   7908  O  O   . PHE B  1 268 ? -8.894  77.406 12.000  1.00 14.41 ? 268  PHE B O   1 
ATOM   7909  C  CB  . PHE B  1 268 ? -9.542  76.387 14.845  1.00 14.59 ? 268  PHE B CB  1 
ATOM   7910  C  CG  . PHE B  1 268 ? -10.695 75.452 14.724  1.00 14.55 ? 268  PHE B CG  1 
ATOM   7911  C  CD1 . PHE B  1 268 ? -10.670 74.207 15.355  1.00 14.46 ? 268  PHE B CD1 1 
ATOM   7912  C  CD2 . PHE B  1 268 ? -11.810 75.799 13.965  1.00 15.23 ? 268  PHE B CD2 1 
ATOM   7913  C  CE1 . PHE B  1 268 ? -11.739 73.322 15.234  1.00 13.97 ? 268  PHE B CE1 1 
ATOM   7914  C  CE2 . PHE B  1 268 ? -12.894 74.910 13.836  1.00 16.51 ? 268  PHE B CE2 1 
ATOM   7915  C  CZ  . PHE B  1 268 ? -12.857 73.671 14.473  1.00 14.17 ? 268  PHE B CZ  1 
ATOM   7916  N  N   . PHE B  1 269 ? -9.107  75.157 11.776  1.00 14.02 ? 269  PHE B N   1 
ATOM   7917  C  CA  . PHE B  1 269 ? -9.517  75.212 10.371  1.00 14.36 ? 269  PHE B CA  1 
ATOM   7918  C  C   . PHE B  1 269 ? -10.692 74.299 10.002  1.00 13.88 ? 269  PHE B C   1 
ATOM   7919  O  O   . PHE B  1 269 ? -10.971 73.320 10.676  1.00 13.92 ? 269  PHE B O   1 
ATOM   7920  C  CB  . PHE B  1 269 ? -8.349  74.815 9.444   1.00 16.11 ? 269  PHE B CB  1 
ATOM   7921  C  CG  . PHE B  1 269 ? -7.058  75.585 9.670   1.00 16.39 ? 269  PHE B CG  1 
ATOM   7922  C  CD1 . PHE B  1 269 ? -6.147  75.182 10.649  1.00 16.06 ? 269  PHE B CD1 1 
ATOM   7923  C  CD2 . PHE B  1 269 ? -6.740  76.683 8.871   1.00 16.82 ? 269  PHE B CD2 1 
ATOM   7924  C  CE1 . PHE B  1 269 ? -4.936  75.857 10.831  1.00 15.67 ? 269  PHE B CE1 1 
ATOM   7925  C  CE2 . PHE B  1 269 ? -5.525  77.376 9.041   1.00 17.19 ? 269  PHE B CE2 1 
ATOM   7926  C  CZ  . PHE B  1 269 ? -4.619  76.958 10.025  1.00 16.65 ? 269  PHE B CZ  1 
ATOM   7927  N  N   . VAL B  1 270 ? -11.358 74.607 8.896   1.00 14.88 ? 270  VAL B N   1 
ATOM   7928  C  CA  . VAL B  1 270 ? -12.443 73.764 8.406   1.00 14.62 ? 270  VAL B CA  1 
ATOM   7929  C  C   . VAL B  1 270 ? -12.284 73.626 6.883   1.00 15.75 ? 270  VAL B C   1 
ATOM   7930  O  O   . VAL B  1 270 ? -12.116 74.634 6.188   1.00 16.13 ? 270  VAL B O   1 
ATOM   7931  C  CB  . VAL B  1 270 ? -13.827 74.381 8.669   1.00 15.11 ? 270  VAL B CB  1 
ATOM   7932  C  CG1 . VAL B  1 270 ? -14.912 73.378 8.253   1.00 12.63 ? 270  VAL B CG1 1 
ATOM   7933  C  CG2 . VAL B  1 270 ? -13.969 74.772 10.145  1.00 14.29 ? 270  VAL B CG2 1 
ATOM   7934  N  N   . VAL B  1 271 ? -12.329 72.395 6.363   1.00 15.55 ? 271  VAL B N   1 
ATOM   7935  C  CA  . VAL B  1 271 ? -12.222 72.194 4.920   1.00 15.07 ? 271  VAL B CA  1 
ATOM   7936  C  C   . VAL B  1 271 ? -13.469 71.453 4.435   1.00 16.61 ? 271  VAL B C   1 
ATOM   7937  O  O   . VAL B  1 271 ? -14.030 70.621 5.171   1.00 16.58 ? 271  VAL B O   1 
ATOM   7938  C  CB  . VAL B  1 271 ? -10.943 71.378 4.530   1.00 15.33 ? 271  VAL B CB  1 
ATOM   7939  C  CG1 . VAL B  1 271 ? -11.022 69.968 5.081   1.00 14.85 ? 271  VAL B CG1 1 
ATOM   7940  C  CG2 . VAL B  1 271 ? -10.779 71.345 3.014   1.00 14.01 ? 271  VAL B CG2 1 
ATOM   7941  N  N   . ASN B  1 272 ? -13.921 71.779 3.222   1.00 16.19 ? 272  ASN B N   1 
ATOM   7942  C  CA  . ASN B  1 272 ? -15.095 71.120 2.638   1.00 17.42 ? 272  ASN B CA  1 
ATOM   7943  C  C   . ASN B  1 272 ? -14.605 69.890 1.866   1.00 16.53 ? 272  ASN B C   1 
ATOM   7944  O  O   . ASN B  1 272 ? -14.122 70.023 0.731   1.00 16.28 ? 272  ASN B O   1 
ATOM   7945  C  CB  . ASN B  1 272 ? -15.820 72.087 1.694   1.00 18.32 ? 272  ASN B CB  1 
ATOM   7946  C  CG  . ASN B  1 272 ? -17.050 71.478 1.062   1.00 20.20 ? 272  ASN B CG  1 
ATOM   7947  O  OD1 . ASN B  1 272 ? -18.031 72.186 0.782   1.00 22.81 ? 272  ASN B OD1 1 
ATOM   7948  N  ND2 . ASN B  1 272 ? -17.017 70.182 0.823   1.00 19.07 ? 272  ASN B ND2 1 
ATOM   7949  N  N   . THR B  1 273 ? -14.724 68.706 2.468   1.00 15.44 ? 273  THR B N   1 
ATOM   7950  C  CA  . THR B  1 273 ? -14.245 67.485 1.819   1.00 16.76 ? 273  THR B CA  1 
ATOM   7951  C  C   . THR B  1 273 ? -15.023 67.127 0.557   1.00 18.19 ? 273  THR B C   1 
ATOM   7952  O  O   . THR B  1 273 ? -14.538 66.345 -0.265  1.00 17.69 ? 273  THR B O   1 
ATOM   7953  C  CB  . THR B  1 273 ? -14.276 66.247 2.756   1.00 16.89 ? 273  THR B CB  1 
ATOM   7954  O  OG1 . THR B  1 273 ? -15.637 65.867 3.013   1.00 15.73 ? 273  THR B OG1 1 
ATOM   7955  C  CG2 . THR B  1 273 ? -13.526 66.546 4.088   1.00 16.20 ? 273  THR B CG2 1 
ATOM   7956  N  N   . ASP B  1 274 ? -16.232 67.667 0.398   1.00 19.33 ? 274  ASP B N   1 
ATOM   7957  C  CA  . ASP B  1 274 ? -16.999 67.358 -0.811  1.00 20.13 ? 274  ASP B CA  1 
ATOM   7958  C  C   . ASP B  1 274 ? -16.414 68.026 -2.049  1.00 20.67 ? 274  ASP B C   1 
ATOM   7959  O  O   . ASP B  1 274 ? -16.749 67.663 -3.174  1.00 19.54 ? 274  ASP B O   1 
ATOM   7960  C  CB  . ASP B  1 274 ? -18.450 67.793 -0.679  1.00 21.17 ? 274  ASP B CB  1 
ATOM   7961  C  CG  . ASP B  1 274 ? -19.303 66.778 0.069   1.00 21.92 ? 274  ASP B CG  1 
ATOM   7962  O  OD1 . ASP B  1 274 ? -18.891 65.604 0.221   1.00 22.92 ? 274  ASP B OD1 1 
ATOM   7963  O  OD2 . ASP B  1 274 ? -20.394 67.174 0.489   1.00 22.27 ? 274  ASP B OD2 1 
ATOM   7964  N  N   . SER B  1 275 ? -15.538 69.002 -1.854  1.00 20.51 ? 275  SER B N   1 
ATOM   7965  C  CA  . SER B  1 275 ? -14.953 69.686 -2.997  1.00 22.57 ? 275  SER B CA  1 
ATOM   7966  C  C   . SER B  1 275 ? -13.587 69.121 -3.388  1.00 22.46 ? 275  SER B C   1 
ATOM   7967  O  O   . SER B  1 275 ? -13.010 69.530 -4.398  1.00 22.61 ? 275  SER B O   1 
ATOM   7968  C  CB  . SER B  1 275 ? -14.807 71.177 -2.697  1.00 22.99 ? 275  SER B CB  1 
ATOM   7969  O  OG  . SER B  1 275 ? -13.760 71.364 -1.766  1.00 25.70 ? 275  SER B OG  1 
ATOM   7970  N  N   . LEU B  1 276 ? -13.084 68.171 -2.607  1.00 21.06 ? 276  LEU B N   1 
ATOM   7971  C  CA  . LEU B  1 276 ? -11.764 67.597 -2.859  1.00 21.48 ? 276  LEU B CA  1 
ATOM   7972  C  C   . LEU B  1 276 ? -11.533 67.041 -4.269  1.00 22.07 ? 276  LEU B C   1 
ATOM   7973  O  O   . LEU B  1 276 ? -10.472 67.247 -4.844  1.00 21.96 ? 276  LEU B O   1 
ATOM   7974  C  CB  . LEU B  1 276 ? -11.455 66.503 -1.827  1.00 20.14 ? 276  LEU B CB  1 
ATOM   7975  C  CG  . LEU B  1 276 ? -11.280 66.950 -0.371  1.00 21.66 ? 276  LEU B CG  1 
ATOM   7976  C  CD1 . LEU B  1 276 ? -11.193 65.722 0.535   1.00 20.34 ? 276  LEU B CD1 1 
ATOM   7977  C  CD2 . LEU B  1 276 ? -10.004 67.805 -0.231  1.00 21.18 ? 276  LEU B CD2 1 
ATOM   7978  N  N   . SER B  1 277 ? -12.510 66.339 -4.828  1.00 22.18 ? 277  SER B N   1 
ATOM   7979  C  CA  . SER B  1 277 ? -12.336 65.776 -6.149  1.00 23.14 ? 277  SER B CA  1 
ATOM   7980  C  C   . SER B  1 277 ? -12.649 66.762 -7.263  1.00 23.84 ? 277  SER B C   1 
ATOM   7981  O  O   . SER B  1 277 ? -12.659 66.372 -8.432  1.00 24.38 ? 277  SER B O   1 
ATOM   7982  C  CB  . SER B  1 277 ? -13.214 64.533 -6.316  1.00 24.20 ? 277  SER B CB  1 
ATOM   7983  O  OG  . SER B  1 277 ? -14.588 64.898 -6.295  1.00 26.33 ? 277  SER B OG  1 
ATOM   7984  N  N   . SER B  1 278 ? -12.890 68.027 -6.911  1.00 22.57 ? 278  SER B N   1 
ATOM   7985  C  CA  . SER B  1 278 ? -13.212 69.063 -7.900  1.00 23.69 ? 278  SER B CA  1 
ATOM   7986  C  C   . SER B  1 278 ? -12.177 70.167 -8.013  1.00 22.37 ? 278  SER B C   1 
ATOM   7987  O  O   . SER B  1 278 ? -12.145 70.883 -9.015  1.00 21.68 ? 278  SER B O   1 
ATOM   7988  C  CB  . SER B  1 278 ? -14.562 69.708 -7.599  1.00 23.48 ? 278  SER B CB  1 
ATOM   7989  O  OG  . SER B  1 278 ? -15.588 68.759 -7.791  1.00 27.41 ? 278  SER B OG  1 
ATOM   7990  N  N   . VAL B  1 279 ? -11.361 70.338 -6.982  1.00 21.41 ? 279  VAL B N   1 
ATOM   7991  C  CA  . VAL B  1 279 ? -10.318 71.361 -7.025  1.00 21.90 ? 279  VAL B CA  1 
ATOM   7992  C  C   . VAL B  1 279 ? -8.974  70.716 -6.676  1.00 22.04 ? 279  VAL B C   1 
ATOM   7993  O  O   . VAL B  1 279 ? -8.920  69.752 -5.905  1.00 21.67 ? 279  VAL B O   1 
ATOM   7994  C  CB  . VAL B  1 279 ? -10.634 72.551 -6.074  1.00 22.24 ? 279  VAL B CB  1 
ATOM   7995  C  CG1 . VAL B  1 279 ? -11.889 73.289 -6.574  1.00 22.14 ? 279  VAL B CG1 1 
ATOM   7996  C  CG2 . VAL B  1 279 ? -10.832 72.064 -4.649  1.00 20.88 ? 279  VAL B CG2 1 
ATOM   7997  N  N   . THR B  1 280 ? -7.891  71.225 -7.256  1.00 22.50 ? 280  THR B N   1 
ATOM   7998  C  CA  . THR B  1 280 ? -6.593  70.623 -7.006  1.00 23.77 ? 280  THR B CA  1 
ATOM   7999  C  C   . THR B  1 280 ? -6.133  70.683 -5.552  1.00 24.20 ? 280  THR B C   1 
ATOM   8000  O  O   . THR B  1 280 ? -5.488  69.750 -5.072  1.00 25.70 ? 280  THR B O   1 
ATOM   8001  C  CB  . THR B  1 280 ? -5.501  71.234 -7.910  1.00 23.71 ? 280  THR B CB  1 
ATOM   8002  O  OG1 . THR B  1 280 ? -5.299  72.599 -7.561  1.00 25.14 ? 280  THR B OG1 1 
ATOM   8003  C  CG2 . THR B  1 280 ? -5.919  71.182 -9.357  1.00 22.94 ? 280  THR B CG2 1 
ATOM   8004  N  N   . ASN B  1 281 ? -6.500  71.748 -4.840  1.00 23.52 ? 281  ASN B N   1 
ATOM   8005  C  CA  . ASN B  1 281 ? -6.062  71.927 -3.458  1.00 23.11 ? 281  ASN B CA  1 
ATOM   8006  C  C   . ASN B  1 281 ? -7.146  72.631 -2.636  1.00 22.53 ? 281  ASN B C   1 
ATOM   8007  O  O   . ASN B  1 281 ? -7.146  73.853 -2.541  1.00 22.03 ? 281  ASN B O   1 
ATOM   8008  C  CB  . ASN B  1 281 ? -4.789  72.771 -3.498  1.00 24.06 ? 281  ASN B CB  1 
ATOM   8009  C  CG  . ASN B  1 281 ? -4.029  72.786 -2.188  1.00 26.00 ? 281  ASN B CG  1 
ATOM   8010  O  OD1 . ASN B  1 281 ? -4.381  72.135 -1.205  1.00 24.92 ? 281  ASN B OD1 1 
ATOM   8011  N  ND2 . ASN B  1 281 ? -2.949  73.558 -2.208  1.00 28.01 ? 281  ASN B ND2 1 
ATOM   8012  N  N   . ALA B  1 282 ? -8.063  71.871 -2.042  1.00 22.37 ? 282  ALA B N   1 
ATOM   8013  C  CA  . ALA B  1 282 ? -9.151  72.471 -1.262  1.00 22.70 ? 282  ALA B CA  1 
ATOM   8014  C  C   . ALA B  1 282 ? -8.644  73.386 -0.151  1.00 22.83 ? 282  ALA B C   1 
ATOM   8015  O  O   . ALA B  1 282 ? -7.722  73.045 0.600   1.00 23.44 ? 282  ALA B O   1 
ATOM   8016  C  CB  . ALA B  1 282 ? -10.073 71.377 -0.678  1.00 22.27 ? 282  ALA B CB  1 
ATOM   8017  N  N   . THR B  1 283 ? -9.254  74.560 -0.066  1.00 22.06 ? 283  THR B N   1 
ATOM   8018  C  CA  . THR B  1 283 ? -8.887  75.566 0.923   1.00 22.36 ? 283  THR B CA  1 
ATOM   8019  C  C   . THR B  1 283 ? -9.380  75.274 2.351   1.00 21.50 ? 283  THR B C   1 
ATOM   8020  O  O   . THR B  1 283 ? -10.569 75.047 2.571   1.00 22.35 ? 283  THR B O   1 
ATOM   8021  C  CB  . THR B  1 283 ? -9.446  76.953 0.500   1.00 23.42 ? 283  THR B CB  1 
ATOM   8022  O  OG1 . THR B  1 283 ? -8.991  77.272 -0.819  1.00 26.35 ? 283  THR B OG1 1 
ATOM   8023  C  CG2 . THR B  1 283 ? -8.981  78.027 1.438   1.00 24.59 ? 283  THR B CG2 1 
ATOM   8024  N  N   . SER B  1 284 ? -8.451  75.275 3.306   1.00 20.00 ? 284  SER B N   1 
ATOM   8025  C  CA  . SER B  1 284 ? -8.773  75.092 4.716   1.00 19.41 ? 284  SER B CA  1 
ATOM   8026  C  C   . SER B  1 284 ? -9.088  76.498 5.229   1.00 18.82 ? 284  SER B C   1 
ATOM   8027  O  O   . SER B  1 284 ? -8.201  77.349 5.294   1.00 18.11 ? 284  SER B O   1 
ATOM   8028  C  CB  . SER B  1 284 ? -7.575  74.526 5.494   1.00 18.39 ? 284  SER B CB  1 
ATOM   8029  O  OG  . SER B  1 284 ? -7.486  73.121 5.334   1.00 21.01 ? 284  SER B OG  1 
ATOM   8030  N  N   . ILE B  1 285 ? -10.344 76.746 5.570   1.00 17.52 ? 285  ILE B N   1 
ATOM   8031  C  CA  . ILE B  1 285 ? -10.747 78.057 6.058   1.00 16.82 ? 285  ILE B CA  1 
ATOM   8032  C  C   . ILE B  1 285 ? -10.443 78.164 7.541   1.00 16.92 ? 285  ILE B C   1 
ATOM   8033  O  O   . ILE B  1 285 ? -10.913 77.350 8.333   1.00 15.70 ? 285  ILE B O   1 
ATOM   8034  C  CB  . ILE B  1 285 ? -12.248 78.266 5.864   1.00 16.66 ? 285  ILE B CB  1 
ATOM   8035  C  CG1 . ILE B  1 285 ? -12.607 78.064 4.391   1.00 17.97 ? 285  ILE B CG1 1 
ATOM   8036  C  CG2 . ILE B  1 285 ? -12.646 79.652 6.361   1.00 15.76 ? 285  ILE B CG2 1 
ATOM   8037  C  CD1 . ILE B  1 285 ? -11.976 79.073 3.479   1.00 18.50 ? 285  ILE B CD1 1 
ATOM   8038  N  N   . GLN B  1 286 ? -9.647  79.150 7.930   1.00 17.24 ? 286  GLN B N   1 
ATOM   8039  C  CA  . GLN B  1 286 ? -9.334  79.283 9.343   1.00 17.34 ? 286  GLN B CA  1 
ATOM   8040  C  C   . GLN B  1 286 ? -10.427 80.048 10.069  1.00 17.39 ? 286  GLN B C   1 
ATOM   8041  O  O   . GLN B  1 286 ? -11.057 80.925 9.495   1.00 17.83 ? 286  GLN B O   1 
ATOM   8042  C  CB  . GLN B  1 286 ? -8.001  80.014 9.546   1.00 18.23 ? 286  GLN B CB  1 
ATOM   8043  C  CG  . GLN B  1 286 ? -7.564  80.124 11.020  1.00 17.61 ? 286  GLN B CG  1 
ATOM   8044  C  CD  . GLN B  1 286 ? -6.213  80.824 11.184  1.00 19.97 ? 286  GLN B CD  1 
ATOM   8045  O  OE1 . GLN B  1 286 ? -5.637  81.323 10.209  1.00 19.83 ? 286  GLN B OE1 1 
ATOM   8046  N  NE2 . GLN B  1 286 ? -5.712  80.877 12.418  1.00 18.97 ? 286  GLN B NE2 1 
ATOM   8047  N  N   . ILE B  1 287 ? -10.697 79.664 11.307  1.00 17.46 ? 287  ILE B N   1 
ATOM   8048  C  CA  . ILE B  1 287 ? -11.652 80.403 12.130  1.00 17.86 ? 287  ILE B CA  1 
ATOM   8049  C  C   . ILE B  1 287 ? -10.750 80.862 13.269  1.00 18.94 ? 287  ILE B C   1 
ATOM   8050  O  O   . ILE B  1 287 ? -10.184 80.036 14.015  1.00 17.44 ? 287  ILE B O   1 
ATOM   8051  C  CB  . ILE B  1 287 ? -12.781 79.538 12.703  1.00 18.42 ? 287  ILE B CB  1 
ATOM   8052  C  CG1 . ILE B  1 287 ? -13.686 79.037 11.574  1.00 16.92 ? 287  ILE B CG1 1 
ATOM   8053  C  CG2 . ILE B  1 287 ? -13.629 80.386 13.682  1.00 17.86 ? 287  ILE B CG2 1 
ATOM   8054  C  CD1 . ILE B  1 287 ? -14.678 78.000 12.027  1.00 16.06 ? 287  ILE B CD1 1 
ATOM   8055  N  N   . THR B  1 288 ? -10.572 82.173 13.374  1.00 17.98 ? 288  THR B N   1 
ATOM   8056  C  CA  . THR B  1 288 ? -9.692  82.724 14.392  1.00 19.46 ? 288  THR B CA  1 
ATOM   8057  C  C   . THR B  1 288 ? -10.328 82.899 15.763  1.00 19.86 ? 288  THR B C   1 
ATOM   8058  O  O   . THR B  1 288 ? -11.534 83.086 15.888  1.00 19.63 ? 288  THR B O   1 
ATOM   8059  C  CB  . THR B  1 288 ? -9.131  84.069 13.917  1.00 20.28 ? 288  THR B CB  1 
ATOM   8060  O  OG1 . THR B  1 288 ? -10.212 84.876 13.426  1.00 21.90 ? 288  THR B OG1 1 
ATOM   8061  C  CG2 . THR B  1 288 ? -8.140  83.856 12.784  1.00 21.46 ? 288  THR B CG2 1 
ATOM   8062  N  N   . ALA B  1 289 ? -9.494  82.826 16.794  1.00 19.97 ? 289  ALA B N   1 
ATOM   8063  C  CA  . ALA B  1 289 ? -9.963  82.974 18.170  1.00 20.08 ? 289  ALA B CA  1 
ATOM   8064  C  C   . ALA B  1 289 ? -10.399 84.422 18.316  1.00 20.55 ? 289  ALA B C   1 
ATOM   8065  O  O   . ALA B  1 289 ? -9.918  85.280 17.581  1.00 19.06 ? 289  ALA B O   1 
ATOM   8066  C  CB  . ALA B  1 289 ? -8.829  82.677 19.142  1.00 17.18 ? 289  ALA B CB  1 
ATOM   8067  N  N   . PRO B  1 290 ? -11.321 84.711 19.257  1.00 21.81 ? 290  PRO B N   1 
ATOM   8068  C  CA  . PRO B  1 290 ? -11.786 86.091 19.456  1.00 22.88 ? 290  PRO B CA  1 
ATOM   8069  C  C   . PRO B  1 290 ? -10.667 86.999 19.969  1.00 24.19 ? 290  PRO B C   1 
ATOM   8070  O  O   . PRO B  1 290 ? -9.687  86.524 20.562  1.00 22.58 ? 290  PRO B O   1 
ATOM   8071  C  CB  . PRO B  1 290 ? -12.934 85.931 20.463  1.00 23.75 ? 290  PRO B CB  1 
ATOM   8072  C  CG  . PRO B  1 290 ? -12.558 84.702 21.224  1.00 22.62 ? 290  PRO B CG  1 
ATOM   8073  C  CD  . PRO B  1 290 ? -12.058 83.781 20.126  1.00 21.14 ? 290  PRO B CD  1 
ATOM   8074  N  N   . ALA B  1 291 ? -10.801 88.302 19.719  1.00 24.65 ? 291  ALA B N   1 
ATOM   8075  C  CA  . ALA B  1 291 ? -9.800  89.270 20.166  1.00 25.44 ? 291  ALA B CA  1 
ATOM   8076  C  C   . ALA B  1 291 ? -9.550  89.131 21.665  1.00 25.46 ? 291  ALA B C   1 
ATOM   8077  O  O   . ALA B  1 291 ? -8.431  89.300 22.135  1.00 26.19 ? 291  ALA B O   1 
ATOM   8078  C  CB  . ALA B  1 291 ? -10.264 90.699 19.834  1.00 26.64 ? 291  ALA B CB  1 
ATOM   8079  N  N   . SER B  1 292 ? -10.589 88.807 22.423  1.00 25.79 ? 292  SER B N   1 
ATOM   8080  C  CA  . SER B  1 292 ? -10.416 88.647 23.859  1.00 26.31 ? 292  SER B CA  1 
ATOM   8081  C  C   . SER B  1 292 ? -9.414  87.532 24.197  1.00 26.48 ? 292  SER B C   1 
ATOM   8082  O  O   . SER B  1 292 ? -8.856  87.504 25.302  1.00 26.49 ? 292  SER B O   1 
ATOM   8083  C  CB  . SER B  1 292 ? -11.758 88.350 24.523  1.00 26.17 ? 292  SER B CB  1 
ATOM   8084  O  OG  . SER B  1 292 ? -12.425 87.280 23.870  1.00 27.23 ? 292  SER B OG  1 
ATOM   8085  N  N   . MET B  1 293 ? -9.191  86.614 23.255  1.00 25.42 ? 293  MET B N   1 
ATOM   8086  C  CA  . MET B  1 293 ? -8.247  85.510 23.469  1.00 24.70 ? 293  MET B CA  1 
ATOM   8087  C  C   . MET B  1 293 ? -6.888  85.826 22.859  1.00 24.54 ? 293  MET B C   1 
ATOM   8088  O  O   . MET B  1 293 ? -5.842  85.520 23.434  1.00 23.89 ? 293  MET B O   1 
ATOM   8089  C  CB  . MET B  1 293 ? -8.794  84.208 22.862  1.00 23.26 ? 293  MET B CB  1 
ATOM   8090  C  CG  . MET B  1 293 ? -9.954  83.614 23.632  1.00 21.33 ? 293  MET B CG  1 
ATOM   8091  S  SD  . MET B  1 293 ? -9.461  82.926 25.224  1.00 22.86 ? 293  MET B SD  1 
ATOM   8092  C  CE  . MET B  1 293 ? -10.995 82.864 26.090  1.00 18.83 ? 293  MET B CE  1 
ATOM   8093  N  N   . LEU B  1 294 ? -6.900  86.454 21.690  1.00 25.34 ? 294  LEU B N   1 
ATOM   8094  C  CA  . LEU B  1 294 ? -5.652  86.788 21.024  1.00 25.43 ? 294  LEU B CA  1 
ATOM   8095  C  C   . LEU B  1 294 ? -4.770  87.748 21.848  1.00 25.82 ? 294  LEU B C   1 
ATOM   8096  O  O   . LEU B  1 294 ? -3.569  87.789 21.648  1.00 25.76 ? 294  LEU B O   1 
ATOM   8097  C  CB  . LEU B  1 294 ? -5.959  87.360 19.638  1.00 26.40 ? 294  LEU B CB  1 
ATOM   8098  C  CG  . LEU B  1 294 ? -6.738  86.409 18.700  1.00 26.13 ? 294  LEU B CG  1 
ATOM   8099  C  CD1 . LEU B  1 294 ? -7.036  87.126 17.388  1.00 27.53 ? 294  LEU B CD1 1 
ATOM   8100  C  CD2 . LEU B  1 294 ? -5.929  85.139 18.424  1.00 25.48 ? 294  LEU B CD2 1 
ATOM   8101  N  N   . ILE B  1 295 ? -5.352  88.505 22.781  1.00 26.12 ? 295  ILE B N   1 
ATOM   8102  C  CA  . ILE B  1 295 ? -4.561  89.422 23.616  1.00 26.64 ? 295  ILE B CA  1 
ATOM   8103  C  C   . ILE B  1 295 ? -3.435  88.709 24.381  1.00 25.68 ? 295  ILE B C   1 
ATOM   8104  O  O   . ILE B  1 295 ? -2.469  89.336 24.802  1.00 26.12 ? 295  ILE B O   1 
ATOM   8105  C  CB  . ILE B  1 295 ? -5.412  90.126 24.685  1.00 27.42 ? 295  ILE B CB  1 
ATOM   8106  C  CG1 . ILE B  1 295 ? -6.115  89.075 25.545  1.00 29.15 ? 295  ILE B CG1 1 
ATOM   8107  C  CG2 . ILE B  1 295 ? -6.395  91.064 24.032  1.00 30.19 ? 295  ILE B CG2 1 
ATOM   8108  C  CD1 . ILE B  1 295 ? -6.651  89.591 26.852  1.00 29.55 ? 295  ILE B CD1 1 
ATOM   8109  N  N   . GLY B  1 296 ? -3.570  87.409 24.592  1.00 24.25 ? 296  GLY B N   1 
ATOM   8110  C  CA  . GLY B  1 296 ? -2.530  86.688 25.309  1.00 23.00 ? 296  GLY B CA  1 
ATOM   8111  C  C   . GLY B  1 296 ? -2.523  85.203 24.994  1.00 22.64 ? 296  GLY B C   1 
ATOM   8112  O  O   . GLY B  1 296 ? -3.155  84.770 24.018  1.00 22.21 ? 296  GLY B O   1 
ATOM   8113  N  N   . ASP B  1 297 ? -1.799  84.427 25.803  1.00 20.42 ? 297  ASP B N   1 
ATOM   8114  C  CA  . ASP B  1 297 ? -1.738  82.984 25.620  1.00 19.74 ? 297  ASP B CA  1 
ATOM   8115  C  C   . ASP B  1 297 ? -3.131  82.427 25.838  1.00 17.90 ? 297  ASP B C   1 
ATOM   8116  O  O   . ASP B  1 297 ? -3.863  82.899 26.704  1.00 17.88 ? 297  ASP B O   1 
ATOM   8117  C  CB  . ASP B  1 297 ? -0.797  82.331 26.642  1.00 19.33 ? 297  ASP B CB  1 
ATOM   8118  C  CG  . ASP B  1 297 ? 0.668   82.469 26.269  1.00 20.13 ? 297  ASP B CG  1 
ATOM   8119  O  OD1 . ASP B  1 297 ? 0.955   83.039 25.201  1.00 20.12 ? 297  ASP B OD1 1 
ATOM   8120  O  OD2 . ASP B  1 297 ? 1.535   81.998 27.043  1.00 18.47 ? 297  ASP B OD2 1 
ATOM   8121  N  N   . HIS B  1 298 ? -3.483  81.403 25.076  1.00 16.85 ? 298  HIS B N   1 
ATOM   8122  C  CA  . HIS B  1 298 ? -4.797  80.793 25.222  1.00 17.81 ? 298  HIS B CA  1 
ATOM   8123  C  C   . HIS B  1 298 ? -4.813  79.326 24.783  1.00 18.11 ? 298  HIS B C   1 
ATOM   8124  O  O   . HIS B  1 298 ? -3.810  78.783 24.317  1.00 18.50 ? 298  HIS B O   1 
ATOM   8125  C  CB  . HIS B  1 298 ? -5.856  81.595 24.427  1.00 16.13 ? 298  HIS B CB  1 
ATOM   8126  C  CG  . HIS B  1 298 ? -5.509  81.776 22.985  1.00 16.44 ? 298  HIS B CG  1 
ATOM   8127  N  ND1 . HIS B  1 298 ? -4.623  82.736 22.548  1.00 16.97 ? 298  HIS B ND1 1 
ATOM   8128  C  CD2 . HIS B  1 298 ? -5.861  81.062 21.889  1.00 16.99 ? 298  HIS B CD2 1 
ATOM   8129  C  CE1 . HIS B  1 298 ? -4.442  82.607 21.244  1.00 17.86 ? 298  HIS B CE1 1 
ATOM   8130  N  NE2 . HIS B  1 298 ? -5.181  81.596 20.819  1.00 16.49 ? 298  HIS B NE2 1 
ATOM   8131  N  N   . TYR B  1 299 ? -5.956  78.682 24.959  1.00 17.63 ? 299  TYR B N   1 
ATOM   8132  C  CA  . TYR B  1 299 ? -6.122  77.283 24.560  1.00 17.14 ? 299  TYR B CA  1 
ATOM   8133  C  C   . TYR B  1 299 ? -7.433  77.123 23.807  1.00 16.92 ? 299  TYR B C   1 
ATOM   8134  O  O   . TYR B  1 299 ? -8.353  77.937 23.967  1.00 16.16 ? 299  TYR B O   1 
ATOM   8135  C  CB  . TYR B  1 299 ? -6.221  76.364 25.770  1.00 14.59 ? 299  TYR B CB  1 
ATOM   8136  C  CG  . TYR B  1 299 ? -5.100  76.453 26.777  1.00 14.84 ? 299  TYR B CG  1 
ATOM   8137  C  CD1 . TYR B  1 299 ? -3.831  75.948 26.491  1.00 12.55 ? 299  TYR B CD1 1 
ATOM   8138  C  CD2 . TYR B  1 299 ? -5.337  76.968 28.055  1.00 14.21 ? 299  TYR B CD2 1 
ATOM   8139  C  CE1 . TYR B  1 299 ? -2.812  75.941 27.476  1.00 14.39 ? 299  TYR B CE1 1 
ATOM   8140  C  CE2 . TYR B  1 299 ? -4.326  76.963 29.050  1.00 16.15 ? 299  TYR B CE2 1 
ATOM   8141  C  CZ  . TYR B  1 299 ? -3.075  76.446 28.751  1.00 14.93 ? 299  TYR B CZ  1 
ATOM   8142  O  OH  . TYR B  1 299 ? -2.108  76.425 29.731  1.00 16.39 ? 299  TYR B OH  1 
ATOM   8143  N  N   . LEU B  1 300 ? -7.496  76.075 22.992  1.00 15.93 ? 300  LEU B N   1 
ATOM   8144  C  CA  . LEU B  1 300 ? -8.709  75.693 22.265  1.00 16.38 ? 300  LEU B CA  1 
ATOM   8145  C  C   . LEU B  1 300 ? -9.186  74.558 23.178  1.00 16.53 ? 300  LEU B C   1 
ATOM   8146  O  O   . LEU B  1 300 ? -8.497  73.541 23.308  1.00 16.56 ? 300  LEU B O   1 
ATOM   8147  C  CB  . LEU B  1 300 ? -8.350  75.148 20.877  1.00 15.76 ? 300  LEU B CB  1 
ATOM   8148  C  CG  . LEU B  1 300 ? -9.474  74.424 20.142  1.00 17.05 ? 300  LEU B CG  1 
ATOM   8149  C  CD1 . LEU B  1 300 ? -10.673 75.344 20.018  1.00 16.82 ? 300  LEU B CD1 1 
ATOM   8150  C  CD2 . LEU B  1 300 ? -9.001  73.994 18.763  1.00 17.66 ? 300  LEU B CD2 1 
ATOM   8151  N  N   . CYS B  1 301 ? -10.344 74.707 23.824  1.00 17.80 ? 301  CYS B N   1 
ATOM   8152  C  CA  . CYS B  1 301 ? -10.780 73.668 24.756  1.00 17.82 ? 301  CYS B CA  1 
ATOM   8153  C  C   . CYS B  1 301 ? -12.015 72.867 24.378  1.00 18.32 ? 301  CYS B C   1 
ATOM   8154  O  O   . CYS B  1 301 ? -12.403 71.949 25.104  1.00 18.52 ? 301  CYS B O   1 
ATOM   8155  C  CB  . CYS B  1 301 ? -10.973 74.269 26.161  1.00 19.35 ? 301  CYS B CB  1 
ATOM   8156  S  SG  . CYS B  1 301 ? -12.080 75.703 26.189  1.00 21.55 ? 301  CYS B SG  1 
ATOM   8157  N  N   . ASP B  1 302 ? -12.653 73.213 23.267  1.00 17.93 ? 302  ASP B N   1 
ATOM   8158  C  CA  . ASP B  1 302 ? -13.814 72.465 22.831  1.00 17.19 ? 302  ASP B CA  1 
ATOM   8159  C  C   . ASP B  1 302 ? -14.204 72.724 21.391  1.00 17.61 ? 302  ASP B C   1 
ATOM   8160  O  O   . ASP B  1 302 ? -14.104 73.859 20.889  1.00 18.02 ? 302  ASP B O   1 
ATOM   8161  C  CB  . ASP B  1 302 ? -15.033 72.749 23.721  1.00 17.99 ? 302  ASP B CB  1 
ATOM   8162  C  CG  . ASP B  1 302 ? -16.230 71.885 23.337  1.00 19.69 ? 302  ASP B CG  1 
ATOM   8163  O  OD1 . ASP B  1 302 ? -16.978 72.255 22.395  1.00 19.99 ? 302  ASP B OD1 1 
ATOM   8164  O  OD2 . ASP B  1 302 ? -16.406 70.813 23.963  1.00 19.79 ? 302  ASP B OD2 1 
ATOM   8165  N  N   . VAL B  1 303 ? -14.647 71.659 20.733  1.00 15.90 ? 303  VAL B N   1 
ATOM   8166  C  CA  . VAL B  1 303 ? -15.123 71.741 19.361  1.00 16.61 ? 303  VAL B CA  1 
ATOM   8167  C  C   . VAL B  1 303 ? -16.335 70.826 19.312  1.00 16.70 ? 303  VAL B C   1 
ATOM   8168  O  O   . VAL B  1 303 ? -16.239 69.643 19.634  1.00 17.16 ? 303  VAL B O   1 
ATOM   8169  C  CB  . VAL B  1 303 ? -14.078 71.240 18.334  1.00 16.86 ? 303  VAL B CB  1 
ATOM   8170  C  CG1 . VAL B  1 303 ? -14.680 71.288 16.923  1.00 17.06 ? 303  VAL B CG1 1 
ATOM   8171  C  CG2 . VAL B  1 303 ? -12.818 72.091 18.405  1.00 15.34 ? 303  VAL B CG2 1 
ATOM   8172  N  N   . THR B  1 304 ? -17.475 71.380 18.922  1.00 15.85 ? 304  THR B N   1 
ATOM   8173  C  CA  . THR B  1 304 ? -18.701 70.603 18.854  1.00 15.39 ? 304  THR B CA  1 
ATOM   8174  C  C   . THR B  1 304 ? -19.535 71.143 17.695  1.00 15.44 ? 304  THR B C   1 
ATOM   8175  O  O   . THR B  1 304 ? -19.885 72.327 17.672  1.00 14.56 ? 304  THR B O   1 
ATOM   8176  C  CB  . THR B  1 304 ? -19.525 70.739 20.170  1.00 16.29 ? 304  THR B CB  1 
ATOM   8177  O  OG1 . THR B  1 304 ? -18.746 70.251 21.269  1.00 17.58 ? 304  THR B OG1 1 
ATOM   8178  C  CG2 . THR B  1 304 ? -20.859 69.942 20.087  1.00 14.78 ? 304  THR B CG2 1 
ATOM   8179  N  N   . TRP B  1 305 ? -19.814 70.283 16.719  1.00 15.42 ? 305  TRP B N   1 
ATOM   8180  C  CA  . TRP B  1 305 ? -20.645 70.673 15.584  1.00 16.73 ? 305  TRP B CA  1 
ATOM   8181  C  C   . TRP B  1 305 ? -22.080 70.772 16.088  1.00 17.54 ? 305  TRP B C   1 
ATOM   8182  O  O   . TRP B  1 305 ? -22.489 69.966 16.925  1.00 16.84 ? 305  TRP B O   1 
ATOM   8183  C  CB  . TRP B  1 305 ? -20.589 69.616 14.488  1.00 15.71 ? 305  TRP B CB  1 
ATOM   8184  C  CG  . TRP B  1 305 ? -19.383 69.733 13.630  1.00 15.62 ? 305  TRP B CG  1 
ATOM   8185  C  CD1 . TRP B  1 305 ? -18.184 69.085 13.780  1.00 15.18 ? 305  TRP B CD1 1 
ATOM   8186  C  CD2 . TRP B  1 305 ? -19.259 70.560 12.478  1.00 15.49 ? 305  TRP B CD2 1 
ATOM   8187  N  NE1 . TRP B  1 305 ? -17.316 69.465 12.771  1.00 15.46 ? 305  TRP B NE1 1 
ATOM   8188  C  CE2 . TRP B  1 305 ? -17.954 70.375 11.963  1.00 14.92 ? 305  TRP B CE2 1 
ATOM   8189  C  CE3 . TRP B  1 305 ? -20.130 71.453 11.826  1.00 15.12 ? 305  TRP B CE3 1 
ATOM   8190  C  CZ2 . TRP B  1 305 ? -17.501 71.042 10.824  1.00 16.22 ? 305  TRP B CZ2 1 
ATOM   8191  C  CZ3 . TRP B  1 305 ? -19.678 72.121 10.689  1.00 15.65 ? 305  TRP B CZ3 1 
ATOM   8192  C  CH2 . TRP B  1 305 ? -18.375 71.913 10.201  1.00 17.12 ? 305  TRP B CH2 1 
ATOM   8193  N  N   . ALA B  1 306 ? -22.828 71.752 15.590  1.00 18.37 ? 306  ALA B N   1 
ATOM   8194  C  CA  . ALA B  1 306 ? -24.231 71.916 15.982  1.00 18.75 ? 306  ALA B CA  1 
ATOM   8195  C  C   . ALA B  1 306 ? -25.155 71.430 14.875  1.00 18.99 ? 306  ALA B C   1 
ATOM   8196  O  O   . ALA B  1 306 ? -26.170 70.803 15.152  1.00 20.42 ? 306  ALA B O   1 
ATOM   8197  C  CB  . ALA B  1 306 ? -24.543 73.373 16.309  1.00 16.97 ? 306  ALA B CB  1 
ATOM   8198  N  N   . THR B  1 307 ? -24.809 71.726 13.626  1.00 18.95 ? 307  THR B N   1 
ATOM   8199  C  CA  . THR B  1 307 ? -25.609 71.294 12.478  1.00 19.20 ? 307  THR B CA  1 
ATOM   8200  C  C   . THR B  1 307 ? -24.644 71.070 11.309  1.00 19.32 ? 307  THR B C   1 
ATOM   8201  O  O   . THR B  1 307 ? -23.433 71.178 11.476  1.00 19.55 ? 307  THR B O   1 
ATOM   8202  C  CB  . THR B  1 307 ? -26.637 72.359 12.047  1.00 18.90 ? 307  THR B CB  1 
ATOM   8203  O  OG1 . THR B  1 307 ? -25.950 73.449 11.421  1.00 18.75 ? 307  THR B OG1 1 
ATOM   8204  C  CG2 . THR B  1 307 ? -27.425 72.894 13.266  1.00 19.61 ? 307  THR B CG2 1 
ATOM   8205  N  N   . GLN B  1 308 ? -25.178 70.769 10.133  1.00 18.62 ? 308  GLN B N   1 
ATOM   8206  C  CA  . GLN B  1 308 ? -24.355 70.541 8.947   1.00 17.65 ? 308  GLN B CA  1 
ATOM   8207  C  C   . GLN B  1 308 ? -23.562 71.779 8.587   1.00 17.76 ? 308  GLN B C   1 
ATOM   8208  O  O   . GLN B  1 308 ? -22.523 71.696 7.944   1.00 16.79 ? 308  GLN B O   1 
ATOM   8209  C  CB  . GLN B  1 308 ? -25.232 70.210 7.743   1.00 18.68 ? 308  GLN B CB  1 
ATOM   8210  C  CG  . GLN B  1 308 ? -26.228 69.070 7.967   1.00 21.01 ? 308  GLN B CG  1 
ATOM   8211  C  CD  . GLN B  1 308 ? -25.562 67.772 8.377   1.00 22.10 ? 308  GLN B CD  1 
ATOM   8212  O  OE1 . GLN B  1 308 ? -24.336 67.608 8.243   1.00 25.19 ? 308  GLN B OE1 1 
ATOM   8213  N  NE2 . GLN B  1 308 ? -26.362 66.832 8.873   1.00 21.17 ? 308  GLN B NE2 1 
ATOM   8214  N  N   . GLU B  1 309 ? -24.087 72.936 8.972   1.00 17.48 ? 309  GLU B N   1 
ATOM   8215  C  CA  . GLU B  1 309 ? -23.441 74.192 8.644   1.00 18.18 ? 309  GLU B CA  1 
ATOM   8216  C  C   . GLU B  1 309 ? -23.175 75.120 9.820   1.00 17.45 ? 309  GLU B C   1 
ATOM   8217  O  O   . GLU B  1 309 ? -22.960 76.302 9.630   1.00 18.77 ? 309  GLU B O   1 
ATOM   8218  C  CB  . GLU B  1 309 ? -24.273 74.912 7.574   1.00 18.54 ? 309  GLU B CB  1 
ATOM   8219  C  CG  . GLU B  1 309 ? -24.261 74.168 6.243   1.00 19.81 ? 309  GLU B CG  1 
ATOM   8220  C  CD  . GLU B  1 309 ? -25.186 74.770 5.205   1.00 21.97 ? 309  GLU B CD  1 
ATOM   8221  O  OE1 . GLU B  1 309 ? -25.515 75.975 5.298   1.00 22.17 ? 309  GLU B OE1 1 
ATOM   8222  O  OE2 . GLU B  1 309 ? -25.570 74.023 4.281   1.00 24.55 ? 309  GLU B OE2 1 
ATOM   8223  N  N   . ARG B  1 310 ? -23.171 74.577 11.030  1.00 17.56 ? 310  ARG B N   1 
ATOM   8224  C  CA  . ARG B  1 310 ? -22.915 75.375 12.231  1.00 17.17 ? 310  ARG B CA  1 
ATOM   8225  C  C   . ARG B  1 310 ? -21.951 74.616 13.165  1.00 15.98 ? 310  ARG B C   1 
ATOM   8226  O  O   . ARG B  1 310 ? -22.203 73.483 13.559  1.00 15.66 ? 310  ARG B O   1 
ATOM   8227  C  CB  . ARG B  1 310 ? -24.241 75.690 12.980  1.00 16.75 ? 310  ARG B CB  1 
ATOM   8228  C  CG  . ARG B  1 310 ? -24.061 76.509 14.314  1.00 17.86 ? 310  ARG B CG  1 
ATOM   8229  C  CD  . ARG B  1 310 ? -25.422 76.990 14.884  1.00 17.94 ? 310  ARG B CD  1 
ATOM   8230  N  NE  . ARG B  1 310 ? -26.069 77.918 13.965  1.00 18.85 ? 310  ARG B NE  1 
ATOM   8231  C  CZ  . ARG B  1 310 ? -27.384 78.044 13.815  1.00 20.27 ? 310  ARG B CZ  1 
ATOM   8232  N  NH1 . ARG B  1 310 ? -28.225 77.301 14.528  1.00 20.10 ? 310  ARG B NH1 1 
ATOM   8233  N  NH2 . ARG B  1 310 ? -27.858 78.891 12.916  1.00 19.55 ? 310  ARG B NH2 1 
ATOM   8234  N  N   . ILE B  1 311 ? -20.835 75.239 13.496  1.00 16.96 ? 311  ILE B N   1 
ATOM   8235  C  CA  . ILE B  1 311 ? -19.880 74.616 14.397  1.00 17.59 ? 311  ILE B CA  1 
ATOM   8236  C  C   . ILE B  1 311 ? -19.644 75.583 15.552  1.00 18.38 ? 311  ILE B C   1 
ATOM   8237  O  O   . ILE B  1 311 ? -19.675 76.808 15.370  1.00 19.60 ? 311  ILE B O   1 
ATOM   8238  C  CB  . ILE B  1 311 ? -18.531 74.299 13.680  1.00 16.73 ? 311  ILE B CB  1 
ATOM   8239  C  CG1 . ILE B  1 311 ? -17.606 73.534 14.620  1.00 15.77 ? 311  ILE B CG1 1 
ATOM   8240  C  CG2 . ILE B  1 311 ? -17.852 75.590 13.218  1.00 17.54 ? 311  ILE B CG2 1 
ATOM   8241  C  CD1 . ILE B  1 311 ? -16.296 73.148 13.971  1.00 20.12 ? 311  ILE B CD1 1 
ATOM   8242  N  N   . SER B  1 312 ? -19.476 75.032 16.748  1.00 18.19 ? 312  SER B N   1 
ATOM   8243  C  CA  . SER B  1 312 ? -19.205 75.850 17.909  1.00 17.69 ? 312  SER B CA  1 
ATOM   8244  C  C   . SER B  1 312 ? -17.816 75.461 18.379  1.00 18.80 ? 312  SER B C   1 
ATOM   8245  O  O   . SER B  1 312 ? -17.382 74.296 18.249  1.00 17.06 ? 312  SER B O   1 
ATOM   8246  C  CB  . SER B  1 312 ? -20.213 75.597 19.041  1.00 18.33 ? 312  SER B CB  1 
ATOM   8247  O  OG  . SER B  1 312 ? -19.999 74.357 19.695  1.00 17.39 ? 312  SER B OG  1 
ATOM   8248  N  N   . LEU B  1 313 ? -17.095 76.440 18.886  1.00 17.97 ? 313  LEU B N   1 
ATOM   8249  C  CA  . LEU B  1 313 ? -15.770 76.160 19.396  1.00 19.44 ? 313  LEU B CA  1 
ATOM   8250  C  C   . LEU B  1 313 ? -15.565 77.030 20.607  1.00 19.71 ? 313  LEU B C   1 
ATOM   8251  O  O   . LEU B  1 313 ? -16.155 78.109 20.727  1.00 19.23 ? 313  LEU B O   1 
ATOM   8252  C  CB  . LEU B  1 313 ? -14.680 76.401 18.340  1.00 18.59 ? 313  LEU B CB  1 
ATOM   8253  C  CG  . LEU B  1 313 ? -14.430 77.766 17.717  1.00 20.30 ? 313  LEU B CG  1 
ATOM   8254  C  CD1 . LEU B  1 313 ? -13.073 77.756 17.028  1.00 20.82 ? 313  LEU B CD1 1 
ATOM   8255  C  CD2 . LEU B  1 313 ? -15.528 78.086 16.708  1.00 22.19 ? 313  LEU B CD2 1 
ATOM   8256  N  N   . GLN B  1 314 ? -14.749 76.547 21.530  1.00 19.89 ? 314  GLN B N   1 
ATOM   8257  C  CA  . GLN B  1 314 ? -14.519 77.306 22.733  1.00 18.93 ? 314  GLN B CA  1 
ATOM   8258  C  C   . GLN B  1 314 ? -13.053 77.490 23.028  1.00 18.30 ? 314  GLN B C   1 
ATOM   8259  O  O   . GLN B  1 314 ? -12.241 76.582 22.828  1.00 17.87 ? 314  GLN B O   1 
ATOM   8260  C  CB  . GLN B  1 314 ? -15.194 76.632 23.909  1.00 20.21 ? 314  GLN B CB  1 
ATOM   8261  C  CG  . GLN B  1 314 ? -15.180 77.486 25.138  1.00 22.41 ? 314  GLN B CG  1 
ATOM   8262  C  CD  . GLN B  1 314 ? -15.790 76.770 26.308  1.00 23.96 ? 314  GLN B CD  1 
ATOM   8263  O  OE1 . GLN B  1 314 ? -16.649 77.319 27.015  1.00 24.31 ? 314  GLN B OE1 1 
ATOM   8264  N  NE2 . GLN B  1 314 ? -15.354 75.526 26.525  1.00 21.54 ? 314  GLN B NE2 1 
ATOM   8265  N  N   . TRP B  1 315 ? -12.742 78.681 23.515  1.00 15.87 ? 315  TRP B N   1 
ATOM   8266  C  CA  . TRP B  1 315 ? -11.394 79.055 23.848  1.00 16.11 ? 315  TRP B CA  1 
ATOM   8267  C  C   . TRP B  1 315 ? -11.311 79.354 25.349  1.00 17.43 ? 315  TRP B C   1 
ATOM   8268  O  O   . TRP B  1 315 ? -12.316 79.737 25.968  1.00 17.22 ? 315  TRP B O   1 
ATOM   8269  C  CB  . TRP B  1 315 ? -11.009 80.272 23.019  1.00 15.43 ? 315  TRP B CB  1 
ATOM   8270  C  CG  . TRP B  1 315 ? -11.191 80.043 21.515  1.00 16.88 ? 315  TRP B CG  1 
ATOM   8271  C  CD1 . TRP B  1 315 ? -12.303 80.334 20.762  1.00 16.96 ? 315  TRP B CD1 1 
ATOM   8272  C  CD2 . TRP B  1 315 ? -10.192 79.582 20.592  1.00 16.86 ? 315  TRP B CD2 1 
ATOM   8273  N  NE1 . TRP B  1 315 ? -12.047 80.101 19.426  1.00 18.12 ? 315  TRP B NE1 1 
ATOM   8274  C  CE2 . TRP B  1 315 ? -10.760 79.639 19.295  1.00 17.84 ? 315  TRP B CE2 1 
ATOM   8275  C  CE3 . TRP B  1 315 ? -8.865  79.133 20.733  1.00 15.98 ? 315  TRP B CE3 1 
ATOM   8276  C  CZ2 . TRP B  1 315 ? -10.044 79.267 18.147  1.00 17.39 ? 315  TRP B CZ2 1 
ATOM   8277  C  CZ3 . TRP B  1 315 ? -8.153  78.764 19.593  1.00 15.61 ? 315  TRP B CZ3 1 
ATOM   8278  C  CH2 . TRP B  1 315 ? -8.744  78.836 18.316  1.00 16.01 ? 315  TRP B CH2 1 
ATOM   8279  N  N   . LEU B  1 316 ? -10.118 79.172 25.916  1.00 17.59 ? 316  LEU B N   1 
ATOM   8280  C  CA  . LEU B  1 316 ? -9.868  79.402 27.336  1.00 17.84 ? 316  LEU B CA  1 
ATOM   8281  C  C   . LEU B  1 316 ? -8.564  80.190 27.484  1.00 18.25 ? 316  LEU B C   1 
ATOM   8282  O  O   . LEU B  1 316 ? -7.555  79.849 26.856  1.00 16.98 ? 316  LEU B O   1 
ATOM   8283  C  CB  . LEU B  1 316 ? -9.745  78.051 28.054  1.00 17.04 ? 316  LEU B CB  1 
ATOM   8284  C  CG  . LEU B  1 316 ? -9.522  78.024 29.569  1.00 17.69 ? 316  LEU B CG  1 
ATOM   8285  C  CD1 . LEU B  1 316 ? -10.732 78.666 30.273  1.00 17.70 ? 316  LEU B CD1 1 
ATOM   8286  C  CD2 . LEU B  1 316 ? -9.367  76.588 30.041  1.00 17.12 ? 316  LEU B CD2 1 
ATOM   8287  N  N   . ARG B  1 317 ? -8.582  81.252 28.288  1.00 18.20 ? 317  ARG B N   1 
ATOM   8288  C  CA  . ARG B  1 317 ? -7.373  82.042 28.499  1.00 19.40 ? 317  ARG B CA  1 
ATOM   8289  C  C   . ARG B  1 317 ? -6.363  81.212 29.273  1.00 17.87 ? 317  ARG B C   1 
ATOM   8290  O  O   . ARG B  1 317 ? -6.748  80.341 30.051  1.00 17.89 ? 317  ARG B O   1 
ATOM   8291  C  CB  . ARG B  1 317 ? -7.682  83.317 29.284  1.00 20.45 ? 317  ARG B CB  1 
ATOM   8292  C  CG  . ARG B  1 317 ? -8.288  84.421 28.436  1.00 23.62 ? 317  ARG B CG  1 
ATOM   8293  C  CD  . ARG B  1 317 ? -8.504  85.689 29.265  1.00 25.16 ? 317  ARG B CD  1 
ATOM   8294  N  NE  . ARG B  1 317 ? -8.851  86.812 28.400  1.00 27.04 ? 317  ARG B NE  1 
ATOM   8295  C  CZ  . ARG B  1 317 ? -9.517  87.892 28.801  1.00 27.80 ? 317  ARG B CZ  1 
ATOM   8296  N  NH1 . ARG B  1 317 ? -9.919  88.009 30.057  1.00 28.35 ? 317  ARG B NH1 1 
ATOM   8297  N  NH2 . ARG B  1 317 ? -9.788  88.851 27.936  1.00 28.59 ? 317  ARG B NH2 1 
ATOM   8298  N  N   . ARG B  1 318 ? -5.076  81.478 29.079  1.00 18.39 ? 318  ARG B N   1 
ATOM   8299  C  CA  . ARG B  1 318 ? -4.072  80.706 29.805  1.00 18.62 ? 318  ARG B CA  1 
ATOM   8300  C  C   . ARG B  1 318 ? -4.355  80.834 31.307  1.00 20.71 ? 318  ARG B C   1 
ATOM   8301  O  O   . ARG B  1 318 ? -4.113  79.901 32.059  1.00 20.34 ? 318  ARG B O   1 
ATOM   8302  C  CB  . ARG B  1 318 ? -2.648  81.158 29.474  1.00 17.67 ? 318  ARG B CB  1 
ATOM   8303  C  CG  . ARG B  1 318 ? -1.613  80.282 30.178  1.00 16.43 ? 318  ARG B CG  1 
ATOM   8304  C  CD  . ARG B  1 318 ? -0.213  80.379 29.616  1.00 16.83 ? 318  ARG B CD  1 
ATOM   8305  N  NE  . ARG B  1 318 ? 0.704   79.583 30.442  1.00 16.45 ? 318  ARG B NE  1 
ATOM   8306  C  CZ  . ARG B  1 318 ? 1.926   79.230 30.066  1.00 16.34 ? 318  ARG B CZ  1 
ATOM   8307  N  NH1 . ARG B  1 318 ? 2.377   79.611 28.873  1.00 15.77 ? 318  ARG B NH1 1 
ATOM   8308  N  NH2 . ARG B  1 318 ? 2.688   78.488 30.868  1.00 14.35 ? 318  ARG B NH2 1 
ATOM   8309  N  N   . ILE B  1 319 ? -4.843  81.994 31.740  1.00 22.54 ? 319  ILE B N   1 
ATOM   8310  C  CA  . ILE B  1 319 ? -5.250  82.167 33.136  1.00 25.22 ? 319  ILE B CA  1 
ATOM   8311  C  C   . ILE B  1 319 ? -6.668  81.630 32.983  1.00 25.26 ? 319  ILE B C   1 
ATOM   8312  O  O   . ILE B  1 319 ? -7.568  82.344 32.556  1.00 26.20 ? 319  ILE B O   1 
ATOM   8313  C  CB  . ILE B  1 319 ? -5.299  83.654 33.541  1.00 25.90 ? 319  ILE B CB  1 
ATOM   8314  C  CG1 . ILE B  1 319 ? -3.904  84.246 33.518  1.00 27.22 ? 319  ILE B CG1 1 
ATOM   8315  C  CG2 . ILE B  1 319 ? -5.859  83.795 34.948  1.00 27.39 ? 319  ILE B CG2 1 
ATOM   8316  C  CD1 . ILE B  1 319 ? -2.978  83.541 34.455  1.00 30.42 ? 319  ILE B CD1 1 
ATOM   8317  N  N   . GLN B  1 320 ? -6.849  80.362 33.315  1.00 25.85 ? 320  GLN B N   1 
ATOM   8318  C  CA  . GLN B  1 320 ? -8.107  79.664 33.120  1.00 25.18 ? 320  GLN B CA  1 
ATOM   8319  C  C   . GLN B  1 320 ? -9.355  80.071 33.894  1.00 27.29 ? 320  GLN B C   1 
ATOM   8320  O  O   . GLN B  1 320 ? -10.062 79.229 34.433  1.00 27.63 ? 320  GLN B O   1 
ATOM   8321  C  CB  . GLN B  1 320 ? -7.846  78.184 33.311  1.00 23.53 ? 320  GLN B CB  1 
ATOM   8322  C  CG  . GLN B  1 320 ? -6.693  77.686 32.464  1.00 21.60 ? 320  GLN B CG  1 
ATOM   8323  C  CD  . GLN B  1 320 ? -6.431  76.216 32.650  1.00 20.79 ? 320  GLN B CD  1 
ATOM   8324  O  OE1 . GLN B  1 320 ? -7.368  75.413 32.714  1.00 19.76 ? 320  GLN B OE1 1 
ATOM   8325  N  NE2 . GLN B  1 320 ? -5.151  75.843 32.719  1.00 18.22 ? 320  GLN B NE2 1 
ATOM   8326  N  N   . ASN B  1 321 ? -9.657  81.354 33.914  1.00 28.89 ? 321  ASN B N   1 
ATOM   8327  C  CA  . ASN B  1 321 ? -10.839 81.818 34.637  1.00 30.69 ? 321  ASN B CA  1 
ATOM   8328  C  C   . ASN B  1 321 ? -11.804 82.547 33.690  1.00 29.52 ? 321  ASN B C   1 
ATOM   8329  O  O   . ASN B  1 321 ? -12.760 83.189 34.133  1.00 29.51 ? 321  ASN B O   1 
ATOM   8330  C  CB  . ASN B  1 321 ? -10.386 82.771 35.724  1.00 32.55 ? 321  ASN B CB  1 
ATOM   8331  C  CG  . ASN B  1 321 ? -9.920  84.071 35.159  1.00 37.35 ? 321  ASN B CG  1 
ATOM   8332  O  OD1 . ASN B  1 321 ? -9.208  84.123 34.168  1.00 37.40 ? 321  ASN B OD1 1 
ATOM   8333  N  ND2 . ASN B  1 321 ? -10.355 85.145 35.787  1.00 43.08 ? 321  ASN B ND2 1 
ATOM   8334  N  N   . TYR B  1 322 ? -11.541 82.444 32.391  1.00 27.95 ? 322  TYR B N   1 
ATOM   8335  C  CA  . TYR B  1 322 ? -12.351 83.112 31.383  1.00 26.90 ? 322  TYR B CA  1 
ATOM   8336  C  C   . TYR B  1 322 ? -12.375 82.281 30.096  1.00 26.39 ? 322  TYR B C   1 
ATOM   8337  O  O   . TYR B  1 322 ? -11.330 82.071 29.467  1.00 25.00 ? 322  TYR B O   1 
ATOM   8338  C  CB  . TYR B  1 322 ? -11.737 84.474 31.100  1.00 28.34 ? 322  TYR B CB  1 
ATOM   8339  C  CG  . TYR B  1 322 ? -12.580 85.407 30.272  1.00 29.39 ? 322  TYR B CG  1 
ATOM   8340  C  CD1 . TYR B  1 322 ? -12.361 85.556 28.902  1.00 30.43 ? 322  TYR B CD1 1 
ATOM   8341  C  CD2 . TYR B  1 322 ? -13.577 86.179 30.869  1.00 30.37 ? 322  TYR B CD2 1 
ATOM   8342  C  CE1 . TYR B  1 322 ? -13.116 86.461 28.147  1.00 30.18 ? 322  TYR B CE1 1 
ATOM   8343  C  CE2 . TYR B  1 322 ? -14.336 87.082 30.124  1.00 31.68 ? 322  TYR B CE2 1 
ATOM   8344  C  CZ  . TYR B  1 322 ? -14.098 87.217 28.773  1.00 31.46 ? 322  TYR B CZ  1 
ATOM   8345  O  OH  . TYR B  1 322 ? -14.834 88.123 28.052  1.00 33.24 ? 322  TYR B OH  1 
ATOM   8346  N  N   . SER B  1 323 ? -13.562 81.807 29.716  1.00 25.00 ? 323  SER B N   1 
ATOM   8347  C  CA  . SER B  1 323 ? -13.739 81.005 28.505  1.00 23.23 ? 323  SER B CA  1 
ATOM   8348  C  C   . SER B  1 323 ? -14.699 81.713 27.555  1.00 22.47 ? 323  SER B C   1 
ATOM   8349  O  O   . SER B  1 323 ? -15.621 82.418 27.989  1.00 23.23 ? 323  SER B O   1 
ATOM   8350  C  CB  . SER B  1 323 ? -14.319 79.634 28.847  1.00 22.41 ? 323  SER B CB  1 
ATOM   8351  O  OG  . SER B  1 323 ? -15.657 79.788 29.280  1.00 23.61 ? 323  SER B OG  1 
ATOM   8352  N  N   . VAL B  1 324 ? -14.488 81.527 26.263  1.00 19.93 ? 324  VAL B N   1 
ATOM   8353  C  CA  . VAL B  1 324 ? -15.346 82.154 25.266  1.00 19.71 ? 324  VAL B CA  1 
ATOM   8354  C  C   . VAL B  1 324 ? -15.755 81.124 24.220  1.00 19.81 ? 324  VAL B C   1 
ATOM   8355  O  O   . VAL B  1 324 ? -14.900 80.513 23.562  1.00 19.15 ? 324  VAL B O   1 
ATOM   8356  C  CB  . VAL B  1 324 ? -14.620 83.307 24.527  1.00 19.68 ? 324  VAL B CB  1 
ATOM   8357  C  CG1 . VAL B  1 324 ? -15.545 83.913 23.473  1.00 19.54 ? 324  VAL B CG1 1 
ATOM   8358  C  CG2 . VAL B  1 324 ? -14.166 84.368 25.514  1.00 18.43 ? 324  VAL B CG2 1 
ATOM   8359  N  N   . MET B  1 325 ? -17.053 80.930 24.074  1.00 18.42 ? 325  MET B N   1 
ATOM   8360  C  CA  . MET B  1 325 ? -17.572 80.000 23.081  1.00 17.87 ? 325  MET B CA  1 
ATOM   8361  C  C   . MET B  1 325 ? -18.177 80.751 21.895  1.00 17.81 ? 325  MET B C   1 
ATOM   8362  O  O   . MET B  1 325 ? -19.065 81.590 22.075  1.00 17.55 ? 325  MET B O   1 
ATOM   8363  C  CB  . MET B  1 325 ? -18.644 79.118 23.697  1.00 18.19 ? 325  MET B CB  1 
ATOM   8364  C  CG  . MET B  1 325 ? -19.374 78.239 22.692  1.00 19.48 ? 325  MET B CG  1 
ATOM   8365  S  SD  . MET B  1 325 ? -20.937 77.805 23.416  1.00 21.57 ? 325  MET B SD  1 
ATOM   8366  C  CE  . MET B  1 325 ? -21.601 76.700 22.203  1.00 19.49 ? 325  MET B CE  1 
ATOM   8367  N  N   . ASP B  1 326 ? -17.680 80.442 20.699  1.00 16.46 ? 326  ASP B N   1 
ATOM   8368  C  CA  . ASP B  1 326 ? -18.155 81.032 19.454  1.00 16.53 ? 326  ASP B CA  1 
ATOM   8369  C  C   . ASP B  1 326 ? -19.036 80.023 18.739  1.00 16.21 ? 326  ASP B C   1 
ATOM   8370  O  O   . ASP B  1 326 ? -18.792 78.815 18.793  1.00 14.58 ? 326  ASP B O   1 
ATOM   8371  C  CB  . ASP B  1 326 ? -16.986 81.400 18.522  1.00 16.71 ? 326  ASP B CB  1 
ATOM   8372  C  CG  . ASP B  1 326 ? -16.552 82.839 18.668  1.00 18.84 ? 326  ASP B CG  1 
ATOM   8373  O  OD1 . ASP B  1 326 ? -17.387 83.675 19.102  1.00 18.86 ? 326  ASP B OD1 1 
ATOM   8374  O  OD2 . ASP B  1 326 ? -15.379 83.147 18.328  1.00 17.82 ? 326  ASP B OD2 1 
ATOM   8375  N  N   . ILE B  1 327 ? -20.055 80.524 18.054  1.00 15.52 ? 327  ILE B N   1 
ATOM   8376  C  CA  . ILE B  1 327 ? -20.963 79.667 17.313  1.00 16.25 ? 327  ILE B CA  1 
ATOM   8377  C  C   . ILE B  1 327 ? -20.940 80.218 15.896  1.00 17.11 ? 327  ILE B C   1 
ATOM   8378  O  O   . ILE B  1 327 ? -21.440 81.309 15.614  1.00 17.45 ? 327  ILE B O   1 
ATOM   8379  C  CB  . ILE B  1 327 ? -22.346 79.688 17.969  1.00 16.43 ? 327  ILE B CB  1 
ATOM   8380  C  CG1 . ILE B  1 327 ? -22.212 79.060 19.381  1.00 17.59 ? 327  ILE B CG1 1 
ATOM   8381  C  CG2 . ILE B  1 327 ? -23.342 78.921 17.120  1.00 15.64 ? 327  ILE B CG2 1 
ATOM   8382  C  CD1 . ILE B  1 327 ? -23.480 79.115 20.224  1.00 16.36 ? 327  ILE B CD1 1 
ATOM   8383  N  N   . CYS B  1 328 ? -20.350 79.434 15.003  1.00 18.32 ? 328  CYS B N   1 
ATOM   8384  C  CA  . CYS B  1 328 ? -20.124 79.863 13.631  1.00 19.43 ? 328  CYS B CA  1 
ATOM   8385  C  C   . CYS B  1 328 ? -20.914 79.181 12.522  1.00 19.67 ? 328  CYS B C   1 
ATOM   8386  O  O   . CYS B  1 328 ? -21.013 77.953 12.469  1.00 19.87 ? 328  CYS B O   1 
ATOM   8387  C  CB  . CYS B  1 328 ? -18.628 79.716 13.356  1.00 20.66 ? 328  CYS B CB  1 
ATOM   8388  S  SG  . CYS B  1 328 ? -17.561 80.221 14.748  1.00 22.16 ? 328  CYS B SG  1 
ATOM   8389  N  N   . ASP B  1 329 ? -21.449 79.999 11.619  1.00 20.10 ? 329  ASP B N   1 
ATOM   8390  C  CA  . ASP B  1 329 ? -22.236 79.520 10.492  1.00 20.40 ? 329  ASP B CA  1 
ATOM   8391  C  C   . ASP B  1 329 ? -21.488 79.610 9.168   1.00 21.84 ? 329  ASP B C   1 
ATOM   8392  O  O   . ASP B  1 329 ? -20.713 80.536 8.934   1.00 19.75 ? 329  ASP B O   1 
ATOM   8393  C  CB  . ASP B  1 329 ? -23.530 80.321 10.381  1.00 20.98 ? 329  ASP B CB  1 
ATOM   8394  C  CG  . ASP B  1 329 ? -24.532 79.939 11.439  1.00 23.71 ? 329  ASP B CG  1 
ATOM   8395  O  OD1 . ASP B  1 329 ? -24.176 79.171 12.359  1.00 24.26 ? 329  ASP B OD1 1 
ATOM   8396  O  OD2 . ASP B  1 329 ? -25.674 80.404 11.349  1.00 24.82 ? 329  ASP B OD2 1 
ATOM   8397  N  N   . TYR B  1 330 ? -21.736 78.640 8.297   1.00 23.56 ? 330  TYR B N   1 
ATOM   8398  C  CA  . TYR B  1 330 ? -21.097 78.627 7.000   1.00 26.51 ? 330  TYR B CA  1 
ATOM   8399  C  C   . TYR B  1 330 ? -21.844 79.613 6.102   1.00 28.10 ? 330  TYR B C   1 
ATOM   8400  O  O   . TYR B  1 330 ? -23.071 79.597 6.053   1.00 27.92 ? 330  TYR B O   1 
ATOM   8401  C  CB  . TYR B  1 330 ? -21.169 77.227 6.400   1.00 27.18 ? 330  TYR B CB  1 
ATOM   8402  C  CG  . TYR B  1 330 ? -20.557 77.145 5.029   1.00 27.79 ? 330  TYR B CG  1 
ATOM   8403  C  CD1 . TYR B  1 330 ? -19.197 77.399 4.837   1.00 27.63 ? 330  TYR B CD1 1 
ATOM   8404  C  CD2 . TYR B  1 330 ? -21.342 76.843 3.917   1.00 28.16 ? 330  TYR B CD2 1 
ATOM   8405  C  CE1 . TYR B  1 330 ? -18.633 77.355 3.575   1.00 28.06 ? 330  TYR B CE1 1 
ATOM   8406  C  CE2 . TYR B  1 330 ? -20.789 76.793 2.646   1.00 28.93 ? 330  TYR B CE2 1 
ATOM   8407  C  CZ  . TYR B  1 330 ? -19.429 77.052 2.483   1.00 28.76 ? 330  TYR B CZ  1 
ATOM   8408  O  OH  . TYR B  1 330 ? -18.867 77.004 1.230   1.00 29.89 ? 330  TYR B OH  1 
ATOM   8409  N  N   . ASP B  1 331 ? -21.095 80.461 5.409   1.00 30.19 ? 331  ASP B N   1 
ATOM   8410  C  CA  . ASP B  1 331 ? -21.640 81.465 4.491   1.00 33.12 ? 331  ASP B CA  1 
ATOM   8411  C  C   . ASP B  1 331 ? -21.448 80.909 3.082   1.00 34.98 ? 331  ASP B C   1 
ATOM   8412  O  O   . ASP B  1 331 ? -20.371 81.033 2.498   1.00 35.13 ? 331  ASP B O   1 
ATOM   8413  C  CB  . ASP B  1 331 ? -20.861 82.772 4.640   1.00 34.01 ? 331  ASP B CB  1 
ATOM   8414  C  CG  . ASP B  1 331 ? -21.437 83.916 3.802   1.00 35.75 ? 331  ASP B CG  1 
ATOM   8415  O  OD1 . ASP B  1 331 ? -22.306 83.668 2.936   1.00 36.21 ? 331  ASP B OD1 1 
ATOM   8416  O  OD2 . ASP B  1 331 ? -20.997 85.071 4.015   1.00 36.31 ? 331  ASP B OD2 1 
ATOM   8417  N  N   . GLU B  1 332 ? -22.498 80.306 2.549   1.00 37.17 ? 332  GLU B N   1 
ATOM   8418  C  CA  . GLU B  1 332 ? -22.466 79.685 1.232   1.00 40.33 ? 332  GLU B CA  1 
ATOM   8419  C  C   . GLU B  1 332 ? -22.124 80.606 0.066   1.00 41.79 ? 332  GLU B C   1 
ATOM   8420  O  O   . GLU B  1 332 ? -21.930 80.129 -1.055  1.00 42.45 ? 332  GLU B O   1 
ATOM   8421  C  CB  . GLU B  1 332 ? -23.812 79.013 0.972   1.00 42.14 ? 332  GLU B CB  1 
ATOM   8422  C  CG  . GLU B  1 332 ? -23.931 78.323 -0.368  1.00 45.05 ? 332  GLU B CG  1 
ATOM   8423  C  CD  . GLU B  1 332 ? -25.319 77.748 -0.588  1.00 47.28 ? 332  GLU B CD  1 
ATOM   8424  O  OE1 . GLU B  1 332 ? -25.720 76.833 0.174   1.00 47.54 ? 332  GLU B OE1 1 
ATOM   8425  O  OE2 . GLU B  1 332 ? -26.018 78.215 -1.521  1.00 48.54 ? 332  GLU B OE2 1 
ATOM   8426  N  N   . SER B  1 333 ? -22.049 81.913 0.315   1.00 42.29 ? 333  SER B N   1 
ATOM   8427  C  CA  . SER B  1 333 ? -21.738 82.853 -0.755  1.00 42.95 ? 333  SER B CA  1 
ATOM   8428  C  C   . SER B  1 333 ? -20.286 83.320 -0.711  1.00 43.80 ? 333  SER B C   1 
ATOM   8429  O  O   . SER B  1 333 ? -19.789 83.896 -1.679  1.00 44.49 ? 333  SER B O   1 
ATOM   8430  C  CB  . SER B  1 333 ? -22.663 84.075 -0.687  1.00 43.35 ? 333  SER B CB  1 
ATOM   8431  O  OG  . SER B  1 333 ? -22.315 84.928 0.394   1.00 43.02 ? 333  SER B OG  1 
ATOM   8432  N  N   . SER B  1 334 ? -19.611 83.086 0.412   1.00 43.46 ? 334  SER B N   1 
ATOM   8433  C  CA  . SER B  1 334 ? -18.215 83.488 0.555   1.00 42.49 ? 334  SER B CA  1 
ATOM   8434  C  C   . SER B  1 334 ? -17.352 82.296 0.933   1.00 41.59 ? 334  SER B C   1 
ATOM   8435  O  O   . SER B  1 334 ? -16.137 82.412 1.049   1.00 42.64 ? 334  SER B O   1 
ATOM   8436  C  CB  . SER B  1 334 ? -18.067 84.578 1.625   1.00 42.38 ? 334  SER B CB  1 
ATOM   8437  O  OG  . SER B  1 334 ? -18.286 84.062 2.930   1.00 43.56 ? 334  SER B OG  1 
ATOM   8438  N  N   . GLY B  1 335 ? -17.984 81.146 1.118   1.00 40.38 ? 335  GLY B N   1 
ATOM   8439  C  CA  . GLY B  1 335 ? -17.244 79.960 1.498   1.00 38.27 ? 335  GLY B CA  1 
ATOM   8440  C  C   . GLY B  1 335 ? -16.512 80.152 2.814   1.00 37.12 ? 335  GLY B C   1 
ATOM   8441  O  O   . GLY B  1 335 ? -15.610 79.382 3.146   1.00 37.37 ? 335  GLY B O   1 
ATOM   8442  N  N   . ARG B  1 336 ? -16.901 81.175 3.571   1.00 35.26 ? 336  ARG B N   1 
ATOM   8443  C  CA  . ARG B  1 336 ? -16.255 81.463 4.848   1.00 33.92 ? 336  ARG B CA  1 
ATOM   8444  C  C   . ARG B  1 336 ? -17.122 81.074 6.052   1.00 31.35 ? 336  ARG B C   1 
ATOM   8445  O  O   . ARG B  1 336 ? -18.275 80.666 5.899   1.00 31.10 ? 336  ARG B O   1 
ATOM   8446  C  CB  . ARG B  1 336 ? -15.922 82.955 4.924   1.00 35.86 ? 336  ARG B CB  1 
ATOM   8447  C  CG  . ARG B  1 336 ? -15.142 83.502 3.725   1.00 38.24 ? 336  ARG B CG  1 
ATOM   8448  C  CD  . ARG B  1 336 ? -13.708 82.988 3.676   1.00 39.57 ? 336  ARG B CD  1 
ATOM   8449  N  NE  . ARG B  1 336 ? -12.992 83.243 4.932   1.00 40.71 ? 336  ARG B NE  1 
ATOM   8450  C  CZ  . ARG B  1 336 ? -11.687 83.056 5.105   1.00 40.43 ? 336  ARG B CZ  1 
ATOM   8451  N  NH1 . ARG B  1 336 ? -10.933 82.619 4.101   1.00 40.68 ? 336  ARG B NH1 1 
ATOM   8452  N  NH2 . ARG B  1 336 ? -11.141 83.271 6.293   1.00 41.55 ? 336  ARG B NH2 1 
ATOM   8453  N  N   . TRP B  1 337 ? -16.548 81.185 7.243   1.00 28.30 ? 337  TRP B N   1 
ATOM   8454  C  CA  . TRP B  1 337 ? -17.261 80.876 8.465   1.00 26.73 ? 337  TRP B CA  1 
ATOM   8455  C  C   . TRP B  1 337 ? -17.353 82.131 9.324   1.00 27.24 ? 337  TRP B C   1 
ATOM   8456  O  O   . TRP B  1 337 ? -16.349 82.767 9.627   1.00 28.87 ? 337  TRP B O   1 
ATOM   8457  C  CB  . TRP B  1 337 ? -16.562 79.750 9.220   1.00 23.22 ? 337  TRP B CB  1 
ATOM   8458  C  CG  . TRP B  1 337 ? -16.661 78.421 8.506   1.00 19.23 ? 337  TRP B CG  1 
ATOM   8459  C  CD1 . TRP B  1 337 ? -15.845 77.949 7.511   1.00 16.61 ? 337  TRP B CD1 1 
ATOM   8460  C  CD2 . TRP B  1 337 ? -17.651 77.413 8.724   1.00 17.35 ? 337  TRP B CD2 1 
ATOM   8461  N  NE1 . TRP B  1 337 ? -16.267 76.704 7.099   1.00 17.94 ? 337  TRP B NE1 1 
ATOM   8462  C  CE2 . TRP B  1 337 ? -17.374 76.351 7.825   1.00 17.45 ? 337  TRP B CE2 1 
ATOM   8463  C  CE3 . TRP B  1 337 ? -18.748 77.300 9.593   1.00 16.51 ? 337  TRP B CE3 1 
ATOM   8464  C  CZ2 . TRP B  1 337 ? -18.152 75.195 7.769   1.00 17.11 ? 337  TRP B CZ2 1 
ATOM   8465  C  CZ3 . TRP B  1 337 ? -19.525 76.149 9.540   1.00 17.30 ? 337  TRP B CZ3 1 
ATOM   8466  C  CH2 . TRP B  1 337 ? -19.223 75.110 8.632   1.00 17.70 ? 337  TRP B CH2 1 
ATOM   8467  N  N   . ASN B  1 338 ? -18.566 82.496 9.706   1.00 26.97 ? 338  ASN B N   1 
ATOM   8468  C  CA  . ASN B  1 338 ? -18.762 83.694 10.505  1.00 27.51 ? 338  ASN B CA  1 
ATOM   8469  C  C   . ASN B  1 338 ? -19.385 83.386 11.857  1.00 25.94 ? 338  ASN B C   1 
ATOM   8470  O  O   . ASN B  1 338 ? -20.363 82.635 11.959  1.00 24.41 ? 338  ASN B O   1 
ATOM   8471  C  CB  . ASN B  1 338 ? -19.628 84.687 9.727   1.00 29.34 ? 338  ASN B CB  1 
ATOM   8472  C  CG  . ASN B  1 338 ? -18.937 85.186 8.465   1.00 32.50 ? 338  ASN B CG  1 
ATOM   8473  O  OD1 . ASN B  1 338 ? -19.504 85.121 7.366   1.00 34.48 ? 338  ASN B OD1 1 
ATOM   8474  N  ND2 . ASN B  1 338 ? -17.708 85.688 8.616   1.00 32.02 ? 338  ASN B ND2 1 
ATOM   8475  N  N   . CYS B  1 339 ? -18.806 83.988 12.886  1.00 24.22 ? 339  CYS B N   1 
ATOM   8476  C  CA  . CYS B  1 339 ? -19.266 83.777 14.241  1.00 24.34 ? 339  CYS B CA  1 
ATOM   8477  C  C   . CYS B  1 339 ? -19.860 85.083 14.817  1.00 23.79 ? 339  CYS B C   1 
ATOM   8478  O  O   . CYS B  1 339 ? -19.137 85.992 15.250  1.00 23.85 ? 339  CYS B O   1 
ATOM   8479  C  CB  . CYS B  1 339 ? -18.094 83.255 15.088  1.00 23.67 ? 339  CYS B CB  1 
ATOM   8480  S  SG  . CYS B  1 339 ? -16.936 82.089 14.218  1.00 23.62 ? 339  CYS B SG  1 
ATOM   8481  N  N   . LEU B  1 340 ? -21.184 85.175 14.800  1.00 22.73 ? 340  LEU B N   1 
ATOM   8482  C  CA  . LEU B  1 340 ? -21.881 86.360 15.308  1.00 21.85 ? 340  LEU B CA  1 
ATOM   8483  C  C   . LEU B  1 340 ? -21.603 86.551 16.781  1.00 21.19 ? 340  LEU B C   1 
ATOM   8484  O  O   . LEU B  1 340 ? -21.824 85.644 17.584  1.00 19.11 ? 340  LEU B O   1 
ATOM   8485  C  CB  . LEU B  1 340 ? -23.388 86.213 15.114  1.00 23.46 ? 340  LEU B CB  1 
ATOM   8486  C  CG  . LEU B  1 340 ? -23.877 86.223 13.676  1.00 24.28 ? 340  LEU B CG  1 
ATOM   8487  C  CD1 . LEU B  1 340 ? -25.358 85.892 13.662  1.00 25.48 ? 340  LEU B CD1 1 
ATOM   8488  C  CD2 . LEU B  1 340 ? -23.611 87.595 13.063  1.00 25.59 ? 340  LEU B CD2 1 
ATOM   8489  N  N   . VAL B  1 341 ? -21.121 87.735 17.140  1.00 19.78 ? 341  VAL B N   1 
ATOM   8490  C  CA  . VAL B  1 341 ? -20.827 88.015 18.533  1.00 20.85 ? 341  VAL B CA  1 
ATOM   8491  C  C   . VAL B  1 341 ? -22.088 87.838 19.397  1.00 19.23 ? 341  VAL B C   1 
ATOM   8492  O  O   . VAL B  1 341 ? -21.984 87.536 20.574  1.00 19.65 ? 341  VAL B O   1 
ATOM   8493  C  CB  . VAL B  1 341 ? -20.220 89.445 18.700  1.00 22.35 ? 341  VAL B CB  1 
ATOM   8494  C  CG1 . VAL B  1 341 ? -21.203 90.477 18.181  1.00 26.07 ? 341  VAL B CG1 1 
ATOM   8495  C  CG2 . VAL B  1 341 ? -19.873 89.720 20.179  1.00 22.97 ? 341  VAL B CG2 1 
ATOM   8496  N  N   . ALA B  1 342 ? -23.273 87.998 18.816  1.00 18.34 ? 342  ALA B N   1 
ATOM   8497  C  CA  . ALA B  1 342 ? -24.509 87.820 19.582  1.00 17.79 ? 342  ALA B CA  1 
ATOM   8498  C  C   . ALA B  1 342 ? -24.706 86.351 19.958  1.00 18.33 ? 342  ALA B C   1 
ATOM   8499  O  O   . ALA B  1 342 ? -25.585 86.021 20.771  1.00 18.12 ? 342  ALA B O   1 
ATOM   8500  C  CB  . ALA B  1 342 ? -25.705 88.301 18.781  1.00 17.79 ? 342  ALA B CB  1 
ATOM   8501  N  N   . ARG B  1 343 ? -23.899 85.474 19.352  1.00 18.22 ? 343  ARG B N   1 
ATOM   8502  C  CA  . ARG B  1 343 ? -23.981 84.041 19.622  1.00 18.51 ? 343  ARG B CA  1 
ATOM   8503  C  C   . ARG B  1 343 ? -22.771 83.544 20.386  1.00 18.31 ? 343  ARG B C   1 
ATOM   8504  O  O   . ARG B  1 343 ? -22.547 82.339 20.491  1.00 19.41 ? 343  ARG B O   1 
ATOM   8505  C  CB  . ARG B  1 343 ? -24.114 83.244 18.319  1.00 19.76 ? 343  ARG B CB  1 
ATOM   8506  C  CG  . ARG B  1 343 ? -25.433 83.470 17.601  1.00 21.04 ? 343  ARG B CG  1 
ATOM   8507  C  CD  . ARG B  1 343 ? -25.405 82.840 16.219  1.00 23.27 ? 343  ARG B CD  1 
ATOM   8508  N  NE  . ARG B  1 343 ? -26.681 83.015 15.522  1.00 23.92 ? 343  ARG B NE  1 
ATOM   8509  C  CZ  . ARG B  1 343 ? -26.922 82.581 14.291  1.00 25.15 ? 343  ARG B CZ  1 
ATOM   8510  N  NH1 . ARG B  1 343 ? -25.976 81.951 13.616  1.00 25.66 ? 343  ARG B NH1 1 
ATOM   8511  N  NH2 . ARG B  1 343 ? -28.113 82.775 13.736  1.00 26.32 ? 343  ARG B NH2 1 
ATOM   8512  N  N   . GLN B  1 344 ? -21.988 84.483 20.899  1.00 18.36 ? 344  GLN B N   1 
ATOM   8513  C  CA  . GLN B  1 344 ? -20.788 84.192 21.670  1.00 18.62 ? 344  GLN B CA  1 
ATOM   8514  C  C   . GLN B  1 344 ? -21.213 84.075 23.125  1.00 20.21 ? 344  GLN B C   1 
ATOM   8515  O  O   . GLN B  1 344 ? -21.995 84.898 23.612  1.00 22.73 ? 344  GLN B O   1 
ATOM   8516  C  CB  . GLN B  1 344 ? -19.799 85.338 21.491  1.00 17.78 ? 344  GLN B CB  1 
ATOM   8517  C  CG  . GLN B  1 344 ? -18.419 85.093 22.028  1.00 18.90 ? 344  GLN B CG  1 
ATOM   8518  C  CD  . GLN B  1 344 ? -17.484 86.288 21.779  1.00 19.94 ? 344  GLN B CD  1 
ATOM   8519  O  OE1 . GLN B  1 344 ? -17.472 87.247 22.549  1.00 19.77 ? 344  GLN B OE1 1 
ATOM   8520  N  NE2 . GLN B  1 344 ? -16.709 86.227 20.698  1.00 18.62 ? 344  GLN B NE2 1 
ATOM   8521  N  N   . HIS B  1 345 ? -20.724 83.050 23.816  1.00 20.70 ? 345  HIS B N   1 
ATOM   8522  C  CA  . HIS B  1 345 ? -21.070 82.824 25.220  1.00 20.84 ? 345  HIS B CA  1 
ATOM   8523  C  C   . HIS B  1 345 ? -19.831 82.804 26.093  1.00 22.49 ? 345  HIS B C   1 
ATOM   8524  O  O   . HIS B  1 345 ? -18.835 82.143 25.768  1.00 22.50 ? 345  HIS B O   1 
ATOM   8525  C  CB  . HIS B  1 345 ? -21.824 81.512 25.353  1.00 19.15 ? 345  HIS B CB  1 
ATOM   8526  C  CG  . HIS B  1 345 ? -23.141 81.518 24.644  1.00 18.03 ? 345  HIS B CG  1 
ATOM   8527  N  ND1 . HIS B  1 345 ? -23.253 81.336 23.283  1.00 18.48 ? 345  HIS B ND1 1 
ATOM   8528  C  CD2 . HIS B  1 345 ? -24.394 81.746 25.098  1.00 14.99 ? 345  HIS B CD2 1 
ATOM   8529  C  CE1 . HIS B  1 345 ? -24.521 81.447 22.929  1.00 16.39 ? 345  HIS B CE1 1 
ATOM   8530  N  NE2 . HIS B  1 345 ? -25.233 81.699 24.012  1.00 16.90 ? 345  HIS B NE2 1 
ATOM   8531  N  N   . ILE B  1 346 ? -19.906 83.507 27.215  1.00 22.52 ? 346  ILE B N   1 
ATOM   8532  C  CA  . ILE B  1 346 ? -18.772 83.619 28.103  1.00 23.66 ? 346  ILE B CA  1 
ATOM   8533  C  C   . ILE B  1 346 ? -18.964 82.993 29.476  1.00 25.01 ? 346  ILE B C   1 
ATOM   8534  O  O   . ILE B  1 346 ? -20.081 82.960 30.013  1.00 24.58 ? 346  ILE B O   1 
ATOM   8535  C  CB  . ILE B  1 346 ? -18.403 85.116 28.276  1.00 24.68 ? 346  ILE B CB  1 
ATOM   8536  C  CG1 . ILE B  1 346 ? -17.971 85.679 26.915  1.00 26.43 ? 346  ILE B CG1 1 
ATOM   8537  C  CG2 . ILE B  1 346 ? -17.292 85.285 29.333  1.00 24.69 ? 346  ILE B CG2 1 
ATOM   8538  C  CD1 . ILE B  1 346 ? -17.823 87.182 26.870  1.00 29.20 ? 346  ILE B CD1 1 
ATOM   8539  N  N   . GLU B  1 347 ? -17.876 82.451 30.020  1.00 25.17 ? 347  GLU B N   1 
ATOM   8540  C  CA  . GLU B  1 347 ? -17.895 81.894 31.373  1.00 28.08 ? 347  GLU B CA  1 
ATOM   8541  C  C   . GLU B  1 347 ? -16.735 82.509 32.132  1.00 29.90 ? 347  GLU B C   1 
ATOM   8542  O  O   . GLU B  1 347 ? -15.654 82.735 31.564  1.00 30.05 ? 347  GLU B O   1 
ATOM   8543  C  CB  . GLU B  1 347 ? -17.775 80.375 31.370  1.00 26.76 ? 347  GLU B CB  1 
ATOM   8544  C  CG  . GLU B  1 347 ? -19.097 79.689 31.093  1.00 27.60 ? 347  GLU B CG  1 
ATOM   8545  C  CD  . GLU B  1 347 ? -19.021 78.176 31.115  1.00 27.48 ? 347  GLU B CD  1 
ATOM   8546  O  OE1 . GLU B  1 347 ? -19.470 77.557 30.136  1.00 28.72 ? 347  GLU B OE1 1 
ATOM   8547  O  OE2 . GLU B  1 347 ? -18.534 77.593 32.103  1.00 29.24 ? 347  GLU B OE2 1 
ATOM   8548  N  N   . MET B  1 348 ? -16.974 82.799 33.405  1.00 31.37 ? 348  MET B N   1 
ATOM   8549  C  CA  . MET B  1 348 ? -15.974 83.405 34.264  1.00 33.66 ? 348  MET B CA  1 
ATOM   8550  C  C   . MET B  1 348 ? -15.897 82.647 35.575  1.00 34.70 ? 348  MET B C   1 
ATOM   8551  O  O   . MET B  1 348 ? -16.904 82.164 36.100  1.00 34.30 ? 348  MET B O   1 
ATOM   8552  C  CB  . MET B  1 348 ? -16.320 84.866 34.548  1.00 34.99 ? 348  MET B CB  1 
ATOM   8553  C  CG  . MET B  1 348 ? -16.326 85.726 33.321  1.00 37.79 ? 348  MET B CG  1 
ATOM   8554  S  SD  . MET B  1 348 ? -16.426 87.454 33.744  1.00 40.67 ? 348  MET B SD  1 
ATOM   8555  C  CE  . MET B  1 348 ? -17.718 87.989 32.584  1.00 39.83 ? 348  MET B CE  1 
ATOM   8556  N  N   . SER B  1 349 ? -14.694 82.564 36.112  1.00 35.75 ? 349  SER B N   1 
ATOM   8557  C  CA  . SER B  1 349 ? -14.489 81.851 37.348  1.00 37.37 ? 349  SER B CA  1 
ATOM   8558  C  C   . SER B  1 349 ? -15.020 82.690 38.474  1.00 37.44 ? 349  SER B C   1 
ATOM   8559  O  O   . SER B  1 349 ? -14.971 83.918 38.424  1.00 38.91 ? 349  SER B O   1 
ATOM   8560  C  CB  . SER B  1 349 ? -13.011 81.634 37.594  1.00 38.74 ? 349  SER B CB  1 
ATOM   8561  O  OG  . SER B  1 349 ? -12.490 82.809 38.193  1.00 41.67 ? 349  SER B OG  1 
ATOM   8562  N  N   . THR B  1 350 ? -15.522 82.018 39.495  1.00 37.18 ? 350  THR B N   1 
ATOM   8563  C  CA  . THR B  1 350 ? -16.041 82.689 40.665  1.00 36.59 ? 350  THR B CA  1 
ATOM   8564  C  C   . THR B  1 350 ? -15.082 82.375 41.822  1.00 36.03 ? 350  THR B C   1 
ATOM   8565  O  O   . THR B  1 350 ? -14.088 83.080 42.047  1.00 35.05 ? 350  THR B O   1 
ATOM   8566  C  CB  . THR B  1 350 ? -17.477 82.187 40.971  1.00 37.33 ? 350  THR B CB  1 
ATOM   8567  O  OG1 . THR B  1 350 ? -17.485 80.752 41.056  1.00 37.79 ? 350  THR B OG1 1 
ATOM   8568  C  CG2 . THR B  1 350 ? -18.433 82.612 39.852  1.00 37.54 ? 350  THR B CG2 1 
ATOM   8569  N  N   . THR B  1 351 ? -15.358 81.278 42.516  1.00 35.32 ? 351  THR B N   1 
ATOM   8570  C  CA  . THR B  1 351 ? -14.547 80.870 43.649  1.00 34.92 ? 351  THR B CA  1 
ATOM   8571  C  C   . THR B  1 351 ? -13.362 79.954 43.284  1.00 34.01 ? 351  THR B C   1 
ATOM   8572  O  O   . THR B  1 351 ? -12.585 79.566 44.156  1.00 35.13 ? 351  THR B O   1 
ATOM   8573  C  CB  . THR B  1 351 ? -15.452 80.179 44.674  1.00 35.27 ? 351  THR B CB  1 
ATOM   8574  O  OG1 . THR B  1 351 ? -16.195 79.140 44.021  1.00 36.08 ? 351  THR B OG1 1 
ATOM   8575  C  CG2 . THR B  1 351 ? -16.445 81.177 45.256  1.00 34.80 ? 351  THR B CG2 1 
ATOM   8576  N  N   . GLY B  1 352 ? -13.218 79.615 42.003  1.00 32.20 ? 352  GLY B N   1 
ATOM   8577  C  CA  . GLY B  1 352 ? -12.129 78.748 41.599  1.00 29.72 ? 352  GLY B CA  1 
ATOM   8578  C  C   . GLY B  1 352 ? -11.849 78.764 40.112  1.00 28.79 ? 352  GLY B C   1 
ATOM   8579  O  O   . GLY B  1 352 ? -11.709 79.833 39.515  1.00 29.30 ? 352  GLY B O   1 
ATOM   8580  N  N   . TRP B  1 353 ? -11.761 77.588 39.496  1.00 26.51 ? 353  TRP B N   1 
ATOM   8581  C  CA  . TRP B  1 353 ? -11.490 77.527 38.063  1.00 25.28 ? 353  TRP B CA  1 
ATOM   8582  C  C   . TRP B  1 353 ? -12.800 77.296 37.303  1.00 23.93 ? 353  TRP B C   1 
ATOM   8583  O  O   . TRP B  1 353 ? -13.867 77.332 37.894  1.00 25.21 ? 353  TRP B O   1 
ATOM   8584  C  CB  . TRP B  1 353 ? -10.471 76.419 37.765  1.00 24.52 ? 353  TRP B CB  1 
ATOM   8585  C  CG  . TRP B  1 353 ? -10.846 75.083 38.328  1.00 23.39 ? 353  TRP B CG  1 
ATOM   8586  C  CD1 . TRP B  1 353 ? -11.518 74.086 37.689  1.00 22.91 ? 353  TRP B CD1 1 
ATOM   8587  C  CD2 . TRP B  1 353 ? -10.620 74.625 39.666  1.00 22.52 ? 353  TRP B CD2 1 
ATOM   8588  N  NE1 . TRP B  1 353 ? -11.731 73.032 38.546  1.00 22.40 ? 353  TRP B NE1 1 
ATOM   8589  C  CE2 . TRP B  1 353 ? -11.190 73.337 39.768  1.00 22.73 ? 353  TRP B CE2 1 
ATOM   8590  C  CE3 . TRP B  1 353 ? -9.992  75.178 40.790  1.00 21.92 ? 353  TRP B CE3 1 
ATOM   8591  C  CZ2 . TRP B  1 353 ? -11.151 72.592 40.954  1.00 22.11 ? 353  TRP B CZ2 1 
ATOM   8592  C  CZ3 . TRP B  1 353 ? -9.952  74.443 41.964  1.00 22.01 ? 353  TRP B CZ3 1 
ATOM   8593  C  CH2 . TRP B  1 353 ? -10.528 73.162 42.040  1.00 22.83 ? 353  TRP B CH2 1 
ATOM   8594  N  N   . VAL B  1 354 ? -12.720 77.066 36.002  1.00 22.90 ? 354  VAL B N   1 
ATOM   8595  C  CA  . VAL B  1 354 ? -13.915 76.847 35.191  1.00 21.38 ? 354  VAL B CA  1 
ATOM   8596  C  C   . VAL B  1 354 ? -14.114 75.376 34.857  1.00 21.03 ? 354  VAL B C   1 
ATOM   8597  O  O   . VAL B  1 354 ? -13.242 74.763 34.237  1.00 20.12 ? 354  VAL B O   1 
ATOM   8598  C  CB  . VAL B  1 354 ? -13.827 77.639 33.873  1.00 21.43 ? 354  VAL B CB  1 
ATOM   8599  C  CG1 . VAL B  1 354 ? -15.059 77.376 33.016  1.00 20.89 ? 354  VAL B CG1 1 
ATOM   8600  C  CG2 . VAL B  1 354 ? -13.665 79.143 34.179  1.00 21.68 ? 354  VAL B CG2 1 
ATOM   8601  N  N   . GLY B  1 355 ? -15.255 74.823 35.281  1.00 19.59 ? 355  GLY B N   1 
ATOM   8602  C  CA  . GLY B  1 355 ? -15.583 73.424 35.028  1.00 18.80 ? 355  GLY B CA  1 
ATOM   8603  C  C   . GLY B  1 355 ? -14.902 72.486 36.016  1.00 18.29 ? 355  GLY B C   1 
ATOM   8604  O  O   . GLY B  1 355 ? -14.175 72.939 36.889  1.00 19.20 ? 355  GLY B O   1 
ATOM   8605  N  N   . ARG B  1 356 ? -15.141 71.186 35.902  1.00 17.24 ? 356  ARG B N   1 
ATOM   8606  C  CA  . ARG B  1 356 ? -14.490 70.228 36.792  1.00 17.44 ? 356  ARG B CA  1 
ATOM   8607  C  C   . ARG B  1 356 ? -13.016 70.081 36.393  1.00 18.03 ? 356  ARG B C   1 
ATOM   8608  O  O   . ARG B  1 356 ? -12.117 70.345 37.196  1.00 18.41 ? 356  ARG B O   1 
ATOM   8609  C  CB  . ARG B  1 356 ? -15.208 68.868 36.738  1.00 17.38 ? 356  ARG B CB  1 
ATOM   8610  C  CG  . ARG B  1 356 ? -16.596 68.912 37.381  1.00 16.72 ? 356  ARG B CG  1 
ATOM   8611  C  CD  . ARG B  1 356 ? -17.193 67.524 37.581  1.00 16.93 ? 356  ARG B CD  1 
ATOM   8612  N  NE  . ARG B  1 356 ? -18.409 67.598 38.387  1.00 17.93 ? 356  ARG B NE  1 
ATOM   8613  C  CZ  . ARG B  1 356 ? -19.651 67.454 37.920  1.00 19.47 ? 356  ARG B CZ  1 
ATOM   8614  N  NH1 . ARG B  1 356 ? -19.867 67.225 36.630  1.00 17.55 ? 356  ARG B NH1 1 
ATOM   8615  N  NH2 . ARG B  1 356 ? -20.683 67.522 38.757  1.00 18.34 ? 356  ARG B NH2 1 
ATOM   8616  N  N   . PHE B  1 357 ? -12.780 69.692 35.145  1.00 17.15 ? 357  PHE B N   1 
ATOM   8617  C  CA  . PHE B  1 357 ? -11.427 69.516 34.613  1.00 17.83 ? 357  PHE B CA  1 
ATOM   8618  C  C   . PHE B  1 357 ? -11.265 70.350 33.334  1.00 18.38 ? 357  PHE B C   1 
ATOM   8619  O  O   . PHE B  1 357 ? -10.162 70.452 32.780  1.00 17.28 ? 357  PHE B O   1 
ATOM   8620  C  CB  . PHE B  1 357 ? -11.148 68.034 34.315  1.00 17.33 ? 357  PHE B CB  1 
ATOM   8621  C  CG  . PHE B  1 357 ? -10.868 67.210 35.552  1.00 18.23 ? 357  PHE B CG  1 
ATOM   8622  C  CD1 . PHE B  1 357 ? -9.639  67.302 36.197  1.00 17.43 ? 357  PHE B CD1 1 
ATOM   8623  C  CD2 . PHE B  1 357 ? -11.847 66.383 36.097  1.00 18.41 ? 357  PHE B CD2 1 
ATOM   8624  C  CE1 . PHE B  1 357 ? -9.383  66.583 37.381  1.00 18.18 ? 357  PHE B CE1 1 
ATOM   8625  C  CE2 . PHE B  1 357 ? -11.606 65.657 37.282  1.00 19.23 ? 357  PHE B CE2 1 
ATOM   8626  C  CZ  . PHE B  1 357 ? -10.363 65.762 37.925  1.00 18.25 ? 357  PHE B CZ  1 
ATOM   8627  N  N   . ARG B  1 358 ? -12.369 70.949 32.887  1.00 17.92 ? 358  ARG B N   1 
ATOM   8628  C  CA  . ARG B  1 358 ? -12.385 71.800 31.695  1.00 18.95 ? 358  ARG B CA  1 
ATOM   8629  C  C   . ARG B  1 358 ? -13.773 72.424 31.535  1.00 19.35 ? 358  ARG B C   1 
ATOM   8630  O  O   . ARG B  1 358 ? -14.742 71.934 32.126  1.00 20.36 ? 358  ARG B O   1 
ATOM   8631  C  CB  . ARG B  1 358 ? -12.061 70.974 30.448  1.00 19.32 ? 358  ARG B CB  1 
ATOM   8632  C  CG  . ARG B  1 358 ? -12.971 69.784 30.293  1.00 23.25 ? 358  ARG B CG  1 
ATOM   8633  C  CD  . ARG B  1 358 ? -13.129 69.362 28.845  1.00 26.13 ? 358  ARG B CD  1 
ATOM   8634  N  NE  . ARG B  1 358 ? -14.210 70.095 28.187  1.00 28.01 ? 358  ARG B NE  1 
ATOM   8635  C  CZ  . ARG B  1 358 ? -14.504 69.989 26.892  1.00 28.35 ? 358  ARG B CZ  1 
ATOM   8636  N  NH1 . ARG B  1 358 ? -13.790 69.181 26.113  1.00 27.49 ? 358  ARG B NH1 1 
ATOM   8637  N  NH2 . ARG B  1 358 ? -15.517 70.682 26.380  1.00 27.65 ? 358  ARG B NH2 1 
ATOM   8638  N  N   . PRO B  1 359 ? -13.891 73.523 30.753  1.00 18.85 ? 359  PRO B N   1 
ATOM   8639  C  CA  . PRO B  1 359 ? -15.251 74.078 30.625  1.00 18.60 ? 359  PRO B CA  1 
ATOM   8640  C  C   . PRO B  1 359 ? -16.157 72.969 30.079  1.00 18.43 ? 359  PRO B C   1 
ATOM   8641  O  O   . PRO B  1 359 ? -15.722 72.162 29.263  1.00 17.66 ? 359  PRO B O   1 
ATOM   8642  C  CB  . PRO B  1 359 ? -15.077 75.243 29.648  1.00 18.88 ? 359  PRO B CB  1 
ATOM   8643  C  CG  . PRO B  1 359 ? -13.599 75.670 29.881  1.00 19.70 ? 359  PRO B CG  1 
ATOM   8644  C  CD  . PRO B  1 359 ? -12.898 74.321 30.006  1.00 17.43 ? 359  PRO B CD  1 
ATOM   8645  N  N   . SER B  1 360 ? -17.404 72.921 30.542  1.00 18.52 ? 360  SER B N   1 
ATOM   8646  C  CA  . SER B  1 360 ? -18.337 71.870 30.135  1.00 19.25 ? 360  SER B CA  1 
ATOM   8647  C  C   . SER B  1 360 ? -18.706 71.921 28.660  1.00 20.36 ? 360  SER B C   1 
ATOM   8648  O  O   . SER B  1 360 ? -18.806 73.000 28.068  1.00 20.39 ? 360  SER B O   1 
ATOM   8649  C  CB  . SER B  1 360 ? -19.619 71.924 30.993  1.00 20.63 ? 360  SER B CB  1 
ATOM   8650  O  OG  . SER B  1 360 ? -20.225 73.214 30.967  1.00 19.47 ? 360  SER B OG  1 
ATOM   8651  N  N   . GLU B  1 361 ? -18.934 70.745 28.087  1.00 20.56 ? 361  GLU B N   1 
ATOM   8652  C  CA  . GLU B  1 361 ? -19.283 70.617 26.685  1.00 22.18 ? 361  GLU B CA  1 
ATOM   8653  C  C   . GLU B  1 361 ? -20.746 70.929 26.427  1.00 21.11 ? 361  GLU B C   1 
ATOM   8654  O  O   . GLU B  1 361 ? -21.607 70.671 27.269  1.00 21.59 ? 361  GLU B O   1 
ATOM   8655  C  CB  . GLU B  1 361 ? -18.981 69.195 26.178  1.00 25.22 ? 361  GLU B CB  1 
ATOM   8656  C  CG  . GLU B  1 361 ? -19.341 68.084 27.159  1.00 31.68 ? 361  GLU B CG  1 
ATOM   8657  C  CD  . GLU B  1 361 ? -18.326 67.958 28.298  1.00 35.63 ? 361  GLU B CD  1 
ATOM   8658  O  OE1 . GLU B  1 361 ? -17.166 67.566 28.024  1.00 38.13 ? 361  GLU B OE1 1 
ATOM   8659  O  OE2 . GLU B  1 361 ? -18.678 68.260 29.467  1.00 37.03 ? 361  GLU B OE2 1 
ATOM   8660  N  N   . PRO B  1 362 ? -21.042 71.475 25.242  1.00 19.38 ? 362  PRO B N   1 
ATOM   8661  C  CA  . PRO B  1 362 ? -22.420 71.808 24.888  1.00 18.28 ? 362  PRO B CA  1 
ATOM   8662  C  C   . PRO B  1 362 ? -23.111 70.628 24.221  1.00 18.69 ? 362  PRO B C   1 
ATOM   8663  O  O   . PRO B  1 362 ? -22.471 69.829 23.521  1.00 19.10 ? 362  PRO B O   1 
ATOM   8664  C  CB  . PRO B  1 362 ? -22.245 72.980 23.934  1.00 19.06 ? 362  PRO B CB  1 
ATOM   8665  C  CG  . PRO B  1 362 ? -21.012 72.560 23.141  1.00 17.83 ? 362  PRO B CG  1 
ATOM   8666  C  CD  . PRO B  1 362 ? -20.093 71.971 24.225  1.00 19.03 ? 362  PRO B CD  1 
ATOM   8667  N  N   . HIS B  1 363 ? -24.416 70.522 24.453  1.00 18.05 ? 363  HIS B N   1 
ATOM   8668  C  CA  . HIS B  1 363 ? -25.257 69.482 23.863  1.00 18.66 ? 363  HIS B CA  1 
ATOM   8669  C  C   . HIS B  1 363 ? -26.362 70.242 23.119  1.00 19.20 ? 363  HIS B C   1 
ATOM   8670  O  O   . HIS B  1 363 ? -27.280 70.796 23.730  1.00 19.04 ? 363  HIS B O   1 
ATOM   8671  C  CB  . HIS B  1 363 ? -25.834 68.600 24.972  1.00 19.47 ? 363  HIS B CB  1 
ATOM   8672  C  CG  . HIS B  1 363 ? -24.782 67.864 25.744  1.00 19.61 ? 363  HIS B CG  1 
ATOM   8673  N  ND1 . HIS B  1 363 ? -24.416 66.567 25.451  1.00 20.58 ? 363  HIS B ND1 1 
ATOM   8674  C  CD2 . HIS B  1 363 ? -23.933 68.283 26.713  1.00 19.50 ? 363  HIS B CD2 1 
ATOM   8675  C  CE1 . HIS B  1 363 ? -23.384 66.221 26.198  1.00 20.74 ? 363  HIS B CE1 1 
ATOM   8676  N  NE2 . HIS B  1 363 ? -23.070 67.246 26.973  1.00 21.34 ? 363  HIS B NE2 1 
ATOM   8677  N  N   . PHE B  1 364 ? -26.247 70.281 21.797  1.00 18.53 ? 364  PHE B N   1 
ATOM   8678  C  CA  . PHE B  1 364 ? -27.191 70.998 20.954  1.00 19.47 ? 364  PHE B CA  1 
ATOM   8679  C  C   . PHE B  1 364 ? -28.473 70.269 20.618  1.00 20.59 ? 364  PHE B C   1 
ATOM   8680  O  O   . PHE B  1 364 ? -28.460 69.074 20.345  1.00 21.01 ? 364  PHE B O   1 
ATOM   8681  C  CB  . PHE B  1 364 ? -26.535 71.385 19.622  1.00 18.36 ? 364  PHE B CB  1 
ATOM   8682  C  CG  . PHE B  1 364 ? -25.524 72.500 19.730  1.00 16.77 ? 364  PHE B CG  1 
ATOM   8683  C  CD1 . PHE B  1 364 ? -24.198 72.223 20.065  1.00 16.52 ? 364  PHE B CD1 1 
ATOM   8684  C  CD2 . PHE B  1 364 ? -25.901 73.824 19.490  1.00 13.67 ? 364  PHE B CD2 1 
ATOM   8685  C  CE1 . PHE B  1 364 ? -23.253 73.246 20.162  1.00 15.76 ? 364  PHE B CE1 1 
ATOM   8686  C  CE2 . PHE B  1 364 ? -24.971 74.860 19.583  1.00 14.23 ? 364  PHE B CE2 1 
ATOM   8687  C  CZ  . PHE B  1 364 ? -23.640 74.573 19.921  1.00 15.34 ? 364  PHE B CZ  1 
ATOM   8688  N  N   . THR B  1 365 ? -29.588 70.991 20.639  1.00 20.56 ? 365  THR B N   1 
ATOM   8689  C  CA  . THR B  1 365 ? -30.840 70.378 20.235  1.00 22.08 ? 365  THR B CA  1 
ATOM   8690  C  C   . THR B  1 365 ? -30.656 70.216 18.722  1.00 22.44 ? 365  THR B C   1 
ATOM   8691  O  O   . THR B  1 365 ? -29.780 70.861 18.126  1.00 21.36 ? 365  THR B O   1 
ATOM   8692  C  CB  . THR B  1 365 ? -32.053 71.285 20.514  1.00 22.67 ? 365  THR B CB  1 
ATOM   8693  O  OG1 . THR B  1 365 ? -32.192 72.226 19.451  1.00 27.30 ? 365  THR B OG1 1 
ATOM   8694  C  CG2 . THR B  1 365 ? -31.861 72.042 21.814  1.00 19.69 ? 365  THR B CG2 1 
ATOM   8695  N  N   . LEU B  1 366 ? -31.472 69.360 18.119  1.00 22.78 ? 366  LEU B N   1 
ATOM   8696  C  CA  . LEU B  1 366 ? -31.393 69.051 16.695  1.00 24.16 ? 366  LEU B CA  1 
ATOM   8697  C  C   . LEU B  1 366 ? -31.278 70.234 15.726  1.00 24.07 ? 366  LEU B C   1 
ATOM   8698  O  O   . LEU B  1 366 ? -30.389 70.249 14.866  1.00 23.61 ? 366  LEU B O   1 
ATOM   8699  C  CB  . LEU B  1 366 ? -32.587 68.178 16.293  1.00 24.84 ? 366  LEU B CB  1 
ATOM   8700  C  CG  . LEU B  1 366 ? -32.668 67.705 14.830  1.00 27.03 ? 366  LEU B CG  1 
ATOM   8701  C  CD1 . LEU B  1 366 ? -31.518 66.754 14.514  1.00 26.69 ? 366  LEU B CD1 1 
ATOM   8702  C  CD2 . LEU B  1 366 ? -34.017 67.013 14.601  1.00 26.85 ? 366  LEU B CD2 1 
ATOM   8703  N  N   . ASP B  1 367 ? -32.171 71.214 15.842  1.00 23.25 ? 367  ASP B N   1 
ATOM   8704  C  CA  . ASP B  1 367 ? -32.110 72.357 14.947  1.00 22.78 ? 367  ASP B CA  1 
ATOM   8705  C  C   . ASP B  1 367 ? -30.902 73.278 15.180  1.00 21.59 ? 367  ASP B C   1 
ATOM   8706  O  O   . ASP B  1 367 ? -30.751 74.287 14.489  1.00 21.03 ? 367  ASP B O   1 
ATOM   8707  C  CB  . ASP B  1 367 ? -33.395 73.180 15.034  1.00 23.65 ? 367  ASP B CB  1 
ATOM   8708  C  CG  . ASP B  1 367 ? -33.575 73.861 16.388  1.00 26.25 ? 367  ASP B CG  1 
ATOM   8709  O  OD1 . ASP B  1 367 ? -32.616 73.889 17.202  1.00 25.07 ? 367  ASP B OD1 1 
ATOM   8710  O  OD2 . ASP B  1 367 ? -34.692 74.380 16.633  1.00 26.21 ? 367  ASP B OD2 1 
ATOM   8711  N  N   . GLY B  1 368 ? -30.050 72.942 16.146  1.00 19.40 ? 368  GLY B N   1 
ATOM   8712  C  CA  . GLY B  1 368 ? -28.880 73.773 16.425  1.00 18.30 ? 368  GLY B CA  1 
ATOM   8713  C  C   . GLY B  1 368 ? -29.157 75.189 16.928  1.00 18.75 ? 368  GLY B C   1 
ATOM   8714  O  O   . GLY B  1 368 ? -28.255 76.026 16.926  1.00 17.54 ? 368  GLY B O   1 
ATOM   8715  N  N   . ASN B  1 369 ? -30.378 75.462 17.382  1.00 17.50 ? 369  ASN B N   1 
ATOM   8716  C  CA  . ASN B  1 369 ? -30.720 76.800 17.859  1.00 18.59 ? 369  ASN B CA  1 
ATOM   8717  C  C   . ASN B  1 369 ? -30.678 76.980 19.383  1.00 18.91 ? 369  ASN B C   1 
ATOM   8718  O  O   . ASN B  1 369 ? -30.943 78.070 19.909  1.00 18.16 ? 369  ASN B O   1 
ATOM   8719  C  CB  . ASN B  1 369 ? -32.097 77.224 17.327  1.00 19.10 ? 369  ASN B CB  1 
ATOM   8720  C  CG  . ASN B  1 369 ? -32.088 77.468 15.822  1.00 22.04 ? 369  ASN B CG  1 
ATOM   8721  O  OD1 . ASN B  1 369 ? -31.091 77.955 15.265  1.00 22.20 ? 369  ASN B OD1 1 
ATOM   8722  N  ND2 . ASN B  1 369 ? -33.196 77.149 15.159  1.00 22.28 ? 369  ASN B ND2 1 
ATOM   8723  N  N   . SER B  1 370 ? -30.337 75.911 20.087  1.00 17.68 ? 370  SER B N   1 
ATOM   8724  C  CA  . SER B  1 370 ? -30.227 75.951 21.529  1.00 17.59 ? 370  SER B CA  1 
ATOM   8725  C  C   . SER B  1 370 ? -29.365 74.777 21.984  1.00 17.46 ? 370  SER B C   1 
ATOM   8726  O  O   . SER B  1 370 ? -29.173 73.816 21.240  1.00 16.86 ? 370  SER B O   1 
ATOM   8727  C  CB  . SER B  1 370 ? -31.610 75.894 22.181  1.00 17.59 ? 370  SER B CB  1 
ATOM   8728  O  OG  . SER B  1 370 ? -32.331 74.766 21.734  1.00 18.43 ? 370  SER B OG  1 
ATOM   8729  N  N   . PHE B  1 371 ? -28.821 74.869 23.189  1.00 16.15 ? 371  PHE B N   1 
ATOM   8730  C  CA  . PHE B  1 371 ? -27.981 73.796 23.708  1.00 17.01 ? 371  PHE B CA  1 
ATOM   8731  C  C   . PHE B  1 371 ? -28.022 73.744 25.236  1.00 17.08 ? 371  PHE B C   1 
ATOM   8732  O  O   . PHE B  1 371 ? -28.518 74.669 25.885  1.00 17.66 ? 371  PHE B O   1 
ATOM   8733  C  CB  . PHE B  1 371 ? -26.540 73.978 23.200  1.00 14.95 ? 371  PHE B CB  1 
ATOM   8734  C  CG  . PHE B  1 371 ? -25.875 75.246 23.669  1.00 14.86 ? 371  PHE B CG  1 
ATOM   8735  C  CD1 . PHE B  1 371 ? -25.223 75.292 24.905  1.00 15.32 ? 371  PHE B CD1 1 
ATOM   8736  C  CD2 . PHE B  1 371 ? -25.903 76.406 22.882  1.00 15.28 ? 371  PHE B CD2 1 
ATOM   8737  C  CE1 . PHE B  1 371 ? -24.613 76.472 25.356  1.00 14.91 ? 371  PHE B CE1 1 
ATOM   8738  C  CE2 . PHE B  1 371 ? -25.292 77.588 23.327  1.00 14.44 ? 371  PHE B CE2 1 
ATOM   8739  C  CZ  . PHE B  1 371 ? -24.646 77.622 24.572  1.00 15.40 ? 371  PHE B CZ  1 
ATOM   8740  N  N   . TYR B  1 372 ? -27.516 72.653 25.799  1.00 18.05 ? 372  TYR B N   1 
ATOM   8741  C  CA  . TYR B  1 372 ? -27.471 72.480 27.249  1.00 18.28 ? 372  TYR B CA  1 
ATOM   8742  C  C   . TYR B  1 372 ? -26.022 72.300 27.679  1.00 19.01 ? 372  TYR B C   1 
ATOM   8743  O  O   . TYR B  1 372 ? -25.238 71.682 26.960  1.00 19.37 ? 372  TYR B O   1 
ATOM   8744  C  CB  . TYR B  1 372 ? -28.262 71.237 27.682  1.00 18.28 ? 372  TYR B CB  1 
ATOM   8745  C  CG  . TYR B  1 372 ? -29.706 71.201 27.220  1.00 18.55 ? 372  TYR B CG  1 
ATOM   8746  C  CD1 . TYR B  1 372 ? -30.030 70.881 25.899  1.00 18.69 ? 372  TYR B CD1 1 
ATOM   8747  C  CD2 . TYR B  1 372 ? -30.745 71.496 28.100  1.00 18.94 ? 372  TYR B CD2 1 
ATOM   8748  C  CE1 . TYR B  1 372 ? -31.355 70.859 25.462  1.00 19.71 ? 372  TYR B CE1 1 
ATOM   8749  C  CE2 . TYR B  1 372 ? -32.082 71.476 27.677  1.00 19.55 ? 372  TYR B CE2 1 
ATOM   8750  C  CZ  . TYR B  1 372 ? -32.380 71.162 26.361  1.00 19.78 ? 372  TYR B CZ  1 
ATOM   8751  O  OH  . TYR B  1 372 ? -33.689 71.180 25.931  1.00 18.69 ? 372  TYR B OH  1 
ATOM   8752  N  N   . LYS B  1 373 ? -25.670 72.868 28.831  1.00 19.30 ? 373  LYS B N   1 
ATOM   8753  C  CA  . LYS B  1 373 ? -24.332 72.751 29.417  1.00 19.96 ? 373  LYS B CA  1 
ATOM   8754  C  C   . LYS B  1 373 ? -24.511 72.575 30.911  1.00 19.88 ? 373  LYS B C   1 
ATOM   8755  O  O   . LYS B  1 373 ? -25.477 73.097 31.486  1.00 20.14 ? 373  LYS B O   1 
ATOM   8756  C  CB  . LYS B  1 373 ? -23.504 74.026 29.227  1.00 19.22 ? 373  LYS B CB  1 
ATOM   8757  C  CG  . LYS B  1 373 ? -22.668 74.096 27.977  1.00 19.13 ? 373  LYS B CG  1 
ATOM   8758  C  CD  . LYS B  1 373 ? -21.795 75.342 27.999  1.00 18.02 ? 373  LYS B CD  1 
ATOM   8759  C  CE  . LYS B  1 373 ? -21.005 75.446 26.702  1.00 20.91 ? 373  LYS B CE  1 
ATOM   8760  N  NZ  . LYS B  1 373 ? -20.085 76.611 26.648  1.00 20.93 ? 373  LYS B NZ  1 
ATOM   8761  N  N   . ILE B  1 374 ? -23.595 71.845 31.536  1.00 18.90 ? 374  ILE B N   1 
ATOM   8762  C  CA  . ILE B  1 374 ? -23.644 71.685 32.973  1.00 19.78 ? 374  ILE B CA  1 
ATOM   8763  C  C   . ILE B  1 374 ? -22.892 72.904 33.496  1.00 21.44 ? 374  ILE B C   1 
ATOM   8764  O  O   . ILE B  1 374 ? -21.775 73.174 33.065  1.00 21.58 ? 374  ILE B O   1 
ATOM   8765  C  CB  . ILE B  1 374 ? -22.943 70.397 33.438  1.00 18.80 ? 374  ILE B CB  1 
ATOM   8766  C  CG1 . ILE B  1 374 ? -23.802 69.184 33.050  1.00 17.47 ? 374  ILE B CG1 1 
ATOM   8767  C  CG2 . ILE B  1 374 ? -22.691 70.466 34.945  1.00 17.46 ? 374  ILE B CG2 1 
ATOM   8768  C  CD1 . ILE B  1 374 ? -23.113 67.848 33.262  1.00 18.24 ? 374  ILE B CD1 1 
ATOM   8769  N  N   . ILE B  1 375 ? -23.504 73.659 34.400  1.00 21.39 ? 375  ILE B N   1 
ATOM   8770  C  CA  . ILE B  1 375 ? -22.852 74.843 34.936  1.00 23.30 ? 375  ILE B CA  1 
ATOM   8771  C  C   . ILE B  1 375 ? -23.151 74.941 36.421  1.00 23.63 ? 375  ILE B C   1 
ATOM   8772  O  O   . ILE B  1 375 ? -24.251 74.585 36.849  1.00 23.76 ? 375  ILE B O   1 
ATOM   8773  C  CB  . ILE B  1 375 ? -23.319 76.113 34.150  1.00 24.39 ? 375  ILE B CB  1 
ATOM   8774  C  CG1 . ILE B  1 375 ? -22.255 76.436 33.083  1.00 25.75 ? 375  ILE B CG1 1 
ATOM   8775  C  CG2 . ILE B  1 375 ? -23.465 77.328 35.078  1.00 23.87 ? 375  ILE B CG2 1 
ATOM   8776  C  CD1 . ILE B  1 375 ? -22.755 76.510 31.707  1.00 26.03 ? 375  ILE B CD1 1 
ATOM   8777  N  N   . SER B  1 376 ? -22.196 75.401 37.228  1.00 23.41 ? 376  SER B N   1 
ATOM   8778  C  CA  . SER B  1 376 ? -22.502 75.459 38.645  1.00 25.32 ? 376  SER B CA  1 
ATOM   8779  C  C   . SER B  1 376 ? -23.414 76.652 38.862  1.00 25.37 ? 376  SER B C   1 
ATOM   8780  O  O   . SER B  1 376 ? -23.182 77.742 38.324  1.00 25.66 ? 376  SER B O   1 
ATOM   8781  C  CB  . SER B  1 376 ? -21.236 75.536 39.507  1.00 26.37 ? 376  SER B CB  1 
ATOM   8782  O  OG  . SER B  1 376 ? -20.683 76.821 39.513  1.00 29.22 ? 376  SER B OG  1 
ATOM   8783  N  N   . ASN B  1 377 ? -24.475 76.428 39.626  1.00 25.70 ? 377  ASN B N   1 
ATOM   8784  C  CA  . ASN B  1 377 ? -25.455 77.473 39.880  1.00 26.61 ? 377  ASN B CA  1 
ATOM   8785  C  C   . ASN B  1 377 ? -24.994 78.447 40.960  1.00 28.33 ? 377  ASN B C   1 
ATOM   8786  O  O   . ASN B  1 377 ? -23.826 78.435 41.350  1.00 27.70 ? 377  ASN B O   1 
ATOM   8787  C  CB  . ASN B  1 377 ? -26.802 76.856 40.252  1.00 24.01 ? 377  ASN B CB  1 
ATOM   8788  C  CG  . ASN B  1 377 ? -26.746 76.044 41.514  1.00 23.84 ? 377  ASN B CG  1 
ATOM   8789  O  OD1 . ASN B  1 377 ? -25.875 76.249 42.369  1.00 22.93 ? 377  ASN B OD1 1 
ATOM   8790  N  ND2 . ASN B  1 377 ? -27.691 75.117 41.656  1.00 23.35 ? 377  ASN B ND2 1 
ATOM   8791  N  N   . GLU B  1 378 ? -25.909 79.280 41.448  1.00 30.19 ? 378  GLU B N   1 
ATOM   8792  C  CA  . GLU B  1 378 ? -25.553 80.277 42.449  1.00 33.04 ? 378  GLU B CA  1 
ATOM   8793  C  C   . GLU B  1 378 ? -25.125 79.676 43.784  1.00 32.95 ? 378  GLU B C   1 
ATOM   8794  O  O   . GLU B  1 378 ? -24.380 80.303 44.535  1.00 33.39 ? 378  GLU B O   1 
ATOM   8795  C  CB  . GLU B  1 378 ? -26.709 81.273 42.648  1.00 35.17 ? 378  GLU B CB  1 
ATOM   8796  C  CG  . GLU B  1 378 ? -27.030 82.073 41.375  1.00 40.06 ? 378  GLU B CG  1 
ATOM   8797  C  CD  . GLU B  1 378 ? -27.923 83.301 41.613  1.00 42.95 ? 378  GLU B CD  1 
ATOM   8798  O  OE1 . GLU B  1 378 ? -28.637 83.697 40.660  1.00 44.58 ? 378  GLU B OE1 1 
ATOM   8799  O  OE2 . GLU B  1 378 ? -27.911 83.880 42.733  1.00 44.55 ? 378  GLU B OE2 1 
ATOM   8800  N  N   . GLU B  1 379 ? -25.583 78.463 44.071  1.00 32.91 ? 379  GLU B N   1 
ATOM   8801  C  CA  . GLU B  1 379 ? -25.225 77.778 45.308  1.00 32.93 ? 379  GLU B CA  1 
ATOM   8802  C  C   . GLU B  1 379 ? -23.912 76.994 45.180  1.00 31.32 ? 379  GLU B C   1 
ATOM   8803  O  O   . GLU B  1 379 ? -23.430 76.431 46.157  1.00 31.43 ? 379  GLU B O   1 
ATOM   8804  C  CB  . GLU B  1 379 ? -26.319 76.787 45.705  1.00 35.71 ? 379  GLU B CB  1 
ATOM   8805  C  CG  . GLU B  1 379 ? -27.681 77.363 45.995  1.00 39.43 ? 379  GLU B CG  1 
ATOM   8806  C  CD  . GLU B  1 379 ? -28.720 76.254 46.168  1.00 43.07 ? 379  GLU B CD  1 
ATOM   8807  O  OE1 . GLU B  1 379 ? -28.482 75.330 46.995  1.00 43.82 ? 379  GLU B OE1 1 
ATOM   8808  O  OE2 . GLU B  1 379 ? -29.771 76.299 45.474  1.00 44.18 ? 379  GLU B OE2 1 
ATOM   8809  N  N   . GLY B  1 380 ? -23.350 76.922 43.978  1.00 30.31 ? 380  GLY B N   1 
ATOM   8810  C  CA  . GLY B  1 380 ? -22.114 76.176 43.797  1.00 28.66 ? 380  GLY B CA  1 
ATOM   8811  C  C   . GLY B  1 380 ? -22.280 74.713 43.371  1.00 28.10 ? 380  GLY B C   1 
ATOM   8812  O  O   . GLY B  1 380 ? -21.298 73.963 43.372  1.00 27.74 ? 380  GLY B O   1 
ATOM   8813  N  N   . TYR B  1 381 ? -23.502 74.299 43.019  1.00 26.46 ? 381  TYR B N   1 
ATOM   8814  C  CA  . TYR B  1 381 ? -23.771 72.932 42.557  1.00 24.31 ? 381  TYR B CA  1 
ATOM   8815  C  C   . TYR B  1 381 ? -23.972 72.943 41.046  1.00 24.01 ? 381  TYR B C   1 
ATOM   8816  O  O   . TYR B  1 381 ? -24.690 73.805 40.502  1.00 24.34 ? 381  TYR B O   1 
ATOM   8817  C  CB  . TYR B  1 381 ? -25.014 72.340 43.230  1.00 23.94 ? 381  TYR B CB  1 
ATOM   8818  C  CG  . TYR B  1 381 ? -24.802 72.092 44.699  1.00 23.16 ? 381  TYR B CG  1 
ATOM   8819  C  CD1 . TYR B  1 381 ? -25.010 73.110 45.634  1.00 22.93 ? 381  TYR B CD1 1 
ATOM   8820  C  CD2 . TYR B  1 381 ? -24.301 70.873 45.147  1.00 22.06 ? 381  TYR B CD2 1 
ATOM   8821  C  CE1 . TYR B  1 381 ? -24.715 72.915 46.985  1.00 22.21 ? 381  TYR B CE1 1 
ATOM   8822  C  CE2 . TYR B  1 381 ? -23.994 70.668 46.492  1.00 22.38 ? 381  TYR B CE2 1 
ATOM   8823  C  CZ  . TYR B  1 381 ? -24.202 71.698 47.399  1.00 22.38 ? 381  TYR B CZ  1 
ATOM   8824  O  OH  . TYR B  1 381 ? -23.849 71.520 48.713  1.00 24.43 ? 381  TYR B OH  1 
ATOM   8825  N  N   . ARG B  1 382 ? -23.325 71.993 40.379  1.00 22.01 ? 382  ARG B N   1 
ATOM   8826  C  CA  . ARG B  1 382 ? -23.372 71.876 38.928  1.00 21.16 ? 382  ARG B CA  1 
ATOM   8827  C  C   . ARG B  1 382 ? -24.680 71.254 38.434  1.00 20.77 ? 382  ARG B C   1 
ATOM   8828  O  O   . ARG B  1 382 ? -25.022 70.125 38.774  1.00 20.28 ? 382  ARG B O   1 
ATOM   8829  C  CB  . ARG B  1 382 ? -22.138 71.088 38.464  1.00 20.86 ? 382  ARG B CB  1 
ATOM   8830  C  CG  . ARG B  1 382 ? -20.850 71.834 38.839  1.00 19.84 ? 382  ARG B CG  1 
ATOM   8831  C  CD  . ARG B  1 382 ? -19.516 71.079 38.677  1.00 20.19 ? 382  ARG B CD  1 
ATOM   8832  N  NE  . ARG B  1 382 ? -18.496 71.938 39.270  1.00 19.74 ? 382  ARG B NE  1 
ATOM   8833  C  CZ  . ARG B  1 382 ? -17.892 72.942 38.636  1.00 20.69 ? 382  ARG B CZ  1 
ATOM   8834  N  NH1 . ARG B  1 382 ? -18.158 73.196 37.358  1.00 18.14 ? 382  ARG B NH1 1 
ATOM   8835  N  NH2 . ARG B  1 382 ? -17.125 73.788 39.322  1.00 21.01 ? 382  ARG B NH2 1 
ATOM   8836  N  N   . HIS B  1 383 ? -25.401 72.023 37.619  1.00 20.77 ? 383  HIS B N   1 
ATOM   8837  C  CA  . HIS B  1 383 ? -26.689 71.610 37.082  1.00 20.10 ? 383  HIS B CA  1 
ATOM   8838  C  C   . HIS B  1 383 ? -26.819 71.958 35.601  1.00 20.85 ? 383  HIS B C   1 
ATOM   8839  O  O   . HIS B  1 383 ? -26.052 72.772 35.074  1.00 20.51 ? 383  HIS B O   1 
ATOM   8840  C  CB  . HIS B  1 383 ? -27.796 72.291 37.874  1.00 19.82 ? 383  HIS B CB  1 
ATOM   8841  C  CG  . HIS B  1 383 ? -28.006 71.690 39.226  1.00 21.02 ? 383  HIS B CG  1 
ATOM   8842  N  ND1 . HIS B  1 383 ? -28.683 70.503 39.413  1.00 20.21 ? 383  HIS B ND1 1 
ATOM   8843  C  CD2 . HIS B  1 383 ? -27.571 72.076 40.448  1.00 19.82 ? 383  HIS B CD2 1 
ATOM   8844  C  CE1 . HIS B  1 383 ? -28.656 70.183 40.693  1.00 21.28 ? 383  HIS B CE1 1 
ATOM   8845  N  NE2 . HIS B  1 383 ? -27.987 71.120 41.342  1.00 22.80 ? 383  HIS B NE2 1 
ATOM   8846  N  N   . ILE B  1 384 ? -27.792 71.344 34.939  1.00 19.55 ? 384  ILE B N   1 
ATOM   8847  C  CA  . ILE B  1 384 ? -27.999 71.582 33.526  1.00 19.59 ? 384  ILE B CA  1 
ATOM   8848  C  C   . ILE B  1 384 ? -28.640 72.930 33.272  1.00 20.38 ? 384  ILE B C   1 
ATOM   8849  O  O   . ILE B  1 384 ? -29.661 73.266 33.878  1.00 20.75 ? 384  ILE B O   1 
ATOM   8850  C  CB  . ILE B  1 384 ? -28.867 70.484 32.928  1.00 19.50 ? 384  ILE B CB  1 
ATOM   8851  C  CG1 . ILE B  1 384 ? -28.145 69.141 33.086  1.00 18.44 ? 384  ILE B CG1 1 
ATOM   8852  C  CG2 . ILE B  1 384 ? -29.176 70.800 31.461  1.00 18.30 ? 384  ILE B CG2 1 
ATOM   8853  C  CD1 . ILE B  1 384 ? -29.059 67.944 33.002  1.00 18.68 ? 384  ILE B CD1 1 
ATOM   8854  N  N   . CYS B  1 385 ? -28.029 73.708 32.384  1.00 20.62 ? 385  CYS B N   1 
ATOM   8855  C  CA  . CYS B  1 385 ? -28.553 75.027 32.041  1.00 21.39 ? 385  CYS B CA  1 
ATOM   8856  C  C   . CYS B  1 385 ? -28.860 74.999 30.546  1.00 20.77 ? 385  CYS B C   1 
ATOM   8857  O  O   . CYS B  1 385 ? -28.060 74.513 29.735  1.00 19.90 ? 385  CYS B O   1 
ATOM   8858  C  CB  . CYS B  1 385 ? -27.534 76.131 32.382  1.00 22.49 ? 385  CYS B CB  1 
ATOM   8859  S  SG  . CYS B  1 385 ? -28.323 77.689 32.953  1.00 26.44 ? 385  CYS B SG  1 
ATOM   8860  N  N   . TYR B  1 386 ? -30.044 75.493 30.199  1.00 19.82 ? 386  TYR B N   1 
ATOM   8861  C  CA  . TYR B  1 386 ? -30.514 75.515 28.828  1.00 20.02 ? 386  TYR B CA  1 
ATOM   8862  C  C   . TYR B  1 386 ? -30.283 76.900 28.217  1.00 20.71 ? 386  TYR B C   1 
ATOM   8863  O  O   . TYR B  1 386 ? -30.783 77.901 28.737  1.00 19.44 ? 386  TYR B O   1 
ATOM   8864  C  CB  . TYR B  1 386 ? -32.005 75.164 28.814  1.00 20.53 ? 386  TYR B CB  1 
ATOM   8865  C  CG  . TYR B  1 386 ? -32.653 75.143 27.440  1.00 21.30 ? 386  TYR B CG  1 
ATOM   8866  C  CD1 . TYR B  1 386 ? -32.102 74.401 26.403  1.00 21.07 ? 386  TYR B CD1 1 
ATOM   8867  C  CD2 . TYR B  1 386 ? -33.846 75.830 27.197  1.00 22.95 ? 386  TYR B CD2 1 
ATOM   8868  C  CE1 . TYR B  1 386 ? -32.716 74.332 25.153  1.00 23.64 ? 386  TYR B CE1 1 
ATOM   8869  C  CE2 . TYR B  1 386 ? -34.470 75.773 25.939  1.00 23.98 ? 386  TYR B CE2 1 
ATOM   8870  C  CZ  . TYR B  1 386 ? -33.896 75.022 24.930  1.00 23.14 ? 386  TYR B CZ  1 
ATOM   8871  O  OH  . TYR B  1 386 ? -34.493 74.952 23.699  1.00 25.60 ? 386  TYR B OH  1 
ATOM   8872  N  N   . PHE B  1 387 ? -29.526 76.937 27.120  1.00 20.42 ? 387  PHE B N   1 
ATOM   8873  C  CA  . PHE B  1 387 ? -29.178 78.173 26.402  1.00 20.34 ? 387  PHE B CA  1 
ATOM   8874  C  C   . PHE B  1 387 ? -29.836 78.289 25.019  1.00 21.08 ? 387  PHE B C   1 
ATOM   8875  O  O   . PHE B  1 387 ? -29.992 77.286 24.300  1.00 20.77 ? 387  PHE B O   1 
ATOM   8876  C  CB  . PHE B  1 387 ? -27.676 78.240 26.095  1.00 19.23 ? 387  PHE B CB  1 
ATOM   8877  C  CG  . PHE B  1 387 ? -26.781 78.341 27.290  1.00 18.43 ? 387  PHE B CG  1 
ATOM   8878  C  CD1 . PHE B  1 387 ? -26.116 79.527 27.556  1.00 17.62 ? 387  PHE B CD1 1 
ATOM   8879  C  CD2 . PHE B  1 387 ? -26.529 77.234 28.097  1.00 17.93 ? 387  PHE B CD2 1 
ATOM   8880  C  CE1 . PHE B  1 387 ? -25.202 79.620 28.608  1.00 19.55 ? 387  PHE B CE1 1 
ATOM   8881  C  CE2 . PHE B  1 387 ? -25.613 77.318 29.155  1.00 18.53 ? 387  PHE B CE2 1 
ATOM   8882  C  CZ  . PHE B  1 387 ? -24.952 78.512 29.407  1.00 18.87 ? 387  PHE B CZ  1 
ATOM   8883  N  N   . GLN B  1 388 ? -30.187 79.521 24.651  1.00 19.97 ? 388  GLN B N   1 
ATOM   8884  C  CA  . GLN B  1 388 ? -30.716 79.841 23.324  1.00 21.23 ? 388  GLN B CA  1 
ATOM   8885  C  C   . GLN B  1 388 ? -29.397 80.332 22.699  1.00 20.12 ? 388  GLN B C   1 
ATOM   8886  O  O   . GLN B  1 388 ? -28.680 81.086 23.358  1.00 18.47 ? 388  GLN B O   1 
ATOM   8887  C  CB  . GLN B  1 388 ? -31.716 80.990 23.440  1.00 25.37 ? 388  GLN B CB  1 
ATOM   8888  C  CG  . GLN B  1 388 ? -33.075 80.727 22.841  1.00 29.83 ? 388  GLN B CG  1 
ATOM   8889  C  CD  . GLN B  1 388 ? -33.559 79.314 23.043  1.00 31.84 ? 388  GLN B CD  1 
ATOM   8890  O  OE1 . GLN B  1 388 ? -33.616 78.802 24.166  1.00 35.02 ? 388  GLN B OE1 1 
ATOM   8891  N  NE2 . GLN B  1 388 ? -33.915 78.666 21.947  1.00 34.21 ? 388  GLN B NE2 1 
ATOM   8892  N  N   . ILE B  1 389 ? -29.060 79.949 21.460  1.00 19.45 ? 389  ILE B N   1 
ATOM   8893  C  CA  . ILE B  1 389 ? -27.758 80.352 20.929  1.00 19.34 ? 389  ILE B CA  1 
ATOM   8894  C  C   . ILE B  1 389 ? -27.468 81.836 20.883  1.00 20.58 ? 389  ILE B C   1 
ATOM   8895  O  O   . ILE B  1 389 ? -26.303 82.226 20.918  1.00 19.58 ? 389  ILE B O   1 
ATOM   8896  C  CB  . ILE B  1 389 ? -27.431 79.778 19.507  1.00 19.76 ? 389  ILE B CB  1 
ATOM   8897  C  CG1 . ILE B  1 389 ? -28.484 80.210 18.488  1.00 19.70 ? 389  ILE B CG1 1 
ATOM   8898  C  CG2 . ILE B  1 389 ? -27.216 78.258 19.580  1.00 17.86 ? 389  ILE B CG2 1 
ATOM   8899  C  CD1 . ILE B  1 389 ? -28.106 79.816 17.064  1.00 18.79 ? 389  ILE B CD1 1 
ATOM   8900  N  N   . ASP B  1 390 ? -28.505 82.668 20.807  1.00 20.76 ? 390  ASP B N   1 
ATOM   8901  C  CA  . ASP B  1 390 ? -28.270 84.107 20.755  1.00 22.20 ? 390  ASP B CA  1 
ATOM   8902  C  C   . ASP B  1 390 ? -28.714 84.894 21.991  1.00 23.28 ? 390  ASP B C   1 
ATOM   8903  O  O   . ASP B  1 390 ? -28.961 86.103 21.902  1.00 24.36 ? 390  ASP B O   1 
ATOM   8904  C  CB  . ASP B  1 390 ? -28.905 84.708 19.492  1.00 22.12 ? 390  ASP B CB  1 
ATOM   8905  C  CG  . ASP B  1 390 ? -30.411 84.516 19.441  1.00 23.43 ? 390  ASP B CG  1 
ATOM   8906  O  OD1 . ASP B  1 390 ? -30.989 83.892 20.354  1.00 23.17 ? 390  ASP B OD1 1 
ATOM   8907  O  OD2 . ASP B  1 390 ? -31.025 84.984 18.472  1.00 24.95 ? 390  ASP B OD2 1 
ATOM   8908  N  N   . LYS B  1 391 ? -28.828 84.208 23.129  1.00 22.84 ? 391  LYS B N   1 
ATOM   8909  C  CA  . LYS B  1 391 ? -29.176 84.852 24.392  1.00 24.46 ? 391  LYS B CA  1 
ATOM   8910  C  C   . LYS B  1 391 ? -28.092 84.452 25.391  1.00 24.35 ? 391  LYS B C   1 
ATOM   8911  O  O   . LYS B  1 391 ? -27.757 83.272 25.511  1.00 23.68 ? 391  LYS B O   1 
ATOM   8912  C  CB  . LYS B  1 391 ? -30.554 84.410 24.892  1.00 25.66 ? 391  LYS B CB  1 
ATOM   8913  C  CG  . LYS B  1 391 ? -31.722 84.942 24.049  1.00 29.06 ? 391  LYS B CG  1 
ATOM   8914  C  CD  . LYS B  1 391 ? -33.060 84.344 24.494  1.00 32.13 ? 391  LYS B CD  1 
ATOM   8915  C  CE  . LYS B  1 391 ? -34.232 84.876 23.650  1.00 34.73 ? 391  LYS B CE  1 
ATOM   8916  N  NZ  . LYS B  1 391 ? -35.503 84.122 23.942  1.00 36.56 ? 391  LYS B NZ  1 
ATOM   8917  N  N   . LYS B  1 392 ? -27.531 85.422 26.103  1.00 23.84 ? 392  LYS B N   1 
ATOM   8918  C  CA  . LYS B  1 392 ? -26.453 85.107 27.037  1.00 26.17 ? 392  LYS B CA  1 
ATOM   8919  C  C   . LYS B  1 392 ? -26.865 84.439 28.345  1.00 26.44 ? 392  LYS B C   1 
ATOM   8920  O  O   . LYS B  1 392 ? -26.071 83.713 28.932  1.00 26.97 ? 392  LYS B O   1 
ATOM   8921  C  CB  . LYS B  1 392 ? -25.617 86.368 27.336  1.00 24.70 ? 392  LYS B CB  1 
ATOM   8922  C  CG  . LYS B  1 392 ? -25.081 87.061 26.068  1.00 26.32 ? 392  LYS B CG  1 
ATOM   8923  C  CD  . LYS B  1 392 ? -24.672 86.035 25.008  1.00 25.50 ? 392  LYS B CD  1 
ATOM   8924  C  CE  . LYS B  1 392 ? -24.310 86.707 23.684  1.00 26.02 ? 392  LYS B CE  1 
ATOM   8925  N  NZ  . LYS B  1 392 ? -23.085 87.536 23.805  1.00 25.51 ? 392  LYS B NZ  1 
ATOM   8926  N  N   . ASP B  1 393 ? -28.088 84.686 28.802  1.00 26.83 ? 393  ASP B N   1 
ATOM   8927  C  CA  . ASP B  1 393 ? -28.566 84.103 30.057  1.00 27.48 ? 393  ASP B CA  1 
ATOM   8928  C  C   . ASP B  1 393 ? -29.235 82.759 29.831  1.00 26.96 ? 393  ASP B C   1 
ATOM   8929  O  O   . ASP B  1 393 ? -30.166 82.653 29.038  1.00 27.41 ? 393  ASP B O   1 
ATOM   8930  C  CB  . ASP B  1 393 ? -29.564 85.050 30.732  1.00 29.91 ? 393  ASP B CB  1 
ATOM   8931  C  CG  . ASP B  1 393 ? -28.961 86.403 31.027  1.00 32.77 ? 393  ASP B CG  1 
ATOM   8932  O  OD1 . ASP B  1 393 ? -27.866 86.446 31.629  1.00 34.08 ? 393  ASP B OD1 1 
ATOM   8933  O  OD2 . ASP B  1 393 ? -29.574 87.427 30.658  1.00 35.73 ? 393  ASP B OD2 1 
ATOM   8934  N  N   . CYS B  1 394 ? -28.767 81.736 30.530  1.00 25.84 ? 394  CYS B N   1 
ATOM   8935  C  CA  . CYS B  1 394 ? -29.356 80.424 30.376  1.00 25.32 ? 394  CYS B CA  1 
ATOM   8936  C  C   . CYS B  1 394 ? -30.380 80.170 31.469  1.00 24.72 ? 394  CYS B C   1 
ATOM   8937  O  O   . CYS B  1 394 ? -30.499 80.948 32.416  1.00 24.56 ? 394  CYS B O   1 
ATOM   8938  C  CB  . CYS B  1 394 ? -28.275 79.336 30.402  1.00 25.33 ? 394  CYS B CB  1 
ATOM   8939  S  SG  . CYS B  1 394 ? -27.347 79.184 31.960  1.00 26.61 ? 394  CYS B SG  1 
ATOM   8940  N  N   . THR B  1 395 ? -31.129 79.084 31.322  1.00 23.79 ? 395  THR B N   1 
ATOM   8941  C  CA  . THR B  1 395 ? -32.151 78.704 32.299  1.00 23.25 ? 395  THR B CA  1 
ATOM   8942  C  C   . THR B  1 395 ? -31.815 77.337 32.901  1.00 22.23 ? 395  THR B C   1 
ATOM   8943  O  O   . THR B  1 395 ? -31.700 76.335 32.186  1.00 21.06 ? 395  THR B O   1 
ATOM   8944  C  CB  . THR B  1 395 ? -33.557 78.619 31.637  1.00 23.94 ? 395  THR B CB  1 
ATOM   8945  O  OG1 . THR B  1 395 ? -33.917 79.907 31.108  1.00 24.97 ? 395  THR B OG1 1 
ATOM   8946  C  CG2 . THR B  1 395 ? -34.612 78.167 32.666  1.00 23.76 ? 395  THR B CG2 1 
ATOM   8947  N  N   . PHE B  1 396 ? -31.665 77.289 34.215  1.00 21.55 ? 396  PHE B N   1 
ATOM   8948  C  CA  . PHE B  1 396 ? -31.367 76.024 34.876  1.00 21.87 ? 396  PHE B CA  1 
ATOM   8949  C  C   . PHE B  1 396 ? -32.593 75.134 34.847  1.00 21.67 ? 396  PHE B C   1 
ATOM   8950  O  O   . PHE B  1 396 ? -33.691 75.571 35.173  1.00 21.86 ? 396  PHE B O   1 
ATOM   8951  C  CB  . PHE B  1 396 ? -30.927 76.281 36.313  1.00 22.54 ? 396  PHE B CB  1 
ATOM   8952  C  CG  . PHE B  1 396 ? -29.487 76.683 36.431  1.00 23.84 ? 396  PHE B CG  1 
ATOM   8953  C  CD1 . PHE B  1 396 ? -28.470 75.753 36.205  1.00 24.56 ? 396  PHE B CD1 1 
ATOM   8954  C  CD2 . PHE B  1 396 ? -29.142 77.992 36.742  1.00 23.32 ? 396  PHE B CD2 1 
ATOM   8955  C  CE1 . PHE B  1 396 ? -27.121 76.129 36.290  1.00 23.78 ? 396  PHE B CE1 1 
ATOM   8956  C  CE2 . PHE B  1 396 ? -27.806 78.379 36.828  1.00 23.90 ? 396  PHE B CE2 1 
ATOM   8957  C  CZ  . PHE B  1 396 ? -26.790 77.446 36.602  1.00 24.76 ? 396  PHE B CZ  1 
ATOM   8958  N  N   . ILE B  1 397 ? -32.426 73.894 34.417  1.00 21.16 ? 397  ILE B N   1 
ATOM   8959  C  CA  . ILE B  1 397 ? -33.557 72.999 34.381  1.00 20.31 ? 397  ILE B CA  1 
ATOM   8960  C  C   . ILE B  1 397 ? -33.494 71.973 35.496  1.00 19.98 ? 397  ILE B C   1 
ATOM   8961  O  O   . ILE B  1 397 ? -34.444 71.211 35.682  1.00 19.05 ? 397  ILE B O   1 
ATOM   8962  C  CB  . ILE B  1 397 ? -33.704 72.311 33.016  1.00 20.09 ? 397  ILE B CB  1 
ATOM   8963  C  CG1 . ILE B  1 397 ? -32.629 71.246 32.829  1.00 19.53 ? 397  ILE B CG1 1 
ATOM   8964  C  CG2 . ILE B  1 397 ? -33.595 73.359 31.915  1.00 19.82 ? 397  ILE B CG2 1 
ATOM   8965  C  CD1 . ILE B  1 397 ? -32.777 70.510 31.534  1.00 17.60 ? 397  ILE B CD1 1 
ATOM   8966  N  N   . THR B  1 398 ? -32.375 71.932 36.219  1.00 19.75 ? 398  THR B N   1 
ATOM   8967  C  CA  . THR B  1 398 ? -32.251 71.051 37.379  1.00 20.64 ? 398  THR B CA  1 
ATOM   8968  C  C   . THR B  1 398 ? -31.667 71.915 38.493  1.00 21.25 ? 398  THR B C   1 
ATOM   8969  O  O   . THR B  1 398 ? -31.068 72.951 38.222  1.00 21.42 ? 398  THR B O   1 
ATOM   8970  C  CB  . THR B  1 398 ? -31.311 69.814 37.140  1.00 21.21 ? 398  THR B CB  1 
ATOM   8971  O  OG1 . THR B  1 398 ? -29.977 70.245 36.824  1.00 20.61 ? 398  THR B OG1 1 
ATOM   8972  C  CG2 . THR B  1 398 ? -31.852 68.947 36.029  1.00 19.60 ? 398  THR B CG2 1 
ATOM   8973  N  N   . LYS B  1 399 ? -31.855 71.503 39.742  1.00 22.34 ? 399  LYS B N   1 
ATOM   8974  C  CA  . LYS B  1 399 ? -31.327 72.243 40.888  1.00 24.08 ? 399  LYS B CA  1 
ATOM   8975  C  C   . LYS B  1 399 ? -31.422 71.336 42.110  1.00 23.89 ? 399  LYS B C   1 
ATOM   8976  O  O   . LYS B  1 399 ? -32.165 70.357 42.096  1.00 23.66 ? 399  LYS B O   1 
ATOM   8977  C  CB  . LYS B  1 399 ? -32.142 73.516 41.142  1.00 25.77 ? 399  LYS B CB  1 
ATOM   8978  C  CG  . LYS B  1 399 ? -33.594 73.229 41.541  1.00 30.89 ? 399  LYS B CG  1 
ATOM   8979  C  CD  . LYS B  1 399 ? -34.375 74.514 41.875  1.00 33.74 ? 399  LYS B CD  1 
ATOM   8980  C  CE  . LYS B  1 399 ? -35.833 74.179 42.221  1.00 35.97 ? 399  LYS B CE  1 
ATOM   8981  N  NZ  . LYS B  1 399 ? -36.700 75.387 42.360  1.00 38.20 ? 399  LYS B NZ  1 
ATOM   8982  N  N   . GLY B  1 400 ? -30.677 71.662 43.157  1.00 23.59 ? 400  GLY B N   1 
ATOM   8983  C  CA  . GLY B  1 400 ? -30.698 70.855 44.369  1.00 24.35 ? 400  GLY B CA  1 
ATOM   8984  C  C   . GLY B  1 400 ? -29.299 70.752 44.960  1.00 24.82 ? 400  GLY B C   1 
ATOM   8985  O  O   . GLY B  1 400 ? -28.320 71.134 44.301  1.00 24.43 ? 400  GLY B O   1 
ATOM   8986  N  N   . THR B  1 401 ? -29.180 70.253 46.186  1.00 23.62 ? 401  THR B N   1 
ATOM   8987  C  CA  . THR B  1 401 ? -27.853 70.130 46.785  1.00 23.87 ? 401  THR B CA  1 
ATOM   8988  C  C   . THR B  1 401 ? -27.280 68.777 46.386  1.00 23.36 ? 401  THR B C   1 
ATOM   8989  O  O   . THR B  1 401 ? -27.230 67.832 47.175  1.00 23.43 ? 401  THR B O   1 
ATOM   8990  C  CB  . THR B  1 401 ? -27.906 70.273 48.335  1.00 24.78 ? 401  THR B CB  1 
ATOM   8991  O  OG1 . THR B  1 401 ? -28.770 69.274 48.885  1.00 28.12 ? 401  THR B OG1 1 
ATOM   8992  C  CG2 . THR B  1 401 ? -28.441 71.629 48.716  1.00 24.36 ? 401  THR B CG2 1 
ATOM   8993  N  N   . TRP B  1 402 ? -26.890 68.699 45.119  1.00 21.86 ? 402  TRP B N   1 
ATOM   8994  C  CA  . TRP B  1 402 ? -26.314 67.499 44.510  1.00 20.16 ? 402  TRP B CA  1 
ATOM   8995  C  C   . TRP B  1 402 ? -25.908 67.950 43.116  1.00 18.98 ? 402  TRP B C   1 
ATOM   8996  O  O   . TRP B  1 402 ? -26.232 69.071 42.727  1.00 19.17 ? 402  TRP B O   1 
ATOM   8997  C  CB  . TRP B  1 402 ? -27.343 66.363 44.428  1.00 19.32 ? 402  TRP B CB  1 
ATOM   8998  C  CG  . TRP B  1 402 ? -28.680 66.741 43.837  1.00 18.75 ? 402  TRP B CG  1 
ATOM   8999  C  CD1 . TRP B  1 402 ? -29.799 67.158 44.521  1.00 19.64 ? 402  TRP B CD1 1 
ATOM   9000  C  CD2 . TRP B  1 402 ? -29.045 66.733 42.446  1.00 19.32 ? 402  TRP B CD2 1 
ATOM   9001  N  NE1 . TRP B  1 402 ? -30.827 67.408 43.638  1.00 18.95 ? 402  TRP B NE1 1 
ATOM   9002  C  CE2 . TRP B  1 402 ? -30.392 67.159 42.362  1.00 19.33 ? 402  TRP B CE2 1 
ATOM   9003  C  CE3 . TRP B  1 402 ? -28.363 66.408 41.261  1.00 19.70 ? 402  TRP B CE3 1 
ATOM   9004  C  CZ2 . TRP B  1 402 ? -31.069 67.268 41.141  1.00 19.02 ? 402  TRP B CZ2 1 
ATOM   9005  C  CZ3 . TRP B  1 402 ? -29.036 66.514 40.051  1.00 18.83 ? 402  TRP B CZ3 1 
ATOM   9006  C  CH2 . TRP B  1 402 ? -30.376 66.942 40.001  1.00 19.01 ? 402  TRP B CH2 1 
ATOM   9007  N  N   . GLU B  1 403 ? -25.224 67.101 42.360  1.00 17.96 ? 403  GLU B N   1 
ATOM   9008  C  CA  . GLU B  1 403 ? -24.772 67.521 41.039  1.00 17.85 ? 403  GLU B CA  1 
ATOM   9009  C  C   . GLU B  1 403 ? -25.031 66.579 39.879  1.00 16.66 ? 403  GLU B C   1 
ATOM   9010  O  O   . GLU B  1 403 ? -25.083 65.368 40.038  1.00 15.23 ? 403  GLU B O   1 
ATOM   9011  C  CB  . GLU B  1 403 ? -23.256 67.801 41.062  1.00 18.17 ? 403  GLU B CB  1 
ATOM   9012  C  CG  . GLU B  1 403 ? -22.817 68.787 42.104  1.00 19.15 ? 403  GLU B CG  1 
ATOM   9013  C  CD  . GLU B  1 403 ? -21.445 69.345 41.817  1.00 19.94 ? 403  GLU B CD  1 
ATOM   9014  O  OE1 . GLU B  1 403 ? -20.527 68.547 41.518  1.00 19.03 ? 403  GLU B OE1 1 
ATOM   9015  O  OE2 . GLU B  1 403 ? -21.291 70.586 41.889  1.00 20.10 ? 403  GLU B OE2 1 
ATOM   9016  N  N   . VAL B  1 404 ? -25.149 67.169 38.694  1.00 17.41 ? 404  VAL B N   1 
ATOM   9017  C  CA  . VAL B  1 404 ? -25.326 66.422 37.456  1.00 16.86 ? 404  VAL B CA  1 
ATOM   9018  C  C   . VAL B  1 404 ? -23.894 66.007 37.080  1.00 18.17 ? 404  VAL B C   1 
ATOM   9019  O  O   . VAL B  1 404 ? -22.971 66.836 37.095  1.00 17.75 ? 404  VAL B O   1 
ATOM   9020  C  CB  . VAL B  1 404 ? -25.921 67.324 36.340  1.00 17.07 ? 404  VAL B CB  1 
ATOM   9021  C  CG1 . VAL B  1 404 ? -25.884 66.595 35.017  1.00 17.06 ? 404  VAL B CG1 1 
ATOM   9022  C  CG2 . VAL B  1 404 ? -27.386 67.724 36.684  1.00 15.51 ? 404  VAL B CG2 1 
ATOM   9023  N  N   . ILE B  1 405 ? -23.709 64.728 36.776  1.00 17.46 ? 405  ILE B N   1 
ATOM   9024  C  CA  . ILE B  1 405 ? -22.398 64.199 36.421  1.00 17.06 ? 405  ILE B CA  1 
ATOM   9025  C  C   . ILE B  1 405 ? -22.155 64.345 34.912  1.00 17.46 ? 405  ILE B C   1 
ATOM   9026  O  O   . ILE B  1 405 ? -21.060 64.703 34.488  1.00 17.76 ? 405  ILE B O   1 
ATOM   9027  C  CB  . ILE B  1 405 ? -22.291 62.718 36.779  1.00 16.55 ? 405  ILE B CB  1 
ATOM   9028  C  CG1 . ILE B  1 405 ? -22.612 62.515 38.267  1.00 16.79 ? 405  ILE B CG1 1 
ATOM   9029  C  CG2 . ILE B  1 405 ? -20.868 62.210 36.416  1.00 16.56 ? 405  ILE B CG2 1 
ATOM   9030  C  CD1 . ILE B  1 405 ? -21.654 63.218 39.202  1.00 17.31 ? 405  ILE B CD1 1 
ATOM   9031  N  N   . GLY B  1 406 ? -23.176 64.050 34.115  1.00 16.12 ? 406  GLY B N   1 
ATOM   9032  C  CA  . GLY B  1 406 ? -23.043 64.190 32.679  1.00 17.18 ? 406  GLY B CA  1 
ATOM   9033  C  C   . GLY B  1 406 ? -24.385 64.131 31.959  1.00 17.98 ? 406  GLY B C   1 
ATOM   9034  O  O   . GLY B  1 406 ? -25.373 63.613 32.496  1.00 18.56 ? 406  GLY B O   1 
ATOM   9035  N  N   . ILE B  1 407 ? -24.431 64.691 30.757  1.00 17.16 ? 407  ILE B N   1 
ATOM   9036  C  CA  . ILE B  1 407 ? -25.645 64.650 29.937  1.00 18.16 ? 407  ILE B CA  1 
ATOM   9037  C  C   . ILE B  1 407 ? -25.359 63.468 29.012  1.00 18.14 ? 407  ILE B C   1 
ATOM   9038  O  O   . ILE B  1 407 ? -24.332 63.457 28.350  1.00 18.33 ? 407  ILE B O   1 
ATOM   9039  C  CB  . ILE B  1 407 ? -25.815 65.959 29.114  1.00 17.47 ? 407  ILE B CB  1 
ATOM   9040  C  CG1 . ILE B  1 407 ? -26.160 67.113 30.058  1.00 18.11 ? 407  ILE B CG1 1 
ATOM   9041  C  CG2 . ILE B  1 407 ? -26.927 65.787 28.078  1.00 16.98 ? 407  ILE B CG2 1 
ATOM   9042  C  CD1 . ILE B  1 407 ? -26.118 68.501 29.402  1.00 18.76 ? 407  ILE B CD1 1 
ATOM   9043  N  N   . GLU B  1 408 ? -26.260 62.489 28.962  1.00 18.36 ? 408  GLU B N   1 
ATOM   9044  C  CA  . GLU B  1 408 ? -26.050 61.277 28.163  1.00 18.61 ? 408  GLU B CA  1 
ATOM   9045  C  C   . GLU B  1 408 ? -26.732 61.184 26.808  1.00 18.82 ? 408  GLU B C   1 
ATOM   9046  O  O   . GLU B  1 408 ? -26.235 60.509 25.906  1.00 19.47 ? 408  GLU B O   1 
ATOM   9047  C  CB  . GLU B  1 408 ? -26.452 60.038 28.973  1.00 17.33 ? 408  GLU B CB  1 
ATOM   9048  C  CG  . GLU B  1 408 ? -25.788 59.935 30.329  1.00 18.55 ? 408  GLU B CG  1 
ATOM   9049  C  CD  . GLU B  1 408 ? -24.268 60.056 30.268  1.00 20.20 ? 408  GLU B CD  1 
ATOM   9050  O  OE1 . GLU B  1 408 ? -23.734 61.023 30.835  1.00 23.30 ? 408  GLU B OE1 1 
ATOM   9051  O  OE2 . GLU B  1 408 ? -23.605 59.192 29.668  1.00 20.37 ? 408  GLU B OE2 1 
ATOM   9052  N  N   . ALA B  1 409 ? -27.886 61.814 26.670  1.00 17.89 ? 409  ALA B N   1 
ATOM   9053  C  CA  . ALA B  1 409 ? -28.597 61.771 25.403  1.00 18.09 ? 409  ALA B CA  1 
ATOM   9054  C  C   . ALA B  1 409 ? -29.642 62.865 25.403  1.00 18.02 ? 409  ALA B C   1 
ATOM   9055  O  O   . ALA B  1 409 ? -30.047 63.353 26.465  1.00 16.90 ? 409  ALA B O   1 
ATOM   9056  C  CB  . ALA B  1 409 ? -29.251 60.420 25.210  1.00 17.79 ? 409  ALA B CB  1 
ATOM   9057  N  N   . LEU B  1 410 ? -30.063 63.253 24.204  1.00 17.81 ? 410  LEU B N   1 
ATOM   9058  C  CA  . LEU B  1 410 ? -31.045 64.307 24.040  1.00 17.11 ? 410  LEU B CA  1 
ATOM   9059  C  C   . LEU B  1 410 ? -31.943 63.966 22.874  1.00 17.51 ? 410  LEU B C   1 
ATOM   9060  O  O   . LEU B  1 410 ? -31.454 63.745 21.776  1.00 17.57 ? 410  LEU B O   1 
ATOM   9061  C  CB  . LEU B  1 410 ? -30.337 65.627 23.748  1.00 16.45 ? 410  LEU B CB  1 
ATOM   9062  C  CG  . LEU B  1 410 ? -31.245 66.815 23.449  1.00 15.66 ? 410  LEU B CG  1 
ATOM   9063  C  CD1 . LEU B  1 410 ? -31.988 67.166 24.742  1.00 16.95 ? 410  LEU B CD1 1 
ATOM   9064  C  CD2 . LEU B  1 410 ? -30.434 68.015 22.977  1.00 15.93 ? 410  LEU B CD2 1 
ATOM   9065  N  N   . THR B  1 411 ? -33.245 63.891 23.118  1.00 18.56 ? 411  THR B N   1 
ATOM   9066  C  CA  . THR B  1 411 ? -34.208 63.620 22.055  1.00 19.55 ? 411  THR B CA  1 
ATOM   9067  C  C   . THR B  1 411 ? -35.125 64.829 21.978  1.00 20.41 ? 411  THR B C   1 
ATOM   9068  O  O   . THR B  1 411 ? -34.986 65.765 22.770  1.00 20.20 ? 411  THR B O   1 
ATOM   9069  C  CB  . THR B  1 411 ? -35.069 62.383 22.351  1.00 19.76 ? 411  THR B CB  1 
ATOM   9070  O  OG1 . THR B  1 411 ? -35.905 62.650 23.489  1.00 19.17 ? 411  THR B OG1 1 
ATOM   9071  C  CG2 . THR B  1 411 ? -34.169 61.175 22.603  1.00 19.99 ? 411  THR B CG2 1 
ATOM   9072  N  N   . SER B  1 412 ? -36.070 64.823 21.043  1.00 21.08 ? 412  SER B N   1 
ATOM   9073  C  CA  . SER B  1 412 ? -36.966 65.966 20.938  1.00 22.35 ? 412  SER B CA  1 
ATOM   9074  C  C   . SER B  1 412 ? -37.809 66.140 22.203  1.00 22.44 ? 412  SER B C   1 
ATOM   9075  O  O   . SER B  1 412 ? -38.184 67.257 22.541  1.00 23.18 ? 412  SER B O   1 
ATOM   9076  C  CB  . SER B  1 412 ? -37.876 65.818 19.714  1.00 22.87 ? 412  SER B CB  1 
ATOM   9077  O  OG  . SER B  1 412 ? -38.568 64.588 19.765  1.00 24.40 ? 412  SER B OG  1 
ATOM   9078  N  N   . ASP B  1 413 ? -38.089 65.049 22.912  1.00 22.68 ? 413  ASP B N   1 
ATOM   9079  C  CA  . ASP B  1 413 ? -38.904 65.135 24.124  1.00 23.23 ? 413  ASP B CA  1 
ATOM   9080  C  C   . ASP B  1 413 ? -38.213 64.989 25.479  1.00 23.08 ? 413  ASP B C   1 
ATOM   9081  O  O   . ASP B  1 413 ? -38.744 65.453 26.489  1.00 23.29 ? 413  ASP B O   1 
ATOM   9082  C  CB  . ASP B  1 413 ? -40.044 64.116 24.068  1.00 24.87 ? 413  ASP B CB  1 
ATOM   9083  C  CG  . ASP B  1 413 ? -41.005 64.385 22.929  1.00 27.53 ? 413  ASP B CG  1 
ATOM   9084  O  OD1 . ASP B  1 413 ? -41.174 65.565 22.545  1.00 28.78 ? 413  ASP B OD1 1 
ATOM   9085  O  OD2 . ASP B  1 413 ? -41.600 63.412 22.427  1.00 29.59 ? 413  ASP B OD2 1 
ATOM   9086  N  N   . TYR B  1 414 ? -37.043 64.353 25.516  1.00 22.29 ? 414  TYR B N   1 
ATOM   9087  C  CA  . TYR B  1 414 ? -36.352 64.135 26.787  1.00 21.62 ? 414  TYR B CA  1 
ATOM   9088  C  C   . TYR B  1 414 ? -34.847 64.339 26.781  1.00 20.12 ? 414  TYR B C   1 
ATOM   9089  O  O   . TYR B  1 414 ? -34.195 64.117 25.759  1.00 19.63 ? 414  TYR B O   1 
ATOM   9090  C  CB  . TYR B  1 414 ? -36.597 62.695 27.262  1.00 22.42 ? 414  TYR B CB  1 
ATOM   9091  C  CG  . TYR B  1 414 ? -38.030 62.397 27.626  1.00 24.47 ? 414  TYR B CG  1 
ATOM   9092  C  CD1 . TYR B  1 414 ? -38.906 61.795 26.716  1.00 24.32 ? 414  TYR B CD1 1 
ATOM   9093  C  CD2 . TYR B  1 414 ? -38.518 62.753 28.880  1.00 25.45 ? 414  TYR B CD2 1 
ATOM   9094  C  CE1 . TYR B  1 414 ? -40.251 61.562 27.063  1.00 26.44 ? 414  TYR B CE1 1 
ATOM   9095  C  CE2 . TYR B  1 414 ? -39.839 62.526 29.237  1.00 26.60 ? 414  TYR B CE2 1 
ATOM   9096  C  CZ  . TYR B  1 414 ? -40.704 61.937 28.335  1.00 27.67 ? 414  TYR B CZ  1 
ATOM   9097  O  OH  . TYR B  1 414 ? -42.019 61.761 28.719  1.00 30.29 ? 414  TYR B OH  1 
ATOM   9098  N  N   . LEU B  1 415 ? -34.300 64.743 27.927  1.00 19.18 ? 415  LEU B N   1 
ATOM   9099  C  CA  . LEU B  1 415 ? -32.839 64.854 28.084  1.00 17.79 ? 415  LEU B CA  1 
ATOM   9100  C  C   . LEU B  1 415 ? -32.539 63.838 29.191  1.00 17.78 ? 415  LEU B C   1 
ATOM   9101  O  O   . LEU B  1 415 ? -33.232 63.811 30.217  1.00 17.71 ? 415  LEU B O   1 
ATOM   9102  C  CB  . LEU B  1 415 ? -32.401 66.261 28.518  1.00 16.42 ? 415  LEU B CB  1 
ATOM   9103  C  CG  . LEU B  1 415 ? -30.890 66.442 28.771  1.00 16.48 ? 415  LEU B CG  1 
ATOM   9104  C  CD1 . LEU B  1 415 ? -30.502 67.905 28.649  1.00 15.20 ? 415  LEU B CD1 1 
ATOM   9105  C  CD2 . LEU B  1 415 ? -30.527 65.892 30.159  1.00 15.50 ? 415  LEU B CD2 1 
ATOM   9106  N  N   . TYR B  1 416 ? -31.538 62.987 28.958  1.00 18.03 ? 416  TYR B N   1 
ATOM   9107  C  CA  . TYR B  1 416 ? -31.128 61.940 29.898  1.00 16.39 ? 416  TYR B CA  1 
ATOM   9108  C  C   . TYR B  1 416 ? -29.784 62.322 30.496  1.00 17.52 ? 416  TYR B C   1 
ATOM   9109  O  O   . TYR B  1 416 ? -28.871 62.716 29.762  1.00 16.67 ? 416  TYR B O   1 
ATOM   9110  C  CB  . TYR B  1 416 ? -30.989 60.593 29.168  1.00 16.90 ? 416  TYR B CB  1 
ATOM   9111  C  CG  . TYR B  1 416 ? -32.272 60.082 28.510  1.00 16.90 ? 416  TYR B CG  1 
ATOM   9112  C  CD1 . TYR B  1 416 ? -32.692 60.577 27.278  1.00 16.60 ? 416  TYR B CD1 1 
ATOM   9113  C  CD2 . TYR B  1 416 ? -33.038 59.079 29.108  1.00 16.56 ? 416  TYR B CD2 1 
ATOM   9114  C  CE1 . TYR B  1 416 ? -33.839 60.081 26.644  1.00 17.57 ? 416  TYR B CE1 1 
ATOM   9115  C  CE2 . TYR B  1 416 ? -34.188 58.574 28.489  1.00 17.72 ? 416  TYR B CE2 1 
ATOM   9116  C  CZ  . TYR B  1 416 ? -34.582 59.080 27.252  1.00 18.50 ? 416  TYR B CZ  1 
ATOM   9117  O  OH  . TYR B  1 416 ? -35.699 58.578 26.620  1.00 18.11 ? 416  TYR B OH  1 
ATOM   9118  N  N   . TYR B  1 417 ? -29.662 62.218 31.816  1.00 17.20 ? 417  TYR B N   1 
ATOM   9119  C  CA  . TYR B  1 417 ? -28.420 62.576 32.481  1.00 17.50 ? 417  TYR B CA  1 
ATOM   9120  C  C   . TYR B  1 417 ? -28.126 61.671 33.685  1.00 17.08 ? 417  TYR B C   1 
ATOM   9121  O  O   . TYR B  1 417 ? -29.003 60.973 34.179  1.00 15.88 ? 417  TYR B O   1 
ATOM   9122  C  CB  . TYR B  1 417 ? -28.489 64.042 32.918  1.00 18.48 ? 417  TYR B CB  1 
ATOM   9123  C  CG  . TYR B  1 417 ? -29.491 64.327 34.014  1.00 19.87 ? 417  TYR B CG  1 
ATOM   9124  C  CD1 . TYR B  1 417 ? -29.140 64.194 35.360  1.00 19.57 ? 417  TYR B CD1 1 
ATOM   9125  C  CD2 . TYR B  1 417 ? -30.794 64.725 33.708  1.00 19.08 ? 417  TYR B CD2 1 
ATOM   9126  C  CE1 . TYR B  1 417 ? -30.064 64.458 36.381  1.00 19.23 ? 417  TYR B CE1 1 
ATOM   9127  C  CE2 . TYR B  1 417 ? -31.722 64.987 34.718  1.00 19.32 ? 417  TYR B CE2 1 
ATOM   9128  C  CZ  . TYR B  1 417 ? -31.352 64.853 36.054  1.00 20.80 ? 417  TYR B CZ  1 
ATOM   9129  O  OH  . TYR B  1 417 ? -32.277 65.130 37.050  1.00 19.68 ? 417  TYR B OH  1 
ATOM   9130  N  N   . ILE B  1 418 ? -26.876 61.670 34.130  1.00 16.48 ? 418  ILE B N   1 
ATOM   9131  C  CA  . ILE B  1 418 ? -26.483 60.877 35.276  1.00 16.78 ? 418  ILE B CA  1 
ATOM   9132  C  C   . ILE B  1 418 ? -26.258 61.875 36.396  1.00 16.91 ? 418  ILE B C   1 
ATOM   9133  O  O   . ILE B  1 418 ? -25.699 62.941 36.159  1.00 17.40 ? 418  ILE B O   1 
ATOM   9134  C  CB  . ILE B  1 418 ? -25.120 60.128 35.042  1.00 17.54 ? 418  ILE B CB  1 
ATOM   9135  C  CG1 . ILE B  1 418 ? -25.221 59.147 33.871  1.00 18.23 ? 418  ILE B CG1 1 
ATOM   9136  C  CG2 . ILE B  1 418 ? -24.707 59.415 36.315  1.00 17.14 ? 418  ILE B CG2 1 
ATOM   9137  C  CD1 . ILE B  1 418 ? -25.982 57.901 34.190  1.00 20.28 ? 418  ILE B CD1 1 
ATOM   9138  N  N   . SER B  1 419 ? -26.684 61.559 37.616  1.00 17.20 ? 419  SER B N   1 
ATOM   9139  C  CA  . SER B  1 419 ? -26.438 62.483 38.716  1.00 16.59 ? 419  SER B CA  1 
ATOM   9140  C  C   . SER B  1 419 ? -26.287 61.711 40.014  1.00 17.29 ? 419  SER B C   1 
ATOM   9141  O  O   . SER B  1 419 ? -26.528 60.498 40.049  1.00 15.56 ? 419  SER B O   1 
ATOM   9142  C  CB  . SER B  1 419 ? -27.578 63.490 38.854  1.00 17.27 ? 419  SER B CB  1 
ATOM   9143  O  OG  . SER B  1 419 ? -28.624 62.938 39.642  1.00 19.42 ? 419  SER B OG  1 
ATOM   9144  N  N   . ASN B  1 420 ? -25.856 62.399 41.073  1.00 16.47 ? 420  ASN B N   1 
ATOM   9145  C  CA  . ASN B  1 420 ? -25.727 61.728 42.368  1.00 18.01 ? 420  ASN B CA  1 
ATOM   9146  C  C   . ASN B  1 420 ? -26.829 62.215 43.298  1.00 17.96 ? 420  ASN B C   1 
ATOM   9147  O  O   . ASN B  1 420 ? -26.646 62.300 44.509  1.00 17.61 ? 420  ASN B O   1 
ATOM   9148  C  CB  . ASN B  1 420 ? -24.341 61.962 42.998  1.00 18.27 ? 420  ASN B CB  1 
ATOM   9149  C  CG  . ASN B  1 420 ? -23.984 63.427 43.118  1.00 18.85 ? 420  ASN B CG  1 
ATOM   9150  O  OD1 . ASN B  1 420 ? -24.841 64.299 42.991  1.00 19.29 ? 420  ASN B OD1 1 
ATOM   9151  N  ND2 . ASN B  1 420 ? -22.710 63.705 43.388  1.00 20.65 ? 420  ASN B ND2 1 
ATOM   9152  N  N   . GLU B  1 421 ? -27.987 62.540 42.725  1.00 17.84 ? 421  GLU B N   1 
ATOM   9153  C  CA  . GLU B  1 421 ? -29.089 63.001 43.557  1.00 19.49 ? 421  GLU B CA  1 
ATOM   9154  C  C   . GLU B  1 421 ? -29.609 61.924 44.504  1.00 20.07 ? 421  GLU B C   1 
ATOM   9155  O  O   . GLU B  1 421 ? -29.871 62.203 45.668  1.00 20.47 ? 421  GLU B O   1 
ATOM   9156  C  CB  . GLU B  1 421 ? -30.284 63.497 42.720  1.00 19.06 ? 421  GLU B CB  1 
ATOM   9157  C  CG  . GLU B  1 421 ? -31.468 63.921 43.589  1.00 17.96 ? 421  GLU B CG  1 
ATOM   9158  C  CD  . GLU B  1 421 ? -32.651 64.507 42.790  1.00 20.42 ? 421  GLU B CD  1 
ATOM   9159  O  OE1 . GLU B  1 421 ? -32.617 64.511 41.535  1.00 20.30 ? 421  GLU B OE1 1 
ATOM   9160  O  OE2 . GLU B  1 421 ? -33.626 64.962 43.433  1.00 21.84 ? 421  GLU B OE2 1 
ATOM   9161  N  N   . TYR B  1 422 ? -29.751 60.702 44.005  1.00 21.68 ? 422  TYR B N   1 
ATOM   9162  C  CA  . TYR B  1 422 ? -30.320 59.624 44.804  1.00 22.55 ? 422  TYR B CA  1 
ATOM   9163  C  C   . TYR B  1 422 ? -29.797 59.504 46.229  1.00 23.71 ? 422  TYR B C   1 
ATOM   9164  O  O   . TYR B  1 422 ? -28.591 59.349 46.465  1.00 23.46 ? 422  TYR B O   1 
ATOM   9165  C  CB  . TYR B  1 422 ? -30.181 58.281 44.082  1.00 23.60 ? 422  TYR B CB  1 
ATOM   9166  C  CG  . TYR B  1 422 ? -31.079 57.187 44.648  1.00 26.00 ? 422  TYR B CG  1 
ATOM   9167  C  CD1 . TYR B  1 422 ? -32.466 57.361 44.713  1.00 26.98 ? 422  TYR B CD1 1 
ATOM   9168  C  CD2 . TYR B  1 422 ? -30.547 55.974 45.104  1.00 26.09 ? 422  TYR B CD2 1 
ATOM   9169  C  CE1 . TYR B  1 422 ? -33.306 56.355 45.208  1.00 27.00 ? 422  TYR B CE1 1 
ATOM   9170  C  CE2 . TYR B  1 422 ? -31.386 54.954 45.610  1.00 26.76 ? 422  TYR B CE2 1 
ATOM   9171  C  CZ  . TYR B  1 422 ? -32.757 55.158 45.651  1.00 26.76 ? 422  TYR B CZ  1 
ATOM   9172  O  OH  . TYR B  1 422 ? -33.586 54.158 46.109  1.00 27.53 ? 422  TYR B OH  1 
ATOM   9173  N  N   . LYS B  1 423 ? -30.730 59.587 47.177  1.00 23.48 ? 423  LYS B N   1 
ATOM   9174  C  CA  . LYS B  1 423 ? -30.423 59.488 48.597  1.00 23.18 ? 423  LYS B CA  1 
ATOM   9175  C  C   . LYS B  1 423 ? -29.276 60.388 49.040  1.00 22.25 ? 423  LYS B C   1 
ATOM   9176  O  O   . LYS B  1 423 ? -28.605 60.092 50.014  1.00 21.70 ? 423  LYS B O   1 
ATOM   9177  C  CB  . LYS B  1 423 ? -30.101 58.036 48.946  1.00 24.79 ? 423  LYS B CB  1 
ATOM   9178  C  CG  . LYS B  1 423 ? -31.319 57.106 48.941  1.00 28.38 ? 423  LYS B CG  1 
ATOM   9179  C  CD  . LYS B  1 423 ? -30.886 55.656 49.169  1.00 30.75 ? 423  LYS B CD  1 
ATOM   9180  C  CE  . LYS B  1 423 ? -32.043 54.666 48.961  1.00 33.13 ? 423  LYS B CE  1 
ATOM   9181  N  NZ  . LYS B  1 423 ? -33.280 55.037 49.721  1.00 33.89 ? 423  LYS B NZ  1 
ATOM   9182  N  N   . GLY B  1 424 ? -29.053 61.486 48.329  1.00 22.39 ? 424  GLY B N   1 
ATOM   9183  C  CA  . GLY B  1 424 ? -27.967 62.387 48.691  1.00 21.40 ? 424  GLY B CA  1 
ATOM   9184  C  C   . GLY B  1 424 ? -26.600 61.733 48.859  1.00 21.68 ? 424  GLY B C   1 
ATOM   9185  O  O   . GLY B  1 424 ? -25.808 62.168 49.692  1.00 21.52 ? 424  GLY B O   1 
ATOM   9186  N  N   . MET B  1 425 ? -26.310 60.687 48.085  1.00 21.46 ? 425  MET B N   1 
ATOM   9187  C  CA  . MET B  1 425 ? -25.006 60.011 48.171  1.00 22.18 ? 425  MET B CA  1 
ATOM   9188  C  C   . MET B  1 425 ? -24.137 60.515 47.021  1.00 21.66 ? 425  MET B C   1 
ATOM   9189  O  O   . MET B  1 425 ? -24.310 60.097 45.874  1.00 21.57 ? 425  MET B O   1 
ATOM   9190  C  CB  . MET B  1 425 ? -25.189 58.500 48.074  1.00 22.75 ? 425  MET B CB  1 
ATOM   9191  C  CG  . MET B  1 425 ? -25.888 57.901 49.272  1.00 26.45 ? 425  MET B CG  1 
ATOM   9192  S  SD  . MET B  1 425 ? -26.322 56.180 48.974  1.00 30.15 ? 425  MET B SD  1 
ATOM   9193  C  CE  . MET B  1 425 ? -24.702 55.447 48.977  1.00 27.52 ? 425  MET B CE  1 
ATOM   9194  N  N   . PRO B  1 426 ? -23.185 61.417 47.317  1.00 21.97 ? 426  PRO B N   1 
ATOM   9195  C  CA  . PRO B  1 426 ? -22.328 61.959 46.258  1.00 20.74 ? 426  PRO B CA  1 
ATOM   9196  C  C   . PRO B  1 426 ? -21.514 60.915 45.520  1.00 20.80 ? 426  PRO B C   1 
ATOM   9197  O  O   . PRO B  1 426 ? -21.078 61.144 44.391  1.00 19.31 ? 426  PRO B O   1 
ATOM   9198  C  CB  . PRO B  1 426 ? -21.472 63.001 46.990  1.00 21.51 ? 426  PRO B CB  1 
ATOM   9199  C  CG  . PRO B  1 426 ? -21.437 62.503 48.407  1.00 23.35 ? 426  PRO B CG  1 
ATOM   9200  C  CD  . PRO B  1 426 ? -22.836 61.987 48.635  1.00 22.19 ? 426  PRO B CD  1 
ATOM   9201  N  N   . GLY B  1 427 ? -21.344 59.760 46.154  1.00 20.04 ? 427  GLY B N   1 
ATOM   9202  C  CA  . GLY B  1 427 ? -20.596 58.676 45.552  1.00 19.92 ? 427  GLY B CA  1 
ATOM   9203  C  C   . GLY B  1 427 ? -21.445 57.669 44.787  1.00 20.81 ? 427  GLY B C   1 
ATOM   9204  O  O   . GLY B  1 427 ? -20.937 56.615 44.399  1.00 21.51 ? 427  GLY B O   1 
ATOM   9205  N  N   . GLY B  1 428 ? -22.726 57.979 44.579  1.00 19.91 ? 428  GLY B N   1 
ATOM   9206  C  CA  . GLY B  1 428 ? -23.608 57.092 43.834  1.00 19.25 ? 428  GLY B CA  1 
ATOM   9207  C  C   . GLY B  1 428 ? -23.907 57.733 42.484  1.00 19.60 ? 428  GLY B C   1 
ATOM   9208  O  O   . GLY B  1 428 ? -23.687 58.935 42.324  1.00 18.49 ? 428  GLY B O   1 
ATOM   9209  N  N   . ARG B  1 429 ? -24.395 56.952 41.518  1.00 18.97 ? 429  ARG B N   1 
ATOM   9210  C  CA  . ARG B  1 429 ? -24.688 57.474 40.171  1.00 19.28 ? 429  ARG B CA  1 
ATOM   9211  C  C   . ARG B  1 429 ? -25.932 56.832 39.581  1.00 18.48 ? 429  ARG B C   1 
ATOM   9212  O  O   . ARG B  1 429 ? -26.018 55.606 39.504  1.00 18.45 ? 429  ARG B O   1 
ATOM   9213  C  CB  . ARG B  1 429 ? -23.533 57.174 39.204  1.00 18.60 ? 429  ARG B CB  1 
ATOM   9214  C  CG  . ARG B  1 429 ? -22.144 57.673 39.609  1.00 21.42 ? 429  ARG B CG  1 
ATOM   9215  C  CD  . ARG B  1 429 ? -21.925 59.108 39.186  1.00 22.21 ? 429  ARG B CD  1 
ATOM   9216  N  NE  . ARG B  1 429 ? -20.580 59.601 39.466  1.00 23.35 ? 429  ARG B NE  1 
ATOM   9217  C  CZ  . ARG B  1 429 ? -20.114 59.953 40.666  1.00 26.03 ? 429  ARG B CZ  1 
ATOM   9218  N  NH1 . ARG B  1 429 ? -20.876 59.864 41.754  1.00 25.61 ? 429  ARG B NH1 1 
ATOM   9219  N  NH2 . ARG B  1 429 ? -18.883 60.453 40.770  1.00 25.27 ? 429  ARG B NH2 1 
ATOM   9220  N  N   . ASN B  1 430 ? -26.895 57.644 39.155  1.00 19.12 ? 430  ASN B N   1 
ATOM   9221  C  CA  . ASN B  1 430 ? -28.082 57.073 38.529  1.00 18.03 ? 430  ASN B CA  1 
ATOM   9222  C  C   . ASN B  1 430 ? -28.490 57.831 37.283  1.00 18.24 ? 430  ASN B C   1 
ATOM   9223  O  O   . ASN B  1 430 ? -28.171 59.015 37.128  1.00 18.78 ? 430  ASN B O   1 
ATOM   9224  C  CB  . ASN B  1 430 ? -29.256 57.033 39.512  1.00 17.75 ? 430  ASN B CB  1 
ATOM   9225  C  CG  . ASN B  1 430 ? -29.186 55.839 40.437  1.00 17.49 ? 430  ASN B CG  1 
ATOM   9226  O  OD1 . ASN B  1 430 ? -29.509 54.714 40.046  1.00 16.72 ? 430  ASN B OD1 1 
ATOM   9227  N  ND2 . ASN B  1 430 ? -28.744 56.075 41.663  1.00 16.10 ? 430  ASN B ND2 1 
ATOM   9228  N  N   . LEU B  1 431 ? -29.214 57.137 36.410  1.00 17.26 ? 431  LEU B N   1 
ATOM   9229  C  CA  . LEU B  1 431 ? -29.709 57.702 35.170  1.00 17.81 ? 431  LEU B CA  1 
ATOM   9230  C  C   . LEU B  1 431 ? -31.087 58.349 35.364  1.00 19.06 ? 431  LEU B C   1 
ATOM   9231  O  O   . LEU B  1 431 ? -31.993 57.741 35.951  1.00 18.93 ? 431  LEU B O   1 
ATOM   9232  C  CB  . LEU B  1 431 ? -29.821 56.611 34.106  1.00 16.64 ? 431  LEU B CB  1 
ATOM   9233  C  CG  . LEU B  1 431 ? -30.424 57.072 32.774  1.00 17.51 ? 431  LEU B CG  1 
ATOM   9234  C  CD1 . LEU B  1 431 ? -29.491 58.090 32.118  1.00 15.50 ? 431  LEU B CD1 1 
ATOM   9235  C  CD2 . LEU B  1 431 ? -30.625 55.865 31.853  1.00 18.36 ? 431  LEU B CD2 1 
ATOM   9236  N  N   . TYR B  1 432 ? -31.250 59.574 34.873  1.00 18.65 ? 432  TYR B N   1 
ATOM   9237  C  CA  . TYR B  1 432 ? -32.532 60.267 34.989  1.00 19.95 ? 432  TYR B CA  1 
ATOM   9238  C  C   . TYR B  1 432 ? -32.971 60.766 33.624  1.00 20.60 ? 432  TYR B C   1 
ATOM   9239  O  O   . TYR B  1 432 ? -32.158 60.929 32.710  1.00 19.69 ? 432  TYR B O   1 
ATOM   9240  C  CB  . TYR B  1 432 ? -32.462 61.463 35.951  1.00 19.68 ? 432  TYR B CB  1 
ATOM   9241  C  CG  . TYR B  1 432 ? -32.173 61.096 37.392  1.00 19.29 ? 432  TYR B CG  1 
ATOM   9242  C  CD1 . TYR B  1 432 ? -30.894 60.741 37.792  1.00 19.09 ? 432  TYR B CD1 1 
ATOM   9243  C  CD2 . TYR B  1 432 ? -33.180 61.127 38.360  1.00 20.27 ? 432  TYR B CD2 1 
ATOM   9244  C  CE1 . TYR B  1 432 ? -30.610 60.430 39.131  1.00 20.33 ? 432  TYR B CE1 1 
ATOM   9245  C  CE2 . TYR B  1 432 ? -32.913 60.820 39.703  1.00 19.87 ? 432  TYR B CE2 1 
ATOM   9246  C  CZ  . TYR B  1 432 ? -31.622 60.478 40.076  1.00 19.95 ? 432  TYR B CZ  1 
ATOM   9247  O  OH  . TYR B  1 432 ? -31.324 60.224 41.389  1.00 20.26 ? 432  TYR B OH  1 
ATOM   9248  N  N   . LYS B  1 433 ? -34.267 61.015 33.514  1.00 20.54 ? 433  LYS B N   1 
ATOM   9249  C  CA  . LYS B  1 433 ? -34.889 61.478 32.290  1.00 21.42 ? 433  LYS B CA  1 
ATOM   9250  C  C   . LYS B  1 433 ? -35.736 62.686 32.669  1.00 21.70 ? 433  LYS B C   1 
ATOM   9251  O  O   . LYS B  1 433 ? -36.529 62.616 33.601  1.00 22.70 ? 433  LYS B O   1 
ATOM   9252  C  CB  . LYS B  1 433 ? -35.772 60.353 31.728  1.00 22.50 ? 433  LYS B CB  1 
ATOM   9253  C  CG  . LYS B  1 433 ? -36.809 60.798 30.729  1.00 23.74 ? 433  LYS B CG  1 
ATOM   9254  C  CD  . LYS B  1 433 ? -37.307 59.684 29.830  1.00 24.90 ? 433  LYS B CD  1 
ATOM   9255  C  CE  . LYS B  1 433 ? -38.623 59.098 30.312  1.00 26.81 ? 433  LYS B CE  1 
ATOM   9256  N  NZ  . LYS B  1 433 ? -39.299 58.312 29.224  1.00 23.89 ? 433  LYS B NZ  1 
ATOM   9257  N  N   . ILE B  1 434 ? -35.569 63.799 31.971  1.00 21.96 ? 434  ILE B N   1 
ATOM   9258  C  CA  . ILE B  1 434 ? -36.374 64.966 32.296  1.00 22.46 ? 434  ILE B CA  1 
ATOM   9259  C  C   . ILE B  1 434 ? -37.196 65.388 31.080  1.00 22.68 ? 434  ILE B C   1 
ATOM   9260  O  O   . ILE B  1 434 ? -36.673 65.497 29.970  1.00 21.86 ? 434  ILE B O   1 
ATOM   9261  C  CB  . ILE B  1 434 ? -35.509 66.149 32.837  1.00 22.77 ? 434  ILE B CB  1 
ATOM   9262  C  CG1 . ILE B  1 434 ? -36.401 67.377 33.048  1.00 23.14 ? 434  ILE B CG1 1 
ATOM   9263  C  CG2 . ILE B  1 434 ? -34.351 66.471 31.888  1.00 24.13 ? 434  ILE B CG2 1 
ATOM   9264  C  CD1 . ILE B  1 434 ? -35.717 68.498 33.804  1.00 24.20 ? 434  ILE B CD1 1 
ATOM   9265  N  N   . GLN B  1 435 ? -38.493 65.593 31.298  1.00 21.55 ? 435  GLN B N   1 
ATOM   9266  C  CA  . GLN B  1 435 ? -39.389 65.977 30.216  1.00 23.17 ? 435  GLN B CA  1 
ATOM   9267  C  C   . GLN B  1 435 ? -39.101 67.427 29.830  1.00 21.79 ? 435  GLN B C   1 
ATOM   9268  O  O   . GLN B  1 435 ? -39.235 68.338 30.652  1.00 21.13 ? 435  GLN B O   1 
ATOM   9269  C  CB  . GLN B  1 435 ? -40.860 65.797 30.649  1.00 24.58 ? 435  GLN B CB  1 
ATOM   9270  C  CG  . GLN B  1 435 ? -41.853 65.878 29.495  1.00 28.18 ? 435  GLN B CG  1 
ATOM   9271  C  CD  . GLN B  1 435 ? -43.303 65.661 29.931  1.00 30.32 ? 435  GLN B CD  1 
ATOM   9272  O  OE1 . GLN B  1 435 ? -44.223 66.207 29.331  1.00 33.68 ? 435  GLN B OE1 1 
ATOM   9273  N  NE2 . GLN B  1 435 ? -43.504 64.866 30.968  1.00 30.38 ? 435  GLN B NE2 1 
ATOM   9274  N  N   . LEU B  1 436 ? -38.705 67.637 28.576  1.00 21.78 ? 436  LEU B N   1 
ATOM   9275  C  CA  . LEU B  1 436 ? -38.356 68.977 28.111  1.00 21.88 ? 436  LEU B CA  1 
ATOM   9276  C  C   . LEU B  1 436 ? -39.540 69.951 28.113  1.00 23.64 ? 436  LEU B C   1 
ATOM   9277  O  O   . LEU B  1 436 ? -39.348 71.146 28.300  1.00 23.61 ? 436  LEU B O   1 
ATOM   9278  C  CB  . LEU B  1 436 ? -37.721 68.916 26.715  1.00 20.50 ? 436  LEU B CB  1 
ATOM   9279  C  CG  . LEU B  1 436 ? -36.383 68.167 26.631  1.00 20.71 ? 436  LEU B CG  1 
ATOM   9280  C  CD1 . LEU B  1 436 ? -35.830 68.221 25.198  1.00 20.68 ? 436  LEU B CD1 1 
ATOM   9281  C  CD2 . LEU B  1 436 ? -35.404 68.771 27.606  1.00 20.26 ? 436  LEU B CD2 1 
ATOM   9282  N  N   . SER B  1 437 ? -40.757 69.449 27.923  1.00 24.27 ? 437  SER B N   1 
ATOM   9283  C  CA  . SER B  1 437 ? -41.935 70.324 27.921  1.00 26.45 ? 437  SER B CA  1 
ATOM   9284  C  C   . SER B  1 437 ? -42.504 70.582 29.327  1.00 26.86 ? 437  SER B C   1 
ATOM   9285  O  O   . SER B  1 437 ? -43.461 71.336 29.481  1.00 27.74 ? 437  SER B O   1 
ATOM   9286  C  CB  . SER B  1 437 ? -43.027 69.726 27.030  1.00 25.92 ? 437  SER B CB  1 
ATOM   9287  O  OG  . SER B  1 437 ? -43.435 68.457 27.519  1.00 27.71 ? 437  SER B OG  1 
ATOM   9288  N  N   . ASP B  1 438 ? -41.907 69.965 30.346  1.00 27.28 ? 438  ASP B N   1 
ATOM   9289  C  CA  . ASP B  1 438 ? -42.349 70.126 31.737  1.00 27.62 ? 438  ASP B CA  1 
ATOM   9290  C  C   . ASP B  1 438 ? -41.196 69.663 32.637  1.00 26.98 ? 438  ASP B C   1 
ATOM   9291  O  O   . ASP B  1 438 ? -41.092 68.472 32.975  1.00 26.07 ? 438  ASP B O   1 
ATOM   9292  C  CB  . ASP B  1 438 ? -43.601 69.266 31.985  1.00 29.06 ? 438  ASP B CB  1 
ATOM   9293  C  CG  . ASP B  1 438 ? -44.227 69.491 33.371  1.00 30.93 ? 438  ASP B CG  1 
ATOM   9294  O  OD1 . ASP B  1 438 ? -43.611 70.170 34.225  1.00 32.35 ? 438  ASP B OD1 1 
ATOM   9295  O  OD2 . ASP B  1 438 ? -45.343 68.968 33.606  1.00 32.09 ? 438  ASP B OD2 1 
ATOM   9296  N  N   . TYR B  1 439 ? -40.336 70.609 33.020  1.00 26.33 ? 439  TYR B N   1 
ATOM   9297  C  CA  . TYR B  1 439 ? -39.171 70.307 33.844  1.00 27.11 ? 439  TYR B CA  1 
ATOM   9298  C  C   . TYR B  1 439 ? -39.481 69.680 35.192  1.00 27.28 ? 439  TYR B C   1 
ATOM   9299  O  O   . TYR B  1 439 ? -38.575 69.133 35.831  1.00 26.20 ? 439  TYR B O   1 
ATOM   9300  C  CB  . TYR B  1 439 ? -38.312 71.558 34.093  1.00 26.83 ? 439  TYR B CB  1 
ATOM   9301  C  CG  . TYR B  1 439 ? -37.722 72.179 32.848  1.00 27.60 ? 439  TYR B CG  1 
ATOM   9302  C  CD1 . TYR B  1 439 ? -37.451 71.406 31.720  1.00 27.00 ? 439  TYR B CD1 1 
ATOM   9303  C  CD2 . TYR B  1 439 ? -37.438 73.547 32.796  1.00 27.32 ? 439  TYR B CD2 1 
ATOM   9304  C  CE1 . TYR B  1 439 ? -36.916 71.979 30.566  1.00 27.23 ? 439  TYR B CE1 1 
ATOM   9305  C  CE2 . TYR B  1 439 ? -36.903 74.129 31.644  1.00 27.14 ? 439  TYR B CE2 1 
ATOM   9306  C  CZ  . TYR B  1 439 ? -36.648 73.336 30.534  1.00 27.20 ? 439  TYR B CZ  1 
ATOM   9307  O  OH  . TYR B  1 439 ? -36.130 73.904 29.394  1.00 27.23 ? 439  TYR B OH  1 
ATOM   9308  N  N   . THR B  1 440 ? -40.738 69.767 35.632  1.00 26.84 ? 440  THR B N   1 
ATOM   9309  C  CA  . THR B  1 440 ? -41.114 69.202 36.928  1.00 26.07 ? 440  THR B CA  1 
ATOM   9310  C  C   . THR B  1 440 ? -41.284 67.705 36.775  1.00 25.47 ? 440  THR B C   1 
ATOM   9311  O  O   . THR B  1 440 ? -41.494 67.001 37.753  1.00 26.11 ? 440  THR B O   1 
ATOM   9312  C  CB  . THR B  1 440 ? -42.456 69.797 37.471  1.00 25.75 ? 440  THR B CB  1 
ATOM   9313  O  OG1 . THR B  1 440 ? -43.562 69.152 36.830  1.00 25.03 ? 440  THR B OG1 1 
ATOM   9314  C  CG2 . THR B  1 440 ? -42.531 71.274 37.190  1.00 26.44 ? 440  THR B CG2 1 
ATOM   9315  N  N   . LYS B  1 441 ? -41.219 67.210 35.544  1.00 24.15 ? 441  LYS B N   1 
ATOM   9316  C  CA  . LYS B  1 441 ? -41.351 65.773 35.351  1.00 22.77 ? 441  LYS B CA  1 
ATOM   9317  C  C   . LYS B  1 441 ? -39.961 65.139 35.172  1.00 21.74 ? 441  LYS B C   1 
ATOM   9318  O  O   . LYS B  1 441 ? -39.404 65.114 34.074  1.00 20.86 ? 441  LYS B O   1 
ATOM   9319  C  CB  . LYS B  1 441 ? -42.259 65.474 34.150  1.00 23.99 ? 441  LYS B CB  1 
ATOM   9320  C  CG  . LYS B  1 441 ? -43.726 65.927 34.359  1.00 27.03 ? 441  LYS B CG  1 
ATOM   9321  C  CD  . LYS B  1 441 ? -44.383 65.197 35.554  1.00 28.81 ? 441  LYS B CD  1 
ATOM   9322  C  CE  . LYS B  1 441 ? -45.866 65.557 35.742  1.00 30.34 ? 441  LYS B CE  1 
ATOM   9323  N  NZ  . LYS B  1 441 ? -46.029 67.010 36.062  1.00 32.93 ? 441  LYS B NZ  1 
ATOM   9324  N  N   . VAL B  1 442 ? -39.410 64.639 36.271  1.00 20.24 ? 442  VAL B N   1 
ATOM   9325  C  CA  . VAL B  1 442 ? -38.094 64.010 36.272  1.00 21.00 ? 442  VAL B CA  1 
ATOM   9326  C  C   . VAL B  1 442 ? -38.242 62.593 36.781  1.00 20.70 ? 442  VAL B C   1 
ATOM   9327  O  O   . VAL B  1 442 ? -38.696 62.366 37.903  1.00 20.38 ? 442  VAL B O   1 
ATOM   9328  C  CB  . VAL B  1 442 ? -37.099 64.773 37.184  1.00 20.81 ? 442  VAL B CB  1 
ATOM   9329  C  CG1 . VAL B  1 442 ? -35.810 63.972 37.349  1.00 21.06 ? 442  VAL B CG1 1 
ATOM   9330  C  CG2 . VAL B  1 442 ? -36.776 66.130 36.576  1.00 21.09 ? 442  VAL B CG2 1 
ATOM   9331  N  N   . THR B  1 443 ? -37.853 61.634 35.958  1.00 21.05 ? 443  THR B N   1 
ATOM   9332  C  CA  . THR B  1 443 ? -37.986 60.242 36.346  1.00 20.52 ? 443  THR B CA  1 
ATOM   9333  C  C   . THR B  1 443 ? -36.610 59.606 36.531  1.00 20.91 ? 443  THR B C   1 
ATOM   9334  O  O   . THR B  1 443 ? -35.718 59.794 35.687  1.00 19.92 ? 443  THR B O   1 
ATOM   9335  C  CB  . THR B  1 443 ? -38.744 59.439 35.243  1.00 21.94 ? 443  THR B CB  1 
ATOM   9336  O  OG1 . THR B  1 443 ? -40.020 60.041 34.988  1.00 22.22 ? 443  THR B OG1 1 
ATOM   9337  C  CG2 . THR B  1 443 ? -38.960 57.999 35.684  1.00 21.83 ? 443  THR B CG2 1 
ATOM   9338  N  N   . CYS B  1 444 ? -36.409 58.887 37.634  1.00 19.87 ? 444  CYS B N   1 
ATOM   9339  C  CA  . CYS B  1 444 ? -35.144 58.202 37.804  1.00 19.75 ? 444  CYS B CA  1 
ATOM   9340  C  C   . CYS B  1 444 ? -35.359 56.840 37.158  1.00 19.99 ? 444  CYS B C   1 
ATOM   9341  O  O   . CYS B  1 444 ? -36.263 56.077 37.562  1.00 18.76 ? 444  CYS B O   1 
ATOM   9342  C  CB  . CYS B  1 444 ? -34.746 58.019 39.274  1.00 20.55 ? 444  CYS B CB  1 
ATOM   9343  S  SG  . CYS B  1 444 ? -33.048 57.256 39.333  1.00 21.76 ? 444  CYS B SG  1 
ATOM   9344  N  N   . LEU B  1 445 ? -34.532 56.539 36.156  1.00 19.32 ? 445  LEU B N   1 
ATOM   9345  C  CA  . LEU B  1 445 ? -34.645 55.290 35.408  1.00 20.37 ? 445  LEU B CA  1 
ATOM   9346  C  C   . LEU B  1 445 ? -33.943 54.092 36.004  1.00 21.20 ? 445  LEU B C   1 
ATOM   9347  O  O   . LEU B  1 445 ? -34.309 52.955 35.716  1.00 22.75 ? 445  LEU B O   1 
ATOM   9348  C  CB  . LEU B  1 445 ? -34.124 55.488 33.975  1.00 19.49 ? 445  LEU B CB  1 
ATOM   9349  C  CG  . LEU B  1 445 ? -34.885 56.550 33.189  1.00 20.80 ? 445  LEU B CG  1 
ATOM   9350  C  CD1 . LEU B  1 445 ? -34.374 56.598 31.743  1.00 18.18 ? 445  LEU B CD1 1 
ATOM   9351  C  CD2 . LEU B  1 445 ? -36.400 56.235 33.230  1.00 18.22 ? 445  LEU B CD2 1 
ATOM   9352  N  N   . SER B  1 446 ? -32.936 54.337 36.837  1.00 21.67 ? 446  SER B N   1 
ATOM   9353  C  CA  . SER B  1 446 ? -32.157 53.248 37.413  1.00 21.12 ? 446  SER B CA  1 
ATOM   9354  C  C   . SER B  1 446 ? -32.201 53.080 38.934  1.00 20.74 ? 446  SER B C   1 
ATOM   9355  O  O   . SER B  1 446 ? -31.894 52.001 39.429  1.00 21.76 ? 446  SER B O   1 
ATOM   9356  C  CB  . SER B  1 446 ? -30.691 53.425 37.019  1.00 19.89 ? 446  SER B CB  1 
ATOM   9357  O  OG  . SER B  1 446 ? -30.192 54.652 37.534  1.00 17.68 ? 446  SER B OG  1 
ATOM   9358  N  N   . CYS B  1 447 ? -32.552 54.142 39.655  1.00 20.90 ? 447  CYS B N   1 
ATOM   9359  C  CA  . CYS B  1 447 ? -32.560 54.143 41.120  1.00 22.51 ? 447  CYS B CA  1 
ATOM   9360  C  C   . CYS B  1 447 ? -33.120 52.906 41.809  1.00 22.99 ? 447  CYS B C   1 
ATOM   9361  O  O   . CYS B  1 447 ? -32.459 52.276 42.632  1.00 22.60 ? 447  CYS B O   1 
ATOM   9362  C  CB  . CYS B  1 447 ? -33.326 55.369 41.657  1.00 21.79 ? 447  CYS B CB  1 
ATOM   9363  S  SG  . CYS B  1 447 ? -32.604 56.992 41.300  1.00 23.90 ? 447  CYS B SG  1 
ATOM   9364  N  N   . GLU B  1 448 ? -34.353 52.573 41.457  1.00 23.89 ? 448  GLU B N   1 
ATOM   9365  C  CA  . GLU B  1 448 ? -35.084 51.474 42.071  1.00 25.91 ? 448  GLU B CA  1 
ATOM   9366  C  C   . GLU B  1 448 ? -34.972 50.098 41.389  1.00 25.69 ? 448  GLU B C   1 
ATOM   9367  O  O   . GLU B  1 448 ? -35.617 49.149 41.817  1.00 26.89 ? 448  GLU B O   1 
ATOM   9368  C  CB  . GLU B  1 448 ? -36.558 51.904 42.177  1.00 26.09 ? 448  GLU B CB  1 
ATOM   9369  C  CG  . GLU B  1 448 ? -37.097 52.176 43.573  1.00 31.07 ? 448  GLU B CG  1 
ATOM   9370  C  CD  . GLU B  1 448 ? -36.128 52.864 44.515  1.00 31.18 ? 448  GLU B CD  1 
ATOM   9371  O  OE1 . GLU B  1 448 ? -36.037 54.114 44.528  1.00 31.29 ? 448  GLU B OE1 1 
ATOM   9372  O  OE2 . GLU B  1 448 ? -35.447 52.123 45.248  1.00 34.72 ? 448  GLU B OE2 1 
ATOM   9373  N  N   . LEU B  1 449 ? -34.159 49.961 40.346  1.00 25.85 ? 449  LEU B N   1 
ATOM   9374  C  CA  . LEU B  1 449 ? -34.062 48.656 39.680  1.00 26.17 ? 449  LEU B CA  1 
ATOM   9375  C  C   . LEU B  1 449 ? -33.628 47.547 40.638  1.00 27.49 ? 449  LEU B C   1 
ATOM   9376  O  O   . LEU B  1 449 ? -34.248 46.485 40.700  1.00 27.91 ? 449  LEU B O   1 
ATOM   9377  C  CB  . LEU B  1 449 ? -33.100 48.717 38.496  1.00 25.77 ? 449  LEU B CB  1 
ATOM   9378  C  CG  . LEU B  1 449 ? -33.460 49.665 37.348  1.00 26.10 ? 449  LEU B CG  1 
ATOM   9379  C  CD1 . LEU B  1 449 ? -32.288 49.690 36.350  1.00 25.68 ? 449  LEU B CD1 1 
ATOM   9380  C  CD2 . LEU B  1 449 ? -34.751 49.228 36.676  1.00 25.61 ? 449  LEU B CD2 1 
ATOM   9381  N  N   . ASN B  1 450 ? -32.538 47.783 41.361  1.00 27.75 ? 450  ASN B N   1 
ATOM   9382  C  CA  . ASN B  1 450 ? -32.044 46.841 42.363  1.00 27.99 ? 450  ASN B CA  1 
ATOM   9383  C  C   . ASN B  1 450 ? -31.184 47.724 43.240  1.00 28.56 ? 450  ASN B C   1 
ATOM   9384  O  O   . ASN B  1 450 ? -29.953 47.712 43.149  1.00 28.06 ? 450  ASN B O   1 
ATOM   9385  C  CB  . ASN B  1 450 ? -31.197 45.731 41.753  1.00 27.47 ? 450  ASN B CB  1 
ATOM   9386  C  CG  . ASN B  1 450 ? -30.834 44.658 42.779  1.00 29.41 ? 450  ASN B CG  1 
ATOM   9387  O  OD1 . ASN B  1 450 ? -30.881 44.896 44.009  1.00 27.90 ? 450  ASN B OD1 1 
ATOM   9388  N  ND2 . ASN B  1 450 ? -30.461 43.475 42.289  1.00 28.90 ? 450  ASN B ND2 1 
ATOM   9389  N  N   . PRO B  1 451 ? -31.834 48.513 44.098  1.00 29.10 ? 451  PRO B N   1 
ATOM   9390  C  CA  . PRO B  1 451 ? -31.205 49.455 45.020  1.00 29.11 ? 451  PRO B CA  1 
ATOM   9391  C  C   . PRO B  1 451 ? -30.110 48.927 45.932  1.00 29.64 ? 451  PRO B C   1 
ATOM   9392  O  O   . PRO B  1 451 ? -29.213 49.686 46.325  1.00 28.63 ? 451  PRO B O   1 
ATOM   9393  C  CB  . PRO B  1 451 ? -32.394 50.049 45.783  1.00 29.86 ? 451  PRO B CB  1 
ATOM   9394  C  CG  . PRO B  1 451 ? -33.423 48.945 45.742  1.00 29.94 ? 451  PRO B CG  1 
ATOM   9395  C  CD  . PRO B  1 451 ? -33.290 48.423 44.334  1.00 30.17 ? 451  PRO B CD  1 
ATOM   9396  N  N   . GLU B  1 452 ? -30.162 47.643 46.267  1.00 29.56 ? 452  GLU B N   1 
ATOM   9397  C  CA  . GLU B  1 452 ? -29.147 47.101 47.152  1.00 30.24 ? 452  GLU B CA  1 
ATOM   9398  C  C   . GLU B  1 452 ? -27.914 46.674 46.383  1.00 28.34 ? 452  GLU B C   1 
ATOM   9399  O  O   . GLU B  1 452 ? -26.795 46.870 46.834  1.00 27.92 ? 452  GLU B O   1 
ATOM   9400  C  CB  . GLU B  1 452 ? -29.709 45.927 47.957  1.00 33.87 ? 452  GLU B CB  1 
ATOM   9401  C  CG  . GLU B  1 452 ? -30.951 46.322 48.755  1.00 39.63 ? 452  GLU B CG  1 
ATOM   9402  C  CD  . GLU B  1 452 ? -31.421 45.234 49.695  1.00 43.51 ? 452  GLU B CD  1 
ATOM   9403  O  OE1 . GLU B  1 452 ? -31.675 44.103 49.218  1.00 46.65 ? 452  GLU B OE1 1 
ATOM   9404  O  OE2 . GLU B  1 452 ? -31.544 45.505 50.916  1.00 46.01 ? 452  GLU B OE2 1 
ATOM   9405  N  N   . ARG B  1 453 ? -28.118 46.100 45.211  1.00 26.55 ? 453  ARG B N   1 
ATOM   9406  C  CA  . ARG B  1 453 ? -26.997 45.645 44.408  1.00 25.44 ? 453  ARG B CA  1 
ATOM   9407  C  C   . ARG B  1 453 ? -26.427 46.762 43.523  1.00 24.51 ? 453  ARG B C   1 
ATOM   9408  O  O   . ARG B  1 453 ? -25.220 46.831 43.288  1.00 23.43 ? 453  ARG B O   1 
ATOM   9409  C  CB  . ARG B  1 453 ? -27.437 44.472 43.527  1.00 25.24 ? 453  ARG B CB  1 
ATOM   9410  C  CG  . ARG B  1 453 ? -26.365 44.012 42.573  1.00 25.76 ? 453  ARG B CG  1 
ATOM   9411  C  CD  . ARG B  1 453 ? -26.836 42.888 41.674  1.00 25.69 ? 453  ARG B CD  1 
ATOM   9412  N  NE  . ARG B  1 453 ? -25.748 42.470 40.799  1.00 26.49 ? 453  ARG B NE  1 
ATOM   9413  C  CZ  . ARG B  1 453 ? -25.718 41.329 40.122  1.00 27.03 ? 453  ARG B CZ  1 
ATOM   9414  N  NH1 . ARG B  1 453 ? -26.727 40.472 40.204  1.00 26.64 ? 453  ARG B NH1 1 
ATOM   9415  N  NH2 . ARG B  1 453 ? -24.664 41.038 39.379  1.00 25.98 ? 453  ARG B NH2 1 
ATOM   9416  N  N   . CYS B  1 454 ? -27.302 47.654 43.071  1.00 23.66 ? 454  CYS B N   1 
ATOM   9417  C  CA  . CYS B  1 454 ? -26.904 48.719 42.157  1.00 22.05 ? 454  CYS B CA  1 
ATOM   9418  C  C   . CYS B  1 454 ? -27.137 50.164 42.569  1.00 20.28 ? 454  CYS B C   1 
ATOM   9419  O  O   . CYS B  1 454 ? -28.277 50.626 42.649  1.00 18.17 ? 454  CYS B O   1 
ATOM   9420  C  CB  . CYS B  1 454 ? -27.576 48.454 40.814  1.00 22.00 ? 454  CYS B CB  1 
ATOM   9421  S  SG  . CYS B  1 454 ? -26.990 46.899 40.121  1.00 22.70 ? 454  CYS B SG  1 
ATOM   9422  N  N   . GLN B  1 455 ? -26.035 50.883 42.780  1.00 19.81 ? 455  GLN B N   1 
ATOM   9423  C  CA  . GLN B  1 455 ? -26.091 52.281 43.171  1.00 19.59 ? 455  GLN B CA  1 
ATOM   9424  C  C   . GLN B  1 455 ? -25.138 53.143 42.334  1.00 20.85 ? 455  GLN B C   1 
ATOM   9425  O  O   . GLN B  1 455 ? -25.048 54.351 42.545  1.00 20.98 ? 455  GLN B O   1 
ATOM   9426  C  CB  . GLN B  1 455 ? -25.735 52.423 44.654  1.00 21.89 ? 455  GLN B CB  1 
ATOM   9427  C  CG  . GLN B  1 455 ? -26.811 51.901 45.615  1.00 22.86 ? 455  GLN B CG  1 
ATOM   9428  C  CD  . GLN B  1 455 ? -26.260 51.561 47.003  1.00 25.70 ? 455  GLN B CD  1 
ATOM   9429  O  OE1 . GLN B  1 455 ? -25.366 52.247 47.532  1.00 24.49 ? 455  GLN B OE1 1 
ATOM   9430  N  NE2 . GLN B  1 455 ? -26.804 50.501 47.604  1.00 25.00 ? 455  GLN B NE2 1 
ATOM   9431  N  N   . TYR B  1 456 ? -24.429 52.534 41.389  1.00 20.27 ? 456  TYR B N   1 
ATOM   9432  C  CA  . TYR B  1 456 ? -23.487 53.285 40.554  1.00 20.74 ? 456  TYR B CA  1 
ATOM   9433  C  C   . TYR B  1 456 ? -23.700 52.866 39.099  1.00 20.90 ? 456  TYR B C   1 
ATOM   9434  O  O   . TYR B  1 456 ? -23.289 51.783 38.677  1.00 22.01 ? 456  TYR B O   1 
ATOM   9435  C  CB  . TYR B  1 456 ? -22.052 52.999 41.006  1.00 19.86 ? 456  TYR B CB  1 
ATOM   9436  C  CG  . TYR B  1 456 ? -21.029 54.074 40.662  1.00 20.75 ? 456  TYR B CG  1 
ATOM   9437  C  CD1 . TYR B  1 456 ? -20.495 54.178 39.374  1.00 21.24 ? 456  TYR B CD1 1 
ATOM   9438  C  CD2 . TYR B  1 456 ? -20.579 54.972 41.637  1.00 21.41 ? 456  TYR B CD2 1 
ATOM   9439  C  CE1 . TYR B  1 456 ? -19.539 55.140 39.067  1.00 21.51 ? 456  TYR B CE1 1 
ATOM   9440  C  CE2 . TYR B  1 456 ? -19.619 55.944 41.341  1.00 21.63 ? 456  TYR B CE2 1 
ATOM   9441  C  CZ  . TYR B  1 456 ? -19.105 56.018 40.055  1.00 22.21 ? 456  TYR B CZ  1 
ATOM   9442  O  OH  . TYR B  1 456 ? -18.149 56.961 39.759  1.00 23.20 ? 456  TYR B OH  1 
ATOM   9443  N  N   . TYR B  1 457 ? -24.327 53.747 38.330  1.00 19.06 ? 457  TYR B N   1 
ATOM   9444  C  CA  . TYR B  1 457 ? -24.654 53.445 36.942  1.00 19.32 ? 457  TYR B CA  1 
ATOM   9445  C  C   . TYR B  1 457 ? -23.974 54.315 35.883  1.00 18.49 ? 457  TYR B C   1 
ATOM   9446  O  O   . TYR B  1 457 ? -23.711 55.490 36.122  1.00 18.74 ? 457  TYR B O   1 
ATOM   9447  C  CB  . TYR B  1 457 ? -26.178 53.598 36.743  1.00 18.83 ? 457  TYR B CB  1 
ATOM   9448  C  CG  . TYR B  1 457 ? -27.047 52.489 37.310  1.00 19.52 ? 457  TYR B CG  1 
ATOM   9449  C  CD1 . TYR B  1 457 ? -27.315 51.345 36.552  1.00 18.83 ? 457  TYR B CD1 1 
ATOM   9450  C  CD2 . TYR B  1 457 ? -27.649 52.607 38.568  1.00 19.15 ? 457  TYR B CD2 1 
ATOM   9451  C  CE1 . TYR B  1 457 ? -28.170 50.342 37.021  1.00 19.98 ? 457  TYR B CE1 1 
ATOM   9452  C  CE2 . TYR B  1 457 ? -28.523 51.593 39.054  1.00 18.98 ? 457  TYR B CE2 1 
ATOM   9453  C  CZ  . TYR B  1 457 ? -28.773 50.475 38.268  1.00 19.31 ? 457  TYR B CZ  1 
ATOM   9454  O  OH  . TYR B  1 457 ? -29.639 49.493 38.687  1.00 21.16 ? 457  TYR B OH  1 
ATOM   9455  N  N   . SER B  1 458 ? -23.730 53.717 34.718  1.00 18.56 ? 458  SER B N   1 
ATOM   9456  C  CA  . SER B  1 458 ? -23.227 54.417 33.527  1.00 18.38 ? 458  SER B CA  1 
ATOM   9457  C  C   . SER B  1 458 ? -24.191 53.871 32.456  1.00 18.14 ? 458  SER B C   1 
ATOM   9458  O  O   . SER B  1 458 ? -24.787 52.801 32.638  1.00 18.01 ? 458  SER B O   1 
ATOM   9459  C  CB  . SER B  1 458 ? -21.778 54.055 33.188  1.00 17.37 ? 458  SER B CB  1 
ATOM   9460  O  OG  . SER B  1 458 ? -21.679 52.791 32.574  1.00 20.63 ? 458  SER B OG  1 
ATOM   9461  N  N   . VAL B  1 459 ? -24.357 54.587 31.353  1.00 17.75 ? 459  VAL B N   1 
ATOM   9462  C  CA  . VAL B  1 459 ? -25.285 54.157 30.330  1.00 18.08 ? 459  VAL B CA  1 
ATOM   9463  C  C   . VAL B  1 459 ? -24.743 54.292 28.905  1.00 19.22 ? 459  VAL B C   1 
ATOM   9464  O  O   . VAL B  1 459 ? -23.806 55.041 28.670  1.00 18.82 ? 459  VAL B O   1 
ATOM   9465  C  CB  . VAL B  1 459 ? -26.593 54.985 30.440  1.00 17.40 ? 459  VAL B CB  1 
ATOM   9466  C  CG1 . VAL B  1 459 ? -26.298 56.460 30.185  1.00 17.56 ? 459  VAL B CG1 1 
ATOM   9467  C  CG2 . VAL B  1 459 ? -27.617 54.484 29.463  1.00 16.37 ? 459  VAL B CG2 1 
ATOM   9468  N  N   . SER B  1 460 ? -25.342 53.552 27.971  1.00 19.89 ? 460  SER B N   1 
ATOM   9469  C  CA  . SER B  1 460 ? -24.979 53.595 26.550  1.00 19.94 ? 460  SER B CA  1 
ATOM   9470  C  C   . SER B  1 460 ? -26.248 53.466 25.683  1.00 19.74 ? 460  SER B C   1 
ATOM   9471  O  O   . SER B  1 460 ? -26.865 52.386 25.584  1.00 19.35 ? 460  SER B O   1 
ATOM   9472  C  CB  . SER B  1 460 ? -23.996 52.471 26.212  1.00 22.02 ? 460  SER B CB  1 
ATOM   9473  O  OG  . SER B  1 460 ? -23.848 52.365 24.807  1.00 22.86 ? 460  SER B OG  1 
ATOM   9474  N  N   . PHE B  1 461 ? -26.641 54.581 25.076  1.00 19.39 ? 461  PHE B N   1 
ATOM   9475  C  CA  . PHE B  1 461 ? -27.825 54.641 24.227  1.00 20.09 ? 461  PHE B CA  1 
ATOM   9476  C  C   . PHE B  1 461 ? -27.525 54.215 22.794  1.00 21.29 ? 461  PHE B C   1 
ATOM   9477  O  O   . PHE B  1 461 ? -26.390 54.339 22.336  1.00 21.89 ? 461  PHE B O   1 
ATOM   9478  C  CB  . PHE B  1 461 ? -28.408 56.065 24.222  1.00 19.36 ? 461  PHE B CB  1 
ATOM   9479  C  CG  . PHE B  1 461 ? -29.128 56.448 25.504  1.00 18.78 ? 461  PHE B CG  1 
ATOM   9480  C  CD1 . PHE B  1 461 ? -28.423 56.976 26.586  1.00 18.97 ? 461  PHE B CD1 1 
ATOM   9481  C  CD2 . PHE B  1 461 ? -30.517 56.307 25.616  1.00 18.77 ? 461  PHE B CD2 1 
ATOM   9482  C  CE1 . PHE B  1 461 ? -29.080 57.363 27.758  1.00 18.44 ? 461  PHE B CE1 1 
ATOM   9483  C  CE2 . PHE B  1 461 ? -31.191 56.693 26.792  1.00 17.93 ? 461  PHE B CE2 1 
ATOM   9484  C  CZ  . PHE B  1 461 ? -30.465 57.223 27.862  1.00 17.54 ? 461  PHE B CZ  1 
ATOM   9485  N  N   . SER B  1 462 ? -28.536 53.703 22.094  1.00 21.34 ? 462  SER B N   1 
ATOM   9486  C  CA  . SER B  1 462 ? -28.363 53.291 20.698  1.00 23.55 ? 462  SER B CA  1 
ATOM   9487  C  C   . SER B  1 462 ? -28.323 54.599 19.882  1.00 25.19 ? 462  SER B C   1 
ATOM   9488  O  O   . SER B  1 462 ? -28.576 55.672 20.431  1.00 23.59 ? 462  SER B O   1 
ATOM   9489  C  CB  . SER B  1 462 ? -29.538 52.423 20.257  1.00 21.79 ? 462  SER B CB  1 
ATOM   9490  O  OG  . SER B  1 462 ? -30.744 53.145 20.417  1.00 19.00 ? 462  SER B OG  1 
ATOM   9491  N  N   . LYS B  1 463 ? -28.060 54.520 18.578  1.00 27.73 ? 463  LYS B N   1 
ATOM   9492  C  CA  . LYS B  1 463 ? -27.927 55.738 17.752  1.00 30.48 ? 463  LYS B CA  1 
ATOM   9493  C  C   . LYS B  1 463 ? -28.913 56.887 17.922  1.00 31.26 ? 463  LYS B C   1 
ATOM   9494  O  O   . LYS B  1 463 ? -28.498 58.055 17.937  1.00 31.69 ? 463  LYS B O   1 
ATOM   9495  C  CB  . LYS B  1 463 ? -27.848 55.377 16.262  1.00 32.81 ? 463  LYS B CB  1 
ATOM   9496  C  CG  . LYS B  1 463 ? -26.563 54.645 15.890  1.00 35.82 ? 463  LYS B CG  1 
ATOM   9497  C  CD  . LYS B  1 463 ? -25.335 55.376 16.411  1.00 37.68 ? 463  LYS B CD  1 
ATOM   9498  C  CE  . LYS B  1 463 ? -24.084 54.543 16.212  1.00 39.73 ? 463  LYS B CE  1 
ATOM   9499  N  NZ  . LYS B  1 463 ? -22.830 55.281 16.572  1.00 41.01 ? 463  LYS B NZ  1 
ATOM   9500  N  N   . GLU B  1 464 ? -30.205 56.581 18.022  1.00 31.27 ? 464  GLU B N   1 
ATOM   9501  C  CA  . GLU B  1 464 ? -31.221 57.631 18.202  1.00 31.31 ? 464  GLU B CA  1 
ATOM   9502  C  C   . GLU B  1 464 ? -31.886 57.480 19.568  1.00 30.08 ? 464  GLU B C   1 
ATOM   9503  O  O   . GLU B  1 464 ? -33.037 57.881 19.760  1.00 29.27 ? 464  GLU B O   1 
ATOM   9504  C  CB  . GLU B  1 464 ? -32.302 57.542 17.117  1.00 34.06 ? 464  GLU B CB  1 
ATOM   9505  C  CG  . GLU B  1 464 ? -31.767 57.503 15.698  1.00 37.79 ? 464  GLU B CG  1 
ATOM   9506  C  CD  . GLU B  1 464 ? -30.790 58.626 15.431  1.00 41.01 ? 464  GLU B CD  1 
ATOM   9507  O  OE1 . GLU B  1 464 ? -31.172 59.794 15.665  1.00 42.81 ? 464  GLU B OE1 1 
ATOM   9508  O  OE2 . GLU B  1 464 ? -29.644 58.357 14.992  1.00 43.04 ? 464  GLU B OE2 1 
ATOM   9509  N  N   . ALA B  1 465 ? -31.153 56.880 20.503  1.00 27.96 ? 465  ALA B N   1 
ATOM   9510  C  CA  . ALA B  1 465 ? -31.636 56.665 21.854  1.00 26.79 ? 465  ALA B CA  1 
ATOM   9511  C  C   . ALA B  1 465 ? -32.888 55.785 21.926  1.00 26.79 ? 465  ALA B C   1 
ATOM   9512  O  O   . ALA B  1 465 ? -33.674 55.925 22.854  1.00 27.40 ? 465  ALA B O   1 
ATOM   9513  C  CB  . ALA B  1 465 ? -31.917 58.005 22.516  1.00 25.43 ? 465  ALA B CB  1 
ATOM   9514  N  N   . LYS B  1 466 ? -33.077 54.886 20.967  1.00 26.27 ? 466  LYS B N   1 
ATOM   9515  C  CA  . LYS B  1 466 ? -34.247 54.002 20.984  1.00 26.55 ? 466  LYS B CA  1 
ATOM   9516  C  C   . LYS B  1 466 ? -34.123 52.934 22.093  1.00 25.13 ? 466  LYS B C   1 
ATOM   9517  O  O   . LYS B  1 466 ? -35.125 52.471 22.641  1.00 24.66 ? 466  LYS B O   1 
ATOM   9518  C  CB  . LYS B  1 466 ? -34.422 53.342 19.609  1.00 27.53 ? 466  LYS B CB  1 
ATOM   9519  C  CG  . LYS B  1 466 ? -35.794 52.672 19.368  1.00 32.01 ? 466  LYS B CG  1 
ATOM   9520  C  CD  . LYS B  1 466 ? -35.911 52.239 17.892  1.00 33.84 ? 466  LYS B CD  1 
ATOM   9521  C  CE  . LYS B  1 466 ? -37.340 51.911 17.463  1.00 35.64 ? 466  LYS B CE  1 
ATOM   9522  N  NZ  . LYS B  1 466 ? -37.749 50.516 17.820  1.00 38.03 ? 466  LYS B NZ  1 
ATOM   9523  N  N   . TYR B  1 467 ? -32.892 52.554 22.426  1.00 23.39 ? 467  TYR B N   1 
ATOM   9524  C  CA  . TYR B  1 467 ? -32.627 51.567 23.481  1.00 21.67 ? 467  TYR B CA  1 
ATOM   9525  C  C   . TYR B  1 467 ? -31.437 52.037 24.295  1.00 20.80 ? 467  TYR B C   1 
ATOM   9526  O  O   . TYR B  1 467 ? -30.657 52.863 23.831  1.00 20.35 ? 467  TYR B O   1 
ATOM   9527  C  CB  . TYR B  1 467 ? -32.244 50.205 22.883  1.00 21.31 ? 467  TYR B CB  1 
ATOM   9528  C  CG  . TYR B  1 467 ? -33.303 49.590 22.010  1.00 22.14 ? 467  TYR B CG  1 
ATOM   9529  C  CD1 . TYR B  1 467 ? -34.363 48.871 22.562  1.00 22.88 ? 467  TYR B CD1 1 
ATOM   9530  C  CD2 . TYR B  1 467 ? -33.264 49.750 20.627  1.00 22.62 ? 467  TYR B CD2 1 
ATOM   9531  C  CE1 . TYR B  1 467 ? -35.368 48.324 21.752  1.00 22.94 ? 467  TYR B CE1 1 
ATOM   9532  C  CE2 . TYR B  1 467 ? -34.260 49.211 19.809  1.00 23.42 ? 467  TYR B CE2 1 
ATOM   9533  C  CZ  . TYR B  1 467 ? -35.307 48.506 20.375  1.00 23.08 ? 467  TYR B CZ  1 
ATOM   9534  O  OH  . TYR B  1 467 ? -36.306 48.035 19.557  1.00 24.07 ? 467  TYR B OH  1 
ATOM   9535  N  N   . TYR B  1 468 ? -31.298 51.536 25.515  1.00 19.32 ? 468  TYR B N   1 
ATOM   9536  C  CA  . TYR B  1 468 ? -30.121 51.869 26.294  1.00 19.36 ? 468  TYR B CA  1 
ATOM   9537  C  C   . TYR B  1 468 ? -29.673 50.703 27.160  1.00 19.04 ? 468  TYR B C   1 
ATOM   9538  O  O   . TYR B  1 468 ? -30.492 49.942 27.684  1.00 19.60 ? 468  TYR B O   1 
ATOM   9539  C  CB  . TYR B  1 468 ? -30.305 53.122 27.159  1.00 19.01 ? 468  TYR B CB  1 
ATOM   9540  C  CG  . TYR B  1 468 ? -31.503 53.120 28.084  1.00 21.82 ? 468  TYR B CG  1 
ATOM   9541  C  CD1 . TYR B  1 468 ? -32.759 53.492 27.620  1.00 21.85 ? 468  TYR B CD1 1 
ATOM   9542  C  CD2 . TYR B  1 468 ? -31.369 52.781 29.432  1.00 21.24 ? 468  TYR B CD2 1 
ATOM   9543  C  CE1 . TYR B  1 468 ? -33.862 53.540 28.476  1.00 22.36 ? 468  TYR B CE1 1 
ATOM   9544  C  CE2 . TYR B  1 468 ? -32.455 52.819 30.295  1.00 22.13 ? 468  TYR B CE2 1 
ATOM   9545  C  CZ  . TYR B  1 468 ? -33.699 53.204 29.810  1.00 22.75 ? 468  TYR B CZ  1 
ATOM   9546  O  OH  . TYR B  1 468 ? -34.768 53.267 30.660  1.00 22.43 ? 468  TYR B OH  1 
ATOM   9547  N  N   . GLN B  1 469 ? -28.359 50.548 27.258  1.00 18.41 ? 469  GLN B N   1 
ATOM   9548  C  CA  . GLN B  1 469 ? -27.762 49.505 28.081  1.00 19.04 ? 469  GLN B CA  1 
ATOM   9549  C  C   . GLN B  1 469 ? -27.364 50.171 29.380  1.00 19.74 ? 469  GLN B C   1 
ATOM   9550  O  O   . GLN B  1 469 ? -26.714 51.219 29.372  1.00 19.22 ? 469  GLN B O   1 
ATOM   9551  C  CB  . GLN B  1 469 ? -26.504 48.925 27.434  1.00 18.89 ? 469  GLN B CB  1 
ATOM   9552  C  CG  . GLN B  1 469 ? -25.736 47.992 28.353  1.00 19.22 ? 469  GLN B CG  1 
ATOM   9553  C  CD  . GLN B  1 469 ? -24.346 47.697 27.827  1.00 21.05 ? 469  GLN B CD  1 
ATOM   9554  O  OE1 . GLN B  1 469 ? -23.628 48.611 27.423  1.00 21.97 ? 469  GLN B OE1 1 
ATOM   9555  N  NE2 . GLN B  1 469 ? -23.952 46.426 27.837  1.00 20.45 ? 469  GLN B NE2 1 
ATOM   9556  N  N   . LEU B  1 470 ? -27.784 49.587 30.495  1.00 19.66 ? 470  LEU B N   1 
ATOM   9557  C  CA  . LEU B  1 470 ? -27.415 50.132 31.782  1.00 20.31 ? 470  LEU B CA  1 
ATOM   9558  C  C   . LEU B  1 470 ? -26.255 49.312 32.310  1.00 20.40 ? 470  LEU B C   1 
ATOM   9559  O  O   . LEU B  1 470 ? -26.242 48.090 32.203  1.00 19.08 ? 470  LEU B O   1 
ATOM   9560  C  CB  . LEU B  1 470 ? -28.580 50.083 32.769  1.00 18.99 ? 470  LEU B CB  1 
ATOM   9561  C  CG  . LEU B  1 470 ? -29.559 51.235 32.602  1.00 18.72 ? 470  LEU B CG  1 
ATOM   9562  C  CD1 . LEU B  1 470 ? -30.679 51.095 33.624  1.00 18.94 ? 470  LEU B CD1 1 
ATOM   9563  C  CD2 . LEU B  1 470 ? -28.825 52.553 32.801  1.00 19.06 ? 470  LEU B CD2 1 
ATOM   9564  N  N   . ARG B  1 471 ? -25.287 50.006 32.890  1.00 21.24 ? 471  ARG B N   1 
ATOM   9565  C  CA  . ARG B  1 471 ? -24.107 49.365 33.423  1.00 22.31 ? 471  ARG B CA  1 
ATOM   9566  C  C   . ARG B  1 471 ? -23.994 49.664 34.897  1.00 21.34 ? 471  ARG B C   1 
ATOM   9567  O  O   . ARG B  1 471 ? -23.634 50.766 35.300  1.00 20.35 ? 471  ARG B O   1 
ATOM   9568  C  CB  . ARG B  1 471 ? -22.888 49.862 32.643  1.00 25.04 ? 471  ARG B CB  1 
ATOM   9569  C  CG  . ARG B  1 471 ? -23.102 49.623 31.144  1.00 29.17 ? 471  ARG B CG  1 
ATOM   9570  C  CD  . ARG B  1 471 ? -21.960 50.100 30.264  1.00 33.40 ? 471  ARG B CD  1 
ATOM   9571  N  NE  . ARG B  1 471 ? -21.837 51.563 30.208  1.00 35.57 ? 471  ARG B NE  1 
ATOM   9572  C  CZ  . ARG B  1 471 ? -21.176 52.192 29.244  1.00 36.60 ? 471  ARG B CZ  1 
ATOM   9573  N  NH1 . ARG B  1 471 ? -20.607 51.485 28.276  1.00 37.38 ? 471  ARG B NH1 1 
ATOM   9574  N  NH2 . ARG B  1 471 ? -21.063 53.509 29.253  1.00 37.38 ? 471  ARG B NH2 1 
ATOM   9575  N  N   . CYS B  1 472 ? -24.346 48.672 35.700  1.00 20.78 ? 472  CYS B N   1 
ATOM   9576  C  CA  . CYS B  1 472 ? -24.294 48.801 37.153  1.00 21.62 ? 472  CYS B CA  1 
ATOM   9577  C  C   . CYS B  1 472 ? -22.907 48.341 37.588  1.00 20.83 ? 472  CYS B C   1 
ATOM   9578  O  O   . CYS B  1 472 ? -22.489 47.231 37.253  1.00 21.09 ? 472  CYS B O   1 
ATOM   9579  C  CB  . CYS B  1 472 ? -25.384 47.913 37.773  1.00 22.51 ? 472  CYS B CB  1 
ATOM   9580  S  SG  . CYS B  1 472 ? -25.098 47.406 39.495  1.00 25.27 ? 472  CYS B SG  1 
ATOM   9581  N  N   . SER B  1 473 ? -22.177 49.167 38.325  1.00 21.12 ? 473  SER B N   1 
ATOM   9582  C  CA  . SER B  1 473 ? -20.835 48.739 38.719  1.00 21.90 ? 473  SER B CA  1 
ATOM   9583  C  C   . SER B  1 473 ? -20.639 48.539 40.225  1.00 22.31 ? 473  SER B C   1 
ATOM   9584  O  O   . SER B  1 473 ? -19.522 48.278 40.670  1.00 21.92 ? 473  SER B O   1 
ATOM   9585  C  CB  . SER B  1 473 ? -19.783 49.727 38.176  1.00 21.96 ? 473  SER B CB  1 
ATOM   9586  O  OG  . SER B  1 473 ? -19.934 50.994 38.789  1.00 23.77 ? 473  SER B OG  1 
ATOM   9587  N  N   . GLY B  1 474 ? -21.720 48.649 41.002  1.00 22.28 ? 474  GLY B N   1 
ATOM   9588  C  CA  . GLY B  1 474 ? -21.622 48.469 42.447  1.00 22.68 ? 474  GLY B CA  1 
ATOM   9589  C  C   . GLY B  1 474 ? -22.847 48.962 43.196  1.00 22.46 ? 474  GLY B C   1 
ATOM   9590  O  O   . GLY B  1 474 ? -23.708 49.591 42.591  1.00 22.96 ? 474  GLY B O   1 
ATOM   9591  N  N   . PRO B  1 475 ? -22.933 48.756 44.521  1.00 23.13 ? 475  PRO B N   1 
ATOM   9592  C  CA  . PRO B  1 475 ? -21.949 48.089 45.388  1.00 22.32 ? 475  PRO B CA  1 
ATOM   9593  C  C   . PRO B  1 475 ? -21.835 46.573 45.236  1.00 22.55 ? 475  PRO B C   1 
ATOM   9594  O  O   . PRO B  1 475 ? -20.867 45.979 45.710  1.00 22.80 ? 475  PRO B O   1 
ATOM   9595  C  CB  . PRO B  1 475 ? -22.379 48.517 46.794  1.00 22.93 ? 475  PRO B CB  1 
ATOM   9596  C  CG  . PRO B  1 475 ? -23.884 48.608 46.662  1.00 22.76 ? 475  PRO B CG  1 
ATOM   9597  C  CD  . PRO B  1 475 ? -24.056 49.297 45.308  1.00 21.76 ? 475  PRO B CD  1 
ATOM   9598  N  N   . GLY B  1 476 ? -22.805 45.952 44.569  1.00 22.12 ? 476  GLY B N   1 
ATOM   9599  C  CA  . GLY B  1 476 ? -22.764 44.509 44.373  1.00 22.73 ? 476  GLY B CA  1 
ATOM   9600  C  C   . GLY B  1 476 ? -21.985 44.165 43.113  1.00 23.08 ? 476  GLY B C   1 
ATOM   9601  O  O   . GLY B  1 476 ? -21.299 45.025 42.563  1.00 22.92 ? 476  GLY B O   1 
ATOM   9602  N  N   . LEU B  1 477 ? -22.078 42.927 42.643  1.00 22.59 ? 477  LEU B N   1 
ATOM   9603  C  CA  . LEU B  1 477 ? -21.365 42.542 41.427  1.00 23.17 ? 477  LEU B CA  1 
ATOM   9604  C  C   . LEU B  1 477 ? -21.959 43.292 40.227  1.00 23.90 ? 477  LEU B C   1 
ATOM   9605  O  O   . LEU B  1 477 ? -23.166 43.558 40.183  1.00 24.37 ? 477  LEU B O   1 
ATOM   9606  C  CB  . LEU B  1 477 ? -21.452 41.022 41.205  1.00 23.15 ? 477  LEU B CB  1 
ATOM   9607  C  CG  . LEU B  1 477 ? -20.652 40.194 42.235  1.00 24.42 ? 477  LEU B CG  1 
ATOM   9608  C  CD1 . LEU B  1 477 ? -20.866 38.690 42.019  1.00 24.76 ? 477  LEU B CD1 1 
ATOM   9609  C  CD2 . LEU B  1 477 ? -19.191 40.525 42.092  1.00 23.64 ? 477  LEU B CD2 1 
ATOM   9610  N  N   . PRO B  1 478 ? -21.111 43.669 39.256  1.00 23.56 ? 478  PRO B N   1 
ATOM   9611  C  CA  . PRO B  1 478 ? -21.549 44.391 38.062  1.00 23.86 ? 478  PRO B CA  1 
ATOM   9612  C  C   . PRO B  1 478 ? -22.685 43.664 37.367  1.00 24.03 ? 478  PRO B C   1 
ATOM   9613  O  O   . PRO B  1 478 ? -22.664 42.435 37.221  1.00 24.46 ? 478  PRO B O   1 
ATOM   9614  C  CB  . PRO B  1 478 ? -20.280 44.458 37.214  1.00 23.03 ? 478  PRO B CB  1 
ATOM   9615  C  CG  . PRO B  1 478 ? -19.217 44.588 38.261  1.00 23.66 ? 478  PRO B CG  1 
ATOM   9616  C  CD  . PRO B  1 478 ? -19.647 43.529 39.268  1.00 22.81 ? 478  PRO B CD  1 
ATOM   9617  N  N   . LEU B  1 479 ? -23.670 44.444 36.931  1.00 24.28 ? 479  LEU B N   1 
ATOM   9618  C  CA  . LEU B  1 479 ? -24.851 43.911 36.257  1.00 23.40 ? 479  LEU B CA  1 
ATOM   9619  C  C   . LEU B  1 479 ? -25.132 44.730 35.007  1.00 23.02 ? 479  LEU B C   1 
ATOM   9620  O  O   . LEU B  1 479 ? -25.218 45.949 35.065  1.00 23.14 ? 479  LEU B O   1 
ATOM   9621  C  CB  . LEU B  1 479 ? -26.047 43.976 37.206  1.00 22.29 ? 479  LEU B CB  1 
ATOM   9622  C  CG  . LEU B  1 479 ? -27.381 43.541 36.618  1.00 22.40 ? 479  LEU B CG  1 
ATOM   9623  C  CD1 . LEU B  1 479 ? -27.334 42.090 36.225  1.00 21.69 ? 479  LEU B CD1 1 
ATOM   9624  C  CD2 . LEU B  1 479 ? -28.478 43.776 37.656  1.00 23.31 ? 479  LEU B CD2 1 
ATOM   9625  N  N   . TYR B  1 480 ? -25.270 44.062 33.873  1.00 23.10 ? 480  TYR B N   1 
ATOM   9626  C  CA  . TYR B  1 480 ? -25.524 44.765 32.626  1.00 23.28 ? 480  TYR B CA  1 
ATOM   9627  C  C   . TYR B  1 480 ? -26.903 44.411 32.094  1.00 22.19 ? 480  TYR B C   1 
ATOM   9628  O  O   . TYR B  1 480 ? -27.214 43.231 31.885  1.00 21.53 ? 480  TYR B O   1 
ATOM   9629  C  CB  . TYR B  1 480 ? -24.453 44.400 31.587  1.00 24.89 ? 480  TYR B CB  1 
ATOM   9630  C  CG  . TYR B  1 480 ? -23.050 44.746 32.017  1.00 26.59 ? 480  TYR B CG  1 
ATOM   9631  C  CD1 . TYR B  1 480 ? -22.357 43.951 32.935  1.00 27.95 ? 480  TYR B CD1 1 
ATOM   9632  C  CD2 . TYR B  1 480 ? -22.421 45.879 31.518  1.00 28.61 ? 480  TYR B CD2 1 
ATOM   9633  C  CE1 . TYR B  1 480 ? -21.064 44.285 33.347  1.00 28.80 ? 480  TYR B CE1 1 
ATOM   9634  C  CE2 . TYR B  1 480 ? -21.131 46.227 31.918  1.00 30.13 ? 480  TYR B CE2 1 
ATOM   9635  C  CZ  . TYR B  1 480 ? -20.463 45.427 32.833  1.00 30.19 ? 480  TYR B CZ  1 
ATOM   9636  O  OH  . TYR B  1 480 ? -19.211 45.803 33.240  1.00 31.46 ? 480  TYR B OH  1 
ATOM   9637  N  N   . THR B  1 481 ? -27.715 45.428 31.839  1.00 21.27 ? 481  THR B N   1 
ATOM   9638  C  CA  . THR B  1 481 ? -29.078 45.205 31.351  1.00 21.35 ? 481  THR B CA  1 
ATOM   9639  C  C   . THR B  1 481 ? -29.419 46.053 30.128  1.00 21.19 ? 481  THR B C   1 
ATOM   9640  O  O   . THR B  1 481 ? -28.789 47.080 29.905  1.00 21.24 ? 481  THR B O   1 
ATOM   9641  C  CB  . THR B  1 481 ? -30.081 45.500 32.493  1.00 21.01 ? 481  THR B CB  1 
ATOM   9642  O  OG1 . THR B  1 481 ? -29.832 46.814 33.024  1.00 20.47 ? 481  THR B OG1 1 
ATOM   9643  C  CG2 . THR B  1 481 ? -29.893 44.476 33.629  1.00 20.27 ? 481  THR B CG2 1 
ATOM   9644  N  N   . LEU B  1 482 ? -30.391 45.608 29.327  1.00 20.21 ? 482  LEU B N   1 
ATOM   9645  C  CA  . LEU B  1 482 ? -30.800 46.343 28.128  1.00 20.39 ? 482  LEU B CA  1 
ATOM   9646  C  C   . LEU B  1 482 ? -32.231 46.831 28.309  1.00 20.87 ? 482  LEU B C   1 
ATOM   9647  O  O   . LEU B  1 482 ? -33.086 46.124 28.846  1.00 20.00 ? 482  LEU B O   1 
ATOM   9648  C  CB  . LEU B  1 482 ? -30.703 45.464 26.880  1.00 19.90 ? 482  LEU B CB  1 
ATOM   9649  C  CG  . LEU B  1 482 ? -30.684 46.200 25.533  1.00 20.30 ? 482  LEU B CG  1 
ATOM   9650  C  CD1 . LEU B  1 482 ? -29.401 47.052 25.445  1.00 19.60 ? 482  LEU B CD1 1 
ATOM   9651  C  CD2 . LEU B  1 482 ? -30.727 45.199 24.380  1.00 19.49 ? 482  LEU B CD2 1 
ATOM   9652  N  N   . HIS B  1 483 ? -32.486 48.038 27.835  1.00 21.07 ? 483  HIS B N   1 
ATOM   9653  C  CA  . HIS B  1 483 ? -33.783 48.656 28.010  1.00 20.54 ? 483  HIS B CA  1 
ATOM   9654  C  C   . HIS B  1 483 ? -34.330 49.317 26.754  1.00 21.51 ? 483  HIS B C   1 
ATOM   9655  O  O   . HIS B  1 483 ? -33.577 49.729 25.858  1.00 20.47 ? 483  HIS B O   1 
ATOM   9656  C  CB  . HIS B  1 483 ? -33.671 49.690 29.131  1.00 20.81 ? 483  HIS B CB  1 
ATOM   9657  C  CG  . HIS B  1 483 ? -33.093 49.134 30.395  1.00 22.44 ? 483  HIS B CG  1 
ATOM   9658  N  ND1 . HIS B  1 483 ? -33.871 48.773 31.478  1.00 23.35 ? 483  HIS B ND1 1 
ATOM   9659  C  CD2 . HIS B  1 483 ? -31.819 48.813 30.728  1.00 23.55 ? 483  HIS B CD2 1 
ATOM   9660  C  CE1 . HIS B  1 483 ? -33.101 48.260 32.422  1.00 23.09 ? 483  HIS B CE1 1 
ATOM   9661  N  NE2 . HIS B  1 483 ? -31.852 48.270 31.993  1.00 22.74 ? 483  HIS B NE2 1 
ATOM   9662  N  N   . SER B  1 484 ? -35.658 49.412 26.703  1.00 20.05 ? 484  SER B N   1 
ATOM   9663  C  CA  . SER B  1 484 ? -36.375 50.040 25.596  1.00 21.18 ? 484  SER B CA  1 
ATOM   9664  C  C   . SER B  1 484 ? -36.719 51.466 26.041  1.00 20.97 ? 484  SER B C   1 
ATOM   9665  O  O   . SER B  1 484 ? -37.318 51.647 27.101  1.00 20.78 ? 484  SER B O   1 
ATOM   9666  C  CB  . SER B  1 484 ? -37.659 49.261 25.316  1.00 21.42 ? 484  SER B CB  1 
ATOM   9667  O  OG  . SER B  1 484 ? -38.448 50.006 24.410  1.00 29.10 ? 484  SER B OG  1 
ATOM   9668  N  N   . SER B  1 485 ? -36.355 52.477 25.253  1.00 20.19 ? 485  SER B N   1 
ATOM   9669  C  CA  . SER B  1 485 ? -36.631 53.861 25.652  1.00 20.51 ? 485  SER B CA  1 
ATOM   9670  C  C   . SER B  1 485 ? -38.095 54.271 25.495  1.00 20.34 ? 485  SER B C   1 
ATOM   9671  O  O   . SER B  1 485 ? -38.576 55.186 26.180  1.00 19.49 ? 485  SER B O   1 
ATOM   9672  C  CB  . SER B  1 485 ? -35.780 54.861 24.840  1.00 20.75 ? 485  SER B CB  1 
ATOM   9673  O  OG  . SER B  1 485 ? -34.381 54.650 25.035  1.00 23.75 ? 485  SER B OG  1 
ATOM   9674  N  N   . VAL B  1 486 ? -38.798 53.614 24.584  1.00 20.04 ? 486  VAL B N   1 
ATOM   9675  C  CA  . VAL B  1 486 ? -40.181 53.983 24.323  1.00 20.96 ? 486  VAL B CA  1 
ATOM   9676  C  C   . VAL B  1 486 ? -41.086 53.790 25.537  1.00 20.48 ? 486  VAL B C   1 
ATOM   9677  O  O   . VAL B  1 486 ? -42.010 54.581 25.749  1.00 20.20 ? 486  VAL B O   1 
ATOM   9678  C  CB  . VAL B  1 486 ? -40.734 53.216 23.081  1.00 21.68 ? 486  VAL B CB  1 
ATOM   9679  C  CG1 . VAL B  1 486 ? -40.941 51.755 23.411  1.00 23.03 ? 486  VAL B CG1 1 
ATOM   9680  C  CG2 . VAL B  1 486 ? -42.035 53.874 22.567  1.00 22.09 ? 486  VAL B CG2 1 
ATOM   9681  N  N   . ASN B  1 487 ? -40.786 52.785 26.359  1.00 20.51 ? 487  ASN B N   1 
ATOM   9682  C  CA  . ASN B  1 487 ? -41.595 52.481 27.542  1.00 21.05 ? 487  ASN B CA  1 
ATOM   9683  C  C   . ASN B  1 487 ? -40.731 52.276 28.785  1.00 21.93 ? 487  ASN B C   1 
ATOM   9684  O  O   . ASN B  1 487 ? -41.235 51.902 29.846  1.00 21.25 ? 487  ASN B O   1 
ATOM   9685  C  CB  . ASN B  1 487 ? -42.425 51.223 27.273  1.00 20.77 ? 487  ASN B CB  1 
ATOM   9686  C  CG  . ASN B  1 487 ? -41.559 50.025 26.863  1.00 22.26 ? 487  ASN B CG  1 
ATOM   9687  O  OD1 . ASN B  1 487 ? -42.071 49.009 26.371  1.00 23.82 ? 487  ASN B OD1 1 
ATOM   9688  N  ND2 . ASN B  1 487 ? -40.252 50.137 27.067  1.00 20.06 ? 487  ASN B ND2 1 
ATOM   9689  N  N   . ASP B  1 488 ? -39.430 52.530 28.647  1.00 22.03 ? 488  ASP B N   1 
ATOM   9690  C  CA  . ASP B  1 488 ? -38.484 52.367 29.758  1.00 21.86 ? 488  ASP B CA  1 
ATOM   9691  C  C   . ASP B  1 488 ? -38.588 50.997 30.416  1.00 21.93 ? 488  ASP B C   1 
ATOM   9692  O  O   . ASP B  1 488 ? -38.365 50.854 31.617  1.00 22.45 ? 488  ASP B O   1 
ATOM   9693  C  CB  . ASP B  1 488 ? -38.694 53.472 30.802  1.00 20.14 ? 488  ASP B CB  1 
ATOM   9694  C  CG  . ASP B  1 488 ? -38.177 54.813 30.320  1.00 21.59 ? 488  ASP B CG  1 
ATOM   9695  O  OD1 . ASP B  1 488 ? -38.922 55.814 30.403  1.00 21.56 ? 488  ASP B OD1 1 
ATOM   9696  O  OD2 . ASP B  1 488 ? -37.017 54.868 29.842  1.00 19.94 ? 488  ASP B OD2 1 
ATOM   9697  N  N   . LYS B  1 489 ? -38.920 49.984 29.624  1.00 21.94 ? 489  LYS B N   1 
ATOM   9698  C  CA  . LYS B  1 489 ? -39.049 48.637 30.161  1.00 22.08 ? 489  LYS B CA  1 
ATOM   9699  C  C   . LYS B  1 489 ? -37.766 47.852 29.973  1.00 22.35 ? 489  LYS B C   1 
ATOM   9700  O  O   . LYS B  1 489 ? -37.066 48.013 28.962  1.00 21.16 ? 489  LYS B O   1 
ATOM   9701  C  CB  . LYS B  1 489 ? -40.225 47.905 29.498  1.00 22.63 ? 489  LYS B CB  1 
ATOM   9702  C  CG  . LYS B  1 489 ? -41.587 48.537 29.840  1.00 25.08 ? 489  LYS B CG  1 
ATOM   9703  C  CD  . LYS B  1 489 ? -41.906 48.447 31.348  1.00 25.54 ? 489  LYS B CD  1 
ATOM   9704  C  CE  . LYS B  1 489 ? -42.648 49.696 31.818  1.00 27.26 ? 489  LYS B CE  1 
ATOM   9705  N  NZ  . LYS B  1 489 ? -43.076 49.624 33.253  1.00 28.98 ? 489  LYS B NZ  1 
ATOM   9706  N  N   . GLY B  1 490 ? -37.460 47.021 30.965  1.00 22.14 ? 490  GLY B N   1 
ATOM   9707  C  CA  . GLY B  1 490 ? -36.266 46.203 30.908  1.00 23.39 ? 490  GLY B CA  1 
ATOM   9708  C  C   . GLY B  1 490 ? -36.498 45.134 29.872  1.00 24.35 ? 490  GLY B C   1 
ATOM   9709  O  O   . GLY B  1 490 ? -37.535 44.469 29.908  1.00 23.77 ? 490  GLY B O   1 
ATOM   9710  N  N   . LEU B  1 491 ? -35.563 44.970 28.941  1.00 24.06 ? 491  LEU B N   1 
ATOM   9711  C  CA  . LEU B  1 491 ? -35.730 43.953 27.909  1.00 24.87 ? 491  LEU B CA  1 
ATOM   9712  C  C   . LEU B  1 491 ? -35.147 42.628 28.367  1.00 26.01 ? 491  LEU B C   1 
ATOM   9713  O  O   . LEU B  1 491 ? -35.735 41.569 28.120  1.00 27.02 ? 491  LEU B O   1 
ATOM   9714  C  CB  . LEU B  1 491 ? -35.066 44.392 26.597  1.00 23.90 ? 491  LEU B CB  1 
ATOM   9715  C  CG  . LEU B  1 491 ? -35.688 45.585 25.860  1.00 24.41 ? 491  LEU B CG  1 
ATOM   9716  C  CD1 . LEU B  1 491 ? -34.800 45.953 24.691  1.00 23.50 ? 491  LEU B CD1 1 
ATOM   9717  C  CD2 . LEU B  1 491 ? -37.091 45.242 25.362  1.00 24.18 ? 491  LEU B CD2 1 
ATOM   9718  N  N   . ARG B  1 492 ? -33.982 42.681 29.013  1.00 25.78 ? 492  ARG B N   1 
ATOM   9719  C  CA  . ARG B  1 492 ? -33.335 41.469 29.520  1.00 26.29 ? 492  ARG B CA  1 
ATOM   9720  C  C   . ARG B  1 492 ? -31.988 41.768 30.136  1.00 26.01 ? 492  ARG B C   1 
ATOM   9721  O  O   . ARG B  1 492 ? -31.422 42.833 29.925  1.00 25.56 ? 492  ARG B O   1 
ATOM   9722  C  CB  . ARG B  1 492 ? -33.160 40.434 28.402  1.00 27.16 ? 492  ARG B CB  1 
ATOM   9723  C  CG  . ARG B  1 492 ? -32.324 40.896 27.221  1.00 29.04 ? 492  ARG B CG  1 
ATOM   9724  C  CD  . ARG B  1 492 ? -32.626 40.073 25.959  1.00 30.01 ? 492  ARG B CD  1 
ATOM   9725  N  NE  . ARG B  1 492 ? -32.192 40.844 24.823  1.00 32.71 ? 492  ARG B NE  1 
ATOM   9726  C  CZ  . ARG B  1 492 ? -32.978 41.627 24.094  1.00 32.78 ? 492  ARG B CZ  1 
ATOM   9727  N  NH1 . ARG B  1 492 ? -34.278 41.724 24.349  1.00 32.33 ? 492  ARG B NH1 1 
ATOM   9728  N  NH2 . ARG B  1 492 ? -32.432 42.391 23.161  1.00 32.97 ? 492  ARG B NH2 1 
ATOM   9729  N  N   . VAL B  1 493 ? -31.493 40.813 30.909  1.00 25.67 ? 493  VAL B N   1 
ATOM   9730  C  CA  . VAL B  1 493 ? -30.213 40.919 31.573  1.00 24.98 ? 493  VAL B CA  1 
ATOM   9731  C  C   . VAL B  1 493 ? -29.188 40.473 30.534  1.00 25.29 ? 493  VAL B C   1 
ATOM   9732  O  O   . VAL B  1 493 ? -29.386 39.458 29.862  1.00 25.93 ? 493  VAL B O   1 
ATOM   9733  C  CB  . VAL B  1 493 ? -30.160 39.976 32.796  1.00 25.47 ? 493  VAL B CB  1 
ATOM   9734  C  CG1 . VAL B  1 493 ? -28.729 39.872 33.327  1.00 24.10 ? 493  VAL B CG1 1 
ATOM   9735  C  CG2 . VAL B  1 493 ? -31.109 40.483 33.882  1.00 23.66 ? 493  VAL B CG2 1 
ATOM   9736  N  N   . LEU B  1 494 ? -28.112 41.235 30.382  1.00 24.39 ? 494  LEU B N   1 
ATOM   9737  C  CA  . LEU B  1 494 ? -27.082 40.908 29.399  1.00 24.14 ? 494  LEU B CA  1 
ATOM   9738  C  C   . LEU B  1 494 ? -25.938 40.151 30.054  1.00 24.62 ? 494  LEU B C   1 
ATOM   9739  O  O   . LEU B  1 494 ? -25.385 39.219 29.465  1.00 25.64 ? 494  LEU B O   1 
ATOM   9740  C  CB  . LEU B  1 494 ? -26.558 42.190 28.720  1.00 23.14 ? 494  LEU B CB  1 
ATOM   9741  C  CG  . LEU B  1 494 ? -27.548 43.006 27.870  1.00 22.04 ? 494  LEU B CG  1 
ATOM   9742  C  CD1 . LEU B  1 494 ? -26.892 44.297 27.416  1.00 22.10 ? 494  LEU B CD1 1 
ATOM   9743  C  CD2 . LEU B  1 494 ? -27.993 42.193 26.651  1.00 23.00 ? 494  LEU B CD2 1 
ATOM   9744  N  N   . GLU B  1 495 ? -25.587 40.537 31.272  1.00 24.42 ? 495  GLU B N   1 
ATOM   9745  C  CA  . GLU B  1 495 ? -24.505 39.863 32.003  1.00 25.24 ? 495  GLU B CA  1 
ATOM   9746  C  C   . GLU B  1 495 ? -24.715 40.163 33.477  1.00 25.17 ? 495  GLU B C   1 
ATOM   9747  O  O   . GLU B  1 495 ? -24.799 41.335 33.870  1.00 25.50 ? 495  GLU B O   1 
ATOM   9748  C  CB  . GLU B  1 495 ? -23.135 40.380 31.541  1.00 25.81 ? 495  GLU B CB  1 
ATOM   9749  C  CG  . GLU B  1 495 ? -21.967 39.871 32.385  1.00 25.21 ? 495  GLU B CG  1 
ATOM   9750  C  CD  . GLU B  1 495 ? -21.894 38.354 32.430  1.00 26.41 ? 495  GLU B CD  1 
ATOM   9751  O  OE1 . GLU B  1 495 ? -21.646 37.736 31.374  1.00 26.10 ? 495  GLU B OE1 1 
ATOM   9752  O  OE2 . GLU B  1 495 ? -22.084 37.780 33.526  1.00 28.26 ? 495  GLU B OE2 1 
ATOM   9753  N  N   . ASP B  1 496 ? -24.807 39.113 34.288  1.00 24.98 ? 496  ASP B N   1 
ATOM   9754  C  CA  . ASP B  1 496 ? -25.054 39.292 35.714  1.00 25.73 ? 496  ASP B CA  1 
ATOM   9755  C  C   . ASP B  1 496 ? -23.935 38.819 36.632  1.00 25.42 ? 496  ASP B C   1 
ATOM   9756  O  O   . ASP B  1 496 ? -24.050 38.912 37.854  1.00 25.73 ? 496  ASP B O   1 
ATOM   9757  C  CB  . ASP B  1 496 ? -26.358 38.595 36.118  1.00 27.12 ? 496  ASP B CB  1 
ATOM   9758  C  CG  . ASP B  1 496 ? -26.319 37.092 35.882  1.00 28.17 ? 496  ASP B CG  1 
ATOM   9759  O  OD1 . ASP B  1 496 ? -25.217 36.536 35.672  1.00 28.16 ? 496  ASP B OD1 1 
ATOM   9760  O  OD2 . ASP B  1 496 ? -27.397 36.456 35.917  1.00 30.06 ? 496  ASP B OD2 1 
ATOM   9761  N  N   . ASN B  1 497 ? -22.858 38.316 36.040  1.00 25.96 ? 497  ASN B N   1 
ATOM   9762  C  CA  . ASN B  1 497 ? -21.713 37.837 36.798  1.00 25.63 ? 497  ASN B CA  1 
ATOM   9763  C  C   . ASN B  1 497 ? -22.049 36.724 37.773  1.00 26.62 ? 497  ASN B C   1 
ATOM   9764  O  O   . ASN B  1 497 ? -21.465 36.620 38.850  1.00 25.92 ? 497  ASN B O   1 
ATOM   9765  C  CB  . ASN B  1 497 ? -21.049 39.003 37.521  1.00 24.59 ? 497  ASN B CB  1 
ATOM   9766  C  CG  . ASN B  1 497 ? -19.999 39.669 36.665  1.00 24.90 ? 497  ASN B CG  1 
ATOM   9767  O  OD1 . ASN B  1 497 ? -18.943 39.096 36.421  1.00 24.83 ? 497  ASN B OD1 1 
ATOM   9768  N  ND2 . ASN B  1 497 ? -20.293 40.874 36.180  1.00 24.97 ? 497  ASN B ND2 1 
ATOM   9769  N  N   . SER B  1 498 ? -22.994 35.879 37.381  1.00 27.56 ? 498  SER B N   1 
ATOM   9770  C  CA  . SER B  1 498 ? -23.397 34.756 38.223  1.00 28.36 ? 498  SER B CA  1 
ATOM   9771  C  C   . SER B  1 498 ? -22.208 33.816 38.428  1.00 28.79 ? 498  SER B C   1 
ATOM   9772  O  O   . SER B  1 498 ? -21.994 33.313 39.530  1.00 30.05 ? 498  SER B O   1 
ATOM   9773  C  CB  . SER B  1 498 ? -24.561 34.010 37.567  1.00 28.48 ? 498  SER B CB  1 
ATOM   9774  O  OG  . SER B  1 498 ? -24.185 33.557 36.278  1.00 31.30 ? 498  SER B OG  1 
ATOM   9775  N  N   . ALA B  1 499 ? -21.429 33.595 37.374  1.00 28.51 ? 499  ALA B N   1 
ATOM   9776  C  CA  . ALA B  1 499 ? -20.259 32.725 37.456  1.00 29.15 ? 499  ALA B CA  1 
ATOM   9777  C  C   . ALA B  1 499 ? -19.317 33.201 38.563  1.00 29.34 ? 499  ALA B C   1 
ATOM   9778  O  O   . ALA B  1 499 ? -18.947 32.426 39.443  1.00 30.10 ? 499  ALA B O   1 
ATOM   9779  C  CB  . ALA B  1 499 ? -19.528 32.697 36.108  1.00 28.93 ? 499  ALA B CB  1 
ATOM   9780  N  N   . LEU B  1 500 ? -18.932 34.474 38.524  1.00 29.01 ? 500  LEU B N   1 
ATOM   9781  C  CA  . LEU B  1 500 ? -18.047 35.013 39.549  1.00 28.96 ? 500  LEU B CA  1 
ATOM   9782  C  C   . LEU B  1 500 ? -18.689 34.930 40.930  1.00 29.30 ? 500  LEU B C   1 
ATOM   9783  O  O   . LEU B  1 500 ? -18.013 34.651 41.920  1.00 28.52 ? 500  LEU B O   1 
ATOM   9784  C  CB  . LEU B  1 500 ? -17.691 36.482 39.264  1.00 28.83 ? 500  LEU B CB  1 
ATOM   9785  C  CG  . LEU B  1 500 ? -16.969 37.229 40.404  1.00 27.88 ? 500  LEU B CG  1 
ATOM   9786  C  CD1 . LEU B  1 500 ? -15.589 36.612 40.641  1.00 27.70 ? 500  LEU B CD1 1 
ATOM   9787  C  CD2 . LEU B  1 500 ? -16.830 38.703 40.062  1.00 28.28 ? 500  LEU B CD2 1 
ATOM   9788  N  N   . ASP B  1 501 ? -19.985 35.201 41.008  1.00 29.53 ? 501  ASP B N   1 
ATOM   9789  C  CA  . ASP B  1 501 ? -20.651 35.152 42.300  1.00 31.80 ? 501  ASP B CA  1 
ATOM   9790  C  C   . ASP B  1 501 ? -20.538 33.756 42.917  1.00 32.58 ? 501  ASP B C   1 
ATOM   9791  O  O   . ASP B  1 501 ? -20.382 33.605 44.132  1.00 32.38 ? 501  ASP B O   1 
ATOM   9792  C  CB  . ASP B  1 501 ? -22.124 35.522 42.159  1.00 32.86 ? 501  ASP B CB  1 
ATOM   9793  C  CG  . ASP B  1 501 ? -22.884 35.354 43.457  1.00 34.85 ? 501  ASP B CG  1 
ATOM   9794  O  OD1 . ASP B  1 501 ? -22.730 36.203 44.353  1.00 34.77 ? 501  ASP B OD1 1 
ATOM   9795  O  OD2 . ASP B  1 501 ? -23.626 34.352 43.589  1.00 37.65 ? 501  ASP B OD2 1 
ATOM   9796  N  N   . LYS B  1 502 ? -20.625 32.737 42.071  1.00 33.61 ? 502  LYS B N   1 
ATOM   9797  C  CA  . LYS B  1 502 ? -20.534 31.370 42.540  1.00 34.84 ? 502  LYS B CA  1 
ATOM   9798  C  C   . LYS B  1 502 ? -19.154 31.192 43.163  1.00 34.70 ? 502  LYS B C   1 
ATOM   9799  O  O   . LYS B  1 502 ? -19.044 30.761 44.313  1.00 35.15 ? 502  LYS B O   1 
ATOM   9800  C  CB  . LYS B  1 502 ? -20.729 30.401 41.368  1.00 36.69 ? 502  LYS B CB  1 
ATOM   9801  C  CG  . LYS B  1 502 ? -21.312 29.040 41.738  1.00 39.41 ? 502  LYS B CG  1 
ATOM   9802  C  CD  . LYS B  1 502 ? -20.432 28.272 42.733  1.00 42.14 ? 502  LYS B CD  1 
ATOM   9803  C  CE  . LYS B  1 502 ? -21.065 28.213 44.123  1.00 42.88 ? 502  LYS B CE  1 
ATOM   9804  N  NZ  . LYS B  1 502 ? -20.241 27.427 45.085  1.00 44.65 ? 502  LYS B NZ  1 
ATOM   9805  N  N   . MET B  1 503 ? -18.114 31.550 42.409  1.00 33.65 ? 503  MET B N   1 
ATOM   9806  C  CA  . MET B  1 503 ? -16.730 31.430 42.882  1.00 33.53 ? 503  MET B CA  1 
ATOM   9807  C  C   . MET B  1 503 ? -16.447 32.164 44.195  1.00 33.64 ? 503  MET B C   1 
ATOM   9808  O  O   . MET B  1 503 ? -15.858 31.595 45.117  1.00 33.06 ? 503  MET B O   1 
ATOM   9809  C  CB  . MET B  1 503 ? -15.749 31.943 41.827  1.00 33.69 ? 503  MET B CB  1 
ATOM   9810  C  CG  . MET B  1 503 ? -15.708 31.144 40.543  1.00 34.07 ? 503  MET B CG  1 
ATOM   9811  S  SD  . MET B  1 503 ? -14.546 31.874 39.350  1.00 37.75 ? 503  MET B SD  1 
ATOM   9812  C  CE  . MET B  1 503 ? -13.060 31.091 39.794  1.00 35.06 ? 503  MET B CE  1 
ATOM   9813  N  N   . LEU B  1 504 ? -16.857 33.426 44.273  1.00 33.49 ? 504  LEU B N   1 
ATOM   9814  C  CA  . LEU B  1 504 ? -16.631 34.223 45.469  1.00 34.29 ? 504  LEU B CA  1 
ATOM   9815  C  C   . LEU B  1 504 ? -17.336 33.710 46.730  1.00 35.34 ? 504  LEU B C   1 
ATOM   9816  O  O   . LEU B  1 504 ? -17.027 34.138 47.858  1.00 34.02 ? 504  LEU B O   1 
ATOM   9817  C  CB  . LEU B  1 504 ? -17.047 35.668 45.208  1.00 33.24 ? 504  LEU B CB  1 
ATOM   9818  C  CG  . LEU B  1 504 ? -16.202 36.377 44.151  1.00 32.20 ? 504  LEU B CG  1 
ATOM   9819  C  CD1 . LEU B  1 504 ? -16.611 37.840 44.078  1.00 30.12 ? 504  LEU B CD1 1 
ATOM   9820  C  CD2 . LEU B  1 504 ? -14.726 36.245 44.510  1.00 30.35 ? 504  LEU B CD2 1 
ATOM   9821  N  N   . GLN B  1 505 ? -18.294 32.806 46.546  1.00 36.93 ? 505  GLN B N   1 
ATOM   9822  C  CA  . GLN B  1 505 ? -19.010 32.263 47.691  1.00 38.48 ? 505  GLN B CA  1 
ATOM   9823  C  C   . GLN B  1 505 ? -18.056 31.415 48.539  1.00 38.25 ? 505  GLN B C   1 
ATOM   9824  O  O   . GLN B  1 505 ? -18.225 31.293 49.750  1.00 38.68 ? 505  GLN B O   1 
ATOM   9825  C  CB  . GLN B  1 505 ? -20.203 31.409 47.229  1.00 40.09 ? 505  GLN B CB  1 
ATOM   9826  C  CG  . GLN B  1 505 ? -21.401 32.202 46.718  1.00 42.14 ? 505  GLN B CG  1 
ATOM   9827  C  CD  . GLN B  1 505 ? -21.837 33.300 47.687  1.00 44.04 ? 505  GLN B CD  1 
ATOM   9828  O  OE1 . GLN B  1 505 ? -21.661 34.491 47.414  1.00 44.98 ? 505  GLN B OE1 1 
ATOM   9829  N  NE2 . GLN B  1 505 ? -22.405 32.902 48.826  1.00 45.12 ? 505  GLN B NE2 1 
ATOM   9830  N  N   . ASN B  1 506 ? -17.040 30.853 47.899  1.00 38.55 ? 506  ASN B N   1 
ATOM   9831  C  CA  . ASN B  1 506 ? -16.074 30.004 48.593  1.00 39.14 ? 506  ASN B CA  1 
ATOM   9832  C  C   . ASN B  1 506 ? -14.869 30.789 49.086  1.00 38.15 ? 506  ASN B C   1 
ATOM   9833  O  O   . ASN B  1 506 ? -13.834 30.200 49.401  1.00 38.79 ? 506  ASN B O   1 
ATOM   9834  C  CB  . ASN B  1 506 ? -15.603 28.887 47.660  1.00 40.44 ? 506  ASN B CB  1 
ATOM   9835  C  CG  . ASN B  1 506 ? -16.754 28.225 46.933  1.00 42.57 ? 506  ASN B CG  1 
ATOM   9836  O  OD1 . ASN B  1 506 ? -17.711 27.752 47.559  1.00 43.20 ? 506  ASN B OD1 1 
ATOM   9837  N  ND2 . ASN B  1 506 ? -16.674 28.188 45.600  1.00 43.64 ? 506  ASN B ND2 1 
ATOM   9838  N  N   . VAL B  1 507 ? -15.008 32.113 49.149  1.00 36.29 ? 507  VAL B N   1 
ATOM   9839  C  CA  . VAL B  1 507 ? -13.923 32.977 49.601  1.00 33.84 ? 507  VAL B CA  1 
ATOM   9840  C  C   . VAL B  1 507 ? -14.346 33.942 50.717  1.00 33.24 ? 507  VAL B C   1 
ATOM   9841  O  O   . VAL B  1 507 ? -15.423 34.530 50.675  1.00 32.21 ? 507  VAL B O   1 
ATOM   9842  C  CB  . VAL B  1 507 ? -13.367 33.818 48.425  1.00 33.51 ? 507  VAL B CB  1 
ATOM   9843  C  CG1 . VAL B  1 507 ? -12.179 34.647 48.898  1.00 32.10 ? 507  VAL B CG1 1 
ATOM   9844  C  CG2 . VAL B  1 507 ? -12.984 32.908 47.259  1.00 31.80 ? 507  VAL B CG2 1 
ATOM   9845  N  N   . GLN B  1 508 ? -13.486 34.094 51.719  1.00 32.42 ? 508  GLN B N   1 
ATOM   9846  C  CA  . GLN B  1 508 ? -13.757 35.020 52.811  1.00 32.37 ? 508  GLN B CA  1 
ATOM   9847  C  C   . GLN B  1 508 ? -13.509 36.442 52.297  1.00 32.50 ? 508  GLN B C   1 
ATOM   9848  O  O   . GLN B  1 508 ? -12.483 37.066 52.595  1.00 32.17 ? 508  GLN B O   1 
ATOM   9849  C  CB  . GLN B  1 508 ? -12.830 34.741 53.993  1.00 32.98 ? 508  GLN B CB  1 
ATOM   9850  C  CG  . GLN B  1 508 ? -12.989 33.367 54.592  1.00 33.63 ? 508  GLN B CG  1 
ATOM   9851  C  CD  . GLN B  1 508 ? -12.320 33.270 55.940  1.00 34.49 ? 508  GLN B CD  1 
ATOM   9852  O  OE1 . GLN B  1 508 ? -12.666 34.005 56.862  1.00 34.70 ? 508  GLN B OE1 1 
ATOM   9853  N  NE2 . GLN B  1 508 ? -11.354 32.367 56.063  1.00 34.26 ? 508  GLN B NE2 1 
ATOM   9854  N  N   . MET B  1 509 ? -14.459 36.951 51.520  1.00 31.52 ? 509  MET B N   1 
ATOM   9855  C  CA  . MET B  1 509 ? -14.346 38.281 50.958  1.00 30.50 ? 509  MET B CA  1 
ATOM   9856  C  C   . MET B  1 509 ? -14.535 39.379 52.003  1.00 29.83 ? 509  MET B C   1 
ATOM   9857  O  O   . MET B  1 509 ? -15.258 39.216 52.984  1.00 30.68 ? 509  MET B O   1 
ATOM   9858  C  CB  . MET B  1 509 ? -15.370 38.452 49.830  1.00 30.60 ? 509  MET B CB  1 
ATOM   9859  C  CG  . MET B  1 509 ? -15.104 37.568 48.640  1.00 31.24 ? 509  MET B CG  1 
ATOM   9860  S  SD  . MET B  1 509 ? -13.458 37.922 47.954  1.00 33.21 ? 509  MET B SD  1 
ATOM   9861  C  CE  . MET B  1 509 ? -13.855 39.393 47.020  1.00 31.47 ? 509  MET B CE  1 
ATOM   9862  N  N   . PRO B  1 510 ? -13.853 40.515 51.819  1.00 28.32 ? 510  PRO B N   1 
ATOM   9863  C  CA  . PRO B  1 510 ? -13.978 41.628 52.765  1.00 27.03 ? 510  PRO B CA  1 
ATOM   9864  C  C   . PRO B  1 510 ? -15.272 42.369 52.484  1.00 26.64 ? 510  PRO B C   1 
ATOM   9865  O  O   . PRO B  1 510 ? -15.895 42.152 51.452  1.00 25.98 ? 510  PRO B O   1 
ATOM   9866  C  CB  . PRO B  1 510 ? -12.769 42.493 52.435  1.00 27.18 ? 510  PRO B CB  1 
ATOM   9867  C  CG  . PRO B  1 510 ? -12.622 42.301 50.980  1.00 26.70 ? 510  PRO B CG  1 
ATOM   9868  C  CD  . PRO B  1 510 ? -12.829 40.803 50.802  1.00 28.39 ? 510  PRO B CD  1 
ATOM   9869  N  N   . SER B  1 511 ? -15.677 43.243 53.390  1.00 26.20 ? 511  SER B N   1 
ATOM   9870  C  CA  . SER B  1 511 ? -16.882 44.011 53.161  1.00 26.91 ? 511  SER B CA  1 
ATOM   9871  C  C   . SER B  1 511 ? -16.445 45.461 52.976  1.00 27.59 ? 511  SER B C   1 
ATOM   9872  O  O   . SER B  1 511 ? -15.308 45.829 53.299  1.00 27.56 ? 511  SER B O   1 
ATOM   9873  C  CB  . SER B  1 511 ? -17.837 43.891 54.348  1.00 25.81 ? 511  SER B CB  1 
ATOM   9874  O  OG  . SER B  1 511 ? -17.247 44.411 55.523  1.00 27.57 ? 511  SER B OG  1 
ATOM   9875  N  N   . LYS B  1 512 ? -17.346 46.274 52.447  1.00 27.49 ? 512  LYS B N   1 
ATOM   9876  C  CA  . LYS B  1 512 ? -17.060 47.679 52.216  1.00 27.88 ? 512  LYS B CA  1 
ATOM   9877  C  C   . LYS B  1 512 ? -18.106 48.551 52.881  1.00 27.68 ? 512  LYS B C   1 
ATOM   9878  O  O   . LYS B  1 512 ? -19.302 48.336 52.715  1.00 28.65 ? 512  LYS B O   1 
ATOM   9879  C  CB  . LYS B  1 512 ? -17.030 47.969 50.714  1.00 27.57 ? 512  LYS B CB  1 
ATOM   9880  C  CG  . LYS B  1 512 ? -16.882 49.429 50.368  1.00 28.06 ? 512  LYS B CG  1 
ATOM   9881  C  CD  . LYS B  1 512 ? -16.651 49.609 48.864  1.00 28.54 ? 512  LYS B CD  1 
ATOM   9882  C  CE  . LYS B  1 512 ? -16.663 51.068 48.480  1.00 29.00 ? 512  LYS B CE  1 
ATOM   9883  N  NZ  . LYS B  1 512 ? -16.431 51.235 47.026  1.00 28.64 ? 512  LYS B NZ  1 
ATOM   9884  N  N   . LYS B  1 513 ? -17.648 49.536 53.637  1.00 27.72 ? 513  LYS B N   1 
ATOM   9885  C  CA  . LYS B  1 513 ? -18.546 50.453 54.314  1.00 27.41 ? 513  LYS B CA  1 
ATOM   9886  C  C   . LYS B  1 513 ? -18.368 51.835 53.711  1.00 27.47 ? 513  LYS B C   1 
ATOM   9887  O  O   . LYS B  1 513 ? -17.242 52.267 53.477  1.00 26.15 ? 513  LYS B O   1 
ATOM   9888  C  CB  . LYS B  1 513 ? -18.228 50.514 55.806  1.00 28.63 ? 513  LYS B CB  1 
ATOM   9889  C  CG  . LYS B  1 513 ? -19.095 51.496 56.554  1.00 31.14 ? 513  LYS B CG  1 
ATOM   9890  C  CD  . LYS B  1 513 ? -18.677 51.613 58.004  1.00 34.00 ? 513  LYS B CD  1 
ATOM   9891  C  CE  . LYS B  1 513 ? -19.475 52.700 58.687  1.00 34.94 ? 513  LYS B CE  1 
ATOM   9892  N  NZ  . LYS B  1 513 ? -20.927 52.545 58.368  1.00 35.76 ? 513  LYS B NZ  1 
ATOM   9893  N  N   . LEU B  1 514 ? -19.481 52.519 53.451  1.00 26.94 ? 514  LEU B N   1 
ATOM   9894  C  CA  . LEU B  1 514 ? -19.462 53.866 52.883  1.00 26.66 ? 514  LEU B CA  1 
ATOM   9895  C  C   . LEU B  1 514 ? -20.295 54.723 53.822  1.00 27.40 ? 514  LEU B C   1 
ATOM   9896  O  O   . LEU B  1 514 ? -21.460 54.426 54.067  1.00 26.69 ? 514  LEU B O   1 
ATOM   9897  C  CB  . LEU B  1 514 ? -20.076 53.857 51.482  1.00 26.85 ? 514  LEU B CB  1 
ATOM   9898  C  CG  . LEU B  1 514 ? -20.298 55.231 50.843  1.00 27.06 ? 514  LEU B CG  1 
ATOM   9899  C  CD1 . LEU B  1 514 ? -18.954 55.929 50.640  1.00 26.10 ? 514  LEU B CD1 1 
ATOM   9900  C  CD2 . LEU B  1 514 ? -21.040 55.069 49.521  1.00 26.36 ? 514  LEU B CD2 1 
ATOM   9901  N  N   . ASP B  1 515 ? -19.708 55.792 54.346  1.00 27.93 ? 515  ASP B N   1 
ATOM   9902  C  CA  . ASP B  1 515 ? -20.418 56.631 55.304  1.00 29.07 ? 515  ASP B CA  1 
ATOM   9903  C  C   . ASP B  1 515 ? -19.715 57.988 55.349  1.00 29.73 ? 515  ASP B C   1 
ATOM   9904  O  O   . ASP B  1 515 ? -18.790 58.243 54.565  1.00 29.36 ? 515  ASP B O   1 
ATOM   9905  C  CB  . ASP B  1 515 ? -20.355 55.944 56.677  1.00 30.74 ? 515  ASP B CB  1 
ATOM   9906  C  CG  . ASP B  1 515 ? -21.514 56.325 57.608  1.00 32.32 ? 515  ASP B CG  1 
ATOM   9907  O  OD1 . ASP B  1 515 ? -21.584 55.722 58.704  1.00 33.53 ? 515  ASP B OD1 1 
ATOM   9908  O  OD2 . ASP B  1 515 ? -22.336 57.205 57.265  1.00 32.37 ? 515  ASP B OD2 1 
ATOM   9909  N  N   . PHE B  1 516 ? -20.141 58.851 56.265  1.00 29.85 ? 516  PHE B N   1 
ATOM   9910  C  CA  . PHE B  1 516 ? -19.537 60.167 56.379  1.00 30.73 ? 516  PHE B CA  1 
ATOM   9911  C  C   . PHE B  1 516 ? -19.305 60.571 57.822  1.00 31.59 ? 516  PHE B C   1 
ATOM   9912  O  O   . PHE B  1 516 ? -19.833 59.949 58.744  1.00 30.94 ? 516  PHE B O   1 
ATOM   9913  C  CB  . PHE B  1 516 ? -20.416 61.230 55.709  1.00 30.52 ? 516  PHE B CB  1 
ATOM   9914  C  CG  . PHE B  1 516 ? -21.800 61.352 56.305  1.00 31.59 ? 516  PHE B CG  1 
ATOM   9915  C  CD1 . PHE B  1 516 ? -22.839 60.538 55.858  1.00 31.82 ? 516  PHE B CD1 1 
ATOM   9916  C  CD2 . PHE B  1 516 ? -22.060 62.273 57.314  1.00 32.11 ? 516  PHE B CD2 1 
ATOM   9917  C  CE1 . PHE B  1 516 ? -24.126 60.634 56.405  1.00 32.15 ? 516  PHE B CE1 1 
ATOM   9918  C  CE2 . PHE B  1 516 ? -23.345 62.380 57.873  1.00 33.42 ? 516  PHE B CE2 1 
ATOM   9919  C  CZ  . PHE B  1 516 ? -24.381 61.552 57.411  1.00 32.42 ? 516  PHE B CZ  1 
ATOM   9920  N  N   . ILE B  1 517 ? -18.487 61.606 57.996  1.00 31.65 ? 517  ILE B N   1 
ATOM   9921  C  CA  . ILE B  1 517 ? -18.205 62.161 59.304  1.00 33.39 ? 517  ILE B CA  1 
ATOM   9922  C  C   . ILE B  1 517 ? -18.447 63.648 59.109  1.00 34.42 ? 517  ILE B C   1 
ATOM   9923  O  O   . ILE B  1 517 ? -18.244 64.179 58.007  1.00 34.60 ? 517  ILE B O   1 
ATOM   9924  C  CB  . ILE B  1 517 ? -16.748 61.961 59.755  1.00 33.28 ? 517  ILE B CB  1 
ATOM   9925  C  CG1 . ILE B  1 517 ? -15.815 62.714 58.816  1.00 33.75 ? 517  ILE B CG1 1 
ATOM   9926  C  CG2 . ILE B  1 517 ? -16.407 60.478 59.800  1.00 33.13 ? 517  ILE B CG2 1 
ATOM   9927  C  CD1 . ILE B  1 517 ? -14.536 63.156 59.474  1.00 35.26 ? 517  ILE B CD1 1 
ATOM   9928  N  N   . ILE B  1 518 ? -18.878 64.322 60.169  1.00 35.20 ? 518  ILE B N   1 
ATOM   9929  C  CA  . ILE B  1 518 ? -19.161 65.747 60.082  1.00 35.82 ? 518  ILE B CA  1 
ATOM   9930  C  C   . ILE B  1 518 ? -18.014 66.577 60.635  1.00 36.51 ? 518  ILE B C   1 
ATOM   9931  O  O   . ILE B  1 518 ? -17.585 66.355 61.759  1.00 37.18 ? 518  ILE B O   1 
ATOM   9932  C  CB  . ILE B  1 518 ? -20.445 66.096 60.867  1.00 36.41 ? 518  ILE B CB  1 
ATOM   9933  C  CG1 . ILE B  1 518 ? -21.627 65.308 60.297  1.00 36.37 ? 518  ILE B CG1 1 
ATOM   9934  C  CG2 . ILE B  1 518 ? -20.707 67.595 60.806  1.00 36.43 ? 518  ILE B CG2 1 
ATOM   9935  C  CD1 . ILE B  1 518 ? -22.959 65.569 60.999  1.00 38.42 ? 518  ILE B CD1 1 
ATOM   9936  N  N   . LEU B  1 519 ? -17.511 67.516 59.836  1.00 36.63 ? 519  LEU B N   1 
ATOM   9937  C  CA  . LEU B  1 519 ? -16.439 68.417 60.266  1.00 37.53 ? 519  LEU B CA  1 
ATOM   9938  C  C   . LEU B  1 519 ? -16.862 69.843 59.918  1.00 38.53 ? 519  LEU B C   1 
ATOM   9939  O  O   . LEU B  1 519 ? -17.306 70.103 58.802  1.00 38.84 ? 519  LEU B O   1 
ATOM   9940  C  CB  . LEU B  1 519 ? -15.124 68.092 59.557  1.00 37.11 ? 519  LEU B CB  1 
ATOM   9941  C  CG  . LEU B  1 519 ? -14.435 66.750 59.840  1.00 37.78 ? 519  LEU B CG  1 
ATOM   9942  C  CD1 . LEU B  1 519 ? -13.181 66.657 58.979  1.00 36.82 ? 519  LEU B CD1 1 
ATOM   9943  C  CD2 . LEU B  1 519 ? -14.075 66.627 61.322  1.00 37.22 ? 519  LEU B CD2 1 
ATOM   9944  N  N   . ASN B  1 520 ? -16.731 70.762 60.871  1.00 39.86 ? 520  ASN B N   1 
ATOM   9945  C  CA  . ASN B  1 520 ? -17.114 72.161 60.649  1.00 40.59 ? 520  ASN B CA  1 
ATOM   9946  C  C   . ASN B  1 520 ? -18.526 72.239 60.056  1.00 40.52 ? 520  ASN B C   1 
ATOM   9947  O  O   . ASN B  1 520 ? -18.791 73.041 59.158  1.00 40.61 ? 520  ASN B O   1 
ATOM   9948  C  CB  . ASN B  1 520 ? -16.106 72.850 59.713  1.00 42.14 ? 520  ASN B CB  1 
ATOM   9949  C  CG  . ASN B  1 520 ? -14.739 73.064 60.371  1.00 44.08 ? 520  ASN B CG  1 
ATOM   9950  O  OD1 . ASN B  1 520 ? -14.281 72.232 61.157  1.00 45.58 ? 520  ASN B OD1 1 
ATOM   9951  N  ND2 . ASN B  1 520 ? -14.076 74.173 60.035  1.00 44.98 ? 520  ASN B ND2 1 
ATOM   9952  N  N   . GLU B  1 521 ? -19.417 71.393 60.572  1.00 40.04 ? 521  GLU B N   1 
ATOM   9953  C  CA  . GLU B  1 521 ? -20.816 71.334 60.150  1.00 39.51 ? 521  GLU B CA  1 
ATOM   9954  C  C   . GLU B  1 521 ? -21.036 70.893 58.701  1.00 38.90 ? 521  GLU B C   1 
ATOM   9955  O  O   . GLU B  1 521 ? -22.122 71.051 58.140  1.00 38.37 ? 521  GLU B O   1 
ATOM   9956  C  CB  . GLU B  1 521 ? -21.524 72.678 60.403  1.00 41.34 ? 521  GLU B CB  1 
ATOM   9957  C  CG  . GLU B  1 521 ? -21.617 73.055 61.892  1.00 44.08 ? 521  GLU B CG  1 
ATOM   9958  C  CD  . GLU B  1 521 ? -22.774 74.011 62.218  1.00 46.10 ? 521  GLU B CD  1 
ATOM   9959  O  OE1 . GLU B  1 521 ? -22.911 74.388 63.408  1.00 46.71 ? 521  GLU B OE1 1 
ATOM   9960  O  OE2 . GLU B  1 521 ? -23.551 74.382 61.300  1.00 46.45 ? 521  GLU B OE2 1 
ATOM   9961  N  N   . THR B  1 522 ? -20.007 70.335 58.084  1.00 37.55 ? 522  THR B N   1 
ATOM   9962  C  CA  . THR B  1 522 ? -20.161 69.856 56.718  1.00 35.73 ? 522  THR B CA  1 
ATOM   9963  C  C   . THR B  1 522 ? -19.721 68.401 56.700  1.00 33.36 ? 522  THR B C   1 
ATOM   9964  O  O   . THR B  1 522 ? -18.762 68.028 57.367  1.00 33.18 ? 522  THR B O   1 
ATOM   9965  C  CB  . THR B  1 522 ? -19.353 70.730 55.720  1.00 36.03 ? 522  THR B CB  1 
ATOM   9966  O  OG1 . THR B  1 522 ? -18.861 69.914 54.648  1.00 38.25 ? 522  THR B OG1 1 
ATOM   9967  C  CG2 . THR B  1 522 ? -18.198 71.428 56.427  1.00 37.69 ? 522  THR B CG2 1 
ATOM   9968  N  N   . LYS B  1 523 ? -20.442 67.563 55.967  1.00 31.50 ? 523  LYS B N   1 
ATOM   9969  C  CA  . LYS B  1 523 ? -20.087 66.162 55.939  1.00 29.66 ? 523  LYS B CA  1 
ATOM   9970  C  C   . LYS B  1 523 ? -19.107 65.779 54.840  1.00 28.04 ? 523  LYS B C   1 
ATOM   9971  O  O   . LYS B  1 523 ? -19.184 66.244 53.702  1.00 26.14 ? 523  LYS B O   1 
ATOM   9972  C  CB  . LYS B  1 523 ? -21.334 65.295 55.836  1.00 32.08 ? 523  LYS B CB  1 
ATOM   9973  C  CG  . LYS B  1 523 ? -22.018 65.378 54.523  1.00 34.14 ? 523  LYS B CG  1 
ATOM   9974  C  CD  . LYS B  1 523 ? -23.134 64.349 54.428  1.00 36.82 ? 523  LYS B CD  1 
ATOM   9975  C  CE  . LYS B  1 523 ? -24.342 64.731 55.266  1.00 38.11 ? 523  LYS B CE  1 
ATOM   9976  N  NZ  . LYS B  1 523 ? -25.534 63.976 54.759  1.00 38.36 ? 523  LYS B NZ  1 
ATOM   9977  N  N   . PHE B  1 524 ? -18.183 64.913 55.216  1.00 26.32 ? 524  PHE B N   1 
ATOM   9978  C  CA  . PHE B  1 524 ? -17.176 64.411 54.309  1.00 24.77 ? 524  PHE B CA  1 
ATOM   9979  C  C   . PHE B  1 524 ? -17.280 62.907 54.343  1.00 23.81 ? 524  PHE B C   1 
ATOM   9980  O  O   . PHE B  1 524 ? -17.309 62.292 55.421  1.00 22.03 ? 524  PHE B O   1 
ATOM   9981  C  CB  . PHE B  1 524 ? -15.794 64.890 54.743  1.00 24.98 ? 524  PHE B CB  1 
ATOM   9982  C  CG  . PHE B  1 524 ? -15.618 66.382 54.635  1.00 25.88 ? 524  PHE B CG  1 
ATOM   9983  C  CD1 . PHE B  1 524 ? -15.853 67.209 55.730  1.00 26.16 ? 524  PHE B CD1 1 
ATOM   9984  C  CD2 . PHE B  1 524 ? -15.248 66.962 53.425  1.00 25.84 ? 524  PHE B CD2 1 
ATOM   9985  C  CE1 . PHE B  1 524 ? -15.723 68.581 55.620  1.00 25.72 ? 524  PHE B CE1 1 
ATOM   9986  C  CE2 . PHE B  1 524 ? -15.118 68.338 53.307  1.00 25.68 ? 524  PHE B CE2 1 
ATOM   9987  C  CZ  . PHE B  1 524 ? -15.356 69.149 54.408  1.00 26.54 ? 524  PHE B CZ  1 
ATOM   9988  N  N   . TRP B  1 525 ? -17.365 62.325 53.148  1.00 23.01 ? 525  TRP B N   1 
ATOM   9989  C  CA  . TRP B  1 525 ? -17.506 60.890 52.975  1.00 21.70 ? 525  TRP B CA  1 
ATOM   9990  C  C   . TRP B  1 525 ? -16.214 60.094 53.012  1.00 22.35 ? 525  TRP B C   1 
ATOM   9991  O  O   . TRP B  1 525 ? -15.129 60.595 52.705  1.00 22.01 ? 525  TRP B O   1 
ATOM   9992  C  CB  . TRP B  1 525 ? -18.243 60.620 51.658  1.00 20.98 ? 525  TRP B CB  1 
ATOM   9993  C  CG  . TRP B  1 525 ? -19.636 61.141 51.691  1.00 20.25 ? 525  TRP B CG  1 
ATOM   9994  C  CD1 . TRP B  1 525 ? -20.028 62.442 51.624  1.00 19.80 ? 525  TRP B CD1 1 
ATOM   9995  C  CD2 . TRP B  1 525 ? -20.822 60.369 51.906  1.00 20.62 ? 525  TRP B CD2 1 
ATOM   9996  N  NE1 . TRP B  1 525 ? -21.393 62.538 51.793  1.00 20.11 ? 525  TRP B NE1 1 
ATOM   9997  C  CE2 . TRP B  1 525 ? -21.905 61.277 51.969  1.00 21.15 ? 525  TRP B CE2 1 
ATOM   9998  C  CE3 . TRP B  1 525 ? -21.074 58.994 52.057  1.00 20.71 ? 525  TRP B CE3 1 
ATOM   9999  C  CZ2 . TRP B  1 525 ? -23.230 60.855 52.177  1.00 21.85 ? 525  TRP B CZ2 1 
ATOM   10000 C  CZ3 . TRP B  1 525 ? -22.392 58.571 52.265  1.00 20.96 ? 525  TRP B CZ3 1 
ATOM   10001 C  CH2 . TRP B  1 525 ? -23.452 59.505 52.322  1.00 22.35 ? 525  TRP B CH2 1 
ATOM   10002 N  N   . TYR B  1 526 ? -16.342 58.833 53.385  1.00 21.78 ? 526  TYR B N   1 
ATOM   10003 C  CA  . TYR B  1 526 ? -15.198 57.950 53.443  1.00 23.01 ? 526  TYR B CA  1 
ATOM   10004 C  C   . TYR B  1 526 ? -15.707 56.544 53.230  1.00 22.76 ? 526  TYR B C   1 
ATOM   10005 O  O   . TYR B  1 526 ? -16.916 56.279 53.334  1.00 22.54 ? 526  TYR B O   1 
ATOM   10006 C  CB  . TYR B  1 526 ? -14.495 58.050 54.807  1.00 23.93 ? 526  TYR B CB  1 
ATOM   10007 C  CG  . TYR B  1 526 ? -15.274 57.425 55.951  1.00 26.16 ? 526  TYR B CG  1 
ATOM   10008 C  CD1 . TYR B  1 526 ? -15.127 56.076 56.267  1.00 26.08 ? 526  TYR B CD1 1 
ATOM   10009 C  CD2 . TYR B  1 526 ? -16.200 58.175 56.677  1.00 26.44 ? 526  TYR B CD2 1 
ATOM   10010 C  CE1 . TYR B  1 526 ? -15.888 55.480 57.277  1.00 28.16 ? 526  TYR B CE1 1 
ATOM   10011 C  CE2 . TYR B  1 526 ? -16.974 57.595 57.692  1.00 28.01 ? 526  TYR B CE2 1 
ATOM   10012 C  CZ  . TYR B  1 526 ? -16.814 56.244 57.985  1.00 29.04 ? 526  TYR B CZ  1 
ATOM   10013 O  OH  . TYR B  1 526 ? -17.599 55.663 58.958  1.00 29.25 ? 526  TYR B OH  1 
ATOM   10014 N  N   . GLN B  1 527 ? -14.797 55.650 52.883  1.00 21.31 ? 527  GLN B N   1 
ATOM   10015 C  CA  . GLN B  1 527 ? -15.174 54.269 52.721  1.00 21.36 ? 527  GLN B CA  1 
ATOM   10016 C  C   . GLN B  1 527 ? -14.111 53.455 53.420  1.00 21.98 ? 527  GLN B C   1 
ATOM   10017 O  O   . GLN B  1 527 ? -12.992 53.935 53.627  1.00 22.48 ? 527  GLN B O   1 
ATOM   10018 C  CB  . GLN B  1 527 ? -15.251 53.875 51.251  1.00 20.85 ? 527  GLN B CB  1 
ATOM   10019 C  CG  . GLN B  1 527 ? -13.946 54.021 50.480  1.00 21.06 ? 527  GLN B CG  1 
ATOM   10020 C  CD  . GLN B  1 527 ? -14.065 53.487 49.059  1.00 21.92 ? 527  GLN B CD  1 
ATOM   10021 O  OE1 . GLN B  1 527 ? -15.022 53.810 48.346  1.00 20.49 ? 527  GLN B OE1 1 
ATOM   10022 N  NE2 . GLN B  1 527 ? -13.088 52.673 48.639  1.00 19.86 ? 527  GLN B NE2 1 
ATOM   10023 N  N   . MET B  1 528 ? -14.464 52.240 53.812  1.00 20.97 ? 528  MET B N   1 
ATOM   10024 C  CA  . MET B  1 528 ? -13.503 51.367 54.448  1.00 22.20 ? 528  MET B CA  1 
ATOM   10025 C  C   . MET B  1 528 ? -13.680 49.970 53.895  1.00 22.42 ? 528  MET B C   1 
ATOM   10026 O  O   . MET B  1 528 ? -14.809 49.489 53.761  1.00 22.79 ? 528  MET B O   1 
ATOM   10027 C  CB  . MET B  1 528 ? -13.700 51.312 55.968  1.00 22.11 ? 528  MET B CB  1 
ATOM   10028 C  CG  . MET B  1 528 ? -13.329 52.560 56.729  1.00 22.26 ? 528  MET B CG  1 
ATOM   10029 S  SD  . MET B  1 528 ? -13.466 52.243 58.515  1.00 25.17 ? 528  MET B SD  1 
ATOM   10030 C  CE  . MET B  1 528 ? -12.832 53.732 59.198  1.00 22.82 ? 528  MET B CE  1 
ATOM   10031 N  N   . ILE B  1 529 ? -12.572 49.337 53.533  1.00 22.32 ? 529  ILE B N   1 
ATOM   10032 C  CA  . ILE B  1 529 ? -12.609 47.967 53.074  1.00 22.86 ? 529  ILE B CA  1 
ATOM   10033 C  C   . ILE B  1 529 ? -12.271 47.251 54.381  1.00 24.02 ? 529  ILE B C   1 
ATOM   10034 O  O   . ILE B  1 529 ? -11.168 47.388 54.920  1.00 22.70 ? 529  ILE B O   1 
ATOM   10035 C  CB  . ILE B  1 529 ? -11.554 47.694 52.008  1.00 23.07 ? 529  ILE B CB  1 
ATOM   10036 C  CG1 . ILE B  1 529 ? -11.719 48.684 50.854  1.00 22.91 ? 529  ILE B CG1 1 
ATOM   10037 C  CG2 . ILE B  1 529 ? -11.703 46.265 51.495  1.00 22.27 ? 529  ILE B CG2 1 
ATOM   10038 C  CD1 . ILE B  1 529 ? -13.074 48.602 50.124  1.00 24.18 ? 529  ILE B CD1 1 
ATOM   10039 N  N   . LEU B  1 530 ? -13.248 46.515 54.905  1.00 25.11 ? 530  LEU B N   1 
ATOM   10040 C  CA  . LEU B  1 530 ? -13.105 45.827 56.190  1.00 25.07 ? 530  LEU B CA  1 
ATOM   10041 C  C   . LEU B  1 530 ? -12.831 44.321 56.052  1.00 25.77 ? 530  LEU B C   1 
ATOM   10042 O  O   . LEU B  1 530 ? -13.437 43.641 55.226  1.00 26.05 ? 530  LEU B O   1 
ATOM   10043 C  CB  . LEU B  1 530 ? -14.382 46.076 57.015  1.00 24.60 ? 530  LEU B CB  1 
ATOM   10044 C  CG  . LEU B  1 530 ? -14.821 47.537 57.255  1.00 25.27 ? 530  LEU B CG  1 
ATOM   10045 C  CD1 . LEU B  1 530 ? -16.281 47.602 57.782  1.00 25.02 ? 530  LEU B CD1 1 
ATOM   10046 C  CD2 . LEU B  1 530 ? -13.874 48.202 58.237  1.00 24.37 ? 530  LEU B CD2 1 
ATOM   10047 N  N   . PRO B  1 531 ? -11.904 43.780 56.865  1.00 26.38 ? 531  PRO B N   1 
ATOM   10048 C  CA  . PRO B  1 531 ? -11.564 42.353 56.819  1.00 26.84 ? 531  PRO B CA  1 
ATOM   10049 C  C   . PRO B  1 531 ? -12.782 41.478 57.084  1.00 28.03 ? 531  PRO B C   1 
ATOM   10050 O  O   . PRO B  1 531 ? -13.743 41.911 57.715  1.00 28.40 ? 531  PRO B O   1 
ATOM   10051 C  CB  . PRO B  1 531 ? -10.545 42.198 57.948  1.00 27.29 ? 531  PRO B CB  1 
ATOM   10052 C  CG  . PRO B  1 531 ? -9.893  43.545 58.010  1.00 27.56 ? 531  PRO B CG  1 
ATOM   10053 C  CD  . PRO B  1 531 ? -11.078 44.484 57.861  1.00 26.53 ? 531  PRO B CD  1 
ATOM   10054 N  N   . PRO B  1 532 ? -12.752 40.231 56.617  1.00 29.27 ? 532  PRO B N   1 
ATOM   10055 C  CA  . PRO B  1 532 ? -13.874 39.317 56.836  1.00 30.74 ? 532  PRO B CA  1 
ATOM   10056 C  C   . PRO B  1 532 ? -14.132 39.233 58.338  1.00 32.21 ? 532  PRO B C   1 
ATOM   10057 O  O   . PRO B  1 532 ? -13.222 39.456 59.139  1.00 31.47 ? 532  PRO B O   1 
ATOM   10058 C  CB  . PRO B  1 532 ? -13.340 37.992 56.315  1.00 30.96 ? 532  PRO B CB  1 
ATOM   10059 C  CG  . PRO B  1 532 ? -12.362 38.396 55.267  1.00 31.10 ? 532  PRO B CG  1 
ATOM   10060 C  CD  . PRO B  1 532 ? -11.660 39.568 55.886  1.00 29.76 ? 532  PRO B CD  1 
ATOM   10061 N  N   . HIS B  1 533 ? -15.364 38.939 58.728  1.00 33.26 ? 533  HIS B N   1 
ATOM   10062 C  CA  . HIS B  1 533 ? -15.660 38.794 60.151  1.00 34.20 ? 533  HIS B CA  1 
ATOM   10063 C  C   . HIS B  1 533 ? -15.150 39.955 60.979  1.00 34.82 ? 533  HIS B C   1 
ATOM   10064 O  O   . HIS B  1 533 ? -14.630 39.759 62.077  1.00 34.58 ? 533  HIS B O   1 
ATOM   10065 C  CB  . HIS B  1 533 ? -15.026 37.502 60.657  1.00 34.75 ? 533  HIS B CB  1 
ATOM   10066 C  CG  . HIS B  1 533 ? -15.352 36.319 59.805  1.00 36.26 ? 533  HIS B CG  1 
ATOM   10067 N  ND1 . HIS B  1 533 ? -14.387 35.497 59.265  1.00 37.06 ? 533  HIS B ND1 1 
ATOM   10068 C  CD2 . HIS B  1 533 ? -16.542 35.840 59.368  1.00 36.86 ? 533  HIS B CD2 1 
ATOM   10069 C  CE1 . HIS B  1 533 ? -14.968 34.561 58.532  1.00 36.83 ? 533  HIS B CE1 1 
ATOM   10070 N  NE2 . HIS B  1 533 ? -16.274 34.747 58.579  1.00 37.58 ? 533  HIS B NE2 1 
ATOM   10071 N  N   . PHE B  1 534 ? -15.304 41.165 60.452  1.00 34.68 ? 534  PHE B N   1 
ATOM   10072 C  CA  . PHE B  1 534 ? -14.855 42.362 61.145  1.00 35.50 ? 534  PHE B CA  1 
ATOM   10073 C  C   . PHE B  1 534 ? -15.439 42.457 62.557  1.00 36.31 ? 534  PHE B C   1 
ATOM   10074 O  O   . PHE B  1 534 ? -16.645 42.305 62.755  1.00 36.84 ? 534  PHE B O   1 
ATOM   10075 C  CB  . PHE B  1 534 ? -15.255 43.599 60.340  1.00 35.24 ? 534  PHE B CB  1 
ATOM   10076 C  CG  . PHE B  1 534 ? -14.889 44.892 60.999  1.00 36.01 ? 534  PHE B CG  1 
ATOM   10077 C  CD1 . PHE B  1 534 ? -13.556 45.239 61.181  1.00 35.99 ? 534  PHE B CD1 1 
ATOM   10078 C  CD2 . PHE B  1 534 ? -15.877 45.759 61.450  1.00 36.65 ? 534  PHE B CD2 1 
ATOM   10079 C  CE1 . PHE B  1 534 ? -13.211 46.424 61.800  1.00 36.47 ? 534  PHE B CE1 1 
ATOM   10080 C  CE2 . PHE B  1 534 ? -15.538 46.951 62.072  1.00 37.36 ? 534  PHE B CE2 1 
ATOM   10081 C  CZ  . PHE B  1 534 ? -14.197 47.285 62.248  1.00 36.64 ? 534  PHE B CZ  1 
ATOM   10082 N  N   . ASP B  1 535 ? -14.583 42.715 63.536  1.00 36.41 ? 535  ASP B N   1 
ATOM   10083 C  CA  . ASP B  1 535 ? -15.032 42.836 64.916  1.00 36.94 ? 535  ASP B CA  1 
ATOM   10084 C  C   . ASP B  1 535 ? -14.644 44.196 65.461  1.00 37.04 ? 535  ASP B C   1 
ATOM   10085 O  O   . ASP B  1 535 ? -13.463 44.480 65.666  1.00 36.94 ? 535  ASP B O   1 
ATOM   10086 C  CB  . ASP B  1 535 ? -14.406 41.743 65.773  1.00 36.93 ? 535  ASP B CB  1 
ATOM   10087 C  CG  . ASP B  1 535 ? -14.864 41.807 67.213  1.00 37.81 ? 535  ASP B CG  1 
ATOM   10088 O  OD1 . ASP B  1 535 ? -14.625 40.830 67.942  1.00 39.33 ? 535  ASP B OD1 1 
ATOM   10089 O  OD2 . ASP B  1 535 ? -15.456 42.830 67.620  1.00 38.34 ? 535  ASP B OD2 1 
ATOM   10090 N  N   . LYS B  1 536 ? -15.637 45.035 65.725  1.00 37.37 ? 536  LYS B N   1 
ATOM   10091 C  CA  . LYS B  1 536 ? -15.347 46.376 66.210  1.00 38.89 ? 536  LYS B CA  1 
ATOM   10092 C  C   . LYS B  1 536 ? -14.749 46.484 67.610  1.00 38.74 ? 536  LYS B C   1 
ATOM   10093 O  O   . LYS B  1 536 ? -14.406 47.579 68.056  1.00 37.90 ? 536  LYS B O   1 
ATOM   10094 C  CB  . LYS B  1 536 ? -16.598 47.242 66.096  1.00 40.91 ? 536  LYS B CB  1 
ATOM   10095 C  CG  . LYS B  1 536 ? -17.886 46.549 66.526  1.00 43.23 ? 536  LYS B CG  1 
ATOM   10096 C  CD  . LYS B  1 536 ? -19.077 47.139 65.761  1.00 45.19 ? 536  LYS B CD  1 
ATOM   10097 C  CE  . LYS B  1 536 ? -18.981 48.666 65.675  1.00 45.47 ? 536  LYS B CE  1 
ATOM   10098 N  NZ  . LYS B  1 536 ? -18.813 49.261 67.027  1.00 46.07 ? 536  LYS B NZ  1 
ATOM   10099 N  N   . SER B  1 537 ? -14.608 45.352 68.293  1.00 38.63 ? 537  SER B N   1 
ATOM   10100 C  CA  . SER B  1 537 ? -14.028 45.354 69.634  1.00 39.63 ? 537  SER B CA  1 
ATOM   10101 C  C   . SER B  1 537 ? -12.517 45.125 69.513  1.00 39.53 ? 537  SER B C   1 
ATOM   10102 O  O   . SER B  1 537 ? -11.802 45.105 70.516  1.00 40.09 ? 537  SER B O   1 
ATOM   10103 C  CB  . SER B  1 537 ? -14.636 44.239 70.489  1.00 39.46 ? 537  SER B CB  1 
ATOM   10104 O  OG  . SER B  1 537 ? -14.023 42.998 70.183  1.00 41.11 ? 537  SER B OG  1 
ATOM   10105 N  N   . LYS B  1 538 ? -12.041 44.938 68.282  1.00 38.82 ? 538  LYS B N   1 
ATOM   10106 C  CA  . LYS B  1 538 ? -10.622 44.714 68.043  1.00 37.14 ? 538  LYS B CA  1 
ATOM   10107 C  C   . LYS B  1 538 ? -9.924  45.942 67.466  1.00 36.19 ? 538  LYS B C   1 
ATOM   10108 O  O   . LYS B  1 538 ? -10.566 46.881 66.986  1.00 35.31 ? 538  LYS B O   1 
ATOM   10109 C  CB  . LYS B  1 538 ? -10.436 43.517 67.110  1.00 38.40 ? 538  LYS B CB  1 
ATOM   10110 C  CG  . LYS B  1 538 ? -11.089 42.250 67.639  1.00 39.92 ? 538  LYS B CG  1 
ATOM   10111 C  CD  . LYS B  1 538 ? -10.594 41.014 66.909  1.00 41.24 ? 538  LYS B CD  1 
ATOM   10112 C  CE  . LYS B  1 538 ? -11.246 39.753 67.455  1.00 42.48 ? 538  LYS B CE  1 
ATOM   10113 N  NZ  . LYS B  1 538 ? -10.479 38.522 67.070  1.00 42.73 ? 538  LYS B NZ  1 
ATOM   10114 N  N   . LYS B  1 539 ? -8.600  45.934 67.532  1.00 34.80 ? 539  LYS B N   1 
ATOM   10115 C  CA  . LYS B  1 539 ? -7.807  47.035 67.012  1.00 34.13 ? 539  LYS B CA  1 
ATOM   10116 C  C   . LYS B  1 539 ? -7.118  46.518 65.750  1.00 32.66 ? 539  LYS B C   1 
ATOM   10117 O  O   . LYS B  1 539 ? -6.210  45.698 65.830  1.00 32.34 ? 539  LYS B O   1 
ATOM   10118 C  CB  . LYS B  1 539 ? -6.762  47.455 68.047  1.00 35.20 ? 539  LYS B CB  1 
ATOM   10119 C  CG  . LYS B  1 539 ? -7.339  47.950 69.361  1.00 36.48 ? 539  LYS B CG  1 
ATOM   10120 C  CD  . LYS B  1 539 ? -7.966  49.311 69.192  1.00 38.24 ? 539  LYS B CD  1 
ATOM   10121 C  CE  . LYS B  1 539 ? -8.438  49.882 70.515  1.00 38.79 ? 539  LYS B CE  1 
ATOM   10122 N  NZ  . LYS B  1 539 ? -8.983  51.258 70.323  1.00 39.87 ? 539  LYS B NZ  1 
ATOM   10123 N  N   . TYR B  1 540 ? -7.560  46.980 64.586  1.00 31.10 ? 540  TYR B N   1 
ATOM   10124 C  CA  . TYR B  1 540 ? -6.972  46.531 63.323  1.00 29.46 ? 540  TYR B CA  1 
ATOM   10125 C  C   . TYR B  1 540 ? -5.968  47.558 62.820  1.00 28.25 ? 540  TYR B C   1 
ATOM   10126 O  O   . TYR B  1 540 ? -6.080  48.750 63.113  1.00 27.48 ? 540  TYR B O   1 
ATOM   10127 C  CB  . TYR B  1 540 ? -8.054  46.380 62.242  1.00 29.86 ? 540  TYR B CB  1 
ATOM   10128 C  CG  . TYR B  1 540 ? -9.066  45.286 62.468  1.00 29.96 ? 540  TYR B CG  1 
ATOM   10129 C  CD1 . TYR B  1 540 ? -8.948  44.058 61.823  1.00 30.42 ? 540  TYR B CD1 1 
ATOM   10130 C  CD2 . TYR B  1 540 ? -10.142 45.476 63.330  1.00 31.21 ? 540  TYR B CD2 1 
ATOM   10131 C  CE1 . TYR B  1 540 ? -9.884  43.034 62.033  1.00 30.71 ? 540  TYR B CE1 1 
ATOM   10132 C  CE2 . TYR B  1 540 ? -11.082 44.458 63.552  1.00 31.13 ? 540  TYR B CE2 1 
ATOM   10133 C  CZ  . TYR B  1 540 ? -10.947 43.247 62.905  1.00 30.60 ? 540  TYR B CZ  1 
ATOM   10134 O  OH  . TYR B  1 540 ? -11.865 42.246 63.148  1.00 31.62 ? 540  TYR B OH  1 
ATOM   10135 N  N   . PRO B  1 541 ? -4.945  47.104 62.088  1.00 27.20 ? 541  PRO B N   1 
ATOM   10136 C  CA  . PRO B  1 541 ? -3.994  48.098 61.577  1.00 26.83 ? 541  PRO B CA  1 
ATOM   10137 C  C   . PRO B  1 541 ? -4.760  48.814 60.458  1.00 25.96 ? 541  PRO B C   1 
ATOM   10138 O  O   . PRO B  1 541 ? -5.676  48.224 59.875  1.00 25.39 ? 541  PRO B O   1 
ATOM   10139 C  CB  . PRO B  1 541 ? -2.839  47.239 61.064  1.00 26.35 ? 541  PRO B CB  1 
ATOM   10140 C  CG  . PRO B  1 541 ? -3.508  45.946 60.714  1.00 27.17 ? 541  PRO B CG  1 
ATOM   10141 C  CD  . PRO B  1 541 ? -4.465  45.736 61.845  1.00 27.02 ? 541  PRO B CD  1 
ATOM   10142 N  N   . LEU B  1 542 ? -4.435  50.072 60.168  1.00 25.75 ? 542  LEU B N   1 
ATOM   10143 C  CA  . LEU B  1 542 ? -5.162  50.784 59.112  1.00 25.28 ? 542  LEU B CA  1 
ATOM   10144 C  C   . LEU B  1 542 ? -4.279  51.398 58.019  1.00 24.53 ? 542  LEU B C   1 
ATOM   10145 O  O   . LEU B  1 542 ? -3.265  52.035 58.315  1.00 23.61 ? 542  LEU B O   1 
ATOM   10146 C  CB  . LEU B  1 542 ? -6.034  51.883 59.725  1.00 26.63 ? 542  LEU B CB  1 
ATOM   10147 C  CG  . LEU B  1 542 ? -7.107  52.511 58.826  1.00 28.39 ? 542  LEU B CG  1 
ATOM   10148 C  CD1 . LEU B  1 542 ? -8.250  53.025 59.684  1.00 30.50 ? 542  LEU B CD1 1 
ATOM   10149 C  CD2 . LEU B  1 542 ? -6.514  53.638 58.006  1.00 29.15 ? 542  LEU B CD2 1 
ATOM   10150 N  N   . LEU B  1 543 ? -4.668  51.181 56.762  1.00 22.27 ? 543  LEU B N   1 
ATOM   10151 C  CA  . LEU B  1 543 ? -3.953  51.743 55.614  1.00 21.47 ? 543  LEU B CA  1 
ATOM   10152 C  C   . LEU B  1 543 ? -4.852  52.791 54.949  1.00 20.78 ? 543  LEU B C   1 
ATOM   10153 O  O   . LEU B  1 543 ? -5.965  52.487 54.498  1.00 21.02 ? 543  LEU B O   1 
ATOM   10154 C  CB  . LEU B  1 543 ? -3.583  50.661 54.583  1.00 20.23 ? 543  LEU B CB  1 
ATOM   10155 C  CG  . LEU B  1 543 ? -2.969  51.175 53.260  1.00 18.57 ? 543  LEU B CG  1 
ATOM   10156 C  CD1 . LEU B  1 543 ? -1.673  51.966 53.528  1.00 19.27 ? 543  LEU B CD1 1 
ATOM   10157 C  CD2 . LEU B  1 543 ? -2.677  50.019 52.334  1.00 18.18 ? 543  LEU B CD2 1 
ATOM   10158 N  N   . LEU B  1 544 ? -4.386  54.032 54.931  1.00 19.66 ? 544  LEU B N   1 
ATOM   10159 C  CA  . LEU B  1 544 ? -5.145  55.102 54.302  1.00 20.42 ? 544  LEU B CA  1 
ATOM   10160 C  C   . LEU B  1 544 ? -4.745  55.130 52.823  1.00 20.58 ? 544  LEU B C   1 
ATOM   10161 O  O   . LEU B  1 544 ? -3.600  55.451 52.496  1.00 20.87 ? 544  LEU B O   1 
ATOM   10162 C  CB  . LEU B  1 544 ? -4.813  56.434 54.967  1.00 21.28 ? 544  LEU B CB  1 
ATOM   10163 C  CG  . LEU B  1 544 ? -5.654  57.634 54.562  1.00 21.37 ? 544  LEU B CG  1 
ATOM   10164 C  CD1 . LEU B  1 544 ? -7.114  57.341 54.850  1.00 23.02 ? 544  LEU B CD1 1 
ATOM   10165 C  CD2 . LEU B  1 544 ? -5.203  58.870 55.330  1.00 23.34 ? 544  LEU B CD2 1 
ATOM   10166 N  N   . ASP B  1 545 ? -5.679  54.765 51.945  1.00 19.33 ? 545  ASP B N   1 
ATOM   10167 C  CA  . ASP B  1 545 ? -5.470  54.740 50.486  1.00 19.41 ? 545  ASP B CA  1 
ATOM   10168 C  C   . ASP B  1 545 ? -5.898  56.138 50.001  1.00 20.42 ? 545  ASP B C   1 
ATOM   10169 O  O   . ASP B  1 545 ? -7.081  56.479 50.031  1.00 19.42 ? 545  ASP B O   1 
ATOM   10170 C  CB  . ASP B  1 545 ? -6.353  53.641 49.893  1.00 20.05 ? 545  ASP B CB  1 
ATOM   10171 C  CG  . ASP B  1 545 ? -6.327  53.587 48.376  1.00 21.04 ? 545  ASP B CG  1 
ATOM   10172 O  OD1 . ASP B  1 545 ? -5.935  54.566 47.715  1.00 22.18 ? 545  ASP B OD1 1 
ATOM   10173 O  OD2 . ASP B  1 545 ? -6.731  52.537 47.844  1.00 22.84 ? 545  ASP B OD2 1 
ATOM   10174 N  N   . VAL B  1 546 ? -4.945  56.945 49.544  1.00 19.51 ? 546  VAL B N   1 
ATOM   10175 C  CA  . VAL B  1 546 ? -5.292  58.301 49.156  1.00 19.80 ? 546  VAL B CA  1 
ATOM   10176 C  C   . VAL B  1 546 ? -4.960  58.730 47.734  1.00 18.85 ? 546  VAL B C   1 
ATOM   10177 O  O   . VAL B  1 546 ? -4.039  58.195 47.099  1.00 18.26 ? 546  VAL B O   1 
ATOM   10178 C  CB  . VAL B  1 546 ? -4.643  59.301 50.171  1.00 21.61 ? 546  VAL B CB  1 
ATOM   10179 C  CG1 . VAL B  1 546 ? -3.156  59.070 50.232  1.00 22.29 ? 546  VAL B CG1 1 
ATOM   10180 C  CG2 . VAL B  1 546 ? -4.936  60.746 49.789  1.00 23.26 ? 546  VAL B CG2 1 
ATOM   10181 N  N   . TYR B  1 547 ? -5.764  59.665 47.228  1.00 18.38 ? 547  TYR B N   1 
ATOM   10182 C  CA  . TYR B  1 547 ? -5.536  60.289 45.921  1.00 17.75 ? 547  TYR B CA  1 
ATOM   10183 C  C   . TYR B  1 547 ? -5.685  61.783 46.236  1.00 17.88 ? 547  TYR B C   1 
ATOM   10184 O  O   . TYR B  1 547 ? -4.701  62.529 46.231  1.00 17.95 ? 547  TYR B O   1 
ATOM   10185 C  CB  . TYR B  1 547 ? -6.539  59.841 44.849  1.00 16.34 ? 547  TYR B CB  1 
ATOM   10186 C  CG  . TYR B  1 547 ? -6.172  60.462 43.516  1.00 14.66 ? 547  TYR B CG  1 
ATOM   10187 C  CD1 . TYR B  1 547 ? -6.821  61.602 43.059  1.00 15.71 ? 547  TYR B CD1 1 
ATOM   10188 C  CD2 . TYR B  1 547 ? -5.058  60.004 42.792  1.00 15.82 ? 547  TYR B CD2 1 
ATOM   10189 C  CE1 . TYR B  1 547 ? -6.375  62.293 41.925  1.00 15.68 ? 547  TYR B CE1 1 
ATOM   10190 C  CE2 . TYR B  1 547 ? -4.598  60.685 41.645  1.00 15.07 ? 547  TYR B CE2 1 
ATOM   10191 C  CZ  . TYR B  1 547 ? -5.265  61.836 41.229  1.00 16.81 ? 547  TYR B CZ  1 
ATOM   10192 O  OH  . TYR B  1 547 ? -4.806  62.566 40.156  1.00 18.34 ? 547  TYR B OH  1 
ATOM   10193 N  N   . ALA B  1 548 ? -6.917  62.201 46.521  1.00 17.68 ? 548  ALA B N   1 
ATOM   10194 C  CA  . ALA B  1 548 ? -7.220  63.568 46.947  1.00 17.25 ? 548  ALA B CA  1 
ATOM   10195 C  C   . ALA B  1 548 ? -6.910  64.763 46.038  1.00 17.98 ? 548  ALA B C   1 
ATOM   10196 O  O   . ALA B  1 548 ? -6.808  65.891 46.527  1.00 17.66 ? 548  ALA B O   1 
ATOM   10197 C  CB  . ALA B  1 548 ? -6.571  63.804 48.331  1.00 16.05 ? 548  ALA B CB  1 
ATOM   10198 N  N   . GLY B  1 549 ? -6.772  64.537 44.738  1.00 17.55 ? 549  GLY B N   1 
ATOM   10199 C  CA  . GLY B  1 549 ? -6.526  65.654 43.844  1.00 17.94 ? 549  GLY B CA  1 
ATOM   10200 C  C   . GLY B  1 549 ? -7.803  66.475 43.666  1.00 17.30 ? 549  GLY B C   1 
ATOM   10201 O  O   . GLY B  1 549 ? -8.865  66.055 44.126  1.00 18.01 ? 549  GLY B O   1 
ATOM   10202 N  N   . PRO B  1 550 ? -7.746  67.642 42.999  1.00 16.30 ? 550  PRO B N   1 
ATOM   10203 C  CA  . PRO B  1 550 ? -8.934  68.482 42.794  1.00 15.97 ? 550  PRO B CA  1 
ATOM   10204 C  C   . PRO B  1 550 ? -10.025 67.753 42.008  1.00 16.71 ? 550  PRO B C   1 
ATOM   10205 O  O   . PRO B  1 550 ? -9.777  67.186 40.934  1.00 14.90 ? 550  PRO B O   1 
ATOM   10206 C  CB  . PRO B  1 550 ? -8.378  69.708 42.075  1.00 15.35 ? 550  PRO B CB  1 
ATOM   10207 C  CG  . PRO B  1 550 ? -7.208  69.142 41.299  1.00 15.58 ? 550  PRO B CG  1 
ATOM   10208 C  CD  . PRO B  1 550 ? -6.576  68.197 42.291  1.00 16.41 ? 550  PRO B CD  1 
ATOM   10209 N  N   . CYS B  1 551 ? -11.234 67.785 42.573  1.00 16.41 ? 551  CYS B N   1 
ATOM   10210 C  CA  . CYS B  1 551 ? -12.412 67.111 42.029  1.00 17.35 ? 551  CYS B CA  1 
ATOM   10211 C  C   . CYS B  1 551 ? -12.292 65.587 42.058  1.00 17.59 ? 551  CYS B C   1 
ATOM   10212 O  O   . CYS B  1 551 ? -12.968 64.900 41.300  1.00 18.59 ? 551  CYS B O   1 
ATOM   10213 C  CB  . CYS B  1 551 ? -12.714 67.570 40.605  1.00 17.40 ? 551  CYS B CB  1 
ATOM   10214 S  SG  . CYS B  1 551 ? -14.477 67.184 40.080  1.00 18.61 ? 551  CYS B SG  1 
ATOM   10215 N  N   . SER B  1 552 ? -11.441 65.052 42.934  1.00 16.91 ? 552  SER B N   1 
ATOM   10216 C  CA  . SER B  1 552 ? -11.323 63.601 43.035  1.00 15.85 ? 552  SER B CA  1 
ATOM   10217 C  C   . SER B  1 552 ? -12.473 63.023 43.887  1.00 16.25 ? 552  SER B C   1 
ATOM   10218 O  O   . SER B  1 552 ? -13.200 63.764 44.568  1.00 15.77 ? 552  SER B O   1 
ATOM   10219 C  CB  . SER B  1 552 ? -9.980  63.198 43.668  1.00 17.12 ? 552  SER B CB  1 
ATOM   10220 O  OG  . SER B  1 552 ? -9.857  63.639 45.020  1.00 17.44 ? 552  SER B OG  1 
ATOM   10221 N  N   . GLN B  1 553 ? -12.644 61.708 43.809  1.00 15.11 ? 553  GLN B N   1 
ATOM   10222 C  CA  . GLN B  1 553 ? -13.639 60.998 44.604  1.00 15.60 ? 553  GLN B CA  1 
ATOM   10223 C  C   . GLN B  1 553 ? -13.113 59.607 44.863  1.00 16.01 ? 553  GLN B C   1 
ATOM   10224 O  O   . GLN B  1 553 ? -12.997 58.808 43.942  1.00 15.45 ? 553  GLN B O   1 
ATOM   10225 C  CB  . GLN B  1 553 ? -15.002 60.877 43.906  1.00 16.27 ? 553  GLN B CB  1 
ATOM   10226 C  CG  . GLN B  1 553 ? -16.052 60.167 44.780  1.00 16.62 ? 553  GLN B CG  1 
ATOM   10227 C  CD  . GLN B  1 553 ? -17.479 60.337 44.261  1.00 18.10 ? 553  GLN B CD  1 
ATOM   10228 O  OE1 . GLN B  1 553 ? -17.880 59.696 43.304  1.00 18.91 ? 553  GLN B OE1 1 
ATOM   10229 N  NE2 . GLN B  1 553 ? -18.236 61.214 44.896  1.00 19.44 ? 553  GLN B NE2 1 
ATOM   10230 N  N   . LYS B  1 554 ? -12.781 59.317 46.120  1.00 16.92 ? 554  LYS B N   1 
ATOM   10231 C  CA  . LYS B  1 554 ? -12.278 57.986 46.483  1.00 17.15 ? 554  LYS B CA  1 
ATOM   10232 C  C   . LYS B  1 554 ? -13.255 57.224 47.397  1.00 17.51 ? 554  LYS B C   1 
ATOM   10233 O  O   . LYS B  1 554 ? -12.958 56.132 47.854  1.00 18.39 ? 554  LYS B O   1 
ATOM   10234 C  CB  . LYS B  1 554 ? -10.904 58.109 47.159  1.00 16.77 ? 554  LYS B CB  1 
ATOM   10235 C  CG  . LYS B  1 554 ? -9.794  58.504 46.199  1.00 16.62 ? 554  LYS B CG  1 
ATOM   10236 C  CD  . LYS B  1 554 ? -9.237  57.286 45.452  1.00 15.27 ? 554  LYS B CD  1 
ATOM   10237 C  CE  . LYS B  1 554 ? -8.289  56.503 46.359  1.00 16.71 ? 554  LYS B CE  1 
ATOM   10238 N  NZ  . LYS B  1 554 ? -7.832  55.212 45.760  1.00 16.66 ? 554  LYS B NZ  1 
ATOM   10239 N  N   . ALA B  1 555 ? -14.405 57.820 47.681  1.00 18.28 ? 555  ALA B N   1 
ATOM   10240 C  CA  . ALA B  1 555 ? -15.420 57.165 48.508  1.00 19.06 ? 555  ALA B CA  1 
ATOM   10241 C  C   . ALA B  1 555 ? -16.640 57.061 47.604  1.00 18.33 ? 555  ALA B C   1 
ATOM   10242 O  O   . ALA B  1 555 ? -17.300 58.063 47.330  1.00 18.37 ? 555  ALA B O   1 
ATOM   10243 C  CB  . ALA B  1 555 ? -15.743 58.001 49.732  1.00 18.03 ? 555  ALA B CB  1 
ATOM   10244 N  N   . ASP B  1 556 ? -16.911 55.859 47.113  1.00 18.93 ? 556  ASP B N   1 
ATOM   10245 C  CA  . ASP B  1 556 ? -18.046 55.643 46.224  1.00 19.90 ? 556  ASP B CA  1 
ATOM   10246 C  C   . ASP B  1 556 ? -18.639 54.238 46.397  1.00 20.30 ? 556  ASP B C   1 
ATOM   10247 O  O   . ASP B  1 556 ? -18.171 53.444 47.212  1.00 19.83 ? 556  ASP B O   1 
ATOM   10248 C  CB  . ASP B  1 556 ? -17.641 55.877 44.755  1.00 19.71 ? 556  ASP B CB  1 
ATOM   10249 C  CG  . ASP B  1 556 ? -16.529 54.938 44.280  1.00 20.48 ? 556  ASP B CG  1 
ATOM   10250 O  OD1 . ASP B  1 556 ? -16.468 53.770 44.730  1.00 20.97 ? 556  ASP B OD1 1 
ATOM   10251 O  OD2 . ASP B  1 556 ? -15.718 55.367 43.430  1.00 23.10 ? 556  ASP B OD2 1 
ATOM   10252 N  N   . THR B  1 557 ? -19.654 53.932 45.602  1.00 20.40 ? 557  THR B N   1 
ATOM   10253 C  CA  . THR B  1 557 ? -20.352 52.660 45.697  1.00 20.10 ? 557  THR B CA  1 
ATOM   10254 C  C   . THR B  1 557 ? -19.899 51.607 44.685  1.00 20.40 ? 557  THR B C   1 
ATOM   10255 O  O   . THR B  1 557 ? -20.561 50.595 44.504  1.00 20.50 ? 557  THR B O   1 
ATOM   10256 C  CB  . THR B  1 557 ? -21.871 52.893 45.541  1.00 20.93 ? 557  THR B CB  1 
ATOM   10257 O  OG1 . THR B  1 557 ? -22.129 53.496 44.265  1.00 21.06 ? 557  THR B OG1 1 
ATOM   10258 C  CG2 . THR B  1 557 ? -22.391 53.836 46.645  1.00 19.30 ? 557  THR B CG2 1 
ATOM   10259 N  N   . VAL B  1 558 ? -18.760 51.828 44.041  1.00 20.79 ? 558  VAL B N   1 
ATOM   10260 C  CA  . VAL B  1 558 ? -18.259 50.890 43.043  1.00 19.99 ? 558  VAL B CA  1 
ATOM   10261 C  C   . VAL B  1 558 ? -17.644 49.622 43.662  1.00 21.36 ? 558  VAL B C   1 
ATOM   10262 O  O   . VAL B  1 558 ? -16.961 49.686 44.696  1.00 20.67 ? 558  VAL B O   1 
ATOM   10263 C  CB  . VAL B  1 558 ? -17.197 51.578 42.165  1.00 20.39 ? 558  VAL B CB  1 
ATOM   10264 C  CG1 . VAL B  1 558 ? -16.566 50.562 41.186  1.00 18.13 ? 558  VAL B CG1 1 
ATOM   10265 C  CG2 . VAL B  1 558 ? -17.828 52.745 41.416  1.00 18.47 ? 558  VAL B CG2 1 
ATOM   10266 N  N   . PHE B  1 559 ? -17.904 48.473 43.033  1.00 20.98 ? 559  PHE B N   1 
ATOM   10267 C  CA  . PHE B  1 559 ? -17.354 47.194 43.493  1.00 22.18 ? 559  PHE B CA  1 
ATOM   10268 C  C   . PHE B  1 559 ? -15.987 46.980 42.864  1.00 21.57 ? 559  PHE B C   1 
ATOM   10269 O  O   . PHE B  1 559 ? -15.874 46.950 41.644  1.00 21.22 ? 559  PHE B O   1 
ATOM   10270 C  CB  . PHE B  1 559 ? -18.259 46.029 43.078  1.00 23.36 ? 559  PHE B CB  1 
ATOM   10271 C  CG  . PHE B  1 559 ? -17.671 44.668 43.366  1.00 24.96 ? 559  PHE B CG  1 
ATOM   10272 C  CD1 . PHE B  1 559 ? -17.788 44.096 44.626  1.00 25.54 ? 559  PHE B CD1 1 
ATOM   10273 C  CD2 . PHE B  1 559 ? -16.999 43.959 42.370  1.00 25.49 ? 559  PHE B CD2 1 
ATOM   10274 C  CE1 . PHE B  1 559 ? -17.249 42.834 44.900  1.00 26.23 ? 559  PHE B CE1 1 
ATOM   10275 C  CE2 . PHE B  1 559 ? -16.456 42.690 42.633  1.00 26.81 ? 559  PHE B CE2 1 
ATOM   10276 C  CZ  . PHE B  1 559 ? -16.585 42.133 43.901  1.00 26.96 ? 559  PHE B CZ  1 
ATOM   10277 N  N   . ARG B  1 560 ? -14.953 46.811 43.683  1.00 21.75 ? 560  ARG B N   1 
ATOM   10278 C  CA  . ARG B  1 560 ? -13.620 46.582 43.131  1.00 22.03 ? 560  ARG B CA  1 
ATOM   10279 C  C   . ARG B  1 560 ? -12.906 45.355 43.700  1.00 21.97 ? 560  ARG B C   1 
ATOM   10280 O  O   . ARG B  1 560 ? -13.058 45.027 44.879  1.00 23.34 ? 560  ARG B O   1 
ATOM   10281 C  CB  . ARG B  1 560 ? -12.725 47.812 43.363  1.00 21.51 ? 560  ARG B CB  1 
ATOM   10282 C  CG  . ARG B  1 560 ? -13.251 49.110 42.753  1.00 21.96 ? 560  ARG B CG  1 
ATOM   10283 C  CD  . ARG B  1 560 ? -12.276 50.308 42.956  1.00 21.76 ? 560  ARG B CD  1 
ATOM   10284 N  NE  . ARG B  1 560 ? -12.789 51.540 42.348  1.00 20.64 ? 560  ARG B NE  1 
ATOM   10285 C  CZ  . ARG B  1 560 ? -13.688 52.351 42.899  1.00 20.87 ? 560  ARG B CZ  1 
ATOM   10286 N  NH1 . ARG B  1 560 ? -14.195 52.092 44.102  1.00 20.43 ? 560  ARG B NH1 1 
ATOM   10287 N  NH2 . ARG B  1 560 ? -14.117 53.414 42.222  1.00 21.57 ? 560  ARG B NH2 1 
ATOM   10288 N  N   . LEU B  1 561 ? -12.143 44.674 42.846  1.00 21.31 ? 561  LEU B N   1 
ATOM   10289 C  CA  . LEU B  1 561 ? -11.327 43.542 43.260  1.00 21.05 ? 561  LEU B CA  1 
ATOM   10290 C  C   . LEU B  1 561 ? -9.903  44.074 43.026  1.00 22.25 ? 561  LEU B C   1 
ATOM   10291 O  O   . LEU B  1 561 ? -9.433  44.144 41.886  1.00 20.70 ? 561  LEU B O   1 
ATOM   10292 C  CB  . LEU B  1 561 ? -11.582 42.311 42.390  1.00 21.17 ? 561  LEU B CB  1 
ATOM   10293 C  CG  . LEU B  1 561 ? -12.932 41.611 42.633  1.00 22.30 ? 561  LEU B CG  1 
ATOM   10294 C  CD1 . LEU B  1 561 ? -13.055 40.427 41.708  1.00 21.97 ? 561  LEU B CD1 1 
ATOM   10295 C  CD2 . LEU B  1 561 ? -13.062 41.178 44.088  1.00 22.18 ? 561  LEU B CD2 1 
ATOM   10296 N  N   . ASN B  1 562 ? -9.227  44.473 44.097  1.00 20.99 ? 562  ASN B N   1 
ATOM   10297 C  CA  . ASN B  1 562 ? -7.896  45.042 43.940  1.00 21.82 ? 562  ASN B CA  1 
ATOM   10298 C  C   . ASN B  1 562 ? -6.932  44.702 45.070  1.00 21.68 ? 562  ASN B C   1 
ATOM   10299 O  O   . ASN B  1 562 ? -7.158  43.766 45.835  1.00 22.03 ? 562  ASN B O   1 
ATOM   10300 C  CB  . ASN B  1 562 ? -8.003  46.575 43.772  1.00 20.55 ? 562  ASN B CB  1 
ATOM   10301 C  CG  . ASN B  1 562 ? -8.781  47.231 44.906  1.00 21.73 ? 562  ASN B CG  1 
ATOM   10302 O  OD1 . ASN B  1 562 ? -8.945  46.635 45.975  1.00 22.14 ? 562  ASN B OD1 1 
ATOM   10303 N  ND2 . ASN B  1 562 ? -9.247  48.461 44.689  1.00 19.33 ? 562  ASN B ND2 1 
ATOM   10304 N  N   . TRP B  1 563 ? -5.845  45.462 45.169  1.00 21.76 ? 563  TRP B N   1 
ATOM   10305 C  CA  . TRP B  1 563 ? -4.847  45.208 46.204  1.00 21.30 ? 563  TRP B CA  1 
ATOM   10306 C  C   . TRP B  1 563 ? -5.452  45.320 47.597  1.00 21.50 ? 563  TRP B C   1 
ATOM   10307 O  O   . TRP B  1 563 ? -5.135  44.514 48.481  1.00 21.27 ? 563  TRP B O   1 
ATOM   10308 C  CB  . TRP B  1 563 ? -3.674  46.181 46.053  1.00 19.50 ? 563  TRP B CB  1 
ATOM   10309 C  CG  . TRP B  1 563 ? -2.491  45.904 46.957  1.00 18.42 ? 563  TRP B CG  1 
ATOM   10310 C  CD1 . TRP B  1 563 ? -1.864  44.699 47.169  1.00 17.47 ? 563  TRP B CD1 1 
ATOM   10311 C  CD2 . TRP B  1 563 ? -1.739  46.881 47.693  1.00 17.43 ? 563  TRP B CD2 1 
ATOM   10312 N  NE1 . TRP B  1 563 ? -0.766  44.874 47.989  1.00 17.07 ? 563  TRP B NE1 1 
ATOM   10313 C  CE2 . TRP B  1 563 ? -0.665  46.202 48.321  1.00 17.63 ? 563  TRP B CE2 1 
ATOM   10314 C  CE3 . TRP B  1 563 ? -1.866  48.268 47.874  1.00 17.21 ? 563  TRP B CE3 1 
ATOM   10315 C  CZ2 . TRP B  1 563 ? 0.282   46.866 49.123  1.00 17.13 ? 563  TRP B CZ2 1 
ATOM   10316 C  CZ3 . TRP B  1 563 ? -0.930  48.932 48.671  1.00 19.04 ? 563  TRP B CZ3 1 
ATOM   10317 C  CH2 . TRP B  1 563 ? 0.137   48.224 49.287  1.00 18.37 ? 563  TRP B CH2 1 
ATOM   10318 N  N   . ALA B  1 564 ? -6.309  46.322 47.798  1.00 20.72 ? 564  ALA B N   1 
ATOM   10319 C  CA  . ALA B  1 564 ? -6.949  46.512 49.093  1.00 20.66 ? 564  ALA B CA  1 
ATOM   10320 C  C   . ALA B  1 564 ? -7.798  45.280 49.460  1.00 20.69 ? 564  ALA B C   1 
ATOM   10321 O  O   . ALA B  1 564 ? -7.905  44.927 50.637  1.00 20.00 ? 564  ALA B O   1 
ATOM   10322 C  CB  . ALA B  1 564 ? -7.824  47.776 49.087  1.00 20.06 ? 564  ALA B CB  1 
ATOM   10323 N  N   . THR B  1 565 ? -8.390  44.630 48.456  1.00 20.72 ? 565  THR B N   1 
ATOM   10324 C  CA  . THR B  1 565 ? -9.216  43.436 48.709  1.00 22.03 ? 565  THR B CA  1 
ATOM   10325 C  C   . THR B  1 565 ? -8.370  42.369 49.404  1.00 22.29 ? 565  THR B C   1 
ATOM   10326 O  O   . THR B  1 565 ? -8.806  41.761 50.385  1.00 22.78 ? 565  THR B O   1 
ATOM   10327 C  CB  . THR B  1 565 ? -9.786  42.805 47.415  1.00 21.25 ? 565  THR B CB  1 
ATOM   10328 O  OG1 . THR B  1 565 ? -10.516 43.785 46.665  1.00 20.81 ? 565  THR B OG1 1 
ATOM   10329 C  CG2 . THR B  1 565 ? -10.726 41.653 47.776  1.00 20.23 ? 565  THR B CG2 1 
ATOM   10330 N  N   . TYR B  1 566 ? -7.169  42.142 48.880  1.00 22.51 ? 566  TYR B N   1 
ATOM   10331 C  CA  . TYR B  1 566 ? -6.232  41.188 49.462  1.00 22.76 ? 566  TYR B CA  1 
ATOM   10332 C  C   . TYR B  1 566 ? -5.766  41.673 50.845  1.00 23.72 ? 566  TYR B C   1 
ATOM   10333 O  O   . TYR B  1 566 ? -5.759  40.909 51.827  1.00 22.87 ? 566  TYR B O   1 
ATOM   10334 C  CB  . TYR B  1 566 ? -5.032  41.012 48.520  1.00 22.92 ? 566  TYR B CB  1 
ATOM   10335 C  CG  . TYR B  1 566 ? -3.691  40.805 49.203  1.00 23.21 ? 566  TYR B CG  1 
ATOM   10336 C  CD1 . TYR B  1 566 ? -3.402  39.624 49.887  1.00 23.34 ? 566  TYR B CD1 1 
ATOM   10337 C  CD2 . TYR B  1 566 ? -2.716  41.807 49.173  1.00 22.68 ? 566  TYR B CD2 1 
ATOM   10338 C  CE1 . TYR B  1 566 ? -2.175  39.446 50.527  1.00 23.82 ? 566  TYR B CE1 1 
ATOM   10339 C  CE2 . TYR B  1 566 ? -1.487  41.642 49.808  1.00 23.71 ? 566  TYR B CE2 1 
ATOM   10340 C  CZ  . TYR B  1 566 ? -1.225  40.462 50.483  1.00 24.73 ? 566  TYR B CZ  1 
ATOM   10341 O  OH  . TYR B  1 566 ? -0.032  40.314 51.134  1.00 26.06 ? 566  TYR B OH  1 
ATOM   10342 N  N   . LEU B  1 567 ? -5.398  42.945 50.938  1.00 23.46 ? 567  LEU B N   1 
ATOM   10343 C  CA  . LEU B  1 567 ? -4.924  43.479 52.213  1.00 23.45 ? 567  LEU B CA  1 
ATOM   10344 C  C   . LEU B  1 567 ? -5.979  43.279 53.310  1.00 24.41 ? 567  LEU B C   1 
ATOM   10345 O  O   . LEU B  1 567 ? -5.647  42.885 54.428  1.00 24.89 ? 567  LEU B O   1 
ATOM   10346 C  CB  . LEU B  1 567 ? -4.553  44.963 52.070  1.00 21.69 ? 567  LEU B CB  1 
ATOM   10347 C  CG  . LEU B  1 567 ? -3.283  45.300 51.255  1.00 21.47 ? 567  LEU B CG  1 
ATOM   10348 C  CD1 . LEU B  1 567 ? -3.204  46.803 51.004  1.00 21.17 ? 567  LEU B CD1 1 
ATOM   10349 C  CD2 . LEU B  1 567 ? -2.062  44.850 52.006  1.00 20.82 ? 567  LEU B CD2 1 
ATOM   10350 N  N   . ALA B  1 568 ? -7.250  43.520 52.988  1.00 24.46 ? 568  ALA B N   1 
ATOM   10351 C  CA  . ALA B  1 568 ? -8.316  43.334 53.976  1.00 24.91 ? 568  ALA B CA  1 
ATOM   10352 C  C   . ALA B  1 568 ? -8.631  41.850 54.215  1.00 25.08 ? 568  ALA B C   1 
ATOM   10353 O  O   . ALA B  1 568 ? -8.694  41.401 55.352  1.00 25.31 ? 568  ALA B O   1 
ATOM   10354 C  CB  . ALA B  1 568 ? -9.574  44.052 53.538  1.00 23.97 ? 568  ALA B CB  1 
ATOM   10355 N  N   . SER B  1 569 ? -8.817  41.100 53.140  1.00 24.93 ? 569  SER B N   1 
ATOM   10356 C  CA  . SER B  1 569 ? -9.158  39.691 53.246  1.00 26.44 ? 569  SER B CA  1 
ATOM   10357 C  C   . SER B  1 569 ? -8.083  38.770 53.828  1.00 26.84 ? 569  SER B C   1 
ATOM   10358 O  O   . SER B  1 569 ? -8.360  37.972 54.732  1.00 26.69 ? 569  SER B O   1 
ATOM   10359 C  CB  . SER B  1 569 ? -9.575  39.156 51.879  1.00 24.97 ? 569  SER B CB  1 
ATOM   10360 O  OG  . SER B  1 569 ? -9.798  37.762 51.940  1.00 26.64 ? 569  SER B OG  1 
ATOM   10361 N  N   . THR B  1 570 ? -6.869  38.855 53.297  1.00 26.95 ? 570  THR B N   1 
ATOM   10362 C  CA  . THR B  1 570 ? -5.784  38.007 53.771  1.00 26.97 ? 570  THR B CA  1 
ATOM   10363 C  C   . THR B  1 570 ? -4.941  38.572 54.914  1.00 27.36 ? 570  THR B C   1 
ATOM   10364 O  O   . THR B  1 570 ? -4.566  37.833 55.816  1.00 28.30 ? 570  THR B O   1 
ATOM   10365 C  CB  . THR B  1 570 ? -4.840  37.635 52.616  1.00 27.23 ? 570  THR B CB  1 
ATOM   10366 O  OG1 . THR B  1 570 ? -5.581  36.932 51.612  1.00 27.16 ? 570  THR B OG1 1 
ATOM   10367 C  CG2 . THR B  1 570 ? -3.701  36.741 53.111  1.00 28.59 ? 570  THR B CG2 1 
ATOM   10368 N  N   . GLU B  1 571 ? -4.638  39.867 54.889  1.00 27.18 ? 571  GLU B N   1 
ATOM   10369 C  CA  . GLU B  1 571 ? -3.785  40.462 55.923  1.00 25.82 ? 571  GLU B CA  1 
ATOM   10370 C  C   . GLU B  1 571 ? -4.542  41.114 57.068  1.00 25.10 ? 571  GLU B C   1 
ATOM   10371 O  O   . GLU B  1 571 ? -3.929  41.602 58.018  1.00 24.52 ? 571  GLU B O   1 
ATOM   10372 C  CB  . GLU B  1 571 ? -2.833  41.501 55.298  1.00 26.57 ? 571  GLU B CB  1 
ATOM   10373 C  CG  . GLU B  1 571 ? -1.940  40.972 54.153  1.00 27.16 ? 571  GLU B CG  1 
ATOM   10374 C  CD  . GLU B  1 571 ? -1.105  39.770 54.560  1.00 28.20 ? 571  GLU B CD  1 
ATOM   10375 O  OE1 . GLU B  1 571 ? -0.823  39.648 55.767  1.00 29.08 ? 571  GLU B OE1 1 
ATOM   10376 O  OE2 . GLU B  1 571 ? -0.719  38.953 53.687  1.00 28.54 ? 571  GLU B OE2 1 
ATOM   10377 N  N   . ASN B  1 572 ? -5.870  41.129 56.975  1.00 24.93 ? 572  ASN B N   1 
ATOM   10378 C  CA  . ASN B  1 572 ? -6.717  41.726 58.000  1.00 23.63 ? 572  ASN B CA  1 
ATOM   10379 C  C   . ASN B  1 572 ? -6.413  43.188 58.248  1.00 23.25 ? 572  ASN B C   1 
ATOM   10380 O  O   . ASN B  1 572 ? -6.436  43.665 59.387  1.00 22.49 ? 572  ASN B O   1 
ATOM   10381 C  CB  . ASN B  1 572 ? -6.602  40.962 59.320  1.00 25.22 ? 572  ASN B CB  1 
ATOM   10382 C  CG  . ASN B  1 572 ? -7.157  39.553 59.225  1.00 26.10 ? 572  ASN B CG  1 
ATOM   10383 O  OD1 . ASN B  1 572 ? -6.588  38.629 59.789  1.00 28.15 ? 572  ASN B OD1 1 
ATOM   10384 N  ND2 . ASN B  1 572 ? -8.274  39.385 58.517  1.00 25.84 ? 572  ASN B ND2 1 
ATOM   10385 N  N   . ILE B  1 573 ? -6.137  43.908 57.167  1.00 22.92 ? 573  ILE B N   1 
ATOM   10386 C  CA  . ILE B  1 573 ? -5.853  45.329 57.268  1.00 21.99 ? 573  ILE B CA  1 
ATOM   10387 C  C   . ILE B  1 573 ? -7.079  46.125 56.809  1.00 22.05 ? 573  ILE B C   1 
ATOM   10388 O  O   . ILE B  1 573 ? -7.690  45.802 55.788  1.00 22.03 ? 573  ILE B O   1 
ATOM   10389 C  CB  . ILE B  1 573 ? -4.646  45.715 56.360  1.00 22.18 ? 573  ILE B CB  1 
ATOM   10390 C  CG1 . ILE B  1 573 ? -3.365  45.032 56.852  1.00 21.96 ? 573  ILE B CG1 1 
ATOM   10391 C  CG2 . ILE B  1 573 ? -4.466  47.217 56.340  1.00 21.38 ? 573  ILE B CG2 1 
ATOM   10392 C  CD1 . ILE B  1 573 ? -2.156  45.281 55.914  1.00 20.95 ? 573  ILE B CD1 1 
ATOM   10393 N  N   . ILE B  1 574 ? -7.449  47.157 57.556  1.00 21.39 ? 574  ILE B N   1 
ATOM   10394 C  CA  . ILE B  1 574 ? -8.570  47.989 57.138  1.00 21.82 ? 574  ILE B CA  1 
ATOM   10395 C  C   . ILE B  1 574 ? -8.020  49.013 56.125  1.00 22.37 ? 574  ILE B C   1 
ATOM   10396 O  O   . ILE B  1 574 ? -7.093  49.771 56.449  1.00 22.38 ? 574  ILE B O   1 
ATOM   10397 C  CB  . ILE B  1 574 ? -9.178  48.764 58.324  1.00 21.94 ? 574  ILE B CB  1 
ATOM   10398 C  CG1 . ILE B  1 574 ? -9.822  47.799 59.333  1.00 22.51 ? 574  ILE B CG1 1 
ATOM   10399 C  CG2 . ILE B  1 574 ? -10.216 49.739 57.809  1.00 22.78 ? 574  ILE B CG2 1 
ATOM   10400 C  CD1 . ILE B  1 574 ? -10.332 48.498 60.590  1.00 21.12 ? 574  ILE B CD1 1 
ATOM   10401 N  N   . VAL B  1 575 ? -8.550  49.031 54.901  1.00 21.66 ? 575  VAL B N   1 
ATOM   10402 C  CA  . VAL B  1 575 ? -8.068  50.001 53.909  1.00 20.69 ? 575  VAL B CA  1 
ATOM   10403 C  C   . VAL B  1 575 ? -9.135  51.071 53.719  1.00 20.93 ? 575  VAL B C   1 
ATOM   10404 O  O   . VAL B  1 575 ? -10.235 50.780 53.230  1.00 21.25 ? 575  VAL B O   1 
ATOM   10405 C  CB  . VAL B  1 575 ? -7.751  49.341 52.544  1.00 20.45 ? 575  VAL B CB  1 
ATOM   10406 C  CG1 . VAL B  1 575 ? -7.194  50.382 51.581  1.00 20.68 ? 575  VAL B CG1 1 
ATOM   10407 C  CG2 . VAL B  1 575 ? -6.743  48.243 52.729  1.00 18.96 ? 575  VAL B CG2 1 
ATOM   10408 N  N   . ALA B  1 576 ? -8.797  52.304 54.102  1.00 19.86 ? 576  ALA B N   1 
ATOM   10409 C  CA  . ALA B  1 576 ? -9.724  53.431 54.031  1.00 20.26 ? 576  ALA B CA  1 
ATOM   10410 C  C   . ALA B  1 576 ? -9.366  54.566 53.074  1.00 20.09 ? 576  ALA B C   1 
ATOM   10411 O  O   . ALA B  1 576 ? -8.196  54.783 52.751  1.00 19.65 ? 576  ALA B O   1 
ATOM   10412 C  CB  . ALA B  1 576 ? -9.910  54.013 55.425  1.00 20.49 ? 576  ALA B CB  1 
ATOM   10413 N  N   . SER B  1 577 ? -10.385 55.310 52.649  1.00 19.42 ? 577  SER B N   1 
ATOM   10414 C  CA  . SER B  1 577 ? -10.171 56.460 51.771  1.00 19.76 ? 577  SER B CA  1 
ATOM   10415 C  C   . SER B  1 577 ? -11.136 57.557 52.205  1.00 21.05 ? 577  SER B C   1 
ATOM   10416 O  O   . SER B  1 577 ? -12.258 57.287 52.648  1.00 21.35 ? 577  SER B O   1 
ATOM   10417 C  CB  . SER B  1 577 ? -10.372 56.064 50.310  1.00 20.09 ? 577  SER B CB  1 
ATOM   10418 O  OG  . SER B  1 577 ? -9.427  55.056 49.936  1.00 18.81 ? 577  SER B OG  1 
ATOM   10419 N  N   . PHE B  1 578 ? -10.683 58.798 52.102  1.00 20.90 ? 578  PHE B N   1 
ATOM   10420 C  CA  . PHE B  1 578 ? -11.461 59.939 52.556  1.00 20.30 ? 578  PHE B CA  1 
ATOM   10421 C  C   . PHE B  1 578 ? -11.509 61.015 51.483  1.00 19.97 ? 578  PHE B C   1 
ATOM   10422 O  O   . PHE B  1 578 ? -10.495 61.267 50.827  1.00 18.90 ? 578  PHE B O   1 
ATOM   10423 C  CB  . PHE B  1 578 ? -10.774 60.503 53.803  1.00 21.17 ? 578  PHE B CB  1 
ATOM   10424 C  CG  . PHE B  1 578 ? -11.521 61.614 54.474  1.00 22.69 ? 578  PHE B CG  1 
ATOM   10425 C  CD1 . PHE B  1 578 ? -12.664 61.350 55.225  1.00 23.76 ? 578  PHE B CD1 1 
ATOM   10426 C  CD2 . PHE B  1 578 ? -11.067 62.920 54.383  1.00 22.82 ? 578  PHE B CD2 1 
ATOM   10427 C  CE1 . PHE B  1 578 ? -13.347 62.384 55.886  1.00 24.59 ? 578  PHE B CE1 1 
ATOM   10428 C  CE2 . PHE B  1 578 ? -11.738 63.955 55.034  1.00 22.87 ? 578  PHE B CE2 1 
ATOM   10429 C  CZ  . PHE B  1 578 ? -12.878 63.684 55.787  1.00 23.74 ? 578  PHE B CZ  1 
ATOM   10430 N  N   . ASP B  1 579 ? -12.676 61.644 51.312  1.00 20.06 ? 579  ASP B N   1 
ATOM   10431 C  CA  . ASP B  1 579 ? -12.856 62.743 50.353  1.00 19.52 ? 579  ASP B CA  1 
ATOM   10432 C  C   . ASP B  1 579 ? -13.047 64.037 51.146  1.00 20.60 ? 579  ASP B C   1 
ATOM   10433 O  O   . ASP B  1 579 ? -14.162 64.354 51.592  1.00 20.56 ? 579  ASP B O   1 
ATOM   10434 C  CB  . ASP B  1 579 ? -14.074 62.500 49.453  1.00 19.73 ? 579  ASP B CB  1 
ATOM   10435 C  CG  . ASP B  1 579 ? -13.822 61.427 48.402  1.00 20.58 ? 579  ASP B CG  1 
ATOM   10436 O  OD1 . ASP B  1 579 ? -12.649 61.256 48.000  1.00 19.37 ? 579  ASP B OD1 1 
ATOM   10437 O  OD2 . ASP B  1 579 ? -14.792 60.765 47.967  1.00 20.70 ? 579  ASP B OD2 1 
ATOM   10438 N  N   . GLY B  1 580 ? -11.947 64.767 51.341  1.00 19.91 ? 580  GLY B N   1 
ATOM   10439 C  CA  . GLY B  1 580 ? -11.988 66.008 52.096  1.00 19.80 ? 580  GLY B CA  1 
ATOM   10440 C  C   . GLY B  1 580 ? -12.074 67.236 51.203  1.00 19.65 ? 580  GLY B C   1 
ATOM   10441 O  O   . GLY B  1 580 ? -12.548 67.155 50.080  1.00 20.16 ? 580  GLY B O   1 
ATOM   10442 N  N   . ARG B  1 581 ? -11.612 68.375 51.692  1.00 18.76 ? 581  ARG B N   1 
ATOM   10443 C  CA  . ARG B  1 581 ? -11.664 69.574 50.889  1.00 19.54 ? 581  ARG B CA  1 
ATOM   10444 C  C   . ARG B  1 581 ? -10.900 69.356 49.589  1.00 19.51 ? 581  ARG B C   1 
ATOM   10445 O  O   . ARG B  1 581 ? -9.850  68.698 49.563  1.00 20.34 ? 581  ARG B O   1 
ATOM   10446 C  CB  . ARG B  1 581 ? -11.142 70.775 51.684  1.00 20.10 ? 581  ARG B CB  1 
ATOM   10447 C  CG  . ARG B  1 581 ? -12.187 71.296 52.696  1.00 21.53 ? 581  ARG B CG  1 
ATOM   10448 C  CD  . ARG B  1 581 ? -11.627 72.326 53.677  1.00 21.23 ? 581  ARG B CD  1 
ATOM   10449 N  NE  . ARG B  1 581 ? -10.725 71.710 54.645  1.00 21.65 ? 581  ARG B NE  1 
ATOM   10450 C  CZ  . ARG B  1 581 ? -10.025 72.380 55.556  1.00 23.23 ? 581  ARG B CZ  1 
ATOM   10451 N  NH1 . ARG B  1 581 ? -10.118 73.696 55.634  1.00 24.75 ? 581  ARG B NH1 1 
ATOM   10452 N  NH2 . ARG B  1 581 ? -9.213  71.732 56.381  1.00 23.56 ? 581  ARG B NH2 1 
ATOM   10453 N  N   . GLY B  1 582 ? -11.464 69.881 48.503  1.00 18.86 ? 582  GLY B N   1 
ATOM   10454 C  CA  . GLY B  1 582 ? -10.880 69.718 47.186  1.00 17.37 ? 582  GLY B CA  1 
ATOM   10455 C  C   . GLY B  1 582 ? -11.585 68.595 46.427  1.00 18.04 ? 582  GLY B C   1 
ATOM   10456 O  O   . GLY B  1 582 ? -11.532 68.578 45.205  1.00 17.64 ? 582  GLY B O   1 
ATOM   10457 N  N   . SER B  1 583 ? -12.266 67.675 47.126  1.00 17.47 ? 583  SER B N   1 
ATOM   10458 C  CA  . SER B  1 583 ? -12.910 66.551 46.436  1.00 17.88 ? 583  SER B CA  1 
ATOM   10459 C  C   . SER B  1 583 ? -14.087 67.001 45.592  1.00 17.94 ? 583  SER B C   1 
ATOM   10460 O  O   . SER B  1 583 ? -14.611 68.094 45.797  1.00 17.28 ? 583  SER B O   1 
ATOM   10461 C  CB  . SER B  1 583 ? -13.334 65.451 47.420  1.00 16.75 ? 583  SER B CB  1 
ATOM   10462 O  OG  . SER B  1 583 ? -14.170 65.948 48.443  1.00 18.63 ? 583  SER B OG  1 
ATOM   10463 N  N   . GLY B  1 584 ? -14.523 66.155 44.660  1.00 18.89 ? 584  GLY B N   1 
ATOM   10464 C  CA  . GLY B  1 584 ? -15.588 66.573 43.765  1.00 18.33 ? 584  GLY B CA  1 
ATOM   10465 C  C   . GLY B  1 584 ? -17.003 66.069 43.953  1.00 19.35 ? 584  GLY B C   1 
ATOM   10466 O  O   . GLY B  1 584 ? -17.307 65.315 44.878  1.00 18.23 ? 584  GLY B O   1 
ATOM   10467 N  N   . TYR B  1 585 ? -17.877 66.551 43.067  1.00 19.44 ? 585  TYR B N   1 
ATOM   10468 C  CA  . TYR B  1 585 ? -19.274 66.145 43.021  1.00 18.82 ? 585  TYR B CA  1 
ATOM   10469 C  C   . TYR B  1 585 ? -20.131 66.522 44.225  1.00 19.62 ? 585  TYR B C   1 
ATOM   10470 O  O   . TYR B  1 585 ? -21.214 65.965 44.409  1.00 19.04 ? 585  TYR B O   1 
ATOM   10471 C  CB  . TYR B  1 585 ? -19.315 64.634 42.798  1.00 16.93 ? 585  TYR B CB  1 
ATOM   10472 C  CG  . TYR B  1 585 ? -18.371 64.201 41.694  1.00 16.39 ? 585  TYR B CG  1 
ATOM   10473 C  CD1 . TYR B  1 585 ? -18.570 64.622 40.381  1.00 14.94 ? 585  TYR B CD1 1 
ATOM   10474 C  CD2 . TYR B  1 585 ? -17.246 63.420 41.971  1.00 13.94 ? 585  TYR B CD2 1 
ATOM   10475 C  CE1 . TYR B  1 585 ? -17.668 64.282 39.361  1.00 15.30 ? 585  TYR B CE1 1 
ATOM   10476 C  CE2 . TYR B  1 585 ? -16.339 63.074 40.961  1.00 14.28 ? 585  TYR B CE2 1 
ATOM   10477 C  CZ  . TYR B  1 585 ? -16.551 63.508 39.662  1.00 15.97 ? 585  TYR B CZ  1 
ATOM   10478 O  OH  . TYR B  1 585 ? -15.636 63.192 38.671  1.00 16.81 ? 585  TYR B OH  1 
ATOM   10479 N  N   . GLN B  1 586 ? -19.656 67.473 45.025  1.00 20.48 ? 586  GLN B N   1 
ATOM   10480 C  CA  . GLN B  1 586 ? -20.379 67.905 46.215  1.00 21.01 ? 586  GLN B CA  1 
ATOM   10481 C  C   . GLN B  1 586 ? -20.514 69.426 46.272  1.00 20.95 ? 586  GLN B C   1 
ATOM   10482 O  O   . GLN B  1 586 ? -20.797 69.986 47.330  1.00 20.72 ? 586  GLN B O   1 
ATOM   10483 C  CB  . GLN B  1 586 ? -19.653 67.425 47.481  1.00 21.43 ? 586  GLN B CB  1 
ATOM   10484 C  CG  . GLN B  1 586 ? -19.290 65.953 47.493  1.00 21.98 ? 586  GLN B CG  1 
ATOM   10485 C  CD  . GLN B  1 586 ? -18.088 65.683 48.394  1.00 25.08 ? 586  GLN B CD  1 
ATOM   10486 O  OE1 . GLN B  1 586 ? -18.192 65.728 49.622  1.00 24.35 ? 586  GLN B OE1 1 
ATOM   10487 N  NE2 . GLN B  1 586 ? -16.926 65.427 47.776  1.00 25.16 ? 586  GLN B NE2 1 
ATOM   10488 N  N   . GLY B  1 587 ? -20.297 70.096 45.144  1.00 21.21 ? 587  GLY B N   1 
ATOM   10489 C  CA  . GLY B  1 587 ? -20.409 71.546 45.119  1.00 20.98 ? 587  GLY B CA  1 
ATOM   10490 C  C   . GLY B  1 587 ? -19.075 72.282 45.171  1.00 21.50 ? 587  GLY B C   1 
ATOM   10491 O  O   . GLY B  1 587 ? -18.062 71.738 45.619  1.00 21.14 ? 587  GLY B O   1 
ATOM   10492 N  N   . ASP B  1 588 ? -19.086 73.542 44.744  1.00 22.17 ? 588  ASP B N   1 
ATOM   10493 C  CA  . ASP B  1 588 ? -17.884 74.363 44.711  1.00 23.82 ? 588  ASP B CA  1 
ATOM   10494 C  C   . ASP B  1 588 ? -17.284 74.711 46.064  1.00 23.68 ? 588  ASP B C   1 
ATOM   10495 O  O   . ASP B  1 588 ? -16.075 74.893 46.180  1.00 23.71 ? 588  ASP B O   1 
ATOM   10496 C  CB  . ASP B  1 588 ? -18.151 75.645 43.914  1.00 23.75 ? 588  ASP B CB  1 
ATOM   10497 C  CG  . ASP B  1 588 ? -18.259 75.380 42.428  1.00 24.96 ? 588  ASP B CG  1 
ATOM   10498 O  OD1 . ASP B  1 588 ? -17.930 74.244 42.018  1.00 24.14 ? 588  ASP B OD1 1 
ATOM   10499 O  OD2 . ASP B  1 588 ? -18.660 76.297 41.672  1.00 23.96 ? 588  ASP B OD2 1 
ATOM   10500 N  N   . LYS B  1 589 ? -18.123 74.805 47.081  1.00 24.67 ? 589  LYS B N   1 
ATOM   10501 C  CA  . LYS B  1 589 ? -17.652 75.142 48.418  1.00 26.60 ? 589  LYS B CA  1 
ATOM   10502 C  C   . LYS B  1 589 ? -16.526 74.175 48.812  1.00 25.67 ? 589  LYS B C   1 
ATOM   10503 O  O   . LYS B  1 589 ? -15.470 74.593 49.287  1.00 25.03 ? 589  LYS B O   1 
ATOM   10504 C  CB  . LYS B  1 589 ? -18.811 75.047 49.402  1.00 27.85 ? 589  LYS B CB  1 
ATOM   10505 C  CG  . LYS B  1 589 ? -18.422 75.205 50.854  1.00 32.72 ? 589  LYS B CG  1 
ATOM   10506 C  CD  . LYS B  1 589 ? -18.060 76.632 51.214  1.00 34.59 ? 589  LYS B CD  1 
ATOM   10507 C  CE  . LYS B  1 589 ? -17.777 76.738 52.716  1.00 36.94 ? 589  LYS B CE  1 
ATOM   10508 N  NZ  . LYS B  1 589 ? -18.927 76.252 53.557  1.00 37.87 ? 589  LYS B NZ  1 
ATOM   10509 N  N   . ILE B  1 590 ? -16.762 72.885 48.588  1.00 24.85 ? 590  ILE B N   1 
ATOM   10510 C  CA  . ILE B  1 590 ? -15.782 71.859 48.898  1.00 23.61 ? 590  ILE B CA  1 
ATOM   10511 C  C   . ILE B  1 590 ? -14.708 71.746 47.808  1.00 22.93 ? 590  ILE B C   1 
ATOM   10512 O  O   . ILE B  1 590 ? -13.518 71.769 48.100  1.00 22.93 ? 590  ILE B O   1 
ATOM   10513 C  CB  . ILE B  1 590 ? -16.467 70.464 49.095  1.00 23.03 ? 590  ILE B CB  1 
ATOM   10514 C  CG1 . ILE B  1 590 ? -17.244 70.439 50.415  1.00 22.47 ? 590  ILE B CG1 1 
ATOM   10515 C  CG2 . ILE B  1 590 ? -15.414 69.360 49.095  1.00 22.64 ? 590  ILE B CG2 1 
ATOM   10516 C  CD1 . ILE B  1 590 ? -18.109 69.204 50.627  1.00 20.00 ? 590  ILE B CD1 1 
ATOM   10517 N  N   . MET B  1 591 ? -15.119 71.661 46.552  1.00 22.57 ? 591  MET B N   1 
ATOM   10518 C  CA  . MET B  1 591 ? -14.143 71.505 45.487  1.00 22.72 ? 591  MET B CA  1 
ATOM   10519 C  C   . MET B  1 591 ? -13.146 72.649 45.364  1.00 22.58 ? 591  MET B C   1 
ATOM   10520 O  O   . MET B  1 591 ? -11.952 72.416 45.203  1.00 21.37 ? 591  MET B O   1 
ATOM   10521 C  CB  . MET B  1 591 ? -14.830 71.296 44.143  1.00 21.89 ? 591  MET B CB  1 
ATOM   10522 C  CG  . MET B  1 591 ? -13.850 70.891 43.046  1.00 22.06 ? 591  MET B CG  1 
ATOM   10523 S  SD  . MET B  1 591 ? -14.681 70.427 41.523  1.00 22.83 ? 591  MET B SD  1 
ATOM   10524 C  CE  . MET B  1 591 ? -14.957 72.076 40.807  1.00 22.41 ? 591  MET B CE  1 
ATOM   10525 N  N   . HIS B  1 592 ? -13.620 73.885 45.455  1.00 22.90 ? 592  HIS B N   1 
ATOM   10526 C  CA  . HIS B  1 592 ? -12.713 75.016 45.323  1.00 22.87 ? 592  HIS B CA  1 
ATOM   10527 C  C   . HIS B  1 592 ? -11.951 75.407 46.590  1.00 22.82 ? 592  HIS B C   1 
ATOM   10528 O  O   . HIS B  1 592 ? -11.213 76.401 46.594  1.00 22.38 ? 592  HIS B O   1 
ATOM   10529 C  CB  . HIS B  1 592 ? -13.473 76.229 44.784  1.00 23.64 ? 592  HIS B CB  1 
ATOM   10530 C  CG  . HIS B  1 592 ? -13.919 76.076 43.365  1.00 25.02 ? 592  HIS B CG  1 
ATOM   10531 N  ND1 . HIS B  1 592 ? -14.799 76.950 42.763  1.00 25.60 ? 592  HIS B ND1 1 
ATOM   10532 C  CD2 . HIS B  1 592 ? -13.581 75.169 42.417  1.00 24.59 ? 592  HIS B CD2 1 
ATOM   10533 C  CE1 . HIS B  1 592 ? -14.983 76.590 41.505  1.00 25.58 ? 592  HIS B CE1 1 
ATOM   10534 N  NE2 . HIS B  1 592 ? -14.255 75.513 41.270  1.00 25.39 ? 592  HIS B NE2 1 
ATOM   10535 N  N   . ALA B  1 593 ? -12.092 74.633 47.658  1.00 22.55 ? 593  ALA B N   1 
ATOM   10536 C  CA  . ALA B  1 593 ? -11.397 74.992 48.900  1.00 23.18 ? 593  ALA B CA  1 
ATOM   10537 C  C   . ALA B  1 593 ? -9.888  75.011 48.733  1.00 22.90 ? 593  ALA B C   1 
ATOM   10538 O  O   . ALA B  1 593 ? -9.198  75.728 49.453  1.00 23.37 ? 593  ALA B O   1 
ATOM   10539 C  CB  . ALA B  1 593 ? -11.781 74.049 50.027  1.00 22.49 ? 593  ALA B CB  1 
ATOM   10540 N  N   . ILE B  1 594 ? -9.365  74.231 47.794  1.00 21.82 ? 594  ILE B N   1 
ATOM   10541 C  CA  . ILE B  1 594 ? -7.925  74.229 47.594  1.00 21.63 ? 594  ILE B CA  1 
ATOM   10542 C  C   . ILE B  1 594 ? -7.455  75.072 46.420  1.00 21.58 ? 594  ILE B C   1 
ATOM   10543 O  O   . ILE B  1 594 ? -6.307  74.956 46.013  1.00 21.78 ? 594  ILE B O   1 
ATOM   10544 C  CB  . ILE B  1 594 ? -7.349  72.790 47.450  1.00 20.91 ? 594  ILE B CB  1 
ATOM   10545 C  CG1 . ILE B  1 594 ? -8.054  72.027 46.317  1.00 19.35 ? 594  ILE B CG1 1 
ATOM   10546 C  CG2 . ILE B  1 594 ? -7.479  72.060 48.786  1.00 20.83 ? 594  ILE B CG2 1 
ATOM   10547 C  CD1 . ILE B  1 594 ? -7.501  70.606 46.124  1.00 19.40 ? 594  ILE B CD1 1 
ATOM   10548 N  N   . ASN B  1 595 ? -8.325  75.934 45.897  1.00 21.46 ? 595  ASN B N   1 
ATOM   10549 C  CA  . ASN B  1 595 ? -7.945  76.803 44.775  1.00 22.14 ? 595  ASN B CA  1 
ATOM   10550 C  C   . ASN B  1 595 ? -6.660  77.562 45.126  1.00 22.25 ? 595  ASN B C   1 
ATOM   10551 O  O   . ASN B  1 595 ? -6.544  78.118 46.221  1.00 22.24 ? 595  ASN B O   1 
ATOM   10552 C  CB  . ASN B  1 595 ? -9.054  77.827 44.461  1.00 22.00 ? 595  ASN B CB  1 
ATOM   10553 C  CG  . ASN B  1 595 ? -8.765  78.633 43.179  1.00 23.56 ? 595  ASN B CG  1 
ATOM   10554 O  OD1 . ASN B  1 595 ? -8.982  79.844 43.122  1.00 24.51 ? 595  ASN B OD1 1 
ATOM   10555 N  ND2 . ASN B  1 595 ? -8.281  77.954 42.153  1.00 22.93 ? 595  ASN B ND2 1 
ATOM   10556 N  N   . ARG B  1 596 ? -5.702  77.567 44.204  1.00 21.76 ? 596  ARG B N   1 
ATOM   10557 C  CA  . ARG B  1 596 ? -4.414  78.254 44.384  1.00 22.29 ? 596  ARG B CA  1 
ATOM   10558 C  C   . ARG B  1 596 ? -3.636  77.791 45.621  1.00 21.53 ? 596  ARG B C   1 
ATOM   10559 O  O   . ARG B  1 596 ? -2.600  78.356 45.970  1.00 20.68 ? 596  ARG B O   1 
ATOM   10560 C  CB  . ARG B  1 596 ? -4.627  79.785 44.434  1.00 22.57 ? 596  ARG B CB  1 
ATOM   10561 C  CG  . ARG B  1 596 ? -5.122  80.382 43.091  1.00 23.14 ? 596  ARG B CG  1 
ATOM   10562 C  CD  . ARG B  1 596 ? -5.534  81.846 43.228  1.00 24.04 ? 596  ARG B CD  1 
ATOM   10563 N  NE  . ARG B  1 596 ? -4.417  82.700 43.632  1.00 25.18 ? 596  ARG B NE  1 
ATOM   10564 C  CZ  . ARG B  1 596 ? -3.482  83.143 42.805  1.00 25.09 ? 596  ARG B CZ  1 
ATOM   10565 N  NH1 . ARG B  1 596 ? -3.527  82.818 41.513  1.00 25.39 ? 596  ARG B NH1 1 
ATOM   10566 N  NH2 . ARG B  1 596 ? -2.504  83.906 43.272  1.00 25.21 ? 596  ARG B NH2 1 
ATOM   10567 N  N   . ARG B  1 597 ? -4.128  76.737 46.255  1.00 21.89 ? 597  ARG B N   1 
ATOM   10568 C  CA  . ARG B  1 597 ? -3.524  76.211 47.475  1.00 22.83 ? 597  ARG B CA  1 
ATOM   10569 C  C   . ARG B  1 597 ? -3.361  74.692 47.479  1.00 21.52 ? 597  ARG B C   1 
ATOM   10570 O  O   . ARG B  1 597 ? -3.725  74.030 48.459  1.00 20.91 ? 597  ARG B O   1 
ATOM   10571 C  CB  . ARG B  1 597 ? -4.382  76.632 48.685  1.00 25.26 ? 597  ARG B CB  1 
ATOM   10572 C  CG  . ARG B  1 597 ? -3.749  77.699 49.584  1.00 30.94 ? 597  ARG B CG  1 
ATOM   10573 C  CD  . ARG B  1 597 ? -3.383  78.928 48.790  1.00 34.30 ? 597  ARG B CD  1 
ATOM   10574 N  NE  . ARG B  1 597 ? -2.583  79.906 49.530  1.00 36.84 ? 597  ARG B NE  1 
ATOM   10575 C  CZ  . ARG B  1 597 ? -1.878  80.865 48.932  1.00 39.30 ? 597  ARG B CZ  1 
ATOM   10576 N  NH1 . ARG B  1 597 ? -1.877  80.957 47.598  1.00 37.51 ? 597  ARG B NH1 1 
ATOM   10577 N  NH2 . ARG B  1 597 ? -1.179  81.730 49.657  1.00 39.93 ? 597  ARG B NH2 1 
ATOM   10578 N  N   . LEU B  1 598 ? -2.818  74.126 46.402  1.00 20.34 ? 598  LEU B N   1 
ATOM   10579 C  CA  . LEU B  1 598 ? -2.637  72.671 46.371  1.00 19.48 ? 598  LEU B CA  1 
ATOM   10580 C  C   . LEU B  1 598 ? -1.623  72.338 47.467  1.00 19.46 ? 598  LEU B C   1 
ATOM   10581 O  O   . LEU B  1 598 ? -0.756  73.148 47.784  1.00 18.18 ? 598  LEU B O   1 
ATOM   10582 C  CB  . LEU B  1 598 ? -2.105  72.204 45.001  1.00 18.94 ? 598  LEU B CB  1 
ATOM   10583 C  CG  . LEU B  1 598 ? -2.961  72.392 43.736  1.00 18.49 ? 598  LEU B CG  1 
ATOM   10584 C  CD1 . LEU B  1 598 ? -2.298  71.680 42.583  1.00 16.34 ? 598  LEU B CD1 1 
ATOM   10585 C  CD2 . LEU B  1 598 ? -4.371  71.818 43.953  1.00 19.37 ? 598  LEU B CD2 1 
ATOM   10586 N  N   . GLY B  1 599 ? -1.739  71.164 48.068  1.00 20.01 ? 599  GLY B N   1 
ATOM   10587 C  CA  . GLY B  1 599 ? -0.789  70.806 49.097  1.00 20.68 ? 599  GLY B CA  1 
ATOM   10588 C  C   . GLY B  1 599 ? -1.126  71.341 50.480  1.00 21.30 ? 599  GLY B C   1 
ATOM   10589 O  O   . GLY B  1 599 ? -0.269  71.346 51.371  1.00 21.92 ? 599  GLY B O   1 
ATOM   10590 N  N   . THR B  1 600 ? -2.354  71.807 50.678  1.00 20.51 ? 600  THR B N   1 
ATOM   10591 C  CA  . THR B  1 600 ? -2.728  72.293 52.001  1.00 20.65 ? 600  THR B CA  1 
ATOM   10592 C  C   . THR B  1 600 ? -3.901  71.526 52.588  1.00 21.09 ? 600  THR B C   1 
ATOM   10593 O  O   . THR B  1 600 ? -3.706  70.460 53.181  1.00 21.64 ? 600  THR B O   1 
ATOM   10594 C  CB  . THR B  1 600 ? -3.040  73.816 52.003  1.00 21.41 ? 600  THR B CB  1 
ATOM   10595 O  OG1 . THR B  1 600 ? -4.120  74.104 51.104  1.00 23.01 ? 600  THR B OG1 1 
ATOM   10596 C  CG2 . THR B  1 600 ? -1.805  74.607 51.570  1.00 21.61 ? 600  THR B CG2 1 
ATOM   10597 N  N   . PHE B  1 601 ? -5.120  72.029 52.396  1.00 20.89 ? 601  PHE B N   1 
ATOM   10598 C  CA  . PHE B  1 601 ? -6.282  71.376 52.990  1.00 21.28 ? 601  PHE B CA  1 
ATOM   10599 C  C   . PHE B  1 601 ? -6.514  69.912 52.637  1.00 20.93 ? 601  PHE B C   1 
ATOM   10600 O  O   . PHE B  1 601 ? -6.965  69.134 53.488  1.00 19.69 ? 601  PHE B O   1 
ATOM   10601 C  CB  . PHE B  1 601 ? -7.568  72.151 52.683  1.00 23.06 ? 601  PHE B CB  1 
ATOM   10602 C  CG  . PHE B  1 601 ? -7.578  73.564 53.209  1.00 24.29 ? 601  PHE B CG  1 
ATOM   10603 C  CD1 . PHE B  1 601 ? -7.225  73.837 54.522  1.00 24.39 ? 601  PHE B CD1 1 
ATOM   10604 C  CD2 . PHE B  1 601 ? -7.959  74.617 52.385  1.00 25.02 ? 601  PHE B CD2 1 
ATOM   10605 C  CE1 . PHE B  1 601 ? -7.249  75.148 55.012  1.00 26.08 ? 601  PHE B CE1 1 
ATOM   10606 C  CE2 . PHE B  1 601 ? -7.989  75.927 52.858  1.00 26.31 ? 601  PHE B CE2 1 
ATOM   10607 C  CZ  . PHE B  1 601 ? -7.632  76.193 54.176  1.00 25.99 ? 601  PHE B CZ  1 
ATOM   10608 N  N   . GLU B  1 602 ? -6.241  69.526 51.396  1.00 19.51 ? 602  GLU B N   1 
ATOM   10609 C  CA  . GLU B  1 602 ? -6.477  68.143 51.027  1.00 20.35 ? 602  GLU B CA  1 
ATOM   10610 C  C   . GLU B  1 602 ? -5.481  67.241 51.756  1.00 20.35 ? 602  GLU B C   1 
ATOM   10611 O  O   . GLU B  1 602 ? -5.754  66.068 52.006  1.00 21.14 ? 602  GLU B O   1 
ATOM   10612 C  CB  . GLU B  1 602 ? -6.421  67.959 49.497  1.00 20.29 ? 602  GLU B CB  1 
ATOM   10613 C  CG  . GLU B  1 602 ? -5.058  67.854 48.845  1.00 19.59 ? 602  GLU B CG  1 
ATOM   10614 C  CD  . GLU B  1 602 ? -4.370  69.182 48.669  1.00 21.64 ? 602  GLU B CD  1 
ATOM   10615 O  OE1 . GLU B  1 602 ? -3.545  69.295 47.714  1.00 20.12 ? 602  GLU B OE1 1 
ATOM   10616 O  OE2 . GLU B  1 602 ? -4.626  70.112 49.485  1.00 19.98 ? 602  GLU B OE2 1 
ATOM   10617 N  N   . VAL B  1 603 ? -4.327  67.798 52.107  1.00 21.17 ? 603  VAL B N   1 
ATOM   10618 C  CA  . VAL B  1 603 ? -3.313  67.043 52.845  1.00 20.96 ? 603  VAL B CA  1 
ATOM   10619 C  C   . VAL B  1 603 ? -3.739  66.969 54.318  1.00 21.80 ? 603  VAL B C   1 
ATOM   10620 O  O   . VAL B  1 603 ? -3.777  65.896 54.924  1.00 21.84 ? 603  VAL B O   1 
ATOM   10621 C  CB  . VAL B  1 603 ? -1.942  67.740 52.767  1.00 19.84 ? 603  VAL B CB  1 
ATOM   10622 C  CG1 . VAL B  1 603 ? -0.957  67.050 53.690  1.00 19.19 ? 603  VAL B CG1 1 
ATOM   10623 C  CG2 . VAL B  1 603 ? -1.440  67.737 51.328  1.00 19.29 ? 603  VAL B CG2 1 
ATOM   10624 N  N   . GLU B  1 604 ? -4.078  68.115 54.889  1.00 23.24 ? 604  GLU B N   1 
ATOM   10625 C  CA  . GLU B  1 604 ? -4.487  68.147 56.294  1.00 26.04 ? 604  GLU B CA  1 
ATOM   10626 C  C   . GLU B  1 604 ? -5.728  67.284 56.577  1.00 24.72 ? 604  GLU B C   1 
ATOM   10627 O  O   . GLU B  1 604 ? -5.770  66.583 57.583  1.00 24.98 ? 604  GLU B O   1 
ATOM   10628 C  CB  . GLU B  1 604 ? -4.751  69.601 56.735  1.00 28.91 ? 604  GLU B CB  1 
ATOM   10629 C  CG  . GLU B  1 604 ? -3.551  70.544 56.578  1.00 33.76 ? 604  GLU B CG  1 
ATOM   10630 C  CD  . GLU B  1 604 ? -3.952  72.029 56.501  1.00 38.00 ? 604  GLU B CD  1 
ATOM   10631 O  OE1 . GLU B  1 604 ? -4.545  72.567 57.473  1.00 39.75 ? 604  GLU B OE1 1 
ATOM   10632 O  OE2 . GLU B  1 604 ? -3.674  72.670 55.457  1.00 39.90 ? 604  GLU B OE2 1 
ATOM   10633 N  N   . ASP B  1 605 ? -6.724  67.314 55.691  1.00 23.73 ? 605  ASP B N   1 
ATOM   10634 C  CA  . ASP B  1 605 ? -7.959  66.552 55.923  1.00 23.75 ? 605  ASP B CA  1 
ATOM   10635 C  C   . ASP B  1 605 ? -7.725  65.054 55.939  1.00 23.47 ? 605  ASP B C   1 
ATOM   10636 O  O   . ASP B  1 605 ? -8.460  64.289 56.561  1.00 22.57 ? 605  ASP B O   1 
ATOM   10637 C  CB  . ASP B  1 605 ? -9.038  66.913 54.887  1.00 23.82 ? 605  ASP B CB  1 
ATOM   10638 C  CG  . ASP B  1 605 ? -9.573  68.327 55.081  1.00 25.01 ? 605  ASP B CG  1 
ATOM   10639 O  OD1 . ASP B  1 605 ? -9.275  68.915 56.135  1.00 26.86 ? 605  ASP B OD1 1 
ATOM   10640 O  OD2 . ASP B  1 605 ? -10.286 68.861 54.203  1.00 25.19 ? 605  ASP B OD2 1 
ATOM   10641 N  N   . GLN B  1 606 ? -6.684  64.642 55.245  1.00 23.57 ? 606  GLN B N   1 
ATOM   10642 C  CA  . GLN B  1 606 ? -6.305  63.251 55.178  1.00 23.03 ? 606  GLN B CA  1 
ATOM   10643 C  C   . GLN B  1 606 ? -5.767  62.870 56.573  1.00 24.23 ? 606  GLN B C   1 
ATOM   10644 O  O   . GLN B  1 606 ? -6.084  61.801 57.100  1.00 24.37 ? 606  GLN B O   1 
ATOM   10645 C  CB  . GLN B  1 606 ? -5.236  63.131 54.100  1.00 24.89 ? 606  GLN B CB  1 
ATOM   10646 C  CG  . GLN B  1 606 ? -5.271  61.902 53.246  1.00 24.40 ? 606  GLN B CG  1 
ATOM   10647 C  CD  . GLN B  1 606 ? -6.613  61.586 52.612  1.00 23.03 ? 606  GLN B CD  1 
ATOM   10648 O  OE1 . GLN B  1 606 ? -6.938  60.426 52.456  1.00 22.43 ? 606  GLN B OE1 1 
ATOM   10649 N  NE2 . GLN B  1 606 ? -7.376  62.593 52.227  1.00 24.09 ? 606  GLN B NE2 1 
ATOM   10650 N  N   . ILE B  1 607 ? -4.973  63.755 57.180  1.00 24.80 ? 607  ILE B N   1 
ATOM   10651 C  CA  . ILE B  1 607 ? -4.402  63.507 58.515  1.00 25.93 ? 607  ILE B CA  1 
ATOM   10652 C  C   . ILE B  1 607 ? -5.547  63.484 59.531  1.00 26.02 ? 607  ILE B C   1 
ATOM   10653 O  O   . ILE B  1 607 ? -5.626  62.593 60.376  1.00 26.15 ? 607  ILE B O   1 
ATOM   10654 C  CB  . ILE B  1 607 ? -3.376  64.614 58.916  1.00 24.96 ? 607  ILE B CB  1 
ATOM   10655 C  CG1 . ILE B  1 607 ? -2.203  64.607 57.934  1.00 25.40 ? 607  ILE B CG1 1 
ATOM   10656 C  CG2 . ILE B  1 607 ? -2.838  64.370 60.335  1.00 25.48 ? 607  ILE B CG2 1 
ATOM   10657 C  CD1 . ILE B  1 607 ? -1.278  65.824 58.041  1.00 24.10 ? 607  ILE B CD1 1 
ATOM   10658 N  N   . GLU B  1 608 ? -6.439  64.460 59.429  1.00 26.73 ? 608  GLU B N   1 
ATOM   10659 C  CA  . GLU B  1 608 ? -7.584  64.540 60.326  1.00 27.28 ? 608  GLU B CA  1 
ATOM   10660 C  C   . GLU B  1 608 ? -8.457  63.303 60.146  1.00 28.19 ? 608  GLU B C   1 
ATOM   10661 O  O   . GLU B  1 608 ? -9.038  62.814 61.117  1.00 28.36 ? 608  GLU B O   1 
ATOM   10662 C  CB  . GLU B  1 608 ? -8.397  65.811 60.039  1.00 27.65 ? 608  GLU B CB  1 
ATOM   10663 C  CG  . GLU B  1 608 ? -9.600  66.043 60.968  1.00 29.66 ? 608  GLU B CG  1 
ATOM   10664 C  CD  . GLU B  1 608 ? -9.264  65.884 62.460  1.00 31.46 ? 608  GLU B CD  1 
ATOM   10665 O  OE1 . GLU B  1 608 ? -8.159  66.297 62.884  1.00 31.43 ? 608  GLU B OE1 1 
ATOM   10666 O  OE2 . GLU B  1 608 ? -10.116 65.353 63.209  1.00 31.80 ? 608  GLU B OE2 1 
ATOM   10667 N  N   . ALA B  1 609 ? -8.541  62.785 58.915  1.00 27.71 ? 609  ALA B N   1 
ATOM   10668 C  CA  . ALA B  1 609 ? -9.354  61.596 58.650  1.00 27.39 ? 609  ALA B CA  1 
ATOM   10669 C  C   . ALA B  1 609 ? -8.821  60.425 59.457  1.00 27.87 ? 609  ALA B C   1 
ATOM   10670 O  O   . ALA B  1 609 ? -9.593  59.671 60.053  1.00 27.50 ? 609  ALA B O   1 
ATOM   10671 C  CB  . ALA B  1 609 ? -9.336  61.244 57.164  1.00 26.93 ? 609  ALA B CB  1 
ATOM   10672 N  N   . ALA B  1 610 ? -7.499  60.267 59.463  1.00 27.46 ? 610  ALA B N   1 
ATOM   10673 C  CA  . ALA B  1 610 ? -6.873  59.180 60.213  1.00 27.49 ? 610  ALA B CA  1 
ATOM   10674 C  C   . ALA B  1 610 ? -7.180  59.340 61.710  1.00 27.64 ? 610  ALA B C   1 
ATOM   10675 O  O   . ALA B  1 610 ? -7.493  58.363 62.380  1.00 27.85 ? 610  ALA B O   1 
ATOM   10676 C  CB  . ALA B  1 610 ? -5.361  59.170 59.977  1.00 26.74 ? 610  ALA B CB  1 
ATOM   10677 N  N   . ARG B  1 611 ? -7.101  60.563 62.226  1.00 27.81 ? 611  ARG B N   1 
ATOM   10678 C  CA  . ARG B  1 611 ? -7.390  60.780 63.640  1.00 30.21 ? 611  ARG B CA  1 
ATOM   10679 C  C   . ARG B  1 611 ? -8.827  60.362 63.923  1.00 30.51 ? 611  ARG B C   1 
ATOM   10680 O  O   . ARG B  1 611 ? -9.099  59.670 64.902  1.00 31.23 ? 611  ARG B O   1 
ATOM   10681 C  CB  . ARG B  1 611 ? -7.210  62.243 64.032  1.00 29.32 ? 611  ARG B CB  1 
ATOM   10682 C  CG  . ARG B  1 611 ? -5.804  62.755 63.883  1.00 31.56 ? 611  ARG B CG  1 
ATOM   10683 C  CD  . ARG B  1 611 ? -5.678  64.132 64.511  1.00 31.62 ? 611  ARG B CD  1 
ATOM   10684 N  NE  . ARG B  1 611 ? -4.344  64.697 64.313  1.00 32.76 ? 611  ARG B NE  1 
ATOM   10685 C  CZ  . ARG B  1 611 ? -4.082  65.719 63.503  1.00 33.54 ? 611  ARG B CZ  1 
ATOM   10686 N  NH1 . ARG B  1 611 ? -5.066  66.298 62.811  1.00 33.46 ? 611  ARG B NH1 1 
ATOM   10687 N  NH2 . ARG B  1 611 ? -2.837  66.163 63.383  1.00 33.20 ? 611  ARG B NH2 1 
ATOM   10688 N  N   . GLN B  1 612 ? -9.741  60.781 63.057  1.00 31.43 ? 612  GLN B N   1 
ATOM   10689 C  CA  . GLN B  1 612 ? -11.151 60.447 63.210  1.00 32.69 ? 612  GLN B CA  1 
ATOM   10690 C  C   . GLN B  1 612 ? -11.352 58.944 63.177  1.00 33.26 ? 612  GLN B C   1 
ATOM   10691 O  O   . GLN B  1 612 ? -12.155 58.412 63.940  1.00 34.57 ? 612  GLN B O   1 
ATOM   10692 C  CB  . GLN B  1 612 ? -11.991 61.069 62.093  1.00 33.01 ? 612  GLN B CB  1 
ATOM   10693 C  CG  . GLN B  1 612 ? -12.013 62.586 62.059  1.00 34.19 ? 612  GLN B CG  1 
ATOM   10694 C  CD  . GLN B  1 612 ? -12.872 63.175 63.161  1.00 35.60 ? 612  GLN B CD  1 
ATOM   10695 O  OE1 . GLN B  1 612 ? -13.741 62.496 63.707  1.00 35.75 ? 612  GLN B OE1 1 
ATOM   10696 N  NE2 . GLN B  1 612 ? -12.646 64.445 63.479  1.00 34.64 ? 612  GLN B NE2 1 
ATOM   10697 N  N   . PHE B  1 613 ? -10.644 58.251 62.292  1.00 33.34 ? 613  PHE B N   1 
ATOM   10698 C  CA  . PHE B  1 613 ? -10.801 56.801 62.196  1.00 33.39 ? 613  PHE B CA  1 
ATOM   10699 C  C   . PHE B  1 613 ? -10.324 56.100 63.468  1.00 34.39 ? 613  PHE B C   1 
ATOM   10700 O  O   . PHE B  1 613 ? -10.984 55.189 63.962  1.00 34.34 ? 613  PHE B O   1 
ATOM   10701 C  CB  . PHE B  1 613 ? -10.052 56.238 60.976  1.00 32.48 ? 613  PHE B CB  1 
ATOM   10702 C  CG  . PHE B  1 613 ? -10.597 56.713 59.640  1.00 32.28 ? 613  PHE B CG  1 
ATOM   10703 C  CD1 . PHE B  1 613 ? -11.939 57.061 59.495  1.00 31.37 ? 613  PHE B CD1 1 
ATOM   10704 C  CD2 . PHE B  1 613 ? -9.767  56.770 58.519  1.00 31.11 ? 613  PHE B CD2 1 
ATOM   10705 C  CE1 . PHE B  1 613 ? -12.451 57.457 58.252  1.00 31.54 ? 613  PHE B CE1 1 
ATOM   10706 C  CE2 . PHE B  1 613 ? -10.264 57.162 57.271  1.00 31.29 ? 613  PHE B CE2 1 
ATOM   10707 C  CZ  . PHE B  1 613 ? -11.612 57.507 57.137  1.00 30.93 ? 613  PHE B CZ  1 
ATOM   10708 N  N   . SER B  1 614 ? -9.182  56.517 64.003  1.00 35.34 ? 614  SER B N   1 
ATOM   10709 C  CA  . SER B  1 614 ? -8.699  55.887 65.222  1.00 37.54 ? 614  SER B CA  1 
ATOM   10710 C  C   . SER B  1 614 ? -9.726  56.102 66.352  1.00 37.83 ? 614  SER B C   1 
ATOM   10711 O  O   . SER B  1 614 ? -10.031 55.188 67.120  1.00 37.41 ? 614  SER B O   1 
ATOM   10712 C  CB  . SER B  1 614 ? -7.341  56.462 65.594  1.00 37.99 ? 614  SER B CB  1 
ATOM   10713 O  OG  . SER B  1 614 ? -7.368  57.871 65.510  1.00 40.38 ? 614  SER B OG  1 
ATOM   10714 N  N   . LYS B  1 615 ? -10.285 57.301 66.430  1.00 38.55 ? 615  LYS B N   1 
ATOM   10715 C  CA  . LYS B  1 615 ? -11.285 57.579 67.452  1.00 38.97 ? 615  LYS B CA  1 
ATOM   10716 C  C   . LYS B  1 615 ? -12.509 56.665 67.351  1.00 38.85 ? 615  LYS B C   1 
ATOM   10717 O  O   . LYS B  1 615 ? -13.328 56.634 68.271  1.00 38.64 ? 615  LYS B O   1 
ATOM   10718 C  CB  . LYS B  1 615 ? -11.755 59.020 67.362  1.00 40.45 ? 615  LYS B CB  1 
ATOM   10719 C  CG  . LYS B  1 615 ? -10.750 60.058 67.811  1.00 42.58 ? 615  LYS B CG  1 
ATOM   10720 C  CD  . LYS B  1 615 ? -11.296 61.444 67.515  1.00 43.81 ? 615  LYS B CD  1 
ATOM   10721 C  CE  . LYS B  1 615 ? -12.724 61.601 68.051  1.00 45.13 ? 615  LYS B CE  1 
ATOM   10722 N  NZ  . LYS B  1 615 ? -13.393 62.826 67.519  1.00 46.00 ? 615  LYS B NZ  1 
ATOM   10723 N  N   . MET B  1 616 ? -12.655 55.933 66.244  1.00 38.17 ? 616  MET B N   1 
ATOM   10724 C  CA  . MET B  1 616 ? -13.800 55.029 66.108  1.00 37.19 ? 616  MET B CA  1 
ATOM   10725 C  C   . MET B  1 616 ? -13.581 53.792 66.971  1.00 36.77 ? 616  MET B C   1 
ATOM   10726 O  O   . MET B  1 616 ? -14.490 52.982 67.136  1.00 36.88 ? 616  MET B O   1 
ATOM   10727 C  CB  . MET B  1 616 ? -14.041 54.613 64.648  1.00 36.57 ? 616  MET B CB  1 
ATOM   10728 C  CG  . MET B  1 616 ? -14.406 55.769 63.719  1.00 36.25 ? 616  MET B CG  1 
ATOM   10729 S  SD  . MET B  1 616 ? -15.021 55.232 62.095  1.00 34.95 ? 616  MET B SD  1 
ATOM   10730 C  CE  . MET B  1 616 ? -15.834 56.665 61.579  1.00 34.95 ? 616  MET B CE  1 
ATOM   10731 N  N   . GLY B  1 617 ? -12.365 53.639 67.493  1.00 36.27 ? 617  GLY B N   1 
ATOM   10732 C  CA  . GLY B  1 617 ? -12.071 52.536 68.399  1.00 35.40 ? 617  GLY B CA  1 
ATOM   10733 C  C   . GLY B  1 617 ? -11.649 51.164 67.918  1.00 35.20 ? 617  GLY B C   1 
ATOM   10734 O  O   . GLY B  1 617 ? -11.280 50.327 68.742  1.00 35.71 ? 617  GLY B O   1 
ATOM   10735 N  N   . PHE B  1 618 ? -11.698 50.904 66.615  1.00 34.00 ? 618  PHE B N   1 
ATOM   10736 C  CA  . PHE B  1 618 ? -11.284 49.599 66.105  1.00 32.62 ? 618  PHE B CA  1 
ATOM   10737 C  C   . PHE B  1 618 ? -9.967  49.709 65.325  1.00 31.76 ? 618  PHE B C   1 
ATOM   10738 O  O   . PHE B  1 618 ? -9.635  48.858 64.498  1.00 30.43 ? 618  PHE B O   1 
ATOM   10739 C  CB  . PHE B  1 618 ? -12.396 48.997 65.229  1.00 32.60 ? 618  PHE B CB  1 
ATOM   10740 C  CG  . PHE B  1 618 ? -12.959 49.954 64.214  1.00 32.62 ? 618  PHE B CG  1 
ATOM   10741 C  CD1 . PHE B  1 618 ? -12.208 50.343 63.110  1.00 33.14 ? 618  PHE B CD1 1 
ATOM   10742 C  CD2 . PHE B  1 618 ? -14.250 50.458 64.352  1.00 32.67 ? 618  PHE B CD2 1 
ATOM   10743 C  CE1 . PHE B  1 618 ? -12.738 51.228 62.143  1.00 32.89 ? 618  PHE B CE1 1 
ATOM   10744 C  CE2 . PHE B  1 618 ? -14.788 51.337 63.398  1.00 32.64 ? 618  PHE B CE2 1 
ATOM   10745 C  CZ  . PHE B  1 618 ? -14.029 51.722 62.291  1.00 32.36 ? 618  PHE B CZ  1 
ATOM   10746 N  N   . VAL B  1 619 ? -9.211  50.755 65.618  1.00 31.27 ? 619  VAL B N   1 
ATOM   10747 C  CA  . VAL B  1 619 ? -7.954  50.971 64.932  1.00 31.82 ? 619  VAL B CA  1 
ATOM   10748 C  C   . VAL B  1 619 ? -6.767  50.995 65.882  1.00 32.14 ? 619  VAL B C   1 
ATOM   10749 O  O   . VAL B  1 619 ? -6.804  51.630 66.943  1.00 33.05 ? 619  VAL B O   1 
ATOM   10750 C  CB  . VAL B  1 619 ? -7.982  52.304 64.137  1.00 31.80 ? 619  VAL B CB  1 
ATOM   10751 C  CG1 . VAL B  1 619 ? -6.592  52.604 63.548  1.00 31.39 ? 619  VAL B CG1 1 
ATOM   10752 C  CG2 . VAL B  1 619 ? -9.037  52.228 63.033  1.00 30.71 ? 619  VAL B CG2 1 
ATOM   10753 N  N   . ASP B  1 620 ? -5.714  50.291 65.493  1.00 31.92 ? 620  ASP B N   1 
ATOM   10754 C  CA  . ASP B  1 620 ? -4.487  50.251 66.276  1.00 31.87 ? 620  ASP B CA  1 
ATOM   10755 C  C   . ASP B  1 620 ? -3.660  51.486 65.923  1.00 32.33 ? 620  ASP B C   1 
ATOM   10756 O  O   . ASP B  1 620 ? -3.037  51.531 64.859  1.00 31.48 ? 620  ASP B O   1 
ATOM   10757 C  CB  . ASP B  1 620 ? -3.696  48.987 65.934  1.00 31.02 ? 620  ASP B CB  1 
ATOM   10758 C  CG  . ASP B  1 620 ? -2.367  48.914 66.669  1.00 30.08 ? 620  ASP B CG  1 
ATOM   10759 O  OD1 . ASP B  1 620 ? -2.036  49.868 67.397  1.00 29.23 ? 620  ASP B OD1 1 
ATOM   10760 O  OD2 . ASP B  1 620 ? -1.659  47.904 66.504  1.00 29.83 ? 620  ASP B OD2 1 
ATOM   10761 N  N   . ASN B  1 621 ? -3.647  52.475 66.816  1.00 32.71 ? 621  ASN B N   1 
ATOM   10762 C  CA  . ASN B  1 621 ? -2.900  53.721 66.603  1.00 34.46 ? 621  ASN B CA  1 
ATOM   10763 C  C   . ASN B  1 621 ? -1.418  53.559 66.271  1.00 34.08 ? 621  ASN B C   1 
ATOM   10764 O  O   . ASN B  1 621 ? -0.805  54.456 65.681  1.00 34.01 ? 621  ASN B O   1 
ATOM   10765 C  CB  . ASN B  1 621 ? -2.987  54.614 67.839  1.00 37.41 ? 621  ASN B CB  1 
ATOM   10766 C  CG  . ASN B  1 621 ? -4.354  55.195 68.033  1.00 40.94 ? 621  ASN B CG  1 
ATOM   10767 O  OD1 . ASN B  1 621 ? -4.872  55.899 67.159  1.00 43.85 ? 621  ASN B OD1 1 
ATOM   10768 N  ND2 . ASN B  1 621 ? -4.956  54.916 69.183  1.00 42.58 ? 621  ASN B ND2 1 
ATOM   10769 N  N   . LYS B  1 622 ? -0.840  52.436 66.681  1.00 32.63 ? 622  LYS B N   1 
ATOM   10770 C  CA  . LYS B  1 622 ? 0.573   52.178 66.453  1.00 31.51 ? 622  LYS B CA  1 
ATOM   10771 C  C   . LYS B  1 622 ? 0.816   51.678 65.047  1.00 29.79 ? 622  LYS B C   1 
ATOM   10772 O  O   . LYS B  1 622 ? 1.956   51.609 64.593  1.00 31.13 ? 622  LYS B O   1 
ATOM   10773 C  CB  . LYS B  1 622 ? 1.077   51.137 67.457  1.00 32.80 ? 622  LYS B CB  1 
ATOM   10774 C  CG  . LYS B  1 622 ? 0.975   51.588 68.909  1.00 35.32 ? 622  LYS B CG  1 
ATOM   10775 C  CD  . LYS B  1 622 ? 1.280   50.432 69.876  1.00 37.04 ? 622  LYS B CD  1 
ATOM   10776 C  CE  . LYS B  1 622 ? 0.242   49.285 69.773  1.00 38.98 ? 622  LYS B CE  1 
ATOM   10777 N  NZ  . LYS B  1 622 ? -1.159  49.685 70.130  1.00 38.44 ? 622  LYS B NZ  1 
ATOM   10778 N  N   . ARG B  1 623 ? -0.256  51.312 64.359  1.00 27.25 ? 623  ARG B N   1 
ATOM   10779 C  CA  . ARG B  1 623 ? -0.111  50.807 63.014  1.00 25.46 ? 623  ARG B CA  1 
ATOM   10780 C  C   . ARG B  1 623 ? -1.012  51.492 61.993  1.00 23.50 ? 623  ARG B C   1 
ATOM   10781 O  O   . ARG B  1 623 ? -1.948  50.904 61.471  1.00 22.16 ? 623  ARG B O   1 
ATOM   10782 C  CB  . ARG B  1 623 ? -0.333  49.296 63.011  1.00 26.33 ? 623  ARG B CB  1 
ATOM   10783 C  CG  . ARG B  1 623 ? 0.743   48.525 63.795  1.00 28.64 ? 623  ARG B CG  1 
ATOM   10784 C  CD  . ARG B  1 623 ? 0.110   47.341 64.490  1.00 30.18 ? 623  ARG B CD  1 
ATOM   10785 N  NE  . ARG B  1 623 ? 0.085   46.147 63.663  1.00 32.22 ? 623  ARG B NE  1 
ATOM   10786 C  CZ  . ARG B  1 623 ? -0.827  45.189 63.768  1.00 31.66 ? 623  ARG B CZ  1 
ATOM   10787 N  NH1 . ARG B  1 623 ? -1.808  45.292 64.665  1.00 32.87 ? 623  ARG B NH1 1 
ATOM   10788 N  NH2 . ARG B  1 623 ? -0.742  44.120 62.993  1.00 31.62 ? 623  ARG B NH2 1 
ATOM   10789 N  N   . ILE B  1 624 ? -0.737  52.759 61.734  1.00 22.73 ? 624  ILE B N   1 
ATOM   10790 C  CA  . ILE B  1 624 ? -1.512  53.484 60.741  1.00 22.56 ? 624  ILE B CA  1 
ATOM   10791 C  C   . ILE B  1 624 ? -0.540  53.859 59.626  1.00 21.66 ? 624  ILE B C   1 
ATOM   10792 O  O   . ILE B  1 624 ? 0.473   54.502 59.880  1.00 22.22 ? 624  ILE B O   1 
ATOM   10793 C  CB  . ILE B  1 624 ? -2.128  54.756 61.315  1.00 21.48 ? 624  ILE B CB  1 
ATOM   10794 C  CG1 . ILE B  1 624 ? -3.031  54.409 62.499  1.00 22.58 ? 624  ILE B CG1 1 
ATOM   10795 C  CG2 . ILE B  1 624 ? -2.948  55.449 60.234  1.00 21.93 ? 624  ILE B CG2 1 
ATOM   10796 C  CD1 . ILE B  1 624 ? -3.766  55.622 63.079  1.00 22.56 ? 624  ILE B CD1 1 
ATOM   10797 N  N   . ALA B  1 625 ? -0.840  53.423 58.408  1.00 20.24 ? 625  ALA B N   1 
ATOM   10798 C  CA  . ALA B  1 625 ? 0.010   53.704 57.252  1.00 18.77 ? 625  ALA B CA  1 
ATOM   10799 C  C   . ALA B  1 625 ? -0.769  54.512 56.219  1.00 19.38 ? 625  ALA B C   1 
ATOM   10800 O  O   . ALA B  1 625 ? -1.985  54.727 56.359  1.00 17.54 ? 625  ALA B O   1 
ATOM   10801 C  CB  . ALA B  1 625 ? 0.503   52.398 56.636  1.00 17.31 ? 625  ALA B CB  1 
ATOM   10802 N  N   . ILE B  1 626 ? -0.076  54.966 55.179  1.00 18.90 ? 626  ILE B N   1 
ATOM   10803 C  CA  . ILE B  1 626 ? -0.730  55.756 54.138  1.00 18.94 ? 626  ILE B CA  1 
ATOM   10804 C  C   . ILE B  1 626 ? -0.035  55.551 52.793  1.00 19.63 ? 626  ILE B C   1 
ATOM   10805 O  O   . ILE B  1 626 ? 1.188   55.487 52.733  1.00 19.09 ? 626  ILE B O   1 
ATOM   10806 C  CB  . ILE B  1 626 ? -0.711  57.261 54.524  1.00 19.94 ? 626  ILE B CB  1 
ATOM   10807 C  CG1 . ILE B  1 626 ? -1.386  58.108 53.437  1.00 20.28 ? 626  ILE B CG1 1 
ATOM   10808 C  CG2 . ILE B  1 626 ? 0.723   57.732 54.732  1.00 20.40 ? 626  ILE B CG2 1 
ATOM   10809 C  CD1 . ILE B  1 626 ? -1.553  59.553 53.829  1.00 18.75 ? 626  ILE B CD1 1 
ATOM   10810 N  N   . TRP B  1 627 ? -0.805  55.408 51.715  1.00 19.47 ? 627  TRP B N   1 
ATOM   10811 C  CA  . TRP B  1 627 ? -0.192  55.243 50.408  1.00 18.53 ? 627  TRP B CA  1 
ATOM   10812 C  C   . TRP B  1 627 ? -1.036  55.865 49.318  1.00 18.94 ? 627  TRP B C   1 
ATOM   10813 O  O   . TRP B  1 627 ? -2.234  56.066 49.491  1.00 17.67 ? 627  TRP B O   1 
ATOM   10814 C  CB  . TRP B  1 627 ? 0.076   53.765 50.083  1.00 18.30 ? 627  TRP B CB  1 
ATOM   10815 C  CG  . TRP B  1 627 ? -0.991  53.075 49.277  1.00 18.59 ? 627  TRP B CG  1 
ATOM   10816 C  CD1 . TRP B  1 627 ? -2.221  52.637 49.721  1.00 18.37 ? 627  TRP B CD1 1 
ATOM   10817 C  CD2 . TRP B  1 627 ? -0.921  52.727 47.891  1.00 18.35 ? 627  TRP B CD2 1 
ATOM   10818 N  NE1 . TRP B  1 627 ? -2.909  52.039 48.695  1.00 19.19 ? 627  TRP B NE1 1 
ATOM   10819 C  CE2 . TRP B  1 627 ? -2.139  52.080 47.560  1.00 19.71 ? 627  TRP B CE2 1 
ATOM   10820 C  CE3 . TRP B  1 627 ? 0.053   52.898 46.895  1.00 18.53 ? 627  TRP B CE3 1 
ATOM   10821 C  CZ2 . TRP B  1 627 ? -2.408  51.601 46.269  1.00 20.09 ? 627  TRP B CZ2 1 
ATOM   10822 C  CZ3 . TRP B  1 627 ? -0.207  52.425 45.610  1.00 19.37 ? 627  TRP B CZ3 1 
ATOM   10823 C  CH2 . TRP B  1 627 ? -1.432  51.779 45.307  1.00 20.16 ? 627  TRP B CH2 1 
ATOM   10824 N  N   . GLY B  1 628 ? -0.385  56.184 48.196  1.00 18.33 ? 628  GLY B N   1 
ATOM   10825 C  CA  . GLY B  1 628 ? -1.073  56.782 47.074  1.00 17.46 ? 628  GLY B CA  1 
ATOM   10826 C  C   . GLY B  1 628 ? -0.200  56.778 45.834  1.00 17.88 ? 628  GLY B C   1 
ATOM   10827 O  O   . GLY B  1 628 ? 1.034   56.660 45.885  1.00 14.54 ? 628  GLY B O   1 
ATOM   10828 N  N   . TRP B  1 629 ? -0.853  56.934 44.699  1.00 17.61 ? 629  TRP B N   1 
ATOM   10829 C  CA  . TRP B  1 629 ? -0.159  56.942 43.421  1.00 17.63 ? 629  TRP B CA  1 
ATOM   10830 C  C   . TRP B  1 629 ? -0.459  58.286 42.760  1.00 16.83 ? 629  TRP B C   1 
ATOM   10831 O  O   . TRP B  1 629 ? -1.552  58.822 42.922  1.00 16.73 ? 629  TRP B O   1 
ATOM   10832 C  CB  . TRP B  1 629 ? -0.728  55.797 42.582  1.00 18.88 ? 629  TRP B CB  1 
ATOM   10833 C  CG  . TRP B  1 629 ? 0.073   55.344 41.409  1.00 19.16 ? 629  TRP B CG  1 
ATOM   10834 C  CD1 . TRP B  1 629 ? 0.523   56.110 40.364  1.00 20.18 ? 629  TRP B CD1 1 
ATOM   10835 C  CD2 . TRP B  1 629 ? 0.401   53.990 41.083  1.00 19.69 ? 629  TRP B CD2 1 
ATOM   10836 N  NE1 . TRP B  1 629 ? 1.100   55.306 39.404  1.00 19.50 ? 629  TRP B NE1 1 
ATOM   10837 C  CE2 . TRP B  1 629 ? 1.039   54.002 39.821  1.00 19.60 ? 629  TRP B CE2 1 
ATOM   10838 C  CE3 . TRP B  1 629 ? 0.215   52.759 41.740  1.00 18.74 ? 629  TRP B CE3 1 
ATOM   10839 C  CZ2 . TRP B  1 629 ? 1.494   52.828 39.195  1.00 19.13 ? 629  TRP B CZ2 1 
ATOM   10840 C  CZ3 . TRP B  1 629 ? 0.668   51.595 41.121  1.00 19.15 ? 629  TRP B CZ3 1 
ATOM   10841 C  CH2 . TRP B  1 629 ? 1.300   51.638 39.858  1.00 19.83 ? 629  TRP B CH2 1 
ATOM   10842 N  N   . SER B  1 630 ? 0.519   58.854 42.058  1.00 16.90 ? 630  SER B N   1 
ATOM   10843 C  CA  . SER B  1 630 ? 0.300   60.101 41.335  1.00 16.20 ? 630  SER B CA  1 
ATOM   10844 C  C   . SER B  1 630 ? 0.000   61.253 42.299  1.00 16.14 ? 630  SER B C   1 
ATOM   10845 O  O   . SER B  1 630 ? 0.824   61.555 43.155  1.00 15.69 ? 630  SER B O   1 
ATOM   10846 C  CB  . SER B  1 630 ? -0.861  59.882 40.353  1.00 16.02 ? 630  SER B CB  1 
ATOM   10847 O  OG  . SER B  1 630 ? -0.824  60.812 39.300  1.00 18.43 ? 630  SER B OG  1 
ATOM   10848 N  N   . TYR B  1 631 ? -1.152  61.913 42.166  1.00 14.91 ? 631  TYR B N   1 
ATOM   10849 C  CA  . TYR B  1 631 ? -1.477  62.981 43.104  1.00 14.71 ? 631  TYR B CA  1 
ATOM   10850 C  C   . TYR B  1 631 ? -1.482  62.320 44.480  1.00 15.76 ? 631  TYR B C   1 
ATOM   10851 O  O   . TYR B  1 631 ? -1.128  62.949 45.480  1.00 16.47 ? 631  TYR B O   1 
ATOM   10852 C  CB  . TYR B  1 631 ? -2.852  63.601 42.816  1.00 14.00 ? 631  TYR B CB  1 
ATOM   10853 C  CG  . TYR B  1 631 ? -3.030  64.991 43.427  1.00 14.77 ? 631  TYR B CG  1 
ATOM   10854 C  CD1 . TYR B  1 631 ? -3.298  65.160 44.783  1.00 13.64 ? 631  TYR B CD1 1 
ATOM   10855 C  CD2 . TYR B  1 631 ? -2.934  66.135 42.630  1.00 15.96 ? 631  TYR B CD2 1 
ATOM   10856 C  CE1 . TYR B  1 631 ? -3.472  66.437 45.344  1.00 16.69 ? 631  TYR B CE1 1 
ATOM   10857 C  CE2 . TYR B  1 631 ? -3.102  67.416 43.170  1.00 16.37 ? 631  TYR B CE2 1 
ATOM   10858 C  CZ  . TYR B  1 631 ? -3.371  67.561 44.533  1.00 17.33 ? 631  TYR B CZ  1 
ATOM   10859 O  OH  . TYR B  1 631 ? -3.517  68.822 45.082  1.00 17.67 ? 631  TYR B OH  1 
ATOM   10860 N  N   . GLY B  1 632 ? -1.862  61.040 44.513  1.00 15.58 ? 632  GLY B N   1 
ATOM   10861 C  CA  . GLY B  1 632 ? -1.890  60.291 45.765  1.00 16.46 ? 632  GLY B CA  1 
ATOM   10862 C  C   . GLY B  1 632 ? -0.485  60.146 46.359  1.00 16.39 ? 632  GLY B C   1 
ATOM   10863 O  O   . GLY B  1 632 ? -0.320  60.144 47.587  1.00 16.28 ? 632  GLY B O   1 
ATOM   10864 N  N   . GLY B  1 633 ? 0.518   60.016 45.492  1.00 14.42 ? 633  GLY B N   1 
ATOM   10865 C  CA  . GLY B  1 633 ? 1.905   59.931 45.935  1.00 15.17 ? 633  GLY B CA  1 
ATOM   10866 C  C   . GLY B  1 633 ? 2.329   61.271 46.543  1.00 15.44 ? 633  GLY B C   1 
ATOM   10867 O  O   . GLY B  1 633 ? 3.016   61.318 47.560  1.00 16.70 ? 633  GLY B O   1 
ATOM   10868 N  N   . TYR B  1 634 ? 1.937   62.370 45.905  1.00 14.78 ? 634  TYR B N   1 
ATOM   10869 C  CA  . TYR B  1 634 ? 2.229   63.698 46.417  1.00 14.89 ? 634  TYR B CA  1 
ATOM   10870 C  C   . TYR B  1 634 ? 1.620   63.887 47.820  1.00 15.77 ? 634  TYR B C   1 
ATOM   10871 O  O   . TYR B  1 634 ? 2.335   64.227 48.781  1.00 16.02 ? 634  TYR B O   1 
ATOM   10872 C  CB  . TYR B  1 634 ? 1.672   64.750 45.457  1.00 14.09 ? 634  TYR B CB  1 
ATOM   10873 C  CG  . TYR B  1 634 ? 1.701   66.166 45.984  1.00 13.96 ? 634  TYR B CG  1 
ATOM   10874 C  CD1 . TYR B  1 634 ? 2.913   66.813 46.218  1.00 14.73 ? 634  TYR B CD1 1 
ATOM   10875 C  CD2 . TYR B  1 634 ? 0.518   66.880 46.190  1.00 13.32 ? 634  TYR B CD2 1 
ATOM   10876 C  CE1 . TYR B  1 634 ? 2.952   68.140 46.628  1.00 14.86 ? 634  TYR B CE1 1 
ATOM   10877 C  CE2 . TYR B  1 634 ? 0.542   68.220 46.606  1.00 13.70 ? 634  TYR B CE2 1 
ATOM   10878 C  CZ  . TYR B  1 634 ? 1.765   68.838 46.813  1.00 13.85 ? 634  TYR B CZ  1 
ATOM   10879 O  OH  . TYR B  1 634 ? 1.815   70.158 47.161  1.00 14.87 ? 634  TYR B OH  1 
ATOM   10880 N  N   . VAL B  1 635 ? 0.308   63.667 47.947  1.00 16.47 ? 635  VAL B N   1 
ATOM   10881 C  CA  . VAL B  1 635 ? -0.357  63.824 49.251  1.00 16.60 ? 635  VAL B CA  1 
ATOM   10882 C  C   . VAL B  1 635 ? 0.274   62.900 50.306  1.00 17.21 ? 635  VAL B C   1 
ATOM   10883 O  O   . VAL B  1 635 ? 0.523   63.328 51.435  1.00 17.21 ? 635  VAL B O   1 
ATOM   10884 C  CB  . VAL B  1 635 ? -1.891  63.562 49.155  1.00 16.02 ? 635  VAL B CB  1 
ATOM   10885 C  CG1 . VAL B  1 635 ? -2.519  63.576 50.565  1.00 15.50 ? 635  VAL B CG1 1 
ATOM   10886 C  CG2 . VAL B  1 635 ? -2.549  64.647 48.303  1.00 16.49 ? 635  VAL B CG2 1 
ATOM   10887 N  N   . THR B  1 636 ? 0.546   61.647 49.943  1.00 18.12 ? 636  THR B N   1 
ATOM   10888 C  CA  . THR B  1 636 ? 1.179   60.709 50.884  1.00 18.39 ? 636  THR B CA  1 
ATOM   10889 C  C   . THR B  1 636 ? 2.502   61.285 51.406  1.00 19.36 ? 636  THR B C   1 
ATOM   10890 O  O   . THR B  1 636 ? 2.765   61.293 52.614  1.00 19.53 ? 636  THR B O   1 
ATOM   10891 C  CB  . THR B  1 636 ? 1.489   59.354 50.220  1.00 19.06 ? 636  THR B CB  1 
ATOM   10892 O  OG1 . THR B  1 636 ? 0.257   58.685 49.924  1.00 19.04 ? 636  THR B OG1 1 
ATOM   10893 C  CG2 . THR B  1 636 ? 2.328   58.450 51.162  1.00 16.89 ? 636  THR B CG2 1 
ATOM   10894 N  N   . SER B  1 637 ? 3.333   61.779 50.496  1.00 18.73 ? 637  SER B N   1 
ATOM   10895 C  CA  . SER B  1 637 ? 4.621   62.346 50.885  1.00 18.89 ? 637  SER B CA  1 
ATOM   10896 C  C   . SER B  1 637 ? 4.450   63.590 51.764  1.00 18.74 ? 637  SER B C   1 
ATOM   10897 O  O   . SER B  1 637 ? 5.152   63.755 52.764  1.00 18.41 ? 637  SER B O   1 
ATOM   10898 C  CB  . SER B  1 637 ? 5.432   62.686 49.630  1.00 17.96 ? 637  SER B CB  1 
ATOM   10899 O  OG  . SER B  1 637 ? 5.596   61.539 48.830  1.00 17.94 ? 637  SER B OG  1 
ATOM   10900 N  N   . MET B  1 638 ? 3.526   64.466 51.385  1.00 18.81 ? 638  MET B N   1 
ATOM   10901 C  CA  . MET B  1 638 ? 3.283   65.667 52.162  1.00 18.72 ? 638  MET B CA  1 
ATOM   10902 C  C   . MET B  1 638 ? 2.826   65.272 53.571  1.00 19.87 ? 638  MET B C   1 
ATOM   10903 O  O   . MET B  1 638 ? 3.219   65.891 54.573  1.00 18.92 ? 638  MET B O   1 
ATOM   10904 C  CB  . MET B  1 638 ? 2.220   66.543 51.488  1.00 18.53 ? 638  MET B CB  1 
ATOM   10905 C  CG  . MET B  1 638 ? 2.643   67.150 50.140  1.00 19.58 ? 638  MET B CG  1 
ATOM   10906 S  SD  . MET B  1 638 ? 4.025   68.322 50.260  1.00 21.11 ? 638  MET B SD  1 
ATOM   10907 C  CE  . MET B  1 638 ? 3.169   69.848 50.654  1.00 17.20 ? 638  MET B CE  1 
ATOM   10908 N  N   . VAL B  1 639 ? 1.984   64.247 53.651  1.00 20.06 ? 639  VAL B N   1 
ATOM   10909 C  CA  . VAL B  1 639 ? 1.493   63.777 54.948  1.00 20.56 ? 639  VAL B CA  1 
ATOM   10910 C  C   . VAL B  1 639 ? 2.652   63.165 55.738  1.00 20.96 ? 639  VAL B C   1 
ATOM   10911 O  O   . VAL B  1 639 ? 2.820   63.465 56.910  1.00 21.79 ? 639  VAL B O   1 
ATOM   10912 C  CB  . VAL B  1 639 ? 0.352   62.717 54.803  1.00 19.61 ? 639  VAL B CB  1 
ATOM   10913 C  CG1 . VAL B  1 639 ? 0.138   62.005 56.136  1.00 20.58 ? 639  VAL B CG1 1 
ATOM   10914 C  CG2 . VAL B  1 639 ? -0.957  63.405 54.392  1.00 17.98 ? 639  VAL B CG2 1 
ATOM   10915 N  N   . LEU B  1 640 ? 3.459   62.327 55.095  1.00 21.15 ? 640  LEU B N   1 
ATOM   10916 C  CA  . LEU B  1 640 ? 4.571   61.704 55.790  1.00 20.68 ? 640  LEU B CA  1 
ATOM   10917 C  C   . LEU B  1 640 ? 5.600   62.709 56.258  1.00 22.07 ? 640  LEU B C   1 
ATOM   10918 O  O   . LEU B  1 640 ? 6.321   62.453 57.234  1.00 22.39 ? 640  LEU B O   1 
ATOM   10919 C  CB  . LEU B  1 640 ? 5.238   60.659 54.910  1.00 20.40 ? 640  LEU B CB  1 
ATOM   10920 C  CG  . LEU B  1 640 ? 4.346   59.453 54.639  1.00 20.39 ? 640  LEU B CG  1 
ATOM   10921 C  CD1 . LEU B  1 640 ? 5.015   58.539 53.625  1.00 19.80 ? 640  LEU B CD1 1 
ATOM   10922 C  CD2 . LEU B  1 640 ? 4.086   58.720 55.942  1.00 19.26 ? 640  LEU B CD2 1 
ATOM   10923 N  N   . GLY B  1 641 ? 5.673   63.852 55.580  1.00 21.88 ? 641  GLY B N   1 
ATOM   10924 C  CA  . GLY B  1 641 ? 6.625   64.873 55.974  1.00 22.06 ? 641  GLY B CA  1 
ATOM   10925 C  C   . GLY B  1 641 ? 6.016   66.010 56.783  1.00 22.08 ? 641  GLY B C   1 
ATOM   10926 O  O   . GLY B  1 641 ? 6.664   67.042 56.982  1.00 21.09 ? 641  GLY B O   1 
ATOM   10927 N  N   . SER B  1 642 ? 4.781   65.829 57.253  1.00 21.36 ? 642  SER B N   1 
ATOM   10928 C  CA  . SER B  1 642 ? 4.107   66.874 58.021  1.00 22.68 ? 642  SER B CA  1 
ATOM   10929 C  C   . SER B  1 642 ? 4.493   66.950 59.503  1.00 23.31 ? 642  SER B C   1 
ATOM   10930 O  O   . SER B  1 642 ? 4.211   67.951 60.161  1.00 23.40 ? 642  SER B O   1 
ATOM   10931 C  CB  . SER B  1 642 ? 2.590   66.694 57.947  1.00 22.39 ? 642  SER B CB  1 
ATOM   10932 O  OG  . SER B  1 642 ? 2.193   65.544 58.677  1.00 21.25 ? 642  SER B OG  1 
ATOM   10933 N  N   . GLY B  1 643 ? 5.113   65.900 60.029  1.00 23.41 ? 643  GLY B N   1 
ATOM   10934 C  CA  . GLY B  1 643 ? 5.469   65.893 61.441  1.00 25.17 ? 643  GLY B CA  1 
ATOM   10935 C  C   . GLY B  1 643 ? 4.266   65.625 62.355  1.00 25.22 ? 643  GLY B C   1 
ATOM   10936 O  O   . GLY B  1 643 ? 4.346   65.845 63.571  1.00 24.57 ? 643  GLY B O   1 
ATOM   10937 N  N   . SER B  1 644 ? 3.159   65.143 61.782  1.00 24.75 ? 644  SER B N   1 
ATOM   10938 C  CA  . SER B  1 644 ? 1.931   64.878 62.551  1.00 24.96 ? 644  SER B CA  1 
ATOM   10939 C  C   . SER B  1 644 ? 2.044   63.743 63.553  1.00 24.98 ? 644  SER B C   1 
ATOM   10940 O  O   . SER B  1 644 ? 1.280   63.685 64.520  1.00 25.24 ? 644  SER B O   1 
ATOM   10941 C  CB  . SER B  1 644 ? 0.763   64.544 61.614  1.00 24.08 ? 644  SER B CB  1 
ATOM   10942 O  OG  . SER B  1 644 ? 0.743   63.154 61.329  1.00 22.98 ? 644  SER B OG  1 
ATOM   10943 N  N   . GLY B  1 645 ? 2.967   62.821 63.290  1.00 25.61 ? 645  GLY B N   1 
ATOM   10944 C  CA  . GLY B  1 645 ? 3.152   61.676 64.163  1.00 24.66 ? 645  GLY B CA  1 
ATOM   10945 C  C   . GLY B  1 645 ? 2.055   60.615 64.058  1.00 24.83 ? 645  GLY B C   1 
ATOM   10946 O  O   . GLY B  1 645 ? 2.158   59.552 64.677  1.00 24.81 ? 645  GLY B O   1 
ATOM   10947 N  N   . VAL B  1 646 ? 1.020   60.862 63.263  1.00 23.92 ? 646  VAL B N   1 
ATOM   10948 C  CA  . VAL B  1 646 ? -0.072  59.895 63.146  1.00 22.73 ? 646  VAL B CA  1 
ATOM   10949 C  C   . VAL B  1 646 ? 0.259   58.609 62.394  1.00 23.03 ? 646  VAL B C   1 
ATOM   10950 O  O   . VAL B  1 646 ? -0.216  57.515 62.751  1.00 23.43 ? 646  VAL B O   1 
ATOM   10951 C  CB  . VAL B  1 646 ? -1.320  60.553 62.483  1.00 23.09 ? 646  VAL B CB  1 
ATOM   10952 C  CG1 . VAL B  1 646 ? -2.418  59.511 62.264  1.00 22.49 ? 646  VAL B CG1 1 
ATOM   10953 C  CG2 . VAL B  1 646 ? -1.843  61.686 63.359  1.00 21.65 ? 646  VAL B CG2 1 
ATOM   10954 N  N   . PHE B  1 647 ? 1.099   58.728 61.369  1.00 22.04 ? 647  PHE B N   1 
ATOM   10955 C  CA  . PHE B  1 647 ? 1.457   57.592 60.517  1.00 21.01 ? 647  PHE B CA  1 
ATOM   10956 C  C   . PHE B  1 647 ? 2.827   56.952 60.783  1.00 21.64 ? 647  PHE B C   1 
ATOM   10957 O  O   . PHE B  1 647 ? 3.828   57.640 60.923  1.00 21.70 ? 647  PHE B O   1 
ATOM   10958 C  CB  . PHE B  1 647 ? 1.383   58.051 59.049  1.00 18.95 ? 647  PHE B CB  1 
ATOM   10959 C  CG  . PHE B  1 647 ? 0.043   58.613 58.660  1.00 17.48 ? 647  PHE B CG  1 
ATOM   10960 C  CD1 . PHE B  1 647 ? -0.950  57.789 58.165  1.00 16.48 ? 647  PHE B CD1 1 
ATOM   10961 C  CD2 . PHE B  1 647 ? -0.239  59.958 58.843  1.00 15.76 ? 647  PHE B CD2 1 
ATOM   10962 C  CE1 . PHE B  1 647 ? -2.211  58.294 57.859  1.00 16.71 ? 647  PHE B CE1 1 
ATOM   10963 C  CE2 . PHE B  1 647 ? -1.502  60.478 58.539  1.00 16.96 ? 647  PHE B CE2 1 
ATOM   10964 C  CZ  . PHE B  1 647 ? -2.491  59.641 58.046  1.00 14.52 ? 647  PHE B CZ  1 
ATOM   10965 N  N   . LYS B  1 648 ? 2.867   55.627 60.803  1.00 22.22 ? 648  LYS B N   1 
ATOM   10966 C  CA  . LYS B  1 648 ? 4.118   54.916 61.026  1.00 22.65 ? 648  LYS B CA  1 
ATOM   10967 C  C   . LYS B  1 648 ? 4.968   54.785 59.745  1.00 22.83 ? 648  LYS B C   1 
ATOM   10968 O  O   . LYS B  1 648 ? 6.195   54.931 59.770  1.00 22.48 ? 648  LYS B O   1 
ATOM   10969 C  CB  . LYS B  1 648 ? 3.821   53.525 61.571  1.00 22.36 ? 648  LYS B CB  1 
ATOM   10970 C  CG  . LYS B  1 648 ? 5.060   52.696 61.836  1.00 23.37 ? 648  LYS B CG  1 
ATOM   10971 C  CD  . LYS B  1 648 ? 4.700   51.314 62.286  1.00 24.67 ? 648  LYS B CD  1 
ATOM   10972 C  CE  . LYS B  1 648 ? 5.932   50.467 62.428  1.00 25.73 ? 648  LYS B CE  1 
ATOM   10973 N  NZ  . LYS B  1 648 ? 5.798   49.683 63.660  1.00 28.00 ? 648  LYS B NZ  1 
ATOM   10974 N  N   . CYS B  1 649 ? 4.308   54.517 58.627  1.00 22.13 ? 649  CYS B N   1 
ATOM   10975 C  CA  . CYS B  1 649 ? 5.000   54.347 57.364  1.00 22.06 ? 649  CYS B CA  1 
ATOM   10976 C  C   . CYS B  1 649 ? 4.102   54.778 56.195  1.00 21.66 ? 649  CYS B C   1 
ATOM   10977 O  O   . CYS B  1 649 ? 2.887   54.964 56.357  1.00 19.96 ? 649  CYS B O   1 
ATOM   10978 C  CB  . CYS B  1 649 ? 5.390   52.875 57.207  1.00 24.80 ? 649  CYS B CB  1 
ATOM   10979 S  SG  . CYS B  1 649 ? 3.931   51.779 57.359  1.00 29.30 ? 649  CYS B SG  1 
ATOM   10980 N  N   . GLY B  1 650 ? 4.695   54.940 55.016  1.00 19.86 ? 650  GLY B N   1 
ATOM   10981 C  CA  . GLY B  1 650 ? 3.902   55.325 53.858  1.00 19.51 ? 650  GLY B CA  1 
ATOM   10982 C  C   . GLY B  1 650 ? 4.612   54.968 52.560  1.00 19.27 ? 650  GLY B C   1 
ATOM   10983 O  O   . GLY B  1 650 ? 5.841   54.789 52.554  1.00 16.59 ? 650  GLY B O   1 
ATOM   10984 N  N   . ILE B  1 651 ? 3.843   54.886 51.472  1.00 17.83 ? 651  ILE B N   1 
ATOM   10985 C  CA  . ILE B  1 651 ? 4.372   54.545 50.152  1.00 17.37 ? 651  ILE B CA  1 
ATOM   10986 C  C   . ILE B  1 651 ? 3.902   55.545 49.091  1.00 17.95 ? 651  ILE B C   1 
ATOM   10987 O  O   . ILE B  1 651 ? 2.688   55.733 48.892  1.00 17.86 ? 651  ILE B O   1 
ATOM   10988 C  CB  . ILE B  1 651 ? 3.893   53.142 49.696  1.00 17.10 ? 651  ILE B CB  1 
ATOM   10989 C  CG1 . ILE B  1 651 ? 4.222   52.098 50.778  1.00 17.54 ? 651  ILE B CG1 1 
ATOM   10990 C  CG2 . ILE B  1 651 ? 4.538   52.775 48.363  1.00 14.90 ? 651  ILE B CG2 1 
ATOM   10991 C  CD1 . ILE B  1 651 ? 3.766   50.669 50.422  1.00 16.78 ? 651  ILE B CD1 1 
ATOM   10992 N  N   . ALA B  1 652 ? 4.840   56.197 48.409  1.00 16.91 ? 652  ALA B N   1 
ATOM   10993 C  CA  . ALA B  1 652 ? 4.440   57.126 47.351  1.00 16.29 ? 652  ALA B CA  1 
ATOM   10994 C  C   . ALA B  1 652 ? 4.855   56.532 46.015  1.00 16.22 ? 652  ALA B C   1 
ATOM   10995 O  O   . ALA B  1 652 ? 6.004   56.151 45.836  1.00 15.96 ? 652  ALA B O   1 
ATOM   10996 C  CB  . ALA B  1 652 ? 5.085   58.489 47.556  1.00 15.54 ? 652  ALA B CB  1 
ATOM   10997 N  N   . VAL B  1 653 ? 3.905   56.399 45.094  1.00 16.76 ? 653  VAL B N   1 
ATOM   10998 C  CA  . VAL B  1 653 ? 4.230   55.878 43.770  1.00 16.48 ? 653  VAL B CA  1 
ATOM   10999 C  C   . VAL B  1 653 ? 4.051   56.998 42.750  1.00 15.99 ? 653  VAL B C   1 
ATOM   11000 O  O   . VAL B  1 653 ? 2.995   57.657 42.708  1.00 15.72 ? 653  VAL B O   1 
ATOM   11001 C  CB  . VAL B  1 653 ? 3.335   54.666 43.376  1.00 15.84 ? 653  VAL B CB  1 
ATOM   11002 C  CG1 . VAL B  1 653 ? 3.800   54.069 42.032  1.00 13.08 ? 653  VAL B CG1 1 
ATOM   11003 C  CG2 . VAL B  1 653 ? 3.394   53.594 44.489  1.00 16.15 ? 653  VAL B CG2 1 
ATOM   11004 N  N   . ALA B  1 654 ? 5.086   57.193 41.928  1.00 14.91 ? 654  ALA B N   1 
ATOM   11005 C  CA  . ALA B  1 654 ? 5.114   58.231 40.890  1.00 14.91 ? 654  ALA B CA  1 
ATOM   11006 C  C   . ALA B  1 654 ? 4.521   59.539 41.407  1.00 13.71 ? 654  ALA B C   1 
ATOM   11007 O  O   . ALA B  1 654 ? 3.609   60.117 40.812  1.00 14.37 ? 654  ALA B O   1 
ATOM   11008 C  CB  . ALA B  1 654 ? 4.352   57.764 39.627  1.00 14.20 ? 654  ALA B CB  1 
ATOM   11009 N  N   . PRO B  1 655 ? 5.057   60.043 42.511  1.00 12.69 ? 655  PRO B N   1 
ATOM   11010 C  CA  . PRO B  1 655 ? 4.526   61.288 43.056  1.00 13.88 ? 655  PRO B CA  1 
ATOM   11011 C  C   . PRO B  1 655 ? 4.956   62.598 42.396  1.00 14.09 ? 655  PRO B C   1 
ATOM   11012 O  O   . PRO B  1 655 ? 6.031   62.695 41.818  1.00 13.14 ? 655  PRO B O   1 
ATOM   11013 C  CB  . PRO B  1 655 ? 5.021   61.253 44.499  1.00 12.88 ? 655  PRO B CB  1 
ATOM   11014 C  CG  . PRO B  1 655 ? 6.385   60.645 44.356  1.00 12.88 ? 655  PRO B CG  1 
ATOM   11015 C  CD  . PRO B  1 655 ? 6.095   59.482 43.397  1.00 12.61 ? 655  PRO B CD  1 
ATOM   11016 N  N   . VAL B  1 656 ? 4.096   63.607 42.492  1.00 13.71 ? 656  VAL B N   1 
ATOM   11017 C  CA  . VAL B  1 656 ? 4.479   64.942 42.064  1.00 14.21 ? 656  VAL B CA  1 
ATOM   11018 C  C   . VAL B  1 656 ? 5.242   65.374 43.335  1.00 14.93 ? 656  VAL B C   1 
ATOM   11019 O  O   . VAL B  1 656 ? 4.892   64.919 44.435  1.00 15.58 ? 656  VAL B O   1 
ATOM   11020 C  CB  . VAL B  1 656 ? 3.252   65.866 41.876  1.00 13.58 ? 656  VAL B CB  1 
ATOM   11021 C  CG1 . VAL B  1 656 ? 3.672   67.334 41.932  1.00 12.91 ? 656  VAL B CG1 1 
ATOM   11022 C  CG2 . VAL B  1 656 ? 2.610   65.588 40.519  1.00 12.46 ? 656  VAL B CG2 1 
ATOM   11023 N  N   . SER B  1 657 ? 6.275   66.203 43.200  1.00 15.38 ? 657  SER B N   1 
ATOM   11024 C  CA  . SER B  1 657 ? 7.038   66.671 44.363  1.00 15.59 ? 657  SER B CA  1 
ATOM   11025 C  C   . SER B  1 657 ? 7.125   68.205 44.431  1.00 15.90 ? 657  SER B C   1 
ATOM   11026 O  O   . SER B  1 657 ? 7.351   68.772 45.502  1.00 15.31 ? 657  SER B O   1 
ATOM   11027 C  CB  . SER B  1 657 ? 8.458   66.089 44.363  1.00 16.89 ? 657  SER B CB  1 
ATOM   11028 O  OG  . SER B  1 657 ? 9.208   66.591 43.269  1.00 16.01 ? 657  SER B OG  1 
ATOM   11029 N  N   . ARG B  1 658 ? 6.971   68.872 43.293  1.00 15.48 ? 658  ARG B N   1 
ATOM   11030 C  CA  . ARG B  1 658 ? 6.984   70.331 43.250  1.00 17.51 ? 658  ARG B CA  1 
ATOM   11031 C  C   . ARG B  1 658 ? 6.199   70.708 42.004  1.00 16.87 ? 658  ARG B C   1 
ATOM   11032 O  O   . ARG B  1 658 ? 6.483   70.222 40.901  1.00 15.74 ? 658  ARG B O   1 
ATOM   11033 C  CB  . ARG B  1 658 ? 8.412   70.914 43.204  1.00 19.79 ? 658  ARG B CB  1 
ATOM   11034 C  CG  . ARG B  1 658 ? 9.022   71.078 41.827  1.00 25.65 ? 658  ARG B CG  1 
ATOM   11035 C  CD  . ARG B  1 658 ? 9.786   72.422 41.634  1.00 28.23 ? 658  ARG B CD  1 
ATOM   11036 N  NE  . ARG B  1 658 ? 10.429  72.934 42.837  1.00 26.59 ? 658  ARG B NE  1 
ATOM   11037 C  CZ  . ARG B  1 658 ? 11.180  74.036 42.888  1.00 27.79 ? 658  ARG B CZ  1 
ATOM   11038 N  NH1 . ARG B  1 658 ? 11.409  74.752 41.792  1.00 26.79 ? 658  ARG B NH1 1 
ATOM   11039 N  NH2 . ARG B  1 658 ? 11.670  74.448 44.060  1.00 25.09 ? 658  ARG B NH2 1 
ATOM   11040 N  N   . TRP B  1 659 ? 5.210   71.575 42.178  1.00 15.81 ? 659  TRP B N   1 
ATOM   11041 C  CA  . TRP B  1 659 ? 4.352   71.934 41.072  1.00 15.65 ? 659  TRP B CA  1 
ATOM   11042 C  C   . TRP B  1 659 ? 5.012   72.544 39.833  1.00 15.96 ? 659  TRP B C   1 
ATOM   11043 O  O   . TRP B  1 659 ? 4.524   72.359 38.716  1.00 14.71 ? 659  TRP B O   1 
ATOM   11044 C  CB  . TRP B  1 659 ? 3.193   72.758 41.614  1.00 15.56 ? 659  TRP B CB  1 
ATOM   11045 C  CG  . TRP B  1 659 ? 2.291   71.854 42.420  1.00 15.34 ? 659  TRP B CG  1 
ATOM   11046 C  CD1 . TRP B  1 659 ? 2.099   71.863 43.786  1.00 15.58 ? 659  TRP B CD1 1 
ATOM   11047 C  CD2 . TRP B  1 659 ? 1.528   70.744 41.922  1.00 14.45 ? 659  TRP B CD2 1 
ATOM   11048 N  NE1 . TRP B  1 659 ? 1.270   70.826 44.152  1.00 12.93 ? 659  TRP B NE1 1 
ATOM   11049 C  CE2 . TRP B  1 659 ? 0.905   70.128 43.030  1.00 14.49 ? 659  TRP B CE2 1 
ATOM   11050 C  CE3 . TRP B  1 659 ? 1.310   70.210 40.641  1.00 14.74 ? 659  TRP B CE3 1 
ATOM   11051 C  CZ2 . TRP B  1 659 ? 0.079   69.001 42.896  1.00 14.81 ? 659  TRP B CZ2 1 
ATOM   11052 C  CZ3 . TRP B  1 659 ? 0.490   69.095 40.507  1.00 13.93 ? 659  TRP B CZ3 1 
ATOM   11053 C  CH2 . TRP B  1 659 ? -0.117  68.503 41.625  1.00 14.27 ? 659  TRP B CH2 1 
ATOM   11054 N  N   . GLU B  1 660 ? 6.144   73.219 40.003  1.00 14.78 ? 660  GLU B N   1 
ATOM   11055 C  CA  . GLU B  1 660 ? 6.834   73.757 38.849  1.00 15.75 ? 660  GLU B CA  1 
ATOM   11056 C  C   . GLU B  1 660 ? 7.316   72.647 37.906  1.00 14.91 ? 660  GLU B C   1 
ATOM   11057 O  O   . GLU B  1 660 ? 7.644   72.926 36.753  1.00 15.63 ? 660  GLU B O   1 
ATOM   11058 C  CB  . GLU B  1 660 ? 7.994   74.665 39.291  1.00 16.69 ? 660  GLU B CB  1 
ATOM   11059 C  CG  . GLU B  1 660 ? 7.502   76.063 39.649  1.00 19.91 ? 660  GLU B CG  1 
ATOM   11060 C  CD  . GLU B  1 660 ? 8.416   76.809 40.579  1.00 22.50 ? 660  GLU B CD  1 
ATOM   11061 O  OE1 . GLU B  1 660 ? 8.388   76.529 41.800  1.00 23.16 ? 660  GLU B OE1 1 
ATOM   11062 O  OE2 . GLU B  1 660 ? 9.163   77.687 40.091  1.00 24.89 ? 660  GLU B OE2 1 
ATOM   11063 N  N   . TYR B  1 661 ? 7.369   71.398 38.372  1.00 14.24 ? 661  TYR B N   1 
ATOM   11064 C  CA  . TYR B  1 661 ? 7.787   70.297 37.477  1.00 14.27 ? 661  TYR B CA  1 
ATOM   11065 C  C   . TYR B  1 661 ? 6.616   69.708 36.675  1.00 14.24 ? 661  TYR B C   1 
ATOM   11066 O  O   . TYR B  1 661 ? 6.840   68.965 35.705  1.00 15.67 ? 661  TYR B O   1 
ATOM   11067 C  CB  . TYR B  1 661 ? 8.424   69.115 38.227  1.00 13.95 ? 661  TYR B CB  1 
ATOM   11068 C  CG  . TYR B  1 661 ? 9.680   69.384 39.048  1.00 15.81 ? 661  TYR B CG  1 
ATOM   11069 C  CD1 . TYR B  1 661 ? 10.558  70.434 38.738  1.00 16.03 ? 661  TYR B CD1 1 
ATOM   11070 C  CD2 . TYR B  1 661 ? 9.985   68.574 40.150  1.00 15.72 ? 661  TYR B CD2 1 
ATOM   11071 C  CE1 . TYR B  1 661 ? 11.713  70.669 39.521  1.00 15.83 ? 661  TYR B CE1 1 
ATOM   11072 C  CE2 . TYR B  1 661 ? 11.125  68.800 40.939  1.00 16.53 ? 661  TYR B CE2 1 
ATOM   11073 C  CZ  . TYR B  1 661 ? 11.983  69.855 40.617  1.00 17.11 ? 661  TYR B CZ  1 
ATOM   11074 O  OH  . TYR B  1 661 ? 13.090  70.094 41.413  1.00 15.23 ? 661  TYR B OH  1 
ATOM   11075 N  N   . TYR B  1 662 ? 5.379   70.001 37.074  1.00 12.76 ? 662  TYR B N   1 
ATOM   11076 C  CA  . TYR B  1 662 ? 4.252   69.422 36.347  1.00 13.44 ? 662  TYR B CA  1 
ATOM   11077 C  C   . TYR B  1 662 ? 3.821   70.324 35.194  1.00 13.15 ? 662  TYR B C   1 
ATOM   11078 O  O   . TYR B  1 662 ? 4.279   71.461 35.105  1.00 12.46 ? 662  TYR B O   1 
ATOM   11079 C  CB  . TYR B  1 662 ? 3.073   69.099 37.284  1.00 12.13 ? 662  TYR B CB  1 
ATOM   11080 C  CG  . TYR B  1 662 ? 2.167   68.046 36.660  1.00 13.65 ? 662  TYR B CG  1 
ATOM   11081 C  CD1 . TYR B  1 662 ? 2.678   66.806 36.265  1.00 12.49 ? 662  TYR B CD1 1 
ATOM   11082 C  CD2 . TYR B  1 662 ? 0.828   68.321 36.390  1.00 13.17 ? 662  TYR B CD2 1 
ATOM   11083 C  CE1 . TYR B  1 662 ? 1.880   65.872 35.610  1.00 12.61 ? 662  TYR B CE1 1 
ATOM   11084 C  CE2 . TYR B  1 662 ? 0.024   67.405 35.738  1.00 12.70 ? 662  TYR B CE2 1 
ATOM   11085 C  CZ  . TYR B  1 662 ? 0.543   66.189 35.347  1.00 13.41 ? 662  TYR B CZ  1 
ATOM   11086 O  OH  . TYR B  1 662 ? -0.290  65.311 34.680  1.00 11.77 ? 662  TYR B OH  1 
ATOM   11087 N  N   . ASP B  1 663 ? 2.931   69.845 34.327  1.00 13.53 ? 663  ASP B N   1 
ATOM   11088 C  CA  . ASP B  1 663 ? 2.574   70.654 33.168  1.00 14.38 ? 663  ASP B CA  1 
ATOM   11089 C  C   . ASP B  1 663 ? 1.732   71.924 33.390  1.00 15.14 ? 663  ASP B C   1 
ATOM   11090 O  O   . ASP B  1 663 ? 1.018   72.059 34.385  1.00 15.35 ? 663  ASP B O   1 
ATOM   11091 C  CB  . ASP B  1 663 ? 1.957   69.777 32.052  1.00 14.07 ? 663  ASP B CB  1 
ATOM   11092 C  CG  . ASP B  1 663 ? 0.592   69.238 32.400  1.00 14.62 ? 663  ASP B CG  1 
ATOM   11093 O  OD1 . ASP B  1 663 ? -0.348  70.052 32.579  1.00 13.27 ? 663  ASP B OD1 1 
ATOM   11094 O  OD2 . ASP B  1 663 ? 0.463   67.996 32.487  1.00 14.81 ? 663  ASP B OD2 1 
ATOM   11095 N  N   . SER B  1 664 ? 1.843   72.863 32.452  1.00 15.87 ? 664  SER B N   1 
ATOM   11096 C  CA  . SER B  1 664 ? 1.131   74.137 32.528  1.00 16.31 ? 664  SER B CA  1 
ATOM   11097 C  C   . SER B  1 664 ? -0.407  74.074 32.641  1.00 16.26 ? 664  SER B C   1 
ATOM   11098 O  O   . SER B  1 664 ? -0.988  74.670 33.550  1.00 16.35 ? 664  SER B O   1 
ATOM   11099 C  CB  . SER B  1 664 ? 1.519   75.016 31.326  1.00 15.90 ? 664  SER B CB  1 
ATOM   11100 O  OG  . SER B  1 664 ? 1.214   74.399 30.086  1.00 17.76 ? 664  SER B OG  1 
ATOM   11101 N  N   . VAL B  1 665 ? -1.055  73.364 31.719  1.00 16.35 ? 665  VAL B N   1 
ATOM   11102 C  CA  . VAL B  1 665 ? -2.521  73.267 31.690  1.00 16.69 ? 665  VAL B CA  1 
ATOM   11103 C  C   . VAL B  1 665 ? -3.132  72.796 33.017  1.00 17.20 ? 665  VAL B C   1 
ATOM   11104 O  O   . VAL B  1 665 ? -3.987  73.471 33.601  1.00 16.94 ? 665  VAL B O   1 
ATOM   11105 C  CB  . VAL B  1 665 ? -2.977  72.322 30.540  1.00 16.33 ? 665  VAL B CB  1 
ATOM   11106 C  CG1 . VAL B  1 665 ? -4.511  72.244 30.482  1.00 16.75 ? 665  VAL B CG1 1 
ATOM   11107 C  CG2 . VAL B  1 665 ? -2.423  72.834 29.209  1.00 15.63 ? 665  VAL B CG2 1 
ATOM   11108 N  N   . TYR B  1 666 ? -2.691  71.647 33.503  1.00 16.67 ? 666  TYR B N   1 
ATOM   11109 C  CA  . TYR B  1 666 ? -3.229  71.139 34.750  1.00 17.31 ? 666  TYR B CA  1 
ATOM   11110 C  C   . TYR B  1 666 ? -2.826  72.006 35.957  1.00 17.01 ? 666  TYR B C   1 
ATOM   11111 O  O   . TYR B  1 666 ? -3.684  72.492 36.698  1.00 16.23 ? 666  TYR B O   1 
ATOM   11112 C  CB  . TYR B  1 666 ? -2.772  69.697 34.976  1.00 16.32 ? 666  TYR B CB  1 
ATOM   11113 C  CG  . TYR B  1 666 ? -3.244  69.093 36.289  1.00 16.33 ? 666  TYR B CG  1 
ATOM   11114 C  CD1 . TYR B  1 666 ? -2.578  69.366 37.493  1.00 16.89 ? 666  TYR B CD1 1 
ATOM   11115 C  CD2 . TYR B  1 666 ? -4.335  68.221 36.323  1.00 17.42 ? 666  TYR B CD2 1 
ATOM   11116 C  CE1 . TYR B  1 666 ? -2.986  68.770 38.702  1.00 16.19 ? 666  TYR B CE1 1 
ATOM   11117 C  CE2 . TYR B  1 666 ? -4.757  67.620 37.523  1.00 16.96 ? 666  TYR B CE2 1 
ATOM   11118 C  CZ  . TYR B  1 666 ? -4.078  67.893 38.698  1.00 17.00 ? 666  TYR B CZ  1 
ATOM   11119 O  OH  . TYR B  1 666 ? -4.464  67.247 39.848  1.00 17.75 ? 666  TYR B OH  1 
ATOM   11120 N  N   . THR B  1 667 ? -1.527  72.222 36.131  1.00 16.52 ? 667  THR B N   1 
ATOM   11121 C  CA  . THR B  1 667 ? -1.021  72.993 37.271  1.00 16.10 ? 667  THR B CA  1 
ATOM   11122 C  C   . THR B  1 667 ? -1.534  74.420 37.384  1.00 16.85 ? 667  THR B C   1 
ATOM   11123 O  O   . THR B  1 667 ? -2.000  74.835 38.448  1.00 16.82 ? 667  THR B O   1 
ATOM   11124 C  CB  . THR B  1 667 ? 0.507   73.065 37.255  1.00 15.28 ? 667  THR B CB  1 
ATOM   11125 O  OG1 . THR B  1 667 ? 1.021   71.769 36.953  1.00 15.34 ? 667  THR B OG1 1 
ATOM   11126 C  CG2 . THR B  1 667 ? 1.049   73.515 38.633  1.00 13.65 ? 667  THR B CG2 1 
ATOM   11127 N  N   . GLU B  1 668 ? -1.452  75.177 36.294  1.00 16.62 ? 668  GLU B N   1 
ATOM   11128 C  CA  . GLU B  1 668 ? -1.893  76.562 36.325  1.00 16.66 ? 668  GLU B CA  1 
ATOM   11129 C  C   . GLU B  1 668 ? -3.393  76.702 36.553  1.00 17.50 ? 668  GLU B C   1 
ATOM   11130 O  O   . GLU B  1 668 ? -3.846  77.740 37.046  1.00 16.60 ? 668  GLU B O   1 
ATOM   11131 C  CB  . GLU B  1 668 ? -1.473  77.270 35.038  1.00 16.41 ? 668  GLU B CB  1 
ATOM   11132 C  CG  . GLU B  1 668 ? 0.042   77.292 34.858  1.00 16.48 ? 668  GLU B CG  1 
ATOM   11133 C  CD  . GLU B  1 668 ? 0.469   77.805 33.507  1.00 16.29 ? 668  GLU B CD  1 
ATOM   11134 O  OE1 . GLU B  1 668 ? -0.371  78.393 32.784  1.00 15.51 ? 668  GLU B OE1 1 
ATOM   11135 O  OE2 . GLU B  1 668 ? 1.660   77.625 33.165  1.00 16.27 ? 668  GLU B OE2 1 
ATOM   11136 N  N   . ARG B  1 669 ? -4.163  75.661 36.224  1.00 17.25 ? 669  ARG B N   1 
ATOM   11137 C  CA  . ARG B  1 669 ? -5.602  75.749 36.432  1.00 17.23 ? 669  ARG B CA  1 
ATOM   11138 C  C   . ARG B  1 669 ? -5.923  75.919 37.905  1.00 17.53 ? 669  ARG B C   1 
ATOM   11139 O  O   . ARG B  1 669 ? -6.838  76.663 38.272  1.00 16.69 ? 669  ARG B O   1 
ATOM   11140 C  CB  . ARG B  1 669 ? -6.320  74.499 35.905  1.00 17.74 ? 669  ARG B CB  1 
ATOM   11141 C  CG  . ARG B  1 669 ? -7.830  74.546 36.166  1.00 18.10 ? 669  ARG B CG  1 
ATOM   11142 C  CD  . ARG B  1 669 ? -8.601  73.632 35.213  1.00 19.29 ? 669  ARG B CD  1 
ATOM   11143 N  NE  . ARG B  1 669 ? -8.235  72.259 35.415  1.00 20.57 ? 669  ARG B NE  1 
ATOM   11144 C  CZ  . ARG B  1 669 ? -7.692  71.462 34.493  1.00 19.77 ? 669  ARG B CZ  1 
ATOM   11145 N  NH1 . ARG B  1 669 ? -7.450  71.891 33.261  1.00 16.99 ? 669  ARG B NH1 1 
ATOM   11146 N  NH2 . ARG B  1 669 ? -7.363  70.223 34.837  1.00 17.42 ? 669  ARG B NH2 1 
ATOM   11147 N  N   . TYR B  1 670 ? -5.169  75.216 38.743  1.00 17.18 ? 670  TYR B N   1 
ATOM   11148 C  CA  . TYR B  1 670 ? -5.384  75.257 40.177  1.00 18.05 ? 670  TYR B CA  1 
ATOM   11149 C  C   . TYR B  1 670 ? -4.403  76.165 40.919  1.00 18.99 ? 670  TYR B C   1 
ATOM   11150 O  O   . TYR B  1 670 ? -4.718  76.681 41.988  1.00 19.60 ? 670  TYR B O   1 
ATOM   11151 C  CB  . TYR B  1 670 ? -5.251  73.852 40.767  1.00 16.57 ? 670  TYR B CB  1 
ATOM   11152 C  CG  . TYR B  1 670 ? -5.981  72.786 39.993  1.00 17.59 ? 670  TYR B CG  1 
ATOM   11153 C  CD1 . TYR B  1 670 ? -7.375  72.718 39.993  1.00 17.69 ? 670  TYR B CD1 1 
ATOM   11154 C  CD2 . TYR B  1 670 ? -5.278  71.881 39.205  1.00 16.47 ? 670  TYR B CD2 1 
ATOM   11155 C  CE1 . TYR B  1 670 ? -8.054  71.765 39.206  1.00 17.38 ? 670  TYR B CE1 1 
ATOM   11156 C  CE2 . TYR B  1 670 ? -5.934  70.936 38.423  1.00 16.47 ? 670  TYR B CE2 1 
ATOM   11157 C  CZ  . TYR B  1 670 ? -7.321  70.885 38.426  1.00 17.32 ? 670  TYR B CZ  1 
ATOM   11158 O  OH  . TYR B  1 670 ? -7.955  69.944 37.649  1.00 16.69 ? 670  TYR B OH  1 
ATOM   11159 N  N   . MET B  1 671 ? -3.231  76.380 40.338  1.00 19.53 ? 671  MET B N   1 
ATOM   11160 C  CA  . MET B  1 671 ? -2.186  77.147 40.998  1.00 18.85 ? 671  MET B CA  1 
ATOM   11161 C  C   . MET B  1 671 ? -1.827  78.492 40.408  1.00 19.65 ? 671  MET B C   1 
ATOM   11162 O  O   . MET B  1 671 ? -1.028  79.220 40.991  1.00 19.48 ? 671  MET B O   1 
ATOM   11163 C  CB  . MET B  1 671 ? -0.934  76.276 41.058  1.00 20.49 ? 671  MET B CB  1 
ATOM   11164 C  CG  . MET B  1 671 ? -1.067  75.081 41.992  1.00 19.81 ? 671  MET B CG  1 
ATOM   11165 S  SD  . MET B  1 671 ? -0.953  75.627 43.694  1.00 22.77 ? 671  MET B SD  1 
ATOM   11166 C  CE  . MET B  1 671 ? 0.852   75.692 43.860  1.00 21.73 ? 671  MET B CE  1 
ATOM   11167 N  N   . GLY B  1 672 ? -2.403  78.836 39.263  1.00 19.92 ? 672  GLY B N   1 
ATOM   11168 C  CA  . GLY B  1 672 ? -2.055  80.104 38.646  1.00 20.87 ? 672  GLY B CA  1 
ATOM   11169 C  C   . GLY B  1 672 ? -0.605  80.022 38.166  1.00 22.22 ? 672  GLY B C   1 
ATOM   11170 O  O   . GLY B  1 672 ? -0.113  78.924 37.913  1.00 21.76 ? 672  GLY B O   1 
ATOM   11171 N  N   . LEU B  1 673 ? 0.086   81.161 38.063  1.00 22.71 ? 673  LEU B N   1 
ATOM   11172 C  CA  . LEU B  1 673 ? 1.469   81.181 37.596  1.00 23.08 ? 673  LEU B CA  1 
ATOM   11173 C  C   . LEU B  1 673 ? 2.518   81.233 38.689  1.00 23.42 ? 673  LEU B C   1 
ATOM   11174 O  O   . LEU B  1 673 ? 2.329   81.869 39.716  1.00 24.28 ? 673  LEU B O   1 
ATOM   11175 C  CB  . LEU B  1 673 ? 1.683   82.352 36.658  1.00 23.17 ? 673  LEU B CB  1 
ATOM   11176 C  CG  . LEU B  1 673 ? 0.959   82.224 35.333  1.00 24.03 ? 673  LEU B CG  1 
ATOM   11177 C  CD1 . LEU B  1 673 ? 1.092   83.514 34.545  1.00 25.45 ? 673  LEU B CD1 1 
ATOM   11178 C  CD2 . LEU B  1 673 ? 1.561   81.071 34.557  1.00 23.82 ? 673  LEU B CD2 1 
ATOM   11179 N  N   . PRO B  1 674 ? 3.659   80.563 38.475  1.00 24.11 ? 674  PRO B N   1 
ATOM   11180 C  CA  . PRO B  1 674 ? 4.731   80.551 39.471  1.00 25.06 ? 674  PRO B CA  1 
ATOM   11181 C  C   . PRO B  1 674 ? 5.595   81.830 39.399  1.00 26.66 ? 674  PRO B C   1 
ATOM   11182 O  O   . PRO B  1 674 ? 6.795   81.772 39.151  1.00 26.29 ? 674  PRO B O   1 
ATOM   11183 C  CB  . PRO B  1 674 ? 5.502   79.283 39.103  1.00 24.72 ? 674  PRO B CB  1 
ATOM   11184 C  CG  . PRO B  1 674 ? 5.428   79.303 37.602  1.00 23.71 ? 674  PRO B CG  1 
ATOM   11185 C  CD  . PRO B  1 674 ? 3.979   79.672 37.338  1.00 24.15 ? 674  PRO B CD  1 
ATOM   11186 N  N   . THR B  1 675 ? 4.981   82.985 39.620  1.00 27.30 ? 675  THR B N   1 
ATOM   11187 C  CA  . THR B  1 675 ? 5.709   84.241 39.554  1.00 28.67 ? 675  THR B CA  1 
ATOM   11188 C  C   . THR B  1 675 ? 5.431   85.060 40.803  1.00 30.12 ? 675  THR B C   1 
ATOM   11189 O  O   . THR B  1 675 ? 4.364   84.946 41.416  1.00 29.98 ? 675  THR B O   1 
ATOM   11190 C  CB  . THR B  1 675 ? 5.293   85.064 38.306  1.00 29.00 ? 675  THR B CB  1 
ATOM   11191 O  OG1 . THR B  1 675 ? 3.913   85.440 38.418  1.00 28.67 ? 675  THR B OG1 1 
ATOM   11192 C  CG2 . THR B  1 675 ? 5.485   84.244 37.037  1.00 26.39 ? 675  THR B CG2 1 
ATOM   11193 N  N   . PRO B  1 676 ? 6.393   85.898 41.205  1.00 31.10 ? 676  PRO B N   1 
ATOM   11194 C  CA  . PRO B  1 676 ? 6.153   86.701 42.407  1.00 31.33 ? 676  PRO B CA  1 
ATOM   11195 C  C   . PRO B  1 676 ? 4.883   87.548 42.326  1.00 31.19 ? 676  PRO B C   1 
ATOM   11196 O  O   . PRO B  1 676 ? 4.214   87.744 43.338  1.00 30.74 ? 676  PRO B O   1 
ATOM   11197 C  CB  . PRO B  1 676 ? 7.436   87.524 42.549  1.00 31.80 ? 676  PRO B CB  1 
ATOM   11198 C  CG  . PRO B  1 676 ? 7.987   87.583 41.147  1.00 32.80 ? 676  PRO B CG  1 
ATOM   11199 C  CD  . PRO B  1 676 ? 7.694   86.212 40.586  1.00 32.05 ? 676  PRO B CD  1 
ATOM   11200 N  N   . GLU B  1 677 ? 4.515   88.013 41.135  1.00 31.44 ? 677  GLU B N   1 
ATOM   11201 C  CA  . GLU B  1 677 ? 3.300   88.820 41.041  1.00 32.17 ? 677  GLU B CA  1 
ATOM   11202 C  C   . GLU B  1 677 ? 2.035   87.965 41.097  1.00 31.08 ? 677  GLU B C   1 
ATOM   11203 O  O   . GLU B  1 677 ? 0.931   88.494 41.080  1.00 30.50 ? 677  GLU B O   1 
ATOM   11204 C  CB  . GLU B  1 677 ? 3.261   89.669 39.763  1.00 34.53 ? 677  GLU B CB  1 
ATOM   11205 C  CG  . GLU B  1 677 ? 4.606   90.094 39.221  1.00 38.60 ? 677  GLU B CG  1 
ATOM   11206 C  CD  . GLU B  1 677 ? 5.269   88.965 38.457  1.00 39.60 ? 677  GLU B CD  1 
ATOM   11207 O  OE1 . GLU B  1 677 ? 4.715   88.526 37.420  1.00 41.46 ? 677  GLU B OE1 1 
ATOM   11208 O  OE2 . GLU B  1 677 ? 6.336   88.517 38.903  1.00 41.13 ? 677  GLU B OE2 1 
ATOM   11209 N  N   . ASP B  1 678 ? 2.183   86.647 41.147  1.00 29.55 ? 678  ASP B N   1 
ATOM   11210 C  CA  . ASP B  1 678 ? 1.003   85.809 41.223  1.00 27.99 ? 678  ASP B CA  1 
ATOM   11211 C  C   . ASP B  1 678 ? 1.029   84.788 42.349  1.00 27.18 ? 678  ASP B C   1 
ATOM   11212 O  O   . ASP B  1 678 ? 0.665   85.111 43.470  1.00 28.35 ? 678  ASP B O   1 
ATOM   11213 C  CB  . ASP B  1 678 ? 0.725   85.110 39.883  1.00 27.41 ? 678  ASP B CB  1 
ATOM   11214 C  CG  . ASP B  1 678 ? -0.612  84.373 39.880  1.00 27.51 ? 678  ASP B CG  1 
ATOM   11215 O  OD1 . ASP B  1 678 ? -1.342  84.466 40.888  1.00 27.02 ? 678  ASP B OD1 1 
ATOM   11216 O  OD2 . ASP B  1 678 ? -0.937  83.704 38.874  1.00 28.09 ? 678  ASP B OD2 1 
ATOM   11217 N  N   . ASN B  1 679 ? 1.473   83.564 42.088  1.00 25.74 ? 679  ASN B N   1 
ATOM   11218 C  CA  . ASN B  1 679 ? 1.414   82.578 43.156  1.00 24.53 ? 679  ASN B CA  1 
ATOM   11219 C  C   . ASN B  1 679 ? 2.700   81.825 43.476  1.00 24.40 ? 679  ASN B C   1 
ATOM   11220 O  O   . ASN B  1 679 ? 2.657   80.750 44.079  1.00 24.22 ? 679  ASN B O   1 
ATOM   11221 C  CB  . ASN B  1 679 ? 0.280   81.600 42.833  1.00 22.46 ? 679  ASN B CB  1 
ATOM   11222 C  CG  . ASN B  1 679 ? -0.249  80.881 44.056  1.00 22.98 ? 679  ASN B CG  1 
ATOM   11223 O  OD1 . ASN B  1 679 ? -0.247  81.424 45.150  1.00 22.36 ? 679  ASN B OD1 1 
ATOM   11224 N  ND2 . ASN B  1 679 ? -0.735  79.652 43.865  1.00 22.21 ? 679  ASN B ND2 1 
ATOM   11225 N  N   . LEU B  1 680 ? 3.839   82.394 43.098  1.00 24.48 ? 680  LEU B N   1 
ATOM   11226 C  CA  . LEU B  1 680 ? 5.135   81.757 43.343  1.00 25.33 ? 680  LEU B CA  1 
ATOM   11227 C  C   . LEU B  1 680 ? 5.320   81.298 44.784  1.00 25.70 ? 680  LEU B C   1 
ATOM   11228 O  O   . LEU B  1 680 ? 5.775   80.178 45.041  1.00 25.43 ? 680  LEU B O   1 
ATOM   11229 C  CB  . LEU B  1 680 ? 6.272   82.713 42.991  1.00 25.71 ? 680  LEU B CB  1 
ATOM   11230 C  CG  . LEU B  1 680 ? 7.674   82.173 43.263  1.00 27.57 ? 680  LEU B CG  1 
ATOM   11231 C  CD1 . LEU B  1 680 ? 7.929   80.948 42.363  1.00 28.17 ? 680  LEU B CD1 1 
ATOM   11232 C  CD2 . LEU B  1 680 ? 8.717   83.261 42.994  1.00 28.25 ? 680  LEU B CD2 1 
ATOM   11233 N  N   . ASP B  1 681 ? 4.977   82.157 45.734  1.00 25.80 ? 681  ASP B N   1 
ATOM   11234 C  CA  . ASP B  1 681 ? 5.160   81.776 47.120  1.00 26.30 ? 681  ASP B CA  1 
ATOM   11235 C  C   . ASP B  1 681 ? 4.496   80.456 47.464  1.00 25.36 ? 681  ASP B C   1 
ATOM   11236 O  O   . ASP B  1 681 ? 5.100   79.622 48.139  1.00 24.16 ? 681  ASP B O   1 
ATOM   11237 C  CB  . ASP B  1 681 ? 4.681   82.890 48.050  1.00 27.92 ? 681  ASP B CB  1 
ATOM   11238 C  CG  . ASP B  1 681 ? 5.643   84.077 48.071  1.00 30.10 ? 681  ASP B CG  1 
ATOM   11239 O  OD1 . ASP B  1 681 ? 6.748   83.968 47.489  1.00 30.18 ? 681  ASP B OD1 1 
ATOM   11240 O  OD2 . ASP B  1 681 ? 5.302   85.114 48.679  1.00 32.04 ? 681  ASP B OD2 1 
ATOM   11241 N  N   . HIS B  1 682 ? 3.263   80.232 47.010  1.00 25.24 ? 682  HIS B N   1 
ATOM   11242 C  CA  . HIS B  1 682 ? 2.667   78.948 47.354  1.00 24.04 ? 682  HIS B CA  1 
ATOM   11243 C  C   . HIS B  1 682 ? 3.288   77.805 46.563  1.00 23.08 ? 682  HIS B C   1 
ATOM   11244 O  O   . HIS B  1 682 ? 3.342   76.682 47.051  1.00 22.37 ? 682  HIS B O   1 
ATOM   11245 C  CB  . HIS B  1 682 ? 1.157   78.901 47.183  1.00 24.76 ? 682  HIS B CB  1 
ATOM   11246 C  CG  . HIS B  1 682 ? 0.576   77.621 47.694  1.00 26.23 ? 682  HIS B CG  1 
ATOM   11247 N  ND1 . HIS B  1 682 ? 0.736   77.209 49.002  1.00 27.44 ? 682  HIS B ND1 1 
ATOM   11248 C  CD2 . HIS B  1 682 ? -0.054  76.606 47.057  1.00 25.42 ? 682  HIS B CD2 1 
ATOM   11249 C  CE1 . HIS B  1 682 ? 0.234   75.995 49.146  1.00 27.31 ? 682  HIS B CE1 1 
ATOM   11250 N  NE2 . HIS B  1 682 ? -0.251  75.607 47.980  1.00 25.50 ? 682  HIS B NE2 1 
ATOM   11251 N  N   . TYR B  1 683 ? 3.763   78.079 45.351  1.00 22.74 ? 683  TYR B N   1 
ATOM   11252 C  CA  . TYR B  1 683 ? 4.423   77.040 44.553  1.00 22.43 ? 683  TYR B CA  1 
ATOM   11253 C  C   . TYR B  1 683 ? 5.644   76.546 45.310  1.00 23.53 ? 683  TYR B C   1 
ATOM   11254 O  O   . TYR B  1 683 ? 5.913   75.347 45.349  1.00 24.78 ? 683  TYR B O   1 
ATOM   11255 C  CB  . TYR B  1 683 ? 4.917   77.588 43.212  1.00 21.50 ? 683  TYR B CB  1 
ATOM   11256 C  CG  . TYR B  1 683 ? 4.004   77.374 42.028  1.00 21.80 ? 683  TYR B CG  1 
ATOM   11257 C  CD1 . TYR B  1 683 ? 4.105   76.231 41.234  1.00 21.61 ? 683  TYR B CD1 1 
ATOM   11258 C  CD2 . TYR B  1 683 ? 3.088   78.355 41.652  1.00 21.10 ? 683  TYR B CD2 1 
ATOM   11259 C  CE1 . TYR B  1 683 ? 3.308   76.087 40.072  1.00 20.37 ? 683  TYR B CE1 1 
ATOM   11260 C  CE2 . TYR B  1 683 ? 2.301   78.223 40.514  1.00 21.54 ? 683  TYR B CE2 1 
ATOM   11261 C  CZ  . TYR B  1 683 ? 2.417   77.091 39.723  1.00 22.19 ? 683  TYR B CZ  1 
ATOM   11262 O  OH  . TYR B  1 683 ? 1.655   77.004 38.569  1.00 20.66 ? 683  TYR B OH  1 
ATOM   11263 N  N   . ARG B  1 684 ? 6.387   77.475 45.912  1.00 23.46 ? 684  ARG B N   1 
ATOM   11264 C  CA  . ARG B  1 684 ? 7.615   77.120 46.634  1.00 24.06 ? 684  ARG B CA  1 
ATOM   11265 C  C   . ARG B  1 684 ? 7.383   76.557 48.035  1.00 24.47 ? 684  ARG B C   1 
ATOM   11266 O  O   . ARG B  1 684 ? 8.232   75.867 48.589  1.00 24.74 ? 684  ARG B O   1 
ATOM   11267 C  CB  . ARG B  1 684 ? 8.557   78.346 46.694  1.00 24.12 ? 684  ARG B CB  1 
ATOM   11268 C  CG  . ARG B  1 684 ? 9.035   78.814 45.312  1.00 23.81 ? 684  ARG B CG  1 
ATOM   11269 C  CD  . ARG B  1 684 ? 9.858   77.714 44.636  1.00 26.79 ? 684  ARG B CD  1 
ATOM   11270 N  NE  . ARG B  1 684 ? 10.136  77.948 43.214  1.00 25.96 ? 684  ARG B NE  1 
ATOM   11271 C  CZ  . ARG B  1 684 ? 10.903  78.926 42.741  1.00 27.30 ? 684  ARG B CZ  1 
ATOM   11272 N  NH1 . ARG B  1 684 ? 11.484  79.790 43.573  1.00 26.36 ? 684  ARG B NH1 1 
ATOM   11273 N  NH2 . ARG B  1 684 ? 11.114  79.023 41.430  1.00 25.67 ? 684  ARG B NH2 1 
ATOM   11274 N  N   . ASN B  1 685 ? 6.205   76.820 48.579  1.00 25.57 ? 685  ASN B N   1 
ATOM   11275 C  CA  . ASN B  1 685 ? 5.847   76.382 49.914  1.00 25.56 ? 685  ASN B CA  1 
ATOM   11276 C  C   . ASN B  1 685 ? 5.175   75.003 49.952  1.00 24.64 ? 685  ASN B C   1 
ATOM   11277 O  O   . ASN B  1 685 ? 5.030   74.407 51.017  1.00 24.92 ? 685  ASN B O   1 
ATOM   11278 C  CB  . ASN B  1 685 ? 4.892   77.415 50.521  1.00 29.48 ? 685  ASN B CB  1 
ATOM   11279 C  CG  . ASN B  1 685 ? 5.158   77.662 51.980  1.00 33.36 ? 685  ASN B CG  1 
ATOM   11280 O  OD1 . ASN B  1 685 ? 4.230   77.886 52.767  1.00 36.76 ? 685  ASN B OD1 1 
ATOM   11281 N  ND2 . ASN B  1 685 ? 6.436   77.628 52.360  1.00 36.13 ? 685  ASN B ND2 1 
ATOM   11282 N  N   . SER B  1 686 ? 4.782   74.493 48.792  1.00 21.76 ? 686  SER B N   1 
ATOM   11283 C  CA  . SER B  1 686 ? 4.062   73.228 48.719  1.00 19.66 ? 686  SER B CA  1 
ATOM   11284 C  C   . SER B  1 686 ? 4.854   72.038 48.171  1.00 19.64 ? 686  SER B C   1 
ATOM   11285 O  O   . SER B  1 686 ? 4.276   71.067 47.668  1.00 18.82 ? 686  SER B O   1 
ATOM   11286 C  CB  . SER B  1 686 ? 2.789   73.431 47.877  1.00 19.30 ? 686  SER B CB  1 
ATOM   11287 O  OG  . SER B  1 686 ? 3.108   73.912 46.568  1.00 16.55 ? 686  SER B OG  1 
ATOM   11288 N  N   . THR B  1 687 ? 6.176   72.106 48.262  1.00 18.79 ? 687  THR B N   1 
ATOM   11289 C  CA  . THR B  1 687 ? 7.003   71.018 47.757  1.00 18.06 ? 687  THR B CA  1 
ATOM   11290 C  C   . THR B  1 687 ? 7.221   69.957 48.801  1.00 17.36 ? 687  THR B C   1 
ATOM   11291 O  O   . THR B  1 687 ? 7.217   70.237 49.993  1.00 18.40 ? 687  THR B O   1 
ATOM   11292 C  CB  . THR B  1 687 ? 8.407   71.483 47.353  1.00 18.42 ? 687  THR B CB  1 
ATOM   11293 O  OG1 . THR B  1 687 ? 9.155   71.800 48.534  1.00 19.29 ? 687  THR B OG1 1 
ATOM   11294 C  CG2 . THR B  1 687 ? 8.327   72.711 46.444  1.00 20.02 ? 687  THR B CG2 1 
ATOM   11295 N  N   . VAL B  1 688 ? 7.429   68.733 48.338  1.00 17.53 ? 688  VAL B N   1 
ATOM   11296 C  CA  . VAL B  1 688 ? 7.721   67.630 49.226  1.00 17.62 ? 688  VAL B CA  1 
ATOM   11297 C  C   . VAL B  1 688 ? 9.121   67.856 49.809  1.00 17.59 ? 688  VAL B C   1 
ATOM   11298 O  O   . VAL B  1 688 ? 9.341   67.658 51.010  1.00 17.73 ? 688  VAL B O   1 
ATOM   11299 C  CB  . VAL B  1 688 ? 7.679   66.260 48.458  1.00 16.92 ? 688  VAL B CB  1 
ATOM   11300 C  CG1 . VAL B  1 688 ? 8.194   65.116 49.343  1.00 14.77 ? 688  VAL B CG1 1 
ATOM   11301 C  CG2 . VAL B  1 688 ? 6.229   65.970 48.028  1.00 15.98 ? 688  VAL B CG2 1 
ATOM   11302 N  N   . MET B  1 689 ? 10.053  68.293 48.970  1.00 17.05 ? 689  MET B N   1 
ATOM   11303 C  CA  . MET B  1 689 ? 11.439  68.487 49.408  1.00 17.44 ? 689  MET B CA  1 
ATOM   11304 C  C   . MET B  1 689 ? 11.651  69.322 50.675  1.00 18.12 ? 689  MET B C   1 
ATOM   11305 O  O   . MET B  1 689 ? 12.554  69.031 51.469  1.00 16.73 ? 689  MET B O   1 
ATOM   11306 C  CB  . MET B  1 689 ? 12.284  69.095 48.271  1.00 16.57 ? 689  MET B CB  1 
ATOM   11307 C  CG  . MET B  1 689 ? 12.658  68.112 47.128  1.00 17.64 ? 689  MET B CG  1 
ATOM   11308 S  SD  . MET B  1 689 ? 11.283  67.524 46.059  1.00 16.13 ? 689  MET B SD  1 
ATOM   11309 C  CE  . MET B  1 689 ? 11.265  68.906 44.838  1.00 16.54 ? 689  MET B CE  1 
ATOM   11310 N  N   . SER B  1 690 ? 10.848  70.364 50.845  1.00 18.43 ? 690  SER B N   1 
ATOM   11311 C  CA  . SER B  1 690 ? 11.001  71.233 52.004  1.00 20.38 ? 690  SER B CA  1 
ATOM   11312 C  C   . SER B  1 690 ? 10.653  70.560 53.321  1.00 21.38 ? 690  SER B C   1 
ATOM   11313 O  O   . SER B  1 690 ? 10.918  71.116 54.381  1.00 22.13 ? 690  SER B O   1 
ATOM   11314 C  CB  . SER B  1 690 ? 10.153  72.499 51.853  1.00 20.31 ? 690  SER B CB  1 
ATOM   11315 O  OG  . SER B  1 690 ? 8.762   72.192 51.815  1.00 21.32 ? 690  SER B OG  1 
ATOM   11316 N  N   . ARG B  1 691 ? 10.077  69.367 53.266  1.00 21.28 ? 691  ARG B N   1 
ATOM   11317 C  CA  . ARG B  1 691 ? 9.681   68.659 54.482  1.00 20.54 ? 691  ARG B CA  1 
ATOM   11318 C  C   . ARG B  1 691 ? 10.561  67.452 54.760  1.00 19.94 ? 691  ARG B C   1 
ATOM   11319 O  O   . ARG B  1 691 ? 10.256  66.624 55.633  1.00 17.87 ? 691  ARG B O   1 
ATOM   11320 C  CB  . ARG B  1 691 ? 8.203   68.263 54.341  1.00 22.75 ? 691  ARG B CB  1 
ATOM   11321 C  CG  . ARG B  1 691 ? 7.342   69.534 54.245  1.00 24.89 ? 691  ARG B CG  1 
ATOM   11322 C  CD  . ARG B  1 691 ? 6.076   69.390 53.423  1.00 27.97 ? 691  ARG B CD  1 
ATOM   11323 N  NE  . ARG B  1 691 ? 4.987   68.772 54.151  1.00 29.95 ? 691  ARG B NE  1 
ATOM   11324 C  CZ  . ARG B  1 691 ? 3.801   69.339 54.367  1.00 30.66 ? 691  ARG B CZ  1 
ATOM   11325 N  NH1 . ARG B  1 691 ? 3.535   70.563 53.916  1.00 30.26 ? 691  ARG B NH1 1 
ATOM   11326 N  NH2 . ARG B  1 691 ? 2.867   68.659 55.024  1.00 27.93 ? 691  ARG B NH2 1 
ATOM   11327 N  N   . ALA B  1 692 ? 11.673  67.382 54.030  1.00 18.89 ? 692  ALA B N   1 
ATOM   11328 C  CA  . ALA B  1 692 ? 12.605  66.256 54.128  1.00 20.83 ? 692  ALA B CA  1 
ATOM   11329 C  C   . ALA B  1 692 ? 12.993  65.864 55.558  1.00 21.44 ? 692  ALA B C   1 
ATOM   11330 O  O   . ALA B  1 692 ? 12.941  64.692 55.937  1.00 21.98 ? 692  ALA B O   1 
ATOM   11331 C  CB  . ALA B  1 692 ? 13.850  66.561 53.324  1.00 19.54 ? 692  ALA B CB  1 
ATOM   11332 N  N   . GLU B  1 693 ? 13.358  66.859 56.352  1.00 23.09 ? 693  GLU B N   1 
ATOM   11333 C  CA  . GLU B  1 693 ? 13.779  66.623 57.713  1.00 24.77 ? 693  GLU B CA  1 
ATOM   11334 C  C   . GLU B  1 693 ? 12.728  65.865 58.525  1.00 24.44 ? 693  GLU B C   1 
ATOM   11335 O  O   . GLU B  1 693 ? 13.072  65.059 59.375  1.00 24.43 ? 693  GLU B O   1 
ATOM   11336 C  CB  . GLU B  1 693 ? 14.116  67.955 58.389  1.00 26.70 ? 693  GLU B CB  1 
ATOM   11337 C  CG  . GLU B  1 693 ? 14.547  67.807 59.845  1.00 31.19 ? 693  GLU B CG  1 
ATOM   11338 C  CD  . GLU B  1 693 ? 15.966  67.300 59.987  1.00 33.25 ? 693  GLU B CD  1 
ATOM   11339 O  OE1 . GLU B  1 693 ? 16.344  66.892 61.105  1.00 35.48 ? 693  GLU B OE1 1 
ATOM   11340 O  OE2 . GLU B  1 693 ? 16.706  67.322 58.981  1.00 35.38 ? 693  GLU B OE2 1 
ATOM   11341 N  N   . ASN B  1 694 ? 11.447  66.104 58.267  1.00 24.86 ? 694  ASN B N   1 
ATOM   11342 C  CA  . ASN B  1 694 ? 10.407  65.411 59.027  1.00 24.51 ? 694  ASN B CA  1 
ATOM   11343 C  C   . ASN B  1 694 ? 10.281  63.950 58.690  1.00 24.12 ? 694  ASN B C   1 
ATOM   11344 O  O   . ASN B  1 694 ? 9.645   63.214 59.433  1.00 24.13 ? 694  ASN B O   1 
ATOM   11345 C  CB  . ASN B  1 694 ? 9.042   66.077 58.861  1.00 25.80 ? 694  ASN B CB  1 
ATOM   11346 C  CG  . ASN B  1 694 ? 8.954   67.386 59.607  1.00 28.15 ? 694  ASN B CG  1 
ATOM   11347 O  OD1 . ASN B  1 694 ? 9.601   67.554 60.647  1.00 30.40 ? 694  ASN B OD1 1 
ATOM   11348 N  ND2 . ASN B  1 694 ? 8.167   68.319 59.095  1.00 28.02 ? 694  ASN B ND2 1 
ATOM   11349 N  N   . PHE B  1 695 ? 10.889  63.517 57.583  1.00 22.87 ? 695  PHE B N   1 
ATOM   11350 C  CA  . PHE B  1 695 ? 10.816  62.114 57.193  1.00 22.06 ? 695  PHE B CA  1 
ATOM   11351 C  C   . PHE B  1 695 ? 11.636  61.235 58.122  1.00 22.52 ? 695  PHE B C   1 
ATOM   11352 O  O   . PHE B  1 695 ? 11.562  60.014 58.060  1.00 20.96 ? 695  PHE B O   1 
ATOM   11353 C  CB  . PHE B  1 695 ? 11.287  61.924 55.746  1.00 20.43 ? 695  PHE B CB  1 
ATOM   11354 C  CG  . PHE B  1 695 ? 10.233  62.249 54.719  1.00 18.08 ? 695  PHE B CG  1 
ATOM   11355 C  CD1 . PHE B  1 695 ? 9.584   61.236 54.037  1.00 16.16 ? 695  PHE B CD1 1 
ATOM   11356 C  CD2 . PHE B  1 695 ? 9.902   63.564 54.438  1.00 17.12 ? 695  PHE B CD2 1 
ATOM   11357 C  CE1 . PHE B  1 695 ? 8.611   61.528 53.077  1.00 17.41 ? 695  PHE B CE1 1 
ATOM   11358 C  CE2 . PHE B  1 695 ? 8.926   63.874 53.476  1.00 17.46 ? 695  PHE B CE2 1 
ATOM   11359 C  CZ  . PHE B  1 695 ? 8.285   62.847 52.800  1.00 15.98 ? 695  PHE B CZ  1 
ATOM   11360 N  N   . LYS B  1 696 ? 12.426  61.854 58.986  1.00 23.93 ? 696  LYS B N   1 
ATOM   11361 C  CA  . LYS B  1 696 ? 13.210  61.066 59.931  1.00 26.74 ? 696  LYS B CA  1 
ATOM   11362 C  C   . LYS B  1 696 ? 12.275  60.349 60.916  1.00 27.04 ? 696  LYS B C   1 
ATOM   11363 O  O   . LYS B  1 696 ? 12.695  59.437 61.604  1.00 27.33 ? 696  LYS B O   1 
ATOM   11364 C  CB  . LYS B  1 696 ? 14.155  61.975 60.722  1.00 28.34 ? 696  LYS B CB  1 
ATOM   11365 C  CG  . LYS B  1 696 ? 15.411  62.342 59.960  1.00 30.92 ? 696  LYS B CG  1 
ATOM   11366 C  CD  . LYS B  1 696 ? 16.232  63.410 60.673  1.00 33.03 ? 696  LYS B CD  1 
ATOM   11367 C  CE  . LYS B  1 696 ? 17.536  63.685 59.914  1.00 34.08 ? 696  LYS B CE  1 
ATOM   11368 N  NZ  . LYS B  1 696 ? 18.177  64.963 60.343  1.00 36.39 ? 696  LYS B NZ  1 
ATOM   11369 N  N   . GLN B  1 697 ? 11.009  60.762 60.959  1.00 26.71 ? 697  GLN B N   1 
ATOM   11370 C  CA  . GLN B  1 697 ? 10.033  60.196 61.888  1.00 27.39 ? 697  GLN B CA  1 
ATOM   11371 C  C   . GLN B  1 697 ? 9.219   59.009 61.339  1.00 26.17 ? 697  GLN B C   1 
ATOM   11372 O  O   . GLN B  1 697 ? 8.466   58.362 62.093  1.00 26.15 ? 697  GLN B O   1 
ATOM   11373 C  CB  . GLN B  1 697 ? 9.053   61.298 62.355  1.00 29.24 ? 697  GLN B CB  1 
ATOM   11374 C  CG  . GLN B  1 697 ? 9.694   62.565 62.950  1.00 33.42 ? 697  GLN B CG  1 
ATOM   11375 C  CD  . GLN B  1 697 ? 8.700   63.748 63.088  1.00 36.45 ? 697  GLN B CD  1 
ATOM   11376 O  OE1 . GLN B  1 697 ? 7.785   63.724 63.919  1.00 37.61 ? 697  GLN B OE1 1 
ATOM   11377 N  NE2 . GLN B  1 697 ? 8.887   64.781 62.264  1.00 36.72 ? 697  GLN B NE2 1 
ATOM   11378 N  N   . VAL B  1 698 ? 9.378   58.700 60.051  1.00 23.69 ? 698  VAL B N   1 
ATOM   11379 C  CA  . VAL B  1 698 ? 8.608   57.617 59.427  1.00 20.85 ? 698  VAL B CA  1 
ATOM   11380 C  C   . VAL B  1 698 ? 9.395   56.665 58.523  1.00 21.63 ? 698  VAL B C   1 
ATOM   11381 O  O   . VAL B  1 698 ? 10.555  56.919 58.186  1.00 19.68 ? 698  VAL B O   1 
ATOM   11382 C  CB  . VAL B  1 698 ? 7.487   58.195 58.546  1.00 20.53 ? 698  VAL B CB  1 
ATOM   11383 C  CG1 . VAL B  1 698 ? 6.634   59.191 59.336  1.00 19.19 ? 698  VAL B CG1 1 
ATOM   11384 C  CG2 . VAL B  1 698 ? 8.094   58.852 57.314  1.00 18.15 ? 698  VAL B CG2 1 
ATOM   11385 N  N   . GLU B  1 699 ? 8.742   55.566 58.144  1.00 20.91 ? 699  GLU B N   1 
ATOM   11386 C  CA  . GLU B  1 699 ? 9.309   54.599 57.206  1.00 22.08 ? 699  GLU B CA  1 
ATOM   11387 C  C   . GLU B  1 699 ? 8.667   54.968 55.871  1.00 21.05 ? 699  GLU B C   1 
ATOM   11388 O  O   . GLU B  1 699 ? 7.439   54.962 55.748  1.00 19.30 ? 699  GLU B O   1 
ATOM   11389 C  CB  . GLU B  1 699 ? 8.941   53.175 57.593  1.00 24.44 ? 699  GLU B CB  1 
ATOM   11390 C  CG  . GLU B  1 699 ? 9.696   52.688 58.818  1.00 28.92 ? 699  GLU B CG  1 
ATOM   11391 C  CD  . GLU B  1 699 ? 9.236   51.311 59.243  1.00 32.21 ? 699  GLU B CD  1 
ATOM   11392 O  OE1 . GLU B  1 699 ? 9.302   50.378 58.404  1.00 33.15 ? 699  GLU B OE1 1 
ATOM   11393 O  OE2 . GLU B  1 699 ? 8.804   51.172 60.411  1.00 33.03 ? 699  GLU B OE2 1 
ATOM   11394 N  N   . TYR B  1 700 ? 9.506   55.309 54.898  1.00 18.56 ? 700  TYR B N   1 
ATOM   11395 C  CA  . TYR B  1 700 ? 9.058   55.744 53.576  1.00 17.77 ? 700  TYR B CA  1 
ATOM   11396 C  C   . TYR B  1 700 ? 9.577   54.848 52.460  1.00 17.06 ? 700  TYR B C   1 
ATOM   11397 O  O   . TYR B  1 700 ? 10.737  54.428 52.486  1.00 15.90 ? 700  TYR B O   1 
ATOM   11398 C  CB  . TYR B  1 700 ? 9.563   57.175 53.351  1.00 17.13 ? 700  TYR B CB  1 
ATOM   11399 C  CG  . TYR B  1 700 ? 9.170   57.875 52.064  1.00 17.22 ? 700  TYR B CG  1 
ATOM   11400 C  CD1 . TYR B  1 700 ? 7.840   57.942 51.653  1.00 16.16 ? 700  TYR B CD1 1 
ATOM   11401 C  CD2 . TYR B  1 700 ? 10.118  58.630 51.348  1.00 17.46 ? 700  TYR B CD2 1 
ATOM   11402 C  CE1 . TYR B  1 700 ? 7.454   58.755 50.573  1.00 16.50 ? 700  TYR B CE1 1 
ATOM   11403 C  CE2 . TYR B  1 700 ? 9.740   59.444 50.269  1.00 16.28 ? 700  TYR B CE2 1 
ATOM   11404 C  CZ  . TYR B  1 700 ? 8.402   59.503 49.896  1.00 16.59 ? 700  TYR B CZ  1 
ATOM   11405 O  OH  . TYR B  1 700 ? 8.003   60.356 48.889  1.00 15.71 ? 700  TYR B OH  1 
ATOM   11406 N  N   . LEU B  1 701 ? 8.710   54.563 51.490  1.00 15.98 ? 701  LEU B N   1 
ATOM   11407 C  CA  . LEU B  1 701 ? 9.066   53.769 50.325  1.00 15.51 ? 701  LEU B CA  1 
ATOM   11408 C  C   . LEU B  1 701 ? 8.697   54.636 49.140  1.00 16.61 ? 701  LEU B C   1 
ATOM   11409 O  O   . LEU B  1 701 ? 7.523   55.004 48.986  1.00 17.46 ? 701  LEU B O   1 
ATOM   11410 C  CB  . LEU B  1 701 ? 8.274   52.459 50.284  1.00 14.91 ? 701  LEU B CB  1 
ATOM   11411 C  CG  . LEU B  1 701 ? 8.344   51.611 48.988  1.00 13.72 ? 701  LEU B CG  1 
ATOM   11412 C  CD1 . LEU B  1 701 ? 9.782   51.377 48.555  1.00 13.42 ? 701  LEU B CD1 1 
ATOM   11413 C  CD2 . LEU B  1 701 ? 7.647   50.271 49.245  1.00 12.58 ? 701  LEU B CD2 1 
ATOM   11414 N  N   . LEU B  1 702 ? 9.685   54.965 48.308  1.00 16.41 ? 702  LEU B N   1 
ATOM   11415 C  CA  . LEU B  1 702 ? 9.480   55.830 47.127  1.00 15.10 ? 702  LEU B CA  1 
ATOM   11416 C  C   . LEU B  1 702 ? 9.667   54.974 45.885  1.00 14.80 ? 702  LEU B C   1 
ATOM   11417 O  O   . LEU B  1 702 ? 10.656  54.257 45.776  1.00 15.71 ? 702  LEU B O   1 
ATOM   11418 C  CB  . LEU B  1 702 ? 10.509  56.965 47.141  1.00 14.16 ? 702  LEU B CB  1 
ATOM   11419 C  CG  . LEU B  1 702 ? 10.482  57.998 46.019  1.00 15.36 ? 702  LEU B CG  1 
ATOM   11420 C  CD1 . LEU B  1 702 ? 9.170   58.778 46.055  1.00 12.51 ? 702  LEU B CD1 1 
ATOM   11421 C  CD2 . LEU B  1 702 ? 11.677  58.967 46.177  1.00 15.90 ? 702  LEU B CD2 1 
ATOM   11422 N  N   . ILE B  1 703 ? 8.732   55.079 44.942  1.00 14.75 ? 703  ILE B N   1 
ATOM   11423 C  CA  . ILE B  1 703 ? 8.740   54.262 43.733  1.00 14.97 ? 703  ILE B CA  1 
ATOM   11424 C  C   . ILE B  1 703 ? 8.411   55.103 42.490  1.00 14.47 ? 703  ILE B C   1 
ATOM   11425 O  O   . ILE B  1 703 ? 7.501   55.923 42.523  1.00 14.18 ? 703  ILE B O   1 
ATOM   11426 C  CB  . ILE B  1 703 ? 7.670   53.126 43.877  1.00 14.58 ? 703  ILE B CB  1 
ATOM   11427 C  CG1 . ILE B  1 703 ? 7.964   52.295 45.142  1.00 16.27 ? 703  ILE B CG1 1 
ATOM   11428 C  CG2 . ILE B  1 703 ? 7.634   52.247 42.640  1.00 13.87 ? 703  ILE B CG2 1 
ATOM   11429 C  CD1 . ILE B  1 703 ? 6.892   51.247 45.490  1.00 15.52 ? 703  ILE B CD1 1 
ATOM   11430 N  N   . HIS B  1 704 ? 9.116   54.878 41.387  1.00 13.62 ? 704  HIS B N   1 
ATOM   11431 C  CA  . HIS B  1 704 ? 8.862   55.665 40.171  1.00 13.56 ? 704  HIS B CA  1 
ATOM   11432 C  C   . HIS B  1 704 ? 9.349   54.934 38.900  1.00 13.31 ? 704  HIS B C   1 
ATOM   11433 O  O   . HIS B  1 704 ? 10.385  54.275 38.909  1.00 13.11 ? 704  HIS B O   1 
ATOM   11434 C  CB  . HIS B  1 704 ? 9.581   57.031 40.287  1.00 10.85 ? 704  HIS B CB  1 
ATOM   11435 C  CG  . HIS B  1 704 ? 8.839   58.174 39.657  1.00 12.01 ? 704  HIS B CG  1 
ATOM   11436 N  ND1 . HIS B  1 704 ? 8.460   59.295 40.371  1.00 11.65 ? 704  HIS B ND1 1 
ATOM   11437 C  CD2 . HIS B  1 704 ? 8.402   58.371 38.387  1.00 11.04 ? 704  HIS B CD2 1 
ATOM   11438 C  CE1 . HIS B  1 704 ? 7.820   60.130 39.571  1.00 12.39 ? 704  HIS B CE1 1 
ATOM   11439 N  NE2 . HIS B  1 704 ? 7.770   59.593 38.361  1.00 13.03 ? 704  HIS B NE2 1 
ATOM   11440 N  N   . GLY B  1 705 ? 8.604   55.052 37.805  1.00 13.63 ? 705  GLY B N   1 
ATOM   11441 C  CA  . GLY B  1 705 ? 9.046   54.423 36.576  1.00 12.89 ? 705  GLY B CA  1 
ATOM   11442 C  C   . GLY B  1 705 ? 9.984   55.404 35.890  1.00 13.05 ? 705  GLY B C   1 
ATOM   11443 O  O   . GLY B  1 705 ? 9.706   56.599 35.843  1.00 12.44 ? 705  GLY B O   1 
ATOM   11444 N  N   . THR B  1 706 ? 11.100  54.923 35.359  1.00 13.69 ? 706  THR B N   1 
ATOM   11445 C  CA  . THR B  1 706 ? 12.060  55.824 34.715  1.00 13.57 ? 706  THR B CA  1 
ATOM   11446 C  C   . THR B  1 706 ? 11.601  56.449 33.392  1.00 14.44 ? 706  THR B C   1 
ATOM   11447 O  O   . THR B  1 706 ? 12.132  57.481 32.978  1.00 14.12 ? 706  THR B O   1 
ATOM   11448 C  CB  . THR B  1 706 ? 13.417  55.108 34.497  1.00 14.51 ? 706  THR B CB  1 
ATOM   11449 O  OG1 . THR B  1 706 ? 13.263  54.021 33.566  1.00 13.52 ? 706  THR B OG1 1 
ATOM   11450 C  CG2 . THR B  1 706 ? 13.918  54.539 35.831  1.00 13.57 ? 706  THR B CG2 1 
ATOM   11451 N  N   . ALA B  1 707 ? 10.615  55.848 32.728  1.00 12.37 ? 707  ALA B N   1 
ATOM   11452 C  CA  . ALA B  1 707 ? 10.143  56.406 31.464  1.00 12.98 ? 707  ALA B CA  1 
ATOM   11453 C  C   . ALA B  1 707 ? 8.785   57.083 31.632  1.00 13.63 ? 707  ALA B C   1 
ATOM   11454 O  O   . ALA B  1 707 ? 7.958   57.086 30.702  1.00 12.20 ? 707  ALA B O   1 
ATOM   11455 C  CB  . ALA B  1 707 ? 10.051  55.317 30.383  1.00 10.86 ? 707  ALA B CB  1 
ATOM   11456 N  N   . ASP B  1 708 ? 8.558   57.643 32.817  1.00 12.88 ? 708  ASP B N   1 
ATOM   11457 C  CA  . ASP B  1 708 ? 7.306   58.338 33.109  1.00 14.43 ? 708  ASP B CA  1 
ATOM   11458 C  C   . ASP B  1 708 ? 7.313   59.684 32.374  1.00 14.67 ? 708  ASP B C   1 
ATOM   11459 O  O   . ASP B  1 708 ? 8.025   60.615 32.752  1.00 13.25 ? 708  ASP B O   1 
ATOM   11460 C  CB  . ASP B  1 708 ? 7.168   58.567 34.619  1.00 13.59 ? 708  ASP B CB  1 
ATOM   11461 C  CG  . ASP B  1 708 ? 5.759   58.936 35.034  1.00 14.45 ? 708  ASP B CG  1 
ATOM   11462 O  OD1 . ASP B  1 708 ? 5.055   59.662 34.290  1.00 16.40 ? 708  ASP B OD1 1 
ATOM   11463 O  OD2 . ASP B  1 708 ? 5.353   58.519 36.137  1.00 12.60 ? 708  ASP B OD2 1 
ATOM   11464 N  N   . ASP B  1 709 ? 6.515   59.767 31.313  1.00 13.63 ? 709  ASP B N   1 
ATOM   11465 C  CA  . ASP B  1 709 ? 6.413   60.968 30.492  1.00 14.16 ? 709  ASP B CA  1 
ATOM   11466 C  C   . ASP B  1 709 ? 5.479   61.994 31.111  1.00 14.20 ? 709  ASP B C   1 
ATOM   11467 O  O   . ASP B  1 709 ? 5.471   63.142 30.699  1.00 15.17 ? 709  ASP B O   1 
ATOM   11468 C  CB  . ASP B  1 709 ? 5.830   60.604 29.134  1.00 14.78 ? 709  ASP B CB  1 
ATOM   11469 C  CG  . ASP B  1 709 ? 4.460   59.921 29.265  1.00 16.98 ? 709  ASP B CG  1 
ATOM   11470 O  OD1 . ASP B  1 709 ? 4.423   58.727 29.645  1.00 15.85 ? 709  ASP B OD1 1 
ATOM   11471 O  OD2 . ASP B  1 709 ? 3.428   60.578 29.000  1.00 17.46 ? 709  ASP B OD2 1 
ATOM   11472 N  N   . ASN B  1 710 ? 4.685   61.558 32.081  1.00 14.78 ? 710  ASN B N   1 
ATOM   11473 C  CA  . ASN B  1 710 ? 3.677   62.399 32.739  1.00 15.94 ? 710  ASN B CA  1 
ATOM   11474 C  C   . ASN B  1 710 ? 4.234   63.132 33.975  1.00 15.62 ? 710  ASN B C   1 
ATOM   11475 O  O   . ASN B  1 710 ? 4.396   64.350 33.955  1.00 15.60 ? 710  ASN B O   1 
ATOM   11476 C  CB  . ASN B  1 710 ? 2.501   61.496 33.114  1.00 16.22 ? 710  ASN B CB  1 
ATOM   11477 C  CG  . ASN B  1 710 ? 1.261   62.265 33.480  1.00 16.92 ? 710  ASN B CG  1 
ATOM   11478 O  OD1 . ASN B  1 710 ? 1.316   63.439 33.820  1.00 13.79 ? 710  ASN B OD1 1 
ATOM   11479 N  ND2 . ASN B  1 710 ? 0.123   61.585 33.434  1.00 18.63 ? 710  ASN B ND2 1 
ATOM   11480 N  N   . VAL B  1 711 ? 4.465   62.391 35.059  1.00 15.79 ? 711  VAL B N   1 
ATOM   11481 C  CA  . VAL B  1 711 ? 5.077   62.927 36.286  1.00 14.29 ? 711  VAL B CA  1 
ATOM   11482 C  C   . VAL B  1 711 ? 6.521   62.444 36.081  1.00 14.21 ? 711  VAL B C   1 
ATOM   11483 O  O   . VAL B  1 711 ? 6.828   61.273 36.294  1.00 14.34 ? 711  VAL B O   1 
ATOM   11484 C  CB  . VAL B  1 711 ? 4.459   62.276 37.545  1.00 14.33 ? 711  VAL B CB  1 
ATOM   11485 C  CG1 . VAL B  1 711 ? 5.174   62.778 38.821  1.00 12.68 ? 711  VAL B CG1 1 
ATOM   11486 C  CG2 . VAL B  1 711 ? 2.953   62.611 37.607  1.00 14.06 ? 711  VAL B CG2 1 
ATOM   11487 N  N   . HIS B  1 712 ? 7.408   63.340 35.663  1.00 14.49 ? 712  HIS B N   1 
ATOM   11488 C  CA  . HIS B  1 712 ? 8.770   62.919 35.343  1.00 15.01 ? 712  HIS B CA  1 
ATOM   11489 C  C   . HIS B  1 712 ? 9.533   62.296 36.500  1.00 14.07 ? 712  HIS B C   1 
ATOM   11490 O  O   . HIS B  1 712 ? 9.361   62.688 37.647  1.00 13.73 ? 712  HIS B O   1 
ATOM   11491 C  CB  . HIS B  1 712 ? 9.542   64.086 34.703  1.00 14.10 ? 712  HIS B CB  1 
ATOM   11492 C  CG  . HIS B  1 712 ? 8.786   64.747 33.587  1.00 14.97 ? 712  HIS B CG  1 
ATOM   11493 N  ND1 . HIS B  1 712 ? 8.127   64.024 32.609  1.00 17.12 ? 712  HIS B ND1 1 
ATOM   11494 C  CD2 . HIS B  1 712 ? 8.493   66.046 33.352  1.00 12.45 ? 712  HIS B CD2 1 
ATOM   11495 C  CE1 . HIS B  1 712 ? 7.452   64.853 31.828  1.00 15.74 ? 712  HIS B CE1 1 
ATOM   11496 N  NE2 . HIS B  1 712 ? 7.657   66.087 32.262  1.00 16.51 ? 712  HIS B NE2 1 
ATOM   11497 N  N   . PHE B  1 713 ? 10.341  61.285 36.183  1.00 14.00 ? 713  PHE B N   1 
ATOM   11498 C  CA  . PHE B  1 713 ? 11.143  60.589 37.191  1.00 13.65 ? 713  PHE B CA  1 
ATOM   11499 C  C   . PHE B  1 713 ? 11.860  61.664 38.004  1.00 14.85 ? 713  PHE B C   1 
ATOM   11500 O  O   . PHE B  1 713 ? 12.169  61.469 39.179  1.00 15.44 ? 713  PHE B O   1 
ATOM   11501 C  CB  . PHE B  1 713 ? 12.170  59.663 36.521  1.00 13.30 ? 713  PHE B CB  1 
ATOM   11502 C  CG  . PHE B  1 713 ? 13.005  58.867 37.502  1.00 13.70 ? 713  PHE B CG  1 
ATOM   11503 C  CD1 . PHE B  1 713 ? 12.501  57.705 38.081  1.00 13.91 ? 713  PHE B CD1 1 
ATOM   11504 C  CD2 . PHE B  1 713 ? 14.271  59.307 37.880  1.00 12.64 ? 713  PHE B CD2 1 
ATOM   11505 C  CE1 . PHE B  1 713 ? 13.255  56.983 39.042  1.00 14.17 ? 713  PHE B CE1 1 
ATOM   11506 C  CE2 . PHE B  1 713 ? 15.034  58.601 38.831  1.00 14.16 ? 713  PHE B CE2 1 
ATOM   11507 C  CZ  . PHE B  1 713 ? 14.522  57.438 39.413  1.00 14.77 ? 713  PHE B CZ  1 
ATOM   11508 N  N   . GLN B  1 714 ? 12.115  62.797 37.346  1.00 14.54 ? 714  GLN B N   1 
ATOM   11509 C  CA  . GLN B  1 714 ? 12.753  63.959 37.959  1.00 15.06 ? 714  GLN B CA  1 
ATOM   11510 C  C   . GLN B  1 714 ? 12.121  64.264 39.320  1.00 13.87 ? 714  GLN B C   1 
ATOM   11511 O  O   . GLN B  1 714 ? 12.819  64.550 40.290  1.00 14.87 ? 714  GLN B O   1 
ATOM   11512 C  CB  . GLN B  1 714 ? 12.581  65.188 37.045  1.00 13.07 ? 714  GLN B CB  1 
ATOM   11513 C  CG  . GLN B  1 714 ? 12.730  66.553 37.742  1.00 13.85 ? 714  GLN B CG  1 
ATOM   11514 C  CD  . GLN B  1 714 ? 12.197  67.687 36.898  1.00 16.16 ? 714  GLN B CD  1 
ATOM   11515 O  OE1 . GLN B  1 714 ? 11.106  67.570 36.312  1.00 15.45 ? 714  GLN B OE1 1 
ATOM   11516 N  NE2 . GLN B  1 714 ? 12.941  68.803 36.839  1.00 12.43 ? 714  GLN B NE2 1 
ATOM   11517 N  N   . GLN B  1 715 ? 10.798  64.213 39.385  1.00 13.54 ? 715  GLN B N   1 
ATOM   11518 C  CA  . GLN B  1 715 ? 10.083  64.527 40.619  1.00 12.34 ? 715  GLN B CA  1 
ATOM   11519 C  C   . GLN B  1 715 ? 10.561  63.664 41.796  1.00 12.75 ? 715  GLN B C   1 
ATOM   11520 O  O   . GLN B  1 715 ? 10.781  64.183 42.894  1.00 11.75 ? 715  GLN B O   1 
ATOM   11521 C  CB  . GLN B  1 715 ? 8.575   64.392 40.364  1.00 13.56 ? 715  GLN B CB  1 
ATOM   11522 C  CG  . GLN B  1 715 ? 8.152   65.247 39.145  1.00 13.74 ? 715  GLN B CG  1 
ATOM   11523 C  CD  . GLN B  1 715 ? 7.010   66.194 39.426  1.00 13.67 ? 715  GLN B CD  1 
ATOM   11524 O  OE1 . GLN B  1 715 ? 6.884   66.702 40.540  1.00 14.92 ? 715  GLN B OE1 1 
ATOM   11525 N  NE2 . GLN B  1 715 ? 6.174   66.456 38.410  1.00 12.36 ? 715  GLN B NE2 1 
ATOM   11526 N  N   . SER B  1 716 ? 10.730  62.361 41.583  1.00 12.43 ? 716  SER B N   1 
ATOM   11527 C  CA  . SER B  1 716 ? 11.224  61.509 42.664  1.00 13.77 ? 716  SER B CA  1 
ATOM   11528 C  C   . SER B  1 716 ? 12.741  61.627 42.829  1.00 14.59 ? 716  SER B C   1 
ATOM   11529 O  O   . SER B  1 716 ? 13.251  61.405 43.920  1.00 14.77 ? 716  SER B O   1 
ATOM   11530 C  CB  . SER B  1 716 ? 10.844  60.049 42.449  1.00 14.07 ? 716  SER B CB  1 
ATOM   11531 O  OG  . SER B  1 716 ? 9.468   59.898 42.726  1.00 14.73 ? 716  SER B OG  1 
ATOM   11532 N  N   . ALA B  1 717 ? 13.462  61.962 41.756  1.00 14.45 ? 717  ALA B N   1 
ATOM   11533 C  CA  . ALA B  1 717 ? 14.915  62.139 41.856  1.00 14.83 ? 717  ALA B CA  1 
ATOM   11534 C  C   . ALA B  1 717 ? 15.207  63.311 42.803  1.00 14.34 ? 717  ALA B C   1 
ATOM   11535 O  O   . ALA B  1 717 ? 16.193  63.280 43.534  1.00 14.84 ? 717  ALA B O   1 
ATOM   11536 C  CB  . ALA B  1 717 ? 15.540  62.420 40.474  1.00 14.11 ? 717  ALA B CB  1 
ATOM   11537 N  N   . GLN B  1 718 ? 14.355  64.336 42.803  1.00 13.76 ? 718  GLN B N   1 
ATOM   11538 C  CA  . GLN B  1 718 ? 14.574  65.477 43.697  1.00 14.26 ? 718  GLN B CA  1 
ATOM   11539 C  C   . GLN B  1 718 ? 14.141  65.130 45.126  1.00 14.23 ? 718  GLN B C   1 
ATOM   11540 O  O   . GLN B  1 718 ? 14.702  65.647 46.084  1.00 14.15 ? 718  GLN B O   1 
ATOM   11541 C  CB  . GLN B  1 718 ? 13.843  66.728 43.174  1.00 14.46 ? 718  GLN B CB  1 
ATOM   11542 C  CG  . GLN B  1 718 ? 14.416  67.235 41.852  1.00 15.32 ? 718  GLN B CG  1 
ATOM   11543 C  CD  . GLN B  1 718 ? 15.766  67.931 42.010  1.00 15.36 ? 718  GLN B CD  1 
ATOM   11544 O  OE1 . GLN B  1 718 ? 16.375  67.889 43.071  1.00 14.65 ? 718  GLN B OE1 1 
ATOM   11545 N  NE2 . GLN B  1 718 ? 16.232  68.575 40.946  1.00 15.03 ? 718  GLN B NE2 1 
ATOM   11546 N  N   . ILE B  1 719 ? 13.139  64.264 45.286  1.00 14.38 ? 719  ILE B N   1 
ATOM   11547 C  CA  . ILE B  1 719 ? 12.737  63.881 46.634  1.00 13.60 ? 719  ILE B CA  1 
ATOM   11548 C  C   . ILE B  1 719 ? 13.875  63.072 47.275  1.00 14.49 ? 719  ILE B C   1 
ATOM   11549 O  O   . ILE B  1 719 ? 14.295  63.355 48.408  1.00 13.21 ? 719  ILE B O   1 
ATOM   11550 C  CB  . ILE B  1 719 ? 11.480  62.977 46.661  1.00 14.03 ? 719  ILE B CB  1 
ATOM   11551 C  CG1 . ILE B  1 719 ? 10.205  63.756 46.277  1.00 13.08 ? 719  ILE B CG1 1 
ATOM   11552 C  CG2 . ILE B  1 719 ? 11.320  62.403 48.064  1.00 12.32 ? 719  ILE B CG2 1 
ATOM   11553 C  CD1 . ILE B  1 719 ? 8.981   62.838 46.119  1.00 12.34 ? 719  ILE B CD1 1 
ATOM   11554 N  N   . SER B  1 720 ? 14.379  62.071 46.557  1.00 13.94 ? 720  SER B N   1 
ATOM   11555 C  CA  . SER B  1 720 ? 15.437  61.231 47.113  1.00 14.76 ? 720  SER B CA  1 
ATOM   11556 C  C   . SER B  1 720 ? 16.700  62.026 47.452  1.00 16.07 ? 720  SER B C   1 
ATOM   11557 O  O   . SER B  1 720 ? 17.348  61.780 48.484  1.00 16.74 ? 720  SER B O   1 
ATOM   11558 C  CB  . SER B  1 720 ? 15.782  60.088 46.152  1.00 13.74 ? 720  SER B CB  1 
ATOM   11559 O  OG  . SER B  1 720 ? 16.396  60.557 44.976  1.00 13.97 ? 720  SER B OG  1 
ATOM   11560 N  N   . LYS B  1 721 ? 17.051  62.986 46.605  1.00 15.87 ? 721  LYS B N   1 
ATOM   11561 C  CA  . LYS B  1 721 ? 18.252  63.771 46.869  1.00 16.84 ? 721  LYS B CA  1 
ATOM   11562 C  C   . LYS B  1 721 ? 18.065  64.645 48.105  1.00 16.59 ? 721  LYS B C   1 
ATOM   11563 O  O   . LYS B  1 721 ? 19.011  64.839 48.875  1.00 16.80 ? 721  LYS B O   1 
ATOM   11564 C  CB  . LYS B  1 721 ? 18.623  64.640 45.654  1.00 16.29 ? 721  LYS B CB  1 
ATOM   11565 C  CG  . LYS B  1 721 ? 19.824  65.576 45.875  1.00 15.25 ? 721  LYS B CG  1 
ATOM   11566 C  CD  . LYS B  1 721 ? 20.511  65.993 44.558  1.00 16.16 ? 721  LYS B CD  1 
ATOM   11567 C  CE  . LYS B  1 721 ? 19.590  66.682 43.546  1.00 17.34 ? 721  LYS B CE  1 
ATOM   11568 N  NZ  . LYS B  1 721 ? 19.036  67.990 44.003  1.00 17.11 ? 721  LYS B NZ  1 
ATOM   11569 N  N   . ALA B  1 722 ? 16.858  65.175 48.288  1.00 16.32 ? 722  ALA B N   1 
ATOM   11570 C  CA  . ALA B  1 722 ? 16.582  66.019 49.444  1.00 16.92 ? 722  ALA B CA  1 
ATOM   11571 C  C   . ALA B  1 722 ? 16.680  65.179 50.716  1.00 18.06 ? 722  ALA B C   1 
ATOM   11572 O  O   . ALA B  1 722 ? 17.192  65.654 51.740  1.00 18.11 ? 722  ALA B O   1 
ATOM   11573 C  CB  . ALA B  1 722 ? 15.188  66.658 49.334  1.00 17.51 ? 722  ALA B CB  1 
ATOM   11574 N  N   . LEU B  1 723 ? 16.196  63.937 50.654  1.00 16.51 ? 723  LEU B N   1 
ATOM   11575 C  CA  . LEU B  1 723 ? 16.255  63.041 51.817  1.00 16.51 ? 723  LEU B CA  1 
ATOM   11576 C  C   . LEU B  1 723 ? 17.710  62.679 52.095  1.00 16.89 ? 723  LEU B C   1 
ATOM   11577 O  O   . LEU B  1 723 ? 18.158  62.692 53.236  1.00 16.24 ? 723  LEU B O   1 
ATOM   11578 C  CB  . LEU B  1 723 ? 15.442  61.768 51.565  1.00 16.32 ? 723  LEU B CB  1 
ATOM   11579 C  CG  . LEU B  1 723 ? 13.919  61.975 51.423  1.00 17.14 ? 723  LEU B CG  1 
ATOM   11580 C  CD1 . LEU B  1 723 ? 13.237  60.636 51.102  1.00 16.64 ? 723  LEU B CD1 1 
ATOM   11581 C  CD2 . LEU B  1 723 ? 13.379  62.554 52.709  1.00 17.80 ? 723  LEU B CD2 1 
ATOM   11582 N  N   . VAL B  1 724 ? 18.457  62.350 51.052  1.00 16.75 ? 724  VAL B N   1 
ATOM   11583 C  CA  . VAL B  1 724 ? 19.867  62.040 51.241  1.00 17.59 ? 724  VAL B CA  1 
ATOM   11584 C  C   . VAL B  1 724 ? 20.588  63.240 51.899  1.00 18.45 ? 724  VAL B C   1 
ATOM   11585 O  O   . VAL B  1 724 ? 21.393  63.061 52.816  1.00 18.00 ? 724  VAL B O   1 
ATOM   11586 C  CB  . VAL B  1 724 ? 20.552  61.733 49.901  1.00 16.61 ? 724  VAL B CB  1 
ATOM   11587 C  CG1 . VAL B  1 724 ? 22.089  61.681 50.096  1.00 16.65 ? 724  VAL B CG1 1 
ATOM   11588 C  CG2 . VAL B  1 724 ? 20.027  60.398 49.347  1.00 16.75 ? 724  VAL B CG2 1 
ATOM   11589 N  N   . ASP B  1 725 ? 20.277  64.453 51.437  1.00 18.87 ? 725  ASP B N   1 
ATOM   11590 C  CA  . ASP B  1 725 ? 20.911  65.664 51.946  1.00 20.29 ? 725  ASP B CA  1 
ATOM   11591 C  C   . ASP B  1 725 ? 20.685  65.960 53.428  1.00 20.70 ? 725  ASP B C   1 
ATOM   11592 O  O   . ASP B  1 725 ? 21.489  66.662 54.038  1.00 20.08 ? 725  ASP B O   1 
ATOM   11593 C  CB  . ASP B  1 725 ? 20.495  66.887 51.125  1.00 22.37 ? 725  ASP B CB  1 
ATOM   11594 C  CG  . ASP B  1 725 ? 21.146  66.922 49.746  1.00 24.01 ? 725  ASP B CG  1 
ATOM   11595 O  OD1 . ASP B  1 725 ? 22.012  66.071 49.443  1.00 26.52 ? 725  ASP B OD1 1 
ATOM   11596 O  OD2 . ASP B  1 725 ? 20.784  67.815 48.963  1.00 27.62 ? 725  ASP B OD2 1 
ATOM   11597 N  N   . VAL B  1 726 ? 19.600  65.463 54.011  1.00 19.99 ? 726  VAL B N   1 
ATOM   11598 C  CA  . VAL B  1 726 ? 19.374  65.698 55.435  1.00 20.83 ? 726  VAL B CA  1 
ATOM   11599 C  C   . VAL B  1 726 ? 19.603  64.406 56.224  1.00 20.82 ? 726  VAL B C   1 
ATOM   11600 O  O   . VAL B  1 726 ? 19.277  64.329 57.401  1.00 20.42 ? 726  VAL B O   1 
ATOM   11601 C  CB  . VAL B  1 726 ? 17.951  66.225 55.730  1.00 22.19 ? 726  VAL B CB  1 
ATOM   11602 C  CG1 . VAL B  1 726 ? 17.767  67.600 55.090  1.00 22.81 ? 726  VAL B CG1 1 
ATOM   11603 C  CG2 . VAL B  1 726 ? 16.905  65.250 55.208  1.00 21.67 ? 726  VAL B CG2 1 
ATOM   11604 N  N   . GLY B  1 727 ? 20.174  63.400 55.562  1.00 19.86 ? 727  GLY B N   1 
ATOM   11605 C  CA  . GLY B  1 727 ? 20.466  62.148 56.227  1.00 19.79 ? 727  GLY B CA  1 
ATOM   11606 C  C   . GLY B  1 727 ? 19.286  61.294 56.656  1.00 20.64 ? 727  GLY B C   1 
ATOM   11607 O  O   . GLY B  1 727 ? 19.290  60.697 57.735  1.00 19.55 ? 727  GLY B O   1 
ATOM   11608 N  N   . VAL B  1 728 ? 18.267  61.227 55.814  1.00 19.37 ? 728  VAL B N   1 
ATOM   11609 C  CA  . VAL B  1 728 ? 17.110  60.403 56.112  1.00 20.08 ? 728  VAL B CA  1 
ATOM   11610 C  C   . VAL B  1 728 ? 17.189  59.078 55.346  1.00 19.30 ? 728  VAL B C   1 
ATOM   11611 O  O   . VAL B  1 728 ? 17.390  59.063 54.133  1.00 18.80 ? 728  VAL B O   1 
ATOM   11612 C  CB  . VAL B  1 728 ? 15.800  61.130 55.699  1.00 21.14 ? 728  VAL B CB  1 
ATOM   11613 C  CG1 . VAL B  1 728 ? 14.609  60.209 55.864  1.00 20.69 ? 728  VAL B CG1 1 
ATOM   11614 C  CG2 . VAL B  1 728 ? 15.617  62.373 56.560  1.00 22.93 ? 728  VAL B CG2 1 
ATOM   11615 N  N   . ASP B  1 729 ? 17.050  57.966 56.052  1.00 18.91 ? 729  ASP B N   1 
ATOM   11616 C  CA  . ASP B  1 729 ? 17.051  56.675 55.387  1.00 18.90 ? 729  ASP B CA  1 
ATOM   11617 C  C   . ASP B  1 729 ? 15.629  56.358 54.914  1.00 18.63 ? 729  ASP B C   1 
ATOM   11618 O  O   . ASP B  1 729 ? 14.657  56.704 55.583  1.00 19.10 ? 729  ASP B O   1 
ATOM   11619 C  CB  . ASP B  1 729 ? 17.508  55.575 56.334  1.00 20.52 ? 729  ASP B CB  1 
ATOM   11620 C  CG  . ASP B  1 729 ? 17.736  54.283 55.609  1.00 20.46 ? 729  ASP B CG  1 
ATOM   11621 O  OD1 . ASP B  1 729 ? 18.397  54.340 54.540  1.00 21.39 ? 729  ASP B OD1 1 
ATOM   11622 O  OD2 . ASP B  1 729 ? 17.254  53.230 56.076  1.00 20.91 ? 729  ASP B OD2 1 
ATOM   11623 N  N   . PHE B  1 730 ? 15.507  55.704 53.764  1.00 17.93 ? 730  PHE B N   1 
ATOM   11624 C  CA  . PHE B  1 730 ? 14.193  55.336 53.210  1.00 17.12 ? 730  PHE B CA  1 
ATOM   11625 C  C   . PHE B  1 730 ? 14.361  54.178 52.233  1.00 17.24 ? 730  PHE B C   1 
ATOM   11626 O  O   . PHE B  1 730 ? 15.469  53.777 51.926  1.00 17.68 ? 730  PHE B O   1 
ATOM   11627 C  CB  . PHE B  1 730 ? 13.550  56.530 52.480  1.00 16.24 ? 730  PHE B CB  1 
ATOM   11628 C  CG  . PHE B  1 730 ? 14.357  57.028 51.307  1.00 16.09 ? 730  PHE B CG  1 
ATOM   11629 C  CD1 . PHE B  1 730 ? 15.499  57.790 51.505  1.00 16.65 ? 730  PHE B CD1 1 
ATOM   11630 C  CD2 . PHE B  1 730 ? 13.986  56.711 50.007  1.00 16.10 ? 730  PHE B CD2 1 
ATOM   11631 C  CE1 . PHE B  1 730 ? 16.263  58.234 50.413  1.00 16.75 ? 730  PHE B CE1 1 
ATOM   11632 C  CE2 . PHE B  1 730 ? 14.736  57.145 48.916  1.00 16.06 ? 730  PHE B CE2 1 
ATOM   11633 C  CZ  . PHE B  1 730 ? 15.874  57.906 49.118  1.00 15.85 ? 730  PHE B CZ  1 
ATOM   11634 N  N   . GLN B  1 731 ? 13.259  53.618 51.765  1.00 18.91 ? 731  GLN B N   1 
ATOM   11635 C  CA  . GLN B  1 731 ? 13.325  52.518 50.812  1.00 20.14 ? 731  GLN B CA  1 
ATOM   11636 C  C   . GLN B  1 731 ? 12.981  53.078 49.430  1.00 19.76 ? 731  GLN B C   1 
ATOM   11637 O  O   . GLN B  1 731 ? 12.169  53.992 49.304  1.00 19.04 ? 731  GLN B O   1 
ATOM   11638 C  CB  . GLN B  1 731 ? 12.306  51.432 51.165  1.00 21.86 ? 731  GLN B CB  1 
ATOM   11639 C  CG  . GLN B  1 731 ? 12.503  50.747 52.510  1.00 26.47 ? 731  GLN B CG  1 
ATOM   11640 C  CD  . GLN B  1 731 ? 13.503  49.624 52.422  1.00 29.67 ? 731  GLN B CD  1 
ATOM   11641 O  OE1 . GLN B  1 731 ? 14.710  49.851 52.460  1.00 30.64 ? 731  GLN B OE1 1 
ATOM   11642 N  NE2 . GLN B  1 731 ? 13.005  48.394 52.274  1.00 30.90 ? 731  GLN B NE2 1 
ATOM   11643 N  N   . ALA B  1 732 ? 13.575  52.519 48.388  1.00 17.81 ? 732  ALA B N   1 
ATOM   11644 C  CA  . ALA B  1 732 ? 13.279  53.019 47.066  1.00 17.59 ? 732  ALA B CA  1 
ATOM   11645 C  C   . ALA B  1 732 ? 13.222  51.916 46.046  1.00 16.63 ? 732  ALA B C   1 
ATOM   11646 O  O   . ALA B  1 732 ? 13.731  50.815 46.257  1.00 14.86 ? 732  ALA B O   1 
ATOM   11647 C  CB  . ALA B  1 732 ? 14.332  54.059 46.640  1.00 16.91 ? 732  ALA B CB  1 
ATOM   11648 N  N   . MET B  1 733 ? 12.557  52.214 44.944  1.00 16.26 ? 733  MET B N   1 
ATOM   11649 C  CA  . MET B  1 733 ? 12.489  51.273 43.839  1.00 15.10 ? 733  MET B CA  1 
ATOM   11650 C  C   . MET B  1 733 ? 12.211  52.034 42.543  1.00 15.50 ? 733  MET B C   1 
ATOM   11651 O  O   . MET B  1 733 ? 11.268  52.824 42.461  1.00 14.85 ? 733  MET B O   1 
ATOM   11652 C  CB  . MET B  1 733 ? 11.395  50.222 44.091  1.00 15.83 ? 733  MET B CB  1 
ATOM   11653 C  CG  . MET B  1 733 ? 11.217  49.190 42.961  1.00 16.54 ? 733  MET B CG  1 
ATOM   11654 S  SD  . MET B  1 733 ? 12.673  48.108 42.657  1.00 18.81 ? 733  MET B SD  1 
ATOM   11655 C  CE  . MET B  1 733 ? 12.790  47.245 44.204  1.00 17.30 ? 733  MET B CE  1 
ATOM   11656 N  N   . TRP B  1 734 ? 13.054  51.830 41.540  1.00 15.27 ? 734  TRP B N   1 
ATOM   11657 C  CA  . TRP B  1 734 ? 12.811  52.460 40.249  1.00 14.63 ? 734  TRP B CA  1 
ATOM   11658 C  C   . TRP B  1 734 ? 12.334  51.327 39.349  1.00 14.97 ? 734  TRP B C   1 
ATOM   11659 O  O   . TRP B  1 734 ? 12.711  50.174 39.565  1.00 14.39 ? 734  TRP B O   1 
ATOM   11660 C  CB  . TRP B  1 734 ? 14.094  53.078 39.660  1.00 12.40 ? 734  TRP B CB  1 
ATOM   11661 C  CG  . TRP B  1 734 ? 15.097  52.068 39.156  1.00 12.56 ? 734  TRP B CG  1 
ATOM   11662 C  CD1 . TRP B  1 734 ? 15.044  51.374 37.976  1.00 13.03 ? 734  TRP B CD1 1 
ATOM   11663 C  CD2 . TRP B  1 734 ? 16.303  51.638 39.815  1.00 11.49 ? 734  TRP B CD2 1 
ATOM   11664 N  NE1 . TRP B  1 734 ? 16.141  50.547 37.864  1.00 11.59 ? 734  TRP B NE1 1 
ATOM   11665 C  CE2 . TRP B  1 734 ? 16.927  50.688 38.976  1.00 11.20 ? 734  TRP B CE2 1 
ATOM   11666 C  CE3 . TRP B  1 734 ? 16.914  51.963 41.033  1.00 11.40 ? 734  TRP B CE3 1 
ATOM   11667 C  CZ2 . TRP B  1 734 ? 18.139  50.057 39.311  1.00 10.93 ? 734  TRP B CZ2 1 
ATOM   11668 C  CZ3 . TRP B  1 734 ? 18.127  51.330 41.374  1.00 12.80 ? 734  TRP B CZ3 1 
ATOM   11669 C  CH2 . TRP B  1 734 ? 18.722  50.389 40.514  1.00 11.41 ? 734  TRP B CH2 1 
ATOM   11670 N  N   . TYR B  1 735 ? 11.508  51.636 38.354  1.00 14.36 ? 735  TYR B N   1 
ATOM   11671 C  CA  . TYR B  1 735 ? 11.063  50.606 37.427  1.00 13.59 ? 735  TYR B CA  1 
ATOM   11672 C  C   . TYR B  1 735 ? 11.518  50.991 36.028  1.00 13.64 ? 735  TYR B C   1 
ATOM   11673 O  O   . TYR B  1 735 ? 10.947  51.863 35.384  1.00 12.99 ? 735  TYR B O   1 
ATOM   11674 C  CB  . TYR B  1 735 ? 9.545   50.428 37.493  1.00 13.64 ? 735  TYR B CB  1 
ATOM   11675 C  CG  . TYR B  1 735 ? 9.155   49.501 38.622  1.00 15.16 ? 735  TYR B CG  1 
ATOM   11676 C  CD1 . TYR B  1 735 ? 9.394   48.126 38.530  1.00 15.54 ? 735  TYR B CD1 1 
ATOM   11677 C  CD2 . TYR B  1 735 ? 8.666   50.005 39.829  1.00 13.18 ? 735  TYR B CD2 1 
ATOM   11678 C  CE1 . TYR B  1 735 ? 9.167   47.282 39.612  1.00 14.53 ? 735  TYR B CE1 1 
ATOM   11679 C  CE2 . TYR B  1 735 ? 8.437   49.177 40.905  1.00 13.25 ? 735  TYR B CE2 1 
ATOM   11680 C  CZ  . TYR B  1 735 ? 8.691   47.823 40.797  1.00 14.87 ? 735  TYR B CZ  1 
ATOM   11681 O  OH  . TYR B  1 735 ? 8.499   47.010 41.886  1.00 15.84 ? 735  TYR B OH  1 
ATOM   11682 N  N   . THR B  1 736 ? 12.561  50.316 35.572  1.00 14.00 ? 736  THR B N   1 
ATOM   11683 C  CA  . THR B  1 736 ? 13.139  50.568 34.269  1.00 13.78 ? 736  THR B CA  1 
ATOM   11684 C  C   . THR B  1 736 ? 12.140  50.548 33.139  1.00 15.24 ? 736  THR B C   1 
ATOM   11685 O  O   . THR B  1 736 ? 11.431  49.560 32.940  1.00 15.15 ? 736  THR B O   1 
ATOM   11686 C  CB  . THR B  1 736 ? 14.241  49.538 33.967  1.00 14.39 ? 736  THR B CB  1 
ATOM   11687 O  OG1 . THR B  1 736 ? 15.264  49.674 34.962  1.00 12.47 ? 736  THR B OG1 1 
ATOM   11688 C  CG2 . THR B  1 736 ? 14.832  49.749 32.539  1.00 13.54 ? 736  THR B CG2 1 
ATOM   11689 N  N   . ASP B  1 737 ? 12.100  51.654 32.402  1.00 15.38 ? 737  ASP B N   1 
ATOM   11690 C  CA  . ASP B  1 737 ? 11.244  51.824 31.242  1.00 15.23 ? 737  ASP B CA  1 
ATOM   11691 C  C   . ASP B  1 737 ? 9.737   51.754 31.475  1.00 16.15 ? 737  ASP B C   1 
ATOM   11692 O  O   . ASP B  1 737 ? 8.973   51.574 30.516  1.00 15.87 ? 737  ASP B O   1 
ATOM   11693 C  CB  . ASP B  1 737 ? 11.635  50.831 30.141  1.00 16.39 ? 737  ASP B CB  1 
ATOM   11694 C  CG  . ASP B  1 737 ? 12.996  51.126 29.536  1.00 16.81 ? 737  ASP B CG  1 
ATOM   11695 O  OD1 . ASP B  1 737 ? 13.560  52.203 29.817  1.00 15.82 ? 737  ASP B OD1 1 
ATOM   11696 O  OD2 . ASP B  1 737 ? 13.505  50.280 28.752  1.00 17.95 ? 737  ASP B OD2 1 
ATOM   11697 N  N   . GLU B  1 738 ? 9.297   51.915 32.721  1.00 15.06 ? 738  GLU B N   1 
ATOM   11698 C  CA  . GLU B  1 738 ? 7.862   51.909 33.006  1.00 15.34 ? 738  GLU B CA  1 
ATOM   11699 C  C   . GLU B  1 738 ? 7.403   53.371 33.042  1.00 16.90 ? 738  GLU B C   1 
ATOM   11700 O  O   . GLU B  1 738 ? 8.191   54.271 33.373  1.00 16.10 ? 738  GLU B O   1 
ATOM   11701 C  CB  . GLU B  1 738 ? 7.565   51.222 34.355  1.00 14.97 ? 738  GLU B CB  1 
ATOM   11702 C  CG  . GLU B  1 738 ? 7.662   49.692 34.323  1.00 16.77 ? 738  GLU B CG  1 
ATOM   11703 C  CD  . GLU B  1 738 ? 6.660   49.079 33.339  1.00 19.85 ? 738  GLU B CD  1 
ATOM   11704 O  OE1 . GLU B  1 738 ? 5.463   49.405 33.461  1.00 19.84 ? 738  GLU B OE1 1 
ATOM   11705 O  OE2 . GLU B  1 738 ? 7.062   48.292 32.447  1.00 22.45 ? 738  GLU B OE2 1 
ATOM   11706 N  N   . ASP B  1 739 ? 6.151   53.622 32.674  1.00 15.98 ? 739  ASP B N   1 
ATOM   11707 C  CA  . ASP B  1 739 ? 5.668   54.990 32.713  1.00 16.79 ? 739  ASP B CA  1 
ATOM   11708 C  C   . ASP B  1 739 ? 4.777   55.245 33.940  1.00 16.10 ? 739  ASP B C   1 
ATOM   11709 O  O   . ASP B  1 739 ? 4.872   54.519 34.944  1.00 16.16 ? 739  ASP B O   1 
ATOM   11710 C  CB  . ASP B  1 739 ? 4.956   55.353 31.407  1.00 15.49 ? 739  ASP B CB  1 
ATOM   11711 C  CG  . ASP B  1 739 ? 3.676   54.554 31.180  1.00 17.97 ? 739  ASP B CG  1 
ATOM   11712 O  OD1 . ASP B  1 739 ? 3.109   53.988 32.149  1.00 14.79 ? 739  ASP B OD1 1 
ATOM   11713 O  OD2 . ASP B  1 739 ? 3.240   54.525 30.011  1.00 16.88 ? 739  ASP B OD2 1 
ATOM   11714 N  N   . HIS B  1 740 ? 3.923   56.265 33.873  1.00 15.55 ? 740  HIS B N   1 
ATOM   11715 C  CA  . HIS B  1 740 ? 3.084   56.614 35.008  1.00 16.62 ? 740  HIS B CA  1 
ATOM   11716 C  C   . HIS B  1 740 ? 2.110   55.507 35.446  1.00 18.04 ? 740  HIS B C   1 
ATOM   11717 O  O   . HIS B  1 740 ? 1.623   55.533 36.575  1.00 17.82 ? 740  HIS B O   1 
ATOM   11718 C  CB  . HIS B  1 740 ? 2.307   57.911 34.717  1.00 15.79 ? 740  HIS B CB  1 
ATOM   11719 C  CG  . HIS B  1 740 ? 1.816   58.616 35.950  1.00 15.89 ? 740  HIS B CG  1 
ATOM   11720 N  ND1 . HIS B  1 740 ? 2.657   59.015 36.967  1.00 15.46 ? 740  HIS B ND1 1 
ATOM   11721 C  CD2 . HIS B  1 740 ? 0.577   59.044 36.301  1.00 15.79 ? 740  HIS B CD2 1 
ATOM   11722 C  CE1 . HIS B  1 740 ? 1.962   59.662 37.888  1.00 15.60 ? 740  HIS B CE1 1 
ATOM   11723 N  NE2 . HIS B  1 740 ? 0.697   59.694 37.507  1.00 15.78 ? 740  HIS B NE2 1 
ATOM   11724 N  N   . GLY B  1 741 ? 1.820   54.546 34.566  1.00 17.69 ? 741  GLY B N   1 
ATOM   11725 C  CA  . GLY B  1 741 ? 0.908   53.480 34.939  1.00 17.89 ? 741  GLY B CA  1 
ATOM   11726 C  C   . GLY B  1 741 ? 1.602   52.257 35.536  1.00 18.59 ? 741  GLY B C   1 
ATOM   11727 O  O   . GLY B  1 741 ? 0.943   51.458 36.203  1.00 18.68 ? 741  GLY B O   1 
ATOM   11728 N  N   . ILE B  1 742 ? 2.917   52.125 35.323  1.00 17.44 ? 742  ILE B N   1 
ATOM   11729 C  CA  . ILE B  1 742 ? 3.692   50.981 35.807  1.00 17.03 ? 742  ILE B CA  1 
ATOM   11730 C  C   . ILE B  1 742 ? 2.733   49.805 35.642  1.00 18.18 ? 742  ILE B C   1 
ATOM   11731 O  O   . ILE B  1 742 ? 2.439   49.064 36.595  1.00 17.52 ? 742  ILE B O   1 
ATOM   11732 C  CB  . ILE B  1 742 ? 4.080   51.133 37.283  1.00 15.16 ? 742  ILE B CB  1 
ATOM   11733 C  CG1 . ILE B  1 742 ? 4.724   52.493 37.518  1.00 15.48 ? 742  ILE B CG1 1 
ATOM   11734 C  CG2 . ILE B  1 742 ? 5.064   50.020 37.659  1.00 14.23 ? 742  ILE B CG2 1 
ATOM   11735 C  CD1 . ILE B  1 742 ? 5.320   52.686 38.912  1.00 16.29 ? 742  ILE B CD1 1 
ATOM   11736 N  N   . ALA B  1 743 ? 2.243   49.674 34.410  1.00 18.49 ? 743  ALA B N   1 
ATOM   11737 C  CA  . ALA B  1 743 ? 1.238   48.687 34.079  1.00 19.59 ? 743  ALA B CA  1 
ATOM   11738 C  C   . ALA B  1 743 ? 1.657   47.496 33.269  1.00 20.21 ? 743  ALA B C   1 
ATOM   11739 O  O   . ALA B  1 743 ? 0.807   46.677 32.939  1.00 19.52 ? 743  ALA B O   1 
ATOM   11740 C  CB  . ALA B  1 743 ? 0.050   49.376 33.384  1.00 21.02 ? 743  ALA B CB  1 
ATOM   11741 N  N   . SER B  1 744 ? 2.934   47.373 32.913  1.00 20.76 ? 744  SER B N   1 
ATOM   11742 C  CA  . SER B  1 744 ? 3.317   46.177 32.165  1.00 22.00 ? 744  SER B CA  1 
ATOM   11743 C  C   . SER B  1 744 ? 3.025   45.008 33.126  1.00 21.88 ? 744  SER B C   1 
ATOM   11744 O  O   . SER B  1 744 ? 3.090   45.148 34.351  1.00 22.44 ? 744  SER B O   1 
ATOM   11745 C  CB  . SER B  1 744 ? 4.809   46.195 31.792  1.00 22.00 ? 744  SER B CB  1 
ATOM   11746 O  OG  . SER B  1 744 ? 5.610   45.814 32.905  1.00 25.49 ? 744  SER B OG  1 
ATOM   11747 N  N   . SER B  1 745 ? 2.697   43.866 32.556  1.00 22.50 ? 745  SER B N   1 
ATOM   11748 C  CA  . SER B  1 745 ? 2.374   42.674 33.325  1.00 23.44 ? 745  SER B CA  1 
ATOM   11749 C  C   . SER B  1 745 ? 3.393   42.350 34.432  1.00 22.49 ? 745  SER B C   1 
ATOM   11750 O  O   . SER B  1 745 ? 3.037   42.204 35.602  1.00 21.47 ? 745  SER B O   1 
ATOM   11751 C  CB  . SER B  1 745 ? 2.259   41.499 32.360  1.00 24.22 ? 745  SER B CB  1 
ATOM   11752 O  OG  . SER B  1 745 ? 2.013   40.312 33.057  1.00 28.68 ? 745  SER B OG  1 
ATOM   11753 N  N   . THR B  1 746 ? 4.660   42.240 34.059  1.00 22.01 ? 746  THR B N   1 
ATOM   11754 C  CA  . THR B  1 746 ? 5.700   41.920 35.031  1.00 21.97 ? 746  THR B CA  1 
ATOM   11755 C  C   . THR B  1 746 ? 5.920   43.003 36.083  1.00 20.98 ? 746  THR B C   1 
ATOM   11756 O  O   . THR B  1 746 ? 6.015   42.702 37.267  1.00 21.10 ? 746  THR B O   1 
ATOM   11757 C  CB  . THR B  1 746 ? 7.030   41.593 34.316  1.00 22.14 ? 746  THR B CB  1 
ATOM   11758 O  OG1 . THR B  1 746 ? 7.399   42.667 33.443  1.00 23.59 ? 746  THR B OG1 1 
ATOM   11759 C  CG2 . THR B  1 746 ? 6.872   40.317 33.494  1.00 22.54 ? 746  THR B CG2 1 
ATOM   11760 N  N   . ALA B  1 747 ? 5.969   44.265 35.664  1.00 20.65 ? 747  ALA B N   1 
ATOM   11761 C  CA  . ALA B  1 747 ? 6.190   45.349 36.615  1.00 19.57 ? 747  ALA B CA  1 
ATOM   11762 C  C   . ALA B  1 747 ? 5.013   45.493 37.575  1.00 18.99 ? 747  ALA B C   1 
ATOM   11763 O  O   . ALA B  1 747 ? 5.205   45.743 38.761  1.00 18.69 ? 747  ALA B O   1 
ATOM   11764 C  CB  . ALA B  1 747 ? 6.432   46.657 35.890  1.00 18.07 ? 747  ALA B CB  1 
ATOM   11765 N  N   . HIS B  1 748 ? 3.797   45.338 37.060  1.00 17.65 ? 748  HIS B N   1 
ATOM   11766 C  CA  . HIS B  1 748 ? 2.597   45.438 37.891  1.00 16.75 ? 748  HIS B CA  1 
ATOM   11767 C  C   . HIS B  1 748 ? 2.674   44.432 39.034  1.00 17.54 ? 748  HIS B C   1 
ATOM   11768 O  O   . HIS B  1 748 ? 2.432   44.756 40.184  1.00 17.37 ? 748  HIS B O   1 
ATOM   11769 C  CB  . HIS B  1 748 ? 1.351   45.130 37.066  1.00 17.24 ? 748  HIS B CB  1 
ATOM   11770 C  CG  . HIS B  1 748 ? 0.108   44.940 37.886  1.00 17.54 ? 748  HIS B CG  1 
ATOM   11771 N  ND1 . HIS B  1 748 ? -0.553  45.983 38.497  1.00 18.34 ? 748  HIS B ND1 1 
ATOM   11772 C  CD2 . HIS B  1 748 ? -0.618  43.828 38.155  1.00 18.26 ? 748  HIS B CD2 1 
ATOM   11773 C  CE1 . HIS B  1 748 ? -1.636  45.527 39.102  1.00 19.41 ? 748  HIS B CE1 1 
ATOM   11774 N  NE2 . HIS B  1 748 ? -1.699  44.221 38.910  1.00 19.24 ? 748  HIS B NE2 1 
ATOM   11775 N  N   . GLN B  1 749 ? 3.018   43.198 38.712  1.00 17.51 ? 749  GLN B N   1 
ATOM   11776 C  CA  . GLN B  1 749 ? 3.103   42.176 39.742  1.00 18.75 ? 749  GLN B CA  1 
ATOM   11777 C  C   . GLN B  1 749 ? 4.250   42.470 40.687  1.00 17.60 ? 749  GLN B C   1 
ATOM   11778 O  O   . GLN B  1 749 ? 4.137   42.255 41.887  1.00 16.97 ? 749  GLN B O   1 
ATOM   11779 C  CB  . GLN B  1 749 ? 3.292   40.807 39.084  1.00 18.82 ? 749  GLN B CB  1 
ATOM   11780 C  CG  . GLN B  1 749 ? 2.152   40.490 38.122  1.00 20.90 ? 749  GLN B CG  1 
ATOM   11781 C  CD  . GLN B  1 749 ? 2.275   39.121 37.500  1.00 23.61 ? 749  GLN B CD  1 
ATOM   11782 O  OE1 . GLN B  1 749 ? 2.202   38.103 38.192  1.00 26.20 ? 749  GLN B OE1 1 
ATOM   11783 N  NE2 . GLN B  1 749 ? 2.458   39.083 36.186  1.00 24.06 ? 749  GLN B NE2 1 
ATOM   11784 N  N   . HIS B  1 750 ? 5.349   42.985 40.143  1.00 17.18 ? 750  HIS B N   1 
ATOM   11785 C  CA  . HIS B  1 750 ? 6.519   43.258 40.958  1.00 16.04 ? 750  HIS B CA  1 
ATOM   11786 C  C   . HIS B  1 750 ? 6.303   44.410 41.940  1.00 15.78 ? 750  HIS B C   1 
ATOM   11787 O  O   . HIS B  1 750 ? 6.683   44.301 43.100  1.00 16.07 ? 750  HIS B O   1 
ATOM   11788 C  CB  . HIS B  1 750 ? 7.734   43.534 40.067  1.00 15.79 ? 750  HIS B CB  1 
ATOM   11789 C  CG  . HIS B  1 750 ? 9.043   43.448 40.790  1.00 16.92 ? 750  HIS B CG  1 
ATOM   11790 N  ND1 . HIS B  1 750 ? 9.559   44.492 41.528  1.00 17.01 ? 750  HIS B ND1 1 
ATOM   11791 C  CD2 . HIS B  1 750 ? 9.948   42.443 40.880  1.00 17.16 ? 750  HIS B CD2 1 
ATOM   11792 C  CE1 . HIS B  1 750 ? 10.727  44.135 42.037  1.00 16.80 ? 750  HIS B CE1 1 
ATOM   11793 N  NE2 . HIS B  1 750 ? 10.985  42.896 41.659  1.00 16.93 ? 750  HIS B NE2 1 
ATOM   11794 N  N   . ILE B  1 751 ? 5.662   45.495 41.515  1.00 15.35 ? 751  ILE B N   1 
ATOM   11795 C  CA  . ILE B  1 751 ? 5.475   46.597 42.441  1.00 14.99 ? 751  ILE B CA  1 
ATOM   11796 C  C   . ILE B  1 751 ? 4.494   46.238 43.561  1.00 15.84 ? 751  ILE B C   1 
ATOM   11797 O  O   . ILE B  1 751 ? 4.734   46.548 44.727  1.00 15.76 ? 751  ILE B O   1 
ATOM   11798 C  CB  . ILE B  1 751 ? 5.040   47.908 41.718  1.00 14.09 ? 751  ILE B CB  1 
ATOM   11799 C  CG1 . ILE B  1 751 ? 4.973   49.064 42.731  1.00 12.54 ? 751  ILE B CG1 1 
ATOM   11800 C  CG2 . ILE B  1 751 ? 3.699   47.713 41.020  1.00 13.58 ? 751  ILE B CG2 1 
ATOM   11801 C  CD1 . ILE B  1 751 ? 4.585   50.428 42.114  1.00 11.36 ? 751  ILE B CD1 1 
ATOM   11802 N  N   . TYR B  1 752 ? 3.404   45.556 43.243  1.00 16.06 ? 752  TYR B N   1 
ATOM   11803 C  CA  . TYR B  1 752 ? 2.469   45.204 44.311  1.00 16.17 ? 752  TYR B CA  1 
ATOM   11804 C  C   . TYR B  1 752 ? 3.065   44.165 45.254  1.00 16.09 ? 752  TYR B C   1 
ATOM   11805 O  O   . TYR B  1 752 ? 2.760   44.150 46.440  1.00 17.55 ? 752  TYR B O   1 
ATOM   11806 C  CB  . TYR B  1 752 ? 1.151   44.732 43.713  1.00 16.20 ? 752  TYR B CB  1 
ATOM   11807 C  CG  . TYR B  1 752 ? 0.261   45.910 43.387  1.00 16.73 ? 752  TYR B CG  1 
ATOM   11808 C  CD1 . TYR B  1 752 ? -0.400  46.612 44.402  1.00 16.40 ? 752  TYR B CD1 1 
ATOM   11809 C  CD2 . TYR B  1 752 ? 0.142   46.374 42.075  1.00 18.09 ? 752  TYR B CD2 1 
ATOM   11810 C  CE1 . TYR B  1 752 ? -1.165  47.761 44.112  1.00 17.56 ? 752  TYR B CE1 1 
ATOM   11811 C  CE2 . TYR B  1 752 ? -0.617  47.519 41.775  1.00 17.25 ? 752  TYR B CE2 1 
ATOM   11812 C  CZ  . TYR B  1 752 ? -1.263  48.201 42.796  1.00 17.43 ? 752  TYR B CZ  1 
ATOM   11813 O  OH  . TYR B  1 752 ? -2.001  49.313 42.475  1.00 17.79 ? 752  TYR B OH  1 
ATOM   11814 N  N   . THR B  1 753 ? 3.931   43.309 44.734  1.00 16.81 ? 753  THR B N   1 
ATOM   11815 C  CA  . THR B  1 753 ? 4.574   42.324 45.582  1.00 17.08 ? 753  THR B CA  1 
ATOM   11816 C  C   . THR B  1 753 ? 5.519   43.096 46.503  1.00 17.52 ? 753  THR B C   1 
ATOM   11817 O  O   . THR B  1 753 ? 5.525   42.884 47.723  1.00 19.21 ? 753  THR B O   1 
ATOM   11818 C  CB  . THR B  1 753 ? 5.357   41.309 44.735  1.00 17.37 ? 753  THR B CB  1 
ATOM   11819 O  OG1 . THR B  1 753 ? 4.429   40.485 44.022  1.00 18.30 ? 753  THR B OG1 1 
ATOM   11820 C  CG2 . THR B  1 753 ? 6.252   40.430 45.603  1.00 16.62 ? 753  THR B CG2 1 
ATOM   11821 N  N   . HIS B  1 754 ? 6.287   44.027 45.931  1.00 16.65 ? 754  HIS B N   1 
ATOM   11822 C  CA  . HIS B  1 754 ? 7.227   44.813 46.731  1.00 15.78 ? 754  HIS B CA  1 
ATOM   11823 C  C   . HIS B  1 754 ? 6.510   45.623 47.807  1.00 16.45 ? 754  HIS B C   1 
ATOM   11824 O  O   . HIS B  1 754 ? 6.951   45.663 48.949  1.00 16.15 ? 754  HIS B O   1 
ATOM   11825 C  CB  . HIS B  1 754 ? 8.045   45.773 45.862  1.00 15.45 ? 754  HIS B CB  1 
ATOM   11826 C  CG  . HIS B  1 754 ? 9.305   46.247 46.522  1.00 16.61 ? 754  HIS B CG  1 
ATOM   11827 N  ND1 . HIS B  1 754 ? 10.380  45.413 46.763  1.00 17.29 ? 754  HIS B ND1 1 
ATOM   11828 C  CD2 . HIS B  1 754 ? 9.664   47.465 46.991  1.00 15.92 ? 754  HIS B CD2 1 
ATOM   11829 C  CE1 . HIS B  1 754 ? 11.343  46.099 47.348  1.00 18.64 ? 754  HIS B CE1 1 
ATOM   11830 N  NE2 . HIS B  1 754 ? 10.934  47.348 47.495  1.00 16.99 ? 754  HIS B NE2 1 
ATOM   11831 N  N   . MET B  1 755 ? 5.408   46.279 47.444  1.00 16.47 ? 755  MET B N   1 
ATOM   11832 C  CA  . MET B  1 755 ? 4.664   47.084 48.405  1.00 17.05 ? 755  MET B CA  1 
ATOM   11833 C  C   . MET B  1 755 ? 4.036   46.212 49.488  1.00 17.71 ? 755  MET B C   1 
ATOM   11834 O  O   . MET B  1 755 ? 3.940   46.634 50.644  1.00 18.76 ? 755  MET B O   1 
ATOM   11835 C  CB  . MET B  1 755 ? 3.578   47.918 47.699  1.00 17.63 ? 755  MET B CB  1 
ATOM   11836 C  CG  . MET B  1 755 ? 4.135   48.963 46.712  1.00 18.17 ? 755  MET B CG  1 
ATOM   11837 S  SD  . MET B  1 755 ? 2.943   50.232 46.234  1.00 21.24 ? 755  MET B SD  1 
ATOM   11838 C  CE  . MET B  1 755 ? 1.775   49.187 45.338  1.00 17.19 ? 755  MET B CE  1 
ATOM   11839 N  N   . SER B  1 756 ? 3.610   45.002 49.121  1.00 17.32 ? 756  SER B N   1 
ATOM   11840 C  CA  . SER B  1 756 ? 3.006   44.092 50.098  1.00 19.16 ? 756  SER B CA  1 
ATOM   11841 C  C   . SER B  1 756 ? 4.008   43.763 51.210  1.00 18.95 ? 756  SER B C   1 
ATOM   11842 O  O   . SER B  1 756 ? 3.649   43.801 52.379  1.00 19.38 ? 756  SER B O   1 
ATOM   11843 C  CB  . SER B  1 756 ? 2.529   42.802 49.424  1.00 19.15 ? 756  SER B CB  1 
ATOM   11844 O  OG  . SER B  1 756 ? 1.465   43.060 48.518  1.00 20.86 ? 756  SER B OG  1 
ATOM   11845 N  N   . HIS B  1 757 ? 5.255   43.439 50.855  1.00 20.44 ? 757  HIS B N   1 
ATOM   11846 C  CA  . HIS B  1 757 ? 6.268   43.161 51.878  1.00 20.88 ? 757  HIS B CA  1 
ATOM   11847 C  C   . HIS B  1 757 ? 6.498   44.378 52.765  1.00 21.17 ? 757  HIS B C   1 
ATOM   11848 O  O   . HIS B  1 757 ? 6.653   44.250 53.981  1.00 21.86 ? 757  HIS B O   1 
ATOM   11849 C  CB  . HIS B  1 757 ? 7.619   42.790 51.264  1.00 21.82 ? 757  HIS B CB  1 
ATOM   11850 C  CG  . HIS B  1 757 ? 7.611   41.497 50.516  1.00 23.37 ? 757  HIS B CG  1 
ATOM   11851 N  ND1 . HIS B  1 757 ? 7.101   40.332 51.050  1.00 24.28 ? 757  HIS B ND1 1 
ATOM   11852 C  CD2 . HIS B  1 757 ? 8.053   41.182 49.274  1.00 22.90 ? 757  HIS B CD2 1 
ATOM   11853 C  CE1 . HIS B  1 757 ? 7.225   39.354 50.166  1.00 24.55 ? 757  HIS B CE1 1 
ATOM   11854 N  NE2 . HIS B  1 757 ? 7.799   39.845 49.079  1.00 24.11 ? 757  HIS B NE2 1 
ATOM   11855 N  N   . PHE B  1 758 ? 6.540   45.563 52.160  1.00 20.16 ? 758  PHE B N   1 
ATOM   11856 C  CA  . PHE B  1 758 ? 6.782   46.760 52.944  1.00 20.97 ? 758  PHE B CA  1 
ATOM   11857 C  C   . PHE B  1 758 ? 5.675   46.982 53.968  1.00 21.44 ? 758  PHE B C   1 
ATOM   11858 O  O   . PHE B  1 758 ? 5.952   47.296 55.126  1.00 22.43 ? 758  PHE B O   1 
ATOM   11859 C  CB  . PHE B  1 758 ? 6.890   47.995 52.047  1.00 20.64 ? 758  PHE B CB  1 
ATOM   11860 C  CG  . PHE B  1 758 ? 7.254   49.248 52.790  1.00 20.01 ? 758  PHE B CG  1 
ATOM   11861 C  CD1 . PHE B  1 758 ? 8.579   49.509 53.142  1.00 19.16 ? 758  PHE B CD1 1 
ATOM   11862 C  CD2 . PHE B  1 758 ? 6.279   50.174 53.131  1.00 18.94 ? 758  PHE B CD2 1 
ATOM   11863 C  CE1 . PHE B  1 758 ? 8.923   50.679 53.816  1.00 17.71 ? 758  PHE B CE1 1 
ATOM   11864 C  CE2 . PHE B  1 758 ? 6.619   51.343 53.806  1.00 19.11 ? 758  PHE B CE2 1 
ATOM   11865 C  CZ  . PHE B  1 758 ? 7.942   51.591 54.145  1.00 18.80 ? 758  PHE B CZ  1 
ATOM   11866 N  N   . ILE B  1 759 ? 4.423   46.836 53.548  1.00 21.10 ? 759  ILE B N   1 
ATOM   11867 C  CA  . ILE B  1 759 ? 3.306   47.043 54.469  1.00 21.68 ? 759  ILE B CA  1 
ATOM   11868 C  C   . ILE B  1 759 ? 3.282   45.987 55.580  1.00 22.27 ? 759  ILE B C   1 
ATOM   11869 O  O   . ILE B  1 759 ? 3.172   46.323 56.758  1.00 21.81 ? 759  ILE B O   1 
ATOM   11870 C  CB  . ILE B  1 759 ? 1.945   47.013 53.732  1.00 21.54 ? 759  ILE B CB  1 
ATOM   11871 C  CG1 . ILE B  1 759 ? 1.841   48.213 52.782  1.00 23.10 ? 759  ILE B CG1 1 
ATOM   11872 C  CG2 . ILE B  1 759 ? 0.806   47.079 54.735  1.00 22.05 ? 759  ILE B CG2 1 
ATOM   11873 C  CD1 . ILE B  1 759 ? 1.994   49.554 53.474  1.00 22.71 ? 759  ILE B CD1 1 
ATOM   11874 N  N   . LYS B  1 760 ? 3.368   44.716 55.204  1.00 23.19 ? 760  LYS B N   1 
ATOM   11875 C  CA  . LYS B  1 760 ? 3.353   43.648 56.199  1.00 24.54 ? 760  LYS B CA  1 
ATOM   11876 C  C   . LYS B  1 760 ? 4.490   43.843 57.189  1.00 24.92 ? 760  LYS B C   1 
ATOM   11877 O  O   . LYS B  1 760 ? 4.320   43.648 58.383  1.00 24.46 ? 760  LYS B O   1 
ATOM   11878 C  CB  . LYS B  1 760 ? 3.481   42.292 55.519  1.00 24.56 ? 760  LYS B CB  1 
ATOM   11879 C  CG  . LYS B  1 760 ? 2.286   41.982 54.634  1.00 27.74 ? 760  LYS B CG  1 
ATOM   11880 C  CD  . LYS B  1 760 ? 2.434   40.650 53.921  1.00 29.52 ? 760  LYS B CD  1 
ATOM   11881 C  CE  . LYS B  1 760 ? 2.413   39.512 54.910  1.00 30.08 ? 760  LYS B CE  1 
ATOM   11882 N  NZ  . LYS B  1 760 ? 2.539   38.213 54.196  1.00 33.35 ? 760  LYS B NZ  1 
ATOM   11883 N  N   . GLN B  1 761 ? 5.649   44.241 56.686  1.00 25.87 ? 761  GLN B N   1 
ATOM   11884 C  CA  . GLN B  1 761 ? 6.813   44.476 57.538  1.00 27.51 ? 761  GLN B CA  1 
ATOM   11885 C  C   . GLN B  1 761 ? 6.523   45.625 58.512  1.00 27.06 ? 761  GLN B C   1 
ATOM   11886 O  O   . GLN B  1 761 ? 6.791   45.532 59.713  1.00 25.47 ? 761  GLN B O   1 
ATOM   11887 C  CB  . GLN B  1 761 ? 8.026   44.785 56.652  1.00 30.16 ? 761  GLN B CB  1 
ATOM   11888 C  CG  . GLN B  1 761 ? 9.228   45.295 57.391  1.00 34.69 ? 761  GLN B CG  1 
ATOM   11889 C  CD  . GLN B  1 761 ? 9.178   46.796 57.602  1.00 36.63 ? 761  GLN B CD  1 
ATOM   11890 O  OE1 . GLN B  1 761 ? 9.674   47.298 58.610  1.00 37.86 ? 761  GLN B OE1 1 
ATOM   11891 N  NE2 . GLN B  1 761 ? 8.591   47.524 56.642  1.00 37.93 ? 761  GLN B NE2 1 
ATOM   11892 N  N   . CYS B  1 762 ? 5.944   46.700 57.988  1.00 26.47 ? 762  CYS B N   1 
ATOM   11893 C  CA  . CYS B  1 762 ? 5.605   47.859 58.806  1.00 27.23 ? 762  CYS B CA  1 
ATOM   11894 C  C   . CYS B  1 762 ? 4.577   47.530 59.895  1.00 26.87 ? 762  CYS B C   1 
ATOM   11895 O  O   . CYS B  1 762 ? 4.617   48.096 60.992  1.00 26.20 ? 762  CYS B O   1 
ATOM   11896 C  CB  . CYS B  1 762 ? 5.057   48.983 57.919  1.00 27.71 ? 762  CYS B CB  1 
ATOM   11897 S  SG  . CYS B  1 762 ? 4.391   50.414 58.822  1.00 28.93 ? 762  CYS B SG  1 
ATOM   11898 N  N   . PHE B  1 763 ? 3.658   46.624 59.582  1.00 26.82 ? 763  PHE B N   1 
ATOM   11899 C  CA  . PHE B  1 763 ? 2.625   46.249 60.527  1.00 28.43 ? 763  PHE B CA  1 
ATOM   11900 C  C   . PHE B  1 763 ? 3.001   44.975 61.262  1.00 30.34 ? 763  PHE B C   1 
ATOM   11901 O  O   . PHE B  1 763 ? 2.138   44.333 61.859  1.00 31.17 ? 763  PHE B O   1 
ATOM   11902 C  CB  . PHE B  1 763 ? 1.275   46.026 59.821  1.00 26.60 ? 763  PHE B CB  1 
ATOM   11903 C  CG  . PHE B  1 763 ? 0.631   47.282 59.286  1.00 24.13 ? 763  PHE B CG  1 
ATOM   11904 C  CD1 . PHE B  1 763 ? 0.953   48.526 59.807  1.00 23.88 ? 763  PHE B CD1 1 
ATOM   11905 C  CD2 . PHE B  1 763 ? -0.340  47.205 58.280  1.00 23.30 ? 763  PHE B CD2 1 
ATOM   11906 C  CE1 . PHE B  1 763 ? 0.318   49.682 59.340  1.00 23.49 ? 763  PHE B CE1 1 
ATOM   11907 C  CE2 . PHE B  1 763 ? -0.975  48.353 57.813  1.00 22.07 ? 763  PHE B CE2 1 
ATOM   11908 C  CZ  . PHE B  1 763 ? -0.643  49.586 58.344  1.00 22.30 ? 763  PHE B CZ  1 
ATOM   11909 N  N   . SER B  1 764 ? 4.272   44.596 61.195  1.00 31.94 ? 764  SER B N   1 
ATOM   11910 C  CA  . SER B  1 764 ? 4.743   43.394 61.874  1.00 35.04 ? 764  SER B CA  1 
ATOM   11911 C  C   . SER B  1 764 ? 3.842   42.207 61.559  1.00 37.07 ? 764  SER B C   1 
ATOM   11912 O  O   . SER B  1 764 ? 3.413   41.498 62.471  1.00 38.52 ? 764  SER B O   1 
ATOM   11913 C  CB  . SER B  1 764 ? 4.746   43.595 63.397  1.00 33.93 ? 764  SER B CB  1 
ATOM   11914 O  OG  . SER B  1 764 ? 5.355   44.823 63.754  1.00 34.13 ? 764  SER B OG  1 
ATOM   11915 N  N   . LEU B  1 765 ? 3.553   41.991 60.279  1.00 39.59 ? 765  LEU B N   1 
ATOM   11916 C  CA  . LEU B  1 765 ? 2.693   40.890 59.863  1.00 41.41 ? 765  LEU B CA  1 
ATOM   11917 C  C   . LEU B  1 765 ? 3.492   39.763 59.209  1.00 43.22 ? 765  LEU B C   1 
ATOM   11918 O  O   . LEU B  1 765 ? 4.215   39.990 58.232  1.00 43.09 ? 765  LEU B O   1 
ATOM   11919 C  CB  . LEU B  1 765 ? 1.619   41.393 58.889  1.00 40.94 ? 765  LEU B CB  1 
ATOM   11920 C  CG  . LEU B  1 765 ? 0.598   42.379 59.458  1.00 41.54 ? 765  LEU B CG  1 
ATOM   11921 C  CD1 . LEU B  1 765 ? -0.400  42.781 58.359  1.00 41.01 ? 765  LEU B CD1 1 
ATOM   11922 C  CD2 . LEU B  1 765 ? -0.142  41.740 60.645  1.00 41.23 ? 765  LEU B CD2 1 
ATOM   11923 N  N   . PRO B  1 766 ? 3.353   38.524 59.732  1.00 44.77 ? 766  PRO B N   1 
ATOM   11924 C  CA  . PRO B  1 766 ? 4.047   37.328 59.227  1.00 45.52 ? 766  PRO B CA  1 
ATOM   11925 C  C   . PRO B  1 766 ? 3.757   37.103 57.748  1.00 45.90 ? 766  PRO B C   1 
ATOM   11926 O  O   . PRO B  1 766 ? 4.641   36.543 57.066  1.00 46.34 ? 766  PRO B O   1 
ATOM   11927 C  CB  . PRO B  1 766 ? 3.482   36.192 60.092  1.00 45.82 ? 766  PRO B CB  1 
ATOM   11928 C  CG  . PRO B  1 766 ? 3.090   36.886 61.362  1.00 45.76 ? 766  PRO B CG  1 
ATOM   11929 C  CD  . PRO B  1 766 ? 2.450   38.161 60.842  1.00 45.06 ? 766  PRO B CD  1 
ATOM   11930 O  OXT . PRO B  1 766 ? 2.641   37.467 57.305  1.00 45.60 ? 766  PRO B OXT 1 
HETATM 11931 C  C1  . NAG C  2 .   ? 47.984  80.178 59.089  1.00 55.78 ? 1092 NAG A C1  1 
HETATM 11932 C  C2  . NAG C  2 .   ? 48.665  80.546 60.436  1.00 56.08 ? 1092 NAG A C2  1 
HETATM 11933 C  C3  . NAG C  2 .   ? 48.290  79.532 61.543  1.00 56.37 ? 1092 NAG A C3  1 
HETATM 11934 C  C4  . NAG C  2 .   ? 46.778  79.327 61.602  1.00 56.81 ? 1092 NAG A C4  1 
HETATM 11935 C  C5  . NAG C  2 .   ? 46.281  78.902 60.218  1.00 56.80 ? 1092 NAG A C5  1 
HETATM 11936 C  C6  . NAG C  2 .   ? 44.775  78.648 60.176  1.00 57.25 ? 1092 NAG A C6  1 
HETATM 11937 C  C7  . NAG C  2 .   ? 50.914  81.235 61.082  1.00 56.30 ? 1092 NAG A C7  1 
HETATM 11938 C  C8  . NAG C  2 .   ? 52.405  81.190 60.769  1.00 55.86 ? 1092 NAG A C8  1 
HETATM 11939 N  N2  . NAG C  2 .   ? 50.111  80.571 60.246  1.00 56.05 ? 1092 NAG A N2  1 
HETATM 11940 O  O3  . NAG C  2 .   ? 48.741  80.003 62.805  1.00 56.78 ? 1092 NAG A O3  1 
HETATM 11941 O  O4  . NAG C  2 .   ? 46.446  78.348 62.576  1.00 56.90 ? 1092 NAG A O4  1 
HETATM 11942 O  O5  . NAG C  2 .   ? 46.568  79.951 59.267  1.00 55.87 ? 1092 NAG A O5  1 
HETATM 11943 O  O6  . NAG C  2 .   ? 44.266  78.787 58.852  1.00 57.88 ? 1092 NAG A O6  1 
HETATM 11944 O  O7  . NAG C  2 .   ? 50.507  81.862 62.076  1.00 55.73 ? 1092 NAG A O7  1 
HETATM 11945 C  C1  . NAG D  2 .   ? 46.885  81.680 12.426  1.00 40.07 ? 1281 NAG A C1  1 
HETATM 11946 C  C2  . NAG D  2 .   ? 46.644  82.916 11.549  1.00 41.57 ? 1281 NAG A C2  1 
HETATM 11947 C  C3  . NAG D  2 .   ? 45.198  83.414 11.704  1.00 41.99 ? 1281 NAG A C3  1 
HETATM 11948 C  C4  . NAG D  2 .   ? 44.234  82.267 11.389  1.00 42.01 ? 1281 NAG A C4  1 
HETATM 11949 C  C5  . NAG D  2 .   ? 44.567  81.056 12.280  1.00 41.20 ? 1281 NAG A C5  1 
HETATM 11950 C  C6  . NAG D  2 .   ? 43.681  79.860 11.990  1.00 40.62 ? 1281 NAG A C6  1 
HETATM 11951 C  C7  . NAG D  2 .   ? 48.680  84.138 11.166  1.00 42.37 ? 1281 NAG A C7  1 
HETATM 11952 C  C8  . NAG D  2 .   ? 49.629  85.238 11.601  1.00 42.27 ? 1281 NAG A C8  1 
HETATM 11953 N  N2  . NAG D  2 .   ? 47.586  83.960 11.904  1.00 41.69 ? 1281 NAG A N2  1 
HETATM 11954 O  O3  . NAG D  2 .   ? 44.969  84.498 10.814  1.00 43.49 ? 1281 NAG A O3  1 
HETATM 11955 O  O4  . NAG D  2 .   ? 42.886  82.680 11.594  1.00 43.12 ? 1281 NAG A O4  1 
HETATM 11956 O  O5  . NAG D  2 .   ? 45.945  80.643 12.079  1.00 41.03 ? 1281 NAG A O5  1 
HETATM 11957 O  O6  . NAG D  2 .   ? 44.132  79.148 10.855  1.00 40.28 ? 1281 NAG A O6  1 
HETATM 11958 O  O7  . NAG D  2 .   ? 48.935  83.460 10.161  1.00 41.92 ? 1281 NAG A O7  1 
HETATM 11959 C  C1  . NAG E  2 .   ? 43.201  22.885 38.007  1.00 53.66 ? 1520 NAG A C1  1 
HETATM 11960 C  C2  . NAG E  2 .   ? 42.172  22.066 37.193  1.00 54.38 ? 1520 NAG A C2  1 
HETATM 11961 C  C3  . NAG E  2 .   ? 41.228  22.992 36.389  1.00 54.75 ? 1520 NAG A C3  1 
HETATM 11962 C  C4  . NAG E  2 .   ? 40.634  24.088 37.299  1.00 54.49 ? 1520 NAG A C4  1 
HETATM 11963 C  C5  . NAG E  2 .   ? 41.786  24.824 37.997  1.00 54.66 ? 1520 NAG A C5  1 
HETATM 11964 C  C6  . NAG E  2 .   ? 41.341  25.935 38.929  1.00 54.81 ? 1520 NAG A C6  1 
HETATM 11965 C  C7  . NAG E  2 .   ? 43.733  21.600 35.388  1.00 56.18 ? 1520 NAG A C7  1 
HETATM 11966 C  C8  . NAG E  2 .   ? 44.417  20.566 34.504  1.00 55.79 ? 1520 NAG A C8  1 
HETATM 11967 N  N2  . NAG E  2 .   ? 42.867  21.148 36.299  1.00 55.39 ? 1520 NAG A N2  1 
HETATM 11968 O  O3  . NAG E  2 .   ? 40.177  22.219 35.812  1.00 55.23 ? 1520 NAG A O3  1 
HETATM 11969 O  O4  . NAG E  2 .   ? 39.846  24.999 36.541  1.00 54.62 ? 1520 NAG A O4  1 
HETATM 11970 O  O5  . NAG E  2 .   ? 42.541  23.896 38.793  1.00 54.65 ? 1520 NAG A O5  1 
HETATM 11971 O  O6  . NAG E  2 .   ? 42.456  26.497 39.612  1.00 54.89 ? 1520 NAG A O6  1 
HETATM 11972 O  O7  . NAG E  2 .   ? 43.987  22.799 35.234  1.00 56.76 ? 1520 NAG A O7  1 
HETATM 11973 NA NA  . NA  F  3 .   ? 67.902  58.556 62.056  1.00 23.96 ? 1521 NA  A NA  1 
HETATM 11974 C  C2  . 524 G  4 .   ? 47.879  52.612 33.567  1.00 22.22 ? 1522 524 A C2  1 
HETATM 11975 C  C4  . 524 G  4 .   ? 45.416  52.466 33.168  1.00 20.09 ? 1522 524 A C4  1 
HETATM 11976 C  C5  . 524 G  4 .   ? 45.183  51.939 34.434  1.00 20.60 ? 1522 524 A C5  1 
HETATM 11977 C  C1  . 524 G  4 .   ? 47.630  52.045 34.913  1.00 22.05 ? 1522 524 A C1  1 
HETATM 11978 C  C3  . 524 G  4 .   ? 46.800  52.804 32.738  1.00 21.52 ? 1522 524 A C3  1 
HETATM 11979 N  N6  . 524 G  4 .   ? 46.371  51.739 35.310  1.00 21.72 ? 1522 524 A N6  1 
HETATM 11980 N  N7  . 524 G  4 .   ? 46.382  51.282 36.462  1.00 22.52 ? 1522 524 A N7  1 
HETATM 11981 C  C8  . 524 G  4 .   ? 47.666  51.287 36.844  1.00 21.48 ? 1522 524 A C8  1 
HETATM 11982 N  N9  . 524 G  4 .   ? 48.496  51.765 35.893  1.00 24.10 ? 1522 524 A N9  1 
HETATM 11983 C  C14 . 524 G  4 .   ? 39.491  51.790 36.107  1.00 17.60 ? 1522 524 A C14 1 
HETATM 11984 C  C15 . 524 G  4 .   ? 38.368  51.308 35.148  1.00 17.32 ? 1522 524 A C15 1 
HETATM 11985 C  C16 . 524 G  4 .   ? 36.953  51.246 35.754  1.00 17.34 ? 1522 524 A C16 1 
HETATM 11986 N  N17 . 524 G  4 .   ? 36.158  50.161 35.702  1.00 16.93 ? 1522 524 A N17 1 
HETATM 11987 C  C18 . 524 G  4 .   ? 39.694  50.678 37.237  1.00 18.79 ? 1522 524 A C18 1 
HETATM 11988 N  N19 . 524 G  4 .   ? 38.200  52.221 34.033  1.00 17.53 ? 1522 524 A N19 1 
HETATM 11989 O  O20 . 524 G  4 .   ? 36.535  52.277 36.289  1.00 16.51 ? 1522 524 A O20 1 
HETATM 11990 O  O21 . 524 G  4 .   ? 39.755  49.496 36.802  1.00 18.78 ? 1522 524 A O21 1 
HETATM 11991 N  N22 . 524 G  4 .   ? 39.825  50.916 38.624  1.00 18.81 ? 1522 524 A N22 1 
HETATM 11992 C  C23 . 524 G  4 .   ? 39.790  52.187 39.354  1.00 18.02 ? 1522 524 A C23 1 
HETATM 11993 C  C27 . 524 G  4 .   ? 40.034  49.709 39.458  1.00 18.27 ? 1522 524 A C27 1 
HETATM 11994 C  C31 . 524 G  4 .   ? 36.486  48.867 35.137  1.00 16.49 ? 1522 524 A C31 1 
HETATM 11995 C  C32 . 524 G  4 .   ? 35.208  48.051 35.384  1.00 18.18 ? 1522 524 A C32 1 
HETATM 11996 C  C33 . 524 G  4 .   ? 34.115  48.922 36.045  1.00 17.58 ? 1522 524 A C33 1 
HETATM 11997 C  C34 . 524 G  4 .   ? 34.854  50.298 36.240  1.00 16.90 ? 1522 524 A C34 1 
HETATM 11998 F  F41 . 524 G  4 .   ? 35.495  47.244 36.479  1.00 17.45 ? 1522 524 A F41 1 
HETATM 11999 C  C43 . 524 G  4 .   ? 43.854  51.562 35.007  1.00 18.69 ? 1522 524 A C43 1 
HETATM 12000 C  C44 . 524 G  4 .   ? 43.324  52.776 35.783  1.00 18.14 ? 1522 524 A C44 1 
HETATM 12001 C  C45 . 524 G  4 .   ? 41.953  52.513 36.438  1.00 18.52 ? 1522 524 A C45 1 
HETATM 12002 C  C46 . 524 G  4 .   ? 40.875  52.013 35.406  1.00 17.69 ? 1522 524 A C46 1 
HETATM 12003 C  C47 . 524 G  4 .   ? 41.464  50.784 34.614  1.00 18.11 ? 1522 524 A C47 1 
HETATM 12004 C  C48 . 524 G  4 .   ? 42.796  51.148 33.947  1.00 19.86 ? 1522 524 A C48 1 
HETATM 12005 C  C1  . NAG H  2 .   ? -14.627 31.021 17.104  1.00 51.42 ? 2092 NAG B C1  1 
HETATM 12006 C  C2  . NAG H  2 .   ? -15.377 29.668 17.128  1.00 51.05 ? 2092 NAG B C2  1 
HETATM 12007 C  C3  . NAG H  2 .   ? -15.114 28.920 18.448  1.00 51.03 ? 2092 NAG B C3  1 
HETATM 12008 C  C4  . NAG H  2 .   ? -13.621 28.896 18.806  1.00 51.17 ? 2092 NAG B C4  1 
HETATM 12009 C  C5  . NAG H  2 .   ? -13.066 30.321 18.762  1.00 51.22 ? 2092 NAG B C5  1 
HETATM 12010 C  C6  . NAG H  2 .   ? -11.591 30.434 19.108  1.00 51.33 ? 2092 NAG B C6  1 
HETATM 12011 C  C7  . NAG H  2 .   ? -17.659 28.976 16.649  1.00 53.13 ? 2092 NAG B C7  1 
HETATM 12012 C  C8  . NAG H  2 .   ? -19.131 29.360 16.538  1.00 52.54 ? 2092 NAG B C8  1 
HETATM 12013 N  N2  . NAG H  2 .   ? -16.801 29.935 16.997  1.00 52.23 ? 2092 NAG B N2  1 
HETATM 12014 O  O3  . NAG H  2 .   ? -15.602 27.587 18.357  1.00 50.91 ? 2092 NAG B O3  1 
HETATM 12015 O  O4  . NAG H  2 .   ? -13.445 28.355 20.107  1.00 50.86 ? 2092 NAG B O4  1 
HETATM 12016 O  O5  . NAG H  2 .   ? -13.237 30.858 17.444  1.00 51.58 ? 2092 NAG B O5  1 
HETATM 12017 O  O6  . NAG H  2 .   ? -11.333 31.637 19.825  1.00 51.07 ? 2092 NAG B O6  1 
HETATM 12018 O  O7  . NAG H  2 .   ? -17.312 27.813 16.421  1.00 54.81 ? 2092 NAG B O7  1 
HETATM 12019 C  C1  . NAG I  2 .   ? 4.026   48.273 5.598   1.00 46.17 ? 2150 NAG B C1  1 
HETATM 12020 C  C2  . NAG I  2 .   ? 3.641   48.095 4.115   1.00 47.74 ? 2150 NAG B C2  1 
HETATM 12021 C  C3  . NAG I  2 .   ? 3.942   46.668 3.593   1.00 48.71 ? 2150 NAG B C3  1 
HETATM 12022 C  C4  . NAG I  2 .   ? 5.384   46.271 3.941   1.00 49.53 ? 2150 NAG B C4  1 
HETATM 12023 C  C5  . NAG I  2 .   ? 5.584   46.433 5.460   1.00 49.55 ? 2150 NAG B C5  1 
HETATM 12024 C  C6  . NAG I  2 .   ? 6.984   46.038 5.932   1.00 49.79 ? 2150 NAG B C6  1 
HETATM 12025 C  C7  . NAG I  2 .   ? 1.856   49.503 3.320   1.00 48.01 ? 2150 NAG B C7  1 
HETATM 12026 C  C8  . NAG I  2 .   ? 0.360   49.759 3.199   1.00 47.90 ? 2150 NAG B C8  1 
HETATM 12027 N  N2  . NAG I  2 .   ? 2.229   48.401 3.960   1.00 47.90 ? 2150 NAG B N2  1 
HETATM 12028 O  O3  . NAG I  2 .   ? 3.768   46.630 2.175   1.00 49.14 ? 2150 NAG B O3  1 
HETATM 12029 O  O4  . NAG I  2 .   ? 5.654   44.931 3.539   1.00 49.93 ? 2150 NAG B O4  1 
HETATM 12030 O  O5  . NAG I  2 .   ? 5.374   47.820 5.835   1.00 48.25 ? 2150 NAG B O5  1 
HETATM 12031 O  O6  . NAG I  2 .   ? 7.982   46.920 5.421   1.00 51.56 ? 2150 NAG B O6  1 
HETATM 12032 O  O7  . NAG I  2 .   ? 2.665   50.298 2.827   1.00 48.10 ? 2150 NAG B O7  1 
HETATM 12033 C  C1  . NAG J  2 .   ? -9.451  85.964 36.557  1.00 46.37 ? 2321 NAG B C1  1 
HETATM 12034 C  C2  . NAG J  2 .   ? -10.218 86.554 37.716  1.00 48.37 ? 2321 NAG B C2  1 
HETATM 12035 C  C3  . NAG J  2 .   ? -9.291  87.613 38.360  1.00 49.02 ? 2321 NAG B C3  1 
HETATM 12036 C  C4  . NAG J  2 .   ? -7.988  86.917 38.831  1.00 49.48 ? 2321 NAG B C4  1 
HETATM 12037 C  C5  . NAG J  2 .   ? -7.340  86.104 37.677  1.00 49.22 ? 2321 NAG B C5  1 
HETATM 12038 C  C6  . NAG J  2 .   ? -6.179  85.225 38.144  1.00 50.10 ? 2321 NAG B C6  1 
HETATM 12039 C  C7  . NAG J  2 .   ? -12.643 86.555 37.500  1.00 49.53 ? 2321 NAG B C7  1 
HETATM 12040 C  C8  . NAG J  2 .   ? -13.878 87.210 36.903  1.00 50.05 ? 2321 NAG B C8  1 
HETATM 12041 N  N2  . NAG J  2 .   ? -11.465 87.116 37.213  1.00 49.11 ? 2321 NAG B N2  1 
HETATM 12042 O  O3  . NAG J  2 .   ? -9.942  88.236 39.455  1.00 50.22 ? 2321 NAG B O3  1 
HETATM 12043 O  O4  . NAG J  2 .   ? -7.063  87.881 39.332  1.00 48.95 ? 2321 NAG B O4  1 
HETATM 12044 O  O5  . NAG J  2 .   ? -8.317  85.232 37.047  1.00 48.16 ? 2321 NAG B O5  1 
HETATM 12045 O  O6  . NAG J  2 .   ? -6.638  83.997 38.704  1.00 50.21 ? 2321 NAG B O6  1 
HETATM 12046 O  O7  . NAG J  2 .   ? -12.767 85.567 38.229  1.00 49.36 ? 2321 NAG B O7  1 
HETATM 12047 C  C2  . 524 K  4 .   ? -11.756 66.462 30.170  1.00 19.47 ? 2322 524 B C2  1 
HETATM 12048 C  C4  . 524 K  4 .   ? -9.392  66.553 30.980  1.00 19.74 ? 2322 524 B C4  1 
HETATM 12049 C  C5  . 524 K  4 .   ? -9.656  65.701 32.042  1.00 19.49 ? 2322 524 B C5  1 
HETATM 12050 C  C1  . 524 K  4 .   ? -12.022 65.551 31.314  1.00 20.22 ? 2322 524 B C1  1 
HETATM 12051 C  C3  . 524 K  4 .   ? -10.489 66.939 30.018  1.00 20.39 ? 2322 524 B C3  1 
HETATM 12052 N  N6  . 524 K  4 .   ? -11.029 65.209 32.173  1.00 20.73 ? 2322 524 B N6  1 
HETATM 12053 N  N7  . 524 K  4 .   ? -11.451 64.448 33.045  1.00 20.53 ? 2322 524 B N7  1 
HETATM 12054 C  C8  . 524 K  4 .   ? -12.757 64.277 32.769  1.00 22.21 ? 2322 524 B C8  1 
HETATM 12055 N  N9  . 524 K  4 .   ? -13.160 64.958 31.681  1.00 21.53 ? 2322 524 B N9  1 
HETATM 12056 C  C14 . 524 K  4 .   ? -4.872  63.437 34.743  1.00 15.50 ? 2322 524 B C14 1 
HETATM 12057 C  C15 . 524 K  4 .   ? -3.628  64.322 35.026  1.00 15.54 ? 2322 524 B C15 1 
HETATM 12058 C  C16 . 524 K  4 .   ? -2.464  63.590 35.733  1.00 15.76 ? 2322 524 B C16 1 
HETATM 12059 N  N17 . 524 K  4 .   ? -1.893  64.007 36.881  1.00 16.37 ? 2322 524 B N17 1 
HETATM 12060 C  C18 . 524 K  4 .   ? -5.555  63.049 36.131  1.00 15.88 ? 2322 524 B C18 1 
HETATM 12061 N  N19 . 524 K  4 .   ? -3.037  64.800 33.778  1.00 14.21 ? 2322 524 B N19 1 
HETATM 12062 O  O20 . 524 K  4 .   ? -2.024  62.563 35.163  1.00 14.91 ? 2322 524 B O20 1 
HETATM 12063 O  O21 . 524 K  4 .   ? -5.620  63.984 36.969  1.00 16.02 ? 2322 524 B O21 1 
HETATM 12064 N  N22 . 524 K  4 .   ? -6.083  61.793 36.448  1.00 16.12 ? 2322 524 B N22 1 
HETATM 12065 C  C23 . 524 K  4 .   ? -6.114  60.583 35.617  1.00 15.09 ? 2322 524 B C23 1 
HETATM 12066 C  C27 . 524 K  4 .   ? -6.702  61.687 37.793  1.00 17.28 ? 2322 524 B C27 1 
HETATM 12067 C  C31 . 524 K  4 .   ? -2.280  65.139 37.677  1.00 16.20 ? 2322 524 B C31 1 
HETATM 12068 C  C32 . 524 K  4 .   ? -1.312  65.084 38.839  1.00 17.35 ? 2322 524 B C32 1 
HETATM 12069 C  C33 . 524 K  4 .   ? -0.302  63.935 38.675  1.00 17.64 ? 2322 524 B C33 1 
HETATM 12070 C  C34 . 524 K  4 .   ? -0.794  63.263 37.355  1.00 16.88 ? 2322 524 B C34 1 
HETATM 12071 F  F41 . 524 K  4 .   ? -2.044  64.542 39.876  1.00 17.64 ? 2322 524 B F41 1 
HETATM 12072 C  C43 . 524 K  4 .   ? -8.679  65.216 33.072  1.00 18.84 ? 2322 524 B C43 1 
HETATM 12073 C  C44 . 524 K  4 .   ? -8.182  63.851 32.607  1.00 17.67 ? 2322 524 B C44 1 
HETATM 12074 C  C45 . 524 K  4 .   ? -7.152  63.219 33.552  1.00 16.68 ? 2322 524 B C45 1 
HETATM 12075 C  C46 . 524 K  4 .   ? -5.933  64.151 33.841  1.00 15.82 ? 2322 524 B C46 1 
HETATM 12076 C  C47 . 524 K  4 .   ? -6.490  65.546 34.350  1.00 17.06 ? 2322 524 B C47 1 
HETATM 12077 C  C48 . 524 K  4 .   ? -7.469  66.141 33.303  1.00 17.25 ? 2322 524 B C48 1 
HETATM 12078 C  C1  . NAG L  2 .   ? 69.340  74.554 56.418  1.00 39.11 ? 1085 NAG L C1  1 
HETATM 12079 C  C2  . NAG L  2 .   ? 68.920  75.753 55.517  1.00 40.03 ? 1085 NAG L C2  1 
HETATM 12080 C  C3  . NAG L  2 .   ? 70.113  76.306 54.724  1.00 41.69 ? 1085 NAG L C3  1 
HETATM 12081 C  C4  . NAG L  2 .   ? 71.106  76.705 55.789  1.00 43.08 ? 1085 NAG L C4  1 
HETATM 12082 C  C5  . NAG L  2 .   ? 71.612  75.445 56.485  1.00 42.30 ? 1085 NAG L C5  1 
HETATM 12083 C  C6  . NAG L  2 .   ? 72.708  75.758 57.501  1.00 42.39 ? 1085 NAG L C6  1 
HETATM 12084 C  C7  . NAG L  2 .   ? 66.603  75.680 54.837  1.00 39.28 ? 1085 NAG L C7  1 
HETATM 12085 C  C8  . NAG L  2 .   ? 65.577  75.227 53.815  1.00 38.43 ? 1085 NAG L C8  1 
HETATM 12086 N  N2  . NAG L  2 .   ? 67.872  75.359 54.597  1.00 39.19 ? 1085 NAG L N2  1 
HETATM 12087 O  O3  . NAG L  2 .   ? 69.707  77.439 53.946  1.00 40.98 ? 1085 NAG L O3  1 
HETATM 12088 O  O4  . NAG L  2 .   ? 72.190  77.531 55.313  1.00 47.55 ? 1085 NAG L O4  1 
HETATM 12089 O  O5  . NAG L  2 .   ? 70.515  74.838 57.215  1.00 40.34 ? 1085 NAG L O5  1 
HETATM 12090 O  O6  . NAG L  2 .   ? 73.431  74.590 57.876  1.00 43.77 ? 1085 NAG L O6  1 
HETATM 12091 O  O7  . NAG L  2 .   ? 66.239  76.306 55.838  1.00 39.56 ? 1085 NAG L O7  1 
HETATM 12092 C  C1  . NDG M  5 .   ? 72.801  77.334 54.080  1.00 49.98 ? 1086 NDG L C1  1 
HETATM 12093 C  C2  . NDG M  5 .   ? 74.172  78.018 54.126  1.00 51.07 ? 1086 NDG L C2  1 
HETATM 12094 C  C3  . NDG M  5 .   ? 73.980  79.477 54.573  1.00 51.73 ? 1086 NDG L C3  1 
HETATM 12095 C  C4  . NDG M  5 .   ? 72.939  80.198 53.681  1.00 51.87 ? 1086 NDG L C4  1 
HETATM 12096 C  C5  . NDG M  5 .   ? 71.659  79.351 53.463  1.00 51.22 ? 1086 NDG L C5  1 
HETATM 12097 C  C6  . NDG M  5 .   ? 70.732  79.888 52.380  1.00 50.90 ? 1086 NDG L C6  1 
HETATM 12098 C  C7  . NDG M  5 .   ? 75.797  76.297 54.634  1.00 52.47 ? 1086 NDG L C7  1 
HETATM 12099 C  C8  . NDG M  5 .   ? 76.700  75.623 55.660  1.00 52.53 ? 1086 NDG L C8  1 
HETATM 12100 O  O   . NDG M  5 .   ? 71.998  77.991 53.086  1.00 51.57 ? 1086 NDG L O   1 
HETATM 12101 O  O3  . NDG M  5 .   ? 75.220  80.177 54.540  1.00 52.49 ? 1086 NDG L O3  1 
HETATM 12102 O  O4  . NDG M  5 .   ? 72.590  81.436 54.288  1.00 52.05 ? 1086 NDG L O4  1 
HETATM 12103 O  O6  . NDG M  5 .   ? 70.544  78.935 51.341  1.00 50.30 ? 1086 NDG L O6  1 
HETATM 12104 O  O7  . NDG M  5 .   ? 75.765  75.872 53.476  1.00 52.84 ? 1086 NDG L O7  1 
HETATM 12105 N  N2  . NDG M  5 .   ? 75.060  77.328 55.048  1.00 51.83 ? 1086 NDG L N2  1 
HETATM 12106 C  C1  . NDG N  5 .   ? 37.244  85.053 33.623  1.00 48.17 ? 1150 NDG M C1  1 
HETATM 12107 C  C2  . NDG N  5 .   ? 37.995  86.245 32.994  1.00 50.00 ? 1150 NDG M C2  1 
HETATM 12108 C  C3  . NDG N  5 .   ? 38.343  87.281 34.065  1.00 50.82 ? 1150 NDG M C3  1 
HETATM 12109 C  C4  . NDG N  5 .   ? 37.158  87.597 35.004  1.00 51.04 ? 1150 NDG M C4  1 
HETATM 12110 C  C5  . NDG N  5 .   ? 36.410  86.342 35.465  1.00 49.79 ? 1150 NDG M C5  1 
HETATM 12111 C  C6  . NDG N  5 .   ? 35.090  86.716 36.138  1.00 49.18 ? 1150 NDG M C6  1 
HETATM 12112 C  C7  . NDG N  5 .   ? 39.880  86.493 31.466  1.00 52.32 ? 1150 NDG M C7  1 
HETATM 12113 C  C8  . NDG N  5 .   ? 41.143  85.889 30.867  1.00 52.37 ? 1150 NDG M C8  1 
HETATM 12114 O  O   . NDG N  5 .   ? 36.082  85.506 34.334  1.00 49.01 ? 1150 NDG M O   1 
HETATM 12115 O  O3  . NDG N  5 .   ? 38.757  88.488 33.424  1.00 51.64 ? 1150 NDG M O3  1 
HETATM 12116 O  O4  . NDG N  5 .   ? 37.668  88.277 36.171  1.00 53.34 ? 1150 NDG M O4  1 
HETATM 12117 O  O6  . NDG N  5 .   ? 34.147  87.236 35.197  1.00 47.88 ? 1150 NDG M O6  1 
HETATM 12118 O  O7  . NDG N  5 .   ? 39.518  87.620 31.112  1.00 53.85 ? 1150 NDG M O7  1 
HETATM 12119 N  N2  . NDG N  5 .   ? 39.223  85.761 32.369  1.00 51.51 ? 1150 NDG M N2  1 
HETATM 12120 C  C1  . NAG O  2 .   ? 37.250  89.582 36.418  1.00 54.61 ? 1151 NAG M C1  1 
HETATM 12121 C  C2  . NAG O  2 .   ? 37.349  90.432 35.139  1.00 55.58 ? 1151 NAG M C2  1 
HETATM 12122 C  C3  . NAG O  2 .   ? 36.751  91.834 35.353  1.00 55.55 ? 1151 NAG M C3  1 
HETATM 12123 C  C4  . NAG O  2 .   ? 35.369  91.760 36.042  1.00 55.42 ? 1151 NAG M C4  1 
HETATM 12124 C  C5  . NAG O  2 .   ? 35.439  90.858 37.282  1.00 54.99 ? 1151 NAG M C5  1 
HETATM 12125 C  C6  . NAG O  2 .   ? 34.109  90.681 37.987  1.00 54.57 ? 1151 NAG M C6  1 
HETATM 12126 C  C7  . NAG O  2 .   ? 39.662  91.053 35.540  1.00 56.77 ? 1151 NAG M C7  1 
HETATM 12127 C  C8  . NAG O  2 .   ? 41.093  91.123 35.020  1.00 56.67 ? 1151 NAG M C8  1 
HETATM 12128 N  N2  . NAG O  2 .   ? 38.743  90.543 34.719  1.00 56.24 ? 1151 NAG M N2  1 
HETATM 12129 O  O3  . NAG O  2 .   ? 36.630  92.473 34.087  1.00 55.84 ? 1151 NAG M O3  1 
HETATM 12130 O  O4  . NAG O  2 .   ? 34.939  93.061 36.416  1.00 55.94 ? 1151 NAG M O4  1 
HETATM 12131 O  O5  . NAG O  2 .   ? 35.900  89.547 36.903  1.00 55.34 ? 1151 NAG M O5  1 
HETATM 12132 O  O6  . NAG O  2 .   ? 34.153  89.572 38.871  1.00 54.29 ? 1151 NAG M O6  1 
HETATM 12133 O  O7  . NAG O  2 .   ? 39.396  91.465 36.675  1.00 57.03 ? 1151 NAG M O7  1 
HETATM 12134 C  C1  . NAG P  2 .   ? 67.558  72.494 25.726  1.00 33.13 ? 1219 NAG N C1  1 
HETATM 12135 C  C2  . NAG P  2 .   ? 68.496  73.695 25.806  1.00 35.04 ? 1219 NAG N C2  1 
HETATM 12136 C  C3  . NAG P  2 .   ? 68.606  74.366 24.427  1.00 35.82 ? 1219 NAG N C3  1 
HETATM 12137 C  C4  . NAG P  2 .   ? 68.950  73.332 23.350  1.00 35.78 ? 1219 NAG N C4  1 
HETATM 12138 C  C5  . NAG P  2 .   ? 67.960  72.161 23.420  1.00 34.66 ? 1219 NAG N C5  1 
HETATM 12139 C  C6  . NAG P  2 .   ? 68.239  71.070 22.419  1.00 33.15 ? 1219 NAG N C6  1 
HETATM 12140 C  C7  . NAG P  2 .   ? 68.450  74.666 27.999  1.00 38.90 ? 1219 NAG N C7  1 
HETATM 12141 C  C8  . NAG P  2 .   ? 67.830  75.657 28.966  1.00 39.67 ? 1219 NAG N C8  1 
HETATM 12142 N  N2  . NAG P  2 .   ? 67.956  74.633 26.768  1.00 36.94 ? 1219 NAG N N2  1 
HETATM 12143 O  O3  . NAG P  2 .   ? 69.593  75.385 24.462  1.00 34.53 ? 1219 NAG N O3  1 
HETATM 12144 O  O4  . NAG P  2 .   ? 68.869  73.951 22.061  1.00 39.02 ? 1219 NAG N O4  1 
HETATM 12145 O  O5  . NAG P  2 .   ? 67.999  71.567 24.733  1.00 32.97 ? 1219 NAG N O5  1 
HETATM 12146 O  O6  . NAG P  2 .   ? 69.479  70.448 22.700  1.00 32.37 ? 1219 NAG N O6  1 
HETATM 12147 O  O7  . NAG P  2 .   ? 69.387  73.948 28.362  1.00 40.31 ? 1219 NAG N O7  1 
HETATM 12148 C  C1  . NAG Q  2 .   ? 69.937  73.752 21.195  1.00 42.95 ? 1220 NAG N C1  1 
HETATM 12149 C  C2  . NAG Q  2 .   ? 69.526  74.206 19.791  1.00 43.93 ? 1220 NAG N C2  1 
HETATM 12150 C  C3  . NAG Q  2 .   ? 70.729  74.165 18.833  1.00 45.53 ? 1220 NAG N C3  1 
HETATM 12151 C  C4  . NAG Q  2 .   ? 71.935  74.907 19.414  1.00 46.60 ? 1220 NAG N C4  1 
HETATM 12152 C  C5  . NAG Q  2 .   ? 72.227  74.383 20.831  1.00 46.58 ? 1220 NAG N C5  1 
HETATM 12153 C  C6  . NAG Q  2 .   ? 73.366  75.126 21.507  1.00 47.20 ? 1220 NAG N C6  1 
HETATM 12154 C  C7  . NAG Q  2 .   ? 67.211  73.688 19.337  1.00 43.23 ? 1220 NAG N C7  1 
HETATM 12155 C  C8  . NAG Q  2 .   ? 66.206  72.687 18.792  1.00 43.27 ? 1220 NAG N C8  1 
HETATM 12156 N  N2  . NAG Q  2 .   ? 68.488  73.322 19.293  1.00 43.47 ? 1220 NAG N N2  1 
HETATM 12157 O  O3  . NAG Q  2 .   ? 70.369  74.742 17.584  1.00 46.66 ? 1220 NAG N O3  1 
HETATM 12158 O  O4  . NAG Q  2 .   ? 73.066  74.695 18.572  1.00 48.56 ? 1220 NAG N O4  1 
HETATM 12159 O  O5  . NAG Q  2 .   ? 71.055  74.529 21.669  1.00 44.91 ? 1220 NAG N O5  1 
HETATM 12160 O  O6  . NAG Q  2 .   ? 73.007  76.475 21.774  1.00 48.64 ? 1220 NAG N O6  1 
HETATM 12161 O  O7  . NAG Q  2 .   ? 66.827  74.774 19.793  1.00 43.06 ? 1220 NAG N O7  1 
HETATM 12162 C  C1  . NAG R  2 .   ? 38.281  64.554 12.545  1.00 29.93 ? 1229 NAG O C1  1 
HETATM 12163 C  C2  . NAG R  2 .   ? 38.963  65.442 11.485  1.00 31.79 ? 1229 NAG O C2  1 
HETATM 12164 C  C3  . NAG R  2 .   ? 38.027  65.659 10.300  1.00 34.27 ? 1229 NAG O C3  1 
HETATM 12165 C  C4  . NAG R  2 .   ? 37.565  64.308 9.751   1.00 35.48 ? 1229 NAG O C4  1 
HETATM 12166 C  C5  . NAG R  2 .   ? 36.920  63.501 10.890  1.00 34.82 ? 1229 NAG O C5  1 
HETATM 12167 C  C6  . NAG R  2 .   ? 36.429  62.129 10.481  1.00 34.71 ? 1229 NAG O C6  1 
HETATM 12168 C  C7  . NAG R  2 .   ? 40.599  67.019 12.268  1.00 32.34 ? 1229 NAG O C7  1 
HETATM 12169 C  C8  . NAG R  2 .   ? 40.906  68.394 12.835  1.00 32.68 ? 1229 NAG O C8  1 
HETATM 12170 N  N2  . NAG R  2 .   ? 39.324  66.734 12.037  1.00 31.83 ? 1229 NAG O N2  1 
HETATM 12171 O  O3  . NAG R  2 .   ? 38.695  66.413 9.295   1.00 34.80 ? 1229 NAG O O3  1 
HETATM 12172 O  O4  . NAG R  2 .   ? 36.623  64.515 8.683   1.00 39.94 ? 1229 NAG O O4  1 
HETATM 12173 O  O5  . NAG R  2 .   ? 37.873  63.312 11.959  1.00 30.39 ? 1229 NAG O O5  1 
HETATM 12174 O  O6  . NAG R  2 .   ? 35.982  61.391 11.608  1.00 37.51 ? 1229 NAG O O6  1 
HETATM 12175 O  O7  . NAG R  2 .   ? 41.513  66.215 12.058  1.00 33.39 ? 1229 NAG O O7  1 
HETATM 12176 C  C1  . NDG S  5 .   ? 36.602  63.504 7.738   1.00 44.11 ? 1230 NDG O C1  1 
HETATM 12177 C  C2  . NDG S  5 .   ? 36.817  64.018 6.289   1.00 46.39 ? 1230 NDG O C2  1 
HETATM 12178 C  C3  . NDG S  5 .   ? 35.531  64.490 5.579   1.00 46.97 ? 1230 NDG O C3  1 
HETATM 12179 C  C4  . NDG S  5 .   ? 34.348  63.575 5.883   1.00 47.14 ? 1230 NDG O C4  1 
HETATM 12180 C  C5  . NDG S  5 .   ? 34.238  63.459 7.400   1.00 45.87 ? 1230 NDG O C5  1 
HETATM 12181 C  C6  . NDG S  5 .   ? 33.024  62.712 7.889   1.00 46.13 ? 1230 NDG O C6  1 
HETATM 12182 C  C7  . NDG S  5 .   ? 37.521  66.304 6.704   1.00 49.49 ? 1230 NDG O C7  1 
HETATM 12183 C  C8  . NDG S  5 .   ? 38.603  67.374 6.564   1.00 49.49 ? 1230 NDG O C8  1 
HETATM 12184 O  O   . NDG S  5 .   ? 35.384  62.757 7.889   1.00 45.94 ? 1230 NDG O O   1 
HETATM 12185 O  O3  . NDG S  5 .   ? 35.756  64.512 4.171   1.00 47.38 ? 1230 NDG O O3  1 
HETATM 12186 O  O4  . NDG S  5 .   ? 33.153  64.110 5.332   1.00 47.97 ? 1230 NDG O O4  1 
HETATM 12187 O  O6  . NDG S  5 .   ? 32.688  63.129 9.200   1.00 46.45 ? 1230 NDG O O6  1 
HETATM 12188 O  O7  . NDG S  5 .   ? 36.453  66.582 7.259   1.00 49.88 ? 1230 NDG O O7  1 
HETATM 12189 N  N2  . NDG S  5 .   ? 37.801  65.087 6.232   1.00 48.33 ? 1230 NDG O N2  1 
HETATM 12190 C  C1  . NDG T  5 .   ? 46.757  38.490 20.015  1.00 46.42 ? 1321 NDG P C1  1 
HETATM 12191 C  C2  . NDG T  5 .   ? 47.384  37.288 19.299  1.00 47.90 ? 1321 NDG P C2  1 
HETATM 12192 C  C3  . NDG T  5 .   ? 46.601  37.020 18.000  1.00 49.31 ? 1321 NDG P C3  1 
HETATM 12193 C  C4  . NDG T  5 .   ? 45.070  36.912 18.233  1.00 49.88 ? 1321 NDG P C4  1 
HETATM 12194 C  C5  . NDG T  5 .   ? 44.560  38.070 19.139  1.00 49.12 ? 1321 NDG P C5  1 
HETATM 12195 C  C6  . NDG T  5 .   ? 43.112  37.907 19.606  1.00 48.68 ? 1321 NDG P C6  1 
HETATM 12196 C  C7  . NDG T  5 .   ? 49.763  36.893 19.571  1.00 49.83 ? 1321 NDG P C7  1 
HETATM 12197 C  C8  . NDG T  5 .   ? 51.189  37.270 19.193  1.00 49.29 ? 1321 NDG P C8  1 
HETATM 12198 O  O   . NDG T  5 .   ? 45.382  38.213 20.328  1.00 47.41 ? 1321 NDG P O   1 
HETATM 12199 O  O3  . NDG T  5 .   ? 47.085  35.842 17.370  1.00 48.64 ? 1321 NDG P O3  1 
HETATM 12200 O  O4  . NDG T  5 .   ? 44.410  37.010 16.944  1.00 52.26 ? 1321 NDG P O4  1 
HETATM 12201 O  O6  . NDG T  5 .   ? 42.952  36.769 20.451  1.00 48.75 ? 1321 NDG P O6  1 
HETATM 12202 O  O7  . NDG T  5 .   ? 49.564  35.981 20.388  1.00 50.59 ? 1321 NDG P O7  1 
HETATM 12203 N  N2  . NDG T  5 .   ? 48.778  37.578 18.987  1.00 48.93 ? 1321 NDG P N2  1 
HETATM 12204 C  C1  . NAG U  2 .   ? 43.659  35.939 16.459  1.00 53.26 ? 1322 NAG P C1  1 
HETATM 12205 C  C2  . NAG U  2 .   ? 44.543  34.705 16.216  1.00 53.80 ? 1322 NAG P C2  1 
HETATM 12206 C  C3  . NAG U  2 .   ? 43.661  33.519 15.770  1.00 53.80 ? 1322 NAG P C3  1 
HETATM 12207 C  C4  . NAG U  2 .   ? 42.466  33.308 16.709  1.00 53.63 ? 1322 NAG P C4  1 
HETATM 12208 C  C5  . NAG U  2 .   ? 41.717  34.631 16.902  1.00 53.25 ? 1322 NAG P C5  1 
HETATM 12209 C  C6  . NAG U  2 .   ? 40.554  34.547 17.885  1.00 52.96 ? 1322 NAG P C6  1 
HETATM 12210 C  C7  . NAG U  2 .   ? 45.206  35.508 14.011  1.00 55.03 ? 1322 NAG P C7  1 
HETATM 12211 C  C8  . NAG U  2 .   ? 46.343  35.752 13.022  1.00 54.67 ? 1322 NAG P C8  1 
HETATM 12212 N  N2  . NAG U  2 .   ? 45.548  34.989 15.195  1.00 54.41 ? 1322 NAG P N2  1 
HETATM 12213 O  O3  . NAG U  2 .   ? 44.443  32.334 15.723  1.00 53.52 ? 1322 NAG P O3  1 
HETATM 12214 O  O4  . NAG U  2 .   ? 41.594  32.336 16.153  1.00 53.79 ? 1322 NAG P O4  1 
HETATM 12215 O  O5  . NAG U  2 .   ? 42.621  35.635 17.399  1.00 54.09 ? 1322 NAG P O5  1 
HETATM 12216 O  O6  . NAG U  2 .   ? 39.729  35.705 17.801  1.00 51.72 ? 1322 NAG P O6  1 
HETATM 12217 O  O7  . NAG U  2 .   ? 44.037  35.801 13.699  1.00 54.69 ? 1322 NAG P O7  1 
HETATM 12218 C  C1  . NAG V  2 .   ? -33.584 38.636 14.345  1.00 42.77 ? 2085 NAG Q C1  1 
HETATM 12219 C  C2  . NAG V  2 .   ? -32.775 38.792 13.056  1.00 43.99 ? 2085 NAG Q C2  1 
HETATM 12220 C  C3  . NAG V  2 .   ? -33.637 39.439 11.957  1.00 45.51 ? 2085 NAG Q C3  1 
HETATM 12221 C  C4  . NAG V  2 .   ? -35.008 38.748 11.817  1.00 47.20 ? 2085 NAG Q C4  1 
HETATM 12222 C  C5  . NAG V  2 .   ? -35.661 38.588 13.192  1.00 46.49 ? 2085 NAG Q C5  1 
HETATM 12223 C  C6  . NAG V  2 .   ? -36.979 37.824 13.169  1.00 47.51 ? 2085 NAG Q C6  1 
HETATM 12224 C  C7  . NAG V  2 .   ? -30.414 39.030 13.523  1.00 41.65 ? 2085 NAG Q C7  1 
HETATM 12225 C  C8  . NAG V  2 .   ? -29.226 39.945 13.779  1.00 41.17 ? 2085 NAG Q C8  1 
HETATM 12226 N  N2  . NAG V  2 .   ? -31.596 39.606 13.311  1.00 42.36 ? 2085 NAG Q N2  1 
HETATM 12227 O  O3  . NAG V  2 .   ? -32.943 39.405 10.717  1.00 46.18 ? 2085 NAG Q O3  1 
HETATM 12228 O  O4  . NAG V  2 .   ? -35.869 39.560 11.003  1.00 50.64 ? 2085 NAG Q O4  1 
HETATM 12229 O  O5  . NAG V  2 .   ? -34.776 37.894 14.086  1.00 44.52 ? 2085 NAG Q O5  1 
HETATM 12230 O  O6  . NAG V  2 .   ? -36.773 36.413 13.215  1.00 49.23 ? 2085 NAG Q O6  1 
HETATM 12231 O  O7  . NAG V  2 .   ? -30.258 37.808 13.523  1.00 41.13 ? 2085 NAG Q O7  1 
HETATM 12232 C  C1  . NAG W  2 .   ? -35.820 39.422 9.620   1.00 53.94 ? 2086 NAG Q C1  1 
HETATM 12233 C  C2  . NAG W  2 .   ? -36.795 38.322 9.157   1.00 55.34 ? 2086 NAG Q C2  1 
HETATM 12234 C  C3  . NAG W  2 .   ? -36.895 38.294 7.616   1.00 56.03 ? 2086 NAG Q C3  1 
HETATM 12235 C  C4  . NAG W  2 .   ? -37.193 39.698 7.059   1.00 56.56 ? 2086 NAG Q C4  1 
HETATM 12236 C  C5  . NAG W  2 .   ? -36.155 40.687 7.611   1.00 56.64 ? 2086 NAG Q C5  1 
HETATM 12237 C  C6  . NAG W  2 .   ? -36.360 42.125 7.141   1.00 56.80 ? 2086 NAG Q C6  1 
HETATM 12238 C  C7  . NAG W  2 .   ? -37.129 36.268 10.415  1.00 58.04 ? 2086 NAG Q C7  1 
HETATM 12239 C  C8  . NAG W  2 .   ? -36.553 34.922 10.856  1.00 57.81 ? 2086 NAG Q C8  1 
HETATM 12240 N  N2  . NAG W  2 .   ? -36.346 37.025 9.639   1.00 56.98 ? 2086 NAG Q N2  1 
HETATM 12241 O  O3  . NAG W  2 .   ? -37.927 37.398 7.221   1.00 56.47 ? 2086 NAG Q O3  1 
HETATM 12242 O  O4  . NAG W  2 .   ? -37.154 39.685 5.637   1.00 56.70 ? 2086 NAG Q O4  1 
HETATM 12243 O  O5  . NAG W  2 .   ? -36.208 40.688 9.057   1.00 55.52 ? 2086 NAG Q O5  1 
HETATM 12244 O  O6  . NAG W  2 .   ? -37.632 42.622 7.544   1.00 58.04 ? 2086 NAG Q O6  1 
HETATM 12245 O  O7  . NAG W  2 .   ? -38.270 36.608 10.783  1.00 58.29 ? 2086 NAG Q O7  1 
HETATM 12246 C  C1  . NAG X  2 .   ? -24.509 67.611 4.185   1.00 32.17 ? 2219 NAG R C1  1 
HETATM 12247 C  C2  . NAG X  2 .   ? -25.265 67.259 2.903   1.00 34.92 ? 2219 NAG R C2  1 
HETATM 12248 C  C3  . NAG X  2 .   ? -24.857 68.232 1.777   1.00 36.14 ? 2219 NAG R C3  1 
HETATM 12249 C  C4  . NAG X  2 .   ? -24.925 69.696 2.233   1.00 35.85 ? 2219 NAG R C4  1 
HETATM 12250 C  C5  . NAG X  2 .   ? -24.170 69.862 3.559   1.00 34.00 ? 2219 NAG R C5  1 
HETATM 12251 C  C6  . NAG X  2 .   ? -24.266 71.257 4.125   1.00 33.12 ? 2219 NAG R C6  1 
HETATM 12252 C  C7  . NAG X  2 .   ? -25.760 64.921 2.586   1.00 37.41 ? 2219 NAG R C7  1 
HETATM 12253 C  C8  . NAG X  2 .   ? -25.246 63.548 2.178   1.00 37.45 ? 2219 NAG R C8  1 
HETATM 12254 N  N2  . NAG X  2 .   ? -24.886 65.915 2.525   1.00 36.46 ? 2219 NAG R N2  1 
HETATM 12255 O  O3  . NAG X  2 .   ? -25.689 68.046 0.637   1.00 37.48 ? 2219 NAG R O3  1 
HETATM 12256 O  O4  . NAG X  2 .   ? -24.312 70.525 1.233   1.00 38.35 ? 2219 NAG R O4  1 
HETATM 12257 O  O5  . NAG X  2 .   ? -24.725 68.975 4.540   1.00 32.53 ? 2219 NAG R O5  1 
HETATM 12258 O  O6  . NAG X  2 .   ? -25.617 71.583 4.390   1.00 33.02 ? 2219 NAG R O6  1 
HETATM 12259 O  O7  . NAG X  2 .   ? -26.933 65.073 2.929   1.00 38.01 ? 2219 NAG R O7  1 
HETATM 12260 C  C1  . NAG Y  2 .   ? -25.078 71.555 0.711   1.00 40.44 ? 2220 NAG R C1  1 
HETATM 12261 C  C2  . NAG Y  2 .   ? -24.161 72.466 -0.113  1.00 40.67 ? 2220 NAG R C2  1 
HETATM 12262 C  C3  . NAG Y  2 .   ? -24.969 73.512 -0.899  1.00 41.71 ? 2220 NAG R C3  1 
HETATM 12263 C  C4  . NAG Y  2 .   ? -26.062 72.824 -1.712  1.00 42.64 ? 2220 NAG R C4  1 
HETATM 12264 C  C5  . NAG Y  2 .   ? -26.920 71.964 -0.778  1.00 43.08 ? 2220 NAG R C5  1 
HETATM 12265 C  C6  . NAG Y  2 .   ? -28.025 71.218 -1.514  1.00 43.52 ? 2220 NAG R C6  1 
HETATM 12266 C  C7  . NAG Y  2 .   ? -21.959 72.752 0.804   1.00 39.85 ? 2220 NAG R C7  1 
HETATM 12267 C  C8  . NAG Y  2 .   ? -21.048 73.495 1.763   1.00 40.06 ? 2220 NAG R C8  1 
HETATM 12268 N  N2  . NAG Y  2 .   ? -23.230 73.130 0.772   1.00 39.60 ? 2220 NAG R N2  1 
HETATM 12269 O  O3  . NAG Y  2 .   ? -24.099 74.219 -1.773  1.00 41.95 ? 2220 NAG R O3  1 
HETATM 12270 O  O4  . NAG Y  2 .   ? -26.865 73.793 -2.364  1.00 44.07 ? 2220 NAG R O4  1 
HETATM 12271 O  O5  . NAG Y  2 .   ? -26.091 70.971 -0.125  1.00 41.81 ? 2220 NAG R O5  1 
HETATM 12272 O  O6  . NAG Y  2 .   ? -29.082 70.866 -0.627  1.00 42.74 ? 2220 NAG R O6  1 
HETATM 12273 O  O7  . NAG Y  2 .   ? -21.509 71.841 0.102   1.00 40.93 ? 2220 NAG R O7  1 
HETATM 12274 C  C1  . NAG Z  2 .   ? 5.298   77.754 14.266  1.00 23.97 ? 2229 NAG S C1  1 
HETATM 12275 C  C2  . NAG Z  2 .   ? 5.147   78.329 12.850  1.00 24.71 ? 2229 NAG S C2  1 
HETATM 12276 C  C3  . NAG Z  2 .   ? 6.493   78.890 12.418  1.00 27.02 ? 2229 NAG S C3  1 
HETATM 12277 C  C4  . NAG Z  2 .   ? 7.009   79.915 13.417  1.00 27.88 ? 2229 NAG S C4  1 
HETATM 12278 C  C5  . NAG Z  2 .   ? 6.969   79.370 14.852  1.00 27.89 ? 2229 NAG S C5  1 
HETATM 12279 C  C6  . NAG Z  2 .   ? 7.194   80.502 15.834  1.00 27.85 ? 2229 NAG S C6  1 
HETATM 12280 C  C7  . NAG Z  2 .   ? 3.521   77.230 11.450  1.00 25.05 ? 2229 NAG S C7  1 
HETATM 12281 C  C8  . NAG Z  2 .   ? 3.241   76.138 10.443  1.00 23.83 ? 2229 NAG S C8  1 
HETATM 12282 N  N2  . NAG Z  2 .   ? 4.767   77.304 11.904  1.00 23.77 ? 2229 NAG S N2  1 
HETATM 12283 O  O3  . NAG Z  2 .   ? 6.376   79.480 11.132  1.00 25.49 ? 2229 NAG S O3  1 
HETATM 12284 O  O4  . NAG Z  2 .   ? 8.373   80.206 13.093  1.00 32.87 ? 2229 NAG S O4  1 
HETATM 12285 O  O5  . NAG Z  2 .   ? 5.681   78.793 15.168  1.00 24.04 ? 2229 NAG S O5  1 
HETATM 12286 O  O6  . NAG Z  2 .   ? 7.708   80.019 17.060  1.00 30.47 ? 2229 NAG S O6  1 
HETATM 12287 O  O7  . NAG Z  2 .   ? 2.610   77.971 11.833  1.00 25.80 ? 2229 NAG S O7  1 
HETATM 12288 C  C1  . NAG AA 2 .   ? 8.678   81.509 12.733  1.00 36.86 ? 2230 NAG S C1  1 
HETATM 12289 C  C2  . NAG AA 2 .   ? 10.186  81.734 12.925  1.00 38.67 ? 2230 NAG S C2  1 
HETATM 12290 C  C3  . NAG AA 2 .   ? 10.596  83.106 12.362  1.00 39.75 ? 2230 NAG S C3  1 
HETATM 12291 C  C4  . NAG AA 2 .   ? 10.096  83.288 10.931  1.00 40.42 ? 2230 NAG S C4  1 
HETATM 12292 C  C5  . NAG AA 2 .   ? 8.592   83.001 10.858  1.00 40.76 ? 2230 NAG S C5  1 
HETATM 12293 C  C6  . NAG AA 2 .   ? 8.082   83.047 9.436   1.00 40.71 ? 2230 NAG S C6  1 
HETATM 12294 C  C7  . NAG AA 2 .   ? 10.943  80.524 14.887  1.00 40.23 ? 2230 NAG S C7  1 
HETATM 12295 C  C8  . NAG AA 2 .   ? 11.263  80.546 16.376  1.00 40.33 ? 2230 NAG S C8  1 
HETATM 12296 N  N2  . NAG AA 2 .   ? 10.510  81.661 14.341  1.00 39.14 ? 2230 NAG S N2  1 
HETATM 12297 O  O3  . NAG AA 2 .   ? 12.005  83.221 12.383  1.00 41.75 ? 2230 NAG S O3  1 
HETATM 12298 O  O4  . NAG AA 2 .   ? 10.364  84.612 10.487  1.00 41.67 ? 2230 NAG S O4  1 
HETATM 12299 O  O5  . NAG AA 2 .   ? 8.321   81.672 11.353  1.00 38.10 ? 2230 NAG S O5  1 
HETATM 12300 O  O6  . NAG AA 2 .   ? 8.624   81.969 8.686   1.00 44.08 ? 2230 NAG S O6  1 
HETATM 12301 O  O7  . NAG AA 2 .   ? 11.083  79.476 14.247  1.00 41.29 ? 2230 NAG S O7  1 
HETATM 12302 C  C1  . NAG BA 2 .   ? -2.142  73.761 -1.024  1.00 30.92 ? 2281 NAG T C1  1 
HETATM 12303 C  C2  . NAG BA 2 .   ? -0.671  73.671 -1.429  1.00 31.69 ? 2281 NAG T C2  1 
HETATM 12304 C  C3  . NAG BA 2 .   ? 0.253   74.028 -0.277  1.00 33.69 ? 2281 NAG T C3  1 
HETATM 12305 C  C4  . NAG BA 2 .   ? -0.146  75.396 0.243   1.00 36.01 ? 2281 NAG T C4  1 
HETATM 12306 C  C5  . NAG BA 2 .   ? -1.624  75.377 0.654   1.00 34.92 ? 2281 NAG T C5  1 
HETATM 12307 C  C6  . NAG BA 2 .   ? -2.134  76.697 1.197   1.00 35.01 ? 2281 NAG T C6  1 
HETATM 12308 C  C7  . NAG BA 2 .   ? -0.153  72.189 -3.220  1.00 30.48 ? 2281 NAG T C7  1 
HETATM 12309 C  C8  . NAG BA 2 .   ? 0.172   70.789 -3.719  1.00 29.24 ? 2281 NAG T C8  1 
HETATM 12310 N  N2  . NAG BA 2 .   ? -0.365  72.346 -1.922  1.00 30.62 ? 2281 NAG T N2  1 
HETATM 12311 O  O3  . NAG BA 2 .   ? 1.604   74.034 -0.715  1.00 33.96 ? 2281 NAG T O3  1 
HETATM 12312 O  O4  . NAG BA 2 .   ? 0.668   75.744 1.368   1.00 40.21 ? 2281 NAG T O4  1 
HETATM 12313 O  O5  . NAG BA 2 .   ? -2.430  75.058 -0.484  1.00 32.09 ? 2281 NAG T O5  1 
HETATM 12314 O  O6  . NAG BA 2 .   ? -1.649  77.786 0.429   1.00 37.27 ? 2281 NAG T O6  1 
HETATM 12315 O  O7  . NAG BA 2 .   ? -0.225  73.126 -4.012  1.00 29.42 ? 2281 NAG T O7  1 
HETATM 12316 C  C1  . NAG CA 2 .   ? 1.526   76.804 1.163   1.00 42.70 ? 2282 NAG T C1  1 
HETATM 12317 C  C2  . NAG CA 2 .   ? 1.961   77.347 2.510   1.00 43.77 ? 2282 NAG T C2  1 
HETATM 12318 C  C3  . NAG CA 2 .   ? 2.935   78.517 2.277   1.00 45.22 ? 2282 NAG T C3  1 
HETATM 12319 C  C4  . NAG CA 2 .   ? 4.117   78.025 1.404   1.00 45.42 ? 2282 NAG T C4  1 
HETATM 12320 C  C5  . NAG CA 2 .   ? 3.596   77.389 0.106   1.00 45.71 ? 2282 NAG T C5  1 
HETATM 12321 C  C6  . NAG CA 2 .   ? 4.682   76.821 -0.816  1.00 46.83 ? 2282 NAG T C6  1 
HETATM 12322 C  C7  . NAG CA 2 .   ? 0.227   76.868 4.128   1.00 44.63 ? 2282 NAG T C7  1 
HETATM 12323 C  C8  . NAG CA 2 .   ? -1.006  77.313 4.886   1.00 44.17 ? 2282 NAG T C8  1 
HETATM 12324 N  N2  . NAG CA 2 .   ? 0.788   77.737 3.281   1.00 44.24 ? 2282 NAG T N2  1 
HETATM 12325 O  O3  . NAG CA 2 .   ? 3.411   79.001 3.529   1.00 45.14 ? 2282 NAG T O3  1 
HETATM 12326 O  O4  . NAG CA 2 .   ? 4.981   79.100 1.097   1.00 46.55 ? 2282 NAG T O4  1 
HETATM 12327 O  O5  . NAG CA 2 .   ? 2.665   76.326 0.419   1.00 44.83 ? 2282 NAG T O5  1 
HETATM 12328 O  O6  . NAG CA 2 .   ? 4.984   75.454 -0.536  1.00 45.96 ? 2282 NAG T O6  1 
HETATM 12329 O  O7  . NAG CA 2 .   ? 0.681   75.736 4.329   1.00 45.44 ? 2282 NAG T O7  1 
HETATM 12330 O  O   . HOH DA 6 .   ? 35.491  59.905 40.165  1.00 35.89 ? 1523 HOH A O   1 
HETATM 12331 O  O   . HOH DA 6 .   ? 41.338  39.287 22.738  1.00 25.89 ? 1524 HOH A O   1 
HETATM 12332 O  O   . HOH DA 6 .   ? 37.252  60.163 31.673  1.00 13.29 ? 1525 HOH A O   1 
HETATM 12333 O  O   . HOH DA 6 .   ? 21.893  31.973 43.197  1.00 30.10 ? 1526 HOH A O   1 
HETATM 12334 O  O   . HOH DA 6 .   ? 29.261  51.764 31.209  1.00 12.44 ? 1527 HOH A O   1 
HETATM 12335 O  O   . HOH DA 6 .   ? 8.688   42.358 43.873  1.00 15.72 ? 1528 HOH A O   1 
HETATM 12336 O  O   . HOH DA 6 .   ? 23.659  31.866 47.198  1.00 19.07 ? 1529 HOH A O   1 
HETATM 12337 O  O   . HOH DA 6 .   ? 63.136  42.329 44.786  1.00 14.66 ? 1530 HOH A O   1 
HETATM 12338 O  O   . HOH DA 6 .   ? 56.607  54.024 44.927  1.00 19.27 ? 1531 HOH A O   1 
HETATM 12339 O  O   . HOH DA 6 .   ? 44.285  44.318 33.974  1.00 14.78 ? 1532 HOH A O   1 
HETATM 12340 O  O   . HOH DA 6 .   ? 24.503  57.096 34.014  1.00 12.87 ? 1533 HOH A O   1 
HETATM 12341 O  O   . HOH DA 6 .   ? 54.167  37.154 43.433  1.00 14.99 ? 1534 HOH A O   1 
HETATM 12342 O  O   . HOH DA 6 .   ? 49.612  41.167 30.229  1.00 21.95 ? 1535 HOH A O   1 
HETATM 12343 O  O   . HOH DA 6 .   ? 46.254  35.159 45.476  1.00 17.25 ? 1536 HOH A O   1 
HETATM 12344 O  O   . HOH DA 6 .   ? 32.149  58.709 37.691  1.00 17.26 ? 1537 HOH A O   1 
HETATM 12345 O  O   . HOH DA 6 .   ? 42.129  50.573 30.865  1.00 19.33 ? 1538 HOH A O   1 
HETATM 12346 O  O   . HOH DA 6 .   ? 51.604  39.032 35.725  1.00 14.18 ? 1539 HOH A O   1 
HETATM 12347 O  O   . HOH DA 6 .   ? 26.183  34.673 32.749  1.00 20.07 ? 1540 HOH A O   1 
HETATM 12348 O  O   . HOH DA 6 .   ? 38.396  63.743 29.261  1.00 14.47 ? 1541 HOH A O   1 
HETATM 12349 O  O   . HOH DA 6 .   ? 28.765  40.415 29.142  1.00 18.81 ? 1542 HOH A O   1 
HETATM 12350 O  O   . HOH DA 6 .   ? 64.703  69.887 24.886  1.00 23.03 ? 1543 HOH A O   1 
HETATM 12351 O  O   . HOH DA 6 .   ? 35.956  58.954 24.996  1.00 15.17 ? 1544 HOH A O   1 
HETATM 12352 O  O   . HOH DA 6 .   ? 58.450  49.627 33.081  1.00 12.98 ? 1545 HOH A O   1 
HETATM 12353 O  O   . HOH DA 6 .   ? 39.308  46.681 36.998  1.00 14.28 ? 1546 HOH A O   1 
HETATM 12354 O  O   . HOH DA 6 .   ? 27.157  54.991 40.465  1.00 13.50 ? 1547 HOH A O   1 
HETATM 12355 O  O   . HOH DA 6 .   ? 57.665  51.252 36.039  1.00 28.61 ? 1548 HOH A O   1 
HETATM 12356 O  O   . HOH DA 6 .   ? 60.002  47.200 57.317  1.00 14.93 ? 1549 HOH A O   1 
HETATM 12357 O  O   . HOH DA 6 .   ? 34.499  57.092 37.521  1.00 14.37 ? 1550 HOH A O   1 
HETATM 12358 O  O   . HOH DA 6 .   ? 49.034  37.539 38.865  1.00 18.97 ? 1551 HOH A O   1 
HETATM 12359 O  O   . HOH DA 6 .   ? 29.814  53.043 16.759  1.00 21.49 ? 1552 HOH A O   1 
HETATM 12360 O  O   . HOH DA 6 .   ? 43.942  66.785 12.752  1.00 35.18 ? 1553 HOH A O   1 
HETATM 12361 O  O   . HOH DA 6 .   ? 42.939  56.165 19.054  1.00 17.18 ? 1554 HOH A O   1 
HETATM 12362 O  O   . HOH DA 6 .   ? 38.263  40.224 45.306  1.00 14.47 ? 1555 HOH A O   1 
HETATM 12363 O  O   . HOH DA 6 .   ? 15.495  69.291 38.280  1.00 20.59 ? 1556 HOH A O   1 
HETATM 12364 O  O   . HOH DA 6 .   ? 48.403  60.197 63.992  1.00 16.98 ? 1557 HOH A O   1 
HETATM 12365 O  O   . HOH DA 6 .   ? 43.596  63.583 15.816  1.00 21.26 ? 1558 HOH A O   1 
HETATM 12366 O  O   . HOH DA 6 .   ? 47.100  38.143 46.302  1.00 19.25 ? 1559 HOH A O   1 
HETATM 12367 O  O   . HOH DA 6 .   ? 58.371  42.748 49.121  1.00 14.08 ? 1560 HOH A O   1 
HETATM 12368 O  O   . HOH DA 6 .   ? 21.800  62.287 37.326  1.00 14.94 ? 1561 HOH A O   1 
HETATM 12369 O  O   . HOH DA 6 .   ? 34.023  45.728 53.120  1.00 12.98 ? 1562 HOH A O   1 
HETATM 12370 O  O   . HOH DA 6 .   ? 63.770  60.858 63.669  1.00 14.92 ? 1563 HOH A O   1 
HETATM 12371 O  O   . HOH DA 6 .   ? 40.726  48.049 21.900  1.00 15.67 ? 1564 HOH A O   1 
HETATM 12372 O  O   . HOH DA 6 .   ? 34.928  62.547 25.607  1.00 17.76 ? 1565 HOH A O   1 
HETATM 12373 O  O   . HOH DA 6 .   ? 58.232  73.975 16.122  1.00 28.73 ? 1566 HOH A O   1 
HETATM 12374 O  O   . HOH DA 6 .   ? 55.335  67.696 30.698  1.00 26.49 ? 1567 HOH A O   1 
HETATM 12375 O  O   . HOH DA 6 .   ? 27.900  51.901 64.780  1.00 18.86 ? 1568 HOH A O   1 
HETATM 12376 O  O   . HOH DA 6 .   ? 65.511  58.332 38.207  1.00 25.20 ? 1569 HOH A O   1 
HETATM 12377 O  O   . HOH DA 6 .   ? 65.932  46.102 54.717  1.00 24.98 ? 1570 HOH A O   1 
HETATM 12378 O  O   . HOH DA 6 .   ? 59.920  52.088 57.988  1.00 18.98 ? 1571 HOH A O   1 
HETATM 12379 O  O   . HOH DA 6 .   ? 13.232  47.721 36.699  1.00 15.18 ? 1572 HOH A O   1 
HETATM 12380 O  O   . HOH DA 6 .   ? 20.635  59.838 34.763  1.00 18.57 ? 1573 HOH A O   1 
HETATM 12381 O  O   . HOH DA 6 .   ? 51.126  32.868 37.905  1.00 26.10 ? 1574 HOH A O   1 
HETATM 12382 O  O   . HOH DA 6 .   ? 18.733  48.942 53.907  1.00 19.37 ? 1575 HOH A O   1 
HETATM 12383 O  O   . HOH DA 6 .   ? 42.942  54.961 15.342  1.00 21.39 ? 1576 HOH A O   1 
HETATM 12384 O  O   . HOH DA 6 .   ? 56.463  40.977 49.845  1.00 15.64 ? 1577 HOH A O   1 
HETATM 12385 O  O   . HOH DA 6 .   ? 41.237  52.608 18.299  1.00 15.27 ? 1578 HOH A O   1 
HETATM 12386 O  O   . HOH DA 6 .   ? 39.714  57.513 41.525  1.00 22.92 ? 1579 HOH A O   1 
HETATM 12387 O  O   . HOH DA 6 .   ? 34.411  60.637 37.914  1.00 17.27 ? 1580 HOH A O   1 
HETATM 12388 O  O   . HOH DA 6 .   ? 49.828  33.001 44.007  1.00 24.28 ? 1581 HOH A O   1 
HETATM 12389 O  O   . HOH DA 6 .   ? 53.033  72.279 36.712  1.00 35.91 ? 1582 HOH A O   1 
HETATM 12390 O  O   . HOH DA 6 .   ? 34.288  58.019 55.522  1.00 17.52 ? 1583 HOH A O   1 
HETATM 12391 O  O   . HOH DA 6 .   ? 37.237  59.316 34.396  1.00 14.32 ? 1584 HOH A O   1 
HETATM 12392 O  O   . HOH DA 6 .   ? 35.072  48.419 53.577  1.00 16.83 ? 1585 HOH A O   1 
HETATM 12393 O  O   . HOH DA 6 .   ? 63.065  66.615 57.033  1.00 17.85 ? 1586 HOH A O   1 
HETATM 12394 O  O   . HOH DA 6 .   ? 38.794  65.084 38.287  1.00 16.38 ? 1587 HOH A O   1 
HETATM 12395 O  O   . HOH DA 6 .   ? 42.331  56.293 35.359  1.00 15.45 ? 1588 HOH A O   1 
HETATM 12396 O  O   . HOH DA 6 .   ? 36.887  52.799 15.192  1.00 18.21 ? 1589 HOH A O   1 
HETATM 12397 O  O   . HOH DA 6 .   ? 38.943  50.913 52.102  1.00 21.68 ? 1590 HOH A O   1 
HETATM 12398 O  O   . HOH DA 6 .   ? 14.515  67.883 30.225  1.00 14.00 ? 1591 HOH A O   1 
HETATM 12399 O  O   . HOH DA 6 .   ? 36.739  47.451 51.384  1.00 16.23 ? 1592 HOH A O   1 
HETATM 12400 O  O   . HOH DA 6 .   ? 46.581  84.178 35.297  1.00 30.40 ? 1593 HOH A O   1 
HETATM 12401 O  O   . HOH DA 6 .   ? 39.715  81.900 10.437  1.00 48.81 ? 1594 HOH A O   1 
HETATM 12402 O  O   . HOH DA 6 .   ? 51.607  67.985 31.552  1.00 34.54 ? 1595 HOH A O   1 
HETATM 12403 O  O   . HOH DA 6 .   ? 31.887  33.992 19.594  1.00 34.64 ? 1596 HOH A O   1 
HETATM 12404 O  O   . HOH DA 6 .   ? 33.880  56.220 46.202  1.00 30.01 ? 1597 HOH A O   1 
HETATM 12405 O  O   . HOH DA 6 .   ? 40.639  38.091 39.791  1.00 15.73 ? 1598 HOH A O   1 
HETATM 12406 O  O   . HOH DA 6 .   ? 79.880  51.777 38.612  1.00 31.90 ? 1599 HOH A O   1 
HETATM 12407 O  O   . HOH DA 6 .   ? 57.927  64.947 44.947  1.00 21.34 ? 1600 HOH A O   1 
HETATM 12408 O  O   . HOH DA 6 .   ? 63.314  37.378 34.496  1.00 19.16 ? 1601 HOH A O   1 
HETATM 12409 O  O   . HOH DA 6 .   ? 61.379  34.019 36.600  1.00 34.89 ? 1602 HOH A O   1 
HETATM 12410 O  O   . HOH DA 6 .   ? 68.969  39.997 39.797  1.00 20.26 ? 1603 HOH A O   1 
HETATM 12411 O  O   . HOH DA 6 .   ? 50.742  41.238 37.631  1.00 15.00 ? 1604 HOH A O   1 
HETATM 12412 O  O   . HOH DA 6 .   ? 24.823  31.834 53.762  1.00 18.48 ? 1605 HOH A O   1 
HETATM 12413 O  O   . HOH DA 6 .   ? 36.377  80.984 29.314  1.00 26.86 ? 1606 HOH A O   1 
HETATM 12414 O  O   . HOH DA 6 .   ? 30.545  32.316 36.135  1.00 25.77 ? 1607 HOH A O   1 
HETATM 12415 O  O   . HOH DA 6 .   ? 66.710  69.037 31.562  1.00 31.12 ? 1608 HOH A O   1 
HETATM 12416 O  O   . HOH DA 6 .   ? 56.236  34.933 45.360  1.00 18.98 ? 1609 HOH A O   1 
HETATM 12417 O  O   . HOH DA 6 .   ? 51.618  61.250 52.438  1.00 25.11 ? 1610 HOH A O   1 
HETATM 12418 O  O   . HOH DA 6 .   ? 52.246  64.789 59.434  1.00 27.02 ? 1611 HOH A O   1 
HETATM 12419 O  O   . HOH DA 6 .   ? 37.752  57.093 61.467  1.00 28.75 ? 1612 HOH A O   1 
HETATM 12420 O  O   . HOH DA 6 .   ? 42.894  70.255 35.053  1.00 18.52 ? 1613 HOH A O   1 
HETATM 12421 O  O   . HOH DA 6 .   ? 50.575  61.298 14.357  1.00 20.91 ? 1614 HOH A O   1 
HETATM 12422 O  O   . HOH DA 6 .   ? 39.500  46.208 54.452  1.00 18.21 ? 1615 HOH A O   1 
HETATM 12423 O  O   . HOH DA 6 .   ? 55.382  62.681 49.645  1.00 20.02 ? 1616 HOH A O   1 
HETATM 12424 O  O   . HOH DA 6 .   ? 16.834  43.788 31.151  1.00 25.72 ? 1617 HOH A O   1 
HETATM 12425 O  O   . HOH DA 6 .   ? 75.984  64.605 52.782  1.00 44.97 ? 1618 HOH A O   1 
HETATM 12426 O  O   . HOH DA 6 .   ? 28.521  62.840 37.011  1.00 15.15 ? 1619 HOH A O   1 
HETATM 12427 O  O   . HOH DA 6 .   ? 52.125  39.063 29.304  1.00 19.86 ? 1620 HOH A O   1 
HETATM 12428 O  O   . HOH DA 6 .   ? 36.577  49.818 39.466  1.00 19.48 ? 1621 HOH A O   1 
HETATM 12429 O  O   . HOH DA 6 .   ? 34.397  46.250 45.648  1.00 14.59 ? 1622 HOH A O   1 
HETATM 12430 O  O   . HOH DA 6 .   ? 17.246  48.108 51.504  1.00 29.67 ? 1623 HOH A O   1 
HETATM 12431 O  O   . HOH DA 6 .   ? 18.314  70.931 45.589  1.00 25.77 ? 1624 HOH A O   1 
HETATM 12432 O  O   . HOH DA 6 .   ? 40.467  54.663 16.189  1.00 21.60 ? 1625 HOH A O   1 
HETATM 12433 O  O   . HOH DA 6 .   ? 75.636  41.548 35.961  1.00 24.82 ? 1626 HOH A O   1 
HETATM 12434 O  O   . HOH DA 6 .   ? 38.722  76.085 43.839  1.00 38.52 ? 1627 HOH A O   1 
HETATM 12435 O  O   . HOH DA 6 .   ? 33.460  60.850 50.338  1.00 35.53 ? 1628 HOH A O   1 
HETATM 12436 O  O   . HOH DA 6 .   ? 23.869  26.921 51.900  1.00 21.30 ? 1629 HOH A O   1 
HETATM 12437 O  O   . HOH DA 6 .   ? 30.104  33.950 32.352  1.00 24.73 ? 1630 HOH A O   1 
HETATM 12438 O  O   . HOH DA 6 .   ? 46.848  37.121 23.360  1.00 26.98 ? 1631 HOH A O   1 
HETATM 12439 O  O   . HOH DA 6 .   ? 72.791  46.074 45.655  1.00 20.14 ? 1632 HOH A O   1 
HETATM 12440 O  O   . HOH DA 6 .   ? 63.728  39.991 49.700  1.00 17.87 ? 1633 HOH A O   1 
HETATM 12441 O  O   . HOH DA 6 .   ? 58.664  62.542 29.425  1.00 26.96 ? 1634 HOH A O   1 
HETATM 12442 O  O   . HOH DA 6 .   ? 47.734  45.853 47.217  1.00 20.23 ? 1635 HOH A O   1 
HETATM 12443 O  O   . HOH DA 6 .   ? 22.025  30.410 45.274  1.00 22.76 ? 1636 HOH A O   1 
HETATM 12444 O  O   . HOH DA 6 .   ? 50.392  38.241 50.462  1.00 15.71 ? 1637 HOH A O   1 
HETATM 12445 O  O   . HOH DA 6 .   ? 40.843  40.252 66.341  1.00 25.81 ? 1638 HOH A O   1 
HETATM 12446 O  O   . HOH DA 6 .   ? 17.455  33.547 34.498  1.00 30.78 ? 1639 HOH A O   1 
HETATM 12447 O  O   . HOH DA 6 .   ? 37.488  47.080 46.365  1.00 27.30 ? 1640 HOH A O   1 
HETATM 12448 O  O   . HOH DA 6 .   ? 53.770  50.428 46.692  1.00 13.78 ? 1641 HOH A O   1 
HETATM 12449 O  O   . HOH DA 6 .   ? 46.120  74.390 14.800  1.00 26.85 ? 1642 HOH A O   1 
HETATM 12450 O  O   . HOH DA 6 .   ? 49.114  57.812 56.204  1.00 27.42 ? 1643 HOH A O   1 
HETATM 12451 O  O   . HOH DA 6 .   ? 55.284  81.846 31.737  1.00 24.32 ? 1644 HOH A O   1 
HETATM 12452 O  O   . HOH DA 6 .   ? 67.550  45.831 23.474  1.00 24.76 ? 1645 HOH A O   1 
HETATM 12453 O  O   . HOH DA 6 .   ? 47.637  58.021 14.328  1.00 24.40 ? 1646 HOH A O   1 
HETATM 12454 O  O   . HOH DA 6 .   ? 61.108  81.558 29.986  1.00 29.96 ? 1647 HOH A O   1 
HETATM 12455 O  O   . HOH DA 6 .   ? 55.827  62.014 63.943  1.00 17.54 ? 1648 HOH A O   1 
HETATM 12456 O  O   . HOH DA 6 .   ? 16.920  36.586 32.529  1.00 25.98 ? 1649 HOH A O   1 
HETATM 12457 O  O   . HOH DA 6 .   ? 61.502  44.469 19.304  1.00 24.26 ? 1650 HOH A O   1 
HETATM 12458 O  O   . HOH DA 6 .   ? 52.798  52.419 51.034  1.00 26.95 ? 1651 HOH A O   1 
HETATM 12459 O  O   . HOH DA 6 .   ? 36.602  65.719 28.639  1.00 22.13 ? 1652 HOH A O   1 
HETATM 12460 O  O   . HOH DA 6 .   ? 37.199  38.862 47.554  1.00 17.33 ? 1653 HOH A O   1 
HETATM 12461 O  O   . HOH DA 6 .   ? 54.737  51.906 44.643  1.00 15.84 ? 1654 HOH A O   1 
HETATM 12462 O  O   . HOH DA 6 .   ? 34.819  59.244 35.712  1.00 12.09 ? 1655 HOH A O   1 
HETATM 12463 O  O   . HOH DA 6 .   ? 55.271  37.513 45.741  1.00 18.21 ? 1656 HOH A O   1 
HETATM 12464 O  O   . HOH DA 6 .   ? 18.798  58.234 47.052  1.00 13.67 ? 1657 HOH A O   1 
HETATM 12465 O  O   . HOH DA 6 .   ? 71.057  53.504 47.754  1.00 19.35 ? 1658 HOH A O   1 
HETATM 12466 O  O   . HOH DA 6 .   ? 71.828  53.797 34.509  1.00 17.07 ? 1659 HOH A O   1 
HETATM 12467 O  O   . HOH DA 6 .   ? 40.189  37.459 42.580  1.00 13.31 ? 1660 HOH A O   1 
HETATM 12468 O  O   . HOH DA 6 .   ? 31.273  62.319 19.049  1.00 27.08 ? 1661 HOH A O   1 
HETATM 12469 O  O   . HOH DA 6 .   ? 10.956  43.672 49.812  1.00 21.55 ? 1662 HOH A O   1 
HETATM 12470 O  O   . HOH DA 6 .   ? 37.858  75.731 28.502  1.00 21.95 ? 1663 HOH A O   1 
HETATM 12471 O  O   . HOH DA 6 .   ? 42.273  45.902 54.566  1.00 14.03 ? 1664 HOH A O   1 
HETATM 12472 O  O   . HOH DA 6 .   ? 37.361  27.414 41.781  1.00 34.17 ? 1665 HOH A O   1 
HETATM 12473 O  O   . HOH DA 6 .   ? 48.274  38.579 48.833  1.00 15.72 ? 1666 HOH A O   1 
HETATM 12474 O  O   . HOH DA 6 .   ? 41.227  45.068 37.998  1.00 16.17 ? 1667 HOH A O   1 
HETATM 12475 O  O   . HOH DA 6 .   ? 40.668  40.103 43.687  1.00 15.62 ? 1668 HOH A O   1 
HETATM 12476 O  O   . HOH DA 6 .   ? 27.633  54.630 64.805  1.00 32.21 ? 1669 HOH A O   1 
HETATM 12477 O  O   . HOH DA 6 .   ? 22.161  30.996 53.066  1.00 23.20 ? 1670 HOH A O   1 
HETATM 12478 O  O   . HOH DA 6 .   ? 52.536  53.651 29.482  1.00 34.11 ? 1671 HOH A O   1 
HETATM 12479 O  O   . HOH DA 6 .   ? 38.681  41.884 53.679  1.00 18.13 ? 1672 HOH A O   1 
HETATM 12480 O  O   . HOH DA 6 .   ? 72.604  51.635 32.919  1.00 14.49 ? 1673 HOH A O   1 
HETATM 12481 O  O   . HOH DA 6 .   ? 17.997  58.978 35.732  1.00 23.37 ? 1674 HOH A O   1 
HETATM 12482 O  O   . HOH DA 6 .   ? 66.651  38.864 40.746  1.00 17.37 ? 1675 HOH A O   1 
HETATM 12483 O  O   . HOH DA 6 .   ? 52.603  41.650 29.268  1.00 14.54 ? 1676 HOH A O   1 
HETATM 12484 O  O   . HOH DA 6 .   ? 72.350  56.595 33.676  1.00 31.82 ? 1677 HOH A O   1 
HETATM 12485 O  O   . HOH DA 6 .   ? 21.467  62.045 45.918  1.00 14.27 ? 1678 HOH A O   1 
HETATM 12486 O  O   . HOH DA 6 .   ? 52.894  35.210 29.880  1.00 23.65 ? 1679 HOH A O   1 
HETATM 12487 O  O   . HOH DA 6 .   ? 42.273  59.115 57.370  1.00 34.05 ? 1680 HOH A O   1 
HETATM 12488 O  O   . HOH DA 6 .   ? 45.074  72.103 35.448  1.00 24.90 ? 1681 HOH A O   1 
HETATM 12489 O  O   . HOH DA 6 .   ? 41.983  69.163 43.694  1.00 45.86 ? 1682 HOH A O   1 
HETATM 12490 O  O   . HOH DA 6 .   ? 73.948  57.155 30.624  1.00 19.30 ? 1683 HOH A O   1 
HETATM 12491 O  O   . HOH DA 6 .   ? 67.405  37.789 29.692  1.00 25.21 ? 1684 HOH A O   1 
HETATM 12492 O  O   . HOH DA 6 .   ? 36.356  52.709 39.603  1.00 24.32 ? 1685 HOH A O   1 
HETATM 12493 O  O   . HOH DA 6 .   ? 22.942  59.504 55.896  1.00 18.15 ? 1686 HOH A O   1 
HETATM 12494 O  O   . HOH DA 6 .   ? 55.799  56.870 16.031  1.00 22.30 ? 1687 HOH A O   1 
HETATM 12495 O  O   . HOH DA 6 .   ? 58.987  54.250 56.542  1.00 15.81 ? 1688 HOH A O   1 
HETATM 12496 O  O   . HOH DA 6 .   ? 37.697  78.866 44.564  1.00 25.72 ? 1689 HOH A O   1 
HETATM 12497 O  O   . HOH DA 6 .   ? 20.233  35.659 59.734  1.00 26.91 ? 1690 HOH A O   1 
HETATM 12498 O  O   . HOH DA 6 .   ? 36.200  76.312 36.574  1.00 29.06 ? 1691 HOH A O   1 
HETATM 12499 O  O   . HOH DA 6 .   ? 31.365  65.016 36.537  1.00 21.67 ? 1692 HOH A O   1 
HETATM 12500 O  O   . HOH DA 6 .   ? 41.112  78.343 22.426  1.00 32.12 ? 1693 HOH A O   1 
HETATM 12501 O  O   . HOH DA 6 .   ? 58.675  62.565 63.845  1.00 30.38 ? 1694 HOH A O   1 
HETATM 12502 O  O   . HOH DA 6 .   ? 49.734  59.132 13.156  1.00 28.48 ? 1695 HOH A O   1 
HETATM 12503 O  O   . HOH DA 6 .   ? 45.866  46.378 40.699  1.00 17.94 ? 1696 HOH A O   1 
HETATM 12504 O  O   . HOH DA 6 .   ? 37.805  44.449 53.303  1.00 18.53 ? 1697 HOH A O   1 
HETATM 12505 O  O   . HOH DA 6 .   ? 61.912  54.121 16.044  1.00 20.69 ? 1698 HOH A O   1 
HETATM 12506 O  O   . HOH DA 6 .   ? 46.164  88.851 50.383  1.00 47.19 ? 1699 HOH A O   1 
HETATM 12507 O  O   . HOH DA 6 .   ? 53.620  32.579 41.905  1.00 30.00 ? 1700 HOH A O   1 
HETATM 12508 O  O   . HOH DA 6 .   ? 22.964  55.513 31.961  1.00 15.34 ? 1701 HOH A O   1 
HETATM 12509 O  O   . HOH DA 6 .   ? 61.841  32.952 43.204  1.00 21.19 ? 1702 HOH A O   1 
HETATM 12510 O  O   . HOH DA 6 .   ? 34.755  51.565 53.153  1.00 23.03 ? 1703 HOH A O   1 
HETATM 12511 O  O   . HOH DA 6 .   ? 44.306  57.110 15.244  1.00 20.85 ? 1704 HOH A O   1 
HETATM 12512 O  O   . HOH DA 6 .   ? 15.906  50.401 49.381  1.00 15.80 ? 1705 HOH A O   1 
HETATM 12513 O  O   . HOH DA 6 .   ? 46.690  45.730 59.131  1.00 17.57 ? 1706 HOH A O   1 
HETATM 12514 O  O   . HOH DA 6 .   ? 50.715  30.370 39.645  1.00 20.29 ? 1707 HOH A O   1 
HETATM 12515 O  O   . HOH DA 6 .   ? 22.867  67.857 41.946  1.00 16.75 ? 1708 HOH A O   1 
HETATM 12516 O  O   . HOH DA 6 .   ? 61.950  63.973 42.204  1.00 28.55 ? 1709 HOH A O   1 
HETATM 12517 O  O   . HOH DA 6 .   ? 69.354  66.374 61.541  1.00 29.97 ? 1710 HOH A O   1 
HETATM 12518 O  O   . HOH DA 6 .   ? 27.434  25.323 45.603  1.00 23.73 ? 1711 HOH A O   1 
HETATM 12519 O  O   . HOH DA 6 .   ? 19.333  55.136 59.650  1.00 24.86 ? 1712 HOH A O   1 
HETATM 12520 O  O   . HOH DA 6 .   ? 77.525  57.661 26.363  1.00 20.44 ? 1713 HOH A O   1 
HETATM 12521 O  O   . HOH DA 6 .   ? 18.412  34.259 51.138  1.00 26.27 ? 1714 HOH A O   1 
HETATM 12522 O  O   . HOH DA 6 .   ? 65.095  47.453 18.030  1.00 54.84 ? 1715 HOH A O   1 
HETATM 12523 O  O   . HOH DA 6 .   ? 37.242  78.928 35.951  1.00 29.53 ? 1716 HOH A O   1 
HETATM 12524 O  O   . HOH DA 6 .   ? 63.397  56.649 35.940  1.00 41.09 ? 1717 HOH A O   1 
HETATM 12525 O  O   . HOH DA 6 .   ? 45.450  32.384 28.443  1.00 40.52 ? 1718 HOH A O   1 
HETATM 12526 O  O   . HOH DA 6 .   ? 30.001  51.062 15.101  1.00 30.50 ? 1719 HOH A O   1 
HETATM 12527 O  O   . HOH DA 6 .   ? 39.319  46.874 57.117  1.00 22.97 ? 1720 HOH A O   1 
HETATM 12528 O  O   . HOH DA 6 .   ? 56.084  29.494 35.648  1.00 31.29 ? 1721 HOH A O   1 
HETATM 12529 O  O   . HOH DA 6 .   ? 11.798  39.798 49.132  1.00 31.62 ? 1722 HOH A O   1 
HETATM 12530 O  O   . HOH DA 6 .   ? 75.401  46.901 45.711  1.00 32.24 ? 1723 HOH A O   1 
HETATM 12531 O  O   . HOH DA 6 .   ? 14.982  38.310 32.856  1.00 29.10 ? 1724 HOH A O   1 
HETATM 12532 O  O   . HOH DA 6 .   ? 44.874  65.385 34.652  1.00 24.54 ? 1725 HOH A O   1 
HETATM 12533 O  O   . HOH DA 6 .   ? 9.369   78.327 32.901  1.00 31.49 ? 1726 HOH A O   1 
HETATM 12534 O  O   . HOH DA 6 .   ? 31.259  62.292 36.926  1.00 15.65 ? 1727 HOH A O   1 
HETATM 12535 O  O   . HOH DA 6 .   ? 8.680   40.117 42.599  1.00 19.97 ? 1728 HOH A O   1 
HETATM 12536 O  O   . HOH DA 6 .   ? 30.143  61.358 43.636  1.00 37.08 ? 1729 HOH A O   1 
HETATM 12537 O  O   . HOH DA 6 .   ? 35.776  40.887 14.324  1.00 31.52 ? 1730 HOH A O   1 
HETATM 12538 O  O   . HOH DA 6 .   ? 42.094  53.885 55.440  1.00 19.36 ? 1731 HOH A O   1 
HETATM 12539 O  O   . HOH DA 6 .   ? 26.893  59.319 61.553  1.00 39.84 ? 1732 HOH A O   1 
HETATM 12540 O  O   . HOH DA 6 .   ? 36.324  54.940 52.675  1.00 31.60 ? 1733 HOH A O   1 
HETATM 12541 O  O   . HOH DA 6 .   ? 68.649  43.491 17.332  1.00 38.17 ? 1734 HOH A O   1 
HETATM 12542 O  O   . HOH DA 6 .   ? 72.966  60.350 49.036  1.00 29.72 ? 1735 HOH A O   1 
HETATM 12543 O  O   . HOH DA 6 .   ? 58.954  67.861 59.180  1.00 23.86 ? 1736 HOH A O   1 
HETATM 12544 O  O   . HOH DA 6 .   ? 62.063  79.541 31.728  1.00 31.40 ? 1737 HOH A O   1 
HETATM 12545 O  O   . HOH DA 6 .   ? 42.117  82.458 35.342  1.00 38.24 ? 1738 HOH A O   1 
HETATM 12546 O  O   . HOH DA 6 .   ? 41.640  42.975 67.633  1.00 27.19 ? 1739 HOH A O   1 
HETATM 12547 O  O   . HOH DA 6 .   ? 38.597  56.153 56.667  1.00 27.80 ? 1740 HOH A O   1 
HETATM 12548 O  O   . HOH DA 6 .   ? 40.410  47.288 59.647  1.00 32.28 ? 1741 HOH A O   1 
HETATM 12549 O  O   . HOH DA 6 .   ? 21.574  69.336 43.753  1.00 20.53 ? 1742 HOH A O   1 
HETATM 12550 O  O   . HOH DA 6 .   ? 21.665  40.528 23.076  1.00 25.24 ? 1743 HOH A O   1 
HETATM 12551 O  O   . HOH DA 6 .   ? 27.674  64.151 34.708  1.00 19.19 ? 1744 HOH A O   1 
HETATM 12552 O  O   . HOH DA 6 .   ? 75.897  55.418 29.489  1.00 27.49 ? 1745 HOH A O   1 
HETATM 12553 O  O   . HOH DA 6 .   ? 49.863  48.910 33.927  1.00 21.71 ? 1746 HOH A O   1 
HETATM 12554 O  O   . HOH DA 6 .   ? 35.869  68.931 24.886  1.00 26.26 ? 1747 HOH A O   1 
HETATM 12555 O  O   . HOH DA 6 .   ? 56.929  60.833 67.304  1.00 20.77 ? 1748 HOH A O   1 
HETATM 12556 O  O   . HOH DA 6 .   ? 25.330  31.976 44.946  1.00 21.65 ? 1749 HOH A O   1 
HETATM 12557 O  O   . HOH DA 6 .   ? 62.388  36.581 51.238  1.00 29.82 ? 1750 HOH A O   1 
HETATM 12558 O  O   . HOH DA 6 .   ? 72.886  43.540 30.531  1.00 25.10 ? 1751 HOH A O   1 
HETATM 12559 O  O   . HOH DA 6 .   ? 56.539  60.807 30.228  1.00 31.68 ? 1752 HOH A O   1 
HETATM 12560 O  O   . HOH DA 6 .   ? 17.864  72.152 31.774  1.00 20.94 ? 1753 HOH A O   1 
HETATM 12561 O  O   . HOH DA 6 .   ? 43.128  67.547 35.347  1.00 24.40 ? 1754 HOH A O   1 
HETATM 12562 O  O   . HOH DA 6 .   ? 60.499  51.689 62.613  1.00 33.43 ? 1755 HOH A O   1 
HETATM 12563 O  O   . HOH DA 6 .   ? 33.199  54.264 49.124  1.00 24.82 ? 1756 HOH A O   1 
HETATM 12564 O  O   . HOH DA 6 .   ? 49.395  62.336 30.176  1.00 25.44 ? 1757 HOH A O   1 
HETATM 12565 O  O   . HOH DA 6 .   ? 51.410  50.308 64.404  1.00 17.14 ? 1758 HOH A O   1 
HETATM 12566 O  O   . HOH DA 6 .   ? 62.615  59.001 40.884  1.00 32.45 ? 1759 HOH A O   1 
HETATM 12567 O  O   . HOH DA 6 .   ? 29.552  62.994 41.507  1.00 31.10 ? 1760 HOH A O   1 
HETATM 12568 O  O   . HOH DA 6 .   ? 59.831  57.092 32.702  1.00 41.28 ? 1761 HOH A O   1 
HETATM 12569 O  O   . HOH DA 6 .   ? 38.161  55.041 14.975  1.00 23.92 ? 1762 HOH A O   1 
HETATM 12570 O  O   . HOH DA 6 .   ? 38.359  35.508 42.385  1.00 18.20 ? 1763 HOH A O   1 
HETATM 12571 O  O   . HOH DA 6 .   ? 42.277  46.561 40.308  1.00 18.99 ? 1764 HOH A O   1 
HETATM 12572 O  O   . HOH DA 6 .   ? 34.896  54.995 69.033  1.00 32.01 ? 1765 HOH A O   1 
HETATM 12573 O  O   . HOH DA 6 .   ? 62.069  63.058 39.854  1.00 45.90 ? 1766 HOH A O   1 
HETATM 12574 O  O   . HOH DA 6 .   ? 42.335  46.332 69.985  1.00 34.77 ? 1767 HOH A O   1 
HETATM 12575 O  O   . HOH DA 6 .   ? 27.972  63.964 39.270  1.00 21.78 ? 1768 HOH A O   1 
HETATM 12576 O  O   . HOH DA 6 .   ? 52.268  52.360 65.904  1.00 27.28 ? 1769 HOH A O   1 
HETATM 12577 O  O   . HOH DA 6 .   ? 54.542  61.775 66.169  1.00 37.29 ? 1770 HOH A O   1 
HETATM 12578 O  O   . HOH DA 6 .   ? 28.274  66.507 34.106  1.00 36.10 ? 1771 HOH A O   1 
HETATM 12579 O  O   . HOH DA 6 .   ? 53.238  34.615 43.633  1.00 23.46 ? 1772 HOH A O   1 
HETATM 12580 O  O   . HOH DA 6 .   ? 40.824  48.423 12.761  1.00 26.31 ? 1773 HOH A O   1 
HETATM 12581 O  O   . HOH DA 6 .   ? 18.702  76.049 38.664  1.00 22.14 ? 1774 HOH A O   1 
HETATM 12582 O  O   . HOH DA 6 .   ? 44.347  50.513 38.566  1.00 29.90 ? 1775 HOH A O   1 
HETATM 12583 O  O   . HOH DA 6 .   ? 53.161  32.712 35.576  1.00 21.25 ? 1776 HOH A O   1 
HETATM 12584 O  O   . HOH DA 6 .   ? 50.377  58.836 51.779  1.00 32.38 ? 1777 HOH A O   1 
HETATM 12585 O  O   . HOH DA 6 .   ? 75.901  59.074 30.469  1.00 22.52 ? 1778 HOH A O   1 
HETATM 12586 O  O   . HOH DA 6 .   ? 42.994  62.038 13.998  1.00 24.70 ? 1779 HOH A O   1 
HETATM 12587 O  O   . HOH DA 6 .   ? 52.899  58.422 28.757  1.00 23.48 ? 1780 HOH A O   1 
HETATM 12588 O  O   . HOH DA 6 .   ? 28.173  27.159 60.148  1.00 31.07 ? 1781 HOH A O   1 
HETATM 12589 O  O   . HOH DA 6 .   ? 55.076  84.533 26.380  1.00 23.02 ? 1782 HOH A O   1 
HETATM 12590 O  O   . HOH DA 6 .   ? 27.954  41.998 26.137  1.00 18.40 ? 1783 HOH A O   1 
HETATM 12591 O  O   . HOH DA 6 .   ? 42.741  55.553 37.989  1.00 23.42 ? 1784 HOH A O   1 
HETATM 12592 O  O   . HOH DA 6 .   ? 55.162  42.086 28.834  1.00 22.92 ? 1785 HOH A O   1 
HETATM 12593 O  O   . HOH DA 6 .   ? 55.844  51.064 42.340  1.00 19.89 ? 1786 HOH A O   1 
HETATM 12594 O  O   . HOH DA 6 .   ? 70.412  45.184 26.823  1.00 16.75 ? 1787 HOH A O   1 
HETATM 12595 O  O   . HOH DA 6 .   ? 58.544  65.745 60.859  1.00 26.31 ? 1788 HOH A O   1 
HETATM 12596 O  O   . HOH DA 6 .   ? 50.875  40.848 57.398  1.00 26.65 ? 1789 HOH A O   1 
HETATM 12597 O  O   . HOH DA 6 .   ? 39.861  48.937 42.992  1.00 25.01 ? 1790 HOH A O   1 
HETATM 12598 O  O   . HOH DA 6 .   ? 67.227  52.118 10.862  1.00 38.70 ? 1791 HOH A O   1 
HETATM 12599 O  O   . HOH DA 6 .   ? 40.788  47.611 44.726  1.00 37.13 ? 1792 HOH A O   1 
HETATM 12600 O  O   . HOH DA 6 .   ? 33.070  33.632 22.350  1.00 26.34 ? 1793 HOH A O   1 
HETATM 12601 O  O   . HOH DA 6 .   ? 57.636  55.233 24.951  1.00 24.00 ? 1794 HOH A O   1 
HETATM 12602 O  O   . HOH DA 6 .   ? 72.360  62.695 43.645  1.00 38.15 ? 1795 HOH A O   1 
HETATM 12603 O  O   . HOH DA 6 .   ? 12.355  76.386 32.482  1.00 23.69 ? 1796 HOH A O   1 
HETATM 12604 O  O   . HOH DA 6 .   ? 44.258  60.346 56.120  1.00 45.06 ? 1797 HOH A O   1 
HETATM 12605 O  O   . HOH DA 6 .   ? 22.740  37.498 26.633  1.00 40.03 ? 1798 HOH A O   1 
HETATM 12606 O  O   . HOH DA 6 .   ? 30.564  66.734 49.193  1.00 27.30 ? 1799 HOH A O   1 
HETATM 12607 O  O   . HOH DA 6 .   ? 73.102  51.373 23.640  1.00 35.97 ? 1800 HOH A O   1 
HETATM 12608 O  O   . HOH DA 6 .   ? 41.755  61.412 64.716  1.00 31.02 ? 1801 HOH A O   1 
HETATM 12609 O  O   . HOH DA 6 .   ? 14.889  74.560 33.230  1.00 21.71 ? 1802 HOH A O   1 
HETATM 12610 O  O   . HOH DA 6 .   ? 44.754  54.546 10.878  1.00 49.86 ? 1803 HOH A O   1 
HETATM 12611 O  O   . HOH DA 6 .   ? 76.092  45.279 47.808  1.00 45.27 ? 1804 HOH A O   1 
HETATM 12612 O  O   . HOH DA 6 .   ? 44.698  82.013 26.119  1.00 32.54 ? 1805 HOH A O   1 
HETATM 12613 O  O   . HOH DA 6 .   ? 32.619  49.871 15.056  1.00 40.81 ? 1806 HOH A O   1 
HETATM 12614 O  O   . HOH DA 6 .   ? 20.111  69.442 28.217  1.00 37.50 ? 1807 HOH A O   1 
HETATM 12615 O  O   . HOH DA 6 .   ? 54.549  67.712 10.182  1.00 28.71 ? 1808 HOH A O   1 
HETATM 12616 O  O   . HOH DA 6 .   ? 46.577  62.229 36.547  1.00 31.11 ? 1809 HOH A O   1 
HETATM 12617 O  O   . HOH DA 6 .   ? 51.207  74.509 15.599  1.00 27.77 ? 1810 HOH A O   1 
HETATM 12618 O  O   . HOH DA 6 .   ? 62.845  57.736 31.213  1.00 23.85 ? 1811 HOH A O   1 
HETATM 12619 O  O   . HOH DA 6 .   ? 41.132  56.480 56.303  1.00 35.70 ? 1812 HOH A O   1 
HETATM 12620 O  O   . HOH DA 6 .   ? 65.711  57.480 15.616  1.00 25.66 ? 1813 HOH A O   1 
HETATM 12621 O  O   . HOH DA 6 .   ? 72.500  43.815 27.953  1.00 33.30 ? 1814 HOH A O   1 
HETATM 12622 O  O   . HOH DA 6 .   ? 45.685  61.368 63.728  1.00 24.94 ? 1815 HOH A O   1 
HETATM 12623 O  O   . HOH DA 6 .   ? 38.014  52.181 12.007  1.00 25.23 ? 1816 HOH A O   1 
HETATM 12624 O  O   . HOH DA 6 .   ? 27.541  52.492 17.778  1.00 30.99 ? 1817 HOH A O   1 
HETATM 12625 O  O   . HOH DA 6 .   ? 56.556  62.832 46.909  1.00 20.70 ? 1818 HOH A O   1 
HETATM 12626 O  O   . HOH DA 6 .   ? 61.533  52.495 60.378  1.00 24.16 ? 1819 HOH A O   1 
HETATM 12627 O  O   . HOH DA 6 .   ? 60.331  58.912 43.084  1.00 21.73 ? 1820 HOH A O   1 
HETATM 12628 O  O   . HOH DA 6 .   ? 64.547  35.566 32.966  1.00 30.87 ? 1821 HOH A O   1 
HETATM 12629 O  O   . HOH DA 6 .   ? 50.498  71.035 36.306  1.00 28.22 ? 1822 HOH A O   1 
HETATM 12630 O  O   . HOH DA 6 .   ? 21.367  56.697 30.101  1.00 18.17 ? 1823 HOH A O   1 
HETATM 12631 O  O   . HOH DA 6 .   ? 49.236  77.367 15.010  1.00 57.48 ? 1824 HOH A O   1 
HETATM 12632 O  O   . HOH DA 6 .   ? 18.627  28.749 35.628  1.00 52.29 ? 1825 HOH A O   1 
HETATM 12633 O  O   . HOH DA 6 .   ? 67.623  53.517 55.946  1.00 16.92 ? 1826 HOH A O   1 
HETATM 12634 O  O   . HOH DA 6 .   ? 25.341  59.227 19.548  1.00 28.10 ? 1827 HOH A O   1 
HETATM 12635 O  O   . HOH DA 6 .   ? 43.148  49.144 69.712  1.00 33.63 ? 1828 HOH A O   1 
HETATM 12636 O  O   . HOH DA 6 .   ? 46.521  54.734 36.708  1.00 33.43 ? 1829 HOH A O   1 
HETATM 12637 O  O   . HOH DA 6 .   ? 44.591  41.991 24.517  1.00 32.38 ? 1830 HOH A O   1 
HETATM 12638 O  O   . HOH DA 6 .   ? 42.524  48.009 47.397  1.00 27.75 ? 1831 HOH A O   1 
HETATM 12639 O  O   . HOH DA 6 .   ? 41.848  46.057 43.251  1.00 20.86 ? 1832 HOH A O   1 
HETATM 12640 O  O   . HOH DA 6 .   ? 34.412  46.584 48.224  1.00 29.32 ? 1833 HOH A O   1 
HETATM 12641 O  O   . HOH DA 6 .   ? 51.684  33.203 45.796  1.00 27.16 ? 1834 HOH A O   1 
HETATM 12642 O  O   . HOH DA 6 .   ? 15.025  76.342 35.646  1.00 22.85 ? 1835 HOH A O   1 
HETATM 12643 O  O   . HOH DA 6 .   ? 45.762  71.837 15.309  1.00 29.51 ? 1836 HOH A O   1 
HETATM 12644 O  O   . HOH DA 6 .   ? 42.272  43.193 22.448  1.00 28.45 ? 1837 HOH A O   1 
HETATM 12645 O  O   . HOH DA 6 .   ? 57.523  57.731 31.029  1.00 49.87 ? 1838 HOH A O   1 
HETATM 12646 O  O   . HOH DA 6 .   ? 37.372  50.485 42.046  1.00 28.67 ? 1839 HOH A O   1 
HETATM 12647 O  O   . HOH DA 6 .   ? 56.784  40.526 22.971  1.00 23.27 ? 1840 HOH A O   1 
HETATM 12648 O  O   . HOH DA 6 .   ? 59.501  60.604 65.833  1.00 31.75 ? 1841 HOH A O   1 
HETATM 12649 O  O   . HOH DA 6 .   ? 34.882  64.396 27.941  1.00 29.70 ? 1842 HOH A O   1 
HETATM 12650 O  O   . HOH DA 6 .   ? 60.689  65.989 30.532  1.00 35.37 ? 1843 HOH A O   1 
HETATM 12651 O  O   . HOH DA 6 .   ? 35.823  48.961 49.098  1.00 36.39 ? 1844 HOH A O   1 
HETATM 12652 O  O   . HOH DA 6 .   ? 44.536  46.249 43.283  1.00 30.06 ? 1845 HOH A O   1 
HETATM 12653 O  O   . HOH DA 6 .   ? 24.310  56.761 59.960  1.00 29.92 ? 1846 HOH A O   1 
HETATM 12654 O  O   . HOH DA 6 .   ? 76.662  49.517 39.167  1.00 22.97 ? 1847 HOH A O   1 
HETATM 12655 O  O   . HOH DA 6 .   ? 61.587  33.891 49.801  1.00 39.52 ? 1848 HOH A O   1 
HETATM 12656 O  O   . HOH DA 6 .   ? 26.851  67.654 28.146  1.00 24.24 ? 1849 HOH A O   1 
HETATM 12657 O  O   . HOH DA 6 .   ? 60.191  72.190 14.974  1.00 34.92 ? 1850 HOH A O   1 
HETATM 12658 O  O   . HOH DA 6 .   ? 52.652  55.009 66.130  1.00 31.87 ? 1851 HOH A O   1 
HETATM 12659 O  O   . HOH DA 6 .   ? 59.005  43.820 55.973  1.00 21.88 ? 1852 HOH A O   1 
HETATM 12660 O  O   . HOH DA 6 .   ? 18.224  62.856 29.482  1.00 23.61 ? 1853 HOH A O   1 
HETATM 12661 O  O   . HOH DA 6 .   ? 62.736  67.652 59.420  1.00 34.86 ? 1854 HOH A O   1 
HETATM 12662 O  O   . HOH DA 6 .   ? 34.746  71.327 34.721  1.00 40.24 ? 1855 HOH A O   1 
HETATM 12663 O  O   . HOH DA 6 .   ? 44.239  62.701 38.976  1.00 31.46 ? 1856 HOH A O   1 
HETATM 12664 O  O   . HOH DA 6 .   ? 47.513  52.687 55.868  1.00 28.20 ? 1857 HOH A O   1 
HETATM 12665 O  O   . HOH DA 6 .   ? 63.751  68.064 33.413  1.00 40.83 ? 1858 HOH A O   1 
HETATM 12666 O  O   . HOH DA 6 .   ? 69.150  62.981 19.321  1.00 34.88 ? 1859 HOH A O   1 
HETATM 12667 O  O   . HOH DA 6 .   ? 64.901  45.000 62.098  1.00 42.10 ? 1860 HOH A O   1 
HETATM 12668 O  O   . HOH DA 6 .   ? 63.177  35.192 46.452  1.00 29.46 ? 1861 HOH A O   1 
HETATM 12669 O  O   . HOH DA 6 .   ? 8.489   37.823 44.278  1.00 24.93 ? 1862 HOH A O   1 
HETATM 12670 O  O   . HOH DA 6 .   ? 38.310  61.765 40.825  1.00 22.40 ? 1863 HOH A O   1 
HETATM 12671 O  O   . HOH DA 6 .   ? 55.784  89.197 36.635  1.00 38.84 ? 1864 HOH A O   1 
HETATM 12672 O  O   . HOH DA 6 .   ? 16.427  39.697 46.372  1.00 21.53 ? 1865 HOH A O   1 
HETATM 12673 O  O   . HOH DA 6 .   ? 72.617  47.284 33.458  1.00 22.44 ? 1866 HOH A O   1 
HETATM 12674 O  O   . HOH DA 6 .   ? 34.495  66.568 25.879  1.00 18.68 ? 1867 HOH A O   1 
HETATM 12675 O  O   . HOH DA 6 .   ? 76.265  58.331 54.245  1.00 33.59 ? 1868 HOH A O   1 
HETATM 12676 O  O   . HOH DA 6 .   ? 67.590  52.909 58.796  1.00 23.49 ? 1869 HOH A O   1 
HETATM 12677 O  O   . HOH DA 6 .   ? 50.393  48.750 36.693  1.00 26.02 ? 1870 HOH A O   1 
HETATM 12678 O  O   . HOH DA 6 .   ? 68.500  73.969 52.311  1.00 23.44 ? 1871 HOH A O   1 
HETATM 12679 O  O   . HOH DA 6 .   ? 62.824  34.794 30.455  1.00 36.83 ? 1872 HOH A O   1 
HETATM 12680 O  O   . HOH DA 6 .   ? 37.286  68.171 27.712  1.00 28.81 ? 1873 HOH A O   1 
HETATM 12681 O  O   . HOH DA 6 .   ? 44.072  48.350 40.217  1.00 17.40 ? 1874 HOH A O   1 
HETATM 12682 O  O   . HOH DA 6 .   ? 53.158  35.984 26.096  1.00 38.48 ? 1875 HOH A O   1 
HETATM 12683 O  O   . HOH DA 6 .   ? 48.653  53.591 28.078  1.00 26.34 ? 1876 HOH A O   1 
HETATM 12684 O  O   . HOH DA 6 .   ? 67.100  52.077 53.724  1.00 21.36 ? 1877 HOH A O   1 
HETATM 12685 O  O   . HOH DA 6 .   ? 57.371  55.047 12.310  1.00 34.92 ? 1878 HOH A O   1 
HETATM 12686 O  O   . HOH DA 6 .   ? 75.403  52.191 34.196  1.00 24.93 ? 1879 HOH A O   1 
HETATM 12687 O  O   . HOH DA 6 .   ? 58.414  47.617 23.656  1.00 29.94 ? 1880 HOH A O   1 
HETATM 12688 O  O   . HOH DA 6 .   ? 32.963  43.822 69.228  1.00 30.33 ? 1881 HOH A O   1 
HETATM 12689 O  O   . HOH DA 6 .   ? 78.851  55.032 37.365  1.00 22.48 ? 1882 HOH A O   1 
HETATM 12690 O  O   . HOH DA 6 .   ? 45.905  48.895 26.971  1.00 22.88 ? 1883 HOH A O   1 
HETATM 12691 O  O   . HOH DA 6 .   ? 16.829  69.523 28.734  1.00 33.41 ? 1884 HOH A O   1 
HETATM 12692 O  O   . HOH DA 6 .   ? 46.067  49.123 14.037  1.00 30.18 ? 1885 HOH A O   1 
HETATM 12693 O  O   . HOH DA 6 .   ? 24.592  36.300 29.808  1.00 34.20 ? 1886 HOH A O   1 
HETATM 12694 O  O   . HOH DA 6 .   ? 15.914  70.023 47.337  1.00 28.45 ? 1887 HOH A O   1 
HETATM 12695 O  O   . HOH DA 6 .   ? 58.113  41.318 25.204  1.00 24.12 ? 1888 HOH A O   1 
HETATM 12696 O  O   . HOH DA 6 .   ? 31.973  64.177 40.459  1.00 31.20 ? 1889 HOH A O   1 
HETATM 12697 O  O   . HOH DA 6 .   ? 14.487  36.900 45.586  1.00 27.45 ? 1890 HOH A O   1 
HETATM 12698 O  O   . HOH DA 6 .   ? 44.258  70.374 41.956  1.00 47.34 ? 1891 HOH A O   1 
HETATM 12699 O  O   . HOH DA 6 .   ? 33.518  37.139 69.488  1.00 35.89 ? 1892 HOH A O   1 
HETATM 12700 O  O   . HOH DA 6 .   ? 73.107  54.170 28.021  1.00 19.50 ? 1893 HOH A O   1 
HETATM 12701 O  O   . HOH DA 6 .   ? 11.459  72.816 48.327  1.00 22.45 ? 1894 HOH A O   1 
HETATM 12702 O  O   . HOH DA 6 .   ? 33.038  27.507 42.441  1.00 25.86 ? 1895 HOH A O   1 
HETATM 12703 O  O   . HOH DA 6 .   ? 22.761  31.575 62.244  1.00 36.24 ? 1896 HOH A O   1 
HETATM 12704 O  O   . HOH DA 6 .   ? 9.557   45.406 33.146  1.00 33.32 ? 1897 HOH A O   1 
HETATM 12705 O  O   . HOH DA 6 .   ? 46.705  65.309 65.819  1.00 43.23 ? 1898 HOH A O   1 
HETATM 12706 O  O   . HOH DA 6 .   ? 54.638  57.581 30.545  1.00 38.68 ? 1899 HOH A O   1 
HETATM 12707 O  O   . HOH DA 6 .   ? 57.270  52.483 25.083  1.00 27.02 ? 1900 HOH A O   1 
HETATM 12708 O  O   . HOH DA 6 .   ? 29.111  31.155 38.323  1.00 28.98 ? 1901 HOH A O   1 
HETATM 12709 O  O   . HOH DA 6 .   ? 59.551  74.181 42.762  1.00 29.65 ? 1902 HOH A O   1 
HETATM 12710 O  O   . HOH DA 6 .   ? 27.240  68.774 36.133  1.00 52.74 ? 1903 HOH A O   1 
HETATM 12711 O  O   . HOH DA 6 .   ? 24.021  64.049 44.224  1.00 22.84 ? 1904 HOH A O   1 
HETATM 12712 O  O   . HOH DA 6 .   ? 17.413  77.060 36.736  1.00 27.22 ? 1905 HOH A O   1 
HETATM 12713 O  O   . HOH DA 6 .   ? 69.074  42.050 19.471  1.00 35.22 ? 1906 HOH A O   1 
HETATM 12714 O  O   . HOH DA 6 .   ? 22.055  58.161 60.242  1.00 28.37 ? 1907 HOH A O   1 
HETATM 12715 O  O   . HOH DA 6 .   ? 56.310  48.462 12.673  1.00 36.18 ? 1908 HOH A O   1 
HETATM 12716 O  O   . HOH DA 6 .   ? 20.459  32.962 58.525  1.00 30.89 ? 1909 HOH A O   1 
HETATM 12717 O  O   . HOH DA 6 .   ? 45.594  51.376 29.136  1.00 21.05 ? 1910 HOH A O   1 
HETATM 12718 O  O   . HOH DA 6 .   ? 70.598  67.363 29.267  1.00 32.12 ? 1911 HOH A O   1 
HETATM 12719 O  O   . HOH DA 6 .   ? 52.276  47.516 32.635  1.00 30.23 ? 1912 HOH A O   1 
HETATM 12720 O  O   . HOH DA 6 .   ? 20.855  74.450 38.465  1.00 27.18 ? 1913 HOH A O   1 
HETATM 12721 O  O   . HOH DA 6 .   ? 44.384  53.309 54.458  1.00 26.59 ? 1914 HOH A O   1 
HETATM 12722 O  O   . HOH DA 6 .   ? 24.753  66.336 43.525  1.00 27.95 ? 1915 HOH A O   1 
HETATM 12723 O  O   . HOH DA 6 .   ? 58.980  56.719 43.005  1.00 27.52 ? 1916 HOH A O   1 
HETATM 12724 O  O   . HOH DA 6 .   ? 30.176  26.742 42.098  1.00 40.34 ? 1917 HOH A O   1 
HETATM 12725 O  O   . HOH DA 6 .   ? 21.511  34.921 27.018  1.00 51.06 ? 1918 HOH A O   1 
HETATM 12726 O  O   . HOH DA 6 .   ? 52.872  53.481 44.257  1.00 31.84 ? 1919 HOH A O   1 
HETATM 12727 O  O   . HOH DA 6 .   ? 43.331  65.345 38.437  1.00 27.72 ? 1920 HOH A O   1 
HETATM 12728 O  O   . HOH DA 6 .   ? 48.835  47.632 43.639  1.00 37.61 ? 1921 HOH A O   1 
HETATM 12729 O  O   . HOH DA 6 .   ? 62.886  71.603 60.790  1.00 33.78 ? 1922 HOH A O   1 
HETATM 12730 O  O   . HOH DA 6 .   ? 17.366  46.703 55.161  1.00 27.59 ? 1923 HOH A O   1 
HETATM 12731 O  O   . HOH DA 6 .   ? 34.227  53.715 45.541  1.00 40.77 ? 1924 HOH A O   1 
HETATM 12732 O  O   . HOH DA 6 .   ? 40.308  42.869 20.109  1.00 28.62 ? 1925 HOH A O   1 
HETATM 12733 O  O   . HOH DA 6 .   ? 35.616  55.669 50.206  1.00 41.00 ? 1926 HOH A O   1 
HETATM 12734 O  O   . HOH DA 6 .   ? 47.372  44.509 56.961  1.00 25.55 ? 1927 HOH A O   1 
HETATM 12735 O  O   . HOH DA 6 .   ? 51.248  31.106 42.195  1.00 25.01 ? 1928 HOH A O   1 
HETATM 12736 O  O   . HOH DA 6 .   ? 23.085  37.044 22.006  1.00 30.29 ? 1929 HOH A O   1 
HETATM 12737 O  O   . HOH DA 6 .   ? 64.639  75.448 37.059  1.00 29.43 ? 1930 HOH A O   1 
HETATM 12738 O  O   . HOH DA 6 .   ? 36.188  32.576 22.116  1.00 43.23 ? 1931 HOH A O   1 
HETATM 12739 O  O   . HOH DA 6 .   ? 39.300  59.715 58.827  1.00 44.43 ? 1932 HOH A O   1 
HETATM 12740 O  O   . HOH DA 6 .   ? 73.905  58.466 37.841  1.00 24.72 ? 1933 HOH A O   1 
HETATM 12741 O  O   . HOH DA 6 .   ? 35.417  57.546 39.990  1.00 20.39 ? 1934 HOH A O   1 
HETATM 12742 O  O   . HOH DA 6 .   ? 24.197  57.430 21.678  1.00 27.11 ? 1935 HOH A O   1 
HETATM 12743 O  O   . HOH DA 6 .   ? 16.314  38.257 55.828  1.00 49.91 ? 1936 HOH A O   1 
HETATM 12744 O  O   . HOH DA 6 .   ? 33.774  70.043 41.614  1.00 31.87 ? 1937 HOH A O   1 
HETATM 12745 O  O   . HOH DA 6 .   ? 62.724  73.152 15.915  1.00 31.35 ? 1938 HOH A O   1 
HETATM 12746 O  O   . HOH DA 6 .   ? 66.250  39.616 43.811  1.00 37.87 ? 1939 HOH A O   1 
HETATM 12747 O  O   . HOH DA 6 .   ? 53.455  54.841 68.597  1.00 28.85 ? 1940 HOH A O   1 
HETATM 12748 O  O   . HOH DA 6 .   ? 34.105  57.861 48.977  1.00 40.49 ? 1941 HOH A O   1 
HETATM 12749 O  O   . HOH DA 6 .   ? 10.924  44.249 29.331  1.00 45.22 ? 1942 HOH A O   1 
HETATM 12750 O  O   . HOH DA 6 .   ? 63.243  75.870 27.849  1.00 37.70 ? 1943 HOH A O   1 
HETATM 12751 O  O   . HOH DA 6 .   ? 69.762  47.962 53.352  1.00 38.69 ? 1944 HOH A O   1 
HETATM 12752 O  O   . HOH DA 6 .   ? 59.788  81.353 21.500  1.00 33.37 ? 1945 HOH A O   1 
HETATM 12753 O  O   . HOH DA 6 .   ? 55.513  42.435 26.415  1.00 41.78 ? 1946 HOH A O   1 
HETATM 12754 O  O   . HOH DA 6 .   ? 55.058  44.336 30.712  1.00 26.65 ? 1947 HOH A O   1 
HETATM 12755 O  O   . HOH DA 6 .   ? 50.722  64.719 29.825  1.00 33.19 ? 1948 HOH A O   1 
HETATM 12756 O  O   . HOH DA 6 .   ? 42.871  64.590 9.809   1.00 42.93 ? 1949 HOH A O   1 
HETATM 12757 O  O   . HOH DA 6 .   ? 43.571  57.599 12.408  1.00 31.24 ? 1950 HOH A O   1 
HETATM 12758 O  O   . HOH DA 6 .   ? 64.894  80.562 35.804  1.00 30.92 ? 1951 HOH A O   1 
HETATM 12759 O  O   . HOH DA 6 .   ? 54.573  30.999 30.704  1.00 41.02 ? 1952 HOH A O   1 
HETATM 12760 O  O   . HOH DA 6 .   ? 38.424  79.598 21.768  1.00 48.72 ? 1953 HOH A O   1 
HETATM 12761 O  O   . HOH DA 6 .   ? 41.214  41.843 70.162  1.00 29.22 ? 1954 HOH A O   1 
HETATM 12762 O  O   . HOH DA 6 .   ? 12.824  79.307 32.736  1.00 43.86 ? 1955 HOH A O   1 
HETATM 12763 O  O   . HOH DA 6 .   ? 43.323  83.537 19.311  1.00 34.64 ? 1956 HOH A O   1 
HETATM 12764 O  O   . HOH DA 6 .   ? 48.978  47.917 38.575  1.00 27.41 ? 1957 HOH A O   1 
HETATM 12765 O  O   . HOH DA 6 .   ? 68.941  43.006 51.245  1.00 24.45 ? 1958 HOH A O   1 
HETATM 12766 O  O   . HOH DA 6 .   ? 14.609  48.455 50.137  1.00 21.41 ? 1959 HOH A O   1 
HETATM 12767 O  O   . HOH DA 6 .   ? 73.677  57.365 53.326  1.00 25.52 ? 1960 HOH A O   1 
HETATM 12768 O  O   . HOH DA 6 .   ? 53.962  45.153 33.088  1.00 16.63 ? 1961 HOH A O   1 
HETATM 12769 O  O   . HOH DA 6 .   ? 62.710  45.237 21.414  1.00 24.92 ? 1962 HOH A O   1 
HETATM 12770 O  O   . HOH DA 6 .   ? 57.146  58.057 11.820  1.00 32.77 ? 1963 HOH A O   1 
HETATM 12771 O  O   . HOH DA 6 .   ? 54.463  73.024 43.876  1.00 26.41 ? 1964 HOH A O   1 
HETATM 12772 O  O   . HOH DA 6 .   ? 46.179  61.467 70.374  1.00 28.86 ? 1965 HOH A O   1 
HETATM 12773 O  O   . HOH DA 6 .   ? 64.720  60.508 41.063  1.00 38.65 ? 1966 HOH A O   1 
HETATM 12774 O  O   . HOH DA 6 .   ? 24.735  69.867 40.995  1.00 30.77 ? 1967 HOH A O   1 
HETATM 12775 O  O   . HOH DA 6 .   ? 31.636  56.580 48.895  1.00 23.91 ? 1968 HOH A O   1 
HETATM 12776 O  O   . HOH DA 6 .   ? 57.489  65.267 29.647  1.00 31.06 ? 1969 HOH A O   1 
HETATM 12777 O  O   . HOH DA 6 .   ? 35.924  48.767 44.618  1.00 40.35 ? 1970 HOH A O   1 
HETATM 12778 O  O   . HOH DA 6 .   ? 41.879  44.838 50.343  1.00 27.95 ? 1971 HOH A O   1 
HETATM 12779 O  O   . HOH DA 6 .   ? 68.408  49.710 54.785  1.00 27.42 ? 1972 HOH A O   1 
HETATM 12780 O  O   . HOH DA 6 .   ? 11.908  36.848 45.145  1.00 27.00 ? 1973 HOH A O   1 
HETATM 12781 O  O   . HOH DA 6 .   ? 39.432  82.677 21.129  1.00 38.73 ? 1974 HOH A O   1 
HETATM 12782 O  O   . HOH DA 6 .   ? 60.262  43.117 24.662  1.00 35.39 ? 1975 HOH A O   1 
HETATM 12783 O  O   . HOH DA 6 .   ? 51.459  60.371 29.907  1.00 27.99 ? 1976 HOH A O   1 
HETATM 12784 O  O   . HOH DA 6 .   ? 46.394  84.321 19.219  1.00 41.14 ? 1977 HOH A O   1 
HETATM 12785 O  O   . HOH DA 6 .   ? 64.540  80.483 32.972  1.00 38.66 ? 1978 HOH A O   1 
HETATM 12786 O  O   . HOH DA 6 .   ? 66.322  59.141 35.877  1.00 38.73 ? 1979 HOH A O   1 
HETATM 12787 O  O   . HOH DA 6 .   ? 51.628  51.767 47.198  1.00 25.77 ? 1980 HOH A O   1 
HETATM 12788 O  O   . HOH DA 6 .   ? 13.781  72.538 50.068  1.00 33.94 ? 1981 HOH A O   1 
HETATM 12789 O  O   . HOH DA 6 .   ? 47.117  46.325 26.977  1.00 29.66 ? 1982 HOH A O   1 
HETATM 12790 O  O   . HOH DA 6 .   ? 61.283  83.391 21.762  1.00 39.12 ? 1983 HOH A O   1 
HETATM 12791 O  O   . HOH DA 6 .   ? 43.708  52.898 39.655  1.00 36.51 ? 1984 HOH A O   1 
HETATM 12792 O  O   . HOH DA 6 .   ? 24.562  50.413 61.587  1.00 28.03 ? 1985 HOH A O   1 
HETATM 12793 O  O   . HOH DA 6 .   ? 69.953  62.834 22.451  1.00 34.28 ? 1986 HOH A O   1 
HETATM 12794 O  O   . HOH DA 6 .   ? 24.078  71.353 38.864  1.00 37.32 ? 1987 HOH A O   1 
HETATM 12795 O  O   . HOH DA 6 .   ? 51.048  65.986 54.468  1.00 28.46 ? 1988 HOH A O   1 
HETATM 12796 O  O   . HOH DA 6 .   ? 43.668  45.887 48.314  1.00 21.93 ? 1989 HOH A O   1 
HETATM 12797 O  O   . HOH DA 6 .   ? 66.841  73.402 46.363  1.00 30.89 ? 1990 HOH A O   1 
HETATM 12798 O  O   . HOH DA 6 .   ? 46.162  46.799 45.268  1.00 28.36 ? 1991 HOH A O   1 
HETATM 12799 O  O   . HOH DA 6 .   ? 66.256  77.166 50.749  1.00 31.45 ? 1992 HOH A O   1 
HETATM 12800 O  O   . HOH DA 6 .   ? 43.786  49.472 42.533  1.00 35.70 ? 1993 HOH A O   1 
HETATM 12801 O  O   . HOH DA 6 .   ? 15.291  40.730 48.816  1.00 40.73 ? 1994 HOH A O   1 
HETATM 12802 O  O   . HOH DA 6 .   ? 52.865  42.353 61.810  1.00 35.24 ? 1995 HOH A O   1 
HETATM 12803 O  O   . HOH DA 6 .   ? 55.015  46.037 28.660  1.00 34.11 ? 1996 HOH A O   1 
HETATM 12804 O  O   . HOH DA 6 .   ? 43.026  46.951 57.350  1.00 35.96 ? 1997 HOH A O   1 
HETATM 12805 O  O   . HOH DA 6 .   ? 62.148  72.675 41.344  1.00 33.15 ? 1998 HOH A O   1 
HETATM 12806 O  O   . HOH DA 6 .   ? 51.172  28.926 43.611  1.00 36.59 ? 1999 HOH A O   1 
HETATM 12807 O  O   . HOH DA 6 .   ? 47.355  71.461 36.736  1.00 38.92 ? 2000 HOH A O   1 
HETATM 12808 O  O   . HOH DA 6 .   ? 32.224  69.395 34.955  1.00 37.40 ? 2001 HOH A O   1 
HETATM 12809 O  O   . HOH DA 6 .   ? 50.727  92.646 27.183  1.00 39.24 ? 2002 HOH A O   1 
HETATM 12810 O  O   . HOH DA 6 .   ? 68.106  58.771 33.591  1.00 35.13 ? 2003 HOH A O   1 
HETATM 12811 O  O   . HOH DA 6 .   ? 43.970  46.275 59.429  1.00 37.00 ? 2004 HOH A O   1 
HETATM 12812 O  O   . HOH DA 6 .   ? 51.383  61.781 65.000  1.00 33.99 ? 2005 HOH A O   1 
HETATM 12813 O  O   . HOH DA 6 .   ? 36.299  71.050 29.719  1.00 23.67 ? 2006 HOH A O   1 
HETATM 12814 O  O   . HOH DA 6 .   ? 37.953  48.706 14.327  1.00 41.97 ? 2007 HOH A O   1 
HETATM 12815 O  O   . HOH DA 6 .   ? 36.585  59.494 15.342  1.00 39.71 ? 2008 HOH A O   1 
HETATM 12816 O  O   . HOH DA 6 .   ? 29.294  46.581 19.119  1.00 38.66 ? 2009 HOH A O   1 
HETATM 12817 O  O   . HOH DA 6 .   ? 33.719  39.985 69.737  1.00 45.59 ? 2010 HOH A O   1 
HETATM 12818 O  O   . HOH DA 6 .   ? 52.641  56.029 45.962  1.00 45.53 ? 2011 HOH A O   1 
HETATM 12819 O  O   . HOH DA 6 .   ? 27.382  66.344 50.103  1.00 30.10 ? 2012 HOH A O   1 
HETATM 12820 O  O   . HOH DA 6 .   ? 39.557  46.493 50.582  1.00 35.70 ? 2013 HOH A O   1 
HETATM 12821 O  O   . HOH DA 6 .   ? 48.249  85.731 36.406  1.00 31.88 ? 2014 HOH A O   1 
HETATM 12822 O  O   . HOH DA 6 .   ? 79.622  50.352 36.297  1.00 34.26 ? 2015 HOH A O   1 
HETATM 12823 O  O   . HOH DA 6 .   ? 55.604  52.172 26.884  1.00 17.15 ? 2016 HOH A O   1 
HETATM 12824 O  O   . HOH DA 6 .   ? 59.694  37.065 27.854  1.00 30.32 ? 2017 HOH A O   1 
HETATM 12825 O  O   . HOH DA 6 .   ? 28.495  68.198 21.401  1.00 43.58 ? 2018 HOH A O   1 
HETATM 12826 O  O   . HOH DA 6 .   ? 44.875  89.659 31.506  1.00 46.57 ? 2019 HOH A O   1 
HETATM 12827 O  O   . HOH DA 6 .   ? 69.738  57.953 35.293  1.00 27.53 ? 2020 HOH A O   1 
HETATM 12828 O  O   . HOH DA 6 .   ? 48.799  58.821 35.623  1.00 38.43 ? 2021 HOH A O   1 
HETATM 12829 O  O   . HOH DA 6 .   ? 55.174  29.632 39.277  1.00 37.18 ? 2022 HOH A O   1 
HETATM 12830 O  O   . HOH DA 6 .   ? 49.269  83.303 19.026  1.00 40.56 ? 2023 HOH A O   1 
HETATM 12831 O  O   . HOH DA 6 .   ? 72.974  66.650 43.355  1.00 37.56 ? 2024 HOH A O   1 
HETATM 12832 O  O   . HOH DA 6 .   ? 7.701   36.455 35.217  1.00 29.19 ? 2025 HOH A O   1 
HETATM 12833 O  O   . HOH DA 6 .   ? 28.171  66.576 39.417  1.00 33.27 ? 2026 HOH A O   1 
HETATM 12834 O  O   . HOH DA 6 .   ? 37.099  57.292 58.419  1.00 47.23 ? 2027 HOH A O   1 
HETATM 12835 O  O   . HOH DA 6 .   ? 74.316  62.116 50.265  1.00 33.16 ? 2028 HOH A O   1 
HETATM 12836 O  O   . HOH DA 6 .   ? 54.622  81.417 16.732  1.00 35.98 ? 2029 HOH A O   1 
HETATM 12837 O  O   . HOH DA 6 .   ? 64.143  39.805 24.493  1.00 42.08 ? 2030 HOH A O   1 
HETATM 12838 O  O   . HOH DA 6 .   ? 34.962  80.554 35.796  1.00 43.52 ? 2031 HOH A O   1 
HETATM 12839 O  O   . HOH DA 6 .   ? 52.350  67.713 48.180  1.00 38.52 ? 2032 HOH A O   1 
HETATM 12840 O  O   . HOH DA 6 .   ? 49.196  49.725 45.590  1.00 45.15 ? 2033 HOH A O   1 
HETATM 12841 O  O   . HOH DA 6 .   ? 72.014  49.362 51.727  1.00 35.80 ? 2034 HOH A O   1 
HETATM 12842 O  O   . HOH DA 6 .   ? 43.587  57.504 39.902  1.00 37.10 ? 2035 HOH A O   1 
HETATM 12843 O  O   . HOH DA 6 .   ? 59.237  61.708 43.803  1.00 33.93 ? 2036 HOH A O   1 
HETATM 12844 O  O   . HOH DA 6 .   ? 22.329  30.637 34.818  1.00 44.55 ? 2037 HOH A O   1 
HETATM 12845 O  O   . HOH DA 6 .   ? 33.875  77.550 36.492  1.00 40.81 ? 2038 HOH A O   1 
HETATM 12846 O  O   . HOH DA 6 .   ? 17.230  37.600 58.526  1.00 37.38 ? 2039 HOH A O   1 
HETATM 12847 O  O   . HOH DA 6 .   ? 57.227  86.007 24.948  1.00 37.60 ? 2040 HOH A O   1 
HETATM 12848 O  O   . HOH DA 6 .   ? 68.828  59.784 38.916  1.00 37.62 ? 2041 HOH A O   1 
HETATM 12849 O  O   . HOH DA 6 .   ? 48.462  41.808 57.579  1.00 34.16 ? 2042 HOH A O   1 
HETATM 12850 O  O   . HOH DA 6 .   ? 42.383  63.962 64.181  1.00 37.66 ? 2043 HOH A O   1 
HETATM 12851 O  O   . HOH DA 6 .   ? 47.224  54.562 53.915  1.00 38.19 ? 2044 HOH A O   1 
HETATM 12852 O  O   . HOH DA 6 .   ? 55.029  57.678 48.293  1.00 26.97 ? 2045 HOH A O   1 
HETATM 12853 O  O   . HOH DA 6 .   ? 56.153  48.762 26.885  1.00 37.29 ? 2046 HOH A O   1 
HETATM 12854 O  O   . HOH DA 6 .   ? 44.924  64.200 62.802  1.00 28.01 ? 2047 HOH A O   1 
HETATM 12855 O  O   . HOH DA 6 .   ? 50.513  38.126 26.624  1.00 35.56 ? 2048 HOH A O   1 
HETATM 12856 O  O   . HOH DA 6 .   ? 30.987  64.615 19.872  1.00 32.53 ? 2049 HOH A O   1 
HETATM 12857 O  O   . HOH DA 6 .   ? 53.957  38.485 27.343  1.00 29.73 ? 2050 HOH A O   1 
HETATM 12858 O  O   . HOH DA 6 .   ? 77.082  50.497 36.819  1.00 26.56 ? 2051 HOH A O   1 
HETATM 12859 O  O   . HOH DA 6 .   ? 46.961  51.591 26.882  1.00 23.33 ? 2052 HOH A O   1 
HETATM 12860 O  O   . HOH DA 6 .   ? 56.478  48.241 21.852  1.00 26.39 ? 2053 HOH A O   1 
HETATM 12861 O  O   . HOH DA 6 .   ? 28.571  66.274 19.700  1.00 42.67 ? 2054 HOH A O   1 
HETATM 12862 O  O   . HOH DA 6 .   ? 39.966  66.431 40.599  1.00 36.42 ? 2055 HOH A O   1 
HETATM 12863 O  O   . HOH DA 6 .   ? 17.574  74.639 44.332  1.00 30.61 ? 2056 HOH A O   1 
HETATM 12864 O  O   . HOH DA 6 .   ? 45.126  61.353 66.169  1.00 33.77 ? 2057 HOH A O   1 
HETATM 12865 O  O   . HOH DA 6 .   ? 48.239  64.841 57.570  1.00 31.98 ? 2058 HOH A O   1 
HETATM 12866 O  O   . HOH DA 6 .   ? 42.510  61.668 40.394  1.00 38.55 ? 2059 HOH A O   1 
HETATM 12867 O  O   . HOH DA 6 .   ? 57.966  41.561 57.632  1.00 25.88 ? 2060 HOH A O   1 
HETATM 12868 O  O   . HOH DA 6 .   ? 23.432  32.587 32.255  1.00 38.56 ? 2061 HOH A O   1 
HETATM 12869 O  O   . HOH DA 6 .   ? 33.945  74.216 20.799  1.00 32.21 ? 2062 HOH A O   1 
HETATM 12870 O  O   . HOH DA 6 .   ? 34.071  68.076 43.403  1.00 36.11 ? 2063 HOH A O   1 
HETATM 12871 O  O   . HOH DA 6 .   ? 60.305  45.401 22.698  1.00 29.52 ? 2064 HOH A O   1 
HETATM 12872 O  O   . HOH DA 6 .   ? 60.787  41.957 18.861  1.00 42.12 ? 2065 HOH A O   1 
HETATM 12873 O  O   . HOH DA 6 .   ? 57.129  52.434 10.524  1.00 44.23 ? 2066 HOH A O   1 
HETATM 12874 O  O   . HOH DA 6 .   ? 65.450  40.190 51.880  1.00 30.63 ? 2067 HOH A O   1 
HETATM 12875 O  O   . HOH DA 6 .   ? 33.803  60.803 42.047  1.00 41.01 ? 2068 HOH A O   1 
HETATM 12876 O  O   . HOH DA 6 .   ? 71.997  58.458 44.432  1.00 31.63 ? 2069 HOH A O   1 
HETATM 12877 O  O   . HOH DA 6 .   ? 59.383  70.273 17.153  1.00 30.99 ? 2070 HOH A O   1 
HETATM 12878 O  O   . HOH DA 6 .   ? 61.874  50.069 64.398  1.00 34.29 ? 2071 HOH A O   1 
HETATM 12879 O  O   . HOH DA 6 .   ? 53.411  61.121 50.353  1.00 34.37 ? 2072 HOH A O   1 
HETATM 12880 O  O   . HOH DA 6 .   ? 48.842  72.747 38.311  1.00 38.13 ? 2073 HOH A O   1 
HETATM 12881 O  O   . HOH DA 6 .   ? 18.084  31.913 52.723  1.00 38.57 ? 2074 HOH A O   1 
HETATM 12882 O  O   . HOH DA 6 .   ? 71.074  66.882 31.745  1.00 43.88 ? 2075 HOH A O   1 
HETATM 12883 O  O   . HOH DA 6 .   ? 10.197  33.223 36.891  1.00 39.87 ? 2076 HOH A O   1 
HETATM 12884 O  O   . HOH DA 6 .   ? 44.210  37.793 64.597  1.00 38.51 ? 2077 HOH A O   1 
HETATM 12885 O  O   . HOH DA 6 .   ? 41.624  22.453 48.617  1.00 44.39 ? 2078 HOH A O   1 
HETATM 12886 O  O   . HOH DA 6 .   ? 80.255  43.478 42.115  1.00 36.09 ? 2079 HOH A O   1 
HETATM 12887 O  O   . HOH DA 6 .   ? 20.407  48.309 61.495  1.00 30.15 ? 2080 HOH A O   1 
HETATM 12888 O  O   . HOH DA 6 .   ? 39.634  45.710 19.512  1.00 35.58 ? 2081 HOH A O   1 
HETATM 12889 O  O   . HOH DA 6 .   ? 42.315  39.400 25.112  1.00 33.65 ? 2082 HOH A O   1 
HETATM 12890 O  O   . HOH DA 6 .   ? 55.840  55.049 66.271  1.00 31.61 ? 2083 HOH A O   1 
HETATM 12891 O  O   . HOH DA 6 .   ? 60.460  35.425 47.177  1.00 30.83 ? 2084 HOH A O   1 
HETATM 12892 O  O   . HOH DA 6 .   ? 47.214  64.639 35.828  1.00 34.04 ? 2085 HOH A O   1 
HETATM 12893 O  O   . HOH DA 6 .   ? 22.342  49.318 62.929  1.00 40.05 ? 2086 HOH A O   1 
HETATM 12894 O  O   . HOH DA 6 .   ? 69.990  68.228 51.692  1.00 38.95 ? 2087 HOH A O   1 
HETATM 12895 O  O   . HOH DA 6 .   ? 55.780  35.925 28.914  1.00 36.83 ? 2088 HOH A O   1 
HETATM 12896 O  O   . HOH DA 6 .   ? 42.432  82.703 21.811  1.00 44.61 ? 2089 HOH A O   1 
HETATM 12897 O  O   . HOH DA 6 .   ? 67.667  40.681 50.737  1.00 39.43 ? 2090 HOH A O   1 
HETATM 12898 O  O   . HOH DA 6 .   ? 74.055  40.816 31.334  1.00 36.84 ? 2091 HOH A O   1 
HETATM 12899 O  O   . HOH DA 6 .   ? 46.986  57.431 54.391  1.00 31.84 ? 2092 HOH A O   1 
HETATM 12900 O  O   . HOH DA 6 .   ? 31.179  71.471 20.042  1.00 36.86 ? 2093 HOH A O   1 
HETATM 12901 O  O   . HOH DA 6 .   ? 43.612  32.870 26.242  1.00 38.97 ? 2094 HOH A O   1 
HETATM 12902 O  O   . HOH DA 6 .   ? 48.862  51.390 50.236  1.00 35.78 ? 2095 HOH A O   1 
HETATM 12903 O  O   . HOH DA 6 .   ? 71.089  68.717 17.114  1.00 45.06 ? 2096 HOH A O   1 
HETATM 12904 O  O   . HOH DA 6 .   ? 50.551  48.698 40.928  1.00 33.54 ? 2097 HOH A O   1 
HETATM 12905 O  O   . HOH DA 6 .   ? 69.502  65.380 27.882  1.00 35.55 ? 2098 HOH A O   1 
HETATM 12906 O  O   . HOH DA 6 .   ? 43.251  24.902 51.177  1.00 34.61 ? 2099 HOH A O   1 
HETATM 12907 O  O   . HOH DA 6 .   ? 62.773  80.975 27.869  1.00 34.35 ? 2100 HOH A O   1 
HETATM 12908 O  O   . HOH DA 6 .   ? 18.430  44.097 61.716  1.00 37.65 ? 2101 HOH A O   1 
HETATM 12909 O  O   . HOH DA 6 .   ? 48.508  59.966 10.688  1.00 34.98 ? 2102 HOH A O   1 
HETATM 12910 O  O   . HOH DA 6 .   ? 37.590  22.590 45.710  1.00 42.60 ? 2103 HOH A O   1 
HETATM 12911 O  O   . HOH DA 6 .   ? 54.679  49.795 36.850  1.00 33.23 ? 2104 HOH A O   1 
HETATM 12912 O  O   . HOH DA 6 .   ? 51.909  48.751 44.928  1.00 30.77 ? 2105 HOH A O   1 
HETATM 12913 O  O   . HOH DA 6 .   ? 21.277  26.926 53.217  1.00 40.35 ? 2106 HOH A O   1 
HETATM 12914 O  O   . HOH DA 6 .   ? 36.816  30.418 31.218  1.00 32.16 ? 2107 HOH A O   1 
HETATM 12915 O  O   . HOH DA 6 .   ? 52.868  47.691 64.493  1.00 34.71 ? 2108 HOH A O   1 
HETATM 12916 O  O   . HOH DA 6 .   ? 43.801  45.869 15.640  1.00 35.70 ? 2109 HOH A O   1 
HETATM 12917 O  O   . HOH DA 6 .   ? 54.650  64.960 60.910  1.00 40.95 ? 2110 HOH A O   1 
HETATM 12918 O  O   . HOH DA 6 .   ? 56.666  60.908 11.266  1.00 37.03 ? 2111 HOH A O   1 
HETATM 12919 O  O   . HOH DA 6 .   ? 25.967  67.741 22.524  1.00 38.42 ? 2112 HOH A O   1 
HETATM 12920 O  O   . HOH DA 6 .   ? 54.142  51.151 40.567  1.00 28.65 ? 2113 HOH A O   1 
HETATM 12921 O  O   . HOH DA 6 .   ? 53.279  47.306 35.724  1.00 36.98 ? 2114 HOH A O   1 
HETATM 12922 O  O   . HOH DA 6 .   ? 56.922  42.821 52.811  1.00 38.73 ? 2115 HOH A O   1 
HETATM 12923 O  O   . HOH DA 6 .   ? 35.161  50.758 46.819  1.00 34.42 ? 2116 HOH A O   1 
HETATM 12924 O  O   . HOH DA 6 .   ? 35.864  73.794 29.091  1.00 34.49 ? 2117 HOH A O   1 
HETATM 12925 O  O   . HOH DA 6 .   ? 31.289  30.068 35.462  1.00 33.46 ? 2118 HOH A O   1 
HETATM 12926 O  O   . HOH DA 6 .   ? 26.575  60.158 59.308  1.00 37.44 ? 2119 HOH A O   1 
HETATM 12927 O  O   . HOH DA 6 .   ? 38.281  71.850 14.516  1.00 39.61 ? 2120 HOH A O   1 
HETATM 12928 O  O   . HOH DA 6 .   ? 55.518  49.903 10.354  1.00 33.95 ? 2121 HOH A O   1 
HETATM 12929 O  O   . HOH DA 6 .   ? 24.607  73.505 32.525  1.00 40.91 ? 2122 HOH A O   1 
HETATM 12930 O  O   . HOH DA 6 .   ? 16.589  74.138 30.999  1.00 39.27 ? 2123 HOH A O   1 
HETATM 12931 O  O   . HOH DA 6 .   ? 23.040  51.719 59.476  1.00 33.40 ? 2124 HOH A O   1 
HETATM 12932 O  O   . HOH DA 6 .   ? 28.488  38.257 64.864  1.00 36.92 ? 2125 HOH A O   1 
HETATM 12933 O  O   . HOH DA 6 .   ? 30.835  31.304 27.111  1.00 40.07 ? 2126 HOH A O   1 
HETATM 12934 O  O   . HOH DA 6 .   ? 60.155  58.773 11.835  1.00 38.98 ? 2127 HOH A O   1 
HETATM 12935 O  O   . HOH DA 6 .   ? 26.021  45.721 21.581  1.00 37.63 ? 2128 HOH A O   1 
HETATM 12936 O  O   . HOH DA 6 .   ? 73.599  59.034 42.400  1.00 38.87 ? 2129 HOH A O   1 
HETATM 12937 O  O   . HOH DA 6 .   ? 11.777  76.688 30.075  1.00 36.73 ? 2130 HOH A O   1 
HETATM 12938 O  O   . HOH DA 6 .   ? 21.555  74.957 36.081  1.00 34.57 ? 2131 HOH A O   1 
HETATM 12939 O  O   . HOH DA 6 .   ? 66.034  41.551 54.300  1.00 38.02 ? 2132 HOH A O   1 
HETATM 12940 O  O   . HOH DA 6 .   ? 80.022  39.220 41.538  1.00 34.95 ? 2133 HOH A O   1 
HETATM 12941 O  O   . HOH DA 6 .   ? 46.108  42.354 62.732  1.00 37.08 ? 2134 HOH A O   1 
HETATM 12942 O  O   . HOH DA 6 .   ? 27.774  27.477 41.443  1.00 39.24 ? 2135 HOH A O   1 
HETATM 12943 O  O   . HOH DA 6 .   ? 37.731  25.130 54.676  1.00 36.61 ? 2136 HOH A O   1 
HETATM 12944 O  O   . HOH DA 6 .   ? 69.371  65.165 17.652  1.00 38.96 ? 2137 HOH A O   1 
HETATM 12945 O  O   . HOH DA 6 .   ? 42.765  47.814 63.204  1.00 34.42 ? 2138 HOH A O   1 
HETATM 12946 O  O   . HOH DA 6 .   ? 36.101  73.504 24.824  1.00 36.51 ? 2139 HOH A O   1 
HETATM 12947 O  O   . HOH DA 6 .   ? 80.973  45.722 39.936  1.00 38.70 ? 2140 HOH A O   1 
HETATM 12948 O  O   . HOH DA 6 .   ? 42.321  54.218 12.168  1.00 37.46 ? 2141 HOH A O   1 
HETATM 12949 O  O   . HOH DA 6 .   ? 44.111  29.407 55.381  1.00 37.73 ? 2142 HOH A O   1 
HETATM 12950 O  O   . HOH DA 6 .   ? 64.778  54.006 9.383   1.00 40.26 ? 2143 HOH A O   1 
HETATM 12951 O  O   . HOH DA 6 .   ? 26.590  26.513 52.791  1.00 37.14 ? 2144 HOH A O   1 
HETATM 12952 O  O   . HOH DA 6 .   ? 36.033  55.803 42.547  1.00 35.68 ? 2145 HOH A O   1 
HETATM 12953 O  O   . HOH DA 6 .   ? 49.395  64.686 34.389  1.00 36.14 ? 2146 HOH A O   1 
HETATM 12954 O  O   . HOH DA 6 .   ? 64.916  57.140 34.035  1.00 34.63 ? 2147 HOH A O   1 
HETATM 12955 O  O   . HOH DA 6 .   ? 14.287  36.470 48.448  1.00 38.94 ? 2148 HOH A O   1 
HETATM 12956 O  O   . HOH DA 6 .   ? 73.803  59.669 46.186  1.00 35.12 ? 2149 HOH A O   1 
HETATM 12957 O  O   . HOH DA 6 .   ? 55.981  71.711 37.759  1.00 37.95 ? 2150 HOH A O   1 
HETATM 12958 O  O   . HOH DA 6 .   ? 77.954  59.207 24.386  1.00 36.47 ? 2151 HOH A O   1 
HETATM 12959 O  O   . HOH DA 6 .   ? 20.244  73.397 32.139  1.00 36.39 ? 2152 HOH A O   1 
HETATM 12960 O  O   . HOH DA 6 .   ? 71.726  59.106 17.396  1.00 39.57 ? 2153 HOH A O   1 
HETATM 12961 O  O   . HOH DA 6 .   ? 8.746   38.138 30.973  1.00 37.82 ? 2154 HOH A O   1 
HETATM 12962 O  O   . HOH DA 6 .   ? 44.514  60.240 13.098  1.00 34.94 ? 2155 HOH A O   1 
HETATM 12963 O  O   . HOH DA 6 .   ? 59.893  86.175 26.120  1.00 40.12 ? 2156 HOH A O   1 
HETATM 12964 O  O   . HOH DA 6 .   ? 39.950  26.079 53.421  1.00 32.39 ? 2157 HOH A O   1 
HETATM 12965 O  O   . HOH DA 6 .   ? 36.578  51.879 51.198  1.00 41.84 ? 2158 HOH A O   1 
HETATM 12966 O  O   . HOH DA 6 .   ? 39.904  56.722 71.361  1.00 41.35 ? 2159 HOH A O   1 
HETATM 12967 O  O   . HOH DA 6 .   ? 21.586  30.514 50.797  1.00 43.13 ? 2461 HOH A O   1 
HETATM 12968 O  O   . HOH DA 6 .   ? 14.794  73.924 29.133  1.00 28.98 ? 2801 HOH A O   1 
HETATM 12969 O  O   . HOH DA 6 .   ? 19.617  30.581 49.487  1.00 37.06 ? 2863 HOH A O   1 
HETATM 12970 O  O   . HOH EA 6 .   ? -4.027  54.175 45.623  1.00 28.36 ? 2323 HOH B O   1 
HETATM 12971 O  O   . HOH EA 6 .   ? 6.010   56.005 37.118  1.00 13.41 ? 2324 HOH B O   1 
HETATM 12972 O  O   . HOH EA 6 .   ? 6.164   66.074 35.507  1.00 14.69 ? 2325 HOH B O   1 
HETATM 12973 O  O   . HOH EA 6 .   ? 20.180  49.669 26.850  1.00 17.67 ? 2326 HOH B O   1 
HETATM 12974 O  O   . HOH EA 6 .   ? -8.337  60.442 48.729  1.00 18.52 ? 2327 HOH B O   1 
HETATM 12975 O  O   . HOH EA 6 .   ? 5.115   72.787 44.817  1.00 19.86 ? 2328 HOH B O   1 
HETATM 12976 O  O   . HOH EA 6 .   ? -9.338  66.477 47.713  1.00 19.88 ? 2329 HOH B O   1 
HETATM 12977 O  O   . HOH EA 6 .   ? 19.186  60.549 45.693  1.00 13.81 ? 2330 HOH B O   1 
HETATM 12978 O  O   . HOH EA 6 .   ? -24.024 82.843 27.796  1.00 20.36 ? 2331 HOH B O   1 
HETATM 12979 O  O   . HOH EA 6 .   ? -31.331 63.676 39.338  1.00 17.40 ? 2332 HOH B O   1 
HETATM 12980 O  O   . HOH EA 6 .   ? -6.459  72.312 2.955   1.00 16.07 ? 2333 HOH B O   1 
HETATM 12981 O  O   . HOH EA 6 .   ? -14.836 74.896 38.622  1.00 17.48 ? 2334 HOH B O   1 
HETATM 12982 O  O   . HOH EA 6 .   ? -25.088 63.712 46.319  1.00 20.21 ? 2335 HOH B O   1 
HETATM 12983 O  O   . HOH EA 6 .   ? -13.500 50.234 46.420  1.00 15.96 ? 2336 HOH B O   1 
HETATM 12984 O  O   . HOH EA 6 .   ? -1.711  80.928 22.810  1.00 13.46 ? 2337 HOH B O   1 
HETATM 12985 O  O   . HOH EA 6 .   ? 13.667  48.680 47.844  1.00 15.77 ? 2338 HOH B O   1 
HETATM 12986 O  O   . HOH EA 6 .   ? 5.216   64.738 16.181  1.00 18.43 ? 2339 HOH B O   1 
HETATM 12987 O  O   . HOH EA 6 .   ? 12.567  62.541 34.400  1.00 15.10 ? 2340 HOH B O   1 
HETATM 12988 O  O   . HOH EA 6 .   ? -22.276 70.117 29.862  1.00 12.49 ? 2341 HOH B O   1 
HETATM 12989 O  O   . HOH EA 6 .   ? 20.320  54.178 21.282  1.00 22.77 ? 2342 HOH B O   1 
HETATM 12990 O  O   . HOH EA 6 .   ? -5.877  64.925 39.470  1.00 13.45 ? 2343 HOH B O   1 
HETATM 12991 O  O   . HOH EA 6 .   ? 20.669  55.825 54.654  1.00 15.79 ? 2344 HOH B O   1 
HETATM 12992 O  O   . HOH EA 6 .   ? -19.036 59.637 48.519  1.00 19.49 ? 2345 HOH B O   1 
HETATM 12993 O  O   . HOH EA 6 .   ? -2.614  76.817 23.026  1.00 16.66 ? 2346 HOH B O   1 
HETATM 12994 O  O   . HOH EA 6 .   ? -2.753  77.764 31.881  1.00 15.31 ? 2347 HOH B O   1 
HETATM 12995 O  O   . HOH EA 6 .   ? 0.297   63.557 21.820  1.00 18.42 ? 2348 HOH B O   1 
HETATM 12996 O  O   . HOH EA 6 .   ? 3.739   80.777 25.942  1.00 18.53 ? 2349 HOH B O   1 
HETATM 12997 O  O   . HOH EA 6 .   ? -0.902  61.063 27.993  1.00 15.03 ? 2350 HOH B O   1 
HETATM 12998 O  O   . HOH EA 6 .   ? 16.867  56.847 34.099  1.00 26.38 ? 2351 HOH B O   1 
HETATM 12999 O  O   . HOH EA 6 .   ? 2.846   69.469 24.972  1.00 16.07 ? 2352 HOH B O   1 
HETATM 13000 O  O   . HOH EA 6 .   ? 5.674   71.628 51.737  1.00 24.02 ? 2353 HOH B O   1 
HETATM 13001 O  O   . HOH EA 6 .   ? -15.134 63.236 13.785  1.00 18.24 ? 2354 HOH B O   1 
HETATM 13002 O  O   . HOH EA 6 .   ? -16.801 63.776 50.924  1.00 18.72 ? 2355 HOH B O   1 
HETATM 13003 O  O   . HOH EA 6 .   ? -24.235 55.854 6.997   1.00 21.43 ? 2356 HOH B O   1 
HETATM 13004 O  O   . HOH EA 6 .   ? 0.698   54.733 63.241  1.00 22.56 ? 2357 HOH B O   1 
HETATM 13005 O  O   . HOH EA 6 .   ? -17.078 75.157 1.007   1.00 24.32 ? 2358 HOH B O   1 
HETATM 13006 O  O   . HOH EA 6 .   ? 6.694   63.383 59.686  1.00 27.89 ? 2359 HOH B O   1 
HETATM 13007 O  O   . HOH EA 6 .   ? -7.469  79.765 14.496  1.00 14.41 ? 2360 HOH B O   1 
HETATM 13008 O  O   . HOH EA 6 .   ? -20.265 66.582 51.163  1.00 21.40 ? 2361 HOH B O   1 
HETATM 13009 O  O   . HOH EA 6 .   ? -2.435  55.164 24.209  1.00 17.87 ? 2362 HOH B O   1 
HETATM 13010 O  O   . HOH EA 6 .   ? 9.558   45.861 50.226  1.00 16.64 ? 2363 HOH B O   1 
HETATM 13011 O  O   . HOH EA 6 .   ? -21.746 51.795 21.145  1.00 22.83 ? 2364 HOH B O   1 
HETATM 13012 O  O   . HOH EA 6 .   ? 8.948   56.943 26.867  1.00 19.55 ? 2365 HOH B O   1 
HETATM 13013 O  O   . HOH EA 6 .   ? 13.347  54.590 30.951  1.00 14.32 ? 2366 HOH B O   1 
HETATM 13014 O  O   . HOH EA 6 .   ? 6.410   42.571 4.559   1.00 46.05 ? 2367 HOH B O   1 
HETATM 13015 O  O   . HOH EA 6 .   ? 0.021   62.966 26.176  1.00 13.30 ? 2368 HOH B O   1 
HETATM 13016 O  O   . HOH EA 6 .   ? -20.383 39.037 29.207  1.00 39.47 ? 2369 HOH B O   1 
HETATM 13017 O  O   . HOH EA 6 .   ? 9.965   70.330 19.291  1.00 27.41 ? 2370 HOH B O   1 
HETATM 13018 O  O   . HOH EA 6 .   ? -17.380 68.942 45.468  1.00 18.72 ? 2371 HOH B O   1 
HETATM 13019 O  O   . HOH EA 6 .   ? -6.396  55.288 15.072  1.00 26.68 ? 2372 HOH B O   1 
HETATM 13020 O  O   . HOH EA 6 .   ? -13.671 84.722 14.783  1.00 25.65 ? 2373 HOH B O   1 
HETATM 13021 O  O   . HOH EA 6 .   ? -15.025 87.693 23.379  1.00 27.82 ? 2374 HOH B O   1 
HETATM 13022 O  O   . HOH EA 6 .   ? -6.789  81.892 16.188  1.00 17.45 ? 2375 HOH B O   1 
HETATM 13023 O  O   . HOH EA 6 .   ? -3.714  56.692 44.786  1.00 18.02 ? 2376 HOH B O   1 
HETATM 13024 O  O   . HOH EA 6 .   ? -35.883 53.650 39.340  1.00 25.05 ? 2377 HOH B O   1 
HETATM 13025 O  O   . HOH EA 6 .   ? -21.763 66.573 29.829  1.00 29.86 ? 2378 HOH B O   1 
HETATM 13026 O  O   . HOH EA 6 .   ? 15.980  43.042 27.655  1.00 23.60 ? 2379 HOH B O   1 
HETATM 13027 O  O   . HOH EA 6 .   ? -12.862 56.142 2.108   1.00 19.95 ? 2380 HOH B O   1 
HETATM 13028 O  O   . HOH EA 6 .   ? 14.893  63.322 32.954  1.00 16.45 ? 2381 HOH B O   1 
HETATM 13029 O  O   . HOH EA 6 .   ? -6.471  62.364 29.597  1.00 13.79 ? 2382 HOH B O   1 
HETATM 13030 O  O   . HOH EA 6 .   ? 17.020  50.692 55.423  1.00 24.61 ? 2383 HOH B O   1 
HETATM 13031 O  O   . HOH EA 6 .   ? -24.785 55.105 19.937  1.00 22.07 ? 2384 HOH B O   1 
HETATM 13032 O  O   . HOH EA 6 .   ? -9.028  52.892 67.665  1.00 31.90 ? 2385 HOH B O   1 
HETATM 13033 O  O   . HOH EA 6 .   ? 18.246  46.582 20.397  1.00 29.30 ? 2386 HOH B O   1 
HETATM 13034 O  O   . HOH EA 6 .   ? -29.667 41.285 23.444  1.00 22.75 ? 2387 HOH B O   1 
HETATM 13035 O  O   . HOH EA 6 .   ? -30.729 50.124 41.118  1.00 20.92 ? 2388 HOH B O   1 
HETATM 13036 O  O   . HOH EA 6 .   ? -0.885  73.138 4.641   1.00 23.24 ? 2389 HOH B O   1 
HETATM 13037 O  O   . HOH EA 6 .   ? -8.169  64.926 40.844  1.00 15.89 ? 2390 HOH B O   1 
HETATM 13038 O  O   . HOH EA 6 .   ? -18.477 29.758 38.444  1.00 39.11 ? 2391 HOH B O   1 
HETATM 13039 O  O   . HOH EA 6 .   ? 21.247  57.684 22.164  1.00 31.71 ? 2392 HOH B O   1 
HETATM 13040 O  O   . HOH EA 6 .   ? -2.051  49.832 39.555  1.00 22.16 ? 2393 HOH B O   1 
HETATM 13041 O  O   . HOH EA 6 .   ? -8.602  31.988 47.010  1.00 33.23 ? 2394 HOH B O   1 
HETATM 13042 O  O   . HOH EA 6 .   ? 11.735  74.479 39.185  1.00 30.67 ? 2395 HOH B O   1 
HETATM 13043 O  O   . HOH EA 6 .   ? -5.431  62.429 -4.773  1.00 23.59 ? 2396 HOH B O   1 
HETATM 13044 O  O   . HOH EA 6 .   ? -8.572  81.026 6.010   1.00 27.03 ? 2397 HOH B O   1 
HETATM 13045 O  O   . HOH EA 6 .   ? -11.209 62.419 30.258  1.00 39.13 ? 2398 HOH B O   1 
HETATM 13046 O  O   . HOH EA 6 .   ? 2.728   80.056 23.691  1.00 21.87 ? 2399 HOH B O   1 
HETATM 13047 O  O   . HOH EA 6 .   ? -18.387 75.372 24.421  1.00 25.86 ? 2400 HOH B O   1 
HETATM 13048 O  O   . HOH EA 6 .   ? -9.706  27.095 60.670  1.00 55.81 ? 2401 HOH B O   1 
HETATM 13049 O  O   . HOH EA 6 .   ? -25.103 80.067 3.830   1.00 31.45 ? 2402 HOH B O   1 
HETATM 13050 O  O   . HOH EA 6 .   ? 17.687  42.029 23.949  1.00 31.84 ? 2403 HOH B O   1 
HETATM 13051 O  O   . HOH EA 6 .   ? 2.568   63.988 5.684   1.00 25.86 ? 2404 HOH B O   1 
HETATM 13052 O  O   . HOH EA 6 .   ? -34.402 68.482 22.068  1.00 18.71 ? 2405 HOH B O   1 
HETATM 13053 O  O   . HOH EA 6 .   ? -29.671 81.538 26.463  1.00 21.31 ? 2406 HOH B O   1 
HETATM 13054 O  O   . HOH EA 6 .   ? -19.690 76.482 35.686  1.00 17.05 ? 2407 HOH B O   1 
HETATM 13055 O  O   . HOH EA 6 .   ? -16.667 57.524 41.823  1.00 18.73 ? 2408 HOH B O   1 
HETATM 13056 O  O   . HOH EA 6 .   ? -8.112  58.843 51.098  1.00 17.53 ? 2409 HOH B O   1 
HETATM 13057 O  O   . HOH EA 6 .   ? -1.000  73.656 7.547   1.00 26.69 ? 2410 HOH B O   1 
HETATM 13058 O  O   . HOH EA 6 .   ? -3.760  42.531 39.106  1.00 28.60 ? 2411 HOH B O   1 
HETATM 13059 O  O   . HOH EA 6 .   ? -22.054 81.269 29.098  1.00 21.70 ? 2412 HOH B O   1 
HETATM 13060 O  O   . HOH EA 6 .   ? -8.032  56.705 24.893  1.00 28.04 ? 2413 HOH B O   1 
HETATM 13061 O  O   . HOH EA 6 .   ? -16.546 26.217 20.429  1.00 48.32 ? 2414 HOH B O   1 
HETATM 13062 O  O   . HOH EA 6 .   ? -8.329  69.337 -3.075  1.00 28.63 ? 2415 HOH B O   1 
HETATM 13063 O  O   . HOH EA 6 .   ? -17.733 68.654 41.152  1.00 20.57 ? 2416 HOH B O   1 
HETATM 13064 O  O   . HOH EA 6 .   ? 22.657  68.335 46.076  1.00 41.83 ? 2417 HOH B O   1 
HETATM 13065 O  O   . HOH EA 6 .   ? 14.666  71.061 28.266  1.00 26.74 ? 2418 HOH B O   1 
HETATM 13066 O  O   . HOH EA 6 .   ? 12.075  61.048 21.336  1.00 23.38 ? 2419 HOH B O   1 
HETATM 13067 O  O   . HOH EA 6 .   ? 14.147  72.299 25.412  1.00 24.71 ? 2420 HOH B O   1 
HETATM 13068 O  O   . HOH EA 6 .   ? -28.079 69.368 10.748  1.00 25.74 ? 2421 HOH B O   1 
HETATM 13069 O  O   . HOH EA 6 .   ? 5.184   62.227 61.917  1.00 18.92 ? 2422 HOH B O   1 
HETATM 13070 O  O   . HOH EA 6 .   ? -16.941 40.297 54.680  1.00 29.03 ? 2423 HOH B O   1 
HETATM 13071 O  O   . HOH EA 6 .   ? -5.141  81.066 18.146  1.00 14.80 ? 2424 HOH B O   1 
HETATM 13072 O  O   . HOH EA 6 .   ? 9.720   78.112 28.558  1.00 19.91 ? 2425 HOH B O   1 
HETATM 13073 O  O   . HOH EA 6 .   ? -33.436 60.413 43.066  1.00 23.53 ? 2426 HOH B O   1 
HETATM 13074 O  O   . HOH EA 6 .   ? -19.927 83.401 17.928  1.00 24.05 ? 2427 HOH B O   1 
HETATM 13075 O  O   . HOH EA 6 .   ? -25.848 63.889 9.827   1.00 24.59 ? 2428 HOH B O   1 
HETATM 13076 O  O   . HOH EA 6 .   ? 4.295   66.893 22.390  1.00 18.44 ? 2429 HOH B O   1 
HETATM 13077 O  O   . HOH EA 6 .   ? 23.024  63.825 47.289  1.00 31.00 ? 2430 HOH B O   1 
HETATM 13078 O  O   . HOH EA 6 .   ? -1.866  67.959 61.578  1.00 43.71 ? 2431 HOH B O   1 
HETATM 13079 O  O   . HOH EA 6 .   ? -27.839 59.160 42.214  1.00 15.36 ? 2432 HOH B O   1 
HETATM 13080 O  O   . HOH EA 6 .   ? 2.799   57.808 31.629  1.00 15.83 ? 2433 HOH B O   1 
HETATM 13081 O  O   . HOH EA 6 .   ? -17.071 49.297 15.006  1.00 24.62 ? 2434 HOH B O   1 
HETATM 13082 O  O   . HOH EA 6 .   ? -3.464  65.995 -2.456  1.00 16.93 ? 2435 HOH B O   1 
HETATM 13083 O  O   . HOH EA 6 .   ? -22.050 69.082 7.011   1.00 21.18 ? 2436 HOH B O   1 
HETATM 13084 O  O   . HOH EA 6 .   ? -5.442  57.138 19.306  1.00 26.78 ? 2437 HOH B O   1 
HETATM 13085 O  O   . HOH EA 6 .   ? -2.616  80.075 20.290  1.00 19.90 ? 2438 HOH B O   1 
HETATM 13086 O  O   . HOH EA 6 .   ? -21.389 50.985 24.343  1.00 18.93 ? 2439 HOH B O   1 
HETATM 13087 O  O   . HOH EA 6 .   ? -35.059 42.407 32.250  1.00 45.88 ? 2440 HOH B O   1 
HETATM 13088 O  O   . HOH EA 6 .   ? -17.430 42.576 23.384  1.00 33.47 ? 2441 HOH B O   1 
HETATM 13089 O  O   . HOH EA 6 .   ? -31.482 69.493 47.353  1.00 25.96 ? 2442 HOH B O   1 
HETATM 13090 O  O   . HOH EA 6 .   ? -18.113 74.703 21.875  1.00 16.64 ? 2443 HOH B O   1 
HETATM 13091 O  O   . HOH EA 6 .   ? -6.718  67.429 -5.415  1.00 21.91 ? 2444 HOH B O   1 
HETATM 13092 O  O   . HOH EA 6 .   ? -7.053  51.487 45.505  1.00 16.31 ? 2445 HOH B O   1 
HETATM 13093 O  O   . HOH EA 6 .   ? 19.148  59.365 32.278  1.00 20.38 ? 2446 HOH B O   1 
HETATM 13094 O  O   . HOH EA 6 .   ? -36.312 49.646 32.787  1.00 22.60 ? 2447 HOH B O   1 
HETATM 13095 O  O   . HOH EA 6 .   ? -10.178 69.504 38.945  1.00 17.70 ? 2448 HOH B O   1 
HETATM 13096 O  O   . HOH EA 6 .   ? -19.775 71.990 48.448  1.00 22.39 ? 2449 HOH B O   1 
HETATM 13097 O  O   . HOH EA 6 .   ? 14.824  70.051 52.724  1.00 28.40 ? 2450 HOH B O   1 
HETATM 13098 O  O   . HOH EA 6 .   ? -8.874  49.454 41.960  1.00 25.50 ? 2451 HOH B O   1 
HETATM 13099 O  O   . HOH EA 6 .   ? -31.990 42.528 13.586  1.00 36.39 ? 2452 HOH B O   1 
HETATM 13100 O  O   . HOH EA 6 .   ? -20.363 78.880 27.844  1.00 22.04 ? 2453 HOH B O   1 
HETATM 13101 O  O   . HOH EA 6 .   ? 23.152  61.640 54.015  1.00 20.75 ? 2454 HOH B O   1 
HETATM 13102 O  O   . HOH EA 6 .   ? -1.245  44.991 17.287  1.00 33.21 ? 2455 HOH B O   1 
HETATM 13103 O  O   . HOH EA 6 .   ? -4.964  76.768 52.120  1.00 40.59 ? 2456 HOH B O   1 
HETATM 13104 O  O   . HOH EA 6 .   ? -10.619 87.300 15.614  1.00 36.37 ? 2457 HOH B O   1 
HETATM 13105 O  O   . HOH EA 6 .   ? -3.041  83.673 37.717  1.00 29.14 ? 2458 HOH B O   1 
HETATM 13106 O  O   . HOH EA 6 .   ? -13.052 74.053 -1.143  1.00 31.93 ? 2459 HOH B O   1 
HETATM 13107 O  O   . HOH EA 6 .   ? 4.993   55.385 25.695  1.00 22.02 ? 2460 HOH B O   1 
HETATM 13108 O  O   . HOH EA 6 .   ? 1.089   59.528 29.404  1.00 15.16 ? 2462 HOH B O   1 
HETATM 13109 O  O   . HOH EA 6 .   ? -35.932 72.441 27.322  1.00 27.25 ? 2463 HOH B O   1 
HETATM 13110 O  O   . HOH EA 6 .   ? 0.364   58.977 31.981  1.00 12.78 ? 2464 HOH B O   1 
HETATM 13111 O  O   . HOH EA 6 .   ? -10.919 24.649 61.383  1.00 43.12 ? 2465 HOH B O   1 
HETATM 13112 O  O   . HOH EA 6 .   ? -15.932 67.187 -5.634  1.00 26.91 ? 2466 HOH B O   1 
HETATM 13113 O  O   . HOH EA 6 .   ? 0.279   79.478 23.902  1.00 18.77 ? 2467 HOH B O   1 
HETATM 13114 O  O   . HOH EA 6 .   ? -15.020 75.846 2.475   1.00 17.65 ? 2468 HOH B O   1 
HETATM 13115 O  O   . HOH EA 6 .   ? -11.801 45.625 40.110  1.00 27.28 ? 2469 HOH B O   1 
HETATM 13116 O  O   . HOH EA 6 .   ? -4.983  47.533 43.121  1.00 26.46 ? 2470 HOH B O   1 
HETATM 13117 O  O   . HOH EA 6 .   ? -21.527 58.829 48.906  1.00 17.00 ? 2471 HOH B O   1 
HETATM 13118 O  O   . HOH EA 6 .   ? -29.554 74.900 39.438  1.00 21.77 ? 2472 HOH B O   1 
HETATM 13119 O  O   . HOH EA 6 .   ? -0.156  48.839 37.965  1.00 21.65 ? 2473 HOH B O   1 
HETATM 13120 O  O   . HOH EA 6 .   ? 20.521  58.098 56.015  1.00 19.58 ? 2474 HOH B O   1 
HETATM 13121 O  O   . HOH EA 6 .   ? -14.765 75.215 5.167   1.00 15.78 ? 2475 HOH B O   1 
HETATM 13122 O  O   . HOH EA 6 .   ? -18.895 67.543 17.028  1.00 16.13 ? 2476 HOH B O   1 
HETATM 13123 O  O   . HOH EA 6 .   ? -3.433  60.976 38.329  1.00 19.04 ? 2477 HOH B O   1 
HETATM 13124 O  O   . HOH EA 6 .   ? -0.447  85.515 28.020  1.00 21.65 ? 2478 HOH B O   1 
HETATM 13125 O  O   . HOH EA 6 .   ? -13.066 62.838 39.448  1.00 17.94 ? 2479 HOH B O   1 
HETATM 13126 O  O   . HOH EA 6 .   ? 8.891   56.433 24.134  1.00 29.47 ? 2480 HOH B O   1 
HETATM 13127 O  O   . HOH EA 6 .   ? -30.761 64.520 46.998  1.00 24.22 ? 2481 HOH B O   1 
HETATM 13128 O  O   . HOH EA 6 .   ? -13.613 81.929 8.593   1.00 22.11 ? 2482 HOH B O   1 
HETATM 13129 O  O   . HOH EA 6 .   ? -3.207  61.944 -6.107  1.00 17.12 ? 2483 HOH B O   1 
HETATM 13130 O  O   . HOH EA 6 .   ? 3.728   85.008 45.321  1.00 38.40 ? 2484 HOH B O   1 
HETATM 13131 O  O   . HOH EA 6 .   ? -16.317 42.107 56.411  1.00 23.63 ? 2485 HOH B O   1 
HETATM 13132 O  O   . HOH EA 6 .   ? 14.899  57.594 32.332  1.00 17.73 ? 2486 HOH B O   1 
HETATM 13133 O  O   . HOH EA 6 .   ? -9.328  51.439 48.510  1.00 26.89 ? 2487 HOH B O   1 
HETATM 13134 O  O   . HOH EA 6 .   ? -10.227 62.200 47.499  1.00 19.12 ? 2488 HOH B O   1 
HETATM 13135 O  O   . HOH EA 6 .   ? -13.866 55.875 13.118  1.00 27.54 ? 2489 HOH B O   1 
HETATM 13136 O  O   . HOH EA 6 .   ? 12.088  48.238 27.670  1.00 19.39 ? 2490 HOH B O   1 
HETATM 13137 O  O   . HOH EA 6 .   ? -22.211 84.928 27.764  1.00 15.17 ? 2491 HOH B O   1 
HETATM 13138 O  O   . HOH EA 6 .   ? -4.247  68.514 -2.671  1.00 23.98 ? 2492 HOH B O   1 
HETATM 13139 O  O   . HOH EA 6 .   ? 0.666   68.369 61.009  1.00 43.83 ? 2493 HOH B O   1 
HETATM 13140 O  O   . HOH EA 6 .   ? 7.635   48.391 65.160  1.00 48.50 ? 2494 HOH B O   1 
HETATM 13141 O  O   . HOH EA 6 .   ? -19.863 82.620 33.960  1.00 29.52 ? 2495 HOH B O   1 
HETATM 13142 O  O   . HOH EA 6 .   ? 7.121   55.846 28.485  1.00 18.36 ? 2496 HOH B O   1 
HETATM 13143 O  O   . HOH EA 6 .   ? -9.504  62.521 40.168  1.00 17.46 ? 2497 HOH B O   1 
HETATM 13144 O  O   . HOH EA 6 .   ? 5.157   82.182 33.456  1.00 38.78 ? 2498 HOH B O   1 
HETATM 13145 O  O   . HOH EA 6 .   ? -8.982  38.121 41.141  1.00 24.73 ? 2499 HOH B O   1 
HETATM 13146 O  O   . HOH EA 6 .   ? -15.287 88.629 19.818  1.00 28.03 ? 2500 HOH B O   1 
HETATM 13147 O  O   . HOH EA 6 .   ? -21.571 56.846 35.764  1.00 18.04 ? 2501 HOH B O   1 
HETATM 13148 O  O   . HOH EA 6 .   ? -26.989 66.759 21.403  1.00 27.55 ? 2502 HOH B O   1 
HETATM 13149 O  O   . HOH EA 6 .   ? -11.747 60.295 -4.605  1.00 20.42 ? 2503 HOH B O   1 
HETATM 13150 O  O   . HOH EA 6 .   ? -11.395 75.506 -2.051  1.00 33.56 ? 2504 HOH B O   1 
HETATM 13151 O  O   . HOH EA 6 .   ? 2.754   51.016 14.660  1.00 36.57 ? 2505 HOH B O   1 
HETATM 13152 O  O   . HOH EA 6 .   ? -9.817  64.417 49.430  1.00 18.42 ? 2506 HOH B O   1 
HETATM 13153 O  O   . HOH EA 6 .   ? -5.340  81.287 39.737  1.00 29.27 ? 2507 HOH B O   1 
HETATM 13154 O  O   . HOH EA 6 .   ? 5.512   55.494 7.293   1.00 38.21 ? 2508 HOH B O   1 
HETATM 13155 O  O   . HOH EA 6 .   ? 10.786  60.387 33.464  1.00 14.37 ? 2509 HOH B O   1 
HETATM 13156 O  O   . HOH EA 6 .   ? 25.978  50.647 19.057  1.00 26.23 ? 2510 HOH B O   1 
HETATM 13157 O  O   . HOH EA 6 .   ? -22.501 65.187 50.873  1.00 33.20 ? 2511 HOH B O   1 
HETATM 13158 O  O   . HOH EA 6 .   ? 3.974   37.851 44.549  1.00 25.55 ? 2512 HOH B O   1 
HETATM 13159 O  O   . HOH EA 6 .   ? -6.762  56.179 43.417  1.00 35.69 ? 2513 HOH B O   1 
HETATM 13160 O  O   . HOH EA 6 .   ? -7.464  50.214 19.684  1.00 31.00 ? 2514 HOH B O   1 
HETATM 13161 O  O   . HOH EA 6 .   ? 9.602   80.173 29.869  1.00 36.52 ? 2515 HOH B O   1 
HETATM 13162 O  O   . HOH EA 6 .   ? 23.191  51.452 20.330  1.00 19.01 ? 2516 HOH B O   1 
HETATM 13163 O  O   . HOH EA 6 .   ? -19.163 49.727 47.066  1.00 26.82 ? 2517 HOH B O   1 
HETATM 13164 O  O   . HOH EA 6 .   ? -14.755 47.520 46.354  1.00 33.29 ? 2518 HOH B O   1 
HETATM 13165 O  O   . HOH EA 6 .   ? -13.448 73.156 -9.835  1.00 27.43 ? 2519 HOH B O   1 
HETATM 13166 O  O   . HOH EA 6 .   ? 0.154   70.522 53.898  1.00 24.66 ? 2520 HOH B O   1 
HETATM 13167 O  O   . HOH EA 6 .   ? -19.464 58.940 37.059  1.00 21.38 ? 2521 HOH B O   1 
HETATM 13168 O  O   . HOH EA 6 .   ? -17.168 62.153 48.419  1.00 21.72 ? 2522 HOH B O   1 
HETATM 13169 O  O   . HOH EA 6 .   ? 3.530   58.830 10.951  1.00 28.57 ? 2523 HOH B O   1 
HETATM 13170 O  O   . HOH EA 6 .   ? -11.353 61.750 15.470  1.00 28.81 ? 2524 HOH B O   1 
HETATM 13171 O  O   . HOH EA 6 .   ? 4.922   67.772 6.349   1.00 20.27 ? 2525 HOH B O   1 
HETATM 13172 O  O   . HOH EA 6 .   ? -26.152 65.452 48.287  1.00 29.93 ? 2526 HOH B O   1 
HETATM 13173 O  O   . HOH EA 6 .   ? -22.891 57.138 31.166  1.00 16.69 ? 2527 HOH B O   1 
HETATM 13174 O  O   . HOH EA 6 .   ? -30.552 79.569 13.151  1.00 26.75 ? 2528 HOH B O   1 
HETATM 13175 O  O   . HOH EA 6 .   ? -10.231 60.083 41.876  1.00 29.68 ? 2529 HOH B O   1 
HETATM 13176 O  O   . HOH EA 6 .   ? -19.044 78.625 42.747  1.00 32.76 ? 2530 HOH B O   1 
HETATM 13177 O  O   . HOH EA 6 .   ? -1.576  45.553 34.329  1.00 38.57 ? 2531 HOH B O   1 
HETATM 13178 O  O   . HOH EA 6 .   ? -18.654 71.141 34.958  1.00 20.51 ? 2532 HOH B O   1 
HETATM 13179 O  O   . HOH EA 6 .   ? -36.050 62.659 19.059  1.00 31.28 ? 2533 HOH B O   1 
HETATM 13180 O  O   . HOH EA 6 .   ? -12.933 73.973 1.859   1.00 21.48 ? 2534 HOH B O   1 
HETATM 13181 O  O   . HOH EA 6 .   ? -33.186 67.948 19.796  1.00 19.85 ? 2535 HOH B O   1 
HETATM 13182 O  O   . HOH EA 6 .   ? -9.068  54.441 14.773  1.00 31.29 ? 2536 HOH B O   1 
HETATM 13183 O  O   . HOH EA 6 .   ? -21.437 69.254 51.376  1.00 21.29 ? 2537 HOH B O   1 
HETATM 13184 O  O   . HOH EA 6 .   ? -32.999 80.033 19.892  1.00 41.54 ? 2538 HOH B O   1 
HETATM 13185 O  O   . HOH EA 6 .   ? -41.040 66.932 26.239  1.00 22.52 ? 2539 HOH B O   1 
HETATM 13186 O  O   . HOH EA 6 .   ? -3.434  57.552 -1.417  1.00 31.41 ? 2540 HOH B O   1 
HETATM 13187 O  O   . HOH EA 6 .   ? -26.499 58.791 44.478  1.00 19.25 ? 2541 HOH B O   1 
HETATM 13188 O  O   . HOH EA 6 .   ? -2.770  59.299 36.032  1.00 26.43 ? 2542 HOH B O   1 
HETATM 13189 O  O   . HOH EA 6 .   ? 22.570  48.549 20.062  1.00 26.17 ? 2543 HOH B O   1 
HETATM 13190 O  O   . HOH EA 6 .   ? 16.067  48.151 20.962  1.00 22.22 ? 2544 HOH B O   1 
HETATM 13191 O  O   . HOH EA 6 .   ? 3.584   59.703 16.444  1.00 39.87 ? 2545 HOH B O   1 
HETATM 13192 O  O   . HOH EA 6 .   ? 13.024  45.510 27.429  1.00 22.44 ? 2546 HOH B O   1 
HETATM 13193 O  O   . HOH EA 6 .   ? 3.675   49.057 65.285  1.00 39.02 ? 2547 HOH B O   1 
HETATM 13194 O  O   . HOH EA 6 .   ? 1.859   73.530 51.367  1.00 26.32 ? 2548 HOH B O   1 
HETATM 13195 O  O   . HOH EA 6 .   ? 11.992  56.219 55.834  1.00 18.83 ? 2549 HOH B O   1 
HETATM 13196 O  O   . HOH EA 6 .   ? -6.112  69.083 32.658  1.00 17.17 ? 2550 HOH B O   1 
HETATM 13197 O  O   . HOH EA 6 .   ? -5.947  49.843 41.616  1.00 39.89 ? 2551 HOH B O   1 
HETATM 13198 O  O   . HOH EA 6 .   ? 23.067  57.163 25.162  1.00 22.19 ? 2552 HOH B O   1 
HETATM 13199 O  O   . HOH EA 6 .   ? -18.458 65.902 -4.384  1.00 40.89 ? 2553 HOH B O   1 
HETATM 13200 O  O   . HOH EA 6 .   ? -9.007  37.122 57.201  1.00 26.77 ? 2554 HOH B O   1 
HETATM 13201 O  O   . HOH EA 6 .   ? -17.630 58.492 0.080   1.00 25.63 ? 2555 HOH B O   1 
HETATM 13202 O  O   . HOH EA 6 .   ? 2.271   62.393 17.968  1.00 34.95 ? 2556 HOH B O   1 
HETATM 13203 O  O   . HOH EA 6 .   ? -6.015  48.905 46.026  1.00 19.49 ? 2557 HOH B O   1 
HETATM 13204 O  O   . HOH EA 6 .   ? -24.342 68.301 20.457  1.00 26.30 ? 2558 HOH B O   1 
HETATM 13205 O  O   . HOH EA 6 .   ? 7.231   40.458 37.936  1.00 18.82 ? 2559 HOH B O   1 
HETATM 13206 O  O   . HOH EA 6 .   ? -30.733 53.317 12.945  1.00 37.07 ? 2560 HOH B O   1 
HETATM 13207 O  O   . HOH EA 6 .   ? -33.197 38.331 31.033  1.00 29.19 ? 2561 HOH B O   1 
HETATM 13208 O  O   . HOH EA 6 .   ? -4.204  56.506 17.212  1.00 31.54 ? 2562 HOH B O   1 
HETATM 13209 O  O   . HOH EA 6 .   ? -16.747 70.370 33.348  1.00 27.89 ? 2563 HOH B O   1 
HETATM 13210 O  O   . HOH EA 6 .   ? -8.921  57.778 41.448  1.00 28.85 ? 2564 HOH B O   1 
HETATM 13211 O  O   . HOH EA 6 .   ? 6.624   40.078 40.760  1.00 23.69 ? 2565 HOH B O   1 
HETATM 13212 O  O   . HOH EA 6 .   ? -1.260  78.987 26.127  1.00 16.76 ? 2566 HOH B O   1 
HETATM 13213 O  O   . HOH EA 6 .   ? -10.673 52.378 50.656  1.00 21.22 ? 2567 HOH B O   1 
HETATM 13214 O  O   . HOH EA 6 .   ? -37.016 56.682 27.958  1.00 24.19 ? 2568 HOH B O   1 
HETATM 13215 O  O   . HOH EA 6 .   ? -35.317 68.384 18.570  1.00 33.06 ? 2569 HOH B O   1 
HETATM 13216 O  O   . HOH EA 6 .   ? 11.346  47.254 34.835  1.00 16.45 ? 2570 HOH B O   1 
HETATM 13217 O  O   . HOH EA 6 .   ? 10.779  54.844 22.509  1.00 47.91 ? 2571 HOH B O   1 
HETATM 13218 O  O   . HOH EA 6 .   ? -21.489 58.044 33.263  1.00 21.29 ? 2572 HOH B O   1 
HETATM 13219 O  O   . HOH EA 6 .   ? 2.457   62.335 59.300  1.00 23.25 ? 2573 HOH B O   1 
HETATM 13220 O  O   . HOH EA 6 .   ? -10.479 59.213 -2.350  1.00 19.43 ? 2574 HOH B O   1 
HETATM 13221 O  O   . HOH EA 6 .   ? 11.093  37.197 48.168  1.00 36.55 ? 2575 HOH B O   1 
HETATM 13222 O  O   . HOH EA 6 .   ? -12.581 60.455 40.754  1.00 26.89 ? 2576 HOH B O   1 
HETATM 13223 O  O   . HOH EA 6 .   ? 4.139   64.121 21.781  1.00 26.04 ? 2577 HOH B O   1 
HETATM 13224 O  O   . HOH EA 6 .   ? -13.508 81.561 17.248  1.00 20.28 ? 2578 HOH B O   1 
HETATM 13225 O  O   . HOH EA 6 .   ? -21.524 80.692 33.927  1.00 34.60 ? 2579 HOH B O   1 
HETATM 13226 O  O   . HOH EA 6 .   ? 1.406   36.065 42.618  1.00 34.16 ? 2580 HOH B O   1 
HETATM 13227 O  O   . HOH EA 6 .   ? -21.498 87.268 25.781  1.00 33.92 ? 2581 HOH B O   1 
HETATM 13228 O  O   . HOH EA 6 .   ? -17.443 76.070 36.836  1.00 23.26 ? 2582 HOH B O   1 
HETATM 13229 O  O   . HOH EA 6 .   ? -30.936 77.145 39.824  1.00 28.29 ? 2583 HOH B O   1 
HETATM 13230 O  O   . HOH EA 6 .   ? -10.498 62.775 35.183  1.00 22.36 ? 2584 HOH B O   1 
HETATM 13231 O  O   . HOH EA 6 .   ? -11.205 56.434 15.016  1.00 35.76 ? 2585 HOH B O   1 
HETATM 13232 O  O   . HOH EA 6 .   ? -21.107 51.807 36.251  1.00 23.40 ? 2586 HOH B O   1 
HETATM 13233 O  O   . HOH EA 6 .   ? -10.726 43.667 38.639  1.00 34.21 ? 2587 HOH B O   1 
HETATM 13234 O  O   . HOH EA 6 .   ? 5.977   66.153 2.796   1.00 23.76 ? 2588 HOH B O   1 
HETATM 13235 O  O   . HOH EA 6 .   ? 23.075  44.613 20.076  1.00 37.76 ? 2589 HOH B O   1 
HETATM 13236 O  O   . HOH EA 6 .   ? -32.379 79.660 35.851  1.00 27.22 ? 2590 HOH B O   1 
HETATM 13237 O  O   . HOH EA 6 .   ? -2.771  52.682 39.325  1.00 36.23 ? 2591 HOH B O   1 
HETATM 13238 O  O   . HOH EA 6 .   ? -41.828 60.294 37.043  1.00 25.81 ? 2592 HOH B O   1 
HETATM 13239 O  O   . HOH EA 6 .   ? -24.910 82.250 31.715  1.00 40.48 ? 2593 HOH B O   1 
HETATM 13240 O  O   . HOH EA 6 .   ? -2.685  81.286 9.816   1.00 27.34 ? 2594 HOH B O   1 
HETATM 13241 O  O   . HOH EA 6 .   ? -3.176  54.316 28.499  1.00 31.63 ? 2595 HOH B O   1 
HETATM 13242 O  O   . HOH EA 6 .   ? -23.204 69.359 49.497  1.00 23.76 ? 2596 HOH B O   1 
HETATM 13243 O  O   . HOH EA 6 .   ? 4.447   56.242 28.269  1.00 16.03 ? 2597 HOH B O   1 
HETATM 13244 O  O   . HOH EA 6 .   ? -5.385  52.706 43.477  1.00 38.32 ? 2598 HOH B O   1 
HETATM 13245 O  O   . HOH EA 6 .   ? -16.254 35.462 35.842  1.00 29.45 ? 2599 HOH B O   1 
HETATM 13246 O  O   . HOH EA 6 .   ? -2.022  51.448 -5.072  1.00 44.99 ? 2600 HOH B O   1 
HETATM 13247 O  O   . HOH EA 6 .   ? 4.331   79.193 18.042  1.00 36.02 ? 2601 HOH B O   1 
HETATM 13248 O  O   . HOH EA 6 .   ? -12.915 44.699 47.722  1.00 38.77 ? 2602 HOH B O   1 
HETATM 13249 O  O   . HOH EA 6 .   ? -16.662 68.408 22.997  1.00 45.97 ? 2603 HOH B O   1 
HETATM 13250 O  O   . HOH EA 6 .   ? -17.262 65.911 15.065  1.00 27.85 ? 2604 HOH B O   1 
HETATM 13251 O  O   . HOH EA 6 .   ? 2.523   43.573 29.758  1.00 27.13 ? 2605 HOH B O   1 
HETATM 13252 O  O   . HOH EA 6 .   ? -31.246 74.618 12.028  1.00 40.73 ? 2606 HOH B O   1 
HETATM 13253 O  O   . HOH EA 6 .   ? -1.418  36.308 49.863  1.00 26.99 ? 2607 HOH B O   1 
HETATM 13254 O  O   . HOH EA 6 .   ? -34.550 68.766 42.198  1.00 44.79 ? 2608 HOH B O   1 
HETATM 13255 O  O   . HOH EA 6 .   ? -28.238 47.265 35.241  1.00 19.78 ? 2609 HOH B O   1 
HETATM 13256 O  O   . HOH EA 6 .   ? -33.151 65.791 45.978  1.00 31.04 ? 2610 HOH B O   1 
HETATM 13257 O  O   . HOH EA 6 .   ? 16.518  58.096 58.729  1.00 23.74 ? 2611 HOH B O   1 
HETATM 13258 O  O   . HOH EA 6 .   ? -5.710  85.213 26.440  1.00 28.94 ? 2612 HOH B O   1 
HETATM 13259 O  O   . HOH EA 6 .   ? -0.240  53.105 -6.146  1.00 50.90 ? 2613 HOH B O   1 
HETATM 13260 O  O   . HOH EA 6 .   ? -18.877 61.034 -0.869  1.00 35.74 ? 2614 HOH B O   1 
HETATM 13261 O  O   . HOH EA 6 .   ? -31.954 65.392 19.694  1.00 28.41 ? 2615 HOH B O   1 
HETATM 13262 O  O   . HOH EA 6 .   ? -17.526 52.153 37.689  1.00 24.95 ? 2616 HOH B O   1 
HETATM 13263 O  O   . HOH EA 6 .   ? -17.811 47.758 31.280  1.00 40.82 ? 2617 HOH B O   1 
HETATM 13264 O  O   . HOH EA 6 .   ? 29.175  49.013 18.573  1.00 30.41 ? 2618 HOH B O   1 
HETATM 13265 O  O   . HOH EA 6 .   ? -40.287 55.939 32.751  1.00 18.11 ? 2619 HOH B O   1 
HETATM 13266 O  O   . HOH EA 6 .   ? -19.647 52.252 25.750  1.00 44.68 ? 2620 HOH B O   1 
HETATM 13267 O  O   . HOH EA 6 .   ? -14.819 65.301 -2.915  1.00 24.86 ? 2621 HOH B O   1 
HETATM 13268 O  O   . HOH EA 6 .   ? -26.427 37.880 27.340  1.00 35.62 ? 2622 HOH B O   1 
HETATM 13269 O  O   . HOH EA 6 .   ? -29.861 52.797 43.823  1.00 26.41 ? 2623 HOH B O   1 
HETATM 13270 O  O   . HOH EA 6 .   ? 17.324  41.243 29.754  1.00 27.65 ? 2624 HOH B O   1 
HETATM 13271 O  O   . HOH EA 6 .   ? -20.490 71.682 51.087  1.00 28.64 ? 2625 HOH B O   1 
HETATM 13272 O  O   . HOH EA 6 .   ? -14.027 69.134 22.292  1.00 26.17 ? 2626 HOH B O   1 
HETATM 13273 O  O   . HOH EA 6 .   ? -21.221 79.438 40.732  1.00 30.73 ? 2627 HOH B O   1 
HETATM 13274 O  O   . HOH EA 6 .   ? -36.488 46.820 43.591  1.00 36.69 ? 2628 HOH B O   1 
HETATM 13275 O  O   . HOH EA 6 .   ? 5.544   49.186 30.133  1.00 42.79 ? 2629 HOH B O   1 
HETATM 13276 O  O   . HOH EA 6 .   ? 0.687   56.893 29.343  1.00 23.22 ? 2630 HOH B O   1 
HETATM 13277 O  O   . HOH EA 6 .   ? -17.974 41.912 26.420  1.00 33.19 ? 2631 HOH B O   1 
HETATM 13278 O  O   . HOH EA 6 .   ? -14.381 76.998 48.666  1.00 40.67 ? 2632 HOH B O   1 
HETATM 13279 O  O   . HOH EA 6 .   ? -7.739  60.471 31.298  1.00 28.76 ? 2633 HOH B O   1 
HETATM 13280 O  O   . HOH EA 6 .   ? 20.305  47.710 18.789  1.00 31.23 ? 2634 HOH B O   1 
HETATM 13281 O  O   . HOH EA 6 .   ? -19.002 46.831 47.454  1.00 29.17 ? 2635 HOH B O   1 
HETATM 13282 O  O   . HOH EA 6 .   ? 9.849   45.809 52.866  1.00 30.31 ? 2636 HOH B O   1 
HETATM 13283 O  O   . HOH EA 6 .   ? -22.404 67.247 21.797  1.00 35.93 ? 2637 HOH B O   1 
HETATM 13284 O  O   . HOH EA 6 .   ? -7.322  74.435 -5.981  1.00 38.49 ? 2638 HOH B O   1 
HETATM 13285 O  O   . HOH EA 6 .   ? 11.961  49.438 23.264  1.00 38.64 ? 2639 HOH B O   1 
HETATM 13286 O  O   . HOH EA 6 .   ? -21.877 51.141 53.385  1.00 23.71 ? 2640 HOH B O   1 
HETATM 13287 O  O   . HOH EA 6 .   ? -19.164 55.703 35.530  1.00 33.75 ? 2641 HOH B O   1 
HETATM 13288 O  O   . HOH EA 6 .   ? -21.193 74.989 47.181  1.00 28.53 ? 2642 HOH B O   1 
HETATM 13289 O  O   . HOH EA 6 .   ? -6.396  68.771 -1.107  1.00 22.63 ? 2643 HOH B O   1 
HETATM 13290 O  O   . HOH EA 6 .   ? -5.475  56.021 31.841  1.00 27.99 ? 2644 HOH B O   1 
HETATM 13291 O  O   . HOH EA 6 .   ? 2.284   39.162 50.269  1.00 37.39 ? 2645 HOH B O   1 
HETATM 13292 O  O   . HOH EA 6 .   ? -5.151  79.617 35.775  1.00 21.64 ? 2646 HOH B O   1 
HETATM 13293 O  O   . HOH EA 6 .   ? -22.964 82.719 13.770  1.00 28.60 ? 2647 HOH B O   1 
HETATM 13294 O  O   . HOH EA 6 .   ? -14.546 68.267 33.406  1.00 16.37 ? 2648 HOH B O   1 
HETATM 13295 O  O   . HOH EA 6 .   ? 10.903  48.256 25.119  1.00 29.23 ? 2649 HOH B O   1 
HETATM 13296 O  O   . HOH EA 6 .   ? 5.320   42.407 31.231  1.00 26.85 ? 2650 HOH B O   1 
HETATM 13297 O  O   . HOH EA 6 .   ? -24.744 56.858 24.913  1.00 26.95 ? 2651 HOH B O   1 
HETATM 13298 O  O   . HOH EA 6 .   ? -7.559  58.658 39.680  1.00 26.98 ? 2652 HOH B O   1 
HETATM 13299 O  O   . HOH EA 6 .   ? -1.019  56.695 32.472  1.00 24.20 ? 2653 HOH B O   1 
HETATM 13300 O  O   . HOH EA 6 .   ? -3.949  49.697 43.909  1.00 47.93 ? 2654 HOH B O   1 
HETATM 13301 O  O   . HOH EA 6 .   ? -3.799  52.959 41.719  1.00 46.08 ? 2655 HOH B O   1 
HETATM 13302 O  O   . HOH EA 6 .   ? -37.428 49.440 45.096  1.00 34.95 ? 2656 HOH B O   1 
HETATM 13303 O  O   . HOH EA 6 .   ? -8.123  78.746 36.822  1.00 25.88 ? 2657 HOH B O   1 
HETATM 13304 O  O   . HOH EA 6 .   ? 19.119  59.233 21.767  1.00 41.57 ? 2658 HOH B O   1 
HETATM 13305 O  O   . HOH EA 6 .   ? -28.743 81.842 11.143  1.00 28.46 ? 2659 HOH B O   1 
HETATM 13306 O  O   . HOH EA 6 .   ? -15.902 65.936 34.332  1.00 22.90 ? 2660 HOH B O   1 
HETATM 13307 O  O   . HOH EA 6 .   ? -30.244 70.597 11.365  1.00 30.96 ? 2661 HOH B O   1 
HETATM 13308 O  O   . HOH EA 6 .   ? 8.734   37.956 47.027  1.00 32.60 ? 2662 HOH B O   1 
HETATM 13309 O  O   . HOH EA 6 .   ? -37.583 72.851 25.462  1.00 35.08 ? 2663 HOH B O   1 
HETATM 13310 O  O   . HOH EA 6 .   ? -23.442 66.587 48.602  1.00 30.09 ? 2664 HOH B O   1 
HETATM 13311 O  O   . HOH EA 6 .   ? -9.704  59.500 24.028  1.00 29.83 ? 2665 HOH B O   1 
HETATM 13312 O  O   . HOH EA 6 .   ? -14.293 64.519 -9.665  1.00 29.78 ? 2666 HOH B O   1 
HETATM 13313 O  O   . HOH EA 6 .   ? 3.493   84.428 25.080  1.00 35.04 ? 2667 HOH B O   1 
HETATM 13314 O  O   . HOH EA 6 .   ? -11.867 64.208 17.574  1.00 53.12 ? 2668 HOH B O   1 
HETATM 13315 O  O   . HOH EA 6 .   ? -33.141 36.494 28.633  1.00 45.86 ? 2669 HOH B O   1 
HETATM 13316 O  O   . HOH EA 6 .   ? -27.803 58.308 21.500  1.00 31.82 ? 2670 HOH B O   1 
HETATM 13317 O  O   . HOH EA 6 .   ? 0.424   69.418 56.039  1.00 37.57 ? 2671 HOH B O   1 
HETATM 13318 O  O   . HOH EA 6 .   ? 7.284   53.017 28.698  1.00 27.24 ? 2672 HOH B O   1 
HETATM 13319 O  O   . HOH EA 6 .   ? -29.676 47.007 37.167  1.00 18.42 ? 2673 HOH B O   1 
HETATM 13320 O  O   . HOH EA 6 .   ? -28.173 41.717 10.823  1.00 42.68 ? 2674 HOH B O   1 
HETATM 13321 O  O   . HOH EA 6 .   ? 11.090  78.144 26.109  1.00 35.60 ? 2675 HOH B O   1 
HETATM 13322 O  O   . HOH EA 6 .   ? -15.013 73.190 -12.067 1.00 38.57 ? 2676 HOH B O   1 
HETATM 13323 O  O   . HOH EA 6 .   ? 0.020   78.615 15.989  1.00 22.37 ? 2677 HOH B O   1 
HETATM 13324 O  O   . HOH EA 6 .   ? -21.204 48.686 26.005  1.00 30.62 ? 2678 HOH B O   1 
HETATM 13325 O  O   . HOH EA 6 .   ? -27.010 67.688 12.878  1.00 38.12 ? 2679 HOH B O   1 
HETATM 13326 O  O   . HOH EA 6 .   ? -10.944 49.768 47.086  1.00 30.79 ? 2680 HOH B O   1 
HETATM 13327 O  O   . HOH EA 6 .   ? 11.685  34.818 49.107  1.00 43.24 ? 2681 HOH B O   1 
HETATM 13328 O  O   . HOH EA 6 .   ? 19.093  60.660 28.322  1.00 25.45 ? 2682 HOH B O   1 
HETATM 13329 O  O   . HOH EA 6 .   ? -3.627  82.843 12.874  1.00 35.31 ? 2683 HOH B O   1 
HETATM 13330 O  O   . HOH EA 6 .   ? -22.987 68.483 53.762  1.00 34.40 ? 2684 HOH B O   1 
HETATM 13331 O  O   . HOH EA 6 .   ? -25.105 78.121 6.921   1.00 28.91 ? 2685 HOH B O   1 
HETATM 13332 O  O   . HOH EA 6 .   ? -24.068 57.864 27.539  1.00 28.98 ? 2686 HOH B O   1 
HETATM 13333 O  O   . HOH EA 6 .   ? -19.297 57.815 2.140   1.00 25.57 ? 2687 HOH B O   1 
HETATM 13334 O  O   . HOH EA 6 .   ? 12.842  47.430 39.221  1.00 14.69 ? 2688 HOH B O   1 
HETATM 13335 O  O   . HOH EA 6 .   ? 3.566   60.678 60.946  1.00 25.38 ? 2689 HOH B O   1 
HETATM 13336 O  O   . HOH EA 6 .   ? -8.405  65.008 51.717  1.00 18.23 ? 2690 HOH B O   1 
HETATM 13337 O  O   . HOH EA 6 .   ? -23.641 65.867 45.967  1.00 21.93 ? 2691 HOH B O   1 
HETATM 13338 O  O   . HOH EA 6 .   ? -8.625  70.620 30.637  1.00 25.30 ? 2692 HOH B O   1 
HETATM 13339 O  O   . HOH EA 6 .   ? 5.761   64.490 18.966  1.00 25.48 ? 2693 HOH B O   1 
HETATM 13340 O  O   . HOH EA 6 .   ? -12.861 89.084 17.868  1.00 29.62 ? 2694 HOH B O   1 
HETATM 13341 O  O   . HOH EA 6 .   ? -38.850 54.300 34.798  1.00 19.59 ? 2695 HOH B O   1 
HETATM 13342 O  O   . HOH EA 6 .   ? -17.748 80.090 27.408  1.00 22.10 ? 2696 HOH B O   1 
HETATM 13343 O  O   . HOH EA 6 .   ? -16.975 60.447 12.829  1.00 32.66 ? 2697 HOH B O   1 
HETATM 13344 O  O   . HOH EA 6 .   ? -10.931 71.327 27.266  1.00 27.95 ? 2698 HOH B O   1 
HETATM 13345 O  O   . HOH EA 6 .   ? -39.497 50.320 43.742  1.00 42.22 ? 2699 HOH B O   1 
HETATM 13346 O  O   . HOH EA 6 .   ? -33.571 74.920 19.600  1.00 19.81 ? 2700 HOH B O   1 
HETATM 13347 O  O   . HOH EA 6 .   ? -5.007  83.669 14.773  1.00 32.19 ? 2701 HOH B O   1 
HETATM 13348 O  O   . HOH EA 6 .   ? -18.811 72.787 53.517  1.00 39.46 ? 2702 HOH B O   1 
HETATM 13349 O  O   . HOH EA 6 .   ? -35.095 51.982 33.164  1.00 22.79 ? 2703 HOH B O   1 
HETATM 13350 O  O   . HOH EA 6 .   ? 6.042   36.626 43.846  1.00 28.63 ? 2704 HOH B O   1 
HETATM 13351 O  O   . HOH EA 6 .   ? -10.816 62.176 37.942  1.00 22.94 ? 2705 HOH B O   1 
HETATM 13352 O  O   . HOH EA 6 .   ? 17.161  68.457 51.867  1.00 25.84 ? 2706 HOH B O   1 
HETATM 13353 O  O   . HOH EA 6 .   ? -0.589  35.064 47.531  1.00 36.41 ? 2707 HOH B O   1 
HETATM 13354 O  O   . HOH EA 6 .   ? -29.809 52.264 46.644  1.00 37.20 ? 2708 HOH B O   1 
HETATM 13355 O  O   . HOH EA 6 .   ? -19.317 74.060 34.506  1.00 29.16 ? 2709 HOH B O   1 
HETATM 13356 O  O   . HOH EA 6 .   ? -17.350 77.464 39.479  1.00 29.13 ? 2710 HOH B O   1 
HETATM 13357 O  O   . HOH EA 6 .   ? -6.243  70.764 0.319   1.00 31.31 ? 2711 HOH B O   1 
HETATM 13358 O  O   . HOH EA 6 .   ? 6.319   39.743 53.559  1.00 34.88 ? 2712 HOH B O   1 
HETATM 13359 O  O   . HOH EA 6 .   ? 11.211  48.141 50.386  1.00 35.42 ? 2713 HOH B O   1 
HETATM 13360 O  O   . HOH EA 6 .   ? -36.713 76.666 29.434  1.00 30.35 ? 2714 HOH B O   1 
HETATM 13361 O  O   . HOH EA 6 .   ? -10.898 75.319 33.170  1.00 27.49 ? 2715 HOH B O   1 
HETATM 13362 O  O   . HOH EA 6 .   ? 2.681   83.659 28.622  1.00 36.38 ? 2716 HOH B O   1 
HETATM 13363 O  O   . HOH EA 6 .   ? -42.794 54.640 32.657  1.00 26.61 ? 2717 HOH B O   1 
HETATM 13364 O  O   . HOH EA 6 .   ? 6.182   73.306 9.101   1.00 26.09 ? 2718 HOH B O   1 
HETATM 13365 O  O   . HOH EA 6 .   ? -29.005 38.962 24.414  1.00 30.68 ? 2719 HOH B O   1 
HETATM 13366 O  O   . HOH EA 6 .   ? -31.487 61.468 20.158  1.00 31.08 ? 2720 HOH B O   1 
HETATM 13367 O  O   . HOH EA 6 .   ? -41.215 58.407 33.449  1.00 22.75 ? 2721 HOH B O   1 
HETATM 13368 O  O   . HOH EA 6 .   ? -28.856 79.464 40.503  1.00 36.00 ? 2722 HOH B O   1 
HETATM 13369 O  O   . HOH EA 6 .   ? 9.581   48.018 31.493  1.00 24.08 ? 2723 HOH B O   1 
HETATM 13370 O  O   . HOH EA 6 .   ? -9.347  73.856 31.827  1.00 21.55 ? 2724 HOH B O   1 
HETATM 13371 O  O   . HOH EA 6 .   ? -10.495 35.295 58.209  1.00 33.36 ? 2725 HOH B O   1 
HETATM 13372 O  O   . HOH EA 6 .   ? -14.431 58.667 40.468  1.00 31.28 ? 2726 HOH B O   1 
HETATM 13373 O  O   . HOH EA 6 .   ? 1.629   82.632 46.785  1.00 25.60 ? 2727 HOH B O   1 
HETATM 13374 O  O   . HOH EA 6 .   ? -5.204  50.359 48.453  1.00 22.89 ? 2728 HOH B O   1 
HETATM 13375 O  O   . HOH EA 6 .   ? -35.648 59.041 43.201  1.00 25.19 ? 2729 HOH B O   1 
HETATM 13376 O  O   . HOH EA 6 .   ? -11.371 47.180 47.608  1.00 25.66 ? 2730 HOH B O   1 
HETATM 13377 O  O   . HOH EA 6 .   ? 9.492   71.978 21.041  1.00 31.09 ? 2731 HOH B O   1 
HETATM 13378 O  O   . HOH EA 6 .   ? -25.951 77.760 9.780   1.00 29.97 ? 2732 HOH B O   1 
HETATM 13379 O  O   . HOH EA 6 .   ? -18.658 71.666 42.032  1.00 24.81 ? 2733 HOH B O   1 
HETATM 13380 O  O   . HOH EA 6 .   ? 5.444   82.660 25.862  1.00 37.05 ? 2734 HOH B O   1 
HETATM 13381 O  O   . HOH EA 6 .   ? -20.563 63.950 3.277   1.00 47.97 ? 2735 HOH B O   1 
HETATM 13382 O  O   . HOH EA 6 .   ? 13.468  77.042 44.224  1.00 32.66 ? 2736 HOH B O   1 
HETATM 13383 O  O   . HOH EA 6 .   ? -28.294 62.412 22.033  1.00 25.74 ? 2737 HOH B O   1 
HETATM 13384 O  O   . HOH EA 6 .   ? -36.429 75.962 35.272  1.00 32.70 ? 2738 HOH B O   1 
HETATM 13385 O  O   . HOH EA 6 .   ? -17.852 44.673 20.415  1.00 41.16 ? 2739 HOH B O   1 
HETATM 13386 O  O   . HOH EA 6 .   ? -18.314 75.212 32.161  1.00 27.18 ? 2740 HOH B O   1 
HETATM 13387 O  O   . HOH EA 6 .   ? -13.880 63.123 18.721  1.00 35.85 ? 2741 HOH B O   1 
HETATM 13388 O  O   . HOH EA 6 .   ? -17.229 38.329 56.911  1.00 34.37 ? 2742 HOH B O   1 
HETATM 13389 O  O   . HOH EA 6 .   ? -21.416 89.518 23.157  1.00 40.54 ? 2743 HOH B O   1 
HETATM 13390 O  O   . HOH EA 6 .   ? -38.262 58.192 39.573  1.00 25.51 ? 2744 HOH B O   1 
HETATM 13391 O  O   . HOH EA 6 .   ? -15.024 88.965 25.759  1.00 42.55 ? 2745 HOH B O   1 
HETATM 13392 O  O   . HOH EA 6 .   ? -7.205  40.437 39.685  1.00 37.54 ? 2746 HOH B O   1 
HETATM 13393 O  O   . HOH EA 6 .   ? -10.607 65.054 20.206  1.00 25.06 ? 2747 HOH B O   1 
HETATM 13394 O  O   . HOH EA 6 .   ? 19.917  57.715 58.694  1.00 31.24 ? 2748 HOH B O   1 
HETATM 13395 O  O   . HOH EA 6 .   ? -24.805 80.390 37.710  1.00 29.54 ? 2749 HOH B O   1 
HETATM 13396 O  O   . HOH EA 6 .   ? -18.848 36.186 36.108  1.00 24.68 ? 2750 HOH B O   1 
HETATM 13397 O  O   . HOH EA 6 .   ? -1.278  56.345 37.047  1.00 36.52 ? 2751 HOH B O   1 
HETATM 13398 O  O   . HOH EA 6 .   ? -17.700 87.129 11.018  1.00 44.28 ? 2752 HOH B O   1 
HETATM 13399 O  O   . HOH EA 6 .   ? -13.136 56.134 43.635  1.00 22.73 ? 2753 HOH B O   1 
HETATM 13400 O  O   . HOH EA 6 .   ? -29.953 70.467 51.010  1.00 37.79 ? 2754 HOH B O   1 
HETATM 13401 O  O   . HOH EA 6 .   ? -18.236 64.564 35.417  1.00 37.05 ? 2755 HOH B O   1 
HETATM 13402 O  O   . HOH EA 6 .   ? -35.867 69.689 37.408  1.00 28.93 ? 2756 HOH B O   1 
HETATM 13403 O  O   . HOH EA 6 .   ? -18.385 75.611 28.703  1.00 25.52 ? 2757 HOH B O   1 
HETATM 13404 O  O   . HOH EA 6 .   ? -39.107 46.884 33.504  1.00 28.12 ? 2758 HOH B O   1 
HETATM 13405 O  O   . HOH EA 6 .   ? 10.807  76.713 37.996  1.00 33.43 ? 2759 HOH B O   1 
HETATM 13406 O  O   . HOH EA 6 .   ? -23.608 62.345 4.199   1.00 38.10 ? 2760 HOH B O   1 
HETATM 13407 O  O   . HOH EA 6 .   ? -26.983 55.971 44.700  1.00 28.41 ? 2761 HOH B O   1 
HETATM 13408 O  O   . HOH EA 6 .   ? -33.050 68.401 45.527  1.00 42.28 ? 2762 HOH B O   1 
HETATM 13409 O  O   . HOH EA 6 .   ? 15.924  53.085 58.304  1.00 32.62 ? 2763 HOH B O   1 
HETATM 13410 O  O   . HOH EA 6 .   ? -39.946 61.978 33.180  1.00 33.45 ? 2764 HOH B O   1 
HETATM 13411 O  O   . HOH EA 6 .   ? -43.562 62.779 26.573  1.00 34.88 ? 2765 HOH B O   1 
HETATM 13412 O  O   . HOH EA 6 .   ? -18.808 68.066 33.582  1.00 41.96 ? 2766 HOH B O   1 
HETATM 13413 O  O   . HOH EA 6 .   ? 2.719   86.609 36.611  1.00 28.55 ? 2767 HOH B O   1 
HETATM 13414 O  O   . HOH EA 6 .   ? -21.789 69.132 -0.537  1.00 31.94 ? 2768 HOH B O   1 
HETATM 13415 O  O   . HOH EA 6 .   ? 4.288   85.982 22.950  1.00 48.67 ? 2769 HOH B O   1 
HETATM 13416 O  O   . HOH EA 6 .   ? -1.383  80.936 16.705  1.00 26.12 ? 2770 HOH B O   1 
HETATM 13417 O  O   . HOH EA 6 .   ? -9.236  75.800 -8.009  1.00 43.57 ? 2771 HOH B O   1 
HETATM 13418 O  O   . HOH EA 6 .   ? -19.450 88.116 24.288  1.00 32.62 ? 2772 HOH B O   1 
HETATM 13419 O  O   . HOH EA 6 .   ? -26.215 38.479 24.822  1.00 27.32 ? 2773 HOH B O   1 
HETATM 13420 O  O   . HOH EA 6 .   ? -12.227 83.798 11.630  1.00 33.62 ? 2774 HOH B O   1 
HETATM 13421 O  O   . HOH EA 6 .   ? -12.368 54.474 45.819  1.00 28.86 ? 2775 HOH B O   1 
HETATM 13422 O  O   . HOH EA 6 .   ? -5.008  86.938 28.342  1.00 31.61 ? 2776 HOH B O   1 
HETATM 13423 O  O   . HOH EA 6 .   ? -0.716  76.276 15.098  1.00 20.42 ? 2777 HOH B O   1 
HETATM 13424 O  O   . HOH EA 6 .   ? -14.407 85.247 17.127  1.00 26.04 ? 2778 HOH B O   1 
HETATM 13425 O  O   . HOH EA 6 .   ? -10.360 76.994 34.952  1.00 34.88 ? 2779 HOH B O   1 
HETATM 13426 O  O   . HOH EA 6 .   ? 2.440   63.166 20.352  1.00 36.66 ? 2780 HOH B O   1 
HETATM 13427 O  O   . HOH EA 6 .   ? -37.682 55.858 40.586  1.00 25.01 ? 2781 HOH B O   1 
HETATM 13428 O  O   . HOH EA 6 .   ? -22.949 80.733 31.573  1.00 32.31 ? 2782 HOH B O   1 
HETATM 13429 O  O   . HOH EA 6 .   ? 16.650  59.702 32.266  1.00 27.01 ? 2783 HOH B O   1 
HETATM 13430 O  O   . HOH EA 6 .   ? -28.122 69.177 15.174  1.00 26.74 ? 2784 HOH B O   1 
HETATM 13431 O  O   . HOH EA 6 .   ? -16.515 46.169 47.726  1.00 36.30 ? 2785 HOH B O   1 
HETATM 13432 O  O   . HOH EA 6 .   ? 10.694  75.480 48.042  1.00 24.89 ? 2786 HOH B O   1 
HETATM 13433 O  O   . HOH EA 6 .   ? 13.451  57.640 58.262  1.00 29.48 ? 2787 HOH B O   1 
HETATM 13434 O  O   . HOH EA 6 .   ? -37.043 60.194 41.286  1.00 34.47 ? 2788 HOH B O   1 
HETATM 13435 O  O   . HOH EA 6 .   ? 12.737  69.794 56.132  1.00 41.15 ? 2789 HOH B O   1 
HETATM 13436 O  O   . HOH EA 6 .   ? -9.405  72.858 29.098  1.00 22.16 ? 2790 HOH B O   1 
HETATM 13437 O  O   . HOH EA 6 .   ? -34.324 69.524 39.652  1.00 32.83 ? 2791 HOH B O   1 
HETATM 13438 O  O   . HOH EA 6 .   ? -43.585 52.967 30.719  1.00 23.52 ? 2792 HOH B O   1 
HETATM 13439 O  O   . HOH EA 6 .   ? 9.706   47.606 28.938  1.00 23.64 ? 2793 HOH B O   1 
HETATM 13440 O  O   . HOH EA 6 .   ? -28.989 60.544 20.046  1.00 39.56 ? 2794 HOH B O   1 
HETATM 13441 O  O   . HOH EA 6 .   ? -24.937 37.296 40.107  1.00 36.74 ? 2795 HOH B O   1 
HETATM 13442 O  O   . HOH EA 6 .   ? -33.631 44.498 31.891  1.00 35.41 ? 2796 HOH B O   1 
HETATM 13443 O  O   . HOH EA 6 .   ? -1.728  34.081 51.270  1.00 33.32 ? 2797 HOH B O   1 
HETATM 13444 O  O   . HOH EA 6 .   ? -6.603  55.899 22.580  1.00 32.36 ? 2798 HOH B O   1 
HETATM 13445 O  O   . HOH EA 6 .   ? -23.885 41.231 44.072  1.00 21.83 ? 2799 HOH B O   1 
HETATM 13446 O  O   . HOH EA 6 .   ? -1.012  82.412 18.977  1.00 32.83 ? 2800 HOH B O   1 
HETATM 13447 O  O   . HOH EA 6 .   ? -8.128  57.685 30.612  1.00 42.26 ? 2802 HOH B O   1 
HETATM 13448 O  O   . HOH EA 6 .   ? -1.579  51.801 36.892  1.00 28.79 ? 2803 HOH B O   1 
HETATM 13449 O  O   . HOH EA 6 .   ? -32.959 77.137 12.390  1.00 42.99 ? 2804 HOH B O   1 
HETATM 13450 O  O   . HOH EA 6 .   ? -41.078 59.116 39.337  1.00 37.08 ? 2805 HOH B O   1 
HETATM 13451 O  O   . HOH EA 6 .   ? -13.053 34.151 37.509  1.00 41.48 ? 2806 HOH B O   1 
HETATM 13452 O  O   . HOH EA 6 .   ? 21.951  53.637 19.508  1.00 38.39 ? 2807 HOH B O   1 
HETATM 13453 O  O   . HOH EA 6 .   ? -15.227 64.258 36.252  1.00 32.66 ? 2808 HOH B O   1 
HETATM 13454 O  O   . HOH EA 6 .   ? -33.461 60.927 46.961  1.00 39.14 ? 2809 HOH B O   1 
HETATM 13455 O  O   . HOH EA 6 .   ? -20.309 65.576 13.689  1.00 33.73 ? 2810 HOH B O   1 
HETATM 13456 O  O   . HOH EA 6 .   ? -7.017  78.950 40.108  1.00 33.94 ? 2811 HOH B O   1 
HETATM 13457 O  O   . HOH EA 6 .   ? 18.175  53.879 19.768  1.00 32.47 ? 2812 HOH B O   1 
HETATM 13458 O  O   . HOH EA 6 .   ? -20.284 37.556 45.430  1.00 36.29 ? 2813 HOH B O   1 
HETATM 13459 O  O   . HOH EA 6 .   ? 8.695   75.779 13.187  1.00 28.09 ? 2814 HOH B O   1 
HETATM 13460 O  O   . HOH EA 6 .   ? -14.819 84.199 11.089  1.00 42.56 ? 2815 HOH B O   1 
HETATM 13461 O  O   . HOH EA 6 .   ? -28.040 64.533 20.238  1.00 32.38 ? 2816 HOH B O   1 
HETATM 13462 O  O   . HOH EA 6 .   ? 8.060   54.891 61.906  1.00 31.30 ? 2817 HOH B O   1 
HETATM 13463 O  O   . HOH EA 6 .   ? -17.145 47.410 39.068  1.00 31.30 ? 2818 HOH B O   1 
HETATM 13464 O  O   . HOH EA 6 .   ? -26.417 59.054 23.783  1.00 33.18 ? 2819 HOH B O   1 
HETATM 13465 O  O   . HOH EA 6 .   ? -1.523  57.040 64.994  1.00 34.78 ? 2820 HOH B O   1 
HETATM 13466 O  O   . HOH EA 6 .   ? -8.498  42.942 39.696  1.00 34.36 ? 2821 HOH B O   1 
HETATM 13467 O  O   . HOH EA 6 .   ? 7.781   73.792 50.016  1.00 45.44 ? 2822 HOH B O   1 
HETATM 13468 O  O   . HOH EA 6 .   ? -23.437 54.812 23.606  1.00 41.09 ? 2823 HOH B O   1 
HETATM 13469 O  O   . HOH EA 6 .   ? -17.629 63.377 -1.377  1.00 31.74 ? 2824 HOH B O   1 
HETATM 13470 O  O   . HOH EA 6 .   ? -23.676 62.184 12.259  1.00 29.65 ? 2825 HOH B O   1 
HETATM 13471 O  O   . HOH EA 6 .   ? -11.713 60.375 32.121  1.00 43.45 ? 2826 HOH B O   1 
HETATM 13472 O  O   . HOH EA 6 .   ? -17.892 44.277 34.704  1.00 29.75 ? 2827 HOH B O   1 
HETATM 13473 O  O   . HOH EA 6 .   ? -16.465 60.346 38.362  1.00 49.88 ? 2828 HOH B O   1 
HETATM 13474 O  O   . HOH EA 6 .   ? -38.337 61.564 21.126  1.00 46.72 ? 2829 HOH B O   1 
HETATM 13475 O  O   . HOH EA 6 .   ? 17.684  69.624 49.509  1.00 38.36 ? 2830 HOH B O   1 
HETATM 13476 O  O   . HOH EA 6 .   ? -33.742 66.923 38.294  1.00 28.49 ? 2831 HOH B O   1 
HETATM 13477 O  O   . HOH EA 6 .   ? -5.795  86.376 14.011  1.00 29.33 ? 2832 HOH B O   1 
HETATM 13478 O  O   . HOH EA 6 .   ? -29.834 86.788 27.712  1.00 40.12 ? 2833 HOH B O   1 
HETATM 13479 O  O   . HOH EA 6 .   ? 23.099  66.379 55.843  1.00 34.10 ? 2834 HOH B O   1 
HETATM 13480 O  O   . HOH EA 6 .   ? -14.302 60.291 -5.054  1.00 35.72 ? 2835 HOH B O   1 
HETATM 13481 O  O   . HOH EA 6 .   ? -9.405  60.461 33.409  1.00 39.19 ? 2836 HOH B O   1 
HETATM 13482 O  O   . HOH EA 6 .   ? -1.014  42.966 15.048  1.00 36.87 ? 2837 HOH B O   1 
HETATM 13483 O  O   . HOH EA 6 .   ? -15.451 31.853 56.366  1.00 38.50 ? 2838 HOH B O   1 
HETATM 13484 O  O   . HOH EA 6 .   ? -15.287 65.736 20.104  1.00 44.80 ? 2839 HOH B O   1 
HETATM 13485 O  O   . HOH EA 6 .   ? 19.583  57.238 20.121  1.00 41.75 ? 2840 HOH B O   1 
HETATM 13486 O  O   . HOH EA 6 .   ? 16.460  67.717 45.903  1.00 28.67 ? 2841 HOH B O   1 
HETATM 13487 O  O   . HOH EA 6 .   ? -27.360 75.639 10.528  1.00 22.53 ? 2842 HOH B O   1 
HETATM 13488 O  O   . HOH EA 6 .   ? -17.325 73.674 25.855  1.00 22.89 ? 2843 HOH B O   1 
HETATM 13489 O  O   . HOH EA 6 .   ? 5.064   51.866 30.157  1.00 34.41 ? 2844 HOH B O   1 
HETATM 13490 O  O   . HOH EA 6 .   ? -12.721 61.948 -9.157  1.00 32.84 ? 2845 HOH B O   1 
HETATM 13491 O  O   . HOH EA 6 .   ? 4.251   47.210 63.590  1.00 28.70 ? 2846 HOH B O   1 
HETATM 13492 O  O   . HOH EA 6 .   ? 1.935   83.242 30.861  1.00 35.43 ? 2847 HOH B O   1 
HETATM 13493 O  O   . HOH EA 6 .   ? -35.641 78.617 27.927  1.00 33.18 ? 2848 HOH B O   1 
HETATM 13494 O  O   . HOH EA 6 .   ? -18.648 46.190 29.352  1.00 30.80 ? 2849 HOH B O   1 
HETATM 13495 O  O   . HOH EA 6 .   ? 16.215  42.763 21.191  1.00 44.59 ? 2850 HOH B O   1 
HETATM 13496 O  O   . HOH EA 6 .   ? -37.178 60.054 24.128  1.00 42.25 ? 2851 HOH B O   1 
HETATM 13497 O  O   . HOH EA 6 .   ? 6.879   74.686 42.403  1.00 17.92 ? 2852 HOH B O   1 
HETATM 13498 O  O   . HOH EA 6 .   ? -12.271 67.217 26.843  1.00 25.89 ? 2853 HOH B O   1 
HETATM 13499 O  O   . HOH EA 6 .   ? -14.983 79.540 39.647  1.00 32.89 ? 2854 HOH B O   1 
HETATM 13500 O  O   . HOH EA 6 .   ? 21.793  38.432 28.847  1.00 29.01 ? 2855 HOH B O   1 
HETATM 13501 O  O   . HOH EA 6 .   ? -33.782 70.918 23.491  1.00 25.72 ? 2856 HOH B O   1 
HETATM 13502 O  O   . HOH EA 6 .   ? 10.731  55.613 61.446  1.00 26.85 ? 2857 HOH B O   1 
HETATM 13503 O  O   . HOH EA 6 .   ? -3.568  52.812 24.096  1.00 34.59 ? 2858 HOH B O   1 
HETATM 13504 O  O   . HOH EA 6 .   ? -13.528 89.238 21.918  1.00 24.52 ? 2859 HOH B O   1 
HETATM 13505 O  O   . HOH EA 6 .   ? -36.757 56.295 42.941  1.00 33.72 ? 2860 HOH B O   1 
HETATM 13506 O  O   . HOH EA 6 .   ? 24.128  63.406 56.047  1.00 24.15 ? 2861 HOH B O   1 
HETATM 13507 O  O   . HOH EA 6 .   ? -39.446 51.551 34.093  1.00 35.14 ? 2862 HOH B O   1 
HETATM 13508 O  O   . HOH EA 6 .   ? -21.599 57.072 1.013   1.00 37.07 ? 2864 HOH B O   1 
HETATM 13509 O  O   . HOH EA 6 .   ? -33.584 45.374 34.458  1.00 33.34 ? 2865 HOH B O   1 
HETATM 13510 O  O   . HOH EA 6 .   ? 9.237   65.604 10.299  1.00 29.69 ? 2866 HOH B O   1 
HETATM 13511 O  O   . HOH EA 6 .   ? -0.671  83.164 21.790  1.00 33.41 ? 2867 HOH B O   1 
HETATM 13512 O  O   . HOH EA 6 .   ? -23.236 51.439 49.269  1.00 31.91 ? 2868 HOH B O   1 
HETATM 13513 O  O   . HOH EA 6 .   ? -16.578 63.763 -3.869  1.00 33.89 ? 2869 HOH B O   1 
HETATM 13514 O  O   . HOH EA 6 .   ? -19.207 78.529 34.526  1.00 27.59 ? 2870 HOH B O   1 
HETATM 13515 O  O   . HOH EA 6 .   ? -23.776 54.806 52.544  1.00 41.39 ? 2871 HOH B O   1 
HETATM 13516 O  O   . HOH EA 6 .   ? -9.078  58.843 35.517  1.00 37.85 ? 2872 HOH B O   1 
HETATM 13517 O  O   . HOH EA 6 .   ? -24.931 34.115 33.764  1.00 39.35 ? 2873 HOH B O   1 
HETATM 13518 O  O   . HOH EA 6 .   ? -40.270 46.876 25.363  1.00 30.45 ? 2874 HOH B O   1 
HETATM 13519 O  O   . HOH EA 6 .   ? -46.028 63.516 27.526  1.00 34.85 ? 2875 HOH B O   1 
HETATM 13520 O  O   . HOH EA 6 .   ? -5.617  50.509 4.106   1.00 30.10 ? 2876 HOH B O   1 
HETATM 13521 O  O   . HOH EA 6 .   ? -14.103 47.347 39.348  1.00 36.49 ? 2877 HOH B O   1 
HETATM 13522 O  O   . HOH EA 6 .   ? 12.637  78.306 36.294  1.00 39.70 ? 2878 HOH B O   1 
HETATM 13523 O  O   . HOH EA 6 .   ? -21.515 34.957 34.465  1.00 43.20 ? 2879 HOH B O   1 
HETATM 13524 O  O   . HOH EA 6 .   ? -15.847 78.816 47.935  1.00 35.96 ? 2880 HOH B O   1 
HETATM 13525 O  O   . HOH EA 6 .   ? 8.117   78.853 35.039  1.00 35.90 ? 2881 HOH B O   1 
HETATM 13526 O  O   . HOH EA 6 .   ? -35.184 65.633 40.295  1.00 44.06 ? 2882 HOH B O   1 
HETATM 13527 O  O   . HOH EA 6 .   ? -42.341 62.934 37.677  1.00 38.39 ? 2883 HOH B O   1 
HETATM 13528 O  O   . HOH EA 6 .   ? -0.747  58.861 2.539   1.00 43.49 ? 2884 HOH B O   1 
HETATM 13529 O  O   . HOH EA 6 .   ? -16.199 85.548 13.106  1.00 41.74 ? 2885 HOH B O   1 
HETATM 13530 O  O   . HOH EA 6 .   ? -43.527 65.370 26.045  1.00 30.08 ? 2886 HOH B O   1 
HETATM 13531 O  O   . HOH EA 6 .   ? -4.395  84.877 30.109  1.00 36.61 ? 2887 HOH B O   1 
HETATM 13532 O  O   . HOH EA 6 .   ? 6.901   40.698 57.465  1.00 39.78 ? 2888 HOH B O   1 
HETATM 13533 O  O   . HOH EA 6 .   ? 6.150   38.205 37.121  1.00 32.02 ? 2889 HOH B O   1 
HETATM 13534 O  O   . HOH EA 6 .   ? -2.111  48.539 36.093  1.00 34.73 ? 2890 HOH B O   1 
HETATM 13535 O  O   . HOH EA 6 .   ? -41.024 48.894 34.656  1.00 43.42 ? 2891 HOH B O   1 
HETATM 13536 O  O   . HOH EA 6 .   ? -27.605 67.737 17.847  1.00 38.83 ? 2892 HOH B O   1 
HETATM 13537 O  O   . HOH EA 6 .   ? 12.920  55.698 59.707  1.00 34.97 ? 2893 HOH B O   1 
HETATM 13538 O  O   . HOH EA 6 .   ? -34.861 70.683 17.220  1.00 25.13 ? 2894 HOH B O   1 
HETATM 13539 O  O   . HOH EA 6 .   ? 4.704   59.187 13.073  1.00 36.35 ? 2895 HOH B O   1 
HETATM 13540 O  O   . HOH EA 6 .   ? -2.612  55.849 34.813  1.00 43.61 ? 2896 HOH B O   1 
HETATM 13541 O  O   . HOH EA 6 .   ? -8.365  81.988 40.964  1.00 38.12 ? 2897 HOH B O   1 
HETATM 13542 O  O   . HOH EA 6 .   ? -20.620 50.424 49.273  1.00 39.70 ? 2898 HOH B O   1 
HETATM 13543 O  O   . HOH EA 6 .   ? 3.634   51.188 32.386  1.00 40.78 ? 2899 HOH B O   1 
HETATM 13544 O  O   . HOH EA 6 .   ? -32.465 62.986 48.742  1.00 44.71 ? 2900 HOH B O   1 
HETATM 13545 O  O   . HOH EA 6 .   ? -3.231  73.426 3.853   1.00 38.98 ? 2901 HOH B O   1 
HETATM 13546 O  O   . HOH EA 6 .   ? -5.476  46.455 39.424  1.00 39.24 ? 2902 HOH B O   1 
HETATM 13547 O  O   . HOH EA 6 .   ? 11.140  63.095 19.690  1.00 34.85 ? 2903 HOH B O   1 
HETATM 13548 O  O   . HOH EA 6 .   ? 0.248   35.803 35.089  1.00 41.34 ? 2904 HOH B O   1 
HETATM 13549 O  O   . HOH EA 6 .   ? -17.249 36.222 52.159  1.00 40.05 ? 2905 HOH B O   1 
HETATM 13550 O  O   . HOH EA 6 .   ? -11.181 41.140 36.433  1.00 33.39 ? 2906 HOH B O   1 
HETATM 13551 O  O   . HOH EA 6 .   ? -1.118  50.647 7.253   1.00 45.27 ? 2907 HOH B O   1 
HETATM 13552 O  O   . HOH EA 6 .   ? -10.614 39.331 60.238  1.00 36.73 ? 2908 HOH B O   1 
HETATM 13553 O  O   . HOH EA 6 .   ? -18.264 88.353 13.889  1.00 42.77 ? 2909 HOH B O   1 
HETATM 13554 O  O   . HOH EA 6 .   ? -7.145  51.054 0.872   1.00 48.20 ? 2910 HOH B O   1 
HETATM 13555 O  O   . HOH EA 6 .   ? -17.277 62.431 36.264  1.00 30.30 ? 2911 HOH B O   1 
HETATM 13556 O  O   . HOH EA 6 .   ? 19.145  37.728 29.560  1.00 31.94 ? 2912 HOH B O   1 
HETATM 13557 O  O   . HOH EA 6 .   ? -25.330 36.335 32.475  1.00 30.82 ? 2913 HOH B O   1 
HETATM 13558 O  O   . HOH EA 6 .   ? -11.006 24.144 58.211  1.00 39.65 ? 2914 HOH B O   1 
HETATM 13559 O  O   . HOH EA 6 .   ? 6.875   81.417 30.098  1.00 41.84 ? 2915 HOH B O   1 
HETATM 13560 O  O   . HOH EA 6 .   ? -20.835 84.553 32.119  1.00 37.74 ? 2916 HOH B O   1 
HETATM 13561 O  O   . HOH EA 6 .   ? 6.702   65.279 9.498   1.00 33.48 ? 2917 HOH B O   1 
HETATM 13562 O  O   . HOH EA 6 .   ? -23.077 83.909 11.083  1.00 35.01 ? 2918 HOH B O   1 
HETATM 13563 O  O   . HOH EA 6 .   ? -16.787 58.499 -4.742  1.00 42.24 ? 2919 HOH B O   1 
HETATM 13564 O  O   . HOH EA 6 .   ? -10.699 59.435 37.700  1.00 38.41 ? 2920 HOH B O   1 
HETATM 13565 O  O   . HOH EA 6 .   ? -10.486 87.827 34.736  1.00 38.73 ? 2921 HOH B O   1 
HETATM 13566 O  O   . HOH EA 6 .   ? 2.321   62.443 1.260   1.00 29.23 ? 2922 HOH B O   1 
HETATM 13567 O  O   . HOH EA 6 .   ? -16.002 72.843 53.710  1.00 38.12 ? 2923 HOH B O   1 
HETATM 13568 O  O   . HOH EA 6 .   ? -19.979 91.832 22.966  1.00 43.11 ? 2924 HOH B O   1 
HETATM 13569 O  O   . HOH EA 6 .   ? -0.680  55.212 30.561  1.00 43.02 ? 2925 HOH B O   1 
HETATM 13570 O  O   . HOH EA 6 .   ? -4.950  52.234 69.255  1.00 33.89 ? 2926 HOH B O   1 
HETATM 13571 O  O   . HOH EA 6 .   ? -17.794 86.067 17.420  1.00 33.50 ? 2927 HOH B O   1 
HETATM 13572 O  O   . HOH EA 6 .   ? -19.840 44.964 51.465  1.00 30.71 ? 2928 HOH B O   1 
HETATM 13573 O  O   . HOH EA 6 .   ? -0.371  83.019 31.690  1.00 35.28 ? 2929 HOH B O   1 
HETATM 13574 O  O   . HOH EA 6 .   ? -19.353 57.229 59.951  1.00 41.44 ? 2930 HOH B O   1 
HETATM 13575 O  O   . HOH EA 6 .   ? 0.475   84.893 23.402  1.00 35.33 ? 2931 HOH B O   1 
HETATM 13576 O  O   . HOH EA 6 .   ? -4.855  67.969 59.935  1.00 31.10 ? 2932 HOH B O   1 
HETATM 13577 O  O   . HOH EA 6 .   ? -6.561  48.521 2.877   1.00 37.32 ? 2933 HOH B O   1 
HETATM 13578 O  O   . HOH EA 6 .   ? -19.889 60.296 3.491   1.00 41.34 ? 2934 HOH B O   1 
HETATM 13579 O  O   . HOH EA 6 .   ? -11.416 55.614 41.609  1.00 35.22 ? 2935 HOH B O   1 
HETATM 13580 O  O   . HOH EA 6 .   ? 9.065   79.498 37.970  1.00 34.90 ? 2936 HOH B O   1 
HETATM 13581 O  O   . HOH EA 6 .   ? -40.784 44.714 27.153  1.00 36.90 ? 2937 HOH B O   1 
HETATM 13582 O  O   . HOH EA 6 .   ? 2.446   37.034 40.433  1.00 35.93 ? 2938 HOH B O   1 
HETATM 13583 O  O   . HOH EA 6 .   ? 2.580   50.679 11.620  1.00 34.52 ? 2939 HOH B O   1 
HETATM 13584 O  O   . HOH EA 6 .   ? -37.232 48.043 34.881  1.00 36.08 ? 2940 HOH B O   1 
HETATM 13585 O  O   . HOH EA 6 .   ? -25.807 47.022 49.259  1.00 36.94 ? 2941 HOH B O   1 
HETATM 13586 O  O   . HOH EA 6 .   ? -11.124 82.241 41.152  1.00 37.91 ? 2942 HOH B O   1 
HETATM 13587 O  O   . HOH EA 6 .   ? 4.141   81.903 21.659  1.00 39.10 ? 2943 HOH B O   1 
HETATM 13588 O  O   . HOH EA 6 .   ? -1.729  49.524 25.733  1.00 44.10 ? 2944 HOH B O   1 
HETATM 13589 O  O   . HOH EA 6 .   ? -36.013 45.776 35.586  1.00 37.63 ? 2945 HOH B O   1 
HETATM 13590 O  O   . HOH EA 6 .   ? 6.559   56.042 23.962  1.00 34.54 ? 2946 HOH B O   1 
HETATM 13591 O  O   . HOH EA 6 .   ? -19.612 63.913 32.435  1.00 41.51 ? 2947 HOH B O   1 
HETATM 13592 O  O   . HOH EA 6 .   ? -39.890 71.448 25.020  1.00 36.50 ? 2948 HOH B O   1 
HETATM 13593 O  O   . HOH EA 6 .   ? -33.799 60.710 18.894  1.00 38.70 ? 2949 HOH B O   1 
HETATM 13594 O  O   . HOH EA 6 .   ? -23.425 81.295 35.562  1.00 38.58 ? 2950 HOH B O   1 
HETATM 13595 O  O   . HOH EA 6 .   ? 14.337  59.557 20.728  1.00 40.49 ? 2951 HOH B O   1 
HETATM 13596 O  O   . HOH EA 6 .   ? -1.728  84.822 30.466  1.00 36.76 ? 2952 HOH B O   1 
HETATM 13597 O  O   . HOH EA 6 .   ? -5.815  81.728 7.413   1.00 36.58 ? 2953 HOH B O   1 
HETATM 13598 O  O   . HOH EA 6 .   ? -34.421 42.508 34.953  1.00 44.58 ? 2954 HOH B O   1 
HETATM 13599 O  O   . HOH EA 6 .   ? -23.006 55.119 2.031   1.00 38.59 ? 2955 HOH B O   1 
HETATM 13600 O  O   . HOH EA 6 .   ? -1.568  80.813 33.436  1.00 37.46 ? 2956 HOH B O   1 
HETATM 13601 O  O   . HOH EA 6 .   ? 8.808   48.390 60.757  1.00 36.09 ? 2957 HOH B O   1 
HETATM 13602 O  O   . HOH EA 6 .   ? -7.140  44.382 69.395  1.00 36.39 ? 2958 HOH B O   1 
HETATM 13603 O  O   . HOH EA 6 .   ? -8.386  46.672 40.134  1.00 38.62 ? 2959 HOH B O   1 
HETATM 13604 O  O   . HOH EA 6 .   ? -33.631 84.034 20.772  1.00 41.78 ? 2960 HOH B O   1 
HETATM 13605 O  O   . HOH EA 6 .   ? -12.589 66.957 21.183  1.00 38.48 ? 2961 HOH B O   1 
HETATM 13606 O  O   . HOH EA 6 .   ? -24.486 76.913 48.553  1.00 40.79 ? 2962 HOH B O   1 
HETATM 13607 O  O   . HOH EA 6 .   ? -4.619  48.972 39.338  1.00 42.07 ? 2963 HOH B O   1 
HETATM 13608 O  O   . HOH EA 6 .   ? -37.812 51.883 22.228  1.00 38.67 ? 2964 HOH B O   1 
HETATM 13609 O  O   . HOH EA 6 .   ? -18.569 79.648 38.640  1.00 36.87 ? 2965 HOH B O   1 
HETATM 13610 O  O   . HOH EA 6 .   ? -0.328  76.844 8.515   1.00 40.23 ? 2966 HOH B O   1 
HETATM 13611 O  O   . HOH EA 6 .   ? -5.320  33.584 54.567  1.00 39.17 ? 2967 HOH B O   1 
HETATM 13612 O  O   . HOH EA 6 .   ? -24.723 38.723 9.701   1.00 37.22 ? 2968 HOH B O   1 
HETATM 13613 O  O   . HOH EA 6 .   ? -38.176 77.299 31.436  1.00 48.67 ? 2969 HOH B O   1 
HETATM 13614 O  O   . HOH EA 6 .   ? 3.837   85.612 34.423  1.00 37.09 ? 2970 HOH B O   1 
HETATM 13615 O  O   . HOH EA 6 .   ? -20.505 63.033 14.843  1.00 40.09 ? 2971 HOH B O   1 
HETATM 13616 O  O   . HOH EA 6 .   ? -29.730 66.272 48.455  1.00 37.66 ? 2972 HOH B O   1 
HETATM 13617 O  O   . HOH EA 6 .   ? -8.074  78.338 48.586  1.00 35.07 ? 2973 HOH B O   1 
HETATM 13618 O  O   . HOH FA 6 .   ? 78.472  79.827 55.843  1.00 49.82 ? 2286 HOH L O   1 
HETATM 13619 O  O   . HOH FA 6 .   ? 71.319  74.745 60.218  1.00 39.07 ? 2287 HOH L O   1 
HETATM 13620 O  O   . HOH GA 6 .   ? 74.192  76.753 17.584  1.00 44.79 ? 2285 HOH N O   1 
HETATM 13621 O  O   . HOH GA 6 .   ? 75.130  79.111 17.283  1.00 43.91 ? 2298 HOH N O   1 
HETATM 13622 O  O   . HOH HA 6 .   ? 37.110  68.733 12.586  1.00 36.62 ? 2294 HOH O O   1 
HETATM 13623 O  O   . HOH HA 6 .   ? 38.258  60.652 13.021  1.00 38.08 ? 2297 HOH O O   1 
HETATM 13624 O  O   . HOH IA 6 .   ? -31.348 35.529 14.246  1.00 40.88 ? 2290 HOH Q O   1 
HETATM 13625 O  O   . HOH JA 6 .   ? -24.237 75.199 2.187   1.00 39.31 ? 2289 HOH R O   1 
HETATM 13626 O  O   . HOH JA 6 .   ? -27.486 65.652 5.538   1.00 41.91 ? 2291 HOH R O   1 
HETATM 13627 O  O   . HOH JA 6 .   ? -27.769 70.052 5.058   1.00 43.34 ? 2293 HOH R O   1 
HETATM 13628 O  O   . HOH KA 6 .   ? 0.270   78.036 10.779  1.00 28.28 ? 2284 HOH S O   1 
HETATM 13629 O  O   . HOH KA 6 .   ? 7.030   75.397 11.130  1.00 30.51 ? 2292 HOH S O   1 
HETATM 13630 O  O   . HOH KA 6 .   ? 1.884   79.490 14.480  1.00 23.81 ? 2295 HOH S O   1 
HETATM 13631 O  O   . HOH LA 6 .   ? 3.559   73.835 0.955   1.00 39.62 ? 2283 HOH T O   1 
HETATM 13632 O  O   . HOH LA 6 .   ? -4.871  74.446 0.963   1.00 45.81 ? 2288 HOH T O   1 
HETATM 13633 O  O   . HOH LA 6 .   ? 2.097   76.636 -2.771  1.00 35.08 ? 2296 HOH T O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   PRO 4   4   ?   ?   ?   A . n 
A 1 5   TRP 5   5   ?   ?   ?   A . n 
A 1 6   LYS 6   6   ?   ?   ?   A . n 
A 1 7   VAL 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  GLY 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  LEU 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  ALA 14  14  ?   ?   ?   A . n 
A 1 15  ALA 15  15  ?   ?   ?   A . n 
A 1 16  ALA 16  16  ?   ?   ?   A . n 
A 1 17  LEU 17  17  ?   ?   ?   A . n 
A 1 18  VAL 18  18  ?   ?   ?   A . n 
A 1 19  THR 19  19  ?   ?   ?   A . n 
A 1 20  ILE 20  20  ?   ?   ?   A . n 
A 1 21  ILE 21  21  ?   ?   ?   A . n 
A 1 22  THR 22  22  ?   ?   ?   A . n 
A 1 23  VAL 23  23  ?   ?   ?   A . n 
A 1 24  PRO 24  24  ?   ?   ?   A . n 
A 1 25  VAL 25  25  ?   ?   ?   A . n 
A 1 26  VAL 26  26  ?   ?   ?   A . n 
A 1 27  LEU 27  27  ?   ?   ?   A . n 
A 1 28  LEU 28  28  ?   ?   ?   A . n 
A 1 29  ASN 29  29  ?   ?   ?   A . n 
A 1 30  LYS 30  30  ?   ?   ?   A . n 
A 1 31  GLY 31  31  ?   ?   ?   A . n 
A 1 32  THR 32  32  ?   ?   ?   A . n 
A 1 33  ASP 33  33  ?   ?   ?   A . n 
A 1 34  ASP 34  34  ?   ?   ?   A . n 
A 1 35  ALA 35  35  ?   ?   ?   A . n 
A 1 36  THR 36  36  ?   ?   ?   A . n 
A 1 37  ALA 37  37  ?   ?   ?   A . n 
A 1 38  ASP 38  38  ?   ?   ?   A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  TRP 62  62  62  TRP TRP A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 TYR 120 120 120 TYR TYR A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 TRP 124 124 124 TRP TRP A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 HIS 126 126 126 HIS HIS A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 TYR 132 132 132 TYR TYR A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 TRP 157 157 157 TRP TRP A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 TRP 168 168 168 TRP TRP A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 ASN 179 179 179 ASN ASN A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 TYR 183 183 183 TYR TYR A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 TRP 187 187 187 TRP TRP A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 ILE 193 193 193 ILE ILE A . n 
A 1 194 ILE 194 194 194 ILE ILE A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 TRP 201 201 201 TRP TRP A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 TRP 215 215 215 TRP TRP A . n 
A 1 216 TRP 216 216 216 TRP TRP A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 TYR 225 225 225 TYR TYR A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 PHE 228 228 228 PHE PHE A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 PHE 240 240 240 PHE PHE A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 SER 242 242 242 SER SER A . n 
A 1 243 ASP 243 243 243 ASP ASP A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 GLN 247 247 247 GLN GLN A . n 
A 1 248 TYR 248 248 248 TYR TYR A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 PRO 257 257 257 PRO PRO A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 PHE 268 268 268 PHE PHE A . n 
A 1 269 PHE 269 269 269 PHE PHE A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 THR 283 283 283 THR THR A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 GLN 286 286 286 GLN GLN A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 THR 288 288 288 THR THR A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 PRO 290 290 290 PRO PRO A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 SER 292 292 292 SER SER A . n 
A 1 293 MET 293 293 293 MET MET A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 HIS 298 298 298 HIS HIS A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 CYS 301 301 301 CYS CYS A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 TRP 305 305 305 TRP TRP A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 THR 307 307 307 THR THR A . n 
A 1 308 GLN 308 308 308 GLN GLN A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 ILE 311 311 311 ILE ILE A . n 
A 1 312 SER 312 312 312 SER SER A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 GLN 314 314 314 GLN GLN A . n 
A 1 315 TRP 315 315 315 TRP TRP A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 ARG 318 318 318 ARG ARG A . n 
A 1 319 ILE 319 319 319 ILE ILE A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 ASN 321 321 321 ASN ASN A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 MET 325 325 325 MET MET A . n 
A 1 326 ASP 326 326 326 ASP ASP A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 CYS 328 328 328 CYS CYS A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 ASP 331 331 331 ASP ASP A . n 
A 1 332 GLU 332 332 332 GLU GLU A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 TRP 337 337 337 TRP TRP A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 CYS 339 339 339 CYS CYS A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 HIS 345 345 345 HIS HIS A . n 
A 1 346 ILE 346 346 346 ILE ILE A . n 
A 1 347 GLU 347 347 347 GLU GLU A . n 
A 1 348 MET 348 348 348 MET MET A . n 
A 1 349 SER 349 349 349 SER SER A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 TRP 353 353 353 TRP TRP A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 ARG 356 356 356 ARG ARG A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 ARG 358 358 358 ARG ARG A . n 
A 1 359 PRO 359 359 359 PRO PRO A . n 
A 1 360 SER 360 360 360 SER SER A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 PRO 362 362 362 PRO PRO A . n 
A 1 363 HIS 363 363 363 HIS HIS A . n 
A 1 364 PHE 364 364 364 PHE PHE A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 LEU 366 366 366 LEU LEU A . n 
A 1 367 ASP 367 367 367 ASP ASP A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 SER 370 370 370 SER SER A . n 
A 1 371 PHE 371 371 371 PHE PHE A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 LYS 373 373 373 LYS LYS A . n 
A 1 374 ILE 374 374 374 ILE ILE A . n 
A 1 375 ILE 375 375 375 ILE ILE A . n 
A 1 376 SER 376 376 376 SER SER A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 TYR 381 381 381 TYR TYR A . n 
A 1 382 ARG 382 382 382 ARG ARG A . n 
A 1 383 HIS 383 383 383 HIS HIS A . n 
A 1 384 ILE 384 384 384 ILE ILE A . n 
A 1 385 CYS 385 385 385 CYS CYS A . n 
A 1 386 TYR 386 386 386 TYR TYR A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 GLN 388 388 388 GLN GLN A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 ASP 393 393 393 ASP ASP A . n 
A 1 394 CYS 394 394 394 CYS CYS A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 PHE 396 396 396 PHE PHE A . n 
A 1 397 ILE 397 397 397 ILE ILE A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 LYS 399 399 399 LYS LYS A . n 
A 1 400 GLY 400 400 400 GLY GLY A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 TRP 402 402 402 TRP TRP A . n 
A 1 403 GLU 403 403 403 GLU GLU A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 ILE 407 407 407 ILE ILE A . n 
A 1 408 GLU 408 408 408 GLU GLU A . n 
A 1 409 ALA 409 409 409 ALA ALA A . n 
A 1 410 LEU 410 410 410 LEU LEU A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 SER 412 412 412 SER SER A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 TYR 414 414 414 TYR TYR A . n 
A 1 415 LEU 415 415 415 LEU LEU A . n 
A 1 416 TYR 416 416 416 TYR TYR A . n 
A 1 417 TYR 417 417 417 TYR TYR A . n 
A 1 418 ILE 418 418 418 ILE ILE A . n 
A 1 419 SER 419 419 419 SER SER A . n 
A 1 420 ASN 420 420 420 ASN ASN A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 TYR 422 422 422 TYR TYR A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 GLY 424 424 424 GLY GLY A . n 
A 1 425 MET 425 425 425 MET MET A . n 
A 1 426 PRO 426 426 426 PRO PRO A . n 
A 1 427 GLY 427 427 427 GLY GLY A . n 
A 1 428 GLY 428 428 428 GLY GLY A . n 
A 1 429 ARG 429 429 429 ARG ARG A . n 
A 1 430 ASN 430 430 430 ASN ASN A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 TYR 432 432 432 TYR TYR A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 GLN 435 435 435 GLN GLN A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 SER 437 437 437 SER SER A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 TYR 439 439 439 TYR TYR A . n 
A 1 440 THR 440 440 440 THR THR A . n 
A 1 441 LYS 441 441 441 LYS LYS A . n 
A 1 442 VAL 442 442 442 VAL VAL A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 CYS 444 444 444 CYS CYS A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 SER 446 446 446 SER SER A . n 
A 1 447 CYS 447 447 447 CYS CYS A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 LEU 449 449 449 LEU LEU A . n 
A 1 450 ASN 450 450 450 ASN ASN A . n 
A 1 451 PRO 451 451 451 PRO PRO A . n 
A 1 452 GLU 452 452 452 GLU GLU A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 CYS 454 454 454 CYS CYS A . n 
A 1 455 GLN 455 455 455 GLN GLN A . n 
A 1 456 TYR 456 456 456 TYR TYR A . n 
A 1 457 TYR 457 457 457 TYR TYR A . n 
A 1 458 SER 458 458 458 SER SER A . n 
A 1 459 VAL 459 459 459 VAL VAL A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 PHE 461 461 461 PHE PHE A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 LYS 463 463 463 LYS LYS A . n 
A 1 464 GLU 464 464 464 GLU GLU A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 TYR 467 467 467 TYR TYR A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 GLN 469 469 469 GLN GLN A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 ARG 471 471 471 ARG ARG A . n 
A 1 472 CYS 472 472 472 CYS CYS A . n 
A 1 473 SER 473 473 473 SER SER A . n 
A 1 474 GLY 474 474 474 GLY GLY A . n 
A 1 475 PRO 475 475 475 PRO PRO A . n 
A 1 476 GLY 476 476 476 GLY GLY A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 PRO 478 478 478 PRO PRO A . n 
A 1 479 LEU 479 479 479 LEU LEU A . n 
A 1 480 TYR 480 480 480 TYR TYR A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 HIS 483 483 483 HIS HIS A . n 
A 1 484 SER 484 484 484 SER SER A . n 
A 1 485 SER 485 485 485 SER SER A . n 
A 1 486 VAL 486 486 486 VAL VAL A . n 
A 1 487 ASN 487 487 487 ASN ASN A . n 
A 1 488 ASP 488 488 488 ASP ASP A . n 
A 1 489 LYS 489 489 489 LYS LYS A . n 
A 1 490 GLY 490 490 490 GLY GLY A . n 
A 1 491 LEU 491 491 491 LEU LEU A . n 
A 1 492 ARG 492 492 492 ARG ARG A . n 
A 1 493 VAL 493 493 493 VAL VAL A . n 
A 1 494 LEU 494 494 494 LEU LEU A . n 
A 1 495 GLU 495 495 495 GLU GLU A . n 
A 1 496 ASP 496 496 496 ASP ASP A . n 
A 1 497 ASN 497 497 497 ASN ASN A . n 
A 1 498 SER 498 498 498 SER SER A . n 
A 1 499 ALA 499 499 499 ALA ALA A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
A 1 501 ASP 501 501 501 ASP ASP A . n 
A 1 502 LYS 502 502 502 LYS LYS A . n 
A 1 503 MET 503 503 503 MET MET A . n 
A 1 504 LEU 504 504 504 LEU LEU A . n 
A 1 505 GLN 505 505 505 GLN GLN A . n 
A 1 506 ASN 506 506 506 ASN ASN A . n 
A 1 507 VAL 507 507 507 VAL VAL A . n 
A 1 508 GLN 508 508 508 GLN GLN A . n 
A 1 509 MET 509 509 509 MET MET A . n 
A 1 510 PRO 510 510 510 PRO PRO A . n 
A 1 511 SER 511 511 511 SER SER A . n 
A 1 512 LYS 512 512 512 LYS LYS A . n 
A 1 513 LYS 513 513 513 LYS LYS A . n 
A 1 514 LEU 514 514 514 LEU LEU A . n 
A 1 515 ASP 515 515 515 ASP ASP A . n 
A 1 516 PHE 516 516 516 PHE PHE A . n 
A 1 517 ILE 517 517 517 ILE ILE A . n 
A 1 518 ILE 518 518 518 ILE ILE A . n 
A 1 519 LEU 519 519 519 LEU LEU A . n 
A 1 520 ASN 520 520 520 ASN ASN A . n 
A 1 521 GLU 521 521 521 GLU GLU A . n 
A 1 522 THR 522 522 522 THR THR A . n 
A 1 523 LYS 523 523 523 LYS LYS A . n 
A 1 524 PHE 524 524 524 PHE PHE A . n 
A 1 525 TRP 525 525 525 TRP TRP A . n 
A 1 526 TYR 526 526 526 TYR TYR A . n 
A 1 527 GLN 527 527 527 GLN GLN A . n 
A 1 528 MET 528 528 528 MET MET A . n 
A 1 529 ILE 529 529 529 ILE ILE A . n 
A 1 530 LEU 530 530 530 LEU LEU A . n 
A 1 531 PRO 531 531 531 PRO PRO A . n 
A 1 532 PRO 532 532 532 PRO PRO A . n 
A 1 533 HIS 533 533 533 HIS HIS A . n 
A 1 534 PHE 534 534 534 PHE PHE A . n 
A 1 535 ASP 535 535 535 ASP ASP A . n 
A 1 536 LYS 536 536 536 LYS LYS A . n 
A 1 537 SER 537 537 537 SER SER A . n 
A 1 538 LYS 538 538 538 LYS LYS A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 TYR 540 540 540 TYR TYR A . n 
A 1 541 PRO 541 541 541 PRO PRO A . n 
A 1 542 LEU 542 542 542 LEU LEU A . n 
A 1 543 LEU 543 543 543 LEU LEU A . n 
A 1 544 LEU 544 544 544 LEU LEU A . n 
A 1 545 ASP 545 545 545 ASP ASP A . n 
A 1 546 VAL 546 546 546 VAL VAL A . n 
A 1 547 TYR 547 547 547 TYR TYR A . n 
A 1 548 ALA 548 548 548 ALA ALA A . n 
A 1 549 GLY 549 549 549 GLY GLY A . n 
A 1 550 PRO 550 550 550 PRO PRO A . n 
A 1 551 CYS 551 551 551 CYS CYS A . n 
A 1 552 SER 552 552 552 SER SER A . n 
A 1 553 GLN 553 553 553 GLN GLN A . n 
A 1 554 LYS 554 554 554 LYS LYS A . n 
A 1 555 ALA 555 555 555 ALA ALA A . n 
A 1 556 ASP 556 556 556 ASP ASP A . n 
A 1 557 THR 557 557 557 THR THR A . n 
A 1 558 VAL 558 558 558 VAL VAL A . n 
A 1 559 PHE 559 559 559 PHE PHE A . n 
A 1 560 ARG 560 560 560 ARG ARG A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 ASN 562 562 562 ASN ASN A . n 
A 1 563 TRP 563 563 563 TRP TRP A . n 
A 1 564 ALA 564 564 564 ALA ALA A . n 
A 1 565 THR 565 565 565 THR THR A . n 
A 1 566 TYR 566 566 566 TYR TYR A . n 
A 1 567 LEU 567 567 567 LEU LEU A . n 
A 1 568 ALA 568 568 568 ALA ALA A . n 
A 1 569 SER 569 569 569 SER SER A . n 
A 1 570 THR 570 570 570 THR THR A . n 
A 1 571 GLU 571 571 571 GLU GLU A . n 
A 1 572 ASN 572 572 572 ASN ASN A . n 
A 1 573 ILE 573 573 573 ILE ILE A . n 
A 1 574 ILE 574 574 574 ILE ILE A . n 
A 1 575 VAL 575 575 575 VAL VAL A . n 
A 1 576 ALA 576 576 576 ALA ALA A . n 
A 1 577 SER 577 577 577 SER SER A . n 
A 1 578 PHE 578 578 578 PHE PHE A . n 
A 1 579 ASP 579 579 579 ASP ASP A . n 
A 1 580 GLY 580 580 580 GLY GLY A . n 
A 1 581 ARG 581 581 581 ARG ARG A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 SER 583 583 583 SER SER A . n 
A 1 584 GLY 584 584 584 GLY GLY A . n 
A 1 585 TYR 585 585 585 TYR TYR A . n 
A 1 586 GLN 586 586 586 GLN GLN A . n 
A 1 587 GLY 587 587 587 GLY GLY A . n 
A 1 588 ASP 588 588 588 ASP ASP A . n 
A 1 589 LYS 589 589 589 LYS LYS A . n 
A 1 590 ILE 590 590 590 ILE ILE A . n 
A 1 591 MET 591 591 591 MET MET A . n 
A 1 592 HIS 592 592 592 HIS HIS A . n 
A 1 593 ALA 593 593 593 ALA ALA A . n 
A 1 594 ILE 594 594 594 ILE ILE A . n 
A 1 595 ASN 595 595 595 ASN ASN A . n 
A 1 596 ARG 596 596 596 ARG ARG A . n 
A 1 597 ARG 597 597 597 ARG ARG A . n 
A 1 598 LEU 598 598 598 LEU LEU A . n 
A 1 599 GLY 599 599 599 GLY GLY A . n 
A 1 600 THR 600 600 600 THR THR A . n 
A 1 601 PHE 601 601 601 PHE PHE A . n 
A 1 602 GLU 602 602 602 GLU GLU A . n 
A 1 603 VAL 603 603 603 VAL VAL A . n 
A 1 604 GLU 604 604 604 GLU GLU A . n 
A 1 605 ASP 605 605 605 ASP ASP A . n 
A 1 606 GLN 606 606 606 GLN GLN A . n 
A 1 607 ILE 607 607 607 ILE ILE A . n 
A 1 608 GLU 608 608 608 GLU GLU A . n 
A 1 609 ALA 609 609 609 ALA ALA A . n 
A 1 610 ALA 610 610 610 ALA ALA A . n 
A 1 611 ARG 611 611 611 ARG ARG A . n 
A 1 612 GLN 612 612 612 GLN GLN A . n 
A 1 613 PHE 613 613 613 PHE PHE A . n 
A 1 614 SER 614 614 614 SER SER A . n 
A 1 615 LYS 615 615 615 LYS LYS A . n 
A 1 616 MET 616 616 616 MET MET A . n 
A 1 617 GLY 617 617 617 GLY GLY A . n 
A 1 618 PHE 618 618 618 PHE PHE A . n 
A 1 619 VAL 619 619 619 VAL VAL A . n 
A 1 620 ASP 620 620 620 ASP ASP A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 LYS 622 622 622 LYS LYS A . n 
A 1 623 ARG 623 623 623 ARG ARG A . n 
A 1 624 ILE 624 624 624 ILE ILE A . n 
A 1 625 ALA 625 625 625 ALA ALA A . n 
A 1 626 ILE 626 626 626 ILE ILE A . n 
A 1 627 TRP 627 627 627 TRP TRP A . n 
A 1 628 GLY 628 628 628 GLY GLY A . n 
A 1 629 TRP 629 629 629 TRP TRP A . n 
A 1 630 SER 630 630 630 SER SER A . n 
A 1 631 TYR 631 631 631 TYR TYR A . n 
A 1 632 GLY 632 632 632 GLY GLY A . n 
A 1 633 GLY 633 633 633 GLY GLY A . n 
A 1 634 TYR 634 634 634 TYR TYR A . n 
A 1 635 VAL 635 635 635 VAL VAL A . n 
A 1 636 THR 636 636 636 THR THR A . n 
A 1 637 SER 637 637 637 SER SER A . n 
A 1 638 MET 638 638 638 MET MET A . n 
A 1 639 VAL 639 639 639 VAL VAL A . n 
A 1 640 LEU 640 640 640 LEU LEU A . n 
A 1 641 GLY 641 641 641 GLY GLY A . n 
A 1 642 SER 642 642 642 SER SER A . n 
A 1 643 GLY 643 643 643 GLY GLY A . n 
A 1 644 SER 644 644 644 SER SER A . n 
A 1 645 GLY 645 645 645 GLY GLY A . n 
A 1 646 VAL 646 646 646 VAL VAL A . n 
A 1 647 PHE 647 647 647 PHE PHE A . n 
A 1 648 LYS 648 648 648 LYS LYS A . n 
A 1 649 CYS 649 649 649 CYS CYS A . n 
A 1 650 GLY 650 650 650 GLY GLY A . n 
A 1 651 ILE 651 651 651 ILE ILE A . n 
A 1 652 ALA 652 652 652 ALA ALA A . n 
A 1 653 VAL 653 653 653 VAL VAL A . n 
A 1 654 ALA 654 654 654 ALA ALA A . n 
A 1 655 PRO 655 655 655 PRO PRO A . n 
A 1 656 VAL 656 656 656 VAL VAL A . n 
A 1 657 SER 657 657 657 SER SER A . n 
A 1 658 ARG 658 658 658 ARG ARG A . n 
A 1 659 TRP 659 659 659 TRP TRP A . n 
A 1 660 GLU 660 660 660 GLU GLU A . n 
A 1 661 TYR 661 661 661 TYR TYR A . n 
A 1 662 TYR 662 662 662 TYR TYR A . n 
A 1 663 ASP 663 663 663 ASP ASP A . n 
A 1 664 SER 664 664 664 SER SER A . n 
A 1 665 VAL 665 665 665 VAL VAL A . n 
A 1 666 TYR 666 666 666 TYR TYR A . n 
A 1 667 THR 667 667 667 THR THR A . n 
A 1 668 GLU 668 668 668 GLU GLU A . n 
A 1 669 ARG 669 669 669 ARG ARG A . n 
A 1 670 TYR 670 670 670 TYR TYR A . n 
A 1 671 MET 671 671 671 MET MET A . n 
A 1 672 GLY 672 672 672 GLY GLY A . n 
A 1 673 LEU 673 673 673 LEU LEU A . n 
A 1 674 PRO 674 674 674 PRO PRO A . n 
A 1 675 THR 675 675 675 THR THR A . n 
A 1 676 PRO 676 676 676 PRO PRO A . n 
A 1 677 GLU 677 677 677 GLU GLU A . n 
A 1 678 ASP 678 678 678 ASP ASP A . n 
A 1 679 ASN 679 679 679 ASN ASN A . n 
A 1 680 LEU 680 680 680 LEU LEU A . n 
A 1 681 ASP 681 681 681 ASP ASP A . n 
A 1 682 HIS 682 682 682 HIS HIS A . n 
A 1 683 TYR 683 683 683 TYR TYR A . n 
A 1 684 ARG 684 684 684 ARG ARG A . n 
A 1 685 ASN 685 685 685 ASN ASN A . n 
A 1 686 SER 686 686 686 SER SER A . n 
A 1 687 THR 687 687 687 THR THR A . n 
A 1 688 VAL 688 688 688 VAL VAL A . n 
A 1 689 MET 689 689 689 MET MET A . n 
A 1 690 SER 690 690 690 SER SER A . n 
A 1 691 ARG 691 691 691 ARG ARG A . n 
A 1 692 ALA 692 692 692 ALA ALA A . n 
A 1 693 GLU 693 693 693 GLU GLU A . n 
A 1 694 ASN 694 694 694 ASN ASN A . n 
A 1 695 PHE 695 695 695 PHE PHE A . n 
A 1 696 LYS 696 696 696 LYS LYS A . n 
A 1 697 GLN 697 697 697 GLN GLN A . n 
A 1 698 VAL 698 698 698 VAL VAL A . n 
A 1 699 GLU 699 699 699 GLU GLU A . n 
A 1 700 TYR 700 700 700 TYR TYR A . n 
A 1 701 LEU 701 701 701 LEU LEU A . n 
A 1 702 LEU 702 702 702 LEU LEU A . n 
A 1 703 ILE 703 703 703 ILE ILE A . n 
A 1 704 HIS 704 704 704 HIS HIS A . n 
A 1 705 GLY 705 705 705 GLY GLY A . n 
A 1 706 THR 706 706 706 THR THR A . n 
A 1 707 ALA 707 707 707 ALA ALA A . n 
A 1 708 ASP 708 708 708 ASP ASP A . n 
A 1 709 ASP 709 709 709 ASP ASP A . n 
A 1 710 ASN 710 710 710 ASN ASN A . n 
A 1 711 VAL 711 711 711 VAL VAL A . n 
A 1 712 HIS 712 712 712 HIS HIS A . n 
A 1 713 PHE 713 713 713 PHE PHE A . n 
A 1 714 GLN 714 714 714 GLN GLN A . n 
A 1 715 GLN 715 715 715 GLN GLN A . n 
A 1 716 SER 716 716 716 SER SER A . n 
A 1 717 ALA 717 717 717 ALA ALA A . n 
A 1 718 GLN 718 718 718 GLN GLN A . n 
A 1 719 ILE 719 719 719 ILE ILE A . n 
A 1 720 SER 720 720 720 SER SER A . n 
A 1 721 LYS 721 721 721 LYS LYS A . n 
A 1 722 ALA 722 722 722 ALA ALA A . n 
A 1 723 LEU 723 723 723 LEU LEU A . n 
A 1 724 VAL 724 724 724 VAL VAL A . n 
A 1 725 ASP 725 725 725 ASP ASP A . n 
A 1 726 VAL 726 726 726 VAL VAL A . n 
A 1 727 GLY 727 727 727 GLY GLY A . n 
A 1 728 VAL 728 728 728 VAL VAL A . n 
A 1 729 ASP 729 729 729 ASP ASP A . n 
A 1 730 PHE 730 730 730 PHE PHE A . n 
A 1 731 GLN 731 731 731 GLN GLN A . n 
A 1 732 ALA 732 732 732 ALA ALA A . n 
A 1 733 MET 733 733 733 MET MET A . n 
A 1 734 TRP 734 734 734 TRP TRP A . n 
A 1 735 TYR 735 735 735 TYR TYR A . n 
A 1 736 THR 736 736 736 THR THR A . n 
A 1 737 ASP 737 737 737 ASP ASP A . n 
A 1 738 GLU 738 738 738 GLU GLU A . n 
A 1 739 ASP 739 739 739 ASP ASP A . n 
A 1 740 HIS 740 740 740 HIS HIS A . n 
A 1 741 GLY 741 741 741 GLY GLY A . n 
A 1 742 ILE 742 742 742 ILE ILE A . n 
A 1 743 ALA 743 743 743 ALA ALA A . n 
A 1 744 SER 744 744 744 SER SER A . n 
A 1 745 SER 745 745 745 SER SER A . n 
A 1 746 THR 746 746 746 THR THR A . n 
A 1 747 ALA 747 747 747 ALA ALA A . n 
A 1 748 HIS 748 748 748 HIS HIS A . n 
A 1 749 GLN 749 749 749 GLN GLN A . n 
A 1 750 HIS 750 750 750 HIS HIS A . n 
A 1 751 ILE 751 751 751 ILE ILE A . n 
A 1 752 TYR 752 752 752 TYR TYR A . n 
A 1 753 THR 753 753 753 THR THR A . n 
A 1 754 HIS 754 754 754 HIS HIS A . n 
A 1 755 MET 755 755 755 MET MET A . n 
A 1 756 SER 756 756 756 SER SER A . n 
A 1 757 HIS 757 757 757 HIS HIS A . n 
A 1 758 PHE 758 758 758 PHE PHE A . n 
A 1 759 ILE 759 759 759 ILE ILE A . n 
A 1 760 LYS 760 760 760 LYS LYS A . n 
A 1 761 GLN 761 761 761 GLN GLN A . n 
A 1 762 CYS 762 762 762 CYS CYS A . n 
A 1 763 PHE 763 763 763 PHE PHE A . n 
A 1 764 SER 764 764 764 SER SER A . n 
A 1 765 LEU 765 765 765 LEU LEU A . n 
A 1 766 PRO 766 766 766 PRO PRO A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   PRO 4   4   ?   ?   ?   B . n 
B 1 5   TRP 5   5   ?   ?   ?   B . n 
B 1 6   LYS 6   6   ?   ?   ?   B . n 
B 1 7   VAL 7   7   ?   ?   ?   B . n 
B 1 8   LEU 8   8   ?   ?   ?   B . n 
B 1 9   LEU 9   9   ?   ?   ?   B . n 
B 1 10  GLY 10  10  ?   ?   ?   B . n 
B 1 11  LEU 11  11  ?   ?   ?   B . n 
B 1 12  LEU 12  12  ?   ?   ?   B . n 
B 1 13  GLY 13  13  ?   ?   ?   B . n 
B 1 14  ALA 14  14  ?   ?   ?   B . n 
B 1 15  ALA 15  15  ?   ?   ?   B . n 
B 1 16  ALA 16  16  ?   ?   ?   B . n 
B 1 17  LEU 17  17  ?   ?   ?   B . n 
B 1 18  VAL 18  18  ?   ?   ?   B . n 
B 1 19  THR 19  19  ?   ?   ?   B . n 
B 1 20  ILE 20  20  ?   ?   ?   B . n 
B 1 21  ILE 21  21  ?   ?   ?   B . n 
B 1 22  THR 22  22  ?   ?   ?   B . n 
B 1 23  VAL 23  23  ?   ?   ?   B . n 
B 1 24  PRO 24  24  ?   ?   ?   B . n 
B 1 25  VAL 25  25  ?   ?   ?   B . n 
B 1 26  VAL 26  26  ?   ?   ?   B . n 
B 1 27  LEU 27  27  ?   ?   ?   B . n 
B 1 28  LEU 28  28  ?   ?   ?   B . n 
B 1 29  ASN 29  29  ?   ?   ?   B . n 
B 1 30  LYS 30  30  ?   ?   ?   B . n 
B 1 31  GLY 31  31  ?   ?   ?   B . n 
B 1 32  THR 32  32  ?   ?   ?   B . n 
B 1 33  ASP 33  33  ?   ?   ?   B . n 
B 1 34  ASP 34  34  ?   ?   ?   B . n 
B 1 35  ALA 35  35  ?   ?   ?   B . n 
B 1 36  THR 36  36  ?   ?   ?   B . n 
B 1 37  ALA 37  37  ?   ?   ?   B . n 
B 1 38  ASP 38  38  ?   ?   ?   B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  THR 42  42  42  THR THR B . n 
B 1 43  TYR 43  43  43  TYR TYR B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  THR 46  46  46  THR THR B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  TYR 48  48  48  TYR TYR B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  THR 52  52  52  THR THR B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  LYS 56  56  56  LYS LYS B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  TYR 58  58  58  TYR TYR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ARG 61  61  61  ARG ARG B . n 
B 1 62  TRP 62  62  62  TRP TRP B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  SER 64  64  64  SER SER B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  TYR 70  70  70  TYR TYR B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  GLN 72  72  72  GLN GLN B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  PHE 79  79  79  PHE PHE B . n 
B 1 80  ASN 80  80  80  ASN ASN B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  TYR 83  83  83  TYR TYR B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  ASN 85  85  85  ASN ASN B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  SER 87  87  87  SER SER B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  THR 94  94  94  THR THR B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 PRO 109 109 109 PRO PRO B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 GLN 112 112 112 GLN GLN B . n 
B 1 113 PHE 113 113 113 PHE PHE B . n 
B 1 114 ILE 114 114 114 ILE ILE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 TYR 120 120 120 TYR TYR B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 GLN 123 123 123 GLN GLN B . n 
B 1 124 TRP 124 124 124 TRP TRP B . n 
B 1 125 ARG 125 125 125 ARG ARG B . n 
B 1 126 HIS 126 126 126 HIS HIS B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 TYR 128 128 128 TYR TYR B . n 
B 1 129 THR 129 129 129 THR THR B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 SER 131 131 131 SER SER B . n 
B 1 132 TYR 132 132 132 TYR TYR B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 TYR 135 135 135 TYR TYR B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 ASN 138 138 138 ASN ASN B . n 
B 1 139 LYS 139 139 139 LYS LYS B . n 
B 1 140 ARG 140 140 140 ARG ARG B . n 
B 1 141 GLN 141 141 141 GLN GLN B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ILE 143 143 143 ILE ILE B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 GLU 145 145 145 GLU GLU B . n 
B 1 146 GLU 146 146 146 GLU GLU B . n 
B 1 147 ARG 147 147 147 ARG ARG B . n 
B 1 148 ILE 148 148 148 ILE ILE B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 THR 152 152 152 THR THR B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 THR 156 156 156 THR THR B . n 
B 1 157 TRP 157 157 157 TRP TRP B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PRO 159 159 159 PRO PRO B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 HIS 162 162 162 HIS HIS B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 VAL 167 167 167 VAL VAL B . n 
B 1 168 TRP 168 168 168 TRP TRP B . n 
B 1 169 ASN 169 169 169 ASN ASN B . n 
B 1 170 ASN 170 170 170 ASN ASN B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 TYR 173 173 173 TYR TYR B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 ILE 176 176 176 ILE ILE B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 PRO 178 178 178 PRO PRO B . n 
B 1 179 ASN 179 179 179 ASN ASN B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 PRO 181 181 181 PRO PRO B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 TYR 183 183 183 TYR TYR B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 ILE 185 185 185 ILE ILE B . n 
B 1 186 THR 186 186 186 THR THR B . n 
B 1 187 TRP 187 187 187 TRP TRP B . n 
B 1 188 THR 188 188 188 THR THR B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 LYS 190 190 190 LYS LYS B . n 
B 1 191 GLU 191 191 191 GLU GLU B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 ILE 193 193 193 ILE ILE B . n 
B 1 194 ILE 194 194 194 ILE ILE B . n 
B 1 195 TYR 195 195 195 TYR TYR B . n 
B 1 196 ASN 196 196 196 ASN ASN B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 TRP 201 201 201 TRP TRP B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 TYR 203 203 203 TYR TYR B . n 
B 1 204 GLU 204 204 204 GLU GLU B . n 
B 1 205 GLU 205 205 205 GLU GLU B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 VAL 207 207 207 VAL VAL B . n 
B 1 208 PHE 208 208 208 PHE PHE B . n 
B 1 209 SER 209 209 209 SER SER B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 SER 212 212 212 SER SER B . n 
B 1 213 ALA 213 213 213 ALA ALA B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 TRP 215 215 215 TRP TRP B . n 
B 1 216 TRP 216 216 216 TRP TRP B . n 
B 1 217 SER 217 217 217 SER SER B . n 
B 1 218 PRO 218 218 218 PRO PRO B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 GLY 220 220 220 GLY GLY B . n 
B 1 221 THR 221 221 221 THR THR B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 TYR 225 225 225 TYR TYR B . n 
B 1 226 ALA 226 226 226 ALA ALA B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 PHE 228 228 228 PHE PHE B . n 
B 1 229 ASN 229 229 229 ASN ASN B . n 
B 1 230 ASP 230 230 230 ASP ASP B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 GLU 232 232 232 GLU GLU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 PRO 234 234 234 PRO PRO B . n 
B 1 235 LEU 235 235 235 LEU LEU B . n 
B 1 236 ILE 236 236 236 ILE ILE B . n 
B 1 237 GLU 237 237 237 GLU GLU B . n 
B 1 238 TYR 238 238 238 TYR TYR B . n 
B 1 239 SER 239 239 239 SER SER B . n 
B 1 240 PHE 240 240 240 PHE PHE B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 SER 242 242 242 SER SER B . n 
B 1 243 ASP 243 243 243 ASP ASP B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 SER 245 245 245 SER SER B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 GLN 247 247 247 GLN GLN B . n 
B 1 248 TYR 248 248 248 TYR TYR B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 LYS 250 250 250 LYS LYS B . n 
B 1 251 THR 251 251 251 THR THR B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 VAL 254 254 254 VAL VAL B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 PRO 257 257 257 PRO PRO B . n 
B 1 258 LYS 258 258 258 LYS LYS B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 GLY 260 260 260 GLY GLY B . n 
B 1 261 ALA 261 261 261 ALA ALA B . n 
B 1 262 VAL 262 262 262 VAL VAL B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 PRO 264 264 264 PRO PRO B . n 
B 1 265 THR 265 265 265 THR THR B . n 
B 1 266 VAL 266 266 266 VAL VAL B . n 
B 1 267 LYS 267 267 267 LYS LYS B . n 
B 1 268 PHE 268 268 268 PHE PHE B . n 
B 1 269 PHE 269 269 269 PHE PHE B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 VAL 271 271 271 VAL VAL B . n 
B 1 272 ASN 272 272 272 ASN ASN B . n 
B 1 273 THR 273 273 273 THR THR B . n 
B 1 274 ASP 274 274 274 ASP ASP B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 SER 277 277 277 SER SER B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ASN 281 281 281 ASN ASN B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 THR 283 283 283 THR THR B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ILE 285 285 285 ILE ILE B . n 
B 1 286 GLN 286 286 286 GLN GLN B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 THR 288 288 288 THR THR B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 PRO 290 290 290 PRO PRO B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 SER 292 292 292 SER SER B . n 
B 1 293 MET 293 293 293 MET MET B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 ILE 295 295 295 ILE ILE B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 ASP 297 297 297 ASP ASP B . n 
B 1 298 HIS 298 298 298 HIS HIS B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 CYS 301 301 301 CYS CYS B . n 
B 1 302 ASP 302 302 302 ASP ASP B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 TRP 305 305 305 TRP TRP B . n 
B 1 306 ALA 306 306 306 ALA ALA B . n 
B 1 307 THR 307 307 307 THR THR B . n 
B 1 308 GLN 308 308 308 GLN GLN B . n 
B 1 309 GLU 309 309 309 GLU GLU B . n 
B 1 310 ARG 310 310 310 ARG ARG B . n 
B 1 311 ILE 311 311 311 ILE ILE B . n 
B 1 312 SER 312 312 312 SER SER B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 GLN 314 314 314 GLN GLN B . n 
B 1 315 TRP 315 315 315 TRP TRP B . n 
B 1 316 LEU 316 316 316 LEU LEU B . n 
B 1 317 ARG 317 317 317 ARG ARG B . n 
B 1 318 ARG 318 318 318 ARG ARG B . n 
B 1 319 ILE 319 319 319 ILE ILE B . n 
B 1 320 GLN 320 320 320 GLN GLN B . n 
B 1 321 ASN 321 321 321 ASN ASN B . n 
B 1 322 TYR 322 322 322 TYR TYR B . n 
B 1 323 SER 323 323 323 SER SER B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 MET 325 325 325 MET MET B . n 
B 1 326 ASP 326 326 326 ASP ASP B . n 
B 1 327 ILE 327 327 327 ILE ILE B . n 
B 1 328 CYS 328 328 328 CYS CYS B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 TYR 330 330 330 TYR TYR B . n 
B 1 331 ASP 331 331 331 ASP ASP B . n 
B 1 332 GLU 332 332 332 GLU GLU B . n 
B 1 333 SER 333 333 333 SER SER B . n 
B 1 334 SER 334 334 334 SER SER B . n 
B 1 335 GLY 335 335 335 GLY GLY B . n 
B 1 336 ARG 336 336 336 ARG ARG B . n 
B 1 337 TRP 337 337 337 TRP TRP B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 CYS 339 339 339 CYS CYS B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 ALA 342 342 342 ALA ALA B . n 
B 1 343 ARG 343 343 343 ARG ARG B . n 
B 1 344 GLN 344 344 344 GLN GLN B . n 
B 1 345 HIS 345 345 345 HIS HIS B . n 
B 1 346 ILE 346 346 346 ILE ILE B . n 
B 1 347 GLU 347 347 347 GLU GLU B . n 
B 1 348 MET 348 348 348 MET MET B . n 
B 1 349 SER 349 349 349 SER SER B . n 
B 1 350 THR 350 350 350 THR THR B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 GLY 352 352 352 GLY GLY B . n 
B 1 353 TRP 353 353 353 TRP TRP B . n 
B 1 354 VAL 354 354 354 VAL VAL B . n 
B 1 355 GLY 355 355 355 GLY GLY B . n 
B 1 356 ARG 356 356 356 ARG ARG B . n 
B 1 357 PHE 357 357 357 PHE PHE B . n 
B 1 358 ARG 358 358 358 ARG ARG B . n 
B 1 359 PRO 359 359 359 PRO PRO B . n 
B 1 360 SER 360 360 360 SER SER B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 PRO 362 362 362 PRO PRO B . n 
B 1 363 HIS 363 363 363 HIS HIS B . n 
B 1 364 PHE 364 364 364 PHE PHE B . n 
B 1 365 THR 365 365 365 THR THR B . n 
B 1 366 LEU 366 366 366 LEU LEU B . n 
B 1 367 ASP 367 367 367 ASP ASP B . n 
B 1 368 GLY 368 368 368 GLY GLY B . n 
B 1 369 ASN 369 369 369 ASN ASN B . n 
B 1 370 SER 370 370 370 SER SER B . n 
B 1 371 PHE 371 371 371 PHE PHE B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 LYS 373 373 373 LYS LYS B . n 
B 1 374 ILE 374 374 374 ILE ILE B . n 
B 1 375 ILE 375 375 375 ILE ILE B . n 
B 1 376 SER 376 376 376 SER SER B . n 
B 1 377 ASN 377 377 377 ASN ASN B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 GLY 380 380 380 GLY GLY B . n 
B 1 381 TYR 381 381 381 TYR TYR B . n 
B 1 382 ARG 382 382 382 ARG ARG B . n 
B 1 383 HIS 383 383 383 HIS HIS B . n 
B 1 384 ILE 384 384 384 ILE ILE B . n 
B 1 385 CYS 385 385 385 CYS CYS B . n 
B 1 386 TYR 386 386 386 TYR TYR B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 GLN 388 388 388 GLN GLN B . n 
B 1 389 ILE 389 389 389 ILE ILE B . n 
B 1 390 ASP 390 390 390 ASP ASP B . n 
B 1 391 LYS 391 391 391 LYS LYS B . n 
B 1 392 LYS 392 392 392 LYS LYS B . n 
B 1 393 ASP 393 393 393 ASP ASP B . n 
B 1 394 CYS 394 394 394 CYS CYS B . n 
B 1 395 THR 395 395 395 THR THR B . n 
B 1 396 PHE 396 396 396 PHE PHE B . n 
B 1 397 ILE 397 397 397 ILE ILE B . n 
B 1 398 THR 398 398 398 THR THR B . n 
B 1 399 LYS 399 399 399 LYS LYS B . n 
B 1 400 GLY 400 400 400 GLY GLY B . n 
B 1 401 THR 401 401 401 THR THR B . n 
B 1 402 TRP 402 402 402 TRP TRP B . n 
B 1 403 GLU 403 403 403 GLU GLU B . n 
B 1 404 VAL 404 404 404 VAL VAL B . n 
B 1 405 ILE 405 405 405 ILE ILE B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 ILE 407 407 407 ILE ILE B . n 
B 1 408 GLU 408 408 408 GLU GLU B . n 
B 1 409 ALA 409 409 409 ALA ALA B . n 
B 1 410 LEU 410 410 410 LEU LEU B . n 
B 1 411 THR 411 411 411 THR THR B . n 
B 1 412 SER 412 412 412 SER SER B . n 
B 1 413 ASP 413 413 413 ASP ASP B . n 
B 1 414 TYR 414 414 414 TYR TYR B . n 
B 1 415 LEU 415 415 415 LEU LEU B . n 
B 1 416 TYR 416 416 416 TYR TYR B . n 
B 1 417 TYR 417 417 417 TYR TYR B . n 
B 1 418 ILE 418 418 418 ILE ILE B . n 
B 1 419 SER 419 419 419 SER SER B . n 
B 1 420 ASN 420 420 420 ASN ASN B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 TYR 422 422 422 TYR TYR B . n 
B 1 423 LYS 423 423 423 LYS LYS B . n 
B 1 424 GLY 424 424 424 GLY GLY B . n 
B 1 425 MET 425 425 425 MET MET B . n 
B 1 426 PRO 426 426 426 PRO PRO B . n 
B 1 427 GLY 427 427 427 GLY GLY B . n 
B 1 428 GLY 428 428 428 GLY GLY B . n 
B 1 429 ARG 429 429 429 ARG ARG B . n 
B 1 430 ASN 430 430 430 ASN ASN B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 TYR 432 432 432 TYR TYR B . n 
B 1 433 LYS 433 433 433 LYS LYS B . n 
B 1 434 ILE 434 434 434 ILE ILE B . n 
B 1 435 GLN 435 435 435 GLN GLN B . n 
B 1 436 LEU 436 436 436 LEU LEU B . n 
B 1 437 SER 437 437 437 SER SER B . n 
B 1 438 ASP 438 438 438 ASP ASP B . n 
B 1 439 TYR 439 439 439 TYR TYR B . n 
B 1 440 THR 440 440 440 THR THR B . n 
B 1 441 LYS 441 441 441 LYS LYS B . n 
B 1 442 VAL 442 442 442 VAL VAL B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 CYS 444 444 444 CYS CYS B . n 
B 1 445 LEU 445 445 445 LEU LEU B . n 
B 1 446 SER 446 446 446 SER SER B . n 
B 1 447 CYS 447 447 447 CYS CYS B . n 
B 1 448 GLU 448 448 448 GLU GLU B . n 
B 1 449 LEU 449 449 449 LEU LEU B . n 
B 1 450 ASN 450 450 450 ASN ASN B . n 
B 1 451 PRO 451 451 451 PRO PRO B . n 
B 1 452 GLU 452 452 452 GLU GLU B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 CYS 454 454 454 CYS CYS B . n 
B 1 455 GLN 455 455 455 GLN GLN B . n 
B 1 456 TYR 456 456 456 TYR TYR B . n 
B 1 457 TYR 457 457 457 TYR TYR B . n 
B 1 458 SER 458 458 458 SER SER B . n 
B 1 459 VAL 459 459 459 VAL VAL B . n 
B 1 460 SER 460 460 460 SER SER B . n 
B 1 461 PHE 461 461 461 PHE PHE B . n 
B 1 462 SER 462 462 462 SER SER B . n 
B 1 463 LYS 463 463 463 LYS LYS B . n 
B 1 464 GLU 464 464 464 GLU GLU B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 LYS 466 466 466 LYS LYS B . n 
B 1 467 TYR 467 467 467 TYR TYR B . n 
B 1 468 TYR 468 468 468 TYR TYR B . n 
B 1 469 GLN 469 469 469 GLN GLN B . n 
B 1 470 LEU 470 470 470 LEU LEU B . n 
B 1 471 ARG 471 471 471 ARG ARG B . n 
B 1 472 CYS 472 472 472 CYS CYS B . n 
B 1 473 SER 473 473 473 SER SER B . n 
B 1 474 GLY 474 474 474 GLY GLY B . n 
B 1 475 PRO 475 475 475 PRO PRO B . n 
B 1 476 GLY 476 476 476 GLY GLY B . n 
B 1 477 LEU 477 477 477 LEU LEU B . n 
B 1 478 PRO 478 478 478 PRO PRO B . n 
B 1 479 LEU 479 479 479 LEU LEU B . n 
B 1 480 TYR 480 480 480 TYR TYR B . n 
B 1 481 THR 481 481 481 THR THR B . n 
B 1 482 LEU 482 482 482 LEU LEU B . n 
B 1 483 HIS 483 483 483 HIS HIS B . n 
B 1 484 SER 484 484 484 SER SER B . n 
B 1 485 SER 485 485 485 SER SER B . n 
B 1 486 VAL 486 486 486 VAL VAL B . n 
B 1 487 ASN 487 487 487 ASN ASN B . n 
B 1 488 ASP 488 488 488 ASP ASP B . n 
B 1 489 LYS 489 489 489 LYS LYS B . n 
B 1 490 GLY 490 490 490 GLY GLY B . n 
B 1 491 LEU 491 491 491 LEU LEU B . n 
B 1 492 ARG 492 492 492 ARG ARG B . n 
B 1 493 VAL 493 493 493 VAL VAL B . n 
B 1 494 LEU 494 494 494 LEU LEU B . n 
B 1 495 GLU 495 495 495 GLU GLU B . n 
B 1 496 ASP 496 496 496 ASP ASP B . n 
B 1 497 ASN 497 497 497 ASN ASN B . n 
B 1 498 SER 498 498 498 SER SER B . n 
B 1 499 ALA 499 499 499 ALA ALA B . n 
B 1 500 LEU 500 500 500 LEU LEU B . n 
B 1 501 ASP 501 501 501 ASP ASP B . n 
B 1 502 LYS 502 502 502 LYS LYS B . n 
B 1 503 MET 503 503 503 MET MET B . n 
B 1 504 LEU 504 504 504 LEU LEU B . n 
B 1 505 GLN 505 505 505 GLN GLN B . n 
B 1 506 ASN 506 506 506 ASN ASN B . n 
B 1 507 VAL 507 507 507 VAL VAL B . n 
B 1 508 GLN 508 508 508 GLN GLN B . n 
B 1 509 MET 509 509 509 MET MET B . n 
B 1 510 PRO 510 510 510 PRO PRO B . n 
B 1 511 SER 511 511 511 SER SER B . n 
B 1 512 LYS 512 512 512 LYS LYS B . n 
B 1 513 LYS 513 513 513 LYS LYS B . n 
B 1 514 LEU 514 514 514 LEU LEU B . n 
B 1 515 ASP 515 515 515 ASP ASP B . n 
B 1 516 PHE 516 516 516 PHE PHE B . n 
B 1 517 ILE 517 517 517 ILE ILE B . n 
B 1 518 ILE 518 518 518 ILE ILE B . n 
B 1 519 LEU 519 519 519 LEU LEU B . n 
B 1 520 ASN 520 520 520 ASN ASN B . n 
B 1 521 GLU 521 521 521 GLU GLU B . n 
B 1 522 THR 522 522 522 THR THR B . n 
B 1 523 LYS 523 523 523 LYS LYS B . n 
B 1 524 PHE 524 524 524 PHE PHE B . n 
B 1 525 TRP 525 525 525 TRP TRP B . n 
B 1 526 TYR 526 526 526 TYR TYR B . n 
B 1 527 GLN 527 527 527 GLN GLN B . n 
B 1 528 MET 528 528 528 MET MET B . n 
B 1 529 ILE 529 529 529 ILE ILE B . n 
B 1 530 LEU 530 530 530 LEU LEU B . n 
B 1 531 PRO 531 531 531 PRO PRO B . n 
B 1 532 PRO 532 532 532 PRO PRO B . n 
B 1 533 HIS 533 533 533 HIS HIS B . n 
B 1 534 PHE 534 534 534 PHE PHE B . n 
B 1 535 ASP 535 535 535 ASP ASP B . n 
B 1 536 LYS 536 536 536 LYS LYS B . n 
B 1 537 SER 537 537 537 SER SER B . n 
B 1 538 LYS 538 538 538 LYS LYS B . n 
B 1 539 LYS 539 539 539 LYS LYS B . n 
B 1 540 TYR 540 540 540 TYR TYR B . n 
B 1 541 PRO 541 541 541 PRO PRO B . n 
B 1 542 LEU 542 542 542 LEU LEU B . n 
B 1 543 LEU 543 543 543 LEU LEU B . n 
B 1 544 LEU 544 544 544 LEU LEU B . n 
B 1 545 ASP 545 545 545 ASP ASP B . n 
B 1 546 VAL 546 546 546 VAL VAL B . n 
B 1 547 TYR 547 547 547 TYR TYR B . n 
B 1 548 ALA 548 548 548 ALA ALA B . n 
B 1 549 GLY 549 549 549 GLY GLY B . n 
B 1 550 PRO 550 550 550 PRO PRO B . n 
B 1 551 CYS 551 551 551 CYS CYS B . n 
B 1 552 SER 552 552 552 SER SER B . n 
B 1 553 GLN 553 553 553 GLN GLN B . n 
B 1 554 LYS 554 554 554 LYS LYS B . n 
B 1 555 ALA 555 555 555 ALA ALA B . n 
B 1 556 ASP 556 556 556 ASP ASP B . n 
B 1 557 THR 557 557 557 THR THR B . n 
B 1 558 VAL 558 558 558 VAL VAL B . n 
B 1 559 PHE 559 559 559 PHE PHE B . n 
B 1 560 ARG 560 560 560 ARG ARG B . n 
B 1 561 LEU 561 561 561 LEU LEU B . n 
B 1 562 ASN 562 562 562 ASN ASN B . n 
B 1 563 TRP 563 563 563 TRP TRP B . n 
B 1 564 ALA 564 564 564 ALA ALA B . n 
B 1 565 THR 565 565 565 THR THR B . n 
B 1 566 TYR 566 566 566 TYR TYR B . n 
B 1 567 LEU 567 567 567 LEU LEU B . n 
B 1 568 ALA 568 568 568 ALA ALA B . n 
B 1 569 SER 569 569 569 SER SER B . n 
B 1 570 THR 570 570 570 THR THR B . n 
B 1 571 GLU 571 571 571 GLU GLU B . n 
B 1 572 ASN 572 572 572 ASN ASN B . n 
B 1 573 ILE 573 573 573 ILE ILE B . n 
B 1 574 ILE 574 574 574 ILE ILE B . n 
B 1 575 VAL 575 575 575 VAL VAL B . n 
B 1 576 ALA 576 576 576 ALA ALA B . n 
B 1 577 SER 577 577 577 SER SER B . n 
B 1 578 PHE 578 578 578 PHE PHE B . n 
B 1 579 ASP 579 579 579 ASP ASP B . n 
B 1 580 GLY 580 580 580 GLY GLY B . n 
B 1 581 ARG 581 581 581 ARG ARG B . n 
B 1 582 GLY 582 582 582 GLY GLY B . n 
B 1 583 SER 583 583 583 SER SER B . n 
B 1 584 GLY 584 584 584 GLY GLY B . n 
B 1 585 TYR 585 585 585 TYR TYR B . n 
B 1 586 GLN 586 586 586 GLN GLN B . n 
B 1 587 GLY 587 587 587 GLY GLY B . n 
B 1 588 ASP 588 588 588 ASP ASP B . n 
B 1 589 LYS 589 589 589 LYS LYS B . n 
B 1 590 ILE 590 590 590 ILE ILE B . n 
B 1 591 MET 591 591 591 MET MET B . n 
B 1 592 HIS 592 592 592 HIS HIS B . n 
B 1 593 ALA 593 593 593 ALA ALA B . n 
B 1 594 ILE 594 594 594 ILE ILE B . n 
B 1 595 ASN 595 595 595 ASN ASN B . n 
B 1 596 ARG 596 596 596 ARG ARG B . n 
B 1 597 ARG 597 597 597 ARG ARG B . n 
B 1 598 LEU 598 598 598 LEU LEU B . n 
B 1 599 GLY 599 599 599 GLY GLY B . n 
B 1 600 THR 600 600 600 THR THR B . n 
B 1 601 PHE 601 601 601 PHE PHE B . n 
B 1 602 GLU 602 602 602 GLU GLU B . n 
B 1 603 VAL 603 603 603 VAL VAL B . n 
B 1 604 GLU 604 604 604 GLU GLU B . n 
B 1 605 ASP 605 605 605 ASP ASP B . n 
B 1 606 GLN 606 606 606 GLN GLN B . n 
B 1 607 ILE 607 607 607 ILE ILE B . n 
B 1 608 GLU 608 608 608 GLU GLU B . n 
B 1 609 ALA 609 609 609 ALA ALA B . n 
B 1 610 ALA 610 610 610 ALA ALA B . n 
B 1 611 ARG 611 611 611 ARG ARG B . n 
B 1 612 GLN 612 612 612 GLN GLN B . n 
B 1 613 PHE 613 613 613 PHE PHE B . n 
B 1 614 SER 614 614 614 SER SER B . n 
B 1 615 LYS 615 615 615 LYS LYS B . n 
B 1 616 MET 616 616 616 MET MET B . n 
B 1 617 GLY 617 617 617 GLY GLY B . n 
B 1 618 PHE 618 618 618 PHE PHE B . n 
B 1 619 VAL 619 619 619 VAL VAL B . n 
B 1 620 ASP 620 620 620 ASP ASP B . n 
B 1 621 ASN 621 621 621 ASN ASN B . n 
B 1 622 LYS 622 622 622 LYS LYS B . n 
B 1 623 ARG 623 623 623 ARG ARG B . n 
B 1 624 ILE 624 624 624 ILE ILE B . n 
B 1 625 ALA 625 625 625 ALA ALA B . n 
B 1 626 ILE 626 626 626 ILE ILE B . n 
B 1 627 TRP 627 627 627 TRP TRP B . n 
B 1 628 GLY 628 628 628 GLY GLY B . n 
B 1 629 TRP 629 629 629 TRP TRP B . n 
B 1 630 SER 630 630 630 SER SER B . n 
B 1 631 TYR 631 631 631 TYR TYR B . n 
B 1 632 GLY 632 632 632 GLY GLY B . n 
B 1 633 GLY 633 633 633 GLY GLY B . n 
B 1 634 TYR 634 634 634 TYR TYR B . n 
B 1 635 VAL 635 635 635 VAL VAL B . n 
B 1 636 THR 636 636 636 THR THR B . n 
B 1 637 SER 637 637 637 SER SER B . n 
B 1 638 MET 638 638 638 MET MET B . n 
B 1 639 VAL 639 639 639 VAL VAL B . n 
B 1 640 LEU 640 640 640 LEU LEU B . n 
B 1 641 GLY 641 641 641 GLY GLY B . n 
B 1 642 SER 642 642 642 SER SER B . n 
B 1 643 GLY 643 643 643 GLY GLY B . n 
B 1 644 SER 644 644 644 SER SER B . n 
B 1 645 GLY 645 645 645 GLY GLY B . n 
B 1 646 VAL 646 646 646 VAL VAL B . n 
B 1 647 PHE 647 647 647 PHE PHE B . n 
B 1 648 LYS 648 648 648 LYS LYS B . n 
B 1 649 CYS 649 649 649 CYS CYS B . n 
B 1 650 GLY 650 650 650 GLY GLY B . n 
B 1 651 ILE 651 651 651 ILE ILE B . n 
B 1 652 ALA 652 652 652 ALA ALA B . n 
B 1 653 VAL 653 653 653 VAL VAL B . n 
B 1 654 ALA 654 654 654 ALA ALA B . n 
B 1 655 PRO 655 655 655 PRO PRO B . n 
B 1 656 VAL 656 656 656 VAL VAL B . n 
B 1 657 SER 657 657 657 SER SER B . n 
B 1 658 ARG 658 658 658 ARG ARG B . n 
B 1 659 TRP 659 659 659 TRP TRP B . n 
B 1 660 GLU 660 660 660 GLU GLU B . n 
B 1 661 TYR 661 661 661 TYR TYR B . n 
B 1 662 TYR 662 662 662 TYR TYR B . n 
B 1 663 ASP 663 663 663 ASP ASP B . n 
B 1 664 SER 664 664 664 SER SER B . n 
B 1 665 VAL 665 665 665 VAL VAL B . n 
B 1 666 TYR 666 666 666 TYR TYR B . n 
B 1 667 THR 667 667 667 THR THR B . n 
B 1 668 GLU 668 668 668 GLU GLU B . n 
B 1 669 ARG 669 669 669 ARG ARG B . n 
B 1 670 TYR 670 670 670 TYR TYR B . n 
B 1 671 MET 671 671 671 MET MET B . n 
B 1 672 GLY 672 672 672 GLY GLY B . n 
B 1 673 LEU 673 673 673 LEU LEU B . n 
B 1 674 PRO 674 674 674 PRO PRO B . n 
B 1 675 THR 675 675 675 THR THR B . n 
B 1 676 PRO 676 676 676 PRO PRO B . n 
B 1 677 GLU 677 677 677 GLU GLU B . n 
B 1 678 ASP 678 678 678 ASP ASP B . n 
B 1 679 ASN 679 679 679 ASN ASN B . n 
B 1 680 LEU 680 680 680 LEU LEU B . n 
B 1 681 ASP 681 681 681 ASP ASP B . n 
B 1 682 HIS 682 682 682 HIS HIS B . n 
B 1 683 TYR 683 683 683 TYR TYR B . n 
B 1 684 ARG 684 684 684 ARG ARG B . n 
B 1 685 ASN 685 685 685 ASN ASN B . n 
B 1 686 SER 686 686 686 SER SER B . n 
B 1 687 THR 687 687 687 THR THR B . n 
B 1 688 VAL 688 688 688 VAL VAL B . n 
B 1 689 MET 689 689 689 MET MET B . n 
B 1 690 SER 690 690 690 SER SER B . n 
B 1 691 ARG 691 691 691 ARG ARG B . n 
B 1 692 ALA 692 692 692 ALA ALA B . n 
B 1 693 GLU 693 693 693 GLU GLU B . n 
B 1 694 ASN 694 694 694 ASN ASN B . n 
B 1 695 PHE 695 695 695 PHE PHE B . n 
B 1 696 LYS 696 696 696 LYS LYS B . n 
B 1 697 GLN 697 697 697 GLN GLN B . n 
B 1 698 VAL 698 698 698 VAL VAL B . n 
B 1 699 GLU 699 699 699 GLU GLU B . n 
B 1 700 TYR 700 700 700 TYR TYR B . n 
B 1 701 LEU 701 701 701 LEU LEU B . n 
B 1 702 LEU 702 702 702 LEU LEU B . n 
B 1 703 ILE 703 703 703 ILE ILE B . n 
B 1 704 HIS 704 704 704 HIS HIS B . n 
B 1 705 GLY 705 705 705 GLY GLY B . n 
B 1 706 THR 706 706 706 THR THR B . n 
B 1 707 ALA 707 707 707 ALA ALA B . n 
B 1 708 ASP 708 708 708 ASP ASP B . n 
B 1 709 ASP 709 709 709 ASP ASP B . n 
B 1 710 ASN 710 710 710 ASN ASN B . n 
B 1 711 VAL 711 711 711 VAL VAL B . n 
B 1 712 HIS 712 712 712 HIS HIS B . n 
B 1 713 PHE 713 713 713 PHE PHE B . n 
B 1 714 GLN 714 714 714 GLN GLN B . n 
B 1 715 GLN 715 715 715 GLN GLN B . n 
B 1 716 SER 716 716 716 SER SER B . n 
B 1 717 ALA 717 717 717 ALA ALA B . n 
B 1 718 GLN 718 718 718 GLN GLN B . n 
B 1 719 ILE 719 719 719 ILE ILE B . n 
B 1 720 SER 720 720 720 SER SER B . n 
B 1 721 LYS 721 721 721 LYS LYS B . n 
B 1 722 ALA 722 722 722 ALA ALA B . n 
B 1 723 LEU 723 723 723 LEU LEU B . n 
B 1 724 VAL 724 724 724 VAL VAL B . n 
B 1 725 ASP 725 725 725 ASP ASP B . n 
B 1 726 VAL 726 726 726 VAL VAL B . n 
B 1 727 GLY 727 727 727 GLY GLY B . n 
B 1 728 VAL 728 728 728 VAL VAL B . n 
B 1 729 ASP 729 729 729 ASP ASP B . n 
B 1 730 PHE 730 730 730 PHE PHE B . n 
B 1 731 GLN 731 731 731 GLN GLN B . n 
B 1 732 ALA 732 732 732 ALA ALA B . n 
B 1 733 MET 733 733 733 MET MET B . n 
B 1 734 TRP 734 734 734 TRP TRP B . n 
B 1 735 TYR 735 735 735 TYR TYR B . n 
B 1 736 THR 736 736 736 THR THR B . n 
B 1 737 ASP 737 737 737 ASP ASP B . n 
B 1 738 GLU 738 738 738 GLU GLU B . n 
B 1 739 ASP 739 739 739 ASP ASP B . n 
B 1 740 HIS 740 740 740 HIS HIS B . n 
B 1 741 GLY 741 741 741 GLY GLY B . n 
B 1 742 ILE 742 742 742 ILE ILE B . n 
B 1 743 ALA 743 743 743 ALA ALA B . n 
B 1 744 SER 744 744 744 SER SER B . n 
B 1 745 SER 745 745 745 SER SER B . n 
B 1 746 THR 746 746 746 THR THR B . n 
B 1 747 ALA 747 747 747 ALA ALA B . n 
B 1 748 HIS 748 748 748 HIS HIS B . n 
B 1 749 GLN 749 749 749 GLN GLN B . n 
B 1 750 HIS 750 750 750 HIS HIS B . n 
B 1 751 ILE 751 751 751 ILE ILE B . n 
B 1 752 TYR 752 752 752 TYR TYR B . n 
B 1 753 THR 753 753 753 THR THR B . n 
B 1 754 HIS 754 754 754 HIS HIS B . n 
B 1 755 MET 755 755 755 MET MET B . n 
B 1 756 SER 756 756 756 SER SER B . n 
B 1 757 HIS 757 757 757 HIS HIS B . n 
B 1 758 PHE 758 758 758 PHE PHE B . n 
B 1 759 ILE 759 759 759 ILE ILE B . n 
B 1 760 LYS 760 760 760 LYS LYS B . n 
B 1 761 GLN 761 761 761 GLN GLN B . n 
B 1 762 CYS 762 762 762 CYS CYS B . n 
B 1 763 PHE 763 763 763 PHE PHE B . n 
B 1 764 SER 764 764 764 SER SER B . n 
B 1 765 LEU 765 765 765 LEU LEU B . n 
B 1 766 PRO 766 766 766 PRO PRO B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2 NAG 1   1092 1092 NAG NAG A . 
D  2 NAG 1   1281 1281 NAG NAG A . 
E  2 NAG 1   1520 1520 NAG NAG A . 
F  3 NA  1   1521 1521 NA  NA  A . 
G  4 524 1   1522 1522 524 524 A . 
H  2 NAG 1   2092 2092 NAG NAG B . 
I  2 NAG 1   2150 2150 NAG NAG B . 
J  2 NAG 1   2321 2321 NAG NAG B . 
K  4 524 1   2322 2322 524 524 B . 
L  2 NAG 1   1085 1085 NAG NAG L . 
M  5 NDG 2   1086 1086 NDG NDG L . 
N  5 NDG 1   1150 1150 NDG NDG M . 
O  2 NAG 2   1151 1151 NAG NAG M . 
P  2 NAG 1   1219 1219 NAG NAG N . 
Q  2 NAG 2   1220 1220 NAG NAG N . 
R  2 NAG 1   1229 1229 NAG NAG O . 
S  5 NDG 2   1230 1230 NDG NDG O . 
T  5 NDG 1   1321 1321 NDG NDG P . 
U  2 NAG 2   1322 1322 NAG NAG P . 
V  2 NAG 1   2085 2085 NAG NAG Q . 
W  2 NAG 2   2086 2086 NAG NAG Q . 
X  2 NAG 1   2219 2219 NAG NAG R . 
Y  2 NAG 2   2220 2220 NAG NAG R . 
Z  2 NAG 1   2229 2229 NAG NAG S . 
AA 2 NAG 2   2230 2230 NAG NAG S . 
BA 2 NAG 1   2281 2281 NAG NAG T . 
CA 2 NAG 2   2282 2282 NAG NAG T . 
DA 6 HOH 1   1523 1523 HOH HOH A . 
DA 6 HOH 2   1524 1524 HOH HOH A . 
DA 6 HOH 3   1525 1525 HOH HOH A . 
DA 6 HOH 4   1526 1526 HOH HOH A . 
DA 6 HOH 5   1527 1527 HOH HOH A . 
DA 6 HOH 6   1528 1528 HOH HOH A . 
DA 6 HOH 7   1529 1529 HOH HOH A . 
DA 6 HOH 8   1530 1530 HOH HOH A . 
DA 6 HOH 9   1531 1531 HOH HOH A . 
DA 6 HOH 10  1532 1532 HOH HOH A . 
DA 6 HOH 11  1533 1533 HOH HOH A . 
DA 6 HOH 12  1534 1534 HOH HOH A . 
DA 6 HOH 13  1535 1535 HOH HOH A . 
DA 6 HOH 14  1536 1536 HOH HOH A . 
DA 6 HOH 15  1537 1537 HOH HOH A . 
DA 6 HOH 16  1538 1538 HOH HOH A . 
DA 6 HOH 17  1539 1539 HOH HOH A . 
DA 6 HOH 18  1540 1540 HOH HOH A . 
DA 6 HOH 19  1541 1541 HOH HOH A . 
DA 6 HOH 20  1542 1542 HOH HOH A . 
DA 6 HOH 21  1543 1543 HOH HOH A . 
DA 6 HOH 22  1544 1544 HOH HOH A . 
DA 6 HOH 23  1545 1545 HOH HOH A . 
DA 6 HOH 24  1546 1546 HOH HOH A . 
DA 6 HOH 25  1547 1547 HOH HOH A . 
DA 6 HOH 26  1548 1548 HOH HOH A . 
DA 6 HOH 27  1549 1549 HOH HOH A . 
DA 6 HOH 28  1550 1550 HOH HOH A . 
DA 6 HOH 29  1551 1551 HOH HOH A . 
DA 6 HOH 30  1552 1552 HOH HOH A . 
DA 6 HOH 31  1553 1553 HOH HOH A . 
DA 6 HOH 32  1554 1554 HOH HOH A . 
DA 6 HOH 33  1555 1555 HOH HOH A . 
DA 6 HOH 34  1556 1556 HOH HOH A . 
DA 6 HOH 35  1557 1557 HOH HOH A . 
DA 6 HOH 36  1558 1558 HOH HOH A . 
DA 6 HOH 37  1559 1559 HOH HOH A . 
DA 6 HOH 38  1560 1560 HOH HOH A . 
DA 6 HOH 39  1561 1561 HOH HOH A . 
DA 6 HOH 40  1562 1562 HOH HOH A . 
DA 6 HOH 41  1563 1563 HOH HOH A . 
DA 6 HOH 42  1564 1564 HOH HOH A . 
DA 6 HOH 43  1565 1565 HOH HOH A . 
DA 6 HOH 44  1566 1566 HOH HOH A . 
DA 6 HOH 45  1567 1567 HOH HOH A . 
DA 6 HOH 46  1568 1568 HOH HOH A . 
DA 6 HOH 47  1569 1569 HOH HOH A . 
DA 6 HOH 48  1570 1570 HOH HOH A . 
DA 6 HOH 49  1571 1571 HOH HOH A . 
DA 6 HOH 50  1572 1572 HOH HOH A . 
DA 6 HOH 51  1573 1573 HOH HOH A . 
DA 6 HOH 52  1574 1574 HOH HOH A . 
DA 6 HOH 53  1575 1575 HOH HOH A . 
DA 6 HOH 54  1576 1576 HOH HOH A . 
DA 6 HOH 55  1577 1577 HOH HOH A . 
DA 6 HOH 56  1578 1578 HOH HOH A . 
DA 6 HOH 57  1579 1579 HOH HOH A . 
DA 6 HOH 58  1580 1580 HOH HOH A . 
DA 6 HOH 59  1581 1581 HOH HOH A . 
DA 6 HOH 60  1582 1582 HOH HOH A . 
DA 6 HOH 61  1583 1583 HOH HOH A . 
DA 6 HOH 62  1584 1584 HOH HOH A . 
DA 6 HOH 63  1585 1585 HOH HOH A . 
DA 6 HOH 64  1586 1586 HOH HOH A . 
DA 6 HOH 65  1587 1587 HOH HOH A . 
DA 6 HOH 66  1588 1588 HOH HOH A . 
DA 6 HOH 67  1589 1589 HOH HOH A . 
DA 6 HOH 68  1590 1590 HOH HOH A . 
DA 6 HOH 69  1591 1591 HOH HOH A . 
DA 6 HOH 70  1592 1592 HOH HOH A . 
DA 6 HOH 71  1593 1593 HOH HOH A . 
DA 6 HOH 72  1594 1594 HOH HOH A . 
DA 6 HOH 73  1595 1595 HOH HOH A . 
DA 6 HOH 74  1596 1596 HOH HOH A . 
DA 6 HOH 75  1597 1597 HOH HOH A . 
DA 6 HOH 76  1598 1598 HOH HOH A . 
DA 6 HOH 77  1599 1599 HOH HOH A . 
DA 6 HOH 78  1600 1600 HOH HOH A . 
DA 6 HOH 79  1601 1601 HOH HOH A . 
DA 6 HOH 80  1602 1602 HOH HOH A . 
DA 6 HOH 81  1603 1603 HOH HOH A . 
DA 6 HOH 82  1604 1604 HOH HOH A . 
DA 6 HOH 83  1605 1605 HOH HOH A . 
DA 6 HOH 84  1606 1606 HOH HOH A . 
DA 6 HOH 85  1607 1607 HOH HOH A . 
DA 6 HOH 86  1608 1608 HOH HOH A . 
DA 6 HOH 87  1609 1609 HOH HOH A . 
DA 6 HOH 88  1610 1610 HOH HOH A . 
DA 6 HOH 89  1611 1611 HOH HOH A . 
DA 6 HOH 90  1612 1612 HOH HOH A . 
DA 6 HOH 91  1613 1613 HOH HOH A . 
DA 6 HOH 92  1614 1614 HOH HOH A . 
DA 6 HOH 93  1615 1615 HOH HOH A . 
DA 6 HOH 94  1616 1616 HOH HOH A . 
DA 6 HOH 95  1617 1617 HOH HOH A . 
DA 6 HOH 96  1618 1618 HOH HOH A . 
DA 6 HOH 97  1619 1619 HOH HOH A . 
DA 6 HOH 98  1620 1620 HOH HOH A . 
DA 6 HOH 99  1621 1621 HOH HOH A . 
DA 6 HOH 100 1622 1622 HOH HOH A . 
DA 6 HOH 101 1623 1623 HOH HOH A . 
DA 6 HOH 102 1624 1624 HOH HOH A . 
DA 6 HOH 103 1625 1625 HOH HOH A . 
DA 6 HOH 104 1626 1626 HOH HOH A . 
DA 6 HOH 105 1627 1627 HOH HOH A . 
DA 6 HOH 106 1628 1628 HOH HOH A . 
DA 6 HOH 107 1629 1629 HOH HOH A . 
DA 6 HOH 108 1630 1630 HOH HOH A . 
DA 6 HOH 109 1631 1631 HOH HOH A . 
DA 6 HOH 110 1632 1632 HOH HOH A . 
DA 6 HOH 111 1633 1633 HOH HOH A . 
DA 6 HOH 112 1634 1634 HOH HOH A . 
DA 6 HOH 113 1635 1635 HOH HOH A . 
DA 6 HOH 114 1636 1636 HOH HOH A . 
DA 6 HOH 115 1637 1637 HOH HOH A . 
DA 6 HOH 116 1638 1638 HOH HOH A . 
DA 6 HOH 117 1639 1639 HOH HOH A . 
DA 6 HOH 118 1640 1640 HOH HOH A . 
DA 6 HOH 119 1641 1641 HOH HOH A . 
DA 6 HOH 120 1642 1642 HOH HOH A . 
DA 6 HOH 121 1643 1643 HOH HOH A . 
DA 6 HOH 122 1644 1644 HOH HOH A . 
DA 6 HOH 123 1645 1645 HOH HOH A . 
DA 6 HOH 124 1646 1646 HOH HOH A . 
DA 6 HOH 125 1647 1647 HOH HOH A . 
DA 6 HOH 126 1648 1648 HOH HOH A . 
DA 6 HOH 127 1649 1649 HOH HOH A . 
DA 6 HOH 128 1650 1650 HOH HOH A . 
DA 6 HOH 129 1651 1651 HOH HOH A . 
DA 6 HOH 130 1652 1652 HOH HOH A . 
DA 6 HOH 131 1653 1653 HOH HOH A . 
DA 6 HOH 132 1654 1654 HOH HOH A . 
DA 6 HOH 133 1655 1655 HOH HOH A . 
DA 6 HOH 134 1656 1656 HOH HOH A . 
DA 6 HOH 135 1657 1657 HOH HOH A . 
DA 6 HOH 136 1658 1658 HOH HOH A . 
DA 6 HOH 137 1659 1659 HOH HOH A . 
DA 6 HOH 138 1660 1660 HOH HOH A . 
DA 6 HOH 139 1661 1661 HOH HOH A . 
DA 6 HOH 140 1662 1662 HOH HOH A . 
DA 6 HOH 141 1663 1663 HOH HOH A . 
DA 6 HOH 142 1664 1664 HOH HOH A . 
DA 6 HOH 143 1665 1665 HOH HOH A . 
DA 6 HOH 144 1666 1666 HOH HOH A . 
DA 6 HOH 145 1667 1667 HOH HOH A . 
DA 6 HOH 146 1668 1668 HOH HOH A . 
DA 6 HOH 147 1669 1669 HOH HOH A . 
DA 6 HOH 148 1670 1670 HOH HOH A . 
DA 6 HOH 149 1671 1671 HOH HOH A . 
DA 6 HOH 150 1672 1672 HOH HOH A . 
DA 6 HOH 151 1673 1673 HOH HOH A . 
DA 6 HOH 152 1674 1674 HOH HOH A . 
DA 6 HOH 153 1675 1675 HOH HOH A . 
DA 6 HOH 154 1676 1676 HOH HOH A . 
DA 6 HOH 155 1677 1677 HOH HOH A . 
DA 6 HOH 156 1678 1678 HOH HOH A . 
DA 6 HOH 157 1679 1679 HOH HOH A . 
DA 6 HOH 158 1680 1680 HOH HOH A . 
DA 6 HOH 159 1681 1681 HOH HOH A . 
DA 6 HOH 160 1682 1682 HOH HOH A . 
DA 6 HOH 161 1683 1683 HOH HOH A . 
DA 6 HOH 162 1684 1684 HOH HOH A . 
DA 6 HOH 163 1685 1685 HOH HOH A . 
DA 6 HOH 164 1686 1686 HOH HOH A . 
DA 6 HOH 165 1687 1687 HOH HOH A . 
DA 6 HOH 166 1688 1688 HOH HOH A . 
DA 6 HOH 167 1689 1689 HOH HOH A . 
DA 6 HOH 168 1690 1690 HOH HOH A . 
DA 6 HOH 169 1691 1691 HOH HOH A . 
DA 6 HOH 170 1692 1692 HOH HOH A . 
DA 6 HOH 171 1693 1693 HOH HOH A . 
DA 6 HOH 172 1694 1694 HOH HOH A . 
DA 6 HOH 173 1695 1695 HOH HOH A . 
DA 6 HOH 174 1696 1696 HOH HOH A . 
DA 6 HOH 175 1697 1697 HOH HOH A . 
DA 6 HOH 176 1698 1698 HOH HOH A . 
DA 6 HOH 177 1699 1699 HOH HOH A . 
DA 6 HOH 178 1700 1700 HOH HOH A . 
DA 6 HOH 179 1701 1701 HOH HOH A . 
DA 6 HOH 180 1702 1702 HOH HOH A . 
DA 6 HOH 181 1703 1703 HOH HOH A . 
DA 6 HOH 182 1704 1704 HOH HOH A . 
DA 6 HOH 183 1705 1705 HOH HOH A . 
DA 6 HOH 184 1706 1706 HOH HOH A . 
DA 6 HOH 185 1707 1707 HOH HOH A . 
DA 6 HOH 186 1708 1708 HOH HOH A . 
DA 6 HOH 187 1709 1709 HOH HOH A . 
DA 6 HOH 188 1710 1710 HOH HOH A . 
DA 6 HOH 189 1711 1711 HOH HOH A . 
DA 6 HOH 190 1712 1712 HOH HOH A . 
DA 6 HOH 191 1713 1713 HOH HOH A . 
DA 6 HOH 192 1714 1714 HOH HOH A . 
DA 6 HOH 193 1715 1715 HOH HOH A . 
DA 6 HOH 194 1716 1716 HOH HOH A . 
DA 6 HOH 195 1717 1717 HOH HOH A . 
DA 6 HOH 196 1718 1718 HOH HOH A . 
DA 6 HOH 197 1719 1719 HOH HOH A . 
DA 6 HOH 198 1720 1720 HOH HOH A . 
DA 6 HOH 199 1721 1721 HOH HOH A . 
DA 6 HOH 200 1722 1722 HOH HOH A . 
DA 6 HOH 201 1723 1723 HOH HOH A . 
DA 6 HOH 202 1724 1724 HOH HOH A . 
DA 6 HOH 203 1725 1725 HOH HOH A . 
DA 6 HOH 204 1726 1726 HOH HOH A . 
DA 6 HOH 205 1727 1727 HOH HOH A . 
DA 6 HOH 206 1728 1728 HOH HOH A . 
DA 6 HOH 207 1729 1729 HOH HOH A . 
DA 6 HOH 208 1730 1730 HOH HOH A . 
DA 6 HOH 209 1731 1731 HOH HOH A . 
DA 6 HOH 210 1732 1732 HOH HOH A . 
DA 6 HOH 211 1733 1733 HOH HOH A . 
DA 6 HOH 212 1734 1734 HOH HOH A . 
DA 6 HOH 213 1735 1735 HOH HOH A . 
DA 6 HOH 214 1736 1736 HOH HOH A . 
DA 6 HOH 215 1737 1737 HOH HOH A . 
DA 6 HOH 216 1738 1738 HOH HOH A . 
DA 6 HOH 217 1739 1739 HOH HOH A . 
DA 6 HOH 218 1740 1740 HOH HOH A . 
DA 6 HOH 219 1741 1741 HOH HOH A . 
DA 6 HOH 220 1742 1742 HOH HOH A . 
DA 6 HOH 221 1743 1743 HOH HOH A . 
DA 6 HOH 222 1744 1744 HOH HOH A . 
DA 6 HOH 223 1745 1745 HOH HOH A . 
DA 6 HOH 224 1746 1746 HOH HOH A . 
DA 6 HOH 225 1747 1747 HOH HOH A . 
DA 6 HOH 226 1748 1748 HOH HOH A . 
DA 6 HOH 227 1749 1749 HOH HOH A . 
DA 6 HOH 228 1750 1750 HOH HOH A . 
DA 6 HOH 229 1751 1751 HOH HOH A . 
DA 6 HOH 230 1752 1752 HOH HOH A . 
DA 6 HOH 231 1753 1753 HOH HOH A . 
DA 6 HOH 232 1754 1754 HOH HOH A . 
DA 6 HOH 233 1755 1755 HOH HOH A . 
DA 6 HOH 234 1756 1756 HOH HOH A . 
DA 6 HOH 235 1757 1757 HOH HOH A . 
DA 6 HOH 236 1758 1758 HOH HOH A . 
DA 6 HOH 237 1759 1759 HOH HOH A . 
DA 6 HOH 238 1760 1760 HOH HOH A . 
DA 6 HOH 239 1761 1761 HOH HOH A . 
DA 6 HOH 240 1762 1762 HOH HOH A . 
DA 6 HOH 241 1763 1763 HOH HOH A . 
DA 6 HOH 242 1764 1764 HOH HOH A . 
DA 6 HOH 243 1765 1765 HOH HOH A . 
DA 6 HOH 244 1766 1766 HOH HOH A . 
DA 6 HOH 245 1767 1767 HOH HOH A . 
DA 6 HOH 246 1768 1768 HOH HOH A . 
DA 6 HOH 247 1769 1769 HOH HOH A . 
DA 6 HOH 248 1770 1770 HOH HOH A . 
DA 6 HOH 249 1771 1771 HOH HOH A . 
DA 6 HOH 250 1772 1772 HOH HOH A . 
DA 6 HOH 251 1773 1773 HOH HOH A . 
DA 6 HOH 252 1774 1774 HOH HOH A . 
DA 6 HOH 253 1775 1775 HOH HOH A . 
DA 6 HOH 254 1776 1776 HOH HOH A . 
DA 6 HOH 255 1777 1777 HOH HOH A . 
DA 6 HOH 256 1778 1778 HOH HOH A . 
DA 6 HOH 257 1779 1779 HOH HOH A . 
DA 6 HOH 258 1780 1780 HOH HOH A . 
DA 6 HOH 259 1781 1781 HOH HOH A . 
DA 6 HOH 260 1782 1782 HOH HOH A . 
DA 6 HOH 261 1783 1783 HOH HOH A . 
DA 6 HOH 262 1784 1784 HOH HOH A . 
DA 6 HOH 263 1785 1785 HOH HOH A . 
DA 6 HOH 264 1786 1786 HOH HOH A . 
DA 6 HOH 265 1787 1787 HOH HOH A . 
DA 6 HOH 266 1788 1788 HOH HOH A . 
DA 6 HOH 267 1789 1789 HOH HOH A . 
DA 6 HOH 268 1790 1790 HOH HOH A . 
DA 6 HOH 269 1791 1791 HOH HOH A . 
DA 6 HOH 270 1792 1792 HOH HOH A . 
DA 6 HOH 271 1793 1793 HOH HOH A . 
DA 6 HOH 272 1794 1794 HOH HOH A . 
DA 6 HOH 273 1795 1795 HOH HOH A . 
DA 6 HOH 274 1796 1796 HOH HOH A . 
DA 6 HOH 275 1797 1797 HOH HOH A . 
DA 6 HOH 276 1798 1798 HOH HOH A . 
DA 6 HOH 277 1799 1799 HOH HOH A . 
DA 6 HOH 278 1800 1800 HOH HOH A . 
DA 6 HOH 279 1801 1801 HOH HOH A . 
DA 6 HOH 280 1802 1802 HOH HOH A . 
DA 6 HOH 281 1803 1803 HOH HOH A . 
DA 6 HOH 282 1804 1804 HOH HOH A . 
DA 6 HOH 283 1805 1805 HOH HOH A . 
DA 6 HOH 284 1806 1806 HOH HOH A . 
DA 6 HOH 285 1807 1807 HOH HOH A . 
DA 6 HOH 286 1808 1808 HOH HOH A . 
DA 6 HOH 287 1809 1809 HOH HOH A . 
DA 6 HOH 288 1810 1810 HOH HOH A . 
DA 6 HOH 289 1811 1811 HOH HOH A . 
DA 6 HOH 290 1812 1812 HOH HOH A . 
DA 6 HOH 291 1813 1813 HOH HOH A . 
DA 6 HOH 292 1814 1814 HOH HOH A . 
DA 6 HOH 293 1815 1815 HOH HOH A . 
DA 6 HOH 294 1816 1816 HOH HOH A . 
DA 6 HOH 295 1817 1817 HOH HOH A . 
DA 6 HOH 296 1818 1818 HOH HOH A . 
DA 6 HOH 297 1819 1819 HOH HOH A . 
DA 6 HOH 298 1820 1820 HOH HOH A . 
DA 6 HOH 299 1821 1821 HOH HOH A . 
DA 6 HOH 300 1822 1822 HOH HOH A . 
DA 6 HOH 301 1823 1823 HOH HOH A . 
DA 6 HOH 302 1824 1824 HOH HOH A . 
DA 6 HOH 303 1825 1825 HOH HOH A . 
DA 6 HOH 304 1826 1826 HOH HOH A . 
DA 6 HOH 305 1827 1827 HOH HOH A . 
DA 6 HOH 306 1828 1828 HOH HOH A . 
DA 6 HOH 307 1829 1829 HOH HOH A . 
DA 6 HOH 308 1830 1830 HOH HOH A . 
DA 6 HOH 309 1831 1831 HOH HOH A . 
DA 6 HOH 310 1832 1832 HOH HOH A . 
DA 6 HOH 311 1833 1833 HOH HOH A . 
DA 6 HOH 312 1834 1834 HOH HOH A . 
DA 6 HOH 313 1835 1835 HOH HOH A . 
DA 6 HOH 314 1836 1836 HOH HOH A . 
DA 6 HOH 315 1837 1837 HOH HOH A . 
DA 6 HOH 316 1838 1838 HOH HOH A . 
DA 6 HOH 317 1839 1839 HOH HOH A . 
DA 6 HOH 318 1840 1840 HOH HOH A . 
DA 6 HOH 319 1841 1841 HOH HOH A . 
DA 6 HOH 320 1842 1842 HOH HOH A . 
DA 6 HOH 321 1843 1843 HOH HOH A . 
DA 6 HOH 322 1844 1844 HOH HOH A . 
DA 6 HOH 323 1845 1845 HOH HOH A . 
DA 6 HOH 324 1846 1846 HOH HOH A . 
DA 6 HOH 325 1847 1847 HOH HOH A . 
DA 6 HOH 326 1848 1848 HOH HOH A . 
DA 6 HOH 327 1849 1849 HOH HOH A . 
DA 6 HOH 328 1850 1850 HOH HOH A . 
DA 6 HOH 329 1851 1851 HOH HOH A . 
DA 6 HOH 330 1852 1852 HOH HOH A . 
DA 6 HOH 331 1853 1853 HOH HOH A . 
DA 6 HOH 332 1854 1854 HOH HOH A . 
DA 6 HOH 333 1855 1855 HOH HOH A . 
DA 6 HOH 334 1856 1856 HOH HOH A . 
DA 6 HOH 335 1857 1857 HOH HOH A . 
DA 6 HOH 336 1858 1858 HOH HOH A . 
DA 6 HOH 337 1859 1859 HOH HOH A . 
DA 6 HOH 338 1860 1860 HOH HOH A . 
DA 6 HOH 339 1861 1861 HOH HOH A . 
DA 6 HOH 340 1862 1862 HOH HOH A . 
DA 6 HOH 341 1863 1863 HOH HOH A . 
DA 6 HOH 342 1864 1864 HOH HOH A . 
DA 6 HOH 343 1865 1865 HOH HOH A . 
DA 6 HOH 344 1866 1866 HOH HOH A . 
DA 6 HOH 345 1867 1867 HOH HOH A . 
DA 6 HOH 346 1868 1868 HOH HOH A . 
DA 6 HOH 347 1869 1869 HOH HOH A . 
DA 6 HOH 348 1870 1870 HOH HOH A . 
DA 6 HOH 349 1871 1871 HOH HOH A . 
DA 6 HOH 350 1872 1872 HOH HOH A . 
DA 6 HOH 351 1873 1873 HOH HOH A . 
DA 6 HOH 352 1874 1874 HOH HOH A . 
DA 6 HOH 353 1875 1875 HOH HOH A . 
DA 6 HOH 354 1876 1876 HOH HOH A . 
DA 6 HOH 355 1877 1877 HOH HOH A . 
DA 6 HOH 356 1878 1878 HOH HOH A . 
DA 6 HOH 357 1879 1879 HOH HOH A . 
DA 6 HOH 358 1880 1880 HOH HOH A . 
DA 6 HOH 359 1881 1881 HOH HOH A . 
DA 6 HOH 360 1882 1882 HOH HOH A . 
DA 6 HOH 361 1883 1883 HOH HOH A . 
DA 6 HOH 362 1884 1884 HOH HOH A . 
DA 6 HOH 363 1885 1885 HOH HOH A . 
DA 6 HOH 364 1886 1886 HOH HOH A . 
DA 6 HOH 365 1887 1887 HOH HOH A . 
DA 6 HOH 366 1888 1888 HOH HOH A . 
DA 6 HOH 367 1889 1889 HOH HOH A . 
DA 6 HOH 368 1890 1890 HOH HOH A . 
DA 6 HOH 369 1891 1891 HOH HOH A . 
DA 6 HOH 370 1892 1892 HOH HOH A . 
DA 6 HOH 371 1893 1893 HOH HOH A . 
DA 6 HOH 372 1894 1894 HOH HOH A . 
DA 6 HOH 373 1895 1895 HOH HOH A . 
DA 6 HOH 374 1896 1896 HOH HOH A . 
DA 6 HOH 375 1897 1897 HOH HOH A . 
DA 6 HOH 376 1898 1898 HOH HOH A . 
DA 6 HOH 377 1899 1899 HOH HOH A . 
DA 6 HOH 378 1900 1900 HOH HOH A . 
DA 6 HOH 379 1901 1901 HOH HOH A . 
DA 6 HOH 380 1902 1902 HOH HOH A . 
DA 6 HOH 381 1903 1903 HOH HOH A . 
DA 6 HOH 382 1904 1904 HOH HOH A . 
DA 6 HOH 383 1905 1905 HOH HOH A . 
DA 6 HOH 384 1906 1906 HOH HOH A . 
DA 6 HOH 385 1907 1907 HOH HOH A . 
DA 6 HOH 386 1908 1908 HOH HOH A . 
DA 6 HOH 387 1909 1909 HOH HOH A . 
DA 6 HOH 388 1910 1910 HOH HOH A . 
DA 6 HOH 389 1911 1911 HOH HOH A . 
DA 6 HOH 390 1912 1912 HOH HOH A . 
DA 6 HOH 391 1913 1913 HOH HOH A . 
DA 6 HOH 392 1914 1914 HOH HOH A . 
DA 6 HOH 393 1915 1915 HOH HOH A . 
DA 6 HOH 394 1916 1916 HOH HOH A . 
DA 6 HOH 395 1917 1917 HOH HOH A . 
DA 6 HOH 396 1918 1918 HOH HOH A . 
DA 6 HOH 397 1919 1919 HOH HOH A . 
DA 6 HOH 398 1920 1920 HOH HOH A . 
DA 6 HOH 399 1921 1921 HOH HOH A . 
DA 6 HOH 400 1922 1922 HOH HOH A . 
DA 6 HOH 401 1923 1923 HOH HOH A . 
DA 6 HOH 402 1924 1924 HOH HOH A . 
DA 6 HOH 403 1925 1925 HOH HOH A . 
DA 6 HOH 404 1926 1926 HOH HOH A . 
DA 6 HOH 405 1927 1927 HOH HOH A . 
DA 6 HOH 406 1928 1928 HOH HOH A . 
DA 6 HOH 407 1929 1929 HOH HOH A . 
DA 6 HOH 408 1930 1930 HOH HOH A . 
DA 6 HOH 409 1931 1931 HOH HOH A . 
DA 6 HOH 410 1932 1932 HOH HOH A . 
DA 6 HOH 411 1933 1933 HOH HOH A . 
DA 6 HOH 412 1934 1934 HOH HOH A . 
DA 6 HOH 413 1935 1935 HOH HOH A . 
DA 6 HOH 414 1936 1936 HOH HOH A . 
DA 6 HOH 415 1937 1937 HOH HOH A . 
DA 6 HOH 416 1938 1938 HOH HOH A . 
DA 6 HOH 417 1939 1939 HOH HOH A . 
DA 6 HOH 418 1940 1940 HOH HOH A . 
DA 6 HOH 419 1941 1941 HOH HOH A . 
DA 6 HOH 420 1942 1942 HOH HOH A . 
DA 6 HOH 421 1943 1943 HOH HOH A . 
DA 6 HOH 422 1944 1944 HOH HOH A . 
DA 6 HOH 423 1945 1945 HOH HOH A . 
DA 6 HOH 424 1946 1946 HOH HOH A . 
DA 6 HOH 425 1947 1947 HOH HOH A . 
DA 6 HOH 426 1948 1948 HOH HOH A . 
DA 6 HOH 427 1949 1949 HOH HOH A . 
DA 6 HOH 428 1950 1950 HOH HOH A . 
DA 6 HOH 429 1951 1951 HOH HOH A . 
DA 6 HOH 430 1952 1952 HOH HOH A . 
DA 6 HOH 431 1953 1953 HOH HOH A . 
DA 6 HOH 432 1954 1954 HOH HOH A . 
DA 6 HOH 433 1955 1955 HOH HOH A . 
DA 6 HOH 434 1956 1956 HOH HOH A . 
DA 6 HOH 435 1957 1957 HOH HOH A . 
DA 6 HOH 436 1958 1958 HOH HOH A . 
DA 6 HOH 437 1959 1959 HOH HOH A . 
DA 6 HOH 438 1960 1960 HOH HOH A . 
DA 6 HOH 439 1961 1961 HOH HOH A . 
DA 6 HOH 440 1962 1962 HOH HOH A . 
DA 6 HOH 441 1963 1963 HOH HOH A . 
DA 6 HOH 442 1964 1964 HOH HOH A . 
DA 6 HOH 443 1965 1965 HOH HOH A . 
DA 6 HOH 444 1966 1966 HOH HOH A . 
DA 6 HOH 445 1967 1967 HOH HOH A . 
DA 6 HOH 446 1968 1968 HOH HOH A . 
DA 6 HOH 447 1969 1969 HOH HOH A . 
DA 6 HOH 448 1970 1970 HOH HOH A . 
DA 6 HOH 449 1971 1971 HOH HOH A . 
DA 6 HOH 450 1972 1972 HOH HOH A . 
DA 6 HOH 451 1973 1973 HOH HOH A . 
DA 6 HOH 452 1974 1974 HOH HOH A . 
DA 6 HOH 453 1975 1975 HOH HOH A . 
DA 6 HOH 454 1976 1976 HOH HOH A . 
DA 6 HOH 455 1977 1977 HOH HOH A . 
DA 6 HOH 456 1978 1978 HOH HOH A . 
DA 6 HOH 457 1979 1979 HOH HOH A . 
DA 6 HOH 458 1980 1980 HOH HOH A . 
DA 6 HOH 459 1981 1981 HOH HOH A . 
DA 6 HOH 460 1982 1982 HOH HOH A . 
DA 6 HOH 461 1983 1983 HOH HOH A . 
DA 6 HOH 462 1984 1984 HOH HOH A . 
DA 6 HOH 463 1985 1985 HOH HOH A . 
DA 6 HOH 464 1986 1986 HOH HOH A . 
DA 6 HOH 465 1987 1987 HOH HOH A . 
DA 6 HOH 466 1988 1988 HOH HOH A . 
DA 6 HOH 467 1989 1989 HOH HOH A . 
DA 6 HOH 468 1990 1990 HOH HOH A . 
DA 6 HOH 469 1991 1991 HOH HOH A . 
DA 6 HOH 470 1992 1992 HOH HOH A . 
DA 6 HOH 471 1993 1993 HOH HOH A . 
DA 6 HOH 472 1994 1994 HOH HOH A . 
DA 6 HOH 473 1995 1995 HOH HOH A . 
DA 6 HOH 474 1996 1996 HOH HOH A . 
DA 6 HOH 475 1997 1997 HOH HOH A . 
DA 6 HOH 476 1998 1998 HOH HOH A . 
DA 6 HOH 477 1999 1999 HOH HOH A . 
DA 6 HOH 478 2000 2000 HOH HOH A . 
DA 6 HOH 479 2001 2001 HOH HOH A . 
DA 6 HOH 480 2002 2002 HOH HOH A . 
DA 6 HOH 481 2003 2003 HOH HOH A . 
DA 6 HOH 482 2004 2004 HOH HOH A . 
DA 6 HOH 483 2005 2005 HOH HOH A . 
DA 6 HOH 484 2006 2006 HOH HOH A . 
DA 6 HOH 485 2007 2007 HOH HOH A . 
DA 6 HOH 486 2008 2008 HOH HOH A . 
DA 6 HOH 487 2009 2009 HOH HOH A . 
DA 6 HOH 488 2010 2010 HOH HOH A . 
DA 6 HOH 489 2011 2011 HOH HOH A . 
DA 6 HOH 490 2012 2012 HOH HOH A . 
DA 6 HOH 491 2013 2013 HOH HOH A . 
DA 6 HOH 492 2014 2014 HOH HOH A . 
DA 6 HOH 493 2015 2015 HOH HOH A . 
DA 6 HOH 494 2016 2016 HOH HOH A . 
DA 6 HOH 495 2017 2017 HOH HOH A . 
DA 6 HOH 496 2018 2018 HOH HOH A . 
DA 6 HOH 497 2019 2019 HOH HOH A . 
DA 6 HOH 498 2020 2020 HOH HOH A . 
DA 6 HOH 499 2021 2021 HOH HOH A . 
DA 6 HOH 500 2022 2022 HOH HOH A . 
DA 6 HOH 501 2023 2023 HOH HOH A . 
DA 6 HOH 502 2024 2024 HOH HOH A . 
DA 6 HOH 503 2025 2025 HOH HOH A . 
DA 6 HOH 504 2026 2026 HOH HOH A . 
DA 6 HOH 505 2027 2027 HOH HOH A . 
DA 6 HOH 506 2028 2028 HOH HOH A . 
DA 6 HOH 507 2029 2029 HOH HOH A . 
DA 6 HOH 508 2030 2030 HOH HOH A . 
DA 6 HOH 509 2031 2031 HOH HOH A . 
DA 6 HOH 510 2032 2032 HOH HOH A . 
DA 6 HOH 511 2033 2033 HOH HOH A . 
DA 6 HOH 512 2034 2034 HOH HOH A . 
DA 6 HOH 513 2035 2035 HOH HOH A . 
DA 6 HOH 514 2036 2036 HOH HOH A . 
DA 6 HOH 515 2037 2037 HOH HOH A . 
DA 6 HOH 516 2038 2038 HOH HOH A . 
DA 6 HOH 517 2039 2039 HOH HOH A . 
DA 6 HOH 518 2040 2040 HOH HOH A . 
DA 6 HOH 519 2041 2041 HOH HOH A . 
DA 6 HOH 520 2042 2042 HOH HOH A . 
DA 6 HOH 521 2043 2043 HOH HOH A . 
DA 6 HOH 522 2044 2044 HOH HOH A . 
DA 6 HOH 523 2045 2045 HOH HOH A . 
DA 6 HOH 524 2046 2046 HOH HOH A . 
DA 6 HOH 525 2047 2047 HOH HOH A . 
DA 6 HOH 526 2048 2048 HOH HOH A . 
DA 6 HOH 527 2049 2049 HOH HOH A . 
DA 6 HOH 528 2050 2050 HOH HOH A . 
DA 6 HOH 529 2051 2051 HOH HOH A . 
DA 6 HOH 530 2052 2052 HOH HOH A . 
DA 6 HOH 531 2053 2053 HOH HOH A . 
DA 6 HOH 532 2054 2054 HOH HOH A . 
DA 6 HOH 533 2055 2055 HOH HOH A . 
DA 6 HOH 534 2056 2056 HOH HOH A . 
DA 6 HOH 535 2057 2057 HOH HOH A . 
DA 6 HOH 536 2058 2058 HOH HOH A . 
DA 6 HOH 537 2059 2059 HOH HOH A . 
DA 6 HOH 538 2060 2060 HOH HOH A . 
DA 6 HOH 539 2061 2061 HOH HOH A . 
DA 6 HOH 540 2062 2062 HOH HOH A . 
DA 6 HOH 541 2063 2063 HOH HOH A . 
DA 6 HOH 542 2064 2064 HOH HOH A . 
DA 6 HOH 543 2065 2065 HOH HOH A . 
DA 6 HOH 544 2066 2066 HOH HOH A . 
DA 6 HOH 545 2067 2067 HOH HOH A . 
DA 6 HOH 546 2068 2068 HOH HOH A . 
DA 6 HOH 547 2069 2069 HOH HOH A . 
DA 6 HOH 548 2070 2070 HOH HOH A . 
DA 6 HOH 549 2071 2071 HOH HOH A . 
DA 6 HOH 550 2072 2072 HOH HOH A . 
DA 6 HOH 551 2073 2073 HOH HOH A . 
DA 6 HOH 552 2074 2074 HOH HOH A . 
DA 6 HOH 553 2075 2075 HOH HOH A . 
DA 6 HOH 554 2076 2076 HOH HOH A . 
DA 6 HOH 555 2077 2077 HOH HOH A . 
DA 6 HOH 556 2078 2078 HOH HOH A . 
DA 6 HOH 557 2079 2079 HOH HOH A . 
DA 6 HOH 558 2080 2080 HOH HOH A . 
DA 6 HOH 559 2081 2081 HOH HOH A . 
DA 6 HOH 560 2082 2082 HOH HOH A . 
DA 6 HOH 561 2083 2083 HOH HOH A . 
DA 6 HOH 562 2084 2084 HOH HOH A . 
DA 6 HOH 563 2085 2085 HOH HOH A . 
DA 6 HOH 564 2086 2086 HOH HOH A . 
DA 6 HOH 565 2087 2087 HOH HOH A . 
DA 6 HOH 566 2088 2088 HOH HOH A . 
DA 6 HOH 567 2089 2089 HOH HOH A . 
DA 6 HOH 568 2090 2090 HOH HOH A . 
DA 6 HOH 569 2091 2091 HOH HOH A . 
DA 6 HOH 570 2092 2092 HOH HOH A . 
DA 6 HOH 571 2093 2093 HOH HOH A . 
DA 6 HOH 572 2094 2094 HOH HOH A . 
DA 6 HOH 573 2095 2095 HOH HOH A . 
DA 6 HOH 574 2096 2096 HOH HOH A . 
DA 6 HOH 575 2097 2097 HOH HOH A . 
DA 6 HOH 576 2098 2098 HOH HOH A . 
DA 6 HOH 577 2099 2099 HOH HOH A . 
DA 6 HOH 578 2100 2100 HOH HOH A . 
DA 6 HOH 579 2101 2101 HOH HOH A . 
DA 6 HOH 580 2102 2102 HOH HOH A . 
DA 6 HOH 581 2103 2103 HOH HOH A . 
DA 6 HOH 582 2104 2104 HOH HOH A . 
DA 6 HOH 583 2105 2105 HOH HOH A . 
DA 6 HOH 584 2106 2106 HOH HOH A . 
DA 6 HOH 585 2107 2107 HOH HOH A . 
DA 6 HOH 586 2108 2108 HOH HOH A . 
DA 6 HOH 587 2109 2109 HOH HOH A . 
DA 6 HOH 588 2110 2110 HOH HOH A . 
DA 6 HOH 589 2111 2111 HOH HOH A . 
DA 6 HOH 590 2112 2112 HOH HOH A . 
DA 6 HOH 591 2113 2113 HOH HOH A . 
DA 6 HOH 592 2114 2114 HOH HOH A . 
DA 6 HOH 593 2115 2115 HOH HOH A . 
DA 6 HOH 594 2116 2116 HOH HOH A . 
DA 6 HOH 595 2117 2117 HOH HOH A . 
DA 6 HOH 596 2118 2118 HOH HOH A . 
DA 6 HOH 597 2119 2119 HOH HOH A . 
DA 6 HOH 598 2120 2120 HOH HOH A . 
DA 6 HOH 599 2121 2121 HOH HOH A . 
DA 6 HOH 600 2122 2122 HOH HOH A . 
DA 6 HOH 601 2123 2123 HOH HOH A . 
DA 6 HOH 602 2124 2124 HOH HOH A . 
DA 6 HOH 603 2125 2125 HOH HOH A . 
DA 6 HOH 604 2126 2126 HOH HOH A . 
DA 6 HOH 605 2127 2127 HOH HOH A . 
DA 6 HOH 606 2128 2128 HOH HOH A . 
DA 6 HOH 607 2129 2129 HOH HOH A . 
DA 6 HOH 608 2130 2130 HOH HOH A . 
DA 6 HOH 609 2131 2131 HOH HOH A . 
DA 6 HOH 610 2132 2132 HOH HOH A . 
DA 6 HOH 611 2133 2133 HOH HOH A . 
DA 6 HOH 612 2134 2134 HOH HOH A . 
DA 6 HOH 613 2135 2135 HOH HOH A . 
DA 6 HOH 614 2136 2136 HOH HOH A . 
DA 6 HOH 615 2137 2137 HOH HOH A . 
DA 6 HOH 616 2138 2138 HOH HOH A . 
DA 6 HOH 617 2139 2139 HOH HOH A . 
DA 6 HOH 618 2140 2140 HOH HOH A . 
DA 6 HOH 619 2141 2141 HOH HOH A . 
DA 6 HOH 620 2142 2142 HOH HOH A . 
DA 6 HOH 621 2143 2143 HOH HOH A . 
DA 6 HOH 622 2144 2144 HOH HOH A . 
DA 6 HOH 623 2145 2145 HOH HOH A . 
DA 6 HOH 624 2146 2146 HOH HOH A . 
DA 6 HOH 625 2147 2147 HOH HOH A . 
DA 6 HOH 626 2148 2148 HOH HOH A . 
DA 6 HOH 627 2149 2149 HOH HOH A . 
DA 6 HOH 628 2150 2150 HOH HOH A . 
DA 6 HOH 629 2151 2151 HOH HOH A . 
DA 6 HOH 630 2152 2152 HOH HOH A . 
DA 6 HOH 631 2153 2153 HOH HOH A . 
DA 6 HOH 632 2154 2154 HOH HOH A . 
DA 6 HOH 633 2155 2155 HOH HOH A . 
DA 6 HOH 634 2156 2156 HOH HOH A . 
DA 6 HOH 635 2157 2157 HOH HOH A . 
DA 6 HOH 636 2158 2158 HOH HOH A . 
DA 6 HOH 637 2159 2159 HOH HOH A . 
DA 6 HOH 638 2461 2461 HOH HOH A . 
DA 6 HOH 639 2801 2801 HOH HOH A . 
DA 6 HOH 640 2863 2863 HOH HOH A . 
EA 6 HOH 1   2323 2323 HOH HOH B . 
EA 6 HOH 2   2324 2324 HOH HOH B . 
EA 6 HOH 3   2325 2325 HOH HOH B . 
EA 6 HOH 4   2326 2326 HOH HOH B . 
EA 6 HOH 5   2327 2327 HOH HOH B . 
EA 6 HOH 6   2328 2328 HOH HOH B . 
EA 6 HOH 7   2329 2329 HOH HOH B . 
EA 6 HOH 8   2330 2330 HOH HOH B . 
EA 6 HOH 9   2331 2331 HOH HOH B . 
EA 6 HOH 10  2332 2332 HOH HOH B . 
EA 6 HOH 11  2333 2333 HOH HOH B . 
EA 6 HOH 12  2334 2334 HOH HOH B . 
EA 6 HOH 13  2335 2335 HOH HOH B . 
EA 6 HOH 14  2336 2336 HOH HOH B . 
EA 6 HOH 15  2337 2337 HOH HOH B . 
EA 6 HOH 16  2338 2338 HOH HOH B . 
EA 6 HOH 17  2339 2339 HOH HOH B . 
EA 6 HOH 18  2340 2340 HOH HOH B . 
EA 6 HOH 19  2341 2341 HOH HOH B . 
EA 6 HOH 20  2342 2342 HOH HOH B . 
EA 6 HOH 21  2343 2343 HOH HOH B . 
EA 6 HOH 22  2344 2344 HOH HOH B . 
EA 6 HOH 23  2345 2345 HOH HOH B . 
EA 6 HOH 24  2346 2346 HOH HOH B . 
EA 6 HOH 25  2347 2347 HOH HOH B . 
EA 6 HOH 26  2348 2348 HOH HOH B . 
EA 6 HOH 27  2349 2349 HOH HOH B . 
EA 6 HOH 28  2350 2350 HOH HOH B . 
EA 6 HOH 29  2351 2351 HOH HOH B . 
EA 6 HOH 30  2352 2352 HOH HOH B . 
EA 6 HOH 31  2353 2353 HOH HOH B . 
EA 6 HOH 32  2354 2354 HOH HOH B . 
EA 6 HOH 33  2355 2355 HOH HOH B . 
EA 6 HOH 34  2356 2356 HOH HOH B . 
EA 6 HOH 35  2357 2357 HOH HOH B . 
EA 6 HOH 36  2358 2358 HOH HOH B . 
EA 6 HOH 37  2359 2359 HOH HOH B . 
EA 6 HOH 38  2360 2360 HOH HOH B . 
EA 6 HOH 39  2361 2361 HOH HOH B . 
EA 6 HOH 40  2362 2362 HOH HOH B . 
EA 6 HOH 41  2363 2363 HOH HOH B . 
EA 6 HOH 42  2364 2364 HOH HOH B . 
EA 6 HOH 43  2365 2365 HOH HOH B . 
EA 6 HOH 44  2366 2366 HOH HOH B . 
EA 6 HOH 45  2367 2367 HOH HOH B . 
EA 6 HOH 46  2368 2368 HOH HOH B . 
EA 6 HOH 47  2369 2369 HOH HOH B . 
EA 6 HOH 48  2370 2370 HOH HOH B . 
EA 6 HOH 49  2371 2371 HOH HOH B . 
EA 6 HOH 50  2372 2372 HOH HOH B . 
EA 6 HOH 51  2373 2373 HOH HOH B . 
EA 6 HOH 52  2374 2374 HOH HOH B . 
EA 6 HOH 53  2375 2375 HOH HOH B . 
EA 6 HOH 54  2376 2376 HOH HOH B . 
EA 6 HOH 55  2377 2377 HOH HOH B . 
EA 6 HOH 56  2378 2378 HOH HOH B . 
EA 6 HOH 57  2379 2379 HOH HOH B . 
EA 6 HOH 58  2380 2380 HOH HOH B . 
EA 6 HOH 59  2381 2381 HOH HOH B . 
EA 6 HOH 60  2382 2382 HOH HOH B . 
EA 6 HOH 61  2383 2383 HOH HOH B . 
EA 6 HOH 62  2384 2384 HOH HOH B . 
EA 6 HOH 63  2385 2385 HOH HOH B . 
EA 6 HOH 64  2386 2386 HOH HOH B . 
EA 6 HOH 65  2387 2387 HOH HOH B . 
EA 6 HOH 66  2388 2388 HOH HOH B . 
EA 6 HOH 67  2389 2389 HOH HOH B . 
EA 6 HOH 68  2390 2390 HOH HOH B . 
EA 6 HOH 69  2391 2391 HOH HOH B . 
EA 6 HOH 70  2392 2392 HOH HOH B . 
EA 6 HOH 71  2393 2393 HOH HOH B . 
EA 6 HOH 72  2394 2394 HOH HOH B . 
EA 6 HOH 73  2395 2395 HOH HOH B . 
EA 6 HOH 74  2396 2396 HOH HOH B . 
EA 6 HOH 75  2397 2397 HOH HOH B . 
EA 6 HOH 76  2398 2398 HOH HOH B . 
EA 6 HOH 77  2399 2399 HOH HOH B . 
EA 6 HOH 78  2400 2400 HOH HOH B . 
EA 6 HOH 79  2401 2401 HOH HOH B . 
EA 6 HOH 80  2402 2402 HOH HOH B . 
EA 6 HOH 81  2403 2403 HOH HOH B . 
EA 6 HOH 82  2404 2404 HOH HOH B . 
EA 6 HOH 83  2405 2405 HOH HOH B . 
EA 6 HOH 84  2406 2406 HOH HOH B . 
EA 6 HOH 85  2407 2407 HOH HOH B . 
EA 6 HOH 86  2408 2408 HOH HOH B . 
EA 6 HOH 87  2409 2409 HOH HOH B . 
EA 6 HOH 88  2410 2410 HOH HOH B . 
EA 6 HOH 89  2411 2411 HOH HOH B . 
EA 6 HOH 90  2412 2412 HOH HOH B . 
EA 6 HOH 91  2413 2413 HOH HOH B . 
EA 6 HOH 92  2414 2414 HOH HOH B . 
EA 6 HOH 93  2415 2415 HOH HOH B . 
EA 6 HOH 94  2416 2416 HOH HOH B . 
EA 6 HOH 95  2417 2417 HOH HOH B . 
EA 6 HOH 96  2418 2418 HOH HOH B . 
EA 6 HOH 97  2419 2419 HOH HOH B . 
EA 6 HOH 98  2420 2420 HOH HOH B . 
EA 6 HOH 99  2421 2421 HOH HOH B . 
EA 6 HOH 100 2422 2422 HOH HOH B . 
EA 6 HOH 101 2423 2423 HOH HOH B . 
EA 6 HOH 102 2424 2424 HOH HOH B . 
EA 6 HOH 103 2425 2425 HOH HOH B . 
EA 6 HOH 104 2426 2426 HOH HOH B . 
EA 6 HOH 105 2427 2427 HOH HOH B . 
EA 6 HOH 106 2428 2428 HOH HOH B . 
EA 6 HOH 107 2429 2429 HOH HOH B . 
EA 6 HOH 108 2430 2430 HOH HOH B . 
EA 6 HOH 109 2431 2431 HOH HOH B . 
EA 6 HOH 110 2432 2432 HOH HOH B . 
EA 6 HOH 111 2433 2433 HOH HOH B . 
EA 6 HOH 112 2434 2434 HOH HOH B . 
EA 6 HOH 113 2435 2435 HOH HOH B . 
EA 6 HOH 114 2436 2436 HOH HOH B . 
EA 6 HOH 115 2437 2437 HOH HOH B . 
EA 6 HOH 116 2438 2438 HOH HOH B . 
EA 6 HOH 117 2439 2439 HOH HOH B . 
EA 6 HOH 118 2440 2440 HOH HOH B . 
EA 6 HOH 119 2441 2441 HOH HOH B . 
EA 6 HOH 120 2442 2442 HOH HOH B . 
EA 6 HOH 121 2443 2443 HOH HOH B . 
EA 6 HOH 122 2444 2444 HOH HOH B . 
EA 6 HOH 123 2445 2445 HOH HOH B . 
EA 6 HOH 124 2446 2446 HOH HOH B . 
EA 6 HOH 125 2447 2447 HOH HOH B . 
EA 6 HOH 126 2448 2448 HOH HOH B . 
EA 6 HOH 127 2449 2449 HOH HOH B . 
EA 6 HOH 128 2450 2450 HOH HOH B . 
EA 6 HOH 129 2451 2451 HOH HOH B . 
EA 6 HOH 130 2452 2452 HOH HOH B . 
EA 6 HOH 131 2453 2453 HOH HOH B . 
EA 6 HOH 132 2454 2454 HOH HOH B . 
EA 6 HOH 133 2455 2455 HOH HOH B . 
EA 6 HOH 134 2456 2456 HOH HOH B . 
EA 6 HOH 135 2457 2457 HOH HOH B . 
EA 6 HOH 136 2458 2458 HOH HOH B . 
EA 6 HOH 137 2459 2459 HOH HOH B . 
EA 6 HOH 138 2460 2460 HOH HOH B . 
EA 6 HOH 139 2462 2462 HOH HOH B . 
EA 6 HOH 140 2463 2463 HOH HOH B . 
EA 6 HOH 141 2464 2464 HOH HOH B . 
EA 6 HOH 142 2465 2465 HOH HOH B . 
EA 6 HOH 143 2466 2466 HOH HOH B . 
EA 6 HOH 144 2467 2467 HOH HOH B . 
EA 6 HOH 145 2468 2468 HOH HOH B . 
EA 6 HOH 146 2469 2469 HOH HOH B . 
EA 6 HOH 147 2470 2470 HOH HOH B . 
EA 6 HOH 148 2471 2471 HOH HOH B . 
EA 6 HOH 149 2472 2472 HOH HOH B . 
EA 6 HOH 150 2473 2473 HOH HOH B . 
EA 6 HOH 151 2474 2474 HOH HOH B . 
EA 6 HOH 152 2475 2475 HOH HOH B . 
EA 6 HOH 153 2476 2476 HOH HOH B . 
EA 6 HOH 154 2477 2477 HOH HOH B . 
EA 6 HOH 155 2478 2478 HOH HOH B . 
EA 6 HOH 156 2479 2479 HOH HOH B . 
EA 6 HOH 157 2480 2480 HOH HOH B . 
EA 6 HOH 158 2481 2481 HOH HOH B . 
EA 6 HOH 159 2482 2482 HOH HOH B . 
EA 6 HOH 160 2483 2483 HOH HOH B . 
EA 6 HOH 161 2484 2484 HOH HOH B . 
EA 6 HOH 162 2485 2485 HOH HOH B . 
EA 6 HOH 163 2486 2486 HOH HOH B . 
EA 6 HOH 164 2487 2487 HOH HOH B . 
EA 6 HOH 165 2488 2488 HOH HOH B . 
EA 6 HOH 166 2489 2489 HOH HOH B . 
EA 6 HOH 167 2490 2490 HOH HOH B . 
EA 6 HOH 168 2491 2491 HOH HOH B . 
EA 6 HOH 169 2492 2492 HOH HOH B . 
EA 6 HOH 170 2493 2493 HOH HOH B . 
EA 6 HOH 171 2494 2494 HOH HOH B . 
EA 6 HOH 172 2495 2495 HOH HOH B . 
EA 6 HOH 173 2496 2496 HOH HOH B . 
EA 6 HOH 174 2497 2497 HOH HOH B . 
EA 6 HOH 175 2498 2498 HOH HOH B . 
EA 6 HOH 176 2499 2499 HOH HOH B . 
EA 6 HOH 177 2500 2500 HOH HOH B . 
EA 6 HOH 178 2501 2501 HOH HOH B . 
EA 6 HOH 179 2502 2502 HOH HOH B . 
EA 6 HOH 180 2503 2503 HOH HOH B . 
EA 6 HOH 181 2504 2504 HOH HOH B . 
EA 6 HOH 182 2505 2505 HOH HOH B . 
EA 6 HOH 183 2506 2506 HOH HOH B . 
EA 6 HOH 184 2507 2507 HOH HOH B . 
EA 6 HOH 185 2508 2508 HOH HOH B . 
EA 6 HOH 186 2509 2509 HOH HOH B . 
EA 6 HOH 187 2510 2510 HOH HOH B . 
EA 6 HOH 188 2511 2511 HOH HOH B . 
EA 6 HOH 189 2512 2512 HOH HOH B . 
EA 6 HOH 190 2513 2513 HOH HOH B . 
EA 6 HOH 191 2514 2514 HOH HOH B . 
EA 6 HOH 192 2515 2515 HOH HOH B . 
EA 6 HOH 193 2516 2516 HOH HOH B . 
EA 6 HOH 194 2517 2517 HOH HOH B . 
EA 6 HOH 195 2518 2518 HOH HOH B . 
EA 6 HOH 196 2519 2519 HOH HOH B . 
EA 6 HOH 197 2520 2520 HOH HOH B . 
EA 6 HOH 198 2521 2521 HOH HOH B . 
EA 6 HOH 199 2522 2522 HOH HOH B . 
EA 6 HOH 200 2523 2523 HOH HOH B . 
EA 6 HOH 201 2524 2524 HOH HOH B . 
EA 6 HOH 202 2525 2525 HOH HOH B . 
EA 6 HOH 203 2526 2526 HOH HOH B . 
EA 6 HOH 204 2527 2527 HOH HOH B . 
EA 6 HOH 205 2528 2528 HOH HOH B . 
EA 6 HOH 206 2529 2529 HOH HOH B . 
EA 6 HOH 207 2530 2530 HOH HOH B . 
EA 6 HOH 208 2531 2531 HOH HOH B . 
EA 6 HOH 209 2532 2532 HOH HOH B . 
EA 6 HOH 210 2533 2533 HOH HOH B . 
EA 6 HOH 211 2534 2534 HOH HOH B . 
EA 6 HOH 212 2535 2535 HOH HOH B . 
EA 6 HOH 213 2536 2536 HOH HOH B . 
EA 6 HOH 214 2537 2537 HOH HOH B . 
EA 6 HOH 215 2538 2538 HOH HOH B . 
EA 6 HOH 216 2539 2539 HOH HOH B . 
EA 6 HOH 217 2540 2540 HOH HOH B . 
EA 6 HOH 218 2541 2541 HOH HOH B . 
EA 6 HOH 219 2542 2542 HOH HOH B . 
EA 6 HOH 220 2543 2543 HOH HOH B . 
EA 6 HOH 221 2544 2544 HOH HOH B . 
EA 6 HOH 222 2545 2545 HOH HOH B . 
EA 6 HOH 223 2546 2546 HOH HOH B . 
EA 6 HOH 224 2547 2547 HOH HOH B . 
EA 6 HOH 225 2548 2548 HOH HOH B . 
EA 6 HOH 226 2549 2549 HOH HOH B . 
EA 6 HOH 227 2550 2550 HOH HOH B . 
EA 6 HOH 228 2551 2551 HOH HOH B . 
EA 6 HOH 229 2552 2552 HOH HOH B . 
EA 6 HOH 230 2553 2553 HOH HOH B . 
EA 6 HOH 231 2554 2554 HOH HOH B . 
EA 6 HOH 232 2555 2555 HOH HOH B . 
EA 6 HOH 233 2556 2556 HOH HOH B . 
EA 6 HOH 234 2557 2557 HOH HOH B . 
EA 6 HOH 235 2558 2558 HOH HOH B . 
EA 6 HOH 236 2559 2559 HOH HOH B . 
EA 6 HOH 237 2560 2560 HOH HOH B . 
EA 6 HOH 238 2561 2561 HOH HOH B . 
EA 6 HOH 239 2562 2562 HOH HOH B . 
EA 6 HOH 240 2563 2563 HOH HOH B . 
EA 6 HOH 241 2564 2564 HOH HOH B . 
EA 6 HOH 242 2565 2565 HOH HOH B . 
EA 6 HOH 243 2566 2566 HOH HOH B . 
EA 6 HOH 244 2567 2567 HOH HOH B . 
EA 6 HOH 245 2568 2568 HOH HOH B . 
EA 6 HOH 246 2569 2569 HOH HOH B . 
EA 6 HOH 247 2570 2570 HOH HOH B . 
EA 6 HOH 248 2571 2571 HOH HOH B . 
EA 6 HOH 249 2572 2572 HOH HOH B . 
EA 6 HOH 250 2573 2573 HOH HOH B . 
EA 6 HOH 251 2574 2574 HOH HOH B . 
EA 6 HOH 252 2575 2575 HOH HOH B . 
EA 6 HOH 253 2576 2576 HOH HOH B . 
EA 6 HOH 254 2577 2577 HOH HOH B . 
EA 6 HOH 255 2578 2578 HOH HOH B . 
EA 6 HOH 256 2579 2579 HOH HOH B . 
EA 6 HOH 257 2580 2580 HOH HOH B . 
EA 6 HOH 258 2581 2581 HOH HOH B . 
EA 6 HOH 259 2582 2582 HOH HOH B . 
EA 6 HOH 260 2583 2583 HOH HOH B . 
EA 6 HOH 261 2584 2584 HOH HOH B . 
EA 6 HOH 262 2585 2585 HOH HOH B . 
EA 6 HOH 263 2586 2586 HOH HOH B . 
EA 6 HOH 264 2587 2587 HOH HOH B . 
EA 6 HOH 265 2588 2588 HOH HOH B . 
EA 6 HOH 266 2589 2589 HOH HOH B . 
EA 6 HOH 267 2590 2590 HOH HOH B . 
EA 6 HOH 268 2591 2591 HOH HOH B . 
EA 6 HOH 269 2592 2592 HOH HOH B . 
EA 6 HOH 270 2593 2593 HOH HOH B . 
EA 6 HOH 271 2594 2594 HOH HOH B . 
EA 6 HOH 272 2595 2595 HOH HOH B . 
EA 6 HOH 273 2596 2596 HOH HOH B . 
EA 6 HOH 274 2597 2597 HOH HOH B . 
EA 6 HOH 275 2598 2598 HOH HOH B . 
EA 6 HOH 276 2599 2599 HOH HOH B . 
EA 6 HOH 277 2600 2600 HOH HOH B . 
EA 6 HOH 278 2601 2601 HOH HOH B . 
EA 6 HOH 279 2602 2602 HOH HOH B . 
EA 6 HOH 280 2603 2603 HOH HOH B . 
EA 6 HOH 281 2604 2604 HOH HOH B . 
EA 6 HOH 282 2605 2605 HOH HOH B . 
EA 6 HOH 283 2606 2606 HOH HOH B . 
EA 6 HOH 284 2607 2607 HOH HOH B . 
EA 6 HOH 285 2608 2608 HOH HOH B . 
EA 6 HOH 286 2609 2609 HOH HOH B . 
EA 6 HOH 287 2610 2610 HOH HOH B . 
EA 6 HOH 288 2611 2611 HOH HOH B . 
EA 6 HOH 289 2612 2612 HOH HOH B . 
EA 6 HOH 290 2613 2613 HOH HOH B . 
EA 6 HOH 291 2614 2614 HOH HOH B . 
EA 6 HOH 292 2615 2615 HOH HOH B . 
EA 6 HOH 293 2616 2616 HOH HOH B . 
EA 6 HOH 294 2617 2617 HOH HOH B . 
EA 6 HOH 295 2618 2618 HOH HOH B . 
EA 6 HOH 296 2619 2619 HOH HOH B . 
EA 6 HOH 297 2620 2620 HOH HOH B . 
EA 6 HOH 298 2621 2621 HOH HOH B . 
EA 6 HOH 299 2622 2622 HOH HOH B . 
EA 6 HOH 300 2623 2623 HOH HOH B . 
EA 6 HOH 301 2624 2624 HOH HOH B . 
EA 6 HOH 302 2625 2625 HOH HOH B . 
EA 6 HOH 303 2626 2626 HOH HOH B . 
EA 6 HOH 304 2627 2627 HOH HOH B . 
EA 6 HOH 305 2628 2628 HOH HOH B . 
EA 6 HOH 306 2629 2629 HOH HOH B . 
EA 6 HOH 307 2630 2630 HOH HOH B . 
EA 6 HOH 308 2631 2631 HOH HOH B . 
EA 6 HOH 309 2632 2632 HOH HOH B . 
EA 6 HOH 310 2633 2633 HOH HOH B . 
EA 6 HOH 311 2634 2634 HOH HOH B . 
EA 6 HOH 312 2635 2635 HOH HOH B . 
EA 6 HOH 313 2636 2636 HOH HOH B . 
EA 6 HOH 314 2637 2637 HOH HOH B . 
EA 6 HOH 315 2638 2638 HOH HOH B . 
EA 6 HOH 316 2639 2639 HOH HOH B . 
EA 6 HOH 317 2640 2640 HOH HOH B . 
EA 6 HOH 318 2641 2641 HOH HOH B . 
EA 6 HOH 319 2642 2642 HOH HOH B . 
EA 6 HOH 320 2643 2643 HOH HOH B . 
EA 6 HOH 321 2644 2644 HOH HOH B . 
EA 6 HOH 322 2645 2645 HOH HOH B . 
EA 6 HOH 323 2646 2646 HOH HOH B . 
EA 6 HOH 324 2647 2647 HOH HOH B . 
EA 6 HOH 325 2648 2648 HOH HOH B . 
EA 6 HOH 326 2649 2649 HOH HOH B . 
EA 6 HOH 327 2650 2650 HOH HOH B . 
EA 6 HOH 328 2651 2651 HOH HOH B . 
EA 6 HOH 329 2652 2652 HOH HOH B . 
EA 6 HOH 330 2653 2653 HOH HOH B . 
EA 6 HOH 331 2654 2654 HOH HOH B . 
EA 6 HOH 332 2655 2655 HOH HOH B . 
EA 6 HOH 333 2656 2656 HOH HOH B . 
EA 6 HOH 334 2657 2657 HOH HOH B . 
EA 6 HOH 335 2658 2658 HOH HOH B . 
EA 6 HOH 336 2659 2659 HOH HOH B . 
EA 6 HOH 337 2660 2660 HOH HOH B . 
EA 6 HOH 338 2661 2661 HOH HOH B . 
EA 6 HOH 339 2662 2662 HOH HOH B . 
EA 6 HOH 340 2663 2663 HOH HOH B . 
EA 6 HOH 341 2664 2664 HOH HOH B . 
EA 6 HOH 342 2665 2665 HOH HOH B . 
EA 6 HOH 343 2666 2666 HOH HOH B . 
EA 6 HOH 344 2667 2667 HOH HOH B . 
EA 6 HOH 345 2668 2668 HOH HOH B . 
EA 6 HOH 346 2669 2669 HOH HOH B . 
EA 6 HOH 347 2670 2670 HOH HOH B . 
EA 6 HOH 348 2671 2671 HOH HOH B . 
EA 6 HOH 349 2672 2672 HOH HOH B . 
EA 6 HOH 350 2673 2673 HOH HOH B . 
EA 6 HOH 351 2674 2674 HOH HOH B . 
EA 6 HOH 352 2675 2675 HOH HOH B . 
EA 6 HOH 353 2676 2676 HOH HOH B . 
EA 6 HOH 354 2677 2677 HOH HOH B . 
EA 6 HOH 355 2678 2678 HOH HOH B . 
EA 6 HOH 356 2679 2679 HOH HOH B . 
EA 6 HOH 357 2680 2680 HOH HOH B . 
EA 6 HOH 358 2681 2681 HOH HOH B . 
EA 6 HOH 359 2682 2682 HOH HOH B . 
EA 6 HOH 360 2683 2683 HOH HOH B . 
EA 6 HOH 361 2684 2684 HOH HOH B . 
EA 6 HOH 362 2685 2685 HOH HOH B . 
EA 6 HOH 363 2686 2686 HOH HOH B . 
EA 6 HOH 364 2687 2687 HOH HOH B . 
EA 6 HOH 365 2688 2688 HOH HOH B . 
EA 6 HOH 366 2689 2689 HOH HOH B . 
EA 6 HOH 367 2690 2690 HOH HOH B . 
EA 6 HOH 368 2691 2691 HOH HOH B . 
EA 6 HOH 369 2692 2692 HOH HOH B . 
EA 6 HOH 370 2693 2693 HOH HOH B . 
EA 6 HOH 371 2694 2694 HOH HOH B . 
EA 6 HOH 372 2695 2695 HOH HOH B . 
EA 6 HOH 373 2696 2696 HOH HOH B . 
EA 6 HOH 374 2697 2697 HOH HOH B . 
EA 6 HOH 375 2698 2698 HOH HOH B . 
EA 6 HOH 376 2699 2699 HOH HOH B . 
EA 6 HOH 377 2700 2700 HOH HOH B . 
EA 6 HOH 378 2701 2701 HOH HOH B . 
EA 6 HOH 379 2702 2702 HOH HOH B . 
EA 6 HOH 380 2703 2703 HOH HOH B . 
EA 6 HOH 381 2704 2704 HOH HOH B . 
EA 6 HOH 382 2705 2705 HOH HOH B . 
EA 6 HOH 383 2706 2706 HOH HOH B . 
EA 6 HOH 384 2707 2707 HOH HOH B . 
EA 6 HOH 385 2708 2708 HOH HOH B . 
EA 6 HOH 386 2709 2709 HOH HOH B . 
EA 6 HOH 387 2710 2710 HOH HOH B . 
EA 6 HOH 388 2711 2711 HOH HOH B . 
EA 6 HOH 389 2712 2712 HOH HOH B . 
EA 6 HOH 390 2713 2713 HOH HOH B . 
EA 6 HOH 391 2714 2714 HOH HOH B . 
EA 6 HOH 392 2715 2715 HOH HOH B . 
EA 6 HOH 393 2716 2716 HOH HOH B . 
EA 6 HOH 394 2717 2717 HOH HOH B . 
EA 6 HOH 395 2718 2718 HOH HOH B . 
EA 6 HOH 396 2719 2719 HOH HOH B . 
EA 6 HOH 397 2720 2720 HOH HOH B . 
EA 6 HOH 398 2721 2721 HOH HOH B . 
EA 6 HOH 399 2722 2722 HOH HOH B . 
EA 6 HOH 400 2723 2723 HOH HOH B . 
EA 6 HOH 401 2724 2724 HOH HOH B . 
EA 6 HOH 402 2725 2725 HOH HOH B . 
EA 6 HOH 403 2726 2726 HOH HOH B . 
EA 6 HOH 404 2727 2727 HOH HOH B . 
EA 6 HOH 405 2728 2728 HOH HOH B . 
EA 6 HOH 406 2729 2729 HOH HOH B . 
EA 6 HOH 407 2730 2730 HOH HOH B . 
EA 6 HOH 408 2731 2731 HOH HOH B . 
EA 6 HOH 409 2732 2732 HOH HOH B . 
EA 6 HOH 410 2733 2733 HOH HOH B . 
EA 6 HOH 411 2734 2734 HOH HOH B . 
EA 6 HOH 412 2735 2735 HOH HOH B . 
EA 6 HOH 413 2736 2736 HOH HOH B . 
EA 6 HOH 414 2737 2737 HOH HOH B . 
EA 6 HOH 415 2738 2738 HOH HOH B . 
EA 6 HOH 416 2739 2739 HOH HOH B . 
EA 6 HOH 417 2740 2740 HOH HOH B . 
EA 6 HOH 418 2741 2741 HOH HOH B . 
EA 6 HOH 419 2742 2742 HOH HOH B . 
EA 6 HOH 420 2743 2743 HOH HOH B . 
EA 6 HOH 421 2744 2744 HOH HOH B . 
EA 6 HOH 422 2745 2745 HOH HOH B . 
EA 6 HOH 423 2746 2746 HOH HOH B . 
EA 6 HOH 424 2747 2747 HOH HOH B . 
EA 6 HOH 425 2748 2748 HOH HOH B . 
EA 6 HOH 426 2749 2749 HOH HOH B . 
EA 6 HOH 427 2750 2750 HOH HOH B . 
EA 6 HOH 428 2751 2751 HOH HOH B . 
EA 6 HOH 429 2752 2752 HOH HOH B . 
EA 6 HOH 430 2753 2753 HOH HOH B . 
EA 6 HOH 431 2754 2754 HOH HOH B . 
EA 6 HOH 432 2755 2755 HOH HOH B . 
EA 6 HOH 433 2756 2756 HOH HOH B . 
EA 6 HOH 434 2757 2757 HOH HOH B . 
EA 6 HOH 435 2758 2758 HOH HOH B . 
EA 6 HOH 436 2759 2759 HOH HOH B . 
EA 6 HOH 437 2760 2760 HOH HOH B . 
EA 6 HOH 438 2761 2761 HOH HOH B . 
EA 6 HOH 439 2762 2762 HOH HOH B . 
EA 6 HOH 440 2763 2763 HOH HOH B . 
EA 6 HOH 441 2764 2764 HOH HOH B . 
EA 6 HOH 442 2765 2765 HOH HOH B . 
EA 6 HOH 443 2766 2766 HOH HOH B . 
EA 6 HOH 444 2767 2767 HOH HOH B . 
EA 6 HOH 445 2768 2768 HOH HOH B . 
EA 6 HOH 446 2769 2769 HOH HOH B . 
EA 6 HOH 447 2770 2770 HOH HOH B . 
EA 6 HOH 448 2771 2771 HOH HOH B . 
EA 6 HOH 449 2772 2772 HOH HOH B . 
EA 6 HOH 450 2773 2773 HOH HOH B . 
EA 6 HOH 451 2774 2774 HOH HOH B . 
EA 6 HOH 452 2775 2775 HOH HOH B . 
EA 6 HOH 453 2776 2776 HOH HOH B . 
EA 6 HOH 454 2777 2777 HOH HOH B . 
EA 6 HOH 455 2778 2778 HOH HOH B . 
EA 6 HOH 456 2779 2779 HOH HOH B . 
EA 6 HOH 457 2780 2780 HOH HOH B . 
EA 6 HOH 458 2781 2781 HOH HOH B . 
EA 6 HOH 459 2782 2782 HOH HOH B . 
EA 6 HOH 460 2783 2783 HOH HOH B . 
EA 6 HOH 461 2784 2784 HOH HOH B . 
EA 6 HOH 462 2785 2785 HOH HOH B . 
EA 6 HOH 463 2786 2786 HOH HOH B . 
EA 6 HOH 464 2787 2787 HOH HOH B . 
EA 6 HOH 465 2788 2788 HOH HOH B . 
EA 6 HOH 466 2789 2789 HOH HOH B . 
EA 6 HOH 467 2790 2790 HOH HOH B . 
EA 6 HOH 468 2791 2791 HOH HOH B . 
EA 6 HOH 469 2792 2792 HOH HOH B . 
EA 6 HOH 470 2793 2793 HOH HOH B . 
EA 6 HOH 471 2794 2794 HOH HOH B . 
EA 6 HOH 472 2795 2795 HOH HOH B . 
EA 6 HOH 473 2796 2796 HOH HOH B . 
EA 6 HOH 474 2797 2797 HOH HOH B . 
EA 6 HOH 475 2798 2798 HOH HOH B . 
EA 6 HOH 476 2799 2799 HOH HOH B . 
EA 6 HOH 477 2800 2800 HOH HOH B . 
EA 6 HOH 478 2802 2802 HOH HOH B . 
EA 6 HOH 479 2803 2803 HOH HOH B . 
EA 6 HOH 480 2804 2804 HOH HOH B . 
EA 6 HOH 481 2805 2805 HOH HOH B . 
EA 6 HOH 482 2806 2806 HOH HOH B . 
EA 6 HOH 483 2807 2807 HOH HOH B . 
EA 6 HOH 484 2808 2808 HOH HOH B . 
EA 6 HOH 485 2809 2809 HOH HOH B . 
EA 6 HOH 486 2810 2810 HOH HOH B . 
EA 6 HOH 487 2811 2811 HOH HOH B . 
EA 6 HOH 488 2812 2812 HOH HOH B . 
EA 6 HOH 489 2813 2813 HOH HOH B . 
EA 6 HOH 490 2814 2814 HOH HOH B . 
EA 6 HOH 491 2815 2815 HOH HOH B . 
EA 6 HOH 492 2816 2816 HOH HOH B . 
EA 6 HOH 493 2817 2817 HOH HOH B . 
EA 6 HOH 494 2818 2818 HOH HOH B . 
EA 6 HOH 495 2819 2819 HOH HOH B . 
EA 6 HOH 496 2820 2820 HOH HOH B . 
EA 6 HOH 497 2821 2821 HOH HOH B . 
EA 6 HOH 498 2822 2822 HOH HOH B . 
EA 6 HOH 499 2823 2823 HOH HOH B . 
EA 6 HOH 500 2824 2824 HOH HOH B . 
EA 6 HOH 501 2825 2825 HOH HOH B . 
EA 6 HOH 502 2826 2826 HOH HOH B . 
EA 6 HOH 503 2827 2827 HOH HOH B . 
EA 6 HOH 504 2828 2828 HOH HOH B . 
EA 6 HOH 505 2829 2829 HOH HOH B . 
EA 6 HOH 506 2830 2830 HOH HOH B . 
EA 6 HOH 507 2831 2831 HOH HOH B . 
EA 6 HOH 508 2832 2832 HOH HOH B . 
EA 6 HOH 509 2833 2833 HOH HOH B . 
EA 6 HOH 510 2834 2834 HOH HOH B . 
EA 6 HOH 511 2835 2835 HOH HOH B . 
EA 6 HOH 512 2836 2836 HOH HOH B . 
EA 6 HOH 513 2837 2837 HOH HOH B . 
EA 6 HOH 514 2838 2838 HOH HOH B . 
EA 6 HOH 515 2839 2839 HOH HOH B . 
EA 6 HOH 516 2840 2840 HOH HOH B . 
EA 6 HOH 517 2841 2841 HOH HOH B . 
EA 6 HOH 518 2842 2842 HOH HOH B . 
EA 6 HOH 519 2843 2843 HOH HOH B . 
EA 6 HOH 520 2844 2844 HOH HOH B . 
EA 6 HOH 521 2845 2845 HOH HOH B . 
EA 6 HOH 522 2846 2846 HOH HOH B . 
EA 6 HOH 523 2847 2847 HOH HOH B . 
EA 6 HOH 524 2848 2848 HOH HOH B . 
EA 6 HOH 525 2849 2849 HOH HOH B . 
EA 6 HOH 526 2850 2850 HOH HOH B . 
EA 6 HOH 527 2851 2851 HOH HOH B . 
EA 6 HOH 528 2852 2852 HOH HOH B . 
EA 6 HOH 529 2853 2853 HOH HOH B . 
EA 6 HOH 530 2854 2854 HOH HOH B . 
EA 6 HOH 531 2855 2855 HOH HOH B . 
EA 6 HOH 532 2856 2856 HOH HOH B . 
EA 6 HOH 533 2857 2857 HOH HOH B . 
EA 6 HOH 534 2858 2858 HOH HOH B . 
EA 6 HOH 535 2859 2859 HOH HOH B . 
EA 6 HOH 536 2860 2860 HOH HOH B . 
EA 6 HOH 537 2861 2861 HOH HOH B . 
EA 6 HOH 538 2862 2862 HOH HOH B . 
EA 6 HOH 539 2864 2864 HOH HOH B . 
EA 6 HOH 540 2865 2865 HOH HOH B . 
EA 6 HOH 541 2866 2866 HOH HOH B . 
EA 6 HOH 542 2867 2867 HOH HOH B . 
EA 6 HOH 543 2868 2868 HOH HOH B . 
EA 6 HOH 544 2869 2869 HOH HOH B . 
EA 6 HOH 545 2870 2870 HOH HOH B . 
EA 6 HOH 546 2871 2871 HOH HOH B . 
EA 6 HOH 547 2872 2872 HOH HOH B . 
EA 6 HOH 548 2873 2873 HOH HOH B . 
EA 6 HOH 549 2874 2874 HOH HOH B . 
EA 6 HOH 550 2875 2875 HOH HOH B . 
EA 6 HOH 551 2876 2876 HOH HOH B . 
EA 6 HOH 552 2877 2877 HOH HOH B . 
EA 6 HOH 553 2878 2878 HOH HOH B . 
EA 6 HOH 554 2879 2879 HOH HOH B . 
EA 6 HOH 555 2880 2880 HOH HOH B . 
EA 6 HOH 556 2881 2881 HOH HOH B . 
EA 6 HOH 557 2882 2882 HOH HOH B . 
EA 6 HOH 558 2883 2883 HOH HOH B . 
EA 6 HOH 559 2884 2884 HOH HOH B . 
EA 6 HOH 560 2885 2885 HOH HOH B . 
EA 6 HOH 561 2886 2886 HOH HOH B . 
EA 6 HOH 562 2887 2887 HOH HOH B . 
EA 6 HOH 563 2888 2888 HOH HOH B . 
EA 6 HOH 564 2889 2889 HOH HOH B . 
EA 6 HOH 565 2890 2890 HOH HOH B . 
EA 6 HOH 566 2891 2891 HOH HOH B . 
EA 6 HOH 567 2892 2892 HOH HOH B . 
EA 6 HOH 568 2893 2893 HOH HOH B . 
EA 6 HOH 569 2894 2894 HOH HOH B . 
EA 6 HOH 570 2895 2895 HOH HOH B . 
EA 6 HOH 571 2896 2896 HOH HOH B . 
EA 6 HOH 572 2897 2897 HOH HOH B . 
EA 6 HOH 573 2898 2898 HOH HOH B . 
EA 6 HOH 574 2899 2899 HOH HOH B . 
EA 6 HOH 575 2900 2900 HOH HOH B . 
EA 6 HOH 576 2901 2901 HOH HOH B . 
EA 6 HOH 577 2902 2902 HOH HOH B . 
EA 6 HOH 578 2903 2903 HOH HOH B . 
EA 6 HOH 579 2904 2904 HOH HOH B . 
EA 6 HOH 580 2905 2905 HOH HOH B . 
EA 6 HOH 581 2906 2906 HOH HOH B . 
EA 6 HOH 582 2907 2907 HOH HOH B . 
EA 6 HOH 583 2908 2908 HOH HOH B . 
EA 6 HOH 584 2909 2909 HOH HOH B . 
EA 6 HOH 585 2910 2910 HOH HOH B . 
EA 6 HOH 586 2911 2911 HOH HOH B . 
EA 6 HOH 587 2912 2912 HOH HOH B . 
EA 6 HOH 588 2913 2913 HOH HOH B . 
EA 6 HOH 589 2914 2914 HOH HOH B . 
EA 6 HOH 590 2915 2915 HOH HOH B . 
EA 6 HOH 591 2916 2916 HOH HOH B . 
EA 6 HOH 592 2917 2917 HOH HOH B . 
EA 6 HOH 593 2918 2918 HOH HOH B . 
EA 6 HOH 594 2919 2919 HOH HOH B . 
EA 6 HOH 595 2920 2920 HOH HOH B . 
EA 6 HOH 596 2921 2921 HOH HOH B . 
EA 6 HOH 597 2922 2922 HOH HOH B . 
EA 6 HOH 598 2923 2923 HOH HOH B . 
EA 6 HOH 599 2924 2924 HOH HOH B . 
EA 6 HOH 600 2925 2925 HOH HOH B . 
EA 6 HOH 601 2926 2926 HOH HOH B . 
EA 6 HOH 602 2927 2927 HOH HOH B . 
EA 6 HOH 603 2928 2928 HOH HOH B . 
EA 6 HOH 604 2929 2929 HOH HOH B . 
EA 6 HOH 605 2930 2930 HOH HOH B . 
EA 6 HOH 606 2931 2931 HOH HOH B . 
EA 6 HOH 607 2932 2932 HOH HOH B . 
EA 6 HOH 608 2933 2933 HOH HOH B . 
EA 6 HOH 609 2934 2934 HOH HOH B . 
EA 6 HOH 610 2935 2935 HOH HOH B . 
EA 6 HOH 611 2936 2936 HOH HOH B . 
EA 6 HOH 612 2937 2937 HOH HOH B . 
EA 6 HOH 613 2938 2938 HOH HOH B . 
EA 6 HOH 614 2939 2939 HOH HOH B . 
EA 6 HOH 615 2940 2940 HOH HOH B . 
EA 6 HOH 616 2941 2941 HOH HOH B . 
EA 6 HOH 617 2942 2942 HOH HOH B . 
EA 6 HOH 618 2943 2943 HOH HOH B . 
EA 6 HOH 619 2944 2944 HOH HOH B . 
EA 6 HOH 620 2945 2945 HOH HOH B . 
EA 6 HOH 621 2946 2946 HOH HOH B . 
EA 6 HOH 622 2947 2947 HOH HOH B . 
EA 6 HOH 623 2948 2948 HOH HOH B . 
EA 6 HOH 624 2949 2949 HOH HOH B . 
EA 6 HOH 625 2950 2950 HOH HOH B . 
EA 6 HOH 626 2951 2951 HOH HOH B . 
EA 6 HOH 627 2952 2952 HOH HOH B . 
EA 6 HOH 628 2953 2953 HOH HOH B . 
EA 6 HOH 629 2954 2954 HOH HOH B . 
EA 6 HOH 630 2955 2955 HOH HOH B . 
EA 6 HOH 631 2956 2956 HOH HOH B . 
EA 6 HOH 632 2957 2957 HOH HOH B . 
EA 6 HOH 633 2958 2958 HOH HOH B . 
EA 6 HOH 634 2959 2959 HOH HOH B . 
EA 6 HOH 635 2960 2960 HOH HOH B . 
EA 6 HOH 636 2961 2961 HOH HOH B . 
EA 6 HOH 637 2962 2962 HOH HOH B . 
EA 6 HOH 638 2963 2963 HOH HOH B . 
EA 6 HOH 639 2964 2964 HOH HOH B . 
EA 6 HOH 640 2965 2965 HOH HOH B . 
EA 6 HOH 641 2966 2966 HOH HOH B . 
EA 6 HOH 642 2967 2967 HOH HOH B . 
EA 6 HOH 643 2968 2968 HOH HOH B . 
EA 6 HOH 644 2969 2969 HOH HOH B . 
EA 6 HOH 645 2970 2970 HOH HOH B . 
EA 6 HOH 646 2971 2971 HOH HOH B . 
EA 6 HOH 647 2972 2972 HOH HOH B . 
EA 6 HOH 648 2973 2973 HOH HOH B . 
FA 6 HOH 1   2286 2286 HOH HOH L . 
FA 6 HOH 2   2287 2287 HOH HOH L . 
GA 6 HOH 1   2285 2285 HOH HOH N . 
GA 6 HOH 2   2298 2298 HOH HOH N . 
HA 6 HOH 1   2294 2294 HOH HOH O . 
HA 6 HOH 2   2297 2297 HOH HOH O . 
IA 6 HOH 1   2290 2290 HOH HOH Q . 
JA 6 HOH 1   2289 2289 HOH HOH R . 
JA 6 HOH 2   2291 2291 HOH HOH R . 
JA 6 HOH 3   2293 2293 HOH HOH R . 
KA 6 HOH 1   2284 2284 HOH HOH S . 
KA 6 HOH 2   2292 2292 HOH HOH S . 
KA 6 HOH 3   2295 2295 HOH HOH S . 
LA 6 HOH 1   2283 2283 HOH HOH T . 
LA 6 HOH 2   2288 2288 HOH HOH T . 
LA 6 HOH 3   2296 2296 HOH HOH T . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A ASN 85  A ASN 85  ? ASN 'GLYCOSYLATION SITE' 
2  A ASN 92  A ASN 92  ? ASN 'GLYCOSYLATION SITE' 
3  A ASN 150 A ASN 150 ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 219 A ASN 219 ? ASN 'GLYCOSYLATION SITE' 
5  A ASN 229 A ASN 229 ? ASN 'GLYCOSYLATION SITE' 
6  A ASN 281 A ASN 281 ? ASN 'GLYCOSYLATION SITE' 
7  A ASN 321 A ASN 321 ? ASN 'GLYCOSYLATION SITE' 
8  A ASN 520 A ASN 520 ? ASN 'GLYCOSYLATION SITE' 
9  B ASN 85  B ASN 85  ? ASN 'GLYCOSYLATION SITE' 
10 B ASN 92  B ASN 92  ? ASN 'GLYCOSYLATION SITE' 
11 B ASN 150 B ASN 150 ? ASN 'GLYCOSYLATION SITE' 
12 B ASN 219 B ASN 219 ? ASN 'GLYCOSYLATION SITE' 
13 B ASN 229 B ASN 229 ? ASN 'GLYCOSYLATION SITE' 
14 B ASN 281 B ASN 281 ? ASN 'GLYCOSYLATION SITE' 
15 B ASN 321 B ASN 321 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   undecameric 
_pdbx_struct_assembly.oligomeric_count     11 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA 
# 
_pdbx_struct_assembly_prop.biol_id   1 
_pdbx_struct_assembly_prop.type      'ABSA (A^2)' 
_pdbx_struct_assembly_prop.value     10880 
_pdbx_struct_assembly_prop.details   ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   GLY 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    490 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    GLY 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     490 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    NA 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     1521 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   LEU 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    491 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    LEU 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     491 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 82.9 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 
1 'Structure model' 1 0 2007-11-06 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
CNS         .       ?              package 'Axel T. Brunger' axel.brunger@yale.edu    refinement        
http://cns.csb.yale.edu/v1.1/    Fortran_77 ? 1 
PDB_EXTRACT 3.000   'July 2, 2007' package PDB               sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/ C++        ? 2 
ADSC        Quantum ?              ?       ?                 ?                        'data collection' ? ?          ? 3 
HKL-2000    .       ?              ?       ?                 ?                        'data reduction'  ? ?          ? 4 
HKL-2000    .       ?              ?       ?                 ?                        'data scaling'    ? ?          ? 5 
CNX         .       ?              ?       ?                 ?                        phasing           ? ?          ? 6 
CNX         .       ?              ?       ?                 ?                        refinement        ? ?          ? 7 
# 
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 TYR A 58  ? ? -152.18 80.52   
2  1 SER A 64  ? ? -164.17 -166.77 
3  1 GLN A 123 ? ? -114.90 -104.77 
4  1 TRP A 124 ? ? -87.97  -146.46 
5  1 HIS A 162 ? ? -148.41 31.84   
6  1 ILE A 193 ? ? -128.75 -61.98  
7  1 VAL A 207 ? ? -99.80  -61.79  
8  1 SER A 242 ? ? 62.97   -166.14 
9  1 GLN A 320 ? ? -63.07  44.26   
10 1 ASN A 450 ? ? -164.36 77.66   
11 1 LYS A 536 ? ? -58.38  -8.92   
12 1 TYR A 547 ? ? -126.95 -70.52  
13 1 ARG A 597 ? ? -140.74 52.33   
14 1 THR A 600 ? ? -120.96 -89.85  
15 1 SER A 630 ? ? 63.19   -122.99 
16 1 ASP A 678 ? ? -107.91 -98.86  
17 1 ASN A 710 ? ? -90.69  -71.04  
18 1 ASP A 739 ? ? -100.61 -160.90 
19 1 ILE A 742 ? ? 34.78   52.78   
20 1 ASN B 74  ? ? 69.16   -7.57   
21 1 SER B 106 ? ? -162.25 118.23  
22 1 GLN B 123 ? ? -117.99 -99.33  
23 1 TRP B 124 ? ? -94.53  -141.68 
24 1 ASN B 138 ? ? -63.42  -76.79  
25 1 LYS B 139 ? ? -69.89  12.94   
26 1 ARG B 140 ? ? 36.59   55.84   
27 1 HIS B 162 ? ? -154.36 35.64   
28 1 ASP B 192 ? ? 59.47   9.27    
29 1 ILE B 193 ? ? -126.57 -60.59  
30 1 SER B 242 ? ? 63.12   -163.79 
31 1 GLN B 320 ? ? -65.67  48.64   
32 1 GLU B 332 ? ? -59.56  -8.15   
33 1 THR B 350 ? ? -111.34 -89.22  
34 1 ASP B 367 ? ? -69.47  0.42    
35 1 ASN B 377 ? ? -79.97  -167.49 
36 1 LYS B 423 ? ? 49.36   26.46   
37 1 ASP B 438 ? ? -162.04 91.71   
38 1 ASN B 450 ? ? -159.15 76.88   
39 1 ARG B 492 ? ? 176.36  163.58  
40 1 TYR B 547 ? ? -131.79 -70.27  
41 1 ARG B 596 ? ? 57.16   8.32    
42 1 THR B 600 ? ? -120.40 -93.83  
43 1 SER B 630 ? ? 64.74   -121.64 
44 1 ASP B 678 ? ? -128.55 -93.76  
45 1 ASN B 710 ? ? -90.20  -72.66  
46 1 ASP B 739 ? ? -102.57 -157.74 
47 1 ILE B 742 ? ? 37.01   54.28   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 TYR A 700 ? ? 0.076 'SIDE CHAIN' 
2 1 TYR B 700 ? ? 0.068 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1  ? A MET 1  
2  1 Y 1 A LYS 2  ? A LYS 2  
3  1 Y 1 A THR 3  ? A THR 3  
4  1 Y 1 A PRO 4  ? A PRO 4  
5  1 Y 1 A TRP 5  ? A TRP 5  
6  1 Y 1 A LYS 6  ? A LYS 6  
7  1 Y 1 A VAL 7  ? A VAL 7  
8  1 Y 1 A LEU 8  ? A LEU 8  
9  1 Y 1 A LEU 9  ? A LEU 9  
10 1 Y 1 A GLY 10 ? A GLY 10 
11 1 Y 1 A LEU 11 ? A LEU 11 
12 1 Y 1 A LEU 12 ? A LEU 12 
13 1 Y 1 A GLY 13 ? A GLY 13 
14 1 Y 1 A ALA 14 ? A ALA 14 
15 1 Y 1 A ALA 15 ? A ALA 15 
16 1 Y 1 A ALA 16 ? A ALA 16 
17 1 Y 1 A LEU 17 ? A LEU 17 
18 1 Y 1 A VAL 18 ? A VAL 18 
19 1 Y 1 A THR 19 ? A THR 19 
20 1 Y 1 A ILE 20 ? A ILE 20 
21 1 Y 1 A ILE 21 ? A ILE 21 
22 1 Y 1 A THR 22 ? A THR 22 
23 1 Y 1 A VAL 23 ? A VAL 23 
24 1 Y 1 A PRO 24 ? A PRO 24 
25 1 Y 1 A VAL 25 ? A VAL 25 
26 1 Y 1 A VAL 26 ? A VAL 26 
27 1 Y 1 A LEU 27 ? A LEU 27 
28 1 Y 1 A LEU 28 ? A LEU 28 
29 1 Y 1 A ASN 29 ? A ASN 29 
30 1 Y 1 A LYS 30 ? A LYS 30 
31 1 Y 1 A GLY 31 ? A GLY 31 
32 1 Y 1 A THR 32 ? A THR 32 
33 1 Y 1 A ASP 33 ? A ASP 33 
34 1 Y 1 A ASP 34 ? A ASP 34 
35 1 Y 1 A ALA 35 ? A ALA 35 
36 1 Y 1 A THR 36 ? A THR 36 
37 1 Y 1 A ALA 37 ? A ALA 37 
38 1 Y 1 A ASP 38 ? A ASP 38 
39 1 Y 1 B MET 1  ? B MET 1  
40 1 Y 1 B LYS 2  ? B LYS 2  
41 1 Y 1 B THR 3  ? B THR 3  
42 1 Y 1 B PRO 4  ? B PRO 4  
43 1 Y 1 B TRP 5  ? B TRP 5  
44 1 Y 1 B LYS 6  ? B LYS 6  
45 1 Y 1 B VAL 7  ? B VAL 7  
46 1 Y 1 B LEU 8  ? B LEU 8  
47 1 Y 1 B LEU 9  ? B LEU 9  
48 1 Y 1 B GLY 10 ? B GLY 10 
49 1 Y 1 B LEU 11 ? B LEU 11 
50 1 Y 1 B LEU 12 ? B LEU 12 
51 1 Y 1 B GLY 13 ? B GLY 13 
52 1 Y 1 B ALA 14 ? B ALA 14 
53 1 Y 1 B ALA 15 ? B ALA 15 
54 1 Y 1 B ALA 16 ? B ALA 16 
55 1 Y 1 B LEU 17 ? B LEU 17 
56 1 Y 1 B VAL 18 ? B VAL 18 
57 1 Y 1 B THR 19 ? B THR 19 
58 1 Y 1 B ILE 20 ? B ILE 20 
59 1 Y 1 B ILE 21 ? B ILE 21 
60 1 Y 1 B THR 22 ? B THR 22 
61 1 Y 1 B VAL 23 ? B VAL 23 
62 1 Y 1 B PRO 24 ? B PRO 24 
63 1 Y 1 B VAL 25 ? B VAL 25 
64 1 Y 1 B VAL 26 ? B VAL 26 
65 1 Y 1 B LEU 27 ? B LEU 27 
66 1 Y 1 B LEU 28 ? B LEU 28 
67 1 Y 1 B ASN 29 ? B ASN 29 
68 1 Y 1 B LYS 30 ? B LYS 30 
69 1 Y 1 B GLY 31 ? B GLY 31 
70 1 Y 1 B THR 32 ? B THR 32 
71 1 Y 1 B ASP 33 ? B ASP 33 
72 1 Y 1 B ASP 34 ? B ASP 34 
73 1 Y 1 B ALA 35 ? B ALA 35 
74 1 Y 1 B THR 36 ? B THR 36 
75 1 Y 1 B ALA 37 ? B ALA 37 
76 1 Y 1 B ASP 38 ? B ASP 38 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 'SODIUM ION' NA  
4 
;(2S,3S)-3-AMINO-4-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-5-YLCYCLOHEXYL)BUTANAMIDE
;
524 
5 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 
6 water HOH 
# 
