data_2QTB
# 
_entry.id   2QTB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2QTB         
RCSB  RCSB044028   
WWPDB D_1000044028 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          2QT9 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        2QTB 
_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                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
_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           2QTB 
_cell.length_a           117.863 
_cell.length_b           125.629 
_cell.length_c           136.806 
_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                         2QTB 
_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-(3,3-DIFLUOROPYRROLIDIN-1-YL)-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-6-YLCYCLOHEXYL)BUTANAMIDE
;
448.509   2   ?        ?    ? ? 
5 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208   4   ?        ?    ? ? 
6 water       nat water 18.015    921 ?        ?    ? ? 
# 
_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 2QTB A 1 ? 766 ? P27487 1 ? 766 ? 1 766 
2 1 2QTB 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 2QTB THR A 39 ? UNP P27487 SER 39 ENGINEERED 39 1 
2 2QTB 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 
474 non-polymer         . 
;(2S,3S)-3-AMINO-4-(3,3-DIFLUOROPYRROLIDIN-1-YL)-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-6-YLCYCLOHEXYL)BUTANAMIDE
;
;6-(4-{(1S,2S)-2-AMMONIO-3-(3,3-DIFLUOROPYRROLIDIN-1-YL)-1-[(DIMETHYLAMINO)CARBONYL] -3-OXOPROPYL}CYCLOHEXYL)[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-1-IUM
;
'C22 H30 F2 N6 O2' 448.509 
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          2QTB 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.86 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   57.07 
_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 8.000000, vapor diffusion, hanging drop, temperature 293K' 
_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   2004-06-16 
_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             ? 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.entry_id                     2QTB 
_reflns.observed_criterion_sigma_F   -3.0 
_reflns.observed_criterion_sigma_I   -3.00 
_reflns.d_resolution_high            2.25 
_reflns.d_resolution_low             50.000 
_reflns.number_all                   ? 
_reflns.number_obs                   96646 
_reflns.percent_possible_obs         99.7 
_reflns.pdbx_Rmerge_I_obs            0.090 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.5 
_reflns.B_iso_Wilson_estimate        31.3 
_reflns.pdbx_redundancy              7.3 
_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             2.25 
_reflns_shell.d_res_low              2.33 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   99.2 
_reflns_shell.Rmerge_I_obs           0.443 
_reflns_shell.meanI_over_sigI_obs    1.6 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        7.1 
_reflns_shell.number_unique_all      9531 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2QTB 
_refine.ls_d_res_high                            2.250 
_refine.ls_d_res_low                             30.000 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    99.700 
_refine.ls_number_reflns_obs                     96468 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.ls_R_factor_R_work                       0.187 
_refine.ls_R_factor_R_free                       0.228 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  4847 
_refine.B_iso_mean                               27.900 
_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]                            7.855 
_refine.aniso_B[2][2]                            -3.180 
_refine.aniso_B[3][3]                            -4.675 
_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_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_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                        2QTB 
_refine_analyze.Luzzati_coordinate_error_obs    0.240 
_refine_analyze.Luzzati_sigma_a_obs             0.200 
_refine_analyze.Luzzati_d_res_low_obs           5.000 
_refine_analyze.Luzzati_coordinate_error_free   0.300 
_refine_analyze.Luzzati_sigma_a_free            0.270 
_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         401 
_refine_hist.number_atoms_solvent             921 
_refine_hist.number_atoms_total               13252 
_refine_hist.d_res_high                       2.250 
_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        ? 1.440  ?     ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d ? 24.739 ?     ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d ? 0.842  ?     ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it        ? 0.990  1.500 ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it       ? 1.630  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scbond_it        ? 1.570  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scangle_it       ? 2.370  2.500 ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       2.250 
_refine_ls_shell.d_res_low                        2.330 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.percent_reflns_obs               99.200 
_refine_ls_shell.number_reflns_R_work             9047 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.237 
_refine_ls_shell.R_factor_R_free                  0.304 
_refine_ls_shell.percent_reflns_R_free            5.000 
_refine_ls_shell.number_reflns_R_free             476 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                9523 
_refine_ls_shell.number_reflns_obs                9523 
_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                  2QTB 
_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        2QTB 
_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 ? 
# 
_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  ? LYS A 50  ? THR A 44  LYS A 50  1 ? 7  
HELX_P HELX_P2  2  ASP A 200 ? VAL A 207 ? ASP A 200 VAL A 207 1 ? 8  
HELX_P HELX_P3  3  PRO A 290 ? ILE A 295 ? PRO A 290 ILE A 295 1 ? 6  
HELX_P HELX_P4  4  LEU A 340 ? GLN A 344 ? LEU A 340 GLN A 344 5 ? 5  
HELX_P HELX_P5  5  GLU A 421 ? MET A 425 ? GLU A 421 MET A 425 5 ? 5  
HELX_P HELX_P6  6  ASN A 497 ? GLN A 505 ? ASN A 497 GLN A 505 1 ? 9  
HELX_P HELX_P7  7  ASN A 562 ? THR A 570 ? ASN A 562 THR A 570 1 ? 9  
HELX_P HELX_P8  8  GLY A 587 ? HIS A 592 ? GLY A 587 HIS A 592 1 ? 6  
HELX_P HELX_P9  9  ALA A 593 ? ASN A 595 ? ALA A 593 ASN A 595 5 ? 3  
HELX_P HELX_P10 10 THR A 600 ? LYS A 615 ? THR A 600 LYS A 615 1 ? 16 
HELX_P HELX_P11 11 SER A 630 ? GLY A 641 ? SER A 630 GLY A 641 1 ? 12 
HELX_P HELX_P12 12 ARG A 658 ? TYR A 662 ? ARG A 658 TYR A 662 5 ? 5  
HELX_P HELX_P13 13 ASP A 663 ? GLY A 672 ? ASP A 663 GLY A 672 1 ? 10 
HELX_P HELX_P14 14 ASN A 679 ? SER A 686 ? ASN A 679 SER A 686 1 ? 8  
HELX_P HELX_P15 15 VAL A 688 ? VAL A 698 ? VAL A 688 VAL A 698 5 ? 11 
HELX_P HELX_P16 16 HIS A 712 ? VAL A 726 ? HIS A 712 VAL A 726 1 ? 15 
HELX_P HELX_P17 17 SER A 744 ? PHE A 763 ? SER A 744 PHE A 763 1 ? 20 
HELX_P HELX_P18 18 THR B 44  ? ASN B 51  ? THR B 44  ASN B 51  1 ? 8  
HELX_P HELX_P19 19 ASP B 200 ? VAL B 207 ? ASP B 200 VAL B 207 1 ? 8  
HELX_P HELX_P20 20 ASP B 274 ? LEU B 276 ? ASP B 274 LEU B 276 5 ? 3  
HELX_P HELX_P21 21 PRO B 290 ? ILE B 295 ? PRO B 290 ILE B 295 1 ? 6  
HELX_P HELX_P22 22 VAL B 341 ? GLN B 344 ? VAL B 341 GLN B 344 5 ? 4  
HELX_P HELX_P23 23 GLU B 421 ? MET B 425 ? GLU B 421 MET B 425 5 ? 5  
HELX_P HELX_P24 24 ASN B 497 ? GLN B 505 ? ASN B 497 GLN B 505 1 ? 9  
HELX_P HELX_P25 25 ASN B 562 ? THR B 570 ? ASN B 562 THR B 570 1 ? 9  
HELX_P HELX_P26 26 GLY B 587 ? HIS B 592 ? GLY B 587 HIS B 592 1 ? 6  
HELX_P HELX_P27 27 ALA B 593 ? ASN B 595 ? ALA B 593 ASN B 595 5 ? 3  
HELX_P HELX_P28 28 THR B 600 ? LYS B 615 ? THR B 600 LYS B 615 1 ? 16 
HELX_P HELX_P29 29 SER B 630 ? GLY B 641 ? SER B 630 GLY B 641 1 ? 12 
HELX_P HELX_P30 30 ARG B 658 ? TYR B 662 ? ARG B 658 TYR B 662 5 ? 5  
HELX_P HELX_P31 31 ASP B 663 ? GLY B 672 ? ASP B 663 GLY B 672 1 ? 10 
HELX_P HELX_P32 32 ASN B 679 ? SER B 686 ? ASN B 679 SER B 686 1 ? 8  
HELX_P HELX_P33 33 VAL B 688 ? VAL B 698 ? VAL B 688 VAL B 698 5 ? 11 
HELX_P HELX_P34 34 PHE B 713 ? VAL B 726 ? PHE B 713 VAL B 726 1 ? 14 
HELX_P HELX_P35 35 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 ? ? ? ? ? ? ? 2.052 ? 
disulf2  disulf ? ? A  CYS 385 SG  ? ? ? 1_555 A  CYS 394 SG ? ? A CYS 385  A CYS 394  1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf3  disulf ? ? A  CYS 444 SG  ? ? ? 1_555 A  CYS 447 SG ? ? A CYS 444  A CYS 447  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf4  disulf ? ? A  CYS 454 SG  ? ? ? 1_555 A  CYS 472 SG ? ? A CYS 454  A CYS 472  1_555 ? ? ? ? ? ? ? 2.089 ? 
disulf5  disulf ? ? A  CYS 649 SG  ? ? ? 1_555 A  CYS 762 SG ? ? A CYS 649  A CYS 762  1_555 ? ? ? ? ? ? ? 2.070 ? 
disulf6  disulf ? ? B  CYS 328 SG  ? ? ? 1_555 B  CYS 339 SG ? ? B CYS 328  B CYS 339  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf7  disulf ? ? B  CYS 385 SG  ? ? ? 1_555 B  CYS 394 SG ? ? B CYS 385  B CYS 394  1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf8  disulf ? ? B  CYS 444 SG  ? ? ? 1_555 B  CYS 447 SG ? ? B CYS 444  B CYS 447  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf9  disulf ? ? B  CYS 454 SG  ? ? ? 1_555 B  CYS 472 SG ? ? B CYS 454  B CYS 472  1_555 ? ? ? ? ? ? ? 2.092 ? 
disulf10 disulf ? ? B  CYS 649 SG  ? ? ? 1_555 B  CYS 762 SG ? ? B CYS 649  B CYS 762  1_555 ? ? ? ? ? ? ? 2.061 ? 
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 ? ? ? ? ? ? ? 1.459 ? 
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  M 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 ? ? ? ? ? ? ? 1.450 ? 
covale6  covale ? ? A  ASN 281 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 281  A NAG 1281 1_555 ? ? ? ? ? ? ? 1.458 ? 
covale7  covale ? ? A  ASN 321 ND2 ? ? ? 1_555 T  NDG .   C1 ? ? A ASN 321  P NDG 1321 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale8  covale ? ? A  ASN 520 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 520  A NAG 1520 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale9  covale ? ? B  ASN 85  ND2 ? ? ? 1_555 V  NAG .   C1 ? ? B ASN 85   Q NAG 2085 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale10 covale ? ? B  ASN 92  ND2 ? ? ? 1_555 H  NAG .   C1 ? ? B ASN 92   B NAG 2092 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale11 covale ? ? B  ASN 150 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? B ASN 150  B NAG 2150 1_555 ? ? ? ? ? ? ? 1.458 ? 
covale12 covale ? ? B  ASN 219 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? B ASN 219  R NAG 2219 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale13 covale ? ? B  ASN 229 ND2 ? ? ? 1_555 Z  NAG .   C1 ? ? B ASN 229  S NAG 2229 1_555 ? ? ? ? ? ? ? 1.449 ? 
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 ? ? ? ? ? ? ? 1.445 ? 
covale16 covale ? ? L  NAG .   O4  ? ? ? 1_555 M  NDG .   C1 ? ? L NAG 1085 L NDG 1086 1_555 ? ? ? ? ? ? ? 1.392 ? 
covale17 covale ? ? N  NDG .   O4  ? ? ? 1_555 O  NAG .   C1 ? ? M NDG 1150 M NAG 1151 1_555 ? ? ? ? ? ? ? 1.391 ? 
covale18 covale ? ? P  NAG .   O4  ? ? ? 1_555 Q  NAG .   C1 ? ? M NAG 1219 M NAG 1220 1_555 ? ? ? ? ? ? ? 1.384 ? 
covale19 covale ? ? R  NAG .   O4  ? ? ? 1_555 S  NDG .   C1 ? ? O NAG 1229 O NDG 1230 1_555 ? ? ? ? ? ? ? 1.386 ? 
covale20 covale ? ? T  NDG .   O4  ? ? ? 1_555 U  NAG .   C1 ? ? P NDG 1321 P NAG 1322 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale21 covale ? ? V  NAG .   O4  ? ? ? 1_555 W  NAG .   C1 ? ? Q NAG 2085 Q NAG 2086 1_555 ? ? ? ? ? ? ? 1.386 ? 
covale22 covale ? ? X  NAG .   O4  ? ? ? 1_555 Y  NAG .   C1 ? ? R NAG 2219 R NAG 2220 1_555 ? ? ? ? ? ? ? 1.384 ? 
covale23 covale ? ? Z  NAG .   O4  ? ? ? 1_555 AA NAG .   C1 ? ? S NAG 2229 S NAG 2230 1_555 ? ? ? ? ? ? ? 1.384 ? 
covale24 covale ? ? BA NAG .   O4  ? ? ? 1_555 CA NAG .   C1 ? ? T NAG 2281 T NAG 2282 1_555 ? ? ? ? ? ? ? 1.385 ? 
metalc1  metalc ? ? A  GLY 490 O   ? ? ? 1_555 F  NA  .   NA ? ? A GLY 490  A NA  1522 1_555 ? ? ? ? ? ? ? 2.254 ? 
metalc2  metalc ? ? A  LEU 491 O   ? ? ? 1_555 F  NA  .   NA ? ? A LEU 491  A NA  1522 1_555 ? ? ? ? ? ? ? 2.451 ? 
# 
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 0.52  
2 GLY 474 B . ? GLY 474 B PRO 475 B ? PRO 475 B 1 -0.93 
# 
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 ARG A 61  ? TRP A 62  ? ARG A 61  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 ILE A 285 ? ILE A 287 ? ILE A 285 ILE A 287 
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 ? ASN A 338 ? ARG A 336 ASN A 338 
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 ? ASP A 545 ? TYR A 540 ASP A 545 
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 ASP B 438 ? CYS B 444 ? ASP B 438 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 ASN A 103 ? N ASN A 103 O GLU A 117 ? O GLU A 117 
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 TYR A 166 ? N TYR A 166 O TYR A 173 ? O TYR A 173 
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 TYR A 299 ? N TYR A 299 O LEU A 316 ? O LEU A 316 
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 TYR A 299 ? N TYR A 299 O LEU A 316 ? O LEU A 316 
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 ILE A 405 ? N ILE A 405 O ILE A 418 ? O ILE A 418 
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 ALA A 576 ? O ALA A 576 N ASP A 545 ? N ASP A 545 
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 TRP B 154 ? N TRP B 154 O VAL B 167 ? O VAL B 167 
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 ILE B 703 ? O ILE B 703 
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 ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG M 1151' 
AC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG M 1219' 
AC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG M 1220' 
AC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG O 1229' 
AC9 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NDG O 1230' 
BC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 1281' 
BC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NDG P 1321' 
BC3 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG P 1322' 
BC4 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 1520' 
BC5 Software ? ? ? ? 6  '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 ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG R 2219' 
CC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG R 2220' 
CC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG S 2229' 
CC3 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG S 2230' 
CC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG T 2281' 
CC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG T 2282' 
CC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 2321' 
CC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NA A 1522'  
CC8 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE 474 A 1521' 
CC9 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE 474 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 1633 . ? 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 1  NDG N  .   ? NDG M 1150 . ? 1_555 ? 
17  AC6 5  ASN A  219 ? ASN A 219  . ? 1_555 ? 
18  AC6 5  THR A  221 ? THR A 221  . ? 1_555 ? 
19  AC6 5  GLN A  308 ? GLN A 308  . ? 1_555 ? 
20  AC6 5  GLU A  309 ? GLU A 309  . ? 1_555 ? 
21  AC6 5  NAG Q  .   ? NAG M 1220 . ? 1_555 ? 
22  AC7 5  PHE A  222 ? PHE A 222  . ? 1_555 ? 
23  AC7 5  TYR A  330 ? TYR A 330  . ? 1_555 ? 
24  AC7 5  GLU A  332 ? GLU A 332  . ? 1_555 ? 
25  AC7 5  HOH FA .   ? HOH M 246  . ? 1_555 ? 
26  AC7 5  NAG P  .   ? NAG M 1219 . ? 1_555 ? 
27  AC8 5  ASN A  229 ? ASN A 229  . ? 1_555 ? 
28  AC8 5  THR A  231 ? THR A 231  . ? 1_555 ? 
29  AC8 5  GLU A  232 ? GLU A 232  . ? 1_555 ? 
30  AC8 5  HOH GA .   ? HOH O 760  . ? 1_555 ? 
31  AC8 5  NDG S  .   ? NDG O 1230 . ? 1_555 ? 
32  AC9 1  NAG R  .   ? NAG O 1229 . ? 1_555 ? 
33  BC1 4  TRP A  187 ? TRP A 187  . ? 1_555 ? 
34  BC1 4  VAL A  279 ? VAL A 279  . ? 1_555 ? 
35  BC1 4  ASN A  281 ? ASN A 281  . ? 1_555 ? 
36  BC1 4  HOH DA .   ? HOH A 1654 . ? 1_555 ? 
37  BC2 6  ASN A  321 ? ASN A 321  . ? 1_555 ? 
38  BC2 6  MET A  348 ? MET A 348  . ? 1_555 ? 
39  BC2 6  SER A  349 ? SER A 349  . ? 1_555 ? 
40  BC2 6  THR A  350 ? THR A 350  . ? 1_555 ? 
41  BC2 6  HOH DA .   ? HOH A 1578 . ? 1_555 ? 
42  BC2 6  NAG U  .   ? NAG P 1322 . ? 1_555 ? 
43  BC3 2  ASP A  678 ? ASP A 678  . ? 1_555 ? 
44  BC3 2  NDG T  .   ? NDG P 1321 . ? 1_555 ? 
45  BC4 2  ASN A  520 ? ASN A 520  . ? 1_555 ? 
46  BC4 2  ARG A  581 ? ARG A 581  . ? 1_555 ? 
47  BC5 6  VAL B  78  ? VAL B 78   . ? 1_555 ? 
48  BC5 6  ASN B  85  ? ASN B 85   . ? 1_555 ? 
49  BC5 6  SER B  86  ? SER B 86   . ? 1_555 ? 
50  BC5 6  SER B  87  ? SER B 87   . ? 1_555 ? 
51  BC5 6  HOH HA .   ? HOH Q 524  . ? 1_555 ? 
52  BC5 6  NAG W  .   ? NAG Q 2086 . ? 1_555 ? 
53  BC6 1  NAG V  .   ? NAG Q 2085 . ? 1_555 ? 
54  BC7 5  GLU B  73  ? GLU B 73   . ? 1_555 ? 
55  BC7 5  ASN B  74  ? ASN B 74   . ? 1_555 ? 
56  BC7 5  ASN B  75  ? ASN B 75   . ? 1_555 ? 
57  BC7 5  ASN B  92  ? ASN B 92   . ? 1_555 ? 
58  BC7 5  HOH EA .   ? HOH B 2477 . ? 1_555 ? 
59  BC8 4  ARG B  147 ? ARG B 147  . ? 1_555 ? 
60  BC8 4  ILE B  148 ? ILE B 148  . ? 1_555 ? 
61  BC8 4  ASN B  150 ? ASN B 150  . ? 1_555 ? 
62  BC8 4  HOH EA .   ? HOH B 2443 . ? 1_555 ? 
63  BC9 5  ASN B  219 ? ASN B 219  . ? 1_555 ? 
64  BC9 5  THR B  221 ? THR B 221  . ? 1_555 ? 
65  BC9 5  GLN B  308 ? GLN B 308  . ? 1_555 ? 
66  BC9 5  GLU B  309 ? GLU B 309  . ? 1_555 ? 
67  BC9 5  NAG Y  .   ? NAG R 2220 . ? 1_555 ? 
68  CC1 7  PHE B  222 ? PHE B 222  . ? 1_555 ? 
69  CC1 7  ASN B  272 ? ASN B 272  . ? 1_555 ? 
70  CC1 7  TYR B  330 ? TYR B 330  . ? 1_555 ? 
71  CC1 7  GLU B  332 ? GLU B 332  . ? 1_555 ? 
72  CC1 7  HOH IA .   ? HOH R 466  . ? 1_555 ? 
73  CC1 7  HOH IA .   ? HOH R 529  . ? 1_555 ? 
74  CC1 7  NAG X  .   ? NAG R 2219 . ? 1_555 ? 
75  CC2 6  ILE B  194 ? ILE B 194  . ? 1_555 ? 
76  CC2 6  ASN B  229 ? ASN B 229  . ? 1_555 ? 
77  CC2 6  THR B  231 ? THR B 231  . ? 1_555 ? 
78  CC2 6  GLU B  232 ? GLU B 232  . ? 1_555 ? 
79  CC2 6  HOH JA .   ? HOH S 193  . ? 1_555 ? 
80  CC2 6  NAG AA .   ? NAG S 2230 . ? 1_555 ? 
81  CC3 1  NAG Z  .   ? NAG S 2229 . ? 1_555 ? 
82  CC4 5  ASN A  450 ? ASN A 450  . ? 2_564 ? 
83  CC4 5  TRP B  187 ? TRP B 187  . ? 1_555 ? 
84  CC4 5  ASN B  281 ? ASN B 281  . ? 1_555 ? 
85  CC4 5  HOH KA .   ? HOH T 37   . ? 1_555 ? 
86  CC4 5  NAG CA .   ? NAG T 2282 . ? 1_555 ? 
87  CC5 5  THR B  188 ? THR B 188  . ? 1_555 ? 
88  CC5 5  HOH KA .   ? HOH T 37   . ? 1_555 ? 
89  CC5 5  HOH KA .   ? HOH T 483  . ? 1_555 ? 
90  CC5 5  NAG BA .   ? NAG T 2281 . ? 1_555 ? 
91  CC5 5  HOH KA .   ? HOH T 2778 . ? 1_555 ? 
92  CC6 4  ASN B  321 ? ASN B 321  . ? 1_555 ? 
93  CC6 4  SER B  349 ? SER B 349  . ? 1_555 ? 
94  CC6 4  THR B  350 ? THR B 350  . ? 1_555 ? 
95  CC6 4  HOH EA .   ? HOH B 2747 . ? 1_555 ? 
96  CC7 6  GLY A  490 ? GLY A 490  . ? 1_555 ? 
97  CC7 6  LEU A  491 ? LEU A 491  . ? 1_555 ? 
98  CC7 6  LEU B  276 ? LEU B 276  . ? 2_565 ? 
99  CC7 6  SER B  277 ? SER B 277  . ? 2_565 ? 
100 CC7 6  VAL B  279 ? VAL B 279  . ? 2_565 ? 
101 CC7 6  HOH EA .   ? HOH B 2515 . ? 2_565 ? 
102 CC8 15 ARG A  125 ? ARG A 125  . ? 1_555 ? 
103 CC8 15 GLU A  205 ? GLU A 205  . ? 1_555 ? 
104 CC8 15 GLU A  206 ? GLU A 206  . ? 1_555 ? 
105 CC8 15 VAL A  207 ? VAL A 207  . ? 1_555 ? 
106 CC8 15 SER A  209 ? SER A 209  . ? 1_555 ? 
107 CC8 15 ARG A  358 ? ARG A 358  . ? 1_555 ? 
108 CC8 15 TYR A  547 ? TYR A 547  . ? 1_555 ? 
109 CC8 15 SER A  630 ? SER A 630  . ? 1_555 ? 
110 CC8 15 TYR A  631 ? TYR A 631  . ? 1_555 ? 
111 CC8 15 TRP A  659 ? TRP A 659  . ? 1_555 ? 
112 CC8 15 TYR A  662 ? TYR A 662  . ? 1_555 ? 
113 CC8 15 TYR A  666 ? TYR A 666  . ? 1_555 ? 
114 CC8 15 ASN A  710 ? ASN A 710  . ? 1_555 ? 
115 CC8 15 VAL A  711 ? VAL A 711  . ? 1_555 ? 
116 CC8 15 HOH DA .   ? HOH A 1554 . ? 1_555 ? 
117 CC9 15 ARG B  125 ? ARG B 125  . ? 1_555 ? 
118 CC9 15 GLU B  205 ? GLU B 205  . ? 1_555 ? 
119 CC9 15 GLU B  206 ? GLU B 206  . ? 1_555 ? 
120 CC9 15 VAL B  207 ? VAL B 207  . ? 1_555 ? 
121 CC9 15 SER B  209 ? SER B 209  . ? 1_555 ? 
122 CC9 15 ARG B  358 ? ARG B 358  . ? 1_555 ? 
123 CC9 15 TYR B  547 ? TYR B 547  . ? 1_555 ? 
124 CC9 15 SER B  630 ? SER B 630  . ? 1_555 ? 
125 CC9 15 TYR B  631 ? TYR B 631  . ? 1_555 ? 
126 CC9 15 TRP B  659 ? TRP B 659  . ? 1_555 ? 
127 CC9 15 TYR B  662 ? TYR B 662  . ? 1_555 ? 
128 CC9 15 TYR B  666 ? TYR B 666  . ? 1_555 ? 
129 CC9 15 ASN B  710 ? ASN B 710  . ? 1_555 ? 
130 CC9 15 VAL B  711 ? VAL B 711  . ? 1_555 ? 
131 CC9 15 HOH EA .   ? HOH B 2352 . ? 1_555 ? 
# 
_atom_sites.entry_id                    2QTB 
_atom_sites.fract_transf_matrix[1][1]   0.008484 
_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]   0.007960 
_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]   0.007310 
_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  ? 35.685  48.019 78.842 1.00 53.53 ? 39   THR A N   1 
ATOM   2     C  CA  . THR A  1 39  ? 34.882  49.270 78.974 1.00 52.97 ? 39   THR A CA  1 
ATOM   3     C  C   . THR A  1 39  ? 35.115  50.195 77.774 1.00 51.60 ? 39   THR A C   1 
ATOM   4     O  O   . THR A  1 39  ? 34.285  51.063 77.479 1.00 51.80 ? 39   THR A O   1 
ATOM   5     C  CB  . THR A  1 39  ? 35.236  50.036 80.300 1.00 54.34 ? 39   THR A CB  1 
ATOM   6     O  OG1 . THR A  1 39  ? 34.498  51.269 80.368 1.00 55.33 ? 39   THR A OG1 1 
ATOM   7     C  CG2 . THR A  1 39  ? 36.752  50.325 80.385 1.00 54.69 ? 39   THR A CG2 1 
ATOM   8     N  N   . ARG A  1 40  ? 36.233  49.998 77.074 1.00 49.16 ? 40   ARG A N   1 
ATOM   9     C  CA  . ARG A  1 40  ? 36.544  50.843 75.923 1.00 46.19 ? 40   ARG A CA  1 
ATOM   10    C  C   . ARG A  1 40  ? 35.577  50.653 74.745 1.00 43.38 ? 40   ARG A C   1 
ATOM   11    O  O   . ARG A  1 40  ? 34.988  49.583 74.544 1.00 42.91 ? 40   ARG A O   1 
ATOM   12    C  CB  . ARG A  1 40  ? 38.009  50.643 75.478 1.00 46.74 ? 40   ARG A CB  1 
ATOM   13    C  CG  . ARG A  1 40  ? 38.431  49.216 75.275 1.00 48.16 ? 40   ARG A CG  1 
ATOM   14    C  CD  . ARG A  1 40  ? 39.884  49.106 74.792 1.00 48.89 ? 40   ARG A CD  1 
ATOM   15    N  NE  . ARG A  1 40  ? 40.205  47.703 74.495 1.00 49.98 ? 40   ARG A NE  1 
ATOM   16    C  CZ  . ARG A  1 40  ? 41.217  47.290 73.736 1.00 50.01 ? 40   ARG A CZ  1 
ATOM   17    N  NH1 . ARG A  1 40  ? 42.043  48.172 73.174 1.00 49.71 ? 40   ARG A NH1 1 
ATOM   18    N  NH2 . ARG A  1 40  ? 41.391  45.989 73.526 1.00 49.47 ? 40   ARG A NH2 1 
ATOM   19    N  N   . LYS A  1 41  ? 35.415  51.716 73.971 1.00 40.36 ? 41   LYS A N   1 
ATOM   20    C  CA  . LYS A  1 41  ? 34.513  51.706 72.834 1.00 37.24 ? 41   LYS A CA  1 
ATOM   21    C  C   . LYS A  1 41  ? 35.027  50.939 71.621 1.00 34.47 ? 41   LYS A C   1 
ATOM   22    O  O   . LYS A  1 41  ? 36.179  50.505 71.582 1.00 33.49 ? 41   LYS A O   1 
ATOM   23    C  CB  . LYS A  1 41  ? 34.188  53.146 72.444 1.00 38.84 ? 41   LYS A CB  1 
ATOM   24    C  CG  . LYS A  1 41  ? 35.388  54.085 72.401 1.00 40.71 ? 41   LYS A CG  1 
ATOM   25    C  CD  . LYS A  1 41  ? 34.918  55.499 72.055 1.00 43.19 ? 41   LYS A CD  1 
ATOM   26    C  CE  . LYS A  1 41  ? 36.025  56.539 72.153 1.00 45.00 ? 41   LYS A CE  1 
ATOM   27    N  NZ  . LYS A  1 41  ? 35.455  57.930 72.044 1.00 45.86 ? 41   LYS A NZ  1 
ATOM   28    N  N   . THR A  1 42  ? 34.147  50.750 70.643 1.00 31.22 ? 42   THR A N   1 
ATOM   29    C  CA  . THR A  1 42  ? 34.498  50.059 69.410 1.00 28.16 ? 42   THR A CA  1 
ATOM   30    C  C   . THR A  1 42  ? 34.543  51.085 68.291 1.00 26.56 ? 42   THR A C   1 
ATOM   31    O  O   . THR A  1 42  ? 34.172  52.246 68.486 1.00 25.93 ? 42   THR A O   1 
ATOM   32    C  CB  . THR A  1 42  ? 33.457  48.993 69.028 1.00 28.96 ? 42   THR A CB  1 
ATOM   33    O  OG1 . THR A  1 42  ? 32.219  49.635 68.686 1.00 27.94 ? 42   THR A OG1 1 
ATOM   34    C  CG2 . THR A  1 42  ? 33.239  48.012 70.189 1.00 27.61 ? 42   THR A CG2 1 
ATOM   35    N  N   . TYR A  1 43  ? 34.994  50.654 67.122 1.00 24.15 ? 43   TYR A N   1 
ATOM   36    C  CA  . TYR A  1 43  ? 35.080  51.537 65.974 1.00 22.67 ? 43   TYR A CA  1 
ATOM   37    C  C   . TYR A  1 43  ? 33.703  51.431 65.334 1.00 21.94 ? 43   TYR A C   1 
ATOM   38    O  O   . TYR A  1 43  ? 33.334  50.387 64.791 1.00 20.34 ? 43   TYR A O   1 
ATOM   39    C  CB  . TYR A  1 43  ? 36.170  51.049 65.024 1.00 22.93 ? 43   TYR A CB  1 
ATOM   40    C  CG  . TYR A  1 43  ? 36.415  51.952 63.843 1.00 22.29 ? 43   TYR A CG  1 
ATOM   41    C  CD1 . TYR A  1 43  ? 37.225  53.079 63.952 1.00 21.78 ? 43   TYR A CD1 1 
ATOM   42    C  CD2 . TYR A  1 43  ? 35.828  51.679 62.609 1.00 21.60 ? 43   TYR A CD2 1 
ATOM   43    C  CE1 . TYR A  1 43  ? 37.447  53.916 62.852 1.00 20.88 ? 43   TYR A CE1 1 
ATOM   44    C  CE2 . TYR A  1 43  ? 36.042  52.506 61.511 1.00 21.34 ? 43   TYR A CE2 1 
ATOM   45    C  CZ  . TYR A  1 43  ? 36.848  53.620 61.640 1.00 20.72 ? 43   TYR A CZ  1 
ATOM   46    O  OH  . TYR A  1 43  ? 37.026  54.437 60.556 1.00 21.22 ? 43   TYR A OH  1 
ATOM   47    N  N   . THR A  1 44  ? 32.961  52.529 65.409 1.00 19.86 ? 44   THR A N   1 
ATOM   48    C  CA  . THR A  1 44  ? 31.592  52.587 64.923 1.00 20.57 ? 44   THR A CA  1 
ATOM   49    C  C   . THR A  1 44  ? 31.407  53.100 63.494 1.00 20.85 ? 44   THR A C   1 
ATOM   50    O  O   . THR A  1 44  ? 32.360  53.553 62.844 1.00 20.75 ? 44   THR A O   1 
ATOM   51    C  CB  . THR A  1 44  ? 30.751  53.489 65.846 1.00 19.99 ? 44   THR A CB  1 
ATOM   52    O  OG1 . THR A  1 44  ? 31.133  54.853 65.628 1.00 19.33 ? 44   THR A OG1 1 
ATOM   53    C  CG2 . THR A  1 44  ? 30.968  53.113 67.337 1.00 18.75 ? 44   THR A CG2 1 
ATOM   54    N  N   . LEU A  1 45  ? 30.164  53.049 63.023 1.00 19.94 ? 45   LEU A N   1 
ATOM   55    C  CA  . LEU A  1 45  ? 29.858  53.518 61.686 1.00 20.50 ? 45   LEU A CA  1 
ATOM   56    C  C   . LEU A  1 45  ? 30.063  55.010 61.666 1.00 21.32 ? 45   LEU A C   1 
ATOM   57    O  O   . LEU A  1 45  ? 30.600  55.545 60.698 1.00 22.30 ? 45   LEU A O   1 
ATOM   58    C  CB  . LEU A  1 45  ? 28.417  53.180 61.294 1.00 20.52 ? 45   LEU A CB  1 
ATOM   59    C  CG  . LEU A  1 45  ? 28.000  53.692 59.905 1.00 21.18 ? 45   LEU A CG  1 
ATOM   60    C  CD1 . LEU A  1 45  ? 28.891  53.079 58.828 1.00 17.38 ? 45   LEU A CD1 1 
ATOM   61    C  CD2 . LEU A  1 45  ? 26.515  53.361 59.658 1.00 19.93 ? 45   LEU A CD2 1 
ATOM   62    N  N   . THR A  1 46  ? 29.657  55.695 62.734 1.00 21.63 ? 46   THR A N   1 
ATOM   63    C  CA  . THR A  1 46  ? 29.856  57.149 62.777 1.00 22.57 ? 46   THR A CA  1 
ATOM   64    C  C   . THR A  1 46  ? 31.356  57.481 62.736 1.00 22.93 ? 46   THR A C   1 
ATOM   65    O  O   . THR A  1 46  ? 31.762  58.451 62.106 1.00 23.68 ? 46   THR A O   1 
ATOM   66    C  CB  . THR A  1 46  ? 29.231  57.778 64.045 1.00 24.12 ? 46   THR A CB  1 
ATOM   67    O  OG1 . THR A  1 46  ? 27.809  57.603 64.018 1.00 25.14 ? 46   THR A OG1 1 
ATOM   68    C  CG2 . THR A  1 46  ? 29.527  59.265 64.105 1.00 24.70 ? 46   THR A CG2 1 
ATOM   69    N  N   . ASP A  1 47  ? 32.188  56.678 63.398 1.00 23.21 ? 47   ASP A N   1 
ATOM   70    C  CA  . ASP A  1 47  ? 33.628  56.946 63.381 1.00 23.59 ? 47   ASP A CA  1 
ATOM   71    C  C   . ASP A  1 47  ? 34.140  56.878 61.945 1.00 22.87 ? 47   ASP A C   1 
ATOM   72    O  O   . ASP A  1 47  ? 34.939  57.703 61.521 1.00 22.50 ? 47   ASP A O   1 
ATOM   73    C  CB  . ASP A  1 47  ? 34.380  55.931 64.250 1.00 23.76 ? 47   ASP A CB  1 
ATOM   74    C  CG  . ASP A  1 47  ? 34.127  56.136 65.744 1.00 26.00 ? 47   ASP A CG  1 
ATOM   75    O  OD1 . ASP A  1 47  ? 34.243  55.147 66.496 1.00 27.61 ? 47   ASP A OD1 1 
ATOM   76    O  OD2 . ASP A  1 47  ? 33.829  57.280 66.167 1.00 26.54 ? 47   ASP A OD2 1 
ATOM   77    N  N   . TYR A  1 48  ? 33.673  55.887 61.198 1.00 22.40 ? 48   TYR A N   1 
ATOM   78    C  CA  . TYR A  1 48  ? 34.096  55.743 59.823 1.00 22.12 ? 48   TYR A CA  1 
ATOM   79    C  C   . TYR A  1 48  ? 33.606  56.925 58.976 1.00 22.28 ? 48   TYR A C   1 
ATOM   80    O  O   . TYR A  1 48  ? 34.382  57.552 58.242 1.00 20.79 ? 48   TYR A O   1 
ATOM   81    C  CB  . TYR A  1 48  ? 33.561  54.436 59.247 1.00 21.98 ? 48   TYR A CB  1 
ATOM   82    C  CG  . TYR A  1 48  ? 33.735  54.350 57.751 1.00 23.34 ? 48   TYR A CG  1 
ATOM   83    C  CD1 . TYR A  1 48  ? 34.999  54.475 57.168 1.00 21.76 ? 48   TYR A CD1 1 
ATOM   84    C  CD2 . TYR A  1 48  ? 32.626  54.181 56.909 1.00 23.19 ? 48   TYR A CD2 1 
ATOM   85    C  CE1 . TYR A  1 48  ? 35.159  54.439 55.779 1.00 23.31 ? 48   TYR A CE1 1 
ATOM   86    C  CE2 . TYR A  1 48  ? 32.768  54.144 55.523 1.00 22.82 ? 48   TYR A CE2 1 
ATOM   87    C  CZ  . TYR A  1 48  ? 34.032  54.272 54.957 1.00 24.73 ? 48   TYR A CZ  1 
ATOM   88    O  OH  . TYR A  1 48  ? 34.154  54.232 53.577 1.00 24.57 ? 48   TYR A OH  1 
ATOM   89    N  N   . LEU A  1 49  ? 32.320  57.241 59.109 1.00 22.09 ? 49   LEU A N   1 
ATOM   90    C  CA  . LEU A  1 49  ? 31.696  58.320 58.345 1.00 23.53 ? 49   LEU A CA  1 
ATOM   91    C  C   . LEU A  1 49  ? 32.159  59.739 58.658 1.00 25.62 ? 49   LEU A C   1 
ATOM   92    O  O   . LEU A  1 49  ? 32.223  60.570 57.760 1.00 26.12 ? 49   LEU A O   1 
ATOM   93    C  CB  . LEU A  1 49  ? 30.174  58.251 58.507 1.00 22.22 ? 49   LEU A CB  1 
ATOM   94    C  CG  . LEU A  1 49  ? 29.494  56.980 58.001 1.00 21.09 ? 49   LEU A CG  1 
ATOM   95    C  CD1 . LEU A  1 49  ? 27.989  57.113 58.194 1.00 17.64 ? 49   LEU A CD1 1 
ATOM   96    C  CD2 . LEU A  1 49  ? 29.854  56.748 56.517 1.00 20.13 ? 49   LEU A CD2 1 
ATOM   97    N  N   . LYS A  1 50  ? 32.459  60.021 59.928 1.00 27.24 ? 50   LYS A N   1 
ATOM   98    C  CA  . LYS A  1 50  ? 32.905  61.352 60.330 1.00 28.26 ? 50   LYS A CA  1 
ATOM   99    C  C   . LYS A  1 50  ? 34.426  61.432 60.465 1.00 28.80 ? 50   LYS A C   1 
ATOM   100   O  O   . LYS A  1 50  ? 34.959  62.425 60.960 1.00 28.19 ? 50   LYS A O   1 
ATOM   101   C  CB  . LYS A  1 50  ? 32.270  61.757 61.665 1.00 29.96 ? 50   LYS A CB  1 
ATOM   102   C  CG  . LYS A  1 50  ? 30.741  61.676 61.692 1.00 33.27 ? 50   LYS A CG  1 
ATOM   103   C  CD  . LYS A  1 50  ? 30.108  62.514 60.598 1.00 35.37 ? 50   LYS A CD  1 
ATOM   104   C  CE  . LYS A  1 50  ? 28.600  62.653 60.821 1.00 39.11 ? 50   LYS A CE  1 
ATOM   105   N  NZ  . LYS A  1 50  ? 27.869  61.345 60.915 1.00 42.53 ? 50   LYS A NZ  1 
ATOM   106   N  N   . ASN A  1 51  ? 35.126  60.388 60.043 1.00 29.25 ? 51   ASN A N   1 
ATOM   107   C  CA  . ASN A  1 51  ? 36.589  60.381 60.116 1.00 30.55 ? 51   ASN A CA  1 
ATOM   108   C  C   . ASN A  1 51  ? 37.134  60.736 61.506 1.00 30.23 ? 51   ASN A C   1 
ATOM   109   O  O   . ASN A  1 51  ? 38.065  61.526 61.622 1.00 29.40 ? 51   ASN A O   1 
ATOM   110   C  CB  . ASN A  1 51  ? 37.160  61.362 59.091 1.00 33.00 ? 51   ASN A CB  1 
ATOM   111   C  CG  . ASN A  1 51  ? 36.716  61.049 57.667 1.00 36.46 ? 51   ASN A CG  1 
ATOM   112   O  OD1 . ASN A  1 51  ? 37.134  60.049 57.075 1.00 39.77 ? 51   ASN A OD1 1 
ATOM   113   N  ND2 . ASN A  1 51  ? 35.860  61.905 57.107 1.00 38.74 ? 51   ASN A ND2 1 
ATOM   114   N  N   . THR A  1 52  ? 36.558  60.156 62.556 1.00 30.11 ? 52   THR A N   1 
ATOM   115   C  CA  . THR A  1 52  ? 37.011  60.418 63.919 1.00 29.83 ? 52   THR A CA  1 
ATOM   116   C  C   . THR A  1 52  ? 38.475  60.054 64.127 1.00 30.63 ? 52   THR A C   1 
ATOM   117   O  O   . THR A  1 52  ? 39.180  60.726 64.879 1.00 30.17 ? 52   THR A O   1 
ATOM   118   C  CB  . THR A  1 52  ? 36.195  59.617 64.948 1.00 30.41 ? 52   THR A CB  1 
ATOM   119   O  OG1 . THR A  1 52  ? 34.813  59.969 64.836 1.00 33.74 ? 52   THR A OG1 1 
ATOM   120   C  CG2 . THR A  1 52  ? 36.654  59.935 66.372 1.00 30.01 ? 52   THR A CG2 1 
ATOM   121   N  N   . TYR A  1 53  ? 38.933  58.983 63.481 1.00 30.56 ? 53   TYR A N   1 
ATOM   122   C  CA  . TYR A  1 53  ? 40.321  58.546 63.637 1.00 31.82 ? 53   TYR A CA  1 
ATOM   123   C  C   . TYR A  1 53  ? 41.051  58.752 62.322 1.00 33.18 ? 53   TYR A C   1 
ATOM   124   O  O   . TYR A  1 53  ? 40.987  57.915 61.420 1.00 33.52 ? 53   TYR A O   1 
ATOM   125   C  CB  . TYR A  1 53  ? 40.356  57.077 64.041 1.00 31.96 ? 53   TYR A CB  1 
ATOM   126   C  CG  . TYR A  1 53  ? 39.657  56.825 65.355 1.00 33.09 ? 53   TYR A CG  1 
ATOM   127   C  CD1 . TYR A  1 53  ? 40.231  57.230 66.561 1.00 33.03 ? 53   TYR A CD1 1 
ATOM   128   C  CD2 . TYR A  1 53  ? 38.409  56.207 65.392 1.00 33.36 ? 53   TYR A CD2 1 
ATOM   129   C  CE1 . TYR A  1 53  ? 39.575  57.019 67.786 1.00 34.78 ? 53   TYR A CE1 1 
ATOM   130   C  CE2 . TYR A  1 53  ? 37.742  55.991 66.605 1.00 34.95 ? 53   TYR A CE2 1 
ATOM   131   C  CZ  . TYR A  1 53  ? 38.333  56.397 67.797 1.00 33.55 ? 53   TYR A CZ  1 
ATOM   132   O  OH  . TYR A  1 53  ? 37.694  56.150 68.983 1.00 33.09 ? 53   TYR A OH  1 
ATOM   133   N  N   . ARG A  1 54  ? 41.760  59.869 62.228 1.00 33.69 ? 54   ARG A N   1 
ATOM   134   C  CA  . ARG A  1 54  ? 42.443  60.222 61.004 1.00 34.52 ? 54   ARG A CA  1 
ATOM   135   C  C   . ARG A  1 54  ? 43.906  59.830 60.924 1.00 33.18 ? 54   ARG A C   1 
ATOM   136   O  O   . ARG A  1 54  ? 44.676  60.035 61.863 1.00 32.90 ? 54   ARG A O   1 
ATOM   137   C  CB  . ARG A  1 54  ? 42.304  61.726 60.784 1.00 38.15 ? 54   ARG A CB  1 
ATOM   138   C  CG  . ARG A  1 54  ? 42.382  62.164 59.321 1.00 43.92 ? 54   ARG A CG  1 
ATOM   139   C  CD  . ARG A  1 54  ? 42.290  63.696 59.204 1.00 47.78 ? 54   ARG A CD  1 
ATOM   140   N  NE  . ARG A  1 54  ? 41.228  64.261 60.045 1.00 50.84 ? 54   ARG A NE  1 
ATOM   141   C  CZ  . ARG A  1 54  ? 39.922  64.081 59.849 1.00 52.87 ? 54   ARG A CZ  1 
ATOM   142   N  NH1 . ARG A  1 54  ? 39.489  63.339 58.826 1.00 53.17 ? 54   ARG A NH1 1 
ATOM   143   N  NH2 . ARG A  1 54  ? 39.044  64.658 60.676 1.00 52.91 ? 54   ARG A NH2 1 
ATOM   144   N  N   . LEU A  1 55  ? 44.278  59.255 59.786 1.00 31.68 ? 55   LEU A N   1 
ATOM   145   C  CA  . LEU A  1 55  ? 45.656  58.869 59.534 1.00 30.92 ? 55   LEU A CA  1 
ATOM   146   C  C   . LEU A  1 55  ? 46.398  60.138 59.118 1.00 31.46 ? 55   LEU A C   1 
ATOM   147   O  O   . LEU A  1 55  ? 45.885  60.930 58.318 1.00 31.17 ? 55   LEU A O   1 
ATOM   148   C  CB  . LEU A  1 55  ? 45.727  57.869 58.388 1.00 30.38 ? 55   LEU A CB  1 
ATOM   149   C  CG  . LEU A  1 55  ? 45.175  56.467 58.619 1.00 30.90 ? 55   LEU A CG  1 
ATOM   150   C  CD1 . LEU A  1 55  ? 44.833  55.840 57.273 1.00 32.57 ? 55   LEU A CD1 1 
ATOM   151   C  CD2 . LEU A  1 55  ? 46.190  55.629 59.344 1.00 30.22 ? 55   LEU A CD2 1 
ATOM   152   N  N   . LYS A  1 56  ? 47.583  60.352 59.680 1.00 30.65 ? 56   LYS A N   1 
ATOM   153   C  CA  . LYS A  1 56  ? 48.383  61.505 59.300 1.00 29.95 ? 56   LYS A CA  1 
ATOM   154   C  C   . LYS A  1 56  ? 49.283  61.048 58.176 1.00 29.82 ? 56   LYS A C   1 
ATOM   155   O  O   . LYS A  1 56  ? 49.697  59.883 58.128 1.00 29.14 ? 56   LYS A O   1 
ATOM   156   C  CB  . LYS A  1 56  ? 49.244  62.000 60.450 1.00 29.84 ? 56   LYS A CB  1 
ATOM   157   C  CG  . LYS A  1 56  ? 48.520  62.922 61.392 1.00 31.91 ? 56   LYS A CG  1 
ATOM   158   C  CD  . LYS A  1 56  ? 49.416  63.271 62.579 1.00 34.42 ? 56   LYS A CD  1 
ATOM   159   C  CE  . LYS A  1 56  ? 48.786  64.312 63.501 1.00 34.74 ? 56   LYS A CE  1 
ATOM   160   N  NZ  . LYS A  1 56  ? 49.489  64.328 64.819 1.00 36.28 ? 56   LYS A NZ  1 
ATOM   161   N  N   . LEU A  1 57  ? 49.565  61.975 57.269 1.00 29.95 ? 57   LEU A N   1 
ATOM   162   C  CA  . LEU A  1 57  ? 50.409  61.718 56.113 1.00 30.44 ? 57   LEU A CA  1 
ATOM   163   C  C   . LEU A  1 57  ? 51.576  62.699 56.091 1.00 28.59 ? 57   LEU A C   1 
ATOM   164   O  O   . LEU A  1 57  ? 51.718  63.540 56.979 1.00 27.74 ? 57   LEU A O   1 
ATOM   165   C  CB  . LEU A  1 57  ? 49.592  61.891 54.823 1.00 33.56 ? 57   LEU A CB  1 
ATOM   166   C  CG  . LEU A  1 57  ? 48.577  60.810 54.408 1.00 34.96 ? 57   LEU A CG  1 
ATOM   167   C  CD1 . LEU A  1 57  ? 47.463  60.686 55.436 1.00 36.96 ? 57   LEU A CD1 1 
ATOM   168   C  CD2 . LEU A  1 57  ? 47.989  61.193 53.076 1.00 35.72 ? 57   LEU A CD2 1 
ATOM   169   N  N   . TYR A  1 58  ? 52.410  62.581 55.066 1.00 26.46 ? 58   TYR A N   1 
ATOM   170   C  CA  . TYR A  1 58  ? 53.540  63.474 54.901 1.00 25.02 ? 58   TYR A CA  1 
ATOM   171   C  C   . TYR A  1 58  ? 53.801  63.573 53.408 1.00 25.02 ? 58   TYR A C   1 
ATOM   172   O  O   . TYR A  1 58  ? 54.702  62.932 52.867 1.00 25.82 ? 58   TYR A O   1 
ATOM   173   C  CB  . TYR A  1 58  ? 54.777  62.947 55.635 1.00 23.85 ? 58   TYR A CB  1 
ATOM   174   C  CG  . TYR A  1 58  ? 55.811  64.022 55.899 1.00 22.37 ? 58   TYR A CG  1 
ATOM   175   C  CD1 . TYR A  1 58  ? 55.805  64.750 57.093 1.00 21.99 ? 58   TYR A CD1 1 
ATOM   176   C  CD2 . TYR A  1 58  ? 56.774  64.343 54.940 1.00 22.91 ? 58   TYR A CD2 1 
ATOM   177   C  CE1 . TYR A  1 58  ? 56.726  65.770 57.326 1.00 20.89 ? 58   TYR A CE1 1 
ATOM   178   C  CE2 . TYR A  1 58  ? 57.704  65.363 55.159 1.00 22.25 ? 58   TYR A CE2 1 
ATOM   179   C  CZ  . TYR A  1 58  ? 57.678  66.070 56.345 1.00 22.13 ? 58   TYR A CZ  1 
ATOM   180   O  OH  . TYR A  1 58  ? 58.602  67.062 56.559 1.00 20.26 ? 58   TYR A OH  1 
ATOM   181   N  N   . SER A  1 59  ? 52.983  64.379 52.749 1.00 25.00 ? 59   SER A N   1 
ATOM   182   C  CA  . SER A  1 59  ? 53.085  64.592 51.317 1.00 25.47 ? 59   SER A CA  1 
ATOM   183   C  C   . SER A  1 59  ? 54.067  65.715 51.032 1.00 25.53 ? 59   SER A C   1 
ATOM   184   O  O   . SER A  1 59  ? 53.749  66.884 51.220 1.00 25.53 ? 59   SER A O   1 
ATOM   185   C  CB  . SER A  1 59  ? 51.726  64.978 50.744 1.00 24.61 ? 59   SER A CB  1 
ATOM   186   O  OG  . SER A  1 59  ? 50.786  63.935 50.957 1.00 30.60 ? 59   SER A OG  1 
ATOM   187   N  N   . LEU A  1 60  ? 55.258  65.359 50.584 1.00 25.08 ? 60   LEU A N   1 
ATOM   188   C  CA  . LEU A  1 60  ? 56.250  66.360 50.265 1.00 26.47 ? 60   LEU A CA  1 
ATOM   189   C  C   . LEU A  1 60  ? 56.410  66.442 48.739 1.00 27.35 ? 60   LEU A C   1 
ATOM   190   O  O   . LEU A  1 60  ? 55.926  65.574 48.005 1.00 28.06 ? 60   LEU A O   1 
ATOM   191   C  CB  . LEU A  1 60  ? 57.575  65.994 50.938 1.00 24.20 ? 60   LEU A CB  1 
ATOM   192   C  CG  . LEU A  1 60  ? 58.178  64.636 50.558 1.00 23.05 ? 60   LEU A CG  1 
ATOM   193   C  CD1 . LEU A  1 60  ? 58.775  64.702 49.145 1.00 21.85 ? 60   LEU A CD1 1 
ATOM   194   C  CD2 . LEU A  1 60  ? 59.248  64.268 51.570 1.00 19.98 ? 60   LEU A CD2 1 
ATOM   195   N  N   . ARG A  1 61  ? 57.075  67.487 48.265 1.00 28.51 ? 61   ARG A N   1 
ATOM   196   C  CA  . ARG A  1 61  ? 57.313  67.652 46.832 1.00 29.06 ? 61   ARG A CA  1 
ATOM   197   C  C   . ARG A  1 61  ? 58.786  67.978 46.618 1.00 27.47 ? 61   ARG A C   1 
ATOM   198   O  O   . ARG A  1 61  ? 59.254  69.041 47.027 1.00 26.47 ? 61   ARG A O   1 
ATOM   199   C  CB  . ARG A  1 61  ? 56.482  68.803 46.263 1.00 32.26 ? 61   ARG A CB  1 
ATOM   200   C  CG  . ARG A  1 61  ? 54.988  68.769 46.583 1.00 38.24 ? 61   ARG A CG  1 
ATOM   201   C  CD  . ARG A  1 61  ? 54.294  70.000 45.966 1.00 42.53 ? 61   ARG A CD  1 
ATOM   202   N  NE  . ARG A  1 61  ? 52.868  70.078 46.287 1.00 45.24 ? 61   ARG A NE  1 
ATOM   203   C  CZ  . ARG A  1 61  ? 52.008  70.877 45.657 1.00 46.28 ? 61   ARG A CZ  1 
ATOM   204   N  NH1 . ARG A  1 61  ? 52.434  71.667 44.676 1.00 47.50 ? 61   ARG A NH1 1 
ATOM   205   N  NH2 . ARG A  1 61  ? 50.724  70.880 45.995 1.00 45.96 ? 61   ARG A NH2 1 
ATOM   206   N  N   . TRP A  1 62  ? 59.513  67.072 45.980 1.00 25.56 ? 62   TRP A N   1 
ATOM   207   C  CA  . TRP A  1 62  ? 60.923  67.309 45.714 1.00 27.09 ? 62   TRP A CA  1 
ATOM   208   C  C   . TRP A  1 62  ? 61.101  68.437 44.681 1.00 27.98 ? 62   TRP A C   1 
ATOM   209   O  O   . TRP A  1 62  ? 60.489  68.406 43.606 1.00 27.88 ? 62   TRP A O   1 
ATOM   210   C  CB  . TRP A  1 62  ? 61.582  66.026 45.196 1.00 25.06 ? 62   TRP A CB  1 
ATOM   211   C  CG  . TRP A  1 62  ? 61.732  64.948 46.236 1.00 25.11 ? 62   TRP A CG  1 
ATOM   212   C  CD1 . TRP A  1 62  ? 61.058  63.752 46.302 1.00 23.47 ? 62   TRP A CD1 1 
ATOM   213   C  CD2 . TRP A  1 62  ? 62.658  64.947 47.329 1.00 23.70 ? 62   TRP A CD2 1 
ATOM   214   N  NE1 . TRP A  1 62  ? 61.520  63.008 47.369 1.00 23.67 ? 62   TRP A NE1 1 
ATOM   215   C  CE2 . TRP A  1 62  ? 62.497  63.720 48.016 1.00 22.97 ? 62   TRP A CE2 1 
ATOM   216   C  CE3 . TRP A  1 62  ? 63.612  65.866 47.794 1.00 22.76 ? 62   TRP A CE3 1 
ATOM   217   C  CZ2 . TRP A  1 62  ? 63.257  63.388 49.147 1.00 23.48 ? 62   TRP A CZ2 1 
ATOM   218   C  CZ3 . TRP A  1 62  ? 64.369  65.535 48.918 1.00 23.83 ? 62   TRP A CZ3 1 
ATOM   219   C  CH2 . TRP A  1 62  ? 64.185  64.305 49.582 1.00 23.10 ? 62   TRP A CH2 1 
ATOM   220   N  N   . ILE A  1 63  ? 61.918  69.438 45.005 1.00 28.71 ? 63   ILE A N   1 
ATOM   221   C  CA  . ILE A  1 63  ? 62.159  70.539 44.060 1.00 29.34 ? 63   ILE A CA  1 
ATOM   222   C  C   . ILE A  1 63  ? 63.584  70.524 43.507 1.00 29.20 ? 63   ILE A C   1 
ATOM   223   O  O   . ILE A  1 63  ? 63.918  71.283 42.601 1.00 29.73 ? 63   ILE A O   1 
ATOM   224   C  CB  . ILE A  1 63  ? 61.910  71.924 44.701 1.00 29.98 ? 63   ILE A CB  1 
ATOM   225   C  CG1 . ILE A  1 63  ? 62.858  72.132 45.880 1.00 30.83 ? 63   ILE A CG1 1 
ATOM   226   C  CG2 . ILE A  1 63  ? 60.468  72.043 45.132 1.00 29.37 ? 63   ILE A CG2 1 
ATOM   227   C  CD1 . ILE A  1 63  ? 62.762  73.513 46.505 1.00 32.43 ? 63   ILE A CD1 1 
ATOM   228   N  N   . SER A  1 64  ? 64.425  69.665 44.069 1.00 28.55 ? 64   SER A N   1 
ATOM   229   C  CA  . SER A  1 64  ? 65.805  69.526 43.614 1.00 27.91 ? 64   SER A CA  1 
ATOM   230   C  C   . SER A  1 64  ? 66.312  68.193 44.146 1.00 28.37 ? 64   SER A C   1 
ATOM   231   O  O   . SER A  1 64  ? 65.528  67.347 44.586 1.00 27.36 ? 64   SER A O   1 
ATOM   232   C  CB  . SER A  1 64  ? 66.688  70.672 44.138 1.00 27.56 ? 64   SER A CB  1 
ATOM   233   O  OG  . SER A  1 64  ? 66.877  70.599 45.545 1.00 26.35 ? 64   SER A OG  1 
ATOM   234   N  N   . ASP A  1 65  ? 67.619  68.002 44.124 1.00 27.88 ? 65   ASP A N   1 
ATOM   235   C  CA  . ASP A  1 65  ? 68.179  66.762 44.617 1.00 28.56 ? 65   ASP A CA  1 
ATOM   236   C  C   . ASP A  1 65  ? 68.473  66.848 46.110 1.00 28.79 ? 65   ASP A C   1 
ATOM   237   O  O   . ASP A  1 65  ? 68.840  65.855 46.714 1.00 27.19 ? 65   ASP A O   1 
ATOM   238   C  CB  . ASP A  1 65  ? 69.470  66.448 43.866 1.00 29.29 ? 65   ASP A CB  1 
ATOM   239   C  CG  . ASP A  1 65  ? 69.888  64.992 44.013 1.00 32.35 ? 65   ASP A CG  1 
ATOM   240   O  OD1 . ASP A  1 65  ? 69.009  64.079 43.911 1.00 31.11 ? 65   ASP A OD1 1 
ATOM   241   O  OD2 . ASP A  1 65  ? 71.101  64.751 44.217 1.00 31.92 ? 65   ASP A OD2 1 
ATOM   242   N  N   . HIS A  1 66  ? 68.272  68.031 46.693 1.00 30.02 ? 66   HIS A N   1 
ATOM   243   C  CA  . HIS A  1 66  ? 68.585  68.272 48.104 1.00 31.62 ? 66   HIS A CA  1 
ATOM   244   C  C   . HIS A  1 66  ? 67.451  68.843 48.937 1.00 30.45 ? 66   HIS A C   1 
ATOM   245   O  O   . HIS A  1 66  ? 67.537  68.838 50.161 1.00 31.19 ? 66   HIS A O   1 
ATOM   246   C  CB  . HIS A  1 66  ? 69.761  69.261 48.215 1.00 35.02 ? 66   HIS A CB  1 
ATOM   247   C  CG  . HIS A  1 66  ? 70.821  69.055 47.180 1.00 38.34 ? 66   HIS A CG  1 
ATOM   248   N  ND1 . HIS A  1 66  ? 71.971  68.332 47.421 1.00 41.39 ? 66   HIS A ND1 1 
ATOM   249   C  CD2 . HIS A  1 66  ? 70.867  69.412 45.873 1.00 40.14 ? 66   HIS A CD2 1 
ATOM   250   C  CE1 . HIS A  1 66  ? 72.680  68.246 46.307 1.00 40.65 ? 66   HIS A CE1 1 
ATOM   251   N  NE2 . HIS A  1 66  ? 72.031  68.891 45.352 1.00 41.98 ? 66   HIS A NE2 1 
ATOM   252   N  N   . GLU A  1 67  ? 66.398  69.345 48.300 1.00 29.44 ? 67   GLU A N   1 
ATOM   253   C  CA  . GLU A  1 67  ? 65.307  69.957 49.060 1.00 28.41 ? 67   GLU A CA  1 
ATOM   254   C  C   . GLU A  1 67  ? 63.920  69.564 48.607 1.00 27.62 ? 67   GLU A C   1 
ATOM   255   O  O   . GLU A  1 67  ? 63.737  69.093 47.491 1.00 27.98 ? 67   GLU A O   1 
ATOM   256   C  CB  . GLU A  1 67  ? 65.407  71.486 48.981 1.00 28.33 ? 67   GLU A CB  1 
ATOM   257   C  CG  . GLU A  1 67  ? 66.736  72.062 49.415 1.00 31.27 ? 67   GLU A CG  1 
ATOM   258   C  CD  . GLU A  1 67  ? 66.665  73.576 49.624 1.00 34.22 ? 67   GLU A CD  1 
ATOM   259   O  OE1 . GLU A  1 67  ? 66.227  74.264 48.682 1.00 33.98 ? 67   GLU A OE1 1 
ATOM   260   O  OE2 . GLU A  1 67  ? 67.045  74.069 50.714 1.00 35.47 ? 67   GLU A OE2 1 
ATOM   261   N  N   . TYR A  1 68  ? 62.939  69.776 49.484 1.00 26.68 ? 68   TYR A N   1 
ATOM   262   C  CA  . TYR A  1 68  ? 61.547  69.502 49.167 1.00 25.69 ? 68   TYR A CA  1 
ATOM   263   C  C   . TYR A  1 68  ? 60.594  70.500 49.829 1.00 26.69 ? 68   TYR A C   1 
ATOM   264   O  O   . TYR A  1 68  ? 60.938  71.149 50.828 1.00 25.57 ? 68   TYR A O   1 
ATOM   265   C  CB  . TYR A  1 68  ? 61.187  68.065 49.556 1.00 24.57 ? 68   TYR A CB  1 
ATOM   266   C  CG  . TYR A  1 68  ? 61.158  67.754 51.031 1.00 23.00 ? 68   TYR A CG  1 
ATOM   267   C  CD1 . TYR A  1 68  ? 60.048  68.081 51.814 1.00 24.79 ? 68   TYR A CD1 1 
ATOM   268   C  CD2 . TYR A  1 68  ? 62.214  67.091 51.638 1.00 23.14 ? 68   TYR A CD2 1 
ATOM   269   C  CE1 . TYR A  1 68  ? 59.997  67.753 53.174 1.00 24.63 ? 68   TYR A CE1 1 
ATOM   270   C  CE2 . TYR A  1 68  ? 62.177  66.750 52.989 1.00 23.17 ? 68   TYR A CE2 1 
ATOM   271   C  CZ  . TYR A  1 68  ? 61.071  67.085 53.752 1.00 24.66 ? 68   TYR A CZ  1 
ATOM   272   O  OH  . TYR A  1 68  ? 61.051  66.775 55.092 1.00 23.69 ? 68   TYR A OH  1 
ATOM   273   N  N   . LEU A  1 69  ? 59.404  70.624 49.245 1.00 28.60 ? 69   LEU A N   1 
ATOM   274   C  CA  . LEU A  1 69  ? 58.355  71.519 49.741 1.00 30.26 ? 69   LEU A CA  1 
ATOM   275   C  C   . LEU A  1 69  ? 57.334  70.721 50.534 1.00 32.23 ? 69   LEU A C   1 
ATOM   276   O  O   . LEU A  1 69  ? 56.942  69.622 50.137 1.00 31.66 ? 69   LEU A O   1 
ATOM   277   C  CB  . LEU A  1 69  ? 57.634  72.203 48.584 1.00 29.58 ? 69   LEU A CB  1 
ATOM   278   C  CG  . LEU A  1 69  ? 58.527  73.079 47.712 1.00 29.95 ? 69   LEU A CG  1 
ATOM   279   C  CD1 . LEU A  1 69  ? 57.722  73.656 46.564 1.00 28.74 ? 69   LEU A CD1 1 
ATOM   280   C  CD2 . LEU A  1 69  ? 59.117  74.174 48.576 1.00 30.35 ? 69   LEU A CD2 1 
ATOM   281   N  N   . TYR A  1 70  ? 56.899  71.290 51.650 1.00 34.13 ? 70   TYR A N   1 
ATOM   282   C  CA  . TYR A  1 70  ? 55.933  70.638 52.515 1.00 36.10 ? 70   TYR A CA  1 
ATOM   283   C  C   . TYR A  1 70  ? 55.005  71.698 53.089 1.00 38.40 ? 70   TYR A C   1 
ATOM   284   O  O   . TYR A  1 70  ? 55.457  72.669 53.696 1.00 38.00 ? 70   TYR A O   1 
ATOM   285   C  CB  . TYR A  1 70  ? 56.666  69.923 53.655 1.00 35.49 ? 70   TYR A CB  1 
ATOM   286   C  CG  . TYR A  1 70  ? 55.772  69.170 54.608 1.00 35.21 ? 70   TYR A CG  1 
ATOM   287   C  CD1 . TYR A  1 70  ? 55.132  67.993 54.211 1.00 35.13 ? 70   TYR A CD1 1 
ATOM   288   C  CD2 . TYR A  1 70  ? 55.554  69.636 55.906 1.00 35.65 ? 70   TYR A CD2 1 
ATOM   289   C  CE1 . TYR A  1 70  ? 54.297  67.299 55.082 1.00 34.91 ? 70   TYR A CE1 1 
ATOM   290   C  CE2 . TYR A  1 70  ? 54.717  68.947 56.793 1.00 36.10 ? 70   TYR A CE2 1 
ATOM   291   C  CZ  . TYR A  1 70  ? 54.094  67.781 56.368 1.00 35.72 ? 70   TYR A CZ  1 
ATOM   292   O  OH  . TYR A  1 70  ? 53.266  67.098 57.222 1.00 37.67 ? 70   TYR A OH  1 
ATOM   293   N  N   . LYS A  1 71  ? 53.707  71.514 52.898 1.00 41.98 ? 71   LYS A N   1 
ATOM   294   C  CA  . LYS A  1 71  ? 52.732  72.467 53.420 1.00 45.96 ? 71   LYS A CA  1 
ATOM   295   C  C   . LYS A  1 71  ? 52.387  72.174 54.888 1.00 48.27 ? 71   LYS A C   1 
ATOM   296   O  O   . LYS A  1 71  ? 51.901  71.085 55.217 1.00 49.11 ? 71   LYS A O   1 
ATOM   297   C  CB  . LYS A  1 71  ? 51.460  72.433 52.569 1.00 45.65 ? 71   LYS A CB  1 
ATOM   298   C  CG  . LYS A  1 71  ? 50.359  73.329 53.101 1.00 47.60 ? 71   LYS A CG  1 
ATOM   299   C  CD  . LYS A  1 71  ? 49.191  73.412 52.127 1.00 48.81 ? 71   LYS A CD  1 
ATOM   300   C  CE  . LYS A  1 71  ? 48.133  74.401 52.627 1.00 50.83 ? 71   LYS A CE  1 
ATOM   301   N  NZ  . LYS A  1 71  ? 47.229  74.886 51.523 1.00 51.28 ? 71   LYS A NZ  1 
ATOM   302   N  N   . GLN A  1 72  ? 52.650  73.142 55.765 1.00 50.38 ? 72   GLN A N   1 
ATOM   303   C  CA  . GLN A  1 72  ? 52.359  72.996 57.189 1.00 52.59 ? 72   GLN A CA  1 
ATOM   304   C  C   . GLN A  1 72  ? 51.620  74.245 57.672 1.00 54.51 ? 72   GLN A C   1 
ATOM   305   O  O   . GLN A  1 72  ? 51.990  75.361 57.300 1.00 55.51 ? 72   GLN A O   1 
ATOM   306   C  CB  . GLN A  1 72  ? 53.659  72.833 57.988 1.00 52.44 ? 72   GLN A CB  1 
ATOM   307   C  CG  . GLN A  1 72  ? 53.454  72.142 59.332 1.00 53.89 ? 72   GLN A CG  1 
ATOM   308   C  CD  . GLN A  1 72  ? 54.754  71.867 60.071 1.00 55.34 ? 72   GLN A CD  1 
ATOM   309   O  OE1 . GLN A  1 72  ? 55.423  72.793 60.555 1.00 55.20 ? 72   GLN A OE1 1 
ATOM   310   N  NE2 . GLN A  1 72  ? 55.123  70.584 60.163 1.00 55.11 ? 72   GLN A NE2 1 
ATOM   311   N  N   . GLU A  1 73  ? 50.579  74.077 58.490 1.00 55.65 ? 73   GLU A N   1 
ATOM   312   C  CA  . GLU A  1 73  ? 49.837  75.238 58.997 1.00 56.63 ? 73   GLU A CA  1 
ATOM   313   C  C   . GLU A  1 73  ? 49.403  76.138 57.832 1.00 56.14 ? 73   GLU A C   1 
ATOM   314   O  O   . GLU A  1 73  ? 49.378  77.364 57.969 1.00 56.52 ? 73   GLU A O   1 
ATOM   315   C  CB  . GLU A  1 73  ? 50.732  76.058 59.952 1.00 58.45 ? 73   GLU A CB  1 
ATOM   316   C  CG  . GLU A  1 73  ? 51.085  75.376 61.284 1.00 60.84 ? 73   GLU A CG  1 
ATOM   317   C  CD  . GLU A  1 73  ? 52.277  76.030 62.003 1.00 62.31 ? 73   GLU A CD  1 
ATOM   318   O  OE1 . GLU A  1 73  ? 52.413  75.822 63.239 1.00 62.42 ? 73   GLU A OE1 1 
ATOM   319   O  OE2 . GLU A  1 73  ? 53.083  76.737 61.338 1.00 62.26 ? 73   GLU A OE2 1 
ATOM   320   N  N   . ASN A  1 74  ? 49.064  75.533 56.695 1.00 55.34 ? 74   ASN A N   1 
ATOM   321   C  CA  . ASN A  1 74  ? 48.663  76.289 55.507 1.00 54.52 ? 74   ASN A CA  1 
ATOM   322   C  C   . ASN A  1 74  ? 49.862  77.015 54.870 1.00 53.71 ? 74   ASN A C   1 
ATOM   323   O  O   . ASN A  1 74  ? 49.746  77.619 53.797 1.00 53.49 ? 74   ASN A O   1 
ATOM   324   C  CB  . ASN A  1 74  ? 47.559  77.305 55.846 1.00 55.25 ? 74   ASN A CB  1 
ATOM   325   C  CG  . ASN A  1 74  ? 46.162  76.744 55.624 1.00 56.63 ? 74   ASN A CG  1 
ATOM   326   O  OD1 . ASN A  1 74  ? 45.870  76.167 54.563 1.00 56.76 ? 74   ASN A OD1 1 
ATOM   327   N  ND2 . ASN A  1 74  ? 45.283  76.922 56.617 1.00 56.63 ? 74   ASN A ND2 1 
ATOM   328   N  N   . ASN A  1 75  ? 51.013  76.951 55.541 1.00 52.14 ? 75   ASN A N   1 
ATOM   329   C  CA  . ASN A  1 75  ? 52.244  77.569 55.045 1.00 50.19 ? 75   ASN A CA  1 
ATOM   330   C  C   . ASN A  1 75  ? 53.086  76.571 54.253 1.00 48.47 ? 75   ASN A C   1 
ATOM   331   O  O   . ASN A  1 75  ? 53.059  75.365 54.516 1.00 48.66 ? 75   ASN A O   1 
ATOM   332   C  CB  . ASN A  1 75  ? 53.073  78.086 56.212 1.00 50.91 ? 75   ASN A CB  1 
ATOM   333   C  CG  . ASN A  1 75  ? 52.396  79.210 56.932 1.00 52.92 ? 75   ASN A CG  1 
ATOM   334   O  OD1 . ASN A  1 75  ? 52.416  80.361 56.477 1.00 53.40 ? 75   ASN A OD1 1 
ATOM   335   N  ND2 . ASN A  1 75  ? 51.769  78.892 58.063 1.00 53.68 ? 75   ASN A ND2 1 
ATOM   336   N  N   . ILE A  1 76  ? 53.839  77.074 53.285 1.00 45.71 ? 76   ILE A N   1 
ATOM   337   C  CA  . ILE A  1 76  ? 54.689  76.208 52.485 1.00 42.90 ? 76   ILE A CA  1 
ATOM   338   C  C   . ILE A  1 76  ? 56.116  76.399 52.943 1.00 41.79 ? 76   ILE A C   1 
ATOM   339   O  O   . ILE A  1 76  ? 56.668  77.509 52.868 1.00 42.48 ? 76   ILE A O   1 
ATOM   340   C  CB  . ILE A  1 76  ? 54.567  76.531 50.986 1.00 42.86 ? 76   ILE A CB  1 
ATOM   341   C  CG1 . ILE A  1 76  ? 53.153  76.167 50.513 1.00 41.80 ? 76   ILE A CG1 1 
ATOM   342   C  CG2 . ILE A  1 76  ? 55.615  75.753 50.189 1.00 41.73 ? 76   ILE A CG2 1 
ATOM   343   C  CD1 . ILE A  1 76  ? 52.784  76.721 49.158 1.00 43.39 ? 76   ILE A CD1 1 
ATOM   344   N  N   . LEU A  1 77  ? 56.707  75.314 53.440 1.00 38.50 ? 77   LEU A N   1 
ATOM   345   C  CA  . LEU A  1 77  ? 58.078  75.346 53.930 1.00 36.07 ? 77   LEU A CA  1 
ATOM   346   C  C   . LEU A  1 77  ? 59.003  74.587 52.978 1.00 34.82 ? 77   LEU A C   1 
ATOM   347   O  O   . LEU A  1 77  ? 58.560  73.710 52.227 1.00 34.32 ? 77   LEU A O   1 
ATOM   348   C  CB  . LEU A  1 77  ? 58.139  74.709 55.326 1.00 35.48 ? 77   LEU A CB  1 
ATOM   349   C  CG  . LEU A  1 77  ? 57.175  75.257 56.395 1.00 35.56 ? 77   LEU A CG  1 
ATOM   350   C  CD1 . LEU A  1 77  ? 57.045  74.267 57.536 1.00 35.53 ? 77   LEU A CD1 1 
ATOM   351   C  CD2 . LEU A  1 77  ? 57.680  76.581 56.915 1.00 35.16 ? 77   LEU A CD2 1 
ATOM   352   N  N   . VAL A  1 78  ? 60.281  74.947 52.992 1.00 33.19 ? 78   VAL A N   1 
ATOM   353   C  CA  . VAL A  1 78  ? 61.269  74.265 52.172 1.00 32.40 ? 78   VAL A CA  1 
ATOM   354   C  C   . VAL A  1 78  ? 62.200  73.554 53.147 1.00 31.05 ? 78   VAL A C   1 
ATOM   355   O  O   . VAL A  1 78  ? 62.710  74.161 54.091 1.00 29.80 ? 78   VAL A O   1 
ATOM   356   C  CB  . VAL A  1 78  ? 62.084  75.239 51.278 1.00 32.82 ? 78   VAL A CB  1 
ATOM   357   C  CG1 . VAL A  1 78  ? 62.631  76.393 52.101 1.00 33.60 ? 78   VAL A CG1 1 
ATOM   358   C  CG2 . VAL A  1 78  ? 63.230  74.491 50.632 1.00 32.58 ? 78   VAL A CG2 1 
ATOM   359   N  N   . PHE A  1 79  ? 62.397  72.261 52.928 1.00 29.26 ? 79   PHE A N   1 
ATOM   360   C  CA  . PHE A  1 79  ? 63.239  71.469 53.806 1.00 26.93 ? 79   PHE A CA  1 
ATOM   361   C  C   . PHE A  1 79  ? 64.506  71.042 53.104 1.00 27.84 ? 79   PHE A C   1 
ATOM   362   O  O   . PHE A  1 79  ? 64.507  70.758 51.910 1.00 28.15 ? 79   PHE A O   1 
ATOM   363   C  CB  . PHE A  1 79  ? 62.513  70.195 54.253 1.00 25.89 ? 79   PHE A CB  1 
ATOM   364   C  CG  . PHE A  1 79  ? 61.463  70.415 55.317 1.00 25.81 ? 79   PHE A CG  1 
ATOM   365   C  CD1 . PHE A  1 79  ? 61.729  70.095 56.645 1.00 25.18 ? 79   PHE A CD1 1 
ATOM   366   C  CD2 . PHE A  1 79  ? 60.207  70.922 54.989 1.00 23.08 ? 79   PHE A CD2 1 
ATOM   367   C  CE1 . PHE A  1 79  ? 60.765  70.273 57.633 1.00 24.49 ? 79   PHE A CE1 1 
ATOM   368   C  CE2 . PHE A  1 79  ? 59.238  71.102 55.967 1.00 25.48 ? 79   PHE A CE2 1 
ATOM   369   C  CZ  . PHE A  1 79  ? 59.518  70.777 57.296 1.00 25.10 ? 79   PHE A CZ  1 
ATOM   370   N  N   . ASN A  1 80  ? 65.578  70.978 53.883 1.00 26.94 ? 80   ASN A N   1 
ATOM   371   C  CA  . ASN A  1 80  ? 66.866  70.533 53.430 1.00 27.13 ? 80   ASN A CA  1 
ATOM   372   C  C   . ASN A  1 80  ? 66.859  69.069 53.890 1.00 27.62 ? 80   ASN A C   1 
ATOM   373   O  O   . ASN A  1 80  ? 66.742  68.800 55.078 1.00 27.44 ? 80   ASN A O   1 
ATOM   374   C  CB  . ASN A  1 80  ? 67.940  71.332 54.147 1.00 26.89 ? 80   ASN A CB  1 
ATOM   375   C  CG  . ASN A  1 80  ? 69.317  70.771 53.937 1.00 26.14 ? 80   ASN A CG  1 
ATOM   376   O  OD1 . ASN A  1 80  ? 69.642  69.689 54.424 1.00 28.31 ? 80   ASN A OD1 1 
ATOM   377   N  ND2 . ASN A  1 80  ? 70.145  71.506 53.219 1.00 26.96 ? 80   ASN A ND2 1 
ATOM   378   N  N   . ALA A  1 81  ? 66.976  68.130 52.957 1.00 27.61 ? 81   ALA A N   1 
ATOM   379   C  CA  . ALA A  1 81  ? 66.929  66.704 53.296 1.00 28.12 ? 81   ALA A CA  1 
ATOM   380   C  C   . ALA A  1 81  ? 68.052  66.210 54.203 1.00 28.55 ? 81   ALA A C   1 
ATOM   381   O  O   . ALA A  1 81  ? 67.842  65.387 55.108 1.00 27.00 ? 81   ALA A O   1 
ATOM   382   C  CB  . ALA A  1 81  ? 66.895  65.862 51.998 1.00 26.89 ? 81   ALA A CB  1 
ATOM   383   N  N   . GLU A  1 82  ? 69.255  66.700 53.955 1.00 29.01 ? 82   GLU A N   1 
ATOM   384   C  CA  . GLU A  1 82  ? 70.391  66.266 54.736 1.00 31.39 ? 82   GLU A CA  1 
ATOM   385   C  C   . GLU A  1 82  ? 70.269  66.549 56.236 1.00 31.05 ? 82   GLU A C   1 
ATOM   386   O  O   . GLU A  1 82  ? 70.510  65.672 57.060 1.00 29.19 ? 82   GLU A O   1 
ATOM   387   C  CB  . GLU A  1 82  ? 71.657  66.927 54.195 1.00 34.50 ? 82   GLU A CB  1 
ATOM   388   C  CG  . GLU A  1 82  ? 72.871  66.775 55.084 1.00 39.35 ? 82   GLU A CG  1 
ATOM   389   C  CD  . GLU A  1 82  ? 73.620  65.480 54.868 1.00 43.51 ? 82   GLU A CD  1 
ATOM   390   O  OE1 . GLU A  1 82  ? 73.010  64.381 54.954 1.00 45.43 ? 82   GLU A OE1 1 
ATOM   391   O  OE2 . GLU A  1 82  ? 74.848  65.564 54.615 1.00 47.24 ? 82   GLU A OE2 1 
ATOM   392   N  N   . TYR A  1 83  ? 69.882  67.766 56.590 1.00 31.33 ? 83   TYR A N   1 
ATOM   393   C  CA  . TYR A  1 83  ? 69.818  68.128 58.002 1.00 32.57 ? 83   TYR A CA  1 
ATOM   394   C  C   . TYR A  1 83  ? 68.438  68.240 58.628 1.00 31.73 ? 83   TYR A C   1 
ATOM   395   O  O   . TYR A  1 83  ? 68.306  68.246 59.851 1.00 30.77 ? 83   TYR A O   1 
ATOM   396   C  CB  . TYR A  1 83  ? 70.603  69.424 58.202 1.00 33.47 ? 83   TYR A CB  1 
ATOM   397   C  CG  . TYR A  1 83  ? 72.048  69.284 57.762 1.00 37.29 ? 83   TYR A CG  1 
ATOM   398   C  CD1 . TYR A  1 83  ? 72.562  70.056 56.708 1.00 38.84 ? 83   TYR A CD1 1 
ATOM   399   C  CD2 . TYR A  1 83  ? 72.905  68.385 58.399 1.00 38.43 ? 83   TYR A CD2 1 
ATOM   400   C  CE1 . TYR A  1 83  ? 73.895  69.936 56.310 1.00 40.17 ? 83   TYR A CE1 1 
ATOM   401   C  CE2 . TYR A  1 83  ? 74.242  68.258 58.011 1.00 40.07 ? 83   TYR A CE2 1 
ATOM   402   C  CZ  . TYR A  1 83  ? 74.732  69.033 56.975 1.00 41.66 ? 83   TYR A CZ  1 
ATOM   403   O  OH  . TYR A  1 83  ? 76.071  68.930 56.628 1.00 45.06 ? 83   TYR A OH  1 
ATOM   404   N  N   . GLY A  1 84  ? 67.418  68.322 57.785 1.00 31.01 ? 84   GLY A N   1 
ATOM   405   C  CA  . GLY A  1 84  ? 66.067  68.425 58.286 1.00 31.77 ? 84   GLY A CA  1 
ATOM   406   C  C   . GLY A  1 84  ? 65.623  69.841 58.570 1.00 32.20 ? 84   GLY A C   1 
ATOM   407   O  O   . GLY A  1 84  ? 64.437  70.053 58.835 1.00 32.12 ? 84   GLY A O   1 
ATOM   408   N  N   . ASN A  1 85  ? 66.550  70.804 58.516 1.00 33.07 ? 85   ASN A N   1 
ATOM   409   C  CA  . ASN A  1 85  ? 66.205  72.213 58.784 1.00 33.62 ? 85   ASN A CA  1 
ATOM   410   C  C   . ASN A  1 85  ? 65.336  72.765 57.668 1.00 33.54 ? 85   ASN A C   1 
ATOM   411   O  O   . ASN A  1 85  ? 65.417  72.314 56.526 1.00 32.87 ? 85   ASN A O   1 
ATOM   412   C  CB  . ASN A  1 85  ? 67.462  73.099 58.953 1.00 34.16 ? 85   ASN A CB  1 
ATOM   413   C  CG  . ASN A  1 85  ? 68.337  73.137 57.710 1.00 37.32 ? 85   ASN A CG  1 
ATOM   414   O  OD1 . ASN A  1 85  ? 68.967  72.140 57.357 1.00 37.05 ? 85   ASN A OD1 1 
ATOM   415   N  ND2 . ASN A  1 85  ? 68.387  74.291 57.046 1.00 40.82 ? 85   ASN A ND2 1 
ATOM   416   N  N   . SER A  1 86  ? 64.492  73.728 58.009 1.00 33.56 ? 86   SER A N   1 
ATOM   417   C  CA  . SER A  1 86  ? 63.606  74.317 57.027 1.00 35.19 ? 86   SER A CA  1 
ATOM   418   C  C   . SER A  1 86  ? 63.563  75.836 57.105 1.00 35.34 ? 86   SER A C   1 
ATOM   419   O  O   . SER A  1 86  ? 64.245  76.448 57.926 1.00 35.37 ? 86   SER A O   1 
ATOM   420   C  CB  . SER A  1 86  ? 62.185  73.768 57.186 1.00 35.36 ? 86   SER A CB  1 
ATOM   421   O  OG  . SER A  1 86  ? 61.631  74.120 58.448 1.00 37.45 ? 86   SER A OG  1 
ATOM   422   N  N   . SER A  1 87  ? 62.770  76.417 56.210 1.00 36.18 ? 87   SER A N   1 
ATOM   423   C  CA  . SER A  1 87  ? 62.547  77.862 56.117 1.00 37.14 ? 87   SER A CA  1 
ATOM   424   C  C   . SER A  1 87  ? 61.156  77.990 55.540 1.00 38.55 ? 87   SER A C   1 
ATOM   425   O  O   . SER A  1 87  ? 60.645  77.059 54.899 1.00 38.03 ? 87   SER A O   1 
ATOM   426   C  CB  . SER A  1 87  ? 63.526  78.549 55.154 1.00 35.93 ? 87   SER A CB  1 
ATOM   427   O  OG  . SER A  1 87  ? 64.845  78.619 55.686 1.00 36.92 ? 87   SER A OG  1 
ATOM   428   N  N   . VAL A  1 88  ? 60.531  79.135 55.770 1.00 39.38 ? 88   VAL A N   1 
ATOM   429   C  CA  . VAL A  1 88  ? 59.199  79.362 55.238 1.00 39.81 ? 88   VAL A CA  1 
ATOM   430   C  C   . VAL A  1 88  ? 59.426  79.732 53.789 1.00 40.69 ? 88   VAL A C   1 
ATOM   431   O  O   . VAL A  1 88  ? 60.349  80.486 53.483 1.00 40.98 ? 88   VAL A O   1 
ATOM   432   C  CB  . VAL A  1 88  ? 58.509  80.518 55.970 1.00 40.52 ? 88   VAL A CB  1 
ATOM   433   C  CG1 . VAL A  1 88  ? 57.085  80.696 55.451 1.00 39.99 ? 88   VAL A CG1 1 
ATOM   434   C  CG2 . VAL A  1 88  ? 58.514  80.238 57.480 1.00 40.65 ? 88   VAL A CG2 1 
ATOM   435   N  N   . PHE A  1 89  ? 58.615  79.181 52.894 1.00 40.44 ? 89   PHE A N   1 
ATOM   436   C  CA  . PHE A  1 89  ? 58.762  79.491 51.487 1.00 40.71 ? 89   PHE A CA  1 
ATOM   437   C  C   . PHE A  1 89  ? 57.625  80.418 51.044 1.00 42.67 ? 89   PHE A C   1 
ATOM   438   O  O   . PHE A  1 89  ? 57.814  81.288 50.188 1.00 42.59 ? 89   PHE A O   1 
ATOM   439   C  CB  . PHE A  1 89  ? 58.764  78.197 50.666 1.00 39.65 ? 89   PHE A CB  1 
ATOM   440   C  CG  . PHE A  1 89  ? 58.968  78.415 49.192 1.00 38.19 ? 89   PHE A CG  1 
ATOM   441   C  CD1 . PHE A  1 89  ? 57.911  78.810 48.377 1.00 37.27 ? 89   PHE A CD1 1 
ATOM   442   C  CD2 . PHE A  1 89  ? 60.228  78.261 48.628 1.00 37.94 ? 89   PHE A CD2 1 
ATOM   443   C  CE1 . PHE A  1 89  ? 58.108  79.055 47.018 1.00 38.06 ? 89   PHE A CE1 1 
ATOM   444   C  CE2 . PHE A  1 89  ? 60.440  78.502 47.268 1.00 38.28 ? 89   PHE A CE2 1 
ATOM   445   C  CZ  . PHE A  1 89  ? 59.379  78.900 46.462 1.00 37.73 ? 89   PHE A CZ  1 
ATOM   446   N  N   . LEU A  1 90  ? 56.448  80.239 51.642 1.00 43.99 ? 90   LEU A N   1 
ATOM   447   C  CA  . LEU A  1 90  ? 55.291  81.059 51.303 1.00 45.96 ? 90   LEU A CA  1 
ATOM   448   C  C   . LEU A  1 90  ? 54.339  81.188 52.488 1.00 47.26 ? 90   LEU A C   1 
ATOM   449   O  O   . LEU A  1 90  ? 53.883  80.185 53.051 1.00 46.44 ? 90   LEU A O   1 
ATOM   450   C  CB  . LEU A  1 90  ? 54.542  80.454 50.115 1.00 46.76 ? 90   LEU A CB  1 
ATOM   451   C  CG  . LEU A  1 90  ? 53.457  81.332 49.511 1.00 47.66 ? 90   LEU A CG  1 
ATOM   452   C  CD1 . LEU A  1 90  ? 54.106  82.388 48.631 1.00 47.92 ? 90   LEU A CD1 1 
ATOM   453   C  CD2 . LEU A  1 90  ? 52.507  80.478 48.699 1.00 48.59 ? 90   LEU A CD2 1 
ATOM   454   N  N   . GLU A  1 91  ? 54.036  82.435 52.844 1.00 49.07 ? 91   GLU A N   1 
ATOM   455   C  CA  . GLU A  1 91  ? 53.152  82.750 53.955 1.00 50.10 ? 91   GLU A CA  1 
ATOM   456   C  C   . GLU A  1 91  ? 51.736  82.309 53.692 1.00 50.49 ? 91   GLU A C   1 
ATOM   457   O  O   . GLU A  1 91  ? 51.187  82.535 52.605 1.00 49.50 ? 91   GLU A O   1 
ATOM   458   C  CB  . GLU A  1 91  ? 53.138  84.254 54.216 1.00 51.69 ? 91   GLU A CB  1 
ATOM   459   C  CG  . GLU A  1 91  ? 54.499  84.846 54.493 1.00 53.82 ? 91   GLU A CG  1 
ATOM   460   C  CD  . GLU A  1 91  ? 55.195  84.147 55.635 1.00 55.27 ? 91   GLU A CD  1 
ATOM   461   O  OE1 . GLU A  1 91  ? 54.568  83.990 56.707 1.00 55.58 ? 91   GLU A OE1 1 
ATOM   462   O  OE2 . GLU A  1 91  ? 56.374  83.761 55.465 1.00 57.13 ? 91   GLU A OE2 1 
ATOM   463   N  N   . ASN A  1 92  ? 51.139  81.694 54.707 1.00 51.69 ? 92   ASN A N   1 
ATOM   464   C  CA  . ASN A  1 92  ? 49.755  81.219 54.632 1.00 53.31 ? 92   ASN A CA  1 
ATOM   465   C  C   . ASN A  1 92  ? 48.820  82.425 54.694 1.00 52.81 ? 92   ASN A C   1 
ATOM   466   O  O   . ASN A  1 92  ? 47.605  82.266 54.779 1.00 53.70 ? 92   ASN A O   1 
ATOM   467   C  CB  . ASN A  1 92  ? 49.453  80.298 55.821 1.00 55.12 ? 92   ASN A CB  1 
ATOM   468   C  CG  . ASN A  1 92  ? 49.489  81.045 57.156 1.00 57.44 ? 92   ASN A CG  1 
ATOM   469   O  OD1 . ASN A  1 92  ? 50.524  81.609 57.534 1.00 58.88 ? 92   ASN A OD1 1 
ATOM   470   N  ND2 . ASN A  1 92  ? 48.358  81.083 57.857 1.00 58.94 ? 92   ASN A ND2 1 
ATOM   471   N  N   . SER A  1 93  ? 49.392  83.626 54.667 1.00 51.99 ? 93   SER A N   1 
ATOM   472   C  CA  . SER A  1 93  ? 48.596  84.846 54.737 1.00 51.34 ? 93   SER A CA  1 
ATOM   473   C  C   . SER A  1 93  ? 48.839  85.739 53.536 1.00 50.60 ? 93   SER A C   1 
ATOM   474   O  O   . SER A  1 93  ? 48.122  86.712 53.339 1.00 50.67 ? 93   SER A O   1 
ATOM   475   C  CB  . SER A  1 93  ? 48.949  85.631 55.993 1.00 51.37 ? 93   SER A CB  1 
ATOM   476   O  OG  . SER A  1 93  ? 50.242  86.204 55.852 1.00 51.85 ? 93   SER A OG  1 
ATOM   477   N  N   . THR A  1 94  ? 49.854  85.406 52.744 1.00 50.14 ? 94   THR A N   1 
ATOM   478   C  CA  . THR A  1 94  ? 50.207  86.188 51.561 1.00 49.34 ? 94   THR A CA  1 
ATOM   479   C  C   . THR A  1 94  ? 48.999  86.515 50.688 1.00 49.11 ? 94   THR A C   1 
ATOM   480   O  O   . THR A  1 94  ? 48.931  87.604 50.110 1.00 49.46 ? 94   THR A O   1 
ATOM   481   C  CB  . THR A  1 94  ? 51.248  85.459 50.671 1.00 49.29 ? 94   THR A CB  1 
ATOM   482   O  OG1 . THR A  1 94  ? 52.372  85.056 51.463 1.00 50.09 ? 94   THR A OG1 1 
ATOM   483   C  CG2 . THR A  1 94  ? 51.734  86.380 49.563 1.00 47.86 ? 94   THR A CG2 1 
ATOM   484   N  N   . PHE A  1 95  ? 48.050  85.587 50.588 1.00 48.34 ? 95   PHE A N   1 
ATOM   485   C  CA  . PHE A  1 95  ? 46.867  85.820 49.758 1.00 48.28 ? 95   PHE A CA  1 
ATOM   486   C  C   . PHE A  1 95  ? 45.582  86.046 50.540 1.00 49.24 ? 95   PHE A C   1 
ATOM   487   O  O   . PHE A  1 95  ? 44.494  85.701 50.072 1.00 49.59 ? 95   PHE A O   1 
ATOM   488   C  CB  . PHE A  1 95  ? 46.676  84.652 48.792 1.00 46.66 ? 95   PHE A CB  1 
ATOM   489   C  CG  . PHE A  1 95  ? 47.895  84.360 47.973 1.00 45.19 ? 95   PHE A CG  1 
ATOM   490   C  CD1 . PHE A  1 95  ? 48.352  85.275 47.029 1.00 44.27 ? 95   PHE A CD1 1 
ATOM   491   C  CD2 . PHE A  1 95  ? 48.624  83.193 48.185 1.00 44.49 ? 95   PHE A CD2 1 
ATOM   492   C  CE1 . PHE A  1 95  ? 49.524  85.033 46.315 1.00 44.23 ? 95   PHE A CE1 1 
ATOM   493   C  CE2 . PHE A  1 95  ? 49.792  82.940 47.481 1.00 43.43 ? 95   PHE A CE2 1 
ATOM   494   C  CZ  . PHE A  1 95  ? 50.244  83.861 46.542 1.00 44.03 ? 95   PHE A CZ  1 
ATOM   495   N  N   . ASP A  1 96  ? 45.693  86.636 51.726 1.00 50.50 ? 96   ASP A N   1 
ATOM   496   C  CA  . ASP A  1 96  ? 44.502  86.881 52.531 1.00 51.81 ? 96   ASP A CA  1 
ATOM   497   C  C   . ASP A  1 96  ? 43.456  87.725 51.811 1.00 51.88 ? 96   ASP A C   1 
ATOM   498   O  O   . ASP A  1 96  ? 42.261  87.571 52.063 1.00 52.43 ? 96   ASP A O   1 
ATOM   499   C  CB  . ASP A  1 96  ? 44.871  87.534 53.862 1.00 52.59 ? 96   ASP A CB  1 
ATOM   500   C  CG  . ASP A  1 96  ? 45.426  86.534 54.856 1.00 54.76 ? 96   ASP A CG  1 
ATOM   501   O  OD1 . ASP A  1 96  ? 45.003  85.353 54.809 1.00 55.68 ? 96   ASP A OD1 1 
ATOM   502   O  OD2 . ASP A  1 96  ? 46.264  86.923 55.701 1.00 56.25 ? 96   ASP A OD2 1 
ATOM   503   N  N   . GLU A  1 97  ? 43.886  88.613 50.918 1.00 51.76 ? 97   GLU A N   1 
ATOM   504   C  CA  . GLU A  1 97  ? 42.919  89.439 50.192 1.00 52.18 ? 97   GLU A CA  1 
ATOM   505   C  C   . GLU A  1 97  ? 42.768  89.005 48.745 1.00 51.28 ? 97   GLU A C   1 
ATOM   506   O  O   . GLU A  1 97  ? 42.367  89.803 47.891 1.00 51.46 ? 97   GLU A O   1 
ATOM   507   C  CB  . GLU A  1 97  ? 43.311  90.925 50.230 1.00 53.73 ? 97   GLU A CB  1 
ATOM   508   C  CG  . GLU A  1 97  ? 43.090  91.609 51.584 1.00 56.36 ? 97   GLU A CG  1 
ATOM   509   C  CD  . GLU A  1 97  ? 44.344  91.614 52.446 1.00 58.38 ? 97   GLU A CD  1 
ATOM   510   O  OE1 . GLU A  1 97  ? 44.251  91.984 53.642 1.00 59.02 ? 97   GLU A OE1 1 
ATOM   511   O  OE2 . GLU A  1 97  ? 45.429  91.254 51.922 1.00 59.93 ? 97   GLU A OE2 1 
ATOM   512   N  N   . PHE A  1 98  ? 43.080  87.740 48.467 1.00 50.31 ? 98   PHE A N   1 
ATOM   513   C  CA  . PHE A  1 98  ? 42.981  87.231 47.105 1.00 48.27 ? 98   PHE A CA  1 
ATOM   514   C  C   . PHE A  1 98  ? 41.533  87.213 46.616 1.00 47.83 ? 98   PHE A C   1 
ATOM   515   O  O   . PHE A  1 98  ? 41.271  87.339 45.418 1.00 48.11 ? 98   PHE A O   1 
ATOM   516   C  CB  . PHE A  1 98  ? 43.603  85.839 47.016 1.00 47.55 ? 98   PHE A CB  1 
ATOM   517   C  CG  . PHE A  1 98  ? 43.633  85.286 45.624 1.00 46.83 ? 98   PHE A CG  1 
ATOM   518   C  CD1 . PHE A  1 98  ? 44.224  86.005 44.595 1.00 46.53 ? 98   PHE A CD1 1 
ATOM   519   C  CD2 . PHE A  1 98  ? 43.054  84.051 45.338 1.00 46.24 ? 98   PHE A CD2 1 
ATOM   520   C  CE1 . PHE A  1 98  ? 44.233  85.505 43.291 1.00 46.93 ? 98   PHE A CE1 1 
ATOM   521   C  CE2 . PHE A  1 98  ? 43.058  83.542 44.042 1.00 45.57 ? 98   PHE A CE2 1 
ATOM   522   C  CZ  . PHE A  1 98  ? 43.649  84.269 43.017 1.00 45.78 ? 98   PHE A CZ  1 
ATOM   523   N  N   . GLY A  1 99  ? 40.591  87.055 47.540 1.00 47.19 ? 99   GLY A N   1 
ATOM   524   C  CA  . GLY A  1 99  ? 39.187  87.074 47.160 1.00 47.28 ? 99   GLY A CA  1 
ATOM   525   C  C   . GLY A  1 99  ? 38.648  85.793 46.558 1.00 46.86 ? 99   GLY A C   1 
ATOM   526   O  O   . GLY A  1 99  ? 37.438  85.630 46.377 1.00 47.85 ? 99   GLY A O   1 
ATOM   527   N  N   . HIS A  1 100 ? 39.544  84.881 46.226 1.00 45.86 ? 100  HIS A N   1 
ATOM   528   C  CA  . HIS A  1 100 ? 39.126  83.608 45.669 1.00 44.75 ? 100  HIS A CA  1 
ATOM   529   C  C   . HIS A  1 100 ? 39.622  82.481 46.538 1.00 43.55 ? 100  HIS A C   1 
ATOM   530   O  O   . HIS A  1 100 ? 40.694  82.566 47.138 1.00 43.03 ? 100  HIS A O   1 
ATOM   531   C  CB  . HIS A  1 100 ? 39.688  83.431 44.275 1.00 44.72 ? 100  HIS A CB  1 
ATOM   532   C  CG  . HIS A  1 100 ? 39.055  84.324 43.266 1.00 45.17 ? 100  HIS A CG  1 
ATOM   533   N  ND1 . HIS A  1 100 ? 37.749  84.167 42.859 1.00 46.06 ? 100  HIS A ND1 1 
ATOM   534   C  CD2 . HIS A  1 100 ? 39.548  85.378 42.575 1.00 44.37 ? 100  HIS A CD2 1 
ATOM   535   C  CE1 . HIS A  1 100 ? 37.463  85.088 41.953 1.00 45.45 ? 100  HIS A CE1 1 
ATOM   536   N  NE2 . HIS A  1 100 ? 38.537  85.833 41.764 1.00 44.43 ? 100  HIS A NE2 1 
ATOM   537   N  N   . SER A  1 101 ? 38.837  81.421 46.616 1.00 43.09 ? 101  SER A N   1 
ATOM   538   C  CA  . SER A  1 101 ? 39.263  80.276 47.401 1.00 43.04 ? 101  SER A CA  1 
ATOM   539   C  C   . SER A  1 101 ? 40.270  79.494 46.540 1.00 41.88 ? 101  SER A C   1 
ATOM   540   O  O   . SER A  1 101 ? 39.925  79.003 45.465 1.00 41.25 ? 101  SER A O   1 
ATOM   541   C  CB  . SER A  1 101 ? 38.055  79.404 47.752 1.00 42.61 ? 101  SER A CB  1 
ATOM   542   O  OG  . SER A  1 101 ? 38.368  78.581 48.862 1.00 43.40 ? 101  SER A OG  1 
ATOM   543   N  N   . ILE A  1 102 ? 41.516  79.413 47.001 1.00 40.90 ? 102  ILE A N   1 
ATOM   544   C  CA  . ILE A  1 102 ? 42.554  78.703 46.267 1.00 40.78 ? 102  ILE A CA  1 
ATOM   545   C  C   . ILE A  1 102 ? 42.400  77.188 46.432 1.00 40.22 ? 102  ILE A C   1 
ATOM   546   O  O   . ILE A  1 102 ? 42.468  76.663 47.542 1.00 39.69 ? 102  ILE A O   1 
ATOM   547   C  CB  . ILE A  1 102 ? 43.957  79.092 46.762 1.00 41.69 ? 102  ILE A CB  1 
ATOM   548   C  CG1 . ILE A  1 102 ? 44.086  80.611 46.859 1.00 42.10 ? 102  ILE A CG1 1 
ATOM   549   C  CG2 . ILE A  1 102 ? 45.010  78.553 45.803 1.00 40.77 ? 102  ILE A CG2 1 
ATOM   550   C  CD1 . ILE A  1 102 ? 45.267  81.040 47.704 1.00 42.55 ? 102  ILE A CD1 1 
ATOM   551   N  N   . ASN A  1 103 ? 42.199  76.488 45.327 1.00 40.39 ? 103  ASN A N   1 
ATOM   552   C  CA  . ASN A  1 103 ? 42.034  75.039 45.384 1.00 40.82 ? 103  ASN A CA  1 
ATOM   553   C  C   . ASN A  1 103 ? 43.379  74.357 45.573 1.00 40.07 ? 103  ASN A C   1 
ATOM   554   O  O   . ASN A  1 103 ? 43.509  73.448 46.380 1.00 40.29 ? 103  ASN A O   1 
ATOM   555   C  CB  . ASN A  1 103 ? 41.382  74.514 44.098 1.00 41.24 ? 103  ASN A CB  1 
ATOM   556   C  CG  . ASN A  1 103 ? 41.016  73.042 44.193 1.00 42.63 ? 103  ASN A CG  1 
ATOM   557   O  OD1 . ASN A  1 103 ? 40.124  72.665 44.956 1.00 44.84 ? 103  ASN A OD1 1 
ATOM   558   N  ND2 . ASN A  1 103 ? 41.709  72.200 43.430 1.00 42.19 ? 103  ASN A ND2 1 
ATOM   559   N  N   . ASP A  1 104 ? 44.384  74.809 44.833 1.00 39.70 ? 104  ASP A N   1 
ATOM   560   C  CA  . ASP A  1 104 ? 45.715  74.213 44.912 1.00 38.51 ? 104  ASP A CA  1 
ATOM   561   C  C   . ASP A  1 104 ? 46.729  75.213 44.371 1.00 38.22 ? 104  ASP A C   1 
ATOM   562   O  O   . ASP A  1 104 ? 46.366  76.299 43.908 1.00 37.08 ? 104  ASP A O   1 
ATOM   563   C  CB  . ASP A  1 104 ? 45.748  72.927 44.081 1.00 39.56 ? 104  ASP A CB  1 
ATOM   564   C  CG  . ASP A  1 104 ? 46.921  72.011 44.438 1.00 40.76 ? 104  ASP A CG  1 
ATOM   565   O  OD1 . ASP A  1 104 ? 47.670  72.281 45.411 1.00 40.66 ? 104  ASP A OD1 1 
ATOM   566   O  OD2 . ASP A  1 104 ? 47.083  70.995 43.736 1.00 40.57 ? 104  ASP A OD2 1 
ATOM   567   N  N   . TYR A  1 105 ? 47.999  74.838 44.418 1.00 38.10 ? 105  TYR A N   1 
ATOM   568   C  CA  . TYR A  1 105 ? 49.060  75.715 43.956 1.00 38.55 ? 105  TYR A CA  1 
ATOM   569   C  C   . TYR A  1 105 ? 50.133  74.895 43.284 1.00 38.40 ? 105  TYR A C   1 
ATOM   570   O  O   . TYR A  1 105 ? 50.215  73.683 43.466 1.00 39.09 ? 105  TYR A O   1 
ATOM   571   C  CB  . TYR A  1 105 ? 49.711  76.437 45.126 1.00 40.59 ? 105  TYR A CB  1 
ATOM   572   C  CG  . TYR A  1 105 ? 50.508  75.494 45.995 1.00 43.86 ? 105  TYR A CG  1 
ATOM   573   C  CD1 . TYR A  1 105 ? 49.885  74.721 46.981 1.00 45.75 ? 105  TYR A CD1 1 
ATOM   574   C  CD2 . TYR A  1 105 ? 51.887  75.348 45.818 1.00 45.28 ? 105  TYR A CD2 1 
ATOM   575   C  CE1 . TYR A  1 105 ? 50.623  73.827 47.778 1.00 46.84 ? 105  TYR A CE1 1 
ATOM   576   C  CE2 . TYR A  1 105 ? 52.636  74.455 46.604 1.00 46.87 ? 105  TYR A CE2 1 
ATOM   577   C  CZ  . TYR A  1 105 ? 51.993  73.703 47.585 1.00 47.50 ? 105  TYR A CZ  1 
ATOM   578   O  OH  . TYR A  1 105 ? 52.723  72.843 48.382 1.00 49.96 ? 105  TYR A OH  1 
ATOM   579   N  N   . SER A  1 106 ? 50.988  75.568 42.535 1.00 36.58 ? 106  SER A N   1 
ATOM   580   C  CA  . SER A  1 106 ? 52.058  74.875 41.861 1.00 34.90 ? 106  SER A CA  1 
ATOM   581   C  C   . SER A  1 106 ? 53.199  75.843 41.593 1.00 34.98 ? 106  SER A C   1 
ATOM   582   O  O   . SER A  1 106 ? 53.071  76.787 40.800 1.00 35.07 ? 106  SER A O   1 
ATOM   583   C  CB  . SER A  1 106 ? 51.550  74.280 40.552 1.00 32.76 ? 106  SER A CB  1 
ATOM   584   O  OG  . SER A  1 106 ? 52.639  73.767 39.820 1.00 31.72 ? 106  SER A OG  1 
ATOM   585   N  N   . ILE A  1 107 ? 54.321  75.603 42.254 1.00 33.89 ? 107  ILE A N   1 
ATOM   586   C  CA  . ILE A  1 107 ? 55.482  76.466 42.091 1.00 33.65 ? 107  ILE A CA  1 
ATOM   587   C  C   . ILE A  1 107 ? 56.313  76.060 40.872 1.00 32.85 ? 107  ILE A C   1 
ATOM   588   O  O   . ILE A  1 107 ? 56.507  74.868 40.600 1.00 32.19 ? 107  ILE A O   1 
ATOM   589   C  CB  . ILE A  1 107 ? 56.318  76.426 43.362 1.00 34.00 ? 107  ILE A CB  1 
ATOM   590   C  CG1 . ILE A  1 107 ? 55.473  77.001 44.504 1.00 34.85 ? 107  ILE A CG1 1 
ATOM   591   C  CG2 . ILE A  1 107 ? 57.605  77.214 43.176 1.00 34.63 ? 107  ILE A CG2 1 
ATOM   592   C  CD1 . ILE A  1 107 ? 55.833  76.470 45.865 1.00 36.06 ? 107  ILE A CD1 1 
ATOM   593   N  N   . SER A  1 108 ? 56.770  77.059 40.122 1.00 31.07 ? 108  SER A N   1 
ATOM   594   C  CA  . SER A  1 108 ? 57.572  76.814 38.938 1.00 30.27 ? 108  SER A CA  1 
ATOM   595   C  C   . SER A  1 108 ? 58.836  76.089 39.391 1.00 31.33 ? 108  SER A C   1 
ATOM   596   O  O   . SER A  1 108 ? 59.292  76.256 40.526 1.00 31.07 ? 108  SER A O   1 
ATOM   597   C  CB  . SER A  1 108 ? 57.924  78.135 38.246 1.00 28.75 ? 108  SER A CB  1 
ATOM   598   O  OG  . SER A  1 108 ? 58.664  78.976 39.118 1.00 27.71 ? 108  SER A OG  1 
ATOM   599   N  N   . PRO A  1 109 ? 59.427  75.279 38.502 1.00 31.74 ? 109  PRO A N   1 
ATOM   600   C  CA  . PRO A  1 109 ? 60.640  74.543 38.872 1.00 32.82 ? 109  PRO A CA  1 
ATOM   601   C  C   . PRO A  1 109 ? 61.752  75.437 39.402 1.00 33.88 ? 109  PRO A C   1 
ATOM   602   O  O   . PRO A  1 109 ? 62.497  75.026 40.289 1.00 34.63 ? 109  PRO A O   1 
ATOM   603   C  CB  . PRO A  1 109 ? 61.032  73.829 37.578 1.00 32.26 ? 109  PRO A CB  1 
ATOM   604   C  CG  . PRO A  1 109 ? 59.694  73.671 36.863 1.00 31.87 ? 109  PRO A CG  1 
ATOM   605   C  CD  . PRO A  1 109 ? 59.031  74.996 37.113 1.00 30.73 ? 109  PRO A CD  1 
ATOM   606   N  N   . ASP A  1 110 ? 61.873  76.658 38.882 1.00 33.81 ? 110  ASP A N   1 
ATOM   607   C  CA  . ASP A  1 110 ? 62.932  77.548 39.360 1.00 34.74 ? 110  ASP A CA  1 
ATOM   608   C  C   . ASP A  1 110 ? 62.565  78.330 40.630 1.00 35.44 ? 110  ASP A C   1 
ATOM   609   O  O   . ASP A  1 110 ? 63.330  79.167 41.093 1.00 36.34 ? 110  ASP A O   1 
ATOM   610   C  CB  . ASP A  1 110 ? 63.371  78.502 38.240 1.00 34.86 ? 110  ASP A CB  1 
ATOM   611   C  CG  . ASP A  1 110 ? 62.277  79.471 37.808 1.00 35.37 ? 110  ASP A CG  1 
ATOM   612   O  OD1 . ASP A  1 110 ? 62.372  79.988 36.672 1.00 34.76 ? 110  ASP A OD1 1 
ATOM   613   O  OD2 . ASP A  1 110 ? 61.339  79.729 38.592 1.00 35.19 ? 110  ASP A OD2 1 
ATOM   614   N  N   . GLY A  1 111 ? 61.400  78.035 41.198 1.00 36.10 ? 111  GLY A N   1 
ATOM   615   C  CA  . GLY A  1 111 ? 60.965  78.707 42.416 1.00 37.25 ? 111  GLY A CA  1 
ATOM   616   C  C   . GLY A  1 111 ? 60.610  80.180 42.272 1.00 38.33 ? 111  GLY A C   1 
ATOM   617   O  O   . GLY A  1 111 ? 60.300  80.843 43.261 1.00 38.07 ? 111  GLY A O   1 
ATOM   618   N  N   . GLN A  1 112 ? 60.636  80.688 41.043 1.00 38.43 ? 112  GLN A N   1 
ATOM   619   C  CA  . GLN A  1 112 ? 60.333  82.090 40.790 1.00 39.13 ? 112  GLN A CA  1 
ATOM   620   C  C   . GLN A  1 112 ? 58.857  82.473 40.755 1.00 39.19 ? 112  GLN A C   1 
ATOM   621   O  O   . GLN A  1 112 ? 58.492  83.614 41.082 1.00 39.79 ? 112  GLN A O   1 
ATOM   622   C  CB  . GLN A  1 112 ? 60.997  82.521 39.488 1.00 39.76 ? 112  GLN A CB  1 
ATOM   623   C  CG  . GLN A  1 112 ? 62.502  82.553 39.585 1.00 41.60 ? 112  GLN A CG  1 
ATOM   624   C  CD  . GLN A  1 112 ? 63.147  82.922 38.267 1.00 43.39 ? 112  GLN A CD  1 
ATOM   625   O  OE1 . GLN A  1 112 ? 62.559  83.656 37.465 1.00 43.89 ? 112  GLN A OE1 1 
ATOM   626   N  NE2 . GLN A  1 112 ? 64.367  82.432 38.039 1.00 43.09 ? 112  GLN A NE2 1 
ATOM   627   N  N   . PHE A  1 113 ? 58.005  81.529 40.368 1.00 38.21 ? 113  PHE A N   1 
ATOM   628   C  CA  . PHE A  1 113 ? 56.575  81.787 40.270 1.00 37.24 ? 113  PHE A CA  1 
ATOM   629   C  C   . PHE A  1 113 ? 55.717  80.723 40.940 1.00 37.54 ? 113  PHE A C   1 
ATOM   630   O  O   . PHE A  1 113 ? 56.172  79.617 41.215 1.00 37.92 ? 113  PHE A O   1 
ATOM   631   C  CB  . PHE A  1 113 ? 56.180  81.885 38.802 1.00 36.55 ? 113  PHE A CB  1 
ATOM   632   C  CG  . PHE A  1 113 ? 56.892  82.975 38.064 1.00 37.79 ? 113  PHE A CG  1 
ATOM   633   C  CD1 . PHE A  1 113 ? 56.530  84.313 38.247 1.00 38.30 ? 113  PHE A CD1 1 
ATOM   634   C  CD2 . PHE A  1 113 ? 57.931  82.674 37.196 1.00 37.44 ? 113  PHE A CD2 1 
ATOM   635   C  CE1 . PHE A  1 113 ? 57.199  85.338 37.574 1.00 38.42 ? 113  PHE A CE1 1 
ATOM   636   C  CE2 . PHE A  1 113 ? 58.613  83.691 36.512 1.00 38.82 ? 113  PHE A CE2 1 
ATOM   637   C  CZ  . PHE A  1 113 ? 58.242  85.024 36.704 1.00 38.41 ? 113  PHE A CZ  1 
ATOM   638   N  N   . ILE A  1 114 ? 54.471  81.072 41.217 1.00 36.57 ? 114  ILE A N   1 
ATOM   639   C  CA  . ILE A  1 114 ? 53.554  80.127 41.809 1.00 36.52 ? 114  ILE A CA  1 
ATOM   640   C  C   . ILE A  1 114 ? 52.224  80.269 41.086 1.00 36.68 ? 114  ILE A C   1 
ATOM   641   O  O   . ILE A  1 114 ? 51.726  81.371 40.878 1.00 36.84 ? 114  ILE A O   1 
ATOM   642   C  CB  . ILE A  1 114 ? 53.379  80.351 43.335 1.00 36.69 ? 114  ILE A CB  1 
ATOM   643   C  CG1 . ILE A  1 114 ? 52.398  79.308 43.895 1.00 35.56 ? 114  ILE A CG1 1 
ATOM   644   C  CG2 . ILE A  1 114 ? 52.887  81.756 43.613 1.00 35.73 ? 114  ILE A CG2 1 
ATOM   645   C  CD1 . ILE A  1 114 ? 52.401  79.215 45.409 1.00 34.85 ? 114  ILE A CD1 1 
ATOM   646   N  N   . LEU A  1 115 ? 51.674  79.139 40.673 1.00 36.70 ? 115  LEU A N   1 
ATOM   647   C  CA  . LEU A  1 115 ? 50.415  79.109 39.965 1.00 36.45 ? 115  LEU A CA  1 
ATOM   648   C  C   . LEU A  1 115 ? 49.319  78.891 40.997 1.00 36.18 ? 115  LEU A C   1 
ATOM   649   O  O   . LEU A  1 115 ? 49.360  77.924 41.753 1.00 37.07 ? 115  LEU A O   1 
ATOM   650   C  CB  . LEU A  1 115 ? 50.444  77.966 38.959 1.00 37.51 ? 115  LEU A CB  1 
ATOM   651   C  CG  . LEU A  1 115 ? 49.302  77.812 37.962 1.00 38.16 ? 115  LEU A CG  1 
ATOM   652   C  CD1 . LEU A  1 115 ? 49.296  78.958 36.976 1.00 38.29 ? 115  LEU A CD1 1 
ATOM   653   C  CD2 . LEU A  1 115 ? 49.498  76.500 37.229 1.00 38.66 ? 115  LEU A CD2 1 
ATOM   654   N  N   . LEU A  1 116 ? 48.351  79.795 41.038 1.00 35.58 ? 116  LEU A N   1 
ATOM   655   C  CA  . LEU A  1 116 ? 47.249  79.694 41.990 1.00 35.03 ? 116  LEU A CA  1 
ATOM   656   C  C   . LEU A  1 116 ? 45.991  79.191 41.275 1.00 34.41 ? 116  LEU A C   1 
ATOM   657   O  O   . LEU A  1 116 ? 45.477  79.840 40.363 1.00 33.92 ? 116  LEU A O   1 
ATOM   658   C  CB  . LEU A  1 116 ? 46.992  81.063 42.644 1.00 34.77 ? 116  LEU A CB  1 
ATOM   659   C  CG  . LEU A  1 116 ? 48.147  81.733 43.407 1.00 35.70 ? 116  LEU A CG  1 
ATOM   660   C  CD1 . LEU A  1 116 ? 47.622  82.946 44.192 1.00 35.75 ? 116  LEU A CD1 1 
ATOM   661   C  CD2 . LEU A  1 116 ? 48.775  80.732 44.372 1.00 34.94 ? 116  LEU A CD2 1 
ATOM   662   N  N   . GLU A  1 117 ? 45.494  78.033 41.714 1.00 34.01 ? 117  GLU A N   1 
ATOM   663   C  CA  . GLU A  1 117 ? 44.313  77.391 41.128 1.00 32.43 ? 117  GLU A CA  1 
ATOM   664   C  C   . GLU A  1 117 ? 43.037  77.661 41.939 1.00 32.81 ? 117  GLU A C   1 
ATOM   665   O  O   . GLU A  1 117 ? 43.030  77.534 43.173 1.00 32.19 ? 117  GLU A O   1 
ATOM   666   C  CB  . GLU A  1 117 ? 44.582  75.872 41.031 1.00 32.66 ? 117  GLU A CB  1 
ATOM   667   C  CG  . GLU A  1 117 ? 43.487  74.998 40.394 1.00 32.04 ? 117  GLU A CG  1 
ATOM   668   C  CD  . GLU A  1 117 ? 43.957  73.540 40.178 1.00 32.68 ? 117  GLU A CD  1 
ATOM   669   O  OE1 . GLU A  1 117 ? 44.595  73.245 39.141 1.00 30.22 ? 117  GLU A OE1 1 
ATOM   670   O  OE2 . GLU A  1 117 ? 43.707  72.698 41.065 1.00 33.23 ? 117  GLU A OE2 1 
ATOM   671   N  N   . TYR A  1 118 ? 41.965  78.063 41.255 1.00 31.46 ? 118  TYR A N   1 
ATOM   672   C  CA  . TYR A  1 118 ? 40.701  78.314 41.929 1.00 31.34 ? 118  TYR A CA  1 
ATOM   673   C  C   . TYR A  1 118 ? 39.546  78.109 40.966 1.00 31.06 ? 118  TYR A C   1 
ATOM   674   O  O   . TYR A  1 118 ? 39.767  77.864 39.784 1.00 31.43 ? 118  TYR A O   1 
ATOM   675   C  CB  . TYR A  1 118 ? 40.658  79.721 42.556 1.00 32.38 ? 118  TYR A CB  1 
ATOM   676   C  CG  . TYR A  1 118 ? 40.815  80.871 41.593 1.00 33.38 ? 118  TYR A CG  1 
ATOM   677   C  CD1 . TYR A  1 118 ? 42.058  81.175 41.033 1.00 33.56 ? 118  TYR A CD1 1 
ATOM   678   C  CD2 . TYR A  1 118 ? 39.715  81.647 41.225 1.00 34.14 ? 118  TYR A CD2 1 
ATOM   679   C  CE1 . TYR A  1 118 ? 42.200  82.225 40.129 1.00 34.17 ? 118  TYR A CE1 1 
ATOM   680   C  CE2 . TYR A  1 118 ? 39.844  82.696 40.321 1.00 34.62 ? 118  TYR A CE2 1 
ATOM   681   C  CZ  . TYR A  1 118 ? 41.089  82.979 39.780 1.00 34.66 ? 118  TYR A CZ  1 
ATOM   682   O  OH  . TYR A  1 118 ? 41.221  84.019 38.901 1.00 35.96 ? 118  TYR A OH  1 
ATOM   683   N  N   . ASN A  1 119 ? 38.318  78.193 41.469 1.00 31.19 ? 119  ASN A N   1 
ATOM   684   C  CA  . ASN A  1 119 ? 37.122  77.968 40.647 1.00 31.55 ? 119  ASN A CA  1 
ATOM   685   C  C   . ASN A  1 119 ? 37.158  76.556 40.063 1.00 30.93 ? 119  ASN A C   1 
ATOM   686   O  O   . ASN A  1 119 ? 36.712  76.321 38.936 1.00 30.32 ? 119  ASN A O   1 
ATOM   687   C  CB  . ASN A  1 119 ? 37.018  78.978 39.494 1.00 32.99 ? 119  ASN A CB  1 
ATOM   688   C  CG  . ASN A  1 119 ? 36.561  80.349 39.954 1.00 35.31 ? 119  ASN A CG  1 
ATOM   689   O  OD1 . ASN A  1 119 ? 36.017  80.501 41.050 1.00 34.75 ? 119  ASN A OD1 1 
ATOM   690   N  ND2 . ASN A  1 119 ? 36.767  81.356 39.108 1.00 35.90 ? 119  ASN A ND2 1 
ATOM   691   N  N   . TYR A  1 120 ? 37.697  75.627 40.847 1.00 29.38 ? 120  TYR A N   1 
ATOM   692   C  CA  . TYR A  1 120 ? 37.790  74.232 40.456 1.00 28.57 ? 120  TYR A CA  1 
ATOM   693   C  C   . TYR A  1 120 ? 36.421  73.613 40.174 1.00 27.81 ? 120  TYR A C   1 
ATOM   694   O  O   . TYR A  1 120 ? 35.505  73.709 40.992 1.00 27.74 ? 120  TYR A O   1 
ATOM   695   C  CB  . TYR A  1 120 ? 38.485  73.442 41.572 1.00 29.84 ? 120  TYR A CB  1 
ATOM   696   C  CG  . TYR A  1 120 ? 38.398  71.937 41.441 1.00 30.82 ? 120  TYR A CG  1 
ATOM   697   C  CD1 . TYR A  1 120 ? 39.411  71.207 40.838 1.00 30.88 ? 120  TYR A CD1 1 
ATOM   698   C  CD2 . TYR A  1 120 ? 37.295  71.242 41.943 1.00 32.51 ? 120  TYR A CD2 1 
ATOM   699   C  CE1 . TYR A  1 120 ? 39.336  69.820 40.740 1.00 32.06 ? 120  TYR A CE1 1 
ATOM   700   C  CE2 . TYR A  1 120 ? 37.208  69.863 41.851 1.00 33.15 ? 120  TYR A CE2 1 
ATOM   701   C  CZ  . TYR A  1 120 ? 38.234  69.158 41.248 1.00 32.51 ? 120  TYR A CZ  1 
ATOM   702   O  OH  . TYR A  1 120 ? 38.134  67.790 41.158 1.00 35.01 ? 120  TYR A OH  1 
ATOM   703   N  N   . VAL A  1 121 ? 36.279  72.982 39.015 1.00 26.60 ? 121  VAL A N   1 
ATOM   704   C  CA  . VAL A  1 121 ? 35.033  72.303 38.677 1.00 25.84 ? 121  VAL A CA  1 
ATOM   705   C  C   . VAL A  1 121 ? 35.432  70.933 38.134 1.00 26.19 ? 121  VAL A C   1 
ATOM   706   O  O   . VAL A  1 121 ? 35.982  70.820 37.034 1.00 25.61 ? 121  VAL A O   1 
ATOM   707   C  CB  . VAL A  1 121 ? 34.212  73.028 37.588 1.00 27.14 ? 121  VAL A CB  1 
ATOM   708   C  CG1 . VAL A  1 121 ? 32.903  72.241 37.349 1.00 24.95 ? 121  VAL A CG1 1 
ATOM   709   C  CG2 . VAL A  1 121 ? 33.896  74.492 38.016 1.00 25.79 ? 121  VAL A CG2 1 
ATOM   710   N  N   . LYS A  1 122 ? 35.156  69.896 38.918 1.00 24.42 ? 122  LYS A N   1 
ATOM   711   C  CA  . LYS A  1 122 ? 35.489  68.537 38.539 1.00 23.14 ? 122  LYS A CA  1 
ATOM   712   C  C   . LYS A  1 122 ? 34.751  68.022 37.308 1.00 23.32 ? 122  LYS A C   1 
ATOM   713   O  O   . LYS A  1 122 ? 33.571  68.326 37.099 1.00 22.62 ? 122  LYS A O   1 
ATOM   714   C  CB  . LYS A  1 122 ? 35.192  67.584 39.708 1.00 23.73 ? 122  LYS A CB  1 
ATOM   715   C  CG  . LYS A  1 122 ? 35.460  66.096 39.412 1.00 22.87 ? 122  LYS A CG  1 
ATOM   716   C  CD  . LYS A  1 122 ? 35.052  65.181 40.577 1.00 22.75 ? 122  LYS A CD  1 
ATOM   717   C  CE  . LYS A  1 122 ? 35.214  63.691 40.217 1.00 23.01 ? 122  LYS A CE  1 
ATOM   718   N  NZ  . LYS A  1 122 ? 34.339  63.265 39.083 1.00 23.54 ? 122  LYS A NZ  1 
ATOM   719   N  N   . GLN A  1 123 ? 35.453  67.257 36.477 1.00 22.14 ? 123  GLN A N   1 
ATOM   720   C  CA  . GLN A  1 123 ? 34.778  66.631 35.344 1.00 20.93 ? 123  GLN A CA  1 
ATOM   721   C  C   . GLN A  1 123 ? 34.750  65.112 35.599 1.00 19.60 ? 123  GLN A C   1 
ATOM   722   O  O   . GLN A  1 123 ? 33.901  64.651 36.360 1.00 18.57 ? 123  GLN A O   1 
ATOM   723   C  CB  . GLN A  1 123 ? 35.450  66.942 34.010 1.00 20.94 ? 123  GLN A CB  1 
ATOM   724   C  CG  . GLN A  1 123 ? 34.507  66.636 32.865 1.00 22.26 ? 123  GLN A CG  1 
ATOM   725   C  CD  . GLN A  1 123 ? 35.122  66.829 31.494 1.00 24.62 ? 123  GLN A CD  1 
ATOM   726   O  OE1 . GLN A  1 123 ? 34.418  66.869 30.496 1.00 25.46 ? 123  GLN A OE1 1 
ATOM   727   N  NE2 . GLN A  1 123 ? 36.437  66.935 31.441 1.00 27.65 ? 123  GLN A NE2 1 
ATOM   728   N  N   . TRP A  1 124 ? 35.661  64.343 34.999 1.00 17.64 ? 124  TRP A N   1 
ATOM   729   C  CA  . TRP A  1 124 ? 35.659  62.897 35.224 1.00 17.97 ? 124  TRP A CA  1 
ATOM   730   C  C   . TRP A  1 124 ? 36.591  62.482 36.363 1.00 18.90 ? 124  TRP A C   1 
ATOM   731   O  O   . TRP A  1 124 ? 36.726  63.207 37.353 1.00 19.90 ? 124  TRP A O   1 
ATOM   732   C  CB  . TRP A  1 124 ? 36.020  62.143 33.939 1.00 16.79 ? 124  TRP A CB  1 
ATOM   733   C  CG  . TRP A  1 124 ? 35.221  62.615 32.759 1.00 17.15 ? 124  TRP A CG  1 
ATOM   734   C  CD1 . TRP A  1 124 ? 35.708  62.951 31.520 1.00 17.44 ? 124  TRP A CD1 1 
ATOM   735   C  CD2 . TRP A  1 124 ? 33.803  62.859 32.709 1.00 15.70 ? 124  TRP A CD2 1 
ATOM   736   N  NE1 . TRP A  1 124 ? 34.684  63.394 30.710 1.00 17.42 ? 124  TRP A NE1 1 
ATOM   737   C  CE2 . TRP A  1 124 ? 33.508  63.353 31.412 1.00 16.15 ? 124  TRP A CE2 1 
ATOM   738   C  CE3 . TRP A  1 124 ? 32.755  62.715 33.634 1.00 15.87 ? 124  TRP A CE3 1 
ATOM   739   C  CZ2 . TRP A  1 124 ? 32.209  63.709 31.016 1.00 14.95 ? 124  TRP A CZ2 1 
ATOM   740   C  CZ3 . TRP A  1 124 ? 31.444  63.072 33.235 1.00 13.92 ? 124  TRP A CZ3 1 
ATOM   741   C  CH2 . TRP A  1 124 ? 31.193  63.564 31.936 1.00 14.61 ? 124  TRP A CH2 1 
ATOM   742   N  N   . ARG A  1 125 ? 37.214  61.313 36.254 1.00 19.41 ? 125  ARG A N   1 
ATOM   743   C  CA  . ARG A  1 125 ? 38.103  60.860 37.312 1.00 19.58 ? 125  ARG A CA  1 
ATOM   744   C  C   . ARG A  1 125 ? 39.323  61.763 37.511 1.00 20.33 ? 125  ARG A C   1 
ATOM   745   O  O   . ARG A  1 125 ? 39.707  62.048 38.644 1.00 20.61 ? 125  ARG A O   1 
ATOM   746   C  CB  . ARG A  1 125 ? 38.536  59.410 37.058 1.00 19.60 ? 125  ARG A CB  1 
ATOM   747   C  CG  . ARG A  1 125 ? 39.803  58.994 37.799 1.00 21.70 ? 125  ARG A CG  1 
ATOM   748   C  CD  . ARG A  1 125 ? 39.773  57.623 38.461 1.00 18.78 ? 125  ARG A CD  1 
ATOM   749   N  NE  . ARG A  1 125 ? 38.982  56.608 37.758 1.00 19.75 ? 125  ARG A NE  1 
ATOM   750   C  CZ  . ARG A  1 125 ? 38.399  55.589 38.391 1.00 17.72 ? 125  ARG A CZ  1 
ATOM   751   N  NH1 . ARG A  1 125 ? 38.541  55.478 39.706 1.00 17.75 ? 125  ARG A NH1 1 
ATOM   752   N  NH2 . ARG A  1 125 ? 37.649  54.720 37.738 1.00 15.23 ? 125  ARG A NH2 1 
ATOM   753   N  N   . HIS A  1 126 ? 39.932  62.220 36.426 1.00 19.60 ? 126  HIS A N   1 
ATOM   754   C  CA  . HIS A  1 126 ? 41.106  63.082 36.558 1.00 19.80 ? 126  HIS A CA  1 
ATOM   755   C  C   . HIS A  1 126 ? 40.890  64.505 36.010 1.00 18.83 ? 126  HIS A C   1 
ATOM   756   O  O   . HIS A  1 126 ? 41.510  65.447 36.476 1.00 18.25 ? 126  HIS A O   1 
ATOM   757   C  CB  . HIS A  1 126 ? 42.312  62.450 35.829 1.00 18.58 ? 126  HIS A CB  1 
ATOM   758   C  CG  . HIS A  1 126 ? 42.510  60.994 36.121 1.00 19.81 ? 126  HIS A CG  1 
ATOM   759   N  ND1 . HIS A  1 126 ? 42.942  60.528 37.345 1.00 20.37 ? 126  HIS A ND1 1 
ATOM   760   C  CD2 . HIS A  1 126 ? 42.303  59.899 35.348 1.00 18.39 ? 126  HIS A CD2 1 
ATOM   761   C  CE1 . HIS A  1 126 ? 42.990  59.206 37.315 1.00 20.28 ? 126  HIS A CE1 1 
ATOM   762   N  NE2 . HIS A  1 126 ? 42.606  58.802 36.117 1.00 21.53 ? 126  HIS A NE2 1 
ATOM   763   N  N   . SER A  1 127 ? 40.010  64.646 35.022 1.00 20.04 ? 127  SER A N   1 
ATOM   764   C  CA  . SER A  1 127 ? 39.758  65.940 34.389 1.00 20.27 ? 127  SER A CA  1 
ATOM   765   C  C   . SER A  1 127 ? 38.939  66.933 35.220 1.00 21.11 ? 127  SER A C   1 
ATOM   766   O  O   . SER A  1 127 ? 38.143  66.552 36.078 1.00 21.63 ? 127  SER A O   1 
ATOM   767   C  CB  . SER A  1 127 ? 39.080  65.737 33.034 1.00 19.70 ? 127  SER A CB  1 
ATOM   768   O  OG  . SER A  1 127 ? 37.839  65.066 33.161 1.00 17.45 ? 127  SER A OG  1 
ATOM   769   N  N   . TYR A  1 128 ? 39.168  68.210 34.948 1.00 21.23 ? 128  TYR A N   1 
ATOM   770   C  CA  . TYR A  1 128 ? 38.482  69.316 35.601 1.00 23.05 ? 128  TYR A CA  1 
ATOM   771   C  C   . TYR A  1 128 ? 38.911  70.614 34.929 1.00 24.76 ? 128  TYR A C   1 
ATOM   772   O  O   . TYR A  1 128 ? 39.899  70.639 34.184 1.00 25.61 ? 128  TYR A O   1 
ATOM   773   C  CB  . TYR A  1 128 ? 38.836  69.376 37.099 1.00 21.26 ? 128  TYR A CB  1 
ATOM   774   C  CG  . TYR A  1 128 ? 40.285  69.691 37.427 1.00 21.58 ? 128  TYR A CG  1 
ATOM   775   C  CD1 . TYR A  1 128 ? 40.775  71.002 37.385 1.00 22.47 ? 128  TYR A CD1 1 
ATOM   776   C  CD2 . TYR A  1 128 ? 41.172  68.674 37.811 1.00 21.36 ? 128  TYR A CD2 1 
ATOM   777   C  CE1 . TYR A  1 128 ? 42.107  71.291 37.724 1.00 20.90 ? 128  TYR A CE1 1 
ATOM   778   C  CE2 . TYR A  1 128 ? 42.503  68.952 38.151 1.00 21.14 ? 128  TYR A CE2 1 
ATOM   779   C  CZ  . TYR A  1 128 ? 42.963  70.264 38.109 1.00 22.21 ? 128  TYR A CZ  1 
ATOM   780   O  OH  . TYR A  1 128 ? 44.268  70.540 38.473 1.00 22.02 ? 128  TYR A OH  1 
ATOM   781   N  N   . THR A  1 129 ? 38.157  71.681 35.158 1.00 24.61 ? 129  THR A N   1 
ATOM   782   C  CA  . THR A  1 129 ? 38.554  72.980 34.632 1.00 26.72 ? 129  THR A CA  1 
ATOM   783   C  C   . THR A  1 129 ? 38.728  73.883 35.843 1.00 27.00 ? 129  THR A C   1 
ATOM   784   O  O   . THR A  1 129 ? 38.226  73.590 36.933 1.00 26.76 ? 129  THR A O   1 
ATOM   785   C  CB  . THR A  1 129 ? 37.503  73.617 33.701 1.00 27.36 ? 129  THR A CB  1 
ATOM   786   O  OG1 . THR A  1 129 ? 36.285  73.822 34.423 1.00 30.04 ? 129  THR A OG1 1 
ATOM   787   C  CG2 . THR A  1 129 ? 37.241  72.746 32.503 1.00 26.09 ? 129  THR A CG2 1 
ATOM   788   N  N   . ALA A  1 130 ? 39.453  74.975 35.657 1.00 27.10 ? 130  ALA A N   1 
ATOM   789   C  CA  . ALA A  1 130 ? 39.675  75.904 36.743 1.00 27.91 ? 130  ALA A CA  1 
ATOM   790   C  C   . ALA A  1 130 ? 40.191  77.225 36.211 1.00 29.72 ? 130  ALA A C   1 
ATOM   791   O  O   . ALA A  1 130 ? 40.486  77.365 35.014 1.00 29.60 ? 130  ALA A O   1 
ATOM   792   C  CB  . ALA A  1 130 ? 40.682  75.328 37.724 1.00 26.48 ? 130  ALA A CB  1 
ATOM   793   N  N   . SER A  1 131 ? 40.282  78.197 37.111 1.00 30.79 ? 131  SER A N   1 
ATOM   794   C  CA  . SER A  1 131 ? 40.808  79.508 36.772 1.00 32.56 ? 131  SER A CA  1 
ATOM   795   C  C   . SER A  1 131 ? 42.182  79.560 37.409 1.00 33.64 ? 131  SER A C   1 
ATOM   796   O  O   . SER A  1 131 ? 42.424  78.904 38.428 1.00 32.69 ? 131  SER A O   1 
ATOM   797   C  CB  . SER A  1 131 ? 39.921  80.599 37.349 1.00 32.91 ? 131  SER A CB  1 
ATOM   798   O  OG  . SER A  1 131 ? 38.645  80.542 36.737 1.00 34.17 ? 131  SER A OG  1 
ATOM   799   N  N   . TYR A  1 132 ? 43.087  80.332 36.813 1.00 35.00 ? 132  TYR A N   1 
ATOM   800   C  CA  . TYR A  1 132 ? 44.441  80.441 37.345 1.00 35.74 ? 132  TYR A CA  1 
ATOM   801   C  C   . TYR A  1 132 ? 44.968  81.874 37.399 1.00 37.04 ? 132  TYR A C   1 
ATOM   802   O  O   . TYR A  1 132 ? 44.544  82.739 36.636 1.00 37.77 ? 132  TYR A O   1 
ATOM   803   C  CB  . TYR A  1 132 ? 45.405  79.600 36.501 1.00 35.83 ? 132  TYR A CB  1 
ATOM   804   C  CG  . TYR A  1 132 ? 45.097  78.124 36.483 1.00 35.75 ? 132  TYR A CG  1 
ATOM   805   C  CD1 . TYR A  1 132 ? 44.188  77.590 35.576 1.00 34.90 ? 132  TYR A CD1 1 
ATOM   806   C  CD2 . TYR A  1 132 ? 45.677  77.268 37.419 1.00 35.73 ? 132  TYR A CD2 1 
ATOM   807   C  CE1 . TYR A  1 132 ? 43.857  76.236 35.604 1.00 34.88 ? 132  TYR A CE1 1 
ATOM   808   C  CE2 . TYR A  1 132 ? 45.355  75.920 37.457 1.00 35.65 ? 132  TYR A CE2 1 
ATOM   809   C  CZ  . TYR A  1 132 ? 44.444  75.410 36.553 1.00 35.00 ? 132  TYR A CZ  1 
ATOM   810   O  OH  . TYR A  1 132 ? 44.101  74.083 36.632 1.00 35.10 ? 132  TYR A OH  1 
ATOM   811   N  N   . ASP A  1 133 ? 45.902  82.101 38.312 1.00 37.41 ? 133  ASP A N   1 
ATOM   812   C  CA  . ASP A  1 133 ? 46.563  83.381 38.473 1.00 38.41 ? 133  ASP A CA  1 
ATOM   813   C  C   . ASP A  1 133 ? 48.004  83.018 38.778 1.00 38.68 ? 133  ASP A C   1 
ATOM   814   O  O   . ASP A  1 133 ? 48.266  81.978 39.393 1.00 37.47 ? 133  ASP A O   1 
ATOM   815   C  CB  . ASP A  1 133 ? 45.974  84.177 39.643 1.00 39.92 ? 133  ASP A CB  1 
ATOM   816   C  CG  . ASP A  1 133 ? 44.789  85.040 39.235 1.00 41.09 ? 133  ASP A CG  1 
ATOM   817   O  OD1 . ASP A  1 133 ? 44.010  85.434 40.127 1.00 43.17 ? 133  ASP A OD1 1 
ATOM   818   O  OD2 . ASP A  1 133 ? 44.639  85.337 38.034 1.00 42.32 ? 133  ASP A OD2 1 
ATOM   819   N  N   . ILE A  1 134 ? 48.939  83.853 38.329 1.00 38.28 ? 134  ILE A N   1 
ATOM   820   C  CA  . ILE A  1 134 ? 50.348  83.609 38.577 1.00 37.95 ? 134  ILE A CA  1 
ATOM   821   C  C   . ILE A  1 134 ? 50.885  84.723 39.453 1.00 38.88 ? 134  ILE A C   1 
ATOM   822   O  O   . ILE A  1 134 ? 50.767  85.900 39.115 1.00 38.67 ? 134  ILE A O   1 
ATOM   823   C  CB  . ILE A  1 134 ? 51.159  83.598 37.286 1.00 37.48 ? 134  ILE A CB  1 
ATOM   824   C  CG1 . ILE A  1 134 ? 50.568  82.589 36.307 1.00 35.89 ? 134  ILE A CG1 1 
ATOM   825   C  CG2 . ILE A  1 134 ? 52.625  83.313 37.617 1.00 36.85 ? 134  ILE A CG2 1 
ATOM   826   C  CD1 . ILE A  1 134 ? 51.155  82.679 34.924 1.00 35.99 ? 134  ILE A CD1 1 
ATOM   827   N  N   . TYR A  1 135 ? 51.482  84.336 40.573 1.00 39.42 ? 135  TYR A N   1 
ATOM   828   C  CA  . TYR A  1 135 ? 52.039  85.278 41.521 1.00 40.55 ? 135  TYR A CA  1 
ATOM   829   C  C   . TYR A  1 135 ? 53.566  85.264 41.420 1.00 41.82 ? 135  TYR A C   1 
ATOM   830   O  O   . TYR A  1 135 ? 54.193  84.200 41.479 1.00 41.28 ? 135  TYR A O   1 
ATOM   831   C  CB  . TYR A  1 135 ? 51.604  84.890 42.929 1.00 41.13 ? 135  TYR A CB  1 
ATOM   832   C  CG  . TYR A  1 135 ? 52.083  85.821 44.019 1.00 42.11 ? 135  TYR A CG  1 
ATOM   833   C  CD1 . TYR A  1 135 ? 51.424  87.019 44.285 1.00 42.09 ? 135  TYR A CD1 1 
ATOM   834   C  CD2 . TYR A  1 135 ? 53.192  85.487 44.799 1.00 42.94 ? 135  TYR A CD2 1 
ATOM   835   C  CE1 . TYR A  1 135 ? 51.858  87.862 45.312 1.00 43.20 ? 135  TYR A CE1 1 
ATOM   836   C  CE2 . TYR A  1 135 ? 53.636  86.316 45.819 1.00 43.82 ? 135  TYR A CE2 1 
ATOM   837   C  CZ  . TYR A  1 135 ? 52.967  87.504 46.074 1.00 44.06 ? 135  TYR A CZ  1 
ATOM   838   O  OH  . TYR A  1 135 ? 53.429  88.323 47.088 1.00 45.25 ? 135  TYR A OH  1 
ATOM   839   N  N   . ASP A  1 136 ? 54.160  86.445 41.248 1.00 42.39 ? 136  ASP A N   1 
ATOM   840   C  CA  . ASP A  1 136 ? 55.612  86.573 41.143 1.00 43.42 ? 136  ASP A CA  1 
ATOM   841   C  C   . ASP A  1 136 ? 56.200  86.560 42.558 1.00 44.59 ? 136  ASP A C   1 
ATOM   842   O  O   . ASP A  1 136 ? 55.895  87.437 43.367 1.00 45.39 ? 136  ASP A O   1 
ATOM   843   C  CB  . ASP A  1 136 ? 55.965  87.884 40.445 1.00 43.47 ? 136  ASP A CB  1 
ATOM   844   C  CG  . ASP A  1 136 ? 57.431  87.965 40.057 1.00 43.76 ? 136  ASP A CG  1 
ATOM   845   O  OD1 . ASP A  1 136 ? 58.308  87.737 40.930 1.00 42.58 ? 136  ASP A OD1 1 
ATOM   846   O  OD2 . ASP A  1 136 ? 57.701  88.266 38.873 1.00 43.38 ? 136  ASP A OD2 1 
ATOM   847   N  N   . LEU A  1 137 ? 57.037  85.572 42.858 1.00 45.16 ? 137  LEU A N   1 
ATOM   848   C  CA  . LEU A  1 137 ? 57.619  85.469 44.190 1.00 46.58 ? 137  LEU A CA  1 
ATOM   849   C  C   . LEU A  1 137 ? 58.760  86.454 44.412 1.00 47.82 ? 137  LEU A C   1 
ATOM   850   O  O   . LEU A  1 137 ? 58.968  86.930 45.525 1.00 48.80 ? 137  LEU A O   1 
ATOM   851   C  CB  . LEU A  1 137 ? 58.105  84.040 44.443 1.00 46.17 ? 137  LEU A CB  1 
ATOM   852   C  CG  . LEU A  1 137 ? 57.038  82.935 44.387 1.00 45.91 ? 137  LEU A CG  1 
ATOM   853   C  CD1 . LEU A  1 137 ? 57.721  81.575 44.278 1.00 46.92 ? 137  LEU A CD1 1 
ATOM   854   C  CD2 . LEU A  1 137 ? 56.149  82.995 45.622 1.00 46.84 ? 137  LEU A CD2 1 
ATOM   855   N  N   . ASN A  1 138 ? 59.493  86.774 43.352 1.00 49.22 ? 138  ASN A N   1 
ATOM   856   C  CA  . ASN A  1 138 ? 60.613  87.705 43.460 1.00 50.27 ? 138  ASN A CA  1 
ATOM   857   C  C   . ASN A  1 138 ? 60.103  89.103 43.798 1.00 50.16 ? 138  ASN A C   1 
ATOM   858   O  O   . ASN A  1 138 ? 60.517  89.709 44.788 1.00 51.01 ? 138  ASN A O   1 
ATOM   859   C  CB  . ASN A  1 138 ? 61.389  87.747 42.136 1.00 51.72 ? 138  ASN A CB  1 
ATOM   860   C  CG  . ASN A  1 138 ? 61.781  86.359 41.647 1.00 53.32 ? 138  ASN A CG  1 
ATOM   861   O  OD1 . ASN A  1 138 ? 62.454  85.600 42.365 1.00 53.63 ? 138  ASN A OD1 1 
ATOM   862   N  ND2 . ASN A  1 138 ? 61.361  86.015 40.420 1.00 53.08 ? 138  ASN A ND2 1 
ATOM   863   N  N   . LYS A  1 139 ? 59.193  89.606 42.972 1.00 49.71 ? 139  LYS A N   1 
ATOM   864   C  CA  . LYS A  1 139 ? 58.638  90.927 43.172 1.00 48.85 ? 139  LYS A CA  1 
ATOM   865   C  C   . LYS A  1 139 ? 57.390  90.870 44.053 1.00 49.59 ? 139  LYS A C   1 
ATOM   866   O  O   . LYS A  1 139 ? 56.619  91.842 44.112 1.00 49.55 ? 139  LYS A O   1 
ATOM   867   C  CB  . LYS A  1 139 ? 58.293  91.560 41.825 1.00 47.87 ? 139  LYS A CB  1 
ATOM   868   C  CG  . LYS A  1 139 ? 57.021  91.029 41.191 1.00 47.55 ? 139  LYS A CG  1 
ATOM   869   C  CD  . LYS A  1 139 ? 56.637  91.826 39.941 1.00 47.81 ? 139  LYS A CD  1 
ATOM   870   C  CE  . LYS A  1 139 ? 57.406  91.375 38.703 1.00 47.82 ? 139  LYS A CE  1 
ATOM   871   N  NZ  . LYS A  1 139 ? 58.894  91.397 38.889 1.00 49.22 ? 139  LYS A NZ  1 
ATOM   872   N  N   . ARG A  1 140 ? 57.199  89.743 44.741 1.00 49.34 ? 140  ARG A N   1 
ATOM   873   C  CA  . ARG A  1 140 ? 56.045  89.565 45.626 1.00 49.58 ? 140  ARG A CA  1 
ATOM   874   C  C   . ARG A  1 140 ? 54.814  90.245 45.038 1.00 48.76 ? 140  ARG A C   1 
ATOM   875   O  O   . ARG A  1 140 ? 54.137  91.020 45.721 1.00 48.85 ? 140  ARG A O   1 
ATOM   876   C  CB  . ARG A  1 140 ? 56.318  90.171 47.010 1.00 50.66 ? 140  ARG A CB  1 
ATOM   877   C  CG  . ARG A  1 140 ? 57.552  89.629 47.726 1.00 52.98 ? 140  ARG A CG  1 
ATOM   878   C  CD  . ARG A  1 140 ? 57.461  88.129 47.946 1.00 55.34 ? 140  ARG A CD  1 
ATOM   879   N  NE  . ARG A  1 140 ? 56.254  87.752 48.694 1.00 57.70 ? 140  ARG A NE  1 
ATOM   880   C  CZ  . ARG A  1 140 ? 56.017  86.527 49.165 1.00 58.12 ? 140  ARG A CZ  1 
ATOM   881   N  NH1 . ARG A  1 140 ? 56.909  85.553 48.965 1.00 58.06 ? 140  ARG A NH1 1 
ATOM   882   N  NH2 . ARG A  1 140 ? 54.898  86.279 49.842 1.00 57.27 ? 140  ARG A NH2 1 
ATOM   883   N  N   . GLN A  1 141 ? 54.520  89.962 43.776 1.00 47.57 ? 141  GLN A N   1 
ATOM   884   C  CA  . GLN A  1 141 ? 53.378  90.595 43.125 1.00 47.17 ? 141  GLN A CA  1 
ATOM   885   C  C   . GLN A  1 141 ? 52.597  89.643 42.229 1.00 45.64 ? 141  GLN A C   1 
ATOM   886   O  O   . GLN A  1 141 ? 53.153  88.722 41.644 1.00 45.69 ? 141  GLN A O   1 
ATOM   887   C  CB  . GLN A  1 141 ? 53.868  91.804 42.310 1.00 48.33 ? 141  GLN A CB  1 
ATOM   888   C  CG  . GLN A  1 141 ? 52.881  92.342 41.285 1.00 50.90 ? 141  GLN A CG  1 
ATOM   889   C  CD  . GLN A  1 141 ? 53.501  93.397 40.368 1.00 53.14 ? 141  GLN A CD  1 
ATOM   890   O  OE1 . GLN A  1 141 ? 53.779  94.528 40.791 1.00 53.86 ? 141  GLN A OE1 1 
ATOM   891   N  NE2 . GLN A  1 141 ? 53.727  93.024 39.107 1.00 52.39 ? 141  GLN A NE2 1 
ATOM   892   N  N   . LEU A  1 142 ? 51.298  89.888 42.132 1.00 44.77 ? 142  LEU A N   1 
ATOM   893   C  CA  . LEU A  1 142 ? 50.401  89.092 41.309 1.00 43.99 ? 142  LEU A CA  1 
ATOM   894   C  C   . LEU A  1 142 ? 50.448  89.633 39.883 1.00 43.36 ? 142  LEU A C   1 
ATOM   895   O  O   . LEU A  1 142 ? 50.384  90.849 39.669 1.00 43.78 ? 142  LEU A O   1 
ATOM   896   C  CB  . LEU A  1 142 ? 48.976  89.210 41.849 1.00 44.11 ? 142  LEU A CB  1 
ATOM   897   C  CG  . LEU A  1 142 ? 47.867  88.422 41.151 1.00 46.13 ? 142  LEU A CG  1 
ATOM   898   C  CD1 . LEU A  1 142 ? 47.920  86.936 41.554 1.00 45.43 ? 142  LEU A CD1 1 
ATOM   899   C  CD2 . LEU A  1 142 ? 46.527  89.031 41.544 1.00 46.12 ? 142  LEU A CD2 1 
ATOM   900   N  N   . ILE A  1 143 ? 50.550  88.738 38.909 1.00 41.99 ? 143  ILE A N   1 
ATOM   901   C  CA  . ILE A  1 143 ? 50.601  89.145 37.518 1.00 39.68 ? 143  ILE A CA  1 
ATOM   902   C  C   . ILE A  1 143 ? 49.197  89.390 37.004 1.00 40.27 ? 143  ILE A C   1 
ATOM   903   O  O   . ILE A  1 143 ? 48.310  88.549 37.174 1.00 39.61 ? 143  ILE A O   1 
ATOM   904   C  CB  . ILE A  1 143 ? 51.298  88.075 36.674 1.00 39.77 ? 143  ILE A CB  1 
ATOM   905   C  CG1 . ILE A  1 143 ? 52.754  87.965 37.133 1.00 38.78 ? 143  ILE A CG1 1 
ATOM   906   C  CG2 . ILE A  1 143 ? 51.202  88.416 35.193 1.00 38.59 ? 143  ILE A CG2 1 
ATOM   907   C  CD1 . ILE A  1 143 ? 53.551  86.910 36.416 1.00 39.73 ? 143  ILE A CD1 1 
ATOM   908   N  N   . THR A  1 144 ? 48.996  90.555 36.382 1.00 40.50 ? 144  THR A N   1 
ATOM   909   C  CA  . THR A  1 144 ? 47.692  90.936 35.857 1.00 40.60 ? 144  THR A CA  1 
ATOM   910   C  C   . THR A  1 144 ? 47.629  91.054 34.347 1.00 40.41 ? 144  THR A C   1 
ATOM   911   O  O   . THR A  1 144 ? 46.552  91.186 33.779 1.00 40.56 ? 144  THR A O   1 
ATOM   912   C  CB  . THR A  1 144 ? 47.227  92.276 36.462 1.00 41.66 ? 144  THR A CB  1 
ATOM   913   O  OG1 . THR A  1 144 ? 48.254  93.261 36.280 1.00 42.95 ? 144  THR A OG1 1 
ATOM   914   C  CG2 . THR A  1 144 ? 46.928  92.115 37.954 1.00 42.02 ? 144  THR A CG2 1 
ATOM   915   N  N   . GLU A  1 145 ? 48.769  90.996 33.684 1.00 41.33 ? 145  GLU A N   1 
ATOM   916   C  CA  . GLU A  1 145 ? 48.769  91.098 32.228 1.00 43.24 ? 145  GLU A CA  1 
ATOM   917   C  C   . GLU A  1 145 ? 48.811  89.711 31.578 1.00 43.33 ? 145  GLU A C   1 
ATOM   918   O  O   . GLU A  1 145 ? 49.442  88.791 32.102 1.00 42.07 ? 145  GLU A O   1 
ATOM   919   C  CB  . GLU A  1 145 ? 49.980  91.923 31.777 1.00 45.83 ? 145  GLU A CB  1 
ATOM   920   C  CG  . GLU A  1 145 ? 50.151  93.226 32.567 1.00 49.64 ? 145  GLU A CG  1 
ATOM   921   C  CD  . GLU A  1 145 ? 51.524  93.866 32.388 1.00 53.27 ? 145  GLU A CD  1 
ATOM   922   O  OE1 . GLU A  1 145 ? 51.860  94.788 33.179 1.00 55.37 ? 145  GLU A OE1 1 
ATOM   923   O  OE2 . GLU A  1 145 ? 52.275  93.463 31.459 1.00 54.20 ? 145  GLU A OE2 1 
ATOM   924   N  N   . GLU A  1 146 ? 48.126  89.567 30.447 1.00 43.28 ? 146  GLU A N   1 
ATOM   925   C  CA  . GLU A  1 146 ? 48.108  88.314 29.702 1.00 43.83 ? 146  GLU A CA  1 
ATOM   926   C  C   . GLU A  1 146 ? 47.921  87.099 30.611 1.00 43.91 ? 146  GLU A C   1 
ATOM   927   O  O   . GLU A  1 146 ? 48.743  86.179 30.605 1.00 44.33 ? 146  GLU A O   1 
ATOM   928   C  CB  . GLU A  1 146 ? 49.422  88.154 28.926 1.00 43.99 ? 146  GLU A CB  1 
ATOM   929   C  CG  . GLU A  1 146 ? 49.766  89.309 27.976 1.00 44.81 ? 146  GLU A CG  1 
ATOM   930   C  CD  . GLU A  1 146 ? 48.774  89.457 26.833 1.00 45.42 ? 146  GLU A CD  1 
ATOM   931   O  OE1 . GLU A  1 146 ? 48.252  88.427 26.352 1.00 45.74 ? 146  GLU A OE1 1 
ATOM   932   O  OE2 . GLU A  1 146 ? 48.530  90.604 26.399 1.00 46.39 ? 146  GLU A OE2 1 
ATOM   933   N  N   . ARG A  1 147 ? 46.842  87.083 31.386 1.00 43.32 ? 147  ARG A N   1 
ATOM   934   C  CA  . ARG A  1 147 ? 46.602  85.975 32.300 1.00 42.66 ? 147  ARG A CA  1 
ATOM   935   C  C   . ARG A  1 147 ? 45.890  84.792 31.659 1.00 41.22 ? 147  ARG A C   1 
ATOM   936   O  O   . ARG A  1 147 ? 45.110  84.937 30.713 1.00 40.10 ? 147  ARG A O   1 
ATOM   937   C  CB  . ARG A  1 147 ? 45.814  86.452 33.528 1.00 43.63 ? 147  ARG A CB  1 
ATOM   938   C  CG  . ARG A  1 147 ? 44.960  87.661 33.277 1.00 45.97 ? 147  ARG A CG  1 
ATOM   939   C  CD  . ARG A  1 147 ? 44.125  88.017 34.492 1.00 47.42 ? 147  ARG A CD  1 
ATOM   940   N  NE  . ARG A  1 147 ? 44.922  88.080 35.708 1.00 49.34 ? 147  ARG A NE  1 
ATOM   941   C  CZ  . ARG A  1 147 ? 44.433  88.409 36.901 1.00 50.56 ? 147  ARG A CZ  1 
ATOM   942   N  NH1 . ARG A  1 147 ? 43.143  88.709 37.027 1.00 51.01 ? 147  ARG A NH1 1 
ATOM   943   N  NH2 . ARG A  1 147 ? 45.231  88.434 37.968 1.00 50.15 ? 147  ARG A NH2 1 
ATOM   944   N  N   . ILE A  1 148 ? 46.187  83.611 32.186 1.00 38.84 ? 148  ILE A N   1 
ATOM   945   C  CA  . ILE A  1 148 ? 45.584  82.381 31.704 1.00 36.51 ? 148  ILE A CA  1 
ATOM   946   C  C   . ILE A  1 148 ? 44.067  82.549 31.721 1.00 34.91 ? 148  ILE A C   1 
ATOM   947   O  O   . ILE A  1 148 ? 43.511  83.098 32.667 1.00 32.46 ? 148  ILE A O   1 
ATOM   948   C  CB  . ILE A  1 148 ? 46.001  81.226 32.613 1.00 37.16 ? 148  ILE A CB  1 
ATOM   949   C  CG1 . ILE A  1 148 ? 47.519  81.056 32.526 1.00 36.18 ? 148  ILE A CG1 1 
ATOM   950   C  CG2 . ILE A  1 148 ? 45.215  79.968 32.262 1.00 35.20 ? 148  ILE A CG2 1 
ATOM   951   C  CD1 . ILE A  1 148 ? 48.076  79.974 33.424 1.00 38.30 ? 148  ILE A CD1 1 
ATOM   952   N  N   . PRO A  1 149 ? 43.383  82.079 30.666 1.00 34.66 ? 149  PRO A N   1 
ATOM   953   C  CA  . PRO A  1 149 ? 41.922  82.177 30.544 1.00 35.31 ? 149  PRO A CA  1 
ATOM   954   C  C   . PRO A  1 149 ? 41.189  81.384 31.616 1.00 36.45 ? 149  PRO A C   1 
ATOM   955   O  O   . PRO A  1 149 ? 41.749  80.464 32.218 1.00 36.57 ? 149  PRO A O   1 
ATOM   956   C  CB  . PRO A  1 149 ? 41.632  81.583 29.163 1.00 35.16 ? 149  PRO A CB  1 
ATOM   957   C  CG  . PRO A  1 149 ? 42.963  81.546 28.465 1.00 36.04 ? 149  PRO A CG  1 
ATOM   958   C  CD  . PRO A  1 149 ? 43.947  81.297 29.558 1.00 35.01 ? 149  PRO A CD  1 
ATOM   959   N  N   . ASN A  1 150 ? 39.930  81.742 31.844 1.00 36.84 ? 150  ASN A N   1 
ATOM   960   C  CA  . ASN A  1 150 ? 39.101  81.023 32.799 1.00 37.94 ? 150  ASN A CA  1 
ATOM   961   C  C   . ASN A  1 150 ? 38.629  79.760 32.075 1.00 36.04 ? 150  ASN A C   1 
ATOM   962   O  O   . ASN A  1 150 ? 38.671  79.688 30.842 1.00 35.94 ? 150  ASN A O   1 
ATOM   963   C  CB  . ASN A  1 150 ? 37.918  81.900 33.238 1.00 41.62 ? 150  ASN A CB  1 
ATOM   964   C  CG  . ASN A  1 150 ? 38.299  82.864 34.363 1.00 45.86 ? 150  ASN A CG  1 
ATOM   965   O  OD1 . ASN A  1 150 ? 38.354  82.475 35.525 1.00 47.27 ? 150  ASN A OD1 1 
ATOM   966   N  ND2 . ASN A  1 150 ? 38.600  84.111 34.024 1.00 49.83 ? 150  ASN A ND2 1 
ATOM   967   N  N   . ASN A  1 151 ? 38.209  78.751 32.824 1.00 33.69 ? 151  ASN A N   1 
ATOM   968   C  CA  . ASN A  1 151 ? 37.773  77.516 32.184 1.00 32.68 ? 151  ASN A CA  1 
ATOM   969   C  C   . ASN A  1 151 ? 38.926  76.793 31.492 1.00 30.65 ? 151  ASN A C   1 
ATOM   970   O  O   . ASN A  1 151 ? 38.726  76.090 30.510 1.00 30.05 ? 151  ASN A O   1 
ATOM   971   C  CB  . ASN A  1 151 ? 36.675  77.819 31.172 1.00 33.31 ? 151  ASN A CB  1 
ATOM   972   C  CG  . ASN A  1 151 ? 35.546  78.608 31.788 1.00 34.77 ? 151  ASN A CG  1 
ATOM   973   O  OD1 . ASN A  1 151 ? 34.948  78.177 32.780 1.00 33.26 ? 151  ASN A OD1 1 
ATOM   974   N  ND2 . ASN A  1 151 ? 35.258  79.781 31.221 1.00 34.84 ? 151  ASN A ND2 1 
ATOM   975   N  N   . THR A  1 152 ? 40.137  76.986 32.003 1.00 29.28 ? 152  THR A N   1 
ATOM   976   C  CA  . THR A  1 152 ? 41.301  76.313 31.441 1.00 28.50 ? 152  THR A CA  1 
ATOM   977   C  C   . THR A  1 152 ? 41.185  74.832 31.806 1.00 26.76 ? 152  THR A C   1 
ATOM   978   O  O   . THR A  1 152 ? 40.836  74.487 32.937 1.00 27.28 ? 152  THR A O   1 
ATOM   979   C  CB  . THR A  1 152 ? 42.596  76.923 31.992 1.00 28.33 ? 152  THR A CB  1 
ATOM   980   O  OG1 . THR A  1 152 ? 42.782  78.196 31.373 1.00 30.49 ? 152  THR A OG1 1 
ATOM   981   C  CG2 . THR A  1 152 ? 43.804  76.037 31.689 1.00 28.79 ? 152  THR A CG2 1 
ATOM   982   N  N   . GLN A  1 153 ? 41.462  73.977 30.833 1.00 24.88 ? 153  GLN A N   1 
ATOM   983   C  CA  . GLN A  1 153 ? 41.349  72.542 30.996 1.00 24.44 ? 153  GLN A CA  1 
ATOM   984   C  C   . GLN A  1 153 ? 42.591  71.865 31.566 1.00 24.88 ? 153  GLN A C   1 
ATOM   985   O  O   . GLN A  1 153 ? 42.508  70.836 32.230 1.00 23.43 ? 153  GLN A O   1 
ATOM   986   C  CB  . GLN A  1 153 ? 40.962  71.926 29.652 1.00 24.82 ? 153  GLN A CB  1 
ATOM   987   C  CG  . GLN A  1 153 ? 39.562  72.350 29.189 1.00 25.00 ? 153  GLN A CG  1 
ATOM   988   C  CD  . GLN A  1 153 ? 39.387  72.217 27.693 1.00 25.82 ? 153  GLN A CD  1 
ATOM   989   O  OE1 . GLN A  1 153 ? 40.163  72.784 26.926 1.00 25.19 ? 153  GLN A OE1 1 
ATOM   990   N  NE2 . GLN A  1 153 ? 38.373  71.468 27.268 1.00 23.00 ? 153  GLN A NE2 1 
ATOM   991   N  N   . TRP A  1 154 ? 43.752  72.444 31.314 1.00 24.99 ? 154  TRP A N   1 
ATOM   992   C  CA  . TRP A  1 154 ? 44.985  71.874 31.835 1.00 25.32 ? 154  TRP A CA  1 
ATOM   993   C  C   . TRP A  1 154 ? 46.108  72.873 31.719 1.00 25.07 ? 154  TRP A C   1 
ATOM   994   O  O   . TRP A  1 154 ? 46.179  73.626 30.754 1.00 23.55 ? 154  TRP A O   1 
ATOM   995   C  CB  . TRP A  1 154 ? 45.375  70.608 31.073 1.00 24.31 ? 154  TRP A CB  1 
ATOM   996   C  CG  . TRP A  1 154 ? 46.674  70.030 31.570 1.00 24.95 ? 154  TRP A CG  1 
ATOM   997   C  CD1 . TRP A  1 154 ? 47.892  70.094 30.950 1.00 26.33 ? 154  TRP A CD1 1 
ATOM   998   C  CD2 . TRP A  1 154 ? 46.896  69.353 32.815 1.00 24.77 ? 154  TRP A CD2 1 
ATOM   999   N  NE1 . TRP A  1 154 ? 48.856  69.503 31.733 1.00 26.36 ? 154  TRP A NE1 1 
ATOM   1000  C  CE2 . TRP A  1 154 ? 48.272  69.039 32.882 1.00 25.54 ? 154  TRP A CE2 1 
ATOM   1001  C  CE3 . TRP A  1 154 ? 46.064  68.985 33.884 1.00 25.12 ? 154  TRP A CE3 1 
ATOM   1002  C  CZ2 . TRP A  1 154 ? 48.840  68.369 33.977 1.00 24.49 ? 154  TRP A CZ2 1 
ATOM   1003  C  CZ3 . TRP A  1 154 ? 46.629  68.321 34.976 1.00 24.70 ? 154  TRP A CZ3 1 
ATOM   1004  C  CH2 . TRP A  1 154 ? 48.003  68.020 35.010 1.00 25.07 ? 154  TRP A CH2 1 
ATOM   1005  N  N   . VAL A  1 155 ? 46.992  72.863 32.702 1.00 25.93 ? 155  VAL A N   1 
ATOM   1006  C  CA  . VAL A  1 155 ? 48.125  73.768 32.684 1.00 28.27 ? 155  VAL A CA  1 
ATOM   1007  C  C   . VAL A  1 155 ? 49.309  73.060 33.328 1.00 28.72 ? 155  VAL A C   1 
ATOM   1008  O  O   . VAL A  1 155 ? 49.129  72.249 34.244 1.00 29.72 ? 155  VAL A O   1 
ATOM   1009  C  CB  . VAL A  1 155 ? 47.804  75.100 33.437 1.00 28.46 ? 155  VAL A CB  1 
ATOM   1010  C  CG1 . VAL A  1 155 ? 47.396  74.807 34.868 1.00 30.41 ? 155  VAL A CG1 1 
ATOM   1011  C  CG2 . VAL A  1 155 ? 49.007  76.028 33.411 1.00 29.19 ? 155  VAL A CG2 1 
ATOM   1012  N  N   . THR A  1 156 ? 50.510  73.331 32.817 1.00 28.46 ? 156  THR A N   1 
ATOM   1013  C  CA  . THR A  1 156 ? 51.722  72.727 33.352 1.00 27.27 ? 156  THR A CA  1 
ATOM   1014  C  C   . THR A  1 156 ? 52.974  73.560 33.106 1.00 27.80 ? 156  THR A C   1 
ATOM   1015  O  O   . THR A  1 156 ? 53.201  74.050 31.999 1.00 28.37 ? 156  THR A O   1 
ATOM   1016  C  CB  . THR A  1 156 ? 51.992  71.331 32.733 1.00 27.72 ? 156  THR A CB  1 
ATOM   1017  O  OG1 . THR A  1 156 ? 53.286  70.884 33.142 1.00 28.90 ? 156  THR A OG1 1 
ATOM   1018  C  CG2 . THR A  1 156 ? 51.983  71.377 31.212 1.00 25.57 ? 156  THR A CG2 1 
ATOM   1019  N  N   . TRP A  1 157 ? 53.794  73.707 34.137 1.00 27.74 ? 157  TRP A N   1 
ATOM   1020  C  CA  . TRP A  1 157 ? 55.055  74.419 33.999 1.00 27.49 ? 157  TRP A CA  1 
ATOM   1021  C  C   . TRP A  1 157 ? 55.949  73.518 33.146 1.00 27.54 ? 157  TRP A C   1 
ATOM   1022  O  O   . TRP A  1 157 ? 55.675  72.324 33.013 1.00 26.88 ? 157  TRP A O   1 
ATOM   1023  C  CB  . TRP A  1 157 ? 55.736  74.588 35.353 1.00 27.50 ? 157  TRP A CB  1 
ATOM   1024  C  CG  . TRP A  1 157 ? 55.133  75.595 36.236 1.00 29.17 ? 157  TRP A CG  1 
ATOM   1025  C  CD1 . TRP A  1 157 ? 54.461  75.367 37.396 1.00 28.49 ? 157  TRP A CD1 1 
ATOM   1026  C  CD2 . TRP A  1 157 ? 55.160  77.016 36.053 1.00 28.80 ? 157  TRP A CD2 1 
ATOM   1027  N  NE1 . TRP A  1 157 ? 54.065  76.557 37.955 1.00 28.91 ? 157  TRP A NE1 1 
ATOM   1028  C  CE2 . TRP A  1 157 ? 54.480  77.586 37.150 1.00 28.83 ? 157  TRP A CE2 1 
ATOM   1029  C  CE3 . TRP A  1 157 ? 55.696  77.862 35.071 1.00 28.34 ? 157  TRP A CE3 1 
ATOM   1030  C  CZ2 . TRP A  1 157 ? 54.316  78.970 37.294 1.00 28.57 ? 157  TRP A CZ2 1 
ATOM   1031  C  CZ3 . TRP A  1 157 ? 55.537  79.239 35.218 1.00 28.30 ? 157  TRP A CZ3 1 
ATOM   1032  C  CH2 . TRP A  1 157 ? 54.852  79.776 36.321 1.00 27.93 ? 157  TRP A CH2 1 
ATOM   1033  N  N   . SER A  1 158 ? 56.998  74.084 32.559 1.00 27.07 ? 158  SER A N   1 
ATOM   1034  C  CA  . SER A  1 158 ? 57.938  73.287 31.780 1.00 27.34 ? 158  SER A CA  1 
ATOM   1035  C  C   . SER A  1 158 ? 58.707  72.549 32.865 1.00 27.87 ? 158  SER A C   1 
ATOM   1036  O  O   . SER A  1 158 ? 58.629  72.923 34.031 1.00 28.74 ? 158  SER A O   1 
ATOM   1037  C  CB  . SER A  1 158 ? 58.868  74.195 30.959 1.00 27.54 ? 158  SER A CB  1 
ATOM   1038  O  OG  . SER A  1 158 ? 59.316  75.308 31.726 1.00 27.82 ? 158  SER A OG  1 
ATOM   1039  N  N   . PRO A  1 159 ? 59.440  71.490 32.516 1.00 28.12 ? 159  PRO A N   1 
ATOM   1040  C  CA  . PRO A  1 159 ? 60.175  70.768 33.563 1.00 29.14 ? 159  PRO A CA  1 
ATOM   1041  C  C   . PRO A  1 159 ? 61.303  71.589 34.201 1.00 30.58 ? 159  PRO A C   1 
ATOM   1042  O  O   . PRO A  1 159 ? 61.671  71.377 35.357 1.00 30.93 ? 159  PRO A O   1 
ATOM   1043  C  CB  . PRO A  1 159 ? 60.653  69.498 32.845 1.00 28.26 ? 159  PRO A CB  1 
ATOM   1044  C  CG  . PRO A  1 159 ? 60.779  69.943 31.390 1.00 29.53 ? 159  PRO A CG  1 
ATOM   1045  C  CD  . PRO A  1 159 ? 59.580  70.842 31.200 1.00 28.08 ? 159  PRO A CD  1 
ATOM   1046  N  N   . VAL A  1 160 ? 61.837  72.543 33.453 1.00 31.72 ? 160  VAL A N   1 
ATOM   1047  C  CA  . VAL A  1 160 ? 62.891  73.407 33.972 1.00 32.33 ? 160  VAL A CA  1 
ATOM   1048  C  C   . VAL A  1 160 ? 62.499  74.859 33.698 1.00 32.56 ? 160  VAL A C   1 
ATOM   1049  O  O   . VAL A  1 160 ? 61.785  75.137 32.738 1.00 32.63 ? 160  VAL A O   1 
ATOM   1050  C  CB  . VAL A  1 160 ? 64.243  73.096 33.291 1.00 33.22 ? 160  VAL A CB  1 
ATOM   1051  C  CG1 . VAL A  1 160 ? 65.214  74.242 33.498 1.00 33.87 ? 160  VAL A CG1 1 
ATOM   1052  C  CG2 . VAL A  1 160 ? 64.826  71.807 33.865 1.00 33.07 ? 160  VAL A CG2 1 
ATOM   1053  N  N   . GLY A  1 161 ? 62.945  75.777 34.550 1.00 32.37 ? 161  GLY A N   1 
ATOM   1054  C  CA  . GLY A  1 161 ? 62.628  77.177 34.334 1.00 30.93 ? 161  GLY A CA  1 
ATOM   1055  C  C   . GLY A  1 161 ? 61.205  77.576 34.683 1.00 30.36 ? 161  GLY A C   1 
ATOM   1056  O  O   . GLY A  1 161 ? 60.686  77.207 35.735 1.00 29.53 ? 161  GLY A O   1 
ATOM   1057  N  N   . HIS A  1 162 ? 60.562  78.335 33.804 1.00 29.81 ? 162  HIS A N   1 
ATOM   1058  C  CA  . HIS A  1 162 ? 59.207  78.784 34.086 1.00 29.21 ? 162  HIS A CA  1 
ATOM   1059  C  C   . HIS A  1 162 ? 58.288  78.983 32.899 1.00 28.09 ? 162  HIS A C   1 
ATOM   1060  O  O   . HIS A  1 162 ? 57.431  79.860 32.941 1.00 27.27 ? 162  HIS A O   1 
ATOM   1061  C  CB  . HIS A  1 162 ? 59.235  80.078 34.903 1.00 31.24 ? 162  HIS A CB  1 
ATOM   1062  C  CG  . HIS A  1 162 ? 60.037  81.173 34.274 1.00 34.44 ? 162  HIS A CG  1 
ATOM   1063  N  ND1 . HIS A  1 162 ? 61.157  81.713 34.872 1.00 34.83 ? 162  HIS A ND1 1 
ATOM   1064  C  CD2 . HIS A  1 162 ? 59.883  81.833 33.103 1.00 34.91 ? 162  HIS A CD2 1 
ATOM   1065  C  CE1 . HIS A  1 162 ? 61.655  82.657 34.096 1.00 36.13 ? 162  HIS A CE1 1 
ATOM   1066  N  NE2 . HIS A  1 162 ? 60.901  82.751 33.015 1.00 36.33 ? 162  HIS A NE2 1 
ATOM   1067  N  N   . LYS A  1 163 ? 58.467  78.208 31.836 1.00 27.07 ? 163  LYS A N   1 
ATOM   1068  C  CA  . LYS A  1 163 ? 57.554  78.313 30.707 1.00 27.48 ? 163  LYS A CA  1 
ATOM   1069  C  C   . LYS A  1 163 ? 56.244  77.680 31.165 1.00 28.06 ? 163  LYS A C   1 
ATOM   1070  O  O   . LYS A  1 163 ? 56.217  76.944 32.153 1.00 28.54 ? 163  LYS A O   1 
ATOM   1071  C  CB  . LYS A  1 163 ? 58.044  77.522 29.499 1.00 28.25 ? 163  LYS A CB  1 
ATOM   1072  C  CG  . LYS A  1 163 ? 59.265  78.084 28.788 1.00 31.01 ? 163  LYS A CG  1 
ATOM   1073  C  CD  . LYS A  1 163 ? 59.621  77.217 27.584 1.00 30.02 ? 163  LYS A CD  1 
ATOM   1074  C  CE  . LYS A  1 163 ? 60.941  77.639 26.950 1.00 30.33 ? 163  LYS A CE  1 
ATOM   1075  N  NZ  . LYS A  1 163 ? 61.289  76.762 25.794 1.00 30.36 ? 163  LYS A NZ  1 
ATOM   1076  N  N   . LEU A  1 164 ? 55.166  77.961 30.440 1.00 28.25 ? 164  LEU A N   1 
ATOM   1077  C  CA  . LEU A  1 164 ? 53.854  77.401 30.736 1.00 27.98 ? 164  LEU A CA  1 
ATOM   1078  C  C   . LEU A  1 164 ? 53.223  76.848 29.472 1.00 28.50 ? 164  LEU A C   1 
ATOM   1079  O  O   . LEU A  1 164 ? 53.474  77.327 28.368 1.00 28.38 ? 164  LEU A O   1 
ATOM   1080  C  CB  . LEU A  1 164 ? 52.909  78.468 31.289 1.00 28.20 ? 164  LEU A CB  1 
ATOM   1081  C  CG  . LEU A  1 164 ? 53.040  78.861 32.750 1.00 29.40 ? 164  LEU A CG  1 
ATOM   1082  C  CD1 . LEU A  1 164 ? 52.330  80.174 32.994 1.00 28.27 ? 164  LEU A CD1 1 
ATOM   1083  C  CD2 . LEU A  1 164 ? 52.465  77.745 33.628 1.00 29.40 ? 164  LEU A CD2 1 
ATOM   1084  N  N   . ALA A  1 165 ? 52.404  75.823 29.641 1.00 28.21 ? 165  ALA A N   1 
ATOM   1085  C  CA  . ALA A  1 165 ? 51.660  75.244 28.535 1.00 28.29 ? 165  ALA A CA  1 
ATOM   1086  C  C   . ALA A  1 165 ? 50.286  74.960 29.137 1.00 28.51 ? 165  ALA A C   1 
ATOM   1087  O  O   . ALA A  1 165 ? 50.186  74.355 30.200 1.00 30.11 ? 165  ALA A O   1 
ATOM   1088  C  CB  . ALA A  1 165 ? 52.314  73.972 28.063 1.00 27.35 ? 165  ALA A CB  1 
ATOM   1089  N  N   . TYR A  1 166 ? 49.231  75.449 28.504 1.00 28.30 ? 166  TYR A N   1 
ATOM   1090  C  CA  . TYR A  1 166 ? 47.891  75.194 29.005 1.00 28.40 ? 166  TYR A CA  1 
ATOM   1091  C  C   . TYR A  1 166 ? 46.988  74.913 27.833 1.00 27.17 ? 166  TYR A C   1 
ATOM   1092  O  O   . TYR A  1 166 ? 47.314  75.260 26.701 1.00 27.90 ? 166  TYR A O   1 
ATOM   1093  C  CB  . TYR A  1 166 ? 47.332  76.369 29.838 1.00 29.46 ? 166  TYR A CB  1 
ATOM   1094  C  CG  . TYR A  1 166 ? 47.241  77.686 29.101 1.00 32.67 ? 166  TYR A CG  1 
ATOM   1095  C  CD1 . TYR A  1 166 ? 48.343  78.549 29.040 1.00 33.17 ? 166  TYR A CD1 1 
ATOM   1096  C  CD2 . TYR A  1 166 ? 46.060  78.070 28.452 1.00 32.39 ? 166  TYR A CD2 1 
ATOM   1097  C  CE1 . TYR A  1 166 ? 48.273  79.764 28.352 1.00 34.44 ? 166  TYR A CE1 1 
ATOM   1098  C  CE2 . TYR A  1 166 ? 45.978  79.282 27.760 1.00 34.57 ? 166  TYR A CE2 1 
ATOM   1099  C  CZ  . TYR A  1 166 ? 47.089  80.119 27.717 1.00 35.21 ? 166  TYR A CZ  1 
ATOM   1100  O  OH  . TYR A  1 166 ? 47.023  81.306 27.049 1.00 36.40 ? 166  TYR A OH  1 
ATOM   1101  N  N   . VAL A  1 167 ? 45.869  74.252 28.113 1.00 25.94 ? 167  VAL A N   1 
ATOM   1102  C  CA  . VAL A  1 167 ? 44.894  73.905 27.101 1.00 25.51 ? 167  VAL A CA  1 
ATOM   1103  C  C   . VAL A  1 167 ? 43.611  74.622 27.460 1.00 26.71 ? 167  VAL A C   1 
ATOM   1104  O  O   . VAL A  1 167 ? 43.199  74.618 28.617 1.00 26.46 ? 167  VAL A O   1 
ATOM   1105  C  CB  . VAL A  1 167 ? 44.635  72.399 27.068 1.00 25.12 ? 167  VAL A CB  1 
ATOM   1106  C  CG1 . VAL A  1 167 ? 43.507  72.084 26.103 1.00 22.81 ? 167  VAL A CG1 1 
ATOM   1107  C  CG2 . VAL A  1 167 ? 45.921  71.673 26.664 1.00 23.04 ? 167  VAL A CG2 1 
ATOM   1108  N  N   . TRP A  1 168 ? 42.994  75.249 26.461 1.00 27.38 ? 168  TRP A N   1 
ATOM   1109  C  CA  . TRP A  1 168 ? 41.760  76.002 26.651 1.00 28.13 ? 168  TRP A CA  1 
ATOM   1110  C  C   . TRP A  1 168 ? 40.899  75.762 25.419 1.00 27.83 ? 168  TRP A C   1 
ATOM   1111  O  O   . TRP A  1 168 ? 41.380  75.865 24.290 1.00 27.72 ? 168  TRP A O   1 
ATOM   1112  C  CB  . TRP A  1 168 ? 42.104  77.484 26.796 1.00 29.78 ? 168  TRP A CB  1 
ATOM   1113  C  CG  . TRP A  1 168 ? 40.949  78.359 27.086 1.00 31.88 ? 168  TRP A CG  1 
ATOM   1114  C  CD1 . TRP A  1 168 ? 40.263  78.446 28.262 1.00 32.18 ? 168  TRP A CD1 1 
ATOM   1115  C  CD2 . TRP A  1 168 ? 40.345  79.300 26.194 1.00 32.76 ? 168  TRP A CD2 1 
ATOM   1116  N  NE1 . TRP A  1 168 ? 39.271  79.385 28.161 1.00 32.47 ? 168  TRP A NE1 1 
ATOM   1117  C  CE2 . TRP A  1 168 ? 39.298  79.926 26.901 1.00 33.69 ? 168  TRP A CE2 1 
ATOM   1118  C  CE3 . TRP A  1 168 ? 40.589  79.679 24.866 1.00 34.91 ? 168  TRP A CE3 1 
ATOM   1119  C  CZ2 . TRP A  1 168 ? 38.490  80.915 26.327 1.00 34.33 ? 168  TRP A CZ2 1 
ATOM   1120  C  CZ3 . TRP A  1 168 ? 39.782  80.670 24.290 1.00 35.48 ? 168  TRP A CZ3 1 
ATOM   1121  C  CH2 . TRP A  1 168 ? 38.747  81.273 25.026 1.00 36.03 ? 168  TRP A CH2 1 
ATOM   1122  N  N   . ASN A  1 169 ? 39.638  75.420 25.627 1.00 26.71 ? 169  ASN A N   1 
ATOM   1123  C  CA  . ASN A  1 169 ? 38.758  75.150 24.498 1.00 27.37 ? 169  ASN A CA  1 
ATOM   1124  C  C   . ASN A  1 169 ? 39.360  74.122 23.540 1.00 26.67 ? 169  ASN A C   1 
ATOM   1125  O  O   . ASN A  1 169 ? 39.276  74.259 22.320 1.00 26.90 ? 169  ASN A O   1 
ATOM   1126  C  CB  . ASN A  1 169 ? 38.446  76.449 23.749 1.00 28.56 ? 169  ASN A CB  1 
ATOM   1127  C  CG  . ASN A  1 169 ? 37.495  77.355 24.516 1.00 31.51 ? 169  ASN A CG  1 
ATOM   1128  O  OD1 . ASN A  1 169 ? 37.335  78.522 24.176 1.00 36.35 ? 169  ASN A OD1 1 
ATOM   1129  N  ND2 . ASN A  1 169 ? 36.858  76.823 25.548 1.00 32.12 ? 169  ASN A ND2 1 
ATOM   1130  N  N   . ASN A  1 170 ? 39.976  73.090 24.111 1.00 26.64 ? 170  ASN A N   1 
ATOM   1131  C  CA  . ASN A  1 170 ? 40.573  72.005 23.337 1.00 24.92 ? 170  ASN A CA  1 
ATOM   1132  C  C   . ASN A  1 170 ? 41.775  72.371 22.462 1.00 25.00 ? 170  ASN A C   1 
ATOM   1133  O  O   . ASN A  1 170 ? 42.166  71.589 21.602 1.00 25.73 ? 170  ASN A O   1 
ATOM   1134  C  CB  . ASN A  1 170 ? 39.484  71.334 22.494 1.00 24.11 ? 170  ASN A CB  1 
ATOM   1135  C  CG  . ASN A  1 170 ? 38.479  70.592 23.349 1.00 23.24 ? 170  ASN A CG  1 
ATOM   1136  O  OD1 . ASN A  1 170 ? 38.096  71.076 24.411 1.00 21.86 ? 170  ASN A OD1 1 
ATOM   1137  N  ND2 . ASN A  1 170 ? 38.050  69.417 22.897 1.00 21.62 ? 170  ASN A ND2 1 
ATOM   1138  N  N   . ASP A  1 171 ? 42.353  73.550 22.681 1.00 25.34 ? 171  ASP A N   1 
ATOM   1139  C  CA  . ASP A  1 171 ? 43.532  73.984 21.934 1.00 25.21 ? 171  ASP A CA  1 
ATOM   1140  C  C   . ASP A  1 171 ? 44.714  74.246 22.844 1.00 24.63 ? 171  ASP A C   1 
ATOM   1141  O  O   . ASP A  1 171 ? 44.538  74.620 24.005 1.00 24.45 ? 171  ASP A O   1 
ATOM   1142  C  CB  . ASP A  1 171 ? 43.230  75.240 21.124 1.00 25.77 ? 171  ASP A CB  1 
ATOM   1143  C  CG  . ASP A  1 171 ? 42.579  74.923 19.806 1.00 25.25 ? 171  ASP A CG  1 
ATOM   1144  O  OD1 . ASP A  1 171 ? 41.657  75.657 19.421 1.00 27.37 ? 171  ASP A OD1 1 
ATOM   1145  O  OD2 . ASP A  1 171 ? 42.991  73.937 19.165 1.00 26.61 ? 171  ASP A OD2 1 
ATOM   1146  N  N   . ILE A  1 172 ? 45.920  74.053 22.313 1.00 24.42 ? 172  ILE A N   1 
ATOM   1147  C  CA  . ILE A  1 172 ? 47.144  74.254 23.089 1.00 25.11 ? 172  ILE A CA  1 
ATOM   1148  C  C   . ILE A  1 172 ? 47.735  75.664 22.943 1.00 26.31 ? 172  ILE A C   1 
ATOM   1149  O  O   . ILE A  1 172 ? 47.772  76.205 21.842 1.00 26.20 ? 172  ILE A O   1 
ATOM   1150  C  CB  . ILE A  1 172 ? 48.215  73.255 22.659 1.00 24.95 ? 172  ILE A CB  1 
ATOM   1151  C  CG1 . ILE A  1 172 ? 47.698  71.833 22.851 1.00 24.68 ? 172  ILE A CG1 1 
ATOM   1152  C  CG2 . ILE A  1 172 ? 49.491  73.486 23.460 1.00 24.28 ? 172  ILE A CG2 1 
ATOM   1153  C  CD1 . ILE A  1 172 ? 48.661  70.767 22.378 1.00 24.35 ? 172  ILE A CD1 1 
ATOM   1154  N  N   . TYR A  1 173 ? 48.207  76.218 24.065 1.00 27.04 ? 173  TYR A N   1 
ATOM   1155  C  CA  . TYR A  1 173 ? 48.824  77.539 24.149 1.00 28.32 ? 173  TYR A CA  1 
ATOM   1156  C  C   . TYR A  1 173 ? 50.122  77.430 24.946 1.00 29.26 ? 173  TYR A C   1 
ATOM   1157  O  O   . TYR A  1 173 ? 50.229  76.589 25.832 1.00 28.61 ? 173  TYR A O   1 
ATOM   1158  C  CB  . TYR A  1 173 ? 47.921  78.547 24.884 1.00 28.38 ? 173  TYR A CB  1 
ATOM   1159  C  CG  . TYR A  1 173 ? 46.625  78.862 24.172 1.00 30.87 ? 173  TYR A CG  1 
ATOM   1160  C  CD1 . TYR A  1 173 ? 45.512  78.019 24.293 1.00 29.45 ? 173  TYR A CD1 1 
ATOM   1161  C  CD2 . TYR A  1 173 ? 46.519  79.994 23.341 1.00 29.30 ? 173  TYR A CD2 1 
ATOM   1162  C  CE1 . TYR A  1 173 ? 44.329  78.284 23.609 1.00 29.42 ? 173  TYR A CE1 1 
ATOM   1163  C  CE2 . TYR A  1 173 ? 45.342  80.267 22.652 1.00 29.45 ? 173  TYR A CE2 1 
ATOM   1164  C  CZ  . TYR A  1 173 ? 44.250  79.402 22.788 1.00 30.44 ? 173  TYR A CZ  1 
ATOM   1165  O  OH  . TYR A  1 173 ? 43.105  79.637 22.067 1.00 30.63 ? 173  TYR A OH  1 
ATOM   1166  N  N   . VAL A  1 174 ? 51.098  78.293 24.650 1.00 30.22 ? 174  VAL A N   1 
ATOM   1167  C  CA  . VAL A  1 174 ? 52.367  78.301 25.385 1.00 30.35 ? 174  VAL A CA  1 
ATOM   1168  C  C   . VAL A  1 174 ? 52.751  79.722 25.785 1.00 31.59 ? 174  VAL A C   1 
ATOM   1169  O  O   . VAL A  1 174 ? 52.625  80.648 24.988 1.00 32.66 ? 174  VAL A O   1 
ATOM   1170  C  CB  . VAL A  1 174 ? 53.520  77.720 24.545 1.00 30.11 ? 174  VAL A CB  1 
ATOM   1171  C  CG1 . VAL A  1 174 ? 54.870  78.042 25.227 1.00 29.76 ? 174  VAL A CG1 1 
ATOM   1172  C  CG2 . VAL A  1 174 ? 53.342  76.216 24.391 1.00 30.24 ? 174  VAL A CG2 1 
ATOM   1173  N  N   . LYS A  1 175 ? 53.217  79.887 27.018 1.00 32.19 ? 175  LYS A N   1 
ATOM   1174  C  CA  . LYS A  1 175 ? 53.659  81.183 27.516 1.00 32.89 ? 175  LYS A CA  1 
ATOM   1175  C  C   . LYS A  1 175 ? 55.123  81.063 27.922 1.00 33.37 ? 175  LYS A C   1 
ATOM   1176  O  O   . LYS A  1 175 ? 55.449  80.359 28.883 1.00 32.12 ? 175  LYS A O   1 
ATOM   1177  C  CB  . LYS A  1 175 ? 52.848  81.615 28.738 1.00 34.74 ? 175  LYS A CB  1 
ATOM   1178  C  CG  . LYS A  1 175 ? 51.564  82.357 28.440 1.00 37.27 ? 175  LYS A CG  1 
ATOM   1179  C  CD  . LYS A  1 175 ? 50.724  82.528 29.714 1.00 38.79 ? 175  LYS A CD  1 
ATOM   1180  C  CE  . LYS A  1 175 ? 51.359  83.491 30.696 1.00 39.37 ? 175  LYS A CE  1 
ATOM   1181  N  NZ  . LYS A  1 175 ? 51.201  84.899 30.230 1.00 41.17 ? 175  LYS A NZ  1 
ATOM   1182  N  N   . ILE A  1 176 ? 56.004  81.749 27.198 1.00 33.20 ? 176  ILE A N   1 
ATOM   1183  C  CA  . ILE A  1 176 ? 57.428  81.709 27.503 1.00 32.88 ? 176  ILE A CA  1 
ATOM   1184  C  C   . ILE A  1 176 ? 57.712  82.401 28.826 1.00 34.09 ? 176  ILE A C   1 
ATOM   1185  O  O   . ILE A  1 176 ? 58.628  82.017 29.558 1.00 35.85 ? 176  ILE A O   1 
ATOM   1186  C  CB  . ILE A  1 176 ? 58.248  82.395 26.404 1.00 33.10 ? 176  ILE A CB  1 
ATOM   1187  C  CG1 . ILE A  1 176 ? 58.015  81.677 25.070 1.00 33.67 ? 176  ILE A CG1 1 
ATOM   1188  C  CG2 . ILE A  1 176 ? 59.721  82.417 26.782 1.00 32.50 ? 176  ILE A CG2 1 
ATOM   1189  C  CD1 . ILE A  1 176 ? 58.225  80.169 25.124 1.00 32.18 ? 176  ILE A CD1 1 
ATOM   1190  N  N   . GLU A  1 177 ? 56.918  83.419 29.132 1.00 34.14 ? 177  GLU A N   1 
ATOM   1191  C  CA  . GLU A  1 177 ? 57.066  84.181 30.363 1.00 34.73 ? 177  GLU A CA  1 
ATOM   1192  C  C   . GLU A  1 177 ? 55.672  84.376 30.947 1.00 35.38 ? 177  GLU A C   1 
ATOM   1193  O  O   . GLU A  1 177 ? 54.702  84.546 30.208 1.00 35.25 ? 177  GLU A O   1 
ATOM   1194  C  CB  . GLU A  1 177 ? 57.704  85.537 30.073 1.00 35.99 ? 177  GLU A CB  1 
ATOM   1195  C  CG  . GLU A  1 177 ? 59.108  85.471 29.463 1.00 37.93 ? 177  GLU A CG  1 
ATOM   1196  C  CD  . GLU A  1 177 ? 60.140  84.898 30.425 1.00 39.57 ? 177  GLU A CD  1 
ATOM   1197  O  OE1 . GLU A  1 177 ? 60.027  85.133 31.652 1.00 39.88 ? 177  GLU A OE1 1 
ATOM   1198  O  OE2 . GLU A  1 177 ? 61.082  84.227 29.955 1.00 40.96 ? 177  GLU A OE2 1 
ATOM   1199  N  N   . PRO A  1 178 ? 55.552  84.359 32.282 1.00 35.47 ? 178  PRO A N   1 
ATOM   1200  C  CA  . PRO A  1 178 ? 54.254  84.525 32.948 1.00 36.84 ? 178  PRO A CA  1 
ATOM   1201  C  C   . PRO A  1 178 ? 53.489  85.798 32.602 1.00 38.36 ? 178  PRO A C   1 
ATOM   1202  O  O   . PRO A  1 178 ? 52.258  85.804 32.588 1.00 38.13 ? 178  PRO A O   1 
ATOM   1203  C  CB  . PRO A  1 178 ? 54.608  84.457 34.432 1.00 36.55 ? 178  PRO A CB  1 
ATOM   1204  C  CG  . PRO A  1 178 ? 55.830  83.567 34.447 1.00 37.45 ? 178  PRO A CG  1 
ATOM   1205  C  CD  . PRO A  1 178 ? 56.616  84.066 33.256 1.00 35.04 ? 178  PRO A CD  1 
ATOM   1206  N  N   . ASN A  1 179 ? 54.204  86.879 32.310 1.00 39.57 ? 179  ASN A N   1 
ATOM   1207  C  CA  . ASN A  1 179 ? 53.523  88.132 31.987 1.00 40.45 ? 179  ASN A CA  1 
ATOM   1208  C  C   . ASN A  1 179 ? 53.409  88.432 30.496 1.00 40.09 ? 179  ASN A C   1 
ATOM   1209  O  O   . ASN A  1 179 ? 52.802  89.429 30.126 1.00 40.68 ? 179  ASN A O   1 
ATOM   1210  C  CB  . ASN A  1 179 ? 54.224  89.309 32.663 1.00 40.80 ? 179  ASN A CB  1 
ATOM   1211  C  CG  . ASN A  1 179 ? 55.539  89.650 32.003 1.00 42.42 ? 179  ASN A CG  1 
ATOM   1212  O  OD1 . ASN A  1 179 ? 55.796  90.805 31.673 1.00 44.52 ? 179  ASN A OD1 1 
ATOM   1213  N  ND2 . ASN A  1 179 ? 56.384  88.645 31.807 1.00 42.86 ? 179  ASN A ND2 1 
ATOM   1214  N  N   . LEU A  1 180 ? 53.973  87.584 29.642 1.00 39.33 ? 180  LEU A N   1 
ATOM   1215  C  CA  . LEU A  1 180 ? 53.906  87.828 28.205 1.00 38.44 ? 180  LEU A CA  1 
ATOM   1216  C  C   . LEU A  1 180 ? 52.760  87.112 27.501 1.00 38.18 ? 180  LEU A C   1 
ATOM   1217  O  O   . LEU A  1 180 ? 52.237  86.120 27.998 1.00 38.52 ? 180  LEU A O   1 
ATOM   1218  C  CB  . LEU A  1 180 ? 55.226  87.425 27.546 1.00 38.33 ? 180  LEU A CB  1 
ATOM   1219  C  CG  . LEU A  1 180 ? 56.448  88.247 27.960 1.00 39.22 ? 180  LEU A CG  1 
ATOM   1220  C  CD1 . LEU A  1 180 ? 57.700  87.752 27.231 1.00 38.51 ? 180  LEU A CD1 1 
ATOM   1221  C  CD2 . LEU A  1 180 ? 56.178  89.718 27.645 1.00 39.11 ? 180  LEU A CD2 1 
ATOM   1222  N  N   . PRO A  1 181 ? 52.352  87.616 26.321 1.00 38.15 ? 181  PRO A N   1 
ATOM   1223  C  CA  . PRO A  1 181 ? 51.262  86.997 25.558 1.00 37.75 ? 181  PRO A CA  1 
ATOM   1224  C  C   . PRO A  1 181 ? 51.617  85.588 25.130 1.00 37.11 ? 181  PRO A C   1 
ATOM   1225  O  O   . PRO A  1 181 ? 52.759  85.297 24.774 1.00 36.26 ? 181  PRO A O   1 
ATOM   1226  C  CB  . PRO A  1 181 ? 51.088  87.935 24.364 1.00 37.78 ? 181  PRO A CB  1 
ATOM   1227  C  CG  . PRO A  1 181 ? 52.468  88.504 24.185 1.00 37.75 ? 181  PRO A CG  1 
ATOM   1228  C  CD  . PRO A  1 181 ? 52.869  88.798 25.611 1.00 37.82 ? 181  PRO A CD  1 
ATOM   1229  N  N   . SER A  1 182 ? 50.621  84.716 25.145 1.00 36.82 ? 182  SER A N   1 
ATOM   1230  C  CA  . SER A  1 182 ? 50.843  83.328 24.787 1.00 36.33 ? 182  SER A CA  1 
ATOM   1231  C  C   . SER A  1 182 ? 50.750  83.083 23.288 1.00 36.05 ? 182  SER A C   1 
ATOM   1232  O  O   . SER A  1 182 ? 50.098  83.832 22.567 1.00 37.11 ? 182  SER A O   1 
ATOM   1233  C  CB  . SER A  1 182 ? 49.819  82.459 25.509 1.00 35.55 ? 182  SER A CB  1 
ATOM   1234  O  OG  . SER A  1 182 ? 48.528  82.706 24.997 1.00 34.33 ? 182  SER A OG  1 
ATOM   1235  N  N   . TYR A  1 183 ? 51.414  82.024 22.833 1.00 35.44 ? 183  TYR A N   1 
ATOM   1236  C  CA  . TYR A  1 183 ? 51.400  81.621 21.437 1.00 34.48 ? 183  TYR A CA  1 
ATOM   1237  C  C   . TYR A  1 183 ? 50.375  80.497 21.275 1.00 34.37 ? 183  TYR A C   1 
ATOM   1238  O  O   . TYR A  1 183 ? 50.344  79.563 22.083 1.00 34.83 ? 183  TYR A O   1 
ATOM   1239  C  CB  . TYR A  1 183 ? 52.771  81.087 21.024 1.00 33.58 ? 183  TYR A CB  1 
ATOM   1240  C  CG  . TYR A  1 183 ? 53.913  82.039 21.274 1.00 34.23 ? 183  TYR A CG  1 
ATOM   1241  C  CD1 . TYR A  1 183 ? 54.362  82.911 20.272 1.00 33.80 ? 183  TYR A CD1 1 
ATOM   1242  C  CD2 . TYR A  1 183 ? 54.546  82.076 22.515 1.00 32.65 ? 183  TYR A CD2 1 
ATOM   1243  C  CE1 . TYR A  1 183 ? 55.413  83.787 20.510 1.00 33.52 ? 183  TYR A CE1 1 
ATOM   1244  C  CE2 . TYR A  1 183 ? 55.584  82.941 22.766 1.00 32.93 ? 183  TYR A CE2 1 
ATOM   1245  C  CZ  . TYR A  1 183 ? 56.021  83.799 21.763 1.00 34.71 ? 183  TYR A CZ  1 
ATOM   1246  O  OH  . TYR A  1 183 ? 57.066  84.671 22.027 1.00 34.27 ? 183  TYR A OH  1 
ATOM   1247  N  N   . ARG A  1 184 ? 49.550  80.578 20.235 1.00 33.71 ? 184  ARG A N   1 
ATOM   1248  C  CA  . ARG A  1 184 ? 48.546  79.549 19.960 1.00 33.16 ? 184  ARG A CA  1 
ATOM   1249  C  C   . ARG A  1 184 ? 49.236  78.435 19.204 1.00 32.88 ? 184  ARG A C   1 
ATOM   1250  O  O   . ARG A  1 184 ? 49.770  78.670 18.122 1.00 32.61 ? 184  ARG A O   1 
ATOM   1251  C  CB  . ARG A  1 184 ? 47.443  80.097 19.068 1.00 33.15 ? 184  ARG A CB  1 
ATOM   1252  C  CG  . ARG A  1 184 ? 46.071  80.024 19.661 1.00 35.13 ? 184  ARG A CG  1 
ATOM   1253  C  CD  . ARG A  1 184 ? 45.086  79.125 18.914 1.00 34.74 ? 184  ARG A CD  1 
ATOM   1254  N  NE  . ARG A  1 184 ? 43.770  79.745 19.043 1.00 37.71 ? 184  ARG A NE  1 
ATOM   1255  C  CZ  . ARG A  1 184 ? 42.597  79.215 18.711 1.00 38.31 ? 184  ARG A CZ  1 
ATOM   1256  N  NH1 . ARG A  1 184 ? 42.486  77.994 18.205 1.00 37.89 ? 184  ARG A NH1 1 
ATOM   1257  N  NH2 . ARG A  1 184 ? 41.519  79.955 18.869 1.00 39.96 ? 184  ARG A NH2 1 
ATOM   1258  N  N   . ILE A  1 185 ? 49.215  77.221 19.744 1.00 31.88 ? 185  ILE A N   1 
ATOM   1259  C  CA  . ILE A  1 185 ? 49.870  76.116 19.051 1.00 30.10 ? 185  ILE A CA  1 
ATOM   1260  C  C   . ILE A  1 185 ? 48.940  75.358 18.104 1.00 29.87 ? 185  ILE A C   1 
ATOM   1261  O  O   . ILE A  1 185 ? 49.363  74.919 17.032 1.00 30.53 ? 185  ILE A O   1 
ATOM   1262  C  CB  . ILE A  1 185 ? 50.466  75.106 20.053 1.00 30.12 ? 185  ILE A CB  1 
ATOM   1263  C  CG1 . ILE A  1 185 ? 51.403  75.823 21.034 1.00 29.29 ? 185  ILE A CG1 1 
ATOM   1264  C  CG2 . ILE A  1 185 ? 51.189  74.003 19.302 1.00 28.65 ? 185  ILE A CG2 1 
ATOM   1265  C  CD1 . ILE A  1 185 ? 52.578  76.491 20.373 1.00 29.06 ? 185  ILE A CD1 1 
ATOM   1266  N  N   . THR A  1 186 ? 47.676  75.201 18.495 1.00 28.65 ? 186  THR A N   1 
ATOM   1267  C  CA  . THR A  1 186 ? 46.714  74.466 17.678 1.00 27.11 ? 186  THR A CA  1 
ATOM   1268  C  C   . THR A  1 186 ? 45.495  75.318 17.449 1.00 27.75 ? 186  THR A C   1 
ATOM   1269  O  O   . THR A  1 186 ? 45.192  76.188 18.255 1.00 28.55 ? 186  THR A O   1 
ATOM   1270  C  CB  . THR A  1 186 ? 46.265  73.151 18.368 1.00 25.65 ? 186  THR A CB  1 
ATOM   1271  O  OG1 . THR A  1 186 ? 45.648  73.467 19.623 1.00 23.97 ? 186  THR A OG1 1 
ATOM   1272  C  CG2 . THR A  1 186 ? 47.469  72.227 18.609 1.00 25.13 ? 186  THR A CG2 1 
ATOM   1273  N  N   . TRP A  1 187 ? 44.778  75.052 16.362 1.00 28.78 ? 187  TRP A N   1 
ATOM   1274  C  CA  . TRP A  1 187 ? 43.586  75.836 16.033 1.00 29.84 ? 187  TRP A CA  1 
ATOM   1275  C  C   . TRP A  1 187 ? 42.410  74.946 15.665 1.00 29.21 ? 187  TRP A C   1 
ATOM   1276  O  O   . TRP A  1 187 ? 41.376  75.446 15.247 1.00 28.85 ? 187  TRP A O   1 
ATOM   1277  C  CB  . TRP A  1 187 ? 43.880  76.774 14.844 1.00 30.29 ? 187  TRP A CB  1 
ATOM   1278  C  CG  . TRP A  1 187 ? 45.007  77.715 15.071 1.00 30.88 ? 187  TRP A CG  1 
ATOM   1279  C  CD1 . TRP A  1 187 ? 46.337  77.403 15.137 1.00 31.53 ? 187  TRP A CD1 1 
ATOM   1280  C  CD2 . TRP A  1 187 ? 44.913  79.124 15.309 1.00 32.21 ? 187  TRP A CD2 1 
ATOM   1281  N  NE1 . TRP A  1 187 ? 47.079  78.530 15.408 1.00 32.87 ? 187  TRP A NE1 1 
ATOM   1282  C  CE2 . TRP A  1 187 ? 46.232  79.601 15.518 1.00 32.16 ? 187  TRP A CE2 1 
ATOM   1283  C  CE3 . TRP A  1 187 ? 43.844  80.032 15.367 1.00 31.95 ? 187  TRP A CE3 1 
ATOM   1284  C  CZ2 . TRP A  1 187 ? 46.511  80.948 15.781 1.00 33.41 ? 187  TRP A CZ2 1 
ATOM   1285  C  CZ3 . TRP A  1 187 ? 44.118  81.371 15.628 1.00 33.44 ? 187  TRP A CZ3 1 
ATOM   1286  C  CH2 . TRP A  1 187 ? 45.446  81.818 15.832 1.00 34.13 ? 187  TRP A CH2 1 
ATOM   1287  N  N   . THR A  1 188 ? 42.581  73.635 15.813 1.00 29.91 ? 188  THR A N   1 
ATOM   1288  C  CA  . THR A  1 188 ? 41.542  72.666 15.470 1.00 29.52 ? 188  THR A CA  1 
ATOM   1289  C  C   . THR A  1 188 ? 40.635  72.223 16.628 1.00 30.53 ? 188  THR A C   1 
ATOM   1290  O  O   . THR A  1 188 ? 39.698  71.453 16.415 1.00 30.96 ? 188  THR A O   1 
ATOM   1291  C  CB  . THR A  1 188 ? 42.172  71.394 14.857 1.00 29.92 ? 188  THR A CB  1 
ATOM   1292  O  OG1 . THR A  1 188 ? 43.244  70.942 15.702 1.00 28.14 ? 188  THR A OG1 1 
ATOM   1293  C  CG2 . THR A  1 188 ? 42.703  71.677 13.447 1.00 28.26 ? 188  THR A CG2 1 
ATOM   1294  N  N   . GLY A  1 189 ? 40.910  72.703 17.837 1.00 31.23 ? 189  GLY A N   1 
ATOM   1295  C  CA  . GLY A  1 189 ? 40.108  72.331 18.997 1.00 31.68 ? 189  GLY A CA  1 
ATOM   1296  C  C   . GLY A  1 189 ? 38.594  72.469 18.860 1.00 32.12 ? 189  GLY A C   1 
ATOM   1297  O  O   . GLY A  1 189 ? 38.092  73.542 18.519 1.00 31.73 ? 189  GLY A O   1 
ATOM   1298  N  N   . LYS A  1 190 ? 37.860  71.393 19.153 1.00 31.81 ? 190  LYS A N   1 
ATOM   1299  C  CA  . LYS A  1 190 ? 36.397  71.407 19.046 1.00 31.62 ? 190  LYS A CA  1 
ATOM   1300  C  C   . LYS A  1 190 ? 35.714  70.523 20.092 1.00 31.04 ? 190  LYS A C   1 
ATOM   1301  O  O   . LYS A  1 190 ? 35.865  69.302 20.082 1.00 30.99 ? 190  LYS A O   1 
ATOM   1302  C  CB  . LYS A  1 190 ? 35.992  70.966 17.635 1.00 32.77 ? 190  LYS A CB  1 
ATOM   1303  C  CG  . LYS A  1 190 ? 34.500  71.071 17.315 1.00 34.10 ? 190  LYS A CG  1 
ATOM   1304  C  CD  . LYS A  1 190 ? 34.306  71.007 15.795 1.00 36.42 ? 190  LYS A CD  1 
ATOM   1305  C  CE  . LYS A  1 190 ? 32.841  71.033 15.403 1.00 38.21 ? 190  LYS A CE  1 
ATOM   1306  N  NZ  . LYS A  1 190 ? 32.155  72.224 15.985 1.00 39.99 ? 190  LYS A NZ  1 
ATOM   1307  N  N   . GLU A  1 191 ? 34.951  71.145 20.985 1.00 30.98 ? 191  GLU A N   1 
ATOM   1308  C  CA  . GLU A  1 191 ? 34.257  70.415 22.048 1.00 30.31 ? 191  GLU A CA  1 
ATOM   1309  C  C   . GLU A  1 191 ? 33.700  69.072 21.586 1.00 28.65 ? 191  GLU A C   1 
ATOM   1310  O  O   . GLU A  1 191 ? 33.035  68.997 20.551 1.00 27.40 ? 191  GLU A O   1 
ATOM   1311  C  CB  . GLU A  1 191 ? 33.106  71.246 22.615 1.00 31.97 ? 191  GLU A CB  1 
ATOM   1312  C  CG  . GLU A  1 191 ? 32.682  70.790 23.998 1.00 35.77 ? 191  GLU A CG  1 
ATOM   1313  C  CD  . GLU A  1 191 ? 31.395  71.423 24.438 1.00 39.69 ? 191  GLU A CD  1 
ATOM   1314  O  OE1 . GLU A  1 191 ? 31.120  72.565 23.988 1.00 40.97 ? 191  GLU A OE1 1 
ATOM   1315  O  OE2 . GLU A  1 191 ? 30.653  70.793 25.242 1.00 41.81 ? 191  GLU A OE2 1 
ATOM   1316  N  N   . ASP A  1 192 ? 33.995  68.031 22.367 1.00 26.89 ? 192  ASP A N   1 
ATOM   1317  C  CA  . ASP A  1 192 ? 33.557  66.666 22.111 1.00 26.47 ? 192  ASP A CA  1 
ATOM   1318  C  C   . ASP A  1 192 ? 33.957  66.123 20.757 1.00 26.14 ? 192  ASP A C   1 
ATOM   1319  O  O   . ASP A  1 192 ? 33.441  65.088 20.341 1.00 25.87 ? 192  ASP A O   1 
ATOM   1320  C  CB  . ASP A  1 192 ? 32.027  66.521 22.226 1.00 28.27 ? 192  ASP A CB  1 
ATOM   1321  C  CG  . ASP A  1 192 ? 31.493  66.973 23.566 1.00 31.30 ? 192  ASP A CG  1 
ATOM   1322  O  OD1 . ASP A  1 192 ? 32.197  66.810 24.586 1.00 33.63 ? 192  ASP A OD1 1 
ATOM   1323  O  OD2 . ASP A  1 192 ? 30.353  67.479 23.606 1.00 34.64 ? 192  ASP A OD2 1 
ATOM   1324  N  N   . ILE A  1 193 ? 34.854  66.800 20.050 1.00 25.34 ? 193  ILE A N   1 
ATOM   1325  C  CA  . ILE A  1 193 ? 35.239  66.304 18.733 1.00 26.18 ? 193  ILE A CA  1 
ATOM   1326  C  C   . ILE A  1 193 ? 36.759  66.232 18.549 1.00 25.95 ? 193  ILE A C   1 
ATOM   1327  O  O   . ILE A  1 193 ? 37.287  65.151 18.271 1.00 25.72 ? 193  ILE A O   1 
ATOM   1328  C  CB  . ILE A  1 193 ? 34.617  67.178 17.611 1.00 28.08 ? 193  ILE A CB  1 
ATOM   1329  C  CG1 . ILE A  1 193 ? 33.088  67.242 17.781 1.00 30.26 ? 193  ILE A CG1 1 
ATOM   1330  C  CG2 . ILE A  1 193 ? 34.938  66.574 16.237 1.00 28.18 ? 193  ILE A CG2 1 
ATOM   1331  C  CD1 . ILE A  1 193 ? 32.351  65.932 17.412 1.00 31.75 ? 193  ILE A CD1 1 
ATOM   1332  N  N   . ILE A  1 194 ? 37.450  67.370 18.686 1.00 24.07 ? 194  ILE A N   1 
ATOM   1333  C  CA  . ILE A  1 194 ? 38.904  67.411 18.544 1.00 23.54 ? 194  ILE A CA  1 
ATOM   1334  C  C   . ILE A  1 194 ? 39.573  67.832 19.847 1.00 22.42 ? 194  ILE A C   1 
ATOM   1335  O  O   . ILE A  1 194 ? 39.299  68.901 20.383 1.00 22.01 ? 194  ILE A O   1 
ATOM   1336  C  CB  . ILE A  1 194 ? 39.359  68.397 17.434 1.00 25.18 ? 194  ILE A CB  1 
ATOM   1337  C  CG1 . ILE A  1 194 ? 38.658  68.072 16.116 1.00 24.35 ? 194  ILE A CG1 1 
ATOM   1338  C  CG2 . ILE A  1 194 ? 40.885  68.316 17.258 1.00 24.26 ? 194  ILE A CG2 1 
ATOM   1339  C  CD1 . ILE A  1 194 ? 38.980  66.706 15.564 1.00 25.62 ? 194  ILE A CD1 1 
ATOM   1340  N  N   . TYR A  1 195 ? 40.467  66.986 20.346 1.00 22.33 ? 195  TYR A N   1 
ATOM   1341  C  CA  . TYR A  1 195 ? 41.160  67.257 21.603 1.00 21.93 ? 195  TYR A CA  1 
ATOM   1342  C  C   . TYR A  1 195 ? 42.661  67.433 21.391 1.00 22.49 ? 195  TYR A C   1 
ATOM   1343  O  O   . TYR A  1 195 ? 43.354  66.472 21.054 1.00 23.16 ? 195  TYR A O   1 
ATOM   1344  C  CB  . TYR A  1 195 ? 40.961  66.091 22.583 1.00 22.48 ? 195  TYR A CB  1 
ATOM   1345  C  CG  . TYR A  1 195 ? 39.514  65.703 22.898 1.00 22.26 ? 195  TYR A CG  1 
ATOM   1346  C  CD1 . TYR A  1 195 ? 38.716  65.082 21.946 1.00 21.78 ? 195  TYR A CD1 1 
ATOM   1347  C  CD2 . TYR A  1 195 ? 38.977  65.911 24.176 1.00 21.59 ? 195  TYR A CD2 1 
ATOM   1348  C  CE1 . TYR A  1 195 ? 37.419  64.671 22.249 1.00 23.18 ? 195  TYR A CE1 1 
ATOM   1349  C  CE2 . TYR A  1 195 ? 37.686  65.504 24.496 1.00 21.80 ? 195  TYR A CE2 1 
ATOM   1350  C  CZ  . TYR A  1 195 ? 36.910  64.884 23.525 1.00 23.37 ? 195  TYR A CZ  1 
ATOM   1351  O  OH  . TYR A  1 195 ? 35.628  64.489 23.825 1.00 23.41 ? 195  TYR A OH  1 
ATOM   1352  N  N   . ASN A  1 196 ? 43.170  68.644 21.592 1.00 22.27 ? 196  ASN A N   1 
ATOM   1353  C  CA  . ASN A  1 196 ? 44.604  68.888 21.448 1.00 21.78 ? 196  ASN A CA  1 
ATOM   1354  C  C   . ASN A  1 196 ? 45.253  69.063 22.817 1.00 20.97 ? 196  ASN A C   1 
ATOM   1355  O  O   . ASN A  1 196 ? 44.945  70.013 23.531 1.00 21.10 ? 196  ASN A O   1 
ATOM   1356  C  CB  . ASN A  1 196 ? 44.881  70.162 20.631 1.00 21.46 ? 196  ASN A CB  1 
ATOM   1357  C  CG  . ASN A  1 196 ? 44.379  70.064 19.216 1.00 21.67 ? 196  ASN A CG  1 
ATOM   1358  O  OD1 . ASN A  1 196 ? 44.832  69.232 18.441 1.00 24.61 ? 196  ASN A OD1 1 
ATOM   1359  N  ND2 . ASN A  1 196 ? 43.435  70.913 18.872 1.00 21.23 ? 196  ASN A ND2 1 
ATOM   1360  N  N   . GLY A  1 197 ? 46.171  68.173 23.176 1.00 20.62 ? 197  GLY A N   1 
ATOM   1361  C  CA  . GLY A  1 197 ? 46.839  68.322 24.458 1.00 20.14 ? 197  GLY A CA  1 
ATOM   1362  C  C   . GLY A  1 197 ? 46.115  67.776 25.685 1.00 20.39 ? 197  GLY A C   1 
ATOM   1363  O  O   . GLY A  1 197 ? 46.675  67.834 26.785 1.00 20.96 ? 197  GLY A O   1 
ATOM   1364  N  N   . ILE A  1 198 ? 44.882  67.295 25.508 1.00 19.21 ? 198  ILE A N   1 
ATOM   1365  C  CA  . ILE A  1 198 ? 44.078  66.686 26.580 1.00 19.72 ? 198  ILE A CA  1 
ATOM   1366  C  C   . ILE A  1 198 ? 43.458  65.416 26.016 1.00 19.53 ? 198  ILE A C   1 
ATOM   1367  O  O   . ILE A  1 198 ? 43.326  65.261 24.799 1.00 19.22 ? 198  ILE A O   1 
ATOM   1368  C  CB  . ILE A  1 198 ? 42.925  67.594 27.109 1.00 19.38 ? 198  ILE A CB  1 
ATOM   1369  C  CG1 . ILE A  1 198 ? 42.033  68.074 25.949 1.00 19.17 ? 198  ILE A CG1 1 
ATOM   1370  C  CG2 . ILE A  1 198 ? 43.504  68.753 27.918 1.00 18.40 ? 198  ILE A CG2 1 
ATOM   1371  C  CD1 . ILE A  1 198 ? 40.935  69.047 26.386 1.00 18.02 ? 198  ILE A CD1 1 
ATOM   1372  N  N   . THR A  1 199 ? 43.087  64.505 26.902 1.00 18.44 ? 199  THR A N   1 
ATOM   1373  C  CA  . THR A  1 199 ? 42.519  63.234 26.495 1.00 18.48 ? 199  THR A CA  1 
ATOM   1374  C  C   . THR A  1 199 ? 40.986  63.276 26.461 1.00 19.70 ? 199  THR A C   1 
ATOM   1375  O  O   . THR A  1 199 ? 40.366  64.098 27.137 1.00 19.30 ? 199  THR A O   1 
ATOM   1376  C  CB  . THR A  1 199 ? 42.942  62.153 27.498 1.00 19.65 ? 199  THR A CB  1 
ATOM   1377  O  OG1 . THR A  1 199 ? 42.566  62.586 28.822 1.00 18.83 ? 199  THR A OG1 1 
ATOM   1378  C  CG2 . THR A  1 199 ? 44.492  61.925 27.450 1.00 16.97 ? 199  THR A CG2 1 
ATOM   1379  N  N   . ASP A  1 200 ? 40.384  62.416 25.643 1.00 19.99 ? 200  ASP A N   1 
ATOM   1380  C  CA  . ASP A  1 200 ? 38.931  62.320 25.595 1.00 20.39 ? 200  ASP A CA  1 
ATOM   1381  C  C   . ASP A  1 200 ? 38.580  61.384 26.769 1.00 21.29 ? 200  ASP A C   1 
ATOM   1382  O  O   . ASP A  1 200 ? 39.482  60.951 27.511 1.00 19.94 ? 200  ASP A O   1 
ATOM   1383  C  CB  . ASP A  1 200 ? 38.461  61.732 24.272 1.00 20.17 ? 200  ASP A CB  1 
ATOM   1384  C  CG  . ASP A  1 200 ? 38.864  60.288 24.086 1.00 20.68 ? 200  ASP A CG  1 
ATOM   1385  O  OD1 . ASP A  1 200 ? 39.697  59.764 24.866 1.00 20.02 ? 200  ASP A OD1 1 
ATOM   1386  O  OD2 . ASP A  1 200 ? 38.345  59.668 23.128 1.00 21.22 ? 200  ASP A OD2 1 
ATOM   1387  N  N   . TRP A  1 201 ? 37.302  61.060 26.931 1.00 19.73 ? 201  TRP A N   1 
ATOM   1388  C  CA  . TRP A  1 201 ? 36.878  60.230 28.059 1.00 20.53 ? 201  TRP A CA  1 
ATOM   1389  C  C   . TRP A  1 201 ? 37.629  58.917 28.248 1.00 19.81 ? 201  TRP A C   1 
ATOM   1390  O  O   . TRP A  1 201 ? 38.175  58.665 29.319 1.00 20.51 ? 201  TRP A O   1 
ATOM   1391  C  CB  . TRP A  1 201 ? 35.369  59.911 27.994 1.00 18.94 ? 201  TRP A CB  1 
ATOM   1392  C  CG  . TRP A  1 201 ? 34.874  59.326 29.301 1.00 18.58 ? 201  TRP A CG  1 
ATOM   1393  C  CD1 . TRP A  1 201 ? 34.319  60.018 30.348 1.00 17.70 ? 201  TRP A CD1 1 
ATOM   1394  C  CD2 . TRP A  1 201 ? 35.003  57.968 29.749 1.00 16.45 ? 201  TRP A CD2 1 
ATOM   1395  N  NE1 . TRP A  1 201 ? 34.107  59.186 31.411 1.00 17.67 ? 201  TRP A NE1 1 
ATOM   1396  C  CE2 . TRP A  1 201 ? 34.514  57.920 31.075 1.00 18.36 ? 201  TRP A CE2 1 
ATOM   1397  C  CE3 . TRP A  1 201 ? 35.484  56.791 29.163 1.00 18.02 ? 201  TRP A CE3 1 
ATOM   1398  C  CZ2 . TRP A  1 201 ? 34.493  56.727 31.834 1.00 18.06 ? 201  TRP A CZ2 1 
ATOM   1399  C  CZ3 . TRP A  1 201 ? 35.467  55.600 29.913 1.00 17.23 ? 201  TRP A CZ3 1 
ATOM   1400  C  CH2 . TRP A  1 201 ? 34.974  55.581 31.235 1.00 17.22 ? 201  TRP A CH2 1 
ATOM   1401  N  N   . VAL A  1 202 ? 37.662  58.089 27.208 1.00 20.12 ? 202  VAL A N   1 
ATOM   1402  C  CA  . VAL A  1 202 ? 38.281  56.777 27.323 1.00 18.15 ? 202  VAL A CA  1 
ATOM   1403  C  C   . VAL A  1 202 ? 39.800  56.811 27.510 1.00 19.06 ? 202  VAL A C   1 
ATOM   1404  O  O   . VAL A  1 202 ? 40.370  56.019 28.279 1.00 19.53 ? 202  VAL A O   1 
ATOM   1405  C  CB  . VAL A  1 202 ? 37.854  55.883 26.117 1.00 18.59 ? 202  VAL A CB  1 
ATOM   1406  C  CG1 . VAL A  1 202 ? 38.621  56.268 24.849 1.00 16.98 ? 202  VAL A CG1 1 
ATOM   1407  C  CG2 . VAL A  1 202 ? 38.010  54.396 26.482 1.00 16.16 ? 202  VAL A CG2 1 
ATOM   1408  N  N   . TYR A  1 203 ? 40.471  57.745 26.852 1.00 17.18 ? 203  TYR A N   1 
ATOM   1409  C  CA  . TYR A  1 203 ? 41.913  57.834 27.017 1.00 16.45 ? 203  TYR A CA  1 
ATOM   1410  C  C   . TYR A  1 203 ? 42.257  58.372 28.424 1.00 16.54 ? 203  TYR A C   1 
ATOM   1411  O  O   . TYR A  1 203 ? 43.299  58.052 28.980 1.00 16.46 ? 203  TYR A O   1 
ATOM   1412  C  CB  . TYR A  1 203 ? 42.505  58.739 25.935 1.00 15.93 ? 203  TYR A CB  1 
ATOM   1413  C  CG  . TYR A  1 203 ? 43.031  58.003 24.718 1.00 16.21 ? 203  TYR A CG  1 
ATOM   1414  C  CD1 . TYR A  1 203 ? 42.253  57.833 23.572 1.00 16.43 ? 203  TYR A CD1 1 
ATOM   1415  C  CD2 . TYR A  1 203 ? 44.332  57.495 24.708 1.00 18.45 ? 203  TYR A CD2 1 
ATOM   1416  C  CE1 . TYR A  1 203 ? 42.767  57.186 22.442 1.00 17.29 ? 203  TYR A CE1 1 
ATOM   1417  C  CE2 . TYR A  1 203 ? 44.849  56.843 23.592 1.00 19.15 ? 203  TYR A CE2 1 
ATOM   1418  C  CZ  . TYR A  1 203 ? 44.067  56.699 22.459 1.00 19.58 ? 203  TYR A CZ  1 
ATOM   1419  O  OH  . TYR A  1 203 ? 44.626  56.116 21.342 1.00 20.20 ? 203  TYR A OH  1 
ATOM   1420  N  N   . GLU A  1 204 ? 41.376  59.185 28.996 1.00 16.50 ? 204  GLU A N   1 
ATOM   1421  C  CA  . GLU A  1 204 ? 41.612  59.737 30.318 1.00 16.52 ? 204  GLU A CA  1 
ATOM   1422  C  C   . GLU A  1 204 ? 41.493  58.604 31.348 1.00 16.42 ? 204  GLU A C   1 
ATOM   1423  O  O   . GLU A  1 204 ? 42.368  58.392 32.178 1.00 15.61 ? 204  GLU A O   1 
ATOM   1424  C  CB  . GLU A  1 204 ? 40.573  60.819 30.649 1.00 15.84 ? 204  GLU A CB  1 
ATOM   1425  C  CG  . GLU A  1 204 ? 40.746  61.383 32.062 1.00 16.84 ? 204  GLU A CG  1 
ATOM   1426  C  CD  . GLU A  1 204 ? 39.576  62.227 32.547 1.00 17.65 ? 204  GLU A CD  1 
ATOM   1427  O  OE1 . GLU A  1 204 ? 38.961  62.950 31.727 1.00 18.50 ? 204  GLU A OE1 1 
ATOM   1428  O  OE2 . GLU A  1 204 ? 39.299  62.198 33.769 1.00 18.09 ? 204  GLU A OE2 1 
ATOM   1429  N  N   . GLU A  1 205 ? 40.391  57.877 31.251 1.00 16.63 ? 205  GLU A N   1 
ATOM   1430  C  CA  . GLU A  1 205 ? 40.074  56.795 32.172 1.00 18.21 ? 205  GLU A CA  1 
ATOM   1431  C  C   . GLU A  1 205 ? 40.951  55.546 32.038 1.00 18.39 ? 205  GLU A C   1 
ATOM   1432  O  O   . GLU A  1 205 ? 41.583  55.127 33.010 1.00 18.17 ? 205  GLU A O   1 
ATOM   1433  C  CB  . GLU A  1 205 ? 38.589  56.417 31.991 1.00 16.86 ? 205  GLU A CB  1 
ATOM   1434  C  CG  . GLU A  1 205 ? 38.058  55.279 32.840 1.00 18.62 ? 205  GLU A CG  1 
ATOM   1435  C  CD  . GLU A  1 205 ? 38.271  55.482 34.340 1.00 19.97 ? 205  GLU A CD  1 
ATOM   1436  O  OE1 . GLU A  1 205 ? 38.320  56.637 34.813 1.00 21.27 ? 205  GLU A OE1 1 
ATOM   1437  O  OE2 . GLU A  1 205 ? 38.380  54.469 35.047 1.00 20.67 ? 205  GLU A OE2 1 
ATOM   1438  N  N   . GLU A  1 206 ? 41.037  55.015 30.820 1.00 16.96 ? 206  GLU A N   1 
ATOM   1439  C  CA  . GLU A  1 206 ? 41.729  53.754 30.548 1.00 17.06 ? 206  GLU A CA  1 
ATOM   1440  C  C   . GLU A  1 206 ? 43.190  53.680 30.106 1.00 17.31 ? 206  GLU A C   1 
ATOM   1441  O  O   . GLU A  1 206 ? 43.810  52.643 30.260 1.00 16.29 ? 206  GLU A O   1 
ATOM   1442  C  CB  . GLU A  1 206 ? 40.903  52.990 29.516 1.00 16.20 ? 206  GLU A CB  1 
ATOM   1443  C  CG  . GLU A  1 206 ? 39.412  53.029 29.801 1.00 15.61 ? 206  GLU A CG  1 
ATOM   1444  C  CD  . GLU A  1 206 ? 39.015  52.164 31.002 1.00 16.80 ? 206  GLU A CD  1 
ATOM   1445  O  OE1 . GLU A  1 206 ? 39.902  51.652 31.721 1.00 15.69 ? 206  GLU A OE1 1 
ATOM   1446  O  OE2 . GLU A  1 206 ? 37.808  52.014 31.222 1.00 16.63 ? 206  GLU A OE2 1 
ATOM   1447  N  N   . VAL A  1 207 ? 43.744  54.758 29.562 1.00 18.46 ? 207  VAL A N   1 
ATOM   1448  C  CA  . VAL A  1 207 ? 45.111  54.702 29.063 1.00 18.06 ? 207  VAL A CA  1 
ATOM   1449  C  C   . VAL A  1 207 ? 46.118  55.532 29.843 1.00 19.46 ? 207  VAL A C   1 
ATOM   1450  O  O   . VAL A  1 207 ? 47.053  54.990 30.424 1.00 21.17 ? 207  VAL A O   1 
ATOM   1451  C  CB  . VAL A  1 207 ? 45.132  55.115 27.571 1.00 17.64 ? 207  VAL A CB  1 
ATOM   1452  C  CG1 . VAL A  1 207 ? 46.558  55.042 27.000 1.00 14.23 ? 207  VAL A CG1 1 
ATOM   1453  C  CG2 . VAL A  1 207 ? 44.204  54.218 26.803 1.00 13.34 ? 207  VAL A CG2 1 
ATOM   1454  N  N   . PHE A  1 208 ? 45.925  56.844 29.878 1.00 18.82 ? 208  PHE A N   1 
ATOM   1455  C  CA  . PHE A  1 208 ? 46.859  57.712 30.591 1.00 18.25 ? 208  PHE A CA  1 
ATOM   1456  C  C   . PHE A  1 208 ? 46.540  58.027 32.049 1.00 18.31 ? 208  PHE A C   1 
ATOM   1457  O  O   . PHE A  1 208 ? 47.414  58.510 32.766 1.00 19.10 ? 208  PHE A O   1 
ATOM   1458  C  CB  . PHE A  1 208 ? 47.032  59.011 29.796 1.00 18.01 ? 208  PHE A CB  1 
ATOM   1459  C  CG  . PHE A  1 208 ? 47.679  58.799 28.459 1.00 18.44 ? 208  PHE A CG  1 
ATOM   1460  C  CD1 . PHE A  1 208 ? 49.034  58.486 28.374 1.00 19.08 ? 208  PHE A CD1 1 
ATOM   1461  C  CD2 . PHE A  1 208 ? 46.923  58.829 27.287 1.00 19.18 ? 208  PHE A CD2 1 
ATOM   1462  C  CE1 . PHE A  1 208 ? 49.625  58.197 27.130 1.00 21.19 ? 208  PHE A CE1 1 
ATOM   1463  C  CE2 . PHE A  1 208 ? 47.505  58.540 26.029 1.00 19.26 ? 208  PHE A CE2 1 
ATOM   1464  C  CZ  . PHE A  1 208 ? 48.849  58.224 25.953 1.00 18.88 ? 208  PHE A CZ  1 
ATOM   1465  N  N   . SER A  1 209 ? 45.312  57.749 32.497 1.00 18.76 ? 209  SER A N   1 
ATOM   1466  C  CA  . SER A  1 209 ? 44.921  58.039 33.880 1.00 18.47 ? 209  SER A CA  1 
ATOM   1467  C  C   . SER A  1 209 ? 45.236  59.495 34.166 1.00 19.18 ? 209  SER A C   1 
ATOM   1468  O  O   . SER A  1 209 ? 45.754  59.835 35.228 1.00 20.11 ? 209  SER A O   1 
ATOM   1469  C  CB  . SER A  1 209 ? 45.701  57.158 34.858 1.00 17.03 ? 209  SER A CB  1 
ATOM   1470  O  OG  . SER A  1 209 ? 45.334  55.804 34.692 1.00 20.56 ? 209  SER A OG  1 
ATOM   1471  N  N   . ALA A  1 210 ? 44.912  60.352 33.205 1.00 18.33 ? 210  ALA A N   1 
ATOM   1472  C  CA  . ALA A  1 210 ? 45.192  61.775 33.320 1.00 18.26 ? 210  ALA A CA  1 
ATOM   1473  C  C   . ALA A  1 210 ? 44.464  62.494 32.196 1.00 18.29 ? 210  ALA A C   1 
ATOM   1474  O  O   . ALA A  1 210 ? 44.176  61.911 31.154 1.00 17.98 ? 210  ALA A O   1 
ATOM   1475  C  CB  . ALA A  1 210 ? 46.733  62.025 33.212 1.00 15.71 ? 210  ALA A CB  1 
ATOM   1476  N  N   . TYR A  1 211 ? 44.186  63.770 32.409 1.00 19.15 ? 211  TYR A N   1 
ATOM   1477  C  CA  . TYR A  1 211 ? 43.490  64.584 31.425 1.00 19.05 ? 211  TYR A CA  1 
ATOM   1478  C  C   . TYR A  1 211 ? 44.492  65.131 30.425 1.00 19.87 ? 211  TYR A C   1 
ATOM   1479  O  O   . TYR A  1 211 ? 44.168  65.351 29.255 1.00 21.19 ? 211  TYR A O   1 
ATOM   1480  C  CB  . TYR A  1 211 ? 42.792  65.730 32.148 1.00 17.74 ? 211  TYR A CB  1 
ATOM   1481  C  CG  . TYR A  1 211 ? 41.810  66.562 31.327 1.00 18.44 ? 211  TYR A CG  1 
ATOM   1482  C  CD1 . TYR A  1 211 ? 41.112  66.020 30.252 1.00 17.06 ? 211  TYR A CD1 1 
ATOM   1483  C  CD2 . TYR A  1 211 ? 41.494  67.860 31.727 1.00 16.08 ? 211  TYR A CD2 1 
ATOM   1484  C  CE1 . TYR A  1 211 ? 40.110  66.753 29.607 1.00 18.08 ? 211  TYR A CE1 1 
ATOM   1485  C  CE2 . TYR A  1 211 ? 40.509  68.590 31.096 1.00 17.59 ? 211  TYR A CE2 1 
ATOM   1486  C  CZ  . TYR A  1 211 ? 39.820  68.031 30.048 1.00 17.11 ? 211  TYR A CZ  1 
ATOM   1487  O  OH  . TYR A  1 211 ? 38.813  68.757 29.497 1.00 17.59 ? 211  TYR A OH  1 
ATOM   1488  N  N   . SER A  1 212 ? 45.723  65.320 30.878 1.00 19.89 ? 212  SER A N   1 
ATOM   1489  C  CA  . SER A  1 212 ? 46.742  65.881 30.007 1.00 21.38 ? 212  SER A CA  1 
ATOM   1490  C  C   . SER A  1 212 ? 47.281  64.901 28.998 1.00 21.98 ? 212  SER A C   1 
ATOM   1491  O  O   . SER A  1 212 ? 47.386  63.704 29.263 1.00 21.25 ? 212  SER A O   1 
ATOM   1492  C  CB  . SER A  1 212 ? 47.914  66.430 30.821 1.00 21.96 ? 212  SER A CB  1 
ATOM   1493  O  OG  . SER A  1 212 ? 48.656  65.391 31.414 1.00 25.29 ? 212  SER A OG  1 
ATOM   1494  N  N   . ALA A  1 213 ? 47.604  65.444 27.830 1.00 21.67 ? 213  ALA A N   1 
ATOM   1495  C  CA  . ALA A  1 213 ? 48.203  64.698 26.742 1.00 21.98 ? 213  ALA A CA  1 
ATOM   1496  C  C   . ALA A  1 213 ? 49.317  65.630 26.225 1.00 22.86 ? 213  ALA A C   1 
ATOM   1497  O  O   . ALA A  1 213 ? 49.484  65.841 25.019 1.00 22.30 ? 213  ALA A O   1 
ATOM   1498  C  CB  . ALA A  1 213 ? 47.171  64.412 25.653 1.00 21.28 ? 213  ALA A CB  1 
ATOM   1499  N  N   . LEU A  1 214 ? 50.047  66.204 27.180 1.00 23.08 ? 214  LEU A N   1 
ATOM   1500  C  CA  . LEU A  1 214 ? 51.170  67.115 26.927 1.00 24.14 ? 214  LEU A CA  1 
ATOM   1501  C  C   . LEU A  1 214 ? 52.431  66.553 27.584 1.00 24.48 ? 214  LEU A C   1 
ATOM   1502  O  O   . LEU A  1 214 ? 52.394  66.143 28.748 1.00 24.94 ? 214  LEU A O   1 
ATOM   1503  C  CB  . LEU A  1 214 ? 50.901  68.497 27.535 1.00 23.65 ? 214  LEU A CB  1 
ATOM   1504  C  CG  . LEU A  1 214 ? 49.842  69.351 26.878 1.00 24.42 ? 214  LEU A CG  1 
ATOM   1505  C  CD1 . LEU A  1 214 ? 49.846  70.720 27.519 1.00 24.32 ? 214  LEU A CD1 1 
ATOM   1506  C  CD2 . LEU A  1 214 ? 50.138  69.455 25.396 1.00 25.02 ? 214  LEU A CD2 1 
ATOM   1507  N  N   . TRP A  1 215 ? 53.546  66.574 26.857 1.00 24.29 ? 215  TRP A N   1 
ATOM   1508  C  CA  . TRP A  1 215 ? 54.804  66.052 27.377 1.00 23.74 ? 215  TRP A CA  1 
ATOM   1509  C  C   . TRP A  1 215 ? 55.995  66.925 26.989 1.00 24.15 ? 215  TRP A C   1 
ATOM   1510  O  O   . TRP A  1 215 ? 56.469  66.887 25.846 1.00 23.01 ? 215  TRP A O   1 
ATOM   1511  C  CB  . TRP A  1 215 ? 55.040  64.638 26.848 1.00 22.85 ? 215  TRP A CB  1 
ATOM   1512  C  CG  . TRP A  1 215 ? 53.974  63.658 27.235 1.00 24.10 ? 215  TRP A CG  1 
ATOM   1513  C  CD1 . TRP A  1 215 ? 53.918  62.908 28.384 1.00 23.73 ? 215  TRP A CD1 1 
ATOM   1514  C  CD2 . TRP A  1 215 ? 52.816  63.301 26.471 1.00 22.37 ? 215  TRP A CD2 1 
ATOM   1515  N  NE1 . TRP A  1 215 ? 52.805  62.109 28.370 1.00 23.78 ? 215  TRP A NE1 1 
ATOM   1516  C  CE2 . TRP A  1 215 ? 52.109  62.333 27.211 1.00 23.07 ? 215  TRP A CE2 1 
ATOM   1517  C  CE3 . TRP A  1 215 ? 52.308  63.707 25.234 1.00 23.74 ? 215  TRP A CE3 1 
ATOM   1518  C  CZ2 . TRP A  1 215 ? 50.914  61.765 26.754 1.00 23.30 ? 215  TRP A CZ2 1 
ATOM   1519  C  CZ3 . TRP A  1 215 ? 51.122  63.148 24.774 1.00 23.68 ? 215  TRP A CZ3 1 
ATOM   1520  C  CH2 . TRP A  1 215 ? 50.435  62.186 25.533 1.00 24.33 ? 215  TRP A CH2 1 
ATOM   1521  N  N   . TRP A  1 216 ? 56.469  67.702 27.955 1.00 24.14 ? 216  TRP A N   1 
ATOM   1522  C  CA  . TRP A  1 216 ? 57.618  68.567 27.772 1.00 24.48 ? 216  TRP A CA  1 
ATOM   1523  C  C   . TRP A  1 216 ? 58.887  67.722 27.671 1.00 24.84 ? 216  TRP A C   1 
ATOM   1524  O  O   . TRP A  1 216 ? 59.020  66.703 28.356 1.00 23.87 ? 216  TRP A O   1 
ATOM   1525  C  CB  . TRP A  1 216 ? 57.793  69.489 28.982 1.00 24.45 ? 216  TRP A CB  1 
ATOM   1526  C  CG  . TRP A  1 216 ? 56.904  70.687 29.079 1.00 26.81 ? 216  TRP A CG  1 
ATOM   1527  C  CD1 . TRP A  1 216 ? 55.888  70.880 29.972 1.00 26.86 ? 216  TRP A CD1 1 
ATOM   1528  C  CD2 . TRP A  1 216 ? 57.052  71.924 28.370 1.00 26.40 ? 216  TRP A CD2 1 
ATOM   1529  N  NE1 . TRP A  1 216 ? 55.409  72.159 29.873 1.00 26.78 ? 216  TRP A NE1 1 
ATOM   1530  C  CE2 . TRP A  1 216 ? 56.106  72.824 28.900 1.00 27.61 ? 216  TRP A CE2 1 
ATOM   1531  C  CE3 . TRP A  1 216 ? 57.899  72.360 27.345 1.00 26.83 ? 216  TRP A CE3 1 
ATOM   1532  C  CZ2 . TRP A  1 216 ? 55.983  74.147 28.443 1.00 27.30 ? 216  TRP A CZ2 1 
ATOM   1533  C  CZ3 . TRP A  1 216 ? 57.781  73.666 26.889 1.00 26.49 ? 216  TRP A CZ3 1 
ATOM   1534  C  CH2 . TRP A  1 216 ? 56.827  74.547 27.442 1.00 28.21 ? 216  TRP A CH2 1 
ATOM   1535  N  N   . SER A  1 217 ? 59.827  68.149 26.830 1.00 25.02 ? 217  SER A N   1 
ATOM   1536  C  CA  . SER A  1 217 ? 61.098  67.443 26.723 1.00 24.49 ? 217  SER A CA  1 
ATOM   1537  C  C   . SER A  1 217 ? 61.808  67.781 28.029 1.00 24.40 ? 217  SER A C   1 
ATOM   1538  O  O   . SER A  1 217 ? 61.418  68.715 28.734 1.00 25.14 ? 217  SER A O   1 
ATOM   1539  C  CB  . SER A  1 217 ? 61.902  67.930 25.517 1.00 24.78 ? 217  SER A CB  1 
ATOM   1540  O  OG  . SER A  1 217 ? 62.147  69.315 25.605 1.00 25.69 ? 217  SER A OG  1 
ATOM   1541  N  N   . PRO A  1 218 ? 62.862  67.036 28.370 1.00 25.33 ? 218  PRO A N   1 
ATOM   1542  C  CA  . PRO A  1 218 ? 63.600  67.264 29.616 1.00 26.61 ? 218  PRO A CA  1 
ATOM   1543  C  C   . PRO A  1 218 ? 63.954  68.691 30.013 1.00 28.43 ? 218  PRO A C   1 
ATOM   1544  O  O   . PRO A  1 218 ? 63.769  69.065 31.181 1.00 28.88 ? 218  PRO A O   1 
ATOM   1545  C  CB  . PRO A  1 218 ? 64.827  66.364 29.465 1.00 26.32 ? 218  PRO A CB  1 
ATOM   1546  C  CG  . PRO A  1 218 ? 64.272  65.225 28.657 1.00 26.60 ? 218  PRO A CG  1 
ATOM   1547  C  CD  . PRO A  1 218 ? 63.461  65.933 27.600 1.00 24.41 ? 218  PRO A CD  1 
ATOM   1548  N  N   . ASN A  1 219 ? 64.451  69.493 29.074 1.00 28.32 ? 219  ASN A N   1 
ATOM   1549  C  CA  . ASN A  1 219 ? 64.810  70.870 29.408 1.00 29.90 ? 219  ASN A CA  1 
ATOM   1550  C  C   . ASN A  1 219 ? 63.798  71.936 28.959 1.00 30.10 ? 219  ASN A C   1 
ATOM   1551  O  O   . ASN A  1 219 ? 64.085  73.126 29.040 1.00 29.85 ? 219  ASN A O   1 
ATOM   1552  C  CB  . ASN A  1 219 ? 66.214  71.219 28.868 1.00 30.67 ? 219  ASN A CB  1 
ATOM   1553  C  CG  . ASN A  1 219 ? 66.254  71.336 27.353 1.00 33.01 ? 219  ASN A CG  1 
ATOM   1554  O  OD1 . ASN A  1 219 ? 65.221  71.469 26.692 1.00 30.13 ? 219  ASN A OD1 1 
ATOM   1555  N  ND2 . ASN A  1 219 ? 67.459  71.316 26.795 1.00 35.71 ? 219  ASN A ND2 1 
ATOM   1556  N  N   . GLY A  1 220 ? 62.629  71.511 28.476 1.00 30.49 ? 220  GLY A N   1 
ATOM   1557  C  CA  . GLY A  1 220 ? 61.605  72.460 28.074 1.00 29.75 ? 220  GLY A CA  1 
ATOM   1558  C  C   . GLY A  1 220 ? 61.652  72.955 26.641 1.00 31.05 ? 220  GLY A C   1 
ATOM   1559  O  O   . GLY A  1 220 ? 60.800  73.740 26.208 1.00 31.17 ? 220  GLY A O   1 
ATOM   1560  N  N   . THR A  1 221 ? 62.636  72.507 25.882 1.00 30.54 ? 221  THR A N   1 
ATOM   1561  C  CA  . THR A  1 221 ? 62.737  72.961 24.511 1.00 30.51 ? 221  THR A CA  1 
ATOM   1562  C  C   . THR A  1 221 ? 61.543  72.545 23.671 1.00 30.17 ? 221  THR A C   1 
ATOM   1563  O  O   . THR A  1 221 ? 60.859  73.385 23.076 1.00 30.72 ? 221  THR A O   1 
ATOM   1564  C  CB  . THR A  1 221 ? 64.029  72.443 23.853 1.00 31.09 ? 221  THR A CB  1 
ATOM   1565  O  OG1 . THR A  1 221 ? 65.145  73.128 24.429 1.00 31.18 ? 221  THR A OG1 1 
ATOM   1566  C  CG2 . THR A  1 221 ? 63.998  72.678 22.353 1.00 29.69 ? 221  THR A CG2 1 
ATOM   1567  N  N   . PHE A  1 222 ? 61.298  71.245 23.629 1.00 28.92 ? 222  PHE A N   1 
ATOM   1568  C  CA  . PHE A  1 222 ? 60.204  70.700 22.849 1.00 29.39 ? 222  PHE A CA  1 
ATOM   1569  C  C   . PHE A  1 222 ? 58.951  70.416 23.691 1.00 28.97 ? 222  PHE A C   1 
ATOM   1570  O  O   . PHE A  1 222 ? 59.035  70.135 24.883 1.00 29.47 ? 222  PHE A O   1 
ATOM   1571  C  CB  . PHE A  1 222 ? 60.649  69.402 22.178 1.00 30.04 ? 222  PHE A CB  1 
ATOM   1572  C  CG  . PHE A  1 222 ? 61.751  69.577 21.181 1.00 31.26 ? 222  PHE A CG  1 
ATOM   1573  C  CD1 . PHE A  1 222 ? 61.522  70.263 19.995 1.00 31.06 ? 222  PHE A CD1 1 
ATOM   1574  C  CD2 . PHE A  1 222 ? 63.011  69.016 21.409 1.00 31.76 ? 222  PHE A CD2 1 
ATOM   1575  C  CE1 . PHE A  1 222 ? 62.527  70.389 19.037 1.00 32.92 ? 222  PHE A CE1 1 
ATOM   1576  C  CE2 . PHE A  1 222 ? 64.028  69.135 20.460 1.00 31.94 ? 222  PHE A CE2 1 
ATOM   1577  C  CZ  . PHE A  1 222 ? 63.784  69.824 19.266 1.00 33.00 ? 222  PHE A CZ  1 
ATOM   1578  N  N   . LEU A  1 223 ? 57.794  70.510 23.054 1.00 26.82 ? 223  LEU A N   1 
ATOM   1579  C  CA  . LEU A  1 223 ? 56.545  70.213 23.721 1.00 25.25 ? 223  LEU A CA  1 
ATOM   1580  C  C   . LEU A  1 223 ? 55.861  69.227 22.798 1.00 24.14 ? 223  LEU A C   1 
ATOM   1581  O  O   . LEU A  1 223 ? 55.488  69.573 21.678 1.00 23.42 ? 223  LEU A O   1 
ATOM   1582  C  CB  . LEU A  1 223 ? 55.643  71.452 23.905 1.00 23.94 ? 223  LEU A CB  1 
ATOM   1583  C  CG  . LEU A  1 223 ? 54.235  71.089 24.483 1.00 23.39 ? 223  LEU A CG  1 
ATOM   1584  C  CD1 . LEU A  1 223 ? 54.370  70.680 25.935 1.00 21.08 ? 223  LEU A CD1 1 
ATOM   1585  C  CD2 . LEU A  1 223 ? 53.264  72.254 24.374 1.00 22.20 ? 223  LEU A CD2 1 
ATOM   1586  N  N   . ALA A  1 224 ? 55.753  67.987 23.259 1.00 22.68 ? 224  ALA A N   1 
ATOM   1587  C  CA  . ALA A  1 224 ? 55.092  66.944 22.497 1.00 23.32 ? 224  ALA A CA  1 
ATOM   1588  C  C   . ALA A  1 224 ? 53.635  66.871 22.952 1.00 23.83 ? 224  ALA A C   1 
ATOM   1589  O  O   . ALA A  1 224 ? 53.325  67.139 24.120 1.00 24.17 ? 224  ALA A O   1 
ATOM   1590  C  CB  . ALA A  1 224 ? 55.772  65.613 22.733 1.00 22.46 ? 224  ALA A CB  1 
ATOM   1591  N  N   . TYR A  1 225 ? 52.743  66.507 22.035 1.00 23.81 ? 225  TYR A N   1 
ATOM   1592  C  CA  . TYR A  1 225 ? 51.331  66.387 22.376 1.00 24.41 ? 225  TYR A CA  1 
ATOM   1593  C  C   . TYR A  1 225 ? 50.594  65.454 21.437 1.00 24.32 ? 225  TYR A C   1 
ATOM   1594  O  O   . TYR A  1 225 ? 51.032  65.203 20.306 1.00 24.22 ? 225  TYR A O   1 
ATOM   1595  C  CB  . TYR A  1 225 ? 50.642  67.756 22.377 1.00 25.18 ? 225  TYR A CB  1 
ATOM   1596  C  CG  . TYR A  1 225 ? 50.536  68.420 21.017 1.00 27.98 ? 225  TYR A CG  1 
ATOM   1597  C  CD1 . TYR A  1 225 ? 51.542  69.279 20.551 1.00 28.51 ? 225  TYR A CD1 1 
ATOM   1598  C  CD2 . TYR A  1 225 ? 49.403  68.238 20.215 1.00 28.32 ? 225  TYR A CD2 1 
ATOM   1599  C  CE1 . TYR A  1 225 ? 51.413  69.947 19.322 1.00 28.42 ? 225  TYR A CE1 1 
ATOM   1600  C  CE2 . TYR A  1 225 ? 49.271  68.897 18.988 1.00 29.10 ? 225  TYR A CE2 1 
ATOM   1601  C  CZ  . TYR A  1 225 ? 50.284  69.750 18.556 1.00 30.06 ? 225  TYR A CZ  1 
ATOM   1602  O  OH  . TYR A  1 225 ? 50.166  70.402 17.354 1.00 32.04 ? 225  TYR A OH  1 
ATOM   1603  N  N   . ALA A  1 226 ? 49.484  64.917 21.933 1.00 23.24 ? 226  ALA A N   1 
ATOM   1604  C  CA  . ALA A  1 226 ? 48.649  64.019 21.153 1.00 23.42 ? 226  ALA A CA  1 
ATOM   1605  C  C   . ALA A  1 226 ? 47.386  64.775 20.796 1.00 23.33 ? 226  ALA A C   1 
ATOM   1606  O  O   . ALA A  1 226 ? 47.018  65.740 21.467 1.00 23.61 ? 226  ALA A O   1 
ATOM   1607  C  CB  . ALA A  1 226 ? 48.289  62.794 21.963 1.00 22.41 ? 226  ALA A CB  1 
ATOM   1608  N  N   . GLN A  1 227 ? 46.732  64.330 19.733 1.00 23.57 ? 227  GLN A N   1 
ATOM   1609  C  CA  . GLN A  1 227 ? 45.493  64.934 19.288 1.00 23.60 ? 227  GLN A CA  1 
ATOM   1610  C  C   . GLN A  1 227 ? 44.484  63.807 19.110 1.00 24.02 ? 227  GLN A C   1 
ATOM   1611  O  O   . GLN A  1 227 ? 44.749  62.831 18.401 1.00 24.43 ? 227  GLN A O   1 
ATOM   1612  C  CB  . GLN A  1 227 ? 45.674  65.646 17.955 1.00 23.82 ? 227  GLN A CB  1 
ATOM   1613  C  CG  . GLN A  1 227 ? 44.395  66.315 17.490 1.00 23.31 ? 227  GLN A CG  1 
ATOM   1614  C  CD  . GLN A  1 227 ? 44.453  66.770 16.036 1.00 22.95 ? 227  GLN A CD  1 
ATOM   1615  O  OE1 . GLN A  1 227 ? 44.384  65.955 15.114 1.00 20.73 ? 227  GLN A OE1 1 
ATOM   1616  N  NE2 . GLN A  1 227 ? 44.584  68.074 15.833 1.00 19.43 ? 227  GLN A NE2 1 
ATOM   1617  N  N   . PHE A  1 228 ? 43.329  63.935 19.757 1.00 23.45 ? 228  PHE A N   1 
ATOM   1618  C  CA  . PHE A  1 228 ? 42.309  62.903 19.650 1.00 23.73 ? 228  PHE A CA  1 
ATOM   1619  C  C   . PHE A  1 228 ? 41.121  63.375 18.839 1.00 23.68 ? 228  PHE A C   1 
ATOM   1620  O  O   . PHE A  1 228 ? 40.681  64.519 18.966 1.00 24.62 ? 228  PHE A O   1 
ATOM   1621  C  CB  . PHE A  1 228 ? 41.863  62.471 21.048 1.00 22.40 ? 228  PHE A CB  1 
ATOM   1622  C  CG  . PHE A  1 228 ? 42.993  61.971 21.914 1.00 21.88 ? 228  PHE A CG  1 
ATOM   1623  C  CD1 . PHE A  1 228 ? 43.405  60.639 21.860 1.00 20.28 ? 228  PHE A CD1 1 
ATOM   1624  C  CD2 . PHE A  1 228 ? 43.642  62.838 22.792 1.00 20.37 ? 228  PHE A CD2 1 
ATOM   1625  C  CE1 . PHE A  1 228 ? 44.441  60.185 22.670 1.00 19.19 ? 228  PHE A CE1 1 
ATOM   1626  C  CE2 . PHE A  1 228 ? 44.677  62.387 23.601 1.00 20.99 ? 228  PHE A CE2 1 
ATOM   1627  C  CZ  . PHE A  1 228 ? 45.074  61.062 23.541 1.00 20.60 ? 228  PHE A CZ  1 
ATOM   1628  N  N   . ASN A  1 229 ? 40.614  62.482 17.997 1.00 25.47 ? 229  ASN A N   1 
ATOM   1629  C  CA  . ASN A  1 229 ? 39.464  62.762 17.140 1.00 25.51 ? 229  ASN A CA  1 
ATOM   1630  C  C   . ASN A  1 229 ? 38.332  61.792 17.499 1.00 24.87 ? 229  ASN A C   1 
ATOM   1631  O  O   . ASN A  1 229 ? 38.444  60.595 17.259 1.00 22.76 ? 229  ASN A O   1 
ATOM   1632  C  CB  . ASN A  1 229 ? 39.854  62.570 15.674 1.00 27.97 ? 229  ASN A CB  1 
ATOM   1633  C  CG  . ASN A  1 229 ? 38.854  63.181 14.724 1.00 31.61 ? 229  ASN A CG  1 
ATOM   1634  O  OD1 . ASN A  1 229 ? 37.652  63.201 15.014 1.00 31.28 ? 229  ASN A OD1 1 
ATOM   1635  N  ND2 . ASN A  1 229 ? 39.344  63.676 13.587 1.00 34.06 ? 229  ASN A ND2 1 
ATOM   1636  N  N   . ASP A  1 230 ? 37.245  62.317 18.058 1.00 25.40 ? 230  ASP A N   1 
ATOM   1637  C  CA  . ASP A  1 230 ? 36.109  61.496 18.465 1.00 26.71 ? 230  ASP A CA  1 
ATOM   1638  C  C   . ASP A  1 230 ? 34.895  61.680 17.561 1.00 28.03 ? 230  ASP A C   1 
ATOM   1639  O  O   . ASP A  1 230 ? 33.769  61.283 17.899 1.00 26.64 ? 230  ASP A O   1 
ATOM   1640  C  CB  . ASP A  1 230 ? 35.725  61.828 19.902 1.00 26.78 ? 230  ASP A CB  1 
ATOM   1641  C  CG  . ASP A  1 230 ? 36.678  61.215 20.904 1.00 27.88 ? 230  ASP A CG  1 
ATOM   1642  O  OD1 . ASP A  1 230 ? 37.912  61.318 20.719 1.00 28.81 ? 230  ASP A OD1 1 
ATOM   1643  O  OD2 . ASP A  1 230 ? 36.193  60.632 21.882 1.00 27.60 ? 230  ASP A OD2 1 
ATOM   1644  N  N   . THR A  1 231 ? 35.138  62.270 16.401 1.00 28.53 ? 231  THR A N   1 
ATOM   1645  C  CA  . THR A  1 231 ? 34.089  62.542 15.432 1.00 28.93 ? 231  THR A CA  1 
ATOM   1646  C  C   . THR A  1 231 ? 33.032  61.469 15.305 1.00 29.40 ? 231  THR A C   1 
ATOM   1647  O  O   . THR A  1 231 ? 31.831  61.767 15.372 1.00 30.29 ? 231  THR A O   1 
ATOM   1648  C  CB  . THR A  1 231 ? 34.689  62.817 14.039 1.00 28.82 ? 231  THR A CB  1 
ATOM   1649  O  OG1 . THR A  1 231 ? 35.446  64.034 14.090 1.00 29.95 ? 231  THR A OG1 1 
ATOM   1650  C  CG2 . THR A  1 231 ? 33.588  62.948 12.991 1.00 28.12 ? 231  THR A CG2 1 
ATOM   1651  N  N   . GLU A  1 232 ? 33.446  60.223 15.126 1.00 28.87 ? 232  GLU A N   1 
ATOM   1652  C  CA  . GLU A  1 232 ? 32.445  59.173 14.955 1.00 29.39 ? 232  GLU A CA  1 
ATOM   1653  C  C   . GLU A  1 232 ? 32.180  58.294 16.179 1.00 27.11 ? 232  GLU A C   1 
ATOM   1654  O  O   . GLU A  1 232 ? 31.563  57.247 16.069 1.00 26.68 ? 232  GLU A O   1 
ATOM   1655  C  CB  . GLU A  1 232 ? 32.835  58.305 13.757 1.00 32.51 ? 232  GLU A CB  1 
ATOM   1656  C  CG  . GLU A  1 232 ? 32.716  59.006 12.419 1.00 36.95 ? 232  GLU A CG  1 
ATOM   1657  C  CD  . GLU A  1 232 ? 33.576  58.337 11.359 1.00 41.30 ? 232  GLU A CD  1 
ATOM   1658  O  OE1 . GLU A  1 232 ? 34.814  58.556 11.384 1.00 42.30 ? 232  GLU A OE1 1 
ATOM   1659  O  OE2 . GLU A  1 232 ? 33.024  57.573 10.526 1.00 42.73 ? 232  GLU A OE2 1 
ATOM   1660  N  N   . VAL A  1 233 ? 32.646  58.718 17.342 1.00 25.88 ? 233  VAL A N   1 
ATOM   1661  C  CA  . VAL A  1 233 ? 32.433  57.942 18.553 1.00 24.83 ? 233  VAL A CA  1 
ATOM   1662  C  C   . VAL A  1 233 ? 31.028  58.221 19.066 1.00 23.15 ? 233  VAL A C   1 
ATOM   1663  O  O   . VAL A  1 233 ? 30.671  59.381 19.274 1.00 23.37 ? 233  VAL A O   1 
ATOM   1664  C  CB  . VAL A  1 233 ? 33.439  58.346 19.655 1.00 25.42 ? 233  VAL A CB  1 
ATOM   1665  C  CG1 . VAL A  1 233 ? 33.207  57.494 20.912 1.00 24.95 ? 233  VAL A CG1 1 
ATOM   1666  C  CG2 . VAL A  1 233 ? 34.886  58.195 19.116 1.00 25.76 ? 233  VAL A CG2 1 
ATOM   1667  N  N   . PRO A  1 234 ? 30.210  57.172 19.262 1.00 21.46 ? 234  PRO A N   1 
ATOM   1668  C  CA  . PRO A  1 234 ? 28.848  57.383 19.757 1.00 22.44 ? 234  PRO A CA  1 
ATOM   1669  C  C   . PRO A  1 234 ? 28.889  58.072 21.110 1.00 22.64 ? 234  PRO A C   1 
ATOM   1670  O  O   . PRO A  1 234 ? 29.908  58.037 21.812 1.00 21.23 ? 234  PRO A O   1 
ATOM   1671  C  CB  . PRO A  1 234 ? 28.278  55.964 19.877 1.00 21.15 ? 234  PRO A CB  1 
ATOM   1672  C  CG  . PRO A  1 234 ? 29.069  55.181 18.884 1.00 21.43 ? 234  PRO A CG  1 
ATOM   1673  C  CD  . PRO A  1 234 ? 30.477  55.735 19.080 1.00 21.26 ? 234  PRO A CD  1 
ATOM   1674  N  N   . LEU A  1 235 ? 27.771  58.684 21.472 1.00 22.92 ? 235  LEU A N   1 
ATOM   1675  C  CA  . LEU A  1 235 ? 27.666  59.390 22.736 1.00 23.85 ? 235  LEU A CA  1 
ATOM   1676  C  C   . LEU A  1 235 ? 26.816  58.624 23.743 1.00 22.43 ? 235  LEU A C   1 
ATOM   1677  O  O   . LEU A  1 235 ? 25.801  58.036 23.375 1.00 21.17 ? 235  LEU A O   1 
ATOM   1678  C  CB  . LEU A  1 235 ? 27.015  60.750 22.521 1.00 26.02 ? 235  LEU A CB  1 
ATOM   1679  C  CG  . LEU A  1 235 ? 27.602  61.717 21.483 1.00 29.12 ? 235  LEU A CG  1 
ATOM   1680  C  CD1 . LEU A  1 235 ? 26.502  62.692 21.071 1.00 29.57 ? 235  LEU A CD1 1 
ATOM   1681  C  CD2 . LEU A  1 235 ? 28.803  62.460 22.052 1.00 29.49 ? 235  LEU A CD2 1 
ATOM   1682  N  N   . ILE A  1 236 ? 27.254  58.600 25.002 1.00 19.67 ? 236  ILE A N   1 
ATOM   1683  C  CA  . ILE A  1 236 ? 26.439  57.982 26.039 1.00 18.32 ? 236  ILE A CA  1 
ATOM   1684  C  C   . ILE A  1 236 ? 25.615  59.202 26.507 1.00 19.25 ? 236  ILE A C   1 
ATOM   1685  O  O   . ILE A  1 236 ? 26.130  60.327 26.605 1.00 18.58 ? 236  ILE A O   1 
ATOM   1686  C  CB  . ILE A  1 236 ? 27.287  57.387 27.218 1.00 18.70 ? 236  ILE A CB  1 
ATOM   1687  C  CG1 . ILE A  1 236 ? 26.367  56.950 28.361 1.00 16.70 ? 236  ILE A CG1 1 
ATOM   1688  C  CG2 . ILE A  1 236 ? 28.283  58.423 27.755 1.00 17.71 ? 236  ILE A CG2 1 
ATOM   1689  C  CD1 . ILE A  1 236 ? 25.250  55.976 27.945 1.00 15.43 ? 236  ILE A CD1 1 
ATOM   1690  N  N   . GLU A  1 237 ? 24.334  58.995 26.755 1.00 19.00 ? 237  GLU A N   1 
ATOM   1691  C  CA  . GLU A  1 237 ? 23.473  60.089 27.172 1.00 19.59 ? 237  GLU A CA  1 
ATOM   1692  C  C   . GLU A  1 237 ? 22.732  59.692 28.440 1.00 17.83 ? 237  GLU A C   1 
ATOM   1693  O  O   . GLU A  1 237 ? 22.253  58.584 28.549 1.00 17.24 ? 237  GLU A O   1 
ATOM   1694  C  CB  . GLU A  1 237 ? 22.483  60.413 26.049 1.00 20.17 ? 237  GLU A CB  1 
ATOM   1695  C  CG  . GLU A  1 237 ? 23.169  60.847 24.735 1.00 23.85 ? 237  GLU A CG  1 
ATOM   1696  C  CD  . GLU A  1 237 ? 22.191  61.352 23.672 1.00 26.17 ? 237  GLU A CD  1 
ATOM   1697  O  OE1 . GLU A  1 237 ? 22.629  62.041 22.726 1.00 28.03 ? 237  GLU A OE1 1 
ATOM   1698  O  OE2 . GLU A  1 237 ? 20.983  61.060 23.770 1.00 28.23 ? 237  GLU A OE2 1 
ATOM   1699  N  N   . TYR A  1 238 ? 22.666  60.590 29.406 1.00 18.36 ? 238  TYR A N   1 
ATOM   1700  C  CA  . TYR A  1 238 ? 21.946  60.312 30.645 1.00 18.57 ? 238  TYR A CA  1 
ATOM   1701  C  C   . TYR A  1 238 ? 21.496  61.638 31.232 1.00 18.28 ? 238  TYR A C   1 
ATOM   1702  O  O   . TYR A  1 238 ? 22.035  62.695 30.882 1.00 18.67 ? 238  TYR A O   1 
ATOM   1703  C  CB  . TYR A  1 238 ? 22.818  59.523 31.651 1.00 18.08 ? 238  TYR A CB  1 
ATOM   1704  C  CG  . TYR A  1 238 ? 24.122  60.193 32.035 1.00 19.54 ? 238  TYR A CG  1 
ATOM   1705  C  CD1 . TYR A  1 238 ? 25.322  59.858 31.388 1.00 20.22 ? 238  TYR A CD1 1 
ATOM   1706  C  CD2 . TYR A  1 238 ? 24.164  61.164 33.035 1.00 19.56 ? 238  TYR A CD2 1 
ATOM   1707  C  CE1 . TYR A  1 238 ? 26.530  60.481 31.733 1.00 19.54 ? 238  TYR A CE1 1 
ATOM   1708  C  CE2 . TYR A  1 238 ? 25.369  61.795 33.389 1.00 18.99 ? 238  TYR A CE2 1 
ATOM   1709  C  CZ  . TYR A  1 238 ? 26.535  61.453 32.736 1.00 18.75 ? 238  TYR A CZ  1 
ATOM   1710  O  OH  . TYR A  1 238 ? 27.702  62.097 33.033 1.00 17.73 ? 238  TYR A OH  1 
ATOM   1711  N  N   . SER A  1 239 ? 20.495  61.595 32.105 1.00 17.38 ? 239  SER A N   1 
ATOM   1712  C  CA  . SER A  1 239 ? 19.966  62.812 32.708 1.00 16.83 ? 239  SER A CA  1 
ATOM   1713  C  C   . SER A  1 239 ? 20.737  63.290 33.928 1.00 17.66 ? 239  SER A C   1 
ATOM   1714  O  O   . SER A  1 239 ? 21.309  62.506 34.681 1.00 18.09 ? 239  SER A O   1 
ATOM   1715  C  CB  . SER A  1 239 ? 18.507  62.611 33.136 1.00 15.39 ? 239  SER A CB  1 
ATOM   1716  O  OG  . SER A  1 239 ? 17.685  62.250 32.054 1.00 18.85 ? 239  SER A OG  1 
ATOM   1717  N  N   . PHE A  1 240 ? 20.723  64.596 34.121 1.00 17.53 ? 240  PHE A N   1 
ATOM   1718  C  CA  . PHE A  1 240 ? 21.346  65.193 35.280 1.00 18.33 ? 240  PHE A CA  1 
ATOM   1719  C  C   . PHE A  1 240 ? 20.249  66.093 35.795 1.00 18.30 ? 240  PHE A C   1 
ATOM   1720  O  O   . PHE A  1 240 ? 19.736  66.946 35.056 1.00 18.28 ? 240  PHE A O   1 
ATOM   1721  C  CB  . PHE A  1 240 ? 22.567  66.024 34.918 1.00 18.02 ? 240  PHE A CB  1 
ATOM   1722  C  CG  . PHE A  1 240 ? 23.414  66.342 36.097 1.00 18.46 ? 240  PHE A CG  1 
ATOM   1723  C  CD1 . PHE A  1 240 ? 24.294  65.399 36.598 1.00 19.61 ? 240  PHE A CD1 1 
ATOM   1724  C  CD2 . PHE A  1 240 ? 23.250  67.534 36.779 1.00 19.03 ? 240  PHE A CD2 1 
ATOM   1725  C  CE1 . PHE A  1 240 ? 24.999  65.631 37.789 1.00 20.18 ? 240  PHE A CE1 1 
ATOM   1726  C  CE2 . PHE A  1 240 ? 23.943  67.785 37.968 1.00 20.25 ? 240  PHE A CE2 1 
ATOM   1727  C  CZ  . PHE A  1 240 ? 24.819  66.826 38.470 1.00 20.77 ? 240  PHE A CZ  1 
ATOM   1728  N  N   . TYR A  1 241 ? 19.874  65.911 37.054 1.00 18.16 ? 241  TYR A N   1 
ATOM   1729  C  CA  . TYR A  1 241 ? 18.768  66.692 37.604 1.00 17.79 ? 241  TYR A CA  1 
ATOM   1730  C  C   . TYR A  1 241 ? 19.146  68.018 38.226 1.00 17.65 ? 241  TYR A C   1 
ATOM   1731  O  O   . TYR A  1 241 ? 18.355  68.966 38.188 1.00 18.83 ? 241  TYR A O   1 
ATOM   1732  C  CB  . TYR A  1 241 ? 17.976  65.818 38.582 1.00 16.84 ? 241  TYR A CB  1 
ATOM   1733  C  CG  . TYR A  1 241 ? 17.507  64.544 37.900 1.00 17.83 ? 241  TYR A CG  1 
ATOM   1734  C  CD1 . TYR A  1 241 ? 18.265  63.368 37.970 1.00 17.73 ? 241  TYR A CD1 1 
ATOM   1735  C  CD2 . TYR A  1 241 ? 16.373  64.549 37.083 1.00 17.01 ? 241  TYR A CD2 1 
ATOM   1736  C  CE1 . TYR A  1 241 ? 17.916  62.234 37.240 1.00 17.45 ? 241  TYR A CE1 1 
ATOM   1737  C  CE2 . TYR A  1 241 ? 16.008  63.426 36.344 1.00 17.14 ? 241  TYR A CE2 1 
ATOM   1738  C  CZ  . TYR A  1 241 ? 16.782  62.277 36.423 1.00 18.54 ? 241  TYR A CZ  1 
ATOM   1739  O  OH  . TYR A  1 241 ? 16.442  61.191 35.665 1.00 19.86 ? 241  TYR A OH  1 
ATOM   1740  N  N   . SER A  1 242 ? 20.343  68.086 38.789 1.00 17.27 ? 242  SER A N   1 
ATOM   1741  C  CA  . SER A  1 242 ? 20.827  69.318 39.394 1.00 19.34 ? 242  SER A CA  1 
ATOM   1742  C  C   . SER A  1 242 ? 19.975  69.743 40.593 1.00 19.76 ? 242  SER A C   1 
ATOM   1743  O  O   . SER A  1 242 ? 19.205  68.938 41.141 1.00 19.82 ? 242  SER A O   1 
ATOM   1744  C  CB  . SER A  1 242 ? 20.837  70.422 38.330 1.00 18.30 ? 242  SER A CB  1 
ATOM   1745  O  OG  . SER A  1 242 ? 21.535  71.554 38.782 1.00 19.34 ? 242  SER A OG  1 
ATOM   1746  N  N   . ASP A  1 243 ? 20.120  71.001 41.007 1.00 20.61 ? 243  ASP A N   1 
ATOM   1747  C  CA  . ASP A  1 243 ? 19.357  71.513 42.140 1.00 21.93 ? 243  ASP A CA  1 
ATOM   1748  C  C   . ASP A  1 243 ? 17.879  71.487 41.800 1.00 22.74 ? 243  ASP A C   1 
ATOM   1749  O  O   . ASP A  1 243 ? 17.486  71.500 40.626 1.00 20.63 ? 243  ASP A O   1 
ATOM   1750  C  CB  . ASP A  1 243 ? 19.790  72.934 42.523 1.00 25.02 ? 243  ASP A CB  1 
ATOM   1751  C  CG  . ASP A  1 243 ? 21.255  72.996 42.949 1.00 30.29 ? 243  ASP A CG  1 
ATOM   1752  O  OD1 . ASP A  1 243 ? 21.755  72.008 43.559 1.00 30.73 ? 243  ASP A OD1 1 
ATOM   1753  O  OD2 . ASP A  1 243 ? 21.911  74.035 42.685 1.00 33.20 ? 243  ASP A OD2 1 
ATOM   1754  N  N   . GLU A  1 244 ? 17.052  71.462 42.834 1.00 22.64 ? 244  GLU A N   1 
ATOM   1755  C  CA  . GLU A  1 244 ? 15.636  71.356 42.609 1.00 24.41 ? 244  GLU A CA  1 
ATOM   1756  C  C   . GLU A  1 244 ? 15.062  72.527 41.827 1.00 24.29 ? 244  GLU A C   1 
ATOM   1757  O  O   . GLU A  1 244 ? 13.979  72.422 41.263 1.00 22.76 ? 244  GLU A O   1 
ATOM   1758  C  CB  . GLU A  1 244 ? 14.908  71.127 43.948 1.00 25.58 ? 244  GLU A CB  1 
ATOM   1759  C  CG  . GLU A  1 244 ? 14.307  72.339 44.599 1.00 28.98 ? 244  GLU A CG  1 
ATOM   1760  C  CD  . GLU A  1 244 ? 13.496  71.983 45.855 1.00 30.44 ? 244  GLU A CD  1 
ATOM   1761  O  OE1 . GLU A  1 244 ? 14.102  71.548 46.862 1.00 29.73 ? 244  GLU A OE1 1 
ATOM   1762  O  OE2 . GLU A  1 244 ? 12.254  72.145 45.829 1.00 31.61 ? 244  GLU A OE2 1 
ATOM   1763  N  N   . SER A  1 245 ? 15.800  73.629 41.770 1.00 23.44 ? 245  SER A N   1 
ATOM   1764  C  CA  . SER A  1 245 ? 15.337  74.807 41.062 1.00 21.97 ? 245  SER A CA  1 
ATOM   1765  C  C   . SER A  1 245 ? 15.331  74.592 39.556 1.00 21.56 ? 245  SER A C   1 
ATOM   1766  O  O   . SER A  1 245 ? 14.596  75.266 38.846 1.00 21.99 ? 245  SER A O   1 
ATOM   1767  C  CB  . SER A  1 245 ? 16.198  76.033 41.433 1.00 22.62 ? 245  SER A CB  1 
ATOM   1768  O  OG  . SER A  1 245 ? 17.553  75.872 41.015 1.00 23.67 ? 245  SER A OG  1 
ATOM   1769  N  N   . LEU A  1 246 ? 16.132  73.653 39.056 1.00 20.36 ? 246  LEU A N   1 
ATOM   1770  C  CA  . LEU A  1 246 ? 16.160  73.388 37.608 1.00 19.70 ? 246  LEU A CA  1 
ATOM   1771  C  C   . LEU A  1 246 ? 14.849  72.740 37.149 1.00 19.23 ? 246  LEU A C   1 
ATOM   1772  O  O   . LEU A  1 246 ? 14.554  71.599 37.498 1.00 18.25 ? 246  LEU A O   1 
ATOM   1773  C  CB  . LEU A  1 246 ? 17.316  72.470 37.244 1.00 18.13 ? 246  LEU A CB  1 
ATOM   1774  C  CG  . LEU A  1 246 ? 17.484  72.274 35.743 1.00 19.21 ? 246  LEU A CG  1 
ATOM   1775  C  CD1 . LEU A  1 246 ? 17.892  73.609 35.115 1.00 16.81 ? 246  LEU A CD1 1 
ATOM   1776  C  CD2 . LEU A  1 246 ? 18.557  71.226 35.464 1.00 19.85 ? 246  LEU A CD2 1 
ATOM   1777  N  N   . GLN A  1 247 ? 14.080  73.459 36.347 1.00 19.60 ? 247  GLN A N   1 
ATOM   1778  C  CA  . GLN A  1 247 ? 12.785  72.952 35.906 1.00 19.57 ? 247  GLN A CA  1 
ATOM   1779  C  C   . GLN A  1 247 ? 12.868  71.722 35.004 1.00 20.00 ? 247  GLN A C   1 
ATOM   1780  O  O   . GLN A  1 247 ? 12.147  70.744 35.218 1.00 19.36 ? 247  GLN A O   1 
ATOM   1781  C  CB  . GLN A  1 247 ? 11.988  74.072 35.218 1.00 19.11 ? 247  GLN A CB  1 
ATOM   1782  C  CG  . GLN A  1 247 ? 10.517  73.719 34.992 1.00 19.07 ? 247  GLN A CG  1 
ATOM   1783  C  CD  . GLN A  1 247 ? 9.666   74.916 34.593 1.00 20.54 ? 247  GLN A CD  1 
ATOM   1784  O  OE1 . GLN A  1 247 ? 10.081  75.739 33.770 1.00 21.68 ? 247  GLN A OE1 1 
ATOM   1785  N  NE2 . GLN A  1 247 ? 8.456   75.002 35.152 1.00 17.82 ? 247  GLN A NE2 1 
ATOM   1786  N  N   . TYR A  1 248 ? 13.758  71.764 34.015 1.00 19.38 ? 248  TYR A N   1 
ATOM   1787  C  CA  . TYR A  1 248 ? 13.928  70.656 33.088 1.00 19.46 ? 248  TYR A CA  1 
ATOM   1788  C  C   . TYR A  1 248 ? 15.258  69.945 33.297 1.00 20.46 ? 248  TYR A C   1 
ATOM   1789  O  O   . TYR A  1 248 ? 16.305  70.582 33.307 1.00 20.09 ? 248  TYR A O   1 
ATOM   1790  C  CB  . TYR A  1 248 ? 13.873  71.170 31.643 1.00 18.34 ? 248  TYR A CB  1 
ATOM   1791  C  CG  . TYR A  1 248 ? 12.485  71.535 31.172 1.00 17.74 ? 248  TYR A CG  1 
ATOM   1792  C  CD1 . TYR A  1 248 ? 11.669  70.582 30.571 1.00 15.27 ? 248  TYR A CD1 1 
ATOM   1793  C  CD2 . TYR A  1 248 ? 11.995  72.838 31.302 1.00 16.00 ? 248  TYR A CD2 1 
ATOM   1794  C  CE1 . TYR A  1 248 ? 10.408  70.907 30.104 1.00 16.98 ? 248  TYR A CE1 1 
ATOM   1795  C  CE2 . TYR A  1 248 ? 10.719  73.173 30.831 1.00 16.16 ? 248  TYR A CE2 1 
ATOM   1796  C  CZ  . TYR A  1 248 ? 9.935   72.201 30.233 1.00 15.53 ? 248  TYR A CZ  1 
ATOM   1797  O  OH  . TYR A  1 248 ? 8.674   72.484 29.753 1.00 16.74 ? 248  TYR A OH  1 
ATOM   1798  N  N   . PRO A  1 249 ? 15.233  68.609 33.455 1.00 20.77 ? 249  PRO A N   1 
ATOM   1799  C  CA  . PRO A  1 249 ? 16.496  67.892 33.651 1.00 21.27 ? 249  PRO A CA  1 
ATOM   1800  C  C   . PRO A  1 249 ? 17.407  68.127 32.460 1.00 21.90 ? 249  PRO A C   1 
ATOM   1801  O  O   . PRO A  1 249 ? 16.957  68.273 31.318 1.00 21.43 ? 249  PRO A O   1 
ATOM   1802  C  CB  . PRO A  1 249 ? 16.073  66.421 33.733 1.00 22.30 ? 249  PRO A CB  1 
ATOM   1803  C  CG  . PRO A  1 249 ? 14.640  66.484 34.213 1.00 20.85 ? 249  PRO A CG  1 
ATOM   1804  C  CD  . PRO A  1 249 ? 14.094  67.674 33.431 1.00 19.49 ? 249  PRO A CD  1 
ATOM   1805  N  N   . LYS A  1 250 ? 18.698  68.161 32.736 1.00 21.59 ? 250  LYS A N   1 
ATOM   1806  C  CA  . LYS A  1 250 ? 19.681  68.359 31.699 1.00 21.26 ? 250  LYS A CA  1 
ATOM   1807  C  C   . LYS A  1 250 ? 20.105  66.983 31.187 1.00 20.22 ? 250  LYS A C   1 
ATOM   1808  O  O   . LYS A  1 250 ? 20.128  66.008 31.943 1.00 19.11 ? 250  LYS A O   1 
ATOM   1809  C  CB  . LYS A  1 250 ? 20.869  69.106 32.290 1.00 22.87 ? 250  LYS A CB  1 
ATOM   1810  C  CG  . LYS A  1 250 ? 22.021  69.260 31.351 1.00 29.01 ? 250  LYS A CG  1 
ATOM   1811  C  CD  . LYS A  1 250 ? 23.296  69.659 32.108 1.00 32.45 ? 250  LYS A CD  1 
ATOM   1812  C  CE  . LYS A  1 250 ? 24.493  69.727 31.163 1.00 34.55 ? 250  LYS A CE  1 
ATOM   1813  N  NZ  . LYS A  1 250 ? 25.761  70.014 31.900 1.00 37.48 ? 250  LYS A NZ  1 
ATOM   1814  N  N   . THR A  1 251 ? 20.407  66.897 29.902 1.00 18.79 ? 251  THR A N   1 
ATOM   1815  C  CA  . THR A  1 251 ? 20.869  65.647 29.321 1.00 19.03 ? 251  THR A CA  1 
ATOM   1816  C  C   . THR A  1 251 ? 22.384  65.776 29.084 1.00 20.33 ? 251  THR A C   1 
ATOM   1817  O  O   . THR A  1 251 ? 22.822  66.612 28.293 1.00 20.07 ? 251  THR A O   1 
ATOM   1818  C  CB  . THR A  1 251 ? 20.188  65.348 27.952 1.00 18.28 ? 251  THR A CB  1 
ATOM   1819  O  OG1 . THR A  1 251 ? 18.799  65.077 28.150 1.00 17.06 ? 251  THR A OG1 1 
ATOM   1820  C  CG2 . THR A  1 251 ? 20.820  64.116 27.288 1.00 17.20 ? 251  THR A CG2 1 
ATOM   1821  N  N   . VAL A  1 252 ? 23.183  64.970 29.782 1.00 20.57 ? 252  VAL A N   1 
ATOM   1822  C  CA  . VAL A  1 252 ? 24.634  65.003 29.599 1.00 18.74 ? 252  VAL A CA  1 
ATOM   1823  C  C   . VAL A  1 252 ? 24.977  64.064 28.429 1.00 20.82 ? 252  VAL A C   1 
ATOM   1824  O  O   . VAL A  1 252 ? 24.420  62.963 28.320 1.00 20.30 ? 252  VAL A O   1 
ATOM   1825  C  CB  . VAL A  1 252 ? 25.366  64.547 30.896 1.00 19.77 ? 252  VAL A CB  1 
ATOM   1826  C  CG1 . VAL A  1 252 ? 26.871  64.523 30.667 1.00 19.19 ? 252  VAL A CG1 1 
ATOM   1827  C  CG2 . VAL A  1 252 ? 25.016  65.488 32.065 1.00 18.20 ? 252  VAL A CG2 1 
ATOM   1828  N  N   . ARG A  1 253 ? 25.873  64.505 27.544 1.00 21.72 ? 253  ARG A N   1 
ATOM   1829  C  CA  . ARG A  1 253 ? 26.274  63.708 26.375 1.00 22.56 ? 253  ARG A CA  1 
ATOM   1830  C  C   . ARG A  1 253 ? 27.801  63.561 26.329 1.00 21.37 ? 253  ARG A C   1 
ATOM   1831  O  O   . ARG A  1 253 ? 28.503  64.545 26.261 1.00 21.41 ? 253  ARG A O   1 
ATOM   1832  C  CB  . ARG A  1 253 ? 25.764  64.379 25.088 1.00 23.91 ? 253  ARG A CB  1 
ATOM   1833  C  CG  . ARG A  1 253 ? 24.243  64.545 25.064 1.00 27.37 ? 253  ARG A CG  1 
ATOM   1834  C  CD  . ARG A  1 253 ? 23.708  64.882 23.666 1.00 29.80 ? 253  ARG A CD  1 
ATOM   1835  N  NE  . ARG A  1 253 ? 22.243  64.871 23.645 1.00 33.48 ? 253  ARG A NE  1 
ATOM   1836  C  CZ  . ARG A  1 253 ? 21.459  65.747 24.281 1.00 35.46 ? 253  ARG A CZ  1 
ATOM   1837  N  NH1 . ARG A  1 253 ? 21.985  66.736 25.005 1.00 34.96 ? 253  ARG A NH1 1 
ATOM   1838  N  NH2 . ARG A  1 253 ? 20.137  65.635 24.196 1.00 34.90 ? 253  ARG A NH2 1 
ATOM   1839  N  N   . VAL A  1 254 ? 28.304  62.330 26.368 1.00 21.34 ? 254  VAL A N   1 
ATOM   1840  C  CA  . VAL A  1 254 ? 29.747  62.094 26.368 1.00 19.89 ? 254  VAL A CA  1 
ATOM   1841  C  C   . VAL A  1 254 ? 30.195  61.084 25.316 1.00 19.22 ? 254  VAL A C   1 
ATOM   1842  O  O   . VAL A  1 254 ? 29.664  59.977 25.252 1.00 19.96 ? 254  VAL A O   1 
ATOM   1843  C  CB  . VAL A  1 254 ? 30.225  61.543 27.735 1.00 21.13 ? 254  VAL A CB  1 
ATOM   1844  C  CG1 . VAL A  1 254 ? 31.753  61.540 27.800 1.00 20.04 ? 254  VAL A CG1 1 
ATOM   1845  C  CG2 . VAL A  1 254 ? 29.655  62.381 28.877 1.00 21.08 ? 254  VAL A CG2 1 
ATOM   1846  N  N   . PRO A  1 255 ? 31.176  61.460 24.468 1.00 17.91 ? 255  PRO A N   1 
ATOM   1847  C  CA  . PRO A  1 255 ? 31.665  60.528 23.443 1.00 17.43 ? 255  PRO A CA  1 
ATOM   1848  C  C   . PRO A  1 255 ? 32.296  59.380 24.244 1.00 17.40 ? 255  PRO A C   1 
ATOM   1849  O  O   . PRO A  1 255 ? 33.291  59.567 24.939 1.00 17.19 ? 255  PRO A O   1 
ATOM   1850  C  CB  . PRO A  1 255 ? 32.698  61.355 22.674 1.00 17.43 ? 255  PRO A CB  1 
ATOM   1851  C  CG  . PRO A  1 255 ? 32.199  62.811 22.886 1.00 18.05 ? 255  PRO A CG  1 
ATOM   1852  C  CD  . PRO A  1 255 ? 31.818  62.781 24.342 1.00 16.56 ? 255  PRO A CD  1 
ATOM   1853  N  N   . TYR A  1 256 ? 31.699  58.202 24.152 1.00 16.61 ? 256  TYR A N   1 
ATOM   1854  C  CA  . TYR A  1 256 ? 32.151  57.052 24.916 1.00 15.68 ? 256  TYR A CA  1 
ATOM   1855  C  C   . TYR A  1 256 ? 32.006  55.811 24.048 1.00 15.66 ? 256  TYR A C   1 
ATOM   1856  O  O   . TYR A  1 256 ? 30.896  55.382 23.754 1.00 17.24 ? 256  TYR A O   1 
ATOM   1857  C  CB  . TYR A  1 256 ? 31.255  56.954 26.162 1.00 15.92 ? 256  TYR A CB  1 
ATOM   1858  C  CG  . TYR A  1 256 ? 31.527  55.829 27.136 1.00 13.75 ? 256  TYR A CG  1 
ATOM   1859  C  CD1 . TYR A  1 256 ? 31.352  54.503 26.767 1.00 13.82 ? 256  TYR A CD1 1 
ATOM   1860  C  CD2 . TYR A  1 256 ? 31.900  56.104 28.452 1.00 13.23 ? 256  TYR A CD2 1 
ATOM   1861  C  CE1 . TYR A  1 256 ? 31.537  53.460 27.687 1.00 14.13 ? 256  TYR A CE1 1 
ATOM   1862  C  CE2 . TYR A  1 256 ? 32.085  55.073 29.381 1.00 14.92 ? 256  TYR A CE2 1 
ATOM   1863  C  CZ  . TYR A  1 256 ? 31.900  53.758 28.995 1.00 14.74 ? 256  TYR A CZ  1 
ATOM   1864  O  OH  . TYR A  1 256 ? 32.053  52.746 29.918 1.00 15.89 ? 256  TYR A OH  1 
ATOM   1865  N  N   . PRO A  1 257 ? 33.124  55.209 23.634 1.00 15.61 ? 257  PRO A N   1 
ATOM   1866  C  CA  . PRO A  1 257 ? 33.046  54.015 22.798 1.00 16.87 ? 257  PRO A CA  1 
ATOM   1867  C  C   . PRO A  1 257 ? 32.821  52.755 23.625 1.00 17.71 ? 257  PRO A C   1 
ATOM   1868  O  O   . PRO A  1 257 ? 33.683  52.363 24.398 1.00 17.46 ? 257  PRO A O   1 
ATOM   1869  C  CB  . PRO A  1 257 ? 34.405  53.994 22.101 1.00 15.75 ? 257  PRO A CB  1 
ATOM   1870  C  CG  . PRO A  1 257 ? 35.329  54.473 23.225 1.00 16.11 ? 257  PRO A CG  1 
ATOM   1871  C  CD  . PRO A  1 257 ? 34.527  55.626 23.849 1.00 14.79 ? 257  PRO A CD  1 
ATOM   1872  N  N   . LYS A  1 258 ? 31.656  52.139 23.457 1.00 17.37 ? 258  LYS A N   1 
ATOM   1873  C  CA  . LYS A  1 258 ? 31.359  50.899 24.148 1.00 18.00 ? 258  LYS A CA  1 
ATOM   1874  C  C   . LYS A  1 258 ? 32.023  49.773 23.338 1.00 19.58 ? 258  LYS A C   1 
ATOM   1875  O  O   . LYS A  1 258 ? 32.452  49.990 22.194 1.00 19.82 ? 258  LYS A O   1 
ATOM   1876  C  CB  . LYS A  1 258 ? 29.843  50.704 24.261 1.00 17.09 ? 258  LYS A CB  1 
ATOM   1877  C  CG  . LYS A  1 258 ? 29.208  51.661 25.273 1.00 16.63 ? 258  LYS A CG  1 
ATOM   1878  C  CD  . LYS A  1 258 ? 27.703  51.503 25.353 1.00 17.08 ? 258  LYS A CD  1 
ATOM   1879  C  CE  . LYS A  1 258 ? 27.080  52.537 26.324 1.00 18.82 ? 258  LYS A CE  1 
ATOM   1880  N  NZ  . LYS A  1 258 ? 26.952  52.033 27.718 1.00 19.58 ? 258  LYS A NZ  1 
ATOM   1881  N  N   . ALA A  1 259 ? 32.123  48.577 23.912 1.00 19.43 ? 259  ALA A N   1 
ATOM   1882  C  CA  . ALA A  1 259 ? 32.792  47.476 23.230 1.00 19.86 ? 259  ALA A CA  1 
ATOM   1883  C  C   . ALA A  1 259 ? 32.335  47.264 21.781 1.00 20.58 ? 259  ALA A C   1 
ATOM   1884  O  O   . ALA A  1 259 ? 31.147  47.155 21.498 1.00 20.71 ? 259  ALA A O   1 
ATOM   1885  C  CB  . ALA A  1 259 ? 32.632  46.189 24.050 1.00 19.70 ? 259  ALA A CB  1 
ATOM   1886  N  N   . GLY A  1 260 ? 33.291  47.220 20.865 1.00 20.54 ? 260  GLY A N   1 
ATOM   1887  C  CA  . GLY A  1 260 ? 32.962  47.008 19.467 1.00 21.51 ? 260  GLY A CA  1 
ATOM   1888  C  C   . GLY A  1 260 ? 32.612  48.259 18.687 1.00 22.62 ? 260  GLY A C   1 
ATOM   1889  O  O   . GLY A  1 260 ? 32.596  48.220 17.462 1.00 24.20 ? 260  GLY A O   1 
ATOM   1890  N  N   . ALA A  1 261 ? 32.349  49.368 19.373 1.00 21.82 ? 261  ALA A N   1 
ATOM   1891  C  CA  . ALA A  1 261 ? 31.975  50.604 18.697 1.00 20.97 ? 261  ALA A CA  1 
ATOM   1892  C  C   . ALA A  1 261 ? 33.150  51.325 18.051 1.00 22.07 ? 261  ALA A C   1 
ATOM   1893  O  O   . ALA A  1 261 ? 34.297  50.917 18.201 1.00 24.14 ? 261  ALA A O   1 
ATOM   1894  C  CB  . ALA A  1 261 ? 31.275  51.533 19.674 1.00 19.55 ? 261  ALA A CB  1 
ATOM   1895  N  N   . VAL A  1 262 ? 32.865  52.416 17.345 1.00 20.95 ? 262  VAL A N   1 
ATOM   1896  C  CA  . VAL A  1 262 ? 33.916  53.189 16.700 1.00 19.81 ? 262  VAL A CA  1 
ATOM   1897  C  C   . VAL A  1 262 ? 34.733  53.923 17.761 1.00 20.35 ? 262  VAL A C   1 
ATOM   1898  O  O   . VAL A  1 262 ? 34.180  54.617 18.619 1.00 19.35 ? 262  VAL A O   1 
ATOM   1899  C  CB  . VAL A  1 262 ? 33.319  54.221 15.704 1.00 20.50 ? 262  VAL A CB  1 
ATOM   1900  C  CG1 . VAL A  1 262 ? 34.428  55.115 15.145 1.00 21.30 ? 262  VAL A CG1 1 
ATOM   1901  C  CG2 . VAL A  1 262 ? 32.601  53.489 14.554 1.00 18.32 ? 262  VAL A CG2 1 
ATOM   1902  N  N   . ASN A  1 263 ? 36.053  53.776 17.679 1.00 19.72 ? 263  ASN A N   1 
ATOM   1903  C  CA  . ASN A  1 263 ? 36.990  54.390 18.617 1.00 19.23 ? 263  ASN A CA  1 
ATOM   1904  C  C   . ASN A  1 263 ? 37.523  55.708 18.100 1.00 19.99 ? 263  ASN A C   1 
ATOM   1905  O  O   . ASN A  1 263 ? 37.486  55.975 16.903 1.00 20.73 ? 263  ASN A O   1 
ATOM   1906  C  CB  . ASN A  1 263 ? 38.216  53.502 18.826 1.00 18.41 ? 263  ASN A CB  1 
ATOM   1907  C  CG  . ASN A  1 263 ? 38.050  52.519 19.960 1.00 20.43 ? 263  ASN A CG  1 
ATOM   1908  O  OD1 . ASN A  1 263 ? 37.116  52.634 20.756 1.00 18.31 ? 263  ASN A OD1 1 
ATOM   1909  N  ND2 . ASN A  1 263 ? 38.977  51.548 20.055 1.00 16.83 ? 263  ASN A ND2 1 
ATOM   1910  N  N   . PRO A  1 264 ? 38.025  56.552 19.006 1.00 18.70 ? 264  PRO A N   1 
ATOM   1911  C  CA  . PRO A  1 264 ? 38.580  57.829 18.573 1.00 17.88 ? 264  PRO A CA  1 
ATOM   1912  C  C   . PRO A  1 264 ? 39.897  57.468 17.896 1.00 19.03 ? 264  PRO A C   1 
ATOM   1913  O  O   . PRO A  1 264 ? 40.426  56.370 18.102 1.00 17.67 ? 264  PRO A O   1 
ATOM   1914  C  CB  . PRO A  1 264 ? 38.816  58.577 19.890 1.00 19.89 ? 264  PRO A CB  1 
ATOM   1915  C  CG  . PRO A  1 264 ? 39.077  57.439 20.889 1.00 19.63 ? 264  PRO A CG  1 
ATOM   1916  C  CD  . PRO A  1 264 ? 38.026  56.424 20.477 1.00 18.25 ? 264  PRO A CD  1 
ATOM   1917  N  N   . THR A  1 265 ? 40.415  58.363 17.067 1.00 19.78 ? 265  THR A N   1 
ATOM   1918  C  CA  . THR A  1 265 ? 41.689  58.112 16.414 1.00 20.13 ? 265  THR A CA  1 
ATOM   1919  C  C   . THR A  1 265 ? 42.661  59.078 17.072 1.00 20.83 ? 265  THR A C   1 
ATOM   1920  O  O   . THR A  1 265 ? 42.240  60.034 17.731 1.00 19.94 ? 265  THR A O   1 
ATOM   1921  C  CB  . THR A  1 265 ? 41.614  58.376 14.893 1.00 20.58 ? 265  THR A CB  1 
ATOM   1922  O  OG1 . THR A  1 265 ? 41.073  59.683 14.651 1.00 19.32 ? 265  THR A OG1 1 
ATOM   1923  C  CG2 . THR A  1 265 ? 40.759  57.337 14.231 1.00 18.66 ? 265  THR A CG2 1 
ATOM   1924  N  N   . VAL A  1 266 ? 43.954  58.834 16.884 1.00 20.79 ? 266  VAL A N   1 
ATOM   1925  C  CA  . VAL A  1 266 ? 44.982  59.649 17.515 1.00 20.97 ? 266  VAL A CA  1 
ATOM   1926  C  C   . VAL A  1 266 ? 46.181  59.959 16.598 1.00 22.83 ? 266  VAL A C   1 
ATOM   1927  O  O   . VAL A  1 266 ? 46.561  59.150 15.745 1.00 23.03 ? 266  VAL A O   1 
ATOM   1928  C  CB  . VAL A  1 266 ? 45.509  58.918 18.799 1.00 18.14 ? 266  VAL A CB  1 
ATOM   1929  C  CG1 . VAL A  1 266 ? 46.113  57.567 18.409 1.00 16.01 ? 266  VAL A CG1 1 
ATOM   1930  C  CG2 . VAL A  1 266 ? 46.532  59.771 19.522 1.00 14.49 ? 266  VAL A CG2 1 
ATOM   1931  N  N   . LYS A  1 267 ? 46.769  61.136 16.798 1.00 23.91 ? 267  LYS A N   1 
ATOM   1932  C  CA  . LYS A  1 267 ? 47.937  61.569 16.051 1.00 24.47 ? 267  LYS A CA  1 
ATOM   1933  C  C   . LYS A  1 267 ? 48.855  62.165 17.094 1.00 25.00 ? 267  LYS A C   1 
ATOM   1934  O  O   . LYS A  1 267 ? 48.385  62.622 18.139 1.00 23.37 ? 267  LYS A O   1 
ATOM   1935  C  CB  . LYS A  1 267 ? 47.577  62.631 15.029 1.00 25.03 ? 267  LYS A CB  1 
ATOM   1936  C  CG  . LYS A  1 267 ? 46.707  62.132 13.900 1.00 28.15 ? 267  LYS A CG  1 
ATOM   1937  C  CD  . LYS A  1 267 ? 46.400  63.294 12.969 1.00 30.34 ? 267  LYS A CD  1 
ATOM   1938  C  CE  . LYS A  1 267 ? 45.521  62.890 11.805 1.00 32.40 ? 267  LYS A CE  1 
ATOM   1939  N  NZ  . LYS A  1 267 ? 45.143  64.122 11.049 1.00 35.64 ? 267  LYS A NZ  1 
ATOM   1940  N  N   . PHE A  1 268 ? 50.155  62.167 16.802 1.00 25.33 ? 268  PHE A N   1 
ATOM   1941  C  CA  . PHE A  1 268 ? 51.157  62.670 17.725 1.00 25.69 ? 268  PHE A CA  1 
ATOM   1942  C  C   . PHE A  1 268 ? 51.992  63.784 17.104 1.00 26.12 ? 268  PHE A C   1 
ATOM   1943  O  O   . PHE A  1 268 ? 52.470  63.649 15.984 1.00 26.93 ? 268  PHE A O   1 
ATOM   1944  C  CB  . PHE A  1 268 ? 52.074  61.523 18.148 1.00 24.35 ? 268  PHE A CB  1 
ATOM   1945  C  CG  . PHE A  1 268 ? 52.941  61.857 19.319 1.00 24.97 ? 268  PHE A CG  1 
ATOM   1946  C  CD1 . PHE A  1 268 ? 52.392  61.964 20.596 1.00 25.30 ? 268  PHE A CD1 1 
ATOM   1947  C  CD2 . PHE A  1 268 ? 54.302  62.089 19.151 1.00 25.82 ? 268  PHE A CD2 1 
ATOM   1948  C  CE1 . PHE A  1 268 ? 53.186  62.298 21.696 1.00 25.51 ? 268  PHE A CE1 1 
ATOM   1949  C  CE2 . PHE A  1 268 ? 55.114  62.426 20.246 1.00 25.84 ? 268  PHE A CE2 1 
ATOM   1950  C  CZ  . PHE A  1 268 ? 54.551  62.529 21.521 1.00 25.33 ? 268  PHE A CZ  1 
ATOM   1951  N  N   . PHE A  1 269 ? 52.201  64.871 17.845 1.00 26.67 ? 269  PHE A N   1 
ATOM   1952  C  CA  . PHE A  1 269 ? 52.976  66.001 17.336 1.00 25.97 ? 269  PHE A CA  1 
ATOM   1953  C  C   . PHE A  1 269 ? 54.057  66.506 18.291 1.00 26.50 ? 269  PHE A C   1 
ATOM   1954  O  O   . PHE A  1 269 ? 54.000  66.271 19.501 1.00 26.57 ? 269  PHE A O   1 
ATOM   1955  C  CB  . PHE A  1 269 ? 52.053  67.184 17.019 1.00 26.28 ? 269  PHE A CB  1 
ATOM   1956  C  CG  . PHE A  1 269 ? 50.980  66.874 16.025 1.00 27.03 ? 269  PHE A CG  1 
ATOM   1957  C  CD1 . PHE A  1 269 ? 49.768  66.337 16.438 1.00 27.04 ? 269  PHE A CD1 1 
ATOM   1958  C  CD2 . PHE A  1 269 ? 51.164  67.161 14.672 1.00 27.27 ? 269  PHE A CD2 1 
ATOM   1959  C  CE1 . PHE A  1 269 ? 48.742  66.083 15.512 1.00 27.78 ? 269  PHE A CE1 1 
ATOM   1960  C  CE2 . PHE A  1 269 ? 50.153  66.913 13.737 1.00 26.61 ? 269  PHE A CE2 1 
ATOM   1961  C  CZ  . PHE A  1 269 ? 48.934  66.375 14.161 1.00 28.10 ? 269  PHE A CZ  1 
ATOM   1962  N  N   . VAL A  1 270 ? 55.040  67.209 17.732 1.00 25.77 ? 270  VAL A N   1 
ATOM   1963  C  CA  . VAL A  1 270 ? 56.111  67.801 18.518 1.00 25.39 ? 270  VAL A CA  1 
ATOM   1964  C  C   . VAL A  1 270 ? 56.354  69.209 17.997 1.00 26.14 ? 270  VAL A C   1 
ATOM   1965  O  O   . VAL A  1 270 ? 56.437  69.434 16.787 1.00 24.88 ? 270  VAL A O   1 
ATOM   1966  C  CB  . VAL A  1 270 ? 57.427  67.014 18.425 1.00 25.60 ? 270  VAL A CB  1 
ATOM   1967  C  CG1 . VAL A  1 270 ? 58.458  67.668 19.320 1.00 24.25 ? 270  VAL A CG1 1 
ATOM   1968  C  CG2 . VAL A  1 270 ? 57.213  65.562 18.843 1.00 24.09 ? 270  VAL A CG2 1 
ATOM   1969  N  N   . VAL A  1 271 ? 56.449  70.161 18.918 1.00 26.86 ? 271  VAL A N   1 
ATOM   1970  C  CA  . VAL A  1 271 ? 56.672  71.550 18.539 1.00 28.28 ? 271  VAL A CA  1 
ATOM   1971  C  C   . VAL A  1 271 ? 57.846  72.133 19.325 1.00 29.11 ? 271  VAL A C   1 
ATOM   1972  O  O   . VAL A  1 271 ? 58.036  71.818 20.505 1.00 27.31 ? 271  VAL A O   1 
ATOM   1973  C  CB  . VAL A  1 271 ? 55.403  72.411 18.798 1.00 28.72 ? 271  VAL A CB  1 
ATOM   1974  C  CG1 . VAL A  1 271 ? 55.065  72.429 20.281 1.00 27.62 ? 271  VAL A CG1 1 
ATOM   1975  C  CG2 . VAL A  1 271 ? 55.622  73.829 18.291 1.00 28.72 ? 271  VAL A CG2 1 
ATOM   1976  N  N   . ASN A  1 272 ? 58.631  72.977 18.654 1.00 29.44 ? 272  ASN A N   1 
ATOM   1977  C  CA  . ASN A  1 272 ? 59.790  73.614 19.271 1.00 30.54 ? 272  ASN A CA  1 
ATOM   1978  C  C   . ASN A  1 272 ? 59.312  74.897 19.917 1.00 30.77 ? 272  ASN A C   1 
ATOM   1979  O  O   . ASN A  1 272 ? 58.969  75.841 19.212 1.00 32.28 ? 272  ASN A O   1 
ATOM   1980  C  CB  . ASN A  1 272 ? 60.853  73.952 18.205 1.00 30.97 ? 272  ASN A CB  1 
ATOM   1981  C  CG  . ASN A  1 272 ? 62.186  74.379 18.823 1.00 31.38 ? 272  ASN A CG  1 
ATOM   1982  O  OD1 . ASN A  1 272 ? 62.226  75.152 19.788 1.00 31.62 ? 272  ASN A OD1 1 
ATOM   1983  N  ND2 . ASN A  1 272 ? 63.285  73.873 18.265 1.00 32.67 ? 272  ASN A ND2 1 
ATOM   1984  N  N   . THR A  1 273 ? 59.292  74.959 21.244 1.00 31.66 ? 273  THR A N   1 
ATOM   1985  C  CA  . THR A  1 273 ? 58.823  76.179 21.885 1.00 32.64 ? 273  THR A CA  1 
ATOM   1986  C  C   . THR A  1 273 ? 59.873  77.290 21.919 1.00 34.48 ? 273  THR A C   1 
ATOM   1987  O  O   . THR A  1 273 ? 59.580  78.398 22.374 1.00 34.04 ? 273  THR A O   1 
ATOM   1988  C  CB  . THR A  1 273 ? 58.322  75.923 23.332 1.00 31.80 ? 273  THR A CB  1 
ATOM   1989  O  OG1 . THR A  1 273 ? 59.424  75.580 24.185 1.00 31.41 ? 273  THR A OG1 1 
ATOM   1990  C  CG2 . THR A  1 273 ? 57.309  74.790 23.343 1.00 31.00 ? 273  THR A CG2 1 
ATOM   1991  N  N   . ASP A  1 274 ? 61.083  77.010 21.431 1.00 36.13 ? 274  ASP A N   1 
ATOM   1992  C  CA  . ASP A  1 274 ? 62.137  78.033 21.426 1.00 38.16 ? 274  ASP A CA  1 
ATOM   1993  C  C   . ASP A  1 274 ? 62.119  78.870 20.147 1.00 39.45 ? 274  ASP A C   1 
ATOM   1994  O  O   . ASP A  1 274 ? 62.732  79.939 20.082 1.00 40.31 ? 274  ASP A O   1 
ATOM   1995  C  CB  . ASP A  1 274 ? 63.527  77.412 21.575 1.00 38.83 ? 274  ASP A CB  1 
ATOM   1996  C  CG  . ASP A  1 274 ? 63.857  77.015 23.006 1.00 40.43 ? 274  ASP A CG  1 
ATOM   1997  O  OD1 . ASP A  1 274 ? 63.254  77.549 23.969 1.00 39.97 ? 274  ASP A OD1 1 
ATOM   1998  O  OD2 . ASP A  1 274 ? 64.761  76.166 23.168 1.00 43.37 ? 274  ASP A OD2 1 
ATOM   1999  N  N   . SER A  1 275 ? 61.424  78.383 19.126 1.00 39.53 ? 275  SER A N   1 
ATOM   2000  C  CA  . SER A  1 275 ? 61.359  79.106 17.870 1.00 39.56 ? 275  SER A CA  1 
ATOM   2001  C  C   . SER A  1 275 ? 59.941  79.518 17.509 1.00 39.66 ? 275  SER A C   1 
ATOM   2002  O  O   . SER A  1 275 ? 59.527  79.410 16.350 1.00 39.04 ? 275  SER A O   1 
ATOM   2003  C  CB  . SER A  1 275 ? 61.958  78.253 16.754 1.00 39.73 ? 275  SER A CB  1 
ATOM   2004  O  OG  . SER A  1 275 ? 61.454  76.930 16.813 1.00 41.62 ? 275  SER A OG  1 
ATOM   2005  N  N   . LEU A  1 276 ? 59.195  79.990 18.506 1.00 39.79 ? 276  LEU A N   1 
ATOM   2006  C  CA  . LEU A  1 276 ? 57.819  80.428 18.271 1.00 40.25 ? 276  LEU A CA  1 
ATOM   2007  C  C   . LEU A  1 276 ? 57.798  81.887 17.811 1.00 41.43 ? 276  LEU A C   1 
ATOM   2008  O  O   . LEU A  1 276 ? 58.582  82.715 18.289 1.00 40.85 ? 276  LEU A O   1 
ATOM   2009  C  CB  . LEU A  1 276 ? 56.985  80.279 19.552 1.00 38.64 ? 276  LEU A CB  1 
ATOM   2010  C  CG  . LEU A  1 276 ? 56.764  78.835 20.038 1.00 37.94 ? 276  LEU A CG  1 
ATOM   2011  C  CD1 . LEU A  1 276 ? 56.197  78.837 21.452 1.00 35.12 ? 276  LEU A CD1 1 
ATOM   2012  C  CD2 . LEU A  1 276 ? 55.851  78.113 19.065 1.00 35.50 ? 276  LEU A CD2 1 
ATOM   2013  N  N   . SER A  1 277 ? 56.894  82.198 16.887 1.00 42.96 ? 277  SER A N   1 
ATOM   2014  C  CA  . SER A  1 277 ? 56.786  83.557 16.383 1.00 45.07 ? 277  SER A CA  1 
ATOM   2015  C  C   . SER A  1 277 ? 55.435  84.200 16.658 1.00 46.12 ? 277  SER A C   1 
ATOM   2016  O  O   . SER A  1 277 ? 54.399  83.533 16.682 1.00 46.52 ? 277  SER A O   1 
ATOM   2017  C  CB  . SER A  1 277 ? 57.058  83.597 14.876 1.00 45.40 ? 277  SER A CB  1 
ATOM   2018  O  OG  . SER A  1 277 ? 56.967  84.929 14.400 1.00 45.68 ? 277  SER A OG  1 
ATOM   2019  N  N   . SER A  1 278 ? 55.461  85.513 16.855 1.00 47.52 ? 278  SER A N   1 
ATOM   2020  C  CA  . SER A  1 278 ? 54.252  86.281 17.111 1.00 48.24 ? 278  SER A CA  1 
ATOM   2021  C  C   . SER A  1 278 ? 53.643  86.677 15.773 1.00 48.63 ? 278  SER A C   1 
ATOM   2022  O  O   . SER A  1 278 ? 52.506  87.155 15.707 1.00 49.44 ? 278  SER A O   1 
ATOM   2023  C  CB  . SER A  1 278 ? 54.597  87.544 17.894 1.00 48.26 ? 278  SER A CB  1 
ATOM   2024  O  OG  . SER A  1 278 ? 55.503  87.241 18.943 1.00 50.07 ? 278  SER A OG  1 
ATOM   2025  N  N   . VAL A  1 279 ? 54.403  86.466 14.705 1.00 47.83 ? 279  VAL A N   1 
ATOM   2026  C  CA  . VAL A  1 279 ? 53.945  86.834 13.373 1.00 47.60 ? 279  VAL A CA  1 
ATOM   2027  C  C   . VAL A  1 279 ? 53.568  85.612 12.550 1.00 47.47 ? 279  VAL A C   1 
ATOM   2028  O  O   . VAL A  1 279 ? 52.888  85.725 11.532 1.00 48.48 ? 279  VAL A O   1 
ATOM   2029  C  CB  . VAL A  1 279 ? 55.051  87.614 12.609 1.00 47.85 ? 279  VAL A CB  1 
ATOM   2030  C  CG1 . VAL A  1 279 ? 54.491  88.187 11.310 1.00 48.40 ? 279  VAL A CG1 1 
ATOM   2031  C  CG2 . VAL A  1 279 ? 55.618  88.717 13.490 1.00 47.63 ? 279  VAL A CG2 1 
ATOM   2032  N  N   . THR A  1 280 ? 54.013  84.442 12.987 1.00 46.58 ? 280  THR A N   1 
ATOM   2033  C  CA  . THR A  1 280 ? 53.728  83.227 12.246 1.00 45.88 ? 280  THR A CA  1 
ATOM   2034  C  C   . THR A  1 280 ? 53.161  82.142 13.154 1.00 44.82 ? 280  THR A C   1 
ATOM   2035  O  O   . THR A  1 280 ? 53.552  82.042 14.320 1.00 44.12 ? 280  THR A O   1 
ATOM   2036  C  CB  . THR A  1 280 ? 55.016  82.740 11.566 1.00 46.96 ? 280  THR A CB  1 
ATOM   2037  O  OG1 . THR A  1 280 ? 55.553  83.818 10.788 1.00 47.95 ? 280  THR A OG1 1 
ATOM   2038  C  CG2 . THR A  1 280 ? 54.746  81.542 10.654 1.00 46.21 ? 280  THR A CG2 1 
ATOM   2039  N  N   . ASN A  1 281 ? 52.223  81.354 12.624 1.00 43.70 ? 281  ASN A N   1 
ATOM   2040  C  CA  . ASN A  1 281 ? 51.606  80.272 13.391 1.00 42.89 ? 281  ASN A CA  1 
ATOM   2041  C  C   . ASN A  1 281 ? 52.619  79.157 13.600 1.00 42.29 ? 281  ASN A C   1 
ATOM   2042  O  O   . ASN A  1 281 ? 53.221  78.678 12.642 1.00 43.38 ? 281  ASN A O   1 
ATOM   2043  C  CB  . ASN A  1 281 ? 50.373  79.706 12.672 1.00 42.86 ? 281  ASN A CB  1 
ATOM   2044  C  CG  . ASN A  1 281 ? 49.162  80.607 12.794 1.00 43.66 ? 281  ASN A CG  1 
ATOM   2045  O  OD1 . ASN A  1 281 ? 49.020  81.312 13.802 1.00 44.45 ? 281  ASN A OD1 1 
ATOM   2046  N  ND2 . ASN A  1 281 ? 48.286  80.576 11.782 1.00 44.77 ? 281  ASN A ND2 1 
ATOM   2047  N  N   . ALA A  1 282 ? 52.804  78.757 14.858 1.00 41.47 ? 282  ALA A N   1 
ATOM   2048  C  CA  . ALA A  1 282 ? 53.741  77.697 15.226 1.00 39.27 ? 282  ALA A CA  1 
ATOM   2049  C  C   . ALA A  1 282 ? 53.602  76.503 14.309 1.00 38.34 ? 282  ALA A C   1 
ATOM   2050  O  O   . ALA A  1 282 ? 52.503  76.181 13.865 1.00 37.90 ? 282  ALA A O   1 
ATOM   2051  C  CB  . ALA A  1 282 ? 53.492  77.264 16.657 1.00 39.88 ? 282  ALA A CB  1 
ATOM   2052  N  N   . THR A  1 283 ? 54.714  75.846 14.004 1.00 37.53 ? 283  THR A N   1 
ATOM   2053  C  CA  . THR A  1 283 ? 54.643  74.672 13.146 1.00 37.19 ? 283  THR A CA  1 
ATOM   2054  C  C   . THR A  1 283 ? 54.887  73.427 14.003 1.00 36.79 ? 283  THR A C   1 
ATOM   2055  O  O   . THR A  1 283 ? 55.886  73.343 14.710 1.00 36.67 ? 283  THR A O   1 
ATOM   2056  C  CB  . THR A  1 283 ? 55.686  74.737 12.006 1.00 38.90 ? 283  THR A CB  1 
ATOM   2057  O  OG1 . THR A  1 283 ? 55.458  75.908 11.205 1.00 40.00 ? 283  THR A OG1 1 
ATOM   2058  C  CG2 . THR A  1 283 ? 55.565  73.512 11.122 1.00 38.96 ? 283  THR A CG2 1 
ATOM   2059  N  N   . SER A  1 284 ? 53.951  72.480 13.949 1.00 34.61 ? 284  SER A N   1 
ATOM   2060  C  CA  . SER A  1 284 ? 54.048  71.243 14.706 1.00 32.91 ? 284  SER A CA  1 
ATOM   2061  C  C   . SER A  1 284 ? 54.470  70.124 13.781 1.00 31.74 ? 284  SER A C   1 
ATOM   2062  O  O   . SER A  1 284 ? 53.892  69.950 12.711 1.00 32.35 ? 284  SER A O   1 
ATOM   2063  C  CB  . SER A  1 284 ? 52.697  70.871 15.333 1.00 33.35 ? 284  SER A CB  1 
ATOM   2064  O  OG  . SER A  1 284 ? 52.352  71.731 16.404 1.00 34.47 ? 284  SER A OG  1 
ATOM   2065  N  N   . ILE A  1 285 ? 55.470  69.355 14.194 1.00 30.56 ? 285  ILE A N   1 
ATOM   2066  C  CA  . ILE A  1 285 ? 55.958  68.232 13.393 1.00 29.03 ? 285  ILE A CA  1 
ATOM   2067  C  C   . ILE A  1 285 ? 55.248  66.953 13.848 1.00 29.85 ? 285  ILE A C   1 
ATOM   2068  O  O   . ILE A  1 285 ? 55.227  66.629 15.042 1.00 29.30 ? 285  ILE A O   1 
ATOM   2069  C  CB  . ILE A  1 285 ? 57.484  68.047 13.580 1.00 27.60 ? 285  ILE A CB  1 
ATOM   2070  C  CG1 . ILE A  1 285 ? 58.217  69.338 13.175 1.00 29.36 ? 285  ILE A CG1 1 
ATOM   2071  C  CG2 . ILE A  1 285 ? 57.975  66.883 12.763 1.00 25.77 ? 285  ILE A CG2 1 
ATOM   2072  C  CD1 . ILE A  1 285 ? 58.072  69.700 11.697 1.00 26.53 ? 285  ILE A CD1 1 
ATOM   2073  N  N   . GLN A  1 286 ? 54.682  66.222 12.897 1.00 28.78 ? 286  GLN A N   1 
ATOM   2074  C  CA  . GLN A  1 286 ? 53.996  64.987 13.218 1.00 29.03 ? 286  GLN A CA  1 
ATOM   2075  C  C   . GLN A  1 286 ? 54.895  63.758 13.143 1.00 29.97 ? 286  GLN A C   1 
ATOM   2076  O  O   . GLN A  1 286 ? 55.799  63.671 12.304 1.00 31.16 ? 286  GLN A O   1 
ATOM   2077  C  CB  . GLN A  1 286 ? 52.798  64.781 12.290 1.00 28.17 ? 286  GLN A CB  1 
ATOM   2078  C  CG  . GLN A  1 286 ? 51.956  63.564 12.633 1.00 27.82 ? 286  GLN A CG  1 
ATOM   2079  C  CD  . GLN A  1 286 ? 50.731  63.440 11.738 1.00 29.29 ? 286  GLN A CD  1 
ATOM   2080  O  OE1 . GLN A  1 286 ? 50.461  64.322 10.919 1.00 30.66 ? 286  GLN A OE1 1 
ATOM   2081  N  NE2 . GLN A  1 286 ? 49.978  62.354 11.898 1.00 25.58 ? 286  GLN A NE2 1 
ATOM   2082  N  N   . ILE A  1 287 ? 54.633  62.817 14.045 1.00 28.83 ? 287  ILE A N   1 
ATOM   2083  C  CA  . ILE A  1 287 ? 55.344  61.552 14.114 1.00 28.69 ? 287  ILE A CA  1 
ATOM   2084  C  C   . ILE A  1 287 ? 54.240  60.532 13.947 1.00 28.71 ? 287  ILE A C   1 
ATOM   2085  O  O   . ILE A  1 287 ? 53.380  60.389 14.818 1.00 28.83 ? 287  ILE A O   1 
ATOM   2086  C  CB  . ILE A  1 287 ? 56.008  61.354 15.480 1.00 28.33 ? 287  ILE A CB  1 
ATOM   2087  C  CG1 . ILE A  1 287 ? 57.120  62.376 15.652 1.00 29.44 ? 287  ILE A CG1 1 
ATOM   2088  C  CG2 . ILE A  1 287 ? 56.527  59.951 15.595 1.00 28.37 ? 287  ILE A CG2 1 
ATOM   2089  C  CD1 . ILE A  1 287 ? 57.894  62.249 16.951 1.00 30.86 ? 287  ILE A CD1 1 
ATOM   2090  N  N   . THR A  1 288 ? 54.249  59.838 12.821 1.00 28.26 ? 288  THR A N   1 
ATOM   2091  C  CA  . THR A  1 288 ? 53.221  58.863 12.530 1.00 29.18 ? 288  THR A CA  1 
ATOM   2092  C  C   . THR A  1 288 ? 53.528  57.519 13.177 1.00 29.66 ? 288  THR A C   1 
ATOM   2093  O  O   . THR A  1 288 ? 54.672  57.218 13.503 1.00 28.59 ? 288  THR A O   1 
ATOM   2094  C  CB  . THR A  1 288 ? 53.076  58.714 11.006 1.00 31.07 ? 288  THR A CB  1 
ATOM   2095  O  OG1 . THR A  1 288 ? 54.373  58.522 10.428 1.00 33.86 ? 288  THR A OG1 1 
ATOM   2096  C  CG2 . THR A  1 288 ? 52.481  59.982 10.404 1.00 32.47 ? 288  THR A CG2 1 
ATOM   2097  N  N   . ALA A  1 289 ? 52.497  56.712 13.377 1.00 30.20 ? 289  ALA A N   1 
ATOM   2098  C  CA  . ALA A  1 289 ? 52.684  55.414 14.011 1.00 31.20 ? 289  ALA A CA  1 
ATOM   2099  C  C   . ALA A  1 289 ? 53.212  54.455 12.960 1.00 31.03 ? 289  ALA A C   1 
ATOM   2100  O  O   . ALA A  1 289 ? 53.052  54.701 11.772 1.00 31.70 ? 289  ALA A O   1 
ATOM   2101  C  CB  . ALA A  1 289 ? 51.359  54.919 14.570 1.00 29.30 ? 289  ALA A CB  1 
ATOM   2102  N  N   . PRO A  1 290 ? 53.857  53.359 13.382 1.00 31.61 ? 290  PRO A N   1 
ATOM   2103  C  CA  . PRO A  1 290 ? 54.398  52.376 12.440 1.00 31.43 ? 290  PRO A CA  1 
ATOM   2104  C  C   . PRO A  1 290 ? 53.329  51.704 11.581 1.00 31.96 ? 290  PRO A C   1 
ATOM   2105  O  O   . PRO A  1 290 ? 52.158  51.610 11.977 1.00 30.98 ? 290  PRO A O   1 
ATOM   2106  C  CB  . PRO A  1 290 ? 55.124  51.390 13.352 1.00 31.33 ? 290  PRO A CB  1 
ATOM   2107  C  CG  . PRO A  1 290 ? 54.381  51.505 14.646 1.00 31.34 ? 290  PRO A CG  1 
ATOM   2108  C  CD  . PRO A  1 290 ? 54.188  52.986 14.767 1.00 31.15 ? 290  PRO A CD  1 
ATOM   2109  N  N   . ALA A  1 291 ? 53.745  51.229 10.409 1.00 32.08 ? 291  ALA A N   1 
ATOM   2110  C  CA  . ALA A  1 291 ? 52.842  50.578 9.464  1.00 33.00 ? 291  ALA A CA  1 
ATOM   2111  C  C   . ALA A  1 291 ? 52.067  49.423 10.072 1.00 33.08 ? 291  ALA A C   1 
ATOM   2112  O  O   . ALA A  1 291 ? 50.891  49.234 9.765  1.00 34.41 ? 291  ALA A O   1 
ATOM   2113  C  CB  . ALA A  1 291 ? 53.632  50.081 8.236  1.00 33.42 ? 291  ALA A CB  1 
ATOM   2114  N  N   . SER A  1 292 ? 52.721  48.652 10.935 1.00 32.36 ? 292  SER A N   1 
ATOM   2115  C  CA  . SER A  1 292 ? 52.067  47.507 11.561 1.00 32.35 ? 292  SER A CA  1 
ATOM   2116  C  C   . SER A  1 292 ? 50.927  47.967 12.472 1.00 32.18 ? 292  SER A C   1 
ATOM   2117  O  O   . SER A  1 292 ? 50.145  47.155 12.962 1.00 32.19 ? 292  SER A O   1 
ATOM   2118  C  CB  . SER A  1 292 ? 53.081  46.711 12.379 1.00 32.04 ? 292  SER A CB  1 
ATOM   2119  O  OG  . SER A  1 292 ? 53.546  47.477 13.477 1.00 33.07 ? 292  SER A OG  1 
ATOM   2120  N  N   . MET A  1 293 ? 50.859  49.275 12.691 1.00 30.84 ? 293  MET A N   1 
ATOM   2121  C  CA  . MET A  1 293 ? 49.847  49.879 13.530 1.00 31.70 ? 293  MET A CA  1 
ATOM   2122  C  C   . MET A  1 293 ? 48.787  50.531 12.626 1.00 31.27 ? 293  MET A C   1 
ATOM   2123  O  O   . MET A  1 293 ? 47.586  50.359 12.832 1.00 30.12 ? 293  MET A O   1 
ATOM   2124  C  CB  . MET A  1 293 ? 50.508  50.919 14.441 1.00 31.11 ? 293  MET A CB  1 
ATOM   2125  C  CG  . MET A  1 293 ? 50.063  50.911 15.893 1.00 32.96 ? 293  MET A CG  1 
ATOM   2126  S  SD  . MET A  1 293 ? 50.073  49.320 16.800 1.00 29.99 ? 293  MET A SD  1 
ATOM   2127  C  CE  . MET A  1 293 ? 51.738  49.070 17.125 1.00 33.44 ? 293  MET A CE  1 
ATOM   2128  N  N   . LEU A  1 294 ? 49.235  51.242 11.598 1.00 31.35 ? 294  LEU A N   1 
ATOM   2129  C  CA  . LEU A  1 294 ? 48.321  51.914 10.680 1.00 31.59 ? 294  LEU A CA  1 
ATOM   2130  C  C   . LEU A  1 294 ? 47.408  50.989 9.889  1.00 30.95 ? 294  LEU A C   1 
ATOM   2131  O  O   . LEU A  1 294 ? 46.433  51.439 9.322  1.00 31.10 ? 294  LEU A O   1 
ATOM   2132  C  CB  . LEU A  1 294 ? 49.098  52.795 9.710  1.00 31.45 ? 294  LEU A CB  1 
ATOM   2133  C  CG  . LEU A  1 294 ? 49.856  53.936 10.373 1.00 32.49 ? 294  LEU A CG  1 
ATOM   2134  C  CD1 . LEU A  1 294 ? 50.645  54.674 9.314  1.00 32.50 ? 294  LEU A CD1 1 
ATOM   2135  C  CD2 . LEU A  1 294 ? 48.889  54.876 11.070 1.00 31.91 ? 294  LEU A CD2 1 
ATOM   2136  N  N   . ILE A  1 295 ? 47.704  49.699 9.857  1.00 31.36 ? 295  ILE A N   1 
ATOM   2137  C  CA  . ILE A  1 295 ? 46.850  48.762 9.127  1.00 32.14 ? 295  ILE A CA  1 
ATOM   2138  C  C   . ILE A  1 295 ? 45.429  48.649 9.699  1.00 32.45 ? 295  ILE A C   1 
ATOM   2139  O  O   . ILE A  1 295 ? 44.528  48.124 9.036  1.00 33.18 ? 295  ILE A O   1 
ATOM   2140  C  CB  . ILE A  1 295 ? 47.440  47.344 9.126  1.00 33.16 ? 295  ILE A CB  1 
ATOM   2141  C  CG1 . ILE A  1 295 ? 47.682  46.894 10.567 1.00 32.73 ? 295  ILE A CG1 1 
ATOM   2142  C  CG2 . ILE A  1 295 ? 48.717  47.301 8.293  1.00 34.08 ? 295  ILE A CG2 1 
ATOM   2143  C  CD1 . ILE A  1 295 ? 47.986  45.419 10.688 1.00 33.83 ? 295  ILE A CD1 1 
ATOM   2144  N  N   . GLY A  1 296 ? 45.232  49.111 10.932 1.00 30.81 ? 296  GLY A N   1 
ATOM   2145  C  CA  . GLY A  1 296 ? 43.916  49.032 11.549 1.00 29.63 ? 296  GLY A CA  1 
ATOM   2146  C  C   . GLY A  1 296 ? 43.795  49.912 12.782 1.00 28.38 ? 296  GLY A C   1 
ATOM   2147  O  O   . GLY A  1 296 ? 44.682  50.721 13.060 1.00 27.44 ? 296  GLY A O   1 
ATOM   2148  N  N   . ASP A  1 297 ? 42.702  49.763 13.527 1.00 27.30 ? 297  ASP A N   1 
ATOM   2149  C  CA  . ASP A  1 297 ? 42.514  50.566 14.730 1.00 25.57 ? 297  ASP A CA  1 
ATOM   2150  C  C   . ASP A  1 297 ? 43.697  50.346 15.680 1.00 24.27 ? 297  ASP A C   1 
ATOM   2151  O  O   . ASP A  1 297 ? 44.237  49.245 15.792 1.00 21.55 ? 297  ASP A O   1 
ATOM   2152  C  CB  . ASP A  1 297 ? 41.212  50.194 15.454 1.00 26.69 ? 297  ASP A CB  1 
ATOM   2153  C  CG  . ASP A  1 297 ? 39.960  50.560 14.661 1.00 28.27 ? 297  ASP A CG  1 
ATOM   2154  O  OD1 . ASP A  1 297 ? 40.043  51.417 13.754 1.00 28.73 ? 297  ASP A OD1 1 
ATOM   2155  O  OD2 . ASP A  1 297 ? 38.876  50.002 14.963 1.00 29.49 ? 297  ASP A OD2 1 
ATOM   2156  N  N   . HIS A  1 298 ? 44.088  51.408 16.372 1.00 22.89 ? 298  HIS A N   1 
ATOM   2157  C  CA  . HIS A  1 298 ? 45.196  51.320 17.295 1.00 23.02 ? 298  HIS A CA  1 
ATOM   2158  C  C   . HIS A  1 298 ? 45.083  52.433 18.310 1.00 22.58 ? 298  HIS A C   1 
ATOM   2159  O  O   . HIS A  1 298 ? 44.211  53.298 18.211 1.00 22.98 ? 298  HIS A O   1 
ATOM   2160  C  CB  . HIS A  1 298 ? 46.527  51.439 16.541 1.00 22.01 ? 298  HIS A CB  1 
ATOM   2161  C  CG  . HIS A  1 298 ? 46.646  52.695 15.733 1.00 22.49 ? 298  HIS A CG  1 
ATOM   2162  N  ND1 . HIS A  1 298 ? 46.130  52.813 14.459 1.00 21.10 ? 298  HIS A ND1 1 
ATOM   2163  C  CD2 . HIS A  1 298 ? 47.209  53.891 16.021 1.00 22.49 ? 298  HIS A CD2 1 
ATOM   2164  C  CE1 . HIS A  1 298 ? 46.374  54.025 13.998 1.00 21.94 ? 298  HIS A CE1 1 
ATOM   2165  N  NE2 . HIS A  1 298 ? 47.028  54.700 14.925 1.00 22.95 ? 298  HIS A NE2 1 
ATOM   2166  N  N   . TYR A  1 299 ? 46.003  52.414 19.267 1.00 22.13 ? 299  TYR A N   1 
ATOM   2167  C  CA  . TYR A  1 299 ? 46.045  53.388 20.346 1.00 21.02 ? 299  TYR A CA  1 
ATOM   2168  C  C   . TYR A  1 299 ? 47.477  53.847 20.579 1.00 20.91 ? 299  TYR A C   1 
ATOM   2169  O  O   . TYR A  1 299 ? 48.426  53.120 20.277 1.00 19.74 ? 299  TYR A O   1 
ATOM   2170  C  CB  . TYR A  1 299 ? 45.603  52.758 21.684 1.00 19.99 ? 299  TYR A CB  1 
ATOM   2171  C  CG  . TYR A  1 299 ? 44.254  52.081 21.723 1.00 20.88 ? 299  TYR A CG  1 
ATOM   2172  C  CD1 . TYR A  1 299 ? 43.074  52.822 21.642 1.00 20.18 ? 299  TYR A CD1 1 
ATOM   2173  C  CD2 . TYR A  1 299 ? 44.156  50.697 21.867 1.00 20.18 ? 299  TYR A CD2 1 
ATOM   2174  C  CE1 . TYR A  1 299 ? 41.835  52.198 21.707 1.00 22.03 ? 299  TYR A CE1 1 
ATOM   2175  C  CE2 . TYR A  1 299 ? 42.924  50.069 21.931 1.00 20.93 ? 299  TYR A CE2 1 
ATOM   2176  C  CZ  . TYR A  1 299 ? 41.769  50.820 21.853 1.00 20.53 ? 299  TYR A CZ  1 
ATOM   2177  O  OH  . TYR A  1 299 ? 40.547  50.203 21.949 1.00 21.05 ? 299  TYR A OH  1 
ATOM   2178  N  N   . LEU A  1 300 ? 47.612  55.051 21.142 1.00 20.27 ? 300  LEU A N   1 
ATOM   2179  C  CA  . LEU A  1 300 ? 48.902  55.568 21.549 1.00 20.06 ? 300  LEU A CA  1 
ATOM   2180  C  C   . LEU A  1 300 ? 48.824  55.211 23.046 1.00 20.60 ? 300  LEU A C   1 
ATOM   2181  O  O   . LEU A  1 300 ? 47.901  55.644 23.737 1.00 20.66 ? 300  LEU A O   1 
ATOM   2182  C  CB  . LEU A  1 300 ? 48.970  57.080 21.357 1.00 19.20 ? 300  LEU A CB  1 
ATOM   2183  C  CG  . LEU A  1 300 ? 50.211  57.728 21.986 1.00 20.53 ? 300  LEU A CG  1 
ATOM   2184  C  CD1 . LEU A  1 300 ? 51.470  57.291 21.242 1.00 18.02 ? 300  LEU A CD1 1 
ATOM   2185  C  CD2 . LEU A  1 300 ? 50.057  59.244 21.966 1.00 20.17 ? 300  LEU A CD2 1 
ATOM   2186  N  N   . CYS A  1 301 ? 49.756  54.417 23.559 1.00 21.60 ? 301  CYS A N   1 
ATOM   2187  C  CA  . CYS A  1 301 ? 49.660  54.011 24.970 1.00 22.61 ? 301  CYS A CA  1 
ATOM   2188  C  C   . CYS A  1 301 ? 50.738  54.510 25.919 1.00 22.28 ? 301  CYS A C   1 
ATOM   2189  O  O   . CYS A  1 301 ? 50.611  54.358 27.126 1.00 22.62 ? 301  CYS A O   1 
ATOM   2190  C  CB  . CYS A  1 301 ? 49.560  52.482 25.070 1.00 22.84 ? 301  CYS A CB  1 
ATOM   2191  S  SG  . CYS A  1 301 ? 50.883  51.573 24.214 1.00 26.63 ? 301  CYS A SG  1 
ATOM   2192  N  N   . ASP A  1 302 ? 51.795  55.102 25.375 1.00 22.80 ? 302  ASP A N   1 
ATOM   2193  C  CA  . ASP A  1 302 ? 52.865  55.646 26.203 1.00 22.66 ? 302  ASP A CA  1 
ATOM   2194  C  C   . ASP A  1 302 ? 53.750  56.639 25.458 1.00 22.56 ? 302  ASP A C   1 
ATOM   2195  O  O   . ASP A  1 302 ? 54.015  56.492 24.269 1.00 22.04 ? 302  ASP A O   1 
ATOM   2196  C  CB  . ASP A  1 302 ? 53.757  54.532 26.768 1.00 22.23 ? 302  ASP A CB  1 
ATOM   2197  C  CG  . ASP A  1 302 ? 54.815  55.070 27.723 1.00 24.37 ? 302  ASP A CG  1 
ATOM   2198  O  OD1 . ASP A  1 302 ? 55.909  55.490 27.277 1.00 26.68 ? 302  ASP A OD1 1 
ATOM   2199  O  OD2 . ASP A  1 302 ? 54.537  55.096 28.932 1.00 24.29 ? 302  ASP A OD2 1 
ATOM   2200  N  N   . VAL A  1 303 ? 54.186  57.663 26.178 1.00 22.81 ? 303  VAL A N   1 
ATOM   2201  C  CA  . VAL A  1 303 ? 55.078  58.673 25.641 1.00 21.53 ? 303  VAL A CA  1 
ATOM   2202  C  C   . VAL A  1 303 ? 56.065  58.956 26.762 1.00 22.25 ? 303  VAL A C   1 
ATOM   2203  O  O   . VAL A  1 303 ? 55.680  59.342 27.880 1.00 21.58 ? 303  VAL A O   1 
ATOM   2204  C  CB  . VAL A  1 303 ? 54.354  59.999 25.280 1.00 21.91 ? 303  VAL A CB  1 
ATOM   2205  C  CG1 . VAL A  1 303 ? 55.391  61.045 24.816 1.00 20.08 ? 303  VAL A CG1 1 
ATOM   2206  C  CG2 . VAL A  1 303 ? 53.312  59.763 24.185 1.00 19.19 ? 303  VAL A CG2 1 
ATOM   2207  N  N   . THR A  1 304 ? 57.340  58.744 26.470 1.00 23.20 ? 304  THR A N   1 
ATOM   2208  C  CA  . THR A  1 304 ? 58.396  58.969 27.453 1.00 22.51 ? 304  THR A CA  1 
ATOM   2209  C  C   . THR A  1 304 ? 59.609  59.552 26.740 1.00 23.87 ? 304  THR A C   1 
ATOM   2210  O  O   . THR A  1 304 ? 60.085  58.981 25.764 1.00 24.57 ? 304  THR A O   1 
ATOM   2211  C  CB  . THR A  1 304 ? 58.830  57.646 28.126 1.00 22.53 ? 304  THR A CB  1 
ATOM   2212  O  OG1 . THR A  1 304 ? 57.705  57.026 28.771 1.00 22.13 ? 304  THR A OG1 1 
ATOM   2213  C  CG2 . THR A  1 304 ? 59.921  57.924 29.162 1.00 22.24 ? 304  THR A CG2 1 
ATOM   2214  N  N   . TRP A  1 305 ? 60.102  60.688 27.218 1.00 24.47 ? 305  TRP A N   1 
ATOM   2215  C  CA  . TRP A  1 305 ? 61.283  61.303 26.623 1.00 24.56 ? 305  TRP A CA  1 
ATOM   2216  C  C   . TRP A  1 305 ? 62.528  60.552 27.093 1.00 23.91 ? 305  TRP A C   1 
ATOM   2217  O  O   . TRP A  1 305 ? 62.599  60.128 28.244 1.00 23.19 ? 305  TRP A O   1 
ATOM   2218  C  CB  . TRP A  1 305 ? 61.409  62.780 27.039 1.00 24.57 ? 305  TRP A CB  1 
ATOM   2219  C  CG  . TRP A  1 305 ? 60.544  63.713 26.255 1.00 26.40 ? 305  TRP A CG  1 
ATOM   2220  C  CD1 . TRP A  1 305 ? 59.267  64.099 26.555 1.00 26.68 ? 305  TRP A CD1 1 
ATOM   2221  C  CD2 . TRP A  1 305 ? 60.867  64.333 25.003 1.00 27.09 ? 305  TRP A CD2 1 
ATOM   2222  N  NE1 . TRP A  1 305 ? 58.774  64.916 25.565 1.00 27.26 ? 305  TRP A NE1 1 
ATOM   2223  C  CE2 . TRP A  1 305 ? 59.734  65.077 24.601 1.00 27.99 ? 305  TRP A CE2 1 
ATOM   2224  C  CE3 . TRP A  1 305 ? 62.005  64.330 24.180 1.00 26.89 ? 305  TRP A CE3 1 
ATOM   2225  C  CZ2 . TRP A  1 305 ? 59.703  65.813 23.409 1.00 27.65 ? 305  TRP A CZ2 1 
ATOM   2226  C  CZ3 . TRP A  1 305 ? 61.975  65.059 22.995 1.00 26.26 ? 305  TRP A CZ3 1 
ATOM   2227  C  CH2 . TRP A  1 305 ? 60.829  65.791 22.622 1.00 28.01 ? 305  TRP A CH2 1 
ATOM   2228  N  N   . ALA A  1 306 ? 63.500  60.387 26.201 1.00 25.01 ? 306  ALA A N   1 
ATOM   2229  C  CA  . ALA A  1 306 ? 64.752  59.710 26.534 1.00 24.73 ? 306  ALA A CA  1 
ATOM   2230  C  C   . ALA A  1 306 ? 65.820  60.774 26.779 1.00 25.74 ? 306  ALA A C   1 
ATOM   2231  O  O   . ALA A  1 306 ? 66.553  60.706 27.769 1.00 26.58 ? 306  ALA A O   1 
ATOM   2232  C  CB  . ALA A  1 306 ? 65.186  58.790 25.394 1.00 23.64 ? 306  ALA A CB  1 
ATOM   2233  N  N   . THR A  1 307 ? 65.907  61.754 25.877 1.00 25.23 ? 307  THR A N   1 
ATOM   2234  C  CA  . THR A  1 307 ? 66.889  62.833 26.015 1.00 25.02 ? 307  THR A CA  1 
ATOM   2235  C  C   . THR A  1 307 ? 66.330  64.136 25.467 1.00 26.02 ? 307  THR A C   1 
ATOM   2236  O  O   . THR A  1 307 ? 65.179  64.198 25.036 1.00 25.94 ? 307  THR A O   1 
ATOM   2237  C  CB  . THR A  1 307 ? 68.166  62.560 25.219 1.00 24.53 ? 307  THR A CB  1 
ATOM   2238  O  OG1 . THR A  1 307 ? 67.889  62.784 23.832 1.00 22.66 ? 307  THR A OG1 1 
ATOM   2239  C  CG2 . THR A  1 307 ? 68.644  61.104 25.415 1.00 24.55 ? 307  THR A CG2 1 
ATOM   2240  N  N   . GLN A  1 308 ? 67.170  65.169 25.453 1.00 26.95 ? 308  GLN A N   1 
ATOM   2241  C  CA  . GLN A  1 308 ? 66.756  66.466 24.944 1.00 27.37 ? 308  GLN A CA  1 
ATOM   2242  C  C   . GLN A  1 308 ? 66.300  66.364 23.496 1.00 27.20 ? 308  GLN A C   1 
ATOM   2243  O  O   . GLN A  1 308 ? 65.492  67.174 23.053 1.00 28.96 ? 308  GLN A O   1 
ATOM   2244  C  CB  . GLN A  1 308 ? 67.905  67.483 25.027 1.00 28.18 ? 308  GLN A CB  1 
ATOM   2245  C  CG  . GLN A  1 308 ? 68.493  67.700 26.415 1.00 26.92 ? 308  GLN A CG  1 
ATOM   2246  C  CD  . GLN A  1 308 ? 67.446  68.091 27.438 1.00 28.36 ? 308  GLN A CD  1 
ATOM   2247  O  OE1 . GLN A  1 308 ? 66.311  68.405 27.084 1.00 28.11 ? 308  GLN A OE1 1 
ATOM   2248  N  NE2 . GLN A  1 308 ? 67.827  68.082 28.720 1.00 27.04 ? 308  GLN A NE2 1 
ATOM   2249  N  N   . GLU A  1 309 ? 66.792  65.369 22.761 1.00 26.68 ? 309  GLU A N   1 
ATOM   2250  C  CA  . GLU A  1 309 ? 66.425  65.252 21.348 1.00 27.16 ? 309  GLU A CA  1 
ATOM   2251  C  C   . GLU A  1 309 ? 65.975  63.861 20.889 1.00 26.42 ? 309  GLU A C   1 
ATOM   2252  O  O   . GLU A  1 309 ? 66.019  63.542 19.697 1.00 26.29 ? 309  GLU A O   1 
ATOM   2253  C  CB  . GLU A  1 309 ? 67.601  65.732 20.482 1.00 29.48 ? 309  GLU A CB  1 
ATOM   2254  C  CG  . GLU A  1 309 ? 67.982  67.209 20.705 1.00 32.11 ? 309  GLU A CG  1 
ATOM   2255  C  CD  . GLU A  1 309 ? 69.273  67.623 19.978 1.00 34.75 ? 309  GLU A CD  1 
ATOM   2256  O  OE1 . GLU A  1 309 ? 69.510  67.149 18.847 1.00 36.14 ? 309  GLU A OE1 1 
ATOM   2257  O  OE2 . GLU A  1 309 ? 70.035  68.445 20.530 1.00 36.04 ? 309  GLU A OE2 1 
ATOM   2258  N  N   . ARG A  1 310 ? 65.522  63.045 21.835 1.00 26.30 ? 310  ARG A N   1 
ATOM   2259  C  CA  . ARG A  1 310 ? 65.063  61.691 21.539 1.00 25.92 ? 310  ARG A CA  1 
ATOM   2260  C  C   . ARG A  1 310 ? 63.807  61.386 22.353 1.00 25.88 ? 310  ARG A C   1 
ATOM   2261  O  O   . ARG A  1 310 ? 63.795  61.519 23.587 1.00 25.38 ? 310  ARG A O   1 
ATOM   2262  C  CB  . ARG A  1 310 ? 66.171  60.684 21.877 1.00 25.15 ? 310  ARG A CB  1 
ATOM   2263  C  CG  . ARG A  1 310 ? 65.796  59.195 21.705 1.00 26.08 ? 310  ARG A CG  1 
ATOM   2264  C  CD  . ARG A  1 310 ? 67.033  58.305 21.959 1.00 25.75 ? 310  ARG A CD  1 
ATOM   2265  N  NE  . ARG A  1 310 ? 68.070  58.561 20.955 1.00 27.24 ? 310  ARG A NE  1 
ATOM   2266  C  CZ  . ARG A  1 310 ? 69.375  58.364 21.127 1.00 28.58 ? 310  ARG A CZ  1 
ATOM   2267  N  NH1 . ARG A  1 310 ? 69.857  57.894 22.284 1.00 26.24 ? 310  ARG A NH1 1 
ATOM   2268  N  NH2 . ARG A  1 310 ? 70.206  58.654 20.131 1.00 27.19 ? 310  ARG A NH2 1 
ATOM   2269  N  N   . ILE A  1 311 ? 62.756  60.969 21.662 1.00 24.97 ? 311  ILE A N   1 
ATOM   2270  C  CA  . ILE A  1 311 ? 61.499  60.640 22.318 1.00 24.44 ? 311  ILE A CA  1 
ATOM   2271  C  C   . ILE A  1 311 ? 61.034  59.226 21.938 1.00 25.09 ? 311  ILE A C   1 
ATOM   2272  O  O   . ILE A  1 311 ? 61.236  58.776 20.809 1.00 24.58 ? 311  ILE A O   1 
ATOM   2273  C  CB  . ILE A  1 311 ? 60.420  61.664 21.920 1.00 24.19 ? 311  ILE A CB  1 
ATOM   2274  C  CG1 . ILE A  1 311 ? 59.172  61.511 22.792 1.00 23.57 ? 311  ILE A CG1 1 
ATOM   2275  C  CG2 . ILE A  1 311 ? 60.061  61.484 20.466 1.00 23.21 ? 311  ILE A CG2 1 
ATOM   2276  C  CD1 . ILE A  1 311 ? 58.162  62.607 22.559 1.00 23.07 ? 311  ILE A CD1 1 
ATOM   2277  N  N   . SER A  1 312 ? 60.448  58.496 22.886 1.00 24.59 ? 312  SER A N   1 
ATOM   2278  C  CA  . SER A  1 312 ? 59.943  57.164 22.569 1.00 23.77 ? 312  SER A CA  1 
ATOM   2279  C  C   . SER A  1 312 ? 58.431  57.157 22.728 1.00 25.10 ? 312  SER A C   1 
ATOM   2280  O  O   . SER A  1 312 ? 57.871  57.877 23.565 1.00 25.25 ? 312  SER A O   1 
ATOM   2281  C  CB  . SER A  1 312 ? 60.562  56.090 23.473 1.00 23.86 ? 312  SER A CB  1 
ATOM   2282  O  OG  . SER A  1 312 ? 60.067  56.131 24.796 1.00 23.52 ? 312  SER A OG  1 
ATOM   2283  N  N   . LEU A  1 313 ? 57.777  56.341 21.909 1.00 25.36 ? 313  LEU A N   1 
ATOM   2284  C  CA  . LEU A  1 313 ? 56.332  56.207 21.926 1.00 25.09 ? 313  LEU A CA  1 
ATOM   2285  C  C   . LEU A  1 313 ? 55.982  54.744 21.753 1.00 25.28 ? 313  LEU A C   1 
ATOM   2286  O  O   . LEU A  1 313 ? 56.605  54.047 20.949 1.00 25.28 ? 313  LEU A O   1 
ATOM   2287  C  CB  . LEU A  1 313 ? 55.693  56.929 20.752 1.00 26.45 ? 313  LEU A CB  1 
ATOM   2288  C  CG  . LEU A  1 313 ? 56.239  58.249 20.273 1.00 28.39 ? 313  LEU A CG  1 
ATOM   2289  C  CD1 . LEU A  1 313 ? 55.570  58.586 18.952 1.00 29.81 ? 313  LEU A CD1 1 
ATOM   2290  C  CD2 . LEU A  1 313 ? 55.993  59.324 21.322 1.00 29.99 ? 313  LEU A CD2 1 
ATOM   2291  N  N   . GLN A  1 314 ? 54.983  54.285 22.500 1.00 22.74 ? 314  GLN A N   1 
ATOM   2292  C  CA  . GLN A  1 314 ? 54.510  52.921 22.345 1.00 23.45 ? 314  GLN A CA  1 
ATOM   2293  C  C   . GLN A  1 314 ? 53.081  52.986 21.760 1.00 23.15 ? 314  GLN A C   1 
ATOM   2294  O  O   . GLN A  1 314 ? 52.255  53.810 22.195 1.00 21.67 ? 314  GLN A O   1 
ATOM   2295  C  CB  . GLN A  1 314 ? 54.527  52.179 23.687 1.00 23.58 ? 314  GLN A CB  1 
ATOM   2296  C  CG  . GLN A  1 314 ? 55.927  51.734 24.109 1.00 25.10 ? 314  GLN A CG  1 
ATOM   2297  C  CD  . GLN A  1 314 ? 55.983  51.196 25.528 1.00 25.83 ? 314  GLN A CD  1 
ATOM   2298  O  OE1 . GLN A  1 314 ? 56.172  51.950 26.496 1.00 25.15 ? 314  GLN A OE1 1 
ATOM   2299  N  NE2 . GLN A  1 314 ? 55.818  49.878 25.662 1.00 26.74 ? 314  GLN A NE2 1 
ATOM   2300  N  N   . TRP A  1 315 ? 52.824  52.151 20.752 1.00 21.03 ? 315  TRP A N   1 
ATOM   2301  C  CA  . TRP A  1 315 ? 51.523  52.063 20.105 1.00 21.30 ? 315  TRP A CA  1 
ATOM   2302  C  C   . TRP A  1 315 ? 50.979  50.664 20.359 1.00 21.59 ? 315  TRP A C   1 
ATOM   2303  O  O   . TRP A  1 315 ? 51.728  49.701 20.459 1.00 22.91 ? 315  TRP A O   1 
ATOM   2304  C  CB  . TRP A  1 315 ? 51.625  52.292 18.596 1.00 22.01 ? 315  TRP A CB  1 
ATOM   2305  C  CG  . TRP A  1 315 ? 52.205  53.624 18.192 1.00 23.31 ? 315  TRP A CG  1 
ATOM   2306  C  CD1 . TRP A  1 315 ? 53.518  53.918 18.004 1.00 23.59 ? 315  TRP A CD1 1 
ATOM   2307  C  CD2 . TRP A  1 315 ? 51.479  54.829 17.911 1.00 23.18 ? 315  TRP A CD2 1 
ATOM   2308  N  NE1 . TRP A  1 315 ? 53.663  55.229 17.616 1.00 23.67 ? 315  TRP A NE1 1 
ATOM   2309  C  CE2 . TRP A  1 315 ? 52.425  55.810 17.549 1.00 23.66 ? 315  TRP A CE2 1 
ATOM   2310  C  CE3 . TRP A  1 315 ? 50.119  55.170 17.924 1.00 23.77 ? 315  TRP A CE3 1 
ATOM   2311  C  CZ2 . TRP A  1 315 ? 52.060  57.115 17.202 1.00 23.02 ? 315  TRP A CZ2 1 
ATOM   2312  C  CZ3 . TRP A  1 315 ? 49.754  56.463 17.579 1.00 23.45 ? 315  TRP A CZ3 1 
ATOM   2313  C  CH2 . TRP A  1 315 ? 50.722  57.422 17.221 1.00 22.95 ? 315  TRP A CH2 1 
ATOM   2314  N  N   . LEU A  1 316 ? 49.669  50.555 20.453 1.00 21.70 ? 316  LEU A N   1 
ATOM   2315  C  CA  . LEU A  1 316 ? 49.030  49.286 20.730 1.00 22.10 ? 316  LEU A CA  1 
ATOM   2316  C  C   . LEU A  1 316 ? 47.894  49.061 19.735 1.00 24.22 ? 316  LEU A C   1 
ATOM   2317  O  O   . LEU A  1 316 ? 47.130  49.979 19.450 1.00 24.18 ? 316  LEU A O   1 
ATOM   2318  C  CB  . LEU A  1 316 ? 48.455  49.313 22.153 1.00 20.06 ? 316  LEU A CB  1 
ATOM   2319  C  CG  . LEU A  1 316 ? 47.783  48.068 22.744 1.00 18.68 ? 316  LEU A CG  1 
ATOM   2320  C  CD1 . LEU A  1 316 ? 48.797  46.941 22.894 1.00 17.78 ? 316  LEU A CD1 1 
ATOM   2321  C  CD2 . LEU A  1 316 ? 47.191  48.444 24.112 1.00 18.09 ? 316  LEU A CD2 1 
ATOM   2322  N  N   . ARG A  1 317 ? 47.783  47.845 19.206 1.00 24.33 ? 317  ARG A N   1 
ATOM   2323  C  CA  . ARG A  1 317 ? 46.699  47.547 18.287 1.00 25.83 ? 317  ARG A CA  1 
ATOM   2324  C  C   . ARG A  1 317 ? 45.404  47.407 19.083 1.00 26.14 ? 317  ARG A C   1 
ATOM   2325  O  O   . ARG A  1 317 ? 45.435  47.112 20.290 1.00 26.43 ? 317  ARG A O   1 
ATOM   2326  C  CB  . ARG A  1 317 ? 46.971  46.242 17.530 1.00 27.23 ? 317  ARG A CB  1 
ATOM   2327  C  CG  . ARG A  1 317 ? 48.025  46.363 16.428 1.00 30.12 ? 317  ARG A CG  1 
ATOM   2328  C  CD  . ARG A  1 317 ? 48.149  45.046 15.694 1.00 32.05 ? 317  ARG A CD  1 
ATOM   2329  N  NE  . ARG A  1 317 ? 48.999  45.152 14.506 1.00 35.07 ? 317  ARG A NE  1 
ATOM   2330  C  CZ  . ARG A  1 317 ? 49.667  44.126 13.985 1.00 36.11 ? 317  ARG A CZ  1 
ATOM   2331  N  NH1 . ARG A  1 317 ? 49.589  42.923 14.547 1.00 35.51 ? 317  ARG A NH1 1 
ATOM   2332  N  NH2 . ARG A  1 317 ? 50.409  44.301 12.905 1.00 37.62 ? 317  ARG A NH2 1 
ATOM   2333  N  N   . ARG A  1 318 ? 44.267  47.613 18.424 1.00 25.67 ? 318  ARG A N   1 
ATOM   2334  C  CA  . ARG A  1 318 ? 42.988  47.471 19.111 1.00 24.91 ? 318  ARG A CA  1 
ATOM   2335  C  C   . ARG A  1 318 ? 42.912  46.072 19.742 1.00 24.49 ? 318  ARG A C   1 
ATOM   2336  O  O   . ARG A  1 318 ? 42.338  45.914 20.822 1.00 23.70 ? 318  ARG A O   1 
ATOM   2337  C  CB  . ARG A  1 318 ? 41.819  47.736 18.153 1.00 24.27 ? 318  ARG A CB  1 
ATOM   2338  C  CG  . ARG A  1 318 ? 40.471  47.765 18.880 1.00 23.57 ? 318  ARG A CG  1 
ATOM   2339  C  CD  . ARG A  1 318 ? 39.418  48.621 18.159 1.00 21.24 ? 318  ARG A CD  1 
ATOM   2340  N  NE  . ARG A  1 318 ? 38.131  48.506 18.847 1.00 22.45 ? 318  ARG A NE  1 
ATOM   2341  C  CZ  . ARG A  1 318 ? 37.045  49.203 18.534 1.00 22.42 ? 318  ARG A CZ  1 
ATOM   2342  N  NH1 . ARG A  1 318 ? 37.086  50.072 17.534 1.00 21.35 ? 318  ARG A NH1 1 
ATOM   2343  N  NH2 . ARG A  1 318 ? 35.929  49.045 19.236 1.00 20.59 ? 318  ARG A NH2 1 
ATOM   2344  N  N   . ILE A  1 319 ? 43.480  45.063 19.072 1.00 24.06 ? 319  ILE A N   1 
ATOM   2345  C  CA  . ILE A  1 319 ? 43.551  43.708 19.637 1.00 23.30 ? 319  ILE A CA  1 
ATOM   2346  C  C   . ILE A  1 319 ? 44.816  43.863 20.452 1.00 24.28 ? 319  ILE A C   1 
ATOM   2347  O  O   . ILE A  1 319 ? 45.919  43.796 19.915 1.00 23.73 ? 319  ILE A O   1 
ATOM   2348  C  CB  . ILE A  1 319 ? 43.785  42.638 18.574 1.00 23.80 ? 319  ILE A CB  1 
ATOM   2349  C  CG1 . ILE A  1 319 ? 42.652  42.678 17.560 1.00 23.53 ? 319  ILE A CG1 1 
ATOM   2350  C  CG2 . ILE A  1 319 ? 43.852  41.249 19.231 1.00 22.45 ? 319  ILE A CG2 1 
ATOM   2351  C  CD1 . ILE A  1 319 ? 41.307  42.490 18.191 1.00 26.00 ? 319  ILE A CD1 1 
ATOM   2352  N  N   . GLN A  1 320 ? 44.639  44.081 21.751 1.00 24.76 ? 320  GLN A N   1 
ATOM   2353  C  CA  . GLN A  1 320 ? 45.740  44.383 22.660 1.00 24.96 ? 320  GLN A CA  1 
ATOM   2354  C  C   . GLN A  1 320 ? 46.785  43.352 23.065 1.00 25.69 ? 320  GLN A C   1 
ATOM   2355  O  O   . GLN A  1 320 ? 47.250  43.342 24.208 1.00 26.94 ? 320  GLN A O   1 
ATOM   2356  C  CB  . GLN A  1 320 ? 45.151  45.043 23.905 1.00 22.68 ? 320  GLN A CB  1 
ATOM   2357  C  CG  . GLN A  1 320 ? 44.316  46.267 23.554 1.00 22.21 ? 320  GLN A CG  1 
ATOM   2358  C  CD  . GLN A  1 320 ? 43.707  46.918 24.767 1.00 20.41 ? 320  GLN A CD  1 
ATOM   2359  O  OE1 . GLN A  1 320 ? 44.390  47.148 25.761 1.00 21.60 ? 320  GLN A OE1 1 
ATOM   2360  N  NE2 . GLN A  1 320 ? 42.421  47.227 24.694 1.00 19.59 ? 320  GLN A NE2 1 
ATOM   2361  N  N   . ASN A  1 321 ? 47.195  42.527 22.114 1.00 26.91 ? 321  ASN A N   1 
ATOM   2362  C  CA  . ASN A  1 321 ? 48.218  41.521 22.366 1.00 28.24 ? 321  ASN A CA  1 
ATOM   2363  C  C   . ASN A  1 321 ? 49.484  41.859 21.559 1.00 28.17 ? 321  ASN A C   1 
ATOM   2364  O  O   . ASN A  1 321 ? 50.411  41.055 21.482 1.00 28.79 ? 321  ASN A O   1 
ATOM   2365  C  CB  . ASN A  1 321 ? 47.710  40.134 21.949 1.00 31.98 ? 321  ASN A CB  1 
ATOM   2366  C  CG  . ASN A  1 321 ? 47.336  40.073 20.476 1.00 33.88 ? 321  ASN A CG  1 
ATOM   2367  O  OD1 . ASN A  1 321 ? 47.851  40.844 19.670 1.00 34.87 ? 321  ASN A OD1 1 
ATOM   2368  N  ND2 . ASN A  1 321 ? 46.440  39.172 20.103 1.00 40.25 ? 321  ASN A ND2 1 
ATOM   2369  N  N   . TYR A  1 322 ? 49.532  43.044 20.964 1.00 27.72 ? 322  TYR A N   1 
ATOM   2370  C  CA  . TYR A  1 322 ? 50.686  43.425 20.151 1.00 27.08 ? 322  TYR A CA  1 
ATOM   2371  C  C   . TYR A  1 322 ? 50.945  44.935 20.226 1.00 26.71 ? 322  TYR A C   1 
ATOM   2372  O  O   . TYR A  1 322 ? 50.082  45.731 19.882 1.00 26.22 ? 322  TYR A O   1 
ATOM   2373  C  CB  . TYR A  1 322 ? 50.416  42.994 18.705 1.00 28.52 ? 322  TYR A CB  1 
ATOM   2374  C  CG  . TYR A  1 322 ? 51.569  43.159 17.740 1.00 30.44 ? 322  TYR A CG  1 
ATOM   2375  C  CD1 . TYR A  1 322 ? 51.846  44.390 17.146 1.00 30.31 ? 322  TYR A CD1 1 
ATOM   2376  C  CD2 . TYR A  1 322 ? 52.383  42.068 17.409 1.00 31.08 ? 322  TYR A CD2 1 
ATOM   2377  C  CE1 . TYR A  1 322 ? 52.903  44.533 16.244 1.00 31.43 ? 322  TYR A CE1 1 
ATOM   2378  C  CE2 . TYR A  1 322 ? 53.443  42.206 16.512 1.00 31.72 ? 322  TYR A CE2 1 
ATOM   2379  C  CZ  . TYR A  1 322 ? 53.695  43.437 15.934 1.00 32.15 ? 322  TYR A CZ  1 
ATOM   2380  O  OH  . TYR A  1 322 ? 54.745  43.567 15.048 1.00 34.33 ? 322  TYR A OH  1 
ATOM   2381  N  N   . SER A  1 323 ? 52.125  45.331 20.691 1.00 26.43 ? 323  SER A N   1 
ATOM   2382  C  CA  . SER A  1 323 ? 52.449  46.748 20.786 1.00 27.61 ? 323  SER A CA  1 
ATOM   2383  C  C   . SER A  1 323 ? 53.831  47.002 20.222 1.00 27.66 ? 323  SER A C   1 
ATOM   2384  O  O   . SER A  1 323 ? 54.675  46.108 20.203 1.00 26.53 ? 323  SER A O   1 
ATOM   2385  C  CB  . SER A  1 323 ? 52.382  47.241 22.235 1.00 28.08 ? 323  SER A CB  1 
ATOM   2386  O  OG  . SER A  1 323 ? 53.332  46.568 23.037 1.00 28.71 ? 323  SER A OG  1 
ATOM   2387  N  N   . VAL A  1 324 ? 54.052  48.233 19.769 1.00 27.55 ? 324  VAL A N   1 
ATOM   2388  C  CA  . VAL A  1 324 ? 55.316  48.613 19.163 1.00 27.67 ? 324  VAL A CA  1 
ATOM   2389  C  C   . VAL A  1 324 ? 55.862  49.922 19.727 1.00 27.09 ? 324  VAL A C   1 
ATOM   2390  O  O   . VAL A  1 324 ? 55.142  50.919 19.813 1.00 26.69 ? 324  VAL A O   1 
ATOM   2391  C  CB  . VAL A  1 324 ? 55.153  48.780 17.617 1.00 28.03 ? 324  VAL A CB  1 
ATOM   2392  C  CG1 . VAL A  1 324 ? 56.465  49.201 16.996 1.00 28.38 ? 324  VAL A CG1 1 
ATOM   2393  C  CG2 . VAL A  1 324 ? 54.688  47.478 16.990 1.00 28.56 ? 324  VAL A CG2 1 
ATOM   2394  N  N   . MET A  1 325 ? 57.140  49.914 20.101 1.00 26.19 ? 325  MET A N   1 
ATOM   2395  C  CA  . MET A  1 325 ? 57.791  51.117 20.618 1.00 25.75 ? 325  MET A CA  1 
ATOM   2396  C  C   . MET A  1 325 ? 58.662  51.703 19.518 1.00 26.27 ? 325  MET A C   1 
ATOM   2397  O  O   . MET A  1 325 ? 59.469  50.989 18.897 1.00 25.57 ? 325  MET A O   1 
ATOM   2398  C  CB  . MET A  1 325 ? 58.681  50.812 21.844 1.00 24.54 ? 325  MET A CB  1 
ATOM   2399  C  CG  . MET A  1 325 ? 59.474  52.028 22.374 1.00 24.95 ? 325  MET A CG  1 
ATOM   2400  S  SD  . MET A  1 325 ? 60.689  51.605 23.668 1.00 26.25 ? 325  MET A SD  1 
ATOM   2401  C  CE  . MET A  1 325 ? 60.842  53.042 24.547 1.00 26.78 ? 325  MET A CE  1 
ATOM   2402  N  N   . ASP A  1 326 ? 58.483  52.998 19.272 1.00 25.71 ? 326  ASP A N   1 
ATOM   2403  C  CA  . ASP A  1 326 ? 59.281  53.718 18.287 1.00 26.49 ? 326  ASP A CA  1 
ATOM   2404  C  C   . ASP A  1 326 ? 60.187  54.676 19.061 1.00 27.56 ? 326  ASP A C   1 
ATOM   2405  O  O   . ASP A  1 326 ? 59.758  55.291 20.044 1.00 26.89 ? 326  ASP A O   1 
ATOM   2406  C  CB  . ASP A  1 326 ? 58.389  54.523 17.340 1.00 27.71 ? 326  ASP A CB  1 
ATOM   2407  C  CG  . ASP A  1 326 ? 58.454  54.025 15.906 1.00 30.16 ? 326  ASP A CG  1 
ATOM   2408  O  OD1 . ASP A  1 326 ? 59.335  53.194 15.590 1.00 32.45 ? 326  ASP A OD1 1 
ATOM   2409  O  OD2 . ASP A  1 326 ? 57.630  54.473 15.081 1.00 30.60 ? 326  ASP A OD2 1 
ATOM   2410  N  N   . ILE A  1 327 ? 61.443  54.780 18.639 1.00 26.76 ? 327  ILE A N   1 
ATOM   2411  C  CA  . ILE A  1 327 ? 62.398  55.672 19.284 1.00 28.07 ? 327  ILE A CA  1 
ATOM   2412  C  C   . ILE A  1 327 ? 62.786  56.699 18.233 1.00 29.35 ? 327  ILE A C   1 
ATOM   2413  O  O   . ILE A  1 327 ? 63.357  56.346 17.203 1.00 30.69 ? 327  ILE A O   1 
ATOM   2414  C  CB  . ILE A  1 327 ? 63.617  54.881 19.782 1.00 26.83 ? 327  ILE A CB  1 
ATOM   2415  C  CG1 . ILE A  1 327 ? 63.173  53.955 20.924 1.00 26.14 ? 327  ILE A CG1 1 
ATOM   2416  C  CG2 . ILE A  1 327 ? 64.699  55.827 20.251 1.00 25.92 ? 327  ILE A CG2 1 
ATOM   2417  C  CD1 . ILE A  1 327 ? 64.277  53.136 21.530 1.00 24.78 ? 327  ILE A CD1 1 
ATOM   2418  N  N   . CYS A  1 328 ? 62.477  57.965 18.496 1.00 30.00 ? 328  CYS A N   1 
ATOM   2419  C  CA  . CYS A  1 328 ? 62.712  59.029 17.525 1.00 30.80 ? 328  CYS A CA  1 
ATOM   2420  C  C   . CYS A  1 328 ? 63.680  60.136 17.932 1.00 31.01 ? 328  CYS A C   1 
ATOM   2421  O  O   . CYS A  1 328 ? 63.602  60.665 19.029 1.00 31.61 ? 328  CYS A O   1 
ATOM   2422  C  CB  . CYS A  1 328 ? 61.362  59.635 17.156 1.00 33.05 ? 328  CYS A CB  1 
ATOM   2423  S  SG  . CYS A  1 328 ? 60.026  58.391 16.947 1.00 36.53 ? 328  CYS A SG  1 
ATOM   2424  N  N   . ASP A  1 329 ? 64.581  60.480 17.017 1.00 32.51 ? 329  ASP A N   1 
ATOM   2425  C  CA  . ASP A  1 329 ? 65.593  61.512 17.222 1.00 33.67 ? 329  ASP A CA  1 
ATOM   2426  C  C   . ASP A  1 329 ? 65.337  62.768 16.413 1.00 34.12 ? 329  ASP A C   1 
ATOM   2427  O  O   . ASP A  1 329 ? 64.943  62.695 15.246 1.00 34.00 ? 329  ASP A O   1 
ATOM   2428  C  CB  . ASP A  1 329 ? 66.968  60.975 16.824 1.00 34.45 ? 329  ASP A CB  1 
ATOM   2429  C  CG  . ASP A  1 329 ? 67.486  59.952 17.796 1.00 36.05 ? 329  ASP A CG  1 
ATOM   2430  O  OD1 . ASP A  1 329 ? 66.671  59.439 18.598 1.00 36.13 ? 329  ASP A OD1 1 
ATOM   2431  O  OD2 . ASP A  1 329 ? 68.702  59.659 17.759 1.00 36.33 ? 329  ASP A OD2 1 
ATOM   2432  N  N   . TYR A  1 330 ? 65.577  63.922 17.025 1.00 34.85 ? 330  TYR A N   1 
ATOM   2433  C  CA  . TYR A  1 330 ? 65.403  65.192 16.329 1.00 36.27 ? 330  TYR A CA  1 
ATOM   2434  C  C   . TYR A  1 330 ? 66.579  65.427 15.363 1.00 37.53 ? 330  TYR A C   1 
ATOM   2435  O  O   . TYR A  1 330 ? 67.744  65.211 15.719 1.00 36.37 ? 330  TYR A O   1 
ATOM   2436  C  CB  . TYR A  1 330 ? 65.335  66.342 17.327 1.00 36.02 ? 330  TYR A CB  1 
ATOM   2437  C  CG  . TYR A  1 330 ? 65.265  67.690 16.658 1.00 36.67 ? 330  TYR A CG  1 
ATOM   2438  C  CD1 . TYR A  1 330 ? 64.103  68.113 16.015 1.00 37.50 ? 330  TYR A CD1 1 
ATOM   2439  C  CD2 . TYR A  1 330 ? 66.364  68.549 16.671 1.00 37.95 ? 330  TYR A CD2 1 
ATOM   2440  C  CE1 . TYR A  1 330 ? 64.032  69.367 15.405 1.00 37.49 ? 330  TYR A CE1 1 
ATOM   2441  C  CE2 . TYR A  1 330 ? 66.309  69.805 16.064 1.00 37.59 ? 330  TYR A CE2 1 
ATOM   2442  C  CZ  . TYR A  1 330 ? 65.139  70.211 15.437 1.00 38.57 ? 330  TYR A CZ  1 
ATOM   2443  O  OH  . TYR A  1 330 ? 65.070  71.475 14.882 1.00 39.22 ? 330  TYR A OH  1 
ATOM   2444  N  N   . ASP A  1 331 ? 66.252  65.876 14.152 1.00 39.34 ? 331  ASP A N   1 
ATOM   2445  C  CA  . ASP A  1 331 ? 67.228  66.150 13.088 1.00 41.25 ? 331  ASP A CA  1 
ATOM   2446  C  C   . ASP A  1 331 ? 67.365  67.673 12.880 1.00 42.42 ? 331  ASP A C   1 
ATOM   2447  O  O   . ASP A  1 331 ? 66.450  68.313 12.369 1.00 41.09 ? 331  ASP A O   1 
ATOM   2448  C  CB  . ASP A  1 331 ? 66.738  65.471 11.798 1.00 42.21 ? 331  ASP A CB  1 
ATOM   2449  C  CG  . ASP A  1 331 ? 67.719  65.605 10.638 1.00 43.45 ? 331  ASP A CG  1 
ATOM   2450  O  OD1 . ASP A  1 331 ? 68.064  66.744 10.259 1.00 44.14 ? 331  ASP A OD1 1 
ATOM   2451  O  OD2 . ASP A  1 331 ? 68.135  64.562 10.098 1.00 43.73 ? 331  ASP A OD2 1 
ATOM   2452  N  N   . GLU A  1 332 ? 68.495  68.255 13.282 1.00 44.68 ? 332  GLU A N   1 
ATOM   2453  C  CA  . GLU A  1 332 ? 68.689  69.700 13.125 1.00 47.16 ? 332  GLU A CA  1 
ATOM   2454  C  C   . GLU A  1 332 ? 68.729  70.152 11.668 1.00 48.33 ? 332  GLU A C   1 
ATOM   2455  O  O   . GLU A  1 332 ? 68.574  71.334 11.380 1.00 49.50 ? 332  GLU A O   1 
ATOM   2456  C  CB  . GLU A  1 332 ? 69.983  70.169 13.805 1.00 48.13 ? 332  GLU A CB  1 
ATOM   2457  C  CG  . GLU A  1 332 ? 69.994  70.041 15.310 1.00 50.56 ? 332  GLU A CG  1 
ATOM   2458  C  CD  . GLU A  1 332 ? 71.257  70.605 15.940 1.00 51.92 ? 332  GLU A CD  1 
ATOM   2459  O  OE1 . GLU A  1 332 ? 72.363  70.081 15.668 1.00 53.70 ? 332  GLU A OE1 1 
ATOM   2460  O  OE2 . GLU A  1 332 ? 71.151  71.579 16.720 1.00 53.56 ? 332  GLU A OE2 1 
ATOM   2461  N  N   . SER A  1 333 ? 68.939  69.225 10.743 1.00 49.38 ? 333  SER A N   1 
ATOM   2462  C  CA  . SER A  1 333 ? 69.006  69.598 9.329  1.00 49.73 ? 333  SER A CA  1 
ATOM   2463  C  C   . SER A  1 333 ? 67.628  69.849 8.728  1.00 50.09 ? 333  SER A C   1 
ATOM   2464  O  O   . SER A  1 333 ? 67.403  70.886 8.101  1.00 50.23 ? 333  SER A O   1 
ATOM   2465  C  CB  . SER A  1 333 ? 69.725  68.512 8.529  1.00 49.93 ? 333  SER A CB  1 
ATOM   2466  O  OG  . SER A  1 333 ? 71.007  68.256 9.082  1.00 51.07 ? 333  SER A OG  1 
ATOM   2467  N  N   . SER A  1 334 ? 66.710  68.904 8.919  1.00 49.43 ? 334  SER A N   1 
ATOM   2468  C  CA  . SER A  1 334 ? 65.366  69.047 8.377  1.00 49.14 ? 334  SER A CA  1 
ATOM   2469  C  C   . SER A  1 334 ? 64.376  69.555 9.415  1.00 48.31 ? 334  SER A C   1 
ATOM   2470  O  O   . SER A  1 334 ? 63.276  69.994 9.070  1.00 48.88 ? 334  SER A O   1 
ATOM   2471  C  CB  . SER A  1 334 ? 64.862  67.708 7.828  1.00 50.51 ? 334  SER A CB  1 
ATOM   2472  O  OG  . SER A  1 334 ? 64.569  66.799 8.882  1.00 52.28 ? 334  SER A OG  1 
ATOM   2473  N  N   . GLY A  1 335 ? 64.760  69.493 10.685 1.00 47.14 ? 335  GLY A N   1 
ATOM   2474  C  CA  . GLY A  1 335 ? 63.867  69.942 11.743 1.00 45.10 ? 335  GLY A CA  1 
ATOM   2475  C  C   . GLY A  1 335 ? 62.743  68.942 11.927 1.00 43.39 ? 335  GLY A C   1 
ATOM   2476  O  O   . GLY A  1 335 ? 61.678  69.271 12.451 1.00 44.21 ? 335  GLY A O   1 
ATOM   2477  N  N   . ARG A  1 336 ? 62.990  67.717 11.480 1.00 41.49 ? 336  ARG A N   1 
ATOM   2478  C  CA  . ARG A  1 336 ? 62.018  66.645 11.583 1.00 40.07 ? 336  ARG A CA  1 
ATOM   2479  C  C   . ARG A  1 336 ? 62.474  65.605 12.608 1.00 37.91 ? 336  ARG A C   1 
ATOM   2480  O  O   . ARG A  1 336 ? 63.610  65.628 13.083 1.00 36.92 ? 336  ARG A O   1 
ATOM   2481  C  CB  . ARG A  1 336 ? 61.820  65.967 10.221 1.00 41.84 ? 336  ARG A CB  1 
ATOM   2482  C  CG  . ARG A  1 336 ? 61.549  66.926 9.052  1.00 44.65 ? 336  ARG A CG  1 
ATOM   2483  C  CD  . ARG A  1 336 ? 60.291  67.766 9.251  1.00 48.03 ? 336  ARG A CD  1 
ATOM   2484  N  NE  . ARG A  1 336 ? 59.072  66.945 9.289  1.00 51.08 ? 336  ARG A NE  1 
ATOM   2485  C  CZ  . ARG A  1 336 ? 58.546  66.322 8.235  1.00 52.16 ? 336  ARG A CZ  1 
ATOM   2486  N  NH1 . ARG A  1 336 ? 59.119  66.423 7.038  1.00 53.30 ? 336  ARG A NH1 1 
ATOM   2487  N  NH2 . ARG A  1 336 ? 57.456  65.580 8.384  1.00 51.85 ? 336  ARG A NH2 1 
ATOM   2488  N  N   . TRP A  1 337 ? 61.569  64.701 12.954 1.00 35.44 ? 337  TRP A N   1 
ATOM   2489  C  CA  . TRP A  1 337 ? 61.860  63.640 13.904 1.00 32.92 ? 337  TRP A CA  1 
ATOM   2490  C  C   . TRP A  1 337 ? 61.847  62.317 13.138 1.00 33.76 ? 337  TRP A C   1 
ATOM   2491  O  O   . TRP A  1 337 ? 60.843  61.956 12.529 1.00 33.05 ? 337  TRP A O   1 
ATOM   2492  C  CB  . TRP A  1 337 ? 60.807  63.621 15.020 1.00 30.17 ? 337  TRP A CB  1 
ATOM   2493  C  CG  . TRP A  1 337 ? 60.860  64.819 15.917 1.00 25.87 ? 337  TRP A CG  1 
ATOM   2494  C  CD1 . TRP A  1 337 ? 60.308  66.050 15.683 1.00 25.99 ? 337  TRP A CD1 1 
ATOM   2495  C  CD2 . TRP A  1 337 ? 61.578  64.931 17.153 1.00 26.09 ? 337  TRP A CD2 1 
ATOM   2496  N  NE1 . TRP A  1 337 ? 60.648  66.925 16.694 1.00 25.82 ? 337  TRP A NE1 1 
ATOM   2497  C  CE2 . TRP A  1 337 ? 61.426  66.262 17.609 1.00 25.15 ? 337  TRP A CE2 1 
ATOM   2498  C  CE3 . TRP A  1 337 ? 62.344  64.034 17.919 1.00 25.59 ? 337  TRP A CE3 1 
ATOM   2499  C  CZ2 . TRP A  1 337 ? 62.010  66.718 18.796 1.00 25.61 ? 337  TRP A CZ2 1 
ATOM   2500  C  CZ3 . TRP A  1 337 ? 62.931  64.491 19.100 1.00 24.34 ? 337  TRP A CZ3 1 
ATOM   2501  C  CH2 . TRP A  1 337 ? 62.760  65.821 19.524 1.00 25.23 ? 337  TRP A CH2 1 
ATOM   2502  N  N   . ASN A  1 338 ? 62.972  61.606 13.158 1.00 34.23 ? 338  ASN A N   1 
ATOM   2503  C  CA  . ASN A  1 338 ? 63.092  60.330 12.461 1.00 34.93 ? 338  ASN A CA  1 
ATOM   2504  C  C   . ASN A  1 338 ? 63.104  59.188 13.460 1.00 34.42 ? 338  ASN A C   1 
ATOM   2505  O  O   . ASN A  1 338 ? 63.765  59.268 14.499 1.00 34.11 ? 338  ASN A O   1 
ATOM   2506  C  CB  . ASN A  1 338 ? 64.381  60.305 11.640 1.00 37.32 ? 338  ASN A CB  1 
ATOM   2507  C  CG  . ASN A  1 338 ? 64.374  61.332 10.520 1.00 40.34 ? 338  ASN A CG  1 
ATOM   2508  O  OD1 . ASN A  1 338 ? 65.417  61.894 10.173 1.00 42.89 ? 338  ASN A OD1 1 
ATOM   2509  N  ND2 . ASN A  1 338 ? 63.196  61.571 9.931  1.00 41.38 ? 338  ASN A ND2 1 
ATOM   2510  N  N   . CYS A  1 339 ? 62.376  58.125 13.146 1.00 34.05 ? 339  CYS A N   1 
ATOM   2511  C  CA  . CYS A  1 339 ? 62.318  56.978 14.038 1.00 35.13 ? 339  CYS A CA  1 
ATOM   2512  C  C   . CYS A  1 339 ? 62.876  55.762 13.312 1.00 35.45 ? 339  CYS A C   1 
ATOM   2513  O  O   . CYS A  1 339 ? 62.136  55.040 12.640 1.00 35.54 ? 339  CYS A O   1 
ATOM   2514  C  CB  . CYS A  1 339 ? 60.868  56.696 14.463 1.00 35.74 ? 339  CYS A CB  1 
ATOM   2515  S  SG  . CYS A  1 339 ? 59.830  58.150 14.919 1.00 36.50 ? 339  CYS A SG  1 
ATOM   2516  N  N   . LEU A  1 340 ? 64.179  55.537 13.446 1.00 34.75 ? 340  LEU A N   1 
ATOM   2517  C  CA  . LEU A  1 340 ? 64.826  54.400 12.792 1.00 35.25 ? 340  LEU A CA  1 
ATOM   2518  C  C   . LEU A  1 340 ? 64.151  53.074 13.076 1.00 35.18 ? 340  LEU A C   1 
ATOM   2519  O  O   . LEU A  1 340 ? 63.942  52.695 14.233 1.00 33.75 ? 340  LEU A O   1 
ATOM   2520  C  CB  . LEU A  1 340 ? 66.296  54.288 13.216 1.00 35.62 ? 340  LEU A CB  1 
ATOM   2521  C  CG  . LEU A  1 340 ? 67.251  55.395 12.749 1.00 37.66 ? 340  LEU A CG  1 
ATOM   2522  C  CD1 . LEU A  1 340 ? 68.641  55.185 13.367 1.00 36.24 ? 340  LEU A CD1 1 
ATOM   2523  C  CD2 . LEU A  1 340 ? 67.319  55.380 11.218 1.00 36.75 ? 340  LEU A CD2 1 
ATOM   2524  N  N   . VAL A  1 341 ? 63.828  52.360 12.005 1.00 35.33 ? 341  VAL A N   1 
ATOM   2525  C  CA  . VAL A  1 341 ? 63.204  51.052 12.111 1.00 35.49 ? 341  VAL A CA  1 
ATOM   2526  C  C   . VAL A  1 341 ? 64.049  50.112 12.970 1.00 35.50 ? 341  VAL A C   1 
ATOM   2527  O  O   . VAL A  1 341 ? 63.516  49.292 13.714 1.00 36.56 ? 341  VAL A O   1 
ATOM   2528  C  CB  . VAL A  1 341 ? 63.032  50.421 10.727 1.00 36.48 ? 341  VAL A CB  1 
ATOM   2529  C  CG1 . VAL A  1 341 ? 64.401  50.159 10.111 1.00 37.27 ? 341  VAL A CG1 1 
ATOM   2530  C  CG2 . VAL A  1 341 ? 62.245  49.127 10.838 1.00 37.14 ? 341  VAL A CG2 1 
ATOM   2531  N  N   . ALA A  1 342 ? 65.366  50.228 12.864 1.00 35.09 ? 342  ALA A N   1 
ATOM   2532  C  CA  . ALA A  1 342 ? 66.269  49.384 13.639 1.00 35.54 ? 342  ALA A CA  1 
ATOM   2533  C  C   . ALA A  1 342 ? 66.126  49.626 15.145 1.00 36.01 ? 342  ALA A C   1 
ATOM   2534  O  O   . ALA A  1 342 ? 66.573  48.810 15.958 1.00 36.37 ? 342  ALA A O   1 
ATOM   2535  C  CB  . ALA A  1 342 ? 67.715  49.631 13.217 1.00 34.28 ? 342  ALA A CB  1 
ATOM   2536  N  N   . ARG A  1 343 ? 65.519  50.749 15.516 1.00 35.24 ? 343  ARG A N   1 
ATOM   2537  C  CA  . ARG A  1 343 ? 65.331  51.059 16.923 1.00 34.26 ? 343  ARG A CA  1 
ATOM   2538  C  C   . ARG A  1 343 ? 63.915  50.717 17.408 1.00 34.44 ? 343  ARG A C   1 
ATOM   2539  O  O   . ARG A  1 343 ? 63.507  51.117 18.501 1.00 35.13 ? 343  ARG A O   1 
ATOM   2540  C  CB  . ARG A  1 343 ? 65.647  52.530 17.181 1.00 33.09 ? 343  ARG A CB  1 
ATOM   2541  C  CG  . ARG A  1 343 ? 67.116  52.852 16.988 1.00 33.61 ? 343  ARG A CG  1 
ATOM   2542  C  CD  . ARG A  1 343 ? 67.402  54.324 17.192 1.00 32.77 ? 343  ARG A CD  1 
ATOM   2543  N  NE  . ARG A  1 343 ? 68.835  54.573 17.304 1.00 31.98 ? 343  ARG A NE  1 
ATOM   2544  C  CZ  . ARG A  1 343 ? 69.377  55.782 17.346 1.00 31.96 ? 343  ARG A CZ  1 
ATOM   2545  N  NH1 . ARG A  1 343 ? 68.605  56.866 17.271 1.00 32.11 ? 343  ARG A NH1 1 
ATOM   2546  N  NH2 . ARG A  1 343 ? 70.687  55.906 17.502 1.00 33.11 ? 343  ARG A NH2 1 
ATOM   2547  N  N   . GLN A  1 344 ? 63.171  49.969 16.600 1.00 32.82 ? 344  GLN A N   1 
ATOM   2548  C  CA  . GLN A  1 344 ? 61.823  49.572 16.981 1.00 32.81 ? 344  GLN A CA  1 
ATOM   2549  C  C   . GLN A  1 344 ? 61.860  48.398 17.939 1.00 32.23 ? 344  GLN A C   1 
ATOM   2550  O  O   . GLN A  1 344 ? 62.743  47.542 17.860 1.00 32.86 ? 344  GLN A O   1 
ATOM   2551  C  CB  . GLN A  1 344 ? 60.996  49.186 15.751 1.00 33.39 ? 344  GLN A CB  1 
ATOM   2552  C  CG  . GLN A  1 344 ? 60.027  50.262 15.285 1.00 35.37 ? 344  GLN A CG  1 
ATOM   2553  C  CD  . GLN A  1 344 ? 59.208  49.836 14.064 1.00 36.46 ? 344  GLN A CD  1 
ATOM   2554  O  OE1 . GLN A  1 344 ? 58.798  48.679 13.941 1.00 36.52 ? 344  GLN A OE1 1 
ATOM   2555  N  NE2 . GLN A  1 344 ? 58.952  50.780 13.171 1.00 36.10 ? 344  GLN A NE2 1 
ATOM   2556  N  N   . HIS A  1 345 ? 60.892  48.356 18.845 1.00 31.19 ? 345  HIS A N   1 
ATOM   2557  C  CA  . HIS A  1 345 ? 60.814  47.275 19.810 1.00 31.05 ? 345  HIS A CA  1 
ATOM   2558  C  C   . HIS A  1 345 ? 59.392  46.766 19.895 1.00 31.71 ? 345  HIS A C   1 
ATOM   2559  O  O   . HIS A  1 345 ? 58.466  47.502 20.241 1.00 32.59 ? 345  HIS A O   1 
ATOM   2560  C  CB  . HIS A  1 345 ? 61.302  47.759 21.173 1.00 29.70 ? 345  HIS A CB  1 
ATOM   2561  C  CG  . HIS A  1 345 ? 62.763  48.079 21.189 1.00 28.34 ? 345  HIS A CG  1 
ATOM   2562  N  ND1 . HIS A  1 345 ? 63.734  47.104 21.288 1.00 26.33 ? 345  HIS A ND1 1 
ATOM   2563  C  CD2 . HIS A  1 345 ? 63.421  49.244 20.995 1.00 27.61 ? 345  HIS A CD2 1 
ATOM   2564  C  CE1 . HIS A  1 345 ? 64.924  47.655 21.152 1.00 27.03 ? 345  HIS A CE1 1 
ATOM   2565  N  NE2 . HIS A  1 345 ? 64.765  48.953 20.970 1.00 28.24 ? 345  HIS A NE2 1 
ATOM   2566  N  N   . ILE A  1 346 ? 59.234  45.492 19.570 1.00 31.54 ? 346  ILE A N   1 
ATOM   2567  C  CA  . ILE A  1 346 ? 57.938  44.848 19.587 1.00 31.82 ? 346  ILE A CA  1 
ATOM   2568  C  C   . ILE A  1 346 ? 57.756  44.144 20.903 1.00 32.14 ? 346  ILE A C   1 
ATOM   2569  O  O   . ILE A  1 346 ? 58.709  43.592 21.463 1.00 31.94 ? 346  ILE A O   1 
ATOM   2570  C  CB  . ILE A  1 346 ? 57.828  43.803 18.461 1.00 32.19 ? 346  ILE A CB  1 
ATOM   2571  C  CG1 . ILE A  1 346 ? 57.882  44.503 17.094 1.00 32.83 ? 346  ILE A CG1 1 
ATOM   2572  C  CG2 . ILE A  1 346 ? 56.548  43.006 18.612 1.00 32.24 ? 346  ILE A CG2 1 
ATOM   2573  C  CD1 . ILE A  1 346 ? 57.934  43.537 15.922 1.00 34.44 ? 346  ILE A CD1 1 
ATOM   2574  N  N   . GLU A  1 347 ? 56.525  44.167 21.395 1.00 31.69 ? 347  GLU A N   1 
ATOM   2575  C  CA  . GLU A  1 347 ? 56.186  43.505 22.647 1.00 32.49 ? 347  GLU A CA  1 
ATOM   2576  C  C   . GLU A  1 347 ? 54.831  42.857 22.410 1.00 32.39 ? 347  GLU A C   1 
ATOM   2577  O  O   . GLU A  1 347 ? 53.859  43.538 22.124 1.00 32.24 ? 347  GLU A O   1 
ATOM   2578  C  CB  . GLU A  1 347 ? 56.108  44.531 23.786 1.00 31.79 ? 347  GLU A CB  1 
ATOM   2579  C  CG  . GLU A  1 347 ? 56.031  43.917 25.169 1.00 32.26 ? 347  GLU A CG  1 
ATOM   2580  C  CD  . GLU A  1 347 ? 56.085  44.955 26.280 1.00 33.41 ? 347  GLU A CD  1 
ATOM   2581  O  OE1 . GLU A  1 347 ? 56.648  46.054 26.051 1.00 33.61 ? 347  GLU A OE1 1 
ATOM   2582  O  OE2 . GLU A  1 347 ? 55.583  44.668 27.393 1.00 32.11 ? 347  GLU A OE2 1 
ATOM   2583  N  N   . MET A  1 348 ? 54.772  41.535 22.491 1.00 33.84 ? 348  MET A N   1 
ATOM   2584  C  CA  . MET A  1 348 ? 53.513  40.834 22.261 1.00 34.15 ? 348  MET A CA  1 
ATOM   2585  C  C   . MET A  1 348 ? 53.254  39.802 23.344 1.00 33.05 ? 348  MET A C   1 
ATOM   2586  O  O   . MET A  1 348 ? 54.119  39.530 24.164 1.00 32.40 ? 348  MET A O   1 
ATOM   2587  C  CB  . MET A  1 348 ? 53.506  40.174 20.875 1.00 35.36 ? 348  MET A CB  1 
ATOM   2588  C  CG  . MET A  1 348 ? 54.595  39.142 20.654 1.00 39.55 ? 348  MET A CG  1 
ATOM   2589  S  SD  . MET A  1 348 ? 54.437  38.360 19.021 1.00 47.54 ? 348  MET A SD  1 
ATOM   2590  C  CE  . MET A  1 348 ? 55.735  39.202 18.077 1.00 44.95 ? 348  MET A CE  1 
ATOM   2591  N  N   . SER A  1 349 ? 52.046  39.248 23.363 1.00 33.42 ? 349  SER A N   1 
ATOM   2592  C  CA  . SER A  1 349 ? 51.703  38.248 24.364 1.00 32.96 ? 349  SER A CA  1 
ATOM   2593  C  C   . SER A  1 349 ? 50.908  37.150 23.696 1.00 32.76 ? 349  SER A C   1 
ATOM   2594  O  O   . SER A  1 349 ? 50.032  37.419 22.880 1.00 33.69 ? 349  SER A O   1 
ATOM   2595  C  CB  . SER A  1 349 ? 50.870  38.874 25.491 1.00 33.28 ? 349  SER A CB  1 
ATOM   2596  O  OG  . SER A  1 349 ? 50.518  37.910 26.471 1.00 32.99 ? 349  SER A OG  1 
ATOM   2597  N  N   . THR A  1 350 ? 51.217  35.910 24.048 1.00 32.21 ? 350  THR A N   1 
ATOM   2598  C  CA  . THR A  1 350 ? 50.512  34.770 23.481 1.00 32.61 ? 350  THR A CA  1 
ATOM   2599  C  C   . THR A  1 350 ? 49.450  34.210 24.436 1.00 31.31 ? 350  THR A C   1 
ATOM   2600  O  O   . THR A  1 350 ? 48.589  33.446 24.020 1.00 32.65 ? 350  THR A O   1 
ATOM   2601  C  CB  . THR A  1 350 ? 51.504  33.643 23.119 1.00 33.55 ? 350  THR A CB  1 
ATOM   2602  O  OG1 . THR A  1 350 ? 52.351  33.391 24.244 1.00 34.40 ? 350  THR A OG1 1 
ATOM   2603  C  CG2 . THR A  1 350 ? 52.370  34.043 21.923 1.00 33.77 ? 350  THR A CG2 1 
ATOM   2604  N  N   . THR A  1 351 ? 49.513  34.591 25.710 1.00 29.52 ? 351  THR A N   1 
ATOM   2605  C  CA  . THR A  1 351 ? 48.555  34.105 26.707 1.00 28.35 ? 351  THR A CA  1 
ATOM   2606  C  C   . THR A  1 351 ? 47.467  35.112 27.078 1.00 27.47 ? 351  THR A C   1 
ATOM   2607  O  O   . THR A  1 351 ? 46.409  34.735 27.591 1.00 28.39 ? 351  THR A O   1 
ATOM   2608  C  CB  . THR A  1 351 ? 49.283  33.698 27.996 1.00 28.21 ? 351  THR A CB  1 
ATOM   2609  O  OG1 . THR A  1 351 ? 50.056  34.812 28.467 1.00 29.24 ? 351  THR A OG1 1 
ATOM   2610  C  CG2 . THR A  1 351 ? 50.222  32.508 27.723 1.00 26.94 ? 351  THR A CG2 1 
ATOM   2611  N  N   . GLY A  1 352 ? 47.720  36.391 26.829 1.00 26.22 ? 352  GLY A N   1 
ATOM   2612  C  CA  . GLY A  1 352 ? 46.738  37.404 27.167 1.00 25.31 ? 352  GLY A CA  1 
ATOM   2613  C  C   . GLY A  1 352 ? 46.999  38.711 26.446 1.00 24.82 ? 352  GLY A C   1 
ATOM   2614  O  O   . GLY A  1 352 ? 47.302  38.722 25.254 1.00 25.05 ? 352  GLY A O   1 
ATOM   2615  N  N   . TRP A  1 353 ? 46.893  39.812 27.184 1.00 22.62 ? 353  TRP A N   1 
ATOM   2616  C  CA  . TRP A  1 353 ? 47.109  41.140 26.630 1.00 20.71 ? 353  TRP A CA  1 
ATOM   2617  C  C   . TRP A  1 353 ? 48.546  41.560 26.981 1.00 20.56 ? 353  TRP A C   1 
ATOM   2618  O  O   . TRP A  1 353 ? 49.285  40.778 27.575 1.00 20.32 ? 353  TRP A O   1 
ATOM   2619  C  CB  . TRP A  1 353 ? 46.062  42.101 27.226 1.00 18.60 ? 353  TRP A CB  1 
ATOM   2620  C  CG  . TRP A  1 353 ? 46.041  42.098 28.746 1.00 17.27 ? 353  TRP A CG  1 
ATOM   2621  C  CD1 . TRP A  1 353 ? 46.652  42.983 29.560 1.00 17.46 ? 353  TRP A CD1 1 
ATOM   2622  C  CD2 . TRP A  1 353 ? 45.388  41.139 29.611 1.00 17.43 ? 353  TRP A CD2 1 
ATOM   2623  N  NE1 . TRP A  1 353 ? 46.426  42.654 30.886 1.00 18.09 ? 353  TRP A NE1 1 
ATOM   2624  C  CE2 . TRP A  1 353 ? 45.653  41.526 30.941 1.00 17.46 ? 353  TRP A CE2 1 
ATOM   2625  C  CE3 . TRP A  1 353 ? 44.606  39.995 29.386 1.00 16.92 ? 353  TRP A CE3 1 
ATOM   2626  C  CZ2 . TRP A  1 353 ? 45.169  40.814 32.048 1.00 16.74 ? 353  TRP A CZ2 1 
ATOM   2627  C  CZ3 . TRP A  1 353 ? 44.120  39.284 30.488 1.00 15.35 ? 353  TRP A CZ3 1 
ATOM   2628  C  CH2 . TRP A  1 353 ? 44.406  39.702 31.804 1.00 16.40 ? 353  TRP A CH2 1 
ATOM   2629  N  N   . VAL A  1 354 ? 48.942  42.779 26.625 1.00 19.99 ? 354  VAL A N   1 
ATOM   2630  C  CA  . VAL A  1 354 ? 50.291  43.249 26.911 1.00 20.22 ? 354  VAL A CA  1 
ATOM   2631  C  C   . VAL A  1 354 ? 50.319  44.185 28.119 1.00 20.66 ? 354  VAL A C   1 
ATOM   2632  O  O   . VAL A  1 354 ? 49.583  45.167 28.158 1.00 20.63 ? 354  VAL A O   1 
ATOM   2633  C  CB  . VAL A  1 354 ? 50.886  44.003 25.694 1.00 21.71 ? 354  VAL A CB  1 
ATOM   2634  C  CG1 . VAL A  1 354 ? 52.309  44.481 26.015 1.00 22.01 ? 354  VAL A CG1 1 
ATOM   2635  C  CG2 . VAL A  1 354 ? 50.886  43.100 24.469 1.00 21.65 ? 354  VAL A CG2 1 
ATOM   2636  N  N   . GLY A  1 355 ? 51.183  43.885 29.090 1.00 19.51 ? 355  GLY A N   1 
ATOM   2637  C  CA  . GLY A  1 355 ? 51.287  44.713 30.286 1.00 20.57 ? 355  GLY A CA  1 
ATOM   2638  C  C   . GLY A  1 355 ? 50.206  44.416 31.325 1.00 19.76 ? 355  GLY A C   1 
ATOM   2639  O  O   . GLY A  1 355 ? 49.364  43.554 31.094 1.00 19.68 ? 355  GLY A O   1 
ATOM   2640  N  N   . ARG A  1 356 ? 50.223  45.103 32.467 1.00 18.40 ? 356  ARG A N   1 
ATOM   2641  C  CA  . ARG A  1 356 ? 49.200  44.852 33.484 1.00 19.70 ? 356  ARG A CA  1 
ATOM   2642  C  C   . ARG A  1 356 ? 47.877  45.470 33.029 1.00 19.72 ? 356  ARG A C   1 
ATOM   2643  O  O   . ARG A  1 356 ? 46.851  44.789 32.977 1.00 18.77 ? 356  ARG A O   1 
ATOM   2644  C  CB  . ARG A  1 356 ? 49.641  45.382 34.855 1.00 19.24 ? 356  ARG A CB  1 
ATOM   2645  C  CG  . ARG A  1 356 ? 50.755  44.509 35.479 1.00 19.18 ? 356  ARG A CG  1 
ATOM   2646  C  CD  . ARG A  1 356 ? 51.044  44.884 36.913 1.00 17.29 ? 356  ARG A CD  1 
ATOM   2647  N  NE  . ARG A  1 356 ? 51.956  43.934 37.547 1.00 19.09 ? 356  ARG A NE  1 
ATOM   2648  C  CZ  . ARG A  1 356 ? 53.250  44.157 37.784 1.00 18.28 ? 356  ARG A CZ  1 
ATOM   2649  N  NH1 . ARG A  1 356 ? 53.813  45.308 37.438 1.00 17.52 ? 356  ARG A NH1 1 
ATOM   2650  N  NH2 . ARG A  1 356 ? 53.971  43.236 38.398 1.00 16.80 ? 356  ARG A NH2 1 
ATOM   2651  N  N   . PHE A  1 357 ? 47.917  46.747 32.679 1.00 19.15 ? 357  PHE A N   1 
ATOM   2652  C  CA  . PHE A  1 357 ? 46.750  47.447 32.166 1.00 20.19 ? 357  PHE A CA  1 
ATOM   2653  C  C   . PHE A  1 357 ? 47.145  48.083 30.829 1.00 20.41 ? 357  PHE A C   1 
ATOM   2654  O  O   . PHE A  1 357 ? 46.277  48.478 30.051 1.00 21.81 ? 357  PHE A O   1 
ATOM   2655  C  CB  . PHE A  1 357 ? 46.270  48.504 33.154 1.00 18.81 ? 357  PHE A CB  1 
ATOM   2656  C  CG  . PHE A  1 357 ? 45.623  47.936 34.366 1.00 18.25 ? 357  PHE A CG  1 
ATOM   2657  C  CD1 . PHE A  1 357 ? 44.288  47.556 34.335 1.00 18.48 ? 357  PHE A CD1 1 
ATOM   2658  C  CD2 . PHE A  1 357 ? 46.347  47.758 35.535 1.00 17.62 ? 357  PHE A CD2 1 
ATOM   2659  C  CE1 . PHE A  1 357 ? 43.670  47.011 35.449 1.00 18.44 ? 357  PHE A CE1 1 
ATOM   2660  C  CE2 . PHE A  1 357 ? 45.728  47.207 36.671 1.00 19.95 ? 357  PHE A CE2 1 
ATOM   2661  C  CZ  . PHE A  1 357 ? 44.385  46.830 36.618 1.00 18.97 ? 357  PHE A CZ  1 
ATOM   2662  N  N   . ARG A  1 358 ? 48.454  48.183 30.582 1.00 19.69 ? 358  ARG A N   1 
ATOM   2663  C  CA  . ARG A  1 358 ? 49.008  48.696 29.318 1.00 20.89 ? 358  ARG A CA  1 
ATOM   2664  C  C   . ARG A  1 358 ? 50.510  48.470 29.330 1.00 21.32 ? 358  ARG A C   1 
ATOM   2665  O  O   . ARG A  1 358 ? 51.106  48.274 30.393 1.00 22.99 ? 358  ARG A O   1 
ATOM   2666  C  CB  . ARG A  1 358 ? 48.742  50.199 29.120 1.00 20.38 ? 358  ARG A CB  1 
ATOM   2667  C  CG  . ARG A  1 358 ? 49.451  51.088 30.127 1.00 22.05 ? 358  ARG A CG  1 
ATOM   2668  C  CD  . ARG A  1 358 ? 49.324  52.573 29.802 1.00 21.83 ? 358  ARG A CD  1 
ATOM   2669  N  NE  . ARG A  1 358 ? 49.746  53.369 30.951 1.00 21.88 ? 358  ARG A NE  1 
ATOM   2670  C  CZ  . ARG A  1 358 ? 50.169  54.626 30.894 1.00 22.33 ? 358  ARG A CZ  1 
ATOM   2671  N  NH1 . ARG A  1 358 ? 50.241  55.263 29.726 1.00 22.83 ? 358  ARG A NH1 1 
ATOM   2672  N  NH2 . ARG A  1 358 ? 50.520  55.247 32.010 1.00 18.82 ? 358  ARG A NH2 1 
ATOM   2673  N  N   . PRO A  1 359 ? 51.144  48.478 28.146 1.00 20.48 ? 359  PRO A N   1 
ATOM   2674  C  CA  . PRO A  1 359 ? 52.595  48.276 28.079 1.00 20.24 ? 359  PRO A CA  1 
ATOM   2675  C  C   . PRO A  1 359 ? 53.274  49.201 29.099 1.00 20.37 ? 359  PRO A C   1 
ATOM   2676  O  O   . PRO A  1 359 ? 52.872  50.359 29.261 1.00 19.60 ? 359  PRO A O   1 
ATOM   2677  C  CB  . PRO A  1 359 ? 52.923  48.655 26.633 1.00 19.74 ? 359  PRO A CB  1 
ATOM   2678  C  CG  . PRO A  1 359 ? 51.705  48.220 25.896 1.00 19.71 ? 359  PRO A CG  1 
ATOM   2679  C  CD  . PRO A  1 359 ? 50.580  48.699 26.804 1.00 20.41 ? 359  PRO A CD  1 
ATOM   2680  N  N   . SER A  1 360 ? 54.281  48.682 29.799 1.00 20.88 ? 360  SER A N   1 
ATOM   2681  C  CA  . SER A  1 360 ? 55.003  49.457 30.813 1.00 21.01 ? 360  SER A CA  1 
ATOM   2682  C  C   . SER A  1 360 ? 55.853  50.572 30.177 1.00 21.43 ? 360  SER A C   1 
ATOM   2683  O  O   . SER A  1 360 ? 56.203  50.508 28.998 1.00 19.78 ? 360  SER A O   1 
ATOM   2684  C  CB  . SER A  1 360 ? 55.918  48.540 31.621 1.00 21.42 ? 360  SER A CB  1 
ATOM   2685  O  OG  . SER A  1 360 ? 56.861  47.908 30.772 1.00 21.67 ? 360  SER A OG  1 
ATOM   2686  N  N   . GLU A  1 361 ? 56.192  51.575 30.978 1.00 21.03 ? 361  GLU A N   1 
ATOM   2687  C  CA  . GLU A  1 361 ? 56.982  52.685 30.503 1.00 22.71 ? 361  GLU A CA  1 
ATOM   2688  C  C   . GLU A  1 361 ? 58.462  52.324 30.615 1.00 22.84 ? 361  GLU A C   1 
ATOM   2689  O  O   . GLU A  1 361 ? 58.884  51.609 31.538 1.00 21.00 ? 361  GLU A O   1 
ATOM   2690  C  CB  . GLU A  1 361 ? 56.705  53.956 31.314 1.00 24.07 ? 361  GLU A CB  1 
ATOM   2691  C  CG  . GLU A  1 361 ? 57.400  54.002 32.662 1.00 28.75 ? 361  GLU A CG  1 
ATOM   2692  C  CD  . GLU A  1 361 ? 56.606  53.328 33.763 1.00 32.49 ? 361  GLU A CD  1 
ATOM   2693  O  OE1 . GLU A  1 361 ? 55.868  52.343 33.504 1.00 34.60 ? 361  GLU A OE1 1 
ATOM   2694  O  OE2 . GLU A  1 361 ? 56.728  53.791 34.913 1.00 37.02 ? 361  GLU A OE2 1 
ATOM   2695  N  N   . PRO A  1 362 ? 59.270  52.812 29.660 1.00 21.85 ? 362  PRO A N   1 
ATOM   2696  C  CA  . PRO A  1 362 ? 60.722  52.551 29.635 1.00 21.20 ? 362  PRO A CA  1 
ATOM   2697  C  C   . PRO A  1 362 ? 61.440  53.559 30.527 1.00 20.73 ? 362  PRO A C   1 
ATOM   2698  O  O   . PRO A  1 362 ? 60.963  54.665 30.708 1.00 19.53 ? 362  PRO A O   1 
ATOM   2699  C  CB  . PRO A  1 362 ? 61.078  52.733 28.163 1.00 20.46 ? 362  PRO A CB  1 
ATOM   2700  C  CG  . PRO A  1 362 ? 60.156  53.879 27.753 1.00 21.48 ? 362  PRO A CG  1 
ATOM   2701  C  CD  . PRO A  1 362 ? 58.827  53.567 28.470 1.00 20.74 ? 362  PRO A CD  1 
ATOM   2702  N  N   . HIS A  1 363 ? 62.566  53.161 31.101 1.00 20.19 ? 363  HIS A N   1 
ATOM   2703  C  CA  . HIS A  1 363 ? 63.352  54.052 31.940 1.00 21.18 ? 363  HIS A CA  1 
ATOM   2704  C  C   . HIS A  1 363 ? 64.714  54.170 31.253 1.00 20.65 ? 363  HIS A C   1 
ATOM   2705  O  O   . HIS A  1 363 ? 65.520  53.248 31.288 1.00 19.78 ? 363  HIS A O   1 
ATOM   2706  C  CB  . HIS A  1 363 ? 63.475  53.471 33.353 1.00 20.85 ? 363  HIS A CB  1 
ATOM   2707  C  CG  . HIS A  1 363 ? 62.188  53.486 34.107 1.00 21.53 ? 363  HIS A CG  1 
ATOM   2708  N  ND1 . HIS A  1 363 ? 61.910  54.416 35.087 1.00 21.93 ? 363  HIS A ND1 1 
ATOM   2709  C  CD2 . HIS A  1 363 ? 61.054  52.759 33.945 1.00 19.70 ? 363  HIS A CD2 1 
ATOM   2710  C  CE1 . HIS A  1 363 ? 60.660  54.270 35.490 1.00 19.66 ? 363  HIS A CE1 1 
ATOM   2711  N  NE2 . HIS A  1 363 ? 60.120  53.271 34.810 1.00 22.56 ? 363  HIS A NE2 1 
ATOM   2712  N  N   . PHE A  1 364 ? 64.935  55.299 30.592 1.00 20.28 ? 364  PHE A N   1 
ATOM   2713  C  CA  . PHE A  1 364 ? 66.176  55.518 29.867 1.00 20.31 ? 364  PHE A CA  1 
ATOM   2714  C  C   . PHE A  1 364 ? 67.333  55.954 30.745 1.00 21.11 ? 364  PHE A C   1 
ATOM   2715  O  O   . PHE A  1 364 ? 67.129  56.609 31.778 1.00 21.01 ? 364  PHE A O   1 
ATOM   2716  C  CB  . PHE A  1 364 ? 65.981  56.579 28.763 1.00 19.63 ? 364  PHE A CB  1 
ATOM   2717  C  CG  . PHE A  1 364 ? 65.161  56.103 27.597 1.00 20.17 ? 364  PHE A CG  1 
ATOM   2718  C  CD1 . PHE A  1 364 ? 63.778  56.268 27.581 1.00 20.54 ? 364  PHE A CD1 1 
ATOM   2719  C  CD2 . PHE A  1 364 ? 65.773  55.449 26.523 1.00 19.61 ? 364  PHE A CD2 1 
ATOM   2720  C  CE1 . PHE A  1 364 ? 63.025  55.794 26.515 1.00 19.80 ? 364  PHE A CE1 1 
ATOM   2721  C  CE2 . PHE A  1 364 ? 65.021  54.975 25.460 1.00 20.40 ? 364  PHE A CE2 1 
ATOM   2722  C  CZ  . PHE A  1 364 ? 63.641  55.144 25.453 1.00 20.89 ? 364  PHE A CZ  1 
ATOM   2723  N  N   . THR A  1 365 ? 68.543  55.593 30.314 1.00 21.10 ? 365  THR A N   1 
ATOM   2724  C  CA  . THR A  1 365 ? 69.784  55.975 30.989 1.00 21.68 ? 365  THR A CA  1 
ATOM   2725  C  C   . THR A  1 365 ? 70.085  57.432 30.601 1.00 24.04 ? 365  THR A C   1 
ATOM   2726  O  O   . THR A  1 365 ? 69.436  57.989 29.704 1.00 24.56 ? 365  THR A O   1 
ATOM   2727  C  CB  . THR A  1 365 ? 70.971  55.103 30.522 1.00 20.72 ? 365  THR A CB  1 
ATOM   2728  O  OG1 . THR A  1 365 ? 71.089  55.182 29.093 1.00 18.63 ? 365  THR A OG1 1 
ATOM   2729  C  CG2 . THR A  1 365 ? 70.769  53.654 30.928 1.00 17.75 ? 365  THR A CG2 1 
ATOM   2730  N  N   . LEU A  1 366 ? 71.066  58.043 31.263 1.00 25.15 ? 366  LEU A N   1 
ATOM   2731  C  CA  . LEU A  1 366 ? 71.424  59.437 30.978 1.00 27.59 ? 366  LEU A CA  1 
ATOM   2732  C  C   . LEU A  1 366 ? 71.629  59.733 29.480 1.00 26.68 ? 366  LEU A C   1 
ATOM   2733  O  O   . LEU A  1 366 ? 71.069  60.687 28.952 1.00 27.61 ? 366  LEU A O   1 
ATOM   2734  C  CB  . LEU A  1 366 ? 72.691  59.825 31.751 1.00 29.97 ? 366  LEU A CB  1 
ATOM   2735  C  CG  . LEU A  1 366 ? 73.131  61.276 31.541 1.00 33.73 ? 366  LEU A CG  1 
ATOM   2736  C  CD1 . LEU A  1 366 ? 72.032  62.212 32.064 1.00 34.40 ? 366  LEU A CD1 1 
ATOM   2737  C  CD2 . LEU A  1 366 ? 74.480  61.539 32.259 1.00 35.42 ? 366  LEU A CD2 1 
ATOM   2738  N  N   . ASP A  1 367 ? 72.423  58.919 28.793 1.00 26.51 ? 367  ASP A N   1 
ATOM   2739  C  CA  . ASP A  1 367 ? 72.665  59.146 27.365 1.00 26.12 ? 367  ASP A CA  1 
ATOM   2740  C  C   . ASP A  1 367 ? 71.540  58.678 26.454 1.00 25.32 ? 367  ASP A C   1 
ATOM   2741  O  O   . ASP A  1 367 ? 71.610  58.874 25.250 1.00 25.82 ? 367  ASP A O   1 
ATOM   2742  C  CB  . ASP A  1 367 ? 73.980  58.488 26.909 1.00 27.14 ? 367  ASP A CB  1 
ATOM   2743  C  CG  . ASP A  1 367 ? 74.056  56.984 27.250 1.00 28.88 ? 367  ASP A CG  1 
ATOM   2744  O  OD1 . ASP A  1 367 ? 73.018  56.291 27.259 1.00 27.23 ? 367  ASP A OD1 1 
ATOM   2745  O  OD2 . ASP A  1 367 ? 75.181  56.493 27.491 1.00 30.89 ? 367  ASP A OD2 1 
ATOM   2746  N  N   . GLY A  1 368 ? 70.515  58.045 27.017 1.00 24.69 ? 368  GLY A N   1 
ATOM   2747  C  CA  . GLY A  1 368 ? 69.398  57.589 26.206 1.00 23.15 ? 368  GLY A CA  1 
ATOM   2748  C  C   . GLY A  1 368 ? 69.714  56.461 25.243 1.00 24.40 ? 368  GLY A C   1 
ATOM   2749  O  O   . GLY A  1 368 ? 68.894  56.150 24.371 1.00 23.75 ? 368  GLY A O   1 
ATOM   2750  N  N   . ASN A  1 369 ? 70.880  55.829 25.389 1.00 23.06 ? 369  ASN A N   1 
ATOM   2751  C  CA  . ASN A  1 369 ? 71.247  54.746 24.473 1.00 23.17 ? 369  ASN A CA  1 
ATOM   2752  C  C   . ASN A  1 369 ? 70.712  53.364 24.849 1.00 22.60 ? 369  ASN A C   1 
ATOM   2753  O  O   . ASN A  1 369 ? 70.776  52.430 24.052 1.00 22.10 ? 369  ASN A O   1 
ATOM   2754  C  CB  . ASN A  1 369 ? 72.769  54.672 24.301 1.00 23.41 ? 369  ASN A CB  1 
ATOM   2755  C  CG  . ASN A  1 369 ? 73.333  55.904 23.604 1.00 25.43 ? 369  ASN A CG  1 
ATOM   2756  O  OD1 . ASN A  1 369 ? 72.667  56.518 22.760 1.00 25.03 ? 369  ASN A OD1 1 
ATOM   2757  N  ND2 . ASN A  1 369 ? 74.570  56.263 23.944 1.00 25.24 ? 369  ASN A ND2 1 
ATOM   2758  N  N   . SER A  1 370 ? 70.202  53.230 26.066 1.00 21.94 ? 370  SER A N   1 
ATOM   2759  C  CA  . SER A  1 370 ? 69.650  51.958 26.517 1.00 22.88 ? 370  SER A CA  1 
ATOM   2760  C  C   . SER A  1 370 ? 68.580  52.268 27.553 1.00 22.29 ? 370  SER A C   1 
ATOM   2761  O  O   . SER A  1 370 ? 68.490  53.401 28.041 1.00 24.27 ? 370  SER A O   1 
ATOM   2762  C  CB  . SER A  1 370 ? 70.760  51.066 27.105 1.00 22.13 ? 370  SER A CB  1 
ATOM   2763  O  OG  . SER A  1 370 ? 71.424  51.683 28.197 1.00 23.69 ? 370  SER A OG  1 
ATOM   2764  N  N   . PHE A  1 371 ? 67.765  51.280 27.895 1.00 21.48 ? 371  PHE A N   1 
ATOM   2765  C  CA  . PHE A  1 371 ? 66.705  51.511 28.867 1.00 19.52 ? 371  PHE A CA  1 
ATOM   2766  C  C   . PHE A  1 371 ? 66.229  50.236 29.524 1.00 19.67 ? 371  PHE A C   1 
ATOM   2767  O  O   . PHE A  1 371 ? 66.429  49.130 28.998 1.00 18.39 ? 371  PHE A O   1 
ATOM   2768  C  CB  . PHE A  1 371 ? 65.516  52.212 28.196 1.00 19.16 ? 371  PHE A CB  1 
ATOM   2769  C  CG  . PHE A  1 371 ? 64.858  51.396 27.114 1.00 18.84 ? 371  PHE A CG  1 
ATOM   2770  C  CD1 . PHE A  1 371 ? 63.823  50.509 27.416 1.00 19.23 ? 371  PHE A CD1 1 
ATOM   2771  C  CD2 . PHE A  1 371 ? 65.258  51.532 25.791 1.00 18.11 ? 371  PHE A CD2 1 
ATOM   2772  C  CE1 . PHE A  1 371 ? 63.191  49.764 26.403 1.00 18.94 ? 371  PHE A CE1 1 
ATOM   2773  C  CE2 . PHE A  1 371 ? 64.644  50.807 24.777 1.00 19.58 ? 371  PHE A CE2 1 
ATOM   2774  C  CZ  . PHE A  1 371 ? 63.602  49.916 25.082 1.00 19.35 ? 371  PHE A CZ  1 
ATOM   2775  N  N   . TYR A  1 372 ? 65.580  50.420 30.672 1.00 18.38 ? 372  TYR A N   1 
ATOM   2776  C  CA  . TYR A  1 372 ? 65.039  49.333 31.462 1.00 18.88 ? 372  TYR A CA  1 
ATOM   2777  C  C   . TYR A  1 372 ? 63.512  49.358 31.385 1.00 19.55 ? 372  TYR A C   1 
ATOM   2778  O  O   . TYR A  1 372 ? 62.885  50.422 31.362 1.00 19.45 ? 372  TYR A O   1 
ATOM   2779  C  CB  . TYR A  1 372 ? 65.522  49.466 32.903 1.00 18.52 ? 372  TYR A CB  1 
ATOM   2780  C  CG  . TYR A  1 372 ? 67.031  49.418 33.015 1.00 16.99 ? 372  TYR A CG  1 
ATOM   2781  C  CD1 . TYR A  1 372 ? 67.802  50.572 32.836 1.00 16.15 ? 372  TYR A CD1 1 
ATOM   2782  C  CD2 . TYR A  1 372 ? 67.685  48.215 33.259 1.00 17.03 ? 372  TYR A CD2 1 
ATOM   2783  C  CE1 . TYR A  1 372 ? 69.194  50.525 32.897 1.00 18.40 ? 372  TYR A CE1 1 
ATOM   2784  C  CE2 . TYR A  1 372 ? 69.075  48.148 33.319 1.00 18.26 ? 372  TYR A CE2 1 
ATOM   2785  C  CZ  . TYR A  1 372 ? 69.820  49.302 33.140 1.00 17.23 ? 372  TYR A CZ  1 
ATOM   2786  O  OH  . TYR A  1 372 ? 71.182  49.236 33.189 1.00 19.12 ? 372  TYR A OH  1 
ATOM   2787  N  N   . LYS A  1 373 ? 62.912  48.179 31.344 1.00 19.21 ? 373  LYS A N   1 
ATOM   2788  C  CA  . LYS A  1 373 ? 61.464  48.090 31.214 1.00 19.67 ? 373  LYS A CA  1 
ATOM   2789  C  C   . LYS A  1 373 ? 60.974  46.777 31.837 1.00 20.38 ? 373  LYS A C   1 
ATOM   2790  O  O   . LYS A  1 373 ? 61.595  45.718 31.650 1.00 20.90 ? 373  LYS A O   1 
ATOM   2791  C  CB  . LYS A  1 373 ? 61.111  48.123 29.716 1.00 18.62 ? 373  LYS A CB  1 
ATOM   2792  C  CG  . LYS A  1 373 ? 59.637  48.310 29.356 1.00 19.90 ? 373  LYS A CG  1 
ATOM   2793  C  CD  . LYS A  1 373 ? 59.469  48.215 27.821 1.00 19.48 ? 373  LYS A CD  1 
ATOM   2794  C  CE  . LYS A  1 373 ? 58.231  48.919 27.258 1.00 19.25 ? 373  LYS A CE  1 
ATOM   2795  N  NZ  . LYS A  1 373 ? 56.916  48.252 27.550 1.00 19.65 ? 373  LYS A NZ  1 
ATOM   2796  N  N   . ILE A  1 374 ? 59.864  46.859 32.564 1.00 18.73 ? 374  ILE A N   1 
ATOM   2797  C  CA  . ILE A  1 374 ? 59.269  45.695 33.185 1.00 18.42 ? 374  ILE A CA  1 
ATOM   2798  C  C   . ILE A  1 374 ? 58.464  44.961 32.129 1.00 18.90 ? 374  ILE A C   1 
ATOM   2799  O  O   . ILE A  1 374 ? 57.600  45.554 31.503 1.00 18.64 ? 374  ILE A O   1 
ATOM   2800  C  CB  . ILE A  1 374 ? 58.287  46.095 34.339 1.00 18.23 ? 374  ILE A CB  1 
ATOM   2801  C  CG1 . ILE A  1 374 ? 59.057  46.717 35.490 1.00 15.76 ? 374  ILE A CG1 1 
ATOM   2802  C  CG2 . ILE A  1 374 ? 57.454  44.872 34.792 1.00 14.60 ? 374  ILE A CG2 1 
ATOM   2803  C  CD1 . ILE A  1 374 ? 58.163  47.472 36.502 1.00 15.72 ? 374  ILE A CD1 1 
ATOM   2804  N  N   . ILE A  1 375 ? 58.763  43.682 31.911 1.00 20.55 ? 375  ILE A N   1 
ATOM   2805  C  CA  . ILE A  1 375 ? 58.001  42.893 30.942 1.00 21.51 ? 375  ILE A CA  1 
ATOM   2806  C  C   . ILE A  1 375 ? 57.834  41.468 31.436 1.00 21.37 ? 375  ILE A C   1 
ATOM   2807  O  O   . ILE A  1 375 ? 58.606  40.978 32.265 1.00 20.63 ? 375  ILE A O   1 
ATOM   2808  C  CB  . ILE A  1 375 ? 58.650  42.828 29.525 1.00 22.82 ? 375  ILE A CB  1 
ATOM   2809  C  CG1 . ILE A  1 375 ? 59.990  42.097 29.577 1.00 23.95 ? 375  ILE A CG1 1 
ATOM   2810  C  CG2 . ILE A  1 375 ? 58.814  44.224 28.951 1.00 22.89 ? 375  ILE A CG2 1 
ATOM   2811  C  CD1 . ILE A  1 375 ? 60.598  41.879 28.191 1.00 25.94 ? 375  ILE A CD1 1 
ATOM   2812  N  N   . SER A  1 376 ? 56.808  40.808 30.925 1.00 21.74 ? 376  SER A N   1 
ATOM   2813  C  CA  . SER A  1 376 ? 56.545  39.444 31.321 1.00 23.39 ? 376  SER A CA  1 
ATOM   2814  C  C   . SER A  1 376 ? 57.640  38.544 30.742 1.00 22.50 ? 376  SER A C   1 
ATOM   2815  O  O   . SER A  1 376 ? 57.899  38.579 29.545 1.00 22.21 ? 376  SER A O   1 
ATOM   2816  C  CB  . SER A  1 376 ? 55.172  39.023 30.809 1.00 23.01 ? 376  SER A CB  1 
ATOM   2817  O  OG  . SER A  1 376 ? 54.850  37.756 31.350 1.00 27.59 ? 376  SER A OG  1 
ATOM   2818  N  N   . ASN A  1 377 ? 58.292  37.758 31.595 1.00 23.15 ? 377  ASN A N   1 
ATOM   2819  C  CA  . ASN A  1 377 ? 59.355  36.870 31.146 1.00 23.13 ? 377  ASN A CA  1 
ATOM   2820  C  C   . ASN A  1 377 ? 58.796  35.526 30.675 1.00 25.69 ? 377  ASN A C   1 
ATOM   2821  O  O   . ASN A  1 377 ? 57.577  35.344 30.648 1.00 26.09 ? 377  ASN A O   1 
ATOM   2822  C  CB  . ASN A  1 377 ? 60.395  36.678 32.255 1.00 20.05 ? 377  ASN A CB  1 
ATOM   2823  C  CG  . ASN A  1 377 ? 59.911  35.778 33.382 1.00 19.81 ? 377  ASN A CG  1 
ATOM   2824  O  OD1 . ASN A  1 377 ? 58.809  35.212 33.335 1.00 19.93 ? 377  ASN A OD1 1 
ATOM   2825  N  ND2 . ASN A  1 377 ? 60.741  35.642 34.406 1.00 17.63 ? 377  ASN A ND2 1 
ATOM   2826  N  N   . GLU A  1 378 ? 59.669  34.591 30.297 1.00 28.75 ? 378  GLU A N   1 
ATOM   2827  C  CA  . GLU A  1 378 ? 59.214  33.275 29.792 1.00 32.05 ? 378  GLU A CA  1 
ATOM   2828  C  C   . GLU A  1 378 ? 58.403  32.451 30.781 1.00 31.78 ? 378  GLU A C   1 
ATOM   2829  O  O   . GLU A  1 378 ? 57.667  31.556 30.381 1.00 31.86 ? 378  GLU A O   1 
ATOM   2830  C  CB  . GLU A  1 378 ? 60.405  32.445 29.304 1.00 35.00 ? 378  GLU A CB  1 
ATOM   2831  C  CG  . GLU A  1 378 ? 61.124  33.045 28.091 1.00 40.79 ? 378  GLU A CG  1 
ATOM   2832  C  CD  . GLU A  1 378 ? 60.302  32.975 26.804 1.00 45.04 ? 378  GLU A CD  1 
ATOM   2833  O  OE1 . GLU A  1 378 ? 60.754  33.553 25.784 1.00 47.45 ? 378  GLU A OE1 1 
ATOM   2834  O  OE2 . GLU A  1 378 ? 59.214  32.342 26.803 1.00 47.18 ? 378  GLU A OE2 1 
ATOM   2835  N  N   . GLU A  1 379 ? 58.535  32.745 32.066 1.00 31.39 ? 379  GLU A N   1 
ATOM   2836  C  CA  . GLU A  1 379 ? 57.774  32.025 33.073 1.00 31.64 ? 379  GLU A CA  1 
ATOM   2837  C  C   . GLU A  1 379 ? 56.445  32.742 33.347 1.00 30.56 ? 379  GLU A C   1 
ATOM   2838  O  O   . GLU A  1 379 ? 55.588  32.256 34.094 1.00 29.51 ? 379  GLU A O   1 
ATOM   2839  C  CB  . GLU A  1 379 ? 58.585  31.925 34.364 1.00 35.02 ? 379  GLU A CB  1 
ATOM   2840  C  CG  . GLU A  1 379 ? 59.649  30.853 34.347 1.00 39.37 ? 379  GLU A CG  1 
ATOM   2841  C  CD  . GLU A  1 379 ? 59.053  29.497 34.059 1.00 43.91 ? 379  GLU A CD  1 
ATOM   2842  O  OE1 . GLU A  1 379 ? 58.186  29.030 34.849 1.00 45.86 ? 379  GLU A OE1 1 
ATOM   2843  O  OE2 . GLU A  1 379 ? 59.440  28.889 33.033 1.00 46.26 ? 379  GLU A OE2 1 
ATOM   2844  N  N   . GLY A  1 380 ? 56.272  33.909 32.743 1.00 28.41 ? 380  GLY A N   1 
ATOM   2845  C  CA  . GLY A  1 380 ? 55.052  34.648 32.976 1.00 26.31 ? 380  GLY A CA  1 
ATOM   2846  C  C   . GLY A  1 380 ? 55.140  35.594 34.168 1.00 25.43 ? 380  GLY A C   1 
ATOM   2847  O  O   . GLY A  1 380 ? 54.119  36.096 34.624 1.00 24.86 ? 380  GLY A O   1 
ATOM   2848  N  N   . TYR A  1 381 ? 56.346  35.828 34.687 1.00 24.49 ? 381  TYR A N   1 
ATOM   2849  C  CA  . TYR A  1 381 ? 56.521  36.757 35.799 1.00 22.42 ? 381  TYR A CA  1 
ATOM   2850  C  C   . TYR A  1 381 ? 57.135  38.050 35.295 1.00 22.04 ? 381  TYR A C   1 
ATOM   2851  O  O   . TYR A  1 381 ? 58.091  38.046 34.505 1.00 21.35 ? 381  TYR A O   1 
ATOM   2852  C  CB  . TYR A  1 381 ? 57.402  36.154 36.888 1.00 23.21 ? 381  TYR A CB  1 
ATOM   2853  C  CG  . TYR A  1 381 ? 56.708  35.054 37.644 1.00 24.19 ? 381  TYR A CG  1 
ATOM   2854  C  CD1 . TYR A  1 381 ? 56.642  33.751 37.125 1.00 23.93 ? 381  TYR A CD1 1 
ATOM   2855  C  CD2 . TYR A  1 381 ? 56.076  35.314 38.858 1.00 24.05 ? 381  TYR A CD2 1 
ATOM   2856  C  CE1 . TYR A  1 381 ? 55.960  32.741 37.806 1.00 22.99 ? 381  TYR A CE1 1 
ATOM   2857  C  CE2 . TYR A  1 381 ? 55.389  34.303 39.544 1.00 22.88 ? 381  TYR A CE2 1 
ATOM   2858  C  CZ  . TYR A  1 381 ? 55.341  33.032 39.014 1.00 23.12 ? 381  TYR A CZ  1 
ATOM   2859  O  OH  . TYR A  1 381 ? 54.703  32.035 39.709 1.00 25.90 ? 381  TYR A OH  1 
ATOM   2860  N  N   . ARG A  1 382 ? 56.578  39.163 35.757 1.00 20.31 ? 382  ARG A N   1 
ATOM   2861  C  CA  . ARG A  1 382 ? 57.050  40.473 35.328 1.00 18.82 ? 382  ARG A CA  1 
ATOM   2862  C  C   . ARG A  1 382 ? 58.349  40.863 36.017 1.00 17.61 ? 382  ARG A C   1 
ATOM   2863  O  O   . ARG A  1 382 ? 58.432  40.972 37.235 1.00 15.45 ? 382  ARG A O   1 
ATOM   2864  C  CB  . ARG A  1 382 ? 55.937  41.505 35.547 1.00 18.92 ? 382  ARG A CB  1 
ATOM   2865  C  CG  . ARG A  1 382 ? 54.881  41.385 34.452 1.00 21.11 ? 382  ARG A CG  1 
ATOM   2866  C  CD  . ARG A  1 382 ? 53.503  41.926 34.818 1.00 20.62 ? 382  ARG A CD  1 
ATOM   2867  N  NE  . ARG A  1 382 ? 52.497  41.204 34.041 1.00 21.00 ? 382  ARG A NE  1 
ATOM   2868  C  CZ  . ARG A  1 382 ? 52.292  41.350 32.737 1.00 21.26 ? 382  ARG A CZ  1 
ATOM   2869  N  NH1 . ARG A  1 382 ? 52.997  42.223 32.026 1.00 21.43 ? 382  ARG A NH1 1 
ATOM   2870  N  NH2 . ARG A  1 382 ? 51.436  40.555 32.122 1.00 19.54 ? 382  ARG A NH2 1 
ATOM   2871  N  N   . HIS A  1 383 ? 59.367  41.055 35.194 1.00 17.16 ? 383  HIS A N   1 
ATOM   2872  C  CA  . HIS A  1 383 ? 60.679  41.412 35.667 1.00 17.07 ? 383  HIS A CA  1 
ATOM   2873  C  C   . HIS A  1 383 ? 61.308  42.502 34.814 1.00 17.05 ? 383  HIS A C   1 
ATOM   2874  O  O   . HIS A  1 383 ? 60.820  42.822 33.724 1.00 16.80 ? 383  HIS A O   1 
ATOM   2875  C  CB  . HIS A  1 383 ? 61.548  40.164 35.697 1.00 16.54 ? 383  HIS A CB  1 
ATOM   2876  C  CG  . HIS A  1 383 ? 61.169  39.209 36.778 1.00 16.87 ? 383  HIS A CG  1 
ATOM   2877  N  ND1 . HIS A  1 383 ? 61.489  39.424 38.103 1.00 17.05 ? 383  HIS A ND1 1 
ATOM   2878  C  CD2 . HIS A  1 383 ? 60.461  38.053 36.748 1.00 17.04 ? 383  HIS A CD2 1 
ATOM   2879  C  CE1 . HIS A  1 383 ? 60.997  38.445 38.838 1.00 17.40 ? 383  HIS A CE1 1 
ATOM   2880  N  NE2 . HIS A  1 383 ? 60.366  37.599 38.039 1.00 18.17 ? 383  HIS A NE2 1 
ATOM   2881  N  N   . ILE A  1 384 ? 62.395  43.072 35.311 1.00 17.42 ? 384  ILE A N   1 
ATOM   2882  C  CA  . ILE A  1 384 ? 63.063  44.152 34.596 1.00 19.28 ? 384  ILE A CA  1 
ATOM   2883  C  C   . ILE A  1 384 ? 63.974  43.602 33.498 1.00 20.09 ? 384  ILE A C   1 
ATOM   2884  O  O   . ILE A  1 384 ? 64.795  42.727 33.752 1.00 20.57 ? 384  ILE A O   1 
ATOM   2885  C  CB  . ILE A  1 384 ? 63.891  45.003 35.581 1.00 18.48 ? 384  ILE A CB  1 
ATOM   2886  C  CG1 . ILE A  1 384 ? 62.961  45.598 36.657 1.00 18.69 ? 384  ILE A CG1 1 
ATOM   2887  C  CG2 . ILE A  1 384 ? 64.601  46.123 34.846 1.00 18.83 ? 384  ILE A CG2 1 
ATOM   2888  C  CD1 . ILE A  1 384 ? 63.711  46.100 37.885 1.00 17.12 ? 384  ILE A CD1 1 
ATOM   2889  N  N   . CYS A  1 385 ? 63.825  44.105 32.279 1.00 21.50 ? 385  CYS A N   1 
ATOM   2890  C  CA  . CYS A  1 385 ? 64.672  43.658 31.176 1.00 23.07 ? 385  CYS A CA  1 
ATOM   2891  C  C   . CYS A  1 385 ? 65.491  44.891 30.770 1.00 22.06 ? 385  CYS A C   1 
ATOM   2892  O  O   . CYS A  1 385 ? 65.006  46.018 30.859 1.00 23.29 ? 385  CYS A O   1 
ATOM   2893  C  CB  . CYS A  1 385 ? 63.829  43.132 29.986 1.00 23.83 ? 385  CYS A CB  1 
ATOM   2894  S  SG  . CYS A  1 385 ? 64.678  41.778 29.055 1.00 31.95 ? 385  CYS A SG  1 
ATOM   2895  N  N   . TYR A  1 386 ? 66.732  44.679 30.352 1.00 21.25 ? 386  TYR A N   1 
ATOM   2896  C  CA  . TYR A  1 386 ? 67.608  45.767 29.944 1.00 20.65 ? 386  TYR A CA  1 
ATOM   2897  C  C   . TYR A  1 386 ? 67.687  45.736 28.433 1.00 21.27 ? 386  TYR A C   1 
ATOM   2898  O  O   . TYR A  1 386 ? 68.020  44.703 27.846 1.00 20.86 ? 386  TYR A O   1 
ATOM   2899  C  CB  . TYR A  1 386 ? 69.001  45.588 30.555 1.00 20.61 ? 386  TYR A CB  1 
ATOM   2900  C  CG  . TYR A  1 386 ? 70.031  46.649 30.175 1.00 21.50 ? 386  TYR A CG  1 
ATOM   2901  C  CD1 . TYR A  1 386 ? 69.677  47.993 30.088 1.00 22.12 ? 386  TYR A CD1 1 
ATOM   2902  C  CD2 . TYR A  1 386 ? 71.365  46.307 29.955 1.00 21.81 ? 386  TYR A CD2 1 
ATOM   2903  C  CE1 . TYR A  1 386 ? 70.618  48.973 29.794 1.00 23.55 ? 386  TYR A CE1 1 
ATOM   2904  C  CE2 . TYR A  1 386 ? 72.322  47.280 29.666 1.00 23.86 ? 386  TYR A CE2 1 
ATOM   2905  C  CZ  . TYR A  1 386 ? 71.945  48.606 29.587 1.00 24.31 ? 386  TYR A CZ  1 
ATOM   2906  O  OH  . TYR A  1 386 ? 72.883  49.572 29.315 1.00 26.25 ? 386  TYR A OH  1 
ATOM   2907  N  N   . PHE A  1 387 ? 67.356  46.865 27.813 1.00 21.14 ? 387  PHE A N   1 
ATOM   2908  C  CA  . PHE A  1 387 ? 67.350  46.998 26.353 1.00 21.46 ? 387  PHE A CA  1 
ATOM   2909  C  C   . PHE A  1 387 ? 68.398  47.999 25.854 1.00 21.69 ? 387  PHE A C   1 
ATOM   2910  O  O   . PHE A  1 387 ? 68.696  48.990 26.518 1.00 21.87 ? 387  PHE A O   1 
ATOM   2911  C  CB  . PHE A  1 387 ? 66.003  47.537 25.858 1.00 20.48 ? 387  PHE A CB  1 
ATOM   2912  C  CG  . PHE A  1 387 ? 64.830  46.604 26.023 1.00 19.25 ? 387  PHE A CG  1 
ATOM   2913  C  CD1 . PHE A  1 387 ? 64.313  45.924 24.924 1.00 20.53 ? 387  PHE A CD1 1 
ATOM   2914  C  CD2 . PHE A  1 387 ? 64.145  46.538 27.224 1.00 18.05 ? 387  PHE A CD2 1 
ATOM   2915  C  CE1 . PHE A  1 387 ? 63.109  45.201 25.017 1.00 22.07 ? 387  PHE A CE1 1 
ATOM   2916  C  CE2 . PHE A  1 387 ? 62.943  45.820 27.335 1.00 18.58 ? 387  PHE A CE2 1 
ATOM   2917  C  CZ  . PHE A  1 387 ? 62.423  45.157 26.232 1.00 20.24 ? 387  PHE A CZ  1 
ATOM   2918  N  N   . GLN A  1 388 ? 68.911  47.721 24.660 1.00 22.94 ? 388  GLN A N   1 
ATOM   2919  C  CA  . GLN A  1 388 ? 69.861  48.555 23.910 1.00 23.41 ? 388  GLN A CA  1 
ATOM   2920  C  C   . GLN A  1 388 ? 68.879  49.148 22.880 1.00 23.34 ? 388  GLN A C   1 
ATOM   2921  O  O   . GLN A  1 388 ? 68.095  48.393 22.322 1.00 22.18 ? 388  GLN A O   1 
ATOM   2922  C  CB  . GLN A  1 388 ? 70.855  47.647 23.184 1.00 25.10 ? 388  GLN A CB  1 
ATOM   2923  C  CG  . GLN A  1 388 ? 72.301  47.679 23.645 1.00 26.85 ? 388  GLN A CG  1 
ATOM   2924  C  CD  . GLN A  1 388 ? 72.486  47.933 25.124 1.00 27.50 ? 388  GLN A CD  1 
ATOM   2925  O  OE1 . GLN A  1 388 ? 72.013  47.183 25.982 1.00 31.76 ? 388  GLN A OE1 1 
ATOM   2926  N  NE2 . GLN A  1 388 ? 73.201  48.993 25.432 1.00 27.43 ? 388  GLN A NE2 1 
ATOM   2927  N  N   . ILE A  1 389 ? 68.904  50.450 22.591 1.00 23.87 ? 389  ILE A N   1 
ATOM   2928  C  CA  . ILE A  1 389 ? 67.898  50.978 21.658 1.00 25.52 ? 389  ILE A CA  1 
ATOM   2929  C  C   . ILE A  1 389 ? 67.885  50.397 20.250 1.00 28.27 ? 389  ILE A C   1 
ATOM   2930  O  O   . ILE A  1 389 ? 66.853  50.426 19.562 1.00 26.87 ? 389  ILE A O   1 
ATOM   2931  C  CB  . ILE A  1 389 ? 67.928  52.533 21.527 1.00 24.48 ? 389  ILE A CB  1 
ATOM   2932  C  CG1 . ILE A  1 389 ? 69.262  53.006 20.958 1.00 24.37 ? 389  ILE A CG1 1 
ATOM   2933  C  CG2 . ILE A  1 389 ? 67.628  53.178 22.888 1.00 23.21 ? 389  ILE A CG2 1 
ATOM   2934  C  CD1 . ILE A  1 389 ? 69.275  54.495 20.660 1.00 23.37 ? 389  ILE A CD1 1 
ATOM   2935  N  N   . ASP A  1 390 ? 69.014  49.857 19.816 1.00 29.87 ? 390  ASP A N   1 
ATOM   2936  C  CA  . ASP A  1 390 ? 69.085  49.299 18.479 1.00 32.49 ? 390  ASP A CA  1 
ATOM   2937  C  C   . ASP A  1 390 ? 69.328  47.802 18.501 1.00 33.50 ? 390  ASP A C   1 
ATOM   2938  O  O   . ASP A  1 390 ? 69.922  47.256 17.583 1.00 34.98 ? 390  ASP A O   1 
ATOM   2939  C  CB  . ASP A  1 390 ? 70.184  50.003 17.667 1.00 34.09 ? 390  ASP A CB  1 
ATOM   2940  C  CG  . ASP A  1 390 ? 71.546  49.959 18.353 1.00 36.46 ? 390  ASP A CG  1 
ATOM   2941  O  OD1 . ASP A  1 390 ? 71.623  49.531 19.525 1.00 35.51 ? 390  ASP A OD1 1 
ATOM   2942  O  OD2 . ASP A  1 390 ? 72.544  50.366 17.718 1.00 38.70 ? 390  ASP A OD2 1 
ATOM   2943  N  N   . LYS A  1 391 ? 68.866  47.136 19.551 1.00 33.79 ? 391  LYS A N   1 
ATOM   2944  C  CA  . LYS A  1 391 ? 69.023  45.693 19.654 1.00 34.49 ? 391  LYS A CA  1 
ATOM   2945  C  C   . LYS A  1 391 ? 67.671  45.100 20.016 1.00 34.75 ? 391  LYS A C   1 
ATOM   2946  O  O   . LYS A  1 391 ? 66.966  45.639 20.880 1.00 32.94 ? 391  LYS A O   1 
ATOM   2947  C  CB  . LYS A  1 391 ? 70.062  45.336 20.721 1.00 35.63 ? 391  LYS A CB  1 
ATOM   2948  C  CG  . LYS A  1 391 ? 71.410  44.896 20.148 1.00 38.30 ? 391  LYS A CG  1 
ATOM   2949  C  CD  . LYS A  1 391 ? 72.068  45.987 19.323 1.00 40.58 ? 391  LYS A CD  1 
ATOM   2950  C  CE  . LYS A  1 391 ? 73.356  45.499 18.644 1.00 41.61 ? 391  LYS A CE  1 
ATOM   2951  N  NZ  . LYS A  1 391 ? 74.430  45.161 19.618 1.00 43.12 ? 391  LYS A NZ  1 
ATOM   2952  N  N   . LYS A  1 392 ? 67.314  43.994 19.361 1.00 34.80 ? 392  LYS A N   1 
ATOM   2953  C  CA  . LYS A  1 392 ? 66.031  43.353 19.611 1.00 35.41 ? 392  LYS A CA  1 
ATOM   2954  C  C   . LYS A  1 392 ? 65.983  42.624 20.933 1.00 34.83 ? 392  LYS A C   1 
ATOM   2955  O  O   . LYS A  1 392 ? 65.008  42.736 21.666 1.00 35.10 ? 392  LYS A O   1 
ATOM   2956  C  CB  . LYS A  1 392 ? 65.671  42.362 18.499 1.00 37.57 ? 392  LYS A CB  1 
ATOM   2957  C  CG  . LYS A  1 392 ? 65.547  42.978 17.096 1.00 41.96 ? 392  LYS A CG  1 
ATOM   2958  C  CD  . LYS A  1 392 ? 64.446  44.043 16.988 1.00 44.20 ? 392  LYS A CD  1 
ATOM   2959  C  CE  . LYS A  1 392 ? 64.358  44.620 15.563 1.00 44.98 ? 392  LYS A CE  1 
ATOM   2960  N  NZ  . LYS A  1 392 ? 65.673  45.182 15.111 1.00 46.03 ? 392  LYS A NZ  1 
ATOM   2961  N  N   . ASP A  1 393 ? 67.024  41.871 21.241 1.00 34.19 ? 393  ASP A N   1 
ATOM   2962  C  CA  . ASP A  1 393 ? 67.036  41.119 22.490 1.00 34.54 ? 393  ASP A CA  1 
ATOM   2963  C  C   . ASP A  1 393 ? 67.391  41.963 23.689 1.00 33.09 ? 393  ASP A C   1 
ATOM   2964  O  O   . ASP A  1 393 ? 68.364  42.720 23.682 1.00 32.95 ? 393  ASP A O   1 
ATOM   2965  C  CB  . ASP A  1 393 ? 68.025  39.954 22.436 1.00 36.74 ? 393  ASP A CB  1 
ATOM   2966  C  CG  . ASP A  1 393 ? 67.769  39.033 21.282 1.00 39.01 ? 393  ASP A CG  1 
ATOM   2967  O  OD1 . ASP A  1 393 ? 66.585  38.860 20.887 1.00 39.85 ? 393  ASP A OD1 1 
ATOM   2968  O  OD2 . ASP A  1 393 ? 68.761  38.462 20.780 1.00 41.57 ? 393  ASP A OD2 1 
ATOM   2969  N  N   . CYS A  1 394 ? 66.588  41.816 24.732 1.00 31.05 ? 394  CYS A N   1 
ATOM   2970  C  CA  . CYS A  1 394 ? 66.825  42.531 25.970 1.00 28.81 ? 394  CYS A CA  1 
ATOM   2971  C  C   . CYS A  1 394 ? 67.317  41.465 26.943 1.00 27.48 ? 394  CYS A C   1 
ATOM   2972  O  O   . CYS A  1 394 ? 67.152  40.270 26.687 1.00 25.89 ? 394  CYS A O   1 
ATOM   2973  C  CB  . CYS A  1 394 ? 65.528  43.169 26.471 1.00 29.34 ? 394  CYS A CB  1 
ATOM   2974  S  SG  . CYS A  1 394 ? 64.249  42.011 27.048 1.00 29.96 ? 394  CYS A SG  1 
ATOM   2975  N  N   . THR A  1 395 ? 67.913  41.889 28.051 1.00 25.78 ? 395  THR A N   1 
ATOM   2976  C  CA  . THR A  1 395 ? 68.414  40.952 29.056 1.00 23.98 ? 395  THR A CA  1 
ATOM   2977  C  C   . THR A  1 395 ? 67.701  41.193 30.369 1.00 23.13 ? 395  THR A C   1 
ATOM   2978  O  O   . THR A  1 395 ? 67.647  42.324 30.838 1.00 22.60 ? 395  THR A O   1 
ATOM   2979  C  CB  . THR A  1 395 ? 69.911  41.166 29.305 1.00 24.02 ? 395  THR A CB  1 
ATOM   2980  O  OG1 . THR A  1 395 ? 70.621  41.033 28.074 1.00 24.81 ? 395  THR A OG1 1 
ATOM   2981  C  CG2 . THR A  1 395 ? 70.444  40.161 30.299 1.00 24.98 ? 395  THR A CG2 1 
ATOM   2982  N  N   . PHE A  1 396 ? 67.171  40.137 30.975 1.00 22.49 ? 396  PHE A N   1 
ATOM   2983  C  CA  . PHE A  1 396 ? 66.472  40.272 32.251 1.00 22.38 ? 396  PHE A CA  1 
ATOM   2984  C  C   . PHE A  1 396 ? 67.457  40.422 33.407 1.00 22.35 ? 396  PHE A C   1 
ATOM   2985  O  O   . PHE A  1 396 ? 68.354  39.599 33.576 1.00 23.26 ? 396  PHE A O   1 
ATOM   2986  C  CB  . PHE A  1 396 ? 65.575  39.055 32.501 1.00 21.48 ? 396  PHE A CB  1 
ATOM   2987  C  CG  . PHE A  1 396 ? 64.273  39.104 31.763 1.00 20.50 ? 396  PHE A CG  1 
ATOM   2988  C  CD1 . PHE A  1 396 ? 63.221  39.893 32.226 1.00 19.43 ? 396  PHE A CD1 1 
ATOM   2989  C  CD2 . PHE A  1 396 ? 64.093  38.364 30.601 1.00 20.28 ? 396  PHE A CD2 1 
ATOM   2990  C  CE1 . PHE A  1 396 ? 62.010  39.949 31.536 1.00 18.15 ? 396  PHE A CE1 1 
ATOM   2991  C  CE2 . PHE A  1 396 ? 62.884  38.415 29.900 1.00 20.25 ? 396  PHE A CE2 1 
ATOM   2992  C  CZ  . PHE A  1 396 ? 61.837  39.209 30.371 1.00 18.33 ? 396  PHE A CZ  1 
ATOM   2993  N  N   . ILE A  1 397 ? 67.292  41.463 34.216 1.00 21.23 ? 397  ILE A N   1 
ATOM   2994  C  CA  . ILE A  1 397 ? 68.205  41.652 35.325 1.00 19.28 ? 397  ILE A CA  1 
ATOM   2995  C  C   . ILE A  1 397 ? 67.675  41.137 36.665 1.00 19.09 ? 397  ILE A C   1 
ATOM   2996  O  O   . ILE A  1 397 ? 68.420  41.060 37.642 1.00 17.93 ? 397  ILE A O   1 
ATOM   2997  C  CB  . ILE A  1 397 ? 68.629  43.113 35.417 1.00 19.60 ? 397  ILE A CB  1 
ATOM   2998  C  CG1 . ILE A  1 397 ? 67.540  43.969 36.053 1.00 17.56 ? 397  ILE A CG1 1 
ATOM   2999  C  CG2 . ILE A  1 397 ? 68.944  43.615 34.006 1.00 19.98 ? 397  ILE A CG2 1 
ATOM   3000  C  CD1 . ILE A  1 397 ? 67.928  45.429 36.124 1.00 17.90 ? 397  ILE A CD1 1 
ATOM   3001  N  N   . THR A  1 398 ? 66.387  40.795 36.713 1.00 19.59 ? 398  THR A N   1 
ATOM   3002  C  CA  . THR A  1 398 ? 65.781  40.219 37.917 1.00 20.07 ? 398  THR A CA  1 
ATOM   3003  C  C   . THR A  1 398 ? 65.012  38.999 37.450 1.00 21.12 ? 398  THR A C   1 
ATOM   3004  O  O   . THR A  1 398 ? 64.634  38.901 36.274 1.00 19.99 ? 398  THR A O   1 
ATOM   3005  C  CB  . THR A  1 398 ? 64.764  41.158 38.645 1.00 20.31 ? 398  THR A CB  1 
ATOM   3006  O  OG1 . THR A  1 398 ? 63.732  41.571 37.738 1.00 20.35 ? 398  THR A OG1 1 
ATOM   3007  C  CG2 . THR A  1 398 ? 65.465  42.347 39.256 1.00 18.62 ? 398  THR A CG2 1 
ATOM   3008  N  N   . LYS A  1 399 ? 64.771  38.072 38.369 1.00 21.67 ? 399  LYS A N   1 
ATOM   3009  C  CA  . LYS A  1 399 ? 64.049  36.857 38.024 1.00 23.93 ? 399  LYS A CA  1 
ATOM   3010  C  C   . LYS A  1 399 ? 63.557  36.161 39.291 1.00 23.82 ? 399  LYS A C   1 
ATOM   3011  O  O   . LYS A  1 399 ? 64.034  36.450 40.389 1.00 24.55 ? 399  LYS A O   1 
ATOM   3012  C  CB  . LYS A  1 399 ? 64.966  35.921 37.223 1.00 26.29 ? 399  LYS A CB  1 
ATOM   3013  C  CG  . LYS A  1 399 ? 66.286  35.573 37.925 1.00 28.80 ? 399  LYS A CG  1 
ATOM   3014  C  CD  . LYS A  1 399 ? 67.010  34.404 37.226 1.00 33.25 ? 399  LYS A CD  1 
ATOM   3015  C  CE  . LYS A  1 399 ? 68.420  34.147 37.791 1.00 34.66 ? 399  LYS A CE  1 
ATOM   3016  N  NZ  . LYS A  1 399 ? 68.444  33.904 39.273 1.00 35.97 ? 399  LYS A NZ  1 
ATOM   3017  N  N   . GLY A  1 400 ? 62.612  35.244 39.135 1.00 23.11 ? 400  GLY A N   1 
ATOM   3018  C  CA  . GLY A  1 400 ? 62.072  34.540 40.288 1.00 22.60 ? 400  GLY A CA  1 
ATOM   3019  C  C   . GLY A  1 400 ? 60.549  34.488 40.293 1.00 22.88 ? 400  GLY A C   1 
ATOM   3020  O  O   . GLY A  1 400 ? 59.890  35.164 39.493 1.00 23.52 ? 400  GLY A O   1 
ATOM   3021  N  N   . THR A  1 401 ? 59.980  33.689 41.192 1.00 22.65 ? 401  THR A N   1 
ATOM   3022  C  CA  . THR A  1 401 ? 58.535  33.543 41.264 1.00 22.57 ? 401  THR A CA  1 
ATOM   3023  C  C   . THR A  1 401 ? 57.923  34.635 42.120 1.00 22.02 ? 401  THR A C   1 
ATOM   3024  O  O   . THR A  1 401 ? 57.349  34.389 43.174 1.00 22.69 ? 401  THR A O   1 
ATOM   3025  C  CB  . THR A  1 401 ? 58.139  32.131 41.797 1.00 22.57 ? 401  THR A CB  1 
ATOM   3026  O  OG1 . THR A  1 401 ? 58.705  31.929 43.093 1.00 22.32 ? 401  THR A OG1 1 
ATOM   3027  C  CG2 . THR A  1 401 ? 58.669  31.050 40.864 1.00 21.01 ? 401  THR A CG2 1 
ATOM   3028  N  N   . TRP A  1 402 ? 58.079  35.860 41.637 1.00 21.87 ? 402  TRP A N   1 
ATOM   3029  C  CA  . TRP A  1 402 ? 57.557  37.056 42.282 1.00 20.24 ? 402  TRP A CA  1 
ATOM   3030  C  C   . TRP A  1 402 ? 57.623  38.091 41.178 1.00 20.41 ? 402  TRP A C   1 
ATOM   3031  O  O   . TRP A  1 402 ? 58.098  37.782 40.074 1.00 20.29 ? 402  TRP A O   1 
ATOM   3032  C  CB  . TRP A  1 402 ? 58.425  37.478 43.475 1.00 20.75 ? 402  TRP A CB  1 
ATOM   3033  C  CG  . TRP A  1 402 ? 59.906  37.499 43.225 1.00 20.97 ? 402  TRP A CG  1 
ATOM   3034  C  CD1 . TRP A  1 402 ? 60.787  36.479 43.455 1.00 20.66 ? 402  TRP A CD1 1 
ATOM   3035  C  CD2 . TRP A  1 402 ? 60.688  38.603 42.738 1.00 20.80 ? 402  TRP A CD2 1 
ATOM   3036  N  NE1 . TRP A  1 402 ? 62.068  36.875 43.149 1.00 19.80 ? 402  TRP A NE1 1 
ATOM   3037  C  CE2 . TRP A  1 402 ? 62.041  38.172 42.706 1.00 20.66 ? 402  TRP A CE2 1 
ATOM   3038  C  CE3 . TRP A  1 402 ? 60.380  39.914 42.325 1.00 19.79 ? 402  TRP A CE3 1 
ATOM   3039  C  CZ2 . TRP A  1 402 ? 63.089  39.004 42.279 1.00 20.45 ? 402  TRP A CZ2 1 
ATOM   3040  C  CZ3 . TRP A  1 402 ? 61.418  40.741 41.899 1.00 18.81 ? 402  TRP A CZ3 1 
ATOM   3041  C  CH2 . TRP A  1 402 ? 62.761  40.280 41.880 1.00 20.21 ? 402  TRP A CH2 1 
ATOM   3042  N  N   . GLU A  1 403 ? 57.144  39.303 41.446 1.00 17.94 ? 403  GLU A N   1 
ATOM   3043  C  CA  . GLU A  1 403 ? 57.176  40.328 40.408 1.00 17.92 ? 403  GLU A CA  1 
ATOM   3044  C  C   . GLU A  1 403 ? 57.609  41.713 40.846 1.00 16.80 ? 403  GLU A C   1 
ATOM   3045  O  O   . GLU A  1 403 ? 57.411  42.136 41.982 1.00 17.12 ? 403  GLU A O   1 
ATOM   3046  C  CB  . GLU A  1 403 ? 55.803  40.470 39.738 1.00 17.22 ? 403  GLU A CB  1 
ATOM   3047  C  CG  . GLU A  1 403 ? 55.250  39.192 39.109 1.00 16.61 ? 403  GLU A CG  1 
ATOM   3048  C  CD  . GLU A  1 403 ? 54.104  39.478 38.155 1.00 17.46 ? 403  GLU A CD  1 
ATOM   3049  O  OE1 . GLU A  1 403 ? 53.250  40.314 38.500 1.00 20.19 ? 403  GLU A OE1 1 
ATOM   3050  O  OE2 . GLU A  1 403 ? 54.043  38.868 37.063 1.00 20.01 ? 403  GLU A OE2 1 
ATOM   3051  N  N   . VAL A  1 404 ? 58.215  42.411 39.906 1.00 17.06 ? 404  VAL A N   1 
ATOM   3052  C  CA  . VAL A  1 404 ? 58.624  43.770 40.120 1.00 15.94 ? 404  VAL A CA  1 
ATOM   3053  C  C   . VAL A  1 404 ? 57.338  44.560 39.874 1.00 16.34 ? 404  VAL A C   1 
ATOM   3054  O  O   . VAL A  1 404 ? 56.636  44.316 38.887 1.00 16.68 ? 404  VAL A O   1 
ATOM   3055  C  CB  . VAL A  1 404 ? 59.708  44.152 39.114 1.00 16.13 ? 404  VAL A CB  1 
ATOM   3056  C  CG1 . VAL A  1 404 ? 60.070  45.644 39.267 1.00 15.57 ? 404  VAL A CG1 1 
ATOM   3057  C  CG2 . VAL A  1 404 ? 60.942  43.276 39.354 1.00 13.01 ? 404  VAL A CG2 1 
ATOM   3058  N  N   . ILE A  1 405 ? 57.011  45.472 40.785 1.00 16.68 ? 405  ILE A N   1 
ATOM   3059  C  CA  . ILE A  1 405 ? 55.801  46.296 40.677 1.00 16.18 ? 405  ILE A CA  1 
ATOM   3060  C  C   . ILE A  1 405 ? 56.093  47.518 39.803 1.00 16.93 ? 405  ILE A C   1 
ATOM   3061  O  O   . ILE A  1 405 ? 55.303  47.893 38.927 1.00 18.63 ? 405  ILE A O   1 
ATOM   3062  C  CB  . ILE A  1 405 ? 55.352  46.780 42.079 1.00 17.40 ? 405  ILE A CB  1 
ATOM   3063  C  CG1 . ILE A  1 405 ? 55.306  45.589 43.035 1.00 18.84 ? 405  ILE A CG1 1 
ATOM   3064  C  CG2 . ILE A  1 405 ? 53.997  47.486 42.009 1.00 15.55 ? 405  ILE A CG2 1 
ATOM   3065  C  CD1 . ILE A  1 405 ? 54.311  44.495 42.647 1.00 17.84 ? 405  ILE A CD1 1 
ATOM   3066  N  N   . GLY A  1 406 ? 57.228  48.150 40.046 1.00 16.60 ? 406  GLY A N   1 
ATOM   3067  C  CA  . GLY A  1 406 ? 57.580  49.309 39.252 1.00 16.87 ? 406  GLY A CA  1 
ATOM   3068  C  C   . GLY A  1 406 ? 59.031  49.685 39.449 1.00 17.32 ? 406  GLY A C   1 
ATOM   3069  O  O   . GLY A  1 406 ? 59.632  49.321 40.462 1.00 18.77 ? 406  GLY A O   1 
ATOM   3070  N  N   . ILE A  1 407 ? 59.598  50.373 38.463 1.00 18.50 ? 407  ILE A N   1 
ATOM   3071  C  CA  . ILE A  1 407 ? 60.970  50.873 38.527 1.00 18.47 ? 407  ILE A CA  1 
ATOM   3072  C  C   . ILE A  1 407 ? 60.800  52.274 39.121 1.00 18.72 ? 407  ILE A C   1 
ATOM   3073  O  O   . ILE A  1 407 ? 60.006  53.069 38.623 1.00 18.65 ? 407  ILE A O   1 
ATOM   3074  C  CB  . ILE A  1 407 ? 61.603  50.963 37.123 1.00 17.36 ? 407  ILE A CB  1 
ATOM   3075  C  CG1 . ILE A  1 407 ? 61.881  49.550 36.607 1.00 17.82 ? 407  ILE A CG1 1 
ATOM   3076  C  CG2 . ILE A  1 407 ? 62.895  51.766 37.183 1.00 15.88 ? 407  ILE A CG2 1 
ATOM   3077  C  CD1 . ILE A  1 407 ? 62.097  49.439 35.100 1.00 16.89 ? 407  ILE A CD1 1 
ATOM   3078  N  N   . GLU A  1 408 ? 61.549  52.580 40.174 1.00 19.05 ? 408  GLU A N   1 
ATOM   3079  C  CA  . GLU A  1 408 ? 61.399  53.866 40.857 1.00 19.43 ? 408  GLU A CA  1 
ATOM   3080  C  C   . GLU A  1 408 ? 62.457  54.944 40.596 1.00 19.67 ? 408  GLU A C   1 
ATOM   3081  O  O   . GLU A  1 408 ? 62.143  56.130 40.609 1.00 18.69 ? 408  GLU A O   1 
ATOM   3082  C  CB  . GLU A  1 408 ? 61.297  53.600 42.364 1.00 20.41 ? 408  GLU A CB  1 
ATOM   3083  C  CG  . GLU A  1 408 ? 60.191  52.626 42.737 1.00 22.91 ? 408  GLU A CG  1 
ATOM   3084  C  CD  . GLU A  1 408 ? 58.817  53.129 42.328 1.00 26.06 ? 408  GLU A CD  1 
ATOM   3085  O  OE1 . GLU A  1 408 ? 58.086  52.388 41.631 1.00 29.03 ? 408  GLU A OE1 1 
ATOM   3086  O  OE2 . GLU A  1 408 ? 58.470  54.273 42.689 1.00 27.66 ? 408  GLU A OE2 1 
ATOM   3087  N  N   . ALA A  1 409 ? 63.710  54.540 40.396 1.00 19.34 ? 409  ALA A N   1 
ATOM   3088  C  CA  . ALA A  1 409 ? 64.782  55.488 40.135 1.00 18.48 ? 409  ALA A CA  1 
ATOM   3089  C  C   . ALA A  1 409 ? 65.933  54.770 39.453 1.00 19.23 ? 409  ALA A C   1 
ATOM   3090  O  O   . ALA A  1 409 ? 66.110  53.557 39.619 1.00 19.17 ? 409  ALA A O   1 
ATOM   3091  C  CB  . ALA A  1 409 ? 65.269  56.118 41.440 1.00 18.42 ? 409  ALA A CB  1 
ATOM   3092  N  N   . LEU A  1 410 ? 66.731  55.535 38.719 1.00 18.63 ? 410  LEU A N   1 
ATOM   3093  C  CA  . LEU A  1 410 ? 67.862  54.993 37.996 1.00 19.58 ? 410  LEU A CA  1 
ATOM   3094  C  C   . LEU A  1 410 ? 69.084  55.917 38.051 1.00 20.67 ? 410  LEU A C   1 
ATOM   3095  O  O   . LEU A  1 410 ? 68.981  57.107 37.750 1.00 20.57 ? 410  LEU A O   1 
ATOM   3096  C  CB  . LEU A  1 410 ? 67.472  54.762 36.521 1.00 18.32 ? 410  LEU A CB  1 
ATOM   3097  C  CG  . LEU A  1 410 ? 68.562  54.179 35.593 1.00 18.45 ? 410  LEU A CG  1 
ATOM   3098  C  CD1 . LEU A  1 410 ? 69.022  52.817 36.156 1.00 14.48 ? 410  LEU A CD1 1 
ATOM   3099  C  CD2 . LEU A  1 410 ? 68.033  54.027 34.154 1.00 15.83 ? 410  LEU A CD2 1 
ATOM   3100  N  N   . THR A  1 411 ? 70.223  55.360 38.455 1.00 21.10 ? 411  THR A N   1 
ATOM   3101  C  CA  . THR A  1 411 ? 71.500  56.079 38.480 1.00 22.31 ? 411  THR A CA  1 
ATOM   3102  C  C   . THR A  1 411 ? 72.466  55.205 37.667 1.00 23.15 ? 411  THR A C   1 
ATOM   3103  O  O   . THR A  1 411 ? 72.120  54.089 37.281 1.00 23.25 ? 411  THR A O   1 
ATOM   3104  C  CB  . THR A  1 411 ? 72.100  56.221 39.902 1.00 22.49 ? 411  THR A CB  1 
ATOM   3105  O  OG1 . THR A  1 411 ? 72.500  54.928 40.383 1.00 23.13 ? 411  THR A OG1 1 
ATOM   3106  C  CG2 . THR A  1 411 ? 71.102  56.868 40.852 1.00 20.44 ? 411  THR A CG2 1 
ATOM   3107  N  N   . SER A  1 412 ? 73.671  55.701 37.402 1.00 24.36 ? 412  SER A N   1 
ATOM   3108  C  CA  . SER A  1 412 ? 74.632  54.910 36.632 1.00 24.94 ? 412  SER A CA  1 
ATOM   3109  C  C   . SER A  1 412 ? 75.061  53.642 37.372 1.00 23.43 ? 412  SER A C   1 
ATOM   3110  O  O   . SER A  1 412 ? 75.478  52.676 36.741 1.00 23.96 ? 412  SER A O   1 
ATOM   3111  C  CB  . SER A  1 412 ? 75.875  55.743 36.296 1.00 26.13 ? 412  SER A CB  1 
ATOM   3112  O  OG  . SER A  1 412 ? 76.645  56.007 37.454 1.00 27.32 ? 412  SER A OG  1 
ATOM   3113  N  N   . ASP A  1 413 ? 74.957  53.634 38.697 1.00 22.70 ? 413  ASP A N   1 
ATOM   3114  C  CA  . ASP A  1 413 ? 75.360  52.453 39.468 1.00 23.54 ? 413  ASP A CA  1 
ATOM   3115  C  C   . ASP A  1 413 ? 74.223  51.514 39.898 1.00 22.91 ? 413  ASP A C   1 
ATOM   3116  O  O   . ASP A  1 413 ? 74.413  50.289 39.997 1.00 22.14 ? 413  ASP A O   1 
ATOM   3117  C  CB  . ASP A  1 413 ? 76.135  52.871 40.727 1.00 25.83 ? 413  ASP A CB  1 
ATOM   3118  C  CG  . ASP A  1 413 ? 77.512  53.463 40.412 1.00 28.45 ? 413  ASP A CG  1 
ATOM   3119  O  OD1 . ASP A  1 413 ? 78.252  52.880 39.580 1.00 30.19 ? 413  ASP A OD1 1 
ATOM   3120  O  OD2 . ASP A  1 413 ? 77.857  54.503 41.018 1.00 29.36 ? 413  ASP A OD2 1 
ATOM   3121  N  N   . TYR A  1 414 ? 73.047  52.084 40.156 1.00 20.98 ? 414  TYR A N   1 
ATOM   3122  C  CA  . TYR A  1 414 ? 71.909  51.286 40.615 1.00 20.45 ? 414  TYR A CA  1 
ATOM   3123  C  C   . TYR A  1 414 ? 70.559  51.587 39.974 1.00 19.99 ? 414  TYR A C   1 
ATOM   3124  O  O   . TYR A  1 414 ? 70.313  52.677 39.475 1.00 19.30 ? 414  TYR A O   1 
ATOM   3125  C  CB  . TYR A  1 414 ? 71.708  51.464 42.128 1.00 19.16 ? 414  TYR A CB  1 
ATOM   3126  C  CG  . TYR A  1 414 ? 72.811  50.927 43.010 1.00 18.93 ? 414  TYR A CG  1 
ATOM   3127  C  CD1 . TYR A  1 414 ? 73.808  51.770 43.510 1.00 19.56 ? 414  TYR A CD1 1 
ATOM   3128  C  CD2 . TYR A  1 414 ? 72.852  49.580 43.348 1.00 18.36 ? 414  TYR A CD2 1 
ATOM   3129  C  CE1 . TYR A  1 414 ? 74.820  51.271 44.329 1.00 20.86 ? 414  TYR A CE1 1 
ATOM   3130  C  CE2 . TYR A  1 414 ? 73.852  49.073 44.159 1.00 20.74 ? 414  TYR A CE2 1 
ATOM   3131  C  CZ  . TYR A  1 414 ? 74.833  49.933 44.648 1.00 21.51 ? 414  TYR A CZ  1 
ATOM   3132  O  OH  . TYR A  1 414 ? 75.806  49.443 45.474 1.00 24.04 ? 414  TYR A OH  1 
ATOM   3133  N  N   . LEU A  1 415 ? 69.686  50.593 40.011 1.00 19.43 ? 415  LEU A N   1 
ATOM   3134  C  CA  . LEU A  1 415 ? 68.326  50.760 39.555 1.00 19.07 ? 415  LEU A CA  1 
ATOM   3135  C  C   . LEU A  1 415 ? 67.503  50.390 40.806 1.00 19.73 ? 415  LEU A C   1 
ATOM   3136  O  O   . LEU A  1 415 ? 67.683  49.321 41.394 1.00 18.95 ? 415  LEU A O   1 
ATOM   3137  C  CB  . LEU A  1 415 ? 67.991  49.827 38.394 1.00 19.02 ? 415  LEU A CB  1 
ATOM   3138  C  CG  . LEU A  1 415 ? 66.527  49.957 37.913 1.00 19.57 ? 415  LEU A CG  1 
ATOM   3139  C  CD1 . LEU A  1 415 ? 66.383  49.427 36.481 1.00 18.99 ? 415  LEU A CD1 1 
ATOM   3140  C  CD2 . LEU A  1 415 ? 65.599  49.199 38.890 1.00 18.00 ? 415  LEU A CD2 1 
ATOM   3141  N  N   . TYR A  1 416 ? 66.622  51.293 41.221 1.00 20.30 ? 416  TYR A N   1 
ATOM   3142  C  CA  . TYR A  1 416 ? 65.786  51.078 42.396 1.00 18.64 ? 416  TYR A CA  1 
ATOM   3143  C  C   . TYR A  1 416 ? 64.394  50.650 41.973 1.00 19.04 ? 416  TYR A C   1 
ATOM   3144  O  O   . TYR A  1 416 ? 63.824  51.205 41.022 1.00 19.65 ? 416  TYR A O   1 
ATOM   3145  C  CB  . TYR A  1 416 ? 65.685  52.363 43.209 1.00 17.95 ? 416  TYR A CB  1 
ATOM   3146  C  CG  . TYR A  1 416 ? 67.001  52.845 43.757 1.00 19.15 ? 416  TYR A CG  1 
ATOM   3147  C  CD1 . TYR A  1 416 ? 67.902  53.539 42.950 1.00 19.05 ? 416  TYR A CD1 1 
ATOM   3148  C  CD2 . TYR A  1 416 ? 67.354  52.598 45.090 1.00 20.24 ? 416  TYR A CD2 1 
ATOM   3149  C  CE1 . TYR A  1 416 ? 69.124  53.987 43.449 1.00 19.90 ? 416  TYR A CE1 1 
ATOM   3150  C  CE2 . TYR A  1 416 ? 68.580  53.034 45.607 1.00 19.84 ? 416  TYR A CE2 1 
ATOM   3151  C  CZ  . TYR A  1 416 ? 69.451  53.725 44.780 1.00 19.48 ? 416  TYR A CZ  1 
ATOM   3152  O  OH  . TYR A  1 416 ? 70.643  54.154 45.271 1.00 19.83 ? 416  TYR A OH  1 
ATOM   3153  N  N   . TYR A  1 417 ? 63.830  49.675 42.678 1.00 18.22 ? 417  TYR A N   1 
ATOM   3154  C  CA  . TYR A  1 417 ? 62.500  49.196 42.326 1.00 18.25 ? 417  TYR A CA  1 
ATOM   3155  C  C   . TYR A  1 417 ? 61.749  48.602 43.507 1.00 17.10 ? 417  TYR A C   1 
ATOM   3156  O  O   . TYR A  1 417 ? 62.326  48.300 44.538 1.00 17.37 ? 417  TYR A O   1 
ATOM   3157  C  CB  . TYR A  1 417 ? 62.610  48.153 41.205 1.00 17.01 ? 417  TYR A CB  1 
ATOM   3158  C  CG  . TYR A  1 417 ? 63.236  46.841 41.631 1.00 18.71 ? 417  TYR A CG  1 
ATOM   3159  C  CD1 . TYR A  1 417 ? 62.461  45.808 42.176 1.00 17.86 ? 417  TYR A CD1 1 
ATOM   3160  C  CD2 . TYR A  1 417 ? 64.616  46.638 41.524 1.00 19.25 ? 417  TYR A CD2 1 
ATOM   3161  C  CE1 . TYR A  1 417 ? 63.052  44.597 42.609 1.00 17.12 ? 417  TYR A CE1 1 
ATOM   3162  C  CE2 . TYR A  1 417 ? 65.212  45.432 41.953 1.00 19.27 ? 417  TYR A CE2 1 
ATOM   3163  C  CZ  . TYR A  1 417 ? 64.421  44.420 42.495 1.00 19.27 ? 417  TYR A CZ  1 
ATOM   3164  O  OH  . TYR A  1 417 ? 65.012  43.250 42.923 1.00 18.79 ? 417  TYR A OH  1 
ATOM   3165  N  N   . ILE A  1 418 ? 60.444  48.458 43.339 1.00 17.17 ? 418  ILE A N   1 
ATOM   3166  C  CA  . ILE A  1 418 ? 59.588  47.874 44.353 1.00 16.27 ? 418  ILE A CA  1 
ATOM   3167  C  C   . ILE A  1 418 ? 59.092  46.511 43.840 1.00 17.04 ? 418  ILE A C   1 
ATOM   3168  O  O   . ILE A  1 418 ? 58.710  46.356 42.667 1.00 16.58 ? 418  ILE A O   1 
ATOM   3169  C  CB  . ILE A  1 418 ? 58.401  48.810 44.664 1.00 17.67 ? 418  ILE A CB  1 
ATOM   3170  C  CG1 . ILE A  1 418 ? 58.871  49.923 45.613 1.00 17.63 ? 418  ILE A CG1 1 
ATOM   3171  C  CG2 . ILE A  1 418 ? 57.246  48.017 45.315 1.00 17.15 ? 418  ILE A CG2 1 
ATOM   3172  C  CD1 . ILE A  1 418 ? 57.934  51.047 45.672 1.00 22.94 ? 418  ILE A CD1 1 
ATOM   3173  N  N   . SER A  1 419 ? 59.115  45.512 44.712 1.00 15.96 ? 419  SER A N   1 
ATOM   3174  C  CA  . SER A  1 419 ? 58.674  44.185 44.314 1.00 16.04 ? 419  SER A CA  1 
ATOM   3175  C  C   . SER A  1 419 ? 58.006  43.523 45.495 1.00 16.17 ? 419  SER A C   1 
ATOM   3176  O  O   . SER A  1 419 ? 58.075  44.037 46.623 1.00 14.53 ? 419  SER A O   1 
ATOM   3177  C  CB  . SER A  1 419 ? 59.868  43.336 43.874 1.00 15.84 ? 419  SER A CB  1 
ATOM   3178  O  OG  . SER A  1 419 ? 60.568  42.844 45.013 1.00 15.22 ? 419  SER A OG  1 
ATOM   3179  N  N   . ASN A  1 420 ? 57.343  42.395 45.239 1.00 15.61 ? 420  ASN A N   1 
ATOM   3180  C  CA  . ASN A  1 420 ? 56.696  41.651 46.320 1.00 17.22 ? 420  ASN A CA  1 
ATOM   3181  C  C   . ASN A  1 420 ? 57.507  40.392 46.588 1.00 18.01 ? 420  ASN A C   1 
ATOM   3182  O  O   . ASN A  1 420 ? 56.964  39.368 46.969 1.00 19.46 ? 420  ASN A O   1 
ATOM   3183  C  CB  . ASN A  1 420 ? 55.242  41.290 45.967 1.00 17.76 ? 420  ASN A CB  1 
ATOM   3184  C  CG  . ASN A  1 420 ? 55.113  40.597 44.617 1.00 19.18 ? 420  ASN A CG  1 
ATOM   3185  O  OD1 . ASN A  1 420 ? 56.100  40.122 44.046 1.00 20.11 ? 420  ASN A OD1 1 
ATOM   3186  N  ND2 . ASN A  1 420 ? 53.888  40.533 44.104 1.00 19.32 ? 420  ASN A ND2 1 
ATOM   3187  N  N   . GLU A  1 421 ? 58.821  40.467 46.392 1.00 18.38 ? 421  GLU A N   1 
ATOM   3188  C  CA  . GLU A  1 421 ? 59.669  39.310 46.622 1.00 19.61 ? 421  GLU A CA  1 
ATOM   3189  C  C   . GLU A  1 421 ? 59.791  38.854 48.083 1.00 20.37 ? 421  GLU A C   1 
ATOM   3190  O  O   . GLU A  1 421 ? 59.778  37.666 48.367 1.00 21.56 ? 421  GLU A O   1 
ATOM   3191  C  CB  . GLU A  1 421 ? 61.085  39.549 46.076 1.00 20.64 ? 421  GLU A CB  1 
ATOM   3192  C  CG  . GLU A  1 421 ? 62.105  38.548 46.628 1.00 22.61 ? 421  GLU A CG  1 
ATOM   3193  C  CD  . GLU A  1 421 ? 63.462  38.558 45.928 1.00 24.84 ? 421  GLU A CD  1 
ATOM   3194  O  OE1 . GLU A  1 421 ? 63.903  39.622 45.458 1.00 24.36 ? 421  GLU A OE1 1 
ATOM   3195  O  OE2 . GLU A  1 421 ? 64.104  37.487 45.872 1.00 26.83 ? 421  GLU A OE2 1 
ATOM   3196  N  N   . TYR A  1 422 ? 59.918  39.796 49.003 1.00 20.25 ? 422  TYR A N   1 
ATOM   3197  C  CA  . TYR A  1 422 ? 60.107  39.454 50.396 1.00 20.52 ? 422  TYR A CA  1 
ATOM   3198  C  C   . TYR A  1 422 ? 59.160  38.418 50.988 1.00 20.91 ? 422  TYR A C   1 
ATOM   3199  O  O   . TYR A  1 422 ? 57.938  38.560 50.932 1.00 20.74 ? 422  TYR A O   1 
ATOM   3200  C  CB  . TYR A  1 422 ? 60.071  40.724 51.239 1.00 21.67 ? 422  TYR A CB  1 
ATOM   3201  C  CG  . TYR A  1 422 ? 60.671  40.542 52.614 1.00 24.16 ? 422  TYR A CG  1 
ATOM   3202  C  CD1 . TYR A  1 422 ? 61.984  40.101 52.769 1.00 22.88 ? 422  TYR A CD1 1 
ATOM   3203  C  CD2 . TYR A  1 422 ? 59.936  40.854 53.762 1.00 25.27 ? 422  TYR A CD2 1 
ATOM   3204  C  CE1 . TYR A  1 422 ? 62.552  39.984 54.023 1.00 25.08 ? 422  TYR A CE1 1 
ATOM   3205  C  CE2 . TYR A  1 422 ? 60.496  40.743 55.017 1.00 25.87 ? 422  TYR A CE2 1 
ATOM   3206  C  CZ  . TYR A  1 422 ? 61.805  40.311 55.139 1.00 26.52 ? 422  TYR A CZ  1 
ATOM   3207  O  OH  . TYR A  1 422 ? 62.363  40.262 56.391 1.00 30.69 ? 422  TYR A OH  1 
ATOM   3208  N  N   . LYS A  1 423 ? 59.740  37.374 51.572 1.00 21.37 ? 423  LYS A N   1 
ATOM   3209  C  CA  . LYS A  1 423 ? 58.973  36.309 52.203 1.00 22.67 ? 423  LYS A CA  1 
ATOM   3210  C  C   . LYS A  1 423 ? 57.939  35.705 51.275 1.00 23.47 ? 423  LYS A C   1 
ATOM   3211  O  O   . LYS A  1 423 ? 56.987  35.080 51.728 1.00 22.92 ? 423  LYS A O   1 
ATOM   3212  C  CB  . LYS A  1 423 ? 58.288  36.829 53.472 1.00 22.31 ? 423  LYS A CB  1 
ATOM   3213  C  CG  . LYS A  1 423 ? 59.261  37.143 54.585 1.00 25.83 ? 423  LYS A CG  1 
ATOM   3214  C  CD  . LYS A  1 423 ? 58.604  37.852 55.769 1.00 28.16 ? 423  LYS A CD  1 
ATOM   3215  C  CE  . LYS A  1 423 ? 59.626  38.023 56.905 1.00 32.03 ? 423  LYS A CE  1 
ATOM   3216  N  NZ  . LYS A  1 423 ? 59.149  38.804 58.097 1.00 31.67 ? 423  LYS A NZ  1 
ATOM   3217  N  N   . GLY A  1 424 ? 58.122  35.896 49.971 1.00 24.43 ? 424  GLY A N   1 
ATOM   3218  C  CA  . GLY A  1 424 ? 57.175  35.337 49.017 1.00 24.30 ? 424  GLY A CA  1 
ATOM   3219  C  C   . GLY A  1 424 ? 55.732  35.790 49.230 1.00 23.94 ? 424  GLY A C   1 
ATOM   3220  O  O   . GLY A  1 424 ? 54.799  35.062 48.899 1.00 22.80 ? 424  GLY A O   1 
ATOM   3221  N  N   . MET A  1 425 ? 55.546  36.983 49.783 1.00 22.16 ? 425  MET A N   1 
ATOM   3222  C  CA  . MET A  1 425 ? 54.203  37.498 50.002 1.00 22.74 ? 425  MET A CA  1 
ATOM   3223  C  C   . MET A  1 425 ? 53.809  38.430 48.849 1.00 22.68 ? 425  MET A C   1 
ATOM   3224  O  O   . MET A  1 425 ? 54.272  39.573 48.769 1.00 21.43 ? 425  MET A O   1 
ATOM   3225  C  CB  . MET A  1 425 ? 54.133  38.242 51.339 1.00 23.83 ? 425  MET A CB  1 
ATOM   3226  C  CG  . MET A  1 425 ? 54.442  37.335 52.552 1.00 25.52 ? 425  MET A CG  1 
ATOM   3227  S  SD  . MET A  1 425 ? 54.315  38.183 54.136 1.00 29.50 ? 425  MET A SD  1 
ATOM   3228  C  CE  . MET A  1 425 ? 52.593  38.724 54.073 1.00 28.30 ? 425  MET A CE  1 
ATOM   3229  N  N   . PRO A  1 426 ? 52.934  37.951 47.945 1.00 21.93 ? 426  PRO A N   1 
ATOM   3230  C  CA  . PRO A  1 426 ? 52.502  38.768 46.803 1.00 21.53 ? 426  PRO A CA  1 
ATOM   3231  C  C   . PRO A  1 426 ? 51.799  40.075 47.203 1.00 21.83 ? 426  PRO A C   1 
ATOM   3232  O  O   . PRO A  1 426 ? 51.758  41.039 46.413 1.00 19.79 ? 426  PRO A O   1 
ATOM   3233  C  CB  . PRO A  1 426 ? 51.610  37.817 46.009 1.00 21.40 ? 426  PRO A CB  1 
ATOM   3234  C  CG  . PRO A  1 426 ? 51.021  36.931 47.063 1.00 23.48 ? 426  PRO A CG  1 
ATOM   3235  C  CD  . PRO A  1 426 ? 52.185  36.680 48.016 1.00 22.22 ? 426  PRO A CD  1 
ATOM   3236  N  N   . GLY A  1 427 ? 51.277  40.099 48.433 1.00 20.98 ? 427  GLY A N   1 
ATOM   3237  C  CA  . GLY A  1 427 ? 50.591  41.279 48.943 1.00 20.32 ? 427  GLY A CA  1 
ATOM   3238  C  C   . GLY A  1 427 ? 51.474  42.219 49.759 1.00 19.75 ? 427  GLY A C   1 
ATOM   3239  O  O   . GLY A  1 427 ? 50.969  43.135 50.408 1.00 19.62 ? 427  GLY A O   1 
ATOM   3240  N  N   . GLY A  1 428 ? 52.788  41.984 49.739 1.00 19.97 ? 428  GLY A N   1 
ATOM   3241  C  CA  . GLY A  1 428 ? 53.742  42.835 50.446 1.00 19.43 ? 428  GLY A CA  1 
ATOM   3242  C  C   . GLY A  1 428 ? 54.541  43.606 49.404 1.00 20.43 ? 428  GLY A C   1 
ATOM   3243  O  O   . GLY A  1 428 ? 54.634  43.165 48.252 1.00 20.75 ? 428  GLY A O   1 
ATOM   3244  N  N   . ARG A  1 429 ? 55.104  44.748 49.780 1.00 18.77 ? 429  ARG A N   1 
ATOM   3245  C  CA  . ARG A  1 429 ? 55.864  45.574 48.829 1.00 18.83 ? 429  ARG A CA  1 
ATOM   3246  C  C   . ARG A  1 429 ? 57.110  46.137 49.513 1.00 17.65 ? 429  ARG A C   1 
ATOM   3247  O  O   . ARG A  1 429 ? 57.023  46.714 50.591 1.00 18.21 ? 429  ARG A O   1 
ATOM   3248  C  CB  . ARG A  1 429 ? 55.035  46.783 48.334 1.00 17.93 ? 429  ARG A CB  1 
ATOM   3249  C  CG  . ARG A  1 429 ? 53.680  46.511 47.659 1.00 19.39 ? 429  ARG A CG  1 
ATOM   3250  C  CD  . ARG A  1 429 ? 53.792  46.279 46.152 1.00 20.32 ? 429  ARG A CD  1 
ATOM   3251  N  NE  . ARG A  1 429 ? 52.488  46.180 45.493 1.00 21.23 ? 429  ARG A NE  1 
ATOM   3252  C  CZ  . ARG A  1 429 ? 51.717  45.092 45.499 1.00 24.35 ? 429  ARG A CZ  1 
ATOM   3253  N  NH1 . ARG A  1 429 ? 52.094  43.986 46.131 1.00 20.51 ? 429  ARG A NH1 1 
ATOM   3254  N  NH2 . ARG A  1 429 ? 50.559  45.107 44.847 1.00 26.20 ? 429  ARG A NH2 1 
ATOM   3255  N  N   . ASN A  1 430 ? 58.262  45.988 48.878 1.00 18.13 ? 430  ASN A N   1 
ATOM   3256  C  CA  . ASN A  1 430 ? 59.484  46.517 49.444 1.00 17.62 ? 430  ASN A CA  1 
ATOM   3257  C  C   . ASN A  1 430 ? 60.338  47.164 48.384 1.00 17.95 ? 430  ASN A C   1 
ATOM   3258  O  O   . ASN A  1 430 ? 60.158  46.897 47.190 1.00 16.81 ? 430  ASN A O   1 
ATOM   3259  C  CB  . ASN A  1 430 ? 60.259  45.410 50.162 1.00 18.37 ? 430  ASN A CB  1 
ATOM   3260  C  CG  . ASN A  1 430 ? 59.709  45.140 51.542 1.00 19.05 ? 430  ASN A CG  1 
ATOM   3261  O  OD1 . ASN A  1 430 ? 59.916  45.929 52.464 1.00 20.82 ? 430  ASN A OD1 1 
ATOM   3262  N  ND2 . ASN A  1 430 ? 58.975  44.038 51.688 1.00 17.79 ? 430  ASN A ND2 1 
ATOM   3263  N  N   . LEU A  1 431 ? 61.241  48.039 48.832 1.00 17.49 ? 431  LEU A N   1 
ATOM   3264  C  CA  . LEU A  1 431 ? 62.152  48.752 47.948 1.00 16.95 ? 431  LEU A CA  1 
ATOM   3265  C  C   . LEU A  1 431 ? 63.484  48.021 47.898 1.00 18.26 ? 431  LEU A C   1 
ATOM   3266  O  O   . LEU A  1 431 ? 64.050  47.691 48.954 1.00 17.51 ? 431  LEU A O   1 
ATOM   3267  C  CB  . LEU A  1 431 ? 62.399  50.173 48.457 1.00 16.91 ? 431  LEU A CB  1 
ATOM   3268  C  CG  . LEU A  1 431 ? 63.433  50.959 47.619 1.00 17.01 ? 431  LEU A CG  1 
ATOM   3269  C  CD1 . LEU A  1 431 ? 62.812  51.365 46.281 1.00 14.03 ? 431  LEU A CD1 1 
ATOM   3270  C  CD2 . LEU A  1 431 ? 63.888  52.187 48.379 1.00 15.17 ? 431  LEU A CD2 1 
ATOM   3271  N  N   . TYR A  1 432 ? 63.969  47.784 46.673 1.00 16.67 ? 432  TYR A N   1 
ATOM   3272  C  CA  . TYR A  1 432 ? 65.239  47.116 46.417 1.00 17.11 ? 432  TYR A CA  1 
ATOM   3273  C  C   . TYR A  1 432 ? 66.077  47.940 45.446 1.00 17.97 ? 432  TYR A C   1 
ATOM   3274  O  O   . TYR A  1 432 ? 65.553  48.761 44.695 1.00 18.49 ? 432  TYR A O   1 
ATOM   3275  C  CB  . TYR A  1 432 ? 65.049  45.735 45.752 1.00 16.18 ? 432  TYR A CB  1 
ATOM   3276  C  CG  . TYR A  1 432 ? 64.295  44.711 46.558 1.00 17.07 ? 432  TYR A CG  1 
ATOM   3277  C  CD1 . TYR A  1 432 ? 62.906  44.759 46.667 1.00 16.83 ? 432  TYR A CD1 1 
ATOM   3278  C  CD2 . TYR A  1 432 ? 64.973  43.681 47.214 1.00 17.57 ? 432  TYR A CD2 1 
ATOM   3279  C  CE1 . TYR A  1 432 ? 62.210  43.800 47.412 1.00 18.50 ? 432  TYR A CE1 1 
ATOM   3280  C  CE2 . TYR A  1 432 ? 64.293  42.723 47.954 1.00 18.30 ? 432  TYR A CE2 1 
ATOM   3281  C  CZ  . TYR A  1 432 ? 62.899  42.788 48.050 1.00 19.08 ? 432  TYR A CZ  1 
ATOM   3282  O  OH  . TYR A  1 432 ? 62.217  41.835 48.781 1.00 19.38 ? 432  TYR A OH  1 
ATOM   3283  N  N   . LYS A  1 433 ? 67.384  47.706 45.451 1.00 18.78 ? 433  LYS A N   1 
ATOM   3284  C  CA  . LYS A  1 433 ? 68.272  48.362 44.497 1.00 18.48 ? 433  LYS A CA  1 
ATOM   3285  C  C   . LYS A  1 433 ? 69.115  47.223 43.941 1.00 19.65 ? 433  LYS A C   1 
ATOM   3286  O  O   . LYS A  1 433 ? 69.442  46.274 44.656 1.00 19.64 ? 433  LYS A O   1 
ATOM   3287  C  CB  . LYS A  1 433 ? 69.150  49.437 45.164 1.00 18.79 ? 433  LYS A CB  1 
ATOM   3288  C  CG  . LYS A  1 433 ? 70.210  48.953 46.146 1.00 18.24 ? 433  LYS A CG  1 
ATOM   3289  C  CD  . LYS A  1 433 ? 71.013  50.144 46.665 1.00 20.45 ? 433  LYS A CD  1 
ATOM   3290  C  CE  . LYS A  1 433 ? 72.283  49.702 47.409 1.00 19.59 ? 433  LYS A CE  1 
ATOM   3291  N  NZ  . LYS A  1 433 ? 72.985  50.855 48.017 1.00 18.85 ? 433  LYS A NZ  1 
ATOM   3292  N  N   . ILE A  1 434 ? 69.434  47.287 42.656 1.00 19.75 ? 434  ILE A N   1 
ATOM   3293  C  CA  . ILE A  1 434 ? 70.230  46.241 42.043 1.00 19.37 ? 434  ILE A CA  1 
ATOM   3294  C  C   . ILE A  1 434 ? 71.421  46.925 41.373 1.00 19.75 ? 434  ILE A C   1 
ATOM   3295  O  O   . ILE A  1 434 ? 71.265  47.931 40.678 1.00 19.96 ? 434  ILE A O   1 
ATOM   3296  C  CB  . ILE A  1 434 ? 69.385  45.384 41.005 1.00 19.15 ? 434  ILE A CB  1 
ATOM   3297  C  CG1 . ILE A  1 434 ? 70.251  44.262 40.418 1.00 20.00 ? 434  ILE A CG1 1 
ATOM   3298  C  CG2 . ILE A  1 434 ? 68.839  46.257 39.881 1.00 17.23 ? 434  ILE A CG2 1 
ATOM   3299  C  CD1 . ILE A  1 434 ? 69.524  43.290 39.476 1.00 16.73 ? 434  ILE A CD1 1 
ATOM   3300  N  N   . GLN A  1 435 ? 72.604  46.385 41.629 1.00 19.38 ? 435  GLN A N   1 
ATOM   3301  C  CA  . GLN A  1 435 ? 73.858  46.903 41.095 1.00 20.12 ? 435  GLN A CA  1 
ATOM   3302  C  C   . GLN A  1 435 ? 73.895  46.655 39.599 1.00 19.63 ? 435  GLN A C   1 
ATOM   3303  O  O   . GLN A  1 435 ? 73.892  45.506 39.165 1.00 19.81 ? 435  GLN A O   1 
ATOM   3304  C  CB  . GLN A  1 435 ? 75.031  46.177 41.759 1.00 21.61 ? 435  GLN A CB  1 
ATOM   3305  C  CG  . GLN A  1 435 ? 76.359  46.922 41.764 1.00 24.91 ? 435  GLN A CG  1 
ATOM   3306  C  CD  . GLN A  1 435 ? 77.459  46.105 42.440 1.00 28.04 ? 435  GLN A CD  1 
ATOM   3307  O  OE1 . GLN A  1 435 ? 78.292  45.488 41.774 1.00 32.19 ? 435  GLN A OE1 1 
ATOM   3308  N  NE2 . GLN A  1 435 ? 77.447  46.077 43.763 1.00 27.10 ? 435  GLN A NE2 1 
ATOM   3309  N  N   . LEU A  1 436 ? 73.927  47.715 38.804 1.00 20.25 ? 436  LEU A N   1 
ATOM   3310  C  CA  . LEU A  1 436 ? 73.946  47.525 37.364 1.00 23.40 ? 436  LEU A CA  1 
ATOM   3311  C  C   . LEU A  1 436 ? 75.177  46.761 36.858 1.00 24.76 ? 436  LEU A C   1 
ATOM   3312  O  O   . LEU A  1 436 ? 75.086  46.046 35.860 1.00 26.52 ? 436  LEU A O   1 
ATOM   3313  C  CB  . LEU A  1 436 ? 73.777  48.876 36.661 1.00 21.41 ? 436  LEU A CB  1 
ATOM   3314  C  CG  . LEU A  1 436 ? 72.435  49.506 37.104 1.00 21.47 ? 436  LEU A CG  1 
ATOM   3315  C  CD1 . LEU A  1 436 ? 72.248  50.870 36.470 1.00 20.64 ? 436  LEU A CD1 1 
ATOM   3316  C  CD2 . LEU A  1 436 ? 71.271  48.562 36.735 1.00 18.83 ? 436  LEU A CD2 1 
ATOM   3317  N  N   . SER A  1 437 ? 76.308  46.864 37.551 1.00 25.44 ? 437  SER A N   1 
ATOM   3318  C  CA  . SER A  1 437 ? 77.506  46.141 37.112 1.00 27.29 ? 437  SER A CA  1 
ATOM   3319  C  C   . SER A  1 437 ? 77.527  44.658 37.535 1.00 28.21 ? 437  SER A C   1 
ATOM   3320  O  O   . SER A  1 437 ? 78.352  43.885 37.042 1.00 28.72 ? 437  SER A O   1 
ATOM   3321  C  CB  . SER A  1 437 ? 78.765  46.824 37.642 1.00 26.86 ? 437  SER A CB  1 
ATOM   3322  O  OG  . SER A  1 437 ? 78.852  46.677 39.048 1.00 29.47 ? 437  SER A OG  1 
ATOM   3323  N  N   . ASP A  1 438 ? 76.634  44.258 38.438 1.00 28.17 ? 438  ASP A N   1 
ATOM   3324  C  CA  . ASP A  1 438 ? 76.591  42.861 38.889 1.00 28.67 ? 438  ASP A CA  1 
ATOM   3325  C  C   . ASP A  1 438 ? 75.196  42.537 39.433 1.00 28.06 ? 438  ASP A C   1 
ATOM   3326  O  O   . ASP A  1 438 ? 74.900  42.764 40.612 1.00 27.90 ? 438  ASP A O   1 
ATOM   3327  C  CB  . ASP A  1 438 ? 77.672  42.622 39.957 1.00 28.33 ? 438  ASP A CB  1 
ATOM   3328  C  CG  . ASP A  1 438 ? 77.697  41.184 40.473 1.00 29.35 ? 438  ASP A CG  1 
ATOM   3329  O  OD1 . ASP A  1 438 ? 76.844  40.370 40.060 1.00 31.01 ? 438  ASP A OD1 1 
ATOM   3330  O  OD2 . ASP A  1 438 ? 78.580  40.869 41.303 1.00 30.35 ? 438  ASP A OD2 1 
ATOM   3331  N  N   . TYR A  1 439 ? 74.356  41.990 38.555 1.00 28.07 ? 439  TYR A N   1 
ATOM   3332  C  CA  . TYR A  1 439 ? 72.978  41.663 38.882 1.00 27.81 ? 439  TYR A CA  1 
ATOM   3333  C  C   . TYR A  1 439 ? 72.806  40.674 40.018 1.00 28.32 ? 439  TYR A C   1 
ATOM   3334  O  O   . TYR A  1 439 ? 71.684  40.497 40.489 1.00 29.08 ? 439  TYR A O   1 
ATOM   3335  C  CB  . TYR A  1 439 ? 72.222  41.142 37.650 1.00 26.39 ? 439  TYR A CB  1 
ATOM   3336  C  CG  . TYR A  1 439 ? 72.275  42.038 36.421 1.00 26.27 ? 439  TYR A CG  1 
ATOM   3337  C  CD1 . TYR A  1 439 ? 72.343  43.429 36.539 1.00 24.15 ? 439  TYR A CD1 1 
ATOM   3338  C  CD2 . TYR A  1 439 ? 72.244  41.484 35.135 1.00 24.55 ? 439  TYR A CD2 1 
ATOM   3339  C  CE1 . TYR A  1 439 ? 72.378  44.254 35.400 1.00 25.72 ? 439  TYR A CE1 1 
ATOM   3340  C  CE2 . TYR A  1 439 ? 72.283  42.298 33.992 1.00 25.43 ? 439  TYR A CE2 1 
ATOM   3341  C  CZ  . TYR A  1 439 ? 72.351  43.679 34.127 1.00 25.97 ? 439  TYR A CZ  1 
ATOM   3342  O  OH  . TYR A  1 439 ? 72.416  44.468 32.992 1.00 24.93 ? 439  TYR A OH  1 
ATOM   3343  N  N   . THR A  1 440 ? 73.873  40.006 40.454 1.00 28.38 ? 440  THR A N   1 
ATOM   3344  C  CA  . THR A  1 440 ? 73.711  39.073 41.570 1.00 29.13 ? 440  THR A CA  1 
ATOM   3345  C  C   . THR A  1 440 ? 73.677  39.865 42.878 1.00 28.16 ? 440  THR A C   1 
ATOM   3346  O  O   . THR A  1 440 ? 73.347  39.320 43.924 1.00 28.11 ? 440  THR A O   1 
ATOM   3347  C  CB  . THR A  1 440 ? 74.867  38.066 41.686 1.00 30.19 ? 440  THR A CB  1 
ATOM   3348  O  OG1 . THR A  1 440 ? 76.051  38.766 42.075 1.00 33.06 ? 440  THR A OG1 1 
ATOM   3349  C  CG2 . THR A  1 440 ? 75.102  37.350 40.360 1.00 30.89 ? 440  THR A CG2 1 
ATOM   3350  N  N   . LYS A  1 441 ? 74.023  41.146 42.813 1.00 27.46 ? 441  LYS A N   1 
ATOM   3351  C  CA  . LYS A  1 441 ? 74.022  42.006 44.003 1.00 27.80 ? 441  LYS A CA  1 
ATOM   3352  C  C   . LYS A  1 441 ? 72.726  42.826 44.149 1.00 26.55 ? 441  LYS A C   1 
ATOM   3353  O  O   . LYS A  1 441 ? 72.645  43.966 43.675 1.00 24.69 ? 441  LYS A O   1 
ATOM   3354  C  CB  . LYS A  1 441 ? 75.201  42.980 43.958 1.00 29.94 ? 441  LYS A CB  1 
ATOM   3355  C  CG  . LYS A  1 441 ? 76.578  42.339 43.857 1.00 33.53 ? 441  LYS A CG  1 
ATOM   3356  C  CD  . LYS A  1 441 ? 77.097  41.913 45.213 1.00 36.22 ? 441  LYS A CD  1 
ATOM   3357  C  CE  . LYS A  1 441 ? 78.587  41.583 45.149 1.00 38.60 ? 441  LYS A CE  1 
ATOM   3358  N  NZ  . LYS A  1 441 ? 78.840  40.291 44.454 1.00 40.61 ? 441  LYS A NZ  1 
ATOM   3359  N  N   . VAL A  1 442 ? 71.727  42.240 44.807 1.00 24.89 ? 442  VAL A N   1 
ATOM   3360  C  CA  . VAL A  1 442 ? 70.439  42.892 45.046 1.00 23.82 ? 442  VAL A CA  1 
ATOM   3361  C  C   . VAL A  1 442 ? 70.300  43.152 46.559 1.00 24.30 ? 442  VAL A C   1 
ATOM   3362  O  O   . VAL A  1 442 ? 70.456  42.238 47.370 1.00 24.60 ? 442  VAL A O   1 
ATOM   3363  C  CB  . VAL A  1 442 ? 69.277  41.986 44.567 1.00 23.84 ? 442  VAL A CB  1 
ATOM   3364  C  CG1 . VAL A  1 442 ? 67.925  42.592 44.975 1.00 22.43 ? 442  VAL A CG1 1 
ATOM   3365  C  CG2 . VAL A  1 442 ? 69.346  41.830 43.044 1.00 22.31 ? 442  VAL A CG2 1 
ATOM   3366  N  N   . THR A  1 443 ? 70.015  44.391 46.937 1.00 23.73 ? 443  THR A N   1 
ATOM   3367  C  CA  . THR A  1 443 ? 69.881  44.742 48.349 1.00 23.37 ? 443  THR A CA  1 
ATOM   3368  C  C   . THR A  1 443 ? 68.476  45.236 48.691 1.00 23.65 ? 443  THR A C   1 
ATOM   3369  O  O   . THR A  1 443 ? 67.990  46.184 48.061 1.00 24.25 ? 443  THR A O   1 
ATOM   3370  C  CB  . THR A  1 443 ? 70.859  45.890 48.745 1.00 24.10 ? 443  THR A CB  1 
ATOM   3371  O  OG1 . THR A  1 443 ? 72.181  45.589 48.277 1.00 24.86 ? 443  THR A OG1 1 
ATOM   3372  C  CG2 . THR A  1 443 ? 70.894  46.066 50.274 1.00 22.28 ? 443  THR A CG2 1 
ATOM   3373  N  N   . CYS A  1 444 ? 67.808  44.620 49.666 1.00 23.24 ? 444  CYS A N   1 
ATOM   3374  C  CA  . CYS A  1 444 ? 66.493  45.133 50.033 1.00 24.36 ? 444  CYS A CA  1 
ATOM   3375  C  C   . CYS A  1 444 ? 66.748  46.307 50.977 1.00 23.02 ? 444  CYS A C   1 
ATOM   3376  O  O   . CYS A  1 444 ? 67.508  46.188 51.936 1.00 24.84 ? 444  CYS A O   1 
ATOM   3377  C  CB  . CYS A  1 444 ? 65.612  44.085 50.722 1.00 25.54 ? 444  CYS A CB  1 
ATOM   3378  S  SG  . CYS A  1 444 ? 63.907  44.762 50.980 1.00 28.66 ? 444  CYS A SG  1 
ATOM   3379  N  N   . LEU A  1 445 ? 66.116  47.435 50.695 1.00 21.55 ? 445  LEU A N   1 
ATOM   3380  C  CA  . LEU A  1 445 ? 66.311  48.649 51.478 1.00 21.48 ? 445  LEU A CA  1 
ATOM   3381  C  C   . LEU A  1 445 ? 65.247  48.918 52.530 1.00 21.56 ? 445  LEU A C   1 
ATOM   3382  O  O   . LEU A  1 445 ? 65.455  49.736 53.411 1.00 20.80 ? 445  LEU A O   1 
ATOM   3383  C  CB  . LEU A  1 445 ? 66.392  49.859 50.530 1.00 21.00 ? 445  LEU A CB  1 
ATOM   3384  C  CG  . LEU A  1 445 ? 67.469  49.687 49.434 1.00 21.94 ? 445  LEU A CG  1 
ATOM   3385  C  CD1 . LEU A  1 445 ? 67.402  50.817 48.387 1.00 20.75 ? 445  LEU A CD1 1 
ATOM   3386  C  CD2 . LEU A  1 445 ? 68.841  49.633 50.120 1.00 20.81 ? 445  LEU A CD2 1 
ATOM   3387  N  N   . SER A  1 446 ? 64.111  48.230 52.451 1.00 21.44 ? 446  SER A N   1 
ATOM   3388  C  CA  . SER A  1 446 ? 63.047  48.479 53.410 1.00 22.22 ? 446  SER A CA  1 
ATOM   3389  C  C   . SER A  1 446 ? 62.588  47.248 54.190 1.00 22.48 ? 446  SER A C   1 
ATOM   3390  O  O   . SER A  1 446 ? 61.910  47.386 55.207 1.00 22.88 ? 446  SER A O   1 
ATOM   3391  C  CB  . SER A  1 446 ? 61.841  49.074 52.668 1.00 21.42 ? 446  SER A CB  1 
ATOM   3392  O  OG  . SER A  1 446 ? 61.339  48.136 51.714 1.00 20.26 ? 446  SER A OG  1 
ATOM   3393  N  N   . CYS A  1 447 ? 62.959  46.062 53.716 1.00 22.58 ? 447  CYS A N   1 
ATOM   3394  C  CA  . CYS A  1 447 ? 62.513  44.808 54.331 1.00 24.74 ? 447  CYS A CA  1 
ATOM   3395  C  C   . CYS A  1 447 ? 62.700  44.711 55.828 1.00 24.96 ? 447  CYS A C   1 
ATOM   3396  O  O   . CYS A  1 447 ? 61.786  44.342 56.548 1.00 25.35 ? 447  CYS A O   1 
ATOM   3397  C  CB  . CYS A  1 447 ? 63.222  43.600 53.700 1.00 26.08 ? 447  CYS A CB  1 
ATOM   3398  S  SG  . CYS A  1 447 ? 62.862  43.289 51.927 1.00 30.93 ? 447  CYS A SG  1 
ATOM   3399  N  N   . GLU A  1 448 ? 63.892  45.045 56.294 1.00 25.19 ? 448  GLU A N   1 
ATOM   3400  C  CA  . GLU A  1 448 ? 64.198  44.921 57.696 1.00 26.19 ? 448  GLU A CA  1 
ATOM   3401  C  C   . GLU A  1 448 ? 64.092  46.175 58.557 1.00 24.67 ? 448  GLU A C   1 
ATOM   3402  O  O   . GLU A  1 448 ? 64.455  46.133 59.730 1.00 24.58 ? 448  GLU A O   1 
ATOM   3403  C  CB  . GLU A  1 448 ? 65.595  44.314 57.831 1.00 28.84 ? 448  GLU A CB  1 
ATOM   3404  C  CG  . GLU A  1 448 ? 65.633  42.967 58.523 1.00 35.21 ? 448  GLU A CG  1 
ATOM   3405  C  CD  . GLU A  1 448 ? 64.745  41.941 57.867 1.00 38.95 ? 448  GLU A CD  1 
ATOM   3406  O  OE1 . GLU A  1 448 ? 64.945  41.659 56.661 1.00 40.62 ? 448  GLU A OE1 1 
ATOM   3407  O  OE2 . GLU A  1 448 ? 63.842  41.412 58.560 1.00 41.11 ? 448  GLU A OE2 1 
ATOM   3408  N  N   . LEU A  1 449 ? 63.604  47.283 58.009 1.00 22.56 ? 449  LEU A N   1 
ATOM   3409  C  CA  . LEU A  1 449 ? 63.493  48.508 58.814 1.00 22.61 ? 449  LEU A CA  1 
ATOM   3410  C  C   . LEU A  1 449 ? 62.596  48.300 60.036 1.00 22.69 ? 449  LEU A C   1 
ATOM   3411  O  O   . LEU A  1 449 ? 62.895  48.790 61.121 1.00 22.22 ? 449  LEU A O   1 
ATOM   3412  C  CB  . LEU A  1 449 ? 62.941  49.676 57.980 1.00 19.75 ? 449  LEU A CB  1 
ATOM   3413  C  CG  . LEU A  1 449 ? 63.811  50.163 56.819 1.00 21.14 ? 449  LEU A CG  1 
ATOM   3414  C  CD1 . LEU A  1 449 ? 63.051  51.211 56.028 1.00 20.33 ? 449  LEU A CD1 1 
ATOM   3415  C  CD2 . LEU A  1 449 ? 65.129  50.731 57.345 1.00 20.46 ? 449  LEU A CD2 1 
ATOM   3416  N  N   . ASN A  1 450 ? 61.492  47.583 59.848 1.00 22.54 ? 450  ASN A N   1 
ATOM   3417  C  CA  . ASN A  1 450 ? 60.551  47.310 60.935 1.00 22.95 ? 450  ASN A CA  1 
ATOM   3418  C  C   . ASN A  1 450 ? 59.556  46.315 60.357 1.00 23.07 ? 450  ASN A C   1 
ATOM   3419  O  O   . ASN A  1 450 ? 58.413  46.660 60.032 1.00 21.11 ? 450  ASN A O   1 
ATOM   3420  C  CB  . ASN A  1 450 ? 59.832  48.598 61.340 1.00 23.31 ? 450  ASN A CB  1 
ATOM   3421  C  CG  . ASN A  1 450 ? 59.037  48.441 62.619 1.00 23.32 ? 450  ASN A CG  1 
ATOM   3422  O  OD1 . ASN A  1 450 ? 58.580  47.336 62.956 1.00 24.84 ? 450  ASN A OD1 1 
ATOM   3423  N  ND2 . ASN A  1 450 ? 58.843  49.543 63.325 1.00 23.35 ? 450  ASN A ND2 1 
ATOM   3424  N  N   . PRO A  1 451 ? 59.990  45.057 60.223 1.00 23.93 ? 451  PRO A N   1 
ATOM   3425  C  CA  . PRO A  1 451 ? 59.193  43.962 59.671 1.00 24.31 ? 451  PRO A CA  1 
ATOM   3426  C  C   . PRO A  1 451 ? 57.825  43.699 60.285 1.00 25.33 ? 451  PRO A C   1 
ATOM   3427  O  O   . PRO A  1 451 ? 56.915  43.271 59.585 1.00 25.88 ? 451  PRO A O   1 
ATOM   3428  C  CB  . PRO A  1 451 ? 60.140  42.767 59.759 1.00 24.17 ? 451  PRO A CB  1 
ATOM   3429  C  CG  . PRO A  1 451 ? 60.957  43.075 60.943 1.00 25.08 ? 451  PRO A CG  1 
ATOM   3430  C  CD  . PRO A  1 451 ? 61.242  44.557 60.817 1.00 24.36 ? 451  PRO A CD  1 
ATOM   3431  N  N   . GLU A  1 452 ? 57.663  43.949 61.577 1.00 26.76 ? 452  GLU A N   1 
ATOM   3432  C  CA  . GLU A  1 452 ? 56.363  43.720 62.203 1.00 27.62 ? 452  GLU A CA  1 
ATOM   3433  C  C   . GLU A  1 452 ? 55.350  44.788 61.793 1.00 25.55 ? 452  GLU A C   1 
ATOM   3434  O  O   . GLU A  1 452 ? 54.195  44.497 61.530 1.00 25.88 ? 452  GLU A O   1 
ATOM   3435  C  CB  . GLU A  1 452 ? 56.515  43.711 63.718 1.00 30.56 ? 452  GLU A CB  1 
ATOM   3436  C  CG  . GLU A  1 452 ? 57.348  42.558 64.204 1.00 38.38 ? 452  GLU A CG  1 
ATOM   3437  C  CD  . GLU A  1 452 ? 57.569  42.593 65.703 1.00 43.18 ? 452  GLU A CD  1 
ATOM   3438  O  OE1 . GLU A  1 452 ? 56.602  42.931 66.440 1.00 44.68 ? 452  GLU A OE1 1 
ATOM   3439  O  OE2 . GLU A  1 452 ? 58.704  42.265 66.142 1.00 45.11 ? 452  GLU A OE2 1 
ATOM   3440  N  N   . ARG A  1 453 ? 55.802  46.029 61.737 1.00 23.18 ? 453  ARG A N   1 
ATOM   3441  C  CA  . ARG A  1 453 ? 54.929  47.118 61.382 1.00 21.86 ? 453  ARG A CA  1 
ATOM   3442  C  C   . ARG A  1 453 ? 54.873  47.448 59.903 1.00 20.55 ? 453  ARG A C   1 
ATOM   3443  O  O   . ARG A  1 453 ? 53.839  47.903 59.395 1.00 20.30 ? 453  ARG A O   1 
ATOM   3444  C  CB  . ARG A  1 453 ? 55.350  48.377 62.137 1.00 21.73 ? 453  ARG A CB  1 
ATOM   3445  C  CG  . ARG A  1 453 ? 54.489  49.594 61.825 1.00 18.84 ? 453  ARG A CG  1 
ATOM   3446  C  CD  . ARG A  1 453 ? 55.058  50.809 62.503 1.00 16.23 ? 453  ARG A CD  1 
ATOM   3447  N  NE  . ARG A  1 453 ? 54.266  52.000 62.239 1.00 14.90 ? 453  ARG A NE  1 
ATOM   3448  C  CZ  . ARG A  1 453 ? 54.420  53.136 62.905 1.00 15.03 ? 453  ARG A CZ  1 
ATOM   3449  N  NH1 . ARG A  1 453 ? 55.332  53.199 63.865 1.00 15.61 ? 453  ARG A NH1 1 
ATOM   3450  N  NH2 . ARG A  1 453 ? 53.685  54.202 62.615 1.00 13.13 ? 453  ARG A NH2 1 
ATOM   3451  N  N   . CYS A  1 454 ? 55.965  47.196 59.198 1.00 19.82 ? 454  CYS A N   1 
ATOM   3452  C  CA  . CYS A  1 454 ? 56.032  47.591 57.800 1.00 19.28 ? 454  CYS A CA  1 
ATOM   3453  C  C   . CYS A  1 454 ? 56.368  46.526 56.783 1.00 17.66 ? 454  CYS A C   1 
ATOM   3454  O  O   . CYS A  1 454 ? 57.493  46.035 56.723 1.00 16.47 ? 454  CYS A O   1 
ATOM   3455  C  CB  . CYS A  1 454 ? 57.038  48.730 57.693 1.00 19.55 ? 454  CYS A CB  1 
ATOM   3456  S  SG  . CYS A  1 454 ? 56.435  50.216 58.611 1.00 22.19 ? 454  CYS A SG  1 
ATOM   3457  N  N   . GLN A  1 455 ? 55.378  46.201 55.967 1.00 17.06 ? 455  GLN A N   1 
ATOM   3458  C  CA  . GLN A  1 455 ? 55.504  45.179 54.918 1.00 17.92 ? 455  GLN A CA  1 
ATOM   3459  C  C   . GLN A  1 455 ? 54.975  45.672 53.567 1.00 17.94 ? 455  GLN A C   1 
ATOM   3460  O  O   . GLN A  1 455 ? 54.946  44.914 52.610 1.00 18.88 ? 455  GLN A O   1 
ATOM   3461  C  CB  . GLN A  1 455 ? 54.712  43.943 55.330 1.00 17.38 ? 455  GLN A CB  1 
ATOM   3462  C  CG  . GLN A  1 455 ? 55.311  43.203 56.499 1.00 19.70 ? 455  GLN A CG  1 
ATOM   3463  C  CD  . GLN A  1 455 ? 54.298  42.285 57.169 1.00 23.25 ? 455  GLN A CD  1 
ATOM   3464  O  OE1 . GLN A  1 455 ? 53.358  41.812 56.530 1.00 22.88 ? 455  GLN A OE1 1 
ATOM   3465  N  NE2 . GLN A  1 455 ? 54.493  42.025 58.463 1.00 24.30 ? 455  GLN A NE2 1 
ATOM   3466  N  N   . TYR A  1 456 ? 54.548  46.935 53.489 1.00 18.34 ? 456  TYR A N   1 
ATOM   3467  C  CA  . TYR A  1 456 ? 54.026  47.478 52.234 1.00 17.94 ? 456  TYR A CA  1 
ATOM   3468  C  C   . TYR A  1 456 ? 54.547  48.901 52.078 1.00 18.03 ? 456  TYR A C   1 
ATOM   3469  O  O   . TYR A  1 456 ? 54.080  49.839 52.735 1.00 17.80 ? 456  TYR A O   1 
ATOM   3470  C  CB  . TYR A  1 456 ? 52.491  47.453 52.242 1.00 16.47 ? 456  TYR A CB  1 
ATOM   3471  C  CG  . TYR A  1 456 ? 51.806  47.513 50.881 1.00 16.18 ? 456  TYR A CG  1 
ATOM   3472  C  CD1 . TYR A  1 456 ? 51.663  48.726 50.186 1.00 16.87 ? 456  TYR A CD1 1 
ATOM   3473  C  CD2 . TYR A  1 456 ? 51.233  46.379 50.331 1.00 15.56 ? 456  TYR A CD2 1 
ATOM   3474  C  CE1 . TYR A  1 456 ? 50.952  48.795 48.980 1.00 15.29 ? 456  TYR A CE1 1 
ATOM   3475  C  CE2 . TYR A  1 456 ? 50.521  46.429 49.134 1.00 16.39 ? 456  TYR A CE2 1 
ATOM   3476  C  CZ  . TYR A  1 456 ? 50.379  47.634 48.460 1.00 17.13 ? 456  TYR A CZ  1 
ATOM   3477  O  OH  . TYR A  1 456 ? 49.654  47.664 47.284 1.00 15.80 ? 456  TYR A OH  1 
ATOM   3478  N  N   . TYR A  1 457 ? 55.522  49.059 51.195 1.00 17.93 ? 457  TYR A N   1 
ATOM   3479  C  CA  . TYR A  1 457 ? 56.137  50.360 50.979 1.00 18.26 ? 457  TYR A CA  1 
ATOM   3480  C  C   . TYR A  1 457 ? 55.928  50.966 49.609 1.00 19.78 ? 457  TYR A C   1 
ATOM   3481  O  O   . TYR A  1 457 ? 55.730  50.276 48.612 1.00 19.85 ? 457  TYR A O   1 
ATOM   3482  C  CB  . TYR A  1 457 ? 57.646  50.268 51.189 1.00 17.32 ? 457  TYR A CB  1 
ATOM   3483  C  CG  . TYR A  1 457 ? 58.105  50.096 52.617 1.00 17.62 ? 457  TYR A CG  1 
ATOM   3484  C  CD1 . TYR A  1 457 ? 58.518  51.198 53.370 1.00 16.47 ? 457  TYR A CD1 1 
ATOM   3485  C  CD2 . TYR A  1 457 ? 58.227  48.832 53.183 1.00 17.83 ? 457  TYR A CD2 1 
ATOM   3486  C  CE1 . TYR A  1 457 ? 59.057  51.043 54.643 1.00 16.73 ? 457  TYR A CE1 1 
ATOM   3487  C  CE2 . TYR A  1 457 ? 58.768  48.664 54.478 1.00 17.86 ? 457  TYR A CE2 1 
ATOM   3488  C  CZ  . TYR A  1 457 ? 59.184  49.765 55.189 1.00 16.49 ? 457  TYR A CZ  1 
ATOM   3489  O  OH  . TYR A  1 457 ? 59.771  49.612 56.420 1.00 17.76 ? 457  TYR A OH  1 
ATOM   3490  N  N   . SER A  1 458 ? 56.053  52.281 49.596 1.00 20.55 ? 458  SER A N   1 
ATOM   3491  C  CA  . SER A  1 458 ? 55.966  53.107 48.411 1.00 21.55 ? 458  SER A CA  1 
ATOM   3492  C  C   . SER A  1 458 ? 57.174  54.024 48.623 1.00 20.64 ? 458  SER A C   1 
ATOM   3493  O  O   . SER A  1 458 ? 57.618  54.187 49.766 1.00 18.10 ? 458  SER A O   1 
ATOM   3494  C  CB  . SER A  1 458 ? 54.703  53.942 48.452 1.00 23.12 ? 458  SER A CB  1 
ATOM   3495  O  OG  . SER A  1 458 ? 54.558  54.573 47.222 1.00 30.83 ? 458  SER A OG  1 
ATOM   3496  N  N   . VAL A  1 459 ? 57.679  54.652 47.561 1.00 18.96 ? 459  VAL A N   1 
ATOM   3497  C  CA  . VAL A  1 459 ? 58.854  55.508 47.702 1.00 18.15 ? 459  VAL A CA  1 
ATOM   3498  C  C   . VAL A  1 459 ? 58.843  56.759 46.825 1.00 18.86 ? 459  VAL A C   1 
ATOM   3499  O  O   . VAL A  1 459 ? 58.194  56.790 45.781 1.00 20.97 ? 459  VAL A O   1 
ATOM   3500  C  CB  . VAL A  1 459 ? 60.145  54.686 47.385 1.00 18.62 ? 459  VAL A CB  1 
ATOM   3501  C  CG1 . VAL A  1 459 ? 60.169  54.265 45.897 1.00 16.94 ? 459  VAL A CG1 1 
ATOM   3502  C  CG2 . VAL A  1 459 ? 61.383  55.494 47.751 1.00 18.22 ? 459  VAL A CG2 1 
ATOM   3503  N  N   . SER A  1 460 ? 59.558  57.792 47.262 1.00 18.71 ? 460  SER A N   1 
ATOM   3504  C  CA  . SER A  1 460 ? 59.677  59.040 46.511 1.00 18.69 ? 460  SER A CA  1 
ATOM   3505  C  C   . SER A  1 460 ? 61.132  59.520 46.506 1.00 18.53 ? 460  SER A C   1 
ATOM   3506  O  O   . SER A  1 460 ? 61.673  59.954 47.535 1.00 18.77 ? 460  SER A O   1 
ATOM   3507  C  CB  . SER A  1 460 ? 58.776  60.122 47.112 1.00 20.08 ? 460  SER A CB  1 
ATOM   3508  O  OG  . SER A  1 460 ? 58.853  61.315 46.347 1.00 20.56 ? 460  SER A OG  1 
ATOM   3509  N  N   . PHE A  1 461 ? 61.776  59.454 45.346 1.00 17.49 ? 461  PHE A N   1 
ATOM   3510  C  CA  . PHE A  1 461 ? 63.178  59.868 45.256 1.00 18.00 ? 461  PHE A CA  1 
ATOM   3511  C  C   . PHE A  1 461 ? 63.352  61.355 44.894 1.00 19.18 ? 461  PHE A C   1 
ATOM   3512  O  O   . PHE A  1 461 ? 62.529  61.911 44.180 1.00 19.41 ? 461  PHE A O   1 
ATOM   3513  C  CB  . PHE A  1 461 ? 63.920  59.011 44.207 1.00 15.83 ? 461  PHE A CB  1 
ATOM   3514  C  CG  . PHE A  1 461 ? 64.276  57.615 44.682 1.00 15.07 ? 461  PHE A CG  1 
ATOM   3515  C  CD1 . PHE A  1 461 ? 63.341  56.580 44.644 1.00 14.86 ? 461  PHE A CD1 1 
ATOM   3516  C  CD2 . PHE A  1 461 ? 65.546  57.342 45.179 1.00 13.46 ? 461  PHE A CD2 1 
ATOM   3517  C  CE1 . PHE A  1 461 ? 63.670  55.297 45.099 1.00 14.01 ? 461  PHE A CE1 1 
ATOM   3518  C  CE2 . PHE A  1 461 ? 65.879  56.070 45.633 1.00 13.93 ? 461  PHE A CE2 1 
ATOM   3519  C  CZ  . PHE A  1 461 ? 64.934  55.046 45.591 1.00 14.00 ? 461  PHE A CZ  1 
ATOM   3520  N  N   . SER A  1 462 ? 64.415  61.990 45.395 1.00 20.13 ? 462  SER A N   1 
ATOM   3521  C  CA  . SER A  1 462 ? 64.701  63.385 45.038 1.00 22.87 ? 462  SER A CA  1 
ATOM   3522  C  C   . SER A  1 462 ? 65.176  63.409 43.565 1.00 24.64 ? 462  SER A C   1 
ATOM   3523  O  O   . SER A  1 462 ? 65.415  62.359 42.965 1.00 23.69 ? 462  SER A O   1 
ATOM   3524  C  CB  . SER A  1 462 ? 65.791  63.985 45.944 1.00 22.45 ? 462  SER A CB  1 
ATOM   3525  O  OG  . SER A  1 462 ? 67.051  63.337 45.771 1.00 21.73 ? 462  SER A OG  1 
ATOM   3526  N  N   . LYS A  1 463 ? 65.331  64.602 42.998 1.00 28.23 ? 463  LYS A N   1 
ATOM   3527  C  CA  . LYS A  1 463 ? 65.725  64.755 41.590 1.00 30.32 ? 463  LYS A CA  1 
ATOM   3528  C  C   . LYS A  1 463 ? 66.768  63.819 41.005 1.00 30.45 ? 463  LYS A C   1 
ATOM   3529  O  O   . LYS A  1 463 ? 66.543  63.267 39.930 1.00 31.46 ? 463  LYS A O   1 
ATOM   3530  C  CB  . LYS A  1 463 ? 66.158  66.195 41.312 1.00 32.27 ? 463  LYS A CB  1 
ATOM   3531  C  CG  . LYS A  1 463 ? 65.002  67.164 41.316 1.00 36.81 ? 463  LYS A CG  1 
ATOM   3532  C  CD  . LYS A  1 463 ? 63.987  66.772 40.257 1.00 39.33 ? 463  LYS A CD  1 
ATOM   3533  C  CE  . LYS A  1 463 ? 62.772  67.677 40.283 1.00 41.53 ? 463  LYS A CE  1 
ATOM   3534  N  NZ  . LYS A  1 463 ? 61.670  67.092 39.457 1.00 43.39 ? 463  LYS A NZ  1 
ATOM   3535  N  N   . GLU A  1 464 ? 67.898  63.644 41.681 1.00 29.61 ? 464  GLU A N   1 
ATOM   3536  C  CA  . GLU A  1 464 ? 68.960  62.772 41.171 1.00 29.64 ? 464  GLU A CA  1 
ATOM   3537  C  C   . GLU A  1 464 ? 69.107  61.524 42.035 1.00 28.62 ? 464  GLU A C   1 
ATOM   3538  O  O   . GLU A  1 464 ? 70.178  60.894 42.085 1.00 26.94 ? 464  GLU A O   1 
ATOM   3539  C  CB  . GLU A  1 464 ? 70.307  63.515 41.132 1.00 32.64 ? 464  GLU A CB  1 
ATOM   3540  C  CG  . GLU A  1 464 ? 70.291  64.797 40.322 1.00 36.91 ? 464  GLU A CG  1 
ATOM   3541  C  CD  . GLU A  1 464 ? 69.883  64.544 38.887 1.00 41.50 ? 464  GLU A CD  1 
ATOM   3542  O  OE1 . GLU A  1 464 ? 70.551  63.707 38.227 1.00 44.33 ? 464  GLU A OE1 1 
ATOM   3543  O  OE2 . GLU A  1 464 ? 68.900  65.169 38.411 1.00 42.53 ? 464  GLU A OE2 1 
ATOM   3544  N  N   . ALA A  1 465 ? 68.031  61.179 42.729 1.00 26.56 ? 465  ALA A N   1 
ATOM   3545  C  CA  . ALA A  1 465 ? 68.027  60.007 43.579 1.00 24.78 ? 465  ALA A CA  1 
ATOM   3546  C  C   . ALA A  1 465 ? 69.034  60.057 44.714 1.00 23.20 ? 465  ALA A C   1 
ATOM   3547  O  O   . ALA A  1 465 ? 69.426  59.033 45.247 1.00 21.74 ? 465  ALA A O   1 
ATOM   3548  C  CB  . ALA A  1 465 ? 68.241  58.777 42.748 1.00 23.05 ? 465  ALA A CB  1 
ATOM   3549  N  N   . LYS A  1 466 ? 69.451  61.255 45.092 1.00 24.47 ? 466  LYS A N   1 
ATOM   3550  C  CA  . LYS A  1 466 ? 70.398  61.410 46.203 1.00 24.31 ? 466  LYS A CA  1 
ATOM   3551  C  C   . LYS A  1 466 ? 69.674  61.026 47.522 1.00 24.19 ? 466  LYS A C   1 
ATOM   3552  O  O   . LYS A  1 466 ? 70.276  60.460 48.442 1.00 22.21 ? 466  LYS A O   1 
ATOM   3553  C  CB  . LYS A  1 466 ? 70.857  62.865 46.257 1.00 26.81 ? 466  LYS A CB  1 
ATOM   3554  C  CG  . LYS A  1 466 ? 72.057  63.158 47.161 1.00 30.15 ? 466  LYS A CG  1 
ATOM   3555  C  CD  . LYS A  1 466 ? 72.506  64.624 46.960 1.00 32.86 ? 466  LYS A CD  1 
ATOM   3556  C  CE  . LYS A  1 466 ? 73.631  65.035 47.909 1.00 34.85 ? 466  LYS A CE  1 
ATOM   3557  N  NZ  . LYS A  1 466 ? 74.921  64.393 47.543 1.00 36.82 ? 466  LYS A NZ  1 
ATOM   3558  N  N   . TYR A  1 467 ? 68.375  61.318 47.587 1.00 22.19 ? 467  TYR A N   1 
ATOM   3559  C  CA  . TYR A  1 467 ? 67.566  61.007 48.769 1.00 22.39 ? 467  TYR A CA  1 
ATOM   3560  C  C   . TYR A  1 467 ? 66.252  60.343 48.395 1.00 21.94 ? 467  TYR A C   1 
ATOM   3561  O  O   . TYR A  1 467 ? 65.771  60.488 47.271 1.00 22.35 ? 467  TYR A O   1 
ATOM   3562  C  CB  . TYR A  1 467 ? 67.215  62.281 49.539 1.00 21.22 ? 467  TYR A CB  1 
ATOM   3563  C  CG  . TYR A  1 467 ? 68.391  63.039 50.063 1.00 23.58 ? 467  TYR A CG  1 
ATOM   3564  C  CD1 . TYR A  1 467 ? 69.006  62.666 51.263 1.00 24.08 ? 467  TYR A CD1 1 
ATOM   3565  C  CD2 . TYR A  1 467 ? 68.922  64.114 49.349 1.00 23.23 ? 467  TYR A CD2 1 
ATOM   3566  C  CE1 . TYR A  1 467 ? 70.127  63.349 51.734 1.00 25.72 ? 467  TYR A CE1 1 
ATOM   3567  C  CE2 . TYR A  1 467 ? 70.046  64.798 49.806 1.00 24.42 ? 467  TYR A CE2 1 
ATOM   3568  C  CZ  . TYR A  1 467 ? 70.642  64.411 50.991 1.00 25.67 ? 467  TYR A CZ  1 
ATOM   3569  O  OH  . TYR A  1 467 ? 71.776  65.060 51.422 1.00 27.10 ? 467  TYR A OH  1 
ATOM   3570  N  N   . TYR A  1 468 ? 65.666  59.620 49.342 1.00 21.85 ? 468  TYR A N   1 
ATOM   3571  C  CA  . TYR A  1 468 ? 64.360  59.022 49.096 1.00 20.89 ? 468  TYR A CA  1 
ATOM   3572  C  C   . TYR A  1 468 ? 63.511  58.976 50.350 1.00 21.71 ? 468  TYR A C   1 
ATOM   3573  O  O   . TYR A  1 468 ? 64.023  58.828 51.470 1.00 23.23 ? 468  TYR A O   1 
ATOM   3574  C  CB  . TYR A  1 468 ? 64.462  57.615 48.481 1.00 19.12 ? 468  TYR A CB  1 
ATOM   3575  C  CG  . TYR A  1 468 ? 65.250  56.588 49.272 1.00 18.75 ? 468  TYR A CG  1 
ATOM   3576  C  CD1 . TYR A  1 468 ? 66.635  56.521 49.161 1.00 17.48 ? 468  TYR A CD1 1 
ATOM   3577  C  CD2 . TYR A  1 468 ? 64.606  55.644 50.078 1.00 17.20 ? 468  TYR A CD2 1 
ATOM   3578  C  CE1 . TYR A  1 468 ? 67.372  55.534 49.816 1.00 18.58 ? 468  TYR A CE1 1 
ATOM   3579  C  CE2 . TYR A  1 468 ? 65.332  54.645 50.751 1.00 17.87 ? 468  TYR A CE2 1 
ATOM   3580  C  CZ  . TYR A  1 468 ? 66.726  54.594 50.607 1.00 19.64 ? 468  TYR A CZ  1 
ATOM   3581  O  OH  . TYR A  1 468 ? 67.479  53.599 51.207 1.00 17.04 ? 468  TYR A OH  1 
ATOM   3582  N  N   . GLN A  1 469 ? 62.209  59.170 50.157 1.00 20.50 ? 469  GLN A N   1 
ATOM   3583  C  CA  . GLN A  1 469 ? 61.267  59.108 51.258 1.00 19.56 ? 469  GLN A CA  1 
ATOM   3584  C  C   . GLN A  1 469 ? 60.556  57.772 51.162 1.00 19.40 ? 469  GLN A C   1 
ATOM   3585  O  O   . GLN A  1 469 ? 60.047  57.412 50.102 1.00 19.16 ? 469  GLN A O   1 
ATOM   3586  C  CB  . GLN A  1 469 ? 60.207  60.212 51.174 1.00 17.93 ? 469  GLN A CB  1 
ATOM   3587  C  CG  . GLN A  1 469 ? 59.103  60.024 52.208 1.00 16.66 ? 469  GLN A CG  1 
ATOM   3588  C  CD  . GLN A  1 469 ? 57.843  60.805 51.883 1.00 17.73 ? 469  GLN A CD  1 
ATOM   3589  O  OE1 . GLN A  1 469 ? 57.399  60.832 50.735 1.00 17.04 ? 469  GLN A OE1 1 
ATOM   3590  N  NE2 . GLN A  1 469 ? 57.256  61.440 52.891 1.00 15.56 ? 469  GLN A NE2 1 
ATOM   3591  N  N   . LEU A  1 470 ? 60.550  57.029 52.259 1.00 19.18 ? 470  LEU A N   1 
ATOM   3592  C  CA  . LEU A  1 470 ? 59.858  55.751 52.303 1.00 19.20 ? 470  LEU A CA  1 
ATOM   3593  C  C   . LEU A  1 470 ? 58.515  55.951 52.990 1.00 20.36 ? 470  LEU A C   1 
ATOM   3594  O  O   . LEU A  1 470 ? 58.429  56.619 54.037 1.00 20.75 ? 470  LEU A O   1 
ATOM   3595  C  CB  . LEU A  1 470 ? 60.667  54.718 53.078 1.00 17.48 ? 470  LEU A CB  1 
ATOM   3596  C  CG  . LEU A  1 470 ? 61.714  53.971 52.256 1.00 17.51 ? 470  LEU A CG  1 
ATOM   3597  C  CD1 . LEU A  1 470 ? 62.451  53.045 53.177 1.00 17.75 ? 470  LEU A CD1 1 
ATOM   3598  C  CD2 . LEU A  1 470 ? 61.050  53.186 51.144 1.00 14.16 ? 470  LEU A CD2 1 
ATOM   3599  N  N   . ARG A  1 471 ? 57.469  55.400 52.384 1.00 20.52 ? 471  ARG A N   1 
ATOM   3600  C  CA  . ARG A  1 471 ? 56.122  55.496 52.928 1.00 21.68 ? 471  ARG A CA  1 
ATOM   3601  C  C   . ARG A  1 471 ? 55.586  54.092 53.162 1.00 21.39 ? 471  ARG A C   1 
ATOM   3602  O  O   . ARG A  1 471 ? 55.180  53.392 52.231 1.00 20.48 ? 471  ARG A O   1 
ATOM   3603  C  CB  . ARG A  1 471 ? 55.181  56.245 51.982 1.00 23.03 ? 471  ARG A CB  1 
ATOM   3604  C  CG  . ARG A  1 471 ? 53.711  56.158 52.409 1.00 31.13 ? 471  ARG A CG  1 
ATOM   3605  C  CD  . ARG A  1 471 ? 52.733  56.534 51.289 1.00 36.84 ? 471  ARG A CD  1 
ATOM   3606  N  NE  . ARG A  1 471 ? 51.956  55.375 50.859 1.00 42.47 ? 471  ARG A NE  1 
ATOM   3607  C  CZ  . ARG A  1 471 ? 51.354  55.257 49.677 1.00 45.33 ? 471  ARG A CZ  1 
ATOM   3608  N  NH1 . ARG A  1 471 ? 51.434  56.238 48.780 1.00 46.21 ? 471  ARG A NH1 1 
ATOM   3609  N  NH2 . ARG A  1 471 ? 50.669  54.149 49.390 1.00 46.72 ? 471  ARG A NH2 1 
ATOM   3610  N  N   . CYS A  1 472 ? 55.615  53.685 54.426 1.00 20.24 ? 472  CYS A N   1 
ATOM   3611  C  CA  . CYS A  1 472 ? 55.141  52.377 54.868 1.00 19.41 ? 472  CYS A CA  1 
ATOM   3612  C  C   . CYS A  1 472 ? 53.636  52.561 55.109 1.00 19.22 ? 472  CYS A C   1 
ATOM   3613  O  O   . CYS A  1 472 ? 53.236  53.481 55.809 1.00 18.04 ? 472  CYS A O   1 
ATOM   3614  C  CB  . CYS A  1 472 ? 55.867  51.980 56.168 1.00 20.43 ? 472  CYS A CB  1 
ATOM   3615  S  SG  . CYS A  1 472 ? 54.954  50.896 57.304 1.00 25.89 ? 472  CYS A SG  1 
ATOM   3616  N  N   . SER A  1 473 ? 52.799  51.708 54.521 1.00 19.33 ? 473  SER A N   1 
ATOM   3617  C  CA  . SER A  1 473 ? 51.366  51.828 54.763 1.00 19.65 ? 473  SER A CA  1 
ATOM   3618  C  C   . SER A  1 473 ? 50.709  50.610 55.454 1.00 19.93 ? 473  SER A C   1 
ATOM   3619  O  O   . SER A  1 473 ? 49.484  50.518 55.514 1.00 20.22 ? 473  SER A O   1 
ATOM   3620  C  CB  . SER A  1 473 ? 50.636  52.188 53.461 1.00 19.82 ? 473  SER A CB  1 
ATOM   3621  O  OG  . SER A  1 473 ? 50.845  51.211 52.480 1.00 23.82 ? 473  SER A OG  1 
ATOM   3622  N  N   . GLY A  1 474 ? 51.515  49.696 55.989 1.00 18.47 ? 474  GLY A N   1 
ATOM   3623  C  CA  . GLY A  1 474 ? 50.957  48.541 56.673 1.00 18.37 ? 474  GLY A CA  1 
ATOM   3624  C  C   . GLY A  1 474 ? 51.942  47.409 56.949 1.00 17.59 ? 474  GLY A C   1 
ATOM   3625  O  O   . GLY A  1 474 ? 53.036  47.365 56.370 1.00 18.25 ? 474  GLY A O   1 
ATOM   3626  N  N   . PRO A  1 475 ? 51.549  46.420 57.757 1.00 16.27 ? 475  PRO A N   1 
ATOM   3627  C  CA  . PRO A  1 475 ? 50.265  46.239 58.440 1.00 17.06 ? 475  PRO A CA  1 
ATOM   3628  C  C   . PRO A  1 475 ? 49.984  47.162 59.623 1.00 17.66 ? 475  PRO A C   1 
ATOM   3629  O  O   . PRO A  1 475 ? 48.831  47.314 60.010 1.00 19.48 ? 475  PRO A O   1 
ATOM   3630  C  CB  . PRO A  1 475 ? 50.298  44.768 58.838 1.00 15.28 ? 475  PRO A CB  1 
ATOM   3631  C  CG  . PRO A  1 475 ? 51.746  44.566 59.153 1.00 16.72 ? 475  PRO A CG  1 
ATOM   3632  C  CD  . PRO A  1 475 ? 52.437  45.274 58.005 1.00 16.37 ? 475  PRO A CD  1 
ATOM   3633  N  N   . GLY A  1 476 ? 51.026  47.759 60.203 1.00 18.06 ? 476  GLY A N   1 
ATOM   3634  C  CA  . GLY A  1 476 ? 50.832  48.683 61.313 1.00 16.54 ? 476  GLY A CA  1 
ATOM   3635  C  C   . GLY A  1 476 ? 50.502  50.071 60.771 1.00 18.20 ? 476  GLY A C   1 
ATOM   3636  O  O   . GLY A  1 476 ? 50.294  50.238 59.556 1.00 17.49 ? 476  GLY A O   1 
ATOM   3637  N  N   . LEU A  1 477 ? 50.452  51.074 61.649 1.00 17.75 ? 477  LEU A N   1 
ATOM   3638  C  CA  . LEU A  1 477 ? 50.133  52.445 61.232 1.00 16.46 ? 477  LEU A CA  1 
ATOM   3639  C  C   . LEU A  1 477 ? 51.182  53.012 60.299 1.00 16.34 ? 477  LEU A C   1 
ATOM   3640  O  O   . LEU A  1 477 ? 52.372  52.761 60.471 1.00 15.58 ? 477  LEU A O   1 
ATOM   3641  C  CB  . LEU A  1 477 ? 49.999  53.369 62.446 1.00 17.12 ? 477  LEU A CB  1 
ATOM   3642  C  CG  . LEU A  1 477 ? 48.925  52.976 63.467 1.00 17.63 ? 477  LEU A CG  1 
ATOM   3643  C  CD1 . LEU A  1 477 ? 48.949  53.983 64.616 1.00 16.61 ? 477  LEU A CD1 1 
ATOM   3644  C  CD2 . LEU A  1 477 ? 47.540  52.938 62.796 1.00 16.85 ? 477  LEU A CD2 1 
ATOM   3645  N  N   . PRO A  1 478 ? 50.748  53.785 59.289 1.00 16.91 ? 478  PRO A N   1 
ATOM   3646  C  CA  . PRO A  1 478 ? 51.652  54.398 58.312 1.00 17.26 ? 478  PRO A CA  1 
ATOM   3647  C  C   . PRO A  1 478 ? 52.853  55.065 58.963 1.00 18.47 ? 478  PRO A C   1 
ATOM   3648  O  O   . PRO A  1 478 ? 52.734  55.743 59.997 1.00 18.86 ? 478  PRO A O   1 
ATOM   3649  C  CB  . PRO A  1 478 ? 50.756  55.393 57.580 1.00 17.06 ? 478  PRO A CB  1 
ATOM   3650  C  CG  . PRO A  1 478 ? 49.421  54.660 57.563 1.00 18.77 ? 478  PRO A CG  1 
ATOM   3651  C  CD  . PRO A  1 478 ? 49.343  54.132 58.998 1.00 17.28 ? 478  PRO A CD  1 
ATOM   3652  N  N   . LEU A  1 479 ? 54.008  54.861 58.339 1.00 18.02 ? 479  LEU A N   1 
ATOM   3653  C  CA  . LEU A  1 479 ? 55.261  55.397 58.822 1.00 16.86 ? 479  LEU A CA  1 
ATOM   3654  C  C   . LEU A  1 479 ? 56.033  56.028 57.672 1.00 17.49 ? 479  LEU A C   1 
ATOM   3655  O  O   . LEU A  1 479 ? 56.318  55.365 56.675 1.00 18.61 ? 479  LEU A O   1 
ATOM   3656  C  CB  . LEU A  1 479 ? 56.080  54.265 59.440 1.00 16.41 ? 479  LEU A CB  1 
ATOM   3657  C  CG  . LEU A  1 479 ? 57.478  54.624 59.924 1.00 15.31 ? 479  LEU A CG  1 
ATOM   3658  C  CD1 . LEU A  1 479 ? 57.406  55.807 60.879 1.00 13.96 ? 479  LEU A CD1 1 
ATOM   3659  C  CD2 . LEU A  1 479 ? 58.087  53.405 60.631 1.00 15.27 ? 479  LEU A CD2 1 
ATOM   3660  N  N   . TYR A  1 480 ? 56.372  57.301 57.814 1.00 16.63 ? 480  TYR A N   1 
ATOM   3661  C  CA  . TYR A  1 480 ? 57.109  58.016 56.782 1.00 17.83 ? 480  TYR A CA  1 
ATOM   3662  C  C   . TYR A  1 480 ? 58.508  58.366 57.264 1.00 18.06 ? 480  TYR A C   1 
ATOM   3663  O  O   . TYR A  1 480 ? 58.671  59.021 58.300 1.00 19.03 ? 480  TYR A O   1 
ATOM   3664  C  CB  . TYR A  1 480 ? 56.368  59.301 56.389 1.00 17.74 ? 480  TYR A CB  1 
ATOM   3665  C  CG  . TYR A  1 480 ? 54.960  59.085 55.869 1.00 18.41 ? 480  TYR A CG  1 
ATOM   3666  C  CD1 . TYR A  1 480 ? 53.912  58.739 56.732 1.00 18.38 ? 480  TYR A CD1 1 
ATOM   3667  C  CD2 . TYR A  1 480 ? 54.672  59.236 54.510 1.00 19.81 ? 480  TYR A CD2 1 
ATOM   3668  C  CE1 . TYR A  1 480 ? 52.606  58.552 56.257 1.00 19.19 ? 480  TYR A CE1 1 
ATOM   3669  C  CE2 . TYR A  1 480 ? 53.364  59.050 54.017 1.00 22.15 ? 480  TYR A CE2 1 
ATOM   3670  C  CZ  . TYR A  1 480 ? 52.336  58.709 54.901 1.00 22.13 ? 480  TYR A CZ  1 
ATOM   3671  O  OH  . TYR A  1 480 ? 51.053  58.536 54.411 1.00 24.05 ? 480  TYR A OH  1 
ATOM   3672  N  N   . THR A  1 481 ? 59.510  57.947 56.495 1.00 18.35 ? 481  THR A N   1 
ATOM   3673  C  CA  . THR A  1 481 ? 60.919  58.180 56.823 1.00 18.47 ? 481  THR A CA  1 
ATOM   3674  C  C   . THR A  1 481 ? 61.703  58.762 55.642 1.00 18.94 ? 481  THR A C   1 
ATOM   3675  O  O   . THR A  1 481 ? 61.289  58.641 54.492 1.00 18.28 ? 481  THR A O   1 
ATOM   3676  C  CB  . THR A  1 481 ? 61.605  56.852 57.218 1.00 19.81 ? 481  THR A CB  1 
ATOM   3677  O  OG1 . THR A  1 481 ? 61.253  55.847 56.252 1.00 19.09 ? 481  THR A OG1 1 
ATOM   3678  C  CG2 . THR A  1 481 ? 61.163  56.389 58.612 1.00 19.53 ? 481  THR A CG2 1 
ATOM   3679  N  N   . LEU A  1 482 ? 62.838  59.390 55.940 1.00 18.31 ? 482  LEU A N   1 
ATOM   3680  C  CA  . LEU A  1 482 ? 63.694  59.967 54.919 1.00 19.07 ? 482  LEU A CA  1 
ATOM   3681  C  C   . LEU A  1 482 ? 65.049  59.251 54.971 1.00 19.22 ? 482  LEU A C   1 
ATOM   3682  O  O   . LEU A  1 482 ? 65.563  58.944 56.045 1.00 19.48 ? 482  LEU A O   1 
ATOM   3683  C  CB  . LEU A  1 482 ? 63.876  61.473 55.145 1.00 17.84 ? 482  LEU A CB  1 
ATOM   3684  C  CG  . LEU A  1 482 ? 64.500  62.205 53.946 1.00 19.88 ? 482  LEU A CG  1 
ATOM   3685  C  CD1 . LEU A  1 482 ? 63.520  62.174 52.767 1.00 17.17 ? 482  LEU A CD1 1 
ATOM   3686  C  CD2 . LEU A  1 482 ? 64.832  63.647 54.327 1.00 20.37 ? 482  LEU A CD2 1 
ATOM   3687  N  N   . HIS A  1 483 ? 65.624  58.994 53.806 1.00 19.57 ? 483  HIS A N   1 
ATOM   3688  C  CA  . HIS A  1 483 ? 66.880  58.271 53.711 1.00 19.59 ? 483  HIS A CA  1 
ATOM   3689  C  C   . HIS A  1 483 ? 67.802  58.891 52.671 1.00 20.51 ? 483  HIS A C   1 
ATOM   3690  O  O   . HIS A  1 483 ? 67.345  59.619 51.795 1.00 21.44 ? 483  HIS A O   1 
ATOM   3691  C  CB  . HIS A  1 483 ? 66.597  56.825 53.299 1.00 19.07 ? 483  HIS A CB  1 
ATOM   3692  C  CG  . HIS A  1 483 ? 65.526  56.166 54.103 1.00 18.87 ? 483  HIS A CG  1 
ATOM   3693  N  ND1 . HIS A  1 483 ? 65.789  55.162 55.009 1.00 18.55 ? 483  HIS A ND1 1 
ATOM   3694  C  CD2 . HIS A  1 483 ? 64.188  56.378 54.150 1.00 18.72 ? 483  HIS A CD2 1 
ATOM   3695  C  CE1 . HIS A  1 483 ? 64.660  54.783 55.581 1.00 19.54 ? 483  HIS A CE1 1 
ATOM   3696  N  NE2 . HIS A  1 483 ? 63.674  55.507 55.079 1.00 19.55 ? 483  HIS A NE2 1 
ATOM   3697  N  N   . SER A  1 484 ? 69.096  58.597 52.777 1.00 21.23 ? 484  SER A N   1 
ATOM   3698  C  CA  . SER A  1 484 ? 70.082  59.085 51.813 1.00 23.95 ? 484  SER A CA  1 
ATOM   3699  C  C   . SER A  1 484 ? 70.592  57.861 51.061 1.00 23.14 ? 484  SER A C   1 
ATOM   3700  O  O   . SER A  1 484 ? 70.857  56.812 51.653 1.00 22.95 ? 484  SER A O   1 
ATOM   3701  C  CB  . SER A  1 484 ? 71.243  59.791 52.512 1.00 24.80 ? 484  SER A CB  1 
ATOM   3702  O  OG  . SER A  1 484 ? 71.850  58.916 53.428 1.00 27.86 ? 484  SER A OG  1 
ATOM   3703  N  N   . SER A  1 485 ? 70.741  58.004 49.759 1.00 23.27 ? 485  SER A N   1 
ATOM   3704  C  CA  . SER A  1 485 ? 71.173  56.893 48.921 1.00 25.64 ? 485  SER A CA  1 
ATOM   3705  C  C   . SER A  1 485 ? 72.613  56.401 49.020 1.00 26.44 ? 485  SER A C   1 
ATOM   3706  O  O   . SER A  1 485 ? 72.851  55.188 49.003 1.00 25.84 ? 485  SER A O   1 
ATOM   3707  C  CB  . SER A  1 485 ? 70.879  57.222 47.461 1.00 25.13 ? 485  SER A CB  1 
ATOM   3708  O  OG  . SER A  1 485 ? 69.498  57.502 47.296 1.00 26.95 ? 485  SER A OG  1 
ATOM   3709  N  N   . VAL A  1 486 ? 73.569  57.314 49.129 1.00 27.68 ? 486  VAL A N   1 
ATOM   3710  C  CA  . VAL A  1 486 ? 74.976  56.906 49.150 1.00 29.19 ? 486  VAL A CA  1 
ATOM   3711  C  C   . VAL A  1 486 ? 75.266  55.715 50.079 1.00 30.08 ? 486  VAL A C   1 
ATOM   3712  O  O   . VAL A  1 486 ? 75.987  54.787 49.695 1.00 30.08 ? 486  VAL A O   1 
ATOM   3713  C  CB  . VAL A  1 486 ? 75.911  58.108 49.473 1.00 29.53 ? 486  VAL A CB  1 
ATOM   3714  C  CG1 . VAL A  1 486 ? 75.742  58.541 50.910 1.00 28.48 ? 486  VAL A CG1 1 
ATOM   3715  C  CG2 . VAL A  1 486 ? 77.368  57.729 49.169 1.00 28.50 ? 486  VAL A CG2 1 
ATOM   3716  N  N   . ASN A  1 487 ? 74.718  55.722 51.289 1.00 29.23 ? 487  ASN A N   1 
ATOM   3717  C  CA  . ASN A  1 487 ? 74.931  54.584 52.168 1.00 29.27 ? 487  ASN A CA  1 
ATOM   3718  C  C   . ASN A  1 487 ? 73.625  54.081 52.772 1.00 28.77 ? 487  ASN A C   1 
ATOM   3719  O  O   . ASN A  1 487 ? 73.612  53.342 53.760 1.00 28.72 ? 487  ASN A O   1 
ATOM   3720  C  CB  . ASN A  1 487 ? 75.939  54.932 53.257 1.00 30.85 ? 487  ASN A CB  1 
ATOM   3721  C  CG  . ASN A  1 487 ? 77.367  54.960 52.731 1.00 33.39 ? 487  ASN A CG  1 
ATOM   3722  O  OD1 . ASN A  1 487 ? 77.815  54.021 52.067 1.00 34.77 ? 487  ASN A OD1 1 
ATOM   3723  N  ND2 . ASN A  1 487 ? 78.087  56.038 53.025 1.00 34.26 ? 487  ASN A ND2 1 
ATOM   3724  N  N   . ASP A  1 488 ? 72.521  54.474 52.154 1.00 27.05 ? 488  ASP A N   1 
ATOM   3725  C  CA  . ASP A  1 488 ? 71.210  54.080 52.629 1.00 26.10 ? 488  ASP A CA  1 
ATOM   3726  C  C   . ASP A  1 488 ? 71.024  54.329 54.117 1.00 25.95 ? 488  ASP A C   1 
ATOM   3727  O  O   . ASP A  1 488 ? 70.566  53.461 54.854 1.00 25.79 ? 488  ASP A O   1 
ATOM   3728  C  CB  . ASP A  1 488 ? 70.963  52.619 52.288 1.00 25.48 ? 488  ASP A CB  1 
ATOM   3729  C  CG  . ASP A  1 488 ? 70.970  52.386 50.791 1.00 26.32 ? 488  ASP A CG  1 
ATOM   3730  O  OD1 . ASP A  1 488 ? 71.842  51.647 50.292 1.00 25.85 ? 488  ASP A OD1 1 
ATOM   3731  O  OD2 . ASP A  1 488 ? 70.106  52.974 50.118 1.00 26.40 ? 488  ASP A OD2 1 
ATOM   3732  N  N   . LYS A  1 489 ? 71.384  55.528 54.562 1.00 26.03 ? 489  LYS A N   1 
ATOM   3733  C  CA  . LYS A  1 489 ? 71.205  55.865 55.962 1.00 25.95 ? 489  LYS A CA  1 
ATOM   3734  C  C   . LYS A  1 489 ? 69.757  56.282 56.222 1.00 24.33 ? 489  LYS A C   1 
ATOM   3735  O  O   . LYS A  1 489 ? 69.078  56.824 55.335 1.00 21.51 ? 489  LYS A O   1 
ATOM   3736  C  CB  . LYS A  1 489 ? 72.162  56.984 56.382 1.00 28.42 ? 489  LYS A CB  1 
ATOM   3737  C  CG  . LYS A  1 489 ? 73.607  56.510 56.442 1.00 32.83 ? 489  LYS A CG  1 
ATOM   3738  C  CD  . LYS A  1 489 ? 74.525  57.463 57.193 1.00 37.69 ? 489  LYS A CD  1 
ATOM   3739  C  CE  . LYS A  1 489 ? 74.766  58.752 56.425 1.00 40.15 ? 489  LYS A CE  1 
ATOM   3740  N  NZ  . LYS A  1 489 ? 73.512  59.528 56.239 1.00 41.69 ? 489  LYS A NZ  1 
ATOM   3741  N  N   . GLY A  1 490 ? 69.283  55.964 57.423 1.00 23.31 ? 490  GLY A N   1 
ATOM   3742  C  CA  . GLY A  1 490 ? 67.942  56.335 57.828 1.00 23.16 ? 490  GLY A CA  1 
ATOM   3743  C  C   . GLY A  1 490 ? 68.148  57.660 58.538 1.00 23.14 ? 490  GLY A C   1 
ATOM   3744  O  O   . GLY A  1 490 ? 68.506  57.691 59.710 1.00 23.24 ? 490  GLY A O   1 
ATOM   3745  N  N   . LEU A  1 491 ? 67.931  58.757 57.826 1.00 21.94 ? 491  LEU A N   1 
ATOM   3746  C  CA  . LEU A  1 491 ? 68.137  60.064 58.403 1.00 21.00 ? 491  LEU A CA  1 
ATOM   3747  C  C   . LEU A  1 491 ? 67.187  60.386 59.535 1.00 20.89 ? 491  LEU A C   1 
ATOM   3748  O  O   . LEU A  1 491 ? 67.630  60.656 60.650 1.00 20.98 ? 491  LEU A O   1 
ATOM   3749  C  CB  . LEU A  1 491 ? 68.029  61.138 57.322 1.00 20.47 ? 491  LEU A CB  1 
ATOM   3750  C  CG  . LEU A  1 491 ? 68.959  60.965 56.114 1.00 21.79 ? 491  LEU A CG  1 
ATOM   3751  C  CD1 . LEU A  1 491 ? 68.641  62.023 55.067 1.00 19.50 ? 491  LEU A CD1 1 
ATOM   3752  C  CD2 . LEU A  1 491 ? 70.419  61.067 56.555 1.00 21.44 ? 491  LEU A CD2 1 
ATOM   3753  N  N   . ARG A  1 492 ? 65.885  60.358 59.259 1.00 20.06 ? 492  ARG A N   1 
ATOM   3754  C  CA  . ARG A  1 492 ? 64.915  60.695 60.285 1.00 21.30 ? 492  ARG A CA  1 
ATOM   3755  C  C   . ARG A  1 492 ? 63.487  60.259 60.003 1.00 21.12 ? 492  ARG A C   1 
ATOM   3756  O  O   . ARG A  1 492 ? 63.128  59.937 58.870 1.00 20.99 ? 492  ARG A O   1 
ATOM   3757  C  CB  . ARG A  1 492 ? 64.917  62.214 60.521 1.00 22.03 ? 492  ARG A CB  1 
ATOM   3758  C  CG  . ARG A  1 492 ? 64.269  63.057 59.411 1.00 23.69 ? 492  ARG A CG  1 
ATOM   3759  C  CD  . ARG A  1 492 ? 64.602  64.553 59.597 1.00 23.98 ? 492  ARG A CD  1 
ATOM   3760  N  NE  . ARG A  1 492 ? 66.040  64.723 59.457 1.00 24.91 ? 492  ARG A NE  1 
ATOM   3761  C  CZ  . ARG A  1 492 ? 66.648  65.007 58.308 1.00 24.67 ? 492  ARG A CZ  1 
ATOM   3762  N  NH1 . ARG A  1 492 ? 65.934  65.191 57.201 1.00 24.24 ? 492  ARG A NH1 1 
ATOM   3763  N  NH2 . ARG A  1 492 ? 67.976  65.005 58.248 1.00 23.11 ? 492  ARG A NH2 1 
ATOM   3764  N  N   . VAL A  1 493 ? 62.676  60.283 61.053 1.00 20.32 ? 493  VAL A N   1 
ATOM   3765  C  CA  . VAL A  1 493 ? 61.273  59.933 60.963 1.00 20.88 ? 493  VAL A CA  1 
ATOM   3766  C  C   . VAL A  1 493 ? 60.494  61.216 60.699 1.00 21.59 ? 493  VAL A C   1 
ATOM   3767  O  O   . VAL A  1 493 ? 60.582  62.173 61.479 1.00 22.80 ? 493  VAL A O   1 
ATOM   3768  C  CB  . VAL A  1 493 ? 60.788  59.281 62.276 1.00 21.54 ? 493  VAL A CB  1 
ATOM   3769  C  CG1 . VAL A  1 493 ? 59.269  59.096 62.244 1.00 22.09 ? 493  VAL A CG1 1 
ATOM   3770  C  CG2 . VAL A  1 493 ? 61.488  57.934 62.479 1.00 19.12 ? 493  VAL A CG2 1 
ATOM   3771  N  N   . LEU A  1 494 ? 59.751  61.239 59.591 1.00 20.61 ? 494  LEU A N   1 
ATOM   3772  C  CA  . LEU A  1 494 ? 58.956  62.412 59.194 1.00 20.62 ? 494  LEU A CA  1 
ATOM   3773  C  C   . LEU A  1 494 ? 57.586  62.434 59.866 1.00 20.21 ? 494  LEU A C   1 
ATOM   3774  O  O   . LEU A  1 494 ? 57.098  63.489 60.270 1.00 21.22 ? 494  LEU A O   1 
ATOM   3775  C  CB  . LEU A  1 494 ? 58.794  62.433 57.660 1.00 19.47 ? 494  LEU A CB  1 
ATOM   3776  C  CG  . LEU A  1 494 ? 60.147  62.403 56.900 1.00 19.14 ? 494  LEU A CG  1 
ATOM   3777  C  CD1 . LEU A  1 494 ? 59.940  62.300 55.391 1.00 17.62 ? 494  LEU A CD1 1 
ATOM   3778  C  CD2 . LEU A  1 494 ? 60.936  63.666 57.245 1.00 17.03 ? 494  LEU A CD2 1 
ATOM   3779  N  N   . GLU A  1 495 ? 56.983  61.259 60.005 1.00 19.80 ? 495  GLU A N   1 
ATOM   3780  C  CA  . GLU A  1 495 ? 55.659  61.135 60.609 1.00 19.60 ? 495  GLU A CA  1 
ATOM   3781  C  C   . GLU A  1 495 ? 55.444  59.678 60.995 1.00 19.52 ? 495  GLU A C   1 
ATOM   3782  O  O   . GLU A  1 495 ? 55.518  58.792 60.132 1.00 19.44 ? 495  GLU A O   1 
ATOM   3783  C  CB  . GLU A  1 495 ? 54.588  61.543 59.604 1.00 19.77 ? 495  GLU A CB  1 
ATOM   3784  C  CG  . GLU A  1 495 ? 53.152  61.286 60.088 1.00 20.05 ? 495  GLU A CG  1 
ATOM   3785  C  CD  . GLU A  1 495 ? 52.809  62.112 61.306 1.00 21.43 ? 495  GLU A CD  1 
ATOM   3786  O  OE1 . GLU A  1 495 ? 52.876  63.366 61.214 1.00 24.94 ? 495  GLU A OE1 1 
ATOM   3787  O  OE2 . GLU A  1 495 ? 52.468  61.518 62.362 1.00 20.23 ? 495  GLU A OE2 1 
ATOM   3788  N  N   . ASP A  1 496 ? 55.165  59.435 62.273 1.00 17.64 ? 496  ASP A N   1 
ATOM   3789  C  CA  . ASP A  1 496 ? 54.971  58.078 62.753 1.00 18.52 ? 496  ASP A CA  1 
ATOM   3790  C  C   . ASP A  1 496 ? 53.558  57.735 63.238 1.00 19.14 ? 496  ASP A C   1 
ATOM   3791  O  O   . ASP A  1 496 ? 53.321  56.631 63.734 1.00 19.52 ? 496  ASP A O   1 
ATOM   3792  C  CB  . ASP A  1 496 ? 55.977  57.755 63.875 1.00 18.53 ? 496  ASP A CB  1 
ATOM   3793  C  CG  . ASP A  1 496 ? 55.836  58.669 65.077 1.00 18.80 ? 496  ASP A CG  1 
ATOM   3794  O  OD1 . ASP A  1 496 ? 54.774  59.305 65.262 1.00 17.31 ? 496  ASP A OD1 1 
ATOM   3795  O  OD2 . ASP A  1 496 ? 56.803  58.740 65.853 1.00 21.16 ? 496  ASP A OD2 1 
ATOM   3796  N  N   . ASN A  1 497 ? 52.636  58.676 63.095 1.00 19.19 ? 497  ASN A N   1 
ATOM   3797  C  CA  . ASN A  1 497 ? 51.260  58.496 63.520 1.00 20.95 ? 497  ASN A CA  1 
ATOM   3798  C  C   . ASN A  1 497 ? 51.101  58.103 64.982 1.00 21.42 ? 497  ASN A C   1 
ATOM   3799  O  O   . ASN A  1 497 ? 50.150  57.419 65.335 1.00 20.16 ? 497  ASN A O   1 
ATOM   3800  C  CB  . ASN A  1 497 ? 50.548  57.471 62.621 1.00 21.45 ? 497  ASN A CB  1 
ATOM   3801  C  CG  . ASN A  1 497 ? 49.993  58.102 61.343 1.00 22.81 ? 497  ASN A CG  1 
ATOM   3802  O  OD1 . ASN A  1 497 ? 49.107  58.959 61.389 1.00 22.00 ? 497  ASN A OD1 1 
ATOM   3803  N  ND2 . ASN A  1 497 ? 50.528  57.686 60.199 1.00 22.63 ? 497  ASN A ND2 1 
ATOM   3804  N  N   . SER A  1 498 ? 52.032  58.538 65.828 1.00 21.22 ? 498  SER A N   1 
ATOM   3805  C  CA  . SER A  1 498 ? 51.943  58.223 67.250 1.00 23.30 ? 498  SER A CA  1 
ATOM   3806  C  C   . SER A  1 498 ? 50.663  58.837 67.856 1.00 22.54 ? 498  SER A C   1 
ATOM   3807  O  O   . SER A  1 498 ? 50.098  58.289 68.781 1.00 22.48 ? 498  SER A O   1 
ATOM   3808  C  CB  . SER A  1 498 ? 53.202  58.697 68.001 1.00 23.23 ? 498  SER A CB  1 
ATOM   3809  O  OG  . SER A  1 498 ? 53.426  60.076 67.823 1.00 26.40 ? 498  SER A OG  1 
ATOM   3810  N  N   . ALA A  1 499 ? 50.190  59.950 67.318 1.00 22.18 ? 499  ALA A N   1 
ATOM   3811  C  CA  . ALA A  1 499 ? 48.956  60.532 67.831 1.00 23.06 ? 499  ALA A CA  1 
ATOM   3812  C  C   . ALA A  1 499 ? 47.781  59.544 67.664 1.00 23.86 ? 499  ALA A C   1 
ATOM   3813  O  O   . ALA A  1 499 ? 47.013  59.283 68.617 1.00 25.41 ? 499  ALA A O   1 
ATOM   3814  C  CB  . ALA A  1 499 ? 48.644  61.859 67.111 1.00 21.42 ? 499  ALA A CB  1 
ATOM   3815  N  N   . LEU A  1 500 ? 47.640  58.992 66.461 1.00 21.92 ? 500  LEU A N   1 
ATOM   3816  C  CA  . LEU A  1 500 ? 46.572  58.033 66.164 1.00 21.20 ? 500  LEU A CA  1 
ATOM   3817  C  C   . LEU A  1 500 ? 46.740  56.740 66.977 1.00 21.87 ? 500  LEU A C   1 
ATOM   3818  O  O   . LEU A  1 500 ? 45.756  56.136 67.437 1.00 21.21 ? 500  LEU A O   1 
ATOM   3819  C  CB  . LEU A  1 500 ? 46.568  57.716 64.664 1.00 21.17 ? 500  LEU A CB  1 
ATOM   3820  C  CG  . LEU A  1 500 ? 45.541  56.705 64.157 1.00 20.73 ? 500  LEU A CG  1 
ATOM   3821  C  CD1 . LEU A  1 500 ? 44.128  57.106 64.608 1.00 21.67 ? 500  LEU A CD1 1 
ATOM   3822  C  CD2 . LEU A  1 500 ? 45.636  56.641 62.635 1.00 22.21 ? 500  LEU A CD2 1 
ATOM   3823  N  N   . ASP A  1 501 ? 47.984  56.304 67.130 1.00 22.54 ? 501  ASP A N   1 
ATOM   3824  C  CA  . ASP A  1 501 ? 48.268  55.105 67.904 1.00 25.48 ? 501  ASP A CA  1 
ATOM   3825  C  C   . ASP A  1 501 ? 47.736  55.329 69.330 1.00 26.66 ? 501  ASP A C   1 
ATOM   3826  O  O   . ASP A  1 501 ? 47.107  54.452 69.904 1.00 26.04 ? 501  ASP A O   1 
ATOM   3827  C  CB  . ASP A  1 501 ? 49.773  54.846 67.935 1.00 26.66 ? 501  ASP A CB  1 
ATOM   3828  C  CG  . ASP A  1 501 ? 50.145  53.636 68.780 1.00 28.72 ? 501  ASP A CG  1 
ATOM   3829  O  OD1 . ASP A  1 501 ? 49.798  52.505 68.401 1.00 29.10 ? 501  ASP A OD1 1 
ATOM   3830  O  OD2 . ASP A  1 501 ? 50.777  53.811 69.842 1.00 32.60 ? 501  ASP A OD2 1 
ATOM   3831  N  N   . LYS A  1 502 ? 47.972  56.517 69.884 1.00 28.35 ? 502  LYS A N   1 
ATOM   3832  C  CA  . LYS A  1 502 ? 47.507  56.837 71.234 1.00 30.22 ? 502  LYS A CA  1 
ATOM   3833  C  C   . LYS A  1 502 ? 45.972  56.767 71.294 1.00 30.75 ? 502  LYS A C   1 
ATOM   3834  O  O   . LYS A  1 502 ? 45.398  56.169 72.208 1.00 30.76 ? 502  LYS A O   1 
ATOM   3835  C  CB  . LYS A  1 502 ? 47.995  58.238 71.649 1.00 31.58 ? 502  LYS A CB  1 
ATOM   3836  C  CG  . LYS A  1 502 ? 47.554  58.651 73.064 1.00 35.65 ? 502  LYS A CG  1 
ATOM   3837  C  CD  . LYS A  1 502 ? 47.748  60.153 73.367 1.00 37.36 ? 502  LYS A CD  1 
ATOM   3838  C  CE  . LYS A  1 502 ? 49.219  60.541 73.551 1.00 38.39 ? 502  LYS A CE  1 
ATOM   3839  N  NZ  . LYS A  1 502 ? 50.040  60.423 72.304 1.00 37.93 ? 502  LYS A NZ  1 
ATOM   3840  N  N   . MET A  1 503 ? 45.303  57.364 70.314 1.00 30.92 ? 503  MET A N   1 
ATOM   3841  C  CA  . MET A  1 503 ? 43.848  57.339 70.296 1.00 31.71 ? 503  MET A CA  1 
ATOM   3842  C  C   . MET A  1 503 ? 43.287  55.926 70.139 1.00 31.28 ? 503  MET A C   1 
ATOM   3843  O  O   . MET A  1 503 ? 42.360  55.542 70.842 1.00 31.29 ? 503  MET A O   1 
ATOM   3844  C  CB  . MET A  1 503 ? 43.305  58.218 69.174 1.00 34.85 ? 503  MET A CB  1 
ATOM   3845  C  CG  . MET A  1 503 ? 43.299  59.711 69.456 1.00 37.70 ? 503  MET A CG  1 
ATOM   3846  S  SD  . MET A  1 503 ? 42.382  60.565 68.124 1.00 46.83 ? 503  MET A SD  1 
ATOM   3847  C  CE  . MET A  1 503 ? 40.655  60.321 68.633 1.00 42.93 ? 503  MET A CE  1 
ATOM   3848  N  N   . LEU A  1 504 ? 43.854  55.143 69.231 1.00 30.27 ? 504  LEU A N   1 
ATOM   3849  C  CA  . LEU A  1 504 ? 43.362  53.789 68.997 1.00 30.11 ? 504  LEU A CA  1 
ATOM   3850  C  C   . LEU A  1 504 ? 43.518  52.823 70.169 1.00 31.78 ? 504  LEU A C   1 
ATOM   3851  O  O   . LEU A  1 504 ? 42.918  51.739 70.176 1.00 30.77 ? 504  LEU A O   1 
ATOM   3852  C  CB  . LEU A  1 504 ? 44.017  53.211 67.739 1.00 28.04 ? 504  LEU A CB  1 
ATOM   3853  C  CG  . LEU A  1 504 ? 43.618  53.960 66.458 1.00 26.71 ? 504  LEU A CG  1 
ATOM   3854  C  CD1 . LEU A  1 504 ? 44.250  53.278 65.262 1.00 26.61 ? 504  LEU A CD1 1 
ATOM   3855  C  CD2 . LEU A  1 504 ? 42.103  53.988 66.322 1.00 24.49 ? 504  LEU A CD2 1 
ATOM   3856  N  N   . GLN A  1 505 ? 44.316  53.210 71.162 1.00 33.60 ? 505  GLN A N   1 
ATOM   3857  C  CA  . GLN A  1 505 ? 44.518  52.367 72.346 1.00 36.05 ? 505  GLN A CA  1 
ATOM   3858  C  C   . GLN A  1 505 ? 43.217  52.238 73.149 1.00 35.07 ? 505  GLN A C   1 
ATOM   3859  O  O   . GLN A  1 505 ? 43.003  51.255 73.839 1.00 34.13 ? 505  GLN A O   1 
ATOM   3860  C  CB  . GLN A  1 505 ? 45.615  52.962 73.249 1.00 38.76 ? 505  GLN A CB  1 
ATOM   3861  C  CG  . GLN A  1 505 ? 47.042  52.713 72.773 1.00 42.90 ? 505  GLN A CG  1 
ATOM   3862  C  CD  . GLN A  1 505 ? 48.108  53.303 73.709 1.00 46.44 ? 505  GLN A CD  1 
ATOM   3863  O  OE1 . GLN A  1 505 ? 49.314  53.204 73.435 1.00 47.23 ? 505  GLN A OE1 1 
ATOM   3864  N  NE2 . GLN A  1 505 ? 47.668  53.918 74.815 1.00 47.31 ? 505  GLN A NE2 1 
ATOM   3865  N  N   . ASN A  1 506 ? 42.358  53.247 73.052 1.00 35.29 ? 506  ASN A N   1 
ATOM   3866  C  CA  . ASN A  1 506 ? 41.087  53.244 73.768 1.00 35.66 ? 506  ASN A CA  1 
ATOM   3867  C  C   . ASN A  1 506 ? 39.963  52.636 72.936 1.00 33.84 ? 506  ASN A C   1 
ATOM   3868  O  O   . ASN A  1 506 ? 38.789  52.793 73.272 1.00 33.17 ? 506  ASN A O   1 
ATOM   3869  C  CB  . ASN A  1 506 ? 40.702  54.677 74.146 1.00 38.70 ? 506  ASN A CB  1 
ATOM   3870  C  CG  . ASN A  1 506 ? 41.826  55.411 74.845 1.00 42.63 ? 506  ASN A CG  1 
ATOM   3871  O  OD1 . ASN A  1 506 ? 42.196  55.077 75.976 1.00 45.31 ? 506  ASN A OD1 1 
ATOM   3872  N  ND2 . ASN A  1 506 ? 42.393  56.413 74.168 1.00 44.09 ? 506  ASN A ND2 1 
ATOM   3873  N  N   . VAL A  1 507 ? 40.313  51.949 71.851 1.00 32.17 ? 507  VAL A N   1 
ATOM   3874  C  CA  . VAL A  1 507 ? 39.302  51.347 70.979 1.00 30.26 ? 507  VAL A CA  1 
ATOM   3875  C  C   . VAL A  1 507 ? 39.535  49.857 70.784 1.00 29.89 ? 507  VAL A C   1 
ATOM   3876  O  O   . VAL A  1 507 ? 40.672  49.391 70.731 1.00 29.70 ? 507  VAL A O   1 
ATOM   3877  C  CB  . VAL A  1 507 ? 39.285  52.017 69.565 1.00 29.54 ? 507  VAL A CB  1 
ATOM   3878  C  CG1 . VAL A  1 507 ? 38.154  51.448 68.719 1.00 29.08 ? 507  VAL A CG1 1 
ATOM   3879  C  CG2 . VAL A  1 507 ? 39.111  53.518 69.693 1.00 29.30 ? 507  VAL A CG2 1 
ATOM   3880  N  N   . GLN A  1 508 ? 38.454  49.100 70.679 1.00 29.79 ? 508  GLN A N   1 
ATOM   3881  C  CA  . GLN A  1 508 ? 38.586  47.667 70.448 1.00 29.62 ? 508  GLN A CA  1 
ATOM   3882  C  C   . GLN A  1 508 ? 38.690  47.467 68.933 1.00 28.17 ? 508  GLN A C   1 
ATOM   3883  O  O   . GLN A  1 508 ? 37.682  47.278 68.255 1.00 28.05 ? 508  GLN A O   1 
ATOM   3884  C  CB  . GLN A  1 508 ? 37.362  46.927 70.988 1.00 31.55 ? 508  GLN A CB  1 
ATOM   3885  C  CG  . GLN A  1 508 ? 37.120  47.085 72.487 1.00 33.75 ? 508  GLN A CG  1 
ATOM   3886  C  CD  . GLN A  1 508 ? 35.908  46.294 72.945 1.00 35.78 ? 508  GLN A CD  1 
ATOM   3887  O  OE1 . GLN A  1 508 ? 35.865  45.066 72.799 1.00 37.81 ? 508  GLN A OE1 1 
ATOM   3888  N  NE2 . GLN A  1 508 ? 34.910  46.993 73.488 1.00 35.97 ? 508  GLN A NE2 1 
ATOM   3889  N  N   . MET A  1 509 ? 39.913  47.525 68.420 1.00 26.89 ? 509  MET A N   1 
ATOM   3890  C  CA  . MET A  1 509 ? 40.169  47.374 67.000 1.00 27.22 ? 509  MET A CA  1 
ATOM   3891  C  C   . MET A  1 509 ? 40.232  45.920 66.558 1.00 27.75 ? 509  MET A C   1 
ATOM   3892  O  O   . MET A  1 509 ? 40.721  45.056 67.294 1.00 27.86 ? 509  MET A O   1 
ATOM   3893  C  CB  . MET A  1 509 ? 41.492  48.048 66.620 1.00 27.51 ? 509  MET A CB  1 
ATOM   3894  C  CG  . MET A  1 509 ? 41.506  49.557 66.808 1.00 27.57 ? 509  MET A CG  1 
ATOM   3895  S  SD  . MET A  1 509 ? 40.248  50.344 65.789 1.00 31.04 ? 509  MET A SD  1 
ATOM   3896  C  CE  . MET A  1 509 ? 41.195  50.688 64.323 1.00 28.42 ? 509  MET A CE  1 
ATOM   3897  N  N   . PRO A  1 510 ? 39.731  45.631 65.339 1.00 27.34 ? 510  PRO A N   1 
ATOM   3898  C  CA  . PRO A  1 510 ? 39.737  44.277 64.779 1.00 26.39 ? 510  PRO A CA  1 
ATOM   3899  C  C   . PRO A  1 510 ? 41.171  43.982 64.350 1.00 25.92 ? 510  PRO A C   1 
ATOM   3900  O  O   . PRO A  1 510 ? 41.996  44.885 64.286 1.00 24.70 ? 510  PRO A O   1 
ATOM   3901  C  CB  . PRO A  1 510 ? 38.798  44.403 63.585 1.00 26.39 ? 510  PRO A CB  1 
ATOM   3902  C  CG  . PRO A  1 510 ? 39.117  45.783 63.080 1.00 26.91 ? 510  PRO A CG  1 
ATOM   3903  C  CD  . PRO A  1 510 ? 39.160  46.594 64.372 1.00 27.28 ? 510  PRO A CD  1 
ATOM   3904  N  N   . SER A  1 511 ? 41.463  42.724 64.063 1.00 25.92 ? 511  SER A N   1 
ATOM   3905  C  CA  . SER A  1 511 ? 42.800  42.344 63.626 1.00 26.37 ? 511  SER A CA  1 
ATOM   3906  C  C   . SER A  1 511 ? 42.725  41.858 62.184 1.00 26.62 ? 511  SER A C   1 
ATOM   3907  O  O   . SER A  1 511 ? 41.637  41.632 61.643 1.00 26.42 ? 511  SER A O   1 
ATOM   3908  C  CB  . SER A  1 511 ? 43.359  41.220 64.507 1.00 25.79 ? 511  SER A CB  1 
ATOM   3909  O  OG  . SER A  1 511 ? 42.497  40.097 64.484 1.00 27.63 ? 511  SER A OG  1 
ATOM   3910  N  N   . LYS A  1 512 ? 43.880  41.688 61.556 1.00 27.17 ? 512  LYS A N   1 
ATOM   3911  C  CA  . LYS A  1 512 ? 43.886  41.225 60.186 1.00 27.22 ? 512  LYS A CA  1 
ATOM   3912  C  C   . LYS A  1 512 ? 44.741  40.006 60.005 1.00 27.26 ? 512  LYS A C   1 
ATOM   3913  O  O   . LYS A  1 512 ? 45.890  39.975 60.413 1.00 28.27 ? 512  LYS A O   1 
ATOM   3914  C  CB  . LYS A  1 512 ? 44.374  42.324 59.252 1.00 25.97 ? 512  LYS A CB  1 
ATOM   3915  C  CG  . LYS A  1 512 ? 44.436  41.914 57.787 1.00 27.25 ? 512  LYS A CG  1 
ATOM   3916  C  CD  . LYS A  1 512 ? 44.511  43.181 56.949 1.00 28.21 ? 512  LYS A CD  1 
ATOM   3917  C  CE  . LYS A  1 512 ? 44.815  42.916 55.524 1.00 27.16 ? 512  LYS A CE  1 
ATOM   3918  N  NZ  . LYS A  1 512 ? 45.148  44.218 54.880 1.00 26.76 ? 512  LYS A NZ  1 
ATOM   3919  N  N   . LYS A  1 513 ? 44.159  38.994 59.384 1.00 27.81 ? 513  LYS A N   1 
ATOM   3920  C  CA  . LYS A  1 513 ? 44.874  37.774 59.107 1.00 27.17 ? 513  LYS A CA  1 
ATOM   3921  C  C   . LYS A  1 513 ? 45.069  37.707 57.605 1.00 26.72 ? 513  LYS A C   1 
ATOM   3922  O  O   . LYS A  1 513 ? 44.122  37.892 56.850 1.00 26.11 ? 513  LYS A O   1 
ATOM   3923  C  CB  . LYS A  1 513 ? 44.050  36.587 59.556 1.00 29.08 ? 513  LYS A CB  1 
ATOM   3924  C  CG  . LYS A  1 513 ? 44.680  35.252 59.247 1.00 32.05 ? 513  LYS A CG  1 
ATOM   3925  C  CD  . LYS A  1 513 ? 43.786  34.145 59.778 1.00 35.41 ? 513  LYS A CD  1 
ATOM   3926  C  CE  . LYS A  1 513 ? 44.520  32.823 59.873 1.00 37.92 ? 513  LYS A CE  1 
ATOM   3927  N  NZ  . LYS A  1 513 ? 43.706  31.902 60.726 1.00 41.66 ? 513  LYS A NZ  1 
ATOM   3928  N  N   . LEU A  1 514 ? 46.305  37.478 57.184 1.00 24.86 ? 514  LEU A N   1 
ATOM   3929  C  CA  . LEU A  1 514 ? 46.639  37.354 55.780 1.00 25.01 ? 514  LEU A CA  1 
ATOM   3930  C  C   . LEU A  1 514 ? 47.219  35.945 55.650 1.00 25.63 ? 514  LEU A C   1 
ATOM   3931  O  O   . LEU A  1 514 ? 48.192  35.606 56.318 1.00 24.63 ? 514  LEU A O   1 
ATOM   3932  C  CB  . LEU A  1 514 ? 47.687  38.398 55.381 1.00 24.96 ? 514  LEU A CB  1 
ATOM   3933  C  CG  . LEU A  1 514 ? 48.181  38.282 53.936 1.00 25.05 ? 514  LEU A CG  1 
ATOM   3934  C  CD1 . LEU A  1 514 ? 47.069  38.674 52.977 1.00 25.36 ? 514  LEU A CD1 1 
ATOM   3935  C  CD2 . LEU A  1 514 ? 49.376  39.192 53.741 1.00 26.17 ? 514  LEU A CD2 1 
ATOM   3936  N  N   . ASP A  1 515 ? 46.619  35.118 54.803 1.00 26.76 ? 515  ASP A N   1 
ATOM   3937  C  CA  . ASP A  1 515 ? 47.084  33.744 54.646 1.00 27.95 ? 515  ASP A CA  1 
ATOM   3938  C  C   . ASP A  1 515 ? 46.678  33.272 53.256 1.00 27.75 ? 515  ASP A C   1 
ATOM   3939  O  O   . ASP A  1 515 ? 46.241  34.075 52.439 1.00 27.18 ? 515  ASP A O   1 
ATOM   3940  C  CB  . ASP A  1 515 ? 46.412  32.871 55.705 1.00 30.51 ? 515  ASP A CB  1 
ATOM   3941  C  CG  . ASP A  1 515 ? 47.237  31.662 56.082 1.00 32.86 ? 515  ASP A CG  1 
ATOM   3942  O  OD1 . ASP A  1 515 ? 48.095  31.239 55.289 1.00 34.01 ? 515  ASP A OD1 1 
ATOM   3943  O  OD2 . ASP A  1 515 ? 47.008  31.122 57.180 1.00 36.89 ? 515  ASP A OD2 1 
ATOM   3944  N  N   . PHE A  1 516 ? 46.800  31.974 52.990 1.00 27.67 ? 516  PHE A N   1 
ATOM   3945  C  CA  . PHE A  1 516 ? 46.435  31.435 51.682 1.00 28.49 ? 516  PHE A CA  1 
ATOM   3946  C  C   . PHE A  1 516 ? 45.799  30.058 51.766 1.00 28.93 ? 516  PHE A C   1 
ATOM   3947  O  O   . PHE A  1 516 ? 45.857  29.403 52.797 1.00 29.42 ? 516  PHE A O   1 
ATOM   3948  C  CB  . PHE A  1 516 ? 47.673  31.345 50.778 1.00 28.35 ? 516  PHE A CB  1 
ATOM   3949  C  CG  . PHE A  1 516 ? 48.723  30.391 51.277 1.00 29.70 ? 516  PHE A CG  1 
ATOM   3950  C  CD1 . PHE A  1 516 ? 49.720  30.819 52.153 1.00 31.04 ? 516  PHE A CD1 1 
ATOM   3951  C  CD2 . PHE A  1 516 ? 48.711  29.053 50.881 1.00 30.39 ? 516  PHE A CD2 1 
ATOM   3952  C  CE1 . PHE A  1 516 ? 50.691  29.926 52.630 1.00 31.29 ? 516  PHE A CE1 1 
ATOM   3953  C  CE2 . PHE A  1 516 ? 49.673  28.152 51.349 1.00 29.74 ? 516  PHE A CE2 1 
ATOM   3954  C  CZ  . PHE A  1 516 ? 50.668  28.587 52.225 1.00 30.76 ? 516  PHE A CZ  1 
ATOM   3955  N  N   . ILE A  1 517 ? 45.167  29.639 50.679 1.00 29.31 ? 517  ILE A N   1 
ATOM   3956  C  CA  . ILE A  1 517 ? 44.585  28.313 50.599 1.00 31.33 ? 517  ILE A CA  1 
ATOM   3957  C  C   . ILE A  1 517 ? 45.136  27.775 49.291 1.00 32.68 ? 517  ILE A C   1 
ATOM   3958  O  O   . ILE A  1 517 ? 45.522  28.552 48.413 1.00 32.41 ? 517  ILE A O   1 
ATOM   3959  C  CB  . ILE A  1 517 ? 43.027  28.312 50.571 1.00 31.76 ? 517  ILE A CB  1 
ATOM   3960  C  CG1 . ILE A  1 517 ? 42.506  29.206 49.456 1.00 31.45 ? 517  ILE A CG1 1 
ATOM   3961  C  CG2 . ILE A  1 517 ? 42.482  28.737 51.932 1.00 30.47 ? 517  ILE A CG2 1 
ATOM   3962  C  CD1 . ILE A  1 517 ? 41.003  29.238 49.378 1.00 32.79 ? 517  ILE A CD1 1 
ATOM   3963  N  N   . ILE A  1 518 ? 45.207  26.456 49.169 1.00 34.85 ? 518  ILE A N   1 
ATOM   3964  C  CA  . ILE A  1 518 ? 45.741  25.849 47.961 1.00 37.09 ? 518  ILE A CA  1 
ATOM   3965  C  C   . ILE A  1 518 ? 44.622  25.262 47.129 1.00 38.65 ? 518  ILE A C   1 
ATOM   3966  O  O   . ILE A  1 518 ? 43.692  24.664 47.660 1.00 39.51 ? 518  ILE A O   1 
ATOM   3967  C  CB  . ILE A  1 518 ? 46.758  24.727 48.290 1.00 38.15 ? 518  ILE A CB  1 
ATOM   3968  C  CG1 . ILE A  1 518 ? 47.953  25.311 49.036 1.00 38.22 ? 518  ILE A CG1 1 
ATOM   3969  C  CG2 . ILE A  1 518 ? 47.239  24.048 47.010 1.00 37.94 ? 518  ILE A CG2 1 
ATOM   3970  C  CD1 . ILE A  1 518 ? 49.035  24.288 49.342 1.00 39.55 ? 518  ILE A CD1 1 
ATOM   3971  N  N   . LEU A  1 519 ? 44.707  25.467 45.821 1.00 39.90 ? 519  LEU A N   1 
ATOM   3972  C  CA  . LEU A  1 519 ? 43.730  24.944 44.870 1.00 40.31 ? 519  LEU A CA  1 
ATOM   3973  C  C   . LEU A  1 519 ? 44.594  24.428 43.734 1.00 41.55 ? 519  LEU A C   1 
ATOM   3974  O  O   . LEU A  1 519 ? 45.398  25.184 43.193 1.00 41.10 ? 519  LEU A O   1 
ATOM   3975  C  CB  . LEU A  1 519 ? 42.807  26.060 44.357 1.00 38.52 ? 519  LEU A CB  1 
ATOM   3976  C  CG  . LEU A  1 519 ? 41.840  26.683 45.361 1.00 38.30 ? 519  LEU A CG  1 
ATOM   3977  C  CD1 . LEU A  1 519 ? 41.054  27.819 44.710 1.00 36.13 ? 519  LEU A CD1 1 
ATOM   3978  C  CD2 . LEU A  1 519 ? 40.885  25.619 45.868 1.00 37.69 ? 519  LEU A CD2 1 
ATOM   3979  N  N   . ASN A  1 520 ? 44.458  23.146 43.399 1.00 42.71 ? 520  ASN A N   1 
ATOM   3980  C  CA  . ASN A  1 520 ? 45.238  22.549 42.320 1.00 44.60 ? 520  ASN A CA  1 
ATOM   3981  C  C   . ASN A  1 520 ? 46.710  22.916 42.316 1.00 44.53 ? 520  ASN A C   1 
ATOM   3982  O  O   . ASN A  1 520 ? 47.217  23.458 41.326 1.00 45.03 ? 520  ASN A O   1 
ATOM   3983  C  CB  . ASN A  1 520 ? 44.652  22.929 40.962 1.00 46.99 ? 520  ASN A CB  1 
ATOM   3984  C  CG  . ASN A  1 520 ? 43.603  21.956 40.492 1.00 50.79 ? 520  ASN A CG  1 
ATOM   3985  O  OD1 . ASN A  1 520 ? 42.783  21.477 41.281 1.00 52.67 ? 520  ASN A OD1 1 
ATOM   3986  N  ND2 . ASN A  1 520 ? 43.600  21.688 39.191 1.00 54.00 ? 520  ASN A ND2 1 
ATOM   3987  N  N   . GLU A  1 521 ? 47.399  22.620 43.407 1.00 44.30 ? 521  GLU A N   1 
ATOM   3988  C  CA  . GLU A  1 521 ? 48.827  22.918 43.508 1.00 44.77 ? 521  GLU A CA  1 
ATOM   3989  C  C   . GLU A  1 521 ? 49.152  24.405 43.520 1.00 42.56 ? 521  GLU A C   1 
ATOM   3990  O  O   . GLU A  1 521 ? 50.319  24.773 43.638 1.00 43.21 ? 521  GLU A O   1 
ATOM   3991  C  CB  . GLU A  1 521 ? 49.610  22.247 42.360 1.00 47.73 ? 521  GLU A CB  1 
ATOM   3992  C  CG  . GLU A  1 521 ? 49.723  20.716 42.451 1.00 51.35 ? 521  GLU A CG  1 
ATOM   3993  C  CD  . GLU A  1 521 ? 48.372  20.022 42.405 1.00 53.83 ? 521  GLU A CD  1 
ATOM   3994  O  OE1 . GLU A  1 521 ? 47.636  20.201 41.402 1.00 55.23 ? 521  GLU A OE1 1 
ATOM   3995  O  OE2 . GLU A  1 521 ? 48.043  19.289 43.371 1.00 55.26 ? 521  GLU A OE2 1 
ATOM   3996  N  N   . THR A  1 522 ? 48.147  25.269 43.388 1.00 39.87 ? 522  THR A N   1 
ATOM   3997  C  CA  . THR A  1 522 ? 48.425  26.707 43.399 1.00 36.91 ? 522  THR A CA  1 
ATOM   3998  C  C   . THR A  1 522 ? 47.900  27.400 44.644 1.00 35.51 ? 522  THR A C   1 
ATOM   3999  O  O   . THR A  1 522 ? 46.757  27.181 45.052 1.00 34.73 ? 522  THR A O   1 
ATOM   4000  C  CB  . THR A  1 522 ? 47.814  27.421 42.183 1.00 36.94 ? 522  THR A CB  1 
ATOM   4001  O  OG1 . THR A  1 522 ? 48.458  26.964 40.990 1.00 38.10 ? 522  THR A OG1 1 
ATOM   4002  C  CG2 . THR A  1 522 ? 48.020  28.923 42.292 1.00 35.99 ? 522  THR A CG2 1 
ATOM   4003  N  N   . LYS A  1 523 ? 48.726  28.234 45.266 1.00 32.93 ? 523  LYS A N   1 
ATOM   4004  C  CA  . LYS A  1 523 ? 48.230  28.940 46.428 1.00 33.25 ? 523  LYS A CA  1 
ATOM   4005  C  C   . LYS A  1 523 ? 47.574  30.247 46.017 1.00 30.82 ? 523  LYS A C   1 
ATOM   4006  O  O   . LYS A  1 523 ? 48.020  30.917 45.084 1.00 32.31 ? 523  LYS A O   1 
ATOM   4007  C  CB  . LYS A  1 523 ? 49.346  29.192 47.446 1.00 35.55 ? 523  LYS A CB  1 
ATOM   4008  C  CG  . LYS A  1 523 ? 50.520  29.935 46.917 1.00 38.89 ? 523  LYS A CG  1 
ATOM   4009  C  CD  . LYS A  1 523 ? 51.783  29.509 47.655 1.00 40.57 ? 523  LYS A CD  1 
ATOM   4010  C  CE  . LYS A  1 523 ? 51.801  29.990 49.089 1.00 42.13 ? 523  LYS A CE  1 
ATOM   4011  N  NZ  . LYS A  1 523 ? 53.117  29.643 49.709 1.00 43.65 ? 523  LYS A NZ  1 
ATOM   4012  N  N   . PHE A  1 524 ? 46.480  30.573 46.695 1.00 27.27 ? 524  PHE A N   1 
ATOM   4013  C  CA  . PHE A  1 524 ? 45.742  31.809 46.453 1.00 24.60 ? 524  PHE A CA  1 
ATOM   4014  C  C   . PHE A  1 524 ? 45.582  32.446 47.828 1.00 23.29 ? 524  PHE A C   1 
ATOM   4015  O  O   . PHE A  1 524 ? 45.234  31.765 48.801 1.00 21.83 ? 524  PHE A O   1 
ATOM   4016  C  CB  . PHE A  1 524 ? 44.377  31.523 45.814 1.00 23.15 ? 524  PHE A CB  1 
ATOM   4017  C  CG  . PHE A  1 524 ? 44.471  30.986 44.412 1.00 23.52 ? 524  PHE A CG  1 
ATOM   4018  C  CD1 . PHE A  1 524 ? 44.541  29.611 44.180 1.00 23.57 ? 524  PHE A CD1 1 
ATOM   4019  C  CD2 . PHE A  1 524 ? 44.557  31.860 43.320 1.00 22.61 ? 524  PHE A CD2 1 
ATOM   4020  C  CE1 . PHE A  1 524 ? 44.704  29.111 42.875 1.00 23.52 ? 524  PHE A CE1 1 
ATOM   4021  C  CE2 . PHE A  1 524 ? 44.718  31.377 42.020 1.00 24.44 ? 524  PHE A CE2 1 
ATOM   4022  C  CZ  . PHE A  1 524 ? 44.795  29.996 41.788 1.00 23.41 ? 524  PHE A CZ  1 
ATOM   4023  N  N   . TRP A  1 525 ? 45.850  33.744 47.902 1.00 19.61 ? 525  TRP A N   1 
ATOM   4024  C  CA  . TRP A  1 525 ? 45.792  34.472 49.165 1.00 18.76 ? 525  TRP A CA  1 
ATOM   4025  C  C   . TRP A  1 525 ? 44.441  35.117 49.488 1.00 18.63 ? 525  TRP A C   1 
ATOM   4026  O  O   . TRP A  1 525 ? 43.685  35.512 48.599 1.00 17.98 ? 525  TRP A O   1 
ATOM   4027  C  CB  . TRP A  1 525 ? 46.881  35.572 49.181 1.00 17.17 ? 525  TRP A CB  1 
ATOM   4028  C  CG  . TRP A  1 525 ? 48.294  35.038 49.144 1.00 17.55 ? 525  TRP A CG  1 
ATOM   4029  C  CD1 . TRP A  1 525 ? 48.936  34.477 48.078 1.00 14.99 ? 525  TRP A CD1 1 
ATOM   4030  C  CD2 . TRP A  1 525 ? 49.202  34.949 50.255 1.00 16.96 ? 525  TRP A CD2 1 
ATOM   4031  N  NE1 . TRP A  1 525 ? 50.185  34.036 48.460 1.00 17.22 ? 525  TRP A NE1 1 
ATOM   4032  C  CE2 . TRP A  1 525 ? 50.373  34.315 49.789 1.00 17.19 ? 525  TRP A CE2 1 
ATOM   4033  C  CE3 . TRP A  1 525 ? 49.134  35.347 51.602 1.00 19.07 ? 525  TRP A CE3 1 
ATOM   4034  C  CZ2 . TRP A  1 525 ? 51.481  34.064 50.624 1.00 18.36 ? 525  TRP A CZ2 1 
ATOM   4035  C  CZ3 . TRP A  1 525 ? 50.248  35.097 52.446 1.00 18.09 ? 525  TRP A CZ3 1 
ATOM   4036  C  CH2 . TRP A  1 525 ? 51.396  34.463 51.946 1.00 17.93 ? 525  TRP A CH2 1 
ATOM   4037  N  N   . TYR A  1 526 ? 44.164  35.224 50.781 1.00 18.55 ? 526  TYR A N   1 
ATOM   4038  C  CA  . TYR A  1 526 ? 42.961  35.862 51.277 1.00 18.16 ? 526  TYR A CA  1 
ATOM   4039  C  C   . TYR A  1 526 ? 43.345  36.602 52.542 1.00 17.64 ? 526  TYR A C   1 
ATOM   4040  O  O   . TYR A  1 526 ? 44.419  36.394 53.102 1.00 17.05 ? 526  TYR A O   1 
ATOM   4041  C  CB  . TYR A  1 526 ? 41.878  34.838 51.616 1.00 19.48 ? 526  TYR A CB  1 
ATOM   4042  C  CG  . TYR A  1 526 ? 42.210  33.943 52.794 1.00 22.76 ? 526  TYR A CG  1 
ATOM   4043  C  CD1 . TYR A  1 526 ? 41.942  34.335 54.111 1.00 25.55 ? 526  TYR A CD1 1 
ATOM   4044  C  CD2 . TYR A  1 526 ? 42.759  32.689 52.586 1.00 25.15 ? 526  TYR A CD2 1 
ATOM   4045  C  CE1 . TYR A  1 526 ? 42.210  33.482 55.192 1.00 26.35 ? 526  TYR A CE1 1 
ATOM   4046  C  CE2 . TYR A  1 526 ? 43.035  31.832 53.642 1.00 27.51 ? 526  TYR A CE2 1 
ATOM   4047  C  CZ  . TYR A  1 526 ? 42.757  32.225 54.938 1.00 28.19 ? 526  TYR A CZ  1 
ATOM   4048  O  OH  . TYR A  1 526 ? 43.022  31.348 55.962 1.00 30.69 ? 526  TYR A OH  1 
ATOM   4049  N  N   . GLN A  1 527 ? 42.454  37.470 52.992 1.00 17.14 ? 527  GLN A N   1 
ATOM   4050  C  CA  . GLN A  1 527 ? 42.683  38.186 54.223 1.00 17.58 ? 527  GLN A CA  1 
ATOM   4051  C  C   . GLN A  1 527 ? 41.359  38.208 54.929 1.00 17.82 ? 527  GLN A C   1 
ATOM   4052  O  O   . GLN A  1 527 ? 40.303  38.163 54.295 1.00 18.48 ? 527  GLN A O   1 
ATOM   4053  C  CB  . GLN A  1 527 ? 43.167  39.625 53.978 1.00 17.18 ? 527  GLN A CB  1 
ATOM   4054  C  CG  . GLN A  1 527 ? 42.233  40.515 53.170 1.00 16.45 ? 527  GLN A CG  1 
ATOM   4055  C  CD  . GLN A  1 527 ? 42.676  41.979 53.194 1.00 19.23 ? 527  GLN A CD  1 
ATOM   4056  O  OE1 . GLN A  1 527 ? 43.850  42.293 52.934 1.00 16.79 ? 527  GLN A OE1 1 
ATOM   4057  N  NE2 . GLN A  1 527 ? 41.735  42.884 53.505 1.00 15.66 ? 527  GLN A NE2 1 
ATOM   4058  N  N   . MET A  1 528 ? 41.401  38.248 56.247 1.00 17.41 ? 528  MET A N   1 
ATOM   4059  C  CA  . MET A  1 528 ? 40.164  38.323 57.006 1.00 19.80 ? 528  MET A CA  1 
ATOM   4060  C  C   . MET A  1 528 ? 40.306  39.425 58.042 1.00 19.43 ? 528  MET A C   1 
ATOM   4061  O  O   . MET A  1 528 ? 41.340  39.524 58.705 1.00 20.40 ? 528  MET A O   1 
ATOM   4062  C  CB  . MET A  1 528 ? 39.871  37.001 57.736 1.00 19.43 ? 528  MET A CB  1 
ATOM   4063  C  CG  . MET A  1 528 ? 39.435  35.858 56.864 1.00 19.77 ? 528  MET A CG  1 
ATOM   4064  S  SD  . MET A  1 528 ? 38.949  34.464 57.924 1.00 25.41 ? 528  MET A SD  1 
ATOM   4065  C  CE  . MET A  1 528 ? 38.487  33.232 56.676 1.00 22.79 ? 528  MET A CE  1 
ATOM   4066  N  N   . ILE A  1 529 ? 39.286  40.265 58.153 1.00 19.32 ? 529  ILE A N   1 
ATOM   4067  C  CA  . ILE A  1 529 ? 39.284  41.298 59.169 1.00 19.38 ? 529  ILE A CA  1 
ATOM   4068  C  C   . ILE A  1 529 ? 38.503  40.617 60.281 1.00 20.23 ? 529  ILE A C   1 
ATOM   4069  O  O   . ILE A  1 529 ? 37.304  40.346 60.152 1.00 19.73 ? 529  ILE A O   1 
ATOM   4070  C  CB  . ILE A  1 529 ? 38.558  42.566 58.703 1.00 18.49 ? 529  ILE A CB  1 
ATOM   4071  C  CG1 . ILE A  1 529 ? 39.227  43.096 57.429 1.00 17.82 ? 529  ILE A CG1 1 
ATOM   4072  C  CG2 . ILE A  1 529 ? 38.582  43.628 59.815 1.00 16.27 ? 529  ILE A CG2 1 
ATOM   4073  C  CD1 . ILE A  1 529 ? 40.664  43.494 57.606 1.00 15.48 ? 529  ILE A CD1 1 
ATOM   4074  N  N   . LEU A  1 530 ? 39.197  40.301 61.363 1.00 22.97 ? 530  LEU A N   1 
ATOM   4075  C  CA  . LEU A  1 530 ? 38.577  39.582 62.474 1.00 23.13 ? 530  LEU A CA  1 
ATOM   4076  C  C   . LEU A  1 530 ? 38.142  40.504 63.577 1.00 23.98 ? 530  LEU A C   1 
ATOM   4077  O  O   . LEU A  1 530 ? 38.830  41.477 63.872 1.00 25.17 ? 530  LEU A O   1 
ATOM   4078  C  CB  . LEU A  1 530 ? 39.562  38.566 63.029 1.00 23.12 ? 530  LEU A CB  1 
ATOM   4079  C  CG  . LEU A  1 530 ? 40.129  37.591 62.004 1.00 22.38 ? 530  LEU A CG  1 
ATOM   4080  C  CD1 . LEU A  1 530 ? 41.344  36.832 62.589 1.00 23.34 ? 530  LEU A CD1 1 
ATOM   4081  C  CD2 . LEU A  1 530 ? 39.025  36.627 61.596 1.00 21.09 ? 530  LEU A CD2 1 
ATOM   4082  N  N   . PRO A  1 531 ? 36.982  40.221 64.196 1.00 24.93 ? 531  PRO A N   1 
ATOM   4083  C  CA  . PRO A  1 531 ? 36.474  41.056 65.289 1.00 26.07 ? 531  PRO A CA  1 
ATOM   4084  C  C   . PRO A  1 531 ? 37.382  41.036 66.526 1.00 27.73 ? 531  PRO A C   1 
ATOM   4085  O  O   . PRO A  1 531 ? 38.224  40.143 66.686 1.00 26.05 ? 531  PRO A O   1 
ATOM   4086  C  CB  . PRO A  1 531 ? 35.109  40.433 65.600 1.00 25.48 ? 531  PRO A CB  1 
ATOM   4087  C  CG  . PRO A  1 531 ? 34.678  39.866 64.275 1.00 24.64 ? 531  PRO A CG  1 
ATOM   4088  C  CD  . PRO A  1 531 ? 35.957  39.260 63.747 1.00 23.97 ? 531  PRO A CD  1 
ATOM   4089  N  N   . PRO A  1 532 ? 37.227  42.038 67.411 1.00 28.98 ? 532  PRO A N   1 
ATOM   4090  C  CA  . PRO A  1 532 ? 38.026  42.117 68.643 1.00 31.36 ? 532  PRO A CA  1 
ATOM   4091  C  C   . PRO A  1 532 ? 37.852  40.812 69.441 1.00 32.60 ? 532  PRO A C   1 
ATOM   4092  O  O   . PRO A  1 532 ? 36.824  40.137 69.323 1.00 34.07 ? 532  PRO A O   1 
ATOM   4093  C  CB  . PRO A  1 532 ? 37.406  43.307 69.383 1.00 31.31 ? 532  PRO A CB  1 
ATOM   4094  C  CG  . PRO A  1 532 ? 36.923  44.197 68.265 1.00 30.62 ? 532  PRO A CG  1 
ATOM   4095  C  CD  . PRO A  1 532 ? 36.343  43.211 67.266 1.00 29.52 ? 532  PRO A CD  1 
ATOM   4096  N  N   . HIS A  1 533 ? 38.844  40.451 70.244 1.00 33.40 ? 533  HIS A N   1 
ATOM   4097  C  CA  . HIS A  1 533 ? 38.747  39.236 71.058 1.00 34.12 ? 533  HIS A CA  1 
ATOM   4098  C  C   . HIS A  1 533 ? 38.227  38.045 70.258 1.00 34.67 ? 533  HIS A C   1 
ATOM   4099  O  O   . HIS A  1 533 ? 37.419  37.252 70.751 1.00 34.72 ? 533  HIS A O   1 
ATOM   4100  C  CB  . HIS A  1 533 ? 37.817  39.492 72.235 1.00 34.57 ? 533  HIS A CB  1 
ATOM   4101  C  CG  . HIS A  1 533 ? 38.075  40.796 72.921 1.00 37.06 ? 533  HIS A CG  1 
ATOM   4102  N  ND1 . HIS A  1 533 ? 39.271  41.084 73.547 1.00 38.52 ? 533  HIS A ND1 1 
ATOM   4103  C  CD2 . HIS A  1 533 ? 37.298  41.894 73.068 1.00 37.46 ? 533  HIS A CD2 1 
ATOM   4104  C  CE1 . HIS A  1 533 ? 39.218  42.305 74.053 1.00 38.36 ? 533  HIS A CE1 1 
ATOM   4105  N  NE2 . HIS A  1 533 ? 38.032  42.818 73.778 1.00 39.31 ? 533  HIS A NE2 1 
ATOM   4106  N  N   . PHE A  1 534 ? 38.680  37.921 69.017 1.00 34.26 ? 534  PHE A N   1 
ATOM   4107  C  CA  . PHE A  1 534 ? 38.246  36.810 68.183 1.00 34.03 ? 534  PHE A CA  1 
ATOM   4108  C  C   . PHE A  1 534 ? 38.320  35.482 68.944 1.00 34.41 ? 534  PHE A C   1 
ATOM   4109  O  O   . PHE A  1 534 ? 39.350  35.154 69.528 1.00 35.76 ? 534  PHE A O   1 
ATOM   4110  C  CB  . PHE A  1 534 ? 39.117  36.707 66.936 1.00 32.11 ? 534  PHE A CB  1 
ATOM   4111  C  CG  . PHE A  1 534 ? 38.665  35.640 65.996 1.00 32.31 ? 534  PHE A CG  1 
ATOM   4112  C  CD1 . PHE A  1 534 ? 37.475  35.777 65.294 1.00 31.77 ? 534  PHE A CD1 1 
ATOM   4113  C  CD2 . PHE A  1 534 ? 39.397  34.474 65.851 1.00 33.11 ? 534  PHE A CD2 1 
ATOM   4114  C  CE1 . PHE A  1 534 ? 37.016  34.762 64.465 1.00 32.35 ? 534  PHE A CE1 1 
ATOM   4115  C  CE2 . PHE A  1 534 ? 38.942  33.447 65.018 1.00 34.05 ? 534  PHE A CE2 1 
ATOM   4116  C  CZ  . PHE A  1 534 ? 37.748  33.599 64.326 1.00 31.98 ? 534  PHE A CZ  1 
ATOM   4117  N  N   . ASP A  1 535 ? 37.239  34.709 68.906 1.00 35.22 ? 535  ASP A N   1 
ATOM   4118  C  CA  . ASP A  1 535 ? 37.169  33.414 69.593 1.00 35.00 ? 535  ASP A CA  1 
ATOM   4119  C  C   . ASP A  1 535 ? 36.859  32.300 68.586 1.00 35.52 ? 535  ASP A C   1 
ATOM   4120  O  O   . ASP A  1 535 ? 35.707  32.116 68.200 1.00 35.38 ? 535  ASP A O   1 
ATOM   4121  C  CB  . ASP A  1 535 ? 36.076  33.480 70.660 1.00 34.86 ? 535  ASP A CB  1 
ATOM   4122  C  CG  . ASP A  1 535 ? 35.976  32.204 71.494 1.00 36.61 ? 535  ASP A CG  1 
ATOM   4123  O  OD1 . ASP A  1 535 ? 35.199  32.222 72.468 1.00 36.97 ? 535  ASP A OD1 1 
ATOM   4124  O  OD2 . ASP A  1 535 ? 36.657  31.193 71.187 1.00 35.66 ? 535  ASP A OD2 1 
ATOM   4125  N  N   . LYS A  1 536 ? 37.888  31.564 68.171 1.00 36.23 ? 536  LYS A N   1 
ATOM   4126  C  CA  . LYS A  1 536 ? 37.746  30.482 67.195 1.00 38.18 ? 536  LYS A CA  1 
ATOM   4127  C  C   . LYS A  1 536 ? 36.775  29.366 67.577 1.00 38.88 ? 536  LYS A C   1 
ATOM   4128  O  O   . LYS A  1 536 ? 36.536  28.460 66.778 1.00 38.92 ? 536  LYS A O   1 
ATOM   4129  C  CB  . LYS A  1 536 ? 39.111  29.871 66.898 1.00 40.17 ? 536  LYS A CB  1 
ATOM   4130  C  CG  . LYS A  1 536 ? 39.988  29.754 68.141 1.00 43.27 ? 536  LYS A CG  1 
ATOM   4131  C  CD  . LYS A  1 536 ? 41.316  29.032 67.875 1.00 44.88 ? 536  LYS A CD  1 
ATOM   4132  C  CE  . LYS A  1 536 ? 41.141  27.512 67.870 1.00 46.17 ? 536  LYS A CE  1 
ATOM   4133  N  NZ  . LYS A  1 536 ? 42.456  26.771 67.855 1.00 47.23 ? 536  LYS A NZ  1 
ATOM   4134  N  N   . SER A  1 537 ? 36.211  29.437 68.782 1.00 39.32 ? 537  SER A N   1 
ATOM   4135  C  CA  . SER A  1 537 ? 35.269  28.429 69.238 1.00 39.63 ? 537  SER A CA  1 
ATOM   4136  C  C   . SER A  1 537 ? 33.829  28.898 69.024 1.00 40.59 ? 537  SER A C   1 
ATOM   4137  O  O   . SER A  1 537 ? 32.875  28.199 69.388 1.00 41.33 ? 537  SER A O   1 
ATOM   4138  C  CB  . SER A  1 537 ? 35.498  28.101 70.722 1.00 39.11 ? 537  SER A CB  1 
ATOM   4139  O  OG  . SER A  1 537 ? 34.923  29.082 71.576 1.00 39.75 ? 537  SER A OG  1 
ATOM   4140  N  N   . LYS A  1 538 ? 33.673  30.086 68.445 1.00 40.30 ? 538  LYS A N   1 
ATOM   4141  C  CA  . LYS A  1 538 ? 32.345  30.647 68.166 1.00 39.26 ? 538  LYS A CA  1 
ATOM   4142  C  C   . LYS A  1 538 ? 32.117  30.736 66.660 1.00 38.15 ? 538  LYS A C   1 
ATOM   4143  O  O   . LYS A  1 538 ? 33.075  30.734 65.886 1.00 38.33 ? 538  LYS A O   1 
ATOM   4144  C  CB  . LYS A  1 538 ? 32.224  32.037 68.791 1.00 40.04 ? 538  LYS A CB  1 
ATOM   4145  C  CG  . LYS A  1 538 ? 32.213  32.011 70.311 1.00 42.91 ? 538  LYS A CG  1 
ATOM   4146  C  CD  . LYS A  1 538 ? 31.993  33.394 70.899 1.00 45.00 ? 538  LYS A CD  1 
ATOM   4147  C  CE  . LYS A  1 538 ? 31.377  33.295 72.291 1.00 46.57 ? 538  LYS A CE  1 
ATOM   4148  N  NZ  . LYS A  1 538 ? 30.073  32.550 72.260 1.00 48.19 ? 538  LYS A NZ  1 
ATOM   4149  N  N   . LYS A  1 539 ? 30.853  30.803 66.249 1.00 36.66 ? 539  LYS A N   1 
ATOM   4150  C  CA  . LYS A  1 539 ? 30.501  30.899 64.833 1.00 35.01 ? 539  LYS A CA  1 
ATOM   4151  C  C   . LYS A  1 539 ? 30.199  32.357 64.481 1.00 33.04 ? 539  LYS A C   1 
ATOM   4152  O  O   . LYS A  1 539 ? 29.258  32.944 65.006 1.00 33.34 ? 539  LYS A O   1 
ATOM   4153  C  CB  . LYS A  1 539 ? 29.270  30.048 64.534 1.00 37.13 ? 539  LYS A CB  1 
ATOM   4154  C  CG  . LYS A  1 539 ? 29.406  28.583 64.919 1.00 39.59 ? 539  LYS A CG  1 
ATOM   4155  C  CD  . LYS A  1 539 ? 30.540  27.916 64.166 1.00 41.24 ? 539  LYS A CD  1 
ATOM   4156  C  CE  . LYS A  1 539 ? 30.518  26.416 64.386 1.00 42.93 ? 539  LYS A CE  1 
ATOM   4157  N  NZ  . LYS A  1 539 ? 29.187  25.854 63.980 1.00 43.74 ? 539  LYS A NZ  1 
ATOM   4158  N  N   . TYR A  1 540 ? 30.997  32.950 63.599 1.00 30.05 ? 540  TYR A N   1 
ATOM   4159  C  CA  . TYR A  1 540 ? 30.779  34.349 63.221 1.00 26.61 ? 540  TYR A CA  1 
ATOM   4160  C  C   . TYR A  1 540 ? 30.163  34.489 61.827 1.00 24.48 ? 540  TYR A C   1 
ATOM   4161  O  O   . TYR A  1 540 ? 30.417  33.672 60.936 1.00 23.89 ? 540  TYR A O   1 
ATOM   4162  C  CB  . TYR A  1 540 ? 32.109  35.109 63.216 1.00 26.77 ? 540  TYR A CB  1 
ATOM   4163  C  CG  . TYR A  1 540 ? 32.803  35.247 64.553 1.00 25.69 ? 540  TYR A CG  1 
ATOM   4164  C  CD1 . TYR A  1 540 ? 32.639  36.394 65.321 1.00 25.67 ? 540  TYR A CD1 1 
ATOM   4165  C  CD2 . TYR A  1 540 ? 33.625  34.231 65.050 1.00 25.82 ? 540  TYR A CD2 1 
ATOM   4166  C  CE1 . TYR A  1 540 ? 33.274  36.538 66.557 1.00 26.45 ? 540  TYR A CE1 1 
ATOM   4167  C  CE2 . TYR A  1 540 ? 34.263  34.359 66.288 1.00 26.27 ? 540  TYR A CE2 1 
ATOM   4168  C  CZ  . TYR A  1 540 ? 34.086  35.505 67.033 1.00 27.56 ? 540  TYR A CZ  1 
ATOM   4169  O  OH  . TYR A  1 540 ? 34.705  35.634 68.253 1.00 28.79 ? 540  TYR A OH  1 
ATOM   4170  N  N   . PRO A  1 541 ? 29.293  35.490 61.634 1.00 22.46 ? 541  PRO A N   1 
ATOM   4171  C  CA  . PRO A  1 541 ? 28.731  35.638 60.285 1.00 20.86 ? 541  PRO A CA  1 
ATOM   4172  C  C   . PRO A  1 541 ? 29.922  36.089 59.418 1.00 20.46 ? 541  PRO A C   1 
ATOM   4173  O  O   . PRO A  1 541 ? 30.918  36.585 59.945 1.00 17.85 ? 541  PRO A O   1 
ATOM   4174  C  CB  . PRO A  1 541 ? 27.696  36.744 60.452 1.00 19.87 ? 541  PRO A CB  1 
ATOM   4175  C  CG  . PRO A  1 541 ? 28.215  37.539 61.652 1.00 22.22 ? 541  PRO A CG  1 
ATOM   4176  C  CD  . PRO A  1 541 ? 28.662  36.431 62.577 1.00 22.93 ? 541  PRO A CD  1 
ATOM   4177  N  N   . LEU A  1 542 ? 29.841  35.910 58.109 1.00 19.54 ? 542  LEU A N   1 
ATOM   4178  C  CA  . LEU A  1 542 ? 30.964  36.310 57.275 1.00 19.95 ? 542  LEU A CA  1 
ATOM   4179  C  C   . LEU A  1 542 ? 30.550  37.061 56.007 1.00 19.14 ? 542  LEU A C   1 
ATOM   4180  O  O   . LEU A  1 542 ? 29.690  36.604 55.252 1.00 18.35 ? 542  LEU A O   1 
ATOM   4181  C  CB  . LEU A  1 542 ? 31.808  35.078 56.902 1.00 18.84 ? 542  LEU A CB  1 
ATOM   4182  C  CG  . LEU A  1 542 ? 33.145  35.443 56.223 1.00 20.70 ? 542  LEU A CG  1 
ATOM   4183  C  CD1 . LEU A  1 542 ? 34.224  34.476 56.638 1.00 21.69 ? 542  LEU A CD1 1 
ATOM   4184  C  CD2 . LEU A  1 542 ? 32.977  35.465 54.711 1.00 21.25 ? 542  LEU A CD2 1 
ATOM   4185  N  N   . LEU A  1 543 ? 31.169  38.222 55.800 1.00 18.80 ? 543  LEU A N   1 
ATOM   4186  C  CA  . LEU A  1 543 ? 30.934  39.061 54.623 1.00 17.90 ? 543  LEU A CA  1 
ATOM   4187  C  C   . LEU A  1 543 ? 32.148  38.991 53.683 1.00 18.66 ? 543  LEU A C   1 
ATOM   4188  O  O   . LEU A  1 543 ? 33.272  39.352 54.061 1.00 19.63 ? 543  LEU A O   1 
ATOM   4189  C  CB  . LEU A  1 543 ? 30.685  40.519 55.040 1.00 16.99 ? 543  LEU A CB  1 
ATOM   4190  C  CG  . LEU A  1 543 ? 30.491  41.539 53.900 1.00 18.26 ? 543  LEU A CG  1 
ATOM   4191  C  CD1 . LEU A  1 543 ? 29.241  41.196 53.080 1.00 16.38 ? 543  LEU A CD1 1 
ATOM   4192  C  CD2 . LEU A  1 543 ? 30.403  42.941 54.463 1.00 16.38 ? 543  LEU A CD2 1 
ATOM   4193  N  N   . LEU A  1 544 ? 31.929  38.490 52.469 1.00 17.99 ? 544  LEU A N   1 
ATOM   4194  C  CA  . LEU A  1 544 ? 32.999  38.400 51.489 1.00 18.34 ? 544  LEU A CA  1 
ATOM   4195  C  C   . LEU A  1 544 ? 33.047  39.731 50.717 1.00 18.12 ? 544  LEU A C   1 
ATOM   4196  O  O   . LEU A  1 544 ? 32.124  40.060 49.972 1.00 18.19 ? 544  LEU A O   1 
ATOM   4197  C  CB  . LEU A  1 544 ? 32.744  37.237 50.516 1.00 17.56 ? 544  LEU A CB  1 
ATOM   4198  C  CG  . LEU A  1 544 ? 33.889  36.943 49.538 1.00 18.20 ? 544  LEU A CG  1 
ATOM   4199  C  CD1 . LEU A  1 544 ? 35.162  36.638 50.324 1.00 17.50 ? 544  LEU A CD1 1 
ATOM   4200  C  CD2 . LEU A  1 544 ? 33.529  35.756 48.632 1.00 18.67 ? 544  LEU A CD2 1 
ATOM   4201  N  N   . ASP A  1 545 ? 34.105  40.500 50.940 1.00 18.41 ? 545  ASP A N   1 
ATOM   4202  C  CA  . ASP A  1 545 ? 34.318  41.784 50.271 1.00 17.35 ? 545  ASP A CA  1 
ATOM   4203  C  C   . ASP A  1 545 ? 35.110  41.450 48.998 1.00 17.09 ? 545  ASP A C   1 
ATOM   4204  O  O   . ASP A  1 545 ? 36.260  41.028 49.068 1.00 14.36 ? 545  ASP A O   1 
ATOM   4205  C  CB  . ASP A  1 545 ? 35.146  42.711 51.173 1.00 17.87 ? 545  ASP A CB  1 
ATOM   4206  C  CG  . ASP A  1 545 ? 35.515  44.036 50.489 1.00 20.35 ? 545  ASP A CG  1 
ATOM   4207  O  OD1 . ASP A  1 545 ? 35.366  44.160 49.243 1.00 20.20 ? 545  ASP A OD1 1 
ATOM   4208  O  OD2 . ASP A  1 545 ? 35.966  44.953 51.205 1.00 20.86 ? 545  ASP A OD2 1 
ATOM   4209  N  N   . VAL A  1 546 ? 34.493  41.634 47.840 1.00 17.08 ? 546  VAL A N   1 
ATOM   4210  C  CA  . VAL A  1 546 ? 35.172  41.291 46.606 1.00 18.95 ? 546  VAL A CA  1 
ATOM   4211  C  C   . VAL A  1 546 ? 35.278  42.377 45.556 1.00 17.98 ? 546  VAL A C   1 
ATOM   4212  O  O   . VAL A  1 546 ? 34.437  43.272 45.480 1.00 17.15 ? 546  VAL A O   1 
ATOM   4213  C  CB  . VAL A  1 546 ? 34.478  40.080 45.924 1.00 21.70 ? 546  VAL A CB  1 
ATOM   4214  C  CG1 . VAL A  1 546 ? 32.993  40.359 45.792 1.00 21.91 ? 546  VAL A CG1 1 
ATOM   4215  C  CG2 . VAL A  1 546 ? 35.061  39.824 44.547 1.00 21.28 ? 546  VAL A CG2 1 
ATOM   4216  N  N   . TYR A  1 547 ? 36.352  42.300 44.774 1.00 16.62 ? 547  TYR A N   1 
ATOM   4217  C  CA  . TYR A  1 547 ? 36.534  43.186 43.635 1.00 16.29 ? 547  TYR A CA  1 
ATOM   4218  C  C   . TYR A  1 547 ? 36.803  42.175 42.523 1.00 16.22 ? 547  TYR A C   1 
ATOM   4219  O  O   . TYR A  1 547 ? 35.955  41.974 41.659 1.00 17.02 ? 547  TYR A O   1 
ATOM   4220  C  CB  . TYR A  1 547 ? 37.700  44.144 43.802 1.00 15.56 ? 547  TYR A CB  1 
ATOM   4221  C  CG  . TYR A  1 547 ? 37.767  45.067 42.609 1.00 17.09 ? 547  TYR A CG  1 
ATOM   4222  C  CD1 . TYR A  1 547 ? 38.726  44.883 41.616 1.00 15.81 ? 547  TYR A CD1 1 
ATOM   4223  C  CD2 . TYR A  1 547 ? 36.790  46.060 42.416 1.00 16.86 ? 547  TYR A CD2 1 
ATOM   4224  C  CE1 . TYR A  1 547 ? 38.718  45.645 40.464 1.00 17.06 ? 547  TYR A CE1 1 
ATOM   4225  C  CE2 . TYR A  1 547 ? 36.770  46.829 41.256 1.00 18.19 ? 547  TYR A CE2 1 
ATOM   4226  C  CZ  . TYR A  1 547 ? 37.742  46.606 40.282 1.00 18.33 ? 547  TYR A CZ  1 
ATOM   4227  O  OH  . TYR A  1 547 ? 37.695  47.307 39.103 1.00 20.00 ? 547  TYR A OH  1 
ATOM   4228  N  N   . ALA A  1 548 ? 37.975  41.542 42.556 1.00 16.03 ? 548  ALA A N   1 
ATOM   4229  C  CA  . ALA A  1 548 ? 38.314  40.498 41.619 1.00 15.21 ? 548  ALA A CA  1 
ATOM   4230  C  C   . ALA A  1 548 ? 38.463  40.842 40.145 1.00 17.26 ? 548  ALA A C   1 
ATOM   4231  O  O   . ALA A  1 548 ? 38.380  39.949 39.290 1.00 17.77 ? 548  ALA A O   1 
ATOM   4232  C  CB  . ALA A  1 548 ? 37.311  39.337 41.773 1.00 15.36 ? 548  ALA A CB  1 
ATOM   4233  N  N   . GLY A  1 549 ? 38.685  42.112 39.827 1.00 18.29 ? 549  GLY A N   1 
ATOM   4234  C  CA  . GLY A  1 549 ? 38.880  42.461 38.435 1.00 17.02 ? 549  GLY A CA  1 
ATOM   4235  C  C   . GLY A  1 549 ? 40.229  41.914 38.000 1.00 18.14 ? 549  GLY A C   1 
ATOM   4236  O  O   . GLY A  1 549 ? 40.997  41.411 38.831 1.00 16.68 ? 549  GLY A O   1 
ATOM   4237  N  N   . PRO A  1 550 ? 40.550  41.982 36.695 1.00 17.31 ? 550  PRO A N   1 
ATOM   4238  C  CA  . PRO A  1 550 ? 41.835  41.474 36.206 1.00 17.74 ? 550  PRO A CA  1 
ATOM   4239  C  C   . PRO A  1 550 ? 43.004  42.279 36.758 1.00 17.27 ? 550  PRO A C   1 
ATOM   4240  O  O   . PRO A  1 550 ? 43.023  43.503 36.678 1.00 16.41 ? 550  PRO A O   1 
ATOM   4241  C  CB  . PRO A  1 550 ? 41.703  41.579 34.681 1.00 17.53 ? 550  PRO A CB  1 
ATOM   4242  C  CG  . PRO A  1 550 ? 40.721  42.695 34.500 1.00 18.00 ? 550  PRO A CG  1 
ATOM   4243  C  CD  . PRO A  1 550 ? 39.706  42.426 35.579 1.00 17.67 ? 550  PRO A CD  1 
ATOM   4244  N  N   . CYS A  1 551 ? 43.978  41.566 37.302 1.00 16.70 ? 551  CYS A N   1 
ATOM   4245  C  CA  . CYS A  1 551 ? 45.150  42.159 37.925 1.00 18.07 ? 551  CYS A CA  1 
ATOM   4246  C  C   . CYS A  1 551 ? 44.813  42.903 39.236 1.00 17.47 ? 551  CYS A C   1 
ATOM   4247  O  O   . CYS A  1 551 ? 45.510  43.816 39.639 1.00 17.83 ? 551  CYS A O   1 
ATOM   4248  C  CB  . CYS A  1 551 ? 45.878  43.092 36.956 1.00 16.44 ? 551  CYS A CB  1 
ATOM   4249  S  SG  . CYS A  1 551 ? 47.602  43.456 37.508 1.00 21.26 ? 551  CYS A SG  1 
ATOM   4250  N  N   . SER A  1 552 ? 43.749  42.488 39.906 1.00 18.44 ? 552  SER A N   1 
ATOM   4251  C  CA  . SER A  1 552 ? 43.374  43.120 41.163 1.00 18.18 ? 552  SER A CA  1 
ATOM   4252  C  C   . SER A  1 552 ? 44.056  42.439 42.359 1.00 18.65 ? 552  SER A C   1 
ATOM   4253  O  O   . SER A  1 552 ? 44.561  41.306 42.262 1.00 18.03 ? 552  SER A O   1 
ATOM   4254  C  CB  . SER A  1 552 ? 41.864  43.038 41.355 1.00 18.72 ? 552  SER A CB  1 
ATOM   4255  O  OG  . SER A  1 552 ? 41.447  41.697 41.471 1.00 18.69 ? 552  SER A OG  1 
ATOM   4256  N  N   . GLN A  1 553 ? 44.077  43.127 43.493 1.00 18.49 ? 553  GLN A N   1 
ATOM   4257  C  CA  . GLN A  1 553 ? 44.662  42.533 44.688 1.00 19.10 ? 553  GLN A CA  1 
ATOM   4258  C  C   . GLN A  1 553 ? 43.879  43.058 45.860 1.00 18.15 ? 553  GLN A C   1 
ATOM   4259  O  O   . GLN A  1 553 ? 43.913  44.251 46.133 1.00 17.69 ? 553  GLN A O   1 
ATOM   4260  C  CB  . GLN A  1 553 ? 46.145  42.886 44.839 1.00 19.78 ? 553  GLN A CB  1 
ATOM   4261  C  CG  . GLN A  1 553 ? 46.784  42.157 46.004 1.00 20.07 ? 553  GLN A CG  1 
ATOM   4262  C  CD  . GLN A  1 553 ? 48.297  42.251 46.003 1.00 21.32 ? 553  GLN A CD  1 
ATOM   4263  O  OE1 . GLN A  1 553 ? 48.859  43.302 46.300 1.00 22.95 ? 553  GLN A OE1 1 
ATOM   4264  N  NE2 . GLN A  1 553 ? 48.961  41.154 45.661 1.00 19.68 ? 553  GLN A NE2 1 
ATOM   4265  N  N   . LYS A  1 554 ? 43.173  42.154 46.535 1.00 17.30 ? 554  LYS A N   1 
ATOM   4266  C  CA  . LYS A  1 554 ? 42.341  42.498 47.679 1.00 17.84 ? 554  LYS A CA  1 
ATOM   4267  C  C   . LYS A  1 554 ? 42.835  41.892 48.988 1.00 17.62 ? 554  LYS A C   1 
ATOM   4268  O  O   . LYS A  1 554 ? 42.270  42.148 50.050 1.00 18.22 ? 554  LYS A O   1 
ATOM   4269  C  CB  . LYS A  1 554 ? 40.893  42.085 47.414 1.00 16.70 ? 554  LYS A CB  1 
ATOM   4270  C  CG  . LYS A  1 554 ? 40.179  43.002 46.429 1.00 17.53 ? 554  LYS A CG  1 
ATOM   4271  C  CD  . LYS A  1 554 ? 39.700  44.297 47.112 1.00 18.52 ? 554  LYS A CD  1 
ATOM   4272  C  CE  . LYS A  1 554 ? 38.435  44.065 47.928 1.00 18.01 ? 554  LYS A CE  1 
ATOM   4273  N  NZ  . LYS A  1 554 ? 37.897  45.337 48.483 1.00 18.17 ? 554  LYS A NZ  1 
ATOM   4274  N  N   . ALA A  1 555 ? 43.879  41.075 48.893 1.00 17.10 ? 555  ALA A N   1 
ATOM   4275  C  CA  . ALA A  1 555 ? 44.502  40.469 50.063 1.00 16.54 ? 555  ALA A CA  1 
ATOM   4276  C  C   . ALA A  1 555 ? 45.890  41.079 50.107 1.00 16.54 ? 555  ALA A C   1 
ATOM   4277  O  O   . ALA A  1 555 ? 46.743  40.747 49.281 1.00 16.03 ? 555  ALA A O   1 
ATOM   4278  C  CB  . ALA A  1 555 ? 44.621  38.960 49.909 1.00 14.21 ? 555  ALA A CB  1 
ATOM   4279  N  N   . ASP A  1 556 ? 46.120  41.983 51.052 1.00 17.69 ? 556  ASP A N   1 
ATOM   4280  C  CA  . ASP A  1 556 ? 47.430  42.617 51.168 1.00 18.68 ? 556  ASP A CA  1 
ATOM   4281  C  C   . ASP A  1 556 ? 47.759  43.003 52.608 1.00 18.96 ? 556  ASP A C   1 
ATOM   4282  O  O   . ASP A  1 556 ? 46.968  42.779 53.512 1.00 18.42 ? 556  ASP A O   1 
ATOM   4283  C  CB  . ASP A  1 556 ? 47.507  43.852 50.251 1.00 18.93 ? 556  ASP A CB  1 
ATOM   4284  C  CG  . ASP A  1 556 ? 46.511  44.944 50.631 1.00 22.40 ? 556  ASP A CG  1 
ATOM   4285  O  OD1 . ASP A  1 556 ? 46.231  45.117 51.833 1.00 22.97 ? 556  ASP A OD1 1 
ATOM   4286  O  OD2 . ASP A  1 556 ? 46.031  45.659 49.718 1.00 25.60 ? 556  ASP A OD2 1 
ATOM   4287  N  N   . THR A  1 557 ? 48.924  43.600 52.811 1.00 19.04 ? 557  THR A N   1 
ATOM   4288  C  CA  . THR A  1 557 ? 49.353  43.995 54.147 1.00 19.98 ? 557  THR A CA  1 
ATOM   4289  C  C   . THR A  1 557 ? 49.063  45.463 54.496 1.00 20.40 ? 557  THR A C   1 
ATOM   4290  O  O   . THR A  1 557 ? 49.648  46.019 55.430 1.00 21.20 ? 557  THR A O   1 
ATOM   4291  C  CB  . THR A  1 557 ? 50.875  43.752 54.302 1.00 20.76 ? 557  THR A CB  1 
ATOM   4292  O  OG1 . THR A  1 557 ? 51.571  44.477 53.281 1.00 20.81 ? 557  THR A OG1 1 
ATOM   4293  C  CG2 . THR A  1 557 ? 51.205  42.279 54.166 1.00 19.62 ? 557  THR A CG2 1 
ATOM   4294  N  N   . VAL A  1 558 ? 48.169  46.095 53.747 1.00 19.70 ? 558  VAL A N   1 
ATOM   4295  C  CA  . VAL A  1 558 ? 47.854  47.511 53.977 1.00 19.15 ? 558  VAL A CA  1 
ATOM   4296  C  C   . VAL A  1 558 ? 46.927  47.767 55.171 1.00 19.15 ? 558  VAL A C   1 
ATOM   4297  O  O   . VAL A  1 558 ? 45.940  47.059 55.374 1.00 19.04 ? 558  VAL A O   1 
ATOM   4298  C  CB  . VAL A  1 558 ? 47.226  48.134 52.694 1.00 17.14 ? 558  VAL A CB  1 
ATOM   4299  C  CG1 . VAL A  1 558 ? 46.782  49.563 52.947 1.00 17.24 ? 558  VAL A CG1 1 
ATOM   4300  C  CG2 . VAL A  1 558 ? 48.237  48.095 51.574 1.00 15.11 ? 558  VAL A CG2 1 
ATOM   4301  N  N   . PHE A  1 559 ? 47.256  48.779 55.964 1.00 18.91 ? 559  PHE A N   1 
ATOM   4302  C  CA  . PHE A  1 559 ? 46.433  49.151 57.113 1.00 18.69 ? 559  PHE A CA  1 
ATOM   4303  C  C   . PHE A  1 559 ? 45.276  50.042 56.624 1.00 18.54 ? 559  PHE A C   1 
ATOM   4304  O  O   . PHE A  1 559 ? 45.518  51.038 55.953 1.00 17.24 ? 559  PHE A O   1 
ATOM   4305  C  CB  . PHE A  1 559 ? 47.252  49.932 58.141 1.00 18.51 ? 559  PHE A CB  1 
ATOM   4306  C  CG  . PHE A  1 559 ? 46.425  50.436 59.293 1.00 18.92 ? 559  PHE A CG  1 
ATOM   4307  C  CD1 . PHE A  1 559 ? 46.086  49.587 60.340 1.00 19.90 ? 559  PHE A CD1 1 
ATOM   4308  C  CD2 . PHE A  1 559 ? 45.925  51.735 59.298 1.00 18.96 ? 559  PHE A CD2 1 
ATOM   4309  C  CE1 . PHE A  1 559 ? 45.244  50.017 61.379 1.00 20.32 ? 559  PHE A CE1 1 
ATOM   4310  C  CE2 . PHE A  1 559 ? 45.083  52.177 60.331 1.00 21.14 ? 559  PHE A CE2 1 
ATOM   4311  C  CZ  . PHE A  1 559 ? 44.747  51.313 61.375 1.00 20.30 ? 559  PHE A CZ  1 
ATOM   4312  N  N   . ARG A  1 560 ? 44.036  49.701 56.975 1.00 18.61 ? 560  ARG A N   1 
ATOM   4313  C  CA  . ARG A  1 560 ? 42.882  50.485 56.527 1.00 18.29 ? 560  ARG A CA  1 
ATOM   4314  C  C   . ARG A  1 560 ? 41.819  50.677 57.603 1.00 18.91 ? 560  ARG A C   1 
ATOM   4315  O  O   . ARG A  1 560 ? 41.565  49.782 58.403 1.00 18.32 ? 560  ARG A O   1 
ATOM   4316  C  CB  . ARG A  1 560 ? 42.212  49.817 55.308 1.00 19.02 ? 560  ARG A CB  1 
ATOM   4317  C  CG  . ARG A  1 560 ? 43.132  49.564 54.100 1.00 16.78 ? 560  ARG A CG  1 
ATOM   4318  C  CD  . ARG A  1 560 ? 42.326  49.193 52.849 1.00 17.37 ? 560  ARG A CD  1 
ATOM   4319  N  NE  . ARG A  1 560 ? 43.202  49.109 51.681 1.00 18.55 ? 560  ARG A NE  1 
ATOM   4320  C  CZ  . ARG A  1 560 ? 43.910  48.038 51.349 1.00 19.84 ? 560  ARG A CZ  1 
ATOM   4321  N  NH1 . ARG A  1 560 ? 43.830  46.929 52.087 1.00 22.32 ? 560  ARG A NH1 1 
ATOM   4322  N  NH2 . ARG A  1 560 ? 44.758  48.099 50.327 1.00 18.85 ? 560  ARG A NH2 1 
ATOM   4323  N  N   . LEU A  1 561 ? 41.226  51.866 57.613 1.00 18.21 ? 561  LEU A N   1 
ATOM   4324  C  CA  . LEU A  1 561 ? 40.135  52.210 58.520 1.00 19.31 ? 561  LEU A CA  1 
ATOM   4325  C  C   . LEU A  1 561 ? 38.981  52.444 57.551 1.00 18.48 ? 561  LEU A C   1 
ATOM   4326  O  O   . LEU A  1 561 ? 38.894  53.492 56.907 1.00 17.55 ? 561  LEU A O   1 
ATOM   4327  C  CB  . LEU A  1 561 ? 40.430  53.492 59.299 1.00 18.64 ? 561  LEU A CB  1 
ATOM   4328  C  CG  . LEU A  1 561 ? 41.567  53.427 60.309 1.00 19.87 ? 561  LEU A CG  1 
ATOM   4329  C  CD1 . LEU A  1 561 ? 41.820  54.834 60.899 1.00 18.74 ? 561  LEU A CD1 1 
ATOM   4330  C  CD2 . LEU A  1 561 ? 41.225  52.416 61.395 1.00 18.10 ? 561  LEU A CD2 1 
ATOM   4331  N  N   . ASN A  1 562 ? 38.110  51.457 57.427 1.00 18.39 ? 562  ASN A N   1 
ATOM   4332  C  CA  . ASN A  1 562 ? 37.007  51.573 56.484 1.00 19.19 ? 562  ASN A CA  1 
ATOM   4333  C  C   . ASN A  1 562 ? 35.739  50.899 57.004 1.00 18.52 ? 562  ASN A C   1 
ATOM   4334  O  O   . ASN A  1 562 ? 35.646  50.552 58.183 1.00 18.82 ? 562  ASN A O   1 
ATOM   4335  C  CB  . ASN A  1 562 ? 37.425  50.959 55.138 1.00 18.86 ? 562  ASN A CB  1 
ATOM   4336  C  CG  . ASN A  1 562 ? 37.909  49.528 55.279 1.00 19.32 ? 562  ASN A CG  1 
ATOM   4337  O  OD1 . ASN A  1 562 ? 37.602  48.853 56.265 1.00 19.08 ? 562  ASN A OD1 1 
ATOM   4338  N  ND2 . ASN A  1 562 ? 38.655  49.049 54.286 1.00 19.08 ? 562  ASN A ND2 1 
ATOM   4339  N  N   . TRP A  1 563 ? 34.776  50.707 56.113 1.00 17.36 ? 563  TRP A N   1 
ATOM   4340  C  CA  . TRP A  1 563 ? 33.516  50.097 56.485 1.00 17.20 ? 563  TRP A CA  1 
ATOM   4341  C  C   . TRP A  1 563 ? 33.730  48.757 57.161 1.00 18.90 ? 563  TRP A C   1 
ATOM   4342  O  O   . TRP A  1 563 ? 33.115  48.475 58.194 1.00 18.28 ? 563  TRP A O   1 
ATOM   4343  C  CB  . TRP A  1 563 ? 32.630  49.930 55.262 1.00 16.25 ? 563  TRP A CB  1 
ATOM   4344  C  CG  . TRP A  1 563 ? 31.224  49.491 55.590 1.00 15.00 ? 563  TRP A CG  1 
ATOM   4345  C  CD1 . TRP A  1 563 ? 30.414  49.974 56.595 1.00 15.74 ? 563  TRP A CD1 1 
ATOM   4346  C  CD2 . TRP A  1 563 ? 30.445  48.527 54.879 1.00 13.49 ? 563  TRP A CD2 1 
ATOM   4347  N  NE1 . TRP A  1 563 ? 29.185  49.371 56.548 1.00 14.16 ? 563  TRP A NE1 1 
ATOM   4348  C  CE2 . TRP A  1 563 ? 29.170  48.478 55.506 1.00 14.70 ? 563  TRP A CE2 1 
ATOM   4349  C  CE3 . TRP A  1 563 ? 30.694  47.702 53.771 1.00 10.95 ? 563  TRP A CE3 1 
ATOM   4350  C  CZ2 . TRP A  1 563 ? 28.143  47.628 55.054 1.00 13.45 ? 563  TRP A CZ2 1 
ATOM   4351  C  CZ3 . TRP A  1 563 ? 29.683  46.860 53.321 1.00 12.36 ? 563  TRP A CZ3 1 
ATOM   4352  C  CH2 . TRP A  1 563 ? 28.415  46.830 53.965 1.00 13.97 ? 563  TRP A CH2 1 
ATOM   4353  N  N   . ALA A  1 564 ? 34.608  47.936 56.584 1.00 18.66 ? 564  ALA A N   1 
ATOM   4354  C  CA  . ALA A  1 564 ? 34.918  46.628 57.141 1.00 18.41 ? 564  ALA A CA  1 
ATOM   4355  C  C   . ALA A  1 564 ? 35.431  46.743 58.575 1.00 19.17 ? 564  ALA A C   1 
ATOM   4356  O  O   . ALA A  1 564 ? 35.158  45.858 59.386 1.00 19.63 ? 564  ALA A O   1 
ATOM   4357  C  CB  . ALA A  1 564 ? 35.971  45.915 56.274 1.00 17.98 ? 564  ALA A CB  1 
ATOM   4358  N  N   . THR A  1 565 ? 36.172  47.812 58.889 1.00 18.34 ? 565  THR A N   1 
ATOM   4359  C  CA  . THR A  1 565 ? 36.702  47.982 60.248 1.00 18.44 ? 565  THR A CA  1 
ATOM   4360  C  C   . THR A  1 565 ? 35.532  48.070 61.218 1.00 18.18 ? 565  THR A C   1 
ATOM   4361  O  O   . THR A  1 565 ? 35.574  47.499 62.301 1.00 17.59 ? 565  THR A O   1 
ATOM   4362  C  CB  . THR A  1 565 ? 37.524  49.280 60.421 1.00 18.13 ? 565  THR A CB  1 
ATOM   4363  O  OG1 . THR A  1 565 ? 38.512  49.362 59.397 1.00 20.87 ? 565  THR A OG1 1 
ATOM   4364  C  CG2 . THR A  1 565 ? 38.220  49.301 61.779 1.00 16.87 ? 565  THR A CG2 1 
ATOM   4365  N  N   . TYR A  1 566 ? 34.504  48.816 60.827 1.00 17.77 ? 566  TYR A N   1 
ATOM   4366  C  CA  . TYR A  1 566 ? 33.317  48.966 61.649 1.00 18.00 ? 566  TYR A CA  1 
ATOM   4367  C  C   . TYR A  1 566 ? 32.528  47.657 61.749 1.00 19.69 ? 566  TYR A C   1 
ATOM   4368  O  O   . TYR A  1 566 ? 32.122  47.255 62.839 1.00 20.08 ? 566  TYR A O   1 
ATOM   4369  C  CB  . TYR A  1 566 ? 32.434  50.081 61.085 1.00 18.43 ? 566  TYR A CB  1 
ATOM   4370  C  CG  . TYR A  1 566 ? 30.941  49.846 61.257 1.00 19.75 ? 566  TYR A CG  1 
ATOM   4371  C  CD1 . TYR A  1 566 ? 30.332  49.982 62.503 1.00 20.23 ? 566  TYR A CD1 1 
ATOM   4372  C  CD2 . TYR A  1 566 ? 30.157  49.440 60.183 1.00 20.17 ? 566  TYR A CD2 1 
ATOM   4373  C  CE1 . TYR A  1 566 ? 28.978  49.715 62.677 1.00 22.57 ? 566  TYR A CE1 1 
ATOM   4374  C  CE2 . TYR A  1 566 ? 28.795  49.163 60.340 1.00 21.50 ? 566  TYR A CE2 1 
ATOM   4375  C  CZ  . TYR A  1 566 ? 28.217  49.300 61.587 1.00 22.35 ? 566  TYR A CZ  1 
ATOM   4376  O  OH  . TYR A  1 566 ? 26.898  48.988 61.765 1.00 24.22 ? 566  TYR A OH  1 
ATOM   4377  N  N   . LEU A  1 567 ? 32.326  46.972 60.626 1.00 18.39 ? 567  LEU A N   1 
ATOM   4378  C  CA  . LEU A  1 567 ? 31.575  45.722 60.646 1.00 19.12 ? 567  LEU A CA  1 
ATOM   4379  C  C   . LEU A  1 567 ? 32.190  44.685 61.586 1.00 20.04 ? 567  LEU A C   1 
ATOM   4380  O  O   . LEU A  1 567 ? 31.478  43.922 62.262 1.00 19.53 ? 567  LEU A O   1 
ATOM   4381  C  CB  . LEU A  1 567 ? 31.466  45.142 59.228 1.00 16.81 ? 567  LEU A CB  1 
ATOM   4382  C  CG  . LEU A  1 567 ? 30.578  45.943 58.271 1.00 16.37 ? 567  LEU A CG  1 
ATOM   4383  C  CD1 . LEU A  1 567 ? 30.541  45.275 56.891 1.00 15.84 ? 567  LEU A CD1 1 
ATOM   4384  C  CD2 . LEU A  1 567 ? 29.175  46.040 58.858 1.00 14.92 ? 567  LEU A CD2 1 
ATOM   4385  N  N   . ALA A  1 568 ? 33.515  44.654 61.630 1.00 21.09 ? 568  ALA A N   1 
ATOM   4386  C  CA  . ALA A  1 568 ? 34.204  43.700 62.483 1.00 21.41 ? 568  ALA A CA  1 
ATOM   4387  C  C   . ALA A  1 568 ? 34.265  44.194 63.917 1.00 21.14 ? 568  ALA A C   1 
ATOM   4388  O  O   . ALA A  1 568 ? 33.969  43.450 64.838 1.00 22.03 ? 568  ALA A O   1 
ATOM   4389  C  CB  . ALA A  1 568 ? 35.627  43.448 61.957 1.00 19.14 ? 568  ALA A CB  1 
ATOM   4390  N  N   . SER A  1 569 ? 34.638  45.454 64.100 1.00 21.47 ? 569  SER A N   1 
ATOM   4391  C  CA  . SER A  1 569 ? 34.763  45.994 65.440 1.00 21.85 ? 569  SER A CA  1 
ATOM   4392  C  C   . SER A  1 569 ? 33.439  46.103 66.194 1.00 22.81 ? 569  SER A C   1 
ATOM   4393  O  O   . SER A  1 569 ? 33.341  45.656 67.329 1.00 23.67 ? 569  SER A O   1 
ATOM   4394  C  CB  . SER A  1 569 ? 35.439  47.358 65.394 1.00 21.84 ? 569  SER A CB  1 
ATOM   4395  O  OG  . SER A  1 569 ? 35.662  47.845 66.703 1.00 22.79 ? 569  SER A OG  1 
ATOM   4396  N  N   . THR A  1 570 ? 32.418  46.674 65.565 1.00 22.31 ? 570  THR A N   1 
ATOM   4397  C  CA  . THR A  1 570 ? 31.134  46.846 66.231 1.00 22.36 ? 570  THR A CA  1 
ATOM   4398  C  C   . THR A  1 570 ? 30.106  45.736 66.038 1.00 24.05 ? 570  THR A C   1 
ATOM   4399  O  O   . THR A  1 570 ? 29.402  45.371 66.974 1.00 24.88 ? 570  THR A O   1 
ATOM   4400  C  CB  . THR A  1 570 ? 30.468  48.172 65.806 1.00 21.60 ? 570  THR A CB  1 
ATOM   4401  O  OG1 . THR A  1 570 ? 31.309  49.269 66.180 1.00 21.07 ? 570  THR A OG1 1 
ATOM   4402  C  CG2 . THR A  1 570 ? 29.093  48.327 66.471 1.00 19.65 ? 570  THR A CG2 1 
ATOM   4403  N  N   . GLU A  1 571 ? 30.005  45.198 64.830 1.00 23.99 ? 571  GLU A N   1 
ATOM   4404  C  CA  . GLU A  1 571 ? 29.010  44.170 64.571 1.00 23.37 ? 571  GLU A CA  1 
ATOM   4405  C  C   . GLU A  1 571 ? 29.516  42.734 64.711 1.00 22.77 ? 571  GLU A C   1 
ATOM   4406  O  O   . GLU A  1 571 ? 28.744  41.795 64.596 1.00 21.21 ? 571  GLU A O   1 
ATOM   4407  C  CB  . GLU A  1 571 ? 28.420  44.382 63.177 1.00 23.19 ? 571  GLU A CB  1 
ATOM   4408  C  CG  . GLU A  1 571 ? 27.928  45.809 62.922 1.00 25.33 ? 571  GLU A CG  1 
ATOM   4409  C  CD  . GLU A  1 571 ? 26.782  46.219 63.835 1.00 26.70 ? 571  GLU A CD  1 
ATOM   4410  O  OE1 . GLU A  1 571 ? 26.135  45.320 64.406 1.00 29.90 ? 571  GLU A OE1 1 
ATOM   4411  O  OE2 . GLU A  1 571 ? 26.511  47.430 63.967 1.00 26.03 ? 571  GLU A OE2 1 
ATOM   4412  N  N   . ASN A  1 572 ? 30.811  42.565 64.955 1.00 22.98 ? 572  ASN A N   1 
ATOM   4413  C  CA  . ASN A  1 572 ? 31.390  41.238 65.108 1.00 23.39 ? 572  ASN A CA  1 
ATOM   4414  C  C   . ASN A  1 572 ? 31.241  40.358 63.881 1.00 23.66 ? 572  ASN A C   1 
ATOM   4415  O  O   . ASN A  1 572 ? 31.063  39.142 63.989 1.00 23.58 ? 572  ASN A O   1 
ATOM   4416  C  CB  . ASN A  1 572 ? 30.791  40.517 66.318 1.00 24.35 ? 572  ASN A CB  1 
ATOM   4417  C  CG  . ASN A  1 572 ? 31.180  41.171 67.634 1.00 26.15 ? 572  ASN A CG  1 
ATOM   4418  O  OD1 . ASN A  1 572 ? 30.338  41.752 68.312 1.00 28.49 ? 572  ASN A OD1 1 
ATOM   4419  N  ND2 . ASN A  1 572 ? 32.460  41.096 67.986 1.00 24.61 ? 572  ASN A ND2 1 
ATOM   4420  N  N   . ILE A  1 573 ? 31.351  40.984 62.713 1.00 22.94 ? 573  ILE A N   1 
ATOM   4421  C  CA  . ILE A  1 573 ? 31.276  40.297 61.442 1.00 20.90 ? 573  ILE A CA  1 
ATOM   4422  C  C   . ILE A  1 573 ? 32.662  40.094 60.854 1.00 22.29 ? 573  ILE A C   1 
ATOM   4423  O  O   . ILE A  1 573 ? 33.466  41.033 60.817 1.00 24.33 ? 573  ILE A O   1 
ATOM   4424  C  CB  . ILE A  1 573 ? 30.484  41.122 60.430 1.00 20.85 ? 573  ILE A CB  1 
ATOM   4425  C  CG1 . ILE A  1 573 ? 29.034  41.274 60.904 1.00 20.69 ? 573  ILE A CG1 1 
ATOM   4426  C  CG2 . ILE A  1 573 ? 30.547  40.465 59.055 1.00 18.18 ? 573  ILE A CG2 1 
ATOM   4427  C  CD1 . ILE A  1 573 ? 28.221  42.283 60.122 1.00 19.10 ? 573  ILE A CD1 1 
ATOM   4428  N  N   . ILE A  1 574 ? 32.953  38.884 60.383 1.00 20.08 ? 574  ILE A N   1 
ATOM   4429  C  CA  . ILE A  1 574 ? 34.240  38.645 59.736 1.00 20.74 ? 574  ILE A CA  1 
ATOM   4430  C  C   . ILE A  1 574 ? 34.165  39.129 58.272 1.00 20.25 ? 574  ILE A C   1 
ATOM   4431  O  O   . ILE A  1 574 ? 33.315  38.686 57.494 1.00 20.57 ? 574  ILE A O   1 
ATOM   4432  C  CB  . ILE A  1 574 ? 34.616  37.150 59.724 1.00 21.08 ? 574  ILE A CB  1 
ATOM   4433  C  CG1 . ILE A  1 574 ? 34.822  36.653 61.161 1.00 21.72 ? 574  ILE A CG1 1 
ATOM   4434  C  CG2 . ILE A  1 574 ? 35.869  36.933 58.885 1.00 18.93 ? 574  ILE A CG2 1 
ATOM   4435  C  CD1 . ILE A  1 574 ? 34.941  35.157 61.244 1.00 22.41 ? 574  ILE A CD1 1 
ATOM   4436  N  N   . VAL A  1 575 ? 35.060  40.034 57.898 1.00 20.27 ? 575  VAL A N   1 
ATOM   4437  C  CA  . VAL A  1 575 ? 35.069  40.546 56.537 1.00 18.90 ? 575  VAL A CA  1 
ATOM   4438  C  C   . VAL A  1 575 ? 36.291  39.993 55.854 1.00 19.04 ? 575  VAL A C   1 
ATOM   4439  O  O   . VAL A  1 575 ? 37.426  40.309 56.227 1.00 18.84 ? 575  VAL A O   1 
ATOM   4440  C  CB  . VAL A  1 575 ? 35.120  42.078 56.485 1.00 18.71 ? 575  VAL A CB  1 
ATOM   4441  C  CG1 . VAL A  1 575 ? 35.022  42.539 55.020 1.00 17.13 ? 575  VAL A CG1 1 
ATOM   4442  C  CG2 . VAL A  1 575 ? 33.981  42.669 57.337 1.00 15.87 ? 575  VAL A CG2 1 
ATOM   4443  N  N   . ALA A  1 576 ? 36.044  39.157 54.850 1.00 17.44 ? 576  ALA A N   1 
ATOM   4444  C  CA  . ALA A  1 576 ? 37.110  38.503 54.107 1.00 17.78 ? 576  ALA A CA  1 
ATOM   4445  C  C   . ALA A  1 576 ? 37.194  38.897 52.647 1.00 17.77 ? 576  ALA A C   1 
ATOM   4446  O  O   . ALA A  1 576 ? 36.207  39.324 52.038 1.00 17.83 ? 576  ALA A O   1 
ATOM   4447  C  CB  . ALA A  1 576 ? 36.937  36.984 54.199 1.00 16.86 ? 576  ALA A CB  1 
ATOM   4448  N  N   . SER A  1 577 ? 38.390  38.743 52.093 1.00 16.14 ? 577  SER A N   1 
ATOM   4449  C  CA  . SER A  1 577 ? 38.599  39.010 50.683 1.00 17.69 ? 577  SER A CA  1 
ATOM   4450  C  C   . SER A  1 577 ? 39.547  37.941 50.149 1.00 18.77 ? 577  SER A C   1 
ATOM   4451  O  O   . SER A  1 577 ? 40.411  37.424 50.873 1.00 19.03 ? 577  SER A O   1 
ATOM   4452  C  CB  . SER A  1 577 ? 39.152  40.415 50.464 1.00 17.60 ? 577  SER A CB  1 
ATOM   4453  O  OG  . SER A  1 577 ? 38.225  41.363 50.972 1.00 18.45 ? 577  SER A OG  1 
ATOM   4454  N  N   . PHE A  1 578 ? 39.385  37.625 48.874 1.00 17.28 ? 578  PHE A N   1 
ATOM   4455  C  CA  . PHE A  1 578 ? 40.161  36.578 48.250 1.00 17.06 ? 578  PHE A CA  1 
ATOM   4456  C  C   . PHE A  1 578 ? 40.625  36.939 46.836 1.00 17.23 ? 578  PHE A C   1 
ATOM   4457  O  O   . PHE A  1 578 ? 39.855  37.487 46.037 1.00 17.95 ? 578  PHE A O   1 
ATOM   4458  C  CB  . PHE A  1 578 ? 39.289  35.316 48.218 1.00 17.23 ? 578  PHE A CB  1 
ATOM   4459  C  CG  . PHE A  1 578 ? 39.926  34.142 47.540 1.00 17.79 ? 578  PHE A CG  1 
ATOM   4460  C  CD1 . PHE A  1 578 ? 40.916  33.407 48.181 1.00 17.50 ? 578  PHE A CD1 1 
ATOM   4461  C  CD2 . PHE A  1 578 ? 39.489  33.736 46.280 1.00 16.54 ? 578  PHE A CD2 1 
ATOM   4462  C  CE1 . PHE A  1 578 ? 41.458  32.275 47.579 1.00 18.39 ? 578  PHE A CE1 1 
ATOM   4463  C  CE2 . PHE A  1 578 ? 40.020  32.610 45.668 1.00 18.06 ? 578  PHE A CE2 1 
ATOM   4464  C  CZ  . PHE A  1 578 ? 41.003  31.871 46.317 1.00 17.44 ? 578  PHE A CZ  1 
ATOM   4465  N  N   . ASP A  1 579 ? 41.888  36.640 46.550 1.00 16.76 ? 579  ASP A N   1 
ATOM   4466  C  CA  . ASP A  1 579 ? 42.466  36.870 45.233 1.00 17.38 ? 579  ASP A CA  1 
ATOM   4467  C  C   . ASP A  1 579 ? 42.578  35.540 44.486 1.00 18.15 ? 579  ASP A C   1 
ATOM   4468  O  O   . ASP A  1 579 ? 43.469  34.718 44.763 1.00 17.63 ? 579  ASP A O   1 
ATOM   4469  C  CB  . ASP A  1 579 ? 43.847  37.517 45.335 1.00 16.01 ? 579  ASP A CB  1 
ATOM   4470  C  CG  . ASP A  1 579 ? 43.781  38.925 45.881 1.00 17.31 ? 579  ASP A CG  1 
ATOM   4471  O  OD1 . ASP A  1 579 ? 42.782  39.609 45.573 1.00 18.95 ? 579  ASP A OD1 1 
ATOM   4472  O  OD2 . ASP A  1 579 ? 44.711  39.349 46.601 1.00 15.26 ? 579  ASP A OD2 1 
ATOM   4473  N  N   . GLY A  1 580 ? 41.662  35.325 43.548 1.00 17.77 ? 580  GLY A N   1 
ATOM   4474  C  CA  . GLY A  1 580 ? 41.682  34.085 42.792 1.00 18.39 ? 580  GLY A CA  1 
ATOM   4475  C  C   . GLY A  1 580 ? 42.243  34.259 41.397 1.00 18.94 ? 580  GLY A C   1 
ATOM   4476  O  O   . GLY A  1 580 ? 43.003  35.192 41.129 1.00 18.65 ? 580  GLY A O   1 
ATOM   4477  N  N   . ARG A  1 581 ? 41.862  33.364 40.496 1.00 18.22 ? 581  ARG A N   1 
ATOM   4478  C  CA  . ARG A  1 581 ? 42.353  33.445 39.139 1.00 19.43 ? 581  ARG A CA  1 
ATOM   4479  C  C   . ARG A  1 581 ? 42.009  34.796 38.531 1.00 19.67 ? 581  ARG A C   1 
ATOM   4480  O  O   . ARG A  1 581 ? 40.895  35.304 38.673 1.00 18.99 ? 581  ARG A O   1 
ATOM   4481  C  CB  . ARG A  1 581 ? 41.800  32.291 38.297 1.00 19.65 ? 581  ARG A CB  1 
ATOM   4482  C  CG  . ARG A  1 581 ? 42.649  31.017 38.443 1.00 22.09 ? 581  ARG A CG  1 
ATOM   4483  C  CD  . ARG A  1 581 ? 41.983  29.773 37.833 1.00 20.50 ? 581  ARG A CD  1 
ATOM   4484  N  NE  . ARG A  1 581 ? 40.715  29.436 38.474 1.00 19.88 ? 581  ARG A NE  1 
ATOM   4485  C  CZ  . ARG A  1 581 ? 39.970  28.380 38.144 1.00 22.28 ? 581  ARG A CZ  1 
ATOM   4486  N  NH1 . ARG A  1 581 ? 40.365  27.552 37.172 1.00 19.54 ? 581  ARG A NH1 1 
ATOM   4487  N  NH2 . ARG A  1 581 ? 38.825  28.149 38.782 1.00 20.79 ? 581  ARG A NH2 1 
ATOM   4488  N  N   . GLY A  1 582 ? 42.982  35.381 37.848 1.00 19.76 ? 582  GLY A N   1 
ATOM   4489  C  CA  . GLY A  1 582 ? 42.774  36.694 37.271 1.00 18.52 ? 582  GLY A CA  1 
ATOM   4490  C  C   . GLY A  1 582 ? 43.387  37.800 38.135 1.00 17.42 ? 582  GLY A C   1 
ATOM   4491  O  O   . GLY A  1 582 ? 43.578  38.904 37.637 1.00 18.19 ? 582  GLY A O   1 
ATOM   4492  N  N   . SER A  1 583 ? 43.701  37.519 39.404 1.00 17.28 ? 583  SER A N   1 
ATOM   4493  C  CA  . SER A  1 583 ? 44.287  38.531 40.291 1.00 17.46 ? 583  SER A CA  1 
ATOM   4494  C  C   . SER A  1 583 ? 45.725  38.834 39.845 1.00 16.40 ? 583  SER A C   1 
ATOM   4495  O  O   . SER A  1 583 ? 46.304  38.087 39.063 1.00 16.23 ? 583  SER A O   1 
ATOM   4496  C  CB  . SER A  1 583 ? 44.226  38.075 41.760 1.00 17.15 ? 583  SER A CB  1 
ATOM   4497  O  OG  . SER A  1 583 ? 44.953  36.870 41.945 1.00 19.86 ? 583  SER A OG  1 
ATOM   4498  N  N   . GLY A  1 584 ? 46.312  39.927 40.322 1.00 17.10 ? 584  GLY A N   1 
ATOM   4499  C  CA  . GLY A  1 584 ? 47.638  40.267 39.825 1.00 17.27 ? 584  GLY A CA  1 
ATOM   4500  C  C   . GLY A  1 584 ? 48.831  40.041 40.711 1.00 16.51 ? 584  GLY A C   1 
ATOM   4501  O  O   . GLY A  1 584 ? 48.700  39.501 41.804 1.00 17.00 ? 584  GLY A O   1 
ATOM   4502  N  N   . TYR A  1 585 ? 49.999  40.424 40.195 1.00 15.97 ? 585  TYR A N   1 
ATOM   4503  C  CA  . TYR A  1 585 ? 51.278  40.356 40.909 1.00 16.60 ? 585  TYR A CA  1 
ATOM   4504  C  C   . TYR A  1 585 ? 51.790  38.974 41.282 1.00 17.56 ? 585  TYR A C   1 
ATOM   4505  O  O   . TYR A  1 585 ? 52.696  38.844 42.116 1.00 17.86 ? 585  TYR A O   1 
ATOM   4506  C  CB  . TYR A  1 585 ? 51.187  41.230 42.168 1.00 16.34 ? 585  TYR A CB  1 
ATOM   4507  C  CG  . TYR A  1 585 ? 50.558  42.560 41.862 1.00 15.09 ? 585  TYR A CG  1 
ATOM   4508  C  CD1 . TYR A  1 585 ? 51.201  43.473 41.014 1.00 16.01 ? 585  TYR A CD1 1 
ATOM   4509  C  CD2 . TYR A  1 585 ? 49.280  42.873 42.326 1.00 14.34 ? 585  TYR A CD2 1 
ATOM   4510  C  CE1 . TYR A  1 585 ? 50.588  44.663 40.629 1.00 14.29 ? 585  TYR A CE1 1 
ATOM   4511  C  CE2 . TYR A  1 585 ? 48.650  44.059 41.945 1.00 14.64 ? 585  TYR A CE2 1 
ATOM   4512  C  CZ  . TYR A  1 585 ? 49.304  44.943 41.097 1.00 17.22 ? 585  TYR A CZ  1 
ATOM   4513  O  OH  . TYR A  1 585 ? 48.666  46.083 40.675 1.00 17.15 ? 585  TYR A OH  1 
ATOM   4514  N  N   . GLN A  1 586 ? 51.218  37.950 40.657 1.00 17.49 ? 586  GLN A N   1 
ATOM   4515  C  CA  . GLN A  1 586 ? 51.621  36.579 40.900 1.00 17.81 ? 586  GLN A CA  1 
ATOM   4516  C  C   . GLN A  1 586 ? 51.951  35.844 39.599 1.00 18.49 ? 586  GLN A C   1 
ATOM   4517  O  O   . GLN A  1 586 ? 52.020  34.610 39.579 1.00 20.16 ? 586  GLN A O   1 
ATOM   4518  C  CB  . GLN A  1 586 ? 50.507  35.834 41.639 1.00 16.45 ? 586  GLN A CB  1 
ATOM   4519  C  CG  . GLN A  1 586 ? 50.031  36.543 42.888 1.00 18.03 ? 586  GLN A CG  1 
ATOM   4520  C  CD  . GLN A  1 586 ? 48.580  36.222 43.195 1.00 20.33 ? 586  GLN A CD  1 
ATOM   4521  O  OE1 . GLN A  1 586 ? 48.270  35.148 43.707 1.00 20.66 ? 586  GLN A OE1 1 
ATOM   4522  N  NE2 . GLN A  1 586 ? 47.678  37.139 42.844 1.00 19.22 ? 586  GLN A NE2 1 
ATOM   4523  N  N   . GLY A  1 587 ? 52.149  36.589 38.518 1.00 18.38 ? 587  GLY A N   1 
ATOM   4524  C  CA  . GLY A  1 587 ? 52.461  35.966 37.247 1.00 18.04 ? 587  GLY A CA  1 
ATOM   4525  C  C   . GLY A  1 587 ? 51.260  35.784 36.330 1.00 18.28 ? 587  GLY A C   1 
ATOM   4526  O  O   . GLY A  1 587 ? 50.108  35.717 36.781 1.00 18.76 ? 587  GLY A O   1 
ATOM   4527  N  N   . ASP A  1 588 ? 51.546  35.681 35.038 1.00 19.03 ? 588  ASP A N   1 
ATOM   4528  C  CA  . ASP A  1 588 ? 50.528  35.518 33.986 1.00 20.33 ? 588  ASP A CA  1 
ATOM   4529  C  C   . ASP A  1 588 ? 49.683  34.244 34.028 1.00 20.60 ? 588  ASP A C   1 
ATOM   4530  O  O   . ASP A  1 588 ? 48.563  34.231 33.535 1.00 21.71 ? 588  ASP A O   1 
ATOM   4531  C  CB  . ASP A  1 588 ? 51.190  35.607 32.605 1.00 19.22 ? 588  ASP A CB  1 
ATOM   4532  C  CG  . ASP A  1 588 ? 51.669  37.019 32.270 1.00 21.04 ? 588  ASP A CG  1 
ATOM   4533  O  OD1 . ASP A  1 588 ? 51.401  37.944 33.065 1.00 23.18 ? 588  ASP A OD1 1 
ATOM   4534  O  OD2 . ASP A  1 588 ? 52.296  37.197 31.210 1.00 19.50 ? 588  ASP A OD2 1 
ATOM   4535  N  N   . LYS A  1 589 ? 50.222  33.168 34.584 1.00 22.22 ? 589  LYS A N   1 
ATOM   4536  C  CA  . LYS A  1 589 ? 49.463  31.934 34.645 1.00 24.08 ? 589  LYS A CA  1 
ATOM   4537  C  C   . LYS A  1 589 ? 48.186  32.178 35.447 1.00 23.59 ? 589  LYS A C   1 
ATOM   4538  O  O   . LYS A  1 589 ? 47.129  31.664 35.108 1.00 23.94 ? 589  LYS A O   1 
ATOM   4539  C  CB  . LYS A  1 589 ? 50.282  30.829 35.286 1.00 27.17 ? 589  LYS A CB  1 
ATOM   4540  C  CG  . LYS A  1 589 ? 49.492  29.538 35.468 1.00 33.56 ? 589  LYS A CG  1 
ATOM   4541  C  CD  . LYS A  1 589 ? 48.941  29.001 34.127 1.00 38.44 ? 589  LYS A CD  1 
ATOM   4542  C  CE  . LYS A  1 589 ? 48.259  27.630 34.296 1.00 40.41 ? 589  LYS A CE  1 
ATOM   4543  N  NZ  . LYS A  1 589 ? 49.151  26.669 35.026 1.00 41.79 ? 589  LYS A NZ  1 
ATOM   4544  N  N   . ILE A  1 590 ? 48.296  32.969 36.511 1.00 21.63 ? 590  ILE A N   1 
ATOM   4545  C  CA  . ILE A  1 590 ? 47.149  33.300 37.325 1.00 19.97 ? 590  ILE A CA  1 
ATOM   4546  C  C   . ILE A  1 590 ? 46.394  34.470 36.707 1.00 20.48 ? 590  ILE A C   1 
ATOM   4547  O  O   . ILE A  1 590 ? 45.164  34.411 36.525 1.00 20.74 ? 590  ILE A O   1 
ATOM   4548  C  CB  . ILE A  1 590 ? 47.578  33.680 38.771 1.00 20.61 ? 590  ILE A CB  1 
ATOM   4549  C  CG1 . ILE A  1 590 ? 47.923  32.411 39.552 1.00 19.98 ? 590  ILE A CG1 1 
ATOM   4550  C  CG2 . ILE A  1 590 ? 46.476  34.467 39.470 1.00 17.05 ? 590  ILE A CG2 1 
ATOM   4551  C  CD1 . ILE A  1 590 ? 48.517  32.655 40.930 1.00 19.26 ? 590  ILE A CD1 1 
ATOM   4552  N  N   . MET A  1 591 ? 47.124  35.526 36.352 1.00 20.21 ? 591  MET A N   1 
ATOM   4553  C  CA  . MET A  1 591 ? 46.464  36.705 35.813 1.00 19.74 ? 591  MET A CA  1 
ATOM   4554  C  C   . MET A  1 591 ? 45.735  36.482 34.491 1.00 20.87 ? 591  MET A C   1 
ATOM   4555  O  O   . MET A  1 591 ? 44.615  36.971 34.326 1.00 20.35 ? 591  MET A O   1 
ATOM   4556  C  CB  . MET A  1 591 ? 47.443  37.872 35.663 1.00 18.89 ? 591  MET A CB  1 
ATOM   4557  C  CG  . MET A  1 591 ? 46.720  39.198 35.365 1.00 19.40 ? 591  MET A CG  1 
ATOM   4558  S  SD  . MET A  1 591 ? 47.830  40.672 35.350 1.00 21.88 ? 591  MET A SD  1 
ATOM   4559  C  CE  . MET A  1 591 ? 48.621  40.438 33.754 1.00 18.67 ? 591  MET A CE  1 
ATOM   4560  N  N   . HIS A  1 592 ? 46.343  35.730 33.574 1.00 20.19 ? 592  HIS A N   1 
ATOM   4561  C  CA  . HIS A  1 592 ? 45.728  35.498 32.275 1.00 22.18 ? 592  HIS A CA  1 
ATOM   4562  C  C   . HIS A  1 592 ? 44.730  34.340 32.234 1.00 22.71 ? 592  HIS A C   1 
ATOM   4563  O  O   . HIS A  1 592 ? 44.175  34.028 31.178 1.00 22.72 ? 592  HIS A O   1 
ATOM   4564  C  CB  . HIS A  1 592 ? 46.812  35.276 31.207 1.00 22.50 ? 592  HIS A CB  1 
ATOM   4565  C  CG  . HIS A  1 592 ? 47.557  36.520 30.824 1.00 23.28 ? 592  HIS A CG  1 
ATOM   4566  N  ND1 . HIS A  1 592 ? 48.684  36.499 30.028 1.00 24.32 ? 592  HIS A ND1 1 
ATOM   4567  C  CD2 . HIS A  1 592 ? 47.341  37.825 31.127 1.00 22.94 ? 592  HIS A CD2 1 
ATOM   4568  C  CE1 . HIS A  1 592 ? 49.129  37.730 29.855 1.00 24.76 ? 592  HIS A CE1 1 
ATOM   4569  N  NE2 . HIS A  1 592 ? 48.330  38.556 30.513 1.00 24.94 ? 592  HIS A NE2 1 
ATOM   4570  N  N   . ALA A  1 593 ? 44.485  33.702 33.372 1.00 23.47 ? 593  ALA A N   1 
ATOM   4571  C  CA  . ALA A  1 593 ? 43.553  32.584 33.384 1.00 23.06 ? 593  ALA A CA  1 
ATOM   4572  C  C   . ALA A  1 593 ? 42.176  32.994 32.894 1.00 24.19 ? 593  ALA A C   1 
ATOM   4573  O  O   . ALA A  1 593 ? 41.429  32.148 32.427 1.00 25.02 ? 593  ALA A O   1 
ATOM   4574  C  CB  . ALA A  1 593 ? 43.450  31.999 34.767 1.00 21.46 ? 593  ALA A CB  1 
ATOM   4575  N  N   . ILE A  1 594 ? 41.834  34.279 33.001 1.00 24.01 ? 594  ILE A N   1 
ATOM   4576  C  CA  . ILE A  1 594 ? 40.519  34.739 32.549 1.00 23.78 ? 594  ILE A CA  1 
ATOM   4577  C  C   . ILE A  1 594 ? 40.521  35.464 31.221 1.00 23.41 ? 594  ILE A C   1 
ATOM   4578  O  O   . ILE A  1 594 ? 39.525  36.093 30.855 1.00 23.17 ? 594  ILE A O   1 
ATOM   4579  C  CB  . ILE A  1 594 ? 39.813  35.666 33.575 1.00 24.72 ? 594  ILE A CB  1 
ATOM   4580  C  CG1 . ILE A  1 594 ? 40.688  36.880 33.894 1.00 24.66 ? 594  ILE A CG1 1 
ATOM   4581  C  CG2 . ILE A  1 594 ? 39.442  34.880 34.809 1.00 23.44 ? 594  ILE A CG2 1 
ATOM   4582  C  CD1 . ILE A  1 594 ? 40.125  37.693 35.046 1.00 28.94 ? 594  ILE A CD1 1 
ATOM   4583  N  N   . ASN A  1 595 ? 41.623  35.360 30.494 1.00 22.86 ? 595  ASN A N   1 
ATOM   4584  C  CA  . ASN A  1 595 ? 41.708  35.998 29.197 1.00 24.00 ? 595  ASN A CA  1 
ATOM   4585  C  C   . ASN A  1 595 ? 40.550  35.541 28.290 1.00 23.58 ? 595  ASN A C   1 
ATOM   4586  O  O   . ASN A  1 595 ? 40.313  34.351 28.137 1.00 22.61 ? 595  ASN A O   1 
ATOM   4587  C  CB  . ASN A  1 595 ? 43.056  35.683 28.549 1.00 24.18 ? 595  ASN A CB  1 
ATOM   4588  C  CG  . ASN A  1 595 ? 43.207  36.336 27.186 1.00 25.78 ? 595  ASN A CG  1 
ATOM   4589  O  OD1 . ASN A  1 595 ? 43.200  35.662 26.167 1.00 27.89 ? 595  ASN A OD1 1 
ATOM   4590  N  ND2 . ASN A  1 595 ? 43.330  37.654 27.166 1.00 25.50 ? 595  ASN A ND2 1 
ATOM   4591  N  N   . ARG A  1 596 ? 39.830  36.510 27.726 1.00 23.10 ? 596  ARG A N   1 
ATOM   4592  C  CA  . ARG A  1 596 ? 38.688  36.273 26.830 1.00 23.28 ? 596  ARG A CA  1 
ATOM   4593  C  C   . ARG A  1 596 ? 37.571  35.535 27.539 1.00 23.82 ? 596  ARG A C   1 
ATOM   4594  O  O   . ARG A  1 596 ? 36.632  35.048 26.903 1.00 23.18 ? 596  ARG A O   1 
ATOM   4595  C  CB  . ARG A  1 596 ? 39.114  35.476 25.587 1.00 23.19 ? 596  ARG A CB  1 
ATOM   4596  C  CG  . ARG A  1 596 ? 40.139  36.194 24.702 1.00 23.65 ? 596  ARG A CG  1 
ATOM   4597  C  CD  . ARG A  1 596 ? 40.635  35.278 23.596 1.00 24.66 ? 596  ARG A CD  1 
ATOM   4598  N  NE  . ARG A  1 596 ? 39.538  34.778 22.758 1.00 26.19 ? 596  ARG A NE  1 
ATOM   4599  C  CZ  . ARG A  1 596 ? 38.972  35.461 21.768 1.00 28.47 ? 596  ARG A CZ  1 
ATOM   4600  N  NH1 . ARG A  1 596 ? 39.389  36.693 21.465 1.00 28.89 ? 596  ARG A NH1 1 
ATOM   4601  N  NH2 . ARG A  1 596 ? 37.986  34.908 21.078 1.00 29.27 ? 596  ARG A NH2 1 
ATOM   4602  N  N   . ARG A  1 597 ? 37.654  35.491 28.861 1.00 24.13 ? 597  ARG A N   1 
ATOM   4603  C  CA  . ARG A  1 597 ? 36.682  34.749 29.649 1.00 24.75 ? 597  ARG A CA  1 
ATOM   4604  C  C   . ARG A  1 597 ? 36.289  35.400 30.972 1.00 23.70 ? 597  ARG A C   1 
ATOM   4605  O  O   . ARG A  1 597 ? 36.291  34.731 32.007 1.00 23.16 ? 597  ARG A O   1 
ATOM   4606  C  CB  . ARG A  1 597 ? 37.246  33.355 29.934 1.00 26.30 ? 597  ARG A CB  1 
ATOM   4607  C  CG  . ARG A  1 597 ? 36.640  32.233 29.118 1.00 32.17 ? 597  ARG A CG  1 
ATOM   4608  C  CD  . ARG A  1 597 ? 36.752  32.482 27.643 1.00 36.63 ? 597  ARG A CD  1 
ATOM   4609  N  NE  . ARG A  1 597 ? 36.231  31.393 26.814 1.00 38.06 ? 597  ARG A NE  1 
ATOM   4610  C  CZ  . ARG A  1 597 ? 35.958  31.538 25.523 1.00 38.52 ? 597  ARG A CZ  1 
ATOM   4611  N  NH1 . ARG A  1 597 ? 36.143  32.718 24.946 1.00 38.17 ? 597  ARG A NH1 1 
ATOM   4612  N  NH2 . ARG A  1 597 ? 35.545  30.506 24.801 1.00 38.72 ? 597  ARG A NH2 1 
ATOM   4613  N  N   . LEU A  1 598 ? 35.967  36.691 30.950 1.00 21.51 ? 598  LEU A N   1 
ATOM   4614  C  CA  . LEU A  1 598 ? 35.549  37.370 32.175 1.00 19.63 ? 598  LEU A CA  1 
ATOM   4615  C  C   . LEU A  1 598 ? 34.224  36.756 32.631 1.00 19.31 ? 598  LEU A C   1 
ATOM   4616  O  O   . LEU A  1 598 ? 33.446  36.232 31.820 1.00 17.77 ? 598  LEU A O   1 
ATOM   4617  C  CB  . LEU A  1 598 ? 35.348  38.882 31.934 1.00 18.37 ? 598  LEU A CB  1 
ATOM   4618  C  CG  . LEU A  1 598 ? 36.546  39.733 31.468 1.00 17.44 ? 598  LEU A CG  1 
ATOM   4619  C  CD1 . LEU A  1 598 ? 36.187  41.204 31.526 1.00 17.42 ? 598  LEU A CD1 1 
ATOM   4620  C  CD2 . LEU A  1 598 ? 37.745  39.472 32.343 1.00 16.33 ? 598  LEU A CD2 1 
ATOM   4621  N  N   . GLY A  1 599 ? 33.957  36.821 33.929 1.00 18.83 ? 599  GLY A N   1 
ATOM   4622  C  CA  . GLY A  1 599 ? 32.714  36.264 34.433 1.00 18.88 ? 599  GLY A CA  1 
ATOM   4623  C  C   . GLY A  1 599 ? 32.773  34.754 34.607 1.00 19.47 ? 599  GLY A C   1 
ATOM   4624  O  O   . GLY A  1 599 ? 31.732  34.103 34.725 1.00 20.45 ? 599  GLY A O   1 
ATOM   4625  N  N   . THR A  1 600 ? 33.973  34.180 34.617 1.00 17.50 ? 600  THR A N   1 
ATOM   4626  C  CA  . THR A  1 600 ? 34.062  32.738 34.807 1.00 18.89 ? 600  THR A CA  1 
ATOM   4627  C  C   . THR A  1 600 ? 34.903  32.333 36.011 1.00 18.57 ? 600  THR A C   1 
ATOM   4628  O  O   . THR A  1 600 ? 34.390  32.252 37.128 1.00 19.85 ? 600  THR A O   1 
ATOM   4629  C  CB  . THR A  1 600 ? 34.587  32.003 33.522 1.00 18.33 ? 600  THR A CB  1 
ATOM   4630  O  OG1 . THR A  1 600 ? 35.928  32.425 33.211 1.00 18.69 ? 600  THR A OG1 1 
ATOM   4631  C  CG2 . THR A  1 600 ? 33.684  32.333 32.326 1.00 18.75 ? 600  THR A CG2 1 
ATOM   4632  N  N   . PHE A  1 601 ? 36.199  32.109 35.800 1.00 19.54 ? 601  PHE A N   1 
ATOM   4633  C  CA  . PHE A  1 601 ? 37.059  31.663 36.890 1.00 20.57 ? 601  PHE A CA  1 
ATOM   4634  C  C   . PHE A  1 601 ? 37.140  32.585 38.085 1.00 20.94 ? 601  PHE A C   1 
ATOM   4635  O  O   . PHE A  1 601 ? 37.197  32.103 39.217 1.00 21.42 ? 601  PHE A O   1 
ATOM   4636  C  CB  . PHE A  1 601 ? 38.480  31.359 36.393 1.00 21.09 ? 601  PHE A CB  1 
ATOM   4637  C  CG  . PHE A  1 601 ? 38.538  30.276 35.364 1.00 24.10 ? 601  PHE A CG  1 
ATOM   4638  C  CD1 . PHE A  1 601 ? 37.755  29.133 35.496 1.00 25.42 ? 601  PHE A CD1 1 
ATOM   4639  C  CD2 . PHE A  1 601 ? 39.387  30.382 34.274 1.00 25.68 ? 601  PHE A CD2 1 
ATOM   4640  C  CE1 . PHE A  1 601 ? 37.819  28.114 34.561 1.00 26.61 ? 601  PHE A CE1 1 
ATOM   4641  C  CE2 . PHE A  1 601 ? 39.459  29.365 33.329 1.00 27.75 ? 601  PHE A CE2 1 
ATOM   4642  C  CZ  . PHE A  1 601 ? 38.673  28.227 33.471 1.00 27.26 ? 601  PHE A CZ  1 
ATOM   4643  N  N   . GLU A  1 602 ? 37.146  33.896 37.858 1.00 20.48 ? 602  GLU A N   1 
ATOM   4644  C  CA  . GLU A  1 602 ? 37.248  34.810 38.988 1.00 21.14 ? 602  GLU A CA  1 
ATOM   4645  C  C   . GLU A  1 602 ? 35.965  34.753 39.828 1.00 20.79 ? 602  GLU A C   1 
ATOM   4646  O  O   . GLU A  1 602 ? 36.004  34.967 41.038 1.00 21.57 ? 602  GLU A O   1 
ATOM   4647  C  CB  . GLU A  1 602 ? 37.574  36.244 38.516 1.00 20.41 ? 602  GLU A CB  1 
ATOM   4648  C  CG  . GLU A  1 602 ? 36.417  37.100 38.011 1.00 20.27 ? 602  GLU A CG  1 
ATOM   4649  C  CD  . GLU A  1 602 ? 35.997  36.812 36.571 1.00 22.21 ? 602  GLU A CD  1 
ATOM   4650  O  OE1 . GLU A  1 602 ? 35.474  37.740 35.913 1.00 20.88 ? 602  GLU A OE1 1 
ATOM   4651  O  OE2 . GLU A  1 602 ? 36.169  35.668 36.098 1.00 23.41 ? 602  GLU A OE2 1 
ATOM   4652  N  N   . VAL A  1 603 ? 34.839  34.447 39.192 1.00 20.96 ? 603  VAL A N   1 
ATOM   4653  C  CA  . VAL A  1 603 ? 33.568  34.319 39.917 1.00 20.57 ? 603  VAL A CA  1 
ATOM   4654  C  C   . VAL A  1 603 ? 33.561  32.973 40.675 1.00 21.66 ? 603  VAL A C   1 
ATOM   4655  O  O   . VAL A  1 603 ? 33.283  32.932 41.881 1.00 21.75 ? 603  VAL A O   1 
ATOM   4656  C  CB  . VAL A  1 603 ? 32.370  34.364 38.946 1.00 20.80 ? 603  VAL A CB  1 
ATOM   4657  C  CG1 . VAL A  1 603 ? 31.079  34.091 39.689 1.00 18.99 ? 603  VAL A CG1 1 
ATOM   4658  C  CG2 . VAL A  1 603 ? 32.307  35.731 38.267 1.00 19.87 ? 603  VAL A CG2 1 
ATOM   4659  N  N   . GLU A  1 604 ? 33.893  31.888 39.966 1.00 20.92 ? 604  GLU A N   1 
ATOM   4660  C  CA  . GLU A  1 604 ? 33.948  30.544 40.553 1.00 22.25 ? 604  GLU A CA  1 
ATOM   4661  C  C   . GLU A  1 604 ? 34.913  30.491 41.738 1.00 21.70 ? 604  GLU A C   1 
ATOM   4662  O  O   . GLU A  1 604 ? 34.625  29.855 42.751 1.00 21.17 ? 604  GLU A O   1 
ATOM   4663  C  CB  . GLU A  1 604 ? 34.385  29.496 39.504 1.00 24.47 ? 604  GLU A CB  1 
ATOM   4664  C  CG  . GLU A  1 604 ? 33.361  29.234 38.389 1.00 31.81 ? 604  GLU A CG  1 
ATOM   4665  C  CD  . GLU A  1 604 ? 33.953  28.539 37.141 1.00 35.72 ? 604  GLU A CD  1 
ATOM   4666  O  OE1 . GLU A  1 604 ? 34.520  27.416 37.266 1.00 37.71 ? 604  GLU A OE1 1 
ATOM   4667  O  OE2 . GLU A  1 604 ? 33.846  29.122 36.028 1.00 34.20 ? 604  GLU A OE2 1 
ATOM   4668  N  N   . ASP A  1 605 ? 36.068  31.144 41.614 1.00 21.49 ? 605  ASP A N   1 
ATOM   4669  C  CA  . ASP A  1 605 ? 37.027  31.131 42.714 1.00 21.52 ? 605  ASP A CA  1 
ATOM   4670  C  C   . ASP A  1 605 ? 36.535  31.833 43.986 1.00 20.04 ? 605  ASP A C   1 
ATOM   4671  O  O   . ASP A  1 605 ? 36.904  31.438 45.078 1.00 21.28 ? 605  ASP A O   1 
ATOM   4672  C  CB  . ASP A  1 605 ? 38.386  31.688 42.255 1.00 22.49 ? 605  ASP A CB  1 
ATOM   4673  C  CG  . ASP A  1 605 ? 39.108  30.732 41.314 1.00 23.13 ? 605  ASP A CG  1 
ATOM   4674  O  OD1 . ASP A  1 605 ? 38.601  29.606 41.126 1.00 24.23 ? 605  ASP A OD1 1 
ATOM   4675  O  OD2 . ASP A  1 605 ? 40.173  31.085 40.758 1.00 24.59 ? 605  ASP A OD2 1 
ATOM   4676  N  N   . GLN A  1 606 ? 35.703  32.859 43.856 1.00 19.28 ? 606  GLN A N   1 
ATOM   4677  C  CA  . GLN A  1 606 ? 35.156  33.537 45.033 1.00 19.45 ? 606  GLN A CA  1 
ATOM   4678  C  C   . GLN A  1 606 ? 34.195  32.564 45.758 1.00 19.75 ? 606  GLN A C   1 
ATOM   4679  O  O   . GLN A  1 606 ? 34.159  32.491 47.000 1.00 19.88 ? 606  GLN A O   1 
ATOM   4680  C  CB  . GLN A  1 606 ? 34.381  34.805 44.624 1.00 17.95 ? 606  GLN A CB  1 
ATOM   4681  C  CG  . GLN A  1 606 ? 35.254  35.966 44.088 1.00 17.88 ? 606  GLN A CG  1 
ATOM   4682  C  CD  . GLN A  1 606 ? 36.214  36.486 45.147 1.00 15.94 ? 606  GLN A CD  1 
ATOM   4683  O  OE1 . GLN A  1 606 ? 35.798  36.818 46.244 1.00 17.89 ? 606  GLN A OE1 1 
ATOM   4684  N  NE2 . GLN A  1 606 ? 37.495  36.548 44.822 1.00 15.65 ? 606  GLN A NE2 1 
ATOM   4685  N  N   . ILE A  1 607 ? 33.411  31.819 44.984 1.00 19.99 ? 607  ILE A N   1 
ATOM   4686  C  CA  . ILE A  1 607 ? 32.464  30.880 45.583 1.00 20.30 ? 607  ILE A CA  1 
ATOM   4687  C  C   . ILE A  1 607 ? 33.257  29.798 46.308 1.00 20.69 ? 607  ILE A C   1 
ATOM   4688  O  O   . ILE A  1 607 ? 32.967  29.483 47.459 1.00 21.21 ? 607  ILE A O   1 
ATOM   4689  C  CB  . ILE A  1 607 ? 31.554  30.240 44.515 1.00 19.92 ? 607  ILE A CB  1 
ATOM   4690  C  CG1 . ILE A  1 607 ? 30.763  31.335 43.796 1.00 19.28 ? 607  ILE A CG1 1 
ATOM   4691  C  CG2 . ILE A  1 607 ? 30.605  29.235 45.162 1.00 18.60 ? 607  ILE A CG2 1 
ATOM   4692  C  CD1 . ILE A  1 607 ? 30.086  30.846 42.511 1.00 18.74 ? 607  ILE A CD1 1 
ATOM   4693  N  N   . GLU A  1 608 ? 34.281  29.269 45.639 1.00 21.99 ? 608  GLU A N   1 
ATOM   4694  C  CA  . GLU A  1 608 ? 35.149  28.216 46.198 1.00 23.40 ? 608  GLU A CA  1 
ATOM   4695  C  C   . GLU A  1 608 ? 35.779  28.671 47.526 1.00 23.77 ? 608  GLU A C   1 
ATOM   4696  O  O   . GLU A  1 608 ? 35.873  27.900 48.476 1.00 23.89 ? 608  GLU A O   1 
ATOM   4697  C  CB  . GLU A  1 608 ? 36.277  27.893 45.215 1.00 24.52 ? 608  GLU A CB  1 
ATOM   4698  C  CG  . GLU A  1 608 ? 36.664  26.406 45.008 1.00 29.38 ? 608  GLU A CG  1 
ATOM   4699  C  CD  . GLU A  1 608 ? 36.245  25.457 46.117 1.00 31.22 ? 608  GLU A CD  1 
ATOM   4700  O  OE1 . GLU A  1 608 ? 35.026  25.201 46.256 1.00 33.05 ? 608  GLU A OE1 1 
ATOM   4701  O  OE2 . GLU A  1 608 ? 37.133  24.958 46.849 1.00 31.66 ? 608  GLU A OE2 1 
ATOM   4702  N  N   . ALA A  1 609 ? 36.216  29.927 47.577 1.00 23.66 ? 609  ALA A N   1 
ATOM   4703  C  CA  . ALA A  1 609 ? 36.830  30.462 48.775 1.00 22.61 ? 609  ALA A CA  1 
ATOM   4704  C  C   . ALA A  1 609 ? 35.806  30.530 49.890 1.00 22.05 ? 609  ALA A C   1 
ATOM   4705  O  O   . ALA A  1 609 ? 36.087  30.120 51.021 1.00 20.99 ? 609  ALA A O   1 
ATOM   4706  C  CB  . ALA A  1 609 ? 37.416  31.847 48.505 1.00 22.40 ? 609  ALA A CB  1 
ATOM   4707  N  N   . ALA A  1 610 ? 34.622  31.050 49.577 1.00 21.14 ? 610  ALA A N   1 
ATOM   4708  C  CA  . ALA A  1 610 ? 33.560  31.152 50.580 1.00 23.07 ? 610  ALA A CA  1 
ATOM   4709  C  C   . ALA A  1 610 ? 33.243  29.757 51.082 1.00 24.41 ? 610  ALA A C   1 
ATOM   4710  O  O   . ALA A  1 610 ? 33.142  29.531 52.279 1.00 24.57 ? 610  ALA A O   1 
ATOM   4711  C  CB  . ALA A  1 610 ? 32.312  31.774 49.988 1.00 21.81 ? 610  ALA A CB  1 
ATOM   4712  N  N   . ARG A  1 611 ? 33.097  28.827 50.143 1.00 25.51 ? 611  ARG A N   1 
ATOM   4713  C  CA  . ARG A  1 611 ? 32.808  27.441 50.456 1.00 27.27 ? 611  ARG A CA  1 
ATOM   4714  C  C   . ARG A  1 611 ? 33.833  26.946 51.474 1.00 28.08 ? 611  ARG A C   1 
ATOM   4715  O  O   . ARG A  1 611 ? 33.485  26.341 52.482 1.00 28.26 ? 611  ARG A O   1 
ATOM   4716  C  CB  . ARG A  1 611 ? 32.870  26.632 49.158 1.00 27.58 ? 611  ARG A CB  1 
ATOM   4717  C  CG  . ARG A  1 611 ? 32.385  25.219 49.241 1.00 28.64 ? 611  ARG A CG  1 
ATOM   4718  C  CD  . ARG A  1 611 ? 32.488  24.548 47.857 1.00 29.11 ? 611  ARG A CD  1 
ATOM   4719  N  NE  . ARG A  1 611 ? 31.354  24.854 46.987 1.00 29.23 ? 611  ARG A NE  1 
ATOM   4720  C  CZ  . ARG A  1 611 ? 31.446  25.319 45.739 1.00 30.44 ? 611  ARG A CZ  1 
ATOM   4721  N  NH1 . ARG A  1 611 ? 32.632  25.558 45.182 1.00 28.78 ? 611  ARG A NH1 1 
ATOM   4722  N  NH2 . ARG A  1 611 ? 30.338  25.525 45.033 1.00 29.39 ? 611  ARG A NH2 1 
ATOM   4723  N  N   . GLN A  1 612 ? 35.106  27.220 51.226 1.00 28.60 ? 612  GLN A N   1 
ATOM   4724  C  CA  . GLN A  1 612 ? 36.125  26.782 52.158 1.00 29.93 ? 612  GLN A CA  1 
ATOM   4725  C  C   . GLN A  1 612 ? 36.054  27.497 53.500 1.00 31.40 ? 612  GLN A C   1 
ATOM   4726  O  O   . GLN A  1 612 ? 36.257  26.867 54.542 1.00 32.87 ? 612  GLN A O   1 
ATOM   4727  C  CB  . GLN A  1 612 ? 37.502  26.922 51.529 1.00 29.60 ? 612  GLN A CB  1 
ATOM   4728  C  CG  . GLN A  1 612 ? 37.620  26.012 50.318 1.00 29.79 ? 612  GLN A CG  1 
ATOM   4729  C  CD  . GLN A  1 612 ? 39.024  25.577 50.043 1.00 29.62 ? 612  GLN A CD  1 
ATOM   4730  O  OE1 . GLN A  1 612 ? 39.882  25.643 50.919 1.00 29.70 ? 612  GLN A OE1 1 
ATOM   4731  N  NE2 . GLN A  1 612 ? 39.272  25.110 48.823 1.00 29.36 ? 612  GLN A NE2 1 
ATOM   4732  N  N   . PHE A  1 613 ? 35.748  28.795 53.488 1.00 30.87 ? 613  PHE A N   1 
ATOM   4733  C  CA  . PHE A  1 613 ? 35.634  29.550 54.734 1.00 31.20 ? 613  PHE A CA  1 
ATOM   4734  C  C   . PHE A  1 613 ? 34.449  29.037 55.550 1.00 31.19 ? 613  PHE A C   1 
ATOM   4735  O  O   . PHE A  1 613 ? 34.498  28.991 56.773 1.00 29.69 ? 613  PHE A O   1 
ATOM   4736  C  CB  . PHE A  1 613 ? 35.411  31.047 54.467 1.00 29.04 ? 613  PHE A CB  1 
ATOM   4737  C  CG  . PHE A  1 613 ? 36.533  31.717 53.746 1.00 28.81 ? 613  PHE A CG  1 
ATOM   4738  C  CD1 . PHE A  1 613 ? 37.850  31.353 53.987 1.00 28.85 ? 613  PHE A CD1 1 
ATOM   4739  C  CD2 . PHE A  1 613 ? 36.273  32.734 52.827 1.00 29.30 ? 613  PHE A CD2 1 
ATOM   4740  C  CE1 . PHE A  1 613 ? 38.899  31.993 53.323 1.00 30.07 ? 613  PHE A CE1 1 
ATOM   4741  C  CE2 . PHE A  1 613 ? 37.314  33.381 52.163 1.00 29.16 ? 613  PHE A CE2 1 
ATOM   4742  C  CZ  . PHE A  1 613 ? 38.622  33.015 52.402 1.00 28.61 ? 613  PHE A CZ  1 
ATOM   4743  N  N   . SER A  1 614 ? 33.378  28.670 54.860 1.00 32.50 ? 614  SER A N   1 
ATOM   4744  C  CA  . SER A  1 614 ? 32.196  28.185 55.548 1.00 34.84 ? 614  SER A CA  1 
ATOM   4745  C  C   . SER A  1 614 ? 32.508  26.871 56.246 1.00 36.45 ? 614  SER A C   1 
ATOM   4746  O  O   . SER A  1 614 ? 31.843  26.513 57.209 1.00 38.50 ? 614  SER A O   1 
ATOM   4747  C  CB  . SER A  1 614 ? 31.043  27.958 54.581 1.00 34.30 ? 614  SER A CB  1 
ATOM   4748  O  OG  . SER A  1 614 ? 31.231  26.740 53.893 1.00 33.70 ? 614  SER A OG  1 
ATOM   4749  N  N   . LYS A  1 615 ? 33.519  26.160 55.759 1.00 37.28 ? 615  LYS A N   1 
ATOM   4750  C  CA  . LYS A  1 615 ? 33.894  24.897 56.360 1.00 38.46 ? 615  LYS A CA  1 
ATOM   4751  C  C   . LYS A  1 615 ? 34.805  25.101 57.561 1.00 38.91 ? 615  LYS A C   1 
ATOM   4752  O  O   . LYS A  1 615 ? 35.226  24.137 58.200 1.00 41.01 ? 615  LYS A O   1 
ATOM   4753  C  CB  . LYS A  1 615 ? 34.590  23.992 55.343 1.00 38.32 ? 615  LYS A CB  1 
ATOM   4754  C  CG  . LYS A  1 615 ? 33.658  23.350 54.315 1.00 39.09 ? 615  LYS A CG  1 
ATOM   4755  C  CD  . LYS A  1 615 ? 34.434  22.307 53.510 1.00 40.05 ? 615  LYS A CD  1 
ATOM   4756  C  CE  . LYS A  1 615 ? 33.593  21.623 52.439 1.00 40.53 ? 615  LYS A CE  1 
ATOM   4757  N  NZ  . LYS A  1 615 ? 33.478  22.419 51.181 1.00 40.92 ? 615  LYS A NZ  1 
ATOM   4758  N  N   . MET A  1 616 ? 35.125  26.346 57.874 1.00 38.41 ? 616  MET A N   1 
ATOM   4759  C  CA  . MET A  1 616 ? 35.987  26.614 59.019 1.00 37.52 ? 616  MET A CA  1 
ATOM   4760  C  C   . MET A  1 616 ? 35.137  26.674 60.292 1.00 36.64 ? 616  MET A C   1 
ATOM   4761  O  O   . MET A  1 616 ? 33.976  27.123 60.277 1.00 36.59 ? 616  MET A O   1 
ATOM   4762  C  CB  . MET A  1 616 ? 36.777  27.920 58.816 1.00 38.14 ? 616  MET A CB  1 
ATOM   4763  C  CG  . MET A  1 616 ? 37.923  27.813 57.791 1.00 38.89 ? 616  MET A CG  1 
ATOM   4764  S  SD  . MET A  1 616 ? 38.584  29.436 57.232 1.00 41.09 ? 616  MET A SD  1 
ATOM   4765  C  CE  . MET A  1 616 ? 40.112  28.951 56.354 1.00 36.75 ? 616  MET A CE  1 
ATOM   4766  N  N   . GLY A  1 617 ? 35.727  26.208 61.386 1.00 34.84 ? 617  GLY A N   1 
ATOM   4767  C  CA  . GLY A  1 617 ? 35.033  26.169 62.658 1.00 33.02 ? 617  GLY A CA  1 
ATOM   4768  C  C   . GLY A  1 617 ? 34.450  27.463 63.177 1.00 32.08 ? 617  GLY A C   1 
ATOM   4769  O  O   . GLY A  1 617 ? 33.427  27.440 63.858 1.00 32.96 ? 617  GLY A O   1 
ATOM   4770  N  N   . PHE A  1 618 ? 35.066  28.594 62.855 1.00 30.53 ? 618  PHE A N   1 
ATOM   4771  C  CA  . PHE A  1 618 ? 34.567  29.875 63.362 1.00 28.96 ? 618  PHE A CA  1 
ATOM   4772  C  C   . PHE A  1 618 ? 33.623  30.643 62.429 1.00 27.62 ? 618  PHE A C   1 
ATOM   4773  O  O   . PHE A  1 618 ? 33.308  31.809 62.680 1.00 27.52 ? 618  PHE A O   1 
ATOM   4774  C  CB  . PHE A  1 618 ? 35.757  30.756 63.781 1.00 28.29 ? 618  PHE A CB  1 
ATOM   4775  C  CG  . PHE A  1 618 ? 36.808  30.887 62.721 1.00 30.09 ? 618  PHE A CG  1 
ATOM   4776  C  CD1 . PHE A  1 618 ? 36.647  31.778 61.661 1.00 30.46 ? 618  PHE A CD1 1 
ATOM   4777  C  CD2 . PHE A  1 618 ? 37.939  30.086 62.749 1.00 30.03 ? 618  PHE A CD2 1 
ATOM   4778  C  CE1 . PHE A  1 618 ? 37.598  31.861 60.641 1.00 29.88 ? 618  PHE A CE1 1 
ATOM   4779  C  CE2 . PHE A  1 618 ? 38.899  30.160 61.734 1.00 29.80 ? 618  PHE A CE2 1 
ATOM   4780  C  CZ  . PHE A  1 618 ? 38.726  31.051 60.682 1.00 30.75 ? 618  PHE A CZ  1 
ATOM   4781  N  N   . VAL A  1 619 ? 33.150  29.984 61.374 1.00 26.54 ? 619  VAL A N   1 
ATOM   4782  C  CA  . VAL A  1 619 ? 32.235  30.629 60.438 1.00 26.09 ? 619  VAL A CA  1 
ATOM   4783  C  C   . VAL A  1 619 ? 30.814  30.048 60.502 1.00 25.68 ? 619  VAL A C   1 
ATOM   4784  O  O   . VAL A  1 619 ? 30.633  28.837 60.489 1.00 25.23 ? 619  VAL A O   1 
ATOM   4785  C  CB  . VAL A  1 619 ? 32.760  30.504 58.992 1.00 26.07 ? 619  VAL A CB  1 
ATOM   4786  C  CG1 . VAL A  1 619 ? 31.782  31.132 58.014 1.00 25.15 ? 619  VAL A CG1 1 
ATOM   4787  C  CG2 . VAL A  1 619 ? 34.116  31.186 58.880 1.00 25.90 ? 619  VAL A CG2 1 
ATOM   4788  N  N   . ASP A  1 620 ? 29.802  30.904 60.581 1.00 25.12 ? 620  ASP A N   1 
ATOM   4789  C  CA  . ASP A  1 620 ? 28.417  30.420 60.611 1.00 25.28 ? 620  ASP A CA  1 
ATOM   4790  C  C   . ASP A  1 620 ? 27.938  30.266 59.161 1.00 26.29 ? 620  ASP A C   1 
ATOM   4791  O  O   . ASP A  1 620 ? 27.561  31.259 58.519 1.00 25.95 ? 620  ASP A O   1 
ATOM   4792  C  CB  . ASP A  1 620 ? 27.533  31.427 61.336 1.00 26.55 ? 620  ASP A CB  1 
ATOM   4793  C  CG  . ASP A  1 620 ? 26.062  31.024 61.334 1.00 26.38 ? 620  ASP A CG  1 
ATOM   4794  O  OD1 . ASP A  1 620 ? 25.695  30.018 60.675 1.00 27.22 ? 620  ASP A OD1 1 
ATOM   4795  O  OD2 . ASP A  1 620 ? 25.278  31.732 61.989 1.00 25.67 ? 620  ASP A OD2 1 
ATOM   4796  N  N   . ASN A  1 621 ? 27.927  29.031 58.652 1.00 26.35 ? 621  ASN A N   1 
ATOM   4797  C  CA  . ASN A  1 621 ? 27.554  28.796 57.260 1.00 26.92 ? 621  ASN A CA  1 
ATOM   4798  C  C   . ASN A  1 621 ? 26.141  29.219 56.883 1.00 27.78 ? 621  ASN A C   1 
ATOM   4799  O  O   . ASN A  1 621 ? 25.770  29.182 55.714 1.00 26.74 ? 621  ASN A O   1 
ATOM   4800  C  CB  . ASN A  1 621 ? 27.814  27.329 56.855 1.00 28.73 ? 621  ASN A CB  1 
ATOM   4801  C  CG  . ASN A  1 621 ? 26.751  26.353 57.369 1.00 31.77 ? 621  ASN A CG  1 
ATOM   4802  O  OD1 . ASN A  1 621 ? 26.887  25.138 57.173 1.00 33.17 ? 621  ASN A OD1 1 
ATOM   4803  N  ND2 . ASN A  1 621 ? 25.693  26.868 58.012 1.00 31.25 ? 621  ASN A ND2 1 
ATOM   4804  N  N   . LYS A  1 622 ? 25.360  29.638 57.871 1.00 28.50 ? 622  LYS A N   1 
ATOM   4805  C  CA  . LYS A  1 622 ? 24.005  30.087 57.594 1.00 29.46 ? 622  LYS A CA  1 
ATOM   4806  C  C   . LYS A  1 622 ? 24.009  31.590 57.378 1.00 28.45 ? 622  LYS A C   1 
ATOM   4807  O  O   . LYS A  1 622 ? 23.023  32.160 56.904 1.00 28.74 ? 622  LYS A O   1 
ATOM   4808  C  CB  . LYS A  1 622 ? 23.062  29.723 58.745 1.00 31.37 ? 622  LYS A CB  1 
ATOM   4809  C  CG  . LYS A  1 622 ? 22.792  28.227 58.863 1.00 35.50 ? 622  LYS A CG  1 
ATOM   4810  C  CD  . LYS A  1 622 ? 21.666  27.923 59.871 1.00 40.50 ? 622  LYS A CD  1 
ATOM   4811  C  CE  . LYS A  1 622 ? 22.006  28.377 61.295 1.00 41.71 ? 622  LYS A CE  1 
ATOM   4812  N  NZ  . LYS A  1 622 ? 23.243  27.721 61.819 1.00 44.22 ? 622  LYS A NZ  1 
ATOM   4813  N  N   . ARG A  1 623 ? 25.121  32.235 57.725 1.00 27.16 ? 623  ARG A N   1 
ATOM   4814  C  CA  . ARG A  1 623 ? 25.229  33.683 57.557 1.00 24.75 ? 623  ARG A CA  1 
ATOM   4815  C  C   . ARG A  1 623 ? 26.478  34.126 56.801 1.00 22.89 ? 623  ARG A C   1 
ATOM   4816  O  O   . ARG A  1 623 ? 27.423  34.665 57.365 1.00 22.48 ? 623  ARG A O   1 
ATOM   4817  C  CB  . ARG A  1 623 ? 25.162  34.373 58.913 1.00 25.19 ? 623  ARG A CB  1 
ATOM   4818  C  CG  . ARG A  1 623 ? 23.808  34.251 59.577 1.00 27.79 ? 623  ARG A CG  1 
ATOM   4819  C  CD  . ARG A  1 623 ? 23.995  34.136 61.086 1.00 29.78 ? 623  ARG A CD  1 
ATOM   4820  N  NE  . ARG A  1 623 ? 24.099  35.410 61.756 1.00 29.79 ? 623  ARG A NE  1 
ATOM   4821  C  CZ  . ARG A  1 623 ? 24.751  35.613 62.899 1.00 29.05 ? 623  ARG A CZ  1 
ATOM   4822  N  NH1 . ARG A  1 623 ? 25.375  34.616 63.498 1.00 26.57 ? 623  ARG A NH1 1 
ATOM   4823  N  NH2 . ARG A  1 623 ? 24.753  36.823 63.454 1.00 28.24 ? 623  ARG A NH2 1 
ATOM   4824  N  N   . ILE A  1 624 ? 26.484  33.869 55.510 1.00 21.40 ? 624  ILE A N   1 
ATOM   4825  C  CA  . ILE A  1 624 ? 27.591  34.297 54.688 1.00 22.44 ? 624  ILE A CA  1 
ATOM   4826  C  C   . ILE A  1 624 ? 27.002  35.229 53.632 1.00 22.04 ? 624  ILE A C   1 
ATOM   4827  O  O   . ILE A  1 624 ? 26.004  34.904 52.974 1.00 21.98 ? 624  ILE A O   1 
ATOM   4828  C  CB  . ILE A  1 624 ? 28.288  33.119 54.013 1.00 22.50 ? 624  ILE A CB  1 
ATOM   4829  C  CG1 . ILE A  1 624 ? 28.879  32.205 55.083 1.00 22.31 ? 624  ILE A CG1 1 
ATOM   4830  C  CG2 . ILE A  1 624 ? 29.379  33.641 53.067 1.00 22.95 ? 624  ILE A CG2 1 
ATOM   4831  C  CD1 . ILE A  1 624 ? 29.415  30.915 54.546 1.00 24.26 ? 624  ILE A CD1 1 
ATOM   4832  N  N   . ALA A  1 625 ? 27.607  36.399 53.499 1.00 20.01 ? 625  ALA A N   1 
ATOM   4833  C  CA  . ALA A  1 625 ? 27.141  37.375 52.542 1.00 18.96 ? 625  ALA A CA  1 
ATOM   4834  C  C   . ALA A  1 625 ? 28.289  37.760 51.625 1.00 18.64 ? 625  ALA A C   1 
ATOM   4835  O  O   . ALA A  1 625 ? 29.432  37.350 51.833 1.00 18.60 ? 625  ALA A O   1 
ATOM   4836  C  CB  . ALA A  1 625 ? 26.608  38.601 53.275 1.00 17.82 ? 625  ALA A CB  1 
ATOM   4837  N  N   . ILE A  1 626 ? 27.983  38.561 50.613 1.00 17.94 ? 626  ILE A N   1 
ATOM   4838  C  CA  . ILE A  1 626 ? 28.991  38.998 49.668 1.00 16.98 ? 626  ILE A CA  1 
ATOM   4839  C  C   . ILE A  1 626 ? 28.631  40.396 49.174 1.00 17.23 ? 626  ILE A C   1 
ATOM   4840  O  O   . ILE A  1 626 ? 27.452  40.705 48.989 1.00 18.55 ? 626  ILE A O   1 
ATOM   4841  C  CB  . ILE A  1 626 ? 29.082  37.997 48.475 1.00 17.76 ? 626  ILE A CB  1 
ATOM   4842  C  CG1 . ILE A  1 626 ? 30.137  38.448 47.467 1.00 16.64 ? 626  ILE A CG1 1 
ATOM   4843  C  CG2 . ILE A  1 626 ? 27.734  37.863 47.802 1.00 15.65 ? 626  ILE A CG2 1 
ATOM   4844  C  CD1 . ILE A  1 626 ? 30.451  37.396 46.440 1.00 18.10 ? 626  ILE A CD1 1 
ATOM   4845  N  N   . TRP A  1 627 ? 29.638  41.251 48.973 1.00 16.66 ? 627  TRP A N   1 
ATOM   4846  C  CA  . TRP A  1 627 ? 29.402  42.624 48.451 1.00 16.86 ? 627  TRP A CA  1 
ATOM   4847  C  C   . TRP A  1 627 ? 30.573  43.166 47.626 1.00 17.49 ? 627  TRP A C   1 
ATOM   4848  O  O   . TRP A  1 627 ? 31.720  42.787 47.833 1.00 17.45 ? 627  TRP A O   1 
ATOM   4849  C  CB  . TRP A  1 627 ? 29.073  43.588 49.569 1.00 16.29 ? 627  TRP A CB  1 
ATOM   4850  C  CG  . TRP A  1 627 ? 30.211  44.395 50.101 1.00 18.43 ? 627  TRP A CG  1 
ATOM   4851  C  CD1 . TRP A  1 627 ? 31.161  43.998 51.007 1.00 18.59 ? 627  TRP A CD1 1 
ATOM   4852  C  CD2 . TRP A  1 627 ? 30.504  45.763 49.793 1.00 17.56 ? 627  TRP A CD2 1 
ATOM   4853  N  NE1 . TRP A  1 627 ? 32.013  45.027 51.288 1.00 17.37 ? 627  TRP A NE1 1 
ATOM   4854  C  CE2 . TRP A  1 627 ? 31.637  46.128 50.565 1.00 18.36 ? 627  TRP A CE2 1 
ATOM   4855  C  CE3 . TRP A  1 627 ? 29.924  46.714 48.951 1.00 16.67 ? 627  TRP A CE3 1 
ATOM   4856  C  CZ2 . TRP A  1 627 ? 32.203  47.420 50.525 1.00 17.47 ? 627  TRP A CZ2 1 
ATOM   4857  C  CZ3 . TRP A  1 627 ? 30.482  47.999 48.905 1.00 18.16 ? 627  TRP A CZ3 1 
ATOM   4858  C  CH2 . TRP A  1 627 ? 31.611  48.340 49.693 1.00 18.42 ? 627  TRP A CH2 1 
ATOM   4859  N  N   . GLY A  1 628 ? 30.277  44.092 46.707 1.00 15.39 ? 628  GLY A N   1 
ATOM   4860  C  CA  . GLY A  1 628 ? 31.285  44.661 45.819 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  46.192 44.969 1.00 14.68 ? 628  GLY A O   1 
ATOM   4863  N  N   . TRP A  1 629 ? 31.785  46.708 44.637 1.00 15.58 ? 629  TRP A N   1 
ATOM   4864  C  CA  . TRP A  1 629 ? 31.502  47.931 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 17.88 ? 629  TRP A C   1 
ATOM   4866  O  O   . TRP A  1 629 ? 33.307  47.417 42.495 1.00 17.57 ? 629  TRP A O   1 
ATOM   4867  C  CB  . TRP A  1 629 ? 32.048  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  51.462 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 17.56 ? 630  SER A N   1 
ATOM   4878  C  CA  . SER A  1 630 ? 32.158  48.454 40.231 1.00 18.11 ? 630  SER A CA  1 
ATOM   4879  C  C   . SER A  1 630 ? 32.389  47.015 39.707 1.00 17.45 ? 630  SER A C   1 
ATOM   4880  O  O   . SER A  1 630 ? 31.459  46.212 39.637 1.00 17.49 ? 630  SER A O   1 
ATOM   4881  C  CB  . SER A  1 630 ? 33.493  49.180 40.291 1.00 17.77 ? 630  SER A CB  1 
ATOM   4882  O  OG  . SER A  1 630 ? 33.801  49.791 39.055 1.00 18.32 ? 630  SER A OG  1 
ATOM   4883  N  N   . TYR A  1 631 ? 33.628  46.674 39.324 1.00 17.73 ? 631  TYR A N   1 
ATOM   4884  C  CA  . TYR A  1 631 ? 33.870  45.298 38.909 1.00 17.32 ? 631  TYR A CA  1 
ATOM   4885  C  C   . TYR A  1 631 ? 33.395  44.385 40.041 1.00 16.70 ? 631  TYR A C   1 
ATOM   4886  O  O   . TYR A  1 631 ? 32.893  43.296 39.805 1.00 17.39 ? 631  TYR A O   1 
ATOM   4887  C  CB  . TYR A  1 631 ? 35.353  45.049 38.621 1.00 16.19 ? 631  TYR A CB  1 
ATOM   4888  C  CG  . TYR A  1 631 ? 35.590  43.822 37.762 1.00 17.49 ? 631  TYR A CG  1 
ATOM   4889  C  CD1 . TYR A  1 631 ? 35.411  42.526 38.271 1.00 17.28 ? 631  TYR A CD1 1 
ATOM   4890  C  CD2 . TYR A  1 631 ? 35.944  43.958 36.414 1.00 17.62 ? 631  TYR A CD2 1 
ATOM   4891  C  CE1 . TYR A  1 631 ? 35.574  41.392 37.451 1.00 17.49 ? 631  TYR A CE1 1 
ATOM   4892  C  CE2 . TYR A  1 631 ? 36.110  42.845 35.592 1.00 18.41 ? 631  TYR A CE2 1 
ATOM   4893  C  CZ  . TYR A  1 631 ? 35.922  41.562 36.117 1.00 18.91 ? 631  TYR A CZ  1 
ATOM   4894  O  OH  . TYR A  1 631 ? 36.077  40.477 35.298 1.00 18.76 ? 631  TYR A OH  1 
ATOM   4895  N  N   . GLY A  1 632 ? 33.529  44.850 41.275 1.00 17.10 ? 632  GLY A N   1 
ATOM   4896  C  CA  . GLY A  1 632 ? 33.116  44.044 42.396 1.00 18.61 ? 632  GLY A CA  1 
ATOM   4897  C  C   . GLY A  1 632 ? 31.601  43.868 42.437 1.00 18.39 ? 632  GLY A C   1 
ATOM   4898  O  O   . GLY A  1 632 ? 31.101  42.889 42.982 1.00 18.18 ? 632  GLY A O   1 
ATOM   4899  N  N   . GLY A  1 633 ? 30.862  44.796 41.857 1.00 19.23 ? 633  GLY A N   1 
ATOM   4900  C  CA  . GLY A  1 633 ? 29.444  44.646 41.846 1.00 19.23 ? 633  GLY A CA  1 
ATOM   4901  C  C   . GLY A  1 633 ? 29.060  43.517 40.874 1.00 16.51 ? 633  GLY A C   1 
ATOM   4902  O  O   . GLY A  1 633 ? 28.139  42.734 41.118 1.00 16.52 ? 633  GLY A O   1 
ATOM   4903  N  N   . TYR A  1 634 ? 29.777  43.449 39.778 1.00 16.56 ? 634  TYR A N   1 
ATOM   4904  C  CA  . TYR A  1 634 ? 29.552  42.448 38.746 1.00 16.55 ? 634  TYR A CA  1 
ATOM   4905  C  C   . TYR A  1 634 ? 29.756  41.030 39.307 1.00 16.88 ? 634  TYR A C   1 
ATOM   4906  O  O   . TYR A  1 634 ? 28.878  40.182 39.158 1.00 18.25 ? 634  TYR A O   1 
ATOM   4907  C  CB  . TYR A  1 634 ? 30.496  42.689 37.564 1.00 14.63 ? 634  TYR A CB  1 
ATOM   4908  C  CG  . TYR A  1 634 ? 30.536  41.584 36.528 1.00 15.35 ? 634  TYR A CG  1 
ATOM   4909  C  CD1 . TYR A  1 634 ? 29.428  41.288 35.734 1.00 14.29 ? 634  TYR A CD1 1 
ATOM   4910  C  CD2 . TYR A  1 634 ? 31.710  40.862 36.306 1.00 16.11 ? 634  TYR A CD2 1 
ATOM   4911  C  CE1 . TYR A  1 634 ? 29.496  40.292 34.733 1.00 15.96 ? 634  TYR A CE1 1 
ATOM   4912  C  CE2 . TYR A  1 634 ? 31.788  39.876 35.319 1.00 15.97 ? 634  TYR A CE2 1 
ATOM   4913  C  CZ  . TYR A  1 634 ? 30.685  39.594 34.532 1.00 16.98 ? 634  TYR A CZ  1 
ATOM   4914  O  OH  . TYR A  1 634 ? 30.777  38.632 33.544 1.00 16.85 ? 634  TYR A OH  1 
ATOM   4915  N  N   . VAL A  1 635 ? 30.907  40.787 39.935 1.00 16.28 ? 635  VAL A N   1 
ATOM   4916  C  CA  . VAL A  1 635 ? 31.214  39.468 40.485 1.00 16.18 ? 635  VAL A CA  1 
ATOM   4917  C  C   . VAL A  1 635 ? 30.238  39.063 41.578 1.00 16.26 ? 635  VAL A C   1 
ATOM   4918  O  O   . VAL A  1 635 ? 29.847  37.898 41.654 1.00 15.94 ? 635  VAL A O   1 
ATOM   4919  C  CB  . VAL A  1 635 ? 32.661  39.403 41.037 1.00 16.20 ? 635  VAL A CB  1 
ATOM   4920  C  CG1 . VAL A  1 635 ? 32.873  38.110 41.822 1.00 16.48 ? 635  VAL A CG1 1 
ATOM   4921  C  CG2 . VAL A  1 635 ? 33.660  39.529 39.893 1.00 13.69 ? 635  VAL A CG2 1 
ATOM   4922  N  N   . THR A  1 636 ? 29.852  40.024 42.419 1.00 16.60 ? 636  THR A N   1 
ATOM   4923  C  CA  . THR A  1 636 ? 28.893  39.779 43.483 1.00 17.52 ? 636  THR A CA  1 
ATOM   4924  C  C   . THR A  1 636 ? 27.561  39.347 42.862 1.00 19.31 ? 636  THR A C   1 
ATOM   4925  O  O   . THR A  1 636 ? 26.893  38.438 43.360 1.00 20.73 ? 636  THR A O   1 
ATOM   4926  C  CB  . THR A  1 636 ? 28.654  41.042 44.327 1.00 17.01 ? 636  THR A CB  1 
ATOM   4927  O  OG1 . THR A  1 636 ? 29.784  41.269 45.180 1.00 19.98 ? 636  THR A OG1 1 
ATOM   4928  C  CG2 . THR A  1 636 ? 27.408  40.876 45.181 1.00 15.83 ? 636  THR A CG2 1 
ATOM   4929  N  N   . SER A  1 637 ? 27.186  40.000 41.765 1.00 19.24 ? 637  SER A N   1 
ATOM   4930  C  CA  . SER A  1 637 ? 25.940  39.672 41.087 1.00 20.04 ? 637  SER A CA  1 
ATOM   4931  C  C   . SER A  1 637 ? 26.017  38.325 40.374 1.00 19.65 ? 637  SER A C   1 
ATOM   4932  O  O   . SER A  1 637 ? 25.050  37.567 40.399 1.00 21.03 ? 637  SER A O   1 
ATOM   4933  C  CB  . SER A  1 637 ? 25.558  40.767 40.074 1.00 19.90 ? 637  SER A CB  1 
ATOM   4934  O  OG  . SER A  1 637 ? 25.293  42.001 40.713 1.00 17.20 ? 637  SER A OG  1 
ATOM   4935  N  N   . MET A  1 638 ? 27.142  38.036 39.729 1.00 18.31 ? 638  MET A N   1 
ATOM   4936  C  CA  . MET A  1 638 ? 27.311  36.758 39.028 1.00 18.79 ? 638  MET A CA  1 
ATOM   4937  C  C   . MET A  1 638 ? 27.318  35.611 40.048 1.00 20.20 ? 638  MET A C   1 
ATOM   4938  O  O   . MET A  1 638 ? 26.836  34.500 39.773 1.00 19.83 ? 638  MET A O   1 
ATOM   4939  C  CB  . MET A  1 638 ? 28.623  36.752 38.252 1.00 17.49 ? 638  MET A CB  1 
ATOM   4940  C  CG  . MET A  1 638 ? 28.659  37.721 37.074 1.00 15.67 ? 638  MET A CG  1 
ATOM   4941  S  SD  . MET A  1 638 ? 27.561  37.167 35.727 1.00 18.58 ? 638  MET A SD  1 
ATOM   4942  C  CE  . MET A  1 638 ? 28.628  36.017 34.854 1.00 10.82 ? 638  MET A CE  1 
ATOM   4943  N  N   . VAL A  1 639 ? 27.848  35.892 41.238 1.00 19.81 ? 639  VAL A N   1 
ATOM   4944  C  CA  . VAL A  1 639 ? 27.906  34.887 42.296 1.00 19.33 ? 639  VAL A CA  1 
ATOM   4945  C  C   . VAL A  1 639 ? 26.501  34.588 42.826 1.00 19.22 ? 639  VAL A C   1 
ATOM   4946  O  O   . VAL A  1 639 ? 26.076  33.437 42.892 1.00 18.86 ? 639  VAL A O   1 
ATOM   4947  C  CB  . VAL A  1 639 ? 28.798  35.361 43.466 1.00 19.32 ? 639  VAL A CB  1 
ATOM   4948  C  CG1 . VAL A  1 639 ? 28.537  34.507 44.711 1.00 19.09 ? 639  VAL A CG1 1 
ATOM   4949  C  CG2 . VAL A  1 639 ? 30.260  35.256 43.077 1.00 17.62 ? 639  VAL A CG2 1 
ATOM   4950  N  N   . LEU A  1 640 ? 25.790  35.641 43.197 1.00 19.51 ? 640  LEU A N   1 
ATOM   4951  C  CA  . LEU A  1 640 ? 24.451  35.490 43.717 1.00 19.64 ? 640  LEU A CA  1 
ATOM   4952  C  C   . LEU A  1 640 ? 23.534  34.816 42.700 1.00 20.14 ? 640  LEU A C   1 
ATOM   4953  O  O   . LEU A  1 640 ? 22.556  34.171 43.074 1.00 20.76 ? 640  LEU A O   1 
ATOM   4954  C  CB  . LEU A  1 640 ? 23.879  36.844 44.103 1.00 17.95 ? 640  LEU A CB  1 
ATOM   4955  C  CG  . LEU A  1 640 ? 24.498  37.513 45.310 1.00 19.32 ? 640  LEU A CG  1 
ATOM   4956  C  CD1 . LEU A  1 640 ? 23.894  38.937 45.488 1.00 16.28 ? 640  LEU A CD1 1 
ATOM   4957  C  CD2 . LEU A  1 640 ? 24.239  36.636 46.525 1.00 16.84 ? 640  LEU A CD2 1 
ATOM   4958  N  N   . GLY A  1 641 ? 23.839  34.980 41.418 1.00 20.47 ? 641  GLY A N   1 
ATOM   4959  C  CA  . GLY A  1 641 ? 23.022  34.372 40.378 1.00 20.35 ? 641  GLY A CA  1 
ATOM   4960  C  C   . GLY A  1 641 ? 23.589  33.060 39.872 1.00 21.06 ? 641  GLY A C   1 
ATOM   4961  O  O   . GLY A  1 641 ? 23.187  32.570 38.816 1.00 21.23 ? 641  GLY A O   1 
ATOM   4962  N  N   . SER A  1 642 ? 24.521  32.482 40.624 1.00 20.96 ? 642  SER A N   1 
ATOM   4963  C  CA  . SER A  1 642 ? 25.151  31.226 40.230 1.00 22.06 ? 642  SER A CA  1 
ATOM   4964  C  C   . SER A  1 642 ? 24.415  29.962 40.673 1.00 22.34 ? 642  SER A C   1 
ATOM   4965  O  O   . SER A  1 642 ? 24.642  28.904 40.112 1.00 24.06 ? 642  SER A O   1 
ATOM   4966  C  CB  . SER A  1 642 ? 26.574  31.152 40.787 1.00 22.57 ? 642  SER A CB  1 
ATOM   4967  O  OG  . SER A  1 642 ? 26.547  30.992 42.191 1.00 22.33 ? 642  SER A OG  1 
ATOM   4968  N  N   . GLY A  1 643 ? 23.549  30.065 41.674 1.00 22.80 ? 643  GLY A N   1 
ATOM   4969  C  CA  . GLY A  1 643 ? 22.849  28.886 42.171 1.00 22.34 ? 643  GLY A CA  1 
ATOM   4970  C  C   . GLY A  1 643 ? 23.708  28.068 43.140 1.00 23.15 ? 643  GLY A C   1 
ATOM   4971  O  O   . GLY A  1 643 ? 23.359  26.939 43.497 1.00 22.46 ? 643  GLY A O   1 
ATOM   4972  N  N   . SER A  1 644 ? 24.826  28.645 43.590 1.00 20.95 ? 644  SER A N   1 
ATOM   4973  C  CA  . SER A  1 644 ? 25.729  27.941 44.496 1.00 20.72 ? 644  SER A CA  1 
ATOM   4974  C  C   . SER A  1 644 ? 25.109  27.627 45.858 1.00 20.07 ? 644  SER A C   1 
ATOM   4975  O  O   . SER A  1 644 ? 25.504  26.662 46.514 1.00 19.70 ? 644  SER A O   1 
ATOM   4976  C  CB  . SER A  1 644 ? 27.013  28.741 44.717 1.00 19.03 ? 644  SER A CB  1 
ATOM   4977  O  OG  . SER A  1 644 ? 26.837  29.627 45.807 1.00 18.26 ? 644  SER A OG  1 
ATOM   4978  N  N   . GLY A  1 645 ? 24.163  28.452 46.292 1.00 19.65 ? 645  GLY A N   1 
ATOM   4979  C  CA  . GLY A  1 645 ? 23.514  28.221 47.573 1.00 18.41 ? 645  GLY A CA  1 
ATOM   4980  C  C   . GLY A  1 645 ? 24.368  28.555 48.791 1.00 19.43 ? 645  GLY A C   1 
ATOM   4981  O  O   . GLY A  1 645 ? 23.942  28.377 49.930 1.00 19.62 ? 645  GLY A O   1 
ATOM   4982  N  N   . VAL A  1 646 ? 25.574  29.061 48.560 1.00 20.10 ? 646  VAL A N   1 
ATOM   4983  C  CA  . VAL A  1 646 ? 26.489  29.409 49.649 1.00 18.83 ? 646  VAL A CA  1 
ATOM   4984  C  C   . VAL A  1 646 ? 26.168  30.740 50.340 1.00 21.37 ? 646  VAL A C   1 
ATOM   4985  O  O   . VAL A  1 646 ? 26.354  30.893 51.559 1.00 21.32 ? 646  VAL A O   1 
ATOM   4986  C  CB  . VAL A  1 646 ? 27.925  29.496 49.116 1.00 19.06 ? 646  VAL A CB  1 
ATOM   4987  C  CG1 . VAL A  1 646 ? 28.884  29.911 50.235 1.00 18.25 ? 646  VAL A CG1 1 
ATOM   4988  C  CG2 . VAL A  1 646 ? 28.322  28.145 48.498 1.00 16.34 ? 646  VAL A CG2 1 
ATOM   4989  N  N   . PHE A  1 647 ? 25.672  31.705 49.567 1.00 19.87 ? 647  PHE A N   1 
ATOM   4990  C  CA  . PHE A  1 647 ? 25.407  33.020 50.123 1.00 20.11 ? 647  PHE A CA  1 
ATOM   4991  C  C   . PHE A  1 647 ? 23.947  33.291 50.450 1.00 21.00 ? 647  PHE A C   1 
ATOM   4992  O  O   . PHE A  1 647 ? 23.039  32.904 49.706 1.00 21.68 ? 647  PHE A O   1 
ATOM   4993  C  CB  . PHE A  1 647 ? 25.930  34.089 49.157 1.00 19.66 ? 647  PHE A CB  1 
ATOM   4994  C  CG  . PHE A  1 647 ? 27.394  33.924 48.815 1.00 18.54 ? 647  PHE A CG  1 
ATOM   4995  C  CD1 . PHE A  1 647 ? 28.374  34.592 49.545 1.00 18.55 ? 647  PHE A CD1 1 
ATOM   4996  C  CD2 . PHE A  1 647 ? 27.790  33.030 47.822 1.00 16.68 ? 647  PHE A CD2 1 
ATOM   4997  C  CE1 . PHE A  1 647 ? 29.733  34.368 49.297 1.00 18.68 ? 647  PHE A CE1 1 
ATOM   4998  C  CE2 . PHE A  1 647 ? 29.143  32.795 47.560 1.00 17.46 ? 647  PHE A CE2 1 
ATOM   4999  C  CZ  . PHE A  1 647 ? 30.113  33.465 48.302 1.00 17.84 ? 647  PHE A CZ  1 
ATOM   5000  N  N   . LYS A  1 648 ? 23.721  33.971 51.565 1.00 19.63 ? 648  LYS A N   1 
ATOM   5001  C  CA  . LYS A  1 648 ? 22.357  34.306 51.946 1.00 21.44 ? 648  LYS A CA  1 
ATOM   5002  C  C   . LYS A  1 648 ? 21.894  35.655 51.374 1.00 21.13 ? 648  LYS A C   1 
ATOM   5003  O  O   . LYS A  1 648 ? 20.710  35.851 51.121 1.00 20.02 ? 648  LYS A O   1 
ATOM   5004  C  CB  . LYS A  1 648 ? 22.220  34.338 53.467 1.00 20.36 ? 648  LYS A CB  1 
ATOM   5005  C  CG  . LYS A  1 648 ? 20.841  34.777 53.923 1.00 22.77 ? 648  LYS A CG  1 
ATOM   5006  C  CD  . LYS A  1 648 ? 20.675  34.698 55.439 1.00 25.09 ? 648  LYS A CD  1 
ATOM   5007  C  CE  . LYS A  1 648 ? 19.364  35.339 55.864 1.00 26.82 ? 648  LYS A CE  1 
ATOM   5008  N  NZ  . LYS A  1 648 ? 19.061  35.020 57.274 1.00 29.62 ? 648  LYS A NZ  1 
ATOM   5009  N  N   . CYS A  1 649 ? 22.833  36.574 51.171 1.00 21.07 ? 649  CYS A N   1 
ATOM   5010  C  CA  . CYS A  1 649 ? 22.488  37.895 50.682 1.00 22.22 ? 649  CYS A CA  1 
ATOM   5011  C  C   . CYS A  1 649 ? 23.713  38.562 50.075 1.00 21.45 ? 649  CYS A C   1 
ATOM   5012  O  O   . CYS A  1 649 ? 24.847  38.118 50.312 1.00 21.45 ? 649  CYS A O   1 
ATOM   5013  C  CB  . CYS A  1 649 ? 21.947  38.749 51.835 1.00 24.30 ? 649  CYS A CB  1 
ATOM   5014  S  SG  . CYS A  1 649 ? 23.125  38.913 53.222 1.00 31.14 ? 649  CYS A SG  1 
ATOM   5015  N  N   . GLY A  1 650 ? 23.496  39.626 49.299 1.00 18.66 ? 650  GLY A N   1 
ATOM   5016  C  CA  . GLY A  1 650 ? 24.616  40.309 48.678 1.00 17.44 ? 650  GLY A CA  1 
ATOM   5017  C  C   . GLY A  1 650 ? 24.282  41.718 48.253 1.00 17.04 ? 650  GLY A C   1 
ATOM   5018  O  O   . GLY A  1 650 ? 23.124  42.056 48.016 1.00 16.46 ? 650  GLY A O   1 
ATOM   5019  N  N   . ILE A  1 651 ? 25.304  42.550 48.156 1.00 16.31 ? 651  ILE A N   1 
ATOM   5020  C  CA  . ILE A  1 651 ? 25.099  43.922 47.752 1.00 15.64 ? 651  ILE A CA  1 
ATOM   5021  C  C   . ILE A  1 651 ? 26.014  44.246 46.585 1.00 15.29 ? 651  ILE A C   1 
ATOM   5022  O  O   . ILE A  1 651 ? 27.227  44.056 46.664 1.00 15.49 ? 651  ILE A O   1 
ATOM   5023  C  CB  . ILE A  1 651 ? 25.411  44.930 48.902 1.00 15.35 ? 651  ILE A CB  1 
ATOM   5024  C  CG1 . ILE A  1 651 ? 24.714  44.484 50.192 1.00 14.94 ? 651  ILE A CG1 1 
ATOM   5025  C  CG2 . ILE A  1 651 ? 24.966  46.348 48.490 1.00 12.09 ? 651  ILE A CG2 1 
ATOM   5026  C  CD1 . ILE A  1 651 ? 24.827  45.489 51.352 1.00 13.52 ? 651  ILE A CD1 1 
ATOM   5027  N  N   . ALA A  1 652 ? 25.417  44.733 45.509 1.00 15.03 ? 652  ALA A N   1 
ATOM   5028  C  CA  . ALA A  1 652 ? 26.155  45.123 44.315 1.00 15.09 ? 652  ALA A CA  1 
ATOM   5029  C  C   . ALA A  1 652 ? 26.007  46.640 44.130 1.00 14.92 ? 652  ALA A C   1 
ATOM   5030  O  O   . ALA A  1 652 ? 24.888  47.138 44.027 1.00 16.04 ? 652  ALA A O   1 
ATOM   5031  C  CB  . ALA A  1 652 ? 25.598  44.378 43.087 1.00 12.65 ? 652  ALA A CB  1 
ATOM   5032  N  N   . VAL A  1 653 ? 27.130  47.362 44.095 1.00 15.01 ? 653  VAL A N   1 
ATOM   5033  C  CA  . VAL A  1 653 ? 27.114  48.812 43.905 1.00 15.08 ? 653  VAL A CA  1 
ATOM   5034  C  C   . VAL A  1 653 ? 27.721  49.162 42.540 1.00 15.81 ? 653  VAL A C   1 
ATOM   5035  O  O   . VAL A  1 653 ? 28.844  48.744 42.240 1.00 14.54 ? 653  VAL A O   1 
ATOM   5036  C  CB  . VAL A  1 653 ? 27.940  49.547 45.001 1.00 15.73 ? 653  VAL A CB  1 
ATOM   5037  C  CG1 . VAL A  1 653 ? 27.797  51.054 44.827 1.00 15.40 ? 653  VAL A CG1 1 
ATOM   5038  C  CG2 . VAL A  1 653 ? 27.445  49.156 46.395 1.00 15.23 ? 653  VAL A CG2 1 
ATOM   5039  N  N   . ALA A  1 654 ? 26.985  49.927 41.727 1.00 15.79 ? 654  ALA A N   1 
ATOM   5040  C  CA  . ALA A  1 654 ? 27.446  50.333 40.387 1.00 15.86 ? 654  ALA A CA  1 
ATOM   5041  C  C   . ALA A  1 654 ? 28.138  49.167 39.658 1.00 15.56 ? 654  ALA A C   1 
ATOM   5042  O  O   . ALA A  1 654 ? 29.288  49.277 39.220 1.00 16.65 ? 654  ALA A O   1 
ATOM   5043  C  CB  . ALA A  1 654 ? 28.412  51.523 40.502 1.00 14.56 ? 654  ALA A CB  1 
ATOM   5044  N  N   . PRO A  1 655 ? 27.448  48.027 39.519 1.00 16.39 ? 655  PRO A N   1 
ATOM   5045  C  CA  . PRO A  1 655 ? 28.097  46.906 38.833 1.00 14.91 ? 655  PRO A CA  1 
ATOM   5046  C  C   . PRO A  1 655 ? 28.005  46.961 37.331 1.00 16.00 ? 655  PRO A C   1 
ATOM   5047  O  O   . PRO A  1 655 ? 27.149  47.636 36.777 1.00 15.79 ? 655  PRO A O   1 
ATOM   5048  C  CB  . PRO A  1 655 ? 27.322  45.708 39.341 1.00 15.13 ? 655  PRO A CB  1 
ATOM   5049  C  CG  . PRO A  1 655 ? 25.902  46.255 39.383 1.00 13.29 ? 655  PRO A CG  1 
ATOM   5050  C  CD  . PRO A  1 655 ? 26.128  47.627 40.053 1.00 15.17 ? 655  PRO A CD  1 
ATOM   5051  N  N   . VAL A  1 656 ? 28.891  46.210 36.691 1.00 16.24 ? 656  VAL A N   1 
ATOM   5052  C  CA  . VAL A  1 656 ? 28.860  46.044 35.259 1.00 16.62 ? 656  VAL A CA  1 
ATOM   5053  C  C   . VAL A  1 656 ? 27.863  44.888 35.132 1.00 17.70 ? 656  VAL A C   1 
ATOM   5054  O  O   . VAL A  1 656 ? 27.875  43.988 35.971 1.00 19.32 ? 656  VAL A O   1 
ATOM   5055  C  CB  . VAL A  1 656 ? 30.230  45.614 34.726 1.00 15.96 ? 656  VAL A CB  1 
ATOM   5056  C  CG1 . VAL A  1 656 ? 30.089  44.868 33.408 1.00 14.38 ? 656  VAL A CG1 1 
ATOM   5057  C  CG2 . VAL A  1 656 ? 31.073  46.835 34.522 1.00 13.62 ? 656  VAL A CG2 1 
ATOM   5058  N  N   . SER A  1 657 ? 26.983  44.907 34.138 1.00 18.17 ? 657  SER A N   1 
ATOM   5059  C  CA  . SER A  1 657 ? 26.022  43.807 33.995 1.00 19.34 ? 657  SER A CA  1 
ATOM   5060  C  C   . SER A  1 657 ? 26.222  42.982 32.704 1.00 19.86 ? 657  SER A C   1 
ATOM   5061  O  O   . SER A  1 657 ? 25.918  41.792 32.690 1.00 20.38 ? 657  SER A O   1 
ATOM   5062  C  CB  . SER A  1 657 ? 24.579  44.323 34.091 1.00 19.39 ? 657  SER A CB  1 
ATOM   5063  O  OG  . SER A  1 657 ? 24.238  45.165 33.018 1.00 17.77 ? 657  SER A OG  1 
ATOM   5064  N  N   . ARG A  1 658 ? 26.680  43.617 31.620 1.00 20.07 ? 658  ARG A N   1 
ATOM   5065  C  CA  . ARG A  1 658 ? 26.989  42.916 30.374 1.00 19.84 ? 658  ARG A CA  1 
ATOM   5066  C  C   . ARG A  1 658 ? 28.137  43.706 29.755 1.00 18.78 ? 658  ARG A C   1 
ATOM   5067  O  O   . ARG A  1 658 ? 28.098  44.944 29.700 1.00 18.85 ? 658  ARG A O   1 
ATOM   5068  C  CB  . ARG A  1 658 ? 25.783  42.764 29.408 1.00 22.49 ? 658  ARG A CB  1 
ATOM   5069  C  CG  . ARG A  1 658 ? 25.385  43.966 28.585 1.00 28.15 ? 658  ARG A CG  1 
ATOM   5070  C  CD  . ARG A  1 658 ? 25.007  43.646 27.103 1.00 29.30 ? 658  ARG A CD  1 
ATOM   5071  N  NE  . ARG A  1 658 ? 24.129  42.503 26.917 1.00 30.03 ? 658  ARG A NE  1 
ATOM   5072  C  CZ  . ARG A  1 658 ? 23.724  42.021 25.732 1.00 31.21 ? 658  ARG A CZ  1 
ATOM   5073  N  NH1 . ARG A  1 658 ? 24.099  42.579 24.580 1.00 28.53 ? 658  ARG A NH1 1 
ATOM   5074  N  NH2 . ARG A  1 658 ? 22.946  40.941 25.702 1.00 29.31 ? 658  ARG A NH2 1 
ATOM   5075  N  N   . TRP A  1 659 ? 29.168  42.998 29.308 1.00 16.11 ? 659  TRP A N   1 
ATOM   5076  C  CA  . TRP A  1 659 ? 30.359  43.663 28.795 1.00 16.71 ? 659  TRP A CA  1 
ATOM   5077  C  C   . TRP A  1 659 ? 30.200  44.587 27.610 1.00 17.72 ? 659  TRP A C   1 
ATOM   5078  O  O   . TRP A  1 659 ? 31.010  45.493 27.426 1.00 17.83 ? 659  TRP A O   1 
ATOM   5079  C  CB  . TRP A  1 659 ? 31.480  42.635 28.583 1.00 14.76 ? 659  TRP A CB  1 
ATOM   5080  C  CG  . TRP A  1 659 ? 31.969  42.144 29.932 1.00 15.53 ? 659  TRP A CG  1 
ATOM   5081  C  CD1 . TRP A  1 659 ? 31.747  40.912 30.500 1.00 15.34 ? 659  TRP A CD1 1 
ATOM   5082  C  CD2 . TRP A  1 659 ? 32.627  42.933 30.940 1.00 13.24 ? 659  TRP A CD2 1 
ATOM   5083  N  NE1 . TRP A  1 659 ? 32.217  40.894 31.797 1.00 14.58 ? 659  TRP A NE1 1 
ATOM   5084  C  CE2 . TRP A  1 659 ? 32.759  42.120 32.093 1.00 14.65 ? 659  TRP A CE2 1 
ATOM   5085  C  CE3 . TRP A  1 659 ? 33.110  44.250 30.983 1.00 13.35 ? 659  TRP A CE3 1 
ATOM   5086  C  CZ2 . TRP A  1 659 ? 33.357  42.586 33.284 1.00 13.61 ? 659  TRP A CZ2 1 
ATOM   5087  C  CZ3 . TRP A  1 659 ? 33.705  44.714 32.168 1.00 13.05 ? 659  TRP A CZ3 1 
ATOM   5088  C  CH2 . TRP A  1 659 ? 33.821  43.878 33.300 1.00 13.17 ? 659  TRP A CH2 1 
ATOM   5089  N  N   . GLU A  1 660 ? 29.150  44.389 26.825 1.00 17.92 ? 660  GLU A N   1 
ATOM   5090  C  CA  . GLU A  1 660 ? 28.918  45.265 25.691 1.00 19.51 ? 660  GLU A CA  1 
ATOM   5091  C  C   . GLU A  1 660 ? 28.532  46.673 26.149 1.00 19.00 ? 660  GLU A C   1 
ATOM   5092  O  O   . GLU A  1 660 ? 28.480  47.601 25.344 1.00 19.34 ? 660  GLU A O   1 
ATOM   5093  C  CB  . GLU A  1 660 ? 27.839  44.662 24.770 1.00 20.75 ? 660  GLU A CB  1 
ATOM   5094  C  CG  . GLU A  1 660 ? 28.416  43.599 23.840 1.00 24.54 ? 660  GLU A CG  1 
ATOM   5095  C  CD  . GLU A  1 660 ? 27.378  42.689 23.239 1.00 26.97 ? 660  GLU A CD  1 
ATOM   5096  O  OE1 . GLU A  1 660 ? 26.941  41.741 23.927 1.00 26.84 ? 660  GLU A OE1 1 
ATOM   5097  O  OE2 . GLU A  1 660 ? 26.980  42.927 22.072 1.00 29.79 ? 660  GLU A OE2 1 
ATOM   5098  N  N   . TYR A  1 661 ? 28.262  46.838 27.442 1.00 18.88 ? 661  TYR A N   1 
ATOM   5099  C  CA  . TYR A  1 661 ? 27.895  48.162 27.944 1.00 18.57 ? 661  TYR A CA  1 
ATOM   5100  C  C   . TYR A  1 661 ? 29.100  48.957 28.408 1.00 17.56 ? 661  TYR A C   1 
ATOM   5101  O  O   . TYR A  1 661 ? 29.003  50.161 28.547 1.00 19.67 ? 661  TYR A O   1 
ATOM   5102  C  CB  . TYR A  1 661 ? 26.907  48.090 29.114 1.00 17.90 ? 661  TYR A CB  1 
ATOM   5103  C  CG  . TYR A  1 661 ? 25.568  47.469 28.800 1.00 20.21 ? 661  TYR A CG  1 
ATOM   5104  C  CD1 . TYR A  1 661 ? 25.037  47.494 27.501 1.00 20.91 ? 661  TYR A CD1 1 
ATOM   5105  C  CD2 . TYR A  1 661 ? 24.807  46.876 29.813 1.00 20.34 ? 661  TYR A CD2 1 
ATOM   5106  C  CE1 . TYR A  1 661 ? 23.780  46.937 27.219 1.00 19.31 ? 661  TYR A CE1 1 
ATOM   5107  C  CE2 . TYR A  1 661 ? 23.551  46.322 29.546 1.00 21.97 ? 661  TYR A CE2 1 
ATOM   5108  C  CZ  . TYR A  1 661 ? 23.045  46.353 28.240 1.00 22.22 ? 661  TYR A CZ  1 
ATOM   5109  O  OH  . TYR A  1 661 ? 21.825  45.772 27.971 1.00 20.52 ? 661  TYR A OH  1 
ATOM   5110  N  N   . TYR A  1 662 ? 30.224  48.288 28.651 1.00 17.80 ? 662  TYR A N   1 
ATOM   5111  C  CA  . TYR A  1 662 ? 31.418  48.978 29.120 1.00 18.13 ? 662  TYR A CA  1 
ATOM   5112  C  C   . TYR A  1 662 ? 32.340  49.436 27.975 1.00 18.15 ? 662  TYR A C   1 
ATOM   5113  O  O   . TYR A  1 662 ? 32.217  48.957 26.833 1.00 18.58 ? 662  TYR A O   1 
ATOM   5114  C  CB  . TYR A  1 662 ? 32.178  48.105 30.125 1.00 15.81 ? 662  TYR A CB  1 
ATOM   5115  C  CG  . TYR A  1 662 ? 33.035  48.950 31.025 1.00 15.65 ? 662  TYR A CG  1 
ATOM   5116  C  CD1 . TYR A  1 662 ? 32.474  50.000 31.765 1.00 13.99 ? 662  TYR A CD1 1 
ATOM   5117  C  CD2 . TYR A  1 662 ? 34.425  48.775 31.068 1.00 15.56 ? 662  TYR A CD2 1 
ATOM   5118  C  CE1 . TYR A  1 662 ? 33.269  50.860 32.513 1.00 14.50 ? 662  TYR A CE1 1 
ATOM   5119  C  CE2 . TYR A  1 662 ? 35.233  49.639 31.821 1.00 14.96 ? 662  TYR A CE2 1 
ATOM   5120  C  CZ  . TYR A  1 662 ? 34.642  50.683 32.536 1.00 15.19 ? 662  TYR A CZ  1 
ATOM   5121  O  OH  . TYR A  1 662 ? 35.431  51.558 33.255 1.00 15.75 ? 662  TYR A OH  1 
ATOM   5122  N  N   . ASP A  1 663 ? 33.275  50.341 28.262 1.00 18.04 ? 663  ASP A N   1 
ATOM   5123  C  CA  . ASP A  1 663 ? 34.123  50.865 27.195 1.00 18.32 ? 663  ASP A CA  1 
ATOM   5124  C  C   . ASP A  1 663 ? 35.036  49.876 26.490 1.00 19.24 ? 663  ASP A C   1 
ATOM   5125  O  O   . ASP A  1 663 ? 35.425  48.837 27.024 1.00 18.53 ? 663  ASP A O   1 
ATOM   5126  C  CB  . ASP A  1 663 ? 34.906  52.109 27.664 1.00 17.24 ? 663  ASP A CB  1 
ATOM   5127  C  CG  . ASP A  1 663 ? 36.043  51.795 28.635 1.00 17.91 ? 663  ASP A CG  1 
ATOM   5128  O  OD1 . ASP A  1 663 ? 37.030  51.137 28.233 1.00 16.08 ? 663  ASP A OD1 1 
ATOM   5129  O  OD2 . ASP A  1 663 ? 35.967  52.250 29.800 1.00 17.63 ? 663  ASP A OD2 1 
ATOM   5130  N  N   . SER A  1 664 ? 35.363  50.219 25.256 1.00 18.55 ? 664  SER A N   1 
ATOM   5131  C  CA  . SER A  1 664 ? 36.196  49.373 24.416 1.00 19.36 ? 664  SER A CA  1 
ATOM   5132  C  C   . SER A  1 664 ? 37.635  49.131 24.879 1.00 18.35 ? 664  SER A C   1 
ATOM   5133  O  O   . SER A  1 664 ? 38.095  48.001 24.875 1.00 19.20 ? 664  SER A O   1 
ATOM   5134  C  CB  . SER A  1 664 ? 36.212  49.940 22.998 1.00 19.30 ? 664  SER A CB  1 
ATOM   5135  O  OG  . SER A  1 664 ? 36.690  51.270 23.039 1.00 20.68 ? 664  SER A OG  1 
ATOM   5136  N  N   . VAL A  1 665 ? 38.345  50.173 25.279 1.00 17.87 ? 665  VAL A N   1 
ATOM   5137  C  CA  . VAL A  1 665 ? 39.734  49.985 25.685 1.00 18.34 ? 665  VAL A CA  1 
ATOM   5138  C  C   . VAL A  1 665 ? 39.920  48.960 26.836 1.00 17.70 ? 665  VAL A C   1 
ATOM   5139  O  O   . VAL A  1 665 ? 40.787  48.092 26.773 1.00 17.98 ? 665  VAL A O   1 
ATOM   5140  C  CB  . VAL A  1 665 ? 40.376  51.353 26.036 1.00 16.21 ? 665  VAL A CB  1 
ATOM   5141  C  CG1 . VAL A  1 665 ? 41.837  51.167 26.405 1.00 17.82 ? 665  VAL A CG1 1 
ATOM   5142  C  CG2 . VAL A  1 665 ? 40.264  52.298 24.829 1.00 17.77 ? 665  VAL A CG2 1 
ATOM   5143  N  N   . TYR A  1 666 ? 39.087  49.024 27.863 1.00 17.73 ? 666  TYR A N   1 
ATOM   5144  C  CA  . TYR A  1 666 ? 39.220  48.080 28.972 1.00 17.75 ? 666  TYR A CA  1 
ATOM   5145  C  C   . TYR A  1 666 ? 38.582  46.721 28.640 1.00 17.49 ? 666  TYR A C   1 
ATOM   5146  O  O   . TYR A  1 666 ? 39.209  45.680 28.793 1.00 17.91 ? 666  TYR A O   1 
ATOM   5147  C  CB  . TYR A  1 666 ? 38.580  48.686 30.226 1.00 17.11 ? 666  TYR A CB  1 
ATOM   5148  C  CG  . TYR A  1 666 ? 38.532  47.792 31.440 1.00 16.19 ? 666  TYR A CG  1 
ATOM   5149  C  CD1 . TYR A  1 666 ? 37.555  46.784 31.561 1.00 15.13 ? 666  TYR A CD1 1 
ATOM   5150  C  CD2 . TYR A  1 666 ? 39.447  47.959 32.490 1.00 14.88 ? 666  TYR A CD2 1 
ATOM   5151  C  CE1 . TYR A  1 666 ? 37.492  45.966 32.709 1.00 15.27 ? 666  TYR A CE1 1 
ATOM   5152  C  CE2 . TYR A  1 666 ? 39.396  47.141 33.636 1.00 15.04 ? 666  TYR A CE2 1 
ATOM   5153  C  CZ  . TYR A  1 666 ? 38.422  46.154 33.744 1.00 15.20 ? 666  TYR A CZ  1 
ATOM   5154  O  OH  . TYR A  1 666 ? 38.353  45.370 34.883 1.00 14.80 ? 666  TYR A OH  1 
ATOM   5155  N  N   . THR A  1 667 ? 37.347  46.735 28.160 1.00 16.76 ? 667  THR A N   1 
ATOM   5156  C  CA  . THR A  1 667 ? 36.643  45.494 27.853 1.00 17.31 ? 667  THR A CA  1 
ATOM   5157  C  C   . THR A  1 667 ? 37.328  44.604 26.809 1.00 18.25 ? 667  THR A C   1 
ATOM   5158  O  O   . THR A  1 667 ? 37.551  43.421 27.060 1.00 18.63 ? 667  THR A O   1 
ATOM   5159  C  CB  . THR A  1 667 ? 35.178  45.789 27.413 1.00 16.48 ? 667  THR A CB  1 
ATOM   5160  O  OG1 . THR A  1 667 ? 34.588  46.702 28.344 1.00 14.75 ? 667  THR A OG1 1 
ATOM   5161  C  CG2 . THR A  1 667 ? 34.330  44.506 27.409 1.00 13.67 ? 667  THR A CG2 1 
ATOM   5162  N  N   . GLU A  1 668 ? 37.671  45.174 25.657 1.00 18.73 ? 668  GLU A N   1 
ATOM   5163  C  CA  . GLU A  1 668 ? 38.315  44.421 24.576 1.00 18.77 ? 668  GLU A CA  1 
ATOM   5164  C  C   . GLU A  1 668 ? 39.687  43.874 24.956 1.00 19.29 ? 668  GLU A C   1 
ATOM   5165  O  O   . GLU A  1 668 ? 40.129  42.834 24.433 1.00 20.54 ? 668  GLU A O   1 
ATOM   5166  C  CB  . GLU A  1 668 ? 38.420  45.301 23.335 1.00 18.41 ? 668  GLU A CB  1 
ATOM   5167  C  CG  . GLU A  1 668 ? 37.062  45.681 22.774 1.00 19.38 ? 668  GLU A CG  1 
ATOM   5168  C  CD  . GLU A  1 668 ? 37.158  46.698 21.662 1.00 20.14 ? 668  GLU A CD  1 
ATOM   5169  O  OE1 . GLU A  1 668 ? 38.266  46.896 21.124 1.00 21.21 ? 668  GLU A OE1 1 
ATOM   5170  O  OE2 . GLU A  1 668 ? 36.126  47.291 21.324 1.00 20.17 ? 668  GLU A OE2 1 
ATOM   5171  N  N   . ARG A  1 669 ? 40.359  44.554 25.877 1.00 16.78 ? 669  ARG A N   1 
ATOM   5172  C  CA  . ARG A  1 669 ? 41.664  44.100 26.332 1.00 17.57 ? 669  ARG A CA  1 
ATOM   5173  C  C   . ARG A  1 669 ? 41.539  42.687 26.879 1.00 17.65 ? 669  ARG A C   1 
ATOM   5174  O  O   . ARG A  1 669 ? 42.410  41.857 26.675 1.00 17.05 ? 669  ARG A O   1 
ATOM   5175  C  CB  . ARG A  1 669 ? 42.196  44.997 27.454 1.00 16.96 ? 669  ARG A CB  1 
ATOM   5176  C  CG  . ARG A  1 669 ? 43.481  44.469 28.119 1.00 16.29 ? 669  ARG A CG  1 
ATOM   5177  C  CD  . ARG A  1 669 ? 43.920  45.394 29.247 1.00 17.22 ? 669  ARG A CD  1 
ATOM   5178  N  NE  . ARG A  1 669 ? 43.960  46.779 28.774 1.00 18.70 ? 669  ARG A NE  1 
ATOM   5179  C  CZ  . ARG A  1 669 ? 43.440  47.813 29.424 1.00 19.61 ? 669  ARG A CZ  1 
ATOM   5180  N  NH1 . ARG A  1 669 ? 42.828  47.640 30.594 1.00 16.36 ? 669  ARG A NH1 1 
ATOM   5181  N  NH2 . ARG A  1 669 ? 43.534  49.022 28.893 1.00 19.57 ? 669  ARG A NH2 1 
ATOM   5182  N  N   . TYR A  1 670 ? 40.437  42.435 27.575 1.00 17.93 ? 670  TYR A N   1 
ATOM   5183  C  CA  . TYR A  1 670 ? 40.220  41.146 28.204 1.00 18.72 ? 670  TYR A CA  1 
ATOM   5184  C  C   . TYR A  1 670 ? 39.253  40.252 27.453 1.00 19.66 ? 670  TYR A C   1 
ATOM   5185  O  O   . TYR A  1 670 ? 39.315  39.036 27.591 1.00 18.54 ? 670  TYR A O   1 
ATOM   5186  C  CB  . TYR A  1 670 ? 39.688  41.365 29.623 1.00 16.70 ? 670  TYR A CB  1 
ATOM   5187  C  CG  . TYR A  1 670 ? 40.486  42.384 30.409 1.00 17.75 ? 670  TYR A CG  1 
ATOM   5188  C  CD1 . TYR A  1 670 ? 41.802  42.122 30.804 1.00 17.38 ? 670  TYR A CD1 1 
ATOM   5189  C  CD2 . TYR A  1 670 ? 39.934  43.628 30.738 1.00 15.81 ? 670  TYR A CD2 1 
ATOM   5190  C  CE1 . TYR A  1 670 ? 42.551  43.083 31.509 1.00 18.03 ? 670  TYR A CE1 1 
ATOM   5191  C  CE2 . TYR A  1 670 ? 40.669  44.584 31.434 1.00 17.68 ? 670  TYR A CE2 1 
ATOM   5192  C  CZ  . TYR A  1 670 ? 41.979  44.304 31.818 1.00 16.24 ? 670  TYR A CZ  1 
ATOM   5193  O  OH  . TYR A  1 670 ? 42.692  45.254 32.508 1.00 16.95 ? 670  TYR A OH  1 
ATOM   5194  N  N   . MET A  1 671 ? 38.379  40.849 26.649 1.00 20.16 ? 671  MET A N   1 
ATOM   5195  C  CA  . MET A  1 671 ? 37.352  40.086 25.946 1.00 21.90 ? 671  MET A CA  1 
ATOM   5196  C  C   . MET A  1 671 ? 37.435  40.036 24.425 1.00 23.01 ? 671  MET A C   1 
ATOM   5197  O  O   . MET A  1 671 ? 36.591  39.416 23.778 1.00 23.93 ? 671  MET A O   1 
ATOM   5198  C  CB  . MET A  1 671 ? 35.968  40.648 26.329 1.00 21.69 ? 671  MET A CB  1 
ATOM   5199  C  CG  . MET A  1 671 ? 35.559  40.422 27.778 1.00 23.95 ? 671  MET A CG  1 
ATOM   5200  S  SD  . MET A  1 671 ? 35.000  38.720 28.089 1.00 25.20 ? 671  MET A SD  1 
ATOM   5201  C  CE  . MET A  1 671 ? 33.253  38.849 27.577 1.00 23.04 ? 671  MET A CE  1 
ATOM   5202  N  N   . GLY A  1 672 ? 38.424  40.679 23.825 1.00 23.95 ? 672  GLY A N   1 
ATOM   5203  C  CA  . GLY A  1 672 ? 38.434  40.669 22.374 1.00 25.02 ? 672  GLY A CA  1 
ATOM   5204  C  C   . GLY A  1 672 ? 37.175  41.401 21.899 1.00 25.79 ? 672  GLY A C   1 
ATOM   5205  O  O   . GLY A  1 672 ? 36.523  42.102 22.689 1.00 25.24 ? 672  GLY A O   1 
ATOM   5206  N  N   . LEU A  1 673 ? 36.816  41.238 20.626 1.00 25.21 ? 673  LEU A N   1 
ATOM   5207  C  CA  . LEU A  1 673 ? 35.653  41.924 20.080 1.00 24.10 ? 673  LEU A CA  1 
ATOM   5208  C  C   . LEU A  1 673 ? 34.384  41.100 20.123 1.00 23.87 ? 673  LEU A C   1 
ATOM   5209  O  O   . LEU A  1 673 ? 34.421  39.879 20.009 1.00 24.81 ? 673  LEU A O   1 
ATOM   5210  C  CB  . LEU A  1 673 ? 35.919  42.363 18.640 1.00 24.31 ? 673  LEU A CB  1 
ATOM   5211  C  CG  . LEU A  1 673 ? 37.075  43.338 18.412 1.00 25.93 ? 673  LEU A CG  1 
ATOM   5212  C  CD1 . LEU A  1 673 ? 37.317  43.477 16.930 1.00 26.75 ? 673  LEU A CD1 1 
ATOM   5213  C  CD2 . LEU A  1 673 ? 36.757  44.702 19.019 1.00 26.82 ? 673  LEU A CD2 1 
ATOM   5214  N  N   . PRO A  1 674 ? 33.231  41.771 20.287 1.00 22.55 ? 674  PRO A N   1 
ATOM   5215  C  CA  . PRO A  1 674 ? 31.930  41.110 20.349 1.00 23.26 ? 674  PRO A CA  1 
ATOM   5216  C  C   . PRO A  1 674 ? 31.301  40.926 18.965 1.00 24.57 ? 674  PRO A C   1 
ATOM   5217  O  O   . PRO A  1 674 ? 30.262  41.505 18.657 1.00 23.53 ? 674  PRO A O   1 
ATOM   5218  C  CB  . PRO A  1 674 ? 31.131  42.049 21.241 1.00 22.41 ? 674  PRO A CB  1 
ATOM   5219  C  CG  . PRO A  1 674 ? 31.603  43.381 20.777 1.00 21.47 ? 674  PRO A CG  1 
ATOM   5220  C  CD  . PRO A  1 674 ? 33.102  43.196 20.642 1.00 20.97 ? 674  PRO A CD  1 
ATOM   5221  N  N   . THR A  1 675 ? 31.958  40.124 18.137 1.00 25.76 ? 675  THR A N   1 
ATOM   5222  C  CA  . THR A  1 675 ? 31.472  39.818 16.798 1.00 26.66 ? 675  THR A CA  1 
ATOM   5223  C  C   . THR A  1 675 ? 31.464  38.305 16.737 1.00 28.72 ? 675  THR A C   1 
ATOM   5224  O  O   . THR A  1 675 ? 32.222  37.651 17.451 1.00 28.76 ? 675  THR A O   1 
ATOM   5225  C  CB  . THR A  1 675 ? 32.421  40.303 15.723 1.00 26.21 ? 675  THR A CB  1 
ATOM   5226  O  OG1 . THR A  1 675 ? 33.672  39.621 15.869 1.00 27.26 ? 675  THR A OG1 1 
ATOM   5227  C  CG2 . THR A  1 675 ? 32.652  41.818 15.842 1.00 25.04 ? 675  THR A CG2 1 
ATOM   5228  N  N   . PRO A  1 676 ? 30.600  37.720 15.898 1.00 29.80 ? 676  PRO A N   1 
ATOM   5229  C  CA  . PRO A  1 676 ? 30.576  36.258 15.817 1.00 30.39 ? 676  PRO A CA  1 
ATOM   5230  C  C   . PRO A  1 676 ? 31.948  35.683 15.439 1.00 32.41 ? 676  PRO A C   1 
ATOM   5231  O  O   . PRO A  1 676 ? 32.314  34.585 15.880 1.00 33.18 ? 676  PRO A O   1 
ATOM   5232  C  CB  . PRO A  1 676 ? 29.479  35.983 14.782 1.00 30.45 ? 676  PRO A CB  1 
ATOM   5233  C  CG  . PRO A  1 676 ? 29.387  37.280 13.991 1.00 31.02 ? 676  PRO A CG  1 
ATOM   5234  C  CD  . PRO A  1 676 ? 29.571  38.329 15.041 1.00 29.51 ? 676  PRO A CD  1 
ATOM   5235  N  N   . GLU A  1 677 ? 32.727  36.437 14.661 1.00 33.46 ? 677  GLU A N   1 
ATOM   5236  C  CA  . GLU A  1 677 ? 34.059  35.981 14.254 1.00 34.48 ? 677  GLU A CA  1 
ATOM   5237  C  C   . GLU A  1 677 ? 35.073  36.040 15.394 1.00 33.70 ? 677  GLU A C   1 
ATOM   5238  O  O   . GLU A  1 677 ? 36.157  35.462 15.301 1.00 32.25 ? 677  GLU A O   1 
ATOM   5239  C  CB  . GLU A  1 677 ? 34.600  36.828 13.104 1.00 37.16 ? 677  GLU A CB  1 
ATOM   5240  C  CG  . GLU A  1 677 ? 33.671  36.945 11.897 1.00 42.48 ? 677  GLU A CG  1 
ATOM   5241  C  CD  . GLU A  1 677 ? 32.492  37.861 12.168 1.00 44.50 ? 677  GLU A CD  1 
ATOM   5242  O  OE1 . GLU A  1 677 ? 32.713  38.913 12.819 1.00 45.30 ? 677  GLU A OE1 1 
ATOM   5243  O  OE2 . GLU A  1 677 ? 31.359  37.547 11.721 1.00 46.55 ? 677  GLU A OE2 1 
ATOM   5244  N  N   . ASP A  1 678 ? 34.744  36.754 16.465 1.00 31.98 ? 678  ASP A N   1 
ATOM   5245  C  CA  . ASP A  1 678 ? 35.696  36.838 17.559 1.00 30.14 ? 678  ASP A CA  1 
ATOM   5246  C  C   . ASP A  1 678 ? 35.234  36.227 18.866 1.00 29.42 ? 678  ASP A C   1 
ATOM   5247  O  O   . ASP A  1 678 ? 35.470  35.053 19.097 1.00 29.04 ? 678  ASP A O   1 
ATOM   5248  C  CB  . ASP A  1 678 ? 36.128  38.278 17.818 1.00 30.41 ? 678  ASP A CB  1 
ATOM   5249  C  CG  . ASP A  1 678 ? 37.340  38.361 18.744 1.00 31.10 ? 678  ASP A CG  1 
ATOM   5250  O  OD1 . ASP A  1 678 ? 37.630  37.370 19.455 1.00 29.36 ? 678  ASP A OD1 1 
ATOM   5251  O  OD2 . ASP A  1 678 ? 38.002  39.422 18.770 1.00 31.45 ? 678  ASP A OD2 1 
ATOM   5252  N  N   . ASN A  1 679 ? 34.558  36.996 19.718 1.00 28.27 ? 679  ASN A N   1 
ATOM   5253  C  CA  . ASN A  1 679 ? 34.175  36.453 21.027 1.00 27.57 ? 679  ASN A CA  1 
ATOM   5254  C  C   . ASN A  1 679 ? 32.761  36.785 21.494 1.00 27.35 ? 679  ASN A C   1 
ATOM   5255  O  O   . ASN A  1 679 ? 32.486  36.828 22.698 1.00 26.88 ? 679  ASN A O   1 
ATOM   5256  C  CB  . ASN A  1 679 ? 35.217  36.944 22.053 1.00 27.22 ? 679  ASN A CB  1 
ATOM   5257  C  CG  . ASN A  1 679 ? 35.243  36.117 23.321 1.00 27.81 ? 679  ASN A CG  1 
ATOM   5258  O  OD1 . ASN A  1 679 ? 35.056  34.891 23.297 1.00 26.95 ? 679  ASN A OD1 1 
ATOM   5259  N  ND2 . ASN A  1 679 ? 35.504  36.782 24.440 1.00 25.27 ? 679  ASN A ND2 1 
ATOM   5260  N  N   . LEU A  1 680 ? 31.853  36.994 20.548 1.00 27.56 ? 680  LEU A N   1 
ATOM   5261  C  CA  . LEU A  1 680 ? 30.477  37.340 20.896 1.00 27.32 ? 680  LEU A CA  1 
ATOM   5262  C  C   . LEU A  1 680 ? 29.805  36.315 21.801 1.00 27.98 ? 680  LEU A C   1 
ATOM   5263  O  O   . LEU A  1 680 ? 29.168  36.698 22.781 1.00 28.70 ? 680  LEU A O   1 
ATOM   5264  C  CB  . LEU A  1 680 ? 29.644  37.558 19.628 1.00 26.86 ? 680  LEU A CB  1 
ATOM   5265  C  CG  . LEU A  1 680 ? 28.168  37.975 19.760 1.00 27.55 ? 680  LEU A CG  1 
ATOM   5266  C  CD1 . LEU A  1 680 ? 28.027  39.196 20.670 1.00 25.83 ? 680  LEU A CD1 1 
ATOM   5267  C  CD2 . LEU A  1 680 ? 27.599  38.287 18.371 1.00 25.92 ? 680  LEU A CD2 1 
ATOM   5268  N  N   . ASP A  1 681 ? 29.943  35.022 21.502 1.00 27.09 ? 681  ASP A N   1 
ATOM   5269  C  CA  . ASP A  1 681 ? 29.309  34.022 22.350 1.00 27.17 ? 681  ASP A CA  1 
ATOM   5270  C  C   . ASP A  1 681 ? 29.607  34.246 23.835 1.00 26.77 ? 681  ASP A C   1 
ATOM   5271  O  O   . ASP A  1 681 ? 28.698  34.201 24.657 1.00 27.60 ? 681  ASP A O   1 
ATOM   5272  C  CB  . ASP A  1 681 ? 29.734  32.597 21.973 1.00 27.84 ? 681  ASP A CB  1 
ATOM   5273  C  CG  . ASP A  1 681 ? 29.139  32.139 20.649 1.00 29.78 ? 681  ASP A CG  1 
ATOM   5274  O  OD1 . ASP A  1 681 ? 28.220  32.801 20.139 1.00 30.27 ? 681  ASP A OD1 1 
ATOM   5275  O  OD2 . ASP A  1 681 ? 29.584  31.102 20.117 1.00 32.18 ? 681  ASP A OD2 1 
ATOM   5276  N  N   . HIS A  1 682 ? 30.865  34.485 24.196 1.00 24.74 ? 682  HIS A N   1 
ATOM   5277  C  CA  . HIS A  1 682 ? 31.144  34.676 25.607 1.00 24.30 ? 682  HIS A CA  1 
ATOM   5278  C  C   . HIS A  1 682 ? 30.654  36.023 26.142 1.00 23.51 ? 682  HIS A C   1 
ATOM   5279  O  O   . HIS A  1 682 ? 30.369  36.159 27.333 1.00 22.28 ? 682  HIS A O   1 
ATOM   5280  C  CB  . HIS A  1 682 ? 32.623  34.506 25.932 1.00 25.68 ? 682  HIS A CB  1 
ATOM   5281  C  CG  . HIS A  1 682 ? 32.883  34.574 27.398 1.00 27.73 ? 682  HIS A CG  1 
ATOM   5282  N  ND1 . HIS A  1 682 ? 32.391  33.630 28.275 1.00 28.51 ? 682  HIS A ND1 1 
ATOM   5283  C  CD2 . HIS A  1 682 ? 33.427  35.552 28.160 1.00 27.78 ? 682  HIS A CD2 1 
ATOM   5284  C  CE1 . HIS A  1 682 ? 32.615  34.027 29.517 1.00 28.53 ? 682  HIS A CE1 1 
ATOM   5285  N  NE2 . HIS A  1 682 ? 33.241  35.189 29.474 1.00 28.29 ? 682  HIS A NE2 1 
ATOM   5286  N  N   . TYR A  1 683 ? 30.578  37.021 25.268 1.00 22.73 ? 683  TYR A N   1 
ATOM   5287  C  CA  . TYR A  1 683 ? 30.056  38.318 25.659 1.00 22.95 ? 683  TYR A CA  1 
ATOM   5288  C  C   . TYR A  1 683 ? 28.604  38.085 26.059 1.00 24.28 ? 683  TYR A C   1 
ATOM   5289  O  O   . TYR A  1 683 ? 28.108  38.676 27.020 1.00 24.92 ? 683  TYR A O   1 
ATOM   5290  C  CB  . TYR A  1 683 ? 30.071  39.296 24.486 1.00 21.21 ? 683  TYR A CB  1 
ATOM   5291  C  CG  . TYR A  1 683 ? 31.247  40.259 24.434 1.00 21.98 ? 683  TYR A CG  1 
ATOM   5292  C  CD1 . TYR A  1 683 ? 31.151  41.539 24.988 1.00 20.70 ? 683  TYR A CD1 1 
ATOM   5293  C  CD2 . TYR A  1 683 ? 32.429  39.919 23.765 1.00 20.12 ? 683  TYR A CD2 1 
ATOM   5294  C  CE1 . TYR A  1 683 ? 32.198  42.456 24.869 1.00 19.82 ? 683  TYR A CE1 1 
ATOM   5295  C  CE2 . TYR A  1 683 ? 33.480  40.829 23.639 1.00 19.40 ? 683  TYR A CE2 1 
ATOM   5296  C  CZ  . TYR A  1 683 ? 33.356  42.100 24.197 1.00 20.98 ? 683  TYR A CZ  1 
ATOM   5297  O  OH  . TYR A  1 683 ? 34.399  43.004 24.117 1.00 18.50 ? 683  TYR A OH  1 
ATOM   5298  N  N   . ARG A  1 684 ? 27.919  37.210 25.321 1.00 24.98 ? 684  ARG A N   1 
ATOM   5299  C  CA  . ARG A  1 684 ? 26.509  36.944 25.601 1.00 25.83 ? 684  ARG A CA  1 
ATOM   5300  C  C   . ARG A  1 684 ? 26.276  35.979 26.745 1.00 24.78 ? 684  ARG A C   1 
ATOM   5301  O  O   . ARG A  1 684 ? 25.217  36.005 27.352 1.00 25.99 ? 684  ARG A O   1 
ATOM   5302  C  CB  . ARG A  1 684 ? 25.784  36.450 24.333 1.00 26.75 ? 684  ARG A CB  1 
ATOM   5303  C  CG  . ARG A  1 684 ? 25.788  37.472 23.196 1.00 30.35 ? 684  ARG A CG  1 
ATOM   5304  C  CD  . ARG A  1 684 ? 25.007  38.746 23.575 1.00 32.97 ? 684  ARG A CD  1 
ATOM   5305  N  NE  . ARG A  1 684 ? 25.303  39.874 22.677 1.00 35.78 ? 684  ARG A NE  1 
ATOM   5306  C  CZ  . ARG A  1 684 ? 24.889  39.977 21.411 1.00 37.18 ? 684  ARG A CZ  1 
ATOM   5307  N  NH1 . ARG A  1 684 ? 24.144  39.013 20.864 1.00 37.03 ? 684  ARG A NH1 1 
ATOM   5308  N  NH2 . ARG A  1 684 ? 25.221  41.046 20.692 1.00 34.95 ? 684  ARG A NH2 1 
ATOM   5309  N  N   . ASN A  1 685 ? 27.263  35.146 27.053 1.00 25.45 ? 685  ASN A N   1 
ATOM   5310  C  CA  . ASN A  1 685 ? 27.133  34.178 28.145 1.00 25.55 ? 685  ASN A CA  1 
ATOM   5311  C  C   . ASN A  1 685 ? 27.636  34.689 29.490 1.00 24.24 ? 685  ASN A C   1 
ATOM   5312  O  O   . ASN A  1 685 ? 27.471  34.021 30.518 1.00 23.10 ? 685  ASN A O   1 
ATOM   5313  C  CB  . ASN A  1 685 ? 27.893  32.890 27.817 1.00 27.46 ? 685  ASN A CB  1 
ATOM   5314  C  CG  . ASN A  1 685 ? 27.118  31.988 26.900 1.00 31.13 ? 685  ASN A CG  1 
ATOM   5315  O  OD1 . ASN A  1 685 ? 25.967  31.648 27.181 1.00 34.60 ? 685  ASN A OD1 1 
ATOM   5316  N  ND2 . ASN A  1 685 ? 27.735  31.588 25.791 1.00 35.13 ? 685  ASN A ND2 1 
ATOM   5317  N  N   . SER A  1 686 ? 28.241  35.867 29.496 1.00 21.41 ? 686  SER A N   1 
ATOM   5318  C  CA  . SER A  1 686 ? 28.780  36.381 30.738 1.00 21.07 ? 686  SER A CA  1 
ATOM   5319  C  C   . SER A  1 686 ? 27.985  37.538 31.312 1.00 20.05 ? 686  SER A C   1 
ATOM   5320  O  O   . SER A  1 686 ? 28.541  38.391 31.999 1.00 20.19 ? 686  SER A O   1 
ATOM   5321  C  CB  . SER A  1 686 ? 30.252  36.794 30.540 1.00 20.06 ? 686  SER A CB  1 
ATOM   5322  O  OG  . SER A  1 686 ? 30.390  37.824 29.565 1.00 20.44 ? 686  SER A OG  1 
ATOM   5323  N  N   . THR A  1 687 ? 26.690  37.583 31.034 1.00 18.91 ? 687  THR A N   1 
ATOM   5324  C  CA  . THR A  1 687 ? 25.894  38.681 31.556 1.00 19.17 ? 687  THR A CA  1 
ATOM   5325  C  C   . THR A  1 687 ? 25.218  38.299 32.855 1.00 19.67 ? 687  THR A C   1 
ATOM   5326  O  O   . THR A  1 687 ? 24.995  37.121 33.126 1.00 18.79 ? 687  THR A O   1 
ATOM   5327  C  CB  . THR A  1 687 ? 24.759  39.107 30.604 1.00 21.15 ? 687  THR A CB  1 
ATOM   5328  O  OG1 . THR A  1 687 ? 23.758  38.076 30.554 1.00 21.41 ? 687  THR A OG1 1 
ATOM   5329  C  CG2 . THR A  1 687 ? 25.289  39.377 29.205 1.00 21.50 ? 687  THR A CG2 1 
ATOM   5330  N  N   . VAL A  1 688 ? 24.898  39.313 33.654 1.00 18.41 ? 688  VAL A N   1 
ATOM   5331  C  CA  . VAL A  1 688 ? 24.199  39.105 34.903 1.00 18.08 ? 688  VAL A CA  1 
ATOM   5332  C  C   . VAL A  1 688 ? 22.755  38.736 34.587 1.00 18.19 ? 688  VAL A C   1 
ATOM   5333  O  O   . VAL A  1 688 ? 22.200  37.803 35.172 1.00 18.20 ? 688  VAL A O   1 
ATOM   5334  C  CB  . VAL A  1 688 ? 24.186  40.383 35.763 1.00 16.87 ? 688  VAL A CB  1 
ATOM   5335  C  CG1 . VAL A  1 688 ? 23.272  40.199 36.960 1.00 14.95 ? 688  VAL A CG1 1 
ATOM   5336  C  CG2 . VAL A  1 688 ? 25.596  40.702 36.220 1.00 17.99 ? 688  VAL A CG2 1 
ATOM   5337  N  N   . MET A  1 689 ? 22.148  39.477 33.666 1.00 18.55 ? 689  MET A N   1 
ATOM   5338  C  CA  . MET A  1 689 ? 20.754  39.243 33.288 1.00 18.74 ? 689  MET A CA  1 
ATOM   5339  C  C   . MET A  1 689 ? 20.386  37.777 33.000 1.00 18.72 ? 689  MET A C   1 
ATOM   5340  O  O   . MET A  1 689 ? 19.311  37.319 33.399 1.00 19.49 ? 689  MET A O   1 
ATOM   5341  C  CB  . MET A  1 689 ? 20.382  40.106 32.079 1.00 16.54 ? 689  MET A CB  1 
ATOM   5342  C  CG  . MET A  1 689 ? 20.231  41.601 32.375 1.00 16.94 ? 689  MET A CG  1 
ATOM   5343  S  SD  . MET A  1 689 ? 21.772  42.444 32.828 1.00 19.34 ? 689  MET A SD  1 
ATOM   5344  C  CE  . MET A  1 689 ? 22.468  42.738 31.081 1.00 15.79 ? 689  MET A CE  1 
ATOM   5345  N  N   . SER A  1 690 ? 21.266  37.037 32.338 1.00 18.76 ? 690  SER A N   1 
ATOM   5346  C  CA  . SER A  1 690 ? 20.941  35.646 32.023 1.00 21.42 ? 690  SER A CA  1 
ATOM   5347  C  C   . SER A  1 690 ? 20.778  34.771 33.272 1.00 22.18 ? 690  SER A C   1 
ATOM   5348  O  O   . SER A  1 690 ? 20.183  33.703 33.193 1.00 23.05 ? 690  SER A O   1 
ATOM   5349  C  CB  . SER A  1 690 ? 22.008  35.037 31.109 1.00 20.59 ? 690  SER A CB  1 
ATOM   5350  O  OG  . SER A  1 690 ? 23.259  34.946 31.765 1.00 22.89 ? 690  SER A OG  1 
ATOM   5351  N  N   . ARG A  1 691 ? 21.287  35.222 34.415 1.00 21.73 ? 691  ARG A N   1 
ATOM   5352  C  CA  . ARG A  1 691 ? 21.190  34.444 35.652 1.00 22.43 ? 691  ARG A CA  1 
ATOM   5353  C  C   . ARG A  1 691 ? 20.069  34.891 36.589 1.00 22.22 ? 691  ARG A C   1 
ATOM   5354  O  O   . ARG A  1 691 ? 19.973  34.390 37.720 1.00 21.87 ? 691  ARG A O   1 
ATOM   5355  C  CB  . ARG A  1 691 ? 22.523  34.512 36.413 1.00 22.69 ? 691  ARG A CB  1 
ATOM   5356  C  CG  . ARG A  1 691 ? 23.696  33.993 35.595 1.00 25.08 ? 691  ARG A CG  1 
ATOM   5357  C  CD  . ARG A  1 691 ? 25.034  34.144 36.314 1.00 25.26 ? 691  ARG A CD  1 
ATOM   5358  N  NE  . ARG A  1 691 ? 26.104  33.479 35.577 1.00 25.61 ? 691  ARG A NE  1 
ATOM   5359  C  CZ  . ARG A  1 691 ? 27.176  32.935 36.149 1.00 27.13 ? 691  ARG A CZ  1 
ATOM   5360  N  NH1 . ARG A  1 691 ? 27.322  32.979 37.473 1.00 24.04 ? 691  ARG A NH1 1 
ATOM   5361  N  NH2 . ARG A  1 691 ? 28.093  32.329 35.399 1.00 26.63 ? 691  ARG A NH2 1 
ATOM   5362  N  N   . ALA A  1 692 ? 19.231  35.817 36.124 1.00 21.05 ? 692  ALA A N   1 
ATOM   5363  C  CA  . ALA A  1 692 ? 18.141  36.368 36.937 1.00 23.65 ? 692  ALA A CA  1 
ATOM   5364  C  C   . ALA A  1 692 ? 17.387  35.362 37.832 1.00 25.30 ? 692  ALA A C   1 
ATOM   5365  O  O   . ALA A  1 692 ? 17.250  35.558 39.041 1.00 23.42 ? 692  ALA A O   1 
ATOM   5366  C  CB  . ALA A  1 692 ? 17.136  37.111 36.024 1.00 23.70 ? 692  ALA A CB  1 
ATOM   5367  N  N   . GLU A  1 693 ? 16.907  34.291 37.213 1.00 27.52 ? 693  GLU A N   1 
ATOM   5368  C  CA  . GLU A  1 693 ? 16.143  33.230 37.876 1.00 29.49 ? 693  GLU A CA  1 
ATOM   5369  C  C   . GLU A  1 693 ? 16.799  32.692 39.145 1.00 28.44 ? 693  GLU A C   1 
ATOM   5370  O  O   . GLU A  1 693 ? 16.124  32.392 40.116 1.00 28.95 ? 693  GLU A O   1 
ATOM   5371  C  CB  . GLU A  1 693 ? 15.939  32.084 36.880 1.00 33.44 ? 693  GLU A CB  1 
ATOM   5372  C  CG  . GLU A  1 693 ? 14.924  31.052 37.274 1.00 39.14 ? 693  GLU A CG  1 
ATOM   5373  C  CD  . GLU A  1 693 ? 13.510  31.604 37.276 1.00 42.93 ? 693  GLU A CD  1 
ATOM   5374  O  OE1 . GLU A  1 693 ? 13.030  32.007 38.365 1.00 45.23 ? 693  GLU A OE1 1 
ATOM   5375  O  OE2 . GLU A  1 693 ? 12.885  31.646 36.184 1.00 44.44 ? 693  GLU A OE2 1 
ATOM   5376  N  N   . ASN A  1 694 ? 18.120  32.572 39.140 1.00 28.08 ? 694  ASN A N   1 
ATOM   5377  C  CA  . ASN A  1 694 ? 18.831  32.051 40.300 1.00 26.12 ? 694  ASN A CA  1 
ATOM   5378  C  C   . ASN A  1 694 ? 18.852  32.971 41.513 1.00 25.18 ? 694  ASN A C   1 
ATOM   5379  O  O   . ASN A  1 694 ? 19.302  32.565 42.578 1.00 24.01 ? 694  ASN A O   1 
ATOM   5380  C  CB  . ASN A  1 694 ? 20.256  31.677 39.914 1.00 27.06 ? 694  ASN A CB  1 
ATOM   5381  C  CG  . ASN A  1 694 ? 20.291  30.560 38.893 1.00 28.46 ? 694  ASN A CG  1 
ATOM   5382  O  OD1 . ASN A  1 694 ? 19.472  29.652 38.945 1.00 29.45 ? 694  ASN A OD1 1 
ATOM   5383  N  ND2 . ASN A  1 694 ? 21.230  30.620 37.969 1.00 28.67 ? 694  ASN A ND2 1 
ATOM   5384  N  N   . PHE A  1 695 ? 18.355  34.195 41.367 1.00 23.54 ? 695  PHE A N   1 
ATOM   5385  C  CA  . PHE A  1 695 ? 18.336  35.129 42.493 1.00 23.60 ? 695  PHE A CA  1 
ATOM   5386  C  C   . PHE A  1 695 ? 17.159  34.846 43.451 1.00 25.09 ? 695  PHE A C   1 
ATOM   5387  O  O   . PHE A  1 695 ? 17.055  35.448 44.517 1.00 24.71 ? 695  PHE A O   1 
ATOM   5388  C  CB  . PHE A  1 695 ? 18.242  36.579 41.985 1.00 19.78 ? 695  PHE A CB  1 
ATOM   5389  C  CG  . PHE A  1 695 ? 19.566  37.183 41.585 1.00 19.81 ? 695  PHE A CG  1 
ATOM   5390  C  CD1 . PHE A  1 695 ? 20.179  38.142 42.395 1.00 19.41 ? 695  PHE A CD1 1 
ATOM   5391  C  CD2 . PHE A  1 695 ? 20.175  36.839 40.376 1.00 18.43 ? 695  PHE A CD2 1 
ATOM   5392  C  CE1 . PHE A  1 695 ? 21.376  38.753 42.008 1.00 19.18 ? 695  PHE A CE1 1 
ATOM   5393  C  CE2 . PHE A  1 695 ? 21.371  37.439 39.977 1.00 19.23 ? 695  PHE A CE2 1 
ATOM   5394  C  CZ  . PHE A  1 695 ? 21.977  38.406 40.791 1.00 18.22 ? 695  PHE A CZ  1 
ATOM   5395  N  N   . LYS A  1 696 ? 16.273  33.930 43.072 1.00 27.83 ? 696  LYS A N   1 
ATOM   5396  C  CA  . LYS A  1 696 ? 15.119  33.630 43.910 1.00 30.06 ? 696  LYS A CA  1 
ATOM   5397  C  C   . LYS A  1 696 ? 15.436  33.159 45.316 1.00 30.17 ? 696  LYS A C   1 
ATOM   5398  O  O   . LYS A  1 696 ? 14.634  33.353 46.221 1.00 29.89 ? 696  LYS A O   1 
ATOM   5399  C  CB  . LYS A  1 696 ? 14.207  32.610 43.219 1.00 32.44 ? 696  LYS A CB  1 
ATOM   5400  C  CG  . LYS A  1 696 ? 13.088  33.295 42.441 1.00 37.20 ? 696  LYS A CG  1 
ATOM   5401  C  CD  . LYS A  1 696 ? 12.311  32.361 41.529 1.00 39.15 ? 696  LYS A CD  1 
ATOM   5402  C  CE  . LYS A  1 696 ? 11.157  33.123 40.873 1.00 39.95 ? 696  LYS A CE  1 
ATOM   5403  N  NZ  . LYS A  1 696 ? 10.376  32.264 39.946 1.00 42.33 ? 696  LYS A NZ  1 
ATOM   5404  N  N   . GLN A  1 697 ? 16.597  32.552 45.507 1.00 30.75 ? 697  GLN A N   1 
ATOM   5405  C  CA  . GLN A  1 697 ? 16.953  32.064 46.829 1.00 31.90 ? 697  GLN A CA  1 
ATOM   5406  C  C   . GLN A  1 697 ? 17.885  32.964 47.631 1.00 29.82 ? 697  GLN A C   1 
ATOM   5407  O  O   . GLN A  1 697 ? 18.454  32.503 48.609 1.00 29.59 ? 697  GLN A O   1 
ATOM   5408  C  CB  . GLN A  1 697 ? 17.580  30.668 46.734 1.00 35.60 ? 697  GLN A CB  1 
ATOM   5409  C  CG  . GLN A  1 697 ? 16.643  29.590 46.163 1.00 38.90 ? 697  GLN A CG  1 
ATOM   5410  C  CD  . GLN A  1 697 ? 16.977  28.189 46.666 1.00 41.80 ? 697  GLN A CD  1 
ATOM   5411  O  OE1 . GLN A  1 697 ? 16.600  27.802 47.795 1.00 42.38 ? 697  GLN A OE1 1 
ATOM   5412  N  NE2 . GLN A  1 697 ? 17.697  27.420 45.838 1.00 40.45 ? 697  GLN A NE2 1 
ATOM   5413  N  N   . VAL A  1 698 ? 18.044  34.231 47.237 1.00 27.03 ? 698  VAL A N   1 
ATOM   5414  C  CA  . VAL A  1 698 ? 18.936  35.142 47.977 1.00 25.02 ? 698  VAL A CA  1 
ATOM   5415  C  C   . VAL A  1 698 ? 18.337  36.533 48.175 1.00 24.27 ? 698  VAL A C   1 
ATOM   5416  O  O   . VAL A  1 698 ? 17.401  36.907 47.489 1.00 23.05 ? 698  VAL A O   1 
ATOM   5417  C  CB  . VAL A  1 698 ? 20.322  35.337 47.254 1.00 24.21 ? 698  VAL A CB  1 
ATOM   5418  C  CG1 . VAL A  1 698 ? 20.938  34.020 46.917 1.00 23.20 ? 698  VAL A CG1 1 
ATOM   5419  C  CG2 . VAL A  1 698 ? 20.161  36.193 45.990 1.00 23.28 ? 698  VAL A CG2 1 
ATOM   5420  N  N   . GLU A  1 699 ? 18.879  37.299 49.114 1.00 25.29 ? 699  GLU A N   1 
ATOM   5421  C  CA  . GLU A  1 699 ? 18.400  38.668 49.318 1.00 25.15 ? 699  GLU A CA  1 
ATOM   5422  C  C   . GLU A  1 699 ? 19.432  39.539 48.607 1.00 24.07 ? 699  GLU A C   1 
ATOM   5423  O  O   . GLU A  1 699 ? 20.626  39.445 48.877 1.00 24.67 ? 699  GLU A O   1 
ATOM   5424  C  CB  . GLU A  1 699 ? 18.325  39.007 50.801 1.00 28.11 ? 699  GLU A CB  1 
ATOM   5425  C  CG  . GLU A  1 699 ? 17.238  38.227 51.534 1.00 33.50 ? 699  GLU A CG  1 
ATOM   5426  C  CD  . GLU A  1 699 ? 17.354  38.356 53.036 1.00 36.90 ? 699  GLU A CD  1 
ATOM   5427  O  OE1 . GLU A  1 699 ? 17.280  39.499 53.550 1.00 39.05 ? 699  GLU A OE1 1 
ATOM   5428  O  OE2 . GLU A  1 699 ? 17.528  37.314 53.707 1.00 39.10 ? 699  GLU A OE2 1 
ATOM   5429  N  N   . TYR A  1 700 ? 18.967  40.379 47.696 1.00 21.09 ? 700  TYR A N   1 
ATOM   5430  C  CA  . TYR A  1 700 ? 19.848  41.204 46.886 1.00 20.65 ? 700  TYR A CA  1 
ATOM   5431  C  C   . TYR A  1 700 ? 19.514  42.673 46.972 1.00 19.99 ? 700  TYR A C   1 
ATOM   5432  O  O   . TYR A  1 700 ? 18.355  43.045 46.885 1.00 21.13 ? 700  TYR A O   1 
ATOM   5433  C  CB  . TYR A  1 700 ? 19.718  40.743 45.436 1.00 19.37 ? 700  TYR A CB  1 
ATOM   5434  C  CG  . TYR A  1 700 ? 20.540  41.467 44.387 1.00 19.87 ? 700  TYR A CG  1 
ATOM   5435  C  CD1 . TYR A  1 700 ? 21.929  41.554 44.496 1.00 17.84 ? 700  TYR A CD1 1 
ATOM   5436  C  CD2 . TYR A  1 700 ? 19.945  41.898 43.186 1.00 17.42 ? 700  TYR A CD2 1 
ATOM   5437  C  CE1 . TYR A  1 700 ? 22.707  42.032 43.441 1.00 19.35 ? 700  TYR A CE1 1 
ATOM   5438  C  CE2 . TYR A  1 700 ? 20.715  42.368 42.125 1.00 17.93 ? 700  TYR A CE2 1 
ATOM   5439  C  CZ  . TYR A  1 700 ? 22.095  42.424 42.255 1.00 20.36 ? 700  TYR A CZ  1 
ATOM   5440  O  OH  . TYR A  1 700 ? 22.872  42.793 41.181 1.00 20.51 ? 700  TYR A OH  1 
ATOM   5441  N  N   . LEU A  1 701 ? 20.539  43.495 47.158 1.00 18.13 ? 701  LEU A N   1 
ATOM   5442  C  CA  . LEU A  1 701 ? 20.385  44.940 47.212 1.00 17.43 ? 701  LEU A CA  1 
ATOM   5443  C  C   . LEU A  1 701 ? 21.237  45.457 46.056 1.00 17.85 ? 701  LEU A C   1 
ATOM   5444  O  O   . LEU A  1 701 ? 22.455  45.185 45.997 1.00 18.99 ? 701  LEU A O   1 
ATOM   5445  C  CB  . LEU A  1 701 ? 20.893  45.505 48.545 1.00 15.33 ? 701  LEU A CB  1 
ATOM   5446  C  CG  . LEU A  1 701 ? 21.012  47.029 48.713 1.00 14.96 ? 701  LEU A CG  1 
ATOM   5447  C  CD1 . LEU A  1 701 ? 19.703  47.714 48.364 1.00 13.11 ? 701  LEU A CD1 1 
ATOM   5448  C  CD2 . LEU A  1 701 ? 21.441  47.367 50.148 1.00 15.25 ? 701  LEU A CD2 1 
ATOM   5449  N  N   . LEU A  1 702 ? 20.590  46.179 45.142 1.00 16.45 ? 702  LEU A N   1 
ATOM   5450  C  CA  . LEU A  1 702 ? 21.230  46.756 43.944 1.00 15.31 ? 702  LEU A CA  1 
ATOM   5451  C  C   . LEU A  1 702 ? 21.228  48.282 44.098 1.00 14.58 ? 702  LEU A C   1 
ATOM   5452  O  O   . LEU A  1 702 ? 20.184  48.892 44.320 1.00 14.44 ? 702  LEU A O   1 
ATOM   5453  C  CB  . LEU A  1 702 ? 20.454  46.324 42.680 1.00 13.16 ? 702  LEU A CB  1 
ATOM   5454  C  CG  . LEU A  1 702 ? 20.858  46.877 41.308 1.00 11.80 ? 702  LEU A CG  1 
ATOM   5455  C  CD1 . LEU A  1 702 ? 22.287  46.467 40.952 1.00 9.81  ? 702  LEU A CD1 1 
ATOM   5456  C  CD2 . LEU A  1 702 ? 19.888  46.367 40.253 1.00 10.76 ? 702  LEU A CD2 1 
ATOM   5457  N  N   . ILE A  1 703 ? 22.411  48.884 43.978 1.00 15.61 ? 703  ILE A N   1 
ATOM   5458  C  CA  . ILE A  1 703 ? 22.592  50.317 44.149 1.00 14.98 ? 703  ILE A CA  1 
ATOM   5459  C  C   . ILE A  1 703 ? 23.355  50.945 42.974 1.00 16.77 ? 703  ILE A C   1 
ATOM   5460  O  O   . ILE A  1 703 ? 24.278  50.330 42.444 1.00 16.72 ? 703  ILE A O   1 
ATOM   5461  C  CB  . ILE A  1 703 ? 23.380  50.574 45.464 1.00 14.67 ? 703  ILE A CB  1 
ATOM   5462  C  CG1 . ILE A  1 703 ? 22.653  49.915 46.644 1.00 12.92 ? 703  ILE A CG1 1 
ATOM   5463  C  CG2 . ILE A  1 703 ? 23.588  52.078 45.676 1.00 13.16 ? 703  ILE A CG2 1 
ATOM   5464  C  CD1 . ILE A  1 703 ? 23.329  50.098 48.011 1.00 9.71  ? 703  ILE A CD1 1 
ATOM   5465  N  N   . HIS A  1 704 ? 23.001  52.175 42.588 1.00 17.87 ? 704  HIS A N   1 
ATOM   5466  C  CA  . HIS A  1 704 ? 23.679  52.826 41.464 1.00 18.22 ? 704  HIS A CA  1 
ATOM   5467  C  C   . HIS A  1 704 ? 23.395  54.328 41.367 1.00 17.89 ? 704  HIS A C   1 
ATOM   5468  O  O   . HIS A  1 704 ? 22.265  54.772 41.571 1.00 20.10 ? 704  HIS A O   1 
ATOM   5469  C  CB  . HIS A  1 704 ? 23.248  52.143 40.160 1.00 18.64 ? 704  HIS A CB  1 
ATOM   5470  C  CG  . HIS A  1 704 ? 24.316  52.100 39.114 1.00 20.23 ? 704  HIS A CG  1 
ATOM   5471  N  ND1 . HIS A  1 704 ? 24.702  50.924 38.496 1.00 20.44 ? 704  HIS A ND1 1 
ATOM   5472  C  CD2 . HIS A  1 704 ? 25.061  53.081 38.549 1.00 19.54 ? 704  HIS A CD2 1 
ATOM   5473  C  CE1 . HIS A  1 704 ? 25.633  51.187 37.599 1.00 19.75 ? 704  HIS A CE1 1 
ATOM   5474  N  NE2 . HIS A  1 704 ? 25.871  52.489 37.611 1.00 19.20 ? 704  HIS A NE2 1 
ATOM   5475  N  N   . GLY A  1 705 ? 24.421  55.113 41.059 1.00 17.57 ? 705  GLY A N   1 
ATOM   5476  C  CA  . GLY A  1 705 ? 24.231  56.549 40.924 1.00 16.04 ? 705  GLY A CA  1 
ATOM   5477  C  C   . GLY A  1 705 ? 23.741  56.850 39.517 1.00 15.50 ? 705  GLY A C   1 
ATOM   5478  O  O   . GLY A  1 705 ? 24.295  56.349 38.552 1.00 16.14 ? 705  GLY A O   1 
ATOM   5479  N  N   . THR A  1 706 ? 22.703  57.661 39.392 1.00 16.35 ? 706  THR A N   1 
ATOM   5480  C  CA  . THR A  1 706 ? 22.144  58.001 38.080 1.00 17.06 ? 706  THR A CA  1 
ATOM   5481  C  C   . THR A  1 706 ? 23.068  58.779 37.142 1.00 17.74 ? 706  THR A C   1 
ATOM   5482  O  O   . THR A  1 706 ? 22.905  58.727 35.922 1.00 19.08 ? 706  THR A O   1 
ATOM   5483  C  CB  . THR A  1 706 ? 20.839  58.795 38.219 1.00 17.07 ? 706  THR A CB  1 
ATOM   5484  O  OG1 . THR A  1 706 ? 21.109  60.063 38.822 1.00 16.43 ? 706  THR A OG1 1 
ATOM   5485  C  CG2 . THR A  1 706 ? 19.849  58.026 39.073 1.00 14.97 ? 706  THR A CG2 1 
ATOM   5486  N  N   . ALA A  1 707 ? 24.038  59.496 37.689 1.00 18.13 ? 707  ALA A N   1 
ATOM   5487  C  CA  . ALA A  1 707 ? 24.969  60.247 36.853 1.00 17.31 ? 707  ALA A CA  1 
ATOM   5488  C  C   . ALA A  1 707 ? 26.332  59.540 36.729 1.00 17.28 ? 707  ALA A C   1 
ATOM   5489  O  O   . ALA A  1 707 ? 27.367  60.190 36.658 1.00 17.32 ? 707  ALA A O   1 
ATOM   5490  C  CB  . ALA A  1 707 ? 25.154  61.653 37.413 1.00 15.57 ? 707  ALA A CB  1 
ATOM   5491  N  N   . ASP A  1 708 ? 26.320  58.209 36.683 1.00 17.08 ? 708  ASP A N   1 
ATOM   5492  C  CA  . ASP A  1 708 ? 27.557  57.434 36.559 1.00 16.22 ? 708  ASP A CA  1 
ATOM   5493  C  C   . ASP A  1 708 ? 27.951  57.454 35.087 1.00 16.59 ? 708  ASP A C   1 
ATOM   5494  O  O   . ASP A  1 708 ? 27.285  56.845 34.246 1.00 15.78 ? 708  ASP A O   1 
ATOM   5495  C  CB  . ASP A  1 708 ? 27.330  55.979 37.016 1.00 16.13 ? 708  ASP A CB  1 
ATOM   5496  C  CG  . ASP A  1 708 ? 28.629  55.231 37.305 1.00 16.24 ? 708  ASP A CG  1 
ATOM   5497  O  OD1 . ASP A  1 708 ? 29.635  55.456 36.586 1.00 16.48 ? 708  ASP A OD1 1 
ATOM   5498  O  OD2 . ASP A  1 708 ? 28.642  54.392 38.246 1.00 14.83 ? 708  ASP A OD2 1 
ATOM   5499  N  N   . ASP A  1 709 ? 29.039  58.167 34.792 1.00 16.43 ? 709  ASP A N   1 
ATOM   5500  C  CA  . ASP A  1 709 ? 29.577  58.315 33.437 1.00 16.99 ? 709  ASP A CA  1 
ATOM   5501  C  C   . ASP A  1 709 ? 30.511  57.157 33.080 1.00 17.05 ? 709  ASP A C   1 
ATOM   5502  O  O   . ASP A  1 709 ? 30.886  56.965 31.914 1.00 15.95 ? 709  ASP A O   1 
ATOM   5503  C  CB  . ASP A  1 709 ? 30.375  59.617 33.361 1.00 17.09 ? 709  ASP A CB  1 
ATOM   5504  C  CG  . ASP A  1 709 ? 31.497  59.652 34.384 1.00 16.70 ? 709  ASP A CG  1 
ATOM   5505  O  OD1 . ASP A  1 709 ? 31.214  59.826 35.594 1.00 16.01 ? 709  ASP A OD1 1 
ATOM   5506  O  OD2 . ASP A  1 709 ? 32.657  59.473 33.970 1.00 14.86 ? 709  ASP A OD2 1 
ATOM   5507  N  N   . ASN A  1 710 ? 30.893  56.395 34.097 1.00 16.32 ? 710  ASN A N   1 
ATOM   5508  C  CA  . ASN A  1 710 ? 31.818  55.272 33.921 1.00 16.80 ? 710  ASN A CA  1 
ATOM   5509  C  C   . ASN A  1 710 ? 31.046  53.947 33.655 1.00 17.27 ? 710  ASN A C   1 
ATOM   5510  O  O   . ASN A  1 710 ? 31.079  53.408 32.545 1.00 17.45 ? 710  ASN A O   1 
ATOM   5511  C  CB  . ASN A  1 710 ? 32.698  55.169 35.178 1.00 15.12 ? 710  ASN A CB  1 
ATOM   5512  C  CG  . ASN A  1 710 ? 33.894  54.281 34.977 1.00 15.19 ? 710  ASN A CG  1 
ATOM   5513  O  OD1 . ASN A  1 710 ? 33.905  53.419 34.104 1.00 16.51 ? 710  ASN A OD1 1 
ATOM   5514  N  ND2 . ASN A  1 710 ? 34.902  54.477 35.785 1.00 13.74 ? 710  ASN A ND2 1 
ATOM   5515  N  N   . VAL A  1 711 ? 30.386  53.413 34.683 1.00 16.75 ? 711  VAL A N   1 
ATOM   5516  C  CA  . VAL A  1 711 ? 29.564  52.197 34.538 1.00 15.40 ? 711  VAL A CA  1 
ATOM   5517  C  C   . VAL A  1 711 ? 28.173  52.802 34.473 1.00 15.66 ? 711  VAL A C   1 
ATOM   5518  O  O   . VAL A  1 711 ? 27.587  53.152 35.498 1.00 15.74 ? 711  VAL A O   1 
ATOM   5519  C  CB  . VAL A  1 711 ? 29.675  51.270 35.765 1.00 14.35 ? 711  VAL A CB  1 
ATOM   5520  C  CG1 . VAL A  1 711 ? 28.775  50.055 35.580 1.00 11.04 ? 711  VAL A CG1 1 
ATOM   5521  C  CG2 . VAL A  1 711 ? 31.112  50.842 35.948 1.00 12.32 ? 711  VAL A CG2 1 
ATOM   5522  N  N   . HIS A  1 712 ? 27.636  52.940 33.274 1.00 15.03 ? 712  HIS A N   1 
ATOM   5523  C  CA  . HIS A  1 712 ? 26.356  53.619 33.158 1.00 17.10 ? 712  HIS A CA  1 
ATOM   5524  C  C   . HIS A  1 712 ? 25.196  53.022 33.959 1.00 16.17 ? 712  HIS A C   1 
ATOM   5525  O  O   . HIS A  1 712 ? 25.115  51.807 34.158 1.00 16.73 ? 712  HIS A O   1 
ATOM   5526  C  CB  . HIS A  1 712 ? 26.005  53.782 31.671 1.00 15.85 ? 712  HIS A CB  1 
ATOM   5527  C  CG  . HIS A  1 712 ? 27.138  54.324 30.851 1.00 17.24 ? 712  HIS A CG  1 
ATOM   5528  N  ND1 . HIS A  1 712 ? 27.945  55.361 31.287 1.00 16.88 ? 712  HIS A ND1 1 
ATOM   5529  C  CD2 . HIS A  1 712 ? 27.610  53.969 29.633 1.00 13.57 ? 712  HIS A CD2 1 
ATOM   5530  C  CE1 . HIS A  1 712 ? 28.862  55.613 30.372 1.00 15.47 ? 712  HIS A CE1 1 
ATOM   5531  N  NE2 . HIS A  1 712 ? 28.682  54.783 29.361 1.00 16.87 ? 712  HIS A NE2 1 
ATOM   5532  N  N   . PHE A  1 713 ? 24.318  53.896 34.443 1.00 15.20 ? 713  PHE A N   1 
ATOM   5533  C  CA  . PHE A  1 713 ? 23.151  53.457 35.217 1.00 16.92 ? 713  PHE A CA  1 
ATOM   5534  C  C   . PHE A  1 713 ? 22.458  52.336 34.424 1.00 17.14 ? 713  PHE A C   1 
ATOM   5535  O  O   . PHE A  1 713 ? 21.884  51.408 34.994 1.00 17.00 ? 713  PHE A O   1 
ATOM   5536  C  CB  . PHE A  1 713 ? 22.186  54.634 35.452 1.00 14.72 ? 713  PHE A CB  1 
ATOM   5537  C  CG  . PHE A  1 713 ? 21.020  54.289 36.338 1.00 14.80 ? 713  PHE A CG  1 
ATOM   5538  C  CD1 . PHE A  1 713 ? 21.181  54.206 37.726 1.00 15.56 ? 713  PHE A CD1 1 
ATOM   5539  C  CD2 . PHE A  1 713 ? 19.773  53.997 35.789 1.00 12.96 ? 713  PHE A CD2 1 
ATOM   5540  C  CE1 . PHE A  1 713 ? 20.116  53.821 38.553 1.00 15.86 ? 713  PHE A CE1 1 
ATOM   5541  C  CE2 . PHE A  1 713 ? 18.703  53.607 36.608 1.00 16.49 ? 713  PHE A CE2 1 
ATOM   5542  C  CZ  . PHE A  1 713 ? 18.868  53.518 37.998 1.00 15.51 ? 713  PHE A CZ  1 
ATOM   5543  N  N   . GLN A  1 714 ? 22.540  52.438 33.101 1.00 17.41 ? 714  GLN A N   1 
ATOM   5544  C  CA  . GLN A  1 714 ? 21.979  51.444 32.199 1.00 17.59 ? 714  GLN A CA  1 
ATOM   5545  C  C   . GLN A  1 714 ? 22.266  50.008 32.674 1.00 17.87 ? 714  GLN A C   1 
ATOM   5546  O  O   . GLN A  1 714 ? 21.390  49.162 32.660 1.00 18.86 ? 714  GLN A O   1 
ATOM   5547  C  CB  . GLN A  1 714 ? 22.591  51.629 30.802 1.00 16.42 ? 714  GLN A CB  1 
ATOM   5548  C  CG  . GLN A  1 714 ? 22.515  50.401 29.904 1.00 15.59 ? 714  GLN A CG  1 
ATOM   5549  C  CD  . GLN A  1 714 ? 23.411  50.532 28.664 1.00 17.88 ? 714  GLN A CD  1 
ATOM   5550  O  OE1 . GLN A  1 714 ? 24.589  50.863 28.775 1.00 16.99 ? 714  GLN A OE1 1 
ATOM   5551  N  NE2 . GLN A  1 714 ? 22.859  50.253 27.491 1.00 16.81 ? 714  GLN A NE2 1 
ATOM   5552  N  N   . GLN A  1 715 ? 23.502  49.731 33.063 1.00 16.92 ? 715  GLN A N   1 
ATOM   5553  C  CA  . GLN A  1 715 ? 23.869  48.389 33.495 1.00 17.95 ? 715  GLN A CA  1 
ATOM   5554  C  C   . GLN A  1 715 ? 22.959  47.888 34.635 1.00 18.17 ? 715  GLN A C   1 
ATOM   5555  O  O   . GLN A  1 715 ? 22.520  46.746 34.619 1.00 18.47 ? 715  GLN A O   1 
ATOM   5556  C  CB  . GLN A  1 715 ? 25.347  48.358 33.911 1.00 18.40 ? 715  GLN A CB  1 
ATOM   5557  C  CG  . GLN A  1 715 ? 26.279  48.978 32.851 1.00 18.77 ? 715  GLN A CG  1 
ATOM   5558  C  CD  . GLN A  1 715 ? 27.443  48.086 32.458 1.00 19.01 ? 715  GLN A CD  1 
ATOM   5559  O  OE1 . GLN A  1 715 ? 27.329  46.866 32.471 1.00 20.05 ? 715  GLN A OE1 1 
ATOM   5560  N  NE2 . GLN A  1 715 ? 28.563  48.697 32.076 1.00 17.40 ? 715  GLN A NE2 1 
ATOM   5561  N  N   . SER A  1 716 ? 22.670  48.735 35.616 1.00 17.00 ? 716  SER A N   1 
ATOM   5562  C  CA  . SER A  1 716 ? 21.788  48.319 36.701 1.00 17.95 ? 716  SER A CA  1 
ATOM   5563  C  C   . SER A  1 716 ? 20.324  48.321 36.273 1.00 17.53 ? 716  SER A C   1 
ATOM   5564  O  O   . SER A  1 716 ? 19.530  47.506 36.756 1.00 17.18 ? 716  SER A O   1 
ATOM   5565  C  CB  . SER A  1 716 ? 21.950  49.217 37.924 1.00 18.36 ? 716  SER A CB  1 
ATOM   5566  O  OG  . SER A  1 716 ? 23.042  48.790 38.709 1.00 19.70 ? 716  SER A OG  1 
ATOM   5567  N  N   . ALA A  1 717 ? 19.952  49.243 35.384 1.00 16.86 ? 717  ALA A N   1 
ATOM   5568  C  CA  . ALA A  1 717 ? 18.568  49.293 34.901 1.00 16.37 ? 717  ALA A CA  1 
ATOM   5569  C  C   . ALA A  1 717 ? 18.235  47.987 34.165 1.00 15.72 ? 717  ALA A C   1 
ATOM   5570  O  O   . ALA A  1 717 ? 17.096  47.531 34.205 1.00 15.41 ? 717  ALA A O   1 
ATOM   5571  C  CB  . ALA A  1 717 ? 18.368  50.500 33.960 1.00 16.97 ? 717  ALA A CB  1 
ATOM   5572  N  N   . GLN A  1 718 ? 19.217  47.379 33.495 1.00 14.86 ? 718  GLN A N   1 
ATOM   5573  C  CA  . GLN A  1 718 ? 18.935  46.128 32.795 1.00 15.90 ? 718  GLN A CA  1 
ATOM   5574  C  C   . GLN A  1 718 ? 18.872  44.958 33.796 1.00 15.60 ? 718  GLN A C   1 
ATOM   5575  O  O   . GLN A  1 718 ? 18.147  43.988 33.575 1.00 15.97 ? 718  GLN A O   1 
ATOM   5576  C  CB  . GLN A  1 718 ? 19.980  45.844 31.704 1.00 15.41 ? 718  GLN A CB  1 
ATOM   5577  C  CG  . GLN A  1 718 ? 19.947  46.791 30.497 1.00 15.13 ? 718  GLN A CG  1 
ATOM   5578  C  CD  . GLN A  1 718 ? 18.749  46.585 29.583 1.00 18.09 ? 718  GLN A CD  1 
ATOM   5579  O  OE1 . GLN A  1 718 ? 17.874  45.744 29.829 1.00 19.62 ? 718  GLN A OE1 1 
ATOM   5580  N  NE2 . GLN A  1 718 ? 18.702  47.362 28.517 1.00 19.43 ? 718  GLN A NE2 1 
ATOM   5581  N  N   . ILE A  1 719 ? 19.624  45.048 34.895 1.00 16.05 ? 719  ILE A N   1 
ATOM   5582  C  CA  . ILE A  1 719 ? 19.603  43.983 35.910 1.00 16.27 ? 719  ILE A CA  1 
ATOM   5583  C  C   . ILE A  1 719 ? 18.242  43.982 36.598 1.00 15.92 ? 719  ILE A C   1 
ATOM   5584  O  O   . ILE A  1 719 ? 17.629  42.945 36.746 1.00 17.34 ? 719  ILE A O   1 
ATOM   5585  C  CB  . ILE A  1 719 ? 20.667  44.181 37.035 1.00 16.08 ? 719  ILE A CB  1 
ATOM   5586  C  CG1 . ILE A  1 719 ? 22.091  44.065 36.464 1.00 16.65 ? 719  ILE A CG1 1 
ATOM   5587  C  CG2 . ILE A  1 719 ? 20.455  43.142 38.127 1.00 13.69 ? 719  ILE A CG2 1 
ATOM   5588  C  CD1 . ILE A  1 719 ? 23.220  44.152 37.541 1.00 13.03 ? 719  ILE A CD1 1 
ATOM   5589  N  N   . SER A  1 720 ? 17.778  45.149 37.027 1.00 16.48 ? 720  SER A N   1 
ATOM   5590  C  CA  . SER A  1 720 ? 16.506  45.226 37.719 1.00 16.50 ? 720  SER A CA  1 
ATOM   5591  C  C   . SER A  1 720 ? 15.372  44.734 36.825 1.00 17.45 ? 720  SER A C   1 
ATOM   5592  O  O   . SER A  1 720 ? 14.496  43.990 37.289 1.00 16.38 ? 720  SER A O   1 
ATOM   5593  C  CB  . SER A  1 720 ? 16.230  46.655 38.205 1.00 15.94 ? 720  SER A CB  1 
ATOM   5594  O  OG  . SER A  1 720 ? 16.106  47.562 37.126 1.00 16.63 ? 720  SER A OG  1 
ATOM   5595  N  N   . LYS A  1 721 ? 15.389  45.129 35.549 1.00 17.82 ? 721  LYS A N   1 
ATOM   5596  C  CA  . LYS A  1 721 ? 14.342  44.707 34.604 1.00 18.43 ? 721  LYS A CA  1 
ATOM   5597  C  C   . LYS A  1 721 ? 14.310  43.177 34.407 1.00 18.82 ? 721  LYS A C   1 
ATOM   5598  O  O   . LYS A  1 721 ? 13.234  42.589 34.266 1.00 19.18 ? 721  LYS A O   1 
ATOM   5599  C  CB  . LYS A  1 721 ? 14.521  45.414 33.247 1.00 17.78 ? 721  LYS A CB  1 
ATOM   5600  C  CG  . LYS A  1 721 ? 13.462  45.048 32.189 1.00 18.22 ? 721  LYS A CG  1 
ATOM   5601  C  CD  . LYS A  1 721 ? 13.328  46.139 31.127 1.00 18.52 ? 721  LYS A CD  1 
ATOM   5602  C  CE  . LYS A  1 721 ? 14.654  46.458 30.419 1.00 19.47 ? 721  LYS A CE  1 
ATOM   5603  N  NZ  . LYS A  1 721 ? 15.107  45.371 29.485 1.00 17.68 ? 721  LYS A NZ  1 
ATOM   5604  N  N   . ALA A  1 722 ? 15.476  42.538 34.389 1.00 18.06 ? 722  ALA A N   1 
ATOM   5605  C  CA  . ALA A  1 722 ? 15.523  41.086 34.231 1.00 17.84 ? 722  ALA A CA  1 
ATOM   5606  C  C   . ALA A  1 722 ? 14.995  40.378 35.494 1.00 18.83 ? 722  ALA A C   1 
ATOM   5607  O  O   . ALA A  1 722 ? 14.376  39.313 35.401 1.00 18.43 ? 722  ALA A O   1 
ATOM   5608  C  CB  . ALA A  1 722 ? 16.950  40.642 33.933 1.00 17.83 ? 722  ALA A CB  1 
ATOM   5609  N  N   . LEU A  1 723 ? 15.255  40.959 36.667 1.00 17.98 ? 723  LEU A N   1 
ATOM   5610  C  CA  . LEU A  1 723 ? 14.779  40.375 37.913 1.00 18.35 ? 723  LEU A CA  1 
ATOM   5611  C  C   . LEU A  1 723 ? 13.263  40.541 37.996 1.00 19.53 ? 723  LEU A C   1 
ATOM   5612  O  O   . LEU A  1 723 ? 12.546  39.655 38.476 1.00 21.14 ? 723  LEU A O   1 
ATOM   5613  C  CB  . LEU A  1 723 ? 15.451  41.031 39.117 1.00 17.64 ? 723  LEU A CB  1 
ATOM   5614  C  CG  . LEU A  1 723 ? 16.941  40.720 39.260 1.00 18.64 ? 723  LEU A CG  1 
ATOM   5615  C  CD1 . LEU A  1 723 ? 17.494  41.398 40.484 1.00 16.27 ? 723  LEU A CD1 1 
ATOM   5616  C  CD2 . LEU A  1 723 ? 17.144  39.236 39.378 1.00 16.15 ? 723  LEU A CD2 1 
ATOM   5617  N  N   . VAL A  1 724 ? 12.773  41.678 37.529 1.00 19.36 ? 724  VAL A N   1 
ATOM   5618  C  CA  . VAL A  1 724 ? 11.342  41.925 37.512 1.00 19.42 ? 724  VAL A CA  1 
ATOM   5619  C  C   . VAL A  1 724 ? 10.698  40.911 36.562 1.00 19.74 ? 724  VAL A C   1 
ATOM   5620  O  O   . VAL A  1 724 ? 9.685   40.296 36.893 1.00 19.38 ? 724  VAL A O   1 
ATOM   5621  C  CB  . VAL A  1 724 ? 11.027  43.355 37.001 1.00 18.43 ? 724  VAL A CB  1 
ATOM   5622  C  CG1 . VAL A  1 724 ? 9.534   43.491 36.682 1.00 16.52 ? 724  VAL A CG1 1 
ATOM   5623  C  CG2 . VAL A  1 724 ? 11.418  44.359 38.050 1.00 16.35 ? 724  VAL A CG2 1 
ATOM   5624  N  N   . ASP A  1 725 ? 11.306  40.728 35.390 1.00 20.22 ? 725  ASP A N   1 
ATOM   5625  C  CA  . ASP A  1 725 ? 10.776  39.806 34.397 1.00 21.89 ? 725  ASP A CA  1 
ATOM   5626  C  C   . ASP A  1 725 ? 10.637  38.339 34.812 1.00 22.06 ? 725  ASP A C   1 
ATOM   5627  O  O   . ASP A  1 725 ? 9.837   37.627 34.214 1.00 23.24 ? 725  ASP A O   1 
ATOM   5628  C  CB  . ASP A  1 725 ? 11.565  39.934 33.093 1.00 23.72 ? 725  ASP A CB  1 
ATOM   5629  C  CG  . ASP A  1 725 ? 11.303  41.275 32.394 1.00 26.84 ? 725  ASP A CG  1 
ATOM   5630  O  OD1 . ASP A  1 725 ? 10.403  42.005 32.848 1.00 30.43 ? 725  ASP A OD1 1 
ATOM   5631  O  OD2 . ASP A  1 725 ? 11.978  41.596 31.403 1.00 30.25 ? 725  ASP A OD2 1 
ATOM   5632  N  N   . VAL A  1 726 ? 11.401  37.875 35.809 1.00 21.97 ? 726  VAL A N   1 
ATOM   5633  C  CA  . VAL A  1 726 ? 11.256  36.489 36.286 1.00 20.28 ? 726  VAL A CA  1 
ATOM   5634  C  C   . VAL A  1 726 ? 10.600  36.480 37.671 1.00 20.40 ? 726  VAL A C   1 
ATOM   5635  O  O   . VAL A  1 726 ? 10.610  35.475 38.376 1.00 21.56 ? 726  VAL A O   1 
ATOM   5636  C  CB  . VAL A  1 726 ? 12.613  35.722 36.359 1.00 20.49 ? 726  VAL A CB  1 
ATOM   5637  C  CG1 . VAL A  1 726 ? 13.152  35.467 34.952 1.00 17.97 ? 726  VAL A CG1 1 
ATOM   5638  C  CG2 . VAL A  1 726 ? 13.626  36.504 37.232 1.00 18.84 ? 726  VAL A CG2 1 
ATOM   5639  N  N   . GLY A  1 727 ? 10.031  37.611 38.065 1.00 21.19 ? 727  GLY A N   1 
ATOM   5640  C  CA  . GLY A  1 727 ? 9.362   37.688 39.356 1.00 22.31 ? 727  GLY A CA  1 
ATOM   5641  C  C   . GLY A  1 727 ? 10.210  37.521 40.610 1.00 23.68 ? 727  GLY A C   1 
ATOM   5642  O  O   . GLY A  1 727 ? 9.760   36.915 41.590 1.00 24.80 ? 727  GLY A O   1 
ATOM   5643  N  N   . VAL A  1 728 ? 11.433  38.047 40.600 1.00 22.62 ? 728  VAL A N   1 
ATOM   5644  C  CA  . VAL A  1 728 ? 12.298  37.961 41.773 1.00 21.50 ? 728  VAL A CA  1 
ATOM   5645  C  C   . VAL A  1 728 ? 12.260  39.289 42.532 1.00 22.60 ? 728  VAL A C   1 
ATOM   5646  O  O   . VAL A  1 728 ? 12.478  40.354 41.945 1.00 22.94 ? 728  VAL A O   1 
ATOM   5647  C  CB  . VAL A  1 728 ? 13.764  37.663 41.389 1.00 21.55 ? 728  VAL A CB  1 
ATOM   5648  C  CG1 . VAL A  1 728 ? 14.654  37.823 42.602 1.00 20.00 ? 728  VAL A CG1 1 
ATOM   5649  C  CG2 . VAL A  1 728 ? 13.881  36.239 40.853 1.00 23.53 ? 728  VAL A CG2 1 
ATOM   5650  N  N   . ASP A  1 729 ? 11.967  39.239 43.829 1.00 20.81 ? 729  ASP A N   1 
ATOM   5651  C  CA  . ASP A  1 729 ? 11.926  40.456 44.617 1.00 21.01 ? 729  ASP A CA  1 
ATOM   5652  C  C   . ASP A  1 729 ? 13.352  40.786 45.051 1.00 21.63 ? 729  ASP A C   1 
ATOM   5653  O  O   . ASP A  1 729 ? 14.165  39.889 45.224 1.00 21.66 ? 729  ASP A O   1 
ATOM   5654  C  CB  . ASP A  1 729 ? 11.037  40.275 45.842 1.00 21.44 ? 729  ASP A CB  1 
ATOM   5655  C  CG  . ASP A  1 729 ? 10.891  41.555 46.649 1.00 23.56 ? 729  ASP A CG  1 
ATOM   5656  O  OD1 . ASP A  1 729 ? 10.595  42.619 46.049 1.00 24.78 ? 729  ASP A OD1 1 
ATOM   5657  O  OD2 . ASP A  1 729 ? 11.055  41.515 47.890 1.00 26.16 ? 729  ASP A OD2 1 
ATOM   5658  N  N   . PHE A  1 730 ? 13.657  42.070 45.209 1.00 20.66 ? 730  PHE A N   1 
ATOM   5659  C  CA  . PHE A  1 730 ? 14.995  42.494 45.638 1.00 20.37 ? 730  PHE A CA  1 
ATOM   5660  C  C   . PHE A  1 730 ? 14.909  43.936 46.141 1.00 20.12 ? 730  PHE A C   1 
ATOM   5661  O  O   . PHE A  1 730 ? 13.863  44.581 46.015 1.00 20.34 ? 730  PHE A O   1 
ATOM   5662  C  CB  . PHE A  1 730 ? 15.984  42.399 44.466 1.00 20.04 ? 730  PHE A CB  1 
ATOM   5663  C  CG  . PHE A  1 730 ? 15.652  43.328 43.328 1.00 20.06 ? 730  PHE A CG  1 
ATOM   5664  C  CD1 . PHE A  1 730 ? 16.300  44.548 43.200 1.00 20.61 ? 730  PHE A CD1 1 
ATOM   5665  C  CD2 . PHE A  1 730 ? 14.663  43.001 42.414 1.00 19.96 ? 730  PHE A CD2 1 
ATOM   5666  C  CE1 . PHE A  1 730 ? 15.964  45.445 42.174 1.00 21.14 ? 730  PHE A CE1 1 
ATOM   5667  C  CE2 . PHE A  1 730 ? 14.312  43.888 41.377 1.00 21.54 ? 730  PHE A CE2 1 
ATOM   5668  C  CZ  . PHE A  1 730 ? 14.970  45.109 41.264 1.00 20.82 ? 730  PHE A CZ  1 
ATOM   5669  N  N   . GLN A  1 731 ? 16.001  44.429 46.707 1.00 20.18 ? 731  GLN A N   1 
ATOM   5670  C  CA  . GLN A  1 731 ? 16.078  45.794 47.239 1.00 20.81 ? 731  GLN A CA  1 
ATOM   5671  C  C   . GLN A  1 731 ? 16.893  46.659 46.282 1.00 20.17 ? 731  GLN A C   1 
ATOM   5672  O  O   . GLN A  1 731 ? 17.833  46.175 45.653 1.00 19.32 ? 731  GLN A O   1 
ATOM   5673  C  CB  . GLN A  1 731 ? 16.767  45.776 48.592 1.00 21.38 ? 731  GLN A CB  1 
ATOM   5674  C  CG  . GLN A  1 731 ? 16.283  44.642 49.461 1.00 25.61 ? 731  GLN A CG  1 
ATOM   5675  C  CD  . GLN A  1 731 ? 14.813  44.757 49.769 1.00 28.32 ? 731  GLN A CD  1 
ATOM   5676  O  OE1 . GLN A  1 731 ? 14.046  43.799 49.598 1.00 31.91 ? 731  GLN A OE1 1 
ATOM   5677  N  NE2 . GLN A  1 731 ? 14.401  45.936 50.225 1.00 29.15 ? 731  GLN A NE2 1 
ATOM   5678  N  N   . ALA A  1 732 ? 16.531  47.933 46.174 1.00 19.44 ? 732  ALA A N   1 
ATOM   5679  C  CA  . ALA A  1 732 ? 17.237  48.837 45.285 1.00 18.82 ? 732  ALA A CA  1 
ATOM   5680  C  C   . ALA A  1 732 ? 17.372  50.224 45.861 1.00 19.35 ? 732  ALA A C   1 
ATOM   5681  O  O   . ALA A  1 732 ? 16.618  50.626 46.748 1.00 19.64 ? 732  ALA A O   1 
ATOM   5682  C  CB  . ALA A  1 732 ? 16.502  48.928 43.945 1.00 18.94 ? 732  ALA A CB  1 
ATOM   5683  N  N   . MET A  1 733 ? 18.356  50.953 45.360 1.00 18.30 ? 733  MET A N   1 
ATOM   5684  C  CA  . MET A  1 733 ? 18.550  52.337 45.755 1.00 17.12 ? 733  MET A CA  1 
ATOM   5685  C  C   . MET A  1 733 ? 19.333  53.041 44.652 1.00 17.17 ? 733  MET A C   1 
ATOM   5686  O  O   . MET A  1 733 ? 20.401  52.574 44.248 1.00 17.08 ? 733  MET A O   1 
ATOM   5687  C  CB  . MET A  1 733 ? 19.330  52.435 47.070 1.00 17.38 ? 733  MET A CB  1 
ATOM   5688  C  CG  . MET A  1 733 ? 19.596  53.875 47.519 1.00 17.08 ? 733  MET A CG  1 
ATOM   5689  S  SD  . MET A  1 733 ? 18.113  54.872 47.885 1.00 22.81 ? 733  MET A SD  1 
ATOM   5690  C  CE  . MET A  1 733 ? 17.469  53.960 49.338 1.00 17.04 ? 733  MET A CE  1 
ATOM   5691  N  N   . TRP A  1 734 ? 18.794  54.146 44.160 1.00 15.57 ? 734  TRP A N   1 
ATOM   5692  C  CA  . TRP A  1 734 ? 19.487  54.932 43.150 1.00 16.01 ? 734  TRP A CA  1 
ATOM   5693  C  C   . TRP A  1 734 ? 19.980  56.189 43.866 1.00 16.17 ? 734  TRP A C   1 
ATOM   5694  O  O   . TRP A  1 734 ? 19.366  56.613 44.843 1.00 15.31 ? 734  TRP A O   1 
ATOM   5695  C  CB  . TRP A  1 734 ? 18.549  55.328 41.994 1.00 15.20 ? 734  TRP A CB  1 
ATOM   5696  C  CG  . TRP A  1 734 ? 17.512  56.388 42.340 1.00 15.33 ? 734  TRP A CG  1 
ATOM   5697  C  CD1 . TRP A  1 734 ? 17.722  57.739 42.436 1.00 15.42 ? 734  TRP A CD1 1 
ATOM   5698  C  CD2 . TRP A  1 734 ? 16.132  56.174 42.665 1.00 13.65 ? 734  TRP A CD2 1 
ATOM   5699  N  NE1 . TRP A  1 734 ? 16.567  58.372 42.801 1.00 15.45 ? 734  TRP A NE1 1 
ATOM   5700  C  CE2 . TRP A  1 734 ? 15.573  57.440 42.952 1.00 15.56 ? 734  TRP A CE2 1 
ATOM   5701  C  CE3 . TRP A  1 734 ? 15.313  55.033 42.750 1.00 13.51 ? 734  TRP A CE3 1 
ATOM   5702  C  CZ2 . TRP A  1 734 ? 14.218  57.604 43.323 1.00 14.63 ? 734  TRP A CZ2 1 
ATOM   5703  C  CZ3 . TRP A  1 734 ? 13.970  55.191 43.119 1.00 13.17 ? 734  TRP A CZ3 1 
ATOM   5704  C  CH2 . TRP A  1 734 ? 13.440  56.469 43.401 1.00 14.03 ? 734  TRP A CH2 1 
ATOM   5705  N  N   . TYR A  1 735 ? 21.096  56.763 43.422 1.00 14.54 ? 735  TYR A N   1 
ATOM   5706  C  CA  . TYR A  1 735 ? 21.564  58.004 44.042 1.00 15.37 ? 735  TYR A CA  1 
ATOM   5707  C  C   . TYR A  1 735 ? 21.531  59.098 42.982 1.00 15.59 ? 735  TYR A C   1 
ATOM   5708  O  O   . TYR A  1 735 ? 22.301  59.090 42.024 1.00 16.01 ? 735  TYR A O   1 
ATOM   5709  C  CB  . TYR A  1 735 ? 22.969  57.835 44.643 1.00 14.40 ? 735  TYR A CB  1 
ATOM   5710  C  CG  . TYR A  1 735 ? 22.896  57.177 45.996 1.00 15.40 ? 735  TYR A CG  1 
ATOM   5711  C  CD1 . TYR A  1 735 ? 23.140  55.813 46.156 1.00 13.82 ? 735  TYR A CD1 1 
ATOM   5712  C  CD2 . TYR A  1 735 ? 22.451  57.904 47.105 1.00 16.24 ? 735  TYR A CD2 1 
ATOM   5713  C  CE1 . TYR A  1 735 ? 22.928  55.182 47.393 1.00 15.19 ? 735  TYR A CE1 1 
ATOM   5714  C  CE2 . TYR A  1 735 ? 22.237  57.289 48.336 1.00 16.92 ? 735  TYR A CE2 1 
ATOM   5715  C  CZ  . TYR A  1 735 ? 22.474  55.925 48.473 1.00 16.23 ? 735  TYR A CZ  1 
ATOM   5716  O  OH  . TYR A  1 735 ? 22.228  55.330 49.688 1.00 16.73 ? 735  TYR A OH  1 
ATOM   5717  N  N   . THR A  1 736 ? 20.603  60.024 43.154 1.00 17.05 ? 736  THR A N   1 
ATOM   5718  C  CA  . THR A  1 736 ? 20.429  61.110 42.204 1.00 16.44 ? 736  THR A CA  1 
ATOM   5719  C  C   . THR A  1 736 ? 21.680  61.949 42.029 1.00 17.59 ? 736  THR A C   1 
ATOM   5720  O  O   . THR A  1 736 ? 22.203  62.498 42.999 1.00 17.65 ? 736  THR A O   1 
ATOM   5721  C  CB  . THR A  1 736 ? 19.284  62.049 42.634 1.00 16.35 ? 736  THR A CB  1 
ATOM   5722  O  OG1 . THR A  1 736 ? 18.070  61.299 42.717 1.00 14.61 ? 736  THR A OG1 1 
ATOM   5723  C  CG2 . THR A  1 736 ? 19.117  63.217 41.627 1.00 14.60 ? 736  THR A CG2 1 
ATOM   5724  N  N   . ASP A  1 737 ? 22.141  62.028 40.783 1.00 16.84 ? 737  ASP A N   1 
ATOM   5725  C  CA  . ASP A  1 737 ? 23.304  62.817 40.380 1.00 16.73 ? 737  ASP A CA  1 
ATOM   5726  C  C   . ASP A  1 737 ? 24.673  62.394 40.881 1.00 16.74 ? 737  ASP A C   1 
ATOM   5727  O  O   . ASP A  1 737 ? 25.647  63.134 40.721 1.00 16.13 ? 737  ASP A O   1 
ATOM   5728  C  CB  . ASP A  1 737 ? 23.058  64.299 40.700 1.00 16.47 ? 737  ASP A CB  1 
ATOM   5729  C  CG  . ASP A  1 737 ? 21.967  64.924 39.805 1.00 17.14 ? 737  ASP A CG  1 
ATOM   5730  O  OD1 . ASP A  1 737 ? 21.541  64.269 38.815 1.00 16.82 ? 737  ASP A OD1 1 
ATOM   5731  O  OD2 . ASP A  1 737 ? 21.541  66.067 40.090 1.00 15.58 ? 737  ASP A OD2 1 
ATOM   5732  N  N   . GLU A  1 738 ? 24.756  61.211 41.489 1.00 16.90 ? 738  GLU A N   1 
ATOM   5733  C  CA  . GLU A  1 738 ? 26.037  60.704 41.970 1.00 17.29 ? 738  GLU A CA  1 
ATOM   5734  C  C   . GLU A  1 738 ? 26.676  59.883 40.848 1.00 17.71 ? 738  GLU A C   1 
ATOM   5735  O  O   . GLU A  1 738 ? 25.970  59.227 40.076 1.00 14.82 ? 738  GLU A O   1 
ATOM   5736  C  CB  . GLU A  1 738 ? 25.848  59.807 43.200 1.00 18.60 ? 738  GLU A CB  1 
ATOM   5737  C  CG  . GLU A  1 738 ? 25.515  60.555 44.485 1.00 20.41 ? 738  GLU A CG  1 
ATOM   5738  C  CD  . GLU A  1 738 ? 26.586  61.556 44.846 1.00 22.62 ? 738  GLU A CD  1 
ATOM   5739  O  OE1 . GLU A  1 738 ? 27.731  61.138 45.100 1.00 23.76 ? 738  GLU A OE1 1 
ATOM   5740  O  OE2 . GLU A  1 738 ? 26.287  62.763 44.883 1.00 25.62 ? 738  GLU A OE2 1 
ATOM   5741  N  N   . ASP A  1 739 ? 28.002  59.931 40.739 1.00 16.53 ? 739  ASP A N   1 
ATOM   5742  C  CA  . ASP A  1 739 ? 28.662  59.147 39.705 1.00 18.81 ? 739  ASP A CA  1 
ATOM   5743  C  C   . ASP A  1 739 ? 29.172  57.815 40.270 1.00 18.62 ? 739  ASP A C   1 
ATOM   5744  O  O   . ASP A  1 739 ? 28.673  57.328 41.286 1.00 20.28 ? 739  ASP A O   1 
ATOM   5745  C  CB  . ASP A  1 739 ? 29.804  59.934 39.037 1.00 18.51 ? 739  ASP A CB  1 
ATOM   5746  C  CG  . ASP A  1 739 ? 30.930  60.286 39.999 1.00 21.94 ? 739  ASP A CG  1 
ATOM   5747  O  OD1 . ASP A  1 739 ? 31.094  59.619 41.068 1.00 20.28 ? 739  ASP A OD1 1 
ATOM   5748  O  OD2 . ASP A  1 739 ? 31.684  61.224 39.662 1.00 21.98 ? 739  ASP A OD2 1 
ATOM   5749  N  N   . HIS A  1 740 ? 30.165  57.233 39.615 1.00 18.78 ? 740  HIS A N   1 
ATOM   5750  C  CA  . HIS A  1 740 ? 30.699  55.944 40.023 1.00 19.04 ? 740  HIS A CA  1 
ATOM   5751  C  C   . HIS A  1 740 ? 31.278  55.931 41.443 1.00 19.04 ? 740  HIS A C   1 
ATOM   5752  O  O   . HIS A  1 740 ? 31.358  54.884 42.077 1.00 19.36 ? 740  HIS A O   1 
ATOM   5753  C  CB  . HIS A  1 740 ? 31.762  55.494 39.016 1.00 18.48 ? 740  HIS A CB  1 
ATOM   5754  C  CG  . HIS A  1 740 ? 32.037  54.022 39.043 1.00 19.41 ? 740  HIS A CG  1 
ATOM   5755  N  ND1 . HIS A  1 740 ? 31.053  53.079 38.825 1.00 19.55 ? 740  HIS A ND1 1 
ATOM   5756  C  CD2 . HIS A  1 740 ? 33.182  53.327 39.246 1.00 19.50 ? 740  HIS A CD2 1 
ATOM   5757  C  CE1 . HIS A  1 740 ? 31.582  51.870 38.887 1.00 20.15 ? 740  HIS A CE1 1 
ATOM   5758  N  NE2 . HIS A  1 740 ? 32.873  51.991 39.141 1.00 20.95 ? 740  HIS A NE2 1 
ATOM   5759  N  N   . GLY A  1 741 ? 31.663  57.093 41.952 1.00 19.51 ? 741  GLY A N   1 
ATOM   5760  C  CA  . GLY A  1 741 ? 32.246  57.125 43.281 1.00 18.49 ? 741  GLY A CA  1 
ATOM   5761  C  C   . GLY A  1 741 ? 31.259  57.291 44.422 1.00 20.19 ? 741  GLY A C   1 
ATOM   5762  O  O   . GLY A  1 741 ? 31.604  56.979 45.563 1.00 19.05 ? 741  GLY A O   1 
ATOM   5763  N  N   . ILE A  1 742 ? 30.040  57.749 44.113 1.00 19.21 ? 742  ILE A N   1 
ATOM   5764  C  CA  . ILE A  1 742 ? 29.000  58.009 45.116 1.00 20.35 ? 742  ILE A CA  1 
ATOM   5765  C  C   . ILE A  1 742 ? 29.714  58.579 46.337 1.00 22.03 ? 742  ILE A C   1 
ATOM   5766  O  O   . ILE A  1 742 ? 29.459  58.195 47.476 1.00 23.25 ? 742  ILE A O   1 
ATOM   5767  C  CB  . ILE A  1 742 ? 28.224  56.713 45.499 1.00 20.30 ? 742  ILE A CB  1 
ATOM   5768  C  CG1 . ILE A  1 742 ? 27.747  55.991 44.230 1.00 18.58 ? 742  ILE A CG1 1 
ATOM   5769  C  CG2 . ILE A  1 742 ? 27.006  57.068 46.360 1.00 18.45 ? 742  ILE A CG2 1 
ATOM   5770  C  CD1 . ILE A  1 742 ? 26.863  54.765 44.454 1.00 16.42 ? 742  ILE A CD1 1 
ATOM   5771  N  N   . ALA A  1 743 ? 30.604  59.529 46.071 1.00 21.25 ? 743  ALA A N   1 
ATOM   5772  C  CA  . ALA A  1 743 ? 31.438  60.112 47.102 1.00 21.36 ? 743  ALA A CA  1 
ATOM   5773  C  C   . ALA A  1 743 ? 31.063  61.468 47.665 1.00 21.44 ? 743  ALA A C   1 
ATOM   5774  O  O   . ALA A  1 743 ? 31.782  61.962 48.524 1.00 22.36 ? 743  ALA A O   1 
ATOM   5775  C  CB  . ALA A  1 743 ? 32.908  60.142 46.612 1.00 22.00 ? 743  ALA A CB  1 
ATOM   5776  N  N   . SER A  1 744 ? 29.990  62.102 47.200 1.00 20.95 ? 744  SER A N   1 
ATOM   5777  C  CA  . SER A  1 744 ? 29.642  63.367 47.823 1.00 21.75 ? 744  SER A CA  1 
ATOM   5778  C  C   . SER A  1 744 ? 29.434  62.989 49.305 1.00 22.86 ? 744  SER A C   1 
ATOM   5779  O  O   . SER A  1 744 ? 29.026  61.867 49.618 1.00 22.00 ? 744  SER A O   1 
ATOM   5780  C  CB  . SER A  1 744 ? 28.356  63.945 47.232 1.00 22.76 ? 744  SER A CB  1 
ATOM   5781  O  OG  . SER A  1 744 ? 27.233  63.158 47.587 1.00 28.46 ? 744  SER A OG  1 
ATOM   5782  N  N   . SER A  1 745 ? 29.722  63.917 50.211 1.00 22.99 ? 745  SER A N   1 
ATOM   5783  C  CA  . SER A  1 745 ? 29.597  63.662 51.644 1.00 23.70 ? 745  SER A CA  1 
ATOM   5784  C  C   . SER A  1 745 ? 28.260  63.069 52.113 1.00 23.00 ? 745  SER A C   1 
ATOM   5785  O  O   . SER A  1 745 ? 28.231  62.101 52.890 1.00 22.80 ? 745  SER A O   1 
ATOM   5786  C  CB  . SER A  1 745 ? 29.872  64.942 52.422 1.00 24.86 ? 745  SER A CB  1 
ATOM   5787  O  OG  . SER A  1 745 ? 29.559  64.736 53.782 1.00 29.82 ? 745  SER A OG  1 
ATOM   5788  N  N   . THR A  1 746 ? 27.152  63.642 51.669 1.00 22.23 ? 746  THR A N   1 
ATOM   5789  C  CA  . THR A  1 746 ? 25.855  63.126 52.079 1.00 20.69 ? 746  THR A CA  1 
ATOM   5790  C  C   . THR A  1 746 ? 25.550  61.748 51.453 1.00 20.17 ? 746  THR A C   1 
ATOM   5791  O  O   . THR A  1 746 ? 25.118  60.839 52.150 1.00 17.36 ? 746  THR A O   1 
ATOM   5792  C  CB  . THR A  1 746 ? 24.752  64.147 51.733 1.00 22.32 ? 746  THR A CB  1 
ATOM   5793  O  OG1 . THR A  1 746 ? 24.860  64.547 50.355 1.00 22.46 ? 746  THR A OG1 1 
ATOM   5794  C  CG2 . THR A  1 746 ? 24.891  65.388 52.628 1.00 21.41 ? 746  THR A CG2 1 
ATOM   5795  N  N   . ALA A  1 747 ? 25.808  61.574 50.156 1.00 19.50 ? 747  ALA A N   1 
ATOM   5796  C  CA  . ALA A  1 747 ? 25.531  60.277 49.531 1.00 20.02 ? 747  ALA A CA  1 
ATOM   5797  C  C   . ALA A  1 747 ? 26.352  59.152 50.161 1.00 20.16 ? 747  ALA A C   1 
ATOM   5798  O  O   . ALA A  1 747 ? 25.847  58.049 50.382 1.00 20.18 ? 747  ALA A O   1 
ATOM   5799  C  CB  . ALA A  1 747 ? 25.800  60.335 48.043 1.00 18.80 ? 747  ALA A CB  1 
ATOM   5800  N  N   . HIS A  1 748 ? 27.621  59.445 50.429 1.00 19.62 ? 748  HIS A N   1 
ATOM   5801  C  CA  . HIS A  1 748 ? 28.550  58.498 51.037 1.00 18.85 ? 748  HIS A CA  1 
ATOM   5802  C  C   . HIS A  1 748 ? 27.993  57.986 52.362 1.00 19.18 ? 748  HIS A C   1 
ATOM   5803  O  O   . HIS A  1 748 ? 27.911  56.774 52.595 1.00 16.79 ? 748  HIS A O   1 
ATOM   5804  C  CB  . HIS A  1 748 ? 29.893  59.188 51.269 1.00 19.52 ? 748  HIS A CB  1 
ATOM   5805  C  CG  . HIS A  1 748 ? 30.886  58.347 52.010 1.00 20.80 ? 748  HIS A CG  1 
ATOM   5806  N  ND1 . HIS A  1 748 ? 31.398  57.173 51.501 1.00 20.99 ? 748  HIS A ND1 1 
ATOM   5807  C  CD2 . HIS A  1 748 ? 31.481  58.526 53.215 1.00 19.52 ? 748  HIS A CD2 1 
ATOM   5808  C  CE1 . HIS A  1 748 ? 32.268  56.666 52.359 1.00 21.97 ? 748  HIS A CE1 1 
ATOM   5809  N  NE2 . HIS A  1 748 ? 32.336  57.468 53.407 1.00 21.20 ? 748  HIS A NE2 1 
ATOM   5810  N  N   . GLN A  1 749 ? 27.610  58.921 53.228 1.00 18.70 ? 749  GLN A N   1 
ATOM   5811  C  CA  . GLN A  1 749 ? 27.039  58.542 54.502 1.00 19.13 ? 749  GLN A CA  1 
ATOM   5812  C  C   . GLN A  1 749 ? 25.761  57.752 54.302 1.00 18.95 ? 749  GLN A C   1 
ATOM   5813  O  O   . GLN A  1 749 ? 25.534  56.736 54.964 1.00 19.62 ? 749  GLN A O   1 
ATOM   5814  C  CB  . GLN A  1 749 ? 26.772  59.789 55.344 1.00 19.95 ? 749  GLN A CB  1 
ATOM   5815  C  CG  . GLN A  1 749 ? 28.055  60.486 55.697 1.00 24.10 ? 749  GLN A CG  1 
ATOM   5816  C  CD  . GLN A  1 749 ? 27.837  61.763 56.463 1.00 26.75 ? 749  GLN A CD  1 
ATOM   5817  O  OE1 . GLN A  1 749 ? 27.289  61.750 57.562 1.00 30.89 ? 749  GLN A OE1 1 
ATOM   5818  N  NE2 . GLN A  1 749 ? 28.278  62.878 55.895 1.00 28.03 ? 749  GLN A NE2 1 
ATOM   5819  N  N   . HIS A  1 750 ? 24.928  58.208 53.379 1.00 18.01 ? 750  HIS A N   1 
ATOM   5820  C  CA  . HIS A  1 750 ? 23.658  57.539 53.135 1.00 18.12 ? 750  HIS A CA  1 
ATOM   5821  C  C   . HIS A  1 750 ? 23.808  56.094 52.632 1.00 18.57 ? 750  HIS A C   1 
ATOM   5822  O  O   . HIS A  1 750 ? 23.124  55.192 53.128 1.00 18.29 ? 750  HIS A O   1 
ATOM   5823  C  CB  . HIS A  1 750 ? 22.828  58.349 52.145 1.00 16.51 ? 750  HIS A CB  1 
ATOM   5824  C  CG  . HIS A  1 750 ? 21.374  57.994 52.155 1.00 17.19 ? 750  HIS A CG  1 
ATOM   5825  N  ND1 . HIS A  1 750 ? 20.868  56.904 51.482 1.00 15.77 ? 750  HIS A ND1 1 
ATOM   5826  C  CD2 . HIS A  1 750 ? 20.321  58.558 52.797 1.00 16.46 ? 750  HIS A CD2 1 
ATOM   5827  C  CE1 . HIS A  1 750 ? 19.570  56.812 51.703 1.00 15.24 ? 750  HIS A CE1 1 
ATOM   5828  N  NE2 . HIS A  1 750 ? 19.213  57.805 52.498 1.00 16.83 ? 750  HIS A NE2 1 
ATOM   5829  N  N   . ILE A  1 751 ? 24.714  55.863 51.682 1.00 17.18 ? 751  ILE A N   1 
ATOM   5830  C  CA  . ILE A  1 751 ? 24.868  54.523 51.159 1.00 17.00 ? 751  ILE A CA  1 
ATOM   5831  C  C   . ILE A  1 751 ? 25.380  53.546 52.206 1.00 17.48 ? 751  ILE A C   1 
ATOM   5832  O  O   . ILE A  1 751 ? 24.814  52.458 52.390 1.00 17.60 ? 751  ILE A O   1 
ATOM   5833  C  CB  . ILE A  1 751 ? 25.763  54.492 49.864 1.00 17.02 ? 751  ILE A CB  1 
ATOM   5834  C  CG1 . ILE A  1 751 ? 25.728  53.070 49.235 1.00 16.96 ? 751  ILE A CG1 1 
ATOM   5835  C  CG2 . ILE A  1 751 ? 27.203  54.883 50.182 1.00 15.64 ? 751  ILE A CG2 1 
ATOM   5836  C  CD1 . ILE A  1 751 ? 26.350  52.980 47.811 1.00 11.81 ? 751  ILE A CD1 1 
ATOM   5837  N  N   . TYR A  1 752 ? 26.442  53.921 52.909 1.00 17.43 ? 752  TYR A N   1 
ATOM   5838  C  CA  . TYR A  1 752 ? 26.988  53.034 53.933 1.00 17.75 ? 752  TYR A CA  1 
ATOM   5839  C  C   . TYR A  1 752 ? 25.994  52.818 55.067 1.00 17.33 ? 752  TYR A C   1 
ATOM   5840  O  O   . TYR A  1 752 ? 25.938  51.739 55.653 1.00 17.01 ? 752  TYR A O   1 
ATOM   5841  C  CB  . TYR A  1 752 ? 28.334  53.567 54.436 1.00 17.52 ? 752  TYR A CB  1 
ATOM   5842  C  CG  . TYR A  1 752 ? 29.435  53.184 53.483 1.00 17.33 ? 752  TYR A CG  1 
ATOM   5843  C  CD1 . TYR A  1 752 ? 29.869  51.851 53.403 1.00 16.33 ? 752  TYR A CD1 1 
ATOM   5844  C  CD2 . TYR A  1 752 ? 29.998  54.126 52.609 1.00 15.61 ? 752  TYR A CD2 1 
ATOM   5845  C  CE1 . TYR A  1 752 ? 30.831  51.463 52.490 1.00 15.64 ? 752  TYR A CE1 1 
ATOM   5846  C  CE2 . TYR A  1 752 ? 30.965  53.748 51.680 1.00 15.26 ? 752  TYR A CE2 1 
ATOM   5847  C  CZ  . TYR A  1 752 ? 31.376  52.419 51.634 1.00 16.38 ? 752  TYR A CZ  1 
ATOM   5848  O  OH  . TYR A  1 752 ? 32.359  52.043 50.766 1.00 16.23 ? 752  TYR A OH  1 
ATOM   5849  N  N   . THR A  1 753 ? 25.186  53.829 55.368 1.00 17.61 ? 753  THR A N   1 
ATOM   5850  C  CA  . THR A  1 753 ? 24.170  53.659 56.402 1.00 16.46 ? 753  THR A CA  1 
ATOM   5851  C  C   . THR A  1 753 ? 23.119  52.650 55.911 1.00 17.25 ? 753  THR A C   1 
ATOM   5852  O  O   . THR A  1 753 ? 22.732  51.738 56.633 1.00 17.18 ? 753  THR A O   1 
ATOM   5853  C  CB  . THR A  1 753 ? 23.493  54.990 56.716 1.00 15.24 ? 753  THR A CB  1 
ATOM   5854  O  OG1 . THR A  1 753 ? 24.473  55.877 57.263 1.00 16.50 ? 753  THR A OG1 1 
ATOM   5855  C  CG2 . THR A  1 753 ? 22.357  54.815 57.717 1.00 13.72 ? 753  THR A CG2 1 
ATOM   5856  N  N   . HIS A  1 754 ? 22.694  52.804 54.660 1.00 17.87 ? 754  HIS A N   1 
ATOM   5857  C  CA  . HIS A  1 754 ? 21.689  51.926 54.084 1.00 16.70 ? 754  HIS A CA  1 
ATOM   5858  C  C   . HIS A  1 754 ? 22.207  50.491 53.963 1.00 17.49 ? 754  HIS A C   1 
ATOM   5859  O  O   . HIS A  1 754 ? 21.487  49.533 54.270 1.00 16.93 ? 754  HIS A O   1 
ATOM   5860  C  CB  . HIS A  1 754 ? 21.261  52.469 52.717 1.00 16.66 ? 754  HIS A CB  1 
ATOM   5861  C  CG  . HIS A  1 754 ? 20.012  51.854 52.189 1.00 18.21 ? 754  HIS A CG  1 
ATOM   5862  N  ND1 . HIS A  1 754 ? 18.785  52.021 52.796 1.00 18.03 ? 754  HIS A ND1 1 
ATOM   5863  C  CD2 . HIS A  1 754 ? 19.792  51.050 51.120 1.00 18.79 ? 754  HIS A CD2 1 
ATOM   5864  C  CE1 . HIS A  1 754 ? 17.867  51.352 52.122 1.00 18.36 ? 754  HIS A CE1 1 
ATOM   5865  N  NE2 . HIS A  1 754 ? 18.452  50.753 51.099 1.00 16.77 ? 754  HIS A NE2 1 
ATOM   5866  N  N   . MET A  1 755 ? 23.460  50.330 53.541 1.00 18.06 ? 755  MET A N   1 
ATOM   5867  C  CA  . MET A  1 755 ? 24.026  48.988 53.419 1.00 17.92 ? 755  MET A CA  1 
ATOM   5868  C  C   . MET A  1 755 ? 24.209  48.325 54.792 1.00 18.76 ? 755  MET A C   1 
ATOM   5869  O  O   . MET A  1 755 ? 24.040  47.114 54.909 1.00 18.67 ? 755  MET A O   1 
ATOM   5870  C  CB  . MET A  1 755 ? 25.369  49.012 52.678 1.00 18.16 ? 755  MET A CB  1 
ATOM   5871  C  CG  . MET A  1 755 ? 25.259  49.459 51.225 1.00 20.28 ? 755  MET A CG  1 
ATOM   5872  S  SD  . MET A  1 755 ? 26.772  49.196 50.285 1.00 21.25 ? 755  MET A SD  1 
ATOM   5873  C  CE  . MET A  1 755 ? 27.856  50.293 51.089 1.00 19.23 ? 755  MET A CE  1 
ATOM   5874  N  N   . SER A  1 756 ? 24.559  49.106 55.817 1.00 18.41 ? 756  SER A N   1 
ATOM   5875  C  CA  . SER A  1 756 ? 24.730  48.547 57.159 1.00 19.52 ? 756  SER A CA  1 
ATOM   5876  C  C   . SER A  1 756 ? 23.408  47.939 57.658 1.00 19.04 ? 756  SER A C   1 
ATOM   5877  O  O   . SER A  1 756 ? 23.398  46.824 58.170 1.00 17.94 ? 756  SER A O   1 
ATOM   5878  C  CB  . SER A  1 756 ? 25.214  49.616 58.148 1.00 18.50 ? 756  SER A CB  1 
ATOM   5879  O  OG  . SER A  1 756 ? 26.461  50.146 57.767 1.00 20.65 ? 756  SER A OG  1 
ATOM   5880  N  N   . HIS A  1 757 ? 22.308  48.676 57.522 1.00 19.11 ? 757  HIS A N   1 
ATOM   5881  C  CA  . HIS A  1 757 ? 21.001  48.155 57.930 1.00 20.17 ? 757  HIS A CA  1 
ATOM   5882  C  C   . HIS A  1 757 ? 20.725  46.835 57.204 1.00 19.90 ? 757  HIS A C   1 
ATOM   5883  O  O   . HIS A  1 757 ? 20.276  45.865 57.805 1.00 19.53 ? 757  HIS A O   1 
ATOM   5884  C  CB  . HIS A  1 757 ? 19.859  49.124 57.577 1.00 20.08 ? 757  HIS A CB  1 
ATOM   5885  C  CG  . HIS A  1 757 ? 19.849  50.385 58.386 1.00 22.89 ? 757  HIS A CG  1 
ATOM   5886  N  ND1 . HIS A  1 757 ? 19.884  50.387 59.765 1.00 24.57 ? 757  HIS A ND1 1 
ATOM   5887  C  CD2 . HIS A  1 757 ? 19.786  51.685 58.008 1.00 22.19 ? 757  HIS A CD2 1 
ATOM   5888  C  CE1 . HIS A  1 757 ? 19.850  51.635 60.203 1.00 24.41 ? 757  HIS A CE1 1 
ATOM   5889  N  NE2 . HIS A  1 757 ? 19.789  52.442 59.157 1.00 22.66 ? 757  HIS A NE2 1 
ATOM   5890  N  N   . PHE A  1 758 ? 21.013  46.795 55.907 1.00 20.19 ? 758  PHE A N   1 
ATOM   5891  C  CA  . PHE A  1 758 ? 20.756  45.603 55.110 1.00 19.74 ? 758  PHE A CA  1 
ATOM   5892  C  C   . PHE A  1 758 ? 21.569  44.394 55.593 1.00 19.96 ? 758  PHE A C   1 
ATOM   5893  O  O   . PHE A  1 758 ? 21.024  43.301 55.762 1.00 17.45 ? 758  PHE A O   1 
ATOM   5894  C  CB  . PHE A  1 758 ? 21.055  45.886 53.631 1.00 19.00 ? 758  PHE A CB  1 
ATOM   5895  C  CG  . PHE A  1 758 ? 20.738  44.736 52.719 1.00 17.90 ? 758  PHE A CG  1 
ATOM   5896  C  CD1 . PHE A  1 758 ? 19.439  44.522 52.265 1.00 18.27 ? 758  PHE A CD1 1 
ATOM   5897  C  CD2 . PHE A  1 758 ? 21.733  43.837 52.348 1.00 16.36 ? 758  PHE A CD2 1 
ATOM   5898  C  CE1 . PHE A  1 758 ? 19.138  43.418 51.447 1.00 17.27 ? 758  PHE A CE1 1 
ATOM   5899  C  CE2 . PHE A  1 758 ? 21.441  42.738 51.536 1.00 17.16 ? 758  PHE A CE2 1 
ATOM   5900  C  CZ  . PHE A  1 758 ? 20.135  42.529 51.082 1.00 16.90 ? 758  PHE A CZ  1 
ATOM   5901  N  N   . ILE A  1 759 ? 22.864  44.587 55.812 1.00 20.92 ? 759  ILE A N   1 
ATOM   5902  C  CA  . ILE A  1 759 ? 23.703  43.495 56.267 1.00 21.73 ? 759  ILE A CA  1 
ATOM   5903  C  C   . ILE A  1 759 ? 23.269  43.015 57.649 1.00 22.22 ? 759  ILE A C   1 
ATOM   5904  O  O   . ILE A  1 759 ? 23.099  41.821 57.852 1.00 23.01 ? 759  ILE A O   1 
ATOM   5905  C  CB  . ILE A  1 759 ? 25.199  43.892 56.283 1.00 22.84 ? 759  ILE A CB  1 
ATOM   5906  C  CG1 . ILE A  1 759 ? 25.685  44.086 54.857 1.00 22.92 ? 759  ILE A CG1 1 
ATOM   5907  C  CG2 . ILE A  1 759 ? 26.046  42.773 56.923 1.00 22.14 ? 759  ILE A CG2 1 
ATOM   5908  C  CD1 . ILE A  1 759 ? 25.648  42.804 54.027 1.00 24.87 ? 759  ILE A CD1 1 
ATOM   5909  N  N   . LYS A  1 760 ? 23.076  43.931 58.590 1.00 22.85 ? 760  LYS A N   1 
ATOM   5910  C  CA  . LYS A  1 760 ? 22.635  43.561 59.938 1.00 24.75 ? 760  LYS A CA  1 
ATOM   5911  C  C   . LYS A  1 760 ? 21.305  42.785 59.901 1.00 25.68 ? 760  LYS A C   1 
ATOM   5912  O  O   . LYS A  1 760 ? 21.136  41.783 60.587 1.00 24.15 ? 760  LYS A O   1 
ATOM   5913  C  CB  . LYS A  1 760 ? 22.495  44.820 60.801 1.00 23.30 ? 760  LYS A CB  1 
ATOM   5914  C  CG  . LYS A  1 760 ? 23.845  45.459 61.117 1.00 25.06 ? 760  LYS A CG  1 
ATOM   5915  C  CD  . LYS A  1 760 ? 23.705  46.772 61.848 1.00 26.66 ? 760  LYS A CD  1 
ATOM   5916  C  CE  . LYS A  1 760 ? 23.252  46.588 63.284 1.00 29.13 ? 760  LYS A CE  1 
ATOM   5917  N  NZ  . LYS A  1 760 ? 23.266  47.916 63.979 1.00 34.49 ? 760  LYS A NZ  1 
ATOM   5918  N  N   . GLN A  1 761 ? 20.368  43.262 59.096 1.00 26.23 ? 761  GLN A N   1 
ATOM   5919  C  CA  . GLN A  1 761 ? 19.073  42.607 58.941 1.00 28.93 ? 761  GLN A CA  1 
ATOM   5920  C  C   . GLN A  1 761 ? 19.268  41.169 58.391 1.00 29.48 ? 761  GLN A C   1 
ATOM   5921  O  O   . GLN A  1 761 ? 18.658  40.213 58.884 1.00 30.47 ? 761  GLN A O   1 
ATOM   5922  C  CB  . GLN A  1 761 ? 18.205  43.472 58.015 1.00 30.05 ? 761  GLN A CB  1 
ATOM   5923  C  CG  . GLN A  1 761 ? 17.002  42.809 57.419 1.00 35.86 ? 761  GLN A CG  1 
ATOM   5924  C  CD  . GLN A  1 761 ? 17.345  41.875 56.261 1.00 38.46 ? 761  GLN A CD  1 
ATOM   5925  O  OE1 . GLN A  1 761 ? 17.867  42.303 55.211 1.00 38.75 ? 761  GLN A OE1 1 
ATOM   5926  N  NE2 . GLN A  1 761 ? 17.042  40.584 56.443 1.00 40.32 ? 761  GLN A NE2 1 
ATOM   5927  N  N   . CYS A  1 762 ? 20.133  41.014 57.390 1.00 28.33 ? 762  CYS A N   1 
ATOM   5928  C  CA  . CYS A  1 762 ? 20.419  39.700 56.802 1.00 28.95 ? 762  CYS A CA  1 
ATOM   5929  C  C   . CYS A  1 762 ? 21.046  38.753 57.841 1.00 28.21 ? 762  CYS A C   1 
ATOM   5930  O  O   . CYS A  1 762 ? 20.770  37.555 57.848 1.00 28.24 ? 762  CYS A O   1 
ATOM   5931  C  CB  . CYS A  1 762 ? 21.354  39.858 55.582 1.00 29.01 ? 762  CYS A CB  1 
ATOM   5932  S  SG  . CYS A  1 762 ? 22.092  38.322 54.916 1.00 33.33 ? 762  CYS A SG  1 
ATOM   5933  N  N   . PHE A  1 763 ? 21.870  39.303 58.729 1.00 28.12 ? 763  PHE A N   1 
ATOM   5934  C  CA  . PHE A  1 763 ? 22.547  38.512 59.755 1.00 27.98 ? 763  PHE A CA  1 
ATOM   5935  C  C   . PHE A  1 763 ? 21.780  38.435 61.093 1.00 29.98 ? 763  PHE A C   1 
ATOM   5936  O  O   . PHE A  1 763 ? 22.280  37.857 62.057 1.00 29.52 ? 763  PHE A O   1 
ATOM   5937  C  CB  . PHE A  1 763 ? 23.949  39.085 60.015 1.00 24.83 ? 763  PHE A CB  1 
ATOM   5938  C  CG  . PHE A  1 763 ? 24.944  38.863 58.881 1.00 23.13 ? 763  PHE A CG  1 
ATOM   5939  C  CD1 . PHE A  1 763 ? 24.724  37.884 57.900 1.00 21.07 ? 763  PHE A CD1 1 
ATOM   5940  C  CD2 . PHE A  1 763 ? 26.133  39.597 58.838 1.00 20.55 ? 763  PHE A CD2 1 
ATOM   5941  C  CE1 . PHE A  1 763 ? 25.681  37.642 56.899 1.00 20.50 ? 763  PHE A CE1 1 
ATOM   5942  C  CE2 . PHE A  1 763 ? 27.094  39.370 57.853 1.00 20.19 ? 763  PHE A CE2 1 
ATOM   5943  C  CZ  . PHE A  1 763 ? 26.871  38.385 56.876 1.00 20.76 ? 763  PHE A CZ  1 
ATOM   5944  N  N   . SER A  1 764 ? 20.574  39.002 61.142 1.00 32.08 ? 764  SER A N   1 
ATOM   5945  C  CA  . SER A  1 764 ? 19.760  39.023 62.365 1.00 35.50 ? 764  SER A CA  1 
ATOM   5946  C  C   . SER A  1 764 ? 20.518  39.720 63.498 1.00 38.92 ? 764  SER A C   1 
ATOM   5947  O  O   . SER A  1 764 ? 20.519  39.249 64.642 1.00 39.82 ? 764  SER A O   1 
ATOM   5948  C  CB  . SER A  1 764 ? 19.399  37.609 62.829 1.00 35.48 ? 764  SER A CB  1 
ATOM   5949  O  OG  . SER A  1 764 ? 18.776  36.861 61.803 1.00 35.25 ? 764  SER A OG  1 
ATOM   5950  N  N   . LEU A  1 765 ? 21.166  40.840 63.182 1.00 41.76 ? 765  LEU A N   1 
ATOM   5951  C  CA  . LEU A  1 765 ? 21.920  41.592 64.181 1.00 44.39 ? 765  LEU A CA  1 
ATOM   5952  C  C   . LEU A  1 765 ? 21.151  42.822 64.644 1.00 46.59 ? 765  LEU A C   1 
ATOM   5953  O  O   . LEU A  1 765 ? 20.712  43.636 63.833 1.00 46.83 ? 765  LEU A O   1 
ATOM   5954  C  CB  . LEU A  1 765 ? 23.276  42.014 63.619 1.00 42.94 ? 765  LEU A CB  1 
ATOM   5955  C  CG  . LEU A  1 765 ? 24.133  40.852 63.123 1.00 43.01 ? 765  LEU A CG  1 
ATOM   5956  C  CD1 . LEU A  1 765 ? 25.470  41.385 62.613 1.00 42.67 ? 765  LEU A CD1 1 
ATOM   5957  C  CD2 . LEU A  1 765 ? 24.339  39.840 64.248 1.00 41.59 ? 765  LEU A CD2 1 
ATOM   5958  N  N   . PRO A  1 766 ? 20.972  42.966 65.968 1.00 48.67 ? 766  PRO A N   1 
ATOM   5959  C  CA  . PRO A  1 766 ? 20.250  44.107 66.545 1.00 49.65 ? 766  PRO A CA  1 
ATOM   5960  C  C   . PRO A  1 766 ? 20.799  45.414 65.990 1.00 50.06 ? 766  PRO A C   1 
ATOM   5961  O  O   . PRO A  1 766 ? 19.990  46.327 65.703 1.00 51.03 ? 766  PRO A O   1 
ATOM   5962  C  CB  . PRO A  1 766 ? 20.513  43.964 68.044 1.00 49.99 ? 766  PRO A CB  1 
ATOM   5963  C  CG  . PRO A  1 766 ? 20.621  42.460 68.217 1.00 50.10 ? 766  PRO A CG  1 
ATOM   5964  C  CD  . PRO A  1 766 ? 21.471  42.063 67.025 1.00 49.23 ? 766  PRO A CD  1 
ATOM   5965  O  OXT . PRO A  1 766 ? 22.041  45.501 65.866 1.00 50.46 ? 766  PRO A OXT 1 
ATOM   5966  N  N   . THR B  1 39  ? -12.212 25.390 56.603 1.00 46.36 ? 39   THR B N   1 
ATOM   5967  C  CA  . THR B  1 39  ? -12.207 26.893 56.646 1.00 47.08 ? 39   THR B CA  1 
ATOM   5968  C  C   . THR B  1 39  ? -12.116 27.469 55.225 1.00 46.81 ? 39   THR B C   1 
ATOM   5969  O  O   . THR B  1 39  ? -11.315 27.003 54.404 1.00 47.67 ? 39   THR B O   1 
ATOM   5970  C  CB  . THR B  1 39  ? -10.999 27.426 57.459 1.00 47.91 ? 39   THR B CB  1 
ATOM   5971  O  OG1 . THR B  1 39  ? -10.963 26.807 58.759 1.00 49.21 ? 39   THR B OG1 1 
ATOM   5972  C  CG2 . THR B  1 39  ? -11.099 28.938 57.613 1.00 47.43 ? 39   THR B CG2 1 
ATOM   5973  N  N   . ARG B  1 40  ? -12.940 28.466 54.916 1.00 45.27 ? 40   ARG B N   1 
ATOM   5974  C  CA  . ARG B  1 40  ? -12.885 29.060 53.583 1.00 43.48 ? 40   ARG B CA  1 
ATOM   5975  C  C   . ARG B  1 40  ? -11.568 29.822 53.392 1.00 41.46 ? 40   ARG B C   1 
ATOM   5976  O  O   . ARG B  1 40  ? -11.113 30.536 54.293 1.00 40.95 ? 40   ARG B O   1 
ATOM   5977  C  CB  . ARG B  1 40  ? -14.045 30.036 53.365 1.00 44.23 ? 40   ARG B CB  1 
ATOM   5978  C  CG  . ARG B  1 40  ? -15.363 29.409 52.940 1.00 45.18 ? 40   ARG B CG  1 
ATOM   5979  C  CD  . ARG B  1 40  ? -16.346 30.495 52.520 1.00 44.36 ? 40   ARG B CD  1 
ATOM   5980  N  NE  . ARG B  1 40  ? -16.502 31.517 53.557 1.00 45.38 ? 40   ARG B NE  1 
ATOM   5981  C  CZ  . ARG B  1 40  ? -17.285 32.594 53.448 1.00 45.74 ? 40   ARG B CZ  1 
ATOM   5982  N  NH1 . ARG B  1 40  ? -17.996 32.797 52.339 1.00 44.68 ? 40   ARG B NH1 1 
ATOM   5983  N  NH2 . ARG B  1 40  ? -17.349 33.476 54.445 1.00 44.77 ? 40   ARG B NH2 1 
ATOM   5984  N  N   . LYS B  1 41  ? -10.964 29.667 52.222 1.00 39.19 ? 41   LYS B N   1 
ATOM   5985  C  CA  . LYS B  1 41  ? -9.727  30.373 51.916 1.00 37.80 ? 41   LYS B CA  1 
ATOM   5986  C  C   . LYS B  1 41  ? -10.040 31.871 51.824 1.00 35.38 ? 41   LYS B C   1 
ATOM   5987  O  O   . LYS B  1 41  ? -11.207 32.281 51.774 1.00 33.75 ? 41   LYS B O   1 
ATOM   5988  C  CB  . LYS B  1 41  ? -9.153  29.891 50.577 1.00 38.69 ? 41   LYS B CB  1 
ATOM   5989  C  CG  . LYS B  1 41  ? -10.081 30.107 49.383 1.00 40.56 ? 41   LYS B CG  1 
ATOM   5990  C  CD  . LYS B  1 41  ? -9.570  29.392 48.099 1.00 43.33 ? 41   LYS B CD  1 
ATOM   5991  C  CE  . LYS B  1 41  ? -9.636  27.848 48.241 1.00 45.21 ? 41   LYS B CE  1 
ATOM   5992  N  NZ  . LYS B  1 41  ? -9.293  27.074 46.990 1.00 45.81 ? 41   LYS B NZ  1 
ATOM   5993  N  N   . THR B  1 42  ? -8.997  32.683 51.812 1.00 33.21 ? 42   THR B N   1 
ATOM   5994  C  CA  . THR B  1 42  ? -9.165  34.121 51.716 1.00 32.58 ? 42   THR B CA  1 
ATOM   5995  C  C   . THR B  1 42  ? -8.754  34.593 50.315 1.00 31.08 ? 42   THR B C   1 
ATOM   5996  O  O   . THR B  1 42  ? -8.316  33.796 49.480 1.00 32.02 ? 42   THR B O   1 
ATOM   5997  C  CB  . THR B  1 42  ? -8.304  34.828 52.770 1.00 32.96 ? 42   THR B CB  1 
ATOM   5998  O  OG1 . THR B  1 42  ? -6.929  34.469 52.582 1.00 33.74 ? 42   THR B OG1 1 
ATOM   5999  C  CG2 . THR B  1 42  ? -8.722  34.407 54.160 1.00 33.10 ? 42   THR B CG2 1 
ATOM   6000  N  N   . TYR B  1 43  ? -8.929  35.875 50.045 1.00 29.06 ? 43   TYR B N   1 
ATOM   6001  C  CA  . TYR B  1 43  ? -8.535  36.436 48.748 1.00 27.89 ? 43   TYR B CA  1 
ATOM   6002  C  C   . TYR B  1 43  ? -7.056  36.829 48.913 1.00 27.07 ? 43   TYR B C   1 
ATOM   6003  O  O   . TYR B  1 43  ? -6.737  37.811 49.575 1.00 27.21 ? 43   TYR B O   1 
ATOM   6004  C  CB  . TYR B  1 43  ? -9.385  37.667 48.443 1.00 26.85 ? 43   TYR B CB  1 
ATOM   6005  C  CG  . TYR B  1 43  ? -9.115  38.281 47.089 1.00 26.27 ? 43   TYR B CG  1 
ATOM   6006  C  CD1 . TYR B  1 43  ? -9.694  37.751 45.935 1.00 24.13 ? 43   TYR B CD1 1 
ATOM   6007  C  CD2 . TYR B  1 43  ? -8.290  39.394 46.965 1.00 23.75 ? 43   TYR B CD2 1 
ATOM   6008  C  CE1 . TYR B  1 43  ? -9.463  38.325 44.687 1.00 25.00 ? 43   TYR B CE1 1 
ATOM   6009  C  CE2 . TYR B  1 43  ? -8.051  39.980 45.722 1.00 24.76 ? 43   TYR B CE2 1 
ATOM   6010  C  CZ  . TYR B  1 43  ? -8.637  39.452 44.593 1.00 24.00 ? 43   TYR B CZ  1 
ATOM   6011  O  OH  . TYR B  1 43  ? -8.426  40.054 43.378 1.00 23.30 ? 43   TYR B OH  1 
ATOM   6012  N  N   . THR B  1 44  ? -6.174  36.042 48.310 1.00 26.10 ? 44   THR B N   1 
ATOM   6013  C  CA  . THR B  1 44  ? -4.731  36.221 48.417 1.00 24.93 ? 44   THR B CA  1 
ATOM   6014  C  C   . THR B  1 44  ? -4.106  37.175 47.406 1.00 24.66 ? 44   THR B C   1 
ATOM   6015  O  O   . THR B  1 44  ? -4.751  37.587 46.437 1.00 23.53 ? 44   THR B O   1 
ATOM   6016  C  CB  . THR B  1 44  ? -4.030  34.870 48.230 1.00 24.30 ? 44   THR B CB  1 
ATOM   6017  O  OG1 . THR B  1 44  ? -4.226  34.426 46.878 1.00 21.57 ? 44   THR B OG1 1 
ATOM   6018  C  CG2 . THR B  1 44  ? -4.609  33.822 49.201 1.00 22.51 ? 44   THR B CG2 1 
ATOM   6019  N  N   . LEU B  1 45  ? -2.829  37.487 47.625 1.00 25.06 ? 45   LEU B N   1 
ATOM   6020  C  CA  . LEU B  1 45  ? -2.097  38.372 46.725 1.00 24.50 ? 45   LEU B CA  1 
ATOM   6021  C  C   . LEU B  1 45  ? -2.025  37.713 45.367 1.00 24.64 ? 45   LEU B C   1 
ATOM   6022  O  O   . LEU B  1 45  ? -2.186  38.383 44.354 1.00 25.52 ? 45   LEU B O   1 
ATOM   6023  C  CB  . LEU B  1 45  ? -0.668  38.646 47.234 1.00 23.87 ? 45   LEU B CB  1 
ATOM   6024  C  CG  . LEU B  1 45  ? 0.195   39.553 46.325 1.00 23.71 ? 45   LEU B CG  1 
ATOM   6025  C  CD1 . LEU B  1 45  ? -0.437  40.939 46.210 1.00 20.22 ? 45   LEU B CD1 1 
ATOM   6026  C  CD2 . LEU B  1 45  ? 1.599   39.681 46.895 1.00 22.58 ? 45   LEU B CD2 1 
ATOM   6027  N  N   . THR B  1 46  ? -1.787  36.404 45.334 1.00 24.90 ? 46   THR B N   1 
ATOM   6028  C  CA  . THR B  1 46  ? -1.714  35.699 44.054 1.00 26.31 ? 46   THR B CA  1 
ATOM   6029  C  C   . THR B  1 46  ? -3.050  35.739 43.308 1.00 26.70 ? 46   THR B C   1 
ATOM   6030  O  O   . THR B  1 46  ? -3.076  35.763 42.074 1.00 26.81 ? 46   THR B O   1 
ATOM   6031  C  CB  . THR B  1 46  ? -1.317  34.237 44.225 1.00 26.59 ? 46   THR B CB  1 
ATOM   6032  O  OG1 . THR B  1 46  ? -0.113  34.162 44.986 1.00 31.69 ? 46   THR B OG1 1 
ATOM   6033  C  CG2 . THR B  1 46  ? -1.050  33.618 42.889 1.00 28.06 ? 46   THR B CG2 1 
ATOM   6034  N  N   . ASP B  1 47  ? -4.155  35.723 44.052 1.00 26.61 ? 47   ASP B N   1 
ATOM   6035  C  CA  . ASP B  1 47  ? -5.476  35.780 43.432 1.00 27.96 ? 47   ASP B CA  1 
ATOM   6036  C  C   . ASP B  1 47  ? -5.603  37.094 42.671 1.00 28.11 ? 47   ASP B C   1 
ATOM   6037  O  O   . ASP B  1 47  ? -6.091  37.123 41.537 1.00 27.86 ? 47   ASP B O   1 
ATOM   6038  C  CB  . ASP B  1 47  ? -6.574  35.695 44.493 1.00 28.64 ? 47   ASP B CB  1 
ATOM   6039  C  CG  . ASP B  1 47  ? -6.795  34.277 44.986 1.00 28.83 ? 47   ASP B CG  1 
ATOM   6040  O  OD1 . ASP B  1 47  ? -7.201  34.119 46.145 1.00 30.70 ? 47   ASP B OD1 1 
ATOM   6041  O  OD2 . ASP B  1 47  ? -6.565  33.334 44.210 1.00 30.41 ? 47   ASP B OD2 1 
ATOM   6042  N  N   . TYR B  1 48  ? -5.154  38.176 43.302 1.00 28.13 ? 48   TYR B N   1 
ATOM   6043  C  CA  . TYR B  1 48  ? -5.199  39.490 42.676 1.00 28.97 ? 48   TYR B CA  1 
ATOM   6044  C  C   . TYR B  1 48  ? -4.243  39.531 41.482 1.00 28.56 ? 48   TYR B C   1 
ATOM   6045  O  O   . TYR B  1 48  ? -4.656  39.827 40.364 1.00 28.83 ? 48   TYR B O   1 
ATOM   6046  C  CB  . TYR B  1 48  ? -4.833  40.577 43.701 1.00 28.90 ? 48   TYR B CB  1 
ATOM   6047  C  CG  . TYR B  1 48  ? -4.619  41.951 43.100 1.00 29.48 ? 48   TYR B CG  1 
ATOM   6048  C  CD1 . TYR B  1 48  ? -5.588  42.540 42.288 1.00 29.31 ? 48   TYR B CD1 1 
ATOM   6049  C  CD2 . TYR B  1 48  ? -3.441  42.659 43.336 1.00 28.84 ? 48   TYR B CD2 1 
ATOM   6050  C  CE1 . TYR B  1 48  ? -5.385  43.797 41.727 1.00 29.59 ? 48   TYR B CE1 1 
ATOM   6051  C  CE2 . TYR B  1 48  ? -3.231  43.914 42.787 1.00 28.98 ? 48   TYR B CE2 1 
ATOM   6052  C  CZ  . TYR B  1 48  ? -4.207  44.477 41.982 1.00 29.14 ? 48   TYR B CZ  1 
ATOM   6053  O  OH  . TYR B  1 48  ? -4.016  45.725 41.439 1.00 29.58 ? 48   TYR B OH  1 
ATOM   6054  N  N   . LEU B  1 49  ? -2.975  39.199 41.711 1.00 29.74 ? 49   LEU B N   1 
ATOM   6055  C  CA  . LEU B  1 49  ? -1.973  39.228 40.642 1.00 29.15 ? 49   LEU B CA  1 
ATOM   6056  C  C   . LEU B  1 49  ? -2.218  38.230 39.528 1.00 30.70 ? 49   LEU B C   1 
ATOM   6057  O  O   . LEU B  1 49  ? -1.859  38.477 38.376 1.00 29.94 ? 49   LEU B O   1 
ATOM   6058  C  CB  . LEU B  1 49  ? -0.572  39.008 41.221 1.00 27.78 ? 49   LEU B CB  1 
ATOM   6059  C  CG  . LEU B  1 49  ? -0.199  40.029 42.305 1.00 27.83 ? 49   LEU B CG  1 
ATOM   6060  C  CD1 . LEU B  1 49  ? 1.278   39.880 42.668 1.00 27.75 ? 49   LEU B CD1 1 
ATOM   6061  C  CD2 . LEU B  1 49  ? -0.503  41.436 41.799 1.00 25.68 ? 49   LEU B CD2 1 
ATOM   6062  N  N   . LYS B  1 50  ? -2.831  37.099 39.856 1.00 31.21 ? 50   LYS B N   1 
ATOM   6063  C  CA  . LYS B  1 50  ? -3.091  36.112 38.825 1.00 32.80 ? 50   LYS B CA  1 
ATOM   6064  C  C   . LYS B  1 50  ? -4.497  36.228 38.273 1.00 33.54 ? 50   LYS B C   1 
ATOM   6065  O  O   . LYS B  1 50  ? -4.851  35.531 37.331 1.00 34.06 ? 50   LYS B O   1 
ATOM   6066  C  CB  . LYS B  1 50  ? -2.819  34.708 39.356 1.00 33.22 ? 50   LYS B CB  1 
ATOM   6067  C  CG  . LYS B  1 50  ? -1.333  34.488 39.659 1.00 34.69 ? 50   LYS B CG  1 
ATOM   6068  C  CD  . LYS B  1 50  ? -0.455  34.857 38.454 1.00 34.95 ? 50   LYS B CD  1 
ATOM   6069  C  CE  . LYS B  1 50  ? 1.040   34.629 38.740 1.00 36.28 ? 50   LYS B CE  1 
ATOM   6070  N  NZ  . LYS B  1 50  ? 1.886   34.952 37.552 1.00 35.29 ? 50   LYS B NZ  1 
ATOM   6071  N  N   . ASN B  1 51  ? -5.294  37.113 38.863 1.00 34.43 ? 51   ASN B N   1 
ATOM   6072  C  CA  . ASN B  1 51  ? -6.650  37.342 38.388 1.00 34.73 ? 51   ASN B CA  1 
ATOM   6073  C  C   . ASN B  1 51  ? -7.483  36.060 38.401 1.00 34.48 ? 51   ASN B C   1 
ATOM   6074  O  O   . ASN B  1 51  ? -8.203  35.788 37.443 1.00 34.30 ? 51   ASN B O   1 
ATOM   6075  C  CB  . ASN B  1 51  ? -6.571  37.885 36.958 1.00 36.71 ? 51   ASN B CB  1 
ATOM   6076  C  CG  . ASN B  1 51  ? -7.911  38.371 36.433 1.00 40.36 ? 51   ASN B CG  1 
ATOM   6077  O  OD1 . ASN B  1 51  ? -8.266  38.107 35.276 1.00 42.53 ? 51   ASN B OD1 1 
ATOM   6078  N  ND2 . ASN B  1 51  ? -8.656  39.102 37.267 1.00 39.03 ? 51   ASN B ND2 1 
ATOM   6079  N  N   . THR B  1 52  ? -7.411  35.274 39.472 1.00 33.29 ? 52   THR B N   1 
ATOM   6080  C  CA  . THR B  1 52  ? -8.177  34.040 39.493 1.00 32.59 ? 52   THR B CA  1 
ATOM   6081  C  C   . THR B  1 52  ? -9.692  34.271 39.529 1.00 32.52 ? 52   THR B C   1 
ATOM   6082  O  O   . THR B  1 52  ? -10.446 33.478 38.979 1.00 31.45 ? 52   THR B O   1 
ATOM   6083  C  CB  . THR B  1 52  ? -7.758  33.127 40.668 1.00 32.61 ? 52   THR B CB  1 
ATOM   6084  O  OG1 . THR B  1 52  ? -8.488  33.481 41.844 1.00 34.30 ? 52   THR B OG1 1 
ATOM   6085  C  CG2 . THR B  1 52  ? -6.267  33.270 40.942 1.00 31.25 ? 52   THR B CG2 1 
ATOM   6086  N  N   . TYR B  1 53  ? -10.143 35.345 40.167 1.00 33.02 ? 53   TYR B N   1 
ATOM   6087  C  CA  . TYR B  1 53  ? -11.578 35.639 40.222 1.00 34.50 ? 53   TYR B CA  1 
ATOM   6088  C  C   . TYR B  1 53  ? -11.856 36.718 39.186 1.00 36.08 ? 53   TYR B C   1 
ATOM   6089  O  O   . TYR B  1 53  ? -11.747 37.913 39.459 1.00 35.83 ? 53   TYR B O   1 
ATOM   6090  C  CB  . TYR B  1 53  ? -11.962 36.097 41.622 1.00 34.45 ? 53   TYR B CB  1 
ATOM   6091  C  CG  . TYR B  1 53  ? -11.711 35.017 42.659 1.00 35.48 ? 53   TYR B CG  1 
ATOM   6092  C  CD1 . TYR B  1 53  ? -12.477 33.848 42.684 1.00 36.14 ? 53   TYR B CD1 1 
ATOM   6093  C  CD2 . TYR B  1 53  ? -10.668 35.135 43.571 1.00 34.87 ? 53   TYR B CD2 1 
ATOM   6094  C  CE1 . TYR B  1 53  ? -12.202 32.815 43.600 1.00 36.53 ? 53   TYR B CE1 1 
ATOM   6095  C  CE2 . TYR B  1 53  ? -10.383 34.122 44.485 1.00 36.62 ? 53   TYR B CE2 1 
ATOM   6096  C  CZ  . TYR B  1 53  ? -11.151 32.963 44.496 1.00 36.90 ? 53   TYR B CZ  1 
ATOM   6097  O  OH  . TYR B  1 53  ? -10.853 31.972 45.406 1.00 37.73 ? 53   TYR B OH  1 
ATOM   6098  N  N   . ARG B  1 54  ? -12.204 36.276 37.983 1.00 36.92 ? 54   ARG B N   1 
ATOM   6099  C  CA  . ARG B  1 54  ? -12.427 37.183 36.880 1.00 38.41 ? 54   ARG B CA  1 
ATOM   6100  C  C   . ARG B  1 54  ? -13.796 37.815 36.872 1.00 37.97 ? 54   ARG B C   1 
ATOM   6101  O  O   . ARG B  1 54  ? -14.819 37.146 37.008 1.00 38.82 ? 54   ARG B O   1 
ATOM   6102  C  CB  . ARG B  1 54  ? -12.194 36.453 35.559 1.00 41.36 ? 54   ARG B CB  1 
ATOM   6103  C  CG  . ARG B  1 54  ? -11.969 37.372 34.371 1.00 45.05 ? 54   ARG B CG  1 
ATOM   6104  C  CD  . ARG B  1 54  ? -10.627 37.066 33.729 1.00 47.88 ? 54   ARG B CD  1 
ATOM   6105  N  NE  . ARG B  1 54  ? -10.585 35.720 33.150 1.00 50.98 ? 54   ARG B NE  1 
ATOM   6106  C  CZ  . ARG B  1 54  ? -9.545  34.890 33.239 1.00 52.45 ? 54   ARG B CZ  1 
ATOM   6107  N  NH1 . ARG B  1 54  ? -8.443  35.251 33.897 1.00 51.66 ? 54   ARG B NH1 1 
ATOM   6108  N  NH2 . ARG B  1 54  ? -9.603  33.700 32.648 1.00 53.19 ? 54   ARG B NH2 1 
ATOM   6109  N  N   . LEU B  1 55  ? -13.798 39.124 36.695 1.00 37.02 ? 55   LEU B N   1 
ATOM   6110  C  CA  . LEU B  1 55  ? -15.020 39.891 36.636 1.00 36.14 ? 55   LEU B CA  1 
ATOM   6111  C  C   . LEU B  1 55  ? -15.465 39.904 35.169 1.00 36.60 ? 55   LEU B C   1 
ATOM   6112  O  O   . LEU B  1 55  ? -14.687 40.269 34.286 1.00 37.25 ? 55   LEU B O   1 
ATOM   6113  C  CB  . LEU B  1 55  ? -14.719 41.294 37.130 1.00 35.96 ? 55   LEU B CB  1 
ATOM   6114  C  CG  . LEU B  1 55  ? -15.859 42.165 37.612 1.00 37.12 ? 55   LEU B CG  1 
ATOM   6115  C  CD1 . LEU B  1 55  ? -16.764 41.399 38.575 1.00 37.35 ? 55   LEU B CD1 1 
ATOM   6116  C  CD2 . LEU B  1 55  ? -15.259 43.369 38.290 1.00 36.65 ? 55   LEU B CD2 1 
ATOM   6117  N  N   . LYS B  1 56  ? -16.690 39.466 34.896 1.00 36.14 ? 56   LYS B N   1 
ATOM   6118  C  CA  . LYS B  1 56  ? -17.187 39.470 33.526 1.00 36.39 ? 56   LYS B CA  1 
ATOM   6119  C  C   . LYS B  1 56  ? -17.886 40.773 33.207 1.00 35.87 ? 56   LYS B C   1 
ATOM   6120  O  O   . LYS B  1 56  ? -18.444 41.448 34.081 1.00 35.23 ? 56   LYS B O   1 
ATOM   6121  C  CB  . LYS B  1 56  ? -18.186 38.339 33.276 1.00 38.02 ? 56   LYS B CB  1 
ATOM   6122  C  CG  . LYS B  1 56  ? -17.585 36.974 33.020 1.00 39.91 ? 56   LYS B CG  1 
ATOM   6123  C  CD  . LYS B  1 56  ? -18.671 36.027 32.528 1.00 41.87 ? 56   LYS B CD  1 
ATOM   6124  C  CE  . LYS B  1 56  ? -18.192 34.581 32.446 1.00 43.56 ? 56   LYS B CE  1 
ATOM   6125  N  NZ  . LYS B  1 56  ? -17.072 34.404 31.474 1.00 45.54 ? 56   LYS B NZ  1 
ATOM   6126  N  N   . LEU B  1 57  ? -17.855 41.133 31.938 1.00 36.07 ? 57   LEU B N   1 
ATOM   6127  C  CA  . LEU B  1 57  ? -18.530 42.343 31.512 1.00 36.71 ? 57   LEU B CA  1 
ATOM   6128  C  C   . LEU B  1 57  ? -19.232 42.068 30.200 1.00 35.24 ? 57   LEU B C   1 
ATOM   6129  O  O   . LEU B  1 57  ? -19.218 40.933 29.702 1.00 35.78 ? 57   LEU B O   1 
ATOM   6130  C  CB  . LEU B  1 57  ? -17.536 43.493 31.394 1.00 38.76 ? 57   LEU B CB  1 
ATOM   6131  C  CG  . LEU B  1 57  ? -16.187 43.136 30.807 1.00 40.08 ? 57   LEU B CG  1 
ATOM   6132  C  CD1 . LEU B  1 57  ? -16.302 43.155 29.293 1.00 40.40 ? 57   LEU B CD1 1 
ATOM   6133  C  CD2 . LEU B  1 57  ? -15.138 44.136 31.298 1.00 40.56 ? 57   LEU B CD2 1 
ATOM   6134  N  N   . TYR B  1 58  ? -19.860 43.092 29.646 1.00 32.13 ? 58   TYR B N   1 
ATOM   6135  C  CA  . TYR B  1 58  ? -20.573 42.913 28.399 1.00 30.56 ? 58   TYR B CA  1 
ATOM   6136  C  C   . TYR B  1 58  ? -20.365 44.138 27.505 1.00 30.16 ? 58   TYR B C   1 
ATOM   6137  O  O   . TYR B  1 58  ? -21.185 45.047 27.499 1.00 29.76 ? 58   TYR B O   1 
ATOM   6138  C  CB  . TYR B  1 58  ? -22.067 42.680 28.703 1.00 27.05 ? 58   TYR B CB  1 
ATOM   6139  C  CG  . TYR B  1 58  ? -22.839 42.063 27.559 1.00 27.27 ? 58   TYR B CG  1 
ATOM   6140  C  CD1 . TYR B  1 58  ? -23.243 42.835 26.467 1.00 25.67 ? 58   TYR B CD1 1 
ATOM   6141  C  CD2 . TYR B  1 58  ? -23.148 40.692 27.550 1.00 26.73 ? 58   TYR B CD2 1 
ATOM   6142  C  CE1 . TYR B  1 58  ? -23.938 42.266 25.391 1.00 26.56 ? 58   TYR B CE1 1 
ATOM   6143  C  CE2 . TYR B  1 58  ? -23.843 40.112 26.474 1.00 25.80 ? 58   TYR B CE2 1 
ATOM   6144  C  CZ  . TYR B  1 58  ? -24.235 40.906 25.399 1.00 26.31 ? 58   TYR B CZ  1 
ATOM   6145  O  OH  . TYR B  1 58  ? -24.915 40.361 24.323 1.00 25.71 ? 58   TYR B OH  1 
ATOM   6146  N  N   . SER B  1 59  ? -19.265 44.159 26.764 1.00 29.82 ? 59   SER B N   1 
ATOM   6147  C  CA  . SER B  1 59  ? -18.960 45.285 25.882 1.00 30.33 ? 59   SER B CA  1 
ATOM   6148  C  C   . SER B  1 59  ? -19.592 45.086 24.520 1.00 30.16 ? 59   SER B C   1 
ATOM   6149  O  O   . SER B  1 59  ? -19.215 44.179 23.791 1.00 30.68 ? 59   SER B O   1 
ATOM   6150  C  CB  . SER B  1 59  ? -17.444 45.433 25.686 1.00 30.28 ? 59   SER B CB  1 
ATOM   6151  O  OG  . SER B  1 59  ? -16.766 45.514 26.931 1.00 32.31 ? 59   SER B OG  1 
ATOM   6152  N  N   . LEU B  1 60  ? -20.548 45.937 24.170 1.00 29.26 ? 60   LEU B N   1 
ATOM   6153  C  CA  . LEU B  1 60  ? -21.208 45.839 22.881 1.00 28.64 ? 60   LEU B CA  1 
ATOM   6154  C  C   . LEU B  1 60  ? -20.941 47.125 22.115 1.00 28.90 ? 60   LEU B C   1 
ATOM   6155  O  O   . LEU B  1 60  ? -20.521 48.124 22.696 1.00 29.06 ? 60   LEU B O   1 
ATOM   6156  C  CB  . LEU B  1 60  ? -22.724 45.637 23.078 1.00 26.89 ? 60   LEU B CB  1 
ATOM   6157  C  CG  . LEU B  1 60  ? -23.522 46.732 23.820 1.00 26.84 ? 60   LEU B CG  1 
ATOM   6158  C  CD1 . LEU B  1 60  ? -23.673 47.933 22.900 1.00 23.76 ? 60   LEU B CD1 1 
ATOM   6159  C  CD2 . LEU B  1 60  ? -24.903 46.207 24.263 1.00 22.95 ? 60   LEU B CD2 1 
ATOM   6160  N  N   . ARG B  1 61  ? -21.175 47.094 20.810 1.00 30.09 ? 61   ARG B N   1 
ATOM   6161  C  CA  . ARG B  1 61  ? -20.995 48.270 19.959 1.00 30.63 ? 61   ARG B CA  1 
ATOM   6162  C  C   . ARG B  1 61  ? -22.260 48.446 19.138 1.00 30.50 ? 61   ARG B C   1 
ATOM   6163  O  O   . ARG B  1 61  ? -22.595 47.589 18.323 1.00 31.34 ? 61   ARG B O   1 
ATOM   6164  C  CB  . ARG B  1 61  ? -19.829 48.079 18.991 1.00 32.86 ? 61   ARG B CB  1 
ATOM   6165  C  CG  . ARG B  1 61  ? -18.491 47.851 19.645 1.00 36.23 ? 61   ARG B CG  1 
ATOM   6166  C  CD  . ARG B  1 61  ? -17.401 47.740 18.590 1.00 37.88 ? 61   ARG B CD  1 
ATOM   6167  N  NE  . ARG B  1 61  ? -16.086 47.527 19.189 1.00 38.77 ? 61   ARG B NE  1 
ATOM   6168  C  CZ  . ARG B  1 61  ? -14.964 47.395 18.492 1.00 39.38 ? 61   ARG B CZ  1 
ATOM   6169  N  NH1 . ARG B  1 61  ? -14.992 47.454 17.164 1.00 39.30 ? 61   ARG B NH1 1 
ATOM   6170  N  NH2 . ARG B  1 61  ? -13.817 47.200 19.124 1.00 38.96 ? 61   ARG B NH2 1 
ATOM   6171  N  N   . TRP B  1 62  ? -22.964 49.545 19.353 1.00 30.06 ? 62   TRP B N   1 
ATOM   6172  C  CA  . TRP B  1 62  ? -24.180 49.801 18.605 1.00 30.65 ? 62   TRP B CA  1 
ATOM   6173  C  C   . TRP B  1 62  ? -23.782 50.123 17.176 1.00 31.63 ? 62   TRP B C   1 
ATOM   6174  O  O   . TRP B  1 62  ? -22.858 50.906 16.964 1.00 32.31 ? 62   TRP B O   1 
ATOM   6175  C  CB  . TRP B  1 62  ? -24.936 50.990 19.207 1.00 28.75 ? 62   TRP B CB  1 
ATOM   6176  C  CG  . TRP B  1 62  ? -25.557 50.691 20.540 1.00 29.40 ? 62   TRP B CG  1 
ATOM   6177  C  CD1 . TRP B  1 62  ? -25.137 51.125 21.768 1.00 28.73 ? 62   TRP B CD1 1 
ATOM   6178  C  CD2 . TRP B  1 62  ? -26.724 49.887 20.775 1.00 28.24 ? 62   TRP B CD2 1 
ATOM   6179  N  NE1 . TRP B  1 62  ? -25.977 50.642 22.753 1.00 28.32 ? 62   TRP B NE1 1 
ATOM   6180  C  CE2 . TRP B  1 62  ? -26.956 49.880 22.169 1.00 28.01 ? 62   TRP B CE2 1 
ATOM   6181  C  CE3 . TRP B  1 62  ? -27.593 49.173 19.940 1.00 27.53 ? 62   TRP B CE3 1 
ATOM   6182  C  CZ2 . TRP B  1 62  ? -28.024 49.186 22.748 1.00 27.86 ? 62   TRP B CZ2 1 
ATOM   6183  C  CZ3 . TRP B  1 62  ? -28.654 48.481 20.512 1.00 29.95 ? 62   TRP B CZ3 1 
ATOM   6184  C  CH2 . TRP B  1 62  ? -28.860 48.494 21.908 1.00 27.85 ? 62   TRP B CH2 1 
ATOM   6185  N  N   . ILE B  1 63  ? -24.459 49.530 16.197 1.00 31.99 ? 63   ILE B N   1 
ATOM   6186  C  CA  . ILE B  1 63  ? -24.141 49.816 14.801 1.00 32.96 ? 63   ILE B CA  1 
ATOM   6187  C  C   . ILE B  1 63  ? -25.324 50.468 14.127 1.00 33.53 ? 63   ILE B C   1 
ATOM   6188  O  O   . ILE B  1 63  ? -25.232 50.911 12.981 1.00 34.91 ? 63   ILE B O   1 
ATOM   6189  C  CB  . ILE B  1 63  ? -23.748 48.538 14.019 1.00 33.10 ? 63   ILE B CB  1 
ATOM   6190  C  CG1 . ILE B  1 63  ? -24.916 47.546 13.989 1.00 33.22 ? 63   ILE B CG1 1 
ATOM   6191  C  CG2 . ILE B  1 63  ? -22.548 47.889 14.683 1.00 32.78 ? 63   ILE B CG2 1 
ATOM   6192  C  CD1 . ILE B  1 63  ? -24.721 46.405 13.005 1.00 31.66 ? 63   ILE B CD1 1 
ATOM   6193  N  N   . SER B  1 64  ? -26.431 50.546 14.859 1.00 33.47 ? 64   SER B N   1 
ATOM   6194  C  CA  . SER B  1 64  ? -27.656 51.161 14.355 1.00 33.21 ? 64   SER B CA  1 
ATOM   6195  C  C   . SER B  1 64  ? -28.593 51.461 15.531 1.00 33.70 ? 64   SER B C   1 
ATOM   6196  O  O   . SER B  1 64  ? -28.205 51.354 16.696 1.00 32.63 ? 64   SER B O   1 
ATOM   6197  C  CB  . SER B  1 64  ? -28.367 50.205 13.409 1.00 32.36 ? 64   SER B CB  1 
ATOM   6198  O  OG  . SER B  1 64  ? -28.954 49.151 14.157 1.00 32.54 ? 64   SER B OG  1 
ATOM   6199  N  N   . ASP B  1 65  ? -29.839 51.798 15.228 1.00 33.99 ? 65   ASP B N   1 
ATOM   6200  C  CA  . ASP B  1 65  ? -30.780 52.074 16.288 1.00 35.57 ? 65   ASP B CA  1 
ATOM   6201  C  C   . ASP B  1 65  ? -31.325 50.817 16.968 1.00 36.08 ? 65   ASP B C   1 
ATOM   6202  O  O   . ASP B  1 65  ? -32.019 50.910 17.980 1.00 36.21 ? 65   ASP B O   1 
ATOM   6203  C  CB  . ASP B  1 65  ? -31.935 52.920 15.775 1.00 37.27 ? 65   ASP B CB  1 
ATOM   6204  C  CG  . ASP B  1 65  ? -32.626 53.664 16.895 1.00 39.70 ? 65   ASP B CG  1 
ATOM   6205  O  OD1 . ASP B  1 65  ? -31.920 54.077 17.848 1.00 39.75 ? 65   ASP B OD1 1 
ATOM   6206  O  OD2 . ASP B  1 65  ? -33.861 53.855 16.829 1.00 42.79 ? 65   ASP B OD2 1 
ATOM   6207  N  N   . HIS B  1 66  ? -31.020 49.640 16.436 1.00 35.58 ? 66   HIS B N   1 
ATOM   6208  C  CA  . HIS B  1 66  ? -31.516 48.432 17.073 1.00 37.40 ? 66   HIS B CA  1 
ATOM   6209  C  C   . HIS B  1 66  ? -30.646 47.184 16.952 1.00 35.64 ? 66   HIS B C   1 
ATOM   6210  O  O   . HIS B  1 66  ? -31.106 46.083 17.235 1.00 34.70 ? 66   HIS B O   1 
ATOM   6211  C  CB  . HIS B  1 66  ? -32.931 48.121 16.586 1.00 41.10 ? 66   HIS B CB  1 
ATOM   6212  C  CG  . HIS B  1 66  ? -33.098 48.266 15.112 1.00 44.32 ? 66   HIS B CG  1 
ATOM   6213  N  ND1 . HIS B  1 66  ? -33.214 49.495 14.499 1.00 46.11 ? 66   HIS B ND1 1 
ATOM   6214  C  CD2 . HIS B  1 66  ? -33.105 47.343 14.122 1.00 46.36 ? 66   HIS B CD2 1 
ATOM   6215  C  CE1 . HIS B  1 66  ? -33.282 49.324 13.191 1.00 47.41 ? 66   HIS B CE1 1 
ATOM   6216  N  NE2 . HIS B  1 66  ? -33.218 48.027 12.935 1.00 48.35 ? 66   HIS B NE2 1 
ATOM   6217  N  N   . GLU B  1 67  ? -29.394 47.357 16.539 1.00 34.69 ? 67   GLU B N   1 
ATOM   6218  C  CA  . GLU B  1 67  ? -28.463 46.237 16.432 1.00 33.71 ? 67   GLU B CA  1 
ATOM   6219  C  C   . GLU B  1 67  ? -27.110 46.598 17.022 1.00 32.89 ? 67   GLU B C   1 
ATOM   6220  O  O   . GLU B  1 67  ? -26.661 47.747 16.934 1.00 32.29 ? 67   GLU B O   1 
ATOM   6221  C  CB  . GLU B  1 67  ? -28.248 45.824 14.983 1.00 34.22 ? 67   GLU B CB  1 
ATOM   6222  C  CG  . GLU B  1 67  ? -29.421 45.154 14.330 1.00 36.83 ? 67   GLU B CG  1 
ATOM   6223  C  CD  . GLU B  1 67  ? -29.000 44.418 13.067 1.00 39.23 ? 67   GLU B CD  1 
ATOM   6224  O  OE1 . GLU B  1 67  ? -28.384 45.053 12.179 1.00 38.06 ? 67   GLU B OE1 1 
ATOM   6225  O  OE2 . GLU B  1 67  ? -29.282 43.201 12.973 1.00 40.81 ? 67   GLU B OE2 1 
ATOM   6226  N  N   . TYR B  1 68  ? -26.453 45.611 17.619 1.00 31.90 ? 68   TYR B N   1 
ATOM   6227  C  CA  . TYR B  1 68  ? -25.142 45.834 18.203 1.00 31.80 ? 68   TYR B CA  1 
ATOM   6228  C  C   . TYR B  1 68  ? -24.259 44.630 17.976 1.00 32.77 ? 68   TYR B C   1 
ATOM   6229  O  O   . TYR B  1 68  ? -24.747 43.513 17.813 1.00 32.45 ? 68   TYR B O   1 
ATOM   6230  C  CB  . TYR B  1 68  ? -25.248 46.134 19.703 1.00 30.02 ? 68   TYR B CB  1 
ATOM   6231  C  CG  . TYR B  1 68  ? -25.713 44.992 20.594 1.00 27.37 ? 68   TYR B CG  1 
ATOM   6232  C  CD1 . TYR B  1 68  ? -24.848 43.957 20.957 1.00 27.67 ? 68   TYR B CD1 1 
ATOM   6233  C  CD2 . TYR B  1 68  ? -26.999 44.981 21.120 1.00 26.40 ? 68   TYR B CD2 1 
ATOM   6234  C  CE1 . TYR B  1 68  ? -25.263 42.934 21.832 1.00 26.60 ? 68   TYR B CE1 1 
ATOM   6235  C  CE2 . TYR B  1 68  ? -27.424 43.978 21.986 1.00 25.48 ? 68   TYR B CE2 1 
ATOM   6236  C  CZ  . TYR B  1 68  ? -26.565 42.960 22.342 1.00 26.21 ? 68   TYR B CZ  1 
ATOM   6237  O  OH  . TYR B  1 68  ? -27.008 41.976 23.200 1.00 25.71 ? 68   TYR B OH  1 
ATOM   6238  N  N   . LEU B  1 69  ? -22.952 44.870 17.954 1.00 33.80 ? 69   LEU B N   1 
ATOM   6239  C  CA  . LEU B  1 69  ? -21.987 43.806 17.749 1.00 34.19 ? 69   LEU B CA  1 
ATOM   6240  C  C   . LEU B  1 69  ? -21.473 43.353 19.105 1.00 35.87 ? 69   LEU B C   1 
ATOM   6241  O  O   . LEU B  1 69  ? -21.389 44.137 20.052 1.00 35.83 ? 69   LEU B O   1 
ATOM   6242  C  CB  . LEU B  1 69  ? -20.829 44.308 16.870 1.00 33.38 ? 69   LEU B CB  1 
ATOM   6243  C  CG  . LEU B  1 69  ? -21.216 44.862 15.486 1.00 33.08 ? 69   LEU B CG  1 
ATOM   6244  C  CD1 . LEU B  1 69  ? -19.987 45.420 14.767 1.00 31.23 ? 69   LEU B CD1 1 
ATOM   6245  C  CD2 . LEU B  1 69  ? -21.866 43.758 14.655 1.00 31.22 ? 69   LEU B CD2 1 
ATOM   6246  N  N   . TYR B  1 70  ? -21.152 42.076 19.209 1.00 38.37 ? 70   TYR B N   1 
ATOM   6247  C  CA  . TYR B  1 70  ? -20.638 41.533 20.454 1.00 40.71 ? 70   TYR B CA  1 
ATOM   6248  C  C   . TYR B  1 70  ? -19.702 40.401 20.096 1.00 43.62 ? 70   TYR B C   1 
ATOM   6249  O  O   . TYR B  1 70  ? -20.031 39.579 19.237 1.00 44.46 ? 70   TYR B O   1 
ATOM   6250  C  CB  . TYR B  1 70  ? -21.779 41.000 21.324 1.00 39.87 ? 70   TYR B CB  1 
ATOM   6251  C  CG  . TYR B  1 70  ? -21.319 40.479 22.670 1.00 39.30 ? 70   TYR B CG  1 
ATOM   6252  C  CD1 . TYR B  1 70  ? -20.755 41.336 23.606 1.00 38.31 ? 70   TYR B CD1 1 
ATOM   6253  C  CD2 . TYR B  1 70  ? -21.410 39.122 22.989 1.00 39.82 ? 70   TYR B CD2 1 
ATOM   6254  C  CE1 . TYR B  1 70  ? -20.287 40.866 24.819 1.00 39.74 ? 70   TYR B CE1 1 
ATOM   6255  C  CE2 . TYR B  1 70  ? -20.941 38.639 24.206 1.00 39.89 ? 70   TYR B CE2 1 
ATOM   6256  C  CZ  . TYR B  1 70  ? -20.379 39.521 25.114 1.00 40.00 ? 70   TYR B CZ  1 
ATOM   6257  O  OH  . TYR B  1 70  ? -19.887 39.062 26.314 1.00 43.22 ? 70   TYR B OH  1 
ATOM   6258  N  N   . LYS B  1 71  ? -18.529 40.371 20.726 1.00 47.08 ? 71   LYS B N   1 
ATOM   6259  C  CA  . LYS B  1 71  ? -17.554 39.311 20.475 1.00 49.87 ? 71   LYS B CA  1 
ATOM   6260  C  C   . LYS B  1 71  ? -17.761 38.114 21.409 1.00 51.69 ? 71   LYS B C   1 
ATOM   6261  O  O   . LYS B  1 71  ? -17.687 38.245 22.638 1.00 52.38 ? 71   LYS B O   1 
ATOM   6262  C  CB  . LYS B  1 71  ? -16.127 39.843 20.628 1.00 50.11 ? 71   LYS B CB  1 
ATOM   6263  C  CG  . LYS B  1 71  ? -15.502 40.310 19.310 1.00 52.05 ? 71   LYS B CG  1 
ATOM   6264  C  CD  . LYS B  1 71  ? -13.999 40.564 19.463 1.00 52.91 ? 71   LYS B CD  1 
ATOM   6265  C  CE  . LYS B  1 71  ? -13.268 40.477 18.112 1.00 54.00 ? 71   LYS B CE  1 
ATOM   6266  N  NZ  . LYS B  1 71  ? -11.810 40.847 18.195 1.00 53.46 ? 71   LYS B NZ  1 
ATOM   6267  N  N   . GLN B  1 72  ? -18.026 36.950 20.816 1.00 53.33 ? 72   GLN B N   1 
ATOM   6268  C  CA  . GLN B  1 72  ? -18.247 35.722 21.579 1.00 54.26 ? 72   GLN B CA  1 
ATOM   6269  C  C   . GLN B  1 72  ? -17.512 34.569 20.915 1.00 54.86 ? 72   GLN B C   1 
ATOM   6270  O  O   . GLN B  1 72  ? -17.700 34.320 19.723 1.00 54.75 ? 72   GLN B O   1 
ATOM   6271  C  CB  . GLN B  1 72  ? -19.737 35.401 21.634 1.00 55.02 ? 72   GLN B CB  1 
ATOM   6272  C  CG  . GLN B  1 72  ? -20.103 34.316 22.620 1.00 56.48 ? 72   GLN B CG  1 
ATOM   6273  C  CD  . GLN B  1 72  ? -21.601 34.247 22.855 1.00 58.11 ? 72   GLN B CD  1 
ATOM   6274  O  OE1 . GLN B  1 72  ? -22.345 33.645 22.068 1.00 58.42 ? 72   GLN B OE1 1 
ATOM   6275  N  NE2 . GLN B  1 72  ? -22.060 34.890 23.929 1.00 58.45 ? 72   GLN B NE2 1 
ATOM   6276  N  N   . GLU B  1 73  ? -16.683 33.864 21.687 1.00 55.96 ? 73   GLU B N   1 
ATOM   6277  C  CA  . GLU B  1 73  ? -15.908 32.731 21.160 1.00 56.61 ? 73   GLU B CA  1 
ATOM   6278  C  C   . GLU B  1 73  ? -14.901 33.249 20.111 1.00 56.47 ? 73   GLU B C   1 
ATOM   6279  O  O   . GLU B  1 73  ? -14.526 32.529 19.183 1.00 56.59 ? 73   GLU B O   1 
ATOM   6280  C  CB  . GLU B  1 73  ? -16.848 31.689 20.514 1.00 57.70 ? 73   GLU B CB  1 
ATOM   6281  C  CG  . GLU B  1 73  ? -17.920 31.072 21.455 1.00 59.20 ? 73   GLU B CG  1 
ATOM   6282  C  CD  . GLU B  1 73  ? -19.160 30.541 20.699 1.00 60.15 ? 73   GLU B CD  1 
ATOM   6283  O  OE1 . GLU B  1 73  ? -19.042 29.557 19.927 1.00 60.73 ? 73   GLU B OE1 1 
ATOM   6284  O  OE2 . GLU B  1 73  ? -20.259 31.115 20.881 1.00 60.15 ? 73   GLU B OE2 1 
ATOM   6285  N  N   . ASN B  1 74  ? -14.487 34.507 20.261 1.00 55.86 ? 74   ASN B N   1 
ATOM   6286  C  CA  . ASN B  1 74  ? -13.526 35.148 19.356 1.00 55.00 ? 74   ASN B CA  1 
ATOM   6287  C  C   . ASN B  1 74  ? -14.083 35.543 17.985 1.00 54.20 ? 74   ASN B C   1 
ATOM   6288  O  O   . ASN B  1 74  ? -13.342 36.023 17.115 1.00 54.50 ? 74   ASN B O   1 
ATOM   6289  C  CB  . ASN B  1 74  ? -12.283 34.266 19.184 1.00 55.75 ? 74   ASN B CB  1 
ATOM   6290  C  CG  . ASN B  1 74  ? -10.984 35.048 19.374 1.00 56.62 ? 74   ASN B CG  1 
ATOM   6291  O  OD1 . ASN B  1 74  ? -9.944  34.473 19.707 1.00 57.56 ? 74   ASN B OD1 1 
ATOM   6292  N  ND2 . ASN B  1 74  ? -11.038 36.363 19.151 1.00 56.22 ? 74   ASN B ND2 1 
ATOM   6293  N  N   . ASN B  1 75  ? -15.380 35.332 17.782 1.00 52.73 ? 75   ASN B N   1 
ATOM   6294  C  CA  . ASN B  1 75  ? -16.013 35.740 16.538 1.00 51.35 ? 75   ASN B CA  1 
ATOM   6295  C  C   . ASN B  1 75  ? -16.961 36.901 16.843 1.00 50.03 ? 75   ASN B C   1 
ATOM   6296  O  O   . ASN B  1 75  ? -17.421 37.070 17.984 1.00 50.12 ? 75   ASN B O   1 
ATOM   6297  C  CB  . ASN B  1 75  ? -16.776 34.581 15.885 1.00 53.01 ? 75   ASN B CB  1 
ATOM   6298  C  CG  . ASN B  1 75  ? -17.197 33.519 16.878 1.00 53.55 ? 75   ASN B CG  1 
ATOM   6299  O  OD1 . ASN B  1 75  ? -16.360 32.837 17.469 1.00 54.14 ? 75   ASN B OD1 1 
ATOM   6300  N  ND2 . ASN B  1 75  ? -18.503 33.370 17.066 1.00 54.22 ? 75   ASN B ND2 1 
ATOM   6301  N  N   . ILE B  1 76  ? -17.245 37.708 15.827 1.00 47.31 ? 76   ILE B N   1 
ATOM   6302  C  CA  . ILE B  1 76  ? -18.115 38.859 16.005 1.00 45.23 ? 76   ILE B CA  1 
ATOM   6303  C  C   . ILE B  1 76  ? -19.572 38.561 15.686 1.00 43.80 ? 76   ILE B C   1 
ATOM   6304  O  O   . ILE B  1 76  ? -19.921 38.230 14.552 1.00 43.93 ? 76   ILE B O   1 
ATOM   6305  C  CB  . ILE B  1 76  ? -17.653 40.033 15.124 1.00 44.68 ? 76   ILE B CB  1 
ATOM   6306  C  CG1 . ILE B  1 76  ? -16.203 40.400 15.466 1.00 44.20 ? 76   ILE B CG1 1 
ATOM   6307  C  CG2 . ILE B  1 76  ? -18.560 41.233 15.337 1.00 44.82 ? 76   ILE B CG2 1 
ATOM   6308  C  CD1 . ILE B  1 76  ? -15.627 41.507 14.571 1.00 44.65 ? 76   ILE B CD1 1 
ATOM   6309  N  N   . LEU B  1 77  ? -20.425 38.692 16.692 1.00 41.85 ? 77   LEU B N   1 
ATOM   6310  C  CA  . LEU B  1 77  ? -21.852 38.451 16.515 1.00 40.61 ? 77   LEU B CA  1 
ATOM   6311  C  C   . LEU B  1 77  ? -22.646 39.756 16.425 1.00 39.63 ? 77   LEU B C   1 
ATOM   6312  O  O   . LEU B  1 77  ? -22.216 40.798 16.939 1.00 39.09 ? 77   LEU B O   1 
ATOM   6313  C  CB  . LEU B  1 77  ? -22.376 37.614 17.684 1.00 40.86 ? 77   LEU B CB  1 
ATOM   6314  C  CG  . LEU B  1 77  ? -22.338 36.077 17.582 1.00 41.23 ? 77   LEU B CG  1 
ATOM   6315  C  CD1 . LEU B  1 77  ? -21.104 35.602 16.846 1.00 39.75 ? 77   LEU B CD1 1 
ATOM   6316  C  CD2 . LEU B  1 77  ? -22.400 35.493 18.995 1.00 40.88 ? 77   LEU B CD2 1 
ATOM   6317  N  N   . VAL B  1 78  ? -23.786 39.700 15.740 1.00 37.93 ? 78   VAL B N   1 
ATOM   6318  C  CA  . VAL B  1 78  ? -24.668 40.856 15.622 1.00 36.85 ? 78   VAL B CA  1 
ATOM   6319  C  C   . VAL B  1 78  ? -25.998 40.496 16.307 1.00 36.81 ? 78   VAL B C   1 
ATOM   6320  O  O   . VAL B  1 78  ? -26.647 39.513 15.952 1.00 37.42 ? 78   VAL B O   1 
ATOM   6321  C  CB  . VAL B  1 78  ? -24.924 41.236 14.145 1.00 36.91 ? 78   VAL B CB  1 
ATOM   6322  C  CG1 . VAL B  1 78  ? -25.464 40.037 13.354 1.00 36.79 ? 78   VAL B CG1 1 
ATOM   6323  C  CG2 . VAL B  1 78  ? -25.896 42.405 14.077 1.00 36.30 ? 78   VAL B CG2 1 
ATOM   6324  N  N   . PHE B  1 79  ? -26.391 41.286 17.301 1.00 35.50 ? 79   PHE B N   1 
ATOM   6325  C  CA  . PHE B  1 79  ? -27.621 41.025 18.042 1.00 34.18 ? 79   PHE B CA  1 
ATOM   6326  C  C   . PHE B  1 79  ? -28.743 41.974 17.689 1.00 33.49 ? 79   PHE B C   1 
ATOM   6327  O  O   . PHE B  1 79  ? -28.515 43.137 17.380 1.00 34.08 ? 79   PHE B O   1 
ATOM   6328  C  CB  . PHE B  1 79  ? -27.376 41.151 19.546 1.00 33.02 ? 79   PHE B CB  1 
ATOM   6329  C  CG  . PHE B  1 79  ? -26.687 39.974 20.165 1.00 32.98 ? 79   PHE B CG  1 
ATOM   6330  C  CD1 . PHE B  1 79  ? -27.420 38.995 20.839 1.00 32.71 ? 79   PHE B CD1 1 
ATOM   6331  C  CD2 . PHE B  1 79  ? -25.302 39.863 20.119 1.00 32.63 ? 79   PHE B CD2 1 
ATOM   6332  C  CE1 . PHE B  1 79  ? -26.784 37.921 21.460 1.00 31.92 ? 79   PHE B CE1 1 
ATOM   6333  C  CE2 . PHE B  1 79  ? -24.654 38.793 20.738 1.00 33.08 ? 79   PHE B CE2 1 
ATOM   6334  C  CZ  . PHE B  1 79  ? -25.399 37.821 21.411 1.00 32.69 ? 79   PHE B CZ  1 
ATOM   6335  N  N   . ASN B  1 80  ? -29.964 41.463 17.746 1.00 32.63 ? 80   ASN B N   1 
ATOM   6336  C  CA  . ASN B  1 80  ? -31.138 42.275 17.501 1.00 32.07 ? 80   ASN B CA  1 
ATOM   6337  C  C   . ASN B  1 80  ? -31.565 42.692 18.910 1.00 31.63 ? 80   ASN B C   1 
ATOM   6338  O  O   . ASN B  1 80  ? -31.976 41.855 19.704 1.00 32.07 ? 80   ASN B O   1 
ATOM   6339  C  CB  . ASN B  1 80  ? -32.244 41.448 16.835 1.00 31.99 ? 80   ASN B CB  1 
ATOM   6340  C  CG  . ASN B  1 80  ? -33.546 42.206 16.744 1.00 31.81 ? 80   ASN B CG  1 
ATOM   6341  O  OD1 . ASN B  1 80  ? -34.250 42.376 17.747 1.00 31.28 ? 80   ASN B OD1 1 
ATOM   6342  N  ND2 . ASN B  1 80  ? -33.869 42.692 15.543 1.00 30.32 ? 80   ASN B ND2 1 
ATOM   6343  N  N   . ALA B  1 81  ? -31.450 43.976 19.225 1.00 31.18 ? 81   ALA B N   1 
ATOM   6344  C  CA  . ALA B  1 81  ? -31.802 44.460 20.551 1.00 32.09 ? 81   ALA B CA  1 
ATOM   6345  C  C   . ALA B  1 81  ? -33.211 44.084 21.017 1.00 32.75 ? 81   ALA B C   1 
ATOM   6346  O  O   . ALA B  1 81  ? -33.413 43.688 22.169 1.00 31.54 ? 81   ALA B O   1 
ATOM   6347  C  CB  . ALA B  1 81  ? -31.634 45.985 20.613 1.00 30.51 ? 81   ALA B CB  1 
ATOM   6348  N  N   . GLU B  1 82  ? -34.176 44.226 20.122 1.00 33.11 ? 82   GLU B N   1 
ATOM   6349  C  CA  . GLU B  1 82  ? -35.574 43.958 20.425 1.00 36.07 ? 82   GLU B CA  1 
ATOM   6350  C  C   . GLU B  1 82  ? -35.931 42.531 20.859 1.00 36.05 ? 82   GLU B C   1 
ATOM   6351  O  O   . GLU B  1 82  ? -36.767 42.357 21.744 1.00 35.43 ? 82   GLU B O   1 
ATOM   6352  C  CB  . GLU B  1 82  ? -36.419 44.339 19.215 1.00 38.58 ? 82   GLU B CB  1 
ATOM   6353  C  CG  . GLU B  1 82  ? -37.886 44.543 19.501 1.00 42.92 ? 82   GLU B CG  1 
ATOM   6354  C  CD  . GLU B  1 82  ? -38.672 44.815 18.221 1.00 46.14 ? 82   GLU B CD  1 
ATOM   6355  O  OE1 . GLU B  1 82  ? -38.138 45.509 17.318 1.00 46.82 ? 82   GLU B OE1 1 
ATOM   6356  O  OE2 . GLU B  1 82  ? -39.825 44.344 18.121 1.00 48.12 ? 82   GLU B OE2 1 
ATOM   6357  N  N   . TYR B  1 83  ? -35.300 41.529 20.245 1.00 36.26 ? 83   TYR B N   1 
ATOM   6358  C  CA  . TYR B  1 83  ? -35.598 40.135 20.551 1.00 37.35 ? 83   TYR B CA  1 
ATOM   6359  C  C   . TYR B  1 83  ? -34.467 39.314 21.169 1.00 37.47 ? 83   TYR B C   1 
ATOM   6360  O  O   . TYR B  1 83  ? -34.695 38.212 21.673 1.00 37.43 ? 83   TYR B O   1 
ATOM   6361  C  CB  . TYR B  1 83  ? -36.107 39.434 19.292 1.00 38.43 ? 83   TYR B CB  1 
ATOM   6362  C  CG  . TYR B  1 83  ? -37.290 40.131 18.680 1.00 40.26 ? 83   TYR B CG  1 
ATOM   6363  C  CD1 . TYR B  1 83  ? -37.184 40.782 17.453 1.00 42.45 ? 83   TYR B CD1 1 
ATOM   6364  C  CD2 . TYR B  1 83  ? -38.516 40.167 19.342 1.00 42.10 ? 83   TYR B CD2 1 
ATOM   6365  C  CE1 . TYR B  1 83  ? -38.276 41.456 16.897 1.00 44.10 ? 83   TYR B CE1 1 
ATOM   6366  C  CE2 . TYR B  1 83  ? -39.612 40.838 18.802 1.00 44.48 ? 83   TYR B CE2 1 
ATOM   6367  C  CZ  . TYR B  1 83  ? -39.483 41.481 17.576 1.00 44.98 ? 83   TYR B CZ  1 
ATOM   6368  O  OH  . TYR B  1 83  ? -40.568 42.151 17.042 1.00 48.08 ? 83   TYR B OH  1 
ATOM   6369  N  N   . GLY B  1 84  ? -33.251 39.844 21.130 1.00 36.67 ? 84   GLY B N   1 
ATOM   6370  C  CA  . GLY B  1 84  ? -32.123 39.141 21.716 1.00 36.09 ? 84   GLY B CA  1 
ATOM   6371  C  C   . GLY B  1 84  ? -31.496 38.100 20.811 1.00 36.44 ? 84   GLY B C   1 
ATOM   6372  O  O   . GLY B  1 84  ? -30.478 37.515 21.154 1.00 36.03 ? 84   GLY B O   1 
ATOM   6373  N  N   . ASN B  1 85  ? -32.100 37.858 19.655 1.00 37.65 ? 85   ASN B N   1 
ATOM   6374  C  CA  . ASN B  1 85  ? -31.550 36.873 18.729 1.00 39.56 ? 85   ASN B CA  1 
ATOM   6375  C  C   . ASN B  1 85  ? -30.347 37.460 17.980 1.00 39.73 ? 85   ASN B C   1 
ATOM   6376  O  O   . ASN B  1 85  ? -30.197 38.681 17.859 1.00 39.64 ? 85   ASN B O   1 
ATOM   6377  C  CB  . ASN B  1 85  ? -32.609 36.436 17.723 1.00 40.96 ? 85   ASN B CB  1 
ATOM   6378  C  CG  . ASN B  1 85  ? -33.019 37.552 16.814 1.00 43.39 ? 85   ASN B CG  1 
ATOM   6379  O  OD1 . ASN B  1 85  ? -33.571 38.553 17.258 1.00 44.13 ? 85   ASN B OD1 1 
ATOM   6380  N  ND2 . ASN B  1 85  ? -32.736 37.399 15.529 1.00 46.78 ? 85   ASN B ND2 1 
ATOM   6381  N  N   . SER B  1 86  ? -29.501 36.586 17.456 1.00 39.76 ? 86   SER B N   1 
ATOM   6382  C  CA  . SER B  1 86  ? -28.315 37.042 16.758 1.00 40.51 ? 86   SER B CA  1 
ATOM   6383  C  C   . SER B  1 86  ? -27.891 36.158 15.589 1.00 40.90 ? 86   SER B C   1 
ATOM   6384  O  O   . SER B  1 86  ? -28.534 35.161 15.269 1.00 41.43 ? 86   SER B O   1 
ATOM   6385  C  CB  . SER B  1 86  ? -27.168 37.117 17.755 1.00 39.94 ? 86   SER B CB  1 
ATOM   6386  O  OG  . SER B  1 86  ? -26.962 35.840 18.327 1.00 38.44 ? 86   SER B OG  1 
ATOM   6387  N  N   . SER B  1 87  ? -26.781 36.547 14.968 1.00 41.52 ? 87   SER B N   1 
ATOM   6388  C  CA  . SER B  1 87  ? -26.191 35.825 13.848 1.00 41.75 ? 87   SER B CA  1 
ATOM   6389  C  C   . SER B  1 87  ? -24.695 36.110 13.867 1.00 42.09 ? 87   SER B C   1 
ATOM   6390  O  O   . SER B  1 87  ? -24.235 37.055 14.509 1.00 41.92 ? 87   SER B O   1 
ATOM   6391  C  CB  . SER B  1 87  ? -26.797 36.288 12.517 1.00 41.50 ? 87   SER B CB  1 
ATOM   6392  O  OG  . SER B  1 87  ? -28.179 35.982 12.468 1.00 43.06 ? 87   SER B OG  1 
ATOM   6393  N  N   . VAL B  1 88  ? -23.931 35.278 13.176 1.00 42.46 ? 88   VAL B N   1 
ATOM   6394  C  CA  . VAL B  1 88  ? -22.493 35.456 13.130 1.00 42.93 ? 88   VAL B CA  1 
ATOM   6395  C  C   . VAL B  1 88  ? -22.220 36.561 12.125 1.00 42.97 ? 88   VAL B C   1 
ATOM   6396  O  O   . VAL B  1 88  ? -22.589 36.451 10.961 1.00 43.50 ? 88   VAL B O   1 
ATOM   6397  C  CB  . VAL B  1 88  ? -21.796 34.156 12.683 1.00 43.80 ? 88   VAL B CB  1 
ATOM   6398  C  CG1 . VAL B  1 88  ? -20.285 34.318 12.761 1.00 44.63 ? 88   VAL B CG1 1 
ATOM   6399  C  CG2 . VAL B  1 88  ? -22.249 33.004 13.562 1.00 42.95 ? 88   VAL B CG2 1 
ATOM   6400  N  N   . PHE B  1 89  ? -21.590 37.638 12.582 1.00 42.28 ? 89   PHE B N   1 
ATOM   6401  C  CA  . PHE B  1 89  ? -21.288 38.759 11.703 1.00 41.59 ? 89   PHE B CA  1 
ATOM   6402  C  C   . PHE B  1 89  ? -19.960 38.497 10.992 1.00 41.84 ? 89   PHE B C   1 
ATOM   6403  O  O   . PHE B  1 89  ? -19.841 38.687 9.781  1.00 40.28 ? 89   PHE B O   1 
ATOM   6404  C  CB  . PHE B  1 89  ? -21.221 40.054 12.524 1.00 41.13 ? 89   PHE B CB  1 
ATOM   6405  C  CG  . PHE B  1 89  ? -21.038 41.289 11.693 1.00 40.09 ? 89   PHE B CG  1 
ATOM   6406  C  CD1 . PHE B  1 89  ? -19.776 41.686 11.290 1.00 39.85 ? 89   PHE B CD1 1 
ATOM   6407  C  CD2 . PHE B  1 89  ? -22.133 42.046 11.305 1.00 41.30 ? 89   PHE B CD2 1 
ATOM   6408  C  CE1 . PHE B  1 89  ? -19.596 42.825 10.516 1.00 39.33 ? 89   PHE B CE1 1 
ATOM   6409  C  CE2 . PHE B  1 89  ? -21.970 43.196 10.526 1.00 41.05 ? 89   PHE B CE2 1 
ATOM   6410  C  CZ  . PHE B  1 89  ? -20.693 43.578 10.135 1.00 40.47 ? 89   PHE B CZ  1 
ATOM   6411  N  N   . LEU B  1 90  ? -18.971 38.052 11.758 1.00 42.48 ? 90   LEU B N   1 
ATOM   6412  C  CA  . LEU B  1 90  ? -17.662 37.742 11.219 1.00 44.61 ? 90   LEU B CA  1 
ATOM   6413  C  C   . LEU B  1 90  ? -17.095 36.529 11.929 1.00 46.85 ? 90   LEU B C   1 
ATOM   6414  O  O   . LEU B  1 90  ? -16.772 36.589 13.125 1.00 47.14 ? 90   LEU B O   1 
ATOM   6415  C  CB  . LEU B  1 90  ? -16.711 38.912 11.403 1.00 44.27 ? 90   LEU B CB  1 
ATOM   6416  C  CG  . LEU B  1 90  ? -16.038 39.352 10.108 1.00 44.20 ? 90   LEU B CG  1 
ATOM   6417  C  CD1 . LEU B  1 90  ? -17.104 39.605 9.047  1.00 44.26 ? 90   LEU B CD1 1 
ATOM   6418  C  CD2 . LEU B  1 90  ? -15.224 40.605 10.363 1.00 45.00 ? 90   LEU B CD2 1 
ATOM   6419  N  N   . GLU B  1 91  ? -16.979 35.428 11.191 1.00 49.04 ? 91   GLU B N   1 
ATOM   6420  C  CA  . GLU B  1 91  ? -16.451 34.190 11.751 1.00 50.71 ? 91   GLU B CA  1 
ATOM   6421  C  C   . GLU B  1 91  ? -15.015 34.388 12.231 1.00 51.35 ? 91   GLU B C   1 
ATOM   6422  O  O   . GLU B  1 91  ? -14.188 35.013 11.553 1.00 51.03 ? 91   GLU B O   1 
ATOM   6423  C  CB  . GLU B  1 91  ? -16.510 33.072 10.705 1.00 52.64 ? 91   GLU B CB  1 
ATOM   6424  C  CG  . GLU B  1 91  ? -16.547 31.677 11.314 1.00 55.42 ? 91   GLU B CG  1 
ATOM   6425  C  CD  . GLU B  1 91  ? -17.647 31.542 12.368 1.00 58.33 ? 91   GLU B CD  1 
ATOM   6426  O  OE1 . GLU B  1 91  ? -17.546 32.202 13.443 1.00 58.85 ? 91   GLU B OE1 1 
ATOM   6427  O  OE2 . GLU B  1 91  ? -18.622 30.777 12.128 1.00 58.84 ? 91   GLU B OE2 1 
ATOM   6428  N  N   . ASN B  1 92  ? -14.730 33.858 13.415 1.00 51.54 ? 92   ASN B N   1 
ATOM   6429  C  CA  . ASN B  1 92  ? -13.406 33.967 14.013 1.00 52.50 ? 92   ASN B CA  1 
ATOM   6430  C  C   . ASN B  1 92  ? -12.256 33.524 13.093 1.00 52.80 ? 92   ASN B C   1 
ATOM   6431  O  O   . ASN B  1 92  ? -11.120 33.976 13.257 1.00 53.48 ? 92   ASN B O   1 
ATOM   6432  C  CB  . ASN B  1 92  ? -13.378 33.146 15.303 1.00 53.14 ? 92   ASN B CB  1 
ATOM   6433  C  CG  . ASN B  1 92  ? -13.935 31.751 15.105 1.00 54.22 ? 92   ASN B CG  1 
ATOM   6434  O  OD1 . ASN B  1 92  ? -13.454 31.003 14.260 1.00 53.96 ? 92   ASN B OD1 1 
ATOM   6435  N  ND2 . ASN B  1 92  ? -14.958 31.398 15.878 1.00 56.28 ? 92   ASN B ND2 1 
ATOM   6436  N  N   . SER B  1 93  ? -12.547 32.655 12.125 1.00 52.28 ? 93   SER B N   1 
ATOM   6437  C  CA  . SER B  1 93  ? -11.520 32.149 11.208 1.00 51.98 ? 93   SER B CA  1 
ATOM   6438  C  C   . SER B  1 93  ? -11.351 32.988 9.942  1.00 51.70 ? 93   SER B C   1 
ATOM   6439  O  O   . SER B  1 93  ? -10.521 32.673 9.072  1.00 51.20 ? 93   SER B O   1 
ATOM   6440  C  CB  . SER B  1 93  ? -11.858 30.718 10.793 1.00 52.32 ? 93   SER B CB  1 
ATOM   6441  O  OG  . SER B  1 93  ? -13.059 30.697 10.029 1.00 53.67 ? 93   SER B OG  1 
ATOM   6442  N  N   . THR B  1 94  ? -12.138 34.051 9.831  1.00 50.67 ? 94   THR B N   1 
ATOM   6443  C  CA  . THR B  1 94  ? -12.081 34.901 8.652  1.00 49.96 ? 94   THR B CA  1 
ATOM   6444  C  C   . THR B  1 94  ? -10.669 35.375 8.333  1.00 49.59 ? 94   THR B C   1 
ATOM   6445  O  O   . THR B  1 94  ? -10.304 35.506 7.166  1.00 49.15 ? 94   THR B O   1 
ATOM   6446  C  CB  . THR B  1 94  ? -12.987 36.127 8.817  1.00 49.79 ? 94   THR B CB  1 
ATOM   6447  O  OG1 . THR B  1 94  ? -14.330 35.692 9.081  1.00 49.61 ? 94   THR B OG1 1 
ATOM   6448  C  CG2 . THR B  1 94  ? -12.962 36.983 7.548  1.00 48.85 ? 94   THR B CG2 1 
ATOM   6449  N  N   . PHE B  1 95  ? -9.871  35.610 9.368  1.00 49.46 ? 95   PHE B N   1 
ATOM   6450  C  CA  . PHE B  1 95  ? -8.502  36.095 9.171  1.00 49.86 ? 95   PHE B CA  1 
ATOM   6451  C  C   . PHE B  1 95  ? -7.419  35.200 9.775  1.00 50.32 ? 95   PHE B C   1 
ATOM   6452  O  O   . PHE B  1 95  ? -6.399  35.692 10.261 1.00 50.14 ? 95   PHE B O   1 
ATOM   6453  C  CB  . PHE B  1 95  ? -8.388  37.510 9.744  1.00 48.35 ? 95   PHE B CB  1 
ATOM   6454  C  CG  . PHE B  1 95  ? -9.432  38.447 9.213  1.00 46.47 ? 95   PHE B CG  1 
ATOM   6455  C  CD1 . PHE B  1 95  ? -9.323  38.977 7.930  1.00 45.98 ? 95   PHE B CD1 1 
ATOM   6456  C  CD2 . PHE B  1 95  ? -10.563 38.748 9.968  1.00 46.00 ? 95   PHE B CD2 1 
ATOM   6457  C  CE1 . PHE B  1 95  ? -10.333 39.794 7.398  1.00 45.19 ? 95   PHE B CE1 1 
ATOM   6458  C  CE2 . PHE B  1 95  ? -11.579 39.563 9.447  1.00 45.48 ? 95   PHE B CE2 1 
ATOM   6459  C  CZ  . PHE B  1 95  ? -11.463 40.086 8.157  1.00 44.39 ? 95   PHE B CZ  1 
ATOM   6460  N  N   . ASP B  1 96  ? -7.642  33.889 9.734  1.00 51.36 ? 96   ASP B N   1 
ATOM   6461  C  CA  . ASP B  1 96  ? -6.680  32.927 10.268 1.00 52.01 ? 96   ASP B CA  1 
ATOM   6462  C  C   . ASP B  1 96  ? -5.371  32.947 9.490  1.00 51.93 ? 96   ASP B C   1 
ATOM   6463  O  O   . ASP B  1 96  ? -4.339  32.480 9.981  1.00 52.89 ? 96   ASP B O   1 
ATOM   6464  C  CB  . ASP B  1 96  ? -7.265  31.511 10.223 1.00 52.46 ? 96   ASP B CB  1 
ATOM   6465  C  CG  . ASP B  1 96  ? -8.084  31.192 11.441 1.00 53.11 ? 96   ASP B CG  1 
ATOM   6466  O  OD1 . ASP B  1 96  ? -8.386  32.135 12.207 1.00 53.76 ? 96   ASP B OD1 1 
ATOM   6467  O  OD2 . ASP B  1 96  ? -8.431  30.003 11.635 1.00 54.08 ? 96   ASP B OD2 1 
ATOM   6468  N  N   . GLU B  1 97  ? -5.412  33.488 8.278  1.00 51.27 ? 97   GLU B N   1 
ATOM   6469  C  CA  . GLU B  1 97  ? -4.224  33.539 7.450  1.00 50.69 ? 97   GLU B CA  1 
ATOM   6470  C  C   . GLU B  1 97  ? -3.936  34.959 6.973  1.00 49.62 ? 97   GLU B C   1 
ATOM   6471  O  O   . GLU B  1 97  ? -3.344  35.181 5.908  1.00 48.31 ? 97   GLU B O   1 
ATOM   6472  C  CB  . GLU B  1 97  ? -4.398  32.572 6.280  1.00 52.25 ? 97   GLU B CB  1 
ATOM   6473  C  CG  . GLU B  1 97  ? -4.669  31.144 6.759  1.00 54.25 ? 97   GLU B CG  1 
ATOM   6474  C  CD  . GLU B  1 97  ? -5.570  30.369 5.816  1.00 55.90 ? 97   GLU B CD  1 
ATOM   6475  O  OE1 . GLU B  1 97  ? -6.130  29.329 6.243  1.00 56.36 ? 97   GLU B OE1 1 
ATOM   6476  O  OE2 . GLU B  1 97  ? -5.717  30.798 4.644  1.00 56.97 ? 97   GLU B OE2 1 
ATOM   6477  N  N   . PHE B  1 98  ? -4.362  35.920 7.787  1.00 48.46 ? 98   PHE B N   1 
ATOM   6478  C  CA  . PHE B  1 98  ? -4.143  37.329 7.500  1.00 46.68 ? 98   PHE B CA  1 
ATOM   6479  C  C   . PHE B  1 98  ? -2.639  37.603 7.535  1.00 46.31 ? 98   PHE B C   1 
ATOM   6480  O  O   . PHE B  1 98  ? -2.144  38.511 6.865  1.00 46.19 ? 98   PHE B O   1 
ATOM   6481  C  CB  . PHE B  1 98  ? -4.851  38.190 8.547  1.00 46.50 ? 98   PHE B CB  1 
ATOM   6482  C  CG  . PHE B  1 98  ? -4.699  39.666 8.315  1.00 45.80 ? 98   PHE B CG  1 
ATOM   6483  C  CD1 . PHE B  1 98  ? -5.269  40.270 7.198  1.00 44.71 ? 98   PHE B CD1 1 
ATOM   6484  C  CD2 . PHE B  1 98  ? -3.975  40.449 9.206  1.00 45.54 ? 98   PHE B CD2 1 
ATOM   6485  C  CE1 . PHE B  1 98  ? -5.113  41.632 6.969  1.00 44.16 ? 98   PHE B CE1 1 
ATOM   6486  C  CE2 . PHE B  1 98  ? -3.813  41.818 8.984  1.00 45.47 ? 98   PHE B CE2 1 
ATOM   6487  C  CZ  . PHE B  1 98  ? -4.387  42.405 7.863  1.00 44.67 ? 98   PHE B CZ  1 
ATOM   6488  N  N   . GLY B  1 99  ? -1.914  36.802 8.314  1.00 45.51 ? 99   GLY B N   1 
ATOM   6489  C  CA  . GLY B  1 99  ? -0.477  36.973 8.414  1.00 44.39 ? 99   GLY B CA  1 
ATOM   6490  C  C   . GLY B  1 99  ? -0.085  37.903 9.543  1.00 44.04 ? 99   GLY B C   1 
ATOM   6491  O  O   . GLY B  1 99  ? 1.097   38.199 9.730  1.00 44.61 ? 99   GLY B O   1 
ATOM   6492  N  N   . HIS B  1 100 ? -1.074  38.369 10.298 1.00 42.84 ? 100  HIS B N   1 
ATOM   6493  C  CA  . HIS B  1 100 ? -0.822  39.273 11.423 1.00 42.62 ? 100  HIS B CA  1 
ATOM   6494  C  C   . HIS B  1 100 ? -1.870  39.088 12.510 1.00 41.25 ? 100  HIS B C   1 
ATOM   6495  O  O   . HIS B  1 100 ? -2.956  38.584 12.263 1.00 40.25 ? 100  HIS B O   1 
ATOM   6496  C  CB  . HIS B  1 100 ? -0.866  40.729 10.958 1.00 42.93 ? 100  HIS B CB  1 
ATOM   6497  C  CG  . HIS B  1 100 ? 0.233   41.097 10.011 1.00 43.88 ? 100  HIS B CG  1 
ATOM   6498  N  ND1 . HIS B  1 100 ? 1.501   41.430 10.438 1.00 44.10 ? 100  HIS B ND1 1 
ATOM   6499  C  CD2 . HIS B  1 100 ? 0.245   41.211 8.661  1.00 43.48 ? 100  HIS B CD2 1 
ATOM   6500  C  CE1 . HIS B  1 100 ? 2.248   41.739 9.392  1.00 43.56 ? 100  HIS B CE1 1 
ATOM   6501  N  NE2 . HIS B  1 100 ? 1.509   41.614 8.303  1.00 44.54 ? 100  HIS B NE2 1 
ATOM   6502  N  N   . SER B  1 101 ? -1.549  39.506 13.721 1.00 40.79 ? 101  SER B N   1 
ATOM   6503  C  CA  . SER B  1 101 ? -2.519  39.387 14.787 1.00 41.22 ? 101  SER B CA  1 
ATOM   6504  C  C   . SER B  1 101 ? -3.360  40.672 14.795 1.00 40.82 ? 101  SER B C   1 
ATOM   6505  O  O   . SER B  1 101 ? -2.838  41.765 15.009 1.00 40.71 ? 101  SER B O   1 
ATOM   6506  C  CB  . SER B  1 101 ? -1.806  39.207 16.119 1.00 41.01 ? 101  SER B CB  1 
ATOM   6507  O  OG  . SER B  1 101 ? -2.752  38.866 17.119 1.00 43.45 ? 101  SER B OG  1 
ATOM   6508  N  N   . ILE B  1 102 ? -4.658  40.552 14.544 1.00 40.41 ? 102  ILE B N   1 
ATOM   6509  C  CA  . ILE B  1 102 ? -5.520  41.731 14.522 1.00 39.01 ? 102  ILE B CA  1 
ATOM   6510  C  C   . ILE B  1 102 ? -5.803  42.258 15.931 1.00 38.49 ? 102  ILE B C   1 
ATOM   6511  O  O   . ILE B  1 102 ? -6.411  41.578 16.759 1.00 39.31 ? 102  ILE B O   1 
ATOM   6512  C  CB  . ILE B  1 102 ? -6.835  41.427 13.776 1.00 37.78 ? 102  ILE B CB  1 
ATOM   6513  C  CG1 . ILE B  1 102 ? -6.514  41.135 12.301 1.00 36.98 ? 102  ILE B CG1 1 
ATOM   6514  C  CG2 . ILE B  1 102 ? -7.790  42.621 13.881 1.00 37.13 ? 102  ILE B CG2 1 
ATOM   6515  C  CD1 . ILE B  1 102 ? -7.648  40.539 11.511 1.00 35.89 ? 102  ILE B CD1 1 
ATOM   6516  N  N   . ASN B  1 103 ? -5.344  43.476 16.191 1.00 37.53 ? 103  ASN B N   1 
ATOM   6517  C  CA  . ASN B  1 103 ? -5.512  44.115 17.489 1.00 36.91 ? 103  ASN B CA  1 
ATOM   6518  C  C   . ASN B  1 103 ? -6.913  44.680 17.747 1.00 36.33 ? 103  ASN B C   1 
ATOM   6519  O  O   . ASN B  1 103 ? -7.367  44.722 18.887 1.00 36.63 ? 103  ASN B O   1 
ATOM   6520  C  CB  . ASN B  1 103 ? -4.497  45.248 17.646 1.00 36.93 ? 103  ASN B CB  1 
ATOM   6521  C  CG  . ASN B  1 103 ? -4.663  45.993 18.954 1.00 38.10 ? 103  ASN B CG  1 
ATOM   6522  O  OD1 . ASN B  1 103 ? -4.394  45.445 20.026 1.00 40.34 ? 103  ASN B OD1 1 
ATOM   6523  N  ND2 . ASN B  1 103 ? -5.120  47.236 18.879 1.00 36.52 ? 103  ASN B ND2 1 
ATOM   6524  N  N   . ASP B  1 104 ? -7.591  45.127 16.698 1.00 35.14 ? 104  ASP B N   1 
ATOM   6525  C  CA  . ASP B  1 104 ? -8.916  45.709 16.871 1.00 34.05 ? 104  ASP B CA  1 
ATOM   6526  C  C   . ASP B  1 104 ? -9.539  45.904 15.499 1.00 32.88 ? 104  ASP B C   1 
ATOM   6527  O  O   . ASP B  1 104 ? -8.846  45.838 14.492 1.00 33.35 ? 104  ASP B O   1 
ATOM   6528  C  CB  . ASP B  1 104 ? -8.793  47.062 17.580 1.00 34.48 ? 104  ASP B CB  1 
ATOM   6529  C  CG  . ASP B  1 104 ? -10.072 47.482 18.274 1.00 35.53 ? 104  ASP B CG  1 
ATOM   6530  O  OD1 . ASP B  1 104 ? -11.150 47.018 17.856 1.00 36.40 ? 104  ASP B OD1 1 
ATOM   6531  O  OD2 . ASP B  1 104 ? -9.998  48.288 19.234 1.00 36.39 ? 104  ASP B OD2 1 
ATOM   6532  N  N   . TYR B  1 105 ? -10.842 46.151 15.454 1.00 32.95 ? 105  TYR B N   1 
ATOM   6533  C  CA  . TYR B  1 105 ? -11.536 46.330 14.177 1.00 33.05 ? 105  TYR B CA  1 
ATOM   6534  C  C   . TYR B  1 105 ? -12.508 47.488 14.276 1.00 32.28 ? 105  TYR B C   1 
ATOM   6535  O  O   . TYR B  1 105 ? -12.804 47.966 15.366 1.00 32.45 ? 105  TYR B O   1 
ATOM   6536  C  CB  . TYR B  1 105 ? -12.321 45.067 13.809 1.00 34.32 ? 105  TYR B CB  1 
ATOM   6537  C  CG  . TYR B  1 105 ? -13.458 44.760 14.768 1.00 37.06 ? 105  TYR B CG  1 
ATOM   6538  C  CD1 . TYR B  1 105 ? -13.218 44.127 15.994 1.00 38.22 ? 105  TYR B CD1 1 
ATOM   6539  C  CD2 . TYR B  1 105 ? -14.770 45.137 14.470 1.00 37.58 ? 105  TYR B CD2 1 
ATOM   6540  C  CE1 . TYR B  1 105 ? -14.261 43.883 16.898 1.00 39.35 ? 105  TYR B CE1 1 
ATOM   6541  C  CE2 . TYR B  1 105 ? -15.815 44.898 15.368 1.00 38.44 ? 105  TYR B CE2 1 
ATOM   6542  C  CZ  . TYR B  1 105 ? -15.559 44.275 16.575 1.00 39.24 ? 105  TYR B CZ  1 
ATOM   6543  O  OH  . TYR B  1 105 ? -16.594 44.059 17.465 1.00 39.35 ? 105  TYR B OH  1 
ATOM   6544  N  N   . SER B  1 106 ? -13.007 47.930 13.131 1.00 31.90 ? 106  SER B N   1 
ATOM   6545  C  CA  . SER B  1 106 ? -13.964 49.027 13.084 1.00 31.03 ? 106  SER B CA  1 
ATOM   6546  C  C   . SER B  1 106 ? -14.786 48.944 11.798 1.00 30.52 ? 106  SER B C   1 
ATOM   6547  O  O   . SER B  1 106 ? -14.242 48.967 10.697 1.00 30.19 ? 106  SER B O   1 
ATOM   6548  C  CB  . SER B  1 106 ? -13.235 50.370 13.147 1.00 31.78 ? 106  SER B CB  1 
ATOM   6549  O  OG  . SER B  1 106 ? -14.168 51.428 13.177 1.00 32.90 ? 106  SER B OG  1 
ATOM   6550  N  N   . ILE B  1 107 ? -16.100 48.852 11.940 1.00 31.05 ? 107  ILE B N   1 
ATOM   6551  C  CA  . ILE B  1 107 ? -16.970 48.747 10.782 1.00 30.73 ? 107  ILE B CA  1 
ATOM   6552  C  C   . ILE B  1 107 ? -17.410 50.120 10.364 1.00 29.52 ? 107  ILE B C   1 
ATOM   6553  O  O   . ILE B  1 107 ? -17.744 50.945 11.211 1.00 29.40 ? 107  ILE B O   1 
ATOM   6554  C  CB  . ILE B  1 107 ? -18.229 47.911 11.098 1.00 32.87 ? 107  ILE B CB  1 
ATOM   6555  C  CG1 . ILE B  1 107 ? -17.828 46.465 11.388 1.00 34.29 ? 107  ILE B CG1 1 
ATOM   6556  C  CG2 . ILE B  1 107 ? -19.198 47.940 9.925  1.00 33.46 ? 107  ILE B CG2 1 
ATOM   6557  C  CD1 . ILE B  1 107 ? -17.137 46.303 12.712 1.00 37.18 ? 107  ILE B CD1 1 
ATOM   6558  N  N   . SER B  1 108 ? -17.413 50.377 9.063  1.00 28.02 ? 108  SER B N   1 
ATOM   6559  C  CA  . SER B  1 108 ? -17.846 51.679 8.587  1.00 27.80 ? 108  SER B CA  1 
ATOM   6560  C  C   . SER B  1 108 ? -19.327 51.807 8.954  1.00 28.07 ? 108  SER B C   1 
ATOM   6561  O  O   . SER B  1 108 ? -20.035 50.803 9.096  1.00 28.00 ? 108  SER B O   1 
ATOM   6562  C  CB  . SER B  1 108 ? -17.647 51.781 7.069  1.00 27.68 ? 108  SER B CB  1 
ATOM   6563  O  OG  . SER B  1 108 ? -18.421 50.824 6.378  1.00 25.47 ? 108  SER B OG  1 
ATOM   6564  N  N   . PRO B  1 109 ? -19.810 53.039 9.132  1.00 27.92 ? 109  PRO B N   1 
ATOM   6565  C  CA  . PRO B  1 109 ? -21.217 53.248 9.487  1.00 28.10 ? 109  PRO B CA  1 
ATOM   6566  C  C   . PRO B  1 109 ? -22.233 52.596 8.565  1.00 28.80 ? 109  PRO B C   1 
ATOM   6567  O  O   . PRO B  1 109 ? -23.316 52.210 9.008  1.00 30.37 ? 109  PRO B O   1 
ATOM   6568  C  CB  . PRO B  1 109 ? -21.348 54.764 9.498  1.00 27.92 ? 109  PRO B CB  1 
ATOM   6569  C  CG  . PRO B  1 109 ? -19.962 55.202 9.974  1.00 27.94 ? 109  PRO B CG  1 
ATOM   6570  C  CD  . PRO B  1 109 ? -19.045 54.297 9.193  1.00 26.34 ? 109  PRO B CD  1 
ATOM   6571  N  N   . ASP B  1 110 ? -21.915 52.478 7.283  1.00 28.61 ? 110  ASP B N   1 
ATOM   6572  C  CA  . ASP B  1 110 ? -22.869 51.872 6.354  1.00 28.79 ? 110  ASP B CA  1 
ATOM   6573  C  C   . ASP B  1 110 ? -22.735 50.357 6.269  1.00 28.59 ? 110  ASP B C   1 
ATOM   6574  O  O   . ASP B  1 110 ? -23.393 49.721 5.448  1.00 29.59 ? 110  ASP B O   1 
ATOM   6575  C  CB  . ASP B  1 110 ? -22.721 52.478 4.955  1.00 28.81 ? 110  ASP B CB  1 
ATOM   6576  C  CG  . ASP B  1 110 ? -21.367 52.196 4.331  1.00 30.26 ? 110  ASP B CG  1 
ATOM   6577  O  OD1 . ASP B  1 110 ? -21.094 52.758 3.247  1.00 32.34 ? 110  ASP B OD1 1 
ATOM   6578  O  OD2 . ASP B  1 110 ? -20.576 51.413 4.904  1.00 30.95 ? 110  ASP B OD2 1 
ATOM   6579  N  N   . GLY B  1 111 ? -21.876 49.790 7.111  1.00 28.20 ? 111  GLY B N   1 
ATOM   6580  C  CA  . GLY B  1 111 ? -21.676 48.353 7.121  1.00 28.98 ? 111  GLY B CA  1 
ATOM   6581  C  C   . GLY B  1 111 ? -21.021 47.760 5.880  1.00 29.60 ? 111  GLY B C   1 
ATOM   6582  O  O   . GLY B  1 111 ? -20.910 46.540 5.752  1.00 29.90 ? 111  GLY B O   1 
ATOM   6583  N  N   . GLN B  1 112 ? -20.566 48.596 4.956  1.00 29.29 ? 112  GLN B N   1 
ATOM   6584  C  CA  . GLN B  1 112 ? -19.938 48.057 3.749  1.00 28.67 ? 112  GLN B CA  1 
ATOM   6585  C  C   . GLN B  1 112 ? -18.466 47.646 3.885  1.00 28.14 ? 112  GLN B C   1 
ATOM   6586  O  O   . GLN B  1 112 ? -17.963 46.853 3.088  1.00 28.09 ? 112  GLN B O   1 
ATOM   6587  C  CB  . GLN B  1 112 ? -20.092 49.058 2.607  1.00 29.63 ? 112  GLN B CB  1 
ATOM   6588  C  CG  . GLN B  1 112 ? -21.489 49.070 2.020  1.00 30.69 ? 112  GLN B CG  1 
ATOM   6589  C  CD  . GLN B  1 112 ? -21.715 50.221 1.051  1.00 33.37 ? 112  GLN B CD  1 
ATOM   6590  O  OE1 . GLN B  1 112 ? -20.821 50.591 0.268  1.00 32.87 ? 112  GLN B OE1 1 
ATOM   6591  N  NE2 . GLN B  1 112 ? -22.928 50.789 1.086  1.00 32.53 ? 112  GLN B NE2 1 
ATOM   6592  N  N   . PHE B  1 113 ? -17.780 48.155 4.903  1.00 26.16 ? 113  PHE B N   1 
ATOM   6593  C  CA  . PHE B  1 113 ? -16.371 47.834 5.077  1.00 26.31 ? 113  PHE B CA  1 
ATOM   6594  C  C   . PHE B  1 113 ? -15.968 47.614 6.527  1.00 27.50 ? 113  PHE B C   1 
ATOM   6595  O  O   . PHE B  1 113 ? -16.688 47.996 7.456  1.00 27.38 ? 113  PHE B O   1 
ATOM   6596  C  CB  . PHE B  1 113 ? -15.506 48.965 4.519  1.00 24.09 ? 113  PHE B CB  1 
ATOM   6597  C  CG  . PHE B  1 113 ? -15.642 49.162 3.037  1.00 24.89 ? 113  PHE B CG  1 
ATOM   6598  C  CD1 . PHE B  1 113 ? -14.840 48.442 2.149  1.00 24.26 ? 113  PHE B CD1 1 
ATOM   6599  C  CD2 . PHE B  1 113 ? -16.574 50.060 2.529  1.00 23.61 ? 113  PHE B CD2 1 
ATOM   6600  C  CE1 . PHE B  1 113 ? -14.968 48.615 0.760  1.00 25.82 ? 113  PHE B CE1 1 
ATOM   6601  C  CE2 . PHE B  1 113 ? -16.713 50.240 1.145  1.00 26.20 ? 113  PHE B CE2 1 
ATOM   6602  C  CZ  . PHE B  1 113 ? -15.906 49.516 0.252  1.00 25.10 ? 113  PHE B CZ  1 
ATOM   6603  N  N   . ILE B  1 114 ? -14.816 46.982 6.717  1.00 27.66 ? 114  ILE B N   1 
ATOM   6604  C  CA  . ILE B  1 114 ? -14.307 46.788 8.066  1.00 29.60 ? 114  ILE B CA  1 
ATOM   6605  C  C   . ILE B  1 114 ? -12.833 47.165 8.096  1.00 29.48 ? 114  ILE B C   1 
ATOM   6606  O  O   . ILE B  1 114 ? -12.043 46.735 7.261  1.00 30.32 ? 114  ILE B O   1 
ATOM   6607  C  CB  . ILE B  1 114 ? -14.511 45.341 8.595  1.00 30.42 ? 114  ILE B CB  1 
ATOM   6608  C  CG1 . ILE B  1 114 ? -13.809 45.197 9.950  1.00 30.75 ? 114  ILE B CG1 1 
ATOM   6609  C  CG2 . ILE B  1 114 ? -13.997 44.327 7.599  1.00 30.65 ? 114  ILE B CG2 1 
ATOM   6610  C  CD1 . ILE B  1 114 ? -14.145 43.906 10.686 1.00 33.09 ? 114  ILE B CD1 1 
ATOM   6611  N  N   . LEU B  1 115 ? -12.487 48.011 9.056  1.00 29.16 ? 115  LEU B N   1 
ATOM   6612  C  CA  . LEU B  1 115 ? -11.128 48.486 9.229  1.00 29.50 ? 115  LEU B CA  1 
ATOM   6613  C  C   . LEU B  1 115 ? -10.416 47.505 10.153 1.00 29.72 ? 115  LEU B C   1 
ATOM   6614  O  O   . LEU B  1 115 ? -10.891 47.235 11.255 1.00 30.00 ? 115  LEU B O   1 
ATOM   6615  C  CB  . LEU B  1 115 ? -11.159 49.876 9.865  1.00 28.54 ? 115  LEU B CB  1 
ATOM   6616  C  CG  . LEU B  1 115 ? -9.907  50.724 9.776  1.00 29.31 ? 115  LEU B CG  1 
ATOM   6617  C  CD1 . LEU B  1 115 ? -9.763  51.201 8.337  1.00 31.39 ? 115  LEU B CD1 1 
ATOM   6618  C  CD2 . LEU B  1 115 ? -9.998  51.918 10.720 1.00 28.73 ? 115  LEU B CD2 1 
ATOM   6619  N  N   . LEU B  1 116 ? -9.283  46.976 9.700  1.00 30.05 ? 116  LEU B N   1 
ATOM   6620  C  CA  . LEU B  1 116 ? -8.509  46.017 10.483 1.00 29.25 ? 116  LEU B CA  1 
ATOM   6621  C  C   . LEU B  1 116 ? -7.249  46.691 10.973 1.00 29.12 ? 116  LEU B C   1 
ATOM   6622  O  O   . LEU B  1 116 ? -6.429  47.155 10.178 1.00 29.86 ? 116  LEU B O   1 
ATOM   6623  C  CB  . LEU B  1 116 ? -8.138  44.800 9.629  1.00 30.67 ? 116  LEU B CB  1 
ATOM   6624  C  CG  . LEU B  1 116 ? -9.291  43.964 9.066  1.00 30.88 ? 116  LEU B CG  1 
ATOM   6625  C  CD1 . LEU B  1 116 ? -8.701  42.736 8.400  1.00 34.04 ? 116  LEU B CD1 1 
ATOM   6626  C  CD2 . LEU B  1 116 ? -10.252 43.551 10.172 1.00 31.77 ? 116  LEU B CD2 1 
ATOM   6627  N  N   . GLU B  1 117 ? -7.094  46.735 12.288 1.00 27.79 ? 117  GLU B N   1 
ATOM   6628  C  CA  . GLU B  1 117 ? -5.945  47.384 12.903 1.00 27.17 ? 117  GLU B CA  1 
ATOM   6629  C  C   . GLU B  1 117 ? -4.940  46.377 13.460 1.00 26.75 ? 117  GLU B C   1 
ATOM   6630  O  O   . GLU B  1 117 ? -5.312  45.492 14.222 1.00 26.53 ? 117  GLU B O   1 
ATOM   6631  C  CB  . GLU B  1 117 ? -6.464  48.310 14.019 1.00 27.25 ? 117  GLU B CB  1 
ATOM   6632  C  CG  . GLU B  1 117 ? -5.427  49.000 14.872 1.00 27.21 ? 117  GLU B CG  1 
ATOM   6633  C  CD  . GLU B  1 117 ? -6.057  49.835 15.969 1.00 30.03 ? 117  GLU B CD  1 
ATOM   6634  O  OE1 . GLU B  1 117 ? -6.579  50.930 15.654 1.00 31.10 ? 117  GLU B OE1 1 
ATOM   6635  O  OE2 . GLU B  1 117 ? -6.056  49.395 17.145 1.00 29.61 ? 117  GLU B OE2 1 
ATOM   6636  N  N   . TYR B  1 118 ? -3.670  46.507 13.080 1.00 26.73 ? 118  TYR B N   1 
ATOM   6637  C  CA  . TYR B  1 118 ? -2.638  45.603 13.588 1.00 26.80 ? 118  TYR B CA  1 
ATOM   6638  C  C   . TYR B  1 118 ? -1.295  46.319 13.767 1.00 28.48 ? 118  TYR B C   1 
ATOM   6639  O  O   . TYR B  1 118 ? -1.181  47.505 13.466 1.00 29.55 ? 118  TYR B O   1 
ATOM   6640  C  CB  . TYR B  1 118 ? -2.488  44.375 12.670 1.00 26.56 ? 118  TYR B CB  1 
ATOM   6641  C  CG  . TYR B  1 118 ? -2.099  44.662 11.236 1.00 25.97 ? 118  TYR B CG  1 
ATOM   6642  C  CD1 . TYR B  1 118 ? -3.011  45.203 10.336 1.00 25.61 ? 118  TYR B CD1 1 
ATOM   6643  C  CD2 . TYR B  1 118 ? -0.801  44.387 10.776 1.00 26.08 ? 118  TYR B CD2 1 
ATOM   6644  C  CE1 . TYR B  1 118 ? -2.647  45.465 9.007  1.00 25.57 ? 118  TYR B CE1 1 
ATOM   6645  C  CE2 . TYR B  1 118 ? -0.431  44.642 9.452  1.00 25.77 ? 118  TYR B CE2 1 
ATOM   6646  C  CZ  . TYR B  1 118 ? -1.367  45.182 8.571  1.00 26.08 ? 118  TYR B CZ  1 
ATOM   6647  O  OH  . TYR B  1 118 ? -1.019  45.418 7.255  1.00 27.18 ? 118  TYR B OH  1 
ATOM   6648  N  N   . ASN B  1 119 ? -0.273  45.611 14.246 1.00 29.19 ? 119  ASN B N   1 
ATOM   6649  C  CA  . ASN B  1 119 ? 1.030   46.239 14.483 1.00 29.95 ? 119  ASN B CA  1 
ATOM   6650  C  C   . ASN B  1 119 ? 0.850   47.396 15.461 1.00 29.83 ? 119  ASN B C   1 
ATOM   6651  O  O   . ASN B  1 119 ? 1.461   48.459 15.309 1.00 28.02 ? 119  ASN B O   1 
ATOM   6652  C  CB  . ASN B  1 119 ? 1.646   46.799 13.191 1.00 32.47 ? 119  ASN B CB  1 
ATOM   6653  C  CG  . ASN B  1 119 ? 2.257   45.715 12.298 1.00 34.35 ? 119  ASN B CG  1 
ATOM   6654  O  OD1 . ASN B  1 119 ? 2.806   44.723 12.782 1.00 35.18 ? 119  ASN B OD1 1 
ATOM   6655  N  ND2 . ASN B  1 119 ? 2.185   45.924 10.991 1.00 32.77 ? 119  ASN B ND2 1 
ATOM   6656  N  N   . TYR B  1 120 ? -0.005  47.187 16.455 1.00 29.45 ? 120  TYR B N   1 
ATOM   6657  C  CA  . TYR B  1 120 ? -0.272  48.196 17.464 1.00 29.58 ? 120  TYR B CA  1 
ATOM   6658  C  C   . TYR B  1 120 ? 0.975   48.591 18.247 1.00 28.53 ? 120  TYR B C   1 
ATOM   6659  O  O   . TYR B  1 120 ? 1.617   47.750 18.843 1.00 29.11 ? 120  TYR B O   1 
ATOM   6660  C  CB  . TYR B  1 120 ? -1.314  47.673 18.440 1.00 28.87 ? 120  TYR B CB  1 
ATOM   6661  C  CG  . TYR B  1 120 ? -1.514  48.558 19.643 1.00 30.79 ? 120  TYR B CG  1 
ATOM   6662  C  CD1 . TYR B  1 120 ? -2.394  49.644 19.600 1.00 31.43 ? 120  TYR B CD1 1 
ATOM   6663  C  CD2 . TYR B  1 120 ? -0.861  48.284 20.848 1.00 31.99 ? 120  TYR B CD2 1 
ATOM   6664  C  CE1 . TYR B  1 120 ? -2.633  50.429 20.739 1.00 32.38 ? 120  TYR B CE1 1 
ATOM   6665  C  CE2 . TYR B  1 120 ? -1.086  49.067 21.991 1.00 32.97 ? 120  TYR B CE2 1 
ATOM   6666  C  CZ  . TYR B  1 120 ? -1.979  50.135 21.927 1.00 33.51 ? 120  TYR B CZ  1 
ATOM   6667  O  OH  . TYR B  1 120 ? -2.225  50.896 23.055 1.00 36.90 ? 120  TYR B OH  1 
ATOM   6668  N  N   . VAL B  1 121 ? 1.310   49.871 18.250 1.00 28.49 ? 121  VAL B N   1 
ATOM   6669  C  CA  . VAL B  1 121 ? 2.466   50.341 19.003 1.00 28.18 ? 121  VAL B CA  1 
ATOM   6670  C  C   . VAL B  1 121 ? 2.017   51.492 19.910 1.00 28.08 ? 121  VAL B C   1 
ATOM   6671  O  O   . VAL B  1 121 ? 1.797   52.617 19.454 1.00 27.57 ? 121  VAL B O   1 
ATOM   6672  C  CB  . VAL B  1 121 ? 3.598   50.821 18.059 1.00 29.37 ? 121  VAL B CB  1 
ATOM   6673  C  CG1 . VAL B  1 121 ? 4.806   51.333 18.894 1.00 29.65 ? 121  VAL B CG1 1 
ATOM   6674  C  CG2 . VAL B  1 121 ? 4.044   49.663 17.140 1.00 29.82 ? 121  VAL B CG2 1 
ATOM   6675  N  N   . LYS B  1 122 ? 1.868   51.196 21.194 1.00 27.01 ? 122  LYS B N   1 
ATOM   6676  C  CA  . LYS B  1 122 ? 1.425   52.188 22.168 1.00 27.33 ? 122  LYS B CA  1 
ATOM   6677  C  C   . LYS B  1 122 ? 2.339   53.406 22.334 1.00 26.95 ? 122  LYS B C   1 
ATOM   6678  O  O   . LYS B  1 122 ? 3.555   53.289 22.252 1.00 27.41 ? 122  LYS B O   1 
ATOM   6679  C  CB  . LYS B  1 122 ? 1.277   51.538 23.545 1.00 26.86 ? 122  LYS B CB  1 
ATOM   6680  C  CG  . LYS B  1 122 ? 1.047   52.569 24.651 1.00 27.14 ? 122  LYS B CG  1 
ATOM   6681  C  CD  . LYS B  1 122 ? 0.871   51.938 26.025 1.00 26.87 ? 122  LYS B CD  1 
ATOM   6682  C  CE  . LYS B  1 122 ? 0.375   52.965 27.045 1.00 26.79 ? 122  LYS B CE  1 
ATOM   6683  N  NZ  . LYS B  1 122 ? 1.321   54.109 27.207 1.00 27.03 ? 122  LYS B NZ  1 
ATOM   6684  N  N   . GLN B  1 123 ? 1.751   54.579 22.560 1.00 26.28 ? 123  GLN B N   1 
ATOM   6685  C  CA  . GLN B  1 123 ? 2.555   55.774 22.813 1.00 25.14 ? 123  GLN B CA  1 
ATOM   6686  C  C   . GLN B  1 123 ? 2.215   56.312 24.212 1.00 23.81 ? 123  GLN B C   1 
ATOM   6687  O  O   . GLN B  1 123 ? 2.719   55.780 25.204 1.00 23.99 ? 123  GLN B O   1 
ATOM   6688  C  CB  . GLN B  1 123 ? 2.368   56.870 21.749 1.00 26.06 ? 123  GLN B CB  1 
ATOM   6689  C  CG  . GLN B  1 123 ? 3.206   58.094 22.107 1.00 26.77 ? 123  GLN B CG  1 
ATOM   6690  C  CD  . GLN B  1 123 ? 3.289   59.163 21.028 1.00 28.64 ? 123  GLN B CD  1 
ATOM   6691  O  OE1 . GLN B  1 123 ? 4.360   59.412 20.466 1.00 28.24 ? 123  GLN B OE1 1 
ATOM   6692  N  NE2 . GLN B  1 123 ? 2.170   59.822 20.757 1.00 27.31 ? 123  GLN B NE2 1 
ATOM   6693  N  N   . TRP B  1 124 ? 1.374   57.338 24.325 1.00 21.12 ? 124  TRP B N   1 
ATOM   6694  C  CA  . TRP B  1 124 ? 1.055   57.837 25.667 1.00 19.78 ? 124  TRP B CA  1 
ATOM   6695  C  C   . TRP B  1 124 ? -0.246  57.191 26.180 1.00 19.33 ? 124  TRP B C   1 
ATOM   6696  O  O   . TRP B  1 124 ? -0.526  56.028 25.865 1.00 17.92 ? 124  TRP B O   1 
ATOM   6697  C  CB  . TRP B  1 124 ? 0.961   59.374 25.673 1.00 18.56 ? 124  TRP B CB  1 
ATOM   6698  C  CG  . TRP B  1 124 ? 2.112   60.063 24.959 1.00 18.06 ? 124  TRP B CG  1 
ATOM   6699  C  CD1 . TRP B  1 124 ? 2.018   61.057 24.022 1.00 17.19 ? 124  TRP B CD1 1 
ATOM   6700  C  CD2 . TRP B  1 124 ? 3.514   59.775 25.093 1.00 18.71 ? 124  TRP B CD2 1 
ATOM   6701  N  NE1 . TRP B  1 124 ? 3.271   61.399 23.555 1.00 16.85 ? 124  TRP B NE1 1 
ATOM   6702  C  CE2 . TRP B  1 124 ? 4.206   60.629 24.193 1.00 18.36 ? 124  TRP B CE2 1 
ATOM   6703  C  CE3 . TRP B  1 124 ? 4.251   58.879 25.881 1.00 18.12 ? 124  TRP B CE3 1 
ATOM   6704  C  CZ2 . TRP B  1 124 ? 5.600   60.609 24.057 1.00 17.83 ? 124  TRP B CZ2 1 
ATOM   6705  C  CZ3 . TRP B  1 124 ? 5.645   58.858 25.747 1.00 17.89 ? 124  TRP B CZ3 1 
ATOM   6706  C  CH2 . TRP B  1 124 ? 6.302   59.720 24.837 1.00 18.83 ? 124  TRP B CH2 1 
ATOM   6707  N  N   . ARG B  1 125 ? -1.038  57.932 26.956 1.00 18.87 ? 125  ARG B N   1 
ATOM   6708  C  CA  . ARG B  1 125 ? -2.261  57.377 27.509 1.00 18.27 ? 125  ARG B CA  1 
ATOM   6709  C  C   . ARG B  1 125 ? -3.274  56.969 26.440 1.00 18.73 ? 125  ARG B C   1 
ATOM   6710  O  O   . ARG B  1 125 ? -3.930  55.930 26.567 1.00 18.89 ? 125  ARG B O   1 
ATOM   6711  C  CB  . ARG B  1 125 ? -2.917  58.353 28.497 1.00 16.43 ? 125  ARG B CB  1 
ATOM   6712  C  CG  . ARG B  1 125 ? -4.067  57.719 29.305 1.00 16.20 ? 125  ARG B CG  1 
ATOM   6713  C  CD  . ARG B  1 125 ? -4.805  58.742 30.180 1.00 16.29 ? 125  ARG B CD  1 
ATOM   6714  N  NE  . ARG B  1 125 ? -3.941  59.405 31.160 1.00 17.93 ? 125  ARG B NE  1 
ATOM   6715  C  CZ  . ARG B  1 125 ? -3.749  58.985 32.407 1.00 20.48 ? 125  ARG B CZ  1 
ATOM   6716  N  NH1 . ARG B  1 125 ? -4.362  57.887 32.851 1.00 21.66 ? 125  ARG B NH1 1 
ATOM   6717  N  NH2 . ARG B  1 125 ? -2.955  59.667 33.218 1.00 19.80 ? 125  ARG B NH2 1 
ATOM   6718  N  N   . HIS B  1 126 ? -3.400  57.770 25.387 1.00 18.16 ? 126  HIS B N   1 
ATOM   6719  C  CA  . HIS B  1 126 ? -4.359  57.459 24.332 1.00 18.02 ? 126  HIS B CA  1 
ATOM   6720  C  C   . HIS B  1 126 ? -3.733  57.250 22.949 1.00 18.23 ? 126  HIS B C   1 
ATOM   6721  O  O   . HIS B  1 126 ? -4.273  56.522 22.131 1.00 18.61 ? 126  HIS B O   1 
ATOM   6722  C  CB  . HIS B  1 126 ? -5.387  58.585 24.225 1.00 18.21 ? 126  HIS B CB  1 
ATOM   6723  C  CG  . HIS B  1 126 ? -5.980  58.992 25.529 1.00 19.14 ? 126  HIS B CG  1 
ATOM   6724  N  ND1 . HIS B  1 126 ? -6.905  58.222 26.201 1.00 20.43 ? 126  HIS B ND1 1 
ATOM   6725  C  CD2 . HIS B  1 126 ? -5.779  60.091 26.296 1.00 19.60 ? 126  HIS B CD2 1 
ATOM   6726  C  CE1 . HIS B  1 126 ? -7.248  58.828 27.323 1.00 19.20 ? 126  HIS B CE1 1 
ATOM   6727  N  NE2 . HIS B  1 126 ? -6.578  59.967 27.405 1.00 20.58 ? 126  HIS B NE2 1 
ATOM   6728  N  N   . SER B  1 127 ? -2.604  57.896 22.682 1.00 19.06 ? 127  SER B N   1 
ATOM   6729  C  CA  . SER B  1 127 ? -1.982  57.776 21.370 1.00 19.50 ? 127  SER B CA  1 
ATOM   6730  C  C   . SER B  1 127 ? -1.280  56.439 21.139 1.00 20.74 ? 127  SER B C   1 
ATOM   6731  O  O   . SER B  1 127 ? -0.863  55.769 22.089 1.00 20.01 ? 127  SER B O   1 
ATOM   6732  C  CB  . SER B  1 127 ? -0.980  58.926 21.144 1.00 18.97 ? 127  SER B CB  1 
ATOM   6733  O  OG  . SER B  1 127 ? -0.060  59.047 22.228 1.00 15.22 ? 127  SER B OG  1 
ATOM   6734  N  N   . TYR B  1 128 ? -1.177  56.063 19.865 1.00 20.31 ? 128  TYR B N   1 
ATOM   6735  C  CA  . TYR B  1 128 ? -0.499  54.837 19.446 1.00 22.10 ? 128  TYR B CA  1 
ATOM   6736  C  C   . TYR B  1 128 ? -0.384  54.825 17.924 1.00 22.86 ? 128  TYR B C   1 
ATOM   6737  O  O   . TYR B  1 128 ? -1.097  55.561 17.238 1.00 23.04 ? 128  TYR B O   1 
ATOM   6738  C  CB  . TYR B  1 128 ? -1.280  53.606 19.937 1.00 20.53 ? 128  TYR B CB  1 
ATOM   6739  C  CG  . TYR B  1 128 ? -2.635  53.403 19.292 1.00 21.46 ? 128  TYR B CG  1 
ATOM   6740  C  CD1 . TYR B  1 128 ? -2.744  52.835 18.019 1.00 21.74 ? 128  TYR B CD1 1 
ATOM   6741  C  CD2 . TYR B  1 128 ? -3.815  53.747 19.963 1.00 21.10 ? 128  TYR B CD2 1 
ATOM   6742  C  CE1 . TYR B  1 128 ? -3.979  52.609 17.434 1.00 20.81 ? 128  TYR B CE1 1 
ATOM   6743  C  CE2 . TYR B  1 128 ? -5.067  53.528 19.386 1.00 21.92 ? 128  TYR B CE2 1 
ATOM   6744  C  CZ  . TYR B  1 128 ? -5.140  52.949 18.114 1.00 23.20 ? 128  TYR B CZ  1 
ATOM   6745  O  OH  . TYR B  1 128 ? -6.359  52.660 17.543 1.00 21.54 ? 128  TYR B OH  1 
ATOM   6746  N  N   . THR B  1 129 ? 0.532   54.029 17.391 1.00 23.56 ? 129  THR B N   1 
ATOM   6747  C  CA  . THR B  1 129 ? 0.650   53.914 15.935 1.00 25.40 ? 129  THR B CA  1 
ATOM   6748  C  C   . THR B  1 129 ? 0.254   52.483 15.563 1.00 25.90 ? 129  THR B C   1 
ATOM   6749  O  O   . THR B  1 129 ? 0.304   51.572 16.400 1.00 24.05 ? 129  THR B O   1 
ATOM   6750  C  CB  . THR B  1 129 ? 2.093   54.166 15.417 1.00 27.39 ? 129  THR B CB  1 
ATOM   6751  O  OG1 . THR B  1 129 ? 3.031   53.532 16.299 1.00 29.23 ? 129  THR B OG1 1 
ATOM   6752  C  CG2 . THR B  1 129 ? 2.387   55.673 15.312 1.00 25.22 ? 129  THR B CG2 1 
ATOM   6753  N  N   . ALA B  1 130 ? -0.124  52.288 14.304 1.00 25.94 ? 130  ALA B N   1 
ATOM   6754  C  CA  . ALA B  1 130 ? -0.543  50.981 13.859 1.00 27.09 ? 130  ALA B CA  1 
ATOM   6755  C  C   . ALA B  1 130 ? -0.625  50.881 12.348 1.00 28.78 ? 130  ALA B C   1 
ATOM   6756  O  O   . ALA B  1 130 ? -0.518  51.888 11.629 1.00 29.40 ? 130  ALA B O   1 
ATOM   6757  C  CB  . ALA B  1 130 ? -1.903  50.659 14.455 1.00 26.65 ? 130  ALA B CB  1 
ATOM   6758  N  N   . SER B  1 131 ? -0.800  49.646 11.877 1.00 28.73 ? 131  SER B N   1 
ATOM   6759  C  CA  . SER B  1 131 ? -0.974  49.367 10.453 1.00 28.98 ? 131  SER B CA  1 
ATOM   6760  C  C   . SER B  1 131 ? -2.467  49.075 10.302 1.00 28.50 ? 131  SER B C   1 
ATOM   6761  O  O   . SER B  1 131 ? -3.146  48.737 11.276 1.00 27.54 ? 131  SER B O   1 
ATOM   6762  C  CB  . SER B  1 131 ? -0.157  48.145 10.021 1.00 29.09 ? 131  SER B CB  1 
ATOM   6763  O  OG  . SER B  1 131 ? 1.238   48.407 10.035 1.00 30.05 ? 131  SER B OG  1 
ATOM   6764  N  N   . TYR B  1 132 ? -2.971  49.211 9.086  1.00 28.23 ? 132  TYR B N   1 
ATOM   6765  C  CA  . TYR B  1 132 ? -4.378  48.983 8.830  1.00 28.75 ? 132  TYR B CA  1 
ATOM   6766  C  C   . TYR B  1 132 ? -4.635  48.421 7.453  1.00 29.88 ? 132  TYR B C   1 
ATOM   6767  O  O   . TYR B  1 132 ? -3.962  48.769 6.486  1.00 29.34 ? 132  TYR B O   1 
ATOM   6768  C  CB  . TYR B  1 132 ? -5.182  50.288 8.915  1.00 27.96 ? 132  TYR B CB  1 
ATOM   6769  C  CG  . TYR B  1 132 ? -5.125  51.002 10.239 1.00 27.88 ? 132  TYR B CG  1 
ATOM   6770  C  CD1 . TYR B  1 132 ? -4.028  51.800 10.585 1.00 26.80 ? 132  TYR B CD1 1 
ATOM   6771  C  CD2 . TYR B  1 132 ? -6.140  50.833 11.175 1.00 26.89 ? 132  TYR B CD2 1 
ATOM   6772  C  CE1 . TYR B  1 132 ? -3.953  52.394 11.835 1.00 26.58 ? 132  TYR B CE1 1 
ATOM   6773  C  CE2 . TYR B  1 132 ? -6.071  51.424 12.416 1.00 26.61 ? 132  TYR B CE2 1 
ATOM   6774  C  CZ  . TYR B  1 132 ? -4.985  52.193 12.747 1.00 25.61 ? 132  TYR B CZ  1 
ATOM   6775  O  OH  . TYR B  1 132 ? -4.910  52.715 14.018 1.00 26.76 ? 132  TYR B OH  1 
ATOM   6776  N  N   . ASP B  1 133 ? -5.630  47.555 7.369  1.00 30.31 ? 133  ASP B N   1 
ATOM   6777  C  CA  . ASP B  1 133 ? -6.044  47.026 6.092  1.00 32.42 ? 133  ASP B CA  1 
ATOM   6778  C  C   . ASP B  1 133 ? -7.543  47.186 6.110  1.00 31.65 ? 133  ASP B C   1 
ATOM   6779  O  O   . ASP B  1 133 ? -8.150  47.263 7.177  1.00 32.21 ? 133  ASP B O   1 
ATOM   6780  C  CB  . ASP B  1 133 ? -5.650  45.557 5.919  1.00 34.55 ? 133  ASP B CB  1 
ATOM   6781  C  CG  . ASP B  1 133 ? -4.217  45.401 5.457  1.00 36.66 ? 133  ASP B CG  1 
ATOM   6782  O  OD1 . ASP B  1 133 ? -3.777  46.211 4.617  1.00 36.64 ? 133  ASP B OD1 1 
ATOM   6783  O  OD2 . ASP B  1 133 ? -3.530  44.471 5.929  1.00 39.66 ? 133  ASP B OD2 1 
ATOM   6784  N  N   . ILE B  1 134 ? -8.129  47.267 4.929  1.00 31.25 ? 134  ILE B N   1 
ATOM   6785  C  CA  . ILE B  1 134 ? -9.555  47.422 4.800  1.00 31.10 ? 134  ILE B CA  1 
ATOM   6786  C  C   . ILE B  1 134 ? -10.120 46.192 4.099  1.00 32.60 ? 134  ILE B C   1 
ATOM   6787  O  O   . ILE B  1 134 ? -9.606  45.753 3.073  1.00 32.27 ? 134  ILE B O   1 
ATOM   6788  C  CB  . ILE B  1 134 ? -9.900  48.669 3.986  1.00 29.82 ? 134  ILE B CB  1 
ATOM   6789  C  CG1 . ILE B  1 134 ? -9.414  49.915 4.717  1.00 28.56 ? 134  ILE B CG1 1 
ATOM   6790  C  CG2 . ILE B  1 134 ? -11.403 48.744 3.778  1.00 30.30 ? 134  ILE B CG2 1 
ATOM   6791  C  CD1 . ILE B  1 134 ? -9.477  51.163 3.860  1.00 28.48 ? 134  ILE B CD1 1 
ATOM   6792  N  N   . TYR B  1 135 ? -11.188 45.647 4.665  1.00 33.49 ? 135  TYR B N   1 
ATOM   6793  C  CA  . TYR B  1 135 ? -11.835 44.469 4.115  1.00 34.09 ? 135  TYR B CA  1 
ATOM   6794  C  C   . TYR B  1 135 ? -13.198 44.861 3.574  1.00 33.29 ? 135  TYR B C   1 
ATOM   6795  O  O   . TYR B  1 135 ? -14.002 45.474 4.288  1.00 31.98 ? 135  TYR B O   1 
ATOM   6796  C  CB  . TYR B  1 135 ? -12.000 43.421 5.217  1.00 36.03 ? 135  TYR B CB  1 
ATOM   6797  C  CG  . TYR B  1 135 ? -12.506 42.069 4.759  1.00 38.36 ? 135  TYR B CG  1 
ATOM   6798  C  CD1 . TYR B  1 135 ? -11.638 41.117 4.226  1.00 39.41 ? 135  TYR B CD1 1 
ATOM   6799  C  CD2 . TYR B  1 135 ? -13.849 41.721 4.915  1.00 39.93 ? 135  TYR B CD2 1 
ATOM   6800  C  CE1 . TYR B  1 135 ? -12.094 39.838 3.867  1.00 40.92 ? 135  TYR B CE1 1 
ATOM   6801  C  CE2 . TYR B  1 135 ? -14.317 40.454 4.561  1.00 40.92 ? 135  TYR B CE2 1 
ATOM   6802  C  CZ  . TYR B  1 135 ? -13.438 39.519 4.043  1.00 41.73 ? 135  TYR B CZ  1 
ATOM   6803  O  OH  . TYR B  1 135 ? -13.906 38.266 3.726  1.00 43.22 ? 135  TYR B OH  1 
ATOM   6804  N  N   . ASP B  1 136 ? -13.445 44.518 2.312  1.00 33.06 ? 136  ASP B N   1 
ATOM   6805  C  CA  . ASP B  1 136 ? -14.729 44.795 1.659  1.00 34.84 ? 136  ASP B CA  1 
ATOM   6806  C  C   . ASP B  1 136 ? -15.661 43.661 2.100  1.00 35.56 ? 136  ASP B C   1 
ATOM   6807  O  O   . ASP B  1 136 ? -15.482 42.518 1.701  1.00 34.79 ? 136  ASP B O   1 
ATOM   6808  C  CB  . ASP B  1 136 ? -14.543 44.777 0.136  1.00 36.16 ? 136  ASP B CB  1 
ATOM   6809  C  CG  . ASP B  1 136 ? -15.793 45.158 -0.619 1.00 37.46 ? 136  ASP B CG  1 
ATOM   6810  O  OD1 . ASP B  1 136 ? -16.892 44.680 -0.253 1.00 37.74 ? 136  ASP B OD1 1 
ATOM   6811  O  OD2 . ASP B  1 136 ? -15.679 45.938 -1.599 1.00 39.63 ? 136  ASP B OD2 1 
ATOM   6812  N  N   . LEU B  1 137 ? -16.641 43.985 2.937  1.00 37.49 ? 137  LEU B N   1 
ATOM   6813  C  CA  . LEU B  1 137 ? -17.577 43.003 3.460  1.00 39.18 ? 137  LEU B CA  1 
ATOM   6814  C  C   . LEU B  1 137 ? -18.461 42.363 2.407  1.00 41.71 ? 137  LEU B C   1 
ATOM   6815  O  O   . LEU B  1 137 ? -18.839 41.200 2.525  1.00 42.12 ? 137  LEU B O   1 
ATOM   6816  C  CB  . LEU B  1 137 ? -18.446 43.633 4.547  1.00 37.80 ? 137  LEU B CB  1 
ATOM   6817  C  CG  . LEU B  1 137 ? -17.717 43.884 5.880  1.00 38.42 ? 137  LEU B CG  1 
ATOM   6818  C  CD1 . LEU B  1 137 ? -18.515 44.862 6.774  1.00 36.56 ? 137  LEU B CD1 1 
ATOM   6819  C  CD2 . LEU B  1 137 ? -17.497 42.541 6.572  1.00 36.56 ? 137  LEU B CD2 1 
ATOM   6820  N  N   . ASN B  1 138 ? -18.786 43.116 1.366  1.00 44.38 ? 138  ASN B N   1 
ATOM   6821  C  CA  . ASN B  1 138 ? -19.636 42.579 0.315  1.00 46.30 ? 138  ASN B CA  1 
ATOM   6822  C  C   . ASN B  1 138 ? -18.873 41.627 -0.593 1.00 46.75 ? 138  ASN B C   1 
ATOM   6823  O  O   . ASN B  1 138 ? -19.291 40.486 -0.804 1.00 47.96 ? 138  ASN B O   1 
ATOM   6824  C  CB  . ASN B  1 138 ? -20.247 43.722 -0.497 1.00 47.86 ? 138  ASN B CB  1 
ATOM   6825  C  CG  . ASN B  1 138 ? -21.174 44.587 0.341  1.00 50.17 ? 138  ASN B CG  1 
ATOM   6826  O  OD1 . ASN B  1 138 ? -21.857 44.083 1.243  1.00 50.99 ? 138  ASN B OD1 1 
ATOM   6827  N  ND2 . ASN B  1 138 ? -21.218 45.887 0.043  1.00 51.41 ? 138  ASN B ND2 1 
ATOM   6828  N  N   . LYS B  1 139 ? -17.748 42.093 -1.120 1.00 45.75 ? 139  LYS B N   1 
ATOM   6829  C  CA  . LYS B  1 139 ? -16.930 41.281 -2.003 1.00 45.54 ? 139  LYS B CA  1 
ATOM   6830  C  C   . LYS B  1 139 ? -16.170 40.199 -1.228 1.00 45.74 ? 139  LYS B C   1 
ATOM   6831  O  O   . LYS B  1 139 ? -15.721 39.209 -1.810 1.00 45.41 ? 139  LYS B O   1 
ATOM   6832  C  CB  . LYS B  1 139 ? -15.946 42.180 -2.764 1.00 45.58 ? 139  LYS B CB  1 
ATOM   6833  C  CG  . LYS B  1 139 ? -16.624 43.247 -3.624 1.00 45.66 ? 139  LYS B CG  1 
ATOM   6834  C  CD  . LYS B  1 139 ? -15.608 44.086 -4.382 1.00 47.19 ? 139  LYS B CD  1 
ATOM   6835  C  CE  . LYS B  1 139 ? -16.304 45.081 -5.311 1.00 48.91 ? 139  LYS B CE  1 
ATOM   6836  N  NZ  . LYS B  1 139 ? -15.326 46.040 -5.925 1.00 49.87 ? 139  LYS B NZ  1 
ATOM   6837  N  N   . ARG B  1 140 ? -16.039 40.387 0.083  1.00 45.32 ? 140  ARG B N   1 
ATOM   6838  C  CA  . ARG B  1 140 ? -15.323 39.442 0.934  1.00 45.68 ? 140  ARG B CA  1 
ATOM   6839  C  C   . ARG B  1 140 ? -13.850 39.434 0.581  1.00 45.03 ? 140  ARG B C   1 
ATOM   6840  O  O   . ARG B  1 140 ? -13.188 38.400 0.666  1.00 45.05 ? 140  ARG B O   1 
ATOM   6841  C  CB  . ARG B  1 140 ? -15.865 38.019 0.770  1.00 47.40 ? 140  ARG B CB  1 
ATOM   6842  C  CG  . ARG B  1 140 ? -17.354 37.867 0.989  1.00 49.19 ? 140  ARG B CG  1 
ATOM   6843  C  CD  . ARG B  1 140 ? -17.771 38.443 2.314  1.00 50.87 ? 140  ARG B CD  1 
ATOM   6844  N  NE  . ARG B  1 140 ? -19.063 37.899 2.737  1.00 53.15 ? 140  ARG B NE  1 
ATOM   6845  C  CZ  . ARG B  1 140 ? -19.240 36.642 3.135  1.00 53.62 ? 140  ARG B CZ  1 
ATOM   6846  N  NH1 . ARG B  1 140 ? -18.208 35.803 3.162  1.00 53.42 ? 140  ARG B NH1 1 
ATOM   6847  N  NH2 . ARG B  1 140 ? -20.446 36.231 3.513  1.00 54.15 ? 140  ARG B NH2 1 
ATOM   6848  N  N   . GLN B  1 141 ? -13.338 40.584 0.166  1.00 44.42 ? 141  GLN B N   1 
ATOM   6849  C  CA  . GLN B  1 141 ? -11.932 40.678 -0.190 1.00 43.51 ? 141  GLN B CA  1 
ATOM   6850  C  C   . GLN B  1 141 ? -11.256 41.784 0.599  1.00 42.05 ? 141  GLN B C   1 
ATOM   6851  O  O   . GLN B  1 141 ? -11.874 42.776 0.985  1.00 41.31 ? 141  GLN B O   1 
ATOM   6852  C  CB  . GLN B  1 141 ? -11.762 40.992 -1.674 1.00 44.93 ? 141  GLN B CB  1 
ATOM   6853  C  CG  . GLN B  1 141 ? -12.668 40.228 -2.590 1.00 47.87 ? 141  GLN B CG  1 
ATOM   6854  C  CD  . GLN B  1 141 ? -12.356 40.539 -4.030 1.00 50.24 ? 141  GLN B CD  1 
ATOM   6855  O  OE1 . GLN B  1 141 ? -11.247 40.261 -4.503 1.00 50.99 ? 141  GLN B OE1 1 
ATOM   6856  N  NE2 . GLN B  1 141 ? -13.321 41.132 -4.742 1.00 50.67 ? 141  GLN B NE2 1 
ATOM   6857  N  N   . LEU B  1 142 ? -9.963  41.602 0.800  1.00 40.69 ? 142  LEU B N   1 
ATOM   6858  C  CA  . LEU B  1 142 ? -9.146  42.555 1.508  1.00 39.61 ? 142  LEU B CA  1 
ATOM   6859  C  C   . LEU B  1 142 ? -8.633  43.511 0.436  1.00 38.62 ? 142  LEU B C   1 
ATOM   6860  O  O   . LEU B  1 142 ? -8.095  43.071 -0.574 1.00 39.25 ? 142  LEU B O   1 
ATOM   6861  C  CB  . LEU B  1 142 ? -7.986  41.818 2.154  1.00 39.32 ? 142  LEU B CB  1 
ATOM   6862  C  CG  . LEU B  1 142 ? -7.247  42.558 3.256  1.00 40.76 ? 142  LEU B CG  1 
ATOM   6863  C  CD1 . LEU B  1 142 ? -8.114  42.602 4.500  1.00 38.52 ? 142  LEU B CD1 1 
ATOM   6864  C  CD2 . LEU B  1 142 ? -5.941  41.824 3.534  1.00 40.51 ? 142  LEU B CD2 1 
ATOM   6865  N  N   . ILE B  1 143 ? -8.811  44.810 0.633  1.00 36.53 ? 143  ILE B N   1 
ATOM   6866  C  CA  . ILE B  1 143 ? -8.354  45.768 -0.353 1.00 34.93 ? 143  ILE B CA  1 
ATOM   6867  C  C   . ILE B  1 143 ? -6.836  45.805 -0.378 1.00 34.83 ? 143  ILE B C   1 
ATOM   6868  O  O   . ILE B  1 143 ? -6.192  45.881 0.662  1.00 34.64 ? 143  ILE B O   1 
ATOM   6869  C  CB  . ILE B  1 143 ? -8.937  47.146 -0.042 1.00 35.50 ? 143  ILE B CB  1 
ATOM   6870  C  CG1 . ILE B  1 143 ? -10.461 47.058 -0.157 1.00 33.87 ? 143  ILE B CG1 1 
ATOM   6871  C  CG2 . ILE B  1 143 ? -8.363  48.206 -0.993 1.00 35.73 ? 143  ILE B CG2 1 
ATOM   6872  C  CD1 . ILE B  1 143 ? -11.161 48.330 0.114  1.00 35.58 ? 143  ILE B CD1 1 
ATOM   6873  N  N   . THR B  1 144 ? -6.247  45.746 -1.566 1.00 35.24 ? 144  THR B N   1 
ATOM   6874  C  CA  . THR B  1 144 ? -4.791  45.746 -1.643 1.00 35.80 ? 144  THR B CA  1 
ATOM   6875  C  C   . THR B  1 144 ? -4.169  46.941 -2.320 1.00 35.70 ? 144  THR B C   1 
ATOM   6876  O  O   . THR B  1 144 ? -2.947  47.044 -2.382 1.00 37.14 ? 144  THR B O   1 
ATOM   6877  C  CB  . THR B  1 144 ? -4.272  44.485 -2.352 1.00 36.07 ? 144  THR B CB  1 
ATOM   6878  O  OG1 . THR B  1 144 ? -4.784  44.453 -3.689 1.00 37.11 ? 144  THR B OG1 1 
ATOM   6879  C  CG2 . THR B  1 144 ? -4.726  43.244 -1.614 1.00 35.68 ? 144  THR B CG2 1 
ATOM   6880  N  N   . GLU B  1 145 ? -4.989  47.850 -2.822 1.00 35.53 ? 145  GLU B N   1 
ATOM   6881  C  CA  . GLU B  1 145 ? -4.455  49.038 -3.482 1.00 35.83 ? 145  GLU B CA  1 
ATOM   6882  C  C   . GLU B  1 145 ? -4.700  50.324 -2.684 1.00 35.10 ? 145  GLU B C   1 
ATOM   6883  O  O   . GLU B  1 145 ? -5.675  50.423 -1.928 1.00 32.76 ? 145  GLU B O   1 
ATOM   6884  C  CB  . GLU B  1 145 ? -5.088  49.166 -4.857 1.00 38.31 ? 145  GLU B CB  1 
ATOM   6885  C  CG  . GLU B  1 145 ? -6.594  48.993 -4.824 1.00 42.10 ? 145  GLU B CG  1 
ATOM   6886  C  CD  . GLU B  1 145 ? -7.108  48.315 -6.083 1.00 45.33 ? 145  GLU B CD  1 
ATOM   6887  O  OE1 . GLU B  1 145 ? -6.532  47.259 -6.431 1.00 45.33 ? 145  GLU B OE1 1 
ATOM   6888  O  OE2 . GLU B  1 145 ? -8.071  48.829 -6.712 1.00 46.97 ? 145  GLU B OE2 1 
ATOM   6889  N  N   . GLU B  1 146 ? -3.809  51.299 -2.863 1.00 33.51 ? 146  GLU B N   1 
ATOM   6890  C  CA  . GLU B  1 146 ? -3.934  52.577 -2.189 1.00 33.30 ? 146  GLU B CA  1 
ATOM   6891  C  C   . GLU B  1 146 ? -4.189  52.329 -0.715 1.00 33.69 ? 146  GLU B C   1 
ATOM   6892  O  O   . GLU B  1 146 ? -5.118  52.889 -0.125 1.00 33.96 ? 146  GLU B O   1 
ATOM   6893  C  CB  . GLU B  1 146 ? -5.102  53.359 -2.784 1.00 32.73 ? 146  GLU B CB  1 
ATOM   6894  C  CG  . GLU B  1 146 ? -5.025  53.546 -4.290 1.00 32.37 ? 146  GLU B CG  1 
ATOM   6895  C  CD  . GLU B  1 146 ? -3.856  54.413 -4.725 1.00 33.32 ? 146  GLU B CD  1 
ATOM   6896  O  OE1 . GLU B  1 146 ? -3.429  55.272 -3.935 1.00 32.72 ? 146  GLU B OE1 1 
ATOM   6897  O  OE2 . GLU B  1 146 ? -3.370  54.259 -5.867 1.00 37.18 ? 146  GLU B OE2 1 
ATOM   6898  N  N   . ARG B  1 147 ? -3.367  51.477 -0.122 1.00 33.02 ? 147  ARG B N   1 
ATOM   6899  C  CA  . ARG B  1 147 ? -3.517  51.123 1.282  1.00 33.24 ? 147  ARG B CA  1 
ATOM   6900  C  C   . ARG B  1 147 ? -3.085  52.204 2.267  1.00 31.45 ? 147  ARG B C   1 
ATOM   6901  O  O   . ARG B  1 147 ? -2.175  52.987 2.001  1.00 31.57 ? 147  ARG B O   1 
ATOM   6902  C  CB  . ARG B  1 147 ? -2.728  49.847 1.562  1.00 35.03 ? 147  ARG B CB  1 
ATOM   6903  C  CG  . ARG B  1 147 ? -3.248  48.646 0.793  1.00 38.54 ? 147  ARG B CG  1 
ATOM   6904  C  CD  . ARG B  1 147 ? -2.218  47.550 0.809  1.00 42.44 ? 147  ARG B CD  1 
ATOM   6905  N  NE  . ARG B  1 147 ? -1.944  47.121 2.166  1.00 45.41 ? 147  ARG B NE  1 
ATOM   6906  C  CZ  . ARG B  1 147 ? -0.823  46.516 2.543  1.00 48.79 ? 147  ARG B CZ  1 
ATOM   6907  N  NH1 . ARG B  1 147 ? 0.127   46.273 1.646  1.00 48.72 ? 147  ARG B NH1 1 
ATOM   6908  N  NH2 . ARG B  1 147 ? -0.650  46.161 3.820  1.00 49.78 ? 147  ARG B NH2 1 
ATOM   6909  N  N   . ILE B  1 148 ? -3.769  52.245 3.402  1.00 30.36 ? 148  ILE B N   1 
ATOM   6910  C  CA  . ILE B  1 148 ? -3.449  53.175 4.464  1.00 28.01 ? 148  ILE B CA  1 
ATOM   6911  C  C   . ILE B  1 148 ? -1.995  52.861 4.793  1.00 26.53 ? 148  ILE B C   1 
ATOM   6912  O  O   . ILE B  1 148 ? -1.619  51.703 4.911  1.00 26.42 ? 148  ILE B O   1 
ATOM   6913  C  CB  . ILE B  1 148 ? -4.364  52.915 5.668  1.00 27.84 ? 148  ILE B CB  1 
ATOM   6914  C  CG1 . ILE B  1 148 ? -5.758  53.430 5.344  1.00 27.09 ? 148  ILE B CG1 1 
ATOM   6915  C  CG2 . ILE B  1 148 ? -3.814  53.585 6.921  1.00 28.42 ? 148  ILE B CG2 1 
ATOM   6916  C  CD1 . ILE B  1 148 ? -6.843  52.824 6.198  1.00 29.29 ? 148  ILE B CD1 1 
ATOM   6917  N  N   . PRO B  1 149 ? -1.155  53.892 4.920  1.00 25.76 ? 149  PRO B N   1 
ATOM   6918  C  CA  . PRO B  1 149 ? 0.275   53.747 5.222  1.00 26.16 ? 149  PRO B CA  1 
ATOM   6919  C  C   . PRO B  1 149 ? 0.540   53.070 6.565  1.00 26.50 ? 149  PRO B C   1 
ATOM   6920  O  O   . PRO B  1 149 ? -0.330  53.056 7.444  1.00 25.66 ? 149  PRO B O   1 
ATOM   6921  C  CB  . PRO B  1 149 ? 0.793   55.192 5.253  1.00 25.51 ? 149  PRO B CB  1 
ATOM   6922  C  CG  . PRO B  1 149 ? -0.345  56.037 4.704  1.00 25.84 ? 149  PRO B CG  1 
ATOM   6923  C  CD  . PRO B  1 149 ? -1.586  55.296 5.030  1.00 26.10 ? 149  PRO B CD  1 
ATOM   6924  N  N   . ASN B  1 150 ? 1.743   52.521 6.716  1.00 27.38 ? 150  ASN B N   1 
ATOM   6925  C  CA  . ASN B  1 150 ? 2.145   51.910 7.977  1.00 29.45 ? 150  ASN B CA  1 
ATOM   6926  C  C   . ASN B  1 150 ? 2.539   53.105 8.870  1.00 28.60 ? 150  ASN B C   1 
ATOM   6927  O  O   . ASN B  1 150 ? 2.901   54.182 8.368  1.00 27.49 ? 150  ASN B O   1 
ATOM   6928  C  CB  . ASN B  1 150 ? 3.354   50.968 7.780  1.00 33.14 ? 150  ASN B CB  1 
ATOM   6929  C  CG  . ASN B  1 150 ? 2.997   49.680 7.021  1.00 37.93 ? 150  ASN B CG  1 
ATOM   6930  O  OD1 . ASN B  1 150 ? 1.997   49.014 7.334  1.00 37.67 ? 150  ASN B OD1 1 
ATOM   6931  N  ND2 . ASN B  1 150 ? 3.827   49.339 6.029  1.00 42.12 ? 150  ASN B ND2 1 
ATOM   6932  N  N   . ASN B  1 151 ? 2.461   52.921 10.180 1.00 26.54 ? 151  ASN B N   1 
ATOM   6933  C  CA  . ASN B  1 151 ? 2.804   53.990 11.122 1.00 26.71 ? 151  ASN B CA  1 
ATOM   6934  C  C   . ASN B  1 151 ? 1.760   55.101 11.072 1.00 24.33 ? 151  ASN B C   1 
ATOM   6935  O  O   . ASN B  1 151 ? 2.091   56.268 11.225 1.00 23.45 ? 151  ASN B O   1 
ATOM   6936  C  CB  . ASN B  1 151 ? 4.176   54.596 10.791 1.00 28.97 ? 151  ASN B CB  1 
ATOM   6937  C  CG  . ASN B  1 151 ? 5.258   53.552 10.661 1.00 30.04 ? 151  ASN B CG  1 
ATOM   6938  O  OD1 . ASN B  1 151 ? 5.443   52.730 11.545 1.00 32.95 ? 151  ASN B OD1 1 
ATOM   6939  N  ND2 . ASN B  1 151 ? 5.978   53.582 9.549  1.00 31.06 ? 151  ASN B ND2 1 
ATOM   6940  N  N   . THR B  1 152 ? 0.508   54.727 10.833 1.00 23.26 ? 152  THR B N   1 
ATOM   6941  C  CA  . THR B  1 152 ? -0.567  55.697 10.772 1.00 22.79 ? 152  THR B CA  1 
ATOM   6942  C  C   . THR B  1 152 ? -0.891  56.073 12.210 1.00 21.32 ? 152  THR B C   1 
ATOM   6943  O  O   . THR B  1 152 ? -1.059  55.212 13.070 1.00 21.35 ? 152  THR B O   1 
ATOM   6944  C  CB  . THR B  1 152 ? -1.795  55.102 10.037 1.00 22.71 ? 152  THR B CB  1 
ATOM   6945  O  OG1 . THR B  1 152 ? -1.509  55.043 8.637  1.00 23.44 ? 152  THR B OG1 1 
ATOM   6946  C  CG2 . THR B  1 152 ? -3.026  55.948 10.235 1.00 22.07 ? 152  THR B CG2 1 
ATOM   6947  N  N   . GLN B  1 153 ? -0.956  57.370 12.459 1.00 20.91 ? 153  GLN B N   1 
ATOM   6948  C  CA  . GLN B  1 153 ? -1.199  57.894 13.794 1.00 20.79 ? 153  GLN B CA  1 
ATOM   6949  C  C   . GLN B  1 153 ? -2.649  57.876 14.266 1.00 21.03 ? 153  GLN B C   1 
ATOM   6950  O  O   . GLN B  1 153 ? -2.920  57.754 15.462 1.00 21.36 ? 153  GLN B O   1 
ATOM   6951  C  CB  . GLN B  1 153 ? -0.618  59.307 13.872 1.00 19.29 ? 153  GLN B CB  1 
ATOM   6952  C  CG  . GLN B  1 153 ? 0.927   59.326 13.773 1.00 17.11 ? 153  GLN B CG  1 
ATOM   6953  C  CD  . GLN B  1 153 ? 1.491   60.638 13.229 1.00 17.85 ? 153  GLN B CD  1 
ATOM   6954  O  OE1 . GLN B  1 153 ? 1.087   61.122 12.160 1.00 15.95 ? 153  GLN B OE1 1 
ATOM   6955  N  NE2 . GLN B  1 153 ? 2.451   61.204 13.951 1.00 18.00 ? 153  GLN B NE2 1 
ATOM   6956  N  N   . TRP B  1 154 ? -3.583  58.007 13.333 1.00 20.87 ? 154  TRP B N   1 
ATOM   6957  C  CA  . TRP B  1 154 ? -5.002  57.992 13.678 1.00 20.35 ? 154  TRP B CA  1 
ATOM   6958  C  C   . TRP B  1 154 ? -5.818  57.781 12.422 1.00 20.60 ? 154  TRP B C   1 
ATOM   6959  O  O   . TRP B  1 154 ? -5.416  58.215 11.333 1.00 18.66 ? 154  TRP B O   1 
ATOM   6960  C  CB  . TRP B  1 154 ? -5.416  59.303 14.347 1.00 20.43 ? 154  TRP B CB  1 
ATOM   6961  C  CG  . TRP B  1 154 ? -6.851  59.301 14.738 1.00 22.20 ? 154  TRP B CG  1 
ATOM   6962  C  CD1 . TRP B  1 154 ? -7.873  59.960 14.119 1.00 23.11 ? 154  TRP B CD1 1 
ATOM   6963  C  CD2 . TRP B  1 154 ? -7.448  58.530 15.783 1.00 21.39 ? 154  TRP B CD2 1 
ATOM   6964  N  NE1 . TRP B  1 154 ? -9.072  59.636 14.709 1.00 23.32 ? 154  TRP B NE1 1 
ATOM   6965  C  CE2 . TRP B  1 154 ? -8.838  58.761 15.734 1.00 22.38 ? 154  TRP B CE2 1 
ATOM   6966  C  CE3 . TRP B  1 154 ? -6.941  57.663 16.756 1.00 22.92 ? 154  TRP B CE3 1 
ATOM   6967  C  CZ2 . TRP B  1 154 ? -9.740  58.153 16.626 1.00 24.65 ? 154  TRP B CZ2 1 
ATOM   6968  C  CZ3 . TRP B  1 154 ? -7.839  57.050 17.652 1.00 23.55 ? 154  TRP B CZ3 1 
ATOM   6969  C  CH2 . TRP B  1 154 ? -9.223  57.305 17.573 1.00 22.73 ? 154  TRP B CH2 1 
ATOM   6970  N  N   . VAL B  1 155 ? -6.959  57.110 12.576 1.00 20.78 ? 155  VAL B N   1 
ATOM   6971  C  CA  . VAL B  1 155 ? -7.858  56.834 11.455 1.00 21.72 ? 155  VAL B CA  1 
ATOM   6972  C  C   . VAL B  1 155 ? -9.277  56.816 11.988 1.00 23.03 ? 155  VAL B C   1 
ATOM   6973  O  O   . VAL B  1 155 ? -9.528  56.302 13.086 1.00 22.96 ? 155  VAL B O   1 
ATOM   6974  C  CB  . VAL B  1 155 ? -7.653  55.428 10.831 1.00 23.28 ? 155  VAL B CB  1 
ATOM   6975  C  CG1 . VAL B  1 155 ? -8.580  55.255 9.625  1.00 22.15 ? 155  VAL B CG1 1 
ATOM   6976  C  CG2 . VAL B  1 155 ? -6.229  55.221 10.438 1.00 24.58 ? 155  VAL B CG2 1 
ATOM   6977  N  N   . THR B  1 156 ? -10.204 57.350 11.206 1.00 22.23 ? 156  THR B N   1 
ATOM   6978  C  CA  . THR B  1 156 ? -11.599 57.349 11.610 1.00 22.82 ? 156  THR B CA  1 
ATOM   6979  C  C   . THR B  1 156 ? -12.503 57.391 10.397 1.00 22.34 ? 156  THR B C   1 
ATOM   6980  O  O   . THR B  1 156 ? -12.238 58.114 9.436  1.00 22.23 ? 156  THR B O   1 
ATOM   6981  C  CB  . THR B  1 156 ? -11.951 58.557 12.491 1.00 23.73 ? 156  THR B CB  1 
ATOM   6982  O  OG1 . THR B  1 156 ? -13.361 58.550 12.757 1.00 26.66 ? 156  THR B OG1 1 
ATOM   6983  C  CG2 . THR B  1 156 ? -11.604 59.849 11.783 1.00 23.44 ? 156  THR B CG2 1 
ATOM   6984  N  N   . TRP B  1 157 ? -13.567 56.596 10.443 1.00 22.03 ? 157  TRP B N   1 
ATOM   6985  C  CA  . TRP B  1 157 ? -14.539 56.571 9.363  1.00 22.18 ? 157  TRP B CA  1 
ATOM   6986  C  C   . TRP B  1 157 ? -15.313 57.874 9.474  1.00 21.65 ? 157  TRP B C   1 
ATOM   6987  O  O   . TRP B  1 157 ? -15.240 58.546 10.500 1.00 19.66 ? 157  TRP B O   1 
ATOM   6988  C  CB  . TRP B  1 157 ? -15.537 55.413 9.551  1.00 22.95 ? 157  TRP B CB  1 
ATOM   6989  C  CG  . TRP B  1 157 ? -14.995 54.034 9.289  1.00 24.09 ? 157  TRP B CG  1 
ATOM   6990  C  CD1 . TRP B  1 157 ? -14.739 53.052 10.219 1.00 22.96 ? 157  TRP B CD1 1 
ATOM   6991  C  CD2 . TRP B  1 157 ? -14.673 53.470 8.012  1.00 23.45 ? 157  TRP B CD2 1 
ATOM   6992  N  NE1 . TRP B  1 157 ? -14.281 51.913 9.592  1.00 24.41 ? 157  TRP B NE1 1 
ATOM   6993  C  CE2 . TRP B  1 157 ? -14.230 52.143 8.238  1.00 24.04 ? 157  TRP B CE2 1 
ATOM   6994  C  CE3 . TRP B  1 157 ? -14.718 53.953 6.698  1.00 23.66 ? 157  TRP B CE3 1 
ATOM   6995  C  CZ2 . TRP B  1 157 ? -13.835 51.299 7.193  1.00 23.73 ? 157  TRP B CZ2 1 
ATOM   6996  C  CZ3 . TRP B  1 157 ? -14.327 53.111 5.659  1.00 23.42 ? 157  TRP B CZ3 1 
ATOM   6997  C  CH2 . TRP B  1 157 ? -13.892 51.806 5.912  1.00 22.57 ? 157  TRP B CH2 1 
ATOM   6998  N  N   . SER B  1 158 ? -16.031 58.244 8.415  1.00 22.33 ? 158  SER B N   1 
ATOM   6999  C  CA  . SER B  1 158 ? -16.882 59.424 8.481  1.00 21.92 ? 158  SER B CA  1 
ATOM   7000  C  C   . SER B  1 158 ? -18.087 58.897 9.287  1.00 22.69 ? 158  SER B C   1 
ATOM   7001  O  O   . SER B  1 158 ? -18.319 57.690 9.340  1.00 21.45 ? 158  SER B O   1 
ATOM   7002  C  CB  . SER B  1 158 ? -17.320 59.855 7.087  1.00 21.80 ? 158  SER B CB  1 
ATOM   7003  O  OG  . SER B  1 158 ? -17.750 58.736 6.327  1.00 22.02 ? 158  SER B OG  1 
ATOM   7004  N  N   . PRO B  1 159 ? -18.860 59.786 9.922  1.00 21.94 ? 159  PRO B N   1 
ATOM   7005  C  CA  . PRO B  1 159 ? -20.018 59.349 10.713 1.00 23.29 ? 159  PRO B CA  1 
ATOM   7006  C  C   . PRO B  1 159 ? -21.107 58.652 9.899  1.00 24.31 ? 159  PRO B C   1 
ATOM   7007  O  O   . PRO B  1 159 ? -21.899 57.893 10.446 1.00 24.20 ? 159  PRO B O   1 
ATOM   7008  C  CB  . PRO B  1 159 ? -20.493 60.644 11.385 1.00 23.02 ? 159  PRO B CB  1 
ATOM   7009  C  CG  . PRO B  1 159 ? -20.089 61.709 10.390 1.00 24.10 ? 159  PRO B CG  1 
ATOM   7010  C  CD  . PRO B  1 159 ? -18.729 61.250 9.919  1.00 22.90 ? 159  PRO B CD  1 
ATOM   7011  N  N   . VAL B  1 160 ? -21.137 58.910 8.594  1.00 25.19 ? 160  VAL B N   1 
ATOM   7012  C  CA  . VAL B  1 160 ? -22.100 58.279 7.690  1.00 25.49 ? 160  VAL B CA  1 
ATOM   7013  C  C   . VAL B  1 160 ? -21.315 57.802 6.471  1.00 25.01 ? 160  VAL B C   1 
ATOM   7014  O  O   . VAL B  1 160 ? -20.288 58.381 6.131  1.00 24.70 ? 160  VAL B O   1 
ATOM   7015  C  CB  . VAL B  1 160 ? -23.195 59.277 7.219  1.00 26.77 ? 160  VAL B CB  1 
ATOM   7016  C  CG1 . VAL B  1 160 ? -24.104 58.615 6.208  1.00 28.65 ? 160  VAL B CG1 1 
ATOM   7017  C  CG2 . VAL B  1 160 ? -24.020 59.741 8.400  1.00 27.65 ? 160  VAL B CG2 1 
ATOM   7018  N  N   . GLY B  1 161 ? -21.789 56.742 5.824  1.00 25.22 ? 161  GLY B N   1 
ATOM   7019  C  CA  . GLY B  1 161 ? -21.112 56.228 4.641  1.00 24.14 ? 161  GLY B CA  1 
ATOM   7020  C  C   . GLY B  1 161 ? -19.840 55.480 4.964  1.00 24.19 ? 161  GLY B C   1 
ATOM   7021  O  O   . GLY B  1 161 ? -19.802 54.694 5.909  1.00 23.18 ? 161  GLY B O   1 
ATOM   7022  N  N   . HIS B  1 162 ? -18.782 55.742 4.199  1.00 24.05 ? 162  HIS B N   1 
ATOM   7023  C  CA  . HIS B  1 162 ? -17.506 55.058 4.418  1.00 24.78 ? 162  HIS B CA  1 
ATOM   7024  C  C   . HIS B  1 162 ? -16.272 55.850 3.986  1.00 24.34 ? 162  HIS B C   1 
ATOM   7025  O  O   . HIS B  1 162 ? -15.317 55.274 3.468  1.00 23.66 ? 162  HIS B O   1 
ATOM   7026  C  CB  . HIS B  1 162 ? -17.506 53.691 3.709  1.00 25.37 ? 162  HIS B CB  1 
ATOM   7027  C  CG  . HIS B  1 162 ? -17.812 53.772 2.246  1.00 27.16 ? 162  HIS B CG  1 
ATOM   7028  N  ND1 . HIS B  1 162 ? -19.020 53.374 1.709  1.00 28.14 ? 162  HIS B ND1 1 
ATOM   7029  C  CD2 . HIS B  1 162 ? -17.077 54.243 1.209  1.00 27.55 ? 162  HIS B CD2 1 
ATOM   7030  C  CE1 . HIS B  1 162 ? -19.015 53.597 0.407  1.00 29.17 ? 162  HIS B CE1 1 
ATOM   7031  N  NE2 . HIS B  1 162 ? -17.847 54.124 0.079  1.00 29.72 ? 162  HIS B NE2 1 
ATOM   7032  N  N   . LYS B  1 163 ? -16.310 57.169 4.170  1.00 23.86 ? 163  LYS B N   1 
ATOM   7033  C  CA  . LYS B  1 163 ? -15.165 57.999 3.849  1.00 23.07 ? 163  LYS B CA  1 
ATOM   7034  C  C   . LYS B  1 163 ? -14.212 57.713 5.001  1.00 22.60 ? 163  LYS B C   1 
ATOM   7035  O  O   . LYS B  1 163 ? -14.639 57.231 6.054  1.00 21.71 ? 163  LYS B O   1 
ATOM   7036  C  CB  . LYS B  1 163 ? -15.511 59.489 3.870  1.00 23.70 ? 163  LYS B CB  1 
ATOM   7037  C  CG  . LYS B  1 163 ? -16.440 60.000 2.768  1.00 24.74 ? 163  LYS B CG  1 
ATOM   7038  C  CD  . LYS B  1 163 ? -16.692 61.503 3.003  1.00 23.74 ? 163  LYS B CD  1 
ATOM   7039  C  CE  . LYS B  1 163 ? -17.648 62.095 1.987  1.00 25.26 ? 163  LYS B CE  1 
ATOM   7040  N  NZ  . LYS B  1 163 ? -17.788 63.563 2.165  1.00 24.94 ? 163  LYS B NZ  1 
ATOM   7041  N  N   . LEU B  1 164 ? -12.937 58.028 4.808  1.00 22.21 ? 164  LEU B N   1 
ATOM   7042  C  CA  . LEU B  1 164 ? -11.923 57.814 5.823  1.00 22.36 ? 164  LEU B CA  1 
ATOM   7043  C  C   . LEU B  1 164 ? -10.994 59.004 5.888  1.00 21.77 ? 164  LEU B C   1 
ATOM   7044  O  O   . LEU B  1 164 ? -10.659 59.589 4.868  1.00 23.19 ? 164  LEU B O   1 
ATOM   7045  C  CB  . LEU B  1 164 ? -11.074 56.585 5.491  1.00 23.25 ? 164  LEU B CB  1 
ATOM   7046  C  CG  . LEU B  1 164 ? -11.578 55.167 5.753  1.00 24.19 ? 164  LEU B CG  1 
ATOM   7047  C  CD1 . LEU B  1 164 ? -10.703 54.197 4.986  1.00 24.37 ? 164  LEU B CD1 1 
ATOM   7048  C  CD2 . LEU B  1 164 ? -11.551 54.857 7.251  1.00 23.84 ? 164  LEU B CD2 1 
ATOM   7049  N  N   . ALA B  1 165 ? -10.578 59.354 7.094  1.00 20.90 ? 165  ALA B N   1 
ATOM   7050  C  CA  . ALA B  1 165 ? -9.629  60.439 7.287  1.00 20.25 ? 165  ALA B CA  1 
ATOM   7051  C  C   . ALA B  1 165 ? -8.576  59.819 8.180  1.00 20.15 ? 165  ALA B C   1 
ATOM   7052  O  O   . ALA B  1 165 ? -8.908  59.098 9.121  1.00 20.20 ? 165  ALA B O   1 
ATOM   7053  C  CB  . ALA B  1 165 ? -10.281 61.633 7.993  1.00 18.91 ? 165  ALA B CB  1 
ATOM   7054  N  N   . TYR B  1 166 ? -7.308  60.054 7.869  1.00 19.76 ? 166  TYR B N   1 
ATOM   7055  C  CA  . TYR B  1 166 ? -6.250  59.525 8.707  1.00 18.64 ? 166  TYR B CA  1 
ATOM   7056  C  C   . TYR B  1 166 ? -5.108  60.498 8.774  1.00 17.84 ? 166  TYR B C   1 
ATOM   7057  O  O   . TYR B  1 166 ? -4.972  61.363 7.916  1.00 18.57 ? 166  TYR B O   1 
ATOM   7058  C  CB  . TYR B  1 166 ? -5.736  58.170 8.206  1.00 18.15 ? 166  TYR B CB  1 
ATOM   7059  C  CG  . TYR B  1 166 ? -5.166  58.148 6.800  1.00 18.11 ? 166  TYR B CG  1 
ATOM   7060  C  CD1 . TYR B  1 166 ? -5.989  57.923 5.698  1.00 17.85 ? 166  TYR B CD1 1 
ATOM   7061  C  CD2 . TYR B  1 166 ? -3.802  58.318 6.575  1.00 18.05 ? 166  TYR B CD2 1 
ATOM   7062  C  CE1 . TYR B  1 166 ? -5.471  57.867 4.405  1.00 17.71 ? 166  TYR B CE1 1 
ATOM   7063  C  CE2 . TYR B  1 166 ? -3.268  58.265 5.289  1.00 18.97 ? 166  TYR B CE2 1 
ATOM   7064  C  CZ  . TYR B  1 166 ? -4.104  58.041 4.213  1.00 18.72 ? 166  TYR B CZ  1 
ATOM   7065  O  OH  . TYR B  1 166 ? -3.585  58.014 2.946  1.00 20.82 ? 166  TYR B OH  1 
ATOM   7066  N  N   . VAL B  1 167 ? -4.304  60.361 9.822  1.00 17.50 ? 167  VAL B N   1 
ATOM   7067  C  CA  . VAL B  1 167 ? -3.139  61.201 10.029 1.00 16.95 ? 167  VAL B CA  1 
ATOM   7068  C  C   . VAL B  1 167 ? -1.875  60.348 9.915  1.00 17.69 ? 167  VAL B C   1 
ATOM   7069  O  O   . VAL B  1 167 ? -1.755  59.324 10.579 1.00 18.00 ? 167  VAL B O   1 
ATOM   7070  C  CB  . VAL B  1 167 ? -3.188  61.853 11.410 1.00 16.58 ? 167  VAL B CB  1 
ATOM   7071  C  CG1 . VAL B  1 167 ? -1.981  62.754 11.592 1.00 15.62 ? 167  VAL B CG1 1 
ATOM   7072  C  CG2 . VAL B  1 167 ? -4.511  62.630 11.569 1.00 15.17 ? 167  VAL B CG2 1 
ATOM   7073  N  N   . TRP B  1 168 ? -0.940  60.784 9.075  1.00 17.96 ? 168  TRP B N   1 
ATOM   7074  C  CA  . TRP B  1 168 ? 0.311   60.070 8.848  1.00 19.39 ? 168  TRP B CA  1 
ATOM   7075  C  C   . TRP B  1 168 ? 1.422   61.107 8.719  1.00 20.05 ? 168  TRP B C   1 
ATOM   7076  O  O   . TRP B  1 168 ? 1.307   62.068 7.949  1.00 19.67 ? 168  TRP B O   1 
ATOM   7077  C  CB  . TRP B  1 168 ? 0.205   59.229 7.576  1.00 20.54 ? 168  TRP B CB  1 
ATOM   7078  C  CG  . TRP B  1 168 ? 1.450   58.487 7.236  1.00 22.79 ? 168  TRP B CG  1 
ATOM   7079  C  CD1 . TRP B  1 168 ? 1.932   57.363 7.844  1.00 22.58 ? 168  TRP B CD1 1 
ATOM   7080  C  CD2 . TRP B  1 168 ? 2.388   58.823 6.214  1.00 23.93 ? 168  TRP B CD2 1 
ATOM   7081  N  NE1 . TRP B  1 168 ? 3.109   56.979 7.264  1.00 23.28 ? 168  TRP B NE1 1 
ATOM   7082  C  CE2 . TRP B  1 168 ? 3.416   57.856 6.259  1.00 25.18 ? 168  TRP B CE2 1 
ATOM   7083  C  CE3 . TRP B  1 168 ? 2.465   59.851 5.265  1.00 25.33 ? 168  TRP B CE3 1 
ATOM   7084  C  CZ2 . TRP B  1 168 ? 4.520   57.882 5.383  1.00 27.93 ? 168  TRP B CZ2 1 
ATOM   7085  C  CZ3 . TRP B  1 168 ? 3.566   59.882 4.387  1.00 27.64 ? 168  TRP B CZ3 1 
ATOM   7086  C  CH2 . TRP B  1 168 ? 4.577   58.901 4.455  1.00 27.59 ? 168  TRP B CH2 1 
ATOM   7087  N  N   . ASN B  1 169 ? 2.497   60.911 9.477  1.00 19.39 ? 169  ASN B N   1 
ATOM   7088  C  CA  . ASN B  1 169 ? 3.592   61.868 9.504  1.00 20.08 ? 169  ASN B CA  1 
ATOM   7089  C  C   . ASN B  1 169 ? 3.091   63.275 9.853  1.00 19.79 ? 169  ASN B C   1 
ATOM   7090  O  O   . ASN B  1 169 ? 3.561   64.279 9.303  1.00 18.15 ? 169  ASN B O   1 
ATOM   7091  C  CB  . ASN B  1 169 ? 4.333   61.872 8.172  1.00 22.42 ? 169  ASN B CB  1 
ATOM   7092  C  CG  . ASN B  1 169 ? 5.224   60.649 7.997  1.00 26.34 ? 169  ASN B CG  1 
ATOM   7093  O  OD1 . ASN B  1 169 ? 5.788   60.434 6.917  1.00 31.47 ? 169  ASN B OD1 1 
ATOM   7094  N  ND2 . ASN B  1 169 ? 5.358   59.844 9.051  1.00 25.66 ? 169  ASN B ND2 1 
ATOM   7095  N  N   . ASN B  1 170 ? 2.113   63.329 10.761 1.00 19.04 ? 170  ASN B N   1 
ATOM   7096  C  CA  . ASN B  1 170 ? 1.553   64.592 11.240 1.00 18.07 ? 170  ASN B CA  1 
ATOM   7097  C  C   . ASN B  1 170 ? 0.711   65.420 10.246 1.00 18.07 ? 170  ASN B C   1 
ATOM   7098  O  O   . ASN B  1 170 ? 0.458   66.600 10.474 1.00 17.16 ? 170  ASN B O   1 
ATOM   7099  C  CB  . ASN B  1 170 ? 2.694   65.439 11.809 1.00 17.96 ? 170  ASN B CB  1 
ATOM   7100  C  CG  . ASN B  1 170 ? 3.196   64.907 13.144 1.00 17.90 ? 170  ASN B CG  1 
ATOM   7101  O  OD1 . ASN B  1 170 ? 3.438   63.715 13.299 1.00 18.72 ? 170  ASN B OD1 1 
ATOM   7102  N  ND2 . ASN B  1 170 ? 3.345   65.793 14.110 1.00 17.14 ? 170  ASN B ND2 1 
ATOM   7103  N  N   . ASP B  1 171 ? 0.290   64.795 9.146  1.00 18.28 ? 171  ASP B N   1 
ATOM   7104  C  CA  . ASP B  1 171 ? -0.537  65.462 8.145  1.00 17.54 ? 171  ASP B CA  1 
ATOM   7105  C  C   . ASP B  1 171 ? -1.836  64.683 7.965  1.00 17.49 ? 171  ASP B C   1 
ATOM   7106  O  O   . ASP B  1 171 ? -1.885  63.459 8.122  1.00 15.91 ? 171  ASP B O   1 
ATOM   7107  C  CB  . ASP B  1 171 ? 0.184   65.538 6.793  1.00 18.46 ? 171  ASP B CB  1 
ATOM   7108  C  CG  . ASP B  1 171 ? 1.186   66.688 6.713  1.00 19.88 ? 171  ASP B CG  1 
ATOM   7109  O  OD1 . ASP B  1 171 ? 2.316   66.446 6.229  1.00 19.91 ? 171  ASP B OD1 1 
ATOM   7110  O  OD2 . ASP B  1 171 ? 0.838   67.819 7.108  1.00 17.80 ? 171  ASP B OD2 1 
ATOM   7111  N  N   . ILE B  1 172 ? -2.885  65.393 7.585  1.00 17.40 ? 172  ILE B N   1 
ATOM   7112  C  CA  . ILE B  1 172 ? -4.193  64.782 7.393  1.00 18.02 ? 172  ILE B CA  1 
ATOM   7113  C  C   . ILE B  1 172 ? -4.407  64.333 5.955  1.00 18.49 ? 172  ILE B C   1 
ATOM   7114  O  O   . ILE B  1 172 ? -4.017  65.019 5.020  1.00 17.59 ? 172  ILE B O   1 
ATOM   7115  C  CB  . ILE B  1 172 ? -5.286  65.774 7.756  1.00 17.17 ? 172  ILE B CB  1 
ATOM   7116  C  CG1 . ILE B  1 172 ? -5.156  66.150 9.238  1.00 18.90 ? 172  ILE B CG1 1 
ATOM   7117  C  CG2 . ILE B  1 172 ? -6.656  65.179 7.462  1.00 17.28 ? 172  ILE B CG2 1 
ATOM   7118  C  CD1 . ILE B  1 172 ? -5.931  67.416 9.609  1.00 17.10 ? 172  ILE B CD1 1 
ATOM   7119  N  N   . TYR B  1 173 ? -5.040  63.177 5.811  1.00 18.51 ? 173  TYR B N   1 
ATOM   7120  C  CA  . TYR B  1 173 ? -5.372  62.604 4.523  1.00 19.22 ? 173  TYR B CA  1 
ATOM   7121  C  C   . TYR B  1 173 ? -6.830  62.132 4.545  1.00 18.75 ? 173  TYR B C   1 
ATOM   7122  O  O   . TYR B  1 173 ? -7.341  61.709 5.585  1.00 17.31 ? 173  TYR B O   1 
ATOM   7123  C  CB  . TYR B  1 173 ? -4.473  61.408 4.199  1.00 18.81 ? 173  TYR B CB  1 
ATOM   7124  C  CG  . TYR B  1 173 ? -3.017  61.773 3.989  1.00 20.18 ? 173  TYR B CG  1 
ATOM   7125  C  CD1 . TYR B  1 173 ? -2.165  61.966 5.077  1.00 17.02 ? 173  TYR B CD1 1 
ATOM   7126  C  CD2 . TYR B  1 173 ? -2.487  61.920 2.692  1.00 19.08 ? 173  TYR B CD2 1 
ATOM   7127  C  CE1 . TYR B  1 173 ? -0.832  62.294 4.895  1.00 17.92 ? 173  TYR B CE1 1 
ATOM   7128  C  CE2 . TYR B  1 173 ? -1.141  62.254 2.497  1.00 17.56 ? 173  TYR B CE2 1 
ATOM   7129  C  CZ  . TYR B  1 173 ? -0.328  62.442 3.615  1.00 19.00 ? 173  TYR B CZ  1 
ATOM   7130  O  OH  . TYR B  1 173 ? 0.982   62.814 3.476  1.00 19.74 ? 173  TYR B OH  1 
ATOM   7131  N  N   . VAL B  1 174 ? -7.492  62.209 3.396  1.00 19.10 ? 174  VAL B N   1 
ATOM   7132  C  CA  . VAL B  1 174 ? -8.868  61.761 3.282  1.00 18.81 ? 174  VAL B CA  1 
ATOM   7133  C  C   . VAL B  1 174 ? -9.052  60.795 2.110  1.00 20.27 ? 174  VAL B C   1 
ATOM   7134  O  O   . VAL B  1 174 ? -8.521  61.023 1.027  1.00 20.44 ? 174  VAL B O   1 
ATOM   7135  C  CB  . VAL B  1 174 ? -9.800  62.952 3.090  1.00 18.45 ? 174  VAL B CB  1 
ATOM   7136  C  CG1 . VAL B  1 174 ? -11.220 62.476 2.796  1.00 16.93 ? 174  VAL B CG1 1 
ATOM   7137  C  CG2 . VAL B  1 174 ? -9.767  63.818 4.336  1.00 19.22 ? 174  VAL B CG2 1 
ATOM   7138  N  N   . LYS B  1 175 ? -9.781  59.708 2.344  1.00 21.21 ? 175  LYS B N   1 
ATOM   7139  C  CA  . LYS B  1 175 ? -10.085 58.726 1.301  1.00 22.94 ? 175  LYS B CA  1 
ATOM   7140  C  C   . LYS B  1 175 ? -11.593 58.736 1.116  1.00 23.29 ? 175  LYS B C   1 
ATOM   7141  O  O   . LYS B  1 175 ? -12.327 58.456 2.061  1.00 24.46 ? 175  LYS B O   1 
ATOM   7142  C  CB  . LYS B  1 175 ? -9.656  57.317 1.721  1.00 23.66 ? 175  LYS B CB  1 
ATOM   7143  C  CG  . LYS B  1 175 ? -8.206  56.960 1.399  1.00 26.49 ? 175  LYS B CG  1 
ATOM   7144  C  CD  . LYS B  1 175 ? -7.910  55.516 1.794  1.00 28.64 ? 175  LYS B CD  1 
ATOM   7145  C  CE  . LYS B  1 175 ? -7.290  54.750 0.658  1.00 29.55 ? 175  LYS B CE  1 
ATOM   7146  N  NZ  . LYS B  1 175 ? -5.977  55.339 0.259  1.00 32.71 ? 175  LYS B NZ  1 
ATOM   7147  N  N   . ILE B  1 176 ? -12.062 59.073 -0.080 1.00 23.79 ? 176  ILE B N   1 
ATOM   7148  C  CA  . ILE B  1 176 ? -13.494 59.094 -0.338 1.00 22.70 ? 176  ILE B CA  1 
ATOM   7149  C  C   . ILE B  1 176 ? -13.974 57.657 -0.464 1.00 23.87 ? 176  ILE B C   1 
ATOM   7150  O  O   . ILE B  1 176 ? -15.055 57.324 0.016  1.00 24.41 ? 176  ILE B O   1 
ATOM   7151  C  CB  . ILE B  1 176 ? -13.855 59.865 -1.632 1.00 21.25 ? 176  ILE B CB  1 
ATOM   7152  C  CG1 . ILE B  1 176 ? -13.328 61.297 -1.563 1.00 21.20 ? 176  ILE B CG1 1 
ATOM   7153  C  CG2 . ILE B  1 176 ? -15.369 59.921 -1.801 1.00 21.26 ? 176  ILE B CG2 1 
ATOM   7154  C  CD1 . ILE B  1 176 ? -13.992 62.176 -0.497 1.00 21.76 ? 176  ILE B CD1 1 
ATOM   7155  N  N   . GLU B  1 177 ? -13.166 56.820 -1.120 1.00 24.15 ? 177  GLU B N   1 
ATOM   7156  C  CA  . GLU B  1 177 ? -13.466 55.392 -1.290 1.00 25.42 ? 177  GLU B CA  1 
ATOM   7157  C  C   . GLU B  1 177 ? -12.248 54.624 -0.803 1.00 25.58 ? 177  GLU B C   1 
ATOM   7158  O  O   . GLU B  1 177 ? -11.111 55.021 -1.073 1.00 24.41 ? 177  GLU B O   1 
ATOM   7159  C  CB  . GLU B  1 177 ? -13.707 55.008 -2.755 1.00 26.29 ? 177  GLU B CB  1 
ATOM   7160  C  CG  . GLU B  1 177 ? -14.893 55.688 -3.458 1.00 28.05 ? 177  GLU B CG  1 
ATOM   7161  C  CD  . GLU B  1 177 ? -16.245 55.440 -2.792 1.00 28.60 ? 177  GLU B CD  1 
ATOM   7162  O  OE1 . GLU B  1 177 ? -16.468 54.332 -2.273 1.00 28.74 ? 177  GLU B OE1 1 
ATOM   7163  O  OE2 . GLU B  1 177 ? -17.100 56.353 -2.805 1.00 32.29 ? 177  GLU B OE2 1 
ATOM   7164  N  N   . PRO B  1 178 ? -12.472 53.502 -0.094 1.00 25.96 ? 178  PRO B N   1 
ATOM   7165  C  CA  . PRO B  1 178 ? -11.429 52.642 0.460  1.00 25.68 ? 178  PRO B CA  1 
ATOM   7166  C  C   . PRO B  1 178 ? -10.325 52.217 -0.495 1.00 27.30 ? 178  PRO B C   1 
ATOM   7167  O  O   . PRO B  1 178 ? -9.179  52.016 -0.066 1.00 26.75 ? 178  PRO B O   1 
ATOM   7168  C  CB  . PRO B  1 178 ? -12.216 51.448 0.978  1.00 25.81 ? 178  PRO B CB  1 
ATOM   7169  C  CG  . PRO B  1 178 ? -13.498 52.048 1.388  1.00 25.57 ? 178  PRO B CG  1 
ATOM   7170  C  CD  . PRO B  1 178 ? -13.804 52.955 0.221  1.00 24.38 ? 178  PRO B CD  1 
ATOM   7171  N  N   . ASN B  1 179 ? -10.644 52.068 -1.781 1.00 28.19 ? 179  ASN B N   1 
ATOM   7172  C  CA  . ASN B  1 179 ? -9.617  51.624 -2.729 1.00 29.76 ? 179  ASN B CA  1 
ATOM   7173  C  C   . ASN B  1 179 ? -9.039  52.706 -3.626 1.00 29.66 ? 179  ASN B C   1 
ATOM   7174  O  O   . ASN B  1 179 ? -8.168  52.426 -4.439 1.00 31.22 ? 179  ASN B O   1 
ATOM   7175  C  CB  . ASN B  1 179 ? -10.148 50.485 -3.603 1.00 31.36 ? 179  ASN B CB  1 
ATOM   7176  C  CG  . ASN B  1 179 ? -11.124 50.960 -4.649 1.00 33.43 ? 179  ASN B CG  1 
ATOM   7177  O  OD1 . ASN B  1 179 ? -12.140 51.576 -4.332 1.00 35.60 ? 179  ASN B OD1 1 
ATOM   7178  N  ND2 . ASN B  1 179 ? -10.819 50.676 -5.915 1.00 35.41 ? 179  ASN B ND2 1 
ATOM   7179  N  N   . LEU B  1 180 ? -9.506  53.937 -3.476 1.00 28.67 ? 180  LEU B N   1 
ATOM   7180  C  CA  . LEU B  1 180 ? -9.003  55.021 -4.308 1.00 27.88 ? 180  LEU B CA  1 
ATOM   7181  C  C   . LEU B  1 180 ? -7.905  55.840 -3.617 1.00 27.09 ? 180  LEU B C   1 
ATOM   7182  O  O   . LEU B  1 180 ? -7.690  55.716 -2.403 1.00 25.34 ? 180  LEU B O   1 
ATOM   7183  C  CB  . LEU B  1 180 ? -10.153 55.919 -4.727 1.00 27.10 ? 180  LEU B CB  1 
ATOM   7184  C  CG  . LEU B  1 180 ? -11.274 55.153 -5.433 1.00 27.94 ? 180  LEU B CG  1 
ATOM   7185  C  CD1 . LEU B  1 180 ? -12.371 56.117 -5.784 1.00 27.91 ? 180  LEU B CD1 1 
ATOM   7186  C  CD2 . LEU B  1 180 ? -10.748 54.443 -6.681 1.00 26.90 ? 180  LEU B CD2 1 
ATOM   7187  N  N   . PRO B  1 181 ? -7.186  56.682 -4.388 1.00 26.31 ? 181  PRO B N   1 
ATOM   7188  C  CA  . PRO B  1 181 ? -6.113  57.498 -3.801 1.00 24.80 ? 181  PRO B CA  1 
ATOM   7189  C  C   . PRO B  1 181 ? -6.644  58.500 -2.782 1.00 24.63 ? 181  PRO B C   1 
ATOM   7190  O  O   . PRO B  1 181 ? -7.725  59.068 -2.932 1.00 24.25 ? 181  PRO B O   1 
ATOM   7191  C  CB  . PRO B  1 181 ? -5.501  58.203 -5.017 1.00 24.33 ? 181  PRO B CB  1 
ATOM   7192  C  CG  . PRO B  1 181 ? -5.766  57.225 -6.149 1.00 24.63 ? 181  PRO B CG  1 
ATOM   7193  C  CD  . PRO B  1 181 ? -7.198  56.806 -5.858 1.00 25.55 ? 181  PRO B CD  1 
ATOM   7194  N  N   . SER B  1 182 ? -5.876  58.729 -1.737 1.00 23.93 ? 182  SER B N   1 
ATOM   7195  C  CA  . SER B  1 182 ? -6.309  59.688 -0.752 1.00 24.39 ? 182  SER B CA  1 
ATOM   7196  C  C   . SER B  1 182 ? -5.917  61.093 -1.204 1.00 22.46 ? 182  SER B C   1 
ATOM   7197  O  O   . SER B  1 182 ? -5.129  61.258 -2.128 1.00 21.92 ? 182  SER B O   1 
ATOM   7198  C  CB  . SER B  1 182 ? -5.699  59.343 0.604  1.00 25.72 ? 182  SER B CB  1 
ATOM   7199  O  OG  . SER B  1 182 ? -4.341  59.033 0.475  1.00 27.09 ? 182  SER B OG  1 
ATOM   7200  N  N   . TYR B  1 183 ? -6.528  62.095 -0.586 1.00 21.45 ? 183  TYR B N   1 
ATOM   7201  C  CA  . TYR B  1 183 ? -6.244  63.494 -0.873 1.00 20.03 ? 183  TYR B CA  1 
ATOM   7202  C  C   . TYR B  1 183 ? -5.479  64.042 0.336  1.00 20.52 ? 183  TYR B C   1 
ATOM   7203  O  O   . TYR B  1 183 ? -5.929  63.875 1.477  1.00 20.05 ? 183  TYR B O   1 
ATOM   7204  C  CB  . TYR B  1 183 ? -7.546  64.295 -1.027 1.00 17.79 ? 183  TYR B CB  1 
ATOM   7205  C  CG  . TYR B  1 183 ? -8.431  63.848 -2.164 1.00 18.53 ? 183  TYR B CG  1 
ATOM   7206  C  CD1 . TYR B  1 183 ? -8.264  64.363 -3.462 1.00 17.84 ? 183  TYR B CD1 1 
ATOM   7207  C  CD2 . TYR B  1 183 ? -9.399  62.865 -1.962 1.00 16.80 ? 183  TYR B CD2 1 
ATOM   7208  C  CE1 . TYR B  1 183 ? -9.040  63.899 -4.521 1.00 17.68 ? 183  TYR B CE1 1 
ATOM   7209  C  CE2 . TYR B  1 183 ? -10.172 62.393 -3.013 1.00 19.32 ? 183  TYR B CE2 1 
ATOM   7210  C  CZ  . TYR B  1 183 ? -9.984  62.910 -4.289 1.00 19.80 ? 183  TYR B CZ  1 
ATOM   7211  O  OH  . TYR B  1 183 ? -10.708 62.378 -5.328 1.00 24.50 ? 183  TYR B OH  1 
ATOM   7212  N  N   . ARG B  1 184 ? -4.337  64.690 0.104  1.00 19.49 ? 184  ARG B N   1 
ATOM   7213  C  CA  . ARG B  1 184 ? -3.606  65.255 1.217  1.00 20.10 ? 184  ARG B CA  1 
ATOM   7214  C  C   . ARG B  1 184 ? -4.296  66.563 1.559  1.00 20.13 ? 184  ARG B C   1 
ATOM   7215  O  O   . ARG B  1 184 ? -4.648  67.324 0.662  1.00 20.09 ? 184  ARG B O   1 
ATOM   7216  C  CB  . ARG B  1 184 ? -2.129  65.535 0.882  1.00 22.16 ? 184  ARG B CB  1 
ATOM   7217  C  CG  . ARG B  1 184 ? -1.307  65.609 2.176  1.00 25.46 ? 184  ARG B CG  1 
ATOM   7218  C  CD  . ARG B  1 184 ? -0.049  66.472 2.171  1.00 24.91 ? 184  ARG B CD  1 
ATOM   7219  N  NE  . ARG B  1 184 ? 1.134   65.799 1.676  1.00 26.50 ? 184  ARG B NE  1 
ATOM   7220  C  CZ  . ARG B  1 184 ? 2.357   65.879 2.215  1.00 28.03 ? 184  ARG B CZ  1 
ATOM   7221  N  NH1 . ARG B  1 184 ? 2.599   66.592 3.315  1.00 25.50 ? 184  ARG B NH1 1 
ATOM   7222  N  NH2 . ARG B  1 184 ? 3.371   65.285 1.594  1.00 26.99 ? 184  ARG B NH2 1 
ATOM   7223  N  N   . ILE B  1 185 ? -4.487  66.811 2.853  1.00 19.04 ? 185  ILE B N   1 
ATOM   7224  C  CA  . ILE B  1 185 ? -5.142  68.020 3.340  1.00 18.64 ? 185  ILE B CA  1 
ATOM   7225  C  C   . ILE B  1 185 ? -4.165  69.059 3.916  1.00 18.86 ? 185  ILE B C   1 
ATOM   7226  O  O   . ILE B  1 185 ? -4.430  70.243 3.858  1.00 18.72 ? 185  ILE B O   1 
ATOM   7227  C  CB  . ILE B  1 185 ? -6.176  67.685 4.452  1.00 16.94 ? 185  ILE B CB  1 
ATOM   7228  C  CG1 . ILE B  1 185 ? -7.113  66.563 3.995  1.00 15.20 ? 185  ILE B CG1 1 
ATOM   7229  C  CG2 . ILE B  1 185 ? -6.946  68.948 4.846  1.00 14.60 ? 185  ILE B CG2 1 
ATOM   7230  C  CD1 . ILE B  1 185 ? -7.875  66.829 2.691  1.00 15.76 ? 185  ILE B CD1 1 
ATOM   7231  N  N   . THR B  1 186 ? -3.057  68.599 4.491  1.00 19.08 ? 186  THR B N   1 
ATOM   7232  C  CA  . THR B  1 186 ? -2.064  69.489 5.082  1.00 20.01 ? 186  THR B CA  1 
ATOM   7233  C  C   . THR B  1 186 ? -0.652  69.083 4.667  1.00 19.59 ? 186  THR B C   1 
ATOM   7234  O  O   . THR B  1 186 ? -0.370  67.905 4.467  1.00 19.12 ? 186  THR B O   1 
ATOM   7235  C  CB  . THR B  1 186 ? -2.121  69.439 6.623  1.00 20.91 ? 186  THR B CB  1 
ATOM   7236  O  OG1 . THR B  1 186 ? -1.903  68.090 7.048  1.00 17.82 ? 186  THR B OG1 1 
ATOM   7237  C  CG2 . THR B  1 186 ? -3.481  69.918 7.134  1.00 20.30 ? 186  THR B CG2 1 
ATOM   7238  N  N   . TRP B  1 187 ? 0.240   70.066 4.577  1.00 21.17 ? 187  TRP B N   1 
ATOM   7239  C  CA  . TRP B  1 187 ? 1.637   69.829 4.186  1.00 21.58 ? 187  TRP B CA  1 
ATOM   7240  C  C   . TRP B  1 187 ? 2.617   70.359 5.230  1.00 21.28 ? 187  TRP B C   1 
ATOM   7241  O  O   . TRP B  1 187 ? 3.829   70.252 5.051  1.00 21.72 ? 187  TRP B O   1 
ATOM   7242  C  CB  . TRP B  1 187 ? 1.931   70.502 2.842  1.00 21.83 ? 187  TRP B CB  1 
ATOM   7243  C  CG  . TRP B  1 187 ? 1.426   69.754 1.656  1.00 22.14 ? 187  TRP B CG  1 
ATOM   7244  C  CD1 . TRP B  1 187 ? 2.149   68.942 0.825  1.00 22.23 ? 187  TRP B CD1 1 
ATOM   7245  C  CD2 . TRP B  1 187 ? 0.079   69.747 1.155  1.00 21.62 ? 187  TRP B CD2 1 
ATOM   7246  N  NE1 . TRP B  1 187 ? 1.335   68.432 -0.167 1.00 21.03 ? 187  TRP B NE1 1 
ATOM   7247  C  CE2 . TRP B  1 187 ? 0.062   68.911 0.012  1.00 20.64 ? 187  TRP B CE2 1 
ATOM   7248  C  CE3 . TRP B  1 187 ? -1.113  70.362 1.565  1.00 19.98 ? 187  TRP B CE3 1 
ATOM   7249  C  CZ2 . TRP B  1 187 ? -1.097  68.677 -0.722 1.00 19.95 ? 187  TRP B CZ2 1 
ATOM   7250  C  CZ3 . TRP B  1 187 ? -2.264  70.131 0.839  1.00 19.38 ? 187  TRP B CZ3 1 
ATOM   7251  C  CH2 . TRP B  1 187 ? -2.250  69.294 -0.295 1.00 20.18 ? 187  TRP B CH2 1 
ATOM   7252  N  N   . THR B  1 188 ? 2.087   70.909 6.321  1.00 20.03 ? 188  THR B N   1 
ATOM   7253  C  CA  . THR B  1 188 ? 2.912   71.461 7.394  1.00 19.85 ? 188  THR B CA  1 
ATOM   7254  C  C   . THR B  1 188 ? 3.382   70.461 8.454  1.00 20.44 ? 188  THR B C   1 
ATOM   7255  O  O   . THR B  1 188 ? 4.239   70.789 9.274  1.00 20.43 ? 188  THR B O   1 
ATOM   7256  C  CB  . THR B  1 188 ? 2.156   72.578 8.119  1.00 18.77 ? 188  THR B CB  1 
ATOM   7257  O  OG1 . THR B  1 188 ? 0.871   72.082 8.539  1.00 14.87 ? 188  THR B OG1 1 
ATOM   7258  C  CG2 . THR B  1 188 ? 1.991   73.784 7.192  1.00 17.42 ? 188  THR B CG2 1 
ATOM   7259  N  N   . GLY B  1 189 ? 2.808   69.262 8.442  1.00 19.99 ? 189  GLY B N   1 
ATOM   7260  C  CA  . GLY B  1 189 ? 3.177   68.235 9.404  1.00 21.82 ? 189  GLY B CA  1 
ATOM   7261  C  C   . GLY B  1 189 ? 4.669   68.176 9.693  1.00 22.45 ? 189  GLY B C   1 
ATOM   7262  O  O   . GLY B  1 189 ? 5.477   68.202 8.776  1.00 22.09 ? 189  GLY B O   1 
ATOM   7263  N  N   . LYS B  1 190 ? 5.046   68.095 10.965 1.00 22.55 ? 190  LYS B N   1 
ATOM   7264  C  CA  . LYS B  1 190 ? 6.457   68.053 11.309 1.00 23.60 ? 190  LYS B CA  1 
ATOM   7265  C  C   . LYS B  1 190 ? 6.617   67.411 12.687 1.00 23.82 ? 190  LYS B C   1 
ATOM   7266  O  O   . LYS B  1 190 ? 6.187   67.969 13.706 1.00 21.21 ? 190  LYS B O   1 
ATOM   7267  C  CB  . LYS B  1 190 ? 7.012   69.476 11.307 1.00 26.23 ? 190  LYS B CB  1 
ATOM   7268  C  CG  . LYS B  1 190 ? 8.524   69.626 11.064 1.00 30.08 ? 190  LYS B CG  1 
ATOM   7269  C  CD  . LYS B  1 190 ? 8.834   71.125 10.923 1.00 32.84 ? 190  LYS B CD  1 
ATOM   7270  C  CE  . LYS B  1 190 ? 10.181  71.433 10.279 1.00 37.02 ? 190  LYS B CE  1 
ATOM   7271  N  NZ  . LYS B  1 190 ? 11.363  71.122 11.155 1.00 37.28 ? 190  LYS B NZ  1 
ATOM   7272  N  N   . GLU B  1 191 ? 7.230   66.229 12.701 1.00 24.03 ? 191  GLU B N   1 
ATOM   7273  C  CA  . GLU B  1 191 ? 7.461   65.466 13.924 1.00 25.67 ? 191  GLU B CA  1 
ATOM   7274  C  C   . GLU B  1 191 ? 7.876   66.335 15.114 1.00 24.67 ? 191  GLU B C   1 
ATOM   7275  O  O   . GLU B  1 191 ? 8.850   67.066 15.026 1.00 22.73 ? 191  GLU B O   1 
ATOM   7276  C  CB  . GLU B  1 191 ? 8.536   64.403 13.667 1.00 28.18 ? 191  GLU B CB  1 
ATOM   7277  C  CG  . GLU B  1 191 ? 8.838   63.523 14.897 1.00 34.18 ? 191  GLU B CG  1 
ATOM   7278  C  CD  . GLU B  1 191 ? 9.810   62.385 14.593 1.00 37.16 ? 191  GLU B CD  1 
ATOM   7279  O  OE1 . GLU B  1 191 ? 10.968  62.653 14.203 1.00 39.86 ? 191  GLU B OE1 1 
ATOM   7280  O  OE2 . GLU B  1 191 ? 9.413   61.214 14.748 1.00 41.14 ? 191  GLU B OE2 1 
ATOM   7281  N  N   . ASP B  1 192 ? 7.129   66.239 16.217 1.00 24.23 ? 192  ASP B N   1 
ATOM   7282  C  CA  . ASP B  1 192 ? 7.386   67.004 17.445 1.00 23.55 ? 192  ASP B CA  1 
ATOM   7283  C  C   . ASP B  1 192 ? 7.254   68.511 17.280 1.00 23.80 ? 192  ASP B C   1 
ATOM   7284  O  O   . ASP B  1 192 ? 7.542   69.263 18.219 1.00 24.71 ? 192  ASP B O   1 
ATOM   7285  C  CB  . ASP B  1 192 ? 8.794   66.737 18.016 1.00 24.97 ? 192  ASP B CB  1 
ATOM   7286  C  CG  . ASP B  1 192 ? 9.066   65.265 18.279 1.00 27.12 ? 192  ASP B CG  1 
ATOM   7287  O  OD1 . ASP B  1 192 ? 8.163   64.562 18.774 1.00 27.89 ? 192  ASP B OD1 1 
ATOM   7288  O  OD2 . ASP B  1 192 ? 10.205  64.811 18.007 1.00 28.71 ? 192  ASP B OD2 1 
ATOM   7289  N  N   . ILE B  1 193 ? 6.852   68.976 16.105 1.00 22.33 ? 193  ILE B N   1 
ATOM   7290  C  CA  . ILE B  1 193 ? 6.726   70.422 15.898 1.00 21.45 ? 193  ILE B CA  1 
ATOM   7291  C  C   . ILE B  1 193 ? 5.317   70.845 15.476 1.00 21.06 ? 193  ILE B C   1 
ATOM   7292  O  O   . ILE B  1 193 ? 4.654   71.597 16.188 1.00 20.31 ? 193  ILE B O   1 
ATOM   7293  C  CB  . ILE B  1 193 ? 7.719   70.928 14.836 1.00 20.62 ? 193  ILE B CB  1 
ATOM   7294  C  CG1 . ILE B  1 193 ? 9.160   70.640 15.273 1.00 20.92 ? 193  ILE B CG1 1 
ATOM   7295  C  CG2 . ILE B  1 193 ? 7.528   72.425 14.629 1.00 20.94 ? 193  ILE B CG2 1 
ATOM   7296  C  CD1 . ILE B  1 193 ? 9.686   71.606 16.333 1.00 22.14 ? 193  ILE B CD1 1 
ATOM   7297  N  N   . ILE B  1 194 ? 4.872   70.394 14.306 1.00 19.92 ? 194  ILE B N   1 
ATOM   7298  C  CA  . ILE B  1 194 ? 3.535   70.747 13.857 1.00 18.70 ? 194  ILE B CA  1 
ATOM   7299  C  C   . ILE B  1 194 ? 2.674   69.497 13.826 1.00 18.66 ? 194  ILE B C   1 
ATOM   7300  O  O   . ILE B  1 194 ? 3.037   68.503 13.189 1.00 17.67 ? 194  ILE B O   1 
ATOM   7301  C  CB  . ILE B  1 194 ? 3.540   71.378 12.443 1.00 20.38 ? 194  ILE B CB  1 
ATOM   7302  C  CG1 . ILE B  1 194 ? 4.517   72.564 12.384 1.00 18.70 ? 194  ILE B CG1 1 
ATOM   7303  C  CG2 . ILE B  1 194 ? 2.131   71.827 12.074 1.00 17.65 ? 194  ILE B CG2 1 
ATOM   7304  C  CD1 . ILE B  1 194 ? 4.310   73.634 13.466 1.00 20.24 ? 194  ILE B CD1 1 
ATOM   7305  N  N   . TYR B  1 195 ? 1.539   69.556 14.527 1.00 18.25 ? 195  TYR B N   1 
ATOM   7306  C  CA  . TYR B  1 195 ? 0.583   68.452 14.595 1.00 17.89 ? 195  TYR B CA  1 
ATOM   7307  C  C   . TYR B  1 195 ? -0.756  68.827 13.963 1.00 17.96 ? 195  TYR B C   1 
ATOM   7308  O  O   . TYR B  1 195 ? -1.466  69.698 14.483 1.00 18.33 ? 195  TYR B O   1 
ATOM   7309  C  CB  . TYR B  1 195 ? 0.297   68.056 16.045 1.00 18.34 ? 195  TYR B CB  1 
ATOM   7310  C  CG  . TYR B  1 195 ? 1.502   67.715 16.904 1.00 19.78 ? 195  TYR B CG  1 
ATOM   7311  C  CD1 . TYR B  1 195 ? 2.364   68.713 17.361 1.00 20.41 ? 195  TYR B CD1 1 
ATOM   7312  C  CD2 . TYR B  1 195 ? 1.734   66.405 17.317 1.00 20.01 ? 195  TYR B CD2 1 
ATOM   7313  C  CE1 . TYR B  1 195 ? 3.424   68.418 18.216 1.00 22.10 ? 195  TYR B CE1 1 
ATOM   7314  C  CE2 . TYR B  1 195 ? 2.789   66.094 18.173 1.00 22.69 ? 195  TYR B CE2 1 
ATOM   7315  C  CZ  . TYR B  1 195 ? 3.625   67.112 18.619 1.00 22.00 ? 195  TYR B CZ  1 
ATOM   7316  O  OH  . TYR B  1 195 ? 4.634   66.835 19.486 1.00 21.64 ? 195  TYR B OH  1 
ATOM   7317  N  N   . ASN B  1 196 ? -1.116  68.177 12.858 1.00 17.08 ? 196  ASN B N   1 
ATOM   7318  C  CA  . ASN B  1 196 ? -2.397  68.457 12.197 1.00 15.57 ? 196  ASN B CA  1 
ATOM   7319  C  C   . ASN B  1 196 ? -3.327  67.273 12.414 1.00 16.34 ? 196  ASN B C   1 
ATOM   7320  O  O   . ASN B  1 196 ? -3.003  66.133 12.044 1.00 15.80 ? 196  ASN B O   1 
ATOM   7321  C  CB  . ASN B  1 196 ? -2.217  68.653 10.686 1.00 17.34 ? 196  ASN B CB  1 
ATOM   7322  C  CG  . ASN B  1 196 ? -1.370  69.877 10.341 1.00 18.15 ? 196  ASN B CG  1 
ATOM   7323  O  OD1 . ASN B  1 196 ? -1.800  71.022 10.525 1.00 16.50 ? 196  ASN B OD1 1 
ATOM   7324  N  ND2 . ASN B  1 196 ? -0.149  69.631 9.838  1.00 14.23 ? 196  ASN B ND2 1 
ATOM   7325  N  N   . GLY B  1 197 ? -4.472  67.526 13.032 1.00 14.79 ? 197  GLY B N   1 
ATOM   7326  C  CA  . GLY B  1 197 ? -5.413  66.454 13.231 1.00 14.50 ? 197  GLY B CA  1 
ATOM   7327  C  C   . GLY B  1 197 ? -5.105  65.520 14.382 1.00 15.64 ? 197  GLY B C   1 
ATOM   7328  O  O   . GLY B  1 197 ? -5.850  64.568 14.605 1.00 16.80 ? 197  GLY B O   1 
ATOM   7329  N  N   . ILE B  1 198 ? -3.989  65.744 15.069 1.00 14.34 ? 198  ILE B N   1 
ATOM   7330  C  CA  . ILE B  1 198 ? -3.647  64.949 16.234 1.00 13.97 ? 198  ILE B CA  1 
ATOM   7331  C  C   . ILE B  1 198 ? -3.122  65.924 17.265 1.00 14.53 ? 198  ILE B C   1 
ATOM   7332  O  O   . ILE B  1 198 ? -2.622  67.001 16.926 1.00 14.43 ? 198  ILE B O   1 
ATOM   7333  C  CB  . ILE B  1 198 ? -2.580  63.845 15.954 1.00 13.82 ? 198  ILE B CB  1 
ATOM   7334  C  CG1 . ILE B  1 198 ? -1.303  64.444 15.347 1.00 10.30 ? 198  ILE B CG1 1 
ATOM   7335  C  CG2 . ILE B  1 198 ? -3.180  62.774 15.053 1.00 13.21 ? 198  ILE B CG2 1 
ATOM   7336  C  CD1 . ILE B  1 198 ? -0.180  63.380 15.161 1.00 10.75 ? 198  ILE B CD1 1 
ATOM   7337  N  N   . THR B  1 199 ? -3.259  65.546 18.527 1.00 14.07 ? 199  THR B N   1 
ATOM   7338  C  CA  . THR B  1 199 ? -2.829  66.382 19.628 1.00 13.71 ? 199  THR B CA  1 
ATOM   7339  C  C   . THR B  1 199 ? -1.360  66.178 19.967 1.00 14.11 ? 199  THR B C   1 
ATOM   7340  O  O   . THR B  1 199 ? -0.788  65.150 19.643 1.00 16.46 ? 199  THR B O   1 
ATOM   7341  C  CB  . THR B  1 199 ? -3.648  66.044 20.900 1.00 12.65 ? 199  THR B CB  1 
ATOM   7342  O  OG1 . THR B  1 199 ? -3.588  64.626 21.120 1.00 14.82 ? 199  THR B OG1 1 
ATOM   7343  C  CG2 . THR B  1 199 ? -5.140  66.488 20.753 1.00 11.95 ? 199  THR B CG2 1 
ATOM   7344  N  N   . ASP B  1 200 ? -0.762  67.163 20.625 1.00 14.87 ? 200  ASP B N   1 
ATOM   7345  C  CA  . ASP B  1 200 ? 0.612   67.024 21.105 1.00 15.28 ? 200  ASP B CA  1 
ATOM   7346  C  C   . ASP B  1 200 ? 0.441   66.383 22.486 1.00 14.76 ? 200  ASP B C   1 
ATOM   7347  O  O   . ASP B  1 200 ? -0.681  66.055 22.884 1.00 14.27 ? 200  ASP B O   1 
ATOM   7348  C  CB  . ASP B  1 200 ? 1.329   68.388 21.180 1.00 15.75 ? 200  ASP B CB  1 
ATOM   7349  C  CG  . ASP B  1 200 ? 0.770   69.297 22.267 1.00 17.42 ? 200  ASP B CG  1 
ATOM   7350  O  OD1 . ASP B  1 200 ? -0.399  69.105 22.691 1.00 15.40 ? 200  ASP B OD1 1 
ATOM   7351  O  OD2 . ASP B  1 200 ? 1.490   70.237 22.693 1.00 18.02 ? 200  ASP B OD2 1 
ATOM   7352  N  N   . TRP B  1 201 ? 1.526   66.208 23.228 1.00 15.17 ? 201  TRP B N   1 
ATOM   7353  C  CA  . TRP B  1 201 ? 1.435   65.546 24.521 1.00 15.23 ? 201  TRP B CA  1 
ATOM   7354  C  C   . TRP B  1 201 ? 0.434   66.141 25.518 1.00 15.57 ? 201  TRP B C   1 
ATOM   7355  O  O   . TRP B  1 201 ? -0.419  65.424 26.035 1.00 15.03 ? 201  TRP B O   1 
ATOM   7356  C  CB  . TRP B  1 201 ? 2.816   65.477 25.192 1.00 15.58 ? 201  TRP B CB  1 
ATOM   7357  C  CG  . TRP B  1 201 ? 2.833   64.540 26.375 1.00 17.07 ? 201  TRP B CG  1 
ATOM   7358  C  CD1 . TRP B  1 201 ? 3.182   63.211 26.361 1.00 16.43 ? 201  TRP B CD1 1 
ATOM   7359  C  CD2 . TRP B  1 201 ? 2.351   64.809 27.705 1.00 16.98 ? 201  TRP B CD2 1 
ATOM   7360  N  NE1 . TRP B  1 201 ? 2.939   62.642 27.583 1.00 15.22 ? 201  TRP B NE1 1 
ATOM   7361  C  CE2 . TRP B  1 201 ? 2.431   63.594 28.430 1.00 17.11 ? 201  TRP B CE2 1 
ATOM   7362  C  CE3 . TRP B  1 201 ? 1.856   65.952 28.350 1.00 15.90 ? 201  TRP B CE3 1 
ATOM   7363  C  CZ2 . TRP B  1 201 ? 2.032   63.488 29.781 1.00 17.26 ? 201  TRP B CZ2 1 
ATOM   7364  C  CZ3 . TRP B  1 201 ? 1.456   65.850 29.696 1.00 16.59 ? 201  TRP B CZ3 1 
ATOM   7365  C  CH2 . TRP B  1 201 ? 1.547   64.624 30.393 1.00 18.09 ? 201  TRP B CH2 1 
ATOM   7366  N  N   . VAL B  1 202 ? 0.531   67.443 25.772 1.00 14.98 ? 202  VAL B N   1 
ATOM   7367  C  CA  . VAL B  1 202 ? -0.334  68.074 26.761 1.00 16.23 ? 202  VAL B CA  1 
ATOM   7368  C  C   . VAL B  1 202 ? -1.809  68.167 26.353 1.00 16.00 ? 202  VAL B C   1 
ATOM   7369  O  O   . VAL B  1 202 ? -2.693  68.018 27.200 1.00 16.78 ? 202  VAL B O   1 
ATOM   7370  C  CB  . VAL B  1 202 ? 0.228   69.468 27.182 1.00 16.97 ? 202  VAL B CB  1 
ATOM   7371  C  CG1 . VAL B  1 202 ? -0.080  70.520 26.108 1.00 14.77 ? 202  VAL B CG1 1 
ATOM   7372  C  CG2 . VAL B  1 202 ? -0.310  69.857 28.589 1.00 16.57 ? 202  VAL B CG2 1 
ATOM   7373  N  N   . TYR B  1 203 ? -2.086  68.374 25.069 1.00 14.68 ? 203  TYR B N   1 
ATOM   7374  C  CA  . TYR B  1 203 ? -3.472  68.420 24.624 1.00 13.86 ? 203  TYR B CA  1 
ATOM   7375  C  C   . TYR B  1 203 ? -4.066  67.006 24.694 1.00 14.25 ? 203  TYR B C   1 
ATOM   7376  O  O   . TYR B  1 203 ? -5.231  66.838 25.035 1.00 14.26 ? 203  TYR B O   1 
ATOM   7377  C  CB  . TYR B  1 203 ? -3.571  68.966 23.202 1.00 13.07 ? 203  TYR B CB  1 
ATOM   7378  C  CG  . TYR B  1 203 ? -3.842  70.454 23.168 1.00 13.02 ? 203  TYR B CG  1 
ATOM   7379  C  CD1 . TYR B  1 203 ? -2.817  71.372 22.984 1.00 12.57 ? 203  TYR B CD1 1 
ATOM   7380  C  CD2 . TYR B  1 203 ? -5.138  70.938 23.351 1.00 13.26 ? 203  TYR B CD2 1 
ATOM   7381  C  CE1 . TYR B  1 203 ? -3.077  72.748 22.976 1.00 15.24 ? 203  TYR B CE1 1 
ATOM   7382  C  CE2 . TYR B  1 203 ? -5.417  72.294 23.349 1.00 14.33 ? 203  TYR B CE2 1 
ATOM   7383  C  CZ  . TYR B  1 203 ? -4.381  73.198 23.154 1.00 15.24 ? 203  TYR B CZ  1 
ATOM   7384  O  OH  . TYR B  1 203 ? -4.681  74.533 23.094 1.00 15.60 ? 203  TYR B OH  1 
ATOM   7385  N  N   . GLU B  1 204 ? -3.261  65.995 24.378 1.00 14.36 ? 204  GLU B N   1 
ATOM   7386  C  CA  . GLU B  1 204 ? -3.733  64.616 24.440 1.00 15.62 ? 204  GLU B CA  1 
ATOM   7387  C  C   . GLU B  1 204 ? -4.098  64.251 25.878 1.00 15.78 ? 204  GLU B C   1 
ATOM   7388  O  O   . GLU B  1 204 ? -5.195  63.773 26.157 1.00 16.00 ? 204  GLU B O   1 
ATOM   7389  C  CB  . GLU B  1 204 ? -2.656  63.626 23.949 1.00 15.20 ? 204  GLU B CB  1 
ATOM   7390  C  CG  . GLU B  1 204 ? -3.048  62.178 24.213 1.00 16.03 ? 204  GLU B CG  1 
ATOM   7391  C  CD  . GLU B  1 204 ? -1.992  61.133 23.862 1.00 18.55 ? 204  GLU B CD  1 
ATOM   7392  O  OE1 . GLU B  1 204 ? -1.069  61.406 23.053 1.00 21.31 ? 204  GLU B OE1 1 
ATOM   7393  O  OE2 . GLU B  1 204 ? -2.099  59.995 24.387 1.00 20.77 ? 204  GLU B OE2 1 
ATOM   7394  N  N   . GLU B  1 205 ? -3.168  64.492 26.793 1.00 15.87 ? 205  GLU B N   1 
ATOM   7395  C  CA  . GLU B  1 205 ? -3.369  64.122 28.177 1.00 16.19 ? 205  GLU B CA  1 
ATOM   7396  C  C   . GLU B  1 205 ? -4.340  64.960 28.994 1.00 18.67 ? 205  GLU B C   1 
ATOM   7397  O  O   . GLU B  1 205 ? -5.223  64.422 29.653 1.00 18.92 ? 205  GLU B O   1 
ATOM   7398  C  CB  . GLU B  1 205 ? -2.018  64.108 28.889 1.00 17.27 ? 205  GLU B CB  1 
ATOM   7399  C  CG  . GLU B  1 205 ? -2.093  63.966 30.390 1.00 17.47 ? 205  GLU B CG  1 
ATOM   7400  C  CD  . GLU B  1 205 ? -2.582  62.576 30.822 1.00 21.01 ? 205  GLU B CD  1 
ATOM   7401  O  OE1 . GLU B  1 205 ? -2.710  61.674 29.949 1.00 16.63 ? 205  GLU B OE1 1 
ATOM   7402  O  OE2 . GLU B  1 205 ? -2.828  62.391 32.043 1.00 21.60 ? 205  GLU B OE2 1 
ATOM   7403  N  N   . GLU B  1 206 ? -4.187  66.280 28.936 1.00 18.40 ? 206  GLU B N   1 
ATOM   7404  C  CA  . GLU B  1 206 ? -4.986  67.173 29.760 1.00 18.45 ? 206  GLU B CA  1 
ATOM   7405  C  C   . GLU B  1 206 ? -6.243  67.831 29.216 1.00 18.61 ? 206  GLU B C   1 
ATOM   7406  O  O   . GLU B  1 206 ? -7.092  68.250 29.989 1.00 18.39 ? 206  GLU B O   1 
ATOM   7407  C  CB  . GLU B  1 206 ? -4.062  68.261 30.281 1.00 18.22 ? 206  GLU B CB  1 
ATOM   7408  C  CG  . GLU B  1 206 ? -2.783  67.700 30.859 1.00 19.10 ? 206  GLU B CG  1 
ATOM   7409  C  CD  . GLU B  1 206 ? -2.974  67.084 32.234 1.00 20.28 ? 206  GLU B CD  1 
ATOM   7410  O  OE1 . GLU B  1 206 ? -4.119  66.763 32.595 1.00 19.36 ? 206  GLU B OE1 1 
ATOM   7411  O  OE2 . GLU B  1 206 ? -1.972  66.909 32.951 1.00 21.12 ? 206  GLU B OE2 1 
ATOM   7412  N  N   . VAL B  1 207 ? -6.371  67.920 27.900 1.00 18.87 ? 207  VAL B N   1 
ATOM   7413  C  CA  . VAL B  1 207 ? -7.511  68.604 27.315 1.00 19.02 ? 207  VAL B CA  1 
ATOM   7414  C  C   . VAL B  1 207 ? -8.538  67.735 26.613 1.00 20.82 ? 207  VAL B C   1 
ATOM   7415  O  O   . VAL B  1 207 ? -9.716  67.726 26.993 1.00 21.96 ? 207  VAL B O   1 
ATOM   7416  C  CB  . VAL B  1 207 ? -7.030  69.677 26.330 1.00 19.73 ? 207  VAL B CB  1 
ATOM   7417  C  CG1 . VAL B  1 207 ? -8.194  70.453 25.784 1.00 17.66 ? 207  VAL B CG1 1 
ATOM   7418  C  CG2 . VAL B  1 207 ? -6.044  70.595 27.027 1.00 18.34 ? 207  VAL B CG2 1 
ATOM   7419  N  N   . PHE B  1 208 ? -8.109  67.001 25.593 1.00 19.59 ? 208  PHE B N   1 
ATOM   7420  C  CA  . PHE B  1 208 ? -9.051  66.169 24.850 1.00 19.32 ? 208  PHE B CA  1 
ATOM   7421  C  C   . PHE B  1 208 ? -9.109  64.715 25.264 1.00 19.00 ? 208  PHE B C   1 
ATOM   7422  O  O   . PHE B  1 208 ? -10.019 64.003 24.848 1.00 18.56 ? 208  PHE B O   1 
ATOM   7423  C  CB  . PHE B  1 208 ? -8.752  66.265 23.346 1.00 20.34 ? 208  PHE B CB  1 
ATOM   7424  C  CG  . PHE B  1 208 ? -9.087  67.610 22.759 1.00 21.44 ? 208  PHE B CG  1 
ATOM   7425  C  CD1 . PHE B  1 208 ? -10.415 67.999 22.597 1.00 22.46 ? 208  PHE B CD1 1 
ATOM   7426  C  CD2 . PHE B  1 208 ? -8.085  68.500 22.417 1.00 20.23 ? 208  PHE B CD2 1 
ATOM   7427  C  CE1 . PHE B  1 208 ? -10.739 69.269 22.106 1.00 23.10 ? 208  PHE B CE1 1 
ATOM   7428  C  CE2 . PHE B  1 208 ? -8.390  69.764 21.928 1.00 21.72 ? 208  PHE B CE2 1 
ATOM   7429  C  CZ  . PHE B  1 208 ? -9.717  70.151 21.771 1.00 22.57 ? 208  PHE B CZ  1 
ATOM   7430  N  N   . SER B  1 209 ? -8.168  64.271 26.090 1.00 17.43 ? 209  SER B N   1 
ATOM   7431  C  CA  . SER B  1 209 ? -8.163  62.870 26.514 1.00 18.77 ? 209  SER B CA  1 
ATOM   7432  C  C   . SER B  1 209 ? -8.274  61.976 25.282 1.00 18.04 ? 209  SER B C   1 
ATOM   7433  O  O   . SER B  1 209 ? -8.988  60.982 25.276 1.00 17.64 ? 209  SER B O   1 
ATOM   7434  C  CB  . SER B  1 209 ? -9.336  62.577 27.455 1.00 18.59 ? 209  SER B CB  1 
ATOM   7435  O  OG  . SER B  1 209 ? -9.054  62.991 28.776 1.00 20.83 ? 209  SER B OG  1 
ATOM   7436  N  N   . ALA B  1 210 ? -7.557  62.349 24.235 1.00 18.39 ? 210  ALA B N   1 
ATOM   7437  C  CA  . ALA B  1 210 ? -7.586  61.596 22.995 1.00 18.87 ? 210  ALA B CA  1 
ATOM   7438  C  C   . ALA B  1 210 ? -6.430  62.075 22.145 1.00 19.05 ? 210  ALA B C   1 
ATOM   7439  O  O   . ALA B  1 210 ? -5.889  63.165 22.357 1.00 20.26 ? 210  ALA B O   1 
ATOM   7440  C  CB  . ALA B  1 210 ? -8.921  61.822 22.265 1.00 16.93 ? 210  ALA B CB  1 
ATOM   7441  N  N   . TYR B  1 211 ? -6.045  61.254 21.182 1.00 18.73 ? 211  TYR B N   1 
ATOM   7442  C  CA  . TYR B  1 211 ? -4.941  61.592 20.307 1.00 19.51 ? 211  TYR B CA  1 
ATOM   7443  C  C   . TYR B  1 211 ? -5.477  62.329 19.105 1.00 19.18 ? 211  TYR B C   1 
ATOM   7444  O  O   . TYR B  1 211 ? -4.799  63.179 18.541 1.00 19.38 ? 211  TYR B O   1 
ATOM   7445  C  CB  . TYR B  1 211 ? -4.247  60.306 19.855 1.00 18.85 ? 211  TYR B CB  1 
ATOM   7446  C  CG  . TYR B  1 211 ? -2.995  60.482 19.028 1.00 19.36 ? 211  TYR B CG  1 
ATOM   7447  C  CD1 . TYR B  1 211 ? -2.158  61.582 19.214 1.00 17.14 ? 211  TYR B CD1 1 
ATOM   7448  C  CD2 . TYR B  1 211 ? -2.569  59.467 18.160 1.00 17.95 ? 211  TYR B CD2 1 
ATOM   7449  C  CE1 . TYR B  1 211 ? -0.928  61.661 18.571 1.00 17.59 ? 211  TYR B CE1 1 
ATOM   7450  C  CE2 . TYR B  1 211 ? -1.345  59.539 17.519 1.00 18.64 ? 211  TYR B CE2 1 
ATOM   7451  C  CZ  . TYR B  1 211 ? -0.520  60.634 17.729 1.00 19.69 ? 211  TYR B CZ  1 
ATOM   7452  O  OH  . TYR B  1 211 ? 0.734   60.667 17.138 1.00 18.57 ? 211  TYR B OH  1 
ATOM   7453  N  N   . SER B  1 212 ? -6.700  61.997 18.707 1.00 19.30 ? 212  SER B N   1 
ATOM   7454  C  CA  . SER B  1 212 ? -7.258  62.635 17.534 1.00 20.23 ? 212  SER B CA  1 
ATOM   7455  C  C   . SER B  1 212 ? -7.708  64.059 17.804 1.00 19.78 ? 212  SER B C   1 
ATOM   7456  O  O   . SER B  1 212 ? -8.123  64.411 18.909 1.00 17.73 ? 212  SER B O   1 
ATOM   7457  C  CB  . SER B  1 212 ? -8.408  61.817 16.959 1.00 20.49 ? 212  SER B CB  1 
ATOM   7458  O  OG  . SER B  1 212 ? -9.570  61.960 17.728 1.00 25.20 ? 212  SER B OG  1 
ATOM   7459  N  N   . ALA B  1 213 ? -7.577  64.877 16.768 1.00 19.30 ? 213  ALA B N   1 
ATOM   7460  C  CA  . ALA B  1 213 ? -7.950  66.274 16.819 1.00 19.36 ? 213  ALA B CA  1 
ATOM   7461  C  C   . ALA B  1 213 ? -8.622  66.594 15.493 1.00 19.91 ? 213  ALA B C   1 
ATOM   7462  O  O   . ALA B  1 213 ? -8.282  67.565 14.826 1.00 18.62 ? 213  ALA B O   1 
ATOM   7463  C  CB  . ALA B  1 213 ? -6.713  67.148 17.014 1.00 19.33 ? 213  ALA B CB  1 
ATOM   7464  N  N   . LEU B  1 214 ? -9.539  65.728 15.091 1.00 20.03 ? 214  LEU B N   1 
ATOM   7465  C  CA  . LEU B  1 214 ? -10.294 65.962 13.880 1.00 21.44 ? 214  LEU B CA  1 
ATOM   7466  C  C   . LEU B  1 214 ? -11.747 65.608 14.165 1.00 21.13 ? 214  LEU B C   1 
ATOM   7467  O  O   . LEU B  1 214 ? -12.048 64.703 14.971 1.00 20.93 ? 214  LEU B O   1 
ATOM   7468  C  CB  . LEU B  1 214 ? -9.706  65.207 12.681 1.00 23.89 ? 214  LEU B CB  1 
ATOM   7469  C  CG  . LEU B  1 214 ? -9.318  63.748 12.752 1.00 24.40 ? 214  LEU B CG  1 
ATOM   7470  C  CD1 . LEU B  1 214 ? -10.572 62.905 12.856 1.00 27.04 ? 214  LEU B CD1 1 
ATOM   7471  C  CD2 . LEU B  1 214 ? -8.534  63.390 11.494 1.00 23.83 ? 214  LEU B CD2 1 
ATOM   7472  N  N   . TRP B  1 215 ? -12.645 66.354 13.533 1.00 19.16 ? 215  TRP B N   1 
ATOM   7473  C  CA  . TRP B  1 215 ? -14.075 66.190 13.774 1.00 19.20 ? 215  TRP B CA  1 
ATOM   7474  C  C   . TRP B  1 215 ? -14.922 66.246 12.518 1.00 19.55 ? 215  TRP B C   1 
ATOM   7475  O  O   . TRP B  1 215 ? -15.090 67.317 11.929 1.00 19.30 ? 215  TRP B O   1 
ATOM   7476  C  CB  . TRP B  1 215 ? -14.526 67.298 14.730 1.00 18.64 ? 215  TRP B CB  1 
ATOM   7477  C  CG  . TRP B  1 215 ? -13.837 67.238 16.063 1.00 19.84 ? 215  TRP B CG  1 
ATOM   7478  C  CD1 . TRP B  1 215 ? -14.249 66.538 17.173 1.00 18.97 ? 215  TRP B CD1 1 
ATOM   7479  C  CD2 . TRP B  1 215 ? -12.597 67.869 16.424 1.00 18.43 ? 215  TRP B CD2 1 
ATOM   7480  N  NE1 . TRP B  1 215 ? -13.343 66.699 18.188 1.00 19.83 ? 215  TRP B NE1 1 
ATOM   7481  C  CE2 . TRP B  1 215 ? -12.323 67.511 17.760 1.00 19.17 ? 215  TRP B CE2 1 
ATOM   7482  C  CE3 . TRP B  1 215 ? -11.693 68.700 15.747 1.00 19.64 ? 215  TRP B CE3 1 
ATOM   7483  C  CZ2 . TRP B  1 215 ? -11.179 67.962 18.438 1.00 19.29 ? 215  TRP B CZ2 1 
ATOM   7484  C  CZ3 . TRP B  1 215 ? -10.557 69.146 16.421 1.00 18.79 ? 215  TRP B CZ3 1 
ATOM   7485  C  CH2 . TRP B  1 215 ? -10.312 68.776 17.754 1.00 18.49 ? 215  TRP B CH2 1 
ATOM   7486  N  N   . TRP B  1 216 ? -15.456 65.101 12.109 1.00 19.65 ? 216  TRP B N   1 
ATOM   7487  C  CA  . TRP B  1 216 ? -16.309 65.065 10.939 1.00 19.59 ? 216  TRP B CA  1 
ATOM   7488  C  C   . TRP B  1 216 ? -17.643 65.751 11.286 1.00 20.64 ? 216  TRP B C   1 
ATOM   7489  O  O   . TRP B  1 216 ? -18.101 65.669 12.432 1.00 18.81 ? 216  TRP B O   1 
ATOM   7490  C  CB  . TRP B  1 216 ? -16.614 63.624 10.535 1.00 19.35 ? 216  TRP B CB  1 
ATOM   7491  C  CG  . TRP B  1 216 ? -15.546 62.887 9.819  1.00 19.88 ? 216  TRP B CG  1 
ATOM   7492  C  CD1 . TRP B  1 216 ? -14.734 61.899 10.328 1.00 20.06 ? 216  TRP B CD1 1 
ATOM   7493  C  CD2 . TRP B  1 216 ? -15.255 62.957 8.419  1.00 19.54 ? 216  TRP B CD2 1 
ATOM   7494  N  NE1 . TRP B  1 216 ? -13.972 61.344 9.324  1.00 20.59 ? 216  TRP B NE1 1 
ATOM   7495  C  CE2 . TRP B  1 216 ? -14.271 61.975 8.143  1.00 20.19 ? 216  TRP B CE2 1 
ATOM   7496  C  CE3 . TRP B  1 216 ? -15.736 63.747 7.370  1.00 19.93 ? 216  TRP B CE3 1 
ATOM   7497  C  CZ2 . TRP B  1 216 ? -13.763 61.769 6.861  1.00 18.91 ? 216  TRP B CZ2 1 
ATOM   7498  C  CZ3 . TRP B  1 216 ? -15.236 63.544 6.101  1.00 18.81 ? 216  TRP B CZ3 1 
ATOM   7499  C  CH2 . TRP B  1 216 ? -14.256 62.558 5.855  1.00 19.76 ? 216  TRP B CH2 1 
ATOM   7500  N  N   . SER B  1 217 ? -18.249 66.436 10.312 1.00 20.54 ? 217  SER B N   1 
ATOM   7501  C  CA  . SER B  1 217 ? -19.545 67.073 10.520 1.00 20.97 ? 217  SER B CA  1 
ATOM   7502  C  C   . SER B  1 217 ? -20.530 65.899 10.497 1.00 21.15 ? 217  SER B C   1 
ATOM   7503  O  O   . SER B  1 217 ? -20.193 64.828 10.006 1.00 21.47 ? 217  SER B O   1 
ATOM   7504  C  CB  . SER B  1 217 ? -19.847 68.072 9.395  1.00 21.62 ? 217  SER B CB  1 
ATOM   7505  O  OG  . SER B  1 217 ? -19.986 67.425 8.148  1.00 22.36 ? 217  SER B OG  1 
ATOM   7506  N  N   . PRO B  1 218 ? -21.757 66.086 11.013 1.00 21.53 ? 218  PRO B N   1 
ATOM   7507  C  CA  . PRO B  1 218 ? -22.779 65.023 11.066 1.00 21.79 ? 218  PRO B CA  1 
ATOM   7508  C  C   . PRO B  1 218 ? -22.963 64.103 9.857  1.00 21.28 ? 218  PRO B C   1 
ATOM   7509  O  O   . PRO B  1 218 ? -23.006 62.893 10.018 1.00 21.76 ? 218  PRO B O   1 
ATOM   7510  C  CB  . PRO B  1 218 ? -24.065 65.789 11.417 1.00 21.42 ? 218  PRO B CB  1 
ATOM   7511  C  CG  . PRO B  1 218 ? -23.550 66.913 12.258 1.00 20.02 ? 218  PRO B CG  1 
ATOM   7512  C  CD  . PRO B  1 218 ? -22.329 67.368 11.466 1.00 20.83 ? 218  PRO B CD  1 
ATOM   7513  N  N   . ASN B  1 219 ? -23.072 64.660 8.658  1.00 21.44 ? 219  ASN B N   1 
ATOM   7514  C  CA  . ASN B  1 219 ? -23.258 63.810 7.494  1.00 21.89 ? 219  ASN B CA  1 
ATOM   7515  C  C   . ASN B  1 219 ? -21.952 63.582 6.724  1.00 20.83 ? 219  ASN B C   1 
ATOM   7516  O  O   . ASN B  1 219 ? -21.941 62.979 5.652  1.00 19.97 ? 219  ASN B O   1 
ATOM   7517  C  CB  . ASN B  1 219 ? -24.367 64.354 6.579  1.00 22.28 ? 219  ASN B CB  1 
ATOM   7518  C  CG  . ASN B  1 219 ? -23.956 65.591 5.810  1.00 25.43 ? 219  ASN B CG  1 
ATOM   7519  O  OD1 . ASN B  1 219 ? -22.771 65.918 5.704  1.00 25.69 ? 219  ASN B OD1 1 
ATOM   7520  N  ND2 . ASN B  1 219 ? -24.933 66.280 5.235  1.00 28.52 ? 219  ASN B ND2 1 
ATOM   7521  N  N   . GLY B  1 220 ? -20.856 64.074 7.284  1.00 20.66 ? 220  GLY B N   1 
ATOM   7522  C  CA  . GLY B  1 220 ? -19.559 63.849 6.685  1.00 19.94 ? 220  GLY B CA  1 
ATOM   7523  C  C   . GLY B  1 220 ? -19.067 64.773 5.604  1.00 20.32 ? 220  GLY B C   1 
ATOM   7524  O  O   . GLY B  1 220 ? -17.992 64.545 5.052  1.00 21.07 ? 220  GLY B O   1 
ATOM   7525  N  N   . THR B  1 221 ? -19.823 65.816 5.299  1.00 19.25 ? 221  THR B N   1 
ATOM   7526  C  CA  . THR B  1 221 ? -19.403 66.745 4.266  1.00 19.28 ? 221  THR B CA  1 
ATOM   7527  C  C   . THR B  1 221 ? -18.152 67.512 4.664  1.00 18.90 ? 221  THR B C   1 
ATOM   7528  O  O   . THR B  1 221 ? -17.202 67.579 3.901  1.00 18.65 ? 221  THR B O   1 
ATOM   7529  C  CB  . THR B  1 221 ? -20.509 67.765 3.932  1.00 20.35 ? 221  THR B CB  1 
ATOM   7530  O  OG1 . THR B  1 221 ? -21.555 67.115 3.203  1.00 22.46 ? 221  THR B OG1 1 
ATOM   7531  C  CG2 . THR B  1 221 ? -19.942 68.902 3.073  1.00 19.85 ? 221  THR B CG2 1 
ATOM   7532  N  N   . PHE B  1 222 ? -18.156 68.085 5.864  1.00 18.42 ? 222  PHE B N   1 
ATOM   7533  C  CA  . PHE B  1 222 ? -17.021 68.874 6.343  1.00 17.50 ? 222  PHE B CA  1 
ATOM   7534  C  C   . PHE B  1 222 ? -16.115 68.096 7.295  1.00 17.73 ? 222  PHE B C   1 
ATOM   7535  O  O   . PHE B  1 222 ? -16.567 67.210 8.016  1.00 17.88 ? 222  PHE B O   1 
ATOM   7536  C  CB  . PHE B  1 222 ? -17.516 70.108 7.098  1.00 17.57 ? 222  PHE B CB  1 
ATOM   7537  C  CG  . PHE B  1 222 ? -18.229 71.123 6.244  1.00 18.09 ? 222  PHE B CG  1 
ATOM   7538  C  CD1 . PHE B  1 222 ? -17.520 71.915 5.347  1.00 17.61 ? 222  PHE B CD1 1 
ATOM   7539  C  CD2 . PHE B  1 222 ? -19.598 71.323 6.380  1.00 17.58 ? 222  PHE B CD2 1 
ATOM   7540  C  CE1 . PHE B  1 222 ? -18.152 72.895 4.590  1.00 17.66 ? 222  PHE B CE1 1 
ATOM   7541  C  CE2 . PHE B  1 222 ? -20.253 72.306 5.625  1.00 19.81 ? 222  PHE B CE2 1 
ATOM   7542  C  CZ  . PHE B  1 222 ? -19.522 73.096 4.726  1.00 19.72 ? 222  PHE B CZ  1 
ATOM   7543  N  N   . LEU B  1 223 ? -14.829 68.434 7.297  1.00 18.03 ? 223  LEU B N   1 
ATOM   7544  C  CA  . LEU B  1 223 ? -13.888 67.808 8.217  1.00 17.39 ? 223  LEU B CA  1 
ATOM   7545  C  C   . LEU B  1 223 ? -13.179 68.952 8.934  1.00 17.27 ? 223  LEU B C   1 
ATOM   7546  O  O   . LEU B  1 223 ? -12.444 69.720 8.328  1.00 17.68 ? 223  LEU B O   1 
ATOM   7547  C  CB  . LEU B  1 223 ? -12.859 66.921 7.494  1.00 16.27 ? 223  LEU B CB  1 
ATOM   7548  C  CG  . LEU B  1 223 ? -11.814 66.372 8.498  1.00 18.03 ? 223  LEU B CG  1 
ATOM   7549  C  CD1 . LEU B  1 223 ? -12.497 65.453 9.540  1.00 14.78 ? 223  LEU B CD1 1 
ATOM   7550  C  CD2 . LEU B  1 223 ? -10.724 65.623 7.759  1.00 15.60 ? 223  LEU B CD2 1 
ATOM   7551  N  N   . ALA B  1 224 ? -13.442 69.079 10.226 1.00 16.96 ? 224  ALA B N   1 
ATOM   7552  C  CA  . ALA B  1 224 ? -12.829 70.121 11.019 1.00 18.20 ? 224  ALA B CA  1 
ATOM   7553  C  C   . ALA B  1 224 ? -11.599 69.536 11.704 1.00 18.21 ? 224  ALA B C   1 
ATOM   7554  O  O   . ALA B  1 224 ? -11.532 68.330 11.925 1.00 19.22 ? 224  ALA B O   1 
ATOM   7555  C  CB  . ALA B  1 224 ? -13.824 70.635 12.068 1.00 16.39 ? 224  ALA B CB  1 
ATOM   7556  N  N   . TYR B  1 225 ? -10.623 70.372 12.031 1.00 18.32 ? 225  TYR B N   1 
ATOM   7557  C  CA  . TYR B  1 225 ? -9.434  69.874 12.717 1.00 17.93 ? 225  TYR B CA  1 
ATOM   7558  C  C   . TYR B  1 225 ? -8.616  70.962 13.351 1.00 17.91 ? 225  TYR B C   1 
ATOM   7559  O  O   . TYR B  1 225 ? -8.682  72.120 12.953 1.00 18.74 ? 225  TYR B O   1 
ATOM   7560  C  CB  . TYR B  1 225 ? -8.526  69.099 11.765 1.00 16.62 ? 225  TYR B CB  1 
ATOM   7561  C  CG  . TYR B  1 225 ? -7.933  69.909 10.631 1.00 17.64 ? 225  TYR B CG  1 
ATOM   7562  C  CD1 . TYR B  1 225 ? -8.619  70.056 9.422  1.00 17.05 ? 225  TYR B CD1 1 
ATOM   7563  C  CD2 . TYR B  1 225 ? -6.665  70.491 10.748 1.00 16.82 ? 225  TYR B CD2 1 
ATOM   7564  C  CE1 . TYR B  1 225 ? -8.061  70.755 8.355  1.00 15.03 ? 225  TYR B CE1 1 
ATOM   7565  C  CE2 . TYR B  1 225 ? -6.097  71.193 9.683  1.00 17.55 ? 225  TYR B CE2 1 
ATOM   7566  C  CZ  . TYR B  1 225 ? -6.806  71.320 8.487  1.00 17.61 ? 225  TYR B CZ  1 
ATOM   7567  O  OH  . TYR B  1 225 ? -6.256  72.026 7.436  1.00 15.93 ? 225  TYR B OH  1 
ATOM   7568  N  N   . ALA B  1 226 ? -7.829  70.567 14.336 1.00 17.72 ? 226  ALA B N   1 
ATOM   7569  C  CA  . ALA B  1 226 ? -6.949  71.487 15.032 1.00 18.10 ? 226  ALA B CA  1 
ATOM   7570  C  C   . ALA B  1 226 ? -5.506  71.250 14.568 1.00 18.50 ? 226  ALA B C   1 
ATOM   7571  O  O   . ALA B  1 226 ? -5.155  70.139 14.127 1.00 16.73 ? 226  ALA B O   1 
ATOM   7572  C  CB  . ALA B  1 226 ? -7.038  71.251 16.526 1.00 18.85 ? 226  ALA B CB  1 
ATOM   7573  N  N   . GLN B  1 227 ? -4.694  72.300 14.675 1.00 16.78 ? 227  GLN B N   1 
ATOM   7574  C  CA  . GLN B  1 227 ? -3.288  72.246 14.322 1.00 17.65 ? 227  GLN B CA  1 
ATOM   7575  C  C   . GLN B  1 227 ? -2.527  72.823 15.511 1.00 18.72 ? 227  GLN B C   1 
ATOM   7576  O  O   . GLN B  1 227 ? -2.771  73.957 15.931 1.00 17.82 ? 227  GLN B O   1 
ATOM   7577  C  CB  . GLN B  1 227 ? -2.979  73.087 13.091 1.00 17.65 ? 227  GLN B CB  1 
ATOM   7578  C  CG  . GLN B  1 227 ? -1.519  73.088 12.742 1.00 17.09 ? 227  GLN B CG  1 
ATOM   7579  C  CD  . GLN B  1 227 ? -1.200  74.133 11.689 1.00 20.96 ? 227  GLN B CD  1 
ATOM   7580  O  OE1 . GLN B  1 227 ? -1.045  75.323 12.002 1.00 20.74 ? 227  GLN B OE1 1 
ATOM   7581  N  NE2 . GLN B  1 227 ? -1.125  73.700 10.429 1.00 15.84 ? 227  GLN B NE2 1 
ATOM   7582  N  N   . PHE B  1 228 ? -1.609  72.034 16.057 1.00 19.92 ? 228  PHE B N   1 
ATOM   7583  C  CA  . PHE B  1 228 ? -0.835  72.453 17.214 1.00 19.15 ? 228  PHE B CA  1 
ATOM   7584  C  C   . PHE B  1 228 ? 0.603   72.680 16.795 1.00 20.57 ? 228  PHE B C   1 
ATOM   7585  O  O   . PHE B  1 228 ? 1.179   71.914 16.012 1.00 20.72 ? 228  PHE B O   1 
ATOM   7586  C  CB  . PHE B  1 228 ? -0.913  71.384 18.308 1.00 19.60 ? 228  PHE B CB  1 
ATOM   7587  C  CG  . PHE B  1 228 ? -2.329  71.016 18.713 1.00 17.93 ? 228  PHE B CG  1 
ATOM   7588  C  CD1 . PHE B  1 228 ? -3.040  71.799 19.624 1.00 18.14 ? 228  PHE B CD1 1 
ATOM   7589  C  CD2 . PHE B  1 228 ? -2.945  69.886 18.177 1.00 16.44 ? 228  PHE B CD2 1 
ATOM   7590  C  CE1 . PHE B  1 228 ? -4.350  71.450 19.993 1.00 18.16 ? 228  PHE B CE1 1 
ATOM   7591  C  CE2 . PHE B  1 228 ? -4.247  69.532 18.538 1.00 16.45 ? 228  PHE B CE2 1 
ATOM   7592  C  CZ  . PHE B  1 228 ? -4.949  70.313 19.442 1.00 16.72 ? 228  PHE B CZ  1 
ATOM   7593  N  N   . ASN B  1 229 ? 1.168   73.760 17.323 1.00 21.63 ? 229  ASN B N   1 
ATOM   7594  C  CA  . ASN B  1 229 ? 2.529   74.167 17.030 1.00 20.94 ? 229  ASN B CA  1 
ATOM   7595  C  C   . ASN B  1 229 ? 3.320   74.193 18.330 1.00 20.87 ? 229  ASN B C   1 
ATOM   7596  O  O   . ASN B  1 229 ? 3.063   75.027 19.199 1.00 20.09 ? 229  ASN B O   1 
ATOM   7597  C  CB  . ASN B  1 229 ? 2.498   75.562 16.419 1.00 22.81 ? 229  ASN B CB  1 
ATOM   7598  C  CG  . ASN B  1 229 ? 3.826   75.981 15.886 1.00 25.47 ? 229  ASN B CG  1 
ATOM   7599  O  OD1 . ASN B  1 229 ? 4.863   75.591 16.430 1.00 23.25 ? 229  ASN B OD1 1 
ATOM   7600  N  ND2 . ASN B  1 229 ? 3.797   76.775 14.814 1.00 27.16 ? 229  ASN B ND2 1 
ATOM   7601  N  N   . ASP B  1 230 ? 4.290   73.292 18.456 1.00 20.22 ? 230  ASP B N   1 
ATOM   7602  C  CA  . ASP B  1 230 ? 5.097   73.188 19.669 1.00 20.81 ? 230  ASP B CA  1 
ATOM   7603  C  C   . ASP B  1 230 ? 6.514   73.698 19.452 1.00 21.81 ? 230  ASP B C   1 
ATOM   7604  O  O   . ASP B  1 230 ? 7.423   73.387 20.238 1.00 20.15 ? 230  ASP B O   1 
ATOM   7605  C  CB  . ASP B  1 230 ? 5.166   71.729 20.124 1.00 20.23 ? 230  ASP B CB  1 
ATOM   7606  C  CG  . ASP B  1 230 ? 3.846   71.224 20.670 1.00 21.86 ? 230  ASP B CG  1 
ATOM   7607  O  OD1 . ASP B  1 230 ? 2.803   71.360 19.991 1.00 23.94 ? 230  ASP B OD1 1 
ATOM   7608  O  OD2 . ASP B  1 230 ? 3.849   70.680 21.783 1.00 21.83 ? 230  ASP B OD2 1 
ATOM   7609  N  N   . THR B  1 231 ? 6.699   74.474 18.389 1.00 22.41 ? 231  THR B N   1 
ATOM   7610  C  CA  . THR B  1 231 ? 8.018   75.009 18.042 1.00 23.29 ? 231  THR B CA  1 
ATOM   7611  C  C   . THR B  1 231 ? 8.866   75.478 19.218 1.00 23.67 ? 231  THR B C   1 
ATOM   7612  O  O   . THR B  1 231 ? 10.049  75.148 19.292 1.00 25.61 ? 231  THR B O   1 
ATOM   7613  C  CB  . THR B  1 231 ? 7.913   76.183 17.039 1.00 23.92 ? 231  THR B CB  1 
ATOM   7614  O  OG1 . THR B  1 231 ? 7.388   75.705 15.788 1.00 24.11 ? 231  THR B OG1 1 
ATOM   7615  C  CG2 . THR B  1 231 ? 9.304   76.808 16.806 1.00 24.54 ? 231  THR B CG2 1 
ATOM   7616  N  N   . GLU B  1 232 ? 8.286   76.232 20.142 1.00 23.27 ? 232  GLU B N   1 
ATOM   7617  C  CA  . GLU B  1 232 ? 9.075   76.731 21.273 1.00 24.15 ? 232  GLU B CA  1 
ATOM   7618  C  C   . GLU B  1 232 ? 8.806   76.038 22.613 1.00 22.67 ? 232  GLU B C   1 
ATOM   7619  O  O   . GLU B  1 232 ? 9.240   76.509 23.656 1.00 21.53 ? 232  GLU B O   1 
ATOM   7620  C  CB  . GLU B  1 232 ? 8.860   78.236 21.397 1.00 27.74 ? 232  GLU B CB  1 
ATOM   7621  C  CG  . GLU B  1 232 ? 9.505   78.999 20.237 1.00 34.93 ? 232  GLU B CG  1 
ATOM   7622  C  CD  . GLU B  1 232 ? 9.117   80.471 20.202 1.00 37.75 ? 232  GLU B CD  1 
ATOM   7623  O  OE1 . GLU B  1 232 ? 7.942   80.791 19.886 1.00 39.42 ? 232  GLU B OE1 1 
ATOM   7624  O  OE2 . GLU B  1 232 ? 9.999   81.301 20.498 1.00 39.74 ? 232  GLU B OE2 1 
ATOM   7625  N  N   . VAL B  1 233 ? 8.088   74.920 22.587 1.00 21.83 ? 233  VAL B N   1 
ATOM   7626  C  CA  . VAL B  1 233 ? 7.827   74.191 23.819 1.00 21.12 ? 233  VAL B CA  1 
ATOM   7627  C  C   . VAL B  1 233 ? 9.064   73.380 24.230 1.00 20.42 ? 233  VAL B C   1 
ATOM   7628  O  O   . VAL B  1 233 ? 9.579   72.587 23.447 1.00 19.75 ? 233  VAL B O   1 
ATOM   7629  C  CB  . VAL B  1 233 ? 6.632   73.246 23.654 1.00 20.95 ? 233  VAL B CB  1 
ATOM   7630  C  CG1 . VAL B  1 233 ? 6.429   72.433 24.931 1.00 20.23 ? 233  VAL B CG1 1 
ATOM   7631  C  CG2 . VAL B  1 233 ? 5.372   74.063 23.317 1.00 19.59 ? 233  VAL B CG2 1 
ATOM   7632  N  N   . PRO B  1 234 ? 9.564   73.587 25.464 1.00 19.51 ? 234  PRO B N   1 
ATOM   7633  C  CA  . PRO B  1 234 ? 10.743  72.855 25.948 1.00 18.95 ? 234  PRO B CA  1 
ATOM   7634  C  C   . PRO B  1 234 ? 10.498  71.338 25.947 1.00 20.53 ? 234  PRO B C   1 
ATOM   7635  O  O   . PRO B  1 234 ? 9.342   70.868 26.059 1.00 19.39 ? 234  PRO B O   1 
ATOM   7636  C  CB  . PRO B  1 234 ? 10.954  73.408 27.366 1.00 18.06 ? 234  PRO B CB  1 
ATOM   7637  C  CG  . PRO B  1 234 ? 10.374  74.817 27.279 1.00 18.80 ? 234  PRO B CG  1 
ATOM   7638  C  CD  . PRO B  1 234 ? 9.116   74.588 26.455 1.00 18.57 ? 234  PRO B CD  1 
ATOM   7639  N  N   . LEU B  1 235 ? 11.588  70.579 25.838 1.00 18.96 ? 235  LEU B N   1 
ATOM   7640  C  CA  . LEU B  1 235 ? 11.507  69.118 25.801 1.00 20.61 ? 235  LEU B CA  1 
ATOM   7641  C  C   . LEU B  1 235 ? 11.889  68.446 27.107 1.00 20.19 ? 235  LEU B C   1 
ATOM   7642  O  O   . LEU B  1 235 ? 12.860  68.836 27.765 1.00 20.48 ? 235  LEU B O   1 
ATOM   7643  C  CB  . LEU B  1 235 ? 12.442  68.571 24.713 1.00 21.35 ? 235  LEU B CB  1 
ATOM   7644  C  CG  . LEU B  1 235 ? 12.230  69.110 23.287 1.00 24.44 ? 235  LEU B CG  1 
ATOM   7645  C  CD1 . LEU B  1 235 ? 13.507  68.913 22.467 1.00 24.40 ? 235  LEU B CD1 1 
ATOM   7646  C  CD2 . LEU B  1 235 ? 11.049  68.391 22.650 1.00 24.36 ? 235  LEU B CD2 1 
ATOM   7647  N  N   . ILE B  1 236 ? 11.118  67.441 27.495 1.00 19.13 ? 236  ILE B N   1 
ATOM   7648  C  CA  . ILE B  1 236 ? 11.491  66.667 28.668 1.00 18.53 ? 236  ILE B CA  1 
ATOM   7649  C  C   . ILE B  1 236 ? 12.326  65.579 27.984 1.00 19.32 ? 236  ILE B C   1 
ATOM   7650  O  O   . ILE B  1 236 ? 11.959  65.085 26.913 1.00 18.66 ? 236  ILE B O   1 
ATOM   7651  C  CB  . ILE B  1 236 ? 10.274  66.012 29.388 1.00 17.08 ? 236  ILE B CB  1 
ATOM   7652  C  CG1 . ILE B  1 236 ? 10.763  65.048 30.463 1.00 17.30 ? 236  ILE B CG1 1 
ATOM   7653  C  CG2 . ILE B  1 236 ? 9.400   65.264 28.395 1.00 17.48 ? 236  ILE B CG2 1 
ATOM   7654  C  CD1 . ILE B  1 236 ? 11.718  65.657 31.495 1.00 13.34 ? 236  ILE B CD1 1 
ATOM   7655  N  N   . GLU B  1 237 ? 13.457  65.237 28.583 1.00 18.39 ? 237  GLU B N   1 
ATOM   7656  C  CA  . GLU B  1 237 ? 14.333  64.219 28.029 1.00 18.32 ? 237  GLU B CA  1 
ATOM   7657  C  C   . GLU B  1 237 ? 14.633  63.190 29.106 1.00 16.13 ? 237  GLU B C   1 
ATOM   7658  O  O   . GLU B  1 237 ? 14.871  63.554 30.248 1.00 14.00 ? 237  GLU B O   1 
ATOM   7659  C  CB  . GLU B  1 237 ? 15.638  64.854 27.556 1.00 19.35 ? 237  GLU B CB  1 
ATOM   7660  C  CG  . GLU B  1 237 ? 15.426  65.988 26.594 1.00 25.34 ? 237  GLU B CG  1 
ATOM   7661  C  CD  . GLU B  1 237 ? 16.735  66.553 26.109 1.00 28.51 ? 237  GLU B CD  1 
ATOM   7662  O  OE1 . GLU B  1 237 ? 17.579  66.917 26.945 1.00 34.79 ? 237  GLU B OE1 1 
ATOM   7663  O  OE2 . GLU B  1 237 ? 16.916  66.642 24.895 1.00 31.69 ? 237  GLU B OE2 1 
ATOM   7664  N  N   . TYR B  1 238 ? 14.594  61.911 28.745 1.00 15.60 ? 238  TYR B N   1 
ATOM   7665  C  CA  . TYR B  1 238 ? 14.887  60.847 29.698 1.00 17.28 ? 238  TYR B CA  1 
ATOM   7666  C  C   . TYR B  1 238 ? 15.336  59.650 28.887 1.00 17.45 ? 238  TYR B C   1 
ATOM   7667  O  O   . TYR B  1 238 ? 15.061  59.573 27.690 1.00 17.66 ? 238  TYR B O   1 
ATOM   7668  C  CB  . TYR B  1 238 ? 13.663  60.509 30.577 1.00 16.29 ? 238  TYR B CB  1 
ATOM   7669  C  CG  . TYR B  1 238 ? 12.402  60.092 29.836 1.00 18.07 ? 238  TYR B CG  1 
ATOM   7670  C  CD1 . TYR B  1 238 ? 11.429  61.027 29.485 1.00 18.84 ? 238  TYR B CD1 1 
ATOM   7671  C  CD2 . TYR B  1 238 ? 12.192  58.763 29.468 1.00 18.98 ? 238  TYR B CD2 1 
ATOM   7672  C  CE1 . TYR B  1 238 ? 10.284  60.653 28.779 1.00 17.38 ? 238  TYR B CE1 1 
ATOM   7673  C  CE2 . TYR B  1 238 ? 11.049  58.372 28.760 1.00 18.34 ? 238  TYR B CE2 1 
ATOM   7674  C  CZ  . TYR B  1 238 ? 10.104  59.327 28.415 1.00 18.86 ? 238  TYR B CZ  1 
ATOM   7675  O  OH  . TYR B  1 238 ? 9.014   58.971 27.656 1.00 17.94 ? 238  TYR B OH  1 
ATOM   7676  N  N   . SER B  1 239 ? 16.039  58.726 29.524 1.00 17.11 ? 239  SER B N   1 
ATOM   7677  C  CA  . SER B  1 239 ? 16.551  57.564 28.810 1.00 17.60 ? 239  SER B CA  1 
ATOM   7678  C  C   . SER B  1 239 ? 15.550  56.425 28.775 1.00 18.87 ? 239  SER B C   1 
ATOM   7679  O  O   . SER B  1 239 ? 14.720  56.288 29.667 1.00 18.94 ? 239  SER B O   1 
ATOM   7680  C  CB  . SER B  1 239 ? 17.832  57.051 29.475 1.00 16.33 ? 239  SER B CB  1 
ATOM   7681  O  OG  . SER B  1 239 ? 18.778  58.081 29.639 1.00 18.37 ? 239  SER B OG  1 
ATOM   7682  N  N   . PHE B  1 240 ? 15.646  55.619 27.725 1.00 19.12 ? 240  PHE B N   1 
ATOM   7683  C  CA  . PHE B  1 240 ? 14.820  54.441 27.564 1.00 19.78 ? 240  PHE B CA  1 
ATOM   7684  C  C   . PHE B  1 240 ? 15.864  53.374 27.249 1.00 20.09 ? 240  PHE B C   1 
ATOM   7685  O  O   . PHE B  1 240 ? 16.600  53.485 26.259 1.00 19.24 ? 240  PHE B O   1 
ATOM   7686  C  CB  . PHE B  1 240 ? 13.853  54.582 26.399 1.00 20.00 ? 240  PHE B CB  1 
ATOM   7687  C  CG  . PHE B  1 240 ? 12.772  53.557 26.417 1.00 21.46 ? 240  PHE B CG  1 
ATOM   7688  C  CD1 . PHE B  1 240 ? 11.664  53.722 27.238 1.00 20.78 ? 240  PHE B CD1 1 
ATOM   7689  C  CD2 . PHE B  1 240 ? 12.882  52.397 25.663 1.00 21.89 ? 240  PHE B CD2 1 
ATOM   7690  C  CE1 . PHE B  1 240 ? 10.684  52.749 27.318 1.00 21.52 ? 240  PHE B CE1 1 
ATOM   7691  C  CE2 . PHE B  1 240 ? 11.897  51.409 25.736 1.00 21.95 ? 240  PHE B CE2 1 
ATOM   7692  C  CZ  . PHE B  1 240 ? 10.801  51.595 26.567 1.00 21.27 ? 240  PHE B CZ  1 
ATOM   7693  N  N   . TYR B  1 241 ? 15.937  52.349 28.091 1.00 19.38 ? 241  TYR B N   1 
ATOM   7694  C  CA  . TYR B  1 241 ? 16.956  51.325 27.914 1.00 18.13 ? 241  TYR B CA  1 
ATOM   7695  C  C   . TYR B  1 241 ? 16.618  50.208 26.951 1.00 18.23 ? 241  TYR B C   1 
ATOM   7696  O  O   . TYR B  1 241 ? 17.519  49.614 26.354 1.00 17.47 ? 241  TYR B O   1 
ATOM   7697  C  CB  . TYR B  1 241 ? 17.356  50.775 29.289 1.00 18.06 ? 241  TYR B CB  1 
ATOM   7698  C  CG  . TYR B  1 241 ? 17.721  51.880 30.245 1.00 15.77 ? 241  TYR B CG  1 
ATOM   7699  C  CD1 . TYR B  1 241 ? 16.748  52.483 31.048 1.00 16.61 ? 241  TYR B CD1 1 
ATOM   7700  C  CD2 . TYR B  1 241 ? 19.014  52.407 30.273 1.00 15.86 ? 241  TYR B CD2 1 
ATOM   7701  C  CE1 . TYR B  1 241 ? 17.048  53.602 31.860 1.00 14.96 ? 241  TYR B CE1 1 
ATOM   7702  C  CE2 . TYR B  1 241 ? 19.331  53.532 31.076 1.00 14.88 ? 241  TYR B CE2 1 
ATOM   7703  C  CZ  . TYR B  1 241 ? 18.341  54.118 31.863 1.00 16.84 ? 241  TYR B CZ  1 
ATOM   7704  O  OH  . TYR B  1 241 ? 18.633  55.222 32.640 1.00 18.72 ? 241  TYR B OH  1 
ATOM   7705  N  N   . SER B  1 242 ? 15.326  49.919 26.793 1.00 19.02 ? 242  SER B N   1 
ATOM   7706  C  CA  . SER B  1 242 ? 14.889  48.879 25.858 1.00 19.90 ? 242  SER B CA  1 
ATOM   7707  C  C   . SER B  1 242 ? 15.471  47.505 26.202 1.00 20.82 ? 242  SER B C   1 
ATOM   7708  O  O   . SER B  1 242 ? 15.999  47.293 27.299 1.00 19.16 ? 242  SER B O   1 
ATOM   7709  C  CB  . SER B  1 242 ? 15.316  49.267 24.442 1.00 21.11 ? 242  SER B CB  1 
ATOM   7710  O  OG  . SER B  1 242 ? 14.772  48.395 23.486 1.00 22.16 ? 242  SER B OG  1 
ATOM   7711  N  N   . ASP B  1 243 ? 15.370  46.574 25.260 1.00 21.88 ? 243  ASP B N   1 
ATOM   7712  C  CA  . ASP B  1 243 ? 15.906  45.240 25.475 1.00 23.74 ? 243  ASP B CA  1 
ATOM   7713  C  C   . ASP B  1 243 ? 17.414  45.302 25.737 1.00 23.51 ? 243  ASP B C   1 
ATOM   7714  O  O   . ASP B  1 243 ? 18.106  46.257 25.361 1.00 20.73 ? 243  ASP B O   1 
ATOM   7715  C  CB  . ASP B  1 243 ? 15.634  44.329 24.272 1.00 28.31 ? 243  ASP B CB  1 
ATOM   7716  C  CG  . ASP B  1 243 ? 14.143  44.183 23.975 1.00 34.27 ? 243  ASP B CG  1 
ATOM   7717  O  OD1 . ASP B  1 243 ? 13.307  44.385 24.896 1.00 34.92 ? 243  ASP B OD1 1 
ATOM   7718  O  OD2 . ASP B  1 243 ? 13.796  43.847 22.815 1.00 37.48 ? 243  ASP B OD2 1 
ATOM   7719  N  N   . GLU B  1 244 ? 17.901  44.253 26.384 1.00 23.13 ? 244  GLU B N   1 
ATOM   7720  C  CA  . GLU B  1 244 ? 19.294  44.116 26.767 1.00 24.13 ? 244  GLU B CA  1 
ATOM   7721  C  C   . GLU B  1 244 ? 20.237  44.240 25.557 1.00 23.74 ? 244  GLU B C   1 
ATOM   7722  O  O   . GLU B  1 244 ? 21.386  44.662 25.695 1.00 21.47 ? 244  GLU B O   1 
ATOM   7723  C  CB  . GLU B  1 244 ? 19.445  42.759 27.447 1.00 25.58 ? 244  GLU B CB  1 
ATOM   7724  C  CG  . GLU B  1 244 ? 20.761  42.470 28.091 1.00 29.78 ? 244  GLU B CG  1 
ATOM   7725  C  CD  . GLU B  1 244 ? 20.896  40.978 28.418 1.00 31.72 ? 244  GLU B CD  1 
ATOM   7726  O  OE1 . GLU B  1 244 ? 19.851  40.345 28.726 1.00 29.73 ? 244  GLU B OE1 1 
ATOM   7727  O  OE2 . GLU B  1 244 ? 22.035  40.459 28.370 1.00 31.61 ? 244  GLU B OE2 1 
ATOM   7728  N  N   . SER B  1 245 ? 19.741  43.879 24.371 1.00 23.23 ? 245  SER B N   1 
ATOM   7729  C  CA  . SER B  1 245 ? 20.552  43.941 23.155 1.00 23.00 ? 245  SER B CA  1 
ATOM   7730  C  C   . SER B  1 245 ? 20.907  45.367 22.718 1.00 23.18 ? 245  SER B C   1 
ATOM   7731  O  O   . SER B  1 245 ? 21.876  45.559 21.999 1.00 23.96 ? 245  SER B O   1 
ATOM   7732  C  CB  . SER B  1 245 ? 19.850  43.212 22.005 1.00 22.89 ? 245  SER B CB  1 
ATOM   7733  O  OG  . SER B  1 245 ? 18.602  43.817 21.697 1.00 23.07 ? 245  SER B OG  1 
ATOM   7734  N  N   . LEU B  1 246 ? 20.137  46.372 23.132 1.00 22.07 ? 246  LEU B N   1 
ATOM   7735  C  CA  . LEU B  1 246 ? 20.468  47.750 22.749 1.00 21.84 ? 246  LEU B CA  1 
ATOM   7736  C  C   . LEU B  1 246 ? 21.729  48.187 23.529 1.00 22.13 ? 246  LEU B C   1 
ATOM   7737  O  O   . LEU B  1 246 ? 21.722  48.269 24.766 1.00 21.16 ? 246  LEU B O   1 
ATOM   7738  C  CB  . LEU B  1 246 ? 19.313  48.695 23.069 1.00 20.41 ? 246  LEU B CB  1 
ATOM   7739  C  CG  . LEU B  1 246 ? 19.530  50.140 22.614 1.00 20.45 ? 246  LEU B CG  1 
ATOM   7740  C  CD1 . LEU B  1 246 ? 19.583  50.176 21.067 1.00 19.23 ? 246  LEU B CD1 1 
ATOM   7741  C  CD2 . LEU B  1 246 ? 18.395  51.025 23.141 1.00 20.50 ? 246  LEU B CD2 1 
ATOM   7742  N  N   . GLN B  1 247 ? 22.800  48.481 22.795 1.00 21.69 ? 247  GLN B N   1 
ATOM   7743  C  CA  . GLN B  1 247 ? 24.071  48.847 23.408 1.00 19.87 ? 247  GLN B CA  1 
ATOM   7744  C  C   . GLN B  1 247 ? 24.079  50.235 24.041 1.00 20.13 ? 247  GLN B C   1 
ATOM   7745  O  O   . GLN B  1 247 ? 24.570  50.407 25.161 1.00 18.70 ? 247  GLN B O   1 
ATOM   7746  C  CB  . GLN B  1 247 ? 25.194  48.727 22.373 1.00 18.45 ? 247  GLN B CB  1 
ATOM   7747  C  CG  . GLN B  1 247 ? 26.576  48.989 22.960 1.00 20.00 ? 247  GLN B CG  1 
ATOM   7748  C  CD  . GLN B  1 247 ? 27.692  48.630 21.999 1.00 20.70 ? 247  GLN B CD  1 
ATOM   7749  O  OE1 . GLN B  1 247 ? 27.638  48.968 20.823 1.00 22.39 ? 247  GLN B OE1 1 
ATOM   7750  N  NE2 . GLN B  1 247 ? 28.710  47.943 22.499 1.00 20.17 ? 247  GLN B NE2 1 
ATOM   7751  N  N   . TYR B  1 248 ? 23.548  51.218 23.319 1.00 18.85 ? 248  TYR B N   1 
ATOM   7752  C  CA  . TYR B  1 248 ? 23.471  52.584 23.819 1.00 19.34 ? 248  TYR B CA  1 
ATOM   7753  C  C   . TYR B  1 248 ? 22.027  52.921 24.169 1.00 20.12 ? 248  TYR B C   1 
ATOM   7754  O  O   . TYR B  1 248 ? 21.118  52.696 23.373 1.00 19.66 ? 248  TYR B O   1 
ATOM   7755  C  CB  . TYR B  1 248 ? 23.986  53.581 22.760 1.00 20.80 ? 248  TYR B CB  1 
ATOM   7756  C  CG  . TYR B  1 248 ? 25.506  53.635 22.641 1.00 20.85 ? 248  TYR B CG  1 
ATOM   7757  C  CD1 . TYR B  1 248 ? 26.261  54.520 23.430 1.00 19.36 ? 248  TYR B CD1 1 
ATOM   7758  C  CD2 . TYR B  1 248 ? 26.190  52.784 21.759 1.00 19.48 ? 248  TYR B CD2 1 
ATOM   7759  C  CE1 . TYR B  1 248 ? 27.662  54.558 23.338 1.00 19.13 ? 248  TYR B CE1 1 
ATOM   7760  C  CE2 . TYR B  1 248 ? 27.594  52.809 21.664 1.00 20.13 ? 248  TYR B CE2 1 
ATOM   7761  C  CZ  . TYR B  1 248 ? 28.320  53.702 22.456 1.00 20.28 ? 248  TYR B CZ  1 
ATOM   7762  O  OH  . TYR B  1 248 ? 29.696  53.748 22.360 1.00 20.61 ? 248  TYR B OH  1 
ATOM   7763  N  N   . PRO B  1 249 ? 21.794  53.464 25.372 1.00 20.39 ? 249  PRO B N   1 
ATOM   7764  C  CA  . PRO B  1 249 ? 20.435  53.817 25.774 1.00 19.92 ? 249  PRO B CA  1 
ATOM   7765  C  C   . PRO B  1 249 ? 19.893  54.869 24.823 1.00 21.21 ? 249  PRO B C   1 
ATOM   7766  O  O   . PRO B  1 249 ? 20.646  55.673 24.289 1.00 19.69 ? 249  PRO B O   1 
ATOM   7767  C  CB  . PRO B  1 249 ? 20.625  54.374 27.181 1.00 19.30 ? 249  PRO B CB  1 
ATOM   7768  C  CG  . PRO B  1 249 ? 21.852  53.664 27.667 1.00 20.47 ? 249  PRO B CG  1 
ATOM   7769  C  CD  . PRO B  1 249 ? 22.749  53.725 26.461 1.00 19.81 ? 249  PRO B CD  1 
ATOM   7770  N  N   . LYS B  1 250 ? 18.578  54.879 24.651 1.00 22.39 ? 250  LYS B N   1 
ATOM   7771  C  CA  . LYS B  1 250 ? 17.923  55.830 23.777 1.00 24.16 ? 250  LYS B CA  1 
ATOM   7772  C  C   . LYS B  1 250 ? 17.416  57.015 24.608 1.00 24.53 ? 250  LYS B C   1 
ATOM   7773  O  O   . LYS B  1 250 ? 16.957  56.838 25.744 1.00 24.58 ? 250  LYS B O   1 
ATOM   7774  C  CB  . LYS B  1 250 ? 16.765  55.119 23.071 1.00 28.65 ? 250  LYS B CB  1 
ATOM   7775  C  CG  . LYS B  1 250 ? 15.910  55.972 22.157 1.00 33.83 ? 250  LYS B CG  1 
ATOM   7776  C  CD  . LYS B  1 250 ? 14.956  55.094 21.344 1.00 37.44 ? 250  LYS B CD  1 
ATOM   7777  C  CE  . LYS B  1 250 ? 14.084  55.931 20.397 1.00 41.66 ? 250  LYS B CE  1 
ATOM   7778  N  NZ  . LYS B  1 250 ? 13.048  56.772 21.097 1.00 43.47 ? 250  LYS B NZ  1 
ATOM   7779  N  N   . THR B  1 251 ? 17.528  58.227 24.070 1.00 22.30 ? 251  THR B N   1 
ATOM   7780  C  CA  . THR B  1 251 ? 17.036  59.388 24.790 1.00 21.33 ? 251  THR B CA  1 
ATOM   7781  C  C   . THR B  1 251 ? 15.683  59.801 24.230 1.00 21.55 ? 251  THR B C   1 
ATOM   7782  O  O   . THR B  1 251 ? 15.597  60.258 23.097 1.00 20.57 ? 251  THR B O   1 
ATOM   7783  C  CB  . THR B  1 251 ? 17.973  60.608 24.670 1.00 20.08 ? 251  THR B CB  1 
ATOM   7784  O  OG1 . THR B  1 251 ? 19.223  60.318 25.297 1.00 19.86 ? 251  THR B OG1 1 
ATOM   7785  C  CG2 . THR B  1 251 ? 17.358  61.825 25.385 1.00 19.32 ? 251  THR B CG2 1 
ATOM   7786  N  N   . VAL B  1 252 ? 14.630  59.634 25.023 1.00 20.61 ? 252  VAL B N   1 
ATOM   7787  C  CA  . VAL B  1 252 ? 13.307  60.034 24.575 1.00 19.56 ? 252  VAL B CA  1 
ATOM   7788  C  C   . VAL B  1 252 ? 13.145  61.543 24.787 1.00 20.10 ? 252  VAL B C   1 
ATOM   7789  O  O   . VAL B  1 252 ? 13.484  62.081 25.847 1.00 18.92 ? 252  VAL B O   1 
ATOM   7790  C  CB  . VAL B  1 252 ? 12.223  59.241 25.324 1.00 19.90 ? 252  VAL B CB  1 
ATOM   7791  C  CG1 . VAL B  1 252 ? 10.826  59.766 24.950 1.00 17.96 ? 252  VAL B CG1 1 
ATOM   7792  C  CG2 . VAL B  1 252 ? 12.370  57.749 24.968 1.00 17.06 ? 252  VAL B CG2 1 
ATOM   7793  N  N   . ARG B  1 253 ? 12.653  62.224 23.756 1.00 20.29 ? 253  ARG B N   1 
ATOM   7794  C  CA  . ARG B  1 253 ? 12.471  63.677 23.797 1.00 21.16 ? 253  ARG B CA  1 
ATOM   7795  C  C   . ARG B  1 253 ? 11.050  64.054 23.431 1.00 20.16 ? 253  ARG B C   1 
ATOM   7796  O  O   . ARG B  1 253 ? 10.610  63.817 22.315 1.00 20.83 ? 253  ARG B O   1 
ATOM   7797  C  CB  . ARG B  1 253 ? 13.445  64.357 22.829 1.00 23.51 ? 253  ARG B CB  1 
ATOM   7798  C  CG  . ARG B  1 253 ? 14.907  64.002 23.072 1.00 27.89 ? 253  ARG B CG  1 
ATOM   7799  C  CD  . ARG B  1 253 ? 15.833  64.882 22.251 1.00 32.63 ? 253  ARG B CD  1 
ATOM   7800  N  NE  . ARG B  1 253 ? 17.081  64.185 21.969 1.00 37.96 ? 253  ARG B NE  1 
ATOM   7801  C  CZ  . ARG B  1 253 ? 18.009  63.918 22.881 1.00 39.63 ? 253  ARG B CZ  1 
ATOM   7802  N  NH1 . ARG B  1 253 ? 17.816  64.306 24.136 1.00 42.53 ? 253  ARG B NH1 1 
ATOM   7803  N  NH2 . ARG B  1 253 ? 19.119  63.259 22.548 1.00 38.58 ? 253  ARG B NH2 1 
ATOM   7804  N  N   . VAL B  1 254 ? 10.351  64.685 24.360 1.00 18.51 ? 254  VAL B N   1 
ATOM   7805  C  CA  . VAL B  1 254 ? 8.955   65.039 24.146 1.00 19.05 ? 254  VAL B CA  1 
ATOM   7806  C  C   . VAL B  1 254 ? 8.620   66.494 24.464 1.00 17.26 ? 254  VAL B C   1 
ATOM   7807  O  O   . VAL B  1 254 ? 8.938   66.982 25.544 1.00 19.40 ? 254  VAL B O   1 
ATOM   7808  C  CB  . VAL B  1 254 ? 8.018   64.164 25.051 1.00 18.64 ? 254  VAL B CB  1 
ATOM   7809  C  CG1 . VAL B  1 254 ? 6.552   64.486 24.765 1.00 17.80 ? 254  VAL B CG1 1 
ATOM   7810  C  CG2 . VAL B  1 254 ? 8.312   62.673 24.844 1.00 19.79 ? 254  VAL B CG2 1 
ATOM   7811  N  N   . PRO B  1 255 ? 8.000   67.205 23.518 1.00 14.62 ? 255  PRO B N   1 
ATOM   7812  C  CA  . PRO B  1 255 ? 7.620   68.600 23.758 1.00 16.23 ? 255  PRO B CA  1 
ATOM   7813  C  C   . PRO B  1 255 ? 6.603   68.515 24.905 1.00 16.25 ? 255  PRO B C   1 
ATOM   7814  O  O   . PRO B  1 255 ? 5.514   67.942 24.756 1.00 16.45 ? 255  PRO B O   1 
ATOM   7815  C  CB  . PRO B  1 255 ? 6.969   69.011 22.440 1.00 17.04 ? 255  PRO B CB  1 
ATOM   7816  C  CG  . PRO B  1 255 ? 7.708   68.171 21.436 1.00 15.65 ? 255  PRO B CG  1 
ATOM   7817  C  CD  . PRO B  1 255 ? 7.832   66.839 22.105 1.00 14.15 ? 255  PRO B CD  1 
ATOM   7818  N  N   . TYR B  1 256 ? 6.978   69.085 26.035 1.00 15.41 ? 256  TYR B N   1 
ATOM   7819  C  CA  . TYR B  1 256 ? 6.190   69.032 27.243 1.00 15.05 ? 256  TYR B CA  1 
ATOM   7820  C  C   . TYR B  1 256 ? 6.349   70.340 28.000 1.00 14.82 ? 256  TYR B C   1 
ATOM   7821  O  O   . TYR B  1 256 ? 7.419   70.635 28.522 1.00 15.44 ? 256  TYR B O   1 
ATOM   7822  C  CB  . TYR B  1 256 ? 6.721   67.862 28.097 1.00 14.92 ? 256  TYR B CB  1 
ATOM   7823  C  CG  . TYR B  1 256 ? 5.977   67.565 29.380 1.00 16.13 ? 256  TYR B CG  1 
ATOM   7824  C  CD1 . TYR B  1 256 ? 5.961   68.483 30.434 1.00 15.80 ? 256  TYR B CD1 1 
ATOM   7825  C  CD2 . TYR B  1 256 ? 5.322   66.349 29.557 1.00 14.33 ? 256  TYR B CD2 1 
ATOM   7826  C  CE1 . TYR B  1 256 ? 5.318   68.192 31.635 1.00 16.01 ? 256  TYR B CE1 1 
ATOM   7827  C  CE2 . TYR B  1 256 ? 4.667   66.048 30.750 1.00 15.98 ? 256  TYR B CE2 1 
ATOM   7828  C  CZ  . TYR B  1 256 ? 4.666   66.964 31.780 1.00 16.17 ? 256  TYR B CZ  1 
ATOM   7829  O  OH  . TYR B  1 256 ? 3.990   66.695 32.940 1.00 17.38 ? 256  TYR B OH  1 
ATOM   7830  N  N   . PRO B  1 257 ? 5.282   71.146 28.075 1.00 14.46 ? 257  PRO B N   1 
ATOM   7831  C  CA  . PRO B  1 257 ? 5.363   72.425 28.797 1.00 15.37 ? 257  PRO B CA  1 
ATOM   7832  C  C   . PRO B  1 257 ? 5.149   72.288 30.316 1.00 15.23 ? 257  PRO B C   1 
ATOM   7833  O  O   . PRO B  1 257 ? 4.046   71.965 30.758 1.00 14.97 ? 257  PRO B O   1 
ATOM   7834  C  CB  . PRO B  1 257 ? 4.255   73.263 28.142 1.00 15.66 ? 257  PRO B CB  1 
ATOM   7835  C  CG  . PRO B  1 257 ? 3.165   72.207 27.858 1.00 13.38 ? 257  PRO B CG  1 
ATOM   7836  C  CD  . PRO B  1 257 ? 3.978   70.981 27.399 1.00 13.77 ? 257  PRO B CD  1 
ATOM   7837  N  N   . LYS B  1 258 ? 6.200   72.513 31.108 1.00 15.62 ? 258  LYS B N   1 
ATOM   7838  C  CA  . LYS B  1 258 ? 6.065   72.447 32.560 1.00 16.32 ? 258  LYS B CA  1 
ATOM   7839  C  C   . LYS B  1 258 ? 5.387   73.761 33.018 1.00 17.90 ? 258  LYS B C   1 
ATOM   7840  O  O   . LYS B  1 258 ? 5.236   74.695 32.214 1.00 18.61 ? 258  LYS B O   1 
ATOM   7841  C  CB  . LYS B  1 258 ? 7.446   72.244 33.201 1.00 16.43 ? 258  LYS B CB  1 
ATOM   7842  C  CG  . LYS B  1 258 ? 7.941   70.774 33.101 1.00 16.50 ? 258  LYS B CG  1 
ATOM   7843  C  CD  . LYS B  1 258 ? 9.410   70.596 33.455 1.00 15.01 ? 258  LYS B CD  1 
ATOM   7844  C  CE  . LYS B  1 258 ? 9.848   69.129 33.338 1.00 14.63 ? 258  LYS B CE  1 
ATOM   7845  N  NZ  . LYS B  1 258 ? 9.231   68.214 34.345 1.00 14.72 ? 258  LYS B NZ  1 
ATOM   7846  N  N   . ALA B  1 259 ? 4.958   73.846 34.278 1.00 16.44 ? 259  ALA B N   1 
ATOM   7847  C  CA  . ALA B  1 259 ? 4.268   75.054 34.747 1.00 17.51 ? 259  ALA B CA  1 
ATOM   7848  C  C   . ALA B  1 259 ? 5.004   76.361 34.456 1.00 17.12 ? 259  ALA B C   1 
ATOM   7849  O  O   . ALA B  1 259 ? 6.173   76.512 34.787 1.00 17.78 ? 259  ALA B O   1 
ATOM   7850  C  CB  . ALA B  1 259 ? 3.963   74.944 36.244 1.00 17.02 ? 259  ALA B CB  1 
ATOM   7851  N  N   . GLY B  1 260 ? 4.305   77.301 33.831 1.00 17.98 ? 260  GLY B N   1 
ATOM   7852  C  CA  . GLY B  1 260 ? 4.892   78.591 33.510 1.00 16.67 ? 260  GLY B CA  1 
ATOM   7853  C  C   . GLY B  1 260 ? 5.771   78.640 32.273 1.00 18.79 ? 260  GLY B C   1 
ATOM   7854  O  O   . GLY B  1 260 ? 6.296   79.707 31.955 1.00 19.66 ? 260  GLY B O   1 
ATOM   7855  N  N   . ALA B  1 261 ? 5.940   77.516 31.572 1.00 18.62 ? 261  ALA B N   1 
ATOM   7856  C  CA  . ALA B  1 261 ? 6.787   77.473 30.370 1.00 19.28 ? 261  ALA B CA  1 
ATOM   7857  C  C   . ALA B  1 261 ? 6.044   77.851 29.078 1.00 19.56 ? 261  ALA B C   1 
ATOM   7858  O  O   . ALA B  1 261 ? 4.845   78.108 29.099 1.00 20.36 ? 261  ALA B O   1 
ATOM   7859  C  CB  . ALA B  1 261 ? 7.399   76.083 30.218 1.00 19.03 ? 261  ALA B CB  1 
ATOM   7860  N  N   . VAL B  1 262 ? 6.753   77.879 27.951 1.00 19.58 ? 262  VAL B N   1 
ATOM   7861  C  CA  . VAL B  1 262 ? 6.099   78.227 26.696 1.00 19.08 ? 262  VAL B CA  1 
ATOM   7862  C  C   . VAL B  1 262 ? 5.154   77.105 26.276 1.00 18.96 ? 262  VAL B C   1 
ATOM   7863  O  O   . VAL B  1 262 ? 5.560   75.950 26.144 1.00 18.40 ? 262  VAL B O   1 
ATOM   7864  C  CB  . VAL B  1 262 ? 7.117   78.487 25.554 1.00 19.51 ? 262  VAL B CB  1 
ATOM   7865  C  CG1 . VAL B  1 262 ? 6.372   78.684 24.240 1.00 17.73 ? 262  VAL B CG1 1 
ATOM   7866  C  CG2 . VAL B  1 262 ? 7.950   79.755 25.854 1.00 17.05 ? 262  VAL B CG2 1 
ATOM   7867  N  N   . ASN B  1 263 ? 3.887   77.457 26.076 1.00 18.46 ? 263  ASN B N   1 
ATOM   7868  C  CA  . ASN B  1 263 ? 2.866   76.503 25.659 1.00 18.12 ? 263  ASN B CA  1 
ATOM   7869  C  C   . ASN B  1 263 ? 2.783   76.402 24.145 1.00 18.98 ? 263  ASN B C   1 
ATOM   7870  O  O   . ASN B  1 263 ? 3.257   77.279 23.427 1.00 18.90 ? 263  ASN B O   1 
ATOM   7871  C  CB  . ASN B  1 263 ? 1.486   76.935 26.164 1.00 18.29 ? 263  ASN B CB  1 
ATOM   7872  C  CG  . ASN B  1 263 ? 1.164   76.407 27.557 1.00 19.00 ? 263  ASN B CG  1 
ATOM   7873  O  OD1 . ASN B  1 263 ? 1.870   75.553 28.086 1.00 19.55 ? 263  ASN B OD1 1 
ATOM   7874  N  ND2 . ASN B  1 263 ? 0.073   76.909 28.149 1.00 18.52 ? 263  ASN B ND2 1 
ATOM   7875  N  N   . PRO B  1 264 ? 2.193   75.312 23.635 1.00 18.85 ? 264  PRO B N   1 
ATOM   7876  C  CA  . PRO B  1 264 ? 2.067   75.184 22.189 1.00 18.27 ? 264  PRO B CA  1 
ATOM   7877  C  C   . PRO B  1 264 ? 0.919   76.127 21.827 1.00 18.85 ? 264  PRO B C   1 
ATOM   7878  O  O   . PRO B  1 264 ? 0.100   76.470 22.687 1.00 18.17 ? 264  PRO B O   1 
ATOM   7879  C  CB  . PRO B  1 264 ? 1.655   73.733 22.012 1.00 18.71 ? 264  PRO B CB  1 
ATOM   7880  C  CG  . PRO B  1 264 ? 0.798   73.503 23.214 1.00 18.23 ? 264  PRO B CG  1 
ATOM   7881  C  CD  . PRO B  1 264 ? 1.648   74.118 24.307 1.00 19.38 ? 264  PRO B CD  1 
ATOM   7882  N  N   . THR B  1 265 ? 0.865   76.568 20.579 1.00 18.39 ? 265  THR B N   1 
ATOM   7883  C  CA  . THR B  1 265 ? -0.212  77.449 20.160 1.00 17.31 ? 265  THR B CA  1 
ATOM   7884  C  C   . THR B  1 265 ? -1.085  76.570 19.302 1.00 18.46 ? 265  THR B C   1 
ATOM   7885  O  O   . THR B  1 265 ? -0.669  75.477 18.927 1.00 18.69 ? 265  THR B O   1 
ATOM   7886  C  CB  . THR B  1 265 ? 0.301   78.641 19.333 1.00 16.85 ? 265  THR B CB  1 
ATOM   7887  O  OG1 . THR B  1 265 ? 1.064   78.150 18.220 1.00 14.71 ? 265  THR B OG1 1 
ATOM   7888  C  CG2 . THR B  1 265 ? 1.159   79.589 20.218 1.00 13.07 ? 265  THR B CG2 1 
ATOM   7889  N  N   . VAL B  1 266 ? -2.279  77.052 18.975 1.00 17.81 ? 266  VAL B N   1 
ATOM   7890  C  CA  . VAL B  1 266 ? -3.220  76.270 18.210 1.00 17.39 ? 266  VAL B CA  1 
ATOM   7891  C  C   . VAL B  1 266 ? -4.037  77.067 17.212 1.00 18.91 ? 266  VAL B C   1 
ATOM   7892  O  O   . VAL B  1 266 ? -4.310  78.256 17.422 1.00 19.22 ? 266  VAL B O   1 
ATOM   7893  C  CB  . VAL B  1 266 ? -4.207  75.582 19.170 1.00 17.74 ? 266  VAL B CB  1 
ATOM   7894  C  CG1 . VAL B  1 266 ? -4.932  76.665 20.009 1.00 16.49 ? 266  VAL B CG1 1 
ATOM   7895  C  CG2 . VAL B  1 266 ? -5.201  74.733 18.390 1.00 15.78 ? 266  VAL B CG2 1 
ATOM   7896  N  N   . LYS B  1 267 ? -4.438  76.391 16.134 1.00 19.04 ? 267  LYS B N   1 
ATOM   7897  C  CA  . LYS B  1 267 ? -5.283  76.974 15.092 1.00 19.29 ? 267  LYS B CA  1 
ATOM   7898  C  C   . LYS B  1 267 ? -6.341  75.936 14.722 1.00 20.31 ? 267  LYS B C   1 
ATOM   7899  O  O   . LYS B  1 267 ? -6.116  74.734 14.867 1.00 20.76 ? 267  LYS B O   1 
ATOM   7900  C  CB  . LYS B  1 267 ? -4.460  77.340 13.863 1.00 20.23 ? 267  LYS B CB  1 
ATOM   7901  C  CG  . LYS B  1 267 ? -3.482  78.498 14.070 1.00 22.22 ? 267  LYS B CG  1 
ATOM   7902  C  CD  . LYS B  1 267 ? -2.704  78.731 12.778 1.00 22.93 ? 267  LYS B CD  1 
ATOM   7903  C  CE  . LYS B  1 267 ? -1.724  79.888 12.880 1.00 23.32 ? 267  LYS B CE  1 
ATOM   7904  N  NZ  . LYS B  1 267 ? -1.099  80.083 11.530 1.00 26.18 ? 267  LYS B NZ  1 
ATOM   7905  N  N   . PHE B  1 268 ? -7.491  76.407 14.243 1.00 19.34 ? 268  PHE B N   1 
ATOM   7906  C  CA  . PHE B  1 268 ? -8.610  75.540 13.896 1.00 18.85 ? 268  PHE B CA  1 
ATOM   7907  C  C   . PHE B  1 268 ? -9.000  75.743 12.445 1.00 18.80 ? 268  PHE B C   1 
ATOM   7908  O  O   . PHE B  1 268 ? -9.060  76.880 11.980 1.00 17.76 ? 268  PHE B O   1 
ATOM   7909  C  CB  . PHE B  1 268 ? -9.815  75.878 14.775 1.00 18.83 ? 268  PHE B CB  1 
ATOM   7910  C  CG  . PHE B  1 268 ? -10.919 74.878 14.687 1.00 20.91 ? 268  PHE B CG  1 
ATOM   7911  C  CD1 . PHE B  1 268 ? -10.803 73.640 15.329 1.00 18.88 ? 268  PHE B CD1 1 
ATOM   7912  C  CD2 . PHE B  1 268 ? -12.078 75.156 13.959 1.00 20.00 ? 268  PHE B CD2 1 
ATOM   7913  C  CE1 . PHE B  1 268 ? -11.820 72.708 15.247 1.00 19.16 ? 268  PHE B CE1 1 
ATOM   7914  C  CE2 . PHE B  1 268 ? -13.100 74.214 13.876 1.00 20.18 ? 268  PHE B CE2 1 
ATOM   7915  C  CZ  . PHE B  1 268 ? -12.974 72.992 14.521 1.00 18.68 ? 268  PHE B CZ  1 
ATOM   7916  N  N   . PHE B  1 269 ? -9.281  74.644 11.741 1.00 17.93 ? 269  PHE B N   1 
ATOM   7917  C  CA  . PHE B  1 269 ? -9.654  74.712 10.334 1.00 18.35 ? 269  PHE B CA  1 
ATOM   7918  C  C   . PHE B  1 269 ? -10.813 73.778 9.977  1.00 18.18 ? 269  PHE B C   1 
ATOM   7919  O  O   . PHE B  1 269 ? -11.064 72.792 10.656 1.00 18.87 ? 269  PHE B O   1 
ATOM   7920  C  CB  . PHE B  1 269 ? -8.463  74.318 9.436  1.00 19.61 ? 269  PHE B CB  1 
ATOM   7921  C  CG  . PHE B  1 269 ? -7.207  75.146 9.637  1.00 19.81 ? 269  PHE B CG  1 
ATOM   7922  C  CD1 . PHE B  1 269 ? -6.281  74.815 10.624 1.00 19.36 ? 269  PHE B CD1 1 
ATOM   7923  C  CD2 . PHE B  1 269 ? -6.931  76.216 8.790  1.00 18.95 ? 269  PHE B CD2 1 
ATOM   7924  C  CE1 . PHE B  1 269 ? -5.089  75.541 10.766 1.00 20.64 ? 269  PHE B CE1 1 
ATOM   7925  C  CE2 . PHE B  1 269 ? -5.747  76.950 8.921  1.00 21.73 ? 269  PHE B CE2 1 
ATOM   7926  C  CZ  . PHE B  1 269 ? -4.818  76.611 9.911  1.00 22.33 ? 269  PHE B CZ  1 
ATOM   7927  N  N   . VAL B  1 270 ? -11.495 74.090 8.885  1.00 18.74 ? 270  VAL B N   1 
ATOM   7928  C  CA  . VAL B  1 270 ? -12.570 73.258 8.379  1.00 18.69 ? 270  VAL B CA  1 
ATOM   7929  C  C   . VAL B  1 270 ? -12.397 73.134 6.855  1.00 19.34 ? 270  VAL B C   1 
ATOM   7930  O  O   . VAL B  1 270 ? -12.262 74.154 6.157  1.00 19.05 ? 270  VAL B O   1 
ATOM   7931  C  CB  . VAL B  1 270 ? -13.954 73.865 8.637  1.00 18.76 ? 270  VAL B CB  1 
ATOM   7932  C  CG1 . VAL B  1 270 ? -15.018 72.865 8.202  1.00 17.79 ? 270  VAL B CG1 1 
ATOM   7933  C  CG2 . VAL B  1 270 ? -14.123 74.213 10.105 1.00 18.97 ? 270  VAL B CG2 1 
ATOM   7934  N  N   . VAL B  1 271 ? -12.386 71.900 6.342  1.00 18.03 ? 271  VAL B N   1 
ATOM   7935  C  CA  . VAL B  1 271 ? -12.271 71.687 4.901  1.00 17.96 ? 271  VAL B CA  1 
ATOM   7936  C  C   . VAL B  1 271 ? -13.515 70.962 4.412  1.00 18.17 ? 271  VAL B C   1 
ATOM   7937  O  O   . VAL B  1 271 ? -14.096 70.152 5.137  1.00 18.50 ? 271  VAL B O   1 
ATOM   7938  C  CB  . VAL B  1 271 ? -11.013 70.846 4.504  1.00 17.67 ? 271  VAL B CB  1 
ATOM   7939  C  CG1 . VAL B  1 271 ? -11.094 69.428 5.089  1.00 17.61 ? 271  VAL B CG1 1 
ATOM   7940  C  CG2 . VAL B  1 271 ? -10.894 70.780 2.991  1.00 16.32 ? 271  VAL B CG2 1 
ATOM   7941  N  N   . ASN B  1 272 ? -13.928 71.265 3.185  1.00 18.28 ? 272  ASN B N   1 
ATOM   7942  C  CA  . ASN B  1 272 ? -15.113 70.637 2.586  1.00 18.83 ? 272  ASN B CA  1 
ATOM   7943  C  C   . ASN B  1 272 ? -14.639 69.431 1.785  1.00 19.42 ? 272  ASN B C   1 
ATOM   7944  O  O   . ASN B  1 272 ? -14.125 69.592 0.659  1.00 20.34 ? 272  ASN B O   1 
ATOM   7945  C  CB  . ASN B  1 272 ? -15.826 71.641 1.665  1.00 18.25 ? 272  ASN B CB  1 
ATOM   7946  C  CG  . ASN B  1 272 ? -17.078 71.068 1.001  1.00 19.84 ? 272  ASN B CG  1 
ATOM   7947  O  OD1 . ASN B  1 272 ? -17.968 71.823 0.633  1.00 21.65 ? 272  ASN B OD1 1 
ATOM   7948  N  ND2 . ASN B  1 272 ? -17.146 69.749 0.833  1.00 16.02 ? 272  ASN B ND2 1 
ATOM   7949  N  N   . THR B  1 273 ? -14.793 68.235 2.359  1.00 18.84 ? 273  THR B N   1 
ATOM   7950  C  CA  . THR B  1 273 ? -14.362 67.004 1.693  1.00 19.31 ? 273  THR B CA  1 
ATOM   7951  C  C   . THR B  1 273 ? -15.134 66.676 0.429  1.00 20.51 ? 273  THR B C   1 
ATOM   7952  O  O   . THR B  1 273 ? -14.618 65.962 -0.432 1.00 18.66 ? 273  THR B O   1 
ATOM   7953  C  CB  . THR B  1 273 ? -14.441 65.740 2.612  1.00 19.67 ? 273  THR B CB  1 
ATOM   7954  O  OG1 . THR B  1 273 ? -15.812 65.429 2.909  1.00 20.09 ? 273  THR B OG1 1 
ATOM   7955  C  CG2 . THR B  1 273 ? -13.666 65.970 3.913  1.00 19.83 ? 273  THR B CG2 1 
ATOM   7956  N  N   . ASP B  1 274 ? -16.374 67.157 0.314  1.00 21.73 ? 274  ASP B N   1 
ATOM   7957  C  CA  . ASP B  1 274 ? -17.152 66.872 -0.900 1.00 23.50 ? 274  ASP B CA  1 
ATOM   7958  C  C   . ASP B  1 274 ? -16.559 67.572 -2.114 1.00 23.72 ? 274  ASP B C   1 
ATOM   7959  O  O   . ASP B  1 274 ? -16.895 67.239 -3.245 1.00 23.33 ? 274  ASP B O   1 
ATOM   7960  C  CB  . ASP B  1 274 ? -18.607 67.307 -0.755 1.00 24.63 ? 274  ASP B CB  1 
ATOM   7961  C  CG  . ASP B  1 274 ? -19.434 66.313 0.019  1.00 25.98 ? 274  ASP B CG  1 
ATOM   7962  O  OD1 . ASP B  1 274 ? -19.033 65.135 0.130  1.00 26.12 ? 274  ASP B OD1 1 
ATOM   7963  O  OD2 . ASP B  1 274 ? -20.502 66.714 0.514  1.00 29.66 ? 274  ASP B OD2 1 
ATOM   7964  N  N   . SER B  1 275 ? -15.667 68.530 -1.883 1.00 24.04 ? 275  SER B N   1 
ATOM   7965  C  CA  . SER B  1 275 ? -15.058 69.243 -2.999 1.00 26.40 ? 275  SER B CA  1 
ATOM   7966  C  C   . SER B  1 275 ? -13.688 68.698 -3.395 1.00 25.87 ? 275  SER B C   1 
ATOM   7967  O  O   . SER B  1 275 ? -13.112 69.142 -4.388 1.00 26.89 ? 275  SER B O   1 
ATOM   7968  C  CB  . SER B  1 275 ? -14.921 70.733 -2.678 1.00 26.90 ? 275  SER B CB  1 
ATOM   7969  O  OG  . SER B  1 275 ? -13.812 70.964 -1.828 1.00 29.32 ? 275  SER B OG  1 
ATOM   7970  N  N   . LEU B  1 276 ? -13.181 67.728 -2.642 1.00 23.97 ? 276  LEU B N   1 
ATOM   7971  C  CA  . LEU B  1 276 ? -11.854 67.170 -2.907 1.00 25.26 ? 276  LEU B CA  1 
ATOM   7972  C  C   . LEU B  1 276 ? -11.616 66.608 -4.313 1.00 25.99 ? 276  LEU B C   1 
ATOM   7973  O  O   . LEU B  1 276 ? -10.525 66.759 -4.863 1.00 27.60 ? 276  LEU B O   1 
ATOM   7974  C  CB  . LEU B  1 276 ? -11.514 66.081 -1.882 1.00 23.74 ? 276  LEU B CB  1 
ATOM   7975  C  CG  . LEU B  1 276 ? -11.315 66.511 -0.429 1.00 23.88 ? 276  LEU B CG  1 
ATOM   7976  C  CD1 . LEU B  1 276 ? -11.147 65.267 0.453  1.00 22.67 ? 276  LEU B CD1 1 
ATOM   7977  C  CD2 . LEU B  1 276 ? -10.080 67.429 -0.318 1.00 23.79 ? 276  LEU B CD2 1 
ATOM   7978  N  N   . SER B  1 277 ? -12.611 65.953 -4.893 1.00 25.73 ? 277  SER B N   1 
ATOM   7979  C  CA  . SER B  1 277 ? -12.417 65.385 -6.213 1.00 26.52 ? 277  SER B CA  1 
ATOM   7980  C  C   . SER B  1 277 ? -12.714 66.388 -7.319 1.00 27.18 ? 277  SER B C   1 
ATOM   7981  O  O   . SER B  1 277 ? -12.678 66.032 -8.493 1.00 27.99 ? 277  SER B O   1 
ATOM   7982  C  CB  . SER B  1 277 ? -13.295 64.138 -6.388 1.00 25.59 ? 277  SER B CB  1 
ATOM   7983  O  OG  . SER B  1 277 ? -14.669 64.476 -6.307 1.00 25.67 ? 277  SER B OG  1 
ATOM   7984  N  N   . SER B  1 278 ? -13.001 67.637 -6.947 1.00 27.23 ? 278  SER B N   1 
ATOM   7985  C  CA  . SER B  1 278 ? -13.312 68.682 -7.931 1.00 26.83 ? 278  SER B CA  1 
ATOM   7986  C  C   . SER B  1 278 ? -12.265 69.781 -8.039 1.00 25.68 ? 278  SER B C   1 
ATOM   7987  O  O   . SER B  1 278 ? -12.235 70.521 -9.028 1.00 24.54 ? 278  SER B O   1 
ATOM   7988  C  CB  . SER B  1 278 ? -14.659 69.335 -7.621 1.00 26.89 ? 278  SER B CB  1 
ATOM   7989  O  OG  . SER B  1 278 ? -15.689 68.398 -7.800 1.00 30.47 ? 278  SER B OG  1 
ATOM   7990  N  N   . VAL B  1 279 ? -11.434 69.911 -7.012 1.00 24.51 ? 279  VAL B N   1 
ATOM   7991  C  CA  . VAL B  1 279 ? -10.389 70.917 -7.019 1.00 24.43 ? 279  VAL B CA  1 
ATOM   7992  C  C   . VAL B  1 279 ? -9.075  70.224 -6.695 1.00 24.84 ? 279  VAL B C   1 
ATOM   7993  O  O   . VAL B  1 279 ? -9.056  69.213 -5.984 1.00 23.97 ? 279  VAL B O   1 
ATOM   7994  C  CB  . VAL B  1 279 ? -10.675 72.032 -5.997 1.00 25.20 ? 279  VAL B CB  1 
ATOM   7995  C  CG1 . VAL B  1 279 ? -11.969 72.752 -6.376 1.00 24.51 ? 279  VAL B CG1 1 
ATOM   7996  C  CG2 . VAL B  1 279 ? -10.766 71.448 -4.600 1.00 24.27 ? 279  VAL B CG2 1 
ATOM   7997  N  N   . THR B  1 280 ? -7.976  70.753 -7.225 1.00 24.80 ? 280  THR B N   1 
ATOM   7998  C  CA  . THR B  1 280 ? -6.683  70.122 -6.997 1.00 26.10 ? 280  THR B CA  1 
ATOM   7999  C  C   . THR B  1 280 ? -6.260  70.186 -5.536 1.00 25.25 ? 280  THR B C   1 
ATOM   8000  O  O   . THR B  1 280 ? -5.721  69.224 -4.997 1.00 24.78 ? 280  THR B O   1 
ATOM   8001  C  CB  . THR B  1 280 ? -5.582  70.778 -7.867 1.00 26.43 ? 280  THR B CB  1 
ATOM   8002  O  OG1 . THR B  1 280 ? -5.389  72.123 -7.438 1.00 29.55 ? 280  THR B OG1 1 
ATOM   8003  C  CG2 . THR B  1 280 ? -5.995  70.826 -9.323 1.00 26.42 ? 280  THR B CG2 1 
ATOM   8004  N  N   . ASN B  1 281 ? -6.551  71.309 -4.890 1.00 25.37 ? 281  ASN B N   1 
ATOM   8005  C  CA  . ASN B  1 281 ? -6.130  71.522 -3.514 1.00 25.05 ? 281  ASN B CA  1 
ATOM   8006  C  C   . ASN B  1 281 ? -7.199  72.239 -2.700 1.00 24.42 ? 281  ASN B C   1 
ATOM   8007  O  O   . ASN B  1 281 ? -7.142  73.460 -2.567 1.00 25.56 ? 281  ASN B O   1 
ATOM   8008  C  CB  . ASN B  1 281 ? -4.864  72.375 -3.553 1.00 25.82 ? 281  ASN B CB  1 
ATOM   8009  C  CG  . ASN B  1 281 ? -4.077  72.350 -2.257 1.00 27.71 ? 281  ASN B CG  1 
ATOM   8010  O  OD1 . ASN B  1 281 ? -4.502  71.784 -1.257 1.00 25.72 ? 281  ASN B OD1 1 
ATOM   8011  N  ND2 . ASN B  1 281 ? -2.906  72.981 -2.309 1.00 28.58 ? 281  ASN B ND2 1 
ATOM   8012  N  N   . ALA B  1 282 ? -8.159  71.498 -2.154 1.00 23.84 ? 282  ALA B N   1 
ATOM   8013  C  CA  . ALA B  1 282 ? -9.248  72.094 -1.358 1.00 25.20 ? 282  ALA B CA  1 
ATOM   8014  C  C   . ALA B  1 282 ? -8.735  72.981 -0.217 1.00 25.19 ? 282  ALA B C   1 
ATOM   8015  O  O   . ALA B  1 282 ? -7.819  72.610 0.513  1.00 26.63 ? 282  ALA B O   1 
ATOM   8016  C  CB  . ALA B  1 282 ? -10.168 70.994 -0.800 1.00 24.47 ? 282  ALA B CB  1 
ATOM   8017  N  N   . THR B  1 283 ? -9.349  74.148 -0.072 1.00 25.64 ? 283  THR B N   1 
ATOM   8018  C  CA  . THR B  1 283 ? -8.959  75.135 0.936  1.00 25.26 ? 283  THR B CA  1 
ATOM   8019  C  C   . THR B  1 283 ? -9.437  74.851 2.359  1.00 24.38 ? 283  THR B C   1 
ATOM   8020  O  O   . THR B  1 283 ? -10.626 74.661 2.595  1.00 24.78 ? 283  THR B O   1 
ATOM   8021  C  CB  . THR B  1 283 ? -9.492  76.543 0.564  1.00 26.55 ? 283  THR B CB  1 
ATOM   8022  O  OG1 . THR B  1 283 ? -9.265  76.802 -0.826 1.00 28.11 ? 283  THR B OG1 1 
ATOM   8023  C  CG2 . THR B  1 283 ? -8.778  77.608 1.376  1.00 26.58 ? 283  THR B CG2 1 
ATOM   8024  N  N   . SER B  1 284 ? -8.506  74.833 3.302  1.00 23.52 ? 284  SER B N   1 
ATOM   8025  C  CA  . SER B  1 284 ? -8.857  74.632 4.702  1.00 22.47 ? 284  SER B CA  1 
ATOM   8026  C  C   . SER B  1 284 ? -9.170  76.033 5.225  1.00 22.24 ? 284  SER B C   1 
ATOM   8027  O  O   . SER B  1 284 ? -8.282  76.865 5.339  1.00 22.46 ? 284  SER B O   1 
ATOM   8028  C  CB  . SER B  1 284 ? -7.688  74.028 5.483  1.00 21.11 ? 284  SER B CB  1 
ATOM   8029  O  OG  . SER B  1 284 ? -7.568  72.632 5.231  1.00 25.10 ? 284  SER B OG  1 
ATOM   8030  N  N   . ILE B  1 285 ? -10.443 76.288 5.503  1.00 20.80 ? 285  ILE B N   1 
ATOM   8031  C  CA  . ILE B  1 285 ? -10.883 77.586 5.990  1.00 19.57 ? 285  ILE B CA  1 
ATOM   8032  C  C   . ILE B  1 285 ? -10.575 77.671 7.468  1.00 19.89 ? 285  ILE B C   1 
ATOM   8033  O  O   . ILE B  1 285 ? -11.019 76.833 8.245  1.00 18.63 ? 285  ILE B O   1 
ATOM   8034  C  CB  . ILE B  1 285 ? -12.404 77.752 5.823  1.00 18.63 ? 285  ILE B CB  1 
ATOM   8035  C  CG1 . ILE B  1 285 ? -12.792 77.563 4.355  1.00 18.15 ? 285  ILE B CG1 1 
ATOM   8036  C  CG2 . ILE B  1 285 ? -12.830 79.118 6.369  1.00 17.38 ? 285  ILE B CG2 1 
ATOM   8037  C  CD1 . ILE B  1 285 ? -12.054 78.525 3.413  1.00 20.84 ? 285  ILE B CD1 1 
ATOM   8038  N  N   . GLN B  1 286 ? -9.831  78.683 7.878  1.00 20.66 ? 286  GLN B N   1 
ATOM   8039  C  CA  . GLN B  1 286 ? -9.510  78.795 9.295  1.00 20.46 ? 286  GLN B CA  1 
ATOM   8040  C  C   . GLN B  1 286 ? -10.597 79.557 10.052 1.00 19.99 ? 286  GLN B C   1 
ATOM   8041  O  O   . GLN B  1 286 ? -11.239 80.439 9.491  1.00 20.16 ? 286  GLN B O   1 
ATOM   8042  C  CB  . GLN B  1 286 ? -8.166  79.506 9.490  1.00 19.55 ? 286  GLN B CB  1 
ATOM   8043  C  CG  . GLN B  1 286 ? -7.844  79.802 10.965 1.00 20.16 ? 286  GLN B CG  1 
ATOM   8044  C  CD  . GLN B  1 286 ? -6.475  80.429 11.163 1.00 21.20 ? 286  GLN B CD  1 
ATOM   8045  O  OE1 . GLN B  1 286 ? -5.805  80.812 10.203 1.00 21.13 ? 286  GLN B OE1 1 
ATOM   8046  N  NE2 . GLN B  1 286 ? -6.057  80.545 12.416 1.00 22.13 ? 286  GLN B NE2 1 
ATOM   8047  N  N   . ILE B  1 287 ? -10.813 79.184 11.311 1.00 19.58 ? 287  ILE B N   1 
ATOM   8048  C  CA  . ILE B  1 287 ? -11.773 79.870 12.171 1.00 19.45 ? 287  ILE B CA  1 
ATOM   8049  C  C   . ILE B  1 287 ? -10.933 80.403 13.332 1.00 19.19 ? 287  ILE B C   1 
ATOM   8050  O  O   . ILE B  1 287 ? -10.446 79.638 14.180 1.00 18.06 ? 287  ILE B O   1 
ATOM   8051  C  CB  . ILE B  1 287 ? -12.869 78.922 12.715 1.00 20.77 ? 287  ILE B CB  1 
ATOM   8052  C  CG1 . ILE B  1 287 ? -13.754 78.412 11.567 1.00 20.45 ? 287  ILE B CG1 1 
ATOM   8053  C  CG2 . ILE B  1 287 ? -13.776 79.682 13.690 1.00 21.57 ? 287  ILE B CG2 1 
ATOM   8054  C  CD1 . ILE B  1 287 ? -14.837 77.447 12.018 1.00 20.68 ? 287  ILE B CD1 1 
ATOM   8055  N  N   . THR B  1 288 ? -10.734 81.713 13.358 1.00 18.31 ? 288  THR B N   1 
ATOM   8056  C  CA  . THR B  1 288 ? -9.915  82.312 14.398 1.00 20.14 ? 288  THR B CA  1 
ATOM   8057  C  C   . THR B  1 288 ? -10.601 82.443 15.738 1.00 19.81 ? 288  THR B C   1 
ATOM   8058  O  O   . THR B  1 288 ? -11.817 82.599 15.832 1.00 19.90 ? 288  THR B O   1 
ATOM   8059  C  CB  . THR B  1 288 ? -9.415  83.718 13.965 1.00 21.99 ? 288  THR B CB  1 
ATOM   8060  O  OG1 . THR B  1 288 ? -10.553 84.556 13.725 1.00 25.18 ? 288  THR B OG1 1 
ATOM   8061  C  CG2 . THR B  1 288 ? -8.576  83.632 12.690 1.00 20.38 ? 288  THR B CG2 1 
ATOM   8062  N  N   . ALA B  1 289 ? -9.790  82.376 16.781 1.00 20.72 ? 289  ALA B N   1 
ATOM   8063  C  CA  . ALA B  1 289 ? -10.275 82.504 18.142 1.00 22.24 ? 289  ALA B CA  1 
ATOM   8064  C  C   . ALA B  1 289 ? -10.748 83.943 18.325 1.00 23.31 ? 289  ALA B C   1 
ATOM   8065  O  O   . ALA B  1 289 ? -10.292 84.835 17.615 1.00 23.62 ? 289  ALA B O   1 
ATOM   8066  C  CB  . ALA B  1 289 ? -9.146  82.207 19.119 1.00 20.32 ? 289  ALA B CB  1 
ATOM   8067  N  N   . PRO B  1 290 ? -11.666 84.182 19.279 1.00 24.01 ? 290  PRO B N   1 
ATOM   8068  C  CA  . PRO B  1 290 ? -12.191 85.528 19.553 1.00 24.92 ? 290  PRO B CA  1 
ATOM   8069  C  C   . PRO B  1 290 ? -11.107 86.459 20.096 1.00 25.42 ? 290  PRO B C   1 
ATOM   8070  O  O   . PRO B  1 290 ? -10.076 85.999 20.607 1.00 24.07 ? 290  PRO B O   1 
ATOM   8071  C  CB  . PRO B  1 290 ? -13.295 85.270 20.570 1.00 24.22 ? 290  PRO B CB  1 
ATOM   8072  C  CG  . PRO B  1 290 ? -12.803 84.054 21.288 1.00 26.00 ? 290  PRO B CG  1 
ATOM   8073  C  CD  . PRO B  1 290 ? -12.293 83.187 20.161 1.00 24.00 ? 290  PRO B CD  1 
ATOM   8074  N  N   . ALA B  1 291 ? -11.351 87.766 19.978 1.00 24.90 ? 291  ALA B N   1 
ATOM   8075  C  CA  . ALA B  1 291 ? -10.404 88.780 20.438 1.00 24.24 ? 291  ALA B CA  1 
ATOM   8076  C  C   . ALA B  1 291 ? -10.095 88.608 21.923 1.00 23.12 ? 291  ALA B C   1 
ATOM   8077  O  O   . ALA B  1 291 ? -8.967  88.804 22.363 1.00 24.10 ? 291  ALA B O   1 
ATOM   8078  C  CB  . ALA B  1 291 ? -10.973 90.193 20.153 1.00 23.66 ? 291  ALA B CB  1 
ATOM   8079  N  N   . SER B  1 292 ? -11.101 88.230 22.687 1.00 22.26 ? 292  SER B N   1 
ATOM   8080  C  CA  . SER B  1 292 ? -10.930 88.008 24.109 1.00 24.13 ? 292  SER B CA  1 
ATOM   8081  C  C   . SER B  1 292 ? -9.852  86.934 24.418 1.00 25.75 ? 292  SER B C   1 
ATOM   8082  O  O   . SER B  1 292 ? -9.329  86.872 25.545 1.00 26.43 ? 292  SER B O   1 
ATOM   8083  C  CB  . SER B  1 292 ? -12.262 87.581 24.706 1.00 23.46 ? 292  SER B CB  1 
ATOM   8084  O  OG  . SER B  1 292 ? -12.766 86.451 23.998 1.00 26.56 ? 292  SER B OG  1 
ATOM   8085  N  N   . MET B  1 293 ? -9.536  86.090 23.434 1.00 24.32 ? 293  MET B N   1 
ATOM   8086  C  CA  . MET B  1 293 ? -8.533  85.033 23.617 1.00 25.24 ? 293  MET B CA  1 
ATOM   8087  C  C   . MET B  1 293 ? -7.195  85.389 22.978 1.00 25.32 ? 293  MET B C   1 
ATOM   8088  O  O   . MET B  1 293 ? -6.142  85.035 23.499 1.00 25.69 ? 293  MET B O   1 
ATOM   8089  C  CB  . MET B  1 293 ? -9.021  83.701 23.019 1.00 22.83 ? 293  MET B CB  1 
ATOM   8090  C  CG  . MET B  1 293 ? -10.228 83.111 23.706 1.00 23.11 ? 293  MET B CG  1 
ATOM   8091  S  SD  . MET B  1 293 ? -9.823  82.413 25.331 1.00 23.28 ? 293  MET B SD  1 
ATOM   8092  C  CE  . MET B  1 293 ? -11.341 82.558 26.151 1.00 18.10 ? 293  MET B CE  1 
ATOM   8093  N  N   . LEU B  1 294 ? -7.232  86.094 21.852 1.00 25.65 ? 294  LEU B N   1 
ATOM   8094  C  CA  . LEU B  1 294 ? -5.995  86.460 21.168 1.00 26.59 ? 294  LEU B CA  1 
ATOM   8095  C  C   . LEU B  1 294 ? -5.132  87.457 21.951 1.00 26.94 ? 294  LEU B C   1 
ATOM   8096  O  O   . LEU B  1 294 ? -3.953  87.622 21.649 1.00 26.68 ? 294  LEU B O   1 
ATOM   8097  C  CB  . LEU B  1 294 ? -6.319  86.992 19.770 1.00 24.86 ? 294  LEU B CB  1 
ATOM   8098  C  CG  . LEU B  1 294 ? -7.107  85.994 18.879 1.00 26.66 ? 294  LEU B CG  1 
ATOM   8099  C  CD1 . LEU B  1 294 ? -7.444  86.657 17.539 1.00 25.92 ? 294  LEU B CD1 1 
ATOM   8100  C  CD2 . LEU B  1 294 ? -6.290  84.714 18.631 1.00 24.48 ? 294  LEU B CD2 1 
ATOM   8101  N  N   . ILE B  1 295 ? -5.694  88.115 22.964 1.00 26.74 ? 295  ILE B N   1 
ATOM   8102  C  CA  . ILE B  1 295 ? -4.893  89.050 23.744 1.00 27.86 ? 295  ILE B CA  1 
ATOM   8103  C  C   . ILE B  1 295 ? -3.769  88.335 24.492 1.00 27.38 ? 295  ILE B C   1 
ATOM   8104  O  O   . ILE B  1 295 ? -2.826  88.971 24.940 1.00 27.89 ? 295  ILE B O   1 
ATOM   8105  C  CB  . ILE B  1 295 ? -5.713  89.801 24.809 1.00 29.18 ? 295  ILE B CB  1 
ATOM   8106  C  CG1 . ILE B  1 295 ? -6.380  88.791 25.748 1.00 29.57 ? 295  ILE B CG1 1 
ATOM   8107  C  CG2 . ILE B  1 295 ? -6.710  90.730 24.149 1.00 29.95 ? 295  ILE B CG2 1 
ATOM   8108  C  CD1 . ILE B  1 295 ? -7.140  89.429 26.896 1.00 30.52 ? 295  ILE B CD1 1 
ATOM   8109  N  N   . GLY B  1 296 ? -3.871  87.018 24.641 1.00 26.59 ? 296  GLY B N   1 
ATOM   8110  C  CA  . GLY B  1 296 ? -2.828  86.300 25.352 1.00 24.09 ? 296  GLY B CA  1 
ATOM   8111  C  C   . GLY B  1 296 ? -2.797  84.815 25.054 1.00 23.61 ? 296  GLY B C   1 
ATOM   8112  O  O   . GLY B  1 296 ? -3.414  84.357 24.088 1.00 22.65 ? 296  GLY B O   1 
ATOM   8113  N  N   . ASP B  1 297 ? -2.062  84.054 25.862 1.00 21.82 ? 297  ASP B N   1 
ATOM   8114  C  CA  . ASP B  1 297 ? -2.004  82.612 25.665 1.00 20.71 ? 297  ASP B CA  1 
ATOM   8115  C  C   . ASP B  1 297 ? -3.392  82.051 25.912 1.00 19.30 ? 297  ASP B C   1 
ATOM   8116  O  O   . ASP B  1 297 ? -4.124  82.528 26.773 1.00 19.20 ? 297  ASP B O   1 
ATOM   8117  C  CB  . ASP B  1 297 ? -1.014  81.957 26.632 1.00 21.38 ? 297  ASP B CB  1 
ATOM   8118  C  CG  . ASP B  1 297 ? 0.424   82.162 26.225 1.00 23.27 ? 297  ASP B CG  1 
ATOM   8119  O  OD1 . ASP B  1 297 ? 0.665   82.584 25.071 1.00 25.32 ? 297  ASP B OD1 1 
ATOM   8120  O  OD2 . ASP B  1 297 ? 1.315   81.889 27.058 1.00 23.89 ? 297  ASP B OD2 1 
ATOM   8121  N  N   . HIS B  1 298 ? -3.755  81.034 25.151 1.00 17.96 ? 298  HIS B N   1 
ATOM   8122  C  CA  . HIS B  1 298 ? -5.066  80.420 25.302 1.00 18.63 ? 298  HIS B CA  1 
ATOM   8123  C  C   . HIS B  1 298 ? -4.995  78.968 24.829 1.00 17.93 ? 298  HIS B C   1 
ATOM   8124  O  O   . HIS B  1 298 ? -3.942  78.499 24.404 1.00 17.85 ? 298  HIS B O   1 
ATOM   8125  C  CB  . HIS B  1 298 ? -6.109  81.187 24.469 1.00 17.59 ? 298  HIS B CB  1 
ATOM   8126  C  CG  . HIS B  1 298 ? -5.747  81.312 23.023 1.00 20.10 ? 298  HIS B CG  1 
ATOM   8127  N  ND1 . HIS B  1 298 ? -4.941  82.320 22.539 1.00 21.42 ? 298  HIS B ND1 1 
ATOM   8128  C  CD2 . HIS B  1 298 ? -6.059  80.541 21.952 1.00 20.90 ? 298  HIS B CD2 1 
ATOM   8129  C  CE1 . HIS B  1 298 ? -4.777  82.170 21.236 1.00 22.90 ? 298  HIS B CE1 1 
ATOM   8130  N  NE2 . HIS B  1 298 ? -5.448  81.094 20.853 1.00 20.94 ? 298  HIS B NE2 1 
ATOM   8131  N  N   . TYR B  1 299 ? -6.129  78.279 24.913 1.00 18.09 ? 299  TYR B N   1 
ATOM   8132  C  CA  . TYR B  1 299 ? -6.260  76.886 24.488 1.00 17.34 ? 299  TYR B CA  1 
ATOM   8133  C  C   . TYR B  1 299 ? -7.575  76.681 23.754 1.00 18.03 ? 299  TYR B C   1 
ATOM   8134  O  O   . TYR B  1 299 ? -8.537  77.438 23.945 1.00 16.75 ? 299  TYR B O   1 
ATOM   8135  C  CB  . TYR B  1 299 ? -6.335  75.930 25.681 1.00 15.15 ? 299  TYR B CB  1 
ATOM   8136  C  CG  . TYR B  1 299 ? -5.248  76.057 26.710 1.00 15.91 ? 299  TYR B CG  1 
ATOM   8137  C  CD1 . TYR B  1 299 ? -3.952  75.620 26.444 1.00 14.82 ? 299  TYR B CD1 1 
ATOM   8138  C  CD2 . TYR B  1 299 ? -5.529  76.574 27.973 1.00 15.53 ? 299  TYR B CD2 1 
ATOM   8139  C  CE1 . TYR B  1 299 ? -2.962  75.686 27.421 1.00 16.61 ? 299  TYR B CE1 1 
ATOM   8140  C  CE2 . TYR B  1 299 ? -4.542  76.641 28.949 1.00 18.52 ? 299  TYR B CE2 1 
ATOM   8141  C  CZ  . TYR B  1 299 ? -3.268  76.192 28.666 1.00 16.81 ? 299  TYR B CZ  1 
ATOM   8142  O  OH  . TYR B  1 299 ? -2.309  76.255 29.639 1.00 17.79 ? 299  TYR B OH  1 
ATOM   8143  N  N   . LEU B  1 300 ? -7.610  75.651 22.915 1.00 15.89 ? 300  LEU B N   1 
ATOM   8144  C  CA  . LEU B  1 300 ? -8.854  75.251 22.279 1.00 16.49 ? 300  LEU B CA  1 
ATOM   8145  C  C   . LEU B  1 300 ? -9.284  74.111 23.233 1.00 16.81 ? 300  LEU B C   1 
ATOM   8146  O  O   . LEU B  1 300 ? -8.532  73.151 23.421 1.00 16.19 ? 300  LEU B O   1 
ATOM   8147  C  CB  . LEU B  1 300 ? -8.608  74.699 20.880 1.00 16.31 ? 300  LEU B CB  1 
ATOM   8148  C  CG  . LEU B  1 300 ? -9.844  74.121 20.190 1.00 17.25 ? 300  LEU B CG  1 
ATOM   8149  C  CD1 . LEU B  1 300 ? -10.847 75.232 19.900 1.00 18.56 ? 300  LEU B CD1 1 
ATOM   8150  C  CD2 . LEU B  1 300 ? -9.438  73.440 18.895 1.00 18.11 ? 300  LEU B CD2 1 
ATOM   8151  N  N   . CYS B  1 301 ? -10.463 74.193 23.849 1.00 18.51 ? 301  CYS B N   1 
ATOM   8152  C  CA  . CYS B  1 301 ? -10.855 73.133 24.789 1.00 19.72 ? 301  CYS B CA  1 
ATOM   8153  C  C   . CYS B  1 301 ? -12.078 72.284 24.448 1.00 20.91 ? 301  CYS B C   1 
ATOM   8154  O  O   . CYS B  1 301 ? -12.391 71.340 25.176 1.00 20.36 ? 301  CYS B O   1 
ATOM   8155  C  CB  . CYS B  1 301 ? -11.028 73.709 26.196 1.00 20.63 ? 301  CYS B CB  1 
ATOM   8156  S  SG  . CYS B  1 301 ? -12.270 75.022 26.334 1.00 24.66 ? 301  CYS B SG  1 
ATOM   8157  N  N   . ASP B  1 302 ? -12.771 72.620 23.365 1.00 20.98 ? 302  ASP B N   1 
ATOM   8158  C  CA  . ASP B  1 302 ? -13.927 71.842 22.934 1.00 22.00 ? 302  ASP B CA  1 
ATOM   8159  C  C   . ASP B  1 302 ? -14.336 72.152 21.504 1.00 22.08 ? 302  ASP B C   1 
ATOM   8160  O  O   . ASP B  1 302 ? -14.283 73.306 21.060 1.00 22.67 ? 302  ASP B O   1 
ATOM   8161  C  CB  . ASP B  1 302 ? -15.143 72.083 23.845 1.00 23.42 ? 302  ASP B CB  1 
ATOM   8162  C  CG  . ASP B  1 302 ? -16.303 71.114 23.547 1.00 25.10 ? 302  ASP B CG  1 
ATOM   8163  O  OD1 . ASP B  1 302 ? -17.077 71.350 22.593 1.00 25.24 ? 302  ASP B OD1 1 
ATOM   8164  O  OD2 . ASP B  1 302 ? -16.419 70.100 24.266 1.00 24.96 ? 302  ASP B OD2 1 
ATOM   8165  N  N   . VAL B  1 303 ? -14.717 71.102 20.782 1.00 20.30 ? 303  VAL B N   1 
ATOM   8166  C  CA  . VAL B  1 303 ? -15.210 71.229 19.418 1.00 19.53 ? 303  VAL B CA  1 
ATOM   8167  C  C   . VAL B  1 303 ? -16.433 70.318 19.366 1.00 19.51 ? 303  VAL B C   1 
ATOM   8168  O  O   . VAL B  1 303 ? -16.356 69.132 19.700 1.00 19.44 ? 303  VAL B O   1 
ATOM   8169  C  CB  . VAL B  1 303 ? -14.185 70.758 18.356 1.00 19.74 ? 303  VAL B CB  1 
ATOM   8170  C  CG1 . VAL B  1 303 ? -14.792 70.899 16.949 1.00 17.91 ? 303  VAL B CG1 1 
ATOM   8171  C  CG2 . VAL B  1 303 ? -12.908 71.585 18.454 1.00 18.18 ? 303  VAL B CG2 1 
ATOM   8172  N  N   . THR B  1 304 ? -17.565 70.871 18.962 1.00 18.63 ? 304  THR B N   1 
ATOM   8173  C  CA  . THR B  1 304 ? -18.793 70.090 18.895 1.00 18.24 ? 304  THR B CA  1 
ATOM   8174  C  C   . THR B  1 304 ? -19.652 70.614 17.761 1.00 19.20 ? 304  THR B C   1 
ATOM   8175  O  O   . THR B  1 304 ? -20.034 71.792 17.755 1.00 19.73 ? 304  THR B O   1 
ATOM   8176  C  CB  . THR B  1 304 ? -19.635 70.205 20.201 1.00 18.64 ? 304  THR B CB  1 
ATOM   8177  O  OG1 . THR B  1 304 ? -18.890 69.708 21.319 1.00 18.94 ? 304  THR B OG1 1 
ATOM   8178  C  CG2 . THR B  1 304 ? -20.929 69.409 20.074 1.00 16.31 ? 304  THR B CG2 1 
ATOM   8179  N  N   . TRP B  1 305 ? -19.948 69.748 16.800 1.00 18.51 ? 305  TRP B N   1 
ATOM   8180  C  CA  . TRP B  1 305 ? -20.798 70.129 15.680 1.00 19.51 ? 305  TRP B CA  1 
ATOM   8181  C  C   . TRP B  1 305 ? -22.246 70.240 16.150 1.00 18.90 ? 305  TRP B C   1 
ATOM   8182  O  O   . TRP B  1 305 ? -22.689 69.444 16.978 1.00 18.73 ? 305  TRP B O   1 
ATOM   8183  C  CB  . TRP B  1 305 ? -20.721 69.079 14.568 1.00 18.37 ? 305  TRP B CB  1 
ATOM   8184  C  CG  . TRP B  1 305 ? -19.490 69.173 13.725 1.00 17.78 ? 305  TRP B CG  1 
ATOM   8185  C  CD1 . TRP B  1 305 ? -18.316 68.477 13.874 1.00 17.17 ? 305  TRP B CD1 1 
ATOM   8186  C  CD2 . TRP B  1 305 ? -19.319 70.008 12.588 1.00 17.70 ? 305  TRP B CD2 1 
ATOM   8187  N  NE1 . TRP B  1 305 ? -17.425 68.831 12.888 1.00 16.65 ? 305  TRP B NE1 1 
ATOM   8188  C  CE2 . TRP B  1 305 ? -18.018 69.770 12.081 1.00 18.86 ? 305  TRP B CE2 1 
ATOM   8189  C  CE3 . TRP B  1 305 ? -20.140 70.936 11.938 1.00 18.81 ? 305  TRP B CE3 1 
ATOM   8190  C  CZ2 . TRP B  1 305 ? -17.522 70.432 10.953 1.00 17.68 ? 305  TRP B CZ2 1 
ATOM   8191  C  CZ3 . TRP B  1 305 ? -19.643 71.595 10.817 1.00 19.89 ? 305  TRP B CZ3 1 
ATOM   8192  C  CH2 . TRP B  1 305 ? -18.347 71.334 10.338 1.00 19.15 ? 305  TRP B CH2 1 
ATOM   8193  N  N   . ALA B  1 306 ? -22.977 71.220 15.624 1.00 18.63 ? 306  ALA B N   1 
ATOM   8194  C  CA  . ALA B  1 306 ? -24.383 71.397 15.983 1.00 19.25 ? 306  ALA B CA  1 
ATOM   8195  C  C   . ALA B  1 306 ? -25.298 70.892 14.854 1.00 20.20 ? 306  ALA B C   1 
ATOM   8196  O  O   . ALA B  1 306 ? -26.289 70.215 15.110 1.00 22.24 ? 306  ALA B O   1 
ATOM   8197  C  CB  . ALA B  1 306 ? -24.682 72.863 16.280 1.00 18.01 ? 306  ALA B CB  1 
ATOM   8198  N  N   . THR B  1 307 ? -24.965 71.221 13.614 1.00 20.38 ? 307  THR B N   1 
ATOM   8199  C  CA  . THR B  1 307 ? -25.746 70.790 12.458 1.00 20.70 ? 307  THR B CA  1 
ATOM   8200  C  C   . THR B  1 307 ? -24.751 70.559 11.317 1.00 21.75 ? 307  THR B C   1 
ATOM   8201  O  O   . THR B  1 307 ? -23.537 70.690 11.507 1.00 21.61 ? 307  THR B O   1 
ATOM   8202  C  CB  . THR B  1 307 ? -26.748 71.875 11.974 1.00 20.35 ? 307  THR B CB  1 
ATOM   8203  O  OG1 . THR B  1 307 ? -26.032 72.921 11.299 1.00 18.91 ? 307  THR B OG1 1 
ATOM   8204  C  CG2 . THR B  1 307 ? -27.539 72.474 13.146 1.00 18.54 ? 307  THR B CG2 1 
ATOM   8205  N  N   . GLN B  1 308 ? -25.273 70.231 10.138 1.00 20.87 ? 308  GLN B N   1 
ATOM   8206  C  CA  . GLN B  1 308 ? -24.442 70.007 8.966  1.00 20.29 ? 308  GLN B CA  1 
ATOM   8207  C  C   . GLN B  1 308 ? -23.658 71.269 8.609  1.00 20.32 ? 308  GLN B C   1 
ATOM   8208  O  O   . GLN B  1 308 ? -22.625 71.196 7.943  1.00 18.84 ? 308  GLN B O   1 
ATOM   8209  C  CB  . GLN B  1 308 ? -25.301 69.654 7.747  1.00 20.91 ? 308  GLN B CB  1 
ATOM   8210  C  CG  . GLN B  1 308 ? -26.243 68.436 7.886  1.00 23.43 ? 308  GLN B CG  1 
ATOM   8211  C  CD  . GLN B  1 308 ? -25.543 67.158 8.345  1.00 24.73 ? 308  GLN B CD  1 
ATOM   8212  O  OE1 . GLN B  1 308 ? -24.313 67.006 8.216  1.00 26.40 ? 308  GLN B OE1 1 
ATOM   8213  N  NE2 . GLN B  1 308 ? -26.328 66.223 8.872  1.00 23.17 ? 308  GLN B NE2 1 
ATOM   8214  N  N   . GLU B  1 309 ? -24.153 72.429 9.034  1.00 19.41 ? 309  GLU B N   1 
ATOM   8215  C  CA  . GLU B  1 309 ? -23.488 73.673 8.676  1.00 19.95 ? 309  GLU B CA  1 
ATOM   8216  C  C   . GLU B  1 309 ? -23.250 74.619 9.844  1.00 20.04 ? 309  GLU B C   1 
ATOM   8217  O  O   . GLU B  1 309 ? -23.127 75.831 9.660  1.00 19.74 ? 309  GLU B O   1 
ATOM   8218  C  CB  . GLU B  1 309 ? -24.303 74.381 7.588  1.00 21.29 ? 309  GLU B CB  1 
ATOM   8219  C  CG  . GLU B  1 309 ? -24.343 73.624 6.260  1.00 22.96 ? 309  GLU B CG  1 
ATOM   8220  C  CD  . GLU B  1 309 ? -25.217 74.312 5.213  1.00 26.76 ? 309  GLU B CD  1 
ATOM   8221  O  OE1 . GLU B  1 309 ? -25.333 75.562 5.235  1.00 27.14 ? 309  GLU B OE1 1 
ATOM   8222  O  OE2 . GLU B  1 309 ? -25.779 73.597 4.352  1.00 27.39 ? 309  GLU B OE2 1 
ATOM   8223  N  N   . ARG B  1 310 ? -23.166 74.058 11.046 1.00 20.10 ? 310  ARG B N   1 
ATOM   8224  C  CA  . ARG B  1 310 ? -22.946 74.861 12.248 1.00 20.05 ? 310  ARG B CA  1 
ATOM   8225  C  C   . ARG B  1 310 ? -22.039 74.101 13.211 1.00 18.64 ? 310  ARG B C   1 
ATOM   8226  O  O   . ARG B  1 310 ? -22.329 72.981 13.608 1.00 18.01 ? 310  ARG B O   1 
ATOM   8227  C  CB  . ARG B  1 310 ? -24.289 75.190 12.936 1.00 18.68 ? 310  ARG B CB  1 
ATOM   8228  C  CG  . ARG B  1 310 ? -24.145 75.951 14.283 1.00 20.75 ? 310  ARG B CG  1 
ATOM   8229  C  CD  . ARG B  1 310 ? -25.505 76.496 14.776 1.00 20.42 ? 310  ARG B CD  1 
ATOM   8230  N  NE  . ARG B  1 310 ? -26.085 77.421 13.805 1.00 20.43 ? 310  ARG B NE  1 
ATOM   8231  C  CZ  . ARG B  1 310 ? -27.392 77.660 13.666 1.00 22.35 ? 310  ARG B CZ  1 
ATOM   8232  N  NH1 . ARG B  1 310 ? -28.283 77.051 14.448 1.00 18.46 ? 310  ARG B NH1 1 
ATOM   8233  N  NH2 . ARG B  1 310 ? -27.816 78.475 12.699 1.00 20.48 ? 310  ARG B NH2 1 
ATOM   8234  N  N   . ILE B  1 311 ? -20.938 74.725 13.585 1.00 18.48 ? 311  ILE B N   1 
ATOM   8235  C  CA  . ILE B  1 311 ? -20.013 74.095 14.502 1.00 18.29 ? 311  ILE B CA  1 
ATOM   8236  C  C   . ILE B  1 311 ? -19.777 75.028 15.695 1.00 19.47 ? 311  ILE B C   1 
ATOM   8237  O  O   . ILE B  1 311 ? -19.818 76.268 15.565 1.00 18.38 ? 311  ILE B O   1 
ATOM   8238  C  CB  . ILE B  1 311 ? -18.655 73.741 13.770 1.00 17.62 ? 311  ILE B CB  1 
ATOM   8239  C  CG1 . ILE B  1 311 ? -17.715 72.978 14.707 1.00 17.43 ? 311  ILE B CG1 1 
ATOM   8240  C  CG2 . ILE B  1 311 ? -17.987 74.981 13.279 1.00 16.80 ? 311  ILE B CG2 1 
ATOM   8241  C  CD1 . ILE B  1 311 ? -16.459 72.477 14.019 1.00 19.74 ? 311  ILE B CD1 1 
ATOM   8242  N  N   . SER B  1 312 ? -19.592 74.438 16.872 1.00 19.26 ? 312  SER B N   1 
ATOM   8243  C  CA  . SER B  1 312 ? -19.317 75.251 18.038 1.00 20.62 ? 312  SER B CA  1 
ATOM   8244  C  C   . SER B  1 312 ? -17.942 74.884 18.575 1.00 21.03 ? 312  SER B C   1 
ATOM   8245  O  O   . SER B  1 312 ? -17.524 73.729 18.533 1.00 20.04 ? 312  SER B O   1 
ATOM   8246  C  CB  . SER B  1 312 ? -20.371 75.039 19.125 1.00 20.49 ? 312  SER B CB  1 
ATOM   8247  O  OG  . SER B  1 312 ? -20.100 73.902 19.924 1.00 20.90 ? 312  SER B OG  1 
ATOM   8248  N  N   . LEU B  1 313 ? -17.226 75.885 19.045 1.00 22.08 ? 313  LEU B N   1 
ATOM   8249  C  CA  . LEU B  1 313 ? -15.921 75.650 19.619 1.00 24.26 ? 313  LEU B CA  1 
ATOM   8250  C  C   . LEU B  1 313 ? -15.783 76.491 20.869 1.00 23.59 ? 313  LEU B C   1 
ATOM   8251  O  O   . LEU B  1 313 ? -16.294 77.608 20.942 1.00 23.74 ? 313  LEU B O   1 
ATOM   8252  C  CB  . LEU B  1 313 ? -14.787 75.969 18.630 1.00 25.38 ? 313  LEU B CB  1 
ATOM   8253  C  CG  . LEU B  1 313 ? -14.988 76.882 17.433 1.00 28.56 ? 313  LEU B CG  1 
ATOM   8254  C  CD1 . LEU B  1 313 ? -13.644 77.394 16.953 1.00 29.70 ? 313  LEU B CD1 1 
ATOM   8255  C  CD2 . LEU B  1 313 ? -15.677 76.104 16.312 1.00 32.11 ? 313  LEU B CD2 1 
ATOM   8256  N  N   . GLN B  1 314 ? -15.121 75.932 21.872 1.00 23.09 ? 314  GLN B N   1 
ATOM   8257  C  CA  . GLN B  1 314 ? -14.907 76.642 23.113 1.00 22.98 ? 314  GLN B CA  1 
ATOM   8258  C  C   . GLN B  1 314 ? -13.419 76.884 23.290 1.00 22.12 ? 314  GLN B C   1 
ATOM   8259  O  O   . GLN B  1 314 ? -12.599 75.998 23.050 1.00 20.98 ? 314  GLN B O   1 
ATOM   8260  C  CB  . GLN B  1 314 ? -15.457 75.835 24.285 1.00 25.85 ? 314  GLN B CB  1 
ATOM   8261  C  CG  . GLN B  1 314 ? -16.960 75.583 24.219 1.00 28.70 ? 314  GLN B CG  1 
ATOM   8262  C  CD  . GLN B  1 314 ? -17.452 74.761 25.395 1.00 31.13 ? 314  GLN B CD  1 
ATOM   8263  O  OE1 . GLN B  1 314 ? -17.342 75.177 26.555 1.00 31.44 ? 314  GLN B OE1 1 
ATOM   8264  N  NE2 . GLN B  1 314 ? -17.973 73.573 25.107 1.00 31.44 ? 314  GLN B NE2 1 
ATOM   8265  N  N   . TRP B  1 315 ? -13.086 78.105 23.691 1.00 21.66 ? 315  TRP B N   1 
ATOM   8266  C  CA  . TRP B  1 315 ? -11.712 78.511 23.919 1.00 20.82 ? 315  TRP B CA  1 
ATOM   8267  C  C   . TRP B  1 315 ? -11.545 78.848 25.397 1.00 21.57 ? 315  TRP B C   1 
ATOM   8268  O  O   . TRP B  1 315 ? -12.497 79.246 26.070 1.00 22.69 ? 315  TRP B O   1 
ATOM   8269  C  CB  . TRP B  1 315 ? -11.362 79.723 23.060 1.00 20.44 ? 315  TRP B CB  1 
ATOM   8270  C  CG  . TRP B  1 315 ? -11.544 79.495 21.582 1.00 19.78 ? 315  TRP B CG  1 
ATOM   8271  C  CD1 . TRP B  1 315 ? -12.682 79.698 20.852 1.00 19.61 ? 315  TRP B CD1 1 
ATOM   8272  C  CD2 . TRP B  1 315 ? -10.529 79.100 20.646 1.00 17.82 ? 315  TRP B CD2 1 
ATOM   8273  N  NE1 . TRP B  1 315 ? -12.434 79.470 19.510 1.00 19.02 ? 315  TRP B NE1 1 
ATOM   8274  C  CE2 . TRP B  1 315 ? -11.120 79.102 19.359 1.00 20.08 ? 315  TRP B CE2 1 
ATOM   8275  C  CE3 . TRP B  1 315 ? -9.175  78.753 20.770 1.00 18.85 ? 315  TRP B CE3 1 
ATOM   8276  C  CZ2 . TRP B  1 315 ? -10.399 78.771 18.196 1.00 17.99 ? 315  TRP B CZ2 1 
ATOM   8277  C  CZ3 . TRP B  1 315 ? -8.453  78.426 19.616 1.00 18.87 ? 315  TRP B CZ3 1 
ATOM   8278  C  CH2 . TRP B  1 315 ? -9.073  78.441 18.344 1.00 19.89 ? 315  TRP B CH2 1 
ATOM   8279  N  N   . LEU B  1 316 ? -10.329 78.685 25.891 1.00 20.68 ? 316  LEU B N   1 
ATOM   8280  C  CA  . LEU B  1 316 ? -10.032 78.928 27.286 1.00 21.32 ? 316  LEU B CA  1 
ATOM   8281  C  C   . LEU B  1 316 ? -8.709  79.697 27.431 1.00 21.60 ? 316  LEU B C   1 
ATOM   8282  O  O   . LEU B  1 316 ? -7.707  79.364 26.787 1.00 20.64 ? 316  LEU B O   1 
ATOM   8283  C  CB  . LEU B  1 316 ? -9.940  77.582 28.011 1.00 20.47 ? 316  LEU B CB  1 
ATOM   8284  C  CG  . LEU B  1 316 ? -9.609  77.472 29.504 1.00 20.55 ? 316  LEU B CG  1 
ATOM   8285  C  CD1 . LEU B  1 316 ? -10.701 78.089 30.356 1.00 19.76 ? 316  LEU B CD1 1 
ATOM   8286  C  CD2 . LEU B  1 316 ? -9.465  75.988 29.846 1.00 19.32 ? 316  LEU B CD2 1 
ATOM   8287  N  N   . ARG B  1 317 ? -8.722  80.739 28.255 1.00 20.76 ? 317  ARG B N   1 
ATOM   8288  C  CA  . ARG B  1 317 ? -7.521  81.527 28.506 1.00 21.33 ? 317  ARG B CA  1 
ATOM   8289  C  C   . ARG B  1 317 ? -6.521  80.738 29.338 1.00 20.64 ? 317  ARG B C   1 
ATOM   8290  O  O   . ARG B  1 317 ? -6.907  79.908 30.173 1.00 20.96 ? 317  ARG B O   1 
ATOM   8291  C  CB  . ARG B  1 317 ? -7.876  82.808 29.264 1.00 22.64 ? 317  ARG B CB  1 
ATOM   8292  C  CG  . ARG B  1 317 ? -8.380  83.929 28.380 1.00 26.96 ? 317  ARG B CG  1 
ATOM   8293  C  CD  . ARG B  1 317 ? -8.702  85.165 29.201 1.00 27.24 ? 317  ARG B CD  1 
ATOM   8294  N  NE  . ARG B  1 317 ? -9.141  86.271 28.350 1.00 29.14 ? 317  ARG B NE  1 
ATOM   8295  C  CZ  . ARG B  1 317 ? -9.843  87.313 28.789 1.00 29.71 ? 317  ARG B CZ  1 
ATOM   8296  N  NH1 . ARG B  1 317 ? -10.190 87.388 30.065 1.00 29.41 ? 317  ARG B NH1 1 
ATOM   8297  N  NH2 . ARG B  1 317 ? -10.186 88.284 27.957 1.00 29.46 ? 317  ARG B NH2 1 
ATOM   8298  N  N   . ARG B  1 318 ? -5.238  81.012 29.138 1.00 20.92 ? 318  ARG B N   1 
ATOM   8299  C  CA  . ARG B  1 318 ? -4.212  80.316 29.919 1.00 20.91 ? 318  ARG B CA  1 
ATOM   8300  C  C   . ARG B  1 318 ? -4.555  80.427 31.411 1.00 20.85 ? 318  ARG B C   1 
ATOM   8301  O  O   . ARG B  1 318 ? -4.286  79.514 32.168 1.00 20.55 ? 318  ARG B O   1 
ATOM   8302  C  CB  . ARG B  1 318 ? -2.808  80.869 29.630 1.00 19.51 ? 318  ARG B CB  1 
ATOM   8303  C  CG  . ARG B  1 318 ? -1.737  80.043 30.324 1.00 18.59 ? 318  ARG B CG  1 
ATOM   8304  C  CD  . ARG B  1 318 ? -0.365  80.166 29.704 1.00 18.09 ? 318  ARG B CD  1 
ATOM   8305  N  NE  . ARG B  1 318 ? 0.579   79.323 30.441 1.00 18.11 ? 318  ARG B NE  1 
ATOM   8306  C  CZ  . ARG B  1 318 ? 1.773   78.966 29.984 1.00 18.97 ? 318  ARG B CZ  1 
ATOM   8307  N  NH1 . ARG B  1 318 ? 2.171   79.382 28.784 1.00 18.70 ? 318  ARG B NH1 1 
ATOM   8308  N  NH2 . ARG B  1 318 ? 2.562   78.191 30.721 1.00 16.94 ? 318  ARG B NH2 1 
ATOM   8309  N  N   . ILE B  1 319 ? -5.130  81.551 31.832 1.00 22.57 ? 319  ILE B N   1 
ATOM   8310  C  CA  . ILE B  1 319 ? -5.586  81.684 33.211 1.00 23.48 ? 319  ILE B CA  1 
ATOM   8311  C  C   . ILE B  1 319 ? -6.989  81.081 33.078 1.00 23.88 ? 319  ILE B C   1 
ATOM   8312  O  O   . ILE B  1 319 ? -7.930  81.760 32.670 1.00 25.44 ? 319  ILE B O   1 
ATOM   8313  C  CB  . ILE B  1 319 ? -5.693  83.151 33.641 1.00 24.01 ? 319  ILE B CB  1 
ATOM   8314  C  CG1 . ILE B  1 319 ? -4.312  83.798 33.598 1.00 23.36 ? 319  ILE B CG1 1 
ATOM   8315  C  CG2 . ILE B  1 319 ? -6.258  83.235 35.055 1.00 25.68 ? 319  ILE B CG2 1 
ATOM   8316  C  CD1 . ILE B  1 319 ? -3.293  83.043 34.392 1.00 24.07 ? 319  ILE B CD1 1 
ATOM   8317  N  N   . GLN B  1 320 ? -7.111  79.808 33.429 1.00 22.80 ? 320  GLN B N   1 
ATOM   8318  C  CA  . GLN B  1 320 ? -8.340  79.043 33.241 1.00 22.97 ? 320  GLN B CA  1 
ATOM   8319  C  C   . GLN B  1 320 ? -9.647  79.331 33.976 1.00 23.39 ? 320  GLN B C   1 
ATOM   8320  O  O   . GLN B  1 320 ? -10.346 78.413 34.409 1.00 23.79 ? 320  GLN B O   1 
ATOM   8321  C  CB  . GLN B  1 320 ? -7.990  77.574 33.391 1.00 20.38 ? 320  GLN B CB  1 
ATOM   8322  C  CG  . GLN B  1 320 ? -6.937  77.156 32.413 1.00 19.06 ? 320  GLN B CG  1 
ATOM   8323  C  CD  . GLN B  1 320 ? -6.571  75.706 32.581 1.00 19.50 ? 320  GLN B CD  1 
ATOM   8324  O  OE1 . GLN B  1 320 ? -7.443  74.836 32.697 1.00 16.84 ? 320  GLN B OE1 1 
ATOM   8325  N  NE2 . GLN B  1 320 ? -5.277  75.433 32.593 1.00 16.27 ? 320  GLN B NE2 1 
ATOM   8326  N  N   . ASN B  1 321 ? -10.010 80.594 34.091 1.00 24.86 ? 321  ASN B N   1 
ATOM   8327  C  CA  . ASN B  1 321 ? -11.258 80.909 34.775 1.00 26.74 ? 321  ASN B CA  1 
ATOM   8328  C  C   . ASN B  1 321 ? -12.160 81.734 33.865 1.00 26.02 ? 321  ASN B C   1 
ATOM   8329  O  O   . ASN B  1 321 ? -13.124 82.345 34.312 1.00 25.37 ? 321  ASN B O   1 
ATOM   8330  C  CB  . ASN B  1 321 ? -10.946 81.655 36.057 1.00 28.79 ? 321  ASN B CB  1 
ATOM   8331  C  CG  . ASN B  1 321 ? -10.340 83.004 35.801 1.00 31.82 ? 321  ASN B CG  1 
ATOM   8332  O  OD1 . ASN B  1 321 ? -9.753  83.283 34.753 1.00 30.04 ? 321  ASN B OD1 1 
ATOM   8333  N  ND2 . ASN B  1 321 ? -10.495 83.851 36.803 1.00 38.69 ? 321  ASN B ND2 1 
ATOM   8334  N  N   . TYR B  1 322 ? -11.832 81.724 32.576 1.00 26.07 ? 322  TYR B N   1 
ATOM   8335  C  CA  . TYR B  1 322 ? -12.592 82.441 31.580 1.00 25.48 ? 322  TYR B CA  1 
ATOM   8336  C  C   . TYR B  1 322 ? -12.567 81.674 30.248 1.00 25.80 ? 322  TYR B C   1 
ATOM   8337  O  O   . TYR B  1 322 ? -11.500 81.436 29.675 1.00 24.79 ? 322  TYR B O   1 
ATOM   8338  C  CB  . TYR B  1 322 ? -12.000 83.830 31.415 1.00 26.03 ? 322  TYR B CB  1 
ATOM   8339  C  CG  . TYR B  1 322 ? -12.823 84.780 30.579 1.00 26.63 ? 322  TYR B CG  1 
ATOM   8340  C  CD1 . TYR B  1 322 ? -12.588 84.921 29.213 1.00 27.23 ? 322  TYR B CD1 1 
ATOM   8341  C  CD2 . TYR B  1 322 ? -13.813 85.578 31.169 1.00 28.05 ? 322  TYR B CD2 1 
ATOM   8342  C  CE1 . TYR B  1 322 ? -13.314 85.839 28.443 1.00 28.62 ? 322  TYR B CE1 1 
ATOM   8343  C  CE2 . TYR B  1 322 ? -14.554 86.505 30.407 1.00 29.07 ? 322  TYR B CE2 1 
ATOM   8344  C  CZ  . TYR B  1 322 ? -14.296 86.624 29.049 1.00 29.14 ? 322  TYR B CZ  1 
ATOM   8345  O  OH  . TYR B  1 322 ? -15.029 87.503 28.298 1.00 31.09 ? 322  TYR B OH  1 
ATOM   8346  N  N   . SER B  1 323 ? -13.745 81.271 29.767 1.00 24.87 ? 323  SER B N   1 
ATOM   8347  C  CA  . SER B  1 323 ? -13.843 80.532 28.512 1.00 24.66 ? 323  SER B CA  1 
ATOM   8348  C  C   . SER B  1 323 ? -14.919 81.135 27.629 1.00 25.13 ? 323  SER B C   1 
ATOM   8349  O  O   . SER B  1 323 ? -15.884 81.727 28.108 1.00 25.82 ? 323  SER B O   1 
ATOM   8350  C  CB  . SER B  1 323 ? -14.155 79.053 28.770 1.00 23.80 ? 323  SER B CB  1 
ATOM   8351  O  OG  . SER B  1 323 ? -15.443 78.896 29.327 1.00 26.02 ? 323  SER B OG  1 
ATOM   8352  N  N   . VAL B  1 324 ? -14.753 80.974 26.328 1.00 24.60 ? 324  VAL B N   1 
ATOM   8353  C  CA  . VAL B  1 324 ? -15.696 81.526 25.374 1.00 24.69 ? 324  VAL B CA  1 
ATOM   8354  C  C   . VAL B  1 324 ? -16.106 80.476 24.351 1.00 24.10 ? 324  VAL B C   1 
ATOM   8355  O  O   . VAL B  1 324 ? -15.274 79.733 23.826 1.00 24.91 ? 324  VAL B O   1 
ATOM   8356  C  CB  . VAL B  1 324 ? -15.068 82.721 24.613 1.00 25.01 ? 324  VAL B CB  1 
ATOM   8357  C  CG1 . VAL B  1 324 ? -16.065 83.296 23.648 1.00 26.17 ? 324  VAL B CG1 1 
ATOM   8358  C  CG2 . VAL B  1 324 ? -14.618 83.799 25.591 1.00 26.80 ? 324  VAL B CG2 1 
ATOM   8359  N  N   . MET B  1 325 ? -17.394 80.420 24.063 1.00 23.33 ? 325  MET B N   1 
ATOM   8360  C  CA  . MET B  1 325 ? -17.888 79.497 23.072 1.00 21.46 ? 325  MET B CA  1 
ATOM   8361  C  C   . MET B  1 325 ? -18.405 80.280 21.874 1.00 21.55 ? 325  MET B C   1 
ATOM   8362  O  O   . MET B  1 325 ? -19.254 81.158 22.025 1.00 20.14 ? 325  MET B O   1 
ATOM   8363  C  CB  . MET B  1 325 ? -19.019 78.648 23.634 1.00 23.27 ? 325  MET B CB  1 
ATOM   8364  C  CG  . MET B  1 325 ? -19.676 77.769 22.578 1.00 24.51 ? 325  MET B CG  1 
ATOM   8365  S  SD  . MET B  1 325 ? -21.150 77.041 23.226 1.00 28.98 ? 325  MET B SD  1 
ATOM   8366  C  CE  . MET B  1 325 ? -21.881 76.413 21.773 1.00 29.64 ? 325  MET B CE  1 
ATOM   8367  N  N   . ASP B  1 326 ? -17.863 79.968 20.697 1.00 19.73 ? 326  ASP B N   1 
ATOM   8368  C  CA  . ASP B  1 326 ? -18.287 80.577 19.450 1.00 20.56 ? 326  ASP B CA  1 
ATOM   8369  C  C   . ASP B  1 326 ? -19.150 79.552 18.719 1.00 20.77 ? 326  ASP B C   1 
ATOM   8370  O  O   . ASP B  1 326 ? -18.888 78.348 18.773 1.00 18.81 ? 326  ASP B O   1 
ATOM   8371  C  CB  . ASP B  1 326 ? -17.091 80.914 18.540 1.00 21.63 ? 326  ASP B CB  1 
ATOM   8372  C  CG  . ASP B  1 326 ? -16.637 82.352 18.668 1.00 23.60 ? 326  ASP B CG  1 
ATOM   8373  O  OD1 . ASP B  1 326 ? -17.490 83.230 18.926 1.00 24.55 ? 326  ASP B OD1 1 
ATOM   8374  O  OD2 . ASP B  1 326 ? -15.421 82.610 18.497 1.00 24.46 ? 326  ASP B OD2 1 
ATOM   8375  N  N   . ILE B  1 327 ? -20.165 80.036 18.020 1.00 20.02 ? 327  ILE B N   1 
ATOM   8376  C  CA  . ILE B  1 327 ? -21.044 79.171 17.248 1.00 20.65 ? 327  ILE B CA  1 
ATOM   8377  C  C   . ILE B  1 327 ? -20.948 79.716 15.832 1.00 21.62 ? 327  ILE B C   1 
ATOM   8378  O  O   . ILE B  1 327 ? -21.330 80.855 15.551 1.00 21.94 ? 327  ILE B O   1 
ATOM   8379  C  CB  . ILE B  1 327 ? -22.456 79.196 17.844 1.00 20.08 ? 327  ILE B CB  1 
ATOM   8380  C  CG1 . ILE B  1 327 ? -22.382 78.585 19.252 1.00 20.00 ? 327  ILE B CG1 1 
ATOM   8381  C  CG2 . ILE B  1 327 ? -23.429 78.408 16.977 1.00 17.80 ? 327  ILE B CG2 1 
ATOM   8382  C  CD1 . ILE B  1 327 ? -23.694 78.505 19.971 1.00 20.01 ? 327  ILE B CD1 1 
ATOM   8383  N  N   . CYS B  1 328 ? -20.403 78.893 14.945 1.00 22.51 ? 328  CYS B N   1 
ATOM   8384  C  CA  . CYS B  1 328 ? -20.128 79.320 13.583 1.00 23.28 ? 328  CYS B CA  1 
ATOM   8385  C  C   . CYS B  1 328 ? -20.911 78.640 12.477 1.00 23.85 ? 328  CYS B C   1 
ATOM   8386  O  O   . CYS B  1 328 ? -21.018 77.418 12.424 1.00 24.16 ? 328  CYS B O   1 
ATOM   8387  C  CB  . CYS B  1 328 ? -18.634 79.140 13.347 1.00 24.93 ? 328  CYS B CB  1 
ATOM   8388  S  SG  . CYS B  1 328 ? -17.627 79.662 14.776 1.00 26.68 ? 328  CYS B SG  1 
ATOM   8389  N  N   . ASP B  1 329 ? -21.431 79.465 11.579 1.00 24.42 ? 329  ASP B N   1 
ATOM   8390  C  CA  . ASP B  1 329 ? -22.236 79.005 10.468 1.00 24.95 ? 329  ASP B CA  1 
ATOM   8391  C  C   . ASP B  1 329 ? -21.528 79.084 9.132  1.00 25.58 ? 329  ASP B C   1 
ATOM   8392  O  O   . ASP B  1 329 ? -20.795 80.039 8.856  1.00 24.80 ? 329  ASP B O   1 
ATOM   8393  C  CB  . ASP B  1 329 ? -23.527 79.827 10.405 1.00 25.09 ? 329  ASP B CB  1 
ATOM   8394  C  CG  . ASP B  1 329 ? -24.548 79.383 11.430 1.00 25.88 ? 329  ASP B CG  1 
ATOM   8395  O  OD1 . ASP B  1 329 ? -24.174 78.650 12.374 1.00 28.16 ? 329  ASP B OD1 1 
ATOM   8396  O  OD2 . ASP B  1 329 ? -25.727 79.764 11.295 1.00 26.03 ? 329  ASP B OD2 1 
ATOM   8397  N  N   . TYR B  1 330 ? -21.746 78.071 8.303  1.00 26.03 ? 330  TYR B N   1 
ATOM   8398  C  CA  . TYR B  1 330 ? -21.153 78.053 6.976  1.00 28.17 ? 330  TYR B CA  1 
ATOM   8399  C  C   . TYR B  1 330 ? -21.904 79.053 6.090  1.00 29.28 ? 330  TYR B C   1 
ATOM   8400  O  O   . TYR B  1 330 ? -23.132 79.061 6.061  1.00 27.92 ? 330  TYR B O   1 
ATOM   8401  C  CB  . TYR B  1 330 ? -21.263 76.661 6.362  1.00 27.71 ? 330  TYR B CB  1 
ATOM   8402  C  CG  . TYR B  1 330 ? -20.675 76.592 4.972  1.00 29.45 ? 330  TYR B CG  1 
ATOM   8403  C  CD1 . TYR B  1 330 ? -19.317 76.838 4.757  1.00 29.85 ? 330  TYR B CD1 1 
ATOM   8404  C  CD2 . TYR B  1 330 ? -21.471 76.281 3.870  1.00 30.98 ? 330  TYR B CD2 1 
ATOM   8405  C  CE1 . TYR B  1 330 ? -18.768 76.775 3.479  1.00 30.58 ? 330  TYR B CE1 1 
ATOM   8406  C  CE2 . TYR B  1 330 ? -20.932 76.210 2.583  1.00 30.77 ? 330  TYR B CE2 1 
ATOM   8407  C  CZ  . TYR B  1 330 ? -19.585 76.458 2.395  1.00 31.11 ? 330  TYR B CZ  1 
ATOM   8408  O  OH  . TYR B  1 330 ? -19.048 76.391 1.126  1.00 32.03 ? 330  TYR B OH  1 
ATOM   8409  N  N   . ASP B  1 331 ? -21.153 79.884 5.377  1.00 31.81 ? 331  ASP B N   1 
ATOM   8410  C  CA  . ASP B  1 331 ? -21.700 80.888 4.462  1.00 34.76 ? 331  ASP B CA  1 
ATOM   8411  C  C   . ASP B  1 331 ? -21.549 80.330 3.042  1.00 36.54 ? 331  ASP B C   1 
ATOM   8412  O  O   . ASP B  1 331 ? -20.468 80.376 2.458  1.00 35.71 ? 331  ASP B O   1 
ATOM   8413  C  CB  . ASP B  1 331 ? -20.906 82.186 4.601  1.00 36.41 ? 331  ASP B CB  1 
ATOM   8414  C  CG  . ASP B  1 331 ? -21.403 83.285 3.677  1.00 39.20 ? 331  ASP B CG  1 
ATOM   8415  O  OD1 . ASP B  1 331 ? -22.051 82.967 2.654  1.00 40.92 ? 331  ASP B OD1 1 
ATOM   8416  O  OD2 . ASP B  1 331 ? -21.130 84.468 3.972  1.00 40.78 ? 331  ASP B OD2 1 
ATOM   8417  N  N   . GLU B  1 332 ? -22.640 79.803 2.500  1.00 39.10 ? 332  GLU B N   1 
ATOM   8418  C  CA  . GLU B  1 332 ? -22.650 79.182 1.181  1.00 42.20 ? 332  GLU B CA  1 
ATOM   8419  C  C   . GLU B  1 332 ? -22.183 80.066 0.033  1.00 43.56 ? 332  GLU B C   1 
ATOM   8420  O  O   . GLU B  1 332 ? -21.710 79.557 -0.984 1.00 44.21 ? 332  GLU B O   1 
ATOM   8421  C  CB  . GLU B  1 332 ? -24.054 78.658 0.868  1.00 44.26 ? 332  GLU B CB  1 
ATOM   8422  C  CG  . GLU B  1 332 ? -24.099 77.504 -0.126 1.00 48.54 ? 332  GLU B CG  1 
ATOM   8423  C  CD  . GLU B  1 332 ? -25.511 76.938 -0.311 1.00 51.34 ? 332  GLU B CD  1 
ATOM   8424  O  OE1 . GLU B  1 332 ? -26.179 76.638 0.708  1.00 52.70 ? 332  GLU B OE1 1 
ATOM   8425  O  OE2 . GLU B  1 332 ? -25.954 76.778 -1.477 1.00 53.36 ? 332  GLU B OE2 1 
ATOM   8426  N  N   . SER B  1 333 ? -22.300 81.381 0.184  1.00 44.01 ? 333  SER B N   1 
ATOM   8427  C  CA  . SER B  1 333 ? -21.902 82.276 -0.896 1.00 45.01 ? 333  SER B CA  1 
ATOM   8428  C  C   . SER B  1 333 ? -20.415 82.598 -0.917 1.00 45.34 ? 333  SER B C   1 
ATOM   8429  O  O   . SER B  1 333 ? -19.860 82.848 -1.984 1.00 46.21 ? 333  SER B O   1 
ATOM   8430  C  CB  . SER B  1 333 ? -22.709 83.575 -0.836 1.00 44.98 ? 333  SER B CB  1 
ATOM   8431  O  OG  . SER B  1 333 ? -22.295 84.371 0.256  1.00 46.90 ? 333  SER B OG  1 
ATOM   8432  N  N   . SER B  1 334 ? -19.771 82.600 0.251  1.00 45.22 ? 334  SER B N   1 
ATOM   8433  C  CA  . SER B  1 334 ? -18.338 82.890 0.341  1.00 43.54 ? 334  SER B CA  1 
ATOM   8434  C  C   . SER B  1 334 ? -17.529 81.638 0.679  1.00 42.24 ? 334  SER B C   1 
ATOM   8435  O  O   . SER B  1 334 ? -16.311 81.630 0.582  1.00 42.57 ? 334  SER B O   1 
ATOM   8436  C  CB  . SER B  1 334 ? -18.069 83.965 1.405  1.00 44.44 ? 334  SER B CB  1 
ATOM   8437  O  OG  . SER B  1 334 ? -18.279 83.474 2.730  1.00 46.57 ? 334  SER B OG  1 
ATOM   8438  N  N   . GLY B  1 335 ? -18.212 80.575 1.072  1.00 41.37 ? 335  GLY B N   1 
ATOM   8439  C  CA  . GLY B  1 335 ? -17.510 79.359 1.424  1.00 39.49 ? 335  GLY B CA  1 
ATOM   8440  C  C   . GLY B  1 335 ? -16.714 79.556 2.701  1.00 38.29 ? 335  GLY B C   1 
ATOM   8441  O  O   . GLY B  1 335 ? -15.826 78.765 3.013  1.00 39.39 ? 335  GLY B O   1 
ATOM   8442  N  N   . ARG B  1 336 ? -17.039 80.612 3.438  1.00 36.37 ? 336  ARG B N   1 
ATOM   8443  C  CA  . ARG B  1 336 ? -16.362 80.937 4.689  1.00 34.52 ? 336  ARG B CA  1 
ATOM   8444  C  C   . ARG B  1 336 ? -17.193 80.548 5.921  1.00 32.02 ? 336  ARG B C   1 
ATOM   8445  O  O   . ARG B  1 336 ? -18.359 80.145 5.803  1.00 30.03 ? 336  ARG B O   1 
ATOM   8446  C  CB  . ARG B  1 336 ? -16.086 82.438 4.732  1.00 37.15 ? 336  ARG B CB  1 
ATOM   8447  C  CG  . ARG B  1 336 ? -15.356 82.987 3.505  1.00 39.91 ? 336  ARG B CG  1 
ATOM   8448  C  CD  . ARG B  1 336 ? -13.895 82.593 3.518  1.00 41.89 ? 336  ARG B CD  1 
ATOM   8449  N  NE  . ARG B  1 336 ? -13.294 82.862 4.828  1.00 44.36 ? 336  ARG B NE  1 
ATOM   8450  C  CZ  . ARG B  1 336 ? -12.011 82.663 5.129  1.00 44.12 ? 336  ARG B CZ  1 
ATOM   8451  N  NH1 . ARG B  1 336 ? -11.170 82.198 4.212  1.00 42.69 ? 336  ARG B NH1 1 
ATOM   8452  N  NH2 . ARG B  1 336 ? -11.580 82.900 6.365  1.00 44.89 ? 336  ARG B NH2 1 
ATOM   8453  N  N   . TRP B  1 337 ? -16.583 80.675 7.098  1.00 29.08 ? 337  TRP B N   1 
ATOM   8454  C  CA  . TRP B  1 337 ? -17.261 80.369 8.350  1.00 27.75 ? 337  TRP B CA  1 
ATOM   8455  C  C   . TRP B  1 337 ? -17.351 81.627 9.206  1.00 28.90 ? 337  TRP B C   1 
ATOM   8456  O  O   . TRP B  1 337 ? -16.349 82.276 9.486  1.00 30.18 ? 337  TRP B O   1 
ATOM   8457  C  CB  . TRP B  1 337 ? -16.533 79.259 9.105  1.00 23.65 ? 337  TRP B CB  1 
ATOM   8458  C  CG  . TRP B  1 337 ? -16.690 77.916 8.445  1.00 19.61 ? 337  TRP B CG  1 
ATOM   8459  C  CD1 . TRP B  1 337 ? -15.947 77.410 7.407  1.00 18.00 ? 337  TRP B CD1 1 
ATOM   8460  C  CD2 . TRP B  1 337 ? -17.690 76.945 8.730  1.00 17.90 ? 337  TRP B CD2 1 
ATOM   8461  N  NE1 . TRP B  1 337 ? -16.431 76.180 7.030  1.00 17.62 ? 337  TRP B NE1 1 
ATOM   8462  C  CE2 . TRP B  1 337 ? -17.501 75.870 7.828  1.00 18.30 ? 337  TRP B CE2 1 
ATOM   8463  C  CE3 . TRP B  1 337 ? -18.736 76.874 9.662  1.00 17.81 ? 337  TRP B CE3 1 
ATOM   8464  C  CZ2 . TRP B  1 337 ? -18.322 74.738 7.833  1.00 18.85 ? 337  TRP B CZ2 1 
ATOM   8465  C  CZ3 . TRP B  1 337 ? -19.549 75.750 9.663  1.00 17.41 ? 337  TRP B CZ3 1 
ATOM   8466  C  CH2 . TRP B  1 337 ? -19.341 74.698 8.758  1.00 18.37 ? 337  TRP B CH2 1 
ATOM   8467  N  N   . ASN B  1 338 ? -18.557 81.971 9.625  1.00 29.46 ? 338  ASN B N   1 
ATOM   8468  C  CA  . ASN B  1 338 ? -18.743 83.174 10.423 1.00 30.47 ? 338  ASN B CA  1 
ATOM   8469  C  C   . ASN B  1 338 ? -19.386 82.872 11.766 1.00 29.23 ? 338  ASN B C   1 
ATOM   8470  O  O   . ASN B  1 338 ? -20.381 82.152 11.844 1.00 28.51 ? 338  ASN B O   1 
ATOM   8471  C  CB  . ASN B  1 338 ? -19.606 84.179 9.641  1.00 32.59 ? 338  ASN B CB  1 
ATOM   8472  C  CG  . ASN B  1 338 ? -18.897 84.716 8.392  1.00 35.36 ? 338  ASN B CG  1 
ATOM   8473  O  OD1 . ASN B  1 338 ? -19.481 84.767 7.296  1.00 36.25 ? 338  ASN B OD1 1 
ATOM   8474  N  ND2 . ASN B  1 338 ? -17.640 85.129 8.556  1.00 34.89 ? 338  ASN B ND2 1 
ATOM   8475  N  N   . CYS B  1 339 ? -18.814 83.437 12.820 1.00 28.38 ? 339  CYS B N   1 
ATOM   8476  C  CA  . CYS B  1 339 ? -19.346 83.235 14.160 1.00 28.37 ? 339  CYS B CA  1 
ATOM   8477  C  C   . CYS B  1 339 ? -19.892 84.574 14.689 1.00 28.13 ? 339  CYS B C   1 
ATOM   8478  O  O   . CYS B  1 339 ? -19.131 85.467 15.069 1.00 27.44 ? 339  CYS B O   1 
ATOM   8479  C  CB  . CYS B  1 339 ? -18.242 82.690 15.075 1.00 27.82 ? 339  CYS B CB  1 
ATOM   8480  S  SG  . CYS B  1 339 ? -17.043 81.549 14.248 1.00 30.19 ? 339  CYS B SG  1 
ATOM   8481  N  N   . LEU B  1 340 ? -21.217 84.717 14.684 1.00 27.73 ? 340  LEU B N   1 
ATOM   8482  C  CA  . LEU B  1 340 ? -21.873 85.944 15.149 1.00 26.16 ? 340  LEU B CA  1 
ATOM   8483  C  C   . LEU B  1 340 ? -21.655 86.146 16.635 1.00 25.30 ? 340  LEU B C   1 
ATOM   8484  O  O   . LEU B  1 340 ? -21.935 85.262 17.447 1.00 23.74 ? 340  LEU B O   1 
ATOM   8485  C  CB  . LEU B  1 340 ? -23.378 85.878 14.860 1.00 28.10 ? 340  LEU B CB  1 
ATOM   8486  C  CG  . LEU B  1 340 ? -23.775 85.928 13.385 1.00 28.58 ? 340  LEU B CG  1 
ATOM   8487  C  CD1 . LEU B  1 340 ? -25.183 85.416 13.199 1.00 29.11 ? 340  LEU B CD1 1 
ATOM   8488  C  CD2 . LEU B  1 340 ? -23.636 87.352 12.894 1.00 29.22 ? 340  LEU B CD2 1 
ATOM   8489  N  N   . VAL B  1 341 ? -21.166 87.324 16.989 1.00 24.27 ? 341  VAL B N   1 
ATOM   8490  C  CA  . VAL B  1 341 ? -20.900 87.624 18.371 1.00 23.19 ? 341  VAL B CA  1 
ATOM   8491  C  C   . VAL B  1 341 ? -22.142 87.470 19.238 1.00 22.08 ? 341  VAL B C   1 
ATOM   8492  O  O   . VAL B  1 341 ? -22.040 87.133 20.414 1.00 21.41 ? 341  VAL B O   1 
ATOM   8493  C  CB  . VAL B  1 341 ? -20.255 89.030 18.507 1.00 25.92 ? 341  VAL B CB  1 
ATOM   8494  C  CG1 . VAL B  1 341 ? -21.049 90.038 17.688 1.00 28.87 ? 341  VAL B CG1 1 
ATOM   8495  C  CG2 . VAL B  1 341 ? -20.171 89.440 19.982 1.00 25.65 ? 341  VAL B CG2 1 
ATOM   8496  N  N   . ALA B  1 342 ? -23.320 87.660 18.660 1.00 22.03 ? 342  ALA B N   1 
ATOM   8497  C  CA  . ALA B  1 342 ? -24.554 87.505 19.430 1.00 21.68 ? 342  ALA B CA  1 
ATOM   8498  C  C   . ALA B  1 342 ? -24.806 86.034 19.779 1.00 22.83 ? 342  ALA B C   1 
ATOM   8499  O  O   . ALA B  1 342 ? -25.721 85.728 20.544 1.00 21.49 ? 342  ALA B O   1 
ATOM   8500  C  CB  . ALA B  1 342 ? -25.751 88.069 18.653 1.00 21.46 ? 342  ALA B CB  1 
ATOM   8501  N  N   . ARG B  1 343 ? -23.988 85.132 19.230 1.00 23.20 ? 343  ARG B N   1 
ATOM   8502  C  CA  . ARG B  1 343 ? -24.138 83.705 19.505 1.00 24.02 ? 343  ARG B CA  1 
ATOM   8503  C  C   . ARG B  1 343 ? -22.991 83.205 20.344 1.00 24.90 ? 343  ARG B C   1 
ATOM   8504  O  O   . ARG B  1 343 ? -22.823 81.999 20.538 1.00 25.73 ? 343  ARG B O   1 
ATOM   8505  C  CB  . ARG B  1 343 ? -24.190 82.899 18.205 1.00 24.44 ? 343  ARG B CB  1 
ATOM   8506  C  CG  . ARG B  1 343 ? -25.470 83.088 17.425 1.00 24.89 ? 343  ARG B CG  1 
ATOM   8507  C  CD  . ARG B  1 343 ? -25.399 82.371 16.081 1.00 26.60 ? 343  ARG B CD  1 
ATOM   8508  N  NE  . ARG B  1 343 ? -26.685 82.432 15.393 1.00 27.38 ? 343  ARG B NE  1 
ATOM   8509  C  CZ  . ARG B  1 343 ? -26.882 82.099 14.120 1.00 29.50 ? 343  ARG B CZ  1 
ATOM   8510  N  NH1 . ARG B  1 343 ? -25.870 81.676 13.370 1.00 29.39 ? 343  ARG B NH1 1 
ATOM   8511  N  NH2 . ARG B  1 343 ? -28.099 82.190 13.597 1.00 30.09 ? 343  ARG B NH2 1 
ATOM   8512  N  N   . GLN B  1 344 ? -22.196 84.145 20.834 1.00 25.14 ? 344  GLN B N   1 
ATOM   8513  C  CA  . GLN B  1 344 ? -21.023 83.851 21.651 1.00 24.92 ? 344  GLN B CA  1 
ATOM   8514  C  C   . GLN B  1 344 ? -21.432 83.689 23.109 1.00 26.42 ? 344  GLN B C   1 
ATOM   8515  O  O   . GLN B  1 344 ? -22.178 84.517 23.630 1.00 28.86 ? 344  GLN B O   1 
ATOM   8516  C  CB  . GLN B  1 344 ? -20.046 85.011 21.522 1.00 23.29 ? 344  GLN B CB  1 
ATOM   8517  C  CG  . GLN B  1 344 ? -18.628 84.720 21.897 1.00 24.48 ? 344  GLN B CG  1 
ATOM   8518  C  CD  . GLN B  1 344 ? -17.732 85.922 21.637 1.00 24.76 ? 344  GLN B CD  1 
ATOM   8519  O  OE1 . GLN B  1 344 ? -17.664 86.842 22.446 1.00 25.50 ? 344  GLN B OE1 1 
ATOM   8520  N  NE2 . GLN B  1 344 ? -17.055 85.923 20.496 1.00 24.19 ? 344  GLN B NE2 1 
ATOM   8521  N  N   . HIS B  1 345 ? -20.955 82.638 23.771 1.00 24.46 ? 345  HIS B N   1 
ATOM   8522  C  CA  . HIS B  1 345 ? -21.293 82.430 25.168 1.00 24.76 ? 345  HIS B CA  1 
ATOM   8523  C  C   . HIS B  1 345 ? -20.077 82.442 26.076 1.00 26.37 ? 345  HIS B C   1 
ATOM   8524  O  O   . HIS B  1 345 ? -19.089 81.749 25.829 1.00 27.33 ? 345  HIS B O   1 
ATOM   8525  C  CB  . HIS B  1 345 ? -22.072 81.134 25.319 1.00 21.95 ? 345  HIS B CB  1 
ATOM   8526  C  CG  . HIS B  1 345 ? -23.356 81.129 24.543 1.00 19.94 ? 345  HIS B CG  1 
ATOM   8527  N  ND1 . HIS B  1 345 ? -24.560 81.499 25.098 1.00 18.48 ? 345  HIS B ND1 1 
ATOM   8528  C  CD2 . HIS B  1 345 ? -23.603 80.878 23.236 1.00 17.33 ? 345  HIS B CD2 1 
ATOM   8529  C  CE1 . HIS B  1 345 ? -25.498 81.478 24.166 1.00 17.02 ? 345  HIS B CE1 1 
ATOM   8530  N  NE2 . HIS B  1 345 ? -24.941 81.104 23.028 1.00 19.34 ? 345  HIS B NE2 1 
ATOM   8531  N  N   . ILE B  1 346 ? -20.161 83.242 27.130 1.00 26.14 ? 346  ILE B N   1 
ATOM   8532  C  CA  . ILE B  1 346 ? -19.079 83.381 28.092 1.00 27.43 ? 346  ILE B CA  1 
ATOM   8533  C  C   . ILE B  1 346 ? -19.372 82.543 29.334 1.00 28.92 ? 346  ILE B C   1 
ATOM   8534  O  O   . ILE B  1 346 ? -20.507 82.497 29.816 1.00 28.99 ? 346  ILE B O   1 
ATOM   8535  C  CB  . ILE B  1 346 ? -18.906 84.851 28.493 1.00 27.36 ? 346  ILE B CB  1 
ATOM   8536  C  CG1 . ILE B  1 346 ? -18.423 85.647 27.271 1.00 28.09 ? 346  ILE B CG1 1 
ATOM   8537  C  CG2 . ILE B  1 346 ? -17.941 84.965 29.660 1.00 25.57 ? 346  ILE B CG2 1 
ATOM   8538  C  CD1 . ILE B  1 346 ? -18.332 87.143 27.504 1.00 32.01 ? 346  ILE B CD1 1 
ATOM   8539  N  N   . GLU B  1 347 ? -18.344 81.870 29.842 1.00 29.86 ? 347  GLU B N   1 
ATOM   8540  C  CA  . GLU B  1 347 ? -18.489 81.025 31.023 1.00 31.82 ? 347  GLU B CA  1 
ATOM   8541  C  C   . GLU B  1 347 ? -17.263 81.253 31.879 1.00 33.11 ? 347  GLU B C   1 
ATOM   8542  O  O   . GLU B  1 347 ? -16.192 80.756 31.548 1.00 34.64 ? 347  GLU B O   1 
ATOM   8543  C  CB  . GLU B  1 347 ? -18.581 79.551 30.605 1.00 31.18 ? 347  GLU B CB  1 
ATOM   8544  C  CG  . GLU B  1 347 ? -18.851 78.572 31.734 1.00 31.23 ? 347  GLU B CG  1 
ATOM   8545  C  CD  . GLU B  1 347 ? -18.969 77.133 31.239 1.00 31.94 ? 347  GLU B CD  1 
ATOM   8546  O  OE1 . GLU B  1 347 ? -19.368 76.949 30.070 1.00 32.07 ? 347  GLU B OE1 1 
ATOM   8547  O  OE2 . GLU B  1 347 ? -18.691 76.189 32.013 1.00 31.32 ? 347  GLU B OE2 1 
ATOM   8548  N  N   . MET B  1 348 ? -17.404 82.020 32.959 1.00 34.30 ? 348  MET B N   1 
ATOM   8549  C  CA  . MET B  1 348 ? -16.262 82.289 33.823 1.00 36.15 ? 348  MET B CA  1 
ATOM   8550  C  C   . MET B  1 348 ? -16.516 81.815 35.248 1.00 36.59 ? 348  MET B C   1 
ATOM   8551  O  O   . MET B  1 348 ? -17.640 81.474 35.601 1.00 36.81 ? 348  MET B O   1 
ATOM   8552  C  CB  . MET B  1 348 ? -15.916 83.788 33.796 1.00 38.30 ? 348  MET B CB  1 
ATOM   8553  C  CG  . MET B  1 348 ? -16.953 84.748 34.374 1.00 42.22 ? 348  MET B CG  1 
ATOM   8554  S  SD  . MET B  1 348 ? -16.750 86.454 33.687 1.00 49.30 ? 348  MET B SD  1 
ATOM   8555  C  CE  . MET B  1 348 ? -18.399 86.806 33.024 1.00 47.65 ? 348  MET B CE  1 
ATOM   8556  N  N   . SER B  1 349 ? -15.472 81.757 36.065 1.00 36.14 ? 349  SER B N   1 
ATOM   8557  C  CA  . SER B  1 349 ? -15.653 81.320 37.440 1.00 36.48 ? 349  SER B CA  1 
ATOM   8558  C  C   . SER B  1 349 ? -14.970 82.290 38.360 1.00 36.73 ? 349  SER B C   1 
ATOM   8559  O  O   . SER B  1 349 ? -13.849 82.743 38.086 1.00 37.20 ? 349  SER B O   1 
ATOM   8560  C  CB  . SER B  1 349 ? -15.080 79.916 37.681 1.00 36.28 ? 349  SER B CB  1 
ATOM   8561  O  OG  . SER B  1 349 ? -15.271 79.506 39.040 1.00 35.29 ? 349  SER B OG  1 
ATOM   8562  N  N   . THR B  1 350 ? -15.642 82.591 39.461 1.00 36.67 ? 350  THR B N   1 
ATOM   8563  C  CA  . THR B  1 350 ? -15.111 83.527 40.446 1.00 37.02 ? 350  THR B CA  1 
ATOM   8564  C  C   . THR B  1 350 ? -14.441 82.827 41.621 1.00 35.51 ? 350  THR B C   1 
ATOM   8565  O  O   . THR B  1 350 ? -13.575 83.402 42.262 1.00 36.32 ? 350  THR B O   1 
ATOM   8566  C  CB  . THR B  1 350 ? -16.239 84.431 40.988 1.00 36.91 ? 350  THR B CB  1 
ATOM   8567  O  OG1 . THR B  1 350 ? -17.219 83.624 41.665 1.00 36.12 ? 350  THR B OG1 1 
ATOM   8568  C  CG2 . THR B  1 350 ? -16.908 85.172 39.835 1.00 37.19 ? 350  THR B CG2 1 
ATOM   8569  N  N   . THR B  1 351 ? -14.834 81.584 41.885 1.00 34.28 ? 351  THR B N   1 
ATOM   8570  C  CA  . THR B  1 351 ? -14.272 80.824 43.000 1.00 33.17 ? 351  THR B CA  1 
ATOM   8571  C  C   . THR B  1 351 ? -13.118 79.873 42.623 1.00 32.50 ? 351  THR B C   1 
ATOM   8572  O  O   . THR B  1 351 ? -12.341 79.466 43.481 1.00 32.11 ? 351  THR B O   1 
ATOM   8573  C  CB  . THR B  1 351 ? -15.367 80.008 43.716 1.00 33.37 ? 351  THR B CB  1 
ATOM   8574  O  OG1 . THR B  1 351 ? -16.061 79.188 42.767 1.00 33.69 ? 351  THR B OG1 1 
ATOM   8575  C  CG2 . THR B  1 351 ? -16.362 80.941 44.397 1.00 33.26 ? 351  THR B CG2 1 
ATOM   8576  N  N   . GLY B  1 352 ? -13.015 79.517 41.347 1.00 31.52 ? 352  GLY B N   1 
ATOM   8577  C  CA  . GLY B  1 352 ? -11.953 78.624 40.921 1.00 30.27 ? 352  GLY B CA  1 
ATOM   8578  C  C   . GLY B  1 352 ? -11.740 78.637 39.417 1.00 29.40 ? 352  GLY B C   1 
ATOM   8579  O  O   . GLY B  1 352 ? -11.715 79.696 38.773 1.00 29.76 ? 352  GLY B O   1 
ATOM   8580  N  N   . TRP B  1 353 ? -11.581 77.451 38.850 1.00 27.16 ? 353  TRP B N   1 
ATOM   8581  C  CA  . TRP B  1 353 ? -11.370 77.306 37.408 1.00 24.77 ? 353  TRP B CA  1 
ATOM   8582  C  C   . TRP B  1 353 ? -12.737 77.034 36.758 1.00 23.95 ? 353  TRP B C   1 
ATOM   8583  O  O   . TRP B  1 353 ? -13.751 77.014 37.445 1.00 23.11 ? 353  TRP B O   1 
ATOM   8584  C  CB  . TRP B  1 353 ? -10.397 76.148 37.176 1.00 22.94 ? 353  TRP B CB  1 
ATOM   8585  C  CG  . TRP B  1 353 ? -10.814 74.859 37.854 1.00 22.40 ? 353  TRP B CG  1 
ATOM   8586  C  CD1 . TRP B  1 353 ? -11.509 73.832 37.289 1.00 22.99 ? 353  TRP B CD1 1 
ATOM   8587  C  CD2 . TRP B  1 353 ? -10.560 74.469 39.216 1.00 21.28 ? 353  TRP B CD2 1 
ATOM   8588  N  NE1 . TRP B  1 353 ? -11.700 72.828 38.205 1.00 21.93 ? 353  TRP B NE1 1 
ATOM   8589  C  CE2 . TRP B  1 353 ? -11.128 73.193 39.396 1.00 21.41 ? 353  TRP B CE2 1 
ATOM   8590  C  CE3 . TRP B  1 353 ? -9.904  75.078 40.298 1.00 20.77 ? 353  TRP B CE3 1 
ATOM   8591  C  CZ2 . TRP B  1 353 ? -11.065 72.504 40.619 1.00 21.86 ? 353  TRP B CZ2 1 
ATOM   8592  C  CZ3 . TRP B  1 353 ? -9.840  74.404 41.505 1.00 20.32 ? 353  TRP B CZ3 1 
ATOM   8593  C  CH2 . TRP B  1 353 ? -10.419 73.124 41.660 1.00 21.44 ? 353  TRP B CH2 1 
ATOM   8594  N  N   . VAL B  1 354 ? -12.781 76.842 35.449 1.00 23.13 ? 354  VAL B N   1 
ATOM   8595  C  CA  . VAL B  1 354 ? -14.061 76.577 34.793 1.00 22.41 ? 354  VAL B CA  1 
ATOM   8596  C  C   . VAL B  1 354 ? -14.170 75.097 34.430 1.00 21.78 ? 354  VAL B C   1 
ATOM   8597  O  O   . VAL B  1 354 ? -13.280 74.552 33.783 1.00 20.61 ? 354  VAL B O   1 
ATOM   8598  C  CB  . VAL B  1 354 ? -14.239 77.430 33.503 1.00 22.73 ? 354  VAL B CB  1 
ATOM   8599  C  CG1 . VAL B  1 354 ? -15.521 77.037 32.793 1.00 22.40 ? 354  VAL B CG1 1 
ATOM   8600  C  CG2 . VAL B  1 354 ? -14.296 78.925 33.854 1.00 24.48 ? 354  VAL B CG2 1 
ATOM   8601  N  N   . GLY B  1 355 ? -15.262 74.461 34.862 1.00 21.14 ? 355  GLY B N   1 
ATOM   8602  C  CA  . GLY B  1 355 ? -15.484 73.046 34.587 1.00 21.18 ? 355  GLY B CA  1 
ATOM   8603  C  C   . GLY B  1 355 ? -14.889 72.144 35.658 1.00 20.87 ? 355  GLY B C   1 
ATOM   8604  O  O   . GLY B  1 355 ? -14.206 72.622 36.550 1.00 21.81 ? 355  GLY B O   1 
ATOM   8605  N  N   . ARG B  1 356 ? -15.153 70.843 35.603 1.00 20.63 ? 356  ARG B N   1 
ATOM   8606  C  CA  . ARG B  1 356 ? -14.560 69.943 36.584 1.00 20.74 ? 356  ARG B CA  1 
ATOM   8607  C  C   . ARG B  1 356 ? -13.070 69.849 36.238 1.00 21.68 ? 356  ARG B C   1 
ATOM   8608  O  O   . ARG B  1 356 ? -12.215 70.068 37.098 1.00 22.76 ? 356  ARG B O   1 
ATOM   8609  C  CB  . ARG B  1 356 ? -15.223 68.559 36.532 1.00 20.76 ? 356  ARG B CB  1 
ATOM   8610  C  CG  . ARG B  1 356 ? -16.649 68.572 37.043 1.00 20.15 ? 356  ARG B CG  1 
ATOM   8611  C  CD  . ARG B  1 356 ? -17.158 67.185 37.360 1.00 20.12 ? 356  ARG B CD  1 
ATOM   8612  N  NE  . ARG B  1 356 ? -18.393 67.261 38.138 1.00 21.48 ? 356  ARG B NE  1 
ATOM   8613  C  CZ  . ARG B  1 356 ? -19.621 67.129 37.632 1.00 22.68 ? 356  ARG B CZ  1 
ATOM   8614  N  NH1 . ARG B  1 356 ? -19.805 66.905 36.340 1.00 21.28 ? 356  ARG B NH1 1 
ATOM   8615  N  NH2 . ARG B  1 356 ? -20.671 67.236 38.429 1.00 22.99 ? 356  ARG B NH2 1 
ATOM   8616  N  N   . PHE B  1 357 ? -12.772 69.538 34.974 1.00 20.72 ? 357  PHE B N   1 
ATOM   8617  C  CA  . PHE B  1 357 ? -11.398 69.448 34.492 1.00 21.09 ? 357  PHE B CA  1 
ATOM   8618  C  C   . PHE B  1 357 ? -11.251 70.320 33.253 1.00 21.83 ? 357  PHE B C   1 
ATOM   8619  O  O   . PHE B  1 357 ? -10.135 70.587 32.810 1.00 22.37 ? 357  PHE B O   1 
ATOM   8620  C  CB  . PHE B  1 357 ? -11.025 68.011 34.130 1.00 18.83 ? 357  PHE B CB  1 
ATOM   8621  C  CG  . PHE B  1 357 ? -10.787 67.135 35.319 1.00 19.66 ? 357  PHE B CG  1 
ATOM   8622  C  CD1 . PHE B  1 357 ? -9.589  67.218 36.027 1.00 18.17 ? 357  PHE B CD1 1 
ATOM   8623  C  CD2 . PHE B  1 357 ? -11.773 66.256 35.762 1.00 18.71 ? 357  PHE B CD2 1 
ATOM   8624  C  CE1 . PHE B  1 357 ? -9.371  66.440 37.158 1.00 19.05 ? 357  PHE B CE1 1 
ATOM   8625  C  CE2 . PHE B  1 357 ? -11.564 65.465 36.902 1.00 20.67 ? 357  PHE B CE2 1 
ATOM   8626  C  CZ  . PHE B  1 357 ? -10.364 65.561 37.603 1.00 19.75 ? 357  PHE B CZ  1 
ATOM   8627  N  N   . ARG B  1 358 ? -12.384 70.759 32.706 1.00 20.82 ? 358  ARG B N   1 
ATOM   8628  C  CA  . ARG B  1 358 ? -12.421 71.601 31.518 1.00 21.32 ? 358  ARG B CA  1 
ATOM   8629  C  C   . ARG B  1 358 ? -13.885 71.989 31.301 1.00 21.35 ? 358  ARG B C   1 
ATOM   8630  O  O   . ARG B  1 358 ? -14.796 71.294 31.756 1.00 21.75 ? 358  ARG B O   1 
ATOM   8631  C  CB  . ARG B  1 358 ? -11.946 70.803 30.286 1.00 22.00 ? 358  ARG B CB  1 
ATOM   8632  C  CG  . ARG B  1 358 ? -13.068 69.955 29.709 1.00 25.02 ? 358  ARG B CG  1 
ATOM   8633  C  CD  . ARG B  1 358 ? -12.626 68.778 28.843 1.00 26.82 ? 358  ARG B CD  1 
ATOM   8634  N  NE  . ARG B  1 358 ? -12.502 69.083 27.434 1.00 27.77 ? 358  ARG B NE  1 
ATOM   8635  C  CZ  . ARG B  1 358 ? -12.704 68.203 26.452 1.00 27.15 ? 358  ARG B CZ  1 
ATOM   8636  N  NH1 . ARG B  1 358 ? -13.041 66.945 26.719 1.00 24.12 ? 358  ARG B NH1 1 
ATOM   8637  N  NH2 . ARG B  1 358 ? -12.580 68.594 25.190 1.00 26.20 ? 358  ARG B NH2 1 
ATOM   8638  N  N   . PRO B  1 359 ? -14.133 73.089 30.583 1.00 20.92 ? 359  PRO B N   1 
ATOM   8639  C  CA  . PRO B  1 359 ? -15.533 73.472 30.354 1.00 21.52 ? 359  PRO B CA  1 
ATOM   8640  C  C   . PRO B  1 359 ? -16.311 72.314 29.724 1.00 22.23 ? 359  PRO B C   1 
ATOM   8641  O  O   . PRO B  1 359 ? -15.788 71.604 28.855 1.00 22.69 ? 359  PRO B O   1 
ATOM   8642  C  CB  . PRO B  1 359 ? -15.416 74.679 29.430 1.00 20.63 ? 359  PRO B CB  1 
ATOM   8643  C  CG  . PRO B  1 359 ? -14.098 75.284 29.844 1.00 21.50 ? 359  PRO B CG  1 
ATOM   8644  C  CD  . PRO B  1 359 ? -13.204 74.076 30.010 1.00 20.73 ? 359  PRO B CD  1 
ATOM   8645  N  N   . SER B  1 360 ? -17.549 72.113 30.170 1.00 22.71 ? 360  SER B N   1 
ATOM   8646  C  CA  . SER B  1 360 ? -18.384 71.012 29.667 1.00 24.95 ? 360  SER B CA  1 
ATOM   8647  C  C   . SER B  1 360 ? -18.796 71.170 28.202 1.00 24.87 ? 360  SER B C   1 
ATOM   8648  O  O   . SER B  1 360 ? -18.809 72.283 27.674 1.00 24.95 ? 360  SER B O   1 
ATOM   8649  C  CB  . SER B  1 360 ? -19.639 70.865 30.535 1.00 26.13 ? 360  SER B CB  1 
ATOM   8650  O  OG  . SER B  1 360 ? -20.419 72.058 30.502 1.00 29.48 ? 360  SER B OG  1 
ATOM   8651  N  N   . GLU B  1 361 ? -19.140 70.060 27.553 1.00 24.49 ? 361  GLU B N   1 
ATOM   8652  C  CA  . GLU B  1 361 ? -19.531 70.120 26.158 1.00 26.34 ? 361  GLU B CA  1 
ATOM   8653  C  C   . GLU B  1 361 ? -21.034 70.344 25.983 1.00 25.83 ? 361  GLU B C   1 
ATOM   8654  O  O   . GLU B  1 361 ? -21.851 69.899 26.794 1.00 26.37 ? 361  GLU B O   1 
ATOM   8655  C  CB  . GLU B  1 361 ? -19.084 68.855 25.411 1.00 28.21 ? 361  GLU B CB  1 
ATOM   8656  C  CG  . GLU B  1 361 ? -19.935 67.619 25.601 1.00 33.95 ? 361  GLU B CG  1 
ATOM   8657  C  CD  . GLU B  1 361 ? -19.964 67.108 27.041 1.00 37.70 ? 361  GLU B CD  1 
ATOM   8658  O  OE1 . GLU B  1 361 ? -19.055 67.458 27.847 1.00 37.74 ? 361  GLU B OE1 1 
ATOM   8659  O  OE2 . GLU B  1 361 ? -20.904 66.333 27.366 1.00 39.39 ? 361  GLU B OE2 1 
ATOM   8660  N  N   . PRO B  1 362 ? -21.415 71.055 24.917 1.00 23.98 ? 362  PRO B N   1 
ATOM   8661  C  CA  . PRO B  1 362 ? -22.828 71.332 24.652 1.00 23.11 ? 362  PRO B CA  1 
ATOM   8662  C  C   . PRO B  1 362 ? -23.491 70.187 23.921 1.00 23.16 ? 362  PRO B C   1 
ATOM   8663  O  O   . PRO B  1 362 ? -22.831 69.441 23.197 1.00 23.22 ? 362  PRO B O   1 
ATOM   8664  C  CB  . PRO B  1 362 ? -22.770 72.585 23.787 1.00 23.45 ? 362  PRO B CB  1 
ATOM   8665  C  CG  . PRO B  1 362 ? -21.532 72.327 22.941 1.00 22.72 ? 362  PRO B CG  1 
ATOM   8666  C  CD  . PRO B  1 362 ? -20.541 71.766 23.961 1.00 22.71 ? 362  PRO B CD  1 
ATOM   8667  N  N   . HIS B  1 363 ? -24.799 70.050 24.112 1.00 22.81 ? 363  HIS B N   1 
ATOM   8668  C  CA  . HIS B  1 363 ? -25.579 69.020 23.429 1.00 22.76 ? 363  HIS B CA  1 
ATOM   8669  C  C   . HIS B  1 363 ? -26.677 69.796 22.720 1.00 22.82 ? 363  HIS B C   1 
ATOM   8670  O  O   . HIS B  1 363 ? -27.613 70.295 23.360 1.00 21.96 ? 363  HIS B O   1 
ATOM   8671  C  CB  . HIS B  1 363 ? -26.174 68.049 24.441 1.00 23.36 ? 363  HIS B CB  1 
ATOM   8672  C  CG  . HIS B  1 363 ? -25.142 67.224 25.147 1.00 24.18 ? 363  HIS B CG  1 
ATOM   8673  N  ND1 . HIS B  1 363 ? -24.952 65.883 24.881 1.00 23.60 ? 363  HIS B ND1 1 
ATOM   8674  C  CD2 . HIS B  1 363 ? -24.203 67.562 26.062 1.00 24.16 ? 363  HIS B CD2 1 
ATOM   8675  C  CE1 . HIS B  1 363 ? -23.943 65.433 25.603 1.00 23.46 ? 363  HIS B CE1 1 
ATOM   8676  N  NE2 . HIS B  1 363 ? -23.469 66.429 26.328 1.00 25.07 ? 363  HIS B NE2 1 
ATOM   8677  N  N   . PHE B  1 364 ? -26.548 69.913 21.403 1.00 21.12 ? 364  PHE B N   1 
ATOM   8678  C  CA  . PHE B  1 364 ? -27.520 70.647 20.606 1.00 22.14 ? 364  PHE B CA  1 
ATOM   8679  C  C   . PHE B  1 364 ? -28.779 69.877 20.240 1.00 22.47 ? 364  PHE B C   1 
ATOM   8680  O  O   . PHE B  1 364 ? -28.746 68.670 20.041 1.00 23.45 ? 364  PHE B O   1 
ATOM   8681  C  CB  . PHE B  1 364 ? -26.879 71.152 19.303 1.00 19.57 ? 364  PHE B CB  1 
ATOM   8682  C  CG  . PHE B  1 364 ? -25.778 72.165 19.514 1.00 18.61 ? 364  PHE B CG  1 
ATOM   8683  C  CD1 . PHE B  1 364 ? -24.488 71.751 19.849 1.00 17.25 ? 364  PHE B CD1 1 
ATOM   8684  C  CD2 . PHE B  1 364 ? -26.038 73.533 19.392 1.00 15.62 ? 364  PHE B CD2 1 
ATOM   8685  C  CE1 . PHE B  1 364 ? -23.473 72.686 20.058 1.00 17.46 ? 364  PHE B CE1 1 
ATOM   8686  C  CE2 . PHE B  1 364 ? -25.044 74.467 19.596 1.00 16.08 ? 364  PHE B CE2 1 
ATOM   8687  C  CZ  . PHE B  1 364 ? -23.748 74.046 19.934 1.00 17.61 ? 364  PHE B CZ  1 
ATOM   8688  N  N   . THR B  1 365 ? -29.890 70.598 20.156 1.00 24.13 ? 365  THR B N   1 
ATOM   8689  C  CA  . THR B  1 365 ? -31.160 70.008 19.741 1.00 24.86 ? 365  THR B CA  1 
ATOM   8690  C  C   . THR B  1 365 ? -30.993 69.815 18.238 1.00 24.30 ? 365  THR B C   1 
ATOM   8691  O  O   . THR B  1 365 ? -30.160 70.481 17.615 1.00 22.65 ? 365  THR B O   1 
ATOM   8692  C  CB  . THR B  1 365 ? -32.334 70.958 19.987 1.00 25.39 ? 365  THR B CB  1 
ATOM   8693  O  OG1 . THR B  1 365 ? -32.164 72.114 19.170 1.00 29.59 ? 365  THR B OG1 1 
ATOM   8694  C  CG2 . THR B  1 365 ? -32.361 71.411 21.435 1.00 24.95 ? 365  THR B CG2 1 
ATOM   8695  N  N   . LEU B  1 366 ? -31.786 68.920 17.664 1.00 24.71 ? 366  LEU B N   1 
ATOM   8696  C  CA  . LEU B  1 366 ? -31.717 68.608 16.237 1.00 26.03 ? 366  LEU B CA  1 
ATOM   8697  C  C   . LEU B  1 366 ? -31.565 69.808 15.289 1.00 25.42 ? 366  LEU B C   1 
ATOM   8698  O  O   . LEU B  1 366 ? -30.702 69.801 14.403 1.00 25.31 ? 366  LEU B O   1 
ATOM   8699  C  CB  . LEU B  1 366 ? -32.948 67.801 15.830 1.00 25.79 ? 366  LEU B CB  1 
ATOM   8700  C  CG  . LEU B  1 366 ? -32.944 67.299 14.383 1.00 26.91 ? 366  LEU B CG  1 
ATOM   8701  C  CD1 . LEU B  1 366 ? -31.708 66.437 14.122 1.00 26.67 ? 366  LEU B CD1 1 
ATOM   8702  C  CD2 . LEU B  1 366 ? -34.220 66.493 14.141 1.00 26.59 ? 366  LEU B CD2 1 
ATOM   8703  N  N   . ASP B  1 367 ? -32.394 70.830 15.473 1.00 24.88 ? 367  ASP B N   1 
ATOM   8704  C  CA  . ASP B  1 367 ? -32.328 72.003 14.609 1.00 25.03 ? 367  ASP B CA  1 
ATOM   8705  C  C   . ASP B  1 367 ? -31.126 72.913 14.893 1.00 23.61 ? 367  ASP B C   1 
ATOM   8706  O  O   . ASP B  1 367 ? -30.918 73.903 14.196 1.00 25.08 ? 367  ASP B O   1 
ATOM   8707  C  CB  . ASP B  1 367 ? -33.632 72.814 14.691 1.00 26.23 ? 367  ASP B CB  1 
ATOM   8708  C  CG  . ASP B  1 367 ? -33.853 73.458 16.060 1.00 30.18 ? 367  ASP B CG  1 
ATOM   8709  O  OD1 . ASP B  1 367 ? -32.925 73.442 16.908 1.00 29.56 ? 367  ASP B OD1 1 
ATOM   8710  O  OD2 . ASP B  1 367 ? -34.966 73.999 16.284 1.00 30.93 ? 367  ASP B OD2 1 
ATOM   8711  N  N   . GLY B  1 368 ? -30.347 72.572 15.914 1.00 21.61 ? 368  GLY B N   1 
ATOM   8712  C  CA  . GLY B  1 368 ? -29.171 73.349 16.257 1.00 20.18 ? 368  GLY B CA  1 
ATOM   8713  C  C   . GLY B  1 368 ? -29.409 74.763 16.759 1.00 20.44 ? 368  GLY B C   1 
ATOM   8714  O  O   . GLY B  1 368 ? -28.480 75.564 16.777 1.00 19.13 ? 368  GLY B O   1 
ATOM   8715  N  N   . ASN B  1 369 ? -30.627 75.078 17.189 1.00 19.70 ? 369  ASN B N   1 
ATOM   8716  C  CA  . ASN B  1 369 ? -30.905 76.428 17.672 1.00 20.53 ? 369  ASN B CA  1 
ATOM   8717  C  C   . ASN B  1 369 ? -30.853 76.583 19.191 1.00 20.33 ? 369  ASN B C   1 
ATOM   8718  O  O   . ASN B  1 369 ? -30.998 77.681 19.708 1.00 20.92 ? 369  ASN B O   1 
ATOM   8719  C  CB  . ASN B  1 369 ? -32.255 76.926 17.124 1.00 21.54 ? 369  ASN B CB  1 
ATOM   8720  C  CG  . ASN B  1 369 ? -32.196 77.210 15.622 1.00 24.10 ? 369  ASN B CG  1 
ATOM   8721  O  OD1 . ASN B  1 369 ? -31.159 77.658 15.098 1.00 21.67 ? 369  ASN B OD1 1 
ATOM   8722  N  ND2 . ASN B  1 369 ? -33.302 76.958 14.927 1.00 23.76 ? 369  ASN B ND2 1 
ATOM   8723  N  N   . SER B  1 370 ? -30.637 75.485 19.897 1.00 19.99 ? 370  SER B N   1 
ATOM   8724  C  CA  . SER B  1 370 ? -30.528 75.531 21.342 1.00 20.80 ? 370  SER B CA  1 
ATOM   8725  C  C   . SER B  1 370 ? -29.654 74.379 21.798 1.00 20.38 ? 370  SER B C   1 
ATOM   8726  O  O   . SER B  1 370 ? -29.396 73.449 21.033 1.00 20.62 ? 370  SER B O   1 
ATOM   8727  C  CB  . SER B  1 370 ? -31.908 75.460 22.007 1.00 20.89 ? 370  SER B CB  1 
ATOM   8728  O  OG  . SER B  1 370 ? -32.660 74.372 21.526 1.00 22.11 ? 370  SER B OG  1 
ATOM   8729  N  N   . PHE B  1 371 ? -29.169 74.444 23.028 1.00 19.78 ? 371  PHE B N   1 
ATOM   8730  C  CA  . PHE B  1 371 ? -28.334 73.372 23.534 1.00 20.64 ? 371  PHE B CA  1 
ATOM   8731  C  C   . PHE B  1 371 ? -28.371 73.312 25.045 1.00 20.90 ? 371  PHE B C   1 
ATOM   8732  O  O   . PHE B  1 371 ? -28.724 74.282 25.709 1.00 21.48 ? 371  PHE B O   1 
ATOM   8733  C  CB  . PHE B  1 371 ? -26.885 73.527 23.029 1.00 19.76 ? 371  PHE B CB  1 
ATOM   8734  C  CG  . PHE B  1 371 ? -26.209 74.805 23.459 1.00 19.06 ? 371  PHE B CG  1 
ATOM   8735  C  CD1 . PHE B  1 371 ? -25.587 74.900 24.706 1.00 19.71 ? 371  PHE B CD1 1 
ATOM   8736  C  CD2 . PHE B  1 371 ? -26.180 75.913 22.614 1.00 17.96 ? 371  PHE B CD2 1 
ATOM   8737  C  CE1 . PHE B  1 371 ? -24.937 76.087 25.109 1.00 20.14 ? 371  PHE B CE1 1 
ATOM   8738  C  CE2 . PHE B  1 371 ? -25.532 77.109 23.006 1.00 19.25 ? 371  PHE B CE2 1 
ATOM   8739  C  CZ  . PHE B  1 371 ? -24.913 77.195 24.254 1.00 19.32 ? 371  PHE B CZ  1 
ATOM   8740  N  N   . TYR B  1 372 ? -28.018 72.149 25.572 1.00 21.18 ? 372  TYR B N   1 
ATOM   8741  C  CA  . TYR B  1 372 ? -27.977 71.919 27.000 1.00 21.29 ? 372  TYR B CA  1 
ATOM   8742  C  C   . TYR B  1 372 ? -26.525 71.763 27.363 1.00 21.58 ? 372  TYR B C   1 
ATOM   8743  O  O   . TYR B  1 372 ? -25.750 71.179 26.609 1.00 22.70 ? 372  TYR B O   1 
ATOM   8744  C  CB  . TYR B  1 372 ? -28.747 70.651 27.360 1.00 21.43 ? 372  TYR B CB  1 
ATOM   8745  C  CG  . TYR B  1 372 ? -30.199 70.707 26.950 1.00 20.63 ? 372  TYR B CG  1 
ATOM   8746  C  CD1 . TYR B  1 372 ? -30.578 70.480 25.623 1.00 21.25 ? 372  TYR B CD1 1 
ATOM   8747  C  CD2 . TYR B  1 372 ? -31.186 71.032 27.873 1.00 20.40 ? 372  TYR B CD2 1 
ATOM   8748  C  CE1 . TYR B  1 372 ? -31.912 70.581 25.225 1.00 21.04 ? 372  TYR B CE1 1 
ATOM   8749  C  CE2 . TYR B  1 372 ? -32.525 71.133 27.490 1.00 21.65 ? 372  TYR B CE2 1 
ATOM   8750  C  CZ  . TYR B  1 372 ? -32.877 70.911 26.167 1.00 21.79 ? 372  TYR B CZ  1 
ATOM   8751  O  OH  . TYR B  1 372 ? -34.184 71.032 25.787 1.00 22.89 ? 372  TYR B OH  1 
ATOM   8752  N  N   . LYS B  1 373 ? -26.159 72.289 28.516 1.00 22.30 ? 373  LYS B N   1 
ATOM   8753  C  CA  . LYS B  1 373 ? -24.794 72.211 28.968 1.00 24.26 ? 373  LYS B CA  1 
ATOM   8754  C  C   . LYS B  1 373 ? -24.763 72.181 30.493 1.00 24.52 ? 373  LYS B C   1 
ATOM   8755  O  O   . LYS B  1 373 ? -25.581 72.829 31.151 1.00 23.98 ? 373  LYS B O   1 
ATOM   8756  C  CB  . LYS B  1 373 ? -24.027 73.420 28.448 1.00 26.17 ? 373  LYS B CB  1 
ATOM   8757  C  CG  . LYS B  1 373 ? -22.593 73.432 28.845 1.00 28.91 ? 373  LYS B CG  1 
ATOM   8758  C  CD  . LYS B  1 373 ? -21.832 74.545 28.148 1.00 32.59 ? 373  LYS B CD  1 
ATOM   8759  C  CE  . LYS B  1 373 ? -20.376 74.497 28.598 1.00 35.69 ? 373  LYS B CE  1 
ATOM   8760  N  NZ  . LYS B  1 373 ? -19.522 75.440 27.846 1.00 39.78 ? 373  LYS B NZ  1 
ATOM   8761  N  N   . ILE B  1 374 ? -23.837 71.411 31.056 1.00 24.31 ? 374  ILE B N   1 
ATOM   8762  C  CA  . ILE B  1 374 ? -23.727 71.340 32.503 1.00 23.86 ? 374  ILE B CA  1 
ATOM   8763  C  C   . ILE B  1 374 ? -22.870 72.495 32.980 1.00 25.05 ? 374  ILE B C   1 
ATOM   8764  O  O   . ILE B  1 374 ? -21.763 72.693 32.488 1.00 25.45 ? 374  ILE B O   1 
ATOM   8765  C  CB  . ILE B  1 374 ? -23.062 70.028 32.982 1.00 22.85 ? 374  ILE B CB  1 
ATOM   8766  C  CG1 . ILE B  1 374 ? -23.968 68.840 32.653 1.00 20.40 ? 374  ILE B CG1 1 
ATOM   8767  C  CG2 . ILE B  1 374 ? -22.770 70.113 34.504 1.00 20.91 ? 374  ILE B CG2 1 
ATOM   8768  C  CD1 . ILE B  1 374 ? -23.333 67.492 32.942 1.00 20.56 ? 374  ILE B CD1 1 
ATOM   8769  N  N   . ILE B  1 375 ? -23.391 73.269 33.924 1.00 24.57 ? 375  ILE B N   1 
ATOM   8770  C  CA  . ILE B  1 375 ? -22.639 74.375 34.473 1.00 25.50 ? 375  ILE B CA  1 
ATOM   8771  C  C   . ILE B  1 375 ? -22.949 74.550 35.953 1.00 26.05 ? 375  ILE B C   1 
ATOM   8772  O  O   . ILE B  1 375 ? -24.008 74.138 36.451 1.00 26.42 ? 375  ILE B O   1 
ATOM   8773  C  CB  . ILE B  1 375 ? -22.901 75.732 33.731 1.00 27.03 ? 375  ILE B CB  1 
ATOM   8774  C  CG1 . ILE B  1 375 ? -24.376 76.066 33.722 1.00 25.74 ? 375  ILE B CG1 1 
ATOM   8775  C  CG2 . ILE B  1 375 ? -22.380 75.680 32.273 1.00 24.97 ? 375  ILE B CG2 1 
ATOM   8776  C  CD1 . ILE B  1 375 ? -24.652 77.422 33.065 1.00 27.31 ? 375  ILE B CD1 1 
ATOM   8777  N  N   . SER B  1 376 ? -22.007 75.165 36.653 1.00 25.54 ? 376  SER B N   1 
ATOM   8778  C  CA  . SER B  1 376 ? -22.135 75.409 38.075 1.00 26.12 ? 376  SER B CA  1 
ATOM   8779  C  C   . SER B  1 376 ? -23.188 76.483 38.303 1.00 27.10 ? 376  SER B C   1 
ATOM   8780  O  O   . SER B  1 376 ? -23.088 77.568 37.730 1.00 27.63 ? 376  SER B O   1 
ATOM   8781  C  CB  . SER B  1 376 ? -20.786 75.865 38.616 1.00 25.59 ? 376  SER B CB  1 
ATOM   8782  O  OG  . SER B  1 376 ? -20.866 76.142 39.995 1.00 29.17 ? 376  SER B OG  1 
ATOM   8783  N  N   . ASN B  1 377 ? -24.197 76.202 39.126 1.00 27.77 ? 377  ASN B N   1 
ATOM   8784  C  CA  . ASN B  1 377 ? -25.227 77.214 39.366 1.00 29.54 ? 377  ASN B CA  1 
ATOM   8785  C  C   . ASN B  1 377 ? -24.788 78.245 40.411 1.00 31.48 ? 377  ASN B C   1 
ATOM   8786  O  O   . ASN B  1 377 ? -23.623 78.247 40.833 1.00 31.90 ? 377  ASN B O   1 
ATOM   8787  C  CB  . ASN B  1 377 ? -26.581 76.571 39.764 1.00 26.96 ? 377  ASN B CB  1 
ATOM   8788  C  CG  . ASN B  1 377 ? -26.537 75.849 41.096 1.00 26.47 ? 377  ASN B CG  1 
ATOM   8789  O  OD1 . ASN B  1 377 ? -25.672 76.105 41.932 1.00 25.44 ? 377  ASN B OD1 1 
ATOM   8790  N  ND2 . ASN B  1 377 ? -27.494 74.942 41.305 1.00 25.57 ? 377  ASN B ND2 1 
ATOM   8791  N  N   . GLU B  1 378 ? -25.710 79.113 40.830 1.00 32.99 ? 378  GLU B N   1 
ATOM   8792  C  CA  . GLU B  1 378 ? -25.388 80.151 41.807 1.00 35.60 ? 378  GLU B CA  1 
ATOM   8793  C  C   . GLU B  1 378 ? -24.944 79.571 43.152 1.00 34.65 ? 378  GLU B C   1 
ATOM   8794  O  O   . GLU B  1 378 ? -24.212 80.222 43.889 1.00 34.02 ? 378  GLU B O   1 
ATOM   8795  C  CB  . GLU B  1 378 ? -26.585 81.099 42.010 1.00 38.71 ? 378  GLU B CB  1 
ATOM   8796  C  CG  . GLU B  1 378 ? -27.142 81.695 40.707 1.00 44.72 ? 378  GLU B CG  1 
ATOM   8797  C  CD  . GLU B  1 378 ? -28.220 82.774 40.929 1.00 49.03 ? 378  GLU B CD  1 
ATOM   8798  O  OE1 . GLU B  1 378 ? -29.143 82.902 40.074 1.00 51.24 ? 378  GLU B OE1 1 
ATOM   8799  O  OE2 . GLU B  1 378 ? -28.143 83.508 41.949 1.00 50.97 ? 378  GLU B OE2 1 
ATOM   8800  N  N   . GLU B  1 379 ? -25.375 78.348 43.460 1.00 33.41 ? 379  GLU B N   1 
ATOM   8801  C  CA  . GLU B  1 379 ? -25.007 77.683 44.712 1.00 33.08 ? 379  GLU B CA  1 
ATOM   8802  C  C   . GLU B  1 379 ? -23.712 76.876 44.580 1.00 31.62 ? 379  GLU B C   1 
ATOM   8803  O  O   . GLU B  1 379 ? -23.229 76.306 45.549 1.00 31.19 ? 379  GLU B O   1 
ATOM   8804  C  CB  . GLU B  1 379 ? -26.103 76.711 45.151 1.00 35.65 ? 379  GLU B CB  1 
ATOM   8805  C  CG  . GLU B  1 379 ? -27.421 77.328 45.562 1.00 41.07 ? 379  GLU B CG  1 
ATOM   8806  C  CD  . GLU B  1 379 ? -28.357 76.291 46.194 1.00 45.71 ? 379  GLU B CD  1 
ATOM   8807  O  OE1 . GLU B  1 379 ? -27.914 75.567 47.133 1.00 46.56 ? 379  GLU B OE1 1 
ATOM   8808  O  OE2 . GLU B  1 379 ? -29.539 76.198 45.763 1.00 47.60 ? 379  GLU B OE2 1 
ATOM   8809  N  N   . GLY B  1 380 ? -23.156 76.804 43.380 1.00 30.48 ? 380  GLY B N   1 
ATOM   8810  C  CA  . GLY B  1 380 ? -21.944 76.031 43.206 1.00 29.03 ? 380  GLY B CA  1 
ATOM   8811  C  C   . GLY B  1 380 ? -22.178 74.575 42.796 1.00 28.34 ? 380  GLY B C   1 
ATOM   8812  O  O   . GLY B  1 380 ? -21.213 73.814 42.704 1.00 29.53 ? 380  GLY B O   1 
ATOM   8813  N  N   . TYR B  1 381 ? -23.429 74.172 42.559 1.00 26.86 ? 381  TYR B N   1 
ATOM   8814  C  CA  . TYR B  1 381 ? -23.715 72.794 42.130 1.00 24.96 ? 381  TYR B CA  1 
ATOM   8815  C  C   . TYR B  1 381 ? -23.909 72.740 40.624 1.00 24.44 ? 381  TYR B C   1 
ATOM   8816  O  O   . TYR B  1 381 ? -24.598 73.585 40.036 1.00 22.72 ? 381  TYR B O   1 
ATOM   8817  C  CB  . TYR B  1 381 ? -24.954 72.232 42.823 1.00 23.80 ? 381  TYR B CB  1 
ATOM   8818  C  CG  . TYR B  1 381 ? -24.739 71.992 44.296 1.00 23.91 ? 381  TYR B CG  1 
ATOM   8819  C  CD1 . TYR B  1 381 ? -24.954 73.009 45.227 1.00 23.77 ? 381  TYR B CD1 1 
ATOM   8820  C  CD2 . TYR B  1 381 ? -24.280 70.754 44.758 1.00 22.93 ? 381  TYR B CD2 1 
ATOM   8821  C  CE1 . TYR B  1 381 ? -24.714 72.798 46.600 1.00 24.44 ? 381  TYR B CE1 1 
ATOM   8822  C  CE2 . TYR B  1 381 ? -24.034 70.532 46.117 1.00 23.32 ? 381  TYR B CE2 1 
ATOM   8823  C  CZ  . TYR B  1 381 ? -24.254 71.564 47.030 1.00 23.89 ? 381  TYR B CZ  1 
ATOM   8824  O  OH  . TYR B  1 381 ? -24.009 71.354 48.363 1.00 25.44 ? 381  TYR B OH  1 
ATOM   8825  N  N   . ARG B  1 382 ? -23.288 71.740 40.004 1.00 24.08 ? 382  ARG B N   1 
ATOM   8826  C  CA  . ARG B  1 382 ? -23.342 71.579 38.559 1.00 22.96 ? 382  ARG B CA  1 
ATOM   8827  C  C   . ARG B  1 382 ? -24.649 70.960 38.090 1.00 22.38 ? 382  ARG B C   1 
ATOM   8828  O  O   . ARG B  1 382 ? -24.982 69.828 38.428 1.00 21.80 ? 382  ARG B O   1 
ATOM   8829  C  CB  . ARG B  1 382 ? -22.112 70.778 38.104 1.00 23.32 ? 382  ARG B CB  1 
ATOM   8830  C  CG  . ARG B  1 382 ? -20.832 71.626 38.219 1.00 22.67 ? 382  ARG B CG  1 
ATOM   8831  C  CD  . ARG B  1 382 ? -19.492 70.864 38.232 1.00 22.22 ? 382  ARG B CD  1 
ATOM   8832  N  NE  . ARG B  1 382 ? -18.476 71.761 38.784 1.00 21.78 ? 382  ARG B NE  1 
ATOM   8833  C  CZ  . ARG B  1 382 ? -17.882 72.751 38.113 1.00 22.19 ? 382  ARG B CZ  1 
ATOM   8834  N  NH1 . ARG B  1 382 ? -18.150 72.972 36.827 1.00 20.35 ? 382  ARG B NH1 1 
ATOM   8835  N  NH2 . ARG B  1 382 ? -17.105 73.615 38.765 1.00 21.21 ? 382  ARG B NH2 1 
ATOM   8836  N  N   . HIS B  1 383 ? -25.383 71.743 37.302 1.00 21.90 ? 383  HIS B N   1 
ATOM   8837  C  CA  . HIS B  1 383 ? -26.684 71.345 36.783 1.00 21.72 ? 383  HIS B CA  1 
ATOM   8838  C  C   . HIS B  1 383 ? -26.860 71.653 35.305 1.00 21.45 ? 383  HIS B C   1 
ATOM   8839  O  O   . HIS B  1 383 ? -26.094 72.422 34.720 1.00 20.43 ? 383  HIS B O   1 
ATOM   8840  C  CB  . HIS B  1 383 ? -27.780 72.029 37.597 1.00 21.02 ? 383  HIS B CB  1 
ATOM   8841  C  CG  . HIS B  1 383 ? -27.992 71.402 38.934 1.00 22.69 ? 383  HIS B CG  1 
ATOM   8842  N  ND1 . HIS B  1 383 ? -28.602 70.171 39.085 1.00 22.66 ? 383  HIS B ND1 1 
ATOM   8843  C  CD2 . HIS B  1 383 ? -27.589 71.777 40.170 1.00 21.20 ? 383  HIS B CD2 1 
ATOM   8844  C  CE1 . HIS B  1 383 ? -28.558 69.817 40.355 1.00 22.50 ? 383  HIS B CE1 1 
ATOM   8845  N  NE2 . HIS B  1 383 ? -27.949 70.773 41.034 1.00 22.51 ? 383  HIS B NE2 1 
ATOM   8846  N  N   . ILE B  1 384 ? -27.874 71.054 34.694 1.00 20.45 ? 384  ILE B N   1 
ATOM   8847  C  CA  . ILE B  1 384 ? -28.090 71.271 33.276 1.00 20.15 ? 384  ILE B CA  1 
ATOM   8848  C  C   . ILE B  1 384 ? -28.764 72.602 32.983 1.00 21.00 ? 384  ILE B C   1 
ATOM   8849  O  O   . ILE B  1 384 ? -29.827 72.887 33.508 1.00 20.53 ? 384  ILE B O   1 
ATOM   8850  C  CB  . ILE B  1 384 ? -28.909 70.114 32.700 1.00 19.88 ? 384  ILE B CB  1 
ATOM   8851  C  CG1 . ILE B  1 384 ? -28.149 68.812 32.965 1.00 18.74 ? 384  ILE B CG1 1 
ATOM   8852  C  CG2 . ILE B  1 384 ? -29.185 70.342 31.199 1.00 18.09 ? 384  ILE B CG2 1 
ATOM   8853  C  CD1 . ILE B  1 384 ? -29.004 67.563 32.854 1.00 19.75 ? 384  ILE B CD1 1 
ATOM   8854  N  N   . CYS B  1 385 ? -28.124 73.420 32.147 1.00 23.61 ? 385  CYS B N   1 
ATOM   8855  C  CA  . CYS B  1 385 ? -28.673 74.718 31.773 1.00 25.15 ? 385  CYS B CA  1 
ATOM   8856  C  C   . CYS B  1 385 ? -29.053 74.671 30.299 1.00 24.98 ? 385  CYS B C   1 
ATOM   8857  O  O   . CYS B  1 385 ? -28.285 74.181 29.473 1.00 24.38 ? 385  CYS B O   1 
ATOM   8858  C  CB  . CYS B  1 385 ? -27.658 75.854 32.014 1.00 28.02 ? 385  CYS B CB  1 
ATOM   8859  S  SG  . CYS B  1 385 ? -28.474 77.371 32.635 1.00 34.39 ? 385  CYS B SG  1 
ATOM   8860  N  N   . TYR B  1 386 ? -30.248 75.171 29.981 1.00 24.17 ? 386  TYR B N   1 
ATOM   8861  C  CA  . TYR B  1 386 ? -30.746 75.195 28.616 1.00 24.07 ? 386  TYR B CA  1 
ATOM   8862  C  C   . TYR B  1 386 ? -30.514 76.568 28.008 1.00 24.61 ? 386  TYR B C   1 
ATOM   8863  O  O   . TYR B  1 386 ? -30.996 77.578 28.525 1.00 23.83 ? 386  TYR B O   1 
ATOM   8864  C  CB  . TYR B  1 386 ? -32.231 74.864 28.600 1.00 25.58 ? 386  TYR B CB  1 
ATOM   8865  C  CG  . TYR B  1 386 ? -32.877 74.875 27.226 1.00 25.84 ? 386  TYR B CG  1 
ATOM   8866  C  CD1 . TYR B  1 386 ? -32.346 74.134 26.176 1.00 26.38 ? 386  TYR B CD1 1 
ATOM   8867  C  CD2 . TYR B  1 386 ? -34.066 75.573 27.001 1.00 27.31 ? 386  TYR B CD2 1 
ATOM   8868  C  CE1 . TYR B  1 386 ? -32.981 74.077 24.926 1.00 27.51 ? 386  TYR B CE1 1 
ATOM   8869  C  CE2 . TYR B  1 386 ? -34.714 75.524 25.757 1.00 28.28 ? 386  TYR B CE2 1 
ATOM   8870  C  CZ  . TYR B  1 386 ? -34.166 74.777 24.726 1.00 28.53 ? 386  TYR B CZ  1 
ATOM   8871  O  OH  . TYR B  1 386 ? -34.795 74.738 23.503 1.00 29.27 ? 386  TYR B OH  1 
ATOM   8872  N  N   . PHE B  1 387 ? -29.796 76.575 26.892 1.00 23.59 ? 387  PHE B N   1 
ATOM   8873  C  CA  . PHE B  1 387 ? -29.413 77.793 26.163 1.00 24.59 ? 387  PHE B CA  1 
ATOM   8874  C  C   . PHE B  1 387 ? -30.074 77.933 24.782 1.00 24.24 ? 387  PHE B C   1 
ATOM   8875  O  O   . PHE B  1 387 ? -30.264 76.948 24.062 1.00 23.90 ? 387  PHE B O   1 
ATOM   8876  C  CB  . PHE B  1 387 ? -27.900 77.795 25.872 1.00 22.78 ? 387  PHE B CB  1 
ATOM   8877  C  CG  . PHE B  1 387 ? -27.009 77.974 27.077 1.00 22.24 ? 387  PHE B CG  1 
ATOM   8878  C  CD1 . PHE B  1 387 ? -26.346 79.179 27.278 1.00 21.13 ? 387  PHE B CD1 1 
ATOM   8879  C  CD2 . PHE B  1 387 ? -26.748 76.920 27.946 1.00 21.89 ? 387  PHE B CD2 1 
ATOM   8880  C  CE1 . PHE B  1 387 ? -25.424 79.340 28.318 1.00 22.34 ? 387  PHE B CE1 1 
ATOM   8881  C  CE2 . PHE B  1 387 ? -25.815 77.071 29.002 1.00 22.61 ? 387  PHE B CE2 1 
ATOM   8882  C  CZ  . PHE B  1 387 ? -25.157 78.289 29.179 1.00 21.37 ? 387  PHE B CZ  1 
ATOM   8883  N  N   . GLN B  1 388 ? -30.391 79.167 24.420 1.00 23.01 ? 388  GLN B N   1 
ATOM   8884  C  CA  . GLN B  1 388 ? -30.915 79.492 23.099 1.00 23.68 ? 388  GLN B CA  1 
ATOM   8885  C  C   . GLN B  1 388 ? -29.594 79.961 22.465 1.00 22.74 ? 388  GLN B C   1 
ATOM   8886  O  O   . GLN B  1 388 ? -28.885 80.723 23.111 1.00 19.45 ? 388  GLN B O   1 
ATOM   8887  C  CB  . GLN B  1 388 ? -31.889 80.653 23.220 1.00 28.02 ? 388  GLN B CB  1 
ATOM   8888  C  CG  . GLN B  1 388 ? -33.036 80.567 22.281 1.00 32.69 ? 388  GLN B CG  1 
ATOM   8889  C  CD  . GLN B  1 388 ? -33.694 79.214 22.335 1.00 34.21 ? 388  GLN B CD  1 
ATOM   8890  O  OE1 . GLN B  1 388 ? -34.088 78.750 23.404 1.00 36.08 ? 388  GLN B OE1 1 
ATOM   8891  N  NE2 . GLN B  1 388 ? -33.806 78.561 21.178 1.00 37.03 ? 388  GLN B NE2 1 
ATOM   8892  N  N   . ILE B  1 389 ? -29.232 79.545 21.242 1.00 21.34 ? 389  ILE B N   1 
ATOM   8893  C  CA  . ILE B  1 389 ? -27.914 79.964 20.752 1.00 21.93 ? 389  ILE B CA  1 
ATOM   8894  C  C   . ILE B  1 389 ? -27.611 81.456 20.651 1.00 22.98 ? 389  ILE B C   1 
ATOM   8895  O  O   . ILE B  1 389 ? -26.434 81.838 20.629 1.00 22.01 ? 389  ILE B O   1 
ATOM   8896  C  CB  . ILE B  1 389 ? -27.497 79.333 19.374 1.00 22.03 ? 389  ILE B CB  1 
ATOM   8897  C  CG1 . ILE B  1 389 ? -28.472 79.743 18.268 1.00 22.23 ? 389  ILE B CG1 1 
ATOM   8898  C  CG2 . ILE B  1 389 ? -27.324 77.833 19.517 1.00 20.39 ? 389  ILE B CG2 1 
ATOM   8899  C  CD1 . ILE B  1 389 ? -27.913 79.526 16.882 1.00 18.80 ? 389  ILE B CD1 1 
ATOM   8900  N  N   . ASP B  1 390 ? -28.638 82.297 20.585 1.00 22.59 ? 390  ASP B N   1 
ATOM   8901  C  CA  . ASP B  1 390 ? -28.398 83.732 20.489 1.00 25.56 ? 390  ASP B CA  1 
ATOM   8902  C  C   . ASP B  1 390 ? -28.924 84.537 21.677 1.00 26.89 ? 390  ASP B C   1 
ATOM   8903  O  O   . ASP B  1 390 ? -29.271 85.713 21.523 1.00 27.34 ? 390  ASP B O   1 
ATOM   8904  C  CB  . ASP B  1 390 ? -28.991 84.290 19.193 1.00 25.58 ? 390  ASP B CB  1 
ATOM   8905  C  CG  . ASP B  1 390 ? -30.487 84.151 19.138 1.00 27.87 ? 390  ASP B CG  1 
ATOM   8906  O  OD1 . ASP B  1 390 ? -31.060 83.435 19.991 1.00 26.91 ? 390  ASP B OD1 1 
ATOM   8907  O  OD2 . ASP B  1 390 ? -31.102 84.747 18.228 1.00 30.08 ? 390  ASP B OD2 1 
ATOM   8908  N  N   . LYS B  1 391 ? -29.000 83.895 22.842 1.00 26.43 ? 391  LYS B N   1 
ATOM   8909  C  CA  . LYS B  1 391 ? -29.438 84.541 24.076 1.00 28.61 ? 391  LYS B CA  1 
ATOM   8910  C  C   . LYS B  1 391 ? -28.413 84.125 25.109 1.00 29.62 ? 391  LYS B C   1 
ATOM   8911  O  O   . LYS B  1 391 ? -28.088 82.941 25.224 1.00 30.01 ? 391  LYS B O   1 
ATOM   8912  C  CB  . LYS B  1 391 ? -30.839 84.085 24.499 1.00 29.31 ? 391  LYS B CB  1 
ATOM   8913  C  CG  . LYS B  1 391 ? -31.943 84.476 23.521 1.00 33.25 ? 391  LYS B CG  1 
ATOM   8914  C  CD  . LYS B  1 391 ? -33.331 84.004 23.995 1.00 34.68 ? 391  LYS B CD  1 
ATOM   8915  C  CE  . LYS B  1 391 ? -34.409 84.339 22.962 1.00 36.42 ? 391  LYS B CE  1 
ATOM   8916  N  NZ  . LYS B  1 391 ? -34.077 83.717 21.625 1.00 38.87 ? 391  LYS B NZ  1 
ATOM   8917  N  N   . LYS B  1 392 ? -27.904 85.092 25.863 1.00 30.62 ? 392  LYS B N   1 
ATOM   8918  C  CA  . LYS B  1 392 ? -26.858 84.820 26.844 1.00 32.74 ? 392  LYS B CA  1 
ATOM   8919  C  C   . LYS B  1 392 ? -27.303 84.183 28.148 1.00 33.90 ? 392  LYS B C   1 
ATOM   8920  O  O   . LYS B  1 392 ? -26.559 83.400 28.733 1.00 34.52 ? 392  LYS B O   1 
ATOM   8921  C  CB  . LYS B  1 392 ? -26.060 86.106 27.118 1.00 32.46 ? 392  LYS B CB  1 
ATOM   8922  C  CG  . LYS B  1 392 ? -25.467 86.745 25.843 1.00 32.88 ? 392  LYS B CG  1 
ATOM   8923  C  CD  . LYS B  1 392 ? -24.779 85.702 24.953 1.00 33.15 ? 392  LYS B CD  1 
ATOM   8924  C  CE  . LYS B  1 392 ? -24.476 86.243 23.556 1.00 32.08 ? 392  LYS B CE  1 
ATOM   8925  N  NZ  . LYS B  1 392 ? -23.370 87.240 23.560 1.00 32.30 ? 392  LYS B NZ  1 
ATOM   8926  N  N   . ASP B  1 393 ? -28.494 84.523 28.619 1.00 34.61 ? 393  ASP B N   1 
ATOM   8927  C  CA  . ASP B  1 393 ? -28.974 83.912 29.848 1.00 36.24 ? 393  ASP B CA  1 
ATOM   8928  C  C   . ASP B  1 393 ? -29.550 82.534 29.547 1.00 35.81 ? 393  ASP B C   1 
ATOM   8929  O  O   . ASP B  1 393 ? -30.278 82.361 28.569 1.00 37.25 ? 393  ASP B O   1 
ATOM   8930  C  CB  . ASP B  1 393 ? -30.035 84.790 30.504 1.00 38.93 ? 393  ASP B CB  1 
ATOM   8931  C  CG  . ASP B  1 393 ? -29.467 86.111 30.976 1.00 41.83 ? 393  ASP B CG  1 
ATOM   8932  O  OD1 . ASP B  1 393 ? -28.347 86.099 31.547 1.00 43.53 ? 393  ASP B OD1 1 
ATOM   8933  O  OD2 . ASP B  1 393 ? -30.130 87.157 30.787 1.00 43.81 ? 393  ASP B OD2 1 
ATOM   8934  N  N   . CYS B  1 394 ? -29.203 81.549 30.368 1.00 33.76 ? 394  CYS B N   1 
ATOM   8935  C  CA  . CYS B  1 394 ? -29.718 80.203 30.173 1.00 31.40 ? 394  CYS B CA  1 
ATOM   8936  C  C   . CYS B  1 394 ? -30.707 79.884 31.289 1.00 30.13 ? 394  CYS B C   1 
ATOM   8937  O  O   . CYS B  1 394 ? -30.841 80.642 32.248 1.00 29.14 ? 394  CYS B O   1 
ATOM   8938  C  CB  . CYS B  1 394 ? -28.576 79.176 30.157 1.00 31.44 ? 394  CYS B CB  1 
ATOM   8939  S  SG  . CYS B  1 394 ? -27.613 78.976 31.699 1.00 32.09 ? 394  CYS B SG  1 
ATOM   8940  N  N   . THR B  1 395 ? -31.406 78.766 31.151 1.00 28.30 ? 395  THR B N   1 
ATOM   8941  C  CA  . THR B  1 395 ? -32.392 78.342 32.143 1.00 27.33 ? 395  THR B CA  1 
ATOM   8942  C  C   . THR B  1 395 ? -31.989 76.983 32.730 1.00 25.78 ? 395  THR B C   1 
ATOM   8943  O  O   . THR B  1 395 ? -31.854 76.012 31.998 1.00 24.85 ? 395  THR B O   1 
ATOM   8944  C  CB  . THR B  1 395 ? -33.785 78.196 31.490 1.00 28.24 ? 395  THR B CB  1 
ATOM   8945  O  OG1 . THR B  1 395 ? -34.173 79.444 30.888 1.00 28.98 ? 395  THR B OG1 1 
ATOM   8946  C  CG2 . THR B  1 395 ? -34.824 77.764 32.540 1.00 27.16 ? 395  THR B CG2 1 
ATOM   8947  N  N   . PHE B  1 396 ? -31.793 76.903 34.039 1.00 24.57 ? 396  PHE B N   1 
ATOM   8948  C  CA  . PHE B  1 396 ? -31.425 75.621 34.638 1.00 24.45 ? 396  PHE B CA  1 
ATOM   8949  C  C   . PHE B  1 396 ? -32.644 74.725 34.630 1.00 23.79 ? 396  PHE B C   1 
ATOM   8950  O  O   . PHE B  1 396 ? -33.726 75.167 34.990 1.00 23.99 ? 396  PHE B O   1 
ATOM   8951  C  CB  . PHE B  1 396 ? -30.939 75.819 36.070 1.00 24.29 ? 396  PHE B CB  1 
ATOM   8952  C  CG  . PHE B  1 396 ? -29.524 76.315 36.158 1.00 24.03 ? 396  PHE B CG  1 
ATOM   8953  C  CD1 . PHE B  1 396 ? -28.446 75.435 35.981 1.00 22.71 ? 396  PHE B CD1 1 
ATOM   8954  C  CD2 . PHE B  1 396 ? -29.263 77.658 36.394 1.00 21.66 ? 396  PHE B CD2 1 
ATOM   8955  C  CE1 . PHE B  1 396 ? -27.118 75.897 36.032 1.00 22.39 ? 396  PHE B CE1 1 
ATOM   8956  C  CE2 . PHE B  1 396 ? -27.938 78.130 36.446 1.00 23.13 ? 396  PHE B CE2 1 
ATOM   8957  C  CZ  . PHE B  1 396 ? -26.862 77.242 36.265 1.00 21.29 ? 396  PHE B CZ  1 
ATOM   8958  N  N   . ILE B  1 397 ? -32.485 73.478 34.210 1.00 22.91 ? 397  ILE B N   1 
ATOM   8959  C  CA  . ILE B  1 397 ? -33.626 72.580 34.174 1.00 21.76 ? 397  ILE B CA  1 
ATOM   8960  C  C   . ILE B  1 397 ? -33.593 71.542 35.289 1.00 22.15 ? 397  ILE B C   1 
ATOM   8961  O  O   . ILE B  1 397 ? -34.522 70.749 35.434 1.00 21.85 ? 397  ILE B O   1 
ATOM   8962  C  CB  . ILE B  1 397 ? -33.767 71.905 32.784 1.00 21.75 ? 397  ILE B CB  1 
ATOM   8963  C  CG1 . ILE B  1 397 ? -32.746 70.782 32.607 1.00 20.51 ? 397  ILE B CG1 1 
ATOM   8964  C  CG2 . ILE B  1 397 ? -33.572 72.956 31.703 1.00 21.05 ? 397  ILE B CG2 1 
ATOM   8965  C  CD1 . ILE B  1 397 ? -32.922 70.021 31.288 1.00 19.89 ? 397  ILE B CD1 1 
ATOM   8966  N  N   . THR B  1 398 ? -32.509 71.546 36.063 1.00 22.32 ? 398  THR B N   1 
ATOM   8967  C  CA  . THR B  1 398 ? -32.362 70.668 37.222 1.00 22.71 ? 398  THR B CA  1 
ATOM   8968  C  C   . THR B  1 398 ? -31.720 71.564 38.277 1.00 24.22 ? 398  THR B C   1 
ATOM   8969  O  O   . THR B  1 398 ? -31.108 72.585 37.936 1.00 23.54 ? 398  THR B O   1 
ATOM   8970  C  CB  . THR B  1 398 ? -31.392 69.459 36.981 1.00 23.23 ? 398  THR B CB  1 
ATOM   8971  O  OG1 . THR B  1 398 ? -30.060 69.941 36.707 1.00 22.82 ? 398  THR B OG1 1 
ATOM   8972  C  CG2 . THR B  1 398 ? -31.888 68.581 35.851 1.00 21.23 ? 398  THR B CG2 1 
ATOM   8973  N  N   . LYS B  1 399 ? -31.866 71.193 39.544 1.00 24.43 ? 399  LYS B N   1 
ATOM   8974  C  CA  . LYS B  1 399 ? -31.286 71.950 40.650 1.00 27.54 ? 399  LYS B CA  1 
ATOM   8975  C  C   . LYS B  1 399 ? -31.314 71.062 41.892 1.00 27.40 ? 399  LYS B C   1 
ATOM   8976  O  O   . LYS B  1 399 ? -31.973 70.032 41.896 1.00 28.15 ? 399  LYS B O   1 
ATOM   8977  C  CB  . LYS B  1 399 ? -32.087 73.230 40.921 1.00 29.47 ? 399  LYS B CB  1 
ATOM   8978  C  CG  . LYS B  1 399 ? -33.520 72.958 41.354 1.00 35.00 ? 399  LYS B CG  1 
ATOM   8979  C  CD  . LYS B  1 399 ? -34.312 74.246 41.598 1.00 38.67 ? 399  LYS B CD  1 
ATOM   8980  C  CE  . LYS B  1 399 ? -35.796 73.936 41.873 1.00 41.82 ? 399  LYS B CE  1 
ATOM   8981  N  NZ  . LYS B  1 399 ? -36.598 75.153 42.213 1.00 44.26 ? 399  LYS B NZ  1 
ATOM   8982  N  N   . GLY B  1 400 ? -30.602 71.464 42.939 1.00 26.87 ? 400  GLY B N   1 
ATOM   8983  C  CA  . GLY B  1 400 ? -30.570 70.676 44.163 1.00 27.20 ? 400  GLY B CA  1 
ATOM   8984  C  C   . GLY B  1 400 ? -29.154 70.606 44.722 1.00 27.16 ? 400  GLY B C   1 
ATOM   8985  O  O   . GLY B  1 400 ? -28.204 71.051 44.063 1.00 27.50 ? 400  GLY B O   1 
ATOM   8986  N  N   . THR B  1 401 ? -29.002 70.071 45.932 1.00 26.49 ? 401  THR B N   1 
ATOM   8987  C  CA  . THR B  1 401 ? -27.675 69.947 46.533 1.00 26.33 ? 401  THR B CA  1 
ATOM   8988  C  C   . THR B  1 401 ? -27.073 68.603 46.132 1.00 24.89 ? 401  THR B C   1 
ATOM   8989  O  O   . THR B  1 401 ? -26.831 67.724 46.961 1.00 26.03 ? 401  THR B O   1 
ATOM   8990  C  CB  . THR B  1 401 ? -27.724 70.059 48.087 1.00 26.31 ? 401  THR B CB  1 
ATOM   8991  O  OG1 . THR B  1 401 ? -28.733 69.183 48.597 1.00 28.81 ? 401  THR B OG1 1 
ATOM   8992  C  CG2 . THR B  1 401 ? -28.049 71.480 48.515 1.00 26.74 ? 401  THR B CG2 1 
ATOM   8993  N  N   . TRP B  1 402 ? -26.865 68.460 44.835 1.00 22.91 ? 402  TRP B N   1 
ATOM   8994  C  CA  . TRP B  1 402 ? -26.275 67.273 44.238 1.00 21.69 ? 402  TRP B CA  1 
ATOM   8995  C  C   . TRP B  1 402 ? -25.834 67.737 42.863 1.00 21.24 ? 402  TRP B C   1 
ATOM   8996  O  O   . TRP B  1 402 ? -26.083 68.889 42.490 1.00 20.73 ? 402  TRP B O   1 
ATOM   8997  C  CB  . TRP B  1 402 ? -27.298 66.133 44.114 1.00 21.52 ? 402  TRP B CB  1 
ATOM   8998  C  CG  . TRP B  1 402 ? -28.640 66.534 43.563 1.00 21.32 ? 402  TRP B CG  1 
ATOM   8999  C  CD1 . TRP B  1 402 ? -29.726 66.980 44.276 1.00 19.78 ? 402  TRP B CD1 1 
ATOM   9000  C  CD2 . TRP B  1 402 ? -29.041 66.528 42.183 1.00 21.73 ? 402  TRP B CD2 1 
ATOM   9001  N  NE1 . TRP B  1 402 ? -30.771 67.246 43.424 1.00 22.17 ? 402  TRP B NE1 1 
ATOM   9002  C  CE2 . TRP B  1 402 ? -30.383 66.980 42.136 1.00 21.67 ? 402  TRP B CE2 1 
ATOM   9003  C  CE3 . TRP B  1 402 ? -28.397 66.185 40.982 1.00 20.40 ? 402  TRP B CE3 1 
ATOM   9004  C  CZ2 . TRP B  1 402 ? -31.094 67.100 40.938 1.00 22.04 ? 402  TRP B CZ2 1 
ATOM   9005  C  CZ3 . TRP B  1 402 ? -29.101 66.303 39.792 1.00 22.14 ? 402  TRP B CZ3 1 
ATOM   9006  C  CH2 . TRP B  1 402 ? -30.443 66.758 39.778 1.00 23.09 ? 402  TRP B CH2 1 
ATOM   9007  N  N   . GLU B  1 403 ? -25.192 66.870 42.093 1.00 20.14 ? 403  GLU B N   1 
ATOM   9008  C  CA  . GLU B  1 403 ? -24.755 67.315 40.781 1.00 19.29 ? 403  GLU B CA  1 
ATOM   9009  C  C   . GLU B  1 403 ? -25.007 66.355 39.637 1.00 19.14 ? 403  GLU B C   1 
ATOM   9010  O  O   . GLU B  1 403 ? -25.060 65.139 39.810 1.00 16.95 ? 403  GLU B O   1 
ATOM   9011  C  CB  . GLU B  1 403 ? -23.250 67.633 40.788 1.00 18.04 ? 403  GLU B CB  1 
ATOM   9012  C  CG  . GLU B  1 403 ? -22.790 68.626 41.839 1.00 17.22 ? 403  GLU B CG  1 
ATOM   9013  C  CD  . GLU B  1 403 ? -21.402 69.148 41.556 1.00 18.53 ? 403  GLU B CD  1 
ATOM   9014  O  OE1 . GLU B  1 403 ? -20.499 68.339 41.225 1.00 19.26 ? 403  GLU B OE1 1 
ATOM   9015  O  OE2 . GLU B  1 403 ? -21.208 70.381 41.653 1.00 19.74 ? 403  GLU B OE2 1 
ATOM   9016  N  N   . VAL B  1 404 ? -25.140 66.941 38.453 1.00 19.68 ? 404  VAL B N   1 
ATOM   9017  C  CA  . VAL B  1 404 ? -25.303 66.177 37.232 1.00 18.85 ? 404  VAL B CA  1 
ATOM   9018  C  C   . VAL B  1 404 ? -23.874 65.794 36.800 1.00 20.47 ? 404  VAL B C   1 
ATOM   9019  O  O   . VAL B  1 404 ? -22.982 66.656 36.686 1.00 20.61 ? 404  VAL B O   1 
ATOM   9020  C  CB  . VAL B  1 404 ? -25.950 67.024 36.127 1.00 16.98 ? 404  VAL B CB  1 
ATOM   9021  C  CG1 . VAL B  1 404 ? -25.942 66.232 34.822 1.00 17.51 ? 404  VAL B CG1 1 
ATOM   9022  C  CG2 . VAL B  1 404 ? -27.390 67.398 36.516 1.00 16.24 ? 404  VAL B CG2 1 
ATOM   9023  N  N   . ILE B  1 405 ? -23.669 64.505 36.576 1.00 20.25 ? 405  ILE B N   1 
ATOM   9024  C  CA  . ILE B  1 405 ? -22.380 63.963 36.165 1.00 20.50 ? 405  ILE B CA  1 
ATOM   9025  C  C   . ILE B  1 405 ? -22.176 64.121 34.665 1.00 20.94 ? 405  ILE B C   1 
ATOM   9026  O  O   . ILE B  1 405 ? -21.091 64.485 34.219 1.00 20.80 ? 405  ILE B O   1 
ATOM   9027  C  CB  . ILE B  1 405 ? -22.297 62.473 36.468 1.00 21.97 ? 405  ILE B CB  1 
ATOM   9028  C  CG1 . ILE B  1 405 ? -22.645 62.232 37.945 1.00 22.32 ? 405  ILE B CG1 1 
ATOM   9029  C  CG2 . ILE B  1 405 ? -20.913 61.939 36.067 1.00 19.14 ? 405  ILE B CG2 1 
ATOM   9030  C  CD1 . ILE B  1 405 ? -21.674 62.859 38.903 1.00 23.16 ? 405  ILE B CD1 1 
ATOM   9031  N  N   . GLY B  1 406 ? -23.216 63.812 33.894 1.00 19.40 ? 406  GLY B N   1 
ATOM   9032  C  CA  . GLY B  1 406 ? -23.133 63.944 32.452 1.00 19.23 ? 406  GLY B CA  1 
ATOM   9033  C  C   . GLY B  1 406 ? -24.483 63.805 31.752 1.00 20.41 ? 406  GLY B C   1 
ATOM   9034  O  O   . GLY B  1 406 ? -25.435 63.248 32.306 1.00 20.51 ? 406  GLY B O   1 
ATOM   9035  N  N   . ILE B  1 407 ? -24.555 64.341 30.538 1.00 20.01 ? 407  ILE B N   1 
ATOM   9036  C  CA  . ILE B  1 407 ? -25.735 64.264 29.686 1.00 19.60 ? 407  ILE B CA  1 
ATOM   9037  C  C   . ILE B  1 407 ? -25.400 63.088 28.769 1.00 20.47 ? 407  ILE B C   1 
ATOM   9038  O  O   . ILE B  1 407 ? -24.364 63.100 28.108 1.00 21.46 ? 407  ILE B O   1 
ATOM   9039  C  CB  . ILE B  1 407 ? -25.908 65.569 28.859 1.00 18.55 ? 407  ILE B CB  1 
ATOM   9040  C  CG1 . ILE B  1 407 ? -26.283 66.718 29.786 1.00 19.06 ? 407  ILE B CG1 1 
ATOM   9041  C  CG2 . ILE B  1 407 ? -26.975 65.381 27.793 1.00 16.47 ? 407  ILE B CG2 1 
ATOM   9042  C  CD1 . ILE B  1 407 ? -26.286 68.097 29.124 1.00 16.67 ? 407  ILE B CD1 1 
ATOM   9043  N  N   . GLU B  1 408 ? -26.272 62.084 28.729 1.00 20.94 ? 408  GLU B N   1 
ATOM   9044  C  CA  . GLU B  1 408 ? -26.037 60.860 27.955 1.00 22.00 ? 408  GLU B CA  1 
ATOM   9045  C  C   . GLU B  1 408 ? -26.772 60.768 26.617 1.00 22.75 ? 408  GLU B C   1 
ATOM   9046  O  O   . GLU B  1 408 ? -26.320 60.094 25.695 1.00 23.37 ? 408  GLU B O   1 
ATOM   9047  C  CB  . GLU B  1 408 ? -26.414 59.649 28.819 1.00 21.95 ? 408  GLU B CB  1 
ATOM   9048  C  CG  . GLU B  1 408 ? -25.780 59.670 30.186 1.00 22.97 ? 408  GLU B CG  1 
ATOM   9049  C  CD  . GLU B  1 408 ? -24.252 59.739 30.110 1.00 26.00 ? 408  GLU B CD  1 
ATOM   9050  O  OE1 . GLU B  1 408 ? -23.651 60.529 30.871 1.00 28.87 ? 408  GLU B OE1 1 
ATOM   9051  O  OE2 . GLU B  1 408 ? -23.649 59.007 29.292 1.00 26.10 ? 408  GLU B OE2 1 
ATOM   9052  N  N   . ALA B  1 409 ? -27.924 61.416 26.518 1.00 22.31 ? 409  ALA B N   1 
ATOM   9053  C  CA  . ALA B  1 409 ? -28.678 61.380 25.277 1.00 21.99 ? 409  ALA B CA  1 
ATOM   9054  C  C   . ALA B  1 409 ? -29.718 62.479 25.277 1.00 22.20 ? 409  ALA B C   1 
ATOM   9055  O  O   . ALA B  1 409 ? -30.119 62.970 26.333 1.00 22.06 ? 409  ALA B O   1 
ATOM   9056  C  CB  . ALA B  1 409 ? -29.340 60.028 25.096 1.00 21.55 ? 409  ALA B CB  1 
ATOM   9057  N  N   . LEU B  1 410 ? -30.145 62.854 24.075 1.00 22.95 ? 410  LEU B N   1 
ATOM   9058  C  CA  . LEU B  1 410 ? -31.130 63.906 23.871 1.00 22.61 ? 410  LEU B CA  1 
ATOM   9059  C  C   . LEU B  1 410 ? -32.020 63.526 22.686 1.00 22.75 ? 410  LEU B C   1 
ATOM   9060  O  O   . LEU B  1 410 ? -31.523 63.274 21.587 1.00 23.22 ? 410  LEU B O   1 
ATOM   9061  C  CB  . LEU B  1 410 ? -30.407 65.224 23.572 1.00 20.80 ? 410  LEU B CB  1 
ATOM   9062  C  CG  . LEU B  1 410 ? -31.230 66.489 23.326 1.00 21.66 ? 410  LEU B CG  1 
ATOM   9063  C  CD1 . LEU B  1 410 ? -31.955 66.859 24.603 1.00 20.59 ? 410  LEU B CD1 1 
ATOM   9064  C  CD2 . LEU B  1 410 ? -30.321 67.652 22.909 1.00 21.86 ? 410  LEU B CD2 1 
ATOM   9065  N  N   . THR B  1 411 ? -33.326 63.460 22.913 1.00 22.08 ? 411  THR B N   1 
ATOM   9066  C  CA  . THR B  1 411 ? -34.274 63.163 21.842 1.00 22.91 ? 411  THR B CA  1 
ATOM   9067  C  C   . THR B  1 411 ? -35.169 64.390 21.764 1.00 25.22 ? 411  THR B C   1 
ATOM   9068  O  O   . THR B  1 411 ? -35.039 65.307 22.578 1.00 24.26 ? 411  THR B O   1 
ATOM   9069  C  CB  . THR B  1 411 ? -35.183 61.964 22.160 1.00 22.41 ? 411  THR B CB  1 
ATOM   9070  O  OG1 . THR B  1 411 ? -36.012 62.296 23.283 1.00 22.45 ? 411  THR B OG1 1 
ATOM   9071  C  CG2 . THR B  1 411 ? -34.349 60.714 22.476 1.00 21.45 ? 411  THR B CG2 1 
ATOM   9072  N  N   . SER B  1 412 ? -36.088 64.407 20.803 1.00 25.92 ? 412  SER B N   1 
ATOM   9073  C  CA  . SER B  1 412 ? -36.981 65.546 20.669 1.00 28.20 ? 412  SER B CA  1 
ATOM   9074  C  C   . SER B  1 412 ? -37.863 65.740 21.906 1.00 28.16 ? 412  SER B C   1 
ATOM   9075  O  O   . SER B  1 412 ? -38.337 66.847 22.157 1.00 28.88 ? 412  SER B O   1 
ATOM   9076  C  CB  . SER B  1 412 ? -37.869 65.378 19.436 1.00 27.97 ? 412  SER B CB  1 
ATOM   9077  O  OG  . SER B  1 412 ? -38.589 64.174 19.530 1.00 29.21 ? 412  SER B OG  1 
ATOM   9078  N  N   . ASP B  1 413 ? -38.073 64.678 22.683 1.00 28.00 ? 413  ASP B N   1 
ATOM   9079  C  CA  . ASP B  1 413 ? -38.922 64.785 23.867 1.00 28.31 ? 413  ASP B CA  1 
ATOM   9080  C  C   . ASP B  1 413 ? -38.240 64.668 25.223 1.00 27.74 ? 413  ASP B C   1 
ATOM   9081  O  O   . ASP B  1 413 ? -38.723 65.230 26.213 1.00 27.74 ? 413  ASP B O   1 
ATOM   9082  C  CB  . ASP B  1 413 ? -40.045 63.744 23.820 1.00 31.47 ? 413  ASP B CB  1 
ATOM   9083  C  CG  . ASP B  1 413 ? -41.033 63.987 22.690 1.00 33.02 ? 413  ASP B CG  1 
ATOM   9084  O  OD1 . ASP B  1 413 ? -41.374 65.158 22.426 1.00 35.80 ? 413  ASP B OD1 1 
ATOM   9085  O  OD2 . ASP B  1 413 ? -41.486 63.003 22.078 1.00 35.15 ? 413  ASP B OD2 1 
ATOM   9086  N  N   . TYR B  1 414 ? -37.118 63.958 25.281 1.00 27.04 ? 414  TYR B N   1 
ATOM   9087  C  CA  . TYR B  1 414 ? -36.438 63.751 26.563 1.00 26.22 ? 414  TYR B CA  1 
ATOM   9088  C  C   . TYR B  1 414 ? -34.926 63.960 26.590 1.00 24.21 ? 414  TYR B C   1 
ATOM   9089  O  O   . TYR B  1 414 ? -34.258 63.810 25.577 1.00 23.19 ? 414  TYR B O   1 
ATOM   9090  C  CB  . TYR B  1 414 ? -36.717 62.317 27.053 1.00 26.86 ? 414  TYR B CB  1 
ATOM   9091  C  CG  . TYR B  1 414 ? -38.164 62.030 27.353 1.00 28.54 ? 414  TYR B CG  1 
ATOM   9092  C  CD1 . TYR B  1 414 ? -39.021 61.504 26.380 1.00 28.86 ? 414  TYR B CD1 1 
ATOM   9093  C  CD2 . TYR B  1 414 ? -38.687 62.312 28.616 1.00 29.36 ? 414  TYR B CD2 1 
ATOM   9094  C  CE1 . TYR B  1 414 ? -40.381 61.273 26.675 1.00 30.47 ? 414  TYR B CE1 1 
ATOM   9095  C  CE2 . TYR B  1 414 ? -40.024 62.087 28.915 1.00 30.66 ? 414  TYR B CE2 1 
ATOM   9096  C  CZ  . TYR B  1 414 ? -40.868 61.572 27.947 1.00 31.20 ? 414  TYR B CZ  1 
ATOM   9097  O  OH  . TYR B  1 414 ? -42.197 61.390 28.275 1.00 35.08 ? 414  TYR B OH  1 
ATOM   9098  N  N   . LEU B  1 415 ? -34.399 64.306 27.765 1.00 23.12 ? 415  LEU B N   1 
ATOM   9099  C  CA  . LEU B  1 415 ? -32.961 64.435 27.946 1.00 21.88 ? 415  LEU B CA  1 
ATOM   9100  C  C   . LEU B  1 415 ? -32.622 63.442 29.068 1.00 22.70 ? 415  LEU B C   1 
ATOM   9101  O  O   . LEU B  1 415 ? -33.253 63.448 30.132 1.00 22.95 ? 415  LEU B O   1 
ATOM   9102  C  CB  . LEU B  1 415 ? -32.561 65.858 28.330 1.00 20.92 ? 415  LEU B CB  1 
ATOM   9103  C  CG  . LEU B  1 415 ? -31.054 66.063 28.555 1.00 19.27 ? 415  LEU B CG  1 
ATOM   9104  C  CD1 . LEU B  1 415 ? -30.702 67.518 28.353 1.00 16.05 ? 415  LEU B CD1 1 
ATOM   9105  C  CD2 . LEU B  1 415 ? -30.678 65.575 29.964 1.00 19.14 ? 415  LEU B CD2 1 
ATOM   9106  N  N   . TYR B  1 416 ? -31.666 62.554 28.803 1.00 22.40 ? 416  TYR B N   1 
ATOM   9107  C  CA  . TYR B  1 416 ? -31.256 61.530 29.776 1.00 21.24 ? 416  TYR B CA  1 
ATOM   9108  C  C   . TYR B  1 416 ? -29.908 61.941 30.348 1.00 20.97 ? 416  TYR B C   1 
ATOM   9109  O  O   . TYR B  1 416 ? -29.029 62.371 29.599 1.00 21.38 ? 416  TYR B O   1 
ATOM   9110  C  CB  . TYR B  1 416 ? -31.116 60.162 29.089 1.00 20.09 ? 416  TYR B CB  1 
ATOM   9111  C  CG  . TYR B  1 416 ? -32.358 59.663 28.372 1.00 20.39 ? 416  TYR B CG  1 
ATOM   9112  C  CD1 . TYR B  1 416 ? -32.719 60.167 27.123 1.00 21.31 ? 416  TYR B CD1 1 
ATOM   9113  C  CD2 . TYR B  1 416 ? -33.177 58.694 28.947 1.00 20.27 ? 416  TYR B CD2 1 
ATOM   9114  C  CE1 . TYR B  1 416 ? -33.862 59.714 26.463 1.00 20.65 ? 416  TYR B CE1 1 
ATOM   9115  C  CE2 . TYR B  1 416 ? -34.318 58.239 28.305 1.00 21.34 ? 416  TYR B CE2 1 
ATOM   9116  C  CZ  . TYR B  1 416 ? -34.658 58.748 27.064 1.00 20.71 ? 416  TYR B CZ  1 
ATOM   9117  O  OH  . TYR B  1 416 ? -35.790 58.302 26.426 1.00 21.17 ? 416  TYR B OH  1 
ATOM   9118  N  N   . TYR B  1 417 ? -29.739 61.817 31.662 1.00 20.92 ? 417  TYR B N   1 
ATOM   9119  C  CA  . TYR B  1 417 ? -28.481 62.207 32.295 1.00 20.49 ? 417  TYR B CA  1 
ATOM   9120  C  C   . TYR B  1 417 ? -28.160 61.334 33.512 1.00 21.15 ? 417  TYR B C   1 
ATOM   9121  O  O   . TYR B  1 417 ? -29.025 60.616 34.004 1.00 21.04 ? 417  TYR B O   1 
ATOM   9122  C  CB  . TYR B  1 417 ? -28.540 63.691 32.688 1.00 20.33 ? 417  TYR B CB  1 
ATOM   9123  C  CG  . TYR B  1 417 ? -29.531 63.999 33.792 1.00 20.87 ? 417  TYR B CG  1 
ATOM   9124  C  CD1 . TYR B  1 417 ? -29.155 63.923 35.138 1.00 20.41 ? 417  TYR B CD1 1 
ATOM   9125  C  CD2 . TYR B  1 417 ? -30.850 64.337 33.496 1.00 20.09 ? 417  TYR B CD2 1 
ATOM   9126  C  CE1 . TYR B  1 417 ? -30.067 64.179 36.164 1.00 20.17 ? 417  TYR B CE1 1 
ATOM   9127  C  CE2 . TYR B  1 417 ? -31.769 64.588 34.511 1.00 20.74 ? 417  TYR B CE2 1 
ATOM   9128  C  CZ  . TYR B  1 417 ? -31.376 64.507 35.836 1.00 20.68 ? 417  TYR B CZ  1 
ATOM   9129  O  OH  . TYR B  1 417 ? -32.293 64.729 36.831 1.00 20.82 ? 417  TYR B OH  1 
ATOM   9130  N  N   . ILE B  1 418 ? -26.909 61.383 33.975 1.00 20.56 ? 418  ILE B N   1 
ATOM   9131  C  CA  . ILE B  1 418 ? -26.472 60.596 35.129 1.00 19.52 ? 418  ILE B CA  1 
ATOM   9132  C  C   . ILE B  1 418 ? -26.190 61.587 36.244 1.00 18.89 ? 418  ILE B C   1 
ATOM   9133  O  O   . ILE B  1 418 ? -25.528 62.594 36.006 1.00 18.52 ? 418  ILE B O   1 
ATOM   9134  C  CB  . ILE B  1 418 ? -25.135 59.831 34.839 1.00 20.40 ? 418  ILE B CB  1 
ATOM   9135  C  CG1 . ILE B  1 418 ? -25.346 58.704 33.815 1.00 20.72 ? 418  ILE B CG1 1 
ATOM   9136  C  CG2 . ILE B  1 418 ? -24.555 59.279 36.132 1.00 19.60 ? 418  ILE B CG2 1 
ATOM   9137  C  CD1 . ILE B  1 418 ? -26.282 57.619 34.281 1.00 21.23 ? 418  ILE B CD1 1 
ATOM   9138  N  N   . SER B  1 419 ? -26.671 61.312 37.455 1.00 18.61 ? 419  SER B N   1 
ATOM   9139  C  CA  . SER B  1 419 ? -26.424 62.215 38.583 1.00 19.43 ? 419  SER B CA  1 
ATOM   9140  C  C   . SER B  1 419 ? -26.259 61.419 39.854 1.00 18.97 ? 419  SER B C   1 
ATOM   9141  O  O   . SER B  1 419 ? -26.526 60.216 39.877 1.00 18.15 ? 419  SER B O   1 
ATOM   9142  C  CB  . SER B  1 419 ? -27.581 63.196 38.787 1.00 19.59 ? 419  SER B CB  1 
ATOM   9143  O  OG  . SER B  1 419 ? -28.658 62.567 39.461 1.00 21.75 ? 419  SER B OG  1 
ATOM   9144  N  N   . ASN B  1 420 ? -25.797 62.088 40.904 1.00 18.33 ? 420  ASN B N   1 
ATOM   9145  C  CA  . ASN B  1 420 ? -25.640 61.429 42.194 1.00 19.91 ? 420  ASN B CA  1 
ATOM   9146  C  C   . ASN B  1 420 ? -26.746 61.908 43.135 1.00 19.92 ? 420  ASN B C   1 
ATOM   9147  O  O   . ASN B  1 420 ? -26.544 61.978 44.331 1.00 18.58 ? 420  ASN B O   1 
ATOM   9148  C  CB  . ASN B  1 420 ? -24.267 61.724 42.819 1.00 19.71 ? 420  ASN B CB  1 
ATOM   9149  C  CG  . ASN B  1 420 ? -23.964 63.201 42.906 1.00 20.84 ? 420  ASN B CG  1 
ATOM   9150  O  OD1 . ASN B  1 420 ? -24.832 64.052 42.679 1.00 20.51 ? 420  ASN B OD1 1 
ATOM   9151  N  ND2 . ASN B  1 420 ? -22.713 63.523 43.246 1.00 23.60 ? 420  ASN B ND2 1 
ATOM   9152  N  N   . GLU B  1 421 ? -27.920 62.221 42.586 1.00 21.21 ? 421  GLU B N   1 
ATOM   9153  C  CA  . GLU B  1 421 ? -29.012 62.682 43.430 1.00 23.22 ? 421  GLU B CA  1 
ATOM   9154  C  C   . GLU B  1 421 ? -29.562 61.628 44.386 1.00 23.44 ? 421  GLU B C   1 
ATOM   9155  O  O   . GLU B  1 421 ? -29.804 61.916 45.552 1.00 25.28 ? 421  GLU B O   1 
ATOM   9156  C  CB  . GLU B  1 421 ? -30.193 63.224 42.601 1.00 23.96 ? 421  GLU B CB  1 
ATOM   9157  C  CG  . GLU B  1 421 ? -31.354 63.694 43.492 1.00 22.95 ? 421  GLU B CG  1 
ATOM   9158  C  CD  . GLU B  1 421 ? -32.566 64.195 42.726 1.00 26.13 ? 421  GLU B CD  1 
ATOM   9159  O  OE1 . GLU B  1 421 ? -32.621 64.044 41.488 1.00 25.89 ? 421  GLU B OE1 1 
ATOM   9160  O  OE2 . GLU B  1 421 ? -33.488 64.741 43.375 1.00 28.56 ? 421  GLU B OE2 1 
ATOM   9161  N  N   . TYR B  1 422 ? -29.766 60.418 43.896 1.00 24.12 ? 422  TYR B N   1 
ATOM   9162  C  CA  . TYR B  1 422 ? -30.340 59.371 44.716 1.00 24.44 ? 422  TYR B CA  1 
ATOM   9163  C  C   . TYR B  1 422 ? -29.760 59.238 46.123 1.00 25.60 ? 422  TYR B C   1 
ATOM   9164  O  O   . TYR B  1 422 ? -28.547 59.078 46.309 1.00 25.31 ? 422  TYR B O   1 
ATOM   9165  C  CB  . TYR B  1 422 ? -30.257 58.027 43.994 1.00 24.83 ? 422  TYR B CB  1 
ATOM   9166  C  CG  . TYR B  1 422 ? -31.175 56.966 44.587 1.00 27.12 ? 422  TYR B CG  1 
ATOM   9167  C  CD1 . TYR B  1 422 ? -32.565 57.147 44.616 1.00 27.58 ? 422  TYR B CD1 1 
ATOM   9168  C  CD2 . TYR B  1 422 ? -30.662 55.760 45.063 1.00 26.48 ? 422  TYR B CD2 1 
ATOM   9169  C  CE1 . TYR B  1 422 ? -33.415 56.141 45.094 1.00 27.31 ? 422  TYR B CE1 1 
ATOM   9170  C  CE2 . TYR B  1 422 ? -31.499 54.754 45.540 1.00 26.42 ? 422  TYR B CE2 1 
ATOM   9171  C  CZ  . TYR B  1 422 ? -32.865 54.943 45.550 1.00 27.55 ? 422  TYR B CZ  1 
ATOM   9172  O  OH  . TYR B  1 422 ? -33.686 53.920 45.971 1.00 28.53 ? 422  TYR B OH  1 
ATOM   9173  N  N   . LYS B  1 423 ? -30.662 59.299 47.105 1.00 26.13 ? 423  LYS B N   1 
ATOM   9174  C  CA  . LYS B  1 423 ? -30.342 59.180 48.521 1.00 25.66 ? 423  LYS B CA  1 
ATOM   9175  C  C   . LYS B  1 423 ? -29.268 60.148 48.982 1.00 24.92 ? 423  LYS B C   1 
ATOM   9176  O  O   . LYS B  1 423 ? -28.672 59.958 50.040 1.00 22.52 ? 423  LYS B O   1 
ATOM   9177  C  CB  . LYS B  1 423 ? -29.916 57.746 48.845 1.00 27.32 ? 423  LYS B CB  1 
ATOM   9178  C  CG  . LYS B  1 423 ? -31.023 56.692 48.700 1.00 30.20 ? 423  LYS B CG  1 
ATOM   9179  C  CD  . LYS B  1 423 ? -30.478 55.284 49.013 1.00 33.11 ? 423  LYS B CD  1 
ATOM   9180  C  CE  . LYS B  1 423 ? -31.522 54.175 48.804 1.00 35.42 ? 423  LYS B CE  1 
ATOM   9181  N  NZ  . LYS B  1 423 ? -32.788 54.431 49.560 1.00 37.20 ? 423  LYS B NZ  1 
ATOM   9182  N  N   . GLY B  1 424 ? -29.013 61.184 48.191 1.00 25.02 ? 424  GLY B N   1 
ATOM   9183  C  CA  . GLY B  1 424 ? -27.998 62.157 48.575 1.00 25.70 ? 424  GLY B CA  1 
ATOM   9184  C  C   . GLY B  1 424 ? -26.607 61.544 48.741 1.00 26.11 ? 424  GLY B C   1 
ATOM   9185  O  O   . GLY B  1 424 ? -25.826 62.001 49.578 1.00 26.40 ? 424  GLY B O   1 
ATOM   9186  N  N   . MET B  1 425 ? -26.301 60.519 47.940 1.00 25.14 ? 425  MET B N   1 
ATOM   9187  C  CA  . MET B  1 425 ? -25.007 59.833 47.996 1.00 24.58 ? 425  MET B CA  1 
ATOM   9188  C  C   . MET B  1 425 ? -24.122 60.357 46.866 1.00 23.52 ? 425  MET B C   1 
ATOM   9189  O  O   . MET B  1 425 ? -24.304 59.992 45.691 1.00 23.30 ? 425  MET B O   1 
ATOM   9190  C  CB  . MET B  1 425 ? -25.210 58.319 47.874 1.00 24.34 ? 425  MET B CB  1 
ATOM   9191  C  CG  . MET B  1 425 ? -25.991 57.732 49.053 1.00 27.66 ? 425  MET B CG  1 
ATOM   9192  S  SD  . MET B  1 425 ? -26.181 55.912 49.010 1.00 30.75 ? 425  MET B SD  1 
ATOM   9193  C  CE  . MET B  1 425 ? -24.501 55.369 49.399 1.00 29.45 ? 425  MET B CE  1 
ATOM   9194  N  N   . PRO B  1 426 ? -23.155 61.227 47.204 1.00 21.81 ? 426  PRO B N   1 
ATOM   9195  C  CA  . PRO B  1 426 ? -22.298 61.759 46.139 1.00 21.34 ? 426  PRO B CA  1 
ATOM   9196  C  C   . PRO B  1 426 ? -21.487 60.703 45.417 1.00 21.41 ? 426  PRO B C   1 
ATOM   9197  O  O   . PRO B  1 426 ? -21.045 60.918 44.286 1.00 20.63 ? 426  PRO B O   1 
ATOM   9198  C  CB  . PRO B  1 426 ? -21.456 62.830 46.846 1.00 21.38 ? 426  PRO B CB  1 
ATOM   9199  C  CG  . PRO B  1 426 ? -21.497 62.451 48.316 1.00 22.86 ? 426  PRO B CG  1 
ATOM   9200  C  CD  . PRO B  1 426 ? -22.878 61.856 48.514 1.00 22.23 ? 426  PRO B CD  1 
ATOM   9201  N  N   . GLY B  1 427 ? -21.339 59.550 46.068 1.00 20.83 ? 427  GLY B N   1 
ATOM   9202  C  CA  . GLY B  1 427 ? -20.605 58.446 45.498 1.00 19.46 ? 427  GLY B CA  1 
ATOM   9203  C  C   . GLY B  1 427 ? -21.451 57.465 44.696 1.00 21.37 ? 427  GLY B C   1 
ATOM   9204  O  O   . GLY B  1 427 ? -20.930 56.446 44.248 1.00 21.39 ? 427  GLY B O   1 
ATOM   9205  N  N   . GLY B  1 428 ? -22.748 57.747 44.530 1.00 20.25 ? 428  GLY B N   1 
ATOM   9206  C  CA  . GLY B  1 428 ? -23.606 56.875 43.740 1.00 19.56 ? 428  GLY B CA  1 
ATOM   9207  C  C   . GLY B  1 428 ? -23.887 57.523 42.382 1.00 20.04 ? 428  GLY B C   1 
ATOM   9208  O  O   . GLY B  1 428 ? -23.661 58.724 42.205 1.00 20.82 ? 428  GLY B O   1 
ATOM   9209  N  N   . ARG B  1 429 ? -24.354 56.745 41.410 1.00 19.48 ? 429  ARG B N   1 
ATOM   9210  C  CA  . ARG B  1 429 ? -24.651 57.291 40.078 1.00 20.48 ? 429  ARG B CA  1 
ATOM   9211  C  C   . ARG B  1 429 ? -25.895 56.618 39.522 1.00 20.95 ? 429  ARG B C   1 
ATOM   9212  O  O   . ARG B  1 429 ? -25.986 55.390 39.519 1.00 20.97 ? 429  ARG B O   1 
ATOM   9213  C  CB  . ARG B  1 429 ? -23.489 57.046 39.089 1.00 20.09 ? 429  ARG B CB  1 
ATOM   9214  C  CG  . ARG B  1 429 ? -22.107 57.615 39.485 1.00 21.36 ? 429  ARG B CG  1 
ATOM   9215  C  CD  . ARG B  1 429 ? -21.907 59.045 39.019 1.00 20.59 ? 429  ARG B CD  1 
ATOM   9216  N  NE  . ARG B  1 429 ? -20.587 59.569 39.345 1.00 22.13 ? 429  ARG B NE  1 
ATOM   9217  C  CZ  . ARG B  1 429 ? -20.148 59.851 40.574 1.00 23.81 ? 429  ARG B CZ  1 
ATOM   9218  N  NH1 . ARG B  1 429 ? -20.924 59.653 41.637 1.00 23.53 ? 429  ARG B NH1 1 
ATOM   9219  N  NH2 . ARG B  1 429 ? -18.925 60.366 40.742 1.00 23.65 ? 429  ARG B NH2 1 
ATOM   9220  N  N   . ASN B  1 430 ? -26.856 57.409 39.049 1.00 20.93 ? 430  ASN B N   1 
ATOM   9221  C  CA  . ASN B  1 430 ? -28.065 56.828 38.472 1.00 19.69 ? 430  ASN B CA  1 
ATOM   9222  C  C   . ASN B  1 430 ? -28.484 57.552 37.208 1.00 19.03 ? 430  ASN B C   1 
ATOM   9223  O  O   . ASN B  1 430 ? -28.138 58.707 37.004 1.00 19.01 ? 430  ASN B O   1 
ATOM   9224  C  CB  . ASN B  1 430 ? -29.213 56.847 39.489 1.00 20.60 ? 430  ASN B CB  1 
ATOM   9225  C  CG  . ASN B  1 430 ? -29.173 55.659 40.432 1.00 21.15 ? 430  ASN B CG  1 
ATOM   9226  O  OD1 . ASN B  1 430 ? -29.449 54.511 40.035 1.00 19.08 ? 430  ASN B OD1 1 
ATOM   9227  N  ND2 . ASN B  1 430 ? -28.823 55.924 41.691 1.00 19.77 ? 430  ASN B ND2 1 
ATOM   9228  N  N   . LEU B  1 431 ? -29.229 56.849 36.365 1.00 18.31 ? 431  LEU B N   1 
ATOM   9229  C  CA  . LEU B  1 431 ? -29.716 57.393 35.111 1.00 18.98 ? 431  LEU B CA  1 
ATOM   9230  C  C   . LEU B  1 431 ? -31.094 58.030 35.290 1.00 20.60 ? 431  LEU B C   1 
ATOM   9231  O  O   . LEU B  1 431 ? -31.993 57.432 35.910 1.00 19.95 ? 431  LEU B O   1 
ATOM   9232  C  CB  . LEU B  1 431 ? -29.812 56.291 34.067 1.00 18.05 ? 431  LEU B CB  1 
ATOM   9233  C  CG  . LEU B  1 431 ? -30.392 56.758 32.733 1.00 18.57 ? 431  LEU B CG  1 
ATOM   9234  C  CD1 . LEU B  1 431 ? -29.438 57.758 32.061 1.00 17.14 ? 431  LEU B CD1 1 
ATOM   9235  C  CD2 . LEU B  1 431 ? -30.622 55.540 31.852 1.00 18.20 ? 431  LEU B CD2 1 
ATOM   9236  N  N   . TYR B  1 432 ? -31.255 59.228 34.737 1.00 19.90 ? 432  TYR B N   1 
ATOM   9237  C  CA  . TYR B  1 432 ? -32.508 59.971 34.837 1.00 22.16 ? 432  TYR B CA  1 
ATOM   9238  C  C   . TYR B  1 432 ? -33.008 60.445 33.484 1.00 22.06 ? 432  TYR B C   1 
ATOM   9239  O  O   . TYR B  1 432 ? -32.236 60.632 32.541 1.00 21.59 ? 432  TYR B O   1 
ATOM   9240  C  CB  . TYR B  1 432 ? -32.361 61.189 35.771 1.00 22.26 ? 432  TYR B CB  1 
ATOM   9241  C  CG  . TYR B  1 432 ? -32.104 60.840 37.227 1.00 24.44 ? 432  TYR B CG  1 
ATOM   9242  C  CD1 . TYR B  1 432 ? -30.826 60.492 37.666 1.00 23.74 ? 432  TYR B CD1 1 
ATOM   9243  C  CD2 . TYR B  1 432 ? -33.139 60.889 38.177 1.00 23.74 ? 432  TYR B CD2 1 
ATOM   9244  C  CE1 . TYR B  1 432 ? -30.575 60.213 39.024 1.00 24.90 ? 432  TYR B CE1 1 
ATOM   9245  C  CE2 . TYR B  1 432 ? -32.898 60.607 39.538 1.00 24.05 ? 432  TYR B CE2 1 
ATOM   9246  C  CZ  . TYR B  1 432 ? -31.609 60.275 39.951 1.00 25.27 ? 432  TYR B CZ  1 
ATOM   9247  O  OH  . TYR B  1 432 ? -31.333 60.035 41.288 1.00 25.99 ? 432  TYR B OH  1 
ATOM   9248  N  N   . LYS B  1 433 ? -34.314 60.654 33.419 1.00 23.05 ? 433  LYS B N   1 
ATOM   9249  C  CA  . LYS B  1 433 ? -34.987 61.107 32.214 1.00 23.39 ? 433  LYS B CA  1 
ATOM   9250  C  C   . LYS B  1 433 ? -35.821 62.334 32.570 1.00 24.69 ? 433  LYS B C   1 
ATOM   9251  O  O   . LYS B  1 433 ? -36.607 62.310 33.526 1.00 24.97 ? 433  LYS B O   1 
ATOM   9252  C  CB  . LYS B  1 433 ? -35.905 59.998 31.682 1.00 24.25 ? 433  LYS B CB  1 
ATOM   9253  C  CG  . LYS B  1 433 ? -36.825 60.448 30.576 1.00 26.71 ? 433  LYS B CG  1 
ATOM   9254  C  CD  . LYS B  1 433 ? -37.276 59.319 29.679 1.00 26.78 ? 433  LYS B CD  1 
ATOM   9255  C  CE  . LYS B  1 433 ? -38.581 58.701 30.143 1.00 29.17 ? 433  LYS B CE  1 
ATOM   9256  N  NZ  . LYS B  1 433 ? -39.263 57.992 29.006 1.00 27.67 ? 433  LYS B NZ  1 
ATOM   9257  N  N   . ILE B  1 434 ? -35.649 63.417 31.828 1.00 24.28 ? 434  ILE B N   1 
ATOM   9258  C  CA  . ILE B  1 434 ? -36.446 64.589 32.114 1.00 24.86 ? 434  ILE B CA  1 
ATOM   9259  C  C   . ILE B  1 434 ? -37.208 64.991 30.857 1.00 25.28 ? 434  ILE B C   1 
ATOM   9260  O  O   . ILE B  1 434 ? -36.659 65.008 29.752 1.00 26.03 ? 434  ILE B O   1 
ATOM   9261  C  CB  . ILE B  1 434 ? -35.582 65.760 32.685 1.00 25.19 ? 434  ILE B CB  1 
ATOM   9262  C  CG1 . ILE B  1 434 ? -36.480 66.970 32.990 1.00 25.96 ? 434  ILE B CG1 1 
ATOM   9263  C  CG2 . ILE B  1 434 ? -34.438 66.112 31.744 1.00 25.24 ? 434  ILE B CG2 1 
ATOM   9264  C  CD1 . ILE B  1 434 ? -35.754 68.098 33.726 1.00 25.74 ? 434  ILE B CD1 1 
ATOM   9265  N  N   . GLN B  1 435 ? -38.499 65.249 31.034 1.00 25.37 ? 435  GLN B N   1 
ATOM   9266  C  CA  . GLN B  1 435 ? -39.367 65.626 29.930 1.00 26.66 ? 435  GLN B CA  1 
ATOM   9267  C  C   . GLN B  1 435 ? -39.046 67.060 29.532 1.00 26.30 ? 435  GLN B C   1 
ATOM   9268  O  O   . GLN B  1 435 ? -39.115 67.978 30.349 1.00 25.27 ? 435  GLN B O   1 
ATOM   9269  C  CB  . GLN B  1 435 ? -40.833 65.493 30.355 1.00 27.88 ? 435  GLN B CB  1 
ATOM   9270  C  CG  . GLN B  1 435 ? -41.830 65.593 29.225 1.00 29.34 ? 435  GLN B CG  1 
ATOM   9271  C  CD  . GLN B  1 435 ? -43.253 65.435 29.727 1.00 32.15 ? 435  GLN B CD  1 
ATOM   9272  O  OE1 . GLN B  1 435 ? -43.586 64.444 30.367 1.00 33.10 ? 435  GLN B OE1 1 
ATOM   9273  N  NE2 . GLN B  1 435 ? -44.094 66.419 29.446 1.00 34.54 ? 435  GLN B NE2 1 
ATOM   9274  N  N   . LEU B  1 436 ? -38.693 67.253 28.269 1.00 26.65 ? 436  LEU B N   1 
ATOM   9275  C  CA  . LEU B  1 436 ? -38.327 68.582 27.817 1.00 27.71 ? 436  LEU B CA  1 
ATOM   9276  C  C   . LEU B  1 436 ? -39.505 69.562 27.851 1.00 29.00 ? 436  LEU B C   1 
ATOM   9277  O  O   . LEU B  1 436 ? -39.300 70.762 28.008 1.00 28.97 ? 436  LEU B O   1 
ATOM   9278  C  CB  . LEU B  1 436 ? -37.691 68.513 26.418 1.00 24.95 ? 436  LEU B CB  1 
ATOM   9279  C  CG  . LEU B  1 436 ? -36.403 67.666 26.326 1.00 24.91 ? 436  LEU B CG  1 
ATOM   9280  C  CD1 . LEU B  1 436 ? -35.804 67.761 24.924 1.00 25.21 ? 436  LEU B CD1 1 
ATOM   9281  C  CD2 . LEU B  1 436 ? -35.402 68.137 27.341 1.00 24.01 ? 436  LEU B CD2 1 
ATOM   9282  N  N   . SER B  1 437 ? -40.733 69.063 27.740 1.00 30.67 ? 437  SER B N   1 
ATOM   9283  C  CA  . SER B  1 437 ? -41.908 69.947 27.768 1.00 31.94 ? 437  SER B CA  1 
ATOM   9284  C  C   . SER B  1 437 ? -42.453 70.197 29.177 1.00 32.90 ? 437  SER B C   1 
ATOM   9285  O  O   . SER B  1 437 ? -43.345 71.025 29.359 1.00 34.17 ? 437  SER B O   1 
ATOM   9286  C  CB  . SER B  1 437 ? -43.026 69.373 26.895 1.00 31.27 ? 437  SER B CB  1 
ATOM   9287  O  OG  . SER B  1 437 ? -43.477 68.128 27.405 1.00 32.53 ? 437  SER B OG  1 
ATOM   9288  N  N   . ASP B  1 438 ? -41.917 69.487 30.168 1.00 34.12 ? 438  ASP B N   1 
ATOM   9289  C  CA  . ASP B  1 438 ? -42.358 69.639 31.556 1.00 34.32 ? 438  ASP B CA  1 
ATOM   9290  C  C   . ASP B  1 438 ? -41.228 69.217 32.489 1.00 33.81 ? 438  ASP B C   1 
ATOM   9291  O  O   . ASP B  1 438 ? -41.146 68.050 32.889 1.00 32.69 ? 438  ASP B O   1 
ATOM   9292  C  CB  . ASP B  1 438 ? -43.598 68.771 31.810 1.00 36.71 ? 438  ASP B CB  1 
ATOM   9293  C  CG  . ASP B  1 438 ? -44.278 69.085 33.145 1.00 38.54 ? 438  ASP B CG  1 
ATOM   9294  O  OD1 . ASP B  1 438 ? -43.663 69.780 33.981 1.00 39.20 ? 438  ASP B OD1 1 
ATOM   9295  O  OD2 . ASP B  1 438 ? -45.426 68.622 33.359 1.00 40.93 ? 438  ASP B OD2 1 
ATOM   9296  N  N   . TYR B  1 439 ? -40.368 70.179 32.834 1.00 33.91 ? 439  TYR B N   1 
ATOM   9297  C  CA  . TYR B  1 439 ? -39.210 69.935 33.697 1.00 33.84 ? 439  TYR B CA  1 
ATOM   9298  C  C   . TYR B  1 439 ? -39.533 69.340 35.060 1.00 33.90 ? 439  TYR B C   1 
ATOM   9299  O  O   . TYR B  1 439 ? -38.634 68.819 35.727 1.00 34.20 ? 439  TYR B O   1 
ATOM   9300  C  CB  . TYR B  1 439 ? -38.405 71.222 33.927 1.00 33.76 ? 439  TYR B CB  1 
ATOM   9301  C  CG  . TYR B  1 439 ? -37.818 71.833 32.679 1.00 33.98 ? 439  TYR B CG  1 
ATOM   9302  C  CD1 . TYR B  1 439 ? -37.455 71.035 31.598 1.00 34.41 ? 439  TYR B CD1 1 
ATOM   9303  C  CD2 . TYR B  1 439 ? -37.649 73.211 32.568 1.00 34.29 ? 439  TYR B CD2 1 
ATOM   9304  C  CE1 . TYR B  1 439 ? -36.943 71.593 30.428 1.00 34.50 ? 439  TYR B CE1 1 
ATOM   9305  C  CE2 . TYR B  1 439 ? -37.139 73.779 31.401 1.00 34.05 ? 439  TYR B CE2 1 
ATOM   9306  C  CZ  . TYR B  1 439 ? -36.791 72.966 30.341 1.00 34.06 ? 439  TYR B CZ  1 
ATOM   9307  O  OH  . TYR B  1 439 ? -36.289 73.514 29.187 1.00 34.80 ? 439  TYR B OH  1 
ATOM   9308  N  N   . THR B  1 440 ? -40.790 69.427 35.489 1.00 32.16 ? 440  THR B N   1 
ATOM   9309  C  CA  . THR B  1 440 ? -41.147 68.878 36.791 1.00 31.67 ? 440  THR B CA  1 
ATOM   9310  C  C   . THR B  1 440 ? -41.293 67.378 36.652 1.00 30.91 ? 440  THR B C   1 
ATOM   9311  O  O   . THR B  1 440 ? -41.422 66.665 37.640 1.00 31.93 ? 440  THR B O   1 
ATOM   9312  C  CB  . THR B  1 440 ? -42.488 69.454 37.343 1.00 31.31 ? 440  THR B CB  1 
ATOM   9313  O  OG1 . THR B  1 440 ? -43.584 68.928 36.587 1.00 31.54 ? 440  THR B OG1 1 
ATOM   9314  C  CG2 . THR B  1 440 ? -42.496 70.969 37.262 1.00 31.12 ? 440  THR B CG2 1 
ATOM   9315  N  N   . LYS B  1 441 ? -41.267 66.900 35.417 1.00 29.40 ? 441  LYS B N   1 
ATOM   9316  C  CA  . LYS B  1 441 ? -41.391 65.474 35.180 1.00 28.33 ? 441  LYS B CA  1 
ATOM   9317  C  C   . LYS B  1 441 ? -40.005 64.864 34.994 1.00 26.32 ? 441  LYS B C   1 
ATOM   9318  O  O   . LYS B  1 441 ? -39.412 64.937 33.925 1.00 26.46 ? 441  LYS B O   1 
ATOM   9319  C  CB  . LYS B  1 441 ? -42.283 65.233 33.958 1.00 29.33 ? 441  LYS B CB  1 
ATOM   9320  C  CG  . LYS B  1 441 ? -43.707 65.803 34.124 1.00 31.43 ? 441  LYS B CG  1 
ATOM   9321  C  CD  . LYS B  1 441 ? -44.474 65.113 35.271 1.00 34.83 ? 441  LYS B CD  1 
ATOM   9322  C  CE  . LYS B  1 441 ? -45.944 65.569 35.375 1.00 37.29 ? 441  LYS B CE  1 
ATOM   9323  N  NZ  . LYS B  1 441 ? -46.080 66.960 35.934 1.00 38.99 ? 441  LYS B NZ  1 
ATOM   9324  N  N   . VAL B  1 442 ? -39.487 64.276 36.063 1.00 25.23 ? 442  VAL B N   1 
ATOM   9325  C  CA  . VAL B  1 442 ? -38.171 63.657 36.053 1.00 25.16 ? 442  VAL B CA  1 
ATOM   9326  C  C   . VAL B  1 442 ? -38.324 62.269 36.600 1.00 24.61 ? 442  VAL B C   1 
ATOM   9327  O  O   . VAL B  1 442 ? -38.771 62.095 37.722 1.00 25.03 ? 442  VAL B O   1 
ATOM   9328  C  CB  . VAL B  1 442 ? -37.166 64.389 36.968 1.00 24.76 ? 442  VAL B CB  1 
ATOM   9329  C  CG1 . VAL B  1 442 ? -35.853 63.609 37.014 1.00 25.03 ? 442  VAL B CG1 1 
ATOM   9330  C  CG2 . VAL B  1 442 ? -36.926 65.802 36.472 1.00 24.40 ? 442  VAL B CG2 1 
ATOM   9331  N  N   . THR B  1 443 ? -37.930 61.281 35.813 1.00 24.31 ? 443  THR B N   1 
ATOM   9332  C  CA  . THR B  1 443 ? -38.057 59.896 36.225 1.00 23.84 ? 443  THR B CA  1 
ATOM   9333  C  C   . THR B  1 443 ? -36.673 59.282 36.388 1.00 24.65 ? 443  THR B C   1 
ATOM   9334  O  O   . THR B  1 443 ? -35.809 59.478 35.519 1.00 23.86 ? 443  THR B O   1 
ATOM   9335  C  CB  . THR B  1 443 ? -38.783 59.078 35.135 1.00 24.40 ? 443  THR B CB  1 
ATOM   9336  O  OG1 . THR B  1 443 ? -40.067 59.657 34.862 1.00 25.69 ? 443  THR B OG1 1 
ATOM   9337  C  CG2 . THR B  1 443 ? -38.945 57.637 35.582 1.00 24.75 ? 443  THR B CG2 1 
ATOM   9338  N  N   . CYS B  1 444 ? -36.447 58.558 37.484 1.00 23.95 ? 444  CYS B N   1 
ATOM   9339  C  CA  . CYS B  1 444 ? -35.173 57.888 37.640 1.00 24.41 ? 444  CYS B CA  1 
ATOM   9340  C  C   . CYS B  1 444 ? -35.351 56.511 36.990 1.00 24.71 ? 444  CYS B C   1 
ATOM   9341  O  O   . CYS B  1 444 ? -36.218 55.722 37.402 1.00 24.95 ? 444  CYS B O   1 
ATOM   9342  C  CB  . CYS B  1 444 ? -34.767 57.721 39.112 1.00 25.67 ? 444  CYS B CB  1 
ATOM   9343  S  SG  . CYS B  1 444 ? -33.073 56.957 39.226 1.00 25.67 ? 444  CYS B SG  1 
ATOM   9344  N  N   . LEU B  1 445 ? -34.541 56.216 35.975 1.00 23.66 ? 445  LEU B N   1 
ATOM   9345  C  CA  . LEU B  1 445 ? -34.659 54.935 35.278 1.00 24.63 ? 445  LEU B CA  1 
ATOM   9346  C  C   . LEU B  1 445 ? -33.897 53.749 35.883 1.00 24.45 ? 445  LEU B C   1 
ATOM   9347  O  O   . LEU B  1 445 ? -34.134 52.603 35.503 1.00 26.30 ? 445  LEU B O   1 
ATOM   9348  C  CB  . LEU B  1 445 ? -34.208 55.095 33.828 1.00 21.99 ? 445  LEU B CB  1 
ATOM   9349  C  CG  . LEU B  1 445 ? -34.845 56.259 33.064 1.00 23.47 ? 445  LEU B CG  1 
ATOM   9350  C  CD1 . LEU B  1 445 ? -34.234 56.366 31.668 1.00 20.13 ? 445  LEU B CD1 1 
ATOM   9351  C  CD2 . LEU B  1 445 ? -36.364 56.050 32.983 1.00 22.02 ? 445  LEU B CD2 1 
ATOM   9352  N  N   . SER B  1 446 ? -32.999 54.008 36.829 1.00 24.97 ? 446  SER B N   1 
ATOM   9353  C  CA  . SER B  1 446 ? -32.181 52.937 37.393 1.00 24.13 ? 446  SER B CA  1 
ATOM   9354  C  C   . SER B  1 446 ? -32.202 52.765 38.903 1.00 24.07 ? 446  SER B C   1 
ATOM   9355  O  O   . SER B  1 446 ? -31.845 51.698 39.391 1.00 23.53 ? 446  SER B O   1 
ATOM   9356  C  CB  . SER B  1 446 ? -30.717 53.148 36.986 1.00 23.46 ? 446  SER B CB  1 
ATOM   9357  O  OG  . SER B  1 446 ? -30.211 54.376 37.511 1.00 19.34 ? 446  SER B OG  1 
ATOM   9358  N  N   . CYS B  1 447 ? -32.589 53.823 39.620 1.00 24.54 ? 447  CYS B N   1 
ATOM   9359  C  CA  . CYS B  1 447 ? -32.584 53.852 41.082 1.00 24.99 ? 447  CYS B CA  1 
ATOM   9360  C  C   . CYS B  1 447 ? -33.129 52.632 41.797 1.00 25.91 ? 447  CYS B C   1 
ATOM   9361  O  O   . CYS B  1 447 ? -32.489 52.066 42.677 1.00 24.36 ? 447  CYS B O   1 
ATOM   9362  C  CB  . CYS B  1 447 ? -33.363 55.073 41.597 1.00 25.99 ? 447  CYS B CB  1 
ATOM   9363  S  SG  . CYS B  1 447 ? -32.669 56.695 41.204 1.00 29.77 ? 447  CYS B SG  1 
ATOM   9364  N  N   . GLU B  1 448 ? -34.326 52.234 41.393 1.00 27.44 ? 448  GLU B N   1 
ATOM   9365  C  CA  . GLU B  1 448 ? -35.052 51.145 42.029 1.00 29.14 ? 448  GLU B CA  1 
ATOM   9366  C  C   . GLU B  1 448 ? -34.928 49.772 41.372 1.00 29.01 ? 448  GLU B C   1 
ATOM   9367  O  O   . GLU B  1 448 ? -35.573 48.820 41.804 1.00 29.42 ? 448  GLU B O   1 
ATOM   9368  C  CB  . GLU B  1 448 ? -36.533 51.555 42.092 1.00 30.10 ? 448  GLU B CB  1 
ATOM   9369  C  CG  . GLU B  1 448 ? -37.109 51.828 43.456 1.00 34.07 ? 448  GLU B CG  1 
ATOM   9370  C  CD  . GLU B  1 448 ? -36.173 52.535 44.404 1.00 34.70 ? 448  GLU B CD  1 
ATOM   9371  O  OE1 . GLU B  1 448 ? -36.016 53.768 44.313 1.00 35.56 ? 448  GLU B OE1 1 
ATOM   9372  O  OE2 . GLU B  1 448 ? -35.593 51.835 45.253 1.00 37.53 ? 448  GLU B OE2 1 
ATOM   9373  N  N   . LEU B  1 449 ? -34.123 49.650 40.329 1.00 28.58 ? 449  LEU B N   1 
ATOM   9374  C  CA  . LEU B  1 449 ? -34.009 48.347 39.676 1.00 29.11 ? 449  LEU B CA  1 
ATOM   9375  C  C   . LEU B  1 449 ? -33.567 47.255 40.652 1.00 29.69 ? 449  LEU B C   1 
ATOM   9376  O  O   . LEU B  1 449 ? -34.186 46.195 40.733 1.00 29.56 ? 449  LEU B O   1 
ATOM   9377  C  CB  . LEU B  1 449 ? -33.053 48.423 38.485 1.00 28.38 ? 449  LEU B CB  1 
ATOM   9378  C  CG  . LEU B  1 449 ? -33.487 49.330 37.331 1.00 28.83 ? 449  LEU B CG  1 
ATOM   9379  C  CD1 . LEU B  1 449 ? -32.411 49.313 36.224 1.00 26.77 ? 449  LEU B CD1 1 
ATOM   9380  C  CD2 . LEU B  1 449 ? -34.833 48.858 36.794 1.00 27.56 ? 449  LEU B CD2 1 
ATOM   9381  N  N   . ASN B  1 450 ? -32.496 47.518 41.394 1.00 30.62 ? 450  ASN B N   1 
ATOM   9382  C  CA  . ASN B  1 450 ? -31.988 46.584 42.394 1.00 30.65 ? 450  ASN B CA  1 
ATOM   9383  C  C   . ASN B  1 450 ? -31.161 47.463 43.300 1.00 31.43 ? 450  ASN B C   1 
ATOM   9384  O  O   . ASN B  1 450 ? -29.929 47.444 43.256 1.00 32.19 ? 450  ASN B O   1 
ATOM   9385  C  CB  . ASN B  1 450 ? -31.095 45.526 41.770 1.00 29.75 ? 450  ASN B CB  1 
ATOM   9386  C  CG  . ASN B  1 450 ? -30.833 44.372 42.720 1.00 31.59 ? 450  ASN B CG  1 
ATOM   9387  O  OD1 . ASN B  1 450 ? -30.802 44.551 43.952 1.00 31.02 ? 450  ASN B OD1 1 
ATOM   9388  N  ND2 . ASN B  1 450 ? -30.632 43.183 42.161 1.00 29.90 ? 450  ASN B ND2 1 
ATOM   9389  N  N   . PRO B  1 451 ? -31.836 48.247 44.139 1.00 31.51 ? 451  PRO B N   1 
ATOM   9390  C  CA  . PRO B  1 451 ? -31.183 49.167 45.064 1.00 31.43 ? 451  PRO B CA  1 
ATOM   9391  C  C   . PRO B  1 451 ? -30.086 48.621 45.963 1.00 32.15 ? 451  PRO B C   1 
ATOM   9392  O  O   . PRO B  1 451 ? -29.135 49.342 46.261 1.00 31.48 ? 451  PRO B O   1 
ATOM   9393  C  CB  . PRO B  1 451 ? -32.352 49.770 45.844 1.00 31.59 ? 451  PRO B CB  1 
ATOM   9394  C  CG  . PRO B  1 451 ? -33.386 48.699 45.809 1.00 32.01 ? 451  PRO B CG  1 
ATOM   9395  C  CD  . PRO B  1 451 ? -33.290 48.192 44.380 1.00 32.83 ? 451  PRO B CD  1 
ATOM   9396  N  N   . GLU B  1 452 ? -30.190 47.365 46.391 1.00 32.06 ? 452  GLU B N   1 
ATOM   9397  C  CA  . GLU B  1 452 ? -29.172 46.818 47.284 1.00 32.73 ? 452  GLU B CA  1 
ATOM   9398  C  C   . GLU B  1 452 ? -27.916 46.474 46.523 1.00 30.71 ? 452  GLU B C   1 
ATOM   9399  O  O   . GLU B  1 452 ? -26.806 46.709 46.994 1.00 30.27 ? 452  GLU B O   1 
ATOM   9400  C  CB  . GLU B  1 452 ? -29.669 45.555 48.009 1.00 35.48 ? 452  GLU B CB  1 
ATOM   9401  C  CG  . GLU B  1 452 ? -31.020 45.723 48.691 1.00 41.03 ? 452  GLU B CG  1 
ATOM   9402  C  CD  . GLU B  1 452 ? -32.193 45.412 47.762 1.00 45.26 ? 452  GLU B CD  1 
ATOM   9403  O  OE1 . GLU B  1 452 ? -32.112 45.696 46.535 1.00 46.93 ? 452  GLU B OE1 1 
ATOM   9404  O  OE2 . GLU B  1 452 ? -33.211 44.882 48.269 1.00 48.20 ? 452  GLU B OE2 1 
ATOM   9405  N  N   . ARG B  1 453 ? -28.099 45.924 45.336 1.00 28.57 ? 453  ARG B N   1 
ATOM   9406  C  CA  . ARG B  1 453 ? -26.973 45.506 44.525 1.00 28.07 ? 453  ARG B CA  1 
ATOM   9407  C  C   . ARG B  1 453 ? -26.405 46.589 43.612 1.00 27.78 ? 453  ARG B C   1 
ATOM   9408  O  O   . ARG B  1 453 ? -25.206 46.605 43.349 1.00 27.74 ? 453  ARG B O   1 
ATOM   9409  C  CB  . ARG B  1 453 ? -27.389 44.300 43.672 1.00 26.19 ? 453  ARG B CB  1 
ATOM   9410  C  CG  . ARG B  1 453 ? -26.312 43.794 42.733 1.00 26.15 ? 453  ARG B CG  1 
ATOM   9411  C  CD  . ARG B  1 453 ? -26.782 42.623 41.866 1.00 25.35 ? 453  ARG B CD  1 
ATOM   9412  N  NE  . ARG B  1 453 ? -25.707 42.176 40.989 1.00 25.49 ? 453  ARG B NE  1 
ATOM   9413  C  CZ  . ARG B  1 453 ? -25.743 41.087 40.225 1.00 26.76 ? 453  ARG B CZ  1 
ATOM   9414  N  NH1 . ARG B  1 453 ? -26.821 40.306 40.225 1.00 26.68 ? 453  ARG B NH1 1 
ATOM   9415  N  NH2 . ARG B  1 453 ? -24.695 40.776 39.461 1.00 23.73 ? 453  ARG B NH2 1 
ATOM   9416  N  N   . CYS B  1 454 ? -27.261 47.496 43.147 1.00 26.76 ? 454  CYS B N   1 
ATOM   9417  C  CA  . CYS B  1 454 ? -26.839 48.512 42.187 1.00 25.66 ? 454  CYS B CA  1 
ATOM   9418  C  C   . CYS B  1 454 ? -27.066 49.973 42.539 1.00 24.33 ? 454  CYS B C   1 
ATOM   9419  O  O   . CYS B  1 454 ? -28.199 50.422 42.634 1.00 22.02 ? 454  CYS B O   1 
ATOM   9420  C  CB  . CYS B  1 454 ? -27.511 48.206 40.849 1.00 26.09 ? 454  CYS B CB  1 
ATOM   9421  S  SG  . CYS B  1 454 ? -26.985 46.606 40.178 1.00 27.88 ? 454  CYS B SG  1 
ATOM   9422  N  N   . GLN B  1 455 ? -25.975 50.712 42.700 1.00 24.33 ? 455  GLN B N   1 
ATOM   9423  C  CA  . GLN B  1 455 ? -26.063 52.125 43.026 1.00 26.13 ? 455  GLN B CA  1 
ATOM   9424  C  C   . GLN B  1 455 ? -25.081 52.951 42.193 1.00 26.10 ? 455  GLN B C   1 
ATOM   9425  O  O   . GLN B  1 455 ? -24.943 54.156 42.409 1.00 26.72 ? 455  GLN B O   1 
ATOM   9426  C  CB  . GLN B  1 455 ? -25.781 52.351 44.515 1.00 26.51 ? 455  GLN B CB  1 
ATOM   9427  C  CG  . GLN B  1 455 ? -26.607 51.486 45.456 1.00 30.65 ? 455  GLN B CG  1 
ATOM   9428  C  CD  . GLN B  1 455 ? -26.313 51.778 46.929 1.00 32.90 ? 455  GLN B CD  1 
ATOM   9429  O  OE1 . GLN B  1 455 ? -25.157 51.841 47.349 1.00 32.74 ? 455  GLN B OE1 1 
ATOM   9430  N  NE2 . GLN B  1 455 ? -27.366 51.959 47.714 1.00 35.68 ? 455  GLN B NE2 1 
ATOM   9431  N  N   . TYR B  1 456 ? -24.388 52.313 41.252 1.00 25.75 ? 456  TYR B N   1 
ATOM   9432  C  CA  . TYR B  1 456 ? -23.422 53.028 40.412 1.00 24.69 ? 456  TYR B CA  1 
ATOM   9433  C  C   . TYR B  1 456 ? -23.601 52.548 38.976 1.00 24.33 ? 456  TYR B C   1 
ATOM   9434  O  O   . TYR B  1 456 ? -23.131 51.477 38.572 1.00 25.16 ? 456  TYR B O   1 
ATOM   9435  C  CB  . TYR B  1 456 ? -21.989 52.778 40.903 1.00 24.42 ? 456  TYR B CB  1 
ATOM   9436  C  CG  . TYR B  1 456 ? -20.986 53.870 40.535 1.00 24.13 ? 456  TYR B CG  1 
ATOM   9437  C  CD1 . TYR B  1 456 ? -20.478 53.981 39.240 1.00 24.74 ? 456  TYR B CD1 1 
ATOM   9438  C  CD2 . TYR B  1 456 ? -20.517 54.765 41.504 1.00 25.14 ? 456  TYR B CD2 1 
ATOM   9439  C  CE1 . TYR B  1 456 ? -19.513 54.957 38.913 1.00 24.54 ? 456  TYR B CE1 1 
ATOM   9440  C  CE2 . TYR B  1 456 ? -19.556 55.737 41.199 1.00 25.86 ? 456  TYR B CE2 1 
ATOM   9441  C  CZ  . TYR B  1 456 ? -19.055 55.826 39.903 1.00 26.67 ? 456  TYR B CZ  1 
ATOM   9442  O  OH  . TYR B  1 456 ? -18.080 56.756 39.619 1.00 26.03 ? 456  TYR B OH  1 
ATOM   9443  N  N   . TYR B  1 457 ? -24.293 53.375 38.211 1.00 22.71 ? 457  TYR B N   1 
ATOM   9444  C  CA  . TYR B  1 457 ? -24.631 53.071 36.834 1.00 22.90 ? 457  TYR B CA  1 
ATOM   9445  C  C   . TYR B  1 457 ? -23.975 53.966 35.792 1.00 22.06 ? 457  TYR B C   1 
ATOM   9446  O  O   . TYR B  1 457 ? -23.680 55.127 36.062 1.00 21.03 ? 457  TYR B O   1 
ATOM   9447  C  CB  . TYR B  1 457 ? -26.152 53.230 36.653 1.00 23.27 ? 457  TYR B CB  1 
ATOM   9448  C  CG  . TYR B  1 457 ? -27.021 52.158 37.257 1.00 24.10 ? 457  TYR B CG  1 
ATOM   9449  C  CD1 . TYR B  1 457 ? -27.363 51.024 36.516 1.00 22.43 ? 457  TYR B CD1 1 
ATOM   9450  C  CD2 . TYR B  1 457 ? -27.565 52.305 38.537 1.00 23.05 ? 457  TYR B CD2 1 
ATOM   9451  C  CE1 . TYR B  1 457 ? -28.242 50.063 37.027 1.00 23.82 ? 457  TYR B CE1 1 
ATOM   9452  C  CE2 . TYR B  1 457 ? -28.447 51.335 39.061 1.00 23.24 ? 457  TYR B CE2 1 
ATOM   9453  C  CZ  . TYR B  1 457 ? -28.784 50.225 38.295 1.00 23.79 ? 457  TYR B CZ  1 
ATOM   9454  O  OH  . TYR B  1 457 ? -29.693 49.287 38.753 1.00 25.57 ? 457  TYR B OH  1 
ATOM   9455  N  N   . SER B  1 458 ? -23.797 53.420 34.591 1.00 20.91 ? 458  SER B N   1 
ATOM   9456  C  CA  . SER B  1 458 ? -23.309 54.177 33.435 1.00 21.20 ? 458  SER B CA  1 
ATOM   9457  C  C   . SER B  1 458 ? -24.230 53.588 32.368 1.00 21.58 ? 458  SER B C   1 
ATOM   9458  O  O   . SER B  1 458 ? -24.810 52.520 32.574 1.00 23.13 ? 458  SER B O   1 
ATOM   9459  C  CB  . SER B  1 458 ? -21.830 53.916 33.124 1.00 19.17 ? 458  SER B CB  1 
ATOM   9460  O  OG  . SER B  1 458 ? -21.610 52.577 32.751 1.00 22.55 ? 458  SER B OG  1 
ATOM   9461  N  N   . VAL B  1 459 ? -24.372 54.255 31.234 1.00 21.03 ? 459  VAL B N   1 
ATOM   9462  C  CA  . VAL B  1 459 ? -25.302 53.789 30.231 1.00 21.24 ? 459  VAL B CA  1 
ATOM   9463  C  C   . VAL B  1 459 ? -24.769 53.884 28.805 1.00 22.19 ? 459  VAL B C   1 
ATOM   9464  O  O   . VAL B  1 459 ? -23.840 54.636 28.535 1.00 22.56 ? 459  VAL B O   1 
ATOM   9465  C  CB  . VAL B  1 459 ? -26.611 54.620 30.350 1.00 21.70 ? 459  VAL B CB  1 
ATOM   9466  C  CG1 . VAL B  1 459 ? -26.307 56.099 30.035 1.00 21.60 ? 459  VAL B CG1 1 
ATOM   9467  C  CG2 . VAL B  1 459 ? -27.694 54.070 29.438 1.00 20.19 ? 459  VAL B CG2 1 
ATOM   9468  N  N   . SER B  1 460 ? -25.376 53.117 27.901 1.00 23.30 ? 460  SER B N   1 
ATOM   9469  C  CA  . SER B  1 460 ? -25.005 53.112 26.485 1.00 23.07 ? 460  SER B CA  1 
ATOM   9470  C  C   . SER B  1 460 ? -26.259 53.045 25.586 1.00 22.05 ? 460  SER B C   1 
ATOM   9471  O  O   . SER B  1 460 ? -26.886 51.998 25.453 1.00 21.67 ? 460  SER B O   1 
ATOM   9472  C  CB  . SER B  1 460 ? -24.092 51.919 26.199 1.00 22.03 ? 460  SER B CB  1 
ATOM   9473  O  OG  . SER B  1 460 ? -23.660 51.943 24.856 1.00 22.73 ? 460  SER B OG  1 
ATOM   9474  N  N   . PHE B  1 461 ? -26.605 54.165 24.959 1.00 23.33 ? 461  PHE B N   1 
ATOM   9475  C  CA  . PHE B  1 461 ? -27.786 54.239 24.090 1.00 24.37 ? 461  PHE B CA  1 
ATOM   9476  C  C   . PHE B  1 461 ? -27.502 53.798 22.662 1.00 25.22 ? 461  PHE B C   1 
ATOM   9477  O  O   . PHE B  1 461 ? -26.376 53.933 22.179 1.00 26.20 ? 461  PHE B O   1 
ATOM   9478  C  CB  . PHE B  1 461 ? -28.350 55.666 24.061 1.00 22.59 ? 461  PHE B CB  1 
ATOM   9479  C  CG  . PHE B  1 461 ? -29.039 56.069 25.335 1.00 22.20 ? 461  PHE B CG  1 
ATOM   9480  C  CD1 . PHE B  1 461 ? -28.314 56.605 26.404 1.00 21.15 ? 461  PHE B CD1 1 
ATOM   9481  C  CD2 . PHE B  1 461 ? -30.426 55.926 25.466 1.00 21.34 ? 461  PHE B CD2 1 
ATOM   9482  C  CE1 . PHE B  1 461 ? -28.958 56.986 27.577 1.00 21.26 ? 461  PHE B CE1 1 
ATOM   9483  C  CE2 . PHE B  1 461 ? -31.078 56.308 26.641 1.00 20.19 ? 461  PHE B CE2 1 
ATOM   9484  C  CZ  . PHE B  1 461 ? -30.346 56.844 27.697 1.00 20.49 ? 461  PHE B CZ  1 
ATOM   9485  N  N   . SER B  1 462 ? -28.523 53.270 21.990 1.00 25.70 ? 462  SER B N   1 
ATOM   9486  C  CA  . SER B  1 462 ? -28.374 52.828 20.599 1.00 26.46 ? 462  SER B CA  1 
ATOM   9487  C  C   . SER B  1 462 ? -28.247 54.092 19.756 1.00 28.21 ? 462  SER B C   1 
ATOM   9488  O  O   . SER B  1 462 ? -28.314 55.193 20.286 1.00 27.28 ? 462  SER B O   1 
ATOM   9489  C  CB  . SER B  1 462 ? -29.592 52.017 20.157 1.00 25.02 ? 462  SER B CB  1 
ATOM   9490  O  OG  . SER B  1 462 ? -30.761 52.808 20.209 1.00 23.15 ? 462  SER B OG  1 
ATOM   9491  N  N   . LYS B  1 463 ? -28.095 53.947 18.446 1.00 31.03 ? 463  LYS B N   1 
ATOM   9492  C  CA  . LYS B  1 463 ? -27.920 55.115 17.589 1.00 34.37 ? 463  LYS B CA  1 
ATOM   9493  C  C   . LYS B  1 463 ? -28.924 56.249 17.752 1.00 35.32 ? 463  LYS B C   1 
ATOM   9494  O  O   . LYS B  1 463 ? -28.519 57.405 17.885 1.00 35.66 ? 463  LYS B O   1 
ATOM   9495  C  CB  . LYS B  1 463 ? -27.836 54.694 16.122 1.00 36.78 ? 463  LYS B CB  1 
ATOM   9496  C  CG  . LYS B  1 463 ? -26.509 54.014 15.791 1.00 40.55 ? 463  LYS B CG  1 
ATOM   9497  C  CD  . LYS B  1 463 ? -25.315 54.871 16.244 1.00 42.55 ? 463  LYS B CD  1 
ATOM   9498  C  CE  . LYS B  1 463 ? -23.992 54.141 16.006 1.00 45.35 ? 463  LYS B CE  1 
ATOM   9499  N  NZ  . LYS B  1 463 ? -22.780 54.929 16.396 1.00 45.76 ? 463  LYS B NZ  1 
ATOM   9500  N  N   . GLU B  1 464 ? -30.220 55.951 17.724 1.00 35.01 ? 464  GLU B N   1 
ATOM   9501  C  CA  . GLU B  1 464 ? -31.218 57.011 17.914 1.00 34.64 ? 464  GLU B CA  1 
ATOM   9502  C  C   . GLU B  1 464 ? -31.859 56.887 19.299 1.00 32.51 ? 464  GLU B C   1 
ATOM   9503  O  O   . GLU B  1 464 ? -33.015 57.260 19.498 1.00 30.13 ? 464  GLU B O   1 
ATOM   9504  C  CB  . GLU B  1 464 ? -32.308 56.952 16.833 1.00 38.16 ? 464  GLU B CB  1 
ATOM   9505  C  CG  . GLU B  1 464 ? -31.801 57.161 15.413 1.00 41.83 ? 464  GLU B CG  1 
ATOM   9506  C  CD  . GLU B  1 464 ? -31.054 58.462 15.276 1.00 44.73 ? 464  GLU B CD  1 
ATOM   9507  O  OE1 . GLU B  1 464 ? -31.624 59.505 15.686 1.00 47.16 ? 464  GLU B OE1 1 
ATOM   9508  O  OE2 . GLU B  1 464 ? -29.903 58.455 14.764 1.00 45.34 ? 464  GLU B OE2 1 
ATOM   9509  N  N   . ALA B  1 465 ? -31.103 56.333 20.245 1.00 30.83 ? 465  ALA B N   1 
ATOM   9510  C  CA  . ALA B  1 465 ? -31.580 56.196 21.616 1.00 29.85 ? 465  ALA B CA  1 
ATOM   9511  C  C   . ALA B  1 465 ? -32.846 55.348 21.746 1.00 29.38 ? 465  ALA B C   1 
ATOM   9512  O  O   . ALA B  1 465 ? -33.618 55.521 22.689 1.00 28.30 ? 465  ALA B O   1 
ATOM   9513  C  CB  . ALA B  1 465 ? -31.825 57.585 22.206 1.00 28.07 ? 465  ALA B CB  1 
ATOM   9514  N  N   . LYS B  1 466 ? -33.067 54.435 20.805 1.00 29.68 ? 466  LYS B N   1 
ATOM   9515  C  CA  . LYS B  1 466 ? -34.250 53.575 20.862 1.00 30.13 ? 466  LYS B CA  1 
ATOM   9516  C  C   . LYS B  1 466 ? -34.088 52.511 21.973 1.00 28.98 ? 466  LYS B C   1 
ATOM   9517  O  O   . LYS B  1 466 ? -35.072 52.028 22.538 1.00 28.75 ? 466  LYS B O   1 
ATOM   9518  C  CB  . LYS B  1 466 ? -34.483 52.897 19.498 1.00 31.66 ? 466  LYS B CB  1 
ATOM   9519  C  CG  . LYS B  1 466 ? -35.931 52.403 19.280 1.00 35.42 ? 466  LYS B CG  1 
ATOM   9520  C  CD  . LYS B  1 466 ? -36.097 51.525 18.023 1.00 37.01 ? 466  LYS B CD  1 
ATOM   9521  C  CE  . LYS B  1 466 ? -37.574 51.178 17.784 1.00 39.81 ? 466  LYS B CE  1 
ATOM   9522  N  NZ  . LYS B  1 466 ? -37.802 49.994 16.880 1.00 40.40 ? 466  LYS B NZ  1 
ATOM   9523  N  N   . TYR B  1 467 ? -32.844 52.157 22.284 1.00 26.61 ? 467  TYR B N   1 
ATOM   9524  C  CA  . TYR B  1 467 ? -32.560 51.163 23.323 1.00 25.40 ? 467  TYR B CA  1 
ATOM   9525  C  C   . TYR B  1 467 ? -31.367 51.626 24.134 1.00 23.80 ? 467  TYR B C   1 
ATOM   9526  O  O   . TYR B  1 467 ? -30.574 52.436 23.666 1.00 23.01 ? 467  TYR B O   1 
ATOM   9527  C  CB  . TYR B  1 467 ? -32.188 49.802 22.700 1.00 26.05 ? 467  TYR B CB  1 
ATOM   9528  C  CG  . TYR B  1 467 ? -33.278 49.176 21.865 1.00 27.29 ? 467  TYR B CG  1 
ATOM   9529  C  CD1 . TYR B  1 467 ? -34.376 48.555 22.467 1.00 27.10 ? 467  TYR B CD1 1 
ATOM   9530  C  CD2 . TYR B  1 467 ? -33.243 49.254 20.474 1.00 26.29 ? 467  TYR B CD2 1 
ATOM   9531  C  CE1 . TYR B  1 467 ? -35.421 48.035 21.700 1.00 27.29 ? 467  TYR B CE1 1 
ATOM   9532  C  CE2 . TYR B  1 467 ? -34.275 48.738 19.704 1.00 28.25 ? 467  TYR B CE2 1 
ATOM   9533  C  CZ  . TYR B  1 467 ? -35.361 48.138 20.317 1.00 27.63 ? 467  TYR B CZ  1 
ATOM   9534  O  OH  . TYR B  1 467 ? -36.403 47.681 19.549 1.00 29.06 ? 467  TYR B OH  1 
ATOM   9535  N  N   . TYR B  1 468 ? -31.244 51.122 25.352 1.00 23.02 ? 468  TYR B N   1 
ATOM   9536  C  CA  . TYR B  1 468 ? -30.080 51.442 26.150 1.00 22.84 ? 468  TYR B CA  1 
ATOM   9537  C  C   . TYR B  1 468 ? -29.671 50.291 27.052 1.00 22.94 ? 468  TYR B C   1 
ATOM   9538  O  O   . TYR B  1 468 ? -30.518 49.580 27.596 1.00 22.18 ? 468  TYR B O   1 
ATOM   9539  C  CB  . TYR B  1 468 ? -30.280 52.707 26.985 1.00 21.76 ? 468  TYR B CB  1 
ATOM   9540  C  CG  . TYR B  1 468 ? -31.464 52.683 27.914 1.00 22.27 ? 468  TYR B CG  1 
ATOM   9541  C  CD1 . TYR B  1 468 ? -32.725 53.054 27.465 1.00 21.83 ? 468  TYR B CD1 1 
ATOM   9542  C  CD2 . TYR B  1 468 ? -31.315 52.333 29.261 1.00 22.61 ? 468  TYR B CD2 1 
ATOM   9543  C  CE1 . TYR B  1 468 ? -33.813 53.091 28.319 1.00 22.53 ? 468  TYR B CE1 1 
ATOM   9544  C  CE2 . TYR B  1 468 ? -32.395 52.364 30.138 1.00 22.03 ? 468  TYR B CE2 1 
ATOM   9545  C  CZ  . TYR B  1 468 ? -33.645 52.750 29.661 1.00 23.73 ? 468  TYR B CZ  1 
ATOM   9546  O  OH  . TYR B  1 468 ? -34.720 52.826 30.518 1.00 21.76 ? 468  TYR B OH  1 
ATOM   9547  N  N   . GLN B  1 469 ? -28.354 50.117 27.172 1.00 23.11 ? 469  GLN B N   1 
ATOM   9548  C  CA  . GLN B  1 469 ? -27.742 49.096 28.023 1.00 22.30 ? 469  GLN B CA  1 
ATOM   9549  C  C   . GLN B  1 469 ? -27.331 49.773 29.327 1.00 22.59 ? 469  GLN B C   1 
ATOM   9550  O  O   . GLN B  1 469 ? -26.633 50.788 29.321 1.00 22.17 ? 469  GLN B O   1 
ATOM   9551  C  CB  . GLN B  1 469 ? -26.486 48.501 27.368 1.00 22.18 ? 469  GLN B CB  1 
ATOM   9552  C  CG  . GLN B  1 469 ? -25.690 47.598 28.324 1.00 22.45 ? 469  GLN B CG  1 
ATOM   9553  C  CD  . GLN B  1 469 ? -24.278 47.348 27.839 1.00 24.09 ? 469  GLN B CD  1 
ATOM   9554  O  OE1 . GLN B  1 469 ? -23.579 48.288 27.448 1.00 24.86 ? 469  GLN B OE1 1 
ATOM   9555  N  NE2 . GLN B  1 469 ? -23.843 46.087 27.868 1.00 22.02 ? 469  GLN B NE2 1 
ATOM   9556  N  N   . LEU B  1 470 ? -27.797 49.233 30.443 1.00 22.81 ? 470  LEU B N   1 
ATOM   9557  C  CA  . LEU B  1 470 ? -27.441 49.786 31.722 1.00 22.71 ? 470  LEU B CA  1 
ATOM   9558  C  C   . LEU B  1 470 ? -26.280 48.982 32.265 1.00 23.18 ? 470  LEU B C   1 
ATOM   9559  O  O   . LEU B  1 470 ? -26.245 47.761 32.140 1.00 22.04 ? 470  LEU B O   1 
ATOM   9560  C  CB  . LEU B  1 470 ? -28.617 49.748 32.693 1.00 21.88 ? 470  LEU B CB  1 
ATOM   9561  C  CG  . LEU B  1 470 ? -29.560 50.948 32.602 1.00 22.38 ? 470  LEU B CG  1 
ATOM   9562  C  CD1 . LEU B  1 470 ? -30.665 50.827 33.662 1.00 20.55 ? 470  LEU B CD1 1 
ATOM   9563  C  CD2 . LEU B  1 470 ? -28.772 52.218 32.818 1.00 21.01 ? 470  LEU B CD2 1 
ATOM   9564  N  N   . ARG B  1 471 ? -25.316 49.688 32.842 1.00 24.74 ? 471  ARG B N   1 
ATOM   9565  C  CA  . ARG B  1 471 ? -24.134 49.063 33.396 1.00 26.53 ? 471  ARG B CA  1 
ATOM   9566  C  C   . ARG B  1 471 ? -24.013 49.383 34.864 1.00 24.89 ? 471  ARG B C   1 
ATOM   9567  O  O   . ARG B  1 471 ? -23.676 50.502 35.250 1.00 23.89 ? 471  ARG B O   1 
ATOM   9568  C  CB  . ARG B  1 471 ? -22.892 49.545 32.646 1.00 30.45 ? 471  ARG B CB  1 
ATOM   9569  C  CG  . ARG B  1 471 ? -22.967 49.262 31.152 1.00 36.47 ? 471  ARG B CG  1 
ATOM   9570  C  CD  . ARG B  1 471 ? -21.750 49.766 30.384 1.00 41.93 ? 471  ARG B CD  1 
ATOM   9571  N  NE  . ARG B  1 471 ? -21.779 51.215 30.173 1.00 44.80 ? 471  ARG B NE  1 
ATOM   9572  C  CZ  . ARG B  1 471 ? -21.120 51.828 29.196 1.00 46.82 ? 471  ARG B CZ  1 
ATOM   9573  N  NH1 . ARG B  1 471 ? -20.390 51.116 28.347 1.00 48.26 ? 471  ARG B NH1 1 
ATOM   9574  N  NH2 . ARG B  1 471 ? -21.192 53.147 29.059 1.00 48.33 ? 471  ARG B NH2 1 
ATOM   9575  N  N   . CYS B  1 472 ? -24.318 48.386 35.679 1.00 23.32 ? 472  CYS B N   1 
ATOM   9576  C  CA  . CYS B  1 472 ? -24.244 48.501 37.133 1.00 25.15 ? 472  CYS B CA  1 
ATOM   9577  C  C   . CYS B  1 472 ? -22.843 48.021 37.545 1.00 23.90 ? 472  CYS B C   1 
ATOM   9578  O  O   . CYS B  1 472 ? -22.448 46.901 37.230 1.00 23.90 ? 472  CYS B O   1 
ATOM   9579  C  CB  . CYS B  1 472 ? -25.344 47.623 37.770 1.00 27.24 ? 472  CYS B CB  1 
ATOM   9580  S  SG  . CYS B  1 472 ? -25.070 47.090 39.488 1.00 32.08 ? 472  CYS B SG  1 
ATOM   9581  N  N   . SER B  1 473 ? -22.095 48.852 38.251 1.00 23.67 ? 473  SER B N   1 
ATOM   9582  C  CA  . SER B  1 473 ? -20.762 48.437 38.660 1.00 24.43 ? 473  SER B CA  1 
ATOM   9583  C  C   . SER B  1 473 ? -20.568 48.300 40.168 1.00 23.82 ? 473  SER B C   1 
ATOM   9584  O  O   . SER B  1 473 ? -19.442 48.101 40.629 1.00 23.76 ? 473  SER B O   1 
ATOM   9585  C  CB  . SER B  1 473 ? -19.717 49.405 38.091 1.00 25.27 ? 473  SER B CB  1 
ATOM   9586  O  OG  . SER B  1 473 ? -19.837 50.684 38.683 1.00 28.13 ? 473  SER B OG  1 
ATOM   9587  N  N   . GLY B  1 474 ? -21.657 48.401 40.930 1.00 22.91 ? 474  GLY B N   1 
ATOM   9588  C  CA  . GLY B  1 474 ? -21.561 48.287 42.378 1.00 22.33 ? 474  GLY B CA  1 
ATOM   9589  C  C   . GLY B  1 474 ? -22.814 48.750 43.112 1.00 22.90 ? 474  GLY B C   1 
ATOM   9590  O  O   . GLY B  1 474 ? -23.669 49.393 42.503 1.00 22.32 ? 474  GLY B O   1 
ATOM   9591  N  N   . PRO B  1 475 ? -22.901 48.552 44.447 1.00 23.10 ? 475  PRO B N   1 
ATOM   9592  C  CA  . PRO B  1 475 ? -21.900 47.901 45.309 1.00 22.68 ? 475  PRO B CA  1 
ATOM   9593  C  C   . PRO B  1 475 ? -21.756 46.390 45.183 1.00 23.60 ? 475  PRO B C   1 
ATOM   9594  O  O   . PRO B  1 475 ? -20.766 45.812 45.643 1.00 24.68 ? 475  PRO B O   1 
ATOM   9595  C  CB  . PRO B  1 475 ? -22.327 48.339 46.711 1.00 23.27 ? 475  PRO B CB  1 
ATOM   9596  C  CG  . PRO B  1 475 ? -23.821 48.379 46.600 1.00 22.39 ? 475  PRO B CG  1 
ATOM   9597  C  CD  . PRO B  1 475 ? -24.046 49.040 45.236 1.00 21.05 ? 475  PRO B CD  1 
ATOM   9598  N  N   . GLY B  1 476 ? -22.739 45.745 44.563 1.00 24.17 ? 476  GLY B N   1 
ATOM   9599  C  CA  . GLY B  1 476 ? -22.677 44.307 44.381 1.00 22.88 ? 476  GLY B CA  1 
ATOM   9600  C  C   . GLY B  1 476 ? -21.926 44.004 43.100 1.00 25.05 ? 476  GLY B C   1 
ATOM   9601  O  O   . GLY B  1 476 ? -21.316 44.909 42.508 1.00 24.79 ? 476  GLY B O   1 
ATOM   9602  N  N   . LEU B  1 477 ? -21.952 42.746 42.667 1.00 23.94 ? 477  LEU B N   1 
ATOM   9603  C  CA  . LEU B  1 477 ? -21.269 42.349 41.443 1.00 25.01 ? 477  LEU B CA  1 
ATOM   9604  C  C   . LEU B  1 477 ? -21.871 43.074 40.236 1.00 24.69 ? 477  LEU B C   1 
ATOM   9605  O  O   . LEU B  1 477 ? -23.089 43.271 40.152 1.00 24.97 ? 477  LEU B O   1 
ATOM   9606  C  CB  . LEU B  1 477 ? -21.384 40.830 41.233 1.00 25.78 ? 477  LEU B CB  1 
ATOM   9607  C  CG  . LEU B  1 477 ? -20.625 39.950 42.238 1.00 26.25 ? 477  LEU B CG  1 
ATOM   9608  C  CD1 . LEU B  1 477 ? -20.911 38.483 41.958 1.00 26.68 ? 477  LEU B CD1 1 
ATOM   9609  C  CD2 . LEU B  1 477 ? -19.142 40.222 42.122 1.00 27.29 ? 477  LEU B CD2 1 
ATOM   9610  N  N   . PRO B  1 478 ? -21.025 43.472 39.284 1.00 23.73 ? 478  PRO B N   1 
ATOM   9611  C  CA  . PRO B  1 478 ? -21.561 44.172 38.115 1.00 23.63 ? 478  PRO B CA  1 
ATOM   9612  C  C   . PRO B  1 478 ? -22.702 43.412 37.448 1.00 23.67 ? 478  PRO B C   1 
ATOM   9613  O  O   . PRO B  1 478 ? -22.715 42.173 37.392 1.00 24.77 ? 478  PRO B O   1 
ATOM   9614  C  CB  . PRO B  1 478 ? -20.327 44.346 37.226 1.00 23.64 ? 478  PRO B CB  1 
ATOM   9615  C  CG  . PRO B  1 478 ? -19.233 44.567 38.270 1.00 23.92 ? 478  PRO B CG  1 
ATOM   9616  C  CD  . PRO B  1 478 ? -19.552 43.464 39.275 1.00 23.17 ? 478  PRO B CD  1 
ATOM   9617  N  N   . LEU B  1 479 ? -23.670 44.175 36.956 1.00 23.33 ? 479  LEU B N   1 
ATOM   9618  C  CA  . LEU B  1 479 ? -24.853 43.625 36.299 1.00 22.24 ? 479  LEU B CA  1 
ATOM   9619  C  C   . LEU B  1 479 ? -25.120 44.439 35.036 1.00 21.86 ? 479  LEU B C   1 
ATOM   9620  O  O   . LEU B  1 479 ? -25.215 45.658 35.092 1.00 21.78 ? 479  LEU B O   1 
ATOM   9621  C  CB  . LEU B  1 479 ? -26.055 43.721 37.245 1.00 20.03 ? 479  LEU B CB  1 
ATOM   9622  C  CG  . LEU B  1 479 ? -27.407 43.278 36.696 1.00 20.73 ? 479  LEU B CG  1 
ATOM   9623  C  CD1 . LEU B  1 479 ? -27.339 41.839 36.202 1.00 19.13 ? 479  LEU B CD1 1 
ATOM   9624  C  CD2 . LEU B  1 479 ? -28.476 43.397 37.809 1.00 21.30 ? 479  LEU B CD2 1 
ATOM   9625  N  N   . TYR B  1 480 ? -25.239 43.763 33.903 1.00 22.23 ? 480  TYR B N   1 
ATOM   9626  C  CA  . TYR B  1 480 ? -25.486 44.448 32.643 1.00 23.01 ? 480  TYR B CA  1 
ATOM   9627  C  C   . TYR B  1 480 ? -26.869 44.097 32.115 1.00 23.28 ? 480  TYR B C   1 
ATOM   9628  O  O   . TYR B  1 480 ? -27.208 42.922 31.975 1.00 24.17 ? 480  TYR B O   1 
ATOM   9629  C  CB  . TYR B  1 480 ? -24.414 44.064 31.623 1.00 24.48 ? 480  TYR B CB  1 
ATOM   9630  C  CG  . TYR B  1 480 ? -23.014 44.405 32.068 1.00 25.38 ? 480  TYR B CG  1 
ATOM   9631  C  CD1 . TYR B  1 480 ? -22.345 43.625 33.021 1.00 25.53 ? 480  TYR B CD1 1 
ATOM   9632  C  CD2 . TYR B  1 480 ? -22.356 45.512 31.546 1.00 26.53 ? 480  TYR B CD2 1 
ATOM   9633  C  CE1 . TYR B  1 480 ? -21.052 43.944 33.441 1.00 26.19 ? 480  TYR B CE1 1 
ATOM   9634  C  CE2 . TYR B  1 480 ? -21.058 45.848 31.958 1.00 27.25 ? 480  TYR B CE2 1 
ATOM   9635  C  CZ  . TYR B  1 480 ? -20.418 45.065 32.901 1.00 27.76 ? 480  TYR B CZ  1 
ATOM   9636  O  OH  . TYR B  1 480 ? -19.160 45.422 33.319 1.00 29.99 ? 480  TYR B OH  1 
ATOM   9637  N  N   . THR B  1 481 ? -27.665 45.114 31.816 1.00 23.14 ? 481  THR B N   1 
ATOM   9638  C  CA  . THR B  1 481 ? -29.029 44.888 31.342 1.00 22.67 ? 481  THR B CA  1 
ATOM   9639  C  C   . THR B  1 481 ? -29.366 45.732 30.118 1.00 23.22 ? 481  THR B C   1 
ATOM   9640  O  O   . THR B  1 481 ? -28.758 46.786 29.897 1.00 22.62 ? 481  THR B O   1 
ATOM   9641  C  CB  . THR B  1 481 ? -30.032 45.215 32.476 1.00 23.04 ? 481  THR B CB  1 
ATOM   9642  O  OG1 . THR B  1 481 ? -29.765 46.535 32.991 1.00 21.61 ? 481  THR B OG1 1 
ATOM   9643  C  CG2 . THR B  1 481 ? -29.899 44.200 33.614 1.00 20.26 ? 481  THR B CG2 1 
ATOM   9644  N  N   . LEU B  1 482 ? -30.319 45.254 29.314 1.00 23.09 ? 482  LEU B N   1 
ATOM   9645  C  CA  . LEU B  1 482 ? -30.746 45.962 28.114 1.00 23.56 ? 482  LEU B CA  1 
ATOM   9646  C  C   . LEU B  1 482 ? -32.185 46.444 28.308 1.00 24.75 ? 482  LEU B C   1 
ATOM   9647  O  O   . LEU B  1 482 ? -33.031 45.735 28.870 1.00 25.06 ? 482  LEU B O   1 
ATOM   9648  C  CB  . LEU B  1 482 ? -30.655 45.052 26.889 1.00 22.58 ? 482  LEU B CB  1 
ATOM   9649  C  CG  . LEU B  1 482 ? -30.637 45.795 25.535 1.00 23.96 ? 482  LEU B CG  1 
ATOM   9650  C  CD1 . LEU B  1 482 ? -29.358 46.666 25.442 1.00 21.87 ? 482  LEU B CD1 1 
ATOM   9651  C  CD2 . LEU B  1 482 ? -30.694 44.777 24.374 1.00 21.37 ? 482  LEU B CD2 1 
ATOM   9652  N  N   . HIS B  1 483 ? -32.471 47.643 27.826 1.00 24.32 ? 483  HIS B N   1 
ATOM   9653  C  CA  . HIS B  1 483 ? -33.790 48.229 28.007 1.00 23.88 ? 483  HIS B CA  1 
ATOM   9654  C  C   . HIS B  1 483 ? -34.307 48.911 26.751 1.00 25.10 ? 483  HIS B C   1 
ATOM   9655  O  O   . HIS B  1 483 ? -33.538 49.376 25.898 1.00 24.89 ? 483  HIS B O   1 
ATOM   9656  C  CB  . HIS B  1 483 ? -33.735 49.251 29.150 1.00 23.87 ? 483  HIS B CB  1 
ATOM   9657  C  CG  . HIS B  1 483 ? -33.168 48.698 30.421 1.00 24.88 ? 483  HIS B CG  1 
ATOM   9658  N  ND1 . HIS B  1 483 ? -33.957 48.297 31.480 1.00 25.83 ? 483  HIS B ND1 1 
ATOM   9659  C  CD2 . HIS B  1 483 ? -31.893 48.422 30.780 1.00 25.81 ? 483  HIS B CD2 1 
ATOM   9660  C  CE1 . HIS B  1 483 ? -33.191 47.800 32.435 1.00 25.34 ? 483  HIS B CE1 1 
ATOM   9661  N  NE2 . HIS B  1 483 ? -31.935 47.864 32.038 1.00 26.42 ? 483  HIS B NE2 1 
ATOM   9662  N  N   . SER B  1 484 ? -35.628 48.986 26.658 1.00 24.41 ? 484  SER B N   1 
ATOM   9663  C  CA  . SER B  1 484 ? -36.299 49.607 25.533 1.00 25.48 ? 484  SER B CA  1 
ATOM   9664  C  C   . SER B  1 484 ? -36.695 51.033 25.925 1.00 24.71 ? 484  SER B C   1 
ATOM   9665  O  O   . SER B  1 484 ? -37.379 51.218 26.916 1.00 24.36 ? 484  SER B O   1 
ATOM   9666  C  CB  . SER B  1 484 ? -37.536 48.781 25.203 1.00 26.36 ? 484  SER B CB  1 
ATOM   9667  O  OG  . SER B  1 484 ? -38.353 49.478 24.285 1.00 33.14 ? 484  SER B OG  1 
ATOM   9668  N  N   . SER B  1 485 ? -36.266 52.036 25.159 1.00 24.57 ? 485  SER B N   1 
ATOM   9669  C  CA  . SER B  1 485 ? -36.595 53.434 25.475 1.00 24.89 ? 485  SER B CA  1 
ATOM   9670  C  C   . SER B  1 485 ? -38.085 53.825 25.305 1.00 24.11 ? 485  SER B C   1 
ATOM   9671  O  O   . SER B  1 485 ? -38.587 54.716 25.995 1.00 22.39 ? 485  SER B O   1 
ATOM   9672  C  CB  . SER B  1 485 ? -35.744 54.393 24.624 1.00 25.93 ? 485  SER B CB  1 
ATOM   9673  O  OG  . SER B  1 485 ? -34.356 54.313 24.942 1.00 28.93 ? 485  SER B OG  1 
ATOM   9674  N  N   . VAL B  1 486 ? -38.787 53.152 24.404 1.00 23.83 ? 486  VAL B N   1 
ATOM   9675  C  CA  . VAL B  1 486 ? -40.179 53.480 24.142 1.00 24.35 ? 486  VAL B CA  1 
ATOM   9676  C  C   . VAL B  1 486 ? -41.074 53.344 25.365 1.00 24.77 ? 486  VAL B C   1 
ATOM   9677  O  O   . VAL B  1 486 ? -42.016 54.117 25.536 1.00 25.22 ? 486  VAL B O   1 
ATOM   9678  C  CB  . VAL B  1 486 ? -40.751 52.619 22.969 1.00 24.59 ? 486  VAL B CB  1 
ATOM   9679  C  CG1 . VAL B  1 486 ? -41.048 51.212 23.425 1.00 24.82 ? 486  VAL B CG1 1 
ATOM   9680  C  CG2 . VAL B  1 486 ? -41.999 53.268 22.408 1.00 26.01 ? 486  VAL B CG2 1 
ATOM   9681  N  N   . ASN B  1 487 ? -40.761 52.388 26.235 1.00 25.42 ? 487  ASN B N   1 
ATOM   9682  C  CA  . ASN B  1 487 ? -41.558 52.152 27.441 1.00 25.76 ? 487  ASN B CA  1 
ATOM   9683  C  C   . ASN B  1 487 ? -40.720 51.948 28.711 1.00 25.89 ? 487  ASN B C   1 
ATOM   9684  O  O   . ASN B  1 487 ? -41.263 51.590 29.755 1.00 24.78 ? 487  ASN B O   1 
ATOM   9685  C  CB  . ASN B  1 487 ? -42.435 50.921 27.222 1.00 25.21 ? 487  ASN B CB  1 
ATOM   9686  C  CG  . ASN B  1 487 ? -41.630 49.701 26.787 1.00 27.65 ? 487  ASN B CG  1 
ATOM   9687  O  OD1 . ASN B  1 487 ? -42.204 48.685 26.371 1.00 29.81 ? 487  ASN B OD1 1 
ATOM   9688  N  ND2 . ASN B  1 487 ? -40.305 49.786 26.886 1.00 24.66 ? 487  ASN B ND2 1 
ATOM   9689  N  N   . ASP B  1 488 ? -39.410 52.176 28.612 1.00 25.37 ? 488  ASP B N   1 
ATOM   9690  C  CA  . ASP B  1 488 ? -38.493 51.991 29.733 1.00 25.34 ? 488  ASP B CA  1 
ATOM   9691  C  C   . ASP B  1 488 ? -38.620 50.612 30.397 1.00 26.08 ? 488  ASP B C   1 
ATOM   9692  O  O   . ASP B  1 488 ? -38.438 50.472 31.604 1.00 26.94 ? 488  ASP B O   1 
ATOM   9693  C  CB  . ASP B  1 488 ? -38.679 53.115 30.755 1.00 23.12 ? 488  ASP B CB  1 
ATOM   9694  C  CG  . ASP B  1 488 ? -38.223 54.469 30.215 1.00 26.06 ? 488  ASP B CG  1 
ATOM   9695  O  OD1 . ASP B  1 488 ? -39.000 55.447 30.297 1.00 25.10 ? 488  ASP B OD1 1 
ATOM   9696  O  OD2 . ASP B  1 488 ? -37.078 54.557 29.699 1.00 24.27 ? 488  ASP B OD2 1 
ATOM   9697  N  N   . LYS B  1 489 ? -38.920 49.587 29.600 1.00 26.45 ? 489  LYS B N   1 
ATOM   9698  C  CA  . LYS B  1 489 ? -39.054 48.225 30.128 1.00 26.66 ? 489  LYS B CA  1 
ATOM   9699  C  C   . LYS B  1 489 ? -37.764 47.446 29.916 1.00 26.61 ? 489  LYS B C   1 
ATOM   9700  O  O   . LYS B  1 489 ? -37.082 47.638 28.907 1.00 25.04 ? 489  LYS B O   1 
ATOM   9701  C  CB  . LYS B  1 489 ? -40.220 47.497 29.441 1.00 27.69 ? 489  LYS B CB  1 
ATOM   9702  C  CG  . LYS B  1 489 ? -41.600 48.098 29.771 1.00 30.56 ? 489  LYS B CG  1 
ATOM   9703  C  CD  . LYS B  1 489 ? -41.933 48.010 31.272 1.00 31.05 ? 489  LYS B CD  1 
ATOM   9704  C  CE  . LYS B  1 489 ? -42.205 49.396 31.867 1.00 33.03 ? 489  LYS B CE  1 
ATOM   9705  N  NZ  . LYS B  1 489 ? -42.523 49.329 33.330 1.00 36.53 ? 489  LYS B NZ  1 
ATOM   9706  N  N   . GLY B  1 490 ? -37.431 46.585 30.878 1.00 25.25 ? 490  GLY B N   1 
ATOM   9707  C  CA  . GLY B  1 490 ? -36.226 45.780 30.783 1.00 24.92 ? 490  GLY B CA  1 
ATOM   9708  C  C   . GLY B  1 490 ? -36.474 44.700 29.760 1.00 25.68 ? 490  GLY B C   1 
ATOM   9709  O  O   . GLY B  1 490 ? -37.539 44.098 29.780 1.00 25.20 ? 490  GLY B O   1 
ATOM   9710  N  N   . LEU B  1 491 ? -35.526 44.470 28.851 1.00 25.93 ? 491  LEU B N   1 
ATOM   9711  C  CA  . LEU B  1 491 ? -35.711 43.447 27.822 1.00 27.53 ? 491  LEU B CA  1 
ATOM   9712  C  C   . LEU B  1 491 ? -35.093 42.143 28.290 1.00 27.86 ? 491  LEU B C   1 
ATOM   9713  O  O   . LEU B  1 491 ? -35.592 41.055 27.974 1.00 28.84 ? 491  LEU B O   1 
ATOM   9714  C  CB  . LEU B  1 491 ? -35.069 43.883 26.495 1.00 27.25 ? 491  LEU B CB  1 
ATOM   9715  C  CG  . LEU B  1 491 ? -35.570 45.196 25.882 1.00 26.97 ? 491  LEU B CG  1 
ATOM   9716  C  CD1 . LEU B  1 491 ? -34.690 45.581 24.716 1.00 26.18 ? 491  LEU B CD1 1 
ATOM   9717  C  CD2 . LEU B  1 491 ? -37.010 45.040 25.432 1.00 27.25 ? 491  LEU B CD2 1 
ATOM   9718  N  N   . ARG B  1 492 ? -33.995 42.254 29.034 1.00 27.73 ? 492  ARG B N   1 
ATOM   9719  C  CA  . ARG B  1 492 ? -33.319 41.074 29.566 1.00 27.73 ? 492  ARG B CA  1 
ATOM   9720  C  C   . ARG B  1 492 ? -31.963 41.389 30.166 1.00 26.67 ? 492  ARG B C   1 
ATOM   9721  O  O   . ARG B  1 492 ? -31.425 42.483 30.005 1.00 25.07 ? 492  ARG B O   1 
ATOM   9722  C  CB  . ARG B  1 492 ? -33.138 40.016 28.473 1.00 29.04 ? 492  ARG B CB  1 
ATOM   9723  C  CG  . ARG B  1 492 ? -32.263 40.464 27.305 1.00 31.62 ? 492  ARG B CG  1 
ATOM   9724  C  CD  . ARG B  1 492 ? -32.392 39.520 26.105 1.00 32.95 ? 492  ARG B CD  1 
ATOM   9725  N  NE  . ARG B  1 492 ? -32.133 40.270 24.906 1.00 35.97 ? 492  ARG B NE  1 
ATOM   9726  C  CZ  . ARG B  1 492 ? -33.041 40.999 24.272 1.00 37.50 ? 492  ARG B CZ  1 
ATOM   9727  N  NH1 . ARG B  1 492 ? -34.290 41.049 24.703 1.00 38.31 ? 492  ARG B NH1 1 
ATOM   9728  N  NH2 . ARG B  1 492 ? -32.671 41.766 23.257 1.00 39.32 ? 492  ARG B NH2 1 
ATOM   9729  N  N   . VAL B  1 493 ? -31.429 40.393 30.860 1.00 26.08 ? 493  VAL B N   1 
ATOM   9730  C  CA  . VAL B  1 493 ? -30.141 40.465 31.504 1.00 25.34 ? 493  VAL B CA  1 
ATOM   9731  C  C   . VAL B  1 493 ? -29.114 40.040 30.470 1.00 26.34 ? 493  VAL B C   1 
ATOM   9732  O  O   . VAL B  1 493 ? -29.326 39.074 29.723 1.00 28.06 ? 493  VAL B O   1 
ATOM   9733  C  CB  . VAL B  1 493 ? -30.109 39.517 32.716 1.00 25.66 ? 493  VAL B CB  1 
ATOM   9734  C  CG1 . VAL B  1 493 ? -28.712 39.463 33.311 1.00 24.28 ? 493  VAL B CG1 1 
ATOM   9735  C  CG2 . VAL B  1 493 ? -31.133 40.002 33.764 1.00 22.59 ? 493  VAL B CG2 1 
ATOM   9736  N  N   . LEU B  1 494 ? -28.010 40.768 30.398 1.00 25.24 ? 494  LEU B N   1 
ATOM   9737  C  CA  . LEU B  1 494 ? -26.977 40.448 29.428 1.00 25.14 ? 494  LEU B CA  1 
ATOM   9738  C  C   . LEU B  1 494 ? -25.845 39.692 30.092 1.00 25.63 ? 494  LEU B C   1 
ATOM   9739  O  O   . LEU B  1 494 ? -25.257 38.790 29.493 1.00 26.90 ? 494  LEU B O   1 
ATOM   9740  C  CB  . LEU B  1 494 ? -26.460 41.731 28.773 1.00 24.85 ? 494  LEU B CB  1 
ATOM   9741  C  CG  . LEU B  1 494 ? -27.529 42.491 27.970 1.00 24.63 ? 494  LEU B CG  1 
ATOM   9742  C  CD1 . LEU B  1 494 ? -27.007 43.885 27.598 1.00 24.86 ? 494  LEU B CD1 1 
ATOM   9743  C  CD2 . LEU B  1 494 ? -27.901 41.693 26.723 1.00 24.00 ? 494  LEU B CD2 1 
ATOM   9744  N  N   . GLU B  1 495 ? -25.557 40.047 31.339 1.00 25.57 ? 495  GLU B N   1 
ATOM   9745  C  CA  . GLU B  1 495 ? -24.497 39.400 32.098 1.00 25.59 ? 495  GLU B CA  1 
ATOM   9746  C  C   . GLU B  1 495 ? -24.716 39.761 33.556 1.00 26.42 ? 495  GLU B C   1 
ATOM   9747  O  O   . GLU B  1 495 ? -24.779 40.950 33.915 1.00 26.41 ? 495  GLU B O   1 
ATOM   9748  C  CB  . GLU B  1 495 ? -23.125 39.894 31.626 1.00 26.26 ? 495  GLU B CB  1 
ATOM   9749  C  CG  . GLU B  1 495 ? -21.968 39.392 32.472 1.00 27.06 ? 495  GLU B CG  1 
ATOM   9750  C  CD  . GLU B  1 495 ? -21.825 37.872 32.410 1.00 29.33 ? 495  GLU B CD  1 
ATOM   9751  O  OE1 . GLU B  1 495 ? -21.548 37.357 31.305 1.00 28.44 ? 495  GLU B OE1 1 
ATOM   9752  O  OE2 . GLU B  1 495 ? -21.984 37.196 33.458 1.00 30.41 ? 495  GLU B OE2 1 
ATOM   9753  N  N   . ASP B  1 496 ? -24.848 38.736 34.393 1.00 26.47 ? 496  ASP B N   1 
ATOM   9754  C  CA  . ASP B  1 496 ? -25.083 38.943 35.818 1.00 27.48 ? 496  ASP B CA  1 
ATOM   9755  C  C   . ASP B  1 496 ? -23.930 38.498 36.711 1.00 27.21 ? 496  ASP B C   1 
ATOM   9756  O  O   . ASP B  1 496 ? -24.005 38.635 37.933 1.00 26.65 ? 496  ASP B O   1 
ATOM   9757  C  CB  . ASP B  1 496 ? -26.356 38.223 36.262 1.00 29.45 ? 496  ASP B CB  1 
ATOM   9758  C  CG  . ASP B  1 496 ? -26.288 36.716 36.032 1.00 31.72 ? 496  ASP B CG  1 
ATOM   9759  O  OD1 . ASP B  1 496 ? -25.180 36.190 35.777 1.00 32.12 ? 496  ASP B OD1 1 
ATOM   9760  O  OD2 . ASP B  1 496 ? -27.348 36.066 36.117 1.00 33.60 ? 496  ASP B OD2 1 
ATOM   9761  N  N   . ASN B  1 497 ? -22.870 37.972 36.108 1.00 27.11 ? 497  ASN B N   1 
ATOM   9762  C  CA  . ASN B  1 497 ? -21.716 37.534 36.885 1.00 27.82 ? 497  ASN B CA  1 
ATOM   9763  C  C   . ASN B  1 497 ? -22.028 36.423 37.883 1.00 28.53 ? 497  ASN B C   1 
ATOM   9764  O  O   . ASN B  1 497 ? -21.454 36.358 38.971 1.00 29.21 ? 497  ASN B O   1 
ATOM   9765  C  CB  . ASN B  1 497 ? -21.102 38.727 37.620 1.00 27.53 ? 497  ASN B CB  1 
ATOM   9766  C  CG  . ASN B  1 497 ? -20.055 39.427 36.795 1.00 28.27 ? 497  ASN B CG  1 
ATOM   9767  O  OD1 . ASN B  1 497 ? -19.001 38.859 36.509 1.00 29.93 ? 497  ASN B OD1 1 
ATOM   9768  N  ND2 . ASN B  1 497 ? -20.343 40.659 36.384 1.00 28.60 ? 497  ASN B ND2 1 
ATOM   9769  N  N   . SER B  1 498 ? -22.947 35.551 37.508 1.00 29.50 ? 498  SER B N   1 
ATOM   9770  C  CA  . SER B  1 498 ? -23.327 34.436 38.360 1.00 29.83 ? 498  SER B CA  1 
ATOM   9771  C  C   . SER B  1 498 ? -22.125 33.511 38.556 1.00 29.92 ? 498  SER B C   1 
ATOM   9772  O  O   . SER B  1 498 ? -21.918 32.979 39.647 1.00 31.15 ? 498  SER B O   1 
ATOM   9773  C  CB  . SER B  1 498 ? -24.481 33.668 37.722 1.00 28.77 ? 498  SER B CB  1 
ATOM   9774  O  OG  . SER B  1 498 ? -24.098 33.223 36.432 1.00 29.99 ? 498  SER B OG  1 
ATOM   9775  N  N   . ALA B  1 499 ? -21.324 33.332 37.512 1.00 29.79 ? 499  ALA B N   1 
ATOM   9776  C  CA  . ALA B  1 499 ? -20.142 32.470 37.609 1.00 30.48 ? 499  ALA B CA  1 
ATOM   9777  C  C   . ALA B  1 499 ? -19.217 32.948 38.722 1.00 30.88 ? 499  ALA B C   1 
ATOM   9778  O  O   . ALA B  1 499 ? -18.784 32.162 39.557 1.00 32.02 ? 499  ALA B O   1 
ATOM   9779  C  CB  . ALA B  1 499 ? -19.391 32.450 36.276 1.00 29.83 ? 499  ALA B CB  1 
ATOM   9780  N  N   . LEU B  1 500 ? -18.908 34.241 38.731 1.00 31.30 ? 500  LEU B N   1 
ATOM   9781  C  CA  . LEU B  1 500 ? -18.048 34.811 39.771 1.00 30.55 ? 500  LEU B CA  1 
ATOM   9782  C  C   . LEU B  1 500 ? -18.708 34.742 41.151 1.00 31.72 ? 500  LEU B C   1 
ATOM   9783  O  O   . LEU B  1 500 ? -18.047 34.470 42.151 1.00 31.97 ? 500  LEU B O   1 
ATOM   9784  C  CB  . LEU B  1 500 ? -17.727 36.272 39.449 1.00 29.19 ? 500  LEU B CB  1 
ATOM   9785  C  CG  . LEU B  1 500 ? -17.015 37.091 40.527 1.00 28.21 ? 500  LEU B CG  1 
ATOM   9786  C  CD1 . LEU B  1 500 ? -15.666 36.441 40.884 1.00 28.25 ? 500  LEU B CD1 1 
ATOM   9787  C  CD2 . LEU B  1 500 ? -16.817 38.518 40.023 1.00 28.19 ? 500  LEU B CD2 1 
ATOM   9788  N  N   . ASP B  1 501 ? -20.006 35.018 41.215 1.00 31.89 ? 501  ASP B N   1 
ATOM   9789  C  CA  . ASP B  1 501 ? -20.705 34.971 42.494 1.00 33.77 ? 501  ASP B CA  1 
ATOM   9790  C  C   . ASP B  1 501 ? -20.566 33.572 43.114 1.00 34.91 ? 501  ASP B C   1 
ATOM   9791  O  O   . ASP B  1 501 ? -20.414 33.415 44.322 1.00 34.11 ? 501  ASP B O   1 
ATOM   9792  C  CB  . ASP B  1 501 ? -22.186 35.289 42.295 1.00 35.73 ? 501  ASP B CB  1 
ATOM   9793  C  CG  . ASP B  1 501 ? -22.996 35.125 43.573 1.00 37.24 ? 501  ASP B CG  1 
ATOM   9794  O  OD1 . ASP B  1 501 ? -22.772 35.901 44.522 1.00 38.03 ? 501  ASP B OD1 1 
ATOM   9795  O  OD2 . ASP B  1 501 ? -23.851 34.215 43.627 1.00 39.78 ? 501  ASP B OD2 1 
ATOM   9796  N  N   . LYS B  1 502 ? -20.625 32.555 42.268 1.00 36.39 ? 502  LYS B N   1 
ATOM   9797  C  CA  . LYS B  1 502 ? -20.514 31.186 42.728 1.00 38.19 ? 502  LYS B CA  1 
ATOM   9798  C  C   . LYS B  1 502 ? -19.124 30.966 43.327 1.00 38.47 ? 502  LYS B C   1 
ATOM   9799  O  O   . LYS B  1 502 ? -18.993 30.394 44.411 1.00 37.93 ? 502  LYS B O   1 
ATOM   9800  C  CB  . LYS B  1 502 ? -20.736 30.225 41.559 1.00 40.28 ? 502  LYS B CB  1 
ATOM   9801  C  CG  . LYS B  1 502 ? -20.933 28.771 41.964 1.00 43.45 ? 502  LYS B CG  1 
ATOM   9802  C  CD  . LYS B  1 502 ? -20.699 27.829 40.777 1.00 46.74 ? 502  LYS B CD  1 
ATOM   9803  C  CE  . LYS B  1 502 ? -21.027 26.359 41.116 1.00 48.68 ? 502  LYS B CE  1 
ATOM   9804  N  NZ  . LYS B  1 502 ? -20.271 25.827 42.291 1.00 49.87 ? 502  LYS B NZ  1 
ATOM   9805  N  N   . MET B  1 503 ? -18.089 31.430 42.629 1.00 37.83 ? 503  MET B N   1 
ATOM   9806  C  CA  . MET B  1 503 ? -16.719 31.267 43.113 1.00 37.71 ? 503  MET B CA  1 
ATOM   9807  C  C   . MET B  1 503 ? -16.432 31.979 44.427 1.00 37.31 ? 503  MET B C   1 
ATOM   9808  O  O   . MET B  1 503 ? -15.799 31.409 45.314 1.00 37.08 ? 503  MET B O   1 
ATOM   9809  C  CB  . MET B  1 503 ? -15.723 31.744 42.064 1.00 38.85 ? 503  MET B CB  1 
ATOM   9810  C  CG  . MET B  1 503 ? -15.594 30.819 40.886 1.00 40.81 ? 503  MET B CG  1 
ATOM   9811  S  SD  . MET B  1 503 ? -14.398 31.460 39.701 1.00 47.86 ? 503  MET B SD  1 
ATOM   9812  C  CE  . MET B  1 503 ? -12.850 30.796 40.340 1.00 45.08 ? 503  MET B CE  1 
ATOM   9813  N  N   . LEU B  1 504 ? -16.902 33.217 44.551 1.00 37.08 ? 504  LEU B N   1 
ATOM   9814  C  CA  . LEU B  1 504 ? -16.686 34.012 45.759 1.00 37.24 ? 504  LEU B CA  1 
ATOM   9815  C  C   . LEU B  1 504 ? -17.350 33.457 47.016 1.00 38.90 ? 504  LEU B C   1 
ATOM   9816  O  O   . LEU B  1 504 ? -17.060 33.898 48.146 1.00 38.25 ? 504  LEU B O   1 
ATOM   9817  C  CB  . LEU B  1 504 ? -17.156 35.447 45.522 1.00 34.59 ? 504  LEU B CB  1 
ATOM   9818  C  CG  . LEU B  1 504 ? -16.288 36.197 44.510 1.00 33.39 ? 504  LEU B CG  1 
ATOM   9819  C  CD1 . LEU B  1 504 ? -16.704 37.629 44.462 1.00 30.92 ? 504  LEU B CD1 1 
ATOM   9820  C  CD2 . LEU B  1 504 ? -14.826 36.087 44.907 1.00 32.12 ? 504  LEU B CD2 1 
ATOM   9821  N  N   . GLN B  1 505 ? -18.250 32.498 46.816 1.00 40.27 ? 505  GLN B N   1 
ATOM   9822  C  CA  . GLN B  1 505 ? -18.958 31.863 47.924 1.00 41.74 ? 505  GLN B CA  1 
ATOM   9823  C  C   . GLN B  1 505 ? -17.952 31.147 48.830 1.00 41.29 ? 505  GLN B C   1 
ATOM   9824  O  O   . GLN B  1 505 ? -18.092 31.154 50.050 1.00 41.21 ? 505  GLN B O   1 
ATOM   9825  C  CB  . GLN B  1 505 ? -19.959 30.826 47.388 1.00 43.59 ? 505  GLN B CB  1 
ATOM   9826  C  CG  . GLN B  1 505 ? -20.923 31.331 46.316 1.00 46.17 ? 505  GLN B CG  1 
ATOM   9827  C  CD  . GLN B  1 505 ? -22.082 32.134 46.875 1.00 47.90 ? 505  GLN B CD  1 
ATOM   9828  O  OE1 . GLN B  1 505 ? -21.891 33.066 47.667 1.00 48.38 ? 505  GLN B OE1 1 
ATOM   9829  N  NE2 . GLN B  1 505 ? -23.302 31.783 46.453 1.00 48.96 ? 505  GLN B NE2 1 
ATOM   9830  N  N   . ASN B  1 506 ? -16.937 30.538 48.222 1.00 41.07 ? 506  ASN B N   1 
ATOM   9831  C  CA  . ASN B  1 506 ? -15.931 29.780 48.968 1.00 41.64 ? 506  ASN B CA  1 
ATOM   9832  C  C   . ASN B  1 506 ? -14.766 30.633 49.427 1.00 40.16 ? 506  ASN B C   1 
ATOM   9833  O  O   . ASN B  1 506 ? -13.717 30.104 49.798 1.00 39.92 ? 506  ASN B O   1 
ATOM   9834  C  CB  . ASN B  1 506 ? -15.383 28.640 48.106 1.00 43.90 ? 506  ASN B CB  1 
ATOM   9835  C  CG  . ASN B  1 506 ? -16.466 27.950 47.293 1.00 46.85 ? 506  ASN B CG  1 
ATOM   9836  O  OD1 . ASN B  1 506 ? -17.354 27.282 47.844 1.00 47.82 ? 506  ASN B OD1 1 
ATOM   9837  N  ND2 . ASN B  1 506 ? -16.405 28.119 45.968 1.00 47.61 ? 506  ASN B ND2 1 
ATOM   9838  N  N   . VAL B  1 507 ? -14.950 31.950 49.412 1.00 38.48 ? 507  VAL B N   1 
ATOM   9839  C  CA  . VAL B  1 507 ? -13.880 32.859 49.801 1.00 36.00 ? 507  VAL B CA  1 
ATOM   9840  C  C   . VAL B  1 507 ? -14.310 33.848 50.869 1.00 35.60 ? 507  VAL B C   1 
ATOM   9841  O  O   . VAL B  1 507 ? -15.406 34.416 50.809 1.00 34.79 ? 507  VAL B O   1 
ATOM   9842  C  CB  . VAL B  1 507 ? -13.361 33.664 48.574 1.00 35.98 ? 507  VAL B CB  1 
ATOM   9843  C  CG1 . VAL B  1 507 ? -12.152 34.523 48.977 1.00 34.88 ? 507  VAL B CG1 1 
ATOM   9844  C  CG2 . VAL B  1 507 ? -13.002 32.712 47.434 1.00 34.80 ? 507  VAL B CG2 1 
ATOM   9845  N  N   . GLN B  1 508 ? -13.433 34.057 51.845 1.00 34.62 ? 508  GLN B N   1 
ATOM   9846  C  CA  . GLN B  1 508 ? -13.707 35.000 52.915 1.00 34.37 ? 508  GLN B CA  1 
ATOM   9847  C  C   . GLN B  1 508 ? -13.477 36.420 52.407 1.00 33.71 ? 508  GLN B C   1 
ATOM   9848  O  O   . GLN B  1 508 ? -12.442 37.027 52.665 1.00 34.10 ? 508  GLN B O   1 
ATOM   9849  C  CB  . GLN B  1 508 ? -12.793 34.735 54.112 1.00 35.63 ? 508  GLN B CB  1 
ATOM   9850  C  CG  . GLN B  1 508 ? -13.059 33.428 54.823 1.00 37.00 ? 508  GLN B CG  1 
ATOM   9851  C  CD  . GLN B  1 508 ? -12.421 33.399 56.189 1.00 38.59 ? 508  GLN B CD  1 
ATOM   9852  O  OE1 . GLN B  1 508 ? -12.657 34.291 57.008 1.00 39.78 ? 508  GLN B OE1 1 
ATOM   9853  N  NE2 . GLN B  1 508 ? -11.603 32.380 56.449 1.00 38.72 ? 508  GLN B NE2 1 
ATOM   9854  N  N   . MET B  1 509 ? -14.450 36.952 51.682 1.00 32.71 ? 509  MET B N   1 
ATOM   9855  C  CA  . MET B  1 509 ? -14.336 38.293 51.140 1.00 31.25 ? 509  MET B CA  1 
ATOM   9856  C  C   . MET B  1 509 ? -14.509 39.372 52.208 1.00 31.06 ? 509  MET B C   1 
ATOM   9857  O  O   . MET B  1 509 ? -15.228 39.201 53.193 1.00 30.99 ? 509  MET B O   1 
ATOM   9858  C  CB  . MET B  1 509 ? -15.374 38.498 50.028 1.00 30.64 ? 509  MET B CB  1 
ATOM   9859  C  CG  . MET B  1 509 ? -15.175 37.611 48.816 1.00 30.43 ? 509  MET B CG  1 
ATOM   9860  S  SD  . MET B  1 509 ? -13.549 37.930 48.083 1.00 34.24 ? 509  MET B SD  1 
ATOM   9861  C  CE  . MET B  1 509 ? -13.906 39.428 47.190 1.00 32.82 ? 509  MET B CE  1 
ATOM   9862  N  N   . PRO B  1 510 ? -13.827 40.505 52.032 1.00 30.35 ? 510  PRO B N   1 
ATOM   9863  C  CA  . PRO B  1 510 ? -13.926 41.611 52.985 1.00 29.48 ? 510  PRO B CA  1 
ATOM   9864  C  C   . PRO B  1 510 ? -15.236 42.345 52.715 1.00 29.80 ? 510  PRO B C   1 
ATOM   9865  O  O   . PRO B  1 510 ? -15.853 42.142 51.675 1.00 28.90 ? 510  PRO B O   1 
ATOM   9866  C  CB  . PRO B  1 510 ? -12.719 42.470 52.628 1.00 29.61 ? 510  PRO B CB  1 
ATOM   9867  C  CG  . PRO B  1 510 ? -12.652 42.296 51.139 1.00 29.62 ? 510  PRO B CG  1 
ATOM   9868  C  CD  . PRO B  1 510 ? -12.846 40.805 50.974 1.00 29.74 ? 510  PRO B CD  1 
ATOM   9869  N  N   . SER B  1 511 ? -15.669 43.178 53.649 1.00 29.45 ? 511  SER B N   1 
ATOM   9870  C  CA  . SER B  1 511 ? -16.894 43.931 53.452 1.00 30.08 ? 511  SER B CA  1 
ATOM   9871  C  C   . SER B  1 511 ? -16.493 45.385 53.225 1.00 30.24 ? 511  SER B C   1 
ATOM   9872  O  O   . SER B  1 511 ? -15.375 45.791 53.554 1.00 28.57 ? 511  SER B O   1 
ATOM   9873  C  CB  . SER B  1 511 ? -17.797 43.829 54.678 1.00 29.80 ? 511  SER B CB  1 
ATOM   9874  O  OG  . SER B  1 511 ? -17.184 44.442 55.808 1.00 32.55 ? 511  SER B OG  1 
ATOM   9875  N  N   . LYS B  1 512 ? -17.399 46.168 52.654 1.00 31.14 ? 512  LYS B N   1 
ATOM   9876  C  CA  . LYS B  1 512 ? -17.110 47.571 52.399 1.00 31.53 ? 512  LYS B CA  1 
ATOM   9877  C  C   . LYS B  1 512 ? -18.143 48.472 53.049 1.00 31.76 ? 512  LYS B C   1 
ATOM   9878  O  O   . LYS B  1 512 ? -19.339 48.230 52.955 1.00 33.19 ? 512  LYS B O   1 
ATOM   9879  C  CB  . LYS B  1 512 ? -17.072 47.843 50.893 1.00 30.60 ? 512  LYS B CB  1 
ATOM   9880  C  CG  . LYS B  1 512 ? -16.895 49.321 50.545 1.00 30.66 ? 512  LYS B CG  1 
ATOM   9881  C  CD  . LYS B  1 512 ? -16.717 49.495 49.046 1.00 30.88 ? 512  LYS B CD  1 
ATOM   9882  C  CE  . LYS B  1 512 ? -16.579 50.942 48.672 1.00 30.98 ? 512  LYS B CE  1 
ATOM   9883  N  NZ  . LYS B  1 512 ? -16.361 51.083 47.214 1.00 31.46 ? 512  LYS B NZ  1 
ATOM   9884  N  N   . LYS B  1 513 ? -17.671 49.523 53.701 1.00 32.17 ? 513  LYS B N   1 
ATOM   9885  C  CA  . LYS B  1 513 ? -18.556 50.470 54.345 1.00 31.82 ? 513  LYS B CA  1 
ATOM   9886  C  C   . LYS B  1 513 ? -18.367 51.833 53.708 1.00 31.32 ? 513  LYS B C   1 
ATOM   9887  O  O   . LYS B  1 513 ? -17.240 52.269 53.511 1.00 31.50 ? 513  LYS B O   1 
ATOM   9888  C  CB  . LYS B  1 513 ? -18.238 50.571 55.836 1.00 33.30 ? 513  LYS B CB  1 
ATOM   9889  C  CG  . LYS B  1 513 ? -19.150 51.512 56.593 1.00 34.61 ? 513  LYS B CG  1 
ATOM   9890  C  CD  . LYS B  1 513 ? -18.672 51.676 58.020 1.00 37.80 ? 513  LYS B CD  1 
ATOM   9891  C  CE  . LYS B  1 513 ? -19.464 52.751 58.742 1.00 39.80 ? 513  LYS B CE  1 
ATOM   9892  N  NZ  . LYS B  1 513 ? -20.930 52.480 58.663 1.00 40.38 ? 513  LYS B NZ  1 
ATOM   9893  N  N   . LEU B  1 514 ? -19.475 52.490 53.378 1.00 30.48 ? 514  LEU B N   1 
ATOM   9894  C  CA  . LEU B  1 514 ? -19.474 53.821 52.789 1.00 29.16 ? 514  LEU B CA  1 
ATOM   9895  C  C   . LEU B  1 514 ? -20.326 54.660 53.745 1.00 29.80 ? 514  LEU B C   1 
ATOM   9896  O  O   . LEU B  1 514 ? -21.492 54.339 53.984 1.00 29.77 ? 514  LEU B O   1 
ATOM   9897  C  CB  . LEU B  1 514 ? -20.117 53.785 51.401 1.00 28.65 ? 514  LEU B CB  1 
ATOM   9898  C  CG  . LEU B  1 514 ? -20.379 55.157 50.767 1.00 29.22 ? 514  LEU B CG  1 
ATOM   9899  C  CD1 . LEU B  1 514 ? -19.047 55.856 50.516 1.00 29.01 ? 514  LEU B CD1 1 
ATOM   9900  C  CD2 . LEU B  1 514 ? -21.169 55.002 49.472 1.00 26.98 ? 514  LEU B CD2 1 
ATOM   9901  N  N   . ASP B  1 515 ? -19.746 55.725 54.289 1.00 29.35 ? 515  ASP B N   1 
ATOM   9902  C  CA  . ASP B  1 515 ? -20.446 56.572 55.247 1.00 29.80 ? 515  ASP B CA  1 
ATOM   9903  C  C   . ASP B  1 515 ? -19.765 57.940 55.278 1.00 30.42 ? 515  ASP B C   1 
ATOM   9904  O  O   . ASP B  1 515 ? -18.887 58.218 54.467 1.00 29.99 ? 515  ASP B O   1 
ATOM   9905  C  CB  . ASP B  1 515 ? -20.378 55.924 56.639 1.00 31.02 ? 515  ASP B CB  1 
ATOM   9906  C  CG  . ASP B  1 515 ? -21.492 56.393 57.577 1.00 32.20 ? 515  ASP B CG  1 
ATOM   9907  O  OD1 . ASP B  1 515 ? -21.490 55.963 58.755 1.00 34.70 ? 515  ASP B OD1 1 
ATOM   9908  O  OD2 . ASP B  1 515 ? -22.365 57.175 57.152 1.00 31.46 ? 515  ASP B OD2 1 
ATOM   9909  N  N   . PHE B  1 516 ? -20.149 58.786 56.225 1.00 30.65 ? 516  PHE B N   1 
ATOM   9910  C  CA  . PHE B  1 516 ? -19.557 60.112 56.311 1.00 31.61 ? 516  PHE B CA  1 
ATOM   9911  C  C   . PHE B  1 516 ? -19.357 60.564 57.740 1.00 32.36 ? 516  PHE B C   1 
ATOM   9912  O  O   . PHE B  1 516 ? -19.899 59.972 58.672 1.00 32.57 ? 516  PHE B O   1 
ATOM   9913  C  CB  . PHE B  1 516 ? -20.442 61.145 55.600 1.00 30.39 ? 516  PHE B CB  1 
ATOM   9914  C  CG  . PHE B  1 516 ? -21.827 61.282 56.199 1.00 31.39 ? 516  PHE B CG  1 
ATOM   9915  C  CD1 . PHE B  1 516 ? -22.879 60.493 55.745 1.00 31.40 ? 516  PHE B CD1 1 
ATOM   9916  C  CD2 . PHE B  1 516 ? -22.071 62.196 57.221 1.00 32.45 ? 516  PHE B CD2 1 
ATOM   9917  C  CE1 . PHE B  1 516 ? -24.162 60.608 56.299 1.00 31.45 ? 516  PHE B CE1 1 
ATOM   9918  C  CE2 . PHE B  1 516 ? -23.341 62.324 57.785 1.00 33.51 ? 516  PHE B CE2 1 
ATOM   9919  C  CZ  . PHE B  1 516 ? -24.392 61.524 57.322 1.00 32.75 ? 516  PHE B CZ  1 
ATOM   9920  N  N   . ILE B  1 517 ? -18.556 61.614 57.893 1.00 33.04 ? 517  ILE B N   1 
ATOM   9921  C  CA  . ILE B  1 517 ? -18.310 62.226 59.184 1.00 35.05 ? 517  ILE B CA  1 
ATOM   9922  C  C   . ILE B  1 517 ? -18.595 63.695 58.939 1.00 35.82 ? 517  ILE B C   1 
ATOM   9923  O  O   . ILE B  1 517 ? -18.469 64.172 57.814 1.00 35.58 ? 517  ILE B O   1 
ATOM   9924  C  CB  . ILE B  1 517 ? -16.857 62.087 59.656 1.00 34.83 ? 517  ILE B CB  1 
ATOM   9925  C  CG1 . ILE B  1 517 ? -15.922 62.757 58.659 1.00 35.68 ? 517  ILE B CG1 1 
ATOM   9926  C  CG2 . ILE B  1 517 ? -16.516 60.624 59.869 1.00 35.17 ? 517  ILE B CG2 1 
ATOM   9927  C  CD1 . ILE B  1 517 ? -14.530 62.966 59.197 1.00 36.78 ? 517  ILE B CD1 1 
ATOM   9928  N  N   . ILE B  1 518 ? -18.989 64.408 59.987 1.00 37.60 ? 518  ILE B N   1 
ATOM   9929  C  CA  . ILE B  1 518 ? -19.299 65.825 59.871 1.00 38.22 ? 518  ILE B CA  1 
ATOM   9930  C  C   . ILE B  1 518 ? -18.151 66.659 60.413 1.00 38.80 ? 518  ILE B C   1 
ATOM   9931  O  O   . ILE B  1 518 ? -17.760 66.506 61.561 1.00 39.74 ? 518  ILE B O   1 
ATOM   9932  C  CB  . ILE B  1 518 ? -20.598 66.165 60.650 1.00 38.42 ? 518  ILE B CB  1 
ATOM   9933  C  CG1 . ILE B  1 518 ? -21.776 65.410 60.036 1.00 38.90 ? 518  ILE B CG1 1 
ATOM   9934  C  CG2 . ILE B  1 518 ? -20.864 67.675 60.618 1.00 39.30 ? 518  ILE B CG2 1 
ATOM   9935  C  CD1 . ILE B  1 518 ? -23.113 65.617 60.758 1.00 39.47 ? 518  ILE B CD1 1 
ATOM   9936  N  N   . LEU B  1 519 ? -17.594 67.521 59.572 1.00 39.93 ? 519  LEU B N   1 
ATOM   9937  C  CA  . LEU B  1 519 ? -16.501 68.402 59.973 1.00 40.23 ? 519  LEU B CA  1 
ATOM   9938  C  C   . LEU B  1 519 ? -16.931 69.816 59.592 1.00 40.98 ? 519  LEU B C   1 
ATOM   9939  O  O   . LEU B  1 519 ? -17.245 70.077 58.430 1.00 40.29 ? 519  LEU B O   1 
ATOM   9940  C  CB  . LEU B  1 519 ? -15.215 68.036 59.232 1.00 41.19 ? 519  LEU B CB  1 
ATOM   9941  C  CG  . LEU B  1 519 ? -14.591 66.653 59.452 1.00 41.40 ? 519  LEU B CG  1 
ATOM   9942  C  CD1 . LEU B  1 519 ? -13.439 66.443 58.467 1.00 40.54 ? 519  LEU B CD1 1 
ATOM   9943  C  CD2 . LEU B  1 519 ? -14.096 66.539 60.885 1.00 42.18 ? 519  LEU B CD2 1 
ATOM   9944  N  N   . ASN B  1 520 ? -16.961 70.720 60.566 1.00 42.18 ? 520  ASN B N   1 
ATOM   9945  C  CA  . ASN B  1 520 ? -17.377 72.091 60.301 1.00 44.01 ? 520  ASN B CA  1 
ATOM   9946  C  C   . ASN B  1 520 ? -18.789 72.123 59.739 1.00 44.27 ? 520  ASN B C   1 
ATOM   9947  O  O   . ASN B  1 520 ? -19.105 72.935 58.871 1.00 44.16 ? 520  ASN B O   1 
ATOM   9948  C  CB  . ASN B  1 520 ? -16.431 72.746 59.309 1.00 46.20 ? 520  ASN B CB  1 
ATOM   9949  C  CG  . ASN B  1 520 ? -15.223 73.343 59.975 1.00 48.85 ? 520  ASN B CG  1 
ATOM   9950  O  OD1 . ASN B  1 520 ? -14.607 72.722 60.849 1.00 49.36 ? 520  ASN B OD1 1 
ATOM   9951  N  ND2 . ASN B  1 520 ? -14.860 74.560 59.562 1.00 51.04 ? 520  ASN B ND2 1 
ATOM   9952  N  N   . GLU B  1 521 ? -19.629 71.222 60.236 1.00 44.28 ? 521  GLU B N   1 
ATOM   9953  C  CA  . GLU B  1 521 ? -21.017 71.142 59.812 1.00 44.75 ? 521  GLU B CA  1 
ATOM   9954  C  C   . GLU B  1 521 ? -21.239 70.822 58.326 1.00 43.85 ? 521  GLU B C   1 
ATOM   9955  O  O   . GLU B  1 521 ? -22.262 71.179 57.732 1.00 43.73 ? 521  GLU B O   1 
ATOM   9956  C  CB  . GLU B  1 521 ? -21.754 72.427 60.209 1.00 46.65 ? 521  GLU B CB  1 
ATOM   9957  C  CG  . GLU B  1 521 ? -21.922 72.555 61.722 1.00 49.11 ? 521  GLU B CG  1 
ATOM   9958  C  CD  . GLU B  1 521 ? -22.823 73.704 62.137 1.00 51.20 ? 521  GLU B CD  1 
ATOM   9959  O  OE1 . GLU B  1 521 ? -23.186 73.763 63.340 1.00 51.92 ? 521  GLU B OE1 1 
ATOM   9960  O  OE2 . GLU B  1 521 ? -23.171 74.550 61.277 1.00 51.63 ? 521  GLU B OE2 1 
ATOM   9961  N  N   . THR B  1 522 ? -20.275 70.132 57.730 1.00 41.71 ? 522  THR B N   1 
ATOM   9962  C  CA  . THR B  1 522 ? -20.397 69.717 56.345 1.00 39.37 ? 522  THR B CA  1 
ATOM   9963  C  C   . THR B  1 522 ? -19.969 68.249 56.294 1.00 36.55 ? 522  THR B C   1 
ATOM   9964  O  O   . THR B  1 522 ? -19.060 67.838 57.006 1.00 35.76 ? 522  THR B O   1 
ATOM   9965  C  CB  . THR B  1 522 ? -19.563 70.635 55.412 1.00 39.83 ? 522  THR B CB  1 
ATOM   9966  O  OG1 . THR B  1 522 ? -18.949 69.855 54.384 1.00 42.31 ? 522  THR B OG1 1 
ATOM   9967  C  CG2 . THR B  1 522 ? -18.524 71.388 56.199 1.00 42.49 ? 522  THR B CG2 1 
ATOM   9968  N  N   . LYS B  1 523 ? -20.679 67.454 55.499 1.00 34.31 ? 523  LYS B N   1 
ATOM   9969  C  CA  . LYS B  1 523 ? -20.395 66.032 55.386 1.00 31.79 ? 523  LYS B CA  1 
ATOM   9970  C  C   . LYS B  1 523 ? -19.210 65.735 54.477 1.00 30.16 ? 523  LYS B C   1 
ATOM   9971  O  O   . LYS B  1 523 ? -19.076 66.317 53.398 1.00 30.16 ? 523  LYS B O   1 
ATOM   9972  C  CB  . LYS B  1 523 ? -21.609 65.278 54.834 1.00 33.25 ? 523  LYS B CB  1 
ATOM   9973  C  CG  . LYS B  1 523 ? -22.894 65.430 55.608 1.00 35.26 ? 523  LYS B CG  1 
ATOM   9974  C  CD  . LYS B  1 523 ? -24.044 64.778 54.836 1.00 37.20 ? 523  LYS B CD  1 
ATOM   9975  C  CE  . LYS B  1 523 ? -25.384 65.370 55.254 1.00 38.92 ? 523  LYS B CE  1 
ATOM   9976  N  NZ  . LYS B  1 523 ? -26.508 64.890 54.401 1.00 41.10 ? 523  LYS B NZ  1 
ATOM   9977  N  N   . PHE B  1 524 ? -18.363 64.822 54.927 1.00 27.47 ? 524  PHE B N   1 
ATOM   9978  C  CA  . PHE B  1 524 ? -17.206 64.380 54.173 1.00 26.05 ? 524  PHE B CA  1 
ATOM   9979  C  C   . PHE B  1 524 ? -17.252 62.862 54.174 1.00 25.59 ? 524  PHE B C   1 
ATOM   9980  O  O   . PHE B  1 524 ? -17.144 62.223 55.228 1.00 24.39 ? 524  PHE B O   1 
ATOM   9981  C  CB  . PHE B  1 524 ? -15.918 64.892 54.810 1.00 26.40 ? 524  PHE B CB  1 
ATOM   9982  C  CG  . PHE B  1 524 ? -15.679 66.360 54.575 1.00 27.17 ? 524  PHE B CG  1 
ATOM   9983  C  CD1 . PHE B  1 524 ? -15.849 67.285 55.607 1.00 26.96 ? 524  PHE B CD1 1 
ATOM   9984  C  CD2 . PHE B  1 524 ? -15.314 66.822 53.313 1.00 26.17 ? 524  PHE B CD2 1 
ATOM   9985  C  CE1 . PHE B  1 524 ? -15.661 68.644 55.386 1.00 26.56 ? 524  PHE B CE1 1 
ATOM   9986  C  CE2 . PHE B  1 524 ? -15.123 68.185 53.081 1.00 27.08 ? 524  PHE B CE2 1 
ATOM   9987  C  CZ  . PHE B  1 524 ? -15.298 69.100 54.125 1.00 27.44 ? 524  PHE B CZ  1 
ATOM   9988  N  N   . TRP B  1 525 ? -17.436 62.288 52.987 1.00 24.28 ? 525  TRP B N   1 
ATOM   9989  C  CA  . TRP B  1 525 ? -17.550 60.836 52.834 1.00 23.51 ? 525  TRP B CA  1 
ATOM   9990  C  C   . TRP B  1 525 ? -16.254 60.019 52.877 1.00 23.74 ? 525  TRP B C   1 
ATOM   9991  O  O   . TRP B  1 525 ? -15.177 60.501 52.536 1.00 22.92 ? 525  TRP B O   1 
ATOM   9992  C  CB  . TRP B  1 525 ? -18.303 60.534 51.537 1.00 24.01 ? 525  TRP B CB  1 
ATOM   9993  C  CG  . TRP B  1 525 ? -19.703 61.039 51.553 1.00 24.35 ? 525  TRP B CG  1 
ATOM   9994  C  CD1 . TRP B  1 525 ? -20.106 62.334 51.482 1.00 23.39 ? 525  TRP B CD1 1 
ATOM   9995  C  CD2 . TRP B  1 525 ? -20.887 60.253 51.739 1.00 24.91 ? 525  TRP B CD2 1 
ATOM   9996  N  NE1 . TRP B  1 525 ? -21.476 62.414 51.620 1.00 25.07 ? 525  TRP B NE1 1 
ATOM   9997  C  CE2 . TRP B  1 525 ? -21.980 61.149 51.778 1.00 25.69 ? 525  TRP B CE2 1 
ATOM   9998  C  CE3 . TRP B  1 525 ? -21.130 58.878 51.880 1.00 24.41 ? 525  TRP B CE3 1 
ATOM   9999  C  CZ2 . TRP B  1 525 ? -23.303 60.715 51.950 1.00 25.85 ? 525  TRP B CZ2 1 
ATOM   10000 C  CZ3 . TRP B  1 525 ? -22.442 58.442 52.050 1.00 24.37 ? 525  TRP B CZ3 1 
ATOM   10001 C  CH2 . TRP B  1 525 ? -23.513 59.359 52.082 1.00 25.38 ? 525  TRP B CH2 1 
ATOM   10002 N  N   . TYR B  1 526 ? -16.373 58.769 53.307 1.00 22.96 ? 526  TYR B N   1 
ATOM   10003 C  CA  . TYR B  1 526 ? -15.231 57.880 53.380 1.00 23.47 ? 526  TYR B CA  1 
ATOM   10004 C  C   . TYR B  1 526 ? -15.726 56.465 53.191 1.00 22.89 ? 526  TYR B C   1 
ATOM   10005 O  O   . TYR B  1 526 ? -16.918 56.196 53.313 1.00 22.92 ? 526  TYR B O   1 
ATOM   10006 C  CB  . TYR B  1 526 ? -14.526 57.998 54.742 1.00 24.52 ? 526  TYR B CB  1 
ATOM   10007 C  CG  . TYR B  1 526 ? -15.306 57.398 55.895 1.00 26.88 ? 526  TYR B CG  1 
ATOM   10008 C  CD1 . TYR B  1 526 ? -15.242 56.035 56.177 1.00 27.95 ? 526  TYR B CD1 1 
ATOM   10009 C  CD2 . TYR B  1 526 ? -16.135 58.194 56.685 1.00 28.66 ? 526  TYR B CD2 1 
ATOM   10010 C  CE1 . TYR B  1 526 ? -15.990 55.478 57.222 1.00 30.55 ? 526  TYR B CE1 1 
ATOM   10011 C  CE2 . TYR B  1 526 ? -16.884 57.657 57.725 1.00 29.12 ? 526  TYR B CE2 1 
ATOM   10012 C  CZ  . TYR B  1 526 ? -16.813 56.301 57.989 1.00 30.78 ? 526  TYR B CZ  1 
ATOM   10013 O  OH  . TYR B  1 526 ? -17.592 55.769 58.991 1.00 32.36 ? 526  TYR B OH  1 
ATOM   10014 N  N   . GLN B  1 527 ? -14.811 55.564 52.868 1.00 22.12 ? 527  GLN B N   1 
ATOM   10015 C  CA  . GLN B  1 527 ? -15.166 54.171 52.712 1.00 21.96 ? 527  GLN B CA  1 
ATOM   10016 C  C   . GLN B  1 527 ? -14.085 53.385 53.432 1.00 22.32 ? 527  GLN B C   1 
ATOM   10017 O  O   . GLN B  1 527 ? -12.973 53.887 53.612 1.00 22.05 ? 527  GLN B O   1 
ATOM   10018 C  CB  . GLN B  1 527 ? -15.253 53.768 51.229 1.00 20.51 ? 527  GLN B CB  1 
ATOM   10019 C  CG  . GLN B  1 527 ? -13.966 53.861 50.427 1.00 21.93 ? 527  GLN B CG  1 
ATOM   10020 C  CD  . GLN B  1 527 ? -14.111 53.261 49.022 1.00 22.88 ? 527  GLN B CD  1 
ATOM   10021 O  OE1 . GLN B  1 527 ? -15.102 53.516 48.324 1.00 22.32 ? 527  GLN B OE1 1 
ATOM   10022 N  NE2 . GLN B  1 527 ? -13.113 52.475 48.597 1.00 22.78 ? 527  GLN B NE2 1 
ATOM   10023 N  N   . MET B  1 528 ? -14.423 52.177 53.874 1.00 22.09 ? 528  MET B N   1 
ATOM   10024 C  CA  . MET B  1 528 ? -13.475 51.312 54.557 1.00 23.28 ? 528  MET B CA  1 
ATOM   10025 C  C   . MET B  1 528 ? -13.636 49.900 54.043 1.00 24.42 ? 528  MET B C   1 
ATOM   10026 O  O   . MET B  1 528 ? -14.755 49.399 53.983 1.00 26.23 ? 528  MET B O   1 
ATOM   10027 C  CB  . MET B  1 528 ? -13.724 51.284 56.072 1.00 23.75 ? 528  MET B CB  1 
ATOM   10028 C  CG  . MET B  1 528 ? -13.245 52.486 56.850 1.00 24.00 ? 528  MET B CG  1 
ATOM   10029 S  SD  . MET B  1 528 ? -13.500 52.236 58.650 1.00 26.91 ? 528  MET B SD  1 
ATOM   10030 C  CE  . MET B  1 528 ? -12.798 53.782 59.296 1.00 24.29 ? 528  MET B CE  1 
ATOM   10031 N  N   . ILE B  1 529 ? -12.536 49.262 53.647 1.00 24.68 ? 529  ILE B N   1 
ATOM   10032 C  CA  . ILE B  1 529 ? -12.593 47.873 53.205 1.00 23.68 ? 529  ILE B CA  1 
ATOM   10033 C  C   . ILE B  1 529 ? -12.284 47.144 54.503 1.00 25.80 ? 529  ILE B C   1 
ATOM   10034 O  O   . ILE B  1 529 ? -11.164 47.214 55.013 1.00 26.20 ? 529  ILE B O   1 
ATOM   10035 C  CB  . ILE B  1 529 ? -11.514 47.542 52.167 1.00 23.11 ? 529  ILE B CB  1 
ATOM   10036 C  CG1 . ILE B  1 529 ? -11.625 48.501 50.969 1.00 21.70 ? 529  ILE B CG1 1 
ATOM   10037 C  CG2 . ILE B  1 529 ? -11.645 46.084 51.723 1.00 21.76 ? 529  ILE B CG2 1 
ATOM   10038 C  CD1 . ILE B  1 529 ? -12.972 48.503 50.293 1.00 21.16 ? 529  ILE B CD1 1 
ATOM   10039 N  N   . LEU B  1 530 ? -13.292 46.465 55.044 1.00 26.84 ? 530  LEU B N   1 
ATOM   10040 C  CA  . LEU B  1 530 ? -13.178 45.754 56.317 1.00 27.56 ? 530  LEU B CA  1 
ATOM   10041 C  C   . LEU B  1 530 ? -12.873 44.263 56.191 1.00 27.97 ? 530  LEU B C   1 
ATOM   10042 O  O   . LEU B  1 530 ? -13.437 43.559 55.359 1.00 27.77 ? 530  LEU B O   1 
ATOM   10043 C  CB  . LEU B  1 530 ? -14.469 45.955 57.116 1.00 28.95 ? 530  LEU B CB  1 
ATOM   10044 C  CG  . LEU B  1 530 ? -14.882 47.407 57.422 1.00 30.41 ? 530  LEU B CG  1 
ATOM   10045 C  CD1 . LEU B  1 530 ? -16.342 47.467 57.909 1.00 29.51 ? 530  LEU B CD1 1 
ATOM   10046 C  CD2 . LEU B  1 530 ? -13.941 47.978 58.466 1.00 29.60 ? 530  LEU B CD2 1 
ATOM   10047 N  N   . PRO B  1 531 ? -11.949 43.765 57.014 1.00 28.46 ? 531  PRO B N   1 
ATOM   10048 C  CA  . PRO B  1 531 ? -11.591 42.347 56.975 1.00 29.40 ? 531  PRO B CA  1 
ATOM   10049 C  C   . PRO B  1 531 ? -12.809 41.463 57.247 1.00 30.92 ? 531  PRO B C   1 
ATOM   10050 O  O   . PRO B  1 531 ? -13.779 41.906 57.858 1.00 31.01 ? 531  PRO B O   1 
ATOM   10051 C  CB  . PRO B  1 531 ? -10.565 42.230 58.092 1.00 29.84 ? 531  PRO B CB  1 
ATOM   10052 C  CG  . PRO B  1 531 ? -9.867  43.568 58.025 1.00 29.85 ? 531  PRO B CG  1 
ATOM   10053 C  CD  . PRO B  1 531 ? -11.036 44.525 57.886 1.00 28.29 ? 531  PRO B CD  1 
ATOM   10054 N  N   . PRO B  1 532 ? -12.778 40.205 56.795 1.00 32.21 ? 532  PRO B N   1 
ATOM   10055 C  CA  . PRO B  1 532 ? -13.915 39.310 57.040 1.00 33.59 ? 532  PRO B CA  1 
ATOM   10056 C  C   . PRO B  1 532 ? -14.150 39.191 58.547 1.00 34.67 ? 532  PRO B C   1 
ATOM   10057 O  O   . PRO B  1 532 ? -13.231 39.402 59.338 1.00 33.22 ? 532  PRO B O   1 
ATOM   10058 C  CB  . PRO B  1 532 ? -13.445 37.990 56.454 1.00 33.53 ? 532  PRO B CB  1 
ATOM   10059 C  CG  . PRO B  1 532 ? -12.542 38.420 55.333 1.00 34.25 ? 532  PRO B CG  1 
ATOM   10060 C  CD  . PRO B  1 532 ? -11.758 39.551 55.960 1.00 33.14 ? 532  PRO B CD  1 
ATOM   10061 N  N   . HIS B  1 533 ? -15.378 38.867 58.947 1.00 36.09 ? 533  HIS B N   1 
ATOM   10062 C  CA  . HIS B  1 533 ? -15.680 38.696 60.374 1.00 36.85 ? 533  HIS B CA  1 
ATOM   10063 C  C   . HIS B  1 533 ? -15.156 39.856 61.189 1.00 37.68 ? 533  HIS B C   1 
ATOM   10064 O  O   . HIS B  1 533 ? -14.638 39.659 62.285 1.00 38.16 ? 533  HIS B O   1 
ATOM   10065 C  CB  . HIS B  1 533 ? -15.031 37.414 60.879 1.00 36.54 ? 533  HIS B CB  1 
ATOM   10066 C  CG  . HIS B  1 533 ? -15.368 36.217 60.046 1.00 38.76 ? 533  HIS B CG  1 
ATOM   10067 N  ND1 . HIS B  1 533 ? -14.413 35.338 59.582 1.00 38.97 ? 533  HIS B ND1 1 
ATOM   10068 C  CD2 . HIS B  1 533 ? -16.555 35.771 59.569 1.00 39.11 ? 533  HIS B CD2 1 
ATOM   10069 C  CE1 . HIS B  1 533 ? -14.996 34.400 58.854 1.00 38.76 ? 533  HIS B CE1 1 
ATOM   10070 N  NE2 . HIS B  1 533 ? -16.295 34.639 58.830 1.00 39.92 ? 533  HIS B NE2 1 
ATOM   10071 N  N   . PHE B  1 534 ? -15.280 41.063 60.650 1.00 37.88 ? 534  PHE B N   1 
ATOM   10072 C  CA  . PHE B  1 534 ? -14.811 42.256 61.341 1.00 38.88 ? 534  PHE B CA  1 
ATOM   10073 C  C   . PHE B  1 534 ? -15.377 42.342 62.757 1.00 40.23 ? 534  PHE B C   1 
ATOM   10074 O  O   . PHE B  1 534 ? -16.551 42.031 62.982 1.00 41.58 ? 534  PHE B O   1 
ATOM   10075 C  CB  . PHE B  1 534 ? -15.222 43.502 60.547 1.00 38.20 ? 534  PHE B CB  1 
ATOM   10076 C  CG  . PHE B  1 534 ? -14.821 44.802 61.196 1.00 38.04 ? 534  PHE B CG  1 
ATOM   10077 C  CD1 . PHE B  1 534 ? -13.479 45.139 61.338 1.00 37.54 ? 534  PHE B CD1 1 
ATOM   10078 C  CD2 . PHE B  1 534 ? -15.785 45.691 61.652 1.00 37.84 ? 534  PHE B CD2 1 
ATOM   10079 C  CE1 . PHE B  1 534 ? -13.102 46.341 61.917 1.00 37.61 ? 534  PHE B CE1 1 
ATOM   10080 C  CE2 . PHE B  1 534 ? -15.413 46.901 62.236 1.00 38.40 ? 534  PHE B CE2 1 
ATOM   10081 C  CZ  . PHE B  1 534 ? -14.064 47.225 62.369 1.00 37.41 ? 534  PHE B CZ  1 
ATOM   10082 N  N   . ASP B  1 535 ? -14.555 42.775 63.708 1.00 41.20 ? 535  ASP B N   1 
ATOM   10083 C  CA  . ASP B  1 535 ? -15.008 42.913 65.088 1.00 41.79 ? 535  ASP B CA  1 
ATOM   10084 C  C   . ASP B  1 535 ? -14.628 44.274 65.669 1.00 42.06 ? 535  ASP B C   1 
ATOM   10085 O  O   . ASP B  1 535 ? -13.459 44.527 65.977 1.00 41.65 ? 535  ASP B O   1 
ATOM   10086 C  CB  . ASP B  1 535 ? -14.424 41.804 65.951 1.00 42.31 ? 535  ASP B CB  1 
ATOM   10087 C  CG  . ASP B  1 535 ? -14.883 41.899 67.392 1.00 44.06 ? 535  ASP B CG  1 
ATOM   10088 O  OD1 . ASP B  1 535 ? -14.522 41.013 68.189 1.00 44.64 ? 535  ASP B OD1 1 
ATOM   10089 O  OD2 . ASP B  1 535 ? -15.604 42.867 67.725 1.00 44.48 ? 535  ASP B OD2 1 
ATOM   10090 N  N   . LYS B  1 536 ? -15.622 45.142 65.837 1.00 42.20 ? 536  LYS B N   1 
ATOM   10091 C  CA  . LYS B  1 536 ? -15.370 46.487 66.345 1.00 43.30 ? 536  LYS B CA  1 
ATOM   10092 C  C   . LYS B  1 536 ? -14.773 46.531 67.744 1.00 42.57 ? 536  LYS B C   1 
ATOM   10093 O  O   . LYS B  1 536 ? -14.469 47.611 68.256 1.00 41.56 ? 536  LYS B O   1 
ATOM   10094 C  CB  . LYS B  1 536 ? -16.655 47.337 66.292 1.00 45.81 ? 536  LYS B CB  1 
ATOM   10095 C  CG  . LYS B  1 536 ? -17.770 46.912 67.255 1.00 48.25 ? 536  LYS B CG  1 
ATOM   10096 C  CD  . LYS B  1 536 ? -19.088 47.647 66.955 1.00 50.19 ? 536  LYS B CD  1 
ATOM   10097 C  CE  . LYS B  1 536 ? -18.941 49.176 66.972 1.00 50.91 ? 536  LYS B CE  1 
ATOM   10098 N  NZ  . LYS B  1 536 ? -18.832 49.765 68.350 1.00 51.99 ? 536  LYS B NZ  1 
ATOM   10099 N  N   . SER B  1 537 ? -14.599 45.359 68.353 1.00 41.71 ? 537  SER B N   1 
ATOM   10100 C  CA  . SER B  1 537 ? -14.024 45.279 69.690 1.00 42.46 ? 537  SER B CA  1 
ATOM   10101 C  C   . SER B  1 537 ? -12.515 45.036 69.623 1.00 42.31 ? 537  SER B C   1 
ATOM   10102 O  O   . SER B  1 537 ? -11.856 44.931 70.656 1.00 42.53 ? 537  SER B O   1 
ATOM   10103 C  CB  . SER B  1 537 ? -14.664 44.142 70.492 1.00 42.19 ? 537  SER B CB  1 
ATOM   10104 O  OG  . SER B  1 537 ? -13.997 42.916 70.227 1.00 42.68 ? 537  SER B OG  1 
ATOM   10105 N  N   . LYS B  1 538 ? -11.976 44.910 68.412 1.00 42.23 ? 538  LYS B N   1 
ATOM   10106 C  CA  . LYS B  1 538 ? -10.540 44.703 68.242 1.00 40.72 ? 538  LYS B CA  1 
ATOM   10107 C  C   . LYS B  1 538 ? -9.867  45.930 67.655 1.00 39.22 ? 538  LYS B C   1 
ATOM   10108 O  O   . LYS B  1 538 ? -10.528 46.837 67.145 1.00 38.41 ? 538  LYS B O   1 
ATOM   10109 C  CB  . LYS B  1 538 ? -10.265 43.513 67.331 1.00 41.97 ? 538  LYS B CB  1 
ATOM   10110 C  CG  . LYS B  1 538 ? -10.762 42.190 67.878 1.00 44.82 ? 538  LYS B CG  1 
ATOM   10111 C  CD  . LYS B  1 538 ? -10.271 41.063 67.000 1.00 46.34 ? 538  LYS B CD  1 
ATOM   10112 C  CE  . LYS B  1 538 ? -10.978 39.755 67.308 1.00 47.82 ? 538  LYS B CE  1 
ATOM   10113 N  NZ  . LYS B  1 538 ? -10.446 38.665 66.429 1.00 49.18 ? 538  LYS B NZ  1 
ATOM   10114 N  N   . LYS B  1 539 ? -8.542  45.952 67.739 1.00 38.00 ? 539  LYS B N   1 
ATOM   10115 C  CA  . LYS B  1 539 ? -7.760  47.051 67.202 1.00 36.62 ? 539  LYS B CA  1 
ATOM   10116 C  C   . LYS B  1 539 ? -7.091  46.552 65.923 1.00 35.32 ? 539  LYS B C   1 
ATOM   10117 O  O   . LYS B  1 539 ? -6.204  45.701 65.969 1.00 35.56 ? 539  LYS B O   1 
ATOM   10118 C  CB  . LYS B  1 539 ? -6.701  47.483 68.219 1.00 37.78 ? 539  LYS B CB  1 
ATOM   10119 C  CG  . LYS B  1 539 ? -7.271  48.032 69.536 1.00 39.31 ? 539  LYS B CG  1 
ATOM   10120 C  CD  . LYS B  1 539 ? -7.915  49.397 69.332 1.00 40.83 ? 539  LYS B CD  1 
ATOM   10121 C  CE  . LYS B  1 539 ? -8.354  50.012 70.658 1.00 41.90 ? 539  LYS B CE  1 
ATOM   10122 N  NZ  . LYS B  1 539 ? -9.076  51.313 70.453 1.00 42.89 ? 539  LYS B NZ  1 
ATOM   10123 N  N   . TYR B  1 540 ? -7.513  47.079 64.778 1.00 32.96 ? 540  TYR B N   1 
ATOM   10124 C  CA  . TYR B  1 540 ? -6.944  46.656 63.500 1.00 30.25 ? 540  TYR B CA  1 
ATOM   10125 C  C   . TYR B  1 540 ? -5.939  47.652 62.941 1.00 28.79 ? 540  TYR B C   1 
ATOM   10126 O  O   . TYR B  1 540 ? -6.087  48.859 63.123 1.00 28.16 ? 540  TYR B O   1 
ATOM   10127 C  CB  . TYR B  1 540 ? -8.046  46.502 62.450 1.00 29.97 ? 540  TYR B CB  1 
ATOM   10128 C  CG  . TYR B  1 540 ? -9.003  45.375 62.688 1.00 30.86 ? 540  TYR B CG  1 
ATOM   10129 C  CD1 . TYR B  1 540 ? -8.830  44.145 62.060 1.00 31.13 ? 540  TYR B CD1 1 
ATOM   10130 C  CD2 . TYR B  1 540 ? -10.098 45.540 63.533 1.00 32.16 ? 540  TYR B CD2 1 
ATOM   10131 C  CE1 . TYR B  1 540 ? -9.735  43.093 62.263 1.00 32.29 ? 540  TYR B CE1 1 
ATOM   10132 C  CE2 . TYR B  1 540 ? -11.007 44.497 63.748 1.00 33.09 ? 540  TYR B CE2 1 
ATOM   10133 C  CZ  . TYR B  1 540 ? -10.824 43.283 63.113 1.00 32.36 ? 540  TYR B CZ  1 
ATOM   10134 O  OH  . TYR B  1 540 ? -11.737 42.274 63.317 1.00 33.32 ? 540  TYR B OH  1 
ATOM   10135 N  N   . PRO B  1 541 ? -4.880  47.163 62.273 1.00 27.08 ? 541  PRO B N   1 
ATOM   10136 C  CA  . PRO B  1 541 ? -3.958  48.162 61.725 1.00 26.65 ? 541  PRO B CA  1 
ATOM   10137 C  C   . PRO B  1 541 ? -4.719  48.817 60.563 1.00 25.63 ? 541  PRO B C   1 
ATOM   10138 O  O   . PRO B  1 541 ? -5.550  48.161 59.929 1.00 22.82 ? 541  PRO B O   1 
ATOM   10139 C  CB  . PRO B  1 541 ? -2.765  47.321 61.262 1.00 25.62 ? 541  PRO B CB  1 
ATOM   10140 C  CG  . PRO B  1 541 ? -3.360  45.985 60.987 1.00 25.40 ? 541  PRO B CG  1 
ATOM   10141 C  CD  . PRO B  1 541 ? -4.353  45.801 62.098 1.00 25.77 ? 541  PRO B CD  1 
ATOM   10142 N  N   . LEU B  1 542 ? -4.452  50.093 60.295 1.00 25.50 ? 542  LEU B N   1 
ATOM   10143 C  CA  . LEU B  1 542 ? -5.154  50.791 59.218 1.00 25.74 ? 542  LEU B CA  1 
ATOM   10144 C  C   . LEU B  1 542 ? -4.248  51.364 58.120 1.00 25.27 ? 542  LEU B C   1 
ATOM   10145 O  O   . LEU B  1 542 ? -3.201  51.954 58.414 1.00 25.50 ? 542  LEU B O   1 
ATOM   10146 C  CB  . LEU B  1 542 ? -6.004  51.919 59.810 1.00 26.75 ? 542  LEU B CB  1 
ATOM   10147 C  CG  . LEU B  1 542 ? -7.062  52.571 58.914 1.00 28.72 ? 542  LEU B CG  1 
ATOM   10148 C  CD1 . LEU B  1 542 ? -8.101  53.279 59.776 1.00 29.18 ? 542  LEU B CD1 1 
ATOM   10149 C  CD2 . LEU B  1 542 ? -6.415  53.553 57.971 1.00 29.41 ? 542  LEU B CD2 1 
ATOM   10150 N  N   . LEU B  1 543 ? -4.655  51.166 56.862 1.00 23.38 ? 543  LEU B N   1 
ATOM   10151 C  CA  . LEU B  1 543 ? -3.943  51.694 55.700 1.00 22.72 ? 543  LEU B CA  1 
ATOM   10152 C  C   . LEU B  1 543 ? -4.823  52.738 54.999 1.00 22.81 ? 543  LEU B C   1 
ATOM   10153 O  O   . LEU B  1 543 ? -5.915  52.431 54.513 1.00 23.38 ? 543  LEU B O   1 
ATOM   10154 C  CB  . LEU B  1 543 ? -3.582  50.580 54.701 1.00 22.79 ? 543  LEU B CB  1 
ATOM   10155 C  CG  . LEU B  1 543 ? -2.914  51.057 53.388 1.00 21.88 ? 543  LEU B CG  1 
ATOM   10156 C  CD1 . LEU B  1 543 ? -1.703  51.936 53.712 1.00 21.58 ? 543  LEU B CD1 1 
ATOM   10157 C  CD2 . LEU B  1 543 ? -2.489  49.859 52.535 1.00 20.86 ? 543  LEU B CD2 1 
ATOM   10158 N  N   . LEU B  1 544 ? -4.363  53.981 54.976 1.00 21.71 ? 544  LEU B N   1 
ATOM   10159 C  CA  . LEU B  1 544 ? -5.122  55.033 54.316 1.00 21.20 ? 544  LEU B CA  1 
ATOM   10160 C  C   . LEU B  1 544 ? -4.715  55.038 52.848 1.00 21.51 ? 544  LEU B C   1 
ATOM   10161 O  O   . LEU B  1 544 ? -3.556  55.312 52.522 1.00 20.97 ? 544  LEU B O   1 
ATOM   10162 C  CB  . LEU B  1 544 ? -4.812  56.387 54.948 1.00 21.60 ? 544  LEU B CB  1 
ATOM   10163 C  CG  . LEU B  1 544 ? -5.659  57.563 54.478 1.00 21.38 ? 544  LEU B CG  1 
ATOM   10164 C  CD1 . LEU B  1 544 ? -7.133  57.242 54.689 1.00 23.53 ? 544  LEU B CD1 1 
ATOM   10165 C  CD2 . LEU B  1 544 ? -5.274  58.816 55.250 1.00 22.75 ? 544  LEU B CD2 1 
ATOM   10166 N  N   . ASP B  1 545 ? -5.664  54.704 51.981 1.00 20.80 ? 545  ASP B N   1 
ATOM   10167 C  CA  . ASP B  1 545 ? -5.462  54.662 50.535 1.00 21.49 ? 545  ASP B CA  1 
ATOM   10168 C  C   . ASP B  1 545 ? -5.880  56.056 50.059 1.00 21.98 ? 545  ASP B C   1 
ATOM   10169 O  O   . ASP B  1 545 ? -7.059  56.420 50.115 1.00 21.84 ? 545  ASP B O   1 
ATOM   10170 C  CB  . ASP B  1 545 ? -6.361  53.575 49.938 1.00 23.02 ? 545  ASP B CB  1 
ATOM   10171 C  CG  . ASP B  1 545 ? -6.236  53.449 48.441 1.00 24.69 ? 545  ASP B CG  1 
ATOM   10172 O  OD1 . ASP B  1 545 ? -5.913  54.446 47.761 1.00 27.49 ? 545  ASP B OD1 1 
ATOM   10173 O  OD2 . ASP B  1 545 ? -6.488  52.341 47.928 1.00 27.09 ? 545  ASP B OD2 1 
ATOM   10174 N  N   . VAL B  1 546 ? -4.921  56.839 49.586 1.00 20.67 ? 546  VAL B N   1 
ATOM   10175 C  CA  . VAL B  1 546 ? -5.247  58.186 49.181 1.00 20.65 ? 546  VAL B CA  1 
ATOM   10176 C  C   . VAL B  1 546 ? -4.899  58.613 47.762 1.00 19.21 ? 546  VAL B C   1 
ATOM   10177 O  O   . VAL B  1 546 ? -3.971  58.104 47.148 1.00 19.48 ? 546  VAL B O   1 
ATOM   10178 C  CB  . VAL B  1 546 ? -4.617  59.185 50.188 1.00 22.86 ? 546  VAL B CB  1 
ATOM   10179 C  CG1 . VAL B  1 546 ? -3.161  58.838 50.388 1.00 25.34 ? 546  VAL B CG1 1 
ATOM   10180 C  CG2 . VAL B  1 546 ? -4.738  60.610 49.680 1.00 24.92 ? 546  VAL B CG2 1 
ATOM   10181 N  N   . TYR B  1 547 ? -5.706  59.527 47.233 1.00 18.99 ? 547  TYR B N   1 
ATOM   10182 C  CA  . TYR B  1 547 ? -5.466  60.115 45.918 1.00 19.51 ? 547  TYR B CA  1 
ATOM   10183 C  C   . TYR B  1 547 ? -5.625  61.604 46.203 1.00 18.53 ? 547  TYR B C   1 
ATOM   10184 O  O   . TYR B  1 547 ? -4.646  62.337 46.247 1.00 21.05 ? 547  TYR B O   1 
ATOM   10185 C  CB  . TYR B  1 547 ? -6.467  59.640 44.858 1.00 18.59 ? 547  TYR B CB  1 
ATOM   10186 C  CG  . TYR B  1 547 ? -6.099  60.230 43.531 1.00 18.62 ? 547  TYR B CG  1 
ATOM   10187 C  CD1 . TYR B  1 547 ? -6.797  61.319 43.021 1.00 17.39 ? 547  TYR B CD1 1 
ATOM   10188 C  CD2 . TYR B  1 547 ? -4.955  59.793 42.845 1.00 17.94 ? 547  TYR B CD2 1 
ATOM   10189 C  CE1 . TYR B  1 547 ? -6.377  61.962 41.885 1.00 17.21 ? 547  TYR B CE1 1 
ATOM   10190 C  CE2 . TYR B  1 547 ? -4.518  60.444 41.690 1.00 17.05 ? 547  TYR B CE2 1 
ATOM   10191 C  CZ  . TYR B  1 547 ? -5.244  61.535 41.222 1.00 18.11 ? 547  TYR B CZ  1 
ATOM   10192 O  OH  . TYR B  1 547 ? -4.836  62.233 40.109 1.00 16.33 ? 547  TYR B OH  1 
ATOM   10193 N  N   . ALA B  1 548 ? -6.864  62.041 46.396 1.00 18.05 ? 548  ALA B N   1 
ATOM   10194 C  CA  . ALA B  1 548 ? -7.159  63.412 46.792 1.00 16.21 ? 548  ALA B CA  1 
ATOM   10195 C  C   . ALA B  1 548 ? -6.814  64.598 45.889 1.00 17.18 ? 548  ALA B C   1 
ATOM   10196 O  O   . ALA B  1 548 ? -6.679  65.723 46.383 1.00 16.08 ? 548  ALA B O   1 
ATOM   10197 C  CB  . ALA B  1 548 ? -6.578  63.642 48.181 1.00 17.21 ? 548  ALA B CB  1 
ATOM   10198 N  N   . GLY B  1 549 ? -6.691  64.375 44.586 1.00 17.11 ? 549  GLY B N   1 
ATOM   10199 C  CA  . GLY B  1 549 ? -6.428  65.496 43.703 1.00 18.26 ? 549  GLY B CA  1 
ATOM   10200 C  C   . GLY B  1 549 ? -7.733  66.260 43.487 1.00 19.30 ? 549  GLY B C   1 
ATOM   10201 O  O   . GLY B  1 549 ? -8.793  65.815 43.922 1.00 19.81 ? 549  GLY B O   1 
ATOM   10202 N  N   . PRO B  1 550 ? -7.706  67.403 42.790 1.00 19.77 ? 550  PRO B N   1 
ATOM   10203 C  CA  . PRO B  1 550 ? -8.943  68.177 42.562 1.00 18.39 ? 550  PRO B CA  1 
ATOM   10204 C  C   . PRO B  1 550 ? -10.050 67.452 41.790 1.00 18.62 ? 550  PRO B C   1 
ATOM   10205 O  O   . PRO B  1 550 ? -9.821  66.900 40.719 1.00 18.16 ? 550  PRO B O   1 
ATOM   10206 C  CB  . PRO B  1 550 ? -8.444  69.421 41.843 1.00 19.48 ? 550  PRO B CB  1 
ATOM   10207 C  CG  . PRO B  1 550 ? -7.169  68.907 41.118 1.00 21.16 ? 550  PRO B CG  1 
ATOM   10208 C  CD  . PRO B  1 550 ? -6.535  68.044 42.158 1.00 19.52 ? 550  PRO B CD  1 
ATOM   10209 N  N   . CYS B  1 551 ? -11.255 67.483 42.358 1.00 18.34 ? 551  CYS B N   1 
ATOM   10210 C  CA  . CYS B  1 551 ? -12.428 66.824 41.814 1.00 19.46 ? 551  CYS B CA  1 
ATOM   10211 C  C   . CYS B  1 551 ? -12.322 65.310 41.859 1.00 19.79 ? 551  CYS B C   1 
ATOM   10212 O  O   . CYS B  1 551 ? -12.976 64.628 41.074 1.00 21.75 ? 551  CYS B O   1 
ATOM   10213 C  CB  . CYS B  1 551 ? -12.690 67.262 40.375 1.00 19.04 ? 551  CYS B CB  1 
ATOM   10214 S  SG  . CYS B  1 551 ? -14.430 66.986 39.841 1.00 21.98 ? 551  CYS B SG  1 
ATOM   10215 N  N   . SER B  1 552 ? -11.480 64.784 42.746 1.00 19.46 ? 552  SER B N   1 
ATOM   10216 C  CA  . SER B  1 552 ? -11.341 63.335 42.881 1.00 18.90 ? 552  SER B CA  1 
ATOM   10217 C  C   . SER B  1 552 ? -12.466 62.782 43.774 1.00 19.25 ? 552  SER B C   1 
ATOM   10218 O  O   . SER B  1 552 ? -13.173 63.534 44.468 1.00 19.78 ? 552  SER B O   1 
ATOM   10219 C  CB  . SER B  1 552 ? -9.978  62.964 43.507 1.00 20.09 ? 552  SER B CB  1 
ATOM   10220 O  OG  . SER B  1 552 ? -9.854  63.367 44.879 1.00 19.31 ? 552  SER B OG  1 
ATOM   10221 N  N   . GLN B  1 553 ? -12.631 61.468 43.735 1.00 18.56 ? 553  GLN B N   1 
ATOM   10222 C  CA  . GLN B  1 553 ? -13.618 60.784 44.545 1.00 18.82 ? 553  GLN B CA  1 
ATOM   10223 C  C   . GLN B  1 553 ? -13.104 59.386 44.826 1.00 18.87 ? 553  GLN B C   1 
ATOM   10224 O  O   . GLN B  1 553 ? -13.060 58.546 43.935 1.00 17.24 ? 553  GLN B O   1 
ATOM   10225 C  CB  . GLN B  1 553 ? -14.982 60.690 43.832 1.00 19.59 ? 553  GLN B CB  1 
ATOM   10226 C  CG  . GLN B  1 553 ? -16.079 60.071 44.700 1.00 19.78 ? 553  GLN B CG  1 
ATOM   10227 C  CD  . GLN B  1 553 ? -17.485 60.194 44.095 1.00 20.29 ? 553  GLN B CD  1 
ATOM   10228 O  OE1 . GLN B  1 553 ? -17.819 59.521 43.122 1.00 21.51 ? 553  GLN B OE1 1 
ATOM   10229 N  NE2 . GLN B  1 553 ? -18.304 61.054 44.682 1.00 17.80 ? 553  GLN B NE2 1 
ATOM   10230 N  N   . LYS B  1 554 ? -12.707 59.141 46.070 1.00 19.87 ? 554  LYS B N   1 
ATOM   10231 C  CA  . LYS B  1 554 ? -12.218 57.826 46.456 1.00 20.48 ? 554  LYS B CA  1 
ATOM   10232 C  C   . LYS B  1 554 ? -13.237 57.071 47.312 1.00 21.35 ? 554  LYS B C   1 
ATOM   10233 O  O   . LYS B  1 554 ? -13.023 55.913 47.667 1.00 22.02 ? 554  LYS B O   1 
ATOM   10234 C  CB  . LYS B  1 554 ? -10.879 57.966 47.184 1.00 19.69 ? 554  LYS B CB  1 
ATOM   10235 C  CG  . LYS B  1 554 ? -9.740  58.360 46.258 1.00 20.85 ? 554  LYS B CG  1 
ATOM   10236 C  CD  . LYS B  1 554 ? -9.204  57.146 45.477 1.00 20.00 ? 554  LYS B CD  1 
ATOM   10237 C  CE  . LYS B  1 554 ? -8.353  56.260 46.405 1.00 21.00 ? 554  LYS B CE  1 
ATOM   10238 N  NZ  . LYS B  1 554 ? -7.869  55.001 45.761 1.00 21.68 ? 554  LYS B NZ  1 
ATOM   10239 N  N   . ALA B  1 555 ? -14.349 57.721 47.643 1.00 22.13 ? 555  ALA B N   1 
ATOM   10240 C  CA  . ALA B  1 555 ? -15.389 57.055 48.428 1.00 22.22 ? 555  ALA B CA  1 
ATOM   10241 C  C   . ALA B  1 555 ? -16.602 56.885 47.523 1.00 21.79 ? 555  ALA B C   1 
ATOM   10242 O  O   . ALA B  1 555 ? -17.282 57.855 47.193 1.00 21.68 ? 555  ALA B O   1 
ATOM   10243 C  CB  . ALA B  1 555 ? -15.758 57.894 49.667 1.00 21.74 ? 555  ALA B CB  1 
ATOM   10244 N  N   . ASP B  1 556 ? -16.856 55.649 47.108 1.00 22.48 ? 556  ASP B N   1 
ATOM   10245 C  CA  . ASP B  1 556 ? -17.978 55.384 46.234 1.00 23.59 ? 556  ASP B CA  1 
ATOM   10246 C  C   . ASP B  1 556 ? -18.576 53.994 46.435 1.00 23.96 ? 556  ASP B C   1 
ATOM   10247 O  O   . ASP B  1 556 ? -18.134 53.232 47.300 1.00 25.18 ? 556  ASP B O   1 
ATOM   10248 C  CB  . ASP B  1 556 ? -17.586 55.586 44.759 1.00 24.55 ? 556  ASP B CB  1 
ATOM   10249 C  CG  . ASP B  1 556 ? -16.459 54.674 44.312 1.00 26.20 ? 556  ASP B CG  1 
ATOM   10250 O  OD1 . ASP B  1 556 ? -16.390 53.519 44.773 1.00 27.92 ? 556  ASP B OD1 1 
ATOM   10251 O  OD2 . ASP B  1 556 ? -15.648 55.104 43.462 1.00 28.88 ? 556  ASP B OD2 1 
ATOM   10252 N  N   . THR B  1 557 ? -19.567 53.672 45.614 1.00 21.95 ? 557  THR B N   1 
ATOM   10253 C  CA  . THR B  1 557 ? -20.279 52.408 45.702 1.00 22.68 ? 557  THR B CA  1 
ATOM   10254 C  C   . THR B  1 557 ? -19.847 51.410 44.629 1.00 23.77 ? 557  THR B C   1 
ATOM   10255 O  O   . THR B  1 557 ? -20.589 50.482 44.305 1.00 24.11 ? 557  THR B O   1 
ATOM   10256 C  CB  . THR B  1 557 ? -21.779 52.652 45.549 1.00 21.59 ? 557  THR B CB  1 
ATOM   10257 O  OG1 . THR B  1 557 ? -22.047 53.090 44.210 1.00 23.72 ? 557  THR B OG1 1 
ATOM   10258 C  CG2 . THR B  1 557 ? -22.253 53.746 46.510 1.00 20.87 ? 557  THR B CG2 1 
ATOM   10259 N  N   . VAL B  1 558 ? -18.651 51.585 44.077 1.00 23.80 ? 558  VAL B N   1 
ATOM   10260 C  CA  . VAL B  1 558 ? -18.192 50.674 43.040 1.00 24.21 ? 558  VAL B CA  1 
ATOM   10261 C  C   . VAL B  1 558 ? -17.605 49.403 43.658 1.00 26.21 ? 558  VAL B C   1 
ATOM   10262 O  O   . VAL B  1 558 ? -16.946 49.460 44.703 1.00 25.48 ? 558  VAL B O   1 
ATOM   10263 C  CB  . VAL B  1 558 ? -17.138 51.358 42.141 1.00 23.47 ? 558  VAL B CB  1 
ATOM   10264 C  CG1 . VAL B  1 558 ? -16.553 50.351 41.156 1.00 21.53 ? 558  VAL B CG1 1 
ATOM   10265 C  CG2 . VAL B  1 558 ? -17.780 52.530 41.397 1.00 21.57 ? 558  VAL B CG2 1 
ATOM   10266 N  N   . PHE B  1 559 ? -17.866 48.257 43.024 1.00 26.13 ? 559  PHE B N   1 
ATOM   10267 C  CA  . PHE B  1 559 ? -17.338 46.983 43.506 1.00 26.43 ? 559  PHE B CA  1 
ATOM   10268 C  C   . PHE B  1 559 ? -15.964 46.740 42.912 1.00 25.57 ? 559  PHE B C   1 
ATOM   10269 O  O   . PHE B  1 559 ? -15.820 46.690 41.701 1.00 25.38 ? 559  PHE B O   1 
ATOM   10270 C  CB  . PHE B  1 559 ? -18.237 45.820 43.091 1.00 26.77 ? 559  PHE B CB  1 
ATOM   10271 C  CG  . PHE B  1 559 ? -17.653 44.466 43.401 1.00 27.39 ? 559  PHE B CG  1 
ATOM   10272 C  CD1 . PHE B  1 559 ? -17.777 43.905 44.672 1.00 27.94 ? 559  PHE B CD1 1 
ATOM   10273 C  CD2 . PHE B  1 559 ? -17.000 43.734 42.412 1.00 29.03 ? 559  PHE B CD2 1 
ATOM   10274 C  CE1 . PHE B  1 559 ? -17.260 42.642 44.954 1.00 25.94 ? 559  PHE B CE1 1 
ATOM   10275 C  CE2 . PHE B  1 559 ? -16.478 42.460 42.685 1.00 27.86 ? 559  PHE B CE2 1 
ATOM   10276 C  CZ  . PHE B  1 559 ? -16.616 41.919 43.960 1.00 28.25 ? 559  PHE B CZ  1 
ATOM   10277 N  N   . ARG B  1 560 ? -14.962 46.550 43.758 1.00 26.05 ? 560  ARG B N   1 
ATOM   10278 C  CA  . ARG B  1 560 ? -13.626 46.306 43.243 1.00 25.73 ? 560  ARG B CA  1 
ATOM   10279 C  C   . ARG B  1 560 ? -12.925 45.091 43.843 1.00 26.10 ? 560  ARG B C   1 
ATOM   10280 O  O   . ARG B  1 560 ? -13.090 44.774 45.023 1.00 26.68 ? 560  ARG B O   1 
ATOM   10281 C  CB  . ARG B  1 560 ? -12.745 47.543 43.459 1.00 24.63 ? 560  ARG B CB  1 
ATOM   10282 C  CG  . ARG B  1 560 ? -13.239 48.801 42.755 1.00 25.44 ? 560  ARG B CG  1 
ATOM   10283 C  CD  . ARG B  1 560 ? -12.290 50.002 42.989 1.00 24.73 ? 560  ARG B CD  1 
ATOM   10284 N  NE  . ARG B  1 560 ? -12.789 51.206 42.327 1.00 24.51 ? 560  ARG B NE  1 
ATOM   10285 C  CZ  . ARG B  1 560 ? -13.620 52.089 42.876 1.00 25.60 ? 560  ARG B CZ  1 
ATOM   10286 N  NH1 . ARG B  1 560 ? -14.056 51.930 44.129 1.00 25.36 ? 560  ARG B NH1 1 
ATOM   10287 N  NH2 . ARG B  1 560 ? -14.049 53.115 42.156 1.00 24.00 ? 560  ARG B NH2 1 
ATOM   10288 N  N   . LEU B  1 561 ? -12.148 44.411 43.004 1.00 25.02 ? 561  LEU B N   1 
ATOM   10289 C  CA  . LEU B  1 561 ? -11.332 43.281 43.423 1.00 24.01 ? 561  LEU B CA  1 
ATOM   10290 C  C   . LEU B  1 561 ? -9.915  43.812 43.197 1.00 24.71 ? 561  LEU B C   1 
ATOM   10291 O  O   . LEU B  1 561 ? -9.417  43.832 42.068 1.00 24.61 ? 561  LEU B O   1 
ATOM   10292 C  CB  . LEU B  1 561 ? -11.587 42.068 42.537 1.00 22.80 ? 561  LEU B CB  1 
ATOM   10293 C  CG  . LEU B  1 561 ? -12.939 41.376 42.760 1.00 23.75 ? 561  LEU B CG  1 
ATOM   10294 C  CD1 . LEU B  1 561 ? -13.041 40.150 41.843 1.00 21.59 ? 561  LEU B CD1 1 
ATOM   10295 C  CD2 . LEU B  1 561 ? -13.080 40.987 44.220 1.00 21.63 ? 561  LEU B CD2 1 
ATOM   10296 N  N   . ASN B  1 562 ? -9.269  44.283 44.256 1.00 24.17 ? 562  ASN B N   1 
ATOM   10297 C  CA  . ASN B  1 562 ? -7.935  44.843 44.081 1.00 25.10 ? 562  ASN B CA  1 
ATOM   10298 C  C   . ASN B  1 562 ? -6.977  44.523 45.224 1.00 24.85 ? 562  ASN B C   1 
ATOM   10299 O  O   . ASN B  1 562 ? -7.216  43.605 46.010 1.00 26.16 ? 562  ASN B O   1 
ATOM   10300 C  CB  . ASN B  1 562 ? -8.039  46.369 43.874 1.00 24.28 ? 562  ASN B CB  1 
ATOM   10301 C  CG  . ASN B  1 562 ? -8.745  47.065 45.024 1.00 24.20 ? 562  ASN B CG  1 
ATOM   10302 O  OD1 . ASN B  1 562 ? -8.891  46.495 46.100 1.00 24.12 ? 562  ASN B OD1 1 
ATOM   10303 N  ND2 . ASN B  1 562 ? -9.166  48.305 44.807 1.00 22.83 ? 562  ASN B ND2 1 
ATOM   10304 N  N   . TRP B  1 563 ? -5.894  45.287 45.310 1.00 23.31 ? 563  TRP B N   1 
ATOM   10305 C  CA  . TRP B  1 563 ? -4.892  45.065 46.339 1.00 22.55 ? 563  TRP B CA  1 
ATOM   10306 C  C   . TRP B  1 563 ? -5.506  45.194 47.728 1.00 23.44 ? 563  TRP B C   1 
ATOM   10307 O  O   . TRP B  1 563 ? -5.192  44.410 48.623 1.00 24.47 ? 563  TRP B O   1 
ATOM   10308 C  CB  . TRP B  1 563 ? -3.729  46.049 46.168 1.00 18.98 ? 563  TRP B CB  1 
ATOM   10309 C  CG  . TRP B  1 563 ? -2.542  45.775 47.047 1.00 19.13 ? 563  TRP B CG  1 
ATOM   10310 C  CD1 . TRP B  1 563 ? -1.922  44.565 47.254 1.00 16.50 ? 563  TRP B CD1 1 
ATOM   10311 C  CD2 . TRP B  1 563 ? -1.775  46.747 47.781 1.00 17.98 ? 563  TRP B CD2 1 
ATOM   10312 N  NE1 . TRP B  1 563 ? -0.820  44.734 48.066 1.00 18.18 ? 563  TRP B NE1 1 
ATOM   10313 C  CE2 . TRP B  1 563 ? -0.709  46.056 48.407 1.00 15.78 ? 563  TRP B CE2 1 
ATOM   10314 C  CE3 . TRP B  1 563 ? -1.887  48.138 47.965 1.00 18.03 ? 563  TRP B CE3 1 
ATOM   10315 C  CZ2 . TRP B  1 563 ? 0.238   46.702 49.203 1.00 14.85 ? 563  TRP B CZ2 1 
ATOM   10316 C  CZ3 . TRP B  1 563 ? -0.942  48.791 48.760 1.00 16.77 ? 563  TRP B CZ3 1 
ATOM   10317 C  CH2 . TRP B  1 563 ? 0.115   48.061 49.374 1.00 16.64 ? 563  TRP B CH2 1 
ATOM   10318 N  N   . ALA B  1 564 ? -6.373  46.184 47.906 1.00 23.14 ? 564  ALA B N   1 
ATOM   10319 C  CA  . ALA B  1 564 ? -7.024  46.396 49.191 1.00 23.56 ? 564  ALA B CA  1 
ATOM   10320 C  C   . ALA B  1 564 ? -7.843  45.159 49.594 1.00 22.85 ? 564  ALA B C   1 
ATOM   10321 O  O   . ALA B  1 564 ? -7.944  44.842 50.774 1.00 22.30 ? 564  ALA B O   1 
ATOM   10322 C  CB  . ALA B  1 564 ? -7.931  47.642 49.135 1.00 21.26 ? 564  ALA B CB  1 
ATOM   10323 N  N   . THR B  1 565 ? -8.415  44.463 48.614 1.00 23.34 ? 565  THR B N   1 
ATOM   10324 C  CA  . THR B  1 565 ? -9.214  43.268 48.909 1.00 24.53 ? 565  THR B CA  1 
ATOM   10325 C  C   . THR B  1 565 ? -8.347  42.220 49.604 1.00 24.66 ? 565  THR B C   1 
ATOM   10326 O  O   . THR B  1 565 ? -8.731  41.661 50.633 1.00 23.82 ? 565  THR B O   1 
ATOM   10327 C  CB  . THR B  1 565 ? -9.790  42.645 47.640 1.00 24.42 ? 565  THR B CB  1 
ATOM   10328 O  OG1 . THR B  1 565 ? -10.439 43.663 46.871 1.00 24.11 ? 565  THR B OG1 1 
ATOM   10329 C  CG2 . THR B  1 565 ? -10.795 41.550 48.007 1.00 23.78 ? 565  THR B CG2 1 
ATOM   10330 N  N   . TYR B  1 566 ? -7.180  41.960 49.027 1.00 24.73 ? 566  TYR B N   1 
ATOM   10331 C  CA  . TYR B  1 566 ? -6.230  41.018 49.597 1.00 24.52 ? 566  TYR B CA  1 
ATOM   10332 C  C   . TYR B  1 566 ? -5.779  41.492 50.983 1.00 25.23 ? 566  TYR B C   1 
ATOM   10333 O  O   . TYR B  1 566 ? -5.798  40.721 51.948 1.00 25.76 ? 566  TYR B O   1 
ATOM   10334 C  CB  . TYR B  1 566 ? -5.026  40.876 48.661 1.00 24.31 ? 566  TYR B CB  1 
ATOM   10335 C  CG  . TYR B  1 566 ? -3.698  40.681 49.359 1.00 23.75 ? 566  TYR B CG  1 
ATOM   10336 C  CD1 . TYR B  1 566 ? -3.408  39.497 50.033 1.00 25.16 ? 566  TYR B CD1 1 
ATOM   10337 C  CD2 . TYR B  1 566 ? -2.741  41.699 49.368 1.00 24.13 ? 566  TYR B CD2 1 
ATOM   10338 C  CE1 . TYR B  1 566 ? -2.187  39.326 50.709 1.00 25.58 ? 566  TYR B CE1 1 
ATOM   10339 C  CE2 . TYR B  1 566 ? -1.518  41.547 50.040 1.00 25.57 ? 566  TYR B CE2 1 
ATOM   10340 C  CZ  . TYR B  1 566 ? -1.256  40.347 50.715 1.00 26.13 ? 566  TYR B CZ  1 
ATOM   10341 O  OH  . TYR B  1 566 ? -0.088  40.190 51.418 1.00 27.06 ? 566  TYR B OH  1 
ATOM   10342 N  N   . LEU B  1 567 ? -5.390  42.759 51.094 1.00 24.77 ? 567  LEU B N   1 
ATOM   10343 C  CA  . LEU B  1 567 ? -4.922  43.286 52.375 1.00 25.05 ? 567  LEU B CA  1 
ATOM   10344 C  C   . LEU B  1 567 ? -5.949  43.110 53.489 1.00 25.71 ? 567  LEU B C   1 
ATOM   10345 O  O   . LEU B  1 567 ? -5.587  42.783 54.622 1.00 25.38 ? 567  LEU B O   1 
ATOM   10346 C  CB  . LEU B  1 567 ? -4.555  44.765 52.247 1.00 24.40 ? 567  LEU B CB  1 
ATOM   10347 C  CG  . LEU B  1 567 ? -3.361  45.129 51.354 1.00 24.23 ? 567  LEU B CG  1 
ATOM   10348 C  CD1 . LEU B  1 567 ? -3.243  46.630 51.318 1.00 22.59 ? 567  LEU B CD1 1 
ATOM   10349 C  CD2 . LEU B  1 567 ? -2.066  44.510 51.890 1.00 23.15 ? 567  LEU B CD2 1 
ATOM   10350 N  N   . ALA B  1 568 ? -7.225  43.332 53.182 1.00 25.84 ? 568  ALA B N   1 
ATOM   10351 C  CA  . ALA B  1 568 ? -8.267  43.174 54.203 1.00 26.36 ? 568  ALA B CA  1 
ATOM   10352 C  C   . ALA B  1 568 ? -8.591  41.690 54.423 1.00 26.67 ? 568  ALA B C   1 
ATOM   10353 O  O   . ALA B  1 568 ? -8.585  41.206 55.550 1.00 26.63 ? 568  ALA B O   1 
ATOM   10354 C  CB  . ALA B  1 568 ? -9.523  43.929 53.797 1.00 25.33 ? 568  ALA B CB  1 
ATOM   10355 N  N   . SER B  1 569 ? -8.831  40.967 53.337 1.00 26.96 ? 569  SER B N   1 
ATOM   10356 C  CA  . SER B  1 569 ? -9.175  39.557 53.428 1.00 28.31 ? 569  SER B CA  1 
ATOM   10357 C  C   . SER B  1 569 ? -8.116  38.632 54.033 1.00 29.51 ? 569  SER B C   1 
ATOM   10358 O  O   . SER B  1 569 ? -8.401  37.851 54.948 1.00 29.50 ? 569  SER B O   1 
ATOM   10359 C  CB  . SER B  1 569 ? -9.569  39.039 52.049 1.00 27.70 ? 569  SER B CB  1 
ATOM   10360 O  OG  . SER B  1 569 ? -9.844  37.655 52.081 1.00 28.46 ? 569  SER B OG  1 
ATOM   10361 N  N   . THR B  1 570 ? -6.896  38.710 53.513 1.00 29.68 ? 570  THR B N   1 
ATOM   10362 C  CA  . THR B  1 570 ? -5.812  37.857 53.984 1.00 28.99 ? 570  THR B CA  1 
ATOM   10363 C  C   . THR B  1 570 ? -5.027  38.436 55.160 1.00 29.54 ? 570  THR B C   1 
ATOM   10364 O  O   . THR B  1 570 ? -4.804  37.741 56.143 1.00 30.76 ? 570  THR B O   1 
ATOM   10365 C  CB  . THR B  1 570 ? -4.857  37.542 52.819 1.00 27.89 ? 570  THR B CB  1 
ATOM   10366 O  OG1 . THR B  1 570 ? -5.602  36.893 51.787 1.00 27.94 ? 570  THR B OG1 1 
ATOM   10367 C  CG2 . THR B  1 570 ? -3.715  36.640 53.260 1.00 27.89 ? 570  THR B CG2 1 
ATOM   10368 N  N   . GLU B  1 571 ? -4.640  39.710 55.077 1.00 29.44 ? 571  GLU B N   1 
ATOM   10369 C  CA  . GLU B  1 571 ? -3.845  40.339 56.126 1.00 28.05 ? 571  GLU B CA  1 
ATOM   10370 C  C   . GLU B  1 571 ? -4.642  41.006 57.239 1.00 28.49 ? 571  GLU B C   1 
ATOM   10371 O  O   . GLU B  1 571 ? -4.058  41.586 58.162 1.00 27.21 ? 571  GLU B O   1 
ATOM   10372 C  CB  . GLU B  1 571 ? -2.884  41.381 55.522 1.00 28.38 ? 571  GLU B CB  1 
ATOM   10373 C  CG  . GLU B  1 571 ? -1.947  40.876 54.399 1.00 29.41 ? 571  GLU B CG  1 
ATOM   10374 C  CD  . GLU B  1 571 ? -1.096  39.659 54.800 1.00 30.44 ? 571  GLU B CD  1 
ATOM   10375 O  OE1 . GLU B  1 571 ? -0.854  39.469 56.005 1.00 30.67 ? 571  GLU B OE1 1 
ATOM   10376 O  OE2 . GLU B  1 571 ? -0.660  38.902 53.910 1.00 30.61 ? 571  GLU B OE2 1 
ATOM   10377 N  N   . ASN B  1 572 ? -5.968  40.956 57.158 1.00 28.44 ? 572  ASN B N   1 
ATOM   10378 C  CA  . ASN B  1 572 ? -6.803  41.585 58.187 1.00 29.05 ? 572  ASN B CA  1 
ATOM   10379 C  C   . ASN B  1 572 ? -6.455  43.058 58.422 1.00 28.38 ? 572  ASN B C   1 
ATOM   10380 O  O   . ASN B  1 572 ? -6.409  43.537 59.561 1.00 28.50 ? 572  ASN B O   1 
ATOM   10381 C  CB  . ASN B  1 572 ? -6.693  40.820 59.507 1.00 30.32 ? 572  ASN B CB  1 
ATOM   10382 C  CG  . ASN B  1 572 ? -7.197  39.391 59.392 1.00 32.36 ? 572  ASN B CG  1 
ATOM   10383 O  OD1 . ASN B  1 572 ? -6.584  38.466 59.923 1.00 35.51 ? 572  ASN B OD1 1 
ATOM   10384 N  ND2 . ASN B  1 572 ? -8.321  39.204 58.700 1.00 32.30 ? 572  ASN B ND2 1 
ATOM   10385 N  N   . ILE B  1 573 ? -6.215  43.775 57.330 1.00 27.41 ? 573  ILE B N   1 
ATOM   10386 C  CA  . ILE B  1 573 ? -5.895  45.195 57.406 1.00 26.16 ? 573  ILE B CA  1 
ATOM   10387 C  C   . ILE B  1 573 ? -7.092  46.025 56.951 1.00 24.86 ? 573  ILE B C   1 
ATOM   10388 O  O   . ILE B  1 573 ? -7.723  45.715 55.946 1.00 24.44 ? 573  ILE B O   1 
ATOM   10389 C  CB  . ILE B  1 573 ? -4.707  45.561 56.469 1.00 26.20 ? 573  ILE B CB  1 
ATOM   10390 C  CG1 . ILE B  1 573 ? -3.409  44.946 56.983 1.00 26.39 ? 573  ILE B CG1 1 
ATOM   10391 C  CG2 . ILE B  1 573 ? -4.609  47.075 56.318 1.00 25.13 ? 573  ILE B CG2 1 
ATOM   10392 C  CD1 . ILE B  1 573 ? -2.249  45.096 55.998 1.00 24.46 ? 573  ILE B CD1 1 
ATOM   10393 N  N   . ILE B  1 574 ? -7.401  47.087 57.676 1.00 23.52 ? 574  ILE B N   1 
ATOM   10394 C  CA  . ILE B  1 574 ? -8.487  47.952 57.247 1.00 23.81 ? 574  ILE B CA  1 
ATOM   10395 C  C   . ILE B  1 574 ? -7.935  48.974 56.226 1.00 24.18 ? 574  ILE B C   1 
ATOM   10396 O  O   . ILE B  1 574 ? -7.015  49.738 56.545 1.00 23.97 ? 574  ILE B O   1 
ATOM   10397 C  CB  . ILE B  1 574 ? -9.079  48.735 58.420 1.00 23.99 ? 574  ILE B CB  1 
ATOM   10398 C  CG1 . ILE B  1 574 ? -9.742  47.771 59.409 1.00 25.10 ? 574  ILE B CG1 1 
ATOM   10399 C  CG2 . ILE B  1 574 ? -10.090 49.748 57.891 1.00 24.18 ? 574  ILE B CG2 1 
ATOM   10400 C  CD1 . ILE B  1 574 ? -10.264 48.453 60.642 1.00 23.88 ? 574  ILE B CD1 1 
ATOM   10401 N  N   . VAL B  1 575 ? -8.469  48.979 55.006 1.00 23.20 ? 575  VAL B N   1 
ATOM   10402 C  CA  . VAL B  1 575 ? -8.014  49.935 53.996 1.00 22.65 ? 575  VAL B CA  1 
ATOM   10403 C  C   . VAL B  1 575 ? -9.079  51.021 53.807 1.00 22.43 ? 575  VAL B C   1 
ATOM   10404 O  O   . VAL B  1 575 ? -10.178 50.753 53.294 1.00 22.90 ? 575  VAL B O   1 
ATOM   10405 C  CB  . VAL B  1 575 ? -7.746  49.263 52.627 1.00 23.44 ? 575  VAL B CB  1 
ATOM   10406 C  CG1 . VAL B  1 575 ? -7.168  50.304 51.653 1.00 22.72 ? 575  VAL B CG1 1 
ATOM   10407 C  CG2 . VAL B  1 575 ? -6.787  48.091 52.790 1.00 22.81 ? 575  VAL B CG2 1 
ATOM   10408 N  N   . ALA B  1 576 ? -8.745  52.242 54.207 1.00 20.46 ? 576  ALA B N   1 
ATOM   10409 C  CA  . ALA B  1 576 ? -9.681  53.355 54.130 1.00 20.70 ? 576  ALA B CA  1 
ATOM   10410 C  C   . ALA B  1 576 ? -9.336  54.464 53.137 1.00 21.08 ? 576  ALA B C   1 
ATOM   10411 O  O   . ALA B  1 576 ? -8.178  54.649 52.760 1.00 20.36 ? 576  ALA B O   1 
ATOM   10412 C  CB  . ALA B  1 576 ? -9.849  53.964 55.529 1.00 21.07 ? 576  ALA B CB  1 
ATOM   10413 N  N   . SER B  1 577 ? -10.363 55.198 52.714 1.00 21.70 ? 577  SER B N   1 
ATOM   10414 C  CA  . SER B  1 577 ? -10.179 56.333 51.805 1.00 22.04 ? 577  SER B CA  1 
ATOM   10415 C  C   . SER B  1 577 ? -11.120 57.445 52.250 1.00 22.51 ? 577  SER B C   1 
ATOM   10416 O  O   . SER B  1 577 ? -12.210 57.190 52.759 1.00 23.38 ? 577  SER B O   1 
ATOM   10417 C  CB  . SER B  1 577 ? -10.457 55.933 50.356 1.00 21.46 ? 577  SER B CB  1 
ATOM   10418 O  OG  . SER B  1 577 ? -9.499  54.972 49.894 1.00 20.50 ? 577  SER B OG  1 
ATOM   10419 N  N   . PHE B  1 578 ? -10.696 58.685 52.053 1.00 23.46 ? 578  PHE B N   1 
ATOM   10420 C  CA  . PHE B  1 578 ? -11.475 59.834 52.491 1.00 23.16 ? 578  PHE B CA  1 
ATOM   10421 C  C   . PHE B  1 578 ? -11.481 60.950 51.447 1.00 23.04 ? 578  PHE B C   1 
ATOM   10422 O  O   . PHE B  1 578 ? -10.435 61.258 50.880 1.00 24.23 ? 578  PHE B O   1 
ATOM   10423 C  CB  . PHE B  1 578 ? -10.849 60.354 53.790 1.00 23.38 ? 578  PHE B CB  1 
ATOM   10424 C  CG  . PHE B  1 578 ? -11.571 61.521 54.396 1.00 24.82 ? 578  PHE B CG  1 
ATOM   10425 C  CD1 . PHE B  1 578 ? -12.724 61.327 55.151 1.00 25.15 ? 578  PHE B CD1 1 
ATOM   10426 C  CD2 . PHE B  1 578 ? -11.100 62.812 54.218 1.00 24.16 ? 578  PHE B CD2 1 
ATOM   10427 C  CE1 . PHE B  1 578 ? -13.392 62.403 55.722 1.00 25.38 ? 578  PHE B CE1 1 
ATOM   10428 C  CE2 . PHE B  1 578 ? -11.768 63.896 54.787 1.00 26.05 ? 578  PHE B CE2 1 
ATOM   10429 C  CZ  . PHE B  1 578 ? -12.916 63.685 55.540 1.00 24.60 ? 578  PHE B CZ  1 
ATOM   10430 N  N   . ASP B  1 579 ? -12.649 61.549 51.198 1.00 22.97 ? 579  ASP B N   1 
ATOM   10431 C  CA  . ASP B  1 579 ? -12.777 62.661 50.248 1.00 22.46 ? 579  ASP B CA  1 
ATOM   10432 C  C   . ASP B  1 579 ? -12.973 63.979 51.019 1.00 23.43 ? 579  ASP B C   1 
ATOM   10433 O  O   . ASP B  1 579 ? -14.080 64.289 51.470 1.00 24.22 ? 579  ASP B O   1 
ATOM   10434 C  CB  . ASP B  1 579 ? -13.966 62.459 49.304 1.00 21.52 ? 579  ASP B CB  1 
ATOM   10435 C  CG  . ASP B  1 579 ? -13.758 61.327 48.309 1.00 21.95 ? 579  ASP B CG  1 
ATOM   10436 O  OD1 . ASP B  1 579 ? -12.617 61.099 47.868 1.00 22.11 ? 579  ASP B OD1 1 
ATOM   10437 O  OD2 . ASP B  1 579 ? -14.752 60.671 47.940 1.00 22.55 ? 579  ASP B OD2 1 
ATOM   10438 N  N   . GLY B  1 580 ? -11.900 64.745 51.183 1.00 22.02 ? 580  GLY B N   1 
ATOM   10439 C  CA  . GLY B  1 580 ? -11.995 66.001 51.909 1.00 21.74 ? 580  GLY B CA  1 
ATOM   10440 C  C   . GLY B  1 580 ? -12.065 67.208 50.994 1.00 21.34 ? 580  GLY B C   1 
ATOM   10441 O  O   . GLY B  1 580 ? -12.514 67.104 49.854 1.00 22.70 ? 580  GLY B O   1 
ATOM   10442 N  N   . ARG B  1 581 ? -11.612 68.356 51.474 1.00 20.32 ? 581  ARG B N   1 
ATOM   10443 C  CA  . ARG B  1 581 ? -11.668 69.550 50.651 1.00 21.40 ? 581  ARG B CA  1 
ATOM   10444 C  C   . ARG B  1 581 ? -10.927 69.318 49.337 1.00 22.13 ? 581  ARG B C   1 
ATOM   10445 O  O   . ARG B  1 581 ? -9.874  68.675 49.311 1.00 22.61 ? 581  ARG B O   1 
ATOM   10446 C  CB  . ARG B  1 581 ? -11.120 70.754 51.427 1.00 21.12 ? 581  ARG B CB  1 
ATOM   10447 C  CG  . ARG B  1 581 ? -12.157 71.305 52.426 1.00 22.61 ? 581  ARG B CG  1 
ATOM   10448 C  CD  . ARG B  1 581 ? -11.606 72.337 53.401 1.00 21.52 ? 581  ARG B CD  1 
ATOM   10449 N  NE  . ARG B  1 581 ? -10.715 71.721 54.381 1.00 22.79 ? 581  ARG B NE  1 
ATOM   10450 C  CZ  . ARG B  1 581 ? -10.073 72.389 55.334 1.00 23.57 ? 581  ARG B CZ  1 
ATOM   10451 N  NH1 . ARG B  1 581 ? -10.232 73.700 55.433 1.00 25.18 ? 581  ARG B NH1 1 
ATOM   10452 N  NH2 . ARG B  1 581 ? -9.264  71.748 56.177 1.00 23.45 ? 581  ARG B NH2 1 
ATOM   10453 N  N   . GLY B  1 582 ? -11.503 69.819 48.246 1.00 21.43 ? 582  GLY B N   1 
ATOM   10454 C  CA  . GLY B  1 582 ? -10.918 69.626 46.932 1.00 20.66 ? 582  GLY B CA  1 
ATOM   10455 C  C   . GLY B  1 582 ? -11.596 68.488 46.156 1.00 20.98 ? 582  GLY B C   1 
ATOM   10456 O  O   . GLY B  1 582 ? -11.544 68.474 44.925 1.00 21.52 ? 582  GLY B O   1 
ATOM   10457 N  N   . SER B  1 583 ? -12.242 67.544 46.849 1.00 19.52 ? 583  SER B N   1 
ATOM   10458 C  CA  . SER B  1 583 ? -12.890 66.422 46.161 1.00 20.31 ? 583  SER B CA  1 
ATOM   10459 C  C   . SER B  1 583 ? -14.107 66.891 45.342 1.00 21.06 ? 583  SER B C   1 
ATOM   10460 O  O   . SER B  1 583 ? -14.664 67.965 45.611 1.00 19.75 ? 583  SER B O   1 
ATOM   10461 C  CB  . SER B  1 583 ? -13.276 65.322 47.159 1.00 20.49 ? 583  SER B CB  1 
ATOM   10462 O  OG  . SER B  1 583 ? -14.116 65.807 48.183 1.00 20.47 ? 583  SER B OG  1 
ATOM   10463 N  N   . GLY B  1 584 ? -14.527 66.088 44.360 1.00 21.13 ? 584  GLY B N   1 
ATOM   10464 C  CA  . GLY B  1 584 ? -15.609 66.514 43.482 1.00 20.85 ? 584  GLY B CA  1 
ATOM   10465 C  C   . GLY B  1 584 ? -17.008 65.955 43.630 1.00 22.02 ? 584  GLY B C   1 
ATOM   10466 O  O   . GLY B  1 584 ? -17.297 65.146 44.516 1.00 22.87 ? 584  GLY B O   1 
ATOM   10467 N  N   . TYR B  1 585 ? -17.889 66.431 42.752 1.00 21.72 ? 585  TYR B N   1 
ATOM   10468 C  CA  . TYR B  1 585 ? -19.281 65.978 42.699 1.00 21.41 ? 585  TYR B CA  1 
ATOM   10469 C  C   . TYR B  1 585 ? -20.097 66.349 43.937 1.00 21.39 ? 585  TYR B C   1 
ATOM   10470 O  O   . TYR B  1 585 ? -21.137 65.750 44.209 1.00 22.31 ? 585  TYR B O   1 
ATOM   10471 C  CB  . TYR B  1 585 ? -19.305 64.456 42.486 1.00 20.65 ? 585  TYR B CB  1 
ATOM   10472 C  CG  . TYR B  1 585 ? -18.356 64.010 41.401 1.00 19.12 ? 585  TYR B CG  1 
ATOM   10473 C  CD1 . TYR B  1 585 ? -18.563 64.370 40.073 1.00 19.09 ? 585  TYR B CD1 1 
ATOM   10474 C  CD2 . TYR B  1 585 ? -17.205 63.286 41.718 1.00 18.60 ? 585  TYR B CD2 1 
ATOM   10475 C  CE1 . TYR B  1 585 ? -17.635 64.022 39.072 1.00 17.46 ? 585  TYR B CE1 1 
ATOM   10476 C  CE2 . TYR B  1 585 ? -16.276 62.941 40.740 1.00 17.59 ? 585  TYR B CE2 1 
ATOM   10477 C  CZ  . TYR B  1 585 ? -16.499 63.322 39.412 1.00 18.73 ? 585  TYR B CZ  1 
ATOM   10478 O  OH  . TYR B  1 585 ? -15.548 63.028 38.460 1.00 18.80 ? 585  TYR B OH  1 
ATOM   10479 N  N   . GLN B  1 586 ? -19.629 67.353 44.665 1.00 21.66 ? 586  GLN B N   1 
ATOM   10480 C  CA  . GLN B  1 586 ? -20.297 67.802 45.873 1.00 22.14 ? 586  GLN B CA  1 
ATOM   10481 C  C   . GLN B  1 586 ? -20.418 69.317 45.939 1.00 22.54 ? 586  GLN B C   1 
ATOM   10482 O  O   . GLN B  1 586 ? -20.590 69.876 47.022 1.00 24.48 ? 586  GLN B O   1 
ATOM   10483 C  CB  . GLN B  1 586 ? -19.526 67.339 47.107 1.00 22.26 ? 586  GLN B CB  1 
ATOM   10484 C  CG  . GLN B  1 586 ? -19.352 65.858 47.217 1.00 22.92 ? 586  GLN B CG  1 
ATOM   10485 C  CD  . GLN B  1 586 ? -18.173 65.518 48.104 1.00 26.35 ? 586  GLN B CD  1 
ATOM   10486 O  OE1 . GLN B  1 586 ? -18.252 65.609 49.334 1.00 25.77 ? 586  GLN B OE1 1 
ATOM   10487 N  NE2 . GLN B  1 586 ? -17.050 65.153 47.476 1.00 26.03 ? 586  GLN B NE2 1 
ATOM   10488 N  N   . GLY B  1 587 ? -20.328 69.988 44.800 1.00 22.20 ? 587  GLY B N   1 
ATOM   10489 C  CA  . GLY B  1 587 ? -20.418 71.438 44.808 1.00 22.53 ? 587  GLY B CA  1 
ATOM   10490 C  C   . GLY B  1 587 ? -19.057 72.115 44.823 1.00 23.29 ? 587  GLY B C   1 
ATOM   10491 O  O   . GLY B  1 587 ? -18.061 71.537 45.268 1.00 22.88 ? 587  GLY B O   1 
ATOM   10492 N  N   . ASP B  1 588 ? -19.022 73.351 44.342 1.00 23.72 ? 588  ASP B N   1 
ATOM   10493 C  CA  . ASP B  1 588 ? -17.798 74.129 44.281 1.00 25.56 ? 588  ASP B CA  1 
ATOM   10494 C  C   . ASP B  1 588 ? -17.227 74.538 45.648 1.00 25.98 ? 588  ASP B C   1 
ATOM   10495 O  O   . ASP B  1 588 ? -16.017 74.747 45.792 1.00 25.37 ? 588  ASP B O   1 
ATOM   10496 C  CB  . ASP B  1 588 ? -18.023 75.373 43.420 1.00 25.18 ? 588  ASP B CB  1 
ATOM   10497 C  CG  . ASP B  1 588 ? -18.088 75.050 41.936 1.00 26.71 ? 588  ASP B CG  1 
ATOM   10498 O  OD1 . ASP B  1 588 ? -17.691 73.925 41.542 1.00 28.02 ? 588  ASP B OD1 1 
ATOM   10499 O  OD2 . ASP B  1 588 ? -18.519 75.925 41.153 1.00 26.43 ? 588  ASP B OD2 1 
ATOM   10500 N  N   . LYS B  1 589 ? -18.090 74.654 46.648 1.00 26.43 ? 589  LYS B N   1 
ATOM   10501 C  CA  . LYS B  1 589 ? -17.636 75.041 47.981 1.00 28.28 ? 589  LYS B CA  1 
ATOM   10502 C  C   . LYS B  1 589 ? -16.509 74.089 48.417 1.00 27.47 ? 589  LYS B C   1 
ATOM   10503 O  O   . LYS B  1 589 ? -15.466 74.523 48.920 1.00 26.50 ? 589  LYS B O   1 
ATOM   10504 C  CB  . LYS B  1 589 ? -18.810 74.982 48.960 1.00 30.85 ? 589  LYS B CB  1 
ATOM   10505 C  CG  . LYS B  1 589 ? -18.429 75.070 50.419 1.00 35.22 ? 589  LYS B CG  1 
ATOM   10506 C  CD  . LYS B  1 589 ? -17.980 76.462 50.802 1.00 39.07 ? 589  LYS B CD  1 
ATOM   10507 C  CE  . LYS B  1 589 ? -17.754 76.581 52.321 1.00 42.11 ? 589  LYS B CE  1 
ATOM   10508 N  NZ  . LYS B  1 589 ? -19.018 76.533 53.123 1.00 43.21 ? 589  LYS B NZ  1 
ATOM   10509 N  N   . ILE B  1 590 ? -16.727 72.791 48.209 1.00 25.51 ? 590  ILE B N   1 
ATOM   10510 C  CA  . ILE B  1 590 ? -15.730 71.789 48.550 1.00 24.36 ? 590  ILE B CA  1 
ATOM   10511 C  C   . ILE B  1 590 ? -14.656 71.673 47.455 1.00 23.52 ? 590  ILE B C   1 
ATOM   10512 O  O   . ILE B  1 590 ? -13.465 71.673 47.751 1.00 23.79 ? 590  ILE B O   1 
ATOM   10513 C  CB  . ILE B  1 590 ? -16.393 70.382 48.782 1.00 23.94 ? 590  ILE B CB  1 
ATOM   10514 C  CG1 . ILE B  1 590 ? -17.168 70.367 50.102 1.00 23.27 ? 590  ILE B CG1 1 
ATOM   10515 C  CG2 . ILE B  1 590 ? -15.338 69.297 48.827 1.00 22.10 ? 590  ILE B CG2 1 
ATOM   10516 C  CD1 . ILE B  1 590 ? -17.934 69.073 50.369 1.00 20.80 ? 590  ILE B CD1 1 
ATOM   10517 N  N   . MET B  1 591 ? -15.067 71.599 46.197 1.00 22.52 ? 591  MET B N   1 
ATOM   10518 C  CA  . MET B  1 591 ? -14.091 71.450 45.128 1.00 23.48 ? 591  MET B CA  1 
ATOM   10519 C  C   . MET B  1 591 ? -13.080 72.578 45.014 1.00 23.65 ? 591  MET B C   1 
ATOM   10520 O  O   . MET B  1 591 ? -11.879 72.325 44.954 1.00 24.02 ? 591  MET B O   1 
ATOM   10521 C  CB  . MET B  1 591 ? -14.774 71.264 43.778 1.00 22.60 ? 591  MET B CB  1 
ATOM   10522 C  CG  . MET B  1 591 ? -13.812 70.753 42.719 1.00 22.81 ? 591  MET B CG  1 
ATOM   10523 S  SD  . MET B  1 591 ? -14.674 70.226 41.248 1.00 24.65 ? 591  MET B SD  1 
ATOM   10524 C  CE  . MET B  1 591 ? -14.993 71.827 40.479 1.00 21.24 ? 591  MET B CE  1 
ATOM   10525 N  N   . HIS B  1 592 ? -13.556 73.816 44.998 1.00 22.92 ? 592  HIS B N   1 
ATOM   10526 C  CA  . HIS B  1 592 ? -12.660 74.956 44.886 1.00 23.92 ? 592  HIS B CA  1 
ATOM   10527 C  C   . HIS B  1 592 ? -11.994 75.366 46.199 1.00 24.44 ? 592  HIS B C   1 
ATOM   10528 O  O   . HIS B  1 592 ? -11.301 76.399 46.245 1.00 25.22 ? 592  HIS B O   1 
ATOM   10529 C  CB  . HIS B  1 592 ? -13.388 76.167 44.287 1.00 22.77 ? 592  HIS B CB  1 
ATOM   10530 C  CG  . HIS B  1 592 ? -13.838 75.962 42.870 1.00 24.65 ? 592  HIS B CG  1 
ATOM   10531 N  ND1 . HIS B  1 592 ? -14.684 76.841 42.222 1.00 24.36 ? 592  HIS B ND1 1 
ATOM   10532 C  CD2 . HIS B  1 592 ? -13.538 74.998 41.964 1.00 24.70 ? 592  HIS B CD2 1 
ATOM   10533 C  CE1 . HIS B  1 592 ? -14.880 76.430 40.982 1.00 25.20 ? 592  HIS B CE1 1 
ATOM   10534 N  NE2 . HIS B  1 592 ? -14.197 75.312 40.798 1.00 24.72 ? 592  HIS B NE2 1 
ATOM   10535 N  N   . ALA B  1 593 ? -12.165 74.578 47.262 1.00 23.58 ? 593  ALA B N   1 
ATOM   10536 C  CA  . ALA B  1 593 ? -11.538 74.942 48.550 1.00 24.43 ? 593  ALA B CA  1 
ATOM   10537 C  C   . ALA B  1 593 ? -10.005 74.994 48.439 1.00 24.10 ? 593  ALA B C   1 
ATOM   10538 O  O   . ALA B  1 593 ? -9.351  75.722 49.190 1.00 24.80 ? 593  ALA B O   1 
ATOM   10539 C  CB  . ALA B  1 593 ? -11.962 73.959 49.656 1.00 21.68 ? 593  ALA B CB  1 
ATOM   10540 N  N   . ILE B  1 594 ? -9.434  74.238 47.500 1.00 23.31 ? 594  ILE B N   1 
ATOM   10541 C  CA  . ILE B  1 594 ? -7.991  74.248 47.338 1.00 23.50 ? 594  ILE B CA  1 
ATOM   10542 C  C   . ILE B  1 594 ? -7.510  75.102 46.191 1.00 23.60 ? 594  ILE B C   1 
ATOM   10543 O  O   . ILE B  1 594 ? -6.354  75.018 45.812 1.00 24.06 ? 594  ILE B O   1 
ATOM   10544 C  CB  . ILE B  1 594 ? -7.411  72.819 47.180 1.00 23.77 ? 594  ILE B CB  1 
ATOM   10545 C  CG1 . ILE B  1 594 ? -8.097  72.087 46.017 1.00 24.07 ? 594  ILE B CG1 1 
ATOM   10546 C  CG2 . ILE B  1 594 ? -7.552  72.066 48.502 1.00 22.70 ? 594  ILE B CG2 1 
ATOM   10547 C  CD1 . ILE B  1 594 ? -7.590  70.671 45.805 1.00 25.69 ? 594  ILE B CD1 1 
ATOM   10548 N  N   . ASN B  1 595 ? -8.385  75.938 45.647 1.00 24.32 ? 595  ASN B N   1 
ATOM   10549 C  CA  . ASN B  1 595 ? -7.994  76.816 44.537 1.00 25.04 ? 595  ASN B CA  1 
ATOM   10550 C  C   . ASN B  1 595 ? -6.716  77.587 44.882 1.00 25.28 ? 595  ASN B C   1 
ATOM   10551 O  O   . ASN B  1 595 ? -6.643  78.250 45.923 1.00 25.87 ? 595  ASN B O   1 
ATOM   10552 C  CB  . ASN B  1 595 ? -9.114  77.815 44.230 1.00 24.59 ? 595  ASN B CB  1 
ATOM   10553 C  CG  . ASN B  1 595 ? -8.805  78.700 43.024 1.00 25.88 ? 595  ASN B CG  1 
ATOM   10554 O  OD1 . ASN B  1 595 ? -9.047  79.897 43.063 1.00 28.01 ? 595  ASN B OD1 1 
ATOM   10555 N  ND2 . ASN B  1 595 ? -8.281  78.113 41.952 1.00 22.15 ? 595  ASN B ND2 1 
ATOM   10556 N  N   . ARG B  1 596 ? -5.723  77.497 43.998 1.00 24.76 ? 596  ARG B N   1 
ATOM   10557 C  CA  . ARG B  1 596 ? -4.425  78.150 44.166 1.00 24.61 ? 596  ARG B CA  1 
ATOM   10558 C  C   . ARG B  1 596 ? -3.679  77.674 45.418 1.00 23.57 ? 596  ARG B C   1 
ATOM   10559 O  O   . ARG B  1 596 ? -2.659  78.255 45.796 1.00 22.17 ? 596  ARG B O   1 
ATOM   10560 C  CB  . ARG B  1 596 ? -4.594  79.683 44.220 1.00 24.30 ? 596  ARG B CB  1 
ATOM   10561 C  CG  . ARG B  1 596 ? -5.072  80.338 42.916 1.00 24.13 ? 596  ARG B CG  1 
ATOM   10562 C  CD  . ARG B  1 596 ? -5.453  81.812 43.183 1.00 26.00 ? 596  ARG B CD  1 
ATOM   10563 N  NE  . ARG B  1 596 ? -4.319  82.649 43.586 1.00 25.27 ? 596  ARG B NE  1 
ATOM   10564 C  CZ  . ARG B  1 596 ? -3.381  83.081 42.751 1.00 26.05 ? 596  ARG B CZ  1 
ATOM   10565 N  NH1 . ARG B  1 596 ? -3.447  82.758 41.465 1.00 26.47 ? 596  ARG B NH1 1 
ATOM   10566 N  NH2 . ARG B  1 596 ? -2.374  83.829 43.196 1.00 25.84 ? 596  ARG B NH2 1 
ATOM   10567 N  N   . ARG B  1 597 ? -4.175  76.605 46.034 1.00 24.58 ? 597  ARG B N   1 
ATOM   10568 C  CA  . ARG B  1 597 ? -3.603  76.077 47.280 1.00 25.51 ? 597  ARG B CA  1 
ATOM   10569 C  C   . ARG B  1 597 ? -3.394  74.575 47.351 1.00 24.23 ? 597  ARG B C   1 
ATOM   10570 O  O   . ARG B  1 597 ? -3.732  73.954 48.370 1.00 23.87 ? 597  ARG B O   1 
ATOM   10571 C  CB  . ARG B  1 597 ? -4.500  76.485 48.461 1.00 28.87 ? 597  ARG B CB  1 
ATOM   10572 C  CG  . ARG B  1 597 ? -3.882  77.504 49.400 1.00 35.16 ? 597  ARG B CG  1 
ATOM   10573 C  CD  . ARG B  1 597 ? -3.338  78.668 48.604 1.00 38.74 ? 597  ARG B CD  1 
ATOM   10574 N  NE  . ARG B  1 597 ? -2.658  79.700 49.390 1.00 41.43 ? 597  ARG B NE  1 
ATOM   10575 C  CZ  . ARG B  1 597 ? -2.027  80.728 48.828 1.00 43.97 ? 597  ARG B CZ  1 
ATOM   10576 N  NH1 . ARG B  1 597 ? -1.994  80.834 47.497 1.00 43.75 ? 597  ARG B NH1 1 
ATOM   10577 N  NH2 . ARG B  1 597 ? -1.442  81.650 49.581 1.00 45.24 ? 597  ARG B NH2 1 
ATOM   10578 N  N   . LEU B  1 598 ? -2.844  73.977 46.297 1.00 22.88 ? 598  LEU B N   1 
ATOM   10579 C  CA  . LEU B  1 598 ? -2.605  72.534 46.316 1.00 22.00 ? 598  LEU B CA  1 
ATOM   10580 C  C   . LEU B  1 598 ? -1.573  72.247 47.399 1.00 21.94 ? 598  LEU B C   1 
ATOM   10581 O  O   . LEU B  1 598 ? -0.706  73.072 47.677 1.00 22.92 ? 598  LEU B O   1 
ATOM   10582 C  CB  . LEU B  1 598 ? -2.078  72.044 44.961 1.00 20.21 ? 598  LEU B CB  1 
ATOM   10583 C  CG  . LEU B  1 598 ? -2.959  72.245 43.721 1.00 19.83 ? 598  LEU B CG  1 
ATOM   10584 C  CD1 . LEU B  1 598 ? -2.320  71.488 42.577 1.00 18.18 ? 598  LEU B CD1 1 
ATOM   10585 C  CD2 . LEU B  1 598 ? -4.397  71.730 43.955 1.00 18.84 ? 598  LEU B CD2 1 
ATOM   10586 N  N   . GLY B  1 599 ? -1.671  71.081 48.014 1.00 21.60 ? 599  GLY B N   1 
ATOM   10587 C  CA  . GLY B  1 599 ? -0.733  70.738 49.049 1.00 21.90 ? 599  GLY B CA  1 
ATOM   10588 C  C   . GLY B  1 599 ? -1.115  71.272 50.416 1.00 22.96 ? 599  GLY B C   1 
ATOM   10589 O  O   . GLY B  1 599 ? -0.280  71.288 51.325 1.00 23.94 ? 599  GLY B O   1 
ATOM   10590 N  N   . THR B  1 600 ? -2.355  71.717 50.592 1.00 22.11 ? 600  THR B N   1 
ATOM   10591 C  CA  . THR B  1 600 ? -2.751  72.209 51.908 1.00 21.75 ? 600  THR B CA  1 
ATOM   10592 C  C   . THR B  1 600 ? -3.943  71.471 52.502 1.00 22.71 ? 600  THR B C   1 
ATOM   10593 O  O   . THR B  1 600 ? -3.769  70.437 53.152 1.00 22.37 ? 600  THR B O   1 
ATOM   10594 C  CB  . THR B  1 600 ? -3.071  73.734 51.885 1.00 22.32 ? 600  THR B CB  1 
ATOM   10595 O  OG1 . THR B  1 600 ? -4.153  74.001 50.981 1.00 23.50 ? 600  THR B OG1 1 
ATOM   10596 C  CG2 . THR B  1 600 ? -1.857  74.524 51.451 1.00 20.80 ? 600  THR B CG2 1 
ATOM   10597 N  N   . PHE B  1 601 ? -5.152  71.977 52.249 1.00 22.45 ? 601  PHE B N   1 
ATOM   10598 C  CA  . PHE B  1 601 ? -6.345  71.378 52.832 1.00 23.22 ? 601  PHE B CA  1 
ATOM   10599 C  C   . PHE B  1 601 ? -6.570  69.913 52.495 1.00 23.38 ? 601  PHE B C   1 
ATOM   10600 O  O   . PHE B  1 601 ? -7.046  69.155 53.335 1.00 22.83 ? 601  PHE B O   1 
ATOM   10601 C  CB  . PHE B  1 601 ? -7.598  72.177 52.457 1.00 24.51 ? 601  PHE B CB  1 
ATOM   10602 C  CG  . PHE B  1 601 ? -7.593  73.604 52.952 1.00 27.19 ? 601  PHE B CG  1 
ATOM   10603 C  CD1 . PHE B  1 601 ? -7.118  73.911 54.225 1.00 28.00 ? 601  PHE B CD1 1 
ATOM   10604 C  CD2 . PHE B  1 601 ? -8.088  74.634 52.153 1.00 27.57 ? 601  PHE B CD2 1 
ATOM   10605 C  CE1 . PHE B  1 601 ? -7.131  75.227 54.707 1.00 29.32 ? 601  PHE B CE1 1 
ATOM   10606 C  CE2 . PHE B  1 601 ? -8.110  75.958 52.621 1.00 30.69 ? 601  PHE B CE2 1 
ATOM   10607 C  CZ  . PHE B  1 601 ? -7.630  76.255 53.904 1.00 30.21 ? 601  PHE B CZ  1 
ATOM   10608 N  N   . GLU B  1 602 ? -6.245  69.512 51.273 1.00 22.70 ? 602  GLU B N   1 
ATOM   10609 C  CA  . GLU B  1 602 ? -6.461  68.129 50.909 1.00 23.66 ? 602  GLU B CA  1 
ATOM   10610 C  C   . GLU B  1 602 ? -5.458  67.243 51.621 1.00 23.10 ? 602  GLU B C   1 
ATOM   10611 O  O   . GLU B  1 602 ? -5.696  66.046 51.780 1.00 24.01 ? 602  GLU B O   1 
ATOM   10612 C  CB  . GLU B  1 602 ? -6.415  67.926 49.378 1.00 24.56 ? 602  GLU B CB  1 
ATOM   10613 C  CG  . GLU B  1 602 ? -5.055  67.786 48.714 1.00 24.02 ? 602  GLU B CG  1 
ATOM   10614 C  CD  . GLU B  1 602 ? -4.327  69.096 48.501 1.00 25.40 ? 602  GLU B CD  1 
ATOM   10615 O  OE1 . GLU B  1 602 ? -3.433  69.138 47.614 1.00 25.70 ? 602  GLU B OE1 1 
ATOM   10616 O  OE2 . GLU B  1 602 ? -4.612  70.088 49.220 1.00 26.82 ? 602  GLU B OE2 1 
ATOM   10617 N  N   . VAL B  1 603 ? -4.349  67.826 52.071 1.00 22.60 ? 603  VAL B N   1 
ATOM   10618 C  CA  . VAL B  1 603 ? -3.349  67.046 52.804 1.00 23.03 ? 603  VAL B CA  1 
ATOM   10619 C  C   . VAL B  1 603 ? -3.780  66.973 54.274 1.00 23.83 ? 603  VAL B C   1 
ATOM   10620 O  O   . VAL B  1 603 ? -3.819  65.897 54.870 1.00 22.85 ? 603  VAL B O   1 
ATOM   10621 C  CB  . VAL B  1 603 ? -1.934  67.681 52.724 1.00 22.58 ? 603  VAL B CB  1 
ATOM   10622 C  CG1 . VAL B  1 603 ? -0.969  66.858 53.553 1.00 22.34 ? 603  VAL B CG1 1 
ATOM   10623 C  CG2 . VAL B  1 603 ? -1.462  67.767 51.279 1.00 20.67 ? 603  VAL B CG2 1 
ATOM   10624 N  N   . GLU B  1 604 ? -4.133  68.114 54.850 1.00 24.87 ? 604  GLU B N   1 
ATOM   10625 C  CA  . GLU B  1 604 ? -4.565  68.137 56.247 1.00 28.12 ? 604  GLU B CA  1 
ATOM   10626 C  C   . GLU B  1 604 ? -5.838  67.295 56.474 1.00 27.58 ? 604  GLU B C   1 
ATOM   10627 O  O   . GLU B  1 604 ? -5.920  66.543 57.447 1.00 26.82 ? 604  GLU B O   1 
ATOM   10628 C  CB  . GLU B  1 604 ? -4.799  69.590 56.699 1.00 30.98 ? 604  GLU B CB  1 
ATOM   10629 C  CG  . GLU B  1 604 ? -3.592  70.508 56.451 1.00 37.11 ? 604  GLU B CG  1 
ATOM   10630 C  CD  . GLU B  1 604 ? -3.921  72.004 56.579 1.00 42.33 ? 604  GLU B CD  1 
ATOM   10631 O  OE1 . GLU B  1 604 ? -4.191  72.487 57.709 1.00 45.08 ? 604  GLU B OE1 1 
ATOM   10632 O  OE2 . GLU B  1 604 ? -3.908  72.705 55.539 1.00 44.89 ? 604  GLU B OE2 1 
ATOM   10633 N  N   . ASP B  1 605 ? -6.822  67.398 55.585 1.00 26.58 ? 605  ASP B N   1 
ATOM   10634 C  CA  . ASP B  1 605 ? -8.047  66.617 55.789 1.00 27.71 ? 605  ASP B CA  1 
ATOM   10635 C  C   . ASP B  1 605 ? -7.768  65.119 55.827 1.00 27.33 ? 605  ASP B C   1 
ATOM   10636 O  O   . ASP B  1 605 ? -8.417  64.377 56.556 1.00 28.48 ? 605  ASP B O   1 
ATOM   10637 C  CB  . ASP B  1 605 ? -9.103  66.954 54.731 1.00 27.20 ? 605  ASP B CB  1 
ATOM   10638 C  CG  . ASP B  1 605 ? -9.649  68.383 54.890 1.00 28.73 ? 605  ASP B CG  1 
ATOM   10639 O  OD1 . ASP B  1 605 ? -9.249  69.065 55.862 1.00 28.26 ? 605  ASP B OD1 1 
ATOM   10640 O  OD2 . ASP B  1 605 ? -10.468 68.832 54.055 1.00 29.80 ? 605  ASP B OD2 1 
ATOM   10641 N  N   . GLN B  1 606 ? -6.776  64.689 55.066 1.00 27.26 ? 606  GLN B N   1 
ATOM   10642 C  CA  . GLN B  1 606 ? -6.376  63.293 55.022 1.00 26.64 ? 606  GLN B CA  1 
ATOM   10643 C  C   . GLN B  1 606 ? -5.805  62.908 56.399 1.00 27.06 ? 606  GLN B C   1 
ATOM   10644 O  O   . GLN B  1 606 ? -6.101  61.831 56.925 1.00 26.56 ? 606  GLN B O   1 
ATOM   10645 C  CB  . GLN B  1 606 ? -5.325  63.126 53.926 1.00 27.90 ? 606  GLN B CB  1 
ATOM   10646 C  CG  . GLN B  1 606 ? -5.368  61.824 53.192 1.00 28.55 ? 606  GLN B CG  1 
ATOM   10647 C  CD  . GLN B  1 606 ? -6.715  61.511 52.555 1.00 27.68 ? 606  GLN B CD  1 
ATOM   10648 O  OE1 . GLN B  1 606 ? -7.074  60.356 52.447 1.00 28.13 ? 606  GLN B OE1 1 
ATOM   10649 N  NE2 . GLN B  1 606 ? -7.450  62.526 52.127 1.00 27.68 ? 606  GLN B NE2 1 
ATOM   10650 N  N   . ILE B  1 607 ? -4.992  63.787 56.987 1.00 27.24 ? 607  ILE B N   1 
ATOM   10651 C  CA  . ILE B  1 607 ? -4.415  63.533 58.319 1.00 27.32 ? 607  ILE B CA  1 
ATOM   10652 C  C   . ILE B  1 607 ? -5.559  63.515 59.346 1.00 28.17 ? 607  ILE B C   1 
ATOM   10653 O  O   . ILE B  1 607 ? -5.637  62.629 60.201 1.00 26.90 ? 607  ILE B O   1 
ATOM   10654 C  CB  . ILE B  1 607 ? -3.400  64.642 58.736 1.00 26.82 ? 607  ILE B CB  1 
ATOM   10655 C  CG1 . ILE B  1 607 ? -2.193  64.619 57.804 1.00 26.55 ? 607  ILE B CG1 1 
ATOM   10656 C  CG2 . ILE B  1 607 ? -2.936  64.436 60.188 1.00 25.83 ? 607  ILE B CG2 1 
ATOM   10657 C  CD1 . ILE B  1 607 ? -1.284  65.847 57.932 1.00 24.65 ? 607  ILE B CD1 1 
ATOM   10658 N  N   . GLU B  1 608 ? -6.438  64.507 59.242 1.00 28.59 ? 608  GLU B N   1 
ATOM   10659 C  CA  . GLU B  1 608 ? -7.583  64.620 60.133 1.00 30.64 ? 608  GLU B CA  1 
ATOM   10660 C  C   . GLU B  1 608 ? -8.484  63.396 60.006 1.00 31.16 ? 608  GLU B C   1 
ATOM   10661 O  O   . GLU B  1 608 ? -9.103  62.974 60.994 1.00 33.01 ? 608  GLU B O   1 
ATOM   10662 C  CB  . GLU B  1 608 ? -8.378  65.900 59.832 1.00 30.84 ? 608  GLU B CB  1 
ATOM   10663 C  CG  . GLU B  1 608 ? -9.617  66.115 60.724 1.00 32.80 ? 608  GLU B CG  1 
ATOM   10664 C  CD  . GLU B  1 608 ? -9.313  66.051 62.225 1.00 34.16 ? 608  GLU B CD  1 
ATOM   10665 O  OE1 . GLU B  1 608 ? -8.239  66.530 62.650 1.00 35.92 ? 608  GLU B OE1 1 
ATOM   10666 O  OE2 . GLU B  1 608 ? -10.156 65.529 62.986 1.00 34.11 ? 608  GLU B OE2 1 
ATOM   10667 N  N   . ALA B  1 609 ? -8.565  62.816 58.809 1.00 29.67 ? 609  ALA B N   1 
ATOM   10668 C  CA  . ALA B  1 609 ? -9.396  61.621 58.614 1.00 28.25 ? 609  ALA B CA  1 
ATOM   10669 C  C   . ALA B  1 609 ? -8.832  60.444 59.401 1.00 28.31 ? 609  ALA B C   1 
ATOM   10670 O  O   . ALA B  1 609 ? -9.588  59.653 59.970 1.00 26.46 ? 609  ALA B O   1 
ATOM   10671 C  CB  . ALA B  1 609 ? -9.474  61.253 57.138 1.00 27.95 ? 609  ALA B CB  1 
ATOM   10672 N  N   . ALA B  1 610 ? -7.504  60.313 59.416 1.00 27.42 ? 610  ALA B N   1 
ATOM   10673 C  CA  . ALA B  1 610 ? -6.868  59.225 60.161 1.00 27.21 ? 610  ALA B CA  1 
ATOM   10674 C  C   . ALA B  1 610 ? -7.178  59.380 61.661 1.00 28.12 ? 610  ALA B C   1 
ATOM   10675 O  O   . ALA B  1 610 ? -7.484  58.401 62.334 1.00 28.72 ? 610  ALA B O   1 
ATOM   10676 C  CB  . ALA B  1 610 ? -5.361  59.218 59.924 1.00 24.72 ? 610  ALA B CB  1 
ATOM   10677 N  N   . ARG B  1 611 ? -7.106  60.605 62.173 1.00 29.39 ? 611  ARG B N   1 
ATOM   10678 C  CA  . ARG B  1 611 ? -7.420  60.860 63.581 1.00 31.99 ? 611  ARG B CA  1 
ATOM   10679 C  C   . ARG B  1 611 ? -8.840  60.395 63.865 1.00 32.34 ? 611  ARG B C   1 
ATOM   10680 O  O   . ARG B  1 611 ? -9.076  59.609 64.778 1.00 33.60 ? 611  ARG B O   1 
ATOM   10681 C  CB  . ARG B  1 611 ? -7.330  62.350 63.907 1.00 30.76 ? 611  ARG B CB  1 
ATOM   10682 C  CG  . ARG B  1 611 ? -5.924  62.891 63.935 1.00 31.38 ? 611  ARG B CG  1 
ATOM   10683 C  CD  . ARG B  1 611 ? -5.914  64.384 64.264 1.00 30.38 ? 611  ARG B CD  1 
ATOM   10684 N  NE  . ARG B  1 611 ? -4.571  64.945 64.123 1.00 31.22 ? 611  ARG B NE  1 
ATOM   10685 C  CZ  . ARG B  1 611 ? -4.260  65.926 63.282 1.00 31.87 ? 611  ARG B CZ  1 
ATOM   10686 N  NH1 . ARG B  1 611 ? -5.200  66.455 62.504 1.00 30.75 ? 611  ARG B NH1 1 
ATOM   10687 N  NH2 . ARG B  1 611 ? -3.012  66.379 63.219 1.00 32.07 ? 611  ARG B NH2 1 
ATOM   10688 N  N   . GLN B  1 612 ? -9.782  60.905 63.078 1.00 34.11 ? 612  GLN B N   1 
ATOM   10689 C  CA  . GLN B  1 612 ? -11.189 60.549 63.207 1.00 34.94 ? 612  GLN B CA  1 
ATOM   10690 C  C   . GLN B  1 612 ? -11.349 59.037 63.207 1.00 35.35 ? 612  GLN B C   1 
ATOM   10691 O  O   . GLN B  1 612 ? -12.149 58.499 63.977 1.00 36.25 ? 612  GLN B O   1 
ATOM   10692 C  CB  . GLN B  1 612 ? -12.006 61.116 62.044 1.00 36.10 ? 612  GLN B CB  1 
ATOM   10693 C  CG  . GLN B  1 612 ? -12.100 62.631 61.994 1.00 38.55 ? 612  GLN B CG  1 
ATOM   10694 C  CD  . GLN B  1 612 ? -12.976 63.186 63.093 1.00 39.30 ? 612  GLN B CD  1 
ATOM   10695 O  OE1 . GLN B  1 612 ? -14.090 62.707 63.303 1.00 40.02 ? 612  GLN B OE1 1 
ATOM   10696 N  NE2 . GLN B  1 612 ? -12.485 64.205 63.792 1.00 38.35 ? 612  GLN B NE2 1 
ATOM   10697 N  N   . PHE B  1 613 ? -10.608 58.349 62.340 1.00 35.00 ? 613  PHE B N   1 
ATOM   10698 C  CA  . PHE B  1 613 ? -10.710 56.898 62.280 1.00 35.96 ? 613  PHE B CA  1 
ATOM   10699 C  C   . PHE B  1 613 ? -10.145 56.295 63.563 1.00 37.05 ? 613  PHE B C   1 
ATOM   10700 O  O   . PHE B  1 613 ? -10.641 55.275 64.046 1.00 36.73 ? 613  PHE B O   1 
ATOM   10701 C  CB  . PHE B  1 613 ? -9.973  56.333 61.060 1.00 35.44 ? 613  PHE B CB  1 
ATOM   10702 C  CG  . PHE B  1 613 ? -10.544 56.775 59.733 1.00 35.64 ? 613  PHE B CG  1 
ATOM   10703 C  CD1 . PHE B  1 613 ? -11.915 56.942 59.566 1.00 35.76 ? 613  PHE B CD1 1 
ATOM   10704 C  CD2 . PHE B  1 613 ? -9.710  56.981 58.639 1.00 35.52 ? 613  PHE B CD2 1 
ATOM   10705 C  CE1 . PHE B  1 613 ? -12.448 57.308 58.327 1.00 35.35 ? 613  PHE B CE1 1 
ATOM   10706 C  CE2 . PHE B  1 613 ? -10.230 57.346 57.397 1.00 35.96 ? 613  PHE B CE2 1 
ATOM   10707 C  CZ  . PHE B  1 613 ? -11.604 57.509 57.243 1.00 35.45 ? 613  PHE B CZ  1 
ATOM   10708 N  N   . SER B  1 614 ? -9.115  56.927 64.122 1.00 38.49 ? 614  SER B N   1 
ATOM   10709 C  CA  . SER B  1 614 ? -8.529  56.443 65.371 1.00 40.82 ? 614  SER B CA  1 
ATOM   10710 C  C   . SER B  1 614 ? -9.615  56.437 66.453 1.00 41.72 ? 614  SER B C   1 
ATOM   10711 O  O   . SER B  1 614 ? -9.819  55.445 67.158 1.00 41.07 ? 614  SER B O   1 
ATOM   10712 C  CB  . SER B  1 614 ? -7.397  57.359 65.812 1.00 41.52 ? 614  SER B CB  1 
ATOM   10713 O  OG  . SER B  1 614 ? -6.384  57.411 64.830 1.00 43.70 ? 614  SER B OG  1 
ATOM   10714 N  N   . LYS B  1 615 ? -10.316 57.559 66.562 1.00 42.77 ? 615  LYS B N   1 
ATOM   10715 C  CA  . LYS B  1 615 ? -11.384 57.699 67.538 1.00 43.60 ? 615  LYS B CA  1 
ATOM   10716 C  C   . LYS B  1 615 ? -12.530 56.712 67.346 1.00 44.06 ? 615  LYS B C   1 
ATOM   10717 O  O   . LYS B  1 615 ? -13.413 56.632 68.197 1.00 45.00 ? 615  LYS B O   1 
ATOM   10718 C  CB  . LYS B  1 615 ? -11.953 59.113 67.497 1.00 44.60 ? 615  LYS B CB  1 
ATOM   10719 C  CG  . LYS B  1 615 ? -10.973 60.199 67.887 1.00 46.90 ? 615  LYS B CG  1 
ATOM   10720 C  CD  . LYS B  1 615 ? -11.649 61.556 67.767 1.00 48.22 ? 615  LYS B CD  1 
ATOM   10721 C  CE  . LYS B  1 615 ? -10.701 62.696 68.133 1.00 49.16 ? 615  LYS B CE  1 
ATOM   10722 N  NZ  . LYS B  1 615 ? -11.380 64.019 67.954 1.00 48.50 ? 615  LYS B NZ  1 
ATOM   10723 N  N   . MET B  1 616 ? -12.549 55.967 66.242 1.00 43.65 ? 616  MET B N   1 
ATOM   10724 C  CA  . MET B  1 616 ? -13.647 55.019 66.041 1.00 42.03 ? 616  MET B CA  1 
ATOM   10725 C  C   . MET B  1 616 ? -13.530 53.794 66.941 1.00 41.12 ? 616  MET B C   1 
ATOM   10726 O  O   . MET B  1 616 ? -14.488 53.026 67.073 1.00 40.97 ? 616  MET B O   1 
ATOM   10727 C  CB  . MET B  1 616 ? -13.766 54.615 64.570 1.00 40.76 ? 616  MET B CB  1 
ATOM   10728 C  CG  . MET B  1 616 ? -14.070 55.821 63.686 1.00 40.17 ? 616  MET B CG  1 
ATOM   10729 S  SD  . MET B  1 616 ? -14.765 55.461 62.063 1.00 38.01 ? 616  MET B SD  1 
ATOM   10730 C  CE  . MET B  1 616 ? -15.439 57.020 61.659 1.00 36.75 ? 616  MET B CE  1 
ATOM   10731 N  N   . GLY B  1 617 ? -12.360 53.626 67.558 1.00 40.28 ? 617  GLY B N   1 
ATOM   10732 C  CA  . GLY B  1 617 ? -12.150 52.535 68.504 1.00 38.88 ? 617  GLY B CA  1 
ATOM   10733 C  C   . GLY B  1 617 ? -11.674 51.175 68.035 1.00 39.14 ? 617  GLY B C   1 
ATOM   10734 O  O   . GLY B  1 617 ? -11.240 50.359 68.852 1.00 40.57 ? 617  GLY B O   1 
ATOM   10735 N  N   . PHE B  1 618 ? -11.758 50.901 66.736 1.00 38.12 ? 618  PHE B N   1 
ATOM   10736 C  CA  . PHE B  1 618 ? -11.308 49.610 66.217 1.00 36.42 ? 618  PHE B CA  1 
ATOM   10737 C  C   . PHE B  1 618 ? -9.999  49.735 65.414 1.00 35.13 ? 618  PHE B C   1 
ATOM   10738 O  O   . PHE B  1 618 ? -9.666  48.886 64.591 1.00 34.79 ? 618  PHE B O   1 
ATOM   10739 C  CB  . PHE B  1 618 ? -12.420 48.969 65.366 1.00 35.79 ? 618  PHE B CB  1 
ATOM   10740 C  CG  . PHE B  1 618 ? -13.036 49.900 64.365 1.00 36.32 ? 618  PHE B CG  1 
ATOM   10741 C  CD1 . PHE B  1 618 ? -12.298 50.380 63.283 1.00 36.50 ? 618  PHE B CD1 1 
ATOM   10742 C  CD2 . PHE B  1 618 ? -14.361 50.295 64.496 1.00 35.84 ? 618  PHE B CD2 1 
ATOM   10743 C  CE1 . PHE B  1 618 ? -12.876 51.240 62.341 1.00 35.94 ? 618  PHE B CE1 1 
ATOM   10744 C  CE2 . PHE B  1 618 ? -14.943 51.151 63.564 1.00 35.77 ? 618  PHE B CE2 1 
ATOM   10745 C  CZ  . PHE B  1 618 ? -14.197 51.626 62.481 1.00 35.44 ? 618  PHE B CZ  1 
ATOM   10746 N  N   . VAL B  1 619 ? -9.246  50.789 65.687 1.00 33.73 ? 619  VAL B N   1 
ATOM   10747 C  CA  . VAL B  1 619 ? -8.001  51.009 64.984 1.00 32.72 ? 619  VAL B CA  1 
ATOM   10748 C  C   . VAL B  1 619 ? -6.848  51.087 65.964 1.00 32.81 ? 619  VAL B C   1 
ATOM   10749 O  O   . VAL B  1 619 ? -6.954  51.701 67.020 1.00 33.11 ? 619  VAL B O   1 
ATOM   10750 C  CB  . VAL B  1 619 ? -8.038  52.323 64.153 1.00 32.15 ? 619  VAL B CB  1 
ATOM   10751 C  CG1 . VAL B  1 619 ? -6.654  52.609 63.552 1.00 31.09 ? 619  VAL B CG1 1 
ATOM   10752 C  CG2 . VAL B  1 619 ? -9.069  52.208 63.038 1.00 30.66 ? 619  VAL B CG2 1 
ATOM   10753 N  N   . ASP B  1 620 ? -5.750  50.448 65.589 1.00 32.89 ? 620  ASP B N   1 
ATOM   10754 C  CA  . ASP B  1 620 ? -4.521  50.412 66.368 1.00 32.78 ? 620  ASP B CA  1 
ATOM   10755 C  C   . ASP B  1 620 ? -3.702  51.652 66.005 1.00 33.78 ? 620  ASP B C   1 
ATOM   10756 O  O   . ASP B  1 620 ? -3.061  51.699 64.951 1.00 33.50 ? 620  ASP B O   1 
ATOM   10757 C  CB  . ASP B  1 620 ? -3.749  49.142 66.004 1.00 31.88 ? 620  ASP B CB  1 
ATOM   10758 C  CG  . ASP B  1 620 ? -2.455  49.008 66.772 1.00 31.36 ? 620  ASP B CG  1 
ATOM   10759 O  OD1 . ASP B  1 620 ? -2.095  49.964 67.496 1.00 29.98 ? 620  ASP B OD1 1 
ATOM   10760 O  OD2 . ASP B  1 620 ? -1.801  47.948 66.639 1.00 30.79 ? 620  ASP B OD2 1 
ATOM   10761 N  N   . ASN B  1 621 ? -3.716  52.659 66.867 1.00 35.54 ? 621  ASN B N   1 
ATOM   10762 C  CA  . ASN B  1 621 ? -2.983  53.887 66.589 1.00 37.75 ? 621  ASN B CA  1 
ATOM   10763 C  C   . ASN B  1 621 ? -1.482  53.715 66.356 1.00 37.71 ? 621  ASN B C   1 
ATOM   10764 O  O   . ASN B  1 621 ? -0.817  54.632 65.863 1.00 38.26 ? 621  ASN B O   1 
ATOM   10765 C  CB  . ASN B  1 621 ? -3.211  54.912 67.707 1.00 41.43 ? 621  ASN B CB  1 
ATOM   10766 C  CG  . ASN B  1 621 ? -4.565  55.605 67.596 1.00 45.81 ? 621  ASN B CG  1 
ATOM   10767 O  OD1 . ASN B  1 621 ? -4.687  56.817 67.852 1.00 48.62 ? 621  ASN B OD1 1 
ATOM   10768 N  ND2 . ASN B  1 621 ? -5.594  54.841 67.216 1.00 47.06 ? 621  ASN B ND2 1 
ATOM   10769 N  N   . LYS B  1 622 ? -0.942  52.550 66.702 1.00 36.24 ? 622  LYS B N   1 
ATOM   10770 C  CA  . LYS B  1 622 ? 0.486   52.315 66.521 1.00 34.86 ? 622  LYS B CA  1 
ATOM   10771 C  C   . LYS B  1 622 ? 0.760   51.799 65.123 1.00 33.27 ? 622  LYS B C   1 
ATOM   10772 O  O   . LYS B  1 622 ? 1.904   51.795 64.665 1.00 32.17 ? 622  LYS B O   1 
ATOM   10773 C  CB  . LYS B  1 622 ? 1.013   51.303 67.556 1.00 36.64 ? 622  LYS B CB  1 
ATOM   10774 C  CG  . LYS B  1 622 ? 0.903   51.767 69.012 1.00 39.29 ? 622  LYS B CG  1 
ATOM   10775 C  CD  . LYS B  1 622 ? 1.482   50.735 70.007 1.00 42.31 ? 622  LYS B CD  1 
ATOM   10776 C  CE  . LYS B  1 622 ? 0.807   49.333 69.907 1.00 44.28 ? 622  LYS B CE  1 
ATOM   10777 N  NZ  . LYS B  1 622 ? -0.634  49.252 70.343 1.00 45.33 ? 622  LYS B NZ  1 
ATOM   10778 N  N   . ARG B  1 623 ? -0.293  51.355 64.445 1.00 30.73 ? 623  ARG B N   1 
ATOM   10779 C  CA  . ARG B  1 623 ? -0.116  50.832 63.110 1.00 29.20 ? 623  ARG B CA  1 
ATOM   10780 C  C   . ARG B  1 623 ? -1.015  51.485 62.070 1.00 26.86 ? 623  ARG B C   1 
ATOM   10781 O  O   . ARG B  1 623 ? -1.924  50.861 61.538 1.00 25.16 ? 623  ARG B O   1 
ATOM   10782 C  CB  . ARG B  1 623 ? -0.303  49.310 63.122 1.00 30.55 ? 623  ARG B CB  1 
ATOM   10783 C  CG  . ARG B  1 623 ? 0.783   48.581 63.926 1.00 31.58 ? 623  ARG B CG  1 
ATOM   10784 C  CD  . ARG B  1 623 ? 0.184   47.420 64.696 1.00 33.45 ? 623  ARG B CD  1 
ATOM   10785 N  NE  . ARG B  1 623 ? 0.169   46.180 63.939 1.00 35.13 ? 623  ARG B NE  1 
ATOM   10786 C  CZ  . ARG B  1 623 ? -0.795  45.269 64.029 1.00 36.39 ? 623  ARG B CZ  1 
ATOM   10787 N  NH1 . ARG B  1 623 ? -1.832  45.477 64.844 1.00 36.65 ? 623  ARG B NH1 1 
ATOM   10788 N  NH2 . ARG B  1 623 ? -0.714  44.147 63.320 1.00 34.57 ? 623  ARG B NH2 1 
ATOM   10789 N  N   . ILE B  1 624 ? -0.756  52.760 61.802 1.00 26.29 ? 624  ILE B N   1 
ATOM   10790 C  CA  . ILE B  1 624 ? -1.499  53.492 60.787 1.00 26.01 ? 624  ILE B CA  1 
ATOM   10791 C  C   . ILE B  1 624 ? -0.538  53.880 59.656 1.00 25.45 ? 624  ILE B C   1 
ATOM   10792 O  O   . ILE B  1 624 ? 0.440   54.594 59.870 1.00 24.38 ? 624  ILE B O   1 
ATOM   10793 C  CB  . ILE B  1 624 ? -2.128  54.749 61.348 1.00 26.22 ? 624  ILE B CB  1 
ATOM   10794 C  CG1 . ILE B  1 624 ? -3.090  54.377 62.482 1.00 27.03 ? 624  ILE B CG1 1 
ATOM   10795 C  CG2 . ILE B  1 624 ? -2.879  55.470 60.232 1.00 25.36 ? 624  ILE B CG2 1 
ATOM   10796 C  CD1 . ILE B  1 624 ? -3.809  55.569 63.081 1.00 26.85 ? 624  ILE B CD1 1 
ATOM   10797 N  N   . ALA B  1 625 ? -0.836  53.394 58.458 1.00 23.95 ? 625  ALA B N   1 
ATOM   10798 C  CA  . ALA B  1 625 ? -0.013  53.653 57.290 1.00 22.59 ? 625  ALA B CA  1 
ATOM   10799 C  C   . ALA B  1 625 ? -0.798  54.438 56.243 1.00 23.31 ? 625  ALA B C   1 
ATOM   10800 O  O   . ALA B  1 625 ? -2.033  54.581 56.319 1.00 23.68 ? 625  ALA B O   1 
ATOM   10801 C  CB  . ALA B  1 625 ? 0.485   52.320 56.697 1.00 20.50 ? 625  ALA B CB  1 
ATOM   10802 N  N   . ILE B  1 626 ? -0.072  54.953 55.265 1.00 21.50 ? 626  ILE B N   1 
ATOM   10803 C  CA  . ILE B  1 626 ? -0.687  55.719 54.198 1.00 22.09 ? 626  ILE B CA  1 
ATOM   10804 C  C   . ILE B  1 626 ? 0.059   55.425 52.887 1.00 22.20 ? 626  ILE B C   1 
ATOM   10805 O  O   . ILE B  1 626 ? 1.269   55.165 52.890 1.00 22.17 ? 626  ILE B O   1 
ATOM   10806 C  CB  . ILE B  1 626 ? -0.649  57.231 54.540 1.00 21.74 ? 626  ILE B CB  1 
ATOM   10807 C  CG1 . ILE B  1 626 ? -1.324  58.042 53.427 1.00 21.41 ? 626  ILE B CG1 1 
ATOM   10808 C  CG2 . ILE B  1 626 ? 0.792   57.683 54.790 1.00 19.87 ? 626  ILE B CG2 1 
ATOM   10809 C  CD1 . ILE B  1 626 ? -1.335  59.540 53.700 1.00 21.44 ? 626  ILE B CD1 1 
ATOM   10810 N  N   . TRP B  1 627 ? -0.676  55.404 51.779 1.00 21.71 ? 627  TRP B N   1 
ATOM   10811 C  CA  . TRP B  1 627 ? -0.078  55.152 50.476 1.00 20.87 ? 627  TRP B CA  1 
ATOM   10812 C  C   . TRP B  1 627 ? -0.963  55.710 49.382 1.00 21.23 ? 627  TRP B C   1 
ATOM   10813 O  O   . TRP B  1 627 ? -2.181  55.844 49.552 1.00 21.92 ? 627  TRP B O   1 
ATOM   10814 C  CB  . TRP B  1 627 ? 0.161   53.650 50.237 1.00 20.12 ? 627  TRP B CB  1 
ATOM   10815 C  CG  . TRP B  1 627 ? -0.904  52.955 49.436 1.00 19.30 ? 627  TRP B CG  1 
ATOM   10816 C  CD1 . TRP B  1 627 ? -2.118  52.518 49.891 1.00 19.92 ? 627  TRP B CD1 1 
ATOM   10817 C  CD2 . TRP B  1 627 ? -0.854  52.606 48.040 1.00 19.05 ? 627  TRP B CD2 1 
ATOM   10818 N  NE1 . TRP B  1 627 ? -2.819  51.917 48.875 1.00 19.81 ? 627  TRP B NE1 1 
ATOM   10819 C  CE2 . TRP B  1 627 ? -2.070  51.958 47.728 1.00 19.24 ? 627  TRP B CE2 1 
ATOM   10820 C  CE3 . TRP B  1 627 ? 0.100   52.779 47.025 1.00 17.94 ? 627  TRP B CE3 1 
ATOM   10821 C  CZ2 . TRP B  1 627 ? -2.358  51.479 46.442 1.00 19.93 ? 627  TRP B CZ2 1 
ATOM   10822 C  CZ3 . TRP B  1 627 ? -0.184  52.303 45.746 1.00 16.47 ? 627  TRP B CZ3 1 
ATOM   10823 C  CH2 . TRP B  1 627 ? -1.400  51.662 45.466 1.00 19.14 ? 627  TRP B CH2 1 
ATOM   10824 N  N   . GLY B  1 628 ? -0.354  56.090 48.227 1.00 18.33 ? 628  GLY B N   1 
ATOM   10825 C  CA  . GLY B  1 628 ? -1.073  56.688 47.105 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   56.691 45.885 1.00 14.54 ? 628  GLY B O   1 
ATOM   10828 N  N   . TRP B  1 629 ? -0.853  56.934 44.730 1.00 17.61 ? 629  TRP B N   1 
ATOM   10829 C  CA  . TRP B  1 629 ? -0.190  56.973 43.452 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 ? -1.583  58.791 42.860 1.00 16.73 ? 629  TRP B O   1 
ATOM   10832 C  CB  . TRP B  1 629 ? -0.665  55.766 42.645 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 17.90 ? 630  SER B N   1 
ATOM   10843 C  CA  . SER B  1 630 ? 0.269   60.101 41.335 1.00 17.20 ? 630  SER B CA  1 
ATOM   10844 C  C   . SER B  1 630 ? 0.000   61.253 42.299 1.00 17.14 ? 630  SER B C   1 
ATOM   10845 O  O   . SER B  1 630 ? 0.824   61.555 43.155 1.00 18.69 ? 630  SER B O   1 
ATOM   10846 C  CB  . SER B  1 630 ? -0.924  59.913 40.384 1.00 17.02 ? 630  SER B CB  1 
ATOM   10847 O  OG  . SER B  1 630 ? -1.043  61.000 39.487 1.00 19.43 ? 630  SER B OG  1 
ATOM   10848 N  N   . TYR B  1 631 ? -1.152  61.882 42.166 1.00 15.91 ? 631  TYR B N   1 
ATOM   10849 C  CA  . TYR B  1 631 ? -1.477  62.950 43.104 1.00 15.71 ? 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 ? -1.159  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 15.00 ? 631  TYR B CB  1 
ATOM   10853 C  CG  . TYR B  1 631 ? -3.030  64.991 43.427 1.00 15.77 ? 631  TYR B CG  1 
ATOM   10854 C  CD1 . TYR B  1 631 ? -3.298  65.160 44.783 1.00 16.64 ? 631  TYR B CD1 1 
ATOM   10855 C  CD2 . TYR B  1 631 ? -2.934  66.135 42.630 1.00 17.96 ? 631  TYR B CD2 1 
ATOM   10856 C  CE1 . TYR B  1 631 ? -3.472  66.437 45.344 1.00 18.69 ? 631  TYR B CE1 1 
ATOM   10857 C  CE2 . TYR B  1 631 ? -3.102  67.416 43.170 1.00 18.37 ? 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 ? -3.548  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 ? -1.859  60.260 45.734 1.00 16.46 ? 632  GLY B CA  1 
ATOM   10862 C  C   . GLY B  1 632 ? -0.454  60.146 46.359 1.00 16.39 ? 632  GLY B C   1 
ATOM   10863 O  O   . GLY B  1 632 ? -0.320  60.269 47.587 1.00 16.28 ? 632  GLY B O   1 
ATOM   10864 N  N   . GLY B  1 633 ? 0.583   59.907 45.543 1.00 18.15 ? 633  GLY B N   1 
ATOM   10865 C  CA  . GLY B  1 633 ? 1.960   59.803 45.999 1.00 16.39 ? 633  GLY B CA  1 
ATOM   10866 C  C   . GLY B  1 633 ? 2.386   61.140 46.594 1.00 17.01 ? 633  GLY B C   1 
ATOM   10867 O  O   . GLY B  1 633 ? 3.089   61.201 47.599 1.00 17.72 ? 633  GLY B O   1 
ATOM   10868 N  N   . TYR B  1 634 ? 1.950   62.225 45.968 1.00 17.04 ? 634  TYR B N   1 
ATOM   10869 C  CA  . TYR B  1 634 ? 2.255   63.558 46.453 1.00 17.12 ? 634  TYR B CA  1 
ATOM   10870 C  C   . TYR B  1 634 ? 1.640   63.757 47.845 1.00 18.58 ? 634  TYR B C   1 
ATOM   10871 O  O   . TYR B  1 634 ? 2.340   64.109 48.802 1.00 18.35 ? 634  TYR B O   1 
ATOM   10872 C  CB  . TYR B  1 634 ? 1.688   64.599 45.525 1.00 16.50 ? 634  TYR B CB  1 
ATOM   10873 C  CG  . TYR B  1 634 ? 1.708   66.024 46.003 1.00 16.06 ? 634  TYR B CG  1 
ATOM   10874 C  CD1 . TYR B  1 634 ? 2.912   66.678 46.248 1.00 17.46 ? 634  TYR B CD1 1 
ATOM   10875 C  CD2 . TYR B  1 634 ? 0.520   66.745 46.172 1.00 15.42 ? 634  TYR B CD2 1 
ATOM   10876 C  CE1 . TYR B  1 634 ? 2.943   68.019 46.638 1.00 18.11 ? 634  TYR B CE1 1 
ATOM   10877 C  CE2 . TYR B  1 634 ? 0.538   68.096 46.564 1.00 15.54 ? 634  TYR B CE2 1 
ATOM   10878 C  CZ  . TYR B  1 634 ? 1.758   68.725 46.784 1.00 17.14 ? 634  TYR B CZ  1 
ATOM   10879 O  OH  . TYR B  1 634 ? 1.796   70.042 47.172 1.00 15.49 ? 634  TYR B OH  1 
ATOM   10880 N  N   . VAL B  1 635 ? 0.336   63.509 47.958 1.00 18.63 ? 635  VAL B N   1 
ATOM   10881 C  CA  . VAL B  1 635 ? -0.349  63.703 49.237 1.00 19.18 ? 635  VAL B CA  1 
ATOM   10882 C  C   . VAL B  1 635 ? 0.284   62.846 50.323 1.00 19.49 ? 635  VAL B C   1 
ATOM   10883 O  O   . VAL B  1 635 ? 0.526   63.331 51.430 1.00 20.15 ? 635  VAL B O   1 
ATOM   10884 C  CB  . VAL B  1 635 ? -1.867  63.416 49.108 1.00 17.72 ? 635  VAL B CB  1 
ATOM   10885 C  CG1 . VAL B  1 635 ? -2.512  63.363 50.480 1.00 17.04 ? 635  VAL B CG1 1 
ATOM   10886 C  CG2 . VAL B  1 635 ? -2.522  64.525 48.277 1.00 16.52 ? 635  VAL B CG2 1 
ATOM   10887 N  N   . THR B  1 636 ? 0.554   61.587 49.997 1.00 19.39 ? 636  THR B N   1 
ATOM   10888 C  CA  . THR B  1 636 ? 1.196   60.659 50.922 1.00 20.90 ? 636  THR B CA  1 
ATOM   10889 C  C   . THR B  1 636 ? 2.505   61.254 51.441 1.00 21.91 ? 636  THR B C   1 
ATOM   10890 O  O   . THR B  1 636 ? 2.756   61.294 52.659 1.00 21.86 ? 636  THR B O   1 
ATOM   10891 C  CB  . THR B  1 636 ? 1.522   59.312 50.223 1.00 21.08 ? 636  THR B CB  1 
ATOM   10892 O  OG1 . THR B  1 636 ? 0.312   58.589 50.004 1.00 22.98 ? 636  THR B OG1 1 
ATOM   10893 C  CG2 . THR B  1 636 ? 2.447   58.458 51.072 1.00 22.11 ? 636  THR B CG2 1 
ATOM   10894 N  N   . SER B  1 637 ? 3.336   61.710 50.504 1.00 21.08 ? 637  SER B N   1 
ATOM   10895 C  CA  . SER B  1 637 ? 4.634   62.302 50.825 1.00 21.04 ? 637  SER B CA  1 
ATOM   10896 C  C   . SER B  1 637 ? 4.447   63.570 51.659 1.00 22.19 ? 637  SER B C   1 
ATOM   10897 O  O   . SER B  1 637 ? 5.163   63.776 52.636 1.00 21.87 ? 637  SER B O   1 
ATOM   10898 C  CB  . SER B  1 637 ? 5.400   62.627 49.533 1.00 19.86 ? 637  SER B CB  1 
ATOM   10899 O  OG  . SER B  1 637 ? 5.532   61.469 48.717 1.00 20.23 ? 637  SER B OG  1 
ATOM   10900 N  N   . MET B  1 638 ? 3.489   64.415 51.280 1.00 21.42 ? 638  MET B N   1 
ATOM   10901 C  CA  . MET B  1 638 ? 3.260   65.621 52.048 1.00 22.97 ? 638  MET B CA  1 
ATOM   10902 C  C   . MET B  1 638 ? 2.835   65.275 53.492 1.00 23.31 ? 638  MET B C   1 
ATOM   10903 O  O   . MET B  1 638 ? 3.277   65.913 54.472 1.00 21.98 ? 638  MET B O   1 
ATOM   10904 C  CB  . MET B  1 638 ? 2.217   66.489 51.352 1.00 22.61 ? 638  MET B CB  1 
ATOM   10905 C  CG  . MET B  1 638 ? 2.743   67.129 50.046 1.00 22.67 ? 638  MET B CG  1 
ATOM   10906 S  SD  . MET B  1 638 ? 3.984   68.407 50.331 1.00 24.62 ? 638  MET B SD  1 
ATOM   10907 C  CE  . MET B  1 638 ? 2.928   69.850 50.605 1.00 21.96 ? 638  MET B CE  1 
ATOM   10908 N  N   . VAL B  1 639 ? 1.992   64.259 53.618 1.00 22.50 ? 639  VAL B N   1 
ATOM   10909 C  CA  . VAL B  1 639 ? 1.532   63.817 54.926 1.00 23.44 ? 639  VAL B CA  1 
ATOM   10910 C  C   . VAL B  1 639 ? 2.681   63.209 55.731 1.00 23.23 ? 639  VAL B C   1 
ATOM   10911 O  O   . VAL B  1 639 ? 2.862   63.552 56.882 1.00 25.15 ? 639  VAL B O   1 
ATOM   10912 C  CB  . VAL B  1 639 ? 0.379   62.780 54.800 1.00 22.49 ? 639  VAL B CB  1 
ATOM   10913 C  CG1 . VAL B  1 639 ? 0.176   62.063 56.136 1.00 22.95 ? 639  VAL B CG1 1 
ATOM   10914 C  CG2 . VAL B  1 639 ? -0.909  63.485 54.398 1.00 21.31 ? 639  VAL B CG2 1 
ATOM   10915 N  N   . LEU B  1 640 ? 3.451   62.310 55.133 1.00 24.01 ? 640  LEU B N   1 
ATOM   10916 C  CA  . LEU B  1 640 ? 4.572   61.710 55.839 1.00 23.04 ? 640  LEU B CA  1 
ATOM   10917 C  C   . LEU B  1 640 ? 5.593   62.765 56.248 1.00 24.20 ? 640  LEU B C   1 
ATOM   10918 O  O   . LEU B  1 640 ? 6.350   62.572 57.196 1.00 24.56 ? 640  LEU B O   1 
ATOM   10919 C  CB  . LEU B  1 640 ? 5.234   60.650 54.970 1.00 22.66 ? 640  LEU B CB  1 
ATOM   10920 C  CG  . LEU B  1 640 ? 4.327   59.441 54.788 1.00 23.71 ? 640  LEU B CG  1 
ATOM   10921 C  CD1 . LEU B  1 640 ? 4.852   58.515 53.696 1.00 24.38 ? 640  LEU B CD1 1 
ATOM   10922 C  CD2 . LEU B  1 640 ? 4.238   58.718 56.106 1.00 22.98 ? 640  LEU B CD2 1 
ATOM   10923 N  N   . GLY B  1 641 ? 5.614   63.890 55.546 1.00 24.41 ? 641  GLY B N   1 
ATOM   10924 C  CA  . GLY B  1 641 ? 6.566   64.930 55.895 1.00 24.98 ? 641  GLY B CA  1 
ATOM   10925 C  C   . GLY B  1 641 ? 5.975   66.061 56.725 1.00 25.02 ? 641  GLY B C   1 
ATOM   10926 O  O   . GLY B  1 641 ? 6.645   67.055 56.983 1.00 23.81 ? 641  GLY B O   1 
ATOM   10927 N  N   . SER B  1 642 ? 4.728   65.916 57.164 1.00 24.88 ? 642  SER B N   1 
ATOM   10928 C  CA  . SER B  1 642 ? 4.086   66.976 57.943 1.00 24.50 ? 642  SER B CA  1 
ATOM   10929 C  C   . SER B  1 642 ? 4.473   67.013 59.421 1.00 25.34 ? 642  SER B C   1 
ATOM   10930 O  O   . SER B  1 642 ? 4.254   68.015 60.083 1.00 25.66 ? 642  SER B O   1 
ATOM   10931 C  CB  . SER B  1 642 ? 2.564   66.849 57.845 1.00 23.37 ? 642  SER B CB  1 
ATOM   10932 O  OG  . SER B  1 642 ? 2.103   65.744 58.599 1.00 23.79 ? 642  SER B OG  1 
ATOM   10933 N  N   . GLY B  1 643 ? 5.042   65.928 59.937 1.00 26.07 ? 643  GLY B N   1 
ATOM   10934 C  CA  . GLY B  1 643 ? 5.398   65.883 61.345 1.00 26.75 ? 643  GLY B CA  1 
ATOM   10935 C  C   . GLY B  1 643 ? 4.178   65.683 62.250 1.00 27.16 ? 643  GLY B C   1 
ATOM   10936 O  O   . GLY B  1 643 ? 4.222   66.005 63.436 1.00 26.23 ? 643  GLY B O   1 
ATOM   10937 N  N   . SER B  1 644 ? 3.090   65.134 61.708 1.00 26.52 ? 644  SER B N   1 
ATOM   10938 C  CA  . SER B  1 644 ? 1.869   64.916 62.495 1.00 25.61 ? 644  SER B CA  1 
ATOM   10939 C  C   . SER B  1 644 ? 1.981   63.808 63.535 1.00 26.20 ? 644  SER B C   1 
ATOM   10940 O  O   . SER B  1 644 ? 1.222   63.782 64.493 1.00 26.59 ? 644  SER B O   1 
ATOM   10941 C  CB  . SER B  1 644 ? 0.686   64.583 61.575 1.00 24.91 ? 644  SER B CB  1 
ATOM   10942 O  OG  . SER B  1 644 ? 0.642   63.192 61.279 1.00 21.95 ? 644  SER B OG  1 
ATOM   10943 N  N   . GLY B  1 645 ? 2.921   62.893 63.336 1.00 26.90 ? 645  GLY B N   1 
ATOM   10944 C  CA  . GLY B  1 645 ? 3.086   61.789 64.259 1.00 26.61 ? 645  GLY B CA  1 
ATOM   10945 C  C   . GLY B  1 645 ? 1.995   60.728 64.122 1.00 27.48 ? 645  GLY B C   1 
ATOM   10946 O  O   . GLY B  1 645 ? 2.048   59.684 64.785 1.00 27.81 ? 645  GLY B O   1 
ATOM   10947 N  N   . VAL B  1 646 ? 1.016   60.958 63.254 1.00 26.49 ? 646  VAL B N   1 
ATOM   10948 C  CA  . VAL B  1 646 ? -0.074  59.989 63.107 1.00 26.25 ? 646  VAL B CA  1 
ATOM   10949 C  C   . VAL B  1 646 ? 0.267   58.693 62.382 1.00 25.49 ? 646  VAL B C   1 
ATOM   10950 O  O   . VAL B  1 646 ? -0.175  57.609 62.777 1.00 24.89 ? 646  VAL B O   1 
ATOM   10951 C  CB  . VAL B  1 646 ? -1.308  60.646 62.414 1.00 26.02 ? 646  VAL B CB  1 
ATOM   10952 C  CG1 . VAL B  1 646 ? -2.434  59.621 62.226 1.00 25.12 ? 646  VAL B CG1 1 
ATOM   10953 C  CG2 . VAL B  1 646 ? -1.806  61.807 63.262 1.00 25.07 ? 646  VAL B CG2 1 
ATOM   10954 N  N   . PHE B  1 647 ? 1.077   58.792 61.336 1.00 25.32 ? 647  PHE B N   1 
ATOM   10955 C  CA  . PHE B  1 647 ? 1.413   57.610 60.547 1.00 24.47 ? 647  PHE B CA  1 
ATOM   10956 C  C   . PHE B  1 647 ? 2.772   56.997 60.869 1.00 25.69 ? 647  PHE B C   1 
ATOM   10957 O  O   . PHE B  1 647 ? 3.739   57.701 61.163 1.00 25.83 ? 647  PHE B O   1 
ATOM   10958 C  CB  . PHE B  1 647 ? 1.345   57.964 59.051 1.00 23.57 ? 647  PHE B CB  1 
ATOM   10959 C  CG  . PHE B  1 647 ? 0.028   58.562 58.637 1.00 21.33 ? 647  PHE B CG  1 
ATOM   10960 C  CD1 . PHE B  1 647 ? -0.982  57.770 58.107 1.00 21.36 ? 647  PHE B CD1 1 
ATOM   10961 C  CD2 . PHE B  1 647 ? -0.216  59.911 58.829 1.00 20.66 ? 647  PHE B CD2 1 
ATOM   10962 C  CE1 . PHE B  1 647 ? -2.217  58.323 57.777 1.00 20.86 ? 647  PHE B CE1 1 
ATOM   10963 C  CE2 . PHE B  1 647 ? -1.447  60.470 58.506 1.00 20.92 ? 647  PHE B CE2 1 
ATOM   10964 C  CZ  . PHE B  1 647 ? -2.445  59.678 57.978 1.00 19.92 ? 647  PHE B CZ  1 
ATOM   10965 N  N   . LYS B  1 648 ? 2.838   55.675 60.795 1.00 25.46 ? 648  LYS B N   1 
ATOM   10966 C  CA  . LYS B  1 648 ? 4.075   54.962 61.046 1.00 26.28 ? 648  LYS B CA  1 
ATOM   10967 C  C   . LYS B  1 648 ? 4.938   54.847 59.781 1.00 26.60 ? 648  LYS B C   1 
ATOM   10968 O  O   . LYS B  1 648 ? 6.155   55.021 59.837 1.00 25.41 ? 648  LYS B O   1 
ATOM   10969 C  CB  . LYS B  1 648 ? 3.768   53.564 61.582 1.00 26.93 ? 648  LYS B CB  1 
ATOM   10970 C  CG  . LYS B  1 648 ? 5.003   52.739 61.827 1.00 29.42 ? 648  LYS B CG  1 
ATOM   10971 C  CD  . LYS B  1 648 ? 4.664   51.420 62.452 1.00 31.17 ? 648  LYS B CD  1 
ATOM   10972 C  CE  . LYS B  1 648 ? 5.928   50.668 62.813 1.00 31.37 ? 648  LYS B CE  1 
ATOM   10973 N  NZ  . LYS B  1 648 ? 5.573   49.551 63.709 1.00 34.54 ? 648  LYS B NZ  1 
ATOM   10974 N  N   . CYS B  1 649 ? 4.305   54.547 58.649 1.00 26.80 ? 649  CYS B N   1 
ATOM   10975 C  CA  . CYS B  1 649 ? 5.022   54.390 57.387 1.00 27.75 ? 649  CYS B CA  1 
ATOM   10976 C  C   . CYS B  1 649 ? 4.110   54.740 56.202 1.00 26.83 ? 649  CYS B C   1 
ATOM   10977 O  O   . CYS B  1 649 ? 2.897   54.925 56.361 1.00 25.94 ? 649  CYS B O   1 
ATOM   10978 C  CB  . CYS B  1 649 ? 5.502   52.951 57.243 1.00 29.48 ? 649  CYS B CB  1 
ATOM   10979 S  SG  . CYS B  1 649 ? 4.096   51.820 57.332 1.00 35.71 ? 649  CYS B SG  1 
ATOM   10980 N  N   . GLY B  1 650 ? 4.697   54.823 55.011 1.00 24.56 ? 650  GLY B N   1 
ATOM   10981 C  CA  . GLY B  1 650 ? 3.914   55.144 53.835 1.00 22.10 ? 650  GLY B CA  1 
ATOM   10982 C  C   . GLY B  1 650 ? 4.643   54.841 52.541 1.00 21.59 ? 650  GLY B C   1 
ATOM   10983 O  O   . GLY B  1 650 ? 5.879   54.783 52.501 1.00 21.09 ? 650  GLY B O   1 
ATOM   10984 N  N   . ILE B  1 651 ? 3.866   54.652 51.478 1.00 19.05 ? 651  ILE B N   1 
ATOM   10985 C  CA  . ILE B  1 651 ? 4.402   54.347 50.161 1.00 18.08 ? 651  ILE B CA  1 
ATOM   10986 C  C   . ILE B  1 651 ? 3.927   55.365 49.117 1.00 18.55 ? 651  ILE B C   1 
ATOM   10987 O  O   . ILE B  1 651 ? 2.715   55.572 48.938 1.00 18.35 ? 651  ILE B O   1 
ATOM   10988 C  CB  . ILE B  1 651 ? 3.941   52.965 49.681 1.00 17.66 ? 651  ILE B CB  1 
ATOM   10989 C  CG1 . ILE B  1 651 ? 4.289   51.907 50.734 1.00 17.40 ? 651  ILE B CG1 1 
ATOM   10990 C  CG2 . ILE B  1 651 ? 4.601   52.641 48.336 1.00 13.73 ? 651  ILE B CG2 1 
ATOM   10991 C  CD1 . ILE B  1 651 ? 3.737   50.529 50.408 1.00 15.44 ? 651  ILE B CD1 1 
ATOM   10992 N  N   . ALA B  1 652 ? 4.877   55.996 48.431 1.00 16.83 ? 652  ALA B N   1 
ATOM   10993 C  CA  . ALA B  1 652 ? 4.527   56.950 47.385 1.00 16.92 ? 652  ALA B CA  1 
ATOM   10994 C  C   . ALA B  1 652 ? 4.957   56.370 46.040 1.00 15.99 ? 652  ALA B C   1 
ATOM   10995 O  O   . ALA B  1 652 ? 6.125   56.054 45.834 1.00 16.14 ? 652  ALA B O   1 
ATOM   10996 C  CB  . ALA B  1 652 ? 5.194   58.315 47.635 1.00 15.60 ? 652  ALA B CB  1 
ATOM   10997 N  N   . VAL B  1 653 ? 4.001   56.202 45.134 1.00 16.98 ? 653  VAL B N   1 
ATOM   10998 C  CA  . VAL B  1 653 ? 4.311   55.661 43.809 1.00 17.28 ? 653  VAL B CA  1 
ATOM   10999 C  C   . VAL B  1 653 ? 4.134   56.752 42.758 1.00 16.01 ? 653  VAL B C   1 
ATOM   11000 O  O   . VAL B  1 653 ? 3.063   57.353 42.652 1.00 14.89 ? 653  VAL B O   1 
ATOM   11001 C  CB  . VAL B  1 653 ? 3.389   54.452 43.439 1.00 17.44 ? 653  VAL B CB  1 
ATOM   11002 C  CG1 . VAL B  1 653 ? 3.848   53.831 42.109 1.00 14.88 ? 653  VAL B CG1 1 
ATOM   11003 C  CG2 . VAL B  1 653 ? 3.410   53.391 44.570 1.00 16.53 ? 653  VAL B CG2 1 
ATOM   11004 N  N   . ALA B  1 654 ? 5.191   56.988 41.981 1.00 15.57 ? 654  ALA B N   1 
ATOM   11005 C  CA  . ALA B  1 654 ? 5.193   58.008 40.924 1.00 15.85 ? 654  ALA B CA  1 
ATOM   11006 C  C   . ALA B  1 654 ? 4.582   59.321 41.415 1.00 15.95 ? 654  ALA B C   1 
ATOM   11007 O  O   . ALA B  1 654 ? 3.638   59.847 40.831 1.00 18.89 ? 654  ALA B O   1 
ATOM   11008 C  CB  . ALA B  1 654 ? 4.439   57.500 39.697 1.00 15.44 ? 654  ALA B CB  1 
ATOM   11009 N  N   . PRO B  1 655 ? 5.115   59.867 42.504 1.00 14.70 ? 655  PRO B N   1 
ATOM   11010 C  CA  . PRO B  1 655 ? 4.568   61.118 43.021 1.00 15.39 ? 655  PRO B CA  1 
ATOM   11011 C  C   . PRO B  1 655 ? 5.017   62.392 42.325 1.00 15.21 ? 655  PRO B C   1 
ATOM   11012 O  O   . PRO B  1 655 ? 6.040   62.430 41.641 1.00 14.53 ? 655  PRO B O   1 
ATOM   11013 C  CB  . PRO B  1 655 ? 5.050   61.116 44.469 1.00 14.71 ? 655  PRO B CB  1 
ATOM   11014 C  CG  . PRO B  1 655 ? 6.406   60.498 44.335 1.00 12.86 ? 655  PRO B CG  1 
ATOM   11015 C  CD  . PRO B  1 655 ? 6.112   59.312 43.433 1.00 13.72 ? 655  PRO B CD  1 
ATOM   11016 N  N   . VAL B  1 656 ? 4.214   63.431 42.507 1.00 15.12 ? 656  VAL B N   1 
ATOM   11017 C  CA  . VAL B  1 656 ? 4.564   64.755 42.043 1.00 16.64 ? 656  VAL B CA  1 
ATOM   11018 C  C   . VAL B  1 656 ? 5.319   65.232 43.297 1.00 16.95 ? 656  VAL B C   1 
ATOM   11019 O  O   . VAL B  1 656 ? 4.936   64.869 44.413 1.00 15.05 ? 656  VAL B O   1 
ATOM   11020 C  CB  . VAL B  1 656 ? 3.303   65.610 41.827 1.00 17.84 ? 656  VAL B CB  1 
ATOM   11021 C  CG1 . VAL B  1 656 ? 3.645   67.110 41.799 1.00 15.83 ? 656  VAL B CG1 1 
ATOM   11022 C  CG2 . VAL B  1 656 ? 2.655   65.195 40.516 1.00 17.22 ? 656  VAL B CG2 1 
ATOM   11023 N  N   . SER B  1 657 ? 6.393   65.990 43.135 1.00 18.68 ? 657  SER B N   1 
ATOM   11024 C  CA  . SER B  1 657 ? 7.117   66.470 44.298 1.00 20.11 ? 657  SER B CA  1 
ATOM   11025 C  C   . SER B  1 657 ? 7.156   67.997 44.352 1.00 20.86 ? 657  SER B C   1 
ATOM   11026 O  O   . SER B  1 657 ? 7.329   68.578 45.427 1.00 20.84 ? 657  SER B O   1 
ATOM   11027 C  CB  . SER B  1 657 ? 8.534   65.890 44.327 1.00 21.71 ? 657  SER B CB  1 
ATOM   11028 O  OG  . SER B  1 657 ? 9.287   66.332 43.225 1.00 23.05 ? 657  SER B OG  1 
ATOM   11029 N  N   . ARG B  1 658 ? 7.016   68.648 43.200 1.00 20.92 ? 658  ARG B N   1 
ATOM   11030 C  CA  . ARG B  1 658 ? 6.965   70.111 43.150 1.00 21.00 ? 658  ARG B CA  1 
ATOM   11031 C  C   . ARG B  1 658 ? 6.194   70.473 41.900 1.00 19.06 ? 658  ARG B C   1 
ATOM   11032 O  O   . ARG B  1 658 ? 6.483   69.968 40.814 1.00 16.82 ? 658  ARG B O   1 
ATOM   11033 C  CB  . ARG B  1 658 ? 8.357   70.778 43.160 1.00 24.01 ? 658  ARG B CB  1 
ATOM   11034 C  CG  . ARG B  1 658 ? 9.118   70.881 41.846 1.00 29.45 ? 658  ARG B CG  1 
ATOM   11035 C  CD  . ARG B  1 658 ? 9.817   72.268 41.648 1.00 30.35 ? 658  ARG B CD  1 
ATOM   11036 N  NE  . ARG B  1 658 ? 10.391  72.864 42.852 1.00 29.14 ? 658  ARG B NE  1 
ATOM   11037 C  CZ  . ARG B  1 658 ? 11.114  73.993 42.876 1.00 30.29 ? 658  ARG B CZ  1 
ATOM   11038 N  NH1 . ARG B  1 658 ? 11.379  74.665 41.755 1.00 28.33 ? 658  ARG B NH1 1 
ATOM   11039 N  NH2 . ARG B  1 658 ? 11.546  74.480 44.038 1.00 26.91 ? 658  ARG B NH2 1 
ATOM   11040 N  N   . TRP B  1 659 ? 5.216   71.360 42.063 1.00 18.26 ? 659  TRP B N   1 
ATOM   11041 C  CA  . TRP B  1 659 ? 4.342   71.721 40.958 1.00 18.70 ? 659  TRP B CA  1 
ATOM   11042 C  C   . TRP B  1 659 ? 4.997   72.285 39.714 1.00 18.84 ? 659  TRP B C   1 
ATOM   11043 O  O   . TRP B  1 659 ? 4.476   72.104 38.619 1.00 19.37 ? 659  TRP B O   1 
ATOM   11044 C  CB  . TRP B  1 659 ? 3.187   72.584 41.477 1.00 16.38 ? 659  TRP B CB  1 
ATOM   11045 C  CG  . TRP B  1 659 ? 2.267   71.710 42.306 1.00 17.96 ? 659  TRP B CG  1 
ATOM   11046 C  CD1 . TRP B  1 659 ? 2.112   71.735 43.671 1.00 17.77 ? 659  TRP B CD1 1 
ATOM   11047 C  CD2 . TRP B  1 659 ? 1.519   70.561 41.849 1.00 17.10 ? 659  TRP B CD2 1 
ATOM   11048 N  NE1 . TRP B  1 659 ? 1.331   70.675 44.087 1.00 16.20 ? 659  TRP B NE1 1 
ATOM   11049 C  CE2 . TRP B  1 659 ? 0.956   69.939 42.996 1.00 16.90 ? 659  TRP B CE2 1 
ATOM   11050 C  CE3 . TRP B  1 659 ? 1.279   69.996 40.587 1.00 16.83 ? 659  TRP B CE3 1 
ATOM   11051 C  CZ2 . TRP B  1 659 ? 0.171   68.778 42.919 1.00 16.14 ? 659  TRP B CZ2 1 
ATOM   11052 C  CZ3 . TRP B  1 659 ? 0.494   68.836 40.506 1.00 16.25 ? 659  TRP B CZ3 1 
ATOM   11053 C  CH2 . TRP B  1 659 ? -0.049  68.242 41.672 1.00 17.47 ? 659  TRP B CH2 1 
ATOM   11054 N  N   . GLU B  1 660 ? 6.151   72.927 39.863 1.00 18.57 ? 660  GLU B N   1 
ATOM   11055 C  CA  . GLU B  1 660 ? 6.850   73.440 38.702 1.00 18.65 ? 660  GLU B CA  1 
ATOM   11056 C  C   . GLU B  1 660 ? 7.356   72.324 37.777 1.00 17.55 ? 660  GLU B C   1 
ATOM   11057 O  O   . GLU B  1 660 ? 7.767   72.616 36.658 1.00 18.44 ? 660  GLU B O   1 
ATOM   11058 C  CB  . GLU B  1 660 ? 8.020   74.370 39.123 1.00 19.04 ? 660  GLU B CB  1 
ATOM   11059 C  CG  . GLU B  1 660 ? 7.562   75.802 39.416 1.00 21.59 ? 660  GLU B CG  1 
ATOM   11060 C  CD  . GLU B  1 660 ? 8.468   76.574 40.357 1.00 24.58 ? 660  GLU B CD  1 
ATOM   11061 O  OE1 . GLU B  1 660 ? 8.510   76.258 41.569 1.00 25.41 ? 660  GLU B OE1 1 
ATOM   11062 O  OE2 . GLU B  1 660 ? 9.150   77.515 39.888 1.00 27.54 ? 660  GLU B OE2 1 
ATOM   11063 N  N   . TYR B  1 661 ? 7.346   71.065 38.222 1.00 16.10 ? 661  TYR B N   1 
ATOM   11064 C  CA  . TYR B  1 661 ? 7.801   69.957 37.346 1.00 16.34 ? 661  TYR B CA  1 
ATOM   11065 C  C   . TYR B  1 661 ? 6.631   69.342 36.557 1.00 15.83 ? 661  TYR B C   1 
ATOM   11066 O  O   . TYR B  1 661 ? 6.851   68.553 35.632 1.00 14.98 ? 661  TYR B O   1 
ATOM   11067 C  CB  . TYR B  1 661 ? 8.433   68.797 38.125 1.00 16.66 ? 661  TYR B CB  1 
ATOM   11068 C  CG  . TYR B  1 661 ? 9.661   69.115 38.953 1.00 19.63 ? 661  TYR B CG  1 
ATOM   11069 C  CD1 . TYR B  1 661 ? 10.493  70.195 38.644 1.00 19.99 ? 661  TYR B CD1 1 
ATOM   11070 C  CD2 . TYR B  1 661 ? 10.003  68.313 40.041 1.00 19.56 ? 661  TYR B CD2 1 
ATOM   11071 C  CE1 . TYR B  1 661 ? 11.636  70.468 39.411 1.00 21.42 ? 661  TYR B CE1 1 
ATOM   11072 C  CE2 . TYR B  1 661 ? 11.136  68.571 40.805 1.00 21.29 ? 661  TYR B CE2 1 
ATOM   11073 C  CZ  . TYR B  1 661 ? 11.943  69.648 40.490 1.00 21.22 ? 661  TYR B CZ  1 
ATOM   11074 O  OH  . TYR B  1 661 ? 13.043  69.908 41.265 1.00 22.56 ? 661  TYR B OH  1 
ATOM   11075 N  N   . TYR B  1 662 ? 5.395   69.676 36.929 1.00 13.87 ? 662  TYR B N   1 
ATOM   11076 C  CA  . TYR B  1 662 ? 4.262   69.100 36.230 1.00 15.67 ? 662  TYR B CA  1 
ATOM   11077 C  C   . TYR B  1 662 ? 3.820   69.979 35.067 1.00 15.21 ? 662  TYR B C   1 
ATOM   11078 O  O   . TYR B  1 662 ? 4.257   71.120 34.961 1.00 16.31 ? 662  TYR B O   1 
ATOM   11079 C  CB  . TYR B  1 662 ? 3.106   68.819 37.198 1.00 12.88 ? 662  TYR B CB  1 
ATOM   11080 C  CG  . TYR B  1 662 ? 2.202   67.756 36.639 1.00 13.82 ? 662  TYR B CG  1 
ATOM   11081 C  CD1 . TYR B  1 662 ? 2.707   66.494 36.319 1.00 13.11 ? 662  TYR B CD1 1 
ATOM   11082 C  CD2 . TYR B  1 662 ? 0.877   68.046 36.309 1.00 13.98 ? 662  TYR B CD2 1 
ATOM   11083 C  CE1 . TYR B  1 662 ? 1.922   65.554 35.663 1.00 14.79 ? 662  TYR B CE1 1 
ATOM   11084 C  CE2 . TYR B  1 662 ? 0.080   67.117 35.653 1.00 13.46 ? 662  TYR B CE2 1 
ATOM   11085 C  CZ  . TYR B  1 662 ? 0.600   65.891 35.327 1.00 14.64 ? 662  TYR B CZ  1 
ATOM   11086 O  OH  . TYR B  1 662 ? -0.174  65.032 34.599 1.00 14.54 ? 662  TYR B OH  1 
ATOM   11087 N  N   . ASP B  1 663 ? 2.961   69.479 34.188 1.00 15.98 ? 663  ASP B N   1 
ATOM   11088 C  CA  . ASP B  1 663 ? 2.571   70.302 33.032 1.00 16.36 ? 663  ASP B CA  1 
ATOM   11089 C  C   . ASP B  1 663 ? 1.701   71.540 33.290 1.00 17.01 ? 663  ASP B C   1 
ATOM   11090 O  O   . ASP B  1 663 ? 0.963   71.621 34.269 1.00 17.14 ? 663  ASP B O   1 
ATOM   11091 C  CB  . ASP B  1 663 ? 1.930   69.426 31.943 1.00 16.58 ? 663  ASP B CB  1 
ATOM   11092 C  CG  . ASP B  1 663 ? 0.549   68.931 32.312 1.00 18.03 ? 663  ASP B CG  1 
ATOM   11093 O  OD1 . ASP B  1 663 ? -0.389  69.746 32.392 1.00 16.49 ? 663  ASP B OD1 1 
ATOM   11094 O  OD2 . ASP B  1 663 ? 0.405   67.711 32.506 1.00 21.05 ? 663  ASP B OD2 1 
ATOM   11095 N  N   . SER B  1 664 ? 1.806   72.494 32.369 1.00 16.22 ? 664  SER B N   1 
ATOM   11096 C  CA  . SER B  1 664 ? 1.092   73.758 32.429 1.00 17.53 ? 664  SER B CA  1 
ATOM   11097 C  C   . SER B  1 664 ? -0.432  73.707 32.533 1.00 18.41 ? 664  SER B C   1 
ATOM   11098 O  O   . SER B  1 664 ? -1.014  74.286 33.450 1.00 18.14 ? 664  SER B O   1 
ATOM   11099 C  CB  . SER B  1 664 ? 1.470   74.618 31.214 1.00 18.84 ? 664  SER B CB  1 
ATOM   11100 O  OG  . SER B  1 664 ? 1.140   73.948 29.996 1.00 18.65 ? 664  SER B OG  1 
ATOM   11101 N  N   . VAL B  1 665 ? -1.081  73.020 31.600 1.00 17.93 ? 665  VAL B N   1 
ATOM   11102 C  CA  . VAL B  1 665 ? -2.542  72.951 31.577 1.00 18.87 ? 665  VAL B CA  1 
ATOM   11103 C  C   . VAL B  1 665 ? -3.176  72.485 32.896 1.00 18.76 ? 665  VAL B C   1 
ATOM   11104 O  O   . VAL B  1 665 ? -4.065  73.144 33.438 1.00 18.90 ? 665  VAL B O   1 
ATOM   11105 C  CB  . VAL B  1 665 ? -3.019  72.050 30.421 1.00 17.24 ? 665  VAL B CB  1 
ATOM   11106 C  CG1 . VAL B  1 665 ? -4.512  72.025 30.367 1.00 17.16 ? 665  VAL B CG1 1 
ATOM   11107 C  CG2 . VAL B  1 665 ? -2.453  72.565 29.107 1.00 18.10 ? 665  VAL B CG2 1 
ATOM   11108 N  N   . TYR B  1 666 ? -2.713  71.356 33.412 1.00 18.93 ? 666  TYR B N   1 
ATOM   11109 C  CA  . TYR B  1 666 ? -3.244  70.836 34.663 1.00 18.95 ? 666  TYR B CA  1 
ATOM   11110 C  C   . TYR B  1 666 ? -2.801  71.690 35.851 1.00 19.17 ? 666  TYR B C   1 
ATOM   11111 O  O   . TYR B  1 666 ? -3.631  72.215 36.605 1.00 19.28 ? 666  TYR B O   1 
ATOM   11112 C  CB  . TYR B  1 666 ? -2.783  69.387 34.865 1.00 17.54 ? 666  TYR B CB  1 
ATOM   11113 C  CG  . TYR B  1 666 ? -3.232  68.759 36.171 1.00 17.37 ? 666  TYR B CG  1 
ATOM   11114 C  CD1 . TYR B  1 666 ? -2.555  69.020 37.375 1.00 17.41 ? 666  TYR B CD1 1 
ATOM   11115 C  CD2 . TYR B  1 666 ? -4.326  67.894 36.206 1.00 17.45 ? 666  TYR B CD2 1 
ATOM   11116 C  CE1 . TYR B  1 666 ? -2.958  68.422 38.580 1.00 18.05 ? 666  TYR B CE1 1 
ATOM   11117 C  CE2 . TYR B  1 666 ? -4.744  67.292 37.396 1.00 16.95 ? 666  TYR B CE2 1 
ATOM   11118 C  CZ  . TYR B  1 666 ? -4.058  67.553 38.570 1.00 18.14 ? 666  TYR B CZ  1 
ATOM   11119 O  OH  . TYR B  1 666 ? -4.439  66.907 39.711 1.00 18.89 ? 666  TYR B OH  1 
ATOM   11120 N  N   . THR B  1 667 ? -1.495  71.850 36.009 1.00 19.39 ? 667  THR B N   1 
ATOM   11121 C  CA  . THR B  1 667 ? -0.968  72.607 37.146 1.00 19.67 ? 667  THR B CA  1 
ATOM   11122 C  C   . THR B  1 667 ? -1.498  74.039 37.263 1.00 20.44 ? 667  THR B C   1 
ATOM   11123 O  O   . THR B  1 667 ? -1.991  74.434 38.321 1.00 20.77 ? 667  THR B O   1 
ATOM   11124 C  CB  . THR B  1 667 ? 0.574   72.669 37.117 1.00 17.97 ? 667  THR B CB  1 
ATOM   11125 O  OG1 . THR B  1 667 ? 1.100   71.344 36.914 1.00 15.26 ? 667  THR B OG1 1 
ATOM   11126 C  CG2 . THR B  1 667 ? 1.098   73.254 38.453 1.00 16.62 ? 667  THR B CG2 1 
ATOM   11127 N  N   . GLU B  1 668 ? -1.389  74.816 36.190 1.00 20.07 ? 668  GLU B N   1 
ATOM   11128 C  CA  . GLU B  1 668 ? -1.837  76.206 36.226 1.00 20.42 ? 668  GLU B CA  1 
ATOM   11129 C  C   . GLU B  1 668 ? -3.337  76.356 36.471 1.00 21.67 ? 668  GLU B C   1 
ATOM   11130 O  O   . GLU B  1 668 ? -3.803  77.382 36.982 1.00 20.88 ? 668  GLU B O   1 
ATOM   11131 C  CB  . GLU B  1 668 ? -1.434  76.888 34.934 1.00 19.42 ? 668  GLU B CB  1 
ATOM   11132 C  CG  . GLU B  1 668 ? 0.072   77.047 34.825 1.00 19.22 ? 668  GLU B CG  1 
ATOM   11133 C  CD  . GLU B  1 668 ? 0.511   77.420 33.436 1.00 19.48 ? 668  GLU B CD  1 
ATOM   11134 O  OE1 . GLU B  1 668 ? -0.342  77.933 32.671 1.00 17.92 ? 668  GLU B OE1 1 
ATOM   11135 O  OE2 . GLU B  1 668 ? 1.710   77.198 33.112 1.00 19.08 ? 668  GLU B OE2 1 
ATOM   11136 N  N   . ARG B  1 669 ? -4.098  75.322 36.144 1.00 21.23 ? 669  ARG B N   1 
ATOM   11137 C  CA  . ARG B  1 669 ? -5.526  75.400 36.349 1.00 21.48 ? 669  ARG B CA  1 
ATOM   11138 C  C   . ARG B  1 669 ? -5.845  75.576 37.818 1.00 21.25 ? 669  ARG B C   1 
ATOM   11139 O  O   . ARG B  1 669 ? -6.782  76.274 38.173 1.00 19.35 ? 669  ARG B O   1 
ATOM   11140 C  CB  . ARG B  1 669 ? -6.204  74.127 35.847 1.00 21.51 ? 669  ARG B CB  1 
ATOM   11141 C  CG  . ARG B  1 669 ? -7.703  74.157 35.985 1.00 21.47 ? 669  ARG B CG  1 
ATOM   11142 C  CD  . ARG B  1 669 ? -8.334  73.299 34.885 1.00 23.02 ? 669  ARG B CD  1 
ATOM   11143 N  NE  . ARG B  1 669 ? -8.043  71.908 35.115 1.00 23.53 ? 669  ARG B NE  1 
ATOM   11144 C  CZ  . ARG B  1 669 ? -7.512  71.066 34.236 1.00 22.36 ? 669  ARG B CZ  1 
ATOM   11145 N  NH1 . ARG B  1 669 ? -7.195  71.459 33.008 1.00 19.89 ? 669  ARG B NH1 1 
ATOM   11146 N  NH2 . ARG B  1 669 ? -7.289  69.809 34.617 1.00 20.64 ? 669  ARG B NH2 1 
ATOM   11147 N  N   . TYR B  1 670 ? -5.060  74.932 38.668 1.00 20.76 ? 670  TYR B N   1 
ATOM   11148 C  CA  . TYR B  1 670 ? -5.321  74.988 40.089 1.00 21.47 ? 670  TYR B CA  1 
ATOM   11149 C  C   . TYR B  1 670 ? -4.370  75.896 40.846 1.00 23.14 ? 670  TYR B C   1 
ATOM   11150 O  O   . TYR B  1 670 ? -4.717  76.395 41.915 1.00 24.15 ? 670  TYR B O   1 
ATOM   11151 C  CB  . TYR B  1 670 ? -5.234  73.578 40.693 1.00 19.61 ? 670  TYR B CB  1 
ATOM   11152 C  CG  . TYR B  1 670 ? -5.980  72.518 39.899 1.00 19.23 ? 670  TYR B CG  1 
ATOM   11153 C  CD1 . TYR B  1 670 ? -7.379  72.465 39.880 1.00 18.20 ? 670  TYR B CD1 1 
ATOM   11154 C  CD2 . TYR B  1 670 ? -5.277  71.594 39.131 1.00 16.34 ? 670  TYR B CD2 1 
ATOM   11155 C  CE1 . TYR B  1 670 ? -8.050  71.513 39.099 1.00 16.65 ? 670  TYR B CE1 1 
ATOM   11156 C  CE2 . TYR B  1 670 ? -5.920  70.661 38.363 1.00 16.98 ? 670  TYR B CE2 1 
ATOM   11157 C  CZ  . TYR B  1 670 ? -7.309  70.620 38.342 1.00 17.80 ? 670  TYR B CZ  1 
ATOM   11158 O  OH  . TYR B  1 670 ? -7.911  69.688 37.527 1.00 18.83 ? 670  TYR B OH  1 
ATOM   11159 N  N   . MET B  1 671 ? -3.185  76.129 40.281 1.00 23.15 ? 671  MET B N   1 
ATOM   11160 C  CA  . MET B  1 671 ? -2.151  76.915 40.939 1.00 22.76 ? 671  MET B CA  1 
ATOM   11161 C  C   . MET B  1 671 ? -1.826  78.256 40.318 1.00 23.38 ? 671  MET B C   1 
ATOM   11162 O  O   . MET B  1 671 ? -1.033  79.017 40.874 1.00 23.59 ? 671  MET B O   1 
ATOM   11163 C  CB  . MET B  1 671 ? -0.861  76.089 40.989 1.00 22.94 ? 671  MET B CB  1 
ATOM   11164 C  CG  . MET B  1 671 ? -0.936  74.856 41.856 1.00 23.23 ? 671  MET B CG  1 
ATOM   11165 S  SD  . MET B  1 671 ? -0.858  75.360 43.565 1.00 25.94 ? 671  MET B SD  1 
ATOM   11166 C  CE  . MET B  1 671 ? 0.951   75.565 43.750 1.00 25.37 ? 671  MET B CE  1 
ATOM   11167 N  N   . GLY B  1 672 ? -2.414  78.553 39.169 1.00 23.20 ? 672  GLY B N   1 
ATOM   11168 C  CA  . GLY B  1 672 ? -2.090  79.804 38.519 1.00 23.51 ? 672  GLY B CA  1 
ATOM   11169 C  C   . GLY B  1 672 ? -0.632  79.749 38.062 1.00 24.72 ? 672  GLY B C   1 
ATOM   11170 O  O   . GLY B  1 672 ? -0.044  78.671 37.967 1.00 23.28 ? 672  GLY B O   1 
ATOM   11171 N  N   . LEU B  1 673 ? -0.033  80.907 37.802 1.00 25.52 ? 673  LEU B N   1 
ATOM   11172 C  CA  . LEU B  1 673 ? 1.352   80.948 37.332 1.00 26.37 ? 673  LEU B CA  1 
ATOM   11173 C  C   . LEU B  1 673 ? 2.419   81.027 38.398 1.00 26.22 ? 673  LEU B C   1 
ATOM   11174 O  O   . LEU B  1 673 ? 2.257   81.706 39.400 1.00 27.02 ? 673  LEU B O   1 
ATOM   11175 C  CB  . LEU B  1 673 ? 1.540   82.110 36.382 1.00 25.55 ? 673  LEU B CB  1 
ATOM   11176 C  CG  . LEU B  1 673 ? 0.767   81.923 35.091 1.00 27.36 ? 673  LEU B CG  1 
ATOM   11177 C  CD1 . LEU B  1 673 ? 0.871   83.196 34.257 1.00 28.93 ? 673  LEU B CD1 1 
ATOM   11178 C  CD2 . LEU B  1 673 ? 1.329   80.727 34.342 1.00 27.56 ? 673  LEU B CD2 1 
ATOM   11179 N  N   . PRO B  1 674 ? 3.547   80.333 38.187 1.00 27.18 ? 674  PRO B N   1 
ATOM   11180 C  CA  . PRO B  1 674 ? 4.645   80.349 39.162 1.00 28.02 ? 674  PRO B CA  1 
ATOM   11181 C  C   . PRO B  1 674 ? 5.537   81.602 39.068 1.00 28.86 ? 674  PRO B C   1 
ATOM   11182 O  O   . PRO B  1 674 ? 6.750   81.501 38.898 1.00 29.91 ? 674  PRO B O   1 
ATOM   11183 C  CB  . PRO B  1 674 ? 5.411   79.070 38.824 1.00 27.79 ? 674  PRO B CB  1 
ATOM   11184 C  CG  . PRO B  1 674 ? 5.284   79.031 37.304 1.00 26.48 ? 674  PRO B CG  1 
ATOM   11185 C  CD  . PRO B  1 674 ? 3.800   79.340 37.123 1.00 26.75 ? 674  PRO B CD  1 
ATOM   11186 N  N   . THR B  1 675 ? 4.942   82.779 39.171 1.00 28.93 ? 675  THR B N   1 
ATOM   11187 C  CA  . THR B  1 675 ? 5.713   84.015 39.105 1.00 29.55 ? 675  THR B CA  1 
ATOM   11188 C  C   . THR B  1 675 ? 5.433   84.839 40.363 1.00 30.45 ? 675  THR B C   1 
ATOM   11189 O  O   . THR B  1 675 ? 4.397   84.670 41.005 1.00 29.06 ? 675  THR B O   1 
ATOM   11190 C  CB  . THR B  1 675 ? 5.331   84.844 37.869 1.00 28.79 ? 675  THR B CB  1 
ATOM   11191 O  OG1 . THR B  1 675 ? 3.969   85.275 37.989 1.00 27.41 ? 675  THR B OG1 1 
ATOM   11192 C  CG2 . THR B  1 675 ? 5.483   83.998 36.586 1.00 28.01 ? 675  THR B CG2 1 
ATOM   11193 N  N   . PRO B  1 676 ? 6.352   85.748 40.728 1.00 32.05 ? 676  PRO B N   1 
ATOM   11194 C  CA  . PRO B  1 676 ? 6.129   86.566 41.935 1.00 33.14 ? 676  PRO B CA  1 
ATOM   11195 C  C   . PRO B  1 676 ? 4.833   87.369 41.914 1.00 33.40 ? 676  PRO B C   1 
ATOM   11196 O  O   . PRO B  1 676 ? 4.187   87.535 42.950 1.00 34.32 ? 676  PRO B O   1 
ATOM   11197 C  CB  . PRO B  1 676 ? 7.385   87.442 42.017 1.00 32.85 ? 676  PRO B CB  1 
ATOM   11198 C  CG  . PRO B  1 676 ? 7.887   87.484 40.584 1.00 33.52 ? 676  PRO B CG  1 
ATOM   11199 C  CD  . PRO B  1 676 ? 7.623   86.093 40.065 1.00 32.53 ? 676  PRO B CD  1 
ATOM   11200 N  N   . GLU B  1 677 ? 4.437   87.835 40.733 1.00 34.21 ? 677  GLU B N   1 
ATOM   11201 C  CA  . GLU B  1 677 ? 3.204   88.606 40.593 1.00 35.35 ? 677  GLU B CA  1 
ATOM   11202 C  C   . GLU B  1 677 ? 1.955   87.731 40.680 1.00 34.75 ? 677  GLU B C   1 
ATOM   11203 O  O   . GLU B  1 677 ? 0.841   88.247 40.708 1.00 34.93 ? 677  GLU B O   1 
ATOM   11204 C  CB  . GLU B  1 677 ? 3.169   89.356 39.254 1.00 38.01 ? 677  GLU B CB  1 
ATOM   11205 C  CG  . GLU B  1 677 ? 4.451   90.110 38.925 1.00 42.35 ? 677  GLU B CG  1 
ATOM   11206 C  CD  . GLU B  1 677 ? 5.473   89.226 38.242 1.00 43.59 ? 677  GLU B CD  1 
ATOM   11207 O  OE1 . GLU B  1 677 ? 5.671   88.078 38.693 1.00 44.58 ? 677  GLU B OE1 1 
ATOM   11208 O  OE2 . GLU B  1 677 ? 6.083   89.685 37.259 1.00 45.76 ? 677  GLU B OE2 1 
ATOM   11209 N  N   . ASP B  1 678 ? 2.118   86.413 40.693 1.00 33.25 ? 678  ASP B N   1 
ATOM   11210 C  CA  . ASP B  1 678 ? 0.943   85.557 40.780 1.00 31.90 ? 678  ASP B CA  1 
ATOM   11211 C  C   . ASP B  1 678 ? 0.989   84.621 41.982 1.00 30.26 ? 678  ASP B C   1 
ATOM   11212 O  O   . ASP B  1 678 ? 0.659   85.037 43.078 1.00 30.72 ? 678  ASP B O   1 
ATOM   11213 C  CB  . ASP B  1 678 ? 0.736   84.748 39.487 1.00 31.74 ? 678  ASP B CB  1 
ATOM   11214 C  CG  . ASP B  1 678 ? -0.621  84.050 39.451 1.00 32.67 ? 678  ASP B CG  1 
ATOM   11215 O  OD1 . ASP B  1 678 ? -1.296  84.035 40.492 1.00 32.71 ? 678  ASP B OD1 1 
ATOM   11216 O  OD2 . ASP B  1 678 ? -1.023  83.513 38.392 1.00 34.88 ? 678  ASP B OD2 1 
ATOM   11217 N  N   . ASN B  1 679 ? 1.420   83.373 41.800 1.00 27.95 ? 679  ASN B N   1 
ATOM   11218 C  CA  . ASN B  1 679 ? 1.415   82.428 42.923 1.00 26.98 ? 679  ASN B CA  1 
ATOM   11219 C  C   . ASN B  1 679 ? 2.735   81.705 43.205 1.00 26.33 ? 679  ASN B C   1 
ATOM   11220 O  O   . ASN B  1 679 ? 2.731   80.630 43.807 1.00 25.91 ? 679  ASN B O   1 
ATOM   11221 C  CB  . ASN B  1 679 ? 0.293   81.393 42.681 1.00 25.15 ? 679  ASN B CB  1 
ATOM   11222 C  CG  . ASN B  1 679 ? -0.205  80.730 43.968 1.00 23.87 ? 679  ASN B CG  1 
ATOM   11223 O  OD1 . ASN B  1 679 ? -0.211  81.341 45.031 1.00 23.03 ? 679  ASN B OD1 1 
ATOM   11224 N  ND2 . ASN B  1 679 ? -0.670  79.484 43.856 1.00 24.18 ? 679  ASN B ND2 1 
ATOM   11225 N  N   . LEU B  1 680 ? 3.861   82.285 42.798 1.00 26.81 ? 680  LEU B N   1 
ATOM   11226 C  CA  . LEU B  1 680 ? 5.153   81.622 42.998 1.00 27.38 ? 680  LEU B CA  1 
ATOM   11227 C  C   . LEU B  1 680 ? 5.406   81.197 44.439 1.00 27.80 ? 680  LEU B C   1 
ATOM   11228 O  O   . LEU B  1 680 ? 5.860   80.079 44.686 1.00 28.47 ? 680  LEU B O   1 
ATOM   11229 C  CB  . LEU B  1 680 ? 6.304   82.516 42.531 1.00 29.09 ? 680  LEU B CB  1 
ATOM   11230 C  CG  . LEU B  1 680 ? 7.738   82.019 42.808 1.00 31.00 ? 680  LEU B CG  1 
ATOM   11231 C  CD1 . LEU B  1 680 ? 7.970   80.684 42.105 1.00 32.07 ? 680  LEU B CD1 1 
ATOM   11232 C  CD2 . LEU B  1 680 ? 8.762   83.056 42.313 1.00 31.72 ? 680  LEU B CD2 1 
ATOM   11233 N  N   . ASP B  1 681 ? 5.112   82.069 45.396 1.00 27.69 ? 681  ASP B N   1 
ATOM   11234 C  CA  . ASP B  1 681 ? 5.350   81.713 46.783 1.00 28.14 ? 681  ASP B CA  1 
ATOM   11235 C  C   . ASP B  1 681 ? 4.675   80.403 47.188 1.00 27.35 ? 681  ASP B C   1 
ATOM   11236 O  O   . ASP B  1 681 ? 5.272   79.600 47.905 1.00 27.22 ? 681  ASP B O   1 
ATOM   11237 C  CB  . ASP B  1 681 ? 4.899   82.834 47.720 1.00 30.03 ? 681  ASP B CB  1 
ATOM   11238 C  CG  . ASP B  1 681 ? 5.786   84.073 47.626 1.00 33.71 ? 681  ASP B CG  1 
ATOM   11239 O  OD1 . ASP B  1 681 ? 6.874   84.005 47.005 1.00 35.10 ? 681  ASP B OD1 1 
ATOM   11240 O  OD2 . ASP B  1 681 ? 5.395   85.120 48.189 1.00 34.51 ? 681  ASP B OD2 1 
ATOM   11241 N  N   . HIS B  1 682 ? 3.437   80.173 46.758 1.00 25.53 ? 682  HIS B N   1 
ATOM   11242 C  CA  . HIS B  1 682 ? 2.813   78.919 47.164 1.00 24.70 ? 682  HIS B CA  1 
ATOM   11243 C  C   . HIS B  1 682 ? 3.406   77.748 46.384 1.00 24.14 ? 682  HIS B C   1 
ATOM   11244 O  O   . HIS B  1 682 ? 3.474   76.633 46.893 1.00 22.74 ? 682  HIS B O   1 
ATOM   11245 C  CB  . HIS B  1 682 ? 1.298   78.928 47.003 1.00 24.68 ? 682  HIS B CB  1 
ATOM   11246 C  CG  . HIS B  1 682 ? 0.665   77.667 47.502 1.00 26.78 ? 682  HIS B CG  1 
ATOM   11247 N  ND1 . HIS B  1 682 ? 0.716   77.286 48.828 1.00 27.04 ? 682  HIS B ND1 1 
ATOM   11248 C  CD2 . HIS B  1 682 ? 0.081   76.638 46.840 1.00 25.72 ? 682  HIS B CD2 1 
ATOM   11249 C  CE1 . HIS B  1 682 ? 0.199   76.076 48.957 1.00 27.52 ? 682  HIS B CE1 1 
ATOM   11250 N  NE2 . HIS B  1 682 ? -0.192  75.661 47.765 1.00 25.32 ? 682  HIS B NE2 1 
ATOM   11251 N  N   . TYR B  1 683 ? 3.831   78.011 45.150 1.00 23.64 ? 683  TYR B N   1 
ATOM   11252 C  CA  . TYR B  1 683 ? 4.468   76.993 44.327 1.00 23.98 ? 683  TYR B CA  1 
ATOM   11253 C  C   . TYR B  1 683 ? 5.692   76.497 45.086 1.00 24.75 ? 683  TYR B C   1 
ATOM   11254 O  O   . TYR B  1 683 ? 5.927   75.293 45.197 1.00 25.72 ? 683  TYR B O   1 
ATOM   11255 C  CB  . TYR B  1 683 ? 4.941   77.582 42.992 1.00 21.69 ? 683  TYR B CB  1 
ATOM   11256 C  CG  . TYR B  1 683 ? 4.043   77.320 41.804 1.00 22.55 ? 683  TYR B CG  1 
ATOM   11257 C  CD1 . TYR B  1 683 ? 4.176   76.158 41.037 1.00 22.09 ? 683  TYR B CD1 1 
ATOM   11258 C  CD2 . TYR B  1 683 ? 3.084   78.259 41.420 1.00 21.90 ? 683  TYR B CD2 1 
ATOM   11259 C  CE1 . TYR B  1 683 ? 3.374   75.948 39.904 1.00 22.19 ? 683  TYR B CE1 1 
ATOM   11260 C  CE2 . TYR B  1 683 ? 2.285   78.063 40.303 1.00 23.60 ? 683  TYR B CE2 1 
ATOM   11261 C  CZ  . TYR B  1 683 ? 2.437   76.903 39.544 1.00 23.17 ? 683  TYR B CZ  1 
ATOM   11262 O  OH  . TYR B  1 683 ? 1.661   76.744 38.417 1.00 22.71 ? 683  TYR B OH  1 
ATOM   11263 N  N   . ARG B  1 684 ? 6.472   77.436 45.607 1.00 25.07 ? 684  ARG B N   1 
ATOM   11264 C  CA  . ARG B  1 684 ? 7.699   77.091 46.332 1.00 26.82 ? 684  ARG B CA  1 
ATOM   11265 C  C   . ARG B  1 684 ? 7.456   76.546 47.743 1.00 26.99 ? 684  ARG B C   1 
ATOM   11266 O  O   . ARG B  1 684 ? 8.327   75.912 48.337 1.00 26.95 ? 684  ARG B O   1 
ATOM   11267 C  CB  . ARG B  1 684 ? 8.617   78.328 46.401 1.00 26.53 ? 684  ARG B CB  1 
ATOM   11268 C  CG  . ARG B  1 684 ? 9.129   78.763 45.033 1.00 27.18 ? 684  ARG B CG  1 
ATOM   11269 C  CD  . ARG B  1 684 ? 9.908   77.615 44.376 1.00 29.21 ? 684  ARG B CD  1 
ATOM   11270 N  NE  . ARG B  1 684 ? 10.148  77.806 42.945 1.00 29.44 ? 684  ARG B NE  1 
ATOM   11271 C  CZ  . ARG B  1 684 ? 10.915  78.760 42.425 1.00 29.74 ? 684  ARG B CZ  1 
ATOM   11272 N  NH1 . ARG B  1 684 ? 11.530  79.631 43.221 1.00 30.26 ? 684  ARG B NH1 1 
ATOM   11273 N  NH2 . ARG B  1 684 ? 11.079  78.836 41.102 1.00 28.70 ? 684  ARG B NH2 1 
ATOM   11274 N  N   . ASN B  1 685 ? 6.250   76.763 48.250 1.00 27.41 ? 685  ASN B N   1 
ATOM   11275 C  CA  . ASN B  1 685 ? 5.895   76.347 49.591 1.00 28.14 ? 685  ASN B CA  1 
ATOM   11276 C  C   . ASN B  1 685 ? 5.218   74.990 49.698 1.00 27.37 ? 685  ASN B C   1 
ATOM   11277 O  O   . ASN B  1 685 ? 5.094   74.433 50.797 1.00 26.68 ? 685  ASN B O   1 
ATOM   11278 C  CB  . ASN B  1 685 ? 4.970   77.393 50.207 1.00 30.71 ? 685  ASN B CB  1 
ATOM   11279 C  CG  . ASN B  1 685 ? 5.249   77.615 51.665 1.00 34.74 ? 685  ASN B CG  1 
ATOM   11280 O  OD1 . ASN B  1 685 ? 4.328   77.639 52.491 1.00 38.31 ? 685  ASN B OD1 1 
ATOM   11281 N  ND2 . ASN B  1 685 ? 6.527   77.790 52.002 1.00 36.39 ? 685  ASN B ND2 1 
ATOM   11282 N  N   . SER B  1 686 ? 4.776   74.459 48.565 1.00 25.39 ? 686  SER B N   1 
ATOM   11283 C  CA  . SER B  1 686 ? 4.057   73.187 48.566 1.00 23.33 ? 686  SER B CA  1 
ATOM   11284 C  C   . SER B  1 686 ? 4.859   72.019 48.026 1.00 23.14 ? 686  SER B C   1 
ATOM   11285 O  O   . SER B  1 686 ? 4.284   71.046 47.545 1.00 23.99 ? 686  SER B O   1 
ATOM   11286 C  CB  . SER B  1 686 ? 2.765   73.331 47.754 1.00 22.10 ? 686  SER B CB  1 
ATOM   11287 O  OG  . SER B  1 686 ? 3.048   73.747 46.422 1.00 20.42 ? 686  SER B OG  1 
ATOM   11288 N  N   . THR B  1 687 ? 6.183   72.099 48.093 1.00 22.11 ? 687  THR B N   1 
ATOM   11289 C  CA  . THR B  1 687 ? 7.007   70.996 47.590 1.00 20.89 ? 687  THR B CA  1 
ATOM   11290 C  C   . THR B  1 687 ? 7.232   69.942 48.660 1.00 20.79 ? 687  THR B C   1 
ATOM   11291 O  O   . THR B  1 687 ? 7.205   70.233 49.850 1.00 19.60 ? 687  THR B O   1 
ATOM   11292 C  CB  . THR B  1 687 ? 8.400   71.458 47.141 1.00 20.63 ? 687  THR B CB  1 
ATOM   11293 O  OG1 . THR B  1 687 ? 9.202   71.712 48.295 1.00 20.20 ? 687  THR B OG1 1 
ATOM   11294 C  CG2 . THR B  1 687 ? 8.307   72.742 46.310 1.00 21.22 ? 687  THR B CG2 1 
ATOM   11295 N  N   . VAL B  1 688 ? 7.455   68.711 48.221 1.00 20.51 ? 688  VAL B N   1 
ATOM   11296 C  CA  . VAL B  1 688 ? 7.739   67.607 49.127 1.00 19.28 ? 688  VAL B CA  1 
ATOM   11297 C  C   . VAL B  1 688 ? 9.144   67.769 49.722 1.00 19.65 ? 688  VAL B C   1 
ATOM   11298 O  O   . VAL B  1 688 ? 9.354   67.498 50.908 1.00 18.56 ? 688  VAL B O   1 
ATOM   11299 C  CB  . VAL B  1 688 ? 7.685   66.256 48.366 1.00 17.86 ? 688  VAL B CB  1 
ATOM   11300 C  CG1 . VAL B  1 688 ? 8.336   65.140 49.187 1.00 17.40 ? 688  VAL B CG1 1 
ATOM   11301 C  CG2 . VAL B  1 688 ? 6.245   65.905 48.059 1.00 14.68 ? 688  VAL B CG2 1 
ATOM   11302 N  N   . MET B  1 689 ? 10.090  68.216 48.887 1.00 19.76 ? 689  MET B N   1 
ATOM   11303 C  CA  . MET B  1 689 ? 11.495  68.384 49.304 1.00 19.85 ? 689  MET B CA  1 
ATOM   11304 C  C   . MET B  1 689 ? 11.697  69.263 50.535 1.00 20.58 ? 689  MET B C   1 
ATOM   11305 O  O   . MET B  1 689 ? 12.560  68.968 51.346 1.00 21.33 ? 689  MET B O   1 
ATOM   11306 C  CB  . MET B  1 689 ? 12.375  68.923 48.166 1.00 18.70 ? 689  MET B CB  1 
ATOM   11307 C  CG  . MET B  1 689 ? 12.713  67.920 47.090 1.00 17.82 ? 689  MET B CG  1 
ATOM   11308 S  SD  . MET B  1 689 ? 11.261  67.439 46.047 1.00 18.48 ? 689  MET B SD  1 
ATOM   11309 C  CE  . MET B  1 689 ? 11.165  68.907 44.863 1.00 16.28 ? 689  MET B CE  1 
ATOM   11310 N  N   . SER B  1 690 ? 10.895  70.310 50.708 1.00 21.17 ? 690  SER B N   1 
ATOM   11311 C  CA  . SER B  1 690 ? 11.067  71.181 51.874 1.00 22.67 ? 690  SER B CA  1 
ATOM   11312 C  C   . SER B  1 690 ? 10.685  70.520 53.208 1.00 23.13 ? 690  SER B C   1 
ATOM   11313 O  O   . SER B  1 690 ? 10.939  71.077 54.273 1.00 23.61 ? 690  SER B O   1 
ATOM   11314 C  CB  . SER B  1 690 ? 10.274  72.478 51.707 1.00 21.10 ? 690  SER B CB  1 
ATOM   11315 O  OG  . SER B  1 690 ? 8.878   72.217 51.610 1.00 23.65 ? 690  SER B OG  1 
ATOM   11316 N  N   . ARG B  1 691 ? 10.101  69.330 53.159 1.00 23.08 ? 691  ARG B N   1 
ATOM   11317 C  CA  . ARG B  1 691 ? 9.711   68.641 54.387 1.00 23.16 ? 691  ARG B CA  1 
ATOM   11318 C  C   . ARG B  1 691 ? 10.586  67.431 54.659 1.00 23.18 ? 691  ARG B C   1 
ATOM   11319 O  O   . ARG B  1 691 ? 10.280  66.625 55.537 1.00 22.20 ? 691  ARG B O   1 
ATOM   11320 C  CB  . ARG B  1 691 ? 8.234   68.231 54.292 1.00 24.15 ? 691  ARG B CB  1 
ATOM   11321 C  CG  . ARG B  1 691 ? 7.313   69.442 54.298 1.00 28.46 ? 691  ARG B CG  1 
ATOM   11322 C  CD  . ARG B  1 691 ? 6.100   69.306 53.421 1.00 30.60 ? 691  ARG B CD  1 
ATOM   11323 N  NE  . ARG B  1 691 ? 4.980   68.678 54.092 1.00 33.26 ? 691  ARG B NE  1 
ATOM   11324 C  CZ  . ARG B  1 691 ? 3.794   69.252 54.281 1.00 33.24 ? 691  ARG B CZ  1 
ATOM   11325 N  NH1 . ARG B  1 691 ? 3.567   70.490 53.857 1.00 31.92 ? 691  ARG B NH1 1 
ATOM   11326 N  NH2 . ARG B  1 691 ? 2.822   68.564 54.875 1.00 32.17 ? 691  ARG B NH2 1 
ATOM   11327 N  N   . ALA B  1 692 ? 11.684  67.325 53.913 1.00 22.94 ? 692  ALA B N   1 
ATOM   11328 C  CA  . ALA B  1 692 ? 12.609  66.189 54.033 1.00 24.23 ? 692  ALA B CA  1 
ATOM   11329 C  C   . ALA B  1 692 ? 13.000  65.832 55.469 1.00 25.19 ? 692  ALA B C   1 
ATOM   11330 O  O   . ALA B  1 692 ? 13.023  64.663 55.846 1.00 24.98 ? 692  ALA B O   1 
ATOM   11331 C  CB  . ALA B  1 692 ? 13.872  66.464 53.209 1.00 24.06 ? 692  ALA B CB  1 
ATOM   11332 N  N   . GLU B  1 693 ? 13.300  66.851 56.262 1.00 27.09 ? 693  GLU B N   1 
ATOM   11333 C  CA  . GLU B  1 693 ? 13.711  66.657 57.641 1.00 28.57 ? 693  GLU B CA  1 
ATOM   11334 C  C   . GLU B  1 693 ? 12.681  65.877 58.463 1.00 28.66 ? 693  GLU B C   1 
ATOM   11335 O  O   . GLU B  1 693 ? 13.046  65.068 59.308 1.00 29.06 ? 693  GLU B O   1 
ATOM   11336 C  CB  . GLU B  1 693 ? 13.977  68.010 58.290 1.00 31.32 ? 693  GLU B CB  1 
ATOM   11337 C  CG  . GLU B  1 693 ? 14.611  67.910 59.656 1.00 37.70 ? 693  GLU B CG  1 
ATOM   11338 C  CD  . GLU B  1 693 ? 16.055  67.448 59.588 1.00 40.06 ? 693  GLU B CD  1 
ATOM   11339 O  OE1 . GLU B  1 693 ? 16.550  66.887 60.592 1.00 42.49 ? 693  GLU B OE1 1 
ATOM   11340 O  OE2 . GLU B  1 693 ? 16.696  67.663 58.534 1.00 42.03 ? 693  GLU B OE2 1 
ATOM   11341 N  N   . ASN B  1 694 ? 11.396  66.105 58.224 1.00 28.03 ? 694  ASN B N   1 
ATOM   11342 C  CA  . ASN B  1 694 ? 10.385  65.386 58.986 1.00 28.00 ? 694  ASN B CA  1 
ATOM   11343 C  C   . ASN B  1 694 ? 10.293  63.905 58.696 1.00 27.20 ? 694  ASN B C   1 
ATOM   11344 O  O   . ASN B  1 694 ? 9.727   63.167 59.494 1.00 27.94 ? 694  ASN B O   1 
ATOM   11345 C  CB  . ASN B  1 694 ? 9.013   66.020 58.800 1.00 29.72 ? 694  ASN B CB  1 
ATOM   11346 C  CG  . ASN B  1 694 ? 8.912   67.352 59.482 1.00 30.80 ? 694  ASN B CG  1 
ATOM   11347 O  OD1 . ASN B  1 694 ? 9.283   67.486 60.648 1.00 33.62 ? 694  ASN B OD1 1 
ATOM   11348 N  ND2 . ASN B  1 694 ? 8.416   68.348 58.771 1.00 32.65 ? 694  ASN B ND2 1 
ATOM   11349 N  N   . PHE B  1 695 ? 10.850  63.467 57.569 1.00 26.21 ? 695  PHE B N   1 
ATOM   11350 C  CA  . PHE B  1 695 ? 10.813  62.051 57.198 1.00 25.24 ? 695  PHE B CA  1 
ATOM   11351 C  C   . PHE B  1 695 ? 11.656  61.184 58.146 1.00 25.52 ? 695  PHE B C   1 
ATOM   11352 O  O   . PHE B  1 695 ? 11.668  59.958 58.044 1.00 24.60 ? 695  PHE B O   1 
ATOM   11353 C  CB  . PHE B  1 695 ? 11.282  61.862 55.745 1.00 22.55 ? 695  PHE B CB  1 
ATOM   11354 C  CG  . PHE B  1 695 ? 10.199  62.114 54.703 1.00 21.06 ? 695  PHE B CG  1 
ATOM   11355 C  CD1 . PHE B  1 695 ? 9.554   61.050 54.074 1.00 18.15 ? 695  PHE B CD1 1 
ATOM   11356 C  CD2 . PHE B  1 695 ? 9.857   63.407 54.326 1.00 18.37 ? 695  PHE B CD2 1 
ATOM   11357 C  CE1 . PHE B  1 695 ? 8.597   61.275 53.081 1.00 18.95 ? 695  PHE B CE1 1 
ATOM   11358 C  CE2 . PHE B  1 695 ? 8.892   63.637 53.323 1.00 17.92 ? 695  PHE B CE2 1 
ATOM   11359 C  CZ  . PHE B  1 695 ? 8.263   62.576 52.708 1.00 15.75 ? 695  PHE B CZ  1 
ATOM   11360 N  N   . LYS B  1 696 ? 12.374  61.809 59.067 1.00 26.55 ? 696  LYS B N   1 
ATOM   11361 C  CA  . LYS B  1 696 ? 13.143  61.010 60.016 1.00 29.13 ? 696  LYS B CA  1 
ATOM   11362 C  C   . LYS B  1 696 ? 12.182  60.281 60.963 1.00 29.16 ? 696  LYS B C   1 
ATOM   11363 O  O   . LYS B  1 696 ? 12.525  59.242 61.508 1.00 30.05 ? 696  LYS B O   1 
ATOM   11364 C  CB  . LYS B  1 696 ? 14.103  61.898 60.809 1.00 30.70 ? 696  LYS B CB  1 
ATOM   11365 C  CG  . LYS B  1 696 ? 15.366  62.206 60.027 1.00 34.43 ? 696  LYS B CG  1 
ATOM   11366 C  CD  . LYS B  1 696 ? 16.190  63.341 60.624 1.00 37.21 ? 696  LYS B CD  1 
ATOM   11367 C  CE  . LYS B  1 696 ? 17.489  63.517 59.829 1.00 38.25 ? 696  LYS B CE  1 
ATOM   11368 N  NZ  . LYS B  1 696 ? 18.215  64.765 60.193 1.00 41.14 ? 696  LYS B NZ  1 
ATOM   11369 N  N   . GLN B  1 697 ? 10.967  60.817 61.100 1.00 29.16 ? 697  GLN B N   1 
ATOM   11370 C  CA  . GLN B  1 697 ? 9.940   60.261 61.981 1.00 29.42 ? 697  GLN B CA  1 
ATOM   11371 C  C   . GLN B  1 697 ? 9.157   59.060 61.415 1.00 28.41 ? 697  GLN B C   1 
ATOM   11372 O  O   . GLN B  1 697 ? 8.358   58.438 62.135 1.00 27.54 ? 697  GLN B O   1 
ATOM   11373 C  CB  . GLN B  1 697 ? 8.936   61.365 62.361 1.00 30.38 ? 697  GLN B CB  1 
ATOM   11374 C  CG  . GLN B  1 697 ? 9.549   62.625 63.019 1.00 33.92 ? 697  GLN B CG  1 
ATOM   11375 C  CD  . GLN B  1 697 ? 8.528   63.765 63.206 1.00 36.45 ? 697  GLN B CD  1 
ATOM   11376 O  OE1 . GLN B  1 697 ? 7.501   63.605 63.887 1.00 37.75 ? 697  GLN B OE1 1 
ATOM   11377 N  NE2 . GLN B  1 697 ? 8.815   64.918 62.607 1.00 35.51 ? 697  GLN B NE2 1 
ATOM   11378 N  N   . VAL B  1 698 ? 9.375   58.724 60.144 1.00 26.79 ? 698  VAL B N   1 
ATOM   11379 C  CA  . VAL B  1 698 ? 8.633   57.625 59.523 1.00 25.21 ? 698  VAL B CA  1 
ATOM   11380 C  C   . VAL B  1 698 ? 9.430   56.697 58.609 1.00 25.58 ? 698  VAL B C   1 
ATOM   11381 O  O   . VAL B  1 698 ? 10.588  56.950 58.287 1.00 25.29 ? 698  VAL B O   1 
ATOM   11382 C  CB  . VAL B  1 698 ? 7.455   58.166 58.674 1.00 25.11 ? 698  VAL B CB  1 
ATOM   11383 C  CG1 . VAL B  1 698 ? 6.573   59.088 59.510 1.00 23.60 ? 698  VAL B CG1 1 
ATOM   11384 C  CG2 . VAL B  1 698 ? 7.991   58.883 57.428 1.00 23.10 ? 698  VAL B CG2 1 
ATOM   11385 N  N   . GLU B  1 699 ? 8.779   55.613 58.200 1.00 25.47 ? 699  GLU B N   1 
ATOM   11386 C  CA  . GLU B  1 699 ? 9.355   54.641 57.278 1.00 26.27 ? 699  GLU B CA  1 
ATOM   11387 C  C   . GLU B  1 699 ? 8.708   54.957 55.922 1.00 25.14 ? 699  GLU B C   1 
ATOM   11388 O  O   . GLU B  1 699 ? 7.474   54.937 55.788 1.00 23.78 ? 699  GLU B O   1 
ATOM   11389 C  CB  . GLU B  1 699 ? 9.011   53.223 57.723 1.00 28.87 ? 699  GLU B CB  1 
ATOM   11390 C  CG  . GLU B  1 699 ? 9.788   52.779 58.956 1.00 33.56 ? 699  GLU B CG  1 
ATOM   11391 C  CD  . GLU B  1 699 ? 9.151   51.587 59.657 1.00 36.34 ? 699  GLU B CD  1 
ATOM   11392 O  OE1 . GLU B  1 699 ? 8.827   50.585 58.976 1.00 38.68 ? 699  GLU B OE1 1 
ATOM   11393 O  OE2 . GLU B  1 699 ? 8.986   51.655 60.895 1.00 37.76 ? 699  GLU B OE2 1 
ATOM   11394 N  N   . TYR B  1 700 ? 9.553   55.233 54.930 1.00 22.32 ? 700  TYR B N   1 
ATOM   11395 C  CA  . TYR B  1 700 ? 9.115   55.629 53.597 1.00 19.99 ? 700  TYR B CA  1 
ATOM   11396 C  C   . TYR B  1 700 ? 9.642   54.728 52.493 1.00 19.47 ? 700  TYR B C   1 
ATOM   11397 O  O   . TYR B  1 700 ? 10.802  54.322 52.520 1.00 18.22 ? 700  TYR B O   1 
ATOM   11398 C  CB  . TYR B  1 700 ? 9.590   57.075 53.374 1.00 19.82 ? 700  TYR B CB  1 
ATOM   11399 C  CG  . TYR B  1 700 ? 9.194   57.784 52.096 1.00 19.74 ? 700  TYR B CG  1 
ATOM   11400 C  CD1 . TYR B  1 700 ? 7.869   57.840 51.681 1.00 19.79 ? 700  TYR B CD1 1 
ATOM   11401 C  CD2 . TYR B  1 700 ? 10.140  58.532 51.373 1.00 19.68 ? 700  TYR B CD2 1 
ATOM   11402 C  CE1 . TYR B  1 700 ? 7.482   58.634 50.582 1.00 19.99 ? 700  TYR B CE1 1 
ATOM   11403 C  CE2 . TYR B  1 700 ? 9.763   59.328 50.278 1.00 19.17 ? 700  TYR B CE2 1 
ATOM   11404 C  CZ  . TYR B  1 700 ? 8.429   59.375 49.894 1.00 20.03 ? 700  TYR B CZ  1 
ATOM   11405 O  OH  . TYR B  1 700 ? 8.031   60.169 48.842 1.00 18.72 ? 700  TYR B OH  1 
ATOM   11406 N  N   . LEU B  1 701 ? 8.767   54.388 51.548 1.00 18.40 ? 701  LEU B N   1 
ATOM   11407 C  CA  . LEU B  1 701 ? 9.127   53.599 50.376 1.00 18.17 ? 701  LEU B CA  1 
ATOM   11408 C  C   . LEU B  1 701 ? 8.724   54.475 49.187 1.00 19.46 ? 701  LEU B C   1 
ATOM   11409 O  O   . LEU B  1 701 ? 7.543   54.843 49.048 1.00 20.02 ? 701  LEU B O   1 
ATOM   11410 C  CB  . LEU B  1 701 ? 8.360   52.277 50.351 1.00 17.95 ? 701  LEU B CB  1 
ATOM   11411 C  CG  . LEU B  1 701 ? 8.401   51.426 49.063 1.00 17.77 ? 701  LEU B CG  1 
ATOM   11412 C  CD1 . LEU B  1 701 ? 9.839   51.170 48.617 1.00 17.60 ? 701  LEU B CD1 1 
ATOM   11413 C  CD2 . LEU B  1 701 ? 7.699   50.125 49.312 1.00 13.67 ? 701  LEU B CD2 1 
ATOM   11414 N  N   . LEU B  1 702 ? 9.716   54.841 48.369 1.00 19.67 ? 702  LEU B N   1 
ATOM   11415 C  CA  . LEU B  1 702 ? 9.539   55.692 47.182 1.00 18.21 ? 702  LEU B CA  1 
ATOM   11416 C  C   . LEU B  1 702 ? 9.726   54.852 45.923 1.00 18.45 ? 702  LEU B C   1 
ATOM   11417 O  O   . LEU B  1 702 ? 10.743  54.203 45.758 1.00 19.31 ? 702  LEU B O   1 
ATOM   11418 C  CB  . LEU B  1 702 ? 10.565  56.824 47.209 1.00 18.21 ? 702  LEU B CB  1 
ATOM   11419 C  CG  . LEU B  1 702 ? 10.607  57.801 46.029 1.00 17.33 ? 702  LEU B CG  1 
ATOM   11420 C  CD1 . LEU B  1 702 ? 9.281   58.541 45.919 1.00 13.14 ? 702  LEU B CD1 1 
ATOM   11421 C  CD2 . LEU B  1 702 ? 11.769  58.793 46.213 1.00 15.84 ? 702  LEU B CD2 1 
ATOM   11422 N  N   . ILE B  1 703 ? 8.744   54.881 45.031 1.00 17.28 ? 703  ILE B N   1 
ATOM   11423 C  CA  . ILE B  1 703 ? 8.764   54.076 43.817 1.00 16.80 ? 703  ILE B CA  1 
ATOM   11424 C  C   . ILE B  1 703 ? 8.432   54.911 42.573 1.00 16.49 ? 703  ILE B C   1 
ATOM   11425 O  O   . ILE B  1 703 ? 7.514   55.734 42.603 1.00 16.07 ? 703  ILE B O   1 
ATOM   11426 C  CB  . ILE B  1 703 ? 7.706   52.930 43.929 1.00 17.14 ? 703  ILE B CB  1 
ATOM   11427 C  CG1 . ILE B  1 703 ? 7.956   52.103 45.200 1.00 17.61 ? 703  ILE B CG1 1 
ATOM   11428 C  CG2 . ILE B  1 703 ? 7.711   52.061 42.666 1.00 16.05 ? 703  ILE B CG2 1 
ATOM   11429 C  CD1 . ILE B  1 703 ? 6.894   51.034 45.487 1.00 14.41 ? 703  ILE B CD1 1 
ATOM   11430 N  N   . HIS B  1 704 ? 9.153   54.683 41.476 1.00 16.43 ? 704  HIS B N   1 
ATOM   11431 C  CA  . HIS B  1 704 ? 8.895   55.448 40.236 1.00 16.43 ? 704  HIS B CA  1 
ATOM   11432 C  C   . HIS B  1 704 ? 9.416   54.726 38.973 1.00 15.64 ? 704  HIS B C   1 
ATOM   11433 O  O   . HIS B  1 704 ? 10.478  54.115 38.988 1.00 16.06 ? 704  HIS B O   1 
ATOM   11434 C  CB  . HIS B  1 704 ? 9.548   56.840 40.351 1.00 14.63 ? 704  HIS B CB  1 
ATOM   11435 C  CG  . HIS B  1 704 ? 8.817   57.929 39.622 1.00 16.28 ? 704  HIS B CG  1 
ATOM   11436 N  ND1 . HIS B  1 704 ? 8.539   59.151 40.203 1.00 13.56 ? 704  HIS B ND1 1 
ATOM   11437 C  CD2 . HIS B  1 704 ? 8.309   57.987 38.364 1.00 15.43 ? 704  HIS B CD2 1 
ATOM   11438 C  CE1 . HIS B  1 704 ? 7.889   59.909 39.338 1.00 17.38 ? 704  HIS B CE1 1 
ATOM   11439 N  NE2 . HIS B  1 704 ? 7.735   59.225 38.214 1.00 16.57 ? 704  HIS B NE2 1 
ATOM   11440 N  N   . GLY B  1 705 ? 8.650   54.778 37.891 1.00 16.02 ? 705  GLY B N   1 
ATOM   11441 C  CA  . GLY B  1 705 ? 9.098   54.158 36.656 1.00 15.98 ? 705  GLY B CA  1 
ATOM   11442 C  C   . GLY B  1 705 ? 10.041  55.136 35.964 1.00 16.68 ? 705  GLY B C   1 
ATOM   11443 O  O   . GLY B  1 705 ? 9.783   56.351 35.940 1.00 16.31 ? 705  GLY B O   1 
ATOM   11444 N  N   . THR B  1 706 ? 11.135  54.633 35.405 1.00 15.75 ? 706  THR B N   1 
ATOM   11445 C  CA  . THR B  1 706 ? 12.098  55.507 34.744 1.00 15.75 ? 706  THR B CA  1 
ATOM   11446 C  C   . THR B  1 706 ? 11.626  56.111 33.424 1.00 16.49 ? 706  THR B C   1 
ATOM   11447 O  O   . THR B  1 706 ? 12.174  57.109 32.989 1.00 18.20 ? 706  THR B O   1 
ATOM   11448 C  CB  . THR B  1 706 ? 13.419  54.771 34.496 1.00 15.73 ? 706  THR B CB  1 
ATOM   11449 O  OG1 . THR B  1 706 ? 13.215  53.693 33.568 1.00 15.79 ? 706  THR B OG1 1 
ATOM   11450 C  CG2 . THR B  1 706 ? 13.933  54.222 35.799 1.00 12.60 ? 706  THR B CG2 1 
ATOM   11451 N  N   . ALA B  1 707 ? 10.618  55.525 32.788 1.00 16.42 ? 707  ALA B N   1 
ATOM   11452 C  CA  . ALA B  1 707 ? 10.135  56.060 31.519 1.00 15.47 ? 707  ALA B CA  1 
ATOM   11453 C  C   . ALA B  1 707 ? 8.768   56.749 31.649 1.00 16.24 ? 707  ALA B C   1 
ATOM   11454 O  O   . ALA B  1 707 ? 7.972   56.765 30.705 1.00 15.32 ? 707  ALA B O   1 
ATOM   11455 C  CB  . ALA B  1 707 ? 10.075  54.935 30.451 1.00 12.22 ? 707  ALA B CB  1 
ATOM   11456 N  N   . ASP B  1 708 ? 8.516   57.318 32.824 1.00 16.14 ? 708  ASP B N   1 
ATOM   11457 C  CA  . ASP B  1 708 ? 7.278   58.035 33.111 1.00 16.62 ? 708  ASP B CA  1 
ATOM   11458 C  C   . ASP B  1 708 ? 7.336   59.370 32.354 1.00 16.95 ? 708  ASP B C   1 
ATOM   11459 O  O   . ASP B  1 708 ? 8.096   60.270 32.712 1.00 15.96 ? 708  ASP B O   1 
ATOM   11460 C  CB  . ASP B  1 708 ? 7.160   58.288 34.622 1.00 17.37 ? 708  ASP B CB  1 
ATOM   11461 C  CG  . ASP B  1 708 ? 5.736   58.630 35.063 1.00 17.79 ? 708  ASP B CG  1 
ATOM   11462 O  OD1 . ASP B  1 708 ? 5.020   59.381 34.358 1.00 17.77 ? 708  ASP B OD1 1 
ATOM   11463 O  OD2 . ASP B  1 708 ? 5.341   58.158 36.143 1.00 17.23 ? 708  ASP B OD2 1 
ATOM   11464 N  N   . ASP B  1 709 ? 6.529   59.478 31.303 1.00 16.28 ? 709  ASP B N   1 
ATOM   11465 C  CA  . ASP B  1 709 ? 6.457   60.666 30.457 1.00 17.11 ? 709  ASP B CA  1 
ATOM   11466 C  C   . ASP B  1 709 ? 5.496   61.687 31.049 1.00 17.37 ? 709  ASP B C   1 
ATOM   11467 O  O   . ASP B  1 709 ? 5.442   62.832 30.613 1.00 17.18 ? 709  ASP B O   1 
ATOM   11468 C  CB  . ASP B  1 709 ? 5.902   60.271 29.094 1.00 17.23 ? 709  ASP B CB  1 
ATOM   11469 C  CG  . ASP B  1 709 ? 4.586   59.489 29.223 1.00 18.26 ? 709  ASP B CG  1 
ATOM   11470 O  OD1 . ASP B  1 709 ? 4.637   58.297 29.602 1.00 18.75 ? 709  ASP B OD1 1 
ATOM   11471 O  OD2 . ASP B  1 709 ? 3.506   60.068 28.977 1.00 16.00 ? 709  ASP B OD2 1 
ATOM   11472 N  N   . ASN B  1 710 ? 4.723   61.248 32.030 1.00 16.37 ? 710  ASN B N   1 
ATOM   11473 C  CA  . ASN B  1 710 ? 3.705   62.074 32.670 1.00 18.22 ? 710  ASN B CA  1 
ATOM   11474 C  C   . ASN B  1 710 ? 4.277   62.790 33.917 1.00 18.00 ? 710  ASN B C   1 
ATOM   11475 O  O   . ASN B  1 710 ? 4.499   63.993 33.892 1.00 18.81 ? 710  ASN B O   1 
ATOM   11476 C  CB  . ASN B  1 710 ? 2.543   61.151 33.020 1.00 16.89 ? 710  ASN B CB  1 
ATOM   11477 C  CG  . ASN B  1 710 ? 1.318   61.897 33.404 1.00 19.46 ? 710  ASN B CG  1 
ATOM   11478 O  OD1 . ASN B  1 710 ? 1.393   63.053 33.847 1.00 19.41 ? 710  ASN B OD1 1 
ATOM   11479 N  ND2 . ASN B  1 710 ? 0.162   61.243 33.268 1.00 19.64 ? 710  ASN B ND2 1 
ATOM   11480 N  N   . VAL B  1 711 ? 4.470   62.049 35.010 1.00 17.17 ? 711  VAL B N   1 
ATOM   11481 C  CA  . VAL B  1 711 ? 5.101   62.584 36.213 1.00 15.78 ? 711  VAL B CA  1 
ATOM   11482 C  C   . VAL B  1 711 ? 6.551   62.099 36.033 1.00 16.22 ? 711  VAL B C   1 
ATOM   11483 O  O   . VAL B  1 711 ? 6.872   60.931 36.253 1.00 15.12 ? 711  VAL B O   1 
ATOM   11484 C  CB  . VAL B  1 711 ? 4.486   61.988 37.503 1.00 16.33 ? 711  VAL B CB  1 
ATOM   11485 C  CG1 . VAL B  1 711 ? 5.277   62.450 38.733 1.00 13.30 ? 711  VAL B CG1 1 
ATOM   11486 C  CG2 . VAL B  1 711 ? 3.020   62.456 37.642 1.00 13.95 ? 711  VAL B CG2 1 
ATOM   11487 N  N   . HIS B  1 712 ? 7.430   62.996 35.604 1.00 15.95 ? 712  HIS B N   1 
ATOM   11488 C  CA  . HIS B  1 712 ? 8.818   62.605 35.331 1.00 16.93 ? 712  HIS B CA  1 
ATOM   11489 C  C   . HIS B  1 712 ? 9.589   62.029 36.508 1.00 16.49 ? 712  HIS B C   1 
ATOM   11490 O  O   . HIS B  1 712 ? 9.432   62.478 37.646 1.00 16.81 ? 712  HIS B O   1 
ATOM   11491 C  CB  . HIS B  1 712 ? 9.562   63.797 34.711 1.00 14.52 ? 712  HIS B CB  1 
ATOM   11492 C  CG  . HIS B  1 712 ? 8.798   64.437 33.594 1.00 15.72 ? 712  HIS B CG  1 
ATOM   11493 N  ND1 . HIS B  1 712 ? 8.097   63.699 32.660 1.00 17.97 ? 712  HIS B ND1 1 
ATOM   11494 C  CD2 . HIS B  1 712 ? 8.583   65.738 33.283 1.00 14.36 ? 712  HIS B CD2 1 
ATOM   11495 C  CE1 . HIS B  1 712 ? 7.482   64.517 31.820 1.00 15.76 ? 712  HIS B CE1 1 
ATOM   11496 N  NE2 . HIS B  1 712 ? 7.763   65.759 32.178 1.00 18.09 ? 712  HIS B NE2 1 
ATOM   11497 N  N   . PHE B  1 713 ? 10.401  61.012 36.219 1.00 17.16 ? 713  PHE B N   1 
ATOM   11498 C  CA  . PHE B  1 713 ? 11.242  60.348 37.227 1.00 16.95 ? 713  PHE B CA  1 
ATOM   11499 C  C   . PHE B  1 713 ? 11.911  61.460 38.015 1.00 17.00 ? 713  PHE B C   1 
ATOM   11500 O  O   . PHE B  1 713 ? 12.174  61.332 39.208 1.00 17.64 ? 713  PHE B O   1 
ATOM   11501 C  CB  . PHE B  1 713 ? 12.332  59.478 36.564 1.00 16.39 ? 713  PHE B CB  1 
ATOM   11502 C  CG  . PHE B  1 713 ? 13.144  58.669 37.547 1.00 17.11 ? 713  PHE B CG  1 
ATOM   11503 C  CD1 . PHE B  1 713 ? 12.604  57.522 38.133 1.00 16.86 ? 713  PHE B CD1 1 
ATOM   11504 C  CD2 . PHE B  1 713 ? 14.415  59.084 37.940 1.00 16.15 ? 713  PHE B CD2 1 
ATOM   11505 C  CE1 . PHE B  1 713 ? 13.314  56.802 39.096 1.00 16.75 ? 713  PHE B CE1 1 
ATOM   11506 C  CE2 . PHE B  1 713 ? 15.133  58.365 38.906 1.00 17.25 ? 713  PHE B CE2 1 
ATOM   11507 C  CZ  . PHE B  1 713 ? 14.581  57.221 39.490 1.00 16.84 ? 713  PHE B CZ  1 
ATOM   11508 N  N   . GLN B  1 714 ? 12.180  62.560 37.316 1.00 16.13 ? 714  GLN B N   1 
ATOM   11509 C  CA  . GLN B  1 714 ? 12.790  63.745 37.909 1.00 15.16 ? 714  GLN B CA  1 
ATOM   11510 C  C   . GLN B  1 714 ? 12.167  64.104 39.271 1.00 14.92 ? 714  GLN B C   1 
ATOM   11511 O  O   . GLN B  1 714 ? 12.860  64.516 40.203 1.00 14.31 ? 714  GLN B O   1 
ATOM   11512 C  CB  . GLN B  1 714 ? 12.620  64.936 36.949 1.00 14.55 ? 714  GLN B CB  1 
ATOM   11513 C  CG  . GLN B  1 714 ? 12.704  66.303 37.636 1.00 13.35 ? 714  GLN B CG  1 
ATOM   11514 C  CD  . GLN B  1 714 ? 12.201  67.425 36.775 1.00 15.35 ? 714  GLN B CD  1 
ATOM   11515 O  OE1 . GLN B  1 714 ? 11.156  67.304 36.122 1.00 16.81 ? 714  GLN B OE1 1 
ATOM   11516 N  NE2 . GLN B  1 714 ? 12.923  68.549 36.782 1.00 13.48 ? 714  GLN B NE2 1 
ATOM   11517 N  N   . GLN B  1 715 ? 10.851  63.965 39.370 1.00 14.76 ? 715  GLN B N   1 
ATOM   11518 C  CA  . GLN B  1 715 ? 10.148  64.306 40.607 1.00 14.35 ? 715  GLN B CA  1 
ATOM   11519 C  C   . GLN B  1 715 ? 10.592  63.465 41.806 1.00 14.21 ? 715  GLN B C   1 
ATOM   11520 O  O   . GLN B  1 715 ? 10.749  64.006 42.892 1.00 14.34 ? 715  GLN B O   1 
ATOM   11521 C  CB  . GLN B  1 715 ? 8.628   64.220 40.382 1.00 13.94 ? 715  GLN B CB  1 
ATOM   11522 C  CG  . GLN B  1 715 ? 8.202   65.056 39.172 1.00 14.56 ? 715  GLN B CG  1 
ATOM   11523 C  CD  . GLN B  1 715 ? 7.044   65.995 39.444 1.00 14.96 ? 715  GLN B CD  1 
ATOM   11524 O  OE1 . GLN B  1 715 ? 6.916   66.556 40.538 1.00 15.19 ? 715  GLN B OE1 1 
ATOM   11525 N  NE2 . GLN B  1 715 ? 6.204   66.193 38.432 1.00 13.18 ? 715  GLN B NE2 1 
ATOM   11526 N  N   . SER B  1 716 ? 10.807  62.161 41.621 1.00 14.04 ? 716  SER B N   1 
ATOM   11527 C  CA  . SER B  1 716 ? 11.273  61.323 42.731 1.00 15.35 ? 716  SER B CA  1 
ATOM   11528 C  C   . SER B  1 716 ? 12.783  61.439 42.902 1.00 15.52 ? 716  SER B C   1 
ATOM   11529 O  O   . SER B  1 716 ? 13.298  61.223 43.995 1.00 15.02 ? 716  SER B O   1 
ATOM   11530 C  CB  . SER B  1 716 ? 10.911  59.853 42.526 1.00 16.28 ? 716  SER B CB  1 
ATOM   11531 O  OG  . SER B  1 716 ? 9.522   59.690 42.670 1.00 15.44 ? 716  SER B OG  1 
ATOM   11532 N  N   . ALA B  1 717 ? 13.489  61.763 41.815 1.00 15.63 ? 717  ALA B N   1 
ATOM   11533 C  CA  . ALA B  1 717 ? 14.937  61.949 41.870 1.00 16.11 ? 717  ALA B CA  1 
ATOM   11534 C  C   . ALA B  1 717 ? 15.229  63.154 42.771 1.00 14.63 ? 717  ALA B C   1 
ATOM   11535 O  O   . ALA B  1 717 ? 16.242  63.191 43.468 1.00 15.91 ? 717  ALA B O   1 
ATOM   11536 C  CB  . ALA B  1 717 ? 15.519  62.178 40.437 1.00 15.43 ? 717  ALA B CB  1 
ATOM   11537 N  N   . GLN B  1 718 ? 14.338  64.135 42.776 1.00 13.72 ? 718  GLN B N   1 
ATOM   11538 C  CA  . GLN B  1 718 ? 14.558  65.300 43.645 1.00 15.90 ? 718  GLN B CA  1 
ATOM   11539 C  C   . GLN B  1 718 ? 14.163  64.984 45.093 1.00 15.56 ? 718  GLN B C   1 
ATOM   11540 O  O   . GLN B  1 718 ? 14.732  65.549 46.027 1.00 15.38 ? 718  GLN B O   1 
ATOM   11541 C  CB  . GLN B  1 718 ? 13.793  66.522 43.125 1.00 14.09 ? 718  GLN B CB  1 
ATOM   11542 C  CG  . GLN B  1 718 ? 14.357  67.042 41.807 1.00 17.11 ? 718  GLN B CG  1 
ATOM   11543 C  CD  . GLN B  1 718 ? 15.725  67.722 41.964 1.00 18.82 ? 718  GLN B CD  1 
ATOM   11544 O  OE1 . GLN B  1 718 ? 16.299  67.745 43.047 1.00 21.55 ? 718  GLN B OE1 1 
ATOM   11545 N  NE2 . GLN B  1 718 ? 16.236  68.289 40.879 1.00 17.41 ? 718  GLN B NE2 1 
ATOM   11546 N  N   . ILE B  1 719 ? 13.198  64.084 45.286 1.00 15.96 ? 719  ILE B N   1 
ATOM   11547 C  CA  . ILE B  1 719 ? 12.803  63.718 46.635 1.00 16.31 ? 719  ILE B CA  1 
ATOM   11548 C  C   . ILE B  1 719 ? 13.926  62.922 47.304 1.00 17.67 ? 719  ILE B C   1 
ATOM   11549 O  O   . ILE B  1 719 ? 14.300  63.185 48.454 1.00 18.14 ? 719  ILE B O   1 
ATOM   11550 C  CB  . ILE B  1 719 ? 11.521  62.862 46.656 1.00 16.38 ? 719  ILE B CB  1 
ATOM   11551 C  CG1 . ILE B  1 719 ? 10.294  63.720 46.368 1.00 15.72 ? 719  ILE B CG1 1 
ATOM   11552 C  CG2 . ILE B  1 719 ? 11.348  62.237 48.027 1.00 14.66 ? 719  ILE B CG2 1 
ATOM   11553 C  CD1 . ILE B  1 719 ? 9.039   62.901 46.127 1.00 16.72 ? 719  ILE B CD1 1 
ATOM   11554 N  N   . SER B  1 720 ? 14.464  61.948 46.584 1.00 17.73 ? 720  SER B N   1 
ATOM   11555 C  CA  . SER B  1 720 ? 15.525  61.134 47.143 1.00 18.24 ? 720  SER B CA  1 
ATOM   11556 C  C   . SER B  1 720 ? 16.756  61.975 47.463 1.00 18.86 ? 720  SER B C   1 
ATOM   11557 O  O   . SER B  1 720 ? 17.348  61.822 48.530 1.00 18.60 ? 720  SER B O   1 
ATOM   11558 C  CB  . SER B  1 720 ? 15.901  60.009 46.186 1.00 17.39 ? 720  SER B CB  1 
ATOM   11559 O  OG  . SER B  1 720 ? 16.460  60.527 45.005 1.00 16.17 ? 720  SER B OG  1 
ATOM   11560 N  N   . LYS B  1 721 ? 17.146  62.858 46.546 1.00 18.65 ? 721  LYS B N   1 
ATOM   11561 C  CA  . LYS B  1 721 ? 18.313  63.700 46.791 1.00 17.71 ? 721  LYS B CA  1 
ATOM   11562 C  C   . LYS B  1 721 ? 18.112  64.541 48.051 1.00 18.12 ? 721  LYS B C   1 
ATOM   11563 O  O   . LYS B  1 721 ? 19.026  64.656 48.872 1.00 16.76 ? 721  LYS B O   1 
ATOM   11564 C  CB  . LYS B  1 721 ? 18.592  64.632 45.599 1.00 16.91 ? 721  LYS B CB  1 
ATOM   11565 C  CG  . LYS B  1 721 ? 19.853  65.490 45.758 1.00 14.94 ? 721  LYS B CG  1 
ATOM   11566 C  CD  . LYS B  1 721 ? 20.488  65.881 44.408 1.00 16.86 ? 721  LYS B CD  1 
ATOM   11567 C  CE  . LYS B  1 721 ? 19.515  66.581 43.462 1.00 15.99 ? 721  LYS B CE  1 
ATOM   11568 N  NZ  . LYS B  1 721 ? 19.064  67.915 43.942 1.00 18.46 ? 721  LYS B NZ  1 
ATOM   11569 N  N   . ALA B  1 722 ? 16.922  65.126 48.196 1.00 17.33 ? 722  ALA B N   1 
ATOM   11570 C  CA  . ALA B  1 722 ? 16.623  65.961 49.360 1.00 18.12 ? 722  ALA B CA  1 
ATOM   11571 C  C   . ALA B  1 722 ? 16.698  65.132 50.650 1.00 18.66 ? 722  ALA B C   1 
ATOM   11572 O  O   . ALA B  1 722 ? 17.154  65.629 51.690 1.00 18.00 ? 722  ALA B O   1 
ATOM   11573 C  CB  . ALA B  1 722 ? 15.233  66.621 49.220 1.00 16.85 ? 722  ALA B CB  1 
ATOM   11574 N  N   . LEU B  1 723 ? 16.281  63.870 50.583 1.00 17.41 ? 723  LEU B N   1 
ATOM   11575 C  CA  . LEU B  1 723 ? 16.332  63.005 51.765 1.00 17.21 ? 723  LEU B CA  1 
ATOM   11576 C  C   . LEU B  1 723 ? 17.776  62.601 52.077 1.00 17.89 ? 723  LEU B C   1 
ATOM   11577 O  O   . LEU B  1 723 ? 18.163  62.497 53.236 1.00 18.71 ? 723  LEU B O   1 
ATOM   11578 C  CB  . LEU B  1 723 ? 15.458  61.759 51.560 1.00 16.13 ? 723  LEU B CB  1 
ATOM   11579 C  CG  . LEU B  1 723 ? 13.936  62.013 51.518 1.00 15.73 ? 723  LEU B CG  1 
ATOM   11580 C  CD1 . LEU B  1 723 ? 13.229  60.719 51.134 1.00 15.01 ? 723  LEU B CD1 1 
ATOM   11581 C  CD2 . LEU B  1 723 ? 13.429  62.508 52.873 1.00 14.17 ? 723  LEU B CD2 1 
ATOM   11582 N  N   . VAL B  1 724 ? 18.575  62.364 51.044 1.00 17.89 ? 724  VAL B N   1 
ATOM   11583 C  CA  . VAL B  1 724 ? 19.973  62.007 51.246 1.00 18.55 ? 724  VAL B CA  1 
ATOM   11584 C  C   . VAL B  1 724 ? 20.681  63.223 51.859 1.00 20.35 ? 724  VAL B C   1 
ATOM   11585 O  O   . VAL B  1 724 ? 21.493  63.092 52.781 1.00 20.55 ? 724  VAL B O   1 
ATOM   11586 C  CB  . VAL B  1 724 ? 20.648  61.621 49.906 1.00 17.18 ? 724  VAL B CB  1 
ATOM   11587 C  CG1 . VAL B  1 724 ? 22.161  61.477 50.089 1.00 16.08 ? 724  VAL B CG1 1 
ATOM   11588 C  CG2 . VAL B  1 724 ? 20.056  60.314 49.398 1.00 18.42 ? 724  VAL B CG2 1 
ATOM   11589 N  N   . ASP B  1 725 ? 20.341  64.406 51.354 1.00 21.00 ? 725  ASP B N   1 
ATOM   11590 C  CA  . ASP B  1 725 ? 20.938  65.636 51.833 1.00 22.56 ? 725  ASP B CA  1 
ATOM   11591 C  C   . ASP B  1 725 ? 20.701  65.935 53.317 1.00 22.88 ? 725  ASP B C   1 
ATOM   11592 O  O   . ASP B  1 725 ? 21.507  66.626 53.922 1.00 23.05 ? 725  ASP B O   1 
ATOM   11593 C  CB  . ASP B  1 725 ? 20.483  66.803 50.964 1.00 25.52 ? 725  ASP B CB  1 
ATOM   11594 C  CG  . ASP B  1 725 ? 21.255  66.882 49.629 1.00 28.44 ? 725  ASP B CG  1 
ATOM   11595 O  OD1 . ASP B  1 725 ? 21.843  65.872 49.186 1.00 30.10 ? 725  ASP B OD1 1 
ATOM   11596 O  OD2 . ASP B  1 725 ? 21.257  67.964 49.018 1.00 32.75 ? 725  ASP B OD2 1 
ATOM   11597 N  N   . VAL B  1 726 ? 19.624  65.424 53.914 1.00 23.05 ? 726  VAL B N   1 
ATOM   11598 C  CA  . VAL B  1 726 ? 19.390  65.667 55.341 1.00 23.24 ? 726  VAL B CA  1 
ATOM   11599 C  C   . VAL B  1 726 ? 19.640  64.414 56.164 1.00 24.06 ? 726  VAL B C   1 
ATOM   11600 O  O   . VAL B  1 726 ? 19.319  64.372 57.346 1.00 22.84 ? 726  VAL B O   1 
ATOM   11601 C  CB  . VAL B  1 726 ? 17.949  66.171 55.662 1.00 24.56 ? 726  VAL B CB  1 
ATOM   11602 C  CG1 . VAL B  1 726 ? 17.710  67.547 54.999 1.00 24.55 ? 726  VAL B CG1 1 
ATOM   11603 C  CG2 . VAL B  1 726 ? 16.913  65.140 55.223 1.00 24.11 ? 726  VAL B CG2 1 
ATOM   11604 N  N   . GLY B  1 727 ? 20.208  63.392 55.532 1.00 24.45 ? 727  GLY B N   1 
ATOM   11605 C  CA  . GLY B  1 727 ? 20.518  62.173 56.247 1.00 24.48 ? 727  GLY B CA  1 
ATOM   11606 C  C   . GLY B  1 727 ? 19.350  61.314 56.689 1.00 25.47 ? 727  GLY B C   1 
ATOM   11607 O  O   . GLY B  1 727 ? 19.349  60.784 57.801 1.00 26.07 ? 727  GLY B O   1 
ATOM   11608 N  N   . VAL B  1 728 ? 18.353  61.161 55.825 1.00 25.11 ? 728  VAL B N   1 
ATOM   11609 C  CA  . VAL B  1 728 ? 17.204  60.324 56.147 1.00 23.44 ? 728  VAL B CA  1 
ATOM   11610 C  C   . VAL B  1 728 ? 17.251  58.987 55.411 1.00 22.91 ? 728  VAL B C   1 
ATOM   11611 O  O   . VAL B  1 728 ? 17.382  58.950 54.190 1.00 22.73 ? 728  VAL B O   1 
ATOM   11612 C  CB  . VAL B  1 728 ? 15.883  61.028 55.770 1.00 24.21 ? 728  VAL B CB  1 
ATOM   11613 C  CG1 . VAL B  1 728 ? 14.692  60.126 56.095 1.00 22.84 ? 728  VAL B CG1 1 
ATOM   11614 C  CG2 . VAL B  1 728 ? 15.775  62.344 56.514 1.00 23.53 ? 728  VAL B CG2 1 
ATOM   11615 N  N   . ASP B  1 729 ? 17.138  57.884 56.136 1.00 22.24 ? 729  ASP B N   1 
ATOM   11616 C  CA  . ASP B  1 729 ? 17.144  56.589 55.463 1.00 22.62 ? 729  ASP B CA  1 
ATOM   11617 C  C   . ASP B  1 729 ? 15.720  56.290 54.992 1.00 21.87 ? 729  ASP B C   1 
ATOM   11618 O  O   . ASP B  1 729 ? 14.755  56.687 55.635 1.00 20.36 ? 729  ASP B O   1 
ATOM   11619 C  CB  . ASP B  1 729 ? 17.611  55.484 56.409 1.00 24.42 ? 729  ASP B CB  1 
ATOM   11620 C  CG  . ASP B  1 729 ? 17.749  54.138 55.710 1.00 26.34 ? 729  ASP B CG  1 
ATOM   11621 O  OD1 . ASP B  1 729 ? 18.414  54.079 54.648 1.00 27.26 ? 729  ASP B OD1 1 
ATOM   11622 O  OD2 . ASP B  1 729 ? 17.194  53.136 56.218 1.00 26.99 ? 729  ASP B OD2 1 
ATOM   11623 N  N   . PHE B  1 730 ? 15.600  55.609 53.859 1.00 20.30 ? 730  PHE B N   1 
ATOM   11624 C  CA  . PHE B  1 730 ? 14.300  55.247 53.299 1.00 19.18 ? 730  PHE B CA  1 
ATOM   11625 C  C   . PHE B  1 730 ? 14.466  54.102 52.317 1.00 19.52 ? 730  PHE B C   1 
ATOM   11626 O  O   . PHE B  1 730 ? 15.583  53.680 52.014 1.00 20.54 ? 730  PHE B O   1 
ATOM   11627 C  CB  . PHE B  1 730 ? 13.661  56.437 52.574 1.00 18.65 ? 730  PHE B CB  1 
ATOM   11628 C  CG  . PHE B  1 730 ? 14.476  56.957 51.410 1.00 17.34 ? 730  PHE B CG  1 
ATOM   11629 C  CD1 . PHE B  1 730 ? 15.601  57.743 51.623 1.00 16.19 ? 730  PHE B CD1 1 
ATOM   11630 C  CD2 . PHE B  1 730 ? 14.116  56.652 50.101 1.00 16.28 ? 730  PHE B CD2 1 
ATOM   11631 C  CE1 . PHE B  1 730 ? 16.358  58.220 50.540 1.00 16.39 ? 730  PHE B CE1 1 
ATOM   11632 C  CE2 . PHE B  1 730 ? 14.864  57.126 49.019 1.00 14.46 ? 730  PHE B CE2 1 
ATOM   11633 C  CZ  . PHE B  1 730 ? 15.986  57.908 49.235 1.00 14.50 ? 730  PHE B CZ  1 
ATOM   11634 N  N   . GLN B  1 731 ? 13.350  53.591 51.831 1.00 20.28 ? 731  GLN B N   1 
ATOM   11635 C  CA  . GLN B  1 731 ? 13.358  52.491 50.875 1.00 21.67 ? 731  GLN B CA  1 
ATOM   11636 C  C   . GLN B  1 731 ? 13.030  53.040 49.486 1.00 20.22 ? 731  GLN B C   1 
ATOM   11637 O  O   . GLN B  1 731 ? 12.231  53.955 49.350 1.00 19.39 ? 731  GLN B O   1 
ATOM   11638 C  CB  . GLN B  1 731 ? 12.301  51.456 51.249 1.00 24.92 ? 731  GLN B CB  1 
ATOM   11639 C  CG  . GLN B  1 731 ? 12.485  50.786 52.594 1.00 31.38 ? 731  GLN B CG  1 
ATOM   11640 C  CD  . GLN B  1 731 ? 13.484  49.676 52.524 1.00 34.93 ? 731  GLN B CD  1 
ATOM   11641 O  OE1 . GLN B  1 731 ? 14.685  49.911 52.633 1.00 38.05 ? 731  GLN B OE1 1 
ATOM   11642 N  NE2 . GLN B  1 731 ? 13.000  48.449 52.301 1.00 37.18 ? 731  GLN B NE2 1 
ATOM   11643 N  N   . ALA B  1 732 ? 13.635  52.468 48.455 1.00 18.46 ? 732  ALA B N   1 
ATOM   11644 C  CA  . ALA B  1 732 ? 13.357  52.927 47.113 1.00 17.35 ? 732  ALA B CA  1 
ATOM   11645 C  C   . ALA B  1 732 ? 13.311  51.788 46.111 1.00 17.00 ? 732  ALA B C   1 
ATOM   11646 O  O   . ALA B  1 732 ? 13.832  50.698 46.360 1.00 16.45 ? 732  ALA B O   1 
ATOM   11647 C  CB  . ALA B  1 732 ? 14.395  53.969 46.682 1.00 16.98 ? 732  ALA B CB  1 
ATOM   11648 N  N   . MET B  1 733 ? 12.647  52.049 44.992 1.00 16.55 ? 733  MET B N   1 
ATOM   11649 C  CA  . MET B  1 733 ? 12.546  51.086 43.907 1.00 17.24 ? 733  MET B CA  1 
ATOM   11650 C  C   . MET B  1 733 ? 12.214  51.836 42.615 1.00 18.20 ? 733  MET B C   1 
ATOM   11651 O  O   . MET B  1 733 ? 11.250  52.622 42.570 1.00 18.03 ? 733  MET B O   1 
ATOM   11652 C  CB  . MET B  1 733 ? 11.457  50.060 44.191 1.00 15.89 ? 733  MET B CB  1 
ATOM   11653 C  CG  . MET B  1 733 ? 11.257  49.084 43.062 1.00 17.12 ? 733  MET B CG  1 
ATOM   11654 S  SD  . MET B  1 733 ? 12.715  48.024 42.793 1.00 21.65 ? 733  MET B SD  1 
ATOM   11655 C  CE  . MET B  1 733 ? 12.742  47.135 44.387 1.00 16.26 ? 733  MET B CE  1 
ATOM   11656 N  N   . TRP B  1 734 ? 13.023  51.617 41.583 1.00 16.55 ? 734  TRP B N   1 
ATOM   11657 C  CA  . TRP B  1 734 ? 12.769  52.234 40.283 1.00 16.83 ? 734  TRP B CA  1 
ATOM   11658 C  C   . TRP B  1 734 ? 12.308  51.078 39.420 1.00 17.15 ? 734  TRP B C   1 
ATOM   11659 O  O   . TRP B  1 734 ? 12.677  49.930 39.693 1.00 17.33 ? 734  TRP B O   1 
ATOM   11660 C  CB  . TRP B  1 734 ? 14.052  52.858 39.684 1.00 15.79 ? 734  TRP B CB  1 
ATOM   11661 C  CG  . TRP B  1 734 ? 15.083  51.870 39.153 1.00 15.76 ? 734  TRP B CG  1 
ATOM   11662 C  CD1 . TRP B  1 734 ? 15.027  51.195 37.964 1.00 16.42 ? 734  TRP B CD1 1 
ATOM   11663 C  CD2 . TRP B  1 734 ? 16.301  51.438 39.796 1.00 15.63 ? 734  TRP B CD2 1 
ATOM   11664 N  NE1 . TRP B  1 734 ? 16.121  50.377 37.831 1.00 15.86 ? 734  TRP B NE1 1 
ATOM   11665 C  CE2 . TRP B  1 734 ? 16.918  50.505 38.935 1.00 14.88 ? 734  TRP B CE2 1 
ATOM   11666 C  CE3 . TRP B  1 734 ? 16.929  51.750 41.015 1.00 14.80 ? 734  TRP B CE3 1 
ATOM   11667 C  CZ2 . TRP B  1 734 ? 18.137  49.879 39.250 1.00 14.57 ? 734  TRP B CZ2 1 
ATOM   11668 C  CZ3 . TRP B  1 734 ? 18.133  51.131 41.329 1.00 13.12 ? 734  TRP B CZ3 1 
ATOM   11669 C  CH2 . TRP B  1 734 ? 18.727  50.205 40.448 1.00 14.11 ? 734  TRP B CH2 1 
ATOM   11670 N  N   . TYR B  1 735 ? 11.482  51.355 38.418 1.00 15.72 ? 735  TYR B N   1 
ATOM   11671 C  CA  . TYR B  1 735 ? 11.047  50.299 37.498 1.00 16.49 ? 735  TYR B CA  1 
ATOM   11672 C  C   . TYR B  1 735 ? 11.499  50.677 36.092 1.00 16.17 ? 735  TYR B C   1 
ATOM   11673 O  O   . TYR B  1 735 ? 10.946  51.567 35.457 1.00 15.59 ? 735  TYR B O   1 
ATOM   11674 C  CB  . TYR B  1 735 ? 9.532   50.111 37.554 1.00 14.85 ? 735  TYR B CB  1 
ATOM   11675 C  CG  . TYR B  1 735 ? 9.162   49.193 38.681 1.00 15.81 ? 735  TYR B CG  1 
ATOM   11676 C  CD1 . TYR B  1 735 ? 9.371   47.808 38.576 1.00 16.66 ? 735  TYR B CD1 1 
ATOM   11677 C  CD2 . TYR B  1 735 ? 8.732   49.702 39.899 1.00 14.95 ? 735  TYR B CD2 1 
ATOM   11678 C  CE1 . TYR B  1 735 ? 9.172   46.978 39.663 1.00 14.81 ? 735  TYR B CE1 1 
ATOM   11679 C  CE2 . TYR B  1 735 ? 8.532   48.879 40.982 1.00 14.38 ? 735  TYR B CE2 1 
ATOM   11680 C  CZ  . TYR B  1 735 ? 8.756   47.536 40.868 1.00 15.80 ? 735  TYR B CZ  1 
ATOM   11681 O  OH  . TYR B  1 735 ? 8.608   46.764 41.992 1.00 18.93 ? 735  TYR B OH  1 
ATOM   11682 N  N   . THR B  1 736 ? 12.540  50.003 35.637 1.00 17.19 ? 736  THR B N   1 
ATOM   11683 C  CA  . THR B  1 736 ? 13.112  50.257 34.328 1.00 16.88 ? 736  THR B CA  1 
ATOM   11684 C  C   . THR B  1 736 ? 12.119  50.238 33.179 1.00 17.35 ? 736  THR B C   1 
ATOM   11685 O  O   . THR B  1 736 ? 11.389  49.272 32.999 1.00 18.14 ? 736  THR B O   1 
ATOM   11686 C  CB  . THR B  1 736 ? 14.221  49.243 34.002 1.00 16.44 ? 736  THR B CB  1 
ATOM   11687 O  OG1 . THR B  1 736 ? 15.270  49.388 34.959 1.00 17.59 ? 736  THR B OG1 1 
ATOM   11688 C  CG2 . THR B  1 736 ? 14.777  49.486 32.574 1.00 16.44 ? 736  THR B CG2 1 
ATOM   11689 N  N   . ASP B  1 737 ? 12.107  51.324 32.411 1.00 17.59 ? 737  ASP B N   1 
ATOM   11690 C  CA  . ASP B  1 737 ? 11.246  51.491 31.237 1.00 16.41 ? 737  ASP B CA  1 
ATOM   11691 C  C   . ASP B  1 737 ? 9.745   51.438 31.467 1.00 17.71 ? 737  ASP B C   1 
ATOM   11692 O  O   . ASP B  1 737 ? 8.994   51.239 30.515 1.00 17.23 ? 737  ASP B O   1 
ATOM   11693 C  CB  . ASP B  1 737 ? 11.613  50.469 30.160 1.00 17.21 ? 737  ASP B CB  1 
ATOM   11694 C  CG  . ASP B  1 737 ? 12.977  50.728 29.557 1.00 17.63 ? 737  ASP B CG  1 
ATOM   11695 O  OD1 . ASP B  1 737 ? 13.587  51.758 29.888 1.00 18.49 ? 737  ASP B OD1 1 
ATOM   11696 O  OD2 . ASP B  1 737 ? 13.443  49.907 28.744 1.00 18.66 ? 737  ASP B OD2 1 
ATOM   11697 N  N   . GLU B  1 738 ? 9.297   51.609 32.711 1.00 17.63 ? 738  GLU B N   1 
ATOM   11698 C  CA  . GLU B  1 738 ? 7.858   51.615 32.993 1.00 17.49 ? 738  GLU B CA  1 
ATOM   11699 C  C   . GLU B  1 738 ? 7.430   53.078 33.034 1.00 18.27 ? 738  GLU B C   1 
ATOM   11700 O  O   . GLU B  1 738 ? 8.231   53.956 33.373 1.00 18.03 ? 738  GLU B O   1 
ATOM   11701 C  CB  . GLU B  1 738 ? 7.558   50.944 34.356 1.00 17.86 ? 738  GLU B CB  1 
ATOM   11702 C  CG  . GLU B  1 738 ? 7.688   49.413 34.375 1.00 18.85 ? 738  GLU B CG  1 
ATOM   11703 C  CD  . GLU B  1 738 ? 6.739   48.739 33.382 1.00 21.70 ? 738  GLU B CD  1 
ATOM   11704 O  OE1 . GLU B  1 738 ? 5.524   48.986 33.472 1.00 22.72 ? 738  GLU B OE1 1 
ATOM   11705 O  OE2 . GLU B  1 738 ? 7.193   47.968 32.509 1.00 24.51 ? 738  GLU B OE2 1 
ATOM   11706 N  N   . ASP B  1 739 ? 6.177   53.347 32.679 1.00 18.97 ? 739  ASP B N   1 
ATOM   11707 C  CA  . ASP B  1 739 ? 5.692   54.710 32.715 1.00 19.18 ? 739  ASP B CA  1 
ATOM   11708 C  C   . ASP B  1 739 ? 4.828   54.966 33.956 1.00 19.21 ? 739  ASP B C   1 
ATOM   11709 O  O   . ASP B  1 739 ? 4.932   54.240 34.953 1.00 20.69 ? 739  ASP B O   1 
ATOM   11710 C  CB  . ASP B  1 739 ? 4.942   55.049 31.424 1.00 20.33 ? 739  ASP B CB  1 
ATOM   11711 C  CG  . ASP B  1 739 ? 3.656   54.250 31.253 1.00 21.62 ? 739  ASP B CG  1 
ATOM   11712 O  OD1 . ASP B  1 739 ? 3.096   53.730 32.251 1.00 20.56 ? 739  ASP B OD1 1 
ATOM   11713 O  OD2 . ASP B  1 739 ? 3.201   54.174 30.106 1.00 20.11 ? 739  ASP B OD2 1 
ATOM   11714 N  N   . HIS B  1 740 ? 3.990   55.993 33.909 1.00 18.38 ? 740  HIS B N   1 
ATOM   11715 C  CA  . HIS B  1 740 ? 3.166   56.347 35.053 1.00 19.36 ? 740  HIS B CA  1 
ATOM   11716 C  C   . HIS B  1 740 ? 2.216   55.239 35.512 1.00 21.29 ? 740  HIS B C   1 
ATOM   11717 O  O   . HIS B  1 740 ? 1.782   55.233 36.666 1.00 21.70 ? 740  HIS B O   1 
ATOM   11718 C  CB  . HIS B  1 740 ? 2.373   57.629 34.760 1.00 19.19 ? 740  HIS B CB  1 
ATOM   11719 C  CG  . HIS B  1 740 ? 1.891   58.333 35.990 1.00 17.95 ? 740  HIS B CG  1 
ATOM   11720 N  ND1 . HIS B  1 740 ? 2.741   58.715 37.012 1.00 18.05 ? 740  HIS B ND1 1 
ATOM   11721 C  CD2 . HIS B  1 740 ? 0.653   58.737 36.369 1.00 17.32 ? 740  HIS B CD2 1 
ATOM   11722 C  CE1 . HIS B  1 740 ? 2.049   59.320 37.958 1.00 18.30 ? 740  HIS B CE1 1 
ATOM   11723 N  NE2 . HIS B  1 740 ? 0.776   59.347 37.592 1.00 17.15 ? 740  HIS B NE2 1 
ATOM   11724 N  N   . GLY B  1 741 ? 1.892   54.310 34.612 1.00 21.81 ? 741  GLY B N   1 
ATOM   11725 C  CA  . GLY B  1 741 ? 0.991   53.229 34.967 1.00 21.21 ? 741  GLY B CA  1 
ATOM   11726 C  C   . GLY B  1 741 ? 1.663   51.985 35.546 1.00 22.14 ? 741  GLY B C   1 
ATOM   11727 O  O   . GLY B  1 741 ? 0.992   51.173 36.196 1.00 23.21 ? 741  GLY B O   1 
ATOM   11728 N  N   . ILE B  1 742 ? 2.974   51.841 35.345 1.00 21.39 ? 742  ILE B N   1 
ATOM   11729 C  CA  . ILE B  1 742 ? 3.714   50.665 35.817 1.00 21.04 ? 742  ILE B CA  1 
ATOM   11730 C  C   . ILE B  1 742 ? 2.763   49.472 35.655 1.00 22.22 ? 742  ILE B C   1 
ATOM   11731 O  O   . ILE B  1 742 ? 2.564   48.662 36.571 1.00 22.69 ? 742  ILE B O   1 
ATOM   11732 C  CB  . ILE B  1 742 ? 4.154   50.822 37.289 1.00 18.85 ? 742  ILE B CB  1 
ATOM   11733 C  CG1 . ILE B  1 742 ? 4.813   52.188 37.489 1.00 19.53 ? 742  ILE B CG1 1 
ATOM   11734 C  CG2 . ILE B  1 742 ? 5.171   49.737 37.628 1.00 17.96 ? 742  ILE B CG2 1 
ATOM   11735 C  CD1 . ILE B  1 742 ? 5.422   52.454 38.880 1.00 18.03 ? 742  ILE B CD1 1 
ATOM   11736 N  N   . ALA B  1 743 ? 2.180   49.396 34.456 1.00 23.28 ? 743  ALA B N   1 
ATOM   11737 C  CA  . ALA B  1 743 ? 1.184   48.391 34.115 1.00 23.41 ? 743  ALA B CA  1 
ATOM   11738 C  C   . ALA B  1 743 ? 1.631   47.164 33.363 1.00 23.48 ? 743  ALA B C   1 
ATOM   11739 O  O   . ALA B  1 743 ? 0.793   46.312 33.070 1.00 23.24 ? 743  ALA B O   1 
ATOM   11740 C  CB  . ALA B  1 743 ? 0.015   49.050 33.342 1.00 23.64 ? 743  ALA B CB  1 
ATOM   11741 N  N   . SER B  1 744 ? 2.908   47.048 33.010 1.00 22.80 ? 744  SER B N   1 
ATOM   11742 C  CA  . SER B  1 744 ? 3.314   45.831 32.307 1.00 23.49 ? 744  SER B CA  1 
ATOM   11743 C  C   . SER B  1 744 ? 3.032   44.677 33.289 1.00 23.19 ? 744  SER B C   1 
ATOM   11744 O  O   . SER B  1 744 ? 3.134   44.835 34.506 1.00 22.63 ? 744  SER B O   1 
ATOM   11745 C  CB  . SER B  1 744 ? 4.804   45.862 31.947 1.00 24.52 ? 744  SER B CB  1 
ATOM   11746 O  OG  . SER B  1 744 ? 5.596   45.453 33.055 1.00 27.54 ? 744  SER B OG  1 
ATOM   11747 N  N   . SER B  1 745 ? 2.673   43.523 32.753 1.00 23.09 ? 745  SER B N   1 
ATOM   11748 C  CA  . SER B  1 745 ? 2.358   42.367 33.581 1.00 23.61 ? 745  SER B CA  1 
ATOM   11749 C  C   . SER B  1 745 ? 3.405   42.030 34.663 1.00 22.42 ? 745  SER B C   1 
ATOM   11750 O  O   . SER B  1 745 ? 3.063   41.855 35.830 1.00 21.61 ? 745  SER B O   1 
ATOM   11751 C  CB  . SER B  1 745 ? 2.136   41.149 32.689 1.00 23.70 ? 745  SER B CB  1 
ATOM   11752 O  OG  . SER B  1 745 ? 1.975   39.996 33.492 1.00 29.31 ? 745  SER B OG  1 
ATOM   11753 N  N   . THR B  1 746 ? 4.674   41.932 34.282 1.00 21.40 ? 746  THR B N   1 
ATOM   11754 C  CA  . THR B  1 746 ? 5.708   41.609 35.260 1.00 20.85 ? 746  THR B CA  1 
ATOM   11755 C  C   . THR B  1 746 ? 5.924   42.705 36.298 1.00 20.66 ? 746  THR B C   1 
ATOM   11756 O  O   . THR B  1 746 ? 5.999   42.424 37.487 1.00 21.17 ? 746  THR B O   1 
ATOM   11757 C  CB  . THR B  1 746 ? 7.045   41.300 34.565 1.00 21.11 ? 746  THR B CB  1 
ATOM   11758 O  OG1 . THR B  1 746 ? 7.430   42.406 33.746 1.00 23.34 ? 746  THR B OG1 1 
ATOM   11759 C  CG2 . THR B  1 746 ? 6.898   40.069 33.679 1.00 21.41 ? 746  THR B CG2 1 
ATOM   11760 N  N   . ALA B  1 747 ? 5.999   43.956 35.848 1.00 18.91 ? 747  ALA B N   1 
ATOM   11761 C  CA  . ALA B  1 747 ? 6.232   45.077 36.749 1.00 18.37 ? 747  ALA B CA  1 
ATOM   11762 C  C   . ALA B  1 747 ? 5.079   45.216 37.745 1.00 18.17 ? 747  ALA B C   1 
ATOM   11763 O  O   . ALA B  1 747 ? 5.299   45.468 38.921 1.00 17.12 ? 747  ALA B O   1 
ATOM   11764 C  CB  . ALA B  1 747 ? 6.405   46.387 35.942 1.00 16.76 ? 747  ALA B CB  1 
ATOM   11765 N  N   . HIS B  1 748 ? 3.856   45.059 37.249 1.00 17.56 ? 748  HIS B N   1 
ATOM   11766 C  CA  . HIS B  1 748 ? 2.656   45.159 38.070 1.00 18.47 ? 748  HIS B CA  1 
ATOM   11767 C  C   . HIS B  1 748 ? 2.705   44.159 39.209 1.00 19.19 ? 748  HIS B C   1 
ATOM   11768 O  O   . HIS B  1 748 ? 2.494   44.501 40.369 1.00 19.80 ? 748  HIS B O   1 
ATOM   11769 C  CB  . HIS B  1 748 ? 1.422   44.886 37.219 1.00 19.52 ? 748  HIS B CB  1 
ATOM   11770 C  CG  . HIS B  1 748 ? 0.168   44.711 38.016 1.00 21.03 ? 748  HIS B CG  1 
ATOM   11771 N  ND1 . HIS B  1 748 ? -0.472  45.761 38.641 1.00 20.36 ? 748  HIS B ND1 1 
ATOM   11772 C  CD2 . HIS B  1 748 ? -0.580  43.610 38.268 1.00 19.64 ? 748  HIS B CD2 1 
ATOM   11773 C  CE1 . HIS B  1 748 ? -1.564  45.317 39.238 1.00 21.44 ? 748  HIS B CE1 1 
ATOM   11774 N  NE2 . HIS B  1 748 ? -1.653  44.015 39.026 1.00 23.19 ? 748  HIS B NE2 1 
ATOM   11775 N  N   . GLN B  1 749 ? 2.972   42.908 38.874 1.00 19.56 ? 749  GLN B N   1 
ATOM   11776 C  CA  . GLN B  1 749 ? 3.055   41.885 39.896 1.00 20.40 ? 749  GLN B CA  1 
ATOM   11777 C  C   . GLN B  1 749 ? 4.209   42.220 40.829 1.00 19.38 ? 749  GLN B C   1 
ATOM   11778 O  O   . GLN B  1 749 ? 4.091   42.067 42.034 1.00 19.50 ? 749  GLN B O   1 
ATOM   11779 C  CB  . GLN B  1 749 ? 3.269   40.517 39.233 1.00 20.58 ? 749  GLN B CB  1 
ATOM   11780 C  CG  . GLN B  1 749 ? 2.107   40.128 38.327 1.00 22.33 ? 749  GLN B CG  1 
ATOM   11781 C  CD  . GLN B  1 749 ? 2.346   38.823 37.618 1.00 24.31 ? 749  GLN B CD  1 
ATOM   11782 O  OE1 . GLN B  1 749 ? 2.477   37.774 38.251 1.00 26.49 ? 749  GLN B OE1 1 
ATOM   11783 N  NE2 . GLN B  1 749 ? 2.404   38.875 36.297 1.00 24.58 ? 749  GLN B NE2 1 
ATOM   11784 N  N   . HIS B  1 750 ? 5.321   42.693 40.268 1.00 18.86 ? 750  HIS B N   1 
ATOM   11785 C  CA  . HIS B  1 750 ? 6.486   43.024 41.078 1.00 17.89 ? 750  HIS B CA  1 
ATOM   11786 C  C   . HIS B  1 750 ? 6.284   44.169 42.072 1.00 18.82 ? 750  HIS B C   1 
ATOM   11787 O  O   . HIS B  1 750 ? 6.679   44.045 43.241 1.00 17.64 ? 750  HIS B O   1 
ATOM   11788 C  CB  . HIS B  1 750 ? 7.690   43.333 40.192 1.00 17.34 ? 750  HIS B CB  1 
ATOM   11789 C  CG  . HIS B  1 750 ? 9.005   43.227 40.907 1.00 18.57 ? 750  HIS B CG  1 
ATOM   11790 N  ND1 . HIS B  1 750 ? 9.563   44.273 41.611 1.00 16.82 ? 750  HIS B ND1 1 
ATOM   11791 C  CD2 . HIS B  1 750 ? 9.865   42.188 41.043 1.00 18.06 ? 750  HIS B CD2 1 
ATOM   11792 C  CE1 . HIS B  1 750 ? 10.708  43.886 42.146 1.00 17.64 ? 750  HIS B CE1 1 
ATOM   11793 N  NE2 . HIS B  1 750 ? 10.915  42.622 41.818 1.00 17.42 ? 750  HIS B NE2 1 
ATOM   11794 N  N   . ILE B  1 751 ? 5.660   45.271 41.645 1.00 17.73 ? 751  ILE B N   1 
ATOM   11795 C  CA  . ILE B  1 751 ? 5.474   46.388 42.568 1.00 17.88 ? 751  ILE B CA  1 
ATOM   11796 C  C   . ILE B  1 751 ? 4.483   46.064 43.704 1.00 18.16 ? 751  ILE B C   1 
ATOM   11797 O  O   . ILE B  1 751 ? 4.722   46.428 44.851 1.00 18.15 ? 751  ILE B O   1 
ATOM   11798 C  CB  . ILE B  1 751 ? 5.053   47.705 41.826 1.00 16.38 ? 751  ILE B CB  1 
ATOM   11799 C  CG1 . ILE B  1 751 ? 4.979   48.861 42.826 1.00 16.45 ? 751  ILE B CG1 1 
ATOM   11800 C  CG2 . ILE B  1 751 ? 3.714   47.524 41.118 1.00 17.45 ? 751  ILE B CG2 1 
ATOM   11801 C  CD1 . ILE B  1 751 ? 4.647   50.229 42.169 1.00 15.15 ? 751  ILE B CD1 1 
ATOM   11802 N  N   . TYR B  1 752 ? 3.386   45.376 43.409 1.00 18.05 ? 752  TYR B N   1 
ATOM   11803 C  CA  . TYR B  1 752 ? 2.447   45.047 44.477 1.00 17.96 ? 752  TYR B CA  1 
ATOM   11804 C  C   . TYR B  1 752 ? 3.030   44.001 45.424 1.00 17.77 ? 752  TYR B C   1 
ATOM   11805 O  O   . TYR B  1 752 ? 2.730   44.005 46.603 1.00 19.18 ? 752  TYR B O   1 
ATOM   11806 C  CB  . TYR B  1 752 ? 1.099   44.613 43.895 1.00 17.12 ? 752  TYR B CB  1 
ATOM   11807 C  CG  . TYR B  1 752 ? 0.240   45.807 43.520 1.00 15.26 ? 752  TYR B CG  1 
ATOM   11808 C  CD1 . TYR B  1 752 ? -0.355  46.598 44.498 1.00 15.15 ? 752  TYR B CD1 1 
ATOM   11809 C  CD2 . TYR B  1 752 ? 0.077   46.183 42.181 1.00 16.87 ? 752  TYR B CD2 1 
ATOM   11810 C  CE1 . TYR B  1 752 ? -1.097  47.745 44.154 1.00 15.85 ? 752  TYR B CE1 1 
ATOM   11811 C  CE2 . TYR B  1 752 ? -0.654  47.323 41.831 1.00 14.55 ? 752  TYR B CE2 1 
ATOM   11812 C  CZ  . TYR B  1 752 ? -1.237  48.098 42.829 1.00 15.20 ? 752  TYR B CZ  1 
ATOM   11813 O  OH  . TYR B  1 752 ? -1.940  49.233 42.485 1.00 17.07 ? 752  TYR B OH  1 
ATOM   11814 N  N   . THR B  1 753 ? 3.882   43.119 44.919 1.00 18.68 ? 753  THR B N   1 
ATOM   11815 C  CA  . THR B  1 753 ? 4.506   42.143 45.789 1.00 19.12 ? 753  THR B CA  1 
ATOM   11816 C  C   . THR B  1 753 ? 5.482   42.896 46.715 1.00 20.82 ? 753  THR B C   1 
ATOM   11817 O  O   . THR B  1 753 ? 5.516   42.669 47.934 1.00 22.29 ? 753  THR B O   1 
ATOM   11818 C  CB  . THR B  1 753 ? 5.281   41.095 44.983 1.00 19.49 ? 753  THR B CB  1 
ATOM   11819 O  OG1 . THR B  1 753 ? 4.364   40.278 44.245 1.00 19.60 ? 753  THR B OG1 1 
ATOM   11820 C  CG2 . THR B  1 753 ? 6.111   40.229 45.905 1.00 18.57 ? 753  THR B CG2 1 
ATOM   11821 N  N   . HIS B  1 754 ? 6.253   43.816 46.134 1.00 19.70 ? 754  HIS B N   1 
ATOM   11822 C  CA  . HIS B  1 754 ? 7.219   44.597 46.901 1.00 20.27 ? 754  HIS B CA  1 
ATOM   11823 C  C   . HIS B  1 754 ? 6.519   45.458 47.952 1.00 20.04 ? 754  HIS B C   1 
ATOM   11824 O  O   . HIS B  1 754 ? 6.984   45.575 49.075 1.00 20.56 ? 754  HIS B O   1 
ATOM   11825 C  CB  . HIS B  1 754 ? 8.046   45.500 45.973 1.00 20.05 ? 754  HIS B CB  1 
ATOM   11826 C  CG  . HIS B  1 754 ? 9.308   46.010 46.600 1.00 20.34 ? 754  HIS B CG  1 
ATOM   11827 N  ND1 . HIS B  1 754 ? 10.414  45.207 46.810 1.00 19.72 ? 754  HIS B ND1 1 
ATOM   11828 C  CD2 . HIS B  1 754 ? 9.639   47.233 47.074 1.00 18.08 ? 754  HIS B CD2 1 
ATOM   11829 C  CE1 . HIS B  1 754 ? 11.368  45.915 47.380 1.00 17.78 ? 754  HIS B CE1 1 
ATOM   11830 N  NE2 . HIS B  1 754 ? 10.924  47.149 47.552 1.00 19.11 ? 754  HIS B NE2 1 
ATOM   11831 N  N   . MET B  1 755 ? 5.407   46.082 47.582 1.00 20.46 ? 755  MET B N   1 
ATOM   11832 C  CA  . MET B  1 755 ? 4.674   46.907 48.531 1.00 20.07 ? 755  MET B CA  1 
ATOM   11833 C  C   . MET B  1 755 ? 4.040   46.063 49.663 1.00 20.04 ? 755  MET B C   1 
ATOM   11834 O  O   . MET B  1 755 ? 3.936   46.526 50.802 1.00 20.54 ? 755  MET B O   1 
ATOM   11835 C  CB  . MET B  1 755 ? 3.607   47.733 47.801 1.00 18.88 ? 755  MET B CB  1 
ATOM   11836 C  CG  . MET B  1 755 ? 4.186   48.821 46.882 1.00 21.33 ? 755  MET B CG  1 
ATOM   11837 S  SD  . MET B  1 755 ? 2.973   50.040 46.324 1.00 23.26 ? 755  MET B SD  1 
ATOM   11838 C  CE  . MET B  1 755 ? 1.982   49.029 45.204 1.00 17.74 ? 755  MET B CE  1 
ATOM   11839 N  N   . SER B  1 756 ? 3.634   44.833 49.363 1.00 19.69 ? 756  SER B N   1 
ATOM   11840 C  CA  . SER B  1 756 ? 3.042   43.974 50.388 1.00 20.89 ? 756  SER B CA  1 
ATOM   11841 C  C   . SER B  1 756 ? 4.053   43.664 51.485 1.00 21.55 ? 756  SER B C   1 
ATOM   11842 O  O   . SER B  1 756 ? 3.731   43.745 52.683 1.00 21.16 ? 756  SER B O   1 
ATOM   11843 C  CB  . SER B  1 756 ? 2.527   42.672 49.775 1.00 21.87 ? 756  SER B CB  1 
ATOM   11844 O  OG  . SER B  1 756 ? 1.492   42.927 48.826 1.00 25.46 ? 756  SER B OG  1 
ATOM   11845 N  N   . HIS B  1 757 ? 5.280   43.314 51.088 1.00 21.79 ? 757  HIS B N   1 
ATOM   11846 C  CA  . HIS B  1 757 ? 6.332   43.017 52.078 1.00 22.49 ? 757  HIS B CA  1 
ATOM   11847 C  C   . HIS B  1 757 ? 6.565   44.229 52.968 1.00 21.89 ? 757  HIS B C   1 
ATOM   11848 O  O   . HIS B  1 757 ? 6.677   44.093 54.184 1.00 23.15 ? 757  HIS B O   1 
ATOM   11849 C  CB  . HIS B  1 757 ? 7.666   42.648 51.401 1.00 22.33 ? 757  HIS B CB  1 
ATOM   11850 C  CG  . HIS B  1 757 ? 7.648   41.319 50.714 1.00 23.83 ? 757  HIS B CG  1 
ATOM   11851 N  ND1 . HIS B  1 757 ? 7.218   40.165 51.334 1.00 25.19 ? 757  HIS B ND1 1 
ATOM   11852 C  CD2 . HIS B  1 757 ? 8.018   40.958 49.463 1.00 23.97 ? 757  HIS B CD2 1 
ATOM   11853 C  CE1 . HIS B  1 757 ? 7.322   39.151 50.492 1.00 25.40 ? 757  HIS B CE1 1 
ATOM   11854 N  NE2 . HIS B  1 757 ? 7.804   39.606 49.350 1.00 24.93 ? 757  HIS B NE2 1 
ATOM   11855 N  N   . PHE B  1 758 ? 6.638   45.411 52.357 1.00 21.48 ? 758  PHE B N   1 
ATOM   11856 C  CA  . PHE B  1 758 ? 6.871   46.630 53.113 1.00 21.72 ? 758  PHE B CA  1 
ATOM   11857 C  C   . PHE B  1 758 ? 5.778   46.892 54.133 1.00 22.53 ? 758  PHE B C   1 
ATOM   11858 O  O   . PHE B  1 758 ? 6.068   47.201 55.283 1.00 24.05 ? 758  PHE B O   1 
ATOM   11859 C  CB  . PHE B  1 758 ? 6.980   47.846 52.187 1.00 20.55 ? 758  PHE B CB  1 
ATOM   11860 C  CG  . PHE B  1 758 ? 7.325   49.120 52.908 1.00 17.34 ? 758  PHE B CG  1 
ATOM   11861 C  CD1 . PHE B  1 758 ? 8.632   49.378 53.289 1.00 15.91 ? 758  PHE B CD1 1 
ATOM   11862 C  CD2 . PHE B  1 758 ? 6.345   50.071 53.177 1.00 16.84 ? 758  PHE B CD2 1 
ATOM   11863 C  CE1 . PHE B  1 758 ? 8.974   50.563 53.939 1.00 14.78 ? 758  PHE B CE1 1 
ATOM   11864 C  CE2 . PHE B  1 758 ? 6.673   51.270 53.829 1.00 16.53 ? 758  PHE B CE2 1 
ATOM   11865 C  CZ  . PHE B  1 758 ? 7.995   51.514 54.201 1.00 15.76 ? 758  PHE B CZ  1 
ATOM   11866 N  N   . ILE B  1 759 ? 4.524   46.792 53.706 1.00 24.62 ? 759  ILE B N   1 
ATOM   11867 C  CA  . ILE B  1 759 ? 3.369   47.025 54.592 1.00 25.07 ? 759  ILE B CA  1 
ATOM   11868 C  C   . ILE B  1 759 ? 3.316   46.003 55.737 1.00 25.59 ? 759  ILE B C   1 
ATOM   11869 O  O   . ILE B  1 759 ? 3.114   46.372 56.895 1.00 25.19 ? 759  ILE B O   1 
ATOM   11870 C  CB  . ILE B  1 759 ? 2.040   46.933 53.803 1.00 25.76 ? 759  ILE B CB  1 
ATOM   11871 C  CG1 . ILE B  1 759 ? 1.928   48.125 52.847 1.00 26.80 ? 759  ILE B CG1 1 
ATOM   11872 C  CG2 . ILE B  1 759 ? 0.849   46.900 54.749 1.00 25.61 ? 759  ILE B CG2 1 
ATOM   11873 C  CD1 . ILE B  1 759 ? 1.948   49.466 53.538 1.00 27.89 ? 759  ILE B CD1 1 
ATOM   11874 N  N   . LYS B  1 760 ? 3.484   44.726 55.398 1.00 25.41 ? 760  LYS B N   1 
ATOM   11875 C  CA  . LYS B  1 760 ? 3.449   43.660 56.392 1.00 26.73 ? 760  LYS B CA  1 
ATOM   11876 C  C   . LYS B  1 760 ? 4.555   43.858 57.404 1.00 28.30 ? 760  LYS B C   1 
ATOM   11877 O  O   . LYS B  1 760 ? 4.348   43.666 58.600 1.00 28.50 ? 760  LYS B O   1 
ATOM   11878 C  CB  . LYS B  1 760 ? 3.593   42.289 55.729 1.00 24.87 ? 760  LYS B CB  1 
ATOM   11879 C  CG  . LYS B  1 760 ? 2.338   41.844 54.985 1.00 25.88 ? 760  LYS B CG  1 
ATOM   11880 C  CD  . LYS B  1 760 ? 2.542   40.566 54.157 1.00 27.25 ? 760  LYS B CD  1 
ATOM   11881 C  CE  . LYS B  1 760 ? 2.537   39.319 55.033 1.00 28.80 ? 760  LYS B CE  1 
ATOM   11882 N  NZ  . LYS B  1 760 ? 2.668   38.070 54.221 1.00 31.81 ? 760  LYS B NZ  1 
ATOM   11883 N  N   . GLN B  1 761 ? 5.731   44.248 56.929 1.00 29.37 ? 761  GLN B N   1 
ATOM   11884 C  CA  . GLN B  1 761 ? 6.859   44.478 57.824 1.00 31.37 ? 761  GLN B CA  1 
ATOM   11885 C  C   . GLN B  1 761 ? 6.566   45.667 58.751 1.00 31.17 ? 761  GLN B C   1 
ATOM   11886 O  O   . GLN B  1 761 ? 6.801   45.593 59.956 1.00 31.13 ? 761  GLN B O   1 
ATOM   11887 C  CB  . GLN B  1 761 ? 8.139   44.704 56.997 1.00 33.86 ? 761  GLN B CB  1 
ATOM   11888 C  CG  . GLN B  1 761 ? 9.286   45.328 57.760 1.00 39.47 ? 761  GLN B CG  1 
ATOM   11889 C  CD  . GLN B  1 761 ? 9.219   46.860 57.810 1.00 43.29 ? 761  GLN B CD  1 
ATOM   11890 O  OE1 . GLN B  1 761 ? 9.621   47.476 58.809 1.00 45.90 ? 761  GLN B OE1 1 
ATOM   11891 N  NE2 . GLN B  1 761 ? 8.734   47.481 56.725 1.00 44.61 ? 761  GLN B NE2 1 
ATOM   11892 N  N   . CYS B  1 762 ? 6.033   46.755 58.197 1.00 31.19 ? 762  CYS B N   1 
ATOM   11893 C  CA  . CYS B  1 762 ? 5.709   47.936 59.000 1.00 31.71 ? 762  CYS B CA  1 
ATOM   11894 C  C   . CYS B  1 762 ? 4.648   47.615 60.072 1.00 31.15 ? 762  CYS B C   1 
ATOM   11895 O  O   . CYS B  1 762 ? 4.656   48.188 61.166 1.00 29.78 ? 762  CYS B O   1 
ATOM   11896 C  CB  . CYS B  1 762 ? 5.227   49.067 58.078 1.00 34.02 ? 762  CYS B CB  1 
ATOM   11897 S  SG  . CYS B  1 762 ? 4.501   50.539 58.895 1.00 38.40 ? 762  CYS B SG  1 
ATOM   11898 N  N   . PHE B  1 763 ? 3.750   46.687 59.754 1.00 30.12 ? 763  PHE B N   1 
ATOM   11899 C  CA  . PHE B  1 763 ? 2.706   46.301 60.684 1.00 31.19 ? 763  PHE B CA  1 
ATOM   11900 C  C   . PHE B  1 763 ? 3.076   45.070 61.493 1.00 32.55 ? 763  PHE B C   1 
ATOM   11901 O  O   . PHE B  1 763 ? 2.248   44.550 62.232 1.00 33.17 ? 763  PHE B O   1 
ATOM   11902 C  CB  . PHE B  1 763 ? 1.386   46.017 59.953 1.00 29.50 ? 763  PHE B CB  1 
ATOM   11903 C  CG  . PHE B  1 763 ? 0.689   47.244 59.434 1.00 26.93 ? 763  PHE B CG  1 
ATOM   11904 C  CD1 . PHE B  1 763 ? 0.993   48.503 59.938 1.00 26.67 ? 763  PHE B CD1 1 
ATOM   11905 C  CD2 . PHE B  1 763 ? -0.311  47.132 58.463 1.00 25.69 ? 763  PHE B CD2 1 
ATOM   11906 C  CE1 . PHE B  1 763 ? 0.313   49.631 59.490 1.00 25.89 ? 763  PHE B CE1 1 
ATOM   11907 C  CE2 . PHE B  1 763 ? -0.996  48.250 58.008 1.00 23.27 ? 763  PHE B CE2 1 
ATOM   11908 C  CZ  . PHE B  1 763 ? -0.687  49.497 58.520 1.00 25.63 ? 763  PHE B CZ  1 
ATOM   11909 N  N   . SER B  1 764 ? 4.307   44.591 61.344 1.00 34.37 ? 764  SER B N   1 
ATOM   11910 C  CA  . SER B  1 764 ? 4.742   43.412 62.081 1.00 37.02 ? 764  SER B CA  1 
ATOM   11911 C  C   . SER B  1 764 ? 3.822   42.230 61.802 1.00 39.38 ? 764  SER B C   1 
ATOM   11912 O  O   . SER B  1 764 ? 3.388   41.541 62.737 1.00 40.10 ? 764  SER B O   1 
ATOM   11913 C  CB  . SER B  1 764 ? 4.735   43.691 63.586 1.00 36.33 ? 764  SER B CB  1 
ATOM   11914 O  OG  . SER B  1 764 ? 5.675   44.705 63.904 1.00 36.35 ? 764  SER B OG  1 
ATOM   11915 N  N   . LEU B  1 765 ? 3.522   42.000 60.526 1.00 40.84 ? 765  LEU B N   1 
ATOM   11916 C  CA  . LEU B  1 765 ? 2.652   40.900 60.129 1.00 43.14 ? 765  LEU B CA  1 
ATOM   11917 C  C   . LEU B  1 765 ? 3.435   39.766 59.487 1.00 45.21 ? 765  LEU B C   1 
ATOM   11918 O  O   . LEU B  1 765 ? 4.210   39.988 58.557 1.00 45.55 ? 765  LEU B O   1 
ATOM   11919 C  CB  . LEU B  1 765 ? 1.582   41.383 59.142 1.00 42.16 ? 765  LEU B CB  1 
ATOM   11920 C  CG  . LEU B  1 765 ? 0.569   42.424 59.650 1.00 43.98 ? 765  LEU B CG  1 
ATOM   11921 C  CD1 . LEU B  1 765 ? -0.379  42.819 58.500 1.00 41.93 ? 765  LEU B CD1 1 
ATOM   11922 C  CD2 . LEU B  1 765 ? -0.228  41.855 60.852 1.00 42.04 ? 765  LEU B CD2 1 
ATOM   11923 N  N   . PRO B  1 766 ? 3.220   38.527 59.964 1.00 47.18 ? 766  PRO B N   1 
ATOM   11924 C  CA  . PRO B  1 766 ? 3.888   37.320 59.457 1.00 48.44 ? 766  PRO B CA  1 
ATOM   11925 C  C   . PRO B  1 766 ? 3.885   37.249 57.928 1.00 49.42 ? 766  PRO B C   1 
ATOM   11926 O  O   . PRO B  1 766 ? 4.972   37.039 57.335 1.00 50.22 ? 766  PRO B O   1 
ATOM   11927 C  CB  . PRO B  1 766 ? 3.069   36.184 60.075 1.00 48.53 ? 766  PRO B CB  1 
ATOM   11928 C  CG  . PRO B  1 766 ? 2.632   36.761 61.373 1.00 48.47 ? 766  PRO B CG  1 
ATOM   11929 C  CD  . PRO B  1 766 ? 2.219   38.174 60.989 1.00 47.69 ? 766  PRO B CD  1 
ATOM   11930 O  OXT . PRO B  1 766 ? 2.786   37.394 57.344 1.00 49.49 ? 766  PRO B OXT 1 
HETATM 11931 C  C1  . NAG C  2 .   ? 47.888  79.943 58.636 1.00 59.55 ? 1092 NAG A C1  1 
HETATM 11932 C  C2  . NAG C  2 .   ? 48.472  80.028 60.070 1.00 59.90 ? 1092 NAG A C2  1 
HETATM 11933 C  C3  . NAG C  2 .   ? 47.834  78.992 61.003 1.00 60.31 ? 1092 NAG A C3  1 
HETATM 11934 C  C4  . NAG C  2 .   ? 46.308  79.120 60.954 1.00 60.77 ? 1092 NAG A C4  1 
HETATM 11935 C  C5  . NAG C  2 .   ? 45.840  78.967 59.497 1.00 61.05 ? 1092 NAG A C5  1 
HETATM 11936 C  C6  . NAG C  2 .   ? 44.328  79.101 59.340 1.00 61.37 ? 1092 NAG A C6  1 
HETATM 11937 C  C7  . NAG C  2 .   ? 50.682  80.507 60.927 1.00 60.01 ? 1092 NAG A C7  1 
HETATM 11938 C  C8  . NAG C  2 .   ? 52.181  80.241 60.867 1.00 59.62 ? 1092 NAG A C8  1 
HETATM 11939 N  N2  . NAG C  2 .   ? 49.913  79.838 60.064 1.00 59.86 ? 1092 NAG A N2  1 
HETATM 11940 O  O3  . NAG C  2 .   ? 48.294  79.196 62.337 1.00 59.97 ? 1092 NAG A O3  1 
HETATM 11941 O  O4  . NAG C  2 .   ? 45.708  78.122 61.772 1.00 60.96 ? 1092 NAG A O4  1 
HETATM 11942 O  O5  . NAG C  2 .   ? 46.442  79.989 58.674 1.00 59.93 ? 1092 NAG A O5  1 
HETATM 11943 O  O6  . NAG C  2 .   ? 43.654  77.897 59.707 1.00 61.88 ? 1092 NAG A O6  1 
HETATM 11944 O  O7  . NAG C  2 .   ? 50.233  81.323 61.745 1.00 59.70 ? 1092 NAG A O7  1 
HETATM 11945 C  C1  . NAG D  2 .   ? 46.897  80.980 11.968 1.00 45.55 ? 1281 NAG A C1  1 
HETATM 11946 C  C2  . NAG D  2 .   ? 46.590  82.259 11.165 1.00 46.59 ? 1281 NAG A C2  1 
HETATM 11947 C  C3  . NAG D  2 .   ? 45.116  82.669 11.386 1.00 47.32 ? 1281 NAG A C3  1 
HETATM 11948 C  C4  . NAG D  2 .   ? 44.196  81.498 11.016 1.00 47.11 ? 1281 NAG A C4  1 
HETATM 11949 C  C5  . NAG D  2 .   ? 44.605  80.260 11.827 1.00 46.12 ? 1281 NAG A C5  1 
HETATM 11950 C  C6  . NAG D  2 .   ? 43.768  79.029 11.528 1.00 45.58 ? 1281 NAG A C6  1 
HETATM 11951 C  C7  . NAG D  2 .   ? 48.563  83.618 10.849 1.00 46.90 ? 1281 NAG A C7  1 
HETATM 11952 C  C8  . NAG D  2 .   ? 49.430  84.763 11.333 1.00 47.27 ? 1281 NAG A C8  1 
HETATM 11953 N  N2  . NAG D  2 .   ? 47.476  83.339 11.566 1.00 47.42 ? 1281 NAG A N2  1 
HETATM 11954 O  O3  . NAG D  2 .   ? 44.797  83.809 10.592 1.00 48.52 ? 1281 NAG A O3  1 
HETATM 11955 O  O4  . NAG D  2 .   ? 42.844  81.839 11.283 1.00 48.04 ? 1281 NAG A O4  1 
HETATM 11956 O  O5  . NAG D  2 .   ? 45.994  79.930 11.562 1.00 46.26 ? 1281 NAG A O5  1 
HETATM 11957 O  O6  . NAG D  2 .   ? 44.111  78.448 10.282 1.00 45.28 ? 1281 NAG A O6  1 
HETATM 11958 O  O7  . NAG D  2 .   ? 48.882  82.992 9.834  1.00 47.35 ? 1281 NAG A O7  1 
HETATM 11959 C  C1  . NAG E  2 .   ? 42.922  22.608 38.297 1.00 56.36 ? 1520 NAG A C1  1 
HETATM 11960 C  C2  . NAG E  2 .   ? 41.843  21.871 37.467 1.00 56.84 ? 1520 NAG A C2  1 
HETATM 11961 C  C3  . NAG E  2 .   ? 41.068  22.879 36.593 1.00 56.67 ? 1520 NAG A C3  1 
HETATM 11962 C  C4  . NAG E  2 .   ? 40.493  24.010 37.474 1.00 56.75 ? 1520 NAG A C4  1 
HETATM 11963 C  C5  . NAG E  2 .   ? 41.661  24.656 38.256 1.00 56.44 ? 1520 NAG A C5  1 
HETATM 11964 C  C6  . NAG E  2 .   ? 41.274  25.783 39.198 1.00 56.59 ? 1520 NAG A C6  1 
HETATM 11965 C  C7  . NAG E  2 .   ? 43.468  21.086 35.835 1.00 58.07 ? 1520 NAG A C7  1 
HETATM 11966 C  C8  . NAG E  2 .   ? 43.997  19.929 34.998 1.00 57.57 ? 1520 NAG A C8  1 
HETATM 11967 N  N2  . NAG E  2 .   ? 42.431  20.830 36.632 1.00 58.05 ? 1520 NAG A N2  1 
HETATM 11968 O  O3  . NAG E  2 .   ? 40.033  22.208 35.895 1.00 56.52 ? 1520 NAG A O3  1 
HETATM 11969 O  O4  . NAG E  2 .   ? 39.817  24.974 36.676 1.00 55.06 ? 1520 NAG A O4  1 
HETATM 11970 O  O5  . NAG E  2 .   ? 42.318  23.661 39.070 1.00 57.16 ? 1520 NAG A O5  1 
HETATM 11971 O  O6  . NAG E  2 .   ? 42.400  26.213 39.960 1.00 55.11 ? 1520 NAG A O6  1 
HETATM 11972 O  O7  . NAG E  2 .   ? 44.002  22.197 35.757 1.00 58.82 ? 1520 NAG A O7  1 
HETATM 11973 NA NA  . NA  F  3 .   ? 68.087  58.521 61.763 1.00 27.31 ? 1522 NA  A NA  1 
HETATM 11974 C  C1  . 474 G  4 .   ? 39.460  51.474 36.307 1.00 21.52 ? 1521 474 A C1  1 
HETATM 11975 C  C2  . 474 G  4 .   ? 38.349  51.084 35.283 1.00 21.01 ? 1521 474 A C2  1 
HETATM 11976 C  C3  . 474 G  4 .   ? 36.934  51.222 35.891 1.00 21.02 ? 1521 474 A C3  1 
HETATM 11977 N  N4  . 474 G  4 .   ? 36.134  50.115 35.865 1.00 20.22 ? 1521 474 A N4  1 
HETATM 11978 C  C5  . 474 G  4 .   ? 39.662  50.503 37.312 1.00 22.38 ? 1521 474 A C5  1 
HETATM 11979 N  N6  . 474 G  4 .   ? 38.335  51.922 34.080 1.00 21.72 ? 1521 474 A N6  1 
HETATM 11980 O  O7  . 474 G  4 .   ? 36.565  52.283 36.369 1.00 21.97 ? 1521 474 A O7  1 
HETATM 11981 O  O8  . 474 G  4 .   ? 39.669  49.341 36.867 1.00 23.66 ? 1521 474 A O8  1 
HETATM 11982 N  N9  . 474 G  4 .   ? 39.841  50.743 38.684 1.00 23.23 ? 1521 474 A N9  1 
HETATM 11983 C  C10 . 474 G  4 .   ? 39.840  52.053 39.365 1.00 21.99 ? 1521 474 A C10 1 
HETATM 11984 C  C14 . 474 G  4 .   ? 40.049  49.540 39.521 1.00 22.51 ? 1521 474 A C14 1 
HETATM 11985 C  C18 . 474 G  4 .   ? 36.468  48.775 35.341 1.00 20.28 ? 1521 474 A C18 1 
HETATM 11986 C  C19 . 474 G  4 .   ? 35.221  47.969 35.621 1.00 22.49 ? 1521 474 A C19 1 
HETATM 11987 C  C20 . 474 G  4 .   ? 34.137  49.000 35.629 1.00 21.91 ? 1521 474 A C20 1 
HETATM 11988 C  C21 . 474 G  4 .   ? 34.775  50.158 36.393 1.00 20.47 ? 1521 474 A C21 1 
HETATM 11989 F  F28 . 474 G  4 .   ? 35.312  47.443 36.859 1.00 22.93 ? 1521 474 A F28 1 
HETATM 11990 C  C29 . 474 G  4 .   ? 43.915  51.570 35.235 1.00 20.91 ? 1521 474 A C29 1 
HETATM 11991 C  C30 . 474 G  4 .   ? 43.212  52.743 35.965 1.00 20.57 ? 1521 474 A C30 1 
HETATM 11992 C  C31 . 474 G  4 .   ? 41.906  52.370 36.639 1.00 20.43 ? 1521 474 A C31 1 
HETATM 11993 C  C32 . 474 G  4 .   ? 40.865  51.830 35.616 1.00 20.95 ? 1521 474 A C32 1 
HETATM 11994 C  C33 . 474 G  4 .   ? 41.539  50.619 34.828 1.00 19.07 ? 1521 474 A C33 1 
HETATM 11995 C  C34 . 474 G  4 .   ? 42.909  50.993 34.184 1.00 21.42 ? 1521 474 A C34 1 
HETATM 11996 C  C48 . 474 G  4 .   ? 47.928  52.338 33.703 1.00 20.63 ? 1521 474 A C48 1 
HETATM 11997 C  C49 . 474 G  4 .   ? 46.835  52.723 32.765 1.00 21.32 ? 1521 474 A C49 1 
HETATM 11998 C  C50 . 474 G  4 .   ? 45.541  52.544 33.161 1.00 20.66 ? 1521 474 A C50 1 
HETATM 11999 C  C51 . 474 G  4 .   ? 45.238  51.889 34.487 1.00 21.46 ? 1521 474 A C51 1 
HETATM 12000 C  C52 . 474 G  4 .   ? 46.237  51.518 35.343 1.00 20.24 ? 1521 474 A C52 1 
HETATM 12001 N  N53 . 474 G  4 .   ? 47.647  51.712 34.878 1.00 22.69 ? 1521 474 A N53 1 
HETATM 12002 N  N54 . 474 G  4 .   ? 48.702  51.468 35.508 1.00 22.13 ? 1521 474 A N54 1 
HETATM 12003 C  C55 . 474 G  4 .   ? 49.696  51.871 34.693 1.00 22.29 ? 1521 474 A C55 1 
HETATM 12004 N  N56 . 474 G  4 .   ? 49.251  52.413 33.533 1.00 22.17 ? 1521 474 A N56 1 
HETATM 12005 F  F62 . 474 G  4 .   ? 35.035  47.002 34.723 1.00 25.80 ? 1521 474 A F62 1 
HETATM 12006 C  C1  . NAG H  2 .   ? -14.716 30.636 17.089 1.00 56.96 ? 2092 NAG B C1  1 
HETATM 12007 C  C2  . NAG H  2 .   ? -15.492 29.300 17.068 1.00 56.83 ? 2092 NAG B C2  1 
HETATM 12008 C  C3  . NAG H  2 .   ? -15.149 28.468 18.327 1.00 57.27 ? 2092 NAG B C3  1 
HETATM 12009 C  C4  . NAG H  2 .   ? -13.644 28.428 18.632 1.00 57.58 ? 2092 NAG B C4  1 
HETATM 12010 C  C5  . NAG H  2 .   ? -13.030 29.836 18.561 1.00 58.14 ? 2092 NAG B C5  1 
HETATM 12011 C  C6  . NAG H  2 .   ? -11.512 29.852 18.722 1.00 58.94 ? 2092 NAG B C6  1 
HETATM 12012 C  C7  . NAG H  2 .   ? -17.849 28.643 16.952 1.00 57.64 ? 2092 NAG B C7  1 
HETATM 12013 C  C8  . NAG H  2 .   ? -19.308 29.085 16.944 1.00 55.93 ? 2092 NAG B C8  1 
HETATM 12014 N  N2  . NAG H  2 .   ? -16.920 29.601 17.043 1.00 57.77 ? 2092 NAG B N2  1 
HETATM 12015 O  O3  . NAG H  2 .   ? -15.617 27.141 18.165 1.00 56.86 ? 2092 NAG B O3  1 
HETATM 12016 O  O4  . NAG H  2 .   ? -13.438 27.881 19.928 1.00 57.96 ? 2092 NAG B O4  1 
HETATM 12017 O  O5  . NAG H  2 .   ? -13.314 30.423 17.281 1.00 57.72 ? 2092 NAG B O5  1 
HETATM 12018 O  O6  . NAG H  2 .   ? -11.061 31.121 19.194 1.00 59.88 ? 2092 NAG B O6  1 
HETATM 12019 O  O7  . NAG H  2 .   ? -17.579 27.443 16.872 1.00 58.29 ? 2092 NAG B O7  1 
HETATM 12020 C  C1  . NAG I  2 .   ? 3.956   47.959 5.577  1.00 46.92 ? 2150 NAG B C1  1 
HETATM 12021 C  C2  . NAG I  2 .   ? 3.727   47.912 4.053  1.00 48.54 ? 2150 NAG B C2  1 
HETATM 12022 C  C3  . NAG I  2 .   ? 4.007   46.505 3.462  1.00 49.66 ? 2150 NAG B C3  1 
HETATM 12023 C  C4  . NAG I  2 .   ? 5.376   46.015 3.912  1.00 50.44 ? 2150 NAG B C4  1 
HETATM 12024 C  C5  . NAG I  2 .   ? 5.439   46.060 5.450  1.00 50.45 ? 2150 NAG B C5  1 
HETATM 12025 C  C6  . NAG I  2 .   ? 6.761   45.560 6.006  1.00 51.08 ? 2150 NAG B C6  1 
HETATM 12026 C  C7  . NAG I  2 .   ? 2.100   49.516 3.299  1.00 49.47 ? 2150 NAG B C7  1 
HETATM 12027 C  C8  . NAG I  2 .   ? 0.636   49.863 3.064  1.00 48.81 ? 2150 NAG B C8  1 
HETATM 12028 N  N2  . NAG I  2 .   ? 2.355   48.308 3.792  1.00 49.36 ? 2150 NAG B N2  1 
HETATM 12029 O  O3  . NAG I  2 .   ? 3.963   46.547 2.036  1.00 50.56 ? 2150 NAG B O3  1 
HETATM 12030 O  O4  . NAG I  2 .   ? 5.607   44.694 3.436  1.00 51.71 ? 2150 NAG B O4  1 
HETATM 12031 O  O5  . NAG I  2 .   ? 5.253   47.427 5.916  1.00 49.03 ? 2150 NAG B O5  1 
HETATM 12032 O  O6  . NAG I  2 .   ? 7.797   46.524 5.849  1.00 52.97 ? 2150 NAG B O6  1 
HETATM 12033 O  O7  . NAG I  2 .   ? 2.990   50.332 3.020  1.00 49.48 ? 2150 NAG B O7  1 
HETATM 12034 C  C1  . NAG J  2 .   ? -9.536  84.900 37.061 1.00 42.55 ? 2321 NAG B C1  1 
HETATM 12035 C  C2  . NAG J  2 .   ? -10.268 85.995 37.814 1.00 44.35 ? 2321 NAG B C2  1 
HETATM 12036 C  C3  . NAG J  2 .   ? -9.293  87.169 38.087 1.00 45.47 ? 2321 NAG B C3  1 
HETATM 12037 C  C4  . NAG J  2 .   ? -8.086  86.623 38.868 1.00 45.61 ? 2321 NAG B C4  1 
HETATM 12038 C  C5  . NAG J  2 .   ? -7.452  85.415 38.134 1.00 45.24 ? 2321 NAG B C5  1 
HETATM 12039 C  C6  . NAG J  2 .   ? -6.369  84.750 38.966 1.00 45.75 ? 2321 NAG B C6  1 
HETATM 12040 C  C7  . NAG J  2 .   ? -12.662 86.049 37.512 1.00 46.74 ? 2321 NAG B C7  1 
HETATM 12041 C  C8  . NAG J  2 .   ? -13.865 86.462 36.689 1.00 48.67 ? 2321 NAG B C8  1 
HETATM 12042 N  N2  . NAG J  2 .   ? -11.452 86.387 37.062 1.00 45.39 ? 2321 NAG B N2  1 
HETATM 12043 O  O3  . NAG J  2 .   ? -9.944  88.178 38.847 1.00 46.26 ? 2321 NAG B O3  1 
HETATM 12044 O  O4  . NAG J  2 .   ? -7.115  87.639 39.087 1.00 45.08 ? 2321 NAG B O4  1 
HETATM 12045 O  O5  . NAG J  2 .   ? -8.455  84.403 37.862 1.00 43.92 ? 2321 NAG B O5  1 
HETATM 12046 O  O6  . NAG J  2 .   ? -6.769  84.621 40.326 1.00 45.14 ? 2321 NAG B O6  1 
HETATM 12047 O  O7  . NAG J  2 .   ? -12.833 85.436 38.568 1.00 47.96 ? 2321 NAG B O7  1 
HETATM 12048 C  C1  . 474 K  4 .   ? -4.866  62.978 34.831 1.00 19.04 ? 2322 474 B C1  1 
HETATM 12049 C  C2  . 474 K  4 .   ? -3.583  63.874 35.006 1.00 19.76 ? 2322 474 B C2  1 
HETATM 12050 C  C3  . 474 K  4 .   ? -2.376  63.075 35.550 1.00 20.39 ? 2322 474 B C3  1 
HETATM 12051 N  N4  . 474 K  4 .   ? -1.855  63.506 36.741 1.00 21.71 ? 2322 474 B N4  1 
HETATM 12052 C  C5  . 474 K  4 .   ? -5.514  62.635 36.053 1.00 19.44 ? 2322 474 B C5  1 
HETATM 12053 N  N6  . 474 K  4 .   ? -3.139  64.491 33.741 1.00 19.35 ? 2322 474 B N6  1 
HETATM 12054 O  O7  . 474 K  4 .   ? -1.928  62.106 34.935 1.00 20.46 ? 2322 474 B O7  1 
HETATM 12055 O  O8  . 474 K  4 .   ? -5.566  63.569 36.867 1.00 18.81 ? 2322 474 B O8  1 
HETATM 12056 N  N9  . 474 K  4 .   ? -6.055  61.385 36.376 1.00 19.70 ? 2322 474 B N9  1 
HETATM 12057 C  C10 . 474 K  4 .   ? -6.054  60.182 35.524 1.00 19.04 ? 2322 474 B C10 1 
HETATM 12058 C  C14 . 474 K  4 .   ? -6.690  61.274 37.711 1.00 19.37 ? 2322 474 B C14 1 
HETATM 12059 C  C18 . 474 K  4 .   ? -2.323  64.630 37.565 1.00 21.46 ? 2322 474 B C18 1 
HETATM 12060 C  C19 . 474 K  4 .   ? -1.423  64.595 38.773 1.00 23.86 ? 2322 474 B C19 1 
HETATM 12061 C  C20 . 474 K  4 .   ? -0.163  63.972 38.252 1.00 22.77 ? 2322 474 B C20 1 
HETATM 12062 C  C21 . 474 K  4 .   ? -0.694  62.841 37.362 1.00 22.04 ? 2322 474 B C21 1 
HETATM 12063 F  F28 . 474 K  4 .   ? -1.979  63.755 39.666 1.00 22.39 ? 2322 474 B F28 1 
HETATM 12064 C  C29 . 474 K  4 .   ? -8.704  64.469 32.888 1.00 19.63 ? 2322 474 B C29 1 
HETATM 12065 C  C30 . 474 K  4 .   ? -7.990  63.216 32.378 1.00 17.81 ? 2322 474 B C30 1 
HETATM 12066 C  C31 . 474 K  4 .   ? -7.028  62.611 33.380 1.00 19.20 ? 2322 474 B C31 1 
HETATM 12067 C  C32 . 474 K  4 .   ? -5.926  63.605 33.792 1.00 18.73 ? 2322 474 B C32 1 
HETATM 12068 C  C33 . 474 K  4 .   ? -6.607  64.942 34.300 1.00 18.83 ? 2322 474 B C33 1 
HETATM 12069 C  C34 . 474 K  4 .   ? -7.649  65.534 33.273 1.00 17.88 ? 2322 474 B C34 1 
HETATM 12070 C  C48 . 474 K  4 .   ? -11.892 66.015 30.404 1.00 20.11 ? 2322 474 B C48 1 
HETATM 12071 C  C49 . 474 K  4 .   ? -10.546 66.462 29.994 1.00 19.90 ? 2322 474 B C49 1 
HETATM 12072 C  C50 . 474 K  4 .   ? -9.468  66.054 30.720 1.00 19.73 ? 2322 474 B C50 1 
HETATM 12073 C  C51 . 474 K  4 .   ? -9.672  65.142 31.909 1.00 19.64 ? 2322 474 B C51 1 
HETATM 12074 C  C52 . 474 K  4 .   ? -10.915 64.742 32.277 1.00 18.74 ? 2322 474 B C52 1 
HETATM 12075 N  N53 . 474 K  4 .   ? -12.053 65.186 31.485 1.00 20.50 ? 2322 474 B N53 1 
HETATM 12076 N  N54 . 474 K  4 .   ? -13.252 64.936 31.658 1.00 22.74 ? 2322 474 B N54 1 
HETATM 12077 C  C55 . 474 K  4 .   ? -13.909 65.583 30.666 1.00 22.25 ? 2322 474 B C55 1 
HETATM 12078 N  N56 . 474 K  4 .   ? -13.093 66.272 29.849 1.00 21.78 ? 2322 474 B N56 1 
HETATM 12079 F  F62 . 474 K  4 .   ? -1.253  65.804 39.303 1.00 25.03 ? 2322 474 B F62 1 
HETATM 12080 C  C1  . NAG L  2 .   ? 69.488  74.556 56.132 1.00 42.99 ? 1085 NAG L C1  1 
HETATM 12081 C  C2  . NAG L  2 .   ? 69.105  75.742 55.200 1.00 44.02 ? 1085 NAG L C2  1 
HETATM 12082 C  C3  . NAG L  2 .   ? 70.310  76.206 54.354 1.00 46.12 ? 1085 NAG L C3  1 
HETATM 12083 C  C4  . NAG L  2 .   ? 71.389  76.552 55.355 1.00 48.02 ? 1085 NAG L C4  1 
HETATM 12084 C  C5  . NAG L  2 .   ? 71.792  75.283 56.100 1.00 47.19 ? 1085 NAG L C5  1 
HETATM 12085 C  C6  . NAG L  2 .   ? 72.964  75.513 57.057 1.00 48.13 ? 1085 NAG L C6  1 
HETATM 12086 C  C7  . NAG L  2 .   ? 66.789  75.766 54.577 1.00 42.36 ? 1085 NAG L C7  1 
HETATM 12087 C  C8  . NAG L  2 .   ? 65.706  75.319 53.620 1.00 40.90 ? 1085 NAG L C8  1 
HETATM 12088 N  N2  . NAG L  2 .   ? 68.024  75.349 54.324 1.00 42.33 ? 1085 NAG L N2  1 
HETATM 12089 O  O3  . NAG L  2 .   ? 69.966  77.354 53.561 1.00 46.29 ? 1085 NAG L O3  1 
HETATM 12090 O  O4  . NAG L  2 .   ? 72.537  77.196 54.766 1.00 52.56 ? 1085 NAG L O4  1 
HETATM 12091 O  O5  . NAG L  2 .   ? 70.673  74.840 56.897 1.00 44.08 ? 1085 NAG L O5  1 
HETATM 12092 O  O6  . NAG L  2 .   ? 73.254  74.352 57.836 1.00 49.91 ? 1085 NAG L O6  1 
HETATM 12093 O  O7  . NAG L  2 .   ? 66.504  76.488 55.542 1.00 43.01 ? 1085 NAG L O7  1 
HETATM 12094 C  C1  . NDG M  5 .   ? 72.990  76.870 53.491 1.00 56.44 ? 1086 NDG L C1  1 
HETATM 12095 C  C2  . NDG M  5 .   ? 74.503  77.114 53.448 1.00 57.61 ? 1086 NDG L C2  1 
HETATM 12096 C  C3  . NDG M  5 .   ? 74.797  78.557 53.910 1.00 58.40 ? 1086 NDG L C3  1 
HETATM 12097 C  C4  . NDG M  5 .   ? 73.913  79.591 53.171 1.00 58.64 ? 1086 NDG L C4  1 
HETATM 12098 C  C5  . NDG M  5 .   ? 72.433  79.139 52.988 1.00 58.10 ? 1086 NDG L C5  1 
HETATM 12099 C  C6  . NDG M  5 .   ? 71.647  79.963 51.959 1.00 57.25 ? 1086 NDG L C6  1 
HETATM 12100 C  C7  . NDG M  5 .   ? 76.299  75.570 53.903 1.00 57.86 ? 1086 NDG L C7  1 
HETATM 12101 C  C8  . NDG M  5 .   ? 76.955  74.579 54.855 1.00 57.60 ? 1086 NDG L C8  1 
HETATM 12102 O  O   . NDG M  5 .   ? 72.356  77.756 52.557 1.00 57.93 ? 1086 NDG L O   1 
HETATM 12103 O  O3  . NDG M  5 .   ? 76.172  78.875 53.701 1.00 59.08 ? 1086 NDG L O3  1 
HETATM 12104 O  O4  . NDG M  5 .   ? 73.947  80.819 53.889 1.00 58.73 ? 1086 NDG L O4  1 
HETATM 12105 O  O6  . NDG M  5 .   ? 71.023  79.131 50.990 1.00 55.44 ? 1086 NDG L O6  1 
HETATM 12106 O  O7  . NDG M  5 .   ? 76.807  75.801 52.810 1.00 58.40 ? 1086 NDG L O7  1 
HETATM 12107 N  N2  . NDG M  5 .   ? 75.179  76.157 54.310 1.00 58.15 ? 1086 NDG L N2  1 
HETATM 12108 C  C1  . NDG N  5 .   ? 37.676  84.910 33.248 1.00 53.17 ? 1150 NDG M C1  1 
HETATM 12109 C  C2  . NDG N  5 .   ? 38.416  86.120 32.597 1.00 54.39 ? 1150 NDG M C2  1 
HETATM 12110 C  C3  . NDG N  5 .   ? 38.706  87.215 33.613 1.00 54.71 ? 1150 NDG M C3  1 
HETATM 12111 C  C4  . NDG N  5 .   ? 37.453  87.562 34.400 1.00 55.21 ? 1150 NDG M C4  1 
HETATM 12112 C  C5  . NDG N  5 .   ? 36.907  86.294 35.073 1.00 54.27 ? 1150 NDG M C5  1 
HETATM 12113 C  C6  . NDG N  5 .   ? 35.657  86.557 35.901 1.00 53.67 ? 1150 NDG M C6  1 
HETATM 12114 C  C7  . NDG N  5 .   ? 39.878  85.811 30.694 1.00 56.17 ? 1150 NDG M C7  1 
HETATM 12115 C  C8  . NDG N  5 .   ? 41.233  85.377 30.144 1.00 56.16 ? 1150 NDG M C8  1 
HETATM 12116 O  O   . NDG N  5 .   ? 36.552  85.323 34.059 1.00 53.59 ? 1150 NDG M O   1 
HETATM 12117 O  O3  . NDG N  5 .   ? 39.193  88.379 32.948 1.00 56.02 ? 1150 NDG M O3  1 
HETATM 12118 O  O4  . NDG N  5 .   ? 37.799  88.559 35.388 1.00 56.89 ? 1150 NDG M O4  1 
HETATM 12119 O  O6  . NDG N  5 .   ? 34.621  87.133 35.111 1.00 53.26 ? 1150 NDG M O6  1 
HETATM 12120 O  O7  . NDG N  5 .   ? 39.013  86.226 29.921 1.00 57.83 ? 1150 NDG M O7  1 
HETATM 12121 N  N2  . NDG N  5 .   ? 39.682  85.709 32.007 1.00 54.62 ? 1150 NDG M N2  1 
HETATM 12122 C  C1  . NAG O  2 .   ? 37.074  89.745 35.435 1.00 57.75 ? 1151 NAG M C1  1 
HETATM 12123 C  C2  . NAG O  2 .   ? 36.624  90.202 34.021 1.00 58.95 ? 1151 NAG M C2  1 
HETATM 12124 C  C3  . NAG O  2 .   ? 35.708  91.442 34.102 1.00 58.19 ? 1151 NAG M C3  1 
HETATM 12125 C  C4  . NAG O  2 .   ? 34.632  91.304 35.194 1.00 58.09 ? 1151 NAG M C4  1 
HETATM 12126 C  C5  . NAG O  2 .   ? 35.223  90.752 36.514 1.00 57.37 ? 1151 NAG M C5  1 
HETATM 12127 C  C6  . NAG O  2 .   ? 34.170  90.426 37.566 1.00 56.64 ? 1151 NAG M C6  1 
HETATM 12128 C  C7  . NAG O  2 .   ? 38.633  91.459 33.464 1.00 61.22 ? 1151 NAG M C7  1 
HETATM 12129 C  C8  . NAG O  2 .   ? 39.793  91.675 32.502 1.00 60.94 ? 1151 NAG M C8  1 
HETATM 12130 N  N2  . NAG O  2 .   ? 37.770  90.488 33.160 1.00 60.13 ? 1151 NAG M N2  1 
HETATM 12131 O  O3  . NAG O  2 .   ? 35.076  91.627 32.844 1.00 58.18 ? 1151 NAG M O3  1 
HETATM 12132 O  O4  . NAG O  2 .   ? 34.038  92.573 35.433 1.00 58.27 ? 1151 NAG M O4  1 
HETATM 12133 O  O5  . NAG O  2 .   ? 35.938  89.527 36.266 1.00 57.84 ? 1151 NAG M O5  1 
HETATM 12134 O  O6  . NAG O  2 .   ? 34.703  89.559 38.557 1.00 55.04 ? 1151 NAG M O6  1 
HETATM 12135 O  O7  . NAG O  2 .   ? 38.531  92.166 34.473 1.00 62.40 ? 1151 NAG M O7  1 
HETATM 12136 C  C1  . NAG P  2 .   ? 67.636  71.922 25.492 1.00 39.48 ? 1219 NAG M C1  1 
HETATM 12137 C  C2  . NAG P  2 .   ? 68.549  73.151 25.578 1.00 41.71 ? 1219 NAG M C2  1 
HETATM 12138 C  C3  . NAG P  2 .   ? 68.725  73.784 24.183 1.00 42.28 ? 1219 NAG M C3  1 
HETATM 12139 C  C4  . NAG P  2 .   ? 69.070  72.730 23.124 1.00 42.01 ? 1219 NAG M C4  1 
HETATM 12140 C  C5  . NAG P  2 .   ? 68.099  71.548 23.200 1.00 41.23 ? 1219 NAG M C5  1 
HETATM 12141 C  C6  . NAG P  2 .   ? 68.397  70.429 22.215 1.00 40.79 ? 1219 NAG M C6  1 
HETATM 12142 C  C7  . NAG P  2 .   ? 68.427  74.329 27.684 1.00 44.92 ? 1219 NAG M C7  1 
HETATM 12143 C  C8  . NAG P  2 .   ? 67.699  75.348 28.543 1.00 44.74 ? 1219 NAG M C8  1 
HETATM 12144 N  N2  . NAG P  2 .   ? 67.931  74.119 26.467 1.00 43.21 ? 1219 NAG M N2  1 
HETATM 12145 O  O3  . NAG P  2 .   ? 69.753  74.773 24.230 1.00 42.62 ? 1219 NAG M O3  1 
HETATM 12146 O  O4  . NAG P  2 .   ? 68.966  73.329 21.829 1.00 44.14 ? 1219 NAG M O4  1 
HETATM 12147 O  O5  . NAG P  2 .   ? 68.122  70.985 24.524 1.00 39.54 ? 1219 NAG M O5  1 
HETATM 12148 O  O6  . NAG P  2 .   ? 69.717  69.924 22.378 1.00 40.67 ? 1219 NAG M O6  1 
HETATM 12149 O  O7  . NAG P  2 .   ? 69.434  73.749 28.121 1.00 44.92 ? 1219 NAG M O7  1 
HETATM 12150 C  C1  . NAG Q  2 .   ? 70.093  73.274 21.027 1.00 46.18 ? 1220 NAG M C1  1 
HETATM 12151 C  C2  . NAG Q  2 .   ? 69.711  73.697 19.606 1.00 46.70 ? 1220 NAG M C2  1 
HETATM 12152 C  C3  . NAG Q  2 .   ? 70.974  73.797 18.721 1.00 48.01 ? 1220 NAG M C3  1 
HETATM 12153 C  C4  . NAG Q  2 .   ? 72.035  74.678 19.384 1.00 48.65 ? 1220 NAG M C4  1 
HETATM 12154 C  C5  . NAG Q  2 .   ? 72.304  74.168 20.805 1.00 48.66 ? 1220 NAG M C5  1 
HETATM 12155 C  C6  . NAG Q  2 .   ? 73.295  75.039 21.552 1.00 49.22 ? 1220 NAG M C6  1 
HETATM 12156 C  C7  . NAG Q  2 .   ? 67.484  72.914 19.078 1.00 45.32 ? 1220 NAG M C7  1 
HETATM 12157 C  C8  . NAG Q  2 .   ? 66.634  71.816 18.465 1.00 44.97 ? 1220 NAG M C8  1 
HETATM 12158 N  N2  . NAG Q  2 .   ? 68.798  72.713 19.054 1.00 46.01 ? 1220 NAG M N2  1 
HETATM 12159 O  O3  . NAG Q  2 .   ? 70.641  74.319 17.446 1.00 47.91 ? 1220 NAG M O3  1 
HETATM 12160 O  O4  . NAG Q  2 .   ? 73.236  74.651 18.623 1.00 50.56 ? 1220 NAG M O4  1 
HETATM 12161 O  O5  . NAG Q  2 .   ? 71.074  74.171 21.567 1.00 47.48 ? 1220 NAG M O5  1 
HETATM 12162 O  O6  . NAG Q  2 .   ? 72.748  76.326 21.793 1.00 48.82 ? 1220 NAG M O6  1 
HETATM 12163 O  O7  . NAG Q  2 .   ? 66.951  73.920 19.567 1.00 44.76 ? 1220 NAG M O7  1 
HETATM 12164 C  C1  . NAG R  2 .   ? 38.457  63.996 12.485 1.00 36.70 ? 1229 NAG O C1  1 
HETATM 12165 C  C2  . NAG R  2 .   ? 39.208  64.798 11.396 1.00 39.14 ? 1229 NAG O C2  1 
HETATM 12166 C  C3  . NAG R  2 .   ? 38.307  65.038 10.190 1.00 41.50 ? 1229 NAG O C3  1 
HETATM 12167 C  C4  . NAG R  2 .   ? 37.749  63.717 9.680  1.00 42.91 ? 1229 NAG O C4  1 
HETATM 12168 C  C5  . NAG R  2 .   ? 36.984  63.069 10.848 1.00 41.46 ? 1229 NAG O C5  1 
HETATM 12169 C  C6  . NAG R  2 .   ? 36.259  61.781 10.531 1.00 41.27 ? 1229 NAG O C6  1 
HETATM 12170 C  C7  . NAG R  2 .   ? 40.908  66.342 12.117 1.00 38.84 ? 1229 NAG O C7  1 
HETATM 12171 C  C8  . NAG R  2 .   ? 41.250  67.729 12.633 1.00 37.77 ? 1229 NAG O C8  1 
HETATM 12172 N  N2  . NAG R  2 .   ? 39.623  66.088 11.906 1.00 39.14 ? 1229 NAG O N2  1 
HETATM 12173 O  O3  . NAG R  2 .   ? 39.037  65.695 9.163  1.00 43.95 ? 1229 NAG O O3  1 
HETATM 12174 O  O4  . NAG R  2 .   ? 36.886  63.972 8.551  1.00 46.38 ? 1229 NAG O O4  1 
HETATM 12175 O  O5  . NAG R  2 .   ? 37.907  62.793 11.929 1.00 37.94 ? 1229 NAG O O5  1 
HETATM 12176 O  O6  . NAG R  2 .   ? 37.068  60.660 10.826 1.00 43.28 ? 1229 NAG O O6  1 
HETATM 12177 O  O7  . NAG R  2 .   ? 41.796  65.510 11.937 1.00 39.50 ? 1229 NAG O O7  1 
HETATM 12178 C  C1  . NDG S  5 .   ? 36.852  62.960 7.605  1.00 49.86 ? 1230 NDG O C1  1 
HETATM 12179 C  C2  . NDG S  5 .   ? 36.923  63.500 6.151  1.00 52.07 ? 1230 NDG O C2  1 
HETATM 12180 C  C3  . NDG S  5 .   ? 35.571  63.980 5.586  1.00 53.04 ? 1230 NDG O C3  1 
HETATM 12181 C  C4  . NDG S  5 .   ? 34.424  63.050 5.973  1.00 52.92 ? 1230 NDG O C4  1 
HETATM 12182 C  C5  . NDG S  5 .   ? 34.462  62.851 7.487  1.00 51.14 ? 1230 NDG O C5  1 
HETATM 12183 C  C6  . NDG S  5 .   ? 33.314  62.026 8.028  1.00 50.54 ? 1230 NDG O C6  1 
HETATM 12184 C  C7  . NDG S  5 .   ? 37.596  65.804 6.509  1.00 55.05 ? 1230 NDG O C7  1 
HETATM 12185 C  C8  . NDG S  5 .   ? 38.635  66.905 6.290  1.00 54.95 ? 1230 NDG O C8  1 
HETATM 12186 O  O   . NDG S  5 .   ? 35.677  62.164 7.833  1.00 51.20 ? 1230 NDG O O   1 
HETATM 12187 O  O3  . NDG S  5 .   ? 35.649  64.058 4.161  1.00 53.88 ? 1230 NDG O O3  1 
HETATM 12188 O  O4  . NDG S  5 .   ? 33.186  63.624 5.571  1.00 54.46 ? 1230 NDG O O4  1 
HETATM 12189 O  O6  . NDG S  5 .   ? 32.639  62.725 9.063  1.00 48.90 ? 1230 NDG O O6  1 
HETATM 12190 O  O7  . NDG S  5 .   ? 36.564  66.053 7.142  1.00 54.79 ? 1230 NDG O O7  1 
HETATM 12191 N  N2  . NDG S  5 .   ? 37.877  64.592 6.021  1.00 53.94 ? 1230 NDG O N2  1 
HETATM 12192 C  C1  . NDG T  5 .   ? 46.509  37.794 20.541 1.00 44.88 ? 1321 NDG P C1  1 
HETATM 12193 C  C2  . NDG T  5 .   ? 47.302  36.923 19.528 1.00 46.97 ? 1321 NDG P C2  1 
HETATM 12194 C  C3  . NDG T  5 .   ? 46.535  36.731 18.227 1.00 48.61 ? 1321 NDG P C3  1 
HETATM 12195 C  C4  . NDG T  5 .   ? 45.076  36.346 18.439 1.00 49.77 ? 1321 NDG P C4  1 
HETATM 12196 C  C5  . NDG T  5 .   ? 44.418  37.287 19.469 1.00 48.97 ? 1321 NDG P C5  1 
HETATM 12197 C  C6  . NDG T  5 .   ? 42.985  36.886 19.805 1.00 48.07 ? 1321 NDG P C6  1 
HETATM 12198 C  C7  . NDG T  5 .   ? 49.718  36.967 19.612 1.00 48.35 ? 1321 NDG P C7  1 
HETATM 12199 C  C8  . NDG T  5 .   ? 51.002  37.678 19.216 1.00 48.25 ? 1321 NDG P C8  1 
HETATM 12200 O  O   . NDG T  5 .   ? 45.175  37.280 20.710 1.00 47.81 ? 1321 NDG P O   1 
HETATM 12201 O  O3  . NDG T  5 .   ? 47.176  35.742 17.442 1.00 47.36 ? 1321 NDG P O3  1 
HETATM 12202 O  O4  . NDG T  5 .   ? 44.412  36.485 17.167 1.00 53.58 ? 1321 NDG P O4  1 
HETATM 12203 O  O6  . NDG T  5 .   ? 42.944  35.600 20.413 1.00 49.45 ? 1321 NDG P O6  1 
HETATM 12204 O  O7  . NDG T  5 .   ? 49.762  35.932 20.284 1.00 48.03 ? 1321 NDG P O7  1 
HETATM 12205 N  N2  . NDG T  5 .   ? 48.581  37.529 19.205 1.00 47.72 ? 1321 NDG P N2  1 
HETATM 12206 C  C1  . NAG U  2 .   ? 43.725  35.415 16.606 1.00 55.54 ? 1322 NAG P C1  1 
HETATM 12207 C  C2  . NAG U  2 .   ? 44.528  34.116 16.586 1.00 56.66 ? 1322 NAG P C2  1 
HETATM 12208 C  C3  . NAG U  2 .   ? 43.681  33.063 15.838 1.00 57.27 ? 1322 NAG P C3  1 
HETATM 12209 C  C4  . NAG U  2 .   ? 42.236  32.972 16.378 1.00 56.93 ? 1322 NAG P C4  1 
HETATM 12210 C  C5  . NAG U  2 .   ? 41.623  34.377 16.556 1.00 56.26 ? 1322 NAG P C5  1 
HETATM 12211 C  C6  . NAG U  2 .   ? 40.282  34.434 17.266 1.00 56.04 ? 1322 NAG P C6  1 
HETATM 12212 C  C7  . NAG U  2 .   ? 45.871  34.816 14.678 1.00 59.69 ? 1322 NAG P C7  1 
HETATM 12213 C  C8  . NAG U  2 .   ? 47.264  34.985 14.076 1.00 58.65 ? 1322 NAG P C8  1 
HETATM 12214 N  N2  . NAG U  2 .   ? 45.808  34.311 15.916 1.00 58.89 ? 1322 NAG P N2  1 
HETATM 12215 O  O3  . NAG U  2 .   ? 44.310  31.795 15.917 1.00 56.68 ? 1322 NAG P O3  1 
HETATM 12216 O  O4  . NAG U  2 .   ? 41.451  32.232 15.457 1.00 56.78 ? 1322 NAG P O4  1 
HETATM 12217 O  O5  . NAG U  2 .   ? 42.512  35.211 17.307 1.00 56.39 ? 1322 NAG P O5  1 
HETATM 12218 O  O6  . NAG U  2 .   ? 39.793  35.768 17.295 1.00 54.70 ? 1322 NAG P O6  1 
HETATM 12219 O  O7  . NAG U  2 .   ? 44.863  35.142 14.019 1.00 60.56 ? 1322 NAG P O7  1 
HETATM 12220 C  C1  . NAG V  2 .   ? -33.614 37.992 14.551 1.00 48.48 ? 2085 NAG Q C1  1 
HETATM 12221 C  C2  . NAG V  2 .   ? -32.885 38.189 13.223 1.00 49.49 ? 2085 NAG Q C2  1 
HETATM 12222 C  C3  . NAG V  2 .   ? -33.865 38.811 12.215 1.00 51.51 ? 2085 NAG Q C3  1 
HETATM 12223 C  C4  . NAG V  2 .   ? -35.177 37.997 12.142 1.00 53.41 ? 2085 NAG Q C4  1 
HETATM 12224 C  C5  . NAG V  2 .   ? -35.750 37.768 13.537 1.00 52.50 ? 2085 NAG Q C5  1 
HETATM 12225 C  C6  . NAG V  2 .   ? -36.978 36.856 13.544 1.00 54.01 ? 2085 NAG Q C6  1 
HETATM 12226 C  C7  . NAG V  2 .   ? -30.509 38.523 13.612 1.00 46.59 ? 2085 NAG Q C7  1 
HETATM 12227 C  C8  . NAG V  2 .   ? -29.357 39.493 13.802 1.00 46.84 ? 2085 NAG Q C8  1 
HETATM 12228 N  N2  . NAG V  2 .   ? -31.720 39.046 13.409 1.00 47.77 ? 2085 NAG Q N2  1 
HETATM 12229 O  O3  . NAG V  2 .   ? -33.248 38.867 10.939 1.00 50.98 ? 2085 NAG Q O3  1 
HETATM 12230 O  O4  . NAG V  2 .   ? -36.164 38.692 11.363 1.00 57.09 ? 2085 NAG Q O4  1 
HETATM 12231 O  O5  . NAG V  2 .   ? -34.756 37.159 14.374 1.00 51.20 ? 2085 NAG Q O5  1 
HETATM 12232 O  O6  . NAG V  2 .   ? -37.326 36.438 14.866 1.00 54.75 ? 2085 NAG Q O6  1 
HETATM 12233 O  O7  . NAG V  2 .   ? -30.294 37.313 13.646 1.00 46.26 ? 2085 NAG Q O7  1 
HETATM 12234 C  C1  . NAG W  2 .   ? -36.046 38.697 9.982  1.00 59.34 ? 2086 NAG Q C1  1 
HETATM 12235 C  C2  . NAG W  2 .   ? -37.297 38.043 9.352  1.00 60.97 ? 2086 NAG Q C2  1 
HETATM 12236 C  C3  . NAG W  2 .   ? -37.277 38.217 7.820  1.00 61.13 ? 2086 NAG Q C3  1 
HETATM 12237 C  C4  . NAG W  2 .   ? -37.129 39.709 7.476  1.00 61.45 ? 2086 NAG Q C4  1 
HETATM 12238 C  C5  . NAG W  2 .   ? -35.854 40.241 8.168  1.00 61.19 ? 2086 NAG Q C5  1 
HETATM 12239 C  C6  . NAG W  2 .   ? -35.540 41.712 7.923  1.00 60.41 ? 2086 NAG Q C6  1 
HETATM 12240 C  C7  . NAG W  2 .   ? -38.245 36.192 10.609 1.00 63.35 ? 2086 NAG Q C7  1 
HETATM 12241 C  C8  . NAG W  2 .   ? -38.239 34.697 10.914 1.00 62.03 ? 2086 NAG Q C8  1 
HETATM 12242 N  N2  . NAG W  2 .   ? -37.365 36.630 9.701  1.00 62.48 ? 2086 NAG Q N2  1 
HETATM 12243 O  O3  . NAG W  2 .   ? -38.474 37.695 7.252  1.00 61.51 ? 2086 NAG Q O3  1 
HETATM 12244 O  O4  . NAG W  2 .   ? -37.048 39.895 6.060  1.00 61.10 ? 2086 NAG Q O4  1 
HETATM 12245 O  O5  . NAG W  2 .   ? -35.960 40.072 9.594  1.00 60.22 ? 2086 NAG Q O5  1 
HETATM 12246 O  O6  . NAG W  2 .   ? -34.208 42.015 8.326  1.00 59.60 ? 2086 NAG Q O6  1 
HETATM 12247 O  O7  . NAG W  2 .   ? -39.043 36.938 11.199 1.00 63.71 ? 2086 NAG Q O7  1 
HETATM 12248 C  C1  . NAG X  2 .   ? -24.599 67.166 4.137  1.00 33.27 ? 2219 NAG R C1  1 
HETATM 12249 C  C2  . NAG X  2 .   ? -25.370 66.799 2.877  1.00 36.45 ? 2219 NAG R C2  1 
HETATM 12250 C  C3  . NAG X  2 .   ? -24.888 67.700 1.730  1.00 37.93 ? 2219 NAG R C3  1 
HETATM 12251 C  C4  . NAG X  2 .   ? -25.001 69.169 2.125  1.00 37.13 ? 2219 NAG R C4  1 
HETATM 12252 C  C5  . NAG X  2 .   ? -24.259 69.409 3.453  1.00 34.80 ? 2219 NAG R C5  1 
HETATM 12253 C  C6  . NAG X  2 .   ? -24.409 70.819 3.961  1.00 32.84 ? 2219 NAG R C6  1 
HETATM 12254 C  C7  . NAG X  2 .   ? -26.066 64.519 2.516  1.00 40.52 ? 2219 NAG R C7  1 
HETATM 12255 C  C8  . NAG X  2 .   ? -25.650 63.093 2.187  1.00 41.47 ? 2219 NAG R C8  1 
HETATM 12256 N  N2  . NAG X  2 .   ? -25.088 65.413 2.566  1.00 39.05 ? 2219 NAG R N2  1 
HETATM 12257 O  O3  . NAG X  2 .   ? -25.633 67.457 0.543  1.00 39.53 ? 2219 NAG R O3  1 
HETATM 12258 O  O4  . NAG X  2 .   ? -24.422 69.975 1.090  1.00 38.92 ? 2219 NAG R O4  1 
HETATM 12259 O  O5  . NAG X  2 .   ? -24.794 68.539 4.470  1.00 32.87 ? 2219 NAG R O5  1 
HETATM 12260 O  O6  . NAG X  2 .   ? -25.760 71.071 4.303  1.00 32.58 ? 2219 NAG R O6  1 
HETATM 12261 O  O7  . NAG X  2 .   ? -27.253 64.798 2.702  1.00 40.66 ? 2219 NAG R O7  1 
HETATM 12262 C  C1  . NAG Y  2 .   ? -25.203 71.023 0.636  1.00 42.13 ? 2220 NAG R C1  1 
HETATM 12263 C  C2  . NAG Y  2 .   ? -24.320 71.965 -0.191 1.00 42.69 ? 2220 NAG R C2  1 
HETATM 12264 C  C3  . NAG Y  2 .   ? -25.144 73.031 -0.926 1.00 44.04 ? 2220 NAG R C3  1 
HETATM 12265 C  C4  . NAG Y  2 .   ? -26.400 72.448 -1.600 1.00 45.10 ? 2220 NAG R C4  1 
HETATM 12266 C  C5  . NAG Y  2 .   ? -27.154 71.498 -0.654 1.00 45.19 ? 2220 NAG R C5  1 
HETATM 12267 C  C6  . NAG Y  2 .   ? -28.298 70.776 -1.363 1.00 45.70 ? 2220 NAG R C6  1 
HETATM 12268 C  C7  . NAG Y  2 .   ? -22.117 72.270 0.724  1.00 41.16 ? 2220 NAG R C7  1 
HETATM 12269 C  C8  . NAG Y  2 .   ? -21.205 73.018 1.674  1.00 41.41 ? 2220 NAG R C8  1 
HETATM 12270 N  N2  . NAG Y  2 .   ? -23.389 72.635 0.697  1.00 41.88 ? 2220 NAG R N2  1 
HETATM 12271 O  O3  . NAG Y  2 .   ? -24.318 73.630 -1.908 1.00 43.91 ? 2220 NAG R O3  1 
HETATM 12272 O  O4  . NAG Y  2 .   ? -27.267 73.503 -1.996 1.00 46.52 ? 2220 NAG R O4  1 
HETATM 12273 O  O5  . NAG Y  2 .   ? -26.260 70.479 -0.162 1.00 42.91 ? 2220 NAG R O5  1 
HETATM 12274 O  O6  . NAG Y  2 .   ? -29.189 70.186 -0.422 1.00 46.26 ? 2220 NAG R O6  1 
HETATM 12275 O  O7  . NAG Y  2 .   ? -21.672 71.363 0.026  1.00 42.19 ? 2220 NAG R O7  1 
HETATM 12276 C  C1  . NAG Z  2 .   ? 5.008   77.431 14.364 1.00 30.35 ? 2229 NAG S C1  1 
HETATM 12277 C  C2  . NAG Z  2 .   ? 4.846   77.974 12.936 1.00 31.72 ? 2229 NAG S C2  1 
HETATM 12278 C  C3  . NAG Z  2 .   ? 6.173   78.559 12.493 1.00 34.70 ? 2229 NAG S C3  1 
HETATM 12279 C  C4  . NAG Z  2 .   ? 6.672   79.624 13.472 1.00 36.01 ? 2229 NAG S C4  1 
HETATM 12280 C  C5  . NAG Z  2 .   ? 6.641   79.098 14.921 1.00 35.76 ? 2229 NAG S C5  1 
HETATM 12281 C  C6  . NAG Z  2 .   ? 6.882   80.215 15.918 1.00 35.71 ? 2229 NAG S C6  1 
HETATM 12282 C  C7  . NAG Z  2 .   ? 3.245   76.853 11.532 1.00 30.41 ? 2229 NAG S C7  1 
HETATM 12283 C  C8  . NAG Z  2 .   ? 2.972   75.755 10.511 1.00 30.62 ? 2229 NAG S C8  1 
HETATM 12284 N  N2  . NAG Z  2 .   ? 4.483   76.941 11.992 1.00 29.36 ? 2229 NAG S N2  1 
HETATM 12285 O  O3  . NAG Z  2 .   ? 6.033   79.106 11.194 1.00 33.25 ? 2229 NAG S O3  1 
HETATM 12286 O  O4  . NAG Z  2 .   ? 8.035   79.936 13.132 1.00 40.30 ? 2229 NAG S O4  1 
HETATM 12287 O  O5  . NAG Z  2 .   ? 5.357   78.509 15.244 1.00 32.29 ? 2229 NAG S O5  1 
HETATM 12288 O  O6  . NAG Z  2 .   ? 7.217   79.695 17.195 1.00 39.78 ? 2229 NAG S O6  1 
HETATM 12289 O  O7  . NAG Z  2 .   ? 2.330   77.584 11.916 1.00 31.10 ? 2229 NAG S O7  1 
HETATM 12290 C  C1  . NAG AA 2 .   ? 8.330   81.235 12.755 1.00 43.02 ? 2230 NAG S C1  1 
HETATM 12291 C  C2  . NAG AA 2 .   ? 9.844   81.437 12.889 1.00 44.46 ? 2230 NAG S C2  1 
HETATM 12292 C  C3  . NAG AA 2 .   ? 10.329  82.742 12.205 1.00 45.02 ? 2230 NAG S C3  1 
HETATM 12293 C  C4  . NAG AA 2 .   ? 9.712   82.927 10.817 1.00 45.82 ? 2230 NAG S C4  1 
HETATM 12294 C  C5  . NAG AA 2 .   ? 8.196   82.735 10.895 1.00 46.45 ? 2230 NAG S C5  1 
HETATM 12295 C  C6  . NAG AA 2 .   ? 7.496   82.880 9.548  1.00 46.45 ? 2230 NAG S C6  1 
HETATM 12296 C  C7  . NAG AA 2 .   ? 10.683  80.389 14.901 1.00 46.17 ? 2230 NAG S C7  1 
HETATM 12297 C  C8  . NAG AA 2 .   ? 10.993  80.488 16.389 1.00 46.05 ? 2230 NAG S C8  1 
HETATM 12298 N  N2  . NAG AA 2 .   ? 10.179  81.468 14.307 1.00 45.04 ? 2230 NAG S N2  1 
HETATM 12299 O  O3  . NAG AA 2 .   ? 11.740  82.685 12.073 1.00 45.33 ? 2230 NAG S O3  1 
HETATM 12300 O  O4  . NAG AA 2 .   ? 10.020  84.211 10.300 1.00 47.19 ? 2230 NAG S O4  1 
HETATM 12301 O  O5  . NAG AA 2 .   ? 7.911   81.406 11.394 1.00 44.24 ? 2230 NAG S O5  1 
HETATM 12302 O  O6  . NAG AA 2 .   ? 8.109   82.066 8.555  1.00 48.67 ? 2230 NAG S O6  1 
HETATM 12303 O  O7  . NAG AA 2 .   ? 10.914  79.338 14.294 1.00 47.17 ? 2230 NAG S O7  1 
HETATM 12304 C  C1  . NAG BA 2 .   ? -2.118  73.219 -1.119 1.00 30.59 ? 2281 NAG T C1  1 
HETATM 12305 C  C2  . NAG BA 2 .   ? -0.639  73.171 -1.509 1.00 31.15 ? 2281 NAG T C2  1 
HETATM 12306 C  C3  . NAG BA 2 .   ? 0.242   73.526 -0.306 1.00 32.73 ? 2281 NAG T C3  1 
HETATM 12307 C  C4  . NAG BA 2 .   ? -0.191  74.882 0.211  1.00 35.03 ? 2281 NAG T C4  1 
HETATM 12308 C  C5  . NAG BA 2 .   ? -1.672  74.835 0.591  1.00 34.32 ? 2281 NAG T C5  1 
HETATM 12309 C  C6  . NAG BA 2 .   ? -2.187  76.173 1.087  1.00 36.24 ? 2281 NAG T C6  1 
HETATM 12310 C  C7  . NAG BA 2 .   ? -0.176  71.673 -3.334 1.00 30.77 ? 2281 NAG T C7  1 
HETATM 12311 C  C8  . NAG BA 2 .   ? 0.131   70.256 -3.796 1.00 30.64 ? 2281 NAG T C8  1 
HETATM 12312 N  N2  . NAG BA 2 .   ? -0.332  71.854 -2.028 1.00 30.29 ? 2281 NAG T N2  1 
HETATM 12313 O  O3  . NAG BA 2 .   ? 1.621   73.551 -0.654 1.00 31.37 ? 2281 NAG T O3  1 
HETATM 12314 O  O4  . NAG BA 2 .   ? 0.591   75.248 1.356  1.00 40.61 ? 2281 NAG T O4  1 
HETATM 12315 O  O5  . NAG BA 2 .   ? -2.459  74.492 -0.559 1.00 31.28 ? 2281 NAG T O5  1 
HETATM 12316 O  O6  . NAG BA 2 .   ? -1.860  77.214 0.180  1.00 38.33 ? 2281 NAG T O6  1 
HETATM 12317 O  O7  . NAG BA 2 .   ? -0.257  72.588 -4.152 1.00 31.32 ? 2281 NAG T O7  1 
HETATM 12318 C  C1  . NAG CA 2 .   ? 1.418   76.348 1.202  1.00 44.21 ? 2282 NAG T C1  1 
HETATM 12319 C  C2  . NAG CA 2 .   ? 1.824   76.882 2.578  1.00 45.28 ? 2282 NAG T C2  1 
HETATM 12320 C  C3  . NAG CA 2 .   ? 2.792   78.079 2.379  1.00 46.92 ? 2282 NAG T C3  1 
HETATM 12321 C  C4  . NAG CA 2 .   ? 3.966   77.687 1.458  1.00 48.20 ? 2282 NAG T C4  1 
HETATM 12322 C  C5  . NAG CA 2 .   ? 3.446   77.064 0.154  1.00 48.02 ? 2282 NAG T C5  1 
HETATM 12323 C  C6  . NAG CA 2 .   ? 4.547   76.568 -0.791 1.00 48.49 ? 2282 NAG T C6  1 
HETATM 12324 C  C7  . NAG CA 2 .   ? 0.042   76.384 4.154  1.00 45.16 ? 2282 NAG T C7  1 
HETATM 12325 C  C8  . NAG CA 2 .   ? -1.219  76.818 4.876  1.00 44.23 ? 2282 NAG T C8  1 
HETATM 12326 N  N2  . NAG CA 2 .   ? 0.623   77.258 3.322  1.00 45.01 ? 2282 NAG T N2  1 
HETATM 12327 O  O3  . NAG CA 2 .   ? 3.301   78.501 3.639  1.00 48.14 ? 2282 NAG T O3  1 
HETATM 12328 O  O4  . NAG CA 2 .   ? 4.764   78.815 1.166  1.00 48.29 ? 2282 NAG T O4  1 
HETATM 12329 O  O5  . NAG CA 2 .   ? 2.579   75.940 0.461  1.00 47.05 ? 2282 NAG T O5  1 
HETATM 12330 O  O6  . NAG CA 2 .   ? 4.727   75.154 -0.730 1.00 48.14 ? 2282 NAG T O6  1 
HETATM 12331 O  O7  . NAG CA 2 .   ? 0.500   75.255 4.367  1.00 44.71 ? 2282 NAG T O7  1 
HETATM 12332 O  O   . HOH DA 6 .   ? 40.419  48.319 42.842 1.00 29.82 ? 1523 HOH A O   1 
HETATM 12333 O  O   . HOH DA 6 .   ? 63.198  42.176 44.712 1.00 14.70 ? 1524 HOH A O   1 
HETATM 12334 O  O   . HOH DA 6 .   ? 32.112  58.375 37.656 1.00 17.24 ? 1525 HOH A O   1 
HETATM 12335 O  O   . HOH DA 6 .   ? 44.362  44.212 34.153 1.00 15.86 ? 1526 HOH A O   1 
HETATM 12336 O  O   . HOH DA 6 .   ? 42.017  45.913 43.361 1.00 27.56 ? 1527 HOH A O   1 
HETATM 12337 O  O   . HOH DA 6 .   ? 49.535  41.123 30.299 1.00 18.60 ? 1528 HOH A O   1 
HETATM 12338 O  O   . HOH DA 6 .   ? 51.760  39.067 35.494 1.00 15.28 ? 1529 HOH A O   1 
HETATM 12339 O  O   . HOH DA 6 .   ? 37.233  59.782 31.648 1.00 16.78 ? 1530 HOH A O   1 
HETATM 12340 O  O   . HOH DA 6 .   ? 36.664  49.973 39.379 1.00 18.65 ? 1531 HOH A O   1 
HETATM 12341 O  O   . HOH DA 6 .   ? 42.127  50.392 31.016 1.00 21.20 ? 1532 HOH A O   1 
HETATM 12342 O  O   . HOH DA 6 .   ? 28.762  40.093 29.265 1.00 18.80 ? 1533 HOH A O   1 
HETATM 12343 O  O   . HOH DA 6 .   ? 29.243  51.620 31.206 1.00 16.07 ? 1534 HOH A O   1 
HETATM 12344 O  O   . HOH DA 6 .   ? 60.116  47.066 57.373 1.00 20.14 ? 1535 HOH A O   1 
HETATM 12345 O  O   . HOH DA 6 .   ? 21.758  62.063 37.244 1.00 16.95 ? 1536 HOH A O   1 
HETATM 12346 O  O   . HOH DA 6 .   ? 26.220  34.472 33.029 1.00 24.98 ? 1537 HOH A O   1 
HETATM 12347 O  O   . HOH DA 6 .   ? 38.400  63.549 29.002 1.00 17.50 ? 1538 HOH A O   1 
HETATM 12348 O  O   . HOH DA 6 .   ? 46.257  35.086 45.549 1.00 17.00 ? 1539 HOH A O   1 
HETATM 12349 O  O   . HOH DA 6 .   ? 58.425  42.617 49.120 1.00 19.42 ? 1540 HOH A O   1 
HETATM 12350 O  O   . HOH DA 6 .   ? 71.190  53.521 47.627 1.00 25.95 ? 1541 HOH A O   1 
HETATM 12351 O  O   . HOH DA 6 .   ? 30.101  52.552 16.616 1.00 23.20 ? 1542 HOH A O   1 
HETATM 12352 O  O   . HOH DA 6 .   ? 40.564  47.525 22.203 1.00 23.21 ? 1543 HOH A O   1 
HETATM 12353 O  O   . HOH DA 6 .   ? 67.830  53.401 55.870 1.00 22.47 ? 1544 HOH A O   1 
HETATM 12354 O  O   . HOH DA 6 .   ? 36.719  47.413 51.328 1.00 18.11 ? 1545 HOH A O   1 
HETATM 12355 O  O   . HOH DA 6 .   ? 54.248  36.943 43.485 1.00 15.64 ? 1546 HOH A O   1 
HETATM 12356 O  O   . HOH DA 6 .   ? 34.625  56.941 37.450 1.00 16.05 ? 1547 HOH A O   1 
HETATM 12357 O  O   . HOH DA 6 .   ? 58.613  49.465 33.147 1.00 15.34 ? 1548 HOH A O   1 
HETATM 12358 O  O   . HOH DA 6 .   ? 38.274  40.046 45.325 1.00 15.63 ? 1549 HOH A O   1 
HETATM 12359 O  O   . HOH DA 6 .   ? 43.662  63.205 15.716 1.00 18.21 ? 1550 HOH A O   1 
HETATM 12360 O  O   . HOH DA 6 .   ? 27.169  54.840 40.477 1.00 16.97 ? 1551 HOH A O   1 
HETATM 12361 O  O   . HOH DA 6 .   ? 56.807  54.000 44.859 1.00 21.97 ? 1552 HOH A O   1 
HETATM 12362 O  O   . HOH DA 6 .   ? 38.687  65.004 38.185 1.00 18.93 ? 1553 HOH A O   1 
HETATM 12363 O  O   . HOH DA 6 .   ? 39.323  46.571 37.117 1.00 15.89 ? 1554 HOH A O   1 
HETATM 12364 O  O   . HOH DA 6 .   ? 23.713  31.726 47.464 1.00 19.22 ? 1555 HOH A O   1 
HETATM 12365 O  O   . HOH DA 6 .   ? 24.465  56.867 33.934 1.00 15.32 ? 1556 HOH A O   1 
HETATM 12366 O  O   . HOH DA 6 .   ? 63.396  37.166 34.495 1.00 34.56 ? 1557 HOH A O   1 
HETATM 12367 O  O   . HOH DA 6 .   ? 34.023  45.665 53.200 1.00 17.73 ? 1558 HOH A O   1 
HETATM 12368 O  O   . HOH DA 6 .   ? 43.064  53.867 15.315 1.00 22.93 ? 1559 HOH A O   1 
HETATM 12369 O  O   . HOH DA 6 .   ? 57.902  51.017 36.173 1.00 22.48 ? 1560 HOH A O   1 
HETATM 12370 O  O   . HOH DA 6 .   ? 47.820  45.562 47.130 1.00 23.25 ? 1561 HOH A O   1 
HETATM 12371 O  O   . HOH DA 6 .   ? 28.496  62.610 36.944 1.00 16.94 ? 1562 HOH A O   1 
HETATM 12372 O  O   . HOH DA 6 .   ? 41.333  52.040 18.272 1.00 17.95 ? 1563 HOH A O   1 
HETATM 12373 O  O   . HOH DA 6 .   ? 40.606  38.020 39.590 1.00 18.64 ? 1564 HOH A O   1 
HETATM 12374 O  O   . HOH DA 6 .   ? 36.621  65.340 28.519 1.00 24.48 ? 1565 HOH A O   1 
HETATM 12375 O  O   . HOH DA 6 .   ? 34.394  46.147 45.668 1.00 15.64 ? 1566 HOH A O   1 
HETATM 12376 O  O   . HOH DA 6 .   ? 56.472  40.874 49.833 1.00 21.41 ? 1567 HOH A O   1 
HETATM 12377 O  O   . HOH DA 6 .   ? 50.480  38.160 50.453 1.00 20.83 ? 1568 HOH A O   1 
HETATM 12378 O  O   . HOH DA 6 .   ? 34.752  58.992 35.631 1.00 16.28 ? 1569 HOH A O   1 
HETATM 12379 O  O   . HOH DA 6 .   ? 40.530  54.118 16.397 1.00 18.91 ? 1570 HOH A O   1 
HETATM 12380 O  O   . HOH DA 6 .   ? 64.883  69.433 25.005 1.00 24.47 ? 1571 HOH A O   1 
HETATM 12381 O  O   . HOH DA 6 .   ? 37.329  59.031 34.357 1.00 18.14 ? 1572 HOH A O   1 
HETATM 12382 O  O   . HOH DA 6 .   ? 53.845  50.379 46.761 1.00 17.64 ? 1573 HOH A O   1 
HETATM 12383 O  O   . HOH DA 6 .   ? 73.977  57.237 53.076 1.00 25.43 ? 1574 HOH A O   1 
HETATM 12384 O  O   . HOH DA 6 .   ? 79.099  54.632 37.206 1.00 23.17 ? 1575 HOH A O   1 
HETATM 12385 O  O   . HOH DA 6 .   ? 40.767  39.938 43.875 1.00 19.88 ? 1576 HOH A O   1 
HETATM 12386 O  O   . HOH DA 6 .   ? 42.504  56.202 35.473 1.00 18.47 ? 1577 HOH A O   1 
HETATM 12387 O  O   . HOH DA 6 .   ? 46.998  36.982 23.264 1.00 25.86 ? 1578 HOH A O   1 
HETATM 12388 O  O   . HOH DA 6 .   ? 55.910  61.908 63.777 1.00 25.23 ? 1579 HOH A O   1 
HETATM 12389 O  O   . HOH DA 6 .   ? 34.896  62.040 25.466 1.00 22.09 ? 1580 HOH A O   1 
HETATM 12390 O  O   . HOH DA 6 .   ? 31.230  62.199 36.960 1.00 20.68 ? 1581 HOH A O   1 
HETATM 12391 O  O   . HOH DA 6 .   ? 30.156  33.346 32.403 1.00 29.78 ? 1582 HOH A O   1 
HETATM 12392 O  O   . HOH DA 6 .   ? 21.410  40.125 23.275 1.00 26.74 ? 1583 HOH A O   1 
HETATM 12393 O  O   . HOH DA 6 .   ? 11.141  43.692 50.084 1.00 26.98 ? 1584 HOH A O   1 
HETATM 12394 O  O   . HOH DA 6 .   ? 51.705  67.589 31.682 1.00 27.59 ? 1585 HOH A O   1 
HETATM 12395 O  O   . HOH DA 6 .   ? 50.048  32.933 44.105 1.00 26.65 ? 1586 HOH A O   1 
HETATM 12396 O  O   . HOH DA 6 .   ? 66.812  68.697 31.476 1.00 30.41 ? 1587 HOH A O   1 
HETATM 12397 O  O   . HOH DA 6 .   ? 34.867  54.999 69.005 1.00 25.21 ? 1588 HOH A O   1 
HETATM 12398 O  O   . HOH DA 6 .   ? 34.171  56.008 46.170 1.00 32.67 ? 1589 HOH A O   1 
HETATM 12399 O  O   . HOH DA 6 .   ? 48.621  60.208 64.059 1.00 25.06 ? 1590 HOH A O   1 
HETATM 12400 O  O   . HOH DA 6 .   ? 43.033  55.504 19.162 1.00 22.90 ? 1591 HOH A O   1 
HETATM 12401 O  O   . HOH DA 6 .   ? 55.230  37.460 45.866 1.00 16.92 ? 1592 HOH A O   1 
HETATM 12402 O  O   . HOH DA 6 .   ? 44.475  67.319 12.922 1.00 39.25 ? 1593 HOH A O   1 
HETATM 12403 O  O   . HOH DA 6 .   ? 65.648  58.308 38.282 1.00 30.92 ? 1594 HOH A O   1 
HETATM 12404 O  O   . HOH DA 6 .   ? 34.550  60.492 37.991 1.00 25.73 ? 1595 HOH A O   1 
HETATM 12405 O  O   . HOH DA 6 .   ? 18.980  58.057 47.132 1.00 16.45 ? 1596 HOH A O   1 
HETATM 12406 O  O   . HOH DA 6 .   ? 34.551  57.970 55.648 1.00 23.99 ? 1597 HOH A O   1 
HETATM 12407 O  O   . HOH DA 6 .   ? 20.992  74.431 38.771 1.00 33.72 ? 1598 HOH A O   1 
HETATM 12408 O  O   . HOH DA 6 .   ? 19.269  54.953 59.655 1.00 27.24 ? 1599 HOH A O   1 
HETATM 12409 O  O   . HOH DA 6 .   ? 35.882  68.627 24.629 1.00 27.76 ? 1600 HOH A O   1 
HETATM 12410 O  O   . HOH DA 6 .   ? 49.047  37.484 38.912 1.00 17.66 ? 1601 HOH A O   1 
HETATM 12411 O  O   . HOH DA 6 .   ? 51.950  33.127 45.924 1.00 23.35 ? 1602 HOH A O   1 
HETATM 12412 O  O   . HOH DA 6 .   ? 55.284  41.925 28.640 1.00 21.16 ? 1603 HOH A O   1 
HETATM 12413 O  O   . HOH DA 6 .   ? 63.350  66.440 56.816 1.00 25.59 ? 1604 HOH A O   1 
HETATM 12414 O  O   . HOH DA 6 .   ? 80.131  51.307 38.035 1.00 40.56 ? 1605 HOH A O   1 
HETATM 12415 O  O   . HOH DA 6 .   ? 41.323  77.771 22.052 1.00 31.90 ? 1606 HOH A O   1 
HETATM 12416 O  O   . HOH DA 6 .   ? 53.151  32.781 35.319 1.00 24.52 ? 1607 HOH A O   1 
HETATM 12417 O  O   . HOH DA 6 .   ? 37.322  38.713 47.595 1.00 20.79 ? 1608 HOH A O   1 
HETATM 12418 O  O   . HOH DA 6 .   ? 20.691  59.574 34.705 1.00 25.42 ? 1609 HOH A O   1 
HETATM 12419 O  O   . HOH DA 6 .   ? 52.115  38.843 28.876 1.00 24.87 ? 1610 HOH A O   1 
HETATM 12420 O  O   . HOH DA 6 .   ? 17.706  72.107 31.479 1.00 23.43 ? 1611 HOH A O   1 
HETATM 12421 O  O   . HOH DA 6 .   ? 28.016  51.959 64.599 1.00 22.73 ? 1612 HOH A O   1 
HETATM 12422 O  O   . HOH DA 6 .   ? 47.385  44.412 56.948 1.00 28.49 ? 1613 HOH A O   1 
HETATM 12423 O  O   . HOH DA 6 .   ? 46.928  54.546 36.545 1.00 28.84 ? 1614 HOH A O   1 
HETATM 12424 O  O   . HOH DA 6 .   ? 70.580  44.926 26.724 1.00 19.74 ? 1615 HOH A O   1 
HETATM 12425 O  O   . HOH DA 6 .   ? 18.833  49.054 53.889 1.00 27.76 ? 1616 HOH A O   1 
HETATM 12426 O  O   . HOH DA 6 .   ? 15.507  69.017 37.939 1.00 24.58 ? 1617 HOH A O   1 
HETATM 12427 O  O   . HOH DA 6 .   ? 36.955  52.272 15.146 1.00 21.78 ? 1618 HOH A O   1 
HETATM 12428 O  O   . HOH DA 6 .   ? 49.481  62.038 30.084 1.00 24.36 ? 1619 HOH A O   1 
HETATM 12429 O  O   . HOH DA 6 .   ? 56.246  34.857 45.348 1.00 25.03 ? 1620 HOH A O   1 
HETATM 12430 O  O   . HOH DA 6 .   ? 61.616  43.941 19.056 1.00 25.30 ? 1621 HOH A O   1 
HETATM 12431 O  O   . HOH DA 6 .   ? 47.116  38.125 46.234 1.00 17.28 ? 1622 HOH A O   1 
HETATM 12432 O  O   . HOH DA 6 .   ? 69.069  39.746 39.867 1.00 24.33 ? 1623 HOH A O   1 
HETATM 12433 O  O   . HOH DA 6 .   ? 58.963  67.753 59.097 1.00 29.56 ? 1624 HOH A O   1 
HETATM 12434 O  O   . HOH DA 6 .   ? 42.277  53.970 55.404 1.00 24.35 ? 1625 HOH A O   1 
HETATM 12435 O  O   . HOH DA 6 .   ? 35.200  48.333 53.631 1.00 22.53 ? 1626 HOH A O   1 
HETATM 12436 O  O   . HOH DA 6 .   ? 59.867  51.911 57.944 1.00 22.80 ? 1627 HOH A O   1 
HETATM 12437 O  O   . HOH DA 6 .   ? 62.057  63.968 42.320 1.00 24.71 ? 1628 HOH A O   1 
HETATM 12438 O  O   . HOH DA 6 .   ? 48.910  57.682 56.100 1.00 28.77 ? 1629 HOH A O   1 
HETATM 12439 O  O   . HOH DA 6 .   ? 39.007  50.756 51.952 1.00 21.48 ? 1630 HOH A O   1 
HETATM 12440 O  O   . HOH DA 6 .   ? 58.292  73.252 15.999 1.00 37.21 ? 1631 HOH A O   1 
HETATM 12441 O  O   . HOH DA 6 .   ? 46.109  48.438 14.246 1.00 29.89 ? 1632 HOH A O   1 
HETATM 12442 O  O   . HOH DA 6 .   ? 66.857  76.717 58.489 1.00 36.49 ? 1633 HOH A O   1 
HETATM 12443 O  O   . HOH DA 6 .   ? 72.924  56.488 33.441 1.00 34.77 ? 1634 HOH A O   1 
HETATM 12444 O  O   . HOH DA 6 .   ? 15.982  50.336 49.347 1.00 22.52 ? 1635 HOH A O   1 
HETATM 12445 O  O   . HOH DA 6 .   ? 52.695  41.483 29.153 1.00 20.04 ? 1636 HOH A O   1 
HETATM 12446 O  O   . HOH DA 6 .   ? 66.075  46.220 54.894 1.00 38.06 ? 1637 HOH A O   1 
HETATM 12447 O  O   . HOH DA 6 .   ? 27.685  25.041 45.923 1.00 24.28 ? 1638 HOH A O   1 
HETATM 12448 O  O   . HOH DA 6 .   ? 13.103  45.127 27.602 1.00 24.53 ? 1639 HOH A O   1 
HETATM 12449 O  O   . HOH DA 6 .   ? 46.574  62.062 36.645 1.00 23.36 ? 1640 HOH A O   1 
HETATM 12450 O  O   . HOH DA 6 .   ? 38.217  61.688 40.902 1.00 27.74 ? 1641 HOH A O   1 
HETATM 12451 O  O   . HOH DA 6 .   ? 62.022  53.484 16.011 1.00 27.90 ? 1642 HOH A O   1 
HETATM 12452 O  O   . HOH DA 6 .   ? 50.622  41.106 37.603 1.00 24.48 ? 1643 HOH A O   1 
HETATM 12453 O  O   . HOH DA 6 .   ? 51.255  32.632 37.935 1.00 28.70 ? 1644 HOH A O   1 
HETATM 12454 O  O   . HOH DA 6 .   ? 62.554  34.585 30.084 1.00 36.93 ? 1645 HOH A O   1 
HETATM 12455 O  O   . HOH DA 6 .   ? 16.979  43.318 31.160 1.00 25.20 ? 1646 HOH A O   1 
HETATM 12456 O  O   . HOH DA 6 .   ? 16.845  36.301 32.638 1.00 23.67 ? 1647 HOH A O   1 
HETATM 12457 O  O   . HOH DA 6 .   ? 72.117  53.547 34.447 1.00 23.17 ? 1648 HOH A O   1 
HETATM 12458 O  O   . HOH DA 6 .   ? 58.609  62.005 29.520 1.00 23.89 ? 1649 HOH A O   1 
HETATM 12459 O  O   . HOH DA 6 .   ? 21.986  30.309 45.644 1.00 24.45 ? 1650 HOH A O   1 
HETATM 12460 O  O   . HOH DA 6 .   ? 40.938  40.298 66.539 1.00 24.39 ? 1651 HOH A O   1 
HETATM 12461 O  O   . HOH DA 6 .   ? 55.502  62.467 49.497 1.00 21.56 ? 1652 HOH A O   1 
HETATM 12462 O  O   . HOH DA 6 .   ? 36.033  58.679 24.774 1.00 28.59 ? 1653 HOH A O   1 
HETATM 12463 O  O   . HOH DA 6 .   ? 40.311  81.649 10.733 1.00 50.33 ? 1654 HOH A O   1 
HETATM 12464 O  O   . HOH DA 6 .   ? 67.905  45.559 23.391 1.00 25.88 ? 1655 HOH A O   1 
HETATM 12465 O  O   . HOH DA 6 .   ? 29.531  62.883 41.610 1.00 31.06 ? 1656 HOH A O   1 
HETATM 12466 O  O   . HOH DA 6 .   ? 9.720   44.887 33.304 1.00 30.02 ? 1657 HOH A O   1 
HETATM 12467 O  O   . HOH DA 6 .   ? 41.890  61.302 64.546 1.00 34.09 ? 1658 HOH A O   1 
HETATM 12468 O  O   . HOH DA 6 .   ? 57.082  60.740 67.319 1.00 23.42 ? 1659 HOH A O   1 
HETATM 12469 O  O   . HOH DA 6 .   ? 31.164  61.977 18.877 1.00 32.15 ? 1660 HOH A O   1 
HETATM 12470 O  O   . HOH DA 6 .   ? 55.304  81.537 31.303 1.00 26.64 ? 1661 HOH A O   1 
HETATM 12471 O  O   . HOH DA 6 .   ? 77.678  57.318 26.201 1.00 30.16 ? 1662 HOH A O   1 
HETATM 12472 O  O   . HOH DA 6 .   ? 14.478  67.623 30.125 1.00 20.51 ? 1663 HOH A O   1 
HETATM 12473 O  O   . HOH DA 6 .   ? 60.985  34.017 36.742 1.00 38.03 ? 1664 HOH A O   1 
HETATM 12474 O  O   . HOH DA 6 .   ? 51.765  61.177 52.454 1.00 27.49 ? 1665 HOH A O   1 
HETATM 12475 O  O   . HOH DA 6 .   ? 40.221  37.562 42.546 1.00 21.71 ? 1666 HOH A O   1 
HETATM 12476 O  O   . HOH DA 6 .   ? 34.230  39.817 69.413 1.00 43.95 ? 1667 HOH A O   1 
HETATM 12477 O  O   . HOH DA 6 .   ? 34.775  51.486 53.005 1.00 25.58 ? 1668 HOH A O   1 
HETATM 12478 O  O   . HOH DA 6 .   ? 74.171  56.969 30.465 1.00 26.09 ? 1669 HOH A O   1 
HETATM 12479 O  O   . HOH DA 6 .   ? 18.245  70.962 45.388 1.00 20.67 ? 1670 HOH A O   1 
HETATM 12480 O  O   . HOH DA 6 .   ? 30.487  66.582 49.227 1.00 34.09 ? 1671 HOH A O   1 
HETATM 12481 O  O   . HOH DA 6 .   ? 31.789  33.652 19.516 1.00 27.08 ? 1672 HOH A O   1 
HETATM 12482 O  O   . HOH DA 6 .   ? 11.912  39.367 49.145 1.00 30.46 ? 1673 HOH A O   1 
HETATM 12483 O  O   . HOH DA 6 .   ? 39.802  57.620 41.691 1.00 24.68 ? 1674 HOH A O   1 
HETATM 12484 O  O   . HOH DA 6 .   ? 42.456  46.434 40.360 1.00 18.98 ? 1675 HOH A O   1 
HETATM 12485 O  O   . HOH DA 6 .   ? 22.037  31.681 43.214 1.00 27.46 ? 1676 HOH A O   1 
HETATM 12486 O  O   . HOH DA 6 .   ? 46.631  45.852 59.014 1.00 21.19 ? 1677 HOH A O   1 
HETATM 12487 O  O   . HOH DA 6 .   ? 54.938  51.662 44.454 1.00 20.14 ? 1678 HOH A O   1 
HETATM 12488 O  O   . HOH DA 6 .   ? 41.454  45.103 38.233 1.00 20.14 ? 1679 HOH A O   1 
HETATM 12489 O  O   . HOH DA 6 .   ? 40.929  47.553 45.145 1.00 31.02 ? 1680 HOH A O   1 
HETATM 12490 O  O   . HOH DA 6 .   ? 48.408  38.596 48.666 1.00 21.39 ? 1681 HOH A O   1 
HETATM 12491 O  O   . HOH DA 6 .   ? 44.376  56.443 15.306 1.00 23.86 ? 1682 HOH A O   1 
HETATM 12492 O  O   . HOH DA 6 .   ? 8.721   39.615 42.746 1.00 21.21 ? 1683 HOH A O   1 
HETATM 12493 O  O   . HOH DA 6 .   ? 27.695  64.021 34.588 1.00 17.74 ? 1684 HOH A O   1 
HETATM 12494 O  O   . HOH DA 6 .   ? 39.636  46.155 54.341 1.00 19.90 ? 1685 HOH A O   1 
HETATM 12495 O  O   . HOH DA 6 .   ? 38.334  54.424 15.057 1.00 24.33 ? 1686 HOH A O   1 
HETATM 12496 O  O   . HOH DA 6 .   ? 37.787  75.536 27.867 1.00 28.33 ? 1687 HOH A O   1 
HETATM 12497 O  O   . HOH DA 6 .   ? 56.625  60.518 30.260 1.00 31.69 ? 1688 HOH A O   1 
HETATM 12498 O  O   . HOH DA 6 .   ? 23.126  59.388 56.050 1.00 18.33 ? 1689 HOH A O   1 
HETATM 12499 O  O   . HOH DA 6 .   ? 28.055  63.768 39.323 1.00 19.89 ? 1690 HOH A O   1 
HETATM 12500 O  O   . HOH DA 6 .   ? 37.218  27.179 41.818 1.00 29.44 ? 1691 HOH A O   1 
HETATM 12501 O  O   . HOH DA 6 .   ? 38.689  41.779 53.726 1.00 19.83 ? 1692 HOH A O   1 
HETATM 12502 O  O   . HOH DA 6 .   ? 59.015  54.094 56.455 1.00 17.29 ? 1693 HOH A O   1 
HETATM 12503 O  O   . HOH DA 6 .   ? 45.442  32.192 28.796 1.00 39.52 ? 1694 HOH A O   1 
HETATM 12504 O  O   . HOH DA 6 .   ? 22.855  55.344 31.998 1.00 19.22 ? 1695 HOH A O   1 
HETATM 12505 O  O   . HOH DA 6 .   ? 42.888  55.578 38.051 1.00 19.07 ? 1696 HOH A O   1 
HETATM 12506 O  O   . HOH DA 6 .   ? 34.459  66.011 25.625 1.00 24.63 ? 1697 HOH A O   1 
HETATM 12507 O  O   . HOH DA 6 .   ? 67.677  52.812 58.817 1.00 23.63 ? 1698 HOH A O   1 
HETATM 12508 O  O   . HOH DA 6 .   ? 36.449  52.629 39.701 1.00 30.55 ? 1699 HOH A O   1 
HETATM 12509 O  O   . HOH DA 6 .   ? 63.734  39.929 49.586 1.00 20.11 ? 1700 HOH A O   1 
HETATM 12510 O  O   . HOH DA 6 .   ? 49.675  48.664 33.753 1.00 24.90 ? 1701 HOH A O   1 
HETATM 12511 O  O   . HOH DA 6 .   ? 24.882  31.594 53.870 1.00 21.26 ? 1702 HOH A O   1 
HETATM 12512 O  O   . HOH DA 6 .   ? 65.601  56.923 15.607 1.00 33.58 ? 1703 HOH A O   1 
HETATM 12513 O  O   . HOH DA 6 .   ? 18.009  58.757 35.708 1.00 28.74 ? 1704 HOH A O   1 
HETATM 12514 O  O   . HOH DA 6 .   ? 43.029  61.604 13.801 1.00 30.10 ? 1705 HOH A O   1 
HETATM 12515 O  O   . HOH DA 6 .   ? 47.587  57.263 14.107 1.00 29.99 ? 1706 HOH A O   1 
HETATM 12516 O  O   . HOH DA 6 .   ? 42.387  45.855 54.506 1.00 21.24 ? 1707 HOH A O   1 
HETATM 12517 O  O   . HOH DA 6 .   ? 11.650  72.864 48.119 1.00 27.34 ? 1708 HOH A O   1 
HETATM 12518 O  O   . HOH DA 6 .   ? 66.570  38.864 40.844 1.00 23.04 ? 1709 HOH A O   1 
HETATM 12519 O  O   . HOH DA 6 .   ? 35.491  59.839 40.278 1.00 35.10 ? 1710 HOH A O   1 
HETATM 12520 O  O   . HOH DA 6 .   ? 72.959  45.948 45.579 1.00 28.42 ? 1711 HOH A O   1 
HETATM 12521 O  O   . HOH DA 6 .   ? 30.777  31.987 36.299 1.00 27.16 ? 1712 HOH A O   1 
HETATM 12522 O  O   . HOH DA 6 .   ? 61.638  52.377 60.153 1.00 26.60 ? 1713 HOH A O   1 
HETATM 12523 O  O   . HOH DA 6 .   ? 44.802  65.240 34.536 1.00 21.50 ? 1714 HOH A O   1 
HETATM 12524 O  O   . HOH DA 6 .   ? 43.155  67.257 35.268 1.00 24.22 ? 1715 HOH A O   1 
HETATM 12525 O  O   . HOH DA 6 .   ? 50.612  60.697 14.350 1.00 23.18 ? 1716 HOH A O   1 
HETATM 12526 O  O   . HOH DA 6 .   ? 18.724  75.900 38.614 1.00 28.78 ? 1717 HOH A O   1 
HETATM 12527 O  O   . HOH DA 6 .   ? 67.021  52.124 53.488 1.00 27.13 ? 1718 HOH A O   1 
HETATM 12528 O  O   . HOH DA 6 .   ? 37.616  57.196 61.755 1.00 35.13 ? 1719 HOH A O   1 
HETATM 12529 O  O   . HOH DA 6 .   ? 52.079  48.774 44.931 1.00 22.94 ? 1720 HOH A O   1 
HETATM 12530 O  O   . HOH DA 6 .   ? 23.820  26.757 52.066 1.00 26.96 ? 1721 HOH A O   1 
HETATM 12531 O  O   . HOH DA 6 .   ? 21.486  61.972 45.739 1.00 17.84 ? 1722 HOH A O   1 
HETATM 12532 O  O   . HOH DA 6 .   ? 42.248  42.716 22.757 1.00 28.36 ? 1723 HOH A O   1 
HETATM 12533 O  O   . HOH DA 6 .   ? 58.015  64.710 44.697 1.00 23.26 ? 1724 HOH A O   1 
HETATM 12534 O  O   . HOH DA 6 .   ? 58.992  62.198 63.667 1.00 34.40 ? 1725 HOH A O   1 
HETATM 12535 O  O   . HOH DA 6 .   ? 50.764  30.290 39.538 1.00 23.81 ? 1726 HOH A O   1 
HETATM 12536 O  O   . HOH DA 6 .   ? 33.306  54.041 49.080 1.00 25.25 ? 1727 HOH A O   1 
HETATM 12537 O  O   . HOH DA 6 .   ? 25.222  31.847 45.032 1.00 31.01 ? 1728 HOH A O   1 
HETATM 12538 O  O   . HOH DA 6 .   ? 53.003  53.053 30.157 1.00 26.33 ? 1729 HOH A O   1 
HETATM 12539 O  O   . HOH DA 6 .   ? 53.656  32.606 41.947 1.00 28.88 ? 1730 HOH A O   1 
HETATM 12540 O  O   . HOH DA 6 .   ? 55.809  36.178 28.881 1.00 35.28 ? 1731 HOH A O   1 
HETATM 12541 O  O   . HOH DA 6 .   ? 72.724  51.327 32.859 1.00 21.19 ? 1732 HOH A O   1 
HETATM 12542 O  O   . HOH DA 6 .   ? 24.420  56.794 59.956 1.00 28.04 ? 1733 HOH A O   1 
HETATM 12543 O  O   . HOH DA 6 .   ? 38.067  75.966 43.393 1.00 33.66 ? 1734 HOH A O   1 
HETATM 12544 O  O   . HOH DA 6 .   ? 69.348  43.028 17.237 1.00 34.71 ? 1735 HOH A O   1 
HETATM 12545 O  O   . HOH DA 6 .   ? 52.592  34.946 29.611 1.00 29.35 ? 1736 HOH A O   1 
HETATM 12546 O  O   . HOH DA 6 .   ? 15.006  38.088 32.951 1.00 27.73 ? 1737 HOH A O   1 
HETATM 12547 O  O   . HOH DA 6 .   ? 50.273  58.843 51.777 1.00 39.43 ? 1738 HOH A O   1 
HETATM 12548 O  O   . HOH DA 6 .   ? 55.295  67.479 30.602 1.00 25.56 ? 1739 HOH A O   1 
HETATM 12549 O  O   . HOH DA 6 .   ? 47.514  52.685 55.511 1.00 21.26 ? 1740 HOH A O   1 
HETATM 12550 O  O   . HOH DA 6 .   ? 46.897  84.040 35.156 1.00 38.95 ? 1741 HOH A O   1 
HETATM 12551 O  O   . HOH DA 6 .   ? 12.420  76.160 32.291 1.00 22.99 ? 1742 HOH A O   1 
HETATM 12552 O  O   . HOH DA 6 .   ? 9.295   78.189 32.819 1.00 35.56 ? 1743 HOH A O   1 
HETATM 12553 O  O   . HOH DA 6 .   ? 35.495  57.418 39.930 1.00 23.44 ? 1744 HOH A O   1 
HETATM 12554 O  O   . HOH DA 6 .   ? 29.997  50.501 15.153 1.00 34.28 ? 1745 HOH A O   1 
HETATM 12555 O  O   . HOH DA 6 .   ? 42.340  59.511 57.612 1.00 39.64 ? 1746 HOH A O   1 
HETATM 12556 O  O   . HOH DA 6 .   ? 22.928  67.559 41.897 1.00 25.56 ? 1747 HOH A O   1 
HETATM 12557 O  O   . HOH DA 6 .   ? 17.304  47.983 51.495 1.00 33.69 ? 1748 HOH A O   1 
HETATM 12558 O  O   . HOH DA 6 .   ? 57.489  54.933 25.310 1.00 21.42 ? 1749 HOH A O   1 
HETATM 12559 O  O   . HOH DA 6 .   ? 38.422  35.447 42.341 1.00 21.58 ? 1750 HOH A O   1 
HETATM 12560 O  O   . HOH DA 6 .   ? 16.045  69.923 47.272 1.00 27.18 ? 1751 HOH A O   1 
HETATM 12561 O  O   . HOH DA 6 .   ? 10.802  43.944 28.577 1.00 49.23 ? 1752 HOH A O   1 
HETATM 12562 O  O   . HOH DA 6 .   ? 27.755  54.719 64.872 1.00 35.18 ? 1753 HOH A O   1 
HETATM 12563 O  O   . HOH DA 6 .   ? 45.848  46.256 40.613 1.00 29.27 ? 1754 HOH A O   1 
HETATM 12564 O  O   . HOH DA 6 .   ? 62.426  62.480 39.711 1.00 38.23 ? 1755 HOH A O   1 
HETATM 12565 O  O   . HOH DA 6 .   ? 52.087  52.358 66.050 1.00 27.95 ? 1756 HOH A O   1 
HETATM 12566 O  O   . HOH DA 6 .   ? 72.848  46.812 33.225 1.00 24.83 ? 1757 HOH A O   1 
HETATM 12567 O  O   . HOH DA 6 .   ? 37.529  46.939 46.221 1.00 29.71 ? 1758 HOH A O   1 
HETATM 12568 O  O   . HOH DA 6 .   ? 57.538  57.456 31.413 1.00 43.80 ? 1759 HOH A O   1 
HETATM 12569 O  O   . HOH DA 6 .   ? 51.918  49.867 32.513 1.00 22.52 ? 1760 HOH A O   1 
HETATM 12570 O  O   . HOH DA 6 .   ? 49.954  58.074 13.193 1.00 29.97 ? 1761 HOH A O   1 
HETATM 12571 O  O   . HOH DA 6 .   ? 63.753  56.470 36.019 1.00 28.74 ? 1762 HOH A O   1 
HETATM 12572 O  O   . HOH DA 6 .   ? 31.528  64.067 39.906 1.00 41.49 ? 1763 HOH A O   1 
HETATM 12573 O  O   . HOH DA 6 .   ? 31.228  64.876 36.645 1.00 24.78 ? 1764 HOH A O   1 
HETATM 12574 O  O   . HOH DA 6 .   ? 42.848  70.128 34.958 1.00 22.27 ? 1765 HOH A O   1 
HETATM 12575 O  O   . HOH DA 6 .   ? 51.395  74.013 15.616 1.00 28.91 ? 1766 HOH A O   1 
HETATM 12576 O  O   . HOH DA 6 .   ? 66.946  73.213 46.225 1.00 30.98 ? 1767 HOH A O   1 
HETATM 12577 O  O   . HOH DA 6 .   ? 33.130  27.407 42.481 1.00 26.48 ? 1768 HOH A O   1 
HETATM 12578 O  O   . HOH DA 6 .   ? 51.550  50.350 64.418 1.00 20.89 ? 1769 HOH A O   1 
HETATM 12579 O  O   . HOH DA 6 .   ? 7.272   40.074 38.121 1.00 20.55 ? 1770 HOH A O   1 
HETATM 12580 O  O   . HOH DA 6 .   ? 33.667  60.650 50.055 1.00 36.04 ? 1771 HOH A O   1 
HETATM 12581 O  O   . HOH DA 6 .   ? 60.405  59.170 42.848 1.00 27.45 ? 1772 HOH A O   1 
HETATM 12582 O  O   . HOH DA 6 .   ? 54.413  44.871 32.318 1.00 26.51 ? 1773 HOH A O   1 
HETATM 12583 O  O   . HOH DA 6 .   ? 72.730  58.405 21.029 1.00 28.62 ? 1774 HOH A O   1 
HETATM 12584 O  O   . HOH DA 6 .   ? 38.170  51.802 12.065 1.00 38.90 ? 1775 HOH A O   1 
HETATM 12585 O  O   . HOH DA 6 .   ? 41.741  42.544 67.731 1.00 34.99 ? 1776 HOH A O   1 
HETATM 12586 O  O   . HOH DA 6 .   ? 44.943  81.971 25.985 1.00 38.88 ? 1777 HOH A O   1 
HETATM 12587 O  O   . HOH DA 6 .   ? 63.044  44.717 21.265 1.00 31.39 ? 1778 HOH A O   1 
HETATM 12588 O  O   . HOH DA 6 .   ? 39.384  46.955 56.953 1.00 22.94 ? 1779 HOH A O   1 
HETATM 12589 O  O   . HOH DA 6 .   ? 50.866  64.056 29.965 1.00 33.71 ? 1780 HOH A O   1 
HETATM 12590 O  O   . HOH DA 6 .   ? 53.014  47.515 35.797 1.00 25.39 ? 1781 HOH A O   1 
HETATM 12591 O  O   . HOH DA 6 .   ? 64.800  35.381 33.208 1.00 28.48 ? 1782 HOH A O   1 
HETATM 12592 O  O   . HOH DA 6 .   ? 37.307  67.805 27.559 1.00 21.96 ? 1783 HOH A O   1 
HETATM 12593 O  O   . HOH DA 6 .   ? 25.445  58.770 19.572 1.00 33.35 ? 1784 HOH A O   1 
HETATM 12594 O  O   . HOH DA 6 .   ? 60.389  71.738 14.972 1.00 37.65 ? 1785 HOH A O   1 
HETATM 12595 O  O   . HOH DA 6 .   ? 32.959  33.305 22.365 1.00 32.37 ? 1786 HOH A O   1 
HETATM 12596 O  O   . HOH DA 6 .   ? 34.810  53.368 44.881 1.00 40.91 ? 1787 HOH A O   1 
HETATM 12597 O  O   . HOH DA 6 .   ? 71.967  58.515 17.191 1.00 30.41 ? 1788 HOH A O   1 
HETATM 12598 O  O   . HOH DA 6 .   ? 46.187  73.766 14.166 1.00 33.01 ? 1789 HOH A O   1 
HETATM 12599 O  O   . HOH DA 6 .   ? 51.276  61.695 64.978 1.00 36.69 ? 1790 HOH A O   1 
HETATM 12600 O  O   . HOH DA 6 .   ? 54.696  45.937 29.320 1.00 41.91 ? 1791 HOH A O   1 
HETATM 12601 O  O   . HOH DA 6 .   ? 56.701  62.854 46.676 1.00 24.11 ? 1792 HOH A O   1 
HETATM 12602 O  O   . HOH DA 6 .   ? 74.040  58.369 37.903 1.00 26.72 ? 1793 HOH A O   1 
HETATM 12603 O  O   . HOH DA 6 .   ? 11.267  37.056 48.054 1.00 34.69 ? 1794 HOH A O   1 
HETATM 12604 O  O   . HOH DA 6 .   ? 67.567  47.806 56.613 1.00 43.77 ? 1795 HOH A O   1 
HETATM 12605 O  O   . HOH DA 6 .   ? 34.228  57.527 49.163 1.00 42.36 ? 1796 HOH A O   1 
HETATM 12606 O  O   . HOH DA 6 .   ? 58.910  43.863 55.759 1.00 30.79 ? 1797 HOH A O   1 
HETATM 12607 O  O   . HOH DA 6 .   ? 55.485  48.224 23.468 1.00 34.16 ? 1798 HOH A O   1 
HETATM 12608 O  O   . HOH DA 6 .   ? 40.974  47.723 12.841 1.00 30.87 ? 1799 HOH A O   1 
HETATM 12609 O  O   . HOH DA 6 .   ? 38.647  56.178 56.970 1.00 28.13 ? 1800 HOH A O   1 
HETATM 12610 O  O   . HOH DA 6 .   ? 52.859  47.650 64.402 1.00 37.41 ? 1801 HOH A O   1 
HETATM 12611 O  O   . HOH DA 6 .   ? 80.262  55.408 40.512 1.00 27.09 ? 1802 HOH A O   1 
HETATM 12612 O  O   . HOH DA 6 .   ? 22.268  30.927 53.204 1.00 27.79 ? 1803 HOH A O   1 
HETATM 12613 O  O   . HOH DA 6 .   ? 37.990  44.419 53.286 1.00 22.12 ? 1804 HOH A O   1 
HETATM 12614 O  O   . HOH DA 6 .   ? 67.400  37.464 29.707 1.00 26.68 ? 1805 HOH A O   1 
HETATM 12615 O  O   . HOH DA 6 .   ? 52.209  64.828 59.146 1.00 34.98 ? 1806 HOH A O   1 
HETATM 12616 O  O   . HOH DA 6 .   ? 55.879  50.964 42.113 1.00 23.27 ? 1807 HOH A O   1 
HETATM 12617 O  O   . HOH DA 6 .   ? 56.951  40.206 23.034 1.00 23.15 ? 1808 HOH A O   1 
HETATM 12618 O  O   . HOH DA 6 .   ? 21.351  56.398 29.978 1.00 21.36 ? 1809 HOH A O   1 
HETATM 12619 O  O   . HOH DA 6 .   ? 54.715  57.031 30.596 1.00 33.37 ? 1810 HOH A O   1 
HETATM 12620 O  O   . HOH DA 6 .   ? 63.167  57.737 31.095 1.00 30.89 ? 1811 HOH A O   1 
HETATM 12621 O  O   . HOH DA 6 .   ? 53.011  71.887 36.577 1.00 42.82 ? 1812 HOH A O   1 
HETATM 12622 O  O   . HOH DA 6 .   ? 42.428  47.860 47.481 1.00 32.11 ? 1813 HOH A O   1 
HETATM 12623 O  O   . HOH DA 6 .   ? 42.347  82.483 34.916 1.00 29.73 ? 1814 HOH A O   1 
HETATM 12624 O  O   . HOH DA 6 .   ? 63.140  35.181 46.610 1.00 25.93 ? 1815 HOH A O   1 
HETATM 12625 O  O   . HOH DA 6 .   ? 50.474  48.607 36.434 1.00 31.39 ? 1816 HOH A O   1 
HETATM 12626 O  O   . HOH DA 6 .   ? 53.405  34.399 43.656 1.00 25.29 ? 1817 HOH A O   1 
HETATM 12627 O  O   . HOH DA 6 .   ? 76.271  55.135 29.225 1.00 30.28 ? 1818 HOH A O   1 
HETATM 12628 O  O   . HOH DA 6 .   ? 26.873  67.498 28.111 1.00 27.83 ? 1819 HOH A O   1 
HETATM 12629 O  O   . HOH DA 6 .   ? 79.569  57.834 39.527 1.00 25.09 ? 1820 HOH A O   1 
HETATM 12630 O  O   . HOH DA 6 .   ? 50.855  40.745 57.423 1.00 30.44 ? 1821 HOH A O   1 
HETATM 12631 O  O   . HOH DA 6 .   ? 76.761  58.252 54.114 1.00 35.02 ? 1822 HOH A O   1 
HETATM 12632 O  O   . HOH DA 6 .   ? 14.901  74.179 33.116 1.00 26.15 ? 1823 HOH A O   1 
HETATM 12633 O  O   . HOH DA 6 .   ? 52.676  52.506 33.003 1.00 27.80 ? 1824 HOH A O   1 
HETATM 12634 O  O   . HOH DA 6 .   ? 73.144  50.869 23.413 1.00 36.33 ? 1825 HOH A O   1 
HETATM 12635 O  O   . HOH DA 6 .   ? 69.918  62.018 22.467 1.00 28.69 ? 1826 HOH A O   1 
HETATM 12636 O  O   . HOH DA 6 .   ? 20.422  32.929 58.848 1.00 31.86 ? 1827 HOH A O   1 
HETATM 12637 O  O   . HOH DA 6 .   ? 46.988  45.909 26.917 1.00 26.13 ? 1828 HOH A O   1 
HETATM 12638 O  O   . HOH DA 6 .   ? 75.739  46.901 45.580 1.00 31.85 ? 1829 HOH A O   1 
HETATM 12639 O  O   . HOH DA 6 .   ? 59.993  56.705 32.495 1.00 39.53 ? 1830 HOH A O   1 
HETATM 12640 O  O   . HOH DA 6 .   ? 59.586  60.499 65.690 1.00 26.67 ? 1831 HOH A O   1 
HETATM 12641 O  O   . HOH DA 6 .   ? 61.095  81.260 29.590 1.00 31.39 ? 1832 HOH A O   1 
HETATM 12642 O  O   . HOH DA 6 .   ? 35.679  40.598 14.269 1.00 41.62 ? 1833 HOH A O   1 
HETATM 12643 O  O   . HOH DA 6 .   ? 52.490  46.994 32.863 1.00 30.45 ? 1834 HOH A O   1 
HETATM 12644 O  O   . HOH DA 6 .   ? 60.066  80.955 21.242 1.00 41.35 ? 1835 HOH A O   1 
HETATM 12645 O  O   . HOH DA 6 .   ? 48.150  64.727 57.350 1.00 31.57 ? 1836 HOH A O   1 
HETATM 12646 O  O   . HOH DA 6 .   ? 14.979  76.086 35.370 1.00 27.05 ? 1837 HOH A O   1 
HETATM 12647 O  O   . HOH DA 6 .   ? 44.970  71.915 35.454 1.00 28.56 ? 1838 HOH A O   1 
HETATM 12648 O  O   . HOH DA 6 .   ? 44.843  46.252 43.318 1.00 41.63 ? 1839 HOH A O   1 
HETATM 12649 O  O   . HOH DA 6 .   ? 8.763   37.452 44.416 1.00 29.21 ? 1840 HOH A O   1 
HETATM 12650 O  O   . HOH DA 6 .   ? 28.617  66.333 34.157 1.00 35.73 ? 1841 HOH A O   1 
HETATM 12651 O  O   . HOH DA 6 .   ? 46.270  61.465 70.201 1.00 28.37 ? 1842 HOH A O   1 
HETATM 12652 O  O   . HOH DA 6 .   ? 41.966  69.187 43.614 1.00 39.72 ? 1843 HOH A O   1 
HETATM 12653 O  O   . HOH DA 6 .   ? 27.382  66.016 50.018 1.00 37.19 ? 1844 HOH A O   1 
HETATM 12654 O  O   . HOH DA 6 .   ? 50.422  70.633 36.152 1.00 28.78 ? 1845 HOH A O   1 
HETATM 12655 O  O   . HOH DA 6 .   ? 26.977  28.828 53.557 1.00 34.52 ? 1846 HOH A O   1 
HETATM 12656 O  O   . HOH DA 6 .   ? 58.209  47.310 23.131 1.00 30.19 ? 1847 HOH A O   1 
HETATM 12657 O  O   . HOH DA 6 .   ? 76.757  49.443 38.972 1.00 35.70 ? 1848 HOH A O   1 
HETATM 12658 O  O   . HOH DA 6 .   ? 33.428  70.337 41.266 1.00 35.97 ? 1849 HOH A O   1 
HETATM 12659 O  O   . HOH DA 6 .   ? 43.261  65.293 38.430 1.00 29.31 ? 1850 HOH A O   1 
HETATM 12660 O  O   . HOH DA 6 .   ? 63.411  75.290 27.428 1.00 34.58 ? 1851 HOH A O   1 
HETATM 12661 O  O   . HOH DA 6 .   ? 76.154  58.838 30.207 1.00 36.09 ? 1852 HOH A O   1 
HETATM 12662 O  O   . HOH DA 6 .   ? 29.182  30.873 38.198 1.00 31.83 ? 1853 HOH A O   1 
HETATM 12663 O  O   . HOH DA 6 .   ? 36.374  54.917 52.570 1.00 28.36 ? 1854 HOH A O   1 
HETATM 12664 O  O   . HOH DA 6 .   ? 47.482  54.696 53.764 1.00 33.39 ? 1855 HOH A O   1 
HETATM 12665 O  O   . HOH DA 6 .   ? 59.325  69.535 16.940 1.00 28.82 ? 1856 HOH A O   1 
HETATM 12666 O  O   . HOH DA 6 .   ? 24.576  50.296 61.517 1.00 34.20 ? 1857 HOH A O   1 
HETATM 12667 O  O   . HOH DA 6 .   ? 55.096  57.809 48.216 1.00 31.48 ? 1858 HOH A O   1 
HETATM 12668 O  O   . HOH DA 6 .   ? 37.458  50.243 42.304 1.00 35.10 ? 1859 HOH A O   1 
HETATM 12669 O  O   . HOH DA 6 .   ? 47.328  64.635 35.494 1.00 29.89 ? 1860 HOH A O   1 
HETATM 12670 O  O   . HOH DA 6 .   ? 20.515  48.272 61.531 1.00 34.30 ? 1861 HOH A O   1 
HETATM 12671 O  O   . HOH DA 6 .   ? 49.553  64.643 34.226 1.00 34.59 ? 1862 HOH A O   1 
HETATM 12672 O  O   . HOH DA 6 .   ? 41.973  44.739 50.483 1.00 25.39 ? 1863 HOH A O   1 
HETATM 12673 O  O   . HOH DA 6 .   ? 28.169  26.752 60.290 1.00 36.34 ? 1864 HOH A O   1 
HETATM 12674 O  O   . HOH DA 6 .   ? 19.796  69.009 28.099 1.00 37.44 ? 1865 HOH A O   1 
HETATM 12675 O  O   . HOH DA 6 .   ? 73.220  66.406 42.987 1.00 37.34 ? 1866 HOH A O   1 
HETATM 12676 O  O   . HOH DA 6 .   ? 14.406  36.605 45.662 1.00 34.19 ? 1867 HOH A O   1 
HETATM 12677 O  O   . HOH DA 6 .   ? 45.963  61.334 63.984 1.00 35.49 ? 1868 HOH A O   1 
HETATM 12678 O  O   . HOH DA 6 .   ? 46.053  71.507 15.388 1.00 38.21 ? 1869 HOH A O   1 
HETATM 12679 O  O   . HOH DA 6 .   ? 39.759  66.108 40.363 1.00 30.76 ? 1870 HOH A O   1 
HETATM 12680 O  O   . HOH DA 6 .   ? 68.968  42.719 51.304 1.00 26.70 ? 1871 HOH A O   1 
HETATM 12681 O  O   . HOH DA 6 .   ? 34.572  53.064 47.238 1.00 43.30 ? 1872 HOH A O   1 
HETATM 12682 O  O   . HOH DA 6 .   ? 58.651  65.684 60.840 1.00 29.25 ? 1873 HOH A O   1 
HETATM 12683 O  O   . HOH DA 6 .   ? 54.571  37.987 27.012 1.00 31.21 ? 1874 HOH A O   1 
HETATM 12684 O  O   . HOH DA 6 .   ? 55.727  29.432 35.622 1.00 41.44 ? 1875 HOH A O   1 
HETATM 12685 O  O   . HOH DA 6 .   ? 41.256  56.445 56.525 1.00 26.39 ? 1876 HOH A O   1 
HETATM 12686 O  O   . HOH DA 6 .   ? 54.838  49.406 36.401 1.00 31.45 ? 1877 HOH A O   1 
HETATM 12687 O  O   . HOH DA 6 .   ? 36.416  70.655 29.434 1.00 31.94 ? 1878 HOH A O   1 
HETATM 12688 O  O   . HOH DA 6 .   ? 22.433  31.535 62.108 1.00 41.86 ? 1879 HOH A O   1 
HETATM 12689 O  O   . HOH DA 6 .   ? 27.926  51.707 17.681 1.00 36.23 ? 1880 HOH A O   1 
HETATM 12690 O  O   . HOH DA 6 .   ? 76.204  59.984 36.728 1.00 40.39 ? 1881 HOH A O   1 
HETATM 12691 O  O   . HOH DA 6 .   ? 17.566  46.743 54.988 1.00 35.90 ? 1882 HOH A O   1 
HETATM 12692 O  O   . HOH DA 6 .   ? 52.826  42.125 61.869 1.00 31.48 ? 1883 HOH A O   1 
HETATM 12693 O  O   . HOH DA 6 .   ? 77.043  37.891 44.364 1.00 41.68 ? 1884 HOH A O   1 
HETATM 12694 O  O   . HOH DA 6 .   ? 62.470  36.680 51.305 1.00 36.01 ? 1885 HOH A O   1 
HETATM 12695 O  O   . HOH DA 6 .   ? 59.391  56.721 42.868 1.00 31.58 ? 1886 HOH A O   1 
HETATM 12696 O  O   . HOH DA 6 .   ? 20.266  35.492 59.994 1.00 26.89 ? 1887 HOH A O   1 
HETATM 12697 O  O   . HOH DA 6 .   ? 37.643  78.994 44.025 1.00 41.43 ? 1888 HOH A O   1 
HETATM 12698 O  O   . HOH DA 6 .   ? 51.264  45.722 63.147 1.00 31.37 ? 1889 HOH A O   1 
HETATM 12699 O  O   . HOH DA 6 .   ? 24.073  63.980 44.134 1.00 34.87 ? 1890 HOH A O   1 
HETATM 12700 O  O   . HOH DA 6 .   ? 73.265  43.287 30.668 1.00 30.92 ? 1891 HOH A O   1 
HETATM 12701 O  O   . HOH DA 6 .   ? 32.742  43.872 69.283 1.00 29.77 ? 1892 HOH A O   1 
HETATM 12702 O  O   . HOH DA 6 .   ? 36.188  29.848 31.272 1.00 49.27 ? 1893 HOH A O   1 
HETATM 12703 O  O   . HOH DA 6 .   ? 57.210  54.703 12.237 1.00 38.06 ? 1894 HOH A O   1 
HETATM 12704 O  O   . HOH DA 6 .   ? 59.054  45.789 25.065 1.00 33.65 ? 1895 HOH A O   1 
HETATM 12705 O  O   . HOH DA 6 .   ? 43.869  41.124 24.204 1.00 32.08 ? 1896 HOH A O   1 
HETATM 12706 O  O   . HOH DA 6 .   ? 66.175  39.359 43.739 1.00 28.62 ? 1897 HOH A O   1 
HETATM 12707 O  O   . HOH DA 6 .   ? 51.298  58.250 31.430 1.00 43.33 ? 1898 HOH A O   1 
HETATM 12708 O  O   . HOH DA 6 .   ? 35.770  55.545 50.082 1.00 37.61 ? 1899 HOH A O   1 
HETATM 12709 O  O   . HOH DA 6 .   ? 24.621  69.608 41.003 1.00 29.85 ? 1900 HOH A O   1 
HETATM 12710 O  O   . HOH DA 6 .   ? 38.245  63.950 42.514 1.00 35.60 ? 1901 HOH A O   1 
HETATM 12711 O  O   . HOH DA 6 .   ? 55.856  56.370 15.904 1.00 25.77 ? 1902 HOH A O   1 
HETATM 12712 O  O   . HOH DA 6 .   ? 76.153  43.715 34.332 1.00 38.13 ? 1903 HOH A O   1 
HETATM 12713 O  O   . HOH DA 6 .   ? 52.770  54.881 65.981 1.00 33.63 ? 1904 HOH A O   1 
HETATM 12714 O  O   . HOH DA 6 .   ? 28.928  68.435 21.518 1.00 46.30 ? 1905 HOH A O   1 
HETATM 12715 O  O   . HOH DA 6 .   ? 24.870  66.233 43.459 1.00 36.15 ? 1906 HOH A O   1 
HETATM 12716 O  O   . HOH DA 6 .   ? 37.233  78.814 35.516 1.00 36.01 ? 1907 HOH A O   1 
HETATM 12717 O  O   . HOH DA 6 .   ? 35.406  50.804 46.745 1.00 33.63 ? 1908 HOH A O   1 
HETATM 12718 O  O   . HOH DA 6 .   ? 55.034  29.062 40.165 1.00 45.58 ? 1909 HOH A O   1 
HETATM 12719 O  O   . HOH DA 6 .   ? 27.848  41.808 26.142 1.00 22.57 ? 1910 HOH A O   1 
HETATM 12720 O  O   . HOH DA 6 .   ? 45.890  49.027 27.316 1.00 27.65 ? 1911 HOH A O   1 
HETATM 12721 O  O   . HOH DA 6 .   ? 52.685  32.466 31.296 1.00 40.19 ? 1912 HOH A O   1 
HETATM 12722 O  O   . HOH DA 6 .   ? 56.664  42.531 52.545 1.00 39.36 ? 1913 HOH A O   1 
HETATM 12723 O  O   . HOH DA 6 .   ? 60.680  65.437 30.272 1.00 39.28 ? 1914 HOH A O   1 
HETATM 12724 O  O   . HOH DA 6 .   ? 63.717  50.881 62.119 1.00 37.78 ? 1915 HOH A O   1 
HETATM 12725 O  O   . HOH DA 6 .   ? 54.547  67.435 10.153 1.00 29.08 ? 1916 HOH A O   1 
HETATM 12726 O  O   . HOH DA 6 .   ? 49.297  82.803 18.487 1.00 28.52 ? 1917 HOH A O   1 
HETATM 12727 O  O   . HOH DA 6 .   ? 42.311  66.280 40.750 1.00 32.11 ? 1918 HOH A O   1 
HETATM 12728 O  O   . HOH DA 6 .   ? 54.484  73.035 43.793 1.00 31.45 ? 1919 HOH A O   1 
HETATM 12729 O  O   . HOH DA 6 .   ? 52.777  52.528 50.797 1.00 25.26 ? 1920 HOH A O   1 
HETATM 12730 O  O   . HOH DA 6 .   ? 57.570  57.387 11.594 1.00 36.75 ? 1921 HOH A O   1 
HETATM 12731 O  O   . HOH DA 6 .   ? 52.632  57.677 28.892 1.00 29.17 ? 1922 HOH A O   1 
HETATM 12732 O  O   . HOH DA 6 .   ? 31.706  56.348 48.813 1.00 24.49 ? 1923 HOH A O   1 
HETATM 12733 O  O   . HOH DA 6 .   ? 11.930  36.612 45.280 1.00 35.79 ? 1924 HOH A O   1 
HETATM 12734 O  O   . HOH DA 6 .   ? 43.724  45.896 48.538 1.00 34.68 ? 1925 HOH A O   1 
HETATM 12735 O  O   . HOH DA 6 .   ? 26.891  58.536 61.450 1.00 40.32 ? 1926 HOH A O   1 
HETATM 12736 O  O   . HOH DA 6 .   ? 52.165  54.434 35.012 1.00 32.21 ? 1927 HOH A O   1 
HETATM 12737 O  O   . HOH DA 6 .   ? 37.155  57.625 58.228 1.00 35.65 ? 1928 HOH A O   1 
HETATM 12738 O  O   . HOH DA 6 .   ? 69.449  41.702 19.430 1.00 41.00 ? 1929 HOH A O   1 
HETATM 12739 O  O   . HOH DA 6 .   ? 73.219  53.754 27.930 1.00 27.73 ? 1930 HOH A O   1 
HETATM 12740 O  O   . HOH DA 6 .   ? 56.928  59.968 11.531 1.00 33.42 ? 1931 HOH A O   1 
HETATM 12741 O  O   . HOH DA 6 .   ? 18.195  62.420 29.281 1.00 31.01 ? 1932 HOH A O   1 
HETATM 12742 O  O   . HOH DA 6 .   ? 75.625  41.268 36.007 1.00 26.75 ? 1933 HOH A O   1 
HETATM 12743 O  O   . HOH DA 6 .   ? 76.744  59.018 39.335 1.00 39.06 ? 1934 HOH A O   1 
HETATM 12744 O  O   . HOH DA 6 .   ? 65.288  57.069 33.825 1.00 41.17 ? 1935 HOH A O   1 
HETATM 12745 O  O   . HOH DA 6 .   ? 6.407   37.765 37.339 1.00 34.03 ? 1936 HOH A O   1 
HETATM 12746 O  O   . HOH DA 6 .   ? 69.655  37.457 38.407 1.00 37.53 ? 1937 HOH A O   1 
HETATM 12747 O  O   . HOH DA 6 .   ? 72.496  49.326 51.505 1.00 39.35 ? 1938 HOH A O   1 
HETATM 12748 O  O   . HOH DA 6 .   ? 36.230  76.284 36.098 1.00 35.06 ? 1939 HOH A O   1 
HETATM 12749 O  O   . HOH DA 6 .   ? 30.464  61.128 43.398 1.00 38.32 ? 1940 HOH A O   1 
HETATM 12750 O  O   . HOH DA 6 .   ? 59.765  37.166 27.514 1.00 38.67 ? 1941 HOH A O   1 
HETATM 12751 O  O   . HOH DA 6 .   ? 35.879  49.024 44.224 1.00 39.02 ? 1942 HOH A O   1 
HETATM 12752 O  O   . HOH DA 6 .   ? 17.439  76.903 36.683 1.00 36.89 ? 1943 HOH A O   1 
HETATM 12753 O  O   . HOH DA 6 .   ? 36.329  80.507 28.968 1.00 37.08 ? 1944 HOH A O   1 
HETATM 12754 O  O   . HOH DA 6 .   ? 48.387  37.177 58.930 1.00 38.10 ? 1945 HOH A O   1 
HETATM 12755 O  O   . HOH DA 6 .   ? 57.759  64.829 29.465 1.00 35.14 ? 1946 HOH A O   1 
HETATM 12756 O  O   . HOH DA 6 .   ? 69.821  57.873 35.012 1.00 36.89 ? 1947 HOH A O   1 
HETATM 12757 O  O   . HOH DA 6 .   ? 56.359  39.948 27.101 1.00 37.98 ? 1948 HOH A O   1 
HETATM 12758 O  O   . HOH DA 6 .   ? 44.079  57.276 12.555 1.00 36.60 ? 1949 HOH A O   1 
HETATM 12759 O  O   . HOH DA 6 .   ? 43.569  46.959 57.674 1.00 40.53 ? 1950 HOH A O   1 
HETATM 12760 O  O   . HOH DA 6 .   ? 41.565  41.990 70.530 1.00 36.86 ? 1951 HOH A O   1 
HETATM 12761 O  O   . HOH DA 6 .   ? 49.432  55.396 35.214 1.00 34.44 ? 1952 HOH A O   1 
HETATM 12762 O  O   . HOH DA 6 .   ? 59.437  74.084 42.459 1.00 34.57 ? 1953 HOH A O   1 
HETATM 12763 O  O   . HOH DA 6 .   ? 51.187  65.808 54.126 1.00 32.77 ? 1954 HOH A O   1 
HETATM 12764 O  O   . HOH DA 6 .   ? 73.094  60.105 48.877 1.00 30.30 ? 1955 HOH A O   1 
HETATM 12765 O  O   . HOH DA 6 .   ? 10.679  32.929 37.347 1.00 38.47 ? 1956 HOH A O   1 
HETATM 12766 O  O   . HOH DA 6 .   ? 49.588  59.886 32.229 1.00 32.15 ? 1957 HOH A O   1 
HETATM 12767 O  O   . HOH DA 6 .   ? 61.923  79.458 31.599 1.00 35.64 ? 1958 HOH A O   1 
HETATM 12768 O  O   . HOH DA 6 .   ? 72.725  67.470 49.975 1.00 40.56 ? 1959 HOH A O   1 
HETATM 12769 O  O   . HOH DA 6 .   ? 47.281  71.359 36.547 1.00 42.27 ? 1960 HOH A O   1 
HETATM 12770 O  O   . HOH DA 6 .   ? 64.589  75.398 36.751 1.00 39.58 ? 1961 HOH A O   1 
HETATM 12771 O  O   . HOH DA 6 .   ? 77.421  50.258 36.797 1.00 36.57 ? 1962 HOH A O   1 
HETATM 12772 O  O   . HOH DA 6 .   ? 43.196  82.877 18.935 1.00 36.89 ? 1963 HOH A O   1 
HETATM 12773 O  O   . HOH DA 6 .   ? 60.524  35.355 47.125 1.00 38.41 ? 1964 HOH A O   1 
HETATM 12774 O  O   . HOH DA 6 .   ? 51.666  51.847 47.423 1.00 38.84 ? 1965 HOH A O   1 
HETATM 12775 O  O   . HOH DA 6 .   ? 46.872  57.370 54.253 1.00 35.64 ? 1966 HOH A O   1 
HETATM 12776 O  O   . HOH DA 6 .   ? 34.686  70.954 34.416 1.00 34.83 ? 1967 HOH A O   1 
HETATM 12777 O  O   . HOH DA 6 .   ? 54.210  51.329 40.344 1.00 32.43 ? 1968 HOH A O   1 
HETATM 12778 O  O   . HOH DA 6 .   ? 48.702  58.922 10.870 1.00 39.00 ? 1969 HOH A O   1 
HETATM 12779 O  O   . HOH DA 6 .   ? 17.047  33.612 34.365 1.00 35.34 ? 1970 HOH A O   1 
HETATM 12780 O  O   . HOH DA 6 .   ? 13.009  78.193 35.968 1.00 36.24 ? 1971 HOH A O   1 
HETATM 12781 O  O   . HOH DA 6 .   ? 14.552  48.424 50.333 1.00 28.77 ? 1972 HOH A O   1 
HETATM 12782 O  O   . HOH DA 6 .   ? 42.540  82.217 21.447 1.00 31.98 ? 1973 HOH A O   1 
HETATM 12783 O  O   . HOH DA 6 .   ? 43.209  49.026 70.005 1.00 37.00 ? 1974 HOH A O   1 
HETATM 12784 O  O   . HOH DA 6 .   ? 18.384  34.149 51.236 1.00 32.40 ? 1975 HOH A O   1 
HETATM 12785 O  O   . HOH EA 6 .   ? 0.402   58.582 31.933 1.00 15.38 ? 2323 HOH B O   1 
HETATM 12786 O  O   . HOH EA 6 .   ? 20.259  49.131 26.958 1.00 15.82 ? 2324 HOH B O   1 
HETATM 12787 O  O   . HOH EA 6 .   ? -0.782  55.091 30.495 1.00 36.36 ? 2325 HOH B O   1 
HETATM 12788 O  O   . HOH EA 6 .   ? 6.089   55.703 37.101 1.00 14.03 ? 2326 HOH B O   1 
HETATM 12789 O  O   . HOH EA 6 .   ? -31.407 63.505 39.019 1.00 18.68 ? 2327 HOH B O   1 
HETATM 12790 O  O   . HOH EA 6 .   ? -2.861  77.297 31.955 1.00 20.69 ? 2328 HOH B O   1 
HETATM 12791 O  O   . HOH EA 6 .   ? -6.665  71.896 2.821  1.00 17.09 ? 2329 HOH B O   1 
HETATM 12792 O  O   . HOH EA 6 .   ? 0.308   63.257 21.613 1.00 19.01 ? 2330 HOH B O   1 
HETATM 12793 O  O   . HOH EA 6 .   ? 5.190   64.263 16.280 1.00 25.97 ? 2331 HOH B O   1 
HETATM 12794 O  O   . HOH EA 6 .   ? 19.211  60.346 45.777 1.00 16.45 ? 2332 HOH B O   1 
HETATM 12795 O  O   . HOH EA 6 .   ? -14.750 74.660 38.232 1.00 17.30 ? 2333 HOH B O   1 
HETATM 12796 O  O   . HOH EA 6 .   ? 6.236   65.863 35.584 1.00 17.16 ? 2334 HOH B O   1 
HETATM 12797 O  O   . HOH EA 6 .   ? -8.262  60.428 48.709 1.00 19.23 ? 2335 HOH B O   1 
HETATM 12798 O  O   . HOH EA 6 .   ? 4.978   72.738 44.621 1.00 20.36 ? 2336 HOH B O   1 
HETATM 12799 O  O   . HOH EA 6 .   ? -19.030 59.534 48.404 1.00 26.28 ? 2337 HOH B O   1 
HETATM 12800 O  O   . HOH EA 6 .   ? -35.936 53.400 39.312 1.00 25.86 ? 2338 HOH B O   1 
HETATM 12801 O  O   . HOH EA 6 .   ? -11.490 62.514 29.866 1.00 28.66 ? 2339 HOH B O   1 
HETATM 12802 O  O   . HOH EA 6 .   ? -1.971  80.566 22.787 1.00 16.09 ? 2340 HOH B O   1 
HETATM 12803 O  O   . HOH EA 6 .   ? -0.829  60.855 27.995 1.00 18.89 ? 2341 HOH B O   1 
HETATM 12804 O  O   . HOH EA 6 .   ? 13.691  48.576 48.001 1.00 19.50 ? 2342 HOH B O   1 
HETATM 12805 O  O   . HOH EA 6 .   ? 2.768   69.114 24.878 1.00 18.99 ? 2343 HOH B O   1 
HETATM 12806 O  O   . HOH EA 6 .   ? -6.571  61.960 29.479 1.00 19.74 ? 2344 HOH B O   1 
HETATM 12807 O  O   . HOH EA 6 .   ? -16.873 63.816 50.852 1.00 21.87 ? 2345 HOH B O   1 
HETATM 12808 O  O   . HOH EA 6 .   ? -13.532 49.951 46.439 1.00 21.15 ? 2346 HOH B O   1 
HETATM 12809 O  O   . HOH EA 6 .   ? -9.290  66.428 47.634 1.00 21.43 ? 2347 HOH B O   1 
HETATM 12810 O  O   . HOH EA 6 .   ? -2.812  76.474 22.844 1.00 18.53 ? 2348 HOH B O   1 
HETATM 12811 O  O   . HOH EA 6 .   ? 10.113  70.067 19.261 1.00 26.48 ? 2349 HOH B O   1 
HETATM 12812 O  O   . HOH EA 6 .   ? -21.364 77.999 28.591 1.00 40.05 ? 2350 HOH B O   1 
HETATM 12813 O  O   . HOH EA 6 .   ? 2.408   63.478 5.712  1.00 25.29 ? 2351 HOH B O   1 
HETATM 12814 O  O   . HOH EA 6 .   ? -6.003  64.600 39.450 1.00 20.80 ? 2352 HOH B O   1 
HETATM 12815 O  O   . HOH EA 6 .   ? -2.325  54.886 24.241 1.00 23.53 ? 2353 HOH B O   1 
HETATM 12816 O  O   . HOH EA 6 .   ? 12.803  47.140 39.309 1.00 14.65 ? 2354 HOH B O   1 
HETATM 12817 O  O   . HOH EA 6 .   ? -17.243 74.528 0.790  1.00 26.58 ? 2355 HOH B O   1 
HETATM 12818 O  O   . HOH EA 6 .   ? 5.595   71.494 51.749 1.00 22.68 ? 2356 HOH B O   1 
HETATM 12819 O  O   . HOH EA 6 .   ? 3.559   80.583 25.985 1.00 19.43 ? 2357 HOH B O   1 
HETATM 12820 O  O   . HOH EA 6 .   ? -3.690  56.601 44.727 1.00 18.99 ? 2358 HOH B O   1 
HETATM 12821 O  O   . HOH EA 6 .   ? 12.589  62.388 34.284 1.00 18.24 ? 2359 HOH B O   1 
HETATM 12822 O  O   . HOH EA 6 .   ? -25.001 63.451 46.145 1.00 23.83 ? 2360 HOH B O   1 
HETATM 12823 O  O   . HOH EA 6 .   ? 2.663   79.767 23.749 1.00 20.91 ? 2361 HOH B O   1 
HETATM 12824 O  O   . HOH EA 6 .   ? 2.861   57.489 31.541 1.00 16.64 ? 2362 HOH B O   1 
HETATM 12825 O  O   . HOH EA 6 .   ? 4.228   66.740 22.365 1.00 21.87 ? 2363 HOH B O   1 
HETATM 12826 O  O   . HOH EA 6 .   ? -6.895  81.455 16.141 1.00 21.18 ? 2364 HOH B O   1 
HETATM 12827 O  O   . HOH EA 6 .   ? -14.855 74.758 5.148  1.00 16.17 ? 2365 HOH B O   1 
HETATM 12828 O  O   . HOH EA 6 .   ? 17.039  50.636 55.516 1.00 21.57 ? 2366 HOH B O   1 
HETATM 12829 O  O   . HOH EA 6 .   ? -20.490 66.574 50.971 1.00 25.59 ? 2367 HOH B O   1 
HETATM 12830 O  O   . HOH EA 6 .   ? -7.605  79.250 14.402 1.00 17.60 ? 2368 HOH B O   1 
HETATM 12831 O  O   . HOH EA 6 .   ? -35.140 51.667 33.119 1.00 25.57 ? 2369 HOH B O   1 
HETATM 12832 O  O   . HOH EA 6 .   ? -15.674 69.585 26.605 1.00 21.61 ? 2370 HOH B O   1 
HETATM 12833 O  O   . HOH EA 6 .   ? 12.072  60.972 21.250 1.00 25.28 ? 2371 HOH B O   1 
HETATM 12834 O  O   . HOH EA 6 .   ? -12.809 55.515 1.929  1.00 21.00 ? 2372 HOH B O   1 
HETATM 12835 O  O   . HOH EA 6 .   ? 17.018  56.771 34.239 1.00 25.09 ? 2373 HOH B O   1 
HETATM 12836 O  O   . HOH EA 6 .   ? 1.084   59.228 29.238 1.00 17.57 ? 2374 HOH B O   1 
HETATM 12837 O  O   . HOH EA 6 .   ? 8.842   56.614 26.664 1.00 17.73 ? 2375 HOH B O   1 
HETATM 12838 O  O   . HOH EA 6 .   ? -5.348  80.581 18.258 1.00 15.93 ? 2376 HOH B O   1 
HETATM 12839 O  O   . HOH EA 6 .   ? 0.630   54.782 63.334 1.00 26.70 ? 2377 HOH B O   1 
HETATM 12840 O  O   . HOH EA 6 .   ? -36.197 49.361 32.719 1.00 25.79 ? 2378 HOH B O   1 
HETATM 12841 O  O   . HOH EA 6 .   ? -14.211 84.483 15.432 1.00 40.00 ? 2379 HOH B O   1 
HETATM 12842 O  O   . HOH EA 6 .   ? 13.368  54.167 30.906 1.00 17.83 ? 2380 HOH B O   1 
HETATM 12843 O  O   . HOH EA 6 .   ? -19.679 76.314 35.453 1.00 22.71 ? 2381 HOH B O   1 
HETATM 12844 O  O   . HOH EA 6 .   ? -3.003  79.571 20.383 1.00 21.90 ? 2382 HOH B O   1 
HETATM 12845 O  O   . HOH EA 6 .   ? -21.199 79.320 40.010 1.00 38.04 ? 2383 HOH B O   1 
HETATM 12846 O  O   . HOH EA 6 .   ? -8.075  56.317 24.564 1.00 23.21 ? 2384 HOH B O   1 
HETATM 12847 O  O   . HOH EA 6 .   ? -3.397  65.532 -2.556 1.00 15.46 ? 2385 HOH B O   1 
HETATM 12848 O  O   . HOH EA 6 .   ? -29.624 46.856 37.398 1.00 19.98 ? 2386 HOH B O   1 
HETATM 12849 O  O   . HOH EA 6 .   ? 6.973   74.470 42.279 1.00 30.77 ? 2387 HOH B O   1 
HETATM 12850 O  O   . HOH EA 6 .   ? -15.243 75.585 2.433  1.00 20.88 ? 2388 HOH B O   1 
HETATM 12851 O  O   . HOH EA 6 .   ? -24.479 82.608 27.644 1.00 25.19 ? 2389 HOH B O   1 
HETATM 12852 O  O   . HOH EA 6 .   ? -22.378 69.409 29.423 1.00 20.06 ? 2390 HOH B O   1 
HETATM 12853 O  O   . HOH EA 6 .   ? -21.926 51.563 20.902 1.00 27.60 ? 2391 HOH B O   1 
HETATM 12854 O  O   . HOH EA 6 .   ? 4.390   55.999 28.227 1.00 19.24 ? 2392 HOH B O   1 
HETATM 12855 O  O   . HOH EA 6 .   ? 20.278  53.730 21.355 1.00 27.54 ? 2393 HOH B O   1 
HETATM 12856 O  O   . HOH EA 6 .   ? -22.137 68.579 6.911  1.00 19.20 ? 2394 HOH B O   1 
HETATM 12857 O  O   . HOH EA 6 .   ? 23.160  61.376 54.027 1.00 19.95 ? 2395 HOH B O   1 
HETATM 12858 O  O   . HOH EA 6 .   ? 4.127   84.878 44.871 1.00 32.15 ? 2396 HOH B O   1 
HETATM 12859 O  O   . HOH EA 6 .   ? -21.383 50.735 24.367 1.00 22.82 ? 2397 HOH B O   1 
HETATM 12860 O  O   . HOH EA 6 .   ? 16.085  42.521 27.512 1.00 28.15 ? 2398 HOH B O   1 
HETATM 12861 O  O   . HOH EA 6 .   ? -3.149  54.065 28.382 1.00 29.40 ? 2399 HOH B O   1 
HETATM 12862 O  O   . HOH EA 6 .   ? -24.090 55.310 6.935  1.00 25.21 ? 2400 HOH B O   1 
HETATM 12863 O  O   . HOH EA 6 .   ? 5.536   55.210 7.626  1.00 34.86 ? 2401 HOH B O   1 
HETATM 12864 O  O   . HOH EA 6 .   ? -30.245 74.956 11.237 1.00 39.02 ? 2402 HOH B O   1 
HETATM 12865 O  O   . HOH EA 6 .   ? 5.491   81.869 33.647 1.00 29.19 ? 2403 HOH B O   1 
HETATM 12866 O  O   . HOH EA 6 .   ? -3.288  60.622 38.282 1.00 23.45 ? 2404 HOH B O   1 
HETATM 12867 O  O   . HOH EA 6 .   ? -30.774 49.773 41.119 1.00 25.27 ? 2405 HOH B O   1 
HETATM 12868 O  O   . HOH EA 6 .   ? -29.816 81.194 26.275 1.00 21.91 ? 2406 HOH B O   1 
HETATM 12869 O  O   . HOH EA 6 .   ? -26.160 65.264 48.181 1.00 35.24 ? 2407 HOH B O   1 
HETATM 12870 O  O   . HOH EA 6 .   ? -16.088 66.742 -5.767 1.00 25.96 ? 2408 HOH B O   1 
HETATM 12871 O  O   . HOH EA 6 .   ? 21.556  69.097 43.687 1.00 23.88 ? 2409 HOH B O   1 
HETATM 12872 O  O   . HOH EA 6 .   ? -8.035  58.810 50.929 1.00 21.48 ? 2410 HOH B O   1 
HETATM 12873 O  O   . HOH EA 6 .   ? 7.236   55.509 28.378 1.00 24.85 ? 2411 HOH B O   1 
HETATM 12874 O  O   . HOH EA 6 .   ? -27.918 58.828 42.042 1.00 21.32 ? 2412 HOH B O   1 
HETATM 12875 O  O   . HOH EA 6 .   ? -15.306 62.651 13.815 1.00 23.32 ? 2413 HOH B O   1 
HETATM 12876 O  O   . HOH EA 6 .   ? -33.426 60.323 42.985 1.00 21.33 ? 2414 HOH B O   1 
HETATM 12877 O  O   . HOH EA 6 .   ? 5.194   54.758 25.681 1.00 27.24 ? 2415 HOH B O   1 
HETATM 12878 O  O   . HOH EA 6 .   ? -9.307  52.917 67.615 1.00 31.37 ? 2416 HOH B O   1 
HETATM 12879 O  O   . HOH EA 6 .   ? 16.425  58.022 58.862 1.00 24.36 ? 2417 HOH B O   1 
HETATM 12880 O  O   . HOH EA 6 .   ? -0.048  62.746 26.044 1.00 16.44 ? 2418 HOH B O   1 
HETATM 12881 O  O   . HOH EA 6 .   ? -11.871 60.062 -4.779 1.00 25.60 ? 2419 HOH B O   1 
HETATM 12882 O  O   . HOH EA 6 .   ? -14.918 64.736 -2.875 1.00 25.66 ? 2420 HOH B O   1 
HETATM 12883 O  O   . HOH EA 6 .   ? 0.067   70.652 53.920 1.00 26.50 ? 2421 HOH B O   1 
HETATM 12884 O  O   . HOH EA 6 .   ? -0.831  44.662 17.030 1.00 30.27 ? 2422 HOH B O   1 
HETATM 12885 O  O   . HOH EA 6 .   ? -2.725  58.922 35.949 1.00 20.73 ? 2423 HOH B O   1 
HETATM 12886 O  O   . HOH EA 6 .   ? 9.737   77.828 28.369 1.00 25.26 ? 2424 HOH B O   1 
HETATM 12887 O  O   . HOH EA 6 .   ? -20.162 82.506 33.743 1.00 22.64 ? 2425 HOH B O   1 
HETATM 12888 O  O   . HOH EA 6 .   ? -17.642 68.422 40.704 1.00 25.23 ? 2426 HOH B O   1 
HETATM 12889 O  O   . HOH EA 6 .   ? -20.074 83.002 17.951 1.00 21.59 ? 2427 HOH B O   1 
HETATM 12890 O  O   . HOH EA 6 .   ? -22.376 84.746 27.714 1.00 20.99 ? 2428 HOH B O   1 
HETATM 12891 O  O   . HOH EA 6 .   ? -7.360  50.156 19.675 1.00 37.76 ? 2429 HOH B O   1 
HETATM 12892 O  O   . HOH EA 6 .   ? -4.862  47.503 43.318 1.00 26.52 ? 2430 HOH B O   1 
HETATM 12893 O  O   . HOH EA 6 .   ? 11.800  74.470 38.886 1.00 28.82 ? 2431 HOH B O   1 
HETATM 12894 O  O   . HOH EA 6 .   ? -37.037 56.279 27.631 1.00 21.72 ? 2432 HOH B O   1 
HETATM 12895 O  O   . HOH EA 6 .   ? -17.289 62.063 48.224 1.00 22.26 ? 2433 HOH B O   1 
HETATM 12896 O  O   . HOH EA 6 .   ? -17.538 44.175 20.364 1.00 41.09 ? 2434 HOH B O   1 
HETATM 12897 O  O   . HOH EA 6 .   ? 1.700   36.138 43.413 1.00 38.01 ? 2435 HOH B O   1 
HETATM 12898 O  O   . HOH EA 6 .   ? -28.576 81.434 10.934 1.00 26.87 ? 2436 HOH B O   1 
HETATM 12899 O  O   . HOH EA 6 .   ? -1.523  78.652 26.170 1.00 18.01 ? 2437 HOH B O   1 
HETATM 12900 O  O   . HOH EA 6 .   ? 14.364  71.889 25.228 1.00 33.97 ? 2438 HOH B O   1 
HETATM 12901 O  O   . HOH EA 6 .   ? -21.537 37.188 26.745 1.00 49.02 ? 2439 HOH B O   1 
HETATM 12902 O  O   . HOH EA 6 .   ? 21.283  57.367 21.928 1.00 32.13 ? 2440 HOH B O   1 
HETATM 12903 O  O   . HOH EA 6 .   ? 20.562  57.984 56.093 1.00 19.87 ? 2441 HOH B O   1 
HETATM 12904 O  O   . HOH EA 6 .   ? -9.011  36.937 57.430 1.00 30.76 ? 2442 HOH B O   1 
HETATM 12905 O  O   . HOH EA 6 .   ? 6.458   42.375 4.316  1.00 50.83 ? 2443 HOH B O   1 
HETATM 12906 O  O   . HOH EA 6 .   ? 6.366   80.236 53.698 1.00 50.20 ? 2444 HOH B O   1 
HETATM 12907 O  O   . HOH EA 6 .   ? -13.626 81.517 8.660  1.00 33.98 ? 2445 HOH B O   1 
HETATM 12908 O  O   . HOH EA 6 .   ? -7.131  51.338 45.580 1.00 21.94 ? 2446 HOH B O   1 
HETATM 12909 O  O   . HOH EA 6 .   ? -13.693 81.027 17.307 1.00 17.96 ? 2447 HOH B O   1 
HETATM 12910 O  O   . HOH EA 6 .   ? -26.062 63.395 9.495  1.00 24.45 ? 2448 HOH B O   1 
HETATM 12911 O  O   . HOH EA 6 .   ? -29.710 52.671 43.795 1.00 25.90 ? 2449 HOH B O   1 
HETATM 12912 O  O   . HOH EA 6 .   ? -18.710 45.720 29.082 1.00 38.81 ? 2450 HOH B O   1 
HETATM 12913 O  O   . HOH EA 6 .   ? -8.508  69.011 -3.086 1.00 24.76 ? 2451 HOH B O   1 
HETATM 12914 O  O   . HOH EA 6 .   ? 5.197   62.298 61.945 1.00 30.43 ? 2452 HOH B O   1 
HETATM 12915 O  O   . HOH EA 6 .   ? -10.930 86.779 15.674 1.00 32.53 ? 2453 HOH B O   1 
HETATM 12916 O  O   . HOH EA 6 .   ? -10.148 69.240 38.778 1.00 20.54 ? 2454 HOH B O   1 
HETATM 12917 O  O   . HOH EA 6 .   ? 8.699   42.164 43.964 1.00 22.48 ? 2455 HOH B O   1 
HETATM 12918 O  O   . HOH EA 6 .   ? 2.517   62.247 17.711 1.00 25.34 ? 2456 HOH B O   1 
HETATM 12919 O  O   . HOH EA 6 .   ? -29.705 74.684 39.138 1.00 22.28 ? 2457 HOH B O   1 
HETATM 12920 O  O   . HOH EA 6 .   ? -17.383 68.702 45.110 1.00 21.38 ? 2458 HOH B O   1 
HETATM 12921 O  O   . HOH EA 6 .   ? -15.197 87.355 23.347 1.00 29.00 ? 2459 HOH B O   1 
HETATM 12922 O  O   . HOH EA 6 .   ? 0.388   69.368 56.005 1.00 27.46 ? 2460 HOH B O   1 
HETATM 12923 O  O   . HOH EA 6 .   ? 3.333   58.565 11.121 1.00 21.33 ? 2461 HOH B O   1 
HETATM 12924 O  O   . HOH EA 6 .   ? 20.669  55.835 54.607 1.00 21.09 ? 2462 HOH B O   1 
HETATM 12925 O  O   . HOH EA 6 .   ? -8.845  49.212 41.932 1.00 29.37 ? 2463 HOH B O   1 
HETATM 12926 O  O   . HOH EA 6 .   ? -5.401  62.094 -4.676 1.00 20.27 ? 2464 HOH B O   1 
HETATM 12927 O  O   . HOH EA 6 .   ? -18.974 67.097 17.094 1.00 24.98 ? 2465 HOH B O   1 
HETATM 12928 O  O   . HOH EA 6 .   ? -16.740 57.578 41.825 1.00 27.19 ? 2466 HOH B O   1 
HETATM 12929 O  O   . HOH EA 6 .   ? -12.362 54.141 45.800 1.00 26.89 ? 2467 HOH B O   1 
HETATM 12930 O  O   . HOH EA 6 .   ? 13.213  47.559 36.841 1.00 16.23 ? 2468 HOH B O   1 
HETATM 12931 O  O   . HOH EA 6 .   ? -20.321 38.547 29.286 1.00 45.54 ? 2469 HOH B O   1 
HETATM 12932 O  O   . HOH EA 6 .   ? -26.358 58.510 44.426 1.00 20.25 ? 2470 HOH B O   1 
HETATM 12933 O  O   . HOH EA 6 .   ? -18.889 78.355 42.323 1.00 31.21 ? 2471 HOH B O   1 
HETATM 12934 O  O   . HOH EA 6 .   ? -24.615 67.995 20.107 1.00 27.36 ? 2472 HOH B O   1 
HETATM 12935 O  O   . HOH EA 6 .   ? -23.327 69.134 49.220 1.00 27.49 ? 2473 HOH B O   1 
HETATM 12936 O  O   . HOH EA 6 .   ? 2.561   50.204 11.380 1.00 31.66 ? 2474 HOH B O   1 
HETATM 12937 O  O   . HOH EA 6 .   ? -33.209 37.963 31.138 1.00 33.25 ? 2475 HOH B O   1 
HETATM 12938 O  O   . HOH EA 6 .   ? -31.301 69.371 47.139 1.00 34.13 ? 2476 HOH B O   1 
HETATM 12939 O  O   . HOH EA 6 .   ? -15.735 25.708 20.195 1.00 44.62 ? 2477 HOH B O   1 
HETATM 12940 O  O   . HOH EA 6 .   ? -7.762  58.674 39.980 1.00 34.02 ? 2478 HOH B O   1 
HETATM 12941 O  O   . HOH EA 6 .   ? -9.086  57.512 41.559 1.00 30.28 ? 2479 HOH B O   1 
HETATM 12942 O  O   . HOH EA 6 .   ? -9.585  62.398 40.042 1.00 23.46 ? 2480 HOH B O   1 
HETATM 12943 O  O   . HOH EA 6 .   ? -6.274  68.579 32.665 1.00 21.05 ? 2481 HOH B O   1 
HETATM 12944 O  O   . HOH EA 6 .   ? -8.375  64.614 40.614 1.00 19.55 ? 2482 HOH B O   1 
HETATM 12945 O  O   . HOH EA 6 .   ? 15.056  62.992 33.003 1.00 22.91 ? 2483 HOH B O   1 
HETATM 12946 O  O   . HOH EA 6 .   ? -18.220 73.738 22.032 1.00 17.81 ? 2484 HOH B O   1 
HETATM 12947 O  O   . HOH EA 6 .   ? 0.016   79.253 23.937 1.00 22.81 ? 2485 HOH B O   1 
HETATM 12948 O  O   . HOH EA 6 .   ? 8.567   56.000 24.183 1.00 38.13 ? 2486 HOH B O   1 
HETATM 12949 O  O   . HOH EA 6 .   ? -4.868  64.704 -4.685 1.00 17.11 ? 2487 HOH B O   1 
HETATM 12950 O  O   . HOH EA 6 .   ? 10.818  60.161 33.421 1.00 16.30 ? 2488 HOH B O   1 
HETATM 12951 O  O   . HOH EA 6 .   ? -19.745 72.100 48.131 1.00 22.19 ? 2489 HOH B O   1 
HETATM 12952 O  O   . HOH EA 6 .   ? 0.896   56.377 29.302 1.00 24.56 ? 2490 HOH B O   1 
HETATM 12953 O  O   . HOH EA 6 .   ? 2.876   50.689 14.478 1.00 26.38 ? 2491 HOH B O   1 
HETATM 12954 O  O   . HOH EA 6 .   ? 9.641   45.804 50.370 1.00 27.26 ? 2492 HOH B O   1 
HETATM 12955 O  O   . HOH EA 6 .   ? -30.761 64.048 47.008 1.00 31.83 ? 2493 HOH B O   1 
HETATM 12956 O  O   . HOH EA 6 .   ? 12.178  47.898 27.924 1.00 24.60 ? 2494 HOH B O   1 
HETATM 12957 O  O   . HOH EA 6 .   ? 9.751   80.309 29.324 1.00 29.56 ? 2495 HOH B O   1 
HETATM 12958 O  O   . HOH EA 6 .   ? 11.241  46.997 34.924 1.00 19.40 ? 2496 HOH B O   1 
HETATM 12959 O  O   . HOH EA 6 .   ? -5.996  48.710 45.970 1.00 22.54 ? 2497 HOH B O   1 
HETATM 12960 O  O   . HOH EA 6 .   ? 23.233  63.888 47.177 1.00 33.59 ? 2498 HOH B O   1 
HETATM 12961 O  O   . HOH EA 6 .   ? 6.397   39.645 53.907 1.00 33.48 ? 2499 HOH B O   1 
HETATM 12962 O  O   . HOH EA 6 .   ? -12.929 73.663 -1.038 1.00 28.74 ? 2500 HOH B O   1 
HETATM 12963 O  O   . HOH EA 6 .   ? -0.912  56.502 32.466 1.00 33.02 ? 2501 HOH B O   1 
HETATM 12964 O  O   . HOH EA 6 .   ? 5.313   42.104 31.310 1.00 30.76 ? 2502 HOH B O   1 
HETATM 12965 O  O   . HOH EA 6 .   ? -8.509  65.019 51.452 1.00 20.22 ? 2503 HOH B O   1 
HETATM 12966 O  O   . HOH EA 6 .   ? 14.888  57.356 32.400 1.00 20.21 ? 2504 HOH B O   1 
HETATM 12967 O  O   . HOH EA 6 .   ? -23.275 66.472 48.324 1.00 29.18 ? 2505 HOH B O   1 
HETATM 12968 O  O   . HOH EA 6 .   ? -40.187 55.653 32.807 1.00 25.33 ? 2506 HOH B O   1 
HETATM 12969 O  O   . HOH EA 6 .   ? 3.030   84.253 25.255 1.00 30.85 ? 2507 HOH B O   1 
HETATM 12970 O  O   . HOH EA 6 .   ? -10.691 74.925 33.518 1.00 28.06 ? 2508 HOH B O   1 
HETATM 12971 O  O   . HOH EA 6 .   ? -8.682  80.582 6.075  1.00 27.31 ? 2509 HOH B O   1 
HETATM 12972 O  O   . HOH EA 6 .   ? -27.250 66.287 20.960 1.00 32.39 ? 2510 HOH B O   1 
HETATM 12973 O  O   . HOH EA 6 .   ? -3.876  42.179 39.054 1.00 29.60 ? 2511 HOH B O   1 
HETATM 12974 O  O   . HOH EA 6 .   ? 14.931  70.197 52.608 1.00 32.34 ? 2512 HOH B O   1 
HETATM 12975 O  O   . HOH EA 6 .   ? -19.437 58.644 36.921 1.00 27.85 ? 2513 HOH B O   1 
HETATM 12976 O  O   . HOH EA 6 .   ? 29.202  48.597 18.561 1.00 39.20 ? 2514 HOH B O   1 
HETATM 12977 O  O   . HOH EA 6 .   ? -6.811  66.981 -5.420 1.00 28.31 ? 2515 HOH B O   1 
HETATM 12978 O  O   . HOH EA 6 .   ? -1.108  49.918 6.894  1.00 31.91 ? 2516 HOH B O   1 
HETATM 12979 O  O   . HOH EA 6 .   ? 9.628   71.901 20.799 1.00 34.05 ? 2517 HOH B O   1 
HETATM 12980 O  O   . HOH EA 6 .   ? -33.195 65.397 45.967 1.00 34.32 ? 2518 HOH B O   1 
HETATM 12981 O  O   . HOH EA 6 .   ? 17.259  40.994 29.690 1.00 30.51 ? 2519 HOH B O   1 
HETATM 12982 O  O   . HOH EA 6 .   ? -2.024  49.817 39.734 1.00 22.45 ? 2520 HOH B O   1 
HETATM 12983 O  O   . HOH EA 6 .   ? 2.561   62.831 20.280 1.00 27.65 ? 2521 HOH B O   1 
HETATM 12984 O  O   . HOH EA 6 .   ? -17.489 65.370 15.153 1.00 25.13 ? 2522 HOH B O   1 
HETATM 12985 O  O   . HOH EA 6 .   ? -11.222 64.083 17.627 1.00 30.14 ? 2523 HOH B O   1 
HETATM 12986 O  O   . HOH EA 6 .   ? -6.174  54.879 15.145 1.00 21.62 ? 2524 HOH B O   1 
HETATM 12987 O  O   . HOH EA 6 .   ? -25.335 77.747 7.011  1.00 24.53 ? 2525 HOH B O   1 
HETATM 12988 O  O   . HOH EA 6 .   ? -24.654 56.408 24.866 1.00 26.09 ? 2526 HOH B O   1 
HETATM 12989 O  O   . HOH EA 6 .   ? -20.636 64.889 13.557 1.00 33.36 ? 2527 HOH B O   1 
HETATM 12990 O  O   . HOH EA 6 .   ? -3.331  61.619 -6.030 1.00 24.01 ? 2528 HOH B O   1 
HETATM 12991 O  O   . HOH EA 6 .   ? -6.825  54.678 26.478 1.00 45.14 ? 2529 HOH B O   1 
HETATM 12992 O  O   . HOH EA 6 .   ? -0.095  48.673 38.163 1.00 21.63 ? 2530 HOH B O   1 
HETATM 12993 O  O   . HOH EA 6 .   ? -16.359 42.134 56.838 1.00 28.13 ? 2531 HOH B O   1 
HETATM 12994 O  O   . HOH EA 6 .   ? -14.074 68.355 22.329 1.00 30.17 ? 2532 HOH B O   1 
HETATM 12995 O  O   . HOH EA 6 .   ? -10.592 52.263 50.670 1.00 21.86 ? 2533 HOH B O   1 
HETATM 12996 O  O   . HOH EA 6 .   ? 4.020   37.689 44.553 1.00 33.70 ? 2534 HOH B O   1 
HETATM 12997 O  O   . HOH EA 6 .   ? -21.859 87.000 25.819 1.00 30.37 ? 2535 HOH B O   1 
HETATM 12998 O  O   . HOH EA 6 .   ? -28.124 46.833 35.077 1.00 27.85 ? 2536 HOH B O   1 
HETATM 12999 O  O   . HOH EA 6 .   ? -9.836  58.825 23.984 1.00 31.43 ? 2537 HOH B O   1 
HETATM 13000 O  O   . HOH EA 6 .   ? -17.268 77.419 39.020 1.00 34.35 ? 2538 HOH B O   1 
HETATM 13001 O  O   . HOH EA 6 .   ? -10.470 34.964 58.317 1.00 35.52 ? 2539 HOH B O   1 
HETATM 13002 O  O   . HOH EA 6 .   ? -6.626  55.201 22.430 1.00 28.01 ? 2540 HOH B O   1 
HETATM 13003 O  O   . HOH EA 6 .   ? 17.365  53.143 19.894 1.00 44.39 ? 2541 HOH B O   1 
HETATM 13004 O  O   . HOH EA 6 .   ? -0.449  85.255 28.032 1.00 34.38 ? 2542 HOH B O   1 
HETATM 13005 O  O   . HOH EA 6 .   ? -8.396  32.080 47.417 1.00 35.00 ? 2543 HOH B O   1 
HETATM 13006 O  O   . HOH EA 6 .   ? -11.676 45.192 40.115 1.00 26.75 ? 2544 HOH B O   1 
HETATM 13007 O  O   . HOH EA 6 .   ? 5.916   72.959 9.035  1.00 28.43 ? 2545 HOH B O   1 
HETATM 13008 O  O   . HOH EA 6 .   ? 23.070  51.068 20.485 1.00 23.85 ? 2546 HOH B O   1 
HETATM 13009 O  O   . HOH EA 6 .   ? -12.017 75.606 53.777 1.00 33.18 ? 2547 HOH B O   1 
HETATM 13010 O  O   . HOH EA 6 .   ? -43.599 62.314 26.182 1.00 37.59 ? 2548 HOH B O   1 
HETATM 13011 O  O   . HOH EA 6 .   ? -4.076  82.540 12.790 1.00 36.74 ? 2549 HOH B O   1 
HETATM 13012 O  O   . HOH EA 6 .   ? -3.987  55.877 17.154 1.00 24.49 ? 2550 HOH B O   1 
HETATM 13013 O  O   . HOH EA 6 .   ? -13.552 72.619 -9.935 1.00 32.41 ? 2551 HOH B O   1 
HETATM 13014 O  O   . HOH EA 6 .   ? -4.290  67.945 -2.876 1.00 25.37 ? 2552 HOH B O   1 
HETATM 13015 O  O   . HOH EA 6 .   ? 18.320  46.154 20.397 1.00 30.30 ? 2553 HOH B O   1 
HETATM 13016 O  O   . HOH EA 6 .   ? -10.273 62.080 47.393 1.00 26.48 ? 2554 HOH B O   1 
HETATM 13017 O  O   . HOH EA 6 .   ? -29.639 40.851 23.399 1.00 24.48 ? 2555 HOH B O   1 
HETATM 13018 O  O   . HOH EA 6 .   ? -13.043 73.660 1.610  1.00 26.64 ? 2556 HOH B O   1 
HETATM 13019 O  O   . HOH EA 6 .   ? -0.787  42.818 15.057 1.00 29.23 ? 2557 HOH B O   1 
HETATM 13020 O  O   . HOH EA 6 .   ? -22.367 80.403 30.374 1.00 40.18 ? 2558 HOH B O   1 
HETATM 13021 O  O   . HOH EA 6 .   ? -19.455 79.096 27.339 1.00 30.39 ? 2559 HOH B O   1 
HETATM 13022 O  O   . HOH EA 6 .   ? -14.415 68.084 32.839 1.00 22.57 ? 2560 HOH B O   1 
HETATM 13023 O  O   . HOH EA 6 .   ? -1.270  73.016 7.429  1.00 31.79 ? 2561 HOH B O   1 
HETATM 13024 O  O   . HOH EA 6 .   ? -10.474 58.735 -2.456 1.00 21.90 ? 2562 HOH B O   1 
HETATM 13025 O  O   . HOH EA 6 .   ? -30.481 70.423 11.382 1.00 28.35 ? 2563 HOH B O   1 
HETATM 13026 O  O   . HOH EA 6 .   ? -21.479 69.087 51.286 1.00 22.98 ? 2564 HOH B O   1 
HETATM 13027 O  O   . HOH EA 6 .   ? -11.241 75.206 -2.024 1.00 36.92 ? 2565 HOH B O   1 
HETATM 13028 O  O   . HOH EA 6 .   ? -4.106  53.973 45.453 1.00 33.58 ? 2566 HOH B O   1 
HETATM 13029 O  O   . HOH EA 6 .   ? 16.049  47.694 21.066 1.00 33.77 ? 2567 HOH B O   1 
HETATM 13030 O  O   . HOH EA 6 .   ? 6.627   39.825 41.011 1.00 24.84 ? 2568 HOH B O   1 
HETATM 13031 O  O   . HOH EA 6 .   ? -5.981  84.699 26.310 1.00 28.47 ? 2569 HOH B O   1 
HETATM 13032 O  O   . HOH EA 6 .   ? -18.603 71.134 41.428 1.00 28.10 ? 2570 HOH B O   1 
HETATM 13033 O  O   . HOH EA 6 .   ? -21.524 56.592 35.615 1.00 21.10 ? 2571 HOH B O   1 
HETATM 13034 O  O   . HOH EA 6 .   ? -17.089 69.961 33.350 1.00 31.70 ? 2572 HOH B O   1 
HETATM 13035 O  O   . HOH EA 6 .   ? 19.147  59.143 32.143 1.00 29.63 ? 2573 HOH B O   1 
HETATM 13036 O  O   . HOH EA 6 .   ? -29.838 52.081 46.601 1.00 39.91 ? 2574 HOH B O   1 
HETATM 13037 O  O   . HOH EA 6 .   ? 25.889  50.501 19.105 1.00 35.00 ? 2575 HOH B O   1 
HETATM 13038 O  O   . HOH EA 6 .   ? -1.789  68.254 61.042 1.00 40.84 ? 2576 HOH B O   1 
HETATM 13039 O  O   . HOH EA 6 .   ? -13.440 63.027 27.605 1.00 40.20 ? 2577 HOH B O   1 
HETATM 13040 O  O   . HOH EA 6 .   ? -26.003 77.211 9.691  1.00 35.27 ? 2578 HOH B O   1 
HETATM 13041 O  O   . HOH EA 6 .   ? -19.046 65.841 -4.260 1.00 42.48 ? 2579 HOH B O   1 
HETATM 13042 O  O   . HOH EA 6 .   ? -4.584  84.222 30.392 1.00 24.41 ? 2580 HOH B O   1 
HETATM 13043 O  O   . HOH EA 6 .   ? -5.251  56.909 19.459 1.00 24.39 ? 2581 HOH B O   1 
HETATM 13044 O  O   . HOH EA 6 .   ? -21.091 51.459 36.167 1.00 27.95 ? 2582 HOH B O   1 
HETATM 13045 O  O   . HOH EA 6 .   ? -10.360 59.457 -7.025 1.00 36.13 ? 2583 HOH B O   1 
HETATM 13046 O  O   . HOH EA 6 .   ? -13.280 88.514 17.920 1.00 37.28 ? 2584 HOH B O   1 
HETATM 13047 O  O   . HOH EA 6 .   ? 3.655   60.577 60.970 1.00 25.05 ? 2585 HOH B O   1 
HETATM 13048 O  O   . HOH EA 6 .   ? -25.095 79.821 3.815  1.00 29.66 ? 2586 HOH B O   1 
HETATM 13049 O  O   . HOH EA 6 .   ? 4.890   58.522 13.203 1.00 35.09 ? 2587 HOH B O   1 
HETATM 13050 O  O   . HOH EA 6 .   ? 1.689   82.527 46.305 1.00 24.12 ? 2588 HOH B O   1 
HETATM 13051 O  O   . HOH EA 6 .   ? 5.669   64.310 19.217 1.00 29.70 ? 2589 HOH B O   1 
HETATM 13052 O  O   . HOH EA 6 .   ? -16.840 40.477 55.113 1.00 30.54 ? 2590 HOH B O   1 
HETATM 13053 O  O   . HOH EA 6 .   ? -9.840  50.904 15.601 1.00 43.54 ? 2591 HOH B O   1 
HETATM 13054 O  O   . HOH EA 6 .   ? -10.632 61.854 37.893 1.00 50.78 ? 2592 HOH B O   1 
HETATM 13055 O  O   . HOH EA 6 .   ? -12.872 83.205 11.633 1.00 39.85 ? 2593 HOH B O   1 
HETATM 13056 O  O   . HOH EA 6 .   ? -10.054 53.649 46.611 1.00 52.34 ? 2594 HOH B O   1 
HETATM 13057 O  O   . HOH EA 6 .   ? -21.355 58.589 48.812 1.00 20.29 ? 2595 HOH B O   1 
HETATM 13058 O  O   . HOH EA 6 .   ? 3.961   63.850 21.899 1.00 30.82 ? 2596 HOH B O   1 
HETATM 13059 O  O   . HOH EA 6 .   ? 16.724  59.475 31.970 1.00 35.48 ? 2597 HOH B O   1 
HETATM 13060 O  O   . HOH EA 6 .   ? -9.873  64.247 49.165 1.00 25.58 ? 2598 HOH B O   1 
HETATM 13061 O  O   . HOH EA 6 .   ? -16.364 67.376 28.356 1.00 21.78 ? 2599 HOH B O   1 
HETATM 13062 O  O   . HOH EA 6 .   ? -23.585 65.512 45.867 1.00 25.35 ? 2600 HOH B O   1 
HETATM 13063 O  O   . HOH EA 6 .   ? -22.906 56.770 31.003 1.00 24.47 ? 2601 HOH B O   1 
HETATM 13064 O  O   . HOH EA 6 .   ? -17.323 75.731 36.377 1.00 30.10 ? 2602 HOH B O   1 
HETATM 13065 O  O   . HOH EA 6 .   ? 0.118   78.299 15.809 1.00 27.18 ? 2603 HOH B O   1 
HETATM 13066 O  O   . HOH EA 6 .   ? -17.325 51.969 37.566 1.00 27.20 ? 2604 HOH B O   1 
HETATM 13067 O  O   . HOH EA 6 .   ? -17.071 48.762 14.941 1.00 27.80 ? 2605 HOH B O   1 
HETATM 13068 O  O   . HOH EA 6 .   ? 7.994   73.591 49.524 1.00 38.73 ? 2606 HOH B O   1 
HETATM 13069 O  O   . HOH EA 6 .   ? 14.684  70.868 28.003 1.00 27.58 ? 2607 HOH B O   1 
HETATM 13070 O  O   . HOH EA 6 .   ? 16.328  67.795 45.805 1.00 27.91 ? 2608 HOH B O   1 
HETATM 13071 O  O   . HOH EA 6 .   ? -8.036  60.082 31.255 1.00 37.48 ? 2609 HOH B O   1 
HETATM 13072 O  O   . HOH EA 6 .   ? -15.746 65.834 33.950 1.00 31.25 ? 2610 HOH B O   1 
HETATM 13073 O  O   . HOH EA 6 .   ? 2.629   62.269 59.433 1.00 26.20 ? 2611 HOH B O   1 
HETATM 13074 O  O   . HOH EA 6 .   ? -19.398 57.225 2.075  1.00 28.10 ? 2612 HOH B O   1 
HETATM 13075 O  O   . HOH EA 6 .   ? -42.241 51.852 34.098 1.00 30.32 ? 2613 HOH B O   1 
HETATM 13076 O  O   . HOH EA 6 .   ? -28.325 69.085 10.544 1.00 33.61 ? 2614 HOH B O   1 
HETATM 13077 O  O   . HOH EA 6 .   ? 6.571   63.362 59.655 1.00 29.52 ? 2615 HOH B O   1 
HETATM 13078 O  O   . HOH EA 6 .   ? -10.663 64.551 20.140 1.00 24.97 ? 2616 HOH B O   1 
HETATM 13079 O  O   . HOH EA 6 .   ? -14.027 55.350 13.071 1.00 30.88 ? 2617 HOH B O   1 
HETATM 13080 O  O   . HOH EA 6 .   ? 3.875   52.848 4.835  1.00 40.11 ? 2618 HOH B O   1 
HETATM 13081 O  O   . HOH EA 6 .   ? 17.083  69.162 28.469 1.00 40.57 ? 2619 HOH B O   1 
HETATM 13082 O  O   . HOH EA 6 .   ? -42.716 54.214 32.499 1.00 35.84 ? 2620 HOH B O   1 
HETATM 13083 O  O   . HOH EA 6 .   ? -2.288  42.352 4.378  1.00 37.93 ? 2621 HOH B O   1 
HETATM 13084 O  O   . HOH EA 6 .   ? -41.208 58.253 33.287 1.00 30.35 ? 2622 HOH B O   1 
HETATM 13085 O  O   . HOH EA 6 .   ? -19.077 49.599 46.879 1.00 31.33 ? 2623 HOH B O   1 
HETATM 13086 O  O   . HOH EA 6 .   ? -23.418 51.644 49.353 1.00 34.30 ? 2624 HOH B O   1 
HETATM 13087 O  O   . HOH EA 6 .   ? 20.242  47.003 18.771 1.00 33.84 ? 2625 HOH B O   1 
HETATM 13088 O  O   . HOH EA 6 .   ? -33.534 67.501 19.326 1.00 22.74 ? 2626 HOH B O   1 
HETATM 13089 O  O   . HOH EA 6 .   ? -20.514 71.858 50.693 1.00 30.98 ? 2627 HOH B O   1 
HETATM 13090 O  O   . HOH EA 6 .   ? -7.350  74.040 -5.980 1.00 36.22 ? 2628 HOH B O   1 
HETATM 13091 O  O   . HOH EA 6 .   ? -4.183  73.857 7.391  1.00 32.36 ? 2629 HOH B O   1 
HETATM 13092 O  O   . HOH EA 6 .   ? -10.317 62.520 -8.004 1.00 29.09 ? 2630 HOH B O   1 
HETATM 13093 O  O   . HOH EA 6 .   ? -12.908 62.661 39.417 1.00 25.47 ? 2631 HOH B O   1 
HETATM 13094 O  O   . HOH EA 6 .   ? -6.593  56.256 43.733 1.00 34.97 ? 2632 HOH B O   1 
HETATM 13095 O  O   . HOH EA 6 .   ? -18.966 71.676 34.397 1.00 31.21 ? 2633 HOH B O   1 
HETATM 13096 O  O   . HOH EA 6 .   ? 2.545   39.175 50.672 1.00 43.70 ? 2634 HOH B O   1 
HETATM 13097 O  O   . HOH EA 6 .   ? -24.952 33.643 33.608 1.00 41.95 ? 2635 HOH B O   1 
HETATM 13098 O  O   . HOH EA 6 .   ? -22.632 65.229 50.836 1.00 26.05 ? 2636 HOH B O   1 
HETATM 13099 O  O   . HOH EA 6 .   ? -4.924  52.457 43.254 1.00 46.53 ? 2637 HOH B O   1 
HETATM 13100 O  O   . HOH EA 6 .   ? 9.697   47.441 29.066 1.00 28.56 ? 2638 HOH B O   1 
HETATM 13101 O  O   . HOH EA 6 .   ? -17.096 47.069 38.952 1.00 33.14 ? 2639 HOH B O   1 
HETATM 13102 O  O   . HOH EA 6 .   ? 10.175  45.788 52.804 1.00 33.39 ? 2640 HOH B O   1 
HETATM 13103 O  O   . HOH EA 6 .   ? -22.039 66.107 29.506 1.00 28.71 ? 2641 HOH B O   1 
HETATM 13104 O  O   . HOH EA 6 .   ? -38.955 53.941 34.563 1.00 29.73 ? 2642 HOH B O   1 
HETATM 13105 O  O   . HOH EA 6 .   ? 7.266   52.570 28.884 1.00 30.09 ? 2643 HOH B O   1 
HETATM 13106 O  O   . HOH EA 6 .   ? -16.111 35.007 35.885 1.00 26.79 ? 2644 HOH B O   1 
HETATM 13107 O  O   . HOH EA 6 .   ? -18.003 44.080 34.836 1.00 36.54 ? 2645 HOH B O   1 
HETATM 13108 O  O   . HOH EA 6 .   ? -9.245  51.400 48.443 1.00 31.49 ? 2646 HOH B O   1 
HETATM 13109 O  O   . HOH EA 6 .   ? -28.322 68.777 14.790 1.00 25.77 ? 2647 HOH B O   1 
HETATM 13110 O  O   . HOH EA 6 .   ? -5.281  83.139 14.965 1.00 30.19 ? 2648 HOH B O   1 
HETATM 13111 O  O   . HOH EA 6 .   ? -34.338 69.218 39.597 1.00 35.99 ? 2649 HOH B O   1 
HETATM 13112 O  O   . HOH EA 6 .   ? -18.765 35.967 36.278 1.00 35.82 ? 2650 HOH B O   1 
HETATM 13113 O  O   . HOH EA 6 .   ? -8.983  38.101 41.498 1.00 35.94 ? 2651 HOH B O   1 
HETATM 13114 O  O   . HOH EA 6 .   ? -1.537  57.396 65.145 1.00 35.55 ? 2652 HOH B O   1 
HETATM 13115 O  O   . HOH EA 6 .   ? 23.143  56.951 25.034 1.00 25.43 ? 2653 HOH B O   1 
HETATM 13116 O  O   . HOH EA 6 .   ? -33.845 74.582 19.291 1.00 33.66 ? 2654 HOH B O   1 
HETATM 13117 O  O   . HOH EA 6 .   ? -17.161 77.603 27.060 1.00 28.68 ? 2655 HOH B O   1 
HETATM 13118 O  O   . HOH EA 6 .   ? -1.718  45.117 34.569 1.00 40.75 ? 2656 HOH B O   1 
HETATM 13119 O  O   . HOH EA 6 .   ? -2.667  52.354 39.298 1.00 41.40 ? 2657 HOH B O   1 
HETATM 13120 O  O   . HOH EA 6 .   ? -18.391 29.553 38.842 1.00 35.61 ? 2658 HOH B O   1 
HETATM 13121 O  O   . HOH EA 6 .   ? -18.750 46.703 47.213 1.00 33.21 ? 2659 HOH B O   1 
HETATM 13122 O  O   . HOH EA 6 .   ? -13.037 55.857 43.925 1.00 36.94 ? 2660 HOH B O   1 
HETATM 13123 O  O   . HOH EA 6 .   ? -10.989 43.362 38.453 1.00 31.76 ? 2661 HOH B O   1 
HETATM 13124 O  O   . HOH EA 6 .   ? -4.213  48.870 39.033 1.00 33.67 ? 2662 HOH B O   1 
HETATM 13125 O  O   . HOH EA 6 .   ? -18.698 73.730 32.179 1.00 39.18 ? 2663 HOH B O   1 
HETATM 13126 O  O   . HOH EA 6 .   ? -30.575 52.656 12.731 1.00 38.70 ? 2664 HOH B O   1 
HETATM 13127 O  O   . HOH EA 6 .   ? -2.004  51.058 -5.205 1.00 37.41 ? 2665 HOH B O   1 
HETATM 13128 O  O   . HOH EA 6 .   ? -22.736 68.741 53.568 1.00 34.47 ? 2666 HOH B O   1 
HETATM 13129 O  O   . HOH EA 6 .   ? -17.314 38.282 56.949 1.00 39.35 ? 2667 HOH B O   1 
HETATM 13130 O  O   . HOH EA 6 .   ? 3.675   52.617 27.586 1.00 41.50 ? 2668 HOH B O   1 
HETATM 13131 O  O   . HOH EA 6 .   ? -5.151  86.383 28.284 1.00 32.78 ? 2669 HOH B O   1 
HETATM 13132 O  O   . HOH EA 6 .   ? -7.130  58.945 20.492 1.00 35.05 ? 2670 HOH B O   1 
HETATM 13133 O  O   . HOH EA 6 .   ? -20.962 48.286 25.905 1.00 33.60 ? 2671 HOH B O   1 
HETATM 13134 O  O   . HOH EA 6 .   ? -3.409  57.052 -1.608 1.00 36.31 ? 2672 HOH B O   1 
HETATM 13135 O  O   . HOH EA 6 .   ? -10.981 61.925 35.267 1.00 39.65 ? 2673 HOH B O   1 
HETATM 13136 O  O   . HOH EA 6 .   ? -10.173 59.757 41.798 1.00 29.75 ? 2674 HOH B O   1 
HETATM 13137 O  O   . HOH EA 6 .   ? 19.895  57.555 58.787 1.00 30.29 ? 2675 HOH B O   1 
HETATM 13138 O  O   . HOH EA 6 .   ? -11.443 55.861 14.809 1.00 33.47 ? 2676 HOH B O   1 
HETATM 13139 O  O   . HOH EA 6 .   ? 17.452  41.710 23.882 1.00 44.10 ? 2677 HOH B O   1 
HETATM 13140 O  O   . HOH EA 6 .   ? -28.399 61.817 21.773 1.00 32.85 ? 2678 HOH B O   1 
HETATM 13141 O  O   . HOH EA 6 .   ? -41.097 66.612 26.100 1.00 28.06 ? 2679 HOH B O   1 
HETATM 13142 O  O   . HOH EA 6 .   ? -11.376 47.136 47.597 1.00 33.63 ? 2680 HOH B O   1 
HETATM 13143 O  O   . HOH EA 6 .   ? 12.991  69.699 56.047 1.00 37.76 ? 2681 HOH B O   1 
HETATM 13144 O  O   . HOH EA 6 .   ? -21.556 57.838 33.055 1.00 25.79 ? 2682 HOH B O   1 
HETATM 13145 O  O   . HOH EA 6 .   ? -7.921  60.549 -5.741 1.00 37.49 ? 2683 HOH B O   1 
HETATM 13146 O  O   . HOH EA 6 .   ? -6.241  70.338 0.292  1.00 33.08 ? 2684 HOH B O   1 
HETATM 13147 O  O   . HOH EA 6 .   ? 17.096  68.465 51.849 1.00 32.19 ? 2685 HOH B O   1 
HETATM 13148 O  O   . HOH EA 6 .   ? -5.246  50.105 48.658 1.00 27.97 ? 2686 HOH B O   1 
HETATM 13149 O  O   . HOH EA 6 .   ? -11.017 82.167 39.530 1.00 34.41 ? 2687 HOH B O   1 
HETATM 13150 O  O   . HOH EA 6 .   ? -31.034 76.842 39.686 1.00 35.73 ? 2688 HOH B O   1 
HETATM 13151 O  O   . HOH EA 6 .   ? 5.227   37.452 41.047 1.00 33.45 ? 2689 HOH B O   1 
HETATM 13152 O  O   . HOH EA 6 .   ? -34.417 68.023 21.909 1.00 27.31 ? 2690 HOH B O   1 
HETATM 13153 O  O   . HOH EA 6 .   ? 19.038  60.393 28.150 1.00 31.19 ? 2691 HOH B O   1 
HETATM 13154 O  O   . HOH EA 6 .   ? -36.155 72.205 26.934 1.00 38.56 ? 2692 HOH B O   1 
HETATM 13155 O  O   . HOH EA 6 .   ? -5.497  74.943 2.491  1.00 39.38 ? 2693 HOH B O   1 
HETATM 13156 O  O   . HOH EA 6 .   ? -24.782 54.756 19.912 1.00 32.29 ? 2694 HOH B O   1 
HETATM 13157 O  O   . HOH EA 6 .   ? 1.927   73.448 51.290 1.00 32.19 ? 2695 HOH B O   1 
HETATM 13158 O  O   . HOH EA 6 .   ? -6.545  68.130 -1.067 1.00 24.04 ? 2696 HOH B O   1 
HETATM 13159 O  O   . HOH EA 6 .   ? 4.432   47.086 63.862 1.00 39.08 ? 2697 HOH B O   1 
HETATM 13160 O  O   . HOH EA 6 .   ? -2.931  80.996 9.667  1.00 23.90 ? 2698 HOH B O   1 
HETATM 13161 O  O   . HOH EA 6 .   ? -17.754 57.980 -0.264 1.00 34.87 ? 2699 HOH B O   1 
HETATM 13162 O  O   . HOH EA 6 .   ? -23.129 54.437 23.728 1.00 42.64 ? 2700 HOH B O   1 
HETATM 13163 O  O   . HOH EA 6 .   ? -12.120 61.301 15.267 1.00 36.52 ? 2701 HOH B O   1 
HETATM 13164 O  O   . HOH EA 6 .   ? 7.949   55.127 62.070 1.00 33.96 ? 2702 HOH B O   1 
HETATM 13165 O  O   . HOH EA 6 .   ? 12.166  56.228 55.810 1.00 27.20 ? 2703 HOH B O   1 
HETATM 13166 O  O   . HOH EA 6 .   ? 21.769  38.173 28.847 1.00 28.41 ? 2704 HOH B O   1 
HETATM 13167 O  O   . HOH EA 6 .   ? 22.440  48.413 19.710 1.00 30.86 ? 2705 HOH B O   1 
HETATM 13168 O  O   . HOH EA 6 .   ? -22.955 82.159 13.733 1.00 27.48 ? 2706 HOH B O   1 
HETATM 13169 O  O   . HOH EA 6 .   ? -1.382  36.209 50.122 1.00 28.42 ? 2707 HOH B O   1 
HETATM 13170 O  O   . HOH EA 6 .   ? -8.818  54.431 15.084 1.00 33.58 ? 2708 HOH B O   1 
HETATM 13171 O  O   . HOH EA 6 .   ? -17.442 66.545 19.361 1.00 27.51 ? 2709 HOH B O   1 
HETATM 13172 O  O   . HOH EA 6 .   ? 21.791  53.207 19.539 1.00 33.64 ? 2710 HOH B O   1 
HETATM 13173 O  O   . HOH EA 6 .   ? -25.324 35.909 32.434 1.00 39.10 ? 2711 HOH B O   1 
HETATM 13174 O  O   . HOH EA 6 .   ? -10.623 49.578 46.980 1.00 37.19 ? 2712 HOH B O   1 
HETATM 13175 O  O   . HOH EA 6 .   ? 9.539   47.751 31.633 1.00 33.58 ? 2713 HOH B O   1 
HETATM 13176 O  O   . HOH EA 6 .   ? -16.081 68.645 30.997 1.00 37.12 ? 2714 HOH B O   1 
HETATM 13177 O  O   . HOH EA 6 .   ? 0.323   53.059 31.191 1.00 30.08 ? 2715 HOH B O   1 
HETATM 13178 O  O   . HOH EA 6 .   ? 0.802   68.257 61.527 1.00 39.58 ? 2716 HOH B O   1 
HETATM 13179 O  O   . HOH EA 6 .   ? -12.456 60.230 40.827 1.00 31.11 ? 2717 HOH B O   1 
HETATM 13180 O  O   . HOH EA 6 .   ? -1.469  80.631 16.503 1.00 29.06 ? 2718 HOH B O   1 
HETATM 13181 O  O   . HOH EA 6 .   ? -23.819 61.596 12.167 1.00 32.01 ? 2719 HOH B O   1 
HETATM 13182 O  O   . HOH EA 6 .   ? -19.491 62.776 62.357 1.00 40.37 ? 2720 HOH B O   1 
HETATM 13183 O  O   . HOH EA 6 .   ? -43.549 52.452 30.639 1.00 35.61 ? 2721 HOH B O   1 
HETATM 13184 O  O   . HOH EA 6 .   ? -18.889 60.478 -1.288 1.00 37.38 ? 2722 HOH B O   1 
HETATM 13185 O  O   . HOH EA 6 .   ? -32.709 79.308 35.877 1.00 35.62 ? 2723 HOH B O   1 
HETATM 13186 O  O   . HOH EA 6 .   ? -16.626 63.614 16.723 1.00 34.78 ? 2724 HOH B O   1 
HETATM 13187 O  O   . HOH EA 6 .   ? 6.855   80.934 29.917 1.00 38.97 ? 2725 HOH B O   1 
HETATM 13188 O  O   . HOH EA 6 .   ? 12.103  49.144 23.077 1.00 33.41 ? 2726 HOH B O   1 
HETATM 13189 O  O   . HOH EA 6 .   ? -14.555 77.002 48.088 1.00 35.98 ? 2727 HOH B O   1 
HETATM 13190 O  O   . HOH EA 6 .   ? -5.202  79.376 35.564 1.00 25.58 ? 2728 HOH B O   1 
HETATM 13191 O  O   . HOH EA 6 .   ? 10.892  75.387 47.991 1.00 38.12 ? 2729 HOH B O   1 
HETATM 13192 O  O   . HOH EA 6 .   ? -33.271 68.184 45.132 1.00 39.98 ? 2730 HOH B O   1 
HETATM 13193 O  O   . HOH EA 6 .   ? -9.172  73.042 31.240 1.00 35.13 ? 2731 HOH B O   1 
HETATM 13194 O  O   . HOH EA 6 .   ? 14.640  73.610 28.821 1.00 41.70 ? 2732 HOH B O   1 
HETATM 13195 O  O   . HOH EA 6 .   ? 21.879  58.290 60.328 1.00 35.32 ? 2733 HOH B O   1 
HETATM 13196 O  O   . HOH EA 6 .   ? -11.211 60.022 19.133 1.00 35.61 ? 2734 HOH B O   1 
HETATM 13197 O  O   . HOH EA 6 .   ? -22.052 60.452 32.985 1.00 36.06 ? 2735 HOH B O   1 
HETATM 13198 O  O   . HOH EA 6 .   ? -15.508 31.929 56.953 1.00 31.30 ? 2736 HOH B O   1 
HETATM 13199 O  O   . HOH EA 6 .   ? -39.384 51.291 34.015 1.00 40.23 ? 2737 HOH B O   1 
HETATM 13200 O  O   . HOH EA 6 .   ? 4.751   67.600 6.275  1.00 26.70 ? 2738 HOH B O   1 
HETATM 13201 O  O   . HOH EA 6 .   ? -14.483 64.043 -9.782 1.00 33.84 ? 2739 HOH B O   1 
HETATM 13202 O  O   . HOH EA 6 .   ? -24.763 37.003 40.186 1.00 34.55 ? 2740 HOH B O   1 
HETATM 13203 O  O   . HOH EA 6 .   ? 8.663   37.724 47.157 1.00 30.72 ? 2741 HOH B O   1 
HETATM 13204 O  O   . HOH EA 6 .   ? -5.492  55.642 31.743 1.00 34.91 ? 2742 HOH B O   1 
HETATM 13205 O  O   . HOH EA 6 .   ? -35.394 51.399 47.910 1.00 37.37 ? 2743 HOH B O   1 
HETATM 13206 O  O   . HOH EA 6 .   ? -45.967 63.180 27.178 1.00 37.05 ? 2744 HOH B O   1 
HETATM 13207 O  O   . HOH EA 6 .   ? -31.953 42.166 13.468 1.00 43.29 ? 2745 HOH B O   1 
HETATM 13208 O  O   . HOH EA 6 .   ? -38.921 46.635 33.518 1.00 34.48 ? 2746 HOH B O   1 
HETATM 13209 O  O   . HOH EA 6 .   ? -4.306  88.131 39.326 1.00 37.88 ? 2747 HOH B O   1 
HETATM 13210 O  O   . HOH EA 6 .   ? -17.673 63.150 -1.501 1.00 38.24 ? 2748 HOH B O   1 
HETATM 13211 O  O   . HOH EA 6 .   ? -32.131 65.180 19.357 1.00 40.81 ? 2749 HOH B O   1 
HETATM 13212 O  O   . HOH EA 6 .   ? -24.010 54.857 52.893 1.00 38.05 ? 2750 HOH B O   1 
HETATM 13213 O  O   . HOH EA 6 .   ? -28.994 38.487 24.339 1.00 33.58 ? 2751 HOH B O   1 
HETATM 13214 O  O   . HOH EA 6 .   ? 6.020   65.214 2.737  1.00 41.87 ? 2752 HOH B O   1 
HETATM 13215 O  O   . HOH EA 6 .   ? 24.060  63.431 56.075 1.00 30.73 ? 2753 HOH B O   1 
HETATM 13216 O  O   . HOH EA 6 .   ? -17.776 41.479 26.555 1.00 38.79 ? 2754 HOH B O   1 
HETATM 13217 O  O   . HOH EA 6 .   ? -0.918  75.906 15.078 1.00 28.67 ? 2755 HOH B O   1 
HETATM 13218 O  O   . HOH EA 6 .   ? 6.203   36.262 44.188 1.00 42.45 ? 2756 HOH B O   1 
HETATM 13219 O  O   . HOH EA 6 .   ? 2.571   43.177 29.949 1.00 35.65 ? 2757 HOH B O   1 
HETATM 13220 O  O   . HOH EA 6 .   ? 5.137   61.384 16.165 1.00 39.04 ? 2758 HOH B O   1 
HETATM 13221 O  O   . HOH EA 6 .   ? -33.765 66.675 38.025 1.00 28.14 ? 2759 HOH B O   1 
HETATM 13222 O  O   . HOH EA 6 .   ? -18.004 85.588 17.380 1.00 35.05 ? 2760 HOH B O   1 
HETATM 13223 O  O   . HOH EA 6 .   ? 11.246  63.001 19.656 1.00 37.45 ? 2761 HOH B O   1 
HETATM 13224 O  O   . HOH EA 6 .   ? -27.229 37.513 39.494 1.00 41.88 ? 2762 HOH B O   1 
HETATM 13225 O  O   . HOH EA 6 .   ? -27.551 75.089 10.529 1.00 33.03 ? 2763 HOH B O   1 
HETATM 13226 O  O   . HOH EA 6 .   ? -26.963 55.721 44.460 1.00 36.37 ? 2764 HOH B O   1 
HETATM 13227 O  O   . HOH EA 6 .   ? -33.451 60.663 46.877 1.00 31.40 ? 2765 HOH B O   1 
HETATM 13228 O  O   . HOH EA 6 .   ? 2.136   86.297 36.310 1.00 37.35 ? 2766 HOH B O   1 
HETATM 13229 O  O   . HOH EA 6 .   ? -18.156 67.015 33.607 1.00 37.23 ? 2767 HOH B O   1 
HETATM 13230 O  O   . HOH EA 6 .   ? -37.569 51.263 22.443 1.00 40.73 ? 2768 HOH B O   1 
HETATM 13231 O  O   . HOH EA 6 .   ? -21.012 74.544 46.444 1.00 37.24 ? 2769 HOH B O   1 
HETATM 13232 O  O   . HOH EA 6 .   ? -20.974 34.625 34.848 1.00 35.91 ? 2770 HOH B O   1 
HETATM 13233 O  O   . HOH EA 6 .   ? -5.629  46.600 39.519 1.00 38.56 ? 2771 HOH B O   1 
HETATM 13234 O  O   . HOH EA 6 .   ? -34.858 70.803 16.975 1.00 41.00 ? 2772 HOH B O   1 
HETATM 13235 O  O   . HOH EA 6 .   ? -35.848 69.373 37.352 1.00 42.35 ? 2773 HOH B O   1 
HETATM 13236 O  O   . HOH EA 6 .   ? -15.892 88.725 25.880 1.00 34.71 ? 2774 HOH B O   1 
HETATM 13237 O  O   . HOH EA 6 .   ? -36.499 46.903 43.631 1.00 45.80 ? 2775 HOH B O   1 
HETATM 13238 O  O   . HOH EA 6 .   ? 10.913  47.871 25.138 1.00 42.82 ? 2776 HOH B O   1 
HETATM 13239 O  O   . HOH EA 6 .   ? -46.605 66.464 31.171 1.00 37.43 ? 2777 HOH B O   1 
HETATM 13240 O  O   . HOH FA 6 .   ? 73.490  76.437 16.937 1.00 49.59 ? 246  HOH M O   1 
HETATM 13241 O  O   . HOH FA 6 .   ? 75.772  77.451 17.444 1.00 42.59 ? 485  HOH M O   1 
HETATM 13242 O  O   . HOH GA 6 .   ? 38.243  59.785 13.387 1.00 46.60 ? 760  HOH O O   1 
HETATM 13243 O  O   . HOH HA 6 .   ? -31.532 39.926 9.460  1.00 43.90 ? 524  HOH Q O   1 
HETATM 13244 O  O   . HOH IA 6 .   ? -24.313 74.638 2.163  1.00 39.22 ? 466  HOH R O   1 
HETATM 13245 O  O   . HOH IA 6 .   ? -21.996 68.917 -0.545 1.00 34.87 ? 529  HOH R O   1 
HETATM 13246 O  O   . HOH JA 6 .   ? -0.032  77.505 10.796 1.00 34.57 ? 193  HOH S O   1 
HETATM 13247 O  O   . HOH JA 6 .   ? 6.597   74.961 10.801 1.00 35.77 ? 769  HOH S O   1 
HETATM 13248 O  O   . HOH JA 6 .   ? 4.159   78.884 18.139 1.00 42.91 ? 898  HOH S O   1 
HETATM 13249 O  O   . HOH KA 6 .   ? 3.931   73.391 0.818  1.00 37.67 ? 37   HOH T O   1 
HETATM 13250 O  O   . HOH KA 6 .   ? 3.284   74.258 3.050  1.00 44.79 ? 483  HOH T O   1 
HETATM 13251 O  O   . HOH KA 6 .   ? 5.091   70.548 -0.070 1.00 26.95 ? 692  HOH T O   1 
HETATM 13252 O  O   . HOH KA 6 .   ? -0.871  72.790 4.655  1.00 22.21 ? 2778 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   1522 1522 NA  NA  A . 
G  4 474 1   1521 1521 474 474 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  4 474 1   2322 2322 474 474 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 M . 
Q  2 NAG 2   1220 1220 NAG NAG M . 
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 . 
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 2461 2461 HOH HOH B . 
EA 6 HOH 140 2462 2462 HOH HOH B . 
EA 6 HOH 141 2463 2463 HOH HOH B . 
EA 6 HOH 142 2464 2464 HOH HOH B . 
EA 6 HOH 143 2465 2465 HOH HOH B . 
EA 6 HOH 144 2466 2466 HOH HOH B . 
EA 6 HOH 145 2467 2467 HOH HOH B . 
EA 6 HOH 146 2468 2468 HOH HOH B . 
EA 6 HOH 147 2469 2469 HOH HOH B . 
EA 6 HOH 148 2470 2470 HOH HOH B . 
EA 6 HOH 149 2471 2471 HOH HOH B . 
EA 6 HOH 150 2472 2472 HOH HOH B . 
EA 6 HOH 151 2473 2473 HOH HOH B . 
EA 6 HOH 152 2474 2474 HOH HOH B . 
EA 6 HOH 153 2475 2475 HOH HOH B . 
EA 6 HOH 154 2476 2476 HOH HOH B . 
EA 6 HOH 155 2477 2477 HOH HOH B . 
EA 6 HOH 156 2478 2478 HOH HOH B . 
EA 6 HOH 157 2479 2479 HOH HOH B . 
EA 6 HOH 158 2480 2480 HOH HOH B . 
EA 6 HOH 159 2481 2481 HOH HOH B . 
EA 6 HOH 160 2482 2482 HOH HOH B . 
EA 6 HOH 161 2483 2483 HOH HOH B . 
EA 6 HOH 162 2484 2484 HOH HOH B . 
EA 6 HOH 163 2485 2485 HOH HOH B . 
EA 6 HOH 164 2486 2486 HOH HOH B . 
EA 6 HOH 165 2487 2487 HOH HOH B . 
EA 6 HOH 166 2488 2488 HOH HOH B . 
EA 6 HOH 167 2489 2489 HOH HOH B . 
EA 6 HOH 168 2490 2490 HOH HOH B . 
EA 6 HOH 169 2491 2491 HOH HOH B . 
EA 6 HOH 170 2492 2492 HOH HOH B . 
EA 6 HOH 171 2493 2493 HOH HOH B . 
EA 6 HOH 172 2494 2494 HOH HOH B . 
EA 6 HOH 173 2495 2495 HOH HOH B . 
EA 6 HOH 174 2496 2496 HOH HOH B . 
EA 6 HOH 175 2497 2497 HOH HOH B . 
EA 6 HOH 176 2498 2498 HOH HOH B . 
EA 6 HOH 177 2499 2499 HOH HOH B . 
EA 6 HOH 178 2500 2500 HOH HOH B . 
EA 6 HOH 179 2501 2501 HOH HOH B . 
EA 6 HOH 180 2502 2502 HOH HOH B . 
EA 6 HOH 181 2503 2503 HOH HOH B . 
EA 6 HOH 182 2504 2504 HOH HOH B . 
EA 6 HOH 183 2505 2505 HOH HOH B . 
EA 6 HOH 184 2506 2506 HOH HOH B . 
EA 6 HOH 185 2507 2507 HOH HOH B . 
EA 6 HOH 186 2508 2508 HOH HOH B . 
EA 6 HOH 187 2509 2509 HOH HOH B . 
EA 6 HOH 188 2510 2510 HOH HOH B . 
EA 6 HOH 189 2511 2511 HOH HOH B . 
EA 6 HOH 190 2512 2512 HOH HOH B . 
EA 6 HOH 191 2513 2513 HOH HOH B . 
EA 6 HOH 192 2514 2514 HOH HOH B . 
EA 6 HOH 193 2515 2515 HOH HOH B . 
EA 6 HOH 194 2516 2516 HOH HOH B . 
EA 6 HOH 195 2517 2517 HOH HOH B . 
EA 6 HOH 196 2518 2518 HOH HOH B . 
EA 6 HOH 197 2519 2519 HOH HOH B . 
EA 6 HOH 198 2520 2520 HOH HOH B . 
EA 6 HOH 199 2521 2521 HOH HOH B . 
EA 6 HOH 200 2522 2522 HOH HOH B . 
EA 6 HOH 201 2523 2523 HOH HOH B . 
EA 6 HOH 202 2524 2524 HOH HOH B . 
EA 6 HOH 203 2525 2525 HOH HOH B . 
EA 6 HOH 204 2526 2526 HOH HOH B . 
EA 6 HOH 205 2527 2527 HOH HOH B . 
EA 6 HOH 206 2528 2528 HOH HOH B . 
EA 6 HOH 207 2529 2529 HOH HOH B . 
EA 6 HOH 208 2530 2530 HOH HOH B . 
EA 6 HOH 209 2531 2531 HOH HOH B . 
EA 6 HOH 210 2532 2532 HOH HOH B . 
EA 6 HOH 211 2533 2533 HOH HOH B . 
EA 6 HOH 212 2534 2534 HOH HOH B . 
EA 6 HOH 213 2535 2535 HOH HOH B . 
EA 6 HOH 214 2536 2536 HOH HOH B . 
EA 6 HOH 215 2537 2537 HOH HOH B . 
EA 6 HOH 216 2538 2538 HOH HOH B . 
EA 6 HOH 217 2539 2539 HOH HOH B . 
EA 6 HOH 218 2540 2540 HOH HOH B . 
EA 6 HOH 219 2541 2541 HOH HOH B . 
EA 6 HOH 220 2542 2542 HOH HOH B . 
EA 6 HOH 221 2543 2543 HOH HOH B . 
EA 6 HOH 222 2544 2544 HOH HOH B . 
EA 6 HOH 223 2545 2545 HOH HOH B . 
EA 6 HOH 224 2546 2546 HOH HOH B . 
EA 6 HOH 225 2547 2547 HOH HOH B . 
EA 6 HOH 226 2548 2548 HOH HOH B . 
EA 6 HOH 227 2549 2549 HOH HOH B . 
EA 6 HOH 228 2550 2550 HOH HOH B . 
EA 6 HOH 229 2551 2551 HOH HOH B . 
EA 6 HOH 230 2552 2552 HOH HOH B . 
EA 6 HOH 231 2553 2553 HOH HOH B . 
EA 6 HOH 232 2554 2554 HOH HOH B . 
EA 6 HOH 233 2555 2555 HOH HOH B . 
EA 6 HOH 234 2556 2556 HOH HOH B . 
EA 6 HOH 235 2557 2557 HOH HOH B . 
EA 6 HOH 236 2558 2558 HOH HOH B . 
EA 6 HOH 237 2559 2559 HOH HOH B . 
EA 6 HOH 238 2560 2560 HOH HOH B . 
EA 6 HOH 239 2561 2561 HOH HOH B . 
EA 6 HOH 240 2562 2562 HOH HOH B . 
EA 6 HOH 241 2563 2563 HOH HOH B . 
EA 6 HOH 242 2564 2564 HOH HOH B . 
EA 6 HOH 243 2565 2565 HOH HOH B . 
EA 6 HOH 244 2566 2566 HOH HOH B . 
EA 6 HOH 245 2567 2567 HOH HOH B . 
EA 6 HOH 246 2568 2568 HOH HOH B . 
EA 6 HOH 247 2569 2569 HOH HOH B . 
EA 6 HOH 248 2570 2570 HOH HOH B . 
EA 6 HOH 249 2571 2571 HOH HOH B . 
EA 6 HOH 250 2572 2572 HOH HOH B . 
EA 6 HOH 251 2573 2573 HOH HOH B . 
EA 6 HOH 252 2574 2574 HOH HOH B . 
EA 6 HOH 253 2575 2575 HOH HOH B . 
EA 6 HOH 254 2576 2576 HOH HOH B . 
EA 6 HOH 255 2577 2577 HOH HOH B . 
EA 6 HOH 256 2578 2578 HOH HOH B . 
EA 6 HOH 257 2579 2579 HOH HOH B . 
EA 6 HOH 258 2580 2580 HOH HOH B . 
EA 6 HOH 259 2581 2581 HOH HOH B . 
EA 6 HOH 260 2582 2582 HOH HOH B . 
EA 6 HOH 261 2583 2583 HOH HOH B . 
EA 6 HOH 262 2584 2584 HOH HOH B . 
EA 6 HOH 263 2585 2585 HOH HOH B . 
EA 6 HOH 264 2586 2586 HOH HOH B . 
EA 6 HOH 265 2587 2587 HOH HOH B . 
EA 6 HOH 266 2588 2588 HOH HOH B . 
EA 6 HOH 267 2589 2589 HOH HOH B . 
EA 6 HOH 268 2590 2590 HOH HOH B . 
EA 6 HOH 269 2591 2591 HOH HOH B . 
EA 6 HOH 270 2592 2592 HOH HOH B . 
EA 6 HOH 271 2593 2593 HOH HOH B . 
EA 6 HOH 272 2594 2594 HOH HOH B . 
EA 6 HOH 273 2595 2595 HOH HOH B . 
EA 6 HOH 274 2596 2596 HOH HOH B . 
EA 6 HOH 275 2597 2597 HOH HOH B . 
EA 6 HOH 276 2598 2598 HOH HOH B . 
EA 6 HOH 277 2599 2599 HOH HOH B . 
EA 6 HOH 278 2600 2600 HOH HOH B . 
EA 6 HOH 279 2601 2601 HOH HOH B . 
EA 6 HOH 280 2602 2602 HOH HOH B . 
EA 6 HOH 281 2603 2603 HOH HOH B . 
EA 6 HOH 282 2604 2604 HOH HOH B . 
EA 6 HOH 283 2605 2605 HOH HOH B . 
EA 6 HOH 284 2606 2606 HOH HOH B . 
EA 6 HOH 285 2607 2607 HOH HOH B . 
EA 6 HOH 286 2608 2608 HOH HOH B . 
EA 6 HOH 287 2609 2609 HOH HOH B . 
EA 6 HOH 288 2610 2610 HOH HOH B . 
EA 6 HOH 289 2611 2611 HOH HOH B . 
EA 6 HOH 290 2612 2612 HOH HOH B . 
EA 6 HOH 291 2613 2613 HOH HOH B . 
EA 6 HOH 292 2614 2614 HOH HOH B . 
EA 6 HOH 293 2615 2615 HOH HOH B . 
EA 6 HOH 294 2616 2616 HOH HOH B . 
EA 6 HOH 295 2617 2617 HOH HOH B . 
EA 6 HOH 296 2618 2618 HOH HOH B . 
EA 6 HOH 297 2619 2619 HOH HOH B . 
EA 6 HOH 298 2620 2620 HOH HOH B . 
EA 6 HOH 299 2621 2621 HOH HOH B . 
EA 6 HOH 300 2622 2622 HOH HOH B . 
EA 6 HOH 301 2623 2623 HOH HOH B . 
EA 6 HOH 302 2624 2624 HOH HOH B . 
EA 6 HOH 303 2625 2625 HOH HOH B . 
EA 6 HOH 304 2626 2626 HOH HOH B . 
EA 6 HOH 305 2627 2627 HOH HOH B . 
EA 6 HOH 306 2628 2628 HOH HOH B . 
EA 6 HOH 307 2629 2629 HOH HOH B . 
EA 6 HOH 308 2630 2630 HOH HOH B . 
EA 6 HOH 309 2631 2631 HOH HOH B . 
EA 6 HOH 310 2632 2632 HOH HOH B . 
EA 6 HOH 311 2633 2633 HOH HOH B . 
EA 6 HOH 312 2634 2634 HOH HOH B . 
EA 6 HOH 313 2635 2635 HOH HOH B . 
EA 6 HOH 314 2636 2636 HOH HOH B . 
EA 6 HOH 315 2637 2637 HOH HOH B . 
EA 6 HOH 316 2638 2638 HOH HOH B . 
EA 6 HOH 317 2639 2639 HOH HOH B . 
EA 6 HOH 318 2640 2640 HOH HOH B . 
EA 6 HOH 319 2641 2641 HOH HOH B . 
EA 6 HOH 320 2642 2642 HOH HOH B . 
EA 6 HOH 321 2643 2643 HOH HOH B . 
EA 6 HOH 322 2644 2644 HOH HOH B . 
EA 6 HOH 323 2645 2645 HOH HOH B . 
EA 6 HOH 324 2646 2646 HOH HOH B . 
EA 6 HOH 325 2647 2647 HOH HOH B . 
EA 6 HOH 326 2648 2648 HOH HOH B . 
EA 6 HOH 327 2649 2649 HOH HOH B . 
EA 6 HOH 328 2650 2650 HOH HOH B . 
EA 6 HOH 329 2651 2651 HOH HOH B . 
EA 6 HOH 330 2652 2652 HOH HOH B . 
EA 6 HOH 331 2653 2653 HOH HOH B . 
EA 6 HOH 332 2654 2654 HOH HOH B . 
EA 6 HOH 333 2655 2655 HOH HOH B . 
EA 6 HOH 334 2656 2656 HOH HOH B . 
EA 6 HOH 335 2657 2657 HOH HOH B . 
EA 6 HOH 336 2658 2658 HOH HOH B . 
EA 6 HOH 337 2659 2659 HOH HOH B . 
EA 6 HOH 338 2660 2660 HOH HOH B . 
EA 6 HOH 339 2661 2661 HOH HOH B . 
EA 6 HOH 340 2662 2662 HOH HOH B . 
EA 6 HOH 341 2663 2663 HOH HOH B . 
EA 6 HOH 342 2664 2664 HOH HOH B . 
EA 6 HOH 343 2665 2665 HOH HOH B . 
EA 6 HOH 344 2666 2666 HOH HOH B . 
EA 6 HOH 345 2667 2667 HOH HOH B . 
EA 6 HOH 346 2668 2668 HOH HOH B . 
EA 6 HOH 347 2669 2669 HOH HOH B . 
EA 6 HOH 348 2670 2670 HOH HOH B . 
EA 6 HOH 349 2671 2671 HOH HOH B . 
EA 6 HOH 350 2672 2672 HOH HOH B . 
EA 6 HOH 351 2673 2673 HOH HOH B . 
EA 6 HOH 352 2674 2674 HOH HOH B . 
EA 6 HOH 353 2675 2675 HOH HOH B . 
EA 6 HOH 354 2676 2676 HOH HOH B . 
EA 6 HOH 355 2677 2677 HOH HOH B . 
EA 6 HOH 356 2678 2678 HOH HOH B . 
EA 6 HOH 357 2679 2679 HOH HOH B . 
EA 6 HOH 358 2680 2680 HOH HOH B . 
EA 6 HOH 359 2681 2681 HOH HOH B . 
EA 6 HOH 360 2682 2682 HOH HOH B . 
EA 6 HOH 361 2683 2683 HOH HOH B . 
EA 6 HOH 362 2684 2684 HOH HOH B . 
EA 6 HOH 363 2685 2685 HOH HOH B . 
EA 6 HOH 364 2686 2686 HOH HOH B . 
EA 6 HOH 365 2687 2687 HOH HOH B . 
EA 6 HOH 366 2688 2688 HOH HOH B . 
EA 6 HOH 367 2689 2689 HOH HOH B . 
EA 6 HOH 368 2690 2690 HOH HOH B . 
EA 6 HOH 369 2691 2691 HOH HOH B . 
EA 6 HOH 370 2692 2692 HOH HOH B . 
EA 6 HOH 371 2693 2693 HOH HOH B . 
EA 6 HOH 372 2694 2694 HOH HOH B . 
EA 6 HOH 373 2695 2695 HOH HOH B . 
EA 6 HOH 374 2696 2696 HOH HOH B . 
EA 6 HOH 375 2697 2697 HOH HOH B . 
EA 6 HOH 376 2698 2698 HOH HOH B . 
EA 6 HOH 377 2699 2699 HOH HOH B . 
EA 6 HOH 378 2700 2700 HOH HOH B . 
EA 6 HOH 379 2701 2701 HOH HOH B . 
EA 6 HOH 380 2702 2702 HOH HOH B . 
EA 6 HOH 381 2703 2703 HOH HOH B . 
EA 6 HOH 382 2704 2704 HOH HOH B . 
EA 6 HOH 383 2705 2705 HOH HOH B . 
EA 6 HOH 384 2706 2706 HOH HOH B . 
EA 6 HOH 385 2707 2707 HOH HOH B . 
EA 6 HOH 386 2708 2708 HOH HOH B . 
EA 6 HOH 387 2709 2709 HOH HOH B . 
EA 6 HOH 388 2710 2710 HOH HOH B . 
EA 6 HOH 389 2711 2711 HOH HOH B . 
EA 6 HOH 390 2712 2712 HOH HOH B . 
EA 6 HOH 391 2713 2713 HOH HOH B . 
EA 6 HOH 392 2714 2714 HOH HOH B . 
EA 6 HOH 393 2715 2715 HOH HOH B . 
EA 6 HOH 394 2716 2716 HOH HOH B . 
EA 6 HOH 395 2717 2717 HOH HOH B . 
EA 6 HOH 396 2718 2718 HOH HOH B . 
EA 6 HOH 397 2719 2719 HOH HOH B . 
EA 6 HOH 398 2720 2720 HOH HOH B . 
EA 6 HOH 399 2721 2721 HOH HOH B . 
EA 6 HOH 400 2722 2722 HOH HOH B . 
EA 6 HOH 401 2723 2723 HOH HOH B . 
EA 6 HOH 402 2724 2724 HOH HOH B . 
EA 6 HOH 403 2725 2725 HOH HOH B . 
EA 6 HOH 404 2726 2726 HOH HOH B . 
EA 6 HOH 405 2727 2727 HOH HOH B . 
EA 6 HOH 406 2728 2728 HOH HOH B . 
EA 6 HOH 407 2729 2729 HOH HOH B . 
EA 6 HOH 408 2730 2730 HOH HOH B . 
EA 6 HOH 409 2731 2731 HOH HOH B . 
EA 6 HOH 410 2732 2732 HOH HOH B . 
EA 6 HOH 411 2733 2733 HOH HOH B . 
EA 6 HOH 412 2734 2734 HOH HOH B . 
EA 6 HOH 413 2735 2735 HOH HOH B . 
EA 6 HOH 414 2736 2736 HOH HOH B . 
EA 6 HOH 415 2737 2737 HOH HOH B . 
EA 6 HOH 416 2738 2738 HOH HOH B . 
EA 6 HOH 417 2739 2739 HOH HOH B . 
EA 6 HOH 418 2740 2740 HOH HOH B . 
EA 6 HOH 419 2741 2741 HOH HOH B . 
EA 6 HOH 420 2742 2742 HOH HOH B . 
EA 6 HOH 421 2743 2743 HOH HOH B . 
EA 6 HOH 422 2744 2744 HOH HOH B . 
EA 6 HOH 423 2745 2745 HOH HOH B . 
EA 6 HOH 424 2746 2746 HOH HOH B . 
EA 6 HOH 425 2747 2747 HOH HOH B . 
EA 6 HOH 426 2748 2748 HOH HOH B . 
EA 6 HOH 427 2749 2749 HOH HOH B . 
EA 6 HOH 428 2750 2750 HOH HOH B . 
EA 6 HOH 429 2751 2751 HOH HOH B . 
EA 6 HOH 430 2752 2752 HOH HOH B . 
EA 6 HOH 431 2753 2753 HOH HOH B . 
EA 6 HOH 432 2754 2754 HOH HOH B . 
EA 6 HOH 433 2755 2755 HOH HOH B . 
EA 6 HOH 434 2756 2756 HOH HOH B . 
EA 6 HOH 435 2757 2757 HOH HOH B . 
EA 6 HOH 436 2758 2758 HOH HOH B . 
EA 6 HOH 437 2759 2759 HOH HOH B . 
EA 6 HOH 438 2760 2760 HOH HOH B . 
EA 6 HOH 439 2761 2761 HOH HOH B . 
EA 6 HOH 440 2762 2762 HOH HOH B . 
EA 6 HOH 441 2763 2763 HOH HOH B . 
EA 6 HOH 442 2764 2764 HOH HOH B . 
EA 6 HOH 443 2765 2765 HOH HOH B . 
EA 6 HOH 444 2766 2766 HOH HOH B . 
EA 6 HOH 445 2767 2767 HOH HOH B . 
EA 6 HOH 446 2768 2768 HOH HOH B . 
EA 6 HOH 447 2769 2769 HOH HOH B . 
EA 6 HOH 448 2770 2770 HOH HOH B . 
EA 6 HOH 449 2771 2771 HOH HOH B . 
EA 6 HOH 450 2772 2772 HOH HOH B . 
EA 6 HOH 451 2773 2773 HOH HOH B . 
EA 6 HOH 452 2774 2774 HOH HOH B . 
EA 6 HOH 453 2775 2775 HOH HOH B . 
EA 6 HOH 454 2776 2776 HOH HOH B . 
EA 6 HOH 455 2777 2777 HOH HOH B . 
FA 6 HOH 1   246  246  HOH HOH M . 
FA 6 HOH 2   485  485  HOH HOH M . 
GA 6 HOH 1   760  760  HOH HOH O . 
HA 6 HOH 1   524  524  HOH HOH Q . 
IA 6 HOH 1   466  466  HOH HOH R . 
IA 6 HOH 2   529  529  HOH HOH R . 
JA 6 HOH 1   193  193  HOH HOH S . 
JA 6 HOH 2   769  769  HOH HOH S . 
JA 6 HOH 3   898  898  HOH HOH S . 
KA 6 HOH 1   37   37   HOH HOH T . 
KA 6 HOH 2   483  483  HOH HOH T . 
KA 6 HOH 3   692  692  HOH HOH T . 
KA 6 HOH 4   2778 2778 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   decameric 
_pdbx_struct_assembly.oligomeric_count     10 
# 
_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 
# 
_pdbx_struct_assembly_prop.biol_id   1 
_pdbx_struct_assembly_prop.type      'ABSA (A^2)' 
_pdbx_struct_assembly_prop.value     10820 
_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     1522 
_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                 86.7 
_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 
3 'Structure model' 1 2 2017-10-25 
# 
_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' 
3 3 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
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 
DENZO       .     ?              package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data reduction'  
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 1 
SCALEPACK   .     ?              package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data scaling'    
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 2 
CNS         .     ?              package 'Axel T. Brunger'    axel.brunger@yale.edu    refinement        
http://cns.csb.yale.edu/v1.1/                    Fortran_77 ? 3 
PDB_EXTRACT 3.000 'July 2, 2007' package PDB                  sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/                 C++        ? 4 
HKL-2000    .     ?              ?       ?                    ?                        'data reduction'  ? ?          ? 5 
HKL-2000    .     ?              ?       ?                    ?                        'data scaling'    ? ?          ? 6 
CNX         .     ?              ?       ?                    ?                        phasing           ? ?          ? 7 
CNX         .     ?              ?       ?                    ?                        refinement        ? ?          ? 8 
# 
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  ? ? -150.68 78.65   
2  1 SER A 64  ? ? -162.07 -164.60 
3  1 ASN A 74  ? ? 71.38   -5.89   
4  1 GLN A 123 ? ? -111.62 -99.28  
5  1 TRP A 124 ? ? -93.36  -145.99 
6  1 ARG A 140 ? ? 36.05   50.55   
7  1 HIS A 162 ? ? -148.97 31.12   
8  1 GLU A 191 ? ? -38.48  130.60  
9  1 ASP A 192 ? ? 56.26   12.51   
10 1 ILE A 193 ? ? -130.38 -58.94  
11 1 SER A 242 ? ? 63.64   -163.94 
12 1 GLN A 320 ? ? -70.36  39.16   
13 1 LYS A 423 ? ? 53.84   19.86   
14 1 ASN A 450 ? ? -172.23 75.13   
15 1 GLU A 521 ? ? 66.35   -2.56   
16 1 LYS A 536 ? ? -58.05  -3.76   
17 1 TYR A 547 ? ? -127.56 -71.08  
18 1 ARG A 597 ? ? -142.53 47.95   
19 1 THR A 600 ? ? -122.02 -91.59  
20 1 SER A 630 ? ? 64.98   -125.84 
21 1 ASP A 678 ? ? -116.20 -88.59  
22 1 ASN A 710 ? ? -91.77  -71.64  
23 1 ASP A 739 ? ? -96.68  -156.88 
24 1 ILE A 742 ? ? 37.38   46.15   
25 1 SER B 64  ? ? -163.73 -168.29 
26 1 HIS B 66  ? ? -149.05 14.18   
27 1 GLN B 123 ? ? -119.14 -99.78  
28 1 TRP B 124 ? ? -95.12  -146.11 
29 1 HIS B 162 ? ? -152.41 35.99   
30 1 ILE B 193 ? ? -122.24 -63.94  
31 1 SER B 242 ? ? 59.82   -165.89 
32 1 GLN B 320 ? ? -66.13  43.11   
33 1 LYS B 423 ? ? 53.57   17.28   
34 1 ASP B 438 ? ? -155.16 88.83   
35 1 ASN B 450 ? ? -159.39 75.18   
36 1 ARG B 492 ? ? 169.51  168.86  
37 1 TYR B 547 ? ? -131.68 -73.79  
38 1 THR B 600 ? ? -122.06 -91.52  
39 1 SER B 630 ? ? 66.61   -122.13 
40 1 ASP B 678 ? ? -122.57 -96.95  
41 1 ASN B 710 ? ? -92.42  -74.70  
42 1 ASP B 739 ? ? -101.86 -159.01 
43 1 ILE B 742 ? ? 36.08   48.87   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    TYR 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     700 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.078 
_pdbx_validate_planes.type            '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-(3,3-DIFLUOROPYRROLIDIN-1-YL)-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-6-YLCYCLOHEXYL)BUTANAMIDE
;
474 
5 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 
6 water HOH 
# 
