data_3HII
# 
_entry.id   3HII 
# 
_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   3HII         
RCSB  RCSB053175   
WWPDB D_1000053175 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3HI7 'The crystal structure of human diamine oxidase'                                   unspecified 
PDB 3HIG 'Crystal structure of human diamine oxidase in complex with the inhibitor berenil' unspecified 
# 
_pdbx_database_status.entry_id                        3HII 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2009-05-20 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'McGrath, A.P.' 1 
'Guss, J.M.'    2 
# 
_citation.id                        primary 
_citation.title                     'Structure and inhibition of human diamine oxidase' 
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            48 
_citation.page_first                9810 
_citation.page_last                 9822 
_citation.year                      2009 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   19764817 
_citation.pdbx_database_id_DOI      10.1021/bi9014192 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'McGrath, A.P.' 1 
primary 'Hilmer, K.M.'  2 
primary 'Collyer, C.A.' 3 
primary 'Shepard, E.M.' 4 
primary 'Elmore, B.O.'  5 
primary 'Brown, D.E.'   6 
primary 'Dooley, D.M.'  7 
primary 'Guss, J.M.'    8 
# 
_cell.entry_id           3HII 
_cell.length_a           92.455 
_cell.length_b           94.690 
_cell.length_c           196.279 
_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                         3HII 
_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 'Amiloride-sensitive amine oxidase' 83463.797 2   1.4.3.22 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'                   63.546    2   ?        ? ? ? 
3 non-polymer syn 'CALCIUM ION'                       40.078    4   ?        ? ? ? 
4 non-polymer syn GLYCEROL                            92.094    1   ?        ? ? ? 
5 non-polymer syn '1,5-BIS(4-AMIDINOPHENOXY)PENTANE'  340.419   2   ?        ? ? ? 
6 non-polymer man N-ACETYL-D-GLUCOSAMINE              221.208   12  ?        ? ? ? 
7 non-polymer man BETA-D-MANNOSE                      180.156   1   ?        ? ? ? 
8 water       nat water                               18.015    916 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Diamine oxidase, DAO, Amiloride-binding protein, ABP, Histaminase, Kidney amine oxidase, KAO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;RSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSSTTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAV
IFFGDQEHPNVTEFAVGPLPGPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNGKFYGSPEELARKYADGEVDV
VVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGPRLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVH
FGGERIAYEVSVQEAVALYGGHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYN(TPQ)DYIWDFIFYPNGVMEAKMHATGYVHATFYTPEGLR
HGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENITNPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKY
LLFTSPQENPWGHKRSYRLQIHSMADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWDPPVVFEQFLHN
NENIENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRDNGPNYVQRWIPEDRDC
SMPPPFSYNGTYRPV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSSTTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAV
IFFGDQEHPNVTEFAVGPLPGPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNGKFYGSPEELARKYADGEVDV
VVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGPRLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVH
FGGERIAYEVSVQEAVALYGGHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMHATGYVHATFYTPEGLRHGTR
LHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENITNPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFT
SPQENPWGHKRSYRLQIHSMADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWDPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRDNGPNYVQRWIPEDRDCSMPP
PFSYNGTYRPV
;
_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   ARG n 
1 2   SER n 
1 3   PRO n 
1 4   GLY n 
1 5   THR n 
1 6   LEU n 
1 7   PRO n 
1 8   ARG n 
1 9   LYS n 
1 10  ALA n 
1 11  GLY n 
1 12  VAL n 
1 13  PHE n 
1 14  SER n 
1 15  ASP n 
1 16  LEU n 
1 17  SER n 
1 18  ASN n 
1 19  GLN n 
1 20  GLU n 
1 21  LEU n 
1 22  LYS n 
1 23  ALA n 
1 24  VAL n 
1 25  HIS n 
1 26  SER n 
1 27  PHE n 
1 28  LEU n 
1 29  TRP n 
1 30  SER n 
1 31  LYS n 
1 32  LYS n 
1 33  GLU n 
1 34  LEU n 
1 35  ARG n 
1 36  LEU n 
1 37  GLN n 
1 38  PRO n 
1 39  SER n 
1 40  SER n 
1 41  THR n 
1 42  THR n 
1 43  THR n 
1 44  MET n 
1 45  ALA n 
1 46  LYS n 
1 47  ASN n 
1 48  THR n 
1 49  VAL n 
1 50  PHE n 
1 51  LEU n 
1 52  ILE n 
1 53  GLU n 
1 54  MET n 
1 55  LEU n 
1 56  LEU n 
1 57  PRO n 
1 58  LYS n 
1 59  LYS n 
1 60  TYR n 
1 61  HIS n 
1 62  VAL n 
1 63  LEU n 
1 64  ARG n 
1 65  PHE n 
1 66  LEU n 
1 67  ASP n 
1 68  LYS n 
1 69  GLY n 
1 70  GLU n 
1 71  ARG n 
1 72  HIS n 
1 73  PRO n 
1 74  VAL n 
1 75  ARG n 
1 76  GLU n 
1 77  ALA n 
1 78  ARG n 
1 79  ALA n 
1 80  VAL n 
1 81  ILE n 
1 82  PHE n 
1 83  PHE n 
1 84  GLY n 
1 85  ASP n 
1 86  GLN n 
1 87  GLU n 
1 88  HIS n 
1 89  PRO n 
1 90  ASN n 
1 91  VAL n 
1 92  THR n 
1 93  GLU n 
1 94  PHE n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  LEU n 
1 100 PRO n 
1 101 GLY n 
1 102 PRO n 
1 103 CYS n 
1 104 TYR n 
1 105 MET n 
1 106 ARG n 
1 107 ALA n 
1 108 LEU n 
1 109 SER n 
1 110 PRO n 
1 111 ARG n 
1 112 PRO n 
1 113 GLY n 
1 114 TYR n 
1 115 GLN n 
1 116 SER n 
1 117 SER n 
1 118 TRP n 
1 119 ALA n 
1 120 SER n 
1 121 ARG n 
1 122 PRO n 
1 123 ILE n 
1 124 SER n 
1 125 THR n 
1 126 ALA n 
1 127 GLU n 
1 128 TYR n 
1 129 ALA n 
1 130 LEU n 
1 131 LEU n 
1 132 TYR n 
1 133 HIS n 
1 134 THR n 
1 135 LEU n 
1 136 GLN n 
1 137 GLU n 
1 138 ALA n 
1 139 THR n 
1 140 LYS n 
1 141 PRO n 
1 142 LEU n 
1 143 HIS n 
1 144 GLN n 
1 145 PHE n 
1 146 PHE n 
1 147 LEU n 
1 148 ASN n 
1 149 THR n 
1 150 THR n 
1 151 GLY n 
1 152 PHE n 
1 153 SER n 
1 154 PHE n 
1 155 GLN n 
1 156 ASP n 
1 157 CYS n 
1 158 HIS n 
1 159 ASP n 
1 160 ARG n 
1 161 CYS n 
1 162 LEU n 
1 163 ALA n 
1 164 PHE n 
1 165 THR n 
1 166 ASP n 
1 167 VAL n 
1 168 ALA n 
1 169 PRO n 
1 170 ARG n 
1 171 GLY n 
1 172 VAL n 
1 173 ALA n 
1 174 SER n 
1 175 GLY n 
1 176 GLN n 
1 177 ARG n 
1 178 ARG n 
1 179 SER n 
1 180 TRP n 
1 181 LEU n 
1 182 ILE n 
1 183 ILE n 
1 184 GLN n 
1 185 ARG n 
1 186 TYR n 
1 187 VAL n 
1 188 GLU n 
1 189 GLY n 
1 190 TYR n 
1 191 PHE n 
1 192 LEU n 
1 193 HIS n 
1 194 PRO n 
1 195 THR n 
1 196 GLY n 
1 197 LEU n 
1 198 GLU n 
1 199 LEU n 
1 200 LEU n 
1 201 VAL n 
1 202 ASP n 
1 203 HIS n 
1 204 GLY n 
1 205 SER n 
1 206 THR n 
1 207 ASP n 
1 208 ALA n 
1 209 GLY n 
1 210 HIS n 
1 211 TRP n 
1 212 ALA n 
1 213 VAL n 
1 214 GLU n 
1 215 GLN n 
1 216 VAL n 
1 217 TRP n 
1 218 TYR n 
1 219 ASN n 
1 220 GLY n 
1 221 LYS n 
1 222 PHE n 
1 223 TYR n 
1 224 GLY n 
1 225 SER n 
1 226 PRO n 
1 227 GLU n 
1 228 GLU n 
1 229 LEU n 
1 230 ALA n 
1 231 ARG n 
1 232 LYS n 
1 233 TYR n 
1 234 ALA n 
1 235 ASP n 
1 236 GLY n 
1 237 GLU n 
1 238 VAL n 
1 239 ASP n 
1 240 VAL n 
1 241 VAL n 
1 242 VAL n 
1 243 LEU n 
1 244 GLU n 
1 245 ASP n 
1 246 PRO n 
1 247 LEU n 
1 248 PRO n 
1 249 GLY n 
1 250 GLY n 
1 251 LYS n 
1 252 GLY n 
1 253 HIS n 
1 254 ASP n 
1 255 SER n 
1 256 THR n 
1 257 GLU n 
1 258 GLU n 
1 259 PRO n 
1 260 PRO n 
1 261 LEU n 
1 262 PHE n 
1 263 SER n 
1 264 SER n 
1 265 HIS n 
1 266 LYS n 
1 267 PRO n 
1 268 ARG n 
1 269 GLY n 
1 270 ASP n 
1 271 PHE n 
1 272 PRO n 
1 273 SER n 
1 274 PRO n 
1 275 ILE n 
1 276 HIS n 
1 277 VAL n 
1 278 SER n 
1 279 GLY n 
1 280 PRO n 
1 281 ARG n 
1 282 LEU n 
1 283 VAL n 
1 284 GLN n 
1 285 PRO n 
1 286 HIS n 
1 287 GLY n 
1 288 PRO n 
1 289 ARG n 
1 290 PHE n 
1 291 ARG n 
1 292 LEU n 
1 293 GLU n 
1 294 GLY n 
1 295 ASN n 
1 296 ALA n 
1 297 VAL n 
1 298 LEU n 
1 299 TYR n 
1 300 GLY n 
1 301 GLY n 
1 302 TRP n 
1 303 SER n 
1 304 PHE n 
1 305 ALA n 
1 306 PHE n 
1 307 ARG n 
1 308 LEU n 
1 309 ARG n 
1 310 SER n 
1 311 SER n 
1 312 SER n 
1 313 GLY n 
1 314 LEU n 
1 315 GLN n 
1 316 VAL n 
1 317 LEU n 
1 318 ASN n 
1 319 VAL n 
1 320 HIS n 
1 321 PHE n 
1 322 GLY n 
1 323 GLY n 
1 324 GLU n 
1 325 ARG n 
1 326 ILE n 
1 327 ALA n 
1 328 TYR n 
1 329 GLU n 
1 330 VAL n 
1 331 SER n 
1 332 VAL n 
1 333 GLN n 
1 334 GLU n 
1 335 ALA n 
1 336 VAL n 
1 337 ALA n 
1 338 LEU n 
1 339 TYR n 
1 340 GLY n 
1 341 GLY n 
1 342 HIS n 
1 343 THR n 
1 344 PRO n 
1 345 ALA n 
1 346 GLY n 
1 347 MET n 
1 348 GLN n 
1 349 THR n 
1 350 LYS n 
1 351 TYR n 
1 352 LEU n 
1 353 ASP n 
1 354 VAL n 
1 355 GLY n 
1 356 TRP n 
1 357 GLY n 
1 358 LEU n 
1 359 GLY n 
1 360 SER n 
1 361 VAL n 
1 362 THR n 
1 363 HIS n 
1 364 GLU n 
1 365 LEU n 
1 366 ALA n 
1 367 PRO n 
1 368 GLY n 
1 369 ILE n 
1 370 ASP n 
1 371 CYS n 
1 372 PRO n 
1 373 GLU n 
1 374 THR n 
1 375 ALA n 
1 376 THR n 
1 377 PHE n 
1 378 LEU n 
1 379 ASP n 
1 380 THR n 
1 381 PHE n 
1 382 HIS n 
1 383 TYR n 
1 384 TYR n 
1 385 ASP n 
1 386 ALA n 
1 387 ASP n 
1 388 ASP n 
1 389 PRO n 
1 390 VAL n 
1 391 HIS n 
1 392 TYR n 
1 393 PRO n 
1 394 ARG n 
1 395 ALA n 
1 396 LEU n 
1 397 CYS n 
1 398 LEU n 
1 399 PHE n 
1 400 GLU n 
1 401 MET n 
1 402 PRO n 
1 403 THR n 
1 404 GLY n 
1 405 VAL n 
1 406 PRO n 
1 407 LEU n 
1 408 ARG n 
1 409 ARG n 
1 410 HIS n 
1 411 PHE n 
1 412 ASN n 
1 413 SER n 
1 414 ASN n 
1 415 PHE n 
1 416 LYS n 
1 417 GLY n 
1 418 GLY n 
1 419 PHE n 
1 420 ASN n 
1 421 PHE n 
1 422 TYR n 
1 423 ALA n 
1 424 GLY n 
1 425 LEU n 
1 426 LYS n 
1 427 GLY n 
1 428 GLN n 
1 429 VAL n 
1 430 LEU n 
1 431 VAL n 
1 432 LEU n 
1 433 ARG n 
1 434 THR n 
1 435 THR n 
1 436 SER n 
1 437 THR n 
1 438 VAL n 
1 439 TYR n 
1 440 ASN n 
1 441 TPQ n 
1 442 ASP n 
1 443 TYR n 
1 444 ILE n 
1 445 TRP n 
1 446 ASP n 
1 447 PHE n 
1 448 ILE n 
1 449 PHE n 
1 450 TYR n 
1 451 PRO n 
1 452 ASN n 
1 453 GLY n 
1 454 VAL n 
1 455 MET n 
1 456 GLU n 
1 457 ALA n 
1 458 LYS n 
1 459 MET n 
1 460 HIS n 
1 461 ALA n 
1 462 THR n 
1 463 GLY n 
1 464 TYR n 
1 465 VAL n 
1 466 HIS n 
1 467 ALA n 
1 468 THR n 
1 469 PHE n 
1 470 TYR n 
1 471 THR n 
1 472 PRO n 
1 473 GLU n 
1 474 GLY n 
1 475 LEU n 
1 476 ARG n 
1 477 HIS n 
1 478 GLY n 
1 479 THR n 
1 480 ARG n 
1 481 LEU n 
1 482 HIS n 
1 483 THR n 
1 484 HIS n 
1 485 LEU n 
1 486 ILE n 
1 487 GLY n 
1 488 ASN n 
1 489 ILE n 
1 490 HIS n 
1 491 THR n 
1 492 HIS n 
1 493 LEU n 
1 494 VAL n 
1 495 HIS n 
1 496 TYR n 
1 497 ARG n 
1 498 VAL n 
1 499 ASP n 
1 500 LEU n 
1 501 ASP n 
1 502 VAL n 
1 503 ALA n 
1 504 GLY n 
1 505 THR n 
1 506 LYS n 
1 507 ASN n 
1 508 SER n 
1 509 PHE n 
1 510 GLN n 
1 511 THR n 
1 512 LEU n 
1 513 GLN n 
1 514 MET n 
1 515 LYS n 
1 516 LEU n 
1 517 GLU n 
1 518 ASN n 
1 519 ILE n 
1 520 THR n 
1 521 ASN n 
1 522 PRO n 
1 523 TRP n 
1 524 SER n 
1 525 PRO n 
1 526 ARG n 
1 527 HIS n 
1 528 ARG n 
1 529 VAL n 
1 530 VAL n 
1 531 GLN n 
1 532 PRO n 
1 533 THR n 
1 534 LEU n 
1 535 GLU n 
1 536 GLN n 
1 537 THR n 
1 538 GLN n 
1 539 TYR n 
1 540 SER n 
1 541 TRP n 
1 542 GLU n 
1 543 ARG n 
1 544 GLN n 
1 545 ALA n 
1 546 ALA n 
1 547 PHE n 
1 548 ARG n 
1 549 PHE n 
1 550 LYS n 
1 551 ARG n 
1 552 LYS n 
1 553 LEU n 
1 554 PRO n 
1 555 LYS n 
1 556 TYR n 
1 557 LEU n 
1 558 LEU n 
1 559 PHE n 
1 560 THR n 
1 561 SER n 
1 562 PRO n 
1 563 GLN n 
1 564 GLU n 
1 565 ASN n 
1 566 PRO n 
1 567 TRP n 
1 568 GLY n 
1 569 HIS n 
1 570 LYS n 
1 571 ARG n 
1 572 SER n 
1 573 TYR n 
1 574 ARG n 
1 575 LEU n 
1 576 GLN n 
1 577 ILE n 
1 578 HIS n 
1 579 SER n 
1 580 MET n 
1 581 ALA n 
1 582 ASP n 
1 583 GLN n 
1 584 VAL n 
1 585 LEU n 
1 586 PRO n 
1 587 PRO n 
1 588 GLY n 
1 589 TRP n 
1 590 GLN n 
1 591 GLU n 
1 592 GLU n 
1 593 GLN n 
1 594 ALA n 
1 595 ILE n 
1 596 THR n 
1 597 TRP n 
1 598 ALA n 
1 599 ARG n 
1 600 TYR n 
1 601 PRO n 
1 602 LEU n 
1 603 ALA n 
1 604 VAL n 
1 605 THR n 
1 606 LYS n 
1 607 TYR n 
1 608 ARG n 
1 609 GLU n 
1 610 SER n 
1 611 GLU n 
1 612 LEU n 
1 613 CYS n 
1 614 SER n 
1 615 SER n 
1 616 SER n 
1 617 ILE n 
1 618 TYR n 
1 619 HIS n 
1 620 GLN n 
1 621 ASN n 
1 622 ASP n 
1 623 PRO n 
1 624 TRP n 
1 625 ASP n 
1 626 PRO n 
1 627 PRO n 
1 628 VAL n 
1 629 VAL n 
1 630 PHE n 
1 631 GLU n 
1 632 GLN n 
1 633 PHE n 
1 634 LEU n 
1 635 HIS n 
1 636 ASN n 
1 637 ASN n 
1 638 GLU n 
1 639 ASN n 
1 640 ILE n 
1 641 GLU n 
1 642 ASN n 
1 643 GLU n 
1 644 ASP n 
1 645 LEU n 
1 646 VAL n 
1 647 ALA n 
1 648 TRP n 
1 649 VAL n 
1 650 THR n 
1 651 VAL n 
1 652 GLY n 
1 653 PHE n 
1 654 LEU n 
1 655 HIS n 
1 656 ILE n 
1 657 PRO n 
1 658 HIS n 
1 659 SER n 
1 660 GLU n 
1 661 ASP n 
1 662 ILE n 
1 663 PRO n 
1 664 ASN n 
1 665 THR n 
1 666 ALA n 
1 667 THR n 
1 668 PRO n 
1 669 GLY n 
1 670 ASN n 
1 671 SER n 
1 672 VAL n 
1 673 GLY n 
1 674 PHE n 
1 675 LEU n 
1 676 LEU n 
1 677 ARG n 
1 678 PRO n 
1 679 PHE n 
1 680 ASN n 
1 681 PHE n 
1 682 PHE n 
1 683 PRO n 
1 684 GLU n 
1 685 ASP n 
1 686 PRO n 
1 687 SER n 
1 688 LEU n 
1 689 ALA n 
1 690 SER n 
1 691 ARG n 
1 692 ASP n 
1 693 THR n 
1 694 VAL n 
1 695 ILE n 
1 696 VAL n 
1 697 TRP n 
1 698 PRO n 
1 699 ARG n 
1 700 ASP n 
1 701 ASN n 
1 702 GLY n 
1 703 PRO n 
1 704 ASN n 
1 705 TYR n 
1 706 VAL n 
1 707 GLN n 
1 708 ARG n 
1 709 TRP n 
1 710 ILE n 
1 711 PRO n 
1 712 GLU n 
1 713 ASP n 
1 714 ARG n 
1 715 ASP n 
1 716 CYS n 
1 717 SER n 
1 718 MET n 
1 719 PRO n 
1 720 PRO n 
1 721 PRO n 
1 722 PHE n 
1 723 SER n 
1 724 TYR n 
1 725 ASN n 
1 726 GLY n 
1 727 THR n 
1 728 TYR n 
1 729 ARG n 
1 730 PRO n 
1 731 VAL 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                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ABP1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7227 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            'Schneider 2' 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ABP1_HUMAN 
_struct_ref.pdbx_db_accession          P19801 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSSTTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAV
IFFGDQEHPNVTEFAVGPLPGPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNGKFYGSPEELARKYADGEVDV
VVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGPRLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVH
FGGERIAYEVSVQEAVALYGGHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMHATGYVHATFYTPEGLRHGTR
LHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENITNPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFT
SPQENPWGHKRSYRLQIHSMADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWDPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRDNGPNYVQRWIPEDRDCSMPP
PFSYNGTYRPV
;
_struct_ref.pdbx_align_begin           21 
_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 3HII A 1 ? 731 ? P19801 21 ? 751 ? 21 751 
2 1 3HII B 1 ? 731 ? P19801 21 ? 751 ? 21 751 
# 
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 3HII ARG A 1 ? UNP P19801 PRO 21 ENGINEERED 21 1 
2 3HII ARG B 1 ? UNP P19801 PRO 21 ENGINEERED 21 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 
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 
BMA D-saccharide        . BETA-D-MANNOSE                                          ? 'C6 H12 O6'      180.156 
CA  non-polymer         . 'CALCIUM ION'                                           ? 'Ca 2'           40.078  
CU  non-polymer         . 'COPPER (II) ION'                                       ? 'Cu 2'           63.546  
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  
GOL non-polymer         . GLYCEROL                                                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       
92.094  
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                                  ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                                           ? 'C9 H11 N O2'    165.189 
PNT non-polymer         . '1,5-BIS(4-AMIDINOPHENOXY)PENTANE'                      ? 'C19 H24 N4 O2'  340.419 
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 
TPQ 'L-peptide linking' n '5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE' 
'5-(2-CARBOXY-2-AMINOETHYL)-4-HYDROXY-1,2-BENZOQUINONE; 2,4,5-TRIHYDROXYPHENYLALANINE QUINONE; TOPA QUINONE' 'C9 H9 N O5'     
211.171 
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          3HII 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.431 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.58 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   52.24 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_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              7.5 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    
'0.1M bis-tris propane, 20%(w/v) PEG 3350, 0.2M sodium sulfate, pH 7.5, vapor diffusion, hanging drop, temperature 298K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.pdbx_collection_date   2008-11-05 
_diffrn_detector.details                'OSMIC MIRRORS' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Ni FILTER' 
_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   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU200' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
# 
_reflns.entry_id                     3HII 
_reflns.d_resolution_high            2.149 
_reflns.d_resolution_low             50.000 
_reflns.number_obs                   89751 
_reflns.pdbx_Rmerge_I_obs            0.103 
_reflns.pdbx_netI_over_sigmaI        9.903 
_reflns.pdbx_chi_squared             1.067 
_reflns.pdbx_redundancy              3.000 
_reflns.percent_possible_obs         95.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.number_all                   89751 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        29.96 
_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_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.149 
_reflns_shell.d_res_low              2.23 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.336 
_reflns_shell.meanI_over_sigI_obs    2.7 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_chi_squared       1.041 
_reflns_shell.pdbx_redundancy        2.40 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      8090 
_reflns_shell.percent_possible_all   87.10 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3HII 
_refine.ls_d_res_high                            2.149 
_refine.ls_d_res_low                             25.840 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    94.980 
_refine.ls_number_reflns_obs                     85093 
_refine.ls_number_reflns_all                     85093 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18359 
_refine.ls_R_factor_R_work                       0.18159 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.22093 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  4554 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               21.017 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            1.200 
_refine.aniso_B[2][2]                            -0.940 
_refine.aniso_B[3][3]                            -0.270 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_refine.overall_SU_R_Cruickshank_DPI             0.245 
_refine.overall_SU_R_free                        0.190 
_refine.pdbx_overall_ESU_R                       0.245 
_refine.pdbx_overall_ESU_R_Free                  0.190 
_refine.overall_SU_ML                            0.118 
_refine.overall_SU_B                             4.494 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HI7' 
_refine.pdbx_method_to_determine_struct          'BY REFINEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.866 
_refine.B_iso_max                                62.23 
_refine.B_iso_min                                11.86 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.30 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11354 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         241 
_refine_hist.number_atoms_solvent             916 
_refine_hist.number_atoms_total               12511 
_refine_hist.d_res_high                       2.149 
_refine_hist.d_res_low                        25.840 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.021  ? 12215 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.020  ? 8166  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.199  1.957  ? 16761 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.784  3.000  ? 19717 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.521  5.000  ? 1482  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.900 22.920 ? 572   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.793 15.000 ? 1721  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       13.985 15.000 ? 76    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.070  0.200  ? 1780  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.005  0.021  ? 13734 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 2697  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.431  1.500  ? 7254  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.081  1.500  ? 2876  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.808  2.000  ? 11775 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.191  3.000  ? 4961  'X-RAY DIFFRACTION' ? 
r_scangle_it                 1.932  4.500  ? 4963  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       2.149 
_refine_ls_shell.d_res_low                        2.204 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               84.910 
_refine_ls_shell.number_reflns_R_work             5522 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.232 
_refine_ls_shell.R_factor_R_free                  0.301 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             290 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                5812 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3HII 
_struct.title                     'Crystal structure of human diamine oxidase in complex with the inhibitor pentamidine' 
_struct.pdbx_descriptor           'Amiloride-sensitive amine oxidase (E.C.1.4.3.22)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3HII 
_struct_keywords.text            
;oxidoreductase, copper amine oxidase, topaquinone, TPQ, diamine oxidase, DAO, human, pentamidine, Glycoprotein, Heparin-binding, Metal-binding, Secreted
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
J N N 7 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 5 ? 
S N N 6 ? 
T N N 6 ? 
U N N 6 ? 
V N N 6 ? 
W N N 6 ? 
X N N 6 ? 
Y N N 8 ? 
Z N N 8 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  ARG A 8   ? SER A 14  ? ARG A 28  SER A 34  5 ? 7  
HELX_P HELX_P2  2  SER A 17  ? LYS A 31  ? SER A 37  LYS A 51  1 ? 15 
HELX_P HELX_P3  3  LYS A 32  ? ARG A 35  ? LYS A 52  ARG A 55  5 ? 4  
HELX_P HELX_P4  4  LYS A 58  ? GLY A 69  ? LYS A 78  GLY A 89  1 ? 12 
HELX_P HELX_P5  5  SER A 116 ? ARG A 121 ? SER A 136 ARG A 141 1 ? 6  
HELX_P HELX_P6  6  SER A 124 ? THR A 139 ? SER A 144 THR A 159 1 ? 16 
HELX_P HELX_P7  7  LEU A 142 ? GLY A 151 ? LEU A 162 GLY A 171 1 ? 10 
HELX_P HELX_P8  8  GLY A 189 ? LEU A 192 ? GLY A 209 LEU A 212 5 ? 4  
HELX_P HELX_P9  9  ASP A 207 ? TRP A 211 ? ASP A 227 TRP A 231 5 ? 5  
HELX_P HELX_P10 10 SER A 225 ? ASP A 235 ? SER A 245 ASP A 255 1 ? 11 
HELX_P HELX_P11 11 THR A 343 ? THR A 349 ? THR A 363 THR A 369 1 ? 7  
HELX_P HELX_P12 12 VAL A 354 ? VAL A 361 ? VAL A 374 VAL A 381 5 ? 8  
HELX_P HELX_P13 13 THR A 471 ? ARG A 476 ? THR A 491 ARG A 496 5 ? 6  
HELX_P HELX_P14 14 TRP A 541 ? ALA A 546 ? TRP A 561 ALA A 566 5 ? 6  
HELX_P HELX_P15 15 TRP A 589 ? TYR A 600 ? TRP A 609 TYR A 620 5 ? 12 
HELX_P HELX_P16 16 ARG A 608 ? LEU A 612 ? ARG A 628 LEU A 632 5 ? 5  
HELX_P HELX_P17 17 GLU A 631 ? ASN A 636 ? GLU A 651 ASN A 656 1 ? 6  
HELX_P HELX_P18 18 HIS A 658 ? ILE A 662 ? HIS A 678 ILE A 682 5 ? 5  
HELX_P HELX_P19 19 ASP A 685 ? SER A 690 ? ASP A 705 SER A 710 5 ? 6  
HELX_P HELX_P20 20 ARG B 8   ? SER B 14  ? ARG B 28  SER B 34  5 ? 7  
HELX_P HELX_P21 21 SER B 17  ? SER B 30  ? SER B 37  SER B 50  1 ? 14 
HELX_P HELX_P22 22 LYS B 31  ? ARG B 35  ? LYS B 51  ARG B 55  5 ? 5  
HELX_P HELX_P23 23 LYS B 58  ? LYS B 68  ? LYS B 78  LYS B 88  1 ? 11 
HELX_P HELX_P24 24 SER B 116 ? ARG B 121 ? SER B 136 ARG B 141 1 ? 6  
HELX_P HELX_P25 25 SER B 124 ? THR B 139 ? SER B 144 THR B 159 1 ? 16 
HELX_P HELX_P26 26 LEU B 142 ? GLY B 151 ? LEU B 162 GLY B 171 1 ? 10 
HELX_P HELX_P27 27 GLY B 189 ? LEU B 192 ? GLY B 209 LEU B 212 5 ? 4  
HELX_P HELX_P28 28 ASP B 207 ? TRP B 211 ? ASP B 227 TRP B 231 5 ? 5  
HELX_P HELX_P29 29 SER B 225 ? ASP B 235 ? SER B 245 ASP B 255 1 ? 11 
HELX_P HELX_P30 30 THR B 343 ? THR B 349 ? THR B 363 THR B 369 1 ? 7  
HELX_P HELX_P31 31 VAL B 354 ? VAL B 361 ? VAL B 374 VAL B 381 5 ? 8  
HELX_P HELX_P32 32 THR B 471 ? ARG B 476 ? THR B 491 ARG B 496 5 ? 6  
HELX_P HELX_P33 33 TRP B 541 ? ALA B 546 ? TRP B 561 ALA B 566 5 ? 6  
HELX_P HELX_P34 34 TRP B 589 ? TYR B 600 ? TRP B 609 TYR B 620 5 ? 12 
HELX_P HELX_P35 35 ARG B 608 ? LEU B 612 ? ARG B 628 LEU B 632 5 ? 5  
HELX_P HELX_P36 36 VAL B 629 ? HIS B 635 ? VAL B 649 HIS B 655 5 ? 7  
HELX_P HELX_P37 37 HIS B 658 ? ILE B 662 ? HIS B 678 ILE B 682 5 ? 5  
HELX_P HELX_P38 38 ASP B 685 ? SER B 690 ? ASP B 705 SER B 710 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 157 SG  ? ? ? 1_555 A CYS 161 SG ? ? A CYS 177  A CYS 181  1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf2  disulf ? ? A CYS 371 SG  ? ? ? 1_555 A CYS 397 SG ? ? A CYS 391  A CYS 417  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf3  disulf ? ? A CYS 716 SG  ? ? ? 1_555 B CYS 716 SG ? ? A CYS 736  B CYS 736  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf4  disulf ? ? B CYS 157 SG  ? ? ? 1_555 B CYS 161 SG ? ? B CYS 177  B CYS 181  1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf5  disulf ? ? B CYS 371 SG  ? ? ? 1_555 B CYS 397 SG ? ? B CYS 391  B CYS 417  1_555 ? ? ? ? ? ? ? 2.066 ? 
covale1  covale ? ? A ASN 440 C   ? ? ? 1_555 A TPQ 441 N  ? ? A ASN 460  A TPQ 461  1_555 ? ? ? ? ? ? ? 1.334 ? 
covale2  covale ? ? A TPQ 441 C   ? ? ? 1_555 A ASP 442 N  ? ? A TPQ 461  A ASP 462  1_555 ? ? ? ? ? ? ? 1.330 ? 
covale3  covale ? ? B ASN 440 C   ? ? ? 1_555 B TPQ 441 N  ? ? B ASN 460  B TPQ 461  1_555 ? ? ? ? ? ? ? 1.332 ? 
covale4  covale ? ? B TPQ 441 C   ? ? ? 1_555 B ASP 442 N  ? ? B TPQ 461  B ASP 462  1_555 ? ? ? ? ? ? ? 1.332 ? 
covale5  covale ? ? A ASN 90  ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 110  A NAG 1101 1_555 ? ? ? ? ? ? ? 1.443 ? 
metalc1  metalc ? ? A TPQ 441 O4  ? ? ? 1_555 C CU  .   CU ? ? A TPQ 461  A CU  801  1_555 ? ? ? ? ? ? ? 2.233 ? 
metalc2  metalc ? ? A HIS 490 NE2 ? ? ? 1_555 C CU  .   CU ? ? A HIS 510  A CU  801  1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc3  metalc ? ? A HIS 492 NE2 ? ? ? 1_555 C CU  .   CU ? ? A HIS 512  A CU  801  1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc4  metalc ? ? A ASP 499 OD1 ? ? ? 1_555 D CA  .   CA ? ? A ASP 519  A CA  802  1_555 ? ? ? ? ? ? ? 2.313 ? 
metalc5  metalc ? ? A LEU 500 O   ? ? ? 1_555 D CA  .   CA ? ? A LEU 520  A CA  802  1_555 ? ? ? ? ? ? ? 2.322 ? 
metalc6  metalc ? ? A ASP 501 OD1 ? ? ? 1_555 D CA  .   CA ? ? A ASP 521  A CA  802  1_555 ? ? ? ? ? ? ? 2.382 ? 
covale6  covale ? ? A ASN 518 ND2 ? ? ? 1_555 K NAG .   C1 ? ? A ASN 538  A NAG 5381 1_555 ? ? ? ? ? ? ? 1.440 ? 
metalc7  metalc ? ? A GLU 542 OE1 ? ? ? 1_555 E CA  .   CA ? ? A GLU 562  A CA  803  1_555 ? ? ? ? ? ? ? 2.504 ? 
metalc8  metalc ? ? A GLU 542 OE2 ? ? ? 1_555 E CA  .   CA ? ? A GLU 562  A CA  803  1_555 ? ? ? ? ? ? ? 2.610 ? 
metalc9  metalc ? ? A PHE 633 O   ? ? ? 1_555 E CA  .   CA ? ? A PHE 653  A CA  803  1_555 ? ? ? ? ? ? ? 2.326 ? 
metalc10 metalc ? ? A ASN 636 OD1 ? ? ? 1_555 E CA  .   CA ? ? A ASN 656  A CA  803  1_555 ? ? ? ? ? ? ? 2.450 ? 
metalc11 metalc ? ? A GLU 638 OE1 ? ? ? 1_555 E CA  .   CA ? ? A GLU 658  A CA  803  1_555 ? ? ? ? ? ? ? 2.449 ? 
metalc12 metalc ? ? A ASP 644 OD1 ? ? ? 1_555 D CA  .   CA ? ? A ASP 664  A CA  802  1_555 ? ? ? ? ? ? ? 2.337 ? 
metalc13 metalc ? ? A LEU 645 O   ? ? ? 1_555 D CA  .   CA ? ? A LEU 665  A CA  802  1_555 ? ? ? ? ? ? ? 2.361 ? 
metalc14 metalc ? ? A HIS 655 ND1 ? ? ? 1_555 C CU  .   CU ? ? A HIS 675  A CU  801  1_555 ? ? ? ? ? ? ? 2.020 ? 
covale7  covale ? ? A ASN 725 ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 745  A NAG 7451 1_555 ? ? ? ? ? ? ? 1.428 ? 
covale8  covale ? ? B ASN 90  ND2 ? ? ? 1_555 S NAG .   C1 ? ? B ASN 110  B NAG 1101 1_555 ? ? ? ? ? ? ? 1.444 ? 
metalc15 metalc ? ? B TPQ 441 O4  ? ? ? 1_555 O CU  .   CU ? ? B TPQ 461  B CU  801  1_555 ? ? ? ? ? ? ? 2.159 ? 
metalc16 metalc ? ? B HIS 490 NE2 ? ? ? 1_555 O CU  .   CU ? ? B HIS 510  B CU  801  1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc17 metalc ? ? B HIS 492 NE2 ? ? ? 1_555 O CU  .   CU ? ? B HIS 512  B CU  801  1_555 ? ? ? ? ? ? ? 2.000 ? 
metalc18 metalc ? ? B ASP 499 OD1 ? ? ? 1_555 P CA  .   CA ? ? B ASP 519  B CA  802  1_555 ? ? ? ? ? ? ? 2.266 ? 
metalc19 metalc ? ? B LEU 500 O   ? ? ? 1_555 P CA  .   CA ? ? B LEU 520  B CA  802  1_555 ? ? ? ? ? ? ? 2.341 ? 
metalc20 metalc ? ? B ASP 501 OD1 ? ? ? 1_555 P CA  .   CA ? ? B ASP 521  B CA  802  1_555 ? ? ? ? ? ? ? 2.220 ? 
covale9  covale ? ? B ASN 518 ND2 ? ? ? 1_555 U NAG .   C1 ? ? B ASN 538  B NAG 5381 1_555 ? ? ? ? ? ? ? 1.431 ? 
metalc21 metalc ? ? B GLU 542 OE1 ? ? ? 1_555 Q CA  .   CA ? ? B GLU 562  B CA  803  1_555 ? ? ? ? ? ? ? 2.597 ? 
metalc22 metalc ? ? B GLU 542 OE2 ? ? ? 1_555 Q CA  .   CA ? ? B GLU 562  B CA  803  1_555 ? ? ? ? ? ? ? 2.700 ? 
metalc23 metalc ? ? B PHE 633 O   ? ? ? 1_555 Q CA  .   CA ? ? B PHE 653  B CA  803  1_555 ? ? ? ? ? ? ? 2.406 ? 
metalc24 metalc ? ? B ASN 636 OD1 ? ? ? 1_555 Q CA  .   CA ? ? B ASN 656  B CA  803  1_555 ? ? ? ? ? ? ? 2.347 ? 
metalc25 metalc ? ? B GLU 638 OE1 ? ? ? 1_555 Q CA  .   CA ? ? B GLU 658  B CA  803  1_555 ? ? ? ? ? ? ? 2.475 ? 
metalc26 metalc ? ? B ASP 644 OD1 ? ? ? 1_555 P CA  .   CA ? ? B ASP 664  B CA  802  1_555 ? ? ? ? ? ? ? 2.259 ? 
metalc27 metalc ? ? B LEU 645 O   ? ? ? 1_555 P CA  .   CA ? ? B LEU 665  B CA  802  1_555 ? ? ? ? ? ? ? 2.316 ? 
metalc28 metalc ? ? B HIS 655 ND1 ? ? ? 1_555 O CU  .   CU ? ? B HIS 675  B CU  801  1_555 ? ? ? ? ? ? ? 2.020 ? 
covale10 covale ? ? B ASN 725 ND2 ? ? ? 1_555 W NAG .   C1 ? ? B ASN 745  B NAG 7451 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale11 covale ? ? H NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? A NAG 1101 A NAG 1102 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale12 covale ? ? I NAG .   O4  ? ? ? 1_555 J BMA .   C1 ? ? A NAG 1102 A BMA 1103 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale13 covale ? ? K NAG .   O4  ? ? ? 1_555 L NAG .   C1 ? ? A NAG 5381 A NAG 5382 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale14 covale ? ? M NAG .   O4  ? ? ? 1_555 N NAG .   C1 ? ? A NAG 7451 A NAG 7452 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale15 covale ? ? S NAG .   O4  ? ? ? 1_555 T NAG .   C1 ? ? B NAG 1101 B NAG 1102 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale16 covale ? ? U NAG .   O4  ? ? ? 1_555 V NAG .   C1 ? ? B NAG 5381 B NAG 5382 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale17 covale ? ? W NAG .   O4  ? ? ? 1_555 X NAG .   C1 ? ? B NAG 7451 B NAG 7452 1_555 ? ? ? ? ? ? ? 1.443 ? 
metalc29 metalc ? ? D CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? A CA  802  A HOH 20   1_555 ? ? ? ? ? ? ? 2.507 ? 
metalc30 metalc ? ? E CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? A CA  803  A HOH 758  1_555 ? ? ? ? ? ? ? 2.381 ? 
metalc31 metalc ? ? E CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? A CA  803  A HOH 817  1_555 ? ? ? ? ? ? ? 2.324 ? 
metalc32 metalc ? ? P CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? B CA  802  B HOH 876  1_555 ? ? ? ? ? ? ? 2.440 ? 
metalc33 metalc ? ? Q CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? B CA  803  B HOH 5    1_555 ? ? ? ? ? ? ? 2.384 ? 
metalc34 metalc ? ? Q CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? B CA  803  B HOH 834  1_555 ? ? ? ? ? ? ? 2.326 ? 
# 
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 97  A . ? GLY 117 A PRO 98  A ? PRO 118 A 1 -6.45 
2 LEU 99  A . ? LEU 119 A PRO 100 A ? PRO 120 A 1 0.91  
3 ALA 168 A . ? ALA 188 A PRO 169 A ? PRO 189 A 1 0.23  
4 ILE 662 A . ? ILE 682 A PRO 663 A ? PRO 683 A 1 3.46  
5 GLY 97  B . ? GLY 117 B PRO 98  B ? PRO 118 B 1 -4.65 
6 LEU 99  B . ? LEU 119 B PRO 100 B ? PRO 120 B 1 -4.42 
7 ALA 168 B . ? ALA 188 B PRO 169 B ? PRO 189 B 1 2.85  
8 ILE 662 B . ? ILE 682 B PRO 663 B ? PRO 683 B 1 0.73  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 20 ? 
B ? 9  ? 
C ? 5  ? 
D ? 5  ? 
E ? 2  ? 
F ? 4  ? 
G ? 3  ? 
H ? 20 ? 
I ? 9  ? 
J ? 5  ? 
K ? 5  ? 
L ? 4  ? 
M ? 3  ? 
# 
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  ? anti-parallel 
A 2  3  ? anti-parallel 
A 3  4  ? anti-parallel 
A 4  5  ? anti-parallel 
A 5  6  ? anti-parallel 
A 6  7  ? anti-parallel 
A 7  8  ? anti-parallel 
A 8  9  ? anti-parallel 
A 9  10 ? anti-parallel 
A 10 11 ? anti-parallel 
A 11 12 ? anti-parallel 
A 12 13 ? anti-parallel 
A 13 14 ? anti-parallel 
A 14 15 ? anti-parallel 
A 15 16 ? anti-parallel 
A 16 17 ? anti-parallel 
A 17 18 ? anti-parallel 
A 18 19 ? anti-parallel 
A 19 20 ? anti-parallel 
B 1  2  ? anti-parallel 
B 2  3  ? anti-parallel 
B 3  4  ? anti-parallel 
B 4  5  ? anti-parallel 
B 5  6  ? anti-parallel 
B 6  7  ? anti-parallel 
B 7  8  ? anti-parallel 
B 8  9  ? anti-parallel 
C 1  2  ? anti-parallel 
C 2  3  ? anti-parallel 
C 3  4  ? anti-parallel 
C 4  5  ? anti-parallel 
D 1  2  ? anti-parallel 
D 2  3  ? anti-parallel 
D 3  4  ? anti-parallel 
D 4  5  ? anti-parallel 
E 1  2  ? anti-parallel 
F 1  2  ? anti-parallel 
F 2  3  ? anti-parallel 
F 3  4  ? anti-parallel 
G 1  2  ? anti-parallel 
G 2  3  ? anti-parallel 
H 1  2  ? anti-parallel 
H 2  3  ? anti-parallel 
H 3  4  ? anti-parallel 
H 4  5  ? anti-parallel 
H 5  6  ? anti-parallel 
H 6  7  ? anti-parallel 
H 7  8  ? anti-parallel 
H 8  9  ? anti-parallel 
H 9  10 ? anti-parallel 
H 10 11 ? anti-parallel 
H 11 12 ? anti-parallel 
H 12 13 ? anti-parallel 
H 13 14 ? anti-parallel 
H 14 15 ? anti-parallel 
H 15 16 ? anti-parallel 
H 16 17 ? anti-parallel 
H 17 18 ? anti-parallel 
H 18 19 ? anti-parallel 
H 19 20 ? anti-parallel 
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
I 5  6  ? anti-parallel 
I 6  7  ? anti-parallel 
I 7  8  ? anti-parallel 
I 8  9  ? anti-parallel 
J 1  2  ? anti-parallel 
J 2  3  ? anti-parallel 
J 3  4  ? anti-parallel 
J 4  5  ? anti-parallel 
K 1  2  ? anti-parallel 
K 2  3  ? anti-parallel 
K 3  4  ? anti-parallel 
K 4  5  ? 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 
# 
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  TYR A 104 ? LEU A 108 ? TYR A 124 LEU A 128 
A 2  ASN A 90  ? GLY A 97  ? ASN A 110 GLY A 117 
A 3  GLU A 76  ? PHE A 83  ? GLU A 96  PHE A 103 
A 4  ASN A 47  ? LEU A 55  ? ASN A 67  LEU A 75  
A 5  THR A 376 ? TYR A 384 ? THR A 396 TYR A 404 
A 6  VAL A 390 ? PRO A 402 ? VAL A 410 PRO A 422 
A 7  GLN A 428 ? SER A 436 ? GLN A 448 SER A 456 
A 8  TPQ A 441 ? PHE A 449 ? TPQ A 461 PHE A 469 
A 9  MET A 455 ? GLY A 463 ? MET A 475 GLY A 483 
A 10 SER A 671 ? PHE A 679 ? SER A 691 PHE A 699 
A 11 LYS A 570 ? HIS A 578 ? LYS A 590 HIS A 598 
A 12 TYR A 556 ? GLU A 564 ? TYR A 576 GLU A 584 
A 13 LYS A 506 ? THR A 520 ? LYS A 526 THR A 540 
A 14 GLU A 643 ? HIS A 655 ? GLU A 663 HIS A 675 
A 15 HIS A 490 ? LEU A 500 ? HIS A 510 LEU A 520 
A 16 GLU A 324 ? TYR A 339 ? GLU A 344 TYR A 359 
A 17 GLY A 313 ? PHE A 321 ? GLY A 333 PHE A 341 
A 18 TRP A 302 ? ARG A 309 ? TRP A 322 ARG A 329 
A 19 ALA A 296 ? TYR A 299 ? ALA A 316 TYR A 319 
A 20 ARG A 291 ? GLU A 293 ? ARG A 311 GLU A 313 
B 1  ARG A 291 ? GLU A 293 ? ARG A 311 GLU A 313 
B 2  ALA A 296 ? TYR A 299 ? ALA A 316 TYR A 319 
B 3  TRP A 302 ? ARG A 309 ? TRP A 322 ARG A 329 
B 4  GLY A 313 ? PHE A 321 ? GLY A 333 PHE A 341 
B 5  GLU A 324 ? TYR A 339 ? GLU A 344 TYR A 359 
B 6  HIS A 490 ? LEU A 500 ? HIS A 510 LEU A 520 
B 7  GLU A 643 ? HIS A 655 ? GLU A 663 HIS A 675 
B 8  LYS A 506 ? THR A 520 ? LYS A 526 THR A 540 
B 9  ARG A 528 ? TYR A 539 ? ARG A 548 TYR A 559 
C 1  LEU A 602 ? LYS A 606 ? LEU A 622 LYS A 626 
C 2  GLU A 643 ? HIS A 655 ? GLU A 663 HIS A 675 
C 3  HIS A 490 ? LEU A 500 ? HIS A 510 LEU A 520 
C 4  GLU A 324 ? TYR A 339 ? GLU A 344 TYR A 359 
C 5  LYS A 350 ? LEU A 352 ? LYS A 370 LEU A 372 
D 1  LEU A 162 ? ASP A 166 ? LEU A 182 ASP A 186 
D 2  ARG A 178 ? ARG A 185 ? ARG A 198 ARG A 205 
D 3  PRO A 194 ? ASP A 202 ? PRO A 214 ASP A 222 
D 4  ALA A 212 ? TYR A 218 ? ALA A 232 TYR A 238 
D 5  LYS A 221 ? PHE A 222 ? LYS A 241 PHE A 242 
E 1  ARG A 281 ? VAL A 283 ? ARG A 301 VAL A 303 
E 2  ARG B 281 ? VAL B 283 ? ARG B 301 VAL B 303 
F 1  ARG A 408 ? SER A 413 ? ARG A 428 SER A 433 
F 2  PHE A 419 ? LEU A 425 ? PHE A 439 LEU A 445 
F 3  VAL A 694 ? TRP A 697 ? VAL A 714 TRP A 717 
F 4  TYR A 705 ? GLN A 707 ? TYR A 725 GLN A 727 
G 1  ALA A 467 ? PHE A 469 ? ALA A 487 PHE A 489 
G 2  LEU A 485 ? ASN A 488 ? LEU A 505 ASN A 508 
G 3  GLY A 478 ? HIS A 482 ? GLY A 498 HIS A 502 
H 1  TYR B 104 ? ALA B 107 ? TYR B 124 ALA B 127 
H 2  ASN B 90  ? GLY B 97  ? ASN B 110 GLY B 117 
H 3  GLU B 76  ? PHE B 83  ? GLU B 96  PHE B 103 
H 4  ASN B 47  ? LEU B 55  ? ASN B 67  LEU B 75  
H 5  THR B 376 ? TYR B 384 ? THR B 396 TYR B 404 
H 6  VAL B 390 ? PRO B 402 ? VAL B 410 PRO B 422 
H 7  GLN B 428 ? THR B 437 ? GLN B 448 THR B 457 
H 8  TPQ B 441 ? PHE B 449 ? TPQ B 461 PHE B 469 
H 9  MET B 455 ? GLY B 463 ? MET B 475 GLY B 483 
H 10 SER B 671 ? PHE B 679 ? SER B 691 PHE B 699 
H 11 LYS B 570 ? HIS B 578 ? LYS B 590 HIS B 598 
H 12 TYR B 556 ? GLU B 564 ? TYR B 576 GLU B 584 
H 13 LYS B 506 ? THR B 520 ? LYS B 526 THR B 540 
H 14 GLU B 643 ? HIS B 655 ? GLU B 663 HIS B 675 
H 15 HIS B 490 ? LEU B 500 ? HIS B 510 LEU B 520 
H 16 GLU B 324 ? TYR B 339 ? GLU B 344 TYR B 359 
H 17 GLY B 313 ? PHE B 321 ? GLY B 333 PHE B 341 
H 18 TRP B 302 ? ARG B 309 ? TRP B 322 ARG B 329 
H 19 ALA B 296 ? TYR B 299 ? ALA B 316 TYR B 319 
H 20 ARG B 291 ? GLU B 293 ? ARG B 311 GLU B 313 
I 1  ARG B 291 ? GLU B 293 ? ARG B 311 GLU B 313 
I 2  ALA B 296 ? TYR B 299 ? ALA B 316 TYR B 319 
I 3  TRP B 302 ? ARG B 309 ? TRP B 322 ARG B 329 
I 4  GLY B 313 ? PHE B 321 ? GLY B 333 PHE B 341 
I 5  GLU B 324 ? TYR B 339 ? GLU B 344 TYR B 359 
I 6  HIS B 490 ? LEU B 500 ? HIS B 510 LEU B 520 
I 7  GLU B 643 ? HIS B 655 ? GLU B 663 HIS B 675 
I 8  LYS B 506 ? THR B 520 ? LYS B 526 THR B 540 
I 9  ARG B 528 ? GLN B 538 ? ARG B 548 GLN B 558 
J 1  LEU B 602 ? LYS B 606 ? LEU B 622 LYS B 626 
J 2  GLU B 643 ? HIS B 655 ? GLU B 663 HIS B 675 
J 3  HIS B 490 ? LEU B 500 ? HIS B 510 LEU B 520 
J 4  GLU B 324 ? TYR B 339 ? GLU B 344 TYR B 359 
J 5  LYS B 350 ? LEU B 352 ? LYS B 370 LEU B 372 
K 1  LEU B 162 ? ASP B 166 ? LEU B 182 ASP B 186 
K 2  ARG B 178 ? ARG B 185 ? ARG B 198 ARG B 205 
K 3  PRO B 194 ? ASP B 202 ? PRO B 214 ASP B 222 
K 4  ALA B 212 ? TYR B 218 ? ALA B 232 TYR B 238 
K 5  LYS B 221 ? PHE B 222 ? LYS B 241 PHE B 242 
L 1  ARG B 408 ? SER B 413 ? ARG B 428 SER B 433 
L 2  PHE B 419 ? LEU B 425 ? PHE B 439 LEU B 445 
L 3  VAL B 694 ? TRP B 697 ? VAL B 714 TRP B 717 
L 4  TYR B 705 ? GLN B 707 ? TYR B 725 GLN B 727 
M 1  ALA B 467 ? PHE B 469 ? ALA B 487 PHE B 489 
M 2  LEU B 485 ? ASN B 488 ? LEU B 505 ASN B 508 
M 3  GLY B 478 ? HIS B 482 ? GLY B 498 HIS B 502 
# 
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  O ARG A 106 ? O ARG A 126 N ALA A 95  ? N ALA A 115 
A 2  3  O VAL A 96  ? O VAL A 116 N ALA A 77  ? N ALA A 97  
A 3  4  O ARG A 78  ? O ARG A 98  N GLU A 53  ? N GLU A 73  
A 4  5  N ILE A 52  ? N ILE A 72  O TYR A 383 ? O TYR A 403 
A 5  6  N THR A 380 ? N THR A 400 O TYR A 392 ? O TYR A 412 
A 6  7  N PHE A 399 ? N PHE A 419 O VAL A 431 ? O VAL A 451 
A 7  8  N LEU A 432 ? N LEU A 452 O PHE A 447 ? O PHE A 467 
A 8  9  N ILE A 448 ? N ILE A 468 O GLU A 456 ? O GLU A 476 
A 9  10 N MET A 455 ? N MET A 475 O LEU A 676 ? O LEU A 696 
A 10 11 O ARG A 677 ? O ARG A 697 N ARG A 574 ? N ARG A 594 
A 11 12 O ARG A 571 ? O ARG A 591 N GLN A 563 ? N GLN A 583 
A 12 13 O LEU A 558 ? O LEU A 578 N GLN A 510 ? N GLN A 530 
A 13 14 N ASN A 507 ? N ASN A 527 O GLU A 643 ? O GLU A 663 
A 14 15 O VAL A 651 ? O VAL A 671 N VAL A 494 ? N VAL A 514 
A 15 16 O LEU A 493 ? O LEU A 513 N VAL A 336 ? N VAL A 356 
A 16 17 O ILE A 326 ? O ILE A 346 N VAL A 319 ? N VAL A 339 
A 17 18 O HIS A 320 ? O HIS A 340 N SER A 303 ? N SER A 323 
A 18 19 O PHE A 304 ? O PHE A 324 N VAL A 297 ? N VAL A 317 
A 19 20 O LEU A 298 ? O LEU A 318 N ARG A 291 ? N ARG A 311 
B 1  2  N ARG A 291 ? N ARG A 311 O LEU A 298 ? O LEU A 318 
B 2  3  N VAL A 297 ? N VAL A 317 O PHE A 304 ? O PHE A 324 
B 3  4  N SER A 303 ? N SER A 323 O HIS A 320 ? O HIS A 340 
B 4  5  N VAL A 319 ? N VAL A 339 O ILE A 326 ? O ILE A 346 
B 5  6  N VAL A 336 ? N VAL A 356 O LEU A 493 ? O LEU A 513 
B 6  7  N VAL A 494 ? N VAL A 514 O VAL A 651 ? O VAL A 671 
B 7  8  O GLU A 643 ? O GLU A 663 N ASN A 507 ? N ASN A 527 
B 8  9  N ILE A 519 ? N ILE A 539 O VAL A 529 ? O VAL A 549 
C 1  2  N THR A 605 ? N THR A 625 O VAL A 646 ? O VAL A 666 
C 2  3  O VAL A 651 ? O VAL A 671 N VAL A 494 ? N VAL A 514 
C 3  4  O LEU A 493 ? O LEU A 513 N VAL A 336 ? N VAL A 356 
C 4  5  N ALA A 337 ? N ALA A 357 O TYR A 351 ? O TYR A 371 
D 1  2  N ALA A 163 ? N ALA A 183 O GLN A 184 ? O GLN A 204 
D 2  3  N SER A 179 ? N SER A 199 O VAL A 201 ? O VAL A 221 
D 3  4  N GLU A 198 ? N GLU A 218 O TRP A 217 ? O TRP A 237 
D 4  5  N TYR A 218 ? N TYR A 238 O LYS A 221 ? O LYS A 241 
E 1  2  N VAL A 283 ? N VAL A 303 O ARG B 281 ? O ARG B 301 
F 1  2  N ASN A 412 ? N ASN A 432 O ASN A 420 ? O ASN A 440 
F 2  3  N TYR A 422 ? N TYR A 442 O VAL A 696 ? O VAL A 716 
F 3  4  N ILE A 695 ? N ILE A 715 O GLN A 707 ? O GLN A 727 
G 1  2  N THR A 468 ? N THR A 488 O ILE A 486 ? O ILE A 506 
G 2  3  O GLY A 487 ? O GLY A 507 N THR A 479 ? N THR A 499 
H 1  2  O ARG B 106 ? O ARG B 126 N ALA B 95  ? N ALA B 115 
H 2  3  O ASN B 90  ? O ASN B 110 N PHE B 83  ? N PHE B 103 
H 3  4  O ARG B 78  ? O ARG B 98  N GLU B 53  ? N GLU B 73  
H 4  5  N ILE B 52  ? N ILE B 72  O TYR B 383 ? O TYR B 403 
H 5  6  N THR B 380 ? N THR B 400 O TYR B 392 ? O TYR B 412 
H 6  7  N PHE B 399 ? N PHE B 419 O VAL B 431 ? O VAL B 451 
H 7  8  N SER B 436 ? N SER B 456 O TYR B 443 ? O TYR B 463 
H 8  9  N ASP B 446 ? N ASP B 466 O LYS B 458 ? O LYS B 478 
H 9  10 N MET B 455 ? N MET B 475 O LEU B 676 ? O LEU B 696 
H 10 11 O ARG B 677 ? O ARG B 697 N ARG B 574 ? N ARG B 594 
H 11 12 O ARG B 571 ? O ARG B 591 N SER B 561 ? N SER B 581 
H 12 13 O LEU B 558 ? O LEU B 578 N GLN B 510 ? N GLN B 530 
H 13 14 N ASN B 507 ? N ASN B 527 O GLU B 643 ? O GLU B 663 
H 14 15 O ALA B 647 ? O ALA B 667 N VAL B 498 ? N VAL B 518 
H 15 16 O HIS B 495 ? O HIS B 515 N GLN B 333 ? N GLN B 353 
H 16 17 O ILE B 326 ? O ILE B 346 N VAL B 319 ? N VAL B 339 
H 17 18 O HIS B 320 ? O HIS B 340 N SER B 303 ? N SER B 323 
H 18 19 O PHE B 304 ? O PHE B 324 N VAL B 297 ? N VAL B 317 
H 19 20 O LEU B 298 ? O LEU B 318 N ARG B 291 ? N ARG B 311 
I 1  2  N ARG B 291 ? N ARG B 311 O LEU B 298 ? O LEU B 318 
I 2  3  N VAL B 297 ? N VAL B 317 O PHE B 304 ? O PHE B 324 
I 3  4  N SER B 303 ? N SER B 323 O HIS B 320 ? O HIS B 340 
I 4  5  N VAL B 319 ? N VAL B 339 O ILE B 326 ? O ILE B 346 
I 5  6  N GLN B 333 ? N GLN B 353 O HIS B 495 ? O HIS B 515 
I 6  7  N VAL B 498 ? N VAL B 518 O ALA B 647 ? O ALA B 667 
I 7  8  O GLU B 643 ? O GLU B 663 N ASN B 507 ? N ASN B 527 
I 8  9  N THR B 511 ? N THR B 531 O THR B 537 ? O THR B 557 
J 1  2  N THR B 605 ? N THR B 625 O VAL B 646 ? O VAL B 666 
J 2  3  O ALA B 647 ? O ALA B 667 N VAL B 498 ? N VAL B 518 
J 3  4  O HIS B 495 ? O HIS B 515 N GLN B 333 ? N GLN B 353 
J 4  5  N ALA B 337 ? N ALA B 357 O TYR B 351 ? O TYR B 371 
K 1  2  N ALA B 163 ? N ALA B 183 O GLN B 184 ? O GLN B 204 
K 2  3  N ILE B 183 ? N ILE B 203 O THR B 195 ? O THR B 215 
K 3  4  N GLU B 198 ? N GLU B 218 O TRP B 217 ? O TRP B 237 
K 4  5  N TYR B 218 ? N TYR B 238 O LYS B 221 ? O LYS B 241 
L 1  2  N ASN B 412 ? N ASN B 432 O ASN B 420 ? O ASN B 440 
L 2  3  N TYR B 422 ? N TYR B 442 O VAL B 696 ? O VAL B 716 
L 3  4  N ILE B 695 ? N ILE B 715 O GLN B 707 ? O GLN B 727 
M 1  2  N THR B 468 ? N THR B 488 O ILE B 486 ? O ILE B 506 
M 2  3  O GLY B 487 ? O GLY B 507 N THR B 479 ? N THR B 499 
# 
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 ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU A 801'   
AC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA A 802'   
AC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA A 803'   
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL A 804'  
AC5 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE PNT A 901'  
AC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 1101' 
AC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 1102' 
AC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE BMA A 1103' 
AC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 5381' 
BC1 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 5382' 
BC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG A 7451' 
BC3 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 7452' 
BC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU B 801'   
BC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA B 802'   
BC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA B 803'   
BC7 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE PNT B 901'  
BC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 1101' 
BC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 1102' 
CC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 5381' 
CC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG B 5382' 
CC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 7451' 
CC4 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG B 7452' 
# 
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 4  TPQ A 441 ? TPQ A 461  . ? 1_555 ? 
2   AC1 4  HIS A 490 ? HIS A 510  . ? 1_555 ? 
3   AC1 4  HIS A 492 ? HIS A 512  . ? 1_555 ? 
4   AC1 4  HIS A 655 ? HIS A 675  . ? 1_555 ? 
5   AC2 6  HOH Y .   ? HOH A 20   . ? 1_555 ? 
6   AC2 6  ASP A 499 ? ASP A 519  . ? 1_555 ? 
7   AC2 6  LEU A 500 ? LEU A 520  . ? 1_555 ? 
8   AC2 6  ASP A 501 ? ASP A 521  . ? 1_555 ? 
9   AC2 6  ASP A 644 ? ASP A 664  . ? 1_555 ? 
10  AC2 6  LEU A 645 ? LEU A 665  . ? 1_555 ? 
11  AC3 6  GLU A 542 ? GLU A 562  . ? 1_555 ? 
12  AC3 6  PHE A 633 ? PHE A 653  . ? 1_555 ? 
13  AC3 6  ASN A 636 ? ASN A 656  . ? 1_555 ? 
14  AC3 6  GLU A 638 ? GLU A 658  . ? 1_555 ? 
15  AC3 6  HOH Y .   ? HOH A 758  . ? 1_555 ? 
16  AC3 6  HOH Y .   ? HOH A 817  . ? 1_555 ? 
17  AC4 7  GLU A 293 ? GLU A 313  . ? 1_555 ? 
18  AC4 7  GLY A 294 ? GLY A 314  . ? 1_555 ? 
19  AC4 7  TRP A 541 ? TRP A 561  . ? 3_455 ? 
20  AC4 7  ASN A 637 ? ASN A 657  . ? 3_455 ? 
21  AC4 7  HOH Y .   ? HOH A 864  . ? 1_555 ? 
22  AC4 7  HOH Y .   ? HOH A 1047 . ? 1_555 ? 
23  AC4 7  HOH Y .   ? HOH A 1132 . ? 1_555 ? 
24  AC5 16 TYR A 128 ? TYR A 148  . ? 1_555 ? 
25  AC5 16 THR A 165 ? THR A 185  . ? 1_555 ? 
26  AC5 16 ASP A 166 ? ASP A 186  . ? 1_555 ? 
27  AC5 16 TYR A 351 ? TYR A 371  . ? 1_555 ? 
28  AC5 16 ASP A 353 ? ASP A 373  . ? 1_555 ? 
29  AC5 16 TRP A 356 ? TRP A 376  . ? 1_555 ? 
30  AC5 16 GLY A 357 ? GLY A 377  . ? 1_555 ? 
31  AC5 16 SER A 360 ? SER A 380  . ? 1_555 ? 
32  AC5 16 VAL A 361 ? VAL A 381  . ? 1_555 ? 
33  AC5 16 TYR A 384 ? TYR A 404  . ? 1_555 ? 
34  AC5 16 VAL A 438 ? VAL A 458  . ? 1_555 ? 
35  AC5 16 TYR A 439 ? TYR A 459  . ? 1_555 ? 
36  AC5 16 ASN A 440 ? ASN A 460  . ? 1_555 ? 
37  AC5 16 HOH Y .   ? HOH A 885  . ? 1_555 ? 
38  AC5 16 HOH Y .   ? HOH A 936  . ? 1_555 ? 
39  AC5 16 PHE B 415 ? PHE B 435  . ? 1_555 ? 
40  AC6 4  GLN A 86  ? GLN A 106  . ? 1_555 ? 
41  AC6 4  ASN A 90  ? ASN A 110  . ? 1_555 ? 
42  AC6 4  THR A 92  ? THR A 112  . ? 1_555 ? 
43  AC6 4  NAG I .   ? NAG A 1102 . ? 1_555 ? 
44  AC7 4  ARG A 699 ? ARG A 719  . ? 3_445 ? 
45  AC7 4  HOH Y .   ? HOH A 857  . ? 1_555 ? 
46  AC7 4  NAG H .   ? NAG A 1101 . ? 1_555 ? 
47  AC7 4  BMA J .   ? BMA A 1103 . ? 1_555 ? 
48  AC8 4  ARG A 699 ? ARG A 719  . ? 3_445 ? 
49  AC8 4  GLY A 702 ? GLY A 722  . ? 3_445 ? 
50  AC8 4  HOH Y .   ? HOH A 795  . ? 3_445 ? 
51  AC8 4  NAG I .   ? NAG A 1102 . ? 1_555 ? 
52  AC9 4  ASN A 518 ? ASN A 538  . ? 1_555 ? 
53  AC9 4  ARG A 528 ? ARG A 548  . ? 1_555 ? 
54  AC9 4  NAG L .   ? NAG A 5382 . ? 1_555 ? 
55  AC9 4  TRP B 589 ? TRP B 609  . ? 1_555 ? 
56  BC1 1  NAG K .   ? NAG A 5381 . ? 1_555 ? 
57  BC2 5  ASN A 725 ? ASN A 745  . ? 1_555 ? 
58  BC2 5  HOH Y .   ? HOH A 797  . ? 1_555 ? 
59  BC2 5  NAG N .   ? NAG A 7452 . ? 1_555 ? 
60  BC2 5  ASN B 704 ? ASN B 724  . ? 1_555 ? 
61  BC2 5  HOH Z .   ? HOH B 1043 . ? 1_555 ? 
62  BC3 1  NAG M .   ? NAG A 7451 . ? 1_555 ? 
63  BC4 4  TPQ B 441 ? TPQ B 461  . ? 1_555 ? 
64  BC4 4  HIS B 490 ? HIS B 510  . ? 1_555 ? 
65  BC4 4  HIS B 492 ? HIS B 512  . ? 1_555 ? 
66  BC4 4  HIS B 655 ? HIS B 675  . ? 1_555 ? 
67  BC5 6  ASP B 499 ? ASP B 519  . ? 1_555 ? 
68  BC5 6  LEU B 500 ? LEU B 520  . ? 1_555 ? 
69  BC5 6  ASP B 501 ? ASP B 521  . ? 1_555 ? 
70  BC5 6  ASP B 644 ? ASP B 664  . ? 1_555 ? 
71  BC5 6  LEU B 645 ? LEU B 665  . ? 1_555 ? 
72  BC5 6  HOH Z .   ? HOH B 876  . ? 1_555 ? 
73  BC6 6  HOH Z .   ? HOH B 5    . ? 1_555 ? 
74  BC6 6  GLU B 542 ? GLU B 562  . ? 1_555 ? 
75  BC6 6  PHE B 633 ? PHE B 653  . ? 1_555 ? 
76  BC6 6  ASN B 636 ? ASN B 656  . ? 1_555 ? 
77  BC6 6  GLU B 638 ? GLU B 658  . ? 1_555 ? 
78  BC6 6  HOH Z .   ? HOH B 834  . ? 1_555 ? 
79  BC7 14 PHE A 415 ? PHE A 435  . ? 1_555 ? 
80  BC7 14 TYR B 128 ? TYR B 148  . ? 1_555 ? 
81  BC7 14 THR B 165 ? THR B 185  . ? 1_555 ? 
82  BC7 14 ASP B 166 ? ASP B 186  . ? 1_555 ? 
83  BC7 14 TYR B 351 ? TYR B 371  . ? 1_555 ? 
84  BC7 14 ASP B 353 ? ASP B 373  . ? 1_555 ? 
85  BC7 14 TRP B 356 ? TRP B 376  . ? 1_555 ? 
86  BC7 14 GLY B 357 ? GLY B 377  . ? 1_555 ? 
87  BC7 14 SER B 360 ? SER B 380  . ? 1_555 ? 
88  BC7 14 VAL B 361 ? VAL B 381  . ? 1_555 ? 
89  BC7 14 TYR B 384 ? TYR B 404  . ? 1_555 ? 
90  BC7 14 TYR B 439 ? TYR B 459  . ? 1_555 ? 
91  BC7 14 ASN B 440 ? ASN B 460  . ? 1_555 ? 
92  BC7 14 HOH Z .   ? HOH B 889  . ? 1_555 ? 
93  BC8 5  GLN B 86  ? GLN B 106  . ? 1_555 ? 
94  BC8 5  ASN B 90  ? ASN B 110  . ? 1_555 ? 
95  BC8 5  THR B 92  ? THR B 112  . ? 1_555 ? 
96  BC8 5  GLU B 237 ? GLU B 257  . ? 4_545 ? 
97  BC8 5  NAG T .   ? NAG B 1102 . ? 1_555 ? 
98  BC9 4  LEU B 34  ? LEU B 54   . ? 1_555 ? 
99  BC9 4  PHE B 83  ? PHE B 103  . ? 1_555 ? 
100 BC9 4  PHE B 94  ? PHE B 114  . ? 1_555 ? 
101 BC9 4  NAG S .   ? NAG B 1101 . ? 1_555 ? 
102 CC1 5  TRP A 589 ? TRP A 609  . ? 1_555 ? 
103 CC1 5  ASN B 518 ? ASN B 538  . ? 1_555 ? 
104 CC1 5  ARG B 528 ? ARG B 548  . ? 1_555 ? 
105 CC1 5  HOH Z .   ? HOH B 760  . ? 1_555 ? 
106 CC1 5  NAG V .   ? NAG B 5382 . ? 1_555 ? 
107 CC2 3  HOH Z .   ? HOH B 760  . ? 1_555 ? 
108 CC2 3  HOH Z .   ? HOH B 872  . ? 1_555 ? 
109 CC2 3  NAG U .   ? NAG B 5381 . ? 1_555 ? 
110 CC3 5  ASN A 704 ? ASN A 724  . ? 1_555 ? 
111 CC3 5  ASN B 725 ? ASN B 745  . ? 1_555 ? 
112 CC3 5  HOH Z .   ? HOH B 1033 . ? 1_555 ? 
113 CC3 5  HOH Z .   ? HOH B 1110 . ? 1_555 ? 
114 CC3 5  NAG X .   ? NAG B 7452 . ? 1_555 ? 
115 CC4 1  NAG W .   ? NAG B 7451 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3HII 
_atom_sites.fract_transf_matrix[1][1]   0.010816 
_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]   0.010561 
_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]   0.005095 
_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  
CA 
CU 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . PRO A 1 7   ? -55.559 1.115   47.121  1.00 44.04 ? 27   PRO A N     1 
ATOM   2     C  CA    . PRO A 1 7   ? -54.548 1.325   48.179  1.00 43.70 ? 27   PRO A CA    1 
ATOM   3     C  C     . PRO A 1 7   ? -55.077 1.071   49.598  1.00 43.09 ? 27   PRO A C     1 
ATOM   4     O  O     . PRO A 1 7   ? -54.300 0.693   50.488  1.00 43.56 ? 27   PRO A O     1 
ATOM   5     C  CB    . PRO A 1 7   ? -54.142 2.798   48.001  1.00 43.79 ? 27   PRO A CB    1 
ATOM   6     C  CG    . PRO A 1 7   ? -54.683 3.205   46.644  1.00 44.05 ? 27   PRO A CG    1 
ATOM   7     C  CD    . PRO A 1 7   ? -55.917 2.376   46.452  1.00 44.18 ? 27   PRO A CD    1 
ATOM   8     N  N     . ARG A 1 8   ? -56.379 1.292   49.803  1.00 41.99 ? 28   ARG A N     1 
ATOM   9     C  CA    . ARG A 1 8   ? -57.064 0.913   51.046  1.00 41.03 ? 28   ARG A CA    1 
ATOM   10    C  C     . ARG A 1 8   ? -57.125 -0.610  51.227  1.00 39.84 ? 28   ARG A C     1 
ATOM   11    O  O     . ARG A 1 8   ? -57.218 -1.099  52.352  1.00 39.85 ? 28   ARG A O     1 
ATOM   12    C  CB    . ARG A 1 8   ? -58.492 1.483   51.071  1.00 41.00 ? 28   ARG A CB    1 
ATOM   13    N  N     . LYS A 1 9   ? -57.078 -1.349  50.119  1.00 38.37 ? 29   LYS A N     1 
ATOM   14    C  CA    . LYS A 1 9   ? -57.077 -2.812  50.155  1.00 37.29 ? 29   LYS A CA    1 
ATOM   15    C  C     . LYS A 1 9   ? -55.838 -3.405  50.828  1.00 35.86 ? 29   LYS A C     1 
ATOM   16    O  O     . LYS A 1 9   ? -55.933 -4.453  51.460  1.00 36.10 ? 29   LYS A O     1 
ATOM   17    C  CB    . LYS A 1 9   ? -57.216 -3.392  48.747  1.00 37.31 ? 29   LYS A CB    1 
ATOM   18    C  CG    . LYS A 1 9   ? -58.561 -3.075  48.102  1.00 38.24 ? 29   LYS A CG    1 
ATOM   19    C  CD    . LYS A 1 9   ? -59.058 -4.211  47.228  1.00 38.55 ? 29   LYS A CD    1 
ATOM   20    C  CE    . LYS A 1 9   ? -60.532 -4.039  46.915  1.00 38.67 ? 29   LYS A CE    1 
ATOM   21    N  NZ    . LYS A 1 9   ? -61.062 -5.204  46.167  1.00 39.14 ? 29   LYS A NZ    1 
ATOM   22    N  N     . ALA A 1 10  ? -54.695 -2.736  50.700  1.00 33.83 ? 30   ALA A N     1 
ATOM   23    C  CA    . ALA A 1 10  ? -53.451 -3.198  51.318  1.00 32.67 ? 30   ALA A CA    1 
ATOM   24    C  C     . ALA A 1 10  ? -53.547 -3.285  52.847  1.00 31.20 ? 30   ALA A C     1 
ATOM   25    O  O     . ALA A 1 10  ? -52.776 -4.002  53.469  1.00 31.12 ? 30   ALA A O     1 
ATOM   26    C  CB    . ALA A 1 10  ? -52.268 -2.295  50.901  1.00 32.38 ? 30   ALA A CB    1 
ATOM   27    N  N     . GLY A 1 11  ? -54.493 -2.547  53.431  1.00 29.84 ? 31   GLY A N     1 
ATOM   28    C  CA    . GLY A 1 11  ? -54.805 -2.604  54.855  1.00 28.69 ? 31   GLY A CA    1 
ATOM   29    C  C     . GLY A 1 11  ? -55.063 -3.999  55.406  1.00 27.66 ? 31   GLY A C     1 
ATOM   30    O  O     . GLY A 1 11  ? -54.832 -4.247  56.585  1.00 27.04 ? 31   GLY A O     1 
ATOM   31    N  N     . VAL A 1 12  ? -55.539 -4.909  54.557  1.00 26.70 ? 32   VAL A N     1 
ATOM   32    C  CA    . VAL A 1 12  ? -55.747 -6.295  54.949  1.00 25.78 ? 32   VAL A CA    1 
ATOM   33    C  C     . VAL A 1 12  ? -54.428 -6.943  55.414  1.00 25.00 ? 32   VAL A C     1 
ATOM   34    O  O     . VAL A 1 12  ? -54.429 -7.779  56.309  1.00 24.18 ? 32   VAL A O     1 
ATOM   35    C  CB    . VAL A 1 12  ? -56.408 -7.106  53.813  1.00 26.13 ? 32   VAL A CB    1 
ATOM   36    C  CG1   . VAL A 1 12  ? -55.432 -7.325  52.668  1.00 25.95 ? 32   VAL A CG1   1 
ATOM   37    C  CG2   . VAL A 1 12  ? -56.967 -8.434  54.349  1.00 25.72 ? 32   VAL A CG2   1 
ATOM   38    N  N     . PHE A 1 13  ? -53.310 -6.511  54.835  1.00 24.37 ? 33   PHE A N     1 
ATOM   39    C  CA    . PHE A 1 13  ? -51.987 -7.023  55.194  1.00 23.85 ? 33   PHE A CA    1 
ATOM   40    C  C     . PHE A 1 13  ? -51.300 -6.202  56.288  1.00 23.79 ? 33   PHE A C     1 
ATOM   41    O  O     . PHE A 1 13  ? -50.189 -6.531  56.702  1.00 23.44 ? 33   PHE A O     1 
ATOM   42    C  CB    . PHE A 1 13  ? -51.082 -7.046  53.959  1.00 23.66 ? 33   PHE A CB    1 
ATOM   43    C  CG    . PHE A 1 13  ? -51.631 -7.847  52.809  1.00 22.53 ? 33   PHE A CG    1 
ATOM   44    C  CD1   . PHE A 1 13  ? -51.773 -9.221  52.910  1.00 21.77 ? 33   PHE A CD1   1 
ATOM   45    C  CD2   . PHE A 1 13  ? -51.978 -7.230  51.617  1.00 21.21 ? 33   PHE A CD2   1 
ATOM   46    C  CE1   . PHE A 1 13  ? -52.255 -9.962  51.850  1.00 20.65 ? 33   PHE A CE1   1 
ATOM   47    C  CE2   . PHE A 1 13  ? -52.478 -7.967  50.558  1.00 21.16 ? 33   PHE A CE2   1 
ATOM   48    C  CZ    . PHE A 1 13  ? -52.612 -9.338  50.671  1.00 20.93 ? 33   PHE A CZ    1 
ATOM   49    N  N     . SER A 1 14  ? -51.956 -5.147  56.759  1.00 23.72 ? 34   SER A N     1 
ATOM   50    C  CA    . SER A 1 14  ? -51.314 -4.188  57.647  1.00 24.35 ? 34   SER A CA    1 
ATOM   51    C  C     . SER A 1 14  ? -51.192 -4.648  59.089  1.00 24.46 ? 34   SER A C     1 
ATOM   52    O  O     . SER A 1 14  ? -52.070 -5.312  59.631  1.00 24.52 ? 34   SER A O     1 
ATOM   53    C  CB    . SER A 1 14  ? -52.055 -2.850  57.629  1.00 24.15 ? 34   SER A CB    1 
ATOM   54    O  OG    . SER A 1 14  ? -53.299 -2.966  58.290  1.00 25.38 ? 34   SER A OG    1 
ATOM   55    N  N     . ASP A 1 15  ? -50.093 -4.248  59.711  1.00 24.78 ? 35   ASP A N     1 
ATOM   56    C  CA    . ASP A 1 15  ? -49.869 -4.495  61.120  1.00 24.92 ? 35   ASP A CA    1 
ATOM   57    C  C     . ASP A 1 15  ? -50.887 -3.774  61.987  1.00 24.73 ? 35   ASP A C     1 
ATOM   58    O  O     . ASP A 1 15  ? -51.551 -2.845  61.553  1.00 24.43 ? 35   ASP A O     1 
ATOM   59    C  CB    . ASP A 1 15  ? -48.462 -4.044  61.511  1.00 25.15 ? 35   ASP A CB    1 
ATOM   60    C  CG    . ASP A 1 15  ? -47.401 -4.948  60.959  1.00 25.84 ? 35   ASP A CG    1 
ATOM   61    O  OD1   . ASP A 1 15  ? -47.529 -6.183  61.127  1.00 28.56 ? 35   ASP A OD1   1 
ATOM   62    O  OD2   . ASP A 1 15  ? -46.447 -4.431  60.353  1.00 24.79 ? 35   ASP A OD2   1 
ATOM   63    N  N     . LEU A 1 16  ? -51.001 -4.223  63.227  1.00 24.91 ? 36   LEU A N     1 
ATOM   64    C  CA    . LEU A 1 16  ? -51.910 -3.608  64.174  1.00 24.85 ? 36   LEU A CA    1 
ATOM   65    C  C     . LEU A 1 16  ? -51.393 -2.217  64.555  1.00 25.17 ? 36   LEU A C     1 
ATOM   66    O  O     . LEU A 1 16  ? -50.189 -2.034  64.752  1.00 24.67 ? 36   LEU A O     1 
ATOM   67    C  CB    . LEU A 1 16  ? -52.034 -4.477  65.423  1.00 24.81 ? 36   LEU A CB    1 
ATOM   68    C  CG    . LEU A 1 16  ? -52.576 -5.894  65.227  1.00 24.21 ? 36   LEU A CG    1 
ATOM   69    C  CD1   . LEU A 1 16  ? -52.552 -6.657  66.550  1.00 23.13 ? 36   LEU A CD1   1 
ATOM   70    C  CD2   . LEU A 1 16  ? -53.981 -5.879  64.610  1.00 22.66 ? 36   LEU A CD2   1 
ATOM   71    N  N     . SER A 1 17  ? -52.310 -1.250  64.647  1.00 25.10 ? 37   SER A N     1 
ATOM   72    C  CA    . SER A 1 17  ? -51.988 0.096   65.123  1.00 25.07 ? 37   SER A CA    1 
ATOM   73    C  C     . SER A 1 17  ? -51.836 0.097   66.630  1.00 24.94 ? 37   SER A C     1 
ATOM   74    O  O     . SER A 1 17  ? -52.265 -0.842  67.300  1.00 24.03 ? 37   SER A O     1 
ATOM   75    C  CB    . SER A 1 17  ? -53.109 1.065   64.775  1.00 25.09 ? 37   SER A CB    1 
ATOM   76    O  OG    . SER A 1 17  ? -54.306 0.708   65.466  1.00 26.54 ? 37   SER A OG    1 
ATOM   77    N  N     . ASN A 1 18  ? -51.260 1.178   67.154  1.00 24.95 ? 38   ASN A N     1 
ATOM   78    C  CA    . ASN A 1 18  ? -51.203 1.411   68.598  1.00 25.29 ? 38   ASN A CA    1 
ATOM   79    C  C     . ASN A 1 18  ? -52.595 1.266   69.236  1.00 25.43 ? 38   ASN A C     1 
ATOM   80    O  O     . ASN A 1 18  ? -52.750 0.600   70.261  1.00 25.32 ? 38   ASN A O     1 
ATOM   81    C  CB    . ASN A 1 18  ? -50.610 2.795   68.880  1.00 25.50 ? 38   ASN A CB    1 
ATOM   82    C  CG    . ASN A 1 18  ? -50.300 3.021   70.344  1.00 25.84 ? 38   ASN A CG    1 
ATOM   83    O  OD1   . ASN A 1 18  ? -50.059 2.084   71.103  1.00 26.99 ? 38   ASN A OD1   1 
ATOM   84    N  ND2   . ASN A 1 18  ? -50.287 4.282   70.746  1.00 27.42 ? 38   ASN A ND2   1 
ATOM   85    N  N     . GLN A 1 19  ? -53.606 1.846   68.592  1.00 25.60 ? 39   GLN A N     1 
ATOM   86    C  CA    . GLN A 1 19  ? -54.993 1.749   69.060  1.00 26.04 ? 39   GLN A CA    1 
ATOM   87    C  C     . GLN A 1 19  ? -55.511 0.307   69.122  1.00 25.98 ? 39   GLN A C     1 
ATOM   88    O  O     . GLN A 1 19  ? -56.112 -0.103  70.109  1.00 26.31 ? 39   GLN A O     1 
ATOM   89    C  CB    . GLN A 1 19  ? -55.919 2.583   68.162  1.00 26.06 ? 39   GLN A CB    1 
ATOM   90    N  N     . GLU A 1 20  ? -55.284 -0.451  68.058  1.00 26.34 ? 40   GLU A N     1 
ATOM   91    C  CA    . GLU A 1 20  ? -55.738 -1.843  67.989  1.00 25.97 ? 40   GLU A CA    1 
ATOM   92    C  C     . GLU A 1 20  ? -55.021 -2.743  68.999  1.00 25.89 ? 40   GLU A C     1 
ATOM   93    O  O     . GLU A 1 20  ? -55.647 -3.608  69.612  1.00 25.83 ? 40   GLU A O     1 
ATOM   94    C  CB    . GLU A 1 20  ? -55.546 -2.399  66.585  1.00 26.34 ? 40   GLU A CB    1 
ATOM   95    C  CG    . GLU A 1 20  ? -56.471 -1.819  65.533  1.00 25.68 ? 40   GLU A CG    1 
ATOM   96    C  CD    . GLU A 1 20  ? -56.093 -2.276  64.135  1.00 26.24 ? 40   GLU A CD    1 
ATOM   97    O  OE1   . GLU A 1 20  ? -54.892 -2.198  63.784  1.00 26.45 ? 40   GLU A OE1   1 
ATOM   98    O  OE2   . GLU A 1 20  ? -56.989 -2.716  63.385  1.00 25.13 ? 40   GLU A OE2   1 
ATOM   99    N  N     . LEU A 1 21  ? -53.717 -2.541  69.171  1.00 25.56 ? 41   LEU A N     1 
ATOM   100   C  CA    . LEU A 1 21  ? -52.969 -3.275  70.173  1.00 25.55 ? 41   LEU A CA    1 
ATOM   101   C  C     . LEU A 1 21  ? -53.602 -3.049  71.557  1.00 26.08 ? 41   LEU A C     1 
ATOM   102   O  O     . LEU A 1 21  ? -53.849 -4.007  72.301  1.00 25.70 ? 41   LEU A O     1 
ATOM   103   C  CB    . LEU A 1 21  ? -51.493 -2.853  70.172  1.00 25.18 ? 41   LEU A CB    1 
ATOM   104   C  CG    . LEU A 1 21  ? -50.641 -3.281  68.966  1.00 24.96 ? 41   LEU A CG    1 
ATOM   105   C  CD1   . LEU A 1 21  ? -49.348 -2.479  68.904  1.00 24.12 ? 41   LEU A CD1   1 
ATOM   106   C  CD2   . LEU A 1 21  ? -50.337 -4.774  69.012  1.00 23.36 ? 41   LEU A CD2   1 
ATOM   107   N  N     . LYS A 1 22  ? -53.863 -1.784  71.888  1.00 26.44 ? 42   LYS A N     1 
ATOM   108   C  CA    . LYS A 1 22  ? -54.501 -1.429  73.158  1.00 26.91 ? 42   LYS A CA    1 
ATOM   109   C  C     . LYS A 1 22  ? -55.882 -2.053  73.282  1.00 27.13 ? 42   LYS A C     1 
ATOM   110   O  O     . LYS A 1 22  ? -56.243 -2.534  74.353  1.00 27.44 ? 42   LYS A O     1 
ATOM   111   C  CB    . LYS A 1 22  ? -54.631 0.090   73.318  1.00 26.87 ? 42   LYS A CB    1 
ATOM   112   C  CG    . LYS A 1 22  ? -53.336 0.812   73.609  1.00 27.69 ? 42   LYS A CG    1 
ATOM   113   C  CD    . LYS A 1 22  ? -53.547 2.329   73.625  1.00 28.73 ? 42   LYS A CD    1 
ATOM   114   C  CE    . LYS A 1 22  ? -52.222 3.082   73.785  1.00 29.26 ? 42   LYS A CE    1 
ATOM   115   N  NZ    . LYS A 1 22  ? -52.355 4.537   73.443  1.00 29.41 ? 42   LYS A NZ    1 
ATOM   116   N  N     . ALA A 1 23  ? -56.650 -2.036  72.196  1.00 27.20 ? 43   ALA A N     1 
ATOM   117   C  CA    . ALA A 1 23  ? -57.995 -2.612  72.205  1.00 27.55 ? 43   ALA A CA    1 
ATOM   118   C  C     . ALA A 1 23  ? -57.972 -4.111  72.491  1.00 28.18 ? 43   ALA A C     1 
ATOM   119   O  O     . ALA A 1 23  ? -58.849 -4.622  73.190  1.00 28.10 ? 43   ALA A O     1 
ATOM   120   C  CB    . ALA A 1 23  ? -58.707 -2.339  70.885  1.00 27.13 ? 43   ALA A CB    1 
ATOM   121   N  N     . VAL A 1 24  ? -56.985 -4.811  71.929  1.00 28.48 ? 44   VAL A N     1 
ATOM   122   C  CA    . VAL A 1 24  ? -56.835 -6.246  72.153  1.00 29.07 ? 44   VAL A CA    1 
ATOM   123   C  C     . VAL A 1 24  ? -56.383 -6.506  73.588  1.00 29.75 ? 44   VAL A C     1 
ATOM   124   O  O     . VAL A 1 24  ? -56.936 -7.361  74.274  1.00 30.12 ? 44   VAL A O     1 
ATOM   125   C  CB    . VAL A 1 24  ? -55.832 -6.905  71.154  1.00 29.12 ? 44   VAL A CB    1 
ATOM   126   C  CG1   . VAL A 1 24  ? -55.473 -8.316  71.604  1.00 28.59 ? 44   VAL A CG1   1 
ATOM   127   C  CG2   . VAL A 1 24  ? -56.412 -6.927  69.726  1.00 28.83 ? 44   VAL A CG2   1 
ATOM   128   N  N     . HIS A 1 25  ? -55.387 -5.753  74.034  1.00 30.35 ? 45   HIS A N     1 
ATOM   129   C  CA    . HIS A 1 25  ? -54.875 -5.880  75.382  1.00 31.45 ? 45   HIS A CA    1 
ATOM   130   C  C     . HIS A 1 25  ? -55.960 -5.603  76.431  1.00 31.59 ? 45   HIS A C     1 
ATOM   131   O  O     . HIS A 1 25  ? -56.047 -6.314  77.433  1.00 31.18 ? 45   HIS A O     1 
ATOM   132   C  CB    . HIS A 1 25  ? -53.693 -4.932  75.579  1.00 31.84 ? 45   HIS A CB    1 
ATOM   133   C  CG    . HIS A 1 25  ? -52.917 -5.195  76.826  1.00 34.47 ? 45   HIS A CG    1 
ATOM   134   N  ND1   . HIS A 1 25  ? -52.337 -4.190  77.566  1.00 38.26 ? 45   HIS A ND1   1 
ATOM   135   C  CD2   . HIS A 1 25  ? -52.631 -6.350  77.470  1.00 37.02 ? 45   HIS A CD2   1 
ATOM   136   C  CE1   . HIS A 1 25  ? -51.720 -4.715  78.610  1.00 38.48 ? 45   HIS A CE1   1 
ATOM   137   N  NE2   . HIS A 1 25  ? -51.883 -6.025  78.573  1.00 37.97 ? 45   HIS A NE2   1 
ATOM   138   N  N     . SER A 1 26  ? -56.775 -4.575  76.185  1.00 31.79 ? 46   SER A N     1 
ATOM   139   C  CA    A SER A 1 26  ? -57.874 -4.218  77.093  0.50 31.96 ? 46   SER A CA    1 
ATOM   140   C  CA    B SER A 1 26  ? -57.881 -4.207  77.076  0.50 32.02 ? 46   SER A CA    1 
ATOM   141   C  C     . SER A 1 26  ? -58.924 -5.317  77.150  1.00 32.03 ? 46   SER A C     1 
ATOM   142   O  O     . SER A 1 26  ? -59.423 -5.650  78.228  1.00 32.09 ? 46   SER A O     1 
ATOM   143   C  CB    A SER A 1 26  ? -58.541 -2.905  76.672  0.50 32.00 ? 46   SER A CB    1 
ATOM   144   C  CB    B SER A 1 26  ? -58.538 -2.909  76.590  0.50 32.08 ? 46   SER A CB    1 
ATOM   145   O  OG    A SER A 1 26  ? -57.719 -1.796  76.977  0.50 31.99 ? 46   SER A OG    1 
ATOM   146   O  OG    B SER A 1 26  ? -59.843 -2.759  77.113  0.50 32.39 ? 46   SER A OG    1 
ATOM   147   N  N     . PHE A 1 27  ? -59.259 -5.873  75.989  1.00 32.06 ? 47   PHE A N     1 
ATOM   148   C  CA    . PHE A 1 27  ? -60.205 -6.972  75.912  1.00 32.18 ? 47   PHE A CA    1 
ATOM   149   C  C     . PHE A 1 27  ? -59.708 -8.182  76.705  1.00 32.40 ? 47   PHE A C     1 
ATOM   150   O  O     . PHE A 1 27  ? -60.475 -8.803  77.441  1.00 32.50 ? 47   PHE A O     1 
ATOM   151   C  CB    . PHE A 1 27  ? -60.457 -7.354  74.457  1.00 32.03 ? 47   PHE A CB    1 
ATOM   152   C  CG    . PHE A 1 27  ? -61.248 -8.620  74.289  1.00 32.03 ? 47   PHE A CG    1 
ATOM   153   C  CD1   . PHE A 1 27  ? -62.630 -8.612  74.417  1.00 32.53 ? 47   PHE A CD1   1 
ATOM   154   C  CD2   . PHE A 1 27  ? -60.612 -9.818  73.990  1.00 31.24 ? 47   PHE A CD2   1 
ATOM   155   C  CE1   . PHE A 1 27  ? -63.360 -9.778  74.266  1.00 32.13 ? 47   PHE A CE1   1 
ATOM   156   C  CE2   . PHE A 1 27  ? -61.330 -10.981 73.836  1.00 31.07 ? 47   PHE A CE2   1 
ATOM   157   C  CZ    . PHE A 1 27  ? -62.710 -10.964 73.972  1.00 32.18 ? 47   PHE A CZ    1 
ATOM   158   N  N     . LEU A 1 28  ? -58.428 -8.513  76.570  1.00 32.66 ? 48   LEU A N     1 
ATOM   159   C  CA    . LEU A 1 28  ? -57.869 -9.623  77.340  1.00 32.95 ? 48   LEU A CA    1 
ATOM   160   C  C     . LEU A 1 28  ? -57.935 -9.320  78.839  1.00 33.56 ? 48   LEU A C     1 
ATOM   161   O  O     . LEU A 1 28  ? -58.355 -10.167 79.634  1.00 33.36 ? 48   LEU A O     1 
ATOM   162   C  CB    . LEU A 1 28  ? -56.439 -9.953  76.892  1.00 32.90 ? 48   LEU A CB    1 
ATOM   163   C  CG    . LEU A 1 28  ? -56.330 -10.557 75.477  1.00 32.37 ? 48   LEU A CG    1 
ATOM   164   C  CD1   . LEU A 1 28  ? -54.871 -10.694 75.043  1.00 31.00 ? 48   LEU A CD1   1 
ATOM   165   C  CD2   . LEU A 1 28  ? -57.039 -11.900 75.392  1.00 29.77 ? 48   LEU A CD2   1 
ATOM   166   N  N     . TRP A 1 29  ? -57.556 -8.104  79.217  1.00 34.35 ? 49   TRP A N     1 
ATOM   167   C  CA    . TRP A 1 29  ? -57.629 -7.686  80.621  1.00 35.29 ? 49   TRP A CA    1 
ATOM   168   C  C     . TRP A 1 29  ? -59.056 -7.633  81.205  1.00 35.59 ? 49   TRP A C     1 
ATOM   169   O  O     . TRP A 1 29  ? -59.219 -7.769  82.411  1.00 35.80 ? 49   TRP A O     1 
ATOM   170   C  CB    . TRP A 1 29  ? -56.902 -6.352  80.830  1.00 35.43 ? 49   TRP A CB    1 
ATOM   171   C  CG    . TRP A 1 29  ? -55.459 -6.566  81.094  1.00 37.02 ? 49   TRP A CG    1 
ATOM   172   C  CD1   . TRP A 1 29  ? -54.557 -7.170  80.262  1.00 38.58 ? 49   TRP A CD1   1 
ATOM   173   C  CD2   . TRP A 1 29  ? -54.745 -6.231  82.283  1.00 37.96 ? 49   TRP A CD2   1 
ATOM   174   N  NE1   . TRP A 1 29  ? -53.320 -7.217  80.859  1.00 39.50 ? 49   TRP A NE1   1 
ATOM   175   C  CE2   . TRP A 1 29  ? -53.405 -6.649  82.099  1.00 38.24 ? 49   TRP A CE2   1 
ATOM   176   C  CE3   . TRP A 1 29  ? -55.102 -5.610  83.485  1.00 39.05 ? 49   TRP A CE3   1 
ATOM   177   C  CZ2   . TRP A 1 29  ? -52.421 -6.464  83.067  1.00 39.14 ? 49   TRP A CZ2   1 
ATOM   178   C  CZ3   . TRP A 1 29  ? -54.124 -5.426  84.450  1.00 39.51 ? 49   TRP A CZ3   1 
ATOM   179   C  CH2   . TRP A 1 29  ? -52.795 -5.853  84.235  1.00 39.77 ? 49   TRP A CH2   1 
ATOM   180   N  N     . SER A 1 30  ? -60.076 -7.468  80.364  1.00 36.04 ? 50   SER A N     1 
ATOM   181   C  CA    . SER A 1 30  ? -61.464 -7.439  80.843  1.00 36.41 ? 50   SER A CA    1 
ATOM   182   C  C     . SER A 1 30  ? -61.990 -8.830  81.230  1.00 37.20 ? 50   SER A C     1 
ATOM   183   O  O     . SER A 1 30  ? -63.016 -8.934  81.907  1.00 37.45 ? 50   SER A O     1 
ATOM   184   C  CB    . SER A 1 30  ? -62.392 -6.790  79.807  1.00 36.31 ? 50   SER A CB    1 
ATOM   185   O  OG    . SER A 1 30  ? -62.726 -7.677  78.753  1.00 35.81 ? 50   SER A OG    1 
ATOM   186   N  N     . LYS A 1 31  ? -61.307 -9.890  80.784  1.00 37.60 ? 51   LYS A N     1 
ATOM   187   C  CA    . LYS A 1 31  ? -61.635 -11.256 81.192  1.00 37.78 ? 51   LYS A CA    1 
ATOM   188   C  C     . LYS A 1 31  ? -60.933 -11.563 82.517  1.00 37.63 ? 51   LYS A C     1 
ATOM   189   O  O     . LYS A 1 31  ? -59.795 -12.036 82.537  1.00 37.49 ? 51   LYS A O     1 
ATOM   190   C  CB    . LYS A 1 31  ? -61.217 -12.267 80.121  1.00 37.94 ? 51   LYS A CB    1 
ATOM   191   C  CG    . LYS A 1 31  ? -61.747 -11.991 78.722  1.00 38.90 ? 51   LYS A CG    1 
ATOM   192   C  CD    . LYS A 1 31  ? -63.257 -11.927 78.686  1.00 40.51 ? 51   LYS A CD    1 
ATOM   193   C  CE    . LYS A 1 31  ? -63.776 -11.847 77.259  1.00 41.21 ? 51   LYS A CE    1 
ATOM   194   N  NZ    . LYS A 1 31  ? -65.235 -11.514 77.214  1.00 41.40 ? 51   LYS A NZ    1 
ATOM   195   N  N     . LYS A 1 32  ? -61.622 -11.285 83.625  1.00 37.52 ? 52   LYS A N     1 
ATOM   196   C  CA    . LYS A 1 32  ? -61.026 -11.395 84.971  1.00 37.30 ? 52   LYS A CA    1 
ATOM   197   C  C     . LYS A 1 32  ? -60.534 -12.802 85.312  1.00 36.75 ? 52   LYS A C     1 
ATOM   198   O  O     . LYS A 1 32  ? -59.616 -12.967 86.118  1.00 36.39 ? 52   LYS A O     1 
ATOM   199   C  CB    . LYS A 1 32  ? -62.020 -10.929 86.048  1.00 37.59 ? 52   LYS A CB    1 
ATOM   200   C  CG    . LYS A 1 32  ? -61.904 -9.458  86.430  1.00 38.00 ? 52   LYS A CG    1 
ATOM   201   C  CD    . LYS A 1 32  ? -61.966 -8.544  85.216  1.00 39.40 ? 52   LYS A CD    1 
ATOM   202   N  N     . GLU A 1 33  ? -61.139 -13.815 84.699  1.00 36.43 ? 53   GLU A N     1 
ATOM   203   C  CA    . GLU A 1 33  ? -60.737 -15.195 84.952  1.00 36.22 ? 53   GLU A CA    1 
ATOM   204   C  C     . GLU A 1 33  ? -59.320 -15.535 84.456  1.00 35.58 ? 53   GLU A C     1 
ATOM   205   O  O     . GLU A 1 33  ? -58.752 -16.537 84.875  1.00 35.33 ? 53   GLU A O     1 
ATOM   206   C  CB    . GLU A 1 33  ? -61.769 -16.179 84.384  1.00 36.39 ? 53   GLU A CB    1 
ATOM   207   C  CG    . GLU A 1 33  ? -61.747 -16.360 82.877  1.00 38.16 ? 53   GLU A CG    1 
ATOM   208   C  CD    . GLU A 1 33  ? -62.491 -15.274 82.114  1.00 39.35 ? 53   GLU A CD    1 
ATOM   209   O  OE1   . GLU A 1 33  ? -62.874 -14.238 82.713  1.00 39.33 ? 53   GLU A OE1   1 
ATOM   210   O  OE2   . GLU A 1 33  ? -62.683 -15.477 80.897  1.00 40.71 ? 53   GLU A OE2   1 
ATOM   211   N  N     . LEU A 1 34  ? -58.754 -14.709 83.574  1.00 34.91 ? 54   LEU A N     1 
ATOM   212   C  CA    . LEU A 1 34  ? -57.391 -14.930 83.077  1.00 34.36 ? 54   LEU A CA    1 
ATOM   213   C  C     . LEU A 1 34  ? -56.339 -14.498 84.090  1.00 34.19 ? 54   LEU A C     1 
ATOM   214   O  O     . LEU A 1 34  ? -55.167 -14.861 83.953  1.00 33.94 ? 54   LEU A O     1 
ATOM   215   C  CB    . LEU A 1 34  ? -57.168 -14.190 81.753  1.00 34.21 ? 54   LEU A CB    1 
ATOM   216   C  CG    . LEU A 1 34  ? -58.071 -14.630 80.600  1.00 33.97 ? 54   LEU A CG    1 
ATOM   217   C  CD1   . LEU A 1 34  ? -57.898 -13.716 79.387  1.00 33.04 ? 54   LEU A CD1   1 
ATOM   218   C  CD2   . LEU A 1 34  ? -57.814 -16.092 80.229  1.00 32.80 ? 54   LEU A CD2   1 
ATOM   219   N  N     . ARG A 1 35  ? -56.754 -13.718 85.095  1.00 33.94 ? 55   ARG A N     1 
ATOM   220   C  CA    . ARG A 1 35  ? -55.865 -13.282 86.175  1.00 33.88 ? 55   ARG A CA    1 
ATOM   221   C  C     . ARG A 1 35  ? -54.563 -12.680 85.629  1.00 33.57 ? 55   ARG A C     1 
ATOM   222   O  O     . ARG A 1 35  ? -53.465 -12.995 86.102  1.00 33.12 ? 55   ARG A O     1 
ATOM   223   C  CB    . ARG A 1 35  ? -55.560 -14.459 87.117  1.00 34.13 ? 55   ARG A CB    1 
ATOM   224   C  CG    . ARG A 1 35  ? -56.777 -15.033 87.833  1.00 35.20 ? 55   ARG A CG    1 
ATOM   225   C  CD    . ARG A 1 35  ? -56.490 -16.413 88.435  1.00 36.77 ? 55   ARG A CD    1 
ATOM   226   N  NE    . ARG A 1 35  ? -55.213 -16.459 89.148  1.00 37.43 ? 55   ARG A NE    1 
ATOM   227   N  N     . LEU A 1 36  ? -54.697 -11.807 84.634  1.00 33.46 ? 56   LEU A N     1 
ATOM   228   C  CA    . LEU A 1 36  ? -53.538 -11.295 83.905  1.00 33.45 ? 56   LEU A CA    1 
ATOM   229   C  C     . LEU A 1 36  ? -52.799 -10.240 84.710  1.00 33.68 ? 56   LEU A C     1 
ATOM   230   O  O     . LEU A 1 36  ? -53.422 -9.370  85.305  1.00 34.27 ? 56   LEU A O     1 
ATOM   231   C  CB    . LEU A 1 36  ? -53.952 -10.720 82.550  1.00 33.03 ? 56   LEU A CB    1 
ATOM   232   C  CG    . LEU A 1 36  ? -54.414 -11.740 81.513  1.00 32.47 ? 56   LEU A CG    1 
ATOM   233   C  CD1   . LEU A 1 36  ? -55.064 -11.039 80.312  1.00 31.08 ? 56   LEU A CD1   1 
ATOM   234   C  CD2   . LEU A 1 36  ? -53.249 -12.614 81.077  1.00 31.60 ? 56   LEU A CD2   1 
ATOM   235   N  N     . GLN A 1 37  ? -51.470 -10.334 84.718  1.00 33.54 ? 57   GLN A N     1 
ATOM   236   C  CA    . GLN A 1 37  ? -50.607 -9.351  85.356  1.00 33.41 ? 57   GLN A CA    1 
ATOM   237   C  C     . GLN A 1 37  ? -49.666 -8.730  84.327  1.00 33.68 ? 57   GLN A C     1 
ATOM   238   O  O     . GLN A 1 37  ? -49.501 -9.276  83.230  1.00 33.47 ? 57   GLN A O     1 
ATOM   239   C  CB    . GLN A 1 37  ? -49.804 -10.015 86.467  1.00 33.45 ? 57   GLN A CB    1 
ATOM   240   C  CG    . GLN A 1 37  ? -50.682 -10.508 87.602  1.00 33.30 ? 57   GLN A CG    1 
ATOM   241   C  CD    . GLN A 1 37  ? -49.897 -11.176 88.694  1.00 32.60 ? 57   GLN A CD    1 
ATOM   242   O  OE1   . GLN A 1 37  ? -48.991 -10.583 89.271  1.00 34.08 ? 57   GLN A OE1   1 
ATOM   243   N  NE2   . GLN A 1 37  ? -50.243 -12.421 88.992  1.00 33.10 ? 57   GLN A NE2   1 
ATOM   244   N  N     . PRO A 1 38  ? -49.051 -7.583  84.670  1.00 33.70 ? 58   PRO A N     1 
ATOM   245   C  CA    . PRO A 1 38  ? -48.101 -6.960  83.756  1.00 33.71 ? 58   PRO A CA    1 
ATOM   246   C  C     . PRO A 1 38  ? -46.851 -7.810  83.550  1.00 33.85 ? 58   PRO A C     1 
ATOM   247   O  O     . PRO A 1 38  ? -46.429 -8.530  84.463  1.00 33.37 ? 58   PRO A O     1 
ATOM   248   C  CB    . PRO A 1 38  ? -47.740 -5.634  84.451  1.00 33.94 ? 58   PRO A CB    1 
ATOM   249   C  CG    . PRO A 1 38  ? -48.791 -5.406  85.487  1.00 33.73 ? 58   PRO A CG    1 
ATOM   250   C  CD    . PRO A 1 38  ? -49.260 -6.774  85.888  1.00 33.94 ? 58   PRO A CD    1 
ATOM   251   N  N     . SER A 1 39  ? -46.262 -7.703  82.359  1.00 34.08 ? 59   SER A N     1 
ATOM   252   C  CA    . SER A 1 39  ? -45.100 -8.506  81.985  1.00 34.57 ? 59   SER A CA    1 
ATOM   253   C  C     . SER A 1 39  ? -43.904 -8.222  82.883  1.00 34.79 ? 59   SER A C     1 
ATOM   254   O  O     . SER A 1 39  ? -43.080 -9.105  83.122  1.00 35.09 ? 59   SER A O     1 
ATOM   255   C  CB    . SER A 1 39  ? -44.715 -8.258  80.520  1.00 34.78 ? 59   SER A CB    1 
ATOM   256   O  OG    . SER A 1 39  ? -44.007 -7.033  80.365  1.00 35.52 ? 59   SER A OG    1 
ATOM   257   N  N     . SER A 1 40  ? -43.825 -6.994  83.392  1.00 34.96 ? 60   SER A N     1 
ATOM   258   C  CA    . SER A 1 40  ? -42.728 -6.583  84.252  1.00 35.00 ? 60   SER A CA    1 
ATOM   259   C  C     . SER A 1 40  ? -42.819 -7.115  85.683  1.00 35.03 ? 60   SER A C     1 
ATOM   260   O  O     . SER A 1 40  ? -41.865 -6.970  86.440  1.00 35.57 ? 60   SER A O     1 
ATOM   261   C  CB    . SER A 1 40  ? -42.633 -5.054  84.288  1.00 35.15 ? 60   SER A CB    1 
ATOM   262   O  OG    . SER A 1 40  ? -43.817 -4.474  84.813  1.00 35.60 ? 60   SER A OG    1 
ATOM   263   N  N     . THR A 1 41  ? -43.948 -7.707  86.069  1.00 34.73 ? 61   THR A N     1 
ATOM   264   C  CA    . THR A 1 41  ? -44.051 -8.340  87.386  1.00 34.62 ? 61   THR A CA    1 
ATOM   265   C  C     . THR A 1 41  ? -42.990 -9.438  87.502  1.00 34.64 ? 61   THR A C     1 
ATOM   266   O  O     . THR A 1 41  ? -42.975 -10.373 86.695  1.00 34.40 ? 61   THR A O     1 
ATOM   267   C  CB    . THR A 1 41  ? -45.433 -8.987  87.611  1.00 34.72 ? 61   THR A CB    1 
ATOM   268   O  OG1   . THR A 1 41  ? -46.467 -8.056  87.278  1.00 35.26 ? 61   THR A OG1   1 
ATOM   269   C  CG2   . THR A 1 41  ? -45.586 -9.439  89.063  1.00 33.89 ? 61   THR A CG2   1 
ATOM   270   N  N     . THR A 1 42  ? -42.124 -9.338  88.508  1.00 34.64 ? 62   THR A N     1 
ATOM   271   C  CA    . THR A 1 42  ? -40.952 -10.221 88.607  1.00 34.79 ? 62   THR A CA    1 
ATOM   272   C  C     . THR A 1 42  ? -41.231 -11.528 89.353  1.00 34.20 ? 62   THR A C     1 
ATOM   273   O  O     . THR A 1 42  ? -40.612 -11.831 90.377  1.00 34.64 ? 62   THR A O     1 
ATOM   274   C  CB    . THR A 1 42  ? -39.740 -9.493  89.241  1.00 34.95 ? 62   THR A CB    1 
ATOM   275   O  OG1   . THR A 1 42  ? -40.169 -8.758  90.392  1.00 36.14 ? 62   THR A OG1   1 
ATOM   276   C  CG2   . THR A 1 42  ? -39.101 -8.530  88.234  1.00 35.89 ? 62   THR A CG2   1 
ATOM   277   N  N     . THR A 1 43  ? -42.174 -12.296 88.819  1.00 33.41 ? 63   THR A N     1 
ATOM   278   C  CA    . THR A 1 43  ? -42.376 -13.689 89.205  1.00 32.24 ? 63   THR A CA    1 
ATOM   279   C  C     . THR A 1 43  ? -42.724 -14.465 87.939  1.00 31.59 ? 63   THR A C     1 
ATOM   280   O  O     . THR A 1 43  ? -43.396 -13.933 87.049  1.00 31.37 ? 63   THR A O     1 
ATOM   281   C  CB    . THR A 1 43  ? -43.516 -13.856 90.243  1.00 32.16 ? 63   THR A CB    1 
ATOM   282   O  OG1   . THR A 1 43  ? -43.701 -15.250 90.530  1.00 32.03 ? 63   THR A OG1   1 
ATOM   283   C  CG2   . THR A 1 43  ? -44.825 -13.276 89.727  1.00 30.87 ? 63   THR A CG2   1 
ATOM   284   N  N     . MET A 1 44  ? -42.270 -15.710 87.863  1.00 30.67 ? 64   MET A N     1 
ATOM   285   C  CA    . MET A 1 44  ? -42.636 -16.592 86.759  1.00 30.28 ? 64   MET A CA    1 
ATOM   286   C  C     . MET A 1 44  ? -44.053 -17.151 86.932  1.00 29.94 ? 64   MET A C     1 
ATOM   287   O  O     . MET A 1 44  ? -44.732 -17.471 85.949  1.00 29.02 ? 64   MET A O     1 
ATOM   288   C  CB    . MET A 1 44  ? -41.632 -17.741 86.632  1.00 30.34 ? 64   MET A CB    1 
ATOM   289   C  CG    . MET A 1 44  ? -40.178 -17.316 86.423  1.00 30.19 ? 64   MET A CG    1 
ATOM   290   S  SD    . MET A 1 44  ? -39.804 -16.575 84.817  1.00 30.37 ? 64   MET A SD    1 
ATOM   291   C  CE    . MET A 1 44  ? -40.468 -14.909 85.001  1.00 30.37 ? 64   MET A CE    1 
ATOM   292   N  N     . ALA A 1 45  ? -44.507 -17.258 88.179  1.00 29.62 ? 65   ALA A N     1 
ATOM   293   C  CA    . ALA A 1 45  ? -45.812 -17.830 88.459  1.00 29.74 ? 65   ALA A CA    1 
ATOM   294   C  C     . ALA A 1 45  ? -46.870 -16.746 88.319  1.00 29.63 ? 65   ALA A C     1 
ATOM   295   O  O     . ALA A 1 45  ? -47.498 -16.358 89.291  1.00 30.11 ? 65   ALA A O     1 
ATOM   296   C  CB    . ALA A 1 45  ? -45.844 -18.472 89.862  1.00 29.46 ? 65   ALA A CB    1 
ATOM   297   N  N     . LYS A 1 46  ? -47.061 -16.278 87.089  1.00 29.57 ? 66   LYS A N     1 
ATOM   298   C  CA    . LYS A 1 46  ? -48.049 -15.256 86.761  1.00 29.19 ? 66   LYS A CA    1 
ATOM   299   C  C     . LYS A 1 46  ? -48.643 -15.571 85.398  1.00 28.58 ? 66   LYS A C     1 
ATOM   300   O  O     . LYS A 1 46  ? -48.011 -16.235 84.585  1.00 28.18 ? 66   LYS A O     1 
ATOM   301   C  CB    . LYS A 1 46  ? -47.393 -13.874 86.708  1.00 29.32 ? 66   LYS A CB    1 
ATOM   302   C  CG    . LYS A 1 46  ? -46.329 -13.761 85.626  1.00 30.38 ? 66   LYS A CG    1 
ATOM   303   C  CD    . LYS A 1 46  ? -45.704 -12.377 85.571  1.00 31.65 ? 66   LYS A CD    1 
ATOM   304   C  CE    . LYS A 1 46  ? -44.616 -12.335 84.503  1.00 32.00 ? 66   LYS A CE    1 
ATOM   305   N  NZ    . LYS A 1 46  ? -43.894 -11.033 84.497  1.00 32.93 ? 66   LYS A NZ    1 
ATOM   306   N  N     . ASN A 1 47  ? -49.851 -15.077 85.158  1.00 28.13 ? 67   ASN A N     1 
ATOM   307   C  CA    . ASN A 1 47  ? -50.456 -15.099 83.835  1.00 27.78 ? 67   ASN A CA    1 
ATOM   308   C  C     . ASN A 1 47  ? -50.220 -13.748 83.139  1.00 27.50 ? 67   ASN A C     1 
ATOM   309   O  O     . ASN A 1 47  ? -50.557 -12.710 83.702  1.00 27.42 ? 67   ASN A O     1 
ATOM   310   C  CB    . ASN A 1 47  ? -51.949 -15.383 83.958  1.00 27.69 ? 67   ASN A CB    1 
ATOM   311   C  CG    . ASN A 1 47  ? -52.247 -16.807 84.417  1.00 27.79 ? 67   ASN A CG    1 
ATOM   312   O  OD1   . ASN A 1 47  ? -51.348 -17.644 84.546  1.00 27.49 ? 67   ASN A OD1   1 
ATOM   313   N  ND2   . ASN A 1 47  ? -53.527 -17.092 84.642  1.00 27.42 ? 67   ASN A ND2   1 
ATOM   314   N  N     . THR A 1 48  ? -49.643 -13.768 81.932  1.00 27.04 ? 68   THR A N     1 
ATOM   315   C  CA    A THR A 1 48  ? -49.294 -12.539 81.210  0.50 26.89 ? 68   THR A CA    1 
ATOM   316   C  CA    B THR A 1 48  ? -49.305 -12.538 81.199  0.50 26.68 ? 68   THR A CA    1 
ATOM   317   C  C     . THR A 1 48  ? -49.497 -12.711 79.700  1.00 26.59 ? 68   THR A C     1 
ATOM   318   O  O     . THR A 1 48  ? -49.381 -13.821 79.176  1.00 26.82 ? 68   THR A O     1 
ATOM   319   C  CB    A THR A 1 48  ? -47.823 -12.127 81.511  0.50 26.93 ? 68   THR A CB    1 
ATOM   320   C  CB    B THR A 1 48  ? -47.836 -12.111 81.430  0.50 26.68 ? 68   THR A CB    1 
ATOM   321   O  OG1   A THR A 1 48  ? -47.632 -10.734 81.233  0.50 27.67 ? 68   THR A OG1   1 
ATOM   322   O  OG1   B THR A 1 48  ? -46.945 -13.107 80.903  0.50 26.51 ? 68   THR A OG1   1 
ATOM   323   C  CG2   A THR A 1 48  ? -46.833 -12.957 80.693  0.50 26.82 ? 68   THR A CG2   1 
ATOM   324   C  CG2   B THR A 1 48  ? -47.561 -11.903 82.905  0.50 26.06 ? 68   THR A CG2   1 
ATOM   325   N  N     . VAL A 1 49  ? -49.797 -11.610 79.012  1.00 25.98 ? 69   VAL A N     1 
ATOM   326   C  CA    . VAL A 1 49  ? -49.890 -11.610 77.562  1.00 25.17 ? 69   VAL A CA    1 
ATOM   327   C  C     . VAL A 1 49  ? -48.493 -11.269 77.020  1.00 24.60 ? 69   VAL A C     1 
ATOM   328   O  O     . VAL A 1 49  ? -47.992 -10.169 77.195  1.00 24.50 ? 69   VAL A O     1 
ATOM   329   C  CB    . VAL A 1 49  ? -50.943 -10.616 77.039  1.00 25.26 ? 69   VAL A CB    1 
ATOM   330   C  CG1   . VAL A 1 49  ? -51.153 -10.808 75.530  1.00 24.89 ? 69   VAL A CG1   1 
ATOM   331   C  CG2   . VAL A 1 49  ? -52.285 -10.777 77.784  1.00 25.12 ? 69   VAL A CG2   1 
ATOM   332   N  N     . PHE A 1 50  ? -47.854 -12.233 76.379  1.00 24.10 ? 70   PHE A N     1 
ATOM   333   C  CA    . PHE A 1 50  ? -46.457 -12.078 75.989  1.00 23.47 ? 70   PHE A CA    1 
ATOM   334   C  C     . PHE A 1 50  ? -46.321 -11.347 74.651  1.00 23.23 ? 70   PHE A C     1 
ATOM   335   O  O     . PHE A 1 50  ? -45.410 -10.523 74.475  1.00 22.81 ? 70   PHE A O     1 
ATOM   336   C  CB    . PHE A 1 50  ? -45.785 -13.436 75.907  1.00 23.13 ? 70   PHE A CB    1 
ATOM   337   C  CG    . PHE A 1 50  ? -44.325 -13.359 75.601  1.00 23.58 ? 70   PHE A CG    1 
ATOM   338   C  CD1   . PHE A 1 50  ? -43.439 -12.861 76.542  1.00 23.47 ? 70   PHE A CD1   1 
ATOM   339   C  CD2   . PHE A 1 50  ? -43.832 -13.782 74.369  1.00 23.62 ? 70   PHE A CD2   1 
ATOM   340   C  CE1   . PHE A 1 50  ? -42.080 -12.787 76.265  1.00 24.88 ? 70   PHE A CE1   1 
ATOM   341   C  CE2   . PHE A 1 50  ? -42.468 -13.710 74.085  1.00 23.10 ? 70   PHE A CE2   1 
ATOM   342   C  CZ    . PHE A 1 50  ? -41.595 -13.218 75.032  1.00 23.33 ? 70   PHE A CZ    1 
ATOM   343   N  N     . LEU A 1 51  ? -47.233 -11.645 73.732  1.00 22.77 ? 71   LEU A N     1 
ATOM   344   C  CA    . LEU A 1 51  ? -47.162 -11.133 72.367  1.00 23.08 ? 71   LEU A CA    1 
ATOM   345   C  C     . LEU A 1 51  ? -48.558 -10.877 71.834  1.00 22.87 ? 71   LEU A C     1 
ATOM   346   O  O     . LEU A 1 51  ? -49.468 -11.675 72.065  1.00 22.49 ? 71   LEU A O     1 
ATOM   347   C  CB    . LEU A 1 51  ? -46.452 -12.149 71.462  1.00 22.98 ? 71   LEU A CB    1 
ATOM   348   C  CG    . LEU A 1 51  ? -46.480 -11.937 69.946  1.00 23.77 ? 71   LEU A CG    1 
ATOM   349   C  CD1   . LEU A 1 51  ? -45.784 -10.633 69.573  1.00 23.92 ? 71   LEU A CD1   1 
ATOM   350   C  CD2   . LEU A 1 51  ? -45.821 -13.119 69.233  1.00 23.79 ? 71   LEU A CD2   1 
ATOM   351   N  N     . ILE A 1 52  ? -48.707 -9.759  71.119  1.00 22.75 ? 72   ILE A N     1 
ATOM   352   C  CA    . ILE A 1 52  ? -49.895 -9.477  70.315  1.00 22.66 ? 72   ILE A CA    1 
ATOM   353   C  C     . ILE A 1 52  ? -49.428 -8.945  68.959  1.00 22.63 ? 72   ILE A C     1 
ATOM   354   O  O     . ILE A 1 52  ? -48.638 -7.992  68.895  1.00 22.13 ? 72   ILE A O     1 
ATOM   355   C  CB    . ILE A 1 52  ? -50.820 -8.400  70.951  1.00 22.81 ? 72   ILE A CB    1 
ATOM   356   C  CG1   . ILE A 1 52  ? -51.276 -8.795  72.358  1.00 22.92 ? 72   ILE A CG1   1 
ATOM   357   C  CG2   . ILE A 1 52  ? -52.035 -8.125  70.052  1.00 22.06 ? 72   ILE A CG2   1 
ATOM   358   C  CD1   . ILE A 1 52  ? -51.884 -7.599  73.139  1.00 22.93 ? 72   ILE A CD1   1 
ATOM   359   N  N     . GLU A 1 53  ? -49.926 -9.556  67.885  1.00 22.49 ? 73   GLU A N     1 
ATOM   360   C  CA    . GLU A 1 53  ? -49.627 -9.103  66.527  1.00 22.44 ? 73   GLU A CA    1 
ATOM   361   C  C     . GLU A 1 53  ? -50.783 -9.476  65.610  1.00 22.58 ? 73   GLU A C     1 
ATOM   362   O  O     . GLU A 1 53  ? -51.609 -10.307 65.963  1.00 22.36 ? 73   GLU A O     1 
ATOM   363   C  CB    . GLU A 1 53  ? -48.307 -9.710  66.026  1.00 22.06 ? 73   GLU A CB    1 
ATOM   364   C  CG    . GLU A 1 53  ? -48.309 -11.235 65.864  1.00 22.07 ? 73   GLU A CG    1 
ATOM   365   C  CD    . GLU A 1 53  ? -46.944 -11.804 65.428  1.00 21.78 ? 73   GLU A CD    1 
ATOM   366   O  OE1   . GLU A 1 53  ? -45.928 -11.093 65.500  1.00 20.31 ? 73   GLU A OE1   1 
ATOM   367   O  OE2   . GLU A 1 53  ? -46.891 -12.971 65.010  1.00 21.91 ? 73   GLU A OE2   1 
ATOM   368   N  N     . MET A 1 54  ? -50.855 -8.838  64.446  1.00 23.02 ? 74   MET A N     1 
ATOM   369   C  CA    . MET A 1 54  ? -51.912 -9.124  63.478  1.00 23.05 ? 74   MET A CA    1 
ATOM   370   C  C     . MET A 1 54  ? -51.787 -10.553 62.949  1.00 23.12 ? 74   MET A C     1 
ATOM   371   O  O     . MET A 1 54  ? -50.683 -11.018 62.650  1.00 22.95 ? 74   MET A O     1 
ATOM   372   C  CB    . MET A 1 54  ? -51.874 -8.133  62.306  1.00 23.13 ? 74   MET A CB    1 
ATOM   373   C  CG    . MET A 1 54  ? -53.042 -8.281  61.337  1.00 23.78 ? 74   MET A CG    1 
ATOM   374   S  SD    . MET A 1 54  ? -52.760 -9.442  59.979  1.00 24.53 ? 74   MET A SD    1 
ATOM   375   C  CE    . MET A 1 54  ? -51.568 -8.543  58.968  1.00 26.73 ? 74   MET A CE    1 
ATOM   376   N  N     . LEU A 1 55  ? -52.941 -11.218 62.820  1.00 22.95 ? 75   LEU A N     1 
ATOM   377   C  CA    . LEU A 1 55  ? -53.041 -12.577 62.333  1.00 22.89 ? 75   LEU A CA    1 
ATOM   378   C  C     . LEU A 1 55  ? -53.665 -12.539 60.944  1.00 23.31 ? 75   LEU A C     1 
ATOM   379   O  O     . LEU A 1 55  ? -54.850 -12.237 60.786  1.00 22.78 ? 75   LEU A O     1 
ATOM   380   C  CB    . LEU A 1 55  ? -53.902 -13.430 63.281  1.00 23.00 ? 75   LEU A CB    1 
ATOM   381   C  CG    . LEU A 1 55  ? -54.170 -14.889 62.878  1.00 23.08 ? 75   LEU A CG    1 
ATOM   382   C  CD1   . LEU A 1 55  ? -52.864 -15.698 62.939  1.00 23.84 ? 75   LEU A CD1   1 
ATOM   383   C  CD2   . LEU A 1 55  ? -55.253 -15.535 63.760  1.00 23.14 ? 75   LEU A CD2   1 
ATOM   384   N  N     . LEU A 1 56  ? -52.855 -12.867 59.942  1.00 23.59 ? 76   LEU A N     1 
ATOM   385   C  CA    . LEU A 1 56  ? -53.281 -12.795 58.556  1.00 24.07 ? 76   LEU A CA    1 
ATOM   386   C  C     . LEU A 1 56  ? -54.531 -13.643 58.307  1.00 23.70 ? 76   LEU A C     1 
ATOM   387   O  O     . LEU A 1 56  ? -54.600 -14.775 58.768  1.00 23.68 ? 76   LEU A O     1 
ATOM   388   C  CB    . LEU A 1 56  ? -52.139 -13.269 57.656  1.00 24.19 ? 76   LEU A CB    1 
ATOM   389   C  CG    . LEU A 1 56  ? -52.182 -12.778 56.222  1.00 25.49 ? 76   LEU A CG    1 
ATOM   390   C  CD1   . LEU A 1 56  ? -52.146 -11.259 56.197  1.00 25.42 ? 76   LEU A CD1   1 
ATOM   391   C  CD2   . LEU A 1 56  ? -51.015 -13.384 55.428  1.00 27.51 ? 76   LEU A CD2   1 
ATOM   392   N  N     . PRO A 1 57  ? -55.525 -13.103 57.582  1.00 23.81 ? 77   PRO A N     1 
ATOM   393   C  CA    . PRO A 1 57  ? -56.666 -13.959 57.232  1.00 24.06 ? 77   PRO A CA    1 
ATOM   394   C  C     . PRO A 1 57  ? -56.273 -15.037 56.231  1.00 24.14 ? 77   PRO A C     1 
ATOM   395   O  O     . PRO A 1 57  ? -55.173 -15.001 55.680  1.00 24.39 ? 77   PRO A O     1 
ATOM   396   C  CB    . PRO A 1 57  ? -57.663 -12.996 56.577  1.00 23.88 ? 77   PRO A CB    1 
ATOM   397   C  CG    . PRO A 1 57  ? -57.133 -11.626 56.799  1.00 23.83 ? 77   PRO A CG    1 
ATOM   398   C  CD    . PRO A 1 57  ? -55.657 -11.761 56.999  1.00 23.80 ? 77   PRO A CD    1 
ATOM   399   N  N     . LYS A 1 58  ? -57.180 -15.970 55.984  1.00 24.30 ? 78   LYS A N     1 
ATOM   400   C  CA    . LYS A 1 58  ? -56.952 -17.015 55.003  1.00 24.87 ? 78   LYS A CA    1 
ATOM   401   C  C     . LYS A 1 58  ? -56.774 -16.432 53.595  1.00 24.89 ? 78   LYS A C     1 
ATOM   402   O  O     . LYS A 1 58  ? -57.480 -15.486 53.195  1.00 25.14 ? 78   LYS A O     1 
ATOM   403   C  CB    . LYS A 1 58  ? -58.107 -18.023 55.021  1.00 25.28 ? 78   LYS A CB    1 
ATOM   404   C  CG    . LYS A 1 58  ? -58.217 -18.799 56.350  1.00 25.56 ? 78   LYS A CG    1 
ATOM   405   C  CD    . LYS A 1 58  ? -59.493 -19.621 56.404  1.00 26.72 ? 78   LYS A CD    1 
ATOM   406   C  CE    . LYS A 1 58  ? -59.474 -20.603 57.568  1.00 27.42 ? 78   LYS A CE    1 
ATOM   407   N  N     . LYS A 1 59  ? -55.833 -17.012 52.853  1.00 24.45 ? 79   LYS A N     1 
ATOM   408   C  CA    . LYS A 1 59  ? -55.524 -16.584 51.482  1.00 24.46 ? 79   LYS A CA    1 
ATOM   409   C  C     . LYS A 1 59  ? -56.747 -16.672 50.579  1.00 24.70 ? 79   LYS A C     1 
ATOM   410   O  O     . LYS A 1 59  ? -56.978 -15.790 49.760  1.00 24.68 ? 79   LYS A O     1 
ATOM   411   C  CB    . LYS A 1 59  ? -54.371 -17.432 50.915  1.00 24.14 ? 79   LYS A CB    1 
ATOM   412   C  CG    . LYS A 1 59  ? -53.899 -17.081 49.491  1.00 23.25 ? 79   LYS A CG    1 
ATOM   413   C  CD    . LYS A 1 59  ? -52.582 -17.838 49.180  1.00 22.17 ? 79   LYS A CD    1 
ATOM   414   C  CE    . LYS A 1 59  ? -52.099 -17.640 47.742  1.00 22.24 ? 79   LYS A CE    1 
ATOM   415   N  NZ    . LYS A 1 59  ? -50.871 -18.445 47.409  1.00 20.43 ? 79   LYS A NZ    1 
ATOM   416   N  N     . TYR A 1 60  ? -57.524 -17.736 50.731  1.00 25.29 ? 80   TYR A N     1 
ATOM   417   C  CA    . TYR A 1 60  ? -58.762 -17.912 49.965  1.00 26.19 ? 80   TYR A CA    1 
ATOM   418   C  C     . TYR A 1 60  ? -59.641 -16.663 50.071  1.00 25.87 ? 80   TYR A C     1 
ATOM   419   O  O     . TYR A 1 60  ? -60.128 -16.142 49.075  1.00 26.16 ? 80   TYR A O     1 
ATOM   420   C  CB    . TYR A 1 60  ? -59.533 -19.140 50.478  1.00 26.67 ? 80   TYR A CB    1 
ATOM   421   C  CG    . TYR A 1 60  ? -60.891 -19.317 49.837  1.00 28.43 ? 80   TYR A CG    1 
ATOM   422   C  CD1   . TYR A 1 60  ? -61.019 -19.925 48.595  1.00 30.50 ? 80   TYR A CD1   1 
ATOM   423   C  CD2   . TYR A 1 60  ? -62.045 -18.858 50.471  1.00 30.98 ? 80   TYR A CD2   1 
ATOM   424   C  CE1   . TYR A 1 60  ? -62.264 -20.079 47.996  1.00 31.73 ? 80   TYR A CE1   1 
ATOM   425   C  CE2   . TYR A 1 60  ? -63.291 -19.004 49.886  1.00 32.32 ? 80   TYR A CE2   1 
ATOM   426   C  CZ    . TYR A 1 60  ? -63.395 -19.619 48.649  1.00 33.39 ? 80   TYR A CZ    1 
ATOM   427   O  OH    . TYR A 1 60  ? -64.635 -19.764 48.068  1.00 37.10 ? 80   TYR A OH    1 
ATOM   428   N  N     . HIS A 1 61  ? -59.805 -16.176 51.290  1.00 26.06 ? 81   HIS A N     1 
ATOM   429   C  CA    . HIS A 1 61  ? -60.665 -15.029 51.560  1.00 26.06 ? 81   HIS A CA    1 
ATOM   430   C  C     . HIS A 1 61  ? -60.034 -13.710 51.115  1.00 25.51 ? 81   HIS A C     1 
ATOM   431   O  O     . HIS A 1 61  ? -60.719 -12.848 50.555  1.00 25.25 ? 81   HIS A O     1 
ATOM   432   C  CB    . HIS A 1 61  ? -60.991 -14.982 53.045  1.00 26.40 ? 81   HIS A CB    1 
ATOM   433   C  CG    . HIS A 1 61  ? -61.870 -16.101 53.497  1.00 28.36 ? 81   HIS A CG    1 
ATOM   434   N  ND1   . HIS A 1 61  ? -63.050 -16.419 52.858  1.00 30.80 ? 81   HIS A ND1   1 
ATOM   435   C  CD2   . HIS A 1 61  ? -61.751 -16.971 54.528  1.00 30.43 ? 81   HIS A CD2   1 
ATOM   436   C  CE1   . HIS A 1 61  ? -63.617 -17.441 53.477  1.00 30.93 ? 81   HIS A CE1   1 
ATOM   437   N  NE2   . HIS A 1 61  ? -62.850 -17.793 54.492  1.00 30.13 ? 81   HIS A NE2   1 
ATOM   438   N  N     . VAL A 1 62  ? -58.735 -13.558 51.375  1.00 24.72 ? 82   VAL A N     1 
ATOM   439   C  CA    . VAL A 1 62  ? -57.994 -12.377 50.950  1.00 24.17 ? 82   VAL A CA    1 
ATOM   440   C  C     . VAL A 1 62  ? -58.068 -12.222 49.430  1.00 24.28 ? 82   VAL A C     1 
ATOM   441   O  O     . VAL A 1 62  ? -58.362 -11.141 48.932  1.00 23.77 ? 82   VAL A O     1 
ATOM   442   C  CB    . VAL A 1 62  ? -56.502 -12.437 51.384  1.00 23.95 ? 82   VAL A CB    1 
ATOM   443   C  CG1   . VAL A 1 62  ? -55.732 -11.250 50.829  1.00 23.37 ? 82   VAL A CG1   1 
ATOM   444   C  CG2   . VAL A 1 62  ? -56.375 -12.491 52.901  1.00 22.19 ? 82   VAL A CG2   1 
ATOM   445   N  N     . LEU A 1 63  ? -57.811 -13.301 48.697  1.00 24.55 ? 83   LEU A N     1 
ATOM   446   C  CA    . LEU A 1 63  ? -57.823 -13.235 47.236  1.00 25.19 ? 83   LEU A CA    1 
ATOM   447   C  C     . LEU A 1 63  ? -59.221 -12.914 46.686  1.00 25.89 ? 83   LEU A C     1 
ATOM   448   O  O     . LEU A 1 63  ? -59.342 -12.179 45.705  1.00 25.88 ? 83   LEU A O     1 
ATOM   449   C  CB    . LEU A 1 63  ? -57.275 -14.525 46.599  1.00 25.08 ? 83   LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 63  ? -55.760 -14.791 46.708  1.00 24.93 ? 83   LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 63  ? -55.370 -15.969 45.828  1.00 23.78 ? 83   LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 63  ? -54.930 -13.573 46.339  1.00 24.61 ? 83   LEU A CD2   1 
ATOM   453   N  N     . ARG A 1 64  ? -60.269 -13.452 47.304  1.00 26.68 ? 84   ARG A N     1 
ATOM   454   C  CA    . ARG A 1 64  ? -61.643 -13.101 46.890  1.00 27.89 ? 84   ARG A CA    1 
ATOM   455   C  C     . ARG A 1 64  ? -61.941 -11.632 47.155  1.00 28.00 ? 84   ARG A C     1 
ATOM   456   O  O     . ARG A 1 64  ? -62.660 -10.990 46.383  1.00 28.13 ? 84   ARG A O     1 
ATOM   457   C  CB    . ARG A 1 64  ? -62.681 -13.998 47.566  1.00 28.06 ? 84   ARG A CB    1 
ATOM   458   C  CG    . ARG A 1 64  ? -62.709 -15.379 46.942  1.00 30.50 ? 84   ARG A CG    1 
ATOM   459   C  CD    . ARG A 1 64  ? -63.421 -16.393 47.804  1.00 34.50 ? 84   ARG A CD    1 
ATOM   460   N  NE    . ARG A 1 64  ? -64.750 -15.939 48.206  1.00 37.90 ? 84   ARG A NE    1 
ATOM   461   C  CZ    . ARG A 1 64  ? -65.809 -15.868 47.401  1.00 39.80 ? 84   ARG A CZ    1 
ATOM   462   N  NH1   . ARG A 1 64  ? -65.721 -16.216 46.119  1.00 40.61 ? 84   ARG A NH1   1 
ATOM   463   N  NH2   . ARG A 1 64  ? -66.969 -15.433 47.887  1.00 41.74 ? 84   ARG A NH2   1 
ATOM   464   N  N     . PHE A 1 65  ? -61.371 -11.106 48.236  1.00 28.14 ? 85   PHE A N     1 
ATOM   465   C  CA    . PHE A 1 65  ? -61.469 -9.684  48.548  1.00 28.56 ? 85   PHE A CA    1 
ATOM   466   C  C     . PHE A 1 65  ? -60.709 -8.877  47.499  1.00 28.46 ? 85   PHE A C     1 
ATOM   467   O  O     . PHE A 1 65  ? -61.260 -7.958  46.898  1.00 28.90 ? 85   PHE A O     1 
ATOM   468   C  CB    . PHE A 1 65  ? -60.924 -9.417  49.953  1.00 28.58 ? 85   PHE A CB    1 
ATOM   469   C  CG    . PHE A 1 65  ? -60.693 -7.963  50.266  1.00 29.68 ? 85   PHE A CG    1 
ATOM   470   C  CD1   . PHE A 1 65  ? -61.746 -7.056  50.257  1.00 30.32 ? 85   PHE A CD1   1 
ATOM   471   C  CD2   . PHE A 1 65  ? -59.422 -7.505  50.590  1.00 30.16 ? 85   PHE A CD2   1 
ATOM   472   C  CE1   . PHE A 1 65  ? -61.535 -5.723  50.559  1.00 30.45 ? 85   PHE A CE1   1 
ATOM   473   C  CE2   . PHE A 1 65  ? -59.204 -6.174  50.890  1.00 30.52 ? 85   PHE A CE2   1 
ATOM   474   C  CZ    . PHE A 1 65  ? -60.265 -5.279  50.882  1.00 30.46 ? 85   PHE A CZ    1 
ATOM   475   N  N     . LEU A 1 66  ? -59.459 -9.255  47.262  1.00 27.91 ? 86   LEU A N     1 
ATOM   476   C  CA    . LEU A 1 66  ? -58.585 -8.534  46.345  1.00 27.68 ? 86   LEU A CA    1 
ATOM   477   C  C     . LEU A 1 66  ? -58.985 -8.648  44.880  1.00 27.51 ? 86   LEU A C     1 
ATOM   478   O  O     . LEU A 1 66  ? -58.937 -7.665  44.159  1.00 27.49 ? 86   LEU A O     1 
ATOM   479   C  CB    . LEU A 1 66  ? -57.134 -9.022  46.485  1.00 27.59 ? 86   LEU A CB    1 
ATOM   480   C  CG    . LEU A 1 66  ? -56.465 -8.849  47.849  1.00 27.08 ? 86   LEU A CG    1 
ATOM   481   C  CD1   . LEU A 1 66  ? -55.061 -9.397  47.784  1.00 26.05 ? 86   LEU A CD1   1 
ATOM   482   C  CD2   . LEU A 1 66  ? -56.469 -7.382  48.284  1.00 25.71 ? 86   LEU A CD2   1 
ATOM   483   N  N     . ASP A 1 67  ? -59.350 -9.842  44.437  1.00 27.76 ? 87   ASP A N     1 
ATOM   484   C  CA    . ASP A 1 67  ? -59.501 -10.108 43.009  1.00 28.01 ? 87   ASP A CA    1 
ATOM   485   C  C     . ASP A 1 67  ? -60.955 -10.221 42.537  1.00 28.67 ? 87   ASP A C     1 
ATOM   486   O  O     . ASP A 1 67  ? -61.203 -10.151 41.338  1.00 28.11 ? 87   ASP A O     1 
ATOM   487   C  CB    . ASP A 1 67  ? -58.769 -11.397 42.620  1.00 27.99 ? 87   ASP A CB    1 
ATOM   488   C  CG    . ASP A 1 67  ? -57.272 -11.379 42.962  1.00 27.89 ? 87   ASP A CG    1 
ATOM   489   O  OD1   . ASP A 1 67  ? -56.705 -10.306 43.264  1.00 26.20 ? 87   ASP A OD1   1 
ATOM   490   O  OD2   . ASP A 1 67  ? -56.660 -12.468 42.912  1.00 27.06 ? 87   ASP A OD2   1 
ATOM   491   N  N     . LYS A 1 68  ? -61.906 -10.426 43.448  1.00 29.65 ? 88   LYS A N     1 
ATOM   492   C  CA    . LYS A 1 68  ? -63.291 -10.740 43.034  1.00 30.78 ? 88   LYS A CA    1 
ATOM   493   C  C     . LYS A 1 68  ? -64.341 -9.839  43.662  1.00 31.23 ? 88   LYS A C     1 
ATOM   494   O  O     . LYS A 1 68  ? -65.527 -10.158 43.608  1.00 31.61 ? 88   LYS A O     1 
ATOM   495   C  CB    . LYS A 1 68  ? -63.656 -12.192 43.369  1.00 31.05 ? 88   LYS A CB    1 
ATOM   496   C  CG    . LYS A 1 68  ? -62.605 -13.222 43.049  1.00 32.73 ? 88   LYS A CG    1 
ATOM   497   C  CD    . LYS A 1 68  ? -62.499 -13.481 41.564  1.00 35.26 ? 88   LYS A CD    1 
ATOM   498   C  CE    . LYS A 1 68  ? -61.607 -14.691 41.287  1.00 37.11 ? 88   LYS A CE    1 
ATOM   499   N  NZ    . LYS A 1 68  ? -62.100 -15.952 41.960  1.00 38.81 ? 88   LYS A NZ    1 
ATOM   500   N  N     . GLY A 1 69  ? -63.918 -8.736  44.271  1.00 31.57 ? 89   GLY A N     1 
ATOM   501   C  CA    . GLY A 1 69  ? -64.843 -7.771  44.839  1.00 31.85 ? 89   GLY A CA    1 
ATOM   502   C  C     . GLY A 1 69  ? -65.603 -8.208  46.081  1.00 32.16 ? 89   GLY A C     1 
ATOM   503   O  O     . GLY A 1 69  ? -66.512 -7.507  46.512  1.00 32.53 ? 89   GLY A O     1 
ATOM   504   N  N     . GLU A 1 70  ? -65.241 -9.341  46.678  1.00 32.39 ? 90   GLU A N     1 
ATOM   505   C  CA    . GLU A 1 70  ? -65.971 -9.844  47.852  1.00 32.45 ? 90   GLU A CA    1 
ATOM   506   C  C     . GLU A 1 70  ? -65.582 -9.064  49.106  1.00 32.23 ? 90   GLU A C     1 
ATOM   507   O  O     . GLU A 1 70  ? -64.720 -8.189  49.054  1.00 32.46 ? 90   GLU A O     1 
ATOM   508   C  CB    . GLU A 1 70  ? -65.745 -11.353 48.033  1.00 32.49 ? 90   GLU A CB    1 
ATOM   509   C  CG    . GLU A 1 70  ? -66.242 -12.199 46.856  1.00 33.44 ? 90   GLU A CG    1 
ATOM   510   C  CD    . GLU A 1 70  ? -67.765 -12.215 46.722  1.00 33.68 ? 90   GLU A CD    1 
ATOM   511   N  N     . ARG A 1 71  ? -66.224 -9.374  50.230  1.00 32.16 ? 91   ARG A N     1 
ATOM   512   C  CA    . ARG A 1 71  ? -66.054 -8.598  51.458  1.00 31.93 ? 91   ARG A CA    1 
ATOM   513   C  C     . ARG A 1 71  ? -64.640 -8.672  52.040  1.00 32.14 ? 91   ARG A C     1 
ATOM   514   O  O     . ARG A 1 71  ? -63.928 -9.663  51.869  1.00 32.03 ? 91   ARG A O     1 
ATOM   515   C  CB    . ARG A 1 71  ? -67.054 -9.064  52.521  1.00 31.78 ? 91   ARG A CB    1 
ATOM   516   N  N     . HIS A 1 72  ? -64.258 -7.606  52.733  1.00 32.34 ? 92   HIS A N     1 
ATOM   517   C  CA    . HIS A 1 72  ? -63.040 -7.561  53.534  1.00 32.63 ? 92   HIS A CA    1 
ATOM   518   C  C     . HIS A 1 72  ? -63.068 -8.728  54.532  1.00 32.21 ? 92   HIS A C     1 
ATOM   519   O  O     . HIS A 1 72  ? -64.085 -8.932  55.206  1.00 32.32 ? 92   HIS A O     1 
ATOM   520   C  CB    . HIS A 1 72  ? -62.983 -6.226  54.292  1.00 32.98 ? 92   HIS A CB    1 
ATOM   521   C  CG    . HIS A 1 72  ? -61.596 -5.747  54.597  1.00 34.82 ? 92   HIS A CG    1 
ATOM   522   N  ND1   . HIS A 1 72  ? -60.764 -6.378  55.499  1.00 36.99 ? 92   HIS A ND1   1 
ATOM   523   C  CD2   . HIS A 1 72  ? -60.909 -4.671  54.144  1.00 36.49 ? 92   HIS A CD2   1 
ATOM   524   C  CE1   . HIS A 1 72  ? -59.620 -5.719  55.575  1.00 37.33 ? 92   HIS A CE1   1 
ATOM   525   N  NE2   . HIS A 1 72  ? -59.681 -4.680  54.763  1.00 37.10 ? 92   HIS A NE2   1 
ATOM   526   N  N     . PRO A 1 73  ? -61.969 -9.508  54.623  1.00 31.32 ? 93   PRO A N     1 
ATOM   527   C  CA    . PRO A 1 73  ? -61.930 -10.550 55.644  1.00 30.61 ? 93   PRO A CA    1 
ATOM   528   C  C     . PRO A 1 73  ? -61.911 -9.961  57.044  1.00 29.74 ? 93   PRO A C     1 
ATOM   529   O  O     . PRO A 1 73  ? -61.440 -8.844  57.233  1.00 29.34 ? 93   PRO A O     1 
ATOM   530   C  CB    . PRO A 1 73  ? -60.606 -11.286 55.355  1.00 30.68 ? 93   PRO A CB    1 
ATOM   531   C  CG    . PRO A 1 73  ? -60.276 -10.951 53.969  1.00 31.06 ? 93   PRO A CG    1 
ATOM   532   C  CD    . PRO A 1 73  ? -60.789 -9.572  53.747  1.00 31.37 ? 93   PRO A CD    1 
ATOM   533   N  N     . VAL A 1 74  ? -62.420 -10.720 58.008  1.00 29.23 ? 94   VAL A N     1 
ATOM   534   C  CA    . VAL A 1 74  ? -62.401 -10.320 59.411  1.00 28.44 ? 94   VAL A CA    1 
ATOM   535   C  C     . VAL A 1 74  ? -60.950 -10.125 59.854  1.00 27.99 ? 94   VAL A C     1 
ATOM   536   O  O     . VAL A 1 74  ? -60.073 -10.923 59.514  1.00 27.77 ? 94   VAL A O     1 
ATOM   537   C  CB    . VAL A 1 74  ? -63.089 -11.373 60.308  1.00 28.73 ? 94   VAL A CB    1 
ATOM   538   C  CG1   . VAL A 1 74  ? -62.863 -11.050 61.780  1.00 29.36 ? 94   VAL A CG1   1 
ATOM   539   C  CG2   . VAL A 1 74  ? -64.600 -11.450 59.990  1.00 28.19 ? 94   VAL A CG2   1 
ATOM   540   N  N     . ARG A 1 75  ? -60.710 -9.040  60.582  1.00 26.93 ? 95   ARG A N     1 
ATOM   541   C  CA    . ARG A 1 75  ? -59.388 -8.707  61.073  1.00 26.20 ? 95   ARG A CA    1 
ATOM   542   C  C     . ARG A 1 75  ? -59.239 -9.230  62.498  1.00 25.63 ? 95   ARG A C     1 
ATOM   543   O  O     . ARG A 1 75  ? -60.130 -9.026  63.342  1.00 25.13 ? 95   ARG A O     1 
ATOM   544   C  CB    . ARG A 1 75  ? -59.188 -7.189  61.018  1.00 26.44 ? 95   ARG A CB    1 
ATOM   545   C  CG    . ARG A 1 75  ? -57.778 -6.710  61.314  1.00 25.79 ? 95   ARG A CG    1 
ATOM   546   C  CD    . ARG A 1 75  ? -57.596 -5.319  60.764  1.00 24.84 ? 95   ARG A CD    1 
ATOM   547   N  NE    . ARG A 1 75  ? -56.441 -4.612  61.310  1.00 23.38 ? 95   ARG A NE    1 
ATOM   548   C  CZ    . ARG A 1 75  ? -55.207 -4.648  60.811  1.00 23.14 ? 95   ARG A CZ    1 
ATOM   549   N  NH1   . ARG A 1 75  ? -54.906 -5.397  59.751  1.00 22.74 ? 95   ARG A NH1   1 
ATOM   550   N  NH2   . ARG A 1 75  ? -54.255 -3.932  61.391  1.00 23.98 ? 95   ARG A NH2   1 
ATOM   551   N  N     . GLU A 1 76  ? -58.122 -9.921  62.747  1.00 24.57 ? 96   GLU A N     1 
ATOM   552   C  CA    . GLU A 1 76  ? -57.840 -10.539 64.042  1.00 23.86 ? 96   GLU A CA    1 
ATOM   553   C  C     . GLU A 1 76  ? -56.412 -10.298 64.494  1.00 23.12 ? 96   GLU A C     1 
ATOM   554   O  O     . GLU A 1 76  ? -55.543 -9.957  63.692  1.00 22.79 ? 96   GLU A O     1 
ATOM   555   C  CB    . GLU A 1 76  ? -58.035 -12.047 63.958  1.00 23.93 ? 96   GLU A CB    1 
ATOM   556   C  CG    . GLU A 1 76  ? -59.387 -12.497 63.470  1.00 24.27 ? 96   GLU A CG    1 
ATOM   557   C  CD    . GLU A 1 76  ? -59.510 -14.010 63.502  1.00 25.36 ? 96   GLU A CD    1 
ATOM   558   O  OE1   . GLU A 1 76  ? -58.669 -14.692 62.878  1.00 24.85 ? 96   GLU A OE1   1 
ATOM   559   O  OE2   . GLU A 1 76  ? -60.432 -14.519 64.165  1.00 25.95 ? 96   GLU A OE2   1 
ATOM   560   N  N     . ALA A 1 77  ? -56.171 -10.524 65.781  1.00 22.43 ? 97   ALA A N     1 
ATOM   561   C  CA    . ALA A 1 77  ? -54.826 -10.459 66.349  1.00 22.17 ? 97   ALA A CA    1 
ATOM   562   C  C     . ALA A 1 77  ? -54.489 -11.796 66.964  1.00 22.17 ? 97   ALA A C     1 
ATOM   563   O  O     . ALA A 1 77  ? -55.338 -12.426 67.594  1.00 22.36 ? 97   ALA A O     1 
ATOM   564   C  CB    . ALA A 1 77  ? -54.724 -9.374  67.418  1.00 21.43 ? 97   ALA A CB    1 
ATOM   565   N  N     . ARG A 1 78  ? -53.243 -12.217 66.783  1.00 21.76 ? 98   ARG A N     1 
ATOM   566   C  CA    . ARG A 1 78  ? -52.687 -13.325 67.537  1.00 21.74 ? 98   ARG A CA    1 
ATOM   567   C  C     . ARG A 1 78  ? -52.313 -12.788 68.916  1.00 21.94 ? 98   ARG A C     1 
ATOM   568   O  O     . ARG A 1 78  ? -51.685 -11.738 69.018  1.00 21.83 ? 98   ARG A O     1 
ATOM   569   C  CB    . ARG A 1 78  ? -51.455 -13.864 66.807  1.00 21.63 ? 98   ARG A CB    1 
ATOM   570   C  CG    . ARG A 1 78  ? -50.614 -14.860 67.575  1.00 22.12 ? 98   ARG A CG    1 
ATOM   571   C  CD    . ARG A 1 78  ? -49.268 -15.042 66.915  1.00 21.25 ? 98   ARG A CD    1 
ATOM   572   N  NE    . ARG A 1 78  ? -48.476 -16.073 67.579  1.00 22.71 ? 98   ARG A NE    1 
ATOM   573   C  CZ    . ARG A 1 78  ? -47.210 -16.358 67.276  1.00 24.31 ? 98   ARG A CZ    1 
ATOM   574   N  NH1   . ARG A 1 78  ? -46.569 -15.660 66.340  1.00 23.71 ? 98   ARG A NH1   1 
ATOM   575   N  NH2   . ARG A 1 78  ? -46.569 -17.327 67.929  1.00 24.35 ? 98   ARG A NH2   1 
ATOM   576   N  N     . ALA A 1 79  ? -52.709 -13.505 69.964  1.00 21.98 ? 99   ALA A N     1 
ATOM   577   C  CA    . ALA A 1 79  ? -52.346 -13.171 71.338  1.00 22.52 ? 99   ALA A CA    1 
ATOM   578   C  C     . ALA A 1 79  ? -51.727 -14.400 71.981  1.00 22.43 ? 99   ALA A C     1 
ATOM   579   O  O     . ALA A 1 79  ? -52.352 -15.447 72.026  1.00 22.93 ? 99   ALA A O     1 
ATOM   580   C  CB    . ALA A 1 79  ? -53.577 -12.750 72.124  1.00 22.78 ? 99   ALA A CB    1 
ATOM   581   N  N     . VAL A 1 80  ? -50.498 -14.276 72.461  1.00 22.73 ? 100  VAL A N     1 
ATOM   582   C  CA    . VAL A 1 80  ? -49.817 -15.381 73.118  1.00 22.63 ? 100  VAL A CA    1 
ATOM   583   C  C     . VAL A 1 80  ? -49.860 -15.125 74.613  1.00 22.99 ? 100  VAL A C     1 
ATOM   584   O  O     . VAL A 1 80  ? -49.335 -14.116 75.091  1.00 22.77 ? 100  VAL A O     1 
ATOM   585   C  CB    . VAL A 1 80  ? -48.357 -15.494 72.669  1.00 22.65 ? 100  VAL A CB    1 
ATOM   586   C  CG1   . VAL A 1 80  ? -47.628 -16.568 73.473  1.00 22.25 ? 100  VAL A CG1   1 
ATOM   587   C  CG2   . VAL A 1 80  ? -48.278 -15.786 71.162  1.00 22.66 ? 100  VAL A CG2   1 
ATOM   588   N  N     . ILE A 1 81  ? -50.487 -16.035 75.347  1.00 23.52 ? 101  ILE A N     1 
ATOM   589   C  CA    . ILE A 1 81  ? -50.607 -15.899 76.800  1.00 24.01 ? 101  ILE A CA    1 
ATOM   590   C  C     . ILE A 1 81  ? -49.772 -16.938 77.533  1.00 24.09 ? 101  ILE A C     1 
ATOM   591   O  O     . ILE A 1 81  ? -49.941 -18.142 77.323  1.00 23.88 ? 101  ILE A O     1 
ATOM   592   C  CB    . ILE A 1 81  ? -52.071 -16.025 77.253  1.00 24.03 ? 101  ILE A CB    1 
ATOM   593   C  CG1   . ILE A 1 81  ? -52.914 -14.932 76.583  1.00 24.67 ? 101  ILE A CG1   1 
ATOM   594   C  CG2   . ILE A 1 81  ? -52.149 -15.923 78.772  1.00 24.42 ? 101  ILE A CG2   1 
ATOM   595   C  CD1   . ILE A 1 81  ? -54.387 -14.975 76.930  1.00 25.78 ? 101  ILE A CD1   1 
ATOM   596   N  N     . PHE A 1 82  ? -48.878 -16.453 78.391  1.00 24.30 ? 102  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 82  ? -48.120 -17.288 79.309  1.00 24.60 ? 102  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 82  ? -48.986 -17.579 80.533  1.00 25.14 ? 102  PHE A C     1 
ATOM   599   O  O     . PHE A 1 82  ? -49.257 -16.680 81.313  1.00 25.70 ? 102  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 82  ? -46.870 -16.540 79.792  1.00 24.22 ? 102  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 82  ? -45.731 -16.504 78.810  1.00 24.11 ? 102  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 82  ? -45.898 -16.830 77.467  1.00 23.62 ? 102  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 82  ? -44.473 -16.101 79.241  1.00 24.61 ? 102  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 82  ? -44.832 -16.785 76.589  1.00 23.61 ? 102  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 82  ? -43.403 -16.048 78.361  1.00 24.23 ? 102  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 82  ? -43.588 -16.392 77.028  1.00 23.97 ? 102  PHE A CZ    1 
ATOM   607   N  N     . PHE A 1 83  ? -49.390 -18.827 80.721  1.00 25.79 ? 103  PHE A N     1 
ATOM   608   C  CA    . PHE A 1 83  ? -50.173 -19.217 81.892  1.00 26.17 ? 103  PHE A CA    1 
ATOM   609   C  C     . PHE A 1 83  ? -49.264 -19.823 82.954  1.00 26.73 ? 103  PHE A C     1 
ATOM   610   O  O     . PHE A 1 83  ? -49.201 -21.035 83.110  1.00 26.44 ? 103  PHE A O     1 
ATOM   611   C  CB    . PHE A 1 83  ? -51.280 -20.202 81.502  1.00 26.07 ? 103  PHE A CB    1 
ATOM   612   C  CG    . PHE A 1 83  ? -52.469 -19.560 80.846  1.00 26.35 ? 103  PHE A CG    1 
ATOM   613   C  CD1   . PHE A 1 83  ? -53.321 -18.738 81.577  1.00 25.88 ? 103  PHE A CD1   1 
ATOM   614   C  CD2   . PHE A 1 83  ? -52.771 -19.809 79.511  1.00 27.04 ? 103  PHE A CD2   1 
ATOM   615   C  CE1   . PHE A 1 83  ? -54.437 -18.165 80.987  1.00 25.66 ? 103  PHE A CE1   1 
ATOM   616   C  CE2   . PHE A 1 83  ? -53.888 -19.231 78.911  1.00 26.68 ? 103  PHE A CE2   1 
ATOM   617   C  CZ    . PHE A 1 83  ? -54.720 -18.404 79.648  1.00 26.23 ? 103  PHE A CZ    1 
ATOM   618   N  N     . GLY A 1 84  ? -48.557 -18.961 83.677  1.00 27.87 ? 104  GLY A N     1 
ATOM   619   C  CA    . GLY A 1 84  ? -47.675 -19.381 84.761  1.00 28.74 ? 104  GLY A CA    1 
ATOM   620   C  C     . GLY A 1 84  ? -48.367 -19.593 86.107  1.00 29.56 ? 104  GLY A C     1 
ATOM   621   O  O     . GLY A 1 84  ? -47.820 -20.286 86.974  1.00 30.15 ? 104  GLY A O     1 
ATOM   622   N  N     . ASP A 1 85  ? -49.569 -19.031 86.274  1.00 30.25 ? 105  ASP A N     1 
ATOM   623   C  CA    . ASP A 1 85  ? -50.236 -18.949 87.587  1.00 31.10 ? 105  ASP A CA    1 
ATOM   624   C  C     . ASP A 1 85  ? -51.226 -20.099 87.767  1.00 31.43 ? 105  ASP A C     1 
ATOM   625   O  O     . ASP A 1 85  ? -52.426 -19.898 87.914  1.00 31.79 ? 105  ASP A O     1 
ATOM   626   C  CB    . ASP A 1 85  ? -50.940 -17.591 87.726  1.00 31.29 ? 105  ASP A CB    1 
ATOM   627   C  CG    . ASP A 1 85  ? -51.414 -17.301 89.142  1.00 32.42 ? 105  ASP A CG    1 
ATOM   628   O  OD1   . ASP A 1 85  ? -50.942 -17.957 90.095  1.00 33.06 ? 105  ASP A OD1   1 
ATOM   629   O  OD2   . ASP A 1 85  ? -52.268 -16.399 89.297  1.00 33.81 ? 105  ASP A OD2   1 
ATOM   630   N  N     . GLN A 1 86  ? -50.698 -21.313 87.737  1.00 31.98 ? 106  GLN A N     1 
ATOM   631   C  CA    . GLN A 1 86  ? -51.504 -22.525 87.819  1.00 32.36 ? 106  GLN A CA    1 
ATOM   632   C  C     . GLN A 1 86  ? -50.555 -23.681 88.058  1.00 32.95 ? 106  GLN A C     1 
ATOM   633   O  O     . GLN A 1 86  ? -49.336 -23.531 87.907  1.00 33.01 ? 106  GLN A O     1 
ATOM   634   C  CB    . GLN A 1 86  ? -52.323 -22.753 86.544  1.00 32.44 ? 106  GLN A CB    1 
ATOM   635   C  CG    . GLN A 1 86  ? -51.495 -22.885 85.241  1.00 32.27 ? 106  GLN A CG    1 
ATOM   636   C  CD    . GLN A 1 86  ? -52.347 -22.761 83.980  1.00 31.72 ? 106  GLN A CD    1 
ATOM   637   O  OE1   . GLN A 1 86  ? -53.236 -21.910 83.898  1.00 32.83 ? 106  GLN A OE1   1 
ATOM   638   N  NE2   . GLN A 1 86  ? -52.066 -23.597 82.987  1.00 30.44 ? 106  GLN A NE2   1 
ATOM   639   N  N     . GLU A 1 87  ? -51.110 -24.824 88.446  1.00 33.38 ? 107  GLU A N     1 
ATOM   640   C  CA    . GLU A 1 87  ? -50.306 -25.999 88.806  1.00 33.53 ? 107  GLU A CA    1 
ATOM   641   C  C     . GLU A 1 87  ? -49.485 -26.544 87.635  1.00 32.89 ? 107  GLU A C     1 
ATOM   642   O  O     . GLU A 1 87  ? -48.337 -26.943 87.809  1.00 32.77 ? 107  GLU A O     1 
ATOM   643   C  CB    . GLU A 1 87  ? -51.224 -27.101 89.323  1.00 34.09 ? 107  GLU A CB    1 
ATOM   644   C  CG    . GLU A 1 87  ? -50.501 -28.277 89.938  1.00 36.18 ? 107  GLU A CG    1 
ATOM   645   C  CD    . GLU A 1 87  ? -51.422 -29.454 90.179  1.00 38.62 ? 107  GLU A CD    1 
ATOM   646   O  OE1   . GLU A 1 87  ? -52.618 -29.390 89.801  1.00 39.96 ? 107  GLU A OE1   1 
ATOM   647   O  OE2   . GLU A 1 87  ? -50.935 -30.450 90.743  1.00 41.20 ? 107  GLU A OE2   1 
ATOM   648   N  N     . HIS A 1 88  ? -50.091 -26.583 86.451  1.00 32.15 ? 108  HIS A N     1 
ATOM   649   C  CA    . HIS A 1 88  ? -49.403 -27.038 85.249  1.00 31.51 ? 108  HIS A CA    1 
ATOM   650   C  C     . HIS A 1 88  ? -49.277 -25.869 84.273  1.00 30.55 ? 108  HIS A C     1 
ATOM   651   O  O     . HIS A 1 88  ? -50.138 -25.676 83.400  1.00 30.37 ? 108  HIS A O     1 
ATOM   652   C  CB    . HIS A 1 88  ? -50.157 -28.204 84.617  1.00 31.60 ? 108  HIS A CB    1 
ATOM   653   C  CG    . HIS A 1 88  ? -50.334 -29.366 85.542  1.00 32.88 ? 108  HIS A CG    1 
ATOM   654   N  ND1   . HIS A 1 88  ? -49.285 -30.169 85.933  1.00 33.42 ? 108  HIS A ND1   1 
ATOM   655   C  CD2   . HIS A 1 88  ? -51.435 -29.854 86.160  1.00 33.28 ? 108  HIS A CD2   1 
ATOM   656   C  CE1   . HIS A 1 88  ? -49.732 -31.102 86.754  1.00 34.61 ? 108  HIS A CE1   1 
ATOM   657   N  NE2   . HIS A 1 88  ? -51.034 -30.937 86.903  1.00 34.97 ? 108  HIS A NE2   1 
ATOM   658   N  N     . PRO A 1 89  ? -48.206 -25.077 84.425  1.00 29.55 ? 109  PRO A N     1 
ATOM   659   C  CA    . PRO A 1 89  ? -48.021 -23.914 83.563  1.00 28.98 ? 109  PRO A CA    1 
ATOM   660   C  C     . PRO A 1 89  ? -48.011 -24.293 82.081  1.00 28.17 ? 109  PRO A C     1 
ATOM   661   O  O     . PRO A 1 89  ? -47.615 -25.390 81.733  1.00 28.04 ? 109  PRO A O     1 
ATOM   662   C  CB    . PRO A 1 89  ? -46.652 -23.373 83.993  1.00 28.93 ? 109  PRO A CB    1 
ATOM   663   C  CG    . PRO A 1 89  ? -46.443 -23.888 85.356  1.00 29.37 ? 109  PRO A CG    1 
ATOM   664   C  CD    . PRO A 1 89  ? -47.095 -25.223 85.383  1.00 29.44 ? 109  PRO A CD    1 
ATOM   665   N  N     . ASN A 1 90  ? -48.493 -23.404 81.224  1.00 27.68 ? 110  ASN A N     1 
ATOM   666   C  CA    . ASN A 1 90  ? -48.395 -23.618 79.785  1.00 27.04 ? 110  ASN A CA    1 
ATOM   667   C  C     . ASN A 1 90  ? -48.440 -22.299 79.019  1.00 26.36 ? 110  ASN A C     1 
ATOM   668   O  O     . ASN A 1 90  ? -48.708 -21.248 79.595  1.00 26.10 ? 110  ASN A O     1 
ATOM   669   C  CB    . ASN A 1 90  ? -49.474 -24.615 79.306  1.00 27.00 ? 110  ASN A CB    1 
ATOM   670   C  CG    . ASN A 1 90  ? -50.857 -23.991 79.136  1.00 27.80 ? 110  ASN A CG    1 
ATOM   671   O  OD1   . ASN A 1 90  ? -51.007 -22.907 78.560  1.00 26.07 ? 110  ASN A OD1   1 
ATOM   672   N  ND2   . ASN A 1 90  ? -51.884 -24.699 79.618  1.00 29.49 ? 110  ASN A ND2   1 
ATOM   673   N  N     . VAL A 1 91  ? -48.141 -22.366 77.727  1.00 25.85 ? 111  VAL A N     1 
ATOM   674   C  CA    . VAL A 1 91  ? -48.364 -21.254 76.816  1.00 25.22 ? 111  VAL A CA    1 
ATOM   675   C  C     . VAL A 1 91  ? -49.529 -21.631 75.920  1.00 25.12 ? 111  VAL A C     1 
ATOM   676   O  O     . VAL A 1 91  ? -49.536 -22.706 75.343  1.00 25.34 ? 111  VAL A O     1 
ATOM   677   C  CB    . VAL A 1 91  ? -47.134 -20.986 75.947  1.00 25.04 ? 111  VAL A CB    1 
ATOM   678   C  CG1   . VAL A 1 91  ? -47.407 -19.849 74.959  1.00 24.00 ? 111  VAL A CG1   1 
ATOM   679   C  CG2   . VAL A 1 91  ? -45.926 -20.677 76.824  1.00 24.46 ? 111  VAL A CG2   1 
ATOM   680   N  N     . THR A 1 92  ? -50.508 -20.746 75.805  1.00 25.08 ? 112  THR A N     1 
ATOM   681   C  CA    . THR A 1 92  ? -51.649 -20.938 74.910  1.00 25.24 ? 112  THR A CA    1 
ATOM   682   C  C     . THR A 1 92  ? -51.796 -19.697 74.043  1.00 24.98 ? 112  THR A C     1 
ATOM   683   O  O     . THR A 1 92  ? -51.639 -18.574 74.538  1.00 25.51 ? 112  THR A O     1 
ATOM   684   C  CB    . THR A 1 92  ? -52.964 -21.103 75.706  1.00 25.44 ? 112  THR A CB    1 
ATOM   685   O  OG1   . THR A 1 92  ? -52.798 -22.112 76.709  1.00 26.83 ? 112  THR A OG1   1 
ATOM   686   C  CG2   . THR A 1 92  ? -54.121 -21.477 74.786  1.00 25.17 ? 112  THR A CG2   1 
ATOM   687   N  N     . GLU A 1 93  ? -52.096 -19.892 72.763  1.00 24.53 ? 113  GLU A N     1 
ATOM   688   C  CA    . GLU A 1 93  ? -52.339 -18.783 71.856  1.00 24.62 ? 113  GLU A CA    1 
ATOM   689   C  C     . GLU A 1 93  ? -53.828 -18.669 71.561  1.00 24.80 ? 113  GLU A C     1 
ATOM   690   O  O     . GLU A 1 93  ? -54.547 -19.661 71.591  1.00 24.89 ? 113  GLU A O     1 
ATOM   691   C  CB    . GLU A 1 93  ? -51.555 -18.950 70.547  1.00 24.30 ? 113  GLU A CB    1 
ATOM   692   C  CG    . GLU A 1 93  ? -50.038 -19.071 70.770  1.00 23.46 ? 113  GLU A CG    1 
ATOM   693   C  CD    . GLU A 1 93  ? -49.221 -18.763 69.532  1.00 22.49 ? 113  GLU A CD    1 
ATOM   694   O  OE1   . GLU A 1 93  ? -49.794 -18.290 68.519  1.00 20.61 ? 113  GLU A OE1   1 
ATOM   695   O  OE2   . GLU A 1 93  ? -47.986 -18.969 69.579  1.00 22.41 ? 113  GLU A OE2   1 
ATOM   696   N  N     . PHE A 1 94  ? -54.276 -17.447 71.295  1.00 24.95 ? 114  PHE A N     1 
ATOM   697   C  CA    . PHE A 1 94  ? -55.649 -17.200 70.859  1.00 25.77 ? 114  PHE A CA    1 
ATOM   698   C  C     . PHE A 1 94  ? -55.653 -16.279 69.660  1.00 25.92 ? 114  PHE A C     1 
ATOM   699   O  O     . PHE A 1 94  ? -54.694 -15.549 69.423  1.00 26.43 ? 114  PHE A O     1 
ATOM   700   C  CB    . PHE A 1 94  ? -56.484 -16.579 71.990  1.00 25.65 ? 114  PHE A CB    1 
ATOM   701   C  CG    . PHE A 1 94  ? -56.540 -17.427 73.236  1.00 26.33 ? 114  PHE A CG    1 
ATOM   702   C  CD1   . PHE A 1 94  ? -55.497 -17.405 74.153  1.00 26.86 ? 114  PHE A CD1   1 
ATOM   703   C  CD2   . PHE A 1 94  ? -57.635 -18.244 73.487  1.00 26.73 ? 114  PHE A CD2   1 
ATOM   704   C  CE1   . PHE A 1 94  ? -55.541 -18.191 75.305  1.00 27.55 ? 114  PHE A CE1   1 
ATOM   705   C  CE2   . PHE A 1 94  ? -57.689 -19.027 74.630  1.00 27.49 ? 114  PHE A CE2   1 
ATOM   706   C  CZ    . PHE A 1 94  ? -56.633 -19.011 75.537  1.00 27.39 ? 114  PHE A CZ    1 
ATOM   707   N  N     . ALA A 1 95  ? -56.730 -16.347 68.890  1.00 26.48 ? 115  ALA A N     1 
ATOM   708   C  CA    . ALA A 1 95  ? -57.031 -15.349 67.882  1.00 26.71 ? 115  ALA A CA    1 
ATOM   709   C  C     . ALA A 1 95  ? -58.119 -14.465 68.466  1.00 27.01 ? 115  ALA A C     1 
ATOM   710   O  O     . ALA A 1 95  ? -59.205 -14.946 68.786  1.00 27.14 ? 115  ALA A O     1 
ATOM   711   C  CB    . ALA A 1 95  ? -57.501 -16.008 66.597  1.00 26.54 ? 115  ALA A CB    1 
ATOM   712   N  N     . VAL A 1 96  ? -57.813 -13.180 68.625  1.00 27.38 ? 116  VAL A N     1 
ATOM   713   C  CA    . VAL A 1 96  ? -58.757 -12.205 69.154  1.00 27.35 ? 116  VAL A CA    1 
ATOM   714   C  C     . VAL A 1 96  ? -59.353 -11.377 68.014  1.00 27.64 ? 116  VAL A C     1 
ATOM   715   O  O     . VAL A 1 96  ? -58.636 -10.860 67.140  1.00 26.92 ? 116  VAL A O     1 
ATOM   716   C  CB    . VAL A 1 96  ? -58.088 -11.275 70.186  1.00 27.33 ? 116  VAL A CB    1 
ATOM   717   C  CG1   . VAL A 1 96  ? -59.097 -10.265 70.734  1.00 26.78 ? 116  VAL A CG1   1 
ATOM   718   C  CG2   . VAL A 1 96  ? -57.466 -12.091 71.312  1.00 27.40 ? 116  VAL A CG2   1 
ATOM   719   N  N     . GLY A 1 97  ? -60.675 -11.260 68.019  1.00 28.01 ? 117  GLY A N     1 
ATOM   720   C  CA    . GLY A 1 97  ? -61.367 -10.463 67.011  1.00 28.43 ? 117  GLY A CA    1 
ATOM   721   C  C     . GLY A 1 97  ? -62.817 -10.197 67.378  1.00 28.66 ? 117  GLY A C     1 
ATOM   722   O  O     . GLY A 1 97  ? -63.258 -10.589 68.458  1.00 28.71 ? 117  GLY A O     1 
ATOM   723   N  N     . PRO A 1 98  ? -63.560 -9.499  66.494  1.00 28.94 ? 118  PRO A N     1 
ATOM   724   C  CA    . PRO A 1 98  ? -63.021 -8.878  65.288  1.00 28.62 ? 118  PRO A CA    1 
ATOM   725   C  C     . PRO A 1 98  ? -62.376 -7.542  65.618  1.00 28.77 ? 118  PRO A C     1 
ATOM   726   O  O     . PRO A 1 98  ? -62.493 -7.047  66.747  1.00 28.31 ? 118  PRO A O     1 
ATOM   727   C  CB    . PRO A 1 98  ? -64.259 -8.676  64.410  1.00 28.82 ? 118  PRO A CB    1 
ATOM   728   C  CG    . PRO A 1 98  ? -65.386 -8.487  65.381  1.00 28.84 ? 118  PRO A CG    1 
ATOM   729   C  CD    . PRO A 1 98  ? -65.006 -9.243  66.645  1.00 29.00 ? 118  PRO A CD    1 
ATOM   730   N  N     . LEU A 1 99  ? -61.675 -6.975  64.643  1.00 28.95 ? 119  LEU A N     1 
ATOM   731   C  CA    . LEU A 1 99  ? -61.098 -5.653  64.798  1.00 29.12 ? 119  LEU A CA    1 
ATOM   732   C  C     . LEU A 1 99  ? -61.660 -4.777  63.689  1.00 29.71 ? 119  LEU A C     1 
ATOM   733   O  O     . LEU A 1 99  ? -61.537 -5.118  62.507  1.00 29.37 ? 119  LEU A O     1 
ATOM   734   C  CB    . LEU A 1 99  ? -59.578 -5.695  64.733  1.00 29.17 ? 119  LEU A CB    1 
ATOM   735   C  CG    . LEU A 1 99  ? -58.843 -6.388  65.882  1.00 29.40 ? 119  LEU A CG    1 
ATOM   736   C  CD1   . LEU A 1 99  ? -57.337 -6.471  65.575  1.00 28.72 ? 119  LEU A CD1   1 
ATOM   737   C  CD2   . LEU A 1 99  ? -59.079 -5.673  67.198  1.00 29.46 ? 119  LEU A CD2   1 
ATOM   738   N  N     . PRO A 1 100 ? -62.295 -3.652  64.058  1.00 30.36 ? 120  PRO A N     1 
ATOM   739   C  CA    . PRO A 1 100 ? -62.493 -3.160  65.423  1.00 30.83 ? 120  PRO A CA    1 
ATOM   740   C  C     . PRO A 1 100 ? -63.576 -3.924  66.201  1.00 31.31 ? 120  PRO A C     1 
ATOM   741   O  O     . PRO A 1 100 ? -64.360 -4.669  65.608  1.00 31.69 ? 120  PRO A O     1 
ATOM   742   C  CB    . PRO A 1 100 ? -62.927 -1.710  65.202  1.00 30.89 ? 120  PRO A CB    1 
ATOM   743   C  CG    . PRO A 1 100 ? -63.645 -1.741  63.879  1.00 30.94 ? 120  PRO A CG    1 
ATOM   744   C  CD    . PRO A 1 100 ? -62.893 -2.752  63.052  1.00 30.49 ? 120  PRO A CD    1 
ATOM   745   N  N     . GLY A 1 101 ? -63.591 -3.730  67.517  1.00 31.76 ? 121  GLY A N     1 
ATOM   746   C  CA    . GLY A 1 101 ? -64.636 -4.258  68.398  1.00 32.22 ? 121  GLY A CA    1 
ATOM   747   C  C     . GLY A 1 101 ? -64.453 -5.702  68.832  1.00 32.46 ? 121  GLY A C     1 
ATOM   748   O  O     . GLY A 1 101 ? -65.325 -6.527  68.586  1.00 32.60 ? 121  GLY A O     1 
ATOM   749   N  N     . PRO A 1 102 ? -63.321 -6.023  69.484  1.00 32.73 ? 122  PRO A N     1 
ATOM   750   C  CA    . PRO A 1 102 ? -63.084 -7.426  69.827  1.00 33.34 ? 122  PRO A CA    1 
ATOM   751   C  C     . PRO A 1 102 ? -64.142 -8.007  70.775  1.00 33.75 ? 122  PRO A C     1 
ATOM   752   O  O     . PRO A 1 102 ? -64.476 -7.369  71.775  1.00 34.16 ? 122  PRO A O     1 
ATOM   753   C  CB    . PRO A 1 102 ? -61.686 -7.409  70.482  1.00 33.17 ? 122  PRO A CB    1 
ATOM   754   C  CG    . PRO A 1 102 ? -61.405 -5.986  70.800  1.00 33.00 ? 122  PRO A CG    1 
ATOM   755   C  CD    . PRO A 1 102 ? -62.172 -5.167  69.824  1.00 32.61 ? 122  PRO A CD    1 
ATOM   756   N  N     A CYS A 1 103 ? -64.674 -9.182  70.421  0.50 34.03 ? 123  CYS A N     1 
ATOM   757   N  N     B CYS A 1 103 ? -64.649 -9.197  70.459  0.50 33.92 ? 123  CYS A N     1 
ATOM   758   C  CA    A CYS A 1 103 ? -65.677 -9.903  71.226  0.50 34.24 ? 123  CYS A CA    1 
ATOM   759   C  CA    B CYS A 1 103 ? -65.638 -9.872  71.306  0.50 34.03 ? 123  CYS A CA    1 
ATOM   760   C  C     A CYS A 1 103 ? -65.236 -11.297 71.669  0.50 34.26 ? 123  CYS A C     1 
ATOM   761   C  C     B CYS A 1 103 ? -65.422 -11.382 71.473  0.50 34.10 ? 123  CYS A C     1 
ATOM   762   O  O     A CYS A 1 103 ? -65.701 -11.790 72.699  0.50 34.40 ? 123  CYS A O     1 
ATOM   763   O  O     B CYS A 1 103 ? -66.256 -12.052 72.088  0.50 34.04 ? 123  CYS A O     1 
ATOM   764   C  CB    A CYS A 1 103 ? -66.973 -10.094 70.438  0.50 34.26 ? 123  CYS A CB    1 
ATOM   765   C  CB    B CYS A 1 103 ? -67.039 -9.647  70.740  0.50 34.05 ? 123  CYS A CB    1 
ATOM   766   S  SG    A CYS A 1 103 ? -67.483 -8.702  69.449  0.50 34.93 ? 123  CYS A SG    1 
ATOM   767   S  SG    B CYS A 1 103 ? -67.385 -10.651 69.283  0.50 34.20 ? 123  CYS A SG    1 
ATOM   768   N  N     . TYR A 1 104 ? -64.351 -11.928 70.900  1.00 34.10 ? 124  TYR A N     1 
ATOM   769   C  CA    . TYR A 1 104 ? -64.004 -13.334 71.102  1.00 34.21 ? 124  TYR A CA    1 
ATOM   770   C  C     . TYR A 1 104 ? -62.497 -13.561 71.184  1.00 34.46 ? 124  TYR A C     1 
ATOM   771   O  O     . TYR A 1 104 ? -61.700 -12.801 70.622  1.00 34.28 ? 124  TYR A O     1 
ATOM   772   C  CB    . TYR A 1 104 ? -64.593 -14.195 69.973  1.00 34.20 ? 124  TYR A CB    1 
ATOM   773   C  CG    . TYR A 1 104 ? -64.040 -13.915 68.580  1.00 34.16 ? 124  TYR A CG    1 
ATOM   774   C  CD1   . TYR A 1 104 ? -62.779 -14.386 68.192  1.00 33.79 ? 124  TYR A CD1   1 
ATOM   775   C  CD2   . TYR A 1 104 ? -64.790 -13.210 67.641  1.00 33.24 ? 124  TYR A CD2   1 
ATOM   776   C  CE1   . TYR A 1 104 ? -62.276 -14.145 66.914  1.00 33.62 ? 124  TYR A CE1   1 
ATOM   777   C  CE2   . TYR A 1 104 ? -64.290 -12.957 66.361  1.00 32.84 ? 124  TYR A CE2   1 
ATOM   778   C  CZ    . TYR A 1 104 ? -63.036 -13.431 66.004  1.00 33.10 ? 124  TYR A CZ    1 
ATOM   779   O  OH    . TYR A 1 104 ? -62.541 -13.182 64.744  1.00 32.27 ? 124  TYR A OH    1 
ATOM   780   N  N     . MET A 1 105 ? -62.125 -14.611 71.910  1.00 34.71 ? 125  MET A N     1 
ATOM   781   C  CA    . MET A 1 105 ? -60.802 -15.192 71.811  1.00 34.79 ? 125  MET A CA    1 
ATOM   782   C  C     . MET A 1 105 ? -60.968 -16.689 71.534  1.00 34.94 ? 125  MET A C     1 
ATOM   783   O  O     . MET A 1 105 ? -61.509 -17.427 72.366  1.00 35.42 ? 125  MET A O     1 
ATOM   784   C  CB    . MET A 1 105 ? -59.978 -14.920 73.069  1.00 34.96 ? 125  MET A CB    1 
ATOM   785   C  CG    . MET A 1 105 ? -60.566 -15.424 74.372  1.00 35.24 ? 125  MET A CG    1 
ATOM   786   S  SD    . MET A 1 105 ? -59.688 -14.738 75.777  1.00 35.99 ? 125  MET A SD    1 
ATOM   787   C  CE    . MET A 1 105 ? -58.136 -15.641 75.725  1.00 35.48 ? 125  MET A CE    1 
ATOM   788   N  N     . ARG A 1 106 ? -60.538 -17.120 70.345  1.00 34.56 ? 126  ARG A N     1 
ATOM   789   C  CA    . ARG A 1 106 ? -60.607 -18.533 69.940  1.00 34.30 ? 126  ARG A CA    1 
ATOM   790   C  C     . ARG A 1 106 ? -59.219 -19.172 69.938  1.00 33.82 ? 126  ARG A C     1 
ATOM   791   O  O     . ARG A 1 106 ? -58.205 -18.477 69.832  1.00 33.64 ? 126  ARG A O     1 
ATOM   792   C  CB    . ARG A 1 106 ? -61.243 -18.675 68.553  1.00 34.33 ? 126  ARG A CB    1 
ATOM   793   C  CG    . ARG A 1 106 ? -60.437 -18.058 67.409  1.00 35.49 ? 126  ARG A CG    1 
ATOM   794   C  CD    . ARG A 1 106 ? -61.175 -18.139 66.067  1.00 36.63 ? 126  ARG A CD    1 
ATOM   795   N  NE    . ARG A 1 106 ? -60.374 -17.558 64.987  1.00 37.20 ? 126  ARG A NE    1 
ATOM   796   C  CZ    . ARG A 1 106 ? -59.349 -18.167 64.389  1.00 38.32 ? 126  ARG A CZ    1 
ATOM   797   N  NH1   . ARG A 1 106 ? -58.983 -19.395 64.748  1.00 38.58 ? 126  ARG A NH1   1 
ATOM   798   N  NH2   . ARG A 1 106 ? -58.676 -17.547 63.423  1.00 38.62 ? 126  ARG A NH2   1 
ATOM   799   N  N     . ALA A 1 107 ? -59.187 -20.501 70.029  1.00 33.12 ? 127  ALA A N     1 
ATOM   800   C  CA    . ALA A 1 107 ? -57.935 -21.255 70.085  1.00 32.69 ? 127  ALA A CA    1 
ATOM   801   C  C     . ALA A 1 107 ? -57.128 -21.050 68.812  1.00 32.24 ? 127  ALA A C     1 
ATOM   802   O  O     . ALA A 1 107 ? -57.687 -20.943 67.721  1.00 32.30 ? 127  ALA A O     1 
ATOM   803   C  CB    . ALA A 1 107 ? -58.205 -22.744 70.307  1.00 32.38 ? 127  ALA A CB    1 
ATOM   804   N  N     . LEU A 1 108 ? -55.813 -20.970 68.965  1.00 31.77 ? 128  LEU A N     1 
ATOM   805   C  CA    . LEU A 1 108 ? -54.919 -20.742 67.839  1.00 31.49 ? 128  LEU A CA    1 
ATOM   806   C  C     . LEU A 1 108 ? -53.707 -21.646 67.993  1.00 31.77 ? 128  LEU A C     1 
ATOM   807   O  O     . LEU A 1 108 ? -53.120 -21.710 69.067  1.00 31.31 ? 128  LEU A O     1 
ATOM   808   C  CB    . LEU A 1 108 ? -54.480 -19.275 67.797  1.00 30.88 ? 128  LEU A CB    1 
ATOM   809   C  CG    . LEU A 1 108 ? -53.639 -18.875 66.583  1.00 30.52 ? 128  LEU A CG    1 
ATOM   810   C  CD1   . LEU A 1 108 ? -54.453 -19.030 65.305  1.00 28.46 ? 128  LEU A CD1   1 
ATOM   811   C  CD2   . LEU A 1 108 ? -53.081 -17.457 66.714  1.00 28.40 ? 128  LEU A CD2   1 
ATOM   812   N  N     . SER A 1 109 ? -53.357 -22.358 66.923  1.00 32.38 ? 129  SER A N     1 
ATOM   813   C  CA    . SER A 1 109 ? -52.232 -23.295 66.943  1.00 32.81 ? 129  SER A CA    1 
ATOM   814   C  C     . SER A 1 109 ? -52.252 -24.212 68.175  1.00 32.53 ? 129  SER A C     1 
ATOM   815   O  O     . SER A 1 109 ? -51.233 -24.364 68.850  1.00 32.53 ? 129  SER A O     1 
ATOM   816   C  CB    . SER A 1 109 ? -50.913 -22.513 66.896  1.00 32.91 ? 129  SER A CB    1 
ATOM   817   O  OG    . SER A 1 109 ? -50.960 -21.502 65.901  1.00 34.79 ? 129  SER A OG    1 
ATOM   818   N  N     . PRO A 1 110 ? -53.417 -24.806 68.490  1.00 32.54 ? 130  PRO A N     1 
ATOM   819   C  CA    . PRO A 1 110 ? -53.447 -25.693 69.651  1.00 32.57 ? 130  PRO A CA    1 
ATOM   820   C  C     . PRO A 1 110 ? -52.605 -26.938 69.389  1.00 32.64 ? 130  PRO A C     1 
ATOM   821   O  O     . PRO A 1 110 ? -52.573 -27.432 68.261  1.00 33.09 ? 130  PRO A O     1 
ATOM   822   C  CB    . PRO A 1 110 ? -54.925 -26.052 69.784  1.00 32.45 ? 130  PRO A CB    1 
ATOM   823   C  CG    . PRO A 1 110 ? -55.467 -25.914 68.400  1.00 32.83 ? 130  PRO A CG    1 
ATOM   824   C  CD    . PRO A 1 110 ? -54.695 -24.812 67.751  1.00 32.43 ? 130  PRO A CD    1 
ATOM   825   N  N     . ARG A 1 111 ? -51.916 -27.420 70.414  1.00 32.42 ? 131  ARG A N     1 
ATOM   826   C  CA    . ARG A 1 111 ? -51.052 -28.588 70.280  1.00 32.46 ? 131  ARG A CA    1 
ATOM   827   C  C     . ARG A 1 111 ? -51.356 -29.558 71.421  1.00 32.65 ? 131  ARG A C     1 
ATOM   828   O  O     . ARG A 1 111 ? -50.509 -29.807 72.278  1.00 32.67 ? 131  ARG A O     1 
ATOM   829   C  CB    . ARG A 1 111 ? -49.576 -28.159 70.280  1.00 32.20 ? 131  ARG A CB    1 
ATOM   830   C  CG    . ARG A 1 111 ? -48.620 -29.225 69.778  1.00 31.65 ? 131  ARG A CG    1 
ATOM   831   C  CD    . ARG A 1 111 ? -47.160 -28.767 69.830  1.00 30.85 ? 131  ARG A CD    1 
ATOM   832   N  NE    . ARG A 1 111 ? -46.256 -29.879 69.533  1.00 30.45 ? 131  ARG A NE    1 
ATOM   833   C  CZ    . ARG A 1 111 ? -44.935 -29.867 69.700  1.00 30.07 ? 131  ARG A CZ    1 
ATOM   834   N  NH1   . ARG A 1 111 ? -44.311 -28.787 70.163  1.00 29.80 ? 131  ARG A NH1   1 
ATOM   835   N  NH2   . ARG A 1 111 ? -44.227 -30.953 69.407  1.00 29.69 ? 131  ARG A NH2   1 
ATOM   836   N  N     . PRO A 1 112 ? -52.585 -30.108 71.438  1.00 32.91 ? 132  PRO A N     1 
ATOM   837   C  CA    . PRO A 1 112 ? -52.987 -30.983 72.538  1.00 33.06 ? 132  PRO A CA    1 
ATOM   838   C  C     . PRO A 1 112 ? -52.125 -32.246 72.619  1.00 33.00 ? 132  PRO A C     1 
ATOM   839   O  O     . PRO A 1 112 ? -51.755 -32.813 71.593  1.00 33.44 ? 132  PRO A O     1 
ATOM   840   C  CB    . PRO A 1 112 ? -54.439 -31.327 72.190  1.00 33.32 ? 132  PRO A CB    1 
ATOM   841   C  CG    . PRO A 1 112 ? -54.492 -31.230 70.708  1.00 32.79 ? 132  PRO A CG    1 
ATOM   842   C  CD    . PRO A 1 112 ? -53.618 -30.049 70.389  1.00 32.86 ? 132  PRO A CD    1 
ATOM   843   N  N     . GLY A 1 113 ? -51.802 -32.667 73.834  1.00 32.89 ? 133  GLY A N     1 
ATOM   844   C  CA    . GLY A 1 113 ? -50.932 -33.819 74.044  1.00 32.80 ? 133  GLY A CA    1 
ATOM   845   C  C     . GLY A 1 113 ? -49.445 -33.507 74.142  1.00 32.49 ? 133  GLY A C     1 
ATOM   846   O  O     . GLY A 1 113 ? -48.644 -34.410 74.407  1.00 33.14 ? 133  GLY A O     1 
ATOM   847   N  N     . TYR A 1 114 ? -49.067 -32.247 73.926  1.00 31.83 ? 134  TYR A N     1 
ATOM   848   C  CA    . TYR A 1 114 ? -47.679 -31.803 74.091  1.00 31.27 ? 134  TYR A CA    1 
ATOM   849   C  C     . TYR A 1 114 ? -47.598 -31.156 75.453  1.00 31.41 ? 134  TYR A C     1 
ATOM   850   O  O     . TYR A 1 114 ? -48.481 -30.386 75.827  1.00 31.35 ? 134  TYR A O     1 
ATOM   851   C  CB    . TYR A 1 114 ? -47.304 -30.804 72.993  1.00 31.05 ? 134  TYR A CB    1 
ATOM   852   C  CG    . TYR A 1 114 ? -45.979 -30.083 73.163  1.00 29.25 ? 134  TYR A CG    1 
ATOM   853   C  CD1   . TYR A 1 114 ? -45.943 -28.707 73.401  1.00 28.14 ? 134  TYR A CD1   1 
ATOM   854   C  CD2   . TYR A 1 114 ? -44.762 -30.758 73.043  1.00 28.28 ? 134  TYR A CD2   1 
ATOM   855   C  CE1   . TYR A 1 114 ? -44.741 -28.023 73.534  1.00 26.74 ? 134  TYR A CE1   1 
ATOM   856   C  CE2   . TYR A 1 114 ? -43.538 -30.073 73.171  1.00 27.52 ? 134  TYR A CE2   1 
ATOM   857   C  CZ    . TYR A 1 114 ? -43.540 -28.710 73.419  1.00 26.77 ? 134  TYR A CZ    1 
ATOM   858   O  OH    . TYR A 1 114 ? -42.353 -28.017 73.545  1.00 26.66 ? 134  TYR A OH    1 
ATOM   859   N  N     . GLN A 1 115 ? -46.546 -31.468 76.196  1.00 31.46 ? 135  GLN A N     1 
ATOM   860   C  CA    . GLN A 1 115 ? -46.474 -31.084 77.598  1.00 31.63 ? 135  GLN A CA    1 
ATOM   861   C  C     . GLN A 1 115 ? -45.353 -30.100 77.934  1.00 31.25 ? 135  GLN A C     1 
ATOM   862   O  O     . GLN A 1 115 ? -45.318 -29.577 79.049  1.00 31.45 ? 135  GLN A O     1 
ATOM   863   C  CB    . GLN A 1 115 ? -46.344 -32.345 78.463  1.00 31.88 ? 135  GLN A CB    1 
ATOM   864   C  CG    . GLN A 1 115 ? -47.607 -33.215 78.476  1.00 32.39 ? 135  GLN A CG    1 
ATOM   865   C  CD    . GLN A 1 115 ? -47.762 -34.016 79.764  1.00 33.64 ? 135  GLN A CD    1 
ATOM   866   N  N     . SER A 1 116 ? -44.464 -29.818 76.981  1.00 30.50 ? 136  SER A N     1 
ATOM   867   C  CA    . SER A 1 116 ? -43.309 -28.969 77.253  1.00 29.92 ? 136  SER A CA    1 
ATOM   868   C  C     . SER A 1 116 ? -43.491 -27.506 76.819  1.00 29.15 ? 136  SER A C     1 
ATOM   869   O  O     . SER A 1 116 ? -42.497 -26.800 76.625  1.00 29.21 ? 136  SER A O     1 
ATOM   870   C  CB    . SER A 1 116 ? -42.058 -29.556 76.592  1.00 29.87 ? 136  SER A CB    1 
ATOM   871   O  OG    . SER A 1 116 ? -41.687 -30.775 77.199  1.00 30.79 ? 136  SER A OG    1 
ATOM   872   N  N     . SER A 1 117 ? -44.727 -27.023 76.686  1.00 28.21 ? 137  SER A N     1 
ATOM   873   C  CA    . SER A 1 117 ? -44.913 -25.654 76.178  1.00 27.31 ? 137  SER A CA    1 
ATOM   874   C  C     . SER A 1 117 ? -44.288 -24.604 77.099  1.00 26.85 ? 137  SER A C     1 
ATOM   875   O  O     . SER A 1 117 ? -43.683 -23.641 76.613  1.00 26.71 ? 137  SER A O     1 
ATOM   876   C  CB    . SER A 1 117 ? -46.378 -25.330 75.884  1.00 27.34 ? 137  SER A CB    1 
ATOM   877   O  OG    . SER A 1 117 ? -47.162 -25.271 77.050  1.00 26.89 ? 137  SER A OG    1 
ATOM   878   N  N     . TRP A 1 118 ? -44.389 -24.797 78.415  1.00 26.09 ? 138  TRP A N     1 
ATOM   879   C  CA    . TRP A 1 118 ? -43.821 -23.824 79.345  1.00 25.75 ? 138  TRP A CA    1 
ATOM   880   C  C     . TRP A 1 118 ? -42.303 -23.762 79.168  1.00 25.30 ? 138  TRP A C     1 
ATOM   881   O  O     . TRP A 1 118 ? -41.741 -22.668 79.045  1.00 25.19 ? 138  TRP A O     1 
ATOM   882   C  CB    . TRP A 1 118 ? -44.211 -24.119 80.807  1.00 25.71 ? 138  TRP A CB    1 
ATOM   883   C  CG    . TRP A 1 118 ? -43.872 -22.998 81.767  1.00 24.76 ? 138  TRP A CG    1 
ATOM   884   C  CD1   . TRP A 1 118 ? -42.892 -23.004 82.724  1.00 24.95 ? 138  TRP A CD1   1 
ATOM   885   C  CD2   . TRP A 1 118 ? -44.497 -21.714 81.850  1.00 24.75 ? 138  TRP A CD2   1 
ATOM   886   N  NE1   . TRP A 1 118 ? -42.876 -21.810 83.399  1.00 24.08 ? 138  TRP A NE1   1 
ATOM   887   C  CE2   . TRP A 1 118 ? -43.851 -20.999 82.885  1.00 25.11 ? 138  TRP A CE2   1 
ATOM   888   C  CE3   . TRP A 1 118 ? -45.550 -21.097 81.156  1.00 25.77 ? 138  TRP A CE3   1 
ATOM   889   C  CZ2   . TRP A 1 118 ? -44.218 -19.698 83.239  1.00 24.34 ? 138  TRP A CZ2   1 
ATOM   890   C  CZ3   . TRP A 1 118 ? -45.919 -19.805 81.514  1.00 25.03 ? 138  TRP A CZ3   1 
ATOM   891   C  CH2   . TRP A 1 118 ? -45.254 -19.122 82.545  1.00 25.47 ? 138  TRP A CH2   1 
ATOM   892   N  N     . ALA A 1 119 ? -41.649 -24.925 79.119  1.00 24.53 ? 139  ALA A N     1 
ATOM   893   C  CA    . ALA A 1 119 ? -40.197 -24.965 78.911  1.00 24.45 ? 139  ALA A CA    1 
ATOM   894   C  C     . ALA A 1 119 ? -39.789 -24.377 77.546  1.00 24.15 ? 139  ALA A C     1 
ATOM   895   O  O     . ALA A 1 119 ? -38.679 -23.853 77.400  1.00 23.87 ? 139  ALA A O     1 
ATOM   896   C  CB    . ALA A 1 119 ? -39.663 -26.387 79.067  1.00 24.68 ? 139  ALA A CB    1 
ATOM   897   N  N     . SER A 1 120 ? -40.686 -24.446 76.561  1.00 23.64 ? 140  SER A N     1 
ATOM   898   C  CA    . SER A 1 120 ? -40.383 -23.944 75.214  1.00 23.67 ? 140  SER A CA    1 
ATOM   899   C  C     . SER A 1 120 ? -40.476 -22.423 75.088  1.00 23.29 ? 140  SER A C     1 
ATOM   900   O  O     . SER A 1 120 ? -40.025 -21.871 74.101  1.00 23.50 ? 140  SER A O     1 
ATOM   901   C  CB    . SER A 1 120 ? -41.327 -24.552 74.178  1.00 23.46 ? 140  SER A CB    1 
ATOM   902   O  OG    . SER A 1 120 ? -42.601 -23.921 74.213  1.00 23.65 ? 140  SER A OG    1 
ATOM   903   N  N     . ARG A 1 121 ? -41.087 -21.758 76.066  1.00 22.95 ? 141  ARG A N     1 
ATOM   904   C  CA    . ARG A 1 121 ? -41.423 -20.345 75.928  1.00 22.79 ? 141  ARG A CA    1 
ATOM   905   C  C     . ARG A 1 121 ? -40.162 -19.474 75.885  1.00 22.54 ? 141  ARG A C     1 
ATOM   906   O  O     . ARG A 1 121 ? -39.132 -19.837 76.468  1.00 21.92 ? 141  ARG A O     1 
ATOM   907   C  CB    . ARG A 1 121 ? -42.384 -19.887 77.043  1.00 23.01 ? 141  ARG A CB    1 
ATOM   908   C  CG    . ARG A 1 121 ? -41.718 -19.408 78.316  1.00 22.78 ? 141  ARG A CG    1 
ATOM   909   C  CD    . ARG A 1 121 ? -42.677 -19.358 79.493  1.00 24.45 ? 141  ARG A CD    1 
ATOM   910   N  NE    . ARG A 1 121 ? -41.985 -18.883 80.695  1.00 24.19 ? 141  ARG A NE    1 
ATOM   911   C  CZ    . ARG A 1 121 ? -41.172 -19.622 81.449  1.00 23.97 ? 141  ARG A CZ    1 
ATOM   912   N  NH1   . ARG A 1 121 ? -40.951 -20.893 81.155  1.00 23.50 ? 141  ARG A NH1   1 
ATOM   913   N  NH2   . ARG A 1 121 ? -40.580 -19.087 82.516  1.00 24.48 ? 141  ARG A NH2   1 
ATOM   914   N  N     . PRO A 1 122 ? -40.238 -18.331 75.175  1.00 22.52 ? 142  PRO A N     1 
ATOM   915   C  CA    . PRO A 1 122 ? -39.133 -17.378 75.166  1.00 22.67 ? 142  PRO A CA    1 
ATOM   916   C  C     . PRO A 1 122 ? -38.806 -16.857 76.550  1.00 23.26 ? 142  PRO A C     1 
ATOM   917   O  O     . PRO A 1 122 ? -39.677 -16.831 77.443  1.00 22.79 ? 142  PRO A O     1 
ATOM   918   C  CB    . PRO A 1 122 ? -39.671 -16.227 74.308  1.00 22.59 ? 142  PRO A CB    1 
ATOM   919   C  CG    . PRO A 1 122 ? -40.635 -16.876 73.395  1.00 21.85 ? 142  PRO A CG    1 
ATOM   920   C  CD    . PRO A 1 122 ? -41.302 -17.924 74.234  1.00 22.38 ? 142  PRO A CD    1 
ATOM   921   N  N     . ILE A 1 123 ? -37.554 -16.448 76.712  1.00 23.47 ? 143  ILE A N     1 
ATOM   922   C  CA    . ILE A 1 123 ? -37.114 -15.766 77.912  1.00 24.11 ? 143  ILE A CA    1 
ATOM   923   C  C     . ILE A 1 123 ? -37.753 -14.372 77.940  1.00 24.66 ? 143  ILE A C     1 
ATOM   924   O  O     . ILE A 1 123 ? -38.272 -13.903 76.935  1.00 24.37 ? 143  ILE A O     1 
ATOM   925   C  CB    . ILE A 1 123 ? -35.574 -15.690 77.962  1.00 24.17 ? 143  ILE A CB    1 
ATOM   926   C  CG1   . ILE A 1 123 ? -35.080 -15.348 79.375  1.00 24.30 ? 143  ILE A CG1   1 
ATOM   927   C  CG2   . ILE A 1 123 ? -35.057 -14.682 76.929  1.00 24.35 ? 143  ILE A CG2   1 
ATOM   928   C  CD1   . ILE A 1 123 ? -33.785 -16.016 79.741  1.00 24.00 ? 143  ILE A CD1   1 
ATOM   929   N  N     . SER A 1 124 ? -37.737 -13.729 79.104  1.00 25.36 ? 144  SER A N     1 
ATOM   930   C  CA    . SER A 1 124 ? -38.385 -12.433 79.283  1.00 25.43 ? 144  SER A CA    1 
ATOM   931   C  C     . SER A 1 124 ? -37.583 -11.562 80.241  1.00 25.89 ? 144  SER A C     1 
ATOM   932   O  O     . SER A 1 124 ? -36.719 -12.052 80.976  1.00 25.87 ? 144  SER A O     1 
ATOM   933   C  CB    . SER A 1 124 ? -39.814 -12.626 79.807  1.00 25.52 ? 144  SER A CB    1 
ATOM   934   O  OG    . SER A 1 124 ? -39.811 -13.221 81.091  1.00 24.80 ? 144  SER A OG    1 
ATOM   935   N  N     . THR A 1 125 ? -37.866 -10.266 80.218  1.00 26.45 ? 145  THR A N     1 
ATOM   936   C  CA    . THR A 1 125 ? -37.199 -9.318  81.110  1.00 26.67 ? 145  THR A CA    1 
ATOM   937   C  C     . THR A 1 125 ? -37.354 -9.712  82.580  1.00 26.63 ? 145  THR A C     1 
ATOM   938   O  O     . THR A 1 125 ? -36.389 -9.657  83.348  1.00 26.80 ? 145  THR A O     1 
ATOM   939   C  CB    . THR A 1 125 ? -37.706 -7.887  80.868  1.00 26.62 ? 145  THR A CB    1 
ATOM   940   O  OG1   . THR A 1 125 ? -37.283 -7.472  79.568  1.00 27.73 ? 145  THR A OG1   1 
ATOM   941   C  CG2   . THR A 1 125 ? -37.133 -6.915  81.882  1.00 26.92 ? 145  THR A CG2   1 
ATOM   942   N  N     . ALA A 1 126 ? -38.553 -10.133 82.969  1.00 26.51 ? 146  ALA A N     1 
ATOM   943   C  CA    . ALA A 1 126 ? -38.786 -10.548 84.358  1.00 26.42 ? 146  ALA A CA    1 
ATOM   944   C  C     . ALA A 1 126 ? -37.866 -11.716 84.717  1.00 26.39 ? 146  ALA A C     1 
ATOM   945   O  O     . ALA A 1 126 ? -37.270 -11.741 85.797  1.00 26.06 ? 146  ALA A O     1 
ATOM   946   C  CB    . ALA A 1 126 ? -40.255 -10.916 84.579  1.00 25.97 ? 146  ALA A CB    1 
ATOM   947   N  N     . GLU A 1 127 ? -37.739 -12.665 83.787  1.00 26.52 ? 147  GLU A N     1 
ATOM   948   C  CA    . GLU A 1 127 ? -36.919 -13.847 84.005  1.00 26.40 ? 147  GLU A CA    1 
ATOM   949   C  C     . GLU A 1 127 ? -35.456 -13.463 84.122  1.00 26.30 ? 147  GLU A C     1 
ATOM   950   O  O     . GLU A 1 127 ? -34.748 -13.989 84.978  1.00 27.03 ? 147  GLU A O     1 
ATOM   951   C  CB    . GLU A 1 127 ? -37.118 -14.878 82.881  1.00 26.40 ? 147  GLU A CB    1 
ATOM   952   C  CG    . GLU A 1 127 ? -36.560 -16.262 83.210  1.00 26.38 ? 147  GLU A CG    1 
ATOM   953   C  CD    . GLU A 1 127 ? -36.997 -17.346 82.239  1.00 26.12 ? 147  GLU A CD    1 
ATOM   954   O  OE1   . GLU A 1 127 ? -37.557 -17.014 81.170  1.00 25.68 ? 147  GLU A OE1   1 
ATOM   955   O  OE2   . GLU A 1 127 ? -36.775 -18.537 82.547  1.00 25.06 ? 147  GLU A OE2   1 
ATOM   956   N  N     . TYR A 1 128 ? -35.002 -12.540 83.278  1.00 26.01 ? 148  TYR A N     1 
ATOM   957   C  CA    . TYR A 1 128 ? -33.621 -12.070 83.359  1.00 26.08 ? 148  TYR A CA    1 
ATOM   958   C  C     . TYR A 1 128 ? -33.319 -11.434 84.720  1.00 26.40 ? 148  TYR A C     1 
ATOM   959   O  O     . TYR A 1 128 ? -32.251 -11.680 85.300  1.00 26.35 ? 148  TYR A O     1 
ATOM   960   C  CB    . TYR A 1 128 ? -33.306 -11.060 82.247  1.00 25.90 ? 148  TYR A CB    1 
ATOM   961   C  CG    . TYR A 1 128 ? -32.883 -11.675 80.934  1.00 25.48 ? 148  TYR A CG    1 
ATOM   962   C  CD1   . TYR A 1 128 ? -31.700 -12.410 80.837  1.00 26.43 ? 148  TYR A CD1   1 
ATOM   963   C  CD2   . TYR A 1 128 ? -33.634 -11.489 79.778  1.00 25.42 ? 148  TYR A CD2   1 
ATOM   964   C  CE1   . TYR A 1 128 ? -31.295 -12.966 79.637  1.00 25.37 ? 148  TYR A CE1   1 
ATOM   965   C  CE2   . TYR A 1 128 ? -33.231 -12.034 78.567  1.00 24.73 ? 148  TYR A CE2   1 
ATOM   966   C  CZ    . TYR A 1 128 ? -32.055 -12.766 78.508  1.00 24.94 ? 148  TYR A CZ    1 
ATOM   967   O  OH    . TYR A 1 128 ? -31.653 -13.312 77.325  1.00 23.51 ? 148  TYR A OH    1 
ATOM   968   N  N     . ALA A 1 129 ? -34.242 -10.605 85.210  1.00 26.54 ? 149  ALA A N     1 
ATOM   969   C  CA    . ALA A 1 129 ? -34.077 -9.957  86.517  1.00 27.23 ? 149  ALA A CA    1 
ATOM   970   C  C     . ALA A 1 129 ? -33.892 -11.011 87.608  1.00 27.57 ? 149  ALA A C     1 
ATOM   971   O  O     . ALA A 1 129 ? -32.973 -10.916 88.415  1.00 27.97 ? 149  ALA A O     1 
ATOM   972   C  CB    . ALA A 1 129 ? -35.271 -9.061  86.840  1.00 26.71 ? 149  ALA A CB    1 
ATOM   973   N  N     . LEU A 1 130 ? -34.756 -12.022 87.611  1.00 27.83 ? 150  LEU A N     1 
ATOM   974   C  CA    . LEU A 1 130 ? -34.640 -13.114 88.576  1.00 27.88 ? 150  LEU A CA    1 
ATOM   975   C  C     . LEU A 1 130 ? -33.336 -13.900 88.383  1.00 28.33 ? 150  LEU A C     1 
ATOM   976   O  O     . LEU A 1 130 ? -32.728 -14.340 89.356  1.00 28.25 ? 150  LEU A O     1 
ATOM   977   C  CB    . LEU A 1 130 ? -35.844 -14.041 88.484  1.00 27.58 ? 150  LEU A CB    1 
ATOM   978   C  CG    . LEU A 1 130 ? -37.194 -13.437 88.883  1.00 26.71 ? 150  LEU A CG    1 
ATOM   979   C  CD1   . LEU A 1 130 ? -38.323 -14.325 88.419  1.00 25.95 ? 150  LEU A CD1   1 
ATOM   980   C  CD2   . LEU A 1 130 ? -37.282 -13.213 90.394  1.00 25.53 ? 150  LEU A CD2   1 
ATOM   981   N  N     . LEU A 1 131 ? -32.895 -14.067 87.138  1.00 28.75 ? 151  LEU A N     1 
ATOM   982   C  CA    . LEU A 1 131 ? -31.618 -14.746 86.890  1.00 29.02 ? 151  LEU A CA    1 
ATOM   983   C  C     . LEU A 1 131 ? -30.477 -13.959 87.511  1.00 29.45 ? 151  LEU A C     1 
ATOM   984   O  O     . LEU A 1 131 ? -29.584 -14.532 88.147  1.00 29.46 ? 151  LEU A O     1 
ATOM   985   C  CB    . LEU A 1 131 ? -31.346 -14.934 85.390  1.00 28.98 ? 151  LEU A CB    1 
ATOM   986   C  CG    . LEU A 1 131 ? -31.968 -16.139 84.687  1.00 28.72 ? 151  LEU A CG    1 
ATOM   987   C  CD1   . LEU A 1 131 ? -31.712 -16.060 83.182  1.00 29.06 ? 151  LEU A CD1   1 
ATOM   988   C  CD2   . LEU A 1 131 ? -31.407 -17.434 85.251  1.00 27.42 ? 151  LEU A CD2   1 
ATOM   989   N  N     . TYR A 1 132 ? -30.503 -12.644 87.326  1.00 29.86 ? 152  TYR A N     1 
ATOM   990   C  CA    . TYR A 1 132 ? -29.465 -11.809 87.886  1.00 30.31 ? 152  TYR A CA    1 
ATOM   991   C  C     . TYR A 1 132 ? -29.481 -11.917 89.422  1.00 30.63 ? 152  TYR A C     1 
ATOM   992   O  O     . TYR A 1 132 ? -28.427 -11.962 90.051  1.00 30.36 ? 152  TYR A O     1 
ATOM   993   C  CB    . TYR A 1 132 ? -29.593 -10.354 87.410  1.00 30.42 ? 152  TYR A CB    1 
ATOM   994   C  CG    . TYR A 1 132 ? -28.249 -9.679  87.181  1.00 30.64 ? 152  TYR A CG    1 
ATOM   995   N  N     . HIS A 1 133 ? -30.672 -11.992 90.011  1.00 31.00 ? 153  HIS A N     1 
ATOM   996   C  CA    . HIS A 1 133 ? -30.804 -12.180 91.463  1.00 31.40 ? 153  HIS A CA    1 
ATOM   997   C  C     . HIS A 1 133 ? -30.219 -13.519 91.901  1.00 31.61 ? 153  HIS A C     1 
ATOM   998   O  O     . HIS A 1 133 ? -29.489 -13.586 92.901  1.00 31.67 ? 153  HIS A O     1 
ATOM   999   C  CB    . HIS A 1 133 ? -32.270 -12.089 91.899  1.00 31.46 ? 153  HIS A CB    1 
ATOM   1000  C  CG    . HIS A 1 133 ? -32.490 -12.382 93.352  0.50 31.17 ? 153  HIS A CG    1 
ATOM   1001  N  ND1   . HIS A 1 133 ? -32.593 -11.390 94.303  0.50 31.63 ? 153  HIS A ND1   1 
ATOM   1002  C  CD2   . HIS A 1 133 ? -32.636 -13.553 94.014  0.50 31.00 ? 153  HIS A CD2   1 
ATOM   1003  C  CE1   . HIS A 1 133 ? -32.791 -11.938 95.488  0.50 31.43 ? 153  HIS A CE1   1 
ATOM   1004  N  NE2   . HIS A 1 133 ? -32.818 -13.250 95.341  0.50 31.17 ? 153  HIS A NE2   1 
ATOM   1005  N  N     . THR A 1 134 ? -30.542 -14.573 91.147  1.00 31.71 ? 154  THR A N     1 
ATOM   1006  C  CA    . THR A 1 134 ? -30.014 -15.910 91.401  1.00 31.79 ? 154  THR A CA    1 
ATOM   1007  C  C     . THR A 1 134 ? -28.484 -15.906 91.358  1.00 31.92 ? 154  THR A C     1 
ATOM   1008  O  O     . THR A 1 134 ? -27.836 -16.482 92.233  1.00 31.74 ? 154  THR A O     1 
ATOM   1009  C  CB    . THR A 1 134 ? -30.548 -16.943 90.384  1.00 31.77 ? 154  THR A CB    1 
ATOM   1010  O  OG1   . THR A 1 134 ? -31.982 -16.929 90.374  1.00 31.87 ? 154  THR A OG1   1 
ATOM   1011  C  CG2   . THR A 1 134 ? -30.075 -18.343 90.738  1.00 32.14 ? 154  THR A CG2   1 
ATOM   1012  N  N     . LEU A 1 135 ? -27.911 -15.236 90.363  1.00 32.15 ? 155  LEU A N     1 
ATOM   1013  C  CA    . LEU A 1 135 ? -26.452 -15.189 90.222  1.00 32.41 ? 155  LEU A CA    1 
ATOM   1014  C  C     . LEU A 1 135 ? -25.786 -14.413 91.355  1.00 32.73 ? 155  LEU A C     1 
ATOM   1015  O  O     . LEU A 1 135 ? -24.736 -14.824 91.849  1.00 32.56 ? 155  LEU A O     1 
ATOM   1016  C  CB    . LEU A 1 135 ? -26.043 -14.573 88.881  1.00 32.60 ? 155  LEU A CB    1 
ATOM   1017  C  CG    . LEU A 1 135 ? -26.186 -15.435 87.620  1.00 32.87 ? 155  LEU A CG    1 
ATOM   1018  C  CD1   . LEU A 1 135 ? -25.549 -14.724 86.438  1.00 33.23 ? 155  LEU A CD1   1 
ATOM   1019  C  CD2   . LEU A 1 135 ? -25.559 -16.792 87.801  1.00 32.65 ? 155  LEU A CD2   1 
ATOM   1020  N  N     . GLN A 1 136 ? -26.388 -13.286 91.743  1.00 33.01 ? 156  GLN A N     1 
ATOM   1021  C  CA    . GLN A 1 136 ? -25.866 -12.447 92.826  1.00 33.57 ? 156  GLN A CA    1 
ATOM   1022  C  C     . GLN A 1 136 ? -25.762 -13.218 94.144  1.00 33.62 ? 156  GLN A C     1 
ATOM   1023  O  O     . GLN A 1 136 ? -24.761 -13.100 94.850  1.00 34.01 ? 156  GLN A O     1 
ATOM   1024  C  CB    . GLN A 1 136 ? -26.736 -11.194 93.010  1.00 34.04 ? 156  GLN A CB    1 
ATOM   1025  C  CG    . GLN A 1 136 ? -26.508 -10.125 91.936  1.00 35.32 ? 156  GLN A CG    1 
ATOM   1026  C  CD    . GLN A 1 136 ? -27.419 -8.927  92.092  1.00 37.97 ? 156  GLN A CD    1 
ATOM   1027  O  OE1   . GLN A 1 136 ? -28.645 -9.061  92.144  1.00 38.86 ? 156  GLN A OE1   1 
ATOM   1028  N  NE2   . GLN A 1 136 ? -26.823 -7.740  92.163  1.00 39.39 ? 156  GLN A NE2   1 
ATOM   1029  N  N     . GLU A 1 137 ? -26.784 -14.016 94.454  1.00 33.29 ? 157  GLU A N     1 
ATOM   1030  C  CA    . GLU A 1 137 ? -26.772 -14.882 95.635  1.00 33.40 ? 157  GLU A CA    1 
ATOM   1031  C  C     . GLU A 1 137 ? -25.828 -16.073 95.451  1.00 32.71 ? 157  GLU A C     1 
ATOM   1032  O  O     . GLU A 1 137 ? -24.929 -16.295 96.263  1.00 32.56 ? 157  GLU A O     1 
ATOM   1033  C  CB    . GLU A 1 137 ? -28.180 -15.403 95.937  1.00 33.80 ? 157  GLU A CB    1 
ATOM   1034  C  CG    . GLU A 1 137 ? -29.182 -14.326 96.360  1.00 35.91 ? 157  GLU A CG    1 
ATOM   1035  C  CD    . GLU A 1 137 ? -29.047 -13.896 97.821  1.00 38.87 ? 157  GLU A CD    1 
ATOM   1036  O  OE1   . GLU A 1 137 ? -28.106 -14.337 98.523  1.00 40.46 ? 157  GLU A OE1   1 
ATOM   1037  O  OE2   . GLU A 1 137 ? -29.902 -13.103 98.268  1.00 41.93 ? 157  GLU A OE2   1 
ATOM   1038  N  N     . ALA A 1 138 ? -26.033 -16.834 94.376  1.00 31.94 ? 158  ALA A N     1 
ATOM   1039  C  CA    . ALA A 1 138 ? -25.288 -18.072 94.163  1.00 31.24 ? 158  ALA A CA    1 
ATOM   1040  C  C     . ALA A 1 138 ? -23.780 -17.845 94.040  1.00 30.80 ? 158  ALA A C     1 
ATOM   1041  O  O     . ALA A 1 138 ? -23.001 -18.699 94.438  1.00 30.49 ? 158  ALA A O     1 
ATOM   1042  C  CB    . ALA A 1 138 ? -25.822 -18.824 92.947  1.00 30.85 ? 158  ALA A CB    1 
ATOM   1043  N  N     . THR A 1 139 ? -23.368 -16.694 93.517  1.00 30.67 ? 159  THR A N     1 
ATOM   1044  C  CA    . THR A 1 139 ? -21.948 -16.439 93.268  1.00 30.58 ? 159  THR A CA    1 
ATOM   1045  C  C     . THR A 1 139 ? -21.239 -15.687 94.407  1.00 30.46 ? 159  THR A C     1 
ATOM   1046  O  O     . THR A 1 139 ? -20.069 -15.334 94.277  1.00 29.65 ? 159  THR A O     1 
ATOM   1047  C  CB    . THR A 1 139 ? -21.731 -15.688 91.927  1.00 30.82 ? 159  THR A CB    1 
ATOM   1048  O  OG1   . THR A 1 139 ? -22.315 -14.380 91.991  1.00 31.05 ? 159  THR A OG1   1 
ATOM   1049  C  CG2   . THR A 1 139 ? -22.335 -16.467 90.757  1.00 30.55 ? 159  THR A CG2   1 
ATOM   1050  N  N     . LYS A 1 140 ? -21.928 -15.477 95.527  1.00 30.68 ? 160  LYS A N     1 
ATOM   1051  C  CA    . LYS A 1 140 ? -21.321 -14.818 96.701  1.00 31.08 ? 160  LYS A CA    1 
ATOM   1052  C  C     . LYS A 1 140 ? -19.977 -15.415 97.142  1.00 30.50 ? 160  LYS A C     1 
ATOM   1053  O  O     . LYS A 1 140 ? -19.032 -14.674 97.411  1.00 30.82 ? 160  LYS A O     1 
ATOM   1054  C  CB    . LYS A 1 140 ? -22.293 -14.790 97.886  1.00 31.61 ? 160  LYS A CB    1 
ATOM   1055  C  CG    . LYS A 1 140 ? -23.395 -13.758 97.739  1.00 33.40 ? 160  LYS A CG    1 
ATOM   1056  C  CD    . LYS A 1 140 ? -24.128 -13.504 99.050  1.00 35.42 ? 160  LYS A CD    1 
ATOM   1057  C  CE    . LYS A 1 140 ? -25.236 -12.476 98.870  1.00 36.31 ? 160  LYS A CE    1 
ATOM   1058  N  NZ    . LYS A 1 140 ? -24.734 -11.210 98.248  1.00 38.22 ? 160  LYS A NZ    1 
ATOM   1059  N  N     . PRO A 1 141 ? -19.866 -16.749 97.187  1.00 29.82 ? 161  PRO A N     1 
ATOM   1060  C  CA    . PRO A 1 141 ? -18.553 -17.320 97.502  1.00 29.47 ? 161  PRO A CA    1 
ATOM   1061  C  C     . PRO A 1 141 ? -17.430 -16.855 96.566  1.00 29.30 ? 161  PRO A C     1 
ATOM   1062  O  O     . PRO A 1 141 ? -16.254 -16.828 96.968  1.00 28.84 ? 161  PRO A O     1 
ATOM   1063  C  CB    . PRO A 1 141 ? -18.774 -18.828 97.351  1.00 29.53 ? 161  PRO A CB    1 
ATOM   1064  C  CG    . PRO A 1 141 ? -20.230 -19.031 97.489  1.00 29.33 ? 161  PRO A CG    1 
ATOM   1065  C  CD    . PRO A 1 141 ? -20.893 -17.786 96.998  1.00 30.16 ? 161  PRO A CD    1 
ATOM   1066  N  N     . LEU A 1 142 ? -17.784 -16.485 95.335  1.00 28.89 ? 162  LEU A N     1 
ATOM   1067  C  CA    . LEU A 1 142 ? -16.781 -16.093 94.339  1.00 28.73 ? 162  LEU A CA    1 
ATOM   1068  C  C     . LEU A 1 142 ? -16.475 -14.587 94.312  1.00 28.69 ? 162  LEU A C     1 
ATOM   1069  O  O     . LEU A 1 142 ? -15.692 -14.121 93.485  1.00 28.19 ? 162  LEU A O     1 
ATOM   1070  C  CB    . LEU A 1 142 ? -17.218 -16.564 92.942  1.00 28.40 ? 162  LEU A CB    1 
ATOM   1071  C  CG    . LEU A 1 142 ? -17.271 -18.072 92.710  1.00 28.12 ? 162  LEU A CG    1 
ATOM   1072  C  CD1   . LEU A 1 142 ? -17.902 -18.365 91.362  1.00 26.40 ? 162  LEU A CD1   1 
ATOM   1073  C  CD2   . LEU A 1 142 ? -15.881 -18.713 92.814  1.00 27.87 ? 162  LEU A CD2   1 
ATOM   1074  N  N     . HIS A 1 143 ? -17.075 -13.821 95.215  1.00 29.10 ? 163  HIS A N     1 
ATOM   1075  C  CA    . HIS A 1 143 ? -16.942 -12.365 95.161  1.00 29.43 ? 163  HIS A CA    1 
ATOM   1076  C  C     . HIS A 1 143 ? -15.474 -11.924 95.118  1.00 29.33 ? 163  HIS A C     1 
ATOM   1077  O  O     . HIS A 1 143 ? -15.049 -11.197 94.218  1.00 28.87 ? 163  HIS A O     1 
ATOM   1078  C  CB    . HIS A 1 143 ? -17.657 -11.733 96.352  1.00 29.74 ? 163  HIS A CB    1 
ATOM   1079  C  CG    . HIS A 1 143 ? -17.530 -10.244 96.415  1.00 31.47 ? 163  HIS A CG    1 
ATOM   1080  N  ND1   . HIS A 1 143 ? -18.213 -9.402  95.564  1.00 32.71 ? 163  HIS A ND1   1 
ATOM   1081  C  CD2   . HIS A 1 143 ? -16.817 -9.445  97.245  1.00 33.03 ? 163  HIS A CD2   1 
ATOM   1082  C  CE1   . HIS A 1 143 ? -17.923 -8.149  95.862  1.00 33.29 ? 163  HIS A CE1   1 
ATOM   1083  N  NE2   . HIS A 1 143 ? -17.077 -8.146  96.877  1.00 33.86 ? 163  HIS A NE2   1 
ATOM   1084  N  N     . GLN A 1 144 ? -14.690 -12.391 96.075  1.00 29.33 ? 164  GLN A N     1 
ATOM   1085  C  CA    . GLN A 1 144 ? -13.292 -11.986 96.154  1.00 29.62 ? 164  GLN A CA    1 
ATOM   1086  C  C     . GLN A 1 144 ? -12.510 -12.505 94.951  1.00 28.93 ? 164  GLN A C     1 
ATOM   1087  O  O     . GLN A 1 144 ? -11.626 -11.827 94.439  1.00 28.65 ? 164  GLN A O     1 
ATOM   1088  C  CB    . GLN A 1 144 ? -12.663 -12.491 97.452  1.00 29.99 ? 164  GLN A CB    1 
ATOM   1089  C  CG    . GLN A 1 144 ? -11.396 -11.772 97.820  1.00 32.77 ? 164  GLN A CG    1 
ATOM   1090  C  CD    . GLN A 1 144 ? -11.629 -10.289 98.009  1.00 35.42 ? 164  GLN A CD    1 
ATOM   1091  O  OE1   . GLN A 1 144 ? -12.437 -9.884  98.847  1.00 38.76 ? 164  GLN A OE1   1 
ATOM   1092  N  NE2   . GLN A 1 144 ? -10.944 -9.471  97.212  1.00 36.53 ? 164  GLN A NE2   1 
ATOM   1093  N  N     . PHE A 1 145 ? -12.838 -13.718 94.519  1.00 28.58 ? 165  PHE A N     1 
ATOM   1094  C  CA    . PHE A 1 145 ? -12.326 -14.261 93.256  1.00 28.46 ? 165  PHE A CA    1 
ATOM   1095  C  C     . PHE A 1 145 ? -12.609 -13.291 92.101  1.00 28.55 ? 165  PHE A C     1 
ATOM   1096  O  O     . PHE A 1 145 ? -11.713 -12.989 91.303  1.00 28.58 ? 165  PHE A O     1 
ATOM   1097  C  CB    . PHE A 1 145 ? -12.951 -15.634 92.983  1.00 28.21 ? 165  PHE A CB    1 
ATOM   1098  C  CG    . PHE A 1 145 ? -12.685 -16.180 91.597  1.00 27.84 ? 165  PHE A CG    1 
ATOM   1099  C  CD1   . PHE A 1 145 ? -11.473 -16.777 91.288  1.00 27.66 ? 165  PHE A CD1   1 
ATOM   1100  C  CD2   . PHE A 1 145 ? -13.669 -16.131 90.615  1.00 27.47 ? 165  PHE A CD2   1 
ATOM   1101  C  CE1   . PHE A 1 145 ? -11.236 -17.295 90.013  1.00 27.80 ? 165  PHE A CE1   1 
ATOM   1102  C  CE2   . PHE A 1 145 ? -13.441 -16.651 89.348  1.00 26.38 ? 165  PHE A CE2   1 
ATOM   1103  C  CZ    . PHE A 1 145 ? -12.226 -17.233 89.049  1.00 26.81 ? 165  PHE A CZ    1 
ATOM   1104  N  N     . PHE A 1 146 ? -13.843 -12.794 92.024  1.00 28.74 ? 166  PHE A N     1 
ATOM   1105  C  CA    . PHE A 1 146 ? -14.216 -11.858 90.961  1.00 29.06 ? 166  PHE A CA    1 
ATOM   1106  C  C     . PHE A 1 146 ? -13.342 -10.604 90.986  1.00 29.62 ? 166  PHE A C     1 
ATOM   1107  O  O     . PHE A 1 146 ? -12.799 -10.187 89.958  1.00 29.81 ? 166  PHE A O     1 
ATOM   1108  C  CB    . PHE A 1 146 ? -15.695 -11.445 91.061  1.00 28.94 ? 166  PHE A CB    1 
ATOM   1109  C  CG    . PHE A 1 146 ? -16.681 -12.548 90.758  1.00 27.89 ? 166  PHE A CG    1 
ATOM   1110  C  CD1   . PHE A 1 146 ? -16.418 -13.522 89.792  1.00 28.12 ? 166  PHE A CD1   1 
ATOM   1111  C  CD2   . PHE A 1 146 ? -17.900 -12.581 91.410  1.00 27.34 ? 166  PHE A CD2   1 
ATOM   1112  C  CE1   . PHE A 1 146 ? -17.345 -14.527 89.518  1.00 27.86 ? 166  PHE A CE1   1 
ATOM   1113  C  CE2   . PHE A 1 146 ? -18.832 -13.583 91.139  1.00 28.21 ? 166  PHE A CE2   1 
ATOM   1114  C  CZ    . PHE A 1 146 ? -18.555 -14.552 90.186  1.00 27.27 ? 166  PHE A CZ    1 
ATOM   1115  N  N     . LEU A 1 147 ? -13.204 -10.008 92.165  1.00 30.40 ? 167  LEU A N     1 
ATOM   1116  C  CA    . LEU A 1 147 ? -12.445 -8.773  92.302  1.00 30.85 ? 167  LEU A CA    1 
ATOM   1117  C  C     . LEU A 1 147 ? -10.980 -8.996  91.933  1.00 31.34 ? 167  LEU A C     1 
ATOM   1118  O  O     . LEU A 1 147 ? -10.405 -8.205  91.185  1.00 31.39 ? 167  LEU A O     1 
ATOM   1119  C  CB    . LEU A 1 147 ? -12.562 -8.210  93.721  1.00 31.04 ? 167  LEU A CB    1 
ATOM   1120  C  CG    . LEU A 1 147 ? -13.915 -7.621  94.125  1.00 31.00 ? 167  LEU A CG    1 
ATOM   1121  C  CD1   . LEU A 1 147 ? -13.837 -7.145  95.576  1.00 31.30 ? 167  LEU A CD1   1 
ATOM   1122  C  CD2   . LEU A 1 147 ? -14.342 -6.471  93.208  1.00 30.52 ? 167  LEU A CD2   1 
ATOM   1123  N  N     . ASN A 1 148 ? -10.390 -10.080 92.433  1.00 31.74 ? 168  ASN A N     1 
ATOM   1124  C  CA    . ASN A 1 148 ? -8.984  -10.380 92.144  1.00 32.11 ? 168  ASN A CA    1 
ATOM   1125  C  C     . ASN A 1 148 ? -8.730  -10.686 90.668  1.00 31.76 ? 168  ASN A C     1 
ATOM   1126  O  O     . ASN A 1 148 ? -7.733  -10.239 90.116  1.00 31.91 ? 168  ASN A O     1 
ATOM   1127  C  CB    . ASN A 1 148 ? -8.480  -11.548 92.994  1.00 32.59 ? 168  ASN A CB    1 
ATOM   1128  C  CG    . ASN A 1 148 ? -8.490  -11.241 94.482  1.00 33.86 ? 168  ASN A CG    1 
ATOM   1129  O  OD1   . ASN A 1 148 ? -8.914  -10.167 94.905  1.00 36.95 ? 168  ASN A OD1   1 
ATOM   1130  N  ND2   . ASN A 1 148 ? -8.030  -12.194 95.286  1.00 35.72 ? 168  ASN A ND2   1 
ATOM   1131  N  N     . THR A 1 149 ? -9.621  -11.442 90.027  1.00 31.31 ? 169  THR A N     1 
ATOM   1132  C  CA    . THR A 1 149 ? -9.399  -11.846 88.626  1.00 30.96 ? 169  THR A CA    1 
ATOM   1133  C  C     . THR A 1 149 ? -9.860  -10.810 87.582  1.00 30.64 ? 169  THR A C     1 
ATOM   1134  O  O     . THR A 1 149 ? -9.304  -10.753 86.480  1.00 30.51 ? 169  THR A O     1 
ATOM   1135  C  CB    . THR A 1 149 ? -10.057 -13.210 88.309  1.00 30.96 ? 169  THR A CB    1 
ATOM   1136  O  OG1   . THR A 1 149 ? -11.460 -13.148 88.583  1.00 31.07 ? 169  THR A OG1   1 
ATOM   1137  C  CG2   . THR A 1 149 ? -9.415  -14.329 89.137  1.00 30.64 ? 169  THR A CG2   1 
ATOM   1138  N  N     . THR A 1 150 ? -10.859 -9.995  87.920  1.00 30.14 ? 170  THR A N     1 
ATOM   1139  C  CA    . THR A 1 150 ? -11.473 -9.084  86.935  1.00 29.85 ? 170  THR A CA    1 
ATOM   1140  C  C     . THR A 1 150 ? -11.574 -7.614  87.344  1.00 29.52 ? 170  THR A C     1 
ATOM   1141  O  O     . THR A 1 150 ? -11.745 -6.758  86.487  1.00 29.56 ? 170  THR A O     1 
ATOM   1142  C  CB    . THR A 1 150 ? -12.896 -9.547  86.598  1.00 29.72 ? 170  THR A CB    1 
ATOM   1143  O  OG1   . THR A 1 150 ? -13.746 -9.355  87.734  1.00 29.01 ? 170  THR A OG1   1 
ATOM   1144  C  CG2   . THR A 1 150 ? -12.898 -11.020 86.200  1.00 29.44 ? 170  THR A CG2   1 
ATOM   1145  N  N     . GLY A 1 151 ? -11.501 -7.319  88.640  1.00 29.16 ? 171  GLY A N     1 
ATOM   1146  C  CA    . GLY A 1 151 ? -11.791 -5.973  89.134  1.00 28.72 ? 171  GLY A CA    1 
ATOM   1147  C  C     . GLY A 1 151 ? -13.269 -5.593  89.092  1.00 28.64 ? 171  GLY A C     1 
ATOM   1148  O  O     . GLY A 1 151 ? -13.628 -4.473  89.460  1.00 28.84 ? 171  GLY A O     1 
ATOM   1149  N  N     . PHE A 1 152 ? -14.130 -6.507  88.638  1.00 28.07 ? 172  PHE A N     1 
ATOM   1150  C  CA    . PHE A 1 152 ? -15.574 -6.261  88.539  1.00 27.62 ? 172  PHE A CA    1 
ATOM   1151  C  C     . PHE A 1 152 ? -16.272 -7.272  89.455  1.00 27.30 ? 172  PHE A C     1 
ATOM   1152  O  O     . PHE A 1 152 ? -15.638 -8.220  89.919  1.00 27.09 ? 172  PHE A O     1 
ATOM   1153  C  CB    . PHE A 1 152 ? -16.074 -6.457  87.094  1.00 27.27 ? 172  PHE A CB    1 
ATOM   1154  C  CG    . PHE A 1 152 ? -15.695 -5.343  86.120  1.00 27.00 ? 172  PHE A CG    1 
ATOM   1155  C  CD1   . PHE A 1 152 ? -14.385 -4.893  85.994  1.00 26.07 ? 172  PHE A CD1   1 
ATOM   1156  C  CD2   . PHE A 1 152 ? -16.653 -4.803  85.273  1.00 25.59 ? 172  PHE A CD2   1 
ATOM   1157  C  CE1   . PHE A 1 152 ? -14.048 -3.897  85.078  1.00 25.12 ? 172  PHE A CE1   1 
ATOM   1158  C  CE2   . PHE A 1 152 ? -16.324 -3.812  84.360  1.00 25.79 ? 172  PHE A CE2   1 
ATOM   1159  C  CZ    . PHE A 1 152 ? -15.020 -3.357  84.264  1.00 25.40 ? 172  PHE A CZ    1 
ATOM   1160  N  N     . SER A 1 153 ? -17.572 -7.093  89.680  1.00 27.01 ? 173  SER A N     1 
ATOM   1161  C  CA    . SER A 1 153 ? -18.335 -7.968  90.582  1.00 27.44 ? 173  SER A CA    1 
ATOM   1162  C  C     . SER A 1 153 ? -19.822 -8.028  90.232  1.00 27.77 ? 173  SER A C     1 
ATOM   1163  O  O     . SER A 1 153 ? -20.304 -7.244  89.411  1.00 26.97 ? 173  SER A O     1 
ATOM   1164  C  CB    . SER A 1 153 ? -18.192 -7.468  92.027  1.00 27.87 ? 173  SER A CB    1 
ATOM   1165  O  OG    . SER A 1 153 ? -18.704 -6.143  92.170  1.00 27.83 ? 173  SER A OG    1 
ATOM   1166  N  N     . PHE A 1 154 ? -20.538 -8.957  90.870  1.00 28.41 ? 174  PHE A N     1 
ATOM   1167  C  CA    . PHE A 1 154 ? -22.001 -9.013  90.799  1.00 28.98 ? 174  PHE A CA    1 
ATOM   1168  C  C     . PHE A 1 154 ? -22.657 -8.301  91.989  1.00 29.86 ? 174  PHE A C     1 
ATOM   1169  O  O     . PHE A 1 154 ? -23.758 -7.770  91.847  1.00 30.08 ? 174  PHE A O     1 
ATOM   1170  C  CB    . PHE A 1 154 ? -22.521 -10.463 90.738  1.00 29.17 ? 174  PHE A CB    1 
ATOM   1171  C  CG    . PHE A 1 154 ? -22.532 -11.064 89.353  1.00 29.16 ? 174  PHE A CG    1 
ATOM   1172  C  CD1   . PHE A 1 154 ? -23.327 -10.522 88.349  1.00 29.87 ? 174  PHE A CD1   1 
ATOM   1173  C  CD2   . PHE A 1 154 ? -21.771 -12.186 89.062  1.00 29.64 ? 174  PHE A CD2   1 
ATOM   1174  C  CE1   . PHE A 1 154 ? -23.342 -11.074 87.070  1.00 30.22 ? 174  PHE A CE1   1 
ATOM   1175  C  CE2   . PHE A 1 154 ? -21.774 -12.748 87.780  1.00 30.35 ? 174  PHE A CE2   1 
ATOM   1176  C  CZ    . PHE A 1 154 ? -22.563 -12.195 86.787  1.00 30.75 ? 174  PHE A CZ    1 
ATOM   1177  N  N     . GLN A 1 155 ? -22.017 -8.311  93.163  1.00 30.76 ? 175  GLN A N     1 
ATOM   1178  C  CA    . GLN A 1 155 ? -22.604 -7.659  94.350  1.00 31.34 ? 175  GLN A CA    1 
ATOM   1179  C  C     . GLN A 1 155 ? -21.964 -6.300  94.609  1.00 31.35 ? 175  GLN A C     1 
ATOM   1180  O  O     . GLN A 1 155 ? -20.756 -6.134  94.407  1.00 31.30 ? 175  GLN A O     1 
ATOM   1181  C  CB    . GLN A 1 155 ? -22.545 -8.558  95.600  1.00 31.75 ? 175  GLN A CB    1 
ATOM   1182  C  CG    . GLN A 1 155 ? -21.189 -8.722  96.264  1.00 33.73 ? 175  GLN A CG    1 
ATOM   1183  C  CD    . GLN A 1 155 ? -21.287 -9.346  97.671  1.00 36.29 ? 175  GLN A CD    1 
ATOM   1184  O  OE1   . GLN A 1 155 ? -22.291 -9.982  98.026  1.00 37.35 ? 175  GLN A OE1   1 
ATOM   1185  N  NE2   . GLN A 1 155 ? -20.234 -9.174  98.464  1.00 35.51 ? 175  GLN A NE2   1 
ATOM   1186  N  N     . ASP A 1 156 ? -22.791 -5.332  95.019  1.00 31.26 ? 176  ASP A N     1 
ATOM   1187  C  CA    . ASP A 1 156 ? -22.347 -3.960  95.343  1.00 31.31 ? 176  ASP A CA    1 
ATOM   1188  C  C     . ASP A 1 156 ? -21.559 -3.285  94.208  1.00 31.22 ? 176  ASP A C     1 
ATOM   1189  O  O     . ASP A 1 156 ? -20.551 -2.633  94.467  1.00 31.03 ? 176  ASP A O     1 
ATOM   1190  C  CB    . ASP A 1 156 ? -21.470 -3.956  96.607  1.00 31.34 ? 176  ASP A CB    1 
ATOM   1191  C  CG    . ASP A 1 156 ? -22.140 -4.611  97.805  1.00 31.54 ? 176  ASP A CG    1 
ATOM   1192  O  OD1   . ASP A 1 156 ? -23.366 -4.468  97.987  1.00 32.55 ? 176  ASP A OD1   1 
ATOM   1193  O  OD2   . ASP A 1 156 ? -21.417 -5.255  98.585  1.00 32.43 ? 176  ASP A OD2   1 
ATOM   1194  N  N     . CYS A 1 157 ? -21.995 -3.460  92.960  1.00 31.04 ? 177  CYS A N     1 
ATOM   1195  C  CA    . CYS A 1 157 ? -21.302 -2.859  91.822  1.00 31.04 ? 177  CYS A CA    1 
ATOM   1196  C  C     . CYS A 1 157 ? -22.072 -1.651  91.327  1.00 31.13 ? 177  CYS A C     1 
ATOM   1197  O  O     . CYS A 1 157 ? -23.282 -1.533  91.559  1.00 30.88 ? 177  CYS A O     1 
ATOM   1198  C  CB    . CYS A 1 157 ? -21.123 -3.861  90.668  1.00 31.22 ? 177  CYS A CB    1 
ATOM   1199  S  SG    . CYS A 1 157 ? -22.653 -4.285  89.772  1.00 30.65 ? 177  CYS A SG    1 
ATOM   1200  N  N     . HIS A 1 158 ? -21.367 -0.759  90.637  1.00 31.02 ? 178  HIS A N     1 
ATOM   1201  C  CA    . HIS A 1 158 ? -21.990 0.436   90.077  1.00 31.20 ? 178  HIS A CA    1 
ATOM   1202  C  C     . HIS A 1 158 ? -21.545 0.644   88.631  1.00 31.14 ? 178  HIS A C     1 
ATOM   1203  O  O     . HIS A 1 158 ? -22.368 0.558   87.722  1.00 31.75 ? 178  HIS A O     1 
ATOM   1204  C  CB    . HIS A 1 158 ? -21.692 1.658   90.962  1.00 31.15 ? 178  HIS A CB    1 
ATOM   1205  C  CG    . HIS A 1 158 ? -22.105 1.470   92.393  1.00 31.82 ? 178  HIS A CG    1 
ATOM   1206  N  ND1   . HIS A 1 158 ? -23.253 2.026   92.917  1.00 32.04 ? 178  HIS A ND1   1 
ATOM   1207  C  CD2   . HIS A 1 158 ? -21.543 0.753   93.396  1.00 30.88 ? 178  HIS A CD2   1 
ATOM   1208  C  CE1   . HIS A 1 158 ? -23.372 1.670   94.184  1.00 32.13 ? 178  HIS A CE1   1 
ATOM   1209  N  NE2   . HIS A 1 158 ? -22.349 0.893   94.498  1.00 32.40 ? 178  HIS A NE2   1 
ATOM   1210  N  N     . ASP A 1 159 ? -20.256 0.915   88.428  1.00 30.87 ? 179  ASP A N     1 
ATOM   1211  C  CA    . ASP A 1 159 ? -19.670 1.076   87.098  1.00 30.73 ? 179  ASP A CA    1 
ATOM   1212  C  C     . ASP A 1 159 ? -18.735 -0.086  86.750  1.00 30.04 ? 179  ASP A C     1 
ATOM   1213  O  O     . ASP A 1 159 ? -18.177 -0.114  85.659  1.00 29.61 ? 179  ASP A O     1 
ATOM   1214  C  CB    . ASP A 1 159 ? -18.885 2.396   87.009  1.00 31.06 ? 179  ASP A CB    1 
ATOM   1215  C  CG    . ASP A 1 159 ? -19.773 3.637   87.151  1.00 32.95 ? 179  ASP A CG    1 
ATOM   1216  O  OD1   . ASP A 1 159 ? -20.929 3.643   86.672  1.00 35.31 ? 179  ASP A OD1   1 
ATOM   1217  O  OD2   . ASP A 1 159 ? -19.300 4.631   87.743  1.00 36.87 ? 179  ASP A OD2   1 
ATOM   1218  N  N     . ARG A 1 160 ? -18.567 -1.043  87.666  1.00 29.39 ? 180  ARG A N     1 
ATOM   1219  C  CA    . ARG A 1 160 ? -17.718 -2.212  87.422  1.00 29.21 ? 180  ARG A CA    1 
ATOM   1220  C  C     . ARG A 1 160 ? -18.514 -3.492  87.682  1.00 28.52 ? 180  ARG A C     1 
ATOM   1221  O  O     . ARG A 1 160 ? -18.176 -4.307  88.555  1.00 28.02 ? 180  ARG A O     1 
ATOM   1222  C  CB    . ARG A 1 160 ? -16.441 -2.149  88.274  1.00 29.51 ? 180  ARG A CB    1 
ATOM   1223  C  CG    . ARG A 1 160 ? -15.641 -0.863  88.063  1.00 31.42 ? 180  ARG A CG    1 
ATOM   1224  C  CD    . ARG A 1 160 ? -14.384 -0.818  88.916  1.00 34.22 ? 180  ARG A CD    1 
ATOM   1225  N  NE    . ARG A 1 160 ? -13.293 -1.564  88.295  1.00 37.38 ? 180  ARG A NE    1 
ATOM   1226  C  CZ    . ARG A 1 160 ? -12.448 -1.077  87.382  1.00 39.21 ? 180  ARG A CZ    1 
ATOM   1227  N  NH1   . ARG A 1 160 ? -12.525 0.185   86.962  1.00 38.66 ? 180  ARG A NH1   1 
ATOM   1228  N  NH2   . ARG A 1 160 ? -11.504 -1.871  86.884  1.00 40.59 ? 180  ARG A NH2   1 
ATOM   1229  N  N     . CYS A 1 161 ? -19.580 -3.653  86.904  1.00 27.75 ? 181  CYS A N     1 
ATOM   1230  C  CA    . CYS A 1 161 ? -20.483 -4.787  87.058  1.00 27.24 ? 181  CYS A CA    1 
ATOM   1231  C  C     . CYS A 1 161 ? -20.147 -5.901  86.077  1.00 26.67 ? 181  CYS A C     1 
ATOM   1232  O  O     . CYS A 1 161 ? -19.817 -5.648  84.912  1.00 25.87 ? 181  CYS A O     1 
ATOM   1233  C  CB    . CYS A 1 161 ? -21.931 -4.365  86.826  1.00 27.13 ? 181  CYS A CB    1 
ATOM   1234  S  SG    . CYS A 1 161 ? -22.571 -3.203  88.014  1.00 28.89 ? 181  CYS A SG    1 
ATOM   1235  N  N     . LEU A 1 162 ? -20.248 -7.134  86.558  1.00 26.04 ? 182  LEU A N     1 
ATOM   1236  C  CA    . LEU A 1 162 ? -20.241 -8.283  85.682  1.00 25.82 ? 182  LEU A CA    1 
ATOM   1237  C  C     . LEU A 1 162 ? -21.619 -8.402  85.064  1.00 25.71 ? 182  LEU A C     1 
ATOM   1238  O  O     . LEU A 1 162 ? -22.610 -7.926  85.618  1.00 25.44 ? 182  LEU A O     1 
ATOM   1239  C  CB    . LEU A 1 162 ? -19.894 -9.554  86.446  1.00 25.93 ? 182  LEU A CB    1 
ATOM   1240  C  CG    . LEU A 1 162 ? -18.461 -9.594  86.970  1.00 25.80 ? 182  LEU A CG    1 
ATOM   1241  C  CD1   . LEU A 1 162 ? -18.257 -10.793 87.907  1.00 24.39 ? 182  LEU A CD1   1 
ATOM   1242  C  CD2   . LEU A 1 162 ? -17.495 -9.627  85.791  1.00 25.45 ? 182  LEU A CD2   1 
ATOM   1243  N  N     . ALA A 1 163 ? -21.661 -8.999  83.885  1.00 25.39 ? 183  ALA A N     1 
ATOM   1244  C  CA    . ALA A 1 163 ? -22.902 -9.268  83.211  1.00 25.31 ? 183  ALA A CA    1 
ATOM   1245  C  C     . ALA A 1 163 ? -22.803 -10.678 82.669  1.00 25.48 ? 183  ALA A C     1 
ATOM   1246  O  O     . ALA A 1 163 ? -21.725 -11.301 82.718  1.00 25.18 ? 183  ALA A O     1 
ATOM   1247  C  CB    . ALA A 1 163 ? -23.123 -8.262  82.095  1.00 25.29 ? 183  ALA A CB    1 
ATOM   1248  N  N     . PHE A 1 164 ? -23.922 -11.193 82.177  1.00 25.45 ? 184  PHE A N     1 
ATOM   1249  C  CA    . PHE A 1 164 ? -23.925 -12.503 81.541  1.00 25.58 ? 184  PHE A CA    1 
ATOM   1250  C  C     . PHE A 1 164 ? -24.703 -12.473 80.229  1.00 25.22 ? 184  PHE A C     1 
ATOM   1251  O  O     . PHE A 1 164 ? -25.542 -11.613 80.015  1.00 25.15 ? 184  PHE A O     1 
ATOM   1252  C  CB    . PHE A 1 164 ? -24.490 -13.574 82.484  1.00 25.69 ? 184  PHE A CB    1 
ATOM   1253  C  CG    . PHE A 1 164 ? -25.946 -13.405 82.797  1.00 25.85 ? 184  PHE A CG    1 
ATOM   1254  C  CD1   . PHE A 1 164 ? -26.912 -14.008 82.004  1.00 26.49 ? 184  PHE A CD1   1 
ATOM   1255  C  CD2   . PHE A 1 164 ? -26.350 -12.629 83.869  1.00 26.35 ? 184  PHE A CD2   1 
ATOM   1256  C  CE1   . PHE A 1 164 ? -28.258 -13.856 82.284  1.00 27.43 ? 184  PHE A CE1   1 
ATOM   1257  C  CE2   . PHE A 1 164 ? -27.701 -12.462 84.151  1.00 27.27 ? 184  PHE A CE2   1 
ATOM   1258  C  CZ    . PHE A 1 164 ? -28.655 -13.076 83.360  1.00 27.15 ? 184  PHE A CZ    1 
ATOM   1259  N  N     . THR A 1 165 ? -24.379 -13.419 79.355  1.00 25.16 ? 185  THR A N     1 
ATOM   1260  C  CA    . THR A 1 165 ? -25.118 -13.667 78.124  1.00 24.66 ? 185  THR A CA    1 
ATOM   1261  C  C     . THR A 1 165 ? -25.574 -15.118 78.185  1.00 24.41 ? 185  THR A C     1 
ATOM   1262  O  O     . THR A 1 165 ? -24.746 -16.015 78.310  1.00 23.96 ? 185  THR A O     1 
ATOM   1263  C  CB    . THR A 1 165 ? -24.207 -13.476 76.895  1.00 24.88 ? 185  THR A CB    1 
ATOM   1264  O  OG1   . THR A 1 165 ? -23.837 -12.091 76.766  1.00 24.97 ? 185  THR A OG1   1 
ATOM   1265  C  CG2   . THR A 1 165 ? -24.888 -13.962 75.618  1.00 24.02 ? 185  THR A CG2   1 
ATOM   1266  N  N     . ASP A 1 166 ? -26.878 -15.360 78.115  1.00 23.85 ? 186  ASP A N     1 
ATOM   1267  C  CA    . ASP A 1 166 ? -27.359 -16.738 78.100  1.00 24.00 ? 186  ASP A CA    1 
ATOM   1268  C  C     . ASP A 1 166 ? -27.338 -17.264 76.675  1.00 23.64 ? 186  ASP A C     1 
ATOM   1269  O  O     . ASP A 1 166 ? -27.574 -16.517 75.720  1.00 23.89 ? 186  ASP A O     1 
ATOM   1270  C  CB    . ASP A 1 166 ? -28.764 -16.866 78.682  1.00 23.99 ? 186  ASP A CB    1 
ATOM   1271  C  CG    . ASP A 1 166 ? -29.767 -15.979 77.978  1.00 24.13 ? 186  ASP A CG    1 
ATOM   1272  O  OD1   . ASP A 1 166 ? -29.420 -14.810 77.729  1.00 24.48 ? 186  ASP A OD1   1 
ATOM   1273  O  OD2   . ASP A 1 166 ? -30.889 -16.439 77.703  1.00 23.83 ? 186  ASP A OD2   1 
ATOM   1274  N  N     . VAL A 1 167 ? -27.037 -18.550 76.538  1.00 23.33 ? 187  VAL A N     1 
ATOM   1275  C  CA    . VAL A 1 167 ? -27.062 -19.211 75.239  1.00 22.94 ? 187  VAL A CA    1 
ATOM   1276  C  C     . VAL A 1 167 ? -28.221 -20.190 75.257  1.00 22.95 ? 187  VAL A C     1 
ATOM   1277  O  O     . VAL A 1 167 ? -28.663 -20.602 76.326  1.00 23.36 ? 187  VAL A O     1 
ATOM   1278  C  CB    . VAL A 1 167 ? -25.736 -19.949 74.932  1.00 22.80 ? 187  VAL A CB    1 
ATOM   1279  C  CG1   . VAL A 1 167 ? -24.575 -18.981 74.966  1.00 21.59 ? 187  VAL A CG1   1 
ATOM   1280  C  CG2   . VAL A 1 167 ? -25.515 -21.113 75.891  1.00 22.32 ? 187  VAL A CG2   1 
ATOM   1281  N  N     . ALA A 1 168 ? -28.725 -20.525 74.075  1.00 22.80 ? 188  ALA A N     1 
ATOM   1282  C  CA    . ALA A 1 168 ? -29.840 -21.452 73.918  1.00 22.34 ? 188  ALA A CA    1 
ATOM   1283  C  C     . ALA A 1 168 ? -29.503 -22.451 72.793  1.00 22.31 ? 188  ALA A C     1 
ATOM   1284  O  O     . ALA A 1 168 ? -28.642 -22.168 71.967  1.00 22.04 ? 188  ALA A O     1 
ATOM   1285  C  CB    . ALA A 1 168 ? -31.097 -20.679 73.605  1.00 22.30 ? 188  ALA A CB    1 
ATOM   1286  N  N     . PRO A 1 169 ? -30.158 -23.627 72.764  1.00 22.33 ? 189  PRO A N     1 
ATOM   1287  C  CA    . PRO A 1 169 ? -31.193 -24.119 73.681  1.00 22.68 ? 189  PRO A CA    1 
ATOM   1288  C  C     . PRO A 1 169 ? -30.642 -24.430 75.084  1.00 22.61 ? 189  PRO A C     1 
ATOM   1289  O  O     . PRO A 1 169 ? -29.416 -24.373 75.309  1.00 21.66 ? 189  PRO A O     1 
ATOM   1290  C  CB    . PRO A 1 169 ? -31.671 -25.406 73.008  1.00 22.60 ? 189  PRO A CB    1 
ATOM   1291  C  CG    . PRO A 1 169 ? -30.456 -25.910 72.297  1.00 22.70 ? 189  PRO A CG    1 
ATOM   1292  C  CD    . PRO A 1 169 ? -29.730 -24.676 71.820  1.00 22.51 ? 189  PRO A CD    1 
ATOM   1293  N  N     . ARG A 1 170 ? -31.561 -24.770 75.986  1.00 22.66 ? 190  ARG A N     1 
ATOM   1294  C  CA    . ARG A 1 170 ? -31.323 -24.738 77.425  1.00 23.28 ? 190  ARG A CA    1 
ATOM   1295  C  C     . ARG A 1 170 ? -31.498 -26.145 78.017  1.00 23.58 ? 190  ARG A C     1 
ATOM   1296  O  O     . ARG A 1 170 ? -32.505 -26.453 78.699  1.00 23.65 ? 190  ARG A O     1 
ATOM   1297  C  CB    . ARG A 1 170 ? -32.275 -23.715 78.079  1.00 23.14 ? 190  ARG A CB    1 
ATOM   1298  C  CG    . ARG A 1 170 ? -32.279 -22.368 77.356  1.00 23.09 ? 190  ARG A CG    1 
ATOM   1299  C  CD    . ARG A 1 170 ? -33.363 -21.395 77.824  1.00 23.00 ? 190  ARG A CD    1 
ATOM   1300  N  NE    . ARG A 1 170 ? -33.356 -20.170 77.007  1.00 22.38 ? 190  ARG A NE    1 
ATOM   1301  C  CZ    . ARG A 1 170 ? -32.560 -19.116 77.197  1.00 22.28 ? 190  ARG A CZ    1 
ATOM   1302  N  NH1   . ARG A 1 170 ? -31.691 -19.087 78.202  1.00 22.34 ? 190  ARG A NH1   1 
ATOM   1303  N  NH2   . ARG A 1 170 ? -32.643 -18.067 76.377  1.00 20.81 ? 190  ARG A NH2   1 
ATOM   1304  N  N     . GLY A 1 171 ? -30.515 -26.995 77.732  1.00 23.38 ? 191  GLY A N     1 
ATOM   1305  C  CA    . GLY A 1 171 ? -30.521 -28.368 78.209  1.00 23.75 ? 191  GLY A CA    1 
ATOM   1306  C  C     . GLY A 1 171 ? -30.164 -29.388 77.143  1.00 24.01 ? 191  GLY A C     1 
ATOM   1307  O  O     . GLY A 1 171 ? -29.582 -29.047 76.108  1.00 24.10 ? 191  GLY A O     1 
ATOM   1308  N  N     . VAL A 1 172 ? -30.512 -30.645 77.419  1.00 24.11 ? 192  VAL A N     1 
ATOM   1309  C  CA    . VAL A 1 172 ? -30.206 -31.765 76.534  1.00 24.01 ? 192  VAL A CA    1 
ATOM   1310  C  C     . VAL A 1 172 ? -31.448 -32.478 76.021  1.00 24.01 ? 192  VAL A C     1 
ATOM   1311  O  O     . VAL A 1 172 ? -31.324 -33.424 75.251  1.00 24.45 ? 192  VAL A O     1 
ATOM   1312  C  CB    . VAL A 1 172 ? -29.305 -32.803 77.238  1.00 24.40 ? 192  VAL A CB    1 
ATOM   1313  C  CG1   . VAL A 1 172 ? -27.965 -32.150 77.661  1.00 24.17 ? 192  VAL A CG1   1 
ATOM   1314  C  CG2   . VAL A 1 172 ? -30.035 -33.443 78.426  1.00 23.19 ? 192  VAL A CG2   1 
ATOM   1315  N  N     . ALA A 1 173 ? -32.637 -32.026 76.419  1.00 23.85 ? 193  ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 173 ? -33.882 -32.669 76.003  1.00 24.00 ? 193  ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 173 ? -35.079 -31.774 76.231  1.00 24.24 ? 193  ALA A C     1 
ATOM   1318  O  O     . ALA A 1 173 ? -35.043 -30.876 77.068  1.00 24.29 ? 193  ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 173 ? -34.084 -33.995 76.752  1.00 23.45 ? 193  ALA A CB    1 
ATOM   1320  N  N     . SER A 1 174 ? -36.148 -32.056 75.491  1.00 24.88 ? 194  SER A N     1 
ATOM   1321  C  CA    . SER A 1 174 ? -37.405 -31.326 75.583  1.00 25.30 ? 194  SER A CA    1 
ATOM   1322  C  C     . SER A 1 174 ? -37.927 -31.255 77.015  1.00 25.28 ? 194  SER A C     1 
ATOM   1323  O  O     . SER A 1 174 ? -37.937 -32.253 77.719  1.00 25.79 ? 194  SER A O     1 
ATOM   1324  C  CB    . SER A 1 174 ? -38.449 -32.004 74.696  1.00 25.49 ? 194  SER A CB    1 
ATOM   1325  O  OG    . SER A 1 174 ? -39.729 -31.438 74.899  1.00 27.62 ? 194  SER A OG    1 
ATOM   1326  N  N     . GLY A 1 175 ? -38.362 -30.072 77.440  1.00 25.40 ? 195  GLY A N     1 
ATOM   1327  C  CA    . GLY A 1 175 ? -38.876 -29.868 78.797  1.00 25.22 ? 195  GLY A CA    1 
ATOM   1328  C  C     . GLY A 1 175 ? -37.871 -29.274 79.769  1.00 25.22 ? 195  GLY A C     1 
ATOM   1329  O  O     . GLY A 1 175 ? -38.243 -28.853 80.863  1.00 25.33 ? 195  GLY A O     1 
ATOM   1330  N  N     . GLN A 1 176 ? -36.599 -29.241 79.379  1.00 25.29 ? 196  GLN A N     1 
ATOM   1331  C  CA    . GLN A 1 176 ? -35.554 -28.673 80.216  1.00 25.19 ? 196  GLN A CA    1 
ATOM   1332  C  C     . GLN A 1 176 ? -35.407 -27.166 79.976  1.00 25.28 ? 196  GLN A C     1 
ATOM   1333  O  O     . GLN A 1 176 ? -35.663 -26.654 78.878  1.00 25.24 ? 196  GLN A O     1 
ATOM   1334  C  CB    . GLN A 1 176 ? -34.222 -29.382 79.961  1.00 25.12 ? 196  GLN A CB    1 
ATOM   1335  C  CG    . GLN A 1 176 ? -34.238 -30.856 80.343  1.00 25.28 ? 196  GLN A CG    1 
ATOM   1336  C  CD    . GLN A 1 176 ? -32.865 -31.529 80.289  1.00 25.82 ? 196  GLN A CD    1 
ATOM   1337  O  OE1   . GLN A 1 176 ? -31.841 -30.893 80.025  1.00 24.14 ? 196  GLN A OE1   1 
ATOM   1338  N  NE2   . GLN A 1 176 ? -32.849 -32.834 80.537  1.00 25.83 ? 196  GLN A NE2   1 
ATOM   1339  N  N     . ARG A 1 177 ? -34.997 -26.466 81.022  1.00 25.04 ? 197  ARG A N     1 
ATOM   1340  C  CA    . ARG A 1 177 ? -34.707 -25.046 80.949  1.00 24.56 ? 197  ARG A CA    1 
ATOM   1341  C  C     . ARG A 1 177 ? -33.477 -24.813 81.811  1.00 24.21 ? 197  ARG A C     1 
ATOM   1342  O  O     . ARG A 1 177 ? -33.548 -24.263 82.923  1.00 24.37 ? 197  ARG A O     1 
ATOM   1343  C  CB    . ARG A 1 177 ? -35.916 -24.224 81.412  1.00 24.84 ? 197  ARG A CB    1 
ATOM   1344  C  CG    . ARG A 1 177 ? -35.859 -22.743 81.013  1.00 25.24 ? 197  ARG A CG    1 
ATOM   1345  C  CD    . ARG A 1 177 ? -37.146 -22.058 81.375  1.00 25.35 ? 197  ARG A CD    1 
ATOM   1346  N  NE    . ARG A 1 177 ? -37.247 -20.694 80.855  1.00 24.75 ? 197  ARG A NE    1 
ATOM   1347  C  CZ    . ARG A 1 177 ? -37.747 -20.359 79.666  1.00 23.85 ? 197  ARG A CZ    1 
ATOM   1348  N  NH1   . ARG A 1 177 ? -38.186 -21.281 78.812  1.00 24.08 ? 197  ARG A NH1   1 
ATOM   1349  N  NH2   . ARG A 1 177 ? -37.796 -19.079 79.316  1.00 23.57 ? 197  ARG A NH2   1 
ATOM   1350  N  N     . ARG A 1 178 ? -32.351 -25.277 81.283  1.00 23.53 ? 198  ARG A N     1 
ATOM   1351  C  CA    . ARG A 1 178 ? -31.064 -25.231 81.967  1.00 23.52 ? 198  ARG A CA    1 
ATOM   1352  C  C     . ARG A 1 178 ? -30.085 -24.486 81.082  1.00 23.04 ? 198  ARG A C     1 
ATOM   1353  O  O     . ARG A 1 178 ? -29.631 -25.032 80.080  1.00 22.87 ? 198  ARG A O     1 
ATOM   1354  C  CB    . ARG A 1 178 ? -30.545 -26.651 82.208  1.00 23.50 ? 198  ARG A CB    1 
ATOM   1355  C  CG    . ARG A 1 178 ? -31.483 -27.545 83.013  1.00 23.87 ? 198  ARG A CG    1 
ATOM   1356  C  CD    . ARG A 1 178 ? -31.153 -29.011 82.761  1.00 24.41 ? 198  ARG A CD    1 
ATOM   1357  N  NE    . ARG A 1 178 ? -29.840 -29.372 83.287  1.00 25.08 ? 198  ARG A NE    1 
ATOM   1358  C  CZ    . ARG A 1 178 ? -29.120 -30.422 82.897  1.00 26.30 ? 198  ARG A CZ    1 
ATOM   1359  N  NH1   . ARG A 1 178 ? -29.548 -31.242 81.933  1.00 26.26 ? 198  ARG A NH1   1 
ATOM   1360  N  NH2   . ARG A 1 178 ? -27.946 -30.647 83.465  1.00 26.94 ? 198  ARG A NH2   1 
ATOM   1361  N  N     . SER A 1 179 ? -29.773 -23.239 81.430  1.00 22.87 ? 199  SER A N     1 
ATOM   1362  C  CA    . SER A 1 179 ? -29.027 -22.362 80.525  1.00 22.67 ? 199  SER A CA    1 
ATOM   1363  C  C     . SER A 1 179 ? -27.563 -22.198 80.919  1.00 22.94 ? 199  SER A C     1 
ATOM   1364  O  O     . SER A 1 179 ? -27.258 -21.941 82.083  1.00 23.08 ? 199  SER A O     1 
ATOM   1365  C  CB    . SER A 1 179 ? -29.684 -20.988 80.474  1.00 22.35 ? 199  SER A CB    1 
ATOM   1366  O  OG    . SER A 1 179 ? -30.989 -21.071 79.937  1.00 22.23 ? 199  SER A OG    1 
ATOM   1367  N  N     . TRP A 1 180 ? -26.659 -22.331 79.949  1.00 22.89 ? 200  TRP A N     1 
ATOM   1368  C  CA    . TRP A 1 180 ? -25.271 -21.927 80.162  1.00 22.97 ? 200  TRP A CA    1 
ATOM   1369  C  C     . TRP A 1 180 ? -25.175 -20.411 80.044  1.00 22.93 ? 200  TRP A C     1 
ATOM   1370  O  O     . TRP A 1 180 ? -25.787 -19.802 79.156  1.00 23.05 ? 200  TRP A O     1 
ATOM   1371  C  CB    . TRP A 1 180 ? -24.320 -22.613 79.182  1.00 23.09 ? 200  TRP A CB    1 
ATOM   1372  C  CG    . TRP A 1 180 ? -23.889 -23.941 79.678  1.00 23.94 ? 200  TRP A CG    1 
ATOM   1373  C  CD1   . TRP A 1 180 ? -24.344 -25.164 79.261  1.00 23.86 ? 200  TRP A CD1   1 
ATOM   1374  C  CD2   . TRP A 1 180 ? -22.931 -24.196 80.715  1.00 24.11 ? 200  TRP A CD2   1 
ATOM   1375  N  NE1   . TRP A 1 180 ? -23.722 -26.161 79.978  1.00 25.24 ? 200  TRP A NE1   1 
ATOM   1376  C  CE2   . TRP A 1 180 ? -22.852 -25.597 80.874  1.00 24.68 ? 200  TRP A CE2   1 
ATOM   1377  C  CE3   . TRP A 1 180 ? -22.131 -23.378 81.524  1.00 24.81 ? 200  TRP A CE3   1 
ATOM   1378  C  CZ2   . TRP A 1 180 ? -22.002 -26.200 81.811  1.00 24.79 ? 200  TRP A CZ2   1 
ATOM   1379  C  CZ3   . TRP A 1 180 ? -21.282 -23.983 82.462  1.00 24.16 ? 200  TRP A CZ3   1 
ATOM   1380  C  CH2   . TRP A 1 180 ? -21.227 -25.381 82.589  1.00 24.64 ? 200  TRP A CH2   1 
ATOM   1381  N  N     . LEU A 1 181 ? -24.416 -19.803 80.946  1.00 22.88 ? 201  LEU A N     1 
ATOM   1382  C  CA    . LEU A 1 181 ? -24.283 -18.353 80.988  1.00 22.82 ? 201  LEU A CA    1 
ATOM   1383  C  C     . LEU A 1 181 ? -22.820 -17.986 80.867  1.00 22.76 ? 201  LEU A C     1 
ATOM   1384  O  O     . LEU A 1 181 ? -21.993 -18.476 81.633  1.00 23.33 ? 201  LEU A O     1 
ATOM   1385  C  CB    . LEU A 1 181 ? -24.861 -17.804 82.292  1.00 22.59 ? 201  LEU A CB    1 
ATOM   1386  C  CG    . LEU A 1 181 ? -26.265 -18.275 82.668  1.00 22.51 ? 201  LEU A CG    1 
ATOM   1387  C  CD1   . LEU A 1 181 ? -26.722 -17.557 83.921  1.00 23.35 ? 201  LEU A CD1   1 
ATOM   1388  C  CD2   . LEU A 1 181 ? -27.288 -18.103 81.539  1.00 19.88 ? 201  LEU A CD2   1 
ATOM   1389  N  N     . ILE A 1 182 ? -22.511 -17.142 79.890  1.00 22.85 ? 202  ILE A N     1 
ATOM   1390  C  CA    . ILE A 1 182 ? -21.170 -16.607 79.701  1.00 22.73 ? 202  ILE A CA    1 
ATOM   1391  C  C     . ILE A 1 182 ? -21.026 -15.326 80.520  1.00 23.07 ? 202  ILE A C     1 
ATOM   1392  O  O     . ILE A 1 182 ? -21.754 -14.350 80.288  1.00 23.64 ? 202  ILE A O     1 
ATOM   1393  C  CB    . ILE A 1 182 ? -20.905 -16.265 78.227  1.00 22.78 ? 202  ILE A CB    1 
ATOM   1394  C  CG1   . ILE A 1 182 ? -21.071 -17.507 77.331  1.00 22.77 ? 202  ILE A CG1   1 
ATOM   1395  C  CG2   . ILE A 1 182 ? -19.507 -15.693 78.069  1.00 21.96 ? 202  ILE A CG2   1 
ATOM   1396  C  CD1   . ILE A 1 182 ? -21.245 -17.175 75.840  1.00 22.15 ? 202  ILE A CD1   1 
ATOM   1397  N  N     . ILE A 1 183 ? -20.090 -15.325 81.468  1.00 22.81 ? 203  ILE A N     1 
ATOM   1398  C  CA    . ILE A 1 183 ? -19.845 -14.169 82.307  1.00 22.15 ? 203  ILE A CA    1 
ATOM   1399  C  C     . ILE A 1 183 ? -18.890 -13.214 81.587  1.00 22.63 ? 203  ILE A C     1 
ATOM   1400  O  O     . ILE A 1 183 ? -17.852 -13.625 81.045  1.00 22.59 ? 203  ILE A O     1 
ATOM   1401  C  CB    . ILE A 1 183 ? -19.251 -14.559 83.690  1.00 22.35 ? 203  ILE A CB    1 
ATOM   1402  C  CG1   . ILE A 1 183 ? -20.071 -15.677 84.354  1.00 21.35 ? 203  ILE A CG1   1 
ATOM   1403  C  CG2   . ILE A 1 183 ? -19.204 -13.333 84.619  1.00 20.46 ? 203  ILE A CG2   1 
ATOM   1404  C  CD1   . ILE A 1 183 ? -21.540 -15.372 84.467  1.00 20.44 ? 203  ILE A CD1   1 
ATOM   1405  N  N     . GLN A 1 184 ? -19.260 -11.939 81.593  1.00 22.68 ? 204  GLN A N     1 
ATOM   1406  C  CA    . GLN A 1 184 ? -18.528 -10.893 80.895  1.00 22.94 ? 204  GLN A CA    1 
ATOM   1407  C  C     . GLN A 1 184 ? -18.412 -9.656  81.780  1.00 23.11 ? 204  GLN A C     1 
ATOM   1408  O  O     . GLN A 1 184 ? -19.172 -9.482  82.747  1.00 22.07 ? 204  GLN A O     1 
ATOM   1409  C  CB    . GLN A 1 184 ? -19.245 -10.497 79.601  1.00 22.95 ? 204  GLN A CB    1 
ATOM   1410  C  CG    . GLN A 1 184 ? -19.390 -11.611 78.548  1.00 22.71 ? 204  GLN A CG    1 
ATOM   1411  C  CD    . GLN A 1 184 ? -20.726 -11.543 77.813  1.00 22.27 ? 204  GLN A CD    1 
ATOM   1412  O  OE1   . GLN A 1 184 ? -21.724 -11.059 78.354  1.00 19.64 ? 204  GLN A OE1   1 
ATOM   1413  N  NE2   . GLN A 1 184 ? -20.748 -12.031 76.575  1.00 20.88 ? 204  GLN A NE2   1 
ATOM   1414  N  N     . ARG A 1 185 ? -17.449 -8.806  81.442  1.00 23.25 ? 205  ARG A N     1 
ATOM   1415  C  CA    . ARG A 1 185 ? -17.343 -7.492  82.050  1.00 24.00 ? 205  ARG A CA    1 
ATOM   1416  C  C     . ARG A 1 185 ? -18.223 -6.511  81.313  1.00 23.87 ? 205  ARG A C     1 
ATOM   1417  O  O     . ARG A 1 185 ? -18.138 -6.386  80.094  1.00 23.95 ? 205  ARG A O     1 
ATOM   1418  C  CB    . ARG A 1 185 ? -15.893 -7.015  82.041  1.00 23.95 ? 205  ARG A CB    1 
ATOM   1419  C  CG    . ARG A 1 185 ? -15.010 -7.897  82.879  1.00 25.15 ? 205  ARG A CG    1 
ATOM   1420  C  CD    . ARG A 1 185 ? -13.786 -7.176  83.369  1.00 26.68 ? 205  ARG A CD    1 
ATOM   1421  N  NE    . ARG A 1 185 ? -12.815 -6.972  82.308  1.00 27.91 ? 205  ARG A NE    1 
ATOM   1422  C  CZ    . ARG A 1 185 ? -11.540 -6.660  82.505  1.00 29.36 ? 205  ARG A CZ    1 
ATOM   1423  N  NH1   . ARG A 1 185 ? -11.062 -6.497  83.731  1.00 30.58 ? 205  ARG A NH1   1 
ATOM   1424  N  NH2   . ARG A 1 185 ? -10.737 -6.498  81.466  1.00 30.58 ? 205  ARG A NH2   1 
ATOM   1425  N  N     . TYR A 1 186 ? -19.068 -5.807  82.056  1.00 24.42 ? 206  TYR A N     1 
ATOM   1426  C  CA    . TYR A 1 186 ? -20.007 -4.870  81.453  1.00 24.74 ? 206  TYR A CA    1 
ATOM   1427  C  C     . TYR A 1 186 ? -19.344 -3.533  81.142  1.00 24.73 ? 206  TYR A C     1 
ATOM   1428  O  O     . TYR A 1 186 ? -19.515 -2.550  81.871  1.00 24.57 ? 206  TYR A O     1 
ATOM   1429  C  CB    . TYR A 1 186 ? -21.231 -4.675  82.352  1.00 25.11 ? 206  TYR A CB    1 
ATOM   1430  C  CG    . TYR A 1 186 ? -22.340 -3.892  81.697  1.00 26.69 ? 206  TYR A CG    1 
ATOM   1431  C  CD1   . TYR A 1 186 ? -22.848 -4.273  80.463  1.00 28.34 ? 206  TYR A CD1   1 
ATOM   1432  C  CD2   . TYR A 1 186 ? -22.873 -2.765  82.303  1.00 29.25 ? 206  TYR A CD2   1 
ATOM   1433  C  CE1   . TYR A 1 186 ? -23.860 -3.558  79.854  1.00 30.32 ? 206  TYR A CE1   1 
ATOM   1434  C  CE2   . TYR A 1 186 ? -23.896 -2.043  81.702  1.00 31.01 ? 206  TYR A CE2   1 
ATOM   1435  C  CZ    . TYR A 1 186 ? -24.381 -2.449  80.475  1.00 31.21 ? 206  TYR A CZ    1 
ATOM   1436  O  OH    . TYR A 1 186 ? -25.393 -1.754  79.862  1.00 35.04 ? 206  TYR A OH    1 
ATOM   1437  N  N     . VAL A 1 187 ? -18.580 -3.526  80.051  1.00 24.56 ? 207  VAL A N     1 
ATOM   1438  C  CA    . VAL A 1 187 ? -17.964 -2.323  79.498  1.00 24.50 ? 207  VAL A CA    1 
ATOM   1439  C  C     . VAL A 1 187 ? -18.501 -2.104  78.075  1.00 24.66 ? 207  VAL A C     1 
ATOM   1440  O  O     . VAL A 1 187 ? -19.270 -2.911  77.571  1.00 25.03 ? 207  VAL A O     1 
ATOM   1441  C  CB    . VAL A 1 187 ? -16.426 -2.447  79.445  1.00 24.46 ? 207  VAL A CB    1 
ATOM   1442  C  CG1   . VAL A 1 187 ? -15.844 -2.530  80.855  1.00 23.62 ? 207  VAL A CG1   1 
ATOM   1443  C  CG2   . VAL A 1 187 ? -16.021 -3.661  78.597  1.00 23.77 ? 207  VAL A CG2   1 
ATOM   1444  N  N     . GLU A 1 188 ? -18.087 -1.016  77.438  1.00 24.71 ? 208  GLU A N     1 
ATOM   1445  C  CA    . GLU A 1 188 ? -18.478 -0.711  76.071  1.00 24.78 ? 208  GLU A CA    1 
ATOM   1446  C  C     . GLU A 1 188 ? -18.150 -1.885  75.160  1.00 24.65 ? 208  GLU A C     1 
ATOM   1447  O  O     . GLU A 1 188 ? -16.988 -2.305  75.067  1.00 24.14 ? 208  GLU A O     1 
ATOM   1448  C  CB    . GLU A 1 188 ? -17.733 0.530   75.583  1.00 25.18 ? 208  GLU A CB    1 
ATOM   1449  C  CG    . GLU A 1 188 ? -18.092 0.986   74.170  1.00 26.32 ? 208  GLU A CG    1 
ATOM   1450  C  CD    . GLU A 1 188 ? -17.222 2.135   73.692  1.00 27.34 ? 208  GLU A CD    1 
ATOM   1451  O  OE1   . GLU A 1 188 ? -16.328 2.566   74.450  1.00 28.27 ? 208  GLU A OE1   1 
ATOM   1452  O  OE2   . GLU A 1 188 ? -17.438 2.609   72.553  1.00 27.82 ? 208  GLU A OE2   1 
ATOM   1453  N  N     . GLY A 1 189 ? -19.173 -2.408  74.487  1.00 24.23 ? 209  GLY A N     1 
ATOM   1454  C  CA    . GLY A 1 189 ? -19.006 -3.573  73.631  1.00 24.02 ? 209  GLY A CA    1 
ATOM   1455  C  C     . GLY A 1 189 ? -18.731 -4.799  74.475  1.00 23.47 ? 209  GLY A C     1 
ATOM   1456  O  O     . GLY A 1 189 ? -17.879 -5.625  74.137  1.00 23.50 ? 209  GLY A O     1 
ATOM   1457  N  N     . TYR A 1 190 ? -19.471 -4.901  75.577  1.00 23.04 ? 210  TYR A N     1 
ATOM   1458  C  CA    . TYR A 1 190 ? -19.290 -5.945  76.596  1.00 22.44 ? 210  TYR A CA    1 
ATOM   1459  C  C     . TYR A 1 190 ? -19.326 -7.362  76.054  1.00 21.73 ? 210  TYR A C     1 
ATOM   1460  O  O     . TYR A 1 190 ? -18.777 -8.261  76.675  1.00 21.11 ? 210  TYR A O     1 
ATOM   1461  C  CB    . TYR A 1 190 ? -20.360 -5.814  77.680  1.00 22.81 ? 210  TYR A CB    1 
ATOM   1462  C  CG    . TYR A 1 190 ? -21.771 -5.951  77.178  1.00 23.85 ? 210  TYR A CG    1 
ATOM   1463  C  CD1   . TYR A 1 190 ? -22.436 -7.162  77.246  1.00 25.50 ? 210  TYR A CD1   1 
ATOM   1464  C  CD2   . TYR A 1 190 ? -22.453 -4.858  76.658  1.00 25.98 ? 210  TYR A CD2   1 
ATOM   1465  C  CE1   . TYR A 1 190 ? -23.751 -7.287  76.792  1.00 27.07 ? 210  TYR A CE1   1 
ATOM   1466  C  CE2   . TYR A 1 190 ? -23.758 -4.973  76.201  1.00 27.24 ? 210  TYR A CE2   1 
ATOM   1467  C  CZ    . TYR A 1 190 ? -24.402 -6.191  76.265  1.00 27.75 ? 210  TYR A CZ    1 
ATOM   1468  O  OH    . TYR A 1 190 ? -25.704 -6.301  75.818  1.00 29.34 ? 210  TYR A OH    1 
ATOM   1469  N  N     . PHE A 1 191 ? -19.994 -7.556  74.910  1.00 21.23 ? 211  PHE A N     1 
ATOM   1470  C  CA    . PHE A 1 191 ? -20.035 -8.843  74.215  1.00 20.73 ? 211  PHE A CA    1 
ATOM   1471  C  C     . PHE A 1 191 ? -18.660 -9.471  74.035  1.00 20.47 ? 211  PHE A C     1 
ATOM   1472  O  O     . PHE A 1 191 ? -18.532 -10.689 74.002  1.00 20.72 ? 211  PHE A O     1 
ATOM   1473  C  CB    . PHE A 1 191 ? -20.650 -8.696  72.819  1.00 20.62 ? 211  PHE A CB    1 
ATOM   1474  C  CG    . PHE A 1 191 ? -21.925 -7.908  72.785  1.00 20.86 ? 211  PHE A CG    1 
ATOM   1475  C  CD1   . PHE A 1 191 ? -21.935 -6.610  72.284  1.00 20.55 ? 211  PHE A CD1   1 
ATOM   1476  C  CD2   . PHE A 1 191 ? -23.115 -8.461  73.229  1.00 21.10 ? 211  PHE A CD2   1 
ATOM   1477  C  CE1   . PHE A 1 191 ? -23.099 -5.884  72.235  1.00 20.50 ? 211  PHE A CE1   1 
ATOM   1478  C  CE2   . PHE A 1 191 ? -24.296 -7.730  73.191  1.00 21.31 ? 211  PHE A CE2   1 
ATOM   1479  C  CZ    . PHE A 1 191 ? -24.288 -6.440  72.699  1.00 21.50 ? 211  PHE A CZ    1 
ATOM   1480  N  N     . LEU A 1 192 ? -17.647 -8.635  73.874  1.00 20.69 ? 212  LEU A N     1 
ATOM   1481  C  CA    . LEU A 1 192 ? -16.289 -9.090  73.597  1.00 20.84 ? 212  LEU A CA    1 
ATOM   1482  C  C     . LEU A 1 192 ? -15.415 -9.192  74.846  1.00 21.24 ? 212  LEU A C     1 
ATOM   1483  O  O     . LEU A 1 192 ? -14.188 -9.289  74.729  1.00 21.59 ? 212  LEU A O     1 
ATOM   1484  C  CB    . LEU A 1 192 ? -15.629 -8.139  72.591  1.00 20.52 ? 212  LEU A CB    1 
ATOM   1485  C  CG    . LEU A 1 192 ? -16.409 -7.912  71.289  1.00 20.58 ? 212  LEU A CG    1 
ATOM   1486  C  CD1   . LEU A 1 192 ? -15.576 -7.109  70.294  1.00 20.77 ? 212  LEU A CD1   1 
ATOM   1487  C  CD2   . LEU A 1 192 ? -16.845 -9.246  70.684  1.00 19.89 ? 212  LEU A CD2   1 
ATOM   1488  N  N     . HIS A 1 193 ? -16.034 -9.212  76.026  1.00 21.46 ? 213  HIS A N     1 
ATOM   1489  C  CA    . HIS A 1 193 ? -15.290 -9.235  77.287  1.00 21.63 ? 213  HIS A CA    1 
ATOM   1490  C  C     . HIS A 1 193 ? -15.662 -10.389 78.233  1.00 22.18 ? 213  HIS A C     1 
ATOM   1491  O  O     . HIS A 1 193 ? -16.092 -10.159 79.368  1.00 22.09 ? 213  HIS A O     1 
ATOM   1492  C  CB    . HIS A 1 193 ? -15.485 -7.887  77.983  1.00 21.87 ? 213  HIS A CB    1 
ATOM   1493  C  CG    . HIS A 1 193 ? -14.863 -6.744  77.248  1.00 21.06 ? 213  HIS A CG    1 
ATOM   1494  N  ND1   . HIS A 1 193 ? -13.568 -6.340  77.472  1.00 21.35 ? 213  HIS A ND1   1 
ATOM   1495  C  CD2   . HIS A 1 193 ? -15.349 -5.933  76.277  1.00 22.01 ? 213  HIS A CD2   1 
ATOM   1496  C  CE1   . HIS A 1 193 ? -13.287 -5.315  76.686  1.00 22.44 ? 213  HIS A CE1   1 
ATOM   1497  N  NE2   . HIS A 1 193 ? -14.347 -5.055  75.942  1.00 21.39 ? 213  HIS A NE2   1 
ATOM   1498  N  N     . PRO A 1 194 ? -15.484 -11.642 77.778  1.00 22.48 ? 214  PRO A N     1 
ATOM   1499  C  CA    . PRO A 1 194 ? -15.683 -12.782 78.656  1.00 22.68 ? 214  PRO A CA    1 
ATOM   1500  C  C     . PRO A 1 194 ? -14.588 -12.865 79.715  1.00 23.13 ? 214  PRO A C     1 
ATOM   1501  O  O     . PRO A 1 194 ? -13.439 -12.460 79.454  1.00 22.70 ? 214  PRO A O     1 
ATOM   1502  C  CB    . PRO A 1 194 ? -15.581 -13.971 77.709  1.00 22.87 ? 214  PRO A CB    1 
ATOM   1503  C  CG    . PRO A 1 194 ? -14.662 -13.506 76.650  1.00 22.92 ? 214  PRO A CG    1 
ATOM   1504  C  CD    . PRO A 1 194 ? -15.000 -12.058 76.455  1.00 22.82 ? 214  PRO A CD    1 
ATOM   1505  N  N     . THR A 1 195 ? -14.944 -13.396 80.886  1.00 23.28 ? 215  THR A N     1 
ATOM   1506  C  CA    . THR A 1 195 ? -14.015 -13.482 82.012  1.00 23.57 ? 215  THR A CA    1 
ATOM   1507  C  C     . THR A 1 195 ? -13.322 -14.828 82.110  1.00 24.07 ? 215  THR A C     1 
ATOM   1508  O  O     . THR A 1 195 ? -12.262 -14.943 82.724  1.00 24.24 ? 215  THR A O     1 
ATOM   1509  C  CB    . THR A 1 195 ? -14.727 -13.190 83.338  1.00 23.57 ? 215  THR A CB    1 
ATOM   1510  O  OG1   . THR A 1 195 ? -15.775 -14.146 83.550  1.00 22.00 ? 215  THR A OG1   1 
ATOM   1511  C  CG2   . THR A 1 195 ? -15.305 -11.780 83.311  1.00 23.05 ? 215  THR A CG2   1 
ATOM   1512  N  N     . GLY A 1 196 ? -13.907 -15.846 81.487  1.00 24.68 ? 216  GLY A N     1 
ATOM   1513  C  CA    . GLY A 1 196 ? -13.389 -17.208 81.593  1.00 24.57 ? 216  GLY A CA    1 
ATOM   1514  C  C     . GLY A 1 196 ? -14.259 -18.080 82.467  1.00 24.61 ? 216  GLY A C     1 
ATOM   1515  O  O     . GLY A 1 196 ? -14.038 -19.282 82.544  1.00 25.17 ? 216  GLY A O     1 
ATOM   1516  N  N     . LEU A 1 197 ? -15.248 -17.481 83.127  1.00 24.76 ? 217  LEU A N     1 
ATOM   1517  C  CA    . LEU A 1 197 ? -16.231 -18.233 83.906  1.00 24.62 ? 217  LEU A CA    1 
ATOM   1518  C  C     . LEU A 1 197 ? -17.485 -18.425 83.077  1.00 24.25 ? 217  LEU A C     1 
ATOM   1519  O  O     . LEU A 1 197 ? -17.918 -17.517 82.385  1.00 24.34 ? 217  LEU A O     1 
ATOM   1520  C  CB    . LEU A 1 197 ? -16.579 -17.487 85.199  1.00 24.74 ? 217  LEU A CB    1 
ATOM   1521  C  CG    . LEU A 1 197 ? -17.533 -18.174 86.180  1.00 25.12 ? 217  LEU A CG    1 
ATOM   1522  C  CD1   . LEU A 1 197 ? -16.899 -19.444 86.816  1.00 25.94 ? 217  LEU A CD1   1 
ATOM   1523  C  CD2   . LEU A 1 197 ? -17.968 -17.191 87.259  1.00 24.39 ? 217  LEU A CD2   1 
ATOM   1524  N  N     . GLU A 1 198 ? -18.058 -19.617 83.138  1.00 24.19 ? 218  GLU A N     1 
ATOM   1525  C  CA    . GLU A 1 198 ? -19.379 -19.856 82.588  1.00 24.28 ? 218  GLU A CA    1 
ATOM   1526  C  C     . GLU A 1 198 ? -20.176 -20.622 83.622  1.00 24.20 ? 218  GLU A C     1 
ATOM   1527  O  O     . GLU A 1 198 ? -19.606 -21.442 84.337  1.00 24.68 ? 218  GLU A O     1 
ATOM   1528  C  CB    . GLU A 1 198 ? -19.269 -20.662 81.300  1.00 24.41 ? 218  GLU A CB    1 
ATOM   1529  C  CG    . GLU A 1 198 ? -18.433 -19.985 80.232  1.00 24.33 ? 218  GLU A CG    1 
ATOM   1530  C  CD    . GLU A 1 198 ? -18.508 -20.690 78.892  1.00 25.32 ? 218  GLU A CD    1 
ATOM   1531  O  OE1   . GLU A 1 198 ? -19.027 -21.823 78.842  1.00 25.49 ? 218  GLU A OE1   1 
ATOM   1532  O  OE2   . GLU A 1 198 ? -18.043 -20.107 77.886  1.00 25.97 ? 218  GLU A OE2   1 
ATOM   1533  N  N     . LEU A 1 199 ? -21.479 -20.369 83.701  1.00 24.13 ? 219  LEU A N     1 
ATOM   1534  C  CA    . LEU A 1 199 ? -22.336 -21.001 84.714  1.00 24.12 ? 219  LEU A CA    1 
ATOM   1535  C  C     . LEU A 1 199 ? -23.598 -21.638 84.121  1.00 23.77 ? 219  LEU A C     1 
ATOM   1536  O  O     . LEU A 1 199 ? -24.271 -21.031 83.297  1.00 23.43 ? 219  LEU A O     1 
ATOM   1537  C  CB    . LEU A 1 199 ? -22.761 -19.967 85.762  1.00 24.14 ? 219  LEU A CB    1 
ATOM   1538  C  CG    . LEU A 1 199 ? -21.664 -19.102 86.378  1.00 24.99 ? 219  LEU A CG    1 
ATOM   1539  C  CD1   . LEU A 1 199 ? -22.287 -18.013 87.281  1.00 25.46 ? 219  LEU A CD1   1 
ATOM   1540  C  CD2   . LEU A 1 199 ? -20.664 -19.965 87.147  1.00 26.12 ? 219  LEU A CD2   1 
ATOM   1541  N  N     . LEU A 1 200 ? -23.920 -22.853 84.566  1.00 23.38 ? 220  LEU A N     1 
ATOM   1542  C  CA    . LEU A 1 200 ? -25.144 -23.532 84.166  1.00 23.33 ? 220  LEU A CA    1 
ATOM   1543  C  C     . LEU A 1 200 ? -26.188 -23.345 85.255  1.00 23.65 ? 220  LEU A C     1 
ATOM   1544  O  O     . LEU A 1 200 ? -25.966 -23.744 86.402  1.00 23.87 ? 220  LEU A O     1 
ATOM   1545  C  CB    . LEU A 1 200 ? -24.903 -25.029 83.959  1.00 23.13 ? 220  LEU A CB    1 
ATOM   1546  C  CG    . LEU A 1 200 ? -26.107 -25.874 83.505  1.00 22.64 ? 220  LEU A CG    1 
ATOM   1547  C  CD1   . LEU A 1 200 ? -26.651 -25.406 82.147  1.00 20.02 ? 220  LEU A CD1   1 
ATOM   1548  C  CD2   . LEU A 1 200 ? -25.749 -27.366 83.464  1.00 20.52 ? 220  LEU A CD2   1 
ATOM   1549  N  N     . VAL A 1 201 ? -27.323 -22.757 84.896  1.00 23.66 ? 221  VAL A N     1 
ATOM   1550  C  CA    . VAL A 1 201 ? -28.415 -22.528 85.842  1.00 23.96 ? 221  VAL A CA    1 
ATOM   1551  C  C     . VAL A 1 201 ? -29.661 -23.266 85.398  1.00 24.66 ? 221  VAL A C     1 
ATOM   1552  O  O     . VAL A 1 201 ? -30.082 -23.130 84.250  1.00 24.76 ? 221  VAL A O     1 
ATOM   1553  C  CB    . VAL A 1 201 ? -28.741 -21.017 85.961  1.00 23.84 ? 221  VAL A CB    1 
ATOM   1554  C  CG1   . VAL A 1 201 ? -29.983 -20.794 86.812  1.00 23.55 ? 221  VAL A CG1   1 
ATOM   1555  C  CG2   . VAL A 1 201 ? -27.532 -20.251 86.520  1.00 22.93 ? 221  VAL A CG2   1 
ATOM   1556  N  N     . ASP A 1 202 ? -30.241 -24.051 86.303  1.00 25.48 ? 222  ASP A N     1 
ATOM   1557  C  CA    . ASP A 1 202 ? -31.569 -24.640 86.095  1.00 26.06 ? 222  ASP A CA    1 
ATOM   1558  C  C     . ASP A 1 202 ? -32.610 -23.629 86.567  1.00 26.38 ? 222  ASP A C     1 
ATOM   1559  O  O     . ASP A 1 202 ? -32.745 -23.393 87.775  1.00 26.89 ? 222  ASP A O     1 
ATOM   1560  C  CB    . ASP A 1 202 ? -31.722 -25.955 86.868  1.00 26.11 ? 222  ASP A CB    1 
ATOM   1561  C  CG    . ASP A 1 202 ? -33.050 -26.669 86.585  1.00 27.50 ? 222  ASP A CG    1 
ATOM   1562  O  OD1   . ASP A 1 202 ? -33.922 -26.127 85.863  1.00 29.53 ? 222  ASP A OD1   1 
ATOM   1563  O  OD2   . ASP A 1 202 ? -33.229 -27.789 87.101  1.00 29.21 ? 222  ASP A OD2   1 
ATOM   1564  N  N     . HIS A 1 203 ? -33.330 -23.029 85.620  1.00 26.24 ? 223  HIS A N     1 
ATOM   1565  C  CA    . HIS A 1 203 ? -34.372 -22.041 85.946  1.00 26.36 ? 223  HIS A CA    1 
ATOM   1566  C  C     . HIS A 1 203 ? -35.764 -22.480 85.455  1.00 26.84 ? 223  HIS A C     1 
ATOM   1567  O  O     . HIS A 1 203 ? -36.584 -21.670 85.050  1.00 27.22 ? 223  HIS A O     1 
ATOM   1568  C  CB    . HIS A 1 203 ? -33.989 -20.617 85.471  1.00 26.29 ? 223  HIS A CB    1 
ATOM   1569  C  CG    . HIS A 1 203 ? -33.614 -20.510 84.020  1.00 24.59 ? 223  HIS A CG    1 
ATOM   1570  N  ND1   . HIS A 1 203 ? -34.333 -19.751 83.125  1.00 23.87 ? 223  HIS A ND1   1 
ATOM   1571  C  CD2   . HIS A 1 203 ? -32.565 -21.010 83.326  1.00 23.85 ? 223  HIS A CD2   1 
ATOM   1572  C  CE1   . HIS A 1 203 ? -33.764 -19.813 81.935  1.00 23.63 ? 223  HIS A CE1   1 
ATOM   1573  N  NE2   . HIS A 1 203 ? -32.692 -20.577 82.027  1.00 22.73 ? 223  HIS A NE2   1 
ATOM   1574  N  N     . GLY A 1 204 ? -36.027 -23.779 85.547  1.00 27.73 ? 224  GLY A N     1 
ATOM   1575  C  CA    . GLY A 1 204 ? -37.293 -24.353 85.098  1.00 28.46 ? 224  GLY A CA    1 
ATOM   1576  C  C     . GLY A 1 204 ? -38.506 -24.039 85.964  1.00 28.90 ? 224  GLY A C     1 
ATOM   1577  O  O     . GLY A 1 204 ? -39.587 -23.759 85.435  1.00 28.94 ? 224  GLY A O     1 
ATOM   1578  N  N     A SER A 1 205 ? -38.328 -24.077 87.285  0.50 29.11 ? 225  SER A N     1 
ATOM   1579  N  N     B SER A 1 205 ? -38.344 -24.085 87.286  0.50 29.23 ? 225  SER A N     1 
ATOM   1580  C  CA    A SER A 1 205 ? -39.446 -23.912 88.219  0.50 29.25 ? 225  SER A CA    1 
ATOM   1581  C  CA    B SER A 1 205 ? -39.496 -23.957 88.185  0.50 29.50 ? 225  SER A CA    1 
ATOM   1582  C  C     A SER A 1 205 ? -39.993 -22.491 88.213  0.50 29.46 ? 225  SER A C     1 
ATOM   1583  C  C     B SER A 1 205 ? -39.992 -22.516 88.251  0.50 29.58 ? 225  SER A C     1 
ATOM   1584  O  O     A SER A 1 205 ? -39.240 -21.533 88.040  0.50 29.58 ? 225  SER A O     1 
ATOM   1585  O  O     B SER A 1 205 ? -39.205 -21.574 88.169  0.50 29.70 ? 225  SER A O     1 
ATOM   1586  C  CB    A SER A 1 205 ? -39.016 -24.279 89.644  0.50 29.30 ? 225  SER A CB    1 
ATOM   1587  C  CB    B SER A 1 205 ? -39.162 -24.467 89.594  0.50 29.57 ? 225  SER A CB    1 
ATOM   1588  O  OG    A SER A 1 205 ? -40.061 -24.028 90.572  0.50 28.43 ? 225  SER A OG    1 
ATOM   1589  O  OG    B SER A 1 205 ? -39.011 -23.401 90.517  0.50 29.64 ? 225  SER A OG    1 
ATOM   1590  N  N     . THR A 1 206 ? -41.302 -22.358 88.410  1.00 29.82 ? 226  THR A N     1 
ATOM   1591  C  CA    . THR A 1 206 ? -41.935 -21.034 88.509  1.00 30.37 ? 226  THR A CA    1 
ATOM   1592  C  C     . THR A 1 206 ? -41.628 -20.346 89.847  1.00 30.97 ? 226  THR A C     1 
ATOM   1593  O  O     . THR A 1 206 ? -41.927 -19.168 90.018  1.00 30.96 ? 226  THR A O     1 
ATOM   1594  C  CB    . THR A 1 206 ? -43.458 -21.109 88.321  1.00 30.38 ? 226  THR A CB    1 
ATOM   1595  O  OG1   . THR A 1 206 ? -44.026 -22.001 89.290  1.00 30.86 ? 226  THR A OG1   1 
ATOM   1596  C  CG2   . THR A 1 206 ? -43.797 -21.592 86.927  1.00 30.20 ? 226  THR A CG2   1 
ATOM   1597  N  N     . ASP A 1 207 ? -41.052 -21.093 90.789  1.00 31.30 ? 227  ASP A N     1 
ATOM   1598  C  CA    . ASP A 1 207 ? -40.517 -20.527 92.011  1.00 31.84 ? 227  ASP A CA    1 
ATOM   1599  C  C     . ASP A 1 207 ? -39.010 -20.335 91.843  1.00 31.70 ? 227  ASP A C     1 
ATOM   1600  O  O     . ASP A 1 207 ? -38.246 -21.298 91.909  1.00 31.55 ? 227  ASP A O     1 
ATOM   1601  C  CB    . ASP A 1 207 ? -40.814 -21.458 93.197  1.00 32.09 ? 227  ASP A CB    1 
ATOM   1602  C  CG    . ASP A 1 207 ? -40.208 -20.961 94.511  1.00 33.43 ? 227  ASP A CG    1 
ATOM   1603  O  OD1   . ASP A 1 207 ? -39.625 -19.855 94.546  1.00 34.63 ? 227  ASP A OD1   1 
ATOM   1604  O  OD2   . ASP A 1 207 ? -40.316 -21.686 95.522  1.00 36.50 ? 227  ASP A OD2   1 
ATOM   1605  N  N     . ALA A 1 208 ? -38.588 -19.088 91.661  1.00 31.64 ? 228  ALA A N     1 
ATOM   1606  C  CA    . ALA A 1 208 ? -37.171 -18.768 91.440  1.00 32.04 ? 228  ALA A CA    1 
ATOM   1607  C  C     . ALA A 1 208 ? -36.258 -19.149 92.605  1.00 32.23 ? 228  ALA A C     1 
ATOM   1608  O  O     . ALA A 1 208 ? -35.046 -19.212 92.434  1.00 32.24 ? 228  ALA A O     1 
ATOM   1609  C  CB    . ALA A 1 208 ? -37.002 -17.291 91.114  1.00 32.13 ? 228  ALA A CB    1 
ATOM   1610  N  N     . GLY A 1 209 ? -36.831 -19.375 93.787  1.00 32.44 ? 229  GLY A N     1 
ATOM   1611  C  CA    . GLY A 1 209 ? -36.072 -19.857 94.936  1.00 32.46 ? 229  GLY A CA    1 
ATOM   1612  C  C     . GLY A 1 209 ? -35.522 -21.263 94.755  1.00 32.66 ? 229  GLY A C     1 
ATOM   1613  O  O     . GLY A 1 209 ? -34.572 -21.654 95.441  1.00 32.82 ? 229  GLY A O     1 
ATOM   1614  N  N     . HIS A 1 210 ? -36.119 -22.031 93.844  1.00 32.65 ? 230  HIS A N     1 
ATOM   1615  C  CA    . HIS A 1 210 ? -35.617 -23.362 93.516  1.00 32.80 ? 230  HIS A CA    1 
ATOM   1616  C  C     . HIS A 1 210 ? -34.474 -23.350 92.504  1.00 32.05 ? 230  HIS A C     1 
ATOM   1617  O  O     . HIS A 1 210 ? -33.826 -24.371 92.300  1.00 32.36 ? 230  HIS A O     1 
ATOM   1618  C  CB    . HIS A 1 210 ? -36.740 -24.235 92.975  1.00 33.17 ? 230  HIS A CB    1 
ATOM   1619  C  CG    . HIS A 1 210 ? -37.798 -24.549 93.982  1.00 35.49 ? 230  HIS A CG    1 
ATOM   1620  N  ND1   . HIS A 1 210 ? -39.092 -24.868 93.626  1.00 37.61 ? 230  HIS A ND1   1 
ATOM   1621  C  CD2   . HIS A 1 210 ? -37.755 -24.595 95.335  1.00 37.45 ? 230  HIS A CD2   1 
ATOM   1622  C  CE1   . HIS A 1 210 ? -39.799 -25.102 94.718  1.00 38.77 ? 230  HIS A CE1   1 
ATOM   1623  N  NE2   . HIS A 1 210 ? -39.012 -24.939 95.768  1.00 38.56 ? 230  HIS A NE2   1 
ATOM   1624  N  N     . TRP A 1 211 ? -34.239 -22.209 91.864  1.00 31.15 ? 231  TRP A N     1 
ATOM   1625  C  CA    . TRP A 1 211 ? -33.235 -22.107 90.812  1.00 30.28 ? 231  TRP A CA    1 
ATOM   1626  C  C     . TRP A 1 211 ? -31.834 -22.320 91.377  1.00 30.42 ? 231  TRP A C     1 
ATOM   1627  O  O     . TRP A 1 211 ? -31.519 -21.844 92.465  1.00 30.42 ? 231  TRP A O     1 
ATOM   1628  C  CB    . TRP A 1 211 ? -33.318 -20.742 90.130  1.00 29.70 ? 231  TRP A CB    1 
ATOM   1629  C  CG    . TRP A 1 211 ? -34.582 -20.514 89.353  1.00 27.93 ? 231  TRP A CG    1 
ATOM   1630  C  CD1   . TRP A 1 211 ? -35.671 -21.338 89.281  1.00 26.41 ? 231  TRP A CD1   1 
ATOM   1631  C  CD2   . TRP A 1 211 ? -34.891 -19.377 88.546  1.00 25.82 ? 231  TRP A CD2   1 
ATOM   1632  N  NE1   . TRP A 1 211 ? -36.631 -20.789 88.470  1.00 25.94 ? 231  TRP A NE1   1 
ATOM   1633  C  CE2   . TRP A 1 211 ? -36.180 -19.581 88.009  1.00 26.84 ? 231  TRP A CE2   1 
ATOM   1634  C  CE3   . TRP A 1 211 ? -34.206 -18.202 88.230  1.00 25.71 ? 231  TRP A CE3   1 
ATOM   1635  C  CZ2   . TRP A 1 211 ? -36.797 -18.653 87.164  1.00 26.38 ? 231  TRP A CZ2   1 
ATOM   1636  C  CZ3   . TRP A 1 211 ? -34.818 -17.280 87.394  1.00 25.82 ? 231  TRP A CZ3   1 
ATOM   1637  C  CH2   . TRP A 1 211 ? -36.101 -17.511 86.874  1.00 26.41 ? 231  TRP A CH2   1 
ATOM   1638  N  N     . ALA A 1 212 ? -30.989 -23.029 90.634  1.00 30.28 ? 232  ALA A N     1 
ATOM   1639  C  CA    . ALA A 1 212 ? -29.670 -23.389 91.147  1.00 30.20 ? 232  ALA A CA    1 
ATOM   1640  C  C     . ALA A 1 212 ? -28.613 -23.354 90.065  1.00 30.08 ? 232  ALA A C     1 
ATOM   1641  O  O     . ALA A 1 212 ? -28.864 -23.780 88.938  1.00 30.10 ? 232  ALA A O     1 
ATOM   1642  C  CB    . ALA A 1 212 ? -29.722 -24.791 91.787  1.00 30.09 ? 232  ALA A CB    1 
ATOM   1643  N  N     . VAL A 1 213 ? -27.436 -22.842 90.416  1.00 30.01 ? 233  VAL A N     1 
ATOM   1644  C  CA    . VAL A 1 213 ? -26.246 -23.033 89.604  1.00 30.31 ? 233  VAL A CA    1 
ATOM   1645  C  C     . VAL A 1 213 ? -25.828 -24.481 89.805  1.00 30.54 ? 233  VAL A C     1 
ATOM   1646  O  O     . VAL A 1 213 ? -25.380 -24.844 90.889  1.00 30.89 ? 233  VAL A O     1 
ATOM   1647  C  CB    . VAL A 1 213 ? -25.089 -22.105 90.036  1.00 30.20 ? 233  VAL A CB    1 
ATOM   1648  C  CG1   . VAL A 1 213 ? -23.817 -22.446 89.277  1.00 29.60 ? 233  VAL A CG1   1 
ATOM   1649  C  CG2   . VAL A 1 213 ? -25.465 -20.654 89.830  1.00 29.81 ? 233  VAL A CG2   1 
ATOM   1650  N  N     . GLU A 1 214 ? -26.004 -25.315 88.785  1.00 30.50 ? 234  GLU A N     1 
ATOM   1651  C  CA    . GLU A 1 214 ? -25.727 -26.745 88.927  1.00 30.45 ? 234  GLU A CA    1 
ATOM   1652  C  C     . GLU A 1 214 ? -24.329 -27.133 88.466  1.00 30.52 ? 234  GLU A C     1 
ATOM   1653  O  O     . GLU A 1 214 ? -23.878 -28.248 88.727  1.00 30.64 ? 234  GLU A O     1 
ATOM   1654  C  CB    . GLU A 1 214 ? -26.781 -27.587 88.206  1.00 30.50 ? 234  GLU A CB    1 
ATOM   1655  C  CG    . GLU A 1 214 ? -26.901 -27.353 86.710  1.00 30.49 ? 234  GLU A CG    1 
ATOM   1656  C  CD    . GLU A 1 214 ? -27.818 -28.371 86.044  1.00 30.11 ? 234  GLU A CD    1 
ATOM   1657  O  OE1   . GLU A 1 214 ? -28.885 -27.979 85.499  1.00 30.45 ? 234  GLU A OE1   1 
ATOM   1658  O  OE2   . GLU A 1 214 ? -27.471 -29.568 86.067  1.00 28.29 ? 234  GLU A OE2   1 
ATOM   1659  N  N     . GLN A 1 215 ? -23.641 -26.223 87.790  1.00 30.50 ? 235  GLN A N     1 
ATOM   1660  C  CA    . GLN A 1 215 ? -22.298 -26.502 87.300  1.00 30.90 ? 235  GLN A CA    1 
ATOM   1661  C  C     . GLN A 1 215 ? -21.578 -25.197 87.009  1.00 29.99 ? 235  GLN A C     1 
ATOM   1662  O  O     . GLN A 1 215 ? -22.209 -24.187 86.728  1.00 29.74 ? 235  GLN A O     1 
ATOM   1663  C  CB    . GLN A 1 215 ? -22.359 -27.381 86.038  1.00 31.53 ? 235  GLN A CB    1 
ATOM   1664  C  CG    . GLN A 1 215 ? -20.996 -27.779 85.432  1.00 33.93 ? 235  GLN A CG    1 
ATOM   1665  C  CD    . GLN A 1 215 ? -20.135 -28.602 86.381  1.00 37.22 ? 235  GLN A CD    1 
ATOM   1666  O  OE1   . GLN A 1 215 ? -19.146 -28.106 86.931  1.00 41.00 ? 235  GLN A OE1   1 
ATOM   1667  N  NE2   . GLN A 1 215 ? -20.513 -29.855 86.586  1.00 37.33 ? 235  GLN A NE2   1 
ATOM   1668  N  N     . VAL A 1 216 ? -20.252 -25.252 87.080  1.00 29.22 ? 236  VAL A N     1 
ATOM   1669  C  CA    . VAL A 1 216 ? -19.382 -24.102 86.914  1.00 28.81 ? 236  VAL A CA    1 
ATOM   1670  C  C     . VAL A 1 216 ? -18.196 -24.499 86.038  1.00 28.59 ? 236  VAL A C     1 
ATOM   1671  O  O     . VAL A 1 216 ? -17.541 -25.507 86.291  1.00 28.85 ? 236  VAL A O     1 
ATOM   1672  C  CB    . VAL A 1 216 ? -18.860 -23.641 88.297  1.00 28.89 ? 236  VAL A CB    1 
ATOM   1673  C  CG1   . VAL A 1 216 ? -17.869 -22.504 88.162  1.00 28.19 ? 236  VAL A CG1   1 
ATOM   1674  C  CG2   . VAL A 1 216 ? -20.031 -23.251 89.198  1.00 28.71 ? 236  VAL A CG2   1 
ATOM   1675  N  N     . TRP A 1 217 ? -17.923 -23.713 85.007  1.00 28.02 ? 237  TRP A N     1 
ATOM   1676  C  CA    . TRP A 1 217 ? -16.747 -23.921 84.174  1.00 27.60 ? 237  TRP A CA    1 
ATOM   1677  C  C     . TRP A 1 217 ? -15.891 -22.668 84.279  1.00 27.48 ? 237  TRP A C     1 
ATOM   1678  O  O     . TRP A 1 217 ? -16.397 -21.562 84.108  1.00 27.57 ? 237  TRP A O     1 
ATOM   1679  C  CB    . TRP A 1 217 ? -17.171 -24.174 82.723  1.00 27.55 ? 237  TRP A CB    1 
ATOM   1680  C  CG    . TRP A 1 217 ? -16.057 -24.492 81.746  1.00 26.77 ? 237  TRP A CG    1 
ATOM   1681  C  CD1   . TRP A 1 217 ? -15.657 -25.730 81.343  1.00 26.53 ? 237  TRP A CD1   1 
ATOM   1682  C  CD2   . TRP A 1 217 ? -15.237 -23.555 81.025  1.00 26.17 ? 237  TRP A CD2   1 
ATOM   1683  N  NE1   . TRP A 1 217 ? -14.638 -25.630 80.428  1.00 26.17 ? 237  TRP A NE1   1 
ATOM   1684  C  CE2   . TRP A 1 217 ? -14.364 -24.307 80.209  1.00 25.94 ? 237  TRP A CE2   1 
ATOM   1685  C  CE3   . TRP A 1 217 ? -15.165 -22.158 80.983  1.00 25.57 ? 237  TRP A CE3   1 
ATOM   1686  C  CZ2   . TRP A 1 217 ? -13.427 -23.711 79.360  1.00 25.71 ? 237  TRP A CZ2   1 
ATOM   1687  C  CZ3   . TRP A 1 217 ? -14.224 -21.563 80.139  1.00 26.17 ? 237  TRP A CZ3   1 
ATOM   1688  C  CH2   . TRP A 1 217 ? -13.364 -22.340 79.347  1.00 25.75 ? 237  TRP A CH2   1 
ATOM   1689  N  N     . TYR A 1 218 ? -14.609 -22.835 84.585  1.00 27.60 ? 238  TYR A N     1 
ATOM   1690  C  CA    . TYR A 1 218 ? -13.676 -21.713 84.575  1.00 27.92 ? 238  TYR A CA    1 
ATOM   1691  C  C     . TYR A 1 218 ? -12.359 -22.099 83.935  1.00 28.33 ? 238  TYR A C     1 
ATOM   1692  O  O     . TYR A 1 218 ? -11.703 -23.041 84.380  1.00 28.30 ? 238  TYR A O     1 
ATOM   1693  C  CB    . TYR A 1 218 ? -13.404 -21.181 85.985  1.00 28.02 ? 238  TYR A CB    1 
ATOM   1694  C  CG    . TYR A 1 218 ? -12.360 -20.096 85.961  1.00 28.08 ? 238  TYR A CG    1 
ATOM   1695  C  CD1   . TYR A 1 218 ? -12.643 -18.865 85.390  1.00 28.16 ? 238  TYR A CD1   1 
ATOM   1696  C  CD2   . TYR A 1 218 ? -11.068 -20.316 86.443  1.00 28.72 ? 238  TYR A CD2   1 
ATOM   1697  C  CE1   . TYR A 1 218 ? -11.694 -17.870 85.327  1.00 27.92 ? 238  TYR A CE1   1 
ATOM   1698  C  CE2   . TYR A 1 218 ? -10.106 -19.315 86.388  1.00 28.07 ? 238  TYR A CE2   1 
ATOM   1699  C  CZ    . TYR A 1 218 ? -10.431 -18.093 85.822  1.00 27.51 ? 238  TYR A CZ    1 
ATOM   1700  O  OH    . TYR A 1 218 ? -9.509  -17.076 85.742  1.00 26.63 ? 238  TYR A OH    1 
ATOM   1701  N  N     . ASN A 1 219 ? -11.982 -21.372 82.886  1.00 29.00 ? 239  ASN A N     1 
ATOM   1702  C  CA    . ASN A 1 219 ? -10.668 -21.498 82.269  1.00 29.41 ? 239  ASN A CA    1 
ATOM   1703  C  C     . ASN A 1 219 ? -10.238 -22.942 82.034  1.00 29.75 ? 239  ASN A C     1 
ATOM   1704  O  O     . ASN A 1 219 ? -9.115  -23.327 82.364  1.00 29.87 ? 239  ASN A O     1 
ATOM   1705  C  CB    . ASN A 1 219 ? -9.614  -20.781 83.119  1.00 29.66 ? 239  ASN A CB    1 
ATOM   1706  C  CG    . ASN A 1 219 ? -8.264  -20.676 82.416  1.00 30.97 ? 239  ASN A CG    1 
ATOM   1707  O  OD1   . ASN A 1 219 ? -8.192  -20.682 81.183  1.00 31.55 ? 239  ASN A OD1   1 
ATOM   1708  N  ND2   . ASN A 1 219 ? -7.187  -20.590 83.199  1.00 31.48 ? 239  ASN A ND2   1 
ATOM   1709  N  N     . GLY A 1 220 ? -11.151 -23.744 81.500  1.00 29.86 ? 240  GLY A N     1 
ATOM   1710  C  CA    . GLY A 1 220 ? -10.821 -25.084 81.017  1.00 30.04 ? 240  GLY A CA    1 
ATOM   1711  C  C     . GLY A 1 220 ? -11.210 -26.231 81.930  1.00 30.25 ? 240  GLY A C     1 
ATOM   1712  O  O     . GLY A 1 220 ? -11.034 -27.388 81.556  1.00 30.20 ? 240  GLY A O     1 
ATOM   1713  N  N     . LYS A 1 221 ? -11.728 -25.932 83.123  1.00 30.50 ? 241  LYS A N     1 
ATOM   1714  C  CA    . LYS A 1 221 ? -12.120 -26.982 84.064  1.00 30.70 ? 241  LYS A CA    1 
ATOM   1715  C  C     . LYS A 1 221 ? -13.522 -26.785 84.617  1.00 30.82 ? 241  LYS A C     1 
ATOM   1716  O  O     . LYS A 1 221 ? -13.989 -25.660 84.789  1.00 30.72 ? 241  LYS A O     1 
ATOM   1717  C  CB    . LYS A 1 221 ? -11.148 -27.050 85.240  1.00 30.81 ? 241  LYS A CB    1 
ATOM   1718  C  CG    . LYS A 1 221 ? -9.742  -27.462 84.878  1.00 31.27 ? 241  LYS A CG    1 
ATOM   1719  C  CD    . LYS A 1 221 ? -8.884  -27.602 86.144  1.00 31.32 ? 241  LYS A CD    1 
ATOM   1720  N  N     . PHE A 1 222 ? -14.170 -27.905 84.913  1.00 31.22 ? 242  PHE A N     1 
ATOM   1721  C  CA    . PHE A 1 222 ? -15.456 -27.912 85.571  1.00 31.51 ? 242  PHE A CA    1 
ATOM   1722  C  C     . PHE A 1 222 ? -15.210 -27.957 87.064  1.00 32.12 ? 242  PHE A C     1 
ATOM   1723  O  O     . PHE A 1 222 ? -14.188 -28.489 87.506  1.00 32.26 ? 242  PHE A O     1 
ATOM   1724  C  CB    . PHE A 1 222 ? -16.272 -29.113 85.117  1.00 31.36 ? 242  PHE A CB    1 
ATOM   1725  C  CG    . PHE A 1 222 ? -16.706 -29.037 83.686  1.00 31.61 ? 242  PHE A CG    1 
ATOM   1726  C  CD1   . PHE A 1 222 ? -17.855 -28.343 83.332  1.00 31.37 ? 242  PHE A CD1   1 
ATOM   1727  C  CD2   . PHE A 1 222 ? -15.968 -29.663 82.688  1.00 32.47 ? 242  PHE A CD2   1 
ATOM   1728  C  CE1   . PHE A 1 222 ? -18.267 -28.268 82.001  1.00 31.52 ? 242  PHE A CE1   1 
ATOM   1729  C  CE2   . PHE A 1 222 ? -16.372 -29.596 81.357  1.00 32.47 ? 242  PHE A CE2   1 
ATOM   1730  C  CZ    . PHE A 1 222 ? -17.523 -28.891 81.013  1.00 31.98 ? 242  PHE A CZ    1 
ATOM   1731  N  N     . TYR A 1 223 ? -16.133 -27.388 87.837  1.00 32.74 ? 243  TYR A N     1 
ATOM   1732  C  CA    . TYR A 1 223 ? -15.945 -27.274 89.287  1.00 33.09 ? 243  TYR A CA    1 
ATOM   1733  C  C     . TYR A 1 223 ? -17.139 -27.668 90.144  1.00 33.63 ? 243  TYR A C     1 
ATOM   1734  O  O     . TYR A 1 223 ? -17.022 -27.682 91.369  1.00 34.96 ? 243  TYR A O     1 
ATOM   1735  C  CB    . TYR A 1 223 ? -15.525 -25.847 89.646  1.00 32.95 ? 243  TYR A CB    1 
ATOM   1736  C  CG    . TYR A 1 223 ? -14.096 -25.561 89.309  1.00 32.49 ? 243  TYR A CG    1 
ATOM   1737  C  CD1   . TYR A 1 223 ? -13.760 -24.866 88.154  1.00 32.24 ? 243  TYR A CD1   1 
ATOM   1738  C  CD2   . TYR A 1 223 ? -13.071 -26.005 90.130  1.00 31.60 ? 243  TYR A CD2   1 
ATOM   1739  C  CE1   . TYR A 1 223 ? -12.443 -24.607 87.835  1.00 31.40 ? 243  TYR A CE1   1 
ATOM   1740  C  CE2   . TYR A 1 223 ? -11.748 -25.753 89.815  1.00 31.42 ? 243  TYR A CE2   1 
ATOM   1741  C  CZ    . TYR A 1 223 ? -11.441 -25.055 88.669  1.00 31.24 ? 243  TYR A CZ    1 
ATOM   1742  O  OH    . TYR A 1 223 ? -10.127 -24.801 88.352  1.00 32.91 ? 243  TYR A OH    1 
ATOM   1743  N  N     . GLY A 1 224 ? -18.289 -27.957 89.551  1.00 33.55 ? 244  GLY A N     1 
ATOM   1744  C  CA    . GLY A 1 224 ? -19.413 -28.473 90.344  1.00 33.69 ? 244  GLY A CA    1 
ATOM   1745  C  C     . GLY A 1 224 ? -20.274 -27.406 91.002  1.00 33.51 ? 244  GLY A C     1 
ATOM   1746  O  O     . GLY A 1 224 ? -21.487 -27.398 90.812  1.00 34.02 ? 244  GLY A O     1 
ATOM   1747  N  N     . SER A 1 225 ? -19.655 -26.518 91.781  1.00 33.35 ? 245  SER A N     1 
ATOM   1748  C  CA    . SER A 1 225 ? -20.369 -25.424 92.455  1.00 33.06 ? 245  SER A CA    1 
ATOM   1749  C  C     . SER A 1 225 ? -19.507 -24.163 92.557  1.00 33.01 ? 245  SER A C     1 
ATOM   1750  O  O     . SER A 1 225 ? -18.286 -24.239 92.458  1.00 32.69 ? 245  SER A O     1 
ATOM   1751  C  CB    . SER A 1 225 ? -20.764 -25.846 93.875  1.00 33.13 ? 245  SER A CB    1 
ATOM   1752  O  OG    . SER A 1 225 ? -19.644 -25.776 94.758  1.00 33.11 ? 245  SER A OG    1 
ATOM   1753  N  N     . PRO A 1 226 ? -20.145 -22.997 92.780  1.00 33.01 ? 246  PRO A N     1 
ATOM   1754  C  CA    . PRO A 1 226 ? -19.385 -21.786 93.097  1.00 33.08 ? 246  PRO A CA    1 
ATOM   1755  C  C     . PRO A 1 226 ? -18.465 -21.944 94.320  1.00 33.23 ? 246  PRO A C     1 
ATOM   1756  O  O     . PRO A 1 226 ? -17.316 -21.486 94.292  1.00 33.12 ? 246  PRO A O     1 
ATOM   1757  C  CB    . PRO A 1 226 ? -20.476 -20.751 93.373  1.00 33.22 ? 246  PRO A CB    1 
ATOM   1758  C  CG    . PRO A 1 226 ? -21.671 -21.238 92.610  1.00 33.32 ? 246  PRO A CG    1 
ATOM   1759  C  CD    . PRO A 1 226 ? -21.580 -22.725 92.570  1.00 32.89 ? 246  PRO A CD    1 
ATOM   1760  N  N     . GLU A 1 227 ? -18.964 -22.602 95.366  1.00 33.32 ? 247  GLU A N     1 
ATOM   1761  C  CA    . GLU A 1 227 ? -18.187 -22.819 96.595  1.00 33.63 ? 247  GLU A CA    1 
ATOM   1762  C  C     . GLU A 1 227 ? -16.905 -23.611 96.339  1.00 33.64 ? 247  GLU A C     1 
ATOM   1763  O  O     . GLU A 1 227 ? -15.839 -23.264 96.861  1.00 33.84 ? 247  GLU A O     1 
ATOM   1764  C  CB    . GLU A 1 227 ? -19.039 -23.527 97.660  1.00 33.60 ? 247  GLU A CB    1 
ATOM   1765  N  N     . GLU A 1 228 ? -16.999 -24.655 95.520  1.00 33.68 ? 248  GLU A N     1 
ATOM   1766  C  CA    . GLU A 1 228 ? -15.835 -25.480 95.199  1.00 33.88 ? 248  GLU A CA    1 
ATOM   1767  C  C     . GLU A 1 228 ? -14.764 -24.669 94.476  1.00 34.08 ? 248  GLU A C     1 
ATOM   1768  O  O     . GLU A 1 228 ? -13.583 -24.764 94.809  1.00 34.38 ? 248  GLU A O     1 
ATOM   1769  C  CB    . GLU A 1 228 ? -16.242 -26.696 94.363  1.00 33.74 ? 248  GLU A CB    1 
ATOM   1770  C  CG    . GLU A 1 228 ? -15.087 -27.608 93.957  0.50 33.73 ? 248  GLU A CG    1 
ATOM   1771  C  CD    . GLU A 1 228 ? -15.547 -28.850 93.211  0.50 33.65 ? 248  GLU A CD    1 
ATOM   1772  O  OE1   . GLU A 1 228 ? -16.614 -29.402 93.554  0.50 33.75 ? 248  GLU A OE1   1 
ATOM   1773  O  OE2   . GLU A 1 228 ? -14.843 -29.272 92.274  0.50 33.35 ? 248  GLU A OE2   1 
ATOM   1774  N  N     . LEU A 1 229 ? -15.163 -23.874 93.485  1.00 34.20 ? 249  LEU A N     1 
ATOM   1775  C  CA    . LEU A 1 229 ? -14.197 -22.996 92.797  1.00 34.08 ? 249  LEU A CA    1 
ATOM   1776  C  C     . LEU A 1 229 ? -13.593 -21.982 93.792  1.00 34.20 ? 249  LEU A C     1 
ATOM   1777  O  O     . LEU A 1 229 ? -12.382 -21.747 93.796  1.00 33.97 ? 249  LEU A O     1 
ATOM   1778  C  CB    . LEU A 1 229 ? -14.861 -22.276 91.615  1.00 33.71 ? 249  LEU A CB    1 
ATOM   1779  C  CG    . LEU A 1 229 ? -14.021 -21.270 90.824  1.00 33.86 ? 249  LEU A CG    1 
ATOM   1780  C  CD1   . LEU A 1 229 ? -12.704 -21.898 90.311  1.00 32.22 ? 249  LEU A CD1   1 
ATOM   1781  C  CD2   . LEU A 1 229 ? -14.846 -20.678 89.665  1.00 32.84 ? 249  LEU A CD2   1 
ATOM   1782  N  N     . ALA A 1 230 ? -14.446 -21.397 94.628  1.00 34.22 ? 250  ALA A N     1 
ATOM   1783  C  CA    . ALA A 1 230 ? -13.999 -20.474 95.674  1.00 34.82 ? 250  ALA A CA    1 
ATOM   1784  C  C     . ALA A 1 230 ? -12.946 -21.132 96.573  1.00 35.25 ? 250  ALA A C     1 
ATOM   1785  O  O     . ALA A 1 230 ? -11.870 -20.575 96.803  1.00 35.50 ? 250  ALA A O     1 
ATOM   1786  C  CB    . ALA A 1 230 ? -15.183 -20.015 96.501  1.00 34.35 ? 250  ALA A CB    1 
ATOM   1787  N  N     . ARG A 1 231 ? -13.263 -22.329 97.056  1.00 35.91 ? 251  ARG A N     1 
ATOM   1788  C  CA    . ARG A 1 231 ? -12.351 -23.099 97.902  1.00 36.28 ? 251  ARG A CA    1 
ATOM   1789  C  C     . ARG A 1 231 ? -11.009 -23.318 97.208  1.00 36.78 ? 251  ARG A C     1 
ATOM   1790  O  O     . ARG A 1 231 ? -9.954  -22.890 97.716  1.00 37.00 ? 251  ARG A O     1 
ATOM   1791  C  CB    . ARG A 1 231 ? -12.976 -24.450 98.260  1.00 36.12 ? 251  ARG A CB    1 
ATOM   1792  N  N     . LYS A 1 232 ? -11.056 -23.976 96.049  1.00 36.89 ? 252  LYS A N     1 
ATOM   1793  C  CA    . LYS A 1 232 ? -9.844  -24.320 95.301  1.00 37.15 ? 252  LYS A CA    1 
ATOM   1794  C  C     . LYS A 1 232 ? -9.025  -23.086 94.947  1.00 37.35 ? 252  LYS A C     1 
ATOM   1795  O  O     . LYS A 1 232 ? -7.793  -23.132 94.950  1.00 37.55 ? 252  LYS A O     1 
ATOM   1796  C  CB    . LYS A 1 232 ? -10.182 -25.110 94.036  1.00 37.31 ? 252  LYS A CB    1 
ATOM   1797  C  CG    . LYS A 1 232 ? -10.653 -26.533 94.310  1.00 37.74 ? 252  LYS A CG    1 
ATOM   1798  C  CD    . LYS A 1 232 ? -10.754 -27.355 93.033  1.00 38.33 ? 252  LYS A CD    1 
ATOM   1799  N  N     . TYR A 1 233 ? -9.704  -21.983 94.654  1.00 37.44 ? 253  TYR A N     1 
ATOM   1800  C  CA    . TYR A 1 233 ? -9.016  -20.717 94.439  1.00 37.68 ? 253  TYR A CA    1 
ATOM   1801  C  C     . TYR A 1 233 ? -8.347  -20.218 95.714  1.00 38.11 ? 253  TYR A C     1 
ATOM   1802  O  O     . TYR A 1 233 ? -7.196  -19.787 95.678  1.00 38.17 ? 253  TYR A O     1 
ATOM   1803  C  CB    . TYR A 1 233 ? -9.974  -19.647 93.938  1.00 37.41 ? 253  TYR A CB    1 
ATOM   1804  C  CG    . TYR A 1 233 ? -9.343  -18.280 93.875  1.00 36.75 ? 253  TYR A CG    1 
ATOM   1805  C  CD1   . TYR A 1 233 ? -8.265  -18.033 93.036  1.00 36.15 ? 253  TYR A CD1   1 
ATOM   1806  C  CD2   . TYR A 1 233 ? -9.818  -17.235 94.660  1.00 36.39 ? 253  TYR A CD2   1 
ATOM   1807  C  CE1   . TYR A 1 233 ? -7.683  -16.777 92.967  1.00 36.43 ? 253  TYR A CE1   1 
ATOM   1808  C  CE2   . TYR A 1 233 ? -9.239  -15.978 94.604  1.00 36.80 ? 253  TYR A CE2   1 
ATOM   1809  C  CZ    . TYR A 1 233 ? -8.173  -15.756 93.756  1.00 36.94 ? 253  TYR A CZ    1 
ATOM   1810  O  OH    . TYR A 1 233 ? -7.599  -14.508 93.697  1.00 38.46 ? 253  TYR A OH    1 
ATOM   1811  N  N     . ALA A 1 234 ? -9.081  -20.245 96.823  1.00 38.73 ? 254  ALA A N     1 
ATOM   1812  C  CA    . ALA A 1 234 ? -8.533  -19.834 98.117  1.00 39.45 ? 254  ALA A CA    1 
ATOM   1813  C  C     . ALA A 1 234 ? -7.291  -20.668 98.444  1.00 39.99 ? 254  ALA A C     1 
ATOM   1814  O  O     . ALA A 1 234 ? -6.265  -20.124 98.842  1.00 40.06 ? 254  ALA A O     1 
ATOM   1815  C  CB    . ALA A 1 234 ? -9.585  -19.964 99.222  1.00 39.16 ? 254  ALA A CB    1 
ATOM   1816  N  N     . ASP A 1 235 ? -7.373  -21.976 98.208  1.00 40.80 ? 255  ASP A N     1 
ATOM   1817  C  CA    . ASP A 1 235 ? -6.258  -22.898 98.463  1.00 41.50 ? 255  ASP A CA    1 
ATOM   1818  C  C     . ASP A 1 235 ? -5.170  -22.887 97.379  1.00 41.77 ? 255  ASP A C     1 
ATOM   1819  O  O     . ASP A 1 235 ? -4.334  -23.799 97.327  1.00 41.97 ? 255  ASP A O     1 
ATOM   1820  C  CB    . ASP A 1 235 ? -6.783  -24.339 98.629  1.00 41.73 ? 255  ASP A CB    1 
ATOM   1821  C  CG    . ASP A 1 235 ? -7.730  -24.487 99.794  1.00 42.11 ? 255  ASP A CG    1 
ATOM   1822  O  OD1   . ASP A 1 235 ? -7.783  -23.573 100.641 1.00 44.43 ? 255  ASP A OD1   1 
ATOM   1823  O  OD2   . ASP A 1 235 ? -8.423  -25.519 99.867  1.00 43.12 ? 255  ASP A OD2   1 
ATOM   1824  N  N     . GLY A 1 236 ? -5.179  -21.881 96.506  1.00 41.98 ? 256  GLY A N     1 
ATOM   1825  C  CA    . GLY A 1 236 ? -4.118  -21.725 95.511  1.00 42.06 ? 256  GLY A CA    1 
ATOM   1826  C  C     . GLY A 1 236 ? -4.025  -22.838 94.474  1.00 42.19 ? 256  GLY A C     1 
ATOM   1827  O  O     . GLY A 1 236 ? -2.977  -23.009 93.843  1.00 42.23 ? 256  GLY A O     1 
ATOM   1828  N  N     . GLU A 1 237 ? -5.119  -23.578 94.281  1.00 42.29 ? 257  GLU A N     1 
ATOM   1829  C  CA    . GLU A 1 237 ? -5.149  -24.717 93.354  1.00 42.37 ? 257  GLU A CA    1 
ATOM   1830  C  C     . GLU A 1 237 ? -5.783  -24.385 91.996  1.00 41.87 ? 257  GLU A C     1 
ATOM   1831  O  O     . GLU A 1 237 ? -6.084  -25.296 91.229  1.00 41.74 ? 257  GLU A O     1 
ATOM   1832  C  CB    . GLU A 1 237 ? -5.930  -25.891 93.957  1.00 42.72 ? 257  GLU A CB    1 
ATOM   1833  C  CG    . GLU A 1 237 ? -5.517  -26.310 95.348  1.00 44.49 ? 257  GLU A CG    1 
ATOM   1834  C  CD    . GLU A 1 237 ? -6.208  -27.594 95.781  1.00 47.10 ? 257  GLU A CD    1 
ATOM   1835  O  OE1   . GLU A 1 237 ? -6.015  -28.624 95.095  1.00 50.10 ? 257  GLU A OE1   1 
ATOM   1836  O  OE2   . GLU A 1 237 ? -6.943  -27.579 96.796  1.00 48.50 ? 257  GLU A OE2   1 
ATOM   1837  N  N     . VAL A 1 238 ? -6.002  -23.105 91.698  1.00 41.35 ? 258  VAL A N     1 
ATOM   1838  C  CA    . VAL A 1 238 ? -6.609  -22.720 90.418  1.00 40.71 ? 258  VAL A CA    1 
ATOM   1839  C  C     . VAL A 1 238 ? -5.676  -21.833 89.612  1.00 40.30 ? 258  VAL A C     1 
ATOM   1840  O  O     . VAL A 1 238 ? -5.289  -20.766 90.073  1.00 40.17 ? 258  VAL A O     1 
ATOM   1841  C  CB    . VAL A 1 238 ? -7.944  -21.977 90.615  1.00 40.61 ? 258  VAL A CB    1 
ATOM   1842  C  CG1   . VAL A 1 238 ? -8.533  -21.563 89.259  1.00 40.48 ? 258  VAL A CG1   1 
ATOM   1843  C  CG2   . VAL A 1 238 ? -8.920  -22.845 91.387  1.00 39.75 ? 258  VAL A CG2   1 
ATOM   1844  N  N     . ASP A 1 239 ? -5.325  -22.282 88.409  1.00 39.87 ? 259  ASP A N     1 
ATOM   1845  C  CA    . ASP A 1 239 ? -4.595  -21.452 87.463  1.00 39.90 ? 259  ASP A CA    1 
ATOM   1846  C  C     . ASP A 1 239 ? -5.562  -20.418 86.904  1.00 39.71 ? 259  ASP A C     1 
ATOM   1847  O  O     . ASP A 1 239 ? -6.354  -20.719 86.013  1.00 39.98 ? 259  ASP A O     1 
ATOM   1848  C  CB    . ASP A 1 239 ? -3.996  -22.299 86.333  1.00 39.98 ? 259  ASP A CB    1 
ATOM   1849  N  N     . VAL A 1 240 ? -5.510  -19.206 87.445  1.00 39.51 ? 260  VAL A N     1 
ATOM   1850  C  CA    . VAL A 1 240 ? -6.435  -18.154 87.046  1.00 39.39 ? 260  VAL A CA    1 
ATOM   1851  C  C     . VAL A 1 240 ? -5.803  -17.224 86.015  1.00 39.46 ? 260  VAL A C     1 
ATOM   1852  O  O     . VAL A 1 240 ? -4.575  -17.144 85.887  1.00 39.01 ? 260  VAL A O     1 
ATOM   1853  C  CB    . VAL A 1 240 ? -6.919  -17.320 88.256  1.00 39.52 ? 260  VAL A CB    1 
ATOM   1854  C  CG1   . VAL A 1 240 ? -7.509  -18.232 89.340  1.00 39.57 ? 260  VAL A CG1   1 
ATOM   1855  C  CG2   . VAL A 1 240 ? -5.791  -16.458 88.822  1.00 39.23 ? 260  VAL A CG2   1 
ATOM   1856  N  N     . VAL A 1 241 ? -6.663  -16.539 85.268  1.00 39.26 ? 261  VAL A N     1 
ATOM   1857  C  CA    . VAL A 1 241 ? -6.229  -15.494 84.360  1.00 39.16 ? 261  VAL A CA    1 
ATOM   1858  C  C     . VAL A 1 241 ? -6.730  -14.177 84.926  1.00 39.27 ? 261  VAL A C     1 
ATOM   1859  O  O     . VAL A 1 241 ? -7.937  -13.924 84.940  1.00 39.08 ? 261  VAL A O     1 
ATOM   1860  C  CB    . VAL A 1 241 ? -6.784  -15.700 82.944  1.00 39.13 ? 261  VAL A CB    1 
ATOM   1861  C  CG1   . VAL A 1 241 ? -6.267  -14.612 82.010  1.00 38.03 ? 261  VAL A CG1   1 
ATOM   1862  C  CG2   . VAL A 1 241 ? -6.412  -17.082 82.428  1.00 38.82 ? 261  VAL A CG2   1 
ATOM   1863  N  N     . VAL A 1 242 ? -5.799  -13.363 85.413  1.00 39.41 ? 262  VAL A N     1 
ATOM   1864  C  CA    . VAL A 1 242 ? -6.101  -12.034 85.928  1.00 39.77 ? 262  VAL A CA    1 
ATOM   1865  C  C     . VAL A 1 242 ? -6.209  -11.062 84.751  1.00 40.48 ? 262  VAL A C     1 
ATOM   1866  O  O     . VAL A 1 242 ? -5.229  -10.820 84.044  1.00 40.34 ? 262  VAL A O     1 
ATOM   1867  C  CB    . VAL A 1 242 ? -5.002  -11.546 86.904  1.00 39.80 ? 262  VAL A CB    1 
ATOM   1868  C  CG1   . VAL A 1 242 ? -5.298  -10.127 87.383  1.00 39.62 ? 262  VAL A CG1   1 
ATOM   1869  C  CG2   . VAL A 1 242 ? -4.862  -12.509 88.087  1.00 38.86 ? 262  VAL A CG2   1 
ATOM   1870  N  N     . LEU A 1 243 ? -7.403  -10.516 84.541  1.00 41.29 ? 263  LEU A N     1 
ATOM   1871  C  CA    . LEU A 1 243 ? -7.657  -9.609  83.419  1.00 41.99 ? 263  LEU A CA    1 
ATOM   1872  C  C     . LEU A 1 243 ? -7.159  -8.211  83.767  1.00 43.12 ? 263  LEU A C     1 
ATOM   1873  O  O     . LEU A 1 243 ? -7.288  -7.777  84.917  1.00 43.23 ? 263  LEU A O     1 
ATOM   1874  C  CB    . LEU A 1 243 ? -9.156  -9.543  83.115  1.00 41.66 ? 263  LEU A CB    1 
ATOM   1875  C  CG    . LEU A 1 243 ? -9.892  -10.869 82.964  1.00 41.07 ? 263  LEU A CG    1 
ATOM   1876  C  CD1   . LEU A 1 243 ? -11.367 -10.620 82.762  1.00 40.31 ? 263  LEU A CD1   1 
ATOM   1877  C  CD2   . LEU A 1 243 ? -9.308  -11.680 81.822  1.00 40.42 ? 263  LEU A CD2   1 
ATOM   1878  N  N     . GLU A 1 244 ? -6.616  -7.502  82.780  1.00 44.46 ? 264  GLU A N     1 
ATOM   1879  C  CA    . GLU A 1 244 ? -6.165  -6.118  82.989  1.00 45.56 ? 264  GLU A CA    1 
ATOM   1880  C  C     . GLU A 1 244 ? -7.358  -5.179  83.190  1.00 46.65 ? 264  GLU A C     1 
ATOM   1881  O  O     . GLU A 1 244 ? -8.509  -5.559  82.953  1.00 46.60 ? 264  GLU A O     1 
ATOM   1882  C  CB    . GLU A 1 244 ? -5.304  -5.634  81.818  1.00 45.42 ? 264  GLU A CB    1 
ATOM   1883  N  N     . ASP A 1 245 ? -7.068  -3.962  83.644  1.00 47.90 ? 265  ASP A N     1 
ATOM   1884  C  CA    . ASP A 1 245 ? -8.090  -2.941  83.871  1.00 49.05 ? 265  ASP A CA    1 
ATOM   1885  C  C     . ASP A 1 245 ? -8.570  -2.429  82.514  1.00 49.71 ? 265  ASP A C     1 
ATOM   1886  O  O     . ASP A 1 245 ? -7.748  -2.048  81.683  1.00 50.05 ? 265  ASP A O     1 
ATOM   1887  C  CB    . ASP A 1 245 ? -7.498  -1.788  84.705  1.00 49.22 ? 265  ASP A CB    1 
ATOM   1888  C  CG    . ASP A 1 245 ? -8.548  -0.784  85.193  1.00 50.01 ? 265  ASP A CG    1 
ATOM   1889  O  OD1   . ASP A 1 245 ? -9.663  -0.708  84.634  1.00 51.29 ? 265  ASP A OD1   1 
ATOM   1890  O  OD2   . ASP A 1 245 ? -8.247  -0.042  86.151  1.00 51.78 ? 265  ASP A OD2   1 
ATOM   1891  N  N     . PRO A 1 246 ? -9.894  -2.446  82.270  1.00 50.49 ? 266  PRO A N     1 
ATOM   1892  C  CA    . PRO A 1 246 ? -10.430 -1.832  81.054  1.00 51.00 ? 266  PRO A CA    1 
ATOM   1893  C  C     . PRO A 1 246 ? -10.719 -0.342  81.227  1.00 51.61 ? 266  PRO A C     1 
ATOM   1894  O  O     . PRO A 1 246 ? -10.417 0.441   80.325  1.00 52.28 ? 266  PRO A O     1 
ATOM   1895  C  CB    . PRO A 1 246 ? -11.727 -2.611  80.805  1.00 50.92 ? 266  PRO A CB    1 
ATOM   1896  C  CG    . PRO A 1 246 ? -12.159 -3.078  82.139  1.00 50.46 ? 266  PRO A CG    1 
ATOM   1897  C  CD    . PRO A 1 246 ? -10.937 -3.167  83.024  1.00 50.55 ? 266  PRO A CD    1 
ATOM   1898  N  N     . LEU A 1 247 ? -11.294 0.038   82.371  1.00 52.06 ? 267  LEU A N     1 
ATOM   1899  C  CA    . LEU A 1 247 ? -11.661 1.427   82.653  1.00 52.14 ? 267  LEU A CA    1 
ATOM   1900  C  C     . LEU A 1 247 ? -10.532 2.135   83.401  1.00 52.42 ? 267  LEU A C     1 
ATOM   1901  O  O     . LEU A 1 247 ? -9.473  2.405   82.831  1.00 52.69 ? 267  LEU A O     1 
ATOM   1902  C  CB    . LEU A 1 247 ? -12.938 1.480   83.495  1.00 52.25 ? 267  LEU A CB    1 
ATOM   1903  C  CG    . LEU A 1 247 ? -14.147 0.683   82.993  1.00 52.19 ? 267  LEU A CG    1 
ATOM   1904  C  CD1   . LEU A 1 247 ? -15.277 0.762   84.003  1.00 51.98 ? 267  LEU A CD1   1 
ATOM   1905  C  CD2   . LEU A 1 247 ? -14.599 1.175   81.622  1.00 52.05 ? 267  LEU A CD2   1 
ATOM   1906  N  N     . GLU A 1 258 ? -6.616  6.716   77.372  1.00 39.27 ? 278  GLU A N     1 
ATOM   1907  C  CA    . GLU A 1 258 ? -6.719  7.588   76.210  1.00 39.04 ? 278  GLU A CA    1 
ATOM   1908  C  C     . GLU A 1 258 ? -7.188  6.821   74.969  1.00 38.73 ? 278  GLU A C     1 
ATOM   1909  O  O     . GLU A 1 258 ? -8.172  7.220   74.338  1.00 39.30 ? 278  GLU A O     1 
ATOM   1910  C  CB    . GLU A 1 258 ? -5.380  8.285   75.933  1.00 39.10 ? 278  GLU A CB    1 
ATOM   1911  N  N     . PRO A 1 259 ? -6.498  5.719   74.609  1.00 37.91 ? 279  PRO A N     1 
ATOM   1912  C  CA    . PRO A 1 259 ? -6.926  5.004   73.393  1.00 37.07 ? 279  PRO A CA    1 
ATOM   1913  C  C     . PRO A 1 259 ? -8.328  4.410   73.522  1.00 36.05 ? 279  PRO A C     1 
ATOM   1914  O  O     . PRO A 1 259 ? -8.750  4.081   74.628  1.00 36.22 ? 279  PRO A O     1 
ATOM   1915  C  CB    . PRO A 1 259 ? -5.892  3.878   73.244  1.00 37.20 ? 279  PRO A CB    1 
ATOM   1916  C  CG    . PRO A 1 259 ? -4.754  4.243   74.149  1.00 37.74 ? 279  PRO A CG    1 
ATOM   1917  C  CD    . PRO A 1 259 ? -5.344  5.066   75.255  1.00 38.15 ? 279  PRO A CD    1 
ATOM   1918  N  N     . PRO A 1 260 ? -9.053  4.270   72.401  1.00 34.61 ? 280  PRO A N     1 
ATOM   1919  C  CA    . PRO A 1 260 ? -10.338 3.577   72.487  1.00 33.63 ? 280  PRO A CA    1 
ATOM   1920  C  C     . PRO A 1 260 ? -10.201 2.125   72.946  1.00 32.35 ? 280  PRO A C     1 
ATOM   1921  O  O     . PRO A 1 260 ? -9.177  1.490   72.711  1.00 31.78 ? 280  PRO A O     1 
ATOM   1922  C  CB    . PRO A 1 260 ? -10.863 3.625   71.044  1.00 33.76 ? 280  PRO A CB    1 
ATOM   1923  C  CG    . PRO A 1 260 ? -10.173 4.775   70.422  1.00 34.12 ? 280  PRO A CG    1 
ATOM   1924  C  CD    . PRO A 1 260 ? -8.805  4.790   71.044  1.00 34.59 ? 280  PRO A CD    1 
ATOM   1925  N  N     . LEU A 1 261 ? -11.234 1.622   73.608  1.00 31.21 ? 281  LEU A N     1 
ATOM   1926  C  CA    . LEU A 1 261 ? -11.324 0.208   73.947  1.00 30.59 ? 281  LEU A CA    1 
ATOM   1927  C  C     . LEU A 1 261 ? -11.413 -0.579  72.639  1.00 29.89 ? 281  LEU A C     1 
ATOM   1928  O  O     . LEU A 1 261 ? -12.082 -0.140  71.696  1.00 29.36 ? 281  LEU A O     1 
ATOM   1929  C  CB    . LEU A 1 261 ? -12.569 -0.034  74.814  1.00 30.48 ? 281  LEU A CB    1 
ATOM   1930  C  CG    . LEU A 1 261 ? -12.584 -1.198  75.798  1.00 31.16 ? 281  LEU A CG    1 
ATOM   1931  C  CD1   . LEU A 1 261 ? -11.367 -1.182  76.709  1.00 30.65 ? 281  LEU A CD1   1 
ATOM   1932  C  CD2   . LEU A 1 261 ? -13.885 -1.152  76.625  1.00 31.57 ? 281  LEU A CD2   1 
ATOM   1933  N  N     . PHE A 1 262 ? -10.729 -1.719  72.559  1.00 29.07 ? 282  PHE A N     1 
ATOM   1934  C  CA    . PHE A 1 262 ? -10.736 -2.512  71.322  1.00 28.61 ? 282  PHE A CA    1 
ATOM   1935  C  C     . PHE A 1 262 ? -12.161 -2.823  70.849  1.00 27.75 ? 282  PHE A C     1 
ATOM   1936  O  O     . PHE A 1 262 ? -12.383 -2.980  69.655  1.00 27.58 ? 282  PHE A O     1 
ATOM   1937  C  CB    . PHE A 1 262 ? -9.902  -3.802  71.454  1.00 28.61 ? 282  PHE A CB    1 
ATOM   1938  C  CG    . PHE A 1 262 ? -10.572 -4.904  72.250  1.00 29.70 ? 282  PHE A CG    1 
ATOM   1939  C  CD1   . PHE A 1 262 ? -11.429 -5.805  71.632  1.00 29.90 ? 282  PHE A CD1   1 
ATOM   1940  C  CD2   . PHE A 1 262 ? -10.316 -5.062  73.605  1.00 29.64 ? 282  PHE A CD2   1 
ATOM   1941  C  CE1   . PHE A 1 262 ? -12.041 -6.818  72.358  1.00 29.43 ? 282  PHE A CE1   1 
ATOM   1942  C  CE2   . PHE A 1 262 ? -10.920 -6.079  74.328  1.00 29.46 ? 282  PHE A CE2   1 
ATOM   1943  C  CZ    . PHE A 1 262 ? -11.783 -6.950  73.707  1.00 29.61 ? 282  PHE A CZ    1 
ATOM   1944  N  N     . SER A 1 263 ? -13.117 -2.885  71.779  1.00 26.70 ? 283  SER A N     1 
ATOM   1945  C  CA    . SER A 1 263 ? -14.511 -3.210  71.456  1.00 25.93 ? 283  SER A CA    1 
ATOM   1946  C  C     . SER A 1 263 ? -15.384 -1.988  71.171  1.00 25.45 ? 283  SER A C     1 
ATOM   1947  O  O     . SER A 1 263 ? -16.605 -2.121  71.038  1.00 25.04 ? 283  SER A O     1 
ATOM   1948  C  CB    . SER A 1 263 ? -15.135 -4.025  72.590  1.00 26.00 ? 283  SER A CB    1 
ATOM   1949  O  OG    . SER A 1 263 ? -15.076 -3.317  73.809  1.00 25.72 ? 283  SER A OG    1 
ATOM   1950  N  N     . SER A 1 264 ? -14.755 -0.815  71.091  1.00 25.09 ? 284  SER A N     1 
ATOM   1951  C  CA    A SER A 1 264 ? -15.426 0.432   70.741  0.50 24.83 ? 284  SER A CA    1 
ATOM   1952  C  CA    B SER A 1 264 ? -15.439 0.428   70.738  0.50 25.25 ? 284  SER A CA    1 
ATOM   1953  C  C     . SER A 1 264 ? -15.384 0.673   69.234  1.00 25.24 ? 284  SER A C     1 
ATOM   1954  O  O     . SER A 1 264 ? -14.457 0.232   68.562  1.00 25.26 ? 284  SER A O     1 
ATOM   1955  C  CB    A SER A 1 264 ? -14.745 1.609   71.446  0.50 24.68 ? 284  SER A CB    1 
ATOM   1956  C  CB    B SER A 1 264 ? -14.814 1.627   71.466  0.50 25.17 ? 284  SER A CB    1 
ATOM   1957  O  OG    A SER A 1 264 ? -15.328 2.840   71.070  0.50 22.41 ? 284  SER A OG    1 
ATOM   1958  O  OG    B SER A 1 264 ? -13.528 1.940   70.961  0.50 25.49 ? 284  SER A OG    1 
ATOM   1959  N  N     . HIS A 1 265 ? -16.379 1.398   68.718  1.00 25.77 ? 285  HIS A N     1 
ATOM   1960  C  CA    . HIS A 1 265 ? -16.379 1.827   67.319  1.00 26.33 ? 285  HIS A CA    1 
ATOM   1961  C  C     . HIS A 1 265 ? -15.551 3.108   67.107  1.00 27.10 ? 285  HIS A C     1 
ATOM   1962  O  O     . HIS A 1 265 ? -15.398 3.557   65.974  1.00 27.09 ? 285  HIS A O     1 
ATOM   1963  C  CB    . HIS A 1 265 ? -17.804 2.086   66.818  1.00 26.29 ? 285  HIS A CB    1 
ATOM   1964  C  CG    . HIS A 1 265 ? -18.565 0.847   66.464  1.00 26.09 ? 285  HIS A CG    1 
ATOM   1965  N  ND1   . HIS A 1 265 ? -19.081 -0.006  67.414  1.00 26.56 ? 285  HIS A ND1   1 
ATOM   1966  C  CD2   . HIS A 1 265 ? -18.942 0.346   65.266  1.00 26.01 ? 285  HIS A CD2   1 
ATOM   1967  C  CE1   . HIS A 1 265 ? -19.725 -0.991  66.816  1.00 25.88 ? 285  HIS A CE1   1 
ATOM   1968  N  NE2   . HIS A 1 265 ? -19.660 -0.797  65.514  1.00 26.07 ? 285  HIS A NE2   1 
ATOM   1969  N  N     . LYS A 1 266 ? -15.033 3.704   68.178  1.00 27.64 ? 286  LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 266 ? -14.313 4.973   68.060  1.00 28.55 ? 286  LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 266 ? -13.110 4.852   67.114  1.00 28.60 ? 286  LYS A C     1 
ATOM   1972  O  O     . LYS A 1 266 ? -12.363 3.880   67.184  1.00 28.66 ? 286  LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 266 ? -13.841 5.453   69.428  1.00 28.84 ? 286  LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 266 ? -14.952 5.963   70.321  1.00 30.60 ? 286  LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 266 ? -14.431 6.222   71.736  1.00 33.19 ? 286  LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 266 ? -15.475 6.915   72.608  1.00 34.53 ? 286  LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 266 ? -15.050 6.949   74.045  1.00 36.53 ? 286  LYS A NZ    1 
ATOM   1978  N  N     . PRO A 1 267 ? -12.927 5.832   66.214  1.00 28.75 ? 287  PRO A N     1 
ATOM   1979  C  CA    . PRO A 1 267 ? -11.808 5.713   65.273  1.00 28.96 ? 287  PRO A CA    1 
ATOM   1980  C  C     . PRO A 1 267 ? -10.434 5.659   65.935  1.00 29.02 ? 287  PRO A C     1 
ATOM   1981  O  O     . PRO A 1 267 ? -10.205 6.314   66.950  1.00 29.29 ? 287  PRO A O     1 
ATOM   1982  C  CB    . PRO A 1 267 ? -11.932 6.974   64.414  1.00 29.23 ? 287  PRO A CB    1 
ATOM   1983  C  CG    . PRO A 1 267 ? -13.347 7.371   64.508  1.00 29.08 ? 287  PRO A CG    1 
ATOM   1984  C  CD    . PRO A 1 267 ? -13.816 6.954   65.871  1.00 28.72 ? 287  PRO A CD    1 
ATOM   1985  N  N     . ARG A 1 268 ? -9.547  4.850   65.374  1.00 29.05 ? 288  ARG A N     1 
ATOM   1986  C  CA    . ARG A 1 268 ? -8.130  4.890   65.708  1.00 29.06 ? 288  ARG A CA    1 
ATOM   1987  C  C     . ARG A 1 268 ? -7.334  4.448   64.495  1.00 29.74 ? 288  ARG A C     1 
ATOM   1988  O  O     . ARG A 1 268 ? -7.883  3.821   63.581  1.00 29.38 ? 288  ARG A O     1 
ATOM   1989  C  CB    . ARG A 1 268 ? -7.800  4.009   66.917  1.00 29.17 ? 288  ARG A CB    1 
ATOM   1990  C  CG    . ARG A 1 268 ? -8.163  2.531   66.798  1.00 28.47 ? 288  ARG A CG    1 
ATOM   1991  C  CD    . ARG A 1 268 ? -9.569  2.236   67.306  1.00 28.47 ? 288  ARG A CD    1 
ATOM   1992  N  NE    . ARG A 1 268 ? -9.801  0.802   67.493  1.00 28.39 ? 288  ARG A NE    1 
ATOM   1993  C  CZ    . ARG A 1 268 ? -10.928 0.265   67.960  1.00 27.84 ? 288  ARG A CZ    1 
ATOM   1994  N  NH1   . ARG A 1 268 ? -11.959 1.026   68.310  1.00 27.43 ? 288  ARG A NH1   1 
ATOM   1995  N  NH2   . ARG A 1 268 ? -11.027 -1.053  68.071  1.00 29.28 ? 288  ARG A NH2   1 
ATOM   1996  N  N     . GLY A 1 269 ? -6.041  4.775   64.500  1.00 30.50 ? 289  GLY A N     1 
ATOM   1997  C  CA    . GLY A 1 269 ? -5.181  4.613   63.328  1.00 30.92 ? 289  GLY A CA    1 
ATOM   1998  C  C     . GLY A 1 269 ? -5.444  5.711   62.310  1.00 31.55 ? 289  GLY A C     1 
ATOM   1999  O  O     . GLY A 1 269 ? -6.423  6.453   62.418  1.00 31.85 ? 289  GLY A O     1 
ATOM   2000  N  N     . ASP A 1 270 ? -4.563  5.816   61.321  1.00 32.26 ? 290  ASP A N     1 
ATOM   2001  C  CA    . ASP A 1 270 ? -4.697  6.797   60.250  1.00 32.99 ? 290  ASP A CA    1 
ATOM   2002  C  C     . ASP A 1 270 ? -4.433  6.130   58.917  1.00 33.08 ? 290  ASP A C     1 
ATOM   2003  O  O     . ASP A 1 270 ? -3.485  5.357   58.790  1.00 33.35 ? 290  ASP A O     1 
ATOM   2004  C  CB    . ASP A 1 270 ? -3.677  7.927   60.414  1.00 33.57 ? 290  ASP A CB    1 
ATOM   2005  C  CG    . ASP A 1 270 ? -3.766  8.606   61.759  1.00 34.56 ? 290  ASP A CG    1 
ATOM   2006  O  OD1   . ASP A 1 270 ? -4.689  9.425   61.958  1.00 36.47 ? 290  ASP A OD1   1 
ATOM   2007  O  OD2   . ASP A 1 270 ? -2.905  8.315   62.616  1.00 36.64 ? 290  ASP A OD2   1 
ATOM   2008  N  N     . PHE A 1 271 ? -5.250  6.444   57.919  1.00 33.14 ? 291  PHE A N     1 
ATOM   2009  C  CA    . PHE A 1 271 ? -4.971  6.015   56.554  1.00 33.12 ? 291  PHE A CA    1 
ATOM   2010  C  C     . PHE A 1 271 ? -3.783  6.800   56.013  1.00 33.52 ? 291  PHE A C     1 
ATOM   2011  O  O     . PHE A 1 271 ? -3.596  7.956   56.377  1.00 33.10 ? 291  PHE A O     1 
ATOM   2012  C  CB    . PHE A 1 271 ? -6.159  6.297   55.641  1.00 33.05 ? 291  PHE A CB    1 
ATOM   2013  C  CG    . PHE A 1 271 ? -7.386  5.484   55.939  1.00 32.01 ? 291  PHE A CG    1 
ATOM   2014  C  CD1   . PHE A 1 271 ? -7.308  4.116   56.159  1.00 30.91 ? 291  PHE A CD1   1 
ATOM   2015  C  CD2   . PHE A 1 271 ? -8.635  6.085   55.939  1.00 31.32 ? 291  PHE A CD2   1 
ATOM   2016  C  CE1   . PHE A 1 271 ? -8.455  3.366   56.406  1.00 30.98 ? 291  PHE A CE1   1 
ATOM   2017  C  CE2   . PHE A 1 271 ? -9.786  5.334   56.180  1.00 31.30 ? 291  PHE A CE2   1 
ATOM   2018  C  CZ    . PHE A 1 271 ? -9.690  3.978   56.414  1.00 29.95 ? 291  PHE A CZ    1 
ATOM   2019  N  N     . PRO A 1 272 ? -2.993  6.189   55.119  1.00 34.08 ? 292  PRO A N     1 
ATOM   2020  C  CA    . PRO A 1 272 ? -1.907  6.945   54.500  1.00 34.61 ? 292  PRO A CA    1 
ATOM   2021  C  C     . PRO A 1 272 ? -2.398  8.104   53.639  1.00 35.14 ? 292  PRO A C     1 
ATOM   2022  O  O     . PRO A 1 272 ? -1.709  9.113   53.550  1.00 35.04 ? 292  PRO A O     1 
ATOM   2023  C  CB    . PRO A 1 272 ? -1.166  5.902   53.651  1.00 34.64 ? 292  PRO A CB    1 
ATOM   2024  C  CG    . PRO A 1 272 ? -2.083  4.734   53.547  1.00 34.71 ? 292  PRO A CG    1 
ATOM   2025  C  CD    . PRO A 1 272 ? -2.964  4.766   54.751  1.00 34.29 ? 292  PRO A CD    1 
ATOM   2026  N  N     . SER A 1 273 ? -3.574  7.964   53.023  1.00 35.83 ? 293  SER A N     1 
ATOM   2027  C  CA    . SER A 1 273 ? -4.157  9.041   52.213  1.00 36.42 ? 293  SER A CA    1 
ATOM   2028  C  C     . SER A 1 273 ? -5.350  9.678   52.931  1.00 36.70 ? 293  SER A C     1 
ATOM   2029  O  O     . SER A 1 273 ? -6.467  9.178   52.804  1.00 37.34 ? 293  SER A O     1 
ATOM   2030  C  CB    . SER A 1 273 ? -4.590  8.511   50.841  1.00 36.33 ? 293  SER A CB    1 
ATOM   2031  N  N     . PRO A 1 274 ? -5.128  10.804  53.648  1.00 36.86 ? 294  PRO A N     1 
ATOM   2032  C  CA    . PRO A 1 274 ? -6.167  11.408  54.505  1.00 36.85 ? 294  PRO A CA    1 
ATOM   2033  C  C     . PRO A 1 274 ? -7.483  11.738  53.794  1.00 36.82 ? 294  PRO A C     1 
ATOM   2034  O  O     . PRO A 1 274 ? -7.466  12.252  52.678  1.00 36.92 ? 294  PRO A O     1 
ATOM   2035  C  CB    . PRO A 1 274 ? -5.519  12.712  55.006  1.00 36.93 ? 294  PRO A CB    1 
ATOM   2036  C  CG    . PRO A 1 274 ? -4.071  12.624  54.657  1.00 36.87 ? 294  PRO A CG    1 
ATOM   2037  C  CD    . PRO A 1 274 ? -3.955  11.689  53.504  1.00 36.95 ? 294  PRO A CD    1 
ATOM   2038  N  N     . ILE A 1 275 ? -8.605  11.447  54.456  1.00 36.68 ? 295  ILE A N     1 
ATOM   2039  C  CA    . ILE A 1 275 ? -9.945  11.787  53.968  1.00 36.51 ? 295  ILE A CA    1 
ATOM   2040  C  C     . ILE A 1 275 ? -10.601 12.763  54.967  1.00 36.40 ? 295  ILE A C     1 
ATOM   2041  O  O     . ILE A 1 275 ? -11.078 12.354  56.039  1.00 36.47 ? 295  ILE A O     1 
ATOM   2042  C  CB    . ILE A 1 275 ? -10.822 10.519  53.815  1.00 36.73 ? 295  ILE A CB    1 
ATOM   2043  C  CG1   . ILE A 1 275 ? -10.241 9.574   52.748  1.00 37.49 ? 295  ILE A CG1   1 
ATOM   2044  C  CG2   . ILE A 1 275 ? -12.256 10.887  53.460  1.00 36.36 ? 295  ILE A CG2   1 
ATOM   2045  C  CD1   . ILE A 1 275 ? -10.959 8.229   52.664  1.00 37.62 ? 295  ILE A CD1   1 
ATOM   2046  N  N     . HIS A 1 276 ? -10.620 14.047  54.615  1.00 35.59 ? 296  HIS A N     1 
ATOM   2047  C  CA    . HIS A 1 276 ? -11.088 15.096  55.524  1.00 35.07 ? 296  HIS A CA    1 
ATOM   2048  C  C     . HIS A 1 276 ? -12.523 15.560  55.269  1.00 34.38 ? 296  HIS A C     1 
ATOM   2049  O  O     . HIS A 1 276 ? -13.072 16.324  56.067  1.00 34.71 ? 296  HIS A O     1 
ATOM   2050  C  CB    . HIS A 1 276 ? -10.154 16.310  55.435  1.00 35.19 ? 296  HIS A CB    1 
ATOM   2051  N  N     . VAL A 1 277 ? -13.131 15.116  54.170  1.00 33.37 ? 297  VAL A N     1 
ATOM   2052  C  CA    . VAL A 1 277 ? -14.460 15.603  53.779  1.00 32.23 ? 297  VAL A CA    1 
ATOM   2053  C  C     . VAL A 1 277 ? -15.477 14.479  53.697  1.00 31.48 ? 297  VAL A C     1 
ATOM   2054  O  O     . VAL A 1 277 ? -15.115 13.306  53.637  1.00 31.18 ? 297  VAL A O     1 
ATOM   2055  C  CB    . VAL A 1 277 ? -14.425 16.350  52.432  1.00 32.39 ? 297  VAL A CB    1 
ATOM   2056  C  CG1   . VAL A 1 277 ? -13.670 17.663  52.576  1.00 32.67 ? 297  VAL A CG1   1 
ATOM   2057  C  CG2   . VAL A 1 277 ? -13.822 15.476  51.325  1.00 31.79 ? 297  VAL A CG2   1 
ATOM   2058  N  N     . SER A 1 278 ? -16.755 14.847  53.717  1.00 30.48 ? 298  SER A N     1 
ATOM   2059  C  CA    . SER A 1 278 ? -17.825 13.877  53.564  1.00 29.93 ? 298  SER A CA    1 
ATOM   2060  C  C     . SER A 1 278 ? -17.796 13.320  52.150  1.00 28.62 ? 298  SER A C     1 
ATOM   2061  O  O     . SER A 1 278 ? -17.456 14.025  51.208  1.00 28.57 ? 298  SER A O     1 
ATOM   2062  C  CB    . SER A 1 278 ? -19.181 14.527  53.847  1.00 30.32 ? 298  SER A CB    1 
ATOM   2063  O  OG    . SER A 1 278 ? -19.223 15.856  53.343  1.00 32.20 ? 298  SER A OG    1 
ATOM   2064  N  N     . GLY A 1 279 ? -18.144 12.049  52.006  1.00 27.41 ? 299  GLY A N     1 
ATOM   2065  C  CA    . GLY A 1 279 ? -18.216 11.427  50.693  1.00 26.52 ? 299  GLY A CA    1 
ATOM   2066  C  C     . GLY A 1 279 ? -19.432 11.903  49.924  1.00 25.54 ? 299  GLY A C     1 
ATOM   2067  O  O     . GLY A 1 279 ? -20.246 12.664  50.441  1.00 24.80 ? 299  GLY A O     1 
ATOM   2068  N  N     . PRO A 1 280 ? -19.574 11.445  48.679  1.00 24.95 ? 300  PRO A N     1 
ATOM   2069  C  CA    . PRO A 1 280 ? -20.771 11.797  47.921  1.00 24.72 ? 300  PRO A CA    1 
ATOM   2070  C  C     . PRO A 1 280 ? -22.050 11.333  48.613  1.00 24.26 ? 300  PRO A C     1 
ATOM   2071  O  O     . PRO A 1 280 ? -22.022 10.385  49.416  1.00 24.16 ? 300  PRO A O     1 
ATOM   2072  C  CB    . PRO A 1 280 ? -20.588 11.083  46.577  1.00 24.88 ? 300  PRO A CB    1 
ATOM   2073  C  CG    . PRO A 1 280 ? -19.342 10.305  46.667  1.00 24.98 ? 300  PRO A CG    1 
ATOM   2074  C  CD    . PRO A 1 280 ? -18.697 10.495  47.977  1.00 24.95 ? 300  PRO A CD    1 
ATOM   2075  N  N     . ARG A 1 281 ? -23.154 12.000  48.291  1.00 23.49 ? 301  ARG A N     1 
ATOM   2076  C  CA    . ARG A 1 281 ? -24.432 11.745  48.934  1.00 23.42 ? 301  ARG A CA    1 
ATOM   2077  C  C     . ARG A 1 281 ? -25.558 11.784  47.907  1.00 23.09 ? 301  ARG A C     1 
ATOM   2078  O  O     . ARG A 1 281 ? -25.472 12.495  46.906  1.00 22.66 ? 301  ARG A O     1 
ATOM   2079  C  CB    . ARG A 1 281 ? -24.692 12.798  50.027  1.00 23.33 ? 301  ARG A CB    1 
ATOM   2080  N  N     . LEU A 1 282 ? -26.609 11.014  48.167  1.00 22.81 ? 302  LEU A N     1 
ATOM   2081  C  CA    . LEU A 1 282 ? -27.829 11.072  47.360  1.00 23.03 ? 302  LEU A CA    1 
ATOM   2082  C  C     . LEU A 1 282 ? -28.592 12.368  47.627  1.00 22.27 ? 302  LEU A C     1 
ATOM   2083  O  O     . LEU A 1 282 ? -28.751 12.746  48.763  1.00 22.32 ? 302  LEU A O     1 
ATOM   2084  C  CB    . LEU A 1 282 ? -28.752 9.888   47.691  1.00 23.22 ? 302  LEU A CB    1 
ATOM   2085  C  CG    . LEU A 1 282 ? -28.511 8.561   46.975  1.00 24.92 ? 302  LEU A CG    1 
ATOM   2086  C  CD1   . LEU A 1 282 ? -27.214 7.928   47.416  1.00 26.10 ? 302  LEU A CD1   1 
ATOM   2087  C  CD2   . LEU A 1 282 ? -29.695 7.600   47.213  1.00 24.82 ? 302  LEU A CD2   1 
ATOM   2088  N  N     . VAL A 1 283 ? -29.047 13.048  46.579  1.00 22.27 ? 303  VAL A N     1 
ATOM   2089  C  CA    . VAL A 1 283 ? -30.047 14.107  46.715  1.00 22.02 ? 303  VAL A CA    1 
ATOM   2090  C  C     . VAL A 1 283 ? -31.306 13.697  45.969  1.00 21.74 ? 303  VAL A C     1 
ATOM   2091  O  O     . VAL A 1 283 ? -31.240 12.960  44.998  1.00 21.67 ? 303  VAL A O     1 
ATOM   2092  C  CB    . VAL A 1 283 ? -29.552 15.471  46.173  1.00 22.46 ? 303  VAL A CB    1 
ATOM   2093  C  CG1   . VAL A 1 283 ? -28.327 15.956  46.960  1.00 22.31 ? 303  VAL A CG1   1 
ATOM   2094  C  CG2   . VAL A 1 283 ? -29.263 15.391  44.673  1.00 22.88 ? 303  VAL A CG2   1 
ATOM   2095  N  N     . GLN A 1 284 ? -32.455 14.173  46.432  1.00 22.01 ? 304  GLN A N     1 
ATOM   2096  C  CA    . GLN A 1 284 ? -33.741 13.818  45.834  1.00 21.77 ? 304  GLN A CA    1 
ATOM   2097  C  C     . GLN A 1 284 ? -34.640 15.073  45.726  1.00 22.15 ? 304  GLN A C     1 
ATOM   2098  O  O     . GLN A 1 284 ? -35.691 15.145  46.334  1.00 21.44 ? 304  GLN A O     1 
ATOM   2099  C  CB    . GLN A 1 284 ? -34.413 12.695  46.646  1.00 21.63 ? 304  GLN A CB    1 
ATOM   2100  C  CG    . GLN A 1 284 ? -35.533 11.967  45.897  1.00 21.04 ? 304  GLN A CG    1 
ATOM   2101  C  CD    . GLN A 1 284 ? -36.161 10.844  46.698  1.00 20.40 ? 304  GLN A CD    1 
ATOM   2102  O  OE1   . GLN A 1 284 ? -36.208 9.699   46.241  1.00 19.44 ? 304  GLN A OE1   1 
ATOM   2103  N  NE2   . GLN A 1 284 ? -36.648 11.162  47.903  1.00 20.19 ? 304  GLN A NE2   1 
ATOM   2104  N  N     . PRO A 1 285 ? -34.218 16.060  44.919  1.00 22.89 ? 305  PRO A N     1 
ATOM   2105  C  CA    . PRO A 1 285 ? -34.940 17.327  44.751  1.00 23.34 ? 305  PRO A CA    1 
ATOM   2106  C  C     . PRO A 1 285 ? -36.393 17.182  44.295  1.00 23.74 ? 305  PRO A C     1 
ATOM   2107  O  O     . PRO A 1 285 ? -37.241 18.009  44.652  1.00 23.67 ? 305  PRO A O     1 
ATOM   2108  C  CB    . PRO A 1 285 ? -34.139 18.026  43.646  1.00 23.68 ? 305  PRO A CB    1 
ATOM   2109  C  CG    . PRO A 1 285 ? -33.450 16.894  42.913  1.00 23.19 ? 305  PRO A CG    1 
ATOM   2110  C  CD    . PRO A 1 285 ? -33.047 16.002  44.029  1.00 22.80 ? 305  PRO A CD    1 
ATOM   2111  N  N     . HIS A 1 286 ? -36.669 16.144  43.511  1.00 23.85 ? 306  HIS A N     1 
ATOM   2112  C  CA    . HIS A 1 286 ? -38.010 15.906  43.002  1.00 24.29 ? 306  HIS A CA    1 
ATOM   2113  C  C     . HIS A 1 286 ? -38.865 15.066  43.939  1.00 23.63 ? 306  HIS A C     1 
ATOM   2114  O  O     . HIS A 1 286 ? -40.031 14.842  43.660  1.00 24.16 ? 306  HIS A O     1 
ATOM   2115  C  CB    . HIS A 1 286 ? -37.917 15.253  41.636  1.00 24.99 ? 306  HIS A CB    1 
ATOM   2116  C  CG    . HIS A 1 286 ? -37.072 16.029  40.679  1.00 27.43 ? 306  HIS A CG    1 
ATOM   2117  N  ND1   . HIS A 1 286 ? -37.427 17.280  40.222  1.00 30.72 ? 306  HIS A ND1   1 
ATOM   2118  C  CD2   . HIS A 1 286 ? -35.862 15.759  40.139  1.00 30.55 ? 306  HIS A CD2   1 
ATOM   2119  C  CE1   . HIS A 1 286 ? -36.482 17.737  39.420  1.00 31.78 ? 306  HIS A CE1   1 
ATOM   2120  N  NE2   . HIS A 1 286 ? -35.522 16.831  39.349  1.00 31.87 ? 306  HIS A NE2   1 
ATOM   2121  N  N     . GLY A 1 287 ? -38.292 14.618  45.056  1.00 22.92 ? 307  GLY A N     1 
ATOM   2122  C  CA    . GLY A 1 287 ? -39.019 13.803  46.018  1.00 22.24 ? 307  GLY A CA    1 
ATOM   2123  C  C     . GLY A 1 287 ? -39.085 12.354  45.586  1.00 21.51 ? 307  GLY A C     1 
ATOM   2124  O  O     . GLY A 1 287 ? -38.523 11.989  44.556  1.00 21.04 ? 307  GLY A O     1 
ATOM   2125  N  N     . PRO A 1 288 ? -39.773 11.509  46.373  1.00 21.07 ? 308  PRO A N     1 
ATOM   2126  C  CA    . PRO A 1 288 ? -39.851 10.085  46.029  1.00 20.84 ? 308  PRO A CA    1 
ATOM   2127  C  C     . PRO A 1 288 ? -40.556 9.837   44.712  1.00 20.84 ? 308  PRO A C     1 
ATOM   2128  O  O     . PRO A 1 288 ? -41.505 10.546  44.372  1.00 20.72 ? 308  PRO A O     1 
ATOM   2129  C  CB    . PRO A 1 288 ? -40.660 9.482   47.185  1.00 20.86 ? 308  PRO A CB    1 
ATOM   2130  C  CG    . PRO A 1 288 ? -40.532 10.481  48.310  1.00 20.84 ? 308  PRO A CG    1 
ATOM   2131  C  CD    . PRO A 1 288 ? -40.453 11.809  47.646  1.00 20.92 ? 308  PRO A CD    1 
ATOM   2132  N  N     . ARG A 1 289 ? -40.076 8.851   43.964  1.00 21.21 ? 309  ARG A N     1 
ATOM   2133  C  CA    . ARG A 1 289 ? -40.719 8.445   42.712  1.00 21.24 ? 309  ARG A CA    1 
ATOM   2134  C  C     . ARG A 1 289 ? -41.637 7.241   42.904  1.00 21.07 ? 309  ARG A C     1 
ATOM   2135  O  O     . ARG A 1 289 ? -42.415 6.890   42.002  1.00 21.37 ? 309  ARG A O     1 
ATOM   2136  C  CB    . ARG A 1 289 ? -39.668 8.144   41.663  1.00 21.13 ? 309  ARG A CB    1 
ATOM   2137  C  CG    . ARG A 1 289 ? -38.794 9.337   41.373  1.00 21.26 ? 309  ARG A CG    1 
ATOM   2138  C  CD    . ARG A 1 289 ? -38.171 9.250   39.991  1.00 21.82 ? 309  ARG A CD    1 
ATOM   2139  N  NE    . ARG A 1 289 ? -37.357 8.048   39.802  1.00 20.09 ? 309  ARG A NE    1 
ATOM   2140  C  CZ    . ARG A 1 289 ? -36.823 7.675   38.633  1.00 20.74 ? 309  ARG A CZ    1 
ATOM   2141  N  NH1   . ARG A 1 289 ? -37.005 8.401   37.536  1.00 20.29 ? 309  ARG A NH1   1 
ATOM   2142  N  NH2   . ARG A 1 289 ? -36.107 6.555   38.552  1.00 20.38 ? 309  ARG A NH2   1 
ATOM   2143  N  N     . PHE A 1 290 ? -41.549 6.619   44.078  1.00 20.31 ? 310  PHE A N     1 
ATOM   2144  C  CA    . PHE A 1 290 ? -42.523 5.603   44.489  1.00 19.68 ? 310  PHE A CA    1 
ATOM   2145  C  C     . PHE A 1 290 ? -43.655 6.271   45.270  1.00 19.58 ? 310  PHE A C     1 
ATOM   2146  O  O     . PHE A 1 290 ? -43.479 7.363   45.825  1.00 18.72 ? 310  PHE A O     1 
ATOM   2147  C  CB    . PHE A 1 290 ? -41.854 4.522   45.348  1.00 19.43 ? 310  PHE A CB    1 
ATOM   2148  C  CG    . PHE A 1 290 ? -41.115 5.065   46.547  1.00 18.88 ? 310  PHE A CG    1 
ATOM   2149  C  CD1   . PHE A 1 290 ? -41.771 5.269   47.750  1.00 17.14 ? 310  PHE A CD1   1 
ATOM   2150  C  CD2   . PHE A 1 290 ? -39.765 5.387   46.461  1.00 17.91 ? 310  PHE A CD2   1 
ATOM   2151  C  CE1   . PHE A 1 290 ? -41.103 5.772   48.846  1.00 16.71 ? 310  PHE A CE1   1 
ATOM   2152  C  CE2   . PHE A 1 290 ? -39.083 5.900   47.556  1.00 17.47 ? 310  PHE A CE2   1 
ATOM   2153  C  CZ    . PHE A 1 290 ? -39.747 6.090   48.751  1.00 17.19 ? 310  PHE A CZ    1 
ATOM   2154  N  N     . ARG A 1 291 ? -44.807 5.602   45.321  1.00 19.35 ? 311  ARG A N     1 
ATOM   2155  C  CA    . ARG A 1 291 ? -45.950 6.081   46.079  1.00 19.45 ? 311  ARG A CA    1 
ATOM   2156  C  C     . ARG A 1 291 ? -46.168 5.158   47.271  1.00 19.53 ? 311  ARG A C     1 
ATOM   2157  O  O     . ARG A 1 291 ? -46.635 4.031   47.115  1.00 19.89 ? 311  ARG A O     1 
ATOM   2158  C  CB    . ARG A 1 291 ? -47.202 6.099   45.212  1.00 19.47 ? 311  ARG A CB    1 
ATOM   2159  C  CG    . ARG A 1 291 ? -46.993 6.702   43.851  1.00 20.55 ? 311  ARG A CG    1 
ATOM   2160  C  CD    . ARG A 1 291 ? -48.304 6.857   43.124  1.00 21.32 ? 311  ARG A CD    1 
ATOM   2161  N  NE    . ARG A 1 291 ? -48.087 7.020   41.695  1.00 23.24 ? 311  ARG A NE    1 
ATOM   2162  C  CZ    . ARG A 1 291 ? -49.054 7.011   40.779  1.00 24.76 ? 311  ARG A CZ    1 
ATOM   2163  N  NH1   . ARG A 1 291 ? -50.320 6.839   41.133  1.00 24.51 ? 311  ARG A NH1   1 
ATOM   2164  N  NH2   . ARG A 1 291 ? -48.746 7.170   39.501  1.00 25.56 ? 311  ARG A NH2   1 
ATOM   2165  N  N     . LEU A 1 292 ? -45.812 5.638   48.452  1.00 18.98 ? 312  LEU A N     1 
ATOM   2166  C  CA    . LEU A 1 292 ? -46.006 4.902   49.687  1.00 18.89 ? 312  LEU A CA    1 
ATOM   2167  C  C     . LEU A 1 292 ? -47.195 5.540   50.394  1.00 19.03 ? 312  LEU A C     1 
ATOM   2168  O  O     . LEU A 1 292 ? -47.171 6.730   50.723  1.00 18.65 ? 312  LEU A O     1 
ATOM   2169  C  CB    . LEU A 1 292 ? -44.761 4.988   50.567  1.00 18.60 ? 312  LEU A CB    1 
ATOM   2170  C  CG    . LEU A 1 292 ? -44.850 4.539   52.039  1.00 19.51 ? 312  LEU A CG    1 
ATOM   2171  C  CD1   . LEU A 1 292 ? -45.158 3.054   52.151  1.00 20.16 ? 312  LEU A CD1   1 
ATOM   2172  C  CD2   . LEU A 1 292 ? -43.546 4.879   52.783  1.00 17.91 ? 312  LEU A CD2   1 
ATOM   2173  N  N     . GLU A 1 293 ? -48.236 4.752   50.592  1.00 18.94 ? 313  GLU A N     1 
ATOM   2174  C  CA    . GLU A 1 293 ? -49.386 5.182   51.346  1.00 19.62 ? 313  GLU A CA    1 
ATOM   2175  C  C     . GLU A 1 293 ? -49.825 4.022   52.251  1.00 19.67 ? 313  GLU A C     1 
ATOM   2176  O  O     . GLU A 1 293 ? -50.203 2.957   51.773  1.00 19.48 ? 313  GLU A O     1 
ATOM   2177  C  CB    . GLU A 1 293 ? -50.504 5.626   50.403  1.00 19.61 ? 313  GLU A CB    1 
ATOM   2178  C  CG    . GLU A 1 293 ? -51.651 6.273   51.133  1.00 21.43 ? 313  GLU A CG    1 
ATOM   2179  C  CD    . GLU A 1 293 ? -52.746 6.760   50.207  1.00 23.29 ? 313  GLU A CD    1 
ATOM   2180  O  OE1   . GLU A 1 293 ? -52.628 6.616   48.977  1.00 25.24 ? 313  GLU A OE1   1 
ATOM   2181  O  OE2   . GLU A 1 293 ? -53.735 7.292   50.725  1.00 26.74 ? 313  GLU A OE2   1 
ATOM   2182  N  N     . GLY A 1 294 ? -49.749 4.243   53.559  1.00 20.08 ? 314  GLY A N     1 
ATOM   2183  C  CA    . GLY A 1 294 ? -49.937 3.187   54.539  1.00 20.52 ? 314  GLY A CA    1 
ATOM   2184  C  C     . GLY A 1 294 ? -48.885 2.110   54.353  1.00 20.72 ? 314  GLY A C     1 
ATOM   2185  O  O     . GLY A 1 294 ? -47.671 2.378   54.364  1.00 21.31 ? 314  GLY A O     1 
ATOM   2186  N  N     . ASN A 1 295 ? -49.344 0.887   54.166  1.00 20.58 ? 315  ASN A N     1 
ATOM   2187  C  CA    . ASN A 1 295 ? -48.438 -0.213  53.869  1.00 20.53 ? 315  ASN A CA    1 
ATOM   2188  C  C     . ASN A 1 295 ? -48.538 -0.637  52.396  1.00 20.10 ? 315  ASN A C     1 
ATOM   2189  O  O     . ASN A 1 295 ? -48.221 -1.775  52.061  1.00 20.30 ? 315  ASN A O     1 
ATOM   2190  C  CB    . ASN A 1 295 ? -48.712 -1.376  54.826  1.00 20.75 ? 315  ASN A CB    1 
ATOM   2191  C  CG    . ASN A 1 295 ? -50.020 -2.099  54.523  1.00 21.87 ? 315  ASN A CG    1 
ATOM   2192  O  OD1   . ASN A 1 295 ? -51.028 -1.475  54.171  1.00 23.48 ? 315  ASN A OD1   1 
ATOM   2193  N  ND2   . ASN A 1 295 ? -49.996 -3.425  54.622  1.00 21.91 ? 315  ASN A ND2   1 
ATOM   2194  N  N     . ALA A 1 296 ? -48.967 0.287   51.526  1.00 19.65 ? 316  ALA A N     1 
ATOM   2195  C  CA    . ALA A 1 296 ? -49.078 0.036   50.082  1.00 19.29 ? 316  ALA A CA    1 
ATOM   2196  C  C     . ALA A 1 296 ? -47.998 0.811   49.344  1.00 19.08 ? 316  ALA A C     1 
ATOM   2197  O  O     . ALA A 1 296 ? -47.790 1.993   49.609  1.00 19.06 ? 316  ALA A O     1 
ATOM   2198  C  CB    . ALA A 1 296 ? -50.452 0.451   49.554  1.00 18.69 ? 316  ALA A CB    1 
ATOM   2199  N  N     . VAL A 1 297 ? -47.345 0.151   48.394  1.00 18.68 ? 317  VAL A N     1 
ATOM   2200  C  CA    . VAL A 1 297 ? -46.298 0.772   47.599  1.00 18.44 ? 317  VAL A CA    1 
ATOM   2201  C  C     . VAL A 1 297 ? -46.574 0.589   46.111  1.00 18.34 ? 317  VAL A C     1 
ATOM   2202  O  O     . VAL A 1 297 ? -46.932 -0.506  45.650  1.00 18.13 ? 317  VAL A O     1 
ATOM   2203  C  CB    . VAL A 1 297 ? -44.900 0.192   47.966  1.00 18.67 ? 317  VAL A CB    1 
ATOM   2204  C  CG1   . VAL A 1 297 ? -43.796 0.818   47.104  1.00 17.66 ? 317  VAL A CG1   1 
ATOM   2205  C  CG2   . VAL A 1 297 ? -44.614 0.419   49.445  1.00 17.85 ? 317  VAL A CG2   1 
ATOM   2206  N  N     . LEU A 1 298 ? -46.436 1.688   45.376  1.00 18.53 ? 318  LEU A N     1 
ATOM   2207  C  CA    . LEU A 1 298 ? -46.404 1.681   43.912  1.00 18.46 ? 318  LEU A CA    1 
ATOM   2208  C  C     . LEU A 1 298 ? -45.052 2.244   43.479  1.00 18.38 ? 318  LEU A C     1 
ATOM   2209  O  O     . LEU A 1 298 ? -44.599 3.225   44.027  1.00 18.36 ? 318  LEU A O     1 
ATOM   2210  C  CB    . LEU A 1 298 ? -47.546 2.528   43.352  1.00 18.35 ? 318  LEU A CB    1 
ATOM   2211  C  CG    . LEU A 1 298 ? -48.953 2.077   43.797  1.00 19.27 ? 318  LEU A CG    1 
ATOM   2212  C  CD1   . LEU A 1 298 ? -50.027 3.144   43.536  1.00 18.54 ? 318  LEU A CD1   1 
ATOM   2213  C  CD2   . LEU A 1 298 ? -49.320 0.761   43.100  1.00 19.81 ? 318  LEU A CD2   1 
ATOM   2214  N  N     . TYR A 1 299 ? -44.406 1.597   42.514  1.00 18.76 ? 319  TYR A N     1 
ATOM   2215  C  CA    . TYR A 1 299 ? -43.105 2.018   42.005  1.00 18.80 ? 319  TYR A CA    1 
ATOM   2216  C  C     . TYR A 1 299 ? -42.961 1.513   40.571  1.00 19.31 ? 319  TYR A C     1 
ATOM   2217  O  O     . TYR A 1 299 ? -42.660 0.336   40.347  1.00 18.38 ? 319  TYR A O     1 
ATOM   2218  C  CB    . TYR A 1 299 ? -41.978 1.453   42.870  1.00 19.15 ? 319  TYR A CB    1 
ATOM   2219  C  CG    . TYR A 1 299 ? -40.577 1.700   42.336  1.00 19.43 ? 319  TYR A CG    1 
ATOM   2220  C  CD1   . TYR A 1 299 ? -40.103 2.989   42.139  1.00 19.63 ? 319  TYR A CD1   1 
ATOM   2221  C  CD2   . TYR A 1 299 ? -39.724 0.639   42.044  1.00 20.99 ? 319  TYR A CD2   1 
ATOM   2222  C  CE1   . TYR A 1 299 ? -38.818 3.218   41.659  1.00 20.77 ? 319  TYR A CE1   1 
ATOM   2223  C  CE2   . TYR A 1 299 ? -38.435 0.859   41.564  1.00 20.51 ? 319  TYR A CE2   1 
ATOM   2224  C  CZ    . TYR A 1 299 ? -37.992 2.147   41.377  1.00 20.46 ? 319  TYR A CZ    1 
ATOM   2225  O  OH    . TYR A 1 299 ? -36.725 2.371   40.905  1.00 20.25 ? 319  TYR A OH    1 
ATOM   2226  N  N     . GLY A 1 300 ? -43.197 2.410   39.615  1.00 19.43 ? 320  GLY A N     1 
ATOM   2227  C  CA    . GLY A 1 300 ? -43.236 2.064   38.194  1.00 19.81 ? 320  GLY A CA    1 
ATOM   2228  C  C     . GLY A 1 300 ? -44.172 0.909   37.902  1.00 19.72 ? 320  GLY A C     1 
ATOM   2229  O  O     . GLY A 1 300 ? -45.415 1.027   38.031  1.00 20.00 ? 320  GLY A O     1 
ATOM   2230  N  N     . GLY A 1 301 ? -43.580 -0.216  37.509  1.00 19.28 ? 321  GLY A N     1 
ATOM   2231  C  CA    . GLY A 1 301 ? -44.342 -1.418  37.215  1.00 18.94 ? 321  GLY A CA    1 
ATOM   2232  C  C     . GLY A 1 301 ? -44.864 -2.105  38.462  1.00 19.00 ? 321  GLY A C     1 
ATOM   2233  O  O     . GLY A 1 301 ? -45.816 -2.888  38.385  1.00 18.57 ? 321  GLY A O     1 
ATOM   2234  N  N     . TRP A 1 302 ? -44.252 -1.813  39.612  1.00 19.03 ? 322  TRP A N     1 
ATOM   2235  C  CA    . TRP A 1 302 ? -44.517 -2.568  40.837  1.00 19.02 ? 322  TRP A CA    1 
ATOM   2236  C  C     . TRP A 1 302 ? -45.733 -2.115  41.633  1.00 19.29 ? 322  TRP A C     1 
ATOM   2237  O  O     . TRP A 1 302 ? -46.065 -0.929  41.687  1.00 19.26 ? 322  TRP A O     1 
ATOM   2238  C  CB    . TRP A 1 302 ? -43.321 -2.496  41.772  1.00 18.84 ? 322  TRP A CB    1 
ATOM   2239  C  CG    . TRP A 1 302 ? -42.075 -3.137  41.250  1.00 18.55 ? 322  TRP A CG    1 
ATOM   2240  C  CD1   . TRP A 1 302 ? -41.019 -2.515  40.656  1.00 17.60 ? 322  TRP A CD1   1 
ATOM   2241  C  CD2   . TRP A 1 302 ? -41.747 -4.531  41.300  1.00 18.10 ? 322  TRP A CD2   1 
ATOM   2242  N  NE1   . TRP A 1 302 ? -40.048 -3.437  40.330  1.00 19.06 ? 322  TRP A NE1   1 
ATOM   2243  C  CE2   . TRP A 1 302 ? -40.474 -4.682  40.709  1.00 18.40 ? 322  TRP A CE2   1 
ATOM   2244  C  CE3   . TRP A 1 302 ? -42.418 -5.669  41.757  1.00 17.72 ? 322  TRP A CE3   1 
ATOM   2245  C  CZ2   . TRP A 1 302 ? -39.851 -5.922  40.594  1.00 19.23 ? 322  TRP A CZ2   1 
ATOM   2246  C  CZ3   . TRP A 1 302 ? -41.796 -6.906  41.636  1.00 17.62 ? 322  TRP A CZ3   1 
ATOM   2247  C  CH2   . TRP A 1 302 ? -40.530 -7.022  41.058  1.00 18.46 ? 322  TRP A CH2   1 
ATOM   2248  N  N     . SER A 1 303 ? -46.356 -3.084  42.289  1.00 19.46 ? 323  SER A N     1 
ATOM   2249  C  CA    . SER A 1 303 ? -47.361 -2.837  43.308  1.00 19.87 ? 323  SER A CA    1 
ATOM   2250  C  C     . SER A 1 303 ? -47.225 -3.911  44.374  1.00 19.73 ? 323  SER A C     1 
ATOM   2251  O  O     . SER A 1 303 ? -47.256 -5.081  44.057  1.00 19.78 ? 323  SER A O     1 
ATOM   2252  C  CB    . SER A 1 303 ? -48.761 -2.899  42.704  1.00 19.98 ? 323  SER A CB    1 
ATOM   2253  O  OG    . SER A 1 303 ? -49.734 -2.809  43.719  1.00 21.84 ? 323  SER A OG    1 
ATOM   2254  N  N     . PHE A 1 304 ? -47.066 -3.514  45.631  1.00 19.77 ? 324  PHE A N     1 
ATOM   2255  C  CA    . PHE A 1 304 ? -47.002 -4.475  46.720  1.00 19.78 ? 324  PHE A CA    1 
ATOM   2256  C  C     . PHE A 1 304 ? -47.407 -3.859  48.055  1.00 19.48 ? 324  PHE A C     1 
ATOM   2257  O  O     . PHE A 1 304 ? -47.476 -2.644  48.197  1.00 19.31 ? 324  PHE A O     1 
ATOM   2258  C  CB    . PHE A 1 304 ? -45.599 -5.099  46.816  1.00 20.08 ? 324  PHE A CB    1 
ATOM   2259  C  CG    . PHE A 1 304 ? -44.500 -4.120  47.180  1.00 19.57 ? 324  PHE A CG    1 
ATOM   2260  C  CD1   . PHE A 1 304 ? -44.168 -3.893  48.512  1.00 18.85 ? 324  PHE A CD1   1 
ATOM   2261  C  CD2   . PHE A 1 304 ? -43.755 -3.486  46.185  1.00 19.38 ? 324  PHE A CD2   1 
ATOM   2262  C  CE1   . PHE A 1 304 ? -43.131 -3.015  48.857  1.00 19.03 ? 324  PHE A CE1   1 
ATOM   2263  C  CE2   . PHE A 1 304 ? -42.714 -2.600  46.513  1.00 18.84 ? 324  PHE A CE2   1 
ATOM   2264  C  CZ    . PHE A 1 304 ? -42.406 -2.358  47.850  1.00 19.31 ? 324  PHE A CZ    1 
ATOM   2265  N  N     . ALA A 1 305 ? -47.706 -4.718  49.015  1.00 19.27 ? 325  ALA A N     1 
ATOM   2266  C  CA    . ALA A 1 305 ? -47.964 -4.300  50.390  1.00 19.27 ? 325  ALA A CA    1 
ATOM   2267  C  C     . ALA A 1 305 ? -46.869 -4.901  51.247  1.00 19.32 ? 325  ALA A C     1 
ATOM   2268  O  O     . ALA A 1 305 ? -46.183 -5.827  50.825  1.00 18.79 ? 325  ALA A O     1 
ATOM   2269  C  CB    . ALA A 1 305 ? -49.341 -4.780  50.860  1.00 18.96 ? 325  ALA A CB    1 
ATOM   2270  N  N     . PHE A 1 306 ? -46.681 -4.372  52.444  1.00 19.96 ? 326  PHE A N     1 
ATOM   2271  C  CA    . PHE A 1 306 ? -45.703 -4.953  53.352  1.00 21.12 ? 326  PHE A CA    1 
ATOM   2272  C  C     . PHE A 1 306 ? -46.235 -4.976  54.758  1.00 21.48 ? 326  PHE A C     1 
ATOM   2273  O  O     . PHE A 1 306 ? -47.231 -4.336  55.077  1.00 22.04 ? 326  PHE A O     1 
ATOM   2274  C  CB    . PHE A 1 306 ? -44.367 -4.199  53.310  1.00 20.99 ? 326  PHE A CB    1 
ATOM   2275  C  CG    . PHE A 1 306 ? -44.481 -2.755  53.690  1.00 23.00 ? 326  PHE A CG    1 
ATOM   2276  C  CD1   . PHE A 1 306 ? -44.353 -2.359  55.012  1.00 23.52 ? 326  PHE A CD1   1 
ATOM   2277  C  CD2   . PHE A 1 306 ? -44.737 -1.790  52.721  1.00 23.26 ? 326  PHE A CD2   1 
ATOM   2278  C  CE1   . PHE A 1 306 ? -44.483 -1.027  55.358  1.00 24.51 ? 326  PHE A CE1   1 
ATOM   2279  C  CE2   . PHE A 1 306 ? -44.855 -0.468  53.063  1.00 23.65 ? 326  PHE A CE2   1 
ATOM   2280  C  CZ    . PHE A 1 306 ? -44.730 -0.084  54.383  1.00 23.81 ? 326  PHE A CZ    1 
ATOM   2281  N  N     . ARG A 1 307 ? -45.570 -5.751  55.591  1.00 21.87 ? 327  ARG A N     1 
ATOM   2282  C  CA    . ARG A 1 307 ? -45.821 -5.713  57.016  1.00 22.42 ? 327  ARG A CA    1 
ATOM   2283  C  C     . ARG A 1 307 ? -44.566 -6.172  57.721  1.00 22.12 ? 327  ARG A C     1 
ATOM   2284  O  O     . ARG A 1 307 ? -43.669 -6.759  57.108  1.00 21.79 ? 327  ARG A O     1 
ATOM   2285  C  CB    . ARG A 1 307 ? -46.982 -6.611  57.399  1.00 22.57 ? 327  ARG A CB    1 
ATOM   2286  C  CG    . ARG A 1 307 ? -46.636 -8.079  57.363  1.00 24.58 ? 327  ARG A CG    1 
ATOM   2287  C  CD    . ARG A 1 307 ? -47.705 -8.921  58.017  1.00 25.95 ? 327  ARG A CD    1 
ATOM   2288  N  NE    . ARG A 1 307 ? -47.777 -8.717  59.460  1.00 26.97 ? 327  ARG A NE    1 
ATOM   2289  C  CZ    . ARG A 1 307 ? -48.355 -9.567  60.308  1.00 26.13 ? 327  ARG A CZ    1 
ATOM   2290  N  NH1   . ARG A 1 307 ? -48.371 -9.293  61.609  1.00 26.39 ? 327  ARG A NH1   1 
ATOM   2291  N  NH2   . ARG A 1 307 ? -48.891 -10.704 59.866  1.00 26.29 ? 327  ARG A NH2   1 
ATOM   2292  N  N     . LEU A 1 308 ? -44.519 -5.890  59.011  1.00 22.09 ? 328  LEU A N     1 
ATOM   2293  C  CA    . LEU A 1 308 ? -43.413 -6.279  59.842  1.00 22.50 ? 328  LEU A CA    1 
ATOM   2294  C  C     . LEU A 1 308 ? -43.990 -7.098  60.998  1.00 22.65 ? 328  LEU A C     1 
ATOM   2295  O  O     . LEU A 1 308 ? -44.472 -6.556  61.989  1.00 22.79 ? 328  LEU A O     1 
ATOM   2296  C  CB    . LEU A 1 308 ? -42.679 -5.031  60.315  1.00 22.41 ? 328  LEU A CB    1 
ATOM   2297  C  CG    . LEU A 1 308 ? -41.505 -5.235  61.268  1.00 23.14 ? 328  LEU A CG    1 
ATOM   2298  C  CD1   . LEU A 1 308 ? -40.376 -5.996  60.594  1.00 22.97 ? 328  LEU A CD1   1 
ATOM   2299  C  CD2   . LEU A 1 308 ? -41.030 -3.880  61.772  1.00 24.60 ? 328  LEU A CD2   1 
ATOM   2300  N  N     . ARG A 1 309 ? -43.978 -8.410  60.834  1.00 23.28 ? 329  ARG A N     1 
ATOM   2301  C  CA    . ARG A 1 309 ? -44.505 -9.318  61.849  1.00 23.83 ? 329  ARG A CA    1 
ATOM   2302  C  C     . ARG A 1 309 ? -43.560 -9.291  63.045  1.00 23.27 ? 329  ARG A C     1 
ATOM   2303  O  O     . ARG A 1 309 ? -42.370 -9.580  62.907  1.00 23.01 ? 329  ARG A O     1 
ATOM   2304  C  CB    . ARG A 1 309 ? -44.641 -10.718 61.256  1.00 24.42 ? 329  ARG A CB    1 
ATOM   2305  C  CG    . ARG A 1 309 ? -45.374 -11.755 62.105  1.00 27.51 ? 329  ARG A CG    1 
ATOM   2306  C  CD    . ARG A 1 309 ? -45.865 -12.896 61.206  1.00 31.21 ? 329  ARG A CD    1 
ATOM   2307  N  NE    . ARG A 1 309 ? -46.360 -14.070 61.938  1.00 35.96 ? 329  ARG A NE    1 
ATOM   2308  C  CZ    . ARG A 1 309 ? -45.659 -15.187 62.189  1.00 38.61 ? 329  ARG A CZ    1 
ATOM   2309  N  NH1   . ARG A 1 309 ? -44.393 -15.318 61.800  1.00 38.87 ? 329  ARG A NH1   1 
ATOM   2310  N  NH2   . ARG A 1 309 ? -46.230 -16.192 62.847  1.00 39.25 ? 329  ARG A NH2   1 
ATOM   2311  N  N     . SER A 1 310 ? -44.079 -8.891  64.204  1.00 23.17 ? 330  SER A N     1 
ATOM   2312  C  CA    . SER A 1 310 ? -43.278 -8.813  65.431  1.00 23.32 ? 330  SER A CA    1 
ATOM   2313  C  C     . SER A 1 310 ? -42.513 -10.102 65.745  1.00 23.47 ? 330  SER A C     1 
ATOM   2314  O  O     . SER A 1 310 ? -41.376 -10.056 66.231  1.00 23.49 ? 330  SER A O     1 
ATOM   2315  C  CB    . SER A 1 310 ? -44.167 -8.442  66.633  1.00 23.58 ? 330  SER A CB    1 
ATOM   2316  O  OG    . SER A 1 310 ? -44.534 -7.076  66.601  1.00 22.98 ? 330  SER A OG    1 
ATOM   2317  N  N     . SER A 1 311 ? -43.129 -11.250 65.480  1.00 23.59 ? 331  SER A N     1 
ATOM   2318  C  CA    . SER A 1 311 ? -42.485 -12.525 65.791  1.00 24.32 ? 331  SER A CA    1 
ATOM   2319  C  C     . SER A 1 311 ? -41.318 -12.835 64.829  1.00 25.07 ? 331  SER A C     1 
ATOM   2320  O  O     . SER A 1 311 ? -40.167 -13.013 65.276  1.00 26.11 ? 331  SER A O     1 
ATOM   2321  C  CB    . SER A 1 311 ? -43.501 -13.675 65.817  1.00 23.71 ? 331  SER A CB    1 
ATOM   2322  O  OG    . SER A 1 311 ? -44.286 -13.715 64.638  1.00 23.16 ? 331  SER A OG    1 
ATOM   2323  N  N     . SER A 1 312 ? -41.610 -12.854 63.530  1.00 25.29 ? 332  SER A N     1 
ATOM   2324  C  CA    . SER A 1 312 ? -40.678 -13.351 62.503  1.00 25.28 ? 332  SER A CA    1 
ATOM   2325  C  C     . SER A 1 312 ? -40.003 -12.293 61.622  1.00 25.46 ? 332  SER A C     1 
ATOM   2326  O  O     . SER A 1 312 ? -38.943 -12.564 61.060  1.00 25.99 ? 332  SER A O     1 
ATOM   2327  C  CB    . SER A 1 312 ? -41.407 -14.343 61.603  1.00 25.12 ? 332  SER A CB    1 
ATOM   2328  O  OG    . SER A 1 312 ? -42.531 -13.739 61.008  1.00 24.78 ? 332  SER A OG    1 
ATOM   2329  N  N     . GLY A 1 313 ? -40.613 -11.117 61.476  1.00 25.41 ? 333  GLY A N     1 
ATOM   2330  C  CA    . GLY A 1 313 ? -40.006 -10.014 60.721  1.00 25.14 ? 333  GLY A CA    1 
ATOM   2331  C  C     . GLY A 1 313 ? -40.719 -9.613  59.432  1.00 25.14 ? 333  GLY A C     1 
ATOM   2332  O  O     . GLY A 1 313 ? -41.938 -9.791  59.289  1.00 24.90 ? 333  GLY A O     1 
ATOM   2333  N  N     . LEU A 1 314 ? -39.927 -9.095  58.494  1.00 24.75 ? 334  LEU A N     1 
ATOM   2334  C  CA    . LEU A 1 314 ? -40.408 -8.390  57.298  1.00 24.63 ? 334  LEU A CA    1 
ATOM   2335  C  C     . LEU A 1 314 ? -41.081 -9.307  56.287  1.00 25.09 ? 334  LEU A C     1 
ATOM   2336  O  O     . LEU A 1 314 ? -40.599 -10.411 56.010  1.00 24.96 ? 334  LEU A O     1 
ATOM   2337  C  CB    . LEU A 1 314 ? -39.225 -7.683  56.621  1.00 24.46 ? 334  LEU A CB    1 
ATOM   2338  C  CG    . LEU A 1 314 ? -39.477 -6.474  55.716  1.00 24.18 ? 334  LEU A CG    1 
ATOM   2339  C  CD1   . LEU A 1 314 ? -40.089 -5.345  56.494  1.00 21.92 ? 334  LEU A CD1   1 
ATOM   2340  C  CD2   . LEU A 1 314 ? -38.167 -6.006  55.099  1.00 23.20 ? 334  LEU A CD2   1 
ATOM   2341  N  N     . GLN A 1 315 ? -42.202 -8.844  55.733  1.00 25.61 ? 335  GLN A N     1 
ATOM   2342  C  CA    . GLN A 1 315 ? -42.877 -9.538  54.633  1.00 25.54 ? 335  GLN A CA    1 
ATOM   2343  C  C     . GLN A 1 315 ? -43.311 -8.563  53.569  1.00 25.03 ? 335  GLN A C     1 
ATOM   2344  O  O     . GLN A 1 315 ? -43.748 -7.456  53.894  1.00 25.89 ? 335  GLN A O     1 
ATOM   2345  C  CB    . GLN A 1 315 ? -44.124 -10.233 55.134  1.00 25.98 ? 335  GLN A CB    1 
ATOM   2346  C  CG    . GLN A 1 315 ? -43.946 -10.990 56.414  1.00 27.16 ? 335  GLN A CG    1 
ATOM   2347  C  CD    . GLN A 1 315 ? -45.093 -11.919 56.664  1.00 29.15 ? 335  GLN A CD    1 
ATOM   2348  O  OE1   . GLN A 1 315 ? -46.148 -11.805 56.040  1.00 30.64 ? 335  GLN A OE1   1 
ATOM   2349  N  NE2   . GLN A 1 315 ? -44.899 -12.853 57.574  1.00 31.42 ? 335  GLN A NE2   1 
ATOM   2350  N  N     . VAL A 1 316 ? -43.199 -8.960  52.305  1.00 24.11 ? 336  VAL A N     1 
ATOM   2351  C  CA    . VAL A 1 316 ? -43.862 -8.234  51.228  1.00 23.49 ? 336  VAL A CA    1 
ATOM   2352  C  C     . VAL A 1 316 ? -44.961 -9.130  50.682  1.00 22.64 ? 336  VAL A C     1 
ATOM   2353  O  O     . VAL A 1 316 ? -44.761 -10.330 50.467  1.00 21.90 ? 336  VAL A O     1 
ATOM   2354  C  CB    . VAL A 1 316 ? -42.904 -7.742  50.112  1.00 23.38 ? 336  VAL A CB    1 
ATOM   2355  C  CG1   . VAL A 1 316 ? -41.885 -6.769  50.687  1.00 24.56 ? 336  VAL A CG1   1 
ATOM   2356  C  CG2   . VAL A 1 316 ? -42.210 -8.895  49.422  1.00 24.75 ? 336  VAL A CG2   1 
ATOM   2357  N  N     . LEU A 1 317 ? -46.133 -8.536  50.487  1.00 21.86 ? 337  LEU A N     1 
ATOM   2358  C  CA    . LEU A 1 317 ? -47.328 -9.276  50.128  1.00 21.18 ? 337  LEU A CA    1 
ATOM   2359  C  C     . LEU A 1 317 ? -47.978 -8.749  48.861  1.00 20.74 ? 337  LEU A C     1 
ATOM   2360  O  O     . LEU A 1 317 ? -47.858 -7.572  48.539  1.00 20.87 ? 337  LEU A O     1 
ATOM   2361  C  CB    . LEU A 1 317 ? -48.312 -9.223  51.298  1.00 21.16 ? 337  LEU A CB    1 
ATOM   2362  C  CG    . LEU A 1 317 ? -47.752 -10.002 52.497  1.00 22.11 ? 337  LEU A CG    1 
ATOM   2363  C  CD1   . LEU A 1 317 ? -47.832 -9.181  53.763  1.00 22.37 ? 337  LEU A CD1   1 
ATOM   2364  C  CD2   . LEU A 1 317 ? -48.446 -11.338 52.640  1.00 21.75 ? 337  LEU A CD2   1 
ATOM   2365  N  N     . ASN A 1 318 ? -48.663 -9.645  48.149  1.00 20.42 ? 338  ASN A N     1 
ATOM   2366  C  CA    . ASN A 1 318 ? -49.508 -9.295  47.006  1.00 19.70 ? 338  ASN A CA    1 
ATOM   2367  C  C     . ASN A 1 318 ? -48.721 -8.542  45.938  1.00 19.18 ? 338  ASN A C     1 
ATOM   2368  O  O     . ASN A 1 318 ? -49.178 -7.549  45.381  1.00 19.23 ? 338  ASN A O     1 
ATOM   2369  C  CB    . ASN A 1 318 ? -50.722 -8.495  47.484  1.00 19.91 ? 338  ASN A CB    1 
ATOM   2370  C  CG    . ASN A 1 318 ? -51.787 -8.361  46.416  1.00 19.93 ? 338  ASN A CG    1 
ATOM   2371  O  OD1   . ASN A 1 318 ? -52.038 -9.302  45.659  1.00 20.14 ? 338  ASN A OD1   1 
ATOM   2372  N  ND2   . ASN A 1 318 ? -52.405 -7.188  46.335  1.00 18.29 ? 338  ASN A ND2   1 
ATOM   2373  N  N     . VAL A 1 319 ? -47.521 -9.049  45.660  1.00 18.72 ? 339  VAL A N     1 
ATOM   2374  C  CA    . VAL A 1 319 ? -46.576 -8.395  44.784  1.00 17.87 ? 339  VAL A CA    1 
ATOM   2375  C  C     . VAL A 1 319 ? -47.010 -8.558  43.336  1.00 18.03 ? 339  VAL A C     1 
ATOM   2376  O  O     . VAL A 1 319 ? -47.108 -9.682  42.838  1.00 17.30 ? 339  VAL A O     1 
ATOM   2377  C  CB    . VAL A 1 319 ? -45.158 -8.982  44.956  1.00 18.07 ? 339  VAL A CB    1 
ATOM   2378  C  CG1   . VAL A 1 319 ? -44.173 -8.292  44.019  1.00 17.64 ? 339  VAL A CG1   1 
ATOM   2379  C  CG2   . VAL A 1 319 ? -44.688 -8.877  46.424  1.00 16.01 ? 339  VAL A CG2   1 
ATOM   2380  N  N     . HIS A 1 320 ? -47.257 -7.425  42.673  1.00 18.12 ? 340  HIS A N     1 
ATOM   2381  C  CA    . HIS A 1 320 ? -47.552 -7.378  41.247  1.00 18.08 ? 340  HIS A CA    1 
ATOM   2382  C  C     . HIS A 1 320 ? -46.457 -6.624  40.502  1.00 18.52 ? 340  HIS A C     1 
ATOM   2383  O  O     . HIS A 1 320 ? -45.799 -5.746  41.065  1.00 17.79 ? 340  HIS A O     1 
ATOM   2384  C  CB    . HIS A 1 320 ? -48.855 -6.623  40.974  1.00 17.80 ? 340  HIS A CB    1 
ATOM   2385  C  CG    . HIS A 1 320 ? -50.094 -7.315  41.446  1.00 17.79 ? 340  HIS A CG    1 
ATOM   2386  N  ND1   . HIS A 1 320 ? -50.331 -7.605  42.771  1.00 17.81 ? 340  HIS A ND1   1 
ATOM   2387  C  CD2   . HIS A 1 320 ? -51.192 -7.730  40.768  1.00 18.16 ? 340  HIS A CD2   1 
ATOM   2388  C  CE1   . HIS A 1 320 ? -51.512 -8.188  42.886  1.00 18.49 ? 340  HIS A CE1   1 
ATOM   2389  N  NE2   . HIS A 1 320 ? -52.054 -8.277  41.686  1.00 17.71 ? 340  HIS A NE2   1 
ATOM   2390  N  N     . PHE A 1 321 ? -46.281 -6.984  39.233  1.00 19.17 ? 341  PHE A N     1 
ATOM   2391  C  CA    . PHE A 1 321 ? -45.626 -6.129  38.264  1.00 20.46 ? 341  PHE A CA    1 
ATOM   2392  C  C     . PHE A 1 321 ? -46.474 -6.105  36.997  1.00 21.35 ? 341  PHE A C     1 
ATOM   2393  O  O     . PHE A 1 321 ? -46.969 -7.141  36.573  1.00 21.86 ? 341  PHE A O     1 
ATOM   2394  C  CB    . PHE A 1 321 ? -44.209 -6.605  37.957  1.00 20.41 ? 341  PHE A CB    1 
ATOM   2395  C  CG    . PHE A 1 321 ? -43.403 -5.607  37.197  1.00 21.23 ? 341  PHE A CG    1 
ATOM   2396  C  CD1   . PHE A 1 321 ? -42.462 -4.818  37.842  1.00 21.67 ? 341  PHE A CD1   1 
ATOM   2397  C  CD2   . PHE A 1 321 ? -43.621 -5.406  35.835  1.00 24.17 ? 341  PHE A CD2   1 
ATOM   2398  C  CE1   . PHE A 1 321 ? -41.710 -3.871  37.133  1.00 21.94 ? 341  PHE A CE1   1 
ATOM   2399  C  CE2   . PHE A 1 321 ? -42.887 -4.449  35.124  1.00 24.30 ? 341  PHE A CE2   1 
ATOM   2400  C  CZ    . PHE A 1 321 ? -41.916 -3.693  35.778  1.00 23.01 ? 341  PHE A CZ    1 
ATOM   2401  N  N     . GLY A 1 322 ? -46.661 -4.918  36.425  1.00 22.10 ? 342  GLY A N     1 
ATOM   2402  C  CA    . GLY A 1 322 ? -47.481 -4.739  35.231  1.00 22.74 ? 342  GLY A CA    1 
ATOM   2403  C  C     . GLY A 1 322 ? -48.969 -5.003  35.428  1.00 23.26 ? 342  GLY A C     1 
ATOM   2404  O  O     . GLY A 1 322 ? -49.690 -5.256  34.465  1.00 23.17 ? 342  GLY A O     1 
ATOM   2405  N  N     . GLY A 1 323 ? -49.435 -4.931  36.668  1.00 23.82 ? 343  GLY A N     1 
ATOM   2406  C  CA    . GLY A 1 323 ? -50.819 -5.273  36.982  1.00 24.11 ? 343  GLY A CA    1 
ATOM   2407  C  C     . GLY A 1 323 ? -51.077 -6.767  37.072  1.00 24.39 ? 343  GLY A C     1 
ATOM   2408  O  O     . GLY A 1 323 ? -52.229 -7.193  37.125  1.00 25.00 ? 343  GLY A O     1 
ATOM   2409  N  N     . GLU A 1 324 ? -50.019 -7.572  37.097  1.00 23.95 ? 344  GLU A N     1 
ATOM   2410  C  CA    . GLU A 1 324 ? -50.176 -9.009  37.249  1.00 24.00 ? 344  GLU A CA    1 
ATOM   2411  C  C     . GLU A 1 324 ? -49.408 -9.523  38.460  1.00 23.07 ? 344  GLU A C     1 
ATOM   2412  O  O     . GLU A 1 324 ? -48.271 -9.103  38.719  1.00 22.30 ? 344  GLU A O     1 
ATOM   2413  C  CB    . GLU A 1 324 ? -49.733 -9.704  35.978  1.00 24.56 ? 344  GLU A CB    1 
ATOM   2414  C  CG    . GLU A 1 324 ? -50.443 -9.126  34.761  1.00 26.91 ? 344  GLU A CG    1 
ATOM   2415  C  CD    . GLU A 1 324 ? -50.245 -9.955  33.544  1.00 29.39 ? 344  GLU A CD    1 
ATOM   2416  O  OE1   . GLU A 1 324 ? -49.505 -9.515  32.636  1.00 33.33 ? 344  GLU A OE1   1 
ATOM   2417  O  OE2   . GLU A 1 324 ? -50.824 -11.052 33.497  1.00 32.13 ? 344  GLU A OE2   1 
ATOM   2418  N  N     . ARG A 1 325 ? -50.041 -10.424 39.207  1.00 22.16 ? 345  ARG A N     1 
ATOM   2419  C  CA    . ARG A 1 325 ? -49.429 -10.969 40.410  1.00 21.62 ? 345  ARG A CA    1 
ATOM   2420  C  C     . ARG A 1 325 ? -48.228 -11.841 40.057  1.00 21.26 ? 345  ARG A C     1 
ATOM   2421  O  O     . ARG A 1 325 ? -48.224 -12.567 39.057  1.00 19.85 ? 345  ARG A O     1 
ATOM   2422  C  CB    . ARG A 1 325 ? -50.430 -11.760 41.259  1.00 21.75 ? 345  ARG A CB    1 
ATOM   2423  C  CG    . ARG A 1 325 ? -49.876 -12.140 42.634  1.00 22.04 ? 345  ARG A CG    1 
ATOM   2424  C  CD    . ARG A 1 325 ? -50.941 -12.717 43.574  1.00 22.45 ? 345  ARG A CD    1 
ATOM   2425  N  NE    . ARG A 1 325 ? -51.922 -11.708 43.995  1.00 23.85 ? 345  ARG A NE    1 
ATOM   2426  C  CZ    . ARG A 1 325 ? -53.221 -11.702 43.670  1.00 23.58 ? 345  ARG A CZ    1 
ATOM   2427  N  NH1   . ARG A 1 325 ? -53.748 -12.662 42.925  1.00 23.79 ? 345  ARG A NH1   1 
ATOM   2428  N  NH2   . ARG A 1 325 ? -54.008 -10.726 44.104  1.00 23.11 ? 345  ARG A NH2   1 
ATOM   2429  N  N     . ILE A 1 326 ? -47.215 -11.729 40.900  1.00 20.80 ? 346  ILE A N     1 
ATOM   2430  C  CA    . ILE A 1 326 ? -45.997 -12.517 40.812  1.00 21.45 ? 346  ILE A CA    1 
ATOM   2431  C  C     . ILE A 1 326 ? -45.813 -13.376 42.068  1.00 20.95 ? 346  ILE A C     1 
ATOM   2432  O  O     . ILE A 1 326 ? -45.478 -14.562 41.963  1.00 20.88 ? 346  ILE A O     1 
ATOM   2433  C  CB    . ILE A 1 326 ? -44.806 -11.584 40.650  1.00 21.78 ? 346  ILE A CB    1 
ATOM   2434  C  CG1   . ILE A 1 326 ? -44.873 -10.928 39.269  1.00 23.79 ? 346  ILE A CG1   1 
ATOM   2435  C  CG2   . ILE A 1 326 ? -43.501 -12.331 40.823  1.00 23.06 ? 346  ILE A CG2   1 
ATOM   2436  C  CD1   . ILE A 1 326 ? -43.970 -9.733  39.152  1.00 27.08 ? 346  ILE A CD1   1 
ATOM   2437  N  N     . ALA A 1 327 ? -46.046 -12.777 43.240  1.00 20.09 ? 347  ALA A N     1 
ATOM   2438  C  CA    . ALA A 1 327 ? -45.904 -13.462 44.531  1.00 20.11 ? 347  ALA A CA    1 
ATOM   2439  C  C     . ALA A 1 327 ? -46.956 -13.001 45.546  1.00 19.96 ? 347  ALA A C     1 
ATOM   2440  O  O     . ALA A 1 327 ? -47.123 -11.806 45.775  1.00 19.90 ? 347  ALA A O     1 
ATOM   2441  C  CB    . ALA A 1 327 ? -44.506 -13.207 45.100  1.00 19.89 ? 347  ALA A CB    1 
ATOM   2442  N  N     . TYR A 1 328 ? -47.647 -13.948 46.177  1.00 19.83 ? 348  TYR A N     1 
ATOM   2443  C  CA    . TYR A 1 328 ? -48.581 -13.605 47.251  1.00 19.52 ? 348  TYR A CA    1 
ATOM   2444  C  C     . TYR A 1 328 ? -47.854 -13.188 48.529  1.00 19.34 ? 348  TYR A C     1 
ATOM   2445  O  O     . TYR A 1 328 ? -48.345 -12.324 49.263  1.00 18.87 ? 348  TYR A O     1 
ATOM   2446  C  CB    . TYR A 1 328 ? -49.531 -14.765 47.554  1.00 19.82 ? 348  TYR A CB    1 
ATOM   2447  C  CG    . TYR A 1 328 ? -50.583 -14.410 48.575  1.00 19.49 ? 348  TYR A CG    1 
ATOM   2448  C  CD1   . TYR A 1 328 ? -51.676 -13.636 48.218  1.00 20.13 ? 348  TYR A CD1   1 
ATOM   2449  C  CD2   . TYR A 1 328 ? -50.478 -14.834 49.899  1.00 19.38 ? 348  TYR A CD2   1 
ATOM   2450  C  CE1   . TYR A 1 328 ? -52.654 -13.300 49.149  1.00 19.86 ? 348  TYR A CE1   1 
ATOM   2451  C  CE2   . TYR A 1 328 ? -51.447 -14.505 50.838  1.00 18.83 ? 348  TYR A CE2   1 
ATOM   2452  C  CZ    . TYR A 1 328 ? -52.536 -13.729 50.449  1.00 20.04 ? 348  TYR A CZ    1 
ATOM   2453  O  OH    . TYR A 1 328 ? -53.513 -13.369 51.345  1.00 21.60 ? 348  TYR A OH    1 
ATOM   2454  N  N     . GLU A 1 329 ? -46.691 -13.801 48.790  1.00 19.05 ? 349  GLU A N     1 
ATOM   2455  C  CA    . GLU A 1 329 ? -45.912 -13.538 50.001  1.00 18.04 ? 349  GLU A CA    1 
ATOM   2456  C  C     . GLU A 1 329 ? -44.449 -13.890 49.783  1.00 17.81 ? 349  GLU A C     1 
ATOM   2457  O  O     . GLU A 1 329 ? -44.123 -14.908 49.159  1.00 18.12 ? 349  GLU A O     1 
ATOM   2458  C  CB    . GLU A 1 329 ? -46.457 -14.367 51.169  1.00 18.53 ? 349  GLU A CB    1 
ATOM   2459  C  CG    . GLU A 1 329 ? -45.750 -14.150 52.540  1.00 18.53 ? 349  GLU A CG    1 
ATOM   2460  C  CD    . GLU A 1 329 ? -46.010 -15.283 53.526  1.00 20.16 ? 349  GLU A CD    1 
ATOM   2461  O  OE1   . GLU A 1 329 ? -46.859 -16.145 53.220  1.00 21.39 ? 349  GLU A OE1   1 
ATOM   2462  O  OE2   . GLU A 1 329 ? -45.363 -15.328 54.601  1.00 19.59 ? 349  GLU A OE2   1 
ATOM   2463  N  N     . VAL A 1 330 ? -43.571 -13.025 50.266  1.00 17.01 ? 350  VAL A N     1 
ATOM   2464  C  CA    . VAL A 1 330 ? -42.167 -13.336 50.424  1.00 17.11 ? 350  VAL A CA    1 
ATOM   2465  C  C     . VAL A 1 330 ? -41.824 -12.866 51.831  1.00 17.22 ? 350  VAL A C     1 
ATOM   2466  O  O     . VAL A 1 330 ? -42.020 -11.690 52.154  1.00 16.63 ? 350  VAL A O     1 
ATOM   2467  C  CB    . VAL A 1 330 ? -41.280 -12.614 49.387  1.00 17.38 ? 350  VAL A CB    1 
ATOM   2468  C  CG1   . VAL A 1 330 ? -39.858 -13.171 49.425  1.00 16.58 ? 350  VAL A CG1   1 
ATOM   2469  C  CG2   . VAL A 1 330 ? -41.882 -12.735 47.977  1.00 16.50 ? 350  VAL A CG2   1 
ATOM   2470  N  N     . SER A 1 331 ? -41.352 -13.782 52.675  1.00 17.09 ? 351  SER A N     1 
ATOM   2471  C  CA    . SER A 1 331 ? -41.145 -13.466 54.076  1.00 16.82 ? 351  SER A CA    1 
ATOM   2472  C  C     . SER A 1 331 ? -39.989 -14.230 54.695  1.00 16.70 ? 351  SER A C     1 
ATOM   2473  O  O     . SER A 1 331 ? -39.725 -15.387 54.348  1.00 16.47 ? 351  SER A O     1 
ATOM   2474  C  CB    . SER A 1 331 ? -42.418 -13.755 54.866  1.00 17.07 ? 351  SER A CB    1 
ATOM   2475  O  OG    . SER A 1 331 ? -42.836 -15.098 54.688  1.00 17.54 ? 351  SER A OG    1 
ATOM   2476  N  N     . VAL A 1 332 ? -39.316 -13.560 55.625  1.00 16.35 ? 352  VAL A N     1 
ATOM   2477  C  CA    . VAL A 1 332 ? -38.339 -14.182 56.500  1.00 16.93 ? 352  VAL A CA    1 
ATOM   2478  C  C     . VAL A 1 332 ? -39.086 -15.136 57.435  1.00 16.76 ? 352  VAL A C     1 
ATOM   2479  O  O     . VAL A 1 332 ? -40.123 -14.780 58.015  1.00 16.16 ? 352  VAL A O     1 
ATOM   2480  C  CB    . VAL A 1 332 ? -37.558 -13.117 57.328  1.00 17.25 ? 352  VAL A CB    1 
ATOM   2481  C  CG1   . VAL A 1 332 ? -36.418 -13.759 58.132  1.00 17.55 ? 352  VAL A CG1   1 
ATOM   2482  C  CG2   . VAL A 1 332 ? -37.015 -12.009 56.400  1.00 18.09 ? 352  VAL A CG2   1 
ATOM   2483  N  N     . GLN A 1 333 ? -38.578 -16.363 57.538  1.00 16.80 ? 353  GLN A N     1 
ATOM   2484  C  CA    . GLN A 1 333 ? -39.179 -17.392 58.383  1.00 17.17 ? 353  GLN A CA    1 
ATOM   2485  C  C     . GLN A 1 333 ? -38.359 -17.711 59.632  1.00 17.61 ? 353  GLN A C     1 
ATOM   2486  O  O     . GLN A 1 333 ? -38.917 -17.972 60.693  1.00 18.15 ? 353  GLN A O     1 
ATOM   2487  C  CB    . GLN A 1 333 ? -39.375 -18.663 57.557  1.00 17.16 ? 353  GLN A CB    1 
ATOM   2488  C  CG    . GLN A 1 333 ? -40.456 -18.515 56.487  1.00 16.87 ? 353  GLN A CG    1 
ATOM   2489  C  CD    . GLN A 1 333 ? -41.834 -18.325 57.091  1.00 16.36 ? 353  GLN A CD    1 
ATOM   2490  O  OE1   . GLN A 1 333 ? -42.207 -19.047 58.012  1.00 16.75 ? 353  GLN A OE1   1 
ATOM   2491  N  NE2   . GLN A 1 333 ? -42.603 -17.366 56.567  1.00 15.98 ? 353  GLN A NE2   1 
ATOM   2492  N  N     . GLU A 1 334 ? -37.036 -17.729 59.496  1.00 17.92 ? 354  GLU A N     1 
ATOM   2493  C  CA    . GLU A 1 334 ? -36.144 -18.044 60.610  1.00 18.32 ? 354  GLU A CA    1 
ATOM   2494  C  C     . GLU A 1 334 ? -34.730 -17.618 60.231  1.00 18.32 ? 354  GLU A C     1 
ATOM   2495  O  O     . GLU A 1 334 ? -34.397 -17.527 59.054  1.00 17.92 ? 354  GLU A O     1 
ATOM   2496  C  CB    . GLU A 1 334 ? -36.184 -19.543 60.939  1.00 18.43 ? 354  GLU A CB    1 
ATOM   2497  C  CG    . GLU A 1 334 ? -35.383 -19.979 62.194  1.00 19.39 ? 354  GLU A CG    1 
ATOM   2498  C  CD    . GLU A 1 334 ? -35.782 -19.227 63.450  1.00 20.41 ? 354  GLU A CD    1 
ATOM   2499  O  OE1   . GLU A 1 334 ? -36.629 -19.743 64.219  1.00 22.13 ? 354  GLU A OE1   1 
ATOM   2500  O  OE2   . GLU A 1 334 ? -35.268 -18.108 63.652  1.00 19.55 ? 354  GLU A OE2   1 
ATOM   2501  N  N     . ALA A 1 335 ? -33.920 -17.327 61.238  1.00 18.85 ? 355  ALA A N     1 
ATOM   2502  C  CA    . ALA A 1 335 ? -32.515 -16.962 61.033  1.00 18.82 ? 355  ALA A CA    1 
ATOM   2503  C  C     . ALA A 1 335 ? -31.732 -17.536 62.196  1.00 18.93 ? 355  ALA A C     1 
ATOM   2504  O  O     . ALA A 1 335 ? -32.058 -17.265 63.351  1.00 18.94 ? 355  ALA A O     1 
ATOM   2505  C  CB    . ALA A 1 335 ? -32.352 -15.469 60.963  1.00 18.49 ? 355  ALA A CB    1 
ATOM   2506  N  N     . VAL A 1 336 ? -30.715 -18.337 61.886  1.00 18.55 ? 356  VAL A N     1 
ATOM   2507  C  CA    . VAL A 1 336 ? -30.031 -19.129 62.895  1.00 18.73 ? 356  VAL A CA    1 
ATOM   2508  C  C     . VAL A 1 336 ? -28.525 -18.949 62.794  1.00 18.95 ? 356  VAL A C     1 
ATOM   2509  O  O     . VAL A 1 336 ? -27.992 -18.604 61.725  1.00 18.89 ? 356  VAL A O     1 
ATOM   2510  C  CB    . VAL A 1 336 ? -30.376 -20.653 62.782  1.00 18.69 ? 356  VAL A CB    1 
ATOM   2511  C  CG1   . VAL A 1 336 ? -31.877 -20.873 62.643  1.00 18.28 ? 356  VAL A CG1   1 
ATOM   2512  C  CG2   . VAL A 1 336 ? -29.651 -21.296 61.617  1.00 18.80 ? 356  VAL A CG2   1 
ATOM   2513  N  N     . ALA A 1 337 ? -27.862 -19.172 63.920  1.00 18.48 ? 357  ALA A N     1 
ATOM   2514  C  CA    . ALA A 1 337 ? -26.421 -19.153 64.009  1.00 18.89 ? 357  ALA A CA    1 
ATOM   2515  C  C     . ALA A 1 337 ? -26.012 -20.373 64.837  1.00 19.06 ? 357  ALA A C     1 
ATOM   2516  O  O     . ALA A 1 337 ? -26.336 -20.466 66.030  1.00 19.67 ? 357  ALA A O     1 
ATOM   2517  C  CB    . ALA A 1 337 ? -25.926 -17.825 64.639  1.00 18.62 ? 357  ALA A CB    1 
ATOM   2518  N  N     . LEU A 1 338 ? -25.339 -21.323 64.189  1.00 18.96 ? 358  LEU A N     1 
ATOM   2519  C  CA    . LEU A 1 338 ? -25.072 -22.631 64.778  1.00 19.00 ? 358  LEU A CA    1 
ATOM   2520  C  C     . LEU A 1 338 ? -23.600 -22.723 65.103  1.00 19.05 ? 358  LEU A C     1 
ATOM   2521  O  O     . LEU A 1 338 ? -22.769 -22.680 64.193  1.00 18.96 ? 358  LEU A O     1 
ATOM   2522  C  CB    . LEU A 1 338 ? -25.455 -23.735 63.793  1.00 18.82 ? 358  LEU A CB    1 
ATOM   2523  C  CG    . LEU A 1 338 ? -26.882 -23.683 63.237  1.00 20.03 ? 358  LEU A CG    1 
ATOM   2524  C  CD1   . LEU A 1 338 ? -27.133 -24.803 62.212  1.00 19.73 ? 358  LEU A CD1   1 
ATOM   2525  C  CD2   . LEU A 1 338 ? -27.908 -23.744 64.387  1.00 19.82 ? 358  LEU A CD2   1 
ATOM   2526  N  N     . TYR A 1 339 ? -23.280 -22.868 66.386  1.00 19.13 ? 359  TYR A N     1 
ATOM   2527  C  CA    . TYR A 1 339 ? -21.907 -22.718 66.858  1.00 19.72 ? 359  TYR A CA    1 
ATOM   2528  C  C     . TYR A 1 339 ? -21.229 -24.022 67.196  1.00 20.15 ? 359  TYR A C     1 
ATOM   2529  O  O     . TYR A 1 339 ? -21.882 -25.024 67.490  1.00 20.43 ? 359  TYR A O     1 
ATOM   2530  C  CB    . TYR A 1 339 ? -21.881 -21.803 68.095  1.00 19.97 ? 359  TYR A CB    1 
ATOM   2531  C  CG    . TYR A 1 339 ? -22.197 -20.370 67.728  1.00 19.21 ? 359  TYR A CG    1 
ATOM   2532  C  CD1   . TYR A 1 339 ? -21.171 -19.458 67.499  1.00 17.39 ? 359  TYR A CD1   1 
ATOM   2533  C  CD2   . TYR A 1 339 ? -23.511 -19.948 67.548  1.00 18.40 ? 359  TYR A CD2   1 
ATOM   2534  C  CE1   . TYR A 1 339 ? -21.437 -18.166 67.121  1.00 17.82 ? 359  TYR A CE1   1 
ATOM   2535  C  CE2   . TYR A 1 339 ? -23.796 -18.640 67.170  1.00 18.61 ? 359  TYR A CE2   1 
ATOM   2536  C  CZ    . TYR A 1 339 ? -22.754 -17.757 66.953  1.00 18.46 ? 359  TYR A CZ    1 
ATOM   2537  O  OH    . TYR A 1 339 ? -23.004 -16.464 66.582  1.00 19.56 ? 359  TYR A OH    1 
ATOM   2538  N  N     . GLY A 1 340 ? -19.901 -23.990 67.153  1.00 20.95 ? 360  GLY A N     1 
ATOM   2539  C  CA    . GLY A 1 340 ? -19.072 -24.993 67.816  1.00 21.51 ? 360  GLY A CA    1 
ATOM   2540  C  C     . GLY A 1 340 ? -18.274 -24.259 68.871  1.00 22.16 ? 360  GLY A C     1 
ATOM   2541  O  O     . GLY A 1 340 ? -18.138 -23.029 68.799  1.00 22.06 ? 360  GLY A O     1 
ATOM   2542  N  N     . GLY A 1 341 ? -17.756 -24.987 69.858  1.00 22.83 ? 361  GLY A N     1 
ATOM   2543  C  CA    . GLY A 1 341 ? -16.916 -24.362 70.871  1.00 23.41 ? 361  GLY A CA    1 
ATOM   2544  C  C     . GLY A 1 341 ? -16.147 -25.291 71.796  1.00 24.11 ? 361  GLY A C     1 
ATOM   2545  O  O     . GLY A 1 341 ? -16.491 -26.462 71.974  1.00 24.25 ? 361  GLY A O     1 
ATOM   2546  N  N     . HIS A 1 342 ? -15.110 -24.721 72.402  1.00 24.76 ? 362  HIS A N     1 
ATOM   2547  C  CA    . HIS A 1 342 ? -14.317 -25.377 73.434  1.00 25.27 ? 362  HIS A CA    1 
ATOM   2548  C  C     . HIS A 1 342 ? -14.951 -25.230 74.819  1.00 25.08 ? 362  HIS A C     1 
ATOM   2549  O  O     . HIS A 1 342 ? -14.782 -26.097 75.677  1.00 25.23 ? 362  HIS A O     1 
ATOM   2550  C  CB    . HIS A 1 342 ? -12.890 -24.816 73.442  1.00 25.71 ? 362  HIS A CB    1 
ATOM   2551  C  CG    . HIS A 1 342 ? -12.802 -23.349 73.755  1.00 28.14 ? 362  HIS A CG    1 
ATOM   2552  N  ND1   . HIS A 1 342 ? -13.372 -22.375 72.958  1.00 30.27 ? 362  HIS A ND1   1 
ATOM   2553  C  CD2   . HIS A 1 342 ? -12.181 -22.688 74.763  1.00 30.61 ? 362  HIS A CD2   1 
ATOM   2554  C  CE1   . HIS A 1 342 ? -13.138 -21.183 73.480  1.00 30.13 ? 362  HIS A CE1   1 
ATOM   2555  N  NE2   . HIS A 1 342 ? -12.407 -21.344 74.570  1.00 30.82 ? 362  HIS A NE2   1 
ATOM   2556  N  N     . THR A 1 343 ? -15.665 -24.133 75.050  1.00 24.79 ? 363  THR A N     1 
ATOM   2557  C  CA    . THR A 1 343 ? -16.351 -23.940 76.325  1.00 24.30 ? 363  THR A CA    1 
ATOM   2558  C  C     . THR A 1 343 ? -17.745 -24.562 76.231  1.00 24.28 ? 363  THR A C     1 
ATOM   2559  O  O     . THR A 1 343 ? -18.254 -24.740 75.124  1.00 24.45 ? 363  THR A O     1 
ATOM   2560  C  CB    . THR A 1 343 ? -16.446 -22.449 76.716  1.00 24.41 ? 363  THR A CB    1 
ATOM   2561  O  OG1   . THR A 1 343 ? -17.495 -21.803 75.979  1.00 23.37 ? 363  THR A OG1   1 
ATOM   2562  C  CG2   . THR A 1 343 ? -15.121 -21.743 76.473  1.00 23.20 ? 363  THR A CG2   1 
ATOM   2563  N  N     . PRO A 1 344 ? -18.361 -24.902 77.383  1.00 24.01 ? 364  PRO A N     1 
ATOM   2564  C  CA    . PRO A 1 344 ? -19.720 -25.473 77.389  1.00 23.78 ? 364  PRO A CA    1 
ATOM   2565  C  C     . PRO A 1 344 ? -20.786 -24.565 76.750  1.00 23.59 ? 364  PRO A C     1 
ATOM   2566  O  O     . PRO A 1 344 ? -21.667 -25.057 76.031  1.00 23.41 ? 364  PRO A O     1 
ATOM   2567  C  CB    . PRO A 1 344 ? -20.029 -25.681 78.884  1.00 24.13 ? 364  PRO A CB    1 
ATOM   2568  C  CG    . PRO A 1 344 ? -18.735 -25.584 79.594  1.00 24.12 ? 364  PRO A CG    1 
ATOM   2569  C  CD    . PRO A 1 344 ? -17.793 -24.799 78.743  1.00 24.17 ? 364  PRO A CD    1 
ATOM   2570  N  N     . ALA A 1 345 ? -20.704 -23.261 77.016  1.00 23.12 ? 365  ALA A N     1 
ATOM   2571  C  CA    . ALA A 1 345 ? -21.604 -22.282 76.397  1.00 23.10 ? 365  ALA A CA    1 
ATOM   2572  C  C     . ALA A 1 345 ? -21.459 -22.292 74.885  1.00 22.92 ? 365  ALA A C     1 
ATOM   2573  O  O     . ALA A 1 345 ? -22.452 -22.241 74.164  1.00 22.54 ? 365  ALA A O     1 
ATOM   2574  C  CB    . ALA A 1 345 ? -21.331 -20.875 76.932  1.00 22.86 ? 365  ALA A CB    1 
ATOM   2575  N  N     . GLY A 1 346 ? -20.215 -22.356 74.417  1.00 22.88 ? 366  GLY A N     1 
ATOM   2576  C  CA    . GLY A 1 346 ? -19.924 -22.346 72.994  1.00 23.06 ? 366  GLY A CA    1 
ATOM   2577  C  C     . GLY A 1 346 ? -20.444 -23.573 72.287  1.00 23.00 ? 366  GLY A C     1 
ATOM   2578  O  O     . GLY A 1 346 ? -21.074 -23.471 71.237  1.00 23.21 ? 366  GLY A O     1 
ATOM   2579  N  N     . MET A 1 347 ? -20.197 -24.744 72.863  1.00 23.37 ? 367  MET A N     1 
ATOM   2580  C  CA    . MET A 1 347 ? -20.697 -25.982 72.270  1.00 23.25 ? 367  MET A CA    1 
ATOM   2581  C  C     . MET A 1 347 ? -22.223 -26.157 72.440  1.00 22.71 ? 367  MET A C     1 
ATOM   2582  O  O     . MET A 1 347 ? -22.829 -27.009 71.796  1.00 22.59 ? 367  MET A O     1 
ATOM   2583  C  CB    . MET A 1 347 ? -19.891 -27.202 72.746  1.00 23.54 ? 367  MET A CB    1 
ATOM   2584  C  CG    . MET A 1 347 ? -19.961 -27.571 74.208  1.00 25.39 ? 367  MET A CG    1 
ATOM   2585  S  SD    . MET A 1 347 ? -18.914 -29.010 74.585  1.00 27.17 ? 367  MET A SD    1 
ATOM   2586  C  CE    . MET A 1 347 ? -17.257 -28.317 74.561  1.00 26.15 ? 367  MET A CE    1 
ATOM   2587  N  N     . GLN A 1 348 ? -22.846 -25.323 73.267  1.00 22.04 ? 368  GLN A N     1 
ATOM   2588  C  CA    . GLN A 1 348 ? -24.294 -25.357 73.453  1.00 21.54 ? 368  GLN A CA    1 
ATOM   2589  C  C     . GLN A 1 348 ? -25.048 -24.515 72.416  1.00 21.36 ? 368  GLN A C     1 
ATOM   2590  O  O     . GLN A 1 348 ? -26.220 -24.770 72.141  1.00 21.25 ? 368  GLN A O     1 
ATOM   2591  C  CB    . GLN A 1 348 ? -24.647 -24.829 74.848  1.00 21.50 ? 368  GLN A CB    1 
ATOM   2592  C  CG    . GLN A 1 348 ? -26.115 -24.998 75.245  1.00 21.26 ? 368  GLN A CG    1 
ATOM   2593  C  CD    . GLN A 1 348 ? -26.497 -26.447 75.390  1.00 20.41 ? 368  GLN A CD    1 
ATOM   2594  O  OE1   . GLN A 1 348 ? -25.636 -27.297 75.619  1.00 20.99 ? 368  GLN A OE1   1 
ATOM   2595  N  NE2   . GLN A 1 348 ? -27.786 -26.743 75.264  1.00 20.31 ? 368  GLN A NE2   1 
ATOM   2596  N  N     . THR A 1 349 ? -24.387 -23.501 71.858  1.00 21.36 ? 369  THR A N     1 
ATOM   2597  C  CA    . THR A 1 349 ? -25.106 -22.419 71.172  1.00 21.08 ? 369  THR A CA    1 
ATOM   2598  C  C     . THR A 1 349 ? -25.640 -22.763 69.789  1.00 21.26 ? 369  THR A C     1 
ATOM   2599  O  O     . THR A 1 349 ? -24.886 -22.909 68.831  1.00 21.28 ? 369  THR A O     1 
ATOM   2600  C  CB    . THR A 1 349 ? -24.264 -21.146 71.044  1.00 20.88 ? 369  THR A CB    1 
ATOM   2601  O  OG1   . THR A 1 349 ? -23.772 -20.773 72.336  1.00 20.86 ? 369  THR A OG1   1 
ATOM   2602  C  CG2   . THR A 1 349 ? -25.112 -20.004 70.444  1.00 19.57 ? 369  THR A CG2   1 
ATOM   2603  N  N     . LYS A 1 350 ? -26.958 -22.878 69.709  1.00 21.53 ? 370  LYS A N     1 
ATOM   2604  C  CA    . LYS A 1 350 ? -27.660 -22.862 68.440  1.00 21.83 ? 370  LYS A CA    1 
ATOM   2605  C  C     . LYS A 1 350 ? -28.758 -21.821 68.549  1.00 21.57 ? 370  LYS A C     1 
ATOM   2606  O  O     . LYS A 1 350 ? -29.857 -22.111 69.017  1.00 21.30 ? 370  LYS A O     1 
ATOM   2607  C  CB    . LYS A 1 350 ? -28.251 -24.235 68.124  1.00 22.29 ? 370  LYS A CB    1 
ATOM   2608  C  CG    . LYS A 1 350 ? -27.237 -25.344 68.057  1.00 24.24 ? 370  LYS A CG    1 
ATOM   2609  C  CD    . LYS A 1 350 ? -27.919 -26.689 67.937  1.00 26.77 ? 370  LYS A CD    1 
ATOM   2610  C  CE    . LYS A 1 350 ? -26.910 -27.801 67.756  1.00 27.67 ? 370  LYS A CE    1 
ATOM   2611  N  NZ    . LYS A 1 350 ? -26.111 -28.010 68.982  1.00 28.77 ? 370  LYS A NZ    1 
ATOM   2612  N  N     . TYR A 1 351 ? -28.455 -20.596 68.137  1.00 21.53 ? 371  TYR A N     1 
ATOM   2613  C  CA    . TYR A 1 351 ? -29.431 -19.517 68.243  1.00 21.81 ? 371  TYR A CA    1 
ATOM   2614  C  C     . TYR A 1 351 ? -30.461 -19.569 67.107  1.00 21.87 ? 371  TYR A C     1 
ATOM   2615  O  O     . TYR A 1 351 ? -30.086 -19.570 65.935  1.00 21.55 ? 371  TYR A O     1 
ATOM   2616  C  CB    . TYR A 1 351 ? -28.746 -18.154 68.228  1.00 21.80 ? 371  TYR A CB    1 
ATOM   2617  C  CG    . TYR A 1 351 ? -28.096 -17.726 69.523  1.00 21.84 ? 371  TYR A CG    1 
ATOM   2618  C  CD1   . TYR A 1 351 ? -28.790 -17.788 70.729  1.00 22.66 ? 371  TYR A CD1   1 
ATOM   2619  C  CD2   . TYR A 1 351 ? -26.810 -17.196 69.530  1.00 21.65 ? 371  TYR A CD2   1 
ATOM   2620  C  CE1   . TYR A 1 351 ? -28.207 -17.370 71.916  1.00 23.00 ? 371  TYR A CE1   1 
ATOM   2621  C  CE2   . TYR A 1 351 ? -26.214 -16.769 70.714  1.00 23.44 ? 371  TYR A CE2   1 
ATOM   2622  C  CZ    . TYR A 1 351 ? -26.918 -16.868 71.905  1.00 22.59 ? 371  TYR A CZ    1 
ATOM   2623  O  OH    . TYR A 1 351 ? -26.348 -16.446 73.080  1.00 24.12 ? 371  TYR A OH    1 
ATOM   2624  N  N     . LEU A 1 352 ? -31.744 -19.601 67.473  1.00 21.88 ? 372  LEU A N     1 
ATOM   2625  C  CA    . LEU A 1 352 ? -32.863 -19.461 66.529  1.00 22.24 ? 372  LEU A CA    1 
ATOM   2626  C  C     . LEU A 1 352 ? -33.598 -18.152 66.828  1.00 22.24 ? 372  LEU A C     1 
ATOM   2627  O  O     . LEU A 1 352 ? -34.333 -18.058 67.812  1.00 22.03 ? 372  LEU A O     1 
ATOM   2628  C  CB    . LEU A 1 352 ? -33.833 -20.633 66.655  1.00 22.08 ? 372  LEU A CB    1 
ATOM   2629  C  CG    . LEU A 1 352 ? -33.453 -21.896 65.898  1.00 23.60 ? 372  LEU A CG    1 
ATOM   2630  C  CD1   . LEU A 1 352 ? -32.151 -22.477 66.416  1.00 22.35 ? 372  LEU A CD1   1 
ATOM   2631  C  CD2   . LEU A 1 352 ? -34.601 -22.919 65.969  1.00 23.54 ? 372  LEU A CD2   1 
ATOM   2632  N  N     . ASP A 1 353 ? -33.423 -17.154 65.967  1.00 22.21 ? 373  ASP A N     1 
ATOM   2633  C  CA    . ASP A 1 353 ? -33.775 -15.781 66.328  1.00 22.86 ? 373  ASP A CA    1 
ATOM   2634  C  C     . ASP A 1 353 ? -35.265 -15.450 66.408  1.00 22.51 ? 373  ASP A C     1 
ATOM   2635  O  O     . ASP A 1 353 ? -35.633 -14.520 67.115  1.00 22.27 ? 373  ASP A O     1 
ATOM   2636  C  CB    . ASP A 1 353 ? -33.053 -14.795 65.415  1.00 23.55 ? 373  ASP A CB    1 
ATOM   2637  C  CG    . ASP A 1 353 ? -31.548 -14.812 65.629  1.00 25.76 ? 373  ASP A CG    1 
ATOM   2638  O  OD1   . ASP A 1 353 ? -31.070 -15.355 66.659  1.00 27.96 ? 373  ASP A OD1   1 
ATOM   2639  O  OD2   . ASP A 1 353 ? -30.837 -14.290 64.765  1.00 31.58 ? 373  ASP A OD2   1 
ATOM   2640  N  N     . VAL A 1 354 ? -36.123 -16.197 65.723  1.00 22.22 ? 374  VAL A N     1 
ATOM   2641  C  CA    . VAL A 1 354 ? -37.565 -16.006 65.881  1.00 22.49 ? 374  VAL A CA    1 
ATOM   2642  C  C     . VAL A 1 354 ? -37.966 -16.307 67.337  1.00 23.01 ? 374  VAL A C     1 
ATOM   2643  O  O     . VAL A 1 354 ? -38.963 -15.781 67.835  1.00 22.93 ? 374  VAL A O     1 
ATOM   2644  C  CB    . VAL A 1 354 ? -38.390 -16.840 64.856  1.00 22.55 ? 374  VAL A CB    1 
ATOM   2645  C  CG1   . VAL A 1 354 ? -39.847 -16.878 65.224  1.00 21.94 ? 374  VAL A CG1   1 
ATOM   2646  C  CG2   . VAL A 1 354 ? -38.219 -16.267 63.440  1.00 21.46 ? 374  VAL A CG2   1 
ATOM   2647  N  N     . GLY A 1 355 ? -37.150 -17.111 68.020  1.00 23.31 ? 375  GLY A N     1 
ATOM   2648  C  CA    . GLY A 1 355 ? -37.311 -17.360 69.446  1.00 23.98 ? 375  GLY A CA    1 
ATOM   2649  C  C     . GLY A 1 355 ? -37.056 -16.137 70.321  1.00 24.30 ? 375  GLY A C     1 
ATOM   2650  O  O     . GLY A 1 355 ? -37.312 -16.178 71.525  1.00 24.32 ? 375  GLY A O     1 
ATOM   2651  N  N     . TRP A 1 356 ? -36.564 -15.059 69.706  1.00 24.49 ? 376  TRP A N     1 
ATOM   2652  C  CA    . TRP A 1 356 ? -36.232 -13.813 70.391  1.00 24.74 ? 376  TRP A CA    1 
ATOM   2653  C  C     . TRP A 1 356 ? -37.001 -12.620 69.832  1.00 24.65 ? 376  TRP A C     1 
ATOM   2654  O  O     . TRP A 1 356 ? -36.661 -11.477 70.121  1.00 25.61 ? 376  TRP A O     1 
ATOM   2655  C  CB    . TRP A 1 356 ? -34.733 -13.551 70.253  1.00 24.78 ? 376  TRP A CB    1 
ATOM   2656  C  CG    . TRP A 1 356 ? -33.894 -14.649 70.817  1.00 25.59 ? 376  TRP A CG    1 
ATOM   2657  C  CD1   . TRP A 1 356 ? -33.514 -15.801 70.190  1.00 25.64 ? 376  TRP A CD1   1 
ATOM   2658  C  CD2   . TRP A 1 356 ? -33.341 -14.710 72.131  1.00 25.75 ? 376  TRP A CD2   1 
ATOM   2659  N  NE1   . TRP A 1 356 ? -32.750 -16.571 71.029  1.00 25.62 ? 376  TRP A NE1   1 
ATOM   2660  C  CE2   . TRP A 1 356 ? -32.630 -15.925 72.230  1.00 25.25 ? 376  TRP A CE2   1 
ATOM   2661  C  CE3   . TRP A 1 356 ? -33.362 -13.848 73.231  1.00 25.67 ? 376  TRP A CE3   1 
ATOM   2662  C  CZ2   . TRP A 1 356 ? -31.953 -16.301 73.387  1.00 26.02 ? 376  TRP A CZ2   1 
ATOM   2663  C  CZ3   . TRP A 1 356 ? -32.703 -14.232 74.389  1.00 25.95 ? 376  TRP A CZ3   1 
ATOM   2664  C  CH2   . TRP A 1 356 ? -31.995 -15.439 74.453  1.00 26.37 ? 376  TRP A CH2   1 
ATOM   2665  N  N     . GLY A 1 357 ? -38.037 -12.876 69.041  1.00 24.49 ? 377  GLY A N     1 
ATOM   2666  C  CA    . GLY A 1 357 ? -38.820 -11.814 68.442  1.00 24.22 ? 377  GLY A CA    1 
ATOM   2667  C  C     . GLY A 1 357 ? -37.985 -11.069 67.424  1.00 24.21 ? 377  GLY A C     1 
ATOM   2668  O  O     . GLY A 1 357 ? -37.770 -9.866  67.538  1.00 24.55 ? 377  GLY A O     1 
ATOM   2669  N  N     . LEU A 1 358 ? -37.513 -11.805 66.426  1.00 24.06 ? 378  LEU A N     1 
ATOM   2670  C  CA    . LEU A 1 358 ? -36.708 -11.253 65.330  1.00 23.94 ? 378  LEU A CA    1 
ATOM   2671  C  C     . LEU A 1 358 ? -37.324 -9.982  64.720  1.00 23.37 ? 378  LEU A C     1 
ATOM   2672  O  O     . LEU A 1 358 ? -36.610 -9.035  64.397  1.00 22.87 ? 378  LEU A O     1 
ATOM   2673  C  CB    . LEU A 1 358 ? -36.527 -12.339 64.260  1.00 24.02 ? 378  LEU A CB    1 
ATOM   2674  C  CG    . LEU A 1 358 ? -35.585 -12.144 63.078  1.00 24.63 ? 378  LEU A CG    1 
ATOM   2675  C  CD1   . LEU A 1 358 ? -34.140 -11.958 63.541  1.00 27.53 ? 378  LEU A CD1   1 
ATOM   2676  C  CD2   . LEU A 1 358 ? -35.710 -13.366 62.173  1.00 24.40 ? 378  LEU A CD2   1 
ATOM   2677  N  N     . GLY A 1 359 ? -38.651 -9.961  64.602  1.00 22.99 ? 379  GLY A N     1 
ATOM   2678  C  CA    . GLY A 1 359 ? -39.364 -8.829  64.008  1.00 22.80 ? 379  GLY A CA    1 
ATOM   2679  C  C     . GLY A 1 359 ? -39.646 -7.644  64.922  1.00 22.83 ? 379  GLY A C     1 
ATOM   2680  O  O     . GLY A 1 359 ? -40.192 -6.645  64.471  1.00 23.47 ? 379  GLY A O     1 
ATOM   2681  N  N     . SER A 1 360 ? -39.281 -7.735  66.197  1.00 22.54 ? 380  SER A N     1 
ATOM   2682  C  CA    . SER A 1 360 ? -39.570 -6.666  67.154  1.00 22.44 ? 380  SER A CA    1 
ATOM   2683  C  C     . SER A 1 360 ? -38.305 -6.053  67.775  1.00 21.68 ? 380  SER A C     1 
ATOM   2684  O  O     . SER A 1 360 ? -38.383 -5.331  68.763  1.00 21.56 ? 380  SER A O     1 
ATOM   2685  C  CB    . SER A 1 360 ? -40.518 -7.175  68.244  1.00 22.67 ? 380  SER A CB    1 
ATOM   2686  O  OG    . SER A 1 360 ? -39.990 -8.332  68.868  1.00 24.38 ? 380  SER A OG    1 
ATOM   2687  N  N     . VAL A 1 361 ? -37.150 -6.339  67.180  1.00 20.71 ? 381  VAL A N     1 
ATOM   2688  C  CA    . VAL A 1 361 ? -35.899 -5.717  67.572  1.00 20.13 ? 381  VAL A CA    1 
ATOM   2689  C  C     . VAL A 1 361 ? -35.419 -4.835  66.419  1.00 19.72 ? 381  VAL A C     1 
ATOM   2690  O  O     . VAL A 1 361 ? -34.228 -4.731  66.122  1.00 19.34 ? 381  VAL A O     1 
ATOM   2691  C  CB    . VAL A 1 361 ? -34.859 -6.765  68.007  1.00 20.25 ? 381  VAL A CB    1 
ATOM   2692  C  CG1   . VAL A 1 361 ? -35.226 -7.301  69.376  1.00 19.95 ? 381  VAL A CG1   1 
ATOM   2693  C  CG2   . VAL A 1 361 ? -34.755 -7.898  66.988  1.00 20.18 ? 381  VAL A CG2   1 
ATOM   2694  N  N     . THR A 1 362 ? -36.406 -4.196  65.798  1.00 19.32 ? 382  THR A N     1 
ATOM   2695  C  CA    . THR A 1 362 ? -36.250 -3.277  64.701  1.00 19.18 ? 382  THR A CA    1 
ATOM   2696  C  C     . THR A 1 362 ? -35.925 -1.876  65.220  1.00 19.37 ? 382  THR A C     1 
ATOM   2697  O  O     . THR A 1 362 ? -36.774 -0.967  65.201  1.00 19.44 ? 382  THR A O     1 
ATOM   2698  C  CB    . THR A 1 362 ? -37.576 -3.215  63.916  1.00 19.35 ? 382  THR A CB    1 
ATOM   2699  O  OG1   . THR A 1 362 ? -38.638 -2.858  64.812  1.00 17.74 ? 382  THR A OG1   1 
ATOM   2700  C  CG2   . THR A 1 362 ? -37.889 -4.583  63.278  1.00 19.23 ? 382  THR A CG2   1 
ATOM   2701  N  N     . HIS A 1 363 ? -34.689 -1.689  65.665  1.00 19.52 ? 383  HIS A N     1 
ATOM   2702  C  CA    . HIS A 1 363 ? -34.328 -0.447  66.347  1.00 19.89 ? 383  HIS A CA    1 
ATOM   2703  C  C     . HIS A 1 363 ? -33.984 0.666   65.368  1.00 19.90 ? 383  HIS A C     1 
ATOM   2704  O  O     . HIS A 1 363 ? -33.913 0.449   64.154  1.00 19.61 ? 383  HIS A O     1 
ATOM   2705  C  CB    . HIS A 1 363 ? -33.272 -0.705  67.433  1.00 20.11 ? 383  HIS A CB    1 
ATOM   2706  C  CG    . HIS A 1 363 ? -33.861 -1.336  68.662  1.00 21.54 ? 383  HIS A CG    1 
ATOM   2707  N  ND1   . HIS A 1 363 ? -34.728 -0.662  69.496  1.00 22.01 ? 383  HIS A ND1   1 
ATOM   2708  C  CD2   . HIS A 1 363 ? -33.772 -2.595  69.154  1.00 23.26 ? 383  HIS A CD2   1 
ATOM   2709  C  CE1   . HIS A 1 363 ? -35.119 -1.469  70.467  1.00 22.62 ? 383  HIS A CE1   1 
ATOM   2710  N  NE2   . HIS A 1 363 ? -34.550 -2.647  70.285  1.00 22.88 ? 383  HIS A NE2   1 
ATOM   2711  N  N     . GLU A 1 364 ? -33.836 1.872   65.899  1.00 20.21 ? 384  GLU A N     1 
ATOM   2712  C  CA    . GLU A 1 364 ? -33.921 3.077   65.101  1.00 20.16 ? 384  GLU A CA    1 
ATOM   2713  C  C     . GLU A 1 364 ? -32.841 3.167   64.023  1.00 20.36 ? 384  GLU A C     1 
ATOM   2714  O  O     . GLU A 1 364 ? -31.645 3.089   64.311  1.00 19.41 ? 384  GLU A O     1 
ATOM   2715  C  CB    . GLU A 1 364 ? -33.881 4.293   66.019  1.00 20.36 ? 384  GLU A CB    1 
ATOM   2716  C  CG    . GLU A 1 364 ? -34.016 5.654   65.324  1.00 21.24 ? 384  GLU A CG    1 
ATOM   2717  C  CD    . GLU A 1 364 ? -34.092 6.796   66.328  1.00 22.95 ? 384  GLU A CD    1 
ATOM   2718  O  OE1   . GLU A 1 364 ? -34.196 6.523   67.558  1.00 22.33 ? 384  GLU A OE1   1 
ATOM   2719  O  OE2   . GLU A 1 364 ? -34.050 7.962   65.889  1.00 22.93 ? 384  GLU A OE2   1 
ATOM   2720  N  N     . LEU A 1 365 ? -33.298 3.339   62.781  1.00 20.45 ? 385  LEU A N     1 
ATOM   2721  C  CA    . LEU A 1 365 ? -32.431 3.495   61.632  1.00 20.85 ? 385  LEU A CA    1 
ATOM   2722  C  C     . LEU A 1 365 ? -31.871 4.915   61.603  1.00 21.20 ? 385  LEU A C     1 
ATOM   2723  O  O     . LEU A 1 365 ? -32.635 5.882   61.649  1.00 21.38 ? 385  LEU A O     1 
ATOM   2724  C  CB    . LEU A 1 365 ? -33.214 3.209   60.338  1.00 21.28 ? 385  LEU A CB    1 
ATOM   2725  C  CG    . LEU A 1 365 ? -33.767 1.786   60.158  1.00 20.81 ? 385  LEU A CG    1 
ATOM   2726  C  CD1   . LEU A 1 365 ? -34.825 1.725   59.030  1.00 20.89 ? 385  LEU A CD1   1 
ATOM   2727  C  CD2   . LEU A 1 365 ? -32.640 0.822   59.892  1.00 20.52 ? 385  LEU A CD2   1 
ATOM   2728  N  N     . ALA A 1 366 ? -30.543 5.030   61.535  1.00 21.37 ? 386  ALA A N     1 
ATOM   2729  C  CA    . ALA A 1 366 ? -29.858 6.323   61.539  1.00 21.45 ? 386  ALA A CA    1 
ATOM   2730  C  C     . ALA A 1 366 ? -29.825 6.943   60.140  1.00 21.78 ? 386  ALA A C     1 
ATOM   2731  O  O     . ALA A 1 366 ? -29.180 6.390   59.241  1.00 21.81 ? 386  ALA A O     1 
ATOM   2732  C  CB    . ALA A 1 366 ? -28.437 6.161   62.074  1.00 21.06 ? 386  ALA A CB    1 
ATOM   2733  N  N     . PRO A 1 367 ? -30.496 8.100   59.947  1.00 22.40 ? 387  PRO A N     1 
ATOM   2734  C  CA    . PRO A 1 367 ? -30.553 8.681   58.602  1.00 22.90 ? 387  PRO A CA    1 
ATOM   2735  C  C     . PRO A 1 367 ? -29.192 9.101   58.069  1.00 23.46 ? 387  PRO A C     1 
ATOM   2736  O  O     . PRO A 1 367 ? -28.428 9.785   58.763  1.00 23.55 ? 387  PRO A O     1 
ATOM   2737  C  CB    . PRO A 1 367 ? -31.464 9.897   58.778  1.00 22.93 ? 387  PRO A CB    1 
ATOM   2738  C  CG    . PRO A 1 367 ? -32.292 9.562   59.980  1.00 22.89 ? 387  PRO A CG    1 
ATOM   2739  C  CD    . PRO A 1 367 ? -31.331 8.866   60.888  1.00 22.41 ? 387  PRO A CD    1 
ATOM   2740  N  N     . GLY A 1 368 ? -28.899 8.676   56.848  1.00 23.69 ? 388  GLY A N     1 
ATOM   2741  C  CA    . GLY A 1 368 ? -27.601 8.916   56.235  1.00 24.20 ? 388  GLY A CA    1 
ATOM   2742  C  C     . GLY A 1 368 ? -26.608 7.795   56.432  1.00 24.43 ? 388  GLY A C     1 
ATOM   2743  O  O     . GLY A 1 368 ? -25.579 7.770   55.753  1.00 25.43 ? 388  GLY A O     1 
ATOM   2744  N  N     . ILE A 1 369 ? -26.901 6.867   57.349  1.00 24.19 ? 389  ILE A N     1 
ATOM   2745  C  CA    . ILE A 1 369 ? -26.005 5.749   57.638  1.00 23.83 ? 389  ILE A CA    1 
ATOM   2746  C  C     . ILE A 1 369 ? -26.710 4.440   57.311  1.00 23.28 ? 389  ILE A C     1 
ATOM   2747  O  O     . ILE A 1 369 ? -26.317 3.750   56.374  1.00 23.69 ? 389  ILE A O     1 
ATOM   2748  C  CB    . ILE A 1 369 ? -25.514 5.765   59.112  1.00 23.85 ? 389  ILE A CB    1 
ATOM   2749  C  CG1   . ILE A 1 369 ? -24.715 7.039   59.399  1.00 25.04 ? 389  ILE A CG1   1 
ATOM   2750  C  CG2   . ILE A 1 369 ? -24.624 4.574   59.391  1.00 23.80 ? 389  ILE A CG2   1 
ATOM   2751  C  CD1   . ILE A 1 369 ? -24.304 7.208   60.863  1.00 24.90 ? 389  ILE A CD1   1 
ATOM   2752  N  N     . ASP A 1 370 ? -27.762 4.119   58.073  1.00 22.64 ? 390  ASP A N     1 
ATOM   2753  C  CA    . ASP A 1 370 ? -28.536 2.881   57.893  1.00 21.55 ? 390  ASP A CA    1 
ATOM   2754  C  C     . ASP A 1 370 ? -29.378 2.904   56.611  1.00 21.19 ? 390  ASP A C     1 
ATOM   2755  O  O     . ASP A 1 370 ? -29.558 1.873   55.962  1.00 19.84 ? 390  ASP A O     1 
ATOM   2756  C  CB    . ASP A 1 370 ? -29.447 2.640   59.099  1.00 21.37 ? 390  ASP A CB    1 
ATOM   2757  C  CG    . ASP A 1 370 ? -28.680 2.277   60.367  1.00 21.43 ? 390  ASP A CG    1 
ATOM   2758  O  OD1   . ASP A 1 370 ? -27.602 1.647   60.284  1.00 22.27 ? 390  ASP A OD1   1 
ATOM   2759  O  OD2   . ASP A 1 370 ? -29.165 2.603   61.471  1.00 19.39 ? 390  ASP A OD2   1 
ATOM   2760  N  N     . CYS A 1 371 ? -29.908 4.080   56.269  1.00 20.99 ? 391  CYS A N     1 
ATOM   2761  C  CA    . CYS A 1 371 ? -30.532 4.315   54.967  1.00 21.27 ? 391  CYS A CA    1 
ATOM   2762  C  C     . CYS A 1 371 ? -30.055 5.686   54.491  1.00 21.25 ? 391  CYS A C     1 
ATOM   2763  O  O     . CYS A 1 371 ? -29.556 6.467   55.294  1.00 21.31 ? 391  CYS A O     1 
ATOM   2764  C  CB    . CYS A 1 371 ? -32.074 4.277   55.052  1.00 21.25 ? 391  CYS A CB    1 
ATOM   2765  S  SG    . CYS A 1 371 ? -32.748 2.918   56.056  1.00 21.55 ? 391  CYS A SG    1 
ATOM   2766  N  N     . PRO A 1 372 ? -30.187 5.979   53.185  1.00 21.57 ? 392  PRO A N     1 
ATOM   2767  C  CA    . PRO A 1 372 ? -29.818 7.324   52.717  1.00 21.97 ? 392  PRO A CA    1 
ATOM   2768  C  C     . PRO A 1 372 ? -30.605 8.425   53.416  1.00 22.35 ? 392  PRO A C     1 
ATOM   2769  O  O     . PRO A 1 372 ? -31.736 8.192   53.860  1.00 22.33 ? 392  PRO A O     1 
ATOM   2770  C  CB    . PRO A 1 372 ? -30.167 7.312   51.222  1.00 21.89 ? 392  PRO A CB    1 
ATOM   2771  C  CG    . PRO A 1 372 ? -30.322 5.894   50.838  1.00 22.12 ? 392  PRO A CG    1 
ATOM   2772  C  CD    . PRO A 1 372 ? -30.563 5.076   52.084  1.00 21.60 ? 392  PRO A CD    1 
ATOM   2773  N  N     . GLU A 1 373 ? -30.008 9.619   53.488  1.00 22.74 ? 393  GLU A N     1 
ATOM   2774  C  CA    . GLU A 1 373 ? -30.659 10.784  54.087  1.00 23.00 ? 393  GLU A CA    1 
ATOM   2775  C  C     . GLU A 1 373 ? -31.967 11.091  53.385  1.00 22.07 ? 393  GLU A C     1 
ATOM   2776  O  O     . GLU A 1 373 ? -32.832 11.726  53.953  1.00 22.15 ? 393  GLU A O     1 
ATOM   2777  C  CB    . GLU A 1 373 ? -29.784 12.036  53.994  1.00 23.51 ? 393  GLU A CB    1 
ATOM   2778  C  CG    . GLU A 1 373 ? -28.487 11.971  54.732  1.00 26.10 ? 393  GLU A CG    1 
ATOM   2779  C  CD    . GLU A 1 373 ? -27.356 11.514  53.861  1.00 29.13 ? 393  GLU A CD    1 
ATOM   2780  O  OE1   . GLU A 1 373 ? -27.535 10.565  53.059  1.00 30.96 ? 393  GLU A OE1   1 
ATOM   2781  O  OE2   . GLU A 1 373 ? -26.274 12.112  53.981  1.00 33.90 ? 393  GLU A OE2   1 
ATOM   2782  N  N     . THR A 1 374 ? -32.077 10.654  52.139  1.00 21.48 ? 394  THR A N     1 
ATOM   2783  C  CA    . THR A 1 374 ? -33.259 10.866  51.318  1.00 20.93 ? 394  THR A CA    1 
ATOM   2784  C  C     . THR A 1 374 ? -34.372 9.809   51.500  1.00 20.58 ? 394  THR A C     1 
ATOM   2785  O  O     . THR A 1 374 ? -35.423 9.897   50.855  1.00 19.85 ? 394  THR A O     1 
ATOM   2786  C  CB    . THR A 1 374 ? -32.829 10.888  49.851  1.00 21.25 ? 394  THR A CB    1 
ATOM   2787  O  OG1   . THR A 1 374 ? -32.093 9.697   49.563  1.00 21.23 ? 394  THR A OG1   1 
ATOM   2788  C  CG2   . THR A 1 374 ? -31.916 12.122  49.558  1.00 20.81 ? 394  THR A CG2   1 
ATOM   2789  N  N     . ALA A 1 375 ? -34.158 8.823   52.372  1.00 19.96 ? 395  ALA A N     1 
ATOM   2790  C  CA    . ALA A 1 375 ? -35.153 7.754   52.564  1.00 19.59 ? 395  ALA A CA    1 
ATOM   2791  C  C     . ALA A 1 375 ? -36.407 8.226   53.288  1.00 19.27 ? 395  ALA A C     1 
ATOM   2792  O  O     . ALA A 1 375 ? -36.373 9.187   54.055  1.00 18.11 ? 395  ALA A O     1 
ATOM   2793  C  CB    . ALA A 1 375 ? -34.547 6.583   53.332  1.00 19.01 ? 395  ALA A CB    1 
ATOM   2794  N  N     . THR A 1 376 ? -37.509 7.515   53.042  1.00 19.18 ? 396  THR A N     1 
ATOM   2795  C  CA    . THR A 1 376 ? -38.699 7.644   53.854  1.00 18.68 ? 396  THR A CA    1 
ATOM   2796  C  C     . THR A 1 376 ? -38.527 6.676   55.011  1.00 19.55 ? 396  THR A C     1 
ATOM   2797  O  O     . THR A 1 376 ? -38.322 5.470   54.799  1.00 19.92 ? 396  THR A O     1 
ATOM   2798  C  CB    . THR A 1 376 ? -39.972 7.289   53.077  1.00 18.94 ? 396  THR A CB    1 
ATOM   2799  O  OG1   . THR A 1 376 ? -40.014 8.047   51.863  1.00 17.42 ? 396  THR A OG1   1 
ATOM   2800  C  CG2   . THR A 1 376 ? -41.235 7.566   53.938  1.00 17.26 ? 396  THR A CG2   1 
ATOM   2801  N  N     . PHE A 1 377 ? -38.591 7.214   56.226  1.00 19.47 ? 397  PHE A N     1 
ATOM   2802  C  CA    . PHE A 1 377 ? -38.418 6.446   57.447  1.00 19.48 ? 397  PHE A CA    1 
ATOM   2803  C  C     . PHE A 1 377 ? -39.781 6.266   58.092  1.00 19.51 ? 397  PHE A C     1 
ATOM   2804  O  O     . PHE A 1 377 ? -40.580 7.195   58.119  1.00 19.90 ? 397  PHE A O     1 
ATOM   2805  C  CB    . PHE A 1 377 ? -37.473 7.170   58.404  1.00 19.38 ? 397  PHE A CB    1 
ATOM   2806  C  CG    . PHE A 1 377 ? -36.052 7.249   57.911  1.00 19.81 ? 397  PHE A CG    1 
ATOM   2807  C  CD1   . PHE A 1 377 ? -35.633 8.313   57.139  1.00 19.55 ? 397  PHE A CD1   1 
ATOM   2808  C  CD2   . PHE A 1 377 ? -35.134 6.254   58.227  1.00 20.32 ? 397  PHE A CD2   1 
ATOM   2809  C  CE1   . PHE A 1 377 ? -34.335 8.392   56.685  1.00 20.08 ? 397  PHE A CE1   1 
ATOM   2810  C  CE2   . PHE A 1 377 ? -33.821 6.326   57.775  1.00 20.45 ? 397  PHE A CE2   1 
ATOM   2811  C  CZ    . PHE A 1 377 ? -33.423 7.395   56.998  1.00 20.18 ? 397  PHE A CZ    1 
ATOM   2812  N  N     . LEU A 1 378 ? -40.042 5.070   58.602  1.00 19.29 ? 398  LEU A N     1 
ATOM   2813  C  CA    . LEU A 1 378 ? -41.352 4.711   59.096  1.00 19.86 ? 398  LEU A CA    1 
ATOM   2814  C  C     . LEU A 1 378 ? -41.273 4.172   60.509  1.00 20.11 ? 398  LEU A C     1 
ATOM   2815  O  O     . LEU A 1 378 ? -40.404 3.366   60.829  1.00 20.03 ? 398  LEU A O     1 
ATOM   2816  C  CB    . LEU A 1 378 ? -41.971 3.647   58.201  1.00 19.77 ? 398  LEU A CB    1 
ATOM   2817  C  CG    . LEU A 1 378 ? -42.290 4.080   56.777  1.00 20.32 ? 398  LEU A CG    1 
ATOM   2818  C  CD1   . LEU A 1 378 ? -42.762 2.883   55.992  1.00 19.16 ? 398  LEU A CD1   1 
ATOM   2819  C  CD2   . LEU A 1 378 ? -43.339 5.206   56.772  1.00 19.48 ? 398  LEU A CD2   1 
ATOM   2820  N  N     . ASP A 1 379 ? -42.199 4.623   61.343  1.00 20.82 ? 399  ASP A N     1 
ATOM   2821  C  CA    . ASP A 1 379 ? -42.348 4.110   62.700  1.00 21.47 ? 399  ASP A CA    1 
ATOM   2822  C  C     . ASP A 1 379 ? -43.173 2.843   62.716  1.00 21.32 ? 399  ASP A C     1 
ATOM   2823  O  O     . ASP A 1 379 ? -43.929 2.568   61.780  1.00 21.23 ? 399  ASP A O     1 
ATOM   2824  C  CB    . ASP A 1 379 ? -43.051 5.141   63.578  1.00 21.68 ? 399  ASP A CB    1 
ATOM   2825  C  CG    . ASP A 1 379 ? -42.243 6.394   63.755  1.00 23.30 ? 399  ASP A CG    1 
ATOM   2826  O  OD1   . ASP A 1 379 ? -41.118 6.483   63.212  1.00 24.18 ? 399  ASP A OD1   1 
ATOM   2827  O  OD2   . ASP A 1 379 ? -42.736 7.290   64.448  1.00 27.42 ? 399  ASP A OD2   1 
ATOM   2828  N  N     . THR A 1 380 ? -43.032 2.071   63.790  1.00 21.30 ? 400  THR A N     1 
ATOM   2829  C  CA    . THR A 1 380 ? -44.000 1.033   64.071  1.00 21.54 ? 400  THR A CA    1 
ATOM   2830  C  C     . THR A 1 380 ? -44.243 0.880   65.563  1.00 21.36 ? 400  THR A C     1 
ATOM   2831  O  O     . THR A 1 380 ? -43.641 1.571   66.379  1.00 21.22 ? 400  THR A O     1 
ATOM   2832  C  CB    . THR A 1 380 ? -43.619 -0.326  63.412  1.00 21.76 ? 400  THR A CB    1 
ATOM   2833  O  OG1   . THR A 1 380 ? -44.808 -1.109  63.240  1.00 21.13 ? 400  THR A OG1   1 
ATOM   2834  C  CG2   . THR A 1 380 ? -42.608 -1.109  64.252  1.00 21.28 ? 400  THR A CG2   1 
ATOM   2835  N  N     . PHE A 1 381 ? -45.177 0.000   65.892  1.00 21.65 ? 401  PHE A N     1 
ATOM   2836  C  CA    . PHE A 1 381 ? -45.465 -0.375  67.263  1.00 22.04 ? 401  PHE A CA    1 
ATOM   2837  C  C     . PHE A 1 381 ? -45.304 -1.883  67.409  1.00 22.42 ? 401  PHE A C     1 
ATOM   2838  O  O     . PHE A 1 381 ? -45.705 -2.642  66.521  1.00 22.24 ? 401  PHE A O     1 
ATOM   2839  C  CB    . PHE A 1 381 ? -46.889 0.037   67.636  1.00 22.20 ? 401  PHE A CB    1 
ATOM   2840  C  CG    . PHE A 1 381 ? -47.015 1.475   68.096  1.00 22.46 ? 401  PHE A CG    1 
ATOM   2841  C  CD1   . PHE A 1 381 ? -47.225 2.496   67.183  1.00 22.63 ? 401  PHE A CD1   1 
ATOM   2842  C  CD2   . PHE A 1 381 ? -46.939 1.791   69.448  1.00 22.85 ? 401  PHE A CD2   1 
ATOM   2843  C  CE1   . PHE A 1 381 ? -47.358 3.816   67.609  1.00 24.00 ? 401  PHE A CE1   1 
ATOM   2844  C  CE2   . PHE A 1 381 ? -47.072 3.107   69.887  1.00 23.22 ? 401  PHE A CE2   1 
ATOM   2845  C  CZ    . PHE A 1 381 ? -47.281 4.119   68.967  1.00 23.28 ? 401  PHE A CZ    1 
ATOM   2846  N  N     . HIS A 1 382 ? -44.693 -2.303  68.516  1.00 22.66 ? 402  HIS A N     1 
ATOM   2847  C  CA    . HIS A 1 382 ? -44.592 -3.718  68.877  1.00 22.95 ? 402  HIS A CA    1 
ATOM   2848  C  C     . HIS A 1 382 ? -45.159 -3.959  70.268  1.00 22.86 ? 402  HIS A C     1 
ATOM   2849  O  O     . HIS A 1 382 ? -44.989 -3.142  71.158  1.00 22.49 ? 402  HIS A O     1 
ATOM   2850  C  CB    . HIS A 1 382 ? -43.127 -4.174  68.891  1.00 22.85 ? 402  HIS A CB    1 
ATOM   2851  C  CG    . HIS A 1 382 ? -42.488 -4.208  67.541  1.00 24.35 ? 402  HIS A CG    1 
ATOM   2852  N  ND1   . HIS A 1 382 ? -42.989 -4.960  66.499  1.00 23.95 ? 402  HIS A ND1   1 
ATOM   2853  C  CD2   . HIS A 1 382 ? -41.382 -3.589  67.064  1.00 25.19 ? 402  HIS A CD2   1 
ATOM   2854  C  CE1   . HIS A 1 382 ? -42.227 -4.789  65.434  1.00 25.13 ? 402  HIS A CE1   1 
ATOM   2855  N  NE2   . HIS A 1 382 ? -41.238 -3.970  65.753  1.00 25.03 ? 402  HIS A NE2   1 
ATOM   2856  N  N     . TYR A 1 383 ? -45.818 -5.096  70.448  1.00 23.55 ? 403  TYR A N     1 
ATOM   2857  C  CA    . TYR A 1 383 ? -46.154 -5.592  71.772  1.00 23.89 ? 403  TYR A CA    1 
ATOM   2858  C  C     . TYR A 1 383 ? -45.523 -6.971  71.923  1.00 24.01 ? 403  TYR A C     1 
ATOM   2859  O  O     . TYR A 1 383 ? -46.074 -7.964  71.464  1.00 23.32 ? 403  TYR A O     1 
ATOM   2860  C  CB    . TYR A 1 383 ? -47.665 -5.651  71.958  1.00 24.23 ? 403  TYR A CB    1 
ATOM   2861  C  CG    . TYR A 1 383 ? -48.082 -6.008  73.365  1.00 25.98 ? 403  TYR A CG    1 
ATOM   2862  C  CD1   . TYR A 1 383 ? -48.437 -5.025  74.283  1.00 28.43 ? 403  TYR A CD1   1 
ATOM   2863  C  CD2   . TYR A 1 383 ? -48.140 -7.330  73.769  1.00 27.98 ? 403  TYR A CD2   1 
ATOM   2864  C  CE1   . TYR A 1 383 ? -48.830 -5.365  75.582  1.00 30.09 ? 403  TYR A CE1   1 
ATOM   2865  C  CE2   . TYR A 1 383 ? -48.521 -7.676  75.044  1.00 30.11 ? 403  TYR A CE2   1 
ATOM   2866  C  CZ    . TYR A 1 383 ? -48.867 -6.698  75.948  1.00 29.97 ? 403  TYR A CZ    1 
ATOM   2867  O  OH    . TYR A 1 383 ? -49.247 -7.082  77.208  1.00 32.38 ? 403  TYR A OH    1 
ATOM   2868  N  N     . TYR A 1 384 ? -44.339 -6.996  72.532  1.00 24.56 ? 404  TYR A N     1 
ATOM   2869  C  CA    . TYR A 1 384 ? -43.562 -8.212  72.741  1.00 25.15 ? 404  TYR A CA    1 
ATOM   2870  C  C     . TYR A 1 384 ? -42.856 -8.077  74.096  1.00 25.30 ? 404  TYR A C     1 
ATOM   2871  O  O     . TYR A 1 384 ? -41.976 -7.235  74.243  1.00 24.83 ? 404  TYR A O     1 
ATOM   2872  C  CB    . TYR A 1 384 ? -42.534 -8.401  71.608  1.00 25.47 ? 404  TYR A CB    1 
ATOM   2873  C  CG    . TYR A 1 384 ? -41.662 -9.634  71.776  1.00 27.10 ? 404  TYR A CG    1 
ATOM   2874  C  CD1   . TYR A 1 384 ? -41.886 -10.786 71.025  1.00 28.37 ? 404  TYR A CD1   1 
ATOM   2875  C  CD2   . TYR A 1 384 ? -40.626 -9.656  72.712  1.00 28.75 ? 404  TYR A CD2   1 
ATOM   2876  C  CE1   . TYR A 1 384 ? -41.090 -11.929 71.202  1.00 29.20 ? 404  TYR A CE1   1 
ATOM   2877  C  CE2   . TYR A 1 384 ? -39.833 -10.787 72.899  1.00 28.98 ? 404  TYR A CE2   1 
ATOM   2878  C  CZ    . TYR A 1 384 ? -40.059 -11.917 72.142  1.00 30.24 ? 404  TYR A CZ    1 
ATOM   2879  O  OH    . TYR A 1 384 ? -39.254 -13.032 72.341  1.00 30.86 ? 404  TYR A OH    1 
ATOM   2880  N  N     . ASP A 1 385 ? -43.240 -8.899  75.075  1.00 25.33 ? 405  ASP A N     1 
ATOM   2881  C  CA    . ASP A 1 385 ? -42.693 -8.810  76.442  1.00 25.69 ? 405  ASP A CA    1 
ATOM   2882  C  C     . ASP A 1 385 ? -42.789 -7.382  77.017  1.00 26.04 ? 405  ASP A C     1 
ATOM   2883  O  O     . ASP A 1 385 ? -41.807 -6.815  77.474  1.00 26.47 ? 405  ASP A O     1 
ATOM   2884  C  CB    . ASP A 1 385 ? -41.240 -9.291  76.478  1.00 25.88 ? 405  ASP A CB    1 
ATOM   2885  C  CG    . ASP A 1 385 ? -40.713 -9.473  77.895  1.00 25.60 ? 405  ASP A CG    1 
ATOM   2886  O  OD1   . ASP A 1 385 ? -41.538 -9.630  78.819  1.00 26.06 ? 405  ASP A OD1   1 
ATOM   2887  O  OD2   . ASP A 1 385 ? -39.476 -9.475  78.080  1.00 24.77 ? 405  ASP A OD2   1 
ATOM   2888  N  N     . ALA A 1 386 ? -43.979 -6.808  76.980  1.00 26.13 ? 406  ALA A N     1 
ATOM   2889  C  CA    . ALA A 1 386 ? -44.159 -5.413  77.367  1.00 26.64 ? 406  ALA A CA    1 
ATOM   2890  C  C     . ALA A 1 386 ? -45.468 -5.243  78.121  1.00 26.71 ? 406  ALA A C     1 
ATOM   2891  O  O     . ALA A 1 386 ? -46.367 -6.069  78.009  1.00 26.59 ? 406  ALA A O     1 
ATOM   2892  C  CB    . ALA A 1 386 ? -44.141 -4.511  76.120  1.00 26.61 ? 406  ALA A CB    1 
ATOM   2893  N  N     . ASP A 1 387 ? -45.564 -4.164  78.886  1.00 27.26 ? 407  ASP A N     1 
ATOM   2894  C  CA    . ASP A 1 387 ? -46.789 -3.833  79.625  1.00 27.57 ? 407  ASP A CA    1 
ATOM   2895  C  C     . ASP A 1 387 ? -47.782 -3.071  78.761  1.00 27.25 ? 407  ASP A C     1 
ATOM   2896  O  O     . ASP A 1 387 ? -48.990 -3.134  78.998  1.00 27.40 ? 407  ASP A O     1 
ATOM   2897  C  CB    . ASP A 1 387 ? -46.450 -2.998  80.858  1.00 27.97 ? 407  ASP A CB    1 
ATOM   2898  C  CG    . ASP A 1 387 ? -45.604 -3.753  81.858  1.00 29.50 ? 407  ASP A CG    1 
ATOM   2899  O  OD1   . ASP A 1 387 ? -45.651 -5.002  81.855  1.00 30.22 ? 407  ASP A OD1   1 
ATOM   2900  O  OD2   . ASP A 1 387 ? -44.899 -3.096  82.659  1.00 32.00 ? 407  ASP A OD2   1 
ATOM   2901  N  N     . ASP A 1 388 ? -47.262 -2.320  77.788  1.00 26.69 ? 408  ASP A N     1 
ATOM   2902  C  CA    . ASP A 1 388 ? -48.077 -1.558  76.848  1.00 26.18 ? 408  ASP A CA    1 
ATOM   2903  C  C     . ASP A 1 388 ? -47.425 -1.622  75.473  1.00 25.42 ? 408  ASP A C     1 
ATOM   2904  O  O     . ASP A 1 388 ? -46.229 -1.898  75.384  1.00 24.82 ? 408  ASP A O     1 
ATOM   2905  C  CB    . ASP A 1 388 ? -48.141 -0.088  77.274  1.00 26.25 ? 408  ASP A CB    1 
ATOM   2906  C  CG    . ASP A 1 388 ? -48.730 0.095   78.651  1.00 27.25 ? 408  ASP A CG    1 
ATOM   2907  O  OD1   . ASP A 1 388 ? -49.973 0.086   78.768  1.00 28.16 ? 408  ASP A OD1   1 
ATOM   2908  O  OD2   . ASP A 1 388 ? -47.947 0.237   79.611  1.00 28.63 ? 408  ASP A OD2   1 
ATOM   2909  N  N     . PRO A 1 389 ? -48.194 -1.336  74.407  1.00 24.56 ? 409  PRO A N     1 
ATOM   2910  C  CA    . PRO A 1 389 ? -47.578 -1.218  73.091  1.00 24.46 ? 409  PRO A CA    1 
ATOM   2911  C  C     . PRO A 1 389 ? -46.468 -0.159  73.099  1.00 24.40 ? 409  PRO A C     1 
ATOM   2912  O  O     . PRO A 1 389 ? -46.593 0.864   73.791  1.00 24.41 ? 409  PRO A O     1 
ATOM   2913  C  CB    . PRO A 1 389 ? -48.736 -0.789  72.193  1.00 24.52 ? 409  PRO A CB    1 
ATOM   2914  C  CG    . PRO A 1 389 ? -49.983 -1.139  72.956  1.00 24.44 ? 409  PRO A CG    1 
ATOM   2915  C  CD    . PRO A 1 389 ? -49.628 -0.994  74.378  1.00 24.44 ? 409  PRO A CD    1 
ATOM   2916  N  N     . VAL A 1 390 ? -45.387 -0.434  72.375  1.00 23.68 ? 410  VAL A N     1 
ATOM   2917  C  CA    . VAL A 1 390 ? -44.182 0.390   72.406  1.00 23.58 ? 410  VAL A CA    1 
ATOM   2918  C  C     . VAL A 1 390 ? -43.895 0.959   71.024  1.00 23.37 ? 410  VAL A C     1 
ATOM   2919  O  O     . VAL A 1 390 ? -43.908 0.223   70.035  1.00 23.18 ? 410  VAL A O     1 
ATOM   2920  C  CB    . VAL A 1 390 ? -42.966 -0.436  72.848  1.00 23.69 ? 410  VAL A CB    1 
ATOM   2921  C  CG1   . VAL A 1 390 ? -41.688 0.426   72.844  1.00 23.01 ? 410  VAL A CG1   1 
ATOM   2922  C  CG2   . VAL A 1 390 ? -43.217 -1.058  74.225  1.00 23.04 ? 410  VAL A CG2   1 
ATOM   2923  N  N     . HIS A 1 391 ? -43.640 2.265   70.970  1.00 22.96 ? 411  HIS A N     1 
ATOM   2924  C  CA    . HIS A 1 391 ? -43.332 2.966   69.727  1.00 22.80 ? 411  HIS A CA    1 
ATOM   2925  C  C     . HIS A 1 391 ? -41.862 2.772   69.361  1.00 22.31 ? 411  HIS A C     1 
ATOM   2926  O  O     . HIS A 1 391 ? -40.974 3.005   70.181  1.00 22.22 ? 411  HIS A O     1 
ATOM   2927  C  CB    . HIS A 1 391 ? -43.643 4.458   69.876  1.00 22.97 ? 411  HIS A CB    1 
ATOM   2928  C  CG    . HIS A 1 391 ? -43.307 5.287   68.671  1.00 23.26 ? 411  HIS A CG    1 
ATOM   2929  N  ND1   . HIS A 1 391 ? -42.157 6.044   68.587  1.00 24.76 ? 411  HIS A ND1   1 
ATOM   2930  C  CD2   . HIS A 1 391 ? -43.981 5.498   67.515  1.00 23.15 ? 411  HIS A CD2   1 
ATOM   2931  C  CE1   . HIS A 1 391 ? -42.136 6.680   67.428  1.00 24.64 ? 411  HIS A CE1   1 
ATOM   2932  N  NE2   . HIS A 1 391 ? -43.233 6.369   66.760  1.00 23.65 ? 411  HIS A NE2   1 
ATOM   2933  N  N     . TYR A 1 392 ? -41.627 2.330   68.129  1.00 21.98 ? 412  TYR A N     1 
ATOM   2934  C  CA    . TYR A 1 392 ? -40.286 2.092   67.602  1.00 21.79 ? 412  TYR A CA    1 
ATOM   2935  C  C     . TYR A 1 392 ? -40.061 3.092   66.476  1.00 21.44 ? 412  TYR A C     1 
ATOM   2936  O  O     . TYR A 1 392 ? -40.598 2.923   65.386  1.00 21.22 ? 412  TYR A O     1 
ATOM   2937  C  CB    . TYR A 1 392 ? -40.155 0.648   67.083  1.00 21.84 ? 412  TYR A CB    1 
ATOM   2938  C  CG    . TYR A 1 392 ? -39.879 -0.365  68.171  1.00 22.39 ? 412  TYR A CG    1 
ATOM   2939  C  CD1   . TYR A 1 392 ? -40.869 -0.707  69.094  1.00 23.55 ? 412  TYR A CD1   1 
ATOM   2940  C  CD2   . TYR A 1 392 ? -38.629 -0.971  68.292  1.00 23.88 ? 412  TYR A CD2   1 
ATOM   2941  C  CE1   . TYR A 1 392 ? -40.627 -1.628  70.097  1.00 22.61 ? 412  TYR A CE1   1 
ATOM   2942  C  CE2   . TYR A 1 392 ? -38.371 -1.888  69.294  1.00 23.80 ? 412  TYR A CE2   1 
ATOM   2943  C  CZ    . TYR A 1 392 ? -39.380 -2.211  70.197  1.00 23.61 ? 412  TYR A CZ    1 
ATOM   2944  O  OH    . TYR A 1 392 ? -39.136 -3.122  71.192  1.00 24.51 ? 412  TYR A OH    1 
ATOM   2945  N  N     . PRO A 1 393 ? -39.283 4.150   66.739  1.00 21.24 ? 413  PRO A N     1 
ATOM   2946  C  CA    . PRO A 1 393 ? -39.052 5.160   65.708  1.00 21.17 ? 413  PRO A CA    1 
ATOM   2947  C  C     . PRO A 1 393 ? -38.154 4.643   64.586  1.00 20.61 ? 413  PRO A C     1 
ATOM   2948  O  O     . PRO A 1 393 ? -37.163 3.977   64.854  1.00 20.35 ? 413  PRO A O     1 
ATOM   2949  C  CB    . PRO A 1 393 ? -38.343 6.296   66.462  1.00 20.88 ? 413  PRO A CB    1 
ATOM   2950  C  CG    . PRO A 1 393 ? -38.213 5.871   67.842  1.00 21.69 ? 413  PRO A CG    1 
ATOM   2951  C  CD    . PRO A 1 393 ? -38.509 4.428   67.954  1.00 21.17 ? 413  PRO A CD    1 
ATOM   2952  N  N     . ARG A 1 394 ? -38.510 4.959   63.349  1.00 20.46 ? 414  ARG A N     1 
ATOM   2953  C  CA    . ARG A 1 394 ? -37.693 4.614   62.189  1.00 20.50 ? 414  ARG A CA    1 
ATOM   2954  C  C     . ARG A 1 394 ? -37.288 3.153   62.215  1.00 19.98 ? 414  ARG A C     1 
ATOM   2955  O  O     . ARG A 1 394 ? -36.108 2.823   62.093  1.00 19.32 ? 414  ARG A O     1 
ATOM   2956  C  CB    . ARG A 1 394 ? -36.446 5.483   62.137  1.00 20.57 ? 414  ARG A CB    1 
ATOM   2957  C  CG    . ARG A 1 394 ? -36.712 6.973   62.154  1.00 21.99 ? 414  ARG A CG    1 
ATOM   2958  C  CD    . ARG A 1 394 ? -35.377 7.644   62.139  1.00 23.94 ? 414  ARG A CD    1 
ATOM   2959  N  NE    . ARG A 1 394 ? -35.423 9.097   62.051  1.00 24.61 ? 414  ARG A NE    1 
ATOM   2960  C  CZ    . ARG A 1 394 ? -34.539 9.904   62.628  1.00 24.69 ? 414  ARG A CZ    1 
ATOM   2961  N  NH1   . ARG A 1 394 ? -33.562 9.410   63.391  1.00 24.29 ? 414  ARG A NH1   1 
ATOM   2962  N  NH2   . ARG A 1 394 ? -34.647 11.213  62.472  1.00 25.82 ? 414  ARG A NH2   1 
ATOM   2963  N  N     . ALA A 1 395 ? -38.283 2.297   62.410  1.00 19.70 ? 415  ALA A N     1 
ATOM   2964  C  CA    . ALA A 1 395 ? -38.101 0.858   62.395  1.00 19.93 ? 415  ALA A CA    1 
ATOM   2965  C  C     . ALA A 1 395 ? -37.821 0.341   60.987  1.00 19.92 ? 415  ALA A C     1 
ATOM   2966  O  O     . ALA A 1 395 ? -37.091 -0.631  60.836  1.00 20.44 ? 415  ALA A O     1 
ATOM   2967  C  CB    . ALA A 1 395 ? -39.340 0.170   62.973  1.00 20.19 ? 415  ALA A CB    1 
ATOM   2968  N  N     . LEU A 1 396 ? -38.436 0.969   59.979  1.00 19.86 ? 416  LEU A N     1 
ATOM   2969  C  CA    . LEU A 1 396 ? -38.228 0.625   58.566  1.00 19.92 ? 416  LEU A CA    1 
ATOM   2970  C  C     . LEU A 1 396 ? -37.868 1.862   57.738  1.00 19.79 ? 416  LEU A C     1 
ATOM   2971  O  O     . LEU A 1 396 ? -38.154 2.999   58.128  1.00 19.38 ? 416  LEU A O     1 
ATOM   2972  C  CB    . LEU A 1 396 ? -39.498 0.044   57.933  1.00 20.21 ? 416  LEU A CB    1 
ATOM   2973  C  CG    . LEU A 1 396 ? -40.324 -1.057  58.574  1.00 20.95 ? 416  LEU A CG    1 
ATOM   2974  C  CD1   . LEU A 1 396 ? -41.373 -0.465  59.534  1.00 19.94 ? 416  LEU A CD1   1 
ATOM   2975  C  CD2   . LEU A 1 396 ? -41.013 -1.879  57.469  1.00 21.48 ? 416  LEU A CD2   1 
ATOM   2976  N  N     . CYS A 1 397 ? -37.270 1.636   56.574  1.00 19.56 ? 417  CYS A N     1 
ATOM   2977  C  CA    . CYS A 1 397 ? -37.127 2.696   55.592  1.00 19.43 ? 417  CYS A CA    1 
ATOM   2978  C  C     . CYS A 1 397 ? -37.384 2.177   54.184  1.00 19.37 ? 417  CYS A C     1 
ATOM   2979  O  O     . CYS A 1 397 ? -37.208 0.985   53.895  1.00 19.14 ? 417  CYS A O     1 
ATOM   2980  C  CB    . CYS A 1 397 ? -35.746 3.344   55.679  1.00 19.76 ? 417  CYS A CB    1 
ATOM   2981  S  SG    . CYS A 1 397 ? -34.443 2.292   55.098  1.00 20.50 ? 417  CYS A SG    1 
ATOM   2982  N  N     . LEU A 1 398 ? -37.801 3.096   53.316  1.00 19.11 ? 418  LEU A N     1 
ATOM   2983  C  CA    . LEU A 1 398 ? -38.074 2.804   51.924  1.00 18.64 ? 418  LEU A CA    1 
ATOM   2984  C  C     . LEU A 1 398 ? -37.406 3.930   51.153  1.00 18.59 ? 418  LEU A C     1 
ATOM   2985  O  O     . LEU A 1 398 ? -37.580 5.097   51.494  1.00 17.77 ? 418  LEU A O     1 
ATOM   2986  C  CB    . LEU A 1 398 ? -39.589 2.764   51.677  1.00 18.71 ? 418  LEU A CB    1 
ATOM   2987  C  CG    . LEU A 1 398 ? -40.104 2.415   50.286  1.00 18.56 ? 418  LEU A CG    1 
ATOM   2988  C  CD1   . LEU A 1 398 ? -39.673 1.020   49.926  1.00 17.56 ? 418  LEU A CD1   1 
ATOM   2989  C  CD2   . LEU A 1 398 ? -41.635 2.543   50.217  1.00 18.69 ? 418  LEU A CD2   1 
ATOM   2990  N  N     . PHE A 1 399 ? -36.614 3.573   50.143  1.00 18.34 ? 419  PHE A N     1 
ATOM   2991  C  CA    . PHE A 1 399 ? -35.855 4.552   49.388  1.00 18.35 ? 419  PHE A CA    1 
ATOM   2992  C  C     . PHE A 1 399 ? -35.450 4.064   48.005  1.00 18.90 ? 419  PHE A C     1 
ATOM   2993  O  O     . PHE A 1 399 ? -35.270 2.861   47.782  1.00 18.83 ? 419  PHE A O     1 
ATOM   2994  C  CB    . PHE A 1 399 ? -34.609 4.974   50.173  1.00 18.41 ? 419  PHE A CB    1 
ATOM   2995  C  CG    . PHE A 1 399 ? -33.619 3.862   50.440  1.00 18.01 ? 419  PHE A CG    1 
ATOM   2996  C  CD1   . PHE A 1 399 ? -32.540 3.652   49.587  1.00 19.51 ? 419  PHE A CD1   1 
ATOM   2997  C  CD2   . PHE A 1 399 ? -33.715 3.092   51.574  1.00 18.35 ? 419  PHE A CD2   1 
ATOM   2998  C  CE1   . PHE A 1 399 ? -31.602 2.661   49.840  1.00 19.11 ? 419  PHE A CE1   1 
ATOM   2999  C  CE2   . PHE A 1 399 ? -32.787 2.080   51.835  1.00 19.41 ? 419  PHE A CE2   1 
ATOM   3000  C  CZ    . PHE A 1 399 ? -31.724 1.873   50.969  1.00 19.78 ? 419  PHE A CZ    1 
ATOM   3001  N  N     . GLU A 1 400 ? -35.320 5.007   47.077  1.00 19.28 ? 420  GLU A N     1 
ATOM   3002  C  CA    . GLU A 1 400 ? -34.779 4.723   45.764  1.00 19.66 ? 420  GLU A CA    1 
ATOM   3003  C  C     . GLU A 1 400 ? -33.325 5.130   45.784  1.00 20.43 ? 420  GLU A C     1 
ATOM   3004  O  O     . GLU A 1 400 ? -32.981 6.160   46.340  1.00 21.07 ? 420  GLU A O     1 
ATOM   3005  C  CB    . GLU A 1 400 ? -35.505 5.490   44.669  1.00 19.37 ? 420  GLU A CB    1 
ATOM   3006  C  CG    . GLU A 1 400 ? -35.191 4.926   43.283  1.00 20.00 ? 420  GLU A CG    1 
ATOM   3007  C  CD    . GLU A 1 400 ? -35.904 5.631   42.147  1.00 19.70 ? 420  GLU A CD    1 
ATOM   3008  O  OE1   . GLU A 1 400 ? -36.362 6.781   42.343  1.00 20.00 ? 420  GLU A OE1   1 
ATOM   3009  O  OE2   . GLU A 1 400 ? -35.993 5.028   41.047  1.00 19.61 ? 420  GLU A OE2   1 
ATOM   3010  N  N     . MET A 1 401 ? -32.468 4.308   45.202  1.00 21.06 ? 421  MET A N     1 
ATOM   3011  C  CA    . MET A 1 401 ? -31.063 4.642   45.129  1.00 21.60 ? 421  MET A CA    1 
ATOM   3012  C  C     . MET A 1 401 ? -30.474 4.242   43.800  1.00 21.11 ? 421  MET A C     1 
ATOM   3013  O  O     . MET A 1 401 ? -30.853 3.227   43.224  1.00 21.07 ? 421  MET A O     1 
ATOM   3014  C  CB    . MET A 1 401 ? -30.272 3.977   46.249  1.00 22.22 ? 421  MET A CB    1 
ATOM   3015  C  CG    . MET A 1 401 ? -30.225 2.475   46.228  1.00 23.57 ? 421  MET A CG    1 
ATOM   3016  S  SD    . MET A 1 401 ? -28.869 1.907   47.279  1.00 28.73 ? 421  MET A SD    1 
ATOM   3017  C  CE    . MET A 1 401 ? -27.496 1.817   46.115  1.00 28.25 ? 421  MET A CE    1 
ATOM   3018  N  N     . PRO A 1 402 ? -29.531 5.043   43.309  1.00 21.00 ? 422  PRO A N     1 
ATOM   3019  C  CA    . PRO A 1 402 ? -28.821 4.629   42.120  1.00 20.42 ? 422  PRO A CA    1 
ATOM   3020  C  C     . PRO A 1 402 ? -27.931 3.445   42.446  1.00 19.98 ? 422  PRO A C     1 
ATOM   3021  O  O     . PRO A 1 402 ? -27.262 3.441   43.474  1.00 18.99 ? 422  PRO A O     1 
ATOM   3022  C  CB    . PRO A 1 402 ? -27.981 5.848   41.755  1.00 20.38 ? 422  PRO A CB    1 
ATOM   3023  C  CG    . PRO A 1 402 ? -28.496 6.951   42.565  1.00 21.42 ? 422  PRO A CG    1 
ATOM   3024  C  CD    . PRO A 1 402 ? -29.110 6.370   43.778  1.00 20.72 ? 422  PRO A CD    1 
ATOM   3025  N  N     . THR A 1 403 ? -27.955 2.439   41.583  1.00 19.98 ? 423  THR A N     1 
ATOM   3026  C  CA    . THR A 1 403 ? -27.132 1.251   41.767  1.00 20.00 ? 423  THR A CA    1 
ATOM   3027  C  C     . THR A 1 403 ? -25.678 1.503   41.350  1.00 20.56 ? 423  THR A C     1 
ATOM   3028  O  O     . THR A 1 403 ? -24.804 0.729   41.675  1.00 21.65 ? 423  THR A O     1 
ATOM   3029  C  CB    . THR A 1 403 ? -27.666 0.114   40.917  1.00 19.68 ? 423  THR A CB    1 
ATOM   3030  O  OG1   . THR A 1 403 ? -27.632 0.518   39.546  1.00 19.20 ? 423  THR A OG1   1 
ATOM   3031  C  CG2   . THR A 1 403 ? -29.111 -0.245  41.320  1.00 18.39 ? 423  THR A CG2   1 
ATOM   3032  N  N     . GLY A 1 404 ? -25.437 2.571   40.600  1.00 21.33 ? 424  GLY A N     1 
ATOM   3033  C  CA    . GLY A 1 404 ? -24.124 2.857   40.039  1.00 21.52 ? 424  GLY A CA    1 
ATOM   3034  C  C     . GLY A 1 404 ? -23.801 2.142   38.732  1.00 21.31 ? 424  GLY A C     1 
ATOM   3035  O  O     . GLY A 1 404 ? -22.746 2.396   38.137  1.00 21.96 ? 424  GLY A O     1 
ATOM   3036  N  N     . VAL A 1 405 ? -24.677 1.246   38.283  1.00 20.64 ? 425  VAL A N     1 
ATOM   3037  C  CA    . VAL A 1 405 ? -24.481 0.544   37.013  1.00 20.16 ? 425  VAL A CA    1 
ATOM   3038  C  C     . VAL A 1 405 ? -25.772 0.611   36.190  1.00 19.90 ? 425  VAL A C     1 
ATOM   3039  O  O     . VAL A 1 405 ? -26.866 0.391   36.732  1.00 19.90 ? 425  VAL A O     1 
ATOM   3040  C  CB    . VAL A 1 405 ? -24.055 -0.930  37.241  1.00 20.50 ? 425  VAL A CB    1 
ATOM   3041  C  CG1   . VAL A 1 405 ? -25.159 -1.723  37.930  1.00 19.91 ? 425  VAL A CG1   1 
ATOM   3042  C  CG2   . VAL A 1 405 ? -23.656 -1.591  35.920  1.00 19.53 ? 425  VAL A CG2   1 
ATOM   3043  N  N     . PRO A 1 406 ? -25.662 0.932   34.885  1.00 19.16 ? 426  PRO A N     1 
ATOM   3044  C  CA    . PRO A 1 406 ? -26.899 1.127   34.123  1.00 18.75 ? 426  PRO A CA    1 
ATOM   3045  C  C     . PRO A 1 406 ? -27.719 -0.155  34.032  1.00 18.22 ? 426  PRO A C     1 
ATOM   3046  O  O     . PRO A 1 406 ? -27.156 -1.239  34.068  1.00 17.83 ? 426  PRO A O     1 
ATOM   3047  C  CB    . PRO A 1 406 ? -26.403 1.584   32.744  1.00 18.76 ? 426  PRO A CB    1 
ATOM   3048  C  CG    . PRO A 1 406 ? -24.968 1.165   32.681  1.00 18.64 ? 426  PRO A CG    1 
ATOM   3049  C  CD    . PRO A 1 406 ? -24.459 1.169   34.066  1.00 18.83 ? 426  PRO A CD    1 
ATOM   3050  N  N     . LEU A 1 407 ? -29.046 -0.041  33.959  1.00 18.32 ? 427  LEU A N     1 
ATOM   3051  C  CA    . LEU A 1 407 ? -29.893 -1.237  33.836  1.00 17.99 ? 427  LEU A CA    1 
ATOM   3052  C  C     . LEU A 1 407 ? -29.601 -1.912  32.496  1.00 18.13 ? 427  LEU A C     1 
ATOM   3053  O  O     . LEU A 1 407 ? -29.507 -3.137  32.405  1.00 17.90 ? 427  LEU A O     1 
ATOM   3054  C  CB    . LEU A 1 407 ? -31.377 -0.890  33.985  1.00 18.02 ? 427  LEU A CB    1 
ATOM   3055  C  CG    . LEU A 1 407 ? -32.331 -2.090  34.108  1.00 18.23 ? 427  LEU A CG    1 
ATOM   3056  C  CD1   . LEU A 1 407 ? -33.569 -1.742  34.934  1.00 19.91 ? 427  LEU A CD1   1 
ATOM   3057  C  CD2   . LEU A 1 407 ? -32.741 -2.596  32.731  1.00 19.19 ? 427  LEU A CD2   1 
ATOM   3058  N  N     . ARG A 1 408 ? -29.443 -1.086  31.467  1.00 18.13 ? 428  ARG A N     1 
ATOM   3059  C  CA    . ARG A 1 408 ? -29.003 -1.536  30.155  1.00 18.24 ? 428  ARG A CA    1 
ATOM   3060  C  C     . ARG A 1 408 ? -28.287 -0.394  29.463  1.00 18.28 ? 428  ARG A C     1 
ATOM   3061  O  O     . ARG A 1 408 ? -28.613 0.781   29.690  1.00 18.13 ? 428  ARG A O     1 
ATOM   3062  C  CB    . ARG A 1 408 ? -30.191 -1.981  29.302  1.00 18.05 ? 428  ARG A CB    1 
ATOM   3063  C  CG    . ARG A 1 408 ? -31.310 -0.946  29.193  1.00 17.58 ? 428  ARG A CG    1 
ATOM   3064  C  CD    . ARG A 1 408 ? -32.446 -1.477  28.327  1.00 17.16 ? 428  ARG A CD    1 
ATOM   3065  N  NE    . ARG A 1 408 ? -33.757 -1.076  28.835  1.00 17.17 ? 428  ARG A NE    1 
ATOM   3066  C  CZ    . ARG A 1 408 ? -34.371 0.078   28.562  1.00 18.88 ? 428  ARG A CZ    1 
ATOM   3067  N  NH1   . ARG A 1 408 ? -33.809 0.991   27.772  1.00 17.96 ? 428  ARG A NH1   1 
ATOM   3068  N  NH2   . ARG A 1 408 ? -35.568 0.322   29.084  1.00 18.85 ? 428  ARG A NH2   1 
ATOM   3069  N  N     . ARG A 1 409 ? -27.306 -0.741  28.635  1.00 18.06 ? 429  ARG A N     1 
ATOM   3070  C  CA    . ARG A 1 409 ? -26.616 0.244   27.831  1.00 18.11 ? 429  ARG A CA    1 
ATOM   3071  C  C     . ARG A 1 409 ? -26.031 -0.424  26.605  1.00 18.21 ? 429  ARG A C     1 
ATOM   3072  O  O     . ARG A 1 409 ? -25.749 -1.621  26.615  1.00 17.81 ? 429  ARG A O     1 
ATOM   3073  C  CB    . ARG A 1 409 ? -25.525 0.952   28.647  1.00 18.01 ? 429  ARG A CB    1 
ATOM   3074  C  CG    . ARG A 1 409 ? -24.334 0.069   29.013  1.00 17.81 ? 429  ARG A CG    1 
ATOM   3075  C  CD    . ARG A 1 409 ? -23.247 0.104   27.953  1.00 18.70 ? 429  ARG A CD    1 
ATOM   3076  N  NE    . ARG A 1 409 ? -22.485 1.350   27.997  1.00 18.33 ? 429  ARG A NE    1 
ATOM   3077  C  CZ    . ARG A 1 409 ? -21.457 1.638   27.200  1.00 19.14 ? 429  ARG A CZ    1 
ATOM   3078  N  NH1   . ARG A 1 409 ? -21.048 0.780   26.270  1.00 17.64 ? 429  ARG A NH1   1 
ATOM   3079  N  NH2   . ARG A 1 409 ? -20.831 2.802   27.330  1.00 19.45 ? 429  ARG A NH2   1 
ATOM   3080  N  N     . HIS A 1 410 ? -25.868 0.362   25.548  1.00 18.51 ? 430  HIS A N     1 
ATOM   3081  C  CA    . HIS A 1 410 ? -25.262 -0.111  24.326  1.00 18.95 ? 430  HIS A CA    1 
ATOM   3082  C  C     . HIS A 1 410 ? -24.629 1.023   23.545  1.00 18.61 ? 430  HIS A C     1 
ATOM   3083  O  O     . HIS A 1 410 ? -25.251 2.055   23.343  1.00 18.65 ? 430  HIS A O     1 
ATOM   3084  C  CB    . HIS A 1 410 ? -26.299 -0.792  23.437  1.00 19.20 ? 430  HIS A CB    1 
ATOM   3085  C  CG    . HIS A 1 410 ? -25.726 -1.296  22.150  1.00 20.02 ? 430  HIS A CG    1 
ATOM   3086  N  ND1   . HIS A 1 410 ? -24.811 -2.324  22.103  1.00 19.87 ? 430  HIS A ND1   1 
ATOM   3087  C  CD2   . HIS A 1 410 ? -25.920 -0.902  20.868  1.00 20.60 ? 430  HIS A CD2   1 
ATOM   3088  C  CE1   . HIS A 1 410 ? -24.476 -2.551  20.844  1.00 20.50 ? 430  HIS A CE1   1 
ATOM   3089  N  NE2   . HIS A 1 410 ? -25.139 -1.705  20.075  1.00 19.50 ? 430  HIS A NE2   1 
ATOM   3090  N  N     . PHE A 1 411 ? -23.394 0.810   23.104  1.00 18.62 ? 431  PHE A N     1 
ATOM   3091  C  CA    . PHE A 1 411 ? -22.725 1.687   22.147  1.00 18.71 ? 431  PHE A CA    1 
ATOM   3092  C  C     . PHE A 1 411 ? -22.760 1.022   20.768  1.00 19.18 ? 431  PHE A C     1 
ATOM   3093  O  O     . PHE A 1 411 ? -22.062 0.024   20.536  1.00 18.93 ? 431  PHE A O     1 
ATOM   3094  C  CB    . PHE A 1 411 ? -21.272 1.902   22.572  1.00 18.81 ? 431  PHE A CB    1 
ATOM   3095  C  CG    . PHE A 1 411 ? -20.525 2.876   21.708  1.00 19.35 ? 431  PHE A CG    1 
ATOM   3096  C  CD1   . PHE A 1 411 ? -19.728 2.433   20.659  1.00 21.47 ? 431  PHE A CD1   1 
ATOM   3097  C  CD2   . PHE A 1 411 ? -20.616 4.234   21.948  1.00 20.01 ? 431  PHE A CD2   1 
ATOM   3098  C  CE1   . PHE A 1 411 ? -19.019 3.341   19.856  1.00 21.32 ? 431  PHE A CE1   1 
ATOM   3099  C  CE2   . PHE A 1 411 ? -19.921 5.145   21.155  1.00 22.07 ? 431  PHE A CE2   1 
ATOM   3100  C  CZ    . PHE A 1 411 ? -19.117 4.691   20.106  1.00 22.28 ? 431  PHE A CZ    1 
ATOM   3101  N  N     . ASN A 1 412 ? -23.580 1.555   19.861  1.00 19.81 ? 432  ASN A N     1 
ATOM   3102  C  CA    . ASN A 1 412 ? -23.706 0.991   18.518  1.00 20.44 ? 432  ASN A CA    1 
ATOM   3103  C  C     . ASN A 1 412 ? -22.694 1.657   17.585  1.00 21.39 ? 432  ASN A C     1 
ATOM   3104  O  O     . ASN A 1 412 ? -22.974 2.690   16.979  1.00 20.39 ? 432  ASN A O     1 
ATOM   3105  C  CB    . ASN A 1 412 ? -25.134 1.151   17.973  1.00 20.36 ? 432  ASN A CB    1 
ATOM   3106  C  CG    . ASN A 1 412 ? -25.442 0.155   16.860  1.00 20.24 ? 432  ASN A CG    1 
ATOM   3107  O  OD1   . ASN A 1 412 ? -25.646 0.527   15.707  1.00 20.31 ? 432  ASN A OD1   1 
ATOM   3108  N  ND2   . ASN A 1 412 ? -25.445 -1.117  17.203  1.00 19.12 ? 432  ASN A ND2   1 
ATOM   3109  N  N     . SER A 1 413 ? -21.508 1.064   17.497  1.00 23.01 ? 433  SER A N     1 
ATOM   3110  C  CA    . SER A 1 413 ? -20.415 1.636   16.723  1.00 24.26 ? 433  SER A CA    1 
ATOM   3111  C  C     . SER A 1 413 ? -20.725 1.591   15.228  1.00 25.41 ? 433  SER A C     1 
ATOM   3112  O  O     . SER A 1 413 ? -21.485 0.731   14.770  1.00 25.43 ? 433  SER A O     1 
ATOM   3113  C  CB    . SER A 1 413 ? -19.127 0.869   17.009  1.00 24.82 ? 433  SER A CB    1 
ATOM   3114  O  OG    . SER A 1 413 ? -18.048 1.366   16.232  1.00 25.30 ? 433  SER A OG    1 
ATOM   3115  N  N     . ASN A 1 414 ? -20.163 2.530   14.471  1.00 26.51 ? 434  ASN A N     1 
ATOM   3116  C  CA    . ASN A 1 414 ? -20.182 2.416   13.010  1.00 27.83 ? 434  ASN A CA    1 
ATOM   3117  C  C     . ASN A 1 414 ? -18.863 1.843   12.481  1.00 28.76 ? 434  ASN A C     1 
ATOM   3118  O  O     . ASN A 1 414 ? -18.670 1.745   11.284  1.00 29.55 ? 434  ASN A O     1 
ATOM   3119  C  CB    . ASN A 1 414 ? -20.533 3.752   12.324  1.00 27.56 ? 434  ASN A CB    1 
ATOM   3120  C  CG    . ASN A 1 414 ? -19.432 4.796   12.438  1.00 27.68 ? 434  ASN A CG    1 
ATOM   3121  O  OD1   . ASN A 1 414 ? -18.297 4.507   12.845  1.00 25.73 ? 434  ASN A OD1   1 
ATOM   3122  N  ND2   . ASN A 1 414 ? -19.767 6.026   12.076  1.00 26.92 ? 434  ASN A ND2   1 
ATOM   3123  N  N     . PHE A 1 415 ? -17.950 1.494   13.382  1.00 30.21 ? 435  PHE A N     1 
ATOM   3124  C  CA    . PHE A 1 415 ? -16.669 0.884   13.012  1.00 31.08 ? 435  PHE A CA    1 
ATOM   3125  C  C     . PHE A 1 415 ? -15.870 1.755   12.034  1.00 31.45 ? 435  PHE A C     1 
ATOM   3126  O  O     . PHE A 1 415 ? -14.995 1.261   11.330  1.00 32.09 ? 435  PHE A O     1 
ATOM   3127  C  CB    . PHE A 1 415 ? -16.905 -0.533  12.438  1.00 31.42 ? 435  PHE A CB    1 
ATOM   3128  C  CG    . PHE A 1 415 ? -17.936 -1.331  13.210  1.00 31.90 ? 435  PHE A CG    1 
ATOM   3129  C  CD1   . PHE A 1 415 ? -19.151 -1.668  12.632  1.00 32.70 ? 435  PHE A CD1   1 
ATOM   3130  C  CD2   . PHE A 1 415 ? -17.700 -1.694  14.530  1.00 33.86 ? 435  PHE A CD2   1 
ATOM   3131  C  CE1   . PHE A 1 415 ? -20.103 -2.374  13.339  1.00 32.97 ? 435  PHE A CE1   1 
ATOM   3132  C  CE2   . PHE A 1 415 ? -18.662 -2.403  15.261  1.00 33.94 ? 435  PHE A CE2   1 
ATOM   3133  C  CZ    . PHE A 1 415 ? -19.860 -2.739  14.663  1.00 33.94 ? 435  PHE A CZ    1 
ATOM   3134  N  N     . LYS A 1 416 ? -16.177 3.050   12.011  1.00 31.53 ? 436  LYS A N     1 
ATOM   3135  C  CA    . LYS A 1 416 ? -15.527 4.008   11.127  1.00 31.40 ? 436  LYS A CA    1 
ATOM   3136  C  C     . LYS A 1 416 ? -15.176 5.269   11.913  1.00 31.03 ? 436  LYS A C     1 
ATOM   3137  O  O     . LYS A 1 416 ? -15.239 6.380   11.380  1.00 31.34 ? 436  LYS A O     1 
ATOM   3138  C  CB    . LYS A 1 416 ? -16.458 4.364   9.957   1.00 31.49 ? 436  LYS A CB    1 
ATOM   3139  N  N     . GLY A 1 417 ? -14.813 5.099   13.183  1.00 30.31 ? 437  GLY A N     1 
ATOM   3140  C  CA    . GLY A 1 417 ? -14.453 6.235   14.040  1.00 29.78 ? 437  GLY A CA    1 
ATOM   3141  C  C     . GLY A 1 417 ? -15.619 6.962   14.690  1.00 29.02 ? 437  GLY A C     1 
ATOM   3142  O  O     . GLY A 1 417 ? -15.422 8.003   15.322  1.00 28.75 ? 437  GLY A O     1 
ATOM   3143  N  N     . GLY A 1 418 ? -16.829 6.428   14.542  1.00 28.14 ? 438  GLY A N     1 
ATOM   3144  C  CA    . GLY A 1 418 ? -18.016 7.052   15.119  1.00 27.38 ? 438  GLY A CA    1 
ATOM   3145  C  C     . GLY A 1 418 ? -19.054 6.043   15.569  1.00 26.72 ? 438  GLY A C     1 
ATOM   3146  O  O     . GLY A 1 418 ? -18.726 4.909   15.916  1.00 27.18 ? 438  GLY A O     1 
ATOM   3147  N  N     . PHE A 1 419 ? -20.316 6.448   15.543  1.00 25.59 ? 439  PHE A N     1 
ATOM   3148  C  CA    . PHE A 1 419 ? -21.383 5.611   16.061  1.00 24.81 ? 439  PHE A CA    1 
ATOM   3149  C  C     . PHE A 1 419 ? -22.708 5.862   15.358  1.00 23.78 ? 439  PHE A C     1 
ATOM   3150  O  O     . PHE A 1 419 ? -22.877 6.869   14.684  1.00 23.39 ? 439  PHE A O     1 
ATOM   3151  C  CB    . PHE A 1 419 ? -21.496 5.775   17.588  1.00 24.98 ? 439  PHE A CB    1 
ATOM   3152  C  CG    . PHE A 1 419 ? -22.177 7.053   18.058  1.00 25.15 ? 439  PHE A CG    1 
ATOM   3153  C  CD1   . PHE A 1 419 ? -23.029 7.012   19.152  1.00 25.11 ? 439  PHE A CD1   1 
ATOM   3154  C  CD2   . PHE A 1 419 ? -21.944 8.284   17.451  1.00 25.61 ? 439  PHE A CD2   1 
ATOM   3155  C  CE1   . PHE A 1 419 ? -23.655 8.162   19.619  1.00 26.16 ? 439  PHE A CE1   1 
ATOM   3156  C  CE2   . PHE A 1 419 ? -22.574 9.440   17.900  1.00 24.93 ? 439  PHE A CE2   1 
ATOM   3157  C  CZ    . PHE A 1 419 ? -23.424 9.386   18.985  1.00 26.24 ? 439  PHE A CZ    1 
ATOM   3158  N  N     . ASN A 1 420 ? -23.624 4.910   15.498  1.00 22.83 ? 440  ASN A N     1 
ATOM   3159  C  CA    . ASN A 1 420 ? -24.994 5.052   15.004  1.00 22.19 ? 440  ASN A CA    1 
ATOM   3160  C  C     . ASN A 1 420 ? -25.899 5.524   16.115  1.00 21.51 ? 440  ASN A C     1 
ATOM   3161  O  O     . ASN A 1 420 ? -26.880 6.230   15.860  1.00 21.86 ? 440  ASN A O     1 
ATOM   3162  C  CB    . ASN A 1 420 ? -25.505 3.721   14.469  1.00 22.35 ? 440  ASN A CB    1 
ATOM   3163  C  CG    . ASN A 1 420 ? -24.605 3.145   13.388  1.00 22.75 ? 440  ASN A CG    1 
ATOM   3164  O  OD1   . ASN A 1 420 ? -24.184 3.857   12.475  1.00 23.01 ? 440  ASN A OD1   1 
ATOM   3165  N  ND2   . ASN A 1 420 ? -24.311 1.852   13.487  1.00 22.03 ? 440  ASN A ND2   1 
ATOM   3166  N  N     . PHE A 1 421 ? -25.592 5.094   17.337  1.00 20.37 ? 441  PHE A N     1 
ATOM   3167  C  CA    . PHE A 1 421 ? -26.236 5.628   18.531  1.00 19.87 ? 441  PHE A CA    1 
ATOM   3168  C  C     . PHE A 1 421 ? -25.585 5.115   19.810  1.00 19.21 ? 441  PHE A C     1 
ATOM   3169  O  O     . PHE A 1 421 ? -24.892 4.101   19.800  1.00 19.66 ? 441  PHE A O     1 
ATOM   3170  C  CB    . PHE A 1 421 ? -27.758 5.329   18.541  1.00 19.87 ? 441  PHE A CB    1 
ATOM   3171  C  CG    . PHE A 1 421 ? -28.105 3.867   18.699  1.00 19.04 ? 441  PHE A CG    1 
ATOM   3172  C  CD1   . PHE A 1 421 ? -28.288 3.055   17.587  1.00 18.41 ? 441  PHE A CD1   1 
ATOM   3173  C  CD2   . PHE A 1 421 ? -28.279 3.312   19.970  1.00 18.66 ? 441  PHE A CD2   1 
ATOM   3174  C  CE1   . PHE A 1 421 ? -28.615 1.716   17.741  1.00 19.57 ? 441  PHE A CE1   1 
ATOM   3175  C  CE2   . PHE A 1 421 ? -28.614 1.975   20.132  1.00 18.53 ? 441  PHE A CE2   1 
ATOM   3176  C  CZ    . PHE A 1 421 ? -28.779 1.172   19.025  1.00 19.45 ? 441  PHE A CZ    1 
ATOM   3177  N  N     . TYR A 1 422 ? -25.763 5.857   20.898  1.00 19.13 ? 442  TYR A N     1 
ATOM   3178  C  CA    . TYR A 1 422 ? -25.608 5.307   22.248  1.00 18.83 ? 442  TYR A CA    1 
ATOM   3179  C  C     . TYR A 1 422 ? -26.978 5.310   22.908  1.00 18.82 ? 442  TYR A C     1 
ATOM   3180  O  O     . TYR A 1 422 ? -27.718 6.282   22.787  1.00 18.72 ? 442  TYR A O     1 
ATOM   3181  C  CB    . TYR A 1 422 ? -24.646 6.123   23.103  1.00 18.83 ? 442  TYR A CB    1 
ATOM   3182  C  CG    . TYR A 1 422 ? -24.724 5.760   24.568  1.00 18.11 ? 442  TYR A CG    1 
ATOM   3183  C  CD1   . TYR A 1 422 ? -23.948 4.740   25.090  1.00 18.94 ? 442  TYR A CD1   1 
ATOM   3184  C  CD2   . TYR A 1 422 ? -25.603 6.411   25.419  1.00 18.71 ? 442  TYR A CD2   1 
ATOM   3185  C  CE1   . TYR A 1 422 ? -24.028 4.391   26.423  1.00 19.25 ? 442  TYR A CE1   1 
ATOM   3186  C  CE2   . TYR A 1 422 ? -25.693 6.065   26.761  1.00 19.02 ? 442  TYR A CE2   1 
ATOM   3187  C  CZ    . TYR A 1 422 ? -24.900 5.055   27.256  1.00 18.66 ? 442  TYR A CZ    1 
ATOM   3188  O  OH    . TYR A 1 422 ? -24.982 4.700   28.583  1.00 18.66 ? 442  TYR A OH    1 
ATOM   3189  N  N     . ALA A 1 423 ? -27.300 4.233   23.614  1.00 18.44 ? 443  ALA A N     1 
ATOM   3190  C  CA    . ALA A 1 423 ? -28.541 4.153   24.383  1.00 18.83 ? 443  ALA A CA    1 
ATOM   3191  C  C     . ALA A 1 423 ? -28.246 3.603   25.767  1.00 18.64 ? 443  ALA A C     1 
ATOM   3192  O  O     . ALA A 1 423 ? -27.485 2.658   25.908  1.00 18.31 ? 443  ALA A O     1 
ATOM   3193  C  CB    . ALA A 1 423 ? -29.588 3.276   23.680  1.00 17.80 ? 443  ALA A CB    1 
ATOM   3194  N  N     . GLY A 1 424 ? -28.866 4.194   26.783  1.00 19.07 ? 444  GLY A N     1 
ATOM   3195  C  CA    . GLY A 1 424 ? -28.669 3.736   28.152  1.00 19.27 ? 444  GLY A CA    1 
ATOM   3196  C  C     . GLY A 1 424 ? -29.793 4.148   29.074  1.00 19.47 ? 444  GLY A C     1 
ATOM   3197  O  O     . GLY A 1 424 ? -30.464 5.148   28.842  1.00 19.19 ? 444  GLY A O     1 
ATOM   3198  N  N     . LEU A 1 425 ? -29.991 3.357   30.122  1.00 19.88 ? 445  LEU A N     1 
ATOM   3199  C  CA    . LEU A 1 425 ? -30.957 3.660   31.165  1.00 20.11 ? 445  LEU A CA    1 
ATOM   3200  C  C     . LEU A 1 425 ? -30.226 3.604   32.497  1.00 19.89 ? 445  LEU A C     1 
ATOM   3201  O  O     . LEU A 1 425 ? -29.694 2.558   32.869  1.00 19.69 ? 445  LEU A O     1 
ATOM   3202  C  CB    . LEU A 1 425 ? -32.128 2.668   31.116  1.00 20.10 ? 445  LEU A CB    1 
ATOM   3203  C  CG    . LEU A 1 425 ? -33.120 2.645   32.290  1.00 20.94 ? 445  LEU A CG    1 
ATOM   3204  C  CD1   . LEU A 1 425 ? -33.674 4.014   32.603  1.00 21.04 ? 445  LEU A CD1   1 
ATOM   3205  C  CD2   . LEU A 1 425 ? -34.266 1.670   32.004  1.00 20.11 ? 445  LEU A CD2   1 
ATOM   3206  N  N     . LYS A 1 426 ? -30.191 4.738   33.199  1.00 20.19 ? 446  LYS A N     1 
ATOM   3207  C  CA    . LYS A 1 426 ? -29.511 4.859   34.492  1.00 20.55 ? 446  LYS A CA    1 
ATOM   3208  C  C     . LYS A 1 426 ? -30.080 3.848   35.484  1.00 20.66 ? 446  LYS A C     1 
ATOM   3209  O  O     . LYS A 1 426 ? -31.289 3.664   35.562  1.00 21.12 ? 446  LYS A O     1 
ATOM   3210  C  CB    . LYS A 1 426 ? -29.662 6.280   35.054  1.00 20.34 ? 446  LYS A CB    1 
ATOM   3211  C  CG    . LYS A 1 426 ? -29.032 6.517   36.418  1.00 21.72 ? 446  LYS A CG    1 
ATOM   3212  C  CD    . LYS A 1 426 ? -29.239 7.963   36.914  1.00 23.01 ? 446  LYS A CD    1 
ATOM   3213  C  CE    . LYS A 1 426 ? -28.635 8.155   38.300  1.00 24.27 ? 446  LYS A CE    1 
ATOM   3214  N  NZ    . LYS A 1 426 ? -28.851 9.525   38.848  1.00 25.72 ? 446  LYS A NZ    1 
ATOM   3215  N  N     . GLY A 1 427 ? -29.197 3.217   36.244  1.00 20.46 ? 447  GLY A N     1 
ATOM   3216  C  CA    . GLY A 1 427 ? -29.588 2.207   37.211  1.00 20.36 ? 447  GLY A CA    1 
ATOM   3217  C  C     . GLY A 1 427 ? -30.133 2.794   38.490  1.00 20.20 ? 447  GLY A C     1 
ATOM   3218  O  O     . GLY A 1 427 ? -29.461 3.591   39.144  1.00 19.94 ? 447  GLY A O     1 
ATOM   3219  N  N     . GLN A 1 428 ? -31.373 2.419   38.808  1.00 20.03 ? 448  GLN A N     1 
ATOM   3220  C  CA    . GLN A 1 428 ? -32.022 2.733   40.074  1.00 20.05 ? 448  GLN A CA    1 
ATOM   3221  C  C     . GLN A 1 428 ? -32.651 1.450   40.642  1.00 19.56 ? 448  GLN A C     1 
ATOM   3222  O  O     . GLN A 1 428 ? -32.947 0.515   39.901  1.00 19.22 ? 448  GLN A O     1 
ATOM   3223  C  CB    . GLN A 1 428 ? -33.132 3.780   39.882  1.00 20.51 ? 448  GLN A CB    1 
ATOM   3224  C  CG    . GLN A 1 428 ? -32.676 5.163   39.374  1.00 21.04 ? 448  GLN A CG    1 
ATOM   3225  C  CD    . GLN A 1 428 ? -32.127 6.082   40.479  1.00 23.41 ? 448  GLN A CD    1 
ATOM   3226  O  OE1   . GLN A 1 428 ? -31.988 5.677   41.640  1.00 24.43 ? 448  GLN A OE1   1 
ATOM   3227  N  NE2   . GLN A 1 428 ? -31.828 7.333   40.113  1.00 21.88 ? 448  GLN A NE2   1 
ATOM   3228  N  N     . VAL A 1 429 ? -32.828 1.423   41.959  1.00 19.02 ? 449  VAL A N     1 
ATOM   3229  C  CA    A VAL A 1 429 ? -33.541 0.341   42.639  0.60 18.77 ? 449  VAL A CA    1 
ATOM   3230  C  CA    B VAL A 1 429 ? -33.566 0.354   42.614  0.40 18.88 ? 449  VAL A CA    1 
ATOM   3231  C  C     . VAL A 1 429 ? -34.321 0.903   43.824  1.00 18.60 ? 449  VAL A C     1 
ATOM   3232  O  O     . VAL A 1 429 ? -33.895 1.880   44.443  1.00 18.51 ? 449  VAL A O     1 
ATOM   3233  C  CB    A VAL A 1 429 ? -32.579 -0.753  43.165  0.60 19.06 ? 449  VAL A CB    1 
ATOM   3234  C  CB    B VAL A 1 429 ? -32.632 -0.799  43.040  0.40 19.09 ? 449  VAL A CB    1 
ATOM   3235  C  CG1   A VAL A 1 429 ? -32.038 -1.608  42.007  0.60 18.23 ? 449  VAL A CG1   1 
ATOM   3236  C  CG1   B VAL A 1 429 ? -32.046 -0.548  44.435  0.40 18.81 ? 449  VAL A CG1   1 
ATOM   3237  C  CG2   A VAL A 1 429 ? -31.444 -0.133  43.996  0.60 18.25 ? 449  VAL A CG2   1 
ATOM   3238  C  CG2   B VAL A 1 429 ? -33.378 -2.125  42.986  0.40 18.93 ? 449  VAL A CG2   1 
ATOM   3239  N  N     . LEU A 1 430 ? -35.454 0.280   44.134  1.00 18.04 ? 450  LEU A N     1 
ATOM   3240  C  CA    . LEU A 1 430 ? -36.242 0.618   45.314  1.00 17.20 ? 450  LEU A CA    1 
ATOM   3241  C  C     . LEU A 1 430 ? -35.851 -0.374  46.400  1.00 16.94 ? 450  LEU A C     1 
ATOM   3242  O  O     . LEU A 1 430 ? -35.782 -1.571  46.138  1.00 16.95 ? 450  LEU A O     1 
ATOM   3243  C  CB    . LEU A 1 430 ? -37.725 0.474   45.020  1.00 16.95 ? 450  LEU A CB    1 
ATOM   3244  C  CG    . LEU A 1 430 ? -38.674 0.723   46.195  1.00 17.03 ? 450  LEU A CG    1 
ATOM   3245  C  CD1   . LEU A 1 430 ? -38.690 2.226   46.540  1.00 16.44 ? 450  LEU A CD1   1 
ATOM   3246  C  CD2   . LEU A 1 430 ? -40.085 0.209   45.862  1.00 15.24 ? 450  LEU A CD2   1 
ATOM   3247  N  N     . VAL A 1 431 ? -35.618 0.117   47.615  1.00 16.51 ? 451  VAL A N     1 
ATOM   3248  C  CA    . VAL A 1 431 ? -35.194 -0.729  48.717  1.00 16.30 ? 451  VAL A CA    1 
ATOM   3249  C  C     . VAL A 1 431 ? -36.120 -0.537  49.911  1.00 16.72 ? 451  VAL A C     1 
ATOM   3250  O  O     . VAL A 1 431 ? -36.288 0.584   50.380  1.00 16.54 ? 451  VAL A O     1 
ATOM   3251  C  CB    . VAL A 1 431 ? -33.773 -0.380  49.171  1.00 16.52 ? 451  VAL A CB    1 
ATOM   3252  C  CG1   . VAL A 1 431 ? -33.364 -1.247  50.382  1.00 16.01 ? 451  VAL A CG1   1 
ATOM   3253  C  CG2   . VAL A 1 431 ? -32.800 -0.519  48.016  1.00 15.41 ? 451  VAL A CG2   1 
ATOM   3254  N  N     . LEU A 1 432 ? -36.707 -1.645  50.378  1.00 16.96 ? 452  LEU A N     1 
ATOM   3255  C  CA    . LEU A 1 432 ? -37.455 -1.718  51.635  1.00 17.09 ? 452  LEU A CA    1 
ATOM   3256  C  C     . LEU A 1 432 ? -36.572 -2.437  52.621  1.00 16.76 ? 452  LEU A C     1 
ATOM   3257  O  O     . LEU A 1 432 ? -36.159 -3.572  52.375  1.00 16.96 ? 452  LEU A O     1 
ATOM   3258  C  CB    . LEU A 1 432 ? -38.755 -2.518  51.459  1.00 17.46 ? 452  LEU A CB    1 
ATOM   3259  C  CG    . LEU A 1 432 ? -39.614 -2.739  52.711  1.00 17.51 ? 452  LEU A CG    1 
ATOM   3260  C  CD1   . LEU A 1 432 ? -40.120 -1.397  53.255  1.00 17.02 ? 452  LEU A CD1   1 
ATOM   3261  C  CD2   . LEU A 1 432 ? -40.780 -3.701  52.412  1.00 16.86 ? 452  LEU A CD2   1 
ATOM   3262  N  N     . ARG A 1 433 ? -36.318 -1.800  53.758  1.00 16.31 ? 453  ARG A N     1 
ATOM   3263  C  CA    . ARG A 1 433 ? -35.339 -2.292  54.699  1.00 15.81 ? 453  ARG A CA    1 
ATOM   3264  C  C     . ARG A 1 433 ? -35.829 -2.201  56.125  1.00 16.10 ? 453  ARG A C     1 
ATOM   3265  O  O     . ARG A 1 433 ? -36.504 -1.239  56.514  1.00 16.10 ? 453  ARG A O     1 
ATOM   3266  C  CB    . ARG A 1 433 ? -34.041 -1.487  54.565  1.00 15.67 ? 453  ARG A CB    1 
ATOM   3267  C  CG    . ARG A 1 433 ? -32.991 -1.782  55.642  1.00 16.58 ? 453  ARG A CG    1 
ATOM   3268  C  CD    . ARG A 1 433 ? -31.706 -1.030  55.332  1.00 17.98 ? 453  ARG A CD    1 
ATOM   3269  N  NE    . ARG A 1 433 ? -31.086 -1.549  54.120  1.00 16.92 ? 453  ARG A NE    1 
ATOM   3270  C  CZ    . ARG A 1 433 ? -30.169 -0.909  53.399  1.00 18.05 ? 453  ARG A CZ    1 
ATOM   3271  N  NH1   . ARG A 1 433 ? -29.756 0.303   53.733  1.00 16.87 ? 453  ARG A NH1   1 
ATOM   3272  N  NH2   . ARG A 1 433 ? -29.665 -1.496  52.316  1.00 18.71 ? 453  ARG A NH2   1 
ATOM   3273  N  N     . THR A 1 434 ? -35.472 -3.211  56.908  1.00 16.48 ? 454  THR A N     1 
ATOM   3274  C  CA    . THR A 1 434 ? -35.524 -3.109  58.357  1.00 16.70 ? 454  THR A CA    1 
ATOM   3275  C  C     . THR A 1 434 ? -34.269 -3.783  58.896  1.00 17.30 ? 454  THR A C     1 
ATOM   3276  O  O     . THR A 1 434 ? -33.396 -4.212  58.127  1.00 17.26 ? 454  THR A O     1 
ATOM   3277  C  CB    . THR A 1 434 ? -36.840 -3.715  58.945  1.00 16.97 ? 454  THR A CB    1 
ATOM   3278  O  OG1   . THR A 1 434 ? -36.950 -3.388  60.338  1.00 15.93 ? 454  THR A OG1   1 
ATOM   3279  C  CG2   . THR A 1 434 ? -36.885 -5.225  58.773  1.00 15.82 ? 454  THR A CG2   1 
ATOM   3280  N  N     . THR A 1 435 ? -34.167 -3.859  60.212  1.00 17.81 ? 455  THR A N     1 
ATOM   3281  C  CA    . THR A 1 435 ? -33.046 -4.504  60.854  1.00 18.33 ? 455  THR A CA    1 
ATOM   3282  C  C     . THR A 1 435 ? -33.560 -5.373  61.993  1.00 19.21 ? 455  THR A C     1 
ATOM   3283  O  O     . THR A 1 435 ? -34.723 -5.261  62.407  1.00 18.85 ? 455  THR A O     1 
ATOM   3284  C  CB    . THR A 1 435 ? -32.061 -3.462  61.441  1.00 18.61 ? 455  THR A CB    1 
ATOM   3285  O  OG1   . THR A 1 435 ? -32.715 -2.706  62.471  1.00 19.09 ? 455  THR A OG1   1 
ATOM   3286  C  CG2   . THR A 1 435 ? -31.545 -2.510  60.358  1.00 17.80 ? 455  THR A CG2   1 
ATOM   3287  N  N     . SER A 1 436 ? -32.695 -6.241  62.493  1.00 19.50 ? 456  SER A N     1 
ATOM   3288  C  CA    . SER A 1 436 ? -32.974 -6.950  63.723  1.00 20.39 ? 456  SER A CA    1 
ATOM   3289  C  C     . SER A 1 436 ? -31.690 -6.995  64.537  1.00 20.92 ? 456  SER A C     1 
ATOM   3290  O  O     . SER A 1 436 ? -30.660 -7.512  64.081  1.00 20.69 ? 456  SER A O     1 
ATOM   3291  C  CB    . SER A 1 436 ? -33.549 -8.343  63.458  1.00 20.44 ? 456  SER A CB    1 
ATOM   3292  O  OG    . SER A 1 436 ? -32.657 -9.140  62.722  1.00 22.81 ? 456  SER A OG    1 
ATOM   3293  N  N     . THR A 1 437 ? -31.748 -6.375  65.714  1.00 21.65 ? 457  THR A N     1 
ATOM   3294  C  CA    . THR A 1 437 ? -30.652 -6.400  66.669  1.00 22.51 ? 457  THR A CA    1 
ATOM   3295  C  C     . THR A 1 437 ? -31.188 -7.003  67.956  1.00 23.63 ? 457  THR A C     1 
ATOM   3296  O  O     . THR A 1 437 ? -31.661 -6.278  68.829  1.00 23.84 ? 457  THR A O     1 
ATOM   3297  C  CB    . THR A 1 437 ? -30.129 -4.993  66.983  1.00 22.24 ? 457  THR A CB    1 
ATOM   3298  O  OG1   . THR A 1 437 ? -29.862 -4.280  65.771  1.00 23.14 ? 457  THR A OG1   1 
ATOM   3299  C  CG2   . THR A 1 437 ? -28.859 -5.066  67.835  1.00 21.79 ? 457  THR A CG2   1 
ATOM   3300  N  N     . VAL A 1 438 ? -31.139 -8.322  68.077  1.00 24.81 ? 458  VAL A N     1 
ATOM   3301  C  CA    . VAL A 1 438 ? -31.616 -8.981  69.303  1.00 25.65 ? 458  VAL A CA    1 
ATOM   3302  C  C     . VAL A 1 438 ? -30.661 -8.694  70.466  1.00 26.09 ? 458  VAL A C     1 
ATOM   3303  O  O     . VAL A 1 438 ? -31.094 -8.461  71.610  1.00 27.36 ? 458  VAL A O     1 
ATOM   3304  C  CB    . VAL A 1 438 ? -31.759 -10.510 69.120  1.00 26.12 ? 458  VAL A CB    1 
ATOM   3305  N  N     . TYR A 1 439 ? -29.367 -8.687  70.172  1.00 25.77 ? 459  TYR A N     1 
ATOM   3306  C  CA    . TYR A 1 439 ? -28.360 -8.549  71.203  1.00 25.88 ? 459  TYR A CA    1 
ATOM   3307  C  C     . TYR A 1 439 ? -27.025 -8.118  70.609  1.00 25.31 ? 459  TYR A C     1 
ATOM   3308  O  O     . TYR A 1 439 ? -26.770 -6.922  70.505  1.00 25.68 ? 459  TYR A O     1 
ATOM   3309  C  CB    . TYR A 1 439 ? -28.254 -9.872  71.957  1.00 26.30 ? 459  TYR A CB    1 
ATOM   3310  C  CG    . TYR A 1 439 ? -27.413 -9.872  73.201  1.00 28.56 ? 459  TYR A CG    1 
ATOM   3311  C  CD1   . TYR A 1 439 ? -27.801 -9.145  74.325  1.00 30.25 ? 459  TYR A CD1   1 
ATOM   3312  C  CD2   . TYR A 1 439 ? -26.255 -10.661 73.287  1.00 31.18 ? 459  TYR A CD2   1 
ATOM   3313  C  CE1   . TYR A 1 439 ? -27.043 -9.184  75.507  1.00 32.28 ? 459  TYR A CE1   1 
ATOM   3314  C  CE2   . TYR A 1 439 ? -25.495 -10.708 74.456  1.00 30.78 ? 459  TYR A CE2   1 
ATOM   3315  C  CZ    . TYR A 1 439 ? -25.891 -9.970  75.557  1.00 32.79 ? 459  TYR A CZ    1 
ATOM   3316  O  OH    . TYR A 1 439 ? -25.143 -10.018 76.707  1.00 33.99 ? 459  TYR A OH    1 
ATOM   3317  N  N     . ASN A 1 440 ? -26.192 -9.068  70.191  1.00 24.98 ? 460  ASN A N     1 
ATOM   3318  C  CA    . ASN A 1 440 ? -24.832 -8.749  69.714  1.00 24.47 ? 460  ASN A CA    1 
ATOM   3319  C  C     . ASN A 1 440 ? -24.770 -8.400  68.227  1.00 24.03 ? 460  ASN A C     1 
ATOM   3320  O  O     . ASN A 1 440 ? -24.134 -7.423  67.855  1.00 23.87 ? 460  ASN A O     1 
ATOM   3321  C  CB    . ASN A 1 440 ? -23.843 -9.879  70.041  1.00 24.24 ? 460  ASN A CB    1 
ATOM   3322  C  CG    . ASN A 1 440 ? -24.256 -11.223 69.467  1.00 24.63 ? 460  ASN A CG    1 
ATOM   3323  O  OD1   . ASN A 1 440 ? -25.314 -11.756 69.809  1.00 25.40 ? 460  ASN A OD1   1 
ATOM   3324  N  ND2   . ASN A 1 440 ? -23.403 -11.798 68.614  1.00 23.69 ? 460  ASN A ND2   1 
HETATM 3325  N  N     . TPQ A 1 441 ? -25.435 -9.203  67.395  1.00 23.53 ? 461  TPQ A N     1 
HETATM 3326  C  CA    . TPQ A 1 441 ? -25.452 -9.018  65.941  1.00 23.64 ? 461  TPQ A CA    1 
HETATM 3327  C  CB    . TPQ A 1 441 ? -25.780 -10.357 65.252  1.00 24.37 ? 461  TPQ A CB    1 
HETATM 3328  C  C     . TPQ A 1 441 ? -26.546 -8.083  65.444  1.00 22.83 ? 461  TPQ A C     1 
HETATM 3329  O  O     . TPQ A 1 441 ? -27.610 -7.989  66.050  1.00 23.09 ? 461  TPQ A O     1 
HETATM 3330  C  C1    . TPQ A 1 441 ? -24.560 -11.152 64.868  1.00 25.56 ? 461  TPQ A C1    1 
HETATM 3331  C  C2    . TPQ A 1 441 ? -24.426 -12.551 65.332  1.00 25.96 ? 461  TPQ A C2    1 
HETATM 3332  O  O2    . TPQ A 1 441 ? -25.300 -13.083 66.050  0.50 25.32 ? 461  TPQ A O2    1 
HETATM 3333  C  C3    . TPQ A 1 441 ? -23.220 -13.316 64.917  1.00 27.15 ? 461  TPQ A C3    1 
HETATM 3334  C  C4    . TPQ A 1 441 ? -22.238 -12.743 64.101  1.00 26.59 ? 461  TPQ A C4    1 
HETATM 3335  O  O4    . TPQ A 1 441 ? -21.235 -13.385 63.764  1.00 24.85 ? 461  TPQ A O4    1 
HETATM 3336  C  C5    . TPQ A 1 441 ? -22.372 -11.349 63.641  1.00 27.40 ? 461  TPQ A C5    1 
HETATM 3337  O  O5    . TPQ A 1 441 ? -21.489 -10.843 62.914  0.50 27.82 ? 461  TPQ A O5    1 
HETATM 3338  C  C6    . TPQ A 1 441 ? -23.581 -10.581 64.051  1.00 26.98 ? 461  TPQ A C6    1 
ATOM   3339  N  N     . ASP A 1 442 ? -26.292 -7.418  64.321  1.00 22.23 ? 462  ASP A N     1 
ATOM   3340  C  CA    . ASP A 1 442 ? -27.304 -6.635  63.632  1.00 21.52 ? 462  ASP A CA    1 
ATOM   3341  C  C     . ASP A 1 442 ? -27.486 -7.211  62.238  1.00 21.21 ? 462  ASP A C     1 
ATOM   3342  O  O     . ASP A 1 442 ? -26.556 -7.202  61.427  1.00 21.47 ? 462  ASP A O     1 
ATOM   3343  C  CB    . ASP A 1 442 ? -26.909 -5.165  63.519  1.00 21.54 ? 462  ASP A CB    1 
ATOM   3344  C  CG    . ASP A 1 442 ? -26.744 -4.491  64.862  1.00 21.66 ? 462  ASP A CG    1 
ATOM   3345  O  OD1   . ASP A 1 442 ? -25.853 -4.916  65.623  1.00 20.54 ? 462  ASP A OD1   1 
ATOM   3346  O  OD2   . ASP A 1 442 ? -27.486 -3.515  65.136  1.00 21.93 ? 462  ASP A OD2   1 
ATOM   3347  N  N     . TYR A 1 443 ? -28.671 -7.756  61.978  1.00 20.53 ? 463  TYR A N     1 
ATOM   3348  C  CA    A TYR A 1 443 ? -28.975 -8.167  60.630  0.50 20.10 ? 463  TYR A CA    1 
ATOM   3349  C  CA    B TYR A 1 443 ? -29.090 -8.214  60.643  0.50 20.07 ? 463  TYR A CA    1 
ATOM   3350  C  C     . TYR A 1 443 ? -29.731 -7.045  59.922  1.00 19.72 ? 463  TYR A C     1 
ATOM   3351  O  O     . TYR A 1 443 ? -30.580 -6.360  60.513  1.00 19.23 ? 463  TYR A O     1 
ATOM   3352  C  CB    A TYR A 1 443 ? -29.698 -9.505  60.641  0.50 19.92 ? 463  TYR A CB    1 
ATOM   3353  C  CB    B TYR A 1 443 ? -30.209 -9.258  60.707  0.50 19.95 ? 463  TYR A CB    1 
ATOM   3354  C  CG    A TYR A 1 443 ? -28.857 -10.558 61.334  0.50 20.80 ? 463  TYR A CG    1 
ATOM   3355  C  CG    B TYR A 1 443 ? -29.922 -10.623 61.280  0.50 20.52 ? 463  TYR A CG    1 
ATOM   3356  C  CD1   A TYR A 1 443 ? -27.721 -11.079 60.728  0.50 20.87 ? 463  TYR A CD1   1 
ATOM   3357  C  CD1   B TYR A 1 443 ? -29.449 -11.648 60.480  0.50 20.64 ? 463  TYR A CD1   1 
ATOM   3358  C  CD2   A TYR A 1 443 ? -29.162 -10.986 62.619  0.50 22.00 ? 463  TYR A CD2   1 
ATOM   3359  C  CD2   B TYR A 1 443 ? -30.226 -10.917 62.600  0.50 21.29 ? 463  TYR A CD2   1 
ATOM   3360  C  CE1   A TYR A 1 443 ? -26.938 -12.025 61.364  0.50 21.26 ? 463  TYR A CE1   1 
ATOM   3361  C  CE1   B TYR A 1 443 ? -29.229 -12.912 60.990  0.50 20.50 ? 463  TYR A CE1   1 
ATOM   3362  C  CE2   A TYR A 1 443 ? -28.381 -11.932 63.263  0.50 22.27 ? 463  TYR A CE2   1 
ATOM   3363  C  CE2   B TYR A 1 443 ? -30.011 -12.173 63.116  0.50 21.29 ? 463  TYR A CE2   1 
ATOM   3364  C  CZ    A TYR A 1 443 ? -27.275 -12.448 62.630  0.50 21.75 ? 463  TYR A CZ    1 
ATOM   3365  C  CZ    B TYR A 1 443 ? -29.514 -13.170 62.305  0.50 21.12 ? 463  TYR A CZ    1 
ATOM   3366  O  OH    A TYR A 1 443 ? -26.511 -13.391 63.275  0.50 22.30 ? 463  TYR A OH    1 
ATOM   3367  O  OH    B TYR A 1 443 ? -29.294 -14.429 62.816  0.50 21.74 ? 463  TYR A OH    1 
ATOM   3368  N  N     . ILE A 1 444 ? -29.381 -6.846  58.659  1.00 19.08 ? 464  ILE A N     1 
ATOM   3369  C  CA    . ILE A 1 444 ? -30.029 -5.860  57.815  1.00 18.63 ? 464  ILE A CA    1 
ATOM   3370  C  C     . ILE A 1 444 ? -30.832 -6.626  56.754  1.00 18.75 ? 464  ILE A C     1 
ATOM   3371  O  O     . ILE A 1 444 ? -30.273 -7.416  55.993  1.00 18.04 ? 464  ILE A O     1 
ATOM   3372  C  CB    . ILE A 1 444 ? -28.989 -4.930  57.158  1.00 18.82 ? 464  ILE A CB    1 
ATOM   3373  C  CG1   . ILE A 1 444 ? -28.052 -4.342  58.229  1.00 19.21 ? 464  ILE A CG1   1 
ATOM   3374  C  CG2   . ILE A 1 444 ? -29.678 -3.809  56.343  1.00 17.57 ? 464  ILE A CG2   1 
ATOM   3375  C  CD1   . ILE A 1 444 ? -27.025 -3.325  57.684  1.00 18.04 ? 464  ILE A CD1   1 
ATOM   3376  N  N     . TRP A 1 445 ? -32.144 -6.388  56.717  1.00 18.67 ? 465  TRP A N     1 
ATOM   3377  C  CA    . TRP A 1 445 ? -33.052 -7.130  55.850  1.00 18.40 ? 465  TRP A CA    1 
ATOM   3378  C  C     . TRP A 1 445 ? -33.564 -6.222  54.747  1.00 18.54 ? 465  TRP A C     1 
ATOM   3379  O  O     . TRP A 1 445 ? -34.246 -5.238  55.035  1.00 18.61 ? 465  TRP A O     1 
ATOM   3380  C  CB    . TRP A 1 445 ? -34.263 -7.627  56.648  1.00 18.32 ? 465  TRP A CB    1 
ATOM   3381  C  CG    . TRP A 1 445 ? -33.917 -8.498  57.800  1.00 18.76 ? 465  TRP A CG    1 
ATOM   3382  C  CD1   . TRP A 1 445 ? -33.873 -8.134  59.112  1.00 18.25 ? 465  TRP A CD1   1 
ATOM   3383  C  CD2   . TRP A 1 445 ? -33.573 -9.884  57.751  1.00 17.90 ? 465  TRP A CD2   1 
ATOM   3384  N  NE1   . TRP A 1 445 ? -33.520 -9.207  59.883  1.00 19.49 ? 465  TRP A NE1   1 
ATOM   3385  C  CE2   . TRP A 1 445 ? -33.333 -10.298 59.075  1.00 18.10 ? 465  TRP A CE2   1 
ATOM   3386  C  CE3   . TRP A 1 445 ? -33.448 -10.822 56.711  1.00 18.88 ? 465  TRP A CE3   1 
ATOM   3387  C  CZ2   . TRP A 1 445 ? -32.967 -11.615 59.401  1.00 17.45 ? 465  TRP A CZ2   1 
ATOM   3388  C  CZ3   . TRP A 1 445 ? -33.089 -12.147 57.039  1.00 18.63 ? 465  TRP A CZ3   1 
ATOM   3389  C  CH2   . TRP A 1 445 ? -32.861 -12.524 58.374  1.00 17.22 ? 465  TRP A CH2   1 
ATOM   3390  N  N     . ASP A 1 446 ? -33.259 -6.567  53.497  1.00 18.37 ? 466  ASP A N     1 
ATOM   3391  C  CA    . ASP A 1 446 ? -33.689 -5.787  52.347  1.00 18.62 ? 466  ASP A CA    1 
ATOM   3392  C  C     . ASP A 1 446 ? -34.596 -6.608  51.445  1.00 18.44 ? 466  ASP A C     1 
ATOM   3393  O  O     . ASP A 1 446 ? -34.387 -7.816  51.248  1.00 18.62 ? 466  ASP A O     1 
ATOM   3394  C  CB    . ASP A 1 446 ? -32.501 -5.345  51.482  1.00 18.65 ? 466  ASP A CB    1 
ATOM   3395  C  CG    . ASP A 1 446 ? -31.513 -4.463  52.210  1.00 19.23 ? 466  ASP A CG    1 
ATOM   3396  O  OD1   . ASP A 1 446 ? -31.778 -3.976  53.340  1.00 19.03 ? 466  ASP A OD1   1 
ATOM   3397  O  OD2   . ASP A 1 446 ? -30.441 -4.251  51.615  1.00 18.07 ? 466  ASP A OD2   1 
ATOM   3398  N  N     . PHE A 1 447 ? -35.595 -5.927  50.896  1.00 18.05 ? 467  PHE A N     1 
ATOM   3399  C  CA    . PHE A 1 447 ? -36.308 -6.387  49.728  1.00 17.74 ? 467  PHE A CA    1 
ATOM   3400  C  C     . PHE A 1 447 ? -36.130 -5.280  48.703  1.00 17.66 ? 467  PHE A C     1 
ATOM   3401  O  O     . PHE A 1 447 ? -36.383 -4.105  48.991  1.00 17.02 ? 467  PHE A O     1 
ATOM   3402  C  CB    . PHE A 1 447 ? -37.781 -6.653  50.050  1.00 18.02 ? 467  PHE A CB    1 
ATOM   3403  C  CG    . PHE A 1 447 ? -38.000 -7.902  50.880  1.00 19.38 ? 467  PHE A CG    1 
ATOM   3404  C  CD1   . PHE A 1 447 ? -38.529 -7.825  52.163  1.00 20.85 ? 467  PHE A CD1   1 
ATOM   3405  C  CD2   . PHE A 1 447 ? -37.656 -9.149  50.382  1.00 18.69 ? 467  PHE A CD2   1 
ATOM   3406  C  CE1   . PHE A 1 447 ? -38.738 -8.974  52.921  1.00 20.76 ? 467  PHE A CE1   1 
ATOM   3407  C  CE2   . PHE A 1 447 ? -37.842 -10.305 51.146  1.00 19.85 ? 467  PHE A CE2   1 
ATOM   3408  C  CZ    . PHE A 1 447 ? -38.385 -10.220 52.412  1.00 19.69 ? 467  PHE A CZ    1 
ATOM   3409  N  N     . ILE A 1 448 ? -35.664 -5.665  47.521  1.00 17.45 ? 468  ILE A N     1 
ATOM   3410  C  CA    . ILE A 1 448 ? -35.176 -4.740  46.524  1.00 17.97 ? 468  ILE A CA    1 
ATOM   3411  C  C     . ILE A 1 448 ? -35.965 -4.946  45.236  1.00 17.74 ? 468  ILE A C     1 
ATOM   3412  O  O     . ILE A 1 448 ? -36.194 -6.085  44.811  1.00 17.75 ? 468  ILE A O     1 
ATOM   3413  C  CB    . ILE A 1 448 ? -33.679 -5.003  46.257  1.00 18.11 ? 468  ILE A CB    1 
ATOM   3414  C  CG1   . ILE A 1 448 ? -32.850 -4.761  47.527  1.00 19.89 ? 468  ILE A CG1   1 
ATOM   3415  C  CG2   . ILE A 1 448 ? -33.172 -4.139  45.139  1.00 19.33 ? 468  ILE A CG2   1 
ATOM   3416  C  CD1   . ILE A 1 448 ? -31.477 -5.485  47.483  1.00 21.69 ? 468  ILE A CD1   1 
ATOM   3417  N  N     . PHE A 1 449 ? -36.356 -3.848  44.599  1.00 17.58 ? 469  PHE A N     1 
ATOM   3418  C  CA    . PHE A 1 449 ? -37.204 -3.920  43.418  1.00 17.72 ? 469  PHE A CA    1 
ATOM   3419  C  C     . PHE A 1 449 ? -36.592 -3.120  42.283  1.00 17.77 ? 469  PHE A C     1 
ATOM   3420  O  O     . PHE A 1 449 ? -36.370 -1.923  42.407  1.00 17.75 ? 469  PHE A O     1 
ATOM   3421  C  CB    . PHE A 1 449 ? -38.620 -3.424  43.742  1.00 17.79 ? 469  PHE A CB    1 
ATOM   3422  C  CG    . PHE A 1 449 ? -39.268 -4.160  44.879  1.00 16.73 ? 469  PHE A CG    1 
ATOM   3423  C  CD1   . PHE A 1 449 ? -39.043 -3.770  46.182  1.00 16.72 ? 469  PHE A CD1   1 
ATOM   3424  C  CD2   . PHE A 1 449 ? -40.098 -5.241  44.642  1.00 17.64 ? 469  PHE A CD2   1 
ATOM   3425  C  CE1   . PHE A 1 449 ? -39.636 -4.453  47.240  1.00 17.68 ? 469  PHE A CE1   1 
ATOM   3426  C  CE2   . PHE A 1 449 ? -40.678 -5.934  45.693  1.00 16.23 ? 469  PHE A CE2   1 
ATOM   3427  C  CZ    . PHE A 1 449 ? -40.453 -5.531  46.988  1.00 16.06 ? 469  PHE A CZ    1 
ATOM   3428  N  N     . TYR A 1 450 ? -36.307 -3.811  41.182  1.00 18.14 ? 470  TYR A N     1 
ATOM   3429  C  CA    . TYR A 1 450 ? -35.641 -3.227  40.027  1.00 17.98 ? 470  TYR A CA    1 
ATOM   3430  C  C     . TYR A 1 450 ? -36.709 -2.859  39.015  1.00 17.80 ? 470  TYR A C     1 
ATOM   3431  O  O     . TYR A 1 450 ? -37.746 -3.512  38.966  1.00 17.58 ? 470  TYR A O     1 
ATOM   3432  C  CB    . TYR A 1 450 ? -34.703 -4.228  39.381  1.00 18.20 ? 470  TYR A CB    1 
ATOM   3433  C  CG    . TYR A 1 450 ? -33.486 -4.631  40.183  1.00 19.09 ? 470  TYR A CG    1 
ATOM   3434  C  CD1   . TYR A 1 450 ? -33.582 -5.570  41.190  1.00 19.98 ? 470  TYR A CD1   1 
ATOM   3435  C  CD2   . TYR A 1 450 ? -32.223 -4.112  39.886  1.00 20.70 ? 470  TYR A CD2   1 
ATOM   3436  C  CE1   . TYR A 1 450 ? -32.465 -5.976  41.907  1.00 20.99 ? 470  TYR A CE1   1 
ATOM   3437  C  CE2   . TYR A 1 450 ? -31.084 -4.516  40.605  1.00 21.98 ? 470  TYR A CE2   1 
ATOM   3438  C  CZ    . TYR A 1 450 ? -31.220 -5.448  41.609  1.00 22.34 ? 470  TYR A CZ    1 
ATOM   3439  O  OH    . TYR A 1 450 ? -30.123 -5.878  42.319  1.00 23.34 ? 470  TYR A OH    1 
ATOM   3440  N  N     . PRO A 1 451 ? -36.469 -1.807  38.205  1.00 17.72 ? 471  PRO A N     1 
ATOM   3441  C  CA    . PRO A 1 451 ? -37.500 -1.321  37.279  1.00 17.70 ? 471  PRO A CA    1 
ATOM   3442  C  C     . PRO A 1 451 ? -37.883 -2.305  36.171  1.00 17.60 ? 471  PRO A C     1 
ATOM   3443  O  O     . PRO A 1 451 ? -38.929 -2.127  35.541  1.00 17.69 ? 471  PRO A O     1 
ATOM   3444  C  CB    . PRO A 1 451 ? -36.861 -0.056  36.684  1.00 17.62 ? 471  PRO A CB    1 
ATOM   3445  C  CG    . PRO A 1 451 ? -35.885 0.387   37.740  1.00 18.25 ? 471  PRO A CG    1 
ATOM   3446  C  CD    . PRO A 1 451 ? -35.301 -0.908  38.213  1.00 17.88 ? 471  PRO A CD    1 
ATOM   3447  N  N     . ASN A 1 452 ? -37.044 -3.323  35.941  1.00 17.52 ? 472  ASN A N     1 
ATOM   3448  C  CA    . ASN A 1 452 ? -37.333 -4.379  34.965  1.00 17.43 ? 472  ASN A CA    1 
ATOM   3449  C  C     . ASN A 1 452 ? -38.015 -5.634  35.544  1.00 17.36 ? 472  ASN A C     1 
ATOM   3450  O  O     . ASN A 1 452 ? -37.975 -6.699  34.929  1.00 17.44 ? 472  ASN A O     1 
ATOM   3451  C  CB    . ASN A 1 452 ? -36.054 -4.762  34.207  1.00 17.21 ? 472  ASN A CB    1 
ATOM   3452  C  CG    . ASN A 1 452 ? -35.062 -5.543  35.063  1.00 17.35 ? 472  ASN A CG    1 
ATOM   3453  O  OD1   . ASN A 1 452 ? -35.118 -5.506  36.297  1.00 16.69 ? 472  ASN A OD1   1 
ATOM   3454  N  ND2   . ASN A 1 452 ? -34.143 -6.248  34.404  1.00 12.96 ? 472  ASN A ND2   1 
ATOM   3455  N  N     . GLY A 1 453 ? -38.650 -5.519  36.707  1.00 17.15 ? 473  GLY A N     1 
ATOM   3456  C  CA    . GLY A 1 453 ? -39.458 -6.638  37.245  1.00 17.22 ? 473  GLY A CA    1 
ATOM   3457  C  C     . GLY A 1 453 ? -38.684 -7.695  38.038  1.00 16.89 ? 473  GLY A C     1 
ATOM   3458  O  O     . GLY A 1 453 ? -39.245 -8.721  38.443  1.00 16.58 ? 473  GLY A O     1 
ATOM   3459  N  N     . VAL A 1 454 ? -37.397 -7.442  38.253  1.00 16.68 ? 474  VAL A N     1 
ATOM   3460  C  CA    . VAL A 1 454 ? -36.572 -8.284  39.101  1.00 16.41 ? 474  VAL A CA    1 
ATOM   3461  C  C     . VAL A 1 454 ? -36.753 -7.831  40.556  1.00 16.99 ? 474  VAL A C     1 
ATOM   3462  O  O     . VAL A 1 454 ? -36.720 -6.636  40.847  1.00 16.79 ? 474  VAL A O     1 
ATOM   3463  C  CB    . VAL A 1 454 ? -35.084 -8.187  38.679  1.00 16.00 ? 474  VAL A CB    1 
ATOM   3464  C  CG1   . VAL A 1 454 ? -34.153 -8.924  39.674  1.00 15.19 ? 474  VAL A CG1   1 
ATOM   3465  C  CG2   . VAL A 1 454 ? -34.923 -8.738  37.273  1.00 15.92 ? 474  VAL A CG2   1 
ATOM   3466  N  N     A MET A 1 455 ? -36.952 -8.775  41.465  0.50 17.31 ? 475  MET A N     1 
ATOM   3467  N  N     B MET A 1 455 ? -36.977 -8.800  41.448  0.50 17.15 ? 475  MET A N     1 
ATOM   3468  C  CA    A MET A 1 455 ? -36.883 -8.441  42.877  0.50 17.76 ? 475  MET A CA    1 
ATOM   3469  C  CA    B MET A 1 455 ? -37.002 -8.573  42.899  0.50 17.46 ? 475  MET A CA    1 
ATOM   3470  C  C     A MET A 1 455 ? -35.898 -9.351  43.576  0.50 17.60 ? 475  MET A C     1 
ATOM   3471  C  C     B MET A 1 455 ? -35.805 -9.306  43.501  0.50 17.43 ? 475  MET A C     1 
ATOM   3472  O  O     A MET A 1 455 ? -35.680 -10.484 43.173  0.50 17.71 ? 475  MET A O     1 
ATOM   3473  O  O     B MET A 1 455 ? -35.314 -10.268 42.924  0.50 17.45 ? 475  MET A O     1 
ATOM   3474  C  CB    A MET A 1 455 ? -38.248 -8.487  43.555  0.50 17.92 ? 475  MET A CB    1 
ATOM   3475  C  CB    B MET A 1 455 ? -38.305 -9.093  43.527  0.50 17.53 ? 475  MET A CB    1 
ATOM   3476  C  CG    A MET A 1 455 ? -38.899 -9.835  43.582  0.50 18.98 ? 475  MET A CG    1 
ATOM   3477  C  CG    B MET A 1 455 ? -38.428 -8.843  45.037  0.50 17.84 ? 475  MET A CG    1 
ATOM   3478  S  SD    A MET A 1 455 ? -40.184 -9.834  44.834  0.50 21.03 ? 475  MET A SD    1 
ATOM   3479  S  SD    B MET A 1 455 ? -39.896 -9.562  45.813  0.50 19.85 ? 475  MET A SD    1 
ATOM   3480  C  CE    A MET A 1 455 ? -39.199 -10.000 46.325  0.50 20.70 ? 475  MET A CE    1 
ATOM   3481  C  CE    B MET A 1 455 ? -39.506 -9.420  47.550  0.50 19.07 ? 475  MET A CE    1 
ATOM   3482  N  N     . GLU A 1 456 ? -35.315 -8.829  44.637  1.00 17.55 ? 476  GLU A N     1 
ATOM   3483  C  CA    . GLU A 1 456 ? -34.202 -9.466  45.299  1.00 17.68 ? 476  GLU A CA    1 
ATOM   3484  C  C     . GLU A 1 456 ? -34.420 -9.367  46.783  1.00 17.53 ? 476  GLU A C     1 
ATOM   3485  O  O     . GLU A 1 456 ? -34.871 -8.337  47.267  1.00 17.61 ? 476  GLU A O     1 
ATOM   3486  C  CB    . GLU A 1 456 ? -32.915 -8.755  44.893  1.00 17.74 ? 476  GLU A CB    1 
ATOM   3487  C  CG    . GLU A 1 456 ? -31.708 -9.135  45.712  1.00 18.83 ? 476  GLU A CG    1 
ATOM   3488  C  CD    . GLU A 1 456 ? -30.427 -8.674  45.076  1.00 19.45 ? 476  GLU A CD    1 
ATOM   3489  O  OE1   . GLU A 1 456 ? -30.465 -7.781  44.197  1.00 19.81 ? 476  GLU A OE1   1 
ATOM   3490  O  OE2   . GLU A 1 456 ? -29.373 -9.208  45.465  1.00 22.75 ? 476  GLU A OE2   1 
ATOM   3491  N  N     . ALA A 1 457 ? -34.135 -10.455 47.491  1.00 17.58 ? 477  ALA A N     1 
ATOM   3492  C  CA    . ALA A 1 457 ? -34.119 -10.471 48.935  1.00 17.74 ? 477  ALA A CA    1 
ATOM   3493  C  C     . ALA A 1 457 ? -32.670 -10.587 49.366  1.00 18.48 ? 477  ALA A C     1 
ATOM   3494  O  O     . ALA A 1 457 ? -31.883 -11.288 48.737  1.00 17.64 ? 477  ALA A O     1 
ATOM   3495  C  CB    . ALA A 1 457 ? -34.915 -11.633 49.462  1.00 17.75 ? 477  ALA A CB    1 
ATOM   3496  N  N     . LYS A 1 458 ? -32.327 -9.902  50.454  1.00 19.32 ? 478  LYS A N     1 
ATOM   3497  C  CA    . LYS A 1 458 ? -30.954 -9.835  50.911  1.00 19.78 ? 478  LYS A CA    1 
ATOM   3498  C  C     . LYS A 1 458 ? -30.927 -9.708  52.437  1.00 19.70 ? 478  LYS A C     1 
ATOM   3499  O  O     . LYS A 1 458 ? -31.751 -9.002  53.041  1.00 19.32 ? 478  LYS A O     1 
ATOM   3500  C  CB    . LYS A 1 458 ? -30.282 -8.627  50.246  1.00 20.42 ? 478  LYS A CB    1 
ATOM   3501  C  CG    . LYS A 1 458 ? -28.766 -8.700  50.174  1.00 22.62 ? 478  LYS A CG    1 
ATOM   3502  C  CD    . LYS A 1 458 ? -28.155 -7.418  49.571  1.00 23.40 ? 478  LYS A CD    1 
ATOM   3503  C  CE    . LYS A 1 458 ? -28.399 -7.308  48.091  1.00 25.21 ? 478  LYS A CE    1 
ATOM   3504  N  NZ    . LYS A 1 458 ? -27.755 -6.105  47.475  1.00 25.69 ? 478  LYS A NZ    1 
ATOM   3505  N  N     . MET A 1 459 ? -30.017 -10.435 53.065  1.00 19.69 ? 479  MET A N     1 
ATOM   3506  C  CA    . MET A 1 459 ? -29.668 -10.195 54.452  1.00 19.93 ? 479  MET A CA    1 
ATOM   3507  C  C     . MET A 1 459 ? -28.187 -9.805  54.493  1.00 19.99 ? 479  MET A C     1 
ATOM   3508  O  O     . MET A 1 459 ? -27.375 -10.394 53.789  1.00 19.47 ? 479  MET A O     1 
ATOM   3509  C  CB    . MET A 1 459 ? -29.944 -11.450 55.278  1.00 20.35 ? 479  MET A CB    1 
ATOM   3510  C  CG    . MET A 1 459 ? -29.636 -11.352 56.766  1.00 21.68 ? 479  MET A CG    1 
ATOM   3511  S  SD    . MET A 1 459 ? -27.898 -11.685 57.204  1.00 26.24 ? 479  MET A SD    1 
ATOM   3512  C  CE    . MET A 1 459 ? -27.549 -13.262 56.434  1.00 26.74 ? 479  MET A CE    1 
ATOM   3513  N  N     . HIS A 1 460 ? -27.847 -8.796  55.291  1.00 20.20 ? 480  HIS A N     1 
ATOM   3514  C  CA    . HIS A 1 460 ? -26.444 -8.481  55.581  1.00 20.54 ? 480  HIS A CA    1 
ATOM   3515  C  C     . HIS A 1 460 ? -26.200 -8.684  57.065  1.00 20.32 ? 480  HIS A C     1 
ATOM   3516  O  O     . HIS A 1 460 ? -27.069 -8.368  57.872  1.00 21.57 ? 480  HIS A O     1 
ATOM   3517  C  CB    . HIS A 1 460 ? -26.093 -7.020  55.267  1.00 20.43 ? 480  HIS A CB    1 
ATOM   3518  C  CG    . HIS A 1 460 ? -26.688 -6.482  54.007  1.00 21.54 ? 480  HIS A CG    1 
ATOM   3519  N  ND1   . HIS A 1 460 ? -25.938 -6.258  52.871  1.00 21.27 ? 480  HIS A ND1   1 
ATOM   3520  C  CD2   . HIS A 1 460 ? -27.941 -6.052  53.726  1.00 21.53 ? 480  HIS A CD2   1 
ATOM   3521  C  CE1   . HIS A 1 460 ? -26.716 -5.747  51.934  1.00 23.37 ? 480  HIS A CE1   1 
ATOM   3522  N  NE2   . HIS A 1 460 ? -27.936 -5.606  52.429  1.00 22.63 ? 480  HIS A NE2   1 
ATOM   3523  N  N     . ALA A 1 461 ? -25.016 -9.158  57.430  1.00 19.90 ? 481  ALA A N     1 
ATOM   3524  C  CA    . ALA A 1 461 ? -24.636 -9.295  58.837  1.00 20.03 ? 481  ALA A CA    1 
ATOM   3525  C  C     . ALA A 1 461 ? -23.626 -8.230  59.264  1.00 19.95 ? 481  ALA A C     1 
ATOM   3526  O  O     . ALA A 1 461 ? -22.629 -7.995  58.571  1.00 19.90 ? 481  ALA A O     1 
ATOM   3527  C  CB    . ALA A 1 461 ? -24.063 -10.669 59.095  1.00 19.91 ? 481  ALA A CB    1 
ATOM   3528  N  N     . THR A 1 462 ? -23.892 -7.594  60.405  1.00 19.75 ? 482  THR A N     1 
ATOM   3529  C  CA    . THR A 1 462 ? -22.918 -6.732  61.061  1.00 19.73 ? 482  THR A CA    1 
ATOM   3530  C  C     . THR A 1 462 ? -23.126 -6.756  62.599  1.00 20.48 ? 482  THR A C     1 
ATOM   3531  O  O     . THR A 1 462 ? -23.819 -7.621  63.106  1.00 20.12 ? 482  THR A O     1 
ATOM   3532  C  CB    . THR A 1 462 ? -22.934 -5.305  60.440  1.00 19.76 ? 482  THR A CB    1 
ATOM   3533  O  OG1   . THR A 1 462 ? -21.899 -4.514  61.029  1.00 18.99 ? 482  THR A OG1   1 
ATOM   3534  C  CG2   . THR A 1 462 ? -24.295 -4.625  60.615  1.00 19.06 ? 482  THR A CG2   1 
ATOM   3535  N  N     . GLY A 1 463 ? -22.519 -5.842  63.355  1.00 20.77 ? 483  GLY A N     1 
ATOM   3536  C  CA    . GLY A 1 463 ? -22.631 -5.917  64.814  1.00 21.01 ? 483  GLY A CA    1 
ATOM   3537  C  C     . GLY A 1 463 ? -21.543 -6.798  65.396  1.00 20.91 ? 483  GLY A C     1 
ATOM   3538  O  O     . GLY A 1 463 ? -20.543 -7.071  64.725  1.00 21.35 ? 483  GLY A O     1 
ATOM   3539  N  N     . TYR A 1 464 ? -21.739 -7.255  66.631  1.00 20.83 ? 484  TYR A N     1 
ATOM   3540  C  CA    . TYR A 1 464 ? -20.707 -8.009  67.369  1.00 20.98 ? 484  TYR A CA    1 
ATOM   3541  C  C     . TYR A 1 464 ? -20.852 -9.519  67.212  1.00 20.94 ? 484  TYR A C     1 
ATOM   3542  O  O     . TYR A 1 464 ? -21.967 -10.038 67.284  1.00 20.43 ? 484  TYR A O     1 
ATOM   3543  C  CB    . TYR A 1 464 ? -20.794 -7.698  68.868  1.00 21.01 ? 484  TYR A CB    1 
ATOM   3544  C  CG    . TYR A 1 464 ? -20.367 -6.304  69.240  1.00 20.74 ? 484  TYR A CG    1 
ATOM   3545  C  CD1   . TYR A 1 464 ? -21.294 -5.269  69.295  1.00 19.97 ? 484  TYR A CD1   1 
ATOM   3546  C  CD2   . TYR A 1 464 ? -19.030 -6.021  69.541  1.00 19.56 ? 484  TYR A CD2   1 
ATOM   3547  C  CE1   . TYR A 1 464 ? -20.906 -3.976  69.629  1.00 21.44 ? 484  TYR A CE1   1 
ATOM   3548  C  CE2   . TYR A 1 464 ? -18.634 -4.739  69.877  1.00 20.69 ? 484  TYR A CE2   1 
ATOM   3549  C  CZ    . TYR A 1 464 ? -19.576 -3.721  69.926  1.00 20.70 ? 484  TYR A CZ    1 
ATOM   3550  O  OH    . TYR A 1 464 ? -19.203 -2.451  70.262  1.00 21.98 ? 484  TYR A OH    1 
ATOM   3551  N  N     . VAL A 1 465 ? -19.726 -10.220 67.046  1.00 20.75 ? 485  VAL A N     1 
ATOM   3552  C  CA    . VAL A 1 465 ? -19.727 -11.695 67.027  1.00 20.77 ? 485  VAL A CA    1 
ATOM   3553  C  C     . VAL A 1 465 ? -20.039 -12.283 68.413  1.00 21.71 ? 485  VAL A C     1 
ATOM   3554  O  O     . VAL A 1 465 ? -19.852 -11.628 69.438  1.00 21.77 ? 485  VAL A O     1 
ATOM   3555  C  CB    . VAL A 1 465 ? -18.370 -12.303 66.524  1.00 20.77 ? 485  VAL A CB    1 
ATOM   3556  C  CG1   . VAL A 1 465 ? -18.029 -11.799 65.124  1.00 19.90 ? 485  VAL A CG1   1 
ATOM   3557  C  CG2   . VAL A 1 465 ? -17.225 -12.022 67.495  1.00 19.34 ? 485  VAL A CG2   1 
ATOM   3558  N  N     . HIS A 1 466 ? -20.541 -13.515 68.413  1.00 22.41 ? 486  HIS A N     1 
ATOM   3559  C  CA    . HIS A 1 466 ? -20.728 -14.324 69.614  1.00 22.90 ? 486  HIS A CA    1 
ATOM   3560  C  C     . HIS A 1 466 ? -19.373 -14.953 69.944  1.00 23.43 ? 486  HIS A C     1 
ATOM   3561  O  O     . HIS A 1 466 ? -18.817 -15.700 69.131  1.00 23.71 ? 486  HIS A O     1 
ATOM   3562  C  CB    . HIS A 1 466 ? -21.773 -15.404 69.324  1.00 22.86 ? 486  HIS A CB    1 
ATOM   3563  C  CG    . HIS A 1 466 ? -22.148 -16.245 70.501  1.00 22.39 ? 486  HIS A CG    1 
ATOM   3564  N  ND1   . HIS A 1 466 ? -22.630 -15.715 71.677  1.00 22.39 ? 486  HIS A ND1   1 
ATOM   3565  C  CD2   . HIS A 1 466 ? -22.159 -17.590 70.662  1.00 22.56 ? 486  HIS A CD2   1 
ATOM   3566  C  CE1   . HIS A 1 466 ? -22.906 -16.695 72.519  1.00 22.46 ? 486  HIS A CE1   1 
ATOM   3567  N  NE2   . HIS A 1 466 ? -22.631 -17.844 71.926  1.00 21.73 ? 486  HIS A NE2   1 
ATOM   3568  N  N     . ALA A 1 467 ? -18.846 -14.651 71.130  1.00 23.82 ? 487  ALA A N     1 
ATOM   3569  C  CA    . ALA A 1 467 ? -17.444 -14.933 71.445  1.00 23.88 ? 487  ALA A CA    1 
ATOM   3570  C  C     . ALA A 1 467 ? -17.294 -15.493 72.851  1.00 24.11 ? 487  ALA A C     1 
ATOM   3571  O  O     . ALA A 1 467 ? -18.090 -15.183 73.734  1.00 23.69 ? 487  ALA A O     1 
ATOM   3572  C  CB    . ALA A 1 467 ? -16.620 -13.662 71.297  1.00 23.46 ? 487  ALA A CB    1 
ATOM   3573  N  N     . THR A 1 468 ? -16.251 -16.299 73.047  1.00 24.51 ? 488  THR A N     1 
ATOM   3574  C  CA    . THR A 1 468 ? -15.984 -16.951 74.336  1.00 24.52 ? 488  THR A CA    1 
ATOM   3575  C  C     . THR A 1 468 ? -14.539 -16.722 74.787  1.00 24.83 ? 488  THR A C     1 
ATOM   3576  O  O     . THR A 1 468 ? -13.714 -16.169 74.041  1.00 24.16 ? 488  THR A O     1 
ATOM   3577  C  CB    . THR A 1 468 ? -16.307 -18.470 74.283  1.00 24.75 ? 488  THR A CB    1 
ATOM   3578  O  OG1   . THR A 1 468 ? -15.630 -19.086 73.178  1.00 24.05 ? 488  THR A OG1   1 
ATOM   3579  C  CG2   . THR A 1 468 ? -17.830 -18.699 74.151  1.00 24.02 ? 488  THR A CG2   1 
ATOM   3580  N  N     . PHE A 1 469 ? -14.249 -17.137 76.018  1.00 25.27 ? 489  PHE A N     1 
ATOM   3581  C  CA    . PHE A 1 469 ? -12.936 -16.919 76.626  1.00 25.67 ? 489  PHE A CA    1 
ATOM   3582  C  C     . PHE A 1 469 ? -11.889 -17.756 75.936  1.00 26.00 ? 489  PHE A C     1 
ATOM   3583  O  O     . PHE A 1 469 ? -12.103 -18.942 75.716  1.00 25.92 ? 489  PHE A O     1 
ATOM   3584  C  CB    . PHE A 1 469 ? -12.968 -17.299 78.105  1.00 25.64 ? 489  PHE A CB    1 
ATOM   3585  C  CG    . PHE A 1 469 ? -11.719 -16.928 78.864  1.00 25.98 ? 489  PHE A CG    1 
ATOM   3586  C  CD1   . PHE A 1 469 ? -11.413 -15.591 79.113  1.00 26.47 ? 489  PHE A CD1   1 
ATOM   3587  C  CD2   . PHE A 1 469 ? -10.877 -17.912 79.379  1.00 26.01 ? 489  PHE A CD2   1 
ATOM   3588  C  CE1   . PHE A 1 469 ? -10.274 -15.244 79.834  1.00 26.30 ? 489  PHE A CE1   1 
ATOM   3589  C  CE2   . PHE A 1 469 ? -9.734  -17.563 80.112  1.00 25.35 ? 489  PHE A CE2   1 
ATOM   3590  C  CZ    . PHE A 1 469 ? -9.434  -16.240 80.332  1.00 25.14 ? 489  PHE A CZ    1 
ATOM   3591  N  N     . TYR A 1 470 ? -10.756 -17.139 75.614  1.00 26.87 ? 490  TYR A N     1 
ATOM   3592  C  CA    . TYR A 1 470 ? -9.656  -17.847 74.945  1.00 27.66 ? 490  TYR A CA    1 
ATOM   3593  C  C     . TYR A 1 470 ? -8.981  -18.859 75.859  1.00 28.09 ? 490  TYR A C     1 
ATOM   3594  O  O     . TYR A 1 470 ? -8.597  -18.543 76.977  1.00 28.24 ? 490  TYR A O     1 
ATOM   3595  C  CB    . TYR A 1 470 ? -8.587  -16.882 74.416  1.00 27.38 ? 490  TYR A CB    1 
ATOM   3596  C  CG    . TYR A 1 470 ? -7.321  -17.599 74.004  1.00 28.53 ? 490  TYR A CG    1 
ATOM   3597  C  CD1   . TYR A 1 470 ? -6.211  -17.648 74.852  1.00 29.64 ? 490  TYR A CD1   1 
ATOM   3598  C  CD2   . TYR A 1 470 ? -7.246  -18.272 72.787  1.00 29.21 ? 490  TYR A CD2   1 
ATOM   3599  C  CE1   . TYR A 1 470 ? -5.062  -18.331 74.487  1.00 29.74 ? 490  TYR A CE1   1 
ATOM   3600  C  CE2   . TYR A 1 470 ? -6.102  -18.948 72.410  1.00 29.39 ? 490  TYR A CE2   1 
ATOM   3601  C  CZ    . TYR A 1 470 ? -5.013  -18.979 73.264  1.00 30.15 ? 490  TYR A CZ    1 
ATOM   3602  O  OH    . TYR A 1 470 ? -3.874  -19.648 72.881  1.00 30.53 ? 490  TYR A OH    1 
ATOM   3603  N  N     . THR A 1 471 ? -8.872  -20.084 75.364  1.00 29.15 ? 491  THR A N     1 
ATOM   3604  C  CA    . THR A 1 471 ? -7.881  -21.047 75.832  1.00 29.77 ? 491  THR A CA    1 
ATOM   3605  C  C     . THR A 1 471 ? -7.348  -21.691 74.557  1.00 30.49 ? 491  THR A C     1 
ATOM   3606  O  O     . THR A 1 471 ? -8.022  -21.613 73.527  1.00 30.49 ? 491  THR A O     1 
ATOM   3607  C  CB    . THR A 1 471 ? -8.489  -22.147 76.694  1.00 29.85 ? 491  THR A CB    1 
ATOM   3608  O  OG1   . THR A 1 471 ? -9.146  -23.093 75.843  1.00 29.51 ? 491  THR A OG1   1 
ATOM   3609  C  CG2   . THR A 1 471 ? -9.485  -21.579 77.715  1.00 29.02 ? 491  THR A CG2   1 
ATOM   3610  N  N     . PRO A 1 472 ? -6.160  -22.337 74.617  1.00 31.04 ? 492  PRO A N     1 
ATOM   3611  C  CA    . PRO A 1 472 ? -5.571  -22.992 73.441  1.00 31.40 ? 492  PRO A CA    1 
ATOM   3612  C  C     . PRO A 1 472 ? -6.497  -23.989 72.741  1.00 31.77 ? 492  PRO A C     1 
ATOM   3613  O  O     . PRO A 1 472 ? -6.507  -24.060 71.516  1.00 31.97 ? 492  PRO A O     1 
ATOM   3614  C  CB    . PRO A 1 472 ? -4.343  -23.700 74.016  1.00 31.53 ? 492  PRO A CB    1 
ATOM   3615  C  CG    . PRO A 1 472 ? -3.929  -22.835 75.162  1.00 31.13 ? 492  PRO A CG    1 
ATOM   3616  C  CD    . PRO A 1 472 ? -5.235  -22.356 75.767  1.00 31.18 ? 492  PRO A CD    1 
ATOM   3617  N  N     . GLU A 1 473 ? -7.283  -24.725 73.522  1.00 32.12 ? 493  GLU A N     1 
ATOM   3618  C  CA    . GLU A 1 473 ? -8.268  -25.675 72.995  1.00 32.27 ? 493  GLU A CA    1 
ATOM   3619  C  C     . GLU A 1 473 ? -9.357  -25.005 72.150  1.00 31.55 ? 493  GLU A C     1 
ATOM   3620  O  O     . GLU A 1 473 ? -10.005 -25.660 71.335  1.00 31.58 ? 493  GLU A O     1 
ATOM   3621  C  CB    . GLU A 1 473 ? -8.933  -26.450 74.145  1.00 32.86 ? 493  GLU A CB    1 
ATOM   3622  C  CG    . GLU A 1 473 ? -8.067  -27.548 74.778  1.00 34.94 ? 493  GLU A CG    1 
ATOM   3623  C  CD    . GLU A 1 473 ? -7.055  -27.038 75.797  1.00 38.58 ? 493  GLU A CD    1 
ATOM   3624  O  OE1   . GLU A 1 473 ? -7.297  -25.985 76.434  1.00 40.27 ? 493  GLU A OE1   1 
ATOM   3625  O  OE2   . GLU A 1 473 ? -6.012  -27.712 75.976  1.00 40.83 ? 493  GLU A OE2   1 
ATOM   3626  N  N     . GLY A 1 474 ? -9.569  -23.708 72.360  1.00 30.89 ? 494  GLY A N     1 
ATOM   3627  C  CA    . GLY A 1 474 ? -10.525 -22.933 71.572  1.00 30.06 ? 494  GLY A CA    1 
ATOM   3628  C  C     . GLY A 1 474 ? -10.198 -22.819 70.098  1.00 29.44 ? 494  GLY A C     1 
ATOM   3629  O  O     . GLY A 1 474 ? -11.099 -22.628 69.274  1.00 28.95 ? 494  GLY A O     1 
ATOM   3630  N  N     . LEU A 1 475 ? -8.918  -22.956 69.757  1.00 28.55 ? 495  LEU A N     1 
ATOM   3631  C  CA    . LEU A 1 475 ? -8.480  -22.829 68.365  1.00 27.87 ? 495  LEU A CA    1 
ATOM   3632  C  C     . LEU A 1 475 ? -9.014  -23.939 67.444  1.00 27.28 ? 495  LEU A C     1 
ATOM   3633  O  O     . LEU A 1 475 ? -9.029  -23.778 66.230  1.00 27.72 ? 495  LEU A O     1 
ATOM   3634  C  CB    . LEU A 1 475 ? -6.951  -22.722 68.298  1.00 27.80 ? 495  LEU A CB    1 
ATOM   3635  C  CG    . LEU A 1 475 ? -6.357  -21.520 69.049  1.00 27.82 ? 495  LEU A CG    1 
ATOM   3636  C  CD1   . LEU A 1 475 ? -4.852  -21.440 68.854  1.00 28.09 ? 495  LEU A CD1   1 
ATOM   3637  C  CD2   . LEU A 1 475 ? -7.007  -20.217 68.601  1.00 28.35 ? 495  LEU A CD2   1 
ATOM   3638  N  N     . ARG A 1 476 ? -9.484  -25.045 68.009  1.00 26.64 ? 496  ARG A N     1 
ATOM   3639  C  CA    . ARG A 1 476 ? -10.161 -26.071 67.221  1.00 26.70 ? 496  ARG A CA    1 
ATOM   3640  C  C     . ARG A 1 476 ? -11.623 -25.710 66.872  1.00 25.94 ? 496  ARG A C     1 
ATOM   3641  O  O     . ARG A 1 476 ? -12.274 -26.437 66.133  1.00 25.11 ? 496  ARG A O     1 
ATOM   3642  C  CB    . ARG A 1 476 ? -10.153 -27.410 67.957  1.00 27.05 ? 496  ARG A CB    1 
ATOM   3643  C  CG    . ARG A 1 476 ? -8.762  -28.023 68.132  1.00 29.22 ? 496  ARG A CG    1 
ATOM   3644  C  CD    . ARG A 1 476 ? -8.810  -29.452 68.708  1.00 31.31 ? 496  ARG A CD    1 
ATOM   3645  N  NE    . ARG A 1 476 ? -9.673  -30.341 67.919  1.00 33.11 ? 496  ARG A NE    1 
ATOM   3646  C  CZ    . ARG A 1 476 ? -10.869 -30.800 68.297  1.00 33.92 ? 496  ARG A CZ    1 
ATOM   3647  N  NH1   . ARG A 1 476 ? -11.383 -30.494 69.482  1.00 34.80 ? 496  ARG A NH1   1 
ATOM   3648  N  NH2   . ARG A 1 476 ? -11.558 -31.589 67.480  1.00 34.20 ? 496  ARG A NH2   1 
ATOM   3649  N  N     . HIS A 1 477 ? -12.134 -24.612 67.420  1.00 25.26 ? 497  HIS A N     1 
ATOM   3650  C  CA    . HIS A 1 477 ? -13.531 -24.236 67.233  1.00 25.04 ? 497  HIS A CA    1 
ATOM   3651  C  C     . HIS A 1 477 ? -13.709 -22.749 66.925  1.00 24.88 ? 497  HIS A C     1 
ATOM   3652  O  O     . HIS A 1 477 ? -14.800 -22.201 67.117  1.00 24.58 ? 497  HIS A O     1 
ATOM   3653  C  CB    . HIS A 1 477 ? -14.329 -24.591 68.480  1.00 24.90 ? 497  HIS A CB    1 
ATOM   3654  C  CG    . HIS A 1 477 ? -14.201 -26.022 68.893  1.00 25.17 ? 497  HIS A CG    1 
ATOM   3655  N  ND1   . HIS A 1 477 ? -14.994 -27.021 68.369  1.00 24.88 ? 497  HIS A ND1   1 
ATOM   3656  C  CD2   . HIS A 1 477 ? -13.385 -26.622 69.792  1.00 24.80 ? 497  HIS A CD2   1 
ATOM   3657  C  CE1   . HIS A 1 477 ? -14.672 -28.172 68.927  1.00 24.26 ? 497  HIS A CE1   1 
ATOM   3658  N  NE2   . HIS A 1 477 ? -13.692 -27.961 69.786  1.00 23.80 ? 497  HIS A NE2   1 
ATOM   3659  N  N     . GLY A 1 478 ? -12.651 -22.109 66.431  1.00 24.69 ? 498  GLY A N     1 
ATOM   3660  C  CA    . GLY A 1 478 ? -12.656 -20.666 66.224  1.00 25.04 ? 498  GLY A CA    1 
ATOM   3661  C  C     . GLY A 1 478 ? -11.271 -20.021 66.168  1.00 25.10 ? 498  GLY A C     1 
ATOM   3662  O  O     . GLY A 1 478 ? -10.255 -20.697 66.012  1.00 24.78 ? 498  GLY A O     1 
ATOM   3663  N  N     . THR A 1 479 ? -11.258 -18.697 66.304  1.00 25.30 ? 499  THR A N     1 
ATOM   3664  C  CA    . THR A 1 479 ? -10.080 -17.883 66.062  1.00 25.21 ? 499  THR A CA    1 
ATOM   3665  C  C     . THR A 1 479 ? -9.850  -16.923 67.213  1.00 25.43 ? 499  THR A C     1 
ATOM   3666  O  O     . THR A 1 479 ? -10.793 -16.290 67.688  1.00 25.28 ? 499  THR A O     1 
ATOM   3667  C  CB    . THR A 1 479 ? -10.269 -17.040 64.782  1.00 25.18 ? 499  THR A CB    1 
ATOM   3668  O  OG1   . THR A 1 479 ? -10.618 -17.899 63.692  1.00 24.50 ? 499  THR A OG1   1 
ATOM   3669  C  CG2   . THR A 1 479 ? -8.998  -16.253 64.443  1.00 24.02 ? 499  THR A CG2   1 
ATOM   3670  N  N     . ARG A 1 480 ? -8.596  -16.817 67.650  1.00 25.58 ? 500  ARG A N     1 
ATOM   3671  C  CA    . ARG A 1 480 ? -8.197  -15.812 68.638  1.00 25.58 ? 500  ARG A CA    1 
ATOM   3672  C  C     . ARG A 1 480 ? -8.236  -14.428 68.015  1.00 25.18 ? 500  ARG A C     1 
ATOM   3673  O  O     . ARG A 1 480 ? -7.540  -14.165 67.025  1.00 24.53 ? 500  ARG A O     1 
ATOM   3674  C  CB    . ARG A 1 480 ? -6.790  -16.095 69.172  1.00 25.91 ? 500  ARG A CB    1 
ATOM   3675  C  CG    . ARG A 1 480 ? -6.456  -15.299 70.418  1.00 27.17 ? 500  ARG A CG    1 
ATOM   3676  C  CD    . ARG A 1 480 ? -5.067  -15.620 70.919  1.00 27.78 ? 500  ARG A CD    1 
ATOM   3677  N  NE    . ARG A 1 480 ? -4.823  -15.042 72.230  1.00 29.40 ? 500  ARG A NE    1 
ATOM   3678  C  CZ    . ARG A 1 480 ? -3.746  -15.286 72.982  1.00 30.59 ? 500  ARG A CZ    1 
ATOM   3679  N  NH1   . ARG A 1 480 ? -2.786  -16.103 72.564  1.00 29.71 ? 500  ARG A NH1   1 
ATOM   3680  N  NH2   . ARG A 1 480 ? -3.632  -14.703 74.166  1.00 30.52 ? 500  ARG A NH2   1 
ATOM   3681  N  N     . LEU A 1 481 ? -9.047  -13.545 68.599  1.00 24.89 ? 501  LEU A N     1 
ATOM   3682  C  CA    . LEU A 1 481 ? -9.276  -12.202 68.046  1.00 24.98 ? 501  LEU A CA    1 
ATOM   3683  C  C     . LEU A 1 481 ? -8.686  -11.096 68.895  1.00 25.22 ? 501  LEU A C     1 
ATOM   3684  O  O     . LEU A 1 481 ? -8.480  -9.963  68.423  1.00 25.48 ? 501  LEU A O     1 
ATOM   3685  C  CB    . LEU A 1 481 ? -10.775 -11.959 67.908  1.00 24.87 ? 501  LEU A CB    1 
ATOM   3686  C  CG    . LEU A 1 481 ? -11.535 -13.025 67.123  1.00 24.60 ? 501  LEU A CG    1 
ATOM   3687  C  CD1   . LEU A 1 481 ? -13.021 -12.688 67.078  1.00 24.40 ? 501  LEU A CD1   1 
ATOM   3688  C  CD2   . LEU A 1 481 ? -10.946 -13.151 65.721  1.00 25.03 ? 501  LEU A CD2   1 
ATOM   3689  N  N     . HIS A 1 482 ? -8.456  -11.417 70.163  1.00 25.53 ? 502  HIS A N     1 
ATOM   3690  C  CA    . HIS A 1 482 ? -7.825  -10.509 71.108  1.00 25.56 ? 502  HIS A CA    1 
ATOM   3691  C  C     . HIS A 1 482 ? -7.182  -11.367 72.191  1.00 25.39 ? 502  HIS A C     1 
ATOM   3692  O  O     . HIS A 1 482 ? -7.213  -12.594 72.096  1.00 24.82 ? 502  HIS A O     1 
ATOM   3693  C  CB    . HIS A 1 482 ? -8.851  -9.532  71.696  1.00 25.61 ? 502  HIS A CB    1 
ATOM   3694  C  CG    . HIS A 1 482 ? -8.264  -8.204  72.061  1.00 26.82 ? 502  HIS A CG    1 
ATOM   3695  N  ND1   . HIS A 1 482 ? -7.794  -7.919  73.329  1.00 25.71 ? 502  HIS A ND1   1 
ATOM   3696  C  CD2   . HIS A 1 482 ? -8.039  -7.094  71.316  1.00 26.46 ? 502  HIS A CD2   1 
ATOM   3697  C  CE1   . HIS A 1 482 ? -7.326  -6.683  73.351  1.00 25.32 ? 502  HIS A CE1   1 
ATOM   3698  N  NE2   . HIS A 1 482 ? -7.467  -6.159  72.145  1.00 26.28 ? 502  HIS A NE2   1 
ATOM   3699  N  N     . THR A 1 483 ? -6.594  -10.723 73.201  1.00 25.75 ? 503  THR A N     1 
ATOM   3700  C  CA    . THR A 1 483 ? -5.796  -11.412 74.221  1.00 25.74 ? 503  THR A CA    1 
ATOM   3701  C  C     . THR A 1 483 ? -6.572  -12.557 74.860  1.00 25.59 ? 503  THR A C     1 
ATOM   3702  O  O     . THR A 1 483 ? -6.090  -13.683 74.887  1.00 25.91 ? 503  THR A O     1 
ATOM   3703  C  CB    . THR A 1 483 ? -5.293  -10.431 75.320  1.00 26.06 ? 503  THR A CB    1 
ATOM   3704  O  OG1   . THR A 1 483 ? -4.669  -9.298  74.707  1.00 27.30 ? 503  THR A OG1   1 
ATOM   3705  C  CG2   . THR A 1 483 ? -4.281  -11.106 76.253  1.00 25.01 ? 503  THR A CG2   1 
ATOM   3706  N  N     . HIS A 1 484 ? -7.787  -12.280 75.317  1.00 25.72 ? 504  HIS A N     1 
ATOM   3707  C  CA    . HIS A 1 484 ? -8.607  -13.274 76.022  1.00 25.79 ? 504  HIS A CA    1 
ATOM   3708  C  C     . HIS A 1 484 ? -9.857  -13.713 75.252  1.00 25.04 ? 504  HIS A C     1 
ATOM   3709  O  O     . HIS A 1 484 ? -10.791 -14.256 75.848  1.00 24.56 ? 504  HIS A O     1 
ATOM   3710  C  CB    . HIS A 1 484 ? -9.043  -12.709 77.390  1.00 26.41 ? 504  HIS A CB    1 
ATOM   3711  C  CG    . HIS A 1 484 ? -7.909  -12.231 78.246  1.00 27.96 ? 504  HIS A CG    1 
ATOM   3712  N  ND1   . HIS A 1 484 ? -6.973  -13.086 78.792  1.00 30.67 ? 504  HIS A ND1   1 
ATOM   3713  C  CD2   . HIS A 1 484 ? -7.566  -10.986 78.658  1.00 29.30 ? 504  HIS A CD2   1 
ATOM   3714  C  CE1   . HIS A 1 484 ? -6.103  -12.388 79.503  1.00 29.89 ? 504  HIS A CE1   1 
ATOM   3715  N  NE2   . HIS A 1 484 ? -6.444  -11.112 79.440  1.00 29.23 ? 504  HIS A NE2   1 
ATOM   3716  N  N     . LEU A 1 485 ? -9.869  -13.519 73.934  1.00 24.44 ? 505  LEU A N     1 
ATOM   3717  C  CA    . LEU A 1 485 ? -11.107 -13.645 73.155  1.00 24.01 ? 505  LEU A CA    1 
ATOM   3718  C  C     . LEU A 1 485 ? -10.999 -14.649 72.005  1.00 23.91 ? 505  LEU A C     1 
ATOM   3719  O  O     . LEU A 1 485 ? -10.073 -14.578 71.199  1.00 22.97 ? 505  LEU A O     1 
ATOM   3720  C  CB    . LEU A 1 485 ? -11.475 -12.278 72.585  1.00 23.78 ? 505  LEU A CB    1 
ATOM   3721  C  CG    . LEU A 1 485 ? -12.869 -12.119 71.969  1.00 24.09 ? 505  LEU A CG    1 
ATOM   3722  C  CD1   . LEU A 1 485 ? -13.983 -12.352 73.010  1.00 22.57 ? 505  LEU A CD1   1 
ATOM   3723  C  CD2   . LEU A 1 485 ? -12.980 -10.733 71.328  1.00 22.31 ? 505  LEU A CD2   1 
ATOM   3724  N  N     . ILE A 1 486 ? -11.963 -15.569 71.935  1.00 23.72 ? 506  ILE A N     1 
ATOM   3725  C  CA    . ILE A 1 486 ? -12.114 -16.472 70.780  1.00 23.54 ? 506  ILE A CA    1 
ATOM   3726  C  C     . ILE A 1 486 ? -13.413 -16.151 70.069  1.00 23.09 ? 506  ILE A C     1 
ATOM   3727  O  O     . ILE A 1 486 ? -14.471 -16.054 70.702  1.00 23.11 ? 506  ILE A O     1 
ATOM   3728  C  CB    . ILE A 1 486 ? -12.160 -17.965 71.181  1.00 23.65 ? 506  ILE A CB    1 
ATOM   3729  C  CG1   . ILE A 1 486 ? -10.757 -18.484 71.506  1.00 24.59 ? 506  ILE A CG1   1 
ATOM   3730  C  CG2   . ILE A 1 486 ? -12.749 -18.815 70.058  1.00 23.92 ? 506  ILE A CG2   1 
ATOM   3731  C  CD1   . ILE A 1 486 ? -10.021 -19.042 70.335  1.00 25.12 ? 506  ILE A CD1   1 
ATOM   3732  N  N     . GLY A 1 487 ? -13.326 -15.961 68.760  1.00 22.36 ? 507  GLY A N     1 
ATOM   3733  C  CA    . GLY A 1 487 ? -14.513 -15.905 67.925  1.00 21.93 ? 507  GLY A CA    1 
ATOM   3734  C  C     . GLY A 1 487 ? -14.861 -17.308 67.485  1.00 21.30 ? 507  GLY A C     1 
ATOM   3735  O  O     . GLY A 1 487 ? -14.154 -17.894 66.672  1.00 21.70 ? 507  GLY A O     1 
ATOM   3736  N  N     . ASN A 1 488 ? -15.947 -17.846 68.024  1.00 20.76 ? 508  ASN A N     1 
ATOM   3737  C  CA    . ASN A 1 488 ? -16.394 -19.204 67.709  1.00 20.34 ? 508  ASN A CA    1 
ATOM   3738  C  C     . ASN A 1 488 ? -16.829 -19.367 66.265  1.00 20.54 ? 508  ASN A C     1 
ATOM   3739  O  O     . ASN A 1 488 ? -17.501 -18.476 65.707  1.00 20.62 ? 508  ASN A O     1 
ATOM   3740  C  CB    . ASN A 1 488 ? -17.565 -19.612 68.616  1.00 20.33 ? 508  ASN A CB    1 
ATOM   3741  C  CG    . ASN A 1 488 ? -17.175 -19.658 70.091  1.00 19.84 ? 508  ASN A CG    1 
ATOM   3742  O  OD1   . ASN A 1 488 ? -16.725 -18.665 70.651  1.00 20.29 ? 508  ASN A OD1   1 
ATOM   3743  N  ND2   . ASN A 1 488 ? -17.345 -20.807 70.714  1.00 19.23 ? 508  ASN A ND2   1 
ATOM   3744  N  N     . ILE A 1 489 ? -16.446 -20.501 65.674  1.00 20.30 ? 509  ILE A N     1 
ATOM   3745  C  CA    . ILE A 1 489 ? -16.917 -20.903 64.355  1.00 20.41 ? 509  ILE A CA    1 
ATOM   3746  C  C     . ILE A 1 489 ? -18.424 -21.115 64.404  1.00 20.38 ? 509  ILE A C     1 
ATOM   3747  O  O     . ILE A 1 489 ? -18.956 -21.620 65.394  1.00 20.50 ? 509  ILE A O     1 
ATOM   3748  C  CB    . ILE A 1 489 ? -16.228 -22.208 63.867  1.00 20.71 ? 509  ILE A CB    1 
ATOM   3749  C  CG1   . ILE A 1 489 ? -16.486 -22.430 62.369  1.00 21.28 ? 509  ILE A CG1   1 
ATOM   3750  C  CG2   . ILE A 1 489 ? -16.679 -23.414 64.686  1.00 19.56 ? 509  ILE A CG2   1 
ATOM   3751  C  CD1   . ILE A 1 489 ? -15.715 -23.630 61.767  1.00 20.77 ? 509  ILE A CD1   1 
ATOM   3752  N  N     . HIS A 1 490 ? -19.104 -20.699 63.341  1.00 19.97 ? 510  HIS A N     1 
ATOM   3753  C  CA    . HIS A 1 490 ? -20.541 -20.870 63.232  1.00 19.66 ? 510  HIS A CA    1 
ATOM   3754  C  C     . HIS A 1 490 ? -21.008 -20.744 61.799  1.00 19.92 ? 510  HIS A C     1 
ATOM   3755  O  O     . HIS A 1 490 ? -20.282 -20.263 60.933  1.00 19.86 ? 510  HIS A O     1 
ATOM   3756  C  CB    . HIS A 1 490 ? -21.276 -19.829 64.093  1.00 19.66 ? 510  HIS A CB    1 
ATOM   3757  C  CG    . HIS A 1 490 ? -20.965 -18.410 63.727  1.00 19.09 ? 510  HIS A CG    1 
ATOM   3758  N  ND1   . HIS A 1 490 ? -19.748 -17.824 63.996  1.00 18.03 ? 510  HIS A ND1   1 
ATOM   3759  C  CD2   . HIS A 1 490 ? -21.711 -17.462 63.106  1.00 20.09 ? 510  HIS A CD2   1 
ATOM   3760  C  CE1   . HIS A 1 490 ? -19.756 -16.577 63.559  1.00 19.46 ? 510  HIS A CE1   1 
ATOM   3761  N  NE2   . HIS A 1 490 ? -20.938 -16.328 63.017  1.00 18.88 ? 510  HIS A NE2   1 
ATOM   3762  N  N     . THR A 1 491 ? -22.246 -21.155 61.568  1.00 20.21 ? 511  THR A N     1 
ATOM   3763  C  CA    . THR A 1 491 ? -22.884 -20.974 60.283  1.00 20.41 ? 511  THR A CA    1 
ATOM   3764  C  C     . THR A 1 491 ? -24.170 -20.195 60.484  1.00 20.74 ? 511  THR A C     1 
ATOM   3765  O  O     . THR A 1 491 ? -24.984 -20.540 61.349  1.00 20.84 ? 511  THR A O     1 
ATOM   3766  C  CB    . THR A 1 491 ? -23.175 -22.336 59.622  1.00 20.67 ? 511  THR A CB    1 
ATOM   3767  O  OG1   . THR A 1 491 ? -21.936 -23.029 59.421  1.00 20.93 ? 511  THR A OG1   1 
ATOM   3768  C  CG2   . THR A 1 491 ? -23.874 -22.170 58.281  1.00 20.99 ? 511  THR A CG2   1 
ATOM   3769  N  N     . HIS A 1 492 ? -24.330 -19.135 59.690  1.00 20.47 ? 512  HIS A N     1 
ATOM   3770  C  CA    . HIS A 1 492 ? -25.575 -18.400 59.590  1.00 20.36 ? 512  HIS A CA    1 
ATOM   3771  C  C     . HIS A 1 492 ? -26.433 -19.092 58.559  1.00 20.23 ? 512  HIS A C     1 
ATOM   3772  O  O     . HIS A 1 492 ? -25.965 -19.361 57.462  1.00 20.36 ? 512  HIS A O     1 
ATOM   3773  C  CB    . HIS A 1 492 ? -25.346 -16.961 59.103  1.00 20.21 ? 512  HIS A CB    1 
ATOM   3774  C  CG    . HIS A 1 492 ? -24.547 -16.118 60.038  1.00 20.81 ? 512  HIS A CG    1 
ATOM   3775  N  ND1   . HIS A 1 492 ? -25.110 -15.446 61.101  1.00 20.79 ? 512  HIS A ND1   1 
ATOM   3776  C  CD2   . HIS A 1 492 ? -23.223 -15.829 60.066  1.00 21.42 ? 512  HIS A CD2   1 
ATOM   3777  C  CE1   . HIS A 1 492 ? -24.168 -14.778 61.744  1.00 20.22 ? 512  HIS A CE1   1 
ATOM   3778  N  NE2   . HIS A 1 492 ? -23.016 -14.992 61.135  1.00 22.34 ? 512  HIS A NE2   1 
ATOM   3779  N  N     . LEU A 1 493 ? -27.691 -19.357 58.895  1.00 20.01 ? 513  LEU A N     1 
ATOM   3780  C  CA    . LEU A 1 493 ? -28.650 -19.885 57.925  1.00 19.80 ? 513  LEU A CA    1 
ATOM   3781  C  C     . LEU A 1 493 ? -29.953 -19.121 58.055  1.00 19.64 ? 513  LEU A C     1 
ATOM   3782  O  O     . LEU A 1 493 ? -30.459 -18.953 59.165  1.00 19.84 ? 513  LEU A O     1 
ATOM   3783  C  CB    . LEU A 1 493 ? -28.908 -21.370 58.151  1.00 19.89 ? 513  LEU A CB    1 
ATOM   3784  C  CG    . LEU A 1 493 ? -27.710 -22.327 58.037  1.00 20.72 ? 513  LEU A CG    1 
ATOM   3785  C  CD1   . LEU A 1 493 ? -28.041 -23.706 58.599  1.00 19.65 ? 513  LEU A CD1   1 
ATOM   3786  C  CD2   . LEU A 1 493 ? -27.247 -22.442 56.580  1.00 18.98 ? 513  LEU A CD2   1 
ATOM   3787  N  N     . VAL A 1 494 ? -30.483 -18.650 56.927  1.00 18.76 ? 514  VAL A N     1 
ATOM   3788  C  CA    . VAL A 1 494 ? -31.766 -17.974 56.896  1.00 18.24 ? 514  VAL A CA    1 
ATOM   3789  C  C     . VAL A 1 494 ? -32.737 -18.748 56.019  1.00 18.16 ? 514  VAL A C     1 
ATOM   3790  O  O     . VAL A 1 494 ? -32.370 -19.228 54.946  1.00 17.79 ? 514  VAL A O     1 
ATOM   3791  C  CB    . VAL A 1 494 ? -31.661 -16.524 56.374  1.00 18.15 ? 514  VAL A CB    1 
ATOM   3792  C  CG1   . VAL A 1 494 ? -33.039 -15.883 56.339  1.00 17.73 ? 514  VAL A CG1   1 
ATOM   3793  C  CG2   . VAL A 1 494 ? -30.697 -15.690 57.254  1.00 17.62 ? 514  VAL A CG2   1 
ATOM   3794  N  N     . HIS A 1 495 ? -33.974 -18.875 56.495  1.00 17.37 ? 515  HIS A N     1 
ATOM   3795  C  CA    . HIS A 1 495 ? -35.026 -19.486 55.710  1.00 17.41 ? 515  HIS A CA    1 
ATOM   3796  C  C     . HIS A 1 495 ? -36.042 -18.446 55.247  1.00 17.19 ? 515  HIS A C     1 
ATOM   3797  O  O     . HIS A 1 495 ? -36.502 -17.623 56.037  1.00 16.79 ? 515  HIS A O     1 
ATOM   3798  C  CB    . HIS A 1 495 ? -35.737 -20.586 56.497  1.00 17.17 ? 515  HIS A CB    1 
ATOM   3799  C  CG    . HIS A 1 495 ? -36.378 -21.617 55.620  1.00 17.23 ? 515  HIS A CG    1 
ATOM   3800  N  ND1   . HIS A 1 495 ? -37.669 -22.065 55.812  1.00 16.44 ? 515  HIS A ND1   1 
ATOM   3801  C  CD2   . HIS A 1 495 ? -35.907 -22.273 54.529  1.00 16.93 ? 515  HIS A CD2   1 
ATOM   3802  C  CE1   . HIS A 1 495 ? -37.954 -22.969 54.889  1.00 17.18 ? 515  HIS A CE1   1 
ATOM   3803  N  NE2   . HIS A 1 495 ? -36.908 -23.105 54.092  1.00 14.82 ? 515  HIS A NE2   1 
ATOM   3804  N  N     . TYR A 1 496 ? -36.383 -18.507 53.961  1.00 16.96 ? 516  TYR A N     1 
ATOM   3805  C  CA    . TYR A 1 496 ? -37.396 -17.625 53.369  1.00 16.75 ? 516  TYR A CA    1 
ATOM   3806  C  C     . TYR A 1 496 ? -38.568 -18.422 52.836  1.00 16.33 ? 516  TYR A C     1 
ATOM   3807  O  O     . TYR A 1 496 ? -38.380 -19.502 52.265  1.00 16.48 ? 516  TYR A O     1 
ATOM   3808  C  CB    . TYR A 1 496 ? -36.815 -16.841 52.201  1.00 16.13 ? 516  TYR A CB    1 
ATOM   3809  C  CG    . TYR A 1 496 ? -35.971 -15.655 52.568  1.00 17.28 ? 516  TYR A CG    1 
ATOM   3810  C  CD1   . TYR A 1 496 ? -34.580 -15.763 52.640  1.00 18.06 ? 516  TYR A CD1   1 
ATOM   3811  C  CD2   . TYR A 1 496 ? -36.545 -14.399 52.772  1.00 16.59 ? 516  TYR A CD2   1 
ATOM   3812  C  CE1   . TYR A 1 496 ? -33.791 -14.668 52.944  1.00 17.46 ? 516  TYR A CE1   1 
ATOM   3813  C  CE2   . TYR A 1 496 ? -35.762 -13.304 53.063  1.00 17.40 ? 516  TYR A CE2   1 
ATOM   3814  C  CZ    . TYR A 1 496 ? -34.385 -13.446 53.159  1.00 17.13 ? 516  TYR A CZ    1 
ATOM   3815  O  OH    . TYR A 1 496 ? -33.606 -12.362 53.461  1.00 19.06 ? 516  TYR A OH    1 
ATOM   3816  N  N     . ARG A 1 497 ? -39.769 -17.866 53.000  1.00 15.84 ? 517  ARG A N     1 
ATOM   3817  C  CA    . ARG A 1 497 ? -40.978 -18.395 52.372  1.00 15.45 ? 517  ARG A CA    1 
ATOM   3818  C  C     . ARG A 1 497 ? -41.259 -17.550 51.158  1.00 15.20 ? 517  ARG A C     1 
ATOM   3819  O  O     . ARG A 1 497 ? -41.340 -16.325 51.252  1.00 15.43 ? 517  ARG A O     1 
ATOM   3820  C  CB    . ARG A 1 497 ? -42.174 -18.321 53.316  1.00 15.27 ? 517  ARG A CB    1 
ATOM   3821  C  CG    . ARG A 1 497 ? -43.491 -18.859 52.727  1.00 14.63 ? 517  ARG A CG    1 
ATOM   3822  C  CD    . ARG A 1 497 ? -44.628 -18.680 53.719  1.00 15.18 ? 517  ARG A CD    1 
ATOM   3823  N  NE    . ARG A 1 497 ? -45.964 -18.860 53.126  1.00 16.64 ? 517  ARG A NE    1 
ATOM   3824  C  CZ    . ARG A 1 497 ? -46.608 -20.025 52.998  1.00 15.96 ? 517  ARG A CZ    1 
ATOM   3825  N  NH1   . ARG A 1 497 ? -46.062 -21.155 53.410  1.00 14.47 ? 517  ARG A NH1   1 
ATOM   3826  N  NH2   . ARG A 1 497 ? -47.819 -20.053 52.452  1.00 17.24 ? 517  ARG A NH2   1 
ATOM   3827  N  N     . VAL A 1 498 ? -41.421 -18.201 50.018  1.00 15.28 ? 518  VAL A N     1 
ATOM   3828  C  CA    . VAL A 1 498 ? -41.581 -17.497 48.756  1.00 15.14 ? 518  VAL A CA    1 
ATOM   3829  C  C     . VAL A 1 498 ? -42.804 -18.047 48.035  1.00 15.25 ? 518  VAL A C     1 
ATOM   3830  O  O     . VAL A 1 498 ? -42.707 -18.922 47.177  1.00 14.78 ? 518  VAL A O     1 
ATOM   3831  C  CB    . VAL A 1 498 ? -40.298 -17.583 47.896  1.00 15.36 ? 518  VAL A CB    1 
ATOM   3832  C  CG1   . VAL A 1 498 ? -40.385 -16.605 46.740  1.00 15.47 ? 518  VAL A CG1   1 
ATOM   3833  C  CG2   . VAL A 1 498 ? -39.046 -17.306 48.749  1.00 15.12 ? 518  VAL A CG2   1 
ATOM   3834  N  N     . ASP A 1 499 ? -43.972 -17.541 48.431  1.00 15.73 ? 519  ASP A N     1 
ATOM   3835  C  CA    . ASP A 1 499 ? -45.236 -17.996 47.866  1.00 16.11 ? 519  ASP A CA    1 
ATOM   3836  C  C     . ASP A 1 499 ? -45.447 -17.275 46.546  1.00 16.38 ? 519  ASP A C     1 
ATOM   3837  O  O     . ASP A 1 499 ? -46.119 -16.248 46.482  1.00 16.42 ? 519  ASP A O     1 
ATOM   3838  C  CB    . ASP A 1 499 ? -46.394 -17.734 48.843  1.00 15.79 ? 519  ASP A CB    1 
ATOM   3839  C  CG    . ASP A 1 499 ? -47.736 -18.242 48.322  1.00 15.71 ? 519  ASP A CG    1 
ATOM   3840  O  OD1   . ASP A 1 499 ? -47.772 -18.908 47.262  1.00 15.46 ? 519  ASP A OD1   1 
ATOM   3841  O  OD2   . ASP A 1 499 ? -48.764 -17.991 48.990  1.00 16.50 ? 519  ASP A OD2   1 
ATOM   3842  N  N     . LEU A 1 500 ? -44.832 -17.806 45.495  1.00 17.24 ? 520  LEU A N     1 
ATOM   3843  C  CA    . LEU A 1 500 ? -45.001 -17.271 44.157  1.00 17.72 ? 520  LEU A CA    1 
ATOM   3844  C  C     . LEU A 1 500 ? -46.387 -17.678 43.636  1.00 17.55 ? 520  LEU A C     1 
ATOM   3845  O  O     . LEU A 1 500 ? -46.796 -18.828 43.789  1.00 16.97 ? 520  LEU A O     1 
ATOM   3846  C  CB    . LEU A 1 500 ? -43.899 -17.775 43.220  1.00 18.13 ? 520  LEU A CB    1 
ATOM   3847  C  CG    . LEU A 1 500 ? -42.483 -17.267 43.552  1.00 19.55 ? 520  LEU A CG    1 
ATOM   3848  C  CD1   . LEU A 1 500 ? -41.404 -18.198 43.006  1.00 19.38 ? 520  LEU A CD1   1 
ATOM   3849  C  CD2   . LEU A 1 500 ? -42.262 -15.834 43.063  1.00 20.49 ? 520  LEU A CD2   1 
ATOM   3850  N  N     . ASP A 1 501 ? -47.108 -16.709 43.072  1.00 17.97 ? 521  ASP A N     1 
ATOM   3851  C  CA    . ASP A 1 501 ? -48.340 -16.943 42.326  1.00 18.26 ? 521  ASP A CA    1 
ATOM   3852  C  C     . ASP A 1 501 ? -48.124 -16.331 40.945  1.00 18.30 ? 521  ASP A C     1 
ATOM   3853  O  O     . ASP A 1 501 ? -48.562 -15.217 40.663  1.00 18.06 ? 521  ASP A O     1 
ATOM   3854  C  CB    . ASP A 1 501 ? -49.546 -16.262 42.987  1.00 18.73 ? 521  ASP A CB    1 
ATOM   3855  C  CG    . ASP A 1 501 ? -50.042 -16.961 44.234  1.00 18.92 ? 521  ASP A CG    1 
ATOM   3856  O  OD1   . ASP A 1 501 ? -49.489 -17.988 44.672  1.00 18.49 ? 521  ASP A OD1   1 
ATOM   3857  O  OD2   . ASP A 1 501 ? -51.027 -16.446 44.800  1.00 22.02 ? 521  ASP A OD2   1 
ATOM   3858  N  N     . VAL A 1 502 ? -47.460 -17.070 40.071  1.00 18.46 ? 522  VAL A N     1 
ATOM   3859  C  CA    . VAL A 1 502 ? -47.021 -16.499 38.802  1.00 18.80 ? 522  VAL A CA    1 
ATOM   3860  C  C     . VAL A 1 502 ? -48.225 -16.320 37.874  1.00 19.61 ? 522  VAL A C     1 
ATOM   3861  O  O     . VAL A 1 502 ? -48.847 -17.289 37.455  1.00 20.27 ? 522  VAL A O     1 
ATOM   3862  C  CB    . VAL A 1 502 ? -45.893 -17.330 38.173  1.00 18.54 ? 522  VAL A CB    1 
ATOM   3863  C  CG1   . VAL A 1 502 ? -45.344 -16.628 36.938  1.00 17.92 ? 522  VAL A CG1   1 
ATOM   3864  C  CG2   . VAL A 1 502 ? -44.773 -17.577 39.231  1.00 17.18 ? 522  VAL A CG2   1 
ATOM   3865  N  N     . ALA A 1 503 ? -48.567 -15.063 37.610  1.00 20.49 ? 523  ALA A N     1 
ATOM   3866  C  CA    . ALA A 1 503 ? -49.761 -14.688 36.862  1.00 21.24 ? 523  ALA A CA    1 
ATOM   3867  C  C     . ALA A 1 503 ? -51.046 -15.328 37.412  1.00 22.31 ? 523  ALA A C     1 
ATOM   3868  O  O     . ALA A 1 503 ? -52.020 -15.455 36.693  1.00 22.65 ? 523  ALA A O     1 
ATOM   3869  C  CB    . ALA A 1 503 ? -49.582 -15.030 35.393  1.00 20.94 ? 523  ALA A CB    1 
ATOM   3870  N  N     . GLY A 1 504 ? -51.061 -15.705 38.688  1.00 23.55 ? 524  GLY A N     1 
ATOM   3871  C  CA    . GLY A 1 504 ? -52.163 -16.505 39.237  1.00 24.11 ? 524  GLY A CA    1 
ATOM   3872  C  C     . GLY A 1 504 ? -51.692 -17.540 40.244  1.00 24.84 ? 524  GLY A C     1 
ATOM   3873  O  O     . GLY A 1 504 ? -50.490 -17.804 40.383  1.00 24.12 ? 524  GLY A O     1 
ATOM   3874  N  N     . THR A 1 505 ? -52.662 -18.133 40.934  1.00 25.31 ? 525  THR A N     1 
ATOM   3875  C  CA    A THR A 1 505 ? -52.414 -19.127 41.961  0.60 25.62 ? 525  THR A CA    1 
ATOM   3876  C  CA    B THR A 1 505 ? -52.383 -19.130 41.969  0.40 25.38 ? 525  THR A CA    1 
ATOM   3877  C  C     . THR A 1 505 ? -51.803 -20.413 41.399  1.00 25.69 ? 525  THR A C     1 
ATOM   3878  O  O     . THR A 1 505 ? -50.852 -20.941 41.950  1.00 25.76 ? 525  THR A O     1 
ATOM   3879  C  CB    A THR A 1 505 ? -53.741 -19.461 42.666  0.60 25.94 ? 525  THR A CB    1 
ATOM   3880  C  CB    B THR A 1 505 ? -53.644 -19.504 42.783  0.40 25.56 ? 525  THR A CB    1 
ATOM   3881  O  OG1   A THR A 1 505 ? -54.490 -18.249 42.854  0.60 26.21 ? 525  THR A OG1   1 
ATOM   3882  O  OG1   B THR A 1 505 ? -54.783 -19.540 41.913  0.40 24.94 ? 525  THR A OG1   1 
ATOM   3883  C  CG2   A THR A 1 505 ? -53.487 -20.111 43.998  0.60 25.81 ? 525  THR A CG2   1 
ATOM   3884  C  CG2   B THR A 1 505 ? -53.875 -18.498 43.918  0.40 25.02 ? 525  THR A CG2   1 
ATOM   3885  N  N     . LYS A 1 506 ? -52.360 -20.909 40.288  1.00 25.86 ? 526  LYS A N     1 
ATOM   3886  C  CA    . LYS A 1 506 ? -51.966 -22.228 39.757  1.00 25.73 ? 526  LYS A CA    1 
ATOM   3887  C  C     . LYS A 1 506 ? -50.693 -22.197 38.913  1.00 23.93 ? 526  LYS A C     1 
ATOM   3888  O  O     . LYS A 1 506 ? -50.677 -21.662 37.804  1.00 23.44 ? 526  LYS A O     1 
ATOM   3889  C  CB    . LYS A 1 506 ? -53.102 -22.858 38.948  1.00 26.52 ? 526  LYS A CB    1 
ATOM   3890  C  CG    . LYS A 1 506 ? -54.383 -23.127 39.763  1.00 30.09 ? 526  LYS A CG    1 
ATOM   3891  C  CD    . LYS A 1 506 ? -54.237 -24.336 40.688  1.00 33.17 ? 526  LYS A CD    1 
ATOM   3892  C  CE    . LYS A 1 506 ? -55.584 -24.776 41.264  1.00 34.97 ? 526  LYS A CE    1 
ATOM   3893  N  NZ    . LYS A 1 506 ? -56.568 -25.115 40.183  1.00 37.44 ? 526  LYS A NZ    1 
ATOM   3894  N  N     . ASN A 1 507 ? -49.648 -22.813 39.452  1.00 22.19 ? 527  ASN A N     1 
ATOM   3895  C  CA    . ASN A 1 507 ? -48.353 -22.887 38.811  1.00 21.23 ? 527  ASN A CA    1 
ATOM   3896  C  C     . ASN A 1 507 ? -47.793 -24.312 38.736  1.00 20.64 ? 527  ASN A C     1 
ATOM   3897  O  O     . ASN A 1 507 ? -48.316 -25.260 39.355  1.00 20.01 ? 527  ASN A O     1 
ATOM   3898  C  CB    . ASN A 1 507 ? -47.345 -22.032 39.577  1.00 21.09 ? 527  ASN A CB    1 
ATOM   3899  C  CG    . ASN A 1 507 ? -47.676 -20.549 39.566  1.00 20.36 ? 527  ASN A CG    1 
ATOM   3900  O  OD1   . ASN A 1 507 ? -47.372 -19.825 40.529  1.00 17.70 ? 527  ASN A OD1   1 
ATOM   3901  N  ND2   . ASN A 1 507 ? -48.265 -20.078 38.470  1.00 19.85 ? 527  ASN A ND2   1 
ATOM   3902  N  N     . SER A 1 508 ? -46.733 -24.445 37.943  1.00 19.75 ? 528  SER A N     1 
ATOM   3903  C  CA    A SER A 1 508 ? -45.924 -25.650 37.944  0.50 19.58 ? 528  SER A CA    1 
ATOM   3904  C  CA    B SER A 1 508 ? -45.913 -25.649 37.911  0.50 19.82 ? 528  SER A CA    1 
ATOM   3905  C  C     . SER A 1 508 ? -44.468 -25.253 38.167  1.00 19.40 ? 528  SER A C     1 
ATOM   3906  O  O     . SER A 1 508 ? -44.135 -24.065 38.191  1.00 19.13 ? 528  SER A O     1 
ATOM   3907  C  CB    A SER A 1 508 ? -46.111 -26.426 36.638  0.50 19.67 ? 528  SER A CB    1 
ATOM   3908  C  CB    B SER A 1 508 ? -46.026 -26.364 36.562  0.50 19.96 ? 528  SER A CB    1 
ATOM   3909  O  OG    A SER A 1 508 ? -47.459 -26.863 36.499  0.50 19.30 ? 528  SER A OG    1 
ATOM   3910  O  OG    B SER A 1 508 ? -45.375 -25.638 35.530  0.50 21.09 ? 528  SER A OG    1 
ATOM   3911  N  N     . PHE A 1 509 ? -43.618 -26.246 38.370  1.00 19.25 ? 529  PHE A N     1 
ATOM   3912  C  CA    . PHE A 1 509 ? -42.203 -26.011 38.585  1.00 19.41 ? 529  PHE A CA    1 
ATOM   3913  C  C     . PHE A 1 509 ? -41.421 -26.852 37.592  1.00 19.95 ? 529  PHE A C     1 
ATOM   3914  O  O     . PHE A 1 509 ? -41.723 -28.016 37.403  1.00 20.53 ? 529  PHE A O     1 
ATOM   3915  C  CB    . PHE A 1 509 ? -41.808 -26.367 40.016  1.00 19.00 ? 529  PHE A CB    1 
ATOM   3916  C  CG    . PHE A 1 509 ? -40.329 -26.287 40.274  1.00 18.36 ? 529  PHE A CG    1 
ATOM   3917  C  CD1   . PHE A 1 509 ? -39.687 -25.055 40.323  1.00 16.03 ? 529  PHE A CD1   1 
ATOM   3918  C  CD2   . PHE A 1 509 ? -39.578 -27.440 40.463  1.00 16.94 ? 529  PHE A CD2   1 
ATOM   3919  C  CE1   . PHE A 1 509 ? -38.316 -24.966 40.559  1.00 17.42 ? 529  PHE A CE1   1 
ATOM   3920  C  CE2   . PHE A 1 509 ? -38.209 -27.359 40.693  1.00 17.91 ? 529  PHE A CE2   1 
ATOM   3921  C  CZ    . PHE A 1 509 ? -37.576 -26.112 40.745  1.00 16.98 ? 529  PHE A CZ    1 
ATOM   3922  N  N     . GLN A 1 510 ? -40.431 -26.248 36.947  1.00 20.44 ? 530  GLN A N     1 
ATOM   3923  C  CA    . GLN A 1 510 ? -39.558 -26.955 36.018  1.00 20.90 ? 530  GLN A CA    1 
ATOM   3924  C  C     . GLN A 1 510 ? -38.165 -26.351 36.083  1.00 20.53 ? 530  GLN A C     1 
ATOM   3925  O  O     . GLN A 1 510 ? -37.978 -25.254 36.616  1.00 20.71 ? 530  GLN A O     1 
ATOM   3926  C  CB    . GLN A 1 510 ? -40.107 -26.892 34.584  1.00 21.33 ? 530  GLN A CB    1 
ATOM   3927  C  CG    . GLN A 1 510 ? -40.170 -25.503 33.983  1.00 23.07 ? 530  GLN A CG    1 
ATOM   3928  C  CD    . GLN A 1 510 ? -40.493 -25.506 32.490  1.00 25.95 ? 530  GLN A CD    1 
ATOM   3929  O  OE1   . GLN A 1 510 ? -41.027 -26.476 31.939  1.00 30.12 ? 530  GLN A OE1   1 
ATOM   3930  N  NE2   . GLN A 1 510 ? -40.172 -24.419 31.836  1.00 26.34 ? 530  GLN A NE2   1 
ATOM   3931  N  N     . THR A 1 511 ? -37.189 -27.076 35.557  1.00 20.28 ? 531  THR A N     1 
ATOM   3932  C  CA    . THR A 1 511 ? -35.820 -26.576 35.497  1.00 20.08 ? 531  THR A CA    1 
ATOM   3933  C  C     . THR A 1 511 ? -35.286 -26.713 34.086  1.00 19.96 ? 531  THR A C     1 
ATOM   3934  O  O     . THR A 1 511 ? -35.801 -27.513 33.297  1.00 19.59 ? 531  THR A O     1 
ATOM   3935  C  CB    . THR A 1 511 ? -34.880 -27.296 36.497  1.00 20.03 ? 531  THR A CB    1 
ATOM   3936  O  OG1   . THR A 1 511 ? -34.835 -28.698 36.217  1.00 21.52 ? 531  THR A OG1   1 
ATOM   3937  C  CG2   . THR A 1 511 ? -35.342 -27.077 37.942  1.00 20.09 ? 531  THR A CG2   1 
ATOM   3938  N  N     . LEU A 1 512 ? -34.278 -25.901 33.764  1.00 19.98 ? 532  LEU A N     1 
ATOM   3939  C  CA    . LEU A 1 512 ? -33.591 -25.976 32.486  1.00 20.16 ? 532  LEU A CA    1 
ATOM   3940  C  C     . LEU A 1 512 ? -32.096 -26.142 32.727  1.00 20.62 ? 532  LEU A C     1 
ATOM   3941  O  O     . LEU A 1 512 ? -31.533 -25.559 33.661  1.00 20.75 ? 532  LEU A O     1 
ATOM   3942  C  CB    . LEU A 1 512 ? -33.841 -24.735 31.628  1.00 19.98 ? 532  LEU A CB    1 
ATOM   3943  C  CG    . LEU A 1 512 ? -35.273 -24.205 31.501  1.00 21.17 ? 532  LEU A CG    1 
ATOM   3944  C  CD1   . LEU A 1 512 ? -35.259 -22.812 30.839  1.00 19.25 ? 532  LEU A CD1   1 
ATOM   3945  C  CD2   . LEU A 1 512 ? -36.221 -25.184 30.759  1.00 18.11 ? 532  LEU A CD2   1 
ATOM   3946  N  N     . GLN A 1 513 ? -31.475 -26.956 31.883  1.00 20.93 ? 533  GLN A N     1 
ATOM   3947  C  CA    . GLN A 1 513 ? -30.052 -27.209 31.935  1.00 21.40 ? 533  GLN A CA    1 
ATOM   3948  C  C     . GLN A 1 513 ? -29.508 -27.218 30.520  1.00 21.66 ? 533  GLN A C     1 
ATOM   3949  O  O     . GLN A 1 513 ? -30.249 -27.462 29.560  1.00 21.50 ? 533  GLN A O     1 
ATOM   3950  C  CB    . GLN A 1 513 ? -29.770 -28.564 32.610  1.00 21.60 ? 533  GLN A CB    1 
ATOM   3951  N  N     . MET A 1 514 ? -28.217 -26.933 30.390  1.00 22.03 ? 534  MET A N     1 
ATOM   3952  C  CA    . MET A 1 514 ? -27.531 -27.148 29.136  1.00 22.73 ? 534  MET A CA    1 
ATOM   3953  C  C     . MET A 1 514 ? -27.086 -28.594 29.095  1.00 22.96 ? 534  MET A C     1 
ATOM   3954  O  O     . MET A 1 514 ? -26.538 -29.097 30.068  1.00 23.48 ? 534  MET A O     1 
ATOM   3955  C  CB    . MET A 1 514 ? -26.315 -26.240 28.997  1.00 22.95 ? 534  MET A CB    1 
ATOM   3956  C  CG    . MET A 1 514 ? -25.666 -26.332 27.619  1.00 24.12 ? 534  MET A CG    1 
ATOM   3957  S  SD    . MET A 1 514 ? -24.338 -27.556 27.505  1.00 26.01 ? 534  MET A SD    1 
ATOM   3958  C  CE    . MET A 1 514 ? -23.023 -26.665 28.318  1.00 26.32 ? 534  MET A CE    1 
ATOM   3959  N  N     . LYS A 1 515 ? -27.345 -29.267 27.979  1.00 23.19 ? 535  LYS A N     1 
ATOM   3960  C  CA    . LYS A 1 515 ? -26.828 -30.613 27.753  1.00 23.22 ? 535  LYS A CA    1 
ATOM   3961  C  C     . LYS A 1 515 ? -26.197 -30.657 26.365  1.00 23.03 ? 535  LYS A C     1 
ATOM   3962  O  O     . LYS A 1 515 ? -26.781 -30.171 25.404  1.00 22.71 ? 535  LYS A O     1 
ATOM   3963  C  CB    . LYS A 1 515 ? -27.946 -31.644 27.863  1.00 23.47 ? 535  LYS A CB    1 
ATOM   3964  C  CG    . LYS A 1 515 ? -27.473 -33.080 27.875  1.00 25.18 ? 535  LYS A CG    1 
ATOM   3965  C  CD    . LYS A 1 515 ? -28.505 -34.000 28.535  1.00 27.40 ? 535  LYS A CD    1 
ATOM   3966  N  N     . LEU A 1 516 ? -25.000 -31.224 26.269  1.00 22.63 ? 536  LEU A N     1 
ATOM   3967  C  CA    . LEU A 1 516 ? -24.312 -31.300 24.996  1.00 22.89 ? 536  LEU A CA    1 
ATOM   3968  C  C     . LEU A 1 516 ? -24.906 -32.416 24.149  1.00 22.80 ? 536  LEU A C     1 
ATOM   3969  O  O     . LEU A 1 516 ? -25.359 -33.427 24.668  1.00 23.23 ? 536  LEU A O     1 
ATOM   3970  C  CB    . LEU A 1 516 ? -22.805 -31.557 25.184  1.00 22.59 ? 536  LEU A CB    1 
ATOM   3971  C  CG    . LEU A 1 516 ? -21.971 -30.498 25.916  1.00 22.85 ? 536  LEU A CG    1 
ATOM   3972  C  CD1   . LEU A 1 516 ? -20.542 -31.000 26.096  1.00 22.63 ? 536  LEU A CD1   1 
ATOM   3973  C  CD2   . LEU A 1 516 ? -21.970 -29.143 25.190  1.00 22.60 ? 536  LEU A CD2   1 
ATOM   3974  N  N     . GLU A 1 517 ? -24.909 -32.214 22.842  1.00 23.11 ? 537  GLU A N     1 
ATOM   3975  C  CA    . GLU A 1 517 ? -25.145 -33.288 21.883  1.00 23.06 ? 537  GLU A CA    1 
ATOM   3976  C  C     . GLU A 1 517 ? -23.894 -33.403 21.004  1.00 23.69 ? 537  GLU A C     1 
ATOM   3977  O  O     . GLU A 1 517 ? -23.070 -32.491 20.935  1.00 23.40 ? 537  GLU A O     1 
ATOM   3978  C  CB    . GLU A 1 517 ? -26.371 -32.995 21.016  1.00 22.96 ? 537  GLU A CB    1 
ATOM   3979  C  CG    . GLU A 1 517 ? -26.198 -31.813 20.073  1.00 22.47 ? 537  GLU A CG    1 
ATOM   3980  C  CD    . GLU A 1 517 ? -27.376 -31.595 19.143  1.00 22.09 ? 537  GLU A CD    1 
ATOM   3981  O  OE1   . GLU A 1 517 ? -28.373 -32.333 19.227  1.00 22.46 ? 537  GLU A OE1   1 
ATOM   3982  O  OE2   . GLU A 1 517 ? -27.298 -30.668 18.318  1.00 22.00 ? 537  GLU A OE2   1 
ATOM   3983  N  N     . ASN A 1 518 ? -23.785 -34.537 20.331  1.00 24.19 ? 538  ASN A N     1 
ATOM   3984  C  CA    . ASN A 1 518 ? -22.661 -34.851 19.492  1.00 24.67 ? 538  ASN A CA    1 
ATOM   3985  C  C     . ASN A 1 518 ? -23.268 -35.376 18.211  1.00 24.85 ? 538  ASN A C     1 
ATOM   3986  O  O     . ASN A 1 518 ? -23.789 -36.492 18.172  1.00 24.64 ? 538  ASN A O     1 
ATOM   3987  C  CB    . ASN A 1 518 ? -21.785 -35.892 20.190  1.00 24.93 ? 538  ASN A CB    1 
ATOM   3988  C  CG    . ASN A 1 518 ? -20.596 -36.330 19.355  1.00 25.91 ? 538  ASN A CG    1 
ATOM   3989  O  OD1   . ASN A 1 518 ? -20.469 -35.968 18.181  1.00 25.34 ? 538  ASN A OD1   1 
ATOM   3990  N  ND2   . ASN A 1 518 ? -19.705 -37.115 19.972  1.00 27.21 ? 538  ASN A ND2   1 
ATOM   3991  N  N     . ILE A 1 519 ? -23.265 -34.531 17.182  1.00 25.16 ? 539  ILE A N     1 
ATOM   3992  C  CA    . ILE A 1 519 ? -23.882 -34.870 15.903  1.00 25.27 ? 539  ILE A CA    1 
ATOM   3993  C  C     . ILE A 1 519 ? -22.856 -34.786 14.781  1.00 25.28 ? 539  ILE A C     1 
ATOM   3994  O  O     . ILE A 1 519 ? -21.780 -34.210 14.945  1.00 24.86 ? 539  ILE A O     1 
ATOM   3995  C  CB    . ILE A 1 519 ? -25.076 -33.939 15.569  1.00 25.05 ? 539  ILE A CB    1 
ATOM   3996  C  CG1   . ILE A 1 519 ? -24.636 -32.473 15.531  1.00 25.68 ? 539  ILE A CG1   1 
ATOM   3997  C  CG2   . ILE A 1 519 ? -26.195 -34.123 16.585  1.00 25.30 ? 539  ILE A CG2   1 
ATOM   3998  C  CD1   . ILE A 1 519 ? -25.672 -31.530 14.957  1.00 25.42 ? 539  ILE A CD1   1 
ATOM   3999  N  N     . THR A 1 520 ? -23.209 -35.387 13.647  1.00 25.51 ? 540  THR A N     1 
ATOM   4000  C  CA    . THR A 1 520 ? -22.492 -35.186 12.396  1.00 25.29 ? 540  THR A CA    1 
ATOM   4001  C  C     . THR A 1 520 ? -22.554 -33.706 12.057  1.00 25.14 ? 540  THR A C     1 
ATOM   4002  O  O     . THR A 1 520 ? -23.625 -33.101 12.129  1.00 24.86 ? 540  THR A O     1 
ATOM   4003  C  CB    . THR A 1 520 ? -23.140 -36.000 11.255  1.00 25.19 ? 540  THR A CB    1 
ATOM   4004  O  OG1   . THR A 1 520 ? -23.117 -37.384 11.602  1.00 26.37 ? 540  THR A OG1   1 
ATOM   4005  C  CG2   . THR A 1 520 ? -22.408 -35.791 9.917   1.00 25.37 ? 540  THR A CG2   1 
ATOM   4006  N  N     . ASN A 1 521 ? -21.404 -33.123 11.726  1.00 25.17 ? 541  ASN A N     1 
ATOM   4007  C  CA    . ASN A 1 521 ? -21.353 -31.748 11.235  1.00 25.53 ? 541  ASN A CA    1 
ATOM   4008  C  C     . ASN A 1 521 ? -22.116 -31.693 9.912   1.00 25.92 ? 541  ASN A C     1 
ATOM   4009  O  O     . ASN A 1 521 ? -21.664 -32.279 8.917   1.00 25.90 ? 541  ASN A O     1 
ATOM   4010  C  CB    . ASN A 1 521 ? -19.905 -31.280 11.059  1.00 25.33 ? 541  ASN A CB    1 
ATOM   4011  C  CG    . ASN A 1 521 ? -19.798 -29.878 10.483  1.00 25.37 ? 541  ASN A CG    1 
ATOM   4012  O  OD1   . ASN A 1 521 ? -20.667 -29.429 9.735   1.00 24.08 ? 541  ASN A OD1   1 
ATOM   4013  N  ND2   . ASN A 1 521 ? -18.715 -29.177 10.832  1.00 24.94 ? 541  ASN A ND2   1 
ATOM   4014  N  N     . PRO A 1 522 ? -23.265 -30.984 9.897   1.00 26.44 ? 542  PRO A N     1 
ATOM   4015  C  CA    . PRO A 1 522 ? -24.194 -31.033 8.771   1.00 27.00 ? 542  PRO A CA    1 
ATOM   4016  C  C     . PRO A 1 522 ? -23.640 -30.515 7.452   1.00 27.31 ? 542  PRO A C     1 
ATOM   4017  O  O     . PRO A 1 522 ? -24.150 -30.901 6.410   1.00 28.23 ? 542  PRO A O     1 
ATOM   4018  C  CB    . PRO A 1 522 ? -25.376 -30.144 9.224   1.00 27.10 ? 542  PRO A CB    1 
ATOM   4019  C  CG    . PRO A 1 522 ? -25.131 -29.819 10.633  1.00 27.00 ? 542  PRO A CG    1 
ATOM   4020  C  CD    . PRO A 1 522 ? -23.672 -29.967 10.883  1.00 26.61 ? 542  PRO A CD    1 
ATOM   4021  N  N     . TRP A 1 523 ? -22.627 -29.651 7.497   1.00 27.35 ? 543  TRP A N     1 
ATOM   4022  C  CA    . TRP A 1 523 ? -22.036 -29.061 6.288   1.00 27.28 ? 543  TRP A CA    1 
ATOM   4023  C  C     . TRP A 1 523 ? -20.616 -29.583 6.018   1.00 27.96 ? 543  TRP A C     1 
ATOM   4024  O  O     . TRP A 1 523 ? -19.966 -29.156 5.067   1.00 27.46 ? 543  TRP A O     1 
ATOM   4025  C  CB    . TRP A 1 523 ? -22.026 -27.531 6.384   1.00 27.03 ? 543  TRP A CB    1 
ATOM   4026  C  CG    . TRP A 1 523 ? -21.429 -26.987 7.663   1.00 25.75 ? 543  TRP A CG    1 
ATOM   4027  C  CD1   . TRP A 1 523 ? -22.086 -26.760 8.847   1.00 23.59 ? 543  TRP A CD1   1 
ATOM   4028  C  CD2   . TRP A 1 523 ? -20.062 -26.617 7.885   1.00 24.19 ? 543  TRP A CD2   1 
ATOM   4029  N  NE1   . TRP A 1 523 ? -21.210 -26.261 9.784   1.00 23.33 ? 543  TRP A NE1   1 
ATOM   4030  C  CE2   . TRP A 1 523 ? -19.961 -26.173 9.225   1.00 22.88 ? 543  TRP A CE2   1 
ATOM   4031  C  CE3   . TRP A 1 523 ? -18.915 -26.615 7.084   1.00 23.97 ? 543  TRP A CE3   1 
ATOM   4032  C  CZ2   . TRP A 1 523 ? -18.764 -25.732 9.776   1.00 23.02 ? 543  TRP A CZ2   1 
ATOM   4033  C  CZ3   . TRP A 1 523 ? -17.727 -26.172 7.626   1.00 23.67 ? 543  TRP A CZ3   1 
ATOM   4034  C  CH2   . TRP A 1 523 ? -17.657 -25.738 8.966   1.00 24.68 ? 543  TRP A CH2   1 
ATOM   4035  N  N     . SER A 1 524 ? -20.142 -30.492 6.867   1.00 28.56 ? 544  SER A N     1 
ATOM   4036  C  CA    . SER A 1 524 ? -18.850 -31.140 6.673   1.00 29.25 ? 544  SER A CA    1 
ATOM   4037  C  C     . SER A 1 524 ? -18.930 -32.548 7.270   1.00 29.80 ? 544  SER A C     1 
ATOM   4038  O  O     . SER A 1 524 ? -18.492 -32.767 8.394   1.00 29.73 ? 544  SER A O     1 
ATOM   4039  C  CB    . SER A 1 524 ? -17.736 -30.320 7.322   1.00 29.33 ? 544  SER A CB    1 
ATOM   4040  O  OG    . SER A 1 524 ? -16.458 -30.887 7.065   1.00 29.83 ? 544  SER A OG    1 
ATOM   4041  N  N     . PRO A 1 525 ? -19.517 -33.502 6.512   1.00 30.73 ? 545  PRO A N     1 
ATOM   4042  C  CA    . PRO A 1 525 ? -19.849 -34.880 6.931   1.00 30.85 ? 545  PRO A CA    1 
ATOM   4043  C  C     . PRO A 1 525 ? -18.730 -35.633 7.664   1.00 30.77 ? 545  PRO A C     1 
ATOM   4044  O  O     . PRO A 1 525 ? -19.021 -36.421 8.559   1.00 31.01 ? 545  PRO A O     1 
ATOM   4045  C  CB    . PRO A 1 525 ? -20.168 -35.591 5.607   1.00 31.38 ? 545  PRO A CB    1 
ATOM   4046  C  CG    . PRO A 1 525 ? -20.541 -34.523 4.666   1.00 31.25 ? 545  PRO A CG    1 
ATOM   4047  C  CD    . PRO A 1 525 ? -19.882 -33.253 5.104   1.00 30.70 ? 545  PRO A CD    1 
ATOM   4048  N  N     . ARG A 1 526 ? -17.472 -35.380 7.305   1.00 30.54 ? 546  ARG A N     1 
ATOM   4049  C  CA    . ARG A 1 526 ? -16.333 -36.045 7.954   1.00 30.13 ? 546  ARG A CA    1 
ATOM   4050  C  C     . ARG A 1 526 ? -16.102 -35.583 9.388   1.00 29.85 ? 546  ARG A C     1 
ATOM   4051  O  O     . ARG A 1 526 ? -15.209 -36.097 10.063  1.00 29.76 ? 546  ARG A O     1 
ATOM   4052  C  CB    . ARG A 1 526 ? -15.042 -35.828 7.152   1.00 30.30 ? 546  ARG A CB    1 
ATOM   4053  C  CG    . ARG A 1 526 ? -15.040 -36.486 5.767   1.00 30.54 ? 546  ARG A CG    1 
ATOM   4054  C  CD    . ARG A 1 526 ? -13.676 -36.358 5.086   1.00 30.46 ? 546  ARG A CD    1 
ATOM   4055  N  N     . HIS A 1 527 ? -16.900 -34.625 9.863   1.00 29.27 ? 547  HIS A N     1 
ATOM   4056  C  CA    . HIS A 1 527 ? -16.648 -33.999 11.155  1.00 28.56 ? 547  HIS A CA    1 
ATOM   4057  C  C     . HIS A 1 527 ? -17.830 -34.049 12.099  1.00 27.99 ? 547  HIS A C     1 
ATOM   4058  O  O     . HIS A 1 527 ? -18.953 -34.331 11.692  1.00 27.49 ? 547  HIS A O     1 
ATOM   4059  C  CB    . HIS A 1 527 ? -16.223 -32.557 10.935  1.00 28.66 ? 547  HIS A CB    1 
ATOM   4060  C  CG    . HIS A 1 527 ? -14.997 -32.427 10.097  1.00 28.94 ? 547  HIS A CG    1 
ATOM   4061  N  ND1   . HIS A 1 527 ? -15.047 -32.193 8.740   1.00 28.06 ? 547  HIS A ND1   1 
ATOM   4062  C  CD2   . HIS A 1 527 ? -13.686 -32.538 10.415  1.00 28.97 ? 547  HIS A CD2   1 
ATOM   4063  C  CE1   . HIS A 1 527 ? -13.817 -32.147 8.263   1.00 28.13 ? 547  HIS A CE1   1 
ATOM   4064  N  NE2   . HIS A 1 527 ? -12.974 -32.360 9.257   1.00 28.32 ? 547  HIS A NE2   1 
ATOM   4065  N  N     . ARG A 1 528 ? -17.546 -33.766 13.371  1.00 27.72 ? 548  ARG A N     1 
ATOM   4066  C  CA    . ARG A 1 528 ? -18.559 -33.744 14.422  1.00 27.37 ? 548  ARG A CA    1 
ATOM   4067  C  C     . ARG A 1 528 ? -18.800 -32.319 14.912  1.00 26.76 ? 548  ARG A C     1 
ATOM   4068  O  O     . ARG A 1 528 ? -17.893 -31.496 14.933  1.00 26.71 ? 548  ARG A O     1 
ATOM   4069  C  CB    . ARG A 1 528 ? -18.128 -34.580 15.634  1.00 27.61 ? 548  ARG A CB    1 
ATOM   4070  C  CG    . ARG A 1 528 ? -17.607 -35.972 15.350  1.00 27.38 ? 548  ARG A CG    1 
ATOM   4071  C  CD    . ARG A 1 528 ? -18.614 -36.822 14.658  1.00 27.73 ? 548  ARG A CD    1 
ATOM   4072  N  NE    . ARG A 1 528 ? -19.804 -37.047 15.469  1.00 28.62 ? 548  ARG A NE    1 
ATOM   4073  C  CZ    . ARG A 1 528 ? -20.887 -37.687 15.040  1.00 28.98 ? 548  ARG A CZ    1 
ATOM   4074  N  NH1   . ARG A 1 528 ? -20.929 -38.182 13.810  1.00 29.33 ? 548  ARG A NH1   1 
ATOM   4075  N  NH2   . ARG A 1 528 ? -21.935 -37.840 15.845  1.00 29.83 ? 548  ARG A NH2   1 
ATOM   4076  N  N     . VAL A 1 529 ? -20.032 -32.053 15.324  1.00 26.14 ? 549  VAL A N     1 
ATOM   4077  C  CA    . VAL A 1 529 ? -20.350 -30.866 16.104  1.00 25.52 ? 549  VAL A CA    1 
ATOM   4078  C  C     . VAL A 1 529 ? -20.761 -31.322 17.498  1.00 25.22 ? 549  VAL A C     1 
ATOM   4079  O  O     . VAL A 1 529 ? -21.782 -32.000 17.657  1.00 25.27 ? 549  VAL A O     1 
ATOM   4080  C  CB    . VAL A 1 529 ? -21.489 -30.059 15.447  1.00 25.67 ? 549  VAL A CB    1 
ATOM   4081  C  CG1   . VAL A 1 529 ? -22.103 -29.066 16.444  1.00 24.69 ? 549  VAL A CG1   1 
ATOM   4082  C  CG2   . VAL A 1 529 ? -20.968 -29.352 14.180  1.00 24.26 ? 549  VAL A CG2   1 
ATOM   4083  N  N     . VAL A 1 530 ? -19.956 -30.976 18.499  1.00 24.69 ? 550  VAL A N     1 
ATOM   4084  C  CA    . VAL A 1 530 ? -20.322 -31.205 19.901  1.00 24.29 ? 550  VAL A CA    1 
ATOM   4085  C  C     . VAL A 1 530 ? -20.767 -29.869 20.480  1.00 23.82 ? 550  VAL A C     1 
ATOM   4086  O  O     . VAL A 1 530 ? -19.960 -28.951 20.590  1.00 23.42 ? 550  VAL A O     1 
ATOM   4087  C  CB    . VAL A 1 530 ? -19.146 -31.764 20.725  1.00 24.34 ? 550  VAL A CB    1 
ATOM   4088  C  CG1   . VAL A 1 530 ? -19.534 -31.881 22.192  1.00 23.36 ? 550  VAL A CG1   1 
ATOM   4089  C  CG2   . VAL A 1 530 ? -18.705 -33.133 20.171  1.00 24.93 ? 550  VAL A CG2   1 
ATOM   4090  N  N     . GLN A 1 531 ? -22.044 -29.751 20.836  1.00 23.33 ? 551  GLN A N     1 
ATOM   4091  C  CA    . GLN A 1 531 ? -22.604 -28.435 21.162  1.00 23.36 ? 551  GLN A CA    1 
ATOM   4092  C  C     . GLN A 1 531 ? -23.755 -28.453 22.173  1.00 23.27 ? 551  GLN A C     1 
ATOM   4093  O  O     . GLN A 1 531 ? -24.443 -29.479 22.332  1.00 23.03 ? 551  GLN A O     1 
ATOM   4094  C  CB    . GLN A 1 531 ? -23.097 -27.752 19.890  1.00 23.43 ? 551  GLN A CB    1 
ATOM   4095  C  CG    . GLN A 1 531 ? -24.377 -28.386 19.312  1.00 24.03 ? 551  GLN A CG    1 
ATOM   4096  C  CD    . GLN A 1 531 ? -25.091 -27.475 18.362  1.00 23.85 ? 551  GLN A CD    1 
ATOM   4097  O  OE1   . GLN A 1 531 ? -24.811 -26.284 18.318  1.00 25.10 ? 551  GLN A OE1   1 
ATOM   4098  N  NE2   . GLN A 1 531 ? -26.035 -28.023 17.599  1.00 24.15 ? 551  GLN A NE2   1 
ATOM   4099  N  N     . PRO A 1 532 ? -23.972 -27.306 22.842  1.00 22.68 ? 552  PRO A N     1 
ATOM   4100  C  CA    . PRO A 1 532 ? -25.069 -27.141 23.790  1.00 22.84 ? 552  PRO A CA    1 
ATOM   4101  C  C     . PRO A 1 532 ? -26.440 -27.369 23.182  1.00 22.43 ? 552  PRO A C     1 
ATOM   4102  O  O     . PRO A 1 532 ? -26.697 -26.975 22.043  1.00 21.83 ? 552  PRO A O     1 
ATOM   4103  C  CB    . PRO A 1 532 ? -24.954 -25.667 24.204  1.00 22.70 ? 552  PRO A CB    1 
ATOM   4104  C  CG    . PRO A 1 532 ? -23.536 -25.353 24.054  1.00 22.88 ? 552  PRO A CG    1 
ATOM   4105  C  CD    . PRO A 1 532 ? -23.080 -26.133 22.850  1.00 22.81 ? 552  PRO A CD    1 
ATOM   4106  N  N     . THR A 1 533 ? -27.301 -28.007 23.956  1.00 22.57 ? 553  THR A N     1 
ATOM   4107  C  CA    . THR A 1 533 ? -28.729 -28.003 23.695  1.00 22.55 ? 553  THR A CA    1 
ATOM   4108  C  C     . THR A 1 533 ? -29.445 -27.599 24.972  1.00 22.91 ? 553  THR A C     1 
ATOM   4109  O  O     . THR A 1 533 ? -28.859 -27.620 26.050  1.00 22.32 ? 553  THR A O     1 
ATOM   4110  C  CB    . THR A 1 533 ? -29.216 -29.381 23.257  1.00 22.74 ? 553  THR A CB    1 
ATOM   4111  O  OG1   . THR A 1 533 ? -29.178 -30.284 24.372  1.00 21.85 ? 553  THR A OG1   1 
ATOM   4112  C  CG2   . THR A 1 533 ? -28.339 -29.923 22.110  1.00 22.36 ? 553  THR A CG2   1 
ATOM   4113  N  N     . LEU A 1 534 ? -30.713 -27.227 24.832  1.00 23.65 ? 554  LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 534 ? -31.548 -26.808 25.946  1.00 24.72 ? 554  LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 534 ? -32.366 -28.015 26.385  1.00 25.26 ? 554  LEU A C     1 
ATOM   4116  O  O     . LEU A 1 534 ? -33.140 -28.548 25.595  1.00 25.74 ? 554  LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 534 ? -32.471 -25.660 25.500  1.00 24.98 ? 554  LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 534 ? -33.582 -25.148 26.420  1.00 25.91 ? 554  LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 534 ? -33.046 -24.807 27.774  1.00 27.28 ? 554  LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 534 ? -34.237 -23.921 25.808  1.00 27.52 ? 554  LEU A CD2   1 
ATOM   4121  N  N     . GLU A 1 535 ? -32.186 -28.436 27.636  1.00 25.77 ? 555  GLU A N     1 
ATOM   4122  C  CA    . GLU A 1 535 ? -32.946 -29.538 28.249  1.00 26.22 ? 555  GLU A CA    1 
ATOM   4123  C  C     . GLU A 1 535 ? -33.933 -28.999 29.296  1.00 26.02 ? 555  GLU A C     1 
ATOM   4124  O  O     . GLU A 1 535 ? -33.522 -28.285 30.217  1.00 25.52 ? 555  GLU A O     1 
ATOM   4125  C  CB    . GLU A 1 535 ? -31.964 -30.480 28.939  1.00 26.97 ? 555  GLU A CB    1 
ATOM   4126  C  CG    . GLU A 1 535 ? -32.552 -31.741 29.546  1.00 29.19 ? 555  GLU A CG    1 
ATOM   4127  C  CD    . GLU A 1 535 ? -31.510 -32.512 30.349  1.00 32.00 ? 555  GLU A CD    1 
ATOM   4128  O  OE1   . GLU A 1 535 ? -31.060 -33.581 29.871  1.00 35.20 ? 555  GLU A OE1   1 
ATOM   4129  O  OE2   . GLU A 1 535 ? -31.123 -32.035 31.442  1.00 31.99 ? 555  GLU A OE2   1 
ATOM   4130  N  N     . GLN A 1 536 ? -35.213 -29.350 29.151  1.00 25.63 ? 556  GLN A N     1 
ATOM   4131  C  CA    . GLN A 1 536 ? -36.256 -29.038 30.135  1.00 25.83 ? 556  GLN A CA    1 
ATOM   4132  C  C     . GLN A 1 536 ? -36.523 -30.255 31.017  1.00 25.16 ? 556  GLN A C     1 
ATOM   4133  O  O     . GLN A 1 536 ? -36.626 -31.371 30.515  1.00 25.29 ? 556  GLN A O     1 
ATOM   4134  C  CB    . GLN A 1 536 ? -37.591 -28.715 29.451  1.00 26.64 ? 556  GLN A CB    1 
ATOM   4135  C  CG    . GLN A 1 536 ? -37.635 -27.488 28.573  1.00 29.24 ? 556  GLN A CG    1 
ATOM   4136  C  CD    . GLN A 1 536 ? -39.070 -26.978 28.345  1.00 33.37 ? 556  GLN A CD    1 
ATOM   4137  O  OE1   . GLN A 1 536 ? -39.935 -27.075 29.231  1.00 36.10 ? 556  GLN A OE1   1 
ATOM   4138  N  NE2   . GLN A 1 536 ? -39.317 -26.420 27.163  1.00 34.47 ? 556  GLN A NE2   1 
ATOM   4139  N  N     . THR A 1 537 ? -36.660 -30.041 32.321  1.00 24.36 ? 557  THR A N     1 
ATOM   4140  C  CA    . THR A 1 537 ? -37.120 -31.086 33.229  1.00 23.72 ? 557  THR A CA    1 
ATOM   4141  C  C     . THR A 1 537 ? -38.379 -30.624 33.951  1.00 23.51 ? 557  THR A C     1 
ATOM   4142  O  O     . THR A 1 537 ? -38.398 -29.554 34.554  1.00 23.41 ? 557  THR A O     1 
ATOM   4143  C  CB    . THR A 1 537 ? -36.060 -31.443 34.267  1.00 23.83 ? 557  THR A CB    1 
ATOM   4144  O  OG1   . THR A 1 537 ? -34.836 -31.773 33.607  1.00 22.80 ? 557  THR A OG1   1 
ATOM   4145  C  CG2   . THR A 1 537 ? -36.530 -32.617 35.131  1.00 22.41 ? 557  THR A CG2   1 
ATOM   4146  N  N     . GLN A 1 538 ? -39.422 -31.440 33.881  1.00 23.25 ? 558  GLN A N     1 
ATOM   4147  C  CA    . GLN A 1 538 ? -40.676 -31.180 34.575  1.00 23.43 ? 558  GLN A CA    1 
ATOM   4148  C  C     . GLN A 1 538 ? -40.666 -31.900 35.916  1.00 22.60 ? 558  GLN A C     1 
ATOM   4149  O  O     . GLN A 1 538 ? -39.959 -32.878 36.086  1.00 23.22 ? 558  GLN A O     1 
ATOM   4150  C  CB    . GLN A 1 538 ? -41.861 -31.659 33.741  1.00 23.74 ? 558  GLN A CB    1 
ATOM   4151  C  CG    . GLN A 1 538 ? -41.815 -31.229 32.296  1.00 26.04 ? 558  GLN A CG    1 
ATOM   4152  C  CD    . GLN A 1 538 ? -41.557 -29.745 32.149  1.00 29.02 ? 558  GLN A CD    1 
ATOM   4153  O  OE1   . GLN A 1 538 ? -42.132 -28.930 32.877  1.00 33.20 ? 558  GLN A OE1   1 
ATOM   4154  N  NE2   . GLN A 1 538 ? -40.681 -29.384 31.220  1.00 30.90 ? 558  GLN A NE2   1 
ATOM   4155  N  N     . TYR A 1 539 ? -41.431 -31.384 36.865  1.00 21.76 ? 559  TYR A N     1 
ATOM   4156  C  CA    . TYR A 1 539 ? -41.498 -31.924 38.218  1.00 20.86 ? 559  TYR A CA    1 
ATOM   4157  C  C     . TYR A 1 539 ? -42.968 -32.101 38.551  1.00 21.04 ? 559  TYR A C     1 
ATOM   4158  O  O     . TYR A 1 539 ? -43.755 -31.170 38.375  1.00 20.87 ? 559  TYR A O     1 
ATOM   4159  C  CB    . TYR A 1 539 ? -40.824 -30.969 39.210  1.00 20.32 ? 559  TYR A CB    1 
ATOM   4160  C  CG    . TYR A 1 539 ? -39.328 -30.829 38.985  1.00 18.48 ? 559  TYR A CG    1 
ATOM   4161  C  CD1   . TYR A 1 539 ? -38.836 -30.117 37.901  1.00 16.97 ? 559  TYR A CD1   1 
ATOM   4162  C  CD2   . TYR A 1 539 ? -38.415 -31.412 39.845  1.00 16.92 ? 559  TYR A CD2   1 
ATOM   4163  C  CE1   . TYR A 1 539 ? -37.480 -29.999 37.674  1.00 17.46 ? 559  TYR A CE1   1 
ATOM   4164  C  CE2   . TYR A 1 539 ? -37.044 -31.302 39.625  1.00 17.06 ? 559  TYR A CE2   1 
ATOM   4165  C  CZ    . TYR A 1 539 ? -36.587 -30.596 38.531  1.00 16.91 ? 559  TYR A CZ    1 
ATOM   4166  O  OH    . TYR A 1 539 ? -35.235 -30.467 38.296  1.00 17.85 ? 559  TYR A OH    1 
ATOM   4167  N  N     . SER A 1 540 ? -43.342 -33.297 39.006  1.00 21.07 ? 560  SER A N     1 
ATOM   4168  C  CA    . SER A 1 540 ? -44.742 -33.613 39.294  1.00 21.04 ? 560  SER A CA    1 
ATOM   4169  C  C     . SER A 1 540 ? -45.050 -33.775 40.779  1.00 20.20 ? 560  SER A C     1 
ATOM   4170  O  O     . SER A 1 540 ? -46.197 -33.673 41.171  1.00 19.89 ? 560  SER A O     1 
ATOM   4171  C  CB    . SER A 1 540 ? -45.143 -34.900 38.569  1.00 21.50 ? 560  SER A CB    1 
ATOM   4172  O  OG    . SER A 1 540 ? -45.307 -34.659 37.186  1.00 23.32 ? 560  SER A OG    1 
ATOM   4173  N  N     . TRP A 1 541 ? -44.041 -34.054 41.599  1.00 20.21 ? 561  TRP A N     1 
ATOM   4174  C  CA    . TRP A 1 541 ? -44.270 -34.359 43.019  1.00 19.76 ? 561  TRP A CA    1 
ATOM   4175  C  C     . TRP A 1 541 ? -43.309 -33.608 43.925  1.00 19.54 ? 561  TRP A C     1 
ATOM   4176  O  O     . TRP A 1 541 ? -42.152 -33.386 43.571  1.00 20.08 ? 561  TRP A O     1 
ATOM   4177  C  CB    . TRP A 1 541 ? -44.162 -35.862 43.251  1.00 19.60 ? 561  TRP A CB    1 
ATOM   4178  C  CG    . TRP A 1 541 ? -44.969 -36.663 42.275  1.00 19.50 ? 561  TRP A CG    1 
ATOM   4179  C  CD1   . TRP A 1 541 ? -44.542 -37.166 41.082  1.00 19.33 ? 561  TRP A CD1   1 
ATOM   4180  C  CD2   . TRP A 1 541 ? -46.344 -37.049 42.407  1.00 18.19 ? 561  TRP A CD2   1 
ATOM   4181  N  NE1   . TRP A 1 541 ? -45.568 -37.835 40.460  1.00 19.64 ? 561  TRP A NE1   1 
ATOM   4182  C  CE2   . TRP A 1 541 ? -46.687 -37.771 41.245  1.00 18.83 ? 561  TRP A CE2   1 
ATOM   4183  C  CE3   . TRP A 1 541 ? -47.322 -36.848 43.389  1.00 17.84 ? 561  TRP A CE3   1 
ATOM   4184  C  CZ2   . TRP A 1 541 ? -47.966 -38.313 41.045  1.00 18.53 ? 561  TRP A CZ2   1 
ATOM   4185  C  CZ3   . TRP A 1 541 ? -48.597 -37.377 43.184  1.00 17.46 ? 561  TRP A CZ3   1 
ATOM   4186  C  CH2   . TRP A 1 541 ? -48.903 -38.101 42.023  1.00 16.51 ? 561  TRP A CH2   1 
ATOM   4187  N  N     . GLU A 1 542 ? -43.788 -33.219 45.103  1.00 19.47 ? 562  GLU A N     1 
ATOM   4188  C  CA    . GLU A 1 542 ? -42.990 -32.392 46.012  1.00 19.17 ? 562  GLU A CA    1 
ATOM   4189  C  C     . GLU A 1 542 ? -41.573 -32.917 46.194  1.00 19.29 ? 562  GLU A C     1 
ATOM   4190  O  O     . GLU A 1 542 ? -40.620 -32.153 46.097  1.00 19.85 ? 562  GLU A O     1 
ATOM   4191  C  CB    . GLU A 1 542 ? -43.668 -32.271 47.374  1.00 19.03 ? 562  GLU A CB    1 
ATOM   4192  C  CG    . GLU A 1 542 ? -44.927 -31.416 47.362  1.00 19.33 ? 562  GLU A CG    1 
ATOM   4193  C  CD    . GLU A 1 542 ? -45.624 -31.396 48.700  1.00 19.62 ? 562  GLU A CD    1 
ATOM   4194  O  OE1   . GLU A 1 542 ? -45.775 -32.485 49.315  1.00 17.70 ? 562  GLU A OE1   1 
ATOM   4195  O  OE2   . GLU A 1 542 ? -46.026 -30.291 49.146  1.00 18.53 ? 562  GLU A OE2   1 
ATOM   4196  N  N     . ARG A 1 543 ? -41.433 -34.222 46.427  1.00 19.51 ? 563  ARG A N     1 
ATOM   4197  C  CA    A ARG A 1 543 ? -40.132 -34.821 46.729  0.60 19.67 ? 563  ARG A CA    1 
ATOM   4198  C  CA    B ARG A 1 543 ? -40.131 -34.802 46.733  0.40 19.55 ? 563  ARG A CA    1 
ATOM   4199  C  C     . ARG A 1 543 ? -39.136 -34.623 45.587  1.00 19.87 ? 563  ARG A C     1 
ATOM   4200  O  O     . ARG A 1 543 ? -37.941 -34.505 45.820  1.00 20.06 ? 563  ARG A O     1 
ATOM   4201  C  CB    A ARG A 1 543 ? -40.262 -36.320 47.043  0.60 19.59 ? 563  ARG A CB    1 
ATOM   4202  C  CB    B ARG A 1 543 ? -40.277 -36.282 47.091  0.40 19.37 ? 563  ARG A CB    1 
ATOM   4203  C  CG    A ARG A 1 543 ? -40.913 -36.658 48.393  0.60 19.58 ? 563  ARG A CG    1 
ATOM   4204  C  CG    B ARG A 1 543 ? -38.979 -36.965 47.485  0.40 18.83 ? 563  ARG A CG    1 
ATOM   4205  C  CD    A ARG A 1 543 ? -39.998 -36.399 49.588  0.60 19.45 ? 563  ARG A CD    1 
ATOM   4206  C  CD    B ARG A 1 543 ? -38.143 -36.153 48.458  0.40 17.32 ? 563  ARG A CD    1 
ATOM   4207  N  NE    A ARG A 1 543 ? -40.476 -37.076 50.799  0.60 19.75 ? 563  ARG A NE    1 
ATOM   4208  N  NE    B ARG A 1 543 ? -38.695 -36.153 49.808  0.40 16.09 ? 563  ARG A NE    1 
ATOM   4209  C  CZ    A ARG A 1 543 ? -39.893 -37.011 52.000  0.60 19.14 ? 563  ARG A CZ    1 
ATOM   4210  C  CZ    B ARG A 1 543 ? -38.158 -35.494 50.832  0.40 14.32 ? 563  ARG A CZ    1 
ATOM   4211  N  NH1   A ARG A 1 543 ? -38.797 -36.287 52.194  0.60 18.83 ? 563  ARG A NH1   1 
ATOM   4212  N  NH1   B ARG A 1 543 ? -37.045 -34.786 50.664  0.40 11.79 ? 563  ARG A NH1   1 
ATOM   4213  N  NH2   A ARG A 1 543 ? -40.413 -37.677 53.025  0.60 20.15 ? 563  ARG A NH2   1 
ATOM   4214  N  NH2   B ARG A 1 543 ? -38.733 -35.550 52.026  0.40 14.91 ? 563  ARG A NH2   1 
ATOM   4215  N  N     . GLN A 1 544 ? -39.630 -34.592 44.352  1.00 20.17 ? 564  GLN A N     1 
ATOM   4216  C  CA    . GLN A 1 544 ? -38.754 -34.376 43.206  1.00 20.69 ? 564  GLN A CA    1 
ATOM   4217  C  C     . GLN A 1 544 ? -38.169 -32.957 43.212  1.00 20.88 ? 564  GLN A C     1 
ATOM   4218  O  O     . GLN A 1 544 ? -37.070 -32.734 42.701  1.00 21.24 ? 564  GLN A O     1 
ATOM   4219  C  CB    . GLN A 1 544 ? -39.518 -34.600 41.901  1.00 21.08 ? 564  GLN A CB    1 
ATOM   4220  C  CG    . GLN A 1 544 ? -40.022 -36.017 41.692  1.00 19.73 ? 564  GLN A CG    1 
ATOM   4221  C  CD    . GLN A 1 544 ? -40.938 -36.099 40.495  1.00 19.60 ? 564  GLN A CD    1 
ATOM   4222  O  OE1   . GLN A 1 544 ? -41.741 -35.198 40.268  1.00 19.06 ? 564  GLN A OE1   1 
ATOM   4223  N  NE2   . GLN A 1 544 ? -40.821 -37.177 39.716  1.00 17.92 ? 564  GLN A NE2   1 
ATOM   4224  N  N     . ALA A 1 545 ? -38.918 -32.010 43.782  1.00 20.82 ? 565  ALA A N     1 
ATOM   4225  C  CA    . ALA A 1 545 ? -38.526 -30.597 43.808  1.00 20.86 ? 565  ALA A CA    1 
ATOM   4226  C  C     . ALA A 1 545 ? -37.905 -30.188 45.160  1.00 20.95 ? 565  ALA A C     1 
ATOM   4227  O  O     . ALA A 1 545 ? -37.769 -28.990 45.446  1.00 20.57 ? 565  ALA A O     1 
ATOM   4228  C  CB    . ALA A 1 545 ? -39.736 -29.722 43.487  1.00 20.57 ? 565  ALA A CB    1 
ATOM   4229  N  N     . ALA A 1 546 ? -37.536 -31.178 45.976  1.00 21.04 ? 566  ALA A N     1 
ATOM   4230  C  CA    . ALA A 1 546 ? -36.854 -30.942 47.245  1.00 21.46 ? 566  ALA A CA    1 
ATOM   4231  C  C     . ALA A 1 546 ? -35.358 -31.152 47.037  1.00 21.84 ? 566  ALA A C     1 
ATOM   4232  O  O     . ALA A 1 546 ? -34.876 -32.274 47.080  1.00 22.14 ? 566  ALA A O     1 
ATOM   4233  C  CB    . ALA A 1 546 ? -37.377 -31.887 48.327  1.00 21.48 ? 566  ALA A CB    1 
ATOM   4234  N  N     . PHE A 1 547 ? -34.625 -30.070 46.817  1.00 22.20 ? 567  PHE A N     1 
ATOM   4235  C  CA    . PHE A 1 547 ? -33.212 -30.167 46.466  1.00 22.60 ? 567  PHE A CA    1 
ATOM   4236  C  C     . PHE A 1 547 ? -32.368 -30.115 47.715  1.00 23.97 ? 567  PHE A C     1 
ATOM   4237  O  O     . PHE A 1 547 ? -32.383 -29.117 48.421  1.00 24.20 ? 567  PHE A O     1 
ATOM   4238  C  CB    . PHE A 1 547 ? -32.819 -29.026 45.522  1.00 22.32 ? 567  PHE A CB    1 
ATOM   4239  C  CG    . PHE A 1 547 ? -33.501 -29.089 44.192  1.00 20.31 ? 567  PHE A CG    1 
ATOM   4240  C  CD1   . PHE A 1 547 ? -32.909 -29.754 43.126  1.00 20.78 ? 567  PHE A CD1   1 
ATOM   4241  C  CD2   . PHE A 1 547 ? -34.749 -28.521 44.014  1.00 19.12 ? 567  PHE A CD2   1 
ATOM   4242  C  CE1   . PHE A 1 547 ? -33.551 -29.839 41.893  1.00 19.84 ? 567  PHE A CE1   1 
ATOM   4243  C  CE2   . PHE A 1 547 ? -35.396 -28.591 42.793  1.00 18.97 ? 567  PHE A CE2   1 
ATOM   4244  C  CZ    . PHE A 1 547 ? -34.795 -29.250 41.727  1.00 18.92 ? 567  PHE A CZ    1 
ATOM   4245  N  N     . ARG A 1 548 ? -31.639 -31.188 47.992  1.00 25.52 ? 568  ARG A N     1 
ATOM   4246  C  CA    . ARG A 1 548 ? -30.723 -31.220 49.129  1.00 27.17 ? 568  ARG A CA    1 
ATOM   4247  C  C     . ARG A 1 548 ? -29.415 -30.563 48.721  1.00 27.98 ? 568  ARG A C     1 
ATOM   4248  O  O     . ARG A 1 548 ? -29.177 -30.338 47.538  1.00 28.06 ? 568  ARG A O     1 
ATOM   4249  C  CB    . ARG A 1 548 ? -30.479 -32.655 49.597  1.00 27.31 ? 568  ARG A CB    1 
ATOM   4250  C  CG    . ARG A 1 548 ? -31.711 -33.335 50.177  1.00 28.06 ? 568  ARG A CG    1 
ATOM   4251  C  CD    . ARG A 1 548 ? -31.532 -34.856 50.242  1.00 29.83 ? 568  ARG A CD    1 
ATOM   4252  N  N     . PHE A 1 549 ? -28.578 -30.250 49.702  1.00 29.29 ? 569  PHE A N     1 
ATOM   4253  C  CA    . PHE A 1 549 ? -27.305 -29.583 49.443  1.00 30.53 ? 569  PHE A CA    1 
ATOM   4254  C  C     . PHE A 1 549 ? -26.320 -30.468 48.675  1.00 31.86 ? 569  PHE A C     1 
ATOM   4255  O  O     . PHE A 1 549 ? -25.459 -29.956 47.968  1.00 32.44 ? 569  PHE A O     1 
ATOM   4256  C  CB    . PHE A 1 549 ? -26.661 -29.085 50.750  1.00 30.58 ? 569  PHE A CB    1 
ATOM   4257  C  CG    . PHE A 1 549 ? -27.201 -27.767 51.221  1.00 30.62 ? 569  PHE A CG    1 
ATOM   4258  C  CD1   . PHE A 1 549 ? -28.086 -27.696 52.286  1.00 30.58 ? 569  PHE A CD1   1 
ATOM   4259  C  CD2   . PHE A 1 549 ? -26.844 -26.591 50.570  1.00 30.69 ? 569  PHE A CD2   1 
ATOM   4260  C  CE1   . PHE A 1 549 ? -28.598 -26.468 52.706  1.00 30.78 ? 569  PHE A CE1   1 
ATOM   4261  C  CE2   . PHE A 1 549 ? -27.345 -25.362 50.992  1.00 30.86 ? 569  PHE A CE2   1 
ATOM   4262  C  CZ    . PHE A 1 549 ? -28.226 -25.304 52.060  1.00 30.97 ? 569  PHE A CZ    1 
ATOM   4263  N  N     . LYS A 1 550 ? -26.433 -31.784 48.825  1.00 33.31 ? 570  LYS A N     1 
ATOM   4264  C  CA    . LYS A 1 550 ? -25.594 -32.721 48.062  1.00 34.43 ? 570  LYS A CA    1 
ATOM   4265  C  C     . LYS A 1 550 ? -25.975 -32.718 46.582  1.00 35.08 ? 570  LYS A C     1 
ATOM   4266  O  O     . LYS A 1 550 ? -25.109 -32.781 45.715  1.00 36.14 ? 570  LYS A O     1 
ATOM   4267  C  CB    . LYS A 1 550 ? -25.727 -34.142 48.620  1.00 34.45 ? 570  LYS A CB    1 
ATOM   4268  N  N     . ARG A 1 551 ? -27.275 -32.628 46.306  1.00 35.47 ? 571  ARG A N     1 
ATOM   4269  C  CA    . ARG A 1 551 ? -27.807 -32.645 44.938  1.00 35.42 ? 571  ARG A CA    1 
ATOM   4270  C  C     . ARG A 1 551 ? -27.319 -31.449 44.113  1.00 35.06 ? 571  ARG A C     1 
ATOM   4271  O  O     . ARG A 1 551 ? -27.117 -30.338 44.648  1.00 35.27 ? 571  ARG A O     1 
ATOM   4272  C  CB    . ARG A 1 551 ? -29.345 -32.645 44.991  1.00 35.81 ? 571  ARG A CB    1 
ATOM   4273  C  CG    . ARG A 1 551 ? -30.081 -32.993 43.674  1.00 36.86 ? 571  ARG A CG    1 
ATOM   4274  C  CD    . ARG A 1 551 ? -31.568 -33.197 43.982  1.00 37.69 ? 571  ARG A CD    1 
ATOM   4275  N  NE    . ARG A 1 551 ? -32.425 -33.482 42.829  1.00 37.52 ? 571  ARG A NE    1 
ATOM   4276  C  CZ    . ARG A 1 551 ? -33.755 -33.589 42.899  1.00 37.85 ? 571  ARG A CZ    1 
ATOM   4277  N  NH1   . ARG A 1 551 ? -34.380 -33.421 44.059  1.00 38.77 ? 571  ARG A NH1   1 
ATOM   4278  N  NH2   . ARG A 1 551 ? -34.473 -33.851 41.810  1.00 37.76 ? 571  ARG A NH2   1 
ATOM   4279  N  N     . LYS A 1 552 ? -27.125 -31.682 42.813  1.00 33.95 ? 572  LYS A N     1 
ATOM   4280  C  CA    . LYS A 1 552 ? -26.789 -30.610 41.870  1.00 32.97 ? 572  LYS A CA    1 
ATOM   4281  C  C     . LYS A 1 552 ? -28.018 -29.719 41.675  1.00 31.58 ? 572  LYS A C     1 
ATOM   4282  O  O     . LYS A 1 552 ? -29.093 -30.218 41.334  1.00 31.92 ? 572  LYS A O     1 
ATOM   4283  C  CB    . LYS A 1 552 ? -26.349 -31.198 40.521  1.00 32.99 ? 572  LYS A CB    1 
ATOM   4284  N  N     . LEU A 1 553 ? -27.866 -28.415 41.919  1.00 29.99 ? 573  LEU A N     1 
ATOM   4285  C  CA    . LEU A 1 553 ? -28.983 -27.464 41.803  1.00 28.19 ? 573  LEU A CA    1 
ATOM   4286  C  C     . LEU A 1 553 ? -28.979 -26.924 40.374  1.00 26.68 ? 573  LEU A C     1 
ATOM   4287  O  O     . LEU A 1 553 ? -28.006 -26.310 39.963  1.00 25.82 ? 573  LEU A O     1 
ATOM   4288  C  CB    . LEU A 1 553 ? -28.835 -26.324 42.828  1.00 28.16 ? 573  LEU A CB    1 
ATOM   4289  C  CG    . LEU A 1 553 ? -30.068 -25.516 43.265  1.00 27.11 ? 573  LEU A CG    1 
ATOM   4290  C  CD1   . LEU A 1 553 ? -31.178 -26.383 43.861  1.00 25.06 ? 573  LEU A CD1   1 
ATOM   4291  C  CD2   . LEU A 1 553 ? -29.684 -24.435 44.278  1.00 25.82 ? 573  LEU A CD2   1 
ATOM   4292  N  N     . PRO A 1 554 ? -30.056 -27.168 39.605  1.00 25.64 ? 574  PRO A N     1 
ATOM   4293  C  CA    . PRO A 1 554 ? -30.081 -26.661 38.229  1.00 24.81 ? 574  PRO A CA    1 
ATOM   4294  C  C     . PRO A 1 554 ? -29.927 -25.140 38.159  1.00 24.04 ? 574  PRO A C     1 
ATOM   4295  O  O     . PRO A 1 554 ? -30.256 -24.423 39.123  1.00 22.71 ? 574  PRO A O     1 
ATOM   4296  C  CB    . PRO A 1 554 ? -31.454 -27.094 37.711  1.00 24.93 ? 574  PRO A CB    1 
ATOM   4297  C  CG    . PRO A 1 554 ? -31.858 -28.220 38.589  1.00 25.40 ? 574  PRO A CG    1 
ATOM   4298  C  CD    . PRO A 1 554 ? -31.277 -27.930 39.927  1.00 25.54 ? 574  PRO A CD    1 
ATOM   4299  N  N     . LYS A 1 555 ? -29.410 -24.677 37.022  1.00 23.30 ? 575  LYS A N     1 
ATOM   4300  C  CA    . LYS A 1 555 ? -29.093 -23.272 36.812  1.00 22.95 ? 575  LYS A CA    1 
ATOM   4301  C  C     . LYS A 1 555 ? -30.336 -22.448 36.580  1.00 22.16 ? 575  LYS A C     1 
ATOM   4302  O  O     . LYS A 1 555 ? -30.333 -21.252 36.866  1.00 22.75 ? 575  LYS A O     1 
ATOM   4303  C  CB    . LYS A 1 555 ? -28.120 -23.108 35.634  1.00 23.47 ? 575  LYS A CB    1 
ATOM   4304  C  CG    . LYS A 1 555 ? -26.750 -23.770 35.869  1.00 23.37 ? 575  LYS A CG    1 
ATOM   4305  N  N     . TYR A 1 556 ? -31.394 -23.072 36.065  1.00 20.92 ? 576  TYR A N     1 
ATOM   4306  C  CA    . TYR A 1 556 ? -32.684 -22.396 35.895  1.00 20.01 ? 576  TYR A CA    1 
ATOM   4307  C  C     . TYR A 1 556 ? -33.774 -23.084 36.694  1.00 19.21 ? 576  TYR A C     1 
ATOM   4308  O  O     . TYR A 1 556 ? -34.206 -24.192 36.358  1.00 18.86 ? 576  TYR A O     1 
ATOM   4309  C  CB    . TYR A 1 556 ? -33.079 -22.317 34.413  1.00 19.73 ? 576  TYR A CB    1 
ATOM   4310  C  CG    . TYR A 1 556 ? -32.374 -21.196 33.702  1.00 20.43 ? 576  TYR A CG    1 
ATOM   4311  C  CD1   . TYR A 1 556 ? -31.013 -21.283 33.403  1.00 20.42 ? 576  TYR A CD1   1 
ATOM   4312  C  CD2   . TYR A 1 556 ? -33.051 -20.024 33.361  1.00 20.14 ? 576  TYR A CD2   1 
ATOM   4313  C  CE1   . TYR A 1 556 ? -30.358 -20.244 32.759  1.00 19.96 ? 576  TYR A CE1   1 
ATOM   4314  C  CE2   . TYR A 1 556 ? -32.405 -18.990 32.723  1.00 20.05 ? 576  TYR A CE2   1 
ATOM   4315  C  CZ    . TYR A 1 556 ? -31.055 -19.104 32.423  1.00 19.98 ? 576  TYR A CZ    1 
ATOM   4316  O  OH    . TYR A 1 556 ? -30.401 -18.053 31.803  1.00 20.28 ? 576  TYR A OH    1 
ATOM   4317  N  N     . LEU A 1 557 ? -34.208 -22.413 37.753  1.00 18.32 ? 577  LEU A N     1 
ATOM   4318  C  CA    . LEU A 1 557 ? -35.275 -22.900 38.616  1.00 17.99 ? 577  LEU A CA    1 
ATOM   4319  C  C     . LEU A 1 557 ? -36.492 -22.038 38.307  1.00 17.98 ? 577  LEU A C     1 
ATOM   4320  O  O     . LEU A 1 557 ? -36.545 -20.867 38.694  1.00 18.16 ? 577  LEU A O     1 
ATOM   4321  C  CB    . LEU A 1 557 ? -34.851 -22.793 40.091  1.00 17.57 ? 577  LEU A CB    1 
ATOM   4322  C  CG    . LEU A 1 557 ? -33.461 -23.367 40.439  1.00 17.58 ? 577  LEU A CG    1 
ATOM   4323  C  CD1   . LEU A 1 557 ? -32.942 -22.858 41.797  1.00 14.81 ? 577  LEU A CD1   1 
ATOM   4324  C  CD2   . LEU A 1 557 ? -33.469 -24.892 40.423  1.00 14.76 ? 577  LEU A CD2   1 
ATOM   4325  N  N     . LEU A 1 558 ? -37.445 -22.598 37.571  1.00 18.26 ? 578  LEU A N     1 
ATOM   4326  C  CA    . LEU A 1 558 ? -38.559 -21.824 37.030  1.00 18.35 ? 578  LEU A CA    1 
ATOM   4327  C  C     . LEU A 1 558 ? -39.909 -22.187 37.667  1.00 18.41 ? 578  LEU A C     1 
ATOM   4328  O  O     . LEU A 1 558 ? -40.232 -23.374 37.844  1.00 18.10 ? 578  LEU A O     1 
ATOM   4329  C  CB    . LEU A 1 558 ? -38.657 -22.032 35.512  1.00 18.51 ? 578  LEU A CB    1 
ATOM   4330  C  CG    . LEU A 1 558 ? -37.426 -21.690 34.661  1.00 20.24 ? 578  LEU A CG    1 
ATOM   4331  C  CD1   . LEU A 1 558 ? -37.739 -21.918 33.185  1.00 19.81 ? 578  LEU A CD1   1 
ATOM   4332  C  CD2   . LEU A 1 558 ? -36.957 -20.258 34.902  1.00 20.15 ? 578  LEU A CD2   1 
ATOM   4333  N  N     . PHE A 1 559 ? -40.682 -21.156 37.997  1.00 17.95 ? 579  PHE A N     1 
ATOM   4334  C  CA    . PHE A 1 559 ? -42.073 -21.313 38.418  1.00 18.05 ? 579  PHE A CA    1 
ATOM   4335  C  C     . PHE A 1 559 ? -42.943 -20.750 37.319  1.00 18.21 ? 579  PHE A C     1 
ATOM   4336  O  O     . PHE A 1 559 ? -42.837 -19.573 36.986  1.00 17.72 ? 579  PHE A O     1 
ATOM   4337  C  CB    . PHE A 1 559 ? -42.297 -20.657 39.773  1.00 17.85 ? 579  PHE A CB    1 
ATOM   4338  C  CG    . PHE A 1 559 ? -41.512 -21.327 40.865  1.00 17.72 ? 579  PHE A CG    1 
ATOM   4339  C  CD1   . PHE A 1 559 ? -40.158 -21.092 41.000  1.00 17.01 ? 579  PHE A CD1   1 
ATOM   4340  C  CD2   . PHE A 1 559 ? -42.112 -22.246 41.707  1.00 16.92 ? 579  PHE A CD2   1 
ATOM   4341  C  CE1   . PHE A 1 559 ? -39.418 -21.743 41.980  1.00 17.18 ? 579  PHE A CE1   1 
ATOM   4342  C  CE2   . PHE A 1 559 ? -41.388 -22.897 42.669  1.00 16.43 ? 579  PHE A CE2   1 
ATOM   4343  C  CZ    . PHE A 1 559 ? -40.028 -22.648 42.807  1.00 16.12 ? 579  PHE A CZ    1 
ATOM   4344  N  N     . THR A 1 560 ? -43.746 -21.619 36.706  1.00 19.09 ? 580  THR A N     1 
ATOM   4345  C  CA    . THR A 1 560 ? -44.416 -21.297 35.447  1.00 20.12 ? 580  THR A CA    1 
ATOM   4346  C  C     . THR A 1 560 ? -45.934 -21.220 35.567  1.00 20.71 ? 580  THR A C     1 
ATOM   4347  O  O     . THR A 1 560 ? -46.542 -21.870 36.414  1.00 20.37 ? 580  THR A O     1 
ATOM   4348  C  CB    . THR A 1 560 ? -44.088 -22.351 34.372  1.00 20.68 ? 580  THR A CB    1 
ATOM   4349  O  OG1   . THR A 1 560 ? -44.846 -23.544 34.637  1.00 23.16 ? 580  THR A OG1   1 
ATOM   4350  C  CG2   . THR A 1 560 ? -42.568 -22.666 34.366  1.00 18.78 ? 580  THR A CG2   1 
ATOM   4351  N  N     . SER A 1 561 ? -46.527 -20.424 34.681  1.00 21.51 ? 581  SER A N     1 
ATOM   4352  C  CA    . SER A 1 561 ? -47.955 -20.381 34.472  1.00 22.13 ? 581  SER A CA    1 
ATOM   4353  C  C     . SER A 1 561 ? -48.276 -21.089 33.162  1.00 23.26 ? 581  SER A C     1 
ATOM   4354  O  O     . SER A 1 561 ? -47.463 -21.068 32.241  1.00 23.46 ? 581  SER A O     1 
ATOM   4355  C  CB    . SER A 1 561 ? -48.413 -18.929 34.372  1.00 22.45 ? 581  SER A CB    1 
ATOM   4356  O  OG    . SER A 1 561 ? -49.800 -18.841 34.101  1.00 22.07 ? 581  SER A OG    1 
ATOM   4357  N  N     . PRO A 1 562 ? -49.476 -21.688 33.045  1.00 24.40 ? 582  PRO A N     1 
ATOM   4358  C  CA    . PRO A 1 562 ? -49.825 -22.290 31.749  1.00 25.31 ? 582  PRO A CA    1 
ATOM   4359  C  C     . PRO A 1 562 ? -49.985 -21.268 30.610  1.00 26.00 ? 582  PRO A C     1 
ATOM   4360  O  O     . PRO A 1 562 ? -49.917 -21.639 29.452  1.00 26.92 ? 582  PRO A O     1 
ATOM   4361  C  CB    . PRO A 1 562 ? -51.150 -23.013 32.035  1.00 25.34 ? 582  PRO A CB    1 
ATOM   4362  C  CG    . PRO A 1 562 ? -51.196 -23.170 33.501  1.00 25.43 ? 582  PRO A CG    1 
ATOM   4363  C  CD    . PRO A 1 562 ? -50.509 -21.948 34.054  1.00 24.13 ? 582  PRO A CD    1 
ATOM   4364  N  N     . GLN A 1 563 ? -50.163 -19.994 30.938  1.00 26.84 ? 583  GLN A N     1 
ATOM   4365  C  CA    . GLN A 1 563 ? -50.237 -18.936 29.925  1.00 27.14 ? 583  GLN A CA    1 
ATOM   4366  C  C     . GLN A 1 563 ? -48.897 -18.786 29.200  1.00 27.02 ? 583  GLN A C     1 
ATOM   4367  O  O     . GLN A 1 563 ? -47.829 -18.862 29.820  1.00 26.03 ? 583  GLN A O     1 
ATOM   4368  C  CB    . GLN A 1 563 ? -50.572 -17.592 30.565  1.00 27.75 ? 583  GLN A CB    1 
ATOM   4369  C  CG    . GLN A 1 563 ? -51.811 -17.559 31.454  1.00 30.24 ? 583  GLN A CG    1 
ATOM   4370  C  CD    . GLN A 1 563 ? -51.936 -16.237 32.187  1.00 33.21 ? 583  GLN A CD    1 
ATOM   4371  O  OE1   . GLN A 1 563 ? -51.471 -15.199 31.699  1.00 35.83 ? 583  GLN A OE1   1 
ATOM   4372  N  NE2   . GLN A 1 563 ? -52.539 -16.266 33.372  1.00 34.41 ? 583  GLN A NE2   1 
ATOM   4373  N  N     . GLU A 1 564 ? -48.972 -18.571 27.889  1.00 26.73 ? 584  GLU A N     1 
ATOM   4374  C  CA    . GLU A 1 564 ? -47.798 -18.406 27.044  1.00 26.77 ? 584  GLU A CA    1 
ATOM   4375  C  C     . GLU A 1 564 ? -47.639 -16.933 26.722  1.00 25.55 ? 584  GLU A C     1 
ATOM   4376  O  O     . GLU A 1 564 ? -48.636 -16.210 26.652  1.00 25.66 ? 584  GLU A O     1 
ATOM   4377  C  CB    . GLU A 1 564 ? -47.962 -19.169 25.731  1.00 27.20 ? 584  GLU A CB    1 
ATOM   4378  C  CG    . GLU A 1 564 ? -47.864 -20.685 25.846  1.00 29.98 ? 584  GLU A CG    1 
ATOM   4379  C  CD    . GLU A 1 564 ? -47.958 -21.371 24.493  1.00 32.89 ? 584  GLU A CD    1 
ATOM   4380  O  OE1   . GLU A 1 564 ? -48.359 -20.711 23.511  1.00 34.80 ? 584  GLU A OE1   1 
ATOM   4381  O  OE2   . GLU A 1 564 ? -47.615 -22.567 24.401  1.00 37.00 ? 584  GLU A OE2   1 
ATOM   4382  N  N     . ASN A 1 565 ? -46.395 -16.492 26.519  1.00 23.90 ? 585  ASN A N     1 
ATOM   4383  C  CA    . ASN A 1 565 ? -46.137 -15.151 25.990  1.00 22.54 ? 585  ASN A CA    1 
ATOM   4384  C  C     . ASN A 1 565 ? -46.416 -15.170 24.484  1.00 22.28 ? 585  ASN A C     1 
ATOM   4385  O  O     . ASN A 1 565 ? -46.739 -16.227 23.952  1.00 21.82 ? 585  ASN A O     1 
ATOM   4386  C  CB    . ASN A 1 565 ? -44.726 -14.668 26.364  1.00 22.37 ? 585  ASN A CB    1 
ATOM   4387  C  CG    . ASN A 1 565 ? -43.606 -15.349 25.581  1.00 21.36 ? 585  ASN A CG    1 
ATOM   4388  O  OD1   . ASN A 1 565 ? -43.833 -16.156 24.680  1.00 19.39 ? 585  ASN A OD1   1 
ATOM   4389  N  ND2   . ASN A 1 565 ? -42.368 -15.013 25.941  1.00 18.89 ? 585  ASN A ND2   1 
ATOM   4390  N  N     . PRO A 1 566 ? -46.317 -14.015 23.794  1.00 21.67 ? 586  PRO A N     1 
ATOM   4391  C  CA    . PRO A 1 566 ? -46.590 -13.986 22.351  1.00 21.48 ? 586  PRO A CA    1 
ATOM   4392  C  C     . PRO A 1 566 ? -45.688 -14.850 21.470  1.00 21.31 ? 586  PRO A C     1 
ATOM   4393  O  O     . PRO A 1 566 ? -46.002 -15.052 20.300  1.00 21.39 ? 586  PRO A O     1 
ATOM   4394  C  CB    . PRO A 1 566 ? -46.397 -12.505 21.991  1.00 21.81 ? 586  PRO A CB    1 
ATOM   4395  C  CG    . PRO A 1 566 ? -46.707 -11.787 23.250  1.00 22.14 ? 586  PRO A CG    1 
ATOM   4396  C  CD    . PRO A 1 566 ? -46.137 -12.657 24.329  1.00 21.74 ? 586  PRO A CD    1 
ATOM   4397  N  N     . TRP A 1 567 ? -44.590 -15.364 22.017  1.00 21.21 ? 587  TRP A N     1 
ATOM   4398  C  CA    . TRP A 1 567 ? -43.627 -16.135 21.241  1.00 20.68 ? 587  TRP A CA    1 
ATOM   4399  C  C     . TRP A 1 567 ? -43.737 -17.636 21.519  1.00 20.62 ? 587  TRP A C     1 
ATOM   4400  O  O     . TRP A 1 567 ? -42.870 -18.402 21.114  1.00 20.65 ? 587  TRP A O     1 
ATOM   4401  C  CB    . TRP A 1 567 ? -42.223 -15.622 21.539  1.00 20.61 ? 587  TRP A CB    1 
ATOM   4402  C  CG    . TRP A 1 567 ? -42.219 -14.140 21.647  1.00 20.78 ? 587  TRP A CG    1 
ATOM   4403  C  CD1   . TRP A 1 567 ? -41.888 -13.395 22.739  1.00 20.55 ? 587  TRP A CD1   1 
ATOM   4404  C  CD2   . TRP A 1 567 ? -42.633 -13.214 20.637  1.00 20.17 ? 587  TRP A CD2   1 
ATOM   4405  N  NE1   . TRP A 1 567 ? -42.044 -12.059 22.461  1.00 20.80 ? 587  TRP A NE1   1 
ATOM   4406  C  CE2   . TRP A 1 567 ? -42.501 -11.924 21.176  1.00 20.14 ? 587  TRP A CE2   1 
ATOM   4407  C  CE3   . TRP A 1 567 ? -43.080 -13.355 19.316  1.00 20.20 ? 587  TRP A CE3   1 
ATOM   4408  C  CZ2   . TRP A 1 567 ? -42.812 -10.776 20.447  1.00 21.52 ? 587  TRP A CZ2   1 
ATOM   4409  C  CZ3   . TRP A 1 567 ? -43.387 -12.216 18.590  1.00 20.25 ? 587  TRP A CZ3   1 
ATOM   4410  C  CH2   . TRP A 1 567 ? -43.255 -10.943 19.156  1.00 21.54 ? 587  TRP A CH2   1 
ATOM   4411  N  N     . GLY A 1 568 ? -44.800 -18.047 22.213  1.00 20.41 ? 588  GLY A N     1 
ATOM   4412  C  CA    . GLY A 1 568 ? -45.080 -19.468 22.450  1.00 20.48 ? 588  GLY A CA    1 
ATOM   4413  C  C     . GLY A 1 568 ? -44.411 -20.071 23.679  1.00 20.46 ? 588  GLY A C     1 
ATOM   4414  O  O     . GLY A 1 568 ? -44.418 -21.297 23.859  1.00 21.49 ? 588  GLY A O     1 
ATOM   4415  N  N     . HIS A 1 569 ? -43.839 -19.231 24.536  1.00 20.10 ? 589  HIS A N     1 
ATOM   4416  C  CA    . HIS A 1 569 ? -43.146 -19.720 25.728  1.00 19.51 ? 589  HIS A CA    1 
ATOM   4417  C  C     . HIS A 1 569 ? -43.940 -19.415 26.975  1.00 19.70 ? 589  HIS A C     1 
ATOM   4418  O  O     . HIS A 1 569 ? -44.528 -18.341 27.092  1.00 19.40 ? 589  HIS A O     1 
ATOM   4419  C  CB    . HIS A 1 569 ? -41.755 -19.111 25.819  1.00 19.25 ? 589  HIS A CB    1 
ATOM   4420  C  CG    . HIS A 1 569 ? -40.825 -19.625 24.772  1.00 18.30 ? 589  HIS A CG    1 
ATOM   4421  N  ND1   . HIS A 1 569 ? -40.182 -20.838 24.884  1.00 16.94 ? 589  HIS A ND1   1 
ATOM   4422  C  CD2   . HIS A 1 569 ? -40.464 -19.111 23.575  1.00 16.55 ? 589  HIS A CD2   1 
ATOM   4423  C  CE1   . HIS A 1 569 ? -39.455 -21.041 23.800  1.00 18.48 ? 589  HIS A CE1   1 
ATOM   4424  N  NE2   . HIS A 1 569 ? -39.607 -20.007 22.992  1.00 17.19 ? 589  HIS A NE2   1 
ATOM   4425  N  N     . LYS A 1 570 ? -43.954 -20.369 27.908  1.00 19.90 ? 590  LYS A N     1 
ATOM   4426  C  CA    . LYS A 1 570 ? -44.732 -20.219 29.135  1.00 19.76 ? 590  LYS A CA    1 
ATOM   4427  C  C     . LYS A 1 570 ? -44.184 -19.068 29.986  1.00 19.91 ? 590  LYS A C     1 
ATOM   4428  O  O     . LYS A 1 570 ? -42.964 -18.838 30.080  1.00 19.36 ? 590  LYS A O     1 
ATOM   4429  C  CB    . LYS A 1 570 ? -44.758 -21.526 29.943  1.00 19.90 ? 590  LYS A CB    1 
ATOM   4430  C  CG    . LYS A 1 570 ? -45.612 -22.635 29.313  1.00 20.15 ? 590  LYS A CG    1 
ATOM   4431  N  N     . ARG A 1 571 ? -45.107 -18.348 30.596  1.00 19.71 ? 591  ARG A N     1 
ATOM   4432  C  CA    . ARG A 1 571 ? -44.774 -17.182 31.387  1.00 20.14 ? 591  ARG A CA    1 
ATOM   4433  C  C     . ARG A 1 571 ? -44.261 -17.660 32.726  1.00 19.43 ? 591  ARG A C     1 
ATOM   4434  O  O     . ARG A 1 571 ? -44.957 -18.374 33.438  1.00 19.55 ? 591  ARG A O     1 
ATOM   4435  C  CB    . ARG A 1 571 ? -46.003 -16.304 31.555  1.00 20.34 ? 591  ARG A CB    1 
ATOM   4436  C  CG    . ARG A 1 571 ? -46.598 -15.870 30.220  1.00 21.65 ? 591  ARG A CG    1 
ATOM   4437  C  CD    . ARG A 1 571 ? -47.822 -15.020 30.446  1.00 22.57 ? 591  ARG A CD    1 
ATOM   4438  N  NE    . ARG A 1 571 ? -47.433 -13.714 30.938  1.00 24.06 ? 591  ARG A NE    1 
ATOM   4439  C  CZ    . ARG A 1 571 ? -48.246 -12.838 31.510  1.00 26.21 ? 591  ARG A CZ    1 
ATOM   4440  N  NH1   . ARG A 1 571 ? -49.536 -13.105 31.688  1.00 26.40 ? 591  ARG A NH1   1 
ATOM   4441  N  NH2   . ARG A 1 571 ? -47.750 -11.670 31.899  1.00 28.87 ? 591  ARG A NH2   1 
ATOM   4442  N  N     . SER A 1 572 ? -43.026 -17.299 33.055  1.00 18.67 ? 592  SER A N     1 
ATOM   4443  C  CA    A SER A 1 572 ? -42.376 -17.816 34.253  0.60 18.05 ? 592  SER A CA    1 
ATOM   4444  C  CA    B SER A 1 572 ? -42.434 -17.788 34.289  0.40 18.41 ? 592  SER A CA    1 
ATOM   4445  C  C     . SER A 1 572 ? -41.611 -16.736 35.010  1.00 18.15 ? 592  SER A C     1 
ATOM   4446  O  O     . SER A 1 572 ? -41.293 -15.675 34.455  1.00 17.69 ? 592  SER A O     1 
ATOM   4447  C  CB    A SER A 1 572 ? -41.410 -18.944 33.877  0.60 17.90 ? 592  SER A CB    1 
ATOM   4448  C  CB    B SER A 1 572 ? -41.582 -19.027 34.011  0.40 18.37 ? 592  SER A CB    1 
ATOM   4449  O  OG    A SER A 1 572 ? -42.024 -19.902 33.029  0.60 16.30 ? 592  SER A OG    1 
ATOM   4450  O  OG    B SER A 1 572 ? -40.326 -18.678 33.473  0.40 18.62 ? 592  SER A OG    1 
ATOM   4451  N  N     . TYR A 1 573 ? -41.329 -17.033 36.278  1.00 17.87 ? 593  TYR A N     1 
ATOM   4452  C  CA    . TYR A 1 573 ? -40.381 -16.295 37.075  1.00 17.83 ? 593  TYR A CA    1 
ATOM   4453  C  C     . TYR A 1 573 ? -39.331 -17.284 37.530  1.00 17.94 ? 593  TYR A C     1 
ATOM   4454  O  O     . TYR A 1 573 ? -39.646 -18.413 37.870  1.00 18.39 ? 593  TYR A O     1 
ATOM   4455  C  CB    . TYR A 1 573 ? -41.045 -15.597 38.265  1.00 17.49 ? 593  TYR A CB    1 
ATOM   4456  C  CG    . TYR A 1 573 ? -41.154 -14.110 38.059  1.00 17.19 ? 593  TYR A CG    1 
ATOM   4457  C  CD1   . TYR A 1 573 ? -42.166 -13.574 37.274  1.00 16.01 ? 593  TYR A CD1   1 
ATOM   4458  C  CD2   . TYR A 1 573 ? -40.229 -13.239 38.626  1.00 16.97 ? 593  TYR A CD2   1 
ATOM   4459  C  CE1   . TYR A 1 573 ? -42.264 -12.209 37.064  1.00 16.86 ? 593  TYR A CE1   1 
ATOM   4460  C  CE2   . TYR A 1 573 ? -40.323 -11.864 38.434  1.00 16.85 ? 593  TYR A CE2   1 
ATOM   4461  C  CZ    . TYR A 1 573 ? -41.354 -11.354 37.651  1.00 17.36 ? 593  TYR A CZ    1 
ATOM   4462  O  OH    . TYR A 1 573 ? -41.464 -9.993  37.437  1.00 16.52 ? 593  TYR A OH    1 
ATOM   4463  N  N     . ARG A 1 574 ? -38.079 -16.840 37.516  1.00 18.59 ? 594  ARG A N     1 
ATOM   4464  C  CA    . ARG A 1 574 ? -36.928 -17.679 37.804  1.00 18.79 ? 594  ARG A CA    1 
ATOM   4465  C  C     . ARG A 1 574 ? -36.396 -17.327 39.179  1.00 18.88 ? 594  ARG A C     1 
ATOM   4466  O  O     . ARG A 1 574 ? -36.228 -16.141 39.484  1.00 18.70 ? 594  ARG A O     1 
ATOM   4467  C  CB    . ARG A 1 574 ? -35.846 -17.403 36.758  1.00 19.04 ? 594  ARG A CB    1 
ATOM   4468  C  CG    . ARG A 1 574 ? -34.526 -18.098 36.994  1.00 19.87 ? 594  ARG A CG    1 
ATOM   4469  C  CD    . ARG A 1 574 ? -33.454 -17.561 36.055  1.00 20.34 ? 594  ARG A CD    1 
ATOM   4470  N  NE    . ARG A 1 574 ? -32.168 -18.200 36.311  1.00 20.46 ? 594  ARG A NE    1 
ATOM   4471  C  CZ    . ARG A 1 574 ? -31.007 -17.827 35.774  1.00 21.78 ? 594  ARG A CZ    1 
ATOM   4472  N  NH1   . ARG A 1 574 ? -30.928 -16.789 34.941  1.00 19.69 ? 594  ARG A NH1   1 
ATOM   4473  N  NH2   . ARG A 1 574 ? -29.903 -18.502 36.081  1.00 23.21 ? 594  ARG A NH2   1 
ATOM   4474  N  N     . LEU A 1 575 ? -36.117 -18.347 39.996  1.00 18.78 ? 595  LEU A N     1 
ATOM   4475  C  CA    . LEU A 1 575 ? -35.486 -18.143 41.296  1.00 19.33 ? 595  LEU A CA    1 
ATOM   4476  C  C     . LEU A 1 575 ? -33.971 -18.361 41.172  1.00 19.95 ? 595  LEU A C     1 
ATOM   4477  O  O     . LEU A 1 575 ? -33.519 -19.404 40.698  1.00 19.92 ? 595  LEU A O     1 
ATOM   4478  C  CB    . LEU A 1 575 ? -36.067 -19.088 42.350  1.00 19.15 ? 595  LEU A CB    1 
ATOM   4479  C  CG    . LEU A 1 575 ? -35.344 -19.116 43.710  1.00 20.16 ? 595  LEU A CG    1 
ATOM   4480  C  CD1   . LEU A 1 575 ? -35.659 -17.881 44.528  1.00 20.90 ? 595  LEU A CD1   1 
ATOM   4481  C  CD2   . LEU A 1 575 ? -35.714 -20.364 44.503  1.00 21.64 ? 595  LEU A CD2   1 
ATOM   4482  N  N     . GLN A 1 576 ? -33.200 -17.376 41.615  1.00 20.63 ? 596  GLN A N     1 
ATOM   4483  C  CA    . GLN A 1 576 ? -31.749 -17.426 41.541  1.00 21.83 ? 596  GLN A CA    1 
ATOM   4484  C  C     . GLN A 1 576 ? -31.178 -17.202 42.939  1.00 21.96 ? 596  GLN A C     1 
ATOM   4485  O  O     . GLN A 1 576 ? -31.368 -16.138 43.528  1.00 22.10 ? 596  GLN A O     1 
ATOM   4486  C  CB    . GLN A 1 576 ? -31.273 -16.355 40.558  1.00 22.30 ? 596  GLN A CB    1 
ATOM   4487  C  CG    . GLN A 1 576 ? -29.767 -16.259 40.373  1.00 24.67 ? 596  GLN A CG    1 
ATOM   4488  C  CD    . GLN A 1 576 ? -29.389 -15.339 39.217  1.00 27.13 ? 596  GLN A CD    1 
ATOM   4489  O  OE1   . GLN A 1 576 ? -30.073 -15.298 38.183  1.00 28.34 ? 596  GLN A OE1   1 
ATOM   4490  N  NE2   . GLN A 1 576 ? -28.299 -14.585 39.391  1.00 28.30 ? 596  GLN A NE2   1 
ATOM   4491  N  N     . ILE A 1 577 ? -30.488 -18.208 43.470  1.00 21.89 ? 597  ILE A N     1 
ATOM   4492  C  CA    . ILE A 1 577 ? -30.056 -18.200 44.856  1.00 22.14 ? 597  ILE A CA    1 
ATOM   4493  C  C     . ILE A 1 577 ? -28.596 -17.756 44.980  1.00 22.49 ? 597  ILE A C     1 
ATOM   4494  O  O     . ILE A 1 577 ? -27.740 -18.252 44.252  1.00 22.30 ? 597  ILE A O     1 
ATOM   4495  C  CB    . ILE A 1 577 ? -30.227 -19.595 45.487  1.00 22.10 ? 597  ILE A CB    1 
ATOM   4496  C  CG1   . ILE A 1 577 ? -31.724 -19.919 45.638  1.00 22.36 ? 597  ILE A CG1   1 
ATOM   4497  C  CG2   . ILE A 1 577 ? -29.500 -19.671 46.825  1.00 21.96 ? 597  ILE A CG2   1 
ATOM   4498  C  CD1   . ILE A 1 577 ? -32.043 -21.395 45.790  1.00 20.46 ? 597  ILE A CD1   1 
ATOM   4499  N  N     A HIS A 1 578 ? -28.338 -16.836 45.912  0.50 22.60 ? 598  HIS A N     1 
ATOM   4500  N  N     B HIS A 1 578 ? -28.338 -16.794 45.874  0.50 22.65 ? 598  HIS A N     1 
ATOM   4501  C  CA    A HIS A 1 578 ? -26.995 -16.355 46.208  0.50 22.81 ? 598  HIS A CA    1 
ATOM   4502  C  CA    B HIS A 1 578 ? -26.979 -16.361 46.205  0.50 22.90 ? 598  HIS A CA    1 
ATOM   4503  C  C     A HIS A 1 578 ? -26.620 -16.779 47.622  0.50 22.88 ? 598  HIS A C     1 
ATOM   4504  C  C     B HIS A 1 578 ? -26.642 -16.800 47.619  0.50 22.93 ? 598  HIS A C     1 
ATOM   4505  O  O     A HIS A 1 578 ? -27.040 -16.152 48.602  0.50 22.58 ? 598  HIS A O     1 
ATOM   4506  O  O     B HIS A 1 578 ? -27.104 -16.200 48.597  0.50 22.65 ? 598  HIS A O     1 
ATOM   4507  C  CB    A HIS A 1 578 ? -26.936 -14.834 46.059  0.50 22.92 ? 598  HIS A CB    1 
ATOM   4508  C  CB    B HIS A 1 578 ? -26.814 -14.843 46.091  0.50 23.05 ? 598  HIS A CB    1 
ATOM   4509  C  CG    A HIS A 1 578 ? -27.136 -14.364 44.651  0.50 23.75 ? 598  HIS A CG    1 
ATOM   4510  C  CG    B HIS A 1 578 ? -25.450 -14.361 46.482  0.50 23.98 ? 598  HIS A CG    1 
ATOM   4511  N  ND1   A HIS A 1 578 ? -26.252 -13.521 44.012  0.50 24.63 ? 598  HIS A ND1   1 
ATOM   4512  N  ND1   B HIS A 1 578 ? -25.230 -13.530 47.561  0.50 25.91 ? 598  HIS A ND1   1 
ATOM   4513  C  CD2   A HIS A 1 578 ? -28.112 -14.634 43.752  0.50 23.61 ? 598  HIS A CD2   1 
ATOM   4514  C  CD2   B HIS A 1 578 ? -24.230 -14.617 45.953  0.50 24.67 ? 598  HIS A CD2   1 
ATOM   4515  C  CE1   A HIS A 1 578 ? -26.678 -13.288 42.784  0.50 24.62 ? 598  HIS A CE1   1 
ATOM   4516  C  CE1   B HIS A 1 578 ? -23.936 -13.289 47.674  0.50 24.94 ? 598  HIS A CE1   1 
ATOM   4517  N  NE2   A HIS A 1 578 ? -27.803 -13.955 42.600  0.50 24.18 ? 598  HIS A NE2   1 
ATOM   4518  N  NE2   B HIS A 1 578 ? -23.307 -13.937 46.711  0.50 24.99 ? 598  HIS A NE2   1 
ATOM   4519  N  N     . SER A 1 579 ? -25.830 -17.845 47.723  1.00 22.89 ? 599  SER A N     1 
ATOM   4520  C  CA    . SER A 1 579 ? -25.566 -18.489 49.008  1.00 23.36 ? 599  SER A CA    1 
ATOM   4521  C  C     . SER A 1 579 ? -24.264 -19.283 49.041  1.00 24.24 ? 599  SER A C     1 
ATOM   4522  O  O     . SER A 1 579 ? -23.774 -19.736 48.009  1.00 23.31 ? 599  SER A O     1 
ATOM   4523  C  CB    . SER A 1 579 ? -26.728 -19.439 49.333  1.00 23.06 ? 599  SER A CB    1 
ATOM   4524  O  OG    . SER A 1 579 ? -26.569 -20.081 50.587  1.00 21.78 ? 599  SER A OG    1 
ATOM   4525  N  N     . MET A 1 580 ? -23.735 -19.435 50.250  1.00 25.13 ? 600  MET A N     1 
ATOM   4526  C  CA    A MET A 1 580 ? -22.585 -20.301 50.511  0.70 26.22 ? 600  MET A CA    1 
ATOM   4527  C  CA    B MET A 1 580 ? -22.586 -20.291 50.508  0.30 25.68 ? 600  MET A CA    1 
ATOM   4528  C  C     . MET A 1 580 ? -22.943 -21.366 51.539  1.00 26.01 ? 600  MET A C     1 
ATOM   4529  O  O     . MET A 1 580 ? -22.063 -22.027 52.080  1.00 26.75 ? 600  MET A O     1 
ATOM   4530  C  CB    A MET A 1 580 ? -21.390 -19.481 51.013  0.70 26.84 ? 600  MET A CB    1 
ATOM   4531  C  CB    B MET A 1 580 ? -21.407 -19.444 50.994  0.30 25.82 ? 600  MET A CB    1 
ATOM   4532  C  CG    A MET A 1 580 ? -20.653 -18.710 49.925  0.70 29.03 ? 600  MET A CG    1 
ATOM   4533  C  CG    B MET A 1 580 ? -21.002 -18.337 50.018  0.30 26.11 ? 600  MET A CG    1 
ATOM   4534  S  SD    A MET A 1 580 ? -19.108 -17.968 50.538  0.70 34.79 ? 600  MET A SD    1 
ATOM   4535  S  SD    B MET A 1 580 ? -22.009 -16.838 50.118  0.30 27.08 ? 600  MET A SD    1 
ATOM   4536  C  CE    A MET A 1 580 ? -18.136 -19.436 50.867  0.70 33.59 ? 600  MET A CE    1 
ATOM   4537  C  CE    B MET A 1 580 ? -21.227 -15.962 51.473  0.30 26.95 ? 600  MET A CE    1 
ATOM   4538  N  N     . ALA A 1 581 ? -24.241 -21.548 51.793  1.00 25.86 ? 601  ALA A N     1 
ATOM   4539  C  CA    . ALA A 1 581 ? -24.725 -22.513 52.782  1.00 25.82 ? 601  ALA A CA    1 
ATOM   4540  C  C     . ALA A 1 581 ? -24.511 -23.967 52.367  1.00 26.02 ? 601  ALA A C     1 
ATOM   4541  O  O     . ALA A 1 581 ? -24.279 -24.277 51.206  1.00 26.16 ? 601  ALA A O     1 
ATOM   4542  C  CB    . ALA A 1 581 ? -26.222 -22.270 53.089  1.00 25.43 ? 601  ALA A CB    1 
ATOM   4543  N  N     . ASP A 1 582 ? -24.624 -24.855 53.343  1.00 26.66 ? 602  ASP A N     1 
ATOM   4544  C  CA    . ASP A 1 582 ? -24.407 -26.279 53.152  1.00 27.21 ? 602  ASP A CA    1 
ATOM   4545  C  C     . ASP A 1 582 ? -25.117 -26.975 54.304  1.00 26.78 ? 602  ASP A C     1 
ATOM   4546  O  O     . ASP A 1 582 ? -25.695 -26.307 55.168  1.00 26.70 ? 602  ASP A O     1 
ATOM   4547  C  CB    . ASP A 1 582 ? -22.903 -26.573 53.182  1.00 27.69 ? 602  ASP A CB    1 
ATOM   4548  C  CG    . ASP A 1 582 ? -22.545 -27.903 52.541  1.00 30.39 ? 602  ASP A CG    1 
ATOM   4549  O  OD1   . ASP A 1 582 ? -23.456 -28.729 52.289  1.00 32.19 ? 602  ASP A OD1   1 
ATOM   4550  O  OD2   . ASP A 1 582 ? -21.334 -28.125 52.292  1.00 33.92 ? 602  ASP A OD2   1 
ATOM   4551  N  N     . GLN A 1 583 ? -25.068 -28.302 54.328  1.00 26.40 ? 603  GLN A N     1 
ATOM   4552  C  CA    . GLN A 1 583 ? -25.602 -29.065 55.443  1.00 26.35 ? 603  GLN A CA    1 
ATOM   4553  C  C     . GLN A 1 583 ? -24.703 -28.855 56.670  1.00 26.43 ? 603  GLN A C     1 
ATOM   4554  O  O     . GLN A 1 583 ? -23.491 -29.082 56.601  1.00 26.19 ? 603  GLN A O     1 
ATOM   4555  C  CB    . GLN A 1 583 ? -25.683 -30.553 55.081  1.00 26.35 ? 603  GLN A CB    1 
ATOM   4556  C  CG    . GLN A 1 583 ? -26.454 -31.388 56.081  1.00 26.32 ? 603  GLN A CG    1 
ATOM   4557  C  CD    . GLN A 1 583 ? -27.879 -30.901 56.248  1.00 27.52 ? 603  GLN A CD    1 
ATOM   4558  O  OE1   . GLN A 1 583 ? -28.612 -30.774 55.271  1.00 28.24 ? 603  GLN A OE1   1 
ATOM   4559  N  NE2   . GLN A 1 583 ? -28.274 -30.609 57.484  1.00 25.99 ? 603  GLN A NE2   1 
ATOM   4560  N  N     . VAL A 1 584 ? -25.288 -28.427 57.787  1.00 26.33 ? 604  VAL A N     1 
ATOM   4561  C  CA    . VAL A 1 584 ? -24.500 -28.171 58.996  1.00 26.49 ? 604  VAL A CA    1 
ATOM   4562  C  C     . VAL A 1 584 ? -24.660 -29.319 59.994  1.00 26.20 ? 604  VAL A C     1 
ATOM   4563  O  O     . VAL A 1 584 ? -23.697 -30.036 60.291  1.00 26.31 ? 604  VAL A O     1 
ATOM   4564  C  CB    . VAL A 1 584 ? -24.877 -26.822 59.638  1.00 26.60 ? 604  VAL A CB    1 
ATOM   4565  C  CG1   . VAL A 1 584 ? -24.031 -26.567 60.896  1.00 27.18 ? 604  VAL A CG1   1 
ATOM   4566  C  CG2   . VAL A 1 584 ? -24.697 -25.693 58.621  1.00 26.18 ? 604  VAL A CG2   1 
ATOM   4567  N  N     . LEU A 1 585 ? -25.871 -29.512 60.498  1.00 25.57 ? 605  LEU A N     1 
ATOM   4568  C  CA    . LEU A 1 585 ? -26.125 -30.596 61.443  1.00 25.31 ? 605  LEU A CA    1 
ATOM   4569  C  C     . LEU A 1 585 ? -26.516 -31.854 60.664  1.00 25.25 ? 605  LEU A C     1 
ATOM   4570  O  O     . LEU A 1 585 ? -27.029 -31.752 59.546  1.00 25.57 ? 605  LEU A O     1 
ATOM   4571  C  CB    . LEU A 1 585 ? -27.236 -30.208 62.429  1.00 25.35 ? 605  LEU A CB    1 
ATOM   4572  C  CG    . LEU A 1 585 ? -26.996 -28.970 63.296  1.00 24.92 ? 605  LEU A CG    1 
ATOM   4573  C  CD1   . LEU A 1 585 ? -28.199 -28.774 64.219  1.00 25.56 ? 605  LEU A CD1   1 
ATOM   4574  C  CD2   . LEU A 1 585 ? -25.688 -29.087 64.101  1.00 23.92 ? 605  LEU A CD2   1 
ATOM   4575  N  N     . PRO A 1 586 ? -26.273 -33.047 61.241  1.00 25.12 ? 606  PRO A N     1 
ATOM   4576  C  CA    . PRO A 1 586 ? -26.678 -34.273 60.551  1.00 25.00 ? 606  PRO A CA    1 
ATOM   4577  C  C     . PRO A 1 586 ? -28.190 -34.450 60.590  1.00 25.06 ? 606  PRO A C     1 
ATOM   4578  O  O     . PRO A 1 586 ? -28.795 -34.267 61.653  1.00 24.90 ? 606  PRO A O     1 
ATOM   4579  C  CB    . PRO A 1 586 ? -25.977 -35.388 61.337  1.00 24.96 ? 606  PRO A CB    1 
ATOM   4580  C  CG    . PRO A 1 586 ? -25.601 -34.795 62.643  1.00 25.27 ? 606  PRO A CG    1 
ATOM   4581  C  CD    . PRO A 1 586 ? -25.655 -33.307 62.552  1.00 25.05 ? 606  PRO A CD    1 
ATOM   4582  N  N     . PRO A 1 587 ? -28.805 -34.761 59.434  1.00 25.19 ? 607  PRO A N     1 
ATOM   4583  C  CA    . PRO A 1 587 ? -30.249 -34.957 59.384  1.00 25.33 ? 607  PRO A CA    1 
ATOM   4584  C  C     . PRO A 1 587 ? -30.731 -36.027 60.366  1.00 25.67 ? 607  PRO A C     1 
ATOM   4585  O  O     . PRO A 1 587 ? -30.195 -37.133 60.391  1.00 25.97 ? 607  PRO A O     1 
ATOM   4586  C  CB    . PRO A 1 587 ? -30.491 -35.393 57.938  1.00 25.64 ? 607  PRO A CB    1 
ATOM   4587  C  CG    . PRO A 1 587 ? -29.375 -34.774 57.172  1.00 25.28 ? 607  PRO A CG    1 
ATOM   4588  C  CD    . PRO A 1 587 ? -28.201 -34.786 58.089  1.00 24.97 ? 607  PRO A CD    1 
ATOM   4589  N  N     . GLY A 1 588 ? -31.712 -35.676 61.186  1.00 25.74 ? 608  GLY A N     1 
ATOM   4590  C  CA    . GLY A 1 588 ? -32.319 -36.616 62.112  1.00 26.04 ? 608  GLY A CA    1 
ATOM   4591  C  C     . GLY A 1 588 ? -31.708 -36.608 63.504  1.00 26.01 ? 608  GLY A C     1 
ATOM   4592  O  O     . GLY A 1 588 ? -32.212 -37.284 64.392  1.00 26.32 ? 608  GLY A O     1 
ATOM   4593  N  N     . TRP A 1 589 ? -30.626 -35.860 63.711  1.00 25.69 ? 609  TRP A N     1 
ATOM   4594  C  CA    . TRP A 1 589 ? -29.967 -35.863 65.010  1.00 25.25 ? 609  TRP A CA    1 
ATOM   4595  C  C     . TRP A 1 589 ? -30.485 -34.757 65.944  1.00 25.08 ? 609  TRP A C     1 
ATOM   4596  O  O     . TRP A 1 589 ? -30.209 -33.576 65.740  1.00 24.71 ? 609  TRP A O     1 
ATOM   4597  C  CB    . TRP A 1 589 ? -28.452 -35.742 64.862  1.00 25.23 ? 609  TRP A CB    1 
ATOM   4598  C  CG    . TRP A 1 589 ? -27.790 -35.660 66.220  1.00 25.69 ? 609  TRP A CG    1 
ATOM   4599  C  CD1   . TRP A 1 589 ? -27.281 -34.545 66.823  1.00 25.09 ? 609  TRP A CD1   1 
ATOM   4600  C  CD2   . TRP A 1 589 ? -27.634 -36.734 67.157  1.00 25.46 ? 609  TRP A CD2   1 
ATOM   4601  N  NE1   . TRP A 1 589 ? -26.791 -34.862 68.072  1.00 26.88 ? 609  TRP A NE1   1 
ATOM   4602  C  CE2   . TRP A 1 589 ? -26.996 -36.201 68.302  1.00 26.55 ? 609  TRP A CE2   1 
ATOM   4603  C  CE3   . TRP A 1 589 ? -27.953 -38.101 67.130  1.00 26.02 ? 609  TRP A CE3   1 
ATOM   4604  C  CZ2   . TRP A 1 589 ? -26.670 -36.984 69.416  1.00 26.91 ? 609  TRP A CZ2   1 
ATOM   4605  C  CZ3   . TRP A 1 589 ? -27.632 -38.890 68.248  1.00 27.44 ? 609  TRP A CZ3   1 
ATOM   4606  C  CH2   . TRP A 1 589 ? -27.000 -38.322 69.376  1.00 27.40 ? 609  TRP A CH2   1 
ATOM   4607  N  N     . GLN A 1 590 ? -31.244 -35.158 66.958  1.00 25.06 ? 610  GLN A N     1 
ATOM   4608  C  CA    . GLN A 1 590 ? -31.613 -34.299 68.076  1.00 25.32 ? 610  GLN A CA    1 
ATOM   4609  C  C     . GLN A 1 590 ? -32.137 -32.910 67.666  1.00 25.16 ? 610  GLN A C     1 
ATOM   4610  O  O     . GLN A 1 590 ? -33.223 -32.811 67.096  1.00 25.03 ? 610  GLN A O     1 
ATOM   4611  C  CB    . GLN A 1 590 ? -30.425 -34.209 69.041  1.00 25.59 ? 610  GLN A CB    1 
ATOM   4612  C  CG    . GLN A 1 590 ? -30.060 -35.543 69.691  1.00 27.35 ? 610  GLN A CG    1 
ATOM   4613  C  CD    . GLN A 1 590 ? -31.160 -36.082 70.608  1.00 29.26 ? 610  GLN A CD    1 
ATOM   4614  O  OE1   . GLN A 1 590 ? -31.919 -35.319 71.204  1.00 32.90 ? 610  GLN A OE1   1 
ATOM   4615  N  NE2   . GLN A 1 590 ? -31.249 -37.397 70.715  1.00 30.47 ? 610  GLN A NE2   1 
ATOM   4616  N  N     . GLU A 1 591 ? -31.362 -31.853 67.926  1.00 25.31 ? 611  GLU A N     1 
ATOM   4617  C  CA    . GLU A 1 591 ? -31.822 -30.467 67.732  1.00 25.32 ? 611  GLU A CA    1 
ATOM   4618  C  C     . GLU A 1 591 ? -32.042 -30.122 66.256  1.00 24.67 ? 611  GLU A C     1 
ATOM   4619  O  O     . GLU A 1 591 ? -32.713 -29.140 65.941  1.00 24.67 ? 611  GLU A O     1 
ATOM   4620  C  CB    . GLU A 1 591 ? -30.820 -29.460 68.314  1.00 25.77 ? 611  GLU A CB    1 
ATOM   4621  C  CG    . GLU A 1 591 ? -30.501 -29.603 69.801  1.00 27.71 ? 611  GLU A CG    1 
ATOM   4622  C  CD    . GLU A 1 591 ? -29.375 -30.587 70.101  1.00 30.02 ? 611  GLU A CD    1 
ATOM   4623  O  OE1   . GLU A 1 591 ? -28.715 -31.094 69.162  1.00 31.50 ? 611  GLU A OE1   1 
ATOM   4624  O  OE2   . GLU A 1 591 ? -29.151 -30.864 71.297  1.00 34.25 ? 611  GLU A OE2   1 
ATOM   4625  N  N     . GLU A 1 592 ? -31.449 -30.910 65.360  1.00 23.73 ? 612  GLU A N     1 
ATOM   4626  C  CA    . GLU A 1 592 ? -31.604 -30.710 63.924  1.00 23.16 ? 612  GLU A CA    1 
ATOM   4627  C  C     . GLU A 1 592 ? -33.067 -30.798 63.510  1.00 22.54 ? 612  GLU A C     1 
ATOM   4628  O  O     . GLU A 1 592 ? -33.445 -30.270 62.466  1.00 22.11 ? 612  GLU A O     1 
ATOM   4629  C  CB    . GLU A 1 592 ? -30.767 -31.729 63.133  1.00 22.90 ? 612  GLU A CB    1 
ATOM   4630  C  CG    . GLU A 1 592 ? -30.693 -31.447 61.620  1.00 22.91 ? 612  GLU A CG    1 
ATOM   4631  C  CD    . GLU A 1 592 ? -31.880 -31.999 60.793  1.00 22.39 ? 612  GLU A CD    1 
ATOM   4632  O  OE1   . GLU A 1 592 ? -32.650 -32.871 61.274  1.00 20.07 ? 612  GLU A OE1   1 
ATOM   4633  O  OE2   . GLU A 1 592 ? -32.032 -31.557 59.630  1.00 21.79 ? 612  GLU A OE2   1 
ATOM   4634  N  N     . GLN A 1 593 ? -33.889 -31.449 64.332  1.00 22.24 ? 613  GLN A N     1 
ATOM   4635  C  CA    . GLN A 1 593 ? -35.342 -31.471 64.125  1.00 22.17 ? 613  GLN A CA    1 
ATOM   4636  C  C     . GLN A 1 593 ? -35.968 -30.052 64.080  1.00 21.95 ? 613  GLN A C     1 
ATOM   4637  O  O     . GLN A 1 593 ? -37.032 -29.848 63.477  1.00 21.38 ? 613  GLN A O     1 
ATOM   4638  C  CB    . GLN A 1 593 ? -36.010 -32.312 65.223  1.00 22.34 ? 613  GLN A CB    1 
ATOM   4639  C  CG    . GLN A 1 593 ? -37.496 -32.645 64.985  1.00 23.31 ? 613  GLN A CG    1 
ATOM   4640  C  CD    . GLN A 1 593 ? -37.718 -33.719 63.915  1.00 24.61 ? 613  GLN A CD    1 
ATOM   4641  O  OE1   . GLN A 1 593 ? -36.811 -34.059 63.142  1.00 25.02 ? 613  GLN A OE1   1 
ATOM   4642  N  NE2   . GLN A 1 593 ? -38.933 -34.255 63.870  1.00 24.13 ? 613  GLN A NE2   1 
ATOM   4643  N  N     . ALA A 1 594 ? -35.313 -29.084 64.727  1.00 21.37 ? 614  ALA A N     1 
ATOM   4644  C  CA    . ALA A 1 594 ? -35.788 -27.700 64.745  1.00 21.13 ? 614  ALA A CA    1 
ATOM   4645  C  C     . ALA A 1 594 ? -35.569 -27.006 63.403  1.00 20.96 ? 614  ALA A C     1 
ATOM   4646  O  O     . ALA A 1 594 ? -36.304 -26.071 63.068  1.00 20.65 ? 614  ALA A O     1 
ATOM   4647  C  CB    . ALA A 1 594 ? -35.080 -26.907 65.866  1.00 21.34 ? 614  ALA A CB    1 
ATOM   4648  N  N     . ILE A 1 595 ? -34.565 -27.471 62.642  1.00 20.40 ? 615  ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 595 ? -34.126 -26.802 61.415  1.00 19.73 ? 615  ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 595 ? -34.018 -27.755 60.210  1.00 19.98 ? 615  ILE A C     1 
ATOM   4651  O  O     . ILE A 1 595 ? -33.046 -27.720 59.441  1.00 20.31 ? 615  ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 595 ? -32.800 -26.026 61.662  1.00 19.95 ? 615  ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 595 ? -31.647 -26.952 62.063  1.00 19.49 ? 615  ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 595 ? -33.007 -24.952 62.770  1.00 18.57 ? 615  ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 595 ? -30.259 -26.302 61.906  1.00 18.83 ? 615  ILE A CD1   1 
ATOM   4656  N  N     . THR A 1 596 ? -35.041 -28.583 60.018  1.00 19.18 ? 616  THR A N     1 
ATOM   4657  C  CA    . THR A 1 596 ? -35.047 -29.527 58.896  1.00 18.73 ? 616  THR A CA    1 
ATOM   4658  C  C     . THR A 1 596 ? -35.147 -28.814 57.545  1.00 18.80 ? 616  THR A C     1 
ATOM   4659  O  O     . THR A 1 596 ? -34.750 -29.364 56.521  1.00 18.94 ? 616  THR A O     1 
ATOM   4660  C  CB    . THR A 1 596 ? -36.156 -30.596 59.036  1.00 18.37 ? 616  THR A CB    1 
ATOM   4661  O  OG1   . THR A 1 596 ? -37.441 -29.972 59.030  1.00 16.51 ? 616  THR A OG1   1 
ATOM   4662  C  CG2   . THR A 1 596 ? -35.978 -31.397 60.354  1.00 18.21 ? 616  THR A CG2   1 
ATOM   4663  N  N     . TRP A 1 597 ? -35.648 -27.579 57.546  1.00 18.89 ? 617  TRP A N     1 
ATOM   4664  C  CA    . TRP A 1 597 ? -35.638 -26.740 56.342  1.00 18.23 ? 617  TRP A CA    1 
ATOM   4665  C  C     . TRP A 1 597 ? -34.227 -26.485 55.819  1.00 18.60 ? 617  TRP A C     1 
ATOM   4666  O  O     . TRP A 1 597 ? -34.043 -26.316 54.619  1.00 18.82 ? 617  TRP A O     1 
ATOM   4667  C  CB    . TRP A 1 597 ? -36.363 -25.410 56.565  1.00 18.10 ? 617  TRP A CB    1 
ATOM   4668  C  CG    . TRP A 1 597 ? -35.957 -24.636 57.806  1.00 17.03 ? 617  TRP A CG    1 
ATOM   4669  C  CD1   . TRP A 1 597 ? -36.615 -24.615 59.004  1.00 16.82 ? 617  TRP A CD1   1 
ATOM   4670  C  CD2   . TRP A 1 597 ? -34.825 -23.767 57.959  1.00 16.40 ? 617  TRP A CD2   1 
ATOM   4671  N  NE1   . TRP A 1 597 ? -35.959 -23.798 59.891  1.00 16.88 ? 617  TRP A NE1   1 
ATOM   4672  C  CE2   . TRP A 1 597 ? -34.860 -23.262 59.273  1.00 15.66 ? 617  TRP A CE2   1 
ATOM   4673  C  CE3   . TRP A 1 597 ? -33.787 -23.358 57.107  1.00 17.94 ? 617  TRP A CE3   1 
ATOM   4674  C  CZ2   . TRP A 1 597 ? -33.897 -22.378 59.759  1.00 15.87 ? 617  TRP A CZ2   1 
ATOM   4675  C  CZ3   . TRP A 1 597 ? -32.825 -22.469 57.594  1.00 15.39 ? 617  TRP A CZ3   1 
ATOM   4676  C  CH2   . TRP A 1 597 ? -32.885 -22.002 58.910  1.00 16.02 ? 617  TRP A CH2   1 
ATOM   4677  N  N     . ALA A 1 598 ? -33.242 -26.476 56.715  1.00 18.56 ? 618  ALA A N     1 
ATOM   4678  C  CA    . ALA A 1 598 ? -31.860 -26.195 56.359  1.00 18.73 ? 618  ALA A CA    1 
ATOM   4679  C  C     . ALA A 1 598 ? -31.199 -27.376 55.647  1.00 18.73 ? 618  ALA A C     1 
ATOM   4680  O  O     . ALA A 1 598 ? -30.014 -27.331 55.335  1.00 18.77 ? 618  ALA A O     1 
ATOM   4681  C  CB    . ALA A 1 598 ? -31.061 -25.797 57.601  1.00 18.62 ? 618  ALA A CB    1 
ATOM   4682  N  N     . ARG A 1 599 ? -31.966 -28.439 55.409  1.00 18.72 ? 619  ARG A N     1 
ATOM   4683  C  CA    . ARG A 1 599 ? -31.549 -29.507 54.504  1.00 18.38 ? 619  ARG A CA    1 
ATOM   4684  C  C     . ARG A 1 599 ? -31.632 -29.089 53.042  1.00 18.30 ? 619  ARG A C     1 
ATOM   4685  O  O     . ARG A 1 599 ? -30.996 -29.697 52.180  1.00 18.14 ? 619  ARG A O     1 
ATOM   4686  C  CB    . ARG A 1 599 ? -32.437 -30.732 54.694  1.00 18.45 ? 619  ARG A CB    1 
ATOM   4687  C  CG    . ARG A 1 599 ? -32.345 -31.346 56.067  1.00 18.67 ? 619  ARG A CG    1 
ATOM   4688  C  CD    . ARG A 1 599 ? -33.304 -32.486 56.221  1.00 18.19 ? 619  ARG A CD    1 
ATOM   4689  N  NE    . ARG A 1 599 ? -33.350 -32.982 57.593  1.00 19.06 ? 619  ARG A NE    1 
ATOM   4690  C  CZ    . ARG A 1 599 ? -34.142 -33.975 57.997  1.00 19.94 ? 619  ARG A CZ    1 
ATOM   4691  N  NH1   . ARG A 1 599 ? -34.946 -34.587 57.136  1.00 20.23 ? 619  ARG A NH1   1 
ATOM   4692  N  NH2   . ARG A 1 599 ? -34.123 -34.365 59.259  1.00 19.90 ? 619  ARG A NH2   1 
ATOM   4693  N  N     . TYR A 1 600 ? -32.435 -28.064 52.766  1.00 18.37 ? 620  TYR A N     1 
ATOM   4694  C  CA    . TYR A 1 600 ? -32.849 -27.740 51.405  1.00 18.22 ? 620  TYR A CA    1 
ATOM   4695  C  C     . TYR A 1 600 ? -32.531 -26.305 51.006  1.00 17.97 ? 620  TYR A C     1 
ATOM   4696  O  O     . TYR A 1 600 ? -33.127 -25.373 51.550  1.00 18.27 ? 620  TYR A O     1 
ATOM   4697  C  CB    . TYR A 1 600 ? -34.360 -27.969 51.278  1.00 18.54 ? 620  TYR A CB    1 
ATOM   4698  C  CG    . TYR A 1 600 ? -34.789 -29.363 51.684  1.00 18.39 ? 620  TYR A CG    1 
ATOM   4699  C  CD1   . TYR A 1 600 ? -34.453 -30.469 50.902  1.00 19.55 ? 620  TYR A CD1   1 
ATOM   4700  C  CD2   . TYR A 1 600 ? -35.513 -29.580 52.846  1.00 18.60 ? 620  TYR A CD2   1 
ATOM   4701  C  CE1   . TYR A 1 600 ? -34.829 -31.761 51.272  1.00 20.23 ? 620  TYR A CE1   1 
ATOM   4702  C  CE2   . TYR A 1 600 ? -35.900 -30.868 53.228  1.00 18.85 ? 620  TYR A CE2   1 
ATOM   4703  C  CZ    . TYR A 1 600 ? -35.565 -31.951 52.434  1.00 19.42 ? 620  TYR A CZ    1 
ATOM   4704  O  OH    . TYR A 1 600 ? -35.942 -33.223 52.800  1.00 19.76 ? 620  TYR A OH    1 
ATOM   4705  N  N     . PRO A 1 601 ? -31.600 -26.111 50.053  1.00 17.71 ? 621  PRO A N     1 
ATOM   4706  C  CA    . PRO A 1 601 ? -31.505 -24.774 49.497  1.00 17.61 ? 621  PRO A CA    1 
ATOM   4707  C  C     . PRO A 1 601 ? -32.818 -24.352 48.831  1.00 17.65 ? 621  PRO A C     1 
ATOM   4708  O  O     . PRO A 1 601 ? -33.189 -23.185 48.900  1.00 17.78 ? 621  PRO A O     1 
ATOM   4709  C  CB    . PRO A 1 601 ? -30.370 -24.884 48.472  1.00 17.32 ? 621  PRO A CB    1 
ATOM   4710  C  CG    . PRO A 1 601 ? -30.141 -26.327 48.274  1.00 17.80 ? 621  PRO A CG    1 
ATOM   4711  C  CD    . PRO A 1 601 ? -30.491 -26.959 49.587  1.00 18.03 ? 621  PRO A CD    1 
ATOM   4712  N  N     . LEU A 1 602 ? -33.499 -25.300 48.195  1.00 17.47 ? 622  LEU A N     1 
ATOM   4713  C  CA    . LEU A 1 602 ? -34.834 -25.061 47.647  1.00 17.42 ? 622  LEU A CA    1 
ATOM   4714  C  C     . LEU A 1 602 ? -35.679 -26.288 47.872  1.00 17.03 ? 622  LEU A C     1 
ATOM   4715  O  O     . LEU A 1 602 ? -35.236 -27.432 47.645  1.00 16.65 ? 622  LEU A O     1 
ATOM   4716  C  CB    . LEU A 1 602 ? -34.801 -24.746 46.135  1.00 17.41 ? 622  LEU A CB    1 
ATOM   4717  C  CG    . LEU A 1 602 ? -36.140 -24.728 45.377  1.00 18.17 ? 622  LEU A CG    1 
ATOM   4718  C  CD1   . LEU A 1 602 ? -37.013 -23.541 45.799  1.00 18.39 ? 622  LEU A CD1   1 
ATOM   4719  C  CD2   . LEU A 1 602 ? -35.931 -24.722 43.828  1.00 16.74 ? 622  LEU A CD2   1 
ATOM   4720  N  N     . ALA A 1 603 ? -36.907 -26.033 48.301  1.00 16.66 ? 623  ALA A N     1 
ATOM   4721  C  CA    . ALA A 1 603 ? -37.929 -27.043 48.364  1.00 16.63 ? 623  ALA A CA    1 
ATOM   4722  C  C     . ALA A 1 603 ? -39.257 -26.382 47.988  1.00 16.71 ? 623  ALA A C     1 
ATOM   4723  O  O     . ALA A 1 603 ? -39.491 -25.204 48.290  1.00 17.22 ? 623  ALA A O     1 
ATOM   4724  C  CB    . ALA A 1 603 ? -37.973 -27.648 49.767  1.00 16.31 ? 623  ALA A CB    1 
ATOM   4725  N  N     . VAL A 1 604 ? -40.115 -27.131 47.316  1.00 16.66 ? 624  VAL A N     1 
ATOM   4726  C  CA    . VAL A 1 604 ? -41.398 -26.602 46.846  1.00 16.74 ? 624  VAL A CA    1 
ATOM   4727  C  C     . VAL A 1 604 ? -42.526 -27.379 47.506  1.00 16.84 ? 624  VAL A C     1 
ATOM   4728  O  O     . VAL A 1 604 ? -42.505 -28.609 47.504  1.00 17.83 ? 624  VAL A O     1 
ATOM   4729  C  CB    . VAL A 1 604 ? -41.487 -26.714 45.302  1.00 16.70 ? 624  VAL A CB    1 
ATOM   4730  C  CG1   . VAL A 1 604 ? -42.786 -26.118 44.775  1.00 16.07 ? 624  VAL A CG1   1 
ATOM   4731  C  CG2   . VAL A 1 604 ? -40.280 -26.018 44.663  1.00 16.13 ? 624  VAL A CG2   1 
ATOM   4732  N  N     . THR A 1 605 ? -43.489 -26.688 48.113  1.00 17.19 ? 625  THR A N     1 
ATOM   4733  C  CA    . THR A 1 605 ? -44.646 -27.378 48.702  1.00 16.78 ? 625  THR A CA    1 
ATOM   4734  C  C     . THR A 1 605 ? -45.971 -26.927 48.107  1.00 17.26 ? 625  THR A C     1 
ATOM   4735  O  O     . THR A 1 605 ? -46.072 -25.867 47.504  1.00 17.63 ? 625  THR A O     1 
ATOM   4736  C  CB    . THR A 1 605 ? -44.707 -27.248 50.247  1.00 17.11 ? 625  THR A CB    1 
ATOM   4737  O  OG1   . THR A 1 605 ? -44.818 -25.868 50.647  1.00 16.81 ? 625  THR A OG1   1 
ATOM   4738  C  CG2   . THR A 1 605 ? -43.476 -27.886 50.888  1.00 16.67 ? 625  THR A CG2   1 
ATOM   4739  N  N     . LYS A 1 606 ? -46.988 -27.757 48.263  1.00 17.55 ? 626  LYS A N     1 
ATOM   4740  C  CA    . LYS A 1 606 ? -48.353 -27.349 47.954  1.00 18.08 ? 626  LYS A CA    1 
ATOM   4741  C  C     . LYS A 1 606 ? -48.870 -26.460 49.079  1.00 18.24 ? 626  LYS A C     1 
ATOM   4742  O  O     . LYS A 1 606 ? -48.766 -26.823 50.253  1.00 18.67 ? 626  LYS A O     1 
ATOM   4743  C  CB    . LYS A 1 606 ? -49.245 -28.571 47.803  1.00 18.13 ? 626  LYS A CB    1 
ATOM   4744  C  CG    . LYS A 1 606 ? -50.732 -28.245 47.659  1.00 18.69 ? 626  LYS A CG    1 
ATOM   4745  C  CD    . LYS A 1 606 ? -51.502 -29.468 47.227  1.00 19.49 ? 626  LYS A CD    1 
ATOM   4746  C  CE    . LYS A 1 606 ? -53.006 -29.252 47.379  1.00 20.65 ? 626  LYS A CE    1 
ATOM   4747  N  NZ    . LYS A 1 606 ? -53.695 -30.166 46.448  1.00 21.80 ? 626  LYS A NZ    1 
ATOM   4748  N  N     . TYR A 1 607 ? -49.409 -25.295 48.718  1.00 19.07 ? 627  TYR A N     1 
ATOM   4749  C  CA    . TYR A 1 607 ? -49.948 -24.335 49.690  1.00 19.28 ? 627  TYR A CA    1 
ATOM   4750  C  C     . TYR A 1 607 ? -50.955 -24.977 50.660  1.00 19.88 ? 627  TYR A C     1 
ATOM   4751  O  O     . TYR A 1 607 ? -51.756 -25.822 50.272  1.00 19.65 ? 627  TYR A O     1 
ATOM   4752  C  CB    . TYR A 1 607 ? -50.624 -23.157 48.987  1.00 19.17 ? 627  TYR A CB    1 
ATOM   4753  C  CG    . TYR A 1 607 ? -51.122 -22.106 49.956  1.00 19.84 ? 627  TYR A CG    1 
ATOM   4754  C  CD1   . TYR A 1 607 ? -52.392 -22.198 50.525  1.00 19.00 ? 627  TYR A CD1   1 
ATOM   4755  C  CD2   . TYR A 1 607 ? -50.314 -21.023 50.326  1.00 20.63 ? 627  TYR A CD2   1 
ATOM   4756  C  CE1   . TYR A 1 607 ? -52.843 -21.246 51.431  1.00 20.55 ? 627  TYR A CE1   1 
ATOM   4757  C  CE2   . TYR A 1 607 ? -50.770 -20.061 51.228  1.00 20.67 ? 627  TYR A CE2   1 
ATOM   4758  C  CZ    . TYR A 1 607 ? -52.027 -20.184 51.778  1.00 20.65 ? 627  TYR A CZ    1 
ATOM   4759  O  OH    . TYR A 1 607 ? -52.465 -19.245 52.667  1.00 21.66 ? 627  TYR A OH    1 
ATOM   4760  N  N     . ARG A 1 608 ? -50.894 -24.549 51.912  1.00 20.34 ? 628  ARG A N     1 
ATOM   4761  C  CA    . ARG A 1 608 ? -51.791 -25.033 52.944  1.00 21.60 ? 628  ARG A CA    1 
ATOM   4762  C  C     . ARG A 1 608 ? -51.764 -24.056 54.120  1.00 21.36 ? 628  ARG A C     1 
ATOM   4763  O  O     . ARG A 1 608 ? -50.683 -23.655 54.561  1.00 20.86 ? 628  ARG A O     1 
ATOM   4764  C  CB    . ARG A 1 608 ? -51.325 -26.423 53.391  1.00 21.78 ? 628  ARG A CB    1 
ATOM   4765  C  CG    . ARG A 1 608 ? -52.263 -27.127 54.287  1.00 22.87 ? 628  ARG A CG    1 
ATOM   4766  C  CD    . ARG A 1 608 ? -51.943 -28.613 54.378  1.00 20.95 ? 628  ARG A CD    1 
ATOM   4767  N  NE    . ARG A 1 608 ? -52.479 -29.277 53.199  1.00 19.68 ? 628  ARG A NE    1 
ATOM   4768  C  CZ    . ARG A 1 608 ? -51.774 -29.883 52.254  1.00 18.09 ? 628  ARG A CZ    1 
ATOM   4769  N  NH1   . ARG A 1 608 ? -50.447 -29.971 52.313  1.00 19.61 ? 628  ARG A NH1   1 
ATOM   4770  N  NH2   . ARG A 1 608 ? -52.418 -30.423 51.237  1.00 18.09 ? 628  ARG A NH2   1 
ATOM   4771  N  N     . GLU A 1 609 ? -52.947 -23.695 54.625  1.00 21.85 ? 629  GLU A N     1 
ATOM   4772  C  CA    . GLU A 1 609 ? -53.084 -22.790 55.778  1.00 22.06 ? 629  GLU A CA    1 
ATOM   4773  C  C     . GLU A 1 609 ? -52.458 -23.339 57.053  1.00 22.75 ? 629  GLU A C     1 
ATOM   4774  O  O     . GLU A 1 609 ? -52.070 -22.580 57.945  1.00 23.27 ? 629  GLU A O     1 
ATOM   4775  C  CB    . GLU A 1 609 ? -54.559 -22.474 56.045  1.00 22.20 ? 629  GLU A CB    1 
ATOM   4776  C  CG    . GLU A 1 609 ? -55.239 -21.618 54.990  1.00 22.10 ? 629  GLU A CG    1 
ATOM   4777  C  CD    . GLU A 1 609 ? -54.702 -20.189 54.940  1.00 23.45 ? 629  GLU A CD    1 
ATOM   4778  O  OE1   . GLU A 1 609 ? -54.268 -19.667 56.003  1.00 23.72 ? 629  GLU A OE1   1 
ATOM   4779  O  OE2   . GLU A 1 609 ? -54.724 -19.587 53.833  1.00 21.53 ? 629  GLU A OE2   1 
ATOM   4780  N  N     . SER A 1 610 ? -52.382 -24.660 57.162  1.00 23.18 ? 630  SER A N     1 
ATOM   4781  C  CA    . SER A 1 610 ? -51.686 -25.284 58.279  1.00 23.32 ? 630  SER A CA    1 
ATOM   4782  C  C     . SER A 1 610 ? -50.166 -25.295 58.094  1.00 23.13 ? 630  SER A C     1 
ATOM   4783  O  O     . SER A 1 610 ? -49.470 -25.788 58.971  1.00 24.19 ? 630  SER A O     1 
ATOM   4784  C  CB    . SER A 1 610 ? -52.186 -26.720 58.493  1.00 23.22 ? 630  SER A CB    1 
ATOM   4785  O  OG    . SER A 1 610 ? -52.155 -27.451 57.279  1.00 24.00 ? 630  SER A OG    1 
ATOM   4786  N  N     . GLU A 1 611 ? -49.647 -24.740 56.997  1.00 22.50 ? 631  GLU A N     1 
ATOM   4787  C  CA    . GLU A 1 611 ? -48.196 -24.763 56.722  1.00 22.26 ? 631  GLU A CA    1 
ATOM   4788  C  C     . GLU A 1 611 ? -47.654 -23.392 56.302  1.00 22.17 ? 631  GLU A C     1 
ATOM   4789  O  O     . GLU A 1 611 ? -46.801 -23.292 55.397  1.00 22.23 ? 631  GLU A O     1 
ATOM   4790  C  CB    . GLU A 1 611 ? -47.866 -25.789 55.621  1.00 21.90 ? 631  GLU A CB    1 
ATOM   4791  C  CG    . GLU A 1 611 ? -48.270 -27.214 55.940  1.00 22.22 ? 631  GLU A CG    1 
ATOM   4792  C  CD    . GLU A 1 611 ? -48.033 -28.178 54.786  1.00 22.66 ? 631  GLU A CD    1 
ATOM   4793  O  OE1   . GLU A 1 611 ? -47.374 -27.796 53.787  1.00 22.16 ? 631  GLU A OE1   1 
ATOM   4794  O  OE2   . GLU A 1 611 ? -48.525 -29.324 54.877  1.00 22.37 ? 631  GLU A OE2   1 
ATOM   4795  N  N     . LEU A 1 612 ? -48.136 -22.339 56.960  1.00 21.80 ? 632  LEU A N     1 
ATOM   4796  C  CA    . LEU A 1 612 ? -47.739 -20.976 56.616  1.00 21.74 ? 632  LEU A CA    1 
ATOM   4797  C  C     . LEU A 1 612 ? -46.319 -20.649 57.087  1.00 21.83 ? 632  LEU A C     1 
ATOM   4798  O  O     . LEU A 1 612 ? -45.702 -19.726 56.562  1.00 21.39 ? 632  LEU A O     1 
ATOM   4799  C  CB    . LEU A 1 612 ? -48.709 -19.953 57.221  1.00 21.56 ? 632  LEU A CB    1 
ATOM   4800  C  CG    . LEU A 1 612 ? -50.179 -20.098 56.809  1.00 22.82 ? 632  LEU A CG    1 
ATOM   4801  C  CD1   . LEU A 1 612 ? -51.079 -19.175 57.629  1.00 23.11 ? 632  LEU A CD1   1 
ATOM   4802  C  CD2   . LEU A 1 612 ? -50.346 -19.848 55.324  1.00 23.26 ? 632  LEU A CD2   1 
ATOM   4803  N  N     . CYS A 1 613 ? -45.826 -21.375 58.093  1.00 21.54 ? 633  CYS A N     1 
ATOM   4804  C  CA    . CYS A 1 613 ? -44.539 -21.069 58.693  1.00 22.35 ? 633  CYS A CA    1 
ATOM   4805  C  C     . CYS A 1 613 ? -43.673 -22.292 58.858  1.00 21.37 ? 633  CYS A C     1 
ATOM   4806  O  O     . CYS A 1 613 ? -44.163 -23.383 59.150  1.00 21.10 ? 633  CYS A O     1 
ATOM   4807  C  CB    . CYS A 1 613 ? -44.712 -20.420 60.067  1.00 22.44 ? 633  CYS A CB    1 
ATOM   4808  S  SG    . CYS A 1 613 ? -45.604 -18.875 60.003  1.00 28.94 ? 633  CYS A SG    1 
ATOM   4809  N  N     . SER A 1 614 ? -42.375 -22.089 58.676  1.00 20.87 ? 634  SER A N     1 
ATOM   4810  C  CA    . SER A 1 614 ? -41.406 -23.162 58.819  1.00 20.42 ? 634  SER A CA    1 
ATOM   4811  C  C     . SER A 1 614 ? -40.797 -23.137 60.205  1.00 19.99 ? 634  SER A C     1 
ATOM   4812  O  O     . SER A 1 614 ? -40.138 -24.092 60.606  1.00 20.46 ? 634  SER A O     1 
ATOM   4813  C  CB    . SER A 1 614 ? -40.319 -23.055 57.754  1.00 20.77 ? 634  SER A CB    1 
ATOM   4814  O  OG    . SER A 1 614 ? -39.677 -21.785 57.771  1.00 20.06 ? 634  SER A OG    1 
ATOM   4815  N  N     . SER A 1 615 ? -40.999 -22.053 60.948  1.00 19.30 ? 635  SER A N     1 
ATOM   4816  C  CA    . SER A 1 615 ? -40.520 -22.011 62.329  1.00 18.95 ? 635  SER A CA    1 
ATOM   4817  C  C     . SER A 1 615 ? -41.543 -21.394 63.260  1.00 18.37 ? 635  SER A C     1 
ATOM   4818  O  O     . SER A 1 615 ? -42.711 -21.270 62.915  1.00 18.20 ? 635  SER A O     1 
ATOM   4819  C  CB    . SER A 1 615 ? -39.190 -21.273 62.421  1.00 18.86 ? 635  SER A CB    1 
ATOM   4820  O  OG    . SER A 1 615 ? -38.546 -21.597 63.639  1.00 19.54 ? 635  SER A OG    1 
ATOM   4821  N  N     . SER A 1 616 ? -41.098 -21.029 64.452  1.00 18.03 ? 636  SER A N     1 
ATOM   4822  C  CA    . SER A 1 616 ? -41.961 -20.428 65.440  1.00 18.09 ? 636  SER A CA    1 
ATOM   4823  C  C     . SER A 1 616 ? -41.103 -19.886 66.560  1.00 18.58 ? 636  SER A C     1 
ATOM   4824  O  O     . SER A 1 616 ? -39.905 -20.212 66.666  1.00 18.52 ? 636  SER A O     1 
ATOM   4825  C  CB    . SER A 1 616 ? -42.945 -21.459 66.017  1.00 18.08 ? 636  SER A CB    1 
ATOM   4826  O  OG    . SER A 1 616 ? -42.315 -22.220 67.037  1.00 17.53 ? 636  SER A OG    1 
ATOM   4827  N  N     . ILE A 1 617 ? -41.729 -19.086 67.413  1.00 19.08 ? 637  ILE A N     1 
ATOM   4828  C  CA    . ILE A 1 617 ? -41.066 -18.568 68.613  1.00 19.76 ? 637  ILE A CA    1 
ATOM   4829  C  C     . ILE A 1 617 ? -40.701 -19.631 69.633  1.00 19.88 ? 637  ILE A C     1 
ATOM   4830  O  O     . ILE A 1 617 ? -39.915 -19.351 70.522  1.00 20.93 ? 637  ILE A O     1 
ATOM   4831  C  CB    . ILE A 1 617 ? -41.907 -17.450 69.330  1.00 19.74 ? 637  ILE A CB    1 
ATOM   4832  C  CG1   . ILE A 1 617 ? -43.247 -17.988 69.861  1.00 20.19 ? 637  ILE A CG1   1 
ATOM   4833  C  CG2   . ILE A 1 617 ? -42.104 -16.268 68.377  1.00 19.64 ? 637  ILE A CG2   1 
ATOM   4834  C  CD1   . ILE A 1 617 ? -44.004 -17.012 70.767  1.00 19.71 ? 637  ILE A CD1   1 
ATOM   4835  N  N     . TYR A 1 618 ? -41.255 -20.840 69.510  1.00 20.32 ? 638  TYR A N     1 
ATOM   4836  C  CA    . TYR A 1 618 ? -40.989 -21.923 70.473  1.00 20.29 ? 638  TYR A CA    1 
ATOM   4837  C  C     . TYR A 1 618 ? -39.793 -22.817 70.104  1.00 20.46 ? 638  TYR A C     1 
ATOM   4838  O  O     . TYR A 1 618 ? -39.302 -23.573 70.950  1.00 19.73 ? 638  TYR A O     1 
ATOM   4839  C  CB    . TYR A 1 618 ? -42.236 -22.780 70.643  1.00 20.54 ? 638  TYR A CB    1 
ATOM   4840  C  CG    . TYR A 1 618 ? -43.469 -21.946 70.933  1.00 21.04 ? 638  TYR A CG    1 
ATOM   4841  C  CD1   . TYR A 1 618 ? -44.429 -21.732 69.948  1.00 22.00 ? 638  TYR A CD1   1 
ATOM   4842  C  CD2   . TYR A 1 618 ? -43.651 -21.342 72.177  1.00 22.43 ? 638  TYR A CD2   1 
ATOM   4843  C  CE1   . TYR A 1 618 ? -45.555 -20.955 70.192  1.00 23.28 ? 638  TYR A CE1   1 
ATOM   4844  C  CE2   . TYR A 1 618 ? -44.780 -20.551 72.434  1.00 23.55 ? 638  TYR A CE2   1 
ATOM   4845  C  CZ    . TYR A 1 618 ? -45.724 -20.363 71.437  1.00 23.50 ? 638  TYR A CZ    1 
ATOM   4846  O  OH    . TYR A 1 618 ? -46.834 -19.588 71.662  1.00 24.69 ? 638  TYR A OH    1 
ATOM   4847  N  N     . HIS A 1 619 ? -39.326 -22.717 68.861  1.00 19.95 ? 639  HIS A N     1 
ATOM   4848  C  CA    . HIS A 1 619 ? -38.271 -23.609 68.362  1.00 20.40 ? 639  HIS A CA    1 
ATOM   4849  C  C     . HIS A 1 619 ? -36.945 -23.476 69.109  1.00 20.64 ? 639  HIS A C     1 
ATOM   4850  O  O     . HIS A 1 619 ? -36.254 -24.473 69.307  1.00 20.50 ? 639  HIS A O     1 
ATOM   4851  C  CB    . HIS A 1 619 ? -38.026 -23.388 66.863  1.00 20.22 ? 639  HIS A CB    1 
ATOM   4852  C  CG    . HIS A 1 619 ? -39.016 -24.085 65.981  1.00 19.92 ? 639  HIS A CG    1 
ATOM   4853  N  ND1   . HIS A 1 619 ? -40.371 -23.832 66.031  1.00 18.66 ? 639  HIS A ND1   1 
ATOM   4854  C  CD2   . HIS A 1 619 ? -38.840 -25.014 65.012  1.00 18.34 ? 639  HIS A CD2   1 
ATOM   4855  C  CE1   . HIS A 1 619 ? -40.986 -24.591 65.142  1.00 19.50 ? 639  HIS A CE1   1 
ATOM   4856  N  NE2   . HIS A 1 619 ? -40.079 -25.314 64.508  1.00 18.26 ? 639  HIS A NE2   1 
ATOM   4857  N  N     . GLN A 1 620 ? -36.592 -22.254 69.509  1.00 20.89 ? 640  GLN A N     1 
ATOM   4858  C  CA    . GLN A 1 620 ? -35.317 -22.008 70.188  1.00 21.01 ? 640  GLN A CA    1 
ATOM   4859  C  C     . GLN A 1 620 ? -35.190 -22.839 71.465  1.00 21.32 ? 640  GLN A C     1 
ATOM   4860  O  O     . GLN A 1 620 ? -34.158 -23.451 71.709  1.00 20.81 ? 640  GLN A O     1 
ATOM   4861  C  CB    . GLN A 1 620 ? -35.177 -20.525 70.522  1.00 20.92 ? 640  GLN A CB    1 
ATOM   4862  C  CG    . GLN A 1 620 ? -33.980 -20.156 71.397  1.00 20.56 ? 640  GLN A CG    1 
ATOM   4863  C  CD    . GLN A 1 620 ? -32.632 -20.308 70.683  1.00 20.85 ? 640  GLN A CD    1 
ATOM   4864  O  OE1   . GLN A 1 620 ? -32.034 -19.318 70.268  1.00 20.44 ? 640  GLN A OE1   1 
ATOM   4865  N  NE2   . GLN A 1 620 ? -32.147 -21.544 70.563  1.00 20.02 ? 640  GLN A NE2   1 
ATOM   4866  N  N     . ASN A 1 621 ? -36.244 -22.842 72.280  1.00 21.61 ? 641  ASN A N     1 
ATOM   4867  C  CA    . ASN A 1 621 ? -36.192 -23.487 73.601  1.00 21.70 ? 641  ASN A CA    1 
ATOM   4868  C  C     . ASN A 1 621 ? -36.763 -24.912 73.670  1.00 21.72 ? 641  ASN A C     1 
ATOM   4869  O  O     . ASN A 1 621 ? -36.636 -25.566 74.703  1.00 22.26 ? 641  ASN A O     1 
ATOM   4870  C  CB    . ASN A 1 621 ? -36.833 -22.583 74.661  1.00 21.24 ? 641  ASN A CB    1 
ATOM   4871  C  CG    . ASN A 1 621 ? -35.997 -21.350 74.962  1.00 21.44 ? 641  ASN A CG    1 
ATOM   4872  O  OD1   . ASN A 1 621 ? -34.777 -21.319 74.712  1.00 20.67 ? 641  ASN A OD1   1 
ATOM   4873  N  ND2   . ASN A 1 621 ? -36.641 -20.333 75.528  1.00 18.74 ? 641  ASN A ND2   1 
ATOM   4874  N  N     . ASP A 1 622 ? -37.375 -25.402 72.595  1.00 22.08 ? 642  ASP A N     1 
ATOM   4875  C  CA    . ASP A 1 622 ? -37.560 -26.862 72.430  1.00 22.13 ? 642  ASP A CA    1 
ATOM   4876  C  C     . ASP A 1 622 ? -37.272 -27.313 70.997  1.00 22.25 ? 642  ASP A C     1 
ATOM   4877  O  O     . ASP A 1 622 ? -38.193 -27.683 70.250  1.00 21.25 ? 642  ASP A O     1 
ATOM   4878  C  CB    . ASP A 1 622 ? -38.961 -27.319 72.848  1.00 22.36 ? 642  ASP A CB    1 
ATOM   4879  C  CG    . ASP A 1 622 ? -39.088 -28.842 72.903  1.00 23.13 ? 642  ASP A CG    1 
ATOM   4880  O  OD1   . ASP A 1 622 ? -38.120 -29.552 72.514  1.00 23.30 ? 642  ASP A OD1   1 
ATOM   4881  O  OD2   . ASP A 1 622 ? -40.156 -29.329 73.340  1.00 24.27 ? 642  ASP A OD2   1 
ATOM   4882  N  N     . PRO A 1 623 ? -35.986 -27.306 70.618  1.00 22.62 ? 643  PRO A N     1 
ATOM   4883  C  CA    . PRO A 1 623 ? -35.581 -27.728 69.284  1.00 23.36 ? 643  PRO A CA    1 
ATOM   4884  C  C     . PRO A 1 623 ? -35.728 -29.228 69.050  1.00 23.58 ? 643  PRO A C     1 
ATOM   4885  O  O     . PRO A 1 623 ? -35.721 -29.673 67.900  1.00 23.92 ? 643  PRO A O     1 
ATOM   4886  C  CB    . PRO A 1 623 ? -34.100 -27.315 69.220  1.00 23.42 ? 643  PRO A CB    1 
ATOM   4887  C  CG    . PRO A 1 623 ? -33.662 -27.288 70.647  1.00 23.22 ? 643  PRO A CG    1 
ATOM   4888  C  CD    . PRO A 1 623 ? -34.844 -26.806 71.405  1.00 22.79 ? 643  PRO A CD    1 
ATOM   4889  N  N     . TRP A 1 624 ? -35.870 -29.989 70.133  1.00 23.75 ? 644  TRP A N     1 
ATOM   4890  C  CA    . TRP A 1 624 ? -36.013 -31.436 70.067  1.00 23.62 ? 644  TRP A CA    1 
ATOM   4891  C  C     . TRP A 1 624 ? -37.415 -31.840 69.617  1.00 23.93 ? 644  TRP A C     1 
ATOM   4892  O  O     . TRP A 1 624 ? -37.569 -32.816 68.885  1.00 24.65 ? 644  TRP A O     1 
ATOM   4893  C  CB    . TRP A 1 624 ? -35.670 -32.062 71.431  1.00 23.64 ? 644  TRP A CB    1 
ATOM   4894  C  CG    . TRP A 1 624 ? -34.289 -31.687 71.909  1.00 23.15 ? 644  TRP A CG    1 
ATOM   4895  C  CD1   . TRP A 1 624 ? -33.121 -32.244 71.517  1.00 23.56 ? 644  TRP A CD1   1 
ATOM   4896  C  CD2   . TRP A 1 624 ? -33.945 -30.651 72.847  1.00 23.79 ? 644  TRP A CD2   1 
ATOM   4897  N  NE1   . TRP A 1 624 ? -32.059 -31.632 72.150  1.00 24.94 ? 644  TRP A NE1   1 
ATOM   4898  C  CE2   . TRP A 1 624 ? -32.540 -30.652 72.975  1.00 24.42 ? 644  TRP A CE2   1 
ATOM   4899  C  CE3   . TRP A 1 624 ? -34.689 -29.734 73.598  1.00 24.37 ? 644  TRP A CE3   1 
ATOM   4900  C  CZ2   . TRP A 1 624 ? -31.863 -29.771 73.816  1.00 24.76 ? 644  TRP A CZ2   1 
ATOM   4901  C  CZ3   . TRP A 1 624 ? -34.017 -28.861 74.432  1.00 24.13 ? 644  TRP A CZ3   1 
ATOM   4902  C  CH2   . TRP A 1 624 ? -32.615 -28.885 74.536  1.00 24.70 ? 644  TRP A CH2   1 
ATOM   4903  N  N     . ASP A 1 625 ? -38.429 -31.081 70.014  1.00 23.71 ? 645  ASP A N     1 
ATOM   4904  C  CA    . ASP A 1 625 ? -39.815 -31.458 69.730  1.00 23.71 ? 645  ASP A CA    1 
ATOM   4905  C  C     . ASP A 1 625 ? -40.664 -30.216 69.445  1.00 23.45 ? 645  ASP A C     1 
ATOM   4906  O  O     . ASP A 1 625 ? -41.633 -29.943 70.151  1.00 23.55 ? 645  ASP A O     1 
ATOM   4907  C  CB    . ASP A 1 625 ? -40.362 -32.258 70.919  1.00 23.89 ? 645  ASP A CB    1 
ATOM   4908  C  CG    . ASP A 1 625 ? -41.719 -32.899 70.650  1.00 25.15 ? 645  ASP A CG    1 
ATOM   4909  O  OD1   . ASP A 1 625 ? -42.216 -32.879 69.490  1.00 24.14 ? 645  ASP A OD1   1 
ATOM   4910  O  OD2   . ASP A 1 625 ? -42.285 -33.435 71.629  1.00 26.19 ? 645  ASP A OD2   1 
ATOM   4911  N  N     . PRO A 1 626 ? -40.310 -29.465 68.384  1.00 23.34 ? 646  PRO A N     1 
ATOM   4912  C  CA    . PRO A 1 626 ? -40.959 -28.182 68.088  1.00 23.28 ? 646  PRO A CA    1 
ATOM   4913  C  C     . PRO A 1 626 ? -42.313 -28.358 67.398  1.00 23.17 ? 646  PRO A C     1 
ATOM   4914  O  O     . PRO A 1 626 ? -42.593 -29.434 66.900  1.00 22.99 ? 646  PRO A O     1 
ATOM   4915  C  CB    . PRO A 1 626 ? -39.966 -27.517 67.142  1.00 23.39 ? 646  PRO A CB    1 
ATOM   4916  C  CG    . PRO A 1 626 ? -39.376 -28.669 66.374  1.00 23.56 ? 646  PRO A CG    1 
ATOM   4917  C  CD    . PRO A 1 626 ? -39.311 -29.818 67.359  1.00 23.59 ? 646  PRO A CD    1 
ATOM   4918  N  N     . PRO A 1 627 ? -43.142 -27.294 67.351  1.00 23.08 ? 647  PRO A N     1 
ATOM   4919  C  CA    . PRO A 1 627 ? -44.506 -27.431 66.810  1.00 22.98 ? 647  PRO A CA    1 
ATOM   4920  C  C     . PRO A 1 627 ? -44.598 -27.497 65.283  1.00 22.55 ? 647  PRO A C     1 
ATOM   4921  O  O     . PRO A 1 627 ? -45.666 -27.789 64.750  1.00 22.39 ? 647  PRO A O     1 
ATOM   4922  C  CB    . PRO A 1 627 ? -45.223 -26.178 67.330  1.00 22.74 ? 647  PRO A CB    1 
ATOM   4923  C  CG    . PRO A 1 627 ? -44.130 -25.184 67.547  1.00 23.46 ? 647  PRO A CG    1 
ATOM   4924  C  CD    . PRO A 1 627 ? -42.890 -25.946 67.895  1.00 23.03 ? 647  PRO A CD    1 
ATOM   4925  N  N     . VAL A 1 628 ? -43.504 -27.207 64.590  1.00 22.30 ? 648  VAL A N     1 
ATOM   4926  C  CA    . VAL A 1 628 ? -43.463 -27.298 63.135  1.00 22.06 ? 648  VAL A CA    1 
ATOM   4927  C  C     . VAL A 1 628 ? -42.139 -27.936 62.733  1.00 21.48 ? 648  VAL A C     1 
ATOM   4928  O  O     . VAL A 1 628 ? -41.081 -27.477 63.166  1.00 21.09 ? 648  VAL A O     1 
ATOM   4929  C  CB    . VAL A 1 628 ? -43.600 -25.909 62.467  1.00 22.45 ? 648  VAL A CB    1 
ATOM   4930  C  CG1   . VAL A 1 628 ? -43.413 -26.010 60.954  1.00 22.46 ? 648  VAL A CG1   1 
ATOM   4931  C  CG2   . VAL A 1 628 ? -44.952 -25.290 62.785  1.00 23.31 ? 648  VAL A CG2   1 
ATOM   4932  N  N     . VAL A 1 629 ? -42.215 -29.015 61.948  1.00 20.61 ? 649  VAL A N     1 
ATOM   4933  C  CA    . VAL A 1 629 ? -41.035 -29.681 61.400  1.00 20.57 ? 649  VAL A CA    1 
ATOM   4934  C  C     . VAL A 1 629 ? -41.162 -29.628 59.885  1.00 20.57 ? 649  VAL A C     1 
ATOM   4935  O  O     . VAL A 1 629 ? -42.023 -30.294 59.293  1.00 20.83 ? 649  VAL A O     1 
ATOM   4936  C  CB    . VAL A 1 629 ? -40.895 -31.145 61.902  1.00 21.14 ? 649  VAL A CB    1 
ATOM   4937  C  CG1   . VAL A 1 629 ? -39.644 -31.820 61.292  1.00 19.76 ? 649  VAL A CG1   1 
ATOM   4938  C  CG2   . VAL A 1 629 ? -40.820 -31.186 63.429  1.00 20.12 ? 649  VAL A CG2   1 
ATOM   4939  N  N     . PHE A 1 630 ? -40.333 -28.805 59.250  1.00 20.28 ? 650  PHE A N     1 
ATOM   4940  C  CA    . PHE A 1 630 ? -40.499 -28.526 57.823  1.00 19.99 ? 650  PHE A CA    1 
ATOM   4941  C  C     . PHE A 1 630 ? -40.523 -29.814 56.987  1.00 20.18 ? 650  PHE A C     1 
ATOM   4942  O  O     . PHE A 1 630 ? -41.297 -29.919 56.034  1.00 19.60 ? 650  PHE A O     1 
ATOM   4943  C  CB    . PHE A 1 630 ? -39.421 -27.573 57.306  1.00 19.75 ? 650  PHE A CB    1 
ATOM   4944  C  CG    . PHE A 1 630 ? -39.514 -27.323 55.830  1.00 19.78 ? 650  PHE A CG    1 
ATOM   4945  C  CD1   . PHE A 1 630 ? -40.400 -26.383 55.331  1.00 19.47 ? 650  PHE A CD1   1 
ATOM   4946  C  CD2   . PHE A 1 630 ? -38.751 -28.070 54.935  1.00 18.22 ? 650  PHE A CD2   1 
ATOM   4947  C  CE1   . PHE A 1 630 ? -40.504 -26.168 53.968  1.00 19.32 ? 650  PHE A CE1   1 
ATOM   4948  C  CE2   . PHE A 1 630 ? -38.850 -27.862 53.574  1.00 18.89 ? 650  PHE A CE2   1 
ATOM   4949  C  CZ    . PHE A 1 630 ? -39.727 -26.911 53.084  1.00 19.19 ? 650  PHE A CZ    1 
ATOM   4950  N  N     . GLU A 1 631 ? -39.682 -30.781 57.346  1.00 20.36 ? 651  GLU A N     1 
ATOM   4951  C  CA    . GLU A 1 631 ? -39.626 -32.083 56.641  1.00 20.79 ? 651  GLU A CA    1 
ATOM   4952  C  C     . GLU A 1 631 ? -41.005 -32.737 56.511  1.00 20.71 ? 651  GLU A C     1 
ATOM   4953  O  O     . GLU A 1 631 ? -41.300 -33.394 55.506  1.00 21.34 ? 651  GLU A O     1 
ATOM   4954  C  CB    . GLU A 1 631 ? -38.654 -33.036 57.354  1.00 20.90 ? 651  GLU A CB    1 
ATOM   4955  C  CG    . GLU A 1 631 ? -38.473 -34.419 56.703  1.00 21.70 ? 651  GLU A CG    1 
ATOM   4956  C  CD    . GLU A 1 631 ? -37.683 -34.389 55.396  1.00 22.22 ? 651  GLU A CD    1 
ATOM   4957  O  OE1   . GLU A 1 631 ? -37.031 -33.368 55.091  1.00 22.05 ? 651  GLU A OE1   1 
ATOM   4958  O  OE2   . GLU A 1 631 ? -37.706 -35.410 54.678  1.00 23.80 ? 651  GLU A OE2   1 
ATOM   4959  N  N     . GLN A 1 632 ? -41.856 -32.534 57.509  1.00 20.77 ? 652  GLN A N     1 
ATOM   4960  C  CA    . GLN A 1 632 ? -43.188 -33.112 57.504  1.00 20.94 ? 652  GLN A CA    1 
ATOM   4961  C  C     . GLN A 1 632 ? -44.071 -32.579 56.377  1.00 20.57 ? 652  GLN A C     1 
ATOM   4962  O  O     . GLN A 1 632 ? -44.980 -33.278 55.933  1.00 20.38 ? 652  GLN A O     1 
ATOM   4963  C  CB    . GLN A 1 632 ? -43.864 -32.959 58.880  1.00 21.43 ? 652  GLN A CB    1 
ATOM   4964  C  CG    . GLN A 1 632 ? -43.157 -33.750 59.988  1.00 23.46 ? 652  GLN A CG    1 
ATOM   4965  C  CD    . GLN A 1 632 ? -43.792 -33.597 61.379  1.00 26.74 ? 652  GLN A CD    1 
ATOM   4966  O  OE1   . GLN A 1 632 ? -44.757 -32.849 61.571  1.00 28.82 ? 652  GLN A OE1   1 
ATOM   4967  N  NE2   . GLN A 1 632 ? -43.235 -34.308 62.356  1.00 27.00 ? 652  GLN A NE2   1 
ATOM   4968  N  N     . PHE A 1 633 ? -43.792 -31.363 55.897  1.00 20.09 ? 653  PHE A N     1 
ATOM   4969  C  CA    . PHE A 1 633 ? -44.516 -30.793 54.762  1.00 19.61 ? 653  PHE A CA    1 
ATOM   4970  C  C     . PHE A 1 633 ? -44.259 -31.601 53.479  1.00 19.57 ? 653  PHE A C     1 
ATOM   4971  O  O     . PHE A 1 633 ? -45.064 -31.558 52.533  1.00 18.84 ? 653  PHE A O     1 
ATOM   4972  C  CB    . PHE A 1 633 ? -44.103 -29.334 54.486  1.00 19.48 ? 653  PHE A CB    1 
ATOM   4973  C  CG    . PHE A 1 633 ? -44.325 -28.360 55.637  1.00 19.51 ? 653  PHE A CG    1 
ATOM   4974  C  CD1   . PHE A 1 633 ? -44.980 -28.720 56.813  1.00 20.30 ? 653  PHE A CD1   1 
ATOM   4975  C  CD2   . PHE A 1 633 ? -43.894 -27.048 55.501  1.00 19.67 ? 653  PHE A CD2   1 
ATOM   4976  C  CE1   . PHE A 1 633 ? -45.171 -27.796 57.829  1.00 20.92 ? 653  PHE A CE1   1 
ATOM   4977  C  CE2   . PHE A 1 633 ? -44.087 -26.124 56.507  1.00 20.52 ? 653  PHE A CE2   1 
ATOM   4978  C  CZ    . PHE A 1 633 ? -44.728 -26.498 57.676  1.00 20.88 ? 653  PHE A CZ    1 
ATOM   4979  N  N     . LEU A 1 634 ? -43.127 -32.307 53.442  1.00 19.55 ? 654  LEU A N     1 
ATOM   4980  C  CA    . LEU A 1 634 ? -42.742 -33.126 52.285  1.00 19.75 ? 654  LEU A CA    1 
ATOM   4981  C  C     . LEU A 1 634 ? -43.219 -34.584 52.387  1.00 19.63 ? 654  LEU A C     1 
ATOM   4982  O  O     . LEU A 1 634 ? -43.227 -35.300 51.392  1.00 20.09 ? 654  LEU A O     1 
ATOM   4983  C  CB    . LEU A 1 634 ? -41.214 -33.109 52.117  1.00 19.58 ? 654  LEU A CB    1 
ATOM   4984  C  CG    . LEU A 1 634 ? -40.517 -31.743 52.081  1.00 19.90 ? 654  LEU A CG    1 
ATOM   4985  C  CD1   . LEU A 1 634 ? -38.998 -31.923 52.093  1.00 19.18 ? 654  LEU A CD1   1 
ATOM   4986  C  CD2   . LEU A 1 634 ? -40.953 -30.946 50.851  1.00 20.01 ? 654  LEU A CD2   1 
ATOM   4987  N  N     . HIS A 1 635 ? -43.597 -35.022 53.581  1.00 19.38 ? 655  HIS A N     1 
ATOM   4988  C  CA    . HIS A 1 635 ? -43.988 -36.412 53.804  1.00 19.66 ? 655  HIS A CA    1 
ATOM   4989  C  C     . HIS A 1 635 ? -45.064 -36.943 52.858  1.00 19.37 ? 655  HIS A C     1 
ATOM   4990  O  O     . HIS A 1 635 ? -44.939 -38.052 52.354  1.00 19.19 ? 655  HIS A O     1 
ATOM   4991  C  CB    . HIS A 1 635 ? -44.443 -36.632 55.250  1.00 19.91 ? 655  HIS A CB    1 
ATOM   4992  C  CG    . HIS A 1 635 ? -43.317 -36.690 56.229  1.00 20.46 ? 655  HIS A CG    1 
ATOM   4993  N  ND1   . HIS A 1 635 ? -43.518 -36.730 57.591  1.00 21.94 ? 655  HIS A ND1   1 
ATOM   4994  C  CD2   . HIS A 1 635 ? -41.975 -36.699 56.044  1.00 20.97 ? 655  HIS A CD2   1 
ATOM   4995  C  CE1   . HIS A 1 635 ? -42.345 -36.793 58.202  1.00 22.41 ? 655  HIS A CE1   1 
ATOM   4996  N  NE2   . HIS A 1 635 ? -41.394 -36.773 57.284  1.00 21.22 ? 655  HIS A NE2   1 
ATOM   4997  N  N     . ASN A 1 636 ? -46.119 -36.170 52.638  1.00 19.12 ? 656  ASN A N     1 
ATOM   4998  C  CA    . ASN A 1 636 ? -47.200 -36.624 51.780  1.00 18.63 ? 656  ASN A CA    1 
ATOM   4999  C  C     . ASN A 1 636 ? -46.911 -36.498 50.274  1.00 18.66 ? 656  ASN A C     1 
ATOM   5000  O  O     . ASN A 1 636 ? -47.722 -36.922 49.451  1.00 18.07 ? 656  ASN A O     1 
ATOM   5001  C  CB    . ASN A 1 636 ? -48.534 -35.973 52.176  1.00 18.75 ? 656  ASN A CB    1 
ATOM   5002  C  CG    . ASN A 1 636 ? -48.495 -34.447 52.157  1.00 18.60 ? 656  ASN A CG    1 
ATOM   5003  O  OD1   . ASN A 1 636 ? -47.533 -33.835 51.686  1.00 19.41 ? 656  ASN A OD1   1 
ATOM   5004  N  ND2   . ASN A 1 636 ? -49.548 -33.828 52.688  1.00 18.06 ? 656  ASN A ND2   1 
ATOM   5005  N  N     . ASN A 1 637 ? -45.757 -35.931 49.922  1.00 18.70 ? 657  ASN A N     1 
ATOM   5006  C  CA    . ASN A 1 637 ? -45.264 -35.935 48.541  1.00 19.07 ? 657  ASN A CA    1 
ATOM   5007  C  C     . ASN A 1 637 ? -46.330 -35.617 47.500  1.00 19.27 ? 657  ASN A C     1 
ATOM   5008  O  O     . ASN A 1 637 ? -46.559 -36.387 46.561  1.00 19.55 ? 657  ASN A O     1 
ATOM   5009  C  CB    . ASN A 1 637 ? -44.607 -37.278 48.195  1.00 18.99 ? 657  ASN A CB    1 
ATOM   5010  C  CG    . ASN A 1 637 ? -43.809 -37.211 46.911  1.00 19.25 ? 657  ASN A CG    1 
ATOM   5011  O  OD1   . ASN A 1 637 ? -43.422 -36.132 46.482  1.00 19.84 ? 657  ASN A OD1   1 
ATOM   5012  N  ND2   . ASN A 1 637 ? -43.576 -38.360 46.280  1.00 19.84 ? 657  ASN A ND2   1 
ATOM   5013  N  N     . GLU A 1 638 ? -46.952 -34.462 47.658  1.00 19.21 ? 658  GLU A N     1 
ATOM   5014  C  CA    . GLU A 1 638 ? -48.134 -34.127 46.885  1.00 19.57 ? 658  GLU A CA    1 
ATOM   5015  C  C     . GLU A 1 638 ? -47.817 -33.744 45.461  1.00 19.61 ? 658  GLU A C     1 
ATOM   5016  O  O     . GLU A 1 638 ? -46.699 -33.301 45.141  1.00 19.59 ? 658  GLU A O     1 
ATOM   5017  C  CB    . GLU A 1 638 ? -48.905 -33.005 47.565  1.00 19.28 ? 658  GLU A CB    1 
ATOM   5018  C  CG    . GLU A 1 638 ? -49.370 -33.382 48.940  1.00 19.02 ? 658  GLU A CG    1 
ATOM   5019  C  CD    . GLU A 1 638 ? -50.007 -32.222 49.670  1.00 20.20 ? 658  GLU A CD    1 
ATOM   5020  O  OE1   . GLU A 1 638 ? -49.269 -31.451 50.322  1.00 16.48 ? 658  GLU A OE1   1 
ATOM   5021  O  OE2   . GLU A 1 638 ? -51.252 -32.096 49.603  1.00 19.80 ? 658  GLU A OE2   1 
ATOM   5022  N  N     . ASN A 1 639 ? -48.814 -33.928 44.604  1.00 19.99 ? 659  ASN A N     1 
ATOM   5023  C  CA    . ASN A 1 639 ? -48.694 -33.554 43.215  1.00 20.60 ? 659  ASN A CA    1 
ATOM   5024  C  C     . ASN A 1 639 ? -48.567 -32.044 43.150  1.00 20.70 ? 659  ASN A C     1 
ATOM   5025  O  O     . ASN A 1 639 ? -49.296 -31.338 43.841  1.00 20.45 ? 659  ASN A O     1 
ATOM   5026  C  CB    . ASN A 1 639 ? -49.899 -34.032 42.405  1.00 20.80 ? 659  ASN A CB    1 
ATOM   5027  C  CG    . ASN A 1 639 ? -49.690 -33.874 40.905  1.00 21.49 ? 659  ASN A CG    1 
ATOM   5028  O  OD1   . ASN A 1 639 ? -49.818 -32.774 40.374  1.00 22.02 ? 659  ASN A OD1   1 
ATOM   5029  N  ND2   . ASN A 1 639 ? -49.356 -34.972 40.221  1.00 20.73 ? 659  ASN A ND2   1 
ATOM   5030  N  N     . ILE A 1 640 ? -47.629 -31.558 42.341  1.00 21.19 ? 660  ILE A N     1 
ATOM   5031  C  CA    . ILE A 1 640 ? -47.403 -30.120 42.211  1.00 21.51 ? 660  ILE A CA    1 
ATOM   5032  C  C     . ILE A 1 640 ? -47.516 -29.608 40.766  1.00 22.70 ? 660  ILE A C     1 
ATOM   5033  O  O     . ILE A 1 640 ? -46.921 -28.587 40.412  1.00 22.40 ? 660  ILE A O     1 
ATOM   5034  C  CB    . ILE A 1 640 ? -46.051 -29.714 42.833  1.00 21.24 ? 660  ILE A CB    1 
ATOM   5035  C  CG1   . ILE A 1 640 ? -44.900 -30.512 42.211  1.00 19.60 ? 660  ILE A CG1   1 
ATOM   5036  C  CG2   . ILE A 1 640 ? -46.123 -29.874 44.372  1.00 19.90 ? 660  ILE A CG2   1 
ATOM   5037  C  CD1   . ILE A 1 640 ? -43.515 -29.966 42.541  1.00 18.93 ? 660  ILE A CD1   1 
ATOM   5038  N  N     . GLU A 1 641 ? -48.295 -30.310 39.948  1.00 23.68 ? 661  GLU A N     1 
ATOM   5039  C  CA    . GLU A 1 641 ? -48.632 -29.842 38.608  1.00 24.67 ? 661  GLU A CA    1 
ATOM   5040  C  C     . GLU A 1 641 ? -49.882 -28.973 38.745  1.00 25.04 ? 661  GLU A C     1 
ATOM   5041  O  O     . GLU A 1 641 ? -50.874 -29.391 39.344  1.00 26.28 ? 661  GLU A O     1 
ATOM   5042  C  CB    . GLU A 1 641 ? -48.943 -31.025 37.679  1.00 25.28 ? 661  GLU A CB    1 
ATOM   5043  C  CG    . GLU A 1 641 ? -47.971 -32.216 37.730  1.00 27.89 ? 661  GLU A CG    1 
ATOM   5044  C  CD    . GLU A 1 641 ? -48.525 -33.457 36.997  1.00 32.64 ? 661  GLU A CD    1 
ATOM   5045  O  OE1   . GLU A 1 641 ? -48.615 -34.545 37.611  1.00 36.29 ? 661  GLU A OE1   1 
ATOM   5046  O  OE2   . GLU A 1 641 ? -48.890 -33.348 35.805  1.00 36.32 ? 661  GLU A OE2   1 
ATOM   5047  N  N     . ASN A 1 642 ? -49.851 -27.764 38.216  1.00 24.89 ? 662  ASN A N     1 
ATOM   5048  C  CA    A ASN A 1 642 ? -51.019 -26.899 38.241  0.50 24.66 ? 662  ASN A CA    1 
ATOM   5049  C  CA    B ASN A 1 642 ? -51.022 -26.895 38.248  0.50 24.81 ? 662  ASN A CA    1 
ATOM   5050  C  C     . ASN A 1 642 ? -51.619 -26.819 39.651  1.00 24.33 ? 662  ASN A C     1 
ATOM   5051  O  O     . ASN A 1 642 ? -52.773 -27.214 39.878  1.00 24.74 ? 662  ASN A O     1 
ATOM   5052  C  CB    A ASN A 1 642 ? -52.055 -27.401 37.233  0.50 24.82 ? 662  ASN A CB    1 
ATOM   5053  C  CB    B ASN A 1 642 ? -52.074 -27.384 37.250  0.50 25.07 ? 662  ASN A CB    1 
ATOM   5054  C  CG    A ASN A 1 642 ? -53.030 -26.325 36.820  0.50 24.82 ? 662  ASN A CG    1 
ATOM   5055  C  CG    B ASN A 1 642 ? -51.612 -27.262 35.821  0.50 25.69 ? 662  ASN A CG    1 
ATOM   5056  O  OD1   A ASN A 1 642 ? -52.633 -25.203 36.525  0.50 25.43 ? 662  ASN A OD1   1 
ATOM   5057  O  OD1   B ASN A 1 642 ? -51.484 -26.157 35.301  0.50 27.06 ? 662  ASN A OD1   1 
ATOM   5058  N  ND2   A ASN A 1 642 ? -54.313 -26.668 36.776  0.50 25.19 ? 662  ASN A ND2   1 
ATOM   5059  N  ND2   B ASN A 1 642 ? -51.366 -28.398 35.171  0.50 26.72 ? 662  ASN A ND2   1 
ATOM   5060  N  N     . GLU A 1 643 ? -50.812 -26.319 40.584  1.00 23.16 ? 663  GLU A N     1 
ATOM   5061  C  CA    A GLU A 1 643 ? -51.215 -26.154 41.983  0.50 22.68 ? 663  GLU A CA    1 
ATOM   5062  C  CA    B GLU A 1 643 ? -51.208 -26.159 41.973  0.50 22.29 ? 663  GLU A CA    1 
ATOM   5063  C  C     . GLU A 1 643 ? -50.672 -24.830 42.507  1.00 22.03 ? 663  GLU A C     1 
ATOM   5064  O  O     . GLU A 1 643 ? -49.786 -24.225 41.901  1.00 21.76 ? 663  GLU A O     1 
ATOM   5065  C  CB    A GLU A 1 643 ? -50.681 -27.299 42.862  0.50 22.70 ? 663  GLU A CB    1 
ATOM   5066  C  CB    B GLU A 1 643 ? -50.660 -27.327 42.798  0.50 22.05 ? 663  GLU A CB    1 
ATOM   5067  C  CG    A GLU A 1 643 ? -51.337 -28.663 42.640  0.50 23.29 ? 663  GLU A CG    1 
ATOM   5068  C  CG    B GLU A 1 643 ? -51.203 -27.406 44.199  0.50 20.86 ? 663  GLU A CG    1 
ATOM   5069  C  CD    A GLU A 1 643 ? -52.675 -28.809 43.341  0.50 23.44 ? 663  GLU A CD    1 
ATOM   5070  C  CD    B GLU A 1 643 ? -52.683 -27.073 44.267  0.50 19.32 ? 663  GLU A CD    1 
ATOM   5071  O  OE1   A GLU A 1 643 ? -52.787 -28.444 44.526  0.50 23.58 ? 663  GLU A OE1   1 
ATOM   5072  O  OE1   B GLU A 1 643 ? -53.482 -27.691 43.520  0.50 18.91 ? 663  GLU A OE1   1 
ATOM   5073  O  OE2   A GLU A 1 643 ? -53.621 -29.306 42.709  0.50 25.75 ? 663  GLU A OE2   1 
ATOM   5074  O  OE2   B GLU A 1 643 ? -53.036 -26.181 45.066  0.50 15.48 ? 663  GLU A OE2   1 
ATOM   5075  N  N     . ASP A 1 644 ? -51.219 -24.389 43.633  1.00 21.46 ? 664  ASP A N     1 
ATOM   5076  C  CA    . ASP A 1 644 ? -50.697 -23.260 44.377  1.00 20.54 ? 664  ASP A CA    1 
ATOM   5077  C  C     . ASP A 1 644 ? -49.423 -23.733 45.092  1.00 20.17 ? 664  ASP A C     1 
ATOM   5078  O  O     . ASP A 1 644 ? -49.496 -24.486 46.067  1.00 20.09 ? 664  ASP A O     1 
ATOM   5079  C  CB    . ASP A 1 644 ? -51.744 -22.768 45.380  1.00 20.15 ? 664  ASP A CB    1 
ATOM   5080  C  CG    . ASP A 1 644 ? -51.328 -21.483 46.084  1.00 20.08 ? 664  ASP A CG    1 
ATOM   5081  O  OD1   . ASP A 1 644 ? -50.169 -21.049 45.924  1.00 17.60 ? 664  ASP A OD1   1 
ATOM   5082  O  OD2   . ASP A 1 644 ? -52.166 -20.907 46.805  1.00 18.17 ? 664  ASP A OD2   1 
ATOM   5083  N  N     . LEU A 1 645 ? -48.268 -23.282 44.598  1.00 19.30 ? 665  LEU A N     1 
ATOM   5084  C  CA    . LEU A 1 645 ? -46.961 -23.721 45.098  1.00 18.97 ? 665  LEU A CA    1 
ATOM   5085  C  C     . LEU A 1 645 ? -46.333 -22.671 46.010  1.00 18.45 ? 665  LEU A C     1 
ATOM   5086  O  O     . LEU A 1 645 ? -46.549 -21.472 45.841  1.00 18.51 ? 665  LEU A O     1 
ATOM   5087  C  CB    . LEU A 1 645 ? -45.993 -23.995 43.926  1.00 18.80 ? 665  LEU A CB    1 
ATOM   5088  C  CG    . LEU A 1 645 ? -46.476 -24.925 42.797  1.00 19.23 ? 665  LEU A CG    1 
ATOM   5089  C  CD1   . LEU A 1 645 ? -45.401 -25.084 41.695  1.00 18.93 ? 665  LEU A CD1   1 
ATOM   5090  C  CD2   . LEU A 1 645 ? -46.883 -26.287 43.358  1.00 18.18 ? 665  LEU A CD2   1 
ATOM   5091  N  N     . VAL A 1 646 ? -45.542 -23.136 46.966  1.00 18.03 ? 666  VAL A N     1 
ATOM   5092  C  CA    . VAL A 1 646 ? -44.692 -22.279 47.768  1.00 17.29 ? 666  VAL A CA    1 
ATOM   5093  C  C     . VAL A 1 646 ? -43.249 -22.758 47.615  1.00 17.40 ? 666  VAL A C     1 
ATOM   5094  O  O     . VAL A 1 646 ? -42.968 -23.925 47.844  1.00 18.05 ? 666  VAL A O     1 
ATOM   5095  C  CB    . VAL A 1 646 ? -45.109 -22.346 49.249  1.00 17.37 ? 666  VAL A CB    1 
ATOM   5096  C  CG1   . VAL A 1 646 ? -44.225 -21.455 50.095  1.00 15.77 ? 666  VAL A CG1   1 
ATOM   5097  C  CG2   . VAL A 1 646 ? -46.607 -21.980 49.390  1.00 17.00 ? 666  VAL A CG2   1 
ATOM   5098  N  N     . ALA A 1 647 ? -42.350 -21.869 47.201  1.00 17.18 ? 667  ALA A N     1 
ATOM   5099  C  CA    . ALA A 1 647 ? -40.919 -22.147 47.212  1.00 17.19 ? 667  ALA A CA    1 
ATOM   5100  C  C     . ALA A 1 647 ? -40.378 -21.758 48.581  1.00 17.16 ? 667  ALA A C     1 
ATOM   5101  O  O     . ALA A 1 647 ? -40.791 -20.760 49.156  1.00 17.51 ? 667  ALA A O     1 
ATOM   5102  C  CB    . ALA A 1 647 ? -40.194 -21.360 46.110  1.00 16.69 ? 667  ALA A CB    1 
ATOM   5103  N  N     . TRP A 1 648 ? -39.494 -22.576 49.126  1.00 17.01 ? 668  TRP A N     1 
ATOM   5104  C  CA    . TRP A 1 648 ? -38.855 -22.267 50.394  1.00 16.89 ? 668  TRP A CA    1 
ATOM   5105  C  C     . TRP A 1 648 ? -37.364 -22.286 50.138  1.00 16.68 ? 668  TRP A C     1 
ATOM   5106  O  O     . TRP A 1 648 ? -36.853 -23.246 49.545  1.00 17.03 ? 668  TRP A O     1 
ATOM   5107  C  CB    . TRP A 1 648 ? -39.202 -23.295 51.465  1.00 16.60 ? 668  TRP A CB    1 
ATOM   5108  C  CG    . TRP A 1 648 ? -40.664 -23.512 51.750  1.00 17.04 ? 668  TRP A CG    1 
ATOM   5109  C  CD1   . TRP A 1 648 ? -41.525 -24.296 51.044  1.00 17.11 ? 668  TRP A CD1   1 
ATOM   5110  C  CD2   . TRP A 1 648 ? -41.410 -22.996 52.860  1.00 16.67 ? 668  TRP A CD2   1 
ATOM   5111  N  NE1   . TRP A 1 648 ? -42.758 -24.297 51.637  1.00 17.10 ? 668  TRP A NE1   1 
ATOM   5112  C  CE2   . TRP A 1 648 ? -42.716 -23.506 52.755  1.00 17.55 ? 668  TRP A CE2   1 
ATOM   5113  C  CE3   . TRP A 1 648 ? -41.098 -22.150 53.933  1.00 16.67 ? 668  TRP A CE3   1 
ATOM   5114  C  CZ2   . TRP A 1 648 ? -43.721 -23.197 53.685  1.00 17.63 ? 668  TRP A CZ2   1 
ATOM   5115  C  CZ3   . TRP A 1 648 ? -42.097 -21.836 54.855  1.00 16.57 ? 668  TRP A CZ3   1 
ATOM   5116  C  CH2   . TRP A 1 648 ? -43.387 -22.368 54.733  1.00 15.63 ? 668  TRP A CH2   1 
ATOM   5117  N  N     . VAL A 1 649 ? -36.672 -21.240 50.584  1.00 16.15 ? 669  VAL A N     1 
ATOM   5118  C  CA    . VAL A 1 649 ? -35.269 -21.041 50.243  1.00 15.93 ? 669  VAL A CA    1 
ATOM   5119  C  C     . VAL A 1 649 ? -34.409 -20.890 51.481  1.00 15.96 ? 669  VAL A C     1 
ATOM   5120  O  O     . VAL A 1 649 ? -34.710 -20.089 52.361  1.00 15.72 ? 669  VAL A O     1 
ATOM   5121  C  CB    . VAL A 1 649 ? -35.088 -19.791 49.369  1.00 16.19 ? 669  VAL A CB    1 
ATOM   5122  C  CG1   . VAL A 1 649 ? -33.624 -19.615 48.969  1.00 15.82 ? 669  VAL A CG1   1 
ATOM   5123  C  CG2   . VAL A 1 649 ? -35.986 -19.861 48.143  1.00 14.93 ? 669  VAL A CG2   1 
ATOM   5124  N  N     . THR A 1 650 ? -33.348 -21.688 51.548  1.00 15.72 ? 670  THR A N     1 
ATOM   5125  C  CA    . THR A 1 650 ? -32.325 -21.542 52.566  1.00 15.78 ? 670  THR A CA    1 
ATOM   5126  C  C     . THR A 1 650 ? -31.112 -20.836 51.962  1.00 16.15 ? 670  THR A C     1 
ATOM   5127  O  O     . THR A 1 650 ? -30.613 -21.220 50.897  1.00 15.85 ? 670  THR A O     1 
ATOM   5128  C  CB    . THR A 1 650 ? -31.868 -22.917 53.095  1.00 15.86 ? 670  THR A CB    1 
ATOM   5129  O  OG1   . THR A 1 650 ? -32.943 -23.538 53.800  1.00 17.00 ? 670  THR A OG1   1 
ATOM   5130  C  CG2   . THR A 1 650 ? -30.643 -22.805 54.022  1.00 14.68 ? 670  THR A CG2   1 
ATOM   5131  N  N     . VAL A 1 651 ? -30.639 -19.807 52.643  1.00 16.58 ? 671  VAL A N     1 
ATOM   5132  C  CA    . VAL A 1 651 ? -29.377 -19.169 52.282  1.00 16.85 ? 671  VAL A CA    1 
ATOM   5133  C  C     . VAL A 1 651 ? -28.550 -19.027 53.540  1.00 17.32 ? 671  VAL A C     1 
ATOM   5134  O  O     . VAL A 1 651 ? -29.086 -19.104 54.652  1.00 17.49 ? 671  VAL A O     1 
ATOM   5135  C  CB    . VAL A 1 651 ? -29.606 -17.787 51.607  1.00 16.76 ? 671  VAL A CB    1 
ATOM   5136  C  CG1   . VAL A 1 651 ? -30.390 -17.951 50.305  1.00 16.92 ? 671  VAL A CG1   1 
ATOM   5137  C  CG2   . VAL A 1 651 ? -30.339 -16.837 52.534  1.00 16.29 ? 671  VAL A CG2   1 
ATOM   5138  N  N     . GLY A 1 652 ? -27.242 -18.847 53.369  1.00 17.74 ? 672  GLY A N     1 
ATOM   5139  C  CA    . GLY A 1 652 ? -26.359 -18.581 54.489  1.00 17.84 ? 672  GLY A CA    1 
ATOM   5140  C  C     . GLY A 1 652 ? -24.889 -18.735 54.148  1.00 18.36 ? 672  GLY A C     1 
ATOM   5141  O  O     . GLY A 1 652 ? -24.515 -18.813 52.974  1.00 17.05 ? 672  GLY A O     1 
ATOM   5142  N  N     . PHE A 1 653 ? -24.066 -18.797 55.192  1.00 18.73 ? 673  PHE A N     1 
ATOM   5143  C  CA    . PHE A 1 653 ? -22.621 -18.909 55.038  1.00 19.18 ? 673  PHE A CA    1 
ATOM   5144  C  C     . PHE A 1 653 ? -21.947 -19.329 56.332  1.00 19.52 ? 673  PHE A C     1 
ATOM   5145  O  O     . PHE A 1 653 ? -22.399 -18.978 57.434  1.00 19.88 ? 673  PHE A O     1 
ATOM   5146  C  CB    . PHE A 1 653 ? -22.015 -17.583 54.527  1.00 19.28 ? 673  PHE A CB    1 
ATOM   5147  C  CG    . PHE A 1 653 ? -22.286 -16.377 55.421  1.00 20.07 ? 673  PHE A CG    1 
ATOM   5148  C  CD1   . PHE A 1 653 ? -21.330 -15.947 56.345  1.00 19.91 ? 673  PHE A CD1   1 
ATOM   5149  C  CD2   . PHE A 1 653 ? -23.470 -15.652 55.302  1.00 21.31 ? 673  PHE A CD2   1 
ATOM   5150  C  CE1   . PHE A 1 653 ? -21.560 -14.834 57.153  1.00 20.39 ? 673  PHE A CE1   1 
ATOM   5151  C  CE2   . PHE A 1 653 ? -23.722 -14.533 56.115  1.00 21.35 ? 673  PHE A CE2   1 
ATOM   5152  C  CZ    . PHE A 1 653 ? -22.760 -14.124 57.047  1.00 20.60 ? 673  PHE A CZ    1 
ATOM   5153  N  N     . LEU A 1 654 ? -20.879 -20.107 56.184  1.00 19.71 ? 674  LEU A N     1 
ATOM   5154  C  CA    . LEU A 1 654 ? -19.957 -20.381 57.266  1.00 20.07 ? 674  LEU A CA    1 
ATOM   5155  C  C     . LEU A 1 654 ? -19.221 -19.085 57.592  1.00 19.84 ? 674  LEU A C     1 
ATOM   5156  O  O     . LEU A 1 654 ? -18.701 -18.409 56.700  1.00 19.79 ? 674  LEU A O     1 
ATOM   5157  C  CB    . LEU A 1 654 ? -18.932 -21.460 56.859  1.00 20.31 ? 674  LEU A CB    1 
ATOM   5158  C  CG    . LEU A 1 654 ? -17.876 -21.870 57.906  1.00 20.43 ? 674  LEU A CG    1 
ATOM   5159  C  CD1   . LEU A 1 654 ? -18.488 -22.643 59.084  1.00 19.19 ? 674  LEU A CD1   1 
ATOM   5160  C  CD2   . LEU A 1 654 ? -16.755 -22.676 57.267  1.00 19.06 ? 674  LEU A CD2   1 
ATOM   5161  N  N     . HIS A 1 655 ? -19.191 -18.744 58.874  1.00 19.70 ? 675  HIS A N     1 
ATOM   5162  C  CA    . HIS A 1 655 ? -18.396 -17.636 59.358  1.00 19.65 ? 675  HIS A CA    1 
ATOM   5163  C  C     . HIS A 1 655 ? -17.316 -18.189 60.313  1.00 19.92 ? 675  HIS A C     1 
ATOM   5164  O  O     . HIS A 1 655 ? -17.612 -18.651 61.427  1.00 19.65 ? 675  HIS A O     1 
ATOM   5165  C  CB    . HIS A 1 655 ? -19.316 -16.602 60.026  1.00 19.86 ? 675  HIS A CB    1 
ATOM   5166  C  CG    . HIS A 1 655 ? -18.607 -15.387 60.545  1.00 19.37 ? 675  HIS A CG    1 
ATOM   5167  N  ND1   . HIS A 1 655 ? -19.250 -14.417 61.281  1.00 18.92 ? 675  HIS A ND1   1 
ATOM   5168  C  CD2   . HIS A 1 655 ? -17.317 -14.988 60.441  1.00 19.10 ? 675  HIS A CD2   1 
ATOM   5169  C  CE1   . HIS A 1 655 ? -18.386 -13.474 61.608  1.00 20.86 ? 675  HIS A CE1   1 
ATOM   5170  N  NE2   . HIS A 1 655 ? -17.204 -13.797 61.111  1.00 20.25 ? 675  HIS A NE2   1 
ATOM   5171  N  N     . ILE A 1 656 ? -16.069 -18.176 59.844  1.00 20.17 ? 676  ILE A N     1 
ATOM   5172  C  CA    . ILE A 1 656 ? -14.902 -18.441 60.696  1.00 20.45 ? 676  ILE A CA    1 
ATOM   5173  C  C     . ILE A 1 656 ? -14.390 -17.056 61.071  1.00 20.66 ? 676  ILE A C     1 
ATOM   5174  O  O     . ILE A 1 656 ? -13.841 -16.353 60.213  1.00 21.15 ? 676  ILE A O     1 
ATOM   5175  C  CB    . ILE A 1 656 ? -13.792 -19.227 59.954  1.00 20.63 ? 676  ILE A CB    1 
ATOM   5176  C  CG1   . ILE A 1 656 ? -14.275 -20.634 59.588  1.00 20.92 ? 676  ILE A CG1   1 
ATOM   5177  C  CG2   . ILE A 1 656 ? -12.507 -19.308 60.800  1.00 20.48 ? 676  ILE A CG2   1 
ATOM   5178  C  CD1   . ILE A 1 656 ? -13.362 -21.364 58.591  1.00 20.47 ? 676  ILE A CD1   1 
ATOM   5179  N  N     . PRO A 1 657 ? -14.595 -16.629 62.331  1.00 20.77 ? 677  PRO A N     1 
ATOM   5180  C  CA    . PRO A 1 657 ? -14.172 -15.261 62.627  1.00 20.56 ? 677  PRO A CA    1 
ATOM   5181  C  C     . PRO A 1 657 ? -12.672 -15.005 62.414  1.00 20.92 ? 677  PRO A C     1 
ATOM   5182  O  O     . PRO A 1 657 ? -11.845 -15.924 62.457  1.00 20.78 ? 677  PRO A O     1 
ATOM   5183  C  CB    . PRO A 1 657 ? -14.564 -15.085 64.086  1.00 21.06 ? 677  PRO A CB    1 
ATOM   5184  C  CG    . PRO A 1 657 ? -15.747 -16.023 64.258  1.00 20.91 ? 677  PRO A CG    1 
ATOM   5185  C  CD    . PRO A 1 657 ? -15.367 -17.219 63.444  1.00 20.87 ? 677  PRO A CD    1 
ATOM   5186  N  N     . HIS A 1 658 ? -12.355 -13.750 62.146  1.00 21.15 ? 678  HIS A N     1 
ATOM   5187  C  CA    . HIS A 1 658 ? -10.993 -13.306 61.933  1.00 20.90 ? 678  HIS A CA    1 
ATOM   5188  C  C     . HIS A 1 658 ? -10.858 -11.948 62.610  1.00 21.03 ? 678  HIS A C     1 
ATOM   5189  O  O     . HIS A 1 658 ? -11.869 -11.322 62.961  1.00 21.14 ? 678  HIS A O     1 
ATOM   5190  C  CB    . HIS A 1 658 ? -10.667 -13.240 60.425  1.00 20.97 ? 678  HIS A CB    1 
ATOM   5191  C  CG    . HIS A 1 658 ? -11.791 -12.733 59.567  1.00 20.41 ? 678  HIS A CG    1 
ATOM   5192  N  ND1   . HIS A 1 658 ? -11.748 -11.510 58.929  1.00 20.96 ? 678  HIS A ND1   1 
ATOM   5193  C  CD2   . HIS A 1 658 ? -12.980 -13.292 59.224  1.00 20.39 ? 678  HIS A CD2   1 
ATOM   5194  C  CE1   . HIS A 1 658 ? -12.869 -11.332 58.245  1.00 21.96 ? 678  HIS A CE1   1 
ATOM   5195  N  NE2   . HIS A 1 658 ? -13.629 -12.403 58.398  1.00 19.60 ? 678  HIS A NE2   1 
ATOM   5196  N  N     . SER A 1 659 ? -9.618  -11.501 62.793  1.00 21.15 ? 679  SER A N     1 
ATOM   5197  C  CA    . SER A 1 659 ? -9.313  -10.294 63.565  1.00 21.18 ? 679  SER A CA    1 
ATOM   5198  C  C     . SER A 1 659 ? -9.981  -9.030  63.034  1.00 21.36 ? 679  SER A C     1 
ATOM   5199  O  O     . SER A 1 659 ? -10.304 -8.124  63.815  1.00 20.99 ? 679  SER A O     1 
ATOM   5200  C  CB    . SER A 1 659 ? -7.797  -10.086 63.650  1.00 21.30 ? 679  SER A CB    1 
ATOM   5201  O  OG    . SER A 1 659 ? -7.217  -10.030 62.367  1.00 21.53 ? 679  SER A OG    1 
ATOM   5202  N  N     . GLU A 1 660 ? -10.210 -8.974  61.722  1.00 21.31 ? 680  GLU A N     1 
ATOM   5203  C  CA    . GLU A 1 660 ? -10.965 -7.868  61.119  1.00 21.14 ? 680  GLU A CA    1 
ATOM   5204  C  C     . GLU A 1 660 ? -12.425 -7.782  61.598  1.00 21.33 ? 680  GLU A C     1 
ATOM   5205  O  O     . GLU A 1 660 ? -13.061 -6.741  61.436  1.00 21.46 ? 680  GLU A O     1 
ATOM   5206  C  CB    . GLU A 1 660 ? -10.931 -7.950  59.584  1.00 21.07 ? 680  GLU A CB    1 
ATOM   5207  C  CG    . GLU A 1 660 ? -9.541  -7.726  58.973  1.00 21.18 ? 680  GLU A CG    1 
ATOM   5208  C  CD    . GLU A 1 660 ? -8.699  -8.982  58.868  1.00 20.93 ? 680  GLU A CD    1 
ATOM   5209  O  OE1   . GLU A 1 660 ? -9.187  -10.079 59.215  1.00 22.04 ? 680  GLU A OE1   1 
ATOM   5210  O  OE2   . GLU A 1 660 ? -7.535  -8.878  58.421  1.00 21.56 ? 680  GLU A OE2   1 
ATOM   5211  N  N     . ASP A 1 661 ? -12.958 -8.848  62.196  1.00 21.24 ? 681  ASP A N     1 
ATOM   5212  C  CA    . ASP A 1 661 ? -14.285 -8.765  62.844  1.00 21.58 ? 681  ASP A CA    1 
ATOM   5213  C  C     . ASP A 1 661 ? -14.308 -7.931  64.140  1.00 21.64 ? 681  ASP A C     1 
ATOM   5214  O  O     . ASP A 1 661 ? -15.360 -7.785  64.750  1.00 21.36 ? 681  ASP A O     1 
ATOM   5215  C  CB    . ASP A 1 661 ? -14.837 -10.166 63.157  1.00 21.54 ? 681  ASP A CB    1 
ATOM   5216  C  CG    . ASP A 1 661 ? -15.288 -10.917 61.926  1.00 21.13 ? 681  ASP A CG    1 
ATOM   5217  O  OD1   . ASP A 1 661 ? -15.901 -10.297 61.044  1.00 23.23 ? 681  ASP A OD1   1 
ATOM   5218  O  OD2   . ASP A 1 661 ? -15.063 -12.146 61.853  1.00 21.18 ? 681  ASP A OD2   1 
ATOM   5219  N  N     . ILE A 1 662 ? -13.162 -7.408  64.576  1.00 21.88 ? 682  ILE A N     1 
ATOM   5220  C  CA    . ILE A 1 662 ? -13.107 -6.587  65.786  1.00 22.02 ? 682  ILE A CA    1 
ATOM   5221  C  C     . ILE A 1 662 ? -13.057 -5.099  65.451  1.00 21.87 ? 682  ILE A C     1 
ATOM   5222  O  O     . ILE A 1 662 ? -12.175 -4.654  64.716  1.00 22.22 ? 682  ILE A O     1 
ATOM   5223  C  CB    . ILE A 1 662 ? -11.869 -6.921  66.643  1.00 22.35 ? 682  ILE A CB    1 
ATOM   5224  C  CG1   . ILE A 1 662 ? -11.906 -8.381  67.107  1.00 22.66 ? 682  ILE A CG1   1 
ATOM   5225  C  CG2   . ILE A 1 662 ? -11.795 -5.979  67.848  1.00 22.85 ? 682  ILE A CG2   1 
ATOM   5226  C  CD1   . ILE A 1 662 ? -13.090 -8.740  67.999  1.00 21.55 ? 682  ILE A CD1   1 
ATOM   5227  N  N     . PRO A 1 663 ? -13.975 -4.305  66.019  1.00 21.59 ? 683  PRO A N     1 
ATOM   5228  C  CA    . PRO A 1 663 ? -15.006 -4.643  66.989  1.00 21.40 ? 683  PRO A CA    1 
ATOM   5229  C  C     . PRO A 1 663 ? -16.246 -5.315  66.400  1.00 21.25 ? 683  PRO A C     1 
ATOM   5230  O  O     . PRO A 1 663 ? -16.945 -6.032  67.113  1.00 21.41 ? 683  PRO A O     1 
ATOM   5231  C  CB    . PRO A 1 663 ? -15.385 -3.278  67.556  1.00 21.58 ? 683  PRO A CB    1 
ATOM   5232  C  CG    . PRO A 1 663 ? -15.172 -2.352  66.415  1.00 21.55 ? 683  PRO A CG    1 
ATOM   5233  C  CD    . PRO A 1 663 ? -13.963 -2.864  65.721  1.00 21.47 ? 683  PRO A CD    1 
ATOM   5234  N  N     . ASN A 1 664 ? -16.529 -5.074  65.128  1.00 21.19 ? 684  ASN A N     1 
ATOM   5235  C  CA    . ASN A 1 664 ? -17.752 -5.589  64.502  1.00 21.72 ? 684  ASN A CA    1 
ATOM   5236  C  C     . ASN A 1 664 ? -17.484 -6.306  63.187  1.00 21.73 ? 684  ASN A C     1 
ATOM   5237  O  O     . ASN A 1 664 ? -16.554 -5.960  62.455  1.00 21.41 ? 684  ASN A O     1 
ATOM   5238  C  CB    . ASN A 1 664 ? -18.693 -4.429  64.178  1.00 21.66 ? 684  ASN A CB    1 
ATOM   5239  C  CG    . ASN A 1 664 ? -19.647 -4.075  65.305  1.00 21.94 ? 684  ASN A CG    1 
ATOM   5240  O  OD1   . ASN A 1 664 ? -20.654 -3.413  65.053  1.00 22.83 ? 684  ASN A OD1   1 
ATOM   5241  N  ND2   . ASN A 1 664 ? -19.357 -4.502  66.529  1.00 21.40 ? 684  ASN A ND2   1 
ATOM   5242  N  N     A THR A 1 665 ? -18.320 -7.297  62.883  0.50 21.81 ? 685  THR A N     1 
ATOM   5243  N  N     B THR A 1 665 ? -18.311 -7.299  62.875  0.50 22.02 ? 685  THR A N     1 
ATOM   5244  C  CA    A THR A 1 665 ? -18.369 -7.874  61.548  0.50 21.67 ? 685  THR A CA    1 
ATOM   5245  C  CA    B THR A 1 665 ? -18.309 -7.866  61.539  0.50 22.10 ? 685  THR A CA    1 
ATOM   5246  C  C     A THR A 1 665 ? -18.833 -6.777  60.588  0.50 21.64 ? 685  THR A C     1 
ATOM   5247  C  C     B THR A 1 665 ? -18.825 -6.789  60.588  0.50 21.86 ? 685  THR A C     1 
ATOM   5248  O  O     A THR A 1 665 ? -19.693 -5.962  60.945  0.50 21.67 ? 685  THR A O     1 
ATOM   5249  O  O     B THR A 1 665 ? -19.710 -6.004  60.949  0.50 21.90 ? 685  THR A O     1 
ATOM   5250  C  CB    A THR A 1 665 ? -19.335 -9.073  61.501  0.50 21.88 ? 685  THR A CB    1 
ATOM   5251  C  CB    B THR A 1 665 ? -19.174 -9.125  61.452  0.50 22.34 ? 685  THR A CB    1 
ATOM   5252  O  OG1   A THR A 1 665 ? -18.853 -10.110 62.365  0.50 21.99 ? 685  THR A OG1   1 
ATOM   5253  O  OG1   B THR A 1 665 ? -20.531 -8.803  61.778  0.50 23.34 ? 685  THR A OG1   1 
ATOM   5254  C  CG2   A THR A 1 665 ? -19.478 -9.618  60.081  0.50 21.08 ? 685  THR A CG2   1 
ATOM   5255  C  CG2   B THR A 1 665 ? -18.668 -10.172 62.417  0.50 22.55 ? 685  THR A CG2   1 
ATOM   5256  N  N     . ALA A 1 666 ? -18.241 -6.729  59.395  1.00 21.33 ? 686  ALA A N     1 
ATOM   5257  C  CA    . ALA A 1 666 ? -18.592 -5.715  58.399  1.00 21.23 ? 686  ALA A CA    1 
ATOM   5258  C  C     . ALA A 1 666 ? -19.464 -6.341  57.299  1.00 21.06 ? 686  ALA A C     1 
ATOM   5259  O  O     . ALA A 1 666 ? -19.431 -7.550  57.096  1.00 20.75 ? 686  ALA A O     1 
ATOM   5260  C  CB    . ALA A 1 666 ? -17.317 -5.097  57.816  1.00 20.98 ? 686  ALA A CB    1 
ATOM   5261  N  N     . THR A 1 667 ? -20.248 -5.519  56.601  1.00 21.51 ? 687  THR A N     1 
ATOM   5262  C  CA    . THR A 1 667 ? -21.201 -6.016  55.589  1.00 21.61 ? 687  THR A CA    1 
ATOM   5263  C  C     . THR A 1 667 ? -20.606 -6.443  54.232  1.00 22.06 ? 687  THR A C     1 
ATOM   5264  O  O     . THR A 1 667 ? -21.206 -7.276  53.549  1.00 21.99 ? 687  THR A O     1 
ATOM   5265  C  CB    . THR A 1 667 ? -22.340 -5.009  55.326  1.00 21.67 ? 687  THR A CB    1 
ATOM   5266  O  OG1   . THR A 1 667 ? -21.806 -3.803  54.762  1.00 20.34 ? 687  THR A OG1   1 
ATOM   5267  C  CG2   . THR A 1 667 ? -23.093 -4.700  56.628  1.00 21.55 ? 687  THR A CG2   1 
ATOM   5268  N  N     . PRO A 1 668 ? -19.455 -5.865  53.819  1.00 22.82 ? 688  PRO A N     1 
ATOM   5269  C  CA    . PRO A 1 668 ? -18.912 -6.272  52.508  1.00 23.13 ? 688  PRO A CA    1 
ATOM   5270  C  C     . PRO A 1 668 ? -18.608 -7.769  52.440  1.00 23.41 ? 688  PRO A C     1 
ATOM   5271  O  O     . PRO A 1 668 ? -17.899 -8.301  53.285  1.00 22.97 ? 688  PRO A O     1 
ATOM   5272  C  CB    . PRO A 1 668 ? -17.638 -5.436  52.381  1.00 23.25 ? 688  PRO A CB    1 
ATOM   5273  C  CG    . PRO A 1 668 ? -17.942 -4.207  53.185  1.00 23.39 ? 688  PRO A CG    1 
ATOM   5274  C  CD    . PRO A 1 668 ? -18.741 -4.687  54.355  1.00 22.55 ? 688  PRO A CD    1 
ATOM   5275  N  N     . GLY A 1 669 ? -19.208 -8.445  51.466  1.00 23.91 ? 689  GLY A N     1 
ATOM   5276  C  CA    . GLY A 1 669 ? -19.061 -9.886  51.307  1.00 23.89 ? 689  GLY A CA    1 
ATOM   5277  C  C     . GLY A 1 669 ? -19.814 -10.716 52.327  1.00 24.39 ? 689  GLY A C     1 
ATOM   5278  O  O     . GLY A 1 669 ? -19.717 -11.943 52.305  1.00 24.06 ? 689  GLY A O     1 
ATOM   5279  N  N     . ASN A 1 670 ? -20.540 -10.064 53.241  1.00 24.62 ? 690  ASN A N     1 
ATOM   5280  C  CA    . ASN A 1 670 ? -21.289 -10.782 54.274  1.00 25.16 ? 690  ASN A CA    1 
ATOM   5281  C  C     . ASN A 1 670 ? -22.799 -10.617 54.058  1.00 24.89 ? 690  ASN A C     1 
ATOM   5282  O  O     . ASN A 1 670 ? -23.543 -10.260 54.983  1.00 24.65 ? 690  ASN A O     1 
ATOM   5283  C  CB    . ASN A 1 670 ? -20.877 -10.335 55.684  1.00 25.15 ? 690  ASN A CB    1 
ATOM   5284  C  CG    . ASN A 1 670 ? -19.548 -10.938 56.134  1.00 27.50 ? 690  ASN A CG    1 
ATOM   5285  O  OD1   . ASN A 1 670 ? -19.186 -12.038 55.723  1.00 28.43 ? 690  ASN A OD1   1 
ATOM   5286  N  ND2   . ASN A 1 670 ? -18.814 -10.213 56.998  1.00 27.04 ? 690  ASN A ND2   1 
ATOM   5287  N  N     . SER A 1 671 ? -23.241 -10.873 52.830  1.00 24.32 ? 691  SER A N     1 
ATOM   5288  C  CA    . SER A 1 671 ? -24.673 -10.915 52.543  1.00 24.42 ? 691  SER A CA    1 
ATOM   5289  C  C     . SER A 1 671 ? -25.043 -12.096 51.664  1.00 23.67 ? 691  SER A C     1 
ATOM   5290  O  O     . SER A 1 671 ? -24.217 -12.606 50.903  1.00 23.94 ? 691  SER A O     1 
ATOM   5291  C  CB    . SER A 1 671 ? -25.164 -9.621  51.893  1.00 24.53 ? 691  SER A CB    1 
ATOM   5292  O  OG    . SER A 1 671 ? -24.535 -9.387  50.654  1.00 26.83 ? 691  SER A OG    1 
ATOM   5293  N  N     . VAL A 1 672 ? -26.298 -12.517 51.798  1.00 22.58 ? 692  VAL A N     1 
ATOM   5294  C  CA    . VAL A 1 672 ? -26.850 -13.619 51.046  1.00 21.82 ? 692  VAL A CA    1 
ATOM   5295  C  C     . VAL A 1 672 ? -28.312 -13.333 50.753  1.00 21.69 ? 692  VAL A C     1 
ATOM   5296  O  O     . VAL A 1 672 ? -28.908 -12.417 51.313  1.00 21.50 ? 692  VAL A O     1 
ATOM   5297  C  CB    . VAL A 1 672 ? -26.738 -14.957 51.816  1.00 22.10 ? 692  VAL A CB    1 
ATOM   5298  C  CG1   . VAL A 1 672 ? -25.324 -15.540 51.677  1.00 21.20 ? 692  VAL A CG1   1 
ATOM   5299  C  CG2   . VAL A 1 672 ? -27.132 -14.783 53.273  1.00 21.48 ? 692  VAL A CG2   1 
ATOM   5300  N  N     . GLY A 1 673 ? -28.883 -14.118 49.861  1.00 21.18 ? 693  GLY A N     1 
ATOM   5301  C  CA    . GLY A 1 673 ? -30.276 -13.960 49.504  1.00 20.92 ? 693  GLY A CA    1 
ATOM   5302  C  C     . GLY A 1 673 ? -30.541 -14.579 48.154  1.00 20.26 ? 693  GLY A C     1 
ATOM   5303  O  O     . GLY A 1 673 ? -29.875 -15.549 47.771  1.00 20.33 ? 693  GLY A O     1 
ATOM   5304  N  N     . PHE A 1 674 ? -31.497 -13.999 47.432  1.00 19.65 ? 694  PHE A N     1 
ATOM   5305  C  CA    . PHE A 1 674 ? -31.931 -14.527 46.144  1.00 19.29 ? 694  PHE A CA    1 
ATOM   5306  C  C     . PHE A 1 674 ? -32.635 -13.478 45.291  1.00 19.64 ? 694  PHE A C     1 
ATOM   5307  O  O     . PHE A 1 674 ? -33.060 -12.431 45.799  1.00 19.10 ? 694  PHE A O     1 
ATOM   5308  C  CB    . PHE A 1 674 ? -32.868 -15.722 46.358  1.00 19.06 ? 694  PHE A CB    1 
ATOM   5309  C  CG    . PHE A 1 674 ? -34.152 -15.380 47.077  1.00 18.21 ? 694  PHE A CG    1 
ATOM   5310  C  CD1   . PHE A 1 674 ? -35.286 -15.039 46.369  1.00 18.14 ? 694  PHE A CD1   1 
ATOM   5311  C  CD2   . PHE A 1 674 ? -34.231 -15.444 48.452  1.00 18.23 ? 694  PHE A CD2   1 
ATOM   5312  C  CE1   . PHE A 1 674 ? -36.484 -14.740 47.023  1.00 18.54 ? 694  PHE A CE1   1 
ATOM   5313  C  CE2   . PHE A 1 674 ? -35.418 -15.151 49.113  1.00 18.65 ? 694  PHE A CE2   1 
ATOM   5314  C  CZ    . PHE A 1 674 ? -36.546 -14.790 48.391  1.00 17.67 ? 694  PHE A CZ    1 
ATOM   5315  N  N     . LEU A 1 675 ? -32.764 -13.786 43.998  1.00 19.70 ? 695  LEU A N     1 
ATOM   5316  C  CA    . LEU A 1 675 ? -33.442 -12.930 43.038  1.00 20.14 ? 695  LEU A CA    1 
ATOM   5317  C  C     . LEU A 1 675 ? -34.623 -13.668 42.420  1.00 19.88 ? 695  LEU A C     1 
ATOM   5318  O  O     . LEU A 1 675 ? -34.568 -14.879 42.212  1.00 19.88 ? 695  LEU A O     1 
ATOM   5319  C  CB    . LEU A 1 675 ? -32.493 -12.511 41.916  1.00 20.91 ? 695  LEU A CB    1 
ATOM   5320  C  CG    . LEU A 1 675 ? -31.440 -11.467 42.273  1.00 22.94 ? 695  LEU A CG    1 
ATOM   5321  C  CD1   . LEU A 1 675 ? -30.291 -12.117 43.010  1.00 25.16 ? 695  LEU A CD1   1 
ATOM   5322  C  CD2   . LEU A 1 675 ? -30.961 -10.762 41.022  1.00 24.94 ? 695  LEU A CD2   1 
ATOM   5323  N  N     . LEU A 1 676 ? -35.694 -12.931 42.154  1.00 19.64 ? 696  LEU A N     1 
ATOM   5324  C  CA    . LEU A 1 676 ? -36.805 -13.418 41.355  1.00 19.66 ? 696  LEU A CA    1 
ATOM   5325  C  C     . LEU A 1 676 ? -36.795 -12.593 40.078  1.00 19.85 ? 696  LEU A C     1 
ATOM   5326  O  O     . LEU A 1 676 ? -36.868 -11.367 40.130  1.00 20.32 ? 696  LEU A O     1 
ATOM   5327  C  CB    . LEU A 1 676 ? -38.115 -13.263 42.110  1.00 19.61 ? 696  LEU A CB    1 
ATOM   5328  C  CG    . LEU A 1 676 ? -38.170 -14.031 43.436  1.00 20.51 ? 696  LEU A CG    1 
ATOM   5329  C  CD1   . LEU A 1 676 ? -39.439 -13.696 44.203  1.00 20.12 ? 696  LEU A CD1   1 
ATOM   5330  C  CD2   . LEU A 1 676 ? -38.054 -15.537 43.204  1.00 20.02 ? 696  LEU A CD2   1 
ATOM   5331  N  N     . ARG A 1 677 ? -36.656 -13.271 38.943  1.00 19.86 ? 697  ARG A N     1 
ATOM   5332  C  CA    A ARG A 1 677 ? -36.463 -12.637 37.646  0.60 19.81 ? 697  ARG A CA    1 
ATOM   5333  C  CA    B ARG A 1 677 ? -36.519 -12.591 37.674  0.40 19.93 ? 697  ARG A CA    1 
ATOM   5334  C  C     . ARG A 1 677 ? -37.496 -13.163 36.654  1.00 19.94 ? 697  ARG A C     1 
ATOM   5335  O  O     . ARG A 1 677 ? -37.666 -14.390 36.541  1.00 19.52 ? 697  ARG A O     1 
ATOM   5336  C  CB    A ARG A 1 677 ? -35.078 -12.985 37.090  0.60 19.75 ? 697  ARG A CB    1 
ATOM   5337  C  CB    B ARG A 1 677 ? -35.070 -12.640 37.162  0.40 20.01 ? 697  ARG A CB    1 
ATOM   5338  C  CG    A ARG A 1 677 ? -33.922 -12.731 38.030  0.60 19.98 ? 697  ARG A CG    1 
ATOM   5339  C  CG    B ARG A 1 677 ? -34.615 -13.965 36.591  0.40 20.58 ? 697  ARG A CG    1 
ATOM   5340  C  CD    A ARG A 1 677 ? -32.596 -13.200 37.431  0.60 20.73 ? 697  ARG A CD    1 
ATOM   5341  C  CD    B ARG A 1 677 ? -33.452 -13.785 35.642  0.40 21.75 ? 697  ARG A CD    1 
ATOM   5342  N  NE    A ARG A 1 677 ? -32.290 -12.584 36.139  0.60 20.85 ? 697  ARG A NE    1 
ATOM   5343  N  NE    B ARG A 1 677 ? -32.186 -13.569 36.332  0.40 22.36 ? 697  ARG A NE    1 
ATOM   5344  C  CZ    A ARG A 1 677 ? -31.158 -12.776 35.458  0.60 22.03 ? 697  ARG A CZ    1 
ATOM   5345  C  CZ    B ARG A 1 677 ? -31.039 -13.330 35.706  0.40 23.31 ? 697  ARG A CZ    1 
ATOM   5346  N  NH1   A ARG A 1 677 ? -30.190 -13.557 35.942  0.60 21.91 ? 697  ARG A NH1   1 
ATOM   5347  N  NH1   B ARG A 1 677 ? -31.014 -13.269 34.382  0.40 23.59 ? 697  ARG A NH1   1 
ATOM   5348  N  NH2   A ARG A 1 677 ? -30.983 -12.174 34.286  0.60 21.87 ? 697  ARG A NH2   1 
ATOM   5349  N  NH2   B ARG A 1 677 ? -29.920 -13.148 36.393  0.40 23.43 ? 697  ARG A NH2   1 
ATOM   5350  N  N     . PRO A 1 678 ? -38.166 -12.260 35.911  1.00 19.95 ? 698  PRO A N     1 
ATOM   5351  C  CA    . PRO A 1 678 ? -39.115 -12.757 34.917  1.00 19.77 ? 698  PRO A CA    1 
ATOM   5352  C  C     . PRO A 1 678 ? -38.388 -13.504 33.792  1.00 19.56 ? 698  PRO A C     1 
ATOM   5353  O  O     . PRO A 1 678 ? -37.278 -13.136 33.386  1.00 20.04 ? 698  PRO A O     1 
ATOM   5354  C  CB    . PRO A 1 678 ? -39.813 -11.492 34.413  1.00 19.63 ? 698  PRO A CB    1 
ATOM   5355  C  CG    . PRO A 1 678 ? -38.869 -10.379 34.701  1.00 20.51 ? 698  PRO A CG    1 
ATOM   5356  C  CD    . PRO A 1 678 ? -38.040 -10.791 35.888  1.00 19.99 ? 698  PRO A CD    1 
ATOM   5357  N  N     . PHE A 1 679 ? -39.011 -14.570 33.324  1.00 18.94 ? 699  PHE A N     1 
ATOM   5358  C  CA    . PHE A 1 679 ? -38.426 -15.432 32.307  1.00 18.68 ? 699  PHE A CA    1 
ATOM   5359  C  C     . PHE A 1 679 ? -39.567 -15.808 31.380  1.00 18.57 ? 699  PHE A C     1 
ATOM   5360  O  O     . PHE A 1 679 ? -40.396 -16.675 31.700  1.00 18.34 ? 699  PHE A O     1 
ATOM   5361  C  CB    . PHE A 1 679 ? -37.784 -16.671 32.948  1.00 18.55 ? 699  PHE A CB    1 
ATOM   5362  C  CG    . PHE A 1 679 ? -37.082 -17.547 31.973  1.00 17.22 ? 699  PHE A CG    1 
ATOM   5363  C  CD1   . PHE A 1 679 ? -35.750 -17.323 31.657  1.00 17.37 ? 699  PHE A CD1   1 
ATOM   5364  C  CD2   . PHE A 1 679 ? -37.753 -18.587 31.350  1.00 16.95 ? 699  PHE A CD2   1 
ATOM   5365  C  CE1   . PHE A 1 679 ? -35.091 -18.140 30.727  1.00 17.37 ? 699  PHE A CE1   1 
ATOM   5366  C  CE2   . PHE A 1 679 ? -37.107 -19.395 30.421  1.00 18.15 ? 699  PHE A CE2   1 
ATOM   5367  C  CZ    . PHE A 1 679 ? -35.765 -19.168 30.116  1.00 16.36 ? 699  PHE A CZ    1 
ATOM   5368  N  N     . ASN A 1 680 ? -39.628 -15.097 30.258  1.00 18.85 ? 700  ASN A N     1 
ATOM   5369  C  CA    . ASN A 1 680 ? -40.700 -15.231 29.259  1.00 18.75 ? 700  ASN A CA    1 
ATOM   5370  C  C     . ASN A 1 680 ? -42.067 -14.826 29.812  1.00 18.61 ? 700  ASN A C     1 
ATOM   5371  O  O     . ASN A 1 680 ? -43.116 -15.223 29.293  1.00 18.37 ? 700  ASN A O     1 
ATOM   5372  C  CB    . ASN A 1 680 ? -40.733 -16.640 28.670  1.00 18.68 ? 700  ASN A CB    1 
ATOM   5373  C  CG    . ASN A 1 680 ? -39.457 -16.994 27.926  1.00 19.19 ? 700  ASN A CG    1 
ATOM   5374  O  OD1   . ASN A 1 680 ? -38.941 -16.199 27.139  1.00 17.50 ? 700  ASN A OD1   1 
ATOM   5375  N  ND2   . ASN A 1 680 ? -38.964 -18.207 28.147  1.00 18.14 ? 700  ASN A ND2   1 
ATOM   5376  N  N     . PHE A 1 681 ? -42.036 -14.010 30.858  1.00 18.86 ? 701  PHE A N     1 
ATOM   5377  C  CA    . PHE A 1 681 ? -43.246 -13.522 31.492  1.00 18.91 ? 701  PHE A CA    1 
ATOM   5378  C  C     . PHE A 1 681 ? -43.835 -12.370 30.689  1.00 18.78 ? 701  PHE A C     1 
ATOM   5379  O  O     . PHE A 1 681 ? -45.034 -12.340 30.438  1.00 18.46 ? 701  PHE A O     1 
ATOM   5380  C  CB    . PHE A 1 681 ? -42.941 -13.068 32.910  1.00 19.00 ? 701  PHE A CB    1 
ATOM   5381  C  CG    . PHE A 1 681 ? -44.166 -12.802 33.742  1.00 19.90 ? 701  PHE A CG    1 
ATOM   5382  C  CD1   . PHE A 1 681 ? -44.743 -11.542 33.767  1.00 21.48 ? 701  PHE A CD1   1 
ATOM   5383  C  CD2   . PHE A 1 681 ? -44.734 -13.807 34.503  1.00 20.90 ? 701  PHE A CD2   1 
ATOM   5384  C  CE1   . PHE A 1 681 ? -45.854 -11.284 34.547  1.00 21.40 ? 701  PHE A CE1   1 
ATOM   5385  C  CE2   . PHE A 1 681 ? -45.847 -13.555 35.284  1.00 21.18 ? 701  PHE A CE2   1 
ATOM   5386  C  CZ    . PHE A 1 681 ? -46.405 -12.294 35.305  1.00 21.45 ? 701  PHE A CZ    1 
ATOM   5387  N  N     . PHE A 1 682 ? -42.979 -11.430 30.306  1.00 18.93 ? 702  PHE A N     1 
ATOM   5388  C  CA    . PHE A 1 682 ? -43.382 -10.244 29.553  1.00 19.63 ? 702  PHE A CA    1 
ATOM   5389  C  C     . PHE A 1 682 ? -42.964 -10.390 28.082  1.00 19.56 ? 702  PHE A C     1 
ATOM   5390  O  O     . PHE A 1 682 ? -42.014 -11.112 27.783  1.00 19.90 ? 702  PHE A O     1 
ATOM   5391  C  CB    . PHE A 1 682 ? -42.729 -8.990  30.151  1.00 19.81 ? 702  PHE A CB    1 
ATOM   5392  C  CG    . PHE A 1 682 ? -43.022 -8.779  31.620  1.00 21.04 ? 702  PHE A CG    1 
ATOM   5393  C  CD1   . PHE A 1 682 ? -42.073 -9.094  32.587  1.00 21.87 ? 702  PHE A CD1   1 
ATOM   5394  C  CD2   . PHE A 1 682 ? -44.243 -8.264  32.033  1.00 21.60 ? 702  PHE A CD2   1 
ATOM   5395  C  CE1   . PHE A 1 682 ? -42.334 -8.895  33.939  1.00 21.98 ? 702  PHE A CE1   1 
ATOM   5396  C  CE2   . PHE A 1 682 ? -44.509 -8.062  33.384  1.00 21.98 ? 702  PHE A CE2   1 
ATOM   5397  C  CZ    . PHE A 1 682 ? -43.556 -8.374  34.333  1.00 22.24 ? 702  PHE A CZ    1 
ATOM   5398  N  N     . PRO A 1 683 ? -43.657 -9.695  27.159  1.00 19.61 ? 703  PRO A N     1 
ATOM   5399  C  CA    . PRO A 1 683 ? -43.330 -9.813  25.726  1.00 19.57 ? 703  PRO A CA    1 
ATOM   5400  C  C     . PRO A 1 683 ? -41.935 -9.311  25.340  1.00 19.11 ? 703  PRO A C     1 
ATOM   5401  O  O     . PRO A 1 683 ? -41.366 -9.774  24.353  1.00 18.92 ? 703  PRO A O     1 
ATOM   5402  C  CB    . PRO A 1 683 ? -44.392 -8.949  25.044  1.00 19.66 ? 703  PRO A CB    1 
ATOM   5403  C  CG    . PRO A 1 683 ? -45.455 -8.763  26.054  1.00 20.06 ? 703  PRO A CG    1 
ATOM   5404  C  CD    . PRO A 1 683 ? -44.809 -8.806  27.383  1.00 19.66 ? 703  PRO A CD    1 
ATOM   5405  N  N     . GLU A 1 684 ? -41.416 -8.362  26.116  1.00 19.04 ? 704  GLU A N     1 
ATOM   5406  C  CA    . GLU A 1 684 ? -40.081 -7.780  25.915  1.00 18.75 ? 704  GLU A CA    1 
ATOM   5407  C  C     . GLU A 1 684 ? -39.695 -7.123  27.238  1.00 18.37 ? 704  GLU A C     1 
ATOM   5408  O  O     . GLU A 1 684 ? -40.474 -7.186  28.206  1.00 17.91 ? 704  GLU A O     1 
ATOM   5409  C  CB    . GLU A 1 684 ? -40.095 -6.757  24.762  1.00 19.08 ? 704  GLU A CB    1 
ATOM   5410  C  CG    . GLU A 1 684 ? -41.256 -5.756  24.857  1.00 19.68 ? 704  GLU A CG    1 
ATOM   5411  C  CD    . GLU A 1 684 ? -41.257 -4.692  23.765  1.00 21.14 ? 704  GLU A CD    1 
ATOM   5412  O  OE1   . GLU A 1 684 ? -40.627 -4.890  22.698  1.00 21.55 ? 704  GLU A OE1   1 
ATOM   5413  O  OE2   . GLU A 1 684 ? -41.912 -3.650  23.979  1.00 20.34 ? 704  GLU A OE2   1 
ATOM   5414  N  N     . ASP A 1 685 ? -38.506 -6.519  27.293  1.00 17.72 ? 705  ASP A N     1 
ATOM   5415  C  CA    . ASP A 1 685 ? -37.995 -5.876  28.516  1.00 17.64 ? 705  ASP A CA    1 
ATOM   5416  C  C     . ASP A 1 685 ? -39.040 -4.972  29.205  1.00 17.41 ? 705  ASP A C     1 
ATOM   5417  O  O     . ASP A 1 685 ? -39.400 -3.929  28.671  1.00 17.52 ? 705  ASP A O     1 
ATOM   5418  C  CB    . ASP A 1 685 ? -36.749 -5.070  28.174  1.00 17.41 ? 705  ASP A CB    1 
ATOM   5419  C  CG    . ASP A 1 685 ? -36.200 -4.273  29.353  1.00 18.43 ? 705  ASP A CG    1 
ATOM   5420  O  OD1   . ASP A 1 685 ? -36.673 -4.424  30.503  1.00 17.22 ? 705  ASP A OD1   1 
ATOM   5421  O  OD2   . ASP A 1 685 ? -35.269 -3.473  29.111  1.00 19.82 ? 705  ASP A OD2   1 
ATOM   5422  N  N     . PRO A 1 686 ? -39.516 -5.362  30.403  1.00 17.49 ? 706  PRO A N     1 
ATOM   5423  C  CA    . PRO A 1 686 ? -40.589 -4.574  31.025  1.00 18.00 ? 706  PRO A CA    1 
ATOM   5424  C  C     . PRO A 1 686 ? -40.165 -3.158  31.440  1.00 18.46 ? 706  PRO A C     1 
ATOM   5425  O  O     . PRO A 1 686 ? -41.028 -2.321  31.678  1.00 18.65 ? 706  PRO A O     1 
ATOM   5426  C  CB    . PRO A 1 686 ? -41.001 -5.429  32.240  1.00 18.14 ? 706  PRO A CB    1 
ATOM   5427  C  CG    . PRO A 1 686 ? -39.859 -6.274  32.526  1.00 17.34 ? 706  PRO A CG    1 
ATOM   5428  C  CD    . PRO A 1 686 ? -39.173 -6.543  31.218  1.00 17.34 ? 706  PRO A CD    1 
ATOM   5429  N  N     . SER A 1 687 ? -38.855 -2.889  31.484  1.00 18.73 ? 707  SER A N     1 
ATOM   5430  C  CA    . SER A 1 687 ? -38.350 -1.554  31.788  1.00 18.98 ? 707  SER A CA    1 
ATOM   5431  C  C     . SER A 1 687 ? -38.461 -0.596  30.602  1.00 19.29 ? 707  SER A C     1 
ATOM   5432  O  O     . SER A 1 687 ? -38.159 0.575   30.737  1.00 19.22 ? 707  SER A O     1 
ATOM   5433  C  CB    . SER A 1 687 ? -36.886 -1.604  32.270  1.00 18.98 ? 707  SER A CB    1 
ATOM   5434  O  OG    . SER A 1 687 ? -35.988 -1.686  31.182  1.00 17.68 ? 707  SER A OG    1 
ATOM   5435  N  N     . LEU A 1 688 ? -38.894 -1.082  29.443  1.00 19.80 ? 708  LEU A N     1 
ATOM   5436  C  CA    . LEU A 1 688 ? -39.084 -0.211  28.285  1.00 19.91 ? 708  LEU A CA    1 
ATOM   5437  C  C     . LEU A 1 688 ? -40.084 0.933   28.496  1.00 20.38 ? 708  LEU A C     1 
ATOM   5438  O  O     . LEU A 1 688 ? -40.019 1.938   27.789  1.00 19.68 ? 708  LEU A O     1 
ATOM   5439  C  CB    . LEU A 1 688 ? -39.471 -1.025  27.056  1.00 20.01 ? 708  LEU A CB    1 
ATOM   5440  C  CG    . LEU A 1 688 ? -38.311 -1.823  26.455  1.00 20.22 ? 708  LEU A CG    1 
ATOM   5441  C  CD1   . LEU A 1 688 ? -38.835 -2.848  25.456  1.00 20.48 ? 708  LEU A CD1   1 
ATOM   5442  C  CD2   . LEU A 1 688 ? -37.252 -0.907  25.825  1.00 18.91 ? 708  LEU A CD2   1 
ATOM   5443  N  N     . ALA A 1 689 ? -40.996 0.792   29.457  1.00 20.88 ? 709  ALA A N     1 
ATOM   5444  C  CA    . ALA A 1 689 ? -41.928 1.877   29.783  1.00 21.26 ? 709  ALA A CA    1 
ATOM   5445  C  C     . ALA A 1 689 ? -41.264 3.019   30.565  1.00 21.49 ? 709  ALA A C     1 
ATOM   5446  O  O     . ALA A 1 689 ? -41.857 4.089   30.708  1.00 21.24 ? 709  ALA A O     1 
ATOM   5447  C  CB    . ALA A 1 689 ? -43.143 1.330   30.560  1.00 21.67 ? 709  ALA A CB    1 
ATOM   5448  N  N     . SER A 1 690 ? -40.048 2.797   31.077  1.00 21.71 ? 710  SER A N     1 
ATOM   5449  C  CA    . SER A 1 690 ? -39.305 3.848   31.760  1.00 21.86 ? 710  SER A CA    1 
ATOM   5450  C  C     . SER A 1 690 ? -39.000 4.990   30.798  1.00 22.12 ? 710  SER A C     1 
ATOM   5451  O  O     . SER A 1 690 ? -38.495 4.766   29.708  1.00 22.61 ? 710  SER A O     1 
ATOM   5452  C  CB    . SER A 1 690 ? -37.990 3.319   32.355  1.00 21.97 ? 710  SER A CB    1 
ATOM   5453  O  OG    . SER A 1 690 ? -37.202 4.382   32.913  1.00 21.41 ? 710  SER A OG    1 
ATOM   5454  N  N     . ARG A 1 691 ? -39.294 6.215   31.214  1.00 22.54 ? 711  ARG A N     1 
ATOM   5455  C  CA    . ARG A 1 691 ? -38.978 7.382   30.405  1.00 23.16 ? 711  ARG A CA    1 
ATOM   5456  C  C     . ARG A 1 691 ? -37.599 7.984   30.723  1.00 22.67 ? 711  ARG A C     1 
ATOM   5457  O  O     . ARG A 1 691 ? -37.235 9.006   30.158  1.00 22.95 ? 711  ARG A O     1 
ATOM   5458  C  CB    . ARG A 1 691 ? -40.089 8.430   30.516  1.00 23.47 ? 711  ARG A CB    1 
ATOM   5459  C  CG    . ARG A 1 691 ? -41.474 7.979   30.006  1.00 25.86 ? 711  ARG A CG    1 
ATOM   5460  C  CD    . ARG A 1 691 ? -41.388 7.070   28.782  1.00 29.12 ? 711  ARG A CD    1 
ATOM   5461  N  NE    . ARG A 1 691 ? -42.591 7.000   27.931  1.00 32.07 ? 711  ARG A NE    1 
ATOM   5462  C  CZ    . ARG A 1 691 ? -43.419 5.954   27.811  1.00 34.36 ? 711  ARG A CZ    1 
ATOM   5463  N  NH1   . ARG A 1 691 ? -43.263 4.855   28.535  1.00 36.01 ? 711  ARG A NH1   1 
ATOM   5464  N  NH2   . ARG A 1 691 ? -44.437 6.009   26.956  1.00 34.82 ? 711  ARG A NH2   1 
ATOM   5465  N  N     . ASP A 1 692 ? -36.824 7.328   31.581  1.00 22.27 ? 712  ASP A N     1 
ATOM   5466  C  CA    . ASP A 1 692 ? -35.478 7.779   31.926  1.00 22.21 ? 712  ASP A CA    1 
ATOM   5467  C  C     . ASP A 1 692 ? -34.443 7.415   30.882  1.00 21.61 ? 712  ASP A C     1 
ATOM   5468  O  O     . ASP A 1 692 ? -33.328 7.913   30.937  1.00 20.55 ? 712  ASP A O     1 
ATOM   5469  C  CB    . ASP A 1 692 ? -35.030 7.157   33.244  1.00 22.90 ? 712  ASP A CB    1 
ATOM   5470  C  CG    . ASP A 1 692 ? -35.882 7.578   34.395  1.00 24.45 ? 712  ASP A CG    1 
ATOM   5471  O  OD1   . ASP A 1 692 ? -36.261 8.763   34.451  1.00 29.11 ? 712  ASP A OD1   1 
ATOM   5472  O  OD2   . ASP A 1 692 ? -36.160 6.724   35.252  1.00 27.97 ? 712  ASP A OD2   1 
ATOM   5473  N  N     . THR A 1 693 ? -34.801 6.519   29.959  1.00 21.38 ? 713  THR A N     1 
ATOM   5474  C  CA    . THR A 1 693 ? -33.900 6.111   28.890  1.00 21.25 ? 713  THR A CA    1 
ATOM   5475  C  C     . THR A 1 693 ? -33.401 7.319   28.082  1.00 21.34 ? 713  THR A C     1 
ATOM   5476  O  O     . THR A 1 693 ? -34.152 8.240   27.778  1.00 20.97 ? 713  THR A O     1 
ATOM   5477  C  CB    . THR A 1 693 ? -34.583 5.122   27.942  1.00 21.30 ? 713  THR A CB    1 
ATOM   5478  O  OG1   . THR A 1 693 ? -35.041 3.993   28.695  1.00 21.30 ? 713  THR A OG1   1 
ATOM   5479  C  CG2   . THR A 1 693 ? -33.613 4.657   26.842  1.00 20.40 ? 713  THR A CG2   1 
ATOM   5480  N  N     . VAL A 1 694 ? -32.118 7.305   27.752  1.00 21.46 ? 714  VAL A N     1 
ATOM   5481  C  CA    . VAL A 1 694 ? -31.542 8.340   26.911  1.00 21.40 ? 714  VAL A CA    1 
ATOM   5482  C  C     . VAL A 1 694 ? -30.886 7.686   25.702  1.00 21.31 ? 714  VAL A C     1 
ATOM   5483  O  O     . VAL A 1 694 ? -30.190 6.677   25.846  1.00 21.29 ? 714  VAL A O     1 
ATOM   5484  C  CB    . VAL A 1 694 ? -30.521 9.168   27.727  1.00 21.57 ? 714  VAL A CB    1 
ATOM   5485  C  CG1   . VAL A 1 694 ? -29.732 10.109  26.827  1.00 21.31 ? 714  VAL A CG1   1 
ATOM   5486  C  CG2   . VAL A 1 694 ? -31.261 9.940   28.850  1.00 20.69 ? 714  VAL A CG2   1 
ATOM   5487  N  N     . ILE A 1 695 ? -31.121 8.254   24.520  1.00 20.86 ? 715  ILE A N     1 
ATOM   5488  C  CA    . ILE A 1 695 ? -30.460 7.815   23.294  1.00 20.82 ? 715  ILE A CA    1 
ATOM   5489  C  C     . ILE A 1 695 ? -29.796 9.018   22.621  1.00 21.22 ? 715  ILE A C     1 
ATOM   5490  O  O     . ILE A 1 695 ? -30.459 10.026  22.354  1.00 21.48 ? 715  ILE A O     1 
ATOM   5491  C  CB    . ILE A 1 695 ? -31.447 7.156   22.277  1.00 20.69 ? 715  ILE A CB    1 
ATOM   5492  C  CG1   . ILE A 1 695 ? -32.371 6.139   22.957  1.00 19.77 ? 715  ILE A CG1   1 
ATOM   5493  C  CG2   . ILE A 1 695 ? -30.664 6.474   21.152  1.00 19.96 ? 715  ILE A CG2   1 
ATOM   5494  C  CD1   . ILE A 1 695 ? -33.360 5.461   21.993  1.00 18.30 ? 715  ILE A CD1   1 
ATOM   5495  N  N     . VAL A 1 696 ? -28.494 8.909   22.366  1.00 21.55 ? 716  VAL A N     1 
ATOM   5496  C  CA    . VAL A 1 696 ? -27.731 9.939   21.659  1.00 21.80 ? 716  VAL A CA    1 
ATOM   5497  C  C     . VAL A 1 696 ? -27.527 9.494   20.218  1.00 22.81 ? 716  VAL A C     1 
ATOM   5498  O  O     . VAL A 1 696 ? -27.059 8.377   19.976  1.00 22.35 ? 716  VAL A O     1 
ATOM   5499  C  CB    . VAL A 1 696 ? -26.351 10.166  22.284  1.00 22.04 ? 716  VAL A CB    1 
ATOM   5500  C  CG1   . VAL A 1 696 ? -25.608 11.307  21.556  1.00 20.25 ? 716  VAL A CG1   1 
ATOM   5501  C  CG2   . VAL A 1 696 ? -26.468 10.450  23.788  1.00 21.27 ? 716  VAL A CG2   1 
ATOM   5502  N  N     . TRP A 1 697 ? -27.872 10.377  19.280  1.00 23.78 ? 717  TRP A N     1 
ATOM   5503  C  CA    . TRP A 1 697 ? -27.815 10.096  17.856  1.00 25.18 ? 717  TRP A CA    1 
ATOM   5504  C  C     . TRP A 1 697 ? -26.861 11.073  17.155  1.00 26.38 ? 717  TRP A C     1 
ATOM   5505  O  O     . TRP A 1 697 ? -26.877 12.265  17.451  1.00 26.24 ? 717  TRP A O     1 
ATOM   5506  C  CB    . TRP A 1 697 ? -29.199 10.283  17.239  1.00 25.26 ? 717  TRP A CB    1 
ATOM   5507  C  CG    . TRP A 1 697 ? -30.296 9.485   17.856  1.00 25.49 ? 717  TRP A CG    1 
ATOM   5508  C  CD1   . TRP A 1 697 ? -31.105 9.870   18.873  1.00 26.15 ? 717  TRP A CD1   1 
ATOM   5509  C  CD2   . TRP A 1 697 ? -30.738 8.180   17.460  1.00 25.40 ? 717  TRP A CD2   1 
ATOM   5510  N  NE1   . TRP A 1 697 ? -32.015 8.882   19.155  1.00 25.80 ? 717  TRP A NE1   1 
ATOM   5511  C  CE2   . TRP A 1 697 ? -31.812 7.833   18.300  1.00 25.46 ? 717  TRP A CE2   1 
ATOM   5512  C  CE3   . TRP A 1 697 ? -30.325 7.269   16.478  1.00 25.79 ? 717  TRP A CE3   1 
ATOM   5513  C  CZ2   . TRP A 1 697 ? -32.488 6.610   18.195  1.00 25.94 ? 717  TRP A CZ2   1 
ATOM   5514  C  CZ3   . TRP A 1 697 ? -30.992 6.050   16.375  1.00 25.82 ? 717  TRP A CZ3   1 
ATOM   5515  C  CH2   . TRP A 1 697 ? -32.061 5.735   17.230  1.00 26.43 ? 717  TRP A CH2   1 
ATOM   5516  N  N     . PRO A 1 698 ? -26.049 10.583  16.206  1.00 27.69 ? 718  PRO A N     1 
ATOM   5517  C  CA    . PRO A 1 698 ? -25.201 11.504  15.457  1.00 29.03 ? 718  PRO A CA    1 
ATOM   5518  C  C     . PRO A 1 698 ? -25.987 12.337  14.437  1.00 30.28 ? 718  PRO A C     1 
ATOM   5519  O  O     . PRO A 1 698 ? -27.055 11.926  14.002  1.00 30.00 ? 718  PRO A O     1 
ATOM   5520  C  CB    . PRO A 1 698 ? -24.247 10.563  14.721  1.00 28.74 ? 718  PRO A CB    1 
ATOM   5521  C  CG    . PRO A 1 698 ? -25.115 9.382   14.412  1.00 28.24 ? 718  PRO A CG    1 
ATOM   5522  C  CD    . PRO A 1 698 ? -25.980 9.219   15.655  1.00 27.86 ? 718  PRO A CD    1 
ATOM   5523  N  N     . ARG A 1 699 ? -25.442 13.498  14.085  1.00 31.95 ? 719  ARG A N     1 
ATOM   5524  C  CA    A ARG A 1 699 ? -26.010 14.359  13.050  0.60 32.86 ? 719  ARG A CA    1 
ATOM   5525  C  CA    B ARG A 1 699 ? -26.005 14.355  13.038  0.40 32.73 ? 719  ARG A CA    1 
ATOM   5526  C  C     . ARG A 1 699 ? -24.876 14.827  12.139  1.00 33.53 ? 719  ARG A C     1 
ATOM   5527  O  O     . ARG A 1 699 ? -23.820 15.212  12.623  1.00 33.49 ? 719  ARG A O     1 
ATOM   5528  C  CB    A ARG A 1 699 ? -26.706 15.570  13.682  0.60 32.92 ? 719  ARG A CB    1 
ATOM   5529  C  CB    B ARG A 1 699 ? -26.709 15.570  13.643  0.40 32.71 ? 719  ARG A CB    1 
ATOM   5530  C  CG    A ARG A 1 699 ? -27.963 15.238  14.499  0.60 33.24 ? 719  ARG A CG    1 
ATOM   5531  C  CG    B ARG A 1 699 ? -28.072 15.270  14.225  0.40 32.59 ? 719  ARG A CG    1 
ATOM   5532  C  CD    A ARG A 1 699 ? -29.131 14.906  13.595  0.60 33.94 ? 719  ARG A CD    1 
ATOM   5533  C  CD    B ARG A 1 699 ? -28.301 16.063  15.488  0.40 32.51 ? 719  ARG A CD    1 
ATOM   5534  N  NE    A ARG A 1 699 ? -30.389 14.693  14.318  0.60 34.15 ? 719  ARG A NE    1 
ATOM   5535  N  NE    B ARG A 1 699 ? -28.836 17.396  15.245  0.40 32.56 ? 719  ARG A NE    1 
ATOM   5536  C  CZ    A ARG A 1 699 ? -30.955 13.510  14.564  0.60 34.28 ? 719  ARG A CZ    1 
ATOM   5537  C  CZ    B ARG A 1 699 ? -28.908 18.350  16.168  0.40 31.79 ? 719  ARG A CZ    1 
ATOM   5538  N  NH1   A ARG A 1 699 ? -30.393 12.371  14.171  0.60 34.44 ? 719  ARG A NH1   1 
ATOM   5539  N  NH1   B ARG A 1 699 ? -28.459 18.126  17.388  0.40 31.30 ? 719  ARG A NH1   1 
ATOM   5540  N  NH2   A ARG A 1 699 ? -32.106 13.464  15.222  0.60 35.22 ? 719  ARG A NH2   1 
ATOM   5541  N  NH2   B ARG A 1 699 ? -29.419 19.535  15.867  0.40 32.06 ? 719  ARG A NH2   1 
ATOM   5542  N  N     . ASP A 1 700 ? -25.097 14.792  10.829  1.00 35.04 ? 720  ASP A N     1 
ATOM   5543  C  CA    . ASP A 1 700 ? -24.052 15.196  9.875   1.00 36.52 ? 720  ASP A CA    1 
ATOM   5544  C  C     . ASP A 1 700 ? -23.708 16.664  10.014  1.00 36.91 ? 720  ASP A C     1 
ATOM   5545  O  O     . ASP A 1 700 ? -24.587 17.512  9.934   1.00 37.77 ? 720  ASP A O     1 
ATOM   5546  C  CB    . ASP A 1 700 ? -24.477 14.891  8.443   1.00 36.87 ? 720  ASP A CB    1 
ATOM   5547  C  CG    . ASP A 1 700 ? -24.403 13.420  8.122   1.00 39.04 ? 720  ASP A CG    1 
ATOM   5548  O  OD1   . ASP A 1 700 ? -23.944 12.639  8.991   1.00 42.27 ? 720  ASP A OD1   1 
ATOM   5549  O  OD2   . ASP A 1 700 ? -24.795 13.039  6.993   1.00 42.68 ? 720  ASP A OD2   1 
ATOM   5550  N  N     . ASN A 1 701 ? -22.431 16.948  10.256  1.00 37.41 ? 721  ASN A N     1 
ATOM   5551  C  CA    . ASN A 1 701 ? -21.932 18.320  10.395  1.00 37.57 ? 721  ASN A CA    1 
ATOM   5552  C  C     . ASN A 1 701 ? -22.556 19.111  11.549  1.00 37.19 ? 721  ASN A C     1 
ATOM   5553  O  O     . ASN A 1 701 ? -22.691 20.329  11.454  1.00 37.63 ? 721  ASN A O     1 
ATOM   5554  C  CB    . ASN A 1 701 ? -22.138 19.092  9.087   1.00 37.99 ? 721  ASN A CB    1 
ATOM   5555  C  CG    . ASN A 1 701 ? -21.689 18.310  7.874   1.00 39.25 ? 721  ASN A CG    1 
ATOM   5556  O  OD1   . ASN A 1 701 ? -20.504 17.996  7.733   1.00 42.33 ? 721  ASN A OD1   1 
ATOM   5557  N  ND2   . ASN A 1 701 ? -22.631 17.986  6.990   1.00 40.28 ? 721  ASN A ND2   1 
ATOM   5558  N  N     . GLY A 1 702 ? -22.927 18.432  12.632  1.00 36.32 ? 722  GLY A N     1 
ATOM   5559  C  CA    . GLY A 1 702 ? -23.491 19.105  13.809  1.00 35.59 ? 722  GLY A CA    1 
ATOM   5560  C  C     . GLY A 1 702 ? -23.238 18.347  15.109  1.00 34.85 ? 722  GLY A C     1 
ATOM   5561  O  O     . GLY A 1 702 ? -22.696 17.242  15.091  1.00 34.61 ? 722  GLY A O     1 
ATOM   5562  N  N     . PRO A 1 703 ? -23.615 18.945  16.254  1.00 33.79 ? 723  PRO A N     1 
ATOM   5563  C  CA    . PRO A 1 703 ? -23.556 18.206  17.509  1.00 33.04 ? 723  PRO A CA    1 
ATOM   5564  C  C     . PRO A 1 703 ? -24.587 17.083  17.496  1.00 31.88 ? 723  PRO A C     1 
ATOM   5565  O  O     . PRO A 1 703 ? -25.497 17.108  16.675  1.00 31.70 ? 723  PRO A O     1 
ATOM   5566  C  CB    . PRO A 1 703 ? -23.907 19.257  18.577  1.00 33.22 ? 723  PRO A CB    1 
ATOM   5567  C  CG    . PRO A 1 703 ? -23.963 20.574  17.865  1.00 33.72 ? 723  PRO A CG    1 
ATOM   5568  C  CD    . PRO A 1 703 ? -24.188 20.289  16.426  1.00 33.90 ? 723  PRO A CD    1 
ATOM   5569  N  N     . ASN A 1 704 ? -24.431 16.106  18.383  1.00 30.54 ? 724  ASN A N     1 
ATOM   5570  C  CA    . ASN A 1 704 ? -25.363 14.976  18.449  1.00 29.60 ? 724  ASN A CA    1 
ATOM   5571  C  C     . ASN A 1 704 ? -26.736 15.424  18.960  1.00 28.94 ? 724  ASN A C     1 
ATOM   5572  O  O     . ASN A 1 704 ? -26.842 16.410  19.670  1.00 28.98 ? 724  ASN A O     1 
ATOM   5573  C  CB    . ASN A 1 704 ? -24.788 13.870  19.342  1.00 28.92 ? 724  ASN A CB    1 
ATOM   5574  C  CG    . ASN A 1 704 ? -23.478 13.298  18.801  1.00 28.60 ? 724  ASN A CG    1 
ATOM   5575  O  OD1   . ASN A 1 704 ? -23.343 13.060  17.605  1.00 26.26 ? 724  ASN A OD1   1 
ATOM   5576  N  ND2   . ASN A 1 704 ? -22.512 13.074  19.687  1.00 27.38 ? 724  ASN A ND2   1 
ATOM   5577  N  N     . TYR A 1 705 ? -27.786 14.722  18.562  1.00 28.40 ? 725  TYR A N     1 
ATOM   5578  C  CA    . TYR A 1 705 ? -29.119 14.916  19.148  1.00 27.99 ? 725  TYR A CA    1 
ATOM   5579  C  C     . TYR A 1 705 ? -29.284 13.978  20.345  1.00 27.01 ? 725  TYR A C     1 
ATOM   5580  O  O     . TYR A 1 705 ? -29.298 12.763  20.181  1.00 26.39 ? 725  TYR A O     1 
ATOM   5581  C  CB    . TYR A 1 705 ? -30.209 14.628  18.116  1.00 28.30 ? 725  TYR A CB    1 
ATOM   5582  C  CG    . TYR A 1 705 ? -31.616 14.495  18.681  1.00 29.74 ? 725  TYR A CG    1 
ATOM   5583  C  CD1   . TYR A 1 705 ? -32.150 15.466  19.521  1.00 32.26 ? 725  TYR A CD1   1 
ATOM   5584  C  CD2   . TYR A 1 705 ? -32.417 13.409  18.352  1.00 31.86 ? 725  TYR A CD2   1 
ATOM   5585  C  CE1   . TYR A 1 705 ? -33.449 15.353  20.030  1.00 33.03 ? 725  TYR A CE1   1 
ATOM   5586  C  CE2   . TYR A 1 705 ? -33.714 13.287  18.855  1.00 33.29 ? 725  TYR A CE2   1 
ATOM   5587  C  CZ    . TYR A 1 705 ? -34.219 14.265  19.693  1.00 34.05 ? 725  TYR A CZ    1 
ATOM   5588  O  OH    . TYR A 1 705 ? -35.501 14.143  20.191  1.00 37.69 ? 725  TYR A OH    1 
ATOM   5589  N  N     . VAL A 1 706 ? -29.392 14.545  21.544  1.00 26.18 ? 726  VAL A N     1 
ATOM   5590  C  CA    . VAL A 1 706 ? -29.606 13.751  22.751  1.00 25.72 ? 726  VAL A CA    1 
ATOM   5591  C  C     . VAL A 1 706 ? -31.111 13.600  22.964  1.00 25.34 ? 726  VAL A C     1 
ATOM   5592  O  O     . VAL A 1 706 ? -31.775 14.532  23.410  1.00 25.57 ? 726  VAL A O     1 
ATOM   5593  C  CB    . VAL A 1 706 ? -28.970 14.409  23.982  1.00 25.79 ? 726  VAL A CB    1 
ATOM   5594  C  CG1   . VAL A 1 706 ? -29.258 13.585  25.237  1.00 25.69 ? 726  VAL A CG1   1 
ATOM   5595  C  CG2   . VAL A 1 706 ? -27.463 14.596  23.773  1.00 24.99 ? 726  VAL A CG2   1 
ATOM   5596  N  N     . GLN A 1 707 ? -31.646 12.435  22.615  1.00 24.86 ? 727  GLN A N     1 
ATOM   5597  C  CA    . GLN A 1 707 ? -33.083 12.166  22.752  1.00 24.56 ? 727  GLN A CA    1 
ATOM   5598  C  C     . GLN A 1 707 ? -33.432 11.785  24.201  1.00 24.55 ? 727  GLN A C     1 
ATOM   5599  O  O     . GLN A 1 707 ? -32.888 10.831  24.746  1.00 24.01 ? 727  GLN A O     1 
ATOM   5600  C  CB    . GLN A 1 707 ? -33.507 11.055  21.792  1.00 24.13 ? 727  GLN A CB    1 
ATOM   5601  C  CG    . GLN A 1 707 ? -35.003 10.933  21.621  1.00 23.90 ? 727  GLN A CG    1 
ATOM   5602  C  CD    . GLN A 1 707 ? -35.394 9.938   20.551  1.00 23.80 ? 727  GLN A CD    1 
ATOM   5603  O  OE1   . GLN A 1 707 ? -34.602 9.073   20.160  1.00 25.29 ? 727  GLN A OE1   1 
ATOM   5604  N  NE2   . GLN A 1 707 ? -36.627 10.038  20.082  1.00 21.22 ? 727  GLN A NE2   1 
ATOM   5605  N  N     . ARG A 1 708 ? -34.341 12.550  24.802  1.00 25.02 ? 728  ARG A N     1 
ATOM   5606  C  CA    . ARG A 1 708 ? -34.807 12.341  26.176  1.00 25.46 ? 728  ARG A CA    1 
ATOM   5607  C  C     . ARG A 1 708 ? -36.320 12.242  26.187  1.00 25.49 ? 728  ARG A C     1 
ATOM   5608  O  O     . ARG A 1 708 ? -36.972 12.713  25.263  1.00 25.26 ? 728  ARG A O     1 
ATOM   5609  C  CB    . ARG A 1 708 ? -34.422 13.528  27.057  1.00 25.71 ? 728  ARG A CB    1 
ATOM   5610  C  CG    . ARG A 1 708 ? -32.983 13.536  27.482  1.00 26.82 ? 728  ARG A CG    1 
ATOM   5611  C  CD    . ARG A 1 708 ? -32.632 14.842  28.180  1.00 27.42 ? 728  ARG A CD    1 
ATOM   5612  N  NE    . ARG A 1 708 ? -31.185 14.968  28.358  1.00 27.61 ? 728  ARG A NE    1 
ATOM   5613  C  CZ    . ARG A 1 708 ? -30.480 14.331  29.290  1.00 28.10 ? 728  ARG A CZ    1 
ATOM   5614  N  NH1   . ARG A 1 708 ? -31.075 13.508  30.151  1.00 27.98 ? 728  ARG A NH1   1 
ATOM   5615  N  NH2   . ARG A 1 708 ? -29.165 14.519  29.368  1.00 29.13 ? 728  ARG A NH2   1 
ATOM   5616  N  N     . TRP A 1 709 ? -36.869 11.625  27.231  1.00 25.45 ? 729  TRP A N     1 
ATOM   5617  C  CA    . TRP A 1 709 ? -38.307 11.692  27.491  1.00 25.72 ? 729  TRP A CA    1 
ATOM   5618  C  C     . TRP A 1 709 ? -38.608 12.290  28.875  1.00 26.32 ? 729  TRP A C     1 
ATOM   5619  O  O     . TRP A 1 709 ? -39.770 12.399  29.271  1.00 26.73 ? 729  TRP A O     1 
ATOM   5620  C  CB    . TRP A 1 709 ? -38.945 10.308  27.323  1.00 25.27 ? 729  TRP A CB    1 
ATOM   5621  C  CG    . TRP A 1 709 ? -38.889 9.839   25.917  1.00 24.36 ? 729  TRP A CG    1 
ATOM   5622  C  CD1   . TRP A 1 709 ? -39.879 9.928   24.987  1.00 24.18 ? 729  TRP A CD1   1 
ATOM   5623  C  CD2   . TRP A 1 709 ? -37.772 9.232   25.259  1.00 22.31 ? 729  TRP A CD2   1 
ATOM   5624  N  NE1   . TRP A 1 709 ? -39.456 9.406   23.798  1.00 23.99 ? 729  TRP A NE1   1 
ATOM   5625  C  CE2   . TRP A 1 709 ? -38.158 8.985   23.930  1.00 23.10 ? 729  TRP A CE2   1 
ATOM   5626  C  CE3   . TRP A 1 709 ? -36.483 8.870   25.667  1.00 21.48 ? 729  TRP A CE3   1 
ATOM   5627  C  CZ2   . TRP A 1 709 ? -37.306 8.376   23.002  1.00 22.27 ? 729  TRP A CZ2   1 
ATOM   5628  C  CZ3   . TRP A 1 709 ? -35.629 8.278   24.742  1.00 21.55 ? 729  TRP A CZ3   1 
ATOM   5629  C  CH2   . TRP A 1 709 ? -36.045 8.032   23.432  1.00 21.62 ? 729  TRP A CH2   1 
ATOM   5630  N  N     . ILE A 1 710 ? -37.557 12.647  29.605  1.00 26.99 ? 730  ILE A N     1 
ATOM   5631  C  CA    . ILE A 1 710 ? -37.655 13.406  30.842  1.00 28.04 ? 730  ILE A CA    1 
ATOM   5632  C  C     . ILE A 1 710 ? -36.528 14.441  30.777  1.00 28.70 ? 730  ILE A C     1 
ATOM   5633  O  O     . ILE A 1 710 ? -35.409 14.098  30.389  1.00 28.97 ? 730  ILE A O     1 
ATOM   5634  C  CB    . ILE A 1 710 ? -37.456 12.518  32.096  1.00 28.10 ? 730  ILE A CB    1 
ATOM   5635  C  CG1   . ILE A 1 710 ? -38.697 11.665  32.368  1.00 28.00 ? 730  ILE A CG1   1 
ATOM   5636  C  CG2   . ILE A 1 710 ? -37.175 13.377  33.323  1.00 28.65 ? 730  ILE A CG2   1 
ATOM   5637  C  CD1   . ILE A 1 710 ? -38.503 10.654  33.493  1.00 29.60 ? 730  ILE A CD1   1 
ATOM   5638  N  N     . PRO A 1 711 ? -36.808 15.702  31.144  1.00 29.45 ? 731  PRO A N     1 
ATOM   5639  C  CA    . PRO A 1 711 ? -35.738 16.696  31.031  1.00 29.93 ? 731  PRO A CA    1 
ATOM   5640  C  C     . PRO A 1 711 ? -34.545 16.367  31.921  1.00 30.19 ? 731  PRO A C     1 
ATOM   5641  O  O     . PRO A 1 711 ? -34.699 15.721  32.959  1.00 29.62 ? 731  PRO A O     1 
ATOM   5642  C  CB    . PRO A 1 711 ? -36.408 18.007  31.473  1.00 29.77 ? 731  PRO A CB    1 
ATOM   5643  C  CG    . PRO A 1 711 ? -37.664 17.603  32.162  1.00 29.97 ? 731  PRO A CG    1 
ATOM   5644  C  CD    . PRO A 1 711 ? -38.081 16.305  31.571  1.00 29.53 ? 731  PRO A CD    1 
ATOM   5645  N  N     . GLU A 1 712 ? -33.367 16.795  31.491  1.00 31.14 ? 732  GLU A N     1 
ATOM   5646  C  CA    . GLU A 1 712 ? -32.159 16.638  32.285  1.00 32.10 ? 732  GLU A CA    1 
ATOM   5647  C  C     . GLU A 1 712 ? -32.336 17.334  33.629  1.00 33.61 ? 732  GLU A C     1 
ATOM   5648  O  O     . GLU A 1 712 ? -32.843 18.451  33.695  1.00 33.63 ? 732  GLU A O     1 
ATOM   5649  C  CB    . GLU A 1 712 ? -30.954 17.224  31.545  1.00 31.75 ? 732  GLU A CB    1 
ATOM   5650  C  CG    . GLU A 1 712 ? -29.625 16.988  32.253  1.00 30.93 ? 732  GLU A CG    1 
ATOM   5651  C  CD    . GLU A 1 712 ? -28.431 17.557  31.507  1.00 29.39 ? 732  GLU A CD    1 
ATOM   5652  O  OE1   . GLU A 1 712 ? -28.609 18.133  30.417  1.00 28.83 ? 732  GLU A OE1   1 
ATOM   5653  O  OE2   . GLU A 1 712 ? -27.300 17.413  32.008  1.00 28.82 ? 732  GLU A OE2   1 
ATOM   5654  N  N     . ASP A 1 713 ? -31.928 16.663  34.701  1.00 35.55 ? 733  ASP A N     1 
ATOM   5655  C  CA    . ASP A 1 713 ? -32.019 17.237  36.041  1.00 37.02 ? 733  ASP A CA    1 
ATOM   5656  C  C     . ASP A 1 713 ? -30.659 17.632  36.586  1.00 37.62 ? 733  ASP A C     1 
ATOM   5657  O  O     . ASP A 1 713 ? -29.735 16.829  36.597  1.00 38.07 ? 733  ASP A O     1 
ATOM   5658  C  CB    . ASP A 1 713 ? -32.633 16.238  37.013  1.00 37.22 ? 733  ASP A CB    1 
ATOM   5659  C  CG    . ASP A 1 713 ? -32.349 16.597  38.470  1.00 38.46 ? 733  ASP A CG    1 
ATOM   5660  O  OD1   . ASP A 1 713 ? -32.759 17.712  38.870  1.00 38.25 ? 733  ASP A OD1   1 
ATOM   5661  O  OD2   . ASP A 1 713 ? -31.718 15.777  39.199  1.00 37.77 ? 733  ASP A OD2   1 
ATOM   5662  N  N     . ARG A 1 714 ? -30.541 18.864  37.060  1.00 38.52 ? 734  ARG A N     1 
ATOM   5663  C  CA    . ARG A 1 714 ? -29.387 19.235  37.886  1.00 39.30 ? 734  ARG A CA    1 
ATOM   5664  C  C     . ARG A 1 714 ? -29.811 19.943  39.183  1.00 39.27 ? 734  ARG A C     1 
ATOM   5665  O  O     . ARG A 1 714 ? -28.958 20.488  39.902  1.00 39.74 ? 734  ARG A O     1 
ATOM   5666  C  CB    . ARG A 1 714 ? -28.403 20.084  37.075  1.00 39.54 ? 734  ARG A CB    1 
ATOM   5667  C  CG    . ARG A 1 714 ? -27.973 19.424  35.757  1.00 41.03 ? 734  ARG A CG    1 
ATOM   5668  C  CD    . ARG A 1 714 ? -27.342 20.427  34.823  1.00 42.99 ? 734  ARG A CD    1 
ATOM   5669  N  NE    . ARG A 1 714 ? -26.025 20.820  35.314  1.00 44.27 ? 734  ARG A NE    1 
ATOM   5670  C  CZ    . ARG A 1 714 ? -25.452 21.999  35.096  1.00 45.78 ? 734  ARG A CZ    1 
ATOM   5671  N  NH1   . ARG A 1 714 ? -26.071 22.946  34.390  1.00 46.75 ? 734  ARG A NH1   1 
ATOM   5672  N  NH2   . ARG A 1 714 ? -24.244 22.236  35.595  1.00 46.55 ? 734  ARG A NH2   1 
ATOM   5673  N  N     . ASP A 1 715 ? -31.109 19.892  39.501  1.00 38.72 ? 735  ASP A N     1 
ATOM   5674  C  CA    . ASP A 1 715 ? -31.651 20.549  40.694  1.00 38.40 ? 735  ASP A CA    1 
ATOM   5675  C  C     . ASP A 1 715 ? -30.950 20.132  41.969  1.00 37.83 ? 735  ASP A C     1 
ATOM   5676  O  O     . ASP A 1 715 ? -30.323 19.079  42.039  1.00 37.86 ? 735  ASP A O     1 
ATOM   5677  C  CB    . ASP A 1 715 ? -33.143 20.248  40.860  1.00 38.48 ? 735  ASP A CB    1 
ATOM   5678  C  CG    . ASP A 1 715 ? -34.003 21.000  39.882  1.00 39.13 ? 735  ASP A CG    1 
ATOM   5679  O  OD1   . ASP A 1 715 ? -33.456 21.528  38.893  1.00 40.52 ? 735  ASP A OD1   1 
ATOM   5680  O  OD2   . ASP A 1 715 ? -35.231 21.072  40.112  1.00 40.53 ? 735  ASP A OD2   1 
ATOM   5681  N  N     . CYS A 1 716 ? -31.094 20.969  42.986  1.00 37.47 ? 736  CYS A N     1 
ATOM   5682  C  CA    . CYS A 1 716 ? -30.512 20.723  44.288  1.00 37.20 ? 736  CYS A CA    1 
ATOM   5683  C  C     . CYS A 1 716 ? -31.545 20.840  45.397  1.00 36.61 ? 736  CYS A C     1 
ATOM   5684  O  O     . CYS A 1 716 ? -32.540 21.555  45.285  1.00 36.50 ? 736  CYS A O     1 
ATOM   5685  C  CB    . CYS A 1 716 ? -29.346 21.686  44.538  1.00 37.34 ? 736  CYS A CB    1 
ATOM   5686  S  SG    . CYS A 1 716 ? -27.730 20.935  44.208  1.00 38.62 ? 736  CYS A SG    1 
ATOM   5687  N  N     . SER A 1 717 ? -31.301 20.095  46.461  1.00 36.29 ? 737  SER A N     1 
ATOM   5688  C  CA    . SER A 1 717 ? -32.118 20.154  47.660  1.00 35.89 ? 737  SER A CA    1 
ATOM   5689  C  C     . SER A 1 717 ? -31.219 19.754  48.803  1.00 35.90 ? 737  SER A C     1 
ATOM   5690  O  O     . SER A 1 717 ? -30.091 19.329  48.577  1.00 35.11 ? 737  SER A O     1 
ATOM   5691  C  CB    . SER A 1 717 ? -33.306 19.197  47.559  1.00 36.00 ? 737  SER A CB    1 
ATOM   5692  O  OG    . SER A 1 717 ? -32.870 17.873  47.295  1.00 34.43 ? 737  SER A OG    1 
ATOM   5693  N  N     . MET A 1 718 ? -31.720 19.895  50.022  1.00 36.11 ? 738  MET A N     1 
ATOM   5694  C  CA    . MET A 1 718 ? -30.972 19.514  51.208  1.00 36.68 ? 738  MET A CA    1 
ATOM   5695  C  C     . MET A 1 718 ? -31.838 18.648  52.094  1.00 36.06 ? 738  MET A C     1 
ATOM   5696  O  O     . MET A 1 718 ? -33.048 18.894  52.216  1.00 35.89 ? 738  MET A O     1 
ATOM   5697  C  CB    . MET A 1 718 ? -30.556 20.733  52.012  1.00 37.29 ? 738  MET A CB    1 
ATOM   5698  C  CG    . MET A 1 718 ? -29.721 21.736  51.257  1.00 39.92 ? 738  MET A CG    1 
ATOM   5699  S  SD    . MET A 1 718 ? -29.242 23.078  52.369  1.00 46.90 ? 738  MET A SD    1 
ATOM   5700  C  CE    . MET A 1 718 ? -30.857 23.615  52.972  1.00 44.74 ? 738  MET A CE    1 
ATOM   5701  N  N     . PRO A 1 719 ? -31.220 17.643  52.730  1.00 35.26 ? 739  PRO A N     1 
ATOM   5702  C  CA    . PRO A 1 719 ? -31.920 16.810  53.687  1.00 34.87 ? 739  PRO A CA    1 
ATOM   5703  C  C     . PRO A 1 719 ? -32.049 17.514  55.027  1.00 34.38 ? 739  PRO A C     1 
ATOM   5704  O  O     . PRO A 1 719 ? -31.270 18.433  55.319  1.00 33.88 ? 739  PRO A O     1 
ATOM   5705  C  CB    . PRO A 1 719 ? -30.982 15.616  53.835  1.00 35.18 ? 739  PRO A CB    1 
ATOM   5706  C  CG    . PRO A 1 719 ? -29.630 16.214  53.683  1.00 34.81 ? 739  PRO A CG    1 
ATOM   5707  C  CD    . PRO A 1 719 ? -29.797 17.266  52.622  1.00 35.21 ? 739  PRO A CD    1 
ATOM   5708  N  N     . PRO A 1 720 ? -32.998 17.063  55.866  1.00 33.93 ? 740  PRO A N     1 
ATOM   5709  C  CA    . PRO A 1 720 ? -33.066 17.675  57.191  1.00 33.60 ? 740  PRO A CA    1 
ATOM   5710  C  C     . PRO A 1 720 ? -31.801 17.356  57.969  1.00 32.95 ? 740  PRO A C     1 
ATOM   5711  O  O     . PRO A 1 720 ? -31.127 16.379  57.649  1.00 32.54 ? 740  PRO A O     1 
ATOM   5712  C  CB    . PRO A 1 720 ? -34.281 17.009  57.850  1.00 33.84 ? 740  PRO A CB    1 
ATOM   5713  C  CG    . PRO A 1 720 ? -34.854 16.059  56.833  1.00 33.99 ? 740  PRO A CG    1 
ATOM   5714  C  CD    . PRO A 1 720 ? -33.879 15.893  55.729  1.00 33.85 ? 740  PRO A CD    1 
ATOM   5715  N  N     . PRO A 1 721 ? -31.465 18.185  58.972  1.00 32.25 ? 741  PRO A N     1 
ATOM   5716  C  CA    . PRO A 1 721 ? -30.334 17.856  59.818  1.00 31.62 ? 741  PRO A CA    1 
ATOM   5717  C  C     . PRO A 1 721 ? -30.511 16.475  60.436  1.00 30.94 ? 741  PRO A C     1 
ATOM   5718  O  O     . PRO A 1 721 ? -31.642 16.036  60.681  1.00 30.71 ? 741  PRO A O     1 
ATOM   5719  C  CB    . PRO A 1 721 ? -30.372 18.940  60.912  1.00 31.87 ? 741  PRO A CB    1 
ATOM   5720  C  CG    . PRO A 1 721 ? -31.106 20.065  60.312  1.00 32.34 ? 741  PRO A CG    1 
ATOM   5721  C  CD    . PRO A 1 721 ? -32.079 19.476  59.337  1.00 32.29 ? 741  PRO A CD    1 
ATOM   5722  N  N     . PHE A 1 722 ? -29.393 15.804  60.668  1.00 30.02 ? 742  PHE A N     1 
ATOM   5723  C  CA    . PHE A 1 722 ? -29.384 14.517  61.323  1.00 29.55 ? 742  PHE A CA    1 
ATOM   5724  C  C     . PHE A 1 722 ? -29.959 14.630  62.725  1.00 29.49 ? 742  PHE A C     1 
ATOM   5725  O  O     . PHE A 1 722 ? -29.612 15.550  63.462  1.00 29.97 ? 742  PHE A O     1 
ATOM   5726  C  CB    . PHE A 1 722 ? -27.954 13.999  61.414  1.00 29.42 ? 742  PHE A CB    1 
ATOM   5727  C  CG    . PHE A 1 722 ? -27.833 12.693  62.139  1.00 28.76 ? 742  PHE A CG    1 
ATOM   5728  C  CD1   . PHE A 1 722 ? -27.900 11.496  61.447  1.00 27.93 ? 742  PHE A CD1   1 
ATOM   5729  C  CD2   . PHE A 1 722 ? -27.661 12.660  63.511  1.00 28.66 ? 742  PHE A CD2   1 
ATOM   5730  C  CE1   . PHE A 1 722 ? -27.790 10.280  62.106  1.00 27.73 ? 742  PHE A CE1   1 
ATOM   5731  C  CE2   . PHE A 1 722 ? -27.556 11.456  64.181  1.00 29.14 ? 742  PHE A CE2   1 
ATOM   5732  C  CZ    . PHE A 1 722 ? -27.621 10.261  63.482  1.00 28.66 ? 742  PHE A CZ    1 
ATOM   5733  N  N     . SER A 1 723 ? -30.843 13.702  63.079  1.00 28.88 ? 743  SER A N     1 
ATOM   5734  C  CA    . SER A 1 723 ? -31.241 13.498  64.467  1.00 28.71 ? 743  SER A CA    1 
ATOM   5735  C  C     . SER A 1 723 ? -31.282 12.001  64.763  1.00 28.35 ? 743  SER A C     1 
ATOM   5736  O  O     . SER A 1 723 ? -31.334 11.168  63.851  1.00 28.36 ? 743  SER A O     1 
ATOM   5737  C  CB    . SER A 1 723 ? -32.600 14.151  64.776  1.00 28.84 ? 743  SER A CB    1 
ATOM   5738  O  OG    . SER A 1 723 ? -33.641 13.599  63.985  1.00 29.65 ? 743  SER A OG    1 
ATOM   5739  N  N     . TYR A 1 724 ? -31.226 11.669  66.046  1.00 27.79 ? 744  TYR A N     1 
ATOM   5740  C  CA    . TYR A 1 724 ? -31.337 10.288  66.500  1.00 27.29 ? 744  TYR A CA    1 
ATOM   5741  C  C     . TYR A 1 724 ? -31.849 10.258  67.936  1.00 26.98 ? 744  TYR A C     1 
ATOM   5742  O  O     . TYR A 1 724 ? -31.330 10.969  68.788  1.00 26.59 ? 744  TYR A O     1 
ATOM   5743  C  CB    . TYR A 1 724 ? -29.983 9.593   66.426  1.00 26.86 ? 744  TYR A CB    1 
ATOM   5744  C  CG    . TYR A 1 724 ? -30.111 8.102   66.475  1.00 26.88 ? 744  TYR A CG    1 
ATOM   5745  C  CD1   . TYR A 1 724 ? -30.411 7.381   65.322  1.00 27.12 ? 744  TYR A CD1   1 
ATOM   5746  C  CD2   . TYR A 1 724 ? -29.963 7.406   67.668  1.00 25.42 ? 744  TYR A CD2   1 
ATOM   5747  C  CE1   . TYR A 1 724 ? -30.541 6.007   65.350  1.00 26.58 ? 744  TYR A CE1   1 
ATOM   5748  C  CE2   . TYR A 1 724 ? -30.088 6.030   67.706  1.00 25.04 ? 744  TYR A CE2   1 
ATOM   5749  C  CZ    . TYR A 1 724 ? -30.380 5.338   66.543  1.00 25.70 ? 744  TYR A CZ    1 
ATOM   5750  O  OH    . TYR A 1 724 ? -30.517 3.981   66.560  1.00 24.98 ? 744  TYR A OH    1 
ATOM   5751  N  N     . ASN A 1 725 ? -32.855 9.428   68.197  1.00 26.46 ? 745  ASN A N     1 
ATOM   5752  C  CA    . ASN A 1 725 ? -33.510 9.395   69.494  1.00 26.13 ? 745  ASN A CA    1 
ATOM   5753  C  C     . ASN A 1 725 ? -32.986 8.328   70.451  1.00 25.87 ? 745  ASN A C     1 
ATOM   5754  O  O     . ASN A 1 725 ? -32.578 8.641   71.571  1.00 25.88 ? 745  ASN A O     1 
ATOM   5755  C  CB    . ASN A 1 725 ? -35.011 9.218   69.319  1.00 26.45 ? 745  ASN A CB    1 
ATOM   5756  C  CG    . ASN A 1 725 ? -35.758 9.469   70.594  1.00 27.07 ? 745  ASN A CG    1 
ATOM   5757  O  OD1   . ASN A 1 725 ? -35.911 8.586   71.425  1.00 27.86 ? 745  ASN A OD1   1 
ATOM   5758  N  ND2   . ASN A 1 725 ? -36.211 10.694  70.765  1.00 30.88 ? 745  ASN A ND2   1 
ATOM   5759  N  N     . GLY A 1 726 ? -33.028 7.069   70.027  1.00 25.43 ? 746  GLY A N     1 
ATOM   5760  C  CA    . GLY A 1 726 ? -32.494 5.959   70.817  1.00 24.72 ? 746  GLY A CA    1 
ATOM   5761  C  C     . GLY A 1 726 ? -33.436 5.355   71.848  1.00 24.43 ? 746  GLY A C     1 
ATOM   5762  O  O     . GLY A 1 726 ? -33.103 4.338   72.464  1.00 24.16 ? 746  GLY A O     1 
ATOM   5763  N  N     . THR A 1 727 ? -34.596 5.971   72.057  1.00 24.12 ? 747  THR A N     1 
ATOM   5764  C  CA    . THR A 1 727 ? -35.595 5.430   72.978  1.00 23.74 ? 747  THR A CA    1 
ATOM   5765  C  C     . THR A 1 727 ? -36.792 4.880   72.223  1.00 23.71 ? 747  THR A C     1 
ATOM   5766  O  O     . THR A 1 727 ? -37.074 5.268   71.085  1.00 23.62 ? 747  THR A O     1 
ATOM   5767  C  CB    . THR A 1 727 ? -36.084 6.465   74.023  1.00 23.68 ? 747  THR A CB    1 
ATOM   5768  O  OG1   . THR A 1 727 ? -37.006 7.373   73.425  1.00 22.89 ? 747  THR A OG1   1 
ATOM   5769  C  CG2   . THR A 1 727 ? -34.910 7.236   74.629  1.00 23.60 ? 747  THR A CG2   1 
ATOM   5770  N  N     . TYR A 1 728 ? -37.471 3.946   72.875  1.00 24.03 ? 748  TYR A N     1 
ATOM   5771  C  CA    . TYR A 1 728 ? -38.617 3.256   72.318  1.00 24.27 ? 748  TYR A CA    1 
ATOM   5772  C  C     . TYR A 1 728 ? -39.557 3.008   73.488  1.00 24.76 ? 748  TYR A C     1 
ATOM   5773  O  O     . TYR A 1 728 ? -39.215 2.277   74.421  1.00 24.44 ? 748  TYR A O     1 
ATOM   5774  C  CB    . TYR A 1 728 ? -38.200 1.942   71.613  1.00 24.05 ? 748  TYR A CB    1 
ATOM   5775  C  CG    . TYR A 1 728 ? -37.146 1.139   72.355  1.00 24.06 ? 748  TYR A CG    1 
ATOM   5776  C  CD1   . TYR A 1 728 ? -37.485 -0.002  73.085  1.00 23.89 ? 748  TYR A CD1   1 
ATOM   5777  C  CD2   . TYR A 1 728 ? -35.808 1.539   72.352  1.00 24.24 ? 748  TYR A CD2   1 
ATOM   5778  C  CE1   . TYR A 1 728 ? -36.510 -0.727  73.778  1.00 24.00 ? 748  TYR A CE1   1 
ATOM   5779  C  CE2   . TYR A 1 728 ? -34.842 0.829   73.045  1.00 22.46 ? 748  TYR A CE2   1 
ATOM   5780  C  CZ    . TYR A 1 728 ? -35.195 -0.291  73.757  1.00 23.83 ? 748  TYR A CZ    1 
ATOM   5781  O  OH    . TYR A 1 728 ? -34.221 -0.986  74.441  1.00 25.40 ? 748  TYR A OH    1 
ATOM   5782  N  N     . ARG A 1 729 ? -40.714 3.664   73.461  1.00 25.32 ? 749  ARG A N     1 
ATOM   5783  C  CA    . ARG A 1 729 ? -41.596 3.706   74.624  1.00 26.23 ? 749  ARG A CA    1 
ATOM   5784  C  C     . ARG A 1 729 ? -43.056 3.708   74.202  1.00 26.07 ? 749  ARG A C     1 
ATOM   5785  O  O     . ARG A 1 729 ? -43.370 4.060   73.075  1.00 25.44 ? 749  ARG A O     1 
ATOM   5786  C  CB    . ARG A 1 729 ? -41.336 4.982   75.450  1.00 26.76 ? 749  ARG A CB    1 
ATOM   5787  C  CG    . ARG A 1 729 ? -39.884 5.289   75.780  1.00 28.47 ? 749  ARG A CG    1 
ATOM   5788  C  CD    . ARG A 1 729 ? -39.398 4.478   76.948  1.00 31.29 ? 749  ARG A CD    1 
ATOM   5789  N  NE    . ARG A 1 729 ? -37.943 4.516   77.099  1.00 33.10 ? 749  ARG A NE    1 
ATOM   5790  C  CZ    . ARG A 1 729 ? -37.244 5.565   77.534  1.00 35.43 ? 749  ARG A CZ    1 
ATOM   5791  N  NH1   . ARG A 1 729 ? -37.843 6.716   77.840  1.00 36.69 ? 749  ARG A NH1   1 
ATOM   5792  N  NH2   . ARG A 1 729 ? -35.920 5.469   77.648  1.00 36.10 ? 749  ARG A NH2   1 
ATOM   5793  N  N     . PRO A 1 730 ? -43.965 3.373   75.127  1.00 27.04 ? 750  PRO A N     1 
ATOM   5794  C  CA    . PRO A 1 730 ? -45.401 3.505   74.829  1.00 27.58 ? 750  PRO A CA    1 
ATOM   5795  C  C     . PRO A 1 730 ? -45.835 4.935   74.512  1.00 28.22 ? 750  PRO A C     1 
ATOM   5796  O  O     . PRO A 1 730 ? -45.216 5.887   74.955  1.00 28.24 ? 750  PRO A O     1 
ATOM   5797  C  CB    . PRO A 1 730 ? -46.081 3.023   76.120  1.00 27.58 ? 750  PRO A CB    1 
ATOM   5798  C  CG    . PRO A 1 730 ? -45.046 2.216   76.833  1.00 27.35 ? 750  PRO A CG    1 
ATOM   5799  C  CD    . PRO A 1 730 ? -43.731 2.841   76.481  1.00 26.94 ? 750  PRO A CD    1 
ATOM   5800  N  N     . VAL A 1 731 ? -46.893 5.074   73.729  1.00 29.25 ? 751  VAL A N     1 
ATOM   5801  C  CA    . VAL A 1 731 ? -47.473 6.375   73.448  1.00 29.79 ? 751  VAL A CA    1 
ATOM   5802  C  C     . VAL A 1 731 ? -48.959 6.294   73.752  1.00 30.43 ? 751  VAL A C     1 
ATOM   5803  O  O     . VAL A 1 731 ? -49.643 5.312   73.433  1.00 30.36 ? 751  VAL A O     1 
ATOM   5804  C  CB    . VAL A 1 731 ? -47.238 6.798   71.988  1.00 30.24 ? 751  VAL A CB    1 
ATOM   5805  C  CG1   . VAL A 1 731 ? -48.167 7.947   71.591  1.00 29.96 ? 751  VAL A CG1   1 
ATOM   5806  C  CG2   . VAL A 1 731 ? -45.761 7.181   71.779  1.00 29.81 ? 751  VAL A CG2   1 
ATOM   5807  O  OXT   . VAL A 1 731 ? -49.493 7.219   74.357  1.00 31.42 ? 751  VAL A OXT   1 
ATOM   5808  N  N     . ARG B 1 8   ? 5.631   9.670   39.989  1.00 45.11 ? 28   ARG B N     1 
ATOM   5809  C  CA    . ARG B 1 8   ? 5.020   8.384   40.420  1.00 44.83 ? 28   ARG B CA    1 
ATOM   5810  C  C     . ARG B 1 8   ? 5.801   7.204   39.845  1.00 44.60 ? 28   ARG B C     1 
ATOM   5811  O  O     . ARG B 1 8   ? 6.152   7.201   38.659  1.00 45.12 ? 28   ARG B O     1 
ATOM   5812  C  CB    . ARG B 1 8   ? 3.552   8.309   39.972  1.00 44.83 ? 28   ARG B CB    1 
ATOM   5813  N  N     . LYS B 1 9   ? 6.067   6.212   40.693  1.00 43.84 ? 29   LYS B N     1 
ATOM   5814  C  CA    . LYS B 1 9   ? 6.653   4.942   40.262  1.00 43.18 ? 29   LYS B CA    1 
ATOM   5815  C  C     . LYS B 1 9   ? 5.659   4.081   39.470  1.00 42.23 ? 29   LYS B C     1 
ATOM   5816  O  O     . LYS B 1 9   ? 6.069   3.268   38.638  1.00 42.19 ? 29   LYS B O     1 
ATOM   5817  C  CB    . LYS B 1 9   ? 7.167   4.158   41.472  1.00 43.44 ? 29   LYS B CB    1 
ATOM   5818  C  CG    . LYS B 1 9   ? 8.331   4.842   42.203  1.00 44.36 ? 29   LYS B CG    1 
ATOM   5819  C  CD    . LYS B 1 9   ? 8.902   3.949   43.304  1.00 45.01 ? 29   LYS B CD    1 
ATOM   5820  C  CE    . LYS B 1 9   ? 10.308  4.378   43.713  1.00 45.21 ? 29   LYS B CE    1 
ATOM   5821  N  NZ    . LYS B 1 9   ? 11.081  3.224   44.258  1.00 45.75 ? 29   LYS B NZ    1 
ATOM   5822  N  N     . ALA B 1 10  ? 4.360   4.280   39.727  1.00 40.80 ? 30   ALA B N     1 
ATOM   5823  C  CA    . ALA B 1 10  ? 3.272   3.604   38.996  1.00 39.50 ? 30   ALA B CA    1 
ATOM   5824  C  C     . ALA B 1 10  ? 3.327   3.783   37.466  1.00 38.24 ? 30   ALA B C     1 
ATOM   5825  O  O     . ALA B 1 10  ? 2.692   3.025   36.725  1.00 38.28 ? 30   ALA B O     1 
ATOM   5826  C  CB    . ALA B 1 10  ? 1.916   4.080   39.525  1.00 39.32 ? 30   ALA B CB    1 
ATOM   5827  N  N     . GLY B 1 11  ? 4.058   4.798   37.009  1.00 36.51 ? 31   GLY B N     1 
ATOM   5828  C  CA    . GLY B 1 11  ? 4.364   4.986   35.591  1.00 35.25 ? 31   GLY B CA    1 
ATOM   5829  C  C     . GLY B 1 11  ? 4.957   3.769   34.897  1.00 34.01 ? 31   GLY B C     1 
ATOM   5830  O  O     . GLY B 1 11  ? 4.742   3.582   33.706  1.00 33.45 ? 31   GLY B O     1 
ATOM   5831  N  N     . VAL B 1 12  ? 5.694   2.936   35.634  1.00 32.74 ? 32   VAL B N     1 
ATOM   5832  C  CA    . VAL B 1 12  ? 6.195   1.665   35.089  1.00 31.87 ? 32   VAL B CA    1 
ATOM   5833  C  C     . VAL B 1 12  ? 5.054   0.779   34.544  1.00 31.33 ? 32   VAL B C     1 
ATOM   5834  O  O     . VAL B 1 12  ? 5.253   0.017   33.591  1.00 30.69 ? 32   VAL B O     1 
ATOM   5835  C  CB    . VAL B 1 12  ? 7.041   0.873   36.126  1.00 31.68 ? 32   VAL B CB    1 
ATOM   5836  C  CG1   . VAL B 1 12  ? 6.184   0.426   37.304  1.00 31.68 ? 32   VAL B CG1   1 
ATOM   5837  C  CG2   . VAL B 1 12  ? 7.703   -0.334  35.471  1.00 30.94 ? 32   VAL B CG2   1 
ATOM   5838  N  N     . PHE B 1 13  ? 3.870   0.900   35.150  1.00 30.81 ? 33   PHE B N     1 
ATOM   5839  C  CA    . PHE B 1 13  ? 2.679   0.154   34.744  1.00 30.56 ? 33   PHE B CA    1 
ATOM   5840  C  C     . PHE B 1 13  ? 1.784   0.901   33.723  1.00 30.65 ? 33   PHE B C     1 
ATOM   5841  O  O     . PHE B 1 13  ? 0.744   0.378   33.320  1.00 30.73 ? 33   PHE B O     1 
ATOM   5842  C  CB    . PHE B 1 13  ? 1.812   -0.175  35.984  1.00 30.38 ? 33   PHE B CB    1 
ATOM   5843  C  CG    . PHE B 1 13  ? 2.523   -0.977  37.041  1.00 29.03 ? 33   PHE B CG    1 
ATOM   5844  C  CD1   . PHE B 1 13  ? 2.935   -2.276  36.787  1.00 28.84 ? 33   PHE B CD1   1 
ATOM   5845  C  CD2   . PHE B 1 13  ? 2.750   -0.446  38.299  1.00 28.35 ? 33   PHE B CD2   1 
ATOM   5846  C  CE1   . PHE B 1 13  ? 3.575   -3.019  37.762  1.00 27.21 ? 33   PHE B CE1   1 
ATOM   5847  C  CE2   . PHE B 1 13  ? 3.396   -1.190  39.277  1.00 27.56 ? 33   PHE B CE2   1 
ATOM   5848  C  CZ    . PHE B 1 13  ? 3.805   -2.474  39.005  1.00 26.84 ? 33   PHE B CZ    1 
ATOM   5849  N  N     . SER B 1 14  ? 2.158   2.109   33.318  1.00 30.48 ? 34   SER B N     1 
ATOM   5850  C  CA    . SER B 1 14  ? 1.249   2.940   32.526  1.00 30.65 ? 34   SER B CA    1 
ATOM   5851  C  C     . SER B 1 14  ? 1.232   2.555   31.045  1.00 30.44 ? 34   SER B C     1 
ATOM   5852  O  O     . SER B 1 14  ? 2.239   2.108   30.482  1.00 30.30 ? 34   SER B O     1 
ATOM   5853  C  CB    . SER B 1 14  ? 1.599   4.417   32.678  1.00 30.70 ? 34   SER B CB    1 
ATOM   5854  O  OG    . SER B 1 14  ? 2.923   4.672   32.244  1.00 32.39 ? 34   SER B OG    1 
ATOM   5855  N  N     . ASP B 1 15  ? 0.069   2.731   30.424  1.00 30.15 ? 35   ASP B N     1 
ATOM   5856  C  CA    . ASP B 1 15  ? -0.097  2.473   29.004  1.00 29.81 ? 35   ASP B CA    1 
ATOM   5857  C  C     . ASP B 1 15  ? 0.677   3.519   28.210  1.00 29.41 ? 35   ASP B C     1 
ATOM   5858  O  O     . ASP B 1 15  ? 1.060   4.557   28.738  1.00 29.20 ? 35   ASP B O     1 
ATOM   5859  C  CB    . ASP B 1 15  ? -1.576  2.521   28.605  1.00 30.03 ? 35   ASP B CB    1 
ATOM   5860  C  CG    . ASP B 1 15  ? -2.382  1.397   29.207  1.00 30.84 ? 35   ASP B CG    1 
ATOM   5861  O  OD1   . ASP B 1 15  ? -2.040  0.209   28.972  1.00 34.25 ? 35   ASP B OD1   1 
ATOM   5862  O  OD2   . ASP B 1 15  ? -3.369  1.695   29.910  1.00 29.89 ? 35   ASP B OD2   1 
ATOM   5863  N  N     . LEU B 1 16  ? 0.906   3.237   26.934  1.00 29.20 ? 36   LEU B N     1 
ATOM   5864  C  CA    . LEU B 1 16  ? 1.632   4.161   26.080  1.00 28.93 ? 36   LEU B CA    1 
ATOM   5865  C  C     . LEU B 1 16  ? 0.784   5.388   25.819  1.00 28.71 ? 36   LEU B C     1 
ATOM   5866  O  O     . LEU B 1 16  ? -0.426  5.284   25.590  1.00 29.03 ? 36   LEU B O     1 
ATOM   5867  C  CB    . LEU B 1 16  ? 2.004   3.504   24.749  1.00 28.89 ? 36   LEU B CB    1 
ATOM   5868  C  CG    . LEU B 1 16  ? 2.863   2.241   24.818  1.00 28.85 ? 36   LEU B CG    1 
ATOM   5869  C  CD1   . LEU B 1 16  ? 3.201   1.769   23.402  1.00 27.98 ? 36   LEU B CD1   1 
ATOM   5870  C  CD2   . LEU B 1 16  ? 4.133   2.467   25.652  1.00 28.29 ? 36   LEU B CD2   1 
ATOM   5871  N  N     . SER B 1 17  ? 1.418   6.554   25.870  1.00 28.27 ? 37   SER B N     1 
ATOM   5872  C  CA    . SER B 1 17  ? 0.766   7.795   25.476  1.00 28.06 ? 37   SER B CA    1 
ATOM   5873  C  C     . SER B 1 17  ? 0.619   7.855   23.953  1.00 27.54 ? 37   SER B C     1 
ATOM   5874  O  O     . SER B 1 17  ? 1.131   6.998   23.228  1.00 27.01 ? 37   SER B O     1 
ATOM   5875  C  CB    . SER B 1 17  ? 1.571   8.999   25.965  1.00 28.19 ? 37   SER B CB    1 
ATOM   5876  O  OG    . SER B 1 17  ? 2.826   9.046   25.320  1.00 28.30 ? 37   SER B OG    1 
ATOM   5877  N  N     . ASN B 1 18  ? -0.113  8.859   23.490  1.00 27.16 ? 38   ASN B N     1 
ATOM   5878  C  CA    . ASN B 1 18  ? -0.213  9.168   22.072  1.00 27.19 ? 38   ASN B CA    1 
ATOM   5879  C  C     . ASN B 1 18  ? 1.187   9.354   21.486  1.00 27.19 ? 38   ASN B C     1 
ATOM   5880  O  O     . ASN B 1 18  ? 1.511   8.796   20.439  1.00 27.08 ? 38   ASN B O     1 
ATOM   5881  C  CB    . ASN B 1 18  ? -1.033  10.448  21.895  1.00 27.25 ? 38   ASN B CB    1 
ATOM   5882  C  CG    . ASN B 1 18  ? -1.541  10.652  20.477  1.00 26.73 ? 38   ASN B CG    1 
ATOM   5883  O  OD1   . ASN B 1 18  ? -1.645  9.720   19.687  1.00 25.66 ? 38   ASN B OD1   1 
ATOM   5884  N  ND2   . ASN B 1 18  ? -1.896  11.892  20.166  1.00 26.74 ? 38   ASN B ND2   1 
ATOM   5885  N  N     . GLN B 1 19  ? 2.014   10.115  22.194  1.00 27.42 ? 39   GLN B N     1 
ATOM   5886  C  CA    . GLN B 1 19  ? 3.385   10.393  21.776  1.00 27.54 ? 39   GLN B CA    1 
ATOM   5887  C  C     . GLN B 1 19  ? 4.185   9.111   21.618  1.00 27.80 ? 39   GLN B C     1 
ATOM   5888  O  O     . GLN B 1 19  ? 4.848   8.907   20.606  1.00 27.85 ? 39   GLN B O     1 
ATOM   5889  C  CB    . GLN B 1 19  ? 4.073   11.318  22.787  1.00 27.55 ? 39   GLN B CB    1 
ATOM   5890  N  N     . GLU B 1 20  ? 4.109   8.239   22.617  1.00 27.93 ? 40   GLU B N     1 
ATOM   5891  C  CA    . GLU B 1 20  ? 4.813   6.970   22.568  1.00 28.00 ? 40   GLU B CA    1 
ATOM   5892  C  C     . GLU B 1 20  ? 4.327   6.057   21.439  1.00 28.07 ? 40   GLU B C     1 
ATOM   5893  O  O     . GLU B 1 20  ? 5.141   5.415   20.758  1.00 27.81 ? 40   GLU B O     1 
ATOM   5894  C  CB    . GLU B 1 20  ? 4.710   6.271   23.917  1.00 28.47 ? 40   GLU B CB    1 
ATOM   5895  C  CG    . GLU B 1 20  ? 5.519   6.964   25.011  1.00 28.98 ? 40   GLU B CG    1 
ATOM   5896  C  CD    . GLU B 1 20  ? 5.368   6.286   26.360  1.00 29.86 ? 40   GLU B CD    1 
ATOM   5897  O  OE1   . GLU B 1 20  ? 4.212   6.093   26.806  1.00 28.82 ? 40   GLU B OE1   1 
ATOM   5898  O  OE2   . GLU B 1 20  ? 6.402   5.949   26.976  1.00 28.98 ? 40   GLU B OE2   1 
ATOM   5899  N  N     . LEU B 1 21  ? 3.014   6.021   21.219  1.00 27.62 ? 41   LEU B N     1 
ATOM   5900  C  CA    . LEU B 1 21  ? 2.451   5.209   20.145  1.00 27.47 ? 41   LEU B CA    1 
ATOM   5901  C  C     . LEU B 1 21  ? 2.962   5.658   18.773  1.00 27.64 ? 41   LEU B C     1 
ATOM   5902  O  O     . LEU B 1 21  ? 3.377   4.833   17.960  1.00 26.83 ? 41   LEU B O     1 
ATOM   5903  C  CB    . LEU B 1 21  ? 0.914   5.215   20.193  1.00 27.22 ? 41   LEU B CB    1 
ATOM   5904  C  CG    . LEU B 1 21  ? 0.296   4.378   21.328  1.00 26.32 ? 41   LEU B CG    1 
ATOM   5905  C  CD1   . LEU B 1 21  ? -1.173  4.719   21.520  1.00 24.52 ? 41   LEU B CD1   1 
ATOM   5906  C  CD2   . LEU B 1 21  ? 0.481   2.880   21.076  1.00 24.39 ? 41   LEU B CD2   1 
ATOM   5907  N  N     . LYS B 1 22  ? 2.906   6.967   18.532  1.00 28.36 ? 42   LYS B N     1 
ATOM   5908  C  CA    . LYS B 1 22  ? 3.487   7.592   17.339  1.00 28.81 ? 42   LYS B CA    1 
ATOM   5909  C  C     . LYS B 1 22  ? 4.982   7.306   17.205  1.00 29.09 ? 42   LYS B C     1 
ATOM   5910  O  O     . LYS B 1 22  ? 5.479   7.072   16.104  1.00 29.74 ? 42   LYS B O     1 
ATOM   5911  C  CB    . LYS B 1 22  ? 3.272   9.107   17.382  1.00 28.94 ? 42   LYS B CB    1 
ATOM   5912  C  CG    . LYS B 1 22  ? 1.847   9.552   17.064  1.00 29.31 ? 42   LYS B CG    1 
ATOM   5913  C  CD    . LYS B 1 22  ? 1.652   11.047  17.335  1.00 29.11 ? 42   LYS B CD    1 
ATOM   5914  C  CE    . LYS B 1 22  ? 0.229   11.492  17.014  1.00 28.61 ? 42   LYS B CE    1 
ATOM   5915  N  NZ    . LYS B 1 22  ? -0.027  12.912  17.390  1.00 27.93 ? 42   LYS B NZ    1 
ATOM   5916  N  N     . ALA B 1 23  ? 5.694   7.314   18.325  1.00 29.27 ? 43   ALA B N     1 
ATOM   5917  C  CA    . ALA B 1 23  ? 7.128   7.045   18.312  1.00 29.46 ? 43   ALA B CA    1 
ATOM   5918  C  C     . ALA B 1 23  ? 7.421   5.613   17.885  1.00 29.74 ? 43   ALA B C     1 
ATOM   5919  O  O     . ALA B 1 23  ? 8.354   5.384   17.116  1.00 29.59 ? 43   ALA B O     1 
ATOM   5920  C  CB    . ALA B 1 23  ? 7.750   7.340   19.683  1.00 29.11 ? 43   ALA B CB    1 
ATOM   5921  N  N     . VAL B 1 24  ? 6.632   4.648   18.371  1.00 29.96 ? 44   VAL B N     1 
ATOM   5922  C  CA    . VAL B 1 24  ? 6.855   3.242   18.008  1.00 30.32 ? 44   VAL B CA    1 
ATOM   5923  C  C     . VAL B 1 24  ? 6.503   3.004   16.536  1.00 31.12 ? 44   VAL B C     1 
ATOM   5924  O  O     . VAL B 1 24  ? 7.220   2.297   15.815  1.00 30.90 ? 44   VAL B O     1 
ATOM   5925  C  CB    . VAL B 1 24  ? 6.077   2.257   18.926  1.00 30.42 ? 44   VAL B CB    1 
ATOM   5926  C  CG1   . VAL B 1 24  ? 6.172   0.837   18.393  1.00 29.30 ? 44   VAL B CG1   1 
ATOM   5927  C  CG2   . VAL B 1 24  ? 6.617   2.316   20.360  1.00 29.79 ? 44   VAL B CG2   1 
ATOM   5928  N  N     . HIS B 1 25  ? 5.402   3.618   16.108  1.00 31.85 ? 45   HIS B N     1 
ATOM   5929  C  CA    . HIS B 1 25  ? 4.930   3.532   14.738  1.00 32.65 ? 45   HIS B CA    1 
ATOM   5930  C  C     . HIS B 1 25  ? 5.932   4.153   13.757  1.00 32.74 ? 45   HIS B C     1 
ATOM   5931  O  O     . HIS B 1 25  ? 6.218   3.564   12.721  1.00 32.44 ? 45   HIS B O     1 
ATOM   5932  C  CB    . HIS B 1 25  ? 3.582   4.238   14.615  1.00 32.98 ? 45   HIS B CB    1 
ATOM   5933  C  CG    . HIS B 1 25  ? 2.825   3.884   13.377  1.00 34.99 ? 45   HIS B CG    1 
ATOM   5934  N  ND1   . HIS B 1 25  ? 2.574   4.793   12.371  1.00 38.06 ? 45   HIS B ND1   1 
ATOM   5935  C  CD2   . HIS B 1 25  ? 2.259   2.721   12.983  1.00 36.74 ? 45   HIS B CD2   1 
ATOM   5936  C  CE1   . HIS B 1 25  ? 1.886   4.204   11.409  1.00 38.30 ? 45   HIS B CE1   1 
ATOM   5937  N  NE2   . HIS B 1 25  ? 1.678   2.947   11.758  1.00 38.95 ? 45   HIS B NE2   1 
ATOM   5938  N  N     . SER B 1 26  ? 6.442   5.339   14.089  1.00 33.03 ? 46   SER B N     1 
ATOM   5939  C  CA    A SER B 1 26  ? 7.441   6.014   13.252  0.60 33.31 ? 46   SER B CA    1 
ATOM   5940  C  CA    B SER B 1 26  ? 7.442   6.023   13.268  0.40 33.21 ? 46   SER B CA    1 
ATOM   5941  C  C     . SER B 1 26  ? 8.686   5.153   13.084  1.00 33.38 ? 46   SER B C     1 
ATOM   5942  O  O     . SER B 1 26  ? 9.176   4.971   11.969  1.00 33.80 ? 46   SER B O     1 
ATOM   5943  C  CB    A SER B 1 26  ? 7.841   7.368   13.843  0.60 33.31 ? 46   SER B CB    1 
ATOM   5944  C  CB    B SER B 1 26  ? 7.829   7.353   13.921  0.40 33.19 ? 46   SER B CB    1 
ATOM   5945  O  OG    A SER B 1 26  ? 6.868   8.353   13.557  0.60 33.96 ? 46   SER B OG    1 
ATOM   5946  O  OG    B SER B 1 26  ? 8.836   8.025   13.188  0.40 33.16 ? 46   SER B OG    1 
ATOM   5947  N  N     . PHE B 1 27  ? 9.185   4.622   14.190  1.00 33.39 ? 47   PHE B N     1 
ATOM   5948  C  CA    . PHE B 1 27  ? 10.376  3.775   14.180  1.00 33.62 ? 47   PHE B CA    1 
ATOM   5949  C  C     . PHE B 1 27  ? 10.226  2.582   13.226  1.00 33.81 ? 47   PHE B C     1 
ATOM   5950  O  O     . PHE B 1 27  ? 11.104  2.313   12.402  1.00 33.41 ? 47   PHE B O     1 
ATOM   5951  C  CB    . PHE B 1 27  ? 10.666  3.310   15.609  1.00 33.50 ? 47   PHE B CB    1 
ATOM   5952  C  CG    . PHE B 1 27  ? 11.686  2.235   15.701  1.00 34.05 ? 47   PHE B CG    1 
ATOM   5953  C  CD1   . PHE B 1 27  ? 13.031  2.528   15.568  1.00 35.25 ? 47   PHE B CD1   1 
ATOM   5954  C  CD2   . PHE B 1 27  ? 11.304  0.924   15.928  1.00 35.15 ? 47   PHE B CD2   1 
ATOM   5955  C  CE1   . PHE B 1 27  ? 13.986  1.528   15.655  1.00 36.08 ? 47   PHE B CE1   1 
ATOM   5956  C  CE2   . PHE B 1 27  ? 12.244  -0.084  16.015  1.00 36.00 ? 47   PHE B CE2   1 
ATOM   5957  C  CZ    . PHE B 1 27  ? 13.590  0.214   15.885  1.00 36.65 ? 47   PHE B CZ    1 
ATOM   5958  N  N     . LEU B 1 28  ? 9.100   1.882   13.329  1.00 33.82 ? 48   LEU B N     1 
ATOM   5959  C  CA    . LEU B 1 28  ? 8.849   0.725   12.483  1.00 33.51 ? 48   LEU B CA    1 
ATOM   5960  C  C     . LEU B 1 28  ? 8.712   1.158   11.020  1.00 33.90 ? 48   LEU B C     1 
ATOM   5961  O  O     . LEU B 1 28  ? 9.243   0.508   10.124  1.00 34.13 ? 48   LEU B O     1 
ATOM   5962  C  CB    . LEU B 1 28  ? 7.605   -0.035  12.963  1.00 33.33 ? 48   LEU B CB    1 
ATOM   5963  C  CG    . LEU B 1 28  ? 7.738   -0.699  14.343  1.00 32.30 ? 48   LEU B CG    1 
ATOM   5964  C  CD1   . LEU B 1 28  ? 6.392   -1.180  14.861  1.00 31.74 ? 48   LEU B CD1   1 
ATOM   5965  C  CD2   . LEU B 1 28  ? 8.738   -1.846  14.303  1.00 30.62 ? 48   LEU B CD2   1 
ATOM   5966  N  N     . TRP B 1 29  ? 8.021   2.266   10.783  1.00 34.44 ? 49   TRP B N     1 
ATOM   5967  C  CA    . TRP B 1 29  ? 7.848   2.773   9.423   1.00 34.81 ? 49   TRP B CA    1 
ATOM   5968  C  C     . TRP B 1 29  ? 9.153   3.250   8.782   1.00 34.86 ? 49   TRP B C     1 
ATOM   5969  O  O     . TRP B 1 29  ? 9.252   3.251   7.567   1.00 35.02 ? 49   TRP B O     1 
ATOM   5970  C  CB    . TRP B 1 29  ? 6.800   3.883   9.370   1.00 35.00 ? 49   TRP B CB    1 
ATOM   5971  C  CG    . TRP B 1 29  ? 5.450   3.364   9.082   1.00 36.07 ? 49   TRP B CG    1 
ATOM   5972  C  CD1   . TRP B 1 29  ? 4.660   2.632   9.925   1.00 37.75 ? 49   TRP B CD1   1 
ATOM   5973  C  CD2   . TRP B 1 29  ? 4.719   3.499   7.861   1.00 36.63 ? 49   TRP B CD2   1 
ATOM   5974  N  NE1   . TRP B 1 29  ? 3.476   2.313   9.304   1.00 38.11 ? 49   TRP B NE1   1 
ATOM   5975  C  CE2   . TRP B 1 29  ? 3.483   2.834   8.038   1.00 36.90 ? 49   TRP B CE2   1 
ATOM   5976  C  CE3   . TRP B 1 29  ? 4.980   4.125   6.637   1.00 36.95 ? 49   TRP B CE3   1 
ATOM   5977  C  CZ2   . TRP B 1 29  ? 2.506   2.779   7.036   1.00 36.75 ? 49   TRP B CZ2   1 
ATOM   5978  C  CZ3   . TRP B 1 29  ? 4.006   4.067   5.635   1.00 36.69 ? 49   TRP B CZ3   1 
ATOM   5979  C  CH2   . TRP B 1 29  ? 2.788   3.396   5.843   1.00 36.69 ? 49   TRP B CH2   1 
ATOM   5980  N  N     . SER B 1 30  ? 10.141  3.639   9.589   1.00 34.92 ? 50   SER B N     1 
ATOM   5981  C  CA    . SER B 1 30  ? 11.454  4.048   9.067   1.00 34.85 ? 50   SER B CA    1 
ATOM   5982  C  C     . SER B 1 30  ? 12.297  2.862   8.585   1.00 35.06 ? 50   SER B C     1 
ATOM   5983  O  O     . SER B 1 30  ? 13.320  3.056   7.922   1.00 35.19 ? 50   SER B O     1 
ATOM   5984  C  CB    . SER B 1 30  ? 12.233  4.827   10.117  1.00 34.63 ? 50   SER B CB    1 
ATOM   5985  O  OG    . SER B 1 30  ? 12.817  3.957   11.067  1.00 34.92 ? 50   SER B OG    1 
ATOM   5986  N  N     . LYS B 1 31  ? 11.883  1.644   8.933   1.00 35.00 ? 51   LYS B N     1 
ATOM   5987  C  CA    . LYS B 1 31  ? 12.529  0.439   8.435   1.00 35.04 ? 51   LYS B CA    1 
ATOM   5988  C  C     . LYS B 1 31  ? 11.907  0.031   7.097   1.00 34.91 ? 51   LYS B C     1 
ATOM   5989  O  O     . LYS B 1 31  ? 10.862  -0.631  7.051   1.00 34.40 ? 51   LYS B O     1 
ATOM   5990  C  CB    . LYS B 1 31  ? 12.404  -0.685  9.455   1.00 35.15 ? 51   LYS B CB    1 
ATOM   5991  C  CG    . LYS B 1 31  ? 13.116  -0.393  10.751  1.00 36.09 ? 51   LYS B CG    1 
ATOM   5992  C  CD    . LYS B 1 31  ? 13.150  -1.630  11.643  1.00 37.90 ? 51   LYS B CD    1 
ATOM   5993  C  CE    . LYS B 1 31  ? 14.111  -1.449  12.794  1.00 38.80 ? 51   LYS B CE    1 
ATOM   5994  N  NZ    . LYS B 1 31  ? 15.526  -1.309  12.329  1.00 40.60 ? 51   LYS B NZ    1 
ATOM   5995  N  N     . LYS B 1 32  ? 12.555  0.440   6.007   1.00 34.54 ? 52   LYS B N     1 
ATOM   5996  C  CA    . LYS B 1 32  ? 11.982  0.290   4.663   1.00 34.31 ? 52   LYS B CA    1 
ATOM   5997  C  C     . LYS B 1 32  ? 11.815  -1.164  4.247   1.00 33.84 ? 52   LYS B C     1 
ATOM   5998  O  O     . LYS B 1 32  ? 10.921  -1.492  3.472   1.00 33.50 ? 52   LYS B O     1 
ATOM   5999  C  CB    . LYS B 1 32  ? 12.840  1.033   3.632   1.00 34.58 ? 52   LYS B CB    1 
ATOM   6000  N  N     . GLU B 1 33  ? 12.665  -2.040  4.773   1.00 33.52 ? 53   GLU B N     1 
ATOM   6001  C  CA    . GLU B 1 33  ? 12.589  -3.465  4.438   1.00 33.46 ? 53   GLU B CA    1 
ATOM   6002  C  C     . GLU B 1 33  ? 11.328  -4.158  4.985   1.00 32.97 ? 53   GLU B C     1 
ATOM   6003  O  O     . GLU B 1 33  ? 11.005  -5.262  4.565   1.00 32.81 ? 53   GLU B O     1 
ATOM   6004  C  CB    . GLU B 1 33  ? 13.865  -4.214  4.875   1.00 33.52 ? 53   GLU B CB    1 
ATOM   6005  C  CG    . GLU B 1 33  ? 14.009  -4.519  6.380   1.00 34.82 ? 53   GLU B CG    1 
ATOM   6006  C  CD    . GLU B 1 33  ? 14.423  -3.316  7.210   1.00 36.49 ? 53   GLU B CD    1 
ATOM   6007  O  OE1   . GLU B 1 33  ? 14.402  -2.181  6.684   1.00 37.43 ? 53   GLU B OE1   1 
ATOM   6008  O  OE2   . GLU B 1 33  ? 14.761  -3.504  8.402   1.00 38.06 ? 53   GLU B OE2   1 
ATOM   6009  N  N     . LEU B 1 34  ? 10.623  -3.517  5.913   1.00 32.69 ? 54   LEU B N     1 
ATOM   6010  C  CA    . LEU B 1 34  ? 9.354   -4.048  6.419   1.00 32.39 ? 54   LEU B CA    1 
ATOM   6011  C  C     . LEU B 1 34  ? 8.188   -3.868  5.432   1.00 31.94 ? 54   LEU B C     1 
ATOM   6012  O  O     . LEU B 1 34  ? 7.171   -4.546  5.551   1.00 31.90 ? 54   LEU B O     1 
ATOM   6013  C  CB    . LEU B 1 34  ? 9.008   -3.405  7.767   1.00 32.51 ? 54   LEU B CB    1 
ATOM   6014  C  CG    . LEU B 1 34  ? 9.986   -3.686  8.922   1.00 32.46 ? 54   LEU B CG    1 
ATOM   6015  C  CD1   . LEU B 1 34  ? 9.467   -3.090  10.219  1.00 32.90 ? 54   LEU B CD1   1 
ATOM   6016  C  CD2   . LEU B 1 34  ? 10.241  -5.183  9.112   1.00 32.07 ? 54   LEU B CD2   1 
ATOM   6017  N  N     . ARG B 1 35  ? 8.339   -2.960  4.469   1.00 31.65 ? 55   ARG B N     1 
ATOM   6018  C  CA    . ARG B 1 35  ? 7.324   -2.717  3.438   1.00 31.41 ? 55   ARG B CA    1 
ATOM   6019  C  C     . ARG B 1 35  ? 5.945   -2.435  4.037   1.00 31.05 ? 55   ARG B C     1 
ATOM   6020  O  O     . ARG B 1 35  ? 4.922   -2.883  3.516   1.00 30.93 ? 55   ARG B O     1 
ATOM   6021  C  CB    . ARG B 1 35  ? 7.231   -3.899  2.468   1.00 31.63 ? 55   ARG B CB    1 
ATOM   6022  C  CG    . ARG B 1 35  ? 8.536   -4.249  1.755   1.00 33.08 ? 55   ARG B CG    1 
ATOM   6023  C  CD    . ARG B 1 35  ? 8.341   -5.347  0.699   1.00 34.73 ? 55   ARG B CD    1 
ATOM   6024  N  NE    . ARG B 1 35  ? 7.281   -5.021  -0.264  1.00 37.61 ? 55   ARG B NE    1 
ATOM   6025  C  CZ    . ARG B 1 35  ? 7.477   -4.391  -1.423  1.00 38.63 ? 55   ARG B CZ    1 
ATOM   6026  N  N     . LEU B 1 36  ? 5.922   -1.661  5.115   1.00 30.51 ? 56   LEU B N     1 
ATOM   6027  C  CA    . LEU B 1 36  ? 4.685   -1.413  5.837   1.00 30.11 ? 56   LEU B CA    1 
ATOM   6028  C  C     . LEU B 1 36  ? 3.716   -0.564  5.031   1.00 30.07 ? 56   LEU B C     1 
ATOM   6029  O  O     . LEU B 1 36  ? 4.116   0.337   4.299   1.00 30.46 ? 56   LEU B O     1 
ATOM   6030  C  CB    . LEU B 1 36  ? 4.974   -0.756  7.186   1.00 29.86 ? 56   LEU B CB    1 
ATOM   6031  C  CG    . LEU B 1 36  ? 5.777   -1.609  8.170   1.00 29.11 ? 56   LEU B CG    1 
ATOM   6032  C  CD1   . LEU B 1 36  ? 6.011   -0.839  9.460   1.00 28.97 ? 56   LEU B CD1   1 
ATOM   6033  C  CD2   . LEU B 1 36  ? 5.099   -2.937  8.448   1.00 27.24 ? 56   LEU B CD2   1 
ATOM   6034  N  N     . GLN B 1 37  ? 2.433   -0.882  5.165   1.00 29.79 ? 57   GLN B N     1 
ATOM   6035  C  CA    . GLN B 1 37  ? 1.359   -0.120  4.559   1.00 29.40 ? 57   GLN B CA    1 
ATOM   6036  C  C     . GLN B 1 37  ? 0.266   0.101   5.623   1.00 29.68 ? 57   GLN B C     1 
ATOM   6037  O  O     . GLN B 1 37  ? 0.201   -0.639  6.609   1.00 29.83 ? 57   GLN B O     1 
ATOM   6038  C  CB    . GLN B 1 37  ? 0.791   -0.875  3.360   1.00 29.40 ? 57   GLN B CB    1 
ATOM   6039  C  CG    . GLN B 1 37  ? 1.815   -1.287  2.320   1.00 29.11 ? 57   GLN B CG    1 
ATOM   6040  C  CD    . GLN B 1 37  ? 1.174   -1.934  1.108   1.00 29.30 ? 57   GLN B CD    1 
ATOM   6041  O  OE1   . GLN B 1 37  ? 0.188   -1.438  0.584   1.00 29.79 ? 57   GLN B OE1   1 
ATOM   6042  N  NE2   . GLN B 1 37  ? 1.726   -3.053  0.667   1.00 29.98 ? 57   GLN B NE2   1 
ATOM   6043  N  N     . PRO B 1 38  ? -0.600  1.112   5.432   1.00 29.60 ? 58   PRO B N     1 
ATOM   6044  C  CA    . PRO B 1 38  ? -1.645  1.360   6.431   1.00 29.53 ? 58   PRO B CA    1 
ATOM   6045  C  C     . PRO B 1 38  ? -2.615  0.189   6.609   1.00 29.59 ? 58   PRO B C     1 
ATOM   6046  O  O     . PRO B 1 38  ? -2.822  -0.595  5.684   1.00 29.46 ? 58   PRO B O     1 
ATOM   6047  C  CB    . PRO B 1 38  ? -2.384  2.590   5.884   1.00 29.64 ? 58   PRO B CB    1 
ATOM   6048  C  CG    . PRO B 1 38  ? -1.494  3.176   4.831   1.00 29.64 ? 58   PRO B CG    1 
ATOM   6049  C  CD    . PRO B 1 38  ? -0.660  2.061   4.307   1.00 29.77 ? 58   PRO B CD    1 
ATOM   6050  N  N     . SER B 1 39  ? -3.195  0.076   7.801   1.00 29.88 ? 59   SER B N     1 
ATOM   6051  C  CA    . SER B 1 39  ? -4.241  -0.906  8.063   1.00 30.43 ? 59   SER B CA    1 
ATOM   6052  C  C     . SER B 1 39  ? -5.384  -0.752  7.062   1.00 30.60 ? 59   SER B C     1 
ATOM   6053  O  O     . SER B 1 39  ? -5.989  -1.739  6.667   1.00 31.05 ? 59   SER B O     1 
ATOM   6054  C  CB    . SER B 1 39  ? -4.800  -0.753  9.484   1.00 30.56 ? 59   SER B CB    1 
ATOM   6055  O  OG    . SER B 1 39  ? -5.674  0.373   9.582   1.00 31.46 ? 59   SER B OG    1 
ATOM   6056  N  N     . SER B 1 40  ? -5.656  0.486   6.646   1.00 30.77 ? 60   SER B N     1 
ATOM   6057  C  CA    . SER B 1 40  ? -6.808  0.789   5.792   1.00 30.95 ? 60   SER B CA    1 
ATOM   6058  C  C     . SER B 1 40  ? -6.665  0.366   4.326   1.00 30.99 ? 60   SER B C     1 
ATOM   6059  O  O     . SER B 1 40  ? -7.650  0.367   3.601   1.00 30.89 ? 60   SER B O     1 
ATOM   6060  C  CB    . SER B 1 40  ? -7.154  2.282   5.872   1.00 30.78 ? 60   SER B CB    1 
ATOM   6061  O  OG    . SER B 1 40  ? -6.069  3.106   5.490   1.00 31.40 ? 60   SER B OG    1 
ATOM   6062  N  N     . THR B 1 41  ? -5.451  0.031   3.884   1.00 31.30 ? 61   THR B N     1 
ATOM   6063  C  CA    . THR B 1 41  ? -5.242  -0.426  2.508   1.00 31.14 ? 61   THR B CA    1 
ATOM   6064  C  C     . THR B 1 41  ? -5.969  -1.755  2.315   1.00 31.29 ? 61   THR B C     1 
ATOM   6065  O  O     . THR B 1 41  ? -5.763  -2.690  3.090   1.00 30.87 ? 61   THR B O     1 
ATOM   6066  C  CB    . THR B 1 41  ? -3.750  -0.599  2.203   1.00 31.49 ? 61   THR B CB    1 
ATOM   6067  O  OG1   . THR B 1 41  ? -3.075  0.629   2.488   1.00 31.63 ? 61   THR B OG1   1 
ATOM   6068  C  CG2   . THR B 1 41  ? -3.512  -1.000  0.742   1.00 30.55 ? 61   THR B CG2   1 
ATOM   6069  N  N     . THR B 1 42  ? -6.815  -1.833  1.285   1.00 31.27 ? 62   THR B N     1 
ATOM   6070  C  CA    . THR B 1 42  ? -7.787  -2.927  1.150   1.00 31.34 ? 62   THR B CA    1 
ATOM   6071  C  C     . THR B 1 42  ? -7.240  -4.106  0.339   1.00 30.90 ? 62   THR B C     1 
ATOM   6072  O  O     . THR B 1 42  ? -7.792  -4.476  -0.717  1.00 30.59 ? 62   THR B O     1 
ATOM   6073  C  CB    . THR B 1 42  ? -9.113  -2.431  0.498   1.00 31.77 ? 62   THR B CB    1 
ATOM   6074  O  OG1   . THR B 1 42  ? -8.841  -1.968  -0.827  1.00 33.20 ? 62   THR B OG1   1 
ATOM   6075  C  CG2   . THR B 1 42  ? -9.730  -1.294  1.309   1.00 31.65 ? 62   THR B CG2   1 
ATOM   6076  N  N     . THR B 1 43  ? -6.140  -4.665  0.839   1.00 29.99 ? 63   THR B N     1 
ATOM   6077  C  CA    . THR B 1 43  ? -5.593  -5.923  0.366   1.00 29.48 ? 63   THR B CA    1 
ATOM   6078  C  C     . THR B 1 43  ? -5.062  -6.660  1.581   1.00 28.87 ? 63   THR B C     1 
ATOM   6079  O  O     . THR B 1 43  ? -4.626  -6.034  2.541   1.00 28.19 ? 63   THR B O     1 
ATOM   6080  C  CB    . THR B 1 43  ? -4.427  -5.735  -0.648  1.00 29.52 ? 63   THR B CB    1 
ATOM   6081  O  OG1   . THR B 1 43  ? -4.003  -7.013  -1.118  1.00 29.22 ? 63   THR B OG1   1 
ATOM   6082  C  CG2   . THR B 1 43  ? -3.225  -5.043  -0.002  1.00 29.92 ? 63   THR B CG2   1 
ATOM   6083  N  N     . MET B 1 44  ? -5.101  -7.987  1.531   1.00 28.59 ? 64   MET B N     1 
ATOM   6084  C  CA    . MET B 1 44  ? -4.518  -8.810  2.579   1.00 28.21 ? 64   MET B CA    1 
ATOM   6085  C  C     . MET B 1 44  ? -3.021  -9.008  2.331   1.00 28.10 ? 64   MET B C     1 
ATOM   6086  O  O     . MET B 1 44  ? -2.278  -9.362  3.250   1.00 28.16 ? 64   MET B O     1 
ATOM   6087  C  CB    . MET B 1 44  ? -5.232  -10.159 2.633   1.00 28.40 ? 64   MET B CB    1 
ATOM   6088  C  CG    . MET B 1 44  ? -6.741  -10.072 2.858   1.00 28.45 ? 64   MET B CG    1 
ATOM   6089  S  SD    . MET B 1 44  ? -7.207  -9.507  4.517   1.00 29.13 ? 64   MET B SD    1 
ATOM   6090  C  CE    . MET B 1 44  ? -7.149  -7.724  4.345   1.00 28.13 ? 64   MET B CE    1 
ATOM   6091  N  N     . ALA B 1 45  ? -2.576  -8.771  1.095   1.00 27.82 ? 65   ALA B N     1 
ATOM   6092  C  CA    . ALA B 1 45  ? -1.178  -9.000  0.707   1.00 27.87 ? 65   ALA B CA    1 
ATOM   6093  C  C     . ALA B 1 45  ? -0.327  -7.769  0.996   1.00 27.73 ? 65   ALA B C     1 
ATOM   6094  O  O     . ALA B 1 45  ? 0.251   -7.174  0.096   1.00 28.02 ? 65   ALA B O     1 
ATOM   6095  C  CB    . ALA B 1 45  ? -1.077  -9.392  -0.776  1.00 27.49 ? 65   ALA B CB    1 
ATOM   6096  N  N     . LYS B 1 46  ? -0.264  -7.401  2.268   1.00 27.88 ? 66   LYS B N     1 
ATOM   6097  C  CA    . LYS B 1 46  ? 0.479   -6.236  2.722   1.00 27.43 ? 66   LYS B CA    1 
ATOM   6098  C  C     . LYS B 1 46  ? 1.076   -6.562  4.081   1.00 27.19 ? 66   LYS B C     1 
ATOM   6099  O  O     . LYS B 1 46  ? 0.599   -7.453  4.786   1.00 26.84 ? 66   LYS B O     1 
ATOM   6100  C  CB    . LYS B 1 46  ? -0.438  -5.024  2.851   1.00 27.95 ? 66   LYS B CB    1 
ATOM   6101  C  CG    . LYS B 1 46  ? -1.567  -5.226  3.860   1.00 28.49 ? 66   LYS B CG    1 
ATOM   6102  C  CD    . LYS B 1 46  ? -2.528  -4.046  3.955   1.00 30.22 ? 66   LYS B CD    1 
ATOM   6103  C  CE    . LYS B 1 46  ? -3.580  -4.336  5.044   1.00 30.25 ? 66   LYS B CE    1 
ATOM   6104  N  NZ    . LYS B 1 46  ? -4.546  -3.254  5.213   1.00 31.96 ? 66   LYS B NZ    1 
ATOM   6105  N  N     . ASN B 1 47  ? 2.141   -5.854  4.423   1.00 26.71 ? 67   ASN B N     1 
ATOM   6106  C  CA    . ASN B 1 47  ? 2.677   -5.867  5.768   1.00 26.21 ? 67   ASN B CA    1 
ATOM   6107  C  C     . ASN B 1 47  ? 2.133   -4.632  6.488   1.00 25.74 ? 67   ASN B C     1 
ATOM   6108  O  O     . ASN B 1 47  ? 2.148   -3.530  5.931   1.00 25.86 ? 67   ASN B O     1 
ATOM   6109  C  CB    . ASN B 1 47  ? 4.201   -5.823  5.732   1.00 26.47 ? 67   ASN B CB    1 
ATOM   6110  C  CG    . ASN B 1 47  ? 4.805   -7.011  5.023   1.00 25.22 ? 67   ASN B CG    1 
ATOM   6111  O  OD1   . ASN B 1 47  ? 4.144   -8.018  4.787   1.00 25.82 ? 67   ASN B OD1   1 
ATOM   6112  N  ND2   . ASN B 1 47  ? 6.073   -6.898  4.685   1.00 24.65 ? 67   ASN B ND2   1 
ATOM   6113  N  N     . THR B 1 48  ? 1.638   -4.823  7.706   1.00 25.00 ? 68   THR B N     1 
ATOM   6114  C  CA    A THR B 1 48  ? 1.042   -3.742  8.470   0.60 24.74 ? 68   THR B CA    1 
ATOM   6115  C  CA    B THR B 1 48  ? 1.015   -3.750  8.477   0.40 24.76 ? 68   THR B CA    1 
ATOM   6116  C  C     . THR B 1 48  ? 1.207   -3.999  9.964   1.00 24.64 ? 68   THR B C     1 
ATOM   6117  O  O     . THR B 1 48  ? 1.224   -5.150  10.404  1.00 24.44 ? 68   THR B O     1 
ATOM   6118  C  CB    A THR B 1 48  ? -0.463  -3.581  8.114   0.60 24.78 ? 68   THR B CB    1 
ATOM   6119  C  CB    B THR B 1 48  ? -0.512  -3.662  8.212   0.40 24.77 ? 68   THR B CB    1 
ATOM   6120  O  OG1   A THR B 1 48  ? -0.953  -2.338  8.626   0.60 24.26 ? 68   THR B OG1   1 
ATOM   6121  O  OG1   B THR B 1 48  ? -1.146  -4.876  8.633   0.40 24.70 ? 68   THR B OG1   1 
ATOM   6122  C  CG2   A THR B 1 48  ? -1.287  -4.727  8.679   0.60 24.68 ? 68   THR B CG2   1 
ATOM   6123  C  CG2   B THR B 1 48  ? -0.808  -3.426  6.739   0.40 24.33 ? 68   THR B CG2   1 
ATOM   6124  N  N     . VAL B 1 49  ? 1.337   -2.921  10.733  1.00 24.66 ? 69   VAL B N     1 
ATOM   6125  C  CA    . VAL B 1 49  ? 1.416   -3.016  12.189  1.00 24.85 ? 69   VAL B CA    1 
ATOM   6126  C  C     . VAL B 1 49  ? -0.022  -3.064  12.720  1.00 24.96 ? 69   VAL B C     1 
ATOM   6127  O  O     . VAL B 1 49  ? -0.754  -2.085  12.624  1.00 25.26 ? 69   VAL B O     1 
ATOM   6128  C  CB    . VAL B 1 49  ? 2.195   -1.826  12.809  1.00 24.68 ? 69   VAL B CB    1 
ATOM   6129  C  CG1   . VAL B 1 49  ? 2.378   -2.028  14.313  1.00 24.70 ? 69   VAL B CG1   1 
ATOM   6130  C  CG2   . VAL B 1 49  ? 3.563   -1.671  12.131  1.00 24.92 ? 69   VAL B CG2   1 
ATOM   6131  N  N     . PHE B 1 50  ? -0.424  -4.217  13.243  1.00 25.23 ? 70   PHE B N     1 
ATOM   6132  C  CA    . PHE B 1 50  ? -1.798  -4.447  13.677  1.00 25.24 ? 70   PHE B CA    1 
ATOM   6133  C  C     . PHE B 1 50  ? -2.054  -3.852  15.068  1.00 25.50 ? 70   PHE B C     1 
ATOM   6134  O  O     . PHE B 1 50  ? -3.099  -3.267  15.318  1.00 25.79 ? 70   PHE B O     1 
ATOM   6135  C  CB    . PHE B 1 50  ? -2.099  -5.949  13.679  1.00 25.06 ? 70   PHE B CB    1 
ATOM   6136  C  CG    . PHE B 1 50  ? -3.523  -6.282  14.010  1.00 26.20 ? 70   PHE B CG    1 
ATOM   6137  C  CD1   . PHE B 1 50  ? -4.547  -5.979  13.123  1.00 25.79 ? 70   PHE B CD1   1 
ATOM   6138  C  CD2   . PHE B 1 50  ? -3.850  -6.887  15.218  1.00 26.67 ? 70   PHE B CD2   1 
ATOM   6139  C  CE1   . PHE B 1 50  ? -5.864  -6.285  13.431  1.00 25.63 ? 70   PHE B CE1   1 
ATOM   6140  C  CE2   . PHE B 1 50  ? -5.183  -7.183  15.530  1.00 26.80 ? 70   PHE B CE2   1 
ATOM   6141  C  CZ    . PHE B 1 50  ? -6.178  -6.883  14.635  1.00 25.50 ? 70   PHE B CZ    1 
ATOM   6142  N  N     . LEU B 1 51  ? -1.095  -4.001  15.969  1.00 25.55 ? 71   LEU B N     1 
ATOM   6143  C  CA    . LEU B 1 51  ? -1.292  -3.618  17.355  1.00 25.61 ? 71   LEU B CA    1 
ATOM   6144  C  C     . LEU B 1 51  ? 0.003   -3.128  17.970  1.00 25.59 ? 71   LEU B C     1 
ATOM   6145  O  O     . LEU B 1 51  ? 1.053   -3.727  17.755  1.00 25.13 ? 71   LEU B O     1 
ATOM   6146  C  CB    . LEU B 1 51  ? -1.815  -4.820  18.139  1.00 25.97 ? 71   LEU B CB    1 
ATOM   6147  C  CG    . LEU B 1 51  ? -1.538  -4.943  19.638  1.00 26.60 ? 71   LEU B CG    1 
ATOM   6148  C  CD1   . LEU B 1 51  ? -2.261  -3.846  20.396  1.00 27.61 ? 71   LEU B CD1   1 
ATOM   6149  C  CD2   . LEU B 1 51  ? -1.977  -6.321  20.110  1.00 26.53 ? 71   LEU B CD2   1 
ATOM   6150  N  N     . ILE B 1 52  ? -0.094  -2.030  18.720  1.00 25.50 ? 72   ILE B N     1 
ATOM   6151  C  CA    . ILE B 1 52  ? 0.979   -1.561  19.587  1.00 25.76 ? 72   ILE B CA    1 
ATOM   6152  C  C     . ILE B 1 52  ? 0.401   -1.255  20.977  1.00 25.93 ? 72   ILE B C     1 
ATOM   6153  O  O     . ILE B 1 52  ? -0.553  -0.486  21.096  1.00 26.24 ? 72   ILE B O     1 
ATOM   6154  C  CB    . ILE B 1 52  ? 1.637   -0.262  19.076  1.00 25.63 ? 72   ILE B CB    1 
ATOM   6155  C  CG1   . ILE B 1 52  ? 2.199   -0.433  17.663  1.00 25.56 ? 72   ILE B CG1   1 
ATOM   6156  C  CG2   . ILE B 1 52  ? 2.748   0.162   20.040  1.00 25.57 ? 72   ILE B CG2   1 
ATOM   6157  C  CD1   . ILE B 1 52  ? 2.534   0.876   16.990  1.00 24.07 ? 72   ILE B CD1   1 
ATOM   6158  N  N     . GLU B 1 53  ? 0.986   -1.853  22.008  1.00 26.00 ? 73   GLU B N     1 
ATOM   6159  C  CA    . GLU B 1 53  ? 0.637   -1.562  23.401  1.00 26.22 ? 73   GLU B CA    1 
ATOM   6160  C  C     . GLU B 1 53  ? 1.889   -1.731  24.267  1.00 26.29 ? 73   GLU B C     1 
ATOM   6161  O  O     . GLU B 1 53  ? 2.884   -2.283  23.812  1.00 25.34 ? 73   GLU B O     1 
ATOM   6162  C  CB    . GLU B 1 53  ? -0.479  -2.498  23.883  1.00 26.27 ? 73   GLU B CB    1 
ATOM   6163  C  CG    . GLU B 1 53  ? -0.102  -3.979  23.858  1.00 26.31 ? 73   GLU B CG    1 
ATOM   6164  C  CD    . GLU B 1 53  ? -1.264  -4.924  24.153  1.00 27.33 ? 73   GLU B CD    1 
ATOM   6165  O  OE1   . GLU B 1 53  ? -2.431  -4.464  24.228  1.00 29.05 ? 73   GLU B OE1   1 
ATOM   6166  O  OE2   . GLU B 1 53  ? -0.996  -6.140  24.301  1.00 26.61 ? 73   GLU B OE2   1 
ATOM   6167  N  N     . MET B 1 54  ? 1.842   -1.249  25.508  1.00 26.74 ? 74   MET B N     1 
ATOM   6168  C  CA    . MET B 1 54  ? 3.005   -1.354  26.399  1.00 26.68 ? 74   MET B CA    1 
ATOM   6169  C  C     . MET B 1 54  ? 3.224   -2.813  26.795  1.00 26.95 ? 74   MET B C     1 
ATOM   6170  O  O     . MET B 1 54  ? 2.265   -3.556  27.042  1.00 26.48 ? 74   MET B O     1 
ATOM   6171  C  CB    . MET B 1 54  ? 2.838   -0.461  27.632  1.00 26.68 ? 74   MET B CB    1 
ATOM   6172  C  CG    . MET B 1 54  ? 4.003   -0.490  28.621  1.00 27.11 ? 74   MET B CG    1 
ATOM   6173  S  SD    . MET B 1 54  ? 3.921   -1.846  29.823  1.00 29.81 ? 74   MET B SD    1 
ATOM   6174  C  CE    . MET B 1 54  ? 2.672   -1.259  30.971  1.00 29.13 ? 74   MET B CE    1 
ATOM   6175  N  N     . LEU B 1 55  ? 4.497   -3.211  26.821  1.00 27.07 ? 75   LEU B N     1 
ATOM   6176  C  CA    . LEU B 1 55  ? 4.916   -4.555  27.185  1.00 27.43 ? 75   LEU B CA    1 
ATOM   6177  C  C     . LEU B 1 55  ? 5.536   -4.508  28.583  1.00 27.58 ? 75   LEU B C     1 
ATOM   6178  O  O     . LEU B 1 55  ? 6.629   -3.964  28.766  1.00 27.65 ? 75   LEU B O     1 
ATOM   6179  C  CB    . LEU B 1 55  ? 5.948   -5.081  26.169  1.00 27.71 ? 75   LEU B CB    1 
ATOM   6180  C  CG    . LEU B 1 55  ? 6.417   -6.534  26.326  1.00 27.96 ? 75   LEU B CG    1 
ATOM   6181  C  CD1   . LEU B 1 55  ? 5.253   -7.490  26.171  1.00 27.79 ? 75   LEU B CD1   1 
ATOM   6182  C  CD2   . LEU B 1 55  ? 7.533   -6.880  25.334  1.00 26.73 ? 75   LEU B CD2   1 
ATOM   6183  N  N     . LEU B 1 56  ? 4.845   -5.087  29.560  1.00 27.45 ? 76   LEU B N     1 
ATOM   6184  C  CA    . LEU B 1 56  ? 5.278   -5.021  30.951  1.00 27.84 ? 76   LEU B CA    1 
ATOM   6185  C  C     . LEU B 1 56  ? 6.690   -5.605  31.142  1.00 27.68 ? 76   LEU B C     1 
ATOM   6186  O  O     . LEU B 1 56  ? 6.991   -6.665  30.608  1.00 27.31 ? 76   LEU B O     1 
ATOM   6187  C  CB    . LEU B 1 56  ? 4.274   -5.749  31.858  1.00 27.90 ? 76   LEU B CB    1 
ATOM   6188  C  CG    . LEU B 1 56  ? 4.152   -5.248  33.300  1.00 29.13 ? 76   LEU B CG    1 
ATOM   6189  C  CD1   . LEU B 1 56  ? 3.958   -3.732  33.368  1.00 28.16 ? 76   LEU B CD1   1 
ATOM   6190  C  CD2   . LEU B 1 56  ? 3.000   -5.966  33.995  1.00 30.13 ? 76   LEU B CD2   1 
ATOM   6191  N  N     . PRO B 1 57  ? 7.557   -4.908  31.894  1.00 27.87 ? 77   PRO B N     1 
ATOM   6192  C  CA    . PRO B 1 57  ? 8.847   -5.492  32.262  1.00 28.17 ? 77   PRO B CA    1 
ATOM   6193  C  C     . PRO B 1 57  ? 8.692   -6.703  33.171  1.00 28.50 ? 77   PRO B C     1 
ATOM   6194  O  O     . PRO B 1 57  ? 7.620   -6.949  33.715  1.00 28.56 ? 77   PRO B O     1 
ATOM   6195  C  CB    . PRO B 1 57  ? 9.552   -4.368  33.042  1.00 28.10 ? 77   PRO B CB    1 
ATOM   6196  C  CG    . PRO B 1 57  ? 8.782   -3.149  32.798  1.00 27.90 ? 77   PRO B CG    1 
ATOM   6197  C  CD    . PRO B 1 57  ? 7.386   -3.562  32.468  1.00 28.06 ? 77   PRO B CD    1 
ATOM   6198  N  N     . LYS B 1 58  ? 9.777   -7.435  33.353  1.00 29.21 ? 78   LYS B N     1 
ATOM   6199  C  CA    . LYS B 1 58  ? 9.790   -8.581  34.253  1.00 29.50 ? 78   LYS B CA    1 
ATOM   6200  C  C     . LYS B 1 58  ? 9.494   -8.151  35.691  1.00 29.41 ? 78   LYS B C     1 
ATOM   6201  O  O     . LYS B 1 58  ? 9.946   -7.092  36.139  1.00 28.65 ? 78   LYS B O     1 
ATOM   6202  C  CB    . LYS B 1 58  ? 11.140  -9.290  34.181  1.00 29.81 ? 78   LYS B CB    1 
ATOM   6203  C  CG    . LYS B 1 58  ? 11.397  -9.975  32.844  1.00 31.27 ? 78   LYS B CG    1 
ATOM   6204  C  CD    . LYS B 1 58  ? 12.798  -10.556 32.811  1.00 33.51 ? 78   LYS B CD    1 
ATOM   6205  C  CE    . LYS B 1 58  ? 13.128  -11.153 31.453  1.00 34.99 ? 78   LYS B CE    1 
ATOM   6206  N  NZ    . LYS B 1 58  ? 14.515  -11.722 31.427  1.00 36.71 ? 78   LYS B NZ    1 
ATOM   6207  N  N     . LYS B 1 59  ? 8.726   -8.982  36.396  1.00 29.44 ? 79   LYS B N     1 
ATOM   6208  C  CA    . LYS B 1 59  ? 8.328   -8.695  37.774  1.00 29.74 ? 79   LYS B CA    1 
ATOM   6209  C  C     . LYS B 1 59  ? 9.541   -8.510  38.677  1.00 30.12 ? 79   LYS B C     1 
ATOM   6210  O  O     . LYS B 1 59  ? 9.530   -7.667  39.563  1.00 30.20 ? 79   LYS B O     1 
ATOM   6211  C  CB    . LYS B 1 59  ? 7.443   -9.819  38.324  1.00 29.34 ? 79   LYS B CB    1 
ATOM   6212  C  CG    . LYS B 1 59  ? 6.845   -9.533  39.696  1.00 28.17 ? 79   LYS B CG    1 
ATOM   6213  C  CD    . LYS B 1 59  ? 5.937   -10.656 40.137  1.00 26.58 ? 79   LYS B CD    1 
ATOM   6214  C  CE    . LYS B 1 59  ? 5.365   -10.415 41.521  1.00 25.63 ? 79   LYS B CE    1 
ATOM   6215  N  NZ    . LYS B 1 59  ? 4.394   -11.466 41.883  1.00 24.01 ? 79   LYS B NZ    1 
ATOM   6216  N  N     . TYR B 1 60  ? 10.572  -9.317  38.447  1.00 30.95 ? 80   TYR B N     1 
ATOM   6217  C  CA    . TYR B 1 60  ? 11.823  -9.229  39.202  1.00 31.49 ? 80   TYR B CA    1 
ATOM   6218  C  C     . TYR B 1 60  ? 12.370  -7.803  39.173  1.00 31.19 ? 80   TYR B C     1 
ATOM   6219  O  O     . TYR B 1 60  ? 12.674  -7.220  40.217  1.00 31.34 ? 80   TYR B O     1 
ATOM   6220  C  CB    . TYR B 1 60  ? 12.846  -10.214 38.629  1.00 31.87 ? 80   TYR B CB    1 
ATOM   6221  C  CG    . TYR B 1 60  ? 14.232  -10.031 39.171  1.00 34.18 ? 80   TYR B CG    1 
ATOM   6222  C  CD1   . TYR B 1 60  ? 14.564  -10.490 40.441  1.00 36.66 ? 80   TYR B CD1   1 
ATOM   6223  C  CD2   . TYR B 1 60  ? 15.212  -9.388  38.421  1.00 36.27 ? 80   TYR B CD2   1 
ATOM   6224  C  CE1   . TYR B 1 60  ? 15.835  -10.317 40.955  1.00 37.79 ? 80   TYR B CE1   1 
ATOM   6225  C  CE2   . TYR B 1 60  ? 16.493  -9.210  38.925  1.00 37.95 ? 80   TYR B CE2   1 
ATOM   6226  C  CZ    . TYR B 1 60  ? 16.794  -9.679  40.193  1.00 39.11 ? 80   TYR B CZ    1 
ATOM   6227  O  OH    . TYR B 1 60  ? 18.054  -9.511  40.705  1.00 41.80 ? 80   TYR B OH    1 
ATOM   6228  N  N     . HIS B 1 61  ? 12.456  -7.238  37.972  1.00 31.06 ? 81   HIS B N     1 
ATOM   6229  C  CA    . HIS B 1 61  ? 12.981  -5.889  37.787  1.00 30.95 ? 81   HIS B CA    1 
ATOM   6230  C  C     . HIS B 1 61  ? 12.025  -4.821  38.328  1.00 30.51 ? 81   HIS B C     1 
ATOM   6231  O  O     . HIS B 1 61  ? 12.464  -3.820  38.904  1.00 30.57 ? 81   HIS B O     1 
ATOM   6232  C  CB    . HIS B 1 61  ? 13.297  -5.630  36.307  1.00 31.23 ? 81   HIS B CB    1 
ATOM   6233  C  CG    . HIS B 1 61  ? 14.382  -6.509  35.753  1.00 32.66 ? 81   HIS B CG    1 
ATOM   6234  N  ND1   . HIS B 1 61  ? 15.595  -6.687  36.386  1.00 33.83 ? 81   HIS B ND1   1 
ATOM   6235  C  CD2   . HIS B 1 61  ? 14.440  -7.251  34.620  1.00 33.44 ? 81   HIS B CD2   1 
ATOM   6236  C  CE1   . HIS B 1 61  ? 16.347  -7.508  35.672  1.00 33.94 ? 81   HIS B CE1   1 
ATOM   6237  N  NE2   . HIS B 1 61  ? 15.671  -7.860  34.594  1.00 33.64 ? 81   HIS B NE2   1 
ATOM   6238  N  N     . VAL B 1 62  ? 10.721  -5.032  38.150  1.00 29.68 ? 82   VAL B N     1 
ATOM   6239  C  CA    . VAL B 1 62  ? 9.725   -4.080  38.646  1.00 29.00 ? 82   VAL B CA    1 
ATOM   6240  C  C     . VAL B 1 62  ? 9.746   -3.992  40.178  1.00 28.89 ? 82   VAL B C     1 
ATOM   6241  O  O     . VAL B 1 62  ? 9.683   -2.904  40.738  1.00 28.27 ? 82   VAL B O     1 
ATOM   6242  C  CB    . VAL B 1 62  ? 8.281   -4.430  38.164  1.00 28.93 ? 82   VAL B CB    1 
ATOM   6243  C  CG1   . VAL B 1 62  ? 7.288   -3.430  38.717  1.00 27.99 ? 82   VAL B CG1   1 
ATOM   6244  C  CG2   . VAL B 1 62  ? 8.204   -4.465  36.635  1.00 27.17 ? 82   VAL B CG2   1 
ATOM   6245  N  N     . LEU B 1 63  ? 9.837   -5.135  40.850  1.00 29.16 ? 83   LEU B N     1 
ATOM   6246  C  CA    . LEU B 1 63  ? 9.865   -5.150  42.317  1.00 29.70 ? 83   LEU B CA    1 
ATOM   6247  C  C     . LEU B 1 63  ? 11.157  -4.551  42.887  1.00 30.14 ? 83   LEU B C     1 
ATOM   6248  O  O     . LEU B 1 63  ? 11.123  -3.909  43.928  1.00 30.17 ? 83   LEU B O     1 
ATOM   6249  C  CB    . LEU B 1 63  ? 9.648   -6.566  42.859  1.00 29.46 ? 83   LEU B CB    1 
ATOM   6250  C  CG    . LEU B 1 63  ? 8.221   -7.114  42.706  1.00 29.86 ? 83   LEU B CG    1 
ATOM   6251  C  CD1   . LEU B 1 63  ? 8.113   -8.513  43.316  1.00 29.45 ? 83   LEU B CD1   1 
ATOM   6252  C  CD2   . LEU B 1 63  ? 7.203   -6.172  43.330  1.00 29.82 ? 83   LEU B CD2   1 
ATOM   6253  N  N     . ARG B 1 64  ? 12.283  -4.748  42.204  1.00 30.75 ? 84   ARG B N     1 
ATOM   6254  C  CA    . ARG B 1 64  ? 13.553  -4.146  42.643  1.00 31.22 ? 84   ARG B CA    1 
ATOM   6255  C  C     . ARG B 1 64  ? 13.499  -2.628  42.496  1.00 31.71 ? 84   ARG B C     1 
ATOM   6256  O  O     . ARG B 1 64  ? 14.078  -1.895  43.300  1.00 32.28 ? 84   ARG B O     1 
ATOM   6257  C  CB    . ARG B 1 64  ? 14.739  -4.725  41.864  1.00 31.14 ? 84   ARG B CB    1 
ATOM   6258  C  CG    . ARG B 1 64  ? 15.247  -6.046  42.401  1.00 31.28 ? 84   ARG B CG    1 
ATOM   6259  C  CD    . ARG B 1 64  ? 16.238  -6.683  41.434  1.00 32.62 ? 84   ARG B CD    1 
ATOM   6260  N  N     . PHE B 1 65  ? 12.793  -2.164  41.470  1.00 32.06 ? 85   PHE B N     1 
ATOM   6261  C  CA    . PHE B 1 65  ? 12.540  -0.738  41.269  1.00 32.29 ? 85   PHE B CA    1 
ATOM   6262  C  C     . PHE B 1 65  ? 11.609  -0.160  42.341  1.00 32.49 ? 85   PHE B C     1 
ATOM   6263  O  O     . PHE B 1 65  ? 11.844  0.939   42.854  1.00 32.63 ? 85   PHE B O     1 
ATOM   6264  C  CB    . PHE B 1 65  ? 11.932  -0.530  39.879  1.00 32.29 ? 85   PHE B CB    1 
ATOM   6265  C  CG    . PHE B 1 65  ? 11.362  0.839   39.649  1.00 33.00 ? 85   PHE B CG    1 
ATOM   6266  C  CD1   . PHE B 1 65  ? 12.170  1.964   39.713  1.00 33.98 ? 85   PHE B CD1   1 
ATOM   6267  C  CD2   . PHE B 1 65  ? 10.012  1.004   39.336  1.00 33.52 ? 85   PHE B CD2   1 
ATOM   6268  C  CE1   . PHE B 1 65  ? 11.640  3.235   39.483  1.00 33.97 ? 85   PHE B CE1   1 
ATOM   6269  C  CE2   . PHE B 1 65  ? 9.478   2.268   39.101  1.00 33.63 ? 85   PHE B CE2   1 
ATOM   6270  C  CZ    . PHE B 1 65  ? 10.290  3.385   39.176  1.00 33.64 ? 85   PHE B CZ    1 
ATOM   6271  N  N     . LEU B 1 66  ? 10.547  -0.898  42.656  1.00 32.42 ? 86   LEU B N     1 
ATOM   6272  C  CA    . LEU B 1 66  ? 9.522   -0.430  43.587  1.00 32.39 ? 86   LEU B CA    1 
ATOM   6273  C  C     . LEU B 1 66  ? 9.954   -0.570  45.042  1.00 32.54 ? 86   LEU B C     1 
ATOM   6274  O  O     . LEU B 1 66  ? 9.750   0.338   45.844  1.00 32.19 ? 86   LEU B O     1 
ATOM   6275  C  CB    . LEU B 1 66  ? 8.215   -1.209  43.375  1.00 32.35 ? 86   LEU B CB    1 
ATOM   6276  C  CG    . LEU B 1 66  ? 7.499   -0.990  42.038  1.00 31.92 ? 86   LEU B CG    1 
ATOM   6277  C  CD1   . LEU B 1 66  ? 6.421   -2.036  41.849  1.00 32.39 ? 86   LEU B CD1   1 
ATOM   6278  C  CD2   . LEU B 1 66  ? 6.912   0.421   41.955  1.00 31.53 ? 86   LEU B CD2   1 
ATOM   6279  N  N     . ASP B 1 67  ? 10.536  -1.715  45.374  1.00 32.97 ? 87   ASP B N     1 
ATOM   6280  C  CA    . ASP B 1 67  ? 10.771  -2.090  46.759  1.00 33.56 ? 87   ASP B CA    1 
ATOM   6281  C  C     . ASP B 1 67  ? 12.210  -1.892  47.224  1.00 34.60 ? 87   ASP B C     1 
ATOM   6282  O  O     . ASP B 1 67  ? 12.435  -1.709  48.415  1.00 34.96 ? 87   ASP B O     1 
ATOM   6283  C  CB    . ASP B 1 67  ? 10.388  -3.553  46.976  1.00 33.30 ? 87   ASP B CB    1 
ATOM   6284  C  CG    . ASP B 1 67  ? 8.919   -3.834  46.677  1.00 32.73 ? 87   ASP B CG    1 
ATOM   6285  O  OD1   . ASP B 1 67  ? 8.137   -2.885  46.463  1.00 31.02 ? 87   ASP B OD1   1 
ATOM   6286  O  OD2   . ASP B 1 67  ? 8.542   -5.020  46.670  1.00 31.37 ? 87   ASP B OD2   1 
ATOM   6287  N  N     . LYS B 1 68  ? 13.178  -1.936  46.309  1.00 35.56 ? 88   LYS B N     1 
ATOM   6288  C  CA    . LYS B 1 68  ? 14.599  -1.921  46.700  1.00 36.25 ? 88   LYS B CA    1 
ATOM   6289  C  C     . LYS B 1 68  ? 15.372  -0.752  46.095  1.00 36.93 ? 88   LYS B C     1 
ATOM   6290  O  O     . LYS B 1 68  ? 16.600  -0.790  46.016  1.00 37.16 ? 88   LYS B O     1 
ATOM   6291  C  CB    . LYS B 1 68  ? 15.266  -3.246  46.319  1.00 36.37 ? 88   LYS B CB    1 
ATOM   6292  C  CG    . LYS B 1 68  ? 14.737  -4.439  47.089  1.00 36.32 ? 88   LYS B CG    1 
ATOM   6293  C  CD    . LYS B 1 68  ? 15.075  -5.741  46.385  1.00 37.56 ? 88   LYS B CD    1 
ATOM   6294  N  N     . GLY B 1 69  ? 14.645  0.280   45.672  1.00 37.53 ? 89   GLY B N     1 
ATOM   6295  C  CA    . GLY B 1 69  ? 15.246  1.513   45.179  1.00 38.07 ? 89   GLY B CA    1 
ATOM   6296  C  C     . GLY B 1 69  ? 16.195  1.385   43.999  1.00 38.44 ? 89   GLY B C     1 
ATOM   6297  O  O     . GLY B 1 69  ? 17.108  2.182   43.872  1.00 38.59 ? 89   GLY B O     1 
ATOM   6298  N  N     . GLU B 1 70  ? 15.977  0.396   43.134  1.00 39.02 ? 90   GLU B N     1 
ATOM   6299  C  CA    . GLU B 1 70  ? 16.853  0.165   41.973  1.00 39.26 ? 90   GLU B CA    1 
ATOM   6300  C  C     . GLU B 1 70  ? 16.357  0.926   40.743  1.00 38.95 ? 90   GLU B C     1 
ATOM   6301  O  O     . GLU B 1 70  ? 15.373  1.663   40.818  1.00 38.83 ? 90   GLU B O     1 
ATOM   6302  C  CB    . GLU B 1 70  ? 16.957  -1.330  41.662  1.00 39.48 ? 90   GLU B CB    1 
ATOM   6303  C  CG    . GLU B 1 70  ? 17.334  -2.158  42.868  1.00 41.35 ? 90   GLU B CG    1 
ATOM   6304  C  CD    . GLU B 1 70  ? 18.408  -3.165  42.568  1.00 43.76 ? 90   GLU B CD    1 
ATOM   6305  O  OE1   . GLU B 1 70  ? 18.116  -4.189  41.899  1.00 46.77 ? 90   GLU B OE1   1 
ATOM   6306  O  OE2   . GLU B 1 70  ? 19.551  -2.920  43.010  1.00 44.98 ? 90   GLU B OE2   1 
ATOM   6307  N  N     . ARG B 1 71  ? 17.050  0.750   39.619  1.00 38.52 ? 91   ARG B N     1 
ATOM   6308  C  CA    . ARG B 1 71  ? 16.752  1.492   38.397  1.00 38.28 ? 91   ARG B CA    1 
ATOM   6309  C  C     . ARG B 1 71  ? 15.339  1.205   37.875  1.00 38.05 ? 91   ARG B C     1 
ATOM   6310  O  O     . ARG B 1 71  ? 14.828  0.091   38.014  1.00 37.98 ? 91   ARG B O     1 
ATOM   6311  C  CB    . ARG B 1 71  ? 17.772  1.149   37.310  1.00 38.11 ? 91   ARG B CB    1 
ATOM   6312  N  N     . HIS B 1 72  ? 14.721  2.225   37.291  1.00 37.58 ? 92   HIS B N     1 
ATOM   6313  C  CA    . HIS B 1 72  ? 13.485  2.065   36.543  1.00 37.68 ? 92   HIS B CA    1 
ATOM   6314  C  C     . HIS B 1 72  ? 13.759  1.053   35.437  1.00 36.94 ? 92   HIS B C     1 
ATOM   6315  O  O     . HIS B 1 72  ? 14.758  1.176   34.729  1.00 36.87 ? 92   HIS B O     1 
ATOM   6316  C  CB    . HIS B 1 72  ? 13.057  3.405   35.938  1.00 37.87 ? 92   HIS B CB    1 
ATOM   6317  C  CG    . HIS B 1 72  ? 11.636  3.441   35.470  1.00 39.73 ? 92   HIS B CG    1 
ATOM   6318  N  ND1   . HIS B 1 72  ? 11.117  2.527   34.574  1.00 41.49 ? 92   HIS B ND1   1 
ATOM   6319  C  CD2   . HIS B 1 72  ? 10.630  4.305   35.749  1.00 41.28 ? 92   HIS B CD2   1 
ATOM   6320  C  CE1   . HIS B 1 72  ? 9.851   2.822   34.332  1.00 41.73 ? 92   HIS B CE1   1 
ATOM   6321  N  NE2   . HIS B 1 72  ? 9.529   3.892   35.036  1.00 41.80 ? 92   HIS B NE2   1 
ATOM   6322  N  N     . PRO B 1 73  ? 12.900  0.026   35.300  1.00 36.18 ? 93   PRO B N     1 
ATOM   6323  C  CA    . PRO B 1 73  ? 13.109  -0.932  34.210  1.00 35.61 ? 93   PRO B CA    1 
ATOM   6324  C  C     . PRO B 1 73  ? 12.996  -0.278  32.834  1.00 34.98 ? 93   PRO B C     1 
ATOM   6325  O  O     . PRO B 1 73  ? 12.451  0.825   32.718  1.00 34.59 ? 93   PRO B O     1 
ATOM   6326  C  CB    . PRO B 1 73  ? 11.991  -1.959  34.408  1.00 35.64 ? 93   PRO B CB    1 
ATOM   6327  C  CG    . PRO B 1 73  ? 11.516  -1.775  35.789  1.00 36.09 ? 93   PRO B CG    1 
ATOM   6328  C  CD    . PRO B 1 73  ? 11.764  -0.351  36.158  1.00 36.28 ? 93   PRO B CD    1 
ATOM   6329  N  N     . VAL B 1 74  ? 13.519  -0.950  31.811  1.00 34.44 ? 94   VAL B N     1 
ATOM   6330  C  CA    . VAL B 1 74  ? 13.410  -0.460  30.435  1.00 33.97 ? 94   VAL B CA    1 
ATOM   6331  C  C     . VAL B 1 74  ? 11.952  -0.517  29.987  1.00 33.34 ? 94   VAL B C     1 
ATOM   6332  O  O     . VAL B 1 74  ? 11.293  -1.538  30.132  1.00 33.50 ? 94   VAL B O     1 
ATOM   6333  C  CB    . VAL B 1 74  ? 14.265  -1.285  29.461  1.00 34.07 ? 94   VAL B CB    1 
ATOM   6334  C  CG1   . VAL B 1 74  ? 14.004  -0.852  28.014  1.00 34.28 ? 94   VAL B CG1   1 
ATOM   6335  C  CG2   . VAL B 1 74  ? 15.747  -1.142  29.804  1.00 34.25 ? 94   VAL B CG2   1 
ATOM   6336  N  N     . ARG B 1 75  ? 11.452  0.593   29.460  1.00 32.50 ? 95   ARG B N     1 
ATOM   6337  C  CA    . ARG B 1 75  ? 10.099  0.647   28.935  1.00 31.67 ? 95   ARG B CA    1 
ATOM   6338  C  C     . ARG B 1 75  ? 10.092  0.191   27.477  1.00 31.23 ? 95   ARG B C     1 
ATOM   6339  O  O     . ARG B 1 75  ? 10.921  0.643   26.676  1.00 31.05 ? 95   ARG B O     1 
ATOM   6340  C  CB    . ARG B 1 75  ? 9.558   2.062   29.055  1.00 31.54 ? 95   ARG B CB    1 
ATOM   6341  C  CG    . ARG B 1 75  ? 8.065   2.205   28.765  1.00 31.22 ? 95   ARG B CG    1 
ATOM   6342  C  CD    . ARG B 1 75  ? 7.615   3.552   29.262  1.00 30.95 ? 95   ARG B CD    1 
ATOM   6343  N  NE    . ARG B 1 75  ? 6.252   3.932   28.898  1.00 31.28 ? 95   ARG B NE    1 
ATOM   6344  C  CZ    . ARG B 1 75  ? 5.141   3.446   29.449  1.00 30.36 ? 95   ARG B CZ    1 
ATOM   6345  N  NH1   . ARG B 1 75  ? 5.189   2.483   30.370  1.00 28.98 ? 95   ARG B NH1   1 
ATOM   6346  N  NH2   . ARG B 1 75  ? 3.963   3.911   29.043  1.00 30.64 ? 95   ARG B NH2   1 
ATOM   6347  N  N     . GLU B 1 76  ? 9.166   -0.711  27.145  1.00 30.38 ? 96   GLU B N     1 
ATOM   6348  C  CA    . GLU B 1 76  ? 9.040   -1.245  25.784  1.00 30.04 ? 96   GLU B CA    1 
ATOM   6349  C  C     . GLU B 1 76  ? 7.600   -1.334  25.316  1.00 29.31 ? 96   GLU B C     1 
ATOM   6350  O  O     . GLU B 1 76  ? 6.658   -1.329  26.123  1.00 29.33 ? 96   GLU B O     1 
ATOM   6351  C  CB    . GLU B 1 76  ? 9.602   -2.658  25.712  1.00 30.38 ? 96   GLU B CB    1 
ATOM   6352  C  CG    . GLU B 1 76  ? 11.046  -2.794  26.058  1.00 31.06 ? 96   GLU B CG    1 
ATOM   6353  C  CD    . GLU B 1 76  ? 11.498  -4.231  25.973  1.00 32.89 ? 96   GLU B CD    1 
ATOM   6354  O  OE1   . GLU B 1 76  ? 10.791  -5.112  26.522  1.00 32.58 ? 96   GLU B OE1   1 
ATOM   6355  O  OE2   . GLU B 1 76  ? 12.555  -4.478  25.349  1.00 33.42 ? 96   GLU B OE2   1 
ATOM   6356  N  N     . ALA B 1 77  ? 7.448   -1.466  24.003  1.00 28.26 ? 97   ALA B N     1 
ATOM   6357  C  CA    . ALA B 1 77  ? 6.154   -1.722  23.380  1.00 27.48 ? 97   ALA B CA    1 
ATOM   6358  C  C     . ALA B 1 77  ? 6.136   -3.118  22.782  1.00 26.92 ? 97   ALA B C     1 
ATOM   6359  O  O     . ALA B 1 77  ? 7.168   -3.640  22.353  1.00 26.33 ? 97   ALA B O     1 
ATOM   6360  C  CB    . ALA B 1 77  ? 5.861   -0.674  22.303  1.00 27.00 ? 97   ALA B CB    1 
ATOM   6361  N  N     . ARG B 1 78  ? 4.954   -3.725  22.800  1.00 26.65 ? 98   ARG B N     1 
ATOM   6362  C  CA    . ARG B 1 78  ? 4.660   -4.938  22.042  1.00 26.11 ? 98   ARG B CA    1 
ATOM   6363  C  C     . ARG B 1 78  ? 4.089   -4.471  20.715  1.00 25.83 ? 98   ARG B C     1 
ATOM   6364  O  O     . ARG B 1 78  ? 3.168   -3.659  20.698  1.00 25.50 ? 98   ARG B O     1 
ATOM   6365  C  CB    . ARG B 1 78  ? 3.622   -5.785  22.778  1.00 26.14 ? 98   ARG B CB    1 
ATOM   6366  C  CG    . ARG B 1 78  ? 3.083   -6.989  22.008  1.00 25.74 ? 98   ARG B CG    1 
ATOM   6367  C  CD    . ARG B 1 78  ? 1.756   -7.444  22.574  1.00 25.57 ? 98   ARG B CD    1 
ATOM   6368  N  NE    . ARG B 1 78  ? 1.168   -8.550  21.828  1.00 26.09 ? 98   ARG B NE    1 
ATOM   6369  C  CZ    . ARG B 1 78  ? -0.058  -9.042  22.033  1.00 27.22 ? 98   ARG B CZ    1 
ATOM   6370  N  NH1   . ARG B 1 78  ? -0.860  -8.533  22.975  1.00 26.05 ? 98   ARG B NH1   1 
ATOM   6371  N  NH2   . ARG B 1 78  ? -0.490  -10.056 21.288  1.00 27.25 ? 98   ARG B NH2   1 
ATOM   6372  N  N     . ALA B 1 79  ? 4.642   -4.973  19.613  1.00 25.26 ? 99   ALA B N     1 
ATOM   6373  C  CA    . ALA B 1 79  ? 4.180   -4.613  18.283  1.00 24.71 ? 99   ALA B CA    1 
ATOM   6374  C  C     . ALA B 1 79  ? 3.882   -5.881  17.517  1.00 24.36 ? 99   ALA B C     1 
ATOM   6375  O  O     . ALA B 1 79  ? 4.761   -6.721  17.337  1.00 24.45 ? 99   ALA B O     1 
ATOM   6376  C  CB    . ALA B 1 79  ? 5.230   -3.790  17.557  1.00 25.00 ? 99   ALA B CB    1 
ATOM   6377  N  N     . VAL B 1 80  ? 2.634   -6.017  17.075  1.00 23.80 ? 100  VAL B N     1 
ATOM   6378  C  CA    . VAL B 1 80  ? 2.199   -7.181  16.319  1.00 23.02 ? 100  VAL B CA    1 
ATOM   6379  C  C     . VAL B 1 80  ? 2.169   -6.805  14.840  1.00 23.21 ? 100  VAL B C     1 
ATOM   6380  O  O     . VAL B 1 80  ? 1.452   -5.870  14.444  1.00 23.11 ? 100  VAL B O     1 
ATOM   6381  C  CB    . VAL B 1 80  ? 0.800   -7.627  16.761  1.00 22.82 ? 100  VAL B CB    1 
ATOM   6382  C  CG1   . VAL B 1 80  ? 0.355   -8.861  15.970  1.00 21.26 ? 100  VAL B CG1   1 
ATOM   6383  C  CG2   . VAL B 1 80  ? 0.783   -7.887  18.266  1.00 21.72 ? 100  VAL B CG2   1 
ATOM   6384  N  N     . ILE B 1 81  ? 2.955   -7.512  14.030  1.00 23.17 ? 101  ILE B N     1 
ATOM   6385  C  CA    . ILE B 1 81  ? 3.053   -7.194  12.601  1.00 23.11 ? 101  ILE B CA    1 
ATOM   6386  C  C     . ILE B 1 81  ? 2.490   -8.335  11.795  1.00 23.32 ? 101  ILE B C     1 
ATOM   6387  O  O     . ILE B 1 81  ? 2.899   -9.484  11.972  1.00 23.49 ? 101  ILE B O     1 
ATOM   6388  C  CB    . ILE B 1 81  ? 4.496   -6.916  12.147  1.00 23.42 ? 101  ILE B CB    1 
ATOM   6389  C  CG1   . ILE B 1 81  ? 5.084   -5.743  12.939  1.00 23.87 ? 101  ILE B CG1   1 
ATOM   6390  C  CG2   . ILE B 1 81  ? 4.528   -6.594  10.650  1.00 22.08 ? 101  ILE B CG2   1 
ATOM   6391  C  CD1   . ILE B 1 81  ? 6.499   -5.345  12.506  1.00 24.66 ? 101  ILE B CD1   1 
ATOM   6392  N  N     . PHE B 1 82  ? 1.519   -8.011  10.942  1.00 23.32 ? 102  PHE B N     1 
ATOM   6393  C  CA    . PHE B 1 82  ? 0.959   -8.943  9.978   1.00 23.43 ? 102  PHE B CA    1 
ATOM   6394  C  C     . PHE B 1 82  ? 1.880   -8.858  8.772   1.00 23.90 ? 102  PHE B C     1 
ATOM   6395  O  O     . PHE B 1 82  ? 1.924   -7.816  8.125   1.00 23.25 ? 102  PHE B O     1 
ATOM   6396  C  CB    . PHE B 1 82  ? -0.453  -8.495  9.545   1.00 23.22 ? 102  PHE B CB    1 
ATOM   6397  C  CG    . PHE B 1 82  ? -1.563  -8.781  10.547  1.00 23.56 ? 102  PHE B CG    1 
ATOM   6398  C  CD1   . PHE B 1 82  ? -1.311  -9.258  11.827  1.00 22.79 ? 102  PHE B CD1   1 
ATOM   6399  C  CD2   . PHE B 1 82  ? -2.884  -8.533  10.188  1.00 22.97 ? 102  PHE B CD2   1 
ATOM   6400  C  CE1   . PHE B 1 82  ? -2.354  -9.501  12.705  1.00 23.45 ? 102  PHE B CE1   1 
ATOM   6401  C  CE2   . PHE B 1 82  ? -3.933  -8.774  11.075  1.00 22.89 ? 102  PHE B CE2   1 
ATOM   6402  C  CZ    . PHE B 1 82  ? -3.675  -9.261  12.321  1.00 21.96 ? 102  PHE B CZ    1 
ATOM   6403  N  N     . PHE B 1 83  ? 2.610   -9.937  8.477   1.00 24.69 ? 103  PHE B N     1 
ATOM   6404  C  CA    . PHE B 1 83  ? 3.446   -10.015 7.267   1.00 25.19 ? 103  PHE B CA    1 
ATOM   6405  C  C     . PHE B 1 83  ? 2.708   -10.751 6.147   1.00 25.75 ? 103  PHE B C     1 
ATOM   6406  O  O     . PHE B 1 83  ? 2.923   -11.948 5.913   1.00 26.34 ? 103  PHE B O     1 
ATOM   6407  C  CB    . PHE B 1 83  ? 4.773   -10.721 7.551   1.00 25.06 ? 103  PHE B CB    1 
ATOM   6408  C  CG    . PHE B 1 83  ? 5.739   -9.904  8.364   1.00 26.16 ? 103  PHE B CG    1 
ATOM   6409  C  CD1   . PHE B 1 83  ? 6.052   -10.263 9.665   1.00 27.59 ? 103  PHE B CD1   1 
ATOM   6410  C  CD2   . PHE B 1 83  ? 6.330   -8.775  7.829   1.00 27.46 ? 103  PHE B CD2   1 
ATOM   6411  C  CE1   . PHE B 1 83  ? 6.946   -9.512  10.412  1.00 28.58 ? 103  PHE B CE1   1 
ATOM   6412  C  CE2   . PHE B 1 83  ? 7.225   -8.015  8.571   1.00 28.45 ? 103  PHE B CE2   1 
ATOM   6413  C  CZ    . PHE B 1 83  ? 7.533   -8.386  9.865   1.00 28.45 ? 103  PHE B CZ    1 
ATOM   6414  N  N     . GLY B 1 84  ? 1.843   -10.030 5.444   1.00 26.19 ? 104  GLY B N     1 
ATOM   6415  C  CA    . GLY B 1 84  ? 1.062   -10.607 4.358   1.00 26.53 ? 104  GLY B CA    1 
ATOM   6416  C  C     . GLY B 1 84  ? 1.700   -10.462 2.989   1.00 26.99 ? 104  GLY B C     1 
ATOM   6417  O  O     . GLY B 1 84  ? 1.273   -11.117 2.047   1.00 26.51 ? 104  GLY B O     1 
ATOM   6418  N  N     . ASP B 1 85  ? 2.709   -9.593  2.881   1.00 27.53 ? 105  ASP B N     1 
ATOM   6419  C  CA    . ASP B 1 85  ? 3.375   -9.298  1.603   1.00 27.91 ? 105  ASP B CA    1 
ATOM   6420  C  C     . ASP B 1 85  ? 4.634   -10.155 1.468   1.00 27.91 ? 105  ASP B C     1 
ATOM   6421  O  O     . ASP B 1 85  ? 5.751   -9.648  1.417   1.00 27.92 ? 105  ASP B O     1 
ATOM   6422  C  CB    . ASP B 1 85  ? 3.723   -7.801  1.547   1.00 28.42 ? 105  ASP B CB    1 
ATOM   6423  C  CG    . ASP B 1 85  ? 4.201   -7.346  0.180   1.00 29.30 ? 105  ASP B CG    1 
ATOM   6424  O  OD1   . ASP B 1 85  ? 4.052   -8.090  -0.804  1.00 30.40 ? 105  ASP B OD1   1 
ATOM   6425  O  OD2   . ASP B 1 85  ? 4.729   -6.219  0.098   1.00 31.27 ? 105  ASP B OD2   1 
ATOM   6426  N  N     . GLN B 1 86  ? 4.435   -11.465 1.445   1.00 27.98 ? 106  GLN B N     1 
ATOM   6427  C  CA    . GLN B 1 86  ? 5.518   -12.427 1.262   1.00 28.18 ? 106  GLN B CA    1 
ATOM   6428  C  C     . GLN B 1 86  ? 4.890   -13.752 0.869   1.00 28.30 ? 106  GLN B C     1 
ATOM   6429  O  O     . GLN B 1 86  ? 3.680   -13.928 1.031   1.00 28.52 ? 106  GLN B O     1 
ATOM   6430  C  CB    . GLN B 1 86  ? 6.365   -12.570 2.531   1.00 28.18 ? 106  GLN B CB    1 
ATOM   6431  C  CG    . GLN B 1 86  ? 5.574   -12.934 3.784   1.00 28.22 ? 106  GLN B CG    1 
ATOM   6432  C  CD    . GLN B 1 86  ? 6.369   -12.766 5.064   1.00 27.23 ? 106  GLN B CD    1 
ATOM   6433  O  OE1   . GLN B 1 86  ? 6.961   -11.714 5.307   1.00 28.14 ? 106  GLN B OE1   1 
ATOM   6434  N  NE2   . GLN B 1 86  ? 6.370   -13.798 5.905   1.00 26.14 ? 106  GLN B NE2   1 
ATOM   6435  N  N     . GLU B 1 87  ? 5.704   -14.661 0.331   1.00 28.10 ? 107  GLU B N     1 
ATOM   6436  C  CA    . GLU B 1 87  ? 5.224   -15.949 -0.169  1.00 27.88 ? 107  GLU B CA    1 
ATOM   6437  C  C     . GLU B 1 87  ? 4.498   -16.752 0.899   1.00 27.43 ? 107  GLU B C     1 
ATOM   6438  O  O     . GLU B 1 87  ? 3.476   -17.388 0.625   1.00 27.51 ? 107  GLU B O     1 
ATOM   6439  C  CB    . GLU B 1 87  ? 6.398   -16.785 -0.705  1.00 28.08 ? 107  GLU B CB    1 
ATOM   6440  N  N     . HIS B 1 88  ? 5.049   -16.735 2.107   1.00 27.15 ? 108  HIS B N     1 
ATOM   6441  C  CA    . HIS B 1 88  ? 4.505   -17.488 3.223   1.00 27.24 ? 108  HIS B CA    1 
ATOM   6442  C  C     . HIS B 1 88  ? 4.117   -16.502 4.334   1.00 26.59 ? 108  HIS B C     1 
ATOM   6443  O  O     . HIS B 1 88  ? 4.910   -16.219 5.239   1.00 25.97 ? 108  HIS B O     1 
ATOM   6444  C  CB    . HIS B 1 88  ? 5.523   -18.524 3.690   1.00 27.60 ? 108  HIS B CB    1 
ATOM   6445  C  CG    . HIS B 1 88  ? 5.884   -19.525 2.636   1.00 28.88 ? 108  HIS B CG    1 
ATOM   6446  N  ND1   . HIS B 1 88  ? 4.978   -20.427 2.125   1.00 31.15 ? 108  HIS B ND1   1 
ATOM   6447  C  CD2   . HIS B 1 88  ? 7.055   -19.766 1.998   1.00 31.16 ? 108  HIS B CD2   1 
ATOM   6448  C  CE1   . HIS B 1 88  ? 5.572   -21.175 1.212   1.00 31.95 ? 108  HIS B CE1   1 
ATOM   6449  N  NE2   . HIS B 1 88  ? 6.835   -20.799 1.121   1.00 31.05 ? 108  HIS B NE2   1 
ATOM   6450  N  N     . PRO B 1 89  ? 2.900   -15.940 4.236   1.00 25.93 ? 109  PRO B N     1 
ATOM   6451  C  CA    . PRO B 1 89  ? 2.450   -14.941 5.201   1.00 25.90 ? 109  PRO B CA    1 
ATOM   6452  C  C     . PRO B 1 89  ? 2.504   -15.431 6.633   1.00 25.28 ? 109  PRO B C     1 
ATOM   6453  O  O     . PRO B 1 89  ? 2.269   -16.610 6.881   1.00 25.23 ? 109  PRO B O     1 
ATOM   6454  C  CB    . PRO B 1 89  ? 0.995   -14.706 4.796   1.00 25.68 ? 109  PRO B CB    1 
ATOM   6455  C  CG    . PRO B 1 89  ? 0.978   -14.998 3.348   1.00 26.20 ? 109  PRO B CG    1 
ATOM   6456  C  CD    . PRO B 1 89  ? 1.904   -16.144 3.169   1.00 25.72 ? 109  PRO B CD    1 
ATOM   6457  N  N     . ASN B 1 90  ? 2.821   -14.536 7.562   1.00 25.01 ? 110  ASN B N     1 
ATOM   6458  C  CA    . ASN B 1 90  ? 2.718   -14.865 8.976   1.00 24.88 ? 110  ASN B CA    1 
ATOM   6459  C  C     . ASN B 1 90  ? 2.470   -13.647 9.843   1.00 24.25 ? 110  ASN B C     1 
ATOM   6460  O  O     . ASN B 1 90  ? 2.473   -12.518 9.351   1.00 24.53 ? 110  ASN B O     1 
ATOM   6461  C  CB    . ASN B 1 90  ? 3.944   -15.667 9.442   1.00 25.02 ? 110  ASN B CB    1 
ATOM   6462  C  CG    . ASN B 1 90  ? 5.169   -14.806 9.712   1.00 26.39 ? 110  ASN B CG    1 
ATOM   6463  O  OD1   . ASN B 1 90  ? 5.089   -13.784 10.396  1.00 26.59 ? 110  ASN B OD1   1 
ATOM   6464  N  ND2   . ASN B 1 90  ? 6.327   -15.238 9.187   1.00 28.07 ? 110  ASN B ND2   1 
ATOM   6465  N  N     . VAL B 1 91  ? 2.200   -13.887 11.121  1.00 23.46 ? 111  VAL B N     1 
ATOM   6466  C  CA    . VAL B 1 91  ? 2.190   -12.832 12.117  1.00 23.13 ? 111  VAL B CA    1 
ATOM   6467  C  C     . VAL B 1 91  ? 3.435   -13.031 12.973  1.00 23.14 ? 111  VAL B C     1 
ATOM   6468  O  O     . VAL B 1 91  ? 3.695   -14.141 13.405  1.00 22.88 ? 111  VAL B O     1 
ATOM   6469  C  CB    . VAL B 1 91  ? 0.948   -12.897 13.033  1.00 22.86 ? 111  VAL B CB    1 
ATOM   6470  C  CG1   . VAL B 1 91  ? 0.955   -11.732 14.009  1.00 22.69 ? 111  VAL B CG1   1 
ATOM   6471  C  CG2   . VAL B 1 91  ? -0.341  -12.897 12.222  1.00 22.99 ? 111  VAL B CG2   1 
ATOM   6472  N  N     . THR B 1 92  ? 4.200   -11.968 13.199  1.00 23.31 ? 112  THR B N     1 
ATOM   6473  C  CA    . THR B 1 92  ? 5.309   -11.997 14.164  1.00 23.72 ? 112  THR B CA    1 
ATOM   6474  C  C     . THR B 1 92  ? 5.189   -10.824 15.125  1.00 24.11 ? 112  THR B C     1 
ATOM   6475  O  O     . THR B 1 92  ? 4.839   -9.712  14.735  1.00 23.88 ? 112  THR B O     1 
ATOM   6476  C  CB    . THR B 1 92  ? 6.691   -11.947 13.469  1.00 23.78 ? 112  THR B CB    1 
ATOM   6477  O  OG1   . THR B 1 92  ? 6.766   -12.976 12.479  1.00 23.95 ? 112  THR B OG1   1 
ATOM   6478  C  CG2   . THR B 1 92  ? 7.822   -12.119 14.474  1.00 22.63 ? 112  THR B CG2   1 
ATOM   6479  N  N     . GLU B 1 93  ? 5.468   -11.087 16.392  1.00 24.95 ? 113  GLU B N     1 
ATOM   6480  C  CA    . GLU B 1 93  ? 5.426   -10.055 17.412  1.00 26.07 ? 113  GLU B CA    1 
ATOM   6481  C  C     . GLU B 1 93  ? 6.833   -9.638  17.776  1.00 26.71 ? 113  GLU B C     1 
ATOM   6482  O  O     . GLU B 1 93  ? 7.747   -10.469 17.796  1.00 26.27 ? 113  GLU B O     1 
ATOM   6483  C  CB    . GLU B 1 93  ? 4.750   -10.575 18.667  1.00 26.19 ? 113  GLU B CB    1 
ATOM   6484  C  CG    . GLU B 1 93  ? 3.382   -11.129 18.426  1.00 26.41 ? 113  GLU B CG    1 
ATOM   6485  C  CD    . GLU B 1 93  ? 2.478   -10.966 19.621  1.00 28.02 ? 113  GLU B CD    1 
ATOM   6486  O  OE1   . GLU B 1 93  ? 2.889   -10.338 20.620  1.00 27.97 ? 113  GLU B OE1   1 
ATOM   6487  O  OE2   . GLU B 1 93  ? 1.343   -11.464 19.561  1.00 29.77 ? 113  GLU B OE2   1 
ATOM   6488  N  N     . PHE B 1 94  ? 6.987   -8.356  18.094  1.00 27.44 ? 114  PHE B N     1 
ATOM   6489  C  CA    . PHE B 1 94  ? 8.272   -7.813  18.488  1.00 27.93 ? 114  PHE B CA    1 
ATOM   6490  C  C     . PHE B 1 94  ? 8.185   -6.998  19.769  1.00 28.31 ? 114  PHE B C     1 
ATOM   6491  O  O     . PHE B 1 94  ? 7.158   -6.394  20.073  1.00 28.39 ? 114  PHE B O     1 
ATOM   6492  C  CB    . PHE B 1 94  ? 8.811   -6.918  17.376  1.00 28.43 ? 114  PHE B CB    1 
ATOM   6493  C  CG    . PHE B 1 94  ? 8.948   -7.614  16.060  1.00 28.57 ? 114  PHE B CG    1 
ATOM   6494  C  CD1   . PHE B 1 94  ? 7.861   -7.717  15.203  1.00 30.03 ? 114  PHE B CD1   1 
ATOM   6495  C  CD2   . PHE B 1 94  ? 10.160  -8.166  15.680  1.00 29.59 ? 114  PHE B CD2   1 
ATOM   6496  C  CE1   . PHE B 1 94  ? 7.979   -8.369  13.975  1.00 30.63 ? 114  PHE B CE1   1 
ATOM   6497  C  CE2   . PHE B 1 94  ? 10.297  -8.816  14.450  1.00 30.47 ? 114  PHE B CE2   1 
ATOM   6498  C  CZ    . PHE B 1 94  ? 9.199   -8.920  13.598  1.00 30.67 ? 114  PHE B CZ    1 
ATOM   6499  N  N     . ALA B 1 95  ? 9.282   -6.986  20.512  1.00 28.63 ? 115  ALA B N     1 
ATOM   6500  C  CA    . ALA B 1 95  ? 9.479   -6.032  21.583  1.00 29.11 ? 115  ALA B CA    1 
ATOM   6501  C  C     . ALA B 1 95  ? 10.220  -4.848  20.956  1.00 29.50 ? 115  ALA B C     1 
ATOM   6502  O  O     . ALA B 1 95  ? 11.312  -5.023  20.408  1.00 29.79 ? 115  ALA B O     1 
ATOM   6503  C  CB    . ALA B 1 95  ? 10.296  -6.659  22.711  1.00 28.71 ? 115  ALA B CB    1 
ATOM   6504  N  N     . VAL B 1 96  ? 9.610   -3.666  20.997  1.00 29.86 ? 116  VAL B N     1 
ATOM   6505  C  CA    . VAL B 1 96  ? 10.222  -2.458  20.466  1.00 29.98 ? 116  VAL B CA    1 
ATOM   6506  C  C     . VAL B 1 96  ? 10.592  -1.550  21.630  1.00 30.96 ? 116  VAL B C     1 
ATOM   6507  O  O     . VAL B 1 96  ? 9.765   -1.278  22.515  1.00 30.56 ? 116  VAL B O     1 
ATOM   6508  C  CB    . VAL B 1 96  ? 9.285   -1.715  19.489  1.00 30.11 ? 116  VAL B CB    1 
ATOM   6509  C  CG1   . VAL B 1 96  ? 9.958   -0.459  18.943  1.00 28.59 ? 116  VAL B CG1   1 
ATOM   6510  C  CG2   . VAL B 1 96  ? 8.871   -2.640  18.342  1.00 29.06 ? 116  VAL B CG2   1 
ATOM   6511  N  N     . GLY B 1 97  ? 11.840  -1.091  21.632  1.00 31.74 ? 117  GLY B N     1 
ATOM   6512  C  CA    . GLY B 1 97  ? 12.357  -0.279  22.733  1.00 32.40 ? 117  GLY B CA    1 
ATOM   6513  C  C     . GLY B 1 97  ? 13.704  0.350   22.407  1.00 32.91 ? 117  GLY B C     1 
ATOM   6514  O  O     . GLY B 1 97  ? 14.246  0.118   21.331  1.00 33.04 ? 117  GLY B O     1 
ATOM   6515  N  N     . PRO B 1 98  ? 14.250  1.160   23.332  1.00 33.36 ? 118  PRO B N     1 
ATOM   6516  C  CA    . PRO B 1 98  ? 13.603  1.555   24.580  1.00 33.47 ? 118  PRO B CA    1 
ATOM   6517  C  C     . PRO B 1 98  ? 12.685  2.731   24.346  1.00 33.26 ? 118  PRO B C     1 
ATOM   6518  O  O     . PRO B 1 98  ? 12.612  3.244   23.233  1.00 33.47 ? 118  PRO B O     1 
ATOM   6519  C  CB    . PRO B 1 98  ? 14.782  1.957   25.474  1.00 33.59 ? 118  PRO B CB    1 
ATOM   6520  C  CG    . PRO B 1 98  ? 15.805  2.479   24.503  1.00 34.00 ? 118  PRO B CG    1 
ATOM   6521  C  CD    . PRO B 1 98  ? 15.626  1.688   23.230  1.00 33.45 ? 118  PRO B CD    1 
ATOM   6522  N  N     . LEU B 1 99  ? 11.975  3.144   25.387  1.00 33.42 ? 119  LEU B N     1 
ATOM   6523  C  CA    . LEU B 1 99  ? 11.114  4.312   25.316  1.00 33.52 ? 119  LEU B CA    1 
ATOM   6524  C  C     . LEU B 1 99  ? 11.499  5.244   26.453  1.00 33.75 ? 119  LEU B C     1 
ATOM   6525  O  O     . LEU B 1 99  ? 11.648  4.796   27.591  1.00 33.87 ? 119  LEU B O     1 
ATOM   6526  C  CB    . LEU B 1 99  ? 9.639   3.909   25.427  1.00 33.57 ? 119  LEU B CB    1 
ATOM   6527  C  CG    . LEU B 1 99  ? 9.073   3.083   24.263  1.00 33.92 ? 119  LEU B CG    1 
ATOM   6528  C  CD1   . LEU B 1 99  ? 7.695   2.485   24.606  1.00 32.98 ? 119  LEU B CD1   1 
ATOM   6529  C  CD2   . LEU B 1 99  ? 8.987   3.922   22.994  1.00 33.34 ? 119  LEU B CD2   1 
ATOM   6530  N  N     . PRO B 1 100 ? 11.694  6.538   26.159  1.00 34.20 ? 120  PRO B N     1 
ATOM   6531  C  CA    . PRO B 1 100 ? 11.666  7.160   24.835  1.00 34.56 ? 120  PRO B CA    1 
ATOM   6532  C  C     . PRO B 1 100 ? 12.891  6.804   23.977  1.00 34.92 ? 120  PRO B C     1 
ATOM   6533  O  O     . PRO B 1 100 ? 13.886  6.284   24.492  1.00 34.63 ? 120  PRO B O     1 
ATOM   6534  C  CB    . PRO B 1 100 ? 11.634  8.654   25.152  1.00 34.32 ? 120  PRO B CB    1 
ATOM   6535  C  CG    . PRO B 1 100 ? 12.284  8.774   26.477  1.00 34.52 ? 120  PRO B CG    1 
ATOM   6536  C  CD    . PRO B 1 100 ? 11.979  7.516   27.224  1.00 34.08 ? 120  PRO B CD    1 
ATOM   6537  N  N     . GLY B 1 101 ? 12.781  7.055   22.671  1.00 35.44 ? 121  GLY B N     1 
ATOM   6538  C  CA    . GLY B 1 101 ? 13.886  6.865   21.726  1.00 35.82 ? 121  GLY B CA    1 
ATOM   6539  C  C     . GLY B 1 101 ? 14.174  5.431   21.317  1.00 36.31 ? 121  GLY B C     1 
ATOM   6540  O  O     . GLY B 1 101 ? 15.276  4.930   21.561  1.00 36.72 ? 121  GLY B O     1 
ATOM   6541  N  N     . PRO B 1 102 ? 13.203  4.759   20.661  1.00 36.61 ? 122  PRO B N     1 
ATOM   6542  C  CA    . PRO B 1 102 ? 13.388  3.347   20.292  1.00 36.92 ? 122  PRO B CA    1 
ATOM   6543  C  C     . PRO B 1 102 ? 14.552  3.103   19.322  1.00 37.50 ? 122  PRO B C     1 
ATOM   6544  O  O     . PRO B 1 102 ? 14.753  3.887   18.398  1.00 37.40 ? 122  PRO B O     1 
ATOM   6545  C  CB    . PRO B 1 102 ? 12.049  2.963   19.638  1.00 36.72 ? 122  PRO B CB    1 
ATOM   6546  C  CG    . PRO B 1 102 ? 11.381  4.240   19.292  1.00 36.61 ? 122  PRO B CG    1 
ATOM   6547  C  CD    . PRO B 1 102 ? 11.903  5.293   20.215  1.00 36.38 ? 122  PRO B CD    1 
ATOM   6548  N  N     A CYS B 1 103 ? 15.303  2.027   19.571  0.70 38.07 ? 123  CYS B N     1 
ATOM   6549  N  N     B CYS B 1 103 ? 15.302  2.025   19.535  0.30 37.60 ? 123  CYS B N     1 
ATOM   6550  C  CA    A CYS B 1 103 ? 16.439  1.608   18.733  0.70 38.68 ? 123  CYS B CA    1 
ATOM   6551  C  CA    B CYS B 1 103 ? 16.388  1.661   18.619  0.30 37.75 ? 123  CYS B CA    1 
ATOM   6552  C  C     A CYS B 1 103 ? 16.265  0.224   18.140  0.70 38.64 ? 123  CYS B C     1 
ATOM   6553  C  C     B CYS B 1 103 ? 16.497  0.163   18.311  0.30 38.07 ? 123  CYS B C     1 
ATOM   6554  O  O     A CYS B 1 103 ? 16.719  -0.033  17.028  0.70 39.06 ? 123  CYS B O     1 
ATOM   6555  O  O     B CYS B 1 103 ? 17.398  -0.235  17.569  0.30 38.13 ? 123  CYS B O     1 
ATOM   6556  C  CB    A CYS B 1 103 ? 17.726  1.550   19.555  0.70 38.77 ? 123  CYS B CB    1 
ATOM   6557  C  CB    B CYS B 1 103 ? 17.731  2.176   19.155  0.30 37.69 ? 123  CYS B CB    1 
ATOM   6558  S  SG    A CYS B 1 103 ? 18.086  3.021   20.445  0.70 40.32 ? 123  CYS B SG    1 
ATOM   6559  S  SG    B CYS B 1 103 ? 18.496  1.129   20.418  0.30 36.86 ? 123  CYS B SG    1 
ATOM   6560  N  N     . TYR B 1 104 ? 15.626  -0.668  18.890  1.00 38.36 ? 124  TYR B N     1 
ATOM   6561  C  CA    . TYR B 1 104 ? 15.588  -2.085  18.544  1.00 38.58 ? 124  TYR B CA    1 
ATOM   6562  C  C     . TYR B 1 104 ? 14.170  -2.625  18.368  1.00 38.75 ? 124  TYR B C     1 
ATOM   6563  O  O     . TYR B 1 104 ? 13.167  -2.000  18.738  1.00 38.98 ? 124  TYR B O     1 
ATOM   6564  C  CB    . TYR B 1 104 ? 16.347  -2.928  19.580  1.00 38.50 ? 124  TYR B CB    1 
ATOM   6565  C  CG    . TYR B 1 104 ? 15.779  -2.866  20.980  1.00 39.02 ? 124  TYR B CG    1 
ATOM   6566  C  CD1   . TYR B 1 104 ? 14.743  -3.712  21.377  1.00 38.65 ? 124  TYR B CD1   1 
ATOM   6567  C  CD2   . TYR B 1 104 ? 16.285  -1.970  21.911  1.00 39.59 ? 124  TYR B CD2   1 
ATOM   6568  C  CE1   . TYR B 1 104 ? 14.225  -3.655  22.663  1.00 38.47 ? 124  TYR B CE1   1 
ATOM   6569  C  CE2   . TYR B 1 104 ? 15.774  -1.906  23.196  1.00 39.22 ? 124  TYR B CE2   1 
ATOM   6570  C  CZ    . TYR B 1 104 ? 14.748  -2.746  23.568  1.00 38.99 ? 124  TYR B CZ    1 
ATOM   6571  O  OH    . TYR B 1 104 ? 14.257  -2.663  24.853  1.00 39.41 ? 124  TYR B OH    1 
ATOM   6572  N  N     . MET B 1 105 ? 14.137  -3.818  17.800  1.00 38.79 ? 125  MET B N     1 
ATOM   6573  C  CA    . MET B 1 105 ? 12.932  -4.510  17.439  1.00 38.85 ? 125  MET B CA    1 
ATOM   6574  C  C     . MET B 1 105 ? 13.298  -5.984  17.568  1.00 38.38 ? 125  MET B C     1 
ATOM   6575  O  O     . MET B 1 105 ? 14.059  -6.495  16.756  1.00 38.60 ? 125  MET B O     1 
ATOM   6576  C  CB    . MET B 1 105 ? 12.600  -4.120  16.003  1.00 38.85 ? 125  MET B CB    1 
ATOM   6577  C  CG    . MET B 1 105 ? 11.462  -4.849  15.344  1.00 39.80 ? 125  MET B CG    1 
ATOM   6578  S  SD    . MET B 1 105 ? 11.266  -4.228  13.650  1.00 39.00 ? 125  MET B SD    1 
ATOM   6579  C  CE    . MET B 1 105 ? 9.984   -5.346  13.069  1.00 40.01 ? 125  MET B CE    1 
ATOM   6580  N  N     . ARG B 1 106 ? 12.802  -6.651  18.606  1.00 38.05 ? 126  ARG B N     1 
ATOM   6581  C  CA    . ARG B 1 106 ? 13.186  -8.042  18.888  1.00 37.94 ? 126  ARG B CA    1 
ATOM   6582  C  C     . ARG B 1 106 ? 11.987  -8.988  18.807  1.00 38.02 ? 126  ARG B C     1 
ATOM   6583  O  O     . ARG B 1 106 ? 11.006  -8.806  19.518  1.00 37.76 ? 126  ARG B O     1 
ATOM   6584  C  CB    . ARG B 1 106 ? 13.829  -8.145  20.274  1.00 37.74 ? 126  ARG B CB    1 
ATOM   6585  N  N     . ALA B 1 107 ? 12.088  -10.002 17.947  1.00 37.99 ? 127  ALA B N     1 
ATOM   6586  C  CA    . ALA B 1 107 ? 11.026  -10.990 17.757  1.00 38.05 ? 127  ALA B CA    1 
ATOM   6587  C  C     . ALA B 1 107 ? 10.717  -11.759 19.045  1.00 38.05 ? 127  ALA B C     1 
ATOM   6588  O  O     . ALA B 1 107 ? 11.619  -12.087 19.805  1.00 37.98 ? 127  ALA B O     1 
ATOM   6589  C  CB    . ALA B 1 107 ? 11.413  -11.959 16.651  1.00 37.93 ? 127  ALA B CB    1 
ATOM   6590  N  N     . LEU B 1 108 ? 9.438   -12.053 19.266  1.00 38.12 ? 128  LEU B N     1 
ATOM   6591  C  CA    . LEU B 1 108 ? 8.980   -12.701 20.487  1.00 38.07 ? 128  LEU B CA    1 
ATOM   6592  C  C     . LEU B 1 108 ? 8.390   -14.072 20.197  1.00 38.43 ? 128  LEU B C     1 
ATOM   6593  O  O     . LEU B 1 108 ? 7.969   -14.346 19.073  1.00 38.81 ? 128  LEU B O     1 
ATOM   6594  C  CB    . LEU B 1 108 ? 7.915   -11.843 21.163  1.00 37.83 ? 128  LEU B CB    1 
ATOM   6595  C  CG    . LEU B 1 108 ? 8.324   -10.413 21.517  1.00 37.89 ? 128  LEU B CG    1 
ATOM   6596  C  CD1   . LEU B 1 108 ? 7.161   -9.651  22.158  1.00 37.87 ? 128  LEU B CD1   1 
ATOM   6597  C  CD2   . LEU B 1 108 ? 9.533   -10.422 22.438  1.00 38.05 ? 128  LEU B CD2   1 
ATOM   6598  N  N     . SER B 1 109 ? 8.395   -14.928 21.219  1.00 38.58 ? 129  SER B N     1 
ATOM   6599  C  CA    . SER B 1 109 ? 7.627   -16.188 21.250  1.00 38.62 ? 129  SER B CA    1 
ATOM   6600  C  C     . SER B 1 109 ? 7.525   -16.983 19.931  1.00 38.34 ? 129  SER B C     1 
ATOM   6601  O  O     . SER B 1 109 ? 6.428   -17.158 19.396  1.00 38.72 ? 129  SER B O     1 
ATOM   6602  C  CB    . SER B 1 109 ? 6.210   -15.905 21.784  1.00 38.60 ? 129  SER B CB    1 
ATOM   6603  N  N     . PRO B 1 110 ? 8.659   -17.498 19.422  1.00 37.65 ? 130  PRO B N     1 
ATOM   6604  C  CA    . PRO B 1 110 ? 8.617   -18.411 18.264  1.00 37.04 ? 130  PRO B CA    1 
ATOM   6605  C  C     . PRO B 1 110 ? 7.876   -19.721 18.559  1.00 36.19 ? 130  PRO B C     1 
ATOM   6606  O  O     . PRO B 1 110 ? 7.879   -20.175 19.698  1.00 36.62 ? 130  PRO B O     1 
ATOM   6607  C  CB    . PRO B 1 110 ? 10.097  -18.697 17.990  1.00 37.31 ? 130  PRO B CB    1 
ATOM   6608  C  CG    . PRO B 1 110 ? 10.814  -18.336 19.271  1.00 37.55 ? 130  PRO B CG    1 
ATOM   6609  C  CD    . PRO B 1 110 ? 10.038  -17.213 19.855  1.00 37.78 ? 130  PRO B CD    1 
ATOM   6610  N  N     . ARG B 1 111 ? 7.244   -20.309 17.544  1.00 34.93 ? 131  ARG B N     1 
ATOM   6611  C  CA    . ARG B 1 111 ? 6.589   -21.621 17.664  1.00 33.83 ? 131  ARG B CA    1 
ATOM   6612  C  C     . ARG B 1 111 ? 7.092   -22.558 16.556  1.00 33.01 ? 131  ARG B C     1 
ATOM   6613  O  O     . ARG B 1 111 ? 6.439   -22.689 15.528  1.00 32.34 ? 131  ARG B O     1 
ATOM   6614  C  CB    . ARG B 1 111 ? 5.059   -21.497 17.549  1.00 33.54 ? 131  ARG B CB    1 
ATOM   6615  C  CG    . ARG B 1 111 ? 4.358   -20.845 18.727  1.00 33.11 ? 131  ARG B CG    1 
ATOM   6616  C  CD    . ARG B 1 111 ? 2.830   -20.892 18.551  1.00 32.29 ? 131  ARG B CD    1 
ATOM   6617  N  NE    . ARG B 1 111 ? 2.301   -22.246 18.709  1.00 31.62 ? 131  ARG B NE    1 
ATOM   6618  C  CZ    . ARG B 1 111 ? 1.027   -22.603 18.532  1.00 31.35 ? 131  ARG B CZ    1 
ATOM   6619  N  NH1   . ARG B 1 111 ? 0.105   -21.714 18.187  1.00 31.90 ? 131  ARG B NH1   1 
ATOM   6620  N  NH2   . ARG B 1 111 ? 0.667   -23.866 18.706  1.00 31.45 ? 131  ARG B NH2   1 
ATOM   6621  N  N     . PRO B 1 112 ? 8.247   -23.219 16.765  1.00 32.40 ? 132  PRO B N     1 
ATOM   6622  C  CA    . PRO B 1 112 ? 8.768   -24.124 15.732  1.00 31.96 ? 132  PRO B CA    1 
ATOM   6623  C  C     . PRO B 1 112 ? 7.774   -25.220 15.370  1.00 31.39 ? 132  PRO B C     1 
ATOM   6624  O  O     . PRO B 1 112 ? 7.242   -25.886 16.256  1.00 31.51 ? 132  PRO B O     1 
ATOM   6625  C  CB    . PRO B 1 112 ? 10.018  -24.734 16.387  1.00 31.97 ? 132  PRO B CB    1 
ATOM   6626  C  CG    . PRO B 1 112 ? 10.431  -23.744 17.415  1.00 32.31 ? 132  PRO B CG    1 
ATOM   6627  C  CD    . PRO B 1 112 ? 9.148   -23.142 17.930  1.00 32.51 ? 132  PRO B CD    1 
ATOM   6628  N  N     . GLY B 1 113 ? 7.522   -25.399 14.081  1.00 30.85 ? 133  GLY B N     1 
ATOM   6629  C  CA    . GLY B 1 113 ? 6.579   -26.417 13.618  1.00 30.52 ? 133  GLY B CA    1 
ATOM   6630  C  C     . GLY B 1 113 ? 5.142   -25.952 13.436  1.00 30.33 ? 133  GLY B C     1 
ATOM   6631  O  O     . GLY B 1 113 ? 4.353   -26.646 12.811  1.00 30.53 ? 133  GLY B O     1 
ATOM   6632  N  N     . TYR B 1 114 ? 4.786   -24.792 13.986  1.00 30.27 ? 134  TYR B N     1 
ATOM   6633  C  CA    . TYR B 1 114 ? 3.424   -24.272 13.865  1.00 30.19 ? 134  TYR B CA    1 
ATOM   6634  C  C     . TYR B 1 114 ? 3.271   -23.531 12.547  1.00 29.94 ? 134  TYR B C     1 
ATOM   6635  O  O     . TYR B 1 114 ? 4.026   -22.611 12.269  1.00 29.91 ? 134  TYR B O     1 
ATOM   6636  C  CB    . TYR B 1 114 ? 3.100   -23.331 15.025  1.00 30.40 ? 134  TYR B CB    1 
ATOM   6637  C  CG    . TYR B 1 114 ? 1.706   -22.743 14.976  1.00 29.58 ? 134  TYR B CG    1 
ATOM   6638  C  CD1   . TYR B 1 114 ? 1.510   -21.370 14.860  1.00 28.80 ? 134  TYR B CD1   1 
ATOM   6639  C  CD2   . TYR B 1 114 ? 0.584   -23.557 15.044  1.00 29.43 ? 134  TYR B CD2   1 
ATOM   6640  C  CE1   . TYR B 1 114 ? 0.222   -20.820 14.814  1.00 27.59 ? 134  TYR B CE1   1 
ATOM   6641  C  CE2   . TYR B 1 114 ? -0.707  -23.015 15.006  1.00 28.65 ? 134  TYR B CE2   1 
ATOM   6642  C  CZ    . TYR B 1 114 ? -0.875  -21.641 14.891  1.00 27.47 ? 134  TYR B CZ    1 
ATOM   6643  O  OH    . TYR B 1 114 ? -2.140  -21.095 14.845  1.00 24.78 ? 134  TYR B OH    1 
ATOM   6644  N  N     . GLN B 1 115 ? 2.280   -23.923 11.753  1.00 29.89 ? 135  GLN B N     1 
ATOM   6645  C  CA    . GLN B 1 115 ? 2.131   -23.409 10.392  1.00 30.22 ? 135  GLN B CA    1 
ATOM   6646  C  C     . GLN B 1 115 ? 0.898   -22.518 10.170  1.00 30.09 ? 135  GLN B C     1 
ATOM   6647  O  O     . GLN B 1 115 ? 0.752   -21.962 9.084   1.00 30.46 ? 135  GLN B O     1 
ATOM   6648  C  CB    . GLN B 1 115 ? 2.122   -24.585 9.403   1.00 30.58 ? 135  GLN B CB    1 
ATOM   6649  C  CG    . GLN B 1 115 ? 3.359   -25.456 9.542   1.00 31.90 ? 135  GLN B CG    1 
ATOM   6650  C  CD    . GLN B 1 115 ? 3.390   -26.653 8.621   1.00 34.53 ? 135  GLN B CD    1 
ATOM   6651  O  OE1   . GLN B 1 115 ? 2.414   -26.974 7.945   1.00 36.92 ? 135  GLN B OE1   1 
ATOM   6652  N  NE2   . GLN B 1 115 ? 4.528   -27.339 8.603   1.00 35.82 ? 135  GLN B NE2   1 
ATOM   6653  N  N     . SER B 1 116 ? 0.052   -22.341 11.191  1.00 29.27 ? 136  SER B N     1 
ATOM   6654  C  CA    . SER B 1 116 ? -1.256  -21.682 11.006  1.00 28.81 ? 136  SER B CA    1 
ATOM   6655  C  C     . SER B 1 116 ? -1.307  -20.235 11.496  1.00 28.38 ? 136  SER B C     1 
ATOM   6656  O  O     . SER B 1 116 ? -2.392  -19.669 11.679  1.00 28.44 ? 136  SER B O     1 
ATOM   6657  C  CB    . SER B 1 116 ? -2.356  -22.496 11.685  1.00 28.61 ? 136  SER B CB    1 
ATOM   6658  O  OG    . SER B 1 116 ? -2.537  -23.730 11.026  1.00 28.21 ? 136  SER B OG    1 
ATOM   6659  N  N     . SER B 1 117 ? -0.133  -19.637 11.681  1.00 27.31 ? 137  SER B N     1 
ATOM   6660  C  CA    . SER B 1 117 ? -0.009  -18.266 12.165  1.00 26.80 ? 137  SER B CA    1 
ATOM   6661  C  C     . SER B 1 117 ? -0.941  -17.272 11.460  1.00 26.37 ? 137  SER B C     1 
ATOM   6662  O  O     . SER B 1 117 ? -1.645  -16.495 12.101  1.00 25.97 ? 137  SER B O     1 
ATOM   6663  C  CB    . SER B 1 117 ? 1.439   -17.806 11.991  1.00 26.71 ? 137  SER B CB    1 
ATOM   6664  O  OG    . SER B 1 117 ? 1.561   -16.435 12.227  1.00 26.73 ? 137  SER B OG    1 
ATOM   6665  N  N     . TRP B 1 118 ? -0.928  -17.296 10.135  1.00 25.71 ? 138  TRP B N     1 
ATOM   6666  C  CA    . TRP B 1 118 ? -1.689  -16.331 9.363   1.00 25.21 ? 138  TRP B CA    1 
ATOM   6667  C  C     . TRP B 1 118 ? -3.194  -16.570 9.540   1.00 25.12 ? 138  TRP B C     1 
ATOM   6668  O  O     . TRP B 1 118 ? -3.965  -15.623 9.678   1.00 25.27 ? 138  TRP B O     1 
ATOM   6669  C  CB    . TRP B 1 118 ? -1.296  -16.412 7.888   1.00 25.11 ? 138  TRP B CB    1 
ATOM   6670  C  CG    . TRP B 1 118 ? -1.834  -15.294 7.040   1.00 24.80 ? 138  TRP B CG    1 
ATOM   6671  C  CD1   . TRP B 1 118 ? -2.738  -15.398 6.024   1.00 23.62 ? 138  TRP B CD1   1 
ATOM   6672  C  CD2   . TRP B 1 118 ? -1.477  -13.912 7.123   1.00 24.02 ? 138  TRP B CD2   1 
ATOM   6673  N  NE1   . TRP B 1 118 ? -2.964  -14.168 5.468   1.00 24.99 ? 138  TRP B NE1   1 
ATOM   6674  C  CE2   . TRP B 1 118 ? -2.207  -13.235 6.129   1.00 24.25 ? 138  TRP B CE2   1 
ATOM   6675  C  CE3   . TRP B 1 118 ? -0.609  -13.180 7.942   1.00 24.78 ? 138  TRP B CE3   1 
ATOM   6676  C  CZ2   . TRP B 1 118 ? -2.110  -11.858 5.939   1.00 24.61 ? 138  TRP B CZ2   1 
ATOM   6677  C  CZ3   . TRP B 1 118 ? -0.517  -11.808 7.757   1.00 25.19 ? 138  TRP B CZ3   1 
ATOM   6678  C  CH2   . TRP B 1 118 ? -1.255  -11.164 6.754   1.00 25.16 ? 138  TRP B CH2   1 
ATOM   6679  N  N     . ALA B 1 119 ? -3.596  -17.837 9.550   1.00 24.78 ? 139  ALA B N     1 
ATOM   6680  C  CA    . ALA B 1 119 ? -4.995  -18.211 9.736   1.00 24.46 ? 139  ALA B CA    1 
ATOM   6681  C  C     . ALA B 1 119 ? -5.508  -17.789 11.108  1.00 24.15 ? 139  ALA B C     1 
ATOM   6682  O  O     . ALA B 1 119 ? -6.696  -17.500 11.273  1.00 23.69 ? 139  ALA B O     1 
ATOM   6683  C  CB    . ALA B 1 119 ? -5.152  -19.698 9.568   1.00 24.32 ? 139  ALA B CB    1 
ATOM   6684  N  N     . SER B 1 120 ? -4.595  -17.760 12.079  1.00 23.95 ? 140  SER B N     1 
ATOM   6685  C  CA    . SER B 1 120 ? -4.925  -17.494 13.479  1.00 23.77 ? 140  SER B CA    1 
ATOM   6686  C  C     . SER B 1 120 ? -5.182  -16.024 13.739  1.00 23.76 ? 140  SER B C     1 
ATOM   6687  O  O     . SER B 1 120 ? -5.748  -15.669 14.771  1.00 24.00 ? 140  SER B O     1 
ATOM   6688  C  CB    . SER B 1 120 ? -3.778  -17.953 14.402  1.00 23.65 ? 140  SER B CB    1 
ATOM   6689  O  OG    . SER B 1 120 ? -2.714  -16.999 14.428  1.00 22.87 ? 140  SER B OG    1 
ATOM   6690  N  N     . ARG B 1 121 ? -4.742  -15.166 12.822  1.00 23.63 ? 141  ARG B N     1 
ATOM   6691  C  CA    . ARG B 1 121 ? -4.750  -13.732 13.073  1.00 23.33 ? 141  ARG B CA    1 
ATOM   6692  C  C     . ARG B 1 121 ? -6.183  -13.193 13.123  1.00 23.10 ? 141  ARG B C     1 
ATOM   6693  O  O     . ARG B 1 121 ? -7.086  -13.745 12.474  1.00 22.83 ? 141  ARG B O     1 
ATOM   6694  C  CB    . ARG B 1 121 ? -3.925  -12.992 12.010  1.00 23.65 ? 141  ARG B CB    1 
ATOM   6695  C  CG    . ARG B 1 121 ? -4.693  -12.703 10.714  1.00 23.81 ? 141  ARG B CG    1 
ATOM   6696  C  CD    . ARG B 1 121 ? -3.780  -12.274 9.581   1.00 23.57 ? 141  ARG B CD    1 
ATOM   6697  N  NE    . ARG B 1 121 ? -4.564  -11.855 8.421   1.00 22.87 ? 141  ARG B NE    1 
ATOM   6698  C  CZ    . ARG B 1 121 ? -5.204  -12.674 7.589   1.00 23.10 ? 141  ARG B CZ    1 
ATOM   6699  N  NH1   . ARG B 1 121 ? -5.158  -13.994 7.746   1.00 23.00 ? 141  ARG B NH1   1 
ATOM   6700  N  NH2   . ARG B 1 121 ? -5.895  -12.165 6.576   1.00 23.90 ? 141  ARG B NH2   1 
ATOM   6701  N  N     . PRO B 1 122 ? -6.400  -12.124 13.907  1.00 22.99 ? 142  PRO B N     1 
ATOM   6702  C  CA    . PRO B 1 122 ? -7.719  -11.489 13.959  1.00 22.76 ? 142  PRO B CA    1 
ATOM   6703  C  C     . PRO B 1 122 ? -8.203  -10.918 12.622  1.00 22.93 ? 142  PRO B C     1 
ATOM   6704  O  O     . PRO B 1 122 ? -7.396  -10.590 11.735  1.00 22.51 ? 142  PRO B O     1 
ATOM   6705  C  CB    . PRO B 1 122 ? -7.521  -10.355 14.963  1.00 22.97 ? 142  PRO B CB    1 
ATOM   6706  C  CG    . PRO B 1 122 ? -6.424  -10.830 15.855  1.00 23.05 ? 142  PRO B CG    1 
ATOM   6707  C  CD    . PRO B 1 122 ? -5.501  -11.605 14.958  1.00 22.64 ? 142  PRO B CD    1 
ATOM   6708  N  N     . ILE B 1 123 ? -9.523  -10.795 12.496  1.00 22.58 ? 143  ILE B N     1 
ATOM   6709  C  CA    . ILE B 1 123 ? -10.124 -10.113 11.356  1.00 22.54 ? 143  ILE B CA    1 
ATOM   6710  C  C     . ILE B 1 123 ? -9.828  -8.617  11.475  1.00 23.09 ? 143  ILE B C     1 
ATOM   6711  O  O     . ILE B 1 123 ? -9.409  -8.143  12.542  1.00 24.00 ? 143  ILE B O     1 
ATOM   6712  C  CB    . ILE B 1 123 ? -11.643 -10.445 11.251  1.00 22.41 ? 143  ILE B CB    1 
ATOM   6713  C  CG1   . ILE B 1 123 ? -12.184 -10.135 9.852   1.00 21.82 ? 143  ILE B CG1   1 
ATOM   6714  C  CG2   . ILE B 1 123 ? -12.447 -9.746  12.356  1.00 20.84 ? 143  ILE B CG2   1 
ATOM   6715  C  CD1   . ILE B 1 123 ? -13.335 -11.026 9.455   1.00 22.45 ? 143  ILE B CD1   1 
ATOM   6716  N  N     . SER B 1 124 ? -9.981  -7.891  10.374  1.00 23.47 ? 144  SER B N     1 
ATOM   6717  C  CA    . SER B 1 124 ? -9.648  -6.469  10.303  1.00 23.91 ? 144  SER B CA    1 
ATOM   6718  C  C     . SER B 1 124 ? -10.656 -5.707  9.444   1.00 24.26 ? 144  SER B C     1 
ATOM   6719  O  O     . SER B 1 124 ? -11.435 -6.292  8.697   1.00 24.54 ? 144  SER B O     1 
ATOM   6720  C  CB    . SER B 1 124 ? -8.246  -6.267  9.720   1.00 24.22 ? 144  SER B CB    1 
ATOM   6721  O  OG    . SER B 1 124 ? -8.196  -6.667  8.364   1.00 24.40 ? 144  SER B OG    1 
ATOM   6722  N  N     . THR B 1 125 ? -10.638 -4.391  9.570   1.00 24.57 ? 145  THR B N     1 
ATOM   6723  C  CA    . THR B 1 125 ? -11.487 -3.537  8.761   1.00 24.91 ? 145  THR B CA    1 
ATOM   6724  C  C     . THR B 1 125 ? -11.308 -3.835  7.272   1.00 24.61 ? 145  THR B C     1 
ATOM   6725  O  O     . THR B 1 125 ? -12.287 -4.052  6.556   1.00 24.61 ? 145  THR B O     1 
ATOM   6726  C  CB    . THR B 1 125 ? -11.223 -2.059  9.093   1.00 25.14 ? 145  THR B CB    1 
ATOM   6727  O  OG1   . THR B 1 125 ? -11.634 -1.816  10.450  1.00 25.61 ? 145  THR B OG1   1 
ATOM   6728  C  CG2   . THR B 1 125 ? -12.001 -1.130  8.157   1.00 25.92 ? 145  THR B CG2   1 
ATOM   6729  N  N     . ALA B 1 126 ? -10.062 -3.902  6.822   1.00 24.09 ? 146  ALA B N     1 
ATOM   6730  C  CA    . ALA B 1 126 ? -9.778  -4.175  5.416   1.00 24.00 ? 146  ALA B CA    1 
ATOM   6731  C  C     . ALA B 1 126 ? -10.321 -5.534  4.979   1.00 23.85 ? 146  ALA B C     1 
ATOM   6732  O  O     . ALA B 1 126 ? -10.811 -5.680  3.857   1.00 23.90 ? 146  ALA B O     1 
ATOM   6733  C  CB    . ALA B 1 126 ? -8.275  -4.071  5.139   1.00 23.86 ? 146  ALA B CB    1 
ATOM   6734  N  N     . GLU B 1 127 ? -10.258 -6.527  5.862   1.00 23.94 ? 147  GLU B N     1 
ATOM   6735  C  CA    . GLU B 1 127 ? -10.760 -7.853  5.524   1.00 23.88 ? 147  GLU B CA    1 
ATOM   6736  C  C     . GLU B 1 127 ? -12.284 -7.819  5.387   1.00 24.30 ? 147  GLU B C     1 
ATOM   6737  O  O     . GLU B 1 127 ? -12.843 -8.460  4.487   1.00 24.57 ? 147  GLU B O     1 
ATOM   6738  C  CB    . GLU B 1 127 ? -10.323 -8.884  6.559   1.00 23.98 ? 147  GLU B CB    1 
ATOM   6739  C  CG    . GLU B 1 127 ? -10.588 -10.306 6.114   1.00 23.50 ? 147  GLU B CG    1 
ATOM   6740  C  CD    . GLU B 1 127 ? -9.831  -11.327 6.907   1.00 22.75 ? 147  GLU B CD    1 
ATOM   6741  O  OE1   . GLU B 1 127 ? -9.266  -10.986 7.968   1.00 23.85 ? 147  GLU B OE1   1 
ATOM   6742  O  OE2   . GLU B 1 127 ? -9.808  -12.486 6.467   1.00 21.39 ? 147  GLU B OE2   1 
ATOM   6743  N  N     . TYR B 1 128 ? -12.937 -7.036  6.248   1.00 24.26 ? 148  TYR B N     1 
ATOM   6744  C  CA    . TYR B 1 128 ? -14.386 -6.813  6.167   1.00 24.58 ? 148  TYR B CA    1 
ATOM   6745  C  C     . TYR B 1 128 ? -14.839 -6.133  4.877   1.00 24.92 ? 148  TYR B C     1 
ATOM   6746  O  O     . TYR B 1 128 ? -15.817 -6.564  4.255   1.00 25.03 ? 148  TYR B O     1 
ATOM   6747  C  CB    . TYR B 1 128 ? -14.873 -5.989  7.361   1.00 24.44 ? 148  TYR B CB    1 
ATOM   6748  C  CG    . TYR B 1 128 ? -15.089 -6.792  8.619   1.00 24.64 ? 148  TYR B CG    1 
ATOM   6749  C  CD1   . TYR B 1 128 ? -15.910 -7.910  8.610   1.00 25.52 ? 148  TYR B CD1   1 
ATOM   6750  C  CD2   . TYR B 1 128 ? -14.517 -6.408  9.832   1.00 25.08 ? 148  TYR B CD2   1 
ATOM   6751  C  CE1   . TYR B 1 128 ? -16.136 -8.650  9.759   1.00 24.84 ? 148  TYR B CE1   1 
ATOM   6752  C  CE2   . TYR B 1 128 ? -14.738 -7.143  10.991  1.00 24.90 ? 148  TYR B CE2   1 
ATOM   6753  C  CZ    . TYR B 1 128 ? -15.560 -8.268  10.940  1.00 24.77 ? 148  TYR B CZ    1 
ATOM   6754  O  OH    . TYR B 1 128 ? -15.811 -9.021  12.060  1.00 21.16 ? 148  TYR B OH    1 
ATOM   6755  N  N     . ALA B 1 129 ? -14.144 -5.071  4.476   1.00 25.26 ? 149  ALA B N     1 
ATOM   6756  C  CA    . ALA B 1 129 ? -14.430 -4.414  3.196   1.00 25.74 ? 149  ALA B CA    1 
ATOM   6757  C  C     . ALA B 1 129 ? -14.330 -5.409  2.033   1.00 26.21 ? 149  ALA B C     1 
ATOM   6758  O  O     . ALA B 1 129 ? -15.141 -5.375  1.106   1.00 26.71 ? 149  ALA B O     1 
ATOM   6759  C  CB    . ALA B 1 129 ? -13.492 -3.219  2.966   1.00 25.64 ? 149  ALA B CB    1 
ATOM   6760  N  N     . LEU B 1 130 ? -13.355 -6.309  2.098   1.00 26.35 ? 150  LEU B N     1 
ATOM   6761  C  CA    . LEU B 1 130 ? -13.185 -7.307  1.051   1.00 26.67 ? 150  LEU B CA    1 
ATOM   6762  C  C     . LEU B 1 130 ? -14.260 -8.396  1.130   1.00 26.75 ? 150  LEU B C     1 
ATOM   6763  O  O     . LEU B 1 130 ? -14.774 -8.840  0.108   1.00 26.41 ? 150  LEU B O     1 
ATOM   6764  C  CB    . LEU B 1 130 ? -11.780 -7.897  1.103   1.00 26.42 ? 150  LEU B CB    1 
ATOM   6765  C  CG    . LEU B 1 130 ? -10.684 -6.906  0.693   1.00 26.99 ? 150  LEU B CG    1 
ATOM   6766  C  CD1   . LEU B 1 130 ? -9.286  -7.397  1.103   1.00 27.64 ? 150  LEU B CD1   1 
ATOM   6767  C  CD2   . LEU B 1 130 ? -10.734 -6.640  -0.815  1.00 25.91 ? 150  LEU B CD2   1 
ATOM   6768  N  N     . LEU B 1 131 ? -14.602 -8.821  2.341   1.00 27.47 ? 151  LEU B N     1 
ATOM   6769  C  CA    . LEU B 1 131 ? -15.688 -9.784  2.531   1.00 27.71 ? 151  LEU B CA    1 
ATOM   6770  C  C     . LEU B 1 131 ? -16.991 -9.254  1.962   1.00 28.26 ? 151  LEU B C     1 
ATOM   6771  O  O     . LEU B 1 131 ? -17.699 -9.962  1.256   1.00 27.84 ? 151  LEU B O     1 
ATOM   6772  C  CB    . LEU B 1 131 ? -15.883 -10.110 4.015   1.00 27.69 ? 151  LEU B CB    1 
ATOM   6773  C  CG    . LEU B 1 131 ? -14.973 -11.205 4.566   1.00 28.04 ? 151  LEU B CG    1 
ATOM   6774  C  CD1   . LEU B 1 131 ? -15.115 -11.274 6.081   1.00 27.46 ? 151  LEU B CD1   1 
ATOM   6775  C  CD2   . LEU B 1 131 ? -15.296 -12.557 3.908   1.00 26.70 ? 151  LEU B CD2   1 
ATOM   6776  N  N     . TYR B 1 132 ? -17.296 -8.001  2.283   1.00 29.23 ? 152  TYR B N     1 
ATOM   6777  C  CA    . TYR B 1 132 ? -18.524 -7.363  1.832   1.00 30.24 ? 152  TYR B CA    1 
ATOM   6778  C  C     . TYR B 1 132 ? -18.549 -7.316  0.301   1.00 30.20 ? 152  TYR B C     1 
ATOM   6779  O  O     . TYR B 1 132 ? -19.579 -7.578  -0.319  1.00 29.89 ? 152  TYR B O     1 
ATOM   6780  C  CB    . TYR B 1 132 ? -18.646 -5.959  2.442   1.00 30.83 ? 152  TYR B CB    1 
ATOM   6781  C  CG    . TYR B 1 132 ? -20.046 -5.385  2.413   1.00 33.45 ? 152  TYR B CG    1 
ATOM   6782  C  CD1   . TYR B 1 132 ? -20.982 -5.731  3.381   1.00 36.19 ? 152  TYR B CD1   1 
ATOM   6783  C  CD2   . TYR B 1 132 ? -20.433 -4.483  1.416   1.00 36.91 ? 152  TYR B CD2   1 
ATOM   6784  C  CE1   . TYR B 1 132 ? -22.273 -5.208  3.365   1.00 37.89 ? 152  TYR B CE1   1 
ATOM   6785  C  CE2   . TYR B 1 132 ? -21.730 -3.950  1.385   1.00 38.26 ? 152  TYR B CE2   1 
ATOM   6786  C  CZ    . TYR B 1 132 ? -22.644 -4.319  2.360   1.00 39.59 ? 152  TYR B CZ    1 
ATOM   6787  O  OH    . TYR B 1 132 ? -23.929 -3.797  2.343   1.00 41.82 ? 152  TYR B OH    1 
ATOM   6788  N  N     . HIS B 1 133 ? -17.405 -7.014  -0.308  1.00 30.29 ? 153  HIS B N     1 
ATOM   6789  C  CA    . HIS B 1 133 ? -17.315 -6.990  -1.767  1.00 30.04 ? 153  HIS B CA    1 
ATOM   6790  C  C     . HIS B 1 133 ? -17.601 -8.375  -2.328  1.00 29.66 ? 153  HIS B C     1 
ATOM   6791  O  O     . HIS B 1 133 ? -18.317 -8.505  -3.315  1.00 29.90 ? 153  HIS B O     1 
ATOM   6792  C  CB    . HIS B 1 133 ? -15.937 -6.505  -2.230  1.00 30.12 ? 153  HIS B CB    1 
ATOM   6793  C  CG    . HIS B 1 133 ? -15.728 -6.608  -3.707  0.50 30.01 ? 153  HIS B CG    1 
ATOM   6794  N  ND1   . HIS B 1 133 ? -16.398 -5.811  -4.609  0.50 30.30 ? 153  HIS B ND1   1 
ATOM   6795  C  CD2   . HIS B 1 133 ? -14.928 -7.417  -4.439  0.50 30.05 ? 153  HIS B CD2   1 
ATOM   6796  C  CE1   . HIS B 1 133 ? -16.019 -6.124  -5.834  0.50 29.43 ? 153  HIS B CE1   1 
ATOM   6797  N  NE2   . HIS B 1 133 ? -15.125 -7.093  -5.758  0.50 30.02 ? 153  HIS B NE2   1 
ATOM   6798  N  N     . THR B 1 134 ? -17.038 -9.401  -1.690  1.00 29.26 ? 154  THR B N     1 
ATOM   6799  C  CA    . THR B 1 134 ? -17.248 -10.783 -2.102  1.00 29.04 ? 154  THR B CA    1 
ATOM   6800  C  C     . THR B 1 134 ? -18.733 -11.151 -1.997  1.00 29.23 ? 154  THR B C     1 
ATOM   6801  O  O     . THR B 1 134 ? -19.286 -11.739 -2.914  1.00 28.94 ? 154  THR B O     1 
ATOM   6802  C  CB    . THR B 1 134 ? -16.391 -11.762 -1.255  1.00 29.18 ? 154  THR B CB    1 
ATOM   6803  O  OG1   . THR B 1 134 ? -15.003 -11.440 -1.401  1.00 29.14 ? 154  THR B OG1   1 
ATOM   6804  C  CG2   . THR B 1 134 ? -16.618 -13.208 -1.663  1.00 27.97 ? 154  THR B CG2   1 
ATOM   6805  N  N     . LEU B 1 135 ? -19.379 -10.780 -0.895  1.00 29.48 ? 155  LEU B N     1 
ATOM   6806  C  CA    . LEU B 1 135 ? -20.797 -11.089 -0.714  1.00 29.97 ? 155  LEU B CA    1 
ATOM   6807  C  C     . LEU B 1 135 ? -21.641 -10.387 -1.755  1.00 30.11 ? 155  LEU B C     1 
ATOM   6808  O  O     . LEU B 1 135 ? -22.518 -10.994 -2.353  1.00 30.17 ? 155  LEU B O     1 
ATOM   6809  C  CB    . LEU B 1 135 ? -21.299 -10.670 0.669   1.00 30.40 ? 155  LEU B CB    1 
ATOM   6810  C  CG    . LEU B 1 135 ? -21.116 -11.591 1.869   1.00 30.34 ? 155  LEU B CG    1 
ATOM   6811  C  CD1   . LEU B 1 135 ? -21.981 -11.056 3.020   1.00 29.79 ? 155  LEU B CD1   1 
ATOM   6812  C  CD2   . LEU B 1 135 ? -21.477 -13.033 1.542   1.00 30.78 ? 155  LEU B CD2   1 
ATOM   6813  N  N     . GLN B 1 136 ? -21.370 -9.101  -1.955  1.00 30.35 ? 156  GLN B N     1 
ATOM   6814  C  CA    . GLN B 1 136 ? -22.117 -8.298  -2.905  1.00 30.44 ? 156  GLN B CA    1 
ATOM   6815  C  C     . GLN B 1 136 ? -22.085 -8.950  -4.284  1.00 30.35 ? 156  GLN B C     1 
ATOM   6816  O  O     . GLN B 1 136 ? -23.121 -9.087  -4.935  1.00 30.75 ? 156  GLN B O     1 
ATOM   6817  C  CB    . GLN B 1 136 ? -21.572 -6.864  -2.957  1.00 30.52 ? 156  GLN B CB    1 
ATOM   6818  N  N     . GLU B 1 137 ? -20.903 -9.383  -4.701  1.00 29.83 ? 157  GLU B N     1 
ATOM   6819  C  CA    . GLU B 1 137 ? -20.732 -10.032 -5.992  1.00 29.69 ? 157  GLU B CA    1 
ATOM   6820  C  C     . GLU B 1 137 ? -21.327 -11.428 -6.016  1.00 28.88 ? 157  GLU B C     1 
ATOM   6821  O  O     . GLU B 1 137 ? -22.116 -11.760 -6.903  1.00 28.45 ? 157  GLU B O     1 
ATOM   6822  C  CB    . GLU B 1 137 ? -19.249 -10.122 -6.332  1.00 30.15 ? 157  GLU B CB    1 
ATOM   6823  C  CG    . GLU B 1 137 ? -18.612 -8.771  -6.535  1.00 32.64 ? 157  GLU B CG    1 
ATOM   6824  C  CD    . GLU B 1 137 ? -19.032 -8.134  -7.843  1.00 35.41 ? 157  GLU B CD    1 
ATOM   6825  O  OE1   . GLU B 1 137 ? -18.787 -8.746  -8.906  1.00 38.42 ? 157  GLU B OE1   1 
ATOM   6826  O  OE2   . GLU B 1 137 ? -19.606 -7.029  -7.808  1.00 36.81 ? 157  GLU B OE2   1 
ATOM   6827  N  N     . ALA B 1 138 ? -20.946 -12.247 -5.041  1.00 27.80 ? 158  ALA B N     1 
ATOM   6828  C  CA    . ALA B 1 138 ? -21.406 -13.629 -4.990  1.00 27.55 ? 158  ALA B CA    1 
ATOM   6829  C  C     . ALA B 1 138 ? -22.932 -13.777 -4.873  1.00 27.03 ? 158  ALA B C     1 
ATOM   6830  O  O     . ALA B 1 138 ? -23.477 -14.785 -5.332  1.00 27.21 ? 158  ALA B O     1 
ATOM   6831  C  CB    . ALA B 1 138 ? -20.715 -14.381 -3.860  1.00 27.42 ? 158  ALA B CB    1 
ATOM   6832  N  N     . THR B 1 139 ? -23.616 -12.797 -4.279  1.00 26.03 ? 159  THR B N     1 
ATOM   6833  C  CA    . THR B 1 139 ? -25.068 -12.908 -4.076  1.00 25.59 ? 159  THR B CA    1 
ATOM   6834  C  C     . THR B 1 139 ? -25.945 -12.224 -5.136  1.00 25.93 ? 159  THR B C     1 
ATOM   6835  O  O     . THR B 1 139 ? -27.163 -12.222 -5.008  1.00 25.86 ? 159  THR B O     1 
ATOM   6836  C  CB    . THR B 1 139 ? -25.493 -12.424 -2.667  1.00 25.61 ? 159  THR B CB    1 
ATOM   6837  O  OG1   . THR B 1 139 ? -25.233 -11.021 -2.520  1.00 23.73 ? 159  THR B OG1   1 
ATOM   6838  C  CG2   . THR B 1 139 ? -24.764 -13.219 -1.593  1.00 23.96 ? 159  THR B CG2   1 
ATOM   6839  N  N     . LYS B 1 140 ? -25.345 -11.696 -6.200  1.00 26.43 ? 160  LYS B N     1 
ATOM   6840  C  CA    . LYS B 1 140 ? -26.121 -11.053 -7.272  1.00 26.99 ? 160  LYS B CA    1 
ATOM   6841  C  C     . LYS B 1 140 ? -27.288 -11.906 -7.811  1.00 26.49 ? 160  LYS B C     1 
ATOM   6842  O  O     . LYS B 1 140 ? -28.358 -11.376 -8.080  1.00 26.13 ? 160  LYS B O     1 
ATOM   6843  C  CB    . LYS B 1 140 ? -25.205 -10.623 -8.427  1.00 27.32 ? 160  LYS B CB    1 
ATOM   6844  C  CG    . LYS B 1 140 ? -24.276 -9.486  -8.045  1.00 29.09 ? 160  LYS B CG    1 
ATOM   6845  C  CD    . LYS B 1 140 ? -23.657 -8.826  -9.253  1.00 31.00 ? 160  LYS B CD    1 
ATOM   6846  C  CE    . LYS B 1 140 ? -22.625 -7.802  -8.816  1.00 32.35 ? 160  LYS B CE    1 
ATOM   6847  N  NZ    . LYS B 1 140 ? -22.303 -6.830  -9.885  1.00 34.19 ? 160  LYS B NZ    1 
ATOM   6848  N  N     . PRO B 1 141 ? -27.082 -13.225 -7.967  1.00 26.00 ? 161  PRO B N     1 
ATOM   6849  C  CA    . PRO B 1 141 ? -28.189 -14.067 -8.411  1.00 25.86 ? 161  PRO B CA    1 
ATOM   6850  C  C     . PRO B 1 141 ? -29.390 -14.070 -7.461  1.00 25.93 ? 161  PRO B C     1 
ATOM   6851  O  O     . PRO B 1 141 ? -30.507 -14.355 -7.891  1.00 25.94 ? 161  PRO B O     1 
ATOM   6852  C  CB    . PRO B 1 141 ? -27.561 -15.464 -8.476  1.00 25.72 ? 161  PRO B CB    1 
ATOM   6853  C  CG    . PRO B 1 141 ? -26.104 -15.220 -8.633  1.00 25.56 ? 161  PRO B CG    1 
ATOM   6854  C  CD    . PRO B 1 141 ? -25.825 -13.988 -7.849  1.00 25.85 ? 161  PRO B CD    1 
ATOM   6855  N  N     . LEU B 1 142 ? -29.154 -13.753 -6.185  1.00 25.92 ? 162  LEU B N     1 
ATOM   6856  C  CA    . LEU B 1 142 ? -30.201 -13.733 -5.160  1.00 25.47 ? 162  LEU B CA    1 
ATOM   6857  C  C     . LEU B 1 142 ? -30.891 -12.370 -5.006  1.00 25.34 ? 162  LEU B C     1 
ATOM   6858  O  O     . LEU B 1 142 ? -31.712 -12.179 -4.095  1.00 24.63 ? 162  LEU B O     1 
ATOM   6859  C  CB    . LEU B 1 142 ? -29.609 -14.157 -3.811  1.00 25.42 ? 162  LEU B CB    1 
ATOM   6860  C  CG    . LEU B 1 142 ? -29.231 -15.630 -3.653  1.00 25.58 ? 162  LEU B CG    1 
ATOM   6861  C  CD1   . LEU B 1 142 ? -28.698 -15.874 -2.245  1.00 25.21 ? 162  LEU B CD1   1 
ATOM   6862  C  CD2   . LEU B 1 142 ? -30.434 -16.532 -3.937  1.00 25.53 ? 162  LEU B CD2   1 
ATOM   6863  N  N     . HIS B 1 143 ? -30.581 -11.431 -5.896  1.00 25.25 ? 163  HIS B N     1 
ATOM   6864  C  CA    . HIS B 1 143 ? -31.116 -10.077 -5.778  1.00 25.36 ? 163  HIS B CA    1 
ATOM   6865  C  C     . HIS B 1 143 ? -32.641 -10.011 -5.657  1.00 25.28 ? 163  HIS B C     1 
ATOM   6866  O  O     . HIS B 1 143 ? -33.158 -9.373  -4.732  1.00 24.76 ? 163  HIS B O     1 
ATOM   6867  C  CB    . HIS B 1 143 ? -30.647 -9.188  -6.931  1.00 25.68 ? 163  HIS B CB    1 
ATOM   6868  C  CG    . HIS B 1 143 ? -30.976 -7.742  -6.732  1.00 26.28 ? 163  HIS B CG    1 
ATOM   6869  N  ND1   . HIS B 1 143 ? -30.333 -6.955  -5.798  1.00 26.69 ? 163  HIS B ND1   1 
ATOM   6870  C  CD2   . HIS B 1 143 ? -31.899 -6.946  -7.325  1.00 27.05 ? 163  HIS B CD2   1 
ATOM   6871  C  CE1   . HIS B 1 143 ? -30.836 -5.733  -5.836  1.00 26.30 ? 163  HIS B CE1   1 
ATOM   6872  N  NE2   . HIS B 1 143 ? -31.791 -5.703  -6.749  1.00 27.18 ? 163  HIS B NE2   1 
ATOM   6873  N  N     . GLN B 1 144 ? -33.356 -10.657 -6.583  1.00 25.40 ? 164  GLN B N     1 
ATOM   6874  C  CA    . GLN B 1 144 ? -34.828 -10.683 -6.533  1.00 25.24 ? 164  GLN B CA    1 
ATOM   6875  C  C     . GLN B 1 144 ? -35.345 -11.468 -5.323  1.00 25.04 ? 164  GLN B C     1 
ATOM   6876  O  O     . GLN B 1 144 ? -36.377 -11.123 -4.729  1.00 25.26 ? 164  GLN B O     1 
ATOM   6877  C  CB    . GLN B 1 144 ? -35.405 -11.279 -7.825  1.00 25.31 ? 164  GLN B CB    1 
ATOM   6878  N  N     . PHE B 1 145 ? -34.637 -12.536 -4.975  1.00 24.76 ? 165  PHE B N     1 
ATOM   6879  C  CA    . PHE B 1 145 ? -34.969 -13.347 -3.799  1.00 24.78 ? 165  PHE B CA    1 
ATOM   6880  C  C     . PHE B 1 145 ? -34.911 -12.476 -2.536  1.00 24.63 ? 165  PHE B C     1 
ATOM   6881  O  O     . PHE B 1 145 ? -35.839 -12.491 -1.716  1.00 23.62 ? 165  PHE B O     1 
ATOM   6882  C  CB    . PHE B 1 145 ? -34.009 -14.539 -3.711  1.00 24.80 ? 165  PHE B CB    1 
ATOM   6883  C  CG    . PHE B 1 145 ? -34.047 -15.263 -2.403  1.00 25.95 ? 165  PHE B CG    1 
ATOM   6884  C  CD1   . PHE B 1 145 ? -35.009 -16.241 -2.165  1.00 26.37 ? 165  PHE B CD1   1 
ATOM   6885  C  CD2   . PHE B 1 145 ? -33.105 -14.979 -1.408  1.00 26.47 ? 165  PHE B CD2   1 
ATOM   6886  C  CE1   . PHE B 1 145 ? -35.045 -16.913 -0.956  1.00 26.72 ? 165  PHE B CE1   1 
ATOM   6887  C  CE2   . PHE B 1 145 ? -33.131 -15.651 -0.195  1.00 26.95 ? 165  PHE B CE2   1 
ATOM   6888  C  CZ    . PHE B 1 145 ? -34.100 -16.619 0.033   1.00 27.01 ? 165  PHE B CZ    1 
ATOM   6889  N  N     . PHE B 1 146 ? -33.826 -11.705 -2.417  1.00 24.40 ? 166  PHE B N     1 
ATOM   6890  C  CA    . PHE B 1 146 ? -33.651 -10.759 -1.322  1.00 24.50 ? 166  PHE B CA    1 
ATOM   6891  C  C     . PHE B 1 146 ? -34.803 -9.755  -1.270  1.00 25.04 ? 166  PHE B C     1 
ATOM   6892  O  O     . PHE B 1 146 ? -35.402 -9.536  -0.216  1.00 24.86 ? 166  PHE B O     1 
ATOM   6893  C  CB    . PHE B 1 146 ? -32.338 -9.970  -1.468  1.00 24.23 ? 166  PHE B CB    1 
ATOM   6894  C  CG    . PHE B 1 146 ? -31.078 -10.765 -1.226  1.00 22.67 ? 166  PHE B CG    1 
ATOM   6895  C  CD1   . PHE B 1 146 ? -31.040 -11.835 -0.362  1.00 22.47 ? 166  PHE B CD1   1 
ATOM   6896  C  CD2   . PHE B 1 146 ? -29.891 -10.373 -1.830  1.00 22.77 ? 166  PHE B CD2   1 
ATOM   6897  C  CE1   . PHE B 1 146 ? -29.842 -12.529 -0.135  1.00 22.95 ? 166  PHE B CE1   1 
ATOM   6898  C  CE2   . PHE B 1 146 ? -28.708 -11.057 -1.605  1.00 21.80 ? 166  PHE B CE2   1 
ATOM   6899  C  CZ    . PHE B 1 146 ? -28.685 -12.132 -0.753  1.00 21.73 ? 166  PHE B CZ    1 
ATOM   6900  N  N     . LEU B 1 147 ? -35.103 -9.139  -2.408  1.00 25.28 ? 167  LEU B N     1 
ATOM   6901  C  CA    . LEU B 1 147 ? -36.141 -8.119  -2.452  1.00 25.66 ? 167  LEU B CA    1 
ATOM   6902  C  C     . LEU B 1 147 ? -37.479 -8.743  -2.064  1.00 25.66 ? 167  LEU B C     1 
ATOM   6903  O  O     . LEU B 1 147 ? -38.173 -8.221  -1.204  1.00 25.03 ? 167  LEU B O     1 
ATOM   6904  C  CB    . LEU B 1 147 ? -36.229 -7.450  -3.831  1.00 25.78 ? 167  LEU B CB    1 
ATOM   6905  C  CG    . LEU B 1 147 ? -35.169 -6.407  -4.237  1.00 27.06 ? 167  LEU B CG    1 
ATOM   6906  C  CD1   . LEU B 1 147 ? -35.516 -5.856  -5.621  1.00 28.27 ? 167  LEU B CD1   1 
ATOM   6907  C  CD2   . LEU B 1 147 ? -35.054 -5.252  -3.242  1.00 27.42 ? 167  LEU B CD2   1 
ATOM   6908  N  N     . ASN B 1 148 ? -37.815 -9.877  -2.671  1.00 26.23 ? 168  ASN B N     1 
ATOM   6909  C  CA    . ASN B 1 148 ? -39.100 -10.533 -2.409  1.00 26.93 ? 168  ASN B CA    1 
ATOM   6910  C  C     . ASN B 1 148 ? -39.271 -11.025 -0.973  1.00 26.39 ? 168  ASN B C     1 
ATOM   6911  O  O     . ASN B 1 148 ? -40.383 -11.001 -0.445  1.00 26.31 ? 168  ASN B O     1 
ATOM   6912  C  CB    . ASN B 1 148 ? -39.319 -11.716 -3.368  1.00 27.36 ? 168  ASN B CB    1 
ATOM   6913  C  CG    . ASN B 1 148 ? -39.610 -11.276 -4.804  1.00 29.48 ? 168  ASN B CG    1 
ATOM   6914  O  OD1   . ASN B 1 148 ? -39.702 -10.079 -5.101  1.00 31.62 ? 168  ASN B OD1   1 
ATOM   6915  N  ND2   . ASN B 1 148 ? -39.749 -12.254 -5.706  1.00 30.18 ? 168  ASN B ND2   1 
ATOM   6916  N  N     . THR B 1 149 ? -38.186 -11.485 -0.353  1.00 25.75 ? 169  THR B N     1 
ATOM   6917  C  CA    . THR B 1 149 ? -38.277 -12.111 0.965   1.00 25.52 ? 169  THR B CA    1 
ATOM   6918  C  C     . THR B 1 149 ? -38.043 -11.137 2.110   1.00 25.48 ? 169  THR B C     1 
ATOM   6919  O  O     . THR B 1 149 ? -38.533 -11.367 3.229   1.00 25.68 ? 169  THR B O     1 
ATOM   6920  C  CB    . THR B 1 149 ? -37.315 -13.317 1.087   1.00 25.68 ? 169  THR B CB    1 
ATOM   6921  O  OG1   . THR B 1 149 ? -35.964 -12.897 0.861   1.00 25.83 ? 169  THR B OG1   1 
ATOM   6922  C  CG2   . THR B 1 149 ? -37.691 -14.400 0.066   1.00 24.95 ? 169  THR B CG2   1 
ATOM   6923  N  N     . THR B 1 150 ? -37.316 -10.048 1.838   1.00 24.78 ? 170  THR B N     1 
ATOM   6924  C  CA    . THR B 1 150 ? -36.954 -9.087  2.883   1.00 24.43 ? 170  THR B CA    1 
ATOM   6925  C  C     . THR B 1 150 ? -37.215 -7.612  2.563   1.00 24.42 ? 170  THR B C     1 
ATOM   6926  O  O     . THR B 1 150 ? -37.225 -6.795  3.478   1.00 24.05 ? 170  THR B O     1 
ATOM   6927  C  CB    . THR B 1 150 ? -35.451 -9.220  3.267   1.00 24.58 ? 170  THR B CB    1 
ATOM   6928  O  OG1   . THR B 1 150 ? -34.639 -8.598  2.263   1.00 22.25 ? 170  THR B OG1   1 
ATOM   6929  C  CG2   . THR B 1 150 ? -35.056 -10.681 3.440   1.00 23.96 ? 170  THR B CG2   1 
ATOM   6930  N  N     . GLY B 1 151 ? -37.399 -7.266  1.286   1.00 24.37 ? 171  GLY B N     1 
ATOM   6931  C  CA    . GLY B 1 151 ? -37.487 -5.862  0.865   1.00 24.61 ? 171  GLY B CA    1 
ATOM   6932  C  C     . GLY B 1 151 ? -36.168 -5.096  0.960   1.00 24.80 ? 171  GLY B C     1 
ATOM   6933  O  O     . GLY B 1 151 ? -36.142 -3.884  0.762   1.00 24.85 ? 171  GLY B O     1 
ATOM   6934  N  N     . PHE B 1 152 ? -35.082 -5.802  1.284   1.00 24.61 ? 172  PHE B N     1 
ATOM   6935  C  CA    . PHE B 1 152 ? -33.748 -5.228  1.412   1.00 24.59 ? 172  PHE B CA    1 
ATOM   6936  C  C     . PHE B 1 152 ? -32.850 -5.958  0.418   1.00 24.79 ? 172  PHE B C     1 
ATOM   6937  O  O     . PHE B 1 152 ? -33.235 -6.994  -0.120  1.00 25.40 ? 172  PHE B O     1 
ATOM   6938  C  CB    . PHE B 1 152 ? -33.191 -5.460  2.826   1.00 24.53 ? 172  PHE B CB    1 
ATOM   6939  C  CG    . PHE B 1 152 ? -33.768 -4.561  3.895   1.00 23.77 ? 172  PHE B CG    1 
ATOM   6940  C  CD1   . PHE B 1 152 ? -35.140 -4.369  4.027   1.00 24.13 ? 172  PHE B CD1   1 
ATOM   6941  C  CD2   . PHE B 1 152 ? -32.927 -3.947  4.805   1.00 23.83 ? 172  PHE B CD2   1 
ATOM   6942  C  CE1   . PHE B 1 152 ? -35.656 -3.561  5.027   1.00 24.42 ? 172  PHE B CE1   1 
ATOM   6943  C  CE2   . PHE B 1 152 ? -33.427 -3.130  5.812   1.00 24.76 ? 172  PHE B CE2   1 
ATOM   6944  C  CZ    . PHE B 1 152 ? -34.797 -2.937  5.927   1.00 24.99 ? 172  PHE B CZ    1 
ATOM   6945  N  N     . SER B 1 153 ? -31.655 -5.434  0.181   1.00 24.89 ? 173  SER B N     1 
ATOM   6946  C  CA    . SER B 1 153 ? -30.691 -6.077  -0.714  1.00 25.19 ? 173  SER B CA    1 
ATOM   6947  C  C     . SER B 1 153 ? -29.283 -5.535  -0.457  1.00 25.38 ? 173  SER B C     1 
ATOM   6948  O  O     . SER B 1 153 ? -29.088 -4.732  0.443   1.00 24.66 ? 173  SER B O     1 
ATOM   6949  C  CB    . SER B 1 153 ? -31.079 -5.832  -2.172  1.00 25.37 ? 173  SER B CB    1 
ATOM   6950  O  OG    . SER B 1 153 ? -30.907 -4.466  -2.503  1.00 25.80 ? 173  SER B OG    1 
ATOM   6951  N  N     . PHE B 1 154 ? -28.318 -5.969  -1.263  1.00 26.43 ? 174  PHE B N     1 
ATOM   6952  C  CA    . PHE B 1 154 ? -26.940 -5.467  -1.194  1.00 27.29 ? 174  PHE B CA    1 
ATOM   6953  C  C     . PHE B 1 154 ? -26.639 -4.407  -2.264  1.00 28.39 ? 174  PHE B C     1 
ATOM   6954  O  O     . PHE B 1 154 ? -25.585 -3.752  -2.232  1.00 29.23 ? 174  PHE B O     1 
ATOM   6955  C  CB    . PHE B 1 154 ? -25.947 -6.619  -1.364  1.00 27.41 ? 174  PHE B CB    1 
ATOM   6956  C  CG    . PHE B 1 154 ? -25.779 -7.475  -0.137  1.00 27.00 ? 174  PHE B CG    1 
ATOM   6957  C  CD1   . PHE B 1 154 ? -25.176 -6.970  0.997   1.00 26.01 ? 174  PHE B CD1   1 
ATOM   6958  C  CD2   . PHE B 1 154 ? -26.212 -8.792  -0.128  1.00 27.64 ? 174  PHE B CD2   1 
ATOM   6959  C  CE1   . PHE B 1 154 ? -25.017 -7.761  2.124   1.00 26.48 ? 174  PHE B CE1   1 
ATOM   6960  C  CE2   . PHE B 1 154 ? -26.053 -9.587  0.997   1.00 27.17 ? 174  PHE B CE2   1 
ATOM   6961  C  CZ    . PHE B 1 154 ? -25.451 -9.070  2.119   1.00 26.26 ? 174  PHE B CZ    1 
ATOM   6962  N  N     . GLN B 1 155 ? -27.535 -4.242  -3.225  1.00 28.71 ? 175  GLN B N     1 
ATOM   6963  C  CA    . GLN B 1 155 ? -27.250 -3.374  -4.359  1.00 29.21 ? 175  GLN B CA    1 
ATOM   6964  C  C     . GLN B 1 155 ? -28.289 -2.288  -4.473  1.00 28.50 ? 175  GLN B C     1 
ATOM   6965  O  O     . GLN B 1 155 ? -29.485 -2.563  -4.425  1.00 28.61 ? 175  GLN B O     1 
ATOM   6966  C  CB    . GLN B 1 155 ? -27.194 -4.196  -5.639  1.00 29.75 ? 175  GLN B CB    1 
ATOM   6967  C  CG    . GLN B 1 155 ? -26.024 -5.153  -5.655  1.00 32.22 ? 175  GLN B CG    1 
ATOM   6968  C  CD    . GLN B 1 155 ? -26.108 -6.124  -6.786  1.00 35.70 ? 175  GLN B CD    1 
ATOM   6969  O  OE1   . GLN B 1 155 ? -27.087 -6.868  -6.907  1.00 39.02 ? 175  GLN B OE1   1 
ATOM   6970  N  NE2   . GLN B 1 155 ? -25.090 -6.132  -7.632  1.00 37.09 ? 175  GLN B NE2   1 
ATOM   6971  N  N     . ASP B 1 156 ? -27.813 -1.055  -4.612  1.00 28.11 ? 176  ASP B N     1 
ATOM   6972  C  CA    . ASP B 1 156 ? -28.661 0.123   -4.707  1.00 28.04 ? 176  ASP B CA    1 
ATOM   6973  C  C     . ASP B 1 156 ? -29.719 0.066   -3.601  1.00 28.05 ? 176  ASP B C     1 
ATOM   6974  O  O     . ASP B 1 156 ? -30.914 0.255   -3.842  1.00 27.72 ? 176  ASP B O     1 
ATOM   6975  C  CB    . ASP B 1 156 ? -29.278 0.201   -6.103  1.00 27.71 ? 176  ASP B CB    1 
ATOM   6976  C  CG    . ASP B 1 156 ? -28.222 0.139   -7.204  1.00 27.99 ? 176  ASP B CG    1 
ATOM   6977  O  OD1   . ASP B 1 156 ? -27.597 1.190   -7.512  1.00 26.01 ? 176  ASP B OD1   1 
ATOM   6978  O  OD2   . ASP B 1 156 ? -27.996 -0.969  -7.741  1.00 26.50 ? 176  ASP B OD2   1 
ATOM   6979  N  N     . CYS B 1 157 ? -29.249 -0.194  -2.382  1.00 27.84 ? 177  CYS B N     1 
ATOM   6980  C  CA    . CYS B 1 157 ? -30.131 -0.496  -1.260  1.00 28.05 ? 177  CYS B CA    1 
ATOM   6981  C  C     . CYS B 1 157 ? -30.391 0.707   -0.350  1.00 28.50 ? 177  CYS B C     1 
ATOM   6982  O  O     . CYS B 1 157 ? -31.469 0.830   0.231   1.00 29.02 ? 177  CYS B O     1 
ATOM   6983  C  CB    . CYS B 1 157 ? -29.565 -1.677  -0.462  1.00 27.76 ? 177  CYS B CB    1 
ATOM   6984  S  SG    . CYS B 1 157 ? -27.871 -1.469  0.104   1.00 27.43 ? 177  CYS B SG    1 
ATOM   6985  N  N     . HIS B 1 158 ? -29.393 1.568   -0.204  1.00 28.94 ? 178  HIS B N     1 
ATOM   6986  C  CA    . HIS B 1 158 ? -29.533 2.839   0.518   1.00 29.33 ? 178  HIS B CA    1 
ATOM   6987  C  C     . HIS B 1 158 ? -30.029 2.700   1.972   1.00 29.70 ? 178  HIS B C     1 
ATOM   6988  O  O     . HIS B 1 158 ? -29.227 2.399   2.860   1.00 29.92 ? 178  HIS B O     1 
ATOM   6989  C  CB    . HIS B 1 158 ? -30.355 3.825   -0.333  1.00 29.36 ? 178  HIS B CB    1 
ATOM   6990  C  CG    . HIS B 1 158 ? -29.795 4.005   -1.710  1.00 29.15 ? 178  HIS B CG    1 
ATOM   6991  N  ND1   . HIS B 1 158 ? -28.583 4.621   -1.941  1.00 29.01 ? 178  HIS B ND1   1 
ATOM   6992  C  CD2   . HIS B 1 158 ? -30.240 3.583   -2.917  1.00 29.57 ? 178  HIS B CD2   1 
ATOM   6993  C  CE1   . HIS B 1 158 ? -28.323 4.599   -3.236  1.00 29.36 ? 178  HIS B CE1   1 
ATOM   6994  N  NE2   . HIS B 1 158 ? -29.310 3.972   -3.850  1.00 29.48 ? 178  HIS B NE2   1 
ATOM   6995  N  N     . ASP B 1 159 ? -31.318 2.912   2.222   1.00 29.91 ? 179  ASP B N     1 
ATOM   6996  C  CA    . ASP B 1 159 ? -31.871 2.780   3.583   1.00 30.43 ? 179  ASP B CA    1 
ATOM   6997  C  C     . ASP B 1 159 ? -32.400 1.364   3.878   1.00 29.76 ? 179  ASP B C     1 
ATOM   6998  O  O     . ASP B 1 159 ? -32.899 1.098   4.975   1.00 29.94 ? 179  ASP B O     1 
ATOM   6999  C  CB    . ASP B 1 159 ? -32.977 3.831   3.824   1.00 30.60 ? 179  ASP B CB    1 
ATOM   7000  C  CG    . ASP B 1 159 ? -34.100 3.750   2.809   1.00 33.32 ? 179  ASP B CG    1 
ATOM   7001  O  OD1   . ASP B 1 159 ? -33.867 3.229   1.692   1.00 37.73 ? 179  ASP B OD1   1 
ATOM   7002  O  OD2   . ASP B 1 159 ? -35.225 4.213   3.110   1.00 37.67 ? 179  ASP B OD2   1 
ATOM   7003  N  N     . ARG B 1 160 ? -32.292 0.463   2.899   1.00 29.16 ? 180  ARG B N     1 
ATOM   7004  C  CA    . ARG B 1 160 ? -32.762 -0.914  3.034   1.00 28.38 ? 180  ARG B CA    1 
ATOM   7005  C  C     . ARG B 1 160 ? -31.675 -1.898  2.611   1.00 27.42 ? 180  ARG B C     1 
ATOM   7006  O  O     . ARG B 1 160 ? -31.831 -2.671  1.657   1.00 26.45 ? 180  ARG B O     1 
ATOM   7007  C  CB    . ARG B 1 160 ? -34.026 -1.108  2.207   1.00 29.10 ? 180  ARG B CB    1 
ATOM   7008  C  CG    . ARG B 1 160 ? -35.211 -0.305  2.714   1.00 31.12 ? 180  ARG B CG    1 
ATOM   7009  C  CD    . ARG B 1 160 ? -36.463 -0.667  1.943   1.00 35.07 ? 180  ARG B CD    1 
ATOM   7010  N  NE    . ARG B 1 160 ? -37.552 0.268   2.216   1.00 38.59 ? 180  ARG B NE    1 
ATOM   7011  C  CZ    . ARG B 1 160 ? -38.511 0.095   3.130   1.00 41.97 ? 180  ARG B CZ    1 
ATOM   7012  N  NH1   . ARG B 1 160 ? -38.557 -0.997  3.896   1.00 42.92 ? 180  ARG B NH1   1 
ATOM   7013  N  NH2   . ARG B 1 160 ? -39.448 1.030   3.275   1.00 43.38 ? 180  ARG B NH2   1 
ATOM   7014  N  N     . CYS B 1 161 ? -30.566 -1.869  3.343   1.00 26.33 ? 181  CYS B N     1 
ATOM   7015  C  CA    . CYS B 1 161 ? -29.423 -2.694  3.019   1.00 25.79 ? 181  CYS B CA    1 
ATOM   7016  C  C     . CYS B 1 161 ? -29.334 -3.896  3.938   1.00 25.12 ? 181  CYS B C     1 
ATOM   7017  O  O     . CYS B 1 161 ? -29.589 -3.802  5.141   1.00 24.68 ? 181  CYS B O     1 
ATOM   7018  C  CB    . CYS B 1 161 ? -28.134 -1.885  3.115   1.00 25.70 ? 181  CYS B CB    1 
ATOM   7019  S  SG    . CYS B 1 161 ? -28.020 -0.530  1.916   1.00 27.69 ? 181  CYS B SG    1 
ATOM   7020  N  N     . LEU B 1 162 ? -28.947 -5.025  3.362   1.00 24.23 ? 182  LEU B N     1 
ATOM   7021  C  CA    . LEU B 1 162 ? -28.587 -6.190  4.145   1.00 23.80 ? 182  LEU B CA    1 
ATOM   7022  C  C     . LEU B 1 162 ? -27.192 -5.981  4.728   1.00 23.52 ? 182  LEU B C     1 
ATOM   7023  O  O     . LEU B 1 162 ? -26.383 -5.223  4.181   1.00 23.40 ? 182  LEU B O     1 
ATOM   7024  C  CB    . LEU B 1 162 ? -28.611 -7.441  3.280   1.00 23.51 ? 182  LEU B CB    1 
ATOM   7025  C  CG    . LEU B 1 162 ? -29.975 -7.822  2.708   1.00 23.63 ? 182  LEU B CG    1 
ATOM   7026  C  CD1   . LEU B 1 162 ? -29.827 -9.017  1.757   1.00 22.08 ? 182  LEU B CD1   1 
ATOM   7027  C  CD2   . LEU B 1 162 ? -30.989 -8.124  3.836   1.00 21.55 ? 182  LEU B CD2   1 
ATOM   7028  N  N     . ALA B 1 163 ? -26.945 -6.626  5.862   1.00 22.76 ? 183  ALA B N     1 
ATOM   7029  C  CA    . ALA B 1 163 ? -25.641 -6.635  6.497   1.00 22.40 ? 183  ALA B CA    1 
ATOM   7030  C  C     . ALA B 1 163 ? -25.349 -8.069  6.910   1.00 22.31 ? 183  ALA B C     1 
ATOM   7031  O  O     . ALA B 1 163 ? -26.212 -8.933  6.791   1.00 21.42 ? 183  ALA B O     1 
ATOM   7032  C  CB    . ALA B 1 163 ? -25.646 -5.730  7.701   1.00 22.28 ? 183  ALA B CB    1 
ATOM   7033  N  N     . PHE B 1 164 ? -24.137 -8.318  7.404   1.00 22.52 ? 184  PHE B N     1 
ATOM   7034  C  CA    . PHE B 1 164 ? -23.794 -9.624  7.926   1.00 22.61 ? 184  PHE B CA    1 
ATOM   7035  C  C     . PHE B 1 164 ? -23.037 -9.562  9.252   1.00 22.75 ? 184  PHE B C     1 
ATOM   7036  O  O     . PHE B 1 164 ? -22.366 -8.570  9.552   1.00 23.54 ? 184  PHE B O     1 
ATOM   7037  C  CB    . PHE B 1 164 ? -23.007 -10.431 6.888   1.00 22.93 ? 184  PHE B CB    1 
ATOM   7038  C  CG    . PHE B 1 164 ? -21.604 -9.948  6.662   1.00 22.87 ? 184  PHE B CG    1 
ATOM   7039  C  CD1   . PHE B 1 164 ? -20.558 -10.439 7.438   1.00 24.19 ? 184  PHE B CD1   1 
ATOM   7040  C  CD2   . PHE B 1 164 ? -21.321 -9.027  5.671   1.00 23.15 ? 184  PHE B CD2   1 
ATOM   7041  C  CE1   . PHE B 1 164 ? -19.250 -10.017 7.225   1.00 24.00 ? 184  PHE B CE1   1 
ATOM   7042  C  CE2   . PHE B 1 164 ? -20.011 -8.589  5.454   1.00 24.02 ? 184  PHE B CE2   1 
ATOM   7043  C  CZ    . PHE B 1 164 ? -18.977 -9.086  6.231   1.00 24.35 ? 184  PHE B CZ    1 
ATOM   7044  N  N     . THR B 1 165 ? -23.171 -10.632 10.033  1.00 22.02 ? 185  THR B N     1 
ATOM   7045  C  CA    . THR B 1 165 ? -22.412 -10.843 11.249  1.00 21.65 ? 185  THR B CA    1 
ATOM   7046  C  C     . THR B 1 165 ? -21.615 -12.132 11.059  1.00 21.44 ? 185  THR B C     1 
ATOM   7047  O  O     . THR B 1 165 ? -22.190 -13.209 10.839  1.00 21.21 ? 185  THR B O     1 
ATOM   7048  C  CB    . THR B 1 165 ? -23.358 -10.993 12.461  1.00 22.07 ? 185  THR B CB    1 
ATOM   7049  O  OG1   . THR B 1 165 ? -24.028 -9.748  12.700  1.00 23.02 ? 185  THR B OG1   1 
ATOM   7050  C  CG2   . THR B 1 165 ? -22.602 -11.429 13.719  1.00 21.12 ? 185  THR B CG2   1 
ATOM   7051  N  N     . ASP B 1 166 ? -20.294 -12.033 11.107  1.00 20.84 ? 186  ASP B N     1 
ATOM   7052  C  CA    . ASP B 1 166 ? -19.488 -13.243 11.066  1.00 20.73 ? 186  ASP B CA    1 
ATOM   7053  C  C     . ASP B 1 166 ? -19.421 -13.893 12.444  1.00 20.07 ? 186  ASP B C     1 
ATOM   7054  O  O     . ASP B 1 166 ? -19.465 -13.206 13.485  1.00 20.92 ? 186  ASP B O     1 
ATOM   7055  C  CB    . ASP B 1 166 ? -18.093 -12.989 10.489  1.00 21.09 ? 186  ASP B CB    1 
ATOM   7056  C  CG    . ASP B 1 166 ? -17.301 -11.993 11.273  1.00 21.10 ? 186  ASP B CG    1 
ATOM   7057  O  OD1   . ASP B 1 166 ? -17.868 -10.951 11.667  1.00 23.65 ? 186  ASP B OD1   1 
ATOM   7058  O  OD2   . ASP B 1 166 ? -16.096 -12.239 11.458  1.00 20.66 ? 186  ASP B OD2   1 
ATOM   7059  N  N     . VAL B 1 167 ? -19.367 -15.221 12.449  1.00 18.99 ? 187  VAL B N     1 
ATOM   7060  C  CA    . VAL B 1 167 ? -19.094 -15.969 13.664  1.00 18.76 ? 187  VAL B CA    1 
ATOM   7061  C  C     . VAL B 1 167 ? -17.695 -16.559 13.573  1.00 19.10 ? 187  VAL B C     1 
ATOM   7062  O  O     . VAL B 1 167 ? -17.115 -16.646 12.503  1.00 18.79 ? 187  VAL B O     1 
ATOM   7063  C  CB    . VAL B 1 167 ? -20.145 -17.080 13.951  1.00 18.37 ? 187  VAL B CB    1 
ATOM   7064  C  CG1   . VAL B 1 167 ? -21.551 -16.496 13.955  1.00 17.53 ? 187  VAL B CG1   1 
ATOM   7065  C  CG2   . VAL B 1 167 ? -20.039 -18.228 12.948  1.00 17.61 ? 187  VAL B CG2   1 
ATOM   7066  N  N     . ALA B 1 168 ? -17.160 -16.931 14.726  1.00 19.67 ? 188  ALA B N     1 
ATOM   7067  C  CA    . ALA B 1 168 ? -15.865 -17.562 14.824  1.00 19.93 ? 188  ALA B CA    1 
ATOM   7068  C  C     . ALA B 1 168 ? -15.985 -18.650 15.885  1.00 20.44 ? 188  ALA B C     1 
ATOM   7069  O  O     . ALA B 1 168 ? -16.854 -18.544 16.772  1.00 20.67 ? 188  ALA B O     1 
ATOM   7070  C  CB    . ALA B 1 168 ? -14.811 -16.543 15.203  1.00 19.81 ? 188  ALA B CB    1 
ATOM   7071  N  N     . PRO B 1 169 ? -15.112 -19.682 15.830  1.00 20.27 ? 189  PRO B N     1 
ATOM   7072  C  CA    . PRO B 1 169 ? -13.996 -19.888 14.903  1.00 20.61 ? 189  PRO B CA    1 
ATOM   7073  C  C     . PRO B 1 169 ? -14.427 -20.247 13.489  1.00 20.72 ? 189  PRO B C     1 
ATOM   7074  O  O     . PRO B 1 169 ? -15.623 -20.461 13.229  1.00 20.32 ? 189  PRO B O     1 
ATOM   7075  C  CB    . PRO B 1 169 ? -13.230 -21.055 15.540  1.00 20.69 ? 189  PRO B CB    1 
ATOM   7076  C  CG    . PRO B 1 169 ? -14.263 -21.783 16.290  1.00 20.31 ? 189  PRO B CG    1 
ATOM   7077  C  CD    . PRO B 1 169 ? -15.134 -20.729 16.862  1.00 19.88 ? 189  PRO B CD    1 
ATOM   7078  N  N     . ARG B 1 170 ? -13.446 -20.320 12.589  1.00 21.03 ? 190  ARG B N     1 
ATOM   7079  C  CA    . ARG B 1 170 ? -13.710 -20.215 11.150  1.00 21.14 ? 190  ARG B CA    1 
ATOM   7080  C  C     . ARG B 1 170 ? -13.224 -21.442 10.407  1.00 21.28 ? 190  ARG B C     1 
ATOM   7081  O  O     . ARG B 1 170 ? -12.227 -21.399 9.663   1.00 21.29 ? 190  ARG B O     1 
ATOM   7082  C  CB    . ARG B 1 170 ? -13.043 -18.953 10.593  1.00 21.40 ? 190  ARG B CB    1 
ATOM   7083  C  CG    . ARG B 1 170 ? -13.373 -17.707 11.366  1.00 21.56 ? 190  ARG B CG    1 
ATOM   7084  C  CD    . ARG B 1 170 ? -12.437 -16.561 11.036  1.00 21.88 ? 190  ARG B CD    1 
ATOM   7085  N  NE    . ARG B 1 170 ? -12.676 -15.458 11.958  1.00 21.04 ? 190  ARG B NE    1 
ATOM   7086  C  CZ    . ARG B 1 170 ? -13.617 -14.530 11.810  1.00 21.00 ? 190  ARG B CZ    1 
ATOM   7087  N  NH1   . ARG B 1 170 ? -14.426 -14.533 10.754  1.00 20.51 ? 190  ARG B NH1   1 
ATOM   7088  N  NH2   . ARG B 1 170 ? -13.740 -13.581 12.728  1.00 20.02 ? 190  ARG B NH2   1 
ATOM   7089  N  N     . GLY B 1 171 ? -13.945 -22.540 10.609  1.00 21.48 ? 191  GLY B N     1 
ATOM   7090  C  CA    . GLY B 1 171 ? -13.588 -23.822 10.016  1.00 21.63 ? 191  GLY B CA    1 
ATOM   7091  C  C     . GLY B 1 171 ? -13.690 -24.964 11.004  1.00 21.80 ? 191  GLY B C     1 
ATOM   7092  O  O     . GLY B 1 171 ? -14.326 -24.836 12.052  1.00 22.23 ? 191  GLY B O     1 
ATOM   7093  N  N     . VAL B 1 172 ? -13.079 -26.088 10.643  1.00 21.79 ? 192  VAL B N     1 
ATOM   7094  C  CA    . VAL B 1 172 ? -13.118 -27.310 11.442  1.00 21.82 ? 192  VAL B CA    1 
ATOM   7095  C  C     . VAL B 1 172 ? -11.728 -27.741 11.940  1.00 22.23 ? 192  VAL B C     1 
ATOM   7096  O  O     . VAL B 1 172 ? -11.633 -28.681 12.723  1.00 22.53 ? 192  VAL B O     1 
ATOM   7097  C  CB    . VAL B 1 172 ? -13.766 -28.477 10.646  1.00 21.89 ? 192  VAL B CB    1 
ATOM   7098  C  CG1   . VAL B 1 172 ? -15.220 -28.185 10.358  1.00 21.40 ? 192  VAL B CG1   1 
ATOM   7099  C  CG2   . VAL B 1 172 ? -13.010 -28.767 9.329   1.00 21.29 ? 192  VAL B CG2   1 
ATOM   7100  N  N     . ALA B 1 173 ? -10.672 -27.039 11.520  1.00 22.15 ? 193  ALA B N     1 
ATOM   7101  C  CA    . ALA B 1 173 ? -9.287  -27.406 11.852  1.00 22.51 ? 193  ALA B CA    1 
ATOM   7102  C  C     . ALA B 1 173 ? -8.335  -26.215 11.802  1.00 22.68 ? 193  ALA B C     1 
ATOM   7103  O  O     . ALA B 1 173 ? -8.613  -25.207 11.161  1.00 22.92 ? 193  ALA B O     1 
ATOM   7104  C  CB    . ALA B 1 173 ? -8.786  -28.484 10.896  1.00 22.50 ? 193  ALA B CB    1 
ATOM   7105  N  N     . SER B 1 174 ? -7.198  -26.360 12.474  1.00 23.01 ? 194  SER B N     1 
ATOM   7106  C  CA    . SER B 1 174 ? -6.151  -25.343 12.500  1.00 23.10 ? 194  SER B CA    1 
ATOM   7107  C  C     . SER B 1 174 ? -5.680  -25.048 11.085  1.00 23.06 ? 194  SER B C     1 
ATOM   7108  O  O     . SER B 1 174 ? -5.409  -25.973 10.327  1.00 23.67 ? 194  SER B O     1 
ATOM   7109  C  CB    . SER B 1 174 ? -4.966  -25.842 13.342  1.00 23.25 ? 194  SER B CB    1 
ATOM   7110  O  OG    . SER B 1 174 ? -3.877  -24.929 13.295  1.00 23.86 ? 194  SER B OG    1 
ATOM   7111  N  N     . GLY B 1 175 ? -5.618  -23.768 10.724  1.00 23.04 ? 195  GLY B N     1 
ATOM   7112  C  CA    . GLY B 1 175 ? -5.155  -23.342 9.401   1.00 22.76 ? 195  GLY B CA    1 
ATOM   7113  C  C     . GLY B 1 175 ? -6.279  -22.870 8.495   1.00 22.68 ? 195  GLY B C     1 
ATOM   7114  O  O     . GLY B 1 175 ? -6.028  -22.238 7.475   1.00 22.30 ? 195  GLY B O     1 
ATOM   7115  N  N     . GLN B 1 176 ? -7.524  -23.172 8.857   1.00 22.64 ? 196  GLN B N     1 
ATOM   7116  C  CA    . GLN B 1 176 ? -8.670  -22.758 8.038   1.00 22.48 ? 196  GLN B CA    1 
ATOM   7117  C  C     . GLN B 1 176 ? -9.108  -21.343 8.359   1.00 22.36 ? 196  GLN B C     1 
ATOM   7118  O  O     . GLN B 1 176 ? -8.872  -20.837 9.459   1.00 22.98 ? 196  GLN B O     1 
ATOM   7119  C  CB    . GLN B 1 176 ? -9.834  -23.747 8.181   1.00 22.51 ? 196  GLN B CB    1 
ATOM   7120  C  CG    . GLN B 1 176 ? -9.426  -25.183 7.795   1.00 22.80 ? 196  GLN B CG    1 
ATOM   7121  C  CD    . GLN B 1 176 ? -10.580 -26.167 7.716   1.00 23.87 ? 196  GLN B CD    1 
ATOM   7122  O  OE1   . GLN B 1 176 ? -11.736 -25.841 8.019   1.00 22.14 ? 196  GLN B OE1   1 
ATOM   7123  N  NE2   . GLN B 1 176 ? -10.271 -27.383 7.280   1.00 23.90 ? 196  GLN B NE2   1 
ATOM   7124  N  N     . ARG B 1 177 ? -9.704  -20.695 7.366   1.00 21.97 ? 197  ARG B N     1 
ATOM   7125  C  CA    . ARG B 1 177 ? -10.345 -19.402 7.536   1.00 21.85 ? 197  ARG B CA    1 
ATOM   7126  C  C     . ARG B 1 177 ? -11.625 -19.399 6.704   1.00 21.57 ? 197  ARG B C     1 
ATOM   7127  O  O     . ARG B 1 177 ? -11.703 -18.794 5.623   1.00 21.66 ? 197  ARG B O     1 
ATOM   7128  C  CB    . ARG B 1 177 ? -9.394  -18.269 7.129   1.00 21.72 ? 197  ARG B CB    1 
ATOM   7129  C  CG    . ARG B 1 177 ? -9.761  -16.918 7.709   1.00 21.35 ? 197  ARG B CG    1 
ATOM   7130  C  CD    . ARG B 1 177 ? -8.619  -15.951 7.481   1.00 22.25 ? 197  ARG B CD    1 
ATOM   7131  N  NE    . ARG B 1 177 ? -8.788  -14.630 8.085   1.00 21.72 ? 197  ARG B NE    1 
ATOM   7132  C  CZ    . ARG B 1 177 ? -8.384  -14.289 9.307   1.00 20.57 ? 197  ARG B CZ    1 
ATOM   7133  N  NH1   . ARG B 1 177 ? -7.824  -15.177 10.120  1.00 21.24 ? 197  ARG B NH1   1 
ATOM   7134  N  NH2   . ARG B 1 177 ? -8.556  -13.043 9.727   1.00 21.00 ? 197  ARG B NH2   1 
ATOM   7135  N  N     . ARG B 1 178 ? -12.614 -20.127 7.217   1.00 21.33 ? 198  ARG B N     1 
ATOM   7136  C  CA    . ARG B 1 178 ? -13.880 -20.344 6.541   1.00 20.88 ? 198  ARG B CA    1 
ATOM   7137  C  C     . ARG B 1 178 ? -14.987 -19.901 7.491   1.00 20.63 ? 198  ARG B C     1 
ATOM   7138  O  O     . ARG B 1 178 ? -15.302 -20.610 8.445   1.00 20.39 ? 198  ARG B O     1 
ATOM   7139  C  CB    . ARG B 1 178 ? -14.047 -21.826 6.197   1.00 21.16 ? 198  ARG B CB    1 
ATOM   7140  C  CG    . ARG B 1 178 ? -12.923 -22.437 5.337   1.00 22.40 ? 198  ARG B CG    1 
ATOM   7141  C  CD    . ARG B 1 178 ? -12.894 -23.966 5.459   1.00 23.70 ? 198  ARG B CD    1 
ATOM   7142  N  NE    . ARG B 1 178 ? -14.038 -24.611 4.813   1.00 24.57 ? 198  ARG B NE    1 
ATOM   7143  C  CZ    . ARG B 1 178 ? -14.501 -25.829 5.101   1.00 25.79 ? 198  ARG B CZ    1 
ATOM   7144  N  NH1   . ARG B 1 178 ? -13.941 -26.579 6.051   1.00 26.31 ? 198  ARG B NH1   1 
ATOM   7145  N  NH2   . ARG B 1 178 ? -15.547 -26.309 4.432   1.00 26.97 ? 198  ARG B NH2   1 
ATOM   7146  N  N     . SER B 1 179 ? -15.570 -18.734 7.230   1.00 20.12 ? 199  SER B N     1 
ATOM   7147  C  CA    . SER B 1 179 ? -16.497 -18.103 8.172   1.00 20.21 ? 199  SER B CA    1 
ATOM   7148  C  C     . SER B 1 179 ? -17.960 -18.223 7.755   1.00 20.40 ? 199  SER B C     1 
ATOM   7149  O  O     . SER B 1 179 ? -18.336 -17.908 6.615   1.00 19.80 ? 199  SER B O     1 
ATOM   7150  C  CB    . SER B 1 179 ? -16.158 -16.616 8.331   1.00 20.23 ? 199  SER B CB    1 
ATOM   7151  O  OG    . SER B 1 179 ? -14.821 -16.442 8.770   1.00 19.89 ? 199  SER B OG    1 
ATOM   7152  N  N     . TRP B 1 180 ? -18.792 -18.654 8.697   1.00 20.60 ? 200  TRP B N     1 
ATOM   7153  C  CA    . TRP B 1 180 ? -20.243 -18.543 8.529   1.00 20.59 ? 200  TRP B CA    1 
ATOM   7154  C  C     . TRP B 1 180 ? -20.702 -17.128 8.822   1.00 20.41 ? 200  TRP B C     1 
ATOM   7155  O  O     . TRP B 1 180 ? -20.306 -16.545 9.819   1.00 21.06 ? 200  TRP B O     1 
ATOM   7156  C  CB    . TRP B 1 180 ? -20.971 -19.522 9.437   1.00 20.61 ? 200  TRP B CB    1 
ATOM   7157  C  CG    . TRP B 1 180 ? -21.076 -20.894 8.861   1.00 21.04 ? 200  TRP B CG    1 
ATOM   7158  C  CD1   . TRP B 1 180 ? -20.411 -22.013 9.274   1.00 22.45 ? 200  TRP B CD1   1 
ATOM   7159  C  CD2   . TRP B 1 180 ? -21.916 -21.305 7.782   1.00 20.71 ? 200  TRP B CD2   1 
ATOM   7160  N  NE1   . TRP B 1 180 ? -20.787 -23.092 8.516   1.00 21.40 ? 200  TRP B NE1   1 
ATOM   7161  C  CE2   . TRP B 1 180 ? -21.710 -22.685 7.593   1.00 21.03 ? 200  TRP B CE2   1 
ATOM   7162  C  CE3   . TRP B 1 180 ? -22.825 -20.641 6.959   1.00 20.03 ? 200  TRP B CE3   1 
ATOM   7163  C  CZ2   . TRP B 1 180 ? -22.376 -23.411 6.610   1.00 21.42 ? 200  TRP B CZ2   1 
ATOM   7164  C  CZ3   . TRP B 1 180 ? -23.482 -21.360 5.988   1.00 20.77 ? 200  TRP B CZ3   1 
ATOM   7165  C  CH2   . TRP B 1 180 ? -23.255 -22.729 5.816   1.00 21.08 ? 200  TRP B CH2   1 
ATOM   7166  N  N     . LEU B 1 181 ? -21.556 -16.596 7.956   1.00 20.55 ? 201  LEU B N     1 
ATOM   7167  C  CA    . LEU B 1 181 ? -22.025 -15.226 8.037   1.00 20.47 ? 201  LEU B CA    1 
ATOM   7168  C  C     . LEU B 1 181 ? -23.540 -15.240 8.183   1.00 20.35 ? 201  LEU B C     1 
ATOM   7169  O  O     . LEU B 1 181 ? -24.232 -15.888 7.396   1.00 20.94 ? 201  LEU B O     1 
ATOM   7170  C  CB    . LEU B 1 181 ? -21.624 -14.462 6.775   1.00 20.74 ? 201  LEU B CB    1 
ATOM   7171  C  CG    . LEU B 1 181 ? -20.145 -14.564 6.362   1.00 20.92 ? 201  LEU B CG    1 
ATOM   7172  C  CD1   . LEU B 1 181 ? -19.902 -13.793 5.085   1.00 22.15 ? 201  LEU B CD1   1 
ATOM   7173  C  CD2   . LEU B 1 181 ? -19.219 -14.078 7.457   1.00 19.32 ? 201  LEU B CD2   1 
ATOM   7174  N  N     . ILE B 1 182 ? -24.037 -14.566 9.215   1.00 19.75 ? 202  ILE B N     1 
ATOM   7175  C  CA    . ILE B 1 182 ? -25.470 -14.425 9.457   1.00 19.47 ? 202  ILE B CA    1 
ATOM   7176  C  C     . ILE B 1 182 ? -25.953 -13.173 8.737   1.00 19.51 ? 202  ILE B C     1 
ATOM   7177  O  O     . ILE B 1 182 ? -25.509 -12.075 9.045   1.00 20.18 ? 202  ILE B O     1 
ATOM   7178  C  CB    . ILE B 1 182 ? -25.788 -14.300 10.959  1.00 18.84 ? 202  ILE B CB    1 
ATOM   7179  C  CG1   . ILE B 1 182 ? -25.335 -15.545 11.720  1.00 18.79 ? 202  ILE B CG1   1 
ATOM   7180  C  CG2   . ILE B 1 182 ? -27.286 -14.122 11.188  1.00 19.18 ? 202  ILE B CG2   1 
ATOM   7181  C  CD1   . ILE B 1 182 ? -25.180 -15.314 13.239  1.00 17.63 ? 202  ILE B CD1   1 
ATOM   7182  N  N     . ILE B 1 183 ? -26.860 -13.340 7.781   1.00 19.79 ? 203  ILE B N     1 
ATOM   7183  C  CA    . ILE B 1 183 ? -27.375 -12.212 7.005   1.00 19.96 ? 203  ILE B CA    1 
ATOM   7184  C  C     . ILE B 1 183 ? -28.509 -11.548 7.781   1.00 20.23 ? 203  ILE B C     1 
ATOM   7185  O  O     . ILE B 1 183 ? -29.419 -12.218 8.287   1.00 19.85 ? 203  ILE B O     1 
ATOM   7186  C  CB    . ILE B 1 183 ? -27.837 -12.646 5.602   1.00 20.10 ? 203  ILE B CB    1 
ATOM   7187  C  CG1   . ILE B 1 183 ? -26.706 -13.375 4.859   1.00 20.41 ? 203  ILE B CG1   1 
ATOM   7188  C  CG2   . ILE B 1 183 ? -28.270 -11.450 4.785   1.00 20.62 ? 203  ILE B CG2   1 
ATOM   7189  C  CD1   . ILE B 1 183 ? -25.387 -12.598 4.813   1.00 20.27 ? 203  ILE B CD1   1 
ATOM   7190  N  N     . GLN B 1 184 ? -28.427 -10.226 7.887   1.00 20.68 ? 204  GLN B N     1 
ATOM   7191  C  CA    . GLN B 1 184 ? -29.362 -9.432  8.692   1.00 21.25 ? 204  GLN B CA    1 
ATOM   7192  C  C     . GLN B 1 184 ? -29.843 -8.220  7.903   1.00 21.42 ? 204  GLN B C     1 
ATOM   7193  O  O     . GLN B 1 184 ? -29.164 -7.763  6.990   1.00 21.60 ? 204  GLN B O     1 
ATOM   7194  C  CB    . GLN B 1 184 ? -28.668 -8.968  9.984   1.00 21.44 ? 204  GLN B CB    1 
ATOM   7195  C  CG    . GLN B 1 184 ? -28.388 -10.097 10.985  1.00 22.24 ? 204  GLN B CG    1 
ATOM   7196  C  CD    . GLN B 1 184 ? -27.058 -9.967  11.701  1.00 23.28 ? 204  GLN B CD    1 
ATOM   7197  O  OE1   . GLN B 1 184 ? -26.111 -9.364  11.192  1.00 25.41 ? 204  GLN B OE1   1 
ATOM   7198  N  NE2   . GLN B 1 184 ? -26.974 -10.556 12.885  1.00 23.52 ? 204  GLN B NE2   1 
ATOM   7199  N  N     . ARG B 1 185 ? -31.020 -7.716  8.246   1.00 21.58 ? 205  ARG B N     1 
ATOM   7200  C  CA    . ARG B 1 185 ? -31.453 -6.394  7.794   1.00 22.10 ? 205  ARG B CA    1 
ATOM   7201  C  C     . ARG B 1 185 ? -30.748 -5.314  8.593   1.00 22.26 ? 205  ARG B C     1 
ATOM   7202  O  O     . ARG B 1 185 ? -30.840 -5.297  9.821   1.00 21.88 ? 205  ARG B O     1 
ATOM   7203  C  CB    . ARG B 1 185 ? -32.935 -6.197  8.027   1.00 21.86 ? 205  ARG B CB    1 
ATOM   7204  C  CG    . ARG B 1 185 ? -33.824 -6.907  7.073   1.00 22.77 ? 205  ARG B CG    1 
ATOM   7205  C  CD    . ARG B 1 185 ? -35.192 -6.999  7.706   1.00 23.95 ? 205  ARG B CD    1 
ATOM   7206  N  NE    . ARG B 1 185 ? -36.245 -6.813  6.748   1.00 25.15 ? 205  ARG B NE    1 
ATOM   7207  C  CZ    . ARG B 1 185 ? -37.535 -6.962  7.009   1.00 26.41 ? 205  ARG B CZ    1 
ATOM   7208  N  NH1   . ARG B 1 185 ? -37.962 -7.317  8.222   1.00 26.70 ? 205  ARG B NH1   1 
ATOM   7209  N  NH2   . ARG B 1 185 ? -38.404 -6.747  6.036   1.00 27.58 ? 205  ARG B NH2   1 
ATOM   7210  N  N     . TYR B 1 186 ? -30.086 -4.392  7.902   1.00 22.53 ? 206  TYR B N     1 
ATOM   7211  C  CA    . TYR B 1 186 ? -29.379 -3.310  8.590   1.00 23.31 ? 206  TYR B CA    1 
ATOM   7212  C  C     . TYR B 1 186 ? -30.365 -2.205  8.987   1.00 22.61 ? 206  TYR B C     1 
ATOM   7213  O  O     . TYR B 1 186 ? -30.616 -1.282  8.225   1.00 22.92 ? 206  TYR B O     1 
ATOM   7214  C  CB    . TYR B 1 186 ? -28.243 -2.777  7.729   1.00 23.30 ? 206  TYR B CB    1 
ATOM   7215  C  CG    . TYR B 1 186 ? -27.337 -1.808  8.440   1.00 26.75 ? 206  TYR B CG    1 
ATOM   7216  C  CD1   . TYR B 1 186 ? -26.683 -2.168  9.618   1.00 29.05 ? 206  TYR B CD1   1 
ATOM   7217  C  CD2   . TYR B 1 186 ? -27.125 -0.530  7.932   1.00 29.30 ? 206  TYR B CD2   1 
ATOM   7218  C  CE1   . TYR B 1 186 ? -25.849 -1.283  10.267  1.00 30.03 ? 206  TYR B CE1   1 
ATOM   7219  C  CE2   . TYR B 1 186 ? -26.292 0.363   8.575   1.00 30.63 ? 206  TYR B CE2   1 
ATOM   7220  C  CZ    . TYR B 1 186 ? -25.658 -0.021  9.739   1.00 31.14 ? 206  TYR B CZ    1 
ATOM   7221  O  OH    . TYR B 1 186 ? -24.829 0.871   10.370  1.00 33.09 ? 206  TYR B OH    1 
ATOM   7222  N  N     . VAL B 1 187 ? -30.952 -2.358  10.172  1.00 21.88 ? 207  VAL B N     1 
ATOM   7223  C  CA    . VAL B 1 187 ? -31.821 -1.351  10.786  1.00 21.12 ? 207  VAL B CA    1 
ATOM   7224  C  C     . VAL B 1 187 ? -31.333 -1.093  12.204  1.00 21.09 ? 207  VAL B C     1 
ATOM   7225  O  O     . VAL B 1 187 ? -30.379 -1.714  12.644  1.00 21.47 ? 207  VAL B O     1 
ATOM   7226  C  CB    . VAL B 1 187 ? -33.298 -1.813  10.813  1.00 20.86 ? 207  VAL B CB    1 
ATOM   7227  C  CG1   . VAL B 1 187 ? -33.778 -2.078  9.397   1.00 19.59 ? 207  VAL B CG1   1 
ATOM   7228  C  CG2   . VAL B 1 187 ? -33.472 -3.063  11.691  1.00 19.57 ? 207  VAL B CG2   1 
ATOM   7229  N  N     . GLU B 1 188 ? -31.980 -0.169  12.910  1.00 21.26 ? 208  GLU B N     1 
ATOM   7230  C  CA    . GLU B 1 188 ? -31.673 0.103   14.314  1.00 21.33 ? 208  GLU B CA    1 
ATOM   7231  C  C     . GLU B 1 188 ? -31.710 -1.205  15.103  1.00 20.95 ? 208  GLU B C     1 
ATOM   7232  O  O     . GLU B 1 188 ? -32.726 -1.899  15.095  1.00 21.35 ? 208  GLU B O     1 
ATOM   7233  C  CB    . GLU B 1 188 ? -32.689 1.097   14.894  1.00 21.38 ? 208  GLU B CB    1 
ATOM   7234  C  CG    . GLU B 1 188 ? -32.313 1.656   16.261  1.00 22.03 ? 208  GLU B CG    1 
ATOM   7235  C  CD    . GLU B 1 188 ? -33.480 2.350   16.944  1.00 21.96 ? 208  GLU B CD    1 
ATOM   7236  O  OE1   . GLU B 1 188 ? -34.513 2.546   16.286  1.00 23.52 ? 208  GLU B OE1   1 
ATOM   7237  O  OE2   . GLU B 1 188 ? -33.378 2.680   18.144  1.00 20.49 ? 208  GLU B OE2   1 
ATOM   7238  N  N     . GLY B 1 189 ? -30.597 -1.545  15.758  1.00 20.64 ? 209  GLY B N     1 
ATOM   7239  C  CA    . GLY B 1 189 ? -30.451 -2.826  16.465  1.00 20.01 ? 209  GLY B CA    1 
ATOM   7240  C  C     . GLY B 1 189 ? -30.464 -4.034  15.532  1.00 19.81 ? 209  GLY B C     1 
ATOM   7241  O  O     . GLY B 1 189 ? -31.075 -5.075  15.843  1.00 19.04 ? 209  GLY B O     1 
ATOM   7242  N  N     . TYR B 1 190 ? -29.769 -3.884  14.398  1.00 19.36 ? 210  TYR B N     1 
ATOM   7243  C  CA    . TYR B 1 190 ? -29.721 -4.884  13.316  1.00 19.22 ? 210  TYR B CA    1 
ATOM   7244  C  C     . TYR B 1 190 ? -29.384 -6.312  13.755  1.00 18.80 ? 210  TYR B C     1 
ATOM   7245  O  O     . TYR B 1 190 ? -29.736 -7.269  13.060  1.00 19.03 ? 210  TYR B O     1 
ATOM   7246  C  CB    . TYR B 1 190 ? -28.729 -4.448  12.228  1.00 19.59 ? 210  TYR B CB    1 
ATOM   7247  C  CG    . TYR B 1 190 ? -27.294 -4.265  12.693  1.00 20.97 ? 210  TYR B CG    1 
ATOM   7248  C  CD1   . TYR B 1 190 ? -26.375 -5.300  12.624  1.00 23.23 ? 210  TYR B CD1   1 
ATOM   7249  C  CD2   . TYR B 1 190 ? -26.860 -3.051  13.196  1.00 24.69 ? 210  TYR B CD2   1 
ATOM   7250  C  CE1   . TYR B 1 190 ? -25.049 -5.116  13.040  1.00 24.41 ? 210  TYR B CE1   1 
ATOM   7251  C  CE2   . TYR B 1 190 ? -25.545 -2.866  13.629  1.00 25.02 ? 210  TYR B CE2   1 
ATOM   7252  C  CZ    . TYR B 1 190 ? -24.646 -3.899  13.544  1.00 25.21 ? 210  TYR B CZ    1 
ATOM   7253  O  OH    . TYR B 1 190 ? -23.339 -3.688  13.975  1.00 27.44 ? 210  TYR B OH    1 
ATOM   7254  N  N     . PHE B 1 191 ? -28.698 -6.442  14.891  1.00 18.35 ? 211  PHE B N     1 
ATOM   7255  C  CA    . PHE B 1 191 ? -28.321 -7.743  15.465  1.00 17.89 ? 211  PHE B CA    1 
ATOM   7256  C  C     . PHE B 1 191 ? -29.510 -8.705  15.627  1.00 17.63 ? 211  PHE B C     1 
ATOM   7257  O  O     . PHE B 1 191 ? -29.321 -9.924  15.603  1.00 16.92 ? 211  PHE B O     1 
ATOM   7258  C  CB    . PHE B 1 191 ? -27.683 -7.583  16.861  1.00 18.00 ? 211  PHE B CB    1 
ATOM   7259  C  CG    . PHE B 1 191 ? -26.656 -6.495  16.963  1.00 18.08 ? 211  PHE B CG    1 
ATOM   7260  C  CD1   . PHE B 1 191 ? -26.960 -5.313  17.608  1.00 19.03 ? 211  PHE B CD1   1 
ATOM   7261  C  CD2   . PHE B 1 191 ? -25.385 -6.658  16.437  1.00 17.39 ? 211  PHE B CD2   1 
ATOM   7262  C  CE1   . PHE B 1 191 ? -26.010 -4.296  17.718  1.00 20.24 ? 211  PHE B CE1   1 
ATOM   7263  C  CE2   . PHE B 1 191 ? -24.433 -5.653  16.549  1.00 18.13 ? 211  PHE B CE2   1 
ATOM   7264  C  CZ    . PHE B 1 191 ? -24.742 -4.470  17.189  1.00 18.20 ? 211  PHE B CZ    1 
ATOM   7265  N  N     . LEU B 1 192 ? -30.709 -8.154  15.828  1.00 17.30 ? 212  LEU B N     1 
ATOM   7266  C  CA    . LEU B 1 192 ? -31.913 -8.945  16.085  1.00 17.54 ? 212  LEU B CA    1 
ATOM   7267  C  C     . LEU B 1 192 ? -32.789 -9.123  14.845  1.00 17.93 ? 212  LEU B C     1 
ATOM   7268  O  O     . LEU B 1 192 ? -33.974 -9.492  14.951  1.00 17.72 ? 212  LEU B O     1 
ATOM   7269  C  CB    . LEU B 1 192 ? -32.746 -8.289  17.185  1.00 17.70 ? 212  LEU B CB    1 
ATOM   7270  C  CG    . LEU B 1 192 ? -32.028 -7.915  18.479  1.00 17.91 ? 212  LEU B CG    1 
ATOM   7271  C  CD1   . LEU B 1 192 ? -33.058 -7.398  19.516  1.00 18.11 ? 212  LEU B CD1   1 
ATOM   7272  C  CD2   . LEU B 1 192 ? -31.234 -9.103  19.014  1.00 16.56 ? 212  LEU B CD2   1 
ATOM   7273  N  N     . HIS B 1 193 ? -32.209 -8.883  13.670  1.00 18.06 ? 213  HIS B N     1 
ATOM   7274  C  CA    . HIS B 1 193 ? -32.966 -8.944  12.424  1.00 18.22 ? 213  HIS B CA    1 
ATOM   7275  C  C     . HIS B 1 193 ? -32.381 -9.922  11.394  1.00 18.56 ? 213  HIS B C     1 
ATOM   7276  O  O     . HIS B 1 193 ? -32.135 -9.543  10.255  1.00 18.51 ? 213  HIS B O     1 
ATOM   7277  C  CB    . HIS B 1 193 ? -33.099 -7.532  11.844  1.00 18.06 ? 213  HIS B CB    1 
ATOM   7278  C  CG    . HIS B 1 193 ? -33.961 -6.627  12.669  1.00 17.32 ? 213  HIS B CG    1 
ATOM   7279  N  ND1   . HIS B 1 193 ? -35.315 -6.490  12.452  1.00 18.64 ? 213  HIS B ND1   1 
ATOM   7280  C  CD2   . HIS B 1 193 ? -33.666 -5.829  13.723  1.00 16.79 ? 213  HIS B CD2   1 
ATOM   7281  C  CE1   . HIS B 1 193 ? -35.816 -5.641  13.335  1.00 17.81 ? 213  HIS B CE1   1 
ATOM   7282  N  NE2   . HIS B 1 193 ? -34.837 -5.232  14.120  1.00 16.99 ? 213  HIS B NE2   1 
ATOM   7283  N  N     . PRO B 1 194 ? -32.184 -11.194 11.788  1.00 18.64 ? 214  PRO B N     1 
ATOM   7284  C  CA    . PRO B 1 194 ? -31.727 -12.185 10.806  1.00 19.13 ? 214  PRO B CA    1 
ATOM   7285  C  C     . PRO B 1 194 ? -32.772 -12.460 9.723   1.00 19.57 ? 214  PRO B C     1 
ATOM   7286  O  O     . PRO B 1 194 ? -33.974 -12.439 10.008  1.00 19.80 ? 214  PRO B O     1 
ATOM   7287  C  CB    . PRO B 1 194 ? -31.525 -13.440 11.651  1.00 18.97 ? 214  PRO B CB    1 
ATOM   7288  C  CG    . PRO B 1 194 ? -32.515 -13.300 12.753  1.00 18.18 ? 214  PRO B CG    1 
ATOM   7289  C  CD    . PRO B 1 194 ? -32.491 -11.823 13.083  1.00 18.54 ? 214  PRO B CD    1 
ATOM   7290  N  N     . THR B 1 195 ? -32.317 -12.721 8.501   1.00 19.89 ? 215  THR B N     1 
ATOM   7291  C  CA    . THR B 1 195 ? -33.223 -12.974 7.373   1.00 20.24 ? 215  THR B CA    1 
ATOM   7292  C  C     . THR B 1 195 ? -33.551 -14.450 7.140   1.00 20.61 ? 215  THR B C     1 
ATOM   7293  O  O     . THR B 1 195 ? -34.542 -14.764 6.476   1.00 20.93 ? 215  THR B O     1 
ATOM   7294  C  CB    . THR B 1 195 ? -32.607 -12.454 6.077   1.00 20.29 ? 215  THR B CB    1 
ATOM   7295  O  OG1   . THR B 1 195 ? -31.373 -13.153 5.841   1.00 20.34 ? 215  THR B OG1   1 
ATOM   7296  C  CG2   . THR B 1 195 ? -32.350 -10.949 6.189   1.00 19.63 ? 215  THR B CG2   1 
ATOM   7297  N  N     . GLY B 1 196 ? -32.709 -15.350 7.661   1.00 20.56 ? 216  GLY B N     1 
ATOM   7298  C  CA    . GLY B 1 196 ? -32.854 -16.783 7.423   1.00 20.21 ? 216  GLY B CA    1 
ATOM   7299  C  C     . GLY B 1 196 ? -31.780 -17.347 6.524   1.00 20.19 ? 216  GLY B C     1 
ATOM   7300  O  O     . GLY B 1 196 ? -31.668 -18.565 6.377   1.00 20.04 ? 216  GLY B O     1 
ATOM   7301  N  N     . LEU B 1 197 ? -30.995 -16.459 5.920   1.00 20.11 ? 217  LEU B N     1 
ATOM   7302  C  CA    . LEU B 1 197 ? -29.872 -16.841 5.077   1.00 20.31 ? 217  LEU B CA    1 
ATOM   7303  C  C     . LEU B 1 197 ? -28.581 -16.787 5.884   1.00 20.61 ? 217  LEU B C     1 
ATOM   7304  O  O     . LEU B 1 197 ? -28.331 -15.812 6.599   1.00 20.98 ? 217  LEU B O     1 
ATOM   7305  C  CB    . LEU B 1 197 ? -29.757 -15.884 3.885   1.00 20.28 ? 217  LEU B CB    1 
ATOM   7306  C  CG    . LEU B 1 197 ? -28.696 -16.275 2.841   1.00 20.43 ? 217  LEU B CG    1 
ATOM   7307  C  CD1   . LEU B 1 197 ? -29.060 -17.593 2.163   1.00 21.55 ? 217  LEU B CD1   1 
ATOM   7308  C  CD2   . LEU B 1 197 ? -28.519 -15.180 1.815   1.00 18.41 ? 217  LEU B CD2   1 
ATOM   7309  N  N     . GLU B 1 198 ? -27.778 -17.837 5.772   1.00 21.04 ? 218  GLU B N     1 
ATOM   7310  C  CA    . GLU B 1 198 ? -26.397 -17.839 6.248   1.00 21.42 ? 218  GLU B CA    1 
ATOM   7311  C  C     . GLU B 1 198 ? -25.496 -18.330 5.131   1.00 21.70 ? 218  GLU B C     1 
ATOM   7312  O  O     . GLU B 1 198 ? -25.928 -19.119 4.295   1.00 21.31 ? 218  GLU B O     1 
ATOM   7313  C  CB    . GLU B 1 198 ? -26.246 -18.737 7.479   1.00 21.41 ? 218  GLU B CB    1 
ATOM   7314  C  CG    . GLU B 1 198 ? -27.208 -18.337 8.609   1.00 22.42 ? 218  GLU B CG    1 
ATOM   7315  C  CD    . GLU B 1 198 ? -27.001 -19.126 9.881   1.00 22.64 ? 218  GLU B CD    1 
ATOM   7316  O  OE1   . GLU B 1 198 ? -26.295 -20.151 9.842   1.00 21.61 ? 218  GLU B OE1   1 
ATOM   7317  O  OE2   . GLU B 1 198 ? -27.545 -18.706 10.925  1.00 23.05 ? 218  GLU B OE2   1 
ATOM   7318  N  N     . LEU B 1 199 ? -24.253 -17.853 5.126   1.00 21.91 ? 219  LEU B N     1 
ATOM   7319  C  CA    . LEU B 1 199 ? -23.305 -18.122 4.047   1.00 22.59 ? 219  LEU B CA    1 
ATOM   7320  C  C     . LEU B 1 199 ? -21.926 -18.478 4.596   1.00 22.29 ? 219  LEU B C     1 
ATOM   7321  O  O     . LEU B 1 199 ? -21.408 -17.793 5.481   1.00 21.74 ? 219  LEU B O     1 
ATOM   7322  C  CB    . LEU B 1 199 ? -23.158 -16.887 3.158   1.00 23.06 ? 219  LEU B CB    1 
ATOM   7323  C  CG    . LEU B 1 199 ? -24.408 -16.416 2.411   1.00 24.68 ? 219  LEU B CG    1 
ATOM   7324  C  CD1   . LEU B 1 199 ? -24.201 -15.026 1.813   1.00 26.20 ? 219  LEU B CD1   1 
ATOM   7325  C  CD2   . LEU B 1 199 ? -24.758 -17.411 1.338   1.00 27.08 ? 219  LEU B CD2   1 
ATOM   7326  N  N     . LEU B 1 200 ? -21.341 -19.546 4.065   1.00 22.08 ? 220  LEU B N     1 
ATOM   7327  C  CA    . LEU B 1 200 ? -19.988 -19.938 4.416   1.00 22.24 ? 220  LEU B CA    1 
ATOM   7328  C  C     . LEU B 1 200 ? -19.031 -19.441 3.346   1.00 22.47 ? 220  LEU B C     1 
ATOM   7329  O  O     . LEU B 1 200 ? -19.175 -19.778 2.161   1.00 22.32 ? 220  LEU B O     1 
ATOM   7330  C  CB    . LEU B 1 200 ? -19.886 -21.452 4.561   1.00 22.06 ? 220  LEU B CB    1 
ATOM   7331  C  CG    . LEU B 1 200 ? -18.514 -22.020 4.933   1.00 22.29 ? 220  LEU B CG    1 
ATOM   7332  C  CD1   . LEU B 1 200 ? -17.993 -21.457 6.259   1.00 21.57 ? 220  LEU B CD1   1 
ATOM   7333  C  CD2   . LEU B 1 200 ? -18.587 -23.551 4.965   1.00 22.80 ? 220  LEU B CD2   1 
ATOM   7334  N  N     . VAL B 1 201 ? -18.054 -18.645 3.769   1.00 22.75 ? 221  VAL B N     1 
ATOM   7335  C  CA    . VAL B 1 201 ? -17.101 -18.023 2.857   1.00 22.75 ? 221  VAL B CA    1 
ATOM   7336  C  C     . VAL B 1 201 ? -15.678 -18.457 3.189   1.00 22.95 ? 221  VAL B C     1 
ATOM   7337  O  O     . VAL B 1 201 ? -15.236 -18.327 4.329   1.00 22.35 ? 221  VAL B O     1 
ATOM   7338  C  CB    . VAL B 1 201 ? -17.201 -16.492 2.937   1.00 22.87 ? 221  VAL B CB    1 
ATOM   7339  C  CG1   . VAL B 1 201 ? -16.095 -15.826 2.112   1.00 23.50 ? 221  VAL B CG1   1 
ATOM   7340  C  CG2   . VAL B 1 201 ? -18.588 -16.012 2.482   1.00 22.96 ? 221  VAL B CG2   1 
ATOM   7341  N  N     . ASP B 1 202 ? -14.966 -18.995 2.204   1.00 23.31 ? 222  ASP B N     1 
ATOM   7342  C  CA    . ASP B 1 202 ? -13.550 -19.301 2.382   1.00 23.79 ? 222  ASP B CA    1 
ATOM   7343  C  C     . ASP B 1 202 ? -12.769 -18.050 2.006   1.00 23.94 ? 222  ASP B C     1 
ATOM   7344  O  O     . ASP B 1 202 ? -12.735 -17.674 0.839   1.00 24.37 ? 222  ASP B O     1 
ATOM   7345  C  CB    . ASP B 1 202 ? -13.124 -20.487 1.509   1.00 24.05 ? 222  ASP B CB    1 
ATOM   7346  C  CG    . ASP B 1 202 ? -11.677 -20.933 1.775   1.00 24.77 ? 222  ASP B CG    1 
ATOM   7347  O  OD1   . ASP B 1 202 ? -10.896 -20.181 2.394   1.00 25.36 ? 222  ASP B OD1   1 
ATOM   7348  O  OD2   . ASP B 1 202 ? -11.316 -22.055 1.370   1.00 27.69 ? 222  ASP B OD2   1 
ATOM   7349  N  N     . HIS B 1 203 ? -12.167 -17.397 2.997   1.00 24.11 ? 223  HIS B N     1 
ATOM   7350  C  CA    . HIS B 1 203 ? -11.393 -16.177 2.755   1.00 23.97 ? 223  HIS B CA    1 
ATOM   7351  C  C     . HIS B 1 203 ? -9.957  -16.282 3.264   1.00 24.29 ? 223  HIS B C     1 
ATOM   7352  O  O     . HIS B 1 203 ? -9.418  -15.331 3.799   1.00 24.31 ? 223  HIS B O     1 
ATOM   7353  C  CB    . HIS B 1 203 ? -12.107 -14.928 3.307   1.00 23.91 ? 223  HIS B CB    1 
ATOM   7354  C  CG    . HIS B 1 203 ? -12.444 -14.987 4.766   1.00 23.40 ? 223  HIS B CG    1 
ATOM   7355  N  ND1   . HIS B 1 203 ? -11.819 -14.192 5.706   1.00 22.96 ? 223  HIS B ND1   1 
ATOM   7356  C  CD2   . HIS B 1 203 ? -13.383 -15.696 5.437   1.00 22.82 ? 223  HIS B CD2   1 
ATOM   7357  C  CE1   . HIS B 1 203 ? -12.342 -14.432 6.898   1.00 23.04 ? 223  HIS B CE1   1 
ATOM   7358  N  NE2   . HIS B 1 203 ? -13.287 -15.345 6.763   1.00 22.71 ? 223  HIS B NE2   1 
ATOM   7359  N  N     . GLY B 1 204 ? -9.334  -17.435 3.047   1.00 25.09 ? 224  GLY B N     1 
ATOM   7360  C  CA    . GLY B 1 204 ? -7.977  -17.690 3.536   1.00 25.90 ? 224  GLY B CA    1 
ATOM   7361  C  C     . GLY B 1 204 ? -6.860  -17.097 2.691   1.00 26.53 ? 224  GLY B C     1 
ATOM   7362  O  O     . GLY B 1 204 ? -5.835  -16.658 3.217   1.00 26.53 ? 224  GLY B O     1 
ATOM   7363  N  N     . SER B 1 205 ? -7.044  -17.098 1.376   1.00 27.33 ? 225  SER B N     1 
ATOM   7364  C  CA    . SER B 1 205 ? -6.012  -16.595 0.465   1.00 27.82 ? 225  SER B CA    1 
ATOM   7365  C  C     . SER B 1 205 ? -5.830  -15.096 0.633   1.00 27.80 ? 225  SER B C     1 
ATOM   7366  O  O     . SER B 1 205 ? -6.793  -14.374 0.882   1.00 27.72 ? 225  SER B O     1 
ATOM   7367  C  CB    . SER B 1 205 ? -6.385  -16.886 -0.987  1.00 27.93 ? 225  SER B CB    1 
ATOM   7368  O  OG    . SER B 1 205 ? -5.543  -16.167 -1.868  1.00 29.01 ? 225  SER B OG    1 
ATOM   7369  N  N     . THR B 1 206 ? -4.599  -14.634 0.463   1.00 27.76 ? 226  THR B N     1 
ATOM   7370  C  CA    . THR B 1 206 ? -4.305  -13.206 0.457   1.00 28.23 ? 226  THR B CA    1 
ATOM   7371  C  C     . THR B 1 206 ? -4.804  -12.502 -0.811  1.00 28.54 ? 226  THR B C     1 
ATOM   7372  O  O     . THR B 1 206 ? -4.793  -11.274 -0.879  1.00 29.04 ? 226  THR B O     1 
ATOM   7373  C  CB    . THR B 1 206 ? -2.799  -12.955 0.580   1.00 28.13 ? 226  THR B CB    1 
ATOM   7374  O  OG1   . THR B 1 206 ? -2.122  -13.610 -0.499  1.00 28.76 ? 226  THR B OG1   1 
ATOM   7375  C  CG2   . THR B 1 206 ? -2.284  -13.491 1.899   1.00 27.88 ? 226  THR B CG2   1 
ATOM   7376  N  N     . ASP B 1 207 ? -5.214  -13.275 -1.816  1.00 28.71 ? 227  ASP B N     1 
ATOM   7377  C  CA    . ASP B 1 207 ? -5.853  -12.731 -3.003  1.00 29.13 ? 227  ASP B CA    1 
ATOM   7378  C  C     . ASP B 1 207 ? -7.364  -12.922 -2.856  1.00 29.03 ? 227  ASP B C     1 
ATOM   7379  O  O     . ASP B 1 207 ? -7.887  -14.018 -3.031  1.00 28.78 ? 227  ASP B O     1 
ATOM   7380  C  CB    . ASP B 1 207 ? -5.327  -13.432 -4.258  1.00 29.39 ? 227  ASP B CB    1 
ATOM   7381  C  CG    . ASP B 1 207 ? -5.877  -12.830 -5.555  1.00 31.32 ? 227  ASP B CG    1 
ATOM   7382  O  OD1   . ASP B 1 207 ? -6.858  -12.055 -5.514  1.00 32.28 ? 227  ASP B OD1   1 
ATOM   7383  O  OD2   . ASP B 1 207 ? -5.318  -13.143 -6.629  1.00 34.22 ? 227  ASP B OD2   1 
ATOM   7384  N  N     . ALA B 1 208 ? -8.056  -11.836 -2.540  1.00 29.21 ? 228  ALA B N     1 
ATOM   7385  C  CA    . ALA B 1 208 ? -9.488  -11.873 -2.304  1.00 29.63 ? 228  ALA B CA    1 
ATOM   7386  C  C     . ALA B 1 208 ? -10.221 -12.367 -3.540  1.00 30.10 ? 228  ALA B C     1 
ATOM   7387  O  O     . ALA B 1 208 ? -11.360 -12.821 -3.449  1.00 29.82 ? 228  ALA B O     1 
ATOM   7388  C  CB    . ALA B 1 208 ? -9.996  -10.504 -1.897  1.00 29.38 ? 228  ALA B CB    1 
ATOM   7389  N  N     . GLY B 1 209 ? -9.556  -12.278 -4.690  1.00 30.48 ? 229  GLY B N     1 
ATOM   7390  C  CA    . GLY B 1 209 ? -10.054 -12.871 -5.921  1.00 31.05 ? 229  GLY B CA    1 
ATOM   7391  C  C     . GLY B 1 209 ? -10.373 -14.348 -5.817  1.00 31.30 ? 229  GLY B C     1 
ATOM   7392  O  O     . GLY B 1 209 ? -11.278 -14.819 -6.489  1.00 31.84 ? 229  GLY B O     1 
ATOM   7393  N  N     . HIS B 1 210 ? -9.641  -15.081 -4.977  1.00 31.58 ? 230  HIS B N     1 
ATOM   7394  C  CA    . HIS B 1 210 ? -9.901  -16.506 -4.760  1.00 31.81 ? 230  HIS B CA    1 
ATOM   7395  C  C     . HIS B 1 210 ? -11.053 -16.825 -3.796  1.00 31.24 ? 230  HIS B C     1 
ATOM   7396  O  O     . HIS B 1 210 ? -11.454 -17.983 -3.692  1.00 31.40 ? 230  HIS B O     1 
ATOM   7397  C  CB    . HIS B 1 210 ? -8.650  -17.203 -4.220  1.00 32.48 ? 230  HIS B CB    1 
ATOM   7398  C  CG    . HIS B 1 210 ? -7.471  -17.144 -5.142  1.00 34.97 ? 230  HIS B CG    1 
ATOM   7399  N  ND1   . HIS B 1 210 ? -6.184  -16.941 -4.689  1.00 37.80 ? 230  HIS B ND1   1 
ATOM   7400  C  CD2   . HIS B 1 210 ? -7.382  -17.267 -6.488  1.00 36.79 ? 230  HIS B CD2   1 
ATOM   7401  C  CE1   . HIS B 1 210 ? -5.353  -16.943 -5.717  1.00 38.39 ? 230  HIS B CE1   1 
ATOM   7402  N  NE2   . HIS B 1 210 ? -6.054  -17.137 -6.819  1.00 38.24 ? 230  HIS B NE2   1 
ATOM   7403  N  N     . TRP B 1 211 ? -11.567 -15.826 -3.078  1.00 30.39 ? 231  TRP B N     1 
ATOM   7404  C  CA    . TRP B 1 211 ? -12.559 -16.073 -2.022  1.00 29.78 ? 231  TRP B CA    1 
ATOM   7405  C  C     . TRP B 1 211 ? -13.877 -16.555 -2.614  1.00 29.54 ? 231  TRP B C     1 
ATOM   7406  O  O     . TRP B 1 211 ? -14.303 -16.075 -3.658  1.00 29.73 ? 231  TRP B O     1 
ATOM   7407  C  CB    . TRP B 1 211 ? -12.801 -14.811 -1.194  1.00 29.44 ? 231  TRP B CB    1 
ATOM   7408  C  CG    . TRP B 1 211 ? -11.614 -14.370 -0.399  1.00 27.93 ? 231  TRP B CG    1 
ATOM   7409  C  CD1   . TRP B 1 211 ? -10.366 -14.925 -0.397  1.00 26.89 ? 231  TRP B CD1   1 
ATOM   7410  C  CD2   . TRP B 1 211 ? -11.556 -13.254 0.490   1.00 27.04 ? 231  TRP B CD2   1 
ATOM   7411  N  NE1   . TRP B 1 211 ? -9.546  -14.237 0.457   1.00 25.37 ? 231  TRP B NE1   1 
ATOM   7412  C  CE2   . TRP B 1 211 ? -10.250 -13.202 1.010   1.00 26.39 ? 231  TRP B CE2   1 
ATOM   7413  C  CE3   . TRP B 1 211 ? -12.485 -12.290 0.900   1.00 28.13 ? 231  TRP B CE3   1 
ATOM   7414  C  CZ2   . TRP B 1 211 ? -9.847  -12.222 1.918   1.00 27.06 ? 231  TRP B CZ2   1 
ATOM   7415  C  CZ3   . TRP B 1 211 ? -12.084 -11.319 1.810   1.00 27.14 ? 231  TRP B CZ3   1 
ATOM   7416  C  CH2   . TRP B 1 211 ? -10.783 -11.300 2.314   1.00 27.08 ? 231  TRP B CH2   1 
ATOM   7417  N  N     . ALA B 1 212 ? -14.520 -17.499 -1.940  1.00 28.96 ? 232  ALA B N     1 
ATOM   7418  C  CA    . ALA B 1 212 ? -15.728 -18.105 -2.485  1.00 28.57 ? 232  ALA B CA    1 
ATOM   7419  C  C     . ALA B 1 212 ? -16.762 -18.392 -1.415  1.00 27.85 ? 232  ALA B C     1 
ATOM   7420  O  O     . ALA B 1 212 ? -16.422 -18.759 -0.293  1.00 26.85 ? 232  ALA B O     1 
ATOM   7421  C  CB    . ALA B 1 212 ? -15.373 -19.399 -3.230  1.00 28.43 ? 232  ALA B CB    1 
ATOM   7422  N  N     . VAL B 1 213 ? -18.031 -18.234 -1.792  1.00 27.54 ? 233  VAL B N     1 
ATOM   7423  C  CA    . VAL B 1 213 ? -19.138 -18.812 -1.043  1.00 27.14 ? 233  VAL B CA    1 
ATOM   7424  C  C     . VAL B 1 213 ? -19.119 -20.308 -1.347  1.00 27.28 ? 233  VAL B C     1 
ATOM   7425  O  O     . VAL B 1 213 ? -19.321 -20.703 -2.479  1.00 27.79 ? 233  VAL B O     1 
ATOM   7426  C  CB    . VAL B 1 213 ? -20.491 -18.212 -1.464  1.00 27.12 ? 233  VAL B CB    1 
ATOM   7427  C  CG1   . VAL B 1 213 ? -21.655 -18.825 -0.651  1.00 26.53 ? 233  VAL B CG1   1 
ATOM   7428  C  CG2   . VAL B 1 213 ? -20.468 -16.692 -1.322  1.00 26.96 ? 233  VAL B CG2   1 
ATOM   7429  N  N     . GLU B 1 214 ? -18.832 -21.137 -0.351  1.00 27.48 ? 234  GLU B N     1 
ATOM   7430  C  CA    . GLU B 1 214 ? -18.743 -22.586 -0.573  1.00 27.73 ? 234  GLU B CA    1 
ATOM   7431  C  C     . GLU B 1 214 ? -19.998 -23.323 -0.121  1.00 27.43 ? 234  GLU B C     1 
ATOM   7432  O  O     . GLU B 1 214 ? -20.152 -24.510 -0.395  1.00 27.25 ? 234  GLU B O     1 
ATOM   7433  C  CB    . GLU B 1 214 ? -17.510 -23.184 0.109   1.00 27.85 ? 234  GLU B CB    1 
ATOM   7434  C  CG    . GLU B 1 214 ? -17.438 -23.006 1.617   1.00 28.77 ? 234  GLU B CG    1 
ATOM   7435  C  CD    . GLU B 1 214 ? -16.274 -23.765 2.238   1.00 29.36 ? 234  GLU B CD    1 
ATOM   7436  O  OE1   . GLU B 1 214 ? -15.312 -23.123 2.716   1.00 29.37 ? 234  GLU B OE1   1 
ATOM   7437  O  OE2   . GLU B 1 214 ? -16.328 -25.013 2.259   1.00 29.50 ? 234  GLU B OE2   1 
ATOM   7438  N  N     . GLN B 1 215 ? -20.888 -22.621 0.567   1.00 27.02 ? 235  GLN B N     1 
ATOM   7439  C  CA    . GLN B 1 215 ? -22.094 -23.239 1.101   1.00 27.01 ? 235  GLN B CA    1 
ATOM   7440  C  C     . GLN B 1 215 ? -23.088 -22.157 1.491   1.00 25.85 ? 235  GLN B C     1 
ATOM   7441  O  O     . GLN B 1 215 ? -22.706 -21.052 1.861   1.00 24.91 ? 235  GLN B O     1 
ATOM   7442  C  CB    . GLN B 1 215 ? -21.752 -24.135 2.308   1.00 27.45 ? 235  GLN B CB    1 
ATOM   7443  C  CG    . GLN B 1 215 ? -22.897 -25.011 2.833   1.00 29.76 ? 235  GLN B CG    1 
ATOM   7444  C  CD    . GLN B 1 215 ? -23.558 -25.866 1.757   1.00 32.26 ? 235  GLN B CD    1 
ATOM   7445  O  OE1   . GLN B 1 215 ? -24.426 -25.392 1.017   1.00 34.72 ? 235  GLN B OE1   1 
ATOM   7446  N  NE2   . GLN B 1 215 ? -23.172 -27.135 1.687   1.00 31.87 ? 235  GLN B NE2   1 
ATOM   7447  N  N     . VAL B 1 216 ? -24.366 -22.493 1.397   1.00 25.17 ? 236  VAL B N     1 
ATOM   7448  C  CA    . VAL B 1 216 ? -25.439 -21.551 1.662   1.00 24.81 ? 236  VAL B CA    1 
ATOM   7449  C  C     . VAL B 1 216 ? -26.512 -22.262 2.470   1.00 24.27 ? 236  VAL B C     1 
ATOM   7450  O  O     . VAL B 1 216 ? -26.850 -23.398 2.158   1.00 23.63 ? 236  VAL B O     1 
ATOM   7451  C  CB    . VAL B 1 216 ? -26.040 -21.048 0.327   1.00 25.08 ? 236  VAL B CB    1 
ATOM   7452  C  CG1   . VAL B 1 216 ? -27.294 -20.230 0.569   1.00 24.62 ? 236  VAL B CG1   1 
ATOM   7453  C  CG2   . VAL B 1 216 ? -24.986 -20.260 -0.466  1.00 24.97 ? 236  VAL B CG2   1 
ATOM   7454  N  N     . TRP B 1 217 ? -27.042 -21.592 3.497   1.00 23.65 ? 237  TRP B N     1 
ATOM   7455  C  CA    . TRP B 1 217 ? -28.108 -22.144 4.329   1.00 23.18 ? 237  TRP B CA    1 
ATOM   7456  C  C     . TRP B 1 217 ? -29.255 -21.163 4.353   1.00 22.98 ? 237  TRP B C     1 
ATOM   7457  O  O     . TRP B 1 217 ? -29.064 -19.981 4.654   1.00 22.57 ? 237  TRP B O     1 
ATOM   7458  C  CB    . TRP B 1 217 ? -27.611 -22.399 5.754   1.00 23.55 ? 237  TRP B CB    1 
ATOM   7459  C  CG    . TRP B 1 217 ? -28.606 -23.048 6.697   1.00 23.65 ? 237  TRP B CG    1 
ATOM   7460  C  CD1   . TRP B 1 217 ? -28.749 -24.380 6.940   1.00 24.28 ? 237  TRP B CD1   1 
ATOM   7461  C  CD2   . TRP B 1 217 ? -29.570 -22.384 7.539   1.00 24.96 ? 237  TRP B CD2   1 
ATOM   7462  N  NE1   . TRP B 1 217 ? -29.744 -24.593 7.872   1.00 24.66 ? 237  TRP B NE1   1 
ATOM   7463  C  CE2   . TRP B 1 217 ? -30.258 -23.383 8.258   1.00 25.30 ? 237  TRP B CE2   1 
ATOM   7464  C  CE3   . TRP B 1 217 ? -29.920 -21.046 7.748   1.00 24.85 ? 237  TRP B CE3   1 
ATOM   7465  C  CZ2   . TRP B 1 217 ? -31.270 -23.082 9.178   1.00 25.61 ? 237  TRP B CZ2   1 
ATOM   7466  C  CZ3   . TRP B 1 217 ? -30.933 -20.749 8.655   1.00 24.33 ? 237  TRP B CZ3   1 
ATOM   7467  C  CH2   . TRP B 1 217 ? -31.598 -21.761 9.349   1.00 25.62 ? 237  TRP B CH2   1 
ATOM   7468  N  N     . TYR B 1 218 ? -30.446 -21.647 4.012   1.00 22.59 ? 238  TYR B N     1 
ATOM   7469  C  CA    . TYR B 1 218 ? -31.639 -20.821 4.076   1.00 22.55 ? 238  TYR B CA    1 
ATOM   7470  C  C     . TYR B 1 218 ? -32.809 -21.574 4.693   1.00 22.68 ? 238  TYR B C     1 
ATOM   7471  O  O     . TYR B 1 218 ? -33.204 -22.629 4.193   1.00 22.57 ? 238  TYR B O     1 
ATOM   7472  C  CB    . TYR B 1 218 ? -32.043 -20.280 2.699   1.00 22.18 ? 238  TYR B CB    1 
ATOM   7473  C  CG    . TYR B 1 218 ? -33.291 -19.458 2.820   1.00 21.67 ? 238  TYR B CG    1 
ATOM   7474  C  CD1   . TYR B 1 218 ? -33.252 -18.211 3.432   1.00 21.78 ? 238  TYR B CD1   1 
ATOM   7475  C  CD2   . TYR B 1 218 ? -34.528 -19.952 2.412   1.00 20.91 ? 238  TYR B CD2   1 
ATOM   7476  C  CE1   . TYR B 1 218 ? -34.397 -17.466 3.609   1.00 21.00 ? 238  TYR B CE1   1 
ATOM   7477  C  CE2   . TYR B 1 218 ? -35.683 -19.199 2.573   1.00 20.33 ? 238  TYR B CE2   1 
ATOM   7478  C  CZ    . TYR B 1 218 ? -35.604 -17.953 3.178   1.00 20.38 ? 238  TYR B CZ    1 
ATOM   7479  O  OH    . TYR B 1 218 ? -36.723 -17.180 3.373   1.00 19.25 ? 238  TYR B OH    1 
ATOM   7480  N  N     . ASN B 1 219 ? -33.359 -21.020 5.774   1.00 22.93 ? 239  ASN B N     1 
ATOM   7481  C  CA    . ASN B 1 219 ? -34.578 -21.537 6.386   1.00 23.44 ? 239  ASN B CA    1 
ATOM   7482  C  C     . ASN B 1 219 ? -34.539 -23.054 6.526   1.00 24.13 ? 239  ASN B C     1 
ATOM   7483  O  O     . ASN B 1 219 ? -35.441 -23.749 6.078   1.00 24.11 ? 239  ASN B O     1 
ATOM   7484  C  CB    . ASN B 1 219 ? -35.808 -21.107 5.571   1.00 23.39 ? 239  ASN B CB    1 
ATOM   7485  C  CG    . ASN B 1 219 ? -37.125 -21.310 6.329   1.00 23.77 ? 239  ASN B CG    1 
ATOM   7486  O  OD1   . ASN B 1 219 ? -37.156 -21.311 7.562   1.00 23.76 ? 239  ASN B OD1   1 
ATOM   7487  N  ND2   . ASN B 1 219 ? -38.218 -21.468 5.588   1.00 22.05 ? 239  ASN B ND2   1 
ATOM   7488  N  N     . GLY B 1 220 ? -33.450 -23.558 7.104   1.00 24.76 ? 240  GLY B N     1 
ATOM   7489  C  CA    . GLY B 1 220 ? -33.351 -24.970 7.474   1.00 25.10 ? 240  GLY B CA    1 
ATOM   7490  C  C     . GLY B 1 220 ? -32.805 -25.929 6.430   1.00 25.53 ? 240  GLY B C     1 
ATOM   7491  O  O     . GLY B 1 220 ? -32.729 -27.119 6.699   1.00 26.25 ? 240  GLY B O     1 
ATOM   7492  N  N     . LYS B 1 221 ? -32.434 -25.441 5.245   1.00 26.06 ? 241  LYS B N     1 
ATOM   7493  C  CA    . LYS B 1 221 ? -31.884 -26.300 4.184   1.00 26.47 ? 241  LYS B CA    1 
ATOM   7494  C  C     . LYS B 1 221 ? -30.576 -25.733 3.653   1.00 25.91 ? 241  LYS B C     1 
ATOM   7495  O  O     . LYS B 1 221 ? -30.413 -24.518 3.586   1.00 25.09 ? 241  LYS B O     1 
ATOM   7496  C  CB    . LYS B 1 221 ? -32.856 -26.435 3.006   1.00 26.83 ? 241  LYS B CB    1 
ATOM   7497  C  CG    . LYS B 1 221 ? -34.281 -26.835 3.367   1.00 29.28 ? 241  LYS B CG    1 
ATOM   7498  C  CD    . LYS B 1 221 ? -34.367 -28.252 3.891   1.00 31.93 ? 241  LYS B CD    1 
ATOM   7499  C  CE    . LYS B 1 221 ? -35.788 -28.594 4.320   1.00 33.01 ? 241  LYS B CE    1 
ATOM   7500  N  NZ    . LYS B 1 221 ? -35.798 -29.857 5.089   1.00 34.41 ? 241  LYS B NZ    1 
ATOM   7501  N  N     . PHE B 1 222 ? -29.661 -26.624 3.265   1.00 25.91 ? 242  PHE B N     1 
ATOM   7502  C  CA    . PHE B 1 222 ? -28.432 -26.234 2.578   1.00 26.31 ? 242  PHE B CA    1 
ATOM   7503  C  C     . PHE B 1 222 ? -28.647 -26.205 1.064   1.00 27.00 ? 242  PHE B C     1 
ATOM   7504  O  O     . PHE B 1 222 ? -29.395 -27.028 0.528   1.00 27.35 ? 242  PHE B O     1 
ATOM   7505  C  CB    . PHE B 1 222 ? -27.290 -27.182 2.927   1.00 26.03 ? 242  PHE B CB    1 
ATOM   7506  C  CG    . PHE B 1 222 ? -26.904 -27.150 4.371   1.00 26.20 ? 242  PHE B CG    1 
ATOM   7507  C  CD1   . PHE B 1 222 ? -25.970 -26.227 4.831   1.00 26.17 ? 242  PHE B CD1   1 
ATOM   7508  C  CD2   . PHE B 1 222 ? -27.471 -28.038 5.279   1.00 25.58 ? 242  PHE B CD2   1 
ATOM   7509  C  CE1   . PHE B 1 222 ? -25.601 -26.196 6.162   1.00 26.51 ? 242  PHE B CE1   1 
ATOM   7510  C  CE2   . PHE B 1 222 ? -27.108 -28.011 6.619   1.00 25.41 ? 242  PHE B CE2   1 
ATOM   7511  C  CZ    . PHE B 1 222 ? -26.168 -27.088 7.060   1.00 26.45 ? 242  PHE B CZ    1 
ATOM   7512  N  N     . TYR B 1 223 ? -27.989 -25.266 0.383   1.00 27.45 ? 243  TYR B N     1 
ATOM   7513  C  CA    . TYR B 1 223 ? -28.161 -25.096 -1.057  1.00 28.11 ? 243  TYR B CA    1 
ATOM   7514  C  C     . TYR B 1 223 ? -26.885 -25.070 -1.892  1.00 29.01 ? 243  TYR B C     1 
ATOM   7515  O  O     . TYR B 1 223 ? -26.980 -24.985 -3.117  1.00 30.42 ? 243  TYR B O     1 
ATOM   7516  C  CB    . TYR B 1 223 ? -28.971 -23.837 -1.352  1.00 27.97 ? 243  TYR B CB    1 
ATOM   7517  C  CG    . TYR B 1 223 ? -30.420 -23.964 -0.950  1.00 27.91 ? 243  TYR B CG    1 
ATOM   7518  C  CD1   . TYR B 1 223 ? -31.350 -24.547 -1.808  1.00 27.93 ? 243  TYR B CD1   1 
ATOM   7519  C  CD2   . TYR B 1 223 ? -30.859 -23.513 0.289   1.00 27.33 ? 243  TYR B CD2   1 
ATOM   7520  C  CE1   . TYR B 1 223 ? -32.680 -24.669 -1.445  1.00 28.02 ? 243  TYR B CE1   1 
ATOM   7521  C  CE2   . TYR B 1 223 ? -32.185 -23.626 0.663   1.00 27.84 ? 243  TYR B CE2   1 
ATOM   7522  C  CZ    . TYR B 1 223 ? -33.090 -24.208 -0.203  1.00 27.45 ? 243  TYR B CZ    1 
ATOM   7523  O  OH    . TYR B 1 223 ? -34.402 -24.313 0.160   1.00 27.24 ? 243  TYR B OH    1 
ATOM   7524  N  N     . GLY B 1 224 ? -25.701 -25.101 -1.293  1.00 28.88 ? 244  GLY B N     1 
ATOM   7525  C  CA    . GLY B 1 224 ? -24.492 -25.279 -2.109  1.00 28.96 ? 244  GLY B CA    1 
ATOM   7526  C  C     . GLY B 1 224 ? -23.944 -24.020 -2.765  1.00 28.81 ? 244  GLY B C     1 
ATOM   7527  O  O     . GLY B 1 224 ? -22.752 -23.754 -2.673  1.00 28.90 ? 244  GLY B O     1 
ATOM   7528  N  N     . SER B 1 225 ? -24.795 -23.251 -3.443  1.00 28.23 ? 245  SER B N     1 
ATOM   7529  C  CA    . SER B 1 225 ? -24.373 -21.955 -3.981  1.00 27.97 ? 245  SER B CA    1 
ATOM   7530  C  C     . SER B 1 225 ? -25.538 -20.972 -4.073  1.00 27.71 ? 245  SER B C     1 
ATOM   7531  O  O     . SER B 1 225 ? -26.700 -21.383 -4.095  1.00 27.91 ? 245  SER B O     1 
ATOM   7532  C  CB    . SER B 1 225 ? -23.752 -22.136 -5.365  1.00 27.91 ? 245  SER B CB    1 
ATOM   7533  O  OG    . SER B 1 225 ? -24.740 -22.504 -6.313  1.00 27.79 ? 245  SER B OG    1 
ATOM   7534  N  N     . PRO B 1 226 ? -25.227 -19.667 -4.129  1.00 27.42 ? 246  PRO B N     1 
ATOM   7535  C  CA    . PRO B 1 226 ? -26.238 -18.642 -4.358  1.00 27.16 ? 246  PRO B CA    1 
ATOM   7536  C  C     . PRO B 1 226 ? -27.030 -18.862 -5.646  1.00 27.02 ? 246  PRO B C     1 
ATOM   7537  O  O     . PRO B 1 226 ? -28.242 -18.632 -5.668  1.00 26.87 ? 246  PRO B O     1 
ATOM   7538  C  CB    . PRO B 1 226 ? -25.415 -17.355 -4.443  1.00 27.18 ? 246  PRO B CB    1 
ATOM   7539  C  CG    . PRO B 1 226 ? -24.187 -17.644 -3.646  1.00 27.48 ? 246  PRO B CG    1 
ATOM   7540  C  CD    . PRO B 1 226 ? -23.900 -19.082 -3.855  1.00 27.38 ? 246  PRO B CD    1 
ATOM   7541  N  N     . GLU B 1 227 ? -26.335 -19.292 -6.702  1.00 26.77 ? 247  GLU B N     1 
ATOM   7542  C  CA    . GLU B 1 227 ? -26.966 -19.661 -7.968  1.00 26.41 ? 247  GLU B CA    1 
ATOM   7543  C  C     . GLU B 1 227 ? -27.996 -20.769 -7.765  1.00 26.34 ? 247  GLU B C     1 
ATOM   7544  O  O     . GLU B 1 227 ? -29.118 -20.666 -8.263  1.00 26.06 ? 247  GLU B O     1 
ATOM   7545  C  CB    . GLU B 1 227 ? -25.909 -20.086 -9.004  1.00 26.34 ? 247  GLU B CB    1 
ATOM   7546  N  N     . GLU B 1 228 ? -27.637 -21.813 -7.016  1.00 26.49 ? 248  GLU B N     1 
ATOM   7547  C  CA    . GLU B 1 228 ? -28.570 -22.924 -6.791  1.00 26.91 ? 248  GLU B CA    1 
ATOM   7548  C  C     . GLU B 1 228 ? -29.816 -22.473 -6.027  1.00 26.27 ? 248  GLU B C     1 
ATOM   7549  O  O     . GLU B 1 228 ? -30.937 -22.815 -6.414  1.00 25.82 ? 248  GLU B O     1 
ATOM   7550  C  CB    . GLU B 1 228 ? -27.916 -24.097 -6.060  1.00 27.30 ? 248  GLU B CB    1 
ATOM   7551  C  CG    . GLU B 1 228 ? -28.839 -25.323 -5.962  1.00 29.82 ? 248  GLU B CG    1 
ATOM   7552  C  CD    . GLU B 1 228 ? -28.295 -26.437 -5.067  1.00 33.59 ? 248  GLU B CD    1 
ATOM   7553  O  OE1   . GLU B 1 228 ? -27.089 -26.759 -5.176  1.00 36.70 ? 248  GLU B OE1   1 
ATOM   7554  O  OE2   . GLU B 1 228 ? -29.079 -26.994 -4.258  1.00 35.76 ? 248  GLU B OE2   1 
ATOM   7555  N  N     . LEU B 1 229 ? -29.622 -21.718 -4.945  1.00 25.62 ? 249  LEU B N     1 
ATOM   7556  C  CA    . LEU B 1 229 ? -30.763 -21.184 -4.193  1.00 25.39 ? 249  LEU B CA    1 
ATOM   7557  C  C     . LEU B 1 229 ? -31.645 -20.302 -5.084  1.00 25.26 ? 249  LEU B C     1 
ATOM   7558  O  O     . LEU B 1 229 ? -32.871 -20.374 -5.015  1.00 25.01 ? 249  LEU B O     1 
ATOM   7559  C  CB    . LEU B 1 229 ? -30.304 -20.420 -2.941  1.00 24.92 ? 249  LEU B CB    1 
ATOM   7560  C  CG    . LEU B 1 229 ? -31.402 -19.735 -2.107  1.00 24.65 ? 249  LEU B CG    1 
ATOM   7561  C  CD1   . LEU B 1 229 ? -32.529 -20.706 -1.752  1.00 23.77 ? 249  LEU B CD1   1 
ATOM   7562  C  CD2   . LEU B 1 229 ? -30.812 -19.089 -0.846  1.00 23.46 ? 249  LEU B CD2   1 
ATOM   7563  N  N     . ALA B 1 230 ? -31.012 -19.489 -5.925  1.00 25.51 ? 250  ALA B N     1 
ATOM   7564  C  CA    . ALA B 1 230 ? -31.726 -18.621 -6.867  1.00 25.70 ? 250  ALA B CA    1 
ATOM   7565  C  C     . ALA B 1 230 ? -32.610 -19.421 -7.836  1.00 25.98 ? 250  ALA B C     1 
ATOM   7566  O  O     . ALA B 1 230 ? -33.793 -19.105 -8.020  1.00 25.67 ? 250  ALA B O     1 
ATOM   7567  C  CB    . ALA B 1 230 ? -30.730 -17.748 -7.639  1.00 25.50 ? 250  ALA B CB    1 
ATOM   7568  N  N     . ARG B 1 231 ? -32.042 -20.468 -8.433  1.00 26.24 ? 251  ARG B N     1 
ATOM   7569  C  CA    . ARG B 1 231 ? -32.769 -21.306 -9.387  1.00 26.32 ? 251  ARG B CA    1 
ATOM   7570  C  C     . ARG B 1 231 ? -33.934 -22.044 -8.714  1.00 26.93 ? 251  ARG B C     1 
ATOM   7571  O  O     . ARG B 1 231 ? -35.058 -22.065 -9.231  1.00 26.82 ? 251  ARG B O     1 
ATOM   7572  C  CB    . ARG B 1 231 ? -31.821 -22.308 -10.054 1.00 26.41 ? 251  ARG B CB    1 
ATOM   7573  N  N     . LYS B 1 232 ? -33.673 -22.628 -7.550  1.00 27.35 ? 252  LYS B N     1 
ATOM   7574  C  CA    . LYS B 1 232 ? -34.721 -23.333 -6.821  1.00 27.86 ? 252  LYS B CA    1 
ATOM   7575  C  C     . LYS B 1 232 ? -35.835 -22.400 -6.363  1.00 27.76 ? 252  LYS B C     1 
ATOM   7576  O  O     . LYS B 1 232 ? -37.005 -22.782 -6.397  1.00 27.73 ? 252  LYS B O     1 
ATOM   7577  C  CB    . LYS B 1 232 ? -34.145 -24.138 -5.662  1.00 27.99 ? 252  LYS B CB    1 
ATOM   7578  C  CG    . LYS B 1 232 ? -33.496 -25.437 -6.139  1.00 29.84 ? 252  LYS B CG    1 
ATOM   7579  C  CD    . LYS B 1 232 ? -33.166 -26.357 -4.993  1.00 32.16 ? 252  LYS B CD    1 
ATOM   7580  C  CE    . LYS B 1 232 ? -32.380 -27.566 -5.456  1.00 34.17 ? 252  LYS B CE    1 
ATOM   7581  N  NZ    . LYS B 1 232 ? -31.461 -28.040 -4.357  1.00 37.56 ? 252  LYS B NZ    1 
ATOM   7582  N  N     . TYR B 1 233 ? -35.470 -21.181 -5.959  1.00 27.57 ? 253  TYR B N     1 
ATOM   7583  C  CA    . TYR B 1 233 ? -36.458 -20.151 -5.658  1.00 27.45 ? 253  TYR B CA    1 
ATOM   7584  C  C     . TYR B 1 233 ? -37.341 -19.876 -6.883  1.00 27.54 ? 253  TYR B C     1 
ATOM   7585  O  O     . TYR B 1 233 ? -38.568 -19.965 -6.810  1.00 26.99 ? 253  TYR B O     1 
ATOM   7586  C  CB    . TYR B 1 233 ? -35.776 -18.858 -5.200  1.00 27.37 ? 253  TYR B CB    1 
ATOM   7587  C  CG    . TYR B 1 233 ? -36.746 -17.723 -5.002  1.00 27.62 ? 253  TYR B CG    1 
ATOM   7588  C  CD1   . TYR B 1 233 ? -37.749 -17.813 -4.043  1.00 27.55 ? 253  TYR B CD1   1 
ATOM   7589  C  CD2   . TYR B 1 233 ? -36.684 -16.574 -5.784  1.00 27.50 ? 253  TYR B CD2   1 
ATOM   7590  C  CE1   . TYR B 1 233 ? -38.652 -16.789 -3.853  1.00 28.14 ? 253  TYR B CE1   1 
ATOM   7591  C  CE2   . TYR B 1 233 ? -37.595 -15.535 -5.601  1.00 27.93 ? 253  TYR B CE2   1 
ATOM   7592  C  CZ    . TYR B 1 233 ? -38.580 -15.660 -4.632  1.00 28.20 ? 253  TYR B CZ    1 
ATOM   7593  O  OH    . TYR B 1 233 ? -39.488 -14.655 -4.416  1.00 28.58 ? 253  TYR B OH    1 
ATOM   7594  N  N     . ALA B 1 234 ? -36.704 -19.553 -8.006  1.00 27.74 ? 254  ALA B N     1 
ATOM   7595  C  CA    . ALA B 1 234 ? -37.419 -19.332 -9.271  1.00 28.09 ? 254  ALA B CA    1 
ATOM   7596  C  C     . ALA B 1 234 ? -38.326 -20.510 -9.642  1.00 28.27 ? 254  ALA B C     1 
ATOM   7597  O  O     . ALA B 1 234 ? -39.435 -20.317 -10.137 1.00 28.95 ? 254  ALA B O     1 
ATOM   7598  C  CB    . ALA B 1 234 ? -36.433 -19.063 -10.398 1.00 27.56 ? 254  ALA B CB    1 
ATOM   7599  N  N     . ASP B 1 235 ? -37.856 -21.728 -9.392  1.00 28.58 ? 255  ASP B N     1 
ATOM   7600  C  CA    . ASP B 1 235 ? -38.600 -22.926 -9.767  1.00 28.63 ? 255  ASP B CA    1 
ATOM   7601  C  C     . ASP B 1 235 ? -39.640 -23.353 -8.748  1.00 29.02 ? 255  ASP B C     1 
ATOM   7602  O  O     . ASP B 1 235 ? -40.262 -24.397 -8.916  1.00 29.54 ? 255  ASP B O     1 
ATOM   7603  C  CB    . ASP B 1 235 ? -37.635 -24.069 -10.064 1.00 28.30 ? 255  ASP B CB    1 
ATOM   7604  C  CG    . ASP B 1 235 ? -36.791 -23.798 -11.289 1.00 27.77 ? 255  ASP B CG    1 
ATOM   7605  O  OD1   . ASP B 1 235 ? -37.124 -22.875 -12.061 1.00 26.59 ? 255  ASP B OD1   1 
ATOM   7606  O  OD2   . ASP B 1 235 ? -35.792 -24.508 -11.484 1.00 28.16 ? 255  ASP B OD2   1 
ATOM   7607  N  N     . GLY B 1 236 ? -39.854 -22.545 -7.714  1.00 29.10 ? 256  GLY B N     1 
ATOM   7608  C  CA    . GLY B 1 236 ? -40.885 -22.829 -6.724  1.00 29.29 ? 256  GLY B CA    1 
ATOM   7609  C  C     . GLY B 1 236 ? -40.498 -23.947 -5.787  1.00 29.57 ? 256  GLY B C     1 
ATOM   7610  O  O     . GLY B 1 236 ? -41.364 -24.628 -5.246  1.00 29.54 ? 256  GLY B O     1 
ATOM   7611  N  N     . GLU B 1 237 ? -39.196 -24.136 -5.580  1.00 30.18 ? 257  GLU B N     1 
ATOM   7612  C  CA    . GLU B 1 237 ? -38.701 -25.231 -4.747  1.00 30.71 ? 257  GLU B CA    1 
ATOM   7613  C  C     . GLU B 1 237 ? -38.010 -24.751 -3.465  1.00 30.78 ? 257  GLU B C     1 
ATOM   7614  O  O     . GLU B 1 237 ? -37.110 -25.420 -2.963  1.00 31.09 ? 257  GLU B O     1 
ATOM   7615  C  CB    . GLU B 1 237 ? -37.723 -26.091 -5.548  1.00 30.88 ? 257  GLU B CB    1 
ATOM   7616  C  CG    . GLU B 1 237 ? -38.338 -26.773 -6.738  1.00 32.78 ? 257  GLU B CG    1 
ATOM   7617  C  CD    . GLU B 1 237 ? -37.396 -27.772 -7.368  1.00 33.88 ? 257  GLU B CD    1 
ATOM   7618  O  OE1   . GLU B 1 237 ? -36.373 -27.359 -7.946  1.00 36.52 ? 257  GLU B OE1   1 
ATOM   7619  O  OE2   . GLU B 1 237 ? -37.682 -28.978 -7.289  1.00 36.15 ? 257  GLU B OE2   1 
ATOM   7620  N  N     . VAL B 1 238 ? -38.411 -23.596 -2.944  1.00 30.95 ? 258  VAL B N     1 
ATOM   7621  C  CA    . VAL B 1 238 ? -37.864 -23.104 -1.683  1.00 30.77 ? 258  VAL B CA    1 
ATOM   7622  C  C     . VAL B 1 238 ? -38.988 -22.689 -0.753  1.00 31.25 ? 258  VAL B C     1 
ATOM   7623  O  O     . VAL B 1 238 ? -39.930 -22.021 -1.150  1.00 31.00 ? 258  VAL B O     1 
ATOM   7624  C  CB    . VAL B 1 238 ? -36.899 -21.911 -1.885  1.00 30.96 ? 258  VAL B CB    1 
ATOM   7625  C  CG1   . VAL B 1 238 ? -36.411 -21.384 -0.533  1.00 29.39 ? 258  VAL B CG1   1 
ATOM   7626  C  CG2   . VAL B 1 238 ? -35.713 -22.316 -2.771  1.00 29.91 ? 258  VAL B CG2   1 
ATOM   7627  N  N     . ASP B 1 239 ? -38.882 -23.115 0.494   1.00 32.23 ? 259  ASP B N     1 
ATOM   7628  C  CA    . ASP B 1 239 ? -39.833 -22.743 1.518   1.00 32.97 ? 259  ASP B CA    1 
ATOM   7629  C  C     . ASP B 1 239 ? -39.374 -21.401 2.068   1.00 32.76 ? 259  ASP B C     1 
ATOM   7630  O  O     . ASP B 1 239 ? -38.454 -21.347 2.885   1.00 33.06 ? 259  ASP B O     1 
ATOM   7631  C  CB    . ASP B 1 239 ? -39.837 -23.810 2.610   1.00 33.63 ? 259  ASP B CB    1 
ATOM   7632  C  CG    . ASP B 1 239 ? -40.879 -23.557 3.666   1.00 35.32 ? 259  ASP B CG    1 
ATOM   7633  O  OD1   . ASP B 1 239 ? -41.884 -22.867 3.377   1.00 38.05 ? 259  ASP B OD1   1 
ATOM   7634  O  OD2   . ASP B 1 239 ? -40.690 -24.066 4.788   1.00 38.87 ? 259  ASP B OD2   1 
ATOM   7635  N  N     . VAL B 1 240 ? -39.976 -20.320 1.579   1.00 32.34 ? 260  VAL B N     1 
ATOM   7636  C  CA    . VAL B 1 240 ? -39.537 -18.988 1.945   1.00 32.10 ? 260  VAL B CA    1 
ATOM   7637  C  C     . VAL B 1 240 ? -40.367 -18.422 3.088   1.00 31.60 ? 260  VAL B C     1 
ATOM   7638  O  O     . VAL B 1 240 ? -41.559 -18.716 3.223   1.00 31.34 ? 260  VAL B O     1 
ATOM   7639  C  CB    . VAL B 1 240 ? -39.582 -17.995 0.749   1.00 32.46 ? 260  VAL B CB    1 
ATOM   7640  C  CG1   . VAL B 1 240 ? -38.744 -18.519 -0.429  1.00 32.51 ? 260  VAL B CG1   1 
ATOM   7641  C  CG2   . VAL B 1 240 ? -41.012 -17.706 0.332   1.00 31.89 ? 260  VAL B CG2   1 
ATOM   7642  N  N     . VAL B 1 241 ? -39.706 -17.626 3.922   1.00 30.89 ? 261  VAL B N     1 
ATOM   7643  C  CA    . VAL B 1 241 ? -40.378 -16.813 4.903   1.00 30.24 ? 261  VAL B CA    1 
ATOM   7644  C  C     . VAL B 1 241 ? -40.213 -15.379 4.425   1.00 29.95 ? 261  VAL B C     1 
ATOM   7645  O  O     . VAL B 1 241 ? -39.094 -14.877 4.334   1.00 29.85 ? 261  VAL B O     1 
ATOM   7646  C  CB    . VAL B 1 241 ? -39.775 -16.983 6.312   1.00 30.38 ? 261  VAL B CB    1 
ATOM   7647  C  CG1   . VAL B 1 241 ? -40.477 -16.050 7.308   1.00 29.70 ? 261  VAL B CG1   1 
ATOM   7648  C  CG2   . VAL B 1 241 ? -39.881 -18.431 6.767   1.00 29.88 ? 261  VAL B CG2   1 
ATOM   7649  N  N     . VAL B 1 242 ? -41.330 -14.750 4.073   1.00 29.31 ? 262  VAL B N     1 
ATOM   7650  C  CA    . VAL B 1 242 ? -41.354 -13.345 3.714   1.00 28.90 ? 262  VAL B CA    1 
ATOM   7651  C  C     . VAL B 1 242 ? -41.406 -12.577 5.026   1.00 29.14 ? 262  VAL B C     1 
ATOM   7652  O  O     . VAL B 1 242 ? -42.366 -12.712 5.776   1.00 28.96 ? 262  VAL B O     1 
ATOM   7653  C  CB    . VAL B 1 242 ? -42.585 -13.021 2.834   1.00 28.91 ? 262  VAL B CB    1 
ATOM   7654  C  CG1   . VAL B 1 242 ? -42.664 -11.539 2.532   1.00 28.23 ? 262  VAL B CG1   1 
ATOM   7655  C  CG2   . VAL B 1 242 ? -42.543 -13.847 1.535   1.00 27.76 ? 262  VAL B CG2   1 
ATOM   7656  N  N     . LEU B 1 243 ? -40.369 -11.790 5.307   1.00 29.36 ? 263  LEU B N     1 
ATOM   7657  C  CA    . LEU B 1 243 ? -40.219 -11.119 6.604   1.00 29.56 ? 263  LEU B CA    1 
ATOM   7658  C  C     . LEU B 1 243 ? -41.256 -10.016 6.806   1.00 29.71 ? 263  LEU B C     1 
ATOM   7659  O  O     . LEU B 1 243 ? -41.570 -9.288  5.867   1.00 30.07 ? 263  LEU B O     1 
ATOM   7660  C  CB    . LEU B 1 243 ? -38.814 -10.521 6.747   1.00 29.37 ? 263  LEU B CB    1 
ATOM   7661  C  CG    . LEU B 1 243 ? -37.616 -11.471 6.670   1.00 29.14 ? 263  LEU B CG    1 
ATOM   7662  C  CD1   . LEU B 1 243 ? -36.333 -10.729 6.965   1.00 28.79 ? 263  LEU B CD1   1 
ATOM   7663  C  CD2   . LEU B 1 243 ? -37.769 -12.627 7.617   1.00 28.82 ? 263  LEU B CD2   1 
ATOM   7664  N  N     . GLU B 1 258 ? -45.940 5.940   14.597  1.00 39.43 ? 278  GLU B N     1 
ATOM   7665  C  CA    . GLU B 1 258 ? -45.125 4.746   14.366  1.00 38.96 ? 278  GLU B CA    1 
ATOM   7666  C  C     . GLU B 1 258 ? -44.534 4.249   15.681  1.00 38.27 ? 278  GLU B C     1 
ATOM   7667  O  O     . GLU B 1 258 ? -43.711 4.943   16.280  1.00 38.97 ? 278  GLU B O     1 
ATOM   7668  C  CB    . GLU B 1 258 ? -43.994 5.055   13.381  1.00 39.11 ? 278  GLU B CB    1 
ATOM   7669  N  N     . PRO B 1 259 ? -44.948 3.057   16.147  1.00 37.07 ? 279  PRO B N     1 
ATOM   7670  C  CA    . PRO B 1 259 ? -44.326 2.498   17.349  1.00 36.07 ? 279  PRO B CA    1 
ATOM   7671  C  C     . PRO B 1 259 ? -42.847 2.175   17.115  1.00 34.66 ? 279  PRO B C     1 
ATOM   7672  O  O     . PRO B 1 259 ? -42.444 1.979   15.974  1.00 34.71 ? 279  PRO B O     1 
ATOM   7673  C  CB    . PRO B 1 259 ? -45.109 1.209   17.579  1.00 36.32 ? 279  PRO B CB    1 
ATOM   7674  C  CG    . PRO B 1 259 ? -45.588 0.833   16.238  1.00 37.04 ? 279  PRO B CG    1 
ATOM   7675  C  CD    . PRO B 1 259 ? -45.915 2.119   15.557  1.00 37.40 ? 279  PRO B CD    1 
ATOM   7676  N  N     . PRO B 1 260 ? -42.035 2.128   18.182  1.00 32.86 ? 280  PRO B N     1 
ATOM   7677  C  CA    . PRO B 1 260 ? -40.623 1.832   17.911  1.00 31.61 ? 280  PRO B CA    1 
ATOM   7678  C  C     . PRO B 1 260 ? -40.412 0.412   17.398  1.00 29.95 ? 280  PRO B C     1 
ATOM   7679  O  O     . PRO B 1 260 ? -41.240 -0.460  17.616  1.00 29.79 ? 280  PRO B O     1 
ATOM   7680  C  CB    . PRO B 1 260 ? -39.947 2.005   19.277  1.00 31.51 ? 280  PRO B CB    1 
ATOM   7681  C  CG    . PRO B 1 260 ? -40.907 2.825   20.092  1.00 32.36 ? 280  PRO B CG    1 
ATOM   7682  C  CD    . PRO B 1 260 ? -42.276 2.452   19.598  1.00 32.87 ? 280  PRO B CD    1 
ATOM   7683  N  N     . LEU B 1 261 ? -39.297 0.200   16.717  1.00 28.25 ? 281  LEU B N     1 
ATOM   7684  C  CA    . LEU B 1 261 ? -38.856 -1.136  16.365  1.00 26.86 ? 281  LEU B CA    1 
ATOM   7685  C  C     . LEU B 1 261 ? -38.598 -1.914  17.662  1.00 24.90 ? 281  LEU B C     1 
ATOM   7686  O  O     . LEU B 1 261 ? -38.123 -1.341  18.647  1.00 23.82 ? 281  LEU B O     1 
ATOM   7687  C  CB    . LEU B 1 261 ? -37.567 -1.031  15.541  1.00 27.20 ? 281  LEU B CB    1 
ATOM   7688  C  CG    . LEU B 1 261 ? -37.317 -2.014  14.413  1.00 28.22 ? 281  LEU B CG    1 
ATOM   7689  C  CD1   . LEU B 1 261 ? -38.533 -2.109  13.512  1.00 28.67 ? 281  LEU B CD1   1 
ATOM   7690  C  CD2   . LEU B 1 261 ? -36.082 -1.537  13.639  1.00 28.57 ? 281  LEU B CD2   1 
ATOM   7691  N  N     . PHE B 1 262 ? -38.895 -3.209  17.668  1.00 23.03 ? 282  PHE B N     1 
ATOM   7692  C  CA    . PHE B 1 262 ? -38.642 -4.034  18.859  1.00 22.04 ? 282  PHE B CA    1 
ATOM   7693  C  C     . PHE B 1 262 ? -37.168 -4.031  19.275  1.00 21.26 ? 282  PHE B C     1 
ATOM   7694  O  O     . PHE B 1 262 ? -36.870 -4.237  20.443  1.00 20.86 ? 282  PHE B O     1 
ATOM   7695  C  CB    . PHE B 1 262 ? -39.149 -5.482  18.682  1.00 21.60 ? 282  PHE B CB    1 
ATOM   7696  C  CG    . PHE B 1 262 ? -38.299 -6.335  17.767  1.00 21.22 ? 282  PHE B CG    1 
ATOM   7697  C  CD1   . PHE B 1 262 ? -37.179 -7.003  18.253  1.00 20.65 ? 282  PHE B CD1   1 
ATOM   7698  C  CD2   . PHE B 1 262 ? -38.637 -6.493  16.430  1.00 20.51 ? 282  PHE B CD2   1 
ATOM   7699  C  CE1   . PHE B 1 262 ? -36.402 -7.795  17.416  1.00 21.17 ? 282  PHE B CE1   1 
ATOM   7700  C  CE2   . PHE B 1 262 ? -37.864 -7.280  15.584  1.00 20.16 ? 282  PHE B CE2   1 
ATOM   7701  C  CZ    . PHE B 1 262 ? -36.748 -7.928  16.075  1.00 21.15 ? 282  PHE B CZ    1 
ATOM   7702  N  N     . SER B 1 263 ? -36.264 -3.783  18.322  1.00 20.90 ? 283  SER B N     1 
ATOM   7703  C  CA    . SER B 1 263 ? -34.808 -3.779  18.577  1.00 20.82 ? 283  SER B CA    1 
ATOM   7704  C  C     . SER B 1 263 ? -34.285 -2.423  19.068  1.00 21.00 ? 283  SER B C     1 
ATOM   7705  O  O     . SER B 1 263 ? -33.074 -2.250  19.302  1.00 20.50 ? 283  SER B O     1 
ATOM   7706  C  CB    . SER B 1 263 ? -34.063 -4.178  17.305  1.00 21.06 ? 283  SER B CB    1 
ATOM   7707  O  OG    . SER B 1 263 ? -34.458 -3.375  16.202  1.00 20.19 ? 283  SER B OG    1 
ATOM   7708  N  N     . SER B 1 264 ? -35.203 -1.467  19.200  1.00 21.03 ? 284  SER B N     1 
ATOM   7709  C  CA    . SER B 1 264 ? -34.890 -0.128  19.667  1.00 21.30 ? 284  SER B CA    1 
ATOM   7710  C  C     . SER B 1 264 ? -35.050 -0.015  21.172  1.00 21.57 ? 284  SER B C     1 
ATOM   7711  O  O     . SER B 1 264 ? -35.894 -0.690  21.765  1.00 21.11 ? 284  SER B O     1 
ATOM   7712  C  CB    . SER B 1 264 ? -35.818 0.891   19.002  1.00 21.36 ? 284  SER B CB    1 
ATOM   7713  O  OG    . SER B 1 264 ? -35.524 2.192   19.482  1.00 22.39 ? 284  SER B OG    1 
ATOM   7714  N  N     . HIS B 1 265 ? -34.258 0.876   21.767  1.00 22.27 ? 285  HIS B N     1 
ATOM   7715  C  CA    . HIS B 1 265 ? -34.359 1.238   23.183  1.00 22.72 ? 285  HIS B CA    1 
ATOM   7716  C  C     . HIS B 1 265 ? -35.478 2.254   23.483  1.00 23.43 ? 285  HIS B C     1 
ATOM   7717  O  O     . HIS B 1 265 ? -35.788 2.525   24.652  1.00 22.96 ? 285  HIS B O     1 
ATOM   7718  C  CB    . HIS B 1 265 ? -33.035 1.843   23.661  1.00 22.87 ? 285  HIS B CB    1 
ATOM   7719  C  CG    . HIS B 1 265 ? -31.976 0.834   23.962  1.00 23.80 ? 285  HIS B CG    1 
ATOM   7720  N  ND1   . HIS B 1 265 ? -31.311 0.136   22.976  1.00 25.08 ? 285  HIS B ND1   1 
ATOM   7721  C  CD2   . HIS B 1 265 ? -31.429 0.438   25.135  1.00 24.75 ? 285  HIS B CD2   1 
ATOM   7722  C  CE1   . HIS B 1 265 ? -30.407 -0.651  23.530  1.00 24.38 ? 285  HIS B CE1   1 
ATOM   7723  N  NE2   . HIS B 1 265 ? -30.462 -0.494  24.839  1.00 24.43 ? 285  HIS B NE2   1 
ATOM   7724  N  N     . LYS B 1 266 ? -36.072 2.830   22.441  1.00 24.10 ? 286  LYS B N     1 
ATOM   7725  C  CA    . LYS B 1 266 ? -37.085 3.873   22.635  1.00 24.67 ? 286  LYS B CA    1 
ATOM   7726  C  C     . LYS B 1 266 ? -38.256 3.396   23.513  1.00 24.19 ? 286  LYS B C     1 
ATOM   7727  O  O     . LYS B 1 266 ? -38.722 2.275   23.371  1.00 23.73 ? 286  LYS B O     1 
ATOM   7728  C  CB    . LYS B 1 266 ? -37.602 4.372   21.291  1.00 25.14 ? 286  LYS B CB    1 
ATOM   7729  C  CG    . LYS B 1 266 ? -36.588 5.185   20.507  1.00 26.94 ? 286  LYS B CG    1 
ATOM   7730  C  CD    . LYS B 1 266 ? -37.139 5.502   19.123  1.00 30.20 ? 286  LYS B CD    1 
ATOM   7731  C  CE    . LYS B 1 266 ? -36.153 6.297   18.276  1.00 31.55 ? 286  LYS B CE    1 
ATOM   7732  N  NZ    . LYS B 1 266 ? -36.741 6.597   16.935  1.00 32.70 ? 286  LYS B NZ    1 
ATOM   7733  N  N     . PRO B 1 267 ? -38.706 4.240   24.454  1.00 24.28 ? 287  PRO B N     1 
ATOM   7734  C  CA    . PRO B 1 267 ? -39.778 3.818   25.347  1.00 24.26 ? 287  PRO B CA    1 
ATOM   7735  C  C     . PRO B 1 267 ? -41.095 3.480   24.652  1.00 24.19 ? 287  PRO B C     1 
ATOM   7736  O  O     . PRO B 1 267 ? -41.481 4.130   23.684  1.00 23.88 ? 287  PRO B O     1 
ATOM   7737  C  CB    . PRO B 1 267 ? -39.967 5.028   26.272  1.00 24.54 ? 287  PRO B CB    1 
ATOM   7738  C  CG    . PRO B 1 267 ? -38.673 5.716   26.263  1.00 24.66 ? 287  PRO B CG    1 
ATOM   7739  C  CD    . PRO B 1 267 ? -38.091 5.502   24.899  1.00 24.27 ? 287  PRO B CD    1 
ATOM   7740  N  N     . ARG B 1 268 ? -41.744 2.426   25.133  1.00 24.39 ? 288  ARG B N     1 
ATOM   7741  C  CA    . ARG B 1 268 ? -43.139 2.142   24.801  1.00 24.57 ? 288  ARG B CA    1 
ATOM   7742  C  C     . ARG B 1 268 ? -43.767 1.389   25.957  1.00 24.84 ? 288  ARG B C     1 
ATOM   7743  O  O     . ARG B 1 268 ? -43.064 0.905   26.854  1.00 24.34 ? 288  ARG B O     1 
ATOM   7744  C  CB    . ARG B 1 268 ? -43.289 1.347   23.494  1.00 24.63 ? 288  ARG B CB    1 
ATOM   7745  C  CG    . ARG B 1 268 ? -42.624 -0.043  23.458  1.00 24.81 ? 288  ARG B CG    1 
ATOM   7746  C  CD    . ARG B 1 268 ? -41.186 0.041   23.017  1.00 23.10 ? 288  ARG B CD    1 
ATOM   7747  N  NE    . ARG B 1 268 ? -40.576 -1.265  22.731  1.00 23.53 ? 288  ARG B NE    1 
ATOM   7748  C  CZ    . ARG B 1 268 ? -39.309 -1.413  22.326  1.00 22.90 ? 288  ARG B CZ    1 
ATOM   7749  N  NH1   . ARG B 1 268 ? -38.537 -0.354  22.139  1.00 21.93 ? 288  ARG B NH1   1 
ATOM   7750  N  NH2   . ARG B 1 268 ? -38.811 -2.615  22.091  1.00 23.66 ? 288  ARG B NH2   1 
ATOM   7751  N  N     . GLY B 1 269 ? -45.090 1.288   25.925  1.00 25.28 ? 289  GLY B N     1 
ATOM   7752  C  CA    . GLY B 1 269 ? -45.837 0.692   27.023  1.00 25.86 ? 289  GLY B CA    1 
ATOM   7753  C  C     . GLY B 1 269 ? -46.006 1.712   28.136  1.00 26.46 ? 289  GLY B C     1 
ATOM   7754  O  O     . GLY B 1 269 ? -45.465 2.814   28.073  1.00 26.72 ? 289  GLY B O     1 
ATOM   7755  N  N     . ASP B 1 270 ? -46.780 1.350   29.147  1.00 27.10 ? 290  ASP B N     1 
ATOM   7756  C  CA    . ASP B 1 270 ? -47.070 2.249   30.267  1.00 27.48 ? 290  ASP B CA    1 
ATOM   7757  C  C     . ASP B 1 270 ? -46.996 1.456   31.549  1.00 27.07 ? 290  ASP B C     1 
ATOM   7758  O  O     . ASP B 1 270 ? -47.589 0.381   31.653  1.00 27.07 ? 290  ASP B O     1 
ATOM   7759  C  CB    . ASP B 1 270 ? -48.482 2.829   30.137  1.00 27.97 ? 290  ASP B CB    1 
ATOM   7760  C  CG    . ASP B 1 270 ? -48.662 3.643   28.871  1.00 29.81 ? 290  ASP B CG    1 
ATOM   7761  O  OD1   . ASP B 1 270 ? -47.949 4.657   28.706  1.00 31.20 ? 290  ASP B OD1   1 
ATOM   7762  O  OD2   . ASP B 1 270 ? -49.515 3.262   28.043  1.00 33.33 ? 290  ASP B OD2   1 
ATOM   7763  N  N     . PHE B 1 271 ? -46.269 1.977   32.526  1.00 26.79 ? 291  PHE B N     1 
ATOM   7764  C  CA    . PHE B 1 271 ? -46.341 1.429   33.865  1.00 26.44 ? 291  PHE B CA    1 
ATOM   7765  C  C     . PHE B 1 271 ? -47.736 1.721   34.438  1.00 26.67 ? 291  PHE B C     1 
ATOM   7766  O  O     . PHE B 1 271 ? -48.391 2.685   34.032  1.00 26.78 ? 291  PHE B O     1 
ATOM   7767  C  CB    . PHE B 1 271 ? -45.280 2.053   34.759  1.00 26.24 ? 291  PHE B CB    1 
ATOM   7768  C  CG    . PHE B 1 271 ? -43.874 1.610   34.454  1.00 25.61 ? 291  PHE B CG    1 
ATOM   7769  C  CD1   . PHE B 1 271 ? -43.581 0.279   34.182  1.00 24.84 ? 291  PHE B CD1   1 
ATOM   7770  C  CD2   . PHE B 1 271 ? -42.826 2.528   34.491  1.00 24.62 ? 291  PHE B CD2   1 
ATOM   7771  C  CE1   . PHE B 1 271 ? -42.274 -0.124  33.922  1.00 25.02 ? 291  PHE B CE1   1 
ATOM   7772  C  CE2   . PHE B 1 271 ? -41.516 2.125   34.240  1.00 24.47 ? 291  PHE B CE2   1 
ATOM   7773  C  CZ    . PHE B 1 271 ? -41.242 0.798   33.954  1.00 24.42 ? 291  PHE B CZ    1 
ATOM   7774  N  N     . PRO B 1 272 ? -48.208 0.882   35.364  1.00 26.84 ? 292  PRO B N     1 
ATOM   7775  C  CA    . PRO B 1 272 ? -49.452 1.204   36.053  1.00 27.01 ? 292  PRO B CA    1 
ATOM   7776  C  C     . PRO B 1 272 ? -49.354 2.498   36.862  1.00 27.02 ? 292  PRO B C     1 
ATOM   7777  O  O     . PRO B 1 272 ? -50.343 3.198   36.992  1.00 26.29 ? 292  PRO B O     1 
ATOM   7778  C  CB    . PRO B 1 272 ? -49.668 0.003   36.981  1.00 27.00 ? 292  PRO B CB    1 
ATOM   7779  C  CG    . PRO B 1 272 ? -48.895 -1.090  36.388  1.00 26.85 ? 292  PRO B CG    1 
ATOM   7780  C  CD    . PRO B 1 272 ? -47.727 -0.470  35.700  1.00 27.14 ? 292  PRO B CD    1 
ATOM   7781  N  N     . SER B 1 273 ? -48.173 2.786   37.405  1.00 27.43 ? 293  SER B N     1 
ATOM   7782  C  CA    . SER B 1 273 ? -47.898 4.052   38.084  1.00 27.95 ? 293  SER B CA    1 
ATOM   7783  C  C     . SER B 1 273 ? -46.761 4.759   37.346  1.00 28.45 ? 293  SER B C     1 
ATOM   7784  O  O     . SER B 1 273 ? -45.594 4.643   37.739  1.00 28.49 ? 293  SER B O     1 
ATOM   7785  C  CB    . SER B 1 273 ? -47.493 3.813   39.540  1.00 27.94 ? 293  SER B CB    1 
ATOM   7786  O  OG    . SER B 1 273 ? -48.401 2.948   40.193  1.00 28.65 ? 293  SER B OG    1 
ATOM   7787  N  N     . PRO B 1 274 ? -47.095 5.498   36.274  1.00 28.89 ? 294  PRO B N     1 
ATOM   7788  C  CA    . PRO B 1 274 ? -46.064 6.171   35.467  1.00 29.23 ? 294  PRO B CA    1 
ATOM   7789  C  C     . PRO B 1 274 ? -45.141 7.086   36.290  1.00 29.69 ? 294  PRO B C     1 
ATOM   7790  O  O     . PRO B 1 274 ? -45.574 7.680   37.285  1.00 29.76 ? 294  PRO B O     1 
ATOM   7791  C  CB    . PRO B 1 274 ? -46.879 6.998   34.466  1.00 29.22 ? 294  PRO B CB    1 
ATOM   7792  C  CG    . PRO B 1 274 ? -48.235 6.398   34.454  1.00 28.79 ? 294  PRO B CG    1 
ATOM   7793  C  CD    . PRO B 1 274 ? -48.457 5.830   35.816  1.00 28.69 ? 294  PRO B CD    1 
ATOM   7794  N  N     . ILE B 1 275 ? -43.879 7.167   35.878  1.00 30.06 ? 295  ILE B N     1 
ATOM   7795  C  CA    . ILE B 1 275 ? -42.890 8.031   36.522  1.00 30.46 ? 295  ILE B CA    1 
ATOM   7796  C  C     . ILE B 1 275 ? -42.477 9.132   35.538  1.00 30.90 ? 295  ILE B C     1 
ATOM   7797  O  O     . ILE B 1 275 ? -42.030 8.853   34.423  1.00 31.00 ? 295  ILE B O     1 
ATOM   7798  C  CB    . ILE B 1 275 ? -41.651 7.229   36.974  1.00 30.41 ? 295  ILE B CB    1 
ATOM   7799  C  CG1   . ILE B 1 275 ? -42.036 6.264   38.114  1.00 30.14 ? 295  ILE B CG1   1 
ATOM   7800  C  CG2   . ILE B 1 275 ? -40.540 8.177   37.416  1.00 29.60 ? 295  ILE B CG2   1 
ATOM   7801  C  CD1   . ILE B 1 275 ? -40.979 5.208   38.427  1.00 27.99 ? 295  ILE B CD1   1 
ATOM   7802  N  N     . HIS B 1 276 ? -42.635 10.383  35.957  1.00 31.35 ? 296  HIS B N     1 
ATOM   7803  C  CA    . HIS B 1 276 ? -42.405 11.518  35.070  1.00 31.68 ? 296  HIS B CA    1 
ATOM   7804  C  C     . HIS B 1 276 ? -41.195 12.363  35.460  1.00 30.67 ? 296  HIS B C     1 
ATOM   7805  O  O     . HIS B 1 276 ? -40.811 13.258  34.713  1.00 31.41 ? 296  HIS B O     1 
ATOM   7806  C  CB    . HIS B 1 276 ? -43.643 12.417  35.048  1.00 32.44 ? 296  HIS B CB    1 
ATOM   7807  C  CG    . HIS B 1 276 ? -44.937 11.680  34.875  1.00 34.72 ? 296  HIS B CG    1 
ATOM   7808  N  ND1   . HIS B 1 276 ? -45.334 11.144  33.668  1.00 38.18 ? 296  HIS B ND1   1 
ATOM   7809  C  CD2   . HIS B 1 276 ? -45.936 11.413  35.751  1.00 36.84 ? 296  HIS B CD2   1 
ATOM   7810  C  CE1   . HIS B 1 276 ? -46.520 10.574  33.808  1.00 38.55 ? 296  HIS B CE1   1 
ATOM   7811  N  NE2   . HIS B 1 276 ? -46.908 10.724  35.064  1.00 37.98 ? 296  HIS B NE2   1 
ATOM   7812  N  N     . VAL B 1 277 ? -40.593 12.102  36.615  1.00 29.39 ? 297  VAL B N     1 
ATOM   7813  C  CA    . VAL B 1 277 ? -39.479 12.926  37.078  1.00 28.11 ? 297  VAL B CA    1 
ATOM   7814  C  C     . VAL B 1 277 ? -38.219 12.101  37.229  1.00 27.44 ? 297  VAL B C     1 
ATOM   7815  O  O     . VAL B 1 277 ? -38.271 10.873  37.269  1.00 27.42 ? 297  VAL B O     1 
ATOM   7816  C  CB    . VAL B 1 277 ? -39.803 13.641  38.408  1.00 27.89 ? 297  VAL B CB    1 
ATOM   7817  C  CG1   . VAL B 1 277 ? -41.116 14.415  38.291  1.00 28.17 ? 297  VAL B CG1   1 
ATOM   7818  C  CG2   . VAL B 1 277 ? -39.866 12.647  39.561  1.00 27.52 ? 297  VAL B CG2   1 
ATOM   7819  N  N     . SER B 1 278 ? -37.088 12.792  37.309  1.00 26.96 ? 298  SER B N     1 
ATOM   7820  C  CA    A SER B 1 278 ? -35.795 12.134  37.447  0.60 26.85 ? 298  SER B CA    1 
ATOM   7821  C  CA    B SER B 1 278 ? -35.786 12.148  37.452  0.40 26.80 ? 298  SER B CA    1 
ATOM   7822  C  C     . SER B 1 278 ? -35.606 11.590  38.863  1.00 26.60 ? 298  SER B C     1 
ATOM   7823  O  O     . SER B 1 278 ? -36.148 12.126  39.832  1.00 26.48 ? 298  SER B O     1 
ATOM   7824  C  CB    A SER B 1 278 ? -34.662 13.098  37.091  0.60 26.93 ? 298  SER B CB    1 
ATOM   7825  C  CB    B SER B 1 278 ? -34.666 13.145  37.145  0.40 26.86 ? 298  SER B CB    1 
ATOM   7826  O  OG    A SER B 1 278 ? -34.643 14.214  37.967  0.60 27.11 ? 298  SER B OG    1 
ATOM   7827  O  OG    B SER B 1 278 ? -35.034 14.024  36.097  0.40 26.78 ? 298  SER B OG    1 
ATOM   7828  N  N     . GLY B 1 279 ? -34.846 10.510  38.973  1.00 26.15 ? 299  GLY B N     1 
ATOM   7829  C  CA    . GLY B 1 279 ? -34.593 9.867   40.255  1.00 25.64 ? 299  GLY B CA    1 
ATOM   7830  C  C     . GLY B 1 279 ? -33.457 10.521  41.011  1.00 25.15 ? 299  GLY B C     1 
ATOM   7831  O  O     . GLY B 1 279 ? -32.830 11.471  40.514  1.00 24.62 ? 299  GLY B O     1 
ATOM   7832  N  N     . PRO B 1 280 ? -33.170 10.010  42.216  1.00 24.54 ? 300  PRO B N     1 
ATOM   7833  C  CA    . PRO B 1 280 ? -32.121 10.585  43.027  1.00 24.53 ? 300  PRO B CA    1 
ATOM   7834  C  C     . PRO B 1 280 ? -30.781 10.520  42.316  1.00 24.28 ? 300  PRO B C     1 
ATOM   7835  O  O     . PRO B 1 280 ? -30.572 9.655   41.461  1.00 24.13 ? 300  PRO B O     1 
ATOM   7836  C  CB    . PRO B 1 280 ? -32.108 9.711   44.292  1.00 24.29 ? 300  PRO B CB    1 
ATOM   7837  C  CG    . PRO B 1 280 ? -33.285 8.875   44.238  1.00 24.93 ? 300  PRO B CG    1 
ATOM   7838  C  CD    . PRO B 1 280 ? -33.747 8.806   42.830  1.00 25.11 ? 300  PRO B CD    1 
ATOM   7839  N  N     . ARG B 1 281 ? -29.889 11.436  42.659  1.00 24.30 ? 301  ARG B N     1 
ATOM   7840  C  CA    . ARG B 1 281 ? -28.563 11.431  42.068  1.00 25.17 ? 301  ARG B CA    1 
ATOM   7841  C  C     . ARG B 1 281 ? -27.496 11.728  43.111  1.00 24.74 ? 301  ARG B C     1 
ATOM   7842  O  O     . ARG B 1 281 ? -27.774 12.312  44.161  1.00 24.63 ? 301  ARG B O     1 
ATOM   7843  C  CB    . ARG B 1 281 ? -28.493 12.405  40.876  1.00 25.68 ? 301  ARG B CB    1 
ATOM   7844  C  CG    . ARG B 1 281 ? -28.364 13.868  41.241  1.00 27.87 ? 301  ARG B CG    1 
ATOM   7845  C  CD    . ARG B 1 281 ? -27.870 14.742  40.068  1.00 30.34 ? 301  ARG B CD    1 
ATOM   7846  N  NE    . ARG B 1 281 ? -27.409 16.033  40.576  1.00 31.52 ? 301  ARG B NE    1 
ATOM   7847  C  CZ    . ARG B 1 281 ? -28.208 17.010  41.012  1.00 33.48 ? 301  ARG B CZ    1 
ATOM   7848  N  NH1   . ARG B 1 281 ? -29.534 16.867  40.980  1.00 33.31 ? 301  ARG B NH1   1 
ATOM   7849  N  NH2   . ARG B 1 281 ? -27.680 18.150  41.475  1.00 33.48 ? 301  ARG B NH2   1 
ATOM   7850  N  N     . LEU B 1 282 ? -26.281 11.290  42.817  1.00 24.72 ? 302  LEU B N     1 
ATOM   7851  C  CA    . LEU B 1 282 ? -25.115 11.594  43.642  1.00 24.92 ? 302  LEU B CA    1 
ATOM   7852  C  C     . LEU B 1 282 ? -24.660 13.040  43.456  1.00 24.40 ? 302  LEU B C     1 
ATOM   7853  O  O     . LEU B 1 282 ? -24.593 13.524  42.339  1.00 23.65 ? 302  LEU B O     1 
ATOM   7854  C  CB    . LEU B 1 282 ? -23.938 10.697  43.265  1.00 25.12 ? 302  LEU B CB    1 
ATOM   7855  C  CG    . LEU B 1 282 ? -23.722 9.415   44.043  1.00 26.69 ? 302  LEU B CG    1 
ATOM   7856  C  CD1   . LEU B 1 282 ? -24.944 8.551   43.965  1.00 26.07 ? 302  LEU B CD1   1 
ATOM   7857  C  CD2   . LEU B 1 282 ? -22.480 8.698   43.466  1.00 26.98 ? 302  LEU B CD2   1 
ATOM   7858  N  N     . VAL B 1 283 ? -24.328 13.708  44.556  1.00 24.41 ? 303  VAL B N     1 
ATOM   7859  C  CA    . VAL B 1 283 ? -23.637 14.997  44.497  1.00 24.30 ? 303  VAL B CA    1 
ATOM   7860  C  C     . VAL B 1 283 ? -22.305 14.840  45.211  1.00 24.03 ? 303  VAL B C     1 
ATOM   7861  O  O     . VAL B 1 283 ? -22.194 14.071  46.160  1.00 23.96 ? 303  VAL B O     1 
ATOM   7862  C  CB    . VAL B 1 283 ? -24.460 16.147  45.111  1.00 24.38 ? 303  VAL B CB    1 
ATOM   7863  C  CG1   . VAL B 1 283 ? -25.749 16.307  44.358  1.00 24.79 ? 303  VAL B CG1   1 
ATOM   7864  C  CG2   . VAL B 1 283 ? -24.728 15.915  46.589  1.00 24.27 ? 303  VAL B CG2   1 
ATOM   7865  N  N     . GLN B 1 284 ? -21.287 15.533  44.717  1.00 23.93 ? 304  GLN B N     1 
ATOM   7866  C  CA    . GLN B 1 284 ? -19.956 15.476  45.304  1.00 23.93 ? 304  GLN B CA    1 
ATOM   7867  C  C     . GLN B 1 284 ? -19.422 16.907  45.473  1.00 24.62 ? 304  GLN B C     1 
ATOM   7868  O  O     . GLN B 1 284 ? -18.412 17.274  44.869  1.00 23.98 ? 304  GLN B O     1 
ATOM   7869  C  CB    . GLN B 1 284 ? -19.026 14.635  44.416  1.00 23.74 ? 304  GLN B CB    1 
ATOM   7870  C  CG    . GLN B 1 284 ? -17.675 14.273  45.063  1.00 22.49 ? 304  GLN B CG    1 
ATOM   7871  C  CD    . GLN B 1 284 ? -16.830 13.363  44.197  1.00 20.27 ? 304  GLN B CD    1 
ATOM   7872  O  OE1   . GLN B 1 284 ? -16.621 12.201  44.527  1.00 19.57 ? 304  GLN B OE1   1 
ATOM   7873  N  NE2   . GLN B 1 284 ? -16.353 13.883  43.076  1.00 19.64 ? 304  GLN B NE2   1 
ATOM   7874  N  N     . PRO B 1 285 ? -20.101 17.725  46.304  1.00 25.53 ? 305  PRO B N     1 
ATOM   7875  C  CA    . PRO B 1 285 ? -19.682 19.131  46.464  1.00 26.03 ? 305  PRO B CA    1 
ATOM   7876  C  C     . PRO B 1 285 ? -18.255 19.338  46.975  1.00 26.30 ? 305  PRO B C     1 
ATOM   7877  O  O     . PRO B 1 285 ? -17.654 20.366  46.673  1.00 26.71 ? 305  PRO B O     1 
ATOM   7878  C  CB    . PRO B 1 285 ? -20.699 19.711  47.472  1.00 26.06 ? 305  PRO B CB    1 
ATOM   7879  C  CG    . PRO B 1 285 ? -21.403 18.547  48.071  1.00 25.89 ? 305  PRO B CG    1 
ATOM   7880  C  CD    . PRO B 1 285 ? -21.319 17.421  47.076  1.00 25.71 ? 305  PRO B CD    1 
ATOM   7881  N  N     . HIS B 1 286 ? -17.712 18.382  47.721  1.00 26.92 ? 306  HIS B N     1 
ATOM   7882  C  CA    . HIS B 1 286 ? -16.378 18.538  48.301  1.00 27.44 ? 306  HIS B CA    1 
ATOM   7883  C  C     . HIS B 1 286 ? -15.296 17.857  47.478  1.00 27.65 ? 306  HIS B C     1 
ATOM   7884  O  O     . HIS B 1 286 ? -14.168 17.701  47.935  1.00 28.23 ? 306  HIS B O     1 
ATOM   7885  C  CB    . HIS B 1 286 ? -16.386 18.038  49.730  1.00 27.99 ? 306  HIS B CB    1 
ATOM   7886  C  CG    . HIS B 1 286 ? -17.504 18.611  50.537  1.00 29.80 ? 306  HIS B CG    1 
ATOM   7887  N  ND1   . HIS B 1 286 ? -17.678 19.969  50.696  1.00 32.38 ? 306  HIS B ND1   1 
ATOM   7888  C  CD2   . HIS B 1 286 ? -18.530 18.018  51.189  1.00 31.44 ? 306  HIS B CD2   1 
ATOM   7889  C  CE1   . HIS B 1 286 ? -18.758 20.189  51.425  1.00 33.11 ? 306  HIS B CE1   1 
ATOM   7890  N  NE2   . HIS B 1 286 ? -19.293 19.022  51.739  1.00 33.30 ? 306  HIS B NE2   1 
ATOM   7891  N  N     . GLY B 1 287 ? -15.638 17.474  46.252  1.00 27.36 ? 307  GLY B N     1 
ATOM   7892  C  CA    . GLY B 1 287 ? -14.683 16.898  45.332  1.00 26.91 ? 307  GLY B CA    1 
ATOM   7893  C  C     . GLY B 1 287 ? -14.354 15.467  45.690  1.00 26.60 ? 307  GLY B C     1 
ATOM   7894  O  O     . GLY B 1 287 ? -14.802 14.973  46.719  1.00 26.25 ? 307  GLY B O     1 
ATOM   7895  N  N     . PRO B 1 288 ? -13.565 14.794  44.835  1.00 26.51 ? 308  PRO B N     1 
ATOM   7896  C  CA    . PRO B 1 288 ? -13.157 13.399  45.047  1.00 26.47 ? 308  PRO B CA    1 
ATOM   7897  C  C     . PRO B 1 288 ? -12.386 13.170  46.345  1.00 26.26 ? 308  PRO B C     1 
ATOM   7898  O  O     . PRO B 1 288 ? -11.620 14.031  46.760  1.00 26.66 ? 308  PRO B O     1 
ATOM   7899  C  CB    . PRO B 1 288 ? -12.239 13.120  43.856  1.00 26.46 ? 308  PRO B CB    1 
ATOM   7900  C  CG    . PRO B 1 288 ? -12.659 14.094  42.802  1.00 26.72 ? 308  PRO B CG    1 
ATOM   7901  C  CD    . PRO B 1 288 ? -13.104 15.316  43.535  1.00 26.43 ? 308  PRO B CD    1 
ATOM   7902  N  N     . ARG B 1 289 ? -12.580 12.005  46.960  1.00 26.03 ? 309  ARG B N     1 
ATOM   7903  C  CA    . ARG B 1 289 ? -11.873 11.642  48.191  1.00 25.66 ? 309  ARG B CA    1 
ATOM   7904  C  C     . ARG B 1 289 ? -10.732 10.690  47.888  1.00 25.73 ? 309  ARG B C     1 
ATOM   7905  O  O     . ARG B 1 289 ? -9.976  10.318  48.772  1.00 26.28 ? 309  ARG B O     1 
ATOM   7906  C  CB    . ARG B 1 289 ? -12.840 11.027  49.207  1.00 25.40 ? 309  ARG B CB    1 
ATOM   7907  C  CG    . ARG B 1 289 ? -14.044 11.921  49.485  1.00 24.51 ? 309  ARG B CG    1 
ATOM   7908  C  CD    . ARG B 1 289 ? -14.639 11.668  50.848  1.00 24.12 ? 309  ARG B CD    1 
ATOM   7909  N  NE    . ARG B 1 289 ? -15.163 10.315  51.000  1.00 24.55 ? 309  ARG B NE    1 
ATOM   7910  C  CZ    . ARG B 1 289 ? -15.584 9.793   52.151  1.00 24.49 ? 309  ARG B CZ    1 
ATOM   7911  N  NH1   . ARG B 1 289 ? -15.538 10.503  53.274  1.00 24.15 ? 309  ARG B NH1   1 
ATOM   7912  N  NH2   . ARG B 1 289 ? -16.053 8.548   52.184  1.00 24.45 ? 309  ARG B NH2   1 
ATOM   7913  N  N     . PHE B 1 290 ? -10.607 10.313  46.623  1.00 25.71 ? 310  PHE B N     1 
ATOM   7914  C  CA    . PHE B 1 290 ? -9.448  9.572   46.143  1.00 25.22 ? 310  PHE B CA    1 
ATOM   7915  C  C     . PHE B 1 290 ? -8.531  10.553  45.427  1.00 25.35 ? 310  PHE B C     1 
ATOM   7916  O  O     . PHE B 1 290 ? -8.971  11.610  44.980  1.00 25.27 ? 310  PHE B O     1 
ATOM   7917  C  CB    . PHE B 1 290 ? -9.885  8.442   45.193  1.00 25.18 ? 310  PHE B CB    1 
ATOM   7918  C  CG    . PHE B 1 290 ? -10.780 8.902   44.076  1.00 23.91 ? 310  PHE B CG    1 
ATOM   7919  C  CD1   . PHE B 1 290 ? -10.248 9.278   42.855  1.00 23.50 ? 310  PHE B CD1   1 
ATOM   7920  C  CD2   . PHE B 1 290 ? -12.152 8.983   44.262  1.00 23.18 ? 310  PHE B CD2   1 
ATOM   7921  C  CE1   . PHE B 1 290 ? -11.070 9.718   41.832  1.00 23.88 ? 310  PHE B CE1   1 
ATOM   7922  C  CE2   . PHE B 1 290 ? -12.985 9.417   43.247  1.00 23.39 ? 310  PHE B CE2   1 
ATOM   7923  C  CZ    . PHE B 1 290 ? -12.441 9.789   42.026  1.00 24.11 ? 310  PHE B CZ    1 
ATOM   7924  N  N     . ARG B 1 291 ? -7.254  10.211  45.336  1.00 25.77 ? 311  ARG B N     1 
ATOM   7925  C  CA    . ARG B 1 291 ? -6.282  11.023  44.606  1.00 26.13 ? 311  ARG B CA    1 
ATOM   7926  C  C     . ARG B 1 291 ? -5.861  10.254  43.369  1.00 26.32 ? 311  ARG B C     1 
ATOM   7927  O  O     . ARG B 1 291 ? -5.476  9.091   43.463  1.00 26.10 ? 311  ARG B O     1 
ATOM   7928  C  CB    . ARG B 1 291 ? -5.057  11.321  45.480  1.00 25.99 ? 311  ARG B CB    1 
ATOM   7929  N  N     . LEU B 1 292 ? -5.960  10.899  42.212  1.00 26.84 ? 312  LEU B N     1 
ATOM   7930  C  CA    . LEU B 1 292 ? -5.545  10.303  40.949  1.00 27.16 ? 312  LEU B CA    1 
ATOM   7931  C  C     . LEU B 1 292 ? -4.410  11.148  40.423  1.00 27.46 ? 312  LEU B C     1 
ATOM   7932  O  O     . LEU B 1 292 ? -4.599  12.330  40.166  1.00 27.80 ? 312  LEU B O     1 
ATOM   7933  C  CB    . LEU B 1 292 ? -6.698  10.301  39.943  1.00 26.99 ? 312  LEU B CB    1 
ATOM   7934  C  CG    . LEU B 1 292 ? -6.419  9.811   38.515  1.00 27.02 ? 312  LEU B CG    1 
ATOM   7935  C  CD1   . LEU B 1 292 ? -6.084  8.324   38.475  1.00 26.60 ? 312  LEU B CD1   1 
ATOM   7936  C  CD2   . LEU B 1 292 ? -7.623  10.095  37.638  1.00 27.32 ? 312  LEU B CD2   1 
ATOM   7937  N  N     . GLU B 1 293 ? -3.233  10.546  40.295  1.00 27.73 ? 313  GLU B N     1 
ATOM   7938  C  CA    . GLU B 1 293 ? -2.092  11.190  39.655  1.00 28.02 ? 313  GLU B CA    1 
ATOM   7939  C  C     . GLU B 1 293 ? -1.592  10.244  38.577  1.00 27.97 ? 313  GLU B C     1 
ATOM   7940  O  O     . GLU B 1 293 ? -0.987  9.223   38.879  1.00 28.18 ? 313  GLU B O     1 
ATOM   7941  C  CB    . GLU B 1 293 ? -0.985  11.480  40.672  1.00 27.85 ? 313  GLU B CB    1 
ATOM   7942  N  N     . GLY B 1 294 ? -1.877  10.581  37.323  1.00 28.37 ? 314  GLY B N     1 
ATOM   7943  C  CA    . GLY B 1 294 ? -1.544  9.723   36.185  1.00 28.33 ? 314  GLY B CA    1 
ATOM   7944  C  C     . GLY B 1 294 ? -2.376  8.455   36.241  1.00 28.31 ? 314  GLY B C     1 
ATOM   7945  O  O     . GLY B 1 294 ? -3.609  8.515   36.217  1.00 28.24 ? 314  GLY B O     1 
ATOM   7946  N  N     . ASN B 1 295 ? -1.696  7.315   36.357  1.00 27.96 ? 315  ASN B N     1 
ATOM   7947  C  CA    . ASN B 1 295 ? -2.359  6.030   36.511  1.00 27.72 ? 315  ASN B CA    1 
ATOM   7948  C  C     . ASN B 1 295 ? -2.253  5.489   37.939  1.00 27.36 ? 315  ASN B C     1 
ATOM   7949  O  O     . ASN B 1 295 ? -2.437  4.294   38.149  1.00 27.42 ? 315  ASN B O     1 
ATOM   7950  C  CB    . ASN B 1 295 ? -1.789  5.021   35.498  1.00 27.93 ? 315  ASN B CB    1 
ATOM   7951  C  CG    . ASN B 1 295 ? -0.403  4.497   35.890  1.00 27.82 ? 315  ASN B CG    1 
ATOM   7952  O  OD1   . ASN B 1 295 ? 0.431   5.244   36.391  1.00 31.29 ? 315  ASN B OD1   1 
ATOM   7953  N  ND2   . ASN B 1 295 ? -0.166  3.215   35.665  1.00 24.76 ? 315  ASN B ND2   1 
ATOM   7954  N  N     . ALA B 1 296 ? -1.964  6.369   38.909  1.00 26.87 ? 316  ALA B N     1 
ATOM   7955  C  CA    . ALA B 1 296 ? -1.808  5.987   40.323  1.00 26.40 ? 316  ALA B CA    1 
ATOM   7956  C  C     . ALA B 1 296 ? -2.989  6.483   41.147  1.00 25.72 ? 316  ALA B C     1 
ATOM   7957  O  O     . ALA B 1 296 ? -3.344  7.653   41.073  1.00 25.43 ? 316  ALA B O     1 
ATOM   7958  C  CB    . ALA B 1 296 ? -0.508  6.561   40.903  1.00 26.45 ? 316  ALA B CB    1 
ATOM   7959  N  N     . VAL B 1 297 ? -3.579  5.597   41.949  1.00 25.31 ? 317  VAL B N     1 
ATOM   7960  C  CA    . VAL B 1 297 ? -4.744  5.957   42.765  1.00 24.62 ? 317  VAL B CA    1 
ATOM   7961  C  C     . VAL B 1 297 ? -4.472  5.763   44.254  1.00 24.26 ? 317  VAL B C     1 
ATOM   7962  O  O     . VAL B 1 297 ? -3.921  4.749   44.664  1.00 24.08 ? 317  VAL B O     1 
ATOM   7963  C  CB    . VAL B 1 297 ? -5.984  5.140   42.361  1.00 24.89 ? 317  VAL B CB    1 
ATOM   7964  C  CG1   . VAL B 1 297 ? -7.213  5.558   43.209  1.00 24.20 ? 317  VAL B CG1   1 
ATOM   7965  C  CG2   . VAL B 1 297 ? -6.273  5.315   40.866  1.00 23.80 ? 317  VAL B CG2   1 
ATOM   7966  N  N     . LEU B 1 298 ? -4.844  6.761   45.050  1.00 24.27 ? 318  LEU B N     1 
ATOM   7967  C  CA    . LEU B 1 298 ? -4.838  6.657   46.511  1.00 24.27 ? 318  LEU B CA    1 
ATOM   7968  C  C     . LEU B 1 298 ? -6.269  6.838   47.005  1.00 23.50 ? 318  LEU B C     1 
ATOM   7969  O  O     . LEU B 1 298 ? -6.985  7.703   46.502  1.00 23.88 ? 318  LEU B O     1 
ATOM   7970  C  CB    . LEU B 1 298 ? -3.951  7.737   47.135  1.00 24.51 ? 318  LEU B CB    1 
ATOM   7971  C  CG    . LEU B 1 298 ? -2.501  7.818   46.656  1.00 26.48 ? 318  LEU B CG    1 
ATOM   7972  C  CD1   . LEU B 1 298 ? -1.892  9.155   47.097  1.00 27.83 ? 318  LEU B CD1   1 
ATOM   7973  C  CD2   . LEU B 1 298 ? -1.682  6.651   47.178  1.00 26.40 ? 318  LEU B CD2   1 
ATOM   7974  N  N     . TYR B 1 299 ? -6.690  6.027   47.971  1.00 22.76 ? 319  TYR B N     1 
ATOM   7975  C  CA    . TYR B 1 299 ? -8.047  6.136   48.542  1.00 22.32 ? 319  TYR B CA    1 
ATOM   7976  C  C     . TYR B 1 299 ? -8.131  5.470   49.912  1.00 22.17 ? 319  TYR B C     1 
ATOM   7977  O  O     . TYR B 1 299 ? -8.115  4.243   50.021  1.00 21.51 ? 319  TYR B O     1 
ATOM   7978  C  CB    . TYR B 1 299 ? -9.065  5.514   47.592  1.00 22.19 ? 319  TYR B CB    1 
ATOM   7979  C  CG    . TYR B 1 299 ? -10.470 5.355   48.136  1.00 21.54 ? 319  TYR B CG    1 
ATOM   7980  C  CD1   . TYR B 1 299 ? -11.271 6.456   48.390  1.00 21.81 ? 319  TYR B CD1   1 
ATOM   7981  C  CD2   . TYR B 1 299 ? -11.011 4.097   48.353  1.00 21.95 ? 319  TYR B CD2   1 
ATOM   7982  C  CE1   . TYR B 1 299 ? -12.576 6.307   48.871  1.00 21.64 ? 319  TYR B CE1   1 
ATOM   7983  C  CE2   . TYR B 1 299 ? -12.317 3.941   48.827  1.00 21.77 ? 319  TYR B CE2   1 
ATOM   7984  C  CZ    . TYR B 1 299 ? -13.091 5.043   49.085  1.00 21.38 ? 319  TYR B CZ    1 
ATOM   7985  O  OH    . TYR B 1 299 ? -14.391 4.876   49.553  1.00 22.57 ? 319  TYR B OH    1 
ATOM   7986  N  N     . GLY B 1 300 ? -8.231  6.289   50.956  1.00 22.66 ? 320  GLY B N     1 
ATOM   7987  C  CA    . GLY B 1 300 ? -8.146  5.799   52.327  1.00 22.72 ? 320  GLY B CA    1 
ATOM   7988  C  C     . GLY B 1 300 ? -6.880  4.986   52.491  1.00 22.99 ? 320  GLY B C     1 
ATOM   7989  O  O     . GLY B 1 300 ? -5.780  5.505   52.318  1.00 23.42 ? 320  GLY B O     1 
ATOM   7990  N  N     . GLY B 1 301 ? -7.033  3.703   52.803  1.00 23.13 ? 321  GLY B N     1 
ATOM   7991  C  CA    . GLY B 1 301 ? -5.885  2.823   52.972  1.00 23.05 ? 321  GLY B CA    1 
ATOM   7992  C  C     . GLY B 1 301 ? -5.279  2.337   51.671  1.00 23.24 ? 321  GLY B C     1 
ATOM   7993  O  O     . GLY B 1 301 ? -4.178  1.773   51.678  1.00 22.95 ? 321  GLY B O     1 
ATOM   7994  N  N     . TRP B 1 302 ? -5.994  2.540   50.558  1.00 23.22 ? 322  TRP B N     1 
ATOM   7995  C  CA    . TRP B 1 302 ? -5.638  1.908   49.287  1.00 23.19 ? 322  TRP B CA    1 
ATOM   7996  C  C     . TRP B 1 302 ? -4.598  2.691   48.503  1.00 23.23 ? 322  TRP B C     1 
ATOM   7997  O  O     . TRP B 1 302 ? -4.661  3.910   48.411  1.00 22.55 ? 322  TRP B O     1 
ATOM   7998  C  CB    . TRP B 1 302 ? -6.858  1.741   48.379  1.00 22.90 ? 322  TRP B CB    1 
ATOM   7999  C  CG    . TRP B 1 302 ? -7.868  0.772   48.863  1.00 22.56 ? 322  TRP B CG    1 
ATOM   8000  C  CD1   . TRP B 1 302 ? -9.046  1.064   49.479  1.00 20.79 ? 322  TRP B CD1   1 
ATOM   8001  C  CD2   . TRP B 1 302 ? -7.817  -0.651  48.750  1.00 22.13 ? 322  TRP B CD2   1 
ATOM   8002  N  NE1   . TRP B 1 302 ? -9.727  -0.084  49.766  1.00 21.40 ? 322  TRP B NE1   1 
ATOM   8003  C  CE2   . TRP B 1 302 ? -8.999  -1.156  49.331  1.00 21.85 ? 322  TRP B CE2   1 
ATOM   8004  C  CE3   . TRP B 1 302 ? -6.891  -1.549  48.223  1.00 21.86 ? 322  TRP B CE3   1 
ATOM   8005  C  CZ2   . TRP B 1 302 ? -9.279  -2.513  49.392  1.00 21.51 ? 322  TRP B CZ2   1 
ATOM   8006  C  CZ3   . TRP B 1 302 ? -7.168  -2.902  48.291  1.00 21.61 ? 322  TRP B CZ3   1 
ATOM   8007  C  CH2   . TRP B 1 302 ? -8.345  -3.370  48.877  1.00 21.85 ? 322  TRP B CH2   1 
ATOM   8008  N  N     . SER B 1 303 ? -3.669  1.955   47.912  1.00 23.30 ? 323  SER B N     1 
ATOM   8009  C  CA    . SER B 1 303 ? -2.797  2.487   46.880  1.00 23.86 ? 323  SER B CA    1 
ATOM   8010  C  C     . SER B 1 303 ? -2.720  1.465   45.748  1.00 23.57 ? 323  SER B C     1 
ATOM   8011  O  O     . SER B 1 303 ? -2.510  0.285   45.999  1.00 23.71 ? 323  SER B O     1 
ATOM   8012  C  CB    . SER B 1 303 ? -1.398  2.747   47.449  1.00 23.91 ? 323  SER B CB    1 
ATOM   8013  O  OG    . SER B 1 303 ? -0.549  3.226   46.425  1.00 26.19 ? 323  SER B OG    1 
ATOM   8014  N  N     . PHE B 1 304 ? -2.914  1.909   44.509  1.00 23.74 ? 324  PHE B N     1 
ATOM   8015  C  CA    . PHE B 1 304 ? -2.733  1.030   43.360  1.00 23.47 ? 324  PHE B CA    1 
ATOM   8016  C  C     . PHE B 1 304 ? -2.505  1.799   42.058  1.00 23.38 ? 324  PHE B C     1 
ATOM   8017  O  O     . PHE B 1 304 ? -2.783  3.004   41.962  1.00 23.11 ? 324  PHE B O     1 
ATOM   8018  C  CB    . PHE B 1 304 ? -3.928  0.072   43.214  1.00 23.58 ? 324  PHE B CB    1 
ATOM   8019  C  CG    . PHE B 1 304 ? -5.234  0.758   42.909  1.00 23.42 ? 324  PHE B CG    1 
ATOM   8020  C  CD1   . PHE B 1 304 ? -5.633  0.971   41.589  1.00 23.21 ? 324  PHE B CD1   1 
ATOM   8021  C  CD2   . PHE B 1 304 ? -6.072  1.167   43.937  1.00 22.98 ? 324  PHE B CD2   1 
ATOM   8022  C  CE1   . PHE B 1 304 ? -6.857  1.588   41.289  1.00 22.88 ? 324  PHE B CE1   1 
ATOM   8023  C  CE2   . PHE B 1 304 ? -7.292  1.782   43.661  1.00 22.45 ? 324  PHE B CE2   1 
ATOM   8024  C  CZ    . PHE B 1 304 ? -7.687  1.999   42.329  1.00 23.24 ? 324  PHE B CZ    1 
ATOM   8025  N  N     . ALA B 1 305 ? -1.984  1.072   41.070  1.00 23.15 ? 325  ALA B N     1 
ATOM   8026  C  CA    . ALA B 1 305 ? -1.828  1.557   39.711  1.00 23.40 ? 325  ALA B CA    1 
ATOM   8027  C  C     . ALA B 1 305 ? -2.796  0.795   38.826  1.00 23.56 ? 325  ALA B C     1 
ATOM   8028  O  O     . ALA B 1 305 ? -3.296  -0.265  39.210  1.00 23.82 ? 325  ALA B O     1 
ATOM   8029  C  CB    . ALA B 1 305 ? -0.407  1.337   39.222  1.00 23.15 ? 325  ALA B CB    1 
ATOM   8030  N  N     . PHE B 1 306 ? -3.060  1.327   37.640  1.00 23.78 ? 326  PHE B N     1 
ATOM   8031  C  CA    . PHE B 1 306 ? -3.930  0.635   36.687  1.00 24.39 ? 326  PHE B CA    1 
ATOM   8032  C  C     . PHE B 1 306 ? -3.485  0.848   35.256  1.00 25.02 ? 326  PHE B C     1 
ATOM   8033  O  O     . PHE B 1 306 ? -2.812  1.831   34.935  1.00 24.69 ? 326  PHE B O     1 
ATOM   8034  C  CB    . PHE B 1 306 ? -5.397  1.080   36.847  1.00 24.28 ? 326  PHE B CB    1 
ATOM   8035  C  CG    . PHE B 1 306 ? -5.630  2.522   36.539  1.00 24.16 ? 326  PHE B CG    1 
ATOM   8036  C  CD1   . PHE B 1 306 ? -5.907  2.929   35.245  1.00 23.45 ? 326  PHE B CD1   1 
ATOM   8037  C  CD2   . PHE B 1 306 ? -5.578  3.477   37.546  1.00 24.81 ? 326  PHE B CD2   1 
ATOM   8038  C  CE1   . PHE B 1 306 ? -6.118  4.270   34.950  1.00 24.33 ? 326  PHE B CE1   1 
ATOM   8039  C  CE2   . PHE B 1 306 ? -5.788  4.817   37.264  1.00 24.78 ? 326  PHE B CE2   1 
ATOM   8040  C  CZ    . PHE B 1 306 ? -6.064  5.215   35.959  1.00 24.42 ? 326  PHE B CZ    1 
ATOM   8041  N  N     . ARG B 1 307 ? -3.871  -0.086  34.398  1.00 26.08 ? 327  ARG B N     1 
ATOM   8042  C  CA    . ARG B 1 307 ? -3.679  0.080   32.973  1.00 26.92 ? 327  ARG B CA    1 
ATOM   8043  C  C     . ARG B 1 307 ? -4.830  -0.546  32.200  1.00 26.95 ? 327  ARG B C     1 
ATOM   8044  O  O     . ARG B 1 307 ? -5.566  -1.391  32.723  1.00 26.97 ? 327  ARG B O     1 
ATOM   8045  C  CB    . ARG B 1 307 ? -2.345  -0.523  32.537  1.00 27.33 ? 327  ARG B CB    1 
ATOM   8046  C  CG    . ARG B 1 307 ? -2.311  -2.024  32.543  1.00 29.14 ? 327  ARG B CG    1 
ATOM   8047  C  CD    . ARG B 1 307 ? -1.081  -2.555  31.835  1.00 31.77 ? 327  ARG B CD    1 
ATOM   8048  N  NE    . ARG B 1 307 ? -1.065  -2.239  30.399  1.00 34.14 ? 327  ARG B NE    1 
ATOM   8049  C  CZ    . ARG B 1 307 ? -0.239  -2.803  29.518  1.00 33.63 ? 327  ARG B CZ    1 
ATOM   8050  N  NH1   . ARG B 1 307 ? -0.288  -2.449  28.232  1.00 34.41 ? 327  ARG B NH1   1 
ATOM   8051  N  NH2   . ARG B 1 307 ? 0.628   -3.730  29.912  1.00 33.27 ? 327  ARG B NH2   1 
ATOM   8052  N  N     . LEU B 1 308 ? -4.985  -0.092  30.965  1.00 26.83 ? 328  LEU B N     1 
ATOM   8053  C  CA    . LEU B 1 308 ? -5.987  -0.605  30.067  1.00 26.93 ? 328  LEU B CA    1 
ATOM   8054  C  C     . LEU B 1 308 ? -5.247  -1.197  28.873  1.00 26.97 ? 328  LEU B C     1 
ATOM   8055  O  O     . LEU B 1 308 ? -4.854  -0.487  27.954  1.00 26.91 ? 328  LEU B O     1 
ATOM   8056  C  CB    . LEU B 1 308 ? -6.939  0.507   29.640  1.00 26.67 ? 328  LEU B CB    1 
ATOM   8057  C  CG    . LEU B 1 308 ? -8.115  0.068   28.761  1.00 27.17 ? 328  LEU B CG    1 
ATOM   8058  C  CD1   . LEU B 1 308 ? -8.822  -1.158  29.330  1.00 27.07 ? 328  LEU B CD1   1 
ATOM   8059  C  CD2   . LEU B 1 308 ? -9.092  1.216   28.611  1.00 27.09 ? 328  LEU B CD2   1 
ATOM   8060  N  N     . ARG B 1 309 ? -5.049  -2.505  28.925  1.00 27.06 ? 329  ARG B N     1 
ATOM   8061  C  CA    . ARG B 1 309 ? -4.316  -3.242  27.913  1.00 27.55 ? 329  ARG B CA    1 
ATOM   8062  C  C     . ARG B 1 309 ? -5.220  -3.424  26.704  1.00 26.81 ? 329  ARG B C     1 
ATOM   8063  O  O     . ARG B 1 309 ? -6.298  -4.015  26.821  1.00 26.67 ? 329  ARG B O     1 
ATOM   8064  C  CB    . ARG B 1 309 ? -3.899  -4.594  28.495  1.00 28.18 ? 329  ARG B CB    1 
ATOM   8065  C  CG    . ARG B 1 309 ? -2.811  -5.329  27.739  1.00 30.36 ? 329  ARG B CG    1 
ATOM   8066  C  CD    . ARG B 1 309 ? -2.267  -6.481  28.567  1.00 33.04 ? 329  ARG B CD    1 
ATOM   8067  N  NE    . ARG B 1 309 ? -1.189  -7.179  27.867  1.00 37.13 ? 329  ARG B NE    1 
ATOM   8068  C  CZ    . ARG B 1 309 ? -1.263  -8.396  27.314  1.00 40.04 ? 329  ARG B CZ    1 
ATOM   8069  N  NH1   . ARG B 1 309 ? -2.382  -9.128  27.365  1.00 41.36 ? 329  ARG B NH1   1 
ATOM   8070  N  NH2   . ARG B 1 309 ? -0.189  -8.901  26.707  1.00 40.34 ? 329  ARG B NH2   1 
ATOM   8071  N  N     . SER B 1 310 ? -4.803  -2.880  25.561  1.00 26.18 ? 330  SER B N     1 
ATOM   8072  C  CA    . SER B 1 310 ? -5.630  -2.875  24.340  1.00 25.67 ? 330  SER B CA    1 
ATOM   8073  C  C     . SER B 1 310 ? -6.091  -4.273  23.944  1.00 25.57 ? 330  SER B C     1 
ATOM   8074  O  O     . SER B 1 310 ? -7.217  -4.444  23.472  1.00 25.48 ? 330  SER B O     1 
ATOM   8075  C  CB    . SER B 1 310 ? -4.865  -2.241  23.168  1.00 25.63 ? 330  SER B CB    1 
ATOM   8076  O  OG    . SER B 1 310 ? -4.502  -0.899  23.455  1.00 23.79 ? 330  SER B OG    1 
ATOM   8077  N  N     . SER B 1 311 ? -5.218  -5.264  24.139  1.00 25.62 ? 331  SER B N     1 
ATOM   8078  C  CA    . SER B 1 311 ? -5.517  -6.652  23.779  1.00 25.93 ? 331  SER B CA    1 
ATOM   8079  C  C     . SER B 1 311 ? -6.520  -7.302  24.738  1.00 26.17 ? 331  SER B C     1 
ATOM   8080  O  O     . SER B 1 311 ? -7.578  -7.773  24.294  1.00 27.83 ? 331  SER B O     1 
ATOM   8081  C  CB    . SER B 1 311 ? -4.229  -7.491  23.684  1.00 25.60 ? 331  SER B CB    1 
ATOM   8082  O  OG    . SER B 1 311 ? -3.417  -7.328  24.831  1.00 25.54 ? 331  SER B OG    1 
ATOM   8083  N  N     . SER B 1 312 ? -6.230  -7.270  26.036  1.00 25.88 ? 332  SER B N     1 
ATOM   8084  C  CA    . SER B 1 312 ? -6.943  -8.107  27.023  1.00 25.54 ? 332  SER B CA    1 
ATOM   8085  C  C     . SER B 1 312 ? -7.837  -7.369  28.022  1.00 25.66 ? 332  SER B C     1 
ATOM   8086  O  O     . SER B 1 312 ? -8.653  -8.002  28.680  1.00 25.79 ? 332  SER B O     1 
ATOM   8087  C  CB    . SER B 1 312 ? -5.936  -8.931  27.817  1.00 25.43 ? 332  SER B CB    1 
ATOM   8088  O  OG    . SER B 1 312 ? -5.085  -8.074  28.538  1.00 24.19 ? 332  SER B OG    1 
ATOM   8089  N  N     . GLY B 1 313 ? -7.660  -6.056  28.163  1.00 25.49 ? 333  GLY B N     1 
ATOM   8090  C  CA    . GLY B 1 313 ? -8.531  -5.245  29.004  1.00 25.12 ? 333  GLY B CA    1 
ATOM   8091  C  C     . GLY B 1 313 ? -7.927  -4.768  30.313  1.00 25.18 ? 333  GLY B C     1 
ATOM   8092  O  O     . GLY B 1 313 ? -6.698  -4.682  30.469  1.00 24.78 ? 333  GLY B O     1 
ATOM   8093  N  N     . LEU B 1 314 ? -8.814  -4.474  31.261  1.00 24.75 ? 334  LEU B N     1 
ATOM   8094  C  CA    . LEU B 1 314 ? -8.465  -3.747  32.474  1.00 24.80 ? 334  LEU B CA    1 
ATOM   8095  C  C     . LEU B 1 314 ? -7.541  -4.519  33.423  1.00 24.83 ? 334  LEU B C     1 
ATOM   8096  O  O     . LEU B 1 314 ? -7.675  -5.729  33.614  1.00 24.68 ? 334  LEU B O     1 
ATOM   8097  C  CB    . LEU B 1 314 ? -9.745  -3.343  33.216  1.00 24.88 ? 334  LEU B CB    1 
ATOM   8098  C  CG    . LEU B 1 314 ? -9.668  -2.228  34.268  1.00 25.08 ? 334  LEU B CG    1 
ATOM   8099  C  CD1   . LEU B 1 314 ? -9.048  -0.958  33.720  1.00 23.31 ? 334  LEU B CD1   1 
ATOM   8100  C  CD2   . LEU B 1 314 ? -11.079 -1.952  34.803  1.00 24.37 ? 334  LEU B CD2   1 
ATOM   8101  N  N     . GLN B 1 315 ? -6.591  -3.800  34.010  1.00 24.72 ? 335  GLN B N     1 
ATOM   8102  C  CA    . GLN B 1 315 ? -5.755  -4.361  35.071  1.00 24.64 ? 335  GLN B CA    1 
ATOM   8103  C  C     . GLN B 1 315 ? -5.570  -3.371  36.197  1.00 24.02 ? 335  GLN B C     1 
ATOM   8104  O  O     . GLN B 1 315 ? -5.505  -2.162  35.966  1.00 23.55 ? 335  GLN B O     1 
ATOM   8105  C  CB    . GLN B 1 315 ? -4.378  -4.730  34.533  1.00 24.75 ? 335  GLN B CB    1 
ATOM   8106  C  CG    . GLN B 1 315 ? -4.429  -5.500  33.249  1.00 25.87 ? 335  GLN B CG    1 
ATOM   8107  C  CD    . GLN B 1 315 ? -3.079  -6.035  32.866  1.00 27.36 ? 335  GLN B CD    1 
ATOM   8108  O  OE1   . GLN B 1 315 ? -2.067  -5.632  33.425  1.00 28.35 ? 335  GLN B OE1   1 
ATOM   8109  N  NE2   . GLN B 1 315 ? -3.054  -6.944  31.902  1.00 27.88 ? 335  GLN B NE2   1 
ATOM   8110  N  N     . VAL B 1 316 ? -5.497  -3.895  37.416  1.00 23.85 ? 336  VAL B N     1 
ATOM   8111  C  CA    . VAL B 1 316 ? -5.010  -3.129  38.549  1.00 23.65 ? 336  VAL B CA    1 
ATOM   8112  C  C     . VAL B 1 316 ? -3.726  -3.815  39.026  1.00 23.33 ? 336  VAL B C     1 
ATOM   8113  O  O     . VAL B 1 316 ? -3.634  -5.046  39.030  1.00 22.64 ? 336  VAL B O     1 
ATOM   8114  C  CB    . VAL B 1 316 ? -6.071  -2.991  39.662  1.00 23.78 ? 336  VAL B CB    1 
ATOM   8115  C  CG1   . VAL B 1 316 ? -7.357  -2.406  39.080  1.00 24.48 ? 336  VAL B CG1   1 
ATOM   8116  C  CG2   . VAL B 1 316 ? -6.351  -4.321  40.319  1.00 24.03 ? 336  VAL B CG2   1 
ATOM   8117  N  N     . LEU B 1 317 ? -2.732  -3.015  39.399  1.00 23.20 ? 337  LEU B N     1 
ATOM   8118  C  CA    . LEU B 1 317 ? -1.402  -3.538  39.729  1.00 23.23 ? 337  LEU B CA    1 
ATOM   8119  C  C     . LEU B 1 317 ? -0.836  -2.902  40.990  1.00 23.14 ? 337  LEU B C     1 
ATOM   8120  O  O     . LEU B 1 317 ? -1.183  -1.778  41.334  1.00 22.94 ? 337  LEU B O     1 
ATOM   8121  C  CB    . LEU B 1 317 ? -0.436  -3.284  38.571  1.00 23.16 ? 337  LEU B CB    1 
ATOM   8122  C  CG    . LEU B 1 317 ? -0.809  -4.003  37.267  1.00 23.26 ? 337  LEU B CG    1 
ATOM   8123  C  CD1   . LEU B 1 317 ? -0.801  -3.010  36.127  1.00 24.23 ? 337  LEU B CD1   1 
ATOM   8124  C  CD2   . LEU B 1 317 ? 0.093   -5.201  36.998  1.00 22.12 ? 337  LEU B CD2   1 
ATOM   8125  N  N     . ASN B 1 318 ? 0.039   -3.645  41.662  1.00 23.10 ? 338  ASN B N     1 
ATOM   8126  C  CA    . ASN B 1 318 ? 0.754   -3.168  42.839  1.00 23.14 ? 338  ASN B CA    1 
ATOM   8127  C  C     . ASN B 1 318 ? -0.200  -2.682  43.918  1.00 22.76 ? 338  ASN B C     1 
ATOM   8128  O  O     . ASN B 1 318 ? 0.026   -1.641  44.545  1.00 22.32 ? 338  ASN B O     1 
ATOM   8129  C  CB    . ASN B 1 318 ? 1.741   -2.058  42.450  1.00 23.21 ? 338  ASN B CB    1 
ATOM   8130  C  CG    . ASN B 1 318 ? 2.790   -1.833  43.507  1.00 23.48 ? 338  ASN B CG    1 
ATOM   8131  O  OD1   . ASN B 1 318 ? 3.196   -2.772  44.186  1.00 24.03 ? 338  ASN B OD1   1 
ATOM   8132  N  ND2   . ASN B 1 318 ? 3.234   -0.589  43.656  1.00 23.60 ? 338  ASN B ND2   1 
ATOM   8133  N  N     . VAL B 1 319 ? -1.266  -3.456  44.128  1.00 22.74 ? 339  VAL B N     1 
ATOM   8134  C  CA    . VAL B 1 319 ? -2.343  -3.056  45.013  1.00 22.78 ? 339  VAL B CA    1 
ATOM   8135  C  C     . VAL B 1 319 ? -1.853  -3.175  46.447  1.00 23.04 ? 339  VAL B C     1 
ATOM   8136  O  O     . VAL B 1 319 ? -1.400  -4.232  46.851  1.00 22.85 ? 339  VAL B O     1 
ATOM   8137  C  CB    . VAL B 1 319 ? -3.633  -3.918  44.823  1.00 22.88 ? 339  VAL B CB    1 
ATOM   8138  C  CG1   . VAL B 1 319 ? -4.739  -3.402  45.725  1.00 22.54 ? 339  VAL B CG1   1 
ATOM   8139  C  CG2   . VAL B 1 319 ? -4.092  -3.920  43.366  1.00 22.25 ? 339  VAL B CG2   1 
ATOM   8140  N  N     . HIS B 1 320 ? -1.942  -2.070  47.185  1.00 23.97 ? 340  HIS B N     1 
ATOM   8141  C  CA    . HIS B 1 320 ? -1.531  -1.974  48.582  1.00 24.65 ? 340  HIS B CA    1 
ATOM   8142  C  C     . HIS B 1 320 ? -2.718  -1.553  49.445  1.00 25.46 ? 340  HIS B C     1 
ATOM   8143  O  O     . HIS B 1 320 ? -3.549  -0.760  49.008  1.00 25.59 ? 340  HIS B O     1 
ATOM   8144  C  CB    . HIS B 1 320 ? -0.458  -0.890  48.739  1.00 24.79 ? 340  HIS B CB    1 
ATOM   8145  C  CG    . HIS B 1 320 ? 0.929   -1.331  48.395  1.00 24.51 ? 340  HIS B CG    1 
ATOM   8146  N  ND1   . HIS B 1 320 ? 1.325   -1.611  47.109  1.00 25.90 ? 340  HIS B ND1   1 
ATOM   8147  C  CD2   . HIS B 1 320 ? 2.024   -1.502  49.172  1.00 25.13 ? 340  HIS B CD2   1 
ATOM   8148  C  CE1   . HIS B 1 320 ? 2.602   -1.959  47.111  1.00 26.24 ? 340  HIS B CE1   1 
ATOM   8149  N  NE2   . HIS B 1 320 ? 3.050   -1.897  48.350  1.00 24.91 ? 340  HIS B NE2   1 
ATOM   8150  N  N     . PHE B 1 321 ? -2.783  -2.063  50.673  1.00 26.36 ? 341  PHE B N     1 
ATOM   8151  C  CA    . PHE B 1 321 ? -3.626  -1.460  51.705  1.00 27.41 ? 341  PHE B CA    1 
ATOM   8152  C  C     . PHE B 1 321 ? -2.804  -1.269  52.976  1.00 28.18 ? 341  PHE B C     1 
ATOM   8153  O  O     . PHE B 1 321 ? -2.170  -2.208  53.439  1.00 28.58 ? 341  PHE B O     1 
ATOM   8154  C  CB    . PHE B 1 321 ? -4.862  -2.309  52.002  1.00 27.29 ? 341  PHE B CB    1 
ATOM   8155  C  CG    . PHE B 1 321 ? -5.915  -1.586  52.799  1.00 27.81 ? 341  PHE B CG    1 
ATOM   8156  C  CD1   . PHE B 1 321 ? -7.060  -1.116  52.186  1.00 28.07 ? 341  PHE B CD1   1 
ATOM   8157  C  CD2   . PHE B 1 321 ? -5.756  -1.365  54.156  1.00 29.36 ? 341  PHE B CD2   1 
ATOM   8158  C  CE1   . PHE B 1 321 ? -8.040  -0.450  52.911  1.00 29.27 ? 341  PHE B CE1   1 
ATOM   8159  C  CE2   . PHE B 1 321 ? -6.734  -0.704  54.892  1.00 29.60 ? 341  PHE B CE2   1 
ATOM   8160  C  CZ    . PHE B 1 321 ? -7.880  -0.243  54.264  1.00 29.06 ? 341  PHE B CZ    1 
ATOM   8161  N  N     . GLY B 1 322 ? -2.821  -0.058  53.529  1.00 28.96 ? 342  GLY B N     1 
ATOM   8162  C  CA    . GLY B 1 322 ? -2.083  0.246   54.754  1.00 29.32 ? 342  GLY B CA    1 
ATOM   8163  C  C     . GLY B 1 322 ? -0.581  0.193   54.550  1.00 29.81 ? 342  GLY B C     1 
ATOM   8164  O  O     . GLY B 1 322 ? 0.164   -0.172  55.458  1.00 30.62 ? 342  GLY B O     1 
ATOM   8165  N  N     . GLY B 1 323 ? -0.136  0.552   53.351  1.00 30.00 ? 343  GLY B N     1 
ATOM   8166  C  CA    . GLY B 1 323 ? 1.281   0.512   53.004  1.00 29.82 ? 343  GLY B CA    1 
ATOM   8167  C  C     . GLY B 1 323 ? 1.830   -0.883  52.778  1.00 29.96 ? 343  GLY B C     1 
ATOM   8168  O  O     . GLY B 1 323 ? 3.042   -1.044  52.592  1.00 30.63 ? 343  GLY B O     1 
ATOM   8169  N  N     . GLU B 1 324 ? 0.962   -1.896  52.778  1.00 29.28 ? 344  GLU B N     1 
ATOM   8170  C  CA    . GLU B 1 324 ? 1.405   -3.268  52.547  1.00 28.81 ? 344  GLU B CA    1 
ATOM   8171  C  C     . GLU B 1 324 ? 0.794   -3.880  51.286  1.00 27.77 ? 344  GLU B C     1 
ATOM   8172  O  O     . GLU B 1 324 ? -0.393  -3.691  51.008  1.00 27.01 ? 344  GLU B O     1 
ATOM   8173  C  CB    . GLU B 1 324 ? 1.087   -4.119  53.756  1.00 29.15 ? 344  GLU B CB    1 
ATOM   8174  C  CG    . GLU B 1 324 ? 1.933   -3.733  54.956  1.00 30.65 ? 344  GLU B CG    1 
ATOM   8175  C  CD    . GLU B 1 324 ? 1.722   -4.662  56.094  1.00 31.02 ? 344  GLU B CD    1 
ATOM   8176  O  OE1   . GLU B 1 324 ? 0.647   -4.586  56.719  1.00 33.23 ? 344  GLU B OE1   1 
ATOM   8177  O  OE2   . GLU B 1 324 ? 2.615   -5.487  56.354  1.00 31.46 ? 344  GLU B OE2   1 
ATOM   8178  N  N     . ARG B 1 325 ? 1.620   -4.606  50.531  1.00 26.71 ? 345  ARG B N     1 
ATOM   8179  C  CA    . ARG B 1 325 ? 1.184   -5.180  49.267  1.00 26.00 ? 345  ARG B CA    1 
ATOM   8180  C  C     . ARG B 1 325 ? 0.205   -6.318  49.493  1.00 25.44 ? 345  ARG B C     1 
ATOM   8181  O  O     . ARG B 1 325 ? 0.390   -7.149  50.392  1.00 24.92 ? 345  ARG B O     1 
ATOM   8182  C  CB    . ARG B 1 325 ? 2.354   -5.677  48.412  1.00 25.99 ? 345  ARG B CB    1 
ATOM   8183  C  CG    . ARG B 1 325 ? 1.898   -6.104  47.002  1.00 25.82 ? 345  ARG B CG    1 
ATOM   8184  C  CD    . ARG B 1 325 ? 3.055   -6.381  46.061  1.00 25.99 ? 345  ARG B CD    1 
ATOM   8185  N  NE    . ARG B 1 325 ? 3.715   -5.135  45.672  1.00 26.93 ? 345  ARG B NE    1 
ATOM   8186  C  CZ    . ARG B 1 325 ? 4.966   -4.792  45.982  1.00 27.06 ? 345  ARG B CZ    1 
ATOM   8187  N  NH1   . ARG B 1 325 ? 5.747   -5.613  46.677  1.00 26.89 ? 345  ARG B NH1   1 
ATOM   8188  N  NH2   . ARG B 1 325 ? 5.441   -3.617  45.576  1.00 26.09 ? 345  ARG B NH2   1 
ATOM   8189  N  N     . ILE B 1 326 ? -0.838  -6.327  48.666  1.00 24.52 ? 346  ILE B N     1 
ATOM   8190  C  CA    . ILE B 1 326 ? -1.850  -7.376  48.668  1.00 24.51 ? 346  ILE B CA    1 
ATOM   8191  C  C     . ILE B 1 326 ? -1.822  -8.197  47.364  1.00 23.69 ? 346  ILE B C     1 
ATOM   8192  O  O     . ILE B 1 326 ? -1.851  -9.424  47.393  1.00 23.14 ? 346  ILE B O     1 
ATOM   8193  C  CB    . ILE B 1 326 ? -3.233  -6.741  48.857  1.00 24.88 ? 346  ILE B CB    1 
ATOM   8194  C  CG1   . ILE B 1 326 ? -3.317  -6.138  50.263  1.00 25.90 ? 346  ILE B CG1   1 
ATOM   8195  C  CG2   . ILE B 1 326 ? -4.330  -7.760  48.637  1.00 25.17 ? 346  ILE B CG2   1 
ATOM   8196  C  CD1   . ILE B 1 326 ? -4.513  -5.222  50.451  1.00 28.23 ? 346  ILE B CD1   1 
ATOM   8197  N  N     . ALA B 1 327 ? -1.769  -7.507  46.228  1.00 23.12 ? 347  ALA B N     1 
ATOM   8198  C  CA    . ALA B 1 327 ? -1.726  -8.155  44.919  1.00 22.74 ? 347  ALA B CA    1 
ATOM   8199  C  C     . ALA B 1 327 ? -0.844  -7.359  43.961  1.00 22.50 ? 347  ALA B C     1 
ATOM   8200  O  O     . ALA B 1 327 ? -0.988  -6.137  43.852  1.00 22.40 ? 347  ALA B O     1 
ATOM   8201  C  CB    . ALA B 1 327 ? -3.138  -8.288  44.343  1.00 22.63 ? 347  ALA B CB    1 
ATOM   8202  N  N     . TYR B 1 328 ? 0.059   -8.049  43.262  1.00 22.29 ? 348  TYR B N     1 
ATOM   8203  C  CA    . TYR B 1 328 ? 0.883   -7.401  42.232  1.00 22.07 ? 348  TYR B CA    1 
ATOM   8204  C  C     . TYR B 1 328 ? 0.066   -7.129  40.970  1.00 21.95 ? 348  TYR B C     1 
ATOM   8205  O  O     . TYR B 1 328 ? 0.269   -6.101  40.306  1.00 22.05 ? 348  TYR B O     1 
ATOM   8206  C  CB    . TYR B 1 328 ? 2.109   -8.261  41.880  1.00 22.04 ? 348  TYR B CB    1 
ATOM   8207  C  CG    . TYR B 1 328 ? 3.015   -7.648  40.826  1.00 22.12 ? 348  TYR B CG    1 
ATOM   8208  C  CD1   . TYR B 1 328 ? 3.921   -6.643  41.162  1.00 22.98 ? 348  TYR B CD1   1 
ATOM   8209  C  CD2   . TYR B 1 328 ? 2.974   -8.076  39.503  1.00 23.20 ? 348  TYR B CD2   1 
ATOM   8210  C  CE1   . TYR B 1 328 ? 4.759   -6.087  40.228  1.00 23.00 ? 348  TYR B CE1   1 
ATOM   8211  C  CE2   . TYR B 1 328 ? 3.812   -7.515  38.543  1.00 23.56 ? 348  TYR B CE2   1 
ATOM   8212  C  CZ    . TYR B 1 328 ? 4.704   -6.518  38.921  1.00 24.08 ? 348  TYR B CZ    1 
ATOM   8213  O  OH    . TYR B 1 328 ? 5.535   -5.951  38.003  1.00 24.24 ? 348  TYR B OH    1 
ATOM   8214  N  N     . GLU B 1 329 ? -0.851  -8.043  40.648  1.00 21.74 ? 349  GLU B N     1 
ATOM   8215  C  CA    . GLU B 1 329 ? -1.677  -7.938  39.440  1.00 21.58 ? 349  GLU B CA    1 
ATOM   8216  C  C     . GLU B 1 329 ? -3.043  -8.591  39.608  1.00 21.26 ? 349  GLU B C     1 
ATOM   8217  O  O     . GLU B 1 329 ? -3.133  -9.724  40.074  1.00 20.52 ? 349  GLU B O     1 
ATOM   8218  C  CB    . GLU B 1 329 ? -0.983  -8.612  38.254  1.00 21.55 ? 349  GLU B CB    1 
ATOM   8219  C  CG    . GLU B 1 329 ? -1.822  -8.627  36.991  1.00 22.66 ? 349  GLU B CG    1 
ATOM   8220  C  CD    . GLU B 1 329 ? -1.183  -9.383  35.840  1.00 24.71 ? 349  GLU B CD    1 
ATOM   8221  O  OE1   . GLU B 1 329 ? -0.069  -9.931  36.021  1.00 25.46 ? 349  GLU B OE1   1 
ATOM   8222  O  OE2   . GLU B 1 329 ? -1.820  -9.441  34.761  1.00 23.46 ? 349  GLU B OE2   1 
ATOM   8223  N  N     . VAL B 1 330 ? -4.092  -7.858  39.224  1.00 21.18 ? 350  VAL B N     1 
ATOM   8224  C  CA    . VAL B 1 330 ? -5.422  -8.428  39.025  1.00 21.07 ? 350  VAL B CA    1 
ATOM   8225  C  C     . VAL B 1 330 ? -5.896  -7.990  37.647  1.00 20.78 ? 350  VAL B C     1 
ATOM   8226  O  O     . VAL B 1 330 ? -6.036  -6.794  37.382  1.00 20.50 ? 350  VAL B O     1 
ATOM   8227  C  CB    . VAL B 1 330 ? -6.428  -8.000  40.114  1.00 21.36 ? 350  VAL B CB    1 
ATOM   8228  C  CG1   . VAL B 1 330 ? -7.696  -8.854  40.030  1.00 20.30 ? 350  VAL B CG1   1 
ATOM   8229  C  CG2   . VAL B 1 330 ? -5.808  -8.133  41.497  1.00 21.31 ? 350  VAL B CG2   1 
ATOM   8230  N  N     . SER B 1 331 ? -6.123  -8.961  36.762  1.00 20.80 ? 351  SER B N     1 
ATOM   8231  C  CA    . SER B 1 331 ? -6.396  -8.668  35.354  1.00 20.56 ? 351  SER B CA    1 
ATOM   8232  C  C     . SER B 1 331 ? -7.388  -9.612  34.688  1.00 20.19 ? 351  SER B C     1 
ATOM   8233  O  O     . SER B 1 331 ? -7.373  -10.824 34.925  1.00 19.89 ? 351  SER B O     1 
ATOM   8234  C  CB    . SER B 1 331 ? -5.091  -8.712  34.553  1.00 20.99 ? 351  SER B CB    1 
ATOM   8235  O  OG    . SER B 1 331 ? -4.404  -9.931  34.748  1.00 20.92 ? 351  SER B OG    1 
ATOM   8236  N  N     . VAL B 1 332 ? -8.215  -9.036  33.819  1.00 19.92 ? 352  VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? -9.025  -9.801  32.889  1.00 19.97 ? 352  VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? -8.109  -10.464 31.874  1.00 19.91 ? 352  VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? -7.260  -9.801  31.282  1.00 19.99 ? 352  VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? -10.023 -8.897  32.128  1.00 20.33 ? 352  VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? -10.884 -9.744  31.184  1.00 19.91 ? 352  VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? -10.901 -8.085  33.116  1.00 20.16 ? 352  VAL B CG2   1 
ATOM   8243  N  N     . GLN B 1 333 ? -8.293  -11.763 31.665  1.00 20.11 ? 353  GLN B N     1 
ATOM   8244  C  CA    . GLN B 1 333 ? -7.465  -12.541 30.736  1.00 20.32 ? 353  GLN B CA    1 
ATOM   8245  C  C     . GLN B 1 333 ? -8.180  -12.971 29.459  1.00 20.41 ? 353  GLN B C     1 
ATOM   8246  O  O     . GLN B 1 333 ? -7.551  -13.075 28.408  1.00 19.84 ? 353  GLN B O     1 
ATOM   8247  C  CB    . GLN B 1 333 ? -6.948  -13.788 31.441  1.00 20.43 ? 353  GLN B CB    1 
ATOM   8248  C  CG    . GLN B 1 333 ? -6.002  -13.479 32.591  1.00 21.87 ? 353  GLN B CG    1 
ATOM   8249  C  CD    . GLN B 1 333 ? -4.670  -12.936 32.109  1.00 22.20 ? 353  GLN B CD    1 
ATOM   8250  O  OE1   . GLN B 1 333 ? -4.050  -13.513 31.223  1.00 23.62 ? 353  GLN B OE1   1 
ATOM   8251  N  NE2   . GLN B 1 333 ? -4.222  -11.835 32.696  1.00 22.88 ? 353  GLN B NE2   1 
ATOM   8252  N  N     . GLU B 1 334 ? -9.475  -13.269 29.561  1.00 20.34 ? 354  GLU B N     1 
ATOM   8253  C  CA    . GLU B 1 334 ? -10.266 -13.699 28.407  1.00 20.53 ? 354  GLU B CA    1 
ATOM   8254  C  C     . GLU B 1 334 ? -11.737 -13.729 28.818  1.00 20.48 ? 354  GLU B C     1 
ATOM   8255  O  O     . GLU B 1 334 ? -12.060 -13.860 30.003  1.00 20.22 ? 354  GLU B O     1 
ATOM   8256  C  CB    . GLU B 1 334 ? -9.798  -15.081 27.924  1.00 20.95 ? 354  GLU B CB    1 
ATOM   8257  C  CG    . GLU B 1 334 ? -10.493 -15.680 26.686  1.00 21.52 ? 354  GLU B CG    1 
ATOM   8258  C  CD    . GLU B 1 334 ? -10.345 -14.845 25.417  1.00 22.51 ? 354  GLU B CD    1 
ATOM   8259  O  OE1   . GLU B 1 334 ? -9.466  -15.160 24.574  1.00 22.15 ? 354  GLU B OE1   1 
ATOM   8260  O  OE2   . GLU B 1 334 ? -11.112 -13.874 25.266  1.00 22.00 ? 354  GLU B OE2   1 
ATOM   8261  N  N     . ALA B 1 335 ? -12.611 -13.586 27.831  1.00 20.22 ? 355  ALA B N     1 
ATOM   8262  C  CA    . ALA B 1 335 ? -14.052 -13.584 28.043  1.00 20.25 ? 355  ALA B CA    1 
ATOM   8263  C  C     . ALA B 1 335 ? -14.652 -14.262 26.834  1.00 20.19 ? 355  ALA B C     1 
ATOM   8264  O  O     . ALA B 1 335 ? -14.382 -13.854 25.701  1.00 19.80 ? 355  ALA B O     1 
ATOM   8265  C  CB    . ALA B 1 335 ? -14.577 -12.166 28.169  1.00 20.14 ? 355  ALA B CB    1 
ATOM   8266  N  N     . VAL B 1 336 ? -15.447 -15.303 27.074  1.00 19.76 ? 356  VAL B N     1 
ATOM   8267  C  CA    . VAL B 1 336 ? -15.940 -16.144 26.005  1.00 19.30 ? 356  VAL B CA    1 
ATOM   8268  C  C     . VAL B 1 336 ? -17.448 -16.309 26.102  1.00 18.98 ? 356  VAL B C     1 
ATOM   8269  O  O     . VAL B 1 336 ? -18.032 -16.161 27.178  1.00 18.62 ? 356  VAL B O     1 
ATOM   8270  C  CB    . VAL B 1 336 ? -15.225 -17.535 25.979  1.00 19.60 ? 356  VAL B CB    1 
ATOM   8271  C  CG1   . VAL B 1 336 ? -13.672 -17.366 26.003  1.00 19.24 ? 356  VAL B CG1   1 
ATOM   8272  C  CG2   . VAL B 1 336 ? -15.680 -18.417 27.142  1.00 19.82 ? 356  VAL B CG2   1 
ATOM   8273  N  N     . ALA B 1 337 ? -18.061 -16.569 24.950  1.00 18.46 ? 357  ALA B N     1 
ATOM   8274  C  CA    . ALA B 1 337 ? -19.470 -16.915 24.851  1.00 18.57 ? 357  ALA B CA    1 
ATOM   8275  C  C     . ALA B 1 337 ? -19.570 -18.127 23.921  1.00 18.73 ? 357  ALA B C     1 
ATOM   8276  O  O     . ALA B 1 337 ? -19.237 -18.053 22.730  1.00 18.79 ? 357  ALA B O     1 
ATOM   8277  C  CB    . ALA B 1 337 ? -20.289 -15.736 24.335  1.00 18.64 ? 357  ALA B CB    1 
ATOM   8278  N  N     . LEU B 1 338 ? -19.975 -19.252 24.501  1.00 18.76 ? 358  LEU B N     1 
ATOM   8279  C  CA    . LEU B 1 338 ? -19.960 -20.542 23.847  1.00 18.85 ? 358  LEU B CA    1 
ATOM   8280  C  C     . LEU B 1 338 ? -21.399 -20.958 23.532  1.00 19.12 ? 358  LEU B C     1 
ATOM   8281  O  O     . LEU B 1 338 ? -22.194 -21.225 24.444  1.00 18.83 ? 358  LEU B O     1 
ATOM   8282  C  CB    . LEU B 1 338 ? -19.303 -21.566 24.770  1.00 19.02 ? 358  LEU B CB    1 
ATOM   8283  C  CG    . LEU B 1 338 ? -17.924 -21.159 25.311  1.00 20.06 ? 358  LEU B CG    1 
ATOM   8284  C  CD1   . LEU B 1 338 ? -17.386 -22.195 26.293  1.00 19.48 ? 358  LEU B CD1   1 
ATOM   8285  C  CD2   . LEU B 1 338 ? -16.938 -20.930 24.156  1.00 19.30 ? 358  LEU B CD2   1 
ATOM   8286  N  N     . TYR B 1 339 ? -21.714 -21.024 22.240  1.00 18.97 ? 359  TYR B N     1 
ATOM   8287  C  CA    . TYR B 1 339 ? -23.087 -21.210 21.779  1.00 18.96 ? 359  TYR B CA    1 
ATOM   8288  C  C     . TYR B 1 339 ? -23.416 -22.613 21.306  1.00 19.00 ? 359  TYR B C     1 
ATOM   8289  O  O     . TYR B 1 339 ? -22.532 -23.389 20.950  1.00 19.09 ? 359  TYR B O     1 
ATOM   8290  C  CB    . TYR B 1 339 ? -23.387 -20.228 20.644  1.00 18.84 ? 359  TYR B CB    1 
ATOM   8291  C  CG    . TYR B 1 339 ? -23.415 -18.809 21.138  1.00 18.46 ? 359  TYR B CG    1 
ATOM   8292  C  CD1   . TYR B 1 339 ? -24.618 -18.192 21.449  1.00 18.00 ? 359  TYR B CD1   1 
ATOM   8293  C  CD2   . TYR B 1 339 ? -22.236 -18.100 21.336  1.00 16.85 ? 359  TYR B CD2   1 
ATOM   8294  C  CE1   . TYR B 1 339 ? -24.651 -16.900 21.926  1.00 18.13 ? 359  TYR B CE1   1 
ATOM   8295  C  CE2   . TYR B 1 339 ? -22.256 -16.815 21.806  1.00 17.44 ? 359  TYR B CE2   1 
ATOM   8296  C  CZ    . TYR B 1 339 ? -23.468 -16.210 22.110  1.00 18.55 ? 359  TYR B CZ    1 
ATOM   8297  O  OH    . TYR B 1 339 ? -23.513 -14.914 22.600  1.00 18.57 ? 359  TYR B OH    1 
ATOM   8298  N  N     . GLY B 1 340 ? -24.710 -22.919 21.345  1.00 18.67 ? 360  GLY B N     1 
ATOM   8299  C  CA    . GLY B 1 340 ? -25.291 -24.024 20.602  1.00 19.07 ? 360  GLY B CA    1 
ATOM   8300  C  C     . GLY B 1 340 ? -26.296 -23.441 19.619  1.00 19.37 ? 360  GLY B C     1 
ATOM   8301  O  O     . GLY B 1 340 ? -26.742 -22.296 19.781  1.00 19.59 ? 360  GLY B O     1 
ATOM   8302  N  N     . GLY B 1 341 ? -26.649 -24.207 18.595  1.00 19.73 ? 361  GLY B N     1 
ATOM   8303  C  CA    . GLY B 1 341 ? -27.612 -23.729 17.611  1.00 20.05 ? 361  GLY B CA    1 
ATOM   8304  C  C     . GLY B 1 341 ? -28.125 -24.758 16.630  1.00 20.27 ? 361  GLY B C     1 
ATOM   8305  O  O     . GLY B 1 341 ? -27.512 -25.797 16.417  1.00 20.04 ? 361  GLY B O     1 
ATOM   8306  N  N     . HIS B 1 342 ? -29.268 -24.430 16.032  1.00 20.69 ? 362  HIS B N     1 
ATOM   8307  C  CA    . HIS B 1 342 ? -29.862 -25.189 14.943  1.00 21.27 ? 362  HIS B CA    1 
ATOM   8308  C  C     . HIS B 1 342 ? -29.310 -24.769 13.584  1.00 21.27 ? 362  HIS B C     1 
ATOM   8309  O  O     . HIS B 1 342 ? -29.286 -25.578 12.656  1.00 21.87 ? 362  HIS B O     1 
ATOM   8310  C  CB    . HIS B 1 342 ? -31.395 -25.028 14.934  1.00 21.52 ? 362  HIS B CB    1 
ATOM   8311  C  CG    . HIS B 1 342 ? -31.872 -23.614 14.765  1.00 23.34 ? 362  HIS B CG    1 
ATOM   8312  N  ND1   . HIS B 1 342 ? -31.503 -22.588 15.614  1.00 26.31 ? 362  HIS B ND1   1 
ATOM   8313  C  CD2   . HIS B 1 342 ? -32.731 -23.067 13.871  1.00 26.08 ? 362  HIS B CD2   1 
ATOM   8314  C  CE1   . HIS B 1 342 ? -32.092 -21.467 15.231  1.00 26.69 ? 362  HIS B CE1   1 
ATOM   8315  N  NE2   . HIS B 1 342 ? -32.859 -21.735 14.187  1.00 25.86 ? 362  HIS B NE2   1 
ATOM   8316  N  N     . THR B 1 343 ? -28.904 -23.510 13.446  1.00 20.96 ? 363  THR B N     1 
ATOM   8317  C  CA    . THR B 1 343 ? -28.330 -23.031 12.187  1.00 20.92 ? 363  THR B CA    1 
ATOM   8318  C  C     . THR B 1 343 ? -26.814 -23.238 12.226  1.00 20.68 ? 363  THR B C     1 
ATOM   8319  O  O     . THR B 1 343 ? -26.224 -23.297 13.300  1.00 21.08 ? 363  THR B O     1 
ATOM   8320  C  CB    . THR B 1 343 ? -28.656 -21.527 11.915  1.00 20.99 ? 363  THR B CB    1 
ATOM   8321  O  OG1   . THR B 1 343 ? -27.745 -20.693 12.639  1.00 21.00 ? 363  THR B OG1   1 
ATOM   8322  C  CG2   . THR B 1 343 ? -30.110 -21.173 12.310  1.00 21.52 ? 363  THR B CG2   1 
ATOM   8323  N  N     . PRO B 1 344 ? -26.175 -23.370 11.059  1.00 20.61 ? 364  PRO B N     1 
ATOM   8324  C  CA    . PRO B 1 344 ? -24.722 -23.588 11.075  1.00 20.67 ? 364  PRO B CA    1 
ATOM   8325  C  C     . PRO B 1 344 ? -23.905 -22.468 11.746  1.00 20.43 ? 364  PRO B C     1 
ATOM   8326  O  O     . PRO B 1 344 ? -22.915 -22.758 12.405  1.00 20.40 ? 364  PRO B O     1 
ATOM   8327  C  CB    . PRO B 1 344 ? -24.354 -23.745 9.600   1.00 20.65 ? 364  PRO B CB    1 
ATOM   8328  C  CG    . PRO B 1 344 ? -25.568 -23.316 8.820   1.00 21.70 ? 364  PRO B CG    1 
ATOM   8329  C  CD    . PRO B 1 344 ? -26.753 -23.485 9.709   1.00 20.68 ? 364  PRO B CD    1 
ATOM   8330  N  N     . ALA B 1 345 ? -24.315 -21.213 11.597  1.00 20.33 ? 365  ALA B N     1 
ATOM   8331  C  CA    . ALA B 1 345 ? -23.652 -20.106 12.294  1.00 20.15 ? 365  ALA B CA    1 
ATOM   8332  C  C     . ALA B 1 345 ? -23.748 -20.301 13.802  1.00 20.40 ? 365  ALA B C     1 
ATOM   8333  O  O     . ALA B 1 345 ? -22.764 -20.162 14.510  1.00 20.25 ? 365  ALA B O     1 
ATOM   8334  C  CB    . ALA B 1 345 ? -24.255 -18.787 11.895  1.00 19.86 ? 365  ALA B CB    1 
ATOM   8335  N  N     . GLY B 1 346 ? -24.946 -20.638 14.273  1.00 20.86 ? 366  GLY B N     1 
ATOM   8336  C  CA    . GLY B 1 346 ? -25.202 -20.866 15.686  1.00 20.96 ? 366  GLY B CA    1 
ATOM   8337  C  C     . GLY B 1 346 ? -24.366 -21.971 16.289  1.00 20.98 ? 366  GLY B C     1 
ATOM   8338  O  O     . GLY B 1 346 ? -23.735 -21.783 17.331  1.00 21.21 ? 366  GLY B O     1 
ATOM   8339  N  N     . MET B 1 347 ? -24.344 -23.128 15.640  1.00 20.81 ? 367  MET B N     1 
ATOM   8340  C  CA    . MET B 1 347 ? -23.555 -24.238 16.162  1.00 20.96 ? 367  MET B CA    1 
ATOM   8341  C  C     . MET B 1 347 ? -22.035 -24.018 15.996  1.00 20.54 ? 367  MET B C     1 
ATOM   8342  O  O     . MET B 1 347 ? -21.246 -24.670 16.675  1.00 19.36 ? 367  MET B O     1 
ATOM   8343  C  CB    . MET B 1 347 ? -24.018 -25.590 15.585  1.00 21.37 ? 367  MET B CB    1 
ATOM   8344  C  CG    . MET B 1 347 ? -23.821 -25.773 14.103  1.00 22.51 ? 367  MET B CG    1 
ATOM   8345  S  SD    . MET B 1 347 ? -24.441 -27.370 13.541  1.00 23.70 ? 367  MET B SD    1 
ATOM   8346  C  CE    . MET B 1 347 ? -26.222 -27.155 13.567  1.00 20.49 ? 367  MET B CE    1 
ATOM   8347  N  N     . GLN B 1 348 ? -21.642 -23.058 15.155  1.00 20.45 ? 368  GLN B N     1 
ATOM   8348  C  CA    . GLN B 1 348 ? -20.229 -22.718 14.966  1.00 20.46 ? 368  GLN B CA    1 
ATOM   8349  C  C     . GLN B 1 348 ? -19.657 -21.795 16.050  1.00 20.80 ? 368  GLN B C     1 
ATOM   8350  O  O     . GLN B 1 348 ? -18.450 -21.829 16.317  1.00 21.64 ? 368  GLN B O     1 
ATOM   8351  C  CB    . GLN B 1 348 ? -20.035 -22.067 13.600  1.00 20.17 ? 368  GLN B CB    1 
ATOM   8352  C  CG    . GLN B 1 348 ? -18.579 -21.859 13.182  1.00 20.24 ? 368  GLN B CG    1 
ATOM   8353  C  CD    . GLN B 1 348 ? -17.828 -23.156 12.973  1.00 19.31 ? 368  GLN B CD    1 
ATOM   8354  O  OE1   . GLN B 1 348 ? -18.421 -24.197 12.713  1.00 20.08 ? 368  GLN B OE1   1 
ATOM   8355  N  NE2   . GLN B 1 348 ? -16.517 -23.096 13.087  1.00 20.55 ? 368  GLN B NE2   1 
ATOM   8356  N  N     . THR B 1 349 ? -20.513 -20.992 16.681  1.00 20.80 ? 369  THR B N     1 
ATOM   8357  C  CA    . THR B 1 349 ? -20.058 -19.830 17.450  1.00 20.38 ? 369  THR B CA    1 
ATOM   8358  C  C     . THR B 1 349 ? -19.453 -20.154 18.811  1.00 20.56 ? 369  THR B C     1 
ATOM   8359  O  O     . THR B 1 349 ? -20.140 -20.603 19.745  1.00 19.94 ? 369  THR B O     1 
ATOM   8360  C  CB    . THR B 1 349 ? -21.189 -18.801 17.669  1.00 20.49 ? 369  THR B CB    1 
ATOM   8361  O  OG1   . THR B 1 349 ? -21.846 -18.516 16.428  1.00 20.19 ? 369  THR B OG1   1 
ATOM   8362  C  CG2   . THR B 1 349 ? -20.631 -17.518 18.246  1.00 18.98 ? 369  THR B CG2   1 
ATOM   8363  N  N     . LYS B 1 350 ? -18.151 -19.913 18.911  1.00 20.83 ? 370  LYS B N     1 
ATOM   8364  C  CA    . LYS B 1 350 ? -17.466 -19.859 20.187  1.00 21.19 ? 370  LYS B CA    1 
ATOM   8365  C  C     . LYS B 1 350 ? -16.638 -18.582 20.154  1.00 21.55 ? 370  LYS B C     1 
ATOM   8366  O  O     . LYS B 1 350 ? -15.521 -18.569 19.614  1.00 21.73 ? 370  LYS B O     1 
ATOM   8367  C  CB    . LYS B 1 350 ? -16.573 -21.078 20.386  1.00 21.33 ? 370  LYS B CB    1 
ATOM   8368  C  CG    . LYS B 1 350 ? -17.326 -22.375 20.455  1.00 22.26 ? 370  LYS B CG    1 
ATOM   8369  C  CD    . LYS B 1 350 ? -16.402 -23.544 20.698  1.00 23.71 ? 370  LYS B CD    1 
ATOM   8370  C  CE    . LYS B 1 350 ? -17.161 -24.862 20.627  1.00 24.21 ? 370  LYS B CE    1 
ATOM   8371  N  NZ    . LYS B 1 350 ? -17.630 -25.142 19.235  1.00 25.22 ? 370  LYS B NZ    1 
ATOM   8372  N  N     . TYR B 1 351 ? -17.202 -17.502 20.686  1.00 21.14 ? 371  TYR B N     1 
ATOM   8373  C  CA    . TYR B 1 351 ? -16.536 -16.217 20.629  1.00 21.44 ? 371  TYR B CA    1 
ATOM   8374  C  C     . TYR B 1 351 ? -15.536 -16.136 21.774  1.00 21.65 ? 371  TYR B C     1 
ATOM   8375  O  O     . TYR B 1 351 ? -15.862 -16.465 22.917  1.00 21.65 ? 371  TYR B O     1 
ATOM   8376  C  CB    . TYR B 1 351 ? -17.521 -15.048 20.750  1.00 21.53 ? 371  TYR B CB    1 
ATOM   8377  C  CG    . TYR B 1 351 ? -18.286 -14.674 19.497  1.00 21.62 ? 371  TYR B CG    1 
ATOM   8378  C  CD1   . TYR B 1 351 ? -17.630 -14.401 18.290  1.00 21.86 ? 371  TYR B CD1   1 
ATOM   8379  C  CD2   . TYR B 1 351 ? -19.672 -14.534 19.530  1.00 19.72 ? 371  TYR B CD2   1 
ATOM   8380  C  CE1   . TYR B 1 351 ? -18.355 -14.025 17.152  1.00 20.10 ? 371  TYR B CE1   1 
ATOM   8381  C  CE2   . TYR B 1 351 ? -20.390 -14.166 18.409  1.00 19.80 ? 371  TYR B CE2   1 
ATOM   8382  C  CZ    . TYR B 1 351 ? -19.736 -13.917 17.221  1.00 20.18 ? 371  TYR B CZ    1 
ATOM   8383  O  OH    . TYR B 1 351 ? -20.478 -13.541 16.103  1.00 20.88 ? 371  TYR B OH    1 
ATOM   8384  N  N     . LEU B 1 352 ? -14.327 -15.701 21.448  1.00 21.71 ? 372  LEU B N     1 
ATOM   8385  C  CA    . LEU B 1 352 ? -13.265 -15.463 22.419  1.00 22.14 ? 372  LEU B CA    1 
ATOM   8386  C  C     . LEU B 1 352 ? -12.837 -14.016 22.182  1.00 22.30 ? 372  LEU B C     1 
ATOM   8387  O  O     . LEU B 1 352 ? -12.180 -13.709 21.187  1.00 21.56 ? 372  LEU B O     1 
ATOM   8388  C  CB    . LEU B 1 352 ? -12.087 -16.418 22.192  1.00 22.40 ? 372  LEU B CB    1 
ATOM   8389  C  CG    . LEU B 1 352 ? -12.206 -17.846 22.728  1.00 22.80 ? 372  LEU B CG    1 
ATOM   8390  C  CD1   . LEU B 1 352 ? -13.472 -18.539 22.242  1.00 24.14 ? 372  LEU B CD1   1 
ATOM   8391  C  CD2   . LEU B 1 352 ? -10.986 -18.663 22.342  1.00 24.04 ? 372  LEU B CD2   1 
ATOM   8392  N  N     . ASP B 1 353 ? -13.223 -13.134 23.096  1.00 22.79 ? 373  ASP B N     1 
ATOM   8393  C  CA    . ASP B 1 353 ? -13.203 -11.703 22.829  1.00 23.42 ? 373  ASP B CA    1 
ATOM   8394  C  C     . ASP B 1 353 ? -11.833 -11.048 22.884  1.00 23.07 ? 373  ASP B C     1 
ATOM   8395  O  O     . ASP B 1 353 ? -11.673 -9.942  22.381  1.00 23.03 ? 373  ASP B O     1 
ATOM   8396  C  CB    . ASP B 1 353 ? -14.186 -10.988 23.760  1.00 23.98 ? 373  ASP B CB    1 
ATOM   8397  C  CG    . ASP B 1 353 ? -15.621 -11.390 23.489  1.00 25.99 ? 373  ASP B CG    1 
ATOM   8398  O  OD1   . ASP B 1 353 ? -15.961 -11.738 22.326  1.00 29.47 ? 373  ASP B OD1   1 
ATOM   8399  O  OD2   . ASP B 1 353 ? -16.416 -11.378 24.439  1.00 30.50 ? 373  ASP B OD2   1 
ATOM   8400  N  N     . VAL B 1 354 ? -10.838 -11.703 23.476  1.00 22.79 ? 374  VAL B N     1 
ATOM   8401  C  CA    . VAL B 1 354 ? -9.482  -11.175 23.379  1.00 22.50 ? 374  VAL B CA    1 
ATOM   8402  C  C     . VAL B 1 354 ? -9.047  -11.233 21.910  1.00 22.68 ? 374  VAL B C     1 
ATOM   8403  O  O     . VAL B 1 354 ? -8.306  -10.368 21.451  1.00 23.04 ? 374  VAL B O     1 
ATOM   8404  C  CB    . VAL B 1 354 ? -8.491  -11.900 24.306  1.00 22.56 ? 374  VAL B CB    1 
ATOM   8405  C  CG1   . VAL B 1 354 ? -7.030  -11.519 23.973  1.00 22.04 ? 374  VAL B CG1   1 
ATOM   8406  C  CG2   . VAL B 1 354 ? -8.811  -11.565 25.754  1.00 21.89 ? 374  VAL B CG2   1 
ATOM   8407  N  N     . GLY B 1 355 ? -9.566  -12.208 21.160  1.00 22.52 ? 375  GLY B N     1 
ATOM   8408  C  CA    . GLY B 1 355 ? -9.357  -12.256 19.715  1.00 22.70 ? 375  GLY B CA    1 
ATOM   8409  C  C     . GLY B 1 355 ? -9.945  -11.087 18.935  1.00 22.96 ? 375  GLY B C     1 
ATOM   8410  O  O     . GLY B 1 355 ? -9.768  -11.017 17.723  1.00 22.91 ? 375  GLY B O     1 
ATOM   8411  N  N     . TRP B 1 356 ? -10.635 -10.175 19.630  1.00 23.28 ? 376  TRP B N     1 
ATOM   8412  C  CA    . TRP B 1 356 ? -11.261 -8.985  19.034  1.00 23.51 ? 376  TRP B CA    1 
ATOM   8413  C  C     . TRP B 1 356 ? -10.790 -7.678  19.684  1.00 23.75 ? 376  TRP B C     1 
ATOM   8414  O  O     . TRP B 1 356 ? -11.428 -6.645  19.518  1.00 24.60 ? 376  TRP B O     1 
ATOM   8415  C  CB    . TRP B 1 356 ? -12.793 -9.085  19.173  1.00 23.39 ? 376  TRP B CB    1 
ATOM   8416  C  CG    . TRP B 1 356 ? -13.349 -10.285 18.486  1.00 23.00 ? 376  TRP B CG    1 
ATOM   8417  C  CD1   . TRP B 1 356 ? -13.397 -11.545 18.965  1.00 21.71 ? 376  TRP B CD1   1 
ATOM   8418  C  CD2   . TRP B 1 356 ? -13.916 -10.329 17.170  1.00 22.67 ? 376  TRP B CD2   1 
ATOM   8419  N  NE1   . TRP B 1 356 ? -13.969 -12.389 18.037  1.00 23.22 ? 376  TRP B NE1   1 
ATOM   8420  C  CE2   . TRP B 1 356 ? -14.293 -11.663 16.923  1.00 22.06 ? 376  TRP B CE2   1 
ATOM   8421  C  CE3   . TRP B 1 356 ? -14.139 -9.367  16.179  1.00 22.45 ? 376  TRP B CE3   1 
ATOM   8422  C  CZ2   . TRP B 1 356 ? -14.879 -12.066 15.722  1.00 22.65 ? 376  TRP B CZ2   1 
ATOM   8423  C  CZ3   . TRP B 1 356 ? -14.713 -9.766  14.982  1.00 22.45 ? 376  TRP B CZ3   1 
ATOM   8424  C  CH2   . TRP B 1 356 ? -15.078 -11.106 14.763  1.00 22.09 ? 376  TRP B CH2   1 
ATOM   8425  N  N     . GLY B 1 357 ? -9.684  -7.709  20.420  1.00 23.73 ? 377  GLY B N     1 
ATOM   8426  C  CA    . GLY B 1 357 ? -9.224  -6.517  21.150  1.00 23.60 ? 377  GLY B CA    1 
ATOM   8427  C  C     . GLY B 1 357 ? -10.198 -6.089  22.234  1.00 23.36 ? 377  GLY B C     1 
ATOM   8428  O  O     . GLY B 1 357 ? -10.760 -5.007  22.184  1.00 23.72 ? 377  GLY B O     1 
ATOM   8429  N  N     . LEU B 1 358 ? -10.401 -6.961  23.214  1.00 23.41 ? 378  LEU B N     1 
ATOM   8430  C  CA    . LEU B 1 358 ? -11.330 -6.718  24.312  1.00 23.11 ? 378  LEU B CA    1 
ATOM   8431  C  C     . LEU B 1 358 ? -11.046 -5.368  24.984  1.00 22.69 ? 378  LEU B C     1 
ATOM   8432  O  O     . LEU B 1 358 ? -11.965 -4.614  25.314  1.00 22.20 ? 378  LEU B O     1 
ATOM   8433  C  CB    . LEU B 1 358 ? -11.212 -7.867  25.323  1.00 23.45 ? 378  LEU B CB    1 
ATOM   8434  C  CG    . LEU B 1 358 ? -12.231 -7.965  26.453  1.00 24.02 ? 378  LEU B CG    1 
ATOM   8435  C  CD1   . LEU B 1 358 ? -13.652 -7.990  25.901  1.00 25.92 ? 378  LEU B CD1   1 
ATOM   8436  C  CD2   . LEU B 1 358 ? -11.961 -9.220  27.254  1.00 23.89 ? 378  LEU B CD2   1 
ATOM   8437  N  N     . GLY B 1 359 ? -9.763  -5.053  25.130  1.00 22.57 ? 379  GLY B N     1 
ATOM   8438  C  CA    . GLY B 1 359 ? -9.326  -3.835  25.795  1.00 22.33 ? 379  GLY B CA    1 
ATOM   8439  C  C     . GLY B 1 359 ? -9.309  -2.570  24.961  1.00 22.27 ? 379  GLY B C     1 
ATOM   8440  O  O     . GLY B 1 359 ? -8.973  -1.514  25.481  1.00 22.10 ? 379  GLY B O     1 
ATOM   8441  N  N     . SER B 1 360 ? -9.670  -2.645  23.679  1.00 22.21 ? 380  SER B N     1 
ATOM   8442  C  CA    . SER B 1 360 ? -9.668  -1.443  22.841  1.00 22.16 ? 380  SER B CA    1 
ATOM   8443  C  C     . SER B 1 360 ? -11.029 -1.109  22.218  1.00 22.16 ? 380  SER B C     1 
ATOM   8444  O  O     . SER B 1 360 ? -11.113 -0.299  21.294  1.00 22.53 ? 380  SER B O     1 
ATOM   8445  C  CB    . SER B 1 360 ? -8.575  -1.539  21.765  1.00 22.32 ? 380  SER B CB    1 
ATOM   8446  O  OG    . SER B 1 360 ? -8.745  -2.662  20.935  1.00 22.59 ? 380  SER B OG    1 
ATOM   8447  N  N     . VAL B 1 361 ? -12.087 -1.722  22.742  1.00 21.53 ? 381  VAL B N     1 
ATOM   8448  C  CA    . VAL B 1 361 ? -13.447 -1.393  22.369  1.00 21.15 ? 381  VAL B CA    1 
ATOM   8449  C  C     . VAL B 1 361 ? -14.103 -0.723  23.581  1.00 21.44 ? 381  VAL B C     1 
ATOM   8450  O  O     . VAL B 1 361 ? -15.299 -0.896  23.869  1.00 21.48 ? 381  VAL B O     1 
ATOM   8451  C  CB    . VAL B 1 361 ? -14.234 -2.628  21.870  1.00 21.49 ? 381  VAL B CB    1 
ATOM   8452  C  CG1   . VAL B 1 361 ? -13.885 -2.922  20.390  1.00 20.79 ? 381  VAL B CG1   1 
ATOM   8453  C  CG2   . VAL B 1 361 ? -14.000 -3.848  22.752  1.00 20.44 ? 381  VAL B CG2   1 
ATOM   8454  N  N     . THR B 1 362 ? -13.282 0.079   24.256  1.00 21.24 ? 382  THR B N     1 
ATOM   8455  C  CA    . THR B 1 362 ? -13.633 0.780   25.471  1.00 21.14 ? 382  THR B CA    1 
ATOM   8456  C  C     . THR B 1 362 ? -14.274 2.103   25.076  1.00 21.23 ? 382  THR B C     1 
ATOM   8457  O  O     . THR B 1 362 ? -13.657 3.161   25.184  1.00 21.29 ? 382  THR B O     1 
ATOM   8458  C  CB    . THR B 1 362 ? -12.365 1.043   26.302  1.00 21.36 ? 382  THR B CB    1 
ATOM   8459  O  OG1   . THR B 1 362 ? -11.400 1.729   25.493  1.00 20.94 ? 382  THR B OG1   1 
ATOM   8460  C  CG2   . THR B 1 362 ? -11.756 -0.264  26.785  1.00 20.94 ? 382  THR B CG2   1 
ATOM   8461  N  N     . HIS B 1 363 ? -15.511 2.034   24.590  1.00 21.10 ? 383  HIS B N     1 
ATOM   8462  C  CA    . HIS B 1 363 ? -16.138 3.191   23.970  1.00 20.90 ? 383  HIS B CA    1 
ATOM   8463  C  C     . HIS B 1 363 ? -16.754 4.118   25.009  1.00 20.74 ? 383  HIS B C     1 
ATOM   8464  O  O     . HIS B 1 363 ? -16.858 3.771   26.194  1.00 20.68 ? 383  HIS B O     1 
ATOM   8465  C  CB    . HIS B 1 363 ? -17.121 2.758   22.871  1.00 21.08 ? 383  HIS B CB    1 
ATOM   8466  C  CG    . HIS B 1 363 ? -16.435 2.382   21.595  1.00 21.99 ? 383  HIS B CG    1 
ATOM   8467  N  ND1   . HIS B 1 363 ? -15.796 3.307   20.797  1.00 23.97 ? 383  HIS B ND1   1 
ATOM   8468  C  CD2   . HIS B 1 363 ? -16.243 1.181   21.004  1.00 23.88 ? 383  HIS B CD2   1 
ATOM   8469  C  CE1   . HIS B 1 363 ? -15.265 2.694   19.755  1.00 23.69 ? 383  HIS B CE1   1 
ATOM   8470  N  NE2   . HIS B 1 363 ? -15.515 1.401   19.861  1.00 24.00 ? 383  HIS B NE2   1 
ATOM   8471  N  N     . GLU B 1 364 ? -17.159 5.298   24.557  1.00 20.48 ? 384  GLU B N     1 
ATOM   8472  C  CA    . GLU B 1 364 ? -17.381 6.435   25.459  1.00 20.62 ? 384  GLU B CA    1 
ATOM   8473  C  C     . GLU B 1 364 ? -18.422 6.206   26.549  1.00 20.21 ? 384  GLU B C     1 
ATOM   8474  O  O     . GLU B 1 364 ? -19.562 5.883   26.270  1.00 20.34 ? 384  GLU B O     1 
ATOM   8475  C  CB    . GLU B 1 364 ? -17.743 7.681   24.652  1.00 20.32 ? 384  GLU B CB    1 
ATOM   8476  C  CG    . GLU B 1 364 ? -17.875 8.964   25.472  1.00 20.69 ? 384  GLU B CG    1 
ATOM   8477  C  CD    . GLU B 1 364 ? -18.121 10.186  24.597  1.00 21.23 ? 384  GLU B CD    1 
ATOM   8478  O  OE1   . GLU B 1 364 ? -17.911 10.089  23.372  1.00 21.60 ? 384  GLU B OE1   1 
ATOM   8479  O  OE2   . GLU B 1 364 ? -18.514 11.244  25.128  1.00 21.55 ? 384  GLU B OE2   1 
ATOM   8480  N  N     . LEU B 1 365 ? -18.011 6.413   27.793  1.00 20.21 ? 385  LEU B N     1 
ATOM   8481  C  CA    . LEU B 1 365 ? -18.910 6.301   28.930  1.00 20.20 ? 385  LEU B CA    1 
ATOM   8482  C  C     . LEU B 1 365 ? -19.798 7.536   29.021  1.00 20.40 ? 385  LEU B C     1 
ATOM   8483  O  O     . LEU B 1 365 ? -19.307 8.662   28.985  1.00 20.33 ? 385  LEU B O     1 
ATOM   8484  C  CB    . LEU B 1 365 ? -18.115 6.118   30.214  1.00 19.90 ? 385  LEU B CB    1 
ATOM   8485  C  CG    . LEU B 1 365 ? -17.309 4.824   30.275  1.00 20.02 ? 385  LEU B CG    1 
ATOM   8486  C  CD1   . LEU B 1 365 ? -16.201 4.898   31.345  1.00 19.82 ? 385  LEU B CD1   1 
ATOM   8487  C  CD2   . LEU B 1 365 ? -18.235 3.622   30.504  1.00 18.80 ? 385  LEU B CD2   1 
ATOM   8488  N  N     . ALA B 1 366 ? -21.109 7.313   29.117  1.00 20.72 ? 386  ALA B N     1 
ATOM   8489  C  CA    . ALA B 1 366 ? -22.092 8.393   29.153  1.00 20.92 ? 386  ALA B CA    1 
ATOM   8490  C  C     . ALA B 1 366 ? -22.278 8.844   30.597  1.00 21.26 ? 386  ALA B C     1 
ATOM   8491  O  O     . ALA B 1 366 ? -22.758 8.065   31.427  1.00 21.36 ? 386  ALA B O     1 
ATOM   8492  C  CB    . ALA B 1 366 ? -23.412 7.938   28.558  1.00 20.67 ? 386  ALA B CB    1 
ATOM   8493  N  N     . PRO B 1 367 ? -21.897 10.098  30.908  1.00 21.60 ? 387  PRO B N     1 
ATOM   8494  C  CA    . PRO B 1 367 ? -21.975 10.572  32.295  1.00 21.60 ? 387  PRO B CA    1 
ATOM   8495  C  C     . PRO B 1 367 ? -23.400 10.592  32.839  1.00 21.83 ? 387  PRO B C     1 
ATOM   8496  O  O     . PRO B 1 367 ? -24.299 11.093  32.180  1.00 21.51 ? 387  PRO B O     1 
ATOM   8497  C  CB    . PRO B 1 367 ? -21.405 11.996  32.222  1.00 21.63 ? 387  PRO B CB    1 
ATOM   8498  C  CG    . PRO B 1 367 ? -20.592 12.031  30.976  1.00 21.70 ? 387  PRO B CG    1 
ATOM   8499  C  CD    . PRO B 1 367 ? -21.319 11.123  30.014  1.00 21.63 ? 387  PRO B CD    1 
ATOM   8500  N  N     . GLY B 1 368 ? -23.592 10.024  34.025  1.00 22.14 ? 388  GLY B N     1 
ATOM   8501  C  CA    . GLY B 1 368 ? -24.921 9.901   34.621  1.00 22.71 ? 388  GLY B CA    1 
ATOM   8502  C  C     . GLY B 1 368 ? -25.556 8.540   34.423  1.00 23.01 ? 388  GLY B C     1 
ATOM   8503  O  O     . GLY B 1 368 ? -26.380 8.126   35.240  1.00 24.25 ? 388  GLY B O     1 
ATOM   8504  N  N     . ILE B 1 369 ? -25.157 7.838   33.360  1.00 22.91 ? 389  ILE B N     1 
ATOM   8505  C  CA    . ILE B 1 369 ? -25.730 6.549   32.987  1.00 22.39 ? 389  ILE B CA    1 
ATOM   8506  C  C     . ILE B 1 369 ? -24.691 5.437   33.225  1.00 22.38 ? 389  ILE B C     1 
ATOM   8507  O  O     . ILE B 1 369 ? -24.868 4.591   34.106  1.00 21.93 ? 389  ILE B O     1 
ATOM   8508  C  CB    . ILE B 1 369 ? -26.204 6.580   31.507  1.00 22.48 ? 389  ILE B CB    1 
ATOM   8509  C  CG1   . ILE B 1 369 ? -27.182 7.745   31.277  1.00 22.88 ? 389  ILE B CG1   1 
ATOM   8510  C  CG2   . ILE B 1 369 ? -26.845 5.256   31.095  1.00 22.29 ? 389  ILE B CG2   1 
ATOM   8511  C  CD1   . ILE B 1 369 ? -27.867 7.732   29.894  1.00 21.92 ? 389  ILE B CD1   1 
ATOM   8512  N  N     . ASP B 1 370 ? -23.587 5.465   32.473  1.00 21.99 ? 390  ASP B N     1 
ATOM   8513  C  CA    . ASP B 1 370 ? -22.542 4.449   32.614  1.00 21.54 ? 390  ASP B CA    1 
ATOM   8514  C  C     . ASP B 1 370 ? -21.741 4.578   33.912  1.00 21.27 ? 390  ASP B C     1 
ATOM   8515  O  O     . ASP B 1 370 ? -21.380 3.587   34.512  1.00 20.73 ? 390  ASP B O     1 
ATOM   8516  C  CB    . ASP B 1 370 ? -21.611 4.484   31.410  1.00 22.02 ? 390  ASP B CB    1 
ATOM   8517  C  CG    . ASP B 1 370 ? -22.307 4.058   30.132  1.00 22.21 ? 390  ASP B CG    1 
ATOM   8518  O  OD1   . ASP B 1 370 ? -23.182 3.157   30.187  1.00 24.57 ? 390  ASP B OD1   1 
ATOM   8519  O  OD2   . ASP B 1 370 ? -21.984 4.623   29.075  1.00 21.11 ? 390  ASP B OD2   1 
ATOM   8520  N  N     . CYS B 1 371 ? -21.465 5.811   34.321  1.00 21.17 ? 391  CYS B N     1 
ATOM   8521  C  CA    . CYS B 1 371 ? -20.919 6.116   35.631  1.00 21.26 ? 391  CYS B CA    1 
ATOM   8522  C  C     . CYS B 1 371 ? -21.696 7.322   36.187  1.00 21.20 ? 391  CYS B C     1 
ATOM   8523  O  O     . CYS B 1 371 ? -22.333 8.053   35.423  1.00 20.83 ? 391  CYS B O     1 
ATOM   8524  C  CB    . CYS B 1 371 ? -19.432 6.455   35.520  1.00 21.52 ? 391  CYS B CB    1 
ATOM   8525  S  SG    . CYS B 1 371 ? -18.489 5.357   34.420  1.00 21.96 ? 391  CYS B SG    1 
ATOM   8526  N  N     . PRO B 1 372 ? -21.653 7.532   37.513  1.00 21.51 ? 392  PRO B N     1 
ATOM   8527  C  CA    . PRO B 1 372 ? -22.366 8.692   38.063  1.00 21.74 ? 392  PRO B CA    1 
ATOM   8528  C  C     . PRO B 1 372 ? -21.901 10.018  37.456  1.00 22.00 ? 392  PRO B C     1 
ATOM   8529  O  O     . PRO B 1 372 ? -20.762 10.123  36.960  1.00 21.29 ? 392  PRO B O     1 
ATOM   8530  C  CB    . PRO B 1 372 ? -22.046 8.639   39.566  1.00 21.55 ? 392  PRO B CB    1 
ATOM   8531  C  CG    . PRO B 1 372 ? -21.681 7.217   39.838  1.00 22.48 ? 392  PRO B CG    1 
ATOM   8532  C  CD    . PRO B 1 372 ? -21.050 6.694   38.568  1.00 21.59 ? 392  PRO B CD    1 
ATOM   8533  N  N     . GLU B 1 373 ? -22.788 11.013  37.508  1.00 22.13 ? 393  GLU B N     1 
ATOM   8534  C  CA    . GLU B 1 373 ? -22.531 12.332  36.943  1.00 22.83 ? 393  GLU B CA    1 
ATOM   8535  C  C     . GLU B 1 373 ? -21.299 12.952  37.594  1.00 22.44 ? 393  GLU B C     1 
ATOM   8536  O  O     . GLU B 1 373 ? -20.633 13.794  37.002  1.00 22.33 ? 393  GLU B O     1 
ATOM   8537  C  CB    . GLU B 1 373 ? -23.731 13.261  37.164  1.00 23.51 ? 393  GLU B CB    1 
ATOM   8538  C  CG    . GLU B 1 373 ? -25.055 12.812  36.509  1.00 26.08 ? 393  GLU B CG    1 
ATOM   8539  C  CD    . GLU B 1 373 ? -25.932 11.904  37.385  1.00 28.47 ? 393  GLU B CD    1 
ATOM   8540  O  OE1   . GLU B 1 373 ? -25.415 11.104  38.206  1.00 27.88 ? 393  GLU B OE1   1 
ATOM   8541  O  OE2   . GLU B 1 373 ? -27.174 11.974  37.223  1.00 33.58 ? 393  GLU B OE2   1 
ATOM   8542  N  N     . THR B 1 374 ? -21.036 12.519  38.826  1.00 22.11 ? 394  THR B N     1 
ATOM   8543  C  CA    . THR B 1 374 ? -19.950 12.999  39.641  1.00 22.02 ? 394  THR B CA    1 
ATOM   8544  C  C     . THR B 1 374 ? -18.615 12.285  39.385  1.00 22.32 ? 394  THR B C     1 
ATOM   8545  O  O     . THR B 1 374 ? -17.607 12.604  40.033  1.00 22.50 ? 394  THR B O     1 
ATOM   8546  C  CB    . THR B 1 374 ? -20.321 12.802  41.124  1.00 22.29 ? 394  THR B CB    1 
ATOM   8547  O  OG1   . THR B 1 374 ? -20.842 11.471  41.316  1.00 21.01 ? 394  THR B OG1   1 
ATOM   8548  C  CG2   . THR B 1 374 ? -21.372 13.826  41.558  1.00 21.93 ? 394  THR B CG2   1 
ATOM   8549  N  N     . ALA B 1 375 ? -18.597 11.323  38.462  1.00 21.63 ? 395  ALA B N     1 
ATOM   8550  C  CA    . ALA B 1 375 ? -17.414 10.486  38.271  1.00 21.52 ? 395  ALA B CA    1 
ATOM   8551  C  C     . ALA B 1 375 ? -16.264 11.224  37.579  1.00 21.15 ? 395  ALA B C     1 
ATOM   8552  O  O     . ALA B 1 375 ? -16.488 12.156  36.817  1.00 21.17 ? 395  ALA B O     1 
ATOM   8553  C  CB    . ALA B 1 375 ? -17.777 9.216   37.486  1.00 20.99 ? 395  ALA B CB    1 
ATOM   8554  N  N     . THR B 1 376 ? -15.034 10.795  37.849  1.00 20.87 ? 396  THR B N     1 
ATOM   8555  C  CA    . THR B 1 376 ? -13.880 11.258  37.072  1.00 21.09 ? 396  THR B CA    1 
ATOM   8556  C  C     . THR B 1 376 ? -13.762 10.378  35.823  1.00 21.44 ? 396  THR B C     1 
ATOM   8557  O  O     . THR B 1 376 ? -13.575 9.167   35.933  1.00 20.87 ? 396  THR B O     1 
ATOM   8558  C  CB    . THR B 1 376 ? -12.584 11.205  37.904  1.00 20.99 ? 396  THR B CB    1 
ATOM   8559  O  OG1   . THR B 1 376 ? -12.737 12.045  39.059  1.00 20.12 ? 396  THR B OG1   1 
ATOM   8560  C  CG2   . THR B 1 376 ? -11.368 11.667  37.080  1.00 20.87 ? 396  THR B CG2   1 
ATOM   8561  N  N     . PHE B 1 377 ? -13.892 10.987  34.645  1.00 21.88 ? 397  PHE B N     1 
ATOM   8562  C  CA    . PHE B 1 377 ? -13.820 10.247  33.385  1.00 22.74 ? 397  PHE B CA    1 
ATOM   8563  C  C     . PHE B 1 377 ? -12.434 10.371  32.773  1.00 22.98 ? 397  PHE B C     1 
ATOM   8564  O  O     . PHE B 1 377 ? -11.872 11.457  32.724  1.00 23.43 ? 397  PHE B O     1 
ATOM   8565  C  CB    . PHE B 1 377 ? -14.889 10.755  32.415  1.00 22.92 ? 397  PHE B CB    1 
ATOM   8566  C  CG    . PHE B 1 377 ? -16.282 10.588  32.932  1.00 23.74 ? 397  PHE B CG    1 
ATOM   8567  C  CD1   . PHE B 1 377 ? -16.862 11.566  33.731  1.00 23.17 ? 397  PHE B CD1   1 
ATOM   8568  C  CD2   . PHE B 1 377 ? -17.002 9.433   32.660  1.00 24.34 ? 397  PHE B CD2   1 
ATOM   8569  C  CE1   . PHE B 1 377 ? -18.150 11.397  34.238  1.00 23.20 ? 397  PHE B CE1   1 
ATOM   8570  C  CE2   . PHE B 1 377 ? -18.293 9.267   33.159  1.00 24.19 ? 397  PHE B CE2   1 
ATOM   8571  C  CZ    . PHE B 1 377 ? -18.860 10.253  33.949  1.00 23.11 ? 397  PHE B CZ    1 
ATOM   8572  N  N     . LEU B 1 378 ? -11.896 9.259   32.292  1.00 23.46 ? 398  LEU B N     1 
ATOM   8573  C  CA    . LEU B 1 378 ? -10.515 9.210   31.809  1.00 23.82 ? 398  LEU B CA    1 
ATOM   8574  C  C     . LEU B 1 378 ? -10.457 8.757   30.360  1.00 24.01 ? 398  LEU B C     1 
ATOM   8575  O  O     . LEU B 1 378 ? -11.111 7.777   29.953  1.00 23.29 ? 398  LEU B O     1 
ATOM   8576  C  CB    . LEU B 1 378 ? -9.679  8.256   32.659  1.00 24.10 ? 398  LEU B CB    1 
ATOM   8577  C  CG    . LEU B 1 378 ? -9.621  8.545   34.154  1.00 25.05 ? 398  LEU B CG    1 
ATOM   8578  C  CD1   . LEU B 1 378 ? -8.753  7.517   34.833  1.00 24.17 ? 398  LEU B CD1   1 
ATOM   8579  C  CD2   . LEU B 1 378 ? -9.103  9.965   34.406  1.00 25.93 ? 398  LEU B CD2   1 
ATOM   8580  N  N     . ASP B 1 379 ? -9.659  9.480   29.586  1.00 24.22 ? 399  ASP B N     1 
ATOM   8581  C  CA    . ASP B 1 379 ? -9.439  9.152   28.191  1.00 24.29 ? 399  ASP B CA    1 
ATOM   8582  C  C     . ASP B 1 379 ? -8.315  8.157   28.063  1.00 24.31 ? 399  ASP B C     1 
ATOM   8583  O  O     . ASP B 1 379 ? -7.563  7.929   29.011  1.00 24.41 ? 399  ASP B O     1 
ATOM   8584  C  CB    . ASP B 1 379 ? -9.094  10.408  27.404  1.00 24.43 ? 399  ASP B CB    1 
ATOM   8585  C  CG    . ASP B 1 379 ? -10.230 11.417  27.385  1.00 25.25 ? 399  ASP B CG    1 
ATOM   8586  O  OD1   . ASP B 1 379 ? -11.284 11.185  28.031  1.00 25.55 ? 399  ASP B OD1   1 
ATOM   8587  O  OD2   . ASP B 1 379 ? -10.063 12.450  26.717  1.00 27.04 ? 399  ASP B OD2   1 
ATOM   8588  N  N     . THR B 1 380 ? -8.213  7.549   26.885  1.00 23.96 ? 400  THR B N     1 
ATOM   8589  C  CA    . THR B 1 380 ? -7.073  6.729   26.568  1.00 23.97 ? 400  THR B CA    1 
ATOM   8590  C  C     . THR B 1 380 ? -6.820  6.708   25.068  1.00 24.00 ? 400  THR B C     1 
ATOM   8591  O  O     . THR B 1 380 ? -7.637  7.184   24.274  1.00 23.57 ? 400  THR B O     1 
ATOM   8592  C  CB    . THR B 1 380 ? -7.246  5.292   27.092  1.00 24.34 ? 400  THR B CB    1 
ATOM   8593  O  OG1   . THR B 1 380 ? -5.958  4.672   27.190  1.00 24.97 ? 400  THR B OG1   1 
ATOM   8594  C  CG2   . THR B 1 380 ? -8.169  4.459   26.177  1.00 22.97 ? 400  THR B CG2   1 
ATOM   8595  N  N     . PHE B 1 381 ? -5.667  6.163   24.701  1.00 23.89 ? 401  PHE B N     1 
ATOM   8596  C  CA    . PHE B 1 381 ? -5.290  6.002   23.302  1.00 23.94 ? 401  PHE B CA    1 
ATOM   8597  C  C     . PHE B 1 381 ? -5.120  4.513   23.002  1.00 23.67 ? 401  PHE B C     1 
ATOM   8598  O  O     . PHE B 1 381 ? -4.553  3.785   23.810  1.00 23.59 ? 401  PHE B O     1 
ATOM   8599  C  CB    . PHE B 1 381 ? -3.988  6.772   23.013  1.00 24.14 ? 401  PHE B CB    1 
ATOM   8600  C  CG    . PHE B 1 381 ? -4.194  8.239   22.735  1.00 24.41 ? 401  PHE B CG    1 
ATOM   8601  C  CD1   . PHE B 1 381 ? -4.161  9.168   23.765  1.00 24.72 ? 401  PHE B CD1   1 
ATOM   8602  C  CD2   . PHE B 1 381 ? -4.416  8.687   21.434  1.00 24.95 ? 401  PHE B CD2   1 
ATOM   8603  C  CE1   . PHE B 1 381 ? -4.357  10.521  23.510  1.00 24.90 ? 401  PHE B CE1   1 
ATOM   8604  C  CE2   . PHE B 1 381 ? -4.613  10.038  21.166  1.00 24.84 ? 401  PHE B CE2   1 
ATOM   8605  C  CZ    . PHE B 1 381 ? -4.574  10.959  22.205  1.00 24.77 ? 401  PHE B CZ    1 
ATOM   8606  N  N     . HIS B 1 382 ? -5.643  4.062   21.861  1.00 23.78 ? 402  HIS B N     1 
ATOM   8607  C  CA    . HIS B 1 382 ? -5.442  2.684   21.385  1.00 23.74 ? 402  HIS B CA    1 
ATOM   8608  C  C     . HIS B 1 382 ? -4.859  2.704   19.984  1.00 24.13 ? 402  HIS B C     1 
ATOM   8609  O  O     . HIS B 1 382 ? -5.227  3.549   19.170  1.00 23.73 ? 402  HIS B O     1 
ATOM   8610  C  CB    . HIS B 1 382 ? -6.750  1.890   21.340  1.00 23.41 ? 402  HIS B CB    1 
ATOM   8611  C  CG    . HIS B 1 382 ? -7.343  1.610   22.684  1.00 23.22 ? 402  HIS B CG    1 
ATOM   8612  N  ND1   . HIS B 1 382 ? -6.681  0.895   23.656  1.00 22.46 ? 402  HIS B ND1   1 
ATOM   8613  C  CD2   . HIS B 1 382 ? -8.551  1.930   23.209  1.00 22.91 ? 402  HIS B CD2   1 
ATOM   8614  C  CE1   . HIS B 1 382 ? -7.442  0.811   24.733  1.00 23.28 ? 402  HIS B CE1   1 
ATOM   8615  N  NE2   . HIS B 1 382 ? -8.585  1.428   24.486  1.00 23.11 ? 402  HIS B NE2   1 
ATOM   8616  N  N     . TYR B 1 383 ? -3.944  1.773   19.715  1.00 24.68 ? 403  TYR B N     1 
ATOM   8617  C  CA    . TYR B 1 383 ? -3.510  1.475   18.350  1.00 24.95 ? 403  TYR B CA    1 
ATOM   8618  C  C     . TYR B 1 383 ? -3.806  -0.005  18.086  1.00 24.83 ? 403  TYR B C     1 
ATOM   8619  O  O     . TYR B 1 383 ? -3.024  -0.889  18.445  1.00 24.33 ? 403  TYR B O     1 
ATOM   8620  C  CB    . TYR B 1 383 ? -2.024  1.800   18.161  1.00 25.52 ? 403  TYR B CB    1 
ATOM   8621  C  CG    . TYR B 1 383 ? -1.526  1.621   16.736  1.00 27.68 ? 403  TYR B CG    1 
ATOM   8622  C  CD1   . TYR B 1 383 ? -1.458  2.701   15.859  1.00 30.40 ? 403  TYR B CD1   1 
ATOM   8623  C  CD2   . TYR B 1 383 ? -1.132  0.373   16.266  1.00 29.65 ? 403  TYR B CD2   1 
ATOM   8624  C  CE1   . TYR B 1 383 ? -1.005  2.540   14.549  1.00 31.92 ? 403  TYR B CE1   1 
ATOM   8625  C  CE2   . TYR B 1 383 ? -0.677  0.201   14.966  1.00 31.20 ? 403  TYR B CE2   1 
ATOM   8626  C  CZ    . TYR B 1 383 ? -0.621  1.285   14.113  1.00 32.83 ? 403  TYR B CZ    1 
ATOM   8627  O  OH    . TYR B 1 383 ? -0.179  1.107   12.824  1.00 35.93 ? 403  TYR B OH    1 
ATOM   8628  N  N     . TYR B 1 384 ? -4.968  -0.260  17.495  1.00 25.07 ? 404  TYR B N     1 
ATOM   8629  C  CA    . TYR B 1 384 ? -5.424  -1.608  17.193  1.00 25.38 ? 404  TYR B CA    1 
ATOM   8630  C  C     . TYR B 1 384 ? -6.177  -1.530  15.865  1.00 25.71 ? 404  TYR B C     1 
ATOM   8631  O  O     . TYR B 1 384 ? -7.204  -0.862  15.789  1.00 25.10 ? 404  TYR B O     1 
ATOM   8632  C  CB    . TYR B 1 384 ? -6.347  -2.136  18.319  1.00 25.59 ? 404  TYR B CB    1 
ATOM   8633  C  CG    . TYR B 1 384 ? -6.912  -3.522  18.062  1.00 26.13 ? 404  TYR B CG    1 
ATOM   8634  C  CD1   . TYR B 1 384 ? -6.406  -4.649  18.714  1.00 28.09 ? 404  TYR B CD1   1 
ATOM   8635  C  CD2   . TYR B 1 384 ? -7.937  -3.710  17.150  1.00 27.71 ? 404  TYR B CD2   1 
ATOM   8636  C  CE1   . TYR B 1 384 ? -6.930  -5.935  18.453  1.00 28.59 ? 404  TYR B CE1   1 
ATOM   8637  C  CE2   . TYR B 1 384 ? -8.458  -4.978  16.878  1.00 27.95 ? 404  TYR B CE2   1 
ATOM   8638  C  CZ    . TYR B 1 384 ? -7.964  -6.080  17.527  1.00 28.93 ? 404  TYR B CZ    1 
ATOM   8639  O  OH    . TYR B 1 384 ? -8.510  -7.319  17.218  1.00 29.38 ? 404  TYR B OH    1 
ATOM   8640  N  N     . ASP B 1 385 ? -5.674  -2.223  14.842  1.00 25.94 ? 405  ASP B N     1 
ATOM   8641  C  CA    . ASP B 1 385 ? -6.235  -2.158  13.483  1.00 26.85 ? 405  ASP B CA    1 
ATOM   8642  C  C     . ASP B 1 385 ? -6.508  -0.701  13.056  1.00 27.22 ? 405  ASP B C     1 
ATOM   8643  O  O     . ASP B 1 385 ? -7.629  -0.336  12.709  1.00 27.18 ? 405  ASP B O     1 
ATOM   8644  C  CB    . ASP B 1 385 ? -7.513  -3.013  13.379  1.00 26.95 ? 405  ASP B CB    1 
ATOM   8645  C  CG    . ASP B 1 385 ? -8.019  -3.150  11.946  1.00 27.99 ? 405  ASP B CG    1 
ATOM   8646  O  OD1   . ASP B 1 385 ? -7.202  -3.015  11.002  1.00 30.03 ? 405  ASP B OD1   1 
ATOM   8647  O  OD2   . ASP B 1 385 ? -9.233  -3.400  11.758  1.00 28.56 ? 405  ASP B OD2   1 
ATOM   8648  N  N     . ALA B 1 386 ? -5.468  0.125   13.102  1.00 27.78 ? 406  ALA B N     1 
ATOM   8649  C  CA    . ALA B 1 386 ? -5.613  1.549   12.855  1.00 28.23 ? 406  ALA B CA    1 
ATOM   8650  C  C     . ALA B 1 386 ? -4.418  2.100   12.091  1.00 28.52 ? 406  ALA B C     1 
ATOM   8651  O  O     . ALA B 1 386 ? -3.329  1.532   12.125  1.00 28.70 ? 406  ALA B O     1 
ATOM   8652  C  CB    . ALA B 1 386 ? -5.779  2.289   14.172  1.00 28.30 ? 406  ALA B CB    1 
ATOM   8653  N  N     . ASP B 1 387 ? -4.636  3.219   11.410  1.00 28.74 ? 407  ASP B N     1 
ATOM   8654  C  CA    . ASP B 1 387 ? -3.579  3.872   10.651  1.00 28.69 ? 407  ASP B CA    1 
ATOM   8655  C  C     . ASP B 1 387 ? -2.729  4.749   11.569  1.00 28.85 ? 407  ASP B C     1 
ATOM   8656  O  O     . ASP B 1 387 ? -1.527  4.894   11.347  1.00 29.13 ? 407  ASP B O     1 
ATOM   8657  C  CB    . ASP B 1 387 ? -4.174  4.696   9.497   1.00 28.66 ? 407  ASP B CB    1 
ATOM   8658  C  CG    . ASP B 1 387 ? -4.660  3.831   8.346   1.00 28.29 ? 407  ASP B CG    1 
ATOM   8659  O  OD1   . ASP B 1 387 ? -4.469  2.604   8.389   1.00 28.19 ? 407  ASP B OD1   1 
ATOM   8660  O  OD2   . ASP B 1 387 ? -5.225  4.376   7.381   1.00 28.67 ? 407  ASP B OD2   1 
ATOM   8661  N  N     . ASP B 1 388 ? -3.367  5.323   12.587  1.00 28.79 ? 408  ASP B N     1 
ATOM   8662  C  CA    . ASP B 1 388 ? -2.716  6.155   13.603  1.00 28.81 ? 408  ASP B CA    1 
ATOM   8663  C  C     . ASP B 1 388 ? -3.283  5.791   14.978  1.00 28.31 ? 408  ASP B C     1 
ATOM   8664  O  O     . ASP B 1 388 ? -4.324  5.135   15.055  1.00 28.59 ? 408  ASP B O     1 
ATOM   8665  C  CB    . ASP B 1 388 ? -2.995  7.628   13.317  1.00 28.89 ? 408  ASP B CB    1 
ATOM   8666  C  CG    . ASP B 1 388 ? -2.507  8.053   11.957  1.00 30.29 ? 408  ASP B CG    1 
ATOM   8667  O  OD1   . ASP B 1 388 ? -1.278  8.057   11.756  1.00 32.82 ? 408  ASP B OD1   1 
ATOM   8668  O  OD2   . ASP B 1 388 ? -3.342  8.378   11.090  1.00 32.92 ? 408  ASP B OD2   1 
ATOM   8669  N  N     . PRO B 1 389 ? -2.611  6.218   16.065  1.00 27.65 ? 409  PRO B N     1 
ATOM   8670  C  CA    . PRO B 1 389 ? -3.176  6.017   17.403  1.00 27.00 ? 409  PRO B CA    1 
ATOM   8671  C  C     . PRO B 1 389 ? -4.498  6.757   17.536  1.00 26.10 ? 409  PRO B C     1 
ATOM   8672  O  O     . PRO B 1 389 ? -4.613  7.886   17.077  1.00 25.92 ? 409  PRO B O     1 
ATOM   8673  C  CB    . PRO B 1 389 ? -2.120  6.624   18.332  1.00 27.19 ? 409  PRO B CB    1 
ATOM   8674  C  CG    . PRO B 1 389 ? -0.868  6.682   17.504  1.00 27.56 ? 409  PRO B CG    1 
ATOM   8675  C  CD    . PRO B 1 389 ? -1.323  6.932   16.121  1.00 27.53 ? 409  PRO B CD    1 
ATOM   8676  N  N     . VAL B 1 390 ? -5.492  6.114   18.138  1.00 25.30 ? 410  VAL B N     1 
ATOM   8677  C  CA    . VAL B 1 390 ? -6.838  6.673   18.201  1.00 24.53 ? 410  VAL B CA    1 
ATOM   8678  C  C     . VAL B 1 390 ? -7.200  7.097   19.629  1.00 24.36 ? 410  VAL B C     1 
ATOM   8679  O  O     . VAL B 1 390 ? -7.020  6.339   20.569  1.00 23.67 ? 410  VAL B O     1 
ATOM   8680  C  CB    . VAL B 1 390 ? -7.861  5.668   17.634  1.00 24.55 ? 410  VAL B CB    1 
ATOM   8681  C  CG1   . VAL B 1 390 ? -9.276  6.236   17.695  1.00 23.04 ? 410  VAL B CG1   1 
ATOM   8682  C  CG2   . VAL B 1 390 ? -7.470  5.291   16.182  1.00 23.33 ? 410  VAL B CG2   1 
ATOM   8683  N  N     . HIS B 1 391 ? -7.693  8.329   19.767  1.00 24.48 ? 411  HIS B N     1 
ATOM   8684  C  CA    . HIS B 1 391 ? -8.159  8.872   21.050  1.00 24.43 ? 411  HIS B CA    1 
ATOM   8685  C  C     . HIS B 1 391 ? -9.536  8.287   21.382  1.00 24.35 ? 411  HIS B C     1 
ATOM   8686  O  O     . HIS B 1 391 ? -10.461 8.363   20.568  1.00 24.41 ? 411  HIS B O     1 
ATOM   8687  C  CB    . HIS B 1 391 ? -8.250  10.398  20.961  1.00 24.46 ? 411  HIS B CB    1 
ATOM   8688  C  CG    . HIS B 1 391 ? -8.679  11.066  22.232  1.00 25.40 ? 411  HIS B CG    1 
ATOM   8689  N  ND1   . HIS B 1 391 ? -9.925  11.625  22.390  1.00 25.94 ? 411  HIS B ND1   1 
ATOM   8690  C  CD2   . HIS B 1 391 ? -8.022  11.278  23.397  1.00 26.33 ? 411  HIS B CD2   1 
ATOM   8691  C  CE1   . HIS B 1 391 ? -10.026 12.140  23.602  1.00 27.13 ? 411  HIS B CE1   1 
ATOM   8692  N  NE2   . HIS B 1 391 ? -8.881  11.947  24.233  1.00 26.15 ? 411  HIS B NE2   1 
ATOM   8693  N  N     . TYR B 1 392 ? -9.661  7.697   22.568  1.00 23.97 ? 412  TYR B N     1 
ATOM   8694  C  CA    . TYR B 1 392 ? -10.945 7.183   23.046  1.00 23.76 ? 412  TYR B CA    1 
ATOM   8695  C  C     . TYR B 1 392 ? -11.407 8.019   24.228  1.00 23.61 ? 412  TYR B C     1 
ATOM   8696  O  O     . TYR B 1 392 ? -10.862 7.880   25.324  1.00 23.67 ? 412  TYR B O     1 
ATOM   8697  C  CB    . TYR B 1 392 ? -10.809 5.717   23.459  1.00 24.08 ? 412  TYR B CB    1 
ATOM   8698  C  CG    . TYR B 1 392 ? -10.881 4.765   22.294  1.00 23.29 ? 412  TYR B CG    1 
ATOM   8699  C  CD1   . TYR B 1 392 ? -9.881  4.751   21.315  1.00 24.77 ? 412  TYR B CD1   1 
ATOM   8700  C  CD2   . TYR B 1 392 ? -11.953 3.895   22.150  1.00 23.53 ? 412  TYR B CD2   1 
ATOM   8701  C  CE1   . TYR B 1 392 ? -9.949  3.883   20.225  1.00 24.09 ? 412  TYR B CE1   1 
ATOM   8702  C  CE2   . TYR B 1 392 ? -12.037 3.032   21.068  1.00 24.27 ? 412  TYR B CE2   1 
ATOM   8703  C  CZ    . TYR B 1 392 ? -11.033 3.026   20.112  1.00 24.58 ? 412  TYR B CZ    1 
ATOM   8704  O  OH    . TYR B 1 392 ? -11.125 2.166   19.053  1.00 23.85 ? 412  TYR B OH    1 
ATOM   8705  N  N     . PRO B 1 393 ? -12.406 8.900   24.018  1.00 23.12 ? 413  PRO B N     1 
ATOM   8706  C  CA    . PRO B 1 393 ? -12.876 9.739   25.130  1.00 23.01 ? 413  PRO B CA    1 
ATOM   8707  C  C     . PRO B 1 393 ? -13.652 8.953   26.190  1.00 22.51 ? 413  PRO B C     1 
ATOM   8708  O  O     . PRO B 1 393 ? -14.436 8.065   25.847  1.00 22.34 ? 413  PRO B O     1 
ATOM   8709  C  CB    . PRO B 1 393 ? -13.789 10.760  24.443  1.00 22.75 ? 413  PRO B CB    1 
ATOM   8710  C  CG    . PRO B 1 393 ? -14.293 10.067  23.246  1.00 23.38 ? 413  PRO B CG    1 
ATOM   8711  C  CD    . PRO B 1 393 ? -13.204 9.115   22.799  1.00 23.55 ? 413  PRO B CD    1 
ATOM   8712  N  N     . ARG B 1 394 ? -13.409 9.270   27.459  1.00 22.22 ? 414  ARG B N     1 
ATOM   8713  C  CA    . ARG B 1 394 ? -14.118 8.647   28.575  1.00 21.95 ? 414  ARG B CA    1 
ATOM   8714  C  C     . ARG B 1 394 ? -14.151 7.118   28.439  1.00 21.76 ? 414  ARG B C     1 
ATOM   8715  O  O     . ARG B 1 394 ? -15.226 6.506   28.479  1.00 21.54 ? 414  ARG B O     1 
ATOM   8716  C  CB    . ARG B 1 394 ? -15.552 9.187   28.652  1.00 22.04 ? 414  ARG B CB    1 
ATOM   8717  C  CG    . ARG B 1 394 ? -15.678 10.708  28.687  1.00 23.06 ? 414  ARG B CG    1 
ATOM   8718  C  CD    . ARG B 1 394 ? -17.154 11.079  28.850  1.00 25.07 ? 414  ARG B CD    1 
ATOM   8719  N  NE    . ARG B 1 394 ? -17.434 12.515  28.980  1.00 25.31 ? 414  ARG B NE    1 
ATOM   8720  C  CZ    . ARG B 1 394 ? -18.477 13.140  28.423  1.00 26.12 ? 414  ARG B CZ    1 
ATOM   8721  N  NH1   . ARG B 1 394 ? -19.332 12.483  27.636  1.00 26.14 ? 414  ARG B NH1   1 
ATOM   8722  N  NH2   . ARG B 1 394 ? -18.656 14.442  28.620  1.00 25.76 ? 414  ARG B NH2   1 
ATOM   8723  N  N     . ALA B 1 395 ? -12.968 6.523   28.270  1.00 21.26 ? 415  ALA B N     1 
ATOM   8724  C  CA    . ALA B 1 395 ? -12.803 5.081   28.103  1.00 20.96 ? 415  ALA B CA    1 
ATOM   8725  C  C     . ALA B 1 395 ? -12.910 4.340   29.436  1.00 20.93 ? 415  ALA B C     1 
ATOM   8726  O  O     . ALA B 1 395 ? -13.344 3.183   29.480  1.00 20.88 ? 415  ALA B O     1 
ATOM   8727  C  CB    . ALA B 1 395 ? -11.437 4.775   27.438  1.00 20.87 ? 415  ALA B CB    1 
ATOM   8728  N  N     . LEU B 1 396 ? -12.458 4.993   30.504  1.00 20.78 ? 416  LEU B N     1 
ATOM   8729  C  CA    . LEU B 1 396 ? -12.653 4.516   31.861  1.00 20.56 ? 416  LEU B CA    1 
ATOM   8730  C  C     . LEU B 1 396 ? -13.255 5.627   32.701  1.00 20.31 ? 416  LEU B C     1 
ATOM   8731  O  O     . LEU B 1 396 ? -13.229 6.793   32.309  1.00 19.95 ? 416  LEU B O     1 
ATOM   8732  C  CB    . LEU B 1 396 ? -11.325 4.110   32.520  1.00 20.99 ? 416  LEU B CB    1 
ATOM   8733  C  CG    . LEU B 1 396 ? -10.229 3.425   31.719  1.00 21.04 ? 416  LEU B CG    1 
ATOM   8734  C  CD1   . LEU B 1 396 ? -9.389  4.466   30.998  1.00 20.94 ? 416  LEU B CD1   1 
ATOM   8735  C  CD2   . LEU B 1 396 ? -9.359  2.573   32.645  1.00 21.69 ? 416  LEU B CD2   1 
ATOM   8736  N  N     . CYS B 1 397 ? -13.773 5.257   33.868  1.00 20.04 ? 417  CYS B N     1 
ATOM   8737  C  CA    . CYS B 1 397 ? -14.158 6.227   34.881  1.00 19.97 ? 417  CYS B CA    1 
ATOM   8738  C  C     . CYS B 1 397 ? -13.766 5.728   36.270  1.00 20.13 ? 417  CYS B C     1 
ATOM   8739  O  O     . CYS B 1 397 ? -13.683 4.520   36.522  1.00 20.90 ? 417  CYS B O     1 
ATOM   8740  C  CB    . CYS B 1 397 ? -15.663 6.516   34.820  1.00 20.21 ? 417  CYS B CB    1 
ATOM   8741  S  SG    . CYS B 1 397 ? -16.678 5.153   35.393  1.00 20.23 ? 417  CYS B SG    1 
ATOM   8742  N  N     . LEU B 1 398 ? -13.534 6.671   37.167  1.00 20.21 ? 418  LEU B N     1 
ATOM   8743  C  CA    . LEU B 1 398 ? -13.127 6.381   38.532  1.00 20.57 ? 418  LEU B CA    1 
ATOM   8744  C  C     . LEU B 1 398 ? -14.037 7.178   39.458  1.00 20.60 ? 418  LEU B C     1 
ATOM   8745  O  O     . LEU B 1 398 ? -14.174 8.383   39.298  1.00 20.32 ? 418  LEU B O     1 
ATOM   8746  C  CB    . LEU B 1 398 ? -11.666 6.791   38.722  1.00 20.39 ? 418  LEU B CB    1 
ATOM   8747  C  CG    . LEU B 1 398 ? -10.994 6.459   40.042  1.00 20.75 ? 418  LEU B CG    1 
ATOM   8748  C  CD1   . LEU B 1 398 ? -11.094 4.953   40.367  1.00 19.36 ? 418  LEU B CD1   1 
ATOM   8749  C  CD2   . LEU B 1 398 ? -9.524  6.946   39.993  1.00 21.01 ? 418  LEU B CD2   1 
ATOM   8750  N  N     . PHE B 1 399 ? -14.685 6.514   40.412  1.00 21.02 ? 419  PHE B N     1 
ATOM   8751  C  CA    . PHE B 1 399 ? -15.663 7.213   41.237  1.00 21.01 ? 419  PHE B CA    1 
ATOM   8752  C  C     . PHE B 1 399 ? -15.946 6.551   42.568  1.00 21.42 ? 419  PHE B C     1 
ATOM   8753  O  O     . PHE B 1 399 ? -15.824 5.338   42.702  1.00 21.80 ? 419  PHE B O     1 
ATOM   8754  C  CB    . PHE B 1 399 ? -16.979 7.429   40.456  1.00 21.06 ? 419  PHE B CB    1 
ATOM   8755  C  CG    . PHE B 1 399 ? -17.727 6.161   40.118  1.00 20.96 ? 419  PHE B CG    1 
ATOM   8756  C  CD1   . PHE B 1 399 ? -18.712 5.660   40.977  1.00 21.07 ? 419  PHE B CD1   1 
ATOM   8757  C  CD2   . PHE B 1 399 ? -17.489 5.496   38.928  1.00 20.21 ? 419  PHE B CD2   1 
ATOM   8758  C  CE1   . PHE B 1 399 ? -19.420 4.510   40.665  1.00 19.02 ? 419  PHE B CE1   1 
ATOM   8759  C  CE2   . PHE B 1 399 ? -18.186 4.334   38.612  1.00 20.24 ? 419  PHE B CE2   1 
ATOM   8760  C  CZ    . PHE B 1 399 ? -19.160 3.844   39.483  1.00 19.84 ? 419  PHE B CZ    1 
ATOM   8761  N  N     . GLU B 1 400 ? -16.310 7.370   43.555  1.00 21.52 ? 420  GLU B N     1 
ATOM   8762  C  CA    . GLU B 1 400 ? -16.798 6.873   44.832  1.00 21.64 ? 420  GLU B CA    1 
ATOM   8763  C  C     . GLU B 1 400 ? -18.320 6.960   44.822  1.00 21.84 ? 420  GLU B C     1 
ATOM   8764  O  O     . GLU B 1 400 ? -18.887 7.940   44.347  1.00 21.49 ? 420  GLU B O     1 
ATOM   8765  C  CB    . GLU B 1 400 ? -16.238 7.697   46.001  1.00 21.54 ? 420  GLU B CB    1 
ATOM   8766  C  CG    . GLU B 1 400 ? -16.640 7.168   47.368  1.00 21.07 ? 420  GLU B CG    1 
ATOM   8767  C  CD    . GLU B 1 400 ? -15.915 7.853   48.515  1.00 21.63 ? 420  GLU B CD    1 
ATOM   8768  O  OE1   . GLU B 1 400 ? -15.610 9.054   48.405  1.00 21.71 ? 420  GLU B OE1   1 
ATOM   8769  O  OE2   . GLU B 1 400 ? -15.651 7.185   49.540  1.00 23.95 ? 420  GLU B OE2   1 
ATOM   8770  N  N     . MET B 1 401 ? -18.983 5.940   45.344  1.00 22.15 ? 421  MET B N     1 
ATOM   8771  C  CA    . MET B 1 401 ? -20.439 5.985   45.430  1.00 23.01 ? 421  MET B CA    1 
ATOM   8772  C  C     . MET B 1 401 ? -20.918 5.329   46.699  1.00 22.28 ? 421  MET B C     1 
ATOM   8773  O  O     . MET B 1 401 ? -20.359 4.311   47.131  1.00 21.83 ? 421  MET B O     1 
ATOM   8774  C  CB    . MET B 1 401 ? -21.105 5.324   44.217  1.00 23.66 ? 421  MET B CB    1 
ATOM   8775  C  CG    . MET B 1 401 ? -20.742 3.863   44.003  1.00 26.78 ? 421  MET B CG    1 
ATOM   8776  S  SD    . MET B 1 401 ? -21.935 3.003   42.950  1.00 31.78 ? 421  MET B SD    1 
ATOM   8777  C  CE    . MET B 1 401 ? -23.341 2.816   44.052  1.00 33.06 ? 421  MET B CE    1 
ATOM   8778  N  N     . PRO B 1 402 ? -21.953 5.913   47.313  1.00 21.77 ? 422  PRO B N     1 
ATOM   8779  C  CA    . PRO B 1 402 ? -22.552 5.213   48.431  1.00 21.77 ? 422  PRO B CA    1 
ATOM   8780  C  C     . PRO B 1 402 ? -23.179 3.881   47.994  1.00 21.47 ? 422  PRO B C     1 
ATOM   8781  O  O     . PRO B 1 402 ? -23.819 3.796   46.945  1.00 20.95 ? 422  PRO B O     1 
ATOM   8782  C  CB    . PRO B 1 402 ? -23.592 6.207   48.975  1.00 21.41 ? 422  PRO B CB    1 
ATOM   8783  C  CG    . PRO B 1 402 ? -23.773 7.210   47.974  1.00 22.10 ? 422  PRO B CG    1 
ATOM   8784  C  CD    . PRO B 1 402 ? -22.583 7.215   47.060  1.00 21.91 ? 422  PRO B CD    1 
ATOM   8785  N  N     . THR B 1 403 ? -22.931 2.845   48.786  1.00 21.96 ? 423  THR B N     1 
ATOM   8786  C  CA    . THR B 1 403 ? -23.477 1.508   48.545  1.00 22.10 ? 423  THR B CA    1 
ATOM   8787  C  C     . THR B 1 403 ? -24.923 1.380   49.032  1.00 22.28 ? 423  THR B C     1 
ATOM   8788  O  O     . THR B 1 403 ? -25.618 0.446   48.678  1.00 22.47 ? 423  THR B O     1 
ATOM   8789  C  CB    . THR B 1 403 ? -22.671 0.464   49.291  1.00 21.73 ? 423  THR B CB    1 
ATOM   8790  O  OG1   . THR B 1 403 ? -22.718 0.761   50.695  1.00 21.56 ? 423  THR B OG1   1 
ATOM   8791  C  CG2   . THR B 1 403 ? -21.220 0.448   48.801  1.00 22.39 ? 423  THR B CG2   1 
ATOM   8792  N  N     . GLY B 1 404 ? -25.351 2.301   49.880  1.00 22.84 ? 424  GLY B N     1 
ATOM   8793  C  CA    . GLY B 1 404 ? -26.692 2.266   50.433  1.00 23.23 ? 424  GLY B CA    1 
ATOM   8794  C  C     . GLY B 1 404 ? -26.843 1.265   51.561  1.00 23.44 ? 424  GLY B C     1 
ATOM   8795  O  O     . GLY B 1 404 ? -27.962 0.964   51.958  1.00 24.53 ? 424  GLY B O     1 
ATOM   8796  N  N     . VAL B 1 405 ? -25.735 0.720   52.061  1.00 23.08 ? 425  VAL B N     1 
ATOM   8797  C  CA    . VAL B 1 405 ? -25.772 -0.168  53.221  1.00 22.80 ? 425  VAL B CA    1 
ATOM   8798  C  C     . VAL B 1 405 ? -24.524 0.109   54.071  1.00 22.34 ? 425  VAL B C     1 
ATOM   8799  O  O     . VAL B 1 405 ? -23.421 0.164   53.537  1.00 22.55 ? 425  VAL B O     1 
ATOM   8800  C  CB    . VAL B 1 405 ? -25.888 -1.669  52.815  1.00 23.07 ? 425  VAL B CB    1 
ATOM   8801  C  CG1   . VAL B 1 405 ? -24.668 -2.135  52.036  1.00 22.26 ? 425  VAL B CG1   1 
ATOM   8802  C  CG2   . VAL B 1 405 ? -26.106 -2.549  54.056  1.00 23.50 ? 425  VAL B CG2   1 
ATOM   8803  N  N     . PRO B 1 406 ? -24.699 0.329   55.388  1.00 21.78 ? 426  PRO B N     1 
ATOM   8804  C  CA    . PRO B 1 406 ? -23.552 0.749   56.174  1.00 21.68 ? 426  PRO B CA    1 
ATOM   8805  C  C     . PRO B 1 406 ? -22.456 -0.288  56.126  1.00 21.41 ? 426  PRO B C     1 
ATOM   8806  O  O     . PRO B 1 406 ? -22.748 -1.485  56.011  1.00 21.21 ? 426  PRO B O     1 
ATOM   8807  C  CB    . PRO B 1 406 ? -24.113 0.898   57.596  1.00 21.84 ? 426  PRO B CB    1 
ATOM   8808  C  CG    . PRO B 1 406 ? -25.455 0.253   57.582  1.00 21.98 ? 426  PRO B CG    1 
ATOM   8809  C  CD    . PRO B 1 406 ? -25.939 0.301   56.184  1.00 22.02 ? 426  PRO B CD    1 
ATOM   8810  N  N     . LEU B 1 407 ? -21.203 0.150   56.184  1.00 21.19 ? 427  LEU B N     1 
ATOM   8811  C  CA    . LEU B 1 407 ? -20.103 -0.808  56.243  1.00 21.39 ? 427  LEU B CA    1 
ATOM   8812  C  C     . LEU B 1 407 ? -20.205 -1.613  57.545  1.00 21.38 ? 427  LEU B C     1 
ATOM   8813  O  O     . LEU B 1 407 ? -19.926 -2.815  57.573  1.00 21.42 ? 427  LEU B O     1 
ATOM   8814  C  CB    . LEU B 1 407 ? -18.743 -0.111  56.122  1.00 21.56 ? 427  LEU B CB    1 
ATOM   8815  C  CG    . LEU B 1 407 ? -17.565 -1.093  56.009  1.00 21.59 ? 427  LEU B CG    1 
ATOM   8816  C  CD1   . LEU B 1 407 ? -16.403 -0.499  55.194  1.00 21.56 ? 427  LEU B CD1   1 
ATOM   8817  C  CD2   . LEU B 1 407 ? -17.091 -1.543  57.389  1.00 21.37 ? 427  LEU B CD2   1 
ATOM   8818  N  N     . ARG B 1 408 ? -20.603 -0.936  58.618  1.00 21.14 ? 428  ARG B N     1 
ATOM   8819  C  CA    . ARG B 1 408 ? -20.916 -1.591  59.882  1.00 21.30 ? 428  ARG B CA    1 
ATOM   8820  C  C     . ARG B 1 408 ? -21.857 -0.708  60.673  1.00 21.21 ? 428  ARG B C     1 
ATOM   8821  O  O     . ARG B 1 408 ? -21.833 0.510   60.528  1.00 20.88 ? 428  ARG B O     1 
ATOM   8822  C  CB    . ARG B 1 408 ? -19.650 -1.856  60.701  1.00 21.32 ? 428  ARG B CB    1 
ATOM   8823  C  CG    . ARG B 1 408 ? -18.753 -0.630  60.908  1.00 22.56 ? 428  ARG B CG    1 
ATOM   8824  C  CD    . ARG B 1 408 ? -17.580 -0.967  61.816  1.00 23.78 ? 428  ARG B CD    1 
ATOM   8825  N  NE    . ARG B 1 408 ? -16.364 -0.271  61.407  1.00 24.64 ? 428  ARG B NE    1 
ATOM   8826  C  CZ    . ARG B 1 408 ? -16.063 0.994   61.690  1.00 26.42 ? 428  ARG B CZ    1 
ATOM   8827  N  NH1   . ARG B 1 408 ? -16.881 1.755   62.403  1.00 28.11 ? 428  ARG B NH1   1 
ATOM   8828  N  NH2   . ARG B 1 408 ? -14.923 1.508   61.244  1.00 27.10 ? 428  ARG B NH2   1 
ATOM   8829  N  N     . ARG B 1 409 ? -22.699 -1.333  61.493  1.00 21.17 ? 429  ARG B N     1 
ATOM   8830  C  CA    . ARG B 1 409 ? -23.591 -0.597  62.382  1.00 20.82 ? 429  ARG B CA    1 
ATOM   8831  C  C     . ARG B 1 409 ? -23.986 -1.485  63.545  1.00 21.13 ? 429  ARG B C     1 
ATOM   8832  O  O     . ARG B 1 409 ? -23.971 -2.710  63.423  1.00 21.02 ? 429  ARG B O     1 
ATOM   8833  C  CB    . ARG B 1 409 ? -24.821 -0.074  61.637  1.00 20.61 ? 429  ARG B CB    1 
ATOM   8834  C  CG    . ARG B 1 409 ? -25.787 -1.140  61.140  1.00 20.13 ? 429  ARG B CG    1 
ATOM   8835  C  CD    . ARG B 1 409 ? -26.837 -1.493  62.184  1.00 20.58 ? 429  ARG B CD    1 
ATOM   8836  N  NE    . ARG B 1 409 ? -27.877 -0.473  62.286  1.00 20.25 ? 429  ARG B NE    1 
ATOM   8837  C  CZ    . ARG B 1 409 ? -28.909 -0.534  63.117  1.00 20.70 ? 429  ARG B CZ    1 
ATOM   8838  N  NH1   . ARG B 1 409 ? -29.049 -1.555  63.966  1.00 19.88 ? 429  ARG B NH1   1 
ATOM   8839  N  NH2   . ARG B 1 409 ? -29.802 0.448   63.113  1.00 22.89 ? 429  ARG B NH2   1 
ATOM   8840  N  N     . HIS B 1 410 ? -24.317 -0.857  64.673  1.00 21.10 ? 430  HIS B N     1 
ATOM   8841  C  CA    . HIS B 1 410 ? -24.777 -1.569  65.849  1.00 20.87 ? 430  HIS B CA    1 
ATOM   8842  C  C     . HIS B 1 410 ? -25.655 -0.694  66.732  1.00 21.12 ? 430  HIS B C     1 
ATOM   8843  O  O     . HIS B 1 410 ? -25.285 0.440   67.051  1.00 20.80 ? 430  HIS B O     1 
ATOM   8844  C  CB    . HIS B 1 410 ? -23.600 -2.067  66.683  1.00 21.07 ? 430  HIS B CB    1 
ATOM   8845  C  CG    . HIS B 1 410 ? -24.017 -2.752  67.941  1.00 19.67 ? 430  HIS B CG    1 
ATOM   8846  N  ND1   . HIS B 1 410 ? -24.693 -3.951  67.940  1.00 21.58 ? 430  HIS B ND1   1 
ATOM   8847  C  CD2   . HIS B 1 410 ? -23.884 -2.397  69.240  1.00 19.58 ? 430  HIS B CD2   1 
ATOM   8848  C  CE1   . HIS B 1 410 ? -24.946 -4.315  69.186  1.00 21.23 ? 430  HIS B CE1   1 
ATOM   8849  N  NE2   . HIS B 1 410 ? -24.460 -3.391  69.995  1.00 19.59 ? 430  HIS B NE2   1 
ATOM   8850  N  N     . PHE B 1 411 ? -26.803 -1.241  67.138  1.00 20.96 ? 431  PHE B N     1 
ATOM   8851  C  CA    . PHE B 1 411 ? -27.665 -0.603  68.115  1.00 21.24 ? 431  PHE B CA    1 
ATOM   8852  C  C     . PHE B 1 411 ? -27.450 -1.321  69.446  1.00 21.70 ? 431  PHE B C     1 
ATOM   8853  O  O     . PHE B 1 411 ? -27.832 -2.477  69.596  1.00 21.49 ? 431  PHE B O     1 
ATOM   8854  C  CB    . PHE B 1 411 ? -29.127 -0.682  67.678  1.00 21.27 ? 431  PHE B CB    1 
ATOM   8855  C  CG    . PHE B 1 411 ? -30.061 0.020   68.599  1.00 20.96 ? 431  PHE B CG    1 
ATOM   8856  C  CD1   . PHE B 1 411 ? -30.652 -0.656  69.660  1.00 21.97 ? 431  PHE B CD1   1 
ATOM   8857  C  CD2   . PHE B 1 411 ? -30.318 1.377   68.439  1.00 21.17 ? 431  PHE B CD2   1 
ATOM   8858  C  CE1   . PHE B 1 411 ? -31.508 0.005   70.532  1.00 21.46 ? 431  PHE B CE1   1 
ATOM   8859  C  CE2   . PHE B 1 411 ? -31.180 2.045   69.295  1.00 21.38 ? 431  PHE B CE2   1 
ATOM   8860  C  CZ    . PHE B 1 411 ? -31.775 1.357   70.348  1.00 21.38 ? 431  PHE B CZ    1 
ATOM   8861  N  N     . ASN B 1 412 ? -26.797 -0.641  70.391  1.00 22.29 ? 432  ASN B N     1 
ATOM   8862  C  CA    . ASN B 1 412 ? -26.485 -1.222  71.696  1.00 22.81 ? 432  ASN B CA    1 
ATOM   8863  C  C     . ASN B 1 412 ? -27.597 -0.882  72.671  1.00 23.40 ? 432  ASN B C     1 
ATOM   8864  O  O     . ASN B 1 412 ? -27.555 0.136   73.350  1.00 23.96 ? 432  ASN B O     1 
ATOM   8865  C  CB    . ASN B 1 412 ? -25.136 -0.705  72.217  1.00 22.54 ? 432  ASN B CB    1 
ATOM   8866  C  CG    . ASN B 1 412 ? -24.524 -1.628  73.240  1.00 22.70 ? 432  ASN B CG    1 
ATOM   8867  O  OD1   . ASN B 1 412 ? -24.479 -1.321  74.430  1.00 23.47 ? 432  ASN B OD1   1 
ATOM   8868  N  ND2   . ASN B 1 412 ? -24.063 -2.777  72.787  1.00 21.24 ? 432  ASN B ND2   1 
ATOM   8869  N  N     . SER B 1 413 ? -28.611 -1.728  72.705  1.00 24.34 ? 433  SER B N     1 
ATOM   8870  C  CA    . SER B 1 413 ? -29.783 -1.502  73.538  1.00 25.12 ? 433  SER B CA    1 
ATOM   8871  C  C     . SER B 1 413 ? -29.450 -1.619  75.016  1.00 25.88 ? 433  SER B C     1 
ATOM   8872  O  O     . SER B 1 413 ? -28.565 -2.388  75.396  1.00 25.07 ? 433  SER B O     1 
ATOM   8873  C  CB    . SER B 1 413 ? -30.846 -2.536  73.196  1.00 25.14 ? 433  SER B CB    1 
ATOM   8874  O  OG    . SER B 1 413 ? -31.943 -2.432  74.067  1.00 26.16 ? 433  SER B OG    1 
ATOM   8875  N  N     . ASN B 1 414 ? -30.164 -0.860  75.849  1.00 27.03 ? 434  ASN B N     1 
ATOM   8876  C  CA    . ASN B 1 414 ? -30.096 -1.072  77.297  1.00 28.29 ? 434  ASN B CA    1 
ATOM   8877  C  C     . ASN B 1 414 ? -31.214 -1.999  77.793  1.00 29.33 ? 434  ASN B C     1 
ATOM   8878  O  O     . ASN B 1 414 ? -31.284 -2.315  78.979  1.00 29.95 ? 434  ASN B O     1 
ATOM   8879  C  CB    . ASN B 1 414 ? -30.056 0.265   78.064  1.00 28.21 ? 434  ASN B CB    1 
ATOM   8880  C  CG    . ASN B 1 414 ? -31.387 1.012   78.063  1.00 28.19 ? 434  ASN B CG    1 
ATOM   8881  O  OD1   . ASN B 1 414 ? -32.425 0.515   77.594  1.00 26.08 ? 434  ASN B OD1   1 
ATOM   8882  N  ND2   . ASN B 1 414 ? -31.355 2.235   78.592  1.00 27.81 ? 434  ASN B ND2   1 
ATOM   8883  N  N     . PHE B 1 415 ? -32.087 -2.418  76.872  1.00 30.41 ? 435  PHE B N     1 
ATOM   8884  C  CA    . PHE B 1 415 ? -33.177 -3.363  77.152  1.00 31.11 ? 435  PHE B CA    1 
ATOM   8885  C  C     . PHE B 1 415 ? -34.195 -2.834  78.178  1.00 31.32 ? 435  PHE B C     1 
ATOM   8886  O  O     . PHE B 1 415 ? -34.955 -3.611  78.753  1.00 31.64 ? 435  PHE B O     1 
ATOM   8887  C  CB    . PHE B 1 415 ? -32.613 -4.730  77.593  1.00 31.24 ? 435  PHE B CB    1 
ATOM   8888  C  CG    . PHE B 1 415 ? -31.519 -5.244  76.699  1.00 32.12 ? 435  PHE B CG    1 
ATOM   8889  C  CD1   . PHE B 1 415 ? -30.201 -5.276  77.134  1.00 32.17 ? 435  PHE B CD1   1 
ATOM   8890  C  CD2   . PHE B 1 415 ? -31.805 -5.661  75.404  1.00 32.66 ? 435  PHE B CD2   1 
ATOM   8891  C  CE1   . PHE B 1 415 ? -29.187 -5.725  76.301  1.00 32.18 ? 435  PHE B CE1   1 
ATOM   8892  C  CE2   . PHE B 1 415 ? -30.799 -6.112  74.569  1.00 32.96 ? 435  PHE B CE2   1 
ATOM   8893  C  CZ    . PHE B 1 415 ? -29.487 -6.143  75.016  1.00 32.59 ? 435  PHE B CZ    1 
ATOM   8894  N  N     . LYS B 1 416 ? -34.195 -1.519  78.397  1.00 31.44 ? 436  LYS B N     1 
ATOM   8895  C  CA    . LYS B 1 416 ? -35.129 -0.836  79.310  1.00 31.33 ? 436  LYS B CA    1 
ATOM   8896  C  C     . LYS B 1 416 ? -35.670 0.394   78.595  1.00 30.43 ? 436  LYS B C     1 
ATOM   8897  O  O     . LYS B 1 416 ? -35.717 1.489   79.167  1.00 30.61 ? 436  LYS B O     1 
ATOM   8898  C  CB    . LYS B 1 416 ? -34.400 -0.379  80.576  1.00 31.71 ? 436  LYS B CB    1 
ATOM   8899  C  CG    . LYS B 1 416 ? -33.905 -1.493  81.469  1.00 33.98 ? 436  LYS B CG    1 
ATOM   8900  C  CD    . LYS B 1 416 ? -32.499 -1.221  82.004  1.00 36.15 ? 436  LYS B CD    1 
ATOM   8901  C  CE    . LYS B 1 416 ? -32.377 0.104   82.727  1.00 37.78 ? 436  LYS B CE    1 
ATOM   8902  N  NZ    . LYS B 1 416 ? -30.963 0.334   83.162  1.00 38.88 ? 436  LYS B NZ    1 
ATOM   8903  N  N     . GLY B 1 417 ? -36.019 0.226   77.325  1.00 29.45 ? 437  GLY B N     1 
ATOM   8904  C  CA    . GLY B 1 417 ? -36.599 1.295   76.534  1.00 28.71 ? 437  GLY B CA    1 
ATOM   8905  C  C     . GLY B 1 417 ? -35.616 2.296   75.967  1.00 28.16 ? 437  GLY B C     1 
ATOM   8906  O  O     . GLY B 1 417 ? -36.032 3.311   75.414  1.00 28.00 ? 437  GLY B O     1 
ATOM   8907  N  N     . GLY B 1 418 ? -34.319 2.017   76.067  1.00 27.65 ? 438  GLY B N     1 
ATOM   8908  C  CA    . GLY B 1 418 ? -33.306 2.941   75.567  1.00 27.12 ? 438  GLY B CA    1 
ATOM   8909  C  C     . GLY B 1 418 ? -32.046 2.283   75.042  1.00 26.70 ? 438  GLY B C     1 
ATOM   8910  O  O     . GLY B 1 418 ? -32.055 1.118   74.651  1.00 27.00 ? 438  GLY B O     1 
ATOM   8911  N  N     . PHE B 1 419 ? -30.955 3.038   75.048  1.00 26.13 ? 439  PHE B N     1 
ATOM   8912  C  CA    . PHE B 1 419 ? -29.710 2.588   74.438  1.00 25.87 ? 439  PHE B CA    1 
ATOM   8913  C  C     . PHE B 1 419 ? -28.472 3.081   75.173  1.00 25.50 ? 439  PHE B C     1 
ATOM   8914  O  O     . PHE B 1 419 ? -28.526 4.050   75.929  1.00 25.52 ? 439  PHE B O     1 
ATOM   8915  C  CB    . PHE B 1 419 ? -29.685 2.945   72.939  1.00 25.71 ? 439  PHE B CB    1 
ATOM   8916  C  CG    . PHE B 1 419 ? -29.308 4.379   72.611  1.00 26.50 ? 439  PHE B CG    1 
ATOM   8917  C  CD1   . PHE B 1 419 ? -28.483 4.640   71.519  1.00 27.15 ? 439  PHE B CD1   1 
ATOM   8918  C  CD2   . PHE B 1 419 ? -29.805 5.462   73.329  1.00 27.39 ? 439  PHE B CD2   1 
ATOM   8919  C  CE1   . PHE B 1 419 ? -28.136 5.943   71.168  1.00 27.39 ? 439  PHE B CE1   1 
ATOM   8920  C  CE2   . PHE B 1 419 ? -29.452 6.776   72.989  1.00 27.86 ? 439  PHE B CE2   1 
ATOM   8921  C  CZ    . PHE B 1 419 ? -28.619 7.013   71.907  1.00 28.02 ? 439  PHE B CZ    1 
ATOM   8922  N  N     . ASN B 1 420 ? -27.374 2.364   74.976  1.00 25.49 ? 440  ASN B N     1 
ATOM   8923  C  CA    . ASN B 1 420 ? -26.058 2.771   75.469  1.00 25.38 ? 440  ASN B CA    1 
ATOM   8924  C  C     . ASN B 1 420 ? -25.320 3.566   74.415  1.00 25.33 ? 440  ASN B C     1 
ATOM   8925  O  O     . ASN B 1 420 ? -24.584 4.503   74.741  1.00 25.58 ? 440  ASN B O     1 
ATOM   8926  C  CB    . ASN B 1 420 ? -25.233 1.552   75.846  1.00 25.15 ? 440  ASN B CB    1 
ATOM   8927  C  CG    . ASN B 1 420 ? -25.913 0.698   76.889  1.00 27.00 ? 440  ASN B CG    1 
ATOM   8928  O  OD1   . ASN B 1 420 ? -26.492 1.220   77.840  1.00 28.12 ? 440  ASN B OD1   1 
ATOM   8929  N  ND2   . ASN B 1 420 ? -25.860 -0.621  76.713  1.00 27.19 ? 440  ASN B ND2   1 
ATOM   8930  N  N     . PHE B 1 421 ? -25.486 3.150   73.156  1.00 24.76 ? 441  PHE B N     1 
ATOM   8931  C  CA    . PHE B 1 421 ? -25.035 3.915   71.998  1.00 24.41 ? 441  PHE B CA    1 
ATOM   8932  C  C     . PHE B 1 421 ? -25.573 3.315   70.703  1.00 24.02 ? 441  PHE B C     1 
ATOM   8933  O  O     . PHE B 1 421 ? -26.021 2.166   70.676  1.00 23.63 ? 441  PHE B O     1 
ATOM   8934  C  CB    . PHE B 1 421 ? -23.491 4.008   71.922  1.00 24.07 ? 441  PHE B CB    1 
ATOM   8935  C  CG    . PHE B 1 421 ? -22.810 2.686   71.719  1.00 24.68 ? 441  PHE B CG    1 
ATOM   8936  C  CD1   . PHE B 1 421 ? -22.497 1.875   72.804  1.00 24.94 ? 441  PHE B CD1   1 
ATOM   8937  C  CD2   . PHE B 1 421 ? -22.480 2.246   70.437  1.00 26.04 ? 441  PHE B CD2   1 
ATOM   8938  C  CE1   . PHE B 1 421 ? -21.886 0.655   72.614  1.00 26.02 ? 441  PHE B CE1   1 
ATOM   8939  C  CE2   . PHE B 1 421 ? -21.853 1.027   70.246  1.00 25.15 ? 441  PHE B CE2   1 
ATOM   8940  C  CZ    . PHE B 1 421 ? -21.557 0.230   71.332  1.00 25.69 ? 441  PHE B CZ    1 
ATOM   8941  N  N     . TYR B 1 422 ? -25.563 4.131   69.650  1.00 23.84 ? 442  TYR B N     1 
ATOM   8942  C  CA    . TYR B 1 422 ? -25.645 3.659   68.272  1.00 23.56 ? 442  TYR B CA    1 
ATOM   8943  C  C     . TYR B 1 422 ? -24.334 4.050   67.600  1.00 23.74 ? 442  TYR B C     1 
ATOM   8944  O  O     . TYR B 1 422 ? -23.886 5.188   67.743  1.00 24.03 ? 442  TYR B O     1 
ATOM   8945  C  CB    . TYR B 1 422 ? -26.820 4.290   67.512  1.00 23.71 ? 442  TYR B CB    1 
ATOM   8946  C  CG    . TYR B 1 422 ? -26.685 4.092   66.018  1.00 23.52 ? 442  TYR B CG    1 
ATOM   8947  C  CD1   . TYR B 1 422 ? -27.157 2.933   65.408  1.00 24.10 ? 442  TYR B CD1   1 
ATOM   8948  C  CD2   . TYR B 1 422 ? -26.030 5.033   65.225  1.00 23.66 ? 442  TYR B CD2   1 
ATOM   8949  C  CE1   . TYR B 1 422 ? -27.010 2.728   64.045  1.00 24.56 ? 442  TYR B CE1   1 
ATOM   8950  C  CE2   . TYR B 1 422 ? -25.876 4.840   63.866  1.00 24.85 ? 442  TYR B CE2   1 
ATOM   8951  C  CZ    . TYR B 1 422 ? -26.369 3.679   63.276  1.00 25.41 ? 442  TYR B CZ    1 
ATOM   8952  O  OH    . TYR B 1 422 ? -26.223 3.472   61.923  1.00 25.18 ? 442  TYR B OH    1 
ATOM   8953  N  N     . ALA B 1 423 ? -23.715 3.100   66.900  1.00 23.24 ? 443  ALA B N     1 
ATOM   8954  C  CA    . ALA B 1 423 ? -22.505 3.346   66.119  1.00 23.20 ? 443  ALA B CA    1 
ATOM   8955  C  C     . ALA B 1 423 ? -22.763 2.924   64.677  1.00 22.90 ? 443  ALA B C     1 
ATOM   8956  O  O     . ALA B 1 423 ? -23.294 1.847   64.432  1.00 22.64 ? 443  ALA B O     1 
ATOM   8957  C  CB    . ALA B 1 423 ? -21.321 2.560   66.690  1.00 22.98 ? 443  ALA B CB    1 
ATOM   8958  N  N     . GLY B 1 424 ? -22.396 3.770   63.724  1.00 22.96 ? 444  GLY B N     1 
ATOM   8959  C  CA    . GLY B 1 424 ? -22.523 3.408   62.309  1.00 23.30 ? 444  GLY B CA    1 
ATOM   8960  C  C     . GLY B 1 424 ? -21.465 4.049   61.421  1.00 23.24 ? 444  GLY B C     1 
ATOM   8961  O  O     . GLY B 1 424 ? -20.979 5.143   61.710  1.00 23.31 ? 444  GLY B O     1 
ATOM   8962  N  N     . LEU B 1 425 ? -21.109 3.350   60.344  1.00 22.75 ? 445  LEU B N     1 
ATOM   8963  C  CA    . LEU B 1 425 ? -20.243 3.885   59.305  1.00 22.35 ? 445  LEU B CA    1 
ATOM   8964  C  C     . LEU B 1 425 ? -20.947 3.748   57.945  1.00 21.98 ? 445  LEU B C     1 
ATOM   8965  O  O     . LEU B 1 425 ? -21.166 2.641   57.450  1.00 21.72 ? 445  LEU B O     1 
ATOM   8966  C  CB    . LEU B 1 425 ? -18.905 3.146   59.299  1.00 22.04 ? 445  LEU B CB    1 
ATOM   8967  C  CG    . LEU B 1 425 ? -17.937 3.531   58.170  1.00 23.06 ? 445  LEU B CG    1 
ATOM   8968  C  CD1   . LEU B 1 425 ? -17.598 5.019   58.190  1.00 22.31 ? 445  LEU B CD1   1 
ATOM   8969  C  CD2   . LEU B 1 425 ? -16.663 2.705   58.252  1.00 23.38 ? 445  LEU B CD2   1 
ATOM   8970  N  N     . LYS B 1 426 ? -21.309 4.884   57.364  1.00 21.90 ? 446  LYS B N     1 
ATOM   8971  C  CA    . LYS B 1 426 ? -21.922 4.950   56.031  1.00 22.01 ? 446  LYS B CA    1 
ATOM   8972  C  C     . LYS B 1 426 ? -21.102 4.139   55.034  1.00 21.74 ? 446  LYS B C     1 
ATOM   8973  O  O     . LYS B 1 426 ? -19.872 4.181   55.060  1.00 21.54 ? 446  LYS B O     1 
ATOM   8974  C  CB    . LYS B 1 426 ? -22.013 6.413   55.558  1.00 21.92 ? 446  LYS B CB    1 
ATOM   8975  C  CG    . LYS B 1 426 ? -22.772 6.613   54.265  1.00 22.82 ? 446  LYS B CG    1 
ATOM   8976  C  CD    . LYS B 1 426 ? -22.757 8.060   53.779  1.00 22.82 ? 446  LYS B CD    1 
ATOM   8977  C  CE    . LYS B 1 426 ? -23.833 8.269   52.724  1.00 23.66 ? 446  LYS B CE    1 
ATOM   8978  N  NZ    . LYS B 1 426 ? -23.591 9.394   51.785  1.00 24.71 ? 446  LYS B NZ    1 
ATOM   8979  N  N     . GLY B 1 427 ? -21.790 3.383   54.179  1.00 21.36 ? 447  GLY B N     1 
ATOM   8980  C  CA    . GLY B 1 427 ? -21.132 2.602   53.140  1.00 21.09 ? 447  GLY B CA    1 
ATOM   8981  C  C     . GLY B 1 427 ? -20.724 3.451   51.947  1.00 20.97 ? 447  GLY B C     1 
ATOM   8982  O  O     . GLY B 1 427 ? -21.543 4.203   51.411  1.00 20.71 ? 447  GLY B O     1 
ATOM   8983  N  N     . GLN B 1 428 ? -19.448 3.351   51.562  1.00 20.78 ? 448  GLN B N     1 
ATOM   8984  C  CA    . GLN B 1 428 ? -18.938 3.919   50.310  1.00 20.80 ? 448  GLN B CA    1 
ATOM   8985  C  C     . GLN B 1 428 ? -18.019 2.903   49.676  1.00 20.63 ? 448  GLN B C     1 
ATOM   8986  O  O     . GLN B 1 428 ? -17.440 2.072   50.375  1.00 20.79 ? 448  GLN B O     1 
ATOM   8987  C  CB    . GLN B 1 428 ? -18.117 5.198   50.542  1.00 21.04 ? 448  GLN B CB    1 
ATOM   8988  C  CG    . GLN B 1 428 ? -18.858 6.373   51.197  1.00 21.41 ? 448  GLN B CG    1 
ATOM   8989  C  CD    . GLN B 1 428 ? -19.604 7.266   50.216  1.00 22.34 ? 448  GLN B CD    1 
ATOM   8990  O  OE1   . GLN B 1 428 ? -19.676 6.993   49.014  1.00 22.09 ? 448  GLN B OE1   1 
ATOM   8991  N  NE2   . GLN B 1 428 ? -20.175 8.346   50.735  1.00 22.89 ? 448  GLN B NE2   1 
ATOM   8992  N  N     . VAL B 1 429 ? -17.882 2.973   48.353  1.00 20.41 ? 449  VAL B N     1 
ATOM   8993  C  CA    A VAL B 1 429 ? -16.921 2.144   47.620  0.60 20.34 ? 449  VAL B CA    1 
ATOM   8994  C  CA    B VAL B 1 429 ? -16.900 2.161   47.651  0.40 20.28 ? 449  VAL B CA    1 
ATOM   8995  C  C     . VAL B 1 429 ? -16.270 2.969   46.524  1.00 20.18 ? 449  VAL B C     1 
ATOM   8996  O  O     . VAL B 1 429 ? -16.890 3.874   45.991  1.00 20.06 ? 449  VAL B O     1 
ATOM   8997  C  CB    A VAL B 1 429 ? -17.584 0.902   46.970  0.60 20.32 ? 449  VAL B CB    1 
ATOM   8998  C  CB    B VAL B 1 429 ? -17.527 0.859   47.111  0.40 20.26 ? 449  VAL B CB    1 
ATOM   8999  C  CG1   A VAL B 1 429 ? -17.863 -0.172  48.017  0.60 20.71 ? 449  VAL B CG1   1 
ATOM   9000  C  CG1   B VAL B 1 429 ? -18.478 1.142   45.944  0.40 19.85 ? 449  VAL B CG1   1 
ATOM   9001  C  CG2   A VAL B 1 429 ? -18.861 1.285   46.221  0.60 19.68 ? 449  VAL B CG2   1 
ATOM   9002  C  CG2   B VAL B 1 429 ? -16.438 -0.119  46.716  0.40 20.19 ? 449  VAL B CG2   1 
ATOM   9003  N  N     . LEU B 1 430 ? -15.018 2.654   46.201  1.00 19.95 ? 450  LEU B N     1 
ATOM   9004  C  CA    . LEU B 1 430 ? -14.354 3.246   45.052  1.00 19.72 ? 450  LEU B CA    1 
ATOM   9005  C  C     . LEU B 1 430 ? -14.511 2.273   43.887  1.00 19.27 ? 450  LEU B C     1 
ATOM   9006  O  O     . LEU B 1 430 ? -14.197 1.102   44.028  1.00 19.86 ? 450  LEU B O     1 
ATOM   9007  C  CB    . LEU B 1 430 ? -12.857 3.459   45.316  1.00 20.17 ? 450  LEU B CB    1 
ATOM   9008  C  CG    . LEU B 1 430 ? -12.103 4.067   44.129  1.00 19.81 ? 450  LEU B CG    1 
ATOM   9009  C  CD1   . LEU B 1 430 ? -12.566 5.518   43.925  1.00 21.04 ? 450  LEU B CD1   1 
ATOM   9010  C  CD2   . LEU B 1 430 ? -10.591 3.985   44.319  1.00 21.40 ? 450  LEU B CD2   1 
ATOM   9011  N  N     . VAL B 1 431 ? -14.955 2.768   42.739  1.00 18.63 ? 451  VAL B N     1 
ATOM   9012  C  CA    . VAL B 1 431 ? -15.157 1.941   41.558  1.00 17.93 ? 451  VAL B CA    1 
ATOM   9013  C  C     . VAL B 1 431 ? -14.252 2.454   40.430  1.00 18.24 ? 451  VAL B C     1 
ATOM   9014  O  O     . VAL B 1 431 ? -14.246 3.651   40.123  1.00 17.77 ? 451  VAL B O     1 
ATOM   9015  C  CB    . VAL B 1 431 ? -16.615 2.008   41.074  1.00 17.83 ? 451  VAL B CB    1 
ATOM   9016  C  CG1   . VAL B 1 431 ? -16.789 1.194   39.776  1.00 18.06 ? 451  VAL B CG1   1 
ATOM   9017  C  CG2   . VAL B 1 431 ? -17.574 1.532   42.177  1.00 16.38 ? 451  VAL B CG2   1 
ATOM   9018  N  N     . LEU B 1 432 ? -13.481 1.531   39.852  1.00 18.22 ? 452  LEU B N     1 
ATOM   9019  C  CA    . LEU B 1 432 ? -12.699 1.752   38.639  1.00 18.39 ? 452  LEU B CA    1 
ATOM   9020  C  C     . LEU B 1 432 ? -13.369 0.922   37.551  1.00 17.84 ? 452  LEU B C     1 
ATOM   9021  O  O     . LEU B 1 432 ? -13.478 -0.295  37.680  1.00 18.49 ? 452  LEU B O     1 
ATOM   9022  C  CB    . LEU B 1 432 ? -11.245 1.269   38.813  1.00 18.27 ? 452  LEU B CB    1 
ATOM   9023  C  CG    . LEU B 1 432 ? -10.423 1.305   37.516  1.00 18.79 ? 452  LEU B CG    1 
ATOM   9024  C  CD1   . LEU B 1 432 ? -10.394 2.720   36.965  1.00 19.44 ? 452  LEU B CD1   1 
ATOM   9025  C  CD2   . LEU B 1 432 ? -9.013  0.783   37.691  1.00 20.87 ? 452  LEU B CD2   1 
ATOM   9026  N  N     . ARG B 1 433 ? -13.816 1.574   36.488  1.00 17.69 ? 453  ARG B N     1 
ATOM   9027  C  CA    . ARG B 1 433 ? -14.654 0.906   35.496  1.00 17.43 ? 453  ARG B CA    1 
ATOM   9028  C  C     . ARG B 1 433 ? -14.227 1.193   34.067  1.00 17.60 ? 453  ARG B C     1 
ATOM   9029  O  O     . ARG B 1 433 ? -13.825 2.308   33.734  1.00 17.56 ? 453  ARG B O     1 
ATOM   9030  C  CB    . ARG B 1 433 ? -16.105 1.339   35.684  1.00 17.20 ? 453  ARG B CB    1 
ATOM   9031  C  CG    . ARG B 1 433 ? -17.044 0.995   34.521  1.00 17.02 ? 453  ARG B CG    1 
ATOM   9032  C  CD    . ARG B 1 433 ? -18.467 1.357   34.881  1.00 17.94 ? 453  ARG B CD    1 
ATOM   9033  N  NE    . ARG B 1 433 ? -18.920 0.566   36.024  1.00 18.94 ? 453  ARG B NE    1 
ATOM   9034  C  CZ    . ARG B 1 433 ? -19.992 0.834   36.769  1.00 19.64 ? 453  ARG B CZ    1 
ATOM   9035  N  NH1   . ARG B 1 433 ? -20.759 1.894   36.521  1.00 18.94 ? 453  ARG B NH1   1 
ATOM   9036  N  NH2   . ARG B 1 433 ? -20.293 0.026   37.782  1.00 20.44 ? 453  ARG B NH2   1 
ATOM   9037  N  N     . THR B 1 434 ? -14.317 0.175   33.227  1.00 17.88 ? 454  THR B N     1 
ATOM   9038  C  CA    . THR B 1 434 ? -14.309 0.380   31.788  1.00 18.18 ? 454  THR B CA    1 
ATOM   9039  C  C     . THR B 1 434 ? -15.382 -0.536  31.196  1.00 18.26 ? 454  THR B C     1 
ATOM   9040  O  O     . THR B 1 434 ? -16.077 -1.240  31.928  1.00 18.76 ? 454  THR B O     1 
ATOM   9041  C  CB    . THR B 1 434 ? -12.902 0.106   31.169  1.00 17.87 ? 454  THR B CB    1 
ATOM   9042  O  OG1   . THR B 1 434 ? -12.907 0.489   29.792  1.00 19.27 ? 454  THR B OG1   1 
ATOM   9043  C  CG2   . THR B 1 434 ? -12.527 -1.354  31.276  1.00 16.84 ? 454  THR B CG2   1 
ATOM   9044  N  N     . THR B 1 435 ? -15.522 -0.526  29.880  1.00 18.60 ? 455  THR B N     1 
ATOM   9045  C  CA    . THR B 1 435 ? -16.449 -1.427  29.200  1.00 19.04 ? 455  THR B CA    1 
ATOM   9046  C  C     . THR B 1 435 ? -15.751 -2.053  28.006  1.00 19.72 ? 455  THR B C     1 
ATOM   9047  O  O     . THR B 1 435 ? -14.641 -1.648  27.638  1.00 20.08 ? 455  THR B O     1 
ATOM   9048  C  CB    . THR B 1 435 ? -17.690 -0.678  28.661  1.00 18.92 ? 455  THR B CB    1 
ATOM   9049  O  OG1   . THR B 1 435 ? -17.264 0.347   27.760  1.00 19.09 ? 455  THR B OG1   1 
ATOM   9050  C  CG2   . THR B 1 435 ? -18.528 -0.056  29.784  1.00 18.66 ? 455  THR B CG2   1 
ATOM   9051  N  N     . SER B 1 436 ? -16.394 -3.044  27.404  1.00 20.56 ? 456  SER B N     1 
ATOM   9052  C  CA    . SER B 1 436 ? -16.002 -3.498  26.066  1.00 21.03 ? 456  SER B CA    1 
ATOM   9053  C  C     . SER B 1 436 ? -17.230 -3.866  25.258  1.00 21.12 ? 456  SER B C     1 
ATOM   9054  O  O     . SER B 1 436 ? -18.036 -4.699  25.675  1.00 21.04 ? 456  SER B O     1 
ATOM   9055  C  CB    . SER B 1 436 ? -15.033 -4.667  26.137  1.00 21.20 ? 456  SER B CB    1 
ATOM   9056  O  OG    . SER B 1 436 ? -15.606 -5.740  26.824  1.00 23.73 ? 456  SER B OG    1 
ATOM   9057  N  N     . THR B 1 437 ? -17.374 -3.203  24.115  1.00 21.50 ? 457  THR B N     1 
ATOM   9058  C  CA    . THR B 1 437 ? -18.394 -3.513  23.142  1.00 21.69 ? 457  THR B CA    1 
ATOM   9059  C  C     . THR B 1 437 ? -17.680 -3.916  21.853  1.00 22.87 ? 457  THR B C     1 
ATOM   9060  O  O     . THR B 1 437 ? -17.270 -3.075  21.065  1.00 23.23 ? 457  THR B O     1 
ATOM   9061  C  CB    . THR B 1 437 ? -19.292 -2.279  22.885  1.00 21.61 ? 457  THR B CB    1 
ATOM   9062  O  OG1   . THR B 1 437 ? -19.681 -1.685  24.134  1.00 20.69 ? 457  THR B OG1   1 
ATOM   9063  C  CG2   . THR B 1 437 ? -20.541 -2.662  22.064  1.00 20.24 ? 457  THR B CG2   1 
ATOM   9064  N  N     . VAL B 1 438 ? -17.489 -5.203  21.634  1.00 24.19 ? 458  VAL B N     1 
ATOM   9065  C  CA    . VAL B 1 438 ? -16.888 -5.622  20.372  1.00 25.07 ? 458  VAL B CA    1 
ATOM   9066  C  C     . VAL B 1 438 ? -17.888 -5.346  19.244  1.00 25.40 ? 458  VAL B C     1 
ATOM   9067  O  O     . VAL B 1 438 ? -17.514 -4.830  18.171  1.00 26.53 ? 458  VAL B O     1 
ATOM   9068  C  CB    . VAL B 1 438 ? -16.500 -7.113  20.378  1.00 25.58 ? 458  VAL B CB    1 
ATOM   9069  N  N     . TYR B 1 439 ? -19.156 -5.644  19.503  1.00 24.54 ? 459  TYR B N     1 
ATOM   9070  C  CA    . TYR B 1 439 ? -20.168 -5.616  18.464  1.00 24.59 ? 459  TYR B CA    1 
ATOM   9071  C  C     . TYR B 1 439 ? -21.566 -5.549  19.076  1.00 23.70 ? 459  TYR B C     1 
ATOM   9072  O  O     . TYR B 1 439 ? -22.093 -4.456  19.273  1.00 24.13 ? 459  TYR B O     1 
ATOM   9073  C  CB    . TYR B 1 439 ? -19.984 -6.863  17.593  1.00 25.04 ? 459  TYR B CB    1 
ATOM   9074  C  CG    . TYR B 1 439 ? -20.788 -6.933  16.321  1.00 27.68 ? 459  TYR B CG    1 
ATOM   9075  C  CD1   . TYR B 1 439 ? -20.544 -6.052  15.274  1.00 30.45 ? 459  TYR B CD1   1 
ATOM   9076  C  CD2   . TYR B 1 439 ? -21.754 -7.924  16.135  1.00 29.38 ? 459  TYR B CD2   1 
ATOM   9077  C  CE1   . TYR B 1 439 ? -21.262 -6.137  14.077  1.00 31.28 ? 459  TYR B CE1   1 
ATOM   9078  C  CE2   . TYR B 1 439 ? -22.467 -8.023  14.948  1.00 29.86 ? 459  TYR B CE2   1 
ATOM   9079  C  CZ    . TYR B 1 439 ? -22.217 -7.125  13.926  1.00 30.66 ? 459  TYR B CZ    1 
ATOM   9080  O  OH    . TYR B 1 439 ? -22.907 -7.214  12.746  1.00 32.77 ? 459  TYR B OH    1 
ATOM   9081  N  N     . ASN B 1 440 ? -22.139 -6.701  19.415  1.00 22.77 ? 460  ASN B N     1 
ATOM   9082  C  CA    . ASN B 1 440 ? -23.525 -6.788  19.886  1.00 22.54 ? 460  ASN B CA    1 
ATOM   9083  C  C     . ASN B 1 440 ? -23.672 -6.584  21.396  1.00 21.96 ? 460  ASN B C     1 
ATOM   9084  O  O     . ASN B 1 440 ? -24.502 -5.786  21.839  1.00 21.50 ? 460  ASN B O     1 
ATOM   9085  C  CB    . ASN B 1 440 ? -24.150 -8.128  19.467  1.00 22.70 ? 460  ASN B CB    1 
ATOM   9086  C  CG    . ASN B 1 440 ? -23.375 -9.321  19.973  1.00 22.67 ? 460  ASN B CG    1 
ATOM   9087  O  OD1   . ASN B 1 440 ? -22.210 -9.484  19.643  1.00 21.95 ? 460  ASN B OD1   1 
ATOM   9088  N  ND2   . ASN B 1 440 ? -24.017 -10.159 20.790  1.00 23.14 ? 460  ASN B ND2   1 
HETATM 9089  N  N     . TPQ B 1 441 ? -22.848 -7.292  22.167  1.00 21.56 ? 461  TPQ B N     1 
HETATM 9090  C  CA    . TPQ B 1 441 ? -22.839 -7.214  23.626  1.00 21.90 ? 461  TPQ B CA    1 
HETATM 9091  C  CB    . TPQ B 1 441 ? -22.212 -8.473  24.219  1.00 22.50 ? 461  TPQ B CB    1 
HETATM 9092  C  C     . TPQ B 1 441 ? -21.940 -6.117  24.200  1.00 21.44 ? 461  TPQ B C     1 
HETATM 9093  O  O     . TPQ B 1 441 ? -20.894 -5.790  23.631  1.00 20.90 ? 461  TPQ B O     1 
HETATM 9094  C  C1    . TPQ B 1 441 ? -23.192 -9.549  24.575  1.00 24.76 ? 461  TPQ B C1    1 
HETATM 9095  C  C2    . TPQ B 1 441 ? -23.009 -10.908 24.022  1.00 24.67 ? 461  TPQ B C2    1 
HETATM 9096  O  O2    . TPQ B 1 441 ? -22.067 -11.155 23.243  0.50 24.10 ? 461  TPQ B O2    1 
HETATM 9097  C  C3    . TPQ B 1 441 ? -23.985 -11.964 24.411  1.00 26.18 ? 461  TPQ B C3    1 
HETATM 9098  C  C4    . TPQ B 1 441 ? -25.055 -11.713 25.281  1.00 25.27 ? 461  TPQ B C4    1 
HETATM 9099  O  O4    . TPQ B 1 441 ? -25.848 -12.630 25.594  1.00 20.99 ? 461  TPQ B O4    1 
HETATM 9100  C  C5    . TPQ B 1 441 ? -25.226 -10.348 25.838  1.00 27.27 ? 461  TPQ B C5    1 
HETATM 9101  O  O5    . TPQ B 1 441 ? -26.168 -10.086 26.630  0.50 27.65 ? 461  TPQ B O5    1 
HETATM 9102  C  C6    . TPQ B 1 441 ? -24.242 -9.289  25.453  1.00 27.15 ? 461  TPQ B C6    1 
ATOM   9103  N  N     . ASP B 1 442 ? -22.329 -5.603  25.366  1.00 20.98 ? 462  ASP B N     1 
ATOM   9104  C  CA    . ASP B 1 442 ? -21.508 -4.665  26.125  1.00 20.09 ? 462  ASP B CA    1 
ATOM   9105  C  C     . ASP B 1 442 ? -21.168 -5.280  27.483  1.00 19.79 ? 462  ASP B C     1 
ATOM   9106  O  O     . ASP B 1 442 ? -22.081 -5.582  28.276  1.00 19.51 ? 462  ASP B O     1 
ATOM   9107  C  CB    . ASP B 1 442 ? -22.263 -3.353  26.346  1.00 20.10 ? 462  ASP B CB    1 
ATOM   9108  C  CG    . ASP B 1 442 ? -22.659 -2.688  25.059  1.00 20.59 ? 462  ASP B CG    1 
ATOM   9109  O  OD1   . ASP B 1 442 ? -23.407 -3.330  24.285  1.00 22.37 ? 462  ASP B OD1   1 
ATOM   9110  O  OD2   . ASP B 1 442 ? -22.236 -1.526  24.818  1.00 19.69 ? 462  ASP B OD2   1 
ATOM   9111  N  N     . TYR B 1 443 ? -19.870 -5.473  27.750  1.00 19.01 ? 463  TYR B N     1 
ATOM   9112  C  CA    A TYR B 1 443 ? -19.484 -5.893  29.075  0.50 18.50 ? 463  TYR B CA    1 
ATOM   9113  C  CA    B TYR B 1 443 ? -19.347 -5.927  29.057  0.50 18.78 ? 463  TYR B CA    1 
ATOM   9114  C  C     . TYR B 1 443 ? -19.010 -4.692  29.875  1.00 18.43 ? 463  TYR B C     1 
ATOM   9115  O  O     . TYR B 1 443 ? -18.363 -3.781  29.354  1.00 18.25 ? 463  TYR B O     1 
ATOM   9116  C  CB    A TYR B 1 443 ? -18.472 -7.025  29.004  0.50 18.54 ? 463  TYR B CB    1 
ATOM   9117  C  CB    B TYR B 1 443 ? -17.998 -6.655  28.941  0.50 19.11 ? 463  TYR B CB    1 
ATOM   9118  C  CG    A TYR B 1 443 ? -19.033 -8.198  28.233  0.50 18.23 ? 463  TYR B CG    1 
ATOM   9119  C  CG    B TYR B 1 443 ? -17.932 -8.001  28.262  0.50 19.77 ? 463  TYR B CG    1 
ATOM   9120  C  CD1   A TYR B 1 443 ? -20.034 -8.990  28.769  0.50 18.16 ? 463  TYR B CD1   1 
ATOM   9121  C  CD1   B TYR B 1 443 ? -17.661 -8.104  26.908  0.50 21.17 ? 463  TYR B CD1   1 
ATOM   9122  C  CD2   A TYR B 1 443 ? -18.603 -8.476  26.949  0.50 19.47 ? 463  TYR B CD2   1 
ATOM   9123  C  CD2   B TYR B 1 443 ? -18.033 -9.170  28.995  0.50 20.59 ? 463  TYR B CD2   1 
ATOM   9124  C  CE1   A TYR B 1 443 ? -20.566 -10.043 28.060  0.50 18.20 ? 463  TYR B CE1   1 
ATOM   9125  C  CE1   B TYR B 1 443 ? -17.560 -9.340  26.296  0.50 21.45 ? 463  TYR B CE1   1 
ATOM   9126  C  CE2   A TYR B 1 443 ? -19.126 -9.532  26.236  0.50 19.15 ? 463  TYR B CE2   1 
ATOM   9127  C  CE2   B TYR B 1 443 ? -17.932 -10.404 28.396  0.50 20.61 ? 463  TYR B CE2   1 
ATOM   9128  C  CZ    A TYR B 1 443 ? -20.107 -10.313 26.796  0.50 18.24 ? 463  TYR B CZ    1 
ATOM   9129  C  CZ    B TYR B 1 443 ? -17.697 -10.485 27.051  0.50 20.83 ? 463  TYR B CZ    1 
ATOM   9130  O  OH    A TYR B 1 443 ? -20.615 -11.370 26.076  0.50 18.27 ? 463  TYR B OH    1 
ATOM   9131  O  OH    B TYR B 1 443 ? -17.602 -11.716 26.465  0.50 22.02 ? 463  TYR B OH    1 
ATOM   9132  N  N     . ILE B 1 444 ? -19.380 -4.685  31.151  1.00 17.94 ? 464  ILE B N     1 
ATOM   9133  C  CA    . ILE B 1 444 ? -19.013 -3.608  32.054  1.00 17.39 ? 464  ILE B CA    1 
ATOM   9134  C  C     . ILE B 1 444 ? -18.050 -4.227  33.058  1.00 17.26 ? 464  ILE B C     1 
ATOM   9135  O  O     . ILE B 1 444 ? -18.422 -5.147  33.786  1.00 17.50 ? 464  ILE B O     1 
ATOM   9136  C  CB    . ILE B 1 444 ? -20.257 -2.998  32.732  1.00 16.79 ? 464  ILE B CB    1 
ATOM   9137  C  CG1   . ILE B 1 444 ? -21.182 -2.410  31.661  1.00 16.90 ? 464  ILE B CG1   1 
ATOM   9138  C  CG2   . ILE B 1 444 ? -19.862 -1.918  33.720  1.00 17.35 ? 464  ILE B CG2   1 
ATOM   9139  C  CD1   . ILE B 1 444 ? -22.560 -2.048  32.140  1.00 16.20 ? 464  ILE B CD1   1 
ATOM   9140  N  N     . TRP B 1 445 ? -16.808 -3.741  33.066  1.00 17.33 ? 465  TRP B N     1 
ATOM   9141  C  CA    . TRP B 1 445 ? -15.738 -4.287  33.922  1.00 16.99 ? 465  TRP B CA    1 
ATOM   9142  C  C     . TRP B 1 445 ? -15.460 -3.360  35.100  1.00 17.42 ? 465  TRP B C     1 
ATOM   9143  O  O     . TRP B 1 445 ? -15.078 -2.211  34.889  1.00 17.67 ? 465  TRP B O     1 
ATOM   9144  C  CB    . TRP B 1 445 ? -14.451 -4.440  33.104  1.00 16.91 ? 465  TRP B CB    1 
ATOM   9145  C  CG    . TRP B 1 445 ? -14.606 -5.284  31.917  1.00 15.35 ? 465  TRP B CG    1 
ATOM   9146  C  CD1   . TRP B 1 445 ? -14.758 -4.868  30.633  1.00 16.10 ? 465  TRP B CD1   1 
ATOM   9147  C  CD2   . TRP B 1 445 ? -14.627 -6.708  31.885  1.00 15.49 ? 465  TRP B CD2   1 
ATOM   9148  N  NE1   . TRP B 1 445 ? -14.873 -5.951  29.795  1.00 16.30 ? 465  TRP B NE1   1 
ATOM   9149  C  CE2   . TRP B 1 445 ? -14.788 -7.093  30.545  1.00 16.16 ? 465  TRP B CE2   1 
ATOM   9150  C  CE3   . TRP B 1 445 ? -14.527 -7.700  32.865  1.00 16.35 ? 465  TRP B CE3   1 
ATOM   9151  C  CZ2   . TRP B 1 445 ? -14.866 -8.427  30.161  1.00 17.73 ? 465  TRP B CZ2   1 
ATOM   9152  C  CZ3   . TRP B 1 445 ? -14.603 -9.015  32.485  1.00 16.48 ? 465  TRP B CZ3   1 
ATOM   9153  C  CH2   . TRP B 1 445 ? -14.770 -9.373  31.144  1.00 16.74 ? 465  TRP B CH2   1 
ATOM   9154  N  N     . ASP B 1 446 ? -15.649 -3.859  36.326  1.00 17.85 ? 466  ASP B N     1 
ATOM   9155  C  CA    . ASP B 1 446 ? -15.416 -3.093  37.564  1.00 18.25 ? 466  ASP B CA    1 
ATOM   9156  C  C     . ASP B 1 446 ? -14.334 -3.708  38.448  1.00 18.23 ? 466  ASP B C     1 
ATOM   9157  O  O     . ASP B 1 446 ? -14.219 -4.917  38.563  1.00 17.59 ? 466  ASP B O     1 
ATOM   9158  C  CB    . ASP B 1 446 ? -16.681 -3.035  38.430  1.00 18.27 ? 466  ASP B CB    1 
ATOM   9159  C  CG    . ASP B 1 446 ? -17.868 -2.376  37.733  1.00 19.62 ? 466  ASP B CG    1 
ATOM   9160  O  OD1   . ASP B 1 446 ? -17.701 -1.785  36.652  1.00 20.22 ? 466  ASP B OD1   1 
ATOM   9161  O  OD2   . ASP B 1 446 ? -18.982 -2.424  38.302  1.00 19.00 ? 466  ASP B OD2   1 
ATOM   9162  N  N     . PHE B 1 447 ? -13.544 -2.841  39.071  1.00 19.06 ? 467  PHE B N     1 
ATOM   9163  C  CA    . PHE B 1 447 ? -12.717 -3.200  40.211  1.00 19.11 ? 467  PHE B CA    1 
ATOM   9164  C  C     . PHE B 1 447 ? -13.120 -2.233  41.314  1.00 19.23 ? 467  PHE B C     1 
ATOM   9165  O  O     . PHE B 1 447 ? -13.127 -1.015  41.126  1.00 18.77 ? 467  PHE B O     1 
ATOM   9166  C  CB    . PHE B 1 447 ? -11.235 -3.081  39.881  1.00 19.50 ? 467  PHE B CB    1 
ATOM   9167  C  CG    . PHE B 1 447 ? -10.743 -4.146  38.954  1.00 20.04 ? 467  PHE B CG    1 
ATOM   9168  C  CD1   . PHE B 1 447 ? -10.329 -3.838  37.669  1.00 21.90 ? 467  PHE B CD1   1 
ATOM   9169  C  CD2   . PHE B 1 447 ? -10.706 -5.468  39.367  1.00 20.79 ? 467  PHE B CD2   1 
ATOM   9170  C  CE1   . PHE B 1 447 ? -9.872  -4.844  36.807  1.00 22.05 ? 467  PHE B CE1   1 
ATOM   9171  C  CE2   . PHE B 1 447 ? -10.265 -6.466  38.522  1.00 21.25 ? 467  PHE B CE2   1 
ATOM   9172  C  CZ    . PHE B 1 447 ? -9.846  -6.157  37.241  1.00 21.83 ? 467  PHE B CZ    1 
ATOM   9173  N  N     . ILE B 1 448 ? -13.480 -2.796  42.456  1.00 19.43 ? 468  ILE B N     1 
ATOM   9174  C  CA    . ILE B 1 448 ? -14.223 -2.088  43.473  1.00 20.04 ? 468  ILE B CA    1 
ATOM   9175  C  C     . ILE B 1 448 ? -13.439 -2.217  44.758  1.00 20.10 ? 468  ILE B C     1 
ATOM   9176  O  O     . ILE B 1 448 ? -13.005 -3.323  45.094  1.00 20.20 ? 468  ILE B O     1 
ATOM   9177  C  CB    . ILE B 1 448 ? -15.628 -2.733  43.629  1.00 20.19 ? 468  ILE B CB    1 
ATOM   9178  C  CG1   . ILE B 1 448 ? -16.427 -2.583  42.329  1.00 21.31 ? 468  ILE B CG1   1 
ATOM   9179  C  CG2   . ILE B 1 448 ? -16.395 -2.105  44.735  1.00 20.62 ? 468  ILE B CG2   1 
ATOM   9180  C  CD1   . ILE B 1 448 ? -17.598 -3.554  42.235  1.00 21.99 ? 468  ILE B CD1   1 
ATOM   9181  N  N     . PHE B 1 449 ? -13.242 -1.095  45.453  1.00 20.01 ? 469  PHE B N     1 
ATOM   9182  C  CA    . PHE B 1 449 ? -12.411 -1.056  46.642  1.00 20.53 ? 469  PHE B CA    1 
ATOM   9183  C  C     . PHE B 1 449 ? -13.202 -0.499  47.823  1.00 20.68 ? 469  PHE B C     1 
ATOM   9184  O  O     . PHE B 1 449 ? -13.651 0.649   47.798  1.00 20.56 ? 469  PHE B O     1 
ATOM   9185  C  CB    . PHE B 1 449 ? -11.154 -0.208  46.400  1.00 20.95 ? 469  PHE B CB    1 
ATOM   9186  C  CG    . PHE B 1 449 ? -10.356 -0.632  45.193  1.00 20.60 ? 469  PHE B CG    1 
ATOM   9187  C  CD1   . PHE B 1 449 ? -10.716 -0.210  43.925  1.00 21.17 ? 469  PHE B CD1   1 
ATOM   9188  C  CD2   . PHE B 1 449 ? -9.244  -1.457  45.331  1.00 21.62 ? 469  PHE B CD2   1 
ATOM   9189  C  CE1   . PHE B 1 449 ? -9.982  -0.602  42.794  1.00 22.36 ? 469  PHE B CE1   1 
ATOM   9190  C  CE2   . PHE B 1 449 ? -8.491  -1.851  44.207  1.00 20.97 ? 469  PHE B CE2   1 
ATOM   9191  C  CZ    . PHE B 1 449 ? -8.867  -1.433  42.941  1.00 21.41 ? 469  PHE B CZ    1 
ATOM   9192  N  N     . TYR B 1 450 ? -13.378 -1.330  48.849  1.00 20.76 ? 470  TYR B N     1 
ATOM   9193  C  CA    . TYR B 1 450 ? -14.137 -0.946  50.036  1.00 20.84 ? 470  TYR B CA    1 
ATOM   9194  C  C     . TYR B 1 450 ? -13.159 -0.377  51.051  1.00 20.98 ? 470  TYR B C     1 
ATOM   9195  O  O     . TYR B 1 450 ? -11.984 -0.768  51.047  1.00 20.97 ? 470  TYR B O     1 
ATOM   9196  C  CB    . TYR B 1 450 ? -14.844 -2.150  50.649  1.00 20.84 ? 470  TYR B CB    1 
ATOM   9197  C  CG    . TYR B 1 450 ? -15.933 -2.772  49.805  1.00 21.83 ? 470  TYR B CG    1 
ATOM   9198  C  CD1   . TYR B 1 450 ? -15.626 -3.542  48.693  1.00 23.44 ? 470  TYR B CD1   1 
ATOM   9199  C  CD2   . TYR B 1 450 ? -17.272 -2.615  50.144  1.00 23.09 ? 470  TYR B CD2   1 
ATOM   9200  C  CE1   . TYR B 1 450 ? -16.631 -4.118  47.915  1.00 25.01 ? 470  TYR B CE1   1 
ATOM   9201  C  CE2   . TYR B 1 450 ? -18.279 -3.197  49.393  1.00 24.26 ? 470  TYR B CE2   1 
ATOM   9202  C  CZ    . TYR B 1 450 ? -17.950 -3.951  48.279  1.00 24.97 ? 470  TYR B CZ    1 
ATOM   9203  O  OH    . TYR B 1 450 ? -18.938 -4.520  47.522  1.00 26.59 ? 470  TYR B OH    1 
ATOM   9204  N  N     . PRO B 1 451 ? -13.635 0.515   51.949  1.00 21.03 ? 471  PRO B N     1 
ATOM   9205  C  CA    . PRO B 1 451 ? -12.759 1.137   52.953  1.00 21.01 ? 471  PRO B CA    1 
ATOM   9206  C  C     . PRO B 1 451 ? -12.136 0.192   53.984  1.00 20.99 ? 471  PRO B C     1 
ATOM   9207  O  O     . PRO B 1 451 ? -11.206 0.604   54.685  1.00 20.97 ? 471  PRO B O     1 
ATOM   9208  C  CB    . PRO B 1 451 ? -13.680 2.142   53.658  1.00 20.86 ? 471  PRO B CB    1 
ATOM   9209  C  CG    . PRO B 1 451 ? -14.742 2.436   52.681  1.00 21.20 ? 471  PRO B CG    1 
ATOM   9210  C  CD    . PRO B 1 451 ? -14.970 1.142   51.941  1.00 21.04 ? 471  PRO B CD    1 
ATOM   9211  N  N     . ASN B 1 452 ? -12.649 -1.037  54.088  1.00 21.00 ? 472  ASN B N     1 
ATOM   9212  C  CA    . ASN B 1 452 ? -12.120 -2.033  55.030  1.00 21.00 ? 472  ASN B CA    1 
ATOM   9213  C  C     . ASN B 1 452 ? -11.174 -3.053  54.389  1.00 20.84 ? 472  ASN B C     1 
ATOM   9214  O  O     . ASN B 1 452 ? -11.029 -4.165  54.881  1.00 21.08 ? 472  ASN B O     1 
ATOM   9215  C  CB    . ASN B 1 452 ? -13.273 -2.769  55.721  1.00 20.77 ? 472  ASN B CB    1 
ATOM   9216  C  CG    . ASN B 1 452 ? -14.080 -3.604  54.763  1.00 21.13 ? 472  ASN B CG    1 
ATOM   9217  O  OD1   . ASN B 1 452 ? -14.008 -3.416  53.538  1.00 19.21 ? 472  ASN B OD1   1 
ATOM   9218  N  ND2   . ASN B 1 452 ? -14.866 -4.531  55.307  1.00 20.37 ? 472  ASN B ND2   1 
ATOM   9219  N  N     . GLY B 1 453 ? -10.548 -2.682  53.276  1.00 21.29 ? 473  GLY B N     1 
ATOM   9220  C  CA    . GLY B 1 453 ? -9.535  -3.528  52.638  1.00 20.99 ? 473  GLY B CA    1 
ATOM   9221  C  C     . GLY B 1 453 ? -10.067 -4.640  51.762  1.00 20.96 ? 473  GLY B C     1 
ATOM   9222  O  O     . GLY B 1 453 ? -9.294  -5.452  51.262  1.00 20.88 ? 473  GLY B O     1 
ATOM   9223  N  N     . VAL B 1 454 ? -11.383 -4.700  51.588  1.00 21.00 ? 474  VAL B N     1 
ATOM   9224  C  CA    . VAL B 1 454 ? -11.986 -5.692  50.706  1.00 21.24 ? 474  VAL B CA    1 
ATOM   9225  C  C     . VAL B 1 454 ? -12.020 -5.122  49.290  1.00 21.44 ? 474  VAL B C     1 
ATOM   9226  O  O     . VAL B 1 454 ? -12.492 -4.010  49.095  1.00 21.68 ? 474  VAL B O     1 
ATOM   9227  C  CB    . VAL B 1 454 ? -13.415 -6.059  51.164  1.00 21.54 ? 474  VAL B CB    1 
ATOM   9228  C  CG1   . VAL B 1 454 ? -14.114 -6.998  50.133  1.00 20.95 ? 474  VAL B CG1   1 
ATOM   9229  C  CG2   . VAL B 1 454 ? -13.371 -6.697  52.553  1.00 20.90 ? 474  VAL B CG2   1 
ATOM   9230  N  N     . MET B 1 455 ? -11.500 -5.861  48.315  1.00 21.82 ? 475  MET B N     1 
ATOM   9231  C  CA    . MET B 1 455 ? -11.659 -5.468  46.911  1.00 22.69 ? 475  MET B CA    1 
ATOM   9232  C  C     . MET B 1 455 ? -12.426 -6.523  46.138  1.00 22.35 ? 475  MET B C     1 
ATOM   9233  O  O     . MET B 1 455 ? -12.415 -7.694  46.475  1.00 22.84 ? 475  MET B O     1 
ATOM   9234  C  CB    . MET B 1 455 ? -10.323 -5.122  46.224  1.00 22.92 ? 475  MET B CB    1 
ATOM   9235  C  CG    . MET B 1 455 ? -9.504  -6.267  45.666  1.00 25.65 ? 475  MET B CG    1 
ATOM   9236  S  SD    . MET B 1 455 ? -8.336  -5.731  44.341  1.00 30.06 ? 475  MET B SD    1 
ATOM   9237  C  CE    . MET B 1 455 ? -9.359  -5.722  42.885  1.00 29.80 ? 475  MET B CE    1 
ATOM   9238  N  N     . GLU B 1 456 ? -13.095 -6.086  45.090  1.00 22.45 ? 476  GLU B N     1 
ATOM   9239  C  CA    . GLU B 1 456 ? -13.996 -6.951  44.350  1.00 22.24 ? 476  GLU B CA    1 
ATOM   9240  C  C     . GLU B 1 456 ? -13.795 -6.743  42.851  1.00 21.82 ? 476  GLU B C     1 
ATOM   9241  O  O     . GLU B 1 456 ? -13.602 -5.618  42.394  1.00 21.54 ? 476  GLU B O     1 
ATOM   9242  C  CB    . GLU B 1 456 ? -15.436 -6.637  44.766  1.00 22.21 ? 476  GLU B CB    1 
ATOM   9243  C  CG    . GLU B 1 456 ? -16.509 -7.428  44.042  1.00 22.94 ? 476  GLU B CG    1 
ATOM   9244  C  CD    . GLU B 1 456 ? -17.914 -7.099  44.537  1.00 23.89 ? 476  GLU B CD    1 
ATOM   9245  O  OE1   . GLU B 1 456 ? -18.070 -6.151  45.329  1.00 24.18 ? 476  GLU B OE1   1 
ATOM   9246  O  OE2   . GLU B 1 456 ? -18.868 -7.780  44.110  1.00 24.49 ? 476  GLU B OE2   1 
ATOM   9247  N  N     . ALA B 1 457 ? -13.818 -7.837  42.096  1.00 21.35 ? 477  ALA B N     1 
ATOM   9248  C  CA    . ALA B 1 457 ? -13.873 -7.759  40.646  1.00 21.26 ? 477  ALA B CA    1 
ATOM   9249  C  C     . ALA B 1 457 ? -15.295 -8.096  40.212  1.00 21.43 ? 477  ALA B C     1 
ATOM   9250  O  O     . ALA B 1 457 ? -15.950 -8.939  40.816  1.00 21.18 ? 477  ALA B O     1 
ATOM   9251  C  CB    . ALA B 1 457 ? -12.884 -8.719  40.022  1.00 20.91 ? 477  ALA B CB    1 
ATOM   9252  N  N     . LYS B 1 458 ? -15.771 -7.426  39.172  1.00 21.87 ? 478  LYS B N     1 
ATOM   9253  C  CA    . LYS B 1 458 ? -17.110 -7.679  38.669  1.00 22.29 ? 478  LYS B CA    1 
ATOM   9254  C  C     . LYS B 1 458 ? -17.193 -7.467  37.159  1.00 21.99 ? 478  LYS B C     1 
ATOM   9255  O  O     . LYS B 1 458 ? -16.587 -6.537  36.618  1.00 21.50 ? 478  LYS B O     1 
ATOM   9256  C  CB    . LYS B 1 458 ? -18.100 -6.764  39.390  1.00 22.75 ? 478  LYS B CB    1 
ATOM   9257  C  CG    . LYS B 1 458 ? -19.514 -7.250  39.396  1.00 24.70 ? 478  LYS B CG    1 
ATOM   9258  C  CD    . LYS B 1 458 ? -20.442 -6.264  40.103  1.00 26.58 ? 478  LYS B CD    1 
ATOM   9259  C  CE    . LYS B 1 458 ? -20.199 -6.175  41.580  1.00 28.45 ? 478  LYS B CE    1 
ATOM   9260  N  NZ    . LYS B 1 458 ? -21.301 -5.402  42.264  1.00 29.90 ? 478  LYS B NZ    1 
ATOM   9261  N  N     . MET B 1 459 ? -17.930 -8.355  36.489  1.00 21.80 ? 479  MET B N     1 
ATOM   9262  C  CA    . MET B 1 459 ? -18.329 -8.163  35.102  1.00 21.45 ? 479  MET B CA    1 
ATOM   9263  C  C     . MET B 1 459 ? -19.859 -8.150  35.051  1.00 21.00 ? 479  MET B C     1 
ATOM   9264  O  O     . MET B 1 459 ? -20.491 -9.003  35.665  1.00 20.57 ? 479  MET B O     1 
ATOM   9265  C  CB    . MET B 1 459 ? -17.767 -9.289  34.237  1.00 21.99 ? 479  MET B CB    1 
ATOM   9266  C  CG    . MET B 1 459 ? -18.095 -9.185  32.752  1.00 23.34 ? 479  MET B CG    1 
ATOM   9267  S  SD    . MET B 1 459 ? -19.708 -9.895  32.343  1.00 29.10 ? 479  MET B SD    1 
ATOM   9268  C  CE    . MET B 1 459 ? -19.371 -11.653 32.336  1.00 27.46 ? 479  MET B CE    1 
ATOM   9269  N  N     . HIS B 1 460 ? -20.442 -7.180  34.336  1.00 20.21 ? 480  HIS B N     1 
ATOM   9270  C  CA    . HIS B 1 460 ? -21.884 -7.172  34.031  1.00 19.89 ? 480  HIS B CA    1 
ATOM   9271  C  C     . HIS B 1 460 ? -22.086 -7.293  32.531  1.00 19.40 ? 480  HIS B C     1 
ATOM   9272  O  O     . HIS B 1 460 ? -21.380 -6.655  31.773  1.00 19.99 ? 480  HIS B O     1 
ATOM   9273  C  CB    . HIS B 1 460 ? -22.570 -5.861  34.460  1.00 19.67 ? 480  HIS B CB    1 
ATOM   9274  C  CG    . HIS B 1 460 ? -22.093 -5.304  35.761  1.00 19.65 ? 480  HIS B CG    1 
ATOM   9275  N  ND1   . HIS B 1 460 ? -22.843 -5.375  36.914  1.00 18.88 ? 480  HIS B ND1   1 
ATOM   9276  C  CD2   . HIS B 1 460 ? -20.962 -4.631  36.086  1.00 19.21 ? 480  HIS B CD2   1 
ATOM   9277  C  CE1   . HIS B 1 460 ? -22.189 -4.779  37.896  1.00 20.11 ? 480  HIS B CE1   1 
ATOM   9278  N  NE2   . HIS B 1 460 ? -21.043 -4.325  37.422  1.00 19.51 ? 480  HIS B NE2   1 
ATOM   9279  N  N     . ALA B 1 461 ? -23.077 -8.067  32.108  1.00 18.97 ? 481  ALA B N     1 
ATOM   9280  C  CA    . ALA B 1 461 ? -23.405 -8.201  30.701  1.00 18.70 ? 481  ALA B CA    1 
ATOM   9281  C  C     . ALA B 1 461 ? -24.670 -7.409  30.382  1.00 18.72 ? 481  ALA B C     1 
ATOM   9282  O  O     . ALA B 1 461 ? -25.676 -7.490  31.100  1.00 18.30 ? 481  ALA B O     1 
ATOM   9283  C  CB    . ALA B 1 461 ? -23.604 -9.659  30.340  1.00 18.56 ? 481  ALA B CB    1 
ATOM   9284  N  N     . THR B 1 462 ? -24.599 -6.630  29.306  1.00 18.61 ? 482  THR B N     1 
ATOM   9285  C  CA    . THR B 1 462 ? -25.772 -5.975  28.740  1.00 18.36 ? 482  THR B CA    1 
ATOM   9286  C  C     . THR B 1 462 ? -25.588 -5.874  27.213  1.00 18.80 ? 482  THR B C     1 
ATOM   9287  O  O     . THR B 1 462 ? -24.786 -6.617  26.636  1.00 19.17 ? 482  THR B O     1 
ATOM   9288  C  CB    . THR B 1 462 ? -26.059 -4.621  29.437  1.00 18.38 ? 482  THR B CB    1 
ATOM   9289  O  OG1   . THR B 1 462 ? -27.247 -4.035  28.890  1.00 17.96 ? 482  THR B OG1   1 
ATOM   9290  C  CG2   . THR B 1 462 ? -24.874 -3.647  29.309  1.00 17.20 ? 482  THR B CG2   1 
ATOM   9291  N  N     . GLY B 1 463 ? -26.316 -4.986  26.551  1.00 18.55 ? 483  GLY B N     1 
ATOM   9292  C  CA    . GLY B 1 463 ? -26.284 -4.925  25.086  1.00 18.45 ? 483  GLY B CA    1 
ATOM   9293  C  C     . GLY B 1 463 ? -27.141 -5.994  24.423  1.00 18.25 ? 483  GLY B C     1 
ATOM   9294  O  O     . GLY B 1 463 ? -28.054 -6.536  25.049  1.00 17.79 ? 483  GLY B O     1 
ATOM   9295  N  N     . TYR B 1 464 ? -26.836 -6.307  23.162  1.00 18.09 ? 484  TYR B N     1 
ATOM   9296  C  CA    . TYR B 1 464 ? -27.668 -7.214  22.359  1.00 18.29 ? 484  TYR B CA    1 
ATOM   9297  C  C     . TYR B 1 464 ? -27.140 -8.640  22.376  1.00 18.36 ? 484  TYR B C     1 
ATOM   9298  O  O     . TYR B 1 464 ? -25.924 -8.865  22.261  1.00 18.59 ? 484  TYR B O     1 
ATOM   9299  C  CB    . TYR B 1 464 ? -27.721 -6.755  20.903  1.00 18.39 ? 484  TYR B CB    1 
ATOM   9300  C  CG    . TYR B 1 464 ? -28.491 -5.468  20.653  1.00 18.70 ? 484  TYR B CG    1 
ATOM   9301  C  CD1   . TYR B 1 464 ? -27.862 -4.233  20.724  1.00 18.58 ? 484  TYR B CD1   1 
ATOM   9302  C  CD2   . TYR B 1 464 ? -29.843 -5.497  20.317  1.00 17.44 ? 484  TYR B CD2   1 
ATOM   9303  C  CE1   . TYR B 1 464 ? -28.561 -3.059  20.486  1.00 18.42 ? 484  TYR B CE1   1 
ATOM   9304  C  CE2   . TYR B 1 464 ? -30.550 -4.335  20.081  1.00 17.06 ? 484  TYR B CE2   1 
ATOM   9305  C  CZ    . TYR B 1 464 ? -29.904 -3.120  20.155  1.00 18.33 ? 484  TYR B CZ    1 
ATOM   9306  O  OH    . TYR B 1 464 ? -30.596 -1.966  19.913  1.00 17.46 ? 484  TYR B OH    1 
ATOM   9307  N  N     . VAL B 1 465 ? -28.059 -9.598  22.477  1.00 18.10 ? 485  VAL B N     1 
ATOM   9308  C  CA    . VAL B 1 465 ? -27.708 -11.015 22.398  1.00 18.09 ? 485  VAL B CA    1 
ATOM   9309  C  C     . VAL B 1 465 ? -27.284 -11.439 20.991  1.00 18.59 ? 485  VAL B C     1 
ATOM   9310  O  O     . VAL B 1 465 ? -27.653 -10.809 19.992  1.00 17.91 ? 485  VAL B O     1 
ATOM   9311  C  CB    . VAL B 1 465 ? -28.890 -11.943 22.820  1.00 18.33 ? 485  VAL B CB    1 
ATOM   9312  C  CG1   . VAL B 1 465 ? -29.221 -11.755 24.297  1.00 17.11 ? 485  VAL B CG1   1 
ATOM   9313  C  CG2   . VAL B 1 465 ? -30.126 -11.735 21.913  1.00 17.61 ? 485  VAL B CG2   1 
ATOM   9314  N  N     . HIS B 1 466 ? -26.508 -12.521 20.937  1.00 18.94 ? 486  HIS B N     1 
ATOM   9315  C  CA    . HIS B 1 466 ? -26.148 -13.181 19.686  1.00 19.40 ? 486  HIS B CA    1 
ATOM   9316  C  C     . HIS B 1 466 ? -27.319 -14.081 19.297  1.00 19.62 ? 486  HIS B C     1 
ATOM   9317  O  O     . HIS B 1 466 ? -27.683 -14.985 20.040  1.00 20.36 ? 486  HIS B O     1 
ATOM   9318  C  CB    . HIS B 1 466 ? -24.872 -13.991 19.887  1.00 19.17 ? 486  HIS B CB    1 
ATOM   9319  C  CG    . HIS B 1 466 ? -24.337 -14.621 18.640  1.00 19.24 ? 486  HIS B CG    1 
ATOM   9320  N  ND1   . HIS B 1 466 ? -24.068 -13.899 17.498  1.00 18.80 ? 486  HIS B ND1   1 
ATOM   9321  C  CD2   . HIS B 1 466 ? -23.976 -15.902 18.374  1.00 18.63 ? 486  HIS B CD2   1 
ATOM   9322  C  CE1   . HIS B 1 466 ? -23.579 -14.710 16.575  1.00 19.41 ? 486  HIS B CE1   1 
ATOM   9323  N  NE2   . HIS B 1 466 ? -23.512 -15.931 17.082  1.00 19.16 ? 486  HIS B NE2   1 
ATOM   9324  N  N     . ALA B 1 467 ? -27.912 -13.813 18.140  1.00 20.00 ? 487  ALA B N     1 
ATOM   9325  C  CA    . ALA B 1 467 ? -29.200 -14.400 17.769  1.00 20.11 ? 487  ALA B CA    1 
ATOM   9326  C  C     . ALA B 1 467 ? -29.224 -14.864 16.314  1.00 20.32 ? 487  ALA B C     1 
ATOM   9327  O  O     . ALA B 1 467 ? -28.476 -14.361 15.475  1.00 20.88 ? 487  ALA B O     1 
ATOM   9328  C  CB    . ALA B 1 467 ? -30.334 -13.385 18.025  1.00 19.47 ? 487  ALA B CB    1 
ATOM   9329  N  N     . THR B 1 468 ? -30.104 -15.817 16.024  1.00 20.54 ? 488  THR B N     1 
ATOM   9330  C  CA    . THR B 1 468 ? -30.221 -16.400 14.689  1.00 20.43 ? 488  THR B CA    1 
ATOM   9331  C  C     . THR B 1 468 ? -31.697 -16.525 14.276  1.00 20.76 ? 488  THR B C     1 
ATOM   9332  O  O     . THR B 1 468 ? -32.606 -16.223 15.067  1.00 20.01 ? 488  THR B O     1 
ATOM   9333  C  CB    . THR B 1 468 ? -29.548 -17.787 14.656  1.00 20.61 ? 488  THR B CB    1 
ATOM   9334  O  OG1   . THR B 1 468 ? -30.071 -18.594 15.724  1.00 19.02 ? 488  THR B OG1   1 
ATOM   9335  C  CG2   . THR B 1 468 ? -28.031 -17.655 14.809  1.00 20.13 ? 488  THR B CG2   1 
ATOM   9336  N  N     . PHE B 1 469 ? -31.921 -16.978 13.045  1.00 20.97 ? 489  PHE B N     1 
ATOM   9337  C  CA    . PHE B 1 469 ? -33.257 -17.010 12.446  1.00 21.46 ? 489  PHE B CA    1 
ATOM   9338  C  C     . PHE B 1 469 ? -34.116 -18.106 13.051  1.00 21.52 ? 489  PHE B C     1 
ATOM   9339  O  O     . PHE B 1 469 ? -33.661 -19.235 13.204  1.00 21.31 ? 489  PHE B O     1 
ATOM   9340  C  CB    . PHE B 1 469 ? -33.137 -17.236 10.940  1.00 21.70 ? 489  PHE B CB    1 
ATOM   9341  C  CG    . PHE B 1 469 ? -34.443 -17.149 10.196  1.00 22.76 ? 489  PHE B CG    1 
ATOM   9342  C  CD1   . PHE B 1 469 ? -35.057 -15.928 9.986   1.00 22.90 ? 489  PHE B CD1   1 
ATOM   9343  C  CD2   . PHE B 1 469 ? -35.032 -18.287 9.668   1.00 24.32 ? 489  PHE B CD2   1 
ATOM   9344  C  CE1   . PHE B 1 469 ? -36.247 -15.843 9.279   1.00 23.89 ? 489  PHE B CE1   1 
ATOM   9345  C  CE2   . PHE B 1 469 ? -36.233 -18.208 8.965   1.00 24.39 ? 489  PHE B CE2   1 
ATOM   9346  C  CZ    . PHE B 1 469 ? -36.839 -16.993 8.776   1.00 23.37 ? 489  PHE B CZ    1 
ATOM   9347  N  N     . TYR B 1 470 ? -35.363 -17.772 13.380  1.00 22.11 ? 490  TYR B N     1 
ATOM   9348  C  CA    . TYR B 1 470 ? -36.296 -18.740 13.947  1.00 22.52 ? 490  TYR B CA    1 
ATOM   9349  C  C     . TYR B 1 470 ? -36.707 -19.843 12.969  1.00 23.08 ? 490  TYR B C     1 
ATOM   9350  O  O     . TYR B 1 470 ? -37.178 -19.558 11.869  1.00 23.17 ? 490  TYR B O     1 
ATOM   9351  C  CB    . TYR B 1 470 ? -37.585 -18.068 14.445  1.00 22.66 ? 490  TYR B CB    1 
ATOM   9352  C  CG    . TYR B 1 470 ? -38.615 -19.107 14.837  1.00 22.41 ? 490  TYR B CG    1 
ATOM   9353  C  CD1   . TYR B 1 470 ? -39.664 -19.435 13.988  1.00 23.15 ? 490  TYR B CD1   1 
ATOM   9354  C  CD2   . TYR B 1 470 ? -38.478 -19.824 16.021  1.00 22.38 ? 490  TYR B CD2   1 
ATOM   9355  C  CE1   . TYR B 1 470 ? -40.582 -20.427 14.331  1.00 23.59 ? 490  TYR B CE1   1 
ATOM   9356  C  CE2   . TYR B 1 470 ? -39.381 -20.806 16.375  1.00 23.30 ? 490  TYR B CE2   1 
ATOM   9357  C  CZ    . TYR B 1 470 ? -40.438 -21.097 15.526  1.00 24.06 ? 490  TYR B CZ    1 
ATOM   9358  O  OH    . TYR B 1 470 ? -41.330 -22.070 15.879  1.00 25.72 ? 490  TYR B OH    1 
ATOM   9359  N  N     . THR B 1 471 ? -36.515 -21.092 13.390  1.00 23.52 ? 491  THR B N     1 
ATOM   9360  C  CA    . THR B 1 471 ? -37.279 -22.241 12.878  1.00 24.48 ? 491  THR B CA    1 
ATOM   9361  C  C     . THR B 1 471 ? -37.665 -23.085 14.095  1.00 25.02 ? 491  THR B C     1 
ATOM   9362  O  O     . THR B 1 471 ? -37.021 -22.967 15.131  1.00 24.98 ? 491  THR B O     1 
ATOM   9363  C  CB    . THR B 1 471 ? -36.475 -23.144 11.900  1.00 24.32 ? 491  THR B CB    1 
ATOM   9364  O  OG1   . THR B 1 471 ? -35.501 -23.900 12.632  1.00 23.70 ? 491  THR B OG1   1 
ATOM   9365  C  CG2   . THR B 1 471 ? -35.794 -22.332 10.805  1.00 23.74 ? 491  THR B CG2   1 
ATOM   9366  N  N     . PRO B 1 472 ? -38.693 -23.953 13.975  1.00 25.94 ? 492  PRO B N     1 
ATOM   9367  C  CA    . PRO B 1 472 ? -39.055 -24.839 15.097  1.00 26.33 ? 492  PRO B CA    1 
ATOM   9368  C  C     . PRO B 1 472 ? -37.865 -25.604 15.695  1.00 26.77 ? 492  PRO B C     1 
ATOM   9369  O  O     . PRO B 1 472 ? -37.774 -25.751 16.916  1.00 26.57 ? 492  PRO B O     1 
ATOM   9370  C  CB    . PRO B 1 472 ? -40.063 -25.803 14.467  1.00 26.37 ? 492  PRO B CB    1 
ATOM   9371  C  CG    . PRO B 1 472 ? -40.732 -24.967 13.397  1.00 26.54 ? 492  PRO B CG    1 
ATOM   9372  C  CD    . PRO B 1 472 ? -39.611 -24.116 12.832  1.00 26.12 ? 492  PRO B CD    1 
ATOM   9373  N  N     . GLU B 1 473 ? -36.948 -26.045 14.835  1.00 27.35 ? 493  GLU B N     1 
ATOM   9374  C  CA    . GLU B 1 473 ? -35.791 -26.835 15.255  1.00 28.03 ? 493  GLU B CA    1 
ATOM   9375  C  C     . GLU B 1 473 ? -34.883 -26.082 16.211  1.00 27.53 ? 493  GLU B C     1 
ATOM   9376  O  O     . GLU B 1 473 ? -34.183 -26.687 17.032  1.00 28.39 ? 493  GLU B O     1 
ATOM   9377  C  CB    . GLU B 1 473 ? -34.973 -27.269 14.042  1.00 28.83 ? 493  GLU B CB    1 
ATOM   9378  C  CG    . GLU B 1 473 ? -35.529 -28.473 13.294  1.00 31.57 ? 493  GLU B CG    1 
ATOM   9379  C  CD    . GLU B 1 473 ? -36.748 -28.170 12.425  1.00 35.36 ? 493  GLU B CD    1 
ATOM   9380  O  OE1   . GLU B 1 473 ? -37.154 -26.994 12.277  1.00 34.97 ? 493  GLU B OE1   1 
ATOM   9381  O  OE2   . GLU B 1 473 ? -37.303 -29.145 11.874  1.00 39.58 ? 493  GLU B OE2   1 
ATOM   9382  N  N     . GLY B 1 474 ? -34.885 -24.760 16.099  1.00 26.78 ? 494  GLY B N     1 
ATOM   9383  C  CA    . GLY B 1 474 ? -34.095 -23.914 16.976  1.00 26.19 ? 494  GLY B CA    1 
ATOM   9384  C  C     . GLY B 1 474 ? -34.465 -23.974 18.440  1.00 25.33 ? 494  GLY B C     1 
ATOM   9385  O  O     . GLY B 1 474 ? -33.631 -23.675 19.295  1.00 25.36 ? 494  GLY B O     1 
ATOM   9386  N  N     . LEU B 1 475 ? -35.699 -24.365 18.742  1.00 24.13 ? 495  LEU B N     1 
ATOM   9387  C  CA    . LEU B 1 475 ? -36.163 -24.397 20.130  1.00 23.63 ? 495  LEU B CA    1 
ATOM   9388  C  C     . LEU B 1 475 ? -35.390 -25.421 20.992  1.00 23.06 ? 495  LEU B C     1 
ATOM   9389  O  O     . LEU B 1 475 ? -35.442 -25.377 22.221  1.00 22.47 ? 495  LEU B O     1 
ATOM   9390  C  CB    . LEU B 1 475 ? -37.680 -24.645 20.177  1.00 23.39 ? 495  LEU B CB    1 
ATOM   9391  C  CG    . LEU B 1 475 ? -38.538 -23.550 19.521  1.00 24.16 ? 495  LEU B CG    1 
ATOM   9392  C  CD1   . LEU B 1 475 ? -40.055 -23.850 19.627  1.00 23.81 ? 495  LEU B CD1   1 
ATOM   9393  C  CD2   . LEU B 1 475 ? -38.222 -22.184 20.139  1.00 24.15 ? 495  LEU B CD2   1 
ATOM   9394  N  N     . ARG B 1 476 ? -34.677 -26.335 20.340  1.00 23.01 ? 496  ARG B N     1 
ATOM   9395  C  CA    . ARG B 1 476 ? -33.742 -27.231 21.017  1.00 23.02 ? 496  ARG B CA    1 
ATOM   9396  C  C     . ARG B 1 476 ? -32.410 -26.554 21.417  1.00 22.36 ? 496  ARG B C     1 
ATOM   9397  O  O     . ARG B 1 476 ? -31.648 -27.129 22.195  1.00 21.89 ? 496  ARG B O     1 
ATOM   9398  C  CB    . ARG B 1 476 ? -33.449 -28.458 20.145  1.00 23.48 ? 496  ARG B CB    1 
ATOM   9399  C  CG    . ARG B 1 476 ? -34.620 -29.435 20.031  1.00 26.28 ? 496  ARG B CG    1 
ATOM   9400  C  CD    . ARG B 1 476 ? -34.237 -30.702 19.247  1.00 28.57 ? 496  ARG B CD    1 
ATOM   9401  N  NE    . ARG B 1 476 ? -33.113 -31.391 19.893  1.00 29.72 ? 496  ARG B NE    1 
ATOM   9402  C  CZ    . ARG B 1 476 ? -31.857 -31.437 19.443  1.00 30.39 ? 496  ARG B CZ    1 
ATOM   9403  N  NH1   . ARG B 1 476 ? -31.505 -30.859 18.301  1.00 31.69 ? 496  ARG B NH1   1 
ATOM   9404  N  NH2   . ARG B 1 476 ? -30.939 -32.087 20.143  1.00 29.78 ? 496  ARG B NH2   1 
ATOM   9405  N  N     . HIS B 1 477 ? -32.128 -25.355 20.900  1.00 21.38 ? 497  HIS B N     1 
ATOM   9406  C  CA    . HIS B 1 477 ? -30.871 -24.665 21.218  1.00 21.37 ? 497  HIS B CA    1 
ATOM   9407  C  C     . HIS B 1 477 ? -31.055 -23.199 21.641  1.00 21.23 ? 497  HIS B C     1 
ATOM   9408  O  O     . HIS B 1 477 ? -30.118 -22.397 21.540  1.00 21.04 ? 497  HIS B O     1 
ATOM   9409  C  CB    . HIS B 1 477 ? -29.939 -24.714 20.015  1.00 21.54 ? 497  HIS B CB    1 
ATOM   9410  C  CG    . HIS B 1 477 ? -29.850 -26.062 19.382  1.00 21.52 ? 497  HIS B CG    1 
ATOM   9411  N  ND1   . HIS B 1 477 ? -28.903 -26.992 19.749  1.00 22.38 ? 497  HIS B ND1   1 
ATOM   9412  C  CD2   . HIS B 1 477 ? -30.606 -26.648 18.425  1.00 20.13 ? 497  HIS B CD2   1 
ATOM   9413  C  CE1   . HIS B 1 477 ? -29.061 -28.084 19.021  1.00 21.57 ? 497  HIS B CE1   1 
ATOM   9414  N  NE2   . HIS B 1 477 ? -30.097 -27.905 18.221  1.00 20.60 ? 497  HIS B NE2   1 
ATOM   9415  N  N     . GLY B 1 478 ? -32.245 -22.858 22.125  1.00 20.54 ? 498  GLY B N     1 
ATOM   9416  C  CA    . GLY B 1 478 ? -32.563 -21.474 22.432  1.00 20.09 ? 498  GLY B CA    1 
ATOM   9417  C  C     . GLY B 1 478 ? -34.049 -21.196 22.554  1.00 19.77 ? 498  GLY B C     1 
ATOM   9418  O  O     . GLY B 1 478 ? -34.873 -22.123 22.643  1.00 19.32 ? 498  GLY B O     1 
ATOM   9419  N  N     . THR B 1 479 ? -34.376 -19.905 22.546  1.00 19.27 ? 499  THR B N     1 
ATOM   9420  C  CA    . THR B 1 479 ? -35.728 -19.418 22.817  1.00 18.90 ? 499  THR B CA    1 
ATOM   9421  C  C     . THR B 1 479 ? -36.194 -18.458 21.734  1.00 18.96 ? 499  THR B C     1 
ATOM   9422  O  O     . THR B 1 479 ? -35.447 -17.581 21.301  1.00 18.45 ? 499  THR B O     1 
ATOM   9423  C  CB    . THR B 1 479 ? -35.753 -18.658 24.152  1.00 18.89 ? 499  THR B CB    1 
ATOM   9424  O  OG1   . THR B 1 479 ? -35.237 -19.503 25.183  1.00 18.33 ? 499  THR B OG1   1 
ATOM   9425  C  CG2   . THR B 1 479 ? -37.171 -18.174 24.510  1.00 17.59 ? 499  THR B CG2   1 
ATOM   9426  N  N     . ARG B 1 480 ? -37.444 -18.607 21.310  1.00 19.24 ? 500  ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 480 ? -38.032 -17.637 20.398  1.00 19.05 ? 500  ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 480 ? -38.286 -16.342 21.164  1.00 18.86 ? 500  ARG B C     1 
ATOM   9429  O  O     . ARG B 1 480 ? -38.989 -16.346 22.167  1.00 18.73 ? 500  ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 480 ? -39.315 -18.179 19.786  1.00 19.25 ? 500  ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 480 ? -39.817 -17.371 18.611  1.00 19.73 ? 500  ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 480 ? -41.061 -18.003 18.029  1.00 19.44 ? 500  ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 480 ? -41.443 -17.405 16.759  1.00 19.82 ? 500  ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 480 ? -42.495 -17.793 16.033  1.00 22.84 ? 500  ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 480 ? -43.286 -18.778 16.460  1.00 22.73 ? 500  ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 480 ? -42.765 -17.189 14.879  1.00 21.88 ? 500  ARG B NH2   1 
ATOM   9437  N  N     . LEU B 1 481 ? -37.691 -15.252 20.676  1.00 18.93 ? 501  LEU B N     1 
ATOM   9438  C  CA    . LEU B 1 481 ? -37.767 -13.920 21.291  1.00 19.24 ? 501  LEU B CA    1 
ATOM   9439  C  C     . LEU B 1 481 ? -38.584 -12.906 20.479  1.00 19.22 ? 501  LEU B C     1 
ATOM   9440  O  O     . LEU B 1 481 ? -39.008 -11.864 20.997  1.00 19.53 ? 501  LEU B O     1 
ATOM   9441  C  CB    . LEU B 1 481 ? -36.352 -13.371 21.470  1.00 19.07 ? 501  LEU B CB    1 
ATOM   9442  C  CG    . LEU B 1 481 ? -35.390 -14.262 22.247  1.00 18.81 ? 501  LEU B CG    1 
ATOM   9443  C  CD1   . LEU B 1 481 ? -34.077 -13.550 22.427  1.00 17.25 ? 501  LEU B CD1   1 
ATOM   9444  C  CD2   . LEU B 1 481 ? -35.988 -14.677 23.589  1.00 18.37 ? 501  LEU B CD2   1 
ATOM   9445  N  N     . HIS B 1 482 ? -38.780 -13.205 19.205  1.00 19.22 ? 502  HIS B N     1 
ATOM   9446  C  CA    . HIS B 1 482 ? -39.641 -12.418 18.346  1.00 19.68 ? 502  HIS B CA    1 
ATOM   9447  C  C     . HIS B 1 482 ? -40.088 -13.302 17.182  1.00 19.60 ? 502  HIS B C     1 
ATOM   9448  O  O     . HIS B 1 482 ? -39.756 -14.489 17.134  1.00 18.96 ? 502  HIS B O     1 
ATOM   9449  C  CB    . HIS B 1 482 ? -38.918 -11.152 17.856  1.00 19.97 ? 502  HIS B CB    1 
ATOM   9450  C  CG    . HIS B 1 482 ? -39.844 -10.016 17.552  1.00 20.89 ? 502  HIS B CG    1 
ATOM   9451  N  ND1   . HIS B 1 482 ? -40.389 -9.815  16.302  1.00 20.87 ? 502  HIS B ND1   1 
ATOM   9452  C  CD2   . HIS B 1 482 ? -40.344 -9.037  18.343  1.00 21.73 ? 502  HIS B CD2   1 
ATOM   9453  C  CE1   . HIS B 1 482 ? -41.189 -8.765  16.338  1.00 21.86 ? 502  HIS B CE1   1 
ATOM   9454  N  NE2   . HIS B 1 482 ? -41.173 -8.269  17.562  1.00 22.38 ? 502  HIS B NE2   1 
ATOM   9455  N  N     . THR B 1 483 ? -40.855 -12.732 16.258  1.00 19.94 ? 503  THR B N     1 
ATOM   9456  C  CA    . THR B 1 483 ? -41.438 -13.490 15.163  1.00 20.06 ? 503  THR B CA    1 
ATOM   9457  C  C     . THR B 1 483 ? -40.396 -14.334 14.430  1.00 20.30 ? 503  THR B C     1 
ATOM   9458  O  O     . THR B 1 483 ? -40.607 -15.529 14.217  1.00 20.96 ? 503  THR B O     1 
ATOM   9459  C  CB    . THR B 1 483 ? -42.165 -12.562 14.179  1.00 20.29 ? 503  THR B CB    1 
ATOM   9460  O  OG1   . THR B 1 483 ? -43.138 -11.781 14.889  1.00 20.56 ? 503  THR B OG1   1 
ATOM   9461  C  CG2   . THR B 1 483 ? -42.855 -13.363 13.089  1.00 20.50 ? 503  THR B CG2   1 
ATOM   9462  N  N     . HIS B 1 484 ? -39.267 -13.735 14.077  1.00 20.23 ? 504  HIS B N     1 
ATOM   9463  C  CA    . HIS B 1 484 ? -38.265 -14.416 13.265  1.00 20.32 ? 504  HIS B CA    1 
ATOM   9464  C  C     . HIS B 1 484 ? -36.943 -14.649 13.994  1.00 19.88 ? 504  HIS B C     1 
ATOM   9465  O  O     . HIS B 1 484 ? -35.904 -14.863 13.352  1.00 19.62 ? 504  HIS B O     1 
ATOM   9466  C  CB    . HIS B 1 484 ? -38.006 -13.594 11.997  1.00 20.56 ? 504  HIS B CB    1 
ATOM   9467  C  CG    . HIS B 1 484 ? -39.222 -13.406 11.146  1.00 21.84 ? 504  HIS B CG    1 
ATOM   9468  N  ND1   . HIS B 1 484 ? -39.923 -14.464 10.606  1.00 22.11 ? 504  HIS B ND1   1 
ATOM   9469  C  CD2   . HIS B 1 484 ? -39.869 -12.284 10.752  1.00 22.50 ? 504  HIS B CD2   1 
ATOM   9470  C  CE1   . HIS B 1 484 ? -40.944 -13.998 9.907   1.00 23.25 ? 504  HIS B CE1   1 
ATOM   9471  N  NE2   . HIS B 1 484 ? -40.932 -12.679 9.979   1.00 22.90 ? 504  HIS B NE2   1 
ATOM   9472  N  N     . LEU B 1 485 ? -36.985 -14.664 15.321  1.00 19.38 ? 505  LEU B N     1 
ATOM   9473  C  CA    . LEU B 1 485 ? -35.764 -14.560 16.124  1.00 19.36 ? 505  LEU B CA    1 
ATOM   9474  C  C     . LEU B 1 485 ? -35.640 -15.650 17.203  1.00 19.61 ? 505  LEU B C     1 
ATOM   9475  O  O     . LEU B 1 485 ? -36.552 -15.834 18.033  1.00 19.38 ? 505  LEU B O     1 
ATOM   9476  C  CB    . LEU B 1 485 ? -35.739 -13.174 16.780  1.00 19.32 ? 505  LEU B CB    1 
ATOM   9477  C  CG    . LEU B 1 485 ? -34.496 -12.732 17.540  1.00 18.83 ? 505  LEU B CG    1 
ATOM   9478  C  CD1   . LEU B 1 485 ? -33.276 -12.659 16.599  1.00 17.71 ? 505  LEU B CD1   1 
ATOM   9479  C  CD2   . LEU B 1 485 ? -34.782 -11.386 18.206  1.00 17.79 ? 505  LEU B CD2   1 
ATOM   9480  N  N     . ILE B 1 486 ? -34.507 -16.353 17.191  1.00 19.38 ? 506  ILE B N     1 
ATOM   9481  C  CA    . ILE B 1 486 ? -34.154 -17.309 18.239  1.00 19.72 ? 506  ILE B CA    1 
ATOM   9482  C  C     . ILE B 1 486 ? -32.976 -16.755 19.016  1.00 19.98 ? 506  ILE B C     1 
ATOM   9483  O  O     . ILE B 1 486 ? -31.960 -16.388 18.425  1.00 19.84 ? 506  ILE B O     1 
ATOM   9484  C  CB    . ILE B 1 486 ? -33.732 -18.684 17.680  1.00 19.80 ? 506  ILE B CB    1 
ATOM   9485  C  CG1   . ILE B 1 486 ? -34.955 -19.502 17.242  1.00 20.98 ? 506  ILE B CG1   1 
ATOM   9486  C  CG2   . ILE B 1 486 ? -32.891 -19.477 18.716  1.00 19.48 ? 506  ILE B CG2   1 
ATOM   9487  C  CD1   . ILE B 1 486 ? -35.575 -20.367 18.315  1.00 21.19 ? 506  ILE B CD1   1 
ATOM   9488  N  N     . GLY B 1 487 ? -33.107 -16.706 20.341  1.00 19.97 ? 507  GLY B N     1 
ATOM   9489  C  CA    . GLY B 1 487 ? -31.975 -16.378 21.202  1.00 20.04 ? 507  GLY B CA    1 
ATOM   9490  C  C     . GLY B 1 487 ? -31.213 -17.646 21.510  1.00 19.43 ? 507  GLY B C     1 
ATOM   9491  O  O     . GLY B 1 487 ? -31.696 -18.484 22.276  1.00 19.97 ? 507  GLY B O     1 
ATOM   9492  N  N     . ASN B 1 488 ? -30.033 -17.803 20.919  1.00 18.36 ? 508  ASN B N     1 
ATOM   9493  C  CA    . ASN B 1 488 ? -29.258 -19.033 21.115  1.00 18.12 ? 508  ASN B CA    1 
ATOM   9494  C  C     . ASN B 1 488 ? -28.779 -19.208 22.544  1.00 17.79 ? 508  ASN B C     1 
ATOM   9495  O  O     . ASN B 1 488 ? -28.336 -18.247 23.193  1.00 17.51 ? 508  ASN B O     1 
ATOM   9496  C  CB    . ASN B 1 488 ? -28.043 -19.100 20.176  1.00 17.99 ? 508  ASN B CB    1 
ATOM   9497  C  CG    . ASN B 1 488 ? -28.447 -19.146 18.713  1.00 18.59 ? 508  ASN B CG    1 
ATOM   9498  O  OD1   . ASN B 1 488 ? -29.120 -18.241 18.241  1.00 19.74 ? 508  ASN B OD1   1 
ATOM   9499  N  ND2   . ASN B 1 488 ? -28.040 -20.194 17.995  1.00 16.70 ? 508  ASN B ND2   1 
ATOM   9500  N  N     . ILE B 1 489 ? -28.868 -20.447 23.020  1.00 17.50 ? 509  ILE B N     1 
ATOM   9501  C  CA    . ILE B 1 489 ? -28.345 -20.806 24.325  1.00 17.98 ? 509  ILE B CA    1 
ATOM   9502  C  C     . ILE B 1 489 ? -26.831 -20.656 24.296  1.00 17.86 ? 509  ILE B C     1 
ATOM   9503  O  O     . ILE B 1 489 ? -26.193 -20.910 23.269  1.00 18.04 ? 509  ILE B O     1 
ATOM   9504  C  CB    . ILE B 1 489 ? -28.732 -22.236 24.706  1.00 18.15 ? 509  ILE B CB    1 
ATOM   9505  C  CG1   . ILE B 1 489 ? -28.329 -22.530 26.150  1.00 19.31 ? 509  ILE B CG1   1 
ATOM   9506  C  CG2   . ILE B 1 489 ? -28.123 -23.264 23.711  1.00 17.61 ? 509  ILE B CG2   1 
ATOM   9507  C  CD1   . ILE B 1 489 ? -28.981 -23.806 26.711  1.00 20.41 ? 509  ILE B CD1   1 
ATOM   9508  N  N     . HIS B 1 490 ? -26.268 -20.195 25.405  1.00 17.72 ? 510  HIS B N     1 
ATOM   9509  C  CA    . HIS B 1 490 ? -24.824 -20.043 25.513  1.00 17.32 ? 510  HIS B CA    1 
ATOM   9510  C  C     . HIS B 1 490 ? -24.387 -19.905 26.952  1.00 17.19 ? 510  HIS B C     1 
ATOM   9511  O  O     . HIS B 1 490 ? -25.200 -19.618 27.832  1.00 16.83 ? 510  HIS B O     1 
ATOM   9512  C  CB    . HIS B 1 490 ? -24.364 -18.812 24.729  1.00 17.46 ? 510  HIS B CB    1 
ATOM   9513  C  CG    . HIS B 1 490 ? -24.996 -17.536 25.185  1.00 17.90 ? 510  HIS B CG    1 
ATOM   9514  N  ND1   . HIS B 1 490 ? -26.317 -17.226 24.931  1.00 17.50 ? 510  HIS B ND1   1 
ATOM   9515  C  CD2   . HIS B 1 490 ? -24.492 -16.496 25.892  1.00 17.72 ? 510  HIS B CD2   1 
ATOM   9516  C  CE1   . HIS B 1 490 ? -26.602 -16.053 25.469  1.00 17.05 ? 510  HIS B CE1   1 
ATOM   9517  N  NE2   . HIS B 1 490 ? -25.508 -15.584 26.050  1.00 17.43 ? 510  HIS B NE2   1 
ATOM   9518  N  N     . THR B 1 491 ? -23.089 -20.096 27.176  1.00 17.13 ? 511  THR B N     1 
ATOM   9519  C  CA    . THR B 1 491 ? -22.481 -19.833 28.460  1.00 16.81 ? 511  THR B CA    1 
ATOM   9520  C  C     . THR B 1 491 ? -21.413 -18.741 28.326  1.00 17.51 ? 511  THR B C     1 
ATOM   9521  O  O     . THR B 1 491 ? -20.581 -18.774 27.411  1.00 17.23 ? 511  THR B O     1 
ATOM   9522  C  CB    . THR B 1 491 ? -21.845 -21.105 29.058  1.00 17.05 ? 511  THR B CB    1 
ATOM   9523  O  OG1   . THR B 1 491 ? -22.836 -22.131 29.160  1.00 17.08 ? 511  THR B OG1   1 
ATOM   9524  C  CG2   . THR B 1 491 ? -21.280 -20.823 30.460  1.00 15.34 ? 511  THR B CG2   1 
ATOM   9525  N  N     . HIS B 1 492 ? -21.469 -17.772 29.237  1.00 17.57 ? 512  HIS B N     1 
ATOM   9526  C  CA    . HIS B 1 492 ? -20.440 -16.754 29.380  1.00 18.22 ? 512  HIS B CA    1 
ATOM   9527  C  C     . HIS B 1 492 ? -19.412 -17.262 30.377  1.00 18.45 ? 512  HIS B C     1 
ATOM   9528  O  O     . HIS B 1 492 ? -19.784 -17.672 31.474  1.00 17.86 ? 512  HIS B O     1 
ATOM   9529  C  CB    . HIS B 1 492 ? -21.018 -15.445 29.934  1.00 17.72 ? 512  HIS B CB    1 
ATOM   9530  C  CG    . HIS B 1 492 ? -21.982 -14.756 29.022  1.00 18.19 ? 512  HIS B CG    1 
ATOM   9531  N  ND1   . HIS B 1 492 ? -21.586 -13.824 28.090  1.00 17.71 ? 512  HIS B ND1   1 
ATOM   9532  C  CD2   . HIS B 1 492 ? -23.332 -14.818 28.941  1.00 17.60 ? 512  HIS B CD2   1 
ATOM   9533  C  CE1   . HIS B 1 492 ? -22.647 -13.376 27.443  1.00 18.00 ? 512  HIS B CE1   1 
ATOM   9534  N  NE2   . HIS B 1 492 ? -23.719 -13.952 27.951  1.00 17.29 ? 512  HIS B NE2   1 
ATOM   9535  N  N     . LEU B 1 493 ? -18.132 -17.221 30.010  1.00 18.96 ? 513  LEU B N     1 
ATOM   9536  C  CA    . LEU B 1 493 ? -17.059 -17.568 30.947  1.00 19.54 ? 513  LEU B CA    1 
ATOM   9537  C  C     . LEU B 1 493 ? -15.979 -16.524 30.844  1.00 19.66 ? 513  LEU B C     1 
ATOM   9538  O  O     . LEU B 1 493 ? -15.624 -16.120 29.742  1.00 20.47 ? 513  LEU B O     1 
ATOM   9539  C  CB    . LEU B 1 493 ? -16.444 -18.923 30.624  1.00 19.98 ? 513  LEU B CB    1 
ATOM   9540  C  CG    . LEU B 1 493 ? -17.311 -20.175 30.695  1.00 20.67 ? 513  LEU B CG    1 
ATOM   9541  C  CD1   . LEU B 1 493 ? -16.601 -21.323 29.986  1.00 21.24 ? 513  LEU B CD1   1 
ATOM   9542  C  CD2   . LEU B 1 493 ? -17.637 -20.525 32.144  1.00 20.87 ? 513  LEU B CD2   1 
ATOM   9543  N  N     . VAL B 1 494 ? -15.456 -16.101 31.992  1.00 19.48 ? 514  VAL B N     1 
ATOM   9544  C  CA    . VAL B 1 494 ? -14.422 -15.084 32.070  1.00 19.28 ? 514  VAL B CA    1 
ATOM   9545  C  C     . VAL B 1 494 ? -13.309 -15.640 32.941  1.00 19.40 ? 514  VAL B C     1 
ATOM   9546  O  O     . VAL B 1 494 ? -13.576 -16.289 33.959  1.00 19.41 ? 514  VAL B O     1 
ATOM   9547  C  CB    . VAL B 1 494 ? -14.956 -13.756 32.686  1.00 19.50 ? 514  VAL B CB    1 
ATOM   9548  C  CG1   . VAL B 1 494 ? -13.876 -12.677 32.684  1.00 18.34 ? 514  VAL B CG1   1 
ATOM   9549  C  CG2   . VAL B 1 494 ? -16.192 -13.262 31.930  1.00 19.06 ? 514  VAL B CG2   1 
ATOM   9550  N  N     . HIS B 1 495 ? -12.069 -15.392 32.529  1.00 19.33 ? 515  HIS B N     1 
ATOM   9551  C  CA    . HIS B 1 495 ? -10.897 -15.791 33.292  1.00 19.38 ? 515  HIS B CA    1 
ATOM   9552  C  C     . HIS B 1 495 ? -10.159 -14.560 33.777  1.00 19.44 ? 515  HIS B C     1 
ATOM   9553  O  O     . HIS B 1 495 ? -9.919  -13.630 32.999  1.00 19.56 ? 515  HIS B O     1 
ATOM   9554  C  CB    . HIS B 1 495 ? -9.931  -16.624 32.453  1.00 19.33 ? 515  HIS B CB    1 
ATOM   9555  C  CG    . HIS B 1 495 ? -9.093  -17.570 33.263  1.00 19.57 ? 515  HIS B CG    1 
ATOM   9556  N  ND1   . HIS B 1 495 ? -7.727  -17.694 33.099  1.00 20.28 ? 515  HIS B ND1   1 
ATOM   9557  C  CD2   . HIS B 1 495 ? -9.435  -18.447 34.236  1.00 19.39 ? 515  HIS B CD2   1 
ATOM   9558  C  CE1   . HIS B 1 495 ? -7.268  -18.610 33.933  1.00 20.53 ? 515  HIS B CE1   1 
ATOM   9559  N  NE2   . HIS B 1 495 ? -8.285  -19.082 34.636  1.00 20.17 ? 515  HIS B NE2   1 
ATOM   9560  N  N     . TYR B 1 496 ? -9.795  -14.585 35.054  1.00 18.92 ? 516  TYR B N     1 
ATOM   9561  C  CA    . TYR B 1 496 ? -9.026  -13.542 35.684  1.00 19.33 ? 516  TYR B CA    1 
ATOM   9562  C  C     . TYR B 1 496 ? -7.705  -14.120 36.156  1.00 18.93 ? 516  TYR B C     1 
ATOM   9563  O  O     . TYR B 1 496 ? -7.648  -15.260 36.614  1.00 19.51 ? 516  TYR B O     1 
ATOM   9564  C  CB    . TYR B 1 496 ? -9.768  -13.012 36.917  1.00 19.05 ? 516  TYR B CB    1 
ATOM   9565  C  CG    . TYR B 1 496 ? -10.931 -12.099 36.644  1.00 19.91 ? 516  TYR B CG    1 
ATOM   9566  C  CD1   . TYR B 1 496 ? -12.238 -12.591 36.551  1.00 20.41 ? 516  TYR B CD1   1 
ATOM   9567  C  CD2   . TYR B 1 496 ? -10.744 -10.732 36.551  1.00 20.18 ? 516  TYR B CD2   1 
ATOM   9568  C  CE1   . TYR B 1 496 ? -13.316 -11.727 36.333  1.00 19.38 ? 516  TYR B CE1   1 
ATOM   9569  C  CE2   . TYR B 1 496 ? -11.796 -9.883  36.342  1.00 19.08 ? 516  TYR B CE2   1 
ATOM   9570  C  CZ    . TYR B 1 496 ? -13.080 -10.376 36.236  1.00 19.99 ? 516  TYR B CZ    1 
ATOM   9571  O  OH    . TYR B 1 496 ? -14.112 -9.485  36.015  1.00 21.02 ? 516  TYR B OH    1 
ATOM   9572  N  N     . ARG B 1 497 ? -6.653  -13.326 36.057  1.00 19.30 ? 517  ARG B N     1 
ATOM   9573  C  CA    . ARG B 1 497 ? -5.370  -13.658 36.668  1.00 19.08 ? 517  ARG B CA    1 
ATOM   9574  C  C     . ARG B 1 497 ? -5.306  -12.862 37.946  1.00 19.29 ? 517  ARG B C     1 
ATOM   9575  O  O     . ARG B 1 497 ? -5.505  -11.648 37.925  1.00 19.10 ? 517  ARG B O     1 
ATOM   9576  C  CB    . ARG B 1 497 ? -4.223  -13.252 35.758  1.00 19.37 ? 517  ARG B CB    1 
ATOM   9577  C  CG    . ARG B 1 497 ? -2.810  -13.446 36.357  1.00 18.55 ? 517  ARG B CG    1 
ATOM   9578  C  CD    . ARG B 1 497 ? -1.774  -12.893 35.410  1.00 20.03 ? 517  ARG B CD    1 
ATOM   9579  N  NE    . ARG B 1 497 ? -0.418  -12.796 35.966  1.00 20.47 ? 517  ARG B NE    1 
ATOM   9580  C  CZ    . ARG B 1 497 ? 0.460   -13.799 36.033  1.00 21.89 ? 517  ARG B CZ    1 
ATOM   9581  N  NH1   . ARG B 1 497 ? 0.151   -15.012 35.613  1.00 22.81 ? 517  ARG B NH1   1 
ATOM   9582  N  NH2   . ARG B 1 497 ? 1.665   -13.585 36.544  1.00 24.56 ? 517  ARG B NH2   1 
ATOM   9583  N  N     . VAL B 1 498 ? -5.050  -13.542 39.062  1.00 19.63 ? 518  VAL B N     1 
ATOM   9584  C  CA    . VAL B 1 498 ? -5.033  -12.884 40.370  1.00 19.54 ? 518  VAL B CA    1 
ATOM   9585  C  C     . VAL B 1 498 ? -3.698  -13.193 41.041  1.00 19.80 ? 518  VAL B C     1 
ATOM   9586  O  O     . VAL B 1 498 ? -3.562  -14.178 41.762  1.00 19.07 ? 518  VAL B O     1 
ATOM   9587  C  CB    . VAL B 1 498 ? -6.230  -13.334 41.242  1.00 19.37 ? 518  VAL B CB    1 
ATOM   9588  C  CG1   . VAL B 1 498 ? -6.371  -12.452 42.463  1.00 18.96 ? 518  VAL B CG1   1 
ATOM   9589  C  CG2   . VAL B 1 498 ? -7.528  -13.301 40.421  1.00 19.30 ? 518  VAL B CG2   1 
ATOM   9590  N  N     . ASP B 1 499 ? -2.707  -12.361 40.749  1.00 20.45 ? 519  ASP B N     1 
ATOM   9591  C  CA    . ASP B 1 499 ? -1.361  -12.551 41.279  1.00 21.02 ? 519  ASP B CA    1 
ATOM   9592  C  C     . ASP B 1 499 ? -1.336  -11.906 42.647  1.00 21.47 ? 519  ASP B C     1 
ATOM   9593  O  O     . ASP B 1 499 ? -0.964  -10.742 42.806  1.00 21.39 ? 519  ASP B O     1 
ATOM   9594  C  CB    . ASP B 1 499 ? -0.306  -11.941 40.358  1.00 20.75 ? 519  ASP B CB    1 
ATOM   9595  C  CG    . ASP B 1 499 ? 1.122   -12.164 40.864  1.00 21.26 ? 519  ASP B CG    1 
ATOM   9596  O  OD1   . ASP B 1 499 ? 1.303   -12.888 41.866  1.00 20.66 ? 519  ASP B OD1   1 
ATOM   9597  O  OD2   . ASP B 1 499 ? 2.063   -11.609 40.257  1.00 22.09 ? 519  ASP B OD2   1 
ATOM   9598  N  N     . LEU B 1 500 ? -1.799  -12.654 43.635  1.00 22.41 ? 520  LEU B N     1 
ATOM   9599  C  CA    . LEU B 1 500 ? -1.801  -12.149 44.998  1.00 23.06 ? 520  LEU B CA    1 
ATOM   9600  C  C     . LEU B 1 500 ? -0.369  -12.222 45.496  1.00 22.93 ? 520  LEU B C     1 
ATOM   9601  O  O     . LEU B 1 500 ? 0.312   -13.214 45.264  1.00 22.01 ? 520  LEU B O     1 
ATOM   9602  C  CB    . LEU B 1 500 ? -2.713  -12.978 45.899  1.00 23.16 ? 520  LEU B CB    1 
ATOM   9603  C  CG    . LEU B 1 500 ? -4.209  -12.859 45.600  1.00 24.41 ? 520  LEU B CG    1 
ATOM   9604  C  CD1   . LEU B 1 500 ? -4.980  -13.871 46.428  1.00 24.07 ? 520  LEU B CD1   1 
ATOM   9605  C  CD2   . LEU B 1 500 ? -4.705  -11.453 45.852  1.00 24.16 ? 520  LEU B CD2   1 
ATOM   9606  N  N     . ASP B 1 501 ? 0.076   -11.153 46.146  1.00 23.61 ? 521  ASP B N     1 
ATOM   9607  C  CA    . ASP B 1 501 ? 1.330   -11.130 46.880  1.00 24.09 ? 521  ASP B CA    1 
ATOM   9608  C  C     . ASP B 1 501 ? 0.981   -10.657 48.300  1.00 24.22 ? 521  ASP B C     1 
ATOM   9609  O  O     . ASP B 1 501 ? 1.154   -9.485  48.639  1.00 24.20 ? 521  ASP B O     1 
ATOM   9610  C  CB    . ASP B 1 501 ? 2.335   -10.178 46.219  1.00 24.04 ? 521  ASP B CB    1 
ATOM   9611  C  CG    . ASP B 1 501 ? 2.977   -10.747 44.940  1.00 24.71 ? 521  ASP B CG    1 
ATOM   9612  O  OD1   . ASP B 1 501 ? 2.702   -11.899 44.503  1.00 24.93 ? 521  ASP B OD1   1 
ATOM   9613  O  OD2   . ASP B 1 501 ? 3.783   -10.003 44.355  1.00 23.98 ? 521  ASP B OD2   1 
ATOM   9614  N  N     . VAL B 1 502 ? 0.462   -11.570 49.117  1.00 24.71 ? 522  VAL B N     1 
ATOM   9615  C  CA    . VAL B 1 502 ? -0.038  -11.205 50.440  1.00 25.00 ? 522  VAL B CA    1 
ATOM   9616  C  C     . VAL B 1 502 ? 1.132   -10.784 51.356  1.00 26.06 ? 522  VAL B C     1 
ATOM   9617  O  O     . VAL B 1 502 ? 1.977   -11.606 51.727  1.00 25.93 ? 522  VAL B O     1 
ATOM   9618  C  CB    . VAL B 1 502 ? -0.847  -12.344 51.083  1.00 25.12 ? 522  VAL B CB    1 
ATOM   9619  C  CG1   . VAL B 1 502 ? -1.406  -11.902 52.443  1.00 23.56 ? 522  VAL B CG1   1 
ATOM   9620  C  CG2   . VAL B 1 502 ? -1.988  -12.791 50.150  1.00 24.76 ? 522  VAL B CG2   1 
ATOM   9621  N  N     . ALA B 1 503 ? 1.172   -9.493  51.683  1.00 27.05 ? 523  ALA B N     1 
ATOM   9622  C  CA    . ALA B 1 503 ? 2.232   -8.894  52.505  1.00 28.27 ? 523  ALA B CA    1 
ATOM   9623  C  C     . ALA B 1 503 ? 3.637   -9.155  51.950  1.00 29.34 ? 523  ALA B C     1 
ATOM   9624  O  O     . ALA B 1 503 ? 4.611   -9.124  52.693  1.00 29.56 ? 523  ALA B O     1 
ATOM   9625  C  CB    . ALA B 1 503 ? 2.133   -9.398  53.943  1.00 27.86 ? 523  ALA B CB    1 
ATOM   9626  N  N     . GLY B 1 504 ? 3.751   -9.401  50.648  1.00 30.68 ? 524  GLY B N     1 
ATOM   9627  C  CA    . GLY B 1 504 ? 5.011   -9.890  50.096  1.00 31.40 ? 524  GLY B CA    1 
ATOM   9628  C  C     . GLY B 1 504 ? 4.839   -10.960 49.038  1.00 32.11 ? 524  GLY B C     1 
ATOM   9629  O  O     . GLY B 1 504 ? 3.746   -11.513 48.848  1.00 32.51 ? 524  GLY B O     1 
ATOM   9630  N  N     . THR B 1 505 ? 5.946   -11.271 48.374  1.00 32.35 ? 525  THR B N     1 
ATOM   9631  C  CA    A THR B 1 505 ? 5.917   -12.140 47.212  0.60 32.45 ? 525  THR B CA    1 
ATOM   9632  C  CA    B THR B 1 505 ? 5.933   -12.153 47.211  0.40 32.44 ? 525  THR B CA    1 
ATOM   9633  C  C     . THR B 1 505 ? 5.637   -13.595 47.571  1.00 32.43 ? 525  THR B C     1 
ATOM   9634  O  O     . THR B 1 505 ? 4.929   -14.284 46.840  1.00 32.83 ? 525  THR B O     1 
ATOM   9635  C  CB    A THR B 1 505 ? 7.236   -12.030 46.419  0.60 32.60 ? 525  THR B CB    1 
ATOM   9636  C  CB    B THR B 1 505 ? 7.274   -12.110 46.428  0.40 32.55 ? 525  THR B CB    1 
ATOM   9637  O  OG1   A THR B 1 505 ? 7.655   -10.658 46.383  0.60 32.23 ? 525  THR B OG1   1 
ATOM   9638  O  OG1   B THR B 1 505 ? 7.212   -13.021 45.324  0.40 32.65 ? 525  THR B OG1   1 
ATOM   9639  C  CG2   A THR B 1 505 ? 7.050   -12.536 44.997  0.60 32.63 ? 525  THR B CG2   1 
ATOM   9640  C  CG2   B THR B 1 505 ? 8.455   -12.486 47.320  0.40 32.31 ? 525  THR B CG2   1 
ATOM   9641  N  N     . LYS B 1 506 ? 6.173   -14.061 48.697  1.00 32.25 ? 526  LYS B N     1 
ATOM   9642  C  CA    . LYS B 1 506 ? 6.115   -15.497 49.004  1.00 31.86 ? 526  LYS B CA    1 
ATOM   9643  C  C     . LYS B 1 506 ? 4.966   -15.891 49.926  1.00 30.87 ? 526  LYS B C     1 
ATOM   9644  O  O     . LYS B 1 506 ? 4.873   -15.426 51.061  1.00 30.96 ? 526  LYS B O     1 
ATOM   9645  C  CB    . LYS B 1 506 ? 7.456   -15.994 49.542  1.00 32.22 ? 526  LYS B CB    1 
ATOM   9646  C  CG    . LYS B 1 506 ? 8.529   -16.097 48.455  1.00 33.29 ? 526  LYS B CG    1 
ATOM   9647  C  CD    . LYS B 1 506 ? 9.630   -17.067 48.847  1.00 35.42 ? 526  LYS B CD    1 
ATOM   9648  C  CE    . LYS B 1 506 ? 10.655  -17.232 47.724  1.00 36.59 ? 526  LYS B CE    1 
ATOM   9649  N  NZ    . LYS B 1 506 ? 11.521  -18.438 47.934  1.00 37.14 ? 526  LYS B NZ    1 
ATOM   9650  N  N     . ASN B 1 507 ? 4.110   -16.773 49.410  1.00 29.56 ? 527  ASN B N     1 
ATOM   9651  C  CA    . ASN B 1 507 ? 2.876   -17.164 50.058  1.00 28.41 ? 527  ASN B CA    1 
ATOM   9652  C  C     . ASN B 1 507 ? 2.707   -18.670 50.035  1.00 28.04 ? 527  ASN B C     1 
ATOM   9653  O  O     . ASN B 1 507 ? 3.436   -19.392 49.340  1.00 27.62 ? 527  ASN B O     1 
ATOM   9654  C  CB    . ASN B 1 507 ? 1.674   -16.539 49.336  1.00 28.04 ? 527  ASN B CB    1 
ATOM   9655  C  CG    . ASN B 1 507 ? 1.637   -15.021 49.427  1.00 27.19 ? 527  ASN B CG    1 
ATOM   9656  O  OD1   . ASN B 1 507 ? 1.142   -14.354 48.518  1.00 25.45 ? 527  ASN B OD1   1 
ATOM   9657  N  ND2   . ASN B 1 507 ? 2.146   -14.471 50.514  1.00 26.35 ? 527  ASN B ND2   1 
ATOM   9658  N  N     . SER B 1 508 ? 1.730   -19.134 50.804  1.00 27.44 ? 528  SER B N     1 
ATOM   9659  C  CA    . SER B 1 508 ? 1.211   -20.481 50.666  1.00 27.43 ? 528  SER B CA    1 
ATOM   9660  C  C     . SER B 1 508 ? -0.307  -20.404 50.420  1.00 26.71 ? 528  SER B C     1 
ATOM   9661  O  O     . SER B 1 508 ? -0.903  -19.332 50.497  1.00 26.31 ? 528  SER B O     1 
ATOM   9662  C  CB    . SER B 1 508 ? 1.567   -21.315 51.898  1.00 27.59 ? 528  SER B CB    1 
ATOM   9663  O  OG    . SER B 1 508 ? 2.982   -21.588 51.930  1.00 30.03 ? 528  SER B OG    1 
ATOM   9664  N  N     . PHE B 1 509 ? -0.903  -21.534 50.074  1.00 26.12 ? 529  PHE B N     1 
ATOM   9665  C  CA    . PHE B 1 509 ? -2.340  -21.632 49.842  1.00 26.01 ? 529  PHE B CA    1 
ATOM   9666  C  C     . PHE B 1 509 ? -2.890  -22.674 50.807  1.00 26.12 ? 529  PHE B C     1 
ATOM   9667  O  O     . PHE B 1 509 ? -2.309  -23.750 50.986  1.00 26.29 ? 529  PHE B O     1 
ATOM   9668  C  CB    . PHE B 1 509 ? -2.657  -22.021 48.390  1.00 25.75 ? 529  PHE B CB    1 
ATOM   9669  C  CG    . PHE B 1 509 ? -4.110  -22.347 48.147  1.00 24.75 ? 529  PHE B CG    1 
ATOM   9670  C  CD1   . PHE B 1 509 ? -5.074  -21.355 48.184  1.00 24.50 ? 529  PHE B CD1   1 
ATOM   9671  C  CD2   . PHE B 1 509 ? -4.512  -23.649 47.862  1.00 25.55 ? 529  PHE B CD2   1 
ATOM   9672  C  CE1   . PHE B 1 509 ? -6.420  -21.652 47.954  1.00 24.22 ? 529  PHE B CE1   1 
ATOM   9673  C  CE2   . PHE B 1 509 ? -5.856  -23.952 47.630  1.00 24.74 ? 529  PHE B CE2   1 
ATOM   9674  C  CZ    . PHE B 1 509 ? -6.806  -22.951 47.678  1.00 24.35 ? 529  PHE B CZ    1 
ATOM   9675  N  N     . GLN B 1 510 ? -4.024  -22.344 51.403  1.00 25.84 ? 530  GLN B N     1 
ATOM   9676  C  CA    . GLN B 1 510 ? -4.616  -23.133 52.464  1.00 25.95 ? 530  GLN B CA    1 
ATOM   9677  C  C     . GLN B 1 510 ? -6.126  -22.956 52.356  1.00 25.02 ? 530  GLN B C     1 
ATOM   9678  O  O     . GLN B 1 510 ? -6.596  -21.899 51.963  1.00 25.34 ? 530  GLN B O     1 
ATOM   9679  C  CB    . GLN B 1 510 ? -4.084  -22.592 53.803  1.00 26.27 ? 530  GLN B CB    1 
ATOM   9680  C  CG    . GLN B 1 510 ? -4.779  -23.082 55.060  1.00 28.59 ? 530  GLN B CG    1 
ATOM   9681  C  CD    . GLN B 1 510 ? -4.449  -22.232 56.292  1.00 30.09 ? 530  GLN B CD    1 
ATOM   9682  O  OE1   . GLN B 1 510 ? -4.042  -21.075 56.185  1.00 33.29 ? 530  GLN B OE1   1 
ATOM   9683  N  NE2   . GLN B 1 510 ? -4.648  -22.805 57.460  1.00 32.25 ? 530  GLN B NE2   1 
ATOM   9684  N  N     . THR B 1 511 ? -6.881  -23.988 52.686  1.00 24.60 ? 531  THR B N     1 
ATOM   9685  C  CA    . THR B 1 511 ? -8.325  -23.876 52.777  1.00 24.16 ? 531  THR B CA    1 
ATOM   9686  C  C     . THR B 1 511 ? -8.800  -24.297 54.166  1.00 24.24 ? 531  THR B C     1 
ATOM   9687  O  O     . THR B 1 511 ? -8.156  -25.111 54.847  1.00 24.29 ? 531  THR B O     1 
ATOM   9688  C  CB    . THR B 1 511 ? -9.059  -24.727 51.698  1.00 24.17 ? 531  THR B CB    1 
ATOM   9689  O  OG1   . THR B 1 511 ? -8.791  -26.120 51.898  1.00 24.08 ? 531  THR B OG1   1 
ATOM   9690  C  CG2   . THR B 1 511 ? -8.635  -24.314 50.272  1.00 23.57 ? 531  THR B CG2   1 
ATOM   9691  N  N     . LEU B 1 512 ? -9.937  -23.741 54.571  1.00 23.64 ? 532  LEU B N     1 
ATOM   9692  C  CA    . LEU B 1 512 ? -10.576 -24.087 55.828  1.00 23.30 ? 532  LEU B CA    1 
ATOM   9693  C  C     . LEU B 1 512 ? -12.004 -24.578 55.561  1.00 23.35 ? 532  LEU B C     1 
ATOM   9694  O  O     . LEU B 1 512 ? -12.696 -24.043 54.687  1.00 22.77 ? 532  LEU B O     1 
ATOM   9695  C  CB    . LEU B 1 512 ? -10.608 -22.882 56.781  1.00 22.85 ? 532  LEU B CB    1 
ATOM   9696  C  CG    . LEU B 1 512 ? -9.319  -22.085 57.005  1.00 22.62 ? 532  LEU B CG    1 
ATOM   9697  C  CD1   . LEU B 1 512 ? -9.589  -20.901 57.918  1.00 21.25 ? 532  LEU B CD1   1 
ATOM   9698  C  CD2   . LEU B 1 512 ? -8.197  -22.962 57.569  1.00 20.05 ? 532  LEU B CD2   1 
ATOM   9699  N  N     . GLN B 1 513 ? -12.421 -25.588 56.322  1.00 23.32 ? 533  GLN B N     1 
ATOM   9700  C  CA    . GLN B 1 513 ? -13.774 -26.134 56.268  1.00 23.82 ? 533  GLN B CA    1 
ATOM   9701  C  C     . GLN B 1 513 ? -14.308 -26.321 57.685  1.00 24.12 ? 533  GLN B C     1 
ATOM   9702  O  O     . GLN B 1 513 ? -13.552 -26.297 58.653  1.00 23.96 ? 533  GLN B O     1 
ATOM   9703  C  CB    . GLN B 1 513 ? -13.785 -27.485 55.546  1.00 23.57 ? 533  GLN B CB    1 
ATOM   9704  N  N     . MET B 1 514 ? -15.617 -26.491 57.802  1.00 24.65 ? 534  MET B N     1 
ATOM   9705  C  CA    . MET B 1 514 ? -16.210 -26.908 59.054  1.00 25.29 ? 534  MET B CA    1 
ATOM   9706  C  C     . MET B 1 514 ? -16.358 -28.415 58.998  1.00 25.29 ? 534  MET B C     1 
ATOM   9707  O  O     . MET B 1 514 ? -16.868 -28.948 58.017  1.00 25.64 ? 534  MET B O     1 
ATOM   9708  C  CB    . MET B 1 514 ? -17.576 -26.249 59.261  1.00 25.65 ? 534  MET B CB    1 
ATOM   9709  C  CG    . MET B 1 514 ? -18.164 -26.471 60.642  1.00 27.08 ? 534  MET B CG    1 
ATOM   9710  S  SD    . MET B 1 514 ? -19.156 -27.984 60.833  1.00 31.03 ? 534  MET B SD    1 
ATOM   9711  C  CE    . MET B 1 514 ? -20.597 -27.606 59.836  1.00 29.48 ? 534  MET B CE    1 
ATOM   9712  N  N     . LYS B 1 515 ? -15.918 -29.093 60.055  1.00 25.28 ? 535  LYS B N     1 
ATOM   9713  C  CA    . LYS B 1 515 ? -16.071 -30.534 60.195  1.00 25.36 ? 535  LYS B CA    1 
ATOM   9714  C  C     . LYS B 1 515 ? -16.688 -30.818 61.553  1.00 25.24 ? 535  LYS B C     1 
ATOM   9715  O  O     . LYS B 1 515 ? -16.250 -30.261 62.561  1.00 25.32 ? 535  LYS B O     1 
ATOM   9716  C  CB    . LYS B 1 515 ? -14.707 -31.219 60.108  1.00 25.53 ? 535  LYS B CB    1 
ATOM   9717  C  CG    . LYS B 1 515 ? -14.761 -32.729 60.183  1.00 27.04 ? 535  LYS B CG    1 
ATOM   9718  N  N     . LEU B 1 516 ? -17.698 -31.678 61.589  1.00 24.58 ? 536  LEU B N     1 
ATOM   9719  C  CA    . LEU B 1 516 ? -18.365 -31.968 62.837  1.00 24.53 ? 536  LEU B CA    1 
ATOM   9720  C  C     . LEU B 1 516 ? -17.554 -32.957 63.665  1.00 24.60 ? 536  LEU B C     1 
ATOM   9721  O  O     . LEU B 1 516 ? -16.888 -33.829 63.123  1.00 24.55 ? 536  LEU B O     1 
ATOM   9722  C  CB    . LEU B 1 516 ? -19.753 -32.551 62.587  1.00 24.40 ? 536  LEU B CB    1 
ATOM   9723  C  CG    . LEU B 1 516 ? -20.819 -31.624 61.998  1.00 23.73 ? 536  LEU B CG    1 
ATOM   9724  C  CD1   . LEU B 1 516 ? -22.068 -32.453 61.724  1.00 22.03 ? 536  LEU B CD1   1 
ATOM   9725  C  CD2   . LEU B 1 516 ? -21.127 -30.459 62.932  1.00 22.17 ? 536  LEU B CD2   1 
ATOM   9726  N  N     . GLU B 1 517 ? -17.622 -32.820 64.983  1.00 24.70 ? 537  GLU B N     1 
ATOM   9727  C  CA    . GLU B 1 517 ? -17.172 -33.877 65.875  1.00 24.77 ? 537  GLU B CA    1 
ATOM   9728  C  C     . GLU B 1 517 ? -18.368 -34.344 66.677  1.00 25.24 ? 537  GLU B C     1 
ATOM   9729  O  O     . GLU B 1 517 ? -19.353 -33.618 66.819  1.00 25.19 ? 537  GLU B O     1 
ATOM   9730  C  CB    . GLU B 1 517 ? -16.063 -33.392 66.805  1.00 24.48 ? 537  GLU B CB    1 
ATOM   9731  C  CG    . GLU B 1 517 ? -16.519 -32.378 67.853  1.00 24.32 ? 537  GLU B CG    1 
ATOM   9732  C  CD    . GLU B 1 517 ? -15.393 -31.933 68.764  1.00 23.71 ? 537  GLU B CD    1 
ATOM   9733  O  OE1   . GLU B 1 517 ? -14.259 -32.397 68.571  1.00 23.18 ? 537  GLU B OE1   1 
ATOM   9734  O  OE2   . GLU B 1 517 ? -15.650 -31.124 69.673  1.00 23.96 ? 537  GLU B OE2   1 
ATOM   9735  N  N     . ASN B 1 518 ? -18.269 -35.567 67.187  1.00 25.71 ? 538  ASN B N     1 
ATOM   9736  C  CA    . ASN B 1 518 ? -19.286 -36.155 68.023  1.00 26.05 ? 538  ASN B CA    1 
ATOM   9737  C  C     . ASN B 1 518 ? -18.626 -36.652 69.306  1.00 26.43 ? 538  ASN B C     1 
ATOM   9738  O  O     . ASN B 1 518 ? -18.005 -37.717 69.310  1.00 26.45 ? 538  ASN B O     1 
ATOM   9739  C  CB    . ASN B 1 518 ? -19.939 -37.296 67.270  1.00 26.16 ? 538  ASN B CB    1 
ATOM   9740  C  CG    . ASN B 1 518 ? -20.980 -38.019 68.082  1.00 26.73 ? 538  ASN B CG    1 
ATOM   9741  O  OD1   . ASN B 1 518 ? -21.216 -37.723 69.256  1.00 25.89 ? 538  ASN B OD1   1 
ATOM   9742  N  ND2   . ASN B 1 518 ? -21.613 -38.989 67.445  1.00 27.85 ? 538  ASN B ND2   1 
ATOM   9743  N  N     . ILE B 1 519 ? -18.748 -35.872 70.384  1.00 26.33 ? 539  ILE B N     1 
ATOM   9744  C  CA    . ILE B 1 519 ? -18.070 -36.191 71.643  1.00 26.31 ? 539  ILE B CA    1 
ATOM   9745  C  C     . ILE B 1 519 ? -19.058 -36.437 72.760  1.00 26.31 ? 539  ILE B C     1 
ATOM   9746  O  O     . ILE B 1 519 ? -20.246 -36.163 72.625  1.00 26.52 ? 539  ILE B O     1 
ATOM   9747  C  CB    . ILE B 1 519 ? -17.075 -35.075 72.071  1.00 26.16 ? 539  ILE B CB    1 
ATOM   9748  C  CG1   . ILE B 1 519 ? -17.800 -33.747 72.351  1.00 26.48 ? 539  ILE B CG1   1 
ATOM   9749  C  CG2   . ILE B 1 519 ? -16.024 -34.876 70.997  1.00 26.26 ? 539  ILE B CG2   1 
ATOM   9750  C  CD1   . ILE B 1 519 ? -16.891 -32.628 72.827  1.00 23.61 ? 539  ILE B CD1   1 
ATOM   9751  N  N     . THR B 1 520 ? -18.553 -36.974 73.865  1.00 26.26 ? 540  THR B N     1 
ATOM   9752  C  CA    . THR B 1 520 ? -19.326 -37.057 75.092  1.00 26.42 ? 540  THR B CA    1 
ATOM   9753  C  C     . THR B 1 520 ? -19.577 -35.632 75.589  1.00 26.43 ? 540  THR B C     1 
ATOM   9754  O  O     . THR B 1 520 ? -18.658 -34.817 75.636  1.00 25.83 ? 540  THR B O     1 
ATOM   9755  C  CB    . THR B 1 520 ? -18.572 -37.833 76.189  1.00 26.44 ? 540  THR B CB    1 
ATOM   9756  O  OG1   . THR B 1 520 ? -18.199 -39.127 75.693  1.00 26.70 ? 540  THR B OG1   1 
ATOM   9757  C  CG2   . THR B 1 520 ? -19.442 -37.995 77.436  1.00 25.99 ? 540  THR B CG2   1 
ATOM   9758  N  N     . ASN B 1 521 ? -20.826 -35.333 75.923  1.00 26.43 ? 541  ASN B N     1 
ATOM   9759  C  CA    . ASN B 1 521 ? -21.152 -34.056 76.528  1.00 26.76 ? 541  ASN B CA    1 
ATOM   9760  C  C     . ASN B 1 521 ? -20.388 -33.953 77.860  1.00 27.02 ? 541  ASN B C     1 
ATOM   9761  O  O     . ASN B 1 521 ? -20.675 -34.697 78.790  1.00 27.05 ? 541  ASN B O     1 
ATOM   9762  C  CB    . ASN B 1 521 ? -22.662 -33.954 76.744  1.00 26.54 ? 541  ASN B CB    1 
ATOM   9763  C  CG    . ASN B 1 521 ? -23.070 -32.659 77.427  1.00 26.68 ? 541  ASN B CG    1 
ATOM   9764  O  OD1   . ASN B 1 521 ? -22.309 -32.094 78.202  1.00 26.24 ? 541  ASN B OD1   1 
ATOM   9765  N  ND2   . ASN B 1 521 ? -24.277 -32.187 77.135  1.00 26.23 ? 541  ASN B ND2   1 
ATOM   9766  N  N     . PRO B 1 522 ? -19.411 -33.036 77.953  1.00 27.58 ? 542  PRO B N     1 
ATOM   9767  C  CA    . PRO B 1 522 ? -18.555 -33.005 79.138  1.00 28.00 ? 542  PRO B CA    1 
ATOM   9768  C  C     . PRO B 1 522 ? -19.241 -32.629 80.450  1.00 28.28 ? 542  PRO B C     1 
ATOM   9769  O  O     . PRO B 1 522 ? -18.611 -32.756 81.488  1.00 28.89 ? 542  PRO B O     1 
ATOM   9770  C  CB    . PRO B 1 522 ? -17.491 -31.962 78.784  1.00 28.14 ? 542  PRO B CB    1 
ATOM   9771  C  CG    . PRO B 1 522 ? -18.105 -31.116 77.770  1.00 28.22 ? 542  PRO B CG    1 
ATOM   9772  C  CD    . PRO B 1 522 ? -19.063 -31.970 77.000  1.00 27.63 ? 542  PRO B CD    1 
ATOM   9773  N  N     . TRP B 1 523 ? -20.500 -32.183 80.416  1.00 28.27 ? 543  TRP B N     1 
ATOM   9774  C  CA    . TRP B 1 523 ? -21.250 -31.867 81.642  1.00 28.15 ? 543  TRP B CA    1 
ATOM   9775  C  C     . TRP B 1 523 ? -22.513 -32.711 81.827  1.00 28.53 ? 543  TRP B C     1 
ATOM   9776  O  O     . TRP B 1 523 ? -23.245 -32.537 82.800  1.00 28.19 ? 543  TRP B O     1 
ATOM   9777  C  CB    . TRP B 1 523 ? -21.602 -30.371 81.690  1.00 28.06 ? 543  TRP B CB    1 
ATOM   9778  C  CG    . TRP B 1 523 ? -22.296 -29.852 80.471  1.00 26.42 ? 543  TRP B CG    1 
ATOM   9779  C  CD1   . TRP B 1 523 ? -21.711 -29.349 79.352  1.00 25.60 ? 543  TRP B CD1   1 
ATOM   9780  C  CD2   . TRP B 1 523 ? -23.706 -29.780 80.257  1.00 24.66 ? 543  TRP B CD2   1 
ATOM   9781  N  NE1   . TRP B 1 523 ? -22.670 -28.961 78.454  1.00 25.40 ? 543  TRP B NE1   1 
ATOM   9782  C  CE2   . TRP B 1 523 ? -23.904 -29.218 78.983  1.00 23.93 ? 543  TRP B CE2   1 
ATOM   9783  C  CE3   . TRP B 1 523 ? -24.822 -30.126 81.026  1.00 23.89 ? 543  TRP B CE3   1 
ATOM   9784  C  CZ2   . TRP B 1 523 ? -25.171 -28.995 78.450  1.00 24.22 ? 543  TRP B CZ2   1 
ATOM   9785  C  CZ3   . TRP B 1 523 ? -26.086 -29.904 80.497  1.00 25.21 ? 543  TRP B CZ3   1 
ATOM   9786  C  CH2   . TRP B 1 523 ? -26.247 -29.342 79.217  1.00 24.48 ? 543  TRP B CH2   1 
ATOM   9787  N  N     . SER B 1 524 ? -22.767 -33.619 80.889  1.00 28.99 ? 544  SER B N     1 
ATOM   9788  C  CA    . SER B 1 524 ? -23.864 -34.570 80.995  1.00 28.98 ? 544  SER B CA    1 
ATOM   9789  C  C     . SER B 1 524 ? -23.416 -35.828 80.242  1.00 29.65 ? 544  SER B C     1 
ATOM   9790  O  O     . SER B 1 524 ? -23.806 -36.035 79.081  1.00 29.53 ? 544  SER B O     1 
ATOM   9791  C  CB    . SER B 1 524 ? -25.146 -33.978 80.415  1.00 28.91 ? 544  SER B CB    1 
ATOM   9792  O  OG    . SER B 1 524 ? -26.248 -34.857 80.554  1.00 27.89 ? 544  SER B OG    1 
ATOM   9793  N  N     . PRO B 1 525 ? -22.578 -36.663 80.903  1.00 30.30 ? 545  PRO B N     1 
ATOM   9794  C  CA    . PRO B 1 525 ? -21.865 -37.820 80.314  1.00 30.43 ? 545  PRO B CA    1 
ATOM   9795  C  C     . PRO B 1 525 ? -22.735 -38.799 79.530  1.00 30.20 ? 545  PRO B C     1 
ATOM   9796  O  O     . PRO B 1 525 ? -22.249 -39.439 78.604  1.00 30.47 ? 545  PRO B O     1 
ATOM   9797  C  CB    . PRO B 1 525 ? -21.258 -38.542 81.527  1.00 30.80 ? 545  PRO B CB    1 
ATOM   9798  C  CG    . PRO B 1 525 ? -21.389 -37.628 82.688  1.00 30.70 ? 545  PRO B CG    1 
ATOM   9799  C  CD    . PRO B 1 525 ? -22.278 -36.491 82.341  1.00 30.56 ? 545  PRO B CD    1 
ATOM   9800  N  N     . ARG B 1 526 ? -24.007 -38.913 79.894  1.00 29.98 ? 546  ARG B N     1 
ATOM   9801  C  CA    . ARG B 1 526 ? -24.927 -39.789 79.183  1.00 29.86 ? 546  ARG B CA    1 
ATOM   9802  C  C     . ARG B 1 526 ? -25.382 -39.208 77.843  1.00 29.56 ? 546  ARG B C     1 
ATOM   9803  O  O     . ARG B 1 526 ? -26.132 -39.853 77.117  1.00 29.86 ? 546  ARG B O     1 
ATOM   9804  C  CB    . ARG B 1 526 ? -26.151 -40.090 80.050  1.00 29.93 ? 546  ARG B CB    1 
ATOM   9805  C  CG    . ARG B 1 526 ? -25.810 -40.751 81.385  1.00 30.74 ? 546  ARG B CG    1 
ATOM   9806  C  CD    . ARG B 1 526 ? -27.073 -41.057 82.192  1.00 32.05 ? 546  ARG B CD    1 
ATOM   9807  N  N     . HIS B 1 527 ? -24.943 -37.995 77.516  1.00 28.92 ? 547  HIS B N     1 
ATOM   9808  C  CA    . HIS B 1 527 ? -25.372 -37.328 76.295  1.00 28.46 ? 547  HIS B CA    1 
ATOM   9809  C  C     . HIS B 1 527 ? -24.181 -37.017 75.408  1.00 27.76 ? 547  HIS B C     1 
ATOM   9810  O  O     . HIS B 1 527 ? -23.036 -37.220 75.802  1.00 27.39 ? 547  HIS B O     1 
ATOM   9811  C  CB    . HIS B 1 527 ? -26.161 -36.067 76.646  1.00 28.40 ? 547  HIS B CB    1 
ATOM   9812  C  CG    . HIS B 1 527 ? -27.372 -36.357 77.473  1.00 29.33 ? 547  HIS B CG    1 
ATOM   9813  N  ND1   . HIS B 1 527 ? -27.356 -36.332 78.850  1.00 30.04 ? 547  HIS B ND1   1 
ATOM   9814  C  CD2   . HIS B 1 527 ? -28.619 -36.741 77.118  1.00 30.18 ? 547  HIS B CD2   1 
ATOM   9815  C  CE1   . HIS B 1 527 ? -28.548 -36.667 79.307  1.00 30.17 ? 547  HIS B CE1   1 
ATOM   9816  N  NE2   . HIS B 1 527 ? -29.333 -36.921 78.276  1.00 29.97 ? 547  HIS B NE2   1 
ATOM   9817  N  N     . ARG B 1 528 ? -24.475 -36.547 74.203  1.00 27.24 ? 548  ARG B N     1 
ATOM   9818  C  CA    . ARG B 1 528 ? -23.467 -36.282 73.192  1.00 26.83 ? 548  ARG B CA    1 
ATOM   9819  C  C     . ARG B 1 528 ? -23.491 -34.816 72.800  1.00 26.23 ? 548  ARG B C     1 
ATOM   9820  O  O     . ARG B 1 528 ? -24.546 -34.187 72.810  1.00 26.45 ? 548  ARG B O     1 
ATOM   9821  C  CB    . ARG B 1 528 ? -23.761 -37.101 71.926  1.00 27.00 ? 548  ARG B CB    1 
ATOM   9822  C  CG    . ARG B 1 528 ? -24.092 -38.565 72.137  1.00 27.21 ? 548  ARG B CG    1 
ATOM   9823  C  CD    . ARG B 1 528 ? -22.935 -39.329 72.708  1.00 27.53 ? 548  ARG B CD    1 
ATOM   9824  N  NE    . ARG B 1 528 ? -21.714 -39.194 71.918  1.00 28.48 ? 548  ARG B NE    1 
ATOM   9825  C  CZ    . ARG B 1 528 ? -20.536 -39.690 72.291  1.00 29.29 ? 548  ARG B CZ    1 
ATOM   9826  N  NH1   . ARG B 1 528 ? -20.424 -40.368 73.431  1.00 29.84 ? 548  ARG B NH1   1 
ATOM   9827  N  NH2   . ARG B 1 528 ? -19.467 -39.510 71.526  1.00 29.20 ? 548  ARG B NH2   1 
ATOM   9828  N  N     . VAL B 1 529 ? -22.334 -34.281 72.430  1.00 25.24 ? 549  VAL B N     1 
ATOM   9829  C  CA    . VAL B 1 529 ? -22.269 -33.008 71.730  1.00 24.45 ? 549  VAL B CA    1 
ATOM   9830  C  C     . VAL B 1 529 ? -21.794 -33.297 70.307  1.00 24.31 ? 549  VAL B C     1 
ATOM   9831  O  O     . VAL B 1 529 ? -20.691 -33.805 70.107  1.00 23.55 ? 549  VAL B O     1 
ATOM   9832  C  CB    . VAL B 1 529 ? -21.333 -32.005 72.445  1.00 24.43 ? 549  VAL B CB    1 
ATOM   9833  C  CG1   . VAL B 1 529 ? -21.064 -30.792 71.564  1.00 24.01 ? 549  VAL B CG1   1 
ATOM   9834  C  CG2   . VAL B 1 529 ? -21.938 -31.578 73.780  1.00 23.79 ? 549  VAL B CG2   1 
ATOM   9835  N  N     . VAL B 1 530 ? -22.655 -33.013 69.330  1.00 24.25 ? 550  VAL B N     1 
ATOM   9836  C  CA    . VAL B 1 530 ? -22.291 -33.090 67.913  1.00 24.38 ? 550  VAL B CA    1 
ATOM   9837  C  C     . VAL B 1 530 ? -22.207 -31.655 67.399  1.00 24.52 ? 550  VAL B C     1 
ATOM   9838  O  O     . VAL B 1 530 ? -23.228 -30.976 67.293  1.00 24.59 ? 550  VAL B O     1 
ATOM   9839  C  CB    . VAL B 1 530 ? -23.310 -33.937 67.109  1.00 24.35 ? 550  VAL B CB    1 
ATOM   9840  C  CG1   . VAL B 1 530 ? -23.011 -33.898 65.616  1.00 24.80 ? 550  VAL B CG1   1 
ATOM   9841  C  CG2   . VAL B 1 530 ? -23.304 -35.382 67.620  1.00 23.37 ? 550  VAL B CG2   1 
ATOM   9842  N  N     . GLN B 1 531 ? -20.990 -31.194 67.117  1.00 24.60 ? 551  GLN B N     1 
ATOM   9843  C  CA    . GLN B 1 531 ? -20.729 -29.768 66.923  1.00 24.70 ? 551  GLN B CA    1 
ATOM   9844  C  C     . GLN B 1 531 ? -19.623 -29.471 65.909  1.00 24.94 ? 551  GLN B C     1 
ATOM   9845  O  O     . GLN B 1 531 ? -18.791 -30.337 65.620  1.00 24.89 ? 551  GLN B O     1 
ATOM   9846  C  CB    . GLN B 1 531 ? -20.341 -29.120 68.252  1.00 24.69 ? 551  GLN B CB    1 
ATOM   9847  C  CG    . GLN B 1 531 ? -18.929 -29.480 68.765  1.00 25.36 ? 551  GLN B CG    1 
ATOM   9848  C  CD    . GLN B 1 531 ? -18.410 -28.503 69.810  1.00 25.29 ? 551  GLN B CD    1 
ATOM   9849  O  OE1   . GLN B 1 531 ? -18.949 -27.421 69.960  1.00 26.18 ? 551  GLN B OE1   1 
ATOM   9850  N  NE2   . GLN B 1 531 ? -17.340 -28.874 70.513  1.00 25.96 ? 551  GLN B NE2   1 
ATOM   9851  N  N     . PRO B 1 532 ? -19.604 -28.229 65.385  1.00 25.05 ? 552  PRO B N     1 
ATOM   9852  C  CA    . PRO B 1 532 ? -18.576 -27.777 64.459  1.00 25.26 ? 552  PRO B CA    1 
ATOM   9853  C  C     . PRO B 1 532 ? -17.178 -27.745 65.047  1.00 25.61 ? 552  PRO B C     1 
ATOM   9854  O  O     . PRO B 1 532 ? -17.004 -27.363 66.207  1.00 25.41 ? 552  PRO B O     1 
ATOM   9855  C  CB    . PRO B 1 532 ? -19.001 -26.346 64.134  1.00 25.15 ? 552  PRO B CB    1 
ATOM   9856  C  CG    . PRO B 1 532 ? -20.457 -26.322 64.347  1.00 25.48 ? 552  PRO B CG    1 
ATOM   9857  C  CD    . PRO B 1 532 ? -20.716 -27.269 65.474  1.00 24.90 ? 552  PRO B CD    1 
ATOM   9858  N  N     . THR B 1 533 ? -16.204 -28.148 64.234  1.00 25.83 ? 553  THR B N     1 
ATOM   9859  C  CA    . THR B 1 533 ? -14.797 -27.863 64.477  1.00 26.18 ? 553  THR B CA    1 
ATOM   9860  C  C     . THR B 1 533 ? -14.210 -27.236 63.223  1.00 27.10 ? 553  THR B C     1 
ATOM   9861  O  O     . THR B 1 533 ? -14.769 -27.344 62.133  1.00 26.71 ? 553  THR B O     1 
ATOM   9862  C  CB    . THR B 1 533 ? -13.986 -29.118 64.777  1.00 26.30 ? 553  THR B CB    1 
ATOM   9863  O  OG1   . THR B 1 533 ? -13.927 -29.934 63.600  1.00 25.49 ? 553  THR B OG1   1 
ATOM   9864  C  CG2   . THR B 1 533 ? -14.592 -29.915 65.938  1.00 25.89 ? 553  THR B CG2   1 
ATOM   9865  N  N     . LEU B 1 534 ? -13.058 -26.602 63.392  1.00 28.30 ? 554  LEU B N     1 
ATOM   9866  C  CA    . LEU B 1 534 ? -12.386 -25.879 62.330  1.00 29.17 ? 554  LEU B CA    1 
ATOM   9867  C  C     . LEU B 1 534 ? -11.288 -26.758 61.773  1.00 29.98 ? 554  LEU B C     1 
ATOM   9868  O  O     . LEU B 1 534 ? -10.379 -27.128 62.503  1.00 30.41 ? 554  LEU B O     1 
ATOM   9869  C  CB    . LEU B 1 534 ? -11.803 -24.583 62.897  1.00 29.44 ? 554  LEU B CB    1 
ATOM   9870  C  CG    . LEU B 1 534 ? -10.882 -23.691 62.058  1.00 30.32 ? 554  LEU B CG    1 
ATOM   9871  C  CD1   . LEU B 1 534 ? -11.324 -23.593 60.619  1.00 30.84 ? 554  LEU B CD1   1 
ATOM   9872  C  CD2   . LEU B 1 534 ? -10.824 -22.310 62.711  1.00 31.34 ? 554  LEU B CD2   1 
ATOM   9873  N  N     . GLU B 1 535 ? -11.373 -27.086 60.482  1.00 30.76 ? 555  GLU B N     1 
ATOM   9874  C  CA    . GLU B 1 535 ? -10.403 -27.964 59.822  1.00 31.10 ? 555  GLU B CA    1 
ATOM   9875  C  C     . GLU B 1 535 ? -9.586  -27.175 58.809  1.00 30.85 ? 555  GLU B C     1 
ATOM   9876  O  O     . GLU B 1 535 ? -10.152 -26.443 57.996  1.00 30.91 ? 555  GLU B O     1 
ATOM   9877  C  CB    . GLU B 1 535 ? -11.151 -29.099 59.130  1.00 31.77 ? 555  GLU B CB    1 
ATOM   9878  C  CG    . GLU B 1 535 ? -10.296 -30.085 58.347  1.00 33.59 ? 555  GLU B CG    1 
ATOM   9879  C  CD    . GLU B 1 535 ? -11.141 -31.012 57.485  1.00 35.42 ? 555  GLU B CD    1 
ATOM   9880  O  OE1   . GLU B 1 535 ? -11.520 -30.609 56.362  1.00 36.37 ? 555  GLU B OE1   1 
ATOM   9881  O  OE2   . GLU B 1 535 ? -11.425 -32.144 57.935  1.00 38.55 ? 555  GLU B OE2   1 
ATOM   9882  N  N     . GLN B 1 536 ? -8.263  -27.331 58.866  1.00 30.21 ? 556  GLN B N     1 
ATOM   9883  C  CA    . GLN B 1 536 ? -7.342  -26.628 57.977  1.00 30.25 ? 556  GLN B CA    1 
ATOM   9884  C  C     . GLN B 1 536 ? -6.663  -27.629 57.057  1.00 30.32 ? 556  GLN B C     1 
ATOM   9885  O  O     . GLN B 1 536 ? -6.217  -28.682 57.507  1.00 30.98 ? 556  GLN B O     1 
ATOM   9886  C  CB    . GLN B 1 536 ? -6.291  -25.859 58.779  1.00 30.01 ? 556  GLN B CB    1 
ATOM   9887  N  N     . THR B 1 537 ? -6.607  -27.313 55.768  1.00 30.06 ? 557  THR B N     1 
ATOM   9888  C  CA    . THR B 1 537 ? -5.949  -28.164 54.781  1.00 29.87 ? 557  THR B CA    1 
ATOM   9889  C  C     . THR B 1 537 ? -4.828  -27.386 54.129  1.00 29.89 ? 557  THR B C     1 
ATOM   9890  O  O     . THR B 1 537 ? -5.047  -26.284 53.652  1.00 29.43 ? 557  THR B O     1 
ATOM   9891  C  CB    . THR B 1 537 ? -6.927  -28.601 53.690  1.00 29.72 ? 557  THR B CB    1 
ATOM   9892  O  OG1   . THR B 1 537 ? -8.019  -29.305 54.288  1.00 30.01 ? 557  THR B OG1   1 
ATOM   9893  C  CG2   . THR B 1 537 ? -6.240  -29.489 52.659  1.00 29.40 ? 557  THR B CG2   1 
ATOM   9894  N  N     . GLN B 1 538 ? -3.625  -27.954 54.131  1.00 30.27 ? 558  GLN B N     1 
ATOM   9895  C  CA    . GLN B 1 538 ? -2.490  -27.362 53.423  1.00 30.67 ? 558  GLN B CA    1 
ATOM   9896  C  C     . GLN B 1 538 ? -2.384  -27.961 52.023  1.00 30.12 ? 558  GLN B C     1 
ATOM   9897  O  O     . GLN B 1 538 ? -2.934  -29.022 51.748  1.00 30.49 ? 558  GLN B O     1 
ATOM   9898  C  CB    . GLN B 1 538 ? -1.189  -27.587 54.192  1.00 31.04 ? 558  GLN B CB    1 
ATOM   9899  C  CG    . GLN B 1 538 ? -1.204  -27.063 55.635  1.00 33.07 ? 558  GLN B CG    1 
ATOM   9900  C  CD    . GLN B 1 538 ? -1.624  -25.600 55.747  1.00 35.07 ? 558  GLN B CD    1 
ATOM   9901  O  OE1   . GLN B 1 538 ? -1.076  -24.731 55.069  1.00 36.88 ? 558  GLN B OE1   1 
ATOM   9902  N  NE2   . GLN B 1 538 ? -2.604  -25.327 56.610  1.00 36.56 ? 558  GLN B NE2   1 
ATOM   9903  N  N     . TYR B 1 539 ? -1.695  -27.255 51.139  1.00 29.83 ? 559  TYR B N     1 
ATOM   9904  C  CA    . TYR B 1 539 ? -1.504  -27.681 49.749  1.00 29.50 ? 559  TYR B CA    1 
ATOM   9905  C  C     . TYR B 1 539 ? -0.033  -27.497 49.387  1.00 29.52 ? 559  TYR B C     1 
ATOM   9906  O  O     . TYR B 1 539 ? 0.518   -26.409 49.541  1.00 29.49 ? 559  TYR B O     1 
ATOM   9907  C  CB    . TYR B 1 539 ? -2.379  -26.845 48.809  1.00 29.21 ? 559  TYR B CB    1 
ATOM   9908  C  CG    . TYR B 1 539 ? -3.864  -27.006 49.056  1.00 28.65 ? 559  TYR B CG    1 
ATOM   9909  C  CD1   . TYR B 1 539 ? -4.481  -26.409 50.158  1.00 27.80 ? 559  TYR B CD1   1 
ATOM   9910  C  CD2   . TYR B 1 539 ? -4.652  -27.760 48.194  1.00 28.13 ? 559  TYR B CD2   1 
ATOM   9911  C  CE1   . TYR B 1 539 ? -5.834  -26.572 50.397  1.00 28.10 ? 559  TYR B CE1   1 
ATOM   9912  C  CE2   . TYR B 1 539 ? -6.004  -27.919 48.421  1.00 28.20 ? 559  TYR B CE2   1 
ATOM   9913  C  CZ    . TYR B 1 539 ? -6.591  -27.324 49.522  1.00 27.54 ? 559  TYR B CZ    1 
ATOM   9914  O  OH    . TYR B 1 539 ? -7.934  -27.478 49.737  1.00 28.33 ? 559  TYR B OH    1 
ATOM   9915  N  N     . SER B 1 540 ? 0.593   -28.565 48.908  1.00 29.61 ? 560  SER B N     1 
ATOM   9916  C  CA    . SER B 1 540 ? 2.022   -28.556 48.616  1.00 29.81 ? 560  SER B CA    1 
ATOM   9917  C  C     . SER B 1 540 ? 2.361   -28.464 47.129  1.00 29.82 ? 560  SER B C     1 
ATOM   9918  O  O     . SER B 1 540 ? 3.430   -27.954 46.771  1.00 30.05 ? 560  SER B O     1 
ATOM   9919  C  CB    . SER B 1 540 ? 2.667   -29.808 49.203  1.00 29.96 ? 560  SER B CB    1 
ATOM   9920  O  OG    . SER B 1 540 ? 2.791   -29.683 50.605  1.00 30.46 ? 560  SER B OG    1 
ATOM   9921  N  N     . TRP B 1 541 ? 1.465   -28.963 46.278  1.00 29.43 ? 561  TRP B N     1 
ATOM   9922  C  CA    . TRP B 1 541 ? 1.744   -29.116 44.851  1.00 29.58 ? 561  TRP B CA    1 
ATOM   9923  C  C     . TRP B 1 541 ? 0.638   -28.501 44.001  1.00 29.09 ? 561  TRP B C     1 
ATOM   9924  O  O     . TRP B 1 541 ? -0.548  -28.638 44.319  1.00 29.51 ? 561  TRP B O     1 
ATOM   9925  C  CB    . TRP B 1 541 ? 1.895   -30.604 44.511  1.00 29.66 ? 561  TRP B CB    1 
ATOM   9926  C  CG    . TRP B 1 541 ? 2.869   -31.311 45.395  1.00 31.21 ? 561  TRP B CG    1 
ATOM   9927  C  CD1   . TRP B 1 541 ? 2.576   -32.140 46.445  1.00 32.67 ? 561  TRP B CD1   1 
ATOM   9928  C  CD2   . TRP B 1 541 ? 4.297   -31.243 45.325  1.00 32.32 ? 561  TRP B CD2   1 
ATOM   9929  N  NE1   . TRP B 1 541 ? 3.732   -32.596 47.022  1.00 32.85 ? 561  TRP B NE1   1 
ATOM   9930  C  CE2   . TRP B 1 541 ? 4.804   -32.060 46.356  1.00 33.69 ? 561  TRP B CE2   1 
ATOM   9931  C  CE3   . TRP B 1 541 ? 5.198   -30.589 44.477  1.00 33.40 ? 561  TRP B CE3   1 
ATOM   9932  C  CZ2   . TRP B 1 541 ? 6.176   -32.229 46.570  1.00 33.62 ? 561  TRP B CZ2   1 
ATOM   9933  C  CZ3   . TRP B 1 541 ? 6.562   -30.752 44.692  1.00 33.26 ? 561  TRP B CZ3   1 
ATOM   9934  C  CH2   . TRP B 1 541 ? 7.036   -31.565 45.729  1.00 33.86 ? 561  TRP B CH2   1 
ATOM   9935  N  N     . GLU B 1 542 ? 1.028   -27.838 42.914  1.00 28.69 ? 562  GLU B N     1 
ATOM   9936  C  CA    . GLU B 1 542 ? 0.076   -27.150 42.030  1.00 28.30 ? 562  GLU B CA    1 
ATOM   9937  C  C     . GLU B 1 542 ? -1.221  -27.936 41.790  1.00 28.10 ? 562  GLU B C     1 
ATOM   9938  O  O     . GLU B 1 542 ? -2.319  -27.397 41.973  1.00 28.18 ? 562  GLU B O     1 
ATOM   9939  C  CB    . GLU B 1 542 ? 0.736   -26.826 40.690  1.00 28.23 ? 562  GLU B CB    1 
ATOM   9940  C  CG    . GLU B 1 542 ? 1.686   -25.649 40.752  1.00 27.91 ? 562  GLU B CG    1 
ATOM   9941  C  CD    . GLU B 1 542 ? 2.359   -25.368 39.427  1.00 27.67 ? 562  GLU B CD    1 
ATOM   9942  O  OE1   . GLU B 1 542 ? 2.674   -26.336 38.705  1.00 27.24 ? 562  GLU B OE1   1 
ATOM   9943  O  OE2   . GLU B 1 542 ? 2.590   -24.181 39.101  1.00 26.67 ? 562  GLU B OE2   1 
ATOM   9944  N  N     . ARG B 1 543 ? -1.080  -29.207 41.415  1.00 27.78 ? 563  ARG B N     1 
ATOM   9945  C  CA    . ARG B 1 543 ? -2.221  -30.067 41.060  1.00 27.57 ? 563  ARG B CA    1 
ATOM   9946  C  C     . ARG B 1 543 ? -3.262  -30.214 42.176  1.00 27.32 ? 563  ARG B C     1 
ATOM   9947  O  O     . ARG B 1 543 ? -4.467  -30.329 41.897  1.00 27.30 ? 563  ARG B O     1 
ATOM   9948  C  CB    . ARG B 1 543 ? -1.729  -31.446 40.616  1.00 27.71 ? 563  ARG B CB    1 
ATOM   9949  C  CG    . ARG B 1 543 ? -2.827  -32.469 40.270  1.00 28.25 ? 563  ARG B CG    1 
ATOM   9950  C  CD    . ARG B 1 543 ? -3.860  -31.968 39.248  1.00 29.18 ? 563  ARG B CD    1 
ATOM   9951  N  NE    . ARG B 1 543 ? -3.287  -31.651 37.940  1.00 28.81 ? 563  ARG B NE    1 
ATOM   9952  C  CZ    . ARG B 1 543 ? -3.957  -31.092 36.931  1.00 28.59 ? 563  ARG B CZ    1 
ATOM   9953  N  NH1   . ARG B 1 543 ? -5.245  -30.766 37.055  1.00 28.33 ? 563  ARG B NH1   1 
ATOM   9954  N  NH2   . ARG B 1 543 ? -3.335  -30.860 35.776  1.00 28.27 ? 563  ARG B NH2   1 
ATOM   9955  N  N     . GLN B 1 544 ? -2.803  -30.214 43.427  1.00 26.61 ? 564  GLN B N     1 
ATOM   9956  C  CA    . GLN B 1 544 ? -3.708  -30.275 44.585  1.00 26.05 ? 564  GLN B CA    1 
ATOM   9957  C  C     . GLN B 1 544 ? -4.609  -29.036 44.674  1.00 25.23 ? 564  GLN B C     1 
ATOM   9958  O  O     . GLN B 1 544 ? -5.705  -29.107 45.206  1.00 25.49 ? 564  GLN B O     1 
ATOM   9959  C  CB    . GLN B 1 544 ? -2.900  -30.376 45.887  1.00 26.09 ? 564  GLN B CB    1 
ATOM   9960  C  CG    . GLN B 1 544 ? -2.039  -31.639 46.027  1.00 25.81 ? 564  GLN B CG    1 
ATOM   9961  C  CD    . GLN B 1 544 ? -1.170  -31.616 47.281  1.00 26.30 ? 564  GLN B CD    1 
ATOM   9962  O  OE1   . GLN B 1 544 ? -0.476  -30.633 47.556  1.00 25.45 ? 564  GLN B OE1   1 
ATOM   9963  N  NE2   . GLN B 1 544 ? -1.210  -32.701 48.046  1.00 25.76 ? 564  GLN B NE2   1 
ATOM   9964  N  N     . ALA B 1 545 ? -4.118  -27.907 44.171  1.00 24.85 ? 565  ALA B N     1 
ATOM   9965  C  CA    . ALA B 1 545 ? -4.826  -26.624 44.209  1.00 24.34 ? 565  ALA B CA    1 
ATOM   9966  C  C     . ALA B 1 545 ? -5.523  -26.272 42.878  1.00 24.02 ? 565  ALA B C     1 
ATOM   9967  O  O     . ALA B 1 545 ? -5.883  -25.111 42.657  1.00 23.69 ? 565  ALA B O     1 
ATOM   9968  C  CB    . ALA B 1 545 ? -3.855  -25.531 44.586  1.00 24.23 ? 565  ALA B CB    1 
ATOM   9969  N  N     . ALA B 1 546 ? -5.685  -27.261 41.998  1.00 23.54 ? 566  ALA B N     1 
ATOM   9970  C  CA    . ALA B 1 546 ? -6.426  -27.092 40.749  1.00 23.62 ? 566  ALA B CA    1 
ATOM   9971  C  C     . ALA B 1 546 ? -7.801  -27.695 40.949  1.00 23.70 ? 566  ALA B C     1 
ATOM   9972  O  O     . ALA B 1 546 ? -7.965  -28.905 40.855  1.00 24.09 ? 566  ALA B O     1 
ATOM   9973  C  CB    . ALA B 1 546 ? -5.712  -27.785 39.608  1.00 23.24 ? 566  ALA B CB    1 
ATOM   9974  N  N     . PHE B 1 547 ? -8.780  -26.855 41.250  1.00 24.18 ? 567  PHE B N     1 
ATOM   9975  C  CA    . PHE B 1 547 ? -10.128 -27.320 41.569  1.00 24.68 ? 567  PHE B CA    1 
ATOM   9976  C  C     . PHE B 1 547 ? -10.954 -27.373 40.301  1.00 25.72 ? 567  PHE B C     1 
ATOM   9977  O  O     . PHE B 1 547 ? -11.140 -26.352 39.647  1.00 25.58 ? 567  PHE B O     1 
ATOM   9978  C  CB    . PHE B 1 547 ? -10.792 -26.378 42.575  1.00 24.45 ? 567  PHE B CB    1 
ATOM   9979  C  CG    . PHE B 1 547 ? -10.089 -26.316 43.896  1.00 23.29 ? 567  PHE B CG    1 
ATOM   9980  C  CD1   . PHE B 1 547 ? -9.004  -25.476 44.078  1.00 22.21 ? 567  PHE B CD1   1 
ATOM   9981  C  CD2   . PHE B 1 547 ? -10.495 -27.123 44.954  1.00 23.16 ? 567  PHE B CD2   1 
ATOM   9982  C  CE1   . PHE B 1 547 ? -8.340  -25.421 45.296  1.00 22.75 ? 567  PHE B CE1   1 
ATOM   9983  C  CE2   . PHE B 1 547 ? -9.839  -27.072 46.182  1.00 22.34 ? 567  PHE B CE2   1 
ATOM   9984  C  CZ    . PHE B 1 547 ? -8.757  -26.225 46.348  1.00 22.64 ? 567  PHE B CZ    1 
ATOM   9985  N  N     . ARG B 1 548 ? -11.420 -28.563 39.941  1.00 27.22 ? 568  ARG B N     1 
ATOM   9986  C  CA    . ARG B 1 548 ? -12.353 -28.723 38.829  1.00 28.75 ? 568  ARG B CA    1 
ATOM   9987  C  C     . ARG B 1 548 ? -13.759 -28.438 39.325  1.00 29.71 ? 568  ARG B C     1 
ATOM   9988  O  O     . ARG B 1 548 ? -14.013 -28.447 40.528  1.00 29.96 ? 568  ARG B O     1 
ATOM   9989  C  CB    . ARG B 1 548 ? -12.292 -30.138 38.251  1.00 29.18 ? 568  ARG B CB    1 
ATOM   9990  C  CG    . ARG B 1 548 ? -10.976 -30.467 37.555  1.00 30.84 ? 568  ARG B CG    1 
ATOM   9991  C  CD    . ARG B 1 548 ? -10.821 -31.955 37.326  1.00 32.96 ? 568  ARG B CD    1 
ATOM   9992  N  NE    . ARG B 1 548 ? -9.589  -32.252 36.598  1.00 35.66 ? 568  ARG B NE    1 
ATOM   9993  N  N     . PHE B 1 549 ? -14.669 -28.184 38.393  1.00 30.99 ? 569  PHE B N     1 
ATOM   9994  C  CA    . PHE B 1 549 ? -16.068 -27.938 38.733  1.00 31.96 ? 569  PHE B CA    1 
ATOM   9995  C  C     . PHE B 1 549 ? -16.725 -29.163 39.367  1.00 33.14 ? 569  PHE B C     1 
ATOM   9996  O  O     . PHE B 1 549 ? -17.698 -29.024 40.095  1.00 33.90 ? 569  PHE B O     1 
ATOM   9997  C  CB    . PHE B 1 549 ? -16.860 -27.484 37.499  1.00 31.72 ? 569  PHE B CB    1 
ATOM   9998  C  CG    . PHE B 1 549 ? -16.570 -26.068 37.086  1.00 31.00 ? 569  PHE B CG    1 
ATOM   9999  C  CD1   . PHE B 1 549 ? -17.063 -25.006 37.833  1.00 30.39 ? 569  PHE B CD1   1 
ATOM   10000 C  CD2   . PHE B 1 549 ? -15.802 -25.791 35.959  1.00 30.12 ? 569  PHE B CD2   1 
ATOM   10001 C  CE1   . PHE B 1 549 ? -16.794 -23.690 37.461  1.00 30.56 ? 569  PHE B CE1   1 
ATOM   10002 C  CE2   . PHE B 1 549 ? -15.534 -24.475 35.584  1.00 29.82 ? 569  PHE B CE2   1 
ATOM   10003 C  CZ    . PHE B 1 549 ? -16.026 -23.428 36.337  1.00 30.22 ? 569  PHE B CZ    1 
ATOM   10004 N  N     . LYS B 1 550 ? -16.209 -30.354 39.079  1.00 34.22 ? 570  LYS B N     1 
ATOM   10005 C  CA    . LYS B 1 550 ? -16.670 -31.575 39.746  1.00 35.03 ? 570  LYS B CA    1 
ATOM   10006 C  C     . LYS B 1 550 ? -16.362 -31.523 41.242  1.00 36.00 ? 570  LYS B C     1 
ATOM   10007 O  O     . LYS B 1 550 ? -17.211 -31.838 42.060  1.00 36.50 ? 570  LYS B O     1 
ATOM   10008 C  CB    . LYS B 1 550 ? -15.993 -32.804 39.137  1.00 34.90 ? 570  LYS B CB    1 
ATOM   10009 N  N     . ARG B 1 551 ? -15.142 -31.107 41.579  1.00 37.04 ? 571  ARG B N     1 
ATOM   10010 C  CA    . ARG B 1 551 ? -14.662 -31.047 42.971  1.00 37.66 ? 571  ARG B CA    1 
ATOM   10011 C  C     . ARG B 1 551 ? -15.466 -30.024 43.804  1.00 37.67 ? 571  ARG B C     1 
ATOM   10012 O  O     . ARG B 1 551 ? -15.905 -28.984 43.288  1.00 38.03 ? 571  ARG B O     1 
ATOM   10013 C  CB    . ARG B 1 551 ? -13.161 -30.689 42.966  1.00 38.18 ? 571  ARG B CB    1 
ATOM   10014 C  CG    . ARG B 1 551 ? -12.340 -31.133 44.190  1.00 39.66 ? 571  ARG B CG    1 
ATOM   10015 C  CD    . ARG B 1 551 ? -10.843 -31.000 43.887  1.00 41.20 ? 571  ARG B CD    1 
ATOM   10016 N  NE    . ARG B 1 551 ? -10.006 -30.916 45.082  1.00 42.51 ? 571  ARG B NE    1 
ATOM   10017 C  CZ    . ARG B 1 551 ? -8.724  -30.544 45.094  1.00 43.08 ? 571  ARG B CZ    1 
ATOM   10018 N  NH1   . ARG B 1 551 ? -8.093  -30.205 43.971  1.00 43.85 ? 571  ARG B NH1   1 
ATOM   10019 N  NH2   . ARG B 1 551 ? -8.063  -30.501 46.246  1.00 43.29 ? 571  ARG B NH2   1 
ATOM   10020 N  N     . LYS B 1 552 ? -15.674 -30.332 45.083  1.00 37.18 ? 572  LYS B N     1 
ATOM   10021 C  CA    . LYS B 1 552 ? -16.342 -29.406 46.010  1.00 36.40 ? 572  LYS B CA    1 
ATOM   10022 C  C     . LYS B 1 552 ? -15.369 -28.283 46.362  1.00 35.27 ? 572  LYS B C     1 
ATOM   10023 O  O     . LYS B 1 552 ? -14.241 -28.551 46.778  1.00 35.85 ? 572  LYS B O     1 
ATOM   10024 C  CB    . LYS B 1 552 ? -16.783 -30.145 47.283  1.00 36.53 ? 572  LYS B CB    1 
ATOM   10025 N  N     . LEU B 1 553 ? -15.785 -27.035 46.163  1.00 33.70 ? 573  LEU B N     1 
ATOM   10026 C  CA    . LEU B 1 553 ? -14.911 -25.888 46.430  1.00 32.60 ? 573  LEU B CA    1 
ATOM   10027 C  C     . LEU B 1 553 ? -15.003 -25.532 47.910  1.00 31.18 ? 573  LEU B C     1 
ATOM   10028 O  O     . LEU B 1 553 ? -16.092 -25.264 48.397  1.00 30.42 ? 573  LEU B O     1 
ATOM   10029 C  CB    . LEU B 1 553 ? -15.317 -24.688 45.565  1.00 32.67 ? 573  LEU B CB    1 
ATOM   10030 C  CG    . LEU B 1 553 ? -14.269 -23.616 45.236  1.00 33.03 ? 573  LEU B CG    1 
ATOM   10031 C  CD1   . LEU B 1 553 ? -12.974 -24.202 44.634  1.00 32.28 ? 573  LEU B CD1   1 
ATOM   10032 C  CD2   . LEU B 1 553 ? -14.881 -22.610 44.266  1.00 31.25 ? 573  LEU B CD2   1 
ATOM   10033 N  N     . PRO B 1 554 ? -13.866 -25.543 48.635  1.00 29.86 ? 574  PRO B N     1 
ATOM   10034 C  CA    . PRO B 1 554 ? -13.913 -25.151 50.044  1.00 29.25 ? 574  PRO B CA    1 
ATOM   10035 C  C     . PRO B 1 554 ? -14.463 -23.734 50.259  1.00 28.66 ? 574  PRO B C     1 
ATOM   10036 O  O     . PRO B 1 554 ? -14.320 -22.865 49.395  1.00 28.00 ? 574  PRO B O     1 
ATOM   10037 C  CB    . PRO B 1 554 ? -12.443 -25.217 50.485  1.00 29.38 ? 574  PRO B CB    1 
ATOM   10038 C  CG    . PRO B 1 554 ? -11.781 -26.105 49.505  1.00 29.82 ? 574  PRO B CG    1 
ATOM   10039 C  CD    . PRO B 1 554 ? -12.503 -25.908 48.211  1.00 29.71 ? 574  PRO B CD    1 
ATOM   10040 N  N     . LYS B 1 555 ? -15.074 -23.510 51.415  1.00 27.96 ? 575  LYS B N     1 
ATOM   10041 C  CA    . LYS B 1 555 ? -15.691 -22.226 51.713  1.00 27.66 ? 575  LYS B CA    1 
ATOM   10042 C  C     . LYS B 1 555 ? -14.656 -21.142 52.004  1.00 26.82 ? 575  LYS B C     1 
ATOM   10043 O  O     . LYS B 1 555 ? -14.924 -19.971 51.748  1.00 27.05 ? 575  LYS B O     1 
ATOM   10044 C  CB    . LYS B 1 555 ? -16.678 -22.361 52.880  1.00 27.97 ? 575  LYS B CB    1 
ATOM   10045 C  CG    . LYS B 1 555 ? -17.791 -23.372 52.633  1.00 29.36 ? 575  LYS B CG    1 
ATOM   10046 C  CD    . LYS B 1 555 ? -18.655 -22.985 51.447  1.00 31.13 ? 575  LYS B CD    1 
ATOM   10047 C  CE    . LYS B 1 555 ? -19.663 -24.083 51.096  1.00 32.95 ? 575  LYS B CE    1 
ATOM   10048 N  NZ    . LYS B 1 555 ? -20.150 -23.906 49.701  1.00 32.44 ? 575  LYS B NZ    1 
ATOM   10049 N  N     . TYR B 1 556 ? -13.484 -21.523 52.520  1.00 25.42 ? 576  TYR B N     1 
ATOM   10050 C  CA    . TYR B 1 556 ? -12.387 -20.569 52.743  1.00 24.52 ? 576  TYR B CA    1 
ATOM   10051 C  C     . TYR B 1 556 ? -11.179 -20.901 51.874  1.00 24.06 ? 576  TYR B C     1 
ATOM   10052 O  O     . TYR B 1 556 ? -10.540 -21.929 52.057  1.00 23.40 ? 576  TYR B O     1 
ATOM   10053 C  CB    . TYR B 1 556 ? -11.997 -20.505 54.229  1.00 24.34 ? 576  TYR B CB    1 
ATOM   10054 C  CG    . TYR B 1 556 ? -12.958 -19.650 55.024  1.00 23.49 ? 576  TYR B CG    1 
ATOM   10055 C  CD1   . TYR B 1 556 ? -14.264 -20.071 55.245  1.00 23.28 ? 576  TYR B CD1   1 
ATOM   10056 C  CD2   . TYR B 1 556 ? -12.579 -18.405 55.512  1.00 22.86 ? 576  TYR B CD2   1 
ATOM   10057 C  CE1   . TYR B 1 556 ? -15.165 -19.278 55.952  1.00 23.89 ? 576  TYR B CE1   1 
ATOM   10058 C  CE2   . TYR B 1 556 ? -13.468 -17.608 56.216  1.00 22.99 ? 576  TYR B CE2   1 
ATOM   10059 C  CZ    . TYR B 1 556 ? -14.761 -18.048 56.430  1.00 23.75 ? 576  TYR B CZ    1 
ATOM   10060 O  OH    . TYR B 1 556 ? -15.649 -17.266 57.128  1.00 23.28 ? 576  TYR B OH    1 
ATOM   10061 N  N     . LEU B 1 557 ? -10.891 -20.016 50.923  1.00 23.39 ? 577  LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 557 ? -9.753  -20.151 50.034  1.00 23.26 ? 577  LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 557 ? -8.729  -19.070 50.406  1.00 23.40 ? 577  LEU B C     1 
ATOM   10064 O  O     . LEU B 1 557 ? -8.929  -17.895 50.122  1.00 23.35 ? 577  LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 557 ? -10.219 -20.015 48.590  1.00 22.79 ? 577  LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 557 ? -11.311 -20.999 48.143  1.00 22.45 ? 577  LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 557 ? -12.031 -20.481 46.896  1.00 20.95 ? 577  LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 557 ? -10.730 -22.384 47.892  1.00 21.03 ? 577  LEU B CD2   1 
ATOM   10069 N  N     . LEU B 1 558 ? -7.651  -19.471 51.074  1.00 23.78 ? 578  LEU B N     1 
ATOM   10070 C  CA    . LEU B 1 558 ? -6.746  -18.514 51.711  1.00 23.97 ? 578  LEU B CA    1 
ATOM   10071 C  C     . LEU B 1 558 ? -5.352  -18.513 51.089  1.00 24.36 ? 578  LEU B C     1 
ATOM   10072 O  O     . LEU B 1 558 ? -4.747  -19.565 50.867  1.00 24.23 ? 578  LEU B O     1 
ATOM   10073 C  CB    . LEU B 1 558 ? -6.611  -18.817 53.200  1.00 24.28 ? 578  LEU B CB    1 
ATOM   10074 C  CG    . LEU B 1 558 ? -7.845  -18.689 54.103  1.00 24.69 ? 578  LEU B CG    1 
ATOM   10075 C  CD1   . LEU B 1 558 ? -7.398  -18.946 55.537  1.00 24.43 ? 578  LEU B CD1   1 
ATOM   10076 C  CD2   . LEU B 1 558 ? -8.515  -17.335 53.986  1.00 23.51 ? 578  LEU B CD2   1 
ATOM   10077 N  N     . PHE B 1 559 ? -4.857  -17.310 50.821  1.00 24.84 ? 579  PHE B N     1 
ATOM   10078 C  CA    . PHE B 1 559 ? -3.472  -17.092 50.437  1.00 25.01 ? 579  PHE B CA    1 
ATOM   10079 C  C     . PHE B 1 559 ? -2.794  -16.405 51.617  1.00 25.78 ? 579  PHE B C     1 
ATOM   10080 O  O     . PHE B 1 559 ? -3.199  -15.324 52.036  1.00 25.54 ? 579  PHE B O     1 
ATOM   10081 C  CB    . PHE B 1 559 ? -3.419  -16.292 49.142  1.00 24.66 ? 579  PHE B CB    1 
ATOM   10082 C  CG    . PHE B 1 559 ? -4.084  -17.004 48.004  1.00 23.48 ? 579  PHE B CG    1 
ATOM   10083 C  CD1   . PHE B 1 559 ? -5.464  -16.986 47.875  1.00 21.80 ? 579  PHE B CD1   1 
ATOM   10084 C  CD2   . PHE B 1 559 ? -3.348  -17.766 47.120  1.00 22.46 ? 579  PHE B CD2   1 
ATOM   10085 C  CE1   . PHE B 1 559 ? -6.096  -17.678 46.845  1.00 21.87 ? 579  PHE B CE1   1 
ATOM   10086 C  CE2   . PHE B 1 559 ? -3.973  -18.461 46.080  1.00 21.99 ? 579  PHE B CE2   1 
ATOM   10087 C  CZ    . PHE B 1 559 ? -5.350  -18.419 45.951  1.00 21.06 ? 579  PHE B CZ    1 
ATOM   10088 N  N     . THR B 1 560 ? -1.787  -17.073 52.169  1.00 26.61 ? 580  THR B N     1 
ATOM   10089 C  CA    . THR B 1 560 ? -1.276  -16.751 53.493  1.00 27.72 ? 580  THR B CA    1 
ATOM   10090 C  C     . THR B 1 560 ? 0.183   -16.338 53.451  1.00 28.28 ? 580  THR B C     1 
ATOM   10091 O  O     . THR B 1 560 ? 0.957   -16.858 52.650  1.00 28.43 ? 580  THR B O     1 
ATOM   10092 C  CB    . THR B 1 560 ? -1.357  -17.971 54.405  1.00 27.73 ? 580  THR B CB    1 
ATOM   10093 O  OG1   . THR B 1 560 ? -0.415  -18.949 53.943  1.00 29.62 ? 580  THR B OG1   1 
ATOM   10094 C  CG2   . THR B 1 560 ? -2.760  -18.569 54.395  1.00 26.44 ? 580  THR B CG2   1 
ATOM   10095 N  N     . SER B 1 561 ? 0.540   -15.404 54.324  1.00 29.21 ? 581  SER B N     1 
ATOM   10096 C  CA    . SER B 1 561 ? 1.925   -15.055 54.586  1.00 29.99 ? 581  SER B CA    1 
ATOM   10097 C  C     . SER B 1 561 ? 2.381   -15.835 55.817  1.00 30.80 ? 581  SER B C     1 
ATOM   10098 O  O     . SER B 1 561 ? 1.558   -16.147 56.686  1.00 31.08 ? 581  SER B O     1 
ATOM   10099 C  CB    . SER B 1 561 ? 2.044   -13.549 54.852  1.00 30.48 ? 581  SER B CB    1 
ATOM   10100 O  OG    . SER B 1 561 ? 3.372   -13.163 55.174  1.00 30.21 ? 581  SER B OG    1 
ATOM   10101 N  N     . PRO B 1 562 ? 3.690   -16.150 55.908  1.00 31.55 ? 582  PRO B N     1 
ATOM   10102 C  CA    . PRO B 1 562 ? 4.239   -16.730 57.143  1.00 31.82 ? 582  PRO B CA    1 
ATOM   10103 C  C     . PRO B 1 562 ? 4.162   -15.787 58.341  1.00 31.97 ? 582  PRO B C     1 
ATOM   10104 O  O     . PRO B 1 562 ? 4.196   -16.245 59.479  1.00 32.21 ? 582  PRO B O     1 
ATOM   10105 C  CB    . PRO B 1 562 ? 5.713   -16.989 56.799  1.00 32.10 ? 582  PRO B CB    1 
ATOM   10106 C  CG    . PRO B 1 562 ? 5.818   -16.882 55.330  1.00 32.16 ? 582  PRO B CG    1 
ATOM   10107 C  CD    . PRO B 1 562 ? 4.723   -15.992 54.869  1.00 31.52 ? 582  PRO B CD    1 
ATOM   10108 N  N     . GLN B 1 563 ? 4.078   -14.484 58.087  1.00 32.21 ? 583  GLN B N     1 
ATOM   10109 C  CA    . GLN B 1 563 ? 3.894   -13.506 59.155  1.00 32.31 ? 583  GLN B CA    1 
ATOM   10110 C  C     . GLN B 1 563 ? 2.587   -13.771 59.897  1.00 32.18 ? 583  GLN B C     1 
ATOM   10111 O  O     . GLN B 1 563 ? 1.577   -14.158 59.286  1.00 31.61 ? 583  GLN B O     1 
ATOM   10112 C  CB    . GLN B 1 563 ? 3.829   -12.089 58.593  1.00 32.86 ? 583  GLN B CB    1 
ATOM   10113 C  CG    . GLN B 1 563 ? 5.058   -11.606 57.864  1.00 34.38 ? 583  GLN B CG    1 
ATOM   10114 C  CD    . GLN B 1 563 ? 4.827   -10.245 57.250  1.00 36.40 ? 583  GLN B CD    1 
ATOM   10115 O  OE1   . GLN B 1 563 ? 4.014   -9.463  57.745  1.00 38.86 ? 583  GLN B OE1   1 
ATOM   10116 N  NE2   . GLN B 1 563 ? 5.531   -9.953  56.163  1.00 37.96 ? 583  GLN B NE2   1 
ATOM   10117 N  N     . GLU B 1 564 ? 2.613   -13.550 61.209  1.00 31.77 ? 584  GLU B N     1 
ATOM   10118 C  CA    . GLU B 1 564 ? 1.438   -13.714 62.039  1.00 31.79 ? 584  GLU B CA    1 
ATOM   10119 C  C     . GLU B 1 564 ? 0.924   -12.358 62.497  1.00 31.05 ? 584  GLU B C     1 
ATOM   10120 O  O     . GLU B 1 564 ? 1.699   -11.429 62.680  1.00 31.16 ? 584  GLU B O     1 
ATOM   10121 C  CB    . GLU B 1 564 ? 1.773   -14.566 63.254  1.00 32.31 ? 584  GLU B CB    1 
ATOM   10122 C  CG    . GLU B 1 564 ? 2.345   -15.931 62.917  1.00 33.44 ? 584  GLU B CG    1 
ATOM   10123 C  CD    . GLU B 1 564 ? 2.376   -16.857 64.117  1.00 35.51 ? 584  GLU B CD    1 
ATOM   10124 O  OE1   . GLU B 1 564 ? 2.427   -16.344 65.256  1.00 36.94 ? 584  GLU B OE1   1 
ATOM   10125 O  OE2   . GLU B 1 564 ? 2.340   -18.097 63.923  1.00 37.63 ? 584  GLU B OE2   1 
ATOM   10126 N  N     . ASN B 1 565 ? -0.389  -12.247 62.680  1.00 30.14 ? 585  ASN B N     1 
ATOM   10127 C  CA    . ASN B 1 565 ? -0.970  -11.058 63.295  1.00 29.21 ? 585  ASN B CA    1 
ATOM   10128 C  C     . ASN B 1 565 ? -0.708  -11.094 64.816  1.00 28.78 ? 585  ASN B C     1 
ATOM   10129 O  O     . ASN B 1 565 ? -0.167  -12.076 65.318  1.00 28.08 ? 585  ASN B O     1 
ATOM   10130 C  CB    . ASN B 1 565 ? -2.465  -10.926 62.927  1.00 28.89 ? 585  ASN B CB    1 
ATOM   10131 C  CG    . ASN B 1 565 ? -3.377  -11.892 63.685  1.00 28.36 ? 585  ASN B CG    1 
ATOM   10132 O  OD1   . ASN B 1 565 ? -2.936  -12.645 64.552  1.00 25.81 ? 585  ASN B OD1   1 
ATOM   10133 N  ND2   . ASN B 1 565 ? -4.677  -11.862 63.351  1.00 26.43 ? 585  ASN B ND2   1 
ATOM   10134 N  N     . PRO B 1 566 ? -1.086  -10.034 65.552  1.00 28.51 ? 586  PRO B N     1 
ATOM   10135 C  CA    . PRO B 1 566 ? -0.815  -10.020 67.000  1.00 28.70 ? 586  PRO B CA    1 
ATOM   10136 C  C     . PRO B 1 566 ? -1.434  -11.146 67.826  1.00 28.50 ? 586  PRO B C     1 
ATOM   10137 O  O     . PRO B 1 566 ? -1.040  -11.321 68.965  1.00 28.59 ? 586  PRO B O     1 
ATOM   10138 C  CB    . PRO B 1 566 ? -1.391  -8.674  67.450  1.00 28.55 ? 586  PRO B CB    1 
ATOM   10139 C  CG    . PRO B 1 566 ? -1.250  -7.812  66.249  1.00 28.70 ? 586  PRO B CG    1 
ATOM   10140 C  CD    . PRO B 1 566 ? -1.593  -8.731  65.097  1.00 28.55 ? 586  PRO B CD    1 
ATOM   10141 N  N     . TRP B 1 567 ? -2.366  -11.904 67.252  1.00 28.54 ? 587  TRP B N     1 
ATOM   10142 C  CA    . TRP B 1 567 ? -3.104  -12.946 67.972  1.00 28.44 ? 587  TRP B CA    1 
ATOM   10143 C  C     . TRP B 1 567 ? -2.646  -14.345 67.579  1.00 28.15 ? 587  TRP B C     1 
ATOM   10144 O  O     . TRP B 1 567 ? -3.267  -15.342 67.967  1.00 28.39 ? 587  TRP B O     1 
ATOM   10145 C  CB    . TRP B 1 567 ? -4.614  -12.764 67.724  1.00 28.84 ? 587  TRP B CB    1 
ATOM   10146 C  CG    . TRP B 1 567 ? -4.973  -11.312 67.801  1.00 29.66 ? 587  TRP B CG    1 
ATOM   10147 C  CD1   . TRP B 1 567 ? -5.444  -10.521 66.791  1.00 30.67 ? 587  TRP B CD1   1 
ATOM   10148 C  CD2   . TRP B 1 567 ? -4.792  -10.456 68.929  1.00 30.42 ? 587  TRP B CD2   1 
ATOM   10149 N  NE1   . TRP B 1 567 ? -5.600  -9.231  67.235  1.00 30.09 ? 587  TRP B NE1   1 
ATOM   10150 C  CE2   . TRP B 1 567 ? -5.208  -9.166  68.546  1.00 31.07 ? 587  TRP B CE2   1 
ATOM   10151 C  CE3   . TRP B 1 567 ? -4.334  -10.659 70.236  1.00 31.56 ? 587  TRP B CE3   1 
ATOM   10152 C  CZ2   . TRP B 1 567 ? -5.178  -8.078  69.426  1.00 32.44 ? 587  TRP B CZ2   1 
ATOM   10153 C  CZ3   . TRP B 1 567 ? -4.310  -9.581  71.110  1.00 31.20 ? 587  TRP B CZ3   1 
ATOM   10154 C  CH2   . TRP B 1 567 ? -4.724  -8.308  70.701  1.00 32.77 ? 587  TRP B CH2   1 
ATOM   10155 N  N     . GLY B 1 568 ? -1.562  -14.417 66.807  1.00 27.57 ? 588  GLY B N     1 
ATOM   10156 C  CA    . GLY B 1 568 ? -0.935  -15.689 66.468  1.00 27.59 ? 588  GLY B CA    1 
ATOM   10157 C  C     . GLY B 1 568 ? -1.454  -16.370 65.213  1.00 27.58 ? 588  GLY B C     1 
ATOM   10158 O  O     . GLY B 1 568 ? -1.110  -17.521 64.955  1.00 28.57 ? 588  GLY B O     1 
ATOM   10159 N  N     . HIS B 1 569 ? -2.289  -15.693 64.434  1.00 26.79 ? 589  HIS B N     1 
ATOM   10160 C  CA    . HIS B 1 569 ? -2.846  -16.301 63.227  1.00 26.52 ? 589  HIS B CA    1 
ATOM   10161 C  C     . HIS B 1 569 ? -2.128  -15.762 62.007  1.00 26.37 ? 589  HIS B C     1 
ATOM   10162 O  O     . HIS B 1 569 ? -1.764  -14.591 61.971  1.00 26.70 ? 589  HIS B O     1 
ATOM   10163 C  CB    . HIS B 1 569 ? -4.350  -16.028 63.133  1.00 26.03 ? 589  HIS B CB    1 
ATOM   10164 C  CG    . HIS B 1 569 ? -5.144  -16.758 64.165  1.00 25.66 ? 589  HIS B CG    1 
ATOM   10165 N  ND1   . HIS B 1 569 ? -5.520  -18.075 64.017  1.00 25.47 ? 589  HIS B ND1   1 
ATOM   10166 C  CD2   . HIS B 1 569 ? -5.601  -16.368 65.377  1.00 24.97 ? 589  HIS B CD2   1 
ATOM   10167 C  CE1   . HIS B 1 569 ? -6.181  -18.464 65.093  1.00 26.38 ? 589  HIS B CE1   1 
ATOM   10168 N  NE2   . HIS B 1 569 ? -6.245  -17.447 65.933  1.00 24.73 ? 589  HIS B NE2   1 
ATOM   10169 N  N     . LYS B 1 570 ? -1.929  -16.611 61.005  1.00 26.34 ? 590  LYS B N     1 
ATOM   10170 C  CA    . LYS B 1 570 ? -1.222  -16.195 59.794  1.00 26.28 ? 590  LYS B CA    1 
ATOM   10171 C  C     . LYS B 1 570 ? -1.977  -15.106 59.036  1.00 26.04 ? 590  LYS B C     1 
ATOM   10172 O  O     . LYS B 1 570 ? -3.200  -15.172 58.884  1.00 25.84 ? 590  LYS B O     1 
ATOM   10173 C  CB    . LYS B 1 570 ? -0.970  -17.393 58.883  1.00 26.64 ? 590  LYS B CB    1 
ATOM   10174 C  CG    . LYS B 1 570 ? 0.260   -18.222 59.270  1.00 27.14 ? 590  LYS B CG    1 
ATOM   10175 C  CD    . LYS B 1 570 ? 0.562   -19.260 58.187  1.00 27.90 ? 590  LYS B CD    1 
ATOM   10176 N  N     . ARG B 1 571 ? -1.240  -14.098 58.573  1.00 25.76 ? 591  ARG B N     1 
ATOM   10177 C  CA    . ARG B 1 571 ? -1.829  -13.004 57.809  1.00 25.80 ? 591  ARG B CA    1 
ATOM   10178 C  C     . ARG B 1 571 ? -2.204  -13.509 56.419  1.00 25.52 ? 591  ARG B C     1 
ATOM   10179 O  O     . ARG B 1 571 ? -1.356  -14.059 55.704  1.00 25.59 ? 591  ARG B O     1 
ATOM   10180 C  CB    . ARG B 1 571 ? -0.873  -11.825 57.727  1.00 25.99 ? 591  ARG B CB    1 
ATOM   10181 C  CG    . ARG B 1 571 ? -0.410  -11.340 59.100  1.00 27.34 ? 591  ARG B CG    1 
ATOM   10182 C  CD    . ARG B 1 571 ? 0.517   -10.181 58.964  1.00 27.91 ? 591  ARG B CD    1 
ATOM   10183 N  NE    . ARG B 1 571 ? -0.213  -8.976  58.569  1.00 29.45 ? 591  ARG B NE    1 
ATOM   10184 C  CZ    . ARG B 1 571 ? 0.329   -7.942  57.939  1.00 30.61 ? 591  ARG B CZ    1 
ATOM   10185 N  NH1   . ARG B 1 571 ? 1.622   -7.951  57.605  1.00 31.34 ? 591  ARG B NH1   1 
ATOM   10186 N  NH2   . ARG B 1 571 ? -0.429  -6.897  57.631  1.00 31.67 ? 591  ARG B NH2   1 
ATOM   10187 N  N     . SER B 1 572 ? -3.478  -13.357 56.050  1.00 24.91 ? 592  SER B N     1 
ATOM   10188 C  CA    A SER B 1 572 ? -4.006  -13.930 54.807  0.60 24.49 ? 592  SER B CA    1 
ATOM   10189 C  CA    B SER B 1 572 ? -3.933  -13.874 54.763  0.40 24.74 ? 592  SER B CA    1 
ATOM   10190 C  C     . SER B 1 572 ? -5.004  -13.017 54.104  1.00 24.30 ? 592  SER B C     1 
ATOM   10191 O  O     . SER B 1 572 ? -5.554  -12.096 54.718  1.00 24.13 ? 592  SER B O     1 
ATOM   10192 C  CB    A SER B 1 572 ? -4.716  -15.256 55.099  0.60 24.42 ? 592  SER B CB    1 
ATOM   10193 C  CB    B SER B 1 572 ? -4.443  -15.302 54.933  0.40 24.76 ? 592  SER B CB    1 
ATOM   10194 O  OG    A SER B 1 572 ? -3.957  -16.105 55.941  0.60 23.52 ? 592  SER B OG    1 
ATOM   10195 O  OG    B SER B 1 572 ? -5.591  -15.328 55.750  0.40 25.29 ? 592  SER B OG    1 
ATOM   10196 N  N     . TYR B 1 573 ? -5.247  -13.311 52.825  1.00 23.82 ? 593  TYR B N     1 
ATOM   10197 C  CA    . TYR B 1 573 ? -6.391  -12.786 52.089  1.00 23.17 ? 593  TYR B CA    1 
ATOM   10198 C  C     . TYR B 1 573 ? -7.213  -13.971 51.593  1.00 23.25 ? 593  TYR B C     1 
ATOM   10199 O  O     . TYR B 1 573 ? -6.676  -15.006 51.178  1.00 23.63 ? 593  TYR B O     1 
ATOM   10200 C  CB    . TYR B 1 573 ? -5.972  -11.855 50.934  1.00 23.37 ? 593  TYR B CB    1 
ATOM   10201 C  CG    . TYR B 1 573 ? -6.216  -10.398 51.247  1.00 21.61 ? 593  TYR B CG    1 
ATOM   10202 C  CD1   . TYR B 1 573 ? -5.378  -9.710  52.120  1.00 21.05 ? 593  TYR B CD1   1 
ATOM   10203 C  CD2   . TYR B 1 573 ? -7.314  -9.718  50.707  1.00 20.96 ? 593  TYR B CD2   1 
ATOM   10204 C  CE1   . TYR B 1 573 ? -5.600  -8.378  52.431  1.00 20.97 ? 593  TYR B CE1   1 
ATOM   10205 C  CE2   . TYR B 1 573 ? -7.553  -8.385  51.005  1.00 20.13 ? 593  TYR B CE2   1 
ATOM   10206 C  CZ    . TYR B 1 573 ? -6.692  -7.713  51.880  1.00 21.87 ? 593  TYR B CZ    1 
ATOM   10207 O  OH    . TYR B 1 573 ? -6.912  -6.394  52.215  1.00 19.79 ? 593  TYR B OH    1 
ATOM   10208 N  N     . ARG B 1 574 ? -8.525  -13.818 51.658  1.00 23.07 ? 594  ARG B N     1 
ATOM   10209 C  CA    . ARG B 1 574 ? -9.461  -14.857 51.273  1.00 22.84 ? 594  ARG B CA    1 
ATOM   10210 C  C     . ARG B 1 574 ? -10.040 -14.539 49.891  1.00 22.53 ? 594  ARG B C     1 
ATOM   10211 O  O     . ARG B 1 574 ? -10.409 -13.395 49.621  1.00 22.08 ? 594  ARG B O     1 
ATOM   10212 C  CB    . ARG B 1 574 ? -10.583 -14.905 52.314  1.00 22.96 ? 594  ARG B CB    1 
ATOM   10213 C  CG    . ARG B 1 574 ? -11.646 -15.925 52.060  1.00 23.73 ? 594  ARG B CG    1 
ATOM   10214 C  CD    . ARG B 1 574 ? -12.884 -15.620 52.881  1.00 23.45 ? 594  ARG B CD    1 
ATOM   10215 N  NE    . ARG B 1 574 ? -13.930 -16.597 52.614  1.00 23.45 ? 594  ARG B NE    1 
ATOM   10216 C  CZ    . ARG B 1 574 ? -15.116 -16.605 53.214  1.00 24.56 ? 594  ARG B CZ    1 
ATOM   10217 N  NH1   . ARG B 1 574 ? -15.415 -15.681 54.114  1.00 24.74 ? 594  ARG B NH1   1 
ATOM   10218 N  NH2   . ARG B 1 574 ? -16.013 -17.534 52.905  1.00 24.94 ? 594  ARG B NH2   1 
ATOM   10219 N  N     . LEU B 1 575 ? -10.116 -15.550 49.026  1.00 22.40 ? 595  LEU B N     1 
ATOM   10220 C  CA    . LEU B 1 575 ? -10.765 -15.415 47.723  1.00 22.56 ? 595  LEU B CA    1 
ATOM   10221 C  C     . LEU B 1 575 ? -12.166 -16.015 47.805  1.00 22.61 ? 595  LEU B C     1 
ATOM   10222 O  O     . LEU B 1 575 ? -12.327 -17.157 48.198  1.00 22.92 ? 595  LEU B O     1 
ATOM   10223 C  CB    . LEU B 1 575 ? -9.949  -16.107 46.627  1.00 22.48 ? 595  LEU B CB    1 
ATOM   10224 C  CG    . LEU B 1 575 ? -10.616 -16.294 45.259  1.00 22.41 ? 595  LEU B CG    1 
ATOM   10225 C  CD1   . LEU B 1 575 ? -10.858 -14.963 44.559  1.00 22.68 ? 595  LEU B CD1   1 
ATOM   10226 C  CD2   . LEU B 1 575 ? -9.758  -17.221 44.391  1.00 23.39 ? 595  LEU B CD2   1 
ATOM   10227 N  N     . GLN B 1 576 ? -13.166 -15.223 47.435  1.00 23.28 ? 596  GLN B N     1 
ATOM   10228 C  CA    . GLN B 1 576 ? -14.577 -15.622 47.477  1.00 23.72 ? 596  GLN B CA    1 
ATOM   10229 C  C     . GLN B 1 576 ? -15.191 -15.395 46.100  1.00 23.35 ? 596  GLN B C     1 
ATOM   10230 O  O     . GLN B 1 576 ? -15.313 -14.255 45.648  1.00 23.30 ? 596  GLN B O     1 
ATOM   10231 C  CB    . GLN B 1 576 ? -15.287 -14.780 48.534  1.00 24.38 ? 596  GLN B CB    1 
ATOM   10232 C  CG    . GLN B 1 576 ? -16.758 -15.039 48.748  1.00 26.29 ? 596  GLN B CG    1 
ATOM   10233 C  CD    . GLN B 1 576 ? -17.293 -14.233 49.930  1.00 29.00 ? 596  GLN B CD    1 
ATOM   10234 O  OE1   . GLN B 1 576 ? -16.611 -14.077 50.944  1.00 30.14 ? 596  GLN B OE1   1 
ATOM   10235 N  NE2   . GLN B 1 576 ? -18.508 -13.708 49.796  1.00 29.79 ? 596  GLN B NE2   1 
ATOM   10236 N  N     . ILE B 1 577 ? -15.579 -16.484 45.445  1.00 22.95 ? 597  ILE B N     1 
ATOM   10237 C  CA    . ILE B 1 577 ? -15.992 -16.462 44.049  1.00 22.67 ? 597  ILE B CA    1 
ATOM   10238 C  C     . ILE B 1 577 ? -17.513 -16.385 43.920  1.00 23.00 ? 597  ILE B C     1 
ATOM   10239 O  O     . ILE B 1 577 ? -18.242 -17.150 44.567  1.00 22.84 ? 597  ILE B O     1 
ATOM   10240 C  CB    . ILE B 1 577 ? -15.486 -17.729 43.314  1.00 22.50 ? 597  ILE B CB    1 
ATOM   10241 C  CG1   . ILE B 1 577 ? -13.951 -17.774 43.317  1.00 22.17 ? 597  ILE B CG1   1 
ATOM   10242 C  CG2   . ILE B 1 577 ? -16.019 -17.782 41.894  1.00 22.35 ? 597  ILE B CG2   1 
ATOM   10243 C  CD1   . ILE B 1 577 ? -13.350 -19.170 43.026  1.00 20.11 ? 597  ILE B CD1   1 
ATOM   10244 N  N     A HIS B 1 578 ? -17.984 -15.473 43.077  0.50 22.98 ? 598  HIS B N     1 
ATOM   10245 N  N     B HIS B 1 578 ? -17.983 -15.447 43.097  0.50 23.05 ? 598  HIS B N     1 
ATOM   10246 C  CA    A HIS B 1 578 ? -19.409 -15.339 42.805  0.50 23.10 ? 598  HIS B CA    1 
ATOM   10247 C  CA    B HIS B 1 578 ? -19.406 -15.317 42.780  0.50 23.21 ? 598  HIS B CA    1 
ATOM   10248 C  C     A HIS B 1 578 ? -19.654 -15.716 41.346  0.50 22.98 ? 598  HIS B C     1 
ATOM   10249 C  C     B HIS B 1 578 ? -19.615 -15.736 41.332  0.50 23.03 ? 598  HIS B C     1 
ATOM   10250 O  O     A HIS B 1 578 ? -19.364 -14.936 40.432  0.50 22.69 ? 598  HIS B O     1 
ATOM   10251 O  O     B HIS B 1 578 ? -19.271 -14.993 40.406  0.50 22.72 ? 598  HIS B O     1 
ATOM   10252 C  CB    A HIS B 1 578 ? -19.883 -13.922 43.133  0.50 23.20 ? 598  HIS B CB    1 
ATOM   10253 C  CB    B HIS B 1 578 ? -19.894 -13.883 42.980  0.50 23.34 ? 598  HIS B CB    1 
ATOM   10254 C  CG    A HIS B 1 578 ? -19.774 -13.581 44.589  0.50 23.73 ? 598  HIS B CG    1 
ATOM   10255 C  CG    B HIS B 1 578 ? -21.358 -13.707 42.718  0.50 24.26 ? 598  HIS B CG    1 
ATOM   10256 N  ND1   A HIS B 1 578 ? -19.455 -12.320 45.043  0.50 24.60 ? 598  HIS B ND1   1 
ATOM   10257 N  ND1   B HIS B 1 578 ? -21.843 -12.942 41.679  0.50 25.60 ? 598  HIS B ND1   1 
ATOM   10258 C  CD2   A HIS B 1 578 ? -19.922 -14.350 45.695  0.50 24.71 ? 598  HIS B CD2   1 
ATOM   10259 C  CD2   B HIS B 1 578 ? -22.444 -14.216 43.348  0.50 25.13 ? 598  HIS B CD2   1 
ATOM   10260 C  CE1   A HIS B 1 578 ? -19.426 -12.324 46.364  0.50 24.69 ? 598  HIS B CE1   1 
ATOM   10261 C  CE1   B HIS B 1 578 ? -23.164 -12.979 41.686  0.50 25.30 ? 598  HIS B CE1   1 
ATOM   10262 N  NE2   A HIS B 1 578 ? -19.701 -13.544 46.785  0.50 24.77 ? 598  HIS B NE2   1 
ATOM   10263 N  NE2   B HIS B 1 578 ? -23.554 -13.744 42.689  0.50 24.91 ? 598  HIS B NE2   1 
ATOM   10264 N  N     . SER B 1 579 ? -20.166 -16.930 41.141  1.00 22.75 ? 599  SER B N     1 
ATOM   10265 C  CA    . SER B 1 579 ? -20.248 -17.529 39.807  1.00 22.98 ? 599  SER B CA    1 
ATOM   10266 C  C     . SER B 1 579 ? -21.335 -18.594 39.692  1.00 23.35 ? 599  SER B C     1 
ATOM   10267 O  O     . SER B 1 579 ? -21.710 -19.209 40.676  1.00 22.72 ? 599  SER B O     1 
ATOM   10268 C  CB    . SER B 1 579 ? -18.895 -18.169 39.477  1.00 22.41 ? 599  SER B CB    1 
ATOM   10269 O  OG    . SER B 1 579 ? -18.915 -18.800 38.212  1.00 21.16 ? 599  SER B OG    1 
ATOM   10270 N  N     . MET B 1 580 ? -21.836 -18.791 38.480  1.00 24.31 ? 600  MET B N     1 
ATOM   10271 C  CA    A MET B 1 580 ? -22.739 -19.910 38.208  0.70 25.17 ? 600  MET B CA    1 
ATOM   10272 C  CA    B MET B 1 580 ? -22.753 -19.885 38.165  0.30 24.84 ? 600  MET B CA    1 
ATOM   10273 C  C     . MET B 1 580 ? -22.128 -20.850 37.163  1.00 25.08 ? 600  MET B C     1 
ATOM   10274 O  O     . MET B 1 580 ? -22.809 -21.712 36.630  1.00 26.03 ? 600  MET B O     1 
ATOM   10275 C  CB    A MET B 1 580 ? -24.113 -19.400 37.761  0.70 25.53 ? 600  MET B CB    1 
ATOM   10276 C  CB    B MET B 1 580 ? -24.066 -19.336 37.597  0.30 24.91 ? 600  MET B CB    1 
ATOM   10277 C  CG    A MET B 1 580 ? -24.836 -18.559 38.810  0.70 27.16 ? 600  MET B CG    1 
ATOM   10278 C  CG    B MET B 1 580 ? -25.237 -19.496 38.526  0.30 25.36 ? 600  MET B CG    1 
ATOM   10279 S  SD    A MET B 1 580 ? -26.570 -18.213 38.370  0.70 31.65 ? 600  MET B SD    1 
ATOM   10280 S  SD    B MET B 1 580 ? -25.051 -18.511 40.014  0.30 25.72 ? 600  MET B SD    1 
ATOM   10281 C  CE    A MET B 1 580 ? -26.366 -17.057 37.011  0.70 30.41 ? 600  MET B CE    1 
ATOM   10282 C  CE    B MET B 1 580 ? -26.579 -18.908 40.874  0.30 25.26 ? 600  MET B CE    1 
ATOM   10283 N  N     . ALA B 1 581 ? -20.825 -20.711 36.910  1.00 25.35 ? 601  ALA B N     1 
ATOM   10284 C  CA    . ALA B 1 581 ? -20.154 -21.500 35.869  1.00 25.17 ? 601  ALA B CA    1 
ATOM   10285 C  C     . ALA B 1 581 ? -20.088 -22.993 36.148  1.00 25.41 ? 601  ALA B C     1 
ATOM   10286 O  O     . ALA B 1 581 ? -20.266 -23.464 37.275  1.00 25.04 ? 601  ALA B O     1 
ATOM   10287 C  CB    . ALA B 1 581 ? -18.754 -20.963 35.592  1.00 24.91 ? 601  ALA B CB    1 
ATOM   10288 N  N     . ASP B 1 582 ? -19.830 -23.727 35.076  1.00 25.95 ? 602  ASP B N     1 
ATOM   10289 C  CA    . ASP B 1 582 ? -19.705 -25.176 35.107  1.00 26.34 ? 602  ASP B CA    1 
ATOM   10290 C  C     . ASP B 1 582 ? -18.830 -25.580 33.933  1.00 25.90 ? 602  ASP B C     1 
ATOM   10291 O  O     . ASP B 1 582 ? -18.468 -24.731 33.112  1.00 25.47 ? 602  ASP B O     1 
ATOM   10292 C  CB    . ASP B 1 582 ? -21.094 -25.797 34.950  1.00 26.69 ? 602  ASP B CB    1 
ATOM   10293 C  CG    . ASP B 1 582 ? -21.189 -27.175 35.544  1.00 28.59 ? 602  ASP B CG    1 
ATOM   10294 O  OD1   . ASP B 1 582 ? -20.135 -27.796 35.852  1.00 31.36 ? 602  ASP B OD1   1 
ATOM   10295 O  OD2   . ASP B 1 582 ? -22.334 -27.642 35.691  1.00 31.48 ? 602  ASP B OD2   1 
ATOM   10296 N  N     . GLN B 1 583 ? -18.497 -26.865 33.843  1.00 26.09 ? 603  GLN B N     1 
ATOM   10297 C  CA    . GLN B 1 583 ? -17.833 -27.391 32.654  1.00 26.18 ? 603  GLN B CA    1 
ATOM   10298 C  C     . GLN B 1 583 ? -18.763 -27.273 31.456  1.00 26.22 ? 603  GLN B C     1 
ATOM   10299 O  O     . GLN B 1 583 ? -19.912 -27.732 31.506  1.00 26.20 ? 603  GLN B O     1 
ATOM   10300 C  CB    . GLN B 1 583 ? -17.427 -28.858 32.842  1.00 26.38 ? 603  GLN B CB    1 
ATOM   10301 C  CG    . GLN B 1 583 ? -16.453 -29.345 31.770  1.00 26.25 ? 603  GLN B CG    1 
ATOM   10302 C  CD    . GLN B 1 583 ? -15.194 -28.489 31.731  1.00 25.74 ? 603  GLN B CD    1 
ATOM   10303 O  OE1   . GLN B 1 583 ? -14.561 -28.279 32.755  1.00 26.05 ? 603  GLN B OE1   1 
ATOM   10304 N  NE2   . GLN B 1 583 ? -14.839 -27.987 30.552  1.00 25.70 ? 603  GLN B NE2   1 
ATOM   10305 N  N     . VAL B 1 584 ? -18.282 -26.645 30.386  1.00 26.38 ? 604  VAL B N     1 
ATOM   10306 C  CA    . VAL B 1 584 ? -19.104 -26.440 29.202  1.00 26.60 ? 604  VAL B CA    1 
ATOM   10307 C  C     . VAL B 1 584 ? -18.719 -27.441 28.122  1.00 26.92 ? 604  VAL B C     1 
ATOM   10308 O  O     . VAL B 1 584 ? -19.517 -28.311 27.775  1.00 27.10 ? 604  VAL B O     1 
ATOM   10309 C  CB    . VAL B 1 584 ? -19.011 -24.996 28.673  1.00 26.76 ? 604  VAL B CB    1 
ATOM   10310 C  CG1   . VAL B 1 584 ? -19.891 -24.826 27.435  1.00 26.49 ? 604  VAL B CG1   1 
ATOM   10311 C  CG2   . VAL B 1 584 ? -19.421 -24.007 29.763  1.00 26.86 ? 604  VAL B CG2   1 
ATOM   10312 N  N     . LEU B 1 585 ? -17.499 -27.323 27.604  1.00 27.02 ? 605  LEU B N     1 
ATOM   10313 C  CA    . LEU B 1 585 ? -17.022 -28.242 26.576  1.00 27.25 ? 605  LEU B CA    1 
ATOM   10314 C  C     . LEU B 1 585 ? -16.372 -29.466 27.221  1.00 26.96 ? 605  LEU B C     1 
ATOM   10315 O  O     . LEU B 1 585 ? -15.899 -29.382 28.351  1.00 27.35 ? 605  LEU B O     1 
ATOM   10316 C  CB    . LEU B 1 585 ? -16.046 -27.539 25.625  1.00 27.19 ? 605  LEU B CB    1 
ATOM   10317 C  CG    . LEU B 1 585 ? -16.629 -26.305 24.925  1.00 27.89 ? 605  LEU B CG    1 
ATOM   10318 C  CD1   . LEU B 1 585 ? -15.579 -25.609 24.044  1.00 29.31 ? 605  LEU B CD1   1 
ATOM   10319 C  CD2   . LEU B 1 585 ? -17.877 -26.656 24.110  1.00 28.20 ? 605  LEU B CD2   1 
ATOM   10320 N  N     . PRO B 1 586 ? -16.374 -30.616 26.518  1.00 26.60 ? 606  PRO B N     1 
ATOM   10321 C  CA    . PRO B 1 586 ? -15.678 -31.795 27.043  1.00 26.05 ? 606  PRO B CA    1 
ATOM   10322 C  C     . PRO B 1 586 ? -14.167 -31.594 27.073  1.00 25.91 ? 606  PRO B C     1 
ATOM   10323 O  O     . PRO B 1 586 ? -13.576 -31.228 26.060  1.00 25.13 ? 606  PRO B O     1 
ATOM   10324 C  CB    . PRO B 1 586 ? -16.032 -32.907 26.048  1.00 25.99 ? 606  PRO B CB    1 
ATOM   10325 C  CG    . PRO B 1 586 ? -17.146 -32.368 25.207  1.00 26.65 ? 606  PRO B CG    1 
ATOM   10326 C  CD    . PRO B 1 586 ? -17.019 -30.885 25.222  1.00 26.63 ? 606  PRO B CD    1 
ATOM   10327 N  N     . PRO B 1 587 ? -13.538 -31.833 28.229  1.00 25.87 ? 607  PRO B N     1 
ATOM   10328 C  CA    . PRO B 1 587 ? -12.088 -31.758 28.264  1.00 26.14 ? 607  PRO B CA    1 
ATOM   10329 C  C     . PRO B 1 587 ? -11.441 -32.613 27.183  1.00 26.29 ? 607  PRO B C     1 
ATOM   10330 O  O     . PRO B 1 587 ? -11.786 -33.778 27.049  1.00 26.72 ? 607  PRO B O     1 
ATOM   10331 C  CB    . PRO B 1 587 ? -11.756 -32.289 29.656  1.00 25.96 ? 607  PRO B CB    1 
ATOM   10332 C  CG    . PRO B 1 587 ? -12.897 -31.815 30.479  1.00 26.02 ? 607  PRO B CG    1 
ATOM   10333 C  CD    . PRO B 1 587 ? -14.100 -32.048 29.574  1.00 26.01 ? 607  PRO B CD    1 
ATOM   10334 N  N     . GLY B 1 588 ? -10.539 -32.021 26.404  1.00 26.56 ? 608  GLY B N     1 
ATOM   10335 C  CA    . GLY B 1 588 ? -9.768  -32.761 25.414  1.00 26.61 ? 608  GLY B CA    1 
ATOM   10336 C  C     . GLY B 1 588 ? -10.377 -32.737 24.033  1.00 26.97 ? 608  GLY B C     1 
ATOM   10337 O  O     . GLY B 1 588 ? -9.750  -33.199 23.087  1.00 27.25 ? 608  GLY B O     1 
ATOM   10338 N  N     . TRP B 1 589 ? -11.579 -32.176 23.889  1.00 27.05 ? 609  TRP B N     1 
ATOM   10339 C  CA    . TRP B 1 589 ? -12.265 -32.207 22.599  1.00 27.23 ? 609  TRP B CA    1 
ATOM   10340 C  C     . TRP B 1 589 ? -12.075 -30.937 21.763  1.00 27.00 ? 609  TRP B C     1 
ATOM   10341 O  O     . TRP B 1 589 ? -12.655 -29.899 22.057  1.00 27.02 ? 609  TRP B O     1 
ATOM   10342 C  CB    . TRP B 1 589 ? -13.759 -32.491 22.773  1.00 27.36 ? 609  TRP B CB    1 
ATOM   10343 C  CG    . TRP B 1 589 ? -14.455 -32.499 21.446  1.00 28.64 ? 609  TRP B CG    1 
ATOM   10344 C  CD1   . TRP B 1 589 ? -15.245 -31.519 20.927  1.00 28.97 ? 609  TRP B CD1   1 
ATOM   10345 C  CD2   . TRP B 1 589 ? -14.364 -33.516 20.445  1.00 29.85 ? 609  TRP B CD2   1 
ATOM   10346 N  NE1   . TRP B 1 589 ? -15.685 -31.879 19.673  1.00 29.69 ? 609  TRP B NE1   1 
ATOM   10347 C  CE2   . TRP B 1 589 ? -15.156 -33.099 19.353  1.00 30.10 ? 609  TRP B CE2   1 
ATOM   10348 C  CE3   . TRP B 1 589 ? -13.709 -34.752 20.375  1.00 30.18 ? 609  TRP B CE3   1 
ATOM   10349 C  CZ2   . TRP B 1 589 ? -15.299 -33.866 18.198  1.00 30.87 ? 609  TRP B CZ2   1 
ATOM   10350 C  CZ3   . TRP B 1 589 ? -13.853 -35.517 19.229  1.00 30.34 ? 609  TRP B CZ3   1 
ATOM   10351 C  CH2   . TRP B 1 589 ? -14.647 -35.074 18.157  1.00 30.87 ? 609  TRP B CH2   1 
ATOM   10352 N  N     . GLN B 1 590 ? -11.258 -31.048 20.716  1.00 27.09 ? 610  GLN B N     1 
ATOM   10353 C  CA    . GLN B 1 590 ? -11.102 -30.030 19.676  1.00 26.99 ? 610  GLN B CA    1 
ATOM   10354 C  C     . GLN B 1 590 ? -10.891 -28.604 20.224  1.00 26.67 ? 610  GLN B C     1 
ATOM   10355 O  O     . GLN B 1 590 ? -9.834  -28.318 20.803  1.00 26.23 ? 610  GLN B O     1 
ATOM   10356 C  CB    . GLN B 1 590 ? -12.284 -30.102 18.686  1.00 27.29 ? 610  GLN B CB    1 
ATOM   10357 C  CG    . GLN B 1 590 ? -12.441 -31.438 17.935  1.00 28.91 ? 610  GLN B CG    1 
ATOM   10358 C  CD    . GLN B 1 590 ? -11.275 -31.770 16.993  1.00 30.89 ? 610  GLN B CD    1 
ATOM   10359 O  OE1   . GLN B 1 590 ? -10.514 -30.899 16.579  1.00 31.19 ? 610  GLN B OE1   1 
ATOM   10360 N  NE2   . GLN B 1 590 ? -11.152 -33.039 16.646  1.00 32.79 ? 610  GLN B NE2   1 
ATOM   10361 N  N     . GLU B 1 591 ? -11.893 -27.726 20.059  1.00 26.24 ? 611  GLU B N     1 
ATOM   10362 C  CA    . GLU B 1 591 ? -11.768 -26.290 20.398  1.00 26.18 ? 611  GLU B CA    1 
ATOM   10363 C  C     . GLU B 1 591 ? -11.596 -26.028 21.895  1.00 25.28 ? 611  GLU B C     1 
ATOM   10364 O  O     . GLU B 1 591 ? -11.139 -24.966 22.275  1.00 24.91 ? 611  GLU B O     1 
ATOM   10365 C  CB    . GLU B 1 591 ? -12.981 -25.478 19.908  1.00 26.33 ? 611  GLU B CB    1 
ATOM   10366 C  CG    . GLU B 1 591 ? -13.259 -25.561 18.406  1.00 28.04 ? 611  GLU B CG    1 
ATOM   10367 C  CD    . GLU B 1 591 ? -14.033 -26.800 18.025  1.00 30.72 ? 611  GLU B CD    1 
ATOM   10368 O  OE1   . GLU B 1 591 ? -14.718 -27.371 18.898  1.00 33.68 ? 611  GLU B OE1   1 
ATOM   10369 O  OE2   . GLU B 1 591 ? -13.948 -27.220 16.857  1.00 35.35 ? 611  GLU B OE2   1 
ATOM   10370 N  N     . GLU B 1 592 ? -11.973 -26.990 22.733  1.00 24.89 ? 612  GLU B N     1 
ATOM   10371 C  CA    . GLU B 1 592 ? -11.808 -26.870 24.184  1.00 24.74 ? 612  GLU B CA    1 
ATOM   10372 C  C     . GLU B 1 592 ? -10.342 -26.622 24.558  1.00 24.76 ? 612  GLU B C     1 
ATOM   10373 O  O     . GLU B 1 592 ? -10.057 -26.055 25.600  1.00 25.07 ? 612  GLU B O     1 
ATOM   10374 C  CB    . GLU B 1 592 ? -12.367 -28.117 24.887  1.00 24.34 ? 612  GLU B CB    1 
ATOM   10375 C  CG    . GLU B 1 592 ? -12.481 -27.999 26.406  1.00 24.09 ? 612  GLU B CG    1 
ATOM   10376 C  CD    . GLU B 1 592 ? -11.193 -28.363 27.170  1.00 23.36 ? 612  GLU B CD    1 
ATOM   10377 O  OE1   . GLU B 1 592 ? -10.315 -29.047 26.604  1.00 22.11 ? 612  GLU B OE1   1 
ATOM   10378 O  OE2   . GLU B 1 592 ? -11.070 -27.972 28.350  1.00 21.47 ? 612  GLU B OE2   1 
ATOM   10379 N  N     . GLN B 1 593 ? -9.419  -27.018 23.682  1.00 24.98 ? 613  GLN B N     1 
ATOM   10380 C  CA    . GLN B 1 593 ? -7.992  -26.746 23.860  1.00 24.82 ? 613  GLN B CA    1 
ATOM   10381 C  C     . GLN B 1 593 ? -7.714  -25.261 24.042  1.00 24.69 ? 613  GLN B C     1 
ATOM   10382 O  O     . GLN B 1 593 ? -6.745  -24.875 24.704  1.00 24.91 ? 613  GLN B O     1 
ATOM   10383 C  CB    . GLN B 1 593 ? -7.205  -27.299 22.664  1.00 25.07 ? 613  GLN B CB    1 
ATOM   10384 C  CG    . GLN B 1 593 ? -5.691  -27.396 22.850  1.00 26.29 ? 613  GLN B CG    1 
ATOM   10385 C  CD    . GLN B 1 593 ? -5.276  -28.413 23.899  1.00 27.90 ? 613  GLN B CD    1 
ATOM   10386 O  OE1   . GLN B 1 593 ? -6.092  -28.893 24.692  1.00 29.39 ? 613  GLN B OE1   1 
ATOM   10387 N  NE2   . GLN B 1 593 ? -3.995  -28.728 23.924  1.00 29.67 ? 613  GLN B NE2   1 
ATOM   10388 N  N     . ALA B 1 594 ? -8.569  -24.421 23.457  1.00 24.22 ? 614  ALA B N     1 
ATOM   10389 C  CA    . ALA B 1 594 ? -8.418  -22.978 23.576  1.00 23.40 ? 614  ALA B CA    1 
ATOM   10390 C  C     . ALA B 1 594 ? -8.778  -22.460 24.969  1.00 22.62 ? 614  ALA B C     1 
ATOM   10391 O  O     . ALA B 1 594 ? -8.308  -21.400 25.361  1.00 22.52 ? 614  ALA B O     1 
ATOM   10392 C  CB    . ALA B 1 594 ? -9.266  -22.269 22.506  1.00 23.31 ? 614  ALA B CB    1 
ATOM   10393 N  N     . ILE B 1 595 ? -9.607  -23.198 25.708  1.00 22.02 ? 615  ILE B N     1 
ATOM   10394 C  CA    . ILE B 1 595 ? -10.156 -22.715 26.980  1.00 21.25 ? 615  ILE B CA    1 
ATOM   10395 C  C     . ILE B 1 595 ? -10.040 -23.728 28.133  1.00 20.87 ? 615  ILE B C     1 
ATOM   10396 O  O     . ILE B 1 595 ? -10.998 -23.941 28.902  1.00 20.78 ? 615  ILE B O     1 
ATOM   10397 C  CB    . ILE B 1 595 ? -11.631 -22.255 26.809  1.00 21.19 ? 615  ILE B CB    1 
ATOM   10398 C  CG1   . ILE B 1 595 ? -12.533 -23.384 26.306  1.00 20.49 ? 615  ILE B CG1   1 
ATOM   10399 C  CG2   . ILE B 1 595 ? -11.712 -21.059 25.834  1.00 20.67 ? 615  ILE B CG2   1 
ATOM   10400 C  CD1   . ILE B 1 595 ? -14.060 -23.075 26.503  1.00 19.46 ? 615  ILE B CD1   1 
ATOM   10401 N  N     . THR B 1 596 ? -8.850  -24.306 28.279  1.00 20.13 ? 616  THR B N     1 
ATOM   10402 C  CA    . THR B 1 596 ? -8.584  -25.308 29.322  1.00 19.96 ? 616  THR B CA    1 
ATOM   10403 C  C     . THR B 1 596 ? -8.635  -24.694 30.713  1.00 20.27 ? 616  THR B C     1 
ATOM   10404 O  O     . THR B 1 596 ? -8.850  -25.390 31.709  1.00 20.88 ? 616  THR B O     1 
ATOM   10405 C  CB    . THR B 1 596 ? -7.206  -26.023 29.122  1.00 19.94 ? 616  THR B CB    1 
ATOM   10406 O  OG1   . THR B 1 596 ? -6.133  -25.067 29.156  1.00 18.83 ? 616  THR B OG1   1 
ATOM   10407 C  CG2   . THR B 1 596 ? -7.187  -26.773 27.798  1.00 19.38 ? 616  THR B CG2   1 
ATOM   10408 N  N     . TRP B 1 597 ? -8.428  -23.389 30.783  1.00 20.41 ? 617  TRP B N     1 
ATOM   10409 C  CA    . TRP B 1 597 ? -8.599  -22.665 32.022  1.00 20.53 ? 617  TRP B CA    1 
ATOM   10410 C  C     . TRP B 1 597 ? -10.032 -22.793 32.568  1.00 21.15 ? 617  TRP B C     1 
ATOM   10411 O  O     . TRP B 1 597 ? -10.220 -22.823 33.784  1.00 21.29 ? 617  TRP B O     1 
ATOM   10412 C  CB    . TRP B 1 597 ? -8.206  -21.197 31.842  1.00 20.63 ? 617  TRP B CB    1 
ATOM   10413 C  CG    . TRP B 1 597 ? -8.847  -20.465 30.682  1.00 19.80 ? 617  TRP B CG    1 
ATOM   10414 C  CD1   . TRP B 1 597 ? -8.281  -20.201 29.464  1.00 20.58 ? 617  TRP B CD1   1 
ATOM   10415 C  CD2   . TRP B 1 597 ? -10.156 -19.872 30.651  1.00 18.41 ? 617  TRP B CD2   1 
ATOM   10416 N  NE1   . TRP B 1 597 ? -9.166  -19.490 28.673  1.00 18.98 ? 617  TRP B NE1   1 
ATOM   10417 C  CE2   . TRP B 1 597 ? -10.317 -19.274 29.383  1.00 17.98 ? 617  TRP B CE2   1 
ATOM   10418 C  CE3   . TRP B 1 597 ? -11.204 -19.783 31.578  1.00 18.80 ? 617  TRP B CE3   1 
ATOM   10419 C  CZ2   . TRP B 1 597 ? -11.491 -18.605 29.014  1.00 18.79 ? 617  TRP B CZ2   1 
ATOM   10420 C  CZ3   . TRP B 1 597 ? -12.372 -19.110 31.211  1.00 18.65 ? 617  TRP B CZ3   1 
ATOM   10421 C  CH2   . TRP B 1 597 ? -12.501 -18.531 29.941  1.00 19.11 ? 617  TRP B CH2   1 
ATOM   10422 N  N     . ALA B 1 598 ? -11.022 -22.931 31.675  1.00 21.46 ? 618  ALA B N     1 
ATOM   10423 C  CA    . ALA B 1 598 ? -12.437 -23.029 32.069  1.00 21.38 ? 618  ALA B CA    1 
ATOM   10424 C  C     . ALA B 1 598 ? -12.759 -24.379 32.664  1.00 21.44 ? 618  ALA B C     1 
ATOM   10425 O  O     . ALA B 1 598 ? -13.907 -24.655 32.975  1.00 21.32 ? 618  ALA B O     1 
ATOM   10426 C  CB    . ALA B 1 598 ? -13.366 -22.754 30.875  1.00 21.16 ? 618  ALA B CB    1 
ATOM   10427 N  N     . ARG B 1 599 ? -11.753 -25.239 32.799  1.00 21.83 ? 619  ARG B N     1 
ATOM   10428 C  CA    . ARG B 1 599 ? -11.892 -26.435 33.628  1.00 21.64 ? 619  ARG B CA    1 
ATOM   10429 C  C     . ARG B 1 599 ? -11.876 -26.091 35.114  1.00 21.46 ? 619  ARG B C     1 
ATOM   10430 O  O     . ARG B 1 599 ? -12.280 -26.903 35.939  1.00 21.90 ? 619  ARG B O     1 
ATOM   10431 C  CB    . ARG B 1 599 ? -10.764 -27.416 33.351  1.00 21.62 ? 619  ARG B CB    1 
ATOM   10432 C  CG    . ARG B 1 599 ? -10.776 -28.008 31.951  1.00 22.49 ? 619  ARG B CG    1 
ATOM   10433 C  CD    . ARG B 1 599 ? -9.481  -28.772 31.667  1.00 22.44 ? 619  ARG B CD    1 
ATOM   10434 N  NE    . ARG B 1 599 ? -9.367  -29.164 30.265  1.00 23.17 ? 619  ARG B NE    1 
ATOM   10435 C  CZ    . ARG B 1 599 ? -8.413  -29.956 29.770  1.00 24.26 ? 619  ARG B CZ    1 
ATOM   10436 N  NH1   . ARG B 1 599 ? -7.473  -30.466 30.554  1.00 24.51 ? 619  ARG B NH1   1 
ATOM   10437 N  NH2   . ARG B 1 599 ? -8.404  -30.256 28.479  1.00 25.11 ? 619  ARG B NH2   1 
ATOM   10438 N  N     . TYR B 1 600 ? -11.395 -24.907 35.466  1.00 21.11 ? 620  TYR B N     1 
ATOM   10439 C  CA    . TYR B 1 600 ? -11.043 -24.636 36.859  1.00 20.93 ? 620  TYR B CA    1 
ATOM   10440 C  C     . TYR B 1 600 ? -11.645 -23.320 37.366  1.00 20.94 ? 620  TYR B C     1 
ATOM   10441 O  O     . TYR B 1 600 ? -11.232 -22.234 36.926  1.00 21.30 ? 620  TYR B O     1 
ATOM   10442 C  CB    . TYR B 1 600 ? -9.520  -24.604 37.016  1.00 20.79 ? 620  TYR B CB    1 
ATOM   10443 C  CG    . TYR B 1 600 ? -8.804  -25.830 36.493  1.00 20.39 ? 620  TYR B CG    1 
ATOM   10444 C  CD1   . TYR B 1 600 ? -8.107  -25.788 35.293  1.00 20.04 ? 620  TYR B CD1   1 
ATOM   10445 C  CD2   . TYR B 1 600 ? -8.811  -27.032 37.201  1.00 20.81 ? 620  TYR B CD2   1 
ATOM   10446 C  CE1   . TYR B 1 600 ? -7.443  -26.906 34.801  1.00 19.56 ? 620  TYR B CE1   1 
ATOM   10447 C  CE2   . TYR B 1 600 ? -8.150  -28.164 36.713  1.00 20.57 ? 620  TYR B CE2   1 
ATOM   10448 C  CZ    . TYR B 1 600 ? -7.463  -28.082 35.507  1.00 20.11 ? 620  TYR B CZ    1 
ATOM   10449 O  OH    . TYR B 1 600 ? -6.800  -29.170 34.999  1.00 20.58 ? 620  TYR B OH    1 
ATOM   10450 N  N     . PRO B 1 601 ? -12.631 -23.404 38.282  1.00 21.03 ? 621  PRO B N     1 
ATOM   10451 C  CA    . PRO B 1 601 ? -13.029 -22.178 38.980  1.00 20.90 ? 621  PRO B CA    1 
ATOM   10452 C  C     . PRO B 1 601 ? -11.836 -21.520 39.676  1.00 20.84 ? 621  PRO B C     1 
ATOM   10453 O  O     . PRO B 1 601 ? -11.745 -20.298 39.736  1.00 20.28 ? 621  PRO B O     1 
ATOM   10454 C  CB    . PRO B 1 601 ? -14.055 -22.657 40.008  1.00 20.93 ? 621  PRO B CB    1 
ATOM   10455 C  CG    . PRO B 1 601 ? -14.015 -24.178 39.977  1.00 21.21 ? 621  PRO B CG    1 
ATOM   10456 C  CD    . PRO B 1 601 ? -13.493 -24.548 38.639  1.00 21.10 ? 621  PRO B CD    1 
ATOM   10457 N  N     . LEU B 1 602 ? -10.930 -22.342 40.197  1.00 21.04 ? 622  LEU B N     1 
ATOM   10458 C  CA    . LEU B 1 602 ? -9.708  -21.848 40.811  1.00 21.06 ? 622  LEU B CA    1 
ATOM   10459 C  C     . LEU B 1 602 ? -8.576  -22.813 40.504  1.00 20.98 ? 622  LEU B C     1 
ATOM   10460 O  O     . LEU B 1 602 ? -8.730  -24.025 40.648  1.00 21.23 ? 622  LEU B O     1 
ATOM   10461 C  CB    . LEU B 1 602 ? -9.871  -21.693 42.329  1.00 20.99 ? 622  LEU B CB    1 
ATOM   10462 C  CG    . LEU B 1 602 ? -8.583  -21.350 43.122  1.00 21.08 ? 622  LEU B CG    1 
ATOM   10463 C  CD1   . LEU B 1 602 ? -8.067  -19.962 42.762  1.00 17.45 ? 622  LEU B CD1   1 
ATOM   10464 C  CD2   . LEU B 1 602 ? -8.785  -21.483 44.644  1.00 19.87 ? 622  LEU B CD2   1 
ATOM   10465 N  N     . ALA B 1 603 ? -7.450  -22.266 40.064  1.00 20.66 ? 623  ALA B N     1 
ATOM   10466 C  CA    . ALA B 1 603 ? -6.204  -23.012 40.010  1.00 20.88 ? 623  ALA B CA    1 
ATOM   10467 C  C     . ALA B 1 603 ? -5.088  -22.106 40.476  1.00 20.89 ? 623  ALA B C     1 
ATOM   10468 O  O     . ALA B 1 603 ? -5.127  -20.894 40.292  1.00 21.04 ? 623  ALA B O     1 
ATOM   10469 C  CB    . ALA B 1 603 ? -5.923  -23.536 38.602  1.00 20.72 ? 623  ALA B CB    1 
ATOM   10470 N  N     . VAL B 1 604 ? -4.084  -22.705 41.088  1.00 21.44 ? 624  VAL B N     1 
ATOM   10471 C  CA    . VAL B 1 604 ? -3.006  -21.943 41.666  1.00 21.94 ? 624  VAL B CA    1 
ATOM   10472 C  C     . VAL B 1 604 ? -1.716  -22.394 41.007  1.00 22.35 ? 624  VAL B C     1 
ATOM   10473 O  O     . VAL B 1 604 ? -1.434  -23.589 40.958  1.00 23.17 ? 624  VAL B O     1 
ATOM   10474 C  CB    . VAL B 1 604 ? -2.961  -22.140 43.195  1.00 22.12 ? 624  VAL B CB    1 
ATOM   10475 C  CG1   . VAL B 1 604 ? -1.891  -21.234 43.835  1.00 21.51 ? 624  VAL B CG1   1 
ATOM   10476 C  CG2   . VAL B 1 604 ? -4.345  -21.858 43.803  1.00 21.38 ? 624  VAL B CG2   1 
ATOM   10477 N  N     . THR B 1 605 ? -0.956  -21.443 40.472  1.00 22.66 ? 625  THR B N     1 
ATOM   10478 C  CA    . THR B 1 605 ? 0.341   -21.752 39.865  1.00 22.82 ? 625  THR B CA    1 
ATOM   10479 C  C     . THR B 1 605 ? 1.470   -20.992 40.534  1.00 23.31 ? 625  THR B C     1 
ATOM   10480 O  O     . THR B 1 605 ? 1.271   -19.944 41.163  1.00 22.54 ? 625  THR B O     1 
ATOM   10481 C  CB    . THR B 1 605 ? 0.396   -21.460 38.329  1.00 22.48 ? 625  THR B CB    1 
ATOM   10482 O  OG1   . THR B 1 605 ? 0.200   -20.060 38.076  1.00 21.20 ? 625  THR B OG1   1 
ATOM   10483 C  CG2   . THR B 1 605 ? -0.652  -22.268 37.594  1.00 22.56 ? 625  THR B CG2   1 
ATOM   10484 N  N     . LYS B 1 606 ? 2.660   -21.563 40.412  1.00 24.39 ? 626  LYS B N     1 
ATOM   10485 C  CA    . LYS B 1 606 ? 3.875   -20.878 40.786  1.00 25.54 ? 626  LYS B CA    1 
ATOM   10486 C  C     . LYS B 1 606 ? 4.127   -19.849 39.692  1.00 26.07 ? 626  LYS B C     1 
ATOM   10487 O  O     . LYS B 1 606 ? 4.009   -20.165 38.499  1.00 26.21 ? 626  LYS B O     1 
ATOM   10488 C  CB    . LYS B 1 606 ? 5.027   -21.873 40.896  1.00 25.76 ? 626  LYS B CB    1 
ATOM   10489 C  CG    . LYS B 1 606 ? 6.394   -21.257 41.117  1.00 27.12 ? 626  LYS B CG    1 
ATOM   10490 C  CD    . LYS B 1 606 ? 7.362   -22.335 41.602  1.00 29.55 ? 626  LYS B CD    1 
ATOM   10491 C  CE    . LYS B 1 606 ? 8.805   -21.926 41.420  1.00 32.03 ? 626  LYS B CE    1 
ATOM   10492 N  NZ    . LYS B 1 606 ? 9.725   -23.046 41.789  1.00 34.48 ? 626  LYS B NZ    1 
ATOM   10493 N  N     . TYR B 1 607 ? 4.437   -18.620 40.098  1.00 26.72 ? 627  TYR B N     1 
ATOM   10494 C  CA    . TYR B 1 607 ? 4.706   -17.534 39.159  1.00 27.41 ? 627  TYR B CA    1 
ATOM   10495 C  C     . TYR B 1 607 ? 5.792   -17.933 38.154  1.00 28.20 ? 627  TYR B C     1 
ATOM   10496 O  O     . TYR B 1 607 ? 6.835   -18.471 38.544  1.00 27.87 ? 627  TYR B O     1 
ATOM   10497 C  CB    . TYR B 1 607 ? 5.121   -16.254 39.903  1.00 27.42 ? 627  TYR B CB    1 
ATOM   10498 C  CG    . TYR B 1 607 ? 5.348   -15.072 38.977  1.00 27.88 ? 627  TYR B CG    1 
ATOM   10499 C  CD1   . TYR B 1 607 ? 6.570   -14.896 38.313  1.00 27.92 ? 627  TYR B CD1   1 
ATOM   10500 C  CD2   . TYR B 1 607 ? 4.340   -14.138 38.752  1.00 28.04 ? 627  TYR B CD2   1 
ATOM   10501 C  CE1   . TYR B 1 607 ? 6.771   -13.828 37.445  1.00 27.50 ? 627  TYR B CE1   1 
ATOM   10502 C  CE2   . TYR B 1 607 ? 4.536   -13.064 37.899  1.00 28.06 ? 627  TYR B CE2   1 
ATOM   10503 C  CZ    . TYR B 1 607 ? 5.744   -12.918 37.239  1.00 28.68 ? 627  TYR B CZ    1 
ATOM   10504 O  OH    . TYR B 1 607 ? 5.914   -11.844 36.391  1.00 28.86 ? 627  TYR B OH    1 
ATOM   10505 N  N     . ARG B 1 608 ? 5.519   -17.672 36.872  1.00 28.86 ? 628  ARG B N     1 
ATOM   10506 C  CA    . ARG B 1 608 ? 6.479   -17.830 35.773  1.00 29.51 ? 628  ARG B CA    1 
ATOM   10507 C  C     . ARG B 1 608 ? 6.272   -16.744 34.706  1.00 29.30 ? 628  ARG B C     1 
ATOM   10508 O  O     . ARG B 1 608 ? 5.137   -16.490 34.280  1.00 27.99 ? 628  ARG B O     1 
ATOM   10509 C  CB    . ARG B 1 608 ? 6.310   -19.195 35.102  1.00 30.25 ? 628  ARG B CB    1 
ATOM   10510 C  CG    . ARG B 1 608 ? 6.783   -20.365 35.937  1.00 32.91 ? 628  ARG B CG    1 
ATOM   10511 C  CD    . ARG B 1 608 ? 6.649   -21.686 35.197  1.00 36.32 ? 628  ARG B CD    1 
ATOM   10512 N  NE    . ARG B 1 608 ? 7.381   -22.741 35.903  1.00 40.05 ? 628  ARG B NE    1 
ATOM   10513 C  CZ    . ARG B 1 608 ? 8.543   -23.279 35.511  1.00 42.37 ? 628  ARG B CZ    1 
ATOM   10514 N  NH1   . ARG B 1 608 ? 9.150   -22.903 34.382  1.00 43.37 ? 628  ARG B NH1   1 
ATOM   10515 N  NH2   . ARG B 1 608 ? 9.109   -24.219 36.260  1.00 42.68 ? 628  ARG B NH2   1 
ATOM   10516 N  N     . GLU B 1 609 ? 7.377   -16.143 34.254  1.00 29.10 ? 629  GLU B N     1 
ATOM   10517 C  CA    . GLU B 1 609 ? 7.344   -15.154 33.180  1.00 29.42 ? 629  GLU B CA    1 
ATOM   10518 C  C     . GLU B 1 609 ? 6.835   -15.739 31.864  1.00 29.08 ? 629  GLU B C     1 
ATOM   10519 O  O     . GLU B 1 609 ? 6.344   -15.013 31.015  1.00 29.15 ? 629  GLU B O     1 
ATOM   10520 C  CB    . GLU B 1 609 ? 8.730   -14.519 32.961  1.00 29.76 ? 629  GLU B CB    1 
ATOM   10521 C  CG    . GLU B 1 609 ? 9.184   -13.557 34.083  1.00 30.56 ? 629  GLU B CG    1 
ATOM   10522 C  CD    . GLU B 1 609 ? 8.404   -12.234 34.141  1.00 31.83 ? 629  GLU B CD    1 
ATOM   10523 O  OE1   . GLU B 1 609 ? 7.917   -11.751 33.094  1.00 31.44 ? 629  GLU B OE1   1 
ATOM   10524 O  OE2   . GLU B 1 609 ? 8.293   -11.662 35.251  1.00 33.14 ? 629  GLU B OE2   1 
ATOM   10525 N  N     . SER B 1 610 ? 6.941   -17.051 31.696  1.00 28.94 ? 630  SER B N     1 
ATOM   10526 C  CA    . SER B 1 610 ? 6.435   -17.700 30.496  1.00 28.93 ? 630  SER B CA    1 
ATOM   10527 C  C     . SER B 1 610 ? 4.927   -17.983 30.573  1.00 28.89 ? 630  SER B C     1 
ATOM   10528 O  O     . SER B 1 610 ? 4.365   -18.529 29.631  1.00 29.08 ? 630  SER B O     1 
ATOM   10529 C  CB    . SER B 1 610 ? 7.174   -19.004 30.273  1.00 28.67 ? 630  SER B CB    1 
ATOM   10530 O  OG    . SER B 1 610 ? 6.945   -19.870 31.362  1.00 29.38 ? 630  SER B OG    1 
ATOM   10531 N  N     . GLU B 1 611 ? 4.288   -17.616 31.685  1.00 28.54 ? 631  GLU B N     1 
ATOM   10532 C  CA    . GLU B 1 611 ? 2.879   -17.910 31.917  1.00 28.23 ? 631  GLU B CA    1 
ATOM   10533 C  C     . GLU B 1 611 ? 2.136   -16.675 32.433  1.00 27.68 ? 631  GLU B C     1 
ATOM   10534 O  O     . GLU B 1 611 ? 1.354   -16.769 33.373  1.00 27.61 ? 631  GLU B O     1 
ATOM   10535 C  CB    . GLU B 1 611 ? 2.752   -19.050 32.934  1.00 28.34 ? 631  GLU B CB    1 
ATOM   10536 C  CG    . GLU B 1 611 ? 3.505   -20.344 32.566  1.00 29.41 ? 631  GLU B CG    1 
ATOM   10537 C  CD    . GLU B 1 611 ? 3.423   -21.407 33.654  1.00 30.66 ? 631  GLU B CD    1 
ATOM   10538 O  OE1   . GLU B 1 611 ? 3.081   -21.076 34.817  1.00 31.54 ? 631  GLU B OE1   1 
ATOM   10539 O  OE2   . GLU B 1 611 ? 3.714   -22.581 33.351  1.00 31.46 ? 631  GLU B OE2   1 
ATOM   10540 N  N     . LEU B 1 612 ? 2.374   -15.517 31.824  1.00 26.86 ? 632  LEU B N     1 
ATOM   10541 C  CA    . LEU B 1 612 ? 1.727   -14.285 32.280  1.00 26.59 ? 632  LEU B CA    1 
ATOM   10542 C  C     . LEU B 1 612 ? 0.256   -14.204 31.852  1.00 26.01 ? 632  LEU B C     1 
ATOM   10543 O  O     . LEU B 1 612 ? -0.530  -13.492 32.473  1.00 25.54 ? 632  LEU B O     1 
ATOM   10544 C  CB    . LEU B 1 612 ? 2.464   -13.054 31.759  1.00 26.57 ? 632  LEU B CB    1 
ATOM   10545 C  CG    . LEU B 1 612 ? 3.959   -12.975 32.072  1.00 27.65 ? 632  LEU B CG    1 
ATOM   10546 C  CD1   . LEU B 1 612 ? 4.502   -11.665 31.517  1.00 27.96 ? 632  LEU B CD1   1 
ATOM   10547 C  CD2   . LEU B 1 612 ? 4.235   -13.114 33.573  1.00 27.89 ? 632  LEU B CD2   1 
ATOM   10548 N  N     . CYS B 1 613 ? -0.102  -14.940 30.803  1.00 25.75 ? 633  CYS B N     1 
ATOM   10549 C  CA    . CYS B 1 613 ? -1.437  -14.877 30.212  1.00 25.94 ? 633  CYS B CA    1 
ATOM   10550 C  C     . CYS B 1 613 ? -2.024  -16.257 29.955  1.00 24.80 ? 633  CYS B C     1 
ATOM   10551 O  O     . CYS B 1 613 ? -1.317  -17.176 29.556  1.00 24.95 ? 633  CYS B O     1 
ATOM   10552 C  CB    . CYS B 1 613 ? -1.380  -14.099 28.892  1.00 25.93 ? 633  CYS B CB    1 
ATOM   10553 S  SG    . CYS B 1 613 ? -0.861  -12.394 29.094  1.00 30.35 ? 633  CYS B SG    1 
ATOM   10554 N  N     . SER B 1 614 ? -3.331  -16.388 30.155  1.00 23.87 ? 634  SER B N     1 
ATOM   10555 C  CA    . SER B 1 614 ? -4.011  -17.646 29.906  1.00 22.98 ? 634  SER B CA    1 
ATOM   10556 C  C     . SER B 1 614 ? -4.584  -17.714 28.491  1.00 22.27 ? 634  SER B C     1 
ATOM   10557 O  O     . SER B 1 614 ? -5.003  -18.775 28.055  1.00 22.13 ? 634  SER B O     1 
ATOM   10558 C  CB    . SER B 1 614 ? -5.118  -17.871 30.942  1.00 23.05 ? 634  SER B CB    1 
ATOM   10559 O  OG    . SER B 1 614 ? -5.954  -16.740 31.056  1.00 23.13 ? 634  SER B OG    1 
ATOM   10560 N  N     . SER B 1 615 ? -4.616  -16.588 27.787  1.00 21.59 ? 635  SER B N     1 
ATOM   10561 C  CA    . SER B 1 615 ? -5.133  -16.554 26.414  1.00 21.23 ? 635  SER B CA    1 
ATOM   10562 C  C     . SER B 1 615 ? -4.264  -15.654 25.545  1.00 20.74 ? 635  SER B C     1 
ATOM   10563 O  O     . SER B 1 615 ? -3.165  -15.273 25.955  1.00 20.95 ? 635  SER B O     1 
ATOM   10564 C  CB    . SER B 1 615 ? -6.589  -16.095 26.402  1.00 21.28 ? 635  SER B CB    1 
ATOM   10565 O  OG    . SER B 1 615 ? -7.228  -16.521 25.215  1.00 22.26 ? 635  SER B OG    1 
ATOM   10566 N  N     . SER B 1 616 ? -4.749  -15.338 24.349  1.00 20.19 ? 636  SER B N     1 
ATOM   10567 C  CA    . SER B 1 616 ? -4.060  -14.449 23.410  1.00 20.16 ? 636  SER B CA    1 
ATOM   10568 C  C     . SER B 1 616 ? -5.058  -14.016 22.332  1.00 19.69 ? 636  SER B C     1 
ATOM   10569 O  O     . SER B 1 616 ? -6.107  -14.627 22.177  1.00 19.12 ? 636  SER B O     1 
ATOM   10570 C  CB    . SER B 1 616 ? -2.882  -15.177 22.739  1.00 20.11 ? 636  SER B CB    1 
ATOM   10571 O  OG    . SER B 1 616 ? -3.336  -16.027 21.676  1.00 20.19 ? 636  SER B OG    1 
ATOM   10572 N  N     . ILE B 1 617 ? -4.709  -12.987 21.568  1.00 20.12 ? 637  ILE B N     1 
ATOM   10573 C  CA    . ILE B 1 617 ? -5.535  -12.547 20.416  1.00 20.44 ? 637  ILE B CA    1 
ATOM   10574 C  C     . ILE B 1 617 ? -5.667  -13.583 19.293  1.00 20.67 ? 637  ILE B C     1 
ATOM   10575 O  O     . ILE B 1 617 ? -6.485  -13.409 18.387  1.00 21.03 ? 637  ILE B O     1 
ATOM   10576 C  CB    . ILE B 1 617 ? -5.005  -11.240 19.775  1.00 20.29 ? 637  ILE B CB    1 
ATOM   10577 C  CG1   . ILE B 1 617 ? -3.597  -11.451 19.193  1.00 20.09 ? 637  ILE B CG1   1 
ATOM   10578 C  CG2   . ILE B 1 617 ? -5.042  -10.110 20.802  1.00 20.44 ? 637  ILE B CG2   1 
ATOM   10579 C  CD1   . ILE B 1 617 ? -3.011  -10.220 18.513  1.00 20.60 ? 637  ILE B CD1   1 
ATOM   10580 N  N     . TYR B 1 618 ? -4.855  -14.638 19.350  1.00 20.93 ? 638  TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 618 ? -4.841  -15.691 18.340  1.00 21.13 ? 638  TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 618 ? -5.790  -16.850 18.643  1.00 20.88 ? 638  TYR B C     1 
ATOM   10583 O  O     . TYR B 1 618 ? -6.166  -17.582 17.732  1.00 20.89 ? 638  TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 618 ? -3.414  -16.238 18.180  1.00 21.32 ? 638  TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 618 ? -2.405  -15.151 17.949  1.00 21.85 ? 638  TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 618 ? -1.473  -14.826 18.922  1.00 22.83 ? 638  TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 618 ? -2.413  -14.415 16.770  1.00 23.94 ? 638  TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 618 ? -0.558  -13.810 18.724  1.00 23.90 ? 638  TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 618 ? -1.501  -13.395 16.553  1.00 23.73 ? 638  TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 618 ? -0.577  -13.093 17.536  1.00 24.48 ? 638  TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 618 ? 0.325   -12.079 17.327  1.00 25.57 ? 638  TYR B OH    1 
ATOM   10592 N  N     . HIS B 1 619 ? -6.167  -17.025 19.906  1.00 20.56 ? 639  HIS B N     1 
ATOM   10593 C  CA    . HIS B 1 619 ? -7.009  -18.164 20.295  1.00 20.80 ? 639  HIS B CA    1 
ATOM   10594 C  C     . HIS B 1 619 ? -8.331  -18.252 19.535  1.00 20.69 ? 639  HIS B C     1 
ATOM   10595 O  O     . HIS B 1 619 ? -8.770  -19.341 19.214  1.00 20.77 ? 639  HIS B O     1 
ATOM   10596 C  CB    . HIS B 1 619 ? -7.297  -18.156 21.802  1.00 21.21 ? 639  HIS B CB    1 
ATOM   10597 C  CG    . HIS B 1 619 ? -6.159  -18.661 22.638  1.00 20.91 ? 639  HIS B CG    1 
ATOM   10598 N  ND1   . HIS B 1 619 ? -4.913  -18.075 22.626  1.00 21.15 ? 639  HIS B ND1   1 
ATOM   10599 C  CD2   . HIS B 1 619 ? -6.086  -19.690 23.516  1.00 20.12 ? 639  HIS B CD2   1 
ATOM   10600 C  CE1   . HIS B 1 619 ? -4.115  -18.729 23.455  1.00 22.09 ? 639  HIS B CE1   1 
ATOM   10601 N  NE2   . HIS B 1 619 ? -4.803  -19.712 24.010  1.00 20.91 ? 639  HIS B NE2   1 
ATOM   10602 N  N     . GLN B 1 620 ? -8.964  -17.117 19.256  1.00 20.70 ? 640  GLN B N     1 
ATOM   10603 C  CA    . GLN B 1 620 ? -10.264 -17.121 18.568  1.00 20.89 ? 640  GLN B CA    1 
ATOM   10604 C  C     . GLN B 1 620 ? -10.216 -17.855 17.229  1.00 21.07 ? 640  GLN B C     1 
ATOM   10605 O  O     . GLN B 1 620 ? -11.116 -18.625 16.908  1.00 20.80 ? 640  GLN B O     1 
ATOM   10606 C  CB    . GLN B 1 620 ? -10.746 -15.684 18.350  1.00 20.78 ? 640  GLN B CB    1 
ATOM   10607 C  CG    . GLN B 1 620 ? -12.000 -15.530 17.501  1.00 20.80 ? 640  GLN B CG    1 
ATOM   10608 C  CD    . GLN B 1 620 ? -13.238 -16.045 18.191  1.00 19.96 ? 640  GLN B CD    1 
ATOM   10609 O  OE1   . GLN B 1 620 ? -14.030 -15.263 18.720  1.00 19.45 ? 640  GLN B OE1   1 
ATOM   10610 N  NE2   . GLN B 1 620 ? -13.416 -17.362 18.197  1.00 20.97 ? 640  GLN B NE2   1 
ATOM   10611 N  N     . ASN B 1 621 ? -9.172  -17.599 16.441  1.00 21.63 ? 641  ASN B N     1 
ATOM   10612 C  CA    . ASN B 1 621 ? -9.120  -18.101 15.070  1.00 21.84 ? 641  ASN B CA    1 
ATOM   10613 C  C     . ASN B 1 621 ? -8.238  -19.352 14.894  1.00 22.11 ? 641  ASN B C     1 
ATOM   10614 O  O     . ASN B 1 621 ? -8.218  -19.949 13.817  1.00 22.04 ? 641  ASN B O     1 
ATOM   10615 C  CB    . ASN B 1 621 ? -8.735  -16.971 14.097  1.00 21.80 ? 641  ASN B CB    1 
ATOM   10616 C  CG    . ASN B 1 621 ? -9.888  -15.997 13.833  1.00 21.93 ? 641  ASN B CG    1 
ATOM   10617 O  OD1   . ASN B 1 621 ? -11.053 -16.301 14.104  1.00 21.84 ? 641  ASN B OD1   1 
ATOM   10618 N  ND2   . ASN B 1 621 ? -9.561  -14.818 13.302  1.00 21.24 ? 641  ASN B ND2   1 
ATOM   10619 N  N     . ASP B 1 622 ? -7.523  -19.753 15.944  1.00 22.37 ? 642  ASP B N     1 
ATOM   10620 C  CA    . ASP B 1 622 ? -6.975  -21.118 16.007  1.00 22.44 ? 642  ASP B CA    1 
ATOM   10621 C  C     . ASP B 1 622 ? -7.147  -21.703 17.411  1.00 22.33 ? 642  ASP B C     1 
ATOM   10622 O  O     . ASP B 1 622 ? -6.167  -21.847 18.155  1.00 22.57 ? 642  ASP B O     1 
ATOM   10623 C  CB    . ASP B 1 622 ? -5.496  -21.178 15.567  1.00 22.20 ? 642  ASP B CB    1 
ATOM   10624 C  CG    . ASP B 1 622 ? -5.020  -22.610 15.301  1.00 22.94 ? 642  ASP B CG    1 
ATOM   10625 O  OD1   . ASP B 1 622 ? -5.788  -23.572 15.560  1.00 22.37 ? 642  ASP B OD1   1 
ATOM   10626 O  OD2   . ASP B 1 622 ? -3.877  -22.781 14.813  1.00 22.78 ? 642  ASP B OD2   1 
ATOM   10627 N  N     . PRO B 1 623 ? -8.392  -22.064 17.773  1.00 22.20 ? 643  PRO B N     1 
ATOM   10628 C  CA    . PRO B 1 623 ? -8.643  -22.665 19.081  1.00 22.29 ? 643  PRO B CA    1 
ATOM   10629 C  C     . PRO B 1 623 ? -8.172  -24.122 19.162  1.00 22.39 ? 643  PRO B C     1 
ATOM   10630 O  O     . PRO B 1 623 ? -8.092  -24.687 20.254  1.00 22.31 ? 643  PRO B O     1 
ATOM   10631 C  CB    . PRO B 1 623 ? -10.170 -22.571 19.221  1.00 22.20 ? 643  PRO B CB    1 
ATOM   10632 C  CG    . PRO B 1 623 ? -10.664 -22.624 17.828  1.00 22.82 ? 643  PRO B CG    1 
ATOM   10633 C  CD    . PRO B 1 623 ? -9.635  -21.901 17.000  1.00 22.10 ? 643  PRO B CD    1 
ATOM   10634 N  N     . TRP B 1 624 ? -7.873  -24.724 18.012  1.00 22.79 ? 644  TRP B N     1 
ATOM   10635 C  CA    . TRP B 1 624 ? -7.434  -26.111 17.969  1.00 23.21 ? 644  TRP B CA    1 
ATOM   10636 C  C     . TRP B 1 624 ? -5.956  -26.237 18.347  1.00 23.26 ? 644  TRP B C     1 
ATOM   10637 O  O     . TRP B 1 624 ? -5.567  -27.217 18.971  1.00 23.77 ? 644  TRP B O     1 
ATOM   10638 C  CB    . TRP B 1 624 ? -7.682  -26.719 16.585  1.00 23.22 ? 644  TRP B CB    1 
ATOM   10639 C  CG    . TRP B 1 624 ? -9.099  -26.609 16.142  1.00 23.31 ? 644  TRP B CG    1 
ATOM   10640 C  CD1   . TRP B 1 624 ? -10.132 -27.430 16.486  1.00 23.48 ? 644  TRP B CD1   1 
ATOM   10641 C  CD2   . TRP B 1 624 ? -9.650  -25.618 15.262  1.00 23.33 ? 644  TRP B CD2   1 
ATOM   10642 N  NE1   . TRP B 1 624 ? -11.296 -27.007 15.881  1.00 24.73 ? 644  TRP B NE1   1 
ATOM   10643 C  CE2   . TRP B 1 624 ? -11.028 -25.897 15.127  1.00 23.98 ? 644  TRP B CE2   1 
ATOM   10644 C  CE3   . TRP B 1 624 ? -9.117  -24.515 14.587  1.00 22.38 ? 644  TRP B CE3   1 
ATOM   10645 C  CZ2   . TRP B 1 624 ? -11.873 -25.118 14.340  1.00 23.88 ? 644  TRP B CZ2   1 
ATOM   10646 C  CZ3   . TRP B 1 624 ? -9.955  -23.752 13.797  1.00 21.58 ? 644  TRP B CZ3   1 
ATOM   10647 C  CH2   . TRP B 1 624 ? -11.314 -24.055 13.678  1.00 22.29 ? 644  TRP B CH2   1 
ATOM   10648 N  N     . ASP B 1 625 ? -5.144  -25.249 17.989  1.00 23.48 ? 645  ASP B N     1 
ATOM   10649 C  CA    . ASP B 1 625 ? -3.706  -25.306 18.268  1.00 23.86 ? 645  ASP B CA    1 
ATOM   10650 C  C     . ASP B 1 625 ? -3.167  -23.939 18.713  1.00 23.47 ? 645  ASP B C     1 
ATOM   10651 O  O     . ASP B 1 625 ? -2.316  -23.350 18.049  1.00 23.91 ? 645  ASP B O     1 
ATOM   10652 C  CB    . ASP B 1 625 ? -2.972  -25.829 17.024  1.00 24.07 ? 645  ASP B CB    1 
ATOM   10653 C  CG    . ASP B 1 625 ? -1.504  -26.185 17.297  1.00 25.75 ? 645  ASP B CG    1 
ATOM   10654 O  OD1   . ASP B 1 625 ? -1.055  -26.119 18.462  1.00 27.03 ? 645  ASP B OD1   1 
ATOM   10655 O  OD2   . ASP B 1 625 ? -0.797  -26.518 16.328  1.00 27.00 ? 645  ASP B OD2   1 
ATOM   10656 N  N     . PRO B 1 626 ? -3.668  -23.425 19.849  1.00 23.01 ? 646  PRO B N     1 
ATOM   10657 C  CA    . PRO B 1 626 ? -3.300  -22.080 20.290  1.00 22.84 ? 646  PRO B CA    1 
ATOM   10658 C  C     . PRO B 1 626 ? -1.906  -21.998 20.915  1.00 22.90 ? 646  PRO B C     1 
ATOM   10659 O  O     . PRO B 1 626 ? -1.374  -23.022 21.349  1.00 22.76 ? 646  PRO B O     1 
ATOM   10660 C  CB    . PRO B 1 626 ? -4.348  -21.778 21.356  1.00 22.77 ? 646  PRO B CB    1 
ATOM   10661 C  CG    . PRO B 1 626 ? -4.636  -23.116 21.950  1.00 22.76 ? 646  PRO B CG    1 
ATOM   10662 C  CD    . PRO B 1 626 ? -4.611  -24.063 20.784  1.00 22.85 ? 646  PRO B CD    1 
ATOM   10663 N  N     . PRO B 1 627 ? -1.340  -20.775 20.999  1.00 22.91 ? 647  PRO B N     1 
ATOM   10664 C  CA    . PRO B 1 627 ? -0.007  -20.563 21.544  1.00 22.84 ? 647  PRO B CA    1 
ATOM   10665 C  C     . PRO B 1 627 ? 0.067   -20.650 23.065  1.00 23.32 ? 647  PRO B C     1 
ATOM   10666 O  O     . PRO B 1 627 ? 1.168   -20.675 23.609  1.00 23.16 ? 647  PRO B O     1 
ATOM   10667 C  CB    . PRO B 1 627 ? 0.344   -19.146 21.083  1.00 22.67 ? 647  PRO B CB    1 
ATOM   10668 C  CG    . PRO B 1 627 ? -0.948  -18.466 20.943  1.00 23.22 ? 647  PRO B CG    1 
ATOM   10669 C  CD    . PRO B 1 627 ? -1.930  -19.518 20.503  1.00 22.85 ? 647  PRO B CD    1 
ATOM   10670 N  N     . VAL B 1 628 ? -1.077  -20.672 23.750  1.00 23.30 ? 648  VAL B N     1 
ATOM   10671 C  CA    . VAL B 1 628 ? -1.083  -20.821 25.196  1.00 23.35 ? 648  VAL B CA    1 
ATOM   10672 C  C     . VAL B 1 628 ? -2.172  -21.810 25.569  1.00 23.44 ? 648  VAL B C     1 
ATOM   10673 O  O     . VAL B 1 628 ? -3.340  -21.603 25.234  1.00 23.03 ? 648  VAL B O     1 
ATOM   10674 C  CB    . VAL B 1 628 ? -1.324  -19.471 25.927  1.00 23.59 ? 648  VAL B CB    1 
ATOM   10675 C  CG1   . VAL B 1 628 ? -1.344  -19.673 27.443  1.00 23.79 ? 648  VAL B CG1   1 
ATOM   10676 C  CG2   . VAL B 1 628 ? -0.273  -18.442 25.548  1.00 23.28 ? 648  VAL B CG2   1 
ATOM   10677 N  N     . VAL B 1 629 ? -1.773  -22.889 26.238  1.00 23.35 ? 649  VAL B N     1 
ATOM   10678 C  CA    . VAL B 1 629 ? -2.698  -23.883 26.753  1.00 23.33 ? 649  VAL B CA    1 
ATOM   10679 C  C     . VAL B 1 629 ? -2.584  -23.907 28.275  1.00 23.71 ? 649  VAL B C     1 
ATOM   10680 O  O     . VAL B 1 629 ? -1.582  -24.387 28.822  1.00 23.45 ? 649  VAL B O     1 
ATOM   10681 C  CB    . VAL B 1 629 ? -2.391  -25.267 26.181  1.00 23.37 ? 649  VAL B CB    1 
ATOM   10682 C  CG1   . VAL B 1 629 ? -3.302  -26.318 26.806  1.00 22.76 ? 649  VAL B CG1   1 
ATOM   10683 C  CG2   . VAL B 1 629 ? -2.519  -25.245 24.648  1.00 22.77 ? 649  VAL B CG2   1 
ATOM   10684 N  N     . PHE B 1 630 ? -3.609  -23.387 28.955  1.00 23.42 ? 650  PHE B N     1 
ATOM   10685 C  CA    . PHE B 1 630 ? -3.534  -23.195 30.403  1.00 23.48 ? 650  PHE B CA    1 
ATOM   10686 C  C     . PHE B 1 630 ? -3.177  -24.476 31.162  1.00 23.79 ? 650  PHE B C     1 
ATOM   10687 O  O     . PHE B 1 630 ? -2.384  -24.428 32.091  1.00 23.73 ? 650  PHE B O     1 
ATOM   10688 C  CB    . PHE B 1 630 ? -4.831  -22.618 30.975  1.00 23.41 ? 650  PHE B CB    1 
ATOM   10689 C  CG    . PHE B 1 630 ? -4.767  -22.420 32.442  1.00 22.92 ? 650  PHE B CG    1 
ATOM   10690 C  CD1   . PHE B 1 630 ? -4.207  -21.272 32.965  1.00 23.58 ? 650  PHE B CD1   1 
ATOM   10691 C  CD2   . PHE B 1 630 ? -5.187  -23.414 33.308  1.00 22.26 ? 650  PHE B CD2   1 
ATOM   10692 C  CE1   . PHE B 1 630 ? -4.110  -21.096 34.325  1.00 23.64 ? 650  PHE B CE1   1 
ATOM   10693 C  CE2   . PHE B 1 630 ? -5.092  -23.241 34.671  1.00 23.02 ? 650  PHE B CE2   1 
ATOM   10694 C  CZ    . PHE B 1 630 ? -4.555  -22.081 35.181  1.00 22.86 ? 650  PHE B CZ    1 
ATOM   10695 N  N     . GLU B 1 631 ? -3.763  -25.601 30.762  1.00 24.21 ? 651  GLU B N     1 
ATOM   10696 C  CA    . GLU B 1 631 ? -3.469  -26.916 31.356  1.00 25.42 ? 651  GLU B CA    1 
ATOM   10697 C  C     . GLU B 1 631 ? -1.965  -27.228 31.457  1.00 25.97 ? 651  GLU B C     1 
ATOM   10698 O  O     . GLU B 1 631 ? -1.526  -27.864 32.422  1.00 26.03 ? 651  GLU B O     1 
ATOM   10699 C  CB    . GLU B 1 631 ? -4.156  -28.025 30.542  1.00 25.54 ? 651  GLU B CB    1 
ATOM   10700 C  CG    . GLU B 1 631 ? -4.049  -29.452 31.128  1.00 26.45 ? 651  GLU B CG    1 
ATOM   10701 C  CD    . GLU B 1 631 ? -4.830  -29.641 32.426  1.00 27.84 ? 651  GLU B CD    1 
ATOM   10702 O  OE1   . GLU B 1 631 ? -5.761  -28.848 32.691  1.00 27.31 ? 651  GLU B OE1   1 
ATOM   10703 O  OE2   . GLU B 1 631 ? -4.516  -30.595 33.177  1.00 27.46 ? 651  GLU B OE2   1 
ATOM   10704 N  N     . GLN B 1 632 ? -1.193  -26.796 30.458  1.00 26.50 ? 652  GLN B N     1 
ATOM   10705 C  CA    . GLN B 1 632 ? 0.248   -27.067 30.425  1.00 27.31 ? 652  GLN B CA    1 
ATOM   10706 C  C     . GLN B 1 632 ? 0.965   -26.357 31.568  1.00 27.16 ? 652  GLN B C     1 
ATOM   10707 O  O     . GLN B 1 632 ? 2.014   -26.808 32.004  1.00 27.17 ? 652  GLN B O     1 
ATOM   10708 C  CB    . GLN B 1 632 ? 0.864   -26.708 29.056  1.00 27.39 ? 652  GLN B CB    1 
ATOM   10709 C  CG    . GLN B 1 632 ? 0.257   -27.566 27.925  1.00 29.44 ? 652  GLN B CG    1 
ATOM   10710 C  CD    . GLN B 1 632 ? 0.685   -27.183 26.503  1.00 31.90 ? 652  GLN B CD    1 
ATOM   10711 O  OE1   . GLN B 1 632 ? 1.310   -26.141 26.262  1.00 34.54 ? 652  GLN B OE1   1 
ATOM   10712 N  NE2   . GLN B 1 632 ? 0.331   -28.040 25.548  1.00 32.63 ? 652  GLN B NE2   1 
ATOM   10713 N  N     . PHE B 1 633 ? 0.383   -25.267 32.071  1.00 27.52 ? 653  PHE B N     1 
ATOM   10714 C  CA    . PHE B 1 633 ? 0.920   -24.592 33.257  1.00 27.72 ? 653  PHE B CA    1 
ATOM   10715 C  C     . PHE B 1 633 ? 0.996   -25.547 34.460  1.00 27.69 ? 653  PHE B C     1 
ATOM   10716 O  O     . PHE B 1 633 ? 1.878   -25.404 35.303  1.00 27.48 ? 653  PHE B O     1 
ATOM   10717 C  CB    . PHE B 1 633 ? 0.057   -23.388 33.659  1.00 27.99 ? 653  PHE B CB    1 
ATOM   10718 C  CG    . PHE B 1 633 ? 0.068   -22.228 32.681  1.00 28.50 ? 653  PHE B CG    1 
ATOM   10719 C  CD1   . PHE B 1 633 ? 0.796   -22.262 31.489  1.00 29.04 ? 653  PHE B CD1   1 
ATOM   10720 C  CD2   . PHE B 1 633 ? -0.697  -21.100 32.958  1.00 28.91 ? 653  PHE B CD2   1 
ATOM   10721 C  CE1   . PHE B 1 633 ? 0.774   -21.188 30.622  1.00 29.45 ? 653  PHE B CE1   1 
ATOM   10722 C  CE2   . PHE B 1 633 ? -0.728  -20.021 32.086  1.00 29.91 ? 653  PHE B CE2   1 
ATOM   10723 C  CZ    . PHE B 1 633 ? 0.007   -20.063 30.919  1.00 30.00 ? 653  PHE B CZ    1 
ATOM   10724 N  N     . LEU B 1 634 ? 0.062   -26.501 34.537  1.00 27.80 ? 654  LEU B N     1 
ATOM   10725 C  CA    . LEU B 1 634 ? -0.008  -27.465 35.639  1.00 27.78 ? 654  LEU B CA    1 
ATOM   10726 C  C     . LEU B 1 634 ? 0.816   -28.745 35.420  1.00 28.41 ? 654  LEU B C     1 
ATOM   10727 O  O     . LEU B 1 634 ? 0.939   -29.551 36.342  1.00 28.30 ? 654  LEU B O     1 
ATOM   10728 C  CB    . LEU B 1 634 ? -1.469  -27.878 35.878  1.00 27.66 ? 654  LEU B CB    1 
ATOM   10729 C  CG    . LEU B 1 634 ? -2.488  -26.756 36.091  1.00 27.34 ? 654  LEU B CG    1 
ATOM   10730 C  CD1   . LEU B 1 634 ? -3.928  -27.298 36.085  1.00 26.40 ? 654  LEU B CD1   1 
ATOM   10731 C  CD2   . LEU B 1 634 ? -2.189  -26.009 37.381  1.00 26.45 ? 654  LEU B CD2   1 
ATOM   10732 N  N     . HIS B 1 635 ? 1.368   -28.939 34.220  1.00 28.94 ? 655  HIS B N     1 
ATOM   10733 C  CA    A HIS B 1 635 ? 2.022   -30.203 33.869  0.50 29.12 ? 655  HIS B CA    1 
ATOM   10734 C  CA    B HIS B 1 635 ? 2.029   -30.206 33.865  0.50 29.10 ? 655  HIS B CA    1 
ATOM   10735 C  C     . HIS B 1 635 ? 3.229   -30.515 34.758  1.00 29.25 ? 655  HIS B C     1 
ATOM   10736 O  O     . HIS B 1 635 ? 3.415   -31.659 35.178  1.00 29.22 ? 655  HIS B O     1 
ATOM   10737 C  CB    A HIS B 1 635 ? 2.429   -30.202 32.390  0.50 29.22 ? 655  HIS B CB    1 
ATOM   10738 C  CB    B HIS B 1 635 ? 2.472   -30.217 32.393  0.50 29.21 ? 655  HIS B CB    1 
ATOM   10739 C  CG    A HIS B 1 635 ? 1.287   -30.458 31.453  0.50 29.34 ? 655  HIS B CG    1 
ATOM   10740 C  CG    B HIS B 1 635 ? 3.061   -31.523 31.947  0.50 29.11 ? 655  HIS B CG    1 
ATOM   10741 N  ND1   A HIS B 1 635 ? 1.455   -30.593 30.091  0.50 29.08 ? 655  HIS B ND1   1 
ATOM   10742 N  ND1   B HIS B 1 635 ? 4.418   -31.716 31.795  0.50 29.50 ? 655  HIS B ND1   1 
ATOM   10743 C  CD2   A HIS B 1 635 ? -0.036  -30.628 31.687  0.50 28.99 ? 655  HIS B CD2   1 
ATOM   10744 C  CD2   B HIS B 1 635 ? 2.477   -32.704 31.632  0.50 29.37 ? 655  HIS B CD2   1 
ATOM   10745 C  CE1   A HIS B 1 635 ? 0.283   -30.822 29.526  0.50 28.81 ? 655  HIS B CE1   1 
ATOM   10746 C  CE1   B HIS B 1 635 ? 4.645   -32.958 31.407  0.50 29.35 ? 655  HIS B CE1   1 
ATOM   10747 N  NE2   A HIS B 1 635 ? -0.637  -30.851 30.472  0.50 28.50 ? 655  HIS B NE2   1 
ATOM   10748 N  NE2   B HIS B 1 635 ? 3.483   -33.579 31.300  0.50 29.75 ? 655  HIS B NE2   1 
ATOM   10749 N  N     . ASN B 1 636 ? 4.050   -29.507 35.047  1.00 29.26 ? 656  ASN B N     1 
ATOM   10750 C  CA    . ASN B 1 636 ? 5.225   -29.743 35.904  1.00 29.53 ? 656  ASN B CA    1 
ATOM   10751 C  C     . ASN B 1 636 ? 4.864   -29.917 37.385  1.00 29.55 ? 656  ASN B C     1 
ATOM   10752 O  O     . ASN B 1 636 ? 5.723   -30.262 38.186  1.00 29.94 ? 656  ASN B O     1 
ATOM   10753 C  CB    . ASN B 1 636 ? 6.299   -28.666 35.721  1.00 29.48 ? 656  ASN B CB    1 
ATOM   10754 C  CG    . ASN B 1 636 ? 5.754   -27.256 35.856  1.00 30.84 ? 656  ASN B CG    1 
ATOM   10755 O  OD1   . ASN B 1 636 ? 4.565   -27.055 36.162  1.00 31.97 ? 656  ASN B OD1   1 
ATOM   10756 N  ND2   . ASN B 1 636 ? 6.610   -26.260 35.600  1.00 30.56 ? 656  ASN B ND2   1 
ATOM   10757 N  N     . ASN B 1 637 ? 3.597   -29.683 37.737  1.00 29.43 ? 657  ASN B N     1 
ATOM   10758 C  CA    . ASN B 1 637 ? 3.091   -29.888 39.098  1.00 29.29 ? 657  ASN B CA    1 
ATOM   10759 C  C     . ASN B 1 637 ? 4.082   -29.451 40.181  1.00 29.51 ? 657  ASN B C     1 
ATOM   10760 O  O     . ASN B 1 637 ? 4.548   -30.252 40.982  1.00 29.27 ? 657  ASN B O     1 
ATOM   10761 C  CB    . ASN B 1 637 ? 2.685   -31.350 39.293  1.00 29.26 ? 657  ASN B CB    1 
ATOM   10762 C  CG    . ASN B 1 637 ? 1.837   -31.566 40.538  1.00 29.41 ? 657  ASN B CG    1 
ATOM   10763 O  OD1   . ASN B 1 637 ? 1.349   -30.613 41.155  1.00 30.14 ? 657  ASN B OD1   1 
ATOM   10764 N  ND2   . ASN B 1 637 ? 1.669   -32.826 40.921  1.00 28.92 ? 657  ASN B ND2   1 
ATOM   10765 N  N     . GLU B 1 638 ? 4.380   -28.160 40.199  1.00 29.80 ? 658  GLU B N     1 
ATOM   10766 C  CA    . GLU B 1 638 ? 5.433   -27.616 41.042  1.00 30.11 ? 658  GLU B CA    1 
ATOM   10767 C  C     . GLU B 1 638 ? 5.003   -27.435 42.493  1.00 30.22 ? 658  GLU B C     1 
ATOM   10768 O  O     . GLU B 1 638 ? 3.805   -27.379 42.808  1.00 29.96 ? 658  GLU B O     1 
ATOM   10769 C  CB    . GLU B 1 638 ? 5.886   -26.265 40.501  1.00 30.41 ? 658  GLU B CB    1 
ATOM   10770 C  CG    . GLU B 1 638 ? 6.407   -26.313 39.080  1.00 31.51 ? 658  GLU B CG    1 
ATOM   10771 C  CD    . GLU B 1 638 ? 6.694   -24.935 38.533  1.00 33.41 ? 658  GLU B CD    1 
ATOM   10772 O  OE1   . GLU B 1 638 ? 5.743   -24.265 38.035  1.00 32.83 ? 658  GLU B OE1   1 
ATOM   10773 O  OE2   . GLU B 1 638 ? 7.885   -24.531 38.592  1.00 33.04 ? 658  GLU B OE2   1 
ATOM   10774 N  N     . ASN B 1 639 ? 6.007   -27.343 43.362  1.00 29.97 ? 659  ASN B N     1 
ATOM   10775 C  CA    . ASN B 1 639 ? 5.806   -27.050 44.773  1.00 29.84 ? 659  ASN B CA    1 
ATOM   10776 C  C     . ASN B 1 639 ? 5.302   -25.622 44.950  1.00 29.71 ? 659  ASN B C     1 
ATOM   10777 O  O     . ASN B 1 639 ? 5.873   -24.696 44.389  1.00 29.64 ? 659  ASN B O     1 
ATOM   10778 C  CB    . ASN B 1 639 ? 7.125   -27.202 45.534  1.00 29.69 ? 659  ASN B CB    1 
ATOM   10779 C  CG    . ASN B 1 639 ? 6.951   -27.061 47.025  1.00 28.87 ? 659  ASN B CG    1 
ATOM   10780 O  OD1   . ASN B 1 639 ? 7.143   -25.987 47.580  1.00 29.26 ? 659  ASN B OD1   1 
ATOM   10781 N  ND2   . ASN B 1 639 ? 6.568   -28.145 47.679  1.00 28.79 ? 659  ASN B ND2   1 
ATOM   10782 N  N     . ILE B 1 640 ? 4.247   -25.452 45.738  1.00 30.10 ? 660  ILE B N     1 
ATOM   10783 C  CA    . ILE B 1 640 ? 3.649   -24.131 45.972  1.00 30.44 ? 660  ILE B CA    1 
ATOM   10784 C  C     . ILE B 1 640 ? 3.674   -23.755 47.458  1.00 31.12 ? 660  ILE B C     1 
ATOM   10785 O  O     . ILE B 1 640 ? 2.899   -22.909 47.915  1.00 31.01 ? 660  ILE B O     1 
ATOM   10786 C  CB    . ILE B 1 640 ? 2.191   -24.046 45.408  1.00 30.56 ? 660  ILE B CB    1 
ATOM   10787 C  CG1   . ILE B 1 640 ? 1.296   -25.147 45.986  1.00 30.35 ? 660  ILE B CG1   1 
ATOM   10788 C  CG2   . ILE B 1 640 ? 2.204   -24.128 43.882  1.00 29.46 ? 660  ILE B CG2   1 
ATOM   10789 C  CD1   . ILE B 1 640 ? -0.192  -24.938 45.705  1.00 30.39 ? 660  ILE B CD1   1 
ATOM   10790 N  N     . GLU B 1 641 ? 4.580   -24.380 48.206  1.00 31.73 ? 661  GLU B N     1 
ATOM   10791 C  CA    . GLU B 1 641 ? 4.803   -24.023 49.599  1.00 32.54 ? 661  GLU B CA    1 
ATOM   10792 C  C     . GLU B 1 641 ? 5.790   -22.884 49.599  1.00 32.47 ? 661  GLU B C     1 
ATOM   10793 O  O     . GLU B 1 641 ? 6.906   -23.040 49.113  1.00 33.61 ? 661  GLU B O     1 
ATOM   10794 C  CB    . GLU B 1 641 ? 5.384   -25.199 50.380  1.00 32.88 ? 661  GLU B CB    1 
ATOM   10795 C  CG    . GLU B 1 641 ? 4.578   -26.472 50.240  1.00 34.51 ? 661  GLU B CG    1 
ATOM   10796 C  CD    . GLU B 1 641 ? 5.118   -27.597 51.089  1.00 36.80 ? 661  GLU B CD    1 
ATOM   10797 O  OE1   . GLU B 1 641 ? 4.414   -27.993 52.040  1.00 39.09 ? 661  GLU B OE1   1 
ATOM   10798 O  OE2   . GLU B 1 641 ? 6.236   -28.083 50.804  1.00 37.43 ? 661  GLU B OE2   1 
ATOM   10799 N  N     . ASN B 1 642 ? 5.383   -21.736 50.114  1.00 32.17 ? 662  ASN B N     1 
ATOM   10800 C  CA    . ASN B 1 642 ? 6.292   -20.616 50.248  1.00 32.11 ? 662  ASN B CA    1 
ATOM   10801 C  C     . ASN B 1 642 ? 6.902   -20.211 48.900  1.00 31.48 ? 662  ASN B C     1 
ATOM   10802 O  O     . ASN B 1 642 ? 8.122   -20.228 48.706  1.00 31.67 ? 662  ASN B O     1 
ATOM   10803 C  CB    . ASN B 1 642 ? 7.378   -20.970 51.269  1.00 32.40 ? 662  ASN B CB    1 
ATOM   10804 C  CG    . ASN B 1 642 ? 8.053   -19.757 51.834  1.00 34.03 ? 662  ASN B CG    1 
ATOM   10805 O  OD1   . ASN B 1 642 ? 7.397   -18.880 52.405  1.00 37.52 ? 662  ASN B OD1   1 
ATOM   10806 N  ND2   . ASN B 1 642 ? 9.378   -19.693 51.689  1.00 36.14 ? 662  ASN B ND2   1 
ATOM   10807 N  N     . GLU B 1 643 ? 6.026   -19.862 47.965  1.00 30.45 ? 663  GLU B N     1 
ATOM   10808 C  CA    . GLU B 1 643 ? 6.423   -19.425 46.633  1.00 29.83 ? 663  GLU B CA    1 
ATOM   10809 C  C     . GLU B 1 643 ? 5.636   -18.198 46.243  1.00 28.81 ? 663  GLU B C     1 
ATOM   10810 O  O     . GLU B 1 643 ? 4.697   -17.801 46.944  1.00 28.50 ? 663  GLU B O     1 
ATOM   10811 C  CB    . GLU B 1 643 ? 6.156   -20.526 45.597  1.00 29.97 ? 663  GLU B CB    1 
ATOM   10812 C  CG    . GLU B 1 643 ? 6.952   -21.808 45.788  1.00 31.43 ? 663  GLU B CG    1 
ATOM   10813 C  CD    . GLU B 1 643 ? 8.463   -21.638 45.601  1.00 33.14 ? 663  GLU B CD    1 
ATOM   10814 O  OE1   . GLU B 1 643 ? 8.916   -20.557 45.168  1.00 33.27 ? 663  GLU B OE1   1 
ATOM   10815 O  OE2   . GLU B 1 643 ? 9.199   -22.607 45.888  1.00 35.61 ? 663  GLU B OE2   1 
ATOM   10816 N  N     . ASP B 1 644 ? 6.021   -17.605 45.117  1.00 27.73 ? 664  ASP B N     1 
ATOM   10817 C  CA    . ASP B 1 644 ? 5.223   -16.572 44.476  1.00 26.84 ? 664  ASP B CA    1 
ATOM   10818 C  C     . ASP B 1 644 ? 4.079   -17.314 43.776  1.00 26.03 ? 664  ASP B C     1 
ATOM   10819 O  O     . ASP B 1 644 ? 4.296   -18.004 42.782  1.00 26.08 ? 664  ASP B O     1 
ATOM   10820 C  CB    . ASP B 1 644 ? 6.072   -15.746 43.490  1.00 26.88 ? 664  ASP B CB    1 
ATOM   10821 C  CG    . ASP B 1 644 ? 5.320   -14.553 42.914  1.00 26.98 ? 664  ASP B CG    1 
ATOM   10822 O  OD1   . ASP B 1 644 ? 4.127   -14.392 43.226  1.00 26.99 ? 664  ASP B OD1   1 
ATOM   10823 O  OD2   . ASP B 1 644 ? 5.916   -13.765 42.145  1.00 27.87 ? 664  ASP B OD2   1 
ATOM   10824 N  N     . LEU B 1 645 ? 2.873   -17.201 44.328  1.00 25.01 ? 665  LEU B N     1 
ATOM   10825 C  CA    . LEU B 1 645 ? 1.712   -17.918 43.799  1.00 24.13 ? 665  LEU B CA    1 
ATOM   10826 C  C     . LEU B 1 645 ? 0.867   -17.002 42.927  1.00 23.38 ? 665  LEU B C     1 
ATOM   10827 O  O     . LEU B 1 645 ? 0.878   -15.784 43.097  1.00 23.21 ? 665  LEU B O     1 
ATOM   10828 C  CB    . LEU B 1 645 ? 0.855   -18.470 44.942  1.00 24.21 ? 665  LEU B CB    1 
ATOM   10829 C  CG    . LEU B 1 645 ? 1.581   -19.292 46.010  1.00 24.35 ? 665  LEU B CG    1 
ATOM   10830 C  CD1   . LEU B 1 645 ? 0.603   -19.806 47.054  1.00 23.63 ? 665  LEU B CD1   1 
ATOM   10831 C  CD2   . LEU B 1 645 ? 2.328   -20.449 45.364  1.00 24.20 ? 665  LEU B CD2   1 
ATOM   10832 N  N     . VAL B 1 646 ? 0.147   -17.599 41.985  1.00 22.78 ? 666  VAL B N     1 
ATOM   10833 C  CA    . VAL B 1 646 ? -0.812  -16.878 41.171  1.00 22.23 ? 666  VAL B CA    1 
ATOM   10834 C  C     . VAL B 1 646 ? -2.123  -17.664 41.180  1.00 21.83 ? 666  VAL B C     1 
ATOM   10835 O  O     . VAL B 1 646 ? -2.147  -18.833 40.786  1.00 21.79 ? 666  VAL B O     1 
ATOM   10836 C  CB    . VAL B 1 646 ? -0.316  -16.708 39.716  1.00 22.17 ? 666  VAL B CB    1 
ATOM   10837 C  CG1   . VAL B 1 646 ? -1.388  -16.012 38.865  1.00 22.30 ? 666  VAL B CG1   1 
ATOM   10838 C  CG2   . VAL B 1 646 ? 1.012   -15.914 39.671  1.00 21.83 ? 666  VAL B CG2   1 
ATOM   10839 N  N     . ALA B 1 647 ? -3.197  -17.035 41.652  1.00 21.36 ? 667  ALA B N     1 
ATOM   10840 C  CA    . ALA B 1 647 ? -4.532  -17.631 41.562  1.00 21.03 ? 667  ALA B CA    1 
ATOM   10841 C  C     . ALA B 1 647 ? -5.101  -17.270 40.208  1.00 20.69 ? 667  ALA B C     1 
ATOM   10842 O  O     . ALA B 1 647 ? -4.955  -16.145 39.747  1.00 21.15 ? 667  ALA B O     1 
ATOM   10843 C  CB    . ALA B 1 647 ? -5.452  -17.123 42.669  1.00 20.83 ? 667  ALA B CB    1 
ATOM   10844 N  N     . TRP B 1 648 ? -5.740  -18.239 39.574  1.00 20.72 ? 668  TRP B N     1 
ATOM   10845 C  CA    . TRP B 1 648 ? -6.424  -18.034 38.313  1.00 20.27 ? 668  TRP B CA    1 
ATOM   10846 C  C     . TRP B 1 648 ? -7.889  -18.402 38.522  1.00 19.63 ? 668  TRP B C     1 
ATOM   10847 O  O     . TRP B 1 648 ? -8.174  -19.513 38.947  1.00 19.94 ? 668  TRP B O     1 
ATOM   10848 C  CB    . TRP B 1 648 ? -5.840  -18.967 37.262  1.00 20.40 ? 668  TRP B CB    1 
ATOM   10849 C  CG    . TRP B 1 648 ? -4.399  -18.804 36.974  1.00 21.07 ? 668  TRP B CG    1 
ATOM   10850 C  CD1   . TRP B 1 648 ? -3.361  -19.421 37.613  1.00 22.18 ? 668  TRP B CD1   1 
ATOM   10851 C  CD2   . TRP B 1 648 ? -3.816  -18.022 35.923  1.00 22.14 ? 668  TRP B CD2   1 
ATOM   10852 N  NE1   . TRP B 1 648 ? -2.166  -19.054 37.033  1.00 22.45 ? 668  TRP B NE1   1 
ATOM   10853 C  CE2   . TRP B 1 648 ? -2.416  -18.204 35.992  1.00 22.07 ? 668  TRP B CE2   1 
ATOM   10854 C  CE3   . TRP B 1 648 ? -4.339  -17.193 34.925  1.00 22.68 ? 668  TRP B CE3   1 
ATOM   10855 C  CZ2   . TRP B 1 648 ? -1.532  -17.573 35.108  1.00 23.28 ? 668  TRP B CZ2   1 
ATOM   10856 C  CZ3   . TRP B 1 648 ? -3.457  -16.557 34.048  1.00 23.42 ? 668  TRP B CZ3   1 
ATOM   10857 C  CH2   . TRP B 1 648 ? -2.070  -16.755 34.144  1.00 22.87 ? 668  TRP B CH2   1 
ATOM   10858 N  N     . VAL B 1 649 ? -8.804  -17.486 38.204  1.00 19.05 ? 669  VAL B N     1 
ATOM   10859 C  CA    . VAL B 1 649 ? -10.226 -17.633 38.563  1.00 18.70 ? 669  VAL B CA    1 
ATOM   10860 C  C     . VAL B 1 649 ? -11.145 -17.613 37.340  1.00 18.52 ? 669  VAL B C     1 
ATOM   10861 O  O     . VAL B 1 649 ? -11.084 -16.686 36.536  1.00 18.33 ? 669  VAL B O     1 
ATOM   10862 C  CB    . VAL B 1 649 ? -10.658 -16.514 39.547  1.00 18.75 ? 669  VAL B CB    1 
ATOM   10863 C  CG1   . VAL B 1 649 ? -12.137 -16.623 39.907  1.00 18.62 ? 669  VAL B CG1   1 
ATOM   10864 C  CG2   . VAL B 1 649 ? -9.816  -16.573 40.804  1.00 17.45 ? 669  VAL B CG2   1 
ATOM   10865 N  N     . THR B 1 650 ? -11.966 -18.651 37.198  1.00 18.09 ? 670  THR B N     1 
ATOM   10866 C  CA    . THR B 1 650 ? -13.016 -18.701 36.183  1.00 17.95 ? 670  THR B CA    1 
ATOM   10867 C  C     . THR B 1 650 ? -14.377 -18.359 36.813  1.00 17.87 ? 670  THR B C     1 
ATOM   10868 O  O     . THR B 1 650 ? -14.761 -18.942 37.831  1.00 18.09 ? 670  THR B O     1 
ATOM   10869 C  CB    . THR B 1 650 ? -13.121 -20.102 35.534  1.00 18.00 ? 670  THR B CB    1 
ATOM   10870 O  OG1   . THR B 1 650 ? -11.873 -20.460 34.920  1.00 17.86 ? 670  THR B OG1   1 
ATOM   10871 C  CG2   . THR B 1 650 ? -14.210 -20.129 34.479  1.00 17.91 ? 670  THR B CG2   1 
ATOM   10872 N  N     . VAL B 1 651 ? -15.074 -17.393 36.227  1.00 17.42 ? 671  VAL B N     1 
ATOM   10873 C  CA    . VAL B 1 651 ? -16.440 -17.065 36.626  1.00 17.41 ? 671  VAL B CA    1 
ATOM   10874 C  C     . VAL B 1 651 ? -17.298 -16.987 35.378  1.00 17.74 ? 671  VAL B C     1 
ATOM   10875 O  O     . VAL B 1 651 ? -16.794 -16.731 34.274  1.00 16.77 ? 671  VAL B O     1 
ATOM   10876 C  CB    . VAL B 1 651 ? -16.531 -15.736 37.426  1.00 17.43 ? 671  VAL B CB    1 
ATOM   10877 C  CG1   . VAL B 1 651 ? -15.699 -15.822 38.682  1.00 17.23 ? 671  VAL B CG1   1 
ATOM   10878 C  CG2   . VAL B 1 651 ? -16.100 -14.526 36.588  1.00 16.93 ? 671  VAL B CG2   1 
ATOM   10879 N  N     . GLY B 1 652 ? -18.596 -17.225 35.539  1.00 18.08 ? 672  GLY B N     1 
ATOM   10880 C  CA    . GLY B 1 652 ? -19.489 -17.237 34.392  1.00 18.02 ? 672  GLY B CA    1 
ATOM   10881 C  C     . GLY B 1 652 ? -20.908 -17.650 34.719  1.00 18.53 ? 672  GLY B C     1 
ATOM   10882 O  O     . GLY B 1 652 ? -21.251 -17.868 35.873  1.00 18.78 ? 672  GLY B O     1 
ATOM   10883 N  N     . PHE B 1 653 ? -21.731 -17.757 33.684  1.00 18.51 ? 673  PHE B N     1 
ATOM   10884 C  CA    . PHE B 1 653 ? -23.108 -18.171 33.857  1.00 18.69 ? 673  PHE B CA    1 
ATOM   10885 C  C     . PHE B 1 653 ? -23.716 -18.634 32.552  1.00 18.69 ? 673  PHE B C     1 
ATOM   10886 O  O     . PHE B 1 653 ? -23.411 -18.113 31.462  1.00 18.69 ? 673  PHE B O     1 
ATOM   10887 C  CB    . PHE B 1 653 ? -23.952 -17.037 34.464  1.00 18.68 ? 673  PHE B CB    1 
ATOM   10888 C  CG    . PHE B 1 653 ? -23.983 -15.783 33.641  1.00 18.15 ? 673  PHE B CG    1 
ATOM   10889 C  CD1   . PHE B 1 653 ? -25.023 -15.548 32.747  1.00 17.83 ? 673  PHE B CD1   1 
ATOM   10890 C  CD2   . PHE B 1 653 ? -22.990 -14.817 33.781  1.00 18.73 ? 673  PHE B CD2   1 
ATOM   10891 C  CE1   . PHE B 1 653 ? -25.061 -14.391 31.987  1.00 18.00 ? 673  PHE B CE1   1 
ATOM   10892 C  CE2   . PHE B 1 653 ? -23.020 -13.651 33.031  1.00 17.67 ? 673  PHE B CE2   1 
ATOM   10893 C  CZ    . PHE B 1 653 ? -24.053 -13.435 32.129  1.00 19.39 ? 673  PHE B CZ    1 
ATOM   10894 N  N     . LEU B 1 654 ? -24.581 -19.629 32.672  1.00 18.75 ? 674  LEU B N     1 
ATOM   10895 C  CA    . LEU B 1 654 ? -25.415 -20.058 31.565  1.00 18.89 ? 674  LEU B CA    1 
ATOM   10896 C  C     . LEU B 1 654 ? -26.418 -18.956 31.284  1.00 18.44 ? 674  LEU B C     1 
ATOM   10897 O  O     . LEU B 1 654 ? -26.992 -18.401 32.196  1.00 19.04 ? 674  LEU B O     1 
ATOM   10898 C  CB    . LEU B 1 654 ? -26.128 -21.360 31.917  1.00 18.77 ? 674  LEU B CB    1 
ATOM   10899 C  CG    . LEU B 1 654 ? -27.074 -21.914 30.853  1.00 19.29 ? 674  LEU B CG    1 
ATOM   10900 C  CD1   . LEU B 1 654 ? -26.330 -22.189 29.540  1.00 18.47 ? 674  LEU B CD1   1 
ATOM   10901 C  CD2   . LEU B 1 654 ? -27.734 -23.161 31.383  1.00 17.78 ? 674  LEU B CD2   1 
ATOM   10902 N  N     . HIS B 1 655 ? -26.611 -18.622 30.018  1.00 18.03 ? 675  HIS B N     1 
ATOM   10903 C  CA    . HIS B 1 655 ? -27.635 -17.663 29.640  1.00 17.64 ? 675  HIS B CA    1 
ATOM   10904 C  C     . HIS B 1 655 ? -28.534 -18.351 28.624  1.00 17.72 ? 675  HIS B C     1 
ATOM   10905 O  O     . HIS B 1 655 ? -28.128 -18.605 27.499  1.00 17.11 ? 675  HIS B O     1 
ATOM   10906 C  CB    . HIS B 1 655 ? -26.975 -16.401 29.082  1.00 17.91 ? 675  HIS B CB    1 
ATOM   10907 C  CG    . HIS B 1 655 ? -27.929 -15.328 28.651  1.00 16.79 ? 675  HIS B CG    1 
ATOM   10908 N  ND1   . HIS B 1 655 ? -27.516 -14.229 27.930  1.00 16.01 ? 675  HIS B ND1   1 
ATOM   10909 C  CD2   . HIS B 1 655 ? -29.265 -15.186 28.820  1.00 16.20 ? 675  HIS B CD2   1 
ATOM   10910 C  CE1   . HIS B 1 655 ? -28.555 -13.452 27.680  1.00 16.91 ? 675  HIS B CE1   1 
ATOM   10911 N  NE2   . HIS B 1 655 ? -29.628 -14.008 28.216  1.00 16.72 ? 675  HIS B NE2   1 
ATOM   10912 N  N     . ILE B 1 656 ? -29.730 -18.729 29.064  1.00 17.77 ? 676  ILE B N     1 
ATOM   10913 C  CA    . ILE B 1 656 ? -30.763 -19.187 28.152  1.00 17.73 ? 676  ILE B CA    1 
ATOM   10914 C  C     . ILE B 1 656 ? -31.593 -17.943 27.878  1.00 17.63 ? 676  ILE B C     1 
ATOM   10915 O  O     . ILE B 1 656 ? -32.241 -17.436 28.784  1.00 17.58 ? 676  ILE B O     1 
ATOM   10916 C  CB    . ILE B 1 656 ? -31.628 -20.297 28.765  1.00 18.12 ? 676  ILE B CB    1 
ATOM   10917 C  CG1   . ILE B 1 656 ? -30.775 -21.542 29.068  1.00 17.79 ? 676  ILE B CG1   1 
ATOM   10918 C  CG2   . ILE B 1 656 ? -32.774 -20.679 27.811  1.00 17.87 ? 676  ILE B CG2   1 
ATOM   10919 C  CD1   . ILE B 1 656 ? -31.507 -22.635 29.839  1.00 16.14 ? 676  ILE B CD1   1 
ATOM   10920 N  N     . PRO B 1 657 ? -31.544 -17.412 26.641  1.00 17.43 ? 677  PRO B N     1 
ATOM   10921 C  CA    . PRO B 1 657 ? -32.260 -16.159 26.453  1.00 17.28 ? 677  PRO B CA    1 
ATOM   10922 C  C     . PRO B 1 657 ? -33.759 -16.260 26.659  1.00 17.23 ? 677  PRO B C     1 
ATOM   10923 O  O     . PRO B 1 657 ? -34.341 -17.341 26.515  1.00 17.33 ? 677  PRO B O     1 
ATOM   10924 C  CB    . PRO B 1 657 ? -31.911 -15.775 25.017  1.00 17.44 ? 677  PRO B CB    1 
ATOM   10925 C  CG    . PRO B 1 657 ? -30.534 -16.362 24.839  1.00 16.89 ? 677  PRO B CG    1 
ATOM   10926 C  CD    . PRO B 1 657 ? -30.654 -17.692 25.500  1.00 17.28 ? 677  PRO B CD    1 
ATOM   10927 N  N     . HIS B 1 658 ? -34.357 -15.128 27.036  1.00 16.90 ? 678  HIS B N     1 
ATOM   10928 C  CA    . HIS B 1 658 ? -35.787 -15.031 27.292  1.00 16.79 ? 678  HIS B CA    1 
ATOM   10929 C  C     . HIS B 1 658 ? -36.278 -13.699 26.724  1.00 16.42 ? 678  HIS B C     1 
ATOM   10930 O  O     . HIS B 1 658 ? -35.474 -12.848 26.371  1.00 16.35 ? 678  HIS B O     1 
ATOM   10931 C  CB    . HIS B 1 658 ? -36.113 -15.191 28.796  1.00 16.64 ? 678  HIS B CB    1 
ATOM   10932 C  CG    . HIS B 1 658 ? -35.201 -14.436 29.712  1.00 17.04 ? 678  HIS B CG    1 
ATOM   10933 N  ND1   . HIS B 1 658 ? -35.628 -13.376 30.482  1.00 18.07 ? 678  HIS B ND1   1 
ATOM   10934 C  CD2   . HIS B 1 658 ? -33.884 -14.601 30.000  1.00 19.31 ? 678  HIS B CD2   1 
ATOM   10935 C  CE1   . HIS B 1 658 ? -34.613 -12.910 31.192  1.00 19.22 ? 678  HIS B CE1   1 
ATOM   10936 N  NE2   . HIS B 1 658 ? -33.545 -13.641 30.926  1.00 18.72 ? 678  HIS B NE2   1 
ATOM   10937 N  N     . SER B 1 659 ? -37.592 -13.542 26.601  1.00 16.16 ? 679  SER B N     1 
ATOM   10938 C  CA    . SER B 1 659 ? -38.161 -12.397 25.892  1.00 16.38 ? 679  SER B CA    1 
ATOM   10939 C  C     . SER B 1 659 ? -37.792 -11.061 26.528  1.00 16.36 ? 679  SER B C     1 
ATOM   10940 O  O     . SER B 1 659 ? -37.678 -10.052 25.833  1.00 15.93 ? 679  SER B O     1 
ATOM   10941 C  CB    . SER B 1 659 ? -39.681 -12.526 25.748  1.00 16.17 ? 679  SER B CB    1 
ATOM   10942 O  OG    . SER B 1 659 ? -40.286 -12.886 26.968  1.00 15.52 ? 679  SER B OG    1 
ATOM   10943 N  N     . GLU B 1 660 ? -37.558 -11.051 27.831  1.00 16.68 ? 680  GLU B N     1 
ATOM   10944 C  CA    . GLU B 1 660 ? -37.144 -9.807  28.485  1.00 17.16 ? 680  GLU B CA    1 
ATOM   10945 C  C     . GLU B 1 660 ? -35.741 -9.333  28.044  1.00 17.63 ? 680  GLU B C     1 
ATOM   10946 O  O     . GLU B 1 660 ? -35.371 -8.183  28.340  1.00 17.98 ? 680  GLU B O     1 
ATOM   10947 C  CB    . GLU B 1 660 ? -37.213 -9.928  30.009  1.00 17.04 ? 680  GLU B CB    1 
ATOM   10948 C  CG    . GLU B 1 660 ? -38.635 -10.177 30.562  1.00 16.62 ? 680  GLU B CG    1 
ATOM   10949 C  CD    . GLU B 1 660 ? -39.069 -11.646 30.569  1.00 15.57 ? 680  GLU B CD    1 
ATOM   10950 O  OE1   . GLU B 1 660 ? -38.290 -12.526 30.129  1.00 14.58 ? 680  GLU B OE1   1 
ATOM   10951 O  OE2   . GLU B 1 660 ? -40.201 -11.918 31.031  1.00 13.24 ? 680  GLU B OE2   1 
ATOM   10952 N  N     . ASP B 1 661 ? -34.976 -10.188 27.349  1.00 17.71 ? 681  ASP B N     1 
ATOM   10953 C  CA    . ASP B 1 661 ? -33.672 -9.787  26.753  1.00 18.14 ? 681  ASP B CA    1 
ATOM   10954 C  C     . ASP B 1 661 ? -33.827 -8.871  25.529  1.00 18.02 ? 681  ASP B C     1 
ATOM   10955 O  O     . ASP B 1 661 ? -32.829 -8.425  24.964  1.00 17.81 ? 681  ASP B O     1 
ATOM   10956 C  CB    . ASP B 1 661 ? -32.841 -11.020 26.322  1.00 18.48 ? 681  ASP B CB    1 
ATOM   10957 C  CG    . ASP B 1 661 ? -32.203 -11.758 27.491  1.00 19.58 ? 681  ASP B CG    1 
ATOM   10958 O  OD1   . ASP B 1 661 ? -31.770 -11.101 28.467  1.00 19.84 ? 681  ASP B OD1   1 
ATOM   10959 O  OD2   . ASP B 1 661 ? -32.123 -13.005 27.423  1.00 20.73 ? 681  ASP B OD2   1 
ATOM   10960 N  N     . ILE B 1 662 ? -35.069 -8.607  25.116  1.00 17.71 ? 682  ILE B N     1 
ATOM   10961 C  CA    . ILE B 1 662 ? -35.354 -7.755  23.969  1.00 17.85 ? 682  ILE B CA    1 
ATOM   10962 C  C     . ILE B 1 662 ? -35.694 -6.332  24.421  1.00 17.95 ? 682  ILE B C     1 
ATOM   10963 O  O     . ILE B 1 662 ? -36.590 -6.156  25.260  1.00 18.11 ? 682  ILE B O     1 
ATOM   10964 C  CB    . ILE B 1 662 ? -36.542 -8.316  23.159  1.00 17.53 ? 682  ILE B CB    1 
ATOM   10965 C  CG1   . ILE B 1 662 ? -36.236 -9.730  22.650  1.00 18.28 ? 682  ILE B CG1   1 
ATOM   10966 C  CG2   . ILE B 1 662 ? -36.880 -7.397  21.988  1.00 18.27 ? 682  ILE B CG2   1 
ATOM   10967 C  CD1   . ILE B 1 662 ? -35.039 -9.817  21.713  1.00 19.14 ? 682  ILE B CD1   1 
ATOM   10968 N  N     . PRO B 1 663 ? -35.003 -5.301  23.870  1.00 17.92 ? 683  PRO B N     1 
ATOM   10969 C  CA    . PRO B 1 663 ? -33.942 -5.283  22.858  1.00 17.82 ? 683  PRO B CA    1 
ATOM   10970 C  C     . PRO B 1 663 ? -32.580 -5.667  23.382  1.00 17.98 ? 683  PRO B C     1 
ATOM   10971 O  O     . PRO B 1 663 ? -31.727 -6.099  22.595  1.00 18.15 ? 683  PRO B O     1 
ATOM   10972 C  CB    . PRO B 1 663 ? -33.896 -3.818  22.424  1.00 18.25 ? 683  PRO B CB    1 
ATOM   10973 C  CG    . PRO B 1 663 ? -34.313 -3.057  23.663  1.00 17.85 ? 683  PRO B CG    1 
ATOM   10974 C  CD    . PRO B 1 663 ? -35.377 -3.932  24.280  1.00 17.93 ? 683  PRO B CD    1 
ATOM   10975 N  N     . ASN B 1 664 ? -32.369 -5.504  24.687  1.00 17.74 ? 684  ASN B N     1 
ATOM   10976 C  CA    . ASN B 1 664 ? -31.083 -5.807  25.311  1.00 17.91 ? 684  ASN B CA    1 
ATOM   10977 C  C     . ASN B 1 664 ? -31.204 -6.652  26.580  1.00 18.05 ? 684  ASN B C     1 
ATOM   10978 O  O     . ASN B 1 664 ? -32.183 -6.525  27.330  1.00 18.12 ? 684  ASN B O     1 
ATOM   10979 C  CB    . ASN B 1 664 ? -30.401 -4.506  25.735  1.00 18.08 ? 684  ASN B CB    1 
ATOM   10980 C  CG    . ASN B 1 664 ? -29.642 -3.812  24.609  1.00 18.50 ? 684  ASN B CG    1 
ATOM   10981 O  OD1   . ASN B 1 664 ? -28.819 -2.946  24.894  1.00 21.14 ? 684  ASN B OD1   1 
ATOM   10982 N  ND2   . ASN B 1 664 ? -29.900 -4.178  23.348  1.00 17.27 ? 684  ASN B ND2   1 
ATOM   10983 N  N     A THR B 1 665 ? -30.205 -7.506  26.810  0.50 17.85 ? 685  THR B N     1 
ATOM   10984 N  N     B THR B 1 665 ? -30.213 -7.505  26.820  0.50 18.18 ? 685  THR B N     1 
ATOM   10985 C  CA    A THR B 1 665 ? -29.972 -8.114  28.117  0.50 17.80 ? 685  THR B CA    1 
ATOM   10986 C  CA    B THR B 1 665 ? -30.047 -8.130  28.120  0.50 18.46 ? 685  THR B CA    1 
ATOM   10987 C  C     A THR B 1 665 ? -29.751 -6.989  29.133  0.50 17.93 ? 685  THR B C     1 
ATOM   10988 C  C     B THR B 1 665 ? -29.744 -7.021  29.134  0.50 18.26 ? 685  THR B C     1 
ATOM   10989 O  O     A THR B 1 665 ? -29.069 -6.010  28.830  0.50 17.80 ? 685  THR B O     1 
ATOM   10990 O  O     B THR B 1 665 ? -29.002 -6.089  28.831  0.50 18.12 ? 685  THR B O     1 
ATOM   10991 C  CB    A THR B 1 665 ? -28.698 -9.002  28.106  0.50 18.09 ? 685  THR B CB    1 
ATOM   10992 C  CB    B THR B 1 665 ? -28.877 -9.129  28.111  0.50 18.86 ? 685  THR B CB    1 
ATOM   10993 O  OG1   A THR B 1 665 ? -28.872 -10.107 27.210  0.50 17.10 ? 685  THR B OG1   1 
ATOM   10994 O  OG1   B THR B 1 665 ? -27.641 -8.414  28.010  0.50 19.91 ? 685  THR B OG1   1 
ATOM   10995 C  CG2   A THR B 1 665 ? -28.375 -9.520  29.516  0.50 16.96 ? 685  THR B CG2   1 
ATOM   10996 C  CG2   B THR B 1 665 ? -28.993 -10.075 26.941  0.50 18.46 ? 685  THR B CG2   1 
ATOM   10997 N  N     . ALA B 1 666 ? -30.336 -7.124  30.321  1.00 18.00 ? 686  ALA B N     1 
ATOM   10998 C  CA    . ALA B 1 666 ? -30.183 -6.123  31.383  1.00 17.92 ? 686  ALA B CA    1 
ATOM   10999 C  C     . ALA B 1 666 ? -29.178 -6.623  32.437  1.00 18.40 ? 686  ALA B C     1 
ATOM   11000 O  O     . ALA B 1 666 ? -28.919 -7.828  32.536  1.00 17.58 ? 686  ALA B O     1 
ATOM   11001 C  CB    . ALA B 1 666 ? -31.540 -5.822  32.025  1.00 17.58 ? 686  ALA B CB    1 
ATOM   11002 N  N     . THR B 1 667 ? -28.620 -5.692  33.219  1.00 19.14 ? 687  THR B N     1 
ATOM   11003 C  CA    . THR B 1 667 ? -27.589 -6.030  34.210  1.00 19.40 ? 687  THR B CA    1 
ATOM   11004 C  C     . THR B 1 667 ? -28.071 -6.655  35.527  1.00 20.04 ? 687  THR B C     1 
ATOM   11005 O  O     . THR B 1 667 ? -27.285 -7.352  36.169  1.00 19.41 ? 687  THR B O     1 
ATOM   11006 C  CB    . THR B 1 667 ? -26.738 -4.819  34.591  1.00 19.45 ? 687  THR B CB    1 
ATOM   11007 O  OG1   . THR B 1 667 ? -27.583 -3.785  35.104  1.00 18.58 ? 687  THR B OG1   1 
ATOM   11008 C  CG2   . THR B 1 667 ? -25.929 -4.310  33.370  1.00 19.69 ? 687  THR B CG2   1 
ATOM   11009 N  N     . PRO B 1 668 ? -29.330 -6.391  35.953  1.00 20.77 ? 688  PRO B N     1 
ATOM   11010 C  CA    . PRO B 1 668 ? -29.710 -6.965  37.247  1.00 21.42 ? 688  PRO B CA    1 
ATOM   11011 C  C     . PRO B 1 668 ? -29.618 -8.482  37.237  1.00 21.82 ? 688  PRO B C     1 
ATOM   11012 O  O     . PRO B 1 668 ? -30.174 -9.128  36.353  1.00 22.18 ? 688  PRO B O     1 
ATOM   11013 C  CB    . PRO B 1 668 ? -31.157 -6.485  37.449  1.00 21.42 ? 688  PRO B CB    1 
ATOM   11014 C  CG    . PRO B 1 668 ? -31.240 -5.229  36.670  1.00 21.34 ? 688  PRO B CG    1 
ATOM   11015 C  CD    . PRO B 1 668 ? -30.356 -5.456  35.456  1.00 20.87 ? 688  PRO B CD    1 
ATOM   11016 N  N     . GLY B 1 669 ? -28.865 -9.020  38.194  1.00 22.58 ? 689  GLY B N     1 
ATOM   11017 C  CA    . GLY B 1 669 ? -28.584 -10.447 38.285  1.00 22.94 ? 689  GLY B CA    1 
ATOM   11018 C  C     . GLY B 1 669 ? -27.693 -11.029 37.198  1.00 23.46 ? 689  GLY B C     1 
ATOM   11019 O  O     . GLY B 1 669 ? -27.493 -12.240 37.162  1.00 23.90 ? 689  GLY B O     1 
ATOM   11020 N  N     . ASN B 1 670 ? -27.167 -10.203 36.299  1.00 23.32 ? 690  ASN B N     1 
ATOM   11021 C  CA    . ASN B 1 670 ? -26.332 -10.711 35.215  1.00 23.48 ? 690  ASN B CA    1 
ATOM   11022 C  C     . ASN B 1 670 ? -24.895 -10.274 35.426  1.00 22.95 ? 690  ASN B C     1 
ATOM   11023 O  O     . ASN B 1 670 ? -24.294 -9.666  34.556  1.00 22.72 ? 690  ASN B O     1 
ATOM   11024 C  CB    . ASN B 1 670 ? -26.848 -10.237 33.846  1.00 24.00 ? 690  ASN B CB    1 
ATOM   11025 C  CG    . ASN B 1 670 ? -27.957 -11.111 33.311  1.00 25.17 ? 690  ASN B CG    1 
ATOM   11026 O  OD1   . ASN B 1 670 ? -27.944 -12.318 33.514  1.00 27.02 ? 690  ASN B OD1   1 
ATOM   11027 N  ND2   . ASN B 1 670 ? -28.936 -10.506 32.625  1.00 26.58 ? 690  ASN B ND2   1 
ATOM   11028 N  N     . SER B 1 671 ? -24.360 -10.582 36.602  1.00 22.57 ? 691  SER B N     1 
ATOM   11029 C  CA    . SER B 1 671 ? -22.985 -10.259 36.913  1.00 22.34 ? 691  SER B CA    1 
ATOM   11030 C  C     . SER B 1 671 ? -22.314 -11.367 37.701  1.00 21.59 ? 691  SER B C     1 
ATOM   11031 O  O     . SER B 1 671 ? -22.954 -12.096 38.455  1.00 21.01 ? 691  SER B O     1 
ATOM   11032 C  CB    . SER B 1 671 ? -22.879 -8.927  37.662  1.00 22.41 ? 691  SER B CB    1 
ATOM   11033 O  OG    . SER B 1 671 ? -23.272 -9.049  39.011  1.00 24.88 ? 691  SER B OG    1 
ATOM   11034 N  N     . VAL B 1 672 ? -21.009 -11.477 37.493  1.00 21.03 ? 692  VAL B N     1 
ATOM   11035 C  CA    . VAL B 1 672 ? -20.169 -12.427 38.196  1.00 20.72 ? 692  VAL B CA    1 
ATOM   11036 C  C     . VAL B 1 672 ? -18.873 -11.747 38.600  1.00 20.70 ? 692  VAL B C     1 
ATOM   11037 O  O     . VAL B 1 672 ? -18.551 -10.640 38.126  1.00 20.49 ? 692  VAL B O     1 
ATOM   11038 C  CB    . VAL B 1 672 ? -19.838 -13.634 37.307  1.00 20.98 ? 692  VAL B CB    1 
ATOM   11039 C  CG1   . VAL B 1 672 ? -21.054 -14.576 37.226  1.00 21.42 ? 692  VAL B CG1   1 
ATOM   11040 C  CG2   . VAL B 1 672 ? -19.378 -13.173 35.915  1.00 19.93 ? 692  VAL B CG2   1 
ATOM   11041 N  N     . GLY B 1 673 ? -18.126 -12.411 39.468  1.00 20.11 ? 693  GLY B N     1 
ATOM   11042 C  CA    . GLY B 1 673 ? -16.846 -11.889 39.894  1.00 20.04 ? 693  GLY B CA    1 
ATOM   11043 C  C     . GLY B 1 673 ? -16.330 -12.616 41.099  1.00 19.97 ? 693  GLY B C     1 
ATOM   11044 O  O     . GLY B 1 673 ? -16.643 -13.789 41.320  1.00 19.99 ? 693  GLY B O     1 
ATOM   11045 N  N     . PHE B 1 674 ? -15.525 -11.911 41.878  1.00 20.44 ? 694  PHE B N     1 
ATOM   11046 C  CA    . PHE B 1 674 ? -14.979 -12.455 43.114  1.00 20.60 ? 694  PHE B CA    1 
ATOM   11047 C  C     . PHE B 1 674 ? -14.610 -11.326 44.058  1.00 20.99 ? 694  PHE B C     1 
ATOM   11048 O  O     . PHE B 1 674 ? -14.482 -10.173 43.640  1.00 20.56 ? 694  PHE B O     1 
ATOM   11049 C  CB    . PHE B 1 674 ? -13.765 -13.352 42.824  1.00 20.83 ? 694  PHE B CB    1 
ATOM   11050 C  CG    . PHE B 1 674 ? -12.638 -12.650 42.101  1.00 21.24 ? 694  PHE B CG    1 
ATOM   11051 C  CD1   . PHE B 1 674 ? -11.575 -12.104 42.806  1.00 21.83 ? 694  PHE B CD1   1 
ATOM   11052 C  CD2   . PHE B 1 674 ? -12.641 -12.537 40.726  1.00 22.06 ? 694  PHE B CD2   1 
ATOM   11053 C  CE1   . PHE B 1 674 ? -10.528 -11.445 42.149  1.00 21.48 ? 694  PHE B CE1   1 
ATOM   11054 C  CE2   . PHE B 1 674 ? -11.591 -11.876 40.058  1.00 23.00 ? 694  PHE B CE2   1 
ATOM   11055 C  CZ    . PHE B 1 674 ? -10.537 -11.336 40.778  1.00 22.04 ? 694  PHE B CZ    1 
ATOM   11056 N  N     . LEU B 1 675 ? -14.481 -11.666 45.337  1.00 21.92 ? 695  LEU B N     1 
ATOM   11057 C  CA    . LEU B 1 675 ? -13.997 -10.741 46.349  1.00 22.76 ? 695  LEU B CA    1 
ATOM   11058 C  C     . LEU B 1 675 ? -12.662 -11.225 46.880  1.00 22.88 ? 695  LEU B C     1 
ATOM   11059 O  O     . LEU B 1 675 ? -12.379 -12.414 46.875  1.00 23.21 ? 695  LEU B O     1 
ATOM   11060 C  CB    . LEU B 1 675 ? -14.983 -10.627 47.518  1.00 23.39 ? 695  LEU B CB    1 
ATOM   11061 C  CG    . LEU B 1 675 ? -16.182 -9.705  47.323  1.00 24.24 ? 695  LEU B CG    1 
ATOM   11062 C  CD1   . LEU B 1 675 ? -17.040 -10.256 46.224  1.00 27.06 ? 695  LEU B CD1   1 
ATOM   11063 C  CD2   . LEU B 1 675 ? -16.969 -9.592  48.606  1.00 26.04 ? 695  LEU B CD2   1 
ATOM   11064 N  N     . LEU B 1 676 ? -11.848 -10.274 47.322  1.00 23.07 ? 696  LEU B N     1 
ATOM   11065 C  CA    . LEU B 1 676 ? -10.633 -10.554 48.059  1.00 23.09 ? 696  LEU B CA    1 
ATOM   11066 C  C     . LEU B 1 676 ? -10.778 -9.865  49.418  1.00 23.25 ? 696  LEU B C     1 
ATOM   11067 O  O     . LEU B 1 676 ? -10.886 -8.644  49.487  1.00 23.91 ? 696  LEU B O     1 
ATOM   11068 C  CB    . LEU B 1 676 ? -9.416  -10.024 47.315  1.00 22.70 ? 696  LEU B CB    1 
ATOM   11069 C  CG    . LEU B 1 676 ? -9.168  -10.565 45.908  1.00 22.09 ? 696  LEU B CG    1 
ATOM   11070 C  CD1   . LEU B 1 676 ? -8.065  -9.750  45.227  1.00 21.97 ? 696  LEU B CD1   1 
ATOM   11071 C  CD2   . LEU B 1 676 ? -8.824  -12.044 45.921  1.00 21.43 ? 696  LEU B CD2   1 
ATOM   11072 N  N     . ARG B 1 677 ? -10.801 -10.653 50.481  1.00 23.12 ? 697  ARG B N     1 
ATOM   11073 C  CA    . ARG B 1 677 ? -11.115 -10.164 51.814  1.00 23.74 ? 697  ARG B CA    1 
ATOM   11074 C  C     . ARG B 1 677 ? -9.934  -10.391 52.740  1.00 23.73 ? 697  ARG B C     1 
ATOM   11075 O  O     . ARG B 1 677 ? -9.364  -11.486 52.739  1.00 23.74 ? 697  ARG B O     1 
ATOM   11076 C  CB    . ARG B 1 677 ? -12.312 -10.930 52.390  1.00 23.81 ? 697  ARG B CB    1 
ATOM   11077 C  CG    . ARG B 1 677 ? -13.546 -10.906 51.482  1.00 25.05 ? 697  ARG B CG    1 
ATOM   11078 C  CD    . ARG B 1 677 ? -14.673 -11.799 51.995  1.00 25.27 ? 697  ARG B CD    1 
ATOM   11079 N  NE    . ARG B 1 677 ? -15.063 -11.455 53.354  1.00 25.86 ? 697  ARG B NE    1 
ATOM   11080 C  CZ    . ARG B 1 677 ? -16.204 -11.823 53.929  1.00 27.73 ? 697  ARG B CZ    1 
ATOM   11081 N  NH1   . ARG B 1 677 ? -17.115 -12.535 53.267  1.00 28.50 ? 697  ARG B NH1   1 
ATOM   11082 N  NH2   . ARG B 1 677 ? -16.440 -11.459 55.178  1.00 28.09 ? 697  ARG B NH2   1 
ATOM   11083 N  N     . PRO B 1 678 ? -9.584  -9.377  53.551  1.00 23.72 ? 698  PRO B N     1 
ATOM   11084 C  CA    . PRO B 1 678 ? -8.582  -9.575  54.598  1.00 23.72 ? 698  PRO B CA    1 
ATOM   11085 C  C     . PRO B 1 678 ? -9.022  -10.660 55.583  1.00 23.29 ? 698  PRO B C     1 
ATOM   11086 O  O     . PRO B 1 678 ? -10.158 -10.618 56.071  1.00 22.97 ? 698  PRO B O     1 
ATOM   11087 C  CB    . PRO B 1 678 ? -8.528  -8.221  55.317  1.00 23.56 ? 698  PRO B CB    1 
ATOM   11088 C  CG    . PRO B 1 678 ? -9.240  -7.281  54.501  1.00 24.22 ? 698  PRO B CG    1 
ATOM   11089 C  CD    . PRO B 1 678 ? -10.136 -8.013  53.563  1.00 23.77 ? 698  PRO B CD    1 
ATOM   11090 N  N     . PHE B 1 679 ? -8.142  -11.625 55.845  1.00 22.71 ? 699  PHE B N     1 
ATOM   11091 C  CA    . PHE B 1 679 ? -8.424  -12.681 56.814  1.00 22.82 ? 699  PHE B CA    1 
ATOM   11092 C  C     . PHE B 1 679 ? -7.239  -12.843 57.779  1.00 23.19 ? 699  PHE B C     1 
ATOM   11093 O  O     . PHE B 1 679 ? -6.253  -13.512 57.462  1.00 22.96 ? 699  PHE B O     1 
ATOM   11094 C  CB    . PHE B 1 679 ? -8.725  -13.990 56.101  1.00 22.41 ? 699  PHE B CB    1 
ATOM   11095 C  CG    . PHE B 1 679 ? -9.179  -15.091 57.018  1.00 21.95 ? 699  PHE B CG    1 
ATOM   11096 C  CD1   . PHE B 1 679 ? -10.518 -15.215 57.361  1.00 21.72 ? 699  PHE B CD1   1 
ATOM   11097 C  CD2   . PHE B 1 679 ? -8.274  -16.007 57.523  1.00 21.01 ? 699  PHE B CD2   1 
ATOM   11098 C  CE1   . PHE B 1 679 ? -10.947 -16.225 58.198  1.00 21.10 ? 699  PHE B CE1   1 
ATOM   11099 C  CE2   . PHE B 1 679 ? -8.688  -17.017 58.368  1.00 21.44 ? 699  PHE B CE2   1 
ATOM   11100 C  CZ    . PHE B 1 679 ? -10.040 -17.130 58.703  1.00 20.97 ? 699  PHE B CZ    1 
ATOM   11101 N  N     . ASN B 1 680 ? -7.365  -12.212 58.947  1.00 23.47 ? 700  ASN B N     1 
ATOM   11102 C  CA    . ASN B 1 680 ? -6.310  -12.143 59.978  1.00 23.42 ? 700  ASN B CA    1 
ATOM   11103 C  C     . ASN B 1 680 ? -5.083  -11.374 59.501  1.00 23.87 ? 700  ASN B C     1 
ATOM   11104 O  O     . ASN B 1 680 ? -3.984  -11.553 60.032  1.00 23.63 ? 700  ASN B O     1 
ATOM   11105 C  CB    . ASN B 1 680 ? -5.918  -13.531 60.487  1.00 23.30 ? 700  ASN B CB    1 
ATOM   11106 C  CG    . ASN B 1 680 ? -7.050  -14.228 61.203  1.00 22.98 ? 700  ASN B CG    1 
ATOM   11107 O  OD1   . ASN B 1 680 ? -7.785  -13.615 61.994  1.00 22.31 ? 700  ASN B OD1   1 
ATOM   11108 N  ND2   . ASN B 1 680 ? -7.206  -15.517 60.929  1.00 21.11 ? 700  ASN B ND2   1 
ATOM   11109 N  N     . PHE B 1 681 ? -5.297  -10.505 58.514  1.00 24.12 ? 701  PHE B N     1 
ATOM   11110 C  CA    . PHE B 1 681 ? -4.235  -9.718  57.917  1.00 24.71 ? 701  PHE B CA    1 
ATOM   11111 C  C     . PHE B 1 681 ? -3.962  -8.486  58.770  1.00 24.87 ? 701  PHE B C     1 
ATOM   11112 O  O     . PHE B 1 681 ? -2.808  -8.123  58.988  1.00 24.49 ? 701  PHE B O     1 
ATOM   11113 C  CB    . PHE B 1 681 ? -4.625  -9.299  56.504  1.00 24.72 ? 701  PHE B CB    1 
ATOM   11114 C  CG    . PHE B 1 681 ? -3.502  -8.696  55.717  1.00 25.37 ? 701  PHE B CG    1 
ATOM   11115 C  CD1   . PHE B 1 681 ? -3.281  -7.334  55.737  1.00 25.65 ? 701  PHE B CD1   1 
ATOM   11116 C  CD2   . PHE B 1 681 ? -2.679  -9.494  54.939  1.00 26.66 ? 701  PHE B CD2   1 
ATOM   11117 C  CE1   . PHE B 1 681 ? -2.252  -6.772  55.011  1.00 27.09 ? 701  PHE B CE1   1 
ATOM   11118 C  CE2   . PHE B 1 681 ? -1.642  -8.937  54.205  1.00 27.67 ? 701  PHE B CE2   1 
ATOM   11119 C  CZ    . PHE B 1 681 ? -1.429  -7.577  54.239  1.00 27.24 ? 701  PHE B CZ    1 
ATOM   11120 N  N     . PHE B 1 682 ? -5.037  -7.846  59.225  1.00 25.04 ? 702  PHE B N     1 
ATOM   11121 C  CA    . PHE B 1 682 ? -4.951  -6.667  60.076  1.00 25.62 ? 702  PHE B CA    1 
ATOM   11122 C  C     . PHE B 1 682 ? -5.283  -7.044  61.518  1.00 25.57 ? 702  PHE B C     1 
ATOM   11123 O  O     . PHE B 1 682 ? -6.038  -7.984  61.740  1.00 26.00 ? 702  PHE B O     1 
ATOM   11124 C  CB    . PHE B 1 682 ? -5.909  -5.585  59.580  1.00 25.61 ? 702  PHE B CB    1 
ATOM   11125 C  CG    . PHE B 1 682 ? -5.660  -5.165  58.161  1.00 26.27 ? 702  PHE B CG    1 
ATOM   11126 C  CD1   . PHE B 1 682 ? -4.608  -4.320  57.850  1.00 26.36 ? 702  PHE B CD1   1 
ATOM   11127 C  CD2   . PHE B 1 682 ? -6.475  -5.620  57.132  1.00 26.39 ? 702  PHE B CD2   1 
ATOM   11128 C  CE1   . PHE B 1 682 ? -4.374  -3.928  56.541  1.00 27.19 ? 702  PHE B CE1   1 
ATOM   11129 C  CE2   . PHE B 1 682 ? -6.246  -5.230  55.817  1.00 26.39 ? 702  PHE B CE2   1 
ATOM   11130 C  CZ    . PHE B 1 682 ? -5.197  -4.385  55.521  1.00 27.04 ? 702  PHE B CZ    1 
ATOM   11131 N  N     . PRO B 1 683 ? -4.720  -6.319  62.500  1.00 25.63 ? 703  PRO B N     1 
ATOM   11132 C  CA    . PRO B 1 683 ? -4.979  -6.619  63.914  1.00 25.63 ? 703  PRO B CA    1 
ATOM   11133 C  C     . PRO B 1 683 ? -6.455  -6.488  64.309  1.00 25.46 ? 703  PRO B C     1 
ATOM   11134 O  O     . PRO B 1 683 ? -6.917  -7.211  65.178  1.00 25.24 ? 703  PRO B O     1 
ATOM   11135 C  CB    . PRO B 1 683 ? -4.145  -5.566  64.662  1.00 25.51 ? 703  PRO B CB    1 
ATOM   11136 C  CG    . PRO B 1 683 ? -3.157  -5.084  63.696  1.00 25.80 ? 703  PRO B CG    1 
ATOM   11137 C  CD    . PRO B 1 683 ? -3.805  -5.173  62.354  1.00 25.61 ? 703  PRO B CD    1 
ATOM   11138 N  N     . GLU B 1 684 ? -7.164  -5.558  63.673  1.00 25.36 ? 704  GLU B N     1 
ATOM   11139 C  CA    . GLU B 1 684 ? -8.594  -5.353  63.894  1.00 25.28 ? 704  GLU B CA    1 
ATOM   11140 C  C     . GLU B 1 684 ? -9.179  -4.748  62.612  1.00 24.99 ? 704  GLU B C     1 
ATOM   11141 O  O     . GLU B 1 684 ? -8.465  -4.611  61.624  1.00 24.79 ? 704  GLU B O     1 
ATOM   11142 C  CB    . GLU B 1 684 ? -8.822  -4.447  65.106  1.00 25.47 ? 704  GLU B CB    1 
ATOM   11143 C  CG    . GLU B 1 684 ? -7.904  -3.235  65.140  1.00 26.46 ? 704  GLU B CG    1 
ATOM   11144 C  CD    . GLU B 1 684 ? -8.189  -2.290  66.280  1.00 26.53 ? 704  GLU B CD    1 
ATOM   11145 O  OE1   . GLU B 1 684 ? -8.761  -2.711  67.307  1.00 28.19 ? 704  GLU B OE1   1 
ATOM   11146 O  OE2   . GLU B 1 684 ? -7.834  -1.110  66.144  1.00 26.31 ? 704  GLU B OE2   1 
ATOM   11147 N  N     . ASP B 1 685 ? -10.468 -4.418  62.613  1.00 24.62 ? 705  ASP B N     1 
ATOM   11148 C  CA    . ASP B 1 685 ? -11.130 -3.820  61.441  1.00 24.51 ? 705  ASP B CA    1 
ATOM   11149 C  C     . ASP B 1 685 ? -10.319 -2.650  60.856  1.00 24.34 ? 705  ASP B C     1 
ATOM   11150 O  O     . ASP B 1 685 ? -10.214 -1.609  61.488  1.00 24.42 ? 705  ASP B O     1 
ATOM   11151 C  CB    . ASP B 1 685 ? -12.534 -3.346  61.848  1.00 24.27 ? 705  ASP B CB    1 
ATOM   11152 C  CG    . ASP B 1 685 ? -13.303 -2.664  60.718  1.00 24.42 ? 705  ASP B CG    1 
ATOM   11153 O  OD1   . ASP B 1 685 ? -12.822 -2.606  59.567  1.00 23.18 ? 705  ASP B OD1   1 
ATOM   11154 O  OD2   . ASP B 1 685 ? -14.424 -2.172  60.998  1.00 25.01 ? 705  ASP B OD2   1 
ATOM   11155 N  N     . PRO B 1 686 ? -9.768  -2.805  59.635  1.00 24.49 ? 706  PRO B N     1 
ATOM   11156 C  CA    . PRO B 1 686 ? -8.948  -1.717  59.055  1.00 24.71 ? 706  PRO B CA    1 
ATOM   11157 C  C     . PRO B 1 686 ? -9.708  -0.430  58.709  1.00 24.65 ? 706  PRO B C     1 
ATOM   11158 O  O     . PRO B 1 686 ? -9.075  0.602   58.516  1.00 24.74 ? 706  PRO B O     1 
ATOM   11159 C  CB    . PRO B 1 686 ? -8.343  -2.353  57.794  1.00 24.69 ? 706  PRO B CB    1 
ATOM   11160 C  CG    . PRO B 1 686 ? -9.227  -3.481  57.468  1.00 24.68 ? 706  PRO B CG    1 
ATOM   11161 C  CD    . PRO B 1 686 ? -9.827  -3.978  58.745  1.00 24.59 ? 706  PRO B CD    1 
ATOM   11162 N  N     . SER B 1 687 ? -11.043 -0.483  58.658  1.00 24.69 ? 707  SER B N     1 
ATOM   11163 C  CA    . SER B 1 687 ? -11.870 0.722   58.469  1.00 24.54 ? 707  SER B CA    1 
ATOM   11164 C  C     . SER B 1 687 ? -11.986 1.595   59.722  1.00 24.78 ? 707  SER B C     1 
ATOM   11165 O  O     . SER B 1 687 ? -12.633 2.639   59.687  1.00 24.34 ? 707  SER B O     1 
ATOM   11166 C  CB    . SER B 1 687 ? -13.291 0.356   57.998  1.00 24.72 ? 707  SER B CB    1 
ATOM   11167 O  OG    . SER B 1 687 ? -14.098 -0.142  59.057  1.00 23.04 ? 707  SER B OG    1 
ATOM   11168 N  N     . LEU B 1 688 ? -11.378 1.182   60.831  1.00 25.07 ? 708  LEU B N     1 
ATOM   11169 C  CA    . LEU B 1 688 ? -11.425 1.989   62.055  1.00 25.13 ? 708  LEU B CA    1 
ATOM   11170 C  C     . LEU B 1 688 ? -10.675 3.318   61.923  1.00 25.58 ? 708  LEU B C     1 
ATOM   11171 O  O     . LEU B 1 688 ? -10.908 4.237   62.696  1.00 25.49 ? 708  LEU B O     1 
ATOM   11172 C  CB    . LEU B 1 688 ? -10.898 1.195   63.246  1.00 25.24 ? 708  LEU B CB    1 
ATOM   11173 C  CG    . LEU B 1 688 ? -11.792 0.039   63.713  1.00 24.67 ? 708  LEU B CG    1 
ATOM   11174 C  CD1   . LEU B 1 688 ? -11.024 -0.875  64.641  1.00 23.40 ? 708  LEU B CD1   1 
ATOM   11175 C  CD2   . LEU B 1 688 ? -13.066 0.560   64.378  1.00 23.11 ? 708  LEU B CD2   1 
ATOM   11176 N  N     . ALA B 1 689 ? -9.794  3.431   60.932  1.00 25.95 ? 709  ALA B N     1 
ATOM   11177 C  CA    . ALA B 1 689 ? -9.147  4.711   60.636  1.00 26.28 ? 709  ALA B CA    1 
ATOM   11178 C  C     . ALA B 1 689 ? -10.104 5.762   60.030  1.00 26.63 ? 709  ALA B C     1 
ATOM   11179 O  O     . ALA B 1 689 ? -9.809  6.961   60.071  1.00 27.09 ? 709  ALA B O     1 
ATOM   11180 C  CB    . ALA B 1 689 ? -7.931  4.492   59.720  1.00 26.19 ? 709  ALA B CB    1 
ATOM   11181 N  N     . SER B 1 690 ? -11.237 5.333   59.468  1.00 26.86 ? 710  SER B N     1 
ATOM   11182 C  CA    . SER B 1 690 ? -12.171 6.267   58.836  1.00 26.76 ? 710  SER B CA    1 
ATOM   11183 C  C     . SER B 1 690 ? -12.754 7.247   59.838  1.00 27.15 ? 710  SER B C     1 
ATOM   11184 O  O     . SER B 1 690 ? -13.221 6.861   60.912  1.00 27.52 ? 710  SER B O     1 
ATOM   11185 C  CB    . SER B 1 690 ? -13.318 5.533   58.134  1.00 26.84 ? 710  SER B CB    1 
ATOM   11186 O  OG    . SER B 1 690 ? -14.299 6.453   57.660  1.00 25.61 ? 710  SER B OG    1 
ATOM   11187 N  N     . ARG B 1 691 ? -12.751 8.519   59.471  1.00 27.47 ? 711  ARG B N     1 
ATOM   11188 C  CA    . ARG B 1 691 ? -13.292 9.556   60.349  1.00 27.97 ? 711  ARG B CA    1 
ATOM   11189 C  C     . ARG B 1 691 ? -14.774 9.835   60.065  1.00 27.64 ? 711  ARG B C     1 
ATOM   11190 O  O     . ARG B 1 691 ? -15.349 10.737  60.659  1.00 28.07 ? 711  ARG B O     1 
ATOM   11191 C  CB    . ARG B 1 691 ? -12.440 10.833  60.261  1.00 28.22 ? 711  ARG B CB    1 
ATOM   11192 C  CG    . ARG B 1 691 ? -11.000 10.689  60.833  1.00 30.15 ? 711  ARG B CG    1 
ATOM   11193 C  CD    . ARG B 1 691 ? -10.984 9.864   62.125  1.00 32.61 ? 711  ARG B CD    1 
ATOM   11194 N  NE    . ARG B 1 691 ? -9.770  10.019  62.929  1.00 34.73 ? 711  ARG B NE    1 
ATOM   11195 C  CZ    . ARG B 1 691 ? -8.686  9.245   62.867  1.00 35.69 ? 711  ARG B CZ    1 
ATOM   11196 N  NH1   . ARG B 1 691 ? -8.602  8.225   62.016  1.00 36.62 ? 711  ARG B NH1   1 
ATOM   11197 N  NH2   . ARG B 1 691 ? -7.663  9.501   63.671  1.00 36.63 ? 711  ARG B NH2   1 
ATOM   11198 N  N     . ASP B 1 692 ? -15.389 9.018   59.207  1.00 27.35 ? 712  ASP B N     1 
ATOM   11199 C  CA    . ASP B 1 692 ? -16.810 9.136   58.874  1.00 27.37 ? 712  ASP B CA    1 
ATOM   11200 C  C     . ASP B 1 692 ? -17.729 8.496   59.918  1.00 26.63 ? 712  ASP B C     1 
ATOM   11201 O  O     . ASP B 1 692 ? -18.928 8.784   59.946  1.00 26.30 ? 712  ASP B O     1 
ATOM   11202 C  CB    . ASP B 1 692 ? -17.083 8.493   57.513  1.00 27.70 ? 712  ASP B CB    1 
ATOM   11203 C  CG    . ASP B 1 692 ? -16.504 9.286   56.366  1.00 29.75 ? 712  ASP B CG    1 
ATOM   11204 O  OD1   . ASP B 1 692 ? -16.353 10.518  56.499  1.00 32.96 ? 712  ASP B OD1   1 
ATOM   11205 O  OD2   . ASP B 1 692 ? -16.208 8.679   55.317  1.00 32.55 ? 712  ASP B OD2   1 
ATOM   11206 N  N     . THR B 1 693 ? -17.167 7.632   60.764  1.00 26.05 ? 713  THR B N     1 
ATOM   11207 C  CA    . THR B 1 693 ? -17.939 6.920   61.787  1.00 25.52 ? 713  THR B CA    1 
ATOM   11208 C  C     . THR B 1 693 ? -18.700 7.905   62.650  1.00 25.12 ? 713  THR B C     1 
ATOM   11209 O  O     . THR B 1 693 ? -18.184 8.962   62.992  1.00 25.09 ? 713  THR B O     1 
ATOM   11210 C  CB    . THR B 1 693 ? -17.026 6.062   62.692  1.00 25.62 ? 713  THR B CB    1 
ATOM   11211 O  OG1   . THR B 1 693 ? -16.334 5.101   61.892  1.00 24.64 ? 713  THR B OG1   1 
ATOM   11212 C  CG2   . THR B 1 693 ? -17.832 5.334   63.778  1.00 25.11 ? 713  THR B CG2   1 
ATOM   11213 N  N     . VAL B 1 694 ? -19.938 7.557   62.977  1.00 24.56 ? 714  VAL B N     1 
ATOM   11214 C  CA    . VAL B 1 694 ? -20.768 8.367   63.856  1.00 24.03 ? 714  VAL B CA    1 
ATOM   11215 C  C     . VAL B 1 694 ? -21.194 7.499   65.038  1.00 23.93 ? 714  VAL B C     1 
ATOM   11216 O  O     . VAL B 1 694 ? -21.600 6.360   64.849  1.00 23.05 ? 714  VAL B O     1 
ATOM   11217 C  CB    . VAL B 1 694 ? -22.003 8.890   63.094  1.00 24.20 ? 714  VAL B CB    1 
ATOM   11218 C  CG1   . VAL B 1 694 ? -22.892 9.736   64.003  1.00 23.34 ? 714  VAL B CG1   1 
ATOM   11219 C  CG2   . VAL B 1 694 ? -21.563 9.675   61.852  1.00 23.53 ? 714  VAL B CG2   1 
ATOM   11220 N  N     . ILE B 1 695 ? -21.059 8.032   66.252  1.00 23.82 ? 715  ILE B N     1 
ATOM   11221 C  CA    . ILE B 1 695 ? -21.563 7.381   67.453  1.00 23.45 ? 715  ILE B CA    1 
ATOM   11222 C  C     . ILE B 1 695 ? -22.524 8.334   68.179  1.00 24.09 ? 715  ILE B C     1 
ATOM   11223 O  O     . ILE B 1 695 ? -22.187 9.504   68.458  1.00 23.70 ? 715  ILE B O     1 
ATOM   11224 C  CB    . ILE B 1 695 ? -20.426 6.934   68.404  1.00 23.36 ? 715  ILE B CB    1 
ATOM   11225 C  CG1   . ILE B 1 695 ? -19.277 6.285   67.612  1.00 23.20 ? 715  ILE B CG1   1 
ATOM   11226 C  CG2   . ILE B 1 695 ? -20.967 5.944   69.451  1.00 23.09 ? 715  ILE B CG2   1 
ATOM   11227 C  CD1   . ILE B 1 695 ? -18.189 5.673   68.462  1.00 21.93 ? 715  ILE B CD1   1 
ATOM   11228 N  N     . VAL B 1 696 ? -23.724 7.833   68.473  1.00 24.12 ? 716  VAL B N     1 
ATOM   11229 C  CA    . VAL B 1 696 ? -24.723 8.590   69.210  1.00 24.59 ? 716  VAL B CA    1 
ATOM   11230 C  C     . VAL B 1 696 ? -24.798 8.046   70.639  1.00 25.38 ? 716  VAL B C     1 
ATOM   11231 O  O     . VAL B 1 696 ? -25.059 6.859   70.838  1.00 25.01 ? 716  VAL B O     1 
ATOM   11232 C  CB    . VAL B 1 696 ? -26.125 8.504   68.549  1.00 24.68 ? 716  VAL B CB    1 
ATOM   11233 C  CG1   . VAL B 1 696 ? -27.128 9.348   69.312  1.00 23.61 ? 716  VAL B CG1   1 
ATOM   11234 C  CG2   . VAL B 1 696 ? -26.076 8.955   67.090  1.00 24.45 ? 716  VAL B CG2   1 
ATOM   11235 N  N     . TRP B 1 697 ? -24.574 8.921   71.621  1.00 26.35 ? 717  TRP B N     1 
ATOM   11236 C  CA    . TRP B 1 697 ? -24.598 8.551   73.036  1.00 27.44 ? 717  TRP B CA    1 
ATOM   11237 C  C     . TRP B 1 697 ? -25.755 9.218   73.769  1.00 28.51 ? 717  TRP B C     1 
ATOM   11238 O  O     . TRP B 1 697 ? -26.083 10.364  73.491  1.00 28.92 ? 717  TRP B O     1 
ATOM   11239 C  CB    . TRP B 1 697 ? -23.305 8.983   73.728  1.00 27.27 ? 717  TRP B CB    1 
ATOM   11240 C  CG    . TRP B 1 697 ? -22.060 8.530   73.073  1.00 26.60 ? 717  TRP B CG    1 
ATOM   11241 C  CD1   . TRP B 1 697 ? -21.353 9.193   72.122  1.00 26.14 ? 717  TRP B CD1   1 
ATOM   11242 C  CD2   . TRP B 1 697 ? -21.340 7.323   73.345  1.00 26.44 ? 717  TRP B CD2   1 
ATOM   11243 N  NE1   . TRP B 1 697 ? -20.236 8.471   71.771  1.00 25.74 ? 717  TRP B NE1   1 
ATOM   11244 C  CE2   . TRP B 1 697 ? -20.210 7.314   72.504  1.00 25.75 ? 717  TRP B CE2   1 
ATOM   11245 C  CE3   . TRP B 1 697 ? -21.551 6.241   74.205  1.00 26.81 ? 717  TRP B CE3   1 
ATOM   11246 C  CZ2   . TRP B 1 697 ? -19.292 6.272   72.501  1.00 26.01 ? 717  TRP B CZ2   1 
ATOM   11247 C  CZ3   . TRP B 1 697 ? -20.639 5.206   74.203  1.00 26.59 ? 717  TRP B CZ3   1 
ATOM   11248 C  CH2   . TRP B 1 697 ? -19.522 5.227   73.356  1.00 26.37 ? 717  TRP B CH2   1 
ATOM   11249 N  N     . PRO B 1 698 ? -26.354 8.518   74.741  1.00 30.21 ? 718  PRO B N     1 
ATOM   11250 C  CA    . PRO B 1 698 ? -27.370 9.145   75.569  1.00 31.69 ? 718  PRO B CA    1 
ATOM   11251 C  C     . PRO B 1 698 ? -26.755 10.095  76.601  1.00 33.18 ? 718  PRO B C     1 
ATOM   11252 O  O     . PRO B 1 698 ? -25.597 9.937   76.977  1.00 33.24 ? 718  PRO B O     1 
ATOM   11253 C  CB    . PRO B 1 698 ? -28.019 7.950   76.263  1.00 31.47 ? 718  PRO B CB    1 
ATOM   11254 C  CG    . PRO B 1 698 ? -26.888 7.012   76.448  1.00 30.95 ? 718  PRO B CG    1 
ATOM   11255 C  CD    . PRO B 1 698 ? -26.051 7.155   75.203  1.00 30.06 ? 718  PRO B CD    1 
ATOM   11256 N  N     . ARG B 1 699 ? -27.534 11.073  77.041  1.00 35.28 ? 719  ARG B N     1 
ATOM   11257 C  CA    . ARG B 1 699 ? -27.104 12.025  78.070  1.00 37.14 ? 719  ARG B CA    1 
ATOM   11258 C  C     . ARG B 1 699 ? -28.206 12.168  79.108  1.00 38.20 ? 719  ARG B C     1 
ATOM   11259 O  O     . ARG B 1 699 ? -29.380 12.317  78.751  1.00 38.51 ? 719  ARG B O     1 
ATOM   11260 C  CB    . ARG B 1 699 ? -26.805 13.393  77.446  1.00 37.34 ? 719  ARG B CB    1 
ATOM   11261 C  CG    . ARG B 1 699 ? -25.528 13.438  76.637  1.00 38.39 ? 719  ARG B CG    1 
ATOM   11262 C  CD    . ARG B 1 699 ? -24.326 13.567  77.536  1.00 40.49 ? 719  ARG B CD    1 
ATOM   11263 N  NE    . ARG B 1 699 ? -23.069 13.237  76.859  1.00 42.44 ? 719  ARG B NE    1 
ATOM   11264 C  CZ    . ARG B 1 699 ? -22.599 12.001  76.665  1.00 43.55 ? 719  ARG B CZ    1 
ATOM   11265 N  NH1   . ARG B 1 699 ? -23.277 10.932  77.072  1.00 43.96 ? 719  ARG B NH1   1 
ATOM   11266 N  NH2   . ARG B 1 699 ? -21.435 11.829  76.049  1.00 44.58 ? 719  ARG B NH2   1 
ATOM   11267 N  N     . ASP B 1 700 ? -27.834 12.120  80.384  1.00 39.71 ? 720  ASP B N     1 
ATOM   11268 C  CA    . ASP B 1 700 ? -28.806 12.272  81.476  1.00 40.85 ? 720  ASP B CA    1 
ATOM   11269 C  C     . ASP B 1 700 ? -29.532 13.610  81.381  1.00 41.07 ? 720  ASP B C     1 
ATOM   11270 O  O     . ASP B 1 700 ? -28.901 14.664  81.405  1.00 41.42 ? 720  ASP B O     1 
ATOM   11271 C  CB    . ASP B 1 700 ? -28.115 12.184  82.838  1.00 41.34 ? 720  ASP B CB    1 
ATOM   11272 C  CG    . ASP B 1 700 ? -27.509 10.821  83.102  1.00 43.10 ? 720  ASP B CG    1 
ATOM   11273 O  OD1   . ASP B 1 700 ? -28.058 9.811   82.605  1.00 46.26 ? 720  ASP B OD1   1 
ATOM   11274 O  OD2   . ASP B 1 700 ? -26.483 10.757  83.818  1.00 45.88 ? 720  ASP B OD2   1 
ATOM   11275 N  N     . ASN B 1 701 ? -30.854 13.553  81.242  1.00 41.38 ? 721  ASN B N     1 
ATOM   11276 C  CA    . ASN B 1 701 ? -31.711 14.742  81.293  1.00 41.61 ? 721  ASN B CA    1 
ATOM   11277 C  C     . ASN B 1 701 ? -31.445 15.781  80.202  1.00 41.55 ? 721  ASN B C     1 
ATOM   11278 O  O     . ASN B 1 701 ? -31.724 16.973  80.402  1.00 42.01 ? 721  ASN B O     1 
ATOM   11279 C  CB    . ASN B 1 701 ? -31.619 15.410  82.676  1.00 41.54 ? 721  ASN B CB    1 
ATOM   11280 N  N     . GLY B 1 702 ? -30.927 15.330  79.056  1.00 40.82 ? 722  GLY B N     1 
ATOM   11281 C  CA    . GLY B 1 702 ? -30.659 16.207  77.912  1.00 40.06 ? 722  GLY B CA    1 
ATOM   11282 C  C     . GLY B 1 702 ? -30.699 15.455  76.588  1.00 39.50 ? 722  GLY B C     1 
ATOM   11283 O  O     . GLY B 1 702 ? -30.909 14.240  76.568  1.00 39.67 ? 722  GLY B O     1 
ATOM   11284 N  N     . PRO B 1 703 ? -30.511 16.171  75.465  1.00 38.25 ? 723  PRO B N     1 
ATOM   11285 C  CA    . PRO B 1 703 ? -30.463 15.502  74.163  1.00 37.29 ? 723  PRO B CA    1 
ATOM   11286 C  C     . PRO B 1 703 ? -29.210 14.648  74.007  1.00 35.99 ? 723  PRO B C     1 
ATOM   11287 O  O     . PRO B 1 703 ? -28.245 14.823  74.757  1.00 35.89 ? 723  PRO B O     1 
ATOM   11288 C  CB    . PRO B 1 703 ? -30.458 16.661  73.150  1.00 37.40 ? 723  PRO B CB    1 
ATOM   11289 C  CG    . PRO B 1 703 ? -30.805 17.899  73.940  1.00 38.01 ? 723  PRO B CG    1 
ATOM   11290 C  CD    . PRO B 1 703 ? -30.358 17.631  75.341  1.00 38.54 ? 723  PRO B CD    1 
ATOM   11291 N  N     . ASN B 1 704 ? -29.235 13.729  73.044  1.00 34.26 ? 724  ASN B N     1 
ATOM   11292 C  CA    . ASN B 1 704 ? -28.108 12.828  72.816  1.00 32.99 ? 724  ASN B CA    1 
ATOM   11293 C  C     . ASN B 1 704 ? -26.897 13.587  72.314  1.00 32.03 ? 724  ASN B C     1 
ATOM   11294 O  O     . ASN B 1 704 ? -27.038 14.608  71.660  1.00 31.66 ? 724  ASN B O     1 
ATOM   11295 C  CB    . ASN B 1 704 ? -28.461 11.745  71.788  1.00 32.79 ? 724  ASN B CB    1 
ATOM   11296 C  CG    . ASN B 1 704 ? -29.560 10.827  72.259  1.00 31.96 ? 724  ASN B CG    1 
ATOM   11297 O  OD1   . ASN B 1 704 ? -30.453 10.485  71.493  1.00 32.04 ? 724  ASN B OD1   1 
ATOM   11298 N  ND2   . ASN B 1 704 ? -29.511 10.433  73.520  1.00 27.71 ? 724  ASN B ND2   1 
ATOM   11299 N  N     . TYR B 1 705 ? -25.716 13.071  72.632  1.00 31.04 ? 725  TYR B N     1 
ATOM   11300 C  CA    . TYR B 1 705 ? -24.471 13.568  72.070  1.00 30.54 ? 725  TYR B CA    1 
ATOM   11301 C  C     . TYR B 1 705 ? -24.185 12.812  70.775  1.00 29.81 ? 725  TYR B C     1 
ATOM   11302 O  O     . TYR B 1 705 ? -24.005 11.599  70.793  1.00 29.61 ? 725  TYR B O     1 
ATOM   11303 C  CB    . TYR B 1 705 ? -23.325 13.363  73.068  1.00 30.34 ? 725  TYR B CB    1 
ATOM   11304 C  CG    . TYR B 1 705 ? -21.959 13.707  72.529  1.00 31.50 ? 725  TYR B CG    1 
ATOM   11305 C  CD1   . TYR B 1 705 ? -21.744 14.883  71.811  1.00 33.00 ? 725  TYR B CD1   1 
ATOM   11306 C  CD2   . TYR B 1 705 ? -20.872 12.865  72.748  1.00 32.20 ? 725  TYR B CD2   1 
ATOM   11307 C  CE1   . TYR B 1 705 ? -20.484 15.204  71.315  1.00 33.73 ? 725  TYR B CE1   1 
ATOM   11308 C  CE2   . TYR B 1 705 ? -19.612 13.181  72.256  1.00 33.04 ? 725  TYR B CE2   1 
ATOM   11309 C  CZ    . TYR B 1 705 ? -19.427 14.349  71.542  1.00 33.58 ? 725  TYR B CZ    1 
ATOM   11310 O  OH    . TYR B 1 705 ? -18.182 14.668  71.058  1.00 35.77 ? 725  TYR B OH    1 
ATOM   11311 N  N     . VAL B 1 706 ? -24.170 13.527  69.656  1.00 29.38 ? 726  VAL B N     1 
ATOM   11312 C  CA    . VAL B 1 706 ? -23.826 12.937  68.373  1.00 29.05 ? 726  VAL B CA    1 
ATOM   11313 C  C     . VAL B 1 706 ? -22.348 13.188  68.088  1.00 29.11 ? 726  VAL B C     1 
ATOM   11314 O  O     . VAL B 1 706 ? -21.969 14.265  67.642  1.00 29.11 ? 726  VAL B O     1 
ATOM   11315 C  CB    . VAL B 1 706 ? -24.680 13.509  67.231  1.00 29.08 ? 726  VAL B CB    1 
ATOM   11316 C  CG1   . VAL B 1 706 ? -24.259 12.880  65.903  1.00 28.52 ? 726  VAL B CG1   1 
ATOM   11317 C  CG2   . VAL B 1 706 ? -26.161 13.281  67.508  1.00 27.91 ? 726  VAL B CG2   1 
ATOM   11318 N  N     . GLN B 1 707 ? -21.519 12.185  68.357  1.00 29.46 ? 727  GLN B N     1 
ATOM   11319 C  CA    . GLN B 1 707 ? -20.075 12.313  68.210  1.00 29.95 ? 727  GLN B CA    1 
ATOM   11320 C  C     . GLN B 1 707 ? -19.672 12.075  66.758  1.00 30.70 ? 727  GLN B C     1 
ATOM   11321 O  O     . GLN B 1 707 ? -20.019 11.053  66.173  1.00 31.08 ? 727  GLN B O     1 
ATOM   11322 C  CB    . GLN B 1 707 ? -19.355 11.325  69.128  1.00 29.80 ? 727  GLN B CB    1 
ATOM   11323 C  CG    . GLN B 1 707 ? -17.839 11.473  69.125  1.00 29.56 ? 727  GLN B CG    1 
ATOM   11324 C  CD    . GLN B 1 707 ? -17.152 10.668  70.212  1.00 29.60 ? 727  GLN B CD    1 
ATOM   11325 O  OE1   . GLN B 1 707 ? -17.659 9.643   70.665  1.00 30.23 ? 727  GLN B OE1   1 
ATOM   11326 N  NE2   . GLN B 1 707 ? -15.974 11.125  70.627  1.00 30.98 ? 727  GLN B NE2   1 
ATOM   11327 N  N     . ARG B 1 708 ? -18.940 13.030  66.190  1.00 31.45 ? 728  ARG B N     1 
ATOM   11328 C  CA    . ARG B 1 708 ? -18.454 12.962  64.814  1.00 31.87 ? 728  ARG B CA    1 
ATOM   11329 C  C     . ARG B 1 708 ? -16.972 13.313  64.783  1.00 32.47 ? 728  ARG B C     1 
ATOM   11330 O  O     . ARG B 1 708 ? -16.454 13.922  65.718  1.00 32.48 ? 728  ARG B O     1 
ATOM   11331 C  CB    . ARG B 1 708 ? -19.192 13.975  63.950  1.00 31.84 ? 728  ARG B CB    1 
ATOM   11332 C  CG    . ARG B 1 708 ? -20.708 13.900  64.010  1.00 32.15 ? 728  ARG B CG    1 
ATOM   11333 C  CD    . ARG B 1 708 ? -21.325 15.046  63.224  1.00 31.76 ? 728  ARG B CD    1 
ATOM   11334 N  NE    . ARG B 1 708 ? -22.749 14.840  62.966  1.00 31.87 ? 728  ARG B NE    1 
ATOM   11335 C  CZ    . ARG B 1 708 ? -23.247 14.116  61.966  1.00 32.13 ? 728  ARG B CZ    1 
ATOM   11336 N  NH1   . ARG B 1 708 ? -22.438 13.505  61.105  1.00 31.93 ? 728  ARG B NH1   1 
ATOM   11337 N  NH2   . ARG B 1 708 ? -24.569 14.007  61.822  1.00 33.02 ? 728  ARG B NH2   1 
ATOM   11338 N  N     . TRP B 1 709 ? -16.297 12.927  63.704  1.00 32.90 ? 729  TRP B N     1 
ATOM   11339 C  CA    . TRP B 1 709 ? -14.904 13.310  63.469  1.00 33.00 ? 729  TRP B CA    1 
ATOM   11340 C  C     . TRP B 1 709 ? -14.729 14.050  62.132  1.00 33.81 ? 729  TRP B C     1 
ATOM   11341 O  O     . TRP B 1 709 ? -13.611 14.385  61.741  1.00 33.66 ? 729  TRP B O     1 
ATOM   11342 C  CB    . TRP B 1 709 ? -14.012 12.071  63.531  1.00 32.79 ? 729  TRP B CB    1 
ATOM   11343 C  CG    . TRP B 1 709 ? -13.906 11.511  64.910  1.00 31.76 ? 729  TRP B CG    1 
ATOM   11344 C  CD1   . TRP B 1 709 ? -12.908 11.741  65.813  1.00 31.19 ? 729  TRP B CD1   1 
ATOM   11345 C  CD2   . TRP B 1 709 ? -14.844 10.644  65.562  1.00 31.28 ? 729  TRP B CD2   1 
ATOM   11346 N  NE1   . TRP B 1 709 ? -13.161 11.067  66.979  1.00 30.74 ? 729  TRP B NE1   1 
ATOM   11347 C  CE2   . TRP B 1 709 ? -14.343 10.386  66.855  1.00 30.89 ? 729  TRP B CE2   1 
ATOM   11348 C  CE3   . TRP B 1 709 ? -16.056 10.057  65.176  1.00 30.71 ? 729  TRP B CE3   1 
ATOM   11349 C  CZ2   . TRP B 1 709 ? -15.016 9.566   67.770  1.00 31.13 ? 729  TRP B CZ2   1 
ATOM   11350 C  CZ3   . TRP B 1 709 ? -16.723 9.242   66.080  1.00 30.74 ? 729  TRP B CZ3   1 
ATOM   11351 C  CH2   . TRP B 1 709 ? -16.201 9.003   67.365  1.00 31.36 ? 729  TRP B CH2   1 
ATOM   11352 N  N     . ILE B 1 710 ? -15.844 14.264  61.433  1.00 34.46 ? 730  ILE B N     1 
ATOM   11353 C  CA    . ILE B 1 710 ? -15.934 15.140  60.270  1.00 35.03 ? 730  ILE B CA    1 
ATOM   11354 C  C     . ILE B 1 710 ? -17.276 15.870  60.427  1.00 35.08 ? 730  ILE B C     1 
ATOM   11355 O  O     . ILE B 1 710 ? -18.252 15.270  60.877  1.00 35.22 ? 730  ILE B O     1 
ATOM   11356 C  CB    . ILE B 1 710 ? -15.880 14.348  58.930  1.00 35.35 ? 730  ILE B CB    1 
ATOM   11357 C  CG1   . ILE B 1 710 ? -14.510 13.680  58.757  1.00 36.28 ? 730  ILE B CG1   1 
ATOM   11358 C  CG2   . ILE B 1 710 ? -16.149 15.264  57.730  1.00 35.45 ? 730  ILE B CG2   1 
ATOM   11359 C  CD1   . ILE B 1 710 ? -14.300 13.008  57.385  1.00 37.46 ? 730  ILE B CD1   1 
ATOM   11360 N  N     . PRO B 1 711 ? -17.334 17.171  60.098  1.00 35.34 ? 731  PRO B N     1 
ATOM   11361 C  CA    . PRO B 1 711 ? -18.598 17.876  60.342  1.00 35.26 ? 731  PRO B CA    1 
ATOM   11362 C  C     . PRO B 1 711 ? -19.731 17.336  59.483  1.00 35.26 ? 731  PRO B C     1 
ATOM   11363 O  O     . PRO B 1 711 ? -19.483 16.845  58.380  1.00 35.00 ? 731  PRO B O     1 
ATOM   11364 C  CB    . PRO B 1 711 ? -18.285 19.325  59.953  1.00 35.30 ? 731  PRO B CB    1 
ATOM   11365 C  CG    . PRO B 1 711 ? -16.789 19.417  59.906  1.00 35.54 ? 731  PRO B CG    1 
ATOM   11366 C  CD    . PRO B 1 711 ? -16.303 18.061  59.533  1.00 35.58 ? 731  PRO B CD    1 
ATOM   11367 N  N     . GLU B 1 712 ? -20.957 17.418  59.992  1.00 35.27 ? 732  GLU B N     1 
ATOM   11368 C  CA    . GLU B 1 712 ? -22.127 17.049  59.211  1.00 35.57 ? 732  GLU B CA    1 
ATOM   11369 C  C     . GLU B 1 712 ? -22.141 17.879  57.936  1.00 36.18 ? 732  GLU B C     1 
ATOM   11370 O  O     . GLU B 1 712 ? -21.821 19.064  57.951  1.00 36.64 ? 732  GLU B O     1 
ATOM   11371 C  CB    . GLU B 1 712 ? -23.424 17.268  59.999  1.00 35.36 ? 732  GLU B CB    1 
ATOM   11372 C  CG    . GLU B 1 712 ? -24.684 16.884  59.220  1.00 34.18 ? 732  GLU B CG    1 
ATOM   11373 C  CD    . GLU B 1 712 ? -25.967 16.957  60.039  1.00 32.89 ? 732  GLU B CD    1 
ATOM   11374 O  OE1   . GLU B 1 712 ? -25.929 17.331  61.229  1.00 31.50 ? 732  GLU B OE1   1 
ATOM   11375 O  OE2   . GLU B 1 712 ? -27.030 16.624  59.478  1.00 32.17 ? 732  GLU B OE2   1 
ATOM   11376 N  N     . ASP B 1 713 ? -22.480 17.248  56.826  1.00 36.82 ? 733  ASP B N     1 
ATOM   11377 C  CA    . ASP B 1 713 ? -22.504 17.937  55.550  1.00 37.45 ? 733  ASP B CA    1 
ATOM   11378 C  C     . ASP B 1 713 ? -23.873 17.768  54.923  1.00 37.46 ? 733  ASP B C     1 
ATOM   11379 O  O     . ASP B 1 713 ? -24.377 16.653  54.841  1.00 37.38 ? 733  ASP B O     1 
ATOM   11380 C  CB    . ASP B 1 713 ? -21.436 17.362  54.621  1.00 37.58 ? 733  ASP B CB    1 
ATOM   11381 C  CG    . ASP B 1 713 ? -21.680 17.716  53.171  1.00 38.87 ? 733  ASP B CG    1 
ATOM   11382 O  OD1   . ASP B 1 713 ? -21.827 18.917  52.870  1.00 40.47 ? 733  ASP B OD1   1 
ATOM   11383 O  OD2   . ASP B 1 713 ? -21.739 16.794  52.328  1.00 41.44 ? 733  ASP B OD2   1 
ATOM   11384 N  N     . ARG B 1 714 ? -24.462 18.875  54.481  1.00 37.66 ? 734  ARG B N     1 
ATOM   11385 C  CA    . ARG B 1 714 ? -25.724 18.837  53.741  1.00 37.84 ? 734  ARG B CA    1 
ATOM   11386 C  C     . ARG B 1 714 ? -25.648 19.658  52.448  1.00 37.44 ? 734  ARG B C     1 
ATOM   11387 O  O     . ARG B 1 714 ? -26.677 19.964  51.846  1.00 37.41 ? 734  ARG B O     1 
ATOM   11388 C  CB    . ARG B 1 714 ? -26.867 19.345  54.625  1.00 38.16 ? 734  ARG B CB    1 
ATOM   11389 C  CG    . ARG B 1 714 ? -27.027 18.602  55.960  1.00 39.66 ? 734  ARG B CG    1 
ATOM   11390 C  CD    . ARG B 1 714 ? -27.772 19.472  56.980  1.00 41.36 ? 734  ARG B CD    1 
ATOM   11391 N  NE    . ARG B 1 714 ? -29.102 19.826  56.495  1.00 42.73 ? 734  ARG B NE    1 
ATOM   11392 C  CZ    . ARG B 1 714 ? -29.783 20.917  56.842  1.00 44.46 ? 734  ARG B CZ    1 
ATOM   11393 N  NH1   . ARG B 1 714 ? -29.274 21.804  57.690  1.00 45.50 ? 734  ARG B NH1   1 
ATOM   11394 N  NH2   . ARG B 1 714 ? -30.991 21.128  56.330  1.00 45.51 ? 734  ARG B NH2   1 
ATOM   11395 N  N     . ASP B 1 715 ? -24.432 19.998  52.016  1.00 37.33 ? 735  ASP B N     1 
ATOM   11396 C  CA    . ASP B 1 715 ? -24.233 20.811  50.815  1.00 37.17 ? 735  ASP B CA    1 
ATOM   11397 C  C     . ASP B 1 715 ? -24.661 20.070  49.560  1.00 36.84 ? 735  ASP B C     1 
ATOM   11398 O  O     . ASP B 1 715 ? -24.489 18.859  49.449  1.00 36.20 ? 735  ASP B O     1 
ATOM   11399 C  CB    . ASP B 1 715 ? -22.764 21.209  50.648  1.00 37.36 ? 735  ASP B CB    1 
ATOM   11400 C  CG    . ASP B 1 715 ? -22.297 22.183  51.703  1.00 37.80 ? 735  ASP B CG    1 
ATOM   11401 O  OD1   . ASP B 1 715 ? -23.121 22.601  52.544  1.00 38.37 ? 735  ASP B OD1   1 
ATOM   11402 O  OD2   . ASP B 1 715 ? -21.100 22.535  51.680  1.00 38.47 ? 735  ASP B OD2   1 
ATOM   11403 N  N     . CYS B 1 716 ? -25.218 20.821  48.618  1.00 36.74 ? 736  CYS B N     1 
ATOM   11404 C  CA    . CYS B 1 716 ? -25.591 20.281  47.327  1.00 36.84 ? 736  CYS B CA    1 
ATOM   11405 C  C     . CYS B 1 716 ? -24.886 21.096  46.265  1.00 36.99 ? 736  CYS B C     1 
ATOM   11406 O  O     . CYS B 1 716 ? -24.654 22.282  46.460  1.00 37.14 ? 736  CYS B O     1 
ATOM   11407 C  CB    . CYS B 1 716 ? -27.103 20.349  47.129  1.00 36.57 ? 736  CYS B CB    1 
ATOM   11408 S  SG    . CYS B 1 716 ? -27.633 19.480  45.648  1.00 36.30 ? 736  CYS B SG    1 
ATOM   11409 N  N     . SER B 1 717 ? -24.529 20.451  45.157  1.00 36.94 ? 737  SER B N     1 
ATOM   11410 C  CA    . SER B 1 717 ? -23.975 21.147  43.998  1.00 37.10 ? 737  SER B CA    1 
ATOM   11411 C  C     . SER B 1 717 ? -24.402 20.444  42.713  1.00 37.26 ? 737  SER B C     1 
ATOM   11412 O  O     . SER B 1 717 ? -24.878 19.308  42.747  1.00 37.37 ? 737  SER B O     1 
ATOM   11413 C  CB    . SER B 1 717 ? -22.446 21.205  44.079  1.00 37.12 ? 737  SER B CB    1 
ATOM   11414 O  OG    . SER B 1 717 ? -21.880 19.915  43.932  1.00 36.81 ? 737  SER B OG    1 
ATOM   11415 N  N     . MET B 1 718 ? -24.215 21.119  41.584  1.00 37.58 ? 738  MET B N     1 
ATOM   11416 C  CA    . MET B 1 718 ? -24.584 20.575  40.281  1.00 37.72 ? 738  MET B CA    1 
ATOM   11417 C  C     . MET B 1 718 ? -23.390 19.931  39.601  1.00 37.19 ? 738  MET B C     1 
ATOM   11418 O  O     . MET B 1 718 ? -22.258 20.406  39.743  1.00 37.53 ? 738  MET B O     1 
ATOM   11419 C  CB    . MET B 1 718 ? -25.092 21.672  39.362  1.00 38.32 ? 738  MET B CB    1 
ATOM   11420 C  CG    . MET B 1 718 ? -26.155 22.558  39.941  1.00 40.44 ? 738  MET B CG    1 
ATOM   11421 S  SD    . MET B 1 718 ? -26.578 23.803  38.709  1.00 46.81 ? 738  MET B SD    1 
ATOM   11422 C  CE    . MET B 1 718 ? -25.094 24.835  38.693  1.00 45.00 ? 738  MET B CE    1 
ATOM   11423 N  N     . PRO B 1 719 ? -23.633 18.861  38.833  1.00 36.31 ? 739  PRO B N     1 
ATOM   11424 C  CA    . PRO B 1 719 ? -22.554 18.287  38.053  1.00 35.66 ? 739  PRO B CA    1 
ATOM   11425 C  C     . PRO B 1 719 ? -22.454 18.994  36.705  1.00 34.65 ? 739  PRO B C     1 
ATOM   11426 O  O     . PRO B 1 719 ? -23.322 19.806  36.376  1.00 34.15 ? 739  PRO B O     1 
ATOM   11427 C  CB    . PRO B 1 719 ? -23.005 16.838  37.872  1.00 35.71 ? 739  PRO B CB    1 
ATOM   11428 C  CG    . PRO B 1 719 ? -24.513 16.937  37.805  1.00 36.26 ? 739  PRO B CG    1 
ATOM   11429 C  CD    . PRO B 1 719 ? -24.918 18.184  38.567  1.00 36.49 ? 739  PRO B CD    1 
ATOM   11430 N  N     . PRO B 1 720 ? -21.401 18.691  35.927  1.00 33.88 ? 740  PRO B N     1 
ATOM   11431 C  CA    . PRO B 1 720 ? -21.332 19.160  34.552  1.00 33.44 ? 740  PRO B CA    1 
ATOM   11432 C  C     . PRO B 1 720 ? -22.614 18.832  33.796  1.00 32.52 ? 740  PRO B C     1 
ATOM   11433 O  O     . PRO B 1 720 ? -23.223 17.802  34.056  1.00 32.34 ? 740  PRO B O     1 
ATOM   11434 C  CB    . PRO B 1 720 ? -20.163 18.361  33.968  1.00 33.69 ? 740  PRO B CB    1 
ATOM   11435 C  CG    . PRO B 1 720 ? -19.269 18.102  35.136  1.00 33.89 ? 740  PRO B CG    1 
ATOM   11436 C  CD    . PRO B 1 720 ? -20.188 17.949  36.321  1.00 34.21 ? 740  PRO B CD    1 
ATOM   11437 N  N     . PRO B 1 721 ? -23.036 19.707  32.877  1.00 31.62 ? 741  PRO B N     1 
ATOM   11438 C  CA    . PRO B 1 721 ? -24.166 19.348  32.028  1.00 30.83 ? 741  PRO B CA    1 
ATOM   11439 C  C     . PRO B 1 721 ? -23.828 18.121  31.179  1.00 29.81 ? 741  PRO B C     1 
ATOM   11440 O  O     . PRO B 1 721 ? -22.653 17.878  30.882  1.00 29.60 ? 741  PRO B O     1 
ATOM   11441 C  CB    . PRO B 1 721 ? -24.346 20.577  31.139  1.00 31.00 ? 741  PRO B CB    1 
ATOM   11442 C  CG    . PRO B 1 721 ? -23.579 21.679  31.816  1.00 31.48 ? 741  PRO B CG    1 
ATOM   11443 C  CD    . PRO B 1 721 ? -22.471 21.019  32.525  1.00 31.98 ? 741  PRO B CD    1 
ATOM   11444 N  N     . PHE B 1 722 ? -24.842 17.353  30.800  1.00 28.67 ? 742  PHE B N     1 
ATOM   11445 C  CA    . PHE B 1 722 ? -24.609 16.148  30.024  1.00 27.73 ? 742  PHE B CA    1 
ATOM   11446 C  C     . PHE B 1 722 ? -24.011 16.502  28.674  1.00 27.33 ? 742  PHE B C     1 
ATOM   11447 O  O     . PHE B 1 722 ? -24.452 17.444  28.025  1.00 27.19 ? 742  PHE B O     1 
ATOM   11448 C  CB    . PHE B 1 722 ? -25.905 15.379  29.792  1.00 27.58 ? 742  PHE B CB    1 
ATOM   11449 C  CG    . PHE B 1 722 ? -25.715 14.122  28.994  1.00 26.72 ? 742  PHE B CG    1 
ATOM   11450 C  CD1   . PHE B 1 722 ? -25.301 12.947  29.619  1.00 25.84 ? 742  PHE B CD1   1 
ATOM   11451 C  CD2   . PHE B 1 722 ? -25.911 14.116  27.624  1.00 26.17 ? 742  PHE B CD2   1 
ATOM   11452 C  CE1   . PHE B 1 722 ? -25.121 11.783  28.890  1.00 25.99 ? 742  PHE B CE1   1 
ATOM   11453 C  CE2   . PHE B 1 722 ? -25.737 12.950  26.886  1.00 26.11 ? 742  PHE B CE2   1 
ATOM   11454 C  CZ    . PHE B 1 722 ? -25.337 11.785  27.521  1.00 26.10 ? 742  PHE B CZ    1 
ATOM   11455 N  N     . SER B 1 723 ? -23.003 15.749  28.261  1.00 26.72 ? 743  SER B N     1 
ATOM   11456 C  CA    . SER B 1 723 ? -22.534 15.801  26.884  1.00 26.53 ? 743  SER B CA    1 
ATOM   11457 C  C     . SER B 1 723 ? -22.065 14.416  26.472  1.00 26.24 ? 743  SER B C     1 
ATOM   11458 O  O     . SER B 1 723 ? -21.721 13.596  27.320  1.00 25.90 ? 743  SER B O     1 
ATOM   11459 C  CB    . SER B 1 723 ? -21.394 16.805  26.720  1.00 26.48 ? 743  SER B CB    1 
ATOM   11460 O  OG    . SER B 1 723 ? -20.183 16.280  27.240  1.00 26.77 ? 743  SER B OG    1 
ATOM   11461 N  N     . TYR B 1 724 ? -22.059 14.173  25.165  1.00 26.44 ? 744  TYR B N     1 
ATOM   11462 C  CA    . TYR B 1 724 ? -21.594 12.908  24.595  1.00 26.09 ? 744  TYR B CA    1 
ATOM   11463 C  C     . TYR B 1 724 ? -21.089 13.177  23.188  1.00 25.99 ? 744  TYR B C     1 
ATOM   11464 O  O     . TYR B 1 724 ? -21.751 13.854  22.403  1.00 26.48 ? 744  TYR B O     1 
ATOM   11465 C  CB    . TYR B 1 724 ? -22.731 11.895  24.564  1.00 25.97 ? 744  TYR B CB    1 
ATOM   11466 C  CG    . TYR B 1 724 ? -22.278 10.464  24.437  1.00 25.01 ? 744  TYR B CG    1 
ATOM   11467 C  CD1   . TYR B 1 724 ? -21.890 9.748   25.556  1.00 24.36 ? 744  TYR B CD1   1 
ATOM   11468 C  CD2   . TYR B 1 724 ? -22.237 9.828   23.201  1.00 24.41 ? 744  TYR B CD2   1 
ATOM   11469 C  CE1   . TYR B 1 724 ? -21.466 8.430   25.459  1.00 25.11 ? 744  TYR B CE1   1 
ATOM   11470 C  CE2   . TYR B 1 724 ? -21.809 8.498   23.086  1.00 24.82 ? 744  TYR B CE2   1 
ATOM   11471 C  CZ    . TYR B 1 724 ? -21.426 7.809   24.223  1.00 24.67 ? 744  TYR B CZ    1 
ATOM   11472 O  OH    . TYR B 1 724 ? -21.021 6.509   24.146  1.00 22.07 ? 744  TYR B OH    1 
ATOM   11473 N  N     . ASN B 1 725 ? -19.908 12.659  22.880  1.00 25.68 ? 745  ASN B N     1 
ATOM   11474 C  CA    . ASN B 1 725 ? -19.273 12.903  21.601  1.00 25.51 ? 745  ASN B CA    1 
ATOM   11475 C  C     . ASN B 1 725 ? -19.550 11.783  20.599  1.00 24.80 ? 745  ASN B C     1 
ATOM   11476 O  O     . ASN B 1 725 ? -20.104 12.023  19.527  1.00 24.36 ? 745  ASN B O     1 
ATOM   11477 C  CB    . ASN B 1 725 ? -17.772 13.054  21.793  1.00 26.01 ? 745  ASN B CB    1 
ATOM   11478 C  CG    . ASN B 1 725 ? -17.091 13.515  20.544  1.00 27.47 ? 745  ASN B CG    1 
ATOM   11479 O  OD1   . ASN B 1 725 ? -16.741 12.721  19.674  1.00 29.20 ? 745  ASN B OD1   1 
ATOM   11480 N  ND2   . ASN B 1 725 ? -16.913 14.819  20.438  1.00 31.34 ? 745  ASN B ND2   1 
ATOM   11481 N  N     . GLY B 1 726 ? -19.146 10.566  20.957  1.00 24.12 ? 746  GLY B N     1 
ATOM   11482 C  CA    . GLY B 1 726 ? -19.416 9.387   20.155  1.00 23.68 ? 746  GLY B CA    1 
ATOM   11483 C  C     . GLY B 1 726 ? -18.397 9.087   19.071  1.00 23.47 ? 746  GLY B C     1 
ATOM   11484 O  O     . GLY B 1 726 ? -18.496 8.049   18.426  1.00 23.34 ? 746  GLY B O     1 
ATOM   11485 N  N     . THR B 1 727 ? -17.432 9.981   18.856  1.00 23.06 ? 747  THR B N     1 
ATOM   11486 C  CA    . THR B 1 727 ? -16.348 9.715   17.911  1.00 22.97 ? 747  THR B CA    1 
ATOM   11487 C  C     . THR B 1 727 ? -15.056 9.405   18.645  1.00 23.52 ? 747  THR B C     1 
ATOM   11488 O  O     . THR B 1 727 ? -14.865 9.804   19.795  1.00 23.37 ? 747  THR B O     1 
ATOM   11489 C  CB    . THR B 1 727 ? -16.094 10.886  16.922  1.00 22.72 ? 747  THR B CB    1 
ATOM   11490 O  OG1   . THR B 1 727 ? -15.444 11.969  17.603  1.00 22.31 ? 747  THR B OG1   1 
ATOM   11491 C  CG2   . THR B 1 727 ? -17.399 11.359  16.269  1.00 21.55 ? 747  THR B CG2   1 
ATOM   11492 N  N     . TYR B 1 728 ? -14.182 8.681   17.954  1.00 24.34 ? 748  TYR B N     1 
ATOM   11493 C  CA    . TYR B 1 728 ? -12.883 8.250   18.474  1.00 25.21 ? 748  TYR B CA    1 
ATOM   11494 C  C     . TYR B 1 728 ? -11.945 8.354   17.269  1.00 26.26 ? 748  TYR B C     1 
ATOM   11495 O  O     . TYR B 1 728 ? -12.097 7.609   16.288  1.00 26.47 ? 748  TYR B O     1 
ATOM   11496 C  CB    . TYR B 1 728 ? -12.951 6.820   19.077  1.00 25.06 ? 748  TYR B CB    1 
ATOM   11497 C  CG    . TYR B 1 728 ? -13.829 5.881   18.280  1.00 24.09 ? 748  TYR B CG    1 
ATOM   11498 C  CD1   . TYR B 1 728 ? -13.275 4.937   17.427  1.00 23.15 ? 748  TYR B CD1   1 
ATOM   11499 C  CD2   . TYR B 1 728 ? -15.219 5.989   18.328  1.00 24.48 ? 748  TYR B CD2   1 
ATOM   11500 C  CE1   . TYR B 1 728 ? -14.076 4.121   16.656  1.00 23.34 ? 748  TYR B CE1   1 
ATOM   11501 C  CE2   . TYR B 1 728 ? -16.032 5.175   17.561  1.00 23.59 ? 748  TYR B CE2   1 
ATOM   11502 C  CZ    . TYR B 1 728 ? -15.458 4.251   16.722  1.00 23.48 ? 748  TYR B CZ    1 
ATOM   11503 O  OH    . TYR B 1 728 ? -16.254 3.440   15.952  1.00 24.36 ? 748  TYR B OH    1 
ATOM   11504 N  N     . ARG B 1 729 ? -11.026 9.322   17.322  1.00 27.41 ? 749  ARG B N     1 
ATOM   11505 C  CA    . ARG B 1 729 ? -10.172 9.666   16.180  1.00 28.48 ? 749  ARG B CA    1 
ATOM   11506 C  C     . ARG B 1 729 ? -8.726  9.941   16.604  1.00 28.62 ? 749  ARG B C     1 
ATOM   11507 O  O     . ARG B 1 729 ? -8.463  10.203  17.777  1.00 28.39 ? 749  ARG B O     1 
ATOM   11508 C  CB    . ARG B 1 729 ? -10.690 10.925  15.484  1.00 28.83 ? 749  ARG B CB    1 
ATOM   11509 C  CG    . ARG B 1 729 ? -12.147 10.907  15.088  1.00 31.20 ? 749  ARG B CG    1 
ATOM   11510 C  CD    . ARG B 1 729 ? -12.393 10.079  13.861  1.00 33.57 ? 749  ARG B CD    1 
ATOM   11511 N  NE    . ARG B 1 729 ? -13.826 9.879   13.652  1.00 35.91 ? 749  ARG B NE    1 
ATOM   11512 C  CZ    . ARG B 1 729 ? -14.661 10.800  13.173  1.00 38.41 ? 749  ARG B CZ    1 
ATOM   11513 N  NH1   . ARG B 1 729 ? -14.225 12.016  12.832  1.00 39.14 ? 749  ARG B NH1   1 
ATOM   11514 N  NH2   . ARG B 1 729 ? -15.950 10.503  13.030  1.00 37.96 ? 749  ARG B NH2   1 
ATOM   11515 N  N     . PRO B 1 730 ? -7.787  9.901   15.640  1.00 28.83 ? 750  PRO B N     1 
ATOM   11516 C  CA    . PRO B 1 730 ? -6.415  10.284  15.954  1.00 29.37 ? 750  PRO B CA    1 
ATOM   11517 C  C     . PRO B 1 730 ? -6.302  11.750  16.365  1.00 29.96 ? 750  PRO B C     1 
ATOM   11518 O  O     . PRO B 1 730 ? -7.146  12.567  16.006  1.00 30.11 ? 750  PRO B O     1 
ATOM   11519 C  CB    . PRO B 1 730 ? -5.650  10.026  14.646  1.00 29.43 ? 750  PRO B CB    1 
ATOM   11520 C  CG    . PRO B 1 730 ? -6.516  9.106   13.848  1.00 29.16 ? 750  PRO B CG    1 
ATOM   11521 C  CD    . PRO B 1 730 ? -7.927  9.431   14.251  1.00 28.82 ? 750  PRO B CD    1 
ATOM   11522 N  N     . VAL B 1 731 ? -5.278  12.060  17.146  1.00 30.50 ? 751  VAL B N     1 
ATOM   11523 C  CA    . VAL B 1 731 ? -5.033  13.421  17.592  1.00 31.10 ? 751  VAL B CA    1 
ATOM   11524 C  C     . VAL B 1 731 ? -3.589  13.772  17.274  1.00 31.49 ? 751  VAL B C     1 
ATOM   11525 O  O     . VAL B 1 731 ? -2.649  13.148  17.782  1.00 31.04 ? 751  VAL B O     1 
ATOM   11526 C  CB    . VAL B 1 731 ? -5.271  13.586  19.103  1.00 31.18 ? 751  VAL B CB    1 
ATOM   11527 C  CG1   . VAL B 1 731 ? -4.767  14.952  19.573  1.00 31.09 ? 751  VAL B CG1   1 
ATOM   11528 C  CG2   . VAL B 1 731 ? -6.747  13.407  19.427  1.00 30.77 ? 751  VAL B CG2   1 
ATOM   11529 O  OXT   . VAL B 1 731 ? -3.367  14.690  16.487  1.00 32.09 ? 751  VAL B OXT   1 
HETATM 11530 CU CU    . CU  C 2 .   ? -21.169 -14.592 61.886  1.00 21.27 ? 801  CU  A CU    1 
HETATM 11531 CA CA    . CA  D 3 .   ? -48.234 -19.931 45.240  1.00 20.49 ? 802  CA  A CA    1 
HETATM 11532 CA CA    . CA  E 3 .   ? -47.004 -31.482 51.252  1.00 19.57 ? 803  CA  A CA    1 
HETATM 11533 C  C1    . GOL F 4 .   ? -49.177 7.024   56.657  1.00 27.00 ? 804  GOL A C1    1 
HETATM 11534 O  O1    . GOL F 4 .   ? -49.682 5.712   56.683  1.00 27.39 ? 804  GOL A O1    1 
HETATM 11535 C  C2    . GOL F 4 .   ? -49.441 7.649   55.297  1.00 25.86 ? 804  GOL A C2    1 
HETATM 11536 O  O2    . GOL F 4 .   ? -48.798 6.890   54.310  1.00 25.19 ? 804  GOL A O2    1 
HETATM 11537 C  C3    . GOL F 4 .   ? -50.933 7.768   55.025  1.00 25.41 ? 804  GOL A C3    1 
HETATM 11538 O  O3    . GOL F 4 .   ? -51.132 8.643   53.934  1.00 25.17 ? 804  GOL A O3    1 
HETATM 11539 C  C1    . PNT G 5 .   ? -28.307 -13.457 73.133  0.75 27.49 ? 901  PNT A C1    1 
HETATM 11540 C  C2    . PNT G 5 .   ? -27.308 -13.603 72.184  0.75 27.23 ? 901  PNT A C2    1 
HETATM 11541 C  C3    . PNT G 5 .   ? -27.627 -13.879 70.861  0.75 27.91 ? 901  PNT A C3    1 
HETATM 11542 C  C4    . PNT G 5 .   ? -28.954 -14.014 70.485  0.75 28.66 ? 901  PNT A C4    1 
HETATM 11543 C  C5    . PNT G 5 .   ? -29.957 -13.885 71.438  0.75 28.55 ? 901  PNT A C5    1 
HETATM 11544 C  C6    . PNT G 5 .   ? -29.632 -13.610 72.757  0.75 27.89 ? 901  PNT A C6    1 
HETATM 11545 C  C7    . PNT G 5 .   ? -28.335 -12.116 75.220  0.75 29.04 ? 901  PNT A C7    1 
HETATM 11546 C  C8    . PNT G 5 .   ? -29.697 -12.308 75.824  0.75 29.76 ? 901  PNT A C8    1 
HETATM 11547 C  C9    . PNT G 5 .   ? -29.322 -14.320 69.077  0.75 30.81 ? 901  PNT A C9    1 
HETATM 11548 C  C10   . PNT G 5 .   ? -30.709 -11.432 75.100  0.75 29.55 ? 901  PNT A C10   1 
HETATM 11549 C  "C1'" . PNT G 5 .   ? -34.120 -9.650  73.986  0.75 30.34 ? 901  PNT A "C1'" 1 
HETATM 11550 C  "C2'" . PNT G 5 .   ? -35.162 -10.530 73.692  0.75 30.70 ? 901  PNT A "C2'" 1 
HETATM 11551 C  "C3'" . PNT G 5 .   ? -36.279 -10.083 72.995  0.75 30.68 ? 901  PNT A "C3'" 1 
HETATM 11552 C  "C4'" . PNT G 5 .   ? -36.369 -8.756  72.594  0.75 30.22 ? 901  PNT A "C4'" 1 
HETATM 11553 C  "C5'" . PNT G 5 .   ? -35.333 -7.873  72.891  0.75 30.80 ? 901  PNT A "C5'" 1 
HETATM 11554 C  "C6'" . PNT G 5 .   ? -34.210 -8.316  73.582  0.75 29.88 ? 901  PNT A "C6'" 1 
HETATM 11555 C  "C7'" . PNT G 5 .   ? -31.920 -9.288  75.005  0.75 29.53 ? 901  PNT A "C7'" 1 
HETATM 11556 C  "C8'" . PNT G 5 .   ? -30.900 -10.092 75.786  0.75 29.45 ? 901  PNT A "C8'" 1 
HETATM 11557 C  "C9'" . PNT G 5 .   ? -37.580 -8.270  71.856  0.75 29.63 ? 901  PNT A "C9'" 1 
HETATM 11558 O  O1    . PNT G 5 .   ? -27.958 -13.227 74.436  0.75 28.30 ? 901  PNT A O1    1 
HETATM 11559 O  "O1'" . PNT G 5 .   ? -33.030 -10.124 74.672  0.75 29.20 ? 901  PNT A "O1'" 1 
HETATM 11560 N  N1    . PNT G 5 .   ? -28.664 -13.882 68.096  0.75 31.73 ? 901  PNT A N1    1 
HETATM 11561 N  N2    . PNT G 5 .   ? -30.368 -15.111 68.855  0.75 32.89 ? 901  PNT A N2    1 
HETATM 11562 N  "N1'" . PNT G 5 .   ? -38.068 -8.975  70.931  0.75 30.25 ? 901  PNT A "N1'" 1 
HETATM 11563 N  "N2'" . PNT G 5 .   ? -38.140 -7.101  72.184  0.75 28.79 ? 901  PNT A "N2'" 1 
HETATM 11564 C  C1    . NAG H 6 .   ? -53.258 -24.273 79.500  1.00 32.68 ? 1101 NAG A C1    1 
HETATM 11565 C  C2    . NAG H 6 .   ? -54.117 -25.523 79.376  1.00 34.84 ? 1101 NAG A C2    1 
HETATM 11566 C  C3    . NAG H 6 .   ? -55.551 -25.094 79.103  1.00 36.22 ? 1101 NAG A C3    1 
HETATM 11567 C  C4    . NAG H 6 .   ? -56.036 -24.143 80.187  1.00 37.07 ? 1101 NAG A C4    1 
HETATM 11568 C  C5    . NAG H 6 .   ? -55.054 -22.971 80.285  1.00 35.21 ? 1101 NAG A C5    1 
HETATM 11569 C  C6    . NAG H 6 .   ? -55.434 -21.955 81.355  1.00 34.89 ? 1101 NAG A C6    1 
HETATM 11570 C  C7    . NAG H 6 .   ? -53.263 -27.607 78.381  1.00 35.85 ? 1101 NAG A C7    1 
HETATM 11571 C  C8    . NAG H 6 .   ? -52.838 -28.289 77.114  1.00 34.51 ? 1101 NAG A C8    1 
HETATM 11572 N  N2    . NAG H 6 .   ? -53.664 -26.336 78.264  1.00 34.69 ? 1101 NAG A N2    1 
HETATM 11573 O  O3    . NAG H 6 .   ? -56.404 -26.213 78.983  1.00 37.17 ? 1101 NAG A O3    1 
HETATM 11574 O  O4    . NAG H 6 .   ? -57.322 -23.691 79.819  1.00 39.60 ? 1101 NAG A O4    1 
HETATM 11575 O  O5    . NAG H 6 .   ? -53.745 -23.458 80.542  1.00 33.22 ? 1101 NAG A O5    1 
HETATM 11576 O  O6    . NAG H 6 .   ? -55.166 -22.502 82.624  1.00 34.53 ? 1101 NAG A O6    1 
HETATM 11577 O  O7    . NAG H 6 .   ? -53.225 -28.228 79.442  1.00 36.11 ? 1101 NAG A O7    1 
HETATM 11578 C  C1    . NAG I 6 .   ? -58.258 -23.764 80.908  1.00 42.90 ? 1102 NAG A C1    1 
HETATM 11579 C  C2    . NAG I 6 .   ? -59.483 -22.964 80.523  1.00 44.07 ? 1102 NAG A C2    1 
HETATM 11580 C  C3    . NAG I 6 .   ? -60.569 -23.000 81.597  1.00 46.13 ? 1102 NAG A C3    1 
HETATM 11581 C  C4    . NAG I 6 .   ? -60.733 -24.339 82.307  1.00 47.03 ? 1102 NAG A C4    1 
HETATM 11582 C  C5    . NAG I 6 .   ? -59.437 -25.151 82.385  1.00 46.90 ? 1102 NAG A C5    1 
HETATM 11583 C  C6    . NAG I 6 .   ? -59.752 -26.622 82.621  1.00 47.65 ? 1102 NAG A C6    1 
HETATM 11584 C  C7    . NAG I 6 .   ? -58.975 -21.021 79.130  1.00 43.22 ? 1102 NAG A C7    1 
HETATM 11585 C  C8    . NAG I 6 .   ? -58.532 -19.588 79.107  1.00 41.30 ? 1102 NAG A C8    1 
HETATM 11586 N  N2    . NAG I 6 .   ? -59.067 -21.588 80.326  1.00 43.92 ? 1102 NAG A N2    1 
HETATM 11587 O  O3    . NAG I 6 .   ? -61.801 -22.628 81.023  1.00 46.72 ? 1102 NAG A O3    1 
HETATM 11588 O  O4    . NAG I 6 .   ? -61.138 -24.029 83.623  1.00 49.14 ? 1102 NAG A O4    1 
HETATM 11589 O  O5    . NAG I 6 .   ? -58.660 -25.072 81.206  1.00 44.28 ? 1102 NAG A O5    1 
HETATM 11590 O  O6    . NAG I 6 .   ? -58.545 -27.288 82.904  1.00 49.06 ? 1102 NAG A O6    1 
HETATM 11591 O  O7    . NAG I 6 .   ? -59.234 -21.617 78.088  1.00 44.18 ? 1102 NAG A O7    1 
HETATM 11592 C  C1    . BMA J 7 .   ? -62.462 -24.373 84.121  1.00 50.33 ? 1103 BMA A C1    1 
HETATM 11593 C  C2    . BMA J 7 .   ? -63.629 -23.951 83.225  1.00 51.10 ? 1103 BMA A C2    1 
HETATM 11594 C  C3    . BMA J 7 .   ? -64.962 -24.361 83.837  1.00 51.34 ? 1103 BMA A C3    1 
HETATM 11595 C  C4    . BMA J 7 .   ? -64.922 -25.798 84.332  1.00 51.09 ? 1103 BMA A C4    1 
HETATM 11596 C  C5    . BMA J 7 .   ? -63.724 -26.018 85.240  1.00 51.69 ? 1103 BMA A C5    1 
HETATM 11597 C  C6    . BMA J 7 .   ? -63.667 -27.460 85.752  1.00 52.10 ? 1103 BMA A C6    1 
HETATM 11598 O  O2    . BMA J 7 .   ? -63.562 -24.496 81.935  1.00 51.77 ? 1103 BMA A O2    1 
HETATM 11599 O  O3    . BMA J 7 .   ? -65.960 -24.245 82.852  1.00 51.92 ? 1103 BMA A O3    1 
HETATM 11600 O  O4    . BMA J 7 .   ? -66.090 -26.077 85.046  1.00 51.39 ? 1103 BMA A O4    1 
HETATM 11601 O  O5    . BMA J 7 .   ? -62.574 -25.735 84.466  1.00 51.50 ? 1103 BMA A O5    1 
HETATM 11602 O  O6    . BMA J 7 .   ? -64.096 -27.555 87.092  1.00 52.29 ? 1103 BMA A O6    1 
HETATM 11603 C  C1    . NAG K 6 .   ? -18.532 -37.633 19.317  1.00 32.54 ? 5381 NAG A C1    1 
HETATM 11604 C  C2    . NAG K 6 .   ? -17.298 -38.009 20.134  1.00 33.68 ? 5381 NAG A C2    1 
HETATM 11605 C  C3    . NAG K 6 .   ? -16.202 -38.548 19.217  1.00 35.87 ? 5381 NAG A C3    1 
HETATM 11606 C  C4    . NAG K 6 .   ? -16.718 -39.699 18.356  1.00 37.59 ? 5381 NAG A C4    1 
HETATM 11607 C  C5    . NAG K 6 .   ? -17.989 -39.239 17.646  1.00 36.21 ? 5381 NAG A C5    1 
HETATM 11608 C  C6    . NAG K 6 .   ? -18.629 -40.341 16.803  1.00 36.44 ? 5381 NAG A C6    1 
HETATM 11609 C  C7    . NAG K 6 .   ? -17.184 -36.537 22.075  1.00 31.68 ? 5381 NAG A C7    1 
HETATM 11610 C  C8    . NAG K 6 .   ? -16.505 -35.359 22.719  1.00 30.18 ? 5381 NAG A C8    1 
HETATM 11611 N  N2    . NAG K 6 .   ? -16.755 -36.886 20.874  1.00 32.58 ? 5381 NAG A N2    1 
HETATM 11612 O  O3    . NAG K 6 .   ? -15.086 -38.929 19.985  1.00 35.37 ? 5381 NAG A O3    1 
HETATM 11613 O  O4    . NAG K 6 .   ? -15.766 -39.973 17.358  1.00 41.19 ? 5381 NAG A O4    1 
HETATM 11614 O  O5    . NAG K 6 .   ? -18.937 -38.782 18.584  1.00 33.31 ? 5381 NAG A O5    1 
HETATM 11615 O  O6    . NAG K 6 .   ? -18.912 -41.441 17.629  1.00 36.53 ? 5381 NAG A O6    1 
HETATM 11616 O  O7    . NAG K 6 .   ? -18.095 -37.132 22.637  1.00 31.95 ? 5381 NAG A O7    1 
HETATM 11617 C  C1    . NAG L 6 .   ? -15.153 -41.270 17.461  1.00 45.40 ? 5382 NAG A C1    1 
HETATM 11618 C  C2    . NAG L 6 .   ? -14.575 -41.574 16.082  1.00 46.62 ? 5382 NAG A C2    1 
HETATM 11619 C  C3    . NAG L 6 .   ? -13.732 -42.839 16.061  1.00 47.88 ? 5382 NAG A C3    1 
HETATM 11620 C  C4    . NAG L 6 .   ? -12.743 -42.868 17.211  1.00 48.47 ? 5382 NAG A C4    1 
HETATM 11621 C  C5    . NAG L 6 .   ? -13.364 -42.464 18.550  1.00 48.61 ? 5382 NAG A C5    1 
HETATM 11622 C  C6    . NAG L 6 .   ? -12.244 -42.201 19.552  1.00 48.97 ? 5382 NAG A C6    1 
HETATM 11623 C  C7    . NAG L 6 .   ? -15.981 -40.766 14.242  1.00 47.99 ? 5382 NAG A C7    1 
HETATM 11624 C  C8    . NAG L 6 .   ? -17.123 -41.092 13.325  1.00 48.08 ? 5382 NAG A C8    1 
HETATM 11625 N  N2    . NAG L 6 .   ? -15.653 -41.718 15.118  1.00 47.33 ? 5382 NAG A N2    1 
HETATM 11626 O  O3    . NAG L 6 .   ? -13.013 -42.925 14.846  1.00 48.31 ? 5382 NAG A O3    1 
HETATM 11627 O  O4    . NAG L 6 .   ? -12.248 -44.187 17.282  1.00 49.75 ? 5382 NAG A O4    1 
HETATM 11628 O  O5    . NAG L 6 .   ? -14.150 -41.282 18.457  1.00 47.08 ? 5382 NAG A O5    1 
HETATM 11629 O  O6    . NAG L 6 .   ? -12.761 -42.230 20.865  1.00 50.17 ? 5382 NAG A O6    1 
HETATM 11630 O  O7    . NAG L 6 .   ? -15.416 -39.671 14.168  1.00 48.22 ? 5382 NAG A O7    1 
HETATM 11631 C  C1    . NAG M 6 .   ? -36.950 11.112  71.913  1.00 35.12 ? 7451 NAG A C1    1 
HETATM 11632 C  C2    . NAG M 6 .   ? -36.383 12.304  72.668  1.00 37.61 ? 7451 NAG A C2    1 
HETATM 11633 C  C3    . NAG M 6 .   ? -37.328 12.810  73.745  1.00 39.27 ? 7451 NAG A C3    1 
HETATM 11634 C  C4    . NAG M 6 .   ? -38.762 12.863  73.246  1.00 41.57 ? 7451 NAG A C4    1 
HETATM 11635 C  C5    . NAG M 6 .   ? -39.181 11.550  72.603  1.00 40.15 ? 7451 NAG A C5    1 
HETATM 11636 C  C6    . NAG M 6 .   ? -40.580 11.654  72.014  1.00 40.48 ? 7451 NAG A C6    1 
HETATM 11637 C  C7    . NAG M 6 .   ? -33.921 12.230  72.772  1.00 38.17 ? 7451 NAG A C7    1 
HETATM 11638 C  C8    . NAG M 6 .   ? -32.752 11.717  73.560  1.00 38.62 ? 7451 NAG A C8    1 
HETATM 11639 N  N2    . NAG M 6 .   ? -35.118 11.920  73.270  1.00 38.06 ? 7451 NAG A N2    1 
HETATM 11640 O  O3    . NAG M 6 .   ? -36.901 14.105  74.074  1.00 38.88 ? 7451 NAG A O3    1 
HETATM 11641 O  O4    . NAG M 6 .   ? -39.649 13.135  74.308  1.00 46.50 ? 7451 NAG A O4    1 
HETATM 11642 O  O5    . NAG M 6 .   ? -38.300 11.285  71.549  1.00 37.20 ? 7451 NAG A O5    1 
HETATM 11643 O  O6    . NAG M 6 .   ? -40.635 12.755  71.134  1.00 40.50 ? 7451 NAG A O6    1 
HETATM 11644 O  O7    . NAG M 6 .   ? -33.738 12.888  71.748  1.00 37.78 ? 7451 NAG A O7    1 
HETATM 11645 C  C1    . NAG N 6 .   ? -40.073 14.506  74.219  1.00 51.14 ? 7452 NAG A C1    1 
HETATM 11646 C  C2    . NAG N 6 .   ? -41.273 14.723  75.120  1.00 52.78 ? 7452 NAG A C2    1 
HETATM 11647 C  C3    . NAG N 6 .   ? -41.713 16.186  75.091  1.00 54.18 ? 7452 NAG A C3    1 
HETATM 11648 C  C4    . NAG N 6 .   ? -40.545 17.178  75.176  1.00 54.74 ? 7452 NAG A C4    1 
HETATM 11649 C  C5    . NAG N 6 .   ? -39.322 16.742  74.369  1.00 54.69 ? 7452 NAG A C5    1 
HETATM 11650 C  C6    . NAG N 6 .   ? -38.099 17.587  74.734  1.00 55.05 ? 7452 NAG A C6    1 
HETATM 11651 C  C7    . NAG N 6 .   ? -42.619 12.679  75.255  1.00 53.66 ? 7452 NAG A C7    1 
HETATM 11652 C  C8    . NAG N 6 .   ? -43.785 11.921  74.692  1.00 53.61 ? 7452 NAG A C8    1 
HETATM 11653 N  N2    . NAG N 6 .   ? -42.366 13.862  74.694  1.00 53.07 ? 7452 NAG A N2    1 
HETATM 11654 O  O3    . NAG N 6 .   ? -42.603 16.393  76.169  1.00 54.97 ? 7452 NAG A O3    1 
HETATM 11655 O  O4    . NAG N 6 .   ? -40.943 18.445  74.684  1.00 55.36 ? 7452 NAG A O4    1 
HETATM 11656 O  O5    . NAG N 6 .   ? -39.037 15.381  74.605  1.00 53.26 ? 7452 NAG A O5    1 
HETATM 11657 O  O6    . NAG N 6 .   ? -37.463 18.038  73.557  1.00 55.25 ? 7452 NAG A O6    1 
HETATM 11658 O  O7    . NAG N 6 .   ? -41.958 12.204  76.182  1.00 54.08 ? 7452 NAG A O7    1 
HETATM 11659 CU CU    . CU  O 2 .   ? -25.617 -13.900 27.324  1.00 19.57 ? 801  CU  B CU    1 
HETATM 11660 CA CA    . CA  P 3 .   ? 1.999   -13.877 43.782  1.00 24.30 ? 802  CA  B CA    1 
HETATM 11661 CA CA    . CA  Q 3 .   ? 3.726   -24.951 36.776  1.00 37.10 ? 803  CA  B CA    1 
HETATM 11662 C  C1    . PNT R 5 .   ? -19.253 -10.005 15.981  0.75 25.00 ? 901  PNT B C1    1 
HETATM 11663 C  C2    . PNT R 5 .   ? -20.172 -10.523 16.880  0.75 24.56 ? 901  PNT B C2    1 
HETATM 11664 C  C3    . PNT R 5 .   ? -19.802 -10.906 18.144  0.75 24.08 ? 901  PNT B C3    1 
HETATM 11665 C  C4    . PNT R 5 .   ? -18.484 -10.781 18.522  0.75 25.04 ? 901  PNT B C4    1 
HETATM 11666 C  C5    . PNT R 5 .   ? -17.538 -10.274 17.636  0.75 25.36 ? 901  PNT B C5    1 
HETATM 11667 C  C6    . PNT R 5 .   ? -17.922 -9.892  16.364  0.75 24.38 ? 901  PNT B C6    1 
HETATM 11668 C  C7    . PNT R 5 .   ? -19.408 -8.815  13.685  0.75 27.59 ? 901  PNT B C7    1 
HETATM 11669 C  C8    . PNT R 5 .   ? -17.954 -8.460  13.559  0.75 28.14 ? 901  PNT B C8    1 
HETATM 11670 C  C9    . PNT R 5 .   ? -18.080 -11.214 19.877  0.75 25.12 ? 901  PNT B C9    1 
HETATM 11671 C  C10   . PNT R 5 .   ? -17.532 -7.343  14.507  0.75 28.73 ? 901  PNT B C10   1 
HETATM 11672 C  "C1'" . PNT R 5 .   ? -14.244 -5.128  15.683  0.75 29.00 ? 901  PNT B "C1'" 1 
HETATM 11673 C  "C2'" . PNT R 5 .   ? -13.053 -5.816  15.956  0.75 28.45 ? 901  PNT B "C2'" 1 
HETATM 11674 C  "C3'" . PNT R 5 .   ? -12.069 -5.236  16.762  0.75 28.60 ? 901  PNT B "C3'" 1 
HETATM 11675 C  "C4'" . PNT R 5 .   ? -12.262 -3.963  17.291  0.75 27.94 ? 901  PNT B "C4'" 1 
HETATM 11676 C  "C5'" . PNT R 5 .   ? -13.439 -3.277  17.013  0.75 28.51 ? 901  PNT B "C5'" 1 
HETATM 11677 C  "C6'" . PNT R 5 .   ? -14.426 -3.847  16.217  0.75 28.50 ? 901  PNT B "C6'" 1 
HETATM 11678 C  "C7'" . PNT R 5 .   ? -16.465 -5.090  14.628  0.75 28.89 ? 901  PNT B "C7'" 1 
HETATM 11679 C  "C8'" . PNT R 5 .   ? -17.342 -6.010  13.794  0.75 28.80 ? 901  PNT B "C8'" 1 
HETATM 11680 C  "C9'" . PNT R 5 .   ? -11.225 -3.306  18.161  0.75 27.93 ? 901  PNT B "C9'" 1 
HETATM 11681 O  O1    . PNT R 5 .   ? -19.793 -9.680  14.760  0.75 26.50 ? 901  PNT B O1    1 
HETATM 11682 O  "O1'" . PNT R 5 .   ? -15.209 -5.716  14.898  0.75 27.62 ? 901  PNT B "O1'" 1 
HETATM 11683 N  N1    . PNT R 5 .   ? -18.851 -11.103 20.863  0.75 25.42 ? 901  PNT B N1    1 
HETATM 11684 N  N2    . PNT R 5 .   ? -16.879 -11.754 20.034  0.75 27.90 ? 901  PNT B N2    1 
HETATM 11685 N  "N1'" . PNT R 5 .   ? -10.724 -3.960  19.115  0.75 28.69 ? 901  PNT B "N1'" 1 
HETATM 11686 N  "N2'" . PNT R 5 .   ? -10.854 -2.040  17.956  0.75 25.25 ? 901  PNT B "N2'" 1 
HETATM 11687 C  C1    . NAG S 6 .   ? 7.579   -14.549 9.394   1.00 31.43 ? 1101 NAG B C1    1 
HETATM 11688 C  C2    . NAG S 6 .   ? 8.735   -15.526 9.575   1.00 33.61 ? 1101 NAG B C2    1 
HETATM 11689 C  C3    . NAG S 6 .   ? 10.089  -14.825 9.715   1.00 34.42 ? 1101 NAG B C3    1 
HETATM 11690 C  C4    . NAG S 6 .   ? 10.225  -13.537 8.901   1.00 34.30 ? 1101 NAG B C4    1 
HETATM 11691 C  C5    . NAG S 6 .   ? 8.937   -12.731 8.851   1.00 33.84 ? 1101 NAG B C5    1 
HETATM 11692 C  C6    . NAG S 6 .   ? 9.096   -11.537 7.909   1.00 34.03 ? 1101 NAG B C6    1 
HETATM 11693 C  C7    . NAG S 6 .   ? 8.387   -17.592 10.799  1.00 36.31 ? 1101 NAG B C7    1 
HETATM 11694 C  C8    . NAG S 6 .   ? 8.168   -18.309 12.096  1.00 36.33 ? 1101 NAG B C8    1 
HETATM 11695 N  N2    . NAG S 6 .   ? 8.520   -16.282 10.806  1.00 34.81 ? 1101 NAG B N2    1 
HETATM 11696 O  O3    . NAG S 6 .   ? 11.109  -15.755 9.398   1.00 32.65 ? 1101 NAG B O3    1 
HETATM 11697 O  O4    . NAG S 6 .   ? 11.164  -12.700 9.534   1.00 36.42 ? 1101 NAG B O4    1 
HETATM 11698 O  O5    . NAG S 6 .   ? 7.879   -13.562 8.434   1.00 33.12 ? 1101 NAG B O5    1 
HETATM 11699 O  O6    . NAG S 6 .   ? 9.164   -11.964 6.566   1.00 32.74 ? 1101 NAG B O6    1 
HETATM 11700 O  O7    . NAG S 6 .   ? 8.432   -18.215 9.753   1.00 39.23 ? 1101 NAG B O7    1 
HETATM 11701 C  C1    . NAG T 6 .   ? 12.360  -12.553 8.754   1.00 39.38 ? 1102 NAG B C1    1 
HETATM 11702 C  C2    . NAG T 6 .   ? 13.166  -11.403 9.340   1.00 39.65 ? 1102 NAG B C2    1 
HETATM 11703 C  C3    . NAG T 6 .   ? 14.533  -11.260 8.679   1.00 41.45 ? 1102 NAG B C3    1 
HETATM 11704 C  C4    . NAG T 6 .   ? 15.235  -12.601 8.519   1.00 42.37 ? 1102 NAG B C4    1 
HETATM 11705 C  C5    . NAG T 6 .   ? 14.277  -13.642 7.937   1.00 43.05 ? 1102 NAG B C5    1 
HETATM 11706 C  C6    . NAG T 6 .   ? 14.928  -15.018 7.785   1.00 43.75 ? 1102 NAG B C6    1 
HETATM 11707 C  C7    . NAG T 6 .   ? 11.962  -9.522  10.304  1.00 38.98 ? 1102 NAG B C7    1 
HETATM 11708 C  C8    . NAG T 6 .   ? 11.216  -8.244  10.065  1.00 38.67 ? 1102 NAG B C8    1 
HETATM 11709 N  N2    . NAG T 6 .   ? 12.430  -10.155 9.234   1.00 38.58 ? 1102 NAG B N2    1 
HETATM 11710 O  O3    . NAG T 6 .   ? 15.330  -10.397 9.463   1.00 42.01 ? 1102 NAG B O3    1 
HETATM 11711 O  O4    . NAG T 6 .   ? 16.325  -12.408 7.644   1.00 44.06 ? 1102 NAG B O4    1 
HETATM 11712 O  O5    . NAG T 6 .   ? 13.136  -13.737 8.769   1.00 40.89 ? 1102 NAG B O5    1 
HETATM 11713 O  O6    . NAG T 6 .   ? 14.783  -15.778 8.967   1.00 45.63 ? 1102 NAG B O6    1 
HETATM 11714 O  O7    . NAG T 6 .   ? 12.104  -9.942  11.454  1.00 39.73 ? 1102 NAG B O7    1 
HETATM 11715 C  C1    . NAG U 6 .   ? -22.617 -39.830 68.022  1.00 31.93 ? 5381 NAG B C1    1 
HETATM 11716 C  C2    . NAG U 6 .   ? -23.692 -40.420 67.119  1.00 32.98 ? 5381 NAG B C2    1 
HETATM 11717 C  C3    . NAG U 6 .   ? -24.629 -41.323 67.911  1.00 34.46 ? 5381 NAG B C3    1 
HETATM 11718 C  C4    . NAG U 6 .   ? -23.865 -42.373 68.708  1.00 35.64 ? 5381 NAG B C4    1 
HETATM 11719 C  C5    . NAG U 6 .   ? -22.783 -41.684 69.529  1.00 35.08 ? 5381 NAG B C5    1 
HETATM 11720 C  C6    . NAG U 6 .   ? -21.901 -42.699 70.254  1.00 34.93 ? 5381 NAG B C6    1 
HETATM 11721 C  C7    . NAG U 6 .   ? -24.169 -38.905 65.255  1.00 31.34 ? 5381 NAG B C7    1 
HETATM 11722 C  C8    . NAG U 6 .   ? -25.077 -37.854 64.670  1.00 30.08 ? 5381 NAG B C8    1 
HETATM 11723 N  N2    . NAG U 6 .   ? -24.479 -39.392 66.451  1.00 32.00 ? 5381 NAG B N2    1 
HETATM 11724 O  O3    . NAG U 6 .   ? -25.508 -41.943 67.009  1.00 33.01 ? 5381 NAG B O3    1 
HETATM 11725 O  O4    . NAG U 6 .   ? -24.764 -42.962 69.628  1.00 39.31 ? 5381 NAG B O4    1 
HETATM 11726 O  O5    . NAG U 6 .   ? -21.967 -40.886 68.706  1.00 32.25 ? 5381 NAG B O5    1 
HETATM 11727 O  O6    . NAG U 6 .   ? -21.209 -43.452 69.288  1.00 35.72 ? 5381 NAG B O6    1 
HETATM 11728 O  O7    . NAG U 6 .   ? -23.181 -39.269 64.636  1.00 30.56 ? 5381 NAG B O7    1 
HETATM 11729 C  C1    . NAG V 6 .   ? -24.860 -44.393 69.561  1.00 42.24 ? 5382 NAG B C1    1 
HETATM 11730 C  C2    . NAG V 6 .   ? -25.346 -44.909 70.921  1.00 44.00 ? 5382 NAG B C2    1 
HETATM 11731 C  C3    . NAG V 6 .   ? -25.788 -46.369 70.877  1.00 45.04 ? 5382 NAG B C3    1 
HETATM 11732 C  C4    . NAG V 6 .   ? -26.752 -46.580 69.723  1.00 45.23 ? 5382 NAG B C4    1 
HETATM 11733 C  C5    . NAG V 6 .   ? -26.071 -46.117 68.441  1.00 45.01 ? 5382 NAG B C5    1 
HETATM 11734 C  C6    . NAG V 6 .   ? -26.992 -46.288 67.241  1.00 44.85 ? 5382 NAG B C6    1 
HETATM 11735 C  C7    . NAG V 6 .   ? -24.303 -43.755 72.825  1.00 45.55 ? 5382 NAG B C7    1 
HETATM 11736 C  C8    . NAG V 6 .   ? -23.151 -43.746 73.791  1.00 46.34 ? 5382 NAG B C8    1 
HETATM 11737 N  N2    . NAG V 6 .   ? -24.313 -44.751 71.932  1.00 44.32 ? 5382 NAG B N2    1 
HETATM 11738 O  O3    . NAG V 6 .   ? -26.429 -46.700 72.089  1.00 45.51 ? 5382 NAG B O3    1 
HETATM 11739 O  O4    . NAG V 6 .   ? -27.146 -47.935 69.650  1.00 45.79 ? 5382 NAG B O4    1 
HETATM 11740 O  O5    . NAG V 6 .   ? -25.757 -44.737 68.541  1.00 43.41 ? 5382 NAG B O5    1 
HETATM 11741 O  O6    . NAG V 6 .   ? -28.088 -45.414 67.403  1.00 45.19 ? 5382 NAG B O6    1 
HETATM 11742 O  O7    . NAG V 6 .   ? -25.155 -42.870 72.892  1.00 45.32 ? 5382 NAG B O7    1 
HETATM 11743 C  C1    . NAG W 6 .   ? -16.279 15.464  19.322  1.00 34.62 ? 7451 NAG B C1    1 
HETATM 11744 C  C2    . NAG W 6 .   ? -17.144 16.543  18.679  1.00 36.13 ? 7451 NAG B C2    1 
HETATM 11745 C  C3    . NAG W 6 .   ? -16.378 17.366  17.649  1.00 36.97 ? 7451 NAG B C3    1 
HETATM 11746 C  C4    . NAG W 6 .   ? -15.039 17.826  18.199  1.00 37.46 ? 7451 NAG B C4    1 
HETATM 11747 C  C5    . NAG W 6 .   ? -14.286 16.589  18.674  1.00 38.28 ? 7451 NAG B C5    1 
HETATM 11748 C  C6    . NAG W 6 .   ? -12.892 16.900  19.214  1.00 38.50 ? 7451 NAG B C6    1 
HETATM 11749 C  C7    . NAG W 6 .   ? -19.517 15.941  18.500  1.00 36.15 ? 7451 NAG B C7    1 
HETATM 11750 C  C8    . NAG W 6 .   ? -20.544 15.241  17.655  1.00 36.54 ? 7451 NAG B C8    1 
HETATM 11751 N  N2    . NAG W 6 .   ? -18.273 15.925  18.025  1.00 35.24 ? 7451 NAG B N2    1 
HETATM 11752 O  O3    . NAG W 6 .   ? -17.171 18.467  17.294  1.00 36.92 ? 7451 NAG B O3    1 
HETATM 11753 O  O4    . NAG W 6 .   ? -14.311 18.473  17.173  1.00 39.35 ? 7451 NAG B O4    1 
HETATM 11754 O  O5    . NAG W 6 .   ? -15.028 15.981  19.707  1.00 35.95 ? 7451 NAG B O5    1 
HETATM 11755 O  O6    . NAG W 6 .   ? -13.001 17.890  20.215  1.00 41.67 ? 7451 NAG B O6    1 
HETATM 11756 O  O7    . NAG W 6 .   ? -19.855 16.480  19.549  1.00 36.24 ? 7451 NAG B O7    1 
HETATM 11757 C  C1    . NAG X 6 .   ? -14.070 19.874  17.420  0.50 38.76 ? 7452 NAG B C1    1 
HETATM 11758 C  C2    . NAG X 6 .   ? -12.906 20.311  16.536  0.50 38.69 ? 7452 NAG B C2    1 
HETATM 11759 C  C3    . NAG X 6 .   ? -12.728 21.820  16.438  0.50 38.97 ? 7452 NAG B C3    1 
HETATM 11760 C  C4    . NAG X 6 .   ? -14.071 22.484  16.218  0.50 39.41 ? 7452 NAG B C4    1 
HETATM 11761 C  C5    . NAG X 6 .   ? -15.006 22.026  17.321  0.50 39.35 ? 7452 NAG B C5    1 
HETATM 11762 C  C6    . NAG X 6 .   ? -16.332 22.770  17.250  0.50 39.19 ? 7452 NAG B C6    1 
HETATM 11763 C  C7    . NAG X 6 .   ? -11.179 18.656  16.432  0.50 37.73 ? 7452 NAG B C7    1 
HETATM 11764 C  C8    . NAG X 6 .   ? -9.906  18.099  17.000  0.50 37.28 ? 7452 NAG B C8    1 
HETATM 11765 N  N2    . NAG X 6 .   ? -11.681 19.722  17.028  0.50 37.80 ? 7452 NAG B N2    1 
HETATM 11766 O  O3    . NAG X 6 .   ? -11.873 22.124  15.358  0.50 39.29 ? 7452 NAG B O3    1 
HETATM 11767 O  O4    . NAG X 6 .   ? -13.921 23.884  16.254  0.50 40.57 ? 7452 NAG B O4    1 
HETATM 11768 O  O5    . NAG X 6 .   ? -15.219 20.642  17.151  0.50 39.28 ? 7452 NAG B O5    1 
HETATM 11769 O  O6    . NAG X 6 .   ? -16.672 22.973  15.898  0.50 39.12 ? 7452 NAG B O6    1 
HETATM 11770 O  O7    . NAG X 6 .   ? -11.731 18.138  15.462  0.50 37.37 ? 7452 NAG B O7    1 
HETATM 11771 O  O     . HOH Y 8 .   ? -11.625 -10.227 75.588  1.00 20.79 ? 2    HOH A O     1 
HETATM 11772 O  O     . HOH Y 8 .   ? -48.524 -17.545 51.575  1.00 16.37 ? 6    HOH A O     1 
HETATM 11773 O  O     . HOH Y 8 .   ? -40.195 -29.953 47.567  1.00 17.38 ? 7    HOH A O     1 
HETATM 11774 O  O     . HOH Y 8 .   ? -30.714 -29.189 58.875  1.00 18.46 ? 8    HOH A O     1 
HETATM 11775 O  O     . HOH Y 8 .   ? -26.896 -26.847 32.990  1.00 26.54 ? 9    HOH A O     1 
HETATM 11776 O  O     . HOH Y 8 .   ? -30.104 13.975  68.422  1.00 45.33 ? 11   HOH A O     1 
HETATM 11777 O  O     . HOH Y 8 .   ? -37.594 -28.544 61.183  1.00 16.99 ? 12   HOH A O     1 
HETATM 11778 O  O     . HOH Y 8 .   ? -53.360 -17.023 56.329  1.00 17.85 ? 13   HOH A O     1 
HETATM 11779 O  O     . HOH Y 8 .   ? -39.907 -15.855 24.841  1.00 21.69 ? 14   HOH A O     1 
HETATM 11780 O  O     . HOH Y 8 .   ? -39.721 -9.371  22.139  1.00 16.83 ? 16   HOH A O     1 
HETATM 11781 O  O     . HOH Y 8 .   ? -44.293 6.301   60.444  1.00 28.18 ? 19   HOH A O     1 
HETATM 11782 O  O     . HOH Y 8 .   ? -48.572 -20.868 42.939  1.00 15.41 ? 20   HOH A O     1 
HETATM 11783 O  O     . HOH Y 8 .   ? -20.771 -14.893 65.912  1.00 16.67 ? 752  HOH A O     1 
HETATM 11784 O  O     . HOH Y 8 .   ? -4.751  -20.473 82.079  1.00 45.46 ? 753  HOH A O     1 
HETATM 11785 O  O     . HOH Y 8 .   ? -8.018  -25.355 78.705  1.00 48.91 ? 754  HOH A O     1 
HETATM 11786 O  O     . HOH Y 8 .   ? -42.053 -26.059 85.112  1.00 56.72 ? 755  HOH A O     1 
HETATM 11787 O  O     . HOH Y 8 .   ? -25.315 11.233  10.880  1.00 50.82 ? 756  HOH A O     1 
HETATM 11788 O  O     . HOH Y 8 .   ? -32.236 15.927  49.324  1.00 16.18 ? 757  HOH A O     1 
HETATM 11789 O  O     . HOH Y 8 .   ? -47.533 -29.182 51.570  1.00 16.07 ? 758  HOH A O     1 
HETATM 11790 O  O     . HOH Y 8 .   ? -47.149 -25.681 52.145  1.00 16.63 ? 759  HOH A O     1 
HETATM 11791 O  O     . HOH Y 8 .   ? -24.751 -18.786 44.952  1.00 46.99 ? 760  HOH A O     1 
HETATM 11792 O  O     . HOH Y 8 .   ? -27.999 -0.126  14.811  1.00 22.38 ? 761  HOH A O     1 
HETATM 11793 O  O     . HOH Y 8 .   ? -35.357 12.194  57.888  1.00 37.23 ? 762  HOH A O     1 
HETATM 11794 O  O     . HOH Y 8 .   ? -44.281 -18.163 66.328  1.00 20.72 ? 763  HOH A O     1 
HETATM 11795 O  O     . HOH Y 8 .   ? -34.054 17.211  25.482  1.00 40.83 ? 764  HOH A O     1 
HETATM 11796 O  O     . HOH Y 8 .   ? -5.793  4.996   69.578  1.00 41.36 ? 765  HOH A O     1 
HETATM 11797 O  O     . HOH Y 8 .   ? -34.948 13.922  42.841  1.00 17.56 ? 766  HOH A O     1 
HETATM 11798 O  O     . HOH Y 8 .   ? -54.595 -11.101 39.218  1.00 49.90 ? 767  HOH A O     1 
HETATM 11799 O  O     . HOH Y 8 .   ? -17.173 -8.540  66.573  1.00 14.59 ? 768  HOH A O     1 
HETATM 11800 O  O     . HOH Y 8 .   ? -64.521 -11.040 83.544  1.00 46.74 ? 769  HOH A O     1 
HETATM 11801 O  O     . HOH Y 8 .   ? -48.508 -5.488  66.320  1.00 32.95 ? 770  HOH A O     1 
HETATM 11802 O  O     . HOH Y 8 .   ? -55.217 -22.262 71.520  1.00 45.83 ? 771  HOH A O     1 
HETATM 11803 O  O     . HOH Y 8 .   ? -37.134 1.787   66.304  1.00 17.52 ? 772  HOH A O     1 
HETATM 11804 O  O     . HOH Y 8 .   ? -26.787 -11.425 48.523  1.00 36.22 ? 773  HOH A O     1 
HETATM 11805 O  O     . HOH Y 8 .   ? -22.106 -11.042 49.905  1.00 38.70 ? 774  HOH A O     1 
HETATM 11806 O  O     . HOH Y 8 .   ? -40.767 -0.647  37.167  1.00 16.19 ? 775  HOH A O     1 
HETATM 11807 O  O     . HOH Y 8 .   ? -45.234 8.234   51.924  1.00 13.95 ? 776  HOH A O     1 
HETATM 11808 O  O     . HOH Y 8 .   ? -47.512 -25.461 32.077  1.00 39.72 ? 777  HOH A O     1 
HETATM 11809 O  O     . HOH Y 8 .   ? -26.899 4.210   38.760  1.00 18.32 ? 778  HOH A O     1 
HETATM 11810 O  O     . HOH Y 8 .   ? -27.917 -22.707 77.372  1.00 22.57 ? 779  HOH A O     1 
HETATM 11811 O  O     . HOH Y 8 .   ? -35.974 7.710   48.034  1.00 18.24 ? 780  HOH A O     1 
HETATM 11812 O  O     . HOH Y 8 .   ? -34.188 -34.259 62.948  1.00 30.18 ? 781  HOH A O     1 
HETATM 11813 O  O     . HOH Y 8 .   ? -52.716 -16.581 58.948  1.00 19.83 ? 782  HOH A O     1 
HETATM 11814 O  O     . HOH Y 8 .   ? -44.466 -1.297  78.295  1.00 41.35 ? 783  HOH A O     1 
HETATM 11815 O  O     . HOH Y 8 .   ? -51.230 6.580   68.805  1.00 46.87 ? 784  HOH A O     1 
HETATM 11816 O  O     . HOH Y 8 .   ? -48.535 -39.581 49.661  1.00 14.12 ? 785  HOH A O     1 
HETATM 11817 O  O     . HOH Y 8 .   ? -66.153 -7.054  73.854  1.00 55.46 ? 786  HOH A O     1 
HETATM 11818 O  O     . HOH Y 8 .   ? -31.679 -2.539  64.895  1.00 16.67 ? 787  HOH A O     1 
HETATM 11819 O  O     . HOH Y 8 .   ? -41.611 -26.405 82.599  1.00 42.29 ? 788  HOH A O     1 
HETATM 11820 O  O     . HOH Y 8 .   ? -42.425 -22.946 27.357  1.00 32.66 ? 789  HOH A O     1 
HETATM 11821 O  O     . HOH Y 8 .   ? -26.532 9.333   50.655  1.00 18.46 ? 790  HOH A O     1 
HETATM 11822 O  O     . HOH Y 8 .   ? -44.269 -32.971 65.202  1.00 38.30 ? 791  HOH A O     1 
HETATM 11823 O  O     . HOH Y 8 .   ? -46.440 -27.508 82.926  1.00 31.62 ? 792  HOH A O     1 
HETATM 11824 O  O     . HOH Y 8 .   ? -42.414 8.325   50.977  1.00 15.52 ? 793  HOH A O     1 
HETATM 11825 O  O     . HOH Y 8 .   ? -52.053 -31.740 44.245  1.00 37.34 ? 794  HOH A O     1 
HETATM 11826 O  O     . HOH Y 8 .   ? -27.125 17.752  10.289  1.00 50.39 ? 795  HOH A O     1 
HETATM 11827 O  O     . HOH Y 8 .   ? -44.762 8.274   40.953  1.00 45.52 ? 796  HOH A O     1 
HETATM 11828 O  O     . HOH Y 8 .   ? -34.984 10.962  75.696  1.00 47.32 ? 797  HOH A O     1 
HETATM 11829 O  O     . HOH Y 8 .   ? -40.192 8.509   61.617  1.00 43.71 ? 798  HOH A O     1 
HETATM 11830 O  O     . HOH Y 8 .   ? -46.118 -12.187 27.945  1.00 26.45 ? 799  HOH A O     1 
HETATM 11831 O  O     . HOH Y 8 .   ? -5.818  -14.297 91.692  1.00 47.64 ? 800  HOH A O     1 
HETATM 11832 O  O     . HOH Y 8 .   ? -54.521 -21.801 47.119  1.00 33.85 ? 805  HOH A O     1 
HETATM 11833 O  O     . HOH Y 8 .   ? -46.552 4.537   55.485  1.00 23.63 ? 806  HOH A O     1 
HETATM 11834 O  O     . HOH Y 8 .   ? -28.271 -22.093 50.027  1.00 21.01 ? 807  HOH A O     1 
HETATM 11835 O  O     . HOH Y 8 .   ? -45.085 -23.371 25.374  1.00 42.15 ? 808  HOH A O     1 
HETATM 11836 O  O     . HOH Y 8 .   ? -40.938 -7.284  21.218  1.00 20.46 ? 809  HOH A O     1 
HETATM 11837 O  O     . HOH Y 8 .   ? -55.097 -0.891  59.093  1.00 50.37 ? 810  HOH A O     1 
HETATM 11838 O  O     . HOH Y 8 .   ? -36.619 -18.563 72.681  1.00 15.66 ? 811  HOH A O     1 
HETATM 11839 O  O     . HOH Y 8 .   ? -48.381 -3.870  39.099  1.00 16.63 ? 812  HOH A O     1 
HETATM 11840 O  O     . HOH Y 8 .   ? -34.571 -9.894  53.207  1.00 17.13 ? 813  HOH A O     1 
HETATM 11841 O  O     . HOH Y 8 .   ? -36.976 -8.733  59.070  1.00 27.76 ? 814  HOH A O     1 
HETATM 11842 O  O     . HOH Y 8 .   ? -16.286 -7.085  55.079  1.00 19.70 ? 815  HOH A O     1 
HETATM 11843 O  O     . HOH Y 8 .   ? -52.134 -5.021  48.172  1.00 20.88 ? 816  HOH A O     1 
HETATM 11844 O  O     . HOH Y 8 .   ? -47.932 -31.440 53.382  1.00 16.23 ? 817  HOH A O     1 
HETATM 11845 O  O     . HOH Y 8 .   ? -33.607 -4.089  72.443  1.00 31.47 ? 818  HOH A O     1 
HETATM 11846 O  O     . HOH Y 8 .   ? -46.619 -6.433  68.128  1.00 17.74 ? 819  HOH A O     1 
HETATM 11847 O  O     . HOH Y 8 .   ? -8.269  -7.449  67.669  1.00 23.13 ? 820  HOH A O     1 
HETATM 11848 O  O     . HOH Y 8 .   ? -42.042 -12.842 58.587  1.00 21.92 ? 821  HOH A O     1 
HETATM 11849 O  O     . HOH Y 8 .   ? -47.069 -33.869 54.714  1.00 23.40 ? 822  HOH A O     1 
HETATM 11850 O  O     . HOH Y 8 .   ? -8.545  -7.403  87.252  1.00 42.97 ? 823  HOH A O     1 
HETATM 11851 O  O     . HOH Y 8 .   ? -23.269 3.860   87.917  1.00 48.90 ? 824  HOH A O     1 
HETATM 11852 O  O     . HOH Y 8 .   ? -43.294 10.598  39.851  1.00 44.13 ? 825  HOH A O     1 
HETATM 11853 O  O     . HOH Y 8 .   ? -42.111 12.506  42.427  1.00 43.46 ? 826  HOH A O     1 
HETATM 11854 O  O     . HOH Y 8 .   ? -6.702  -13.299 64.683  1.00 18.91 ? 827  HOH A O     1 
HETATM 11855 O  O     . HOH Y 8 .   ? -28.090 13.080  31.681  1.00 45.65 ? 828  HOH A O     1 
HETATM 11856 O  O     . HOH Y 8 .   ? -29.911 9.820   33.154  1.00 51.82 ? 829  HOH A O     1 
HETATM 11857 O  O     . HOH Y 8 .   ? -53.329 4.007   66.766  1.00 25.55 ? 830  HOH A O     1 
HETATM 11858 O  O     . HOH Y 8 .   ? -40.694 6.294   71.149  1.00 38.04 ? 831  HOH A O     1 
HETATM 11859 O  O     . HOH Y 8 .   ? -42.735 -27.300 80.282  1.00 24.59 ? 832  HOH A O     1 
HETATM 11860 O  O     . HOH Y 8 .   ? -45.828 -1.368  59.942  1.00 53.10 ? 833  HOH A O     1 
HETATM 11861 O  O     . HOH Y 8 .   ? -34.958 -1.322  62.169  1.00 14.70 ? 834  HOH A O     1 
HETATM 11862 O  O     . HOH Y 8 .   ? -52.724 2.062   52.049  1.00 51.84 ? 835  HOH A O     1 
HETATM 11863 O  O     . HOH Y 8 .   ? -49.221 -25.189 35.860  1.00 31.17 ? 836  HOH A O     1 
HETATM 11864 O  O     . HOH Y 8 .   ? -38.852 -21.472 97.824  1.00 42.73 ? 837  HOH A O     1 
HETATM 11865 O  O     . HOH Y 8 .   ? -44.738 -28.771 38.691  1.00 17.41 ? 838  HOH A O     1 
HETATM 11866 O  O     . HOH Y 8 .   ? -37.265 -27.421 76.509  1.00 23.88 ? 839  HOH A O     1 
HETATM 11867 O  O     . HOH Y 8 .   ? -41.939 -3.859  20.486  1.00 28.80 ? 840  HOH A O     1 
HETATM 11868 O  O     . HOH Y 8 .   ? -26.889 18.778  28.619  1.00 34.69 ? 841  HOH A O     1 
HETATM 11869 O  O     . HOH Y 8 .   ? -53.499 -14.879 53.428  1.00 27.54 ? 842  HOH A O     1 
HETATM 11870 O  O     . HOH Y 8 .   ? -42.043 -32.079 67.004  1.00 27.55 ? 843  HOH A O     1 
HETATM 11871 O  O     . HOH Y 8 .   ? -33.110 -35.290 73.613  1.00 39.55 ? 844  HOH A O     1 
HETATM 11872 O  O     . HOH Y 8 .   ? -21.094 -3.374  52.252  1.00 19.07 ? 845  HOH A O     1 
HETATM 11873 O  O     . HOH Y 8 .   ? -34.421 -36.134 70.637  1.00 44.28 ? 846  HOH A O     1 
HETATM 11874 O  O     . HOH Y 8 .   ? -61.658 -6.960  44.158  1.00 42.05 ? 847  HOH A O     1 
HETATM 11875 O  O     . HOH Y 8 .   ? -14.744 -33.119 14.124  1.00 28.96 ? 848  HOH A O     1 
HETATM 11876 O  O     . HOH Y 8 .   ? -18.392 -15.977 66.557  1.00 20.71 ? 849  HOH A O     1 
HETATM 11877 O  O     . HOH Y 8 .   ? -15.357 -14.151 86.393  1.00 23.71 ? 850  HOH A O     1 
HETATM 11878 O  O     . HOH Y 8 .   ? -33.407 -32.137 38.717  1.00 37.96 ? 851  HOH A O     1 
HETATM 11879 O  O     . HOH Y 8 .   ? -42.909 -4.367  72.691  1.00 19.43 ? 852  HOH A O     1 
HETATM 11880 O  O     . HOH Y 8 .   ? -35.989 -24.711 51.851  1.00 17.77 ? 853  HOH A O     1 
HETATM 11881 O  O     . HOH Y 8 .   ? -28.926 -34.073 73.768  1.00 52.05 ? 854  HOH A O     1 
HETATM 11882 O  O     . HOH Y 8 .   ? -18.229 -13.131 75.510  1.00 21.71 ? 855  HOH A O     1 
HETATM 11883 O  O     . HOH Y 8 .   ? -45.546 1.184   59.302  1.00 42.26 ? 856  HOH A O     1 
HETATM 11884 O  O     . HOH Y 8 .   ? -58.532 -20.256 82.994  1.00 51.31 ? 857  HOH A O     1 
HETATM 11885 O  O     . HOH Y 8 .   ? -46.700 -23.672 60.000  1.00 17.28 ? 858  HOH A O     1 
HETATM 11886 O  O     . HOH Y 8 .   ? -19.797 -26.166 53.479  1.00 50.89 ? 859  HOH A O     1 
HETATM 11887 O  O     . HOH Y 8 .   ? -53.041 -31.375 37.702  1.00 45.26 ? 860  HOH A O     1 
HETATM 11888 O  O     . HOH Y 8 .   ? -53.397 -18.707 60.494  1.00 26.52 ? 861  HOH A O     1 
HETATM 11889 O  O     . HOH Y 8 .   ? -38.693 7.800   70.661  1.00 51.57 ? 862  HOH A O     1 
HETATM 11890 O  O     . HOH Y 8 .   ? -49.326 -13.857 24.928  1.00 41.23 ? 863  HOH A O     1 
HETATM 11891 O  O     . HOH Y 8 .   ? -49.406 4.036   58.430  1.00 32.72 ? 864  HOH A O     1 
HETATM 11892 O  O     . HOH Y 8 .   ? -49.833 1.476   57.621  1.00 54.02 ? 865  HOH A O     1 
HETATM 11893 O  O     . HOH Y 8 .   ? -50.752 -0.166  60.797  1.00 44.43 ? 866  HOH A O     1 
HETATM 11894 O  O     . HOH Y 8 .   ? -32.511 -33.888 46.895  1.00 37.55 ? 867  HOH A O     1 
HETATM 11895 O  O     . HOH Y 8 .   ? -16.026 -8.328  58.384  1.00 35.71 ? 868  HOH A O     1 
HETATM 11896 O  O     . HOH Y 8 .   ? -21.904 -23.117 95.804  1.00 40.03 ? 869  HOH A O     1 
HETATM 11897 O  O     . HOH Y 8 .   ? -24.701 3.306   54.368  1.00 21.54 ? 870  HOH A O     1 
HETATM 11898 O  O     . HOH Y 8 .   ? -7.986  0.996   70.623  1.00 38.05 ? 871  HOH A O     1 
HETATM 11899 O  O     . HOH Y 8 .   ? -21.410 -1.735  18.597  1.00 27.73 ? 872  HOH A O     1 
HETATM 11900 O  O     . HOH Y 8 .   ? -57.090 -21.548 63.691  1.00 47.75 ? 873  HOH A O     1 
HETATM 11901 O  O     . HOH Y 8 .   ? -62.440 -20.917 83.798  1.00 56.54 ? 874  HOH A O     1 
HETATM 11902 O  O     . HOH Y 8 .   ? -41.740 -20.736 21.030  1.00 16.75 ? 875  HOH A O     1 
HETATM 11903 O  O     . HOH Y 8 .   ? -35.162 10.362  29.091  1.00 21.78 ? 876  HOH A O     1 
HETATM 11904 O  O     . HOH Y 8 .   ? -10.511 -4.154  86.124  1.00 36.76 ? 877  HOH A O     1 
HETATM 11905 O  O     . HOH Y 8 .   ? -38.424 -20.668 72.383  1.00 20.56 ? 878  HOH A O     1 
HETATM 11906 O  O     . HOH Y 8 .   ? -56.633 -20.127 52.234  1.00 23.66 ? 879  HOH A O     1 
HETATM 11907 O  O     . HOH Y 8 .   ? -48.238 -23.134 52.828  1.00 16.66 ? 880  HOH A O     1 
HETATM 11908 O  O     . HOH Y 8 .   ? -30.640 -34.413 53.660  1.00 41.43 ? 881  HOH A O     1 
HETATM 11909 O  O     . HOH Y 8 .   ? -34.968 -6.476  31.523  1.00 17.49 ? 882  HOH A O     1 
HETATM 11910 O  O     . HOH Y 8 .   ? -46.851 -31.889 58.251  1.00 51.10 ? 883  HOH A O     1 
HETATM 11911 O  O     . HOH Y 8 .   ? -36.333 -35.150 39.723  1.00 40.83 ? 884  HOH A O     1 
HETATM 11912 O  O     . HOH Y 8 .   ? -27.418 -14.526 65.691  1.00 35.02 ? 885  HOH A O     1 
HETATM 11913 O  O     . HOH Y 8 .   ? -47.286 -29.044 34.877  1.00 35.18 ? 886  HOH A O     1 
HETATM 11914 O  O     . HOH Y 8 .   ? -35.185 4.554   69.264  1.00 23.54 ? 887  HOH A O     1 
HETATM 11915 O  O     . HOH Y 8 .   ? -37.724 8.922   50.226  1.00 19.44 ? 888  HOH A O     1 
HETATM 11916 O  O     . HOH Y 8 .   ? -59.687 -15.479 57.104  1.00 27.64 ? 889  HOH A O     1 
HETATM 11917 O  O     . HOH Y 8 .   ? -21.304 -24.329 61.981  1.00 33.80 ? 890  HOH A O     1 
HETATM 11918 O  O     . HOH Y 8 .   ? -34.305 -25.255 75.700  1.00 27.33 ? 891  HOH A O     1 
HETATM 11919 O  O     . HOH Y 8 .   ? -31.801 -0.517  37.666  1.00 17.31 ? 892  HOH A O     1 
HETATM 11920 O  O     . HOH Y 8 .   ? -50.226 -4.961  45.125  1.00 24.80 ? 893  HOH A O     1 
HETATM 11921 O  O     . HOH Y 8 .   ? -16.578 -21.923 73.476  1.00 23.18 ? 894  HOH A O     1 
HETATM 11922 O  O     . HOH Y 8 .   ? -54.674 -20.053 38.692  1.00 40.46 ? 895  HOH A O     1 
HETATM 11923 O  O     . HOH Y 8 .   ? -37.895 13.093  22.968  1.00 39.52 ? 896  HOH A O     1 
HETATM 11924 O  O     . HOH Y 8 .   ? -26.216 -30.071 74.109  1.00 34.84 ? 897  HOH A O     1 
HETATM 11925 O  O     . HOH Y 8 .   ? -37.082 2.662   27.632  1.00 27.61 ? 898  HOH A O     1 
HETATM 11926 O  O     . HOH Y 8 .   ? -49.087 -30.510 57.186  1.00 31.12 ? 899  HOH A O     1 
HETATM 11927 O  O     . HOH Y 8 .   ? -13.978 -15.959 96.244  1.00 27.57 ? 900  HOH A O     1 
HETATM 11928 O  O     . HOH Y 8 .   ? -50.275 3.395   65.355  1.00 24.82 ? 902  HOH A O     1 
HETATM 11929 O  O     . HOH Y 8 .   ? -26.584 -24.150 40.487  1.00 45.10 ? 903  HOH A O     1 
HETATM 11930 O  O     . HOH Y 8 .   ? -15.927 0.062   17.436  1.00 23.54 ? 904  HOH A O     1 
HETATM 11931 O  O     . HOH Y 8 .   ? -56.130 -28.286 44.548  1.00 60.88 ? 905  HOH A O     1 
HETATM 11932 O  O     . HOH Y 8 .   ? -37.279 22.036  38.749  1.00 46.98 ? 906  HOH A O     1 
HETATM 11933 O  O     . HOH Y 8 .   ? -27.860 6.607   13.569  1.00 27.60 ? 907  HOH A O     1 
HETATM 11934 O  O     . HOH Y 8 .   ? -38.704 5.406   35.321  1.00 30.26 ? 908  HOH A O     1 
HETATM 11935 O  O     . HOH Y 8 .   ? -37.309 -20.063 67.129  1.00 15.84 ? 909  HOH A O     1 
HETATM 11936 O  O     . HOH Y 8 .   ? -22.783 -27.522 76.046  1.00 21.50 ? 910  HOH A O     1 
HETATM 11937 O  O     . HOH Y 8 .   ? -55.635 -24.752 53.110  1.00 27.97 ? 911  HOH A O     1 
HETATM 11938 O  O     . HOH Y 8 .   ? -39.258 -33.887 32.340  1.00 38.72 ? 912  HOH A O     1 
HETATM 11939 O  O     . HOH Y 8 .   ? -50.969 -19.305 36.437  1.00 31.61 ? 913  HOH A O     1 
HETATM 11940 O  O     . HOH Y 8 .   ? -50.248 -15.775 59.803  1.00 28.78 ? 914  HOH A O     1 
HETATM 11941 O  O     . HOH Y 8 .   ? -38.705 -28.024 85.671  1.00 54.52 ? 915  HOH A O     1 
HETATM 11942 O  O     . HOH Y 8 .   ? -35.004 -30.243 83.675  1.00 38.37 ? 916  HOH A O     1 
HETATM 11943 O  O     . HOH Y 8 .   ? -28.859 -19.996 94.219  1.00 47.25 ? 917  HOH A O     1 
HETATM 11944 O  O     . HOH Y 8 .   ? -52.619 -26.592 65.778  1.00 39.42 ? 918  HOH A O     1 
HETATM 11945 O  O     . HOH Y 8 .   ? -32.880 -31.378 85.155  1.00 49.68 ? 919  HOH A O     1 
HETATM 11946 O  O     . HOH Y 8 .   ? -7.642  7.056   68.734  1.00 43.02 ? 920  HOH A O     1 
HETATM 11947 O  O     . HOH Y 8 .   ? -28.320 -28.041 59.433  1.00 26.03 ? 921  HOH A O     1 
HETATM 11948 O  O     . HOH Y 8 .   ? -44.277 4.944   40.668  1.00 24.84 ? 922  HOH A O     1 
HETATM 11949 O  O     . HOH Y 8 .   ? -37.046 -8.904  76.484  1.00 45.62 ? 923  HOH A O     1 
HETATM 11950 O  O     . HOH Y 8 .   ? -33.276 -30.174 32.590  1.00 25.41 ? 924  HOH A O     1 
HETATM 11951 O  O     . HOH Y 8 .   ? -32.600 -28.969 34.680  1.00 29.21 ? 925  HOH A O     1 
HETATM 11952 O  O     . HOH Y 8 .   ? -40.797 -9.738  81.461  1.00 26.93 ? 926  HOH A O     1 
HETATM 11953 O  O     . HOH Y 8 .   ? -36.691 -8.302  32.817  1.00 18.21 ? 927  HOH A O     1 
HETATM 11954 O  O     . HOH Y 8 .   ? -16.583 -16.097 80.361  1.00 22.85 ? 928  HOH A O     1 
HETATM 11955 O  O     . HOH Y 8 .   ? -27.839 -26.859 56.897  1.00 22.59 ? 929  HOH A O     1 
HETATM 11956 O  O     . HOH Y 8 .   ? -0.654  -16.687 74.389  1.00 34.54 ? 930  HOH A O     1 
HETATM 11957 O  O     . HOH Y 8 .   ? -16.450 -33.368 5.563   1.00 35.38 ? 931  HOH A O     1 
HETATM 11958 O  O     . HOH Y 8 .   ? -40.619 -3.159  73.460  1.00 28.43 ? 932  HOH A O     1 
HETATM 11959 O  O     . HOH Y 8 .   ? -42.623 -35.428 36.052  1.00 44.59 ? 933  HOH A O     1 
HETATM 11960 O  O     . HOH Y 8 .   ? -15.371 -6.384  60.170  1.00 20.29 ? 934  HOH A O     1 
HETATM 11961 O  O     . HOH Y 8 .   ? -35.176 -34.218 68.153  1.00 26.95 ? 935  HOH A O     1 
HETATM 11962 O  O     . HOH Y 8 .   ? -36.879 -4.485  71.237  1.00 19.77 ? 936  HOH A O     1 
HETATM 11963 O  O     . HOH Y 8 .   ? -11.967 -7.899  79.382  1.00 33.39 ? 937  HOH A O     1 
HETATM 11964 O  O     . HOH Y 8 .   ? -49.780 -22.378 59.430  1.00 31.58 ? 938  HOH A O     1 
HETATM 11965 O  O     . HOH Y 8 .   ? -42.566 -38.804 51.308  1.00 28.14 ? 939  HOH A O     1 
HETATM 11966 O  O     . HOH Y 8 .   ? -49.206 -6.437  64.077  1.00 21.31 ? 940  HOH A O     1 
HETATM 11967 O  O     . HOH Y 8 .   ? -40.028 -15.892 80.149  1.00 23.12 ? 941  HOH A O     1 
HETATM 11968 O  O     . HOH Y 8 .   ? -27.308 -23.004 47.656  1.00 23.51 ? 942  HOH A O     1 
HETATM 11969 O  O     . HOH Y 8 .   ? -56.228 -7.835  58.393  1.00 17.94 ? 943  HOH A O     1 
HETATM 11970 O  O     . HOH Y 8 .   ? -52.353 -22.607 71.473  1.00 28.11 ? 944  HOH A O     1 
HETATM 11971 O  O     . HOH Y 8 .   ? -43.802 -2.312  30.912  1.00 32.82 ? 945  HOH A O     1 
HETATM 11972 O  O     . HOH Y 8 .   ? -47.687 -27.835 77.323  1.00 35.02 ? 946  HOH A O     1 
HETATM 11973 O  O     . HOH Y 8 .   ? -45.083 -26.196 70.605  1.00 38.49 ? 947  HOH A O     1 
HETATM 11974 O  O     . HOH Y 8 .   ? -47.291 0.504   39.769  1.00 23.44 ? 948  HOH A O     1 
HETATM 11975 O  O     . HOH Y 8 .   ? -49.447 3.438   47.378  1.00 23.58 ? 949  HOH A O     1 
HETATM 11976 O  O     . HOH Y 8 .   ? -36.255 9.509   65.988  1.00 31.61 ? 950  HOH A O     1 
HETATM 11977 O  O     . HOH Y 8 .   ? -59.460 -1.928  64.135  1.00 31.90 ? 951  HOH A O     1 
HETATM 11978 O  O     . HOH Y 8 .   ? -43.570 -26.119 33.270  1.00 29.44 ? 952  HOH A O     1 
HETATM 11979 O  O     . HOH Y 8 .   ? -20.153 16.897  14.262  1.00 44.29 ? 953  HOH A O     1 
HETATM 11980 O  O     . HOH Y 8 .   ? -57.473 -11.105 83.639  1.00 40.39 ? 954  HOH A O     1 
HETATM 11981 O  O     . HOH Y 8 .   ? -35.327 1.999   68.448  1.00 24.03 ? 955  HOH A O     1 
HETATM 11982 O  O     . HOH Y 8 .   ? -24.098 -39.026 13.940  1.00 57.14 ? 956  HOH A O     1 
HETATM 11983 O  O     . HOH Y 8 .   ? -27.543 -26.216 78.434  1.00 24.96 ? 957  HOH A O     1 
HETATM 11984 O  O     . HOH Y 8 .   ? -14.572 -29.337 6.018   1.00 30.05 ? 958  HOH A O     1 
HETATM 11985 O  O     . HOH Y 8 .   ? -32.400 -20.103 38.457  1.00 19.53 ? 959  HOH A O     1 
HETATM 11986 O  O     . HOH Y 8 .   ? -29.049 -31.400 52.703  1.00 25.17 ? 960  HOH A O     1 
HETATM 11987 O  O     . HOH Y 8 .   ? -43.234 -29.066 35.380  1.00 35.86 ? 961  HOH A O     1 
HETATM 11988 O  O     . HOH Y 8 .   ? -27.931 -15.977 61.136  1.00 24.03 ? 962  HOH A O     1 
HETATM 11989 O  O     . HOH Y 8 .   ? -36.605 -23.314 62.627  1.00 23.30 ? 963  HOH A O     1 
HETATM 11990 O  O     . HOH Y 8 .   ? -16.978 -29.826 13.078  1.00 31.86 ? 964  HOH A O     1 
HETATM 11991 O  O     . HOH Y 8 .   ? -39.799 -1.677  75.662  1.00 28.95 ? 965  HOH A O     1 
HETATM 11992 O  O     . HOH Y 8 .   ? -57.291 -13.835 60.804  1.00 25.72 ? 966  HOH A O     1 
HETATM 11993 O  O     . HOH Y 8 .   ? -33.348 18.514  29.145  1.00 28.48 ? 967  HOH A O     1 
HETATM 11994 O  O     . HOH Y 8 .   ? -28.913 -1.004  37.721  1.00 16.30 ? 968  HOH A O     1 
HETATM 11995 O  O     . HOH Y 8 .   ? -37.522 8.192   44.379  1.00 20.56 ? 969  HOH A O     1 
HETATM 11996 O  O     . HOH Y 8 .   ? -13.072 -27.723 78.963  1.00 37.32 ? 970  HOH A O     1 
HETATM 11997 O  O     . HOH Y 8 .   ? -51.299 -31.931 69.173  1.00 46.39 ? 971  HOH A O     1 
HETATM 11998 O  O     . HOH Y 8 .   ? -20.093 -2.164  84.634  1.00 24.39 ? 972  HOH A O     1 
HETATM 11999 O  O     . HOH Y 8 .   ? -21.272 -24.445 57.223  1.00 20.83 ? 973  HOH A O     1 
HETATM 12000 O  O     . HOH Y 8 .   ? -44.390 -5.100  30.134  1.00 35.14 ? 974  HOH A O     1 
HETATM 12001 O  O     . HOH Y 8 .   ? -40.071 0.671   76.227  1.00 27.04 ? 975  HOH A O     1 
HETATM 12002 O  O     . HOH Y 8 .   ? -36.875 -35.626 60.616  1.00 37.95 ? 976  HOH A O     1 
HETATM 12003 O  O     . HOH Y 8 .   ? -30.101 17.408  21.652  1.00 34.51 ? 977  HOH A O     1 
HETATM 12004 O  O     . HOH Y 8 .   ? -54.878 -22.535 64.569  1.00 36.74 ? 978  HOH A O     1 
HETATM 12005 O  O     . HOH Y 8 .   ? -48.889 -13.895 63.567  1.00 26.25 ? 979  HOH A O     1 
HETATM 12006 O  O     . HOH Y 8 .   ? -41.744 -41.386 51.148  1.00 28.79 ? 980  HOH A O     1 
HETATM 12007 O  O     . HOH Y 8 .   ? -61.631 -21.943 70.193  1.00 48.30 ? 981  HOH A O     1 
HETATM 12008 O  O     . HOH Y 8 .   ? -26.887 -22.141 93.301  1.00 39.69 ? 982  HOH A O     1 
HETATM 12009 O  O     . HOH Y 8 .   ? -40.601 -20.204 29.455  1.00 20.44 ? 983  HOH A O     1 
HETATM 12010 O  O     . HOH Y 8 .   ? -19.944 -12.117 72.233  1.00 21.25 ? 984  HOH A O     1 
HETATM 12011 O  O     . HOH Y 8 .   ? -34.572 15.107  23.681  1.00 26.65 ? 985  HOH A O     1 
HETATM 12012 O  O     . HOH Y 8 .   ? -48.233 -12.337 57.740  1.00 35.59 ? 986  HOH A O     1 
HETATM 12013 O  O     . HOH Y 8 .   ? -62.868 -7.231  61.133  1.00 30.03 ? 987  HOH A O     1 
HETATM 12014 O  O     . HOH Y 8 .   ? -16.243 -11.283 58.581  1.00 19.78 ? 988  HOH A O     1 
HETATM 12015 O  O     . HOH Y 8 .   ? -45.253 -21.243 63.493  1.00 25.16 ? 989  HOH A O     1 
HETATM 12016 O  O     . HOH Y 8 .   ? -41.405 -19.061 60.595  1.00 28.75 ? 990  HOH A O     1 
HETATM 12017 O  O     . HOH Y 8 .   ? -11.719 -18.039 97.242  1.00 36.01 ? 991  HOH A O     1 
HETATM 12018 O  O     . HOH Y 8 .   ? -33.321 7.836   48.558  1.00 17.43 ? 992  HOH A O     1 
HETATM 12019 O  O     . HOH Y 8 .   ? -31.417 -15.639 32.068  1.00 33.84 ? 993  HOH A O     1 
HETATM 12020 O  O     . HOH Y 8 .   ? -23.742 -26.275 69.157  1.00 28.13 ? 994  HOH A O     1 
HETATM 12021 O  O     . HOH Y 8 .   ? -5.751  -20.585 93.011  1.00 45.01 ? 995  HOH A O     1 
HETATM 12022 O  O     . HOH Y 8 .   ? -27.267 -32.798 51.333  1.00 25.42 ? 996  HOH A O     1 
HETATM 12023 O  O     . HOH Y 8 .   ? -5.003  6.879   66.414  1.00 44.10 ? 997  HOH A O     1 
HETATM 12024 O  O     . HOH Y 8 .   ? -24.558 -29.110 71.988  1.00 26.84 ? 998  HOH A O     1 
HETATM 12025 O  O     . HOH Y 8 .   ? -51.530 -14.251 87.330  1.00 25.74 ? 999  HOH A O     1 
HETATM 12026 O  O     . HOH Y 8 .   ? -35.820 -34.352 73.775  1.00 32.98 ? 1000 HOH A O     1 
HETATM 12027 O  O     . HOH Y 8 .   ? -30.826 7.052   31.623  1.00 36.51 ? 1001 HOH A O     1 
HETATM 12028 O  O     . HOH Y 8 .   ? -16.828 13.755  48.422  1.00 26.92 ? 1002 HOH A O     1 
HETATM 12029 O  O     . HOH Y 8 .   ? -26.229 -33.221 70.289  1.00 36.25 ? 1003 HOH A O     1 
HETATM 12030 O  O     . HOH Y 8 .   ? -32.515 13.405  60.482  1.00 32.12 ? 1004 HOH A O     1 
HETATM 12031 O  O     . HOH Y 8 .   ? -65.478 -7.181  61.361  1.00 36.91 ? 1005 HOH A O     1 
HETATM 12032 O  O     . HOH Y 8 .   ? -47.390 -24.110 34.096  1.00 30.19 ? 1006 HOH A O     1 
HETATM 12033 O  O     . HOH Y 8 .   ? -28.756 12.607  58.114  1.00 33.04 ? 1007 HOH A O     1 
HETATM 12034 O  O     . HOH Y 8 .   ? -20.645 9.368   14.698  1.00 34.01 ? 1008 HOH A O     1 
HETATM 12035 O  O     . HOH Y 8 .   ? -62.562 -14.077 57.251  1.00 42.54 ? 1009 HOH A O     1 
HETATM 12036 O  O     . HOH Y 8 .   ? -49.312 -19.341 66.181  1.00 35.82 ? 1010 HOH A O     1 
HETATM 12037 O  O     . HOH Y 8 .   ? -38.247 9.638   68.157  1.00 38.56 ? 1011 HOH A O     1 
HETATM 12038 O  O     . HOH Y 8 .   ? -46.495 -7.213  63.657  1.00 23.17 ? 1012 HOH A O     1 
HETATM 12039 O  O     . HOH Y 8 .   ? -48.149 -3.047  57.765  1.00 29.43 ? 1013 HOH A O     1 
HETATM 12040 O  O     . HOH Y 8 .   ? -35.905 -24.112 77.958  1.00 24.72 ? 1014 HOH A O     1 
HETATM 12041 O  O     . HOH Y 8 .   ? -45.450 -16.385 18.069  1.00 38.68 ? 1015 HOH A O     1 
HETATM 12042 O  O     . HOH Y 8 .   ? -16.404 -17.891 77.757  1.00 25.88 ? 1016 HOH A O     1 
HETATM 12043 O  O     . HOH Y 8 .   ? -54.539 -19.826 85.335  1.00 39.16 ? 1017 HOH A O     1 
HETATM 12044 O  O     . HOH Y 8 .   ? -26.671 -21.633 45.519  1.00 35.49 ? 1018 HOH A O     1 
HETATM 12045 O  O     . HOH Y 8 .   ? -21.797 13.898  13.069  1.00 39.34 ? 1019 HOH A O     1 
HETATM 12046 O  O     . HOH Y 8 .   ? -30.475 18.658  28.392  1.00 37.34 ? 1020 HOH A O     1 
HETATM 12047 O  O     . HOH Y 8 .   ? -3.052  -13.988 85.054  1.00 29.36 ? 1021 HOH A O     1 
HETATM 12048 O  O     . HOH Y 8 .   ? -12.203 -10.543 78.183  1.00 35.93 ? 1022 HOH A O     1 
HETATM 12049 O  O     . HOH Y 8 .   ? -35.446 -34.111 81.142  1.00 35.89 ? 1023 HOH A O     1 
HETATM 12050 O  O     . HOH Y 8 .   ? -23.139 14.473  15.291  1.00 24.85 ? 1024 HOH A O     1 
HETATM 12051 O  O     . HOH Y 8 .   ? -52.801 -15.477 42.918  1.00 23.71 ? 1025 HOH A O     1 
HETATM 12052 O  O     . HOH Y 8 .   ? -21.906 -23.654 54.853  1.00 32.35 ? 1026 HOH A O     1 
HETATM 12053 O  O     . HOH Y 8 .   ? -50.585 -2.767  39.606  1.00 39.64 ? 1027 HOH A O     1 
HETATM 12054 O  O     . HOH Y 8 .   ? -32.839 10.231  32.251  1.00 42.65 ? 1028 HOH A O     1 
HETATM 12055 O  O     . HOH Y 8 .   ? -30.812 -34.711 81.331  1.00 33.95 ? 1029 HOH A O     1 
HETATM 12056 O  O     . HOH Y 8 .   ? -42.725 -6.082  28.267  1.00 30.16 ? 1030 HOH A O     1 
HETATM 12057 O  O     . HOH Y 8 .   ? -27.227 -27.092 71.301  1.00 28.59 ? 1031 HOH A O     1 
HETATM 12058 O  O     . HOH Y 8 .   ? -56.626 -16.940 59.733  1.00 39.58 ? 1032 HOH A O     1 
HETATM 12059 O  O     . HOH Y 8 .   ? -53.177 -25.603 47.690  1.00 35.23 ? 1033 HOH A O     1 
HETATM 12060 O  O     . HOH Y 8 .   ? -47.834 -3.140  64.936  1.00 31.46 ? 1034 HOH A O     1 
HETATM 12061 O  O     . HOH Y 8 .   ? -12.685 -30.523 84.023  1.00 39.01 ? 1035 HOH A O     1 
HETATM 12062 O  O     . HOH Y 8 .   ? -26.973 -25.720 46.655  1.00 34.00 ? 1036 HOH A O     1 
HETATM 12063 O  O     . HOH Y 8 .   ? -61.126 -3.710  73.890  1.00 31.33 ? 1037 HOH A O     1 
HETATM 12064 O  O     . HOH Y 8 .   ? -7.134  1.790   62.011  1.00 33.72 ? 1038 HOH A O     1 
HETATM 12065 O  O     . HOH Y 8 .   ? -39.324 10.046  56.395  1.00 33.41 ? 1039 HOH A O     1 
HETATM 12066 O  O     . HOH Y 8 .   ? -23.482 -6.853  52.123  1.00 27.35 ? 1040 HOH A O     1 
HETATM 12067 O  O     . HOH Y 8 .   ? -25.495 -6.307  95.322  1.00 45.24 ? 1041 HOH A O     1 
HETATM 12068 O  O     . HOH Y 8 .   ? -43.553 -7.170  20.707  1.00 39.85 ? 1042 HOH A O     1 
HETATM 12069 O  O     . HOH Y 8 .   ? -23.620 -32.266 28.905  1.00 31.30 ? 1043 HOH A O     1 
HETATM 12070 O  O     . HOH Y 8 .   ? -32.266 -37.826 67.454  1.00 43.15 ? 1044 HOH A O     1 
HETATM 12071 O  O     . HOH Y 8 .   ? -25.987 -25.096 43.915  1.00 37.72 ? 1045 HOH A O     1 
HETATM 12072 O  O     . HOH Y 8 .   ? -39.163 -22.240 27.641  1.00 51.09 ? 1046 HOH A O     1 
HETATM 12073 O  O     . HOH Y 8 .   ? -45.947 7.178   54.404  1.00 23.09 ? 1047 HOH A O     1 
HETATM 12074 O  O     . HOH Y 8 .   ? -29.926 -20.685 42.121  1.00 28.40 ? 1048 HOH A O     1 
HETATM 12075 O  O     . HOH Y 8 .   ? -8.980  -9.677  75.277  1.00 17.99 ? 1049 HOH A O     1 
HETATM 12076 O  O     . HOH Y 8 .   ? -50.042 -13.567 60.618  1.00 31.83 ? 1050 HOH A O     1 
HETATM 12077 O  O     . HOH Y 8 .   ? -35.227 -27.354 83.654  1.00 23.61 ? 1051 HOH A O     1 
HETATM 12078 O  O     . HOH Y 8 .   ? -29.498 -11.104 47.484  1.00 29.78 ? 1052 HOH A O     1 
HETATM 12079 O  O     . HOH Y 8 .   ? -35.741 -10.876 33.506  1.00 27.78 ? 1053 HOH A O     1 
HETATM 12080 O  O     . HOH Y 8 .   ? -50.997 -26.948 81.248  1.00 31.78 ? 1054 HOH A O     1 
HETATM 12081 O  O     . HOH Y 8 .   ? -35.369 -24.633 88.830  1.00 28.57 ? 1055 HOH A O     1 
HETATM 12082 O  O     . HOH Y 8 .   ? -15.029 -3.272  91.408  1.00 32.46 ? 1056 HOH A O     1 
HETATM 12083 O  O     . HOH Y 8 .   ? -38.901 -37.705 55.317  1.00 31.28 ? 1057 HOH A O     1 
HETATM 12084 O  O     . HOH Y 8 .   ? -44.205 -15.754 83.813  1.00 38.71 ? 1058 HOH A O     1 
HETATM 12085 O  O     . HOH Y 8 .   ? -16.700 1.102   79.073  1.00 28.69 ? 1059 HOH A O     1 
HETATM 12086 O  O     . HOH Y 8 .   ? -4.643  9.984   57.562  1.00 36.39 ? 1060 HOH A O     1 
HETATM 12087 O  O     . HOH Y 8 .   ? -56.300 -9.885  60.190  1.00 24.14 ? 1061 HOH A O     1 
HETATM 12088 O  O     . HOH Y 8 .   ? -59.925 -17.348 46.674  1.00 30.48 ? 1062 HOH A O     1 
HETATM 12089 O  O     . HOH Y 8 .   ? -40.430 -33.878 66.050  1.00 36.15 ? 1063 HOH A O     1 
HETATM 12090 O  O     . HOH Y 8 .   ? -64.134 -15.933 73.555  1.00 49.45 ? 1064 HOH A O     1 
HETATM 12091 O  O     . HOH Y 8 .   ? -33.275 2.135   36.240  1.00 27.57 ? 1065 HOH A O     1 
HETATM 12092 O  O     . HOH Y 8 .   ? -42.574 -26.194 71.545  1.00 32.53 ? 1066 HOH A O     1 
HETATM 12093 O  O     . HOH Y 8 .   ? -22.934 -1.470  15.643  1.00 39.24 ? 1067 HOH A O     1 
HETATM 12094 O  O     . HOH Y 8 .   ? -28.415 -28.365 46.037  1.00 41.66 ? 1068 HOH A O     1 
HETATM 12095 O  O     . HOH Y 8 .   ? -56.667 -29.681 47.454  1.00 38.63 ? 1069 HOH A O     1 
HETATM 12096 O  O     . HOH Y 8 .   ? -12.882 -14.458 86.529  1.00 28.34 ? 1070 HOH A O     1 
HETATM 12097 O  O     . HOH Y 8 .   ? -19.625 -10.214 93.368  1.00 31.67 ? 1071 HOH A O     1 
HETATM 12098 O  O     . HOH Y 8 .   ? -7.793  -21.616 64.818  1.00 24.98 ? 1072 HOH A O     1 
HETATM 12099 O  O     . HOH Y 8 .   ? -13.633 3.218   74.289  1.00 35.46 ? 1073 HOH A O     1 
HETATM 12100 O  O     . HOH Y 8 .   ? -23.240 -20.920 96.013  1.00 31.45 ? 1074 HOH A O     1 
HETATM 12101 O  O     . HOH Y 8 .   ? -37.148 17.095  47.725  1.00 30.27 ? 1075 HOH A O     1 
HETATM 12102 O  O     . HOH Y 8 .   ? -7.165  -16.034 77.916  1.00 37.90 ? 1076 HOH A O     1 
HETATM 12103 O  O     . HOH Y 8 .   ? -37.068 13.966  48.993  1.00 28.42 ? 1077 HOH A O     1 
HETATM 12104 O  O     . HOH Y 8 .   ? -42.590 -37.791 37.507  1.00 35.73 ? 1078 HOH A O     1 
HETATM 12105 O  O     . HOH Y 8 .   ? -35.795 -31.276 27.060  1.00 26.94 ? 1079 HOH A O     1 
HETATM 12106 O  O     . HOH Y 8 .   ? -27.891 -38.083 58.984  1.00 46.76 ? 1080 HOH A O     1 
HETATM 12107 O  O     . HOH Y 8 .   ? -45.767 -26.929 79.822  1.00 30.89 ? 1081 HOH A O     1 
HETATM 12108 O  O     . HOH Y 8 .   ? -50.735 -2.981  47.776  1.00 32.02 ? 1082 HOH A O     1 
HETATM 12109 O  O     . HOH Y 8 .   ? -42.324 -12.165 81.875  1.00 50.27 ? 1083 HOH A O     1 
HETATM 12110 O  O     . HOH Y 8 .   ? -34.149 21.493  50.038  1.00 30.60 ? 1084 HOH A O     1 
HETATM 12111 O  O     . HOH Y 8 .   ? -44.926 -4.051  63.808  1.00 39.70 ? 1085 HOH A O     1 
HETATM 12112 O  O     . HOH Y 8 .   ? -42.289 11.526  27.858  1.00 58.06 ? 1086 HOH A O     1 
HETATM 12113 O  O     . HOH Y 8 .   ? -36.634 -7.475  61.811  1.00 26.37 ? 1087 HOH A O     1 
HETATM 12114 O  O     . HOH Y 8 .   ? -62.417 -17.948 45.001  1.00 39.89 ? 1088 HOH A O     1 
HETATM 12115 O  O     . HOH Y 8 .   ? -39.513 -22.877 83.024  1.00 25.05 ? 1089 HOH A O     1 
HETATM 12116 O  O     . HOH Y 8 .   ? -48.536 2.699   73.384  1.00 25.60 ? 1090 HOH A O     1 
HETATM 12117 O  O     . HOH Y 8 .   ? -43.785 -11.182 79.538  1.00 46.79 ? 1091 HOH A O     1 
HETATM 12118 O  O     . HOH Y 8 .   ? -38.654 -19.760 84.369  1.00 31.86 ? 1092 HOH A O     1 
HETATM 12119 O  O     . HOH Y 8 .   ? -34.891 12.093  66.039  1.00 45.41 ? 1093 HOH A O     1 
HETATM 12120 O  O     . HOH Y 8 .   ? -51.614 -17.061 53.998  1.00 32.84 ? 1094 HOH A O     1 
HETATM 12121 O  O     . HOH Y 8 .   ? -46.719 -21.554 89.266  1.00 31.06 ? 1095 HOH A O     1 
HETATM 12122 O  O     . HOH Y 8 .   ? -57.765 1.301   71.804  1.00 30.87 ? 1096 HOH A O     1 
HETATM 12123 O  O     . HOH Y 8 .   ? -65.552 -5.224  63.166  1.00 35.71 ? 1097 HOH A O     1 
HETATM 12124 O  O     . HOH Y 8 .   ? -15.477 -13.854 98.635  1.00 32.74 ? 1098 HOH A O     1 
HETATM 12125 O  O     . HOH Y 8 .   ? -25.150 -30.527 86.234  1.00 39.79 ? 1099 HOH A O     1 
HETATM 12126 O  O     . HOH Y 8 .   ? -20.895 12.212  16.825  1.00 30.46 ? 1100 HOH A O     1 
HETATM 12127 O  O     . HOH Y 8 .   ? -33.147 7.914   37.354  1.00 42.34 ? 1104 HOH A O     1 
HETATM 12128 O  O     . HOH Y 8 .   ? -30.605 14.097  34.039  1.00 44.07 ? 1105 HOH A O     1 
HETATM 12129 O  O     . HOH Y 8 .   ? -39.281 -25.462 82.275  1.00 41.58 ? 1106 HOH A O     1 
HETATM 12130 O  O     . HOH Y 8 .   ? -8.542  10.233  57.259  1.00 48.37 ? 1107 HOH A O     1 
HETATM 12131 O  O     . HOH Y 8 .   ? -34.223 -7.547  83.539  1.00 47.58 ? 1108 HOH A O     1 
HETATM 12132 O  O     . HOH Y 8 .   ? -50.150 -9.086  80.628  1.00 37.14 ? 1109 HOH A O     1 
HETATM 12133 O  O     . HOH Y 8 .   ? -49.716 2.989   75.959  1.00 35.38 ? 1110 HOH A O     1 
HETATM 12134 O  O     . HOH Y 8 .   ? -56.116 -8.198  42.442  1.00 33.66 ? 1111 HOH A O     1 
HETATM 12135 O  O     . HOH Y 8 .   ? -22.305 -12.390 94.008  1.00 36.33 ? 1112 HOH A O     1 
HETATM 12136 O  O     . HOH Y 8 .   ? -59.804 -13.544 59.192  1.00 34.06 ? 1113 HOH A O     1 
HETATM 12137 O  O     . HOH Y 8 .   ? -28.344 -5.554  44.883  1.00 43.07 ? 1114 HOH A O     1 
HETATM 12138 O  O     . HOH Y 8 .   ? -37.677 -12.811 74.437  1.00 21.53 ? 1115 HOH A O     1 
HETATM 12139 O  O     . HOH Y 8 .   ? -22.578 -30.587 85.117  1.00 38.10 ? 1116 HOH A O     1 
HETATM 12140 O  O     . HOH Y 8 .   ? -22.932 3.719   10.035  1.00 55.90 ? 1117 HOH A O     1 
HETATM 12141 O  O     . HOH Y 8 .   ? -49.549 -0.988  46.266  1.00 33.83 ? 1118 HOH A O     1 
HETATM 12142 O  O     . HOH Y 8 .   ? -44.767 -29.871 61.142  1.00 25.20 ? 1119 HOH A O     1 
HETATM 12143 O  O     . HOH Y 8 .   ? -62.421 -4.069  76.503  1.00 41.47 ? 1120 HOH A O     1 
HETATM 12144 O  O     . HOH Y 8 .   ? -18.563 1.804   70.248  1.00 38.08 ? 1121 HOH A O     1 
HETATM 12145 O  O     . HOH Y 8 .   ? -22.372 -0.632  85.018  1.00 44.12 ? 1122 HOH A O     1 
HETATM 12146 O  O     . HOH Y 8 .   ? -8.517  -2.186  74.411  1.00 31.28 ? 1123 HOH A O     1 
HETATM 12147 O  O     . HOH Y 8 .   ? -18.834 -18.784 53.636  1.00 44.87 ? 1124 HOH A O     1 
HETATM 12148 O  O     . HOH Y 8 .   ? -40.753 -16.922 89.926  1.00 32.98 ? 1125 HOH A O     1 
HETATM 12149 O  O     . HOH Y 8 .   ? -39.550 14.600  50.088  1.00 20.67 ? 1126 HOH A O     1 
HETATM 12150 O  O     . HOH Y 8 .   ? -8.722  -19.554 62.641  1.00 37.56 ? 1127 HOH A O     1 
HETATM 12151 O  O     . HOH Y 8 .   ? -37.661 -27.320 82.998  1.00 32.90 ? 1128 HOH A O     1 
HETATM 12152 O  O     . HOH Y 8 .   ? -52.518 -11.644 37.991  1.00 30.46 ? 1129 HOH A O     1 
HETATM 12153 O  O     . HOH Y 8 .   ? -54.319 -9.024  40.615  1.00 36.17 ? 1130 HOH A O     1 
HETATM 12154 O  O     . HOH Y 8 .   ? -10.553 -14.617 84.839  1.00 27.82 ? 1131 HOH A O     1 
HETATM 12155 O  O     . HOH Y 8 .   ? -53.492 8.333   53.196  1.00 29.57 ? 1132 HOH A O     1 
HETATM 12156 O  O     . HOH Y 8 .   ? -30.145 -21.628 39.875  1.00 27.15 ? 1133 HOH A O     1 
HETATM 12157 O  O     . HOH Y 8 .   ? -36.116 -37.087 57.978  1.00 33.33 ? 1134 HOH A O     1 
HETATM 12158 O  O     . HOH Y 8 .   ? -40.993 -35.701 61.815  1.00 34.99 ? 1135 HOH A O     1 
HETATM 12159 O  O     . HOH Y 8 .   ? -36.841 20.118  46.651  1.00 40.79 ? 1136 HOH A O     1 
HETATM 12160 O  O     . HOH Y 8 .   ? -37.389 20.479  42.173  1.00 48.74 ? 1137 HOH A O     1 
HETATM 12161 O  O     . HOH Y 8 .   ? -29.268 14.511  50.686  1.00 28.33 ? 1138 HOH A O     1 
HETATM 12162 O  O     . HOH Y 8 .   ? -39.455 1.656   38.317  1.00 25.16 ? 1139 HOH A O     1 
HETATM 12163 O  O     . HOH Y 8 .   ? -38.361 3.328   36.744  1.00 41.17 ? 1140 HOH A O     1 
HETATM 12164 O  O     . HOH Y 8 .   ? -17.420 8.108   11.894  1.00 37.25 ? 1141 HOH A O     1 
HETATM 12165 O  O     . HOH Y 8 .   ? -11.660 -26.915 76.489  1.00 45.97 ? 1142 HOH A O     1 
HETATM 12166 O  O     . HOH Y 8 .   ? -58.699 -21.573 53.486  1.00 39.69 ? 1143 HOH A O     1 
HETATM 12167 O  O     . HOH Y 8 .   ? -68.615 -11.461 50.055  1.00 52.12 ? 1144 HOH A O     1 
HETATM 12168 O  O     . HOH Y 8 .   ? -54.944 -19.836 58.751  1.00 39.53 ? 1145 HOH A O     1 
HETATM 12169 O  O     . HOH Y 8 .   ? -35.533 18.362  27.617  1.00 30.53 ? 1146 HOH A O     1 
HETATM 12170 O  O     . HOH Y 8 .   ? -28.811 1.815   12.622  1.00 39.81 ? 1147 HOH A O     1 
HETATM 12171 O  O     . HOH Y 8 .   ? -45.576 -16.963 56.784  1.00 23.76 ? 1148 HOH A O     1 
HETATM 12172 O  O     . HOH Y 8 .   ? -43.050 -17.748 62.200  1.00 39.78 ? 1149 HOH A O     1 
HETATM 12173 O  O     . HOH Y 8 .   ? -38.793 -26.213 61.349  1.00 32.36 ? 1150 HOH A O     1 
HETATM 12174 O  O     . HOH Y 8 .   ? -35.056 -17.682 74.808  1.00 28.07 ? 1151 HOH A O     1 
HETATM 12175 O  O     . HOH Y 8 .   ? -54.498 -6.952  44.289  1.00 31.61 ? 1152 HOH A O     1 
HETATM 12176 O  O     . HOH Y 8 .   ? -35.417 -34.594 48.456  1.00 38.28 ? 1153 HOH A O     1 
HETATM 12177 O  O     . HOH Y 8 .   ? -43.242 -3.308  26.298  1.00 37.62 ? 1154 HOH A O     1 
HETATM 12178 O  O     . HOH Y 8 .   ? -48.787 -15.303 57.696  1.00 38.16 ? 1155 HOH A O     1 
HETATM 12179 O  O     . HOH Y 8 .   ? -28.147 -16.944 34.361  1.00 28.96 ? 1156 HOH A O     1 
HETATM 12180 O  O     . HOH Y 8 .   ? -33.430 -10.618 34.615  1.00 34.74 ? 1157 HOH A O     1 
HETATM 12181 O  O     . HOH Y 8 .   ? -20.333 -6.808  49.368  1.00 38.79 ? 1158 HOH A O     1 
HETATM 12182 O  O     . HOH Y 8 .   ? -24.958 -22.880 48.856  1.00 36.62 ? 1159 HOH A O     1 
HETATM 12183 O  O     . HOH Y 8 .   ? -29.251 -26.545 35.001  1.00 49.01 ? 1160 HOH A O     1 
HETATM 12184 O  O     . HOH Y 8 .   ? -33.659 12.057  30.574  1.00 42.90 ? 1161 HOH A O     1 
HETATM 12185 O  O     . HOH Y 8 .   ? -18.746 -37.733 11.647  1.00 39.44 ? 1162 HOH A O     1 
HETATM 12186 O  O     . HOH Y 8 .   ? -58.092 -14.832 42.751  1.00 36.87 ? 1163 HOH A O     1 
HETATM 12187 O  O     . HOH Y 8 .   ? -53.118 -26.173 85.460  1.00 41.36 ? 1164 HOH A O     1 
HETATM 12188 O  O     . HOH Y 8 .   ? -20.800 15.168  49.818  1.00 33.78 ? 1165 HOH A O     1 
HETATM 12189 O  O     . HOH Y 8 .   ? -45.609 0.452   80.065  1.00 33.92 ? 1166 HOH A O     1 
HETATM 12190 O  O     . HOH Y 8 .   ? -63.106 -12.235 51.482  1.00 47.02 ? 1167 HOH A O     1 
HETATM 12191 O  O     . HOH Y 8 .   ? -52.037 -12.109 35.181  1.00 38.83 ? 1168 HOH A O     1 
HETATM 12192 O  O     . HOH Y 8 .   ? -27.333 15.016  33.370  1.00 34.25 ? 1169 HOH A O     1 
HETATM 12193 O  O     . HOH Y 8 .   ? -24.426 -5.138  92.430  1.00 35.29 ? 1170 HOH A O     1 
HETATM 12194 O  O     . HOH Y 8 .   ? -41.529 -33.168 74.094  1.00 34.24 ? 1171 HOH A O     1 
HETATM 12195 O  O     . HOH Y 8 .   ? -38.196 8.775   18.305  1.00 45.96 ? 1172 HOH A O     1 
HETATM 12196 O  O     . HOH Y 8 .   ? -25.692 -36.597 21.232  1.00 39.43 ? 1173 HOH A O     1 
HETATM 12197 O  O     . HOH Y 8 .   ? -42.149 -16.519 81.895  1.00 23.76 ? 1174 HOH A O     1 
HETATM 12198 O  O     . HOH Y 8 .   ? -26.575 -27.021 37.765  1.00 31.52 ? 1175 HOH A O     1 
HETATM 12199 O  O     . HOH Y 8 .   ? -33.276 12.414  56.640  1.00 37.62 ? 1176 HOH A O     1 
HETATM 12200 O  O     . HOH Y 8 .   ? -25.755 -36.973 13.511  1.00 42.09 ? 1177 HOH A O     1 
HETATM 12201 O  O     . HOH Y 8 .   ? -26.166 -33.545 11.930  1.00 36.02 ? 1178 HOH A O     1 
HETATM 12202 O  O     . HOH Y 8 .   ? -35.567 3.172   35.850  1.00 34.30 ? 1179 HOH A O     1 
HETATM 12203 O  O     . HOH Y 8 .   ? -33.214 -34.610 52.859  1.00 57.11 ? 1180 HOH A O     1 
HETATM 12204 O  O     . HOH Y 8 .   ? -53.800 -24.617 89.008  1.00 37.54 ? 1181 HOH A O     1 
HETATM 12205 O  O     . HOH Y 8 .   ? -31.301 13.631  57.904  1.00 31.75 ? 1182 HOH A O     1 
HETATM 12206 O  O     . HOH Y 8 .   ? -56.583 1.654   64.555  1.00 42.18 ? 1183 HOH A O     1 
HETATM 12207 O  O     . HOH Y 8 .   ? -49.593 -4.533  81.181  1.00 27.82 ? 1184 HOH A O     1 
HETATM 12208 O  O     . HOH Y 8 .   ? -9.810  -23.540 86.415  1.00 33.65 ? 1185 HOH A O     1 
HETATM 12209 O  O     . HOH Y 8 .   ? -40.949 -20.859 85.297  1.00 32.87 ? 1186 HOH A O     1 
HETATM 12210 O  O     . HOH Y 8 .   ? -2.830  -18.240 70.441  1.00 38.39 ? 1187 HOH A O     1 
HETATM 12211 O  O     . HOH Y 8 .   ? -48.787 -14.512 90.919  1.00 43.92 ? 1188 HOH A O     1 
HETATM 12212 O  O     . HOH Y 8 .   ? -51.423 1.626   46.302  1.00 37.29 ? 1189 HOH A O     1 
HETATM 12213 O  O     . HOH Y 8 .   ? -60.343 -15.317 44.152  1.00 44.32 ? 1190 HOH A O     1 
HETATM 12214 O  O     . HOH Y 8 .   ? -17.382 -28.497 4.277   1.00 36.77 ? 1191 HOH A O     1 
HETATM 12215 O  O     . HOH Y 8 .   ? -22.862 12.028  11.392  1.00 41.36 ? 1192 HOH A O     1 
HETATM 12216 O  O     . HOH Y 8 .   ? -26.797 -9.064  44.811  1.00 49.63 ? 1193 HOH A O     1 
HETATM 12217 O  O     . HOH Y 8 .   ? -40.808 -29.285 81.340  1.00 45.00 ? 1194 HOH A O     1 
HETATM 12218 O  O     . HOH Y 8 .   ? -58.750 -7.919  57.497  1.00 37.07 ? 1195 HOH A O     1 
HETATM 12219 O  O     . HOH Y 8 .   ? -60.930 -3.670  60.444  1.00 42.22 ? 1196 HOH A O     1 
HETATM 12220 O  O     . HOH Y 8 .   ? -33.611 17.193  61.915  1.00 46.83 ? 1197 HOH A O     1 
HETATM 12221 O  O     . HOH Y 8 .   ? -17.086 -30.229 17.496  1.00 41.71 ? 1198 HOH A O     1 
HETATM 12222 O  O     . HOH Y 8 .   ? -56.116 -18.574 61.677  1.00 41.43 ? 1199 HOH A O     1 
HETATM 12223 O  O     . HOH Y 8 .   ? -31.148 16.884  26.010  1.00 39.78 ? 1200 HOH A O     1 
HETATM 12224 O  O     . HOH Y 8 .   ? -28.774 16.412  27.295  1.00 46.11 ? 1201 HOH A O     1 
HETATM 12225 O  O     . HOH Y 8 .   ? -44.810 -39.099 37.990  1.00 35.15 ? 1202 HOH A O     1 
HETATM 12226 O  O     . HOH Y 8 .   ? -42.689 -2.865  79.253  1.00 45.55 ? 1203 HOH A O     1 
HETATM 12227 O  O     . HOH Y 8 .   ? -51.441 7.018   43.454  1.00 44.51 ? 1204 HOH A O     1 
HETATM 12228 O  O     . HOH Y 8 .   ? -26.192 -31.006 67.688  1.00 38.31 ? 1205 HOH A O     1 
HETATM 12229 O  O     . HOH Y 8 .   ? -15.229 -6.956  99.392  1.00 35.03 ? 1206 HOH A O     1 
HETATM 12230 O  O     . HOH Y 8 .   ? -17.323 -6.280  100.726 1.00 38.49 ? 1207 HOH A O     1 
HETATM 12231 O  O     . HOH Z 8 .   ? -13.386 -18.433 50.322  1.00 22.26 ? 1    HOH B O     1 
HETATM 12232 O  O     . HOH Z 8 .   ? -7.656  -14.998 16.545  1.00 18.61 ? 3    HOH B O     1 
HETATM 12233 O  O     . HOH Z 8 .   ? -6.355  -23.603 26.946  1.00 17.65 ? 4    HOH B O     1 
HETATM 12234 O  O     . HOH Z 8 .   ? 4.605   -24.702 34.574  1.00 20.61 ? 5    HOH B O     1 
HETATM 12235 O  O     . HOH Z 8 .   ? -26.397 3.787   36.081  1.00 16.23 ? 10   HOH B O     1 
HETATM 12236 O  O     . HOH Z 8 .   ? -15.463 2.197   28.047  1.00 16.99 ? 15   HOH B O     1 
HETATM 12237 O  O     . HOH Z 8 .   ? -29.920 -15.075 8.785   1.00 14.94 ? 17   HOH B O     1 
HETATM 12238 O  O     . HOH Z 8 .   ? -6.941  1.899   17.569  1.00 21.17 ? 18   HOH B O     1 
HETATM 12239 O  O     . HOH Z 8 .   ? -18.696 12.055  56.797  1.00 37.43 ? 752  HOH B O     1 
HETATM 12240 O  O     . HOH Z 8 .   ? -14.884 10.692  46.447  1.00 22.80 ? 753  HOH B O     1 
HETATM 12241 O  O     . HOH Z 8 .   ? -38.854 -10.809 14.307  1.00 16.86 ? 754  HOH B O     1 
HETATM 12242 O  O     . HOH Z 8 .   ? -28.063 -15.519 22.586  1.00 21.43 ? 755  HOH B O     1 
HETATM 12243 O  O     . HOH Z 8 .   ? -13.477 14.651  38.841  1.00 31.52 ? 756  HOH B O     1 
HETATM 12244 O  O     . HOH Z 8 .   ? -37.521 -28.078 18.096  1.00 48.16 ? 757  HOH B O     1 
HETATM 12245 O  O     . HOH Z 8 .   ? -26.202 9.771   40.338  1.00 16.71 ? 758  HOH B O     1 
HETATM 12246 O  O     . HOH Z 8 .   ? -2.043  -24.359 8.413   1.00 40.11 ? 759  HOH B O     1 
HETATM 12247 O  O     . HOH Z 8 .   ? -27.927 -42.485 67.964  1.00 45.05 ? 760  HOH B O     1 
HETATM 12248 O  O     . HOH Z 8 .   ? 8.739   7.459   26.398  1.00 45.11 ? 761  HOH B O     1 
HETATM 12249 O  O     . HOH Z 8 .   ? -36.606 -8.227  10.547  1.00 22.69 ? 762  HOH B O     1 
HETATM 12250 O  O     . HOH Z 8 .   ? 1.697   -15.092 26.805  1.00 41.75 ? 763  HOH B O     1 
HETATM 12251 O  O     . HOH Z 8 .   ? -16.319 -24.506 31.463  1.00 21.31 ? 764  HOH B O     1 
HETATM 12252 O  O     . HOH Z 8 .   ? -25.937 -13.936 23.180  1.00 17.09 ? 765  HOH B O     1 
HETATM 12253 O  O     . HOH Z 8 .   ? 10.516  -27.864 44.355  1.00 40.01 ? 766  HOH B O     1 
HETATM 12254 O  O     . HOH Z 8 .   ? -28.551 -7.533  -3.795  1.00 26.10 ? 767  HOH B O     1 
HETATM 12255 O  O     . HOH Z 8 .   ? -5.467  -18.393 6.085   1.00 31.41 ? 768  HOH B O     1 
HETATM 12256 O  O     . HOH Z 8 .   ? 4.187   -15.090 29.306  1.00 33.27 ? 769  HOH B O     1 
HETATM 12257 O  O     . HOH Z 8 .   ? -35.647 -10.851 11.295  1.00 24.53 ? 770  HOH B O     1 
HETATM 12258 O  O     . HOH Z 8 .   ? 2.856   -16.600 36.026  1.00 21.30 ? 771  HOH B O     1 
HETATM 12259 O  O     . HOH Z 8 .   ? -26.232 14.808  55.183  1.00 37.49 ? 772  HOH B O     1 
HETATM 12260 O  O     . HOH Z 8 .   ? -16.595 8.547   21.464  1.00 21.87 ? 773  HOH B O     1 
HETATM 12261 O  O     . HOH Z 8 .   ? -15.609 -3.509  62.973  1.00 20.42 ? 774  HOH B O     1 
HETATM 12262 O  O     . HOH Z 8 .   ? -20.790 -29.865 29.475  1.00 53.19 ? 775  HOH B O     1 
HETATM 12263 O  O     . HOH Z 8 .   ? -18.342 0.676   25.169  1.00 15.60 ? 776  HOH B O     1 
HETATM 12264 O  O     . HOH Z 8 .   ? -2.462  -11.510 22.868  1.00 26.05 ? 777  HOH B O     1 
HETATM 12265 O  O     . HOH Z 8 .   ? 12.689  -12.707 36.039  1.00 45.41 ? 778  HOH B O     1 
HETATM 12266 O  O     . HOH Z 8 .   ? 13.565  3.105   42.855  1.00 51.61 ? 779  HOH B O     1 
HETATM 12267 O  O     . HOH Z 8 .   ? -13.569 -11.503 -3.473  1.00 47.84 ? 780  HOH B O     1 
HETATM 12268 O  O     . HOH Z 8 .   ? -17.858 -13.177 -5.071  1.00 56.66 ? 781  HOH B O     1 
HETATM 12269 O  O     . HOH Z 8 .   ? -20.166 -24.091 22.605  1.00 42.53 ? 782  HOH B O     1 
HETATM 12270 O  O     . HOH Z 8 .   ? -28.469 -21.248 15.286  1.00 15.03 ? 783  HOH B O     1 
HETATM 12271 O  O     . HOH Z 8 .   ? -16.987 -20.420 38.513  1.00 22.86 ? 784  HOH B O     1 
HETATM 12272 O  O     . HOH Z 8 .   ? -21.797 -1.584  75.396  1.00 22.63 ? 785  HOH B O     1 
HETATM 12273 O  O     . HOH Z 8 .   ? -37.716 15.501  36.605  1.00 36.21 ? 786  HOH B O     1 
HETATM 12274 O  O     . HOH Z 8 .   ? 16.506  -9.317  32.480  1.00 54.52 ? 787  HOH B O     1 
HETATM 12275 O  O     . HOH Z 8 .   ? -16.739 13.340  25.118  1.00 24.55 ? 788  HOH B O     1 
HETATM 12276 O  O     . HOH Z 8 .   ? -26.712 -4.987  39.639  1.00 39.67 ? 789  HOH B O     1 
HETATM 12277 O  O     . HOH Z 8 .   ? -18.150 -20.426 43.268  1.00 48.04 ? 790  HOH B O     1 
HETATM 12278 O  O     . HOH Z 8 .   ? -7.423  -29.039 19.798  1.00 25.64 ? 791  HOH B O     1 
HETATM 12279 O  O     . HOH Z 8 .   ? -10.757 -27.049 53.256  1.00 25.84 ? 792  HOH B O     1 
HETATM 12280 O  O     . HOH Z 8 .   ? -10.314 -28.428 55.421  1.00 31.11 ? 793  HOH B O     1 
HETATM 12281 O  O     . HOH Z 8 .   ? -13.993 -4.804  58.333  1.00 20.03 ? 794  HOH B O     1 
HETATM 12282 O  O     . HOH Z 8 .   ? -21.043 -0.574  52.405  1.00 22.96 ? 795  HOH B O     1 
HETATM 12283 O  O     . HOH Z 8 .   ? -36.170 -10.919 13.928  1.00 15.52 ? 796  HOH B O     1 
HETATM 12284 O  O     . HOH Z 8 .   ? -8.643  -18.705 25.942  1.00 16.88 ? 797  HOH B O     1 
HETATM 12285 O  O     . HOH Z 8 .   ? -27.561 -11.165 17.206  1.00 15.68 ? 798  HOH B O     1 
HETATM 12286 O  O     . HOH Z 8 .   ? -25.650 3.900   78.893  1.00 45.97 ? 799  HOH B O     1 
HETATM 12287 O  O     . HOH Z 8 .   ? -13.969 5.861   24.142  1.00 24.45 ? 800  HOH B O     1 
HETATM 12288 O  O     . HOH Z 8 .   ? -6.062  -32.353 41.909  1.00 47.85 ? 804  HOH B O     1 
HETATM 12289 O  O     . HOH Z 8 .   ? -10.030 -31.142 41.009  1.00 43.94 ? 805  HOH B O     1 
HETATM 12290 O  O     . HOH Z 8 .   ? -18.351 18.063  56.138  1.00 44.88 ? 806  HOH B O     1 
HETATM 12291 O  O     . HOH Z 8 .   ? -15.785 -33.631 81.837  1.00 43.99 ? 807  HOH B O     1 
HETATM 12292 O  O     . HOH Z 8 .   ? -33.608 -4.299  26.992  1.00 17.64 ? 808  HOH B O     1 
HETATM 12293 O  O     . HOH Z 8 .   ? -22.684 -22.878 33.500  1.00 45.55 ? 809  HOH B O     1 
HETATM 12294 O  O     . HOH Z 8 .   ? -3.414  -25.315 40.430  1.00 25.80 ? 810  HOH B O     1 
HETATM 12295 O  O     . HOH Z 8 .   ? -6.530  0.560   -0.444  1.00 40.20 ? 811  HOH B O     1 
HETATM 12296 O  O     . HOH Z 8 .   ? -24.125 -20.535 41.811  1.00 55.39 ? 812  HOH B O     1 
HETATM 12297 O  O     . HOH Z 8 .   ? -2.637  -19.606 66.548  1.00 51.50 ? 813  HOH B O     1 
HETATM 12298 O  O     . HOH Z 8 .   ? -25.405 24.126  48.919  1.00 47.94 ? 814  HOH B O     1 
HETATM 12299 O  O     . HOH Z 8 .   ? -22.419 -22.406 40.932  1.00 40.87 ? 815  HOH B O     1 
HETATM 12300 O  O     . HOH Z 8 .   ? -14.580 14.075  26.955  1.00 48.81 ? 816  HOH B O     1 
HETATM 12301 O  O     . HOH Z 8 .   ? -8.395  13.910  38.051  1.00 49.15 ? 817  HOH B O     1 
HETATM 12302 O  O     . HOH Z 8 .   ? -8.806  13.761  35.593  1.00 44.31 ? 818  HOH B O     1 
HETATM 12303 O  O     . HOH Z 8 .   ? 2.810   -8.807  29.459  1.00 32.99 ? 819  HOH B O     1 
HETATM 12304 O  O     . HOH Z 8 .   ? 6.251   -10.474 28.479  1.00 35.05 ? 820  HOH B O     1 
HETATM 12305 O  O     . HOH Z 8 .   ? -20.032 11.001  58.754  1.00 47.45 ? 821  HOH B O     1 
HETATM 12306 O  O     . HOH Z 8 .   ? -14.789 13.948  23.048  1.00 36.09 ? 822  HOH B O     1 
HETATM 12307 O  O     . HOH Z 8 .   ? -9.512  -30.163 14.002  1.00 27.09 ? 823  HOH B O     1 
HETATM 12308 O  O     . HOH Z 8 .   ? -24.354 4.133   51.716  1.00 16.39 ? 824  HOH B O     1 
HETATM 12309 O  O     . HOH Z 8 .   ? -13.801 -28.961 35.149  1.00 26.40 ? 825  HOH B O     1 
HETATM 12310 O  O     . HOH Z 8 .   ? -15.492 -19.099 46.753  1.00 29.75 ? 826  HOH B O     1 
HETATM 12311 O  O     . HOH Z 8 .   ? -25.260 12.601  59.520  1.00 31.63 ? 827  HOH B O     1 
HETATM 12312 O  O     . HOH Z 8 .   ? 2.687   -20.322 10.921  1.00 28.17 ? 828  HOH B O     1 
HETATM 12313 O  O     . HOH Z 8 .   ? -15.494 -25.330 28.873  1.00 27.34 ? 829  HOH B O     1 
HETATM 12314 O  O     . HOH Z 8 .   ? 7.634   -31.351 40.986  1.00 41.64 ? 830  HOH B O     1 
HETATM 12315 O  O     . HOH Z 8 .   ? 1.869   -11.060 37.709  1.00 20.77 ? 831  HOH B O     1 
HETATM 12316 O  O     . HOH Z 8 .   ? -31.968 -28.114 -0.887  1.00 47.78 ? 832  HOH B O     1 
HETATM 12317 O  O     . HOH Z 8 .   ? -11.599 -4.692  30.419  1.00 29.67 ? 833  HOH B O     1 
HETATM 12318 O  O     . HOH Z 8 .   ? 3.638   -22.627 36.749  1.00 27.57 ? 834  HOH B O     1 
HETATM 12319 O  O     . HOH Z 8 .   ? -10.628 -20.197 12.619  1.00 23.94 ? 835  HOH B O     1 
HETATM 12320 O  O     . HOH Z 8 .   ? -18.750 15.923  48.291  1.00 24.52 ? 836  HOH B O     1 
HETATM 12321 O  O     . HOH Z 8 .   ? -22.978 -23.696 31.207  1.00 25.95 ? 837  HOH B O     1 
HETATM 12322 O  O     . HOH Z 8 .   ? -30.281 -29.478 3.517   1.00 29.69 ? 838  HOH B O     1 
HETATM 12323 O  O     . HOH Z 8 .   ? 6.955   0.398   31.599  1.00 24.19 ? 839  HOH B O     1 
HETATM 12324 O  O     . HOH Z 8 .   ? -32.115 -8.209  34.689  1.00 20.36 ? 840  HOH B O     1 
HETATM 12325 O  O     . HOH Z 8 .   ? 14.760  -3.815  32.800  1.00 40.25 ? 841  HOH B O     1 
HETATM 12326 O  O     . HOH Z 8 .   ? 2.477   -13.715 66.717  1.00 47.02 ? 842  HOH B O     1 
HETATM 12327 O  O     . HOH Z 8 .   ? -5.093  2.248   27.053  1.00 40.01 ? 843  HOH B O     1 
HETATM 12328 O  O     . HOH Z 8 .   ? -5.764  -7.369  30.809  1.00 27.35 ? 844  HOH B O     1 
HETATM 12329 O  O     . HOH Z 8 .   ? -41.672 -15.242 -2.438  1.00 40.13 ? 845  HOH B O     1 
HETATM 12330 O  O     . HOH Z 8 .   ? -28.242 -33.851 81.844  1.00 23.70 ? 846  HOH B O     1 
HETATM 12331 O  O     . HOH Z 8 .   ? -7.831  -4.927  68.526  1.00 28.18 ? 847  HOH B O     1 
HETATM 12332 O  O     . HOH Z 8 .   ? -42.725 -20.766 0.538   1.00 44.62 ? 848  HOH B O     1 
HETATM 12333 O  O     . HOH Z 8 .   ? 2.222   -25.406 52.325  1.00 41.89 ? 849  HOH B O     1 
HETATM 12334 O  O     . HOH Z 8 .   ? 9.802   -16.532 35.462  1.00 47.59 ? 850  HOH B O     1 
HETATM 12335 O  O     . HOH Z 8 .   ? -0.248  0.399   26.155  1.00 30.75 ? 851  HOH B O     1 
HETATM 12336 O  O     . HOH Z 8 .   ? 9.874   -12.782 40.012  1.00 45.13 ? 852  HOH B O     1 
HETATM 12337 O  O     . HOH Z 8 .   ? -11.717 11.189  19.605  0.50 13.13 ? 853  HOH B O     1 
HETATM 12338 O  O     . HOH Z 8 .   ? -8.854  -21.108 36.543  1.00 20.94 ? 854  HOH B O     1 
HETATM 12339 O  O     . HOH Z 8 .   ? -32.162 -37.236 78.474  1.00 43.35 ? 855  HOH B O     1 
HETATM 12340 O  O     . HOH Z 8 .   ? -28.527 3.423   -6.495  1.00 25.84 ? 856  HOH B O     1 
HETATM 12341 O  O     . HOH Z 8 .   ? -9.438  -21.765 4.585   1.00 22.88 ? 857  HOH B O     1 
HETATM 12342 O  O     . HOH Z 8 .   ? -28.300 3.953   78.962  1.00 54.64 ? 858  HOH B O     1 
HETATM 12343 O  O     . HOH Z 8 .   ? -7.302  -9.539  9.247   1.00 22.33 ? 859  HOH B O     1 
HETATM 12344 O  O     . HOH Z 8 .   ? -29.772 -17.084 11.204  1.00 20.96 ? 860  HOH B O     1 
HETATM 12345 O  O     . HOH Z 8 .   ? -32.991 -14.039 -7.036  1.00 21.50 ? 861  HOH B O     1 
HETATM 12346 O  O     . HOH Z 8 .   ? -8.856  -15.041 21.865  1.00 16.36 ? 862  HOH B O     1 
HETATM 12347 O  O     . HOH Z 8 .   ? -17.380 -19.112 11.221  1.00 17.93 ? 863  HOH B O     1 
HETATM 12348 O  O     . HOH Z 8 .   ? -33.207 -7.484  29.726  1.00 23.65 ? 864  HOH B O     1 
HETATM 12349 O  O     . HOH Z 8 .   ? -9.686  2.667   53.100  1.00 25.43 ? 865  HOH B O     1 
HETATM 12350 O  O     . HOH Z 8 .   ? -18.337 -17.302 -4.578  1.00 33.47 ? 866  HOH B O     1 
HETATM 12351 O  O     . HOH Z 8 .   ? -25.650 -37.457 81.947  1.00 35.18 ? 867  HOH B O     1 
HETATM 12352 O  O     . HOH Z 8 .   ? -8.180  11.972  30.769  1.00 38.45 ? 868  HOH B O     1 
HETATM 12353 O  O     . HOH Z 8 .   ? -35.330 -23.628 2.269   1.00 29.02 ? 869  HOH B O     1 
HETATM 12354 O  O     . HOH Z 8 .   ? 5.471   -8.796  30.192  1.00 23.60 ? 870  HOH B O     1 
HETATM 12355 O  O     . HOH Z 8 .   ? -42.618 -21.019 18.475  1.00 30.57 ? 871  HOH B O     1 
HETATM 12356 O  O     . HOH Z 8 .   ? -24.928 -40.602 74.703  1.00 49.44 ? 872  HOH B O     1 
HETATM 12357 O  O     . HOH Z 8 .   ? 8.369   -18.475 43.706  1.00 31.75 ? 873  HOH B O     1 
HETATM 12358 O  O     . HOH Z 8 .   ? -25.235 6.647   37.661  1.00 30.50 ? 874  HOH B O     1 
HETATM 12359 O  O     . HOH Z 8 .   ? -37.310 -25.790 0.851   1.00 41.84 ? 875  HOH B O     1 
HETATM 12360 O  O     . HOH Z 8 .   ? 2.631   -14.779 45.959  1.00 23.05 ? 876  HOH B O     1 
HETATM 12361 O  O     . HOH Z 8 .   ? 2.421   -19.203 36.566  1.00 25.84 ? 877  HOH B O     1 
HETATM 12362 O  O     . HOH Z 8 .   ? -34.376 -24.679 -13.956 1.00 62.99 ? 878  HOH B O     1 
HETATM 12363 O  O     . HOH Z 8 .   ? 8.834   -24.248 43.883  1.00 38.87 ? 879  HOH B O     1 
HETATM 12364 O  O     . HOH Z 8 .   ? 8.992   -25.740 50.269  1.00 62.34 ? 880  HOH B O     1 
HETATM 12365 O  O     . HOH Z 8 .   ? -2.150  -19.997 8.172   1.00 24.76 ? 881  HOH B O     1 
HETATM 12366 O  O     . HOH Z 8 .   ? 6.262   -4.489  50.531  1.00 53.15 ? 882  HOH B O     1 
HETATM 12367 O  O     . HOH Z 8 .   ? -11.184 -4.526  13.502  1.00 36.60 ? 883  HOH B O     1 
HETATM 12368 O  O     . HOH Z 8 .   ? -39.953 -21.244 -4.059  1.00 39.26 ? 884  HOH B O     1 
HETATM 12369 O  O     . HOH Z 8 .   ? -11.816 -6.260  56.799  1.00 19.04 ? 885  HOH B O     1 
HETATM 12370 O  O     . HOH Z 8 .   ? -18.892 -13.525 27.998  1.00 25.88 ? 886  HOH B O     1 
HETATM 12371 O  O     . HOH Z 8 .   ? -6.683  5.472   12.371  1.00 41.59 ? 887  HOH B O     1 
HETATM 12372 O  O     . HOH Z 8 .   ? -13.718 12.828  20.482  1.00 38.53 ? 888  HOH B O     1 
HETATM 12373 O  O     . HOH Z 8 .   ? -19.553 -12.276 23.157  0.70 27.20 ? 889  HOH B O     1 
HETATM 12374 O  O     . HOH Z 8 .   ? -29.159 -11.879 13.812  1.00 23.07 ? 890  HOH B O     1 
HETATM 12375 O  O     . HOH Z 8 .   ? -7.099  -33.665 23.438  1.00 51.76 ? 891  HOH B O     1 
HETATM 12376 O  O     . HOH Z 8 .   ? 4.030   -17.884 20.921  1.00 47.88 ? 892  HOH B O     1 
HETATM 12377 O  O     . HOH Z 8 .   ? -27.752 -4.514  71.242  1.00 25.79 ? 893  HOH B O     1 
HETATM 12378 O  O     . HOH Z 8 .   ? 13.221  -6.959  24.557  1.00 46.37 ? 894  HOH B O     1 
HETATM 12379 O  O     . HOH Z 8 .   ? 10.339  -11.608 36.909  1.00 37.31 ? 895  HOH B O     1 
HETATM 12380 O  O     . HOH Z 8 .   ? -18.287 0.502   52.438  1.00 19.40 ? 896  HOH B O     1 
HETATM 12381 O  O     . HOH Z 8 .   ? -7.231  -12.520 -8.974  1.00 61.91 ? 897  HOH B O     1 
HETATM 12382 O  O     . HOH Z 8 .   ? -20.720 -5.211  44.819  1.00 56.68 ? 898  HOH B O     1 
HETATM 12383 O  O     . HOH Z 8 .   ? -7.793  4.087   10.928  1.00 42.49 ? 899  HOH B O     1 
HETATM 12384 O  O     . HOH Z 8 .   ? -6.670  -0.562  63.869  1.00 51.89 ? 900  HOH B O     1 
HETATM 12385 O  O     . HOH Z 8 .   ? 10.348  -14.297 23.452  1.00 49.59 ? 902  HOH B O     1 
HETATM 12386 O  O     . HOH Z 8 .   ? 6.269   -9.256  32.954  1.00 27.14 ? 903  HOH B O     1 
HETATM 12387 O  O     . HOH Z 8 .   ? -14.316 -34.675 63.313  1.00 38.60 ? 904  HOH B O     1 
HETATM 12388 O  O     . HOH Z 8 .   ? -1.614  1.431   50.990  1.00 25.07 ? 905  HOH B O     1 
HETATM 12389 O  O     . HOH Z 8 .   ? -36.521 -14.980 4.587   1.00 16.12 ? 906  HOH B O     1 
HETATM 12390 O  O     . HOH Z 8 .   ? -7.961  -10.160 -7.416  1.00 46.40 ? 907  HOH B O     1 
HETATM 12391 O  O     . HOH Z 8 .   ? -15.729 -38.747 70.243  1.00 35.19 ? 908  HOH B O     1 
HETATM 12392 O  O     . HOH Z 8 .   ? -38.980 5.232   16.103  1.00 50.10 ? 909  HOH B O     1 
HETATM 12393 O  O     . HOH Z 8 .   ? -13.383 8.052   55.564  1.00 42.42 ? 910  HOH B O     1 
HETATM 12394 O  O     . HOH Z 8 .   ? 2.237   3.392   48.022  1.00 48.79 ? 911  HOH B O     1 
HETATM 12395 O  O     . HOH Z 8 .   ? -22.160 14.557  56.695  1.00 52.03 ? 912  HOH B O     1 
HETATM 12396 O  O     . HOH Z 8 .   ? 12.929  -9.413  23.833  1.00 54.47 ? 913  HOH B O     1 
HETATM 12397 O  O     . HOH Z 8 .   ? -13.720 -6.832  36.392  1.00 22.26 ? 914  HOH B O     1 
HETATM 12398 O  O     . HOH Z 8 .   ? 0.515   -18.795 17.592  1.00 38.10 ? 915  HOH B O     1 
HETATM 12399 O  O     . HOH Z 8 .   ? -28.241 -3.744  37.797  1.00 25.32 ? 916  HOH B O     1 
HETATM 12400 O  O     . HOH Z 8 .   ? 5.693   -8.600  46.350  1.00 31.29 ? 917  HOH B O     1 
HETATM 12401 O  O     . HOH Z 8 .   ? -26.113 -35.450 84.540  1.00 48.74 ? 918  HOH B O     1 
HETATM 12402 O  O     . HOH Z 8 .   ? -5.041  -17.043 59.405  1.00 29.18 ? 919  HOH B O     1 
HETATM 12403 O  O     . HOH Z 8 .   ? 2.353   1.637   41.865  1.00 33.29 ? 920  HOH B O     1 
HETATM 12404 O  O     . HOH Z 8 .   ? -23.657 10.655  57.635  1.00 45.43 ? 921  HOH B O     1 
HETATM 12405 O  O     . HOH Z 8 .   ? -26.320 5.907   52.390  1.00 32.14 ? 922  HOH B O     1 
HETATM 12406 O  O     . HOH Z 8 .   ? -8.907  12.888  42.319  1.00 29.45 ? 923  HOH B O     1 
HETATM 12407 O  O     . HOH Z 8 .   ? 5.888   -7.485  36.047  1.00 28.86 ? 924  HOH B O     1 
HETATM 12408 O  O     . HOH Z 8 .   ? -27.153 -36.576 73.448  1.00 30.77 ? 925  HOH B O     1 
HETATM 12409 O  O     . HOH Z 8 .   ? -22.159 17.213  42.313  1.00 22.91 ? 926  HOH B O     1 
HETATM 12410 O  O     . HOH Z 8 .   ? 13.528  -5.257  28.473  1.00 42.11 ? 927  HOH B O     1 
HETATM 12411 O  O     . HOH Z 8 .   ? 14.834  5.820   26.831  1.00 42.61 ? 928  HOH B O     1 
HETATM 12412 O  O     . HOH Z 8 .   ? -24.537 -2.643  -0.159  1.00 29.99 ? 929  HOH B O     1 
HETATM 12413 O  O     . HOH Z 8 .   ? -22.354 -6.013  6.983   1.00 31.40 ? 930  HOH B O     1 
HETATM 12414 O  O     . HOH Z 8 .   ? -32.421 4.679   13.313  1.00 44.07 ? 931  HOH B O     1 
HETATM 12415 O  O     . HOH Z 8 .   ? -41.781 -18.755 10.798  1.00 39.83 ? 932  HOH B O     1 
HETATM 12416 O  O     . HOH Z 8 .   ? -21.196 7.148   58.863  1.00 31.58 ? 933  HOH B O     1 
HETATM 12417 O  O     . HOH Z 8 .   ? 9.214   -4.855  28.801  1.00 31.06 ? 934  HOH B O     1 
HETATM 12418 O  O     . HOH Z 8 .   ? -17.756 11.314  61.865  1.00 30.82 ? 935  HOH B O     1 
HETATM 12419 O  O     . HOH Z 8 .   ? 7.634   -15.613 3.232   1.00 30.42 ? 936  HOH B O     1 
HETATM 12420 O  O     . HOH Z 8 .   ? 0.804   -19.427 8.503   1.00 34.25 ? 937  HOH B O     1 
HETATM 12421 O  O     . HOH Z 8 .   ? -6.382  -2.708  61.748  1.00 26.94 ? 938  HOH B O     1 
HETATM 12422 O  O     . HOH Z 8 .   ? -30.345 -0.364  5.653   1.00 25.35 ? 939  HOH B O     1 
HETATM 12423 O  O     . HOH Z 8 .   ? -25.696 -32.851 83.861  1.00 30.06 ? 940  HOH B O     1 
HETATM 12424 O  O     . HOH Z 8 .   ? -15.046 11.988  40.765  1.00 20.56 ? 941  HOH B O     1 
HETATM 12425 O  O     . HOH Z 8 .   ? -21.196 -24.888 12.236  1.00 28.79 ? 942  HOH B O     1 
HETATM 12426 O  O     . HOH Z 8 .   ? -12.798 -26.117 29.295  1.00 22.16 ? 943  HOH B O     1 
HETATM 12427 O  O     . HOH Z 8 .   ? -11.558 -12.579 14.221  1.00 18.87 ? 944  HOH B O     1 
HETATM 12428 O  O     . HOH Z 8 .   ? -16.789 -23.997 17.000  1.00 27.10 ? 945  HOH B O     1 
HETATM 12429 O  O     . HOH Z 8 .   ? -20.824 -27.531 2.946   1.00 30.31 ? 946  HOH B O     1 
HETATM 12430 O  O     . HOH Z 8 .   ? 1.184   -16.856 28.711  1.00 23.90 ? 947  HOH B O     1 
HETATM 12431 O  O     . HOH Z 8 .   ? 12.205  -6.867  32.354  1.00 33.08 ? 948  HOH B O     1 
HETATM 12432 O  O     . HOH Z 8 .   ? -1.429  -25.577 21.010  1.00 27.02 ? 949  HOH B O     1 
HETATM 12433 O  O     . HOH Z 8 .   ? -14.016 13.790  34.608  1.00 28.44 ? 950  HOH B O     1 
HETATM 12434 O  O     . HOH Z 8 .   ? 2.997   -14.897 16.424  1.00 46.04 ? 951  HOH B O     1 
HETATM 12435 O  O     . HOH Z 8 .   ? -48.252 -1.268  28.746  1.00 48.39 ? 952  HOH B O     1 
HETATM 12436 O  O     . HOH Z 8 .   ? -36.558 11.663  42.555  1.00 22.32 ? 953  HOH B O     1 
HETATM 12437 O  O     . HOH Z 8 .   ? -1.497  10.376  25.323  1.00 36.38 ? 954  HOH B O     1 
HETATM 12438 O  O     . HOH Z 8 .   ? -1.862  -7.963  61.697  1.00 29.52 ? 955  HOH B O     1 
HETATM 12439 O  O     . HOH Z 8 .   ? -34.121 1.545   11.733  1.00 26.09 ? 956  HOH B O     1 
HETATM 12440 O  O     . HOH Z 8 .   ? -15.142 -14.780 57.409  1.00 33.82 ? 957  HOH B O     1 
HETATM 12441 O  O     . HOH Z 8 .   ? -6.964  -28.831 13.940  1.00 24.83 ? 958  HOH B O     1 
HETATM 12442 O  O     . HOH Z 8 .   ? -34.153 -16.517 -8.257  1.00 39.05 ? 959  HOH B O     1 
HETATM 12443 O  O     . HOH Z 8 .   ? -12.962 0.307   19.002  1.00 28.65 ? 960  HOH B O     1 
HETATM 12444 O  O     . HOH Z 8 .   ? -1.698  -26.420 13.635  1.00 29.38 ? 961  HOH B O     1 
HETATM 12445 O  O     . HOH Z 8 .   ? -7.462  -28.074 6.597   1.00 36.03 ? 962  HOH B O     1 
HETATM 12446 O  O     . HOH Z 8 .   ? -7.892  -3.015  8.459   1.00 22.77 ? 963  HOH B O     1 
HETATM 12447 O  O     . HOH Z 8 .   ? -6.391  1.162   59.114  1.00 30.30 ? 964  HOH B O     1 
HETATM 12448 O  O     . HOH Z 8 .   ? -16.984 -26.305 55.207  1.00 22.13 ? 965  HOH B O     1 
HETATM 12449 O  O     . HOH Z 8 .   ? -10.599 6.460   14.210  1.00 35.89 ? 966  HOH B O     1 
HETATM 12450 O  O     . HOH Z 8 .   ? -31.566 -13.008 2.983   1.00 16.05 ? 967  HOH B O     1 
HETATM 12451 O  O     . HOH Z 8 .   ? -25.089 -6.252  37.626  1.00 27.21 ? 968  HOH B O     1 
HETATM 12452 O  O     . HOH Z 8 .   ? -19.098 -32.533 59.053  1.00 29.69 ? 969  HOH B O     1 
HETATM 12453 O  O     . HOH Z 8 .   ? -21.468 -25.503 38.595  1.00 42.15 ? 970  HOH B O     1 
HETATM 12454 O  O     . HOH Z 8 .   ? 10.665  5.870   30.043  1.00 39.44 ? 971  HOH B O     1 
HETATM 12455 O  O     . HOH Z 8 .   ? 8.509   -18.128 41.062  1.00 35.33 ? 972  HOH B O     1 
HETATM 12456 O  O     . HOH Z 8 .   ? -0.938  4.956   44.387  1.00 33.21 ? 973  HOH B O     1 
HETATM 12457 O  O     . HOH Z 8 .   ? -8.870  -24.261 4.408   1.00 45.56 ? 974  HOH B O     1 
HETATM 12458 O  O     . HOH Z 8 .   ? -5.376  -13.766 3.543   1.00 32.13 ? 975  HOH B O     1 
HETATM 12459 O  O     . HOH Z 8 .   ? -42.600 -5.911  18.209  1.00 48.15 ? 976  HOH B O     1 
HETATM 12460 O  O     . HOH Z 8 .   ? -46.466 2.513   24.043  1.00 42.80 ? 977  HOH B O     1 
HETATM 12461 O  O     . HOH Z 8 .   ? -18.448 -9.599  41.988  1.00 20.96 ? 978  HOH B O     1 
HETATM 12462 O  O     . HOH Z 8 .   ? -30.911 -8.610  23.026  1.00 21.16 ? 979  HOH B O     1 
HETATM 12463 O  O     . HOH Z 8 .   ? -18.509 -26.620 1.910   1.00 34.66 ? 980  HOH B O     1 
HETATM 12464 O  O     . HOH Z 8 .   ? -34.185 -13.841 2.839   1.00 20.69 ? 981  HOH B O     1 
HETATM 12465 O  O     . HOH Z 8 .   ? -15.838 5.941   22.089  1.00 23.04 ? 982  HOH B O     1 
HETATM 12466 O  O     . HOH Z 8 .   ? -16.000 -37.226 66.364  1.00 29.66 ? 983  HOH B O     1 
HETATM 12467 O  O     . HOH Z 8 .   ? -2.852  0.343   21.845  1.00 19.26 ? 984  HOH B O     1 
HETATM 12468 O  O     . HOH Z 8 .   ? 0.538   -26.206 12.264  1.00 29.32 ? 985  HOH B O     1 
HETATM 12469 O  O     . HOH Z 8 .   ? -43.416 -9.397  13.670  1.00 29.08 ? 986  HOH B O     1 
HETATM 12470 O  O     . HOH Z 8 .   ? -37.084 -23.554 23.822  1.00 21.22 ? 987  HOH B O     1 
HETATM 12471 O  O     . HOH Z 8 .   ? -32.131 -11.532 -9.007  1.00 40.18 ? 988  HOH B O     1 
HETATM 12472 O  O     . HOH Z 8 .   ? -31.967 1.909   20.188  1.00 28.45 ? 989  HOH B O     1 
HETATM 12473 O  O     . HOH Z 8 .   ? 13.127  3.012   28.887  1.00 35.42 ? 990  HOH B O     1 
HETATM 12474 O  O     . HOH Z 8 .   ? 16.832  -4.576  38.806  1.00 48.19 ? 991  HOH B O     1 
HETATM 12475 O  O     . HOH Z 8 .   ? -31.949 -26.895 11.835  1.00 41.42 ? 992  HOH B O     1 
HETATM 12476 O  O     . HOH Z 8 .   ? -22.273 -40.474 75.674  1.00 32.98 ? 993  HOH B O     1 
HETATM 12477 O  O     . HOH Z 8 .   ? -9.277  -30.117 48.753  1.00 48.04 ? 994  HOH B O     1 
HETATM 12478 O  O     . HOH Z 8 .   ? -2.553  -27.811 21.781  1.00 37.54 ? 995  HOH B O     1 
HETATM 12479 O  O     . HOH Z 8 .   ? 0.332   1.333   45.183  1.00 37.28 ? 996  HOH B O     1 
HETATM 12480 O  O     . HOH Z 8 .   ? -16.032 -34.860 76.045  1.00 33.20 ? 997  HOH B O     1 
HETATM 12481 O  O     . HOH Z 8 .   ? -43.760 -16.198 4.645   1.00 45.44 ? 998  HOH B O     1 
HETATM 12482 O  O     . HOH Z 8 .   ? -20.386 -24.084 19.320  1.00 28.51 ? 999  HOH B O     1 
HETATM 12483 O  O     . HOH Z 8 .   ? -24.798 13.947  33.182  1.00 23.75 ? 1000 HOH B O     1 
HETATM 12484 O  O     . HOH Z 8 .   ? -6.366  -9.392  -0.603  1.00 33.84 ? 1001 HOH B O     1 
HETATM 12485 O  O     . HOH Z 8 .   ? -31.978 -9.337  31.095  1.00 28.05 ? 1002 HOH B O     1 
HETATM 12486 O  O     . HOH Z 8 .   ? -25.794 -32.765 74.849  1.00 24.97 ? 1003 HOH B O     1 
HETATM 12487 O  O     . HOH Z 8 .   ? -7.070  -30.998 39.156  1.00 30.03 ? 1004 HOH B O     1 
HETATM 12488 O  O     . HOH Z 8 .   ? -40.898 -3.918  15.699  1.00 22.27 ? 1005 HOH B O     1 
HETATM 12489 O  O     . HOH Z 8 .   ? -7.274  -21.404 11.751  1.00 26.50 ? 1006 HOH B O     1 
HETATM 12490 O  O     . HOH Z 8 .   ? -31.185 -12.112 30.782  1.00 21.65 ? 1007 HOH B O     1 
HETATM 12491 O  O     . HOH Z 8 .   ? -23.247 4.767   77.053  1.00 30.60 ? 1008 HOH B O     1 
HETATM 12492 O  O     . HOH Z 8 .   ? 5.180   -23.245 30.862  1.00 41.08 ? 1009 HOH B O     1 
HETATM 12493 O  O     . HOH Z 8 .   ? -18.150 14.272  36.829  1.00 31.94 ? 1010 HOH B O     1 
HETATM 12494 O  O     . HOH Z 8 .   ? 0.799   -23.664 49.554  1.00 30.41 ? 1011 HOH B O     1 
HETATM 12495 O  O     . HOH Z 8 .   ? -11.978 -29.802 6.367   1.00 28.72 ? 1012 HOH B O     1 
HETATM 12496 O  O     . HOH Z 8 .   ? 10.557  7.013   16.807  1.00 35.82 ? 1013 HOH B O     1 
HETATM 12497 O  O     . HOH Z 8 .   ? -45.287 -19.860 14.608  1.00 47.94 ? 1014 HOH B O     1 
HETATM 12498 O  O     . HOH Z 8 .   ? -40.600 6.664   33.639  1.00 26.32 ? 1015 HOH B O     1 
HETATM 12499 O  O     . HOH Z 8 .   ? -7.820  -1.459  69.814  1.00 39.07 ? 1016 HOH B O     1 
HETATM 12500 O  O     . HOH Z 8 .   ? -19.249 -26.326 16.088  1.00 25.77 ? 1017 HOH B O     1 
HETATM 12501 O  O     . HOH Z 8 .   ? -16.836 -22.168 9.926   1.00 22.55 ? 1018 HOH B O     1 
HETATM 12502 O  O     . HOH Z 8 .   ? -0.469  3.678   9.008   1.00 32.02 ? 1019 HOH B O     1 
HETATM 12503 O  O     . HOH Z 8 .   ? -22.477 15.323  33.654  1.00 30.07 ? 1020 HOH B O     1 
HETATM 12504 O  O     . HOH Z 8 .   ? 4.885   -16.622 12.792  1.00 37.38 ? 1021 HOH B O     1 
HETATM 12505 O  O     . HOH Z 8 .   ? -39.098 -17.092 10.954  1.00 24.66 ? 1022 HOH B O     1 
HETATM 12506 O  O     . HOH Z 8 .   ? -45.488 -12.582 15.451  1.00 35.91 ? 1023 HOH B O     1 
HETATM 12507 O  O     . HOH Z 8 .   ? -30.534 -27.294 9.213   1.00 38.81 ? 1024 HOH B O     1 
HETATM 12508 O  O     . HOH Z 8 .   ? -36.696 -21.565 25.974  1.00 28.20 ? 1027 HOH B O     1 
HETATM 12509 O  O     . HOH Z 8 .   ? -9.689  -13.381 16.182  1.00 18.71 ? 1028 HOH B O     1 
HETATM 12510 O  O     . HOH Z 8 .   ? 4.225   -26.991 33.401  1.00 25.62 ? 1029 HOH B O     1 
HETATM 12511 O  O     . HOH Z 8 .   ? 14.866  -2.376  38.178  1.00 41.38 ? 1030 HOH B O     1 
HETATM 12512 O  O     . HOH Z 8 .   ? -3.218  10.013  17.368  1.00 29.24 ? 1031 HOH B O     1 
HETATM 12513 O  O     . HOH Z 8 .   ? -19.001 9.882   42.312  1.00 19.57 ? 1032 HOH B O     1 
HETATM 12514 O  O     . HOH Z 8 .   ? -22.593 16.742  20.690  1.00 39.46 ? 1033 HOH B O     1 
HETATM 12515 O  O     . HOH Z 8 .   ? -14.917 -20.276 49.029  1.00 32.61 ? 1034 HOH B O     1 
HETATM 12516 O  O     . HOH Z 8 .   ? -24.287 16.277  69.682  1.00 28.82 ? 1035 HOH B O     1 
HETATM 12517 O  O     . HOH Z 8 .   ? 7.006   9.944   15.988  1.00 47.47 ? 1036 HOH B O     1 
HETATM 12518 O  O     . HOH Z 8 .   ? -6.083  -15.969 5.843   1.00 24.25 ? 1037 HOH B O     1 
HETATM 12519 O  O     . HOH Z 8 .   ? -0.302  -33.546 43.475  1.00 39.37 ? 1038 HOH B O     1 
HETATM 12520 O  O     . HOH Z 8 .   ? -2.218  3.208   32.338  1.00 33.43 ? 1039 HOH B O     1 
HETATM 12521 O  O     . HOH Z 8 .   ? -9.178  -18.447 10.670  1.00 24.87 ? 1040 HOH B O     1 
HETATM 12522 O  O     . HOH Z 8 .   ? 7.252   5.897   34.192  1.00 49.91 ? 1041 HOH B O     1 
HETATM 12523 O  O     . HOH Z 8 .   ? 1.213   12.209  24.147  1.00 37.32 ? 1042 HOH B O     1 
HETATM 12524 O  O     . HOH Z 8 .   ? -30.996 13.931  70.863  1.00 39.70 ? 1043 HOH B O     1 
HETATM 12525 O  O     . HOH Z 8 .   ? -4.871  -13.417 28.409  1.00 28.16 ? 1044 HOH B O     1 
HETATM 12526 O  O     . HOH Z 8 .   ? 7.424   1.659   4.422   1.00 47.00 ? 1045 HOH B O     1 
HETATM 12527 O  O     . HOH Z 8 .   ? -19.083 9.398   53.151  1.00 24.77 ? 1046 HOH B O     1 
HETATM 12528 O  O     . HOH Z 8 .   ? -25.847 -8.812  -4.290  1.00 36.07 ? 1047 HOH B O     1 
HETATM 12529 O  O     . HOH Z 8 .   ? -7.899  -13.225 4.605   1.00 24.42 ? 1048 HOH B O     1 
HETATM 12530 O  O     . HOH Z 8 .   ? -3.101  -19.304 61.414  1.00 32.94 ? 1049 HOH B O     1 
HETATM 12531 O  O     . HOH Z 8 .   ? 3.475   -4.636  2.189   1.00 28.64 ? 1050 HOH B O     1 
HETATM 12532 O  O     . HOH Z 8 .   ? 1.127   -23.192 26.743  1.00 31.01 ? 1051 HOH B O     1 
HETATM 12533 O  O     . HOH Z 8 .   ? -8.475  -29.902 24.818  1.00 31.31 ? 1052 HOH B O     1 
HETATM 12534 O  O     . HOH Z 8 .   ? -24.474 15.822  41.104  1.00 31.19 ? 1053 HOH B O     1 
HETATM 12535 O  O     . HOH Z 8 .   ? -33.992 3.722   78.833  1.00 38.42 ? 1054 HOH B O     1 
HETATM 12536 O  O     . HOH Z 8 .   ? -5.490  -5.171  7.664   1.00 38.83 ? 1055 HOH B O     1 
HETATM 12537 O  O     . HOH Z 8 .   ? -22.805 0.748   11.450  1.00 38.01 ? 1056 HOH B O     1 
HETATM 12538 O  O     . HOH Z 8 .   ? -3.148  -14.477 -6.694  1.00 50.99 ? 1057 HOH B O     1 
HETATM 12539 O  O     . HOH Z 8 .   ? -0.559  -24.832 52.516  1.00 40.07 ? 1058 HOH B O     1 
HETATM 12540 O  O     . HOH Z 8 .   ? -35.249 -21.247 -13.216 1.00 35.42 ? 1059 HOH B O     1 
HETATM 12541 O  O     . HOH Z 8 .   ? 1.781   -18.685 5.614   1.00 32.80 ? 1060 HOH B O     1 
HETATM 12542 O  O     . HOH Z 8 .   ? 12.836  -8.661  42.506  1.00 39.53 ? 1061 HOH B O     1 
HETATM 12543 O  O     . HOH Z 8 .   ? -7.575  8.180   58.755  1.00 28.63 ? 1062 HOH B O     1 
HETATM 12544 O  O     . HOH Z 8 .   ? 8.442   -0.084  5.971   1.00 33.06 ? 1063 HOH B O     1 
HETATM 12545 O  O     . HOH Z 8 .   ? 8.548   -13.923 41.816  1.00 36.86 ? 1064 HOH B O     1 
HETATM 12546 O  O     . HOH Z 8 .   ? -2.776  -0.798  26.084  1.00 24.40 ? 1065 HOH B O     1 
HETATM 12547 O  O     . HOH Z 8 .   ? -40.895 -21.872 6.796   1.00 36.73 ? 1066 HOH B O     1 
HETATM 12548 O  O     . HOH Z 8 .   ? -18.345 15.371  25.048  1.00 35.64 ? 1067 HOH B O     1 
HETATM 12549 O  O     . HOH Z 8 .   ? -25.034 -30.892 69.953  1.00 37.19 ? 1068 HOH B O     1 
HETATM 12550 O  O     . HOH Z 8 .   ? -5.202  -21.233 27.336  1.00 30.08 ? 1069 HOH B O     1 
HETATM 12551 O  O     . HOH Z 8 .   ? 5.756   -2.334  49.070  1.00 34.04 ? 1070 HOH B O     1 
HETATM 12552 O  O     . HOH Z 8 .   ? -1.088  -18.754 4.208   1.00 49.50 ? 1071 HOH B O     1 
HETATM 12553 O  O     . HOH Z 8 .   ? 5.941   -13.839 17.372  1.00 39.39 ? 1072 HOH B O     1 
HETATM 12554 O  O     . HOH Z 8 .   ? -3.919  -17.915 67.859  1.00 29.46 ? 1073 HOH B O     1 
HETATM 12555 O  O     . HOH Z 8 .   ? -17.586 16.646  22.497  1.00 44.00 ? 1074 HOH B O     1 
HETATM 12556 O  O     . HOH Z 8 .   ? -31.074 11.232  38.354  1.00 46.74 ? 1075 HOH B O     1 
HETATM 12557 O  O     . HOH Z 8 .   ? -49.271 9.824   36.216  1.00 46.87 ? 1076 HOH B O     1 
HETATM 12558 O  O     . HOH Z 8 .   ? -32.954 14.125  41.248  1.00 37.73 ? 1077 HOH B O     1 
HETATM 12559 O  O     . HOH Z 8 .   ? -12.185 -3.315  28.126  1.00 30.28 ? 1078 HOH B O     1 
HETATM 12560 O  O     . HOH Z 8 .   ? -19.990 -22.118 39.792  1.00 33.49 ? 1079 HOH B O     1 
HETATM 12561 O  O     . HOH Z 8 .   ? -16.333 10.390  42.840  1.00 17.16 ? 1080 HOH B O     1 
HETATM 12562 O  O     . HOH Z 8 .   ? 4.104   -5.117  51.686  1.00 36.42 ? 1081 HOH B O     1 
HETATM 12563 O  O     . HOH Z 8 .   ? 2.097   -6.185  28.915  1.00 30.49 ? 1082 HOH B O     1 
HETATM 12564 O  O     . HOH Z 8 .   ? 5.307   -0.032  45.516  1.00 30.56 ? 1083 HOH B O     1 
HETATM 12565 O  O     . HOH Z 8 .   ? -15.224 -30.789 36.501  1.00 32.62 ? 1084 HOH B O     1 
HETATM 12566 O  O     . HOH Z 8 .   ? 11.494  -4.089  30.301  1.00 35.90 ? 1085 HOH B O     1 
HETATM 12567 O  O     . HOH Z 8 .   ? -5.705  -32.398 29.348  1.00 42.76 ? 1086 HOH B O     1 
HETATM 12568 O  O     . HOH Z 8 .   ? -27.758 17.502  62.981  1.00 25.37 ? 1087 HOH B O     1 
HETATM 12569 O  O     . HOH Z 8 .   ? -2.787  7.719   8.112   1.00 45.89 ? 1088 HOH B O     1 
HETATM 12570 O  O     . HOH Z 8 .   ? -2.829  -16.733 0.052   1.00 44.08 ? 1089 HOH B O     1 
HETATM 12571 O  O     . HOH Z 8 .   ? -19.118 15.596  67.517  1.00 28.29 ? 1090 HOH B O     1 
HETATM 12572 O  O     . HOH Z 8 .   ? -2.304  11.134  15.060  1.00 27.82 ? 1091 HOH B O     1 
HETATM 12573 O  O     . HOH Z 8 .   ? -31.414 5.650   76.123  1.00 31.54 ? 1092 HOH B O     1 
HETATM 12574 O  O     . HOH Z 8 .   ? -14.881 14.059  68.148  1.00 44.35 ? 1093 HOH B O     1 
HETATM 12575 O  O     . HOH Z 8 .   ? -38.857 -20.733 9.830   1.00 33.54 ? 1094 HOH B O     1 
HETATM 12576 O  O     . HOH Z 8 .   ? 6.070   10.916  19.013  1.00 33.74 ? 1095 HOH B O     1 
HETATM 12577 O  O     . HOH Z 8 .   ? -28.186 -7.586  40.416  1.00 31.05 ? 1096 HOH B O     1 
HETATM 12578 O  O     . HOH Z 8 .   ? -21.486 18.706  62.321  1.00 36.29 ? 1097 HOH B O     1 
HETATM 12579 O  O     . HOH Z 8 .   ? -20.868 -10.242 41.039  1.00 32.01 ? 1098 HOH B O     1 
HETATM 12580 O  O     . HOH Z 8 .   ? 2.321   -19.016 54.471  1.00 28.71 ? 1099 HOH B O     1 
HETATM 12581 O  O     . HOH Z 8 .   ? -2.560  3.648   25.530  1.00 40.58 ? 1100 HOH B O     1 
HETATM 12582 O  O     . HOH Z 8 .   ? -34.984 3.223   13.684  1.00 40.84 ? 1103 HOH B O     1 
HETATM 12583 O  O     . HOH Z 8 .   ? -22.220 -16.442 -7.110  1.00 35.76 ? 1104 HOH B O     1 
HETATM 12584 O  O     . HOH Z 8 .   ? 7.013   -0.811  47.595  1.00 30.42 ? 1105 HOH B O     1 
HETATM 12585 O  O     . HOH Z 8 .   ? -23.023 -23.305 26.542  1.00 37.15 ? 1106 HOH B O     1 
HETATM 12586 O  O     . HOH Z 8 .   ? -1.302  -10.836 32.348  1.00 21.23 ? 1107 HOH B O     1 
HETATM 12587 O  O     . HOH Z 8 .   ? -43.642 4.828   22.048  1.00 39.59 ? 1108 HOH B O     1 
HETATM 12588 O  O     . HOH Z 8 .   ? -17.457 -21.692 41.011  1.00 30.97 ? 1109 HOH B O     1 
HETATM 12589 O  O     . HOH Z 8 .   ? -18.285 15.174  15.408  1.00 44.56 ? 1110 HOH B O     1 
HETATM 12590 O  O     . HOH Z 8 .   ? -20.398 14.357  34.707  1.00 39.10 ? 1111 HOH B O     1 
HETATM 12591 O  O     . HOH Z 8 .   ? -17.196 -24.319 41.694  1.00 38.61 ? 1112 HOH B O     1 
HETATM 12592 O  O     . HOH Z 8 .   ? -43.377 -1.502  28.054  1.00 28.88 ? 1113 HOH B O     1 
HETATM 12593 O  O     . HOH Z 8 .   ? -17.746 3.277   54.148  1.00 35.92 ? 1114 HOH B O     1 
HETATM 12594 O  O     . HOH Z 8 .   ? 10.538  -6.758  46.833  1.00 41.40 ? 1115 HOH B O     1 
HETATM 12595 O  O     . HOH Z 8 .   ? -32.827 -2.667  -1.180  1.00 49.42 ? 1116 HOH B O     1 
HETATM 12596 O  O     . HOH Z 8 .   ? 4.958   10.109  26.594  1.00 43.10 ? 1117 HOH B O     1 
HETATM 12597 O  O     . HOH Z 8 .   ? -5.241  10.062  34.890  1.00 48.54 ? 1118 HOH B O     1 
HETATM 12598 O  O     . HOH Z 8 .   ? -33.913 -25.442 11.044  1.00 38.73 ? 1119 HOH B O     1 
HETATM 12599 O  O     . HOH Z 8 .   ? -3.353  5.378   50.304  1.00 35.66 ? 1120 HOH B O     1 
HETATM 12600 O  O     . HOH Z 8 .   ? -43.257 6.012   33.436  1.00 28.38 ? 1121 HOH B O     1 
HETATM 12601 O  O     . HOH Z 8 .   ? -7.178  -20.584 5.426   1.00 49.95 ? 1122 HOH B O     1 
HETATM 12602 O  O     . HOH Z 8 .   ? -24.763 -28.381 -0.055  1.00 47.14 ? 1123 HOH B O     1 
HETATM 12603 O  O     . HOH Z 8 .   ? -18.339 15.269  32.877  1.00 50.05 ? 1124 HOH B O     1 
HETATM 12604 O  O     . HOH Z 8 .   ? -20.794 -18.076 -5.126  1.00 44.40 ? 1125 HOH B O     1 
HETATM 12605 O  O     . HOH Z 8 .   ? -30.944 -15.434 -10.726 1.00 40.99 ? 1126 HOH B O     1 
HETATM 12606 O  O     . HOH Z 8 .   ? -13.353 -34.794 68.612  1.00 49.04 ? 1127 HOH B O     1 
HETATM 12607 O  O     . HOH Z 8 .   ? -37.159 2.529   16.263  1.00 38.74 ? 1128 HOH B O     1 
HETATM 12608 O  O     . HOH Z 8 .   ? -21.099 15.682  30.989  1.00 33.84 ? 1129 HOH B O     1 
HETATM 12609 O  O     . HOH Z 8 .   ? -6.465  14.113  42.218  1.00 49.07 ? 1130 HOH B O     1 
HETATM 12610 O  O     . HOH Z 8 .   ? 7.945   -9.382  4.135   1.00 40.09 ? 1131 HOH B O     1 
HETATM 12611 O  O     . HOH Z 8 .   ? 4.418   -9.698  35.138  1.00 33.88 ? 1132 HOH B O     1 
HETATM 12612 O  O     . HOH Z 8 .   ? -29.863 11.570  75.970  1.00 31.42 ? 1133 HOH B O     1 
HETATM 12613 O  O     . HOH Z 8 .   ? -10.401 12.855  40.189  1.00 27.12 ? 1134 HOH B O     1 
HETATM 12614 O  O     . HOH Z 8 .   ? -5.897  -19.955 61.239  1.00 51.04 ? 1135 HOH B O     1 
HETATM 12615 O  O     . HOH Z 8 .   ? -23.839 16.221  22.929  1.00 33.59 ? 1136 HOH B O     1 
HETATM 12616 O  O     . HOH Z 8 .   ? -25.681 4.953   45.227  1.00 30.60 ? 1137 HOH B O     1 
HETATM 12617 O  O     . HOH Z 8 .   ? 4.419   -19.474 52.892  1.00 37.48 ? 1138 HOH B O     1 
HETATM 12618 O  O     . HOH Z 8 .   ? -10.844 3.888   14.594  1.00 37.38 ? 1139 HOH B O     1 
HETATM 12619 O  O     . HOH Z 8 .   ? -9.584  2.727   16.713  1.00 36.63 ? 1140 HOH B O     1 
HETATM 12620 O  O     . HOH Z 8 .   ? -21.266 -18.066 44.252  1.00 43.89 ? 1141 HOH B O     1 
HETATM 12621 O  O     . HOH Z 8 .   ? -11.488 9.478   57.072  1.00 33.68 ? 1142 HOH B O     1 
HETATM 12622 O  O     . HOH Z 8 .   ? -21.950 0.201   77.788  1.00 33.53 ? 1143 HOH B O     1 
HETATM 12623 O  O     . HOH Z 8 .   ? -2.882  -29.505 19.587  1.00 53.38 ? 1144 HOH B O     1 
HETATM 12624 O  O     . HOH Z 8 .   ? 8.784   -27.585 42.483  1.00 37.36 ? 1145 HOH B O     1 
HETATM 12625 O  O     . HOH Z 8 .   ? 9.465   0.363   32.301  1.00 32.57 ? 1146 HOH B O     1 
HETATM 12626 O  O     . HOH Z 8 .   ? -38.989 -8.602  11.907  1.00 33.57 ? 1147 HOH B O     1 
HETATM 12627 O  O     . HOH Z 8 .   ? -11.378 4.724   52.011  1.00 38.40 ? 1148 HOH B O     1 
HETATM 12628 O  O     . HOH Z 8 .   ? -0.862  -31.748 36.965  1.00 38.51 ? 1149 HOH B O     1 
HETATM 12629 O  O     . HOH Z 8 .   ? -26.912 1.232   -1.707  1.00 27.11 ? 1150 HOH B O     1 
HETATM 12630 O  O     . HOH Z 8 .   ? -3.447  -11.876 26.944  1.00 29.70 ? 1151 HOH B O     1 
HETATM 12631 O  O     . HOH Z 8 .   ? -10.131 -7.368  15.125  1.00 29.09 ? 1152 HOH B O     1 
HETATM 12632 O  O     . HOH Z 8 .   ? -4.825  -4.042  10.153  1.00 29.61 ? 1153 HOH B O     1 
HETATM 12633 O  O     . HOH Z 8 .   ? -17.631 -26.632 14.161  1.00 38.73 ? 1154 HOH B O     1 
HETATM 12634 O  O     . HOH Z 8 .   ? -12.356 12.826  30.019  1.00 40.00 ? 1155 HOH B O     1 
HETATM 12635 O  O     . HOH Z 8 .   ? 7.495   -1.515  29.493  1.00 33.63 ? 1156 HOH B O     1 
HETATM 12636 O  O     . HOH Z 8 .   ? -5.053  -28.892 10.516  1.00 49.08 ? 1157 HOH B O     1 
HETATM 12637 O  O     . HOH Z 8 .   ? -16.748 -1.880  18.581  1.00 41.98 ? 1158 HOH B O     1 
HETATM 12638 O  O     . HOH Z 8 .   ? -9.325  -33.025 20.000  1.00 38.26 ? 1159 HOH B O     1 
HETATM 12639 O  O     . HOH Z 8 .   ? 0.484   -5.676  32.020  1.00 45.31 ? 1160 HOH B O     1 
HETATM 12640 O  O     . HOH Z 8 .   ? -9.742  -18.173 -0.121  1.00 35.29 ? 1161 HOH B O     1 
HETATM 12641 O  O     . HOH Z 8 .   ? -28.125 -26.754 10.489  1.00 34.43 ? 1162 HOH B O     1 
HETATM 12642 O  O     . HOH Z 8 .   ? -22.400 -26.652 31.283  1.00 33.49 ? 1163 HOH B O     1 
HETATM 12643 O  O     . HOH Z 8 .   ? 6.112   -17.339 7.164   1.00 37.96 ? 1164 HOH B O     1 
HETATM 12644 O  O     . HOH Z 8 .   ? -7.319  -29.242 60.980  1.00 38.33 ? 1165 HOH B O     1 
HETATM 12645 O  O     . HOH Z 8 .   ? -5.118  -9.444  7.421   1.00 25.66 ? 1166 HOH B O     1 
HETATM 12646 O  O     . HOH Z 8 .   ? -1.984  -19.114 16.627  1.00 33.13 ? 1167 HOH B O     1 
HETATM 12647 O  O     . HOH Z 8 .   ? -42.485 -1.211  19.842  1.00 40.12 ? 1168 HOH B O     1 
HETATM 12648 O  O     . HOH Z 8 .   ? 8.369   -13.990 0.070   1.00 51.09 ? 1169 HOH B O     1 
HETATM 12649 O  O     . HOH Z 8 .   ? -15.118 -25.428 15.372  1.00 40.57 ? 1170 HOH B O     1 
HETATM 12650 O  O     . HOH Z 8 .   ? 1.055   -4.821  -1.734  1.00 44.17 ? 1171 HOH B O     1 
HETATM 12651 O  O     . HOH Z 8 .   ? 1.802   -9.802  33.945  1.00 36.71 ? 1172 HOH B O     1 
HETATM 12652 O  O     . HOH Z 8 .   ? -17.975 -16.208 54.830  1.00 36.53 ? 1173 HOH B O     1 
HETATM 12653 O  O     . HOH Z 8 .   ? -30.032 -2.844  -8.318  1.00 29.14 ? 1174 HOH B O     1 
HETATM 12654 O  O     . HOH Z 8 .   ? -44.698 4.263   31.987  1.00 46.05 ? 1175 HOH B O     1 
HETATM 12655 O  O     . HOH Z 8 .   ? 1.388   -6.511  26.075  1.00 38.64 ? 1176 HOH B O     1 
HETATM 12656 O  O     . HOH Z 8 .   ? 1.308   -23.071 6.014   1.00 46.13 ? 1177 HOH B O     1 
HETATM 12657 O  O     . HOH Z 8 .   ? -3.341  -30.656 55.004  1.00 37.65 ? 1178 HOH B O     1 
HETATM 12658 O  O     . HOH Z 8 .   ? 15.253  1.361   6.240   1.00 43.52 ? 1179 HOH B O     1 
HETATM 12659 O  O     . HOH Z 8 .   ? -25.936 15.586  64.178  1.00 42.04 ? 1180 HOH B O     1 
HETATM 12660 O  O     . HOH Z 8 .   ? -17.427 -26.712 50.282  1.00 34.72 ? 1181 HOH B O     1 
HETATM 12661 O  O     . HOH Z 8 .   ? -28.118 1.423   5.073   1.00 39.35 ? 1182 HOH B O     1 
HETATM 12662 O  O     . HOH Z 8 .   ? -11.819 -8.778  56.154  1.00 35.04 ? 1183 HOH B O     1 
HETATM 12663 O  O     . HOH Z 8 .   ? 4.377   -13.034 52.703  1.00 35.08 ? 1184 HOH B O     1 
HETATM 12664 O  O     . HOH Z 8 .   ? 2.752   -11.417 23.047  1.00 55.94 ? 1185 HOH B O     1 
HETATM 12665 O  O     . HOH Z 8 .   ? -15.231 -26.375 42.391  1.00 43.94 ? 1186 HOH B O     1 
HETATM 12666 O  O     . HOH Z 8 .   ? -12.120 16.289  47.842  1.00 28.30 ? 1187 HOH B O     1 
HETATM 12667 O  O     . HOH Z 8 .   ? -1.985  14.264  22.256  1.00 47.54 ? 1188 HOH B O     1 
HETATM 12668 O  O     . HOH Z 8 .   ? 1.167   -0.558  9.551   1.00 43.44 ? 1189 HOH B O     1 
HETATM 12669 O  O     . HOH Z 8 .   ? -43.420 -22.568 14.460  1.00 37.43 ? 1190 HOH B O     1 
HETATM 12670 O  O     . HOH Z 8 .   ? -16.940 16.489  42.276  1.00 40.22 ? 1191 HOH B O     1 
HETATM 12671 O  O     . HOH Z 8 .   ? -5.261  -30.510 27.277  1.00 37.31 ? 1192 HOH B O     1 
HETATM 12672 O  O     . HOH Z 8 .   ? 0.897   13.980  22.432  1.00 40.92 ? 1193 HOH B O     1 
HETATM 12673 O  O     . HOH Z 8 .   ? -2.895  6.242   26.445  1.00 46.32 ? 1194 HOH B O     1 
HETATM 12674 O  O     . HOH Z 8 .   ? -35.902 -27.301 24.269  1.00 42.35 ? 1195 HOH B O     1 
HETATM 12675 O  O     . HOH Z 8 .   ? 12.390  1.242   46.599  1.00 51.60 ? 1196 HOH B O     1 
HETATM 12676 O  O     . HOH Z 8 .   ? -19.780 14.508  57.258  1.00 40.72 ? 1197 HOH B O     1 
HETATM 12677 O  O     . HOH Z 8 .   ? -2.506  9.079   43.238  1.00 38.75 ? 1198 HOH B O     1 
HETATM 12678 O  O     . HOH Z 8 .   ? -12.830 5.988   53.902  1.00 45.05 ? 1199 HOH B O     1 
HETATM 12679 O  O     . HOH Z 8 .   ? -2.784  -32.213 32.183  1.00 50.31 ? 1200 HOH B O     1 
HETATM 12680 O  O     . HOH Z 8 .   ? -44.896 -0.287  20.818  1.00 47.86 ? 1201 HOH B O     1 
HETATM 12681 O  O     . HOH Z 8 .   ? -0.144  -17.240 15.750  1.00 40.98 ? 1202 HOH B O     1 
HETATM 12682 O  O     . HOH Z 8 .   ? -25.452 -10.731 39.684  1.00 34.14 ? 1203 HOH B O     1 
HETATM 12683 O  O     . HOH Z 8 .   ? 3.511   -23.723 53.376  1.00 40.25 ? 1204 HOH B O     1 
HETATM 12684 O  O     . HOH Z 8 .   ? 2.388   -20.714 2.537   1.00 49.45 ? 1205 HOH B O     1 
HETATM 12685 O  O     . HOH Z 8 .   ? -3.422  -21.823 6.897   1.00 38.12 ? 1206 HOH B O     1 
HETATM 12686 O  O     . HOH Z 8 .   ? 8.902   6.714   10.092  1.00 53.11 ? 1207 HOH B 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   ARG 1   21  ?   ?   ?   A . n 
A 1 2   SER 2   22  ?   ?   ?   A . n 
A 1 3   PRO 3   23  ?   ?   ?   A . n 
A 1 4   GLY 4   24  ?   ?   ?   A . n 
A 1 5   THR 5   25  ?   ?   ?   A . n 
A 1 6   LEU 6   26  ?   ?   ?   A . n 
A 1 7   PRO 7   27  27  PRO PRO A . n 
A 1 8   ARG 8   28  28  ARG ARG A . n 
A 1 9   LYS 9   29  29  LYS LYS A . n 
A 1 10  ALA 10  30  30  ALA ALA A . n 
A 1 11  GLY 11  31  31  GLY GLY A . n 
A 1 12  VAL 12  32  32  VAL VAL A . n 
A 1 13  PHE 13  33  33  PHE PHE A . n 
A 1 14  SER 14  34  34  SER SER A . n 
A 1 15  ASP 15  35  35  ASP ASP A . n 
A 1 16  LEU 16  36  36  LEU LEU A . n 
A 1 17  SER 17  37  37  SER SER A . n 
A 1 18  ASN 18  38  38  ASN ASN A . n 
A 1 19  GLN 19  39  39  GLN GLN A . n 
A 1 20  GLU 20  40  40  GLU GLU A . n 
A 1 21  LEU 21  41  41  LEU LEU A . n 
A 1 22  LYS 22  42  42  LYS LYS A . n 
A 1 23  ALA 23  43  43  ALA ALA A . n 
A 1 24  VAL 24  44  44  VAL VAL A . n 
A 1 25  HIS 25  45  45  HIS HIS A . n 
A 1 26  SER 26  46  46  SER SER A . n 
A 1 27  PHE 27  47  47  PHE PHE A . n 
A 1 28  LEU 28  48  48  LEU LEU A . n 
A 1 29  TRP 29  49  49  TRP TRP A . n 
A 1 30  SER 30  50  50  SER SER A . n 
A 1 31  LYS 31  51  51  LYS LYS A . n 
A 1 32  LYS 32  52  52  LYS LYS A . n 
A 1 33  GLU 33  53  53  GLU GLU A . n 
A 1 34  LEU 34  54  54  LEU LEU A . n 
A 1 35  ARG 35  55  55  ARG ARG A . n 
A 1 36  LEU 36  56  56  LEU LEU A . n 
A 1 37  GLN 37  57  57  GLN GLN A . n 
A 1 38  PRO 38  58  58  PRO PRO A . n 
A 1 39  SER 39  59  59  SER SER A . n 
A 1 40  SER 40  60  60  SER SER A . n 
A 1 41  THR 41  61  61  THR THR A . n 
A 1 42  THR 42  62  62  THR THR A . n 
A 1 43  THR 43  63  63  THR THR A . n 
A 1 44  MET 44  64  64  MET MET A . n 
A 1 45  ALA 45  65  65  ALA ALA A . n 
A 1 46  LYS 46  66  66  LYS LYS A . n 
A 1 47  ASN 47  67  67  ASN ASN A . n 
A 1 48  THR 48  68  68  THR THR A . n 
A 1 49  VAL 49  69  69  VAL VAL A . n 
A 1 50  PHE 50  70  70  PHE PHE A . n 
A 1 51  LEU 51  71  71  LEU LEU A . n 
A 1 52  ILE 52  72  72  ILE ILE A . n 
A 1 53  GLU 53  73  73  GLU GLU A . n 
A 1 54  MET 54  74  74  MET MET A . n 
A 1 55  LEU 55  75  75  LEU LEU A . n 
A 1 56  LEU 56  76  76  LEU LEU A . n 
A 1 57  PRO 57  77  77  PRO PRO A . n 
A 1 58  LYS 58  78  78  LYS LYS A . n 
A 1 59  LYS 59  79  79  LYS LYS A . n 
A 1 60  TYR 60  80  80  TYR TYR A . n 
A 1 61  HIS 61  81  81  HIS HIS A . n 
A 1 62  VAL 62  82  82  VAL VAL A . n 
A 1 63  LEU 63  83  83  LEU LEU A . n 
A 1 64  ARG 64  84  84  ARG ARG A . n 
A 1 65  PHE 65  85  85  PHE PHE A . n 
A 1 66  LEU 66  86  86  LEU LEU A . n 
A 1 67  ASP 67  87  87  ASP ASP A . n 
A 1 68  LYS 68  88  88  LYS LYS A . n 
A 1 69  GLY 69  89  89  GLY GLY A . n 
A 1 70  GLU 70  90  90  GLU GLU A . n 
A 1 71  ARG 71  91  91  ARG ARG A . n 
A 1 72  HIS 72  92  92  HIS HIS A . n 
A 1 73  PRO 73  93  93  PRO PRO A . n 
A 1 74  VAL 74  94  94  VAL VAL A . n 
A 1 75  ARG 75  95  95  ARG ARG A . n 
A 1 76  GLU 76  96  96  GLU GLU A . n 
A 1 77  ALA 77  97  97  ALA ALA A . n 
A 1 78  ARG 78  98  98  ARG ARG A . n 
A 1 79  ALA 79  99  99  ALA ALA A . n 
A 1 80  VAL 80  100 100 VAL VAL A . n 
A 1 81  ILE 81  101 101 ILE ILE A . n 
A 1 82  PHE 82  102 102 PHE PHE A . n 
A 1 83  PHE 83  103 103 PHE PHE A . n 
A 1 84  GLY 84  104 104 GLY GLY A . n 
A 1 85  ASP 85  105 105 ASP ASP A . n 
A 1 86  GLN 86  106 106 GLN GLN A . n 
A 1 87  GLU 87  107 107 GLU GLU A . n 
A 1 88  HIS 88  108 108 HIS HIS A . n 
A 1 89  PRO 89  109 109 PRO PRO A . n 
A 1 90  ASN 90  110 110 ASN ASN A . n 
A 1 91  VAL 91  111 111 VAL VAL A . n 
A 1 92  THR 92  112 112 THR THR A . n 
A 1 93  GLU 93  113 113 GLU GLU A . n 
A 1 94  PHE 94  114 114 PHE PHE A . n 
A 1 95  ALA 95  115 115 ALA ALA A . n 
A 1 96  VAL 96  116 116 VAL VAL A . n 
A 1 97  GLY 97  117 117 GLY GLY A . n 
A 1 98  PRO 98  118 118 PRO PRO A . n 
A 1 99  LEU 99  119 119 LEU LEU A . n 
A 1 100 PRO 100 120 120 PRO PRO A . n 
A 1 101 GLY 101 121 121 GLY GLY A . n 
A 1 102 PRO 102 122 122 PRO PRO A . n 
A 1 103 CYS 103 123 123 CYS CYS A . n 
A 1 104 TYR 104 124 124 TYR TYR A . n 
A 1 105 MET 105 125 125 MET MET A . n 
A 1 106 ARG 106 126 126 ARG ARG A . n 
A 1 107 ALA 107 127 127 ALA ALA A . n 
A 1 108 LEU 108 128 128 LEU LEU A . n 
A 1 109 SER 109 129 129 SER SER A . n 
A 1 110 PRO 110 130 130 PRO PRO A . n 
A 1 111 ARG 111 131 131 ARG ARG A . n 
A 1 112 PRO 112 132 132 PRO PRO A . n 
A 1 113 GLY 113 133 133 GLY GLY A . n 
A 1 114 TYR 114 134 134 TYR TYR A . n 
A 1 115 GLN 115 135 135 GLN GLN A . n 
A 1 116 SER 116 136 136 SER SER A . n 
A 1 117 SER 117 137 137 SER SER A . n 
A 1 118 TRP 118 138 138 TRP TRP A . n 
A 1 119 ALA 119 139 139 ALA ALA A . n 
A 1 120 SER 120 140 140 SER SER A . n 
A 1 121 ARG 121 141 141 ARG ARG A . n 
A 1 122 PRO 122 142 142 PRO PRO A . n 
A 1 123 ILE 123 143 143 ILE ILE A . n 
A 1 124 SER 124 144 144 SER SER A . n 
A 1 125 THR 125 145 145 THR THR A . n 
A 1 126 ALA 126 146 146 ALA ALA A . n 
A 1 127 GLU 127 147 147 GLU GLU A . n 
A 1 128 TYR 128 148 148 TYR TYR A . n 
A 1 129 ALA 129 149 149 ALA ALA A . n 
A 1 130 LEU 130 150 150 LEU LEU A . n 
A 1 131 LEU 131 151 151 LEU LEU A . n 
A 1 132 TYR 132 152 152 TYR TYR A . n 
A 1 133 HIS 133 153 153 HIS HIS A . n 
A 1 134 THR 134 154 154 THR THR A . n 
A 1 135 LEU 135 155 155 LEU LEU A . n 
A 1 136 GLN 136 156 156 GLN GLN A . n 
A 1 137 GLU 137 157 157 GLU GLU A . n 
A 1 138 ALA 138 158 158 ALA ALA A . n 
A 1 139 THR 139 159 159 THR THR A . n 
A 1 140 LYS 140 160 160 LYS LYS A . n 
A 1 141 PRO 141 161 161 PRO PRO A . n 
A 1 142 LEU 142 162 162 LEU LEU A . n 
A 1 143 HIS 143 163 163 HIS HIS A . n 
A 1 144 GLN 144 164 164 GLN GLN A . n 
A 1 145 PHE 145 165 165 PHE PHE A . n 
A 1 146 PHE 146 166 166 PHE PHE A . n 
A 1 147 LEU 147 167 167 LEU LEU A . n 
A 1 148 ASN 148 168 168 ASN ASN A . n 
A 1 149 THR 149 169 169 THR THR A . n 
A 1 150 THR 150 170 170 THR THR A . n 
A 1 151 GLY 151 171 171 GLY GLY A . n 
A 1 152 PHE 152 172 172 PHE PHE A . n 
A 1 153 SER 153 173 173 SER SER A . n 
A 1 154 PHE 154 174 174 PHE PHE A . n 
A 1 155 GLN 155 175 175 GLN GLN A . n 
A 1 156 ASP 156 176 176 ASP ASP A . n 
A 1 157 CYS 157 177 177 CYS CYS A . n 
A 1 158 HIS 158 178 178 HIS HIS A . n 
A 1 159 ASP 159 179 179 ASP ASP A . n 
A 1 160 ARG 160 180 180 ARG ARG A . n 
A 1 161 CYS 161 181 181 CYS CYS A . n 
A 1 162 LEU 162 182 182 LEU LEU A . n 
A 1 163 ALA 163 183 183 ALA ALA A . n 
A 1 164 PHE 164 184 184 PHE PHE A . n 
A 1 165 THR 165 185 185 THR THR A . n 
A 1 166 ASP 166 186 186 ASP ASP A . n 
A 1 167 VAL 167 187 187 VAL VAL A . n 
A 1 168 ALA 168 188 188 ALA ALA A . n 
A 1 169 PRO 169 189 189 PRO PRO A . n 
A 1 170 ARG 170 190 190 ARG ARG A . n 
A 1 171 GLY 171 191 191 GLY GLY A . n 
A 1 172 VAL 172 192 192 VAL VAL A . n 
A 1 173 ALA 173 193 193 ALA ALA A . n 
A 1 174 SER 174 194 194 SER SER A . n 
A 1 175 GLY 175 195 195 GLY GLY A . n 
A 1 176 GLN 176 196 196 GLN GLN A . n 
A 1 177 ARG 177 197 197 ARG ARG A . n 
A 1 178 ARG 178 198 198 ARG ARG A . n 
A 1 179 SER 179 199 199 SER SER A . n 
A 1 180 TRP 180 200 200 TRP TRP A . n 
A 1 181 LEU 181 201 201 LEU LEU A . n 
A 1 182 ILE 182 202 202 ILE ILE A . n 
A 1 183 ILE 183 203 203 ILE ILE A . n 
A 1 184 GLN 184 204 204 GLN GLN A . n 
A 1 185 ARG 185 205 205 ARG ARG A . n 
A 1 186 TYR 186 206 206 TYR TYR A . n 
A 1 187 VAL 187 207 207 VAL VAL A . n 
A 1 188 GLU 188 208 208 GLU GLU A . n 
A 1 189 GLY 189 209 209 GLY GLY A . n 
A 1 190 TYR 190 210 210 TYR TYR A . n 
A 1 191 PHE 191 211 211 PHE PHE A . n 
A 1 192 LEU 192 212 212 LEU LEU A . n 
A 1 193 HIS 193 213 213 HIS HIS A . n 
A 1 194 PRO 194 214 214 PRO PRO A . n 
A 1 195 THR 195 215 215 THR THR A . n 
A 1 196 GLY 196 216 216 GLY GLY A . n 
A 1 197 LEU 197 217 217 LEU LEU A . n 
A 1 198 GLU 198 218 218 GLU GLU A . n 
A 1 199 LEU 199 219 219 LEU LEU A . n 
A 1 200 LEU 200 220 220 LEU LEU A . n 
A 1 201 VAL 201 221 221 VAL VAL A . n 
A 1 202 ASP 202 222 222 ASP ASP A . n 
A 1 203 HIS 203 223 223 HIS HIS A . n 
A 1 204 GLY 204 224 224 GLY GLY A . n 
A 1 205 SER 205 225 225 SER SER A . n 
A 1 206 THR 206 226 226 THR THR A . n 
A 1 207 ASP 207 227 227 ASP ASP A . n 
A 1 208 ALA 208 228 228 ALA ALA A . n 
A 1 209 GLY 209 229 229 GLY GLY A . n 
A 1 210 HIS 210 230 230 HIS HIS A . n 
A 1 211 TRP 211 231 231 TRP TRP A . n 
A 1 212 ALA 212 232 232 ALA ALA A . n 
A 1 213 VAL 213 233 233 VAL VAL A . n 
A 1 214 GLU 214 234 234 GLU GLU A . n 
A 1 215 GLN 215 235 235 GLN GLN A . n 
A 1 216 VAL 216 236 236 VAL VAL A . n 
A 1 217 TRP 217 237 237 TRP TRP A . n 
A 1 218 TYR 218 238 238 TYR TYR A . n 
A 1 219 ASN 219 239 239 ASN ASN A . n 
A 1 220 GLY 220 240 240 GLY GLY A . n 
A 1 221 LYS 221 241 241 LYS LYS A . n 
A 1 222 PHE 222 242 242 PHE PHE A . n 
A 1 223 TYR 223 243 243 TYR TYR A . n 
A 1 224 GLY 224 244 244 GLY GLY A . n 
A 1 225 SER 225 245 245 SER SER A . n 
A 1 226 PRO 226 246 246 PRO PRO A . n 
A 1 227 GLU 227 247 247 GLU GLU A . n 
A 1 228 GLU 228 248 248 GLU GLU A . n 
A 1 229 LEU 229 249 249 LEU LEU A . n 
A 1 230 ALA 230 250 250 ALA ALA A . n 
A 1 231 ARG 231 251 251 ARG ARG A . n 
A 1 232 LYS 232 252 252 LYS LYS A . n 
A 1 233 TYR 233 253 253 TYR TYR A . n 
A 1 234 ALA 234 254 254 ALA ALA A . n 
A 1 235 ASP 235 255 255 ASP ASP A . n 
A 1 236 GLY 236 256 256 GLY GLY A . n 
A 1 237 GLU 237 257 257 GLU GLU A . n 
A 1 238 VAL 238 258 258 VAL VAL A . n 
A 1 239 ASP 239 259 259 ASP ASP A . n 
A 1 240 VAL 240 260 260 VAL VAL A . n 
A 1 241 VAL 241 261 261 VAL VAL A . n 
A 1 242 VAL 242 262 262 VAL VAL A . n 
A 1 243 LEU 243 263 263 LEU LEU A . n 
A 1 244 GLU 244 264 264 GLU GLU A . n 
A 1 245 ASP 245 265 265 ASP ASP A . n 
A 1 246 PRO 246 266 266 PRO PRO A . n 
A 1 247 LEU 247 267 267 LEU LEU A . n 
A 1 248 PRO 248 268 ?   ?   ?   A . n 
A 1 249 GLY 249 269 ?   ?   ?   A . n 
A 1 250 GLY 250 270 ?   ?   ?   A . n 
A 1 251 LYS 251 271 ?   ?   ?   A . n 
A 1 252 GLY 252 272 ?   ?   ?   A . n 
A 1 253 HIS 253 273 ?   ?   ?   A . n 
A 1 254 ASP 254 274 ?   ?   ?   A . n 
A 1 255 SER 255 275 ?   ?   ?   A . n 
A 1 256 THR 256 276 ?   ?   ?   A . n 
A 1 257 GLU 257 277 ?   ?   ?   A . n 
A 1 258 GLU 258 278 278 GLU GLU A . n 
A 1 259 PRO 259 279 279 PRO PRO A . n 
A 1 260 PRO 260 280 280 PRO PRO A . n 
A 1 261 LEU 261 281 281 LEU LEU A . n 
A 1 262 PHE 262 282 282 PHE PHE A . n 
A 1 263 SER 263 283 283 SER SER A . n 
A 1 264 SER 264 284 284 SER SER A . n 
A 1 265 HIS 265 285 285 HIS HIS A . n 
A 1 266 LYS 266 286 286 LYS LYS A . n 
A 1 267 PRO 267 287 287 PRO PRO A . n 
A 1 268 ARG 268 288 288 ARG ARG A . n 
A 1 269 GLY 269 289 289 GLY GLY A . n 
A 1 270 ASP 270 290 290 ASP ASP A . n 
A 1 271 PHE 271 291 291 PHE PHE A . n 
A 1 272 PRO 272 292 292 PRO PRO A . n 
A 1 273 SER 273 293 293 SER SER A . n 
A 1 274 PRO 274 294 294 PRO PRO A . n 
A 1 275 ILE 275 295 295 ILE ILE A . n 
A 1 276 HIS 276 296 296 HIS HIS A . n 
A 1 277 VAL 277 297 297 VAL VAL A . n 
A 1 278 SER 278 298 298 SER SER A . n 
A 1 279 GLY 279 299 299 GLY GLY A . n 
A 1 280 PRO 280 300 300 PRO PRO A . n 
A 1 281 ARG 281 301 301 ARG ARG A . n 
A 1 282 LEU 282 302 302 LEU LEU A . n 
A 1 283 VAL 283 303 303 VAL VAL A . n 
A 1 284 GLN 284 304 304 GLN GLN A . n 
A 1 285 PRO 285 305 305 PRO PRO A . n 
A 1 286 HIS 286 306 306 HIS HIS A . n 
A 1 287 GLY 287 307 307 GLY GLY A . n 
A 1 288 PRO 288 308 308 PRO PRO A . n 
A 1 289 ARG 289 309 309 ARG ARG A . n 
A 1 290 PHE 290 310 310 PHE PHE A . n 
A 1 291 ARG 291 311 311 ARG ARG A . n 
A 1 292 LEU 292 312 312 LEU LEU A . n 
A 1 293 GLU 293 313 313 GLU GLU A . n 
A 1 294 GLY 294 314 314 GLY GLY A . n 
A 1 295 ASN 295 315 315 ASN ASN A . n 
A 1 296 ALA 296 316 316 ALA ALA A . n 
A 1 297 VAL 297 317 317 VAL VAL A . n 
A 1 298 LEU 298 318 318 LEU LEU A . n 
A 1 299 TYR 299 319 319 TYR TYR A . n 
A 1 300 GLY 300 320 320 GLY GLY A . n 
A 1 301 GLY 301 321 321 GLY GLY A . n 
A 1 302 TRP 302 322 322 TRP TRP A . n 
A 1 303 SER 303 323 323 SER SER A . n 
A 1 304 PHE 304 324 324 PHE PHE A . n 
A 1 305 ALA 305 325 325 ALA ALA A . n 
A 1 306 PHE 306 326 326 PHE PHE A . n 
A 1 307 ARG 307 327 327 ARG ARG A . n 
A 1 308 LEU 308 328 328 LEU LEU A . n 
A 1 309 ARG 309 329 329 ARG ARG A . n 
A 1 310 SER 310 330 330 SER SER A . n 
A 1 311 SER 311 331 331 SER SER A . n 
A 1 312 SER 312 332 332 SER SER A . n 
A 1 313 GLY 313 333 333 GLY GLY A . n 
A 1 314 LEU 314 334 334 LEU LEU A . n 
A 1 315 GLN 315 335 335 GLN GLN A . n 
A 1 316 VAL 316 336 336 VAL VAL A . n 
A 1 317 LEU 317 337 337 LEU LEU A . n 
A 1 318 ASN 318 338 338 ASN ASN A . n 
A 1 319 VAL 319 339 339 VAL VAL A . n 
A 1 320 HIS 320 340 340 HIS HIS A . n 
A 1 321 PHE 321 341 341 PHE PHE A . n 
A 1 322 GLY 322 342 342 GLY GLY A . n 
A 1 323 GLY 323 343 343 GLY GLY A . n 
A 1 324 GLU 324 344 344 GLU GLU A . n 
A 1 325 ARG 325 345 345 ARG ARG A . n 
A 1 326 ILE 326 346 346 ILE ILE A . n 
A 1 327 ALA 327 347 347 ALA ALA A . n 
A 1 328 TYR 328 348 348 TYR TYR A . n 
A 1 329 GLU 329 349 349 GLU GLU A . n 
A 1 330 VAL 330 350 350 VAL VAL A . n 
A 1 331 SER 331 351 351 SER SER A . n 
A 1 332 VAL 332 352 352 VAL VAL A . n 
A 1 333 GLN 333 353 353 GLN GLN A . n 
A 1 334 GLU 334 354 354 GLU GLU A . n 
A 1 335 ALA 335 355 355 ALA ALA A . n 
A 1 336 VAL 336 356 356 VAL VAL A . n 
A 1 337 ALA 337 357 357 ALA ALA A . n 
A 1 338 LEU 338 358 358 LEU LEU A . n 
A 1 339 TYR 339 359 359 TYR TYR A . n 
A 1 340 GLY 340 360 360 GLY GLY A . n 
A 1 341 GLY 341 361 361 GLY GLY A . n 
A 1 342 HIS 342 362 362 HIS HIS A . n 
A 1 343 THR 343 363 363 THR THR A . n 
A 1 344 PRO 344 364 364 PRO PRO A . n 
A 1 345 ALA 345 365 365 ALA ALA A . n 
A 1 346 GLY 346 366 366 GLY GLY A . n 
A 1 347 MET 347 367 367 MET MET A . n 
A 1 348 GLN 348 368 368 GLN GLN A . n 
A 1 349 THR 349 369 369 THR THR A . n 
A 1 350 LYS 350 370 370 LYS LYS A . n 
A 1 351 TYR 351 371 371 TYR TYR A . n 
A 1 352 LEU 352 372 372 LEU LEU A . n 
A 1 353 ASP 353 373 373 ASP ASP A . n 
A 1 354 VAL 354 374 374 VAL VAL A . n 
A 1 355 GLY 355 375 375 GLY GLY A . n 
A 1 356 TRP 356 376 376 TRP TRP A . n 
A 1 357 GLY 357 377 377 GLY GLY A . n 
A 1 358 LEU 358 378 378 LEU LEU A . n 
A 1 359 GLY 359 379 379 GLY GLY A . n 
A 1 360 SER 360 380 380 SER SER A . n 
A 1 361 VAL 361 381 381 VAL VAL A . n 
A 1 362 THR 362 382 382 THR THR A . n 
A 1 363 HIS 363 383 383 HIS HIS A . n 
A 1 364 GLU 364 384 384 GLU GLU A . n 
A 1 365 LEU 365 385 385 LEU LEU A . n 
A 1 366 ALA 366 386 386 ALA ALA A . n 
A 1 367 PRO 367 387 387 PRO PRO A . n 
A 1 368 GLY 368 388 388 GLY GLY A . n 
A 1 369 ILE 369 389 389 ILE ILE A . n 
A 1 370 ASP 370 390 390 ASP ASP A . n 
A 1 371 CYS 371 391 391 CYS CYS A . n 
A 1 372 PRO 372 392 392 PRO PRO A . n 
A 1 373 GLU 373 393 393 GLU GLU A . n 
A 1 374 THR 374 394 394 THR THR A . n 
A 1 375 ALA 375 395 395 ALA ALA A . n 
A 1 376 THR 376 396 396 THR THR A . n 
A 1 377 PHE 377 397 397 PHE PHE A . n 
A 1 378 LEU 378 398 398 LEU LEU A . n 
A 1 379 ASP 379 399 399 ASP ASP A . n 
A 1 380 THR 380 400 400 THR THR A . n 
A 1 381 PHE 381 401 401 PHE PHE A . n 
A 1 382 HIS 382 402 402 HIS HIS A . n 
A 1 383 TYR 383 403 403 TYR TYR A . n 
A 1 384 TYR 384 404 404 TYR TYR A . n 
A 1 385 ASP 385 405 405 ASP ASP A . n 
A 1 386 ALA 386 406 406 ALA ALA A . n 
A 1 387 ASP 387 407 407 ASP ASP A . n 
A 1 388 ASP 388 408 408 ASP ASP A . n 
A 1 389 PRO 389 409 409 PRO PRO A . n 
A 1 390 VAL 390 410 410 VAL VAL A . n 
A 1 391 HIS 391 411 411 HIS HIS A . n 
A 1 392 TYR 392 412 412 TYR TYR A . n 
A 1 393 PRO 393 413 413 PRO PRO A . n 
A 1 394 ARG 394 414 414 ARG ARG A . n 
A 1 395 ALA 395 415 415 ALA ALA A . n 
A 1 396 LEU 396 416 416 LEU LEU A . n 
A 1 397 CYS 397 417 417 CYS CYS A . n 
A 1 398 LEU 398 418 418 LEU LEU A . n 
A 1 399 PHE 399 419 419 PHE PHE A . n 
A 1 400 GLU 400 420 420 GLU GLU A . n 
A 1 401 MET 401 421 421 MET MET A . n 
A 1 402 PRO 402 422 422 PRO PRO A . n 
A 1 403 THR 403 423 423 THR THR A . n 
A 1 404 GLY 404 424 424 GLY GLY A . n 
A 1 405 VAL 405 425 425 VAL VAL A . n 
A 1 406 PRO 406 426 426 PRO PRO A . n 
A 1 407 LEU 407 427 427 LEU LEU A . n 
A 1 408 ARG 408 428 428 ARG ARG A . n 
A 1 409 ARG 409 429 429 ARG ARG A . n 
A 1 410 HIS 410 430 430 HIS HIS A . n 
A 1 411 PHE 411 431 431 PHE PHE A . n 
A 1 412 ASN 412 432 432 ASN ASN A . n 
A 1 413 SER 413 433 433 SER SER A . n 
A 1 414 ASN 414 434 434 ASN ASN A . n 
A 1 415 PHE 415 435 435 PHE PHE A . n 
A 1 416 LYS 416 436 436 LYS LYS A . n 
A 1 417 GLY 417 437 437 GLY GLY A . n 
A 1 418 GLY 418 438 438 GLY GLY A . n 
A 1 419 PHE 419 439 439 PHE PHE A . n 
A 1 420 ASN 420 440 440 ASN ASN A . n 
A 1 421 PHE 421 441 441 PHE PHE A . n 
A 1 422 TYR 422 442 442 TYR TYR A . n 
A 1 423 ALA 423 443 443 ALA ALA A . n 
A 1 424 GLY 424 444 444 GLY GLY A . n 
A 1 425 LEU 425 445 445 LEU LEU A . n 
A 1 426 LYS 426 446 446 LYS LYS A . n 
A 1 427 GLY 427 447 447 GLY GLY A . n 
A 1 428 GLN 428 448 448 GLN GLN A . n 
A 1 429 VAL 429 449 449 VAL VAL A . n 
A 1 430 LEU 430 450 450 LEU LEU A . n 
A 1 431 VAL 431 451 451 VAL VAL A . n 
A 1 432 LEU 432 452 452 LEU LEU A . n 
A 1 433 ARG 433 453 453 ARG ARG A . n 
A 1 434 THR 434 454 454 THR THR A . n 
A 1 435 THR 435 455 455 THR THR A . n 
A 1 436 SER 436 456 456 SER SER A . n 
A 1 437 THR 437 457 457 THR THR A . n 
A 1 438 VAL 438 458 458 VAL VAL A . n 
A 1 439 TYR 439 459 459 TYR TYR A . n 
A 1 440 ASN 440 460 460 ASN ASN A . n 
A 1 441 TPQ 441 461 461 TPQ TPQ A . n 
A 1 442 ASP 442 462 462 ASP ASP A . n 
A 1 443 TYR 443 463 463 TYR TYR A . n 
A 1 444 ILE 444 464 464 ILE ILE A . n 
A 1 445 TRP 445 465 465 TRP TRP A . n 
A 1 446 ASP 446 466 466 ASP ASP A . n 
A 1 447 PHE 447 467 467 PHE PHE A . n 
A 1 448 ILE 448 468 468 ILE ILE A . n 
A 1 449 PHE 449 469 469 PHE PHE A . n 
A 1 450 TYR 450 470 470 TYR TYR A . n 
A 1 451 PRO 451 471 471 PRO PRO A . n 
A 1 452 ASN 452 472 472 ASN ASN A . n 
A 1 453 GLY 453 473 473 GLY GLY A . n 
A 1 454 VAL 454 474 474 VAL VAL A . n 
A 1 455 MET 455 475 475 MET MET A . n 
A 1 456 GLU 456 476 476 GLU GLU A . n 
A 1 457 ALA 457 477 477 ALA ALA A . n 
A 1 458 LYS 458 478 478 LYS LYS A . n 
A 1 459 MET 459 479 479 MET MET A . n 
A 1 460 HIS 460 480 480 HIS HIS A . n 
A 1 461 ALA 461 481 481 ALA ALA A . n 
A 1 462 THR 462 482 482 THR THR A . n 
A 1 463 GLY 463 483 483 GLY GLY A . n 
A 1 464 TYR 464 484 484 TYR TYR A . n 
A 1 465 VAL 465 485 485 VAL VAL A . n 
A 1 466 HIS 466 486 486 HIS HIS A . n 
A 1 467 ALA 467 487 487 ALA ALA A . n 
A 1 468 THR 468 488 488 THR THR A . n 
A 1 469 PHE 469 489 489 PHE PHE A . n 
A 1 470 TYR 470 490 490 TYR TYR A . n 
A 1 471 THR 471 491 491 THR THR A . n 
A 1 472 PRO 472 492 492 PRO PRO A . n 
A 1 473 GLU 473 493 493 GLU GLU A . n 
A 1 474 GLY 474 494 494 GLY GLY A . n 
A 1 475 LEU 475 495 495 LEU LEU A . n 
A 1 476 ARG 476 496 496 ARG ARG A . n 
A 1 477 HIS 477 497 497 HIS HIS A . n 
A 1 478 GLY 478 498 498 GLY GLY A . n 
A 1 479 THR 479 499 499 THR THR A . n 
A 1 480 ARG 480 500 500 ARG ARG A . n 
A 1 481 LEU 481 501 501 LEU LEU A . n 
A 1 482 HIS 482 502 502 HIS HIS A . n 
A 1 483 THR 483 503 503 THR THR A . n 
A 1 484 HIS 484 504 504 HIS HIS A . n 
A 1 485 LEU 485 505 505 LEU LEU A . n 
A 1 486 ILE 486 506 506 ILE ILE A . n 
A 1 487 GLY 487 507 507 GLY GLY A . n 
A 1 488 ASN 488 508 508 ASN ASN A . n 
A 1 489 ILE 489 509 509 ILE ILE A . n 
A 1 490 HIS 490 510 510 HIS HIS A . n 
A 1 491 THR 491 511 511 THR THR A . n 
A 1 492 HIS 492 512 512 HIS HIS A . n 
A 1 493 LEU 493 513 513 LEU LEU A . n 
A 1 494 VAL 494 514 514 VAL VAL A . n 
A 1 495 HIS 495 515 515 HIS HIS A . n 
A 1 496 TYR 496 516 516 TYR TYR A . n 
A 1 497 ARG 497 517 517 ARG ARG A . n 
A 1 498 VAL 498 518 518 VAL VAL A . n 
A 1 499 ASP 499 519 519 ASP ASP A . n 
A 1 500 LEU 500 520 520 LEU LEU A . n 
A 1 501 ASP 501 521 521 ASP ASP A . n 
A 1 502 VAL 502 522 522 VAL VAL A . n 
A 1 503 ALA 503 523 523 ALA ALA A . n 
A 1 504 GLY 504 524 524 GLY GLY A . n 
A 1 505 THR 505 525 525 THR THR A . n 
A 1 506 LYS 506 526 526 LYS LYS A . n 
A 1 507 ASN 507 527 527 ASN ASN A . n 
A 1 508 SER 508 528 528 SER SER A . n 
A 1 509 PHE 509 529 529 PHE PHE A . n 
A 1 510 GLN 510 530 530 GLN GLN A . n 
A 1 511 THR 511 531 531 THR THR A . n 
A 1 512 LEU 512 532 532 LEU LEU A . n 
A 1 513 GLN 513 533 533 GLN GLN A . n 
A 1 514 MET 514 534 534 MET MET A . n 
A 1 515 LYS 515 535 535 LYS LYS A . n 
A 1 516 LEU 516 536 536 LEU LEU A . n 
A 1 517 GLU 517 537 537 GLU GLU A . n 
A 1 518 ASN 518 538 538 ASN ASN A . n 
A 1 519 ILE 519 539 539 ILE ILE A . n 
A 1 520 THR 520 540 540 THR THR A . n 
A 1 521 ASN 521 541 541 ASN ASN A . n 
A 1 522 PRO 522 542 542 PRO PRO A . n 
A 1 523 TRP 523 543 543 TRP TRP A . n 
A 1 524 SER 524 544 544 SER SER A . n 
A 1 525 PRO 525 545 545 PRO PRO A . n 
A 1 526 ARG 526 546 546 ARG ARG A . n 
A 1 527 HIS 527 547 547 HIS HIS A . n 
A 1 528 ARG 528 548 548 ARG ARG A . n 
A 1 529 VAL 529 549 549 VAL VAL A . n 
A 1 530 VAL 530 550 550 VAL VAL A . n 
A 1 531 GLN 531 551 551 GLN GLN A . n 
A 1 532 PRO 532 552 552 PRO PRO A . n 
A 1 533 THR 533 553 553 THR THR A . n 
A 1 534 LEU 534 554 554 LEU LEU A . n 
A 1 535 GLU 535 555 555 GLU GLU A . n 
A 1 536 GLN 536 556 556 GLN GLN A . n 
A 1 537 THR 537 557 557 THR THR A . n 
A 1 538 GLN 538 558 558 GLN GLN A . n 
A 1 539 TYR 539 559 559 TYR TYR A . n 
A 1 540 SER 540 560 560 SER SER A . n 
A 1 541 TRP 541 561 561 TRP TRP A . n 
A 1 542 GLU 542 562 562 GLU GLU A . n 
A 1 543 ARG 543 563 563 ARG ARG A . n 
A 1 544 GLN 544 564 564 GLN GLN A . n 
A 1 545 ALA 545 565 565 ALA ALA A . n 
A 1 546 ALA 546 566 566 ALA ALA A . n 
A 1 547 PHE 547 567 567 PHE PHE A . n 
A 1 548 ARG 548 568 568 ARG ARG A . n 
A 1 549 PHE 549 569 569 PHE PHE A . n 
A 1 550 LYS 550 570 570 LYS LYS A . n 
A 1 551 ARG 551 571 571 ARG ARG A . n 
A 1 552 LYS 552 572 572 LYS LYS A . n 
A 1 553 LEU 553 573 573 LEU LEU A . n 
A 1 554 PRO 554 574 574 PRO PRO A . n 
A 1 555 LYS 555 575 575 LYS LYS A . n 
A 1 556 TYR 556 576 576 TYR TYR A . n 
A 1 557 LEU 557 577 577 LEU LEU A . n 
A 1 558 LEU 558 578 578 LEU LEU A . n 
A 1 559 PHE 559 579 579 PHE PHE A . n 
A 1 560 THR 560 580 580 THR THR A . n 
A 1 561 SER 561 581 581 SER SER A . n 
A 1 562 PRO 562 582 582 PRO PRO A . n 
A 1 563 GLN 563 583 583 GLN GLN A . n 
A 1 564 GLU 564 584 584 GLU GLU A . n 
A 1 565 ASN 565 585 585 ASN ASN A . n 
A 1 566 PRO 566 586 586 PRO PRO A . n 
A 1 567 TRP 567 587 587 TRP TRP A . n 
A 1 568 GLY 568 588 588 GLY GLY A . n 
A 1 569 HIS 569 589 589 HIS HIS A . n 
A 1 570 LYS 570 590 590 LYS LYS A . n 
A 1 571 ARG 571 591 591 ARG ARG A . n 
A 1 572 SER 572 592 592 SER SER A . n 
A 1 573 TYR 573 593 593 TYR TYR A . n 
A 1 574 ARG 574 594 594 ARG ARG A . n 
A 1 575 LEU 575 595 595 LEU LEU A . n 
A 1 576 GLN 576 596 596 GLN GLN A . n 
A 1 577 ILE 577 597 597 ILE ILE A . n 
A 1 578 HIS 578 598 598 HIS HIS A . n 
A 1 579 SER 579 599 599 SER SER A . n 
A 1 580 MET 580 600 600 MET MET A . n 
A 1 581 ALA 581 601 601 ALA ALA A . n 
A 1 582 ASP 582 602 602 ASP ASP A . n 
A 1 583 GLN 583 603 603 GLN GLN A . n 
A 1 584 VAL 584 604 604 VAL VAL A . n 
A 1 585 LEU 585 605 605 LEU LEU A . n 
A 1 586 PRO 586 606 606 PRO PRO A . n 
A 1 587 PRO 587 607 607 PRO PRO A . n 
A 1 588 GLY 588 608 608 GLY GLY A . n 
A 1 589 TRP 589 609 609 TRP TRP A . n 
A 1 590 GLN 590 610 610 GLN GLN A . n 
A 1 591 GLU 591 611 611 GLU GLU A . n 
A 1 592 GLU 592 612 612 GLU GLU A . n 
A 1 593 GLN 593 613 613 GLN GLN A . n 
A 1 594 ALA 594 614 614 ALA ALA A . n 
A 1 595 ILE 595 615 615 ILE ILE A . n 
A 1 596 THR 596 616 616 THR THR A . n 
A 1 597 TRP 597 617 617 TRP TRP A . n 
A 1 598 ALA 598 618 618 ALA ALA A . n 
A 1 599 ARG 599 619 619 ARG ARG A . n 
A 1 600 TYR 600 620 620 TYR TYR A . n 
A 1 601 PRO 601 621 621 PRO PRO A . n 
A 1 602 LEU 602 622 622 LEU LEU A . n 
A 1 603 ALA 603 623 623 ALA ALA A . n 
A 1 604 VAL 604 624 624 VAL VAL A . n 
A 1 605 THR 605 625 625 THR THR A . n 
A 1 606 LYS 606 626 626 LYS LYS A . n 
A 1 607 TYR 607 627 627 TYR TYR A . n 
A 1 608 ARG 608 628 628 ARG ARG A . n 
A 1 609 GLU 609 629 629 GLU GLU A . n 
A 1 610 SER 610 630 630 SER SER A . n 
A 1 611 GLU 611 631 631 GLU GLU A . n 
A 1 612 LEU 612 632 632 LEU LEU A . n 
A 1 613 CYS 613 633 633 CYS CYS A . n 
A 1 614 SER 614 634 634 SER SER A . n 
A 1 615 SER 615 635 635 SER SER A . n 
A 1 616 SER 616 636 636 SER SER A . n 
A 1 617 ILE 617 637 637 ILE ILE A . n 
A 1 618 TYR 618 638 638 TYR TYR A . n 
A 1 619 HIS 619 639 639 HIS HIS A . n 
A 1 620 GLN 620 640 640 GLN GLN A . n 
A 1 621 ASN 621 641 641 ASN ASN A . n 
A 1 622 ASP 622 642 642 ASP ASP A . n 
A 1 623 PRO 623 643 643 PRO PRO A . n 
A 1 624 TRP 624 644 644 TRP TRP A . n 
A 1 625 ASP 625 645 645 ASP ASP A . n 
A 1 626 PRO 626 646 646 PRO PRO A . n 
A 1 627 PRO 627 647 647 PRO PRO A . n 
A 1 628 VAL 628 648 648 VAL VAL A . n 
A 1 629 VAL 629 649 649 VAL VAL A . n 
A 1 630 PHE 630 650 650 PHE PHE A . n 
A 1 631 GLU 631 651 651 GLU GLU A . n 
A 1 632 GLN 632 652 652 GLN GLN A . n 
A 1 633 PHE 633 653 653 PHE PHE A . n 
A 1 634 LEU 634 654 654 LEU LEU A . n 
A 1 635 HIS 635 655 655 HIS HIS A . n 
A 1 636 ASN 636 656 656 ASN ASN A . n 
A 1 637 ASN 637 657 657 ASN ASN A . n 
A 1 638 GLU 638 658 658 GLU GLU A . n 
A 1 639 ASN 639 659 659 ASN ASN A . n 
A 1 640 ILE 640 660 660 ILE ILE A . n 
A 1 641 GLU 641 661 661 GLU GLU A . n 
A 1 642 ASN 642 662 662 ASN ASN A . n 
A 1 643 GLU 643 663 663 GLU GLU A . n 
A 1 644 ASP 644 664 664 ASP ASP A . n 
A 1 645 LEU 645 665 665 LEU LEU A . n 
A 1 646 VAL 646 666 666 VAL VAL A . n 
A 1 647 ALA 647 667 667 ALA ALA A . n 
A 1 648 TRP 648 668 668 TRP TRP A . n 
A 1 649 VAL 649 669 669 VAL VAL A . n 
A 1 650 THR 650 670 670 THR THR A . n 
A 1 651 VAL 651 671 671 VAL VAL A . n 
A 1 652 GLY 652 672 672 GLY GLY A . n 
A 1 653 PHE 653 673 673 PHE PHE A . n 
A 1 654 LEU 654 674 674 LEU LEU A . n 
A 1 655 HIS 655 675 675 HIS HIS A . n 
A 1 656 ILE 656 676 676 ILE ILE A . n 
A 1 657 PRO 657 677 677 PRO PRO A . n 
A 1 658 HIS 658 678 678 HIS HIS A . n 
A 1 659 SER 659 679 679 SER SER A . n 
A 1 660 GLU 660 680 680 GLU GLU A . n 
A 1 661 ASP 661 681 681 ASP ASP A . n 
A 1 662 ILE 662 682 682 ILE ILE A . n 
A 1 663 PRO 663 683 683 PRO PRO A . n 
A 1 664 ASN 664 684 684 ASN ASN A . n 
A 1 665 THR 665 685 685 THR THR A . n 
A 1 666 ALA 666 686 686 ALA ALA A . n 
A 1 667 THR 667 687 687 THR THR A . n 
A 1 668 PRO 668 688 688 PRO PRO A . n 
A 1 669 GLY 669 689 689 GLY GLY A . n 
A 1 670 ASN 670 690 690 ASN ASN A . n 
A 1 671 SER 671 691 691 SER SER A . n 
A 1 672 VAL 672 692 692 VAL VAL A . n 
A 1 673 GLY 673 693 693 GLY GLY A . n 
A 1 674 PHE 674 694 694 PHE PHE A . n 
A 1 675 LEU 675 695 695 LEU LEU A . n 
A 1 676 LEU 676 696 696 LEU LEU A . n 
A 1 677 ARG 677 697 697 ARG ARG A . n 
A 1 678 PRO 678 698 698 PRO PRO A . n 
A 1 679 PHE 679 699 699 PHE PHE A . n 
A 1 680 ASN 680 700 700 ASN ASN A . n 
A 1 681 PHE 681 701 701 PHE PHE A . n 
A 1 682 PHE 682 702 702 PHE PHE A . n 
A 1 683 PRO 683 703 703 PRO PRO A . n 
A 1 684 GLU 684 704 704 GLU GLU A . n 
A 1 685 ASP 685 705 705 ASP ASP A . n 
A 1 686 PRO 686 706 706 PRO PRO A . n 
A 1 687 SER 687 707 707 SER SER A . n 
A 1 688 LEU 688 708 708 LEU LEU A . n 
A 1 689 ALA 689 709 709 ALA ALA A . n 
A 1 690 SER 690 710 710 SER SER A . n 
A 1 691 ARG 691 711 711 ARG ARG A . n 
A 1 692 ASP 692 712 712 ASP ASP A . n 
A 1 693 THR 693 713 713 THR THR A . n 
A 1 694 VAL 694 714 714 VAL VAL A . n 
A 1 695 ILE 695 715 715 ILE ILE A . n 
A 1 696 VAL 696 716 716 VAL VAL A . n 
A 1 697 TRP 697 717 717 TRP TRP A . n 
A 1 698 PRO 698 718 718 PRO PRO A . n 
A 1 699 ARG 699 719 719 ARG ARG A . n 
A 1 700 ASP 700 720 720 ASP ASP A . n 
A 1 701 ASN 701 721 721 ASN ASN A . n 
A 1 702 GLY 702 722 722 GLY GLY A . n 
A 1 703 PRO 703 723 723 PRO PRO A . n 
A 1 704 ASN 704 724 724 ASN ASN A . n 
A 1 705 TYR 705 725 725 TYR TYR A . n 
A 1 706 VAL 706 726 726 VAL VAL A . n 
A 1 707 GLN 707 727 727 GLN GLN A . n 
A 1 708 ARG 708 728 728 ARG ARG A . n 
A 1 709 TRP 709 729 729 TRP TRP A . n 
A 1 710 ILE 710 730 730 ILE ILE A . n 
A 1 711 PRO 711 731 731 PRO PRO A . n 
A 1 712 GLU 712 732 732 GLU GLU A . n 
A 1 713 ASP 713 733 733 ASP ASP A . n 
A 1 714 ARG 714 734 734 ARG ARG A . n 
A 1 715 ASP 715 735 735 ASP ASP A . n 
A 1 716 CYS 716 736 736 CYS CYS A . n 
A 1 717 SER 717 737 737 SER SER A . n 
A 1 718 MET 718 738 738 MET MET A . n 
A 1 719 PRO 719 739 739 PRO PRO A . n 
A 1 720 PRO 720 740 740 PRO PRO A . n 
A 1 721 PRO 721 741 741 PRO PRO A . n 
A 1 722 PHE 722 742 742 PHE PHE A . n 
A 1 723 SER 723 743 743 SER SER A . n 
A 1 724 TYR 724 744 744 TYR TYR A . n 
A 1 725 ASN 725 745 745 ASN ASN A . n 
A 1 726 GLY 726 746 746 GLY GLY A . n 
A 1 727 THR 727 747 747 THR THR A . n 
A 1 728 TYR 728 748 748 TYR TYR A . n 
A 1 729 ARG 729 749 749 ARG ARG A . n 
A 1 730 PRO 730 750 750 PRO PRO A . n 
A 1 731 VAL 731 751 751 VAL VAL A . n 
B 1 1   ARG 1   21  ?   ?   ?   B . n 
B 1 2   SER 2   22  ?   ?   ?   B . n 
B 1 3   PRO 3   23  ?   ?   ?   B . n 
B 1 4   GLY 4   24  ?   ?   ?   B . n 
B 1 5   THR 5   25  ?   ?   ?   B . n 
B 1 6   LEU 6   26  ?   ?   ?   B . n 
B 1 7   PRO 7   27  ?   ?   ?   B . n 
B 1 8   ARG 8   28  28  ARG ARG B . n 
B 1 9   LYS 9   29  29  LYS LYS B . n 
B 1 10  ALA 10  30  30  ALA ALA B . n 
B 1 11  GLY 11  31  31  GLY GLY B . n 
B 1 12  VAL 12  32  32  VAL VAL B . n 
B 1 13  PHE 13  33  33  PHE PHE B . n 
B 1 14  SER 14  34  34  SER SER B . n 
B 1 15  ASP 15  35  35  ASP ASP B . n 
B 1 16  LEU 16  36  36  LEU LEU B . n 
B 1 17  SER 17  37  37  SER SER B . n 
B 1 18  ASN 18  38  38  ASN ASN B . n 
B 1 19  GLN 19  39  39  GLN GLN B . n 
B 1 20  GLU 20  40  40  GLU GLU B . n 
B 1 21  LEU 21  41  41  LEU LEU B . n 
B 1 22  LYS 22  42  42  LYS LYS B . n 
B 1 23  ALA 23  43  43  ALA ALA B . n 
B 1 24  VAL 24  44  44  VAL VAL B . n 
B 1 25  HIS 25  45  45  HIS HIS B . n 
B 1 26  SER 26  46  46  SER SER B . n 
B 1 27  PHE 27  47  47  PHE PHE B . n 
B 1 28  LEU 28  48  48  LEU LEU B . n 
B 1 29  TRP 29  49  49  TRP TRP B . n 
B 1 30  SER 30  50  50  SER SER B . n 
B 1 31  LYS 31  51  51  LYS LYS B . n 
B 1 32  LYS 32  52  52  LYS LYS B . n 
B 1 33  GLU 33  53  53  GLU GLU B . n 
B 1 34  LEU 34  54  54  LEU LEU B . n 
B 1 35  ARG 35  55  55  ARG ARG B . n 
B 1 36  LEU 36  56  56  LEU LEU B . n 
B 1 37  GLN 37  57  57  GLN GLN B . n 
B 1 38  PRO 38  58  58  PRO PRO B . n 
B 1 39  SER 39  59  59  SER SER B . n 
B 1 40  SER 40  60  60  SER SER B . n 
B 1 41  THR 41  61  61  THR THR B . n 
B 1 42  THR 42  62  62  THR THR B . n 
B 1 43  THR 43  63  63  THR THR B . n 
B 1 44  MET 44  64  64  MET MET B . n 
B 1 45  ALA 45  65  65  ALA ALA B . n 
B 1 46  LYS 46  66  66  LYS LYS B . n 
B 1 47  ASN 47  67  67  ASN ASN B . n 
B 1 48  THR 48  68  68  THR THR B . n 
B 1 49  VAL 49  69  69  VAL VAL B . n 
B 1 50  PHE 50  70  70  PHE PHE B . n 
B 1 51  LEU 51  71  71  LEU LEU B . n 
B 1 52  ILE 52  72  72  ILE ILE B . n 
B 1 53  GLU 53  73  73  GLU GLU B . n 
B 1 54  MET 54  74  74  MET MET B . n 
B 1 55  LEU 55  75  75  LEU LEU B . n 
B 1 56  LEU 56  76  76  LEU LEU B . n 
B 1 57  PRO 57  77  77  PRO PRO B . n 
B 1 58  LYS 58  78  78  LYS LYS B . n 
B 1 59  LYS 59  79  79  LYS LYS B . n 
B 1 60  TYR 60  80  80  TYR TYR B . n 
B 1 61  HIS 61  81  81  HIS HIS B . n 
B 1 62  VAL 62  82  82  VAL VAL B . n 
B 1 63  LEU 63  83  83  LEU LEU B . n 
B 1 64  ARG 64  84  84  ARG ARG B . n 
B 1 65  PHE 65  85  85  PHE PHE B . n 
B 1 66  LEU 66  86  86  LEU LEU B . n 
B 1 67  ASP 67  87  87  ASP ASP B . n 
B 1 68  LYS 68  88  88  LYS LYS B . n 
B 1 69  GLY 69  89  89  GLY GLY B . n 
B 1 70  GLU 70  90  90  GLU GLU B . n 
B 1 71  ARG 71  91  91  ARG ARG B . n 
B 1 72  HIS 72  92  92  HIS HIS B . n 
B 1 73  PRO 73  93  93  PRO PRO B . n 
B 1 74  VAL 74  94  94  VAL VAL B . n 
B 1 75  ARG 75  95  95  ARG ARG B . n 
B 1 76  GLU 76  96  96  GLU GLU B . n 
B 1 77  ALA 77  97  97  ALA ALA B . n 
B 1 78  ARG 78  98  98  ARG ARG B . n 
B 1 79  ALA 79  99  99  ALA ALA B . n 
B 1 80  VAL 80  100 100 VAL VAL B . n 
B 1 81  ILE 81  101 101 ILE ILE B . n 
B 1 82  PHE 82  102 102 PHE PHE B . n 
B 1 83  PHE 83  103 103 PHE PHE B . n 
B 1 84  GLY 84  104 104 GLY GLY B . n 
B 1 85  ASP 85  105 105 ASP ASP B . n 
B 1 86  GLN 86  106 106 GLN GLN B . n 
B 1 87  GLU 87  107 107 GLU GLU B . n 
B 1 88  HIS 88  108 108 HIS HIS B . n 
B 1 89  PRO 89  109 109 PRO PRO B . n 
B 1 90  ASN 90  110 110 ASN ASN B . n 
B 1 91  VAL 91  111 111 VAL VAL B . n 
B 1 92  THR 92  112 112 THR THR B . n 
B 1 93  GLU 93  113 113 GLU GLU B . n 
B 1 94  PHE 94  114 114 PHE PHE B . n 
B 1 95  ALA 95  115 115 ALA ALA B . n 
B 1 96  VAL 96  116 116 VAL VAL B . n 
B 1 97  GLY 97  117 117 GLY GLY B . n 
B 1 98  PRO 98  118 118 PRO PRO B . n 
B 1 99  LEU 99  119 119 LEU LEU B . n 
B 1 100 PRO 100 120 120 PRO PRO B . n 
B 1 101 GLY 101 121 121 GLY GLY B . n 
B 1 102 PRO 102 122 122 PRO PRO B . n 
B 1 103 CYS 103 123 123 CYS CYS B . n 
B 1 104 TYR 104 124 124 TYR TYR B . n 
B 1 105 MET 105 125 125 MET MET B . n 
B 1 106 ARG 106 126 126 ARG ARG B . n 
B 1 107 ALA 107 127 127 ALA ALA B . n 
B 1 108 LEU 108 128 128 LEU LEU B . n 
B 1 109 SER 109 129 129 SER SER B . n 
B 1 110 PRO 110 130 130 PRO PRO B . n 
B 1 111 ARG 111 131 131 ARG ARG B . n 
B 1 112 PRO 112 132 132 PRO PRO B . n 
B 1 113 GLY 113 133 133 GLY GLY B . n 
B 1 114 TYR 114 134 134 TYR TYR B . n 
B 1 115 GLN 115 135 135 GLN GLN B . n 
B 1 116 SER 116 136 136 SER SER B . n 
B 1 117 SER 117 137 137 SER SER B . n 
B 1 118 TRP 118 138 138 TRP TRP B . n 
B 1 119 ALA 119 139 139 ALA ALA B . n 
B 1 120 SER 120 140 140 SER SER B . n 
B 1 121 ARG 121 141 141 ARG ARG B . n 
B 1 122 PRO 122 142 142 PRO PRO B . n 
B 1 123 ILE 123 143 143 ILE ILE B . n 
B 1 124 SER 124 144 144 SER SER B . n 
B 1 125 THR 125 145 145 THR THR B . n 
B 1 126 ALA 126 146 146 ALA ALA B . n 
B 1 127 GLU 127 147 147 GLU GLU B . n 
B 1 128 TYR 128 148 148 TYR TYR B . n 
B 1 129 ALA 129 149 149 ALA ALA B . n 
B 1 130 LEU 130 150 150 LEU LEU B . n 
B 1 131 LEU 131 151 151 LEU LEU B . n 
B 1 132 TYR 132 152 152 TYR TYR B . n 
B 1 133 HIS 133 153 153 HIS HIS B . n 
B 1 134 THR 134 154 154 THR THR B . n 
B 1 135 LEU 135 155 155 LEU LEU B . n 
B 1 136 GLN 136 156 156 GLN GLN B . n 
B 1 137 GLU 137 157 157 GLU GLU B . n 
B 1 138 ALA 138 158 158 ALA ALA B . n 
B 1 139 THR 139 159 159 THR THR B . n 
B 1 140 LYS 140 160 160 LYS LYS B . n 
B 1 141 PRO 141 161 161 PRO PRO B . n 
B 1 142 LEU 142 162 162 LEU LEU B . n 
B 1 143 HIS 143 163 163 HIS HIS B . n 
B 1 144 GLN 144 164 164 GLN GLN B . n 
B 1 145 PHE 145 165 165 PHE PHE B . n 
B 1 146 PHE 146 166 166 PHE PHE B . n 
B 1 147 LEU 147 167 167 LEU LEU B . n 
B 1 148 ASN 148 168 168 ASN ASN B . n 
B 1 149 THR 149 169 169 THR THR B . n 
B 1 150 THR 150 170 170 THR THR B . n 
B 1 151 GLY 151 171 171 GLY GLY B . n 
B 1 152 PHE 152 172 172 PHE PHE B . n 
B 1 153 SER 153 173 173 SER SER B . n 
B 1 154 PHE 154 174 174 PHE PHE B . n 
B 1 155 GLN 155 175 175 GLN GLN B . n 
B 1 156 ASP 156 176 176 ASP ASP B . n 
B 1 157 CYS 157 177 177 CYS CYS B . n 
B 1 158 HIS 158 178 178 HIS HIS B . n 
B 1 159 ASP 159 179 179 ASP ASP B . n 
B 1 160 ARG 160 180 180 ARG ARG B . n 
B 1 161 CYS 161 181 181 CYS CYS B . n 
B 1 162 LEU 162 182 182 LEU LEU B . n 
B 1 163 ALA 163 183 183 ALA ALA B . n 
B 1 164 PHE 164 184 184 PHE PHE B . n 
B 1 165 THR 165 185 185 THR THR B . n 
B 1 166 ASP 166 186 186 ASP ASP B . n 
B 1 167 VAL 167 187 187 VAL VAL B . n 
B 1 168 ALA 168 188 188 ALA ALA B . n 
B 1 169 PRO 169 189 189 PRO PRO B . n 
B 1 170 ARG 170 190 190 ARG ARG B . n 
B 1 171 GLY 171 191 191 GLY GLY B . n 
B 1 172 VAL 172 192 192 VAL VAL B . n 
B 1 173 ALA 173 193 193 ALA ALA B . n 
B 1 174 SER 174 194 194 SER SER B . n 
B 1 175 GLY 175 195 195 GLY GLY B . n 
B 1 176 GLN 176 196 196 GLN GLN B . n 
B 1 177 ARG 177 197 197 ARG ARG B . n 
B 1 178 ARG 178 198 198 ARG ARG B . n 
B 1 179 SER 179 199 199 SER SER B . n 
B 1 180 TRP 180 200 200 TRP TRP B . n 
B 1 181 LEU 181 201 201 LEU LEU B . n 
B 1 182 ILE 182 202 202 ILE ILE B . n 
B 1 183 ILE 183 203 203 ILE ILE B . n 
B 1 184 GLN 184 204 204 GLN GLN B . n 
B 1 185 ARG 185 205 205 ARG ARG B . n 
B 1 186 TYR 186 206 206 TYR TYR B . n 
B 1 187 VAL 187 207 207 VAL VAL B . n 
B 1 188 GLU 188 208 208 GLU GLU B . n 
B 1 189 GLY 189 209 209 GLY GLY B . n 
B 1 190 TYR 190 210 210 TYR TYR B . n 
B 1 191 PHE 191 211 211 PHE PHE B . n 
B 1 192 LEU 192 212 212 LEU LEU B . n 
B 1 193 HIS 193 213 213 HIS HIS B . n 
B 1 194 PRO 194 214 214 PRO PRO B . n 
B 1 195 THR 195 215 215 THR THR B . n 
B 1 196 GLY 196 216 216 GLY GLY B . n 
B 1 197 LEU 197 217 217 LEU LEU B . n 
B 1 198 GLU 198 218 218 GLU GLU B . n 
B 1 199 LEU 199 219 219 LEU LEU B . n 
B 1 200 LEU 200 220 220 LEU LEU B . n 
B 1 201 VAL 201 221 221 VAL VAL B . n 
B 1 202 ASP 202 222 222 ASP ASP B . n 
B 1 203 HIS 203 223 223 HIS HIS B . n 
B 1 204 GLY 204 224 224 GLY GLY B . n 
B 1 205 SER 205 225 225 SER SER B . n 
B 1 206 THR 206 226 226 THR THR B . n 
B 1 207 ASP 207 227 227 ASP ASP B . n 
B 1 208 ALA 208 228 228 ALA ALA B . n 
B 1 209 GLY 209 229 229 GLY GLY B . n 
B 1 210 HIS 210 230 230 HIS HIS B . n 
B 1 211 TRP 211 231 231 TRP TRP B . n 
B 1 212 ALA 212 232 232 ALA ALA B . n 
B 1 213 VAL 213 233 233 VAL VAL B . n 
B 1 214 GLU 214 234 234 GLU GLU B . n 
B 1 215 GLN 215 235 235 GLN GLN B . n 
B 1 216 VAL 216 236 236 VAL VAL B . n 
B 1 217 TRP 217 237 237 TRP TRP B . n 
B 1 218 TYR 218 238 238 TYR TYR B . n 
B 1 219 ASN 219 239 239 ASN ASN B . n 
B 1 220 GLY 220 240 240 GLY GLY B . n 
B 1 221 LYS 221 241 241 LYS LYS B . n 
B 1 222 PHE 222 242 242 PHE PHE B . n 
B 1 223 TYR 223 243 243 TYR TYR B . n 
B 1 224 GLY 224 244 244 GLY GLY B . n 
B 1 225 SER 225 245 245 SER SER B . n 
B 1 226 PRO 226 246 246 PRO PRO B . n 
B 1 227 GLU 227 247 247 GLU GLU B . n 
B 1 228 GLU 228 248 248 GLU GLU B . n 
B 1 229 LEU 229 249 249 LEU LEU B . n 
B 1 230 ALA 230 250 250 ALA ALA B . n 
B 1 231 ARG 231 251 251 ARG ARG B . n 
B 1 232 LYS 232 252 252 LYS LYS B . n 
B 1 233 TYR 233 253 253 TYR TYR B . n 
B 1 234 ALA 234 254 254 ALA ALA B . n 
B 1 235 ASP 235 255 255 ASP ASP B . n 
B 1 236 GLY 236 256 256 GLY GLY B . n 
B 1 237 GLU 237 257 257 GLU GLU B . n 
B 1 238 VAL 238 258 258 VAL VAL B . n 
B 1 239 ASP 239 259 259 ASP ASP B . n 
B 1 240 VAL 240 260 260 VAL VAL B . n 
B 1 241 VAL 241 261 261 VAL VAL B . n 
B 1 242 VAL 242 262 262 VAL VAL B . n 
B 1 243 LEU 243 263 263 LEU LEU B . n 
B 1 244 GLU 244 264 ?   ?   ?   B . n 
B 1 245 ASP 245 265 ?   ?   ?   B . n 
B 1 246 PRO 246 266 ?   ?   ?   B . n 
B 1 247 LEU 247 267 ?   ?   ?   B . n 
B 1 248 PRO 248 268 ?   ?   ?   B . n 
B 1 249 GLY 249 269 ?   ?   ?   B . n 
B 1 250 GLY 250 270 ?   ?   ?   B . n 
B 1 251 LYS 251 271 ?   ?   ?   B . n 
B 1 252 GLY 252 272 ?   ?   ?   B . n 
B 1 253 HIS 253 273 ?   ?   ?   B . n 
B 1 254 ASP 254 274 ?   ?   ?   B . n 
B 1 255 SER 255 275 ?   ?   ?   B . n 
B 1 256 THR 256 276 ?   ?   ?   B . n 
B 1 257 GLU 257 277 ?   ?   ?   B . n 
B 1 258 GLU 258 278 278 GLU GLU B . n 
B 1 259 PRO 259 279 279 PRO PRO B . n 
B 1 260 PRO 260 280 280 PRO PRO B . n 
B 1 261 LEU 261 281 281 LEU LEU B . n 
B 1 262 PHE 262 282 282 PHE PHE B . n 
B 1 263 SER 263 283 283 SER SER B . n 
B 1 264 SER 264 284 284 SER SER B . n 
B 1 265 HIS 265 285 285 HIS HIS B . n 
B 1 266 LYS 266 286 286 LYS LYS B . n 
B 1 267 PRO 267 287 287 PRO PRO B . n 
B 1 268 ARG 268 288 288 ARG ARG B . n 
B 1 269 GLY 269 289 289 GLY GLY B . n 
B 1 270 ASP 270 290 290 ASP ASP B . n 
B 1 271 PHE 271 291 291 PHE PHE B . n 
B 1 272 PRO 272 292 292 PRO PRO B . n 
B 1 273 SER 273 293 293 SER SER B . n 
B 1 274 PRO 274 294 294 PRO PRO B . n 
B 1 275 ILE 275 295 295 ILE ILE B . n 
B 1 276 HIS 276 296 296 HIS HIS B . n 
B 1 277 VAL 277 297 297 VAL VAL B . n 
B 1 278 SER 278 298 298 SER SER B . n 
B 1 279 GLY 279 299 299 GLY GLY B . n 
B 1 280 PRO 280 300 300 PRO PRO B . n 
B 1 281 ARG 281 301 301 ARG ARG B . n 
B 1 282 LEU 282 302 302 LEU LEU B . n 
B 1 283 VAL 283 303 303 VAL VAL B . n 
B 1 284 GLN 284 304 304 GLN GLN B . n 
B 1 285 PRO 285 305 305 PRO PRO B . n 
B 1 286 HIS 286 306 306 HIS HIS B . n 
B 1 287 GLY 287 307 307 GLY GLY B . n 
B 1 288 PRO 288 308 308 PRO PRO B . n 
B 1 289 ARG 289 309 309 ARG ARG B . n 
B 1 290 PHE 290 310 310 PHE PHE B . n 
B 1 291 ARG 291 311 311 ARG ARG B . n 
B 1 292 LEU 292 312 312 LEU LEU B . n 
B 1 293 GLU 293 313 313 GLU GLU B . n 
B 1 294 GLY 294 314 314 GLY GLY B . n 
B 1 295 ASN 295 315 315 ASN ASN B . n 
B 1 296 ALA 296 316 316 ALA ALA B . n 
B 1 297 VAL 297 317 317 VAL VAL B . n 
B 1 298 LEU 298 318 318 LEU LEU B . n 
B 1 299 TYR 299 319 319 TYR TYR B . n 
B 1 300 GLY 300 320 320 GLY GLY B . n 
B 1 301 GLY 301 321 321 GLY GLY B . n 
B 1 302 TRP 302 322 322 TRP TRP B . n 
B 1 303 SER 303 323 323 SER SER B . n 
B 1 304 PHE 304 324 324 PHE PHE B . n 
B 1 305 ALA 305 325 325 ALA ALA B . n 
B 1 306 PHE 306 326 326 PHE PHE B . n 
B 1 307 ARG 307 327 327 ARG ARG B . n 
B 1 308 LEU 308 328 328 LEU LEU B . n 
B 1 309 ARG 309 329 329 ARG ARG B . n 
B 1 310 SER 310 330 330 SER SER B . n 
B 1 311 SER 311 331 331 SER SER B . n 
B 1 312 SER 312 332 332 SER SER B . n 
B 1 313 GLY 313 333 333 GLY GLY B . n 
B 1 314 LEU 314 334 334 LEU LEU B . n 
B 1 315 GLN 315 335 335 GLN GLN B . n 
B 1 316 VAL 316 336 336 VAL VAL B . n 
B 1 317 LEU 317 337 337 LEU LEU B . n 
B 1 318 ASN 318 338 338 ASN ASN B . n 
B 1 319 VAL 319 339 339 VAL VAL B . n 
B 1 320 HIS 320 340 340 HIS HIS B . n 
B 1 321 PHE 321 341 341 PHE PHE B . n 
B 1 322 GLY 322 342 342 GLY GLY B . n 
B 1 323 GLY 323 343 343 GLY GLY B . n 
B 1 324 GLU 324 344 344 GLU GLU B . n 
B 1 325 ARG 325 345 345 ARG ARG B . n 
B 1 326 ILE 326 346 346 ILE ILE B . n 
B 1 327 ALA 327 347 347 ALA ALA B . n 
B 1 328 TYR 328 348 348 TYR TYR B . n 
B 1 329 GLU 329 349 349 GLU GLU B . n 
B 1 330 VAL 330 350 350 VAL VAL B . n 
B 1 331 SER 331 351 351 SER SER B . n 
B 1 332 VAL 332 352 352 VAL VAL B . n 
B 1 333 GLN 333 353 353 GLN GLN B . n 
B 1 334 GLU 334 354 354 GLU GLU B . n 
B 1 335 ALA 335 355 355 ALA ALA B . n 
B 1 336 VAL 336 356 356 VAL VAL B . n 
B 1 337 ALA 337 357 357 ALA ALA B . n 
B 1 338 LEU 338 358 358 LEU LEU B . n 
B 1 339 TYR 339 359 359 TYR TYR B . n 
B 1 340 GLY 340 360 360 GLY GLY B . n 
B 1 341 GLY 341 361 361 GLY GLY B . n 
B 1 342 HIS 342 362 362 HIS HIS B . n 
B 1 343 THR 343 363 363 THR THR B . n 
B 1 344 PRO 344 364 364 PRO PRO B . n 
B 1 345 ALA 345 365 365 ALA ALA B . n 
B 1 346 GLY 346 366 366 GLY GLY B . n 
B 1 347 MET 347 367 367 MET MET B . n 
B 1 348 GLN 348 368 368 GLN GLN B . n 
B 1 349 THR 349 369 369 THR THR B . n 
B 1 350 LYS 350 370 370 LYS LYS B . n 
B 1 351 TYR 351 371 371 TYR TYR B . n 
B 1 352 LEU 352 372 372 LEU LEU B . n 
B 1 353 ASP 353 373 373 ASP ASP B . n 
B 1 354 VAL 354 374 374 VAL VAL B . n 
B 1 355 GLY 355 375 375 GLY GLY B . n 
B 1 356 TRP 356 376 376 TRP TRP B . n 
B 1 357 GLY 357 377 377 GLY GLY B . n 
B 1 358 LEU 358 378 378 LEU LEU B . n 
B 1 359 GLY 359 379 379 GLY GLY B . n 
B 1 360 SER 360 380 380 SER SER B . n 
B 1 361 VAL 361 381 381 VAL VAL B . n 
B 1 362 THR 362 382 382 THR THR B . n 
B 1 363 HIS 363 383 383 HIS HIS B . n 
B 1 364 GLU 364 384 384 GLU GLU B . n 
B 1 365 LEU 365 385 385 LEU LEU B . n 
B 1 366 ALA 366 386 386 ALA ALA B . n 
B 1 367 PRO 367 387 387 PRO PRO B . n 
B 1 368 GLY 368 388 388 GLY GLY B . n 
B 1 369 ILE 369 389 389 ILE ILE B . n 
B 1 370 ASP 370 390 390 ASP ASP B . n 
B 1 371 CYS 371 391 391 CYS CYS B . n 
B 1 372 PRO 372 392 392 PRO PRO B . n 
B 1 373 GLU 373 393 393 GLU GLU B . n 
B 1 374 THR 374 394 394 THR THR B . n 
B 1 375 ALA 375 395 395 ALA ALA B . n 
B 1 376 THR 376 396 396 THR THR B . n 
B 1 377 PHE 377 397 397 PHE PHE B . n 
B 1 378 LEU 378 398 398 LEU LEU B . n 
B 1 379 ASP 379 399 399 ASP ASP B . n 
B 1 380 THR 380 400 400 THR THR B . n 
B 1 381 PHE 381 401 401 PHE PHE B . n 
B 1 382 HIS 382 402 402 HIS HIS B . n 
B 1 383 TYR 383 403 403 TYR TYR B . n 
B 1 384 TYR 384 404 404 TYR TYR B . n 
B 1 385 ASP 385 405 405 ASP ASP B . n 
B 1 386 ALA 386 406 406 ALA ALA B . n 
B 1 387 ASP 387 407 407 ASP ASP B . n 
B 1 388 ASP 388 408 408 ASP ASP B . n 
B 1 389 PRO 389 409 409 PRO PRO B . n 
B 1 390 VAL 390 410 410 VAL VAL B . n 
B 1 391 HIS 391 411 411 HIS HIS B . n 
B 1 392 TYR 392 412 412 TYR TYR B . n 
B 1 393 PRO 393 413 413 PRO PRO B . n 
B 1 394 ARG 394 414 414 ARG ARG B . n 
B 1 395 ALA 395 415 415 ALA ALA B . n 
B 1 396 LEU 396 416 416 LEU LEU B . n 
B 1 397 CYS 397 417 417 CYS CYS B . n 
B 1 398 LEU 398 418 418 LEU LEU B . n 
B 1 399 PHE 399 419 419 PHE PHE B . n 
B 1 400 GLU 400 420 420 GLU GLU B . n 
B 1 401 MET 401 421 421 MET MET B . n 
B 1 402 PRO 402 422 422 PRO PRO B . n 
B 1 403 THR 403 423 423 THR THR B . n 
B 1 404 GLY 404 424 424 GLY GLY B . n 
B 1 405 VAL 405 425 425 VAL VAL B . n 
B 1 406 PRO 406 426 426 PRO PRO B . n 
B 1 407 LEU 407 427 427 LEU LEU B . n 
B 1 408 ARG 408 428 428 ARG ARG B . n 
B 1 409 ARG 409 429 429 ARG ARG B . n 
B 1 410 HIS 410 430 430 HIS HIS B . n 
B 1 411 PHE 411 431 431 PHE PHE B . n 
B 1 412 ASN 412 432 432 ASN ASN B . n 
B 1 413 SER 413 433 433 SER SER B . n 
B 1 414 ASN 414 434 434 ASN ASN B . n 
B 1 415 PHE 415 435 435 PHE PHE B . n 
B 1 416 LYS 416 436 436 LYS LYS B . n 
B 1 417 GLY 417 437 437 GLY GLY B . n 
B 1 418 GLY 418 438 438 GLY GLY B . n 
B 1 419 PHE 419 439 439 PHE PHE B . n 
B 1 420 ASN 420 440 440 ASN ASN B . n 
B 1 421 PHE 421 441 441 PHE PHE B . n 
B 1 422 TYR 422 442 442 TYR TYR B . n 
B 1 423 ALA 423 443 443 ALA ALA B . n 
B 1 424 GLY 424 444 444 GLY GLY B . n 
B 1 425 LEU 425 445 445 LEU LEU B . n 
B 1 426 LYS 426 446 446 LYS LYS B . n 
B 1 427 GLY 427 447 447 GLY GLY B . n 
B 1 428 GLN 428 448 448 GLN GLN B . n 
B 1 429 VAL 429 449 449 VAL VAL B . n 
B 1 430 LEU 430 450 450 LEU LEU B . n 
B 1 431 VAL 431 451 451 VAL VAL B . n 
B 1 432 LEU 432 452 452 LEU LEU B . n 
B 1 433 ARG 433 453 453 ARG ARG B . n 
B 1 434 THR 434 454 454 THR THR B . n 
B 1 435 THR 435 455 455 THR THR B . n 
B 1 436 SER 436 456 456 SER SER B . n 
B 1 437 THR 437 457 457 THR THR B . n 
B 1 438 VAL 438 458 458 VAL VAL B . n 
B 1 439 TYR 439 459 459 TYR TYR B . n 
B 1 440 ASN 440 460 460 ASN ASN B . n 
B 1 441 TPQ 441 461 461 TPQ TPQ B . n 
B 1 442 ASP 442 462 462 ASP ASP B . n 
B 1 443 TYR 443 463 463 TYR TYR B . n 
B 1 444 ILE 444 464 464 ILE ILE B . n 
B 1 445 TRP 445 465 465 TRP TRP B . n 
B 1 446 ASP 446 466 466 ASP ASP B . n 
B 1 447 PHE 447 467 467 PHE PHE B . n 
B 1 448 ILE 448 468 468 ILE ILE B . n 
B 1 449 PHE 449 469 469 PHE PHE B . n 
B 1 450 TYR 450 470 470 TYR TYR B . n 
B 1 451 PRO 451 471 471 PRO PRO B . n 
B 1 452 ASN 452 472 472 ASN ASN B . n 
B 1 453 GLY 453 473 473 GLY GLY B . n 
B 1 454 VAL 454 474 474 VAL VAL B . n 
B 1 455 MET 455 475 475 MET MET B . n 
B 1 456 GLU 456 476 476 GLU GLU B . n 
B 1 457 ALA 457 477 477 ALA ALA B . n 
B 1 458 LYS 458 478 478 LYS LYS B . n 
B 1 459 MET 459 479 479 MET MET B . n 
B 1 460 HIS 460 480 480 HIS HIS B . n 
B 1 461 ALA 461 481 481 ALA ALA B . n 
B 1 462 THR 462 482 482 THR THR B . n 
B 1 463 GLY 463 483 483 GLY GLY B . n 
B 1 464 TYR 464 484 484 TYR TYR B . n 
B 1 465 VAL 465 485 485 VAL VAL B . n 
B 1 466 HIS 466 486 486 HIS HIS B . n 
B 1 467 ALA 467 487 487 ALA ALA B . n 
B 1 468 THR 468 488 488 THR THR B . n 
B 1 469 PHE 469 489 489 PHE PHE B . n 
B 1 470 TYR 470 490 490 TYR TYR B . n 
B 1 471 THR 471 491 491 THR THR B . n 
B 1 472 PRO 472 492 492 PRO PRO B . n 
B 1 473 GLU 473 493 493 GLU GLU B . n 
B 1 474 GLY 474 494 494 GLY GLY B . n 
B 1 475 LEU 475 495 495 LEU LEU B . n 
B 1 476 ARG 476 496 496 ARG ARG B . n 
B 1 477 HIS 477 497 497 HIS HIS B . n 
B 1 478 GLY 478 498 498 GLY GLY B . n 
B 1 479 THR 479 499 499 THR THR B . n 
B 1 480 ARG 480 500 500 ARG ARG B . n 
B 1 481 LEU 481 501 501 LEU LEU B . n 
B 1 482 HIS 482 502 502 HIS HIS B . n 
B 1 483 THR 483 503 503 THR THR B . n 
B 1 484 HIS 484 504 504 HIS HIS B . n 
B 1 485 LEU 485 505 505 LEU LEU B . n 
B 1 486 ILE 486 506 506 ILE ILE B . n 
B 1 487 GLY 487 507 507 GLY GLY B . n 
B 1 488 ASN 488 508 508 ASN ASN B . n 
B 1 489 ILE 489 509 509 ILE ILE B . n 
B 1 490 HIS 490 510 510 HIS HIS B . n 
B 1 491 THR 491 511 511 THR THR B . n 
B 1 492 HIS 492 512 512 HIS HIS B . n 
B 1 493 LEU 493 513 513 LEU LEU B . n 
B 1 494 VAL 494 514 514 VAL VAL B . n 
B 1 495 HIS 495 515 515 HIS HIS B . n 
B 1 496 TYR 496 516 516 TYR TYR B . n 
B 1 497 ARG 497 517 517 ARG ARG B . n 
B 1 498 VAL 498 518 518 VAL VAL B . n 
B 1 499 ASP 499 519 519 ASP ASP B . n 
B 1 500 LEU 500 520 520 LEU LEU B . n 
B 1 501 ASP 501 521 521 ASP ASP B . n 
B 1 502 VAL 502 522 522 VAL VAL B . n 
B 1 503 ALA 503 523 523 ALA ALA B . n 
B 1 504 GLY 504 524 524 GLY GLY B . n 
B 1 505 THR 505 525 525 THR THR B . n 
B 1 506 LYS 506 526 526 LYS LYS B . n 
B 1 507 ASN 507 527 527 ASN ASN B . n 
B 1 508 SER 508 528 528 SER SER B . n 
B 1 509 PHE 509 529 529 PHE PHE B . n 
B 1 510 GLN 510 530 530 GLN GLN B . n 
B 1 511 THR 511 531 531 THR THR B . n 
B 1 512 LEU 512 532 532 LEU LEU B . n 
B 1 513 GLN 513 533 533 GLN GLN B . n 
B 1 514 MET 514 534 534 MET MET B . n 
B 1 515 LYS 515 535 535 LYS LYS B . n 
B 1 516 LEU 516 536 536 LEU LEU B . n 
B 1 517 GLU 517 537 537 GLU GLU B . n 
B 1 518 ASN 518 538 538 ASN ASN B . n 
B 1 519 ILE 519 539 539 ILE ILE B . n 
B 1 520 THR 520 540 540 THR THR B . n 
B 1 521 ASN 521 541 541 ASN ASN B . n 
B 1 522 PRO 522 542 542 PRO PRO B . n 
B 1 523 TRP 523 543 543 TRP TRP B . n 
B 1 524 SER 524 544 544 SER SER B . n 
B 1 525 PRO 525 545 545 PRO PRO B . n 
B 1 526 ARG 526 546 546 ARG ARG B . n 
B 1 527 HIS 527 547 547 HIS HIS B . n 
B 1 528 ARG 528 548 548 ARG ARG B . n 
B 1 529 VAL 529 549 549 VAL VAL B . n 
B 1 530 VAL 530 550 550 VAL VAL B . n 
B 1 531 GLN 531 551 551 GLN GLN B . n 
B 1 532 PRO 532 552 552 PRO PRO B . n 
B 1 533 THR 533 553 553 THR THR B . n 
B 1 534 LEU 534 554 554 LEU LEU B . n 
B 1 535 GLU 535 555 555 GLU GLU B . n 
B 1 536 GLN 536 556 556 GLN GLN B . n 
B 1 537 THR 537 557 557 THR THR B . n 
B 1 538 GLN 538 558 558 GLN GLN B . n 
B 1 539 TYR 539 559 559 TYR TYR B . n 
B 1 540 SER 540 560 560 SER SER B . n 
B 1 541 TRP 541 561 561 TRP TRP B . n 
B 1 542 GLU 542 562 562 GLU GLU B . n 
B 1 543 ARG 543 563 563 ARG ARG B . n 
B 1 544 GLN 544 564 564 GLN GLN B . n 
B 1 545 ALA 545 565 565 ALA ALA B . n 
B 1 546 ALA 546 566 566 ALA ALA B . n 
B 1 547 PHE 547 567 567 PHE PHE B . n 
B 1 548 ARG 548 568 568 ARG ARG B . n 
B 1 549 PHE 549 569 569 PHE PHE B . n 
B 1 550 LYS 550 570 570 LYS LYS B . n 
B 1 551 ARG 551 571 571 ARG ARG B . n 
B 1 552 LYS 552 572 572 LYS LYS B . n 
B 1 553 LEU 553 573 573 LEU LEU B . n 
B 1 554 PRO 554 574 574 PRO PRO B . n 
B 1 555 LYS 555 575 575 LYS LYS B . n 
B 1 556 TYR 556 576 576 TYR TYR B . n 
B 1 557 LEU 557 577 577 LEU LEU B . n 
B 1 558 LEU 558 578 578 LEU LEU B . n 
B 1 559 PHE 559 579 579 PHE PHE B . n 
B 1 560 THR 560 580 580 THR THR B . n 
B 1 561 SER 561 581 581 SER SER B . n 
B 1 562 PRO 562 582 582 PRO PRO B . n 
B 1 563 GLN 563 583 583 GLN GLN B . n 
B 1 564 GLU 564 584 584 GLU GLU B . n 
B 1 565 ASN 565 585 585 ASN ASN B . n 
B 1 566 PRO 566 586 586 PRO PRO B . n 
B 1 567 TRP 567 587 587 TRP TRP B . n 
B 1 568 GLY 568 588 588 GLY GLY B . n 
B 1 569 HIS 569 589 589 HIS HIS B . n 
B 1 570 LYS 570 590 590 LYS LYS B . n 
B 1 571 ARG 571 591 591 ARG ARG B . n 
B 1 572 SER 572 592 592 SER SER B . n 
B 1 573 TYR 573 593 593 TYR TYR B . n 
B 1 574 ARG 574 594 594 ARG ARG B . n 
B 1 575 LEU 575 595 595 LEU LEU B . n 
B 1 576 GLN 576 596 596 GLN GLN B . n 
B 1 577 ILE 577 597 597 ILE ILE B . n 
B 1 578 HIS 578 598 598 HIS HIS B . n 
B 1 579 SER 579 599 599 SER SER B . n 
B 1 580 MET 580 600 600 MET MET B . n 
B 1 581 ALA 581 601 601 ALA ALA B . n 
B 1 582 ASP 582 602 602 ASP ASP B . n 
B 1 583 GLN 583 603 603 GLN GLN B . n 
B 1 584 VAL 584 604 604 VAL VAL B . n 
B 1 585 LEU 585 605 605 LEU LEU B . n 
B 1 586 PRO 586 606 606 PRO PRO B . n 
B 1 587 PRO 587 607 607 PRO PRO B . n 
B 1 588 GLY 588 608 608 GLY GLY B . n 
B 1 589 TRP 589 609 609 TRP TRP B . n 
B 1 590 GLN 590 610 610 GLN GLN B . n 
B 1 591 GLU 591 611 611 GLU GLU B . n 
B 1 592 GLU 592 612 612 GLU GLU B . n 
B 1 593 GLN 593 613 613 GLN GLN B . n 
B 1 594 ALA 594 614 614 ALA ALA B . n 
B 1 595 ILE 595 615 615 ILE ILE B . n 
B 1 596 THR 596 616 616 THR THR B . n 
B 1 597 TRP 597 617 617 TRP TRP B . n 
B 1 598 ALA 598 618 618 ALA ALA B . n 
B 1 599 ARG 599 619 619 ARG ARG B . n 
B 1 600 TYR 600 620 620 TYR TYR B . n 
B 1 601 PRO 601 621 621 PRO PRO B . n 
B 1 602 LEU 602 622 622 LEU LEU B . n 
B 1 603 ALA 603 623 623 ALA ALA B . n 
B 1 604 VAL 604 624 624 VAL VAL B . n 
B 1 605 THR 605 625 625 THR THR B . n 
B 1 606 LYS 606 626 626 LYS LYS B . n 
B 1 607 TYR 607 627 627 TYR TYR B . n 
B 1 608 ARG 608 628 628 ARG ARG B . n 
B 1 609 GLU 609 629 629 GLU GLU B . n 
B 1 610 SER 610 630 630 SER SER B . n 
B 1 611 GLU 611 631 631 GLU GLU B . n 
B 1 612 LEU 612 632 632 LEU LEU B . n 
B 1 613 CYS 613 633 633 CYS CYS B . n 
B 1 614 SER 614 634 634 SER SER B . n 
B 1 615 SER 615 635 635 SER SER B . n 
B 1 616 SER 616 636 636 SER SER B . n 
B 1 617 ILE 617 637 637 ILE ILE B . n 
B 1 618 TYR 618 638 638 TYR TYR B . n 
B 1 619 HIS 619 639 639 HIS HIS B . n 
B 1 620 GLN 620 640 640 GLN GLN B . n 
B 1 621 ASN 621 641 641 ASN ASN B . n 
B 1 622 ASP 622 642 642 ASP ASP B . n 
B 1 623 PRO 623 643 643 PRO PRO B . n 
B 1 624 TRP 624 644 644 TRP TRP B . n 
B 1 625 ASP 625 645 645 ASP ASP B . n 
B 1 626 PRO 626 646 646 PRO PRO B . n 
B 1 627 PRO 627 647 647 PRO PRO B . n 
B 1 628 VAL 628 648 648 VAL VAL B . n 
B 1 629 VAL 629 649 649 VAL VAL B . n 
B 1 630 PHE 630 650 650 PHE PHE B . n 
B 1 631 GLU 631 651 651 GLU GLU B . n 
B 1 632 GLN 632 652 652 GLN GLN B . n 
B 1 633 PHE 633 653 653 PHE PHE B . n 
B 1 634 LEU 634 654 654 LEU LEU B . n 
B 1 635 HIS 635 655 655 HIS HIS B . n 
B 1 636 ASN 636 656 656 ASN ASN B . n 
B 1 637 ASN 637 657 657 ASN ASN B . n 
B 1 638 GLU 638 658 658 GLU GLU B . n 
B 1 639 ASN 639 659 659 ASN ASN B . n 
B 1 640 ILE 640 660 660 ILE ILE B . n 
B 1 641 GLU 641 661 661 GLU GLU B . n 
B 1 642 ASN 642 662 662 ASN ASN B . n 
B 1 643 GLU 643 663 663 GLU GLU B . n 
B 1 644 ASP 644 664 664 ASP ASP B . n 
B 1 645 LEU 645 665 665 LEU LEU B . n 
B 1 646 VAL 646 666 666 VAL VAL B . n 
B 1 647 ALA 647 667 667 ALA ALA B . n 
B 1 648 TRP 648 668 668 TRP TRP B . n 
B 1 649 VAL 649 669 669 VAL VAL B . n 
B 1 650 THR 650 670 670 THR THR B . n 
B 1 651 VAL 651 671 671 VAL VAL B . n 
B 1 652 GLY 652 672 672 GLY GLY B . n 
B 1 653 PHE 653 673 673 PHE PHE B . n 
B 1 654 LEU 654 674 674 LEU LEU B . n 
B 1 655 HIS 655 675 675 HIS HIS B . n 
B 1 656 ILE 656 676 676 ILE ILE B . n 
B 1 657 PRO 657 677 677 PRO PRO B . n 
B 1 658 HIS 658 678 678 HIS HIS B . n 
B 1 659 SER 659 679 679 SER SER B . n 
B 1 660 GLU 660 680 680 GLU GLU B . n 
B 1 661 ASP 661 681 681 ASP ASP B . n 
B 1 662 ILE 662 682 682 ILE ILE B . n 
B 1 663 PRO 663 683 683 PRO PRO B . n 
B 1 664 ASN 664 684 684 ASN ASN B . n 
B 1 665 THR 665 685 685 THR THR B . n 
B 1 666 ALA 666 686 686 ALA ALA B . n 
B 1 667 THR 667 687 687 THR THR B . n 
B 1 668 PRO 668 688 688 PRO PRO B . n 
B 1 669 GLY 669 689 689 GLY GLY B . n 
B 1 670 ASN 670 690 690 ASN ASN B . n 
B 1 671 SER 671 691 691 SER SER B . n 
B 1 672 VAL 672 692 692 VAL VAL B . n 
B 1 673 GLY 673 693 693 GLY GLY B . n 
B 1 674 PHE 674 694 694 PHE PHE B . n 
B 1 675 LEU 675 695 695 LEU LEU B . n 
B 1 676 LEU 676 696 696 LEU LEU B . n 
B 1 677 ARG 677 697 697 ARG ARG B . n 
B 1 678 PRO 678 698 698 PRO PRO B . n 
B 1 679 PHE 679 699 699 PHE PHE B . n 
B 1 680 ASN 680 700 700 ASN ASN B . n 
B 1 681 PHE 681 701 701 PHE PHE B . n 
B 1 682 PHE 682 702 702 PHE PHE B . n 
B 1 683 PRO 683 703 703 PRO PRO B . n 
B 1 684 GLU 684 704 704 GLU GLU B . n 
B 1 685 ASP 685 705 705 ASP ASP B . n 
B 1 686 PRO 686 706 706 PRO PRO B . n 
B 1 687 SER 687 707 707 SER SER B . n 
B 1 688 LEU 688 708 708 LEU LEU B . n 
B 1 689 ALA 689 709 709 ALA ALA B . n 
B 1 690 SER 690 710 710 SER SER B . n 
B 1 691 ARG 691 711 711 ARG ARG B . n 
B 1 692 ASP 692 712 712 ASP ASP B . n 
B 1 693 THR 693 713 713 THR THR B . n 
B 1 694 VAL 694 714 714 VAL VAL B . n 
B 1 695 ILE 695 715 715 ILE ILE B . n 
B 1 696 VAL 696 716 716 VAL VAL B . n 
B 1 697 TRP 697 717 717 TRP TRP B . n 
B 1 698 PRO 698 718 718 PRO PRO B . n 
B 1 699 ARG 699 719 719 ARG ARG B . n 
B 1 700 ASP 700 720 720 ASP ASP B . n 
B 1 701 ASN 701 721 721 ASN ASN B . n 
B 1 702 GLY 702 722 722 GLY GLY B . n 
B 1 703 PRO 703 723 723 PRO PRO B . n 
B 1 704 ASN 704 724 724 ASN ASN B . n 
B 1 705 TYR 705 725 725 TYR TYR B . n 
B 1 706 VAL 706 726 726 VAL VAL B . n 
B 1 707 GLN 707 727 727 GLN GLN B . n 
B 1 708 ARG 708 728 728 ARG ARG B . n 
B 1 709 TRP 709 729 729 TRP TRP B . n 
B 1 710 ILE 710 730 730 ILE ILE B . n 
B 1 711 PRO 711 731 731 PRO PRO B . n 
B 1 712 GLU 712 732 732 GLU GLU B . n 
B 1 713 ASP 713 733 733 ASP ASP B . n 
B 1 714 ARG 714 734 734 ARG ARG B . n 
B 1 715 ASP 715 735 735 ASP ASP B . n 
B 1 716 CYS 716 736 736 CYS CYS B . n 
B 1 717 SER 717 737 737 SER SER B . n 
B 1 718 MET 718 738 738 MET MET B . n 
B 1 719 PRO 719 739 739 PRO PRO B . n 
B 1 720 PRO 720 740 740 PRO PRO B . n 
B 1 721 PRO 721 741 741 PRO PRO B . n 
B 1 722 PHE 722 742 742 PHE PHE B . n 
B 1 723 SER 723 743 743 SER SER B . n 
B 1 724 TYR 724 744 744 TYR TYR B . n 
B 1 725 ASN 725 745 745 ASN ASN B . n 
B 1 726 GLY 726 746 746 GLY GLY B . n 
B 1 727 THR 727 747 747 THR THR B . n 
B 1 728 TYR 728 748 748 TYR TYR B . n 
B 1 729 ARG 729 749 749 ARG ARG B . n 
B 1 730 PRO 730 750 750 PRO PRO B . n 
B 1 731 VAL 731 751 751 VAL VAL 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 CU  1   801  801  CU  CU  A . 
D 3 CA  1   802  802  CA  CA  A . 
E 3 CA  1   803  803  CA  CA  A . 
F 4 GOL 1   804  804  GOL GOL A . 
G 5 PNT 1   901  901  PNT PNT A . 
H 6 NAG 1   1101 1101 NAG NAG A . 
I 6 NAG 2   1102 1102 NAG NAG A . 
J 7 BMA 3   1103 1103 BMA BMA A . 
K 6 NAG 1   5381 5381 NAG NAG A . 
L 6 NAG 2   5382 5382 NAG NAG A . 
M 6 NAG 1   7451 7451 NAG NAG A . 
N 6 NAG 2   7452 7452 NAG NAG A . 
O 2 CU  1   801  801  CU  CU  B . 
P 3 CA  1   802  802  CA  CA  B . 
Q 3 CA  1   803  803  CA  CA  B . 
R 5 PNT 1   901  901  PNT PNT B . 
S 6 NAG 1   1101 1101 NAG NAG B . 
T 6 NAG 2   1102 1102 NAG NAG B . 
U 6 NAG 1   5381 5381 NAG NAG B . 
V 6 NAG 2   5382 5382 NAG NAG B . 
W 6 NAG 1   7451 7451 NAG NAG B . 
X 6 NAG 2   7452 7452 NAG NAG B . 
Y 8 HOH 1   2    2    HOH HOH A . 
Y 8 HOH 2   6    6    HOH HOH A . 
Y 8 HOH 3   7    7    HOH HOH A . 
Y 8 HOH 4   8    8    HOH HOH A . 
Y 8 HOH 5   9    9    HOH HOH A . 
Y 8 HOH 6   11   11   HOH HOH A . 
Y 8 HOH 7   12   12   HOH HOH A . 
Y 8 HOH 8   13   13   HOH HOH A . 
Y 8 HOH 9   14   14   HOH HOH A . 
Y 8 HOH 10  16   16   HOH HOH A . 
Y 8 HOH 11  19   19   HOH HOH A . 
Y 8 HOH 12  20   20   HOH HOH A . 
Y 8 HOH 13  752  21   HOH HOH A . 
Y 8 HOH 14  753  753  HOH HOH A . 
Y 8 HOH 15  754  754  HOH HOH A . 
Y 8 HOH 16  755  755  HOH HOH A . 
Y 8 HOH 17  756  756  HOH HOH A . 
Y 8 HOH 18  757  22   HOH HOH A . 
Y 8 HOH 19  758  23   HOH HOH A . 
Y 8 HOH 20  759  24   HOH HOH A . 
Y 8 HOH 21  760  25   HOH HOH A . 
Y 8 HOH 22  761  27   HOH HOH A . 
Y 8 HOH 23  762  762  HOH HOH A . 
Y 8 HOH 24  763  28   HOH HOH A . 
Y 8 HOH 25  764  764  HOH HOH A . 
Y 8 HOH 26  765  765  HOH HOH A . 
Y 8 HOH 27  766  31   HOH HOH A . 
Y 8 HOH 28  767  767  HOH HOH A . 
Y 8 HOH 29  768  32   HOH HOH A . 
Y 8 HOH 30  769  769  HOH HOH A . 
Y 8 HOH 31  770  770  HOH HOH A . 
Y 8 HOH 32  771  771  HOH HOH A . 
Y 8 HOH 33  772  34   HOH HOH A . 
Y 8 HOH 34  773  773  HOH HOH A . 
Y 8 HOH 35  774  774  HOH HOH A . 
Y 8 HOH 36  775  36   HOH HOH A . 
Y 8 HOH 37  776  40   HOH HOH A . 
Y 8 HOH 38  777  777  HOH HOH A . 
Y 8 HOH 39  778  41   HOH HOH A . 
Y 8 HOH 40  779  42   HOH HOH A . 
Y 8 HOH 41  780  44   HOH HOH A . 
Y 8 HOH 42  781  46   HOH HOH A . 
Y 8 HOH 43  782  48   HOH HOH A . 
Y 8 HOH 44  783  783  HOH HOH A . 
Y 8 HOH 45  784  784  HOH HOH A . 
Y 8 HOH 46  785  49   HOH HOH A . 
Y 8 HOH 47  786  786  HOH HOH A . 
Y 8 HOH 48  787  52   HOH HOH A . 
Y 8 HOH 49  788  788  HOH HOH A . 
Y 8 HOH 50  789  53   HOH HOH A . 
Y 8 HOH 51  790  56   HOH HOH A . 
Y 8 HOH 52  791  791  HOH HOH A . 
Y 8 HOH 53  792  57   HOH HOH A . 
Y 8 HOH 54  793  59   HOH HOH A . 
Y 8 HOH 55  794  794  HOH HOH A . 
Y 8 HOH 56  795  795  HOH HOH A . 
Y 8 HOH 57  796  796  HOH HOH A . 
Y 8 HOH 58  797  797  HOH HOH A . 
Y 8 HOH 59  798  798  HOH HOH A . 
Y 8 HOH 60  799  60   HOH HOH A . 
Y 8 HOH 61  800  800  HOH HOH A . 
Y 8 HOH 62  805  61   HOH HOH A . 
Y 8 HOH 63  806  62   HOH HOH A . 
Y 8 HOH 64  807  64   HOH HOH A . 
Y 8 HOH 65  808  808  HOH HOH A . 
Y 8 HOH 66  809  65   HOH HOH A . 
Y 8 HOH 67  810  810  HOH HOH A . 
Y 8 HOH 68  811  66   HOH HOH A . 
Y 8 HOH 69  812  67   HOH HOH A . 
Y 8 HOH 70  813  68   HOH HOH A . 
Y 8 HOH 71  814  72   HOH HOH A . 
Y 8 HOH 72  815  73   HOH HOH A . 
Y 8 HOH 73  816  74   HOH HOH A . 
Y 8 HOH 74  817  76   HOH HOH A . 
Y 8 HOH 75  818  77   HOH HOH A . 
Y 8 HOH 76  819  78   HOH HOH A . 
Y 8 HOH 77  820  79   HOH HOH A . 
Y 8 HOH 78  821  82   HOH HOH A . 
Y 8 HOH 79  822  83   HOH HOH A . 
Y 8 HOH 80  823  823  HOH HOH A . 
Y 8 HOH 81  824  824  HOH HOH A . 
Y 8 HOH 82  825  825  HOH HOH A . 
Y 8 HOH 83  826  826  HOH HOH A . 
Y 8 HOH 84  827  84   HOH HOH A . 
Y 8 HOH 85  828  828  HOH HOH A . 
Y 8 HOH 86  829  829  HOH HOH A . 
Y 8 HOH 87  830  85   HOH HOH A . 
Y 8 HOH 88  831  831  HOH HOH A . 
Y 8 HOH 89  832  86   HOH HOH A . 
Y 8 HOH 90  833  833  HOH HOH A . 
Y 8 HOH 91  834  90   HOH HOH A . 
Y 8 HOH 92  835  835  HOH HOH A . 
Y 8 HOH 93  836  836  HOH HOH A . 
Y 8 HOH 94  837  837  HOH HOH A . 
Y 8 HOH 95  838  91   HOH HOH A . 
Y 8 HOH 96  839  839  HOH HOH A . 
Y 8 HOH 97  840  94   HOH HOH A . 
Y 8 HOH 98  841  95   HOH HOH A . 
Y 8 HOH 99  842  98   HOH HOH A . 
Y 8 HOH 100 843  99   HOH HOH A . 
Y 8 HOH 101 844  844  HOH HOH A . 
Y 8 HOH 102 845  100  HOH HOH A . 
Y 8 HOH 103 846  846  HOH HOH A . 
Y 8 HOH 104 847  847  HOH HOH A . 
Y 8 HOH 105 848  101  HOH HOH A . 
Y 8 HOH 106 849  102  HOH HOH A . 
Y 8 HOH 107 850  104  HOH HOH A . 
Y 8 HOH 108 851  851  HOH HOH A . 
Y 8 HOH 109 852  107  HOH HOH A . 
Y 8 HOH 110 853  108  HOH HOH A . 
Y 8 HOH 111 854  854  HOH HOH A . 
Y 8 HOH 112 855  109  HOH HOH A . 
Y 8 HOH 113 856  856  HOH HOH A . 
Y 8 HOH 114 857  857  HOH HOH A . 
Y 8 HOH 115 858  110  HOH HOH A . 
Y 8 HOH 116 859  859  HOH HOH A . 
Y 8 HOH 117 860  860  HOH HOH A . 
Y 8 HOH 118 861  112  HOH HOH A . 
Y 8 HOH 119 862  862  HOH HOH A . 
Y 8 HOH 120 863  863  HOH HOH A . 
Y 8 HOH 121 864  864  HOH HOH A . 
Y 8 HOH 122 865  865  HOH HOH A . 
Y 8 HOH 123 866  866  HOH HOH A . 
Y 8 HOH 124 867  867  HOH HOH A . 
Y 8 HOH 125 868  868  HOH HOH A . 
Y 8 HOH 126 869  869  HOH HOH A . 
Y 8 HOH 127 870  113  HOH HOH A . 
Y 8 HOH 128 871  871  HOH HOH A . 
Y 8 HOH 129 872  114  HOH HOH A . 
Y 8 HOH 130 873  873  HOH HOH A . 
Y 8 HOH 131 874  874  HOH HOH A . 
Y 8 HOH 132 875  115  HOH HOH A . 
Y 8 HOH 133 876  116  HOH HOH A . 
Y 8 HOH 134 877  877  HOH HOH A . 
Y 8 HOH 135 878  120  HOH HOH A . 
Y 8 HOH 136 879  122  HOH HOH A . 
Y 8 HOH 137 880  123  HOH HOH A . 
Y 8 HOH 138 881  881  HOH HOH A . 
Y 8 HOH 139 882  127  HOH HOH A . 
Y 8 HOH 140 883  128  HOH HOH A . 
Y 8 HOH 141 884  884  HOH HOH A . 
Y 8 HOH 142 885  885  HOH HOH A . 
Y 8 HOH 143 886  129  HOH HOH A . 
Y 8 HOH 144 887  133  HOH HOH A . 
Y 8 HOH 145 888  134  HOH HOH A . 
Y 8 HOH 146 889  138  HOH HOH A . 
Y 8 HOH 147 890  890  HOH HOH A . 
Y 8 HOH 148 891  140  HOH HOH A . 
Y 8 HOH 149 892  141  HOH HOH A . 
Y 8 HOH 150 893  151  HOH HOH A . 
Y 8 HOH 151 894  152  HOH HOH A . 
Y 8 HOH 152 895  895  HOH HOH A . 
Y 8 HOH 153 896  896  HOH HOH A . 
Y 8 HOH 154 897  154  HOH HOH A . 
Y 8 HOH 155 898  156  HOH HOH A . 
Y 8 HOH 156 899  163  HOH HOH A . 
Y 8 HOH 157 900  164  HOH HOH A . 
Y 8 HOH 158 902  165  HOH HOH A . 
Y 8 HOH 159 903  903  HOH HOH A . 
Y 8 HOH 160 904  168  HOH HOH A . 
Y 8 HOH 161 905  905  HOH HOH A . 
Y 8 HOH 162 906  906  HOH HOH A . 
Y 8 HOH 163 907  176  HOH HOH A . 
Y 8 HOH 164 908  178  HOH HOH A . 
Y 8 HOH 165 909  179  HOH HOH A . 
Y 8 HOH 166 910  180  HOH HOH A . 
Y 8 HOH 167 911  182  HOH HOH A . 
Y 8 HOH 168 912  185  HOH HOH A . 
Y 8 HOH 169 913  187  HOH HOH A . 
Y 8 HOH 170 914  914  HOH HOH A . 
Y 8 HOH 171 915  915  HOH HOH A . 
Y 8 HOH 172 916  916  HOH HOH A . 
Y 8 HOH 173 917  917  HOH HOH A . 
Y 8 HOH 174 918  190  HOH HOH A . 
Y 8 HOH 175 919  919  HOH HOH A . 
Y 8 HOH 176 920  920  HOH HOH A . 
Y 8 HOH 177 921  191  HOH HOH A . 
Y 8 HOH 178 922  192  HOH HOH A . 
Y 8 HOH 179 923  923  HOH HOH A . 
Y 8 HOH 180 924  924  HOH HOH A . 
Y 8 HOH 181 925  925  HOH HOH A . 
Y 8 HOH 182 926  193  HOH HOH A . 
Y 8 HOH 183 927  195  HOH HOH A . 
Y 8 HOH 184 928  202  HOH HOH A . 
Y 8 HOH 185 929  205  HOH HOH A . 
Y 8 HOH 186 930  206  HOH HOH A . 
Y 8 HOH 187 931  207  HOH HOH A . 
Y 8 HOH 188 932  209  HOH HOH A . 
Y 8 HOH 189 933  212  HOH HOH A . 
Y 8 HOH 190 934  213  HOH HOH A . 
Y 8 HOH 191 935  214  HOH HOH A . 
Y 8 HOH 192 936  215  HOH HOH A . 
Y 8 HOH 193 937  216  HOH HOH A . 
Y 8 HOH 194 938  219  HOH HOH A . 
Y 8 HOH 195 939  221  HOH HOH A . 
Y 8 HOH 196 940  223  HOH HOH A . 
Y 8 HOH 197 941  224  HOH HOH A . 
Y 8 HOH 198 942  225  HOH HOH A . 
Y 8 HOH 199 943  226  HOH HOH A . 
Y 8 HOH 200 944  227  HOH HOH A . 
Y 8 HOH 201 945  228  HOH HOH A . 
Y 8 HOH 202 946  230  HOH HOH A . 
Y 8 HOH 203 947  232  HOH HOH A . 
Y 8 HOH 204 948  234  HOH HOH A . 
Y 8 HOH 205 949  235  HOH HOH A . 
Y 8 HOH 206 950  242  HOH HOH A . 
Y 8 HOH 207 951  245  HOH HOH A . 
Y 8 HOH 208 952  246  HOH HOH A . 
Y 8 HOH 209 953  248  HOH HOH A . 
Y 8 HOH 210 954  249  HOH HOH A . 
Y 8 HOH 211 955  251  HOH HOH A . 
Y 8 HOH 212 956  252  HOH HOH A . 
Y 8 HOH 213 957  254  HOH HOH A . 
Y 8 HOH 214 958  255  HOH HOH A . 
Y 8 HOH 215 959  256  HOH HOH A . 
Y 8 HOH 216 960  257  HOH HOH A . 
Y 8 HOH 217 961  258  HOH HOH A . 
Y 8 HOH 218 962  262  HOH HOH A . 
Y 8 HOH 219 963  267  HOH HOH A . 
Y 8 HOH 220 964  268  HOH HOH A . 
Y 8 HOH 221 965  270  HOH HOH A . 
Y 8 HOH 222 966  271  HOH HOH A . 
Y 8 HOH 223 967  273  HOH HOH A . 
Y 8 HOH 224 968  275  HOH HOH A . 
Y 8 HOH 225 969  276  HOH HOH A . 
Y 8 HOH 226 970  277  HOH HOH A . 
Y 8 HOH 227 971  279  HOH HOH A . 
Y 8 HOH 228 972  281  HOH HOH A . 
Y 8 HOH 229 973  282  HOH HOH A . 
Y 8 HOH 230 974  284  HOH HOH A . 
Y 8 HOH 231 975  285  HOH HOH A . 
Y 8 HOH 232 976  289  HOH HOH A . 
Y 8 HOH 233 977  290  HOH HOH A . 
Y 8 HOH 234 978  292  HOH HOH A . 
Y 8 HOH 235 979  293  HOH HOH A . 
Y 8 HOH 236 980  296  HOH HOH A . 
Y 8 HOH 237 981  300  HOH HOH A . 
Y 8 HOH 238 982  305  HOH HOH A . 
Y 8 HOH 239 983  306  HOH HOH A . 
Y 8 HOH 240 984  307  HOH HOH A . 
Y 8 HOH 241 985  308  HOH HOH A . 
Y 8 HOH 242 986  310  HOH HOH A . 
Y 8 HOH 243 987  315  HOH HOH A . 
Y 8 HOH 244 988  317  HOH HOH A . 
Y 8 HOH 245 989  318  HOH HOH A . 
Y 8 HOH 246 990  319  HOH HOH A . 
Y 8 HOH 247 991  320  HOH HOH A . 
Y 8 HOH 248 992  321  HOH HOH A . 
Y 8 HOH 249 993  322  HOH HOH A . 
Y 8 HOH 250 994  323  HOH HOH A . 
Y 8 HOH 251 995  324  HOH HOH A . 
Y 8 HOH 252 996  325  HOH HOH A . 
Y 8 HOH 253 997  326  HOH HOH A . 
Y 8 HOH 254 998  327  HOH HOH A . 
Y 8 HOH 255 999  328  HOH HOH A . 
Y 8 HOH 256 1000 329  HOH HOH A . 
Y 8 HOH 257 1001 330  HOH HOH A . 
Y 8 HOH 258 1002 331  HOH HOH A . 
Y 8 HOH 259 1003 332  HOH HOH A . 
Y 8 HOH 260 1004 333  HOH HOH A . 
Y 8 HOH 261 1005 335  HOH HOH A . 
Y 8 HOH 262 1006 338  HOH HOH A . 
Y 8 HOH 263 1007 340  HOH HOH A . 
Y 8 HOH 264 1008 344  HOH HOH A . 
Y 8 HOH 265 1009 347  HOH HOH A . 
Y 8 HOH 266 1010 348  HOH HOH A . 
Y 8 HOH 267 1011 350  HOH HOH A . 
Y 8 HOH 268 1012 352  HOH HOH A . 
Y 8 HOH 269 1013 353  HOH HOH A . 
Y 8 HOH 270 1014 354  HOH HOH A . 
Y 8 HOH 271 1015 357  HOH HOH A . 
Y 8 HOH 272 1016 358  HOH HOH A . 
Y 8 HOH 273 1017 359  HOH HOH A . 
Y 8 HOH 274 1018 361  HOH HOH A . 
Y 8 HOH 275 1019 363  HOH HOH A . 
Y 8 HOH 276 1020 365  HOH HOH A . 
Y 8 HOH 277 1021 366  HOH HOH A . 
Y 8 HOH 278 1022 369  HOH HOH A . 
Y 8 HOH 279 1023 371  HOH HOH A . 
Y 8 HOH 280 1024 372  HOH HOH A . 
Y 8 HOH 281 1025 374  HOH HOH A . 
Y 8 HOH 282 1026 375  HOH HOH A . 
Y 8 HOH 283 1027 376  HOH HOH A . 
Y 8 HOH 284 1028 378  HOH HOH A . 
Y 8 HOH 285 1029 380  HOH HOH A . 
Y 8 HOH 286 1030 381  HOH HOH A . 
Y 8 HOH 287 1031 383  HOH HOH A . 
Y 8 HOH 288 1032 385  HOH HOH A . 
Y 8 HOH 289 1033 387  HOH HOH A . 
Y 8 HOH 290 1034 391  HOH HOH A . 
Y 8 HOH 291 1035 393  HOH HOH A . 
Y 8 HOH 292 1036 394  HOH HOH A . 
Y 8 HOH 293 1037 396  HOH HOH A . 
Y 8 HOH 294 1038 398  HOH HOH A . 
Y 8 HOH 295 1039 399  HOH HOH A . 
Y 8 HOH 296 1040 400  HOH HOH A . 
Y 8 HOH 297 1041 405  HOH HOH A . 
Y 8 HOH 298 1042 406  HOH HOH A . 
Y 8 HOH 299 1043 408  HOH HOH A . 
Y 8 HOH 300 1044 410  HOH HOH A . 
Y 8 HOH 301 1045 413  HOH HOH A . 
Y 8 HOH 302 1046 415  HOH HOH A . 
Y 8 HOH 303 1047 416  HOH HOH A . 
Y 8 HOH 304 1048 423  HOH HOH A . 
Y 8 HOH 305 1049 424  HOH HOH A . 
Y 8 HOH 306 1050 425  HOH HOH A . 
Y 8 HOH 307 1051 426  HOH HOH A . 
Y 8 HOH 308 1052 433  HOH HOH A . 
Y 8 HOH 309 1053 436  HOH HOH A . 
Y 8 HOH 310 1054 441  HOH HOH A . 
Y 8 HOH 311 1055 446  HOH HOH A . 
Y 8 HOH 312 1056 448  HOH HOH A . 
Y 8 HOH 313 1057 451  HOH HOH A . 
Y 8 HOH 314 1058 452  HOH HOH A . 
Y 8 HOH 315 1059 455  HOH HOH A . 
Y 8 HOH 316 1060 456  HOH HOH A . 
Y 8 HOH 317 1061 459  HOH HOH A . 
Y 8 HOH 318 1062 460  HOH HOH A . 
Y 8 HOH 319 1063 463  HOH HOH A . 
Y 8 HOH 320 1064 465  HOH HOH A . 
Y 8 HOH 321 1065 468  HOH HOH A . 
Y 8 HOH 322 1066 469  HOH HOH A . 
Y 8 HOH 323 1067 471  HOH HOH A . 
Y 8 HOH 324 1068 472  HOH HOH A . 
Y 8 HOH 325 1069 473  HOH HOH A . 
Y 8 HOH 326 1070 474  HOH HOH A . 
Y 8 HOH 327 1071 476  HOH HOH A . 
Y 8 HOH 328 1072 477  HOH HOH A . 
Y 8 HOH 329 1073 478  HOH HOH A . 
Y 8 HOH 330 1074 480  HOH HOH A . 
Y 8 HOH 331 1075 482  HOH HOH A . 
Y 8 HOH 332 1076 484  HOH HOH A . 
Y 8 HOH 333 1077 485  HOH HOH A . 
Y 8 HOH 334 1078 486  HOH HOH A . 
Y 8 HOH 335 1079 489  HOH HOH A . 
Y 8 HOH 336 1080 491  HOH HOH A . 
Y 8 HOH 337 1081 495  HOH HOH A . 
Y 8 HOH 338 1082 496  HOH HOH A . 
Y 8 HOH 339 1083 501  HOH HOH A . 
Y 8 HOH 340 1084 503  HOH HOH A . 
Y 8 HOH 341 1085 504  HOH HOH A . 
Y 8 HOH 342 1086 505  HOH HOH A . 
Y 8 HOH 343 1087 506  HOH HOH A . 
Y 8 HOH 344 1088 507  HOH HOH A . 
Y 8 HOH 345 1089 512  HOH HOH A . 
Y 8 HOH 346 1090 513  HOH HOH A . 
Y 8 HOH 347 1091 514  HOH HOH A . 
Y 8 HOH 348 1092 515  HOH HOH A . 
Y 8 HOH 349 1093 517  HOH HOH A . 
Y 8 HOH 350 1094 519  HOH HOH A . 
Y 8 HOH 351 1095 520  HOH HOH A . 
Y 8 HOH 352 1096 522  HOH HOH A . 
Y 8 HOH 353 1097 526  HOH HOH A . 
Y 8 HOH 354 1098 530  HOH HOH A . 
Y 8 HOH 355 1099 533  HOH HOH A . 
Y 8 HOH 356 1100 534  HOH HOH A . 
Y 8 HOH 357 1104 536  HOH HOH A . 
Y 8 HOH 358 1105 540  HOH HOH A . 
Y 8 HOH 359 1106 542  HOH HOH A . 
Y 8 HOH 360 1107 543  HOH HOH A . 
Y 8 HOH 361 1108 546  HOH HOH A . 
Y 8 HOH 362 1109 547  HOH HOH A . 
Y 8 HOH 363 1110 549  HOH HOH A . 
Y 8 HOH 364 1111 556  HOH HOH A . 
Y 8 HOH 365 1112 558  HOH HOH A . 
Y 8 HOH 366 1113 561  HOH HOH A . 
Y 8 HOH 367 1114 562  HOH HOH A . 
Y 8 HOH 368 1115 563  HOH HOH A . 
Y 8 HOH 369 1116 566  HOH HOH A . 
Y 8 HOH 370 1117 567  HOH HOH A . 
Y 8 HOH 371 1118 575  HOH HOH A . 
Y 8 HOH 372 1119 576  HOH HOH A . 
Y 8 HOH 373 1120 580  HOH HOH A . 
Y 8 HOH 374 1121 588  HOH HOH A . 
Y 8 HOH 375 1122 592  HOH HOH A . 
Y 8 HOH 376 1123 595  HOH HOH A . 
Y 8 HOH 377 1124 598  HOH HOH A . 
Y 8 HOH 378 1125 599  HOH HOH A . 
Y 8 HOH 379 1126 600  HOH HOH A . 
Y 8 HOH 380 1127 602  HOH HOH A . 
Y 8 HOH 381 1128 604  HOH HOH A . 
Y 8 HOH 382 1129 605  HOH HOH A . 
Y 8 HOH 383 1130 606  HOH HOH A . 
Y 8 HOH 384 1131 609  HOH HOH A . 
Y 8 HOH 385 1132 610  HOH HOH A . 
Y 8 HOH 386 1133 611  HOH HOH A . 
Y 8 HOH 387 1134 615  HOH HOH A . 
Y 8 HOH 388 1135 616  HOH HOH A . 
Y 8 HOH 389 1136 617  HOH HOH A . 
Y 8 HOH 390 1137 618  HOH HOH A . 
Y 8 HOH 391 1138 621  HOH HOH A . 
Y 8 HOH 392 1139 622  HOH HOH A . 
Y 8 HOH 393 1140 623  HOH HOH A . 
Y 8 HOH 394 1141 624  HOH HOH A . 
Y 8 HOH 395 1142 625  HOH HOH A . 
Y 8 HOH 396 1143 628  HOH HOH A . 
Y 8 HOH 397 1144 629  HOH HOH A . 
Y 8 HOH 398 1145 630  HOH HOH A . 
Y 8 HOH 399 1146 631  HOH HOH A . 
Y 8 HOH 400 1147 636  HOH HOH A . 
Y 8 HOH 401 1148 639  HOH HOH A . 
Y 8 HOH 402 1149 640  HOH HOH A . 
Y 8 HOH 403 1150 642  HOH HOH A . 
Y 8 HOH 404 1151 645  HOH HOH A . 
Y 8 HOH 405 1152 646  HOH HOH A . 
Y 8 HOH 406 1153 647  HOH HOH A . 
Y 8 HOH 407 1154 648  HOH HOH A . 
Y 8 HOH 408 1155 649  HOH HOH A . 
Y 8 HOH 409 1156 650  HOH HOH A . 
Y 8 HOH 410 1157 651  HOH HOH A . 
Y 8 HOH 411 1158 656  HOH HOH A . 
Y 8 HOH 412 1159 657  HOH HOH A . 
Y 8 HOH 413 1160 660  HOH HOH A . 
Y 8 HOH 414 1161 662  HOH HOH A . 
Y 8 HOH 415 1162 669  HOH HOH A . 
Y 8 HOH 416 1163 671  HOH HOH A . 
Y 8 HOH 417 1164 673  HOH HOH A . 
Y 8 HOH 418 1165 674  HOH HOH A . 
Y 8 HOH 419 1166 675  HOH HOH A . 
Y 8 HOH 420 1167 677  HOH HOH A . 
Y 8 HOH 421 1168 678  HOH HOH A . 
Y 8 HOH 422 1169 679  HOH HOH A . 
Y 8 HOH 423 1170 680  HOH HOH A . 
Y 8 HOH 424 1171 682  HOH HOH A . 
Y 8 HOH 425 1172 683  HOH HOH A . 
Y 8 HOH 426 1173 691  HOH HOH A . 
Y 8 HOH 427 1174 692  HOH HOH A . 
Y 8 HOH 428 1175 693  HOH HOH A . 
Y 8 HOH 429 1176 694  HOH HOH A . 
Y 8 HOH 430 1177 695  HOH HOH A . 
Y 8 HOH 431 1178 696  HOH HOH A . 
Y 8 HOH 432 1179 699  HOH HOH A . 
Y 8 HOH 433 1180 702  HOH HOH A . 
Y 8 HOH 434 1181 704  HOH HOH A . 
Y 8 HOH 435 1182 705  HOH HOH A . 
Y 8 HOH 436 1183 708  HOH HOH A . 
Y 8 HOH 437 1184 709  HOH HOH A . 
Y 8 HOH 438 1185 710  HOH HOH A . 
Y 8 HOH 439 1186 711  HOH HOH A . 
Y 8 HOH 440 1187 712  HOH HOH A . 
Y 8 HOH 441 1188 714  HOH HOH A . 
Y 8 HOH 442 1189 716  HOH HOH A . 
Y 8 HOH 443 1190 718  HOH HOH A . 
Y 8 HOH 444 1191 719  HOH HOH A . 
Y 8 HOH 445 1192 721  HOH HOH A . 
Y 8 HOH 446 1193 722  HOH HOH A . 
Y 8 HOH 447 1194 723  HOH HOH A . 
Y 8 HOH 448 1195 728  HOH HOH A . 
Y 8 HOH 449 1196 732  HOH HOH A . 
Y 8 HOH 450 1197 734  HOH HOH A . 
Y 8 HOH 451 1198 735  HOH HOH A . 
Y 8 HOH 452 1199 736  HOH HOH A . 
Y 8 HOH 453 1200 737  HOH HOH A . 
Y 8 HOH 454 1201 740  HOH HOH A . 
Y 8 HOH 455 1202 741  HOH HOH A . 
Y 8 HOH 456 1203 747  HOH HOH A . 
Y 8 HOH 457 1204 801  HOH HOH A . 
Y 8 HOH 458 1205 901  HOH HOH A . 
Y 8 HOH 459 1206 411  HOH HOH A . 
Y 8 HOH 460 1207 412  HOH HOH A . 
Z 8 HOH 1   1    1    HOH HOH B . 
Z 8 HOH 2   3    3    HOH HOH B . 
Z 8 HOH 3   4    4    HOH HOH B . 
Z 8 HOH 4   5    5    HOH HOH B . 
Z 8 HOH 5   10   10   HOH HOH B . 
Z 8 HOH 6   15   15   HOH HOH B . 
Z 8 HOH 7   17   17   HOH HOH B . 
Z 8 HOH 8   18   18   HOH HOH B . 
Z 8 HOH 9   752  752  HOH HOH B . 
Z 8 HOH 10  753  26   HOH HOH B . 
Z 8 HOH 11  754  29   HOH HOH B . 
Z 8 HOH 12  755  30   HOH HOH B . 
Z 8 HOH 13  756  33   HOH HOH B . 
Z 8 HOH 14  757  757  HOH HOH B . 
Z 8 HOH 15  758  35   HOH HOH B . 
Z 8 HOH 16  759  759  HOH HOH B . 
Z 8 HOH 17  760  760  HOH HOH B . 
Z 8 HOH 18  761  761  HOH HOH B . 
Z 8 HOH 19  762  37   HOH HOH B . 
Z 8 HOH 20  763  763  HOH HOH B . 
Z 8 HOH 21  764  38   HOH HOH B . 
Z 8 HOH 22  765  39   HOH HOH B . 
Z 8 HOH 23  766  766  HOH HOH B . 
Z 8 HOH 24  767  43   HOH HOH B . 
Z 8 HOH 25  768  768  HOH HOH B . 
Z 8 HOH 26  769  45   HOH HOH B . 
Z 8 HOH 27  770  47   HOH HOH B . 
Z 8 HOH 28  771  50   HOH HOH B . 
Z 8 HOH 29  772  772  HOH HOH B . 
Z 8 HOH 30  773  51   HOH HOH B . 
Z 8 HOH 31  774  54   HOH HOH B . 
Z 8 HOH 32  775  775  HOH HOH B . 
Z 8 HOH 33  776  55   HOH HOH B . 
Z 8 HOH 34  777  58   HOH HOH B . 
Z 8 HOH 35  778  778  HOH HOH B . 
Z 8 HOH 36  779  779  HOH HOH B . 
Z 8 HOH 37  780  780  HOH HOH B . 
Z 8 HOH 38  781  781  HOH HOH B . 
Z 8 HOH 39  782  782  HOH HOH B . 
Z 8 HOH 40  783  63   HOH HOH B . 
Z 8 HOH 41  784  69   HOH HOH B . 
Z 8 HOH 42  785  70   HOH HOH B . 
Z 8 HOH 43  786  71   HOH HOH B . 
Z 8 HOH 44  787  787  HOH HOH B . 
Z 8 HOH 45  788  75   HOH HOH B . 
Z 8 HOH 46  789  789  HOH HOH B . 
Z 8 HOH 47  790  790  HOH HOH B . 
Z 8 HOH 48  791  80   HOH HOH B . 
Z 8 HOH 49  792  792  HOH HOH B . 
Z 8 HOH 50  793  793  HOH HOH B . 
Z 8 HOH 51  794  81   HOH HOH B . 
Z 8 HOH 52  795  87   HOH HOH B . 
Z 8 HOH 53  796  88   HOH HOH B . 
Z 8 HOH 54  797  89   HOH HOH B . 
Z 8 HOH 55  798  92   HOH HOH B . 
Z 8 HOH 56  799  799  HOH HOH B . 
Z 8 HOH 57  800  93   HOH HOH B . 
Z 8 HOH 58  804  804  HOH HOH B . 
Z 8 HOH 59  805  805  HOH HOH B . 
Z 8 HOH 60  806  806  HOH HOH B . 
Z 8 HOH 61  807  807  HOH HOH B . 
Z 8 HOH 62  808  96   HOH HOH B . 
Z 8 HOH 63  809  809  HOH HOH B . 
Z 8 HOH 64  810  97   HOH HOH B . 
Z 8 HOH 65  811  811  HOH HOH B . 
Z 8 HOH 66  812  812  HOH HOH B . 
Z 8 HOH 67  813  813  HOH HOH B . 
Z 8 HOH 68  814  814  HOH HOH B . 
Z 8 HOH 69  815  815  HOH HOH B . 
Z 8 HOH 70  816  816  HOH HOH B . 
Z 8 HOH 71  817  817  HOH HOH B . 
Z 8 HOH 72  818  818  HOH HOH B . 
Z 8 HOH 73  819  819  HOH HOH B . 
Z 8 HOH 74  820  820  HOH HOH B . 
Z 8 HOH 75  821  821  HOH HOH B . 
Z 8 HOH 76  822  822  HOH HOH B . 
Z 8 HOH 77  823  103  HOH HOH B . 
Z 8 HOH 78  824  105  HOH HOH B . 
Z 8 HOH 79  825  106  HOH HOH B . 
Z 8 HOH 80  826  111  HOH HOH B . 
Z 8 HOH 81  827  827  HOH HOH B . 
Z 8 HOH 82  828  117  HOH HOH B . 
Z 8 HOH 83  829  118  HOH HOH B . 
Z 8 HOH 84  830  830  HOH HOH B . 
Z 8 HOH 85  831  119  HOH HOH B . 
Z 8 HOH 86  832  832  HOH HOH B . 
Z 8 HOH 87  833  121  HOH HOH B . 
Z 8 HOH 88  834  834  HOH HOH B . 
Z 8 HOH 89  835  124  HOH HOH B . 
Z 8 HOH 90  836  125  HOH HOH B . 
Z 8 HOH 91  837  126  HOH HOH B . 
Z 8 HOH 92  838  130  HOH HOH B . 
Z 8 HOH 93  839  131  HOH HOH B . 
Z 8 HOH 94  840  132  HOH HOH B . 
Z 8 HOH 95  841  841  HOH HOH B . 
Z 8 HOH 96  842  842  HOH HOH B . 
Z 8 HOH 97  843  843  HOH HOH B . 
Z 8 HOH 98  844  135  HOH HOH B . 
Z 8 HOH 99  845  845  HOH HOH B . 
Z 8 HOH 100 846  136  HOH HOH B . 
Z 8 HOH 101 847  137  HOH HOH B . 
Z 8 HOH 102 848  848  HOH HOH B . 
Z 8 HOH 103 849  849  HOH HOH B . 
Z 8 HOH 104 850  850  HOH HOH B . 
Z 8 HOH 105 851  139  HOH HOH B . 
Z 8 HOH 106 852  852  HOH HOH B . 
Z 8 HOH 107 853  853  HOH HOH B . 
Z 8 HOH 108 854  142  HOH HOH B . 
Z 8 HOH 109 855  855  HOH HOH B . 
Z 8 HOH 110 856  143  HOH HOH B . 
Z 8 HOH 111 857  144  HOH HOH B . 
Z 8 HOH 112 858  858  HOH HOH B . 
Z 8 HOH 113 859  145  HOH HOH B . 
Z 8 HOH 114 860  146  HOH HOH B . 
Z 8 HOH 115 861  147  HOH HOH B . 
Z 8 HOH 116 862  148  HOH HOH B . 
Z 8 HOH 117 863  149  HOH HOH B . 
Z 8 HOH 118 864  150  HOH HOH B . 
Z 8 HOH 119 865  153  HOH HOH B . 
Z 8 HOH 120 866  155  HOH HOH B . 
Z 8 HOH 121 867  157  HOH HOH B . 
Z 8 HOH 122 868  158  HOH HOH B . 
Z 8 HOH 123 869  159  HOH HOH B . 
Z 8 HOH 124 870  160  HOH HOH B . 
Z 8 HOH 125 871  161  HOH HOH B . 
Z 8 HOH 126 872  872  HOH HOH B . 
Z 8 HOH 127 873  162  HOH HOH B . 
Z 8 HOH 128 874  166  HOH HOH B . 
Z 8 HOH 129 875  875  HOH HOH B . 
Z 8 HOH 130 876  167  HOH HOH B . 
Z 8 HOH 131 877  169  HOH HOH B . 
Z 8 HOH 132 878  878  HOH HOH B . 
Z 8 HOH 133 879  879  HOH HOH B . 
Z 8 HOH 134 880  880  HOH HOH B . 
Z 8 HOH 135 881  170  HOH HOH B . 
Z 8 HOH 136 882  882  HOH HOH B . 
Z 8 HOH 137 883  883  HOH HOH B . 
Z 8 HOH 138 884  171  HOH HOH B . 
Z 8 HOH 139 885  172  HOH HOH B . 
Z 8 HOH 140 886  886  HOH HOH B . 
Z 8 HOH 141 887  887  HOH HOH B . 
Z 8 HOH 142 888  888  HOH HOH B . 
Z 8 HOH 143 889  889  HOH HOH B . 
Z 8 HOH 144 890  173  HOH HOH B . 
Z 8 HOH 145 891  891  HOH HOH B . 
Z 8 HOH 146 892  892  HOH HOH B . 
Z 8 HOH 147 893  893  HOH HOH B . 
Z 8 HOH 148 894  894  HOH HOH B . 
Z 8 HOH 149 895  174  HOH HOH B . 
Z 8 HOH 150 896  175  HOH HOH B . 
Z 8 HOH 151 897  897  HOH HOH B . 
Z 8 HOH 152 898  898  HOH HOH B . 
Z 8 HOH 153 899  899  HOH HOH B . 
Z 8 HOH 154 900  900  HOH HOH B . 
Z 8 HOH 155 902  902  HOH HOH B . 
Z 8 HOH 156 903  177  HOH HOH B . 
Z 8 HOH 157 904  904  HOH HOH B . 
Z 8 HOH 158 905  181  HOH HOH B . 
Z 8 HOH 159 906  183  HOH HOH B . 
Z 8 HOH 160 907  907  HOH HOH B . 
Z 8 HOH 161 908  908  HOH HOH B . 
Z 8 HOH 162 909  909  HOH HOH B . 
Z 8 HOH 163 910  910  HOH HOH B . 
Z 8 HOH 164 911  911  HOH HOH B . 
Z 8 HOH 165 912  912  HOH HOH B . 
Z 8 HOH 166 913  913  HOH HOH B . 
Z 8 HOH 167 914  184  HOH HOH B . 
Z 8 HOH 168 915  186  HOH HOH B . 
Z 8 HOH 169 916  188  HOH HOH B . 
Z 8 HOH 170 917  189  HOH HOH B . 
Z 8 HOH 171 918  918  HOH HOH B . 
Z 8 HOH 172 919  194  HOH HOH B . 
Z 8 HOH 173 920  196  HOH HOH B . 
Z 8 HOH 174 921  921  HOH HOH B . 
Z 8 HOH 175 922  922  HOH HOH B . 
Z 8 HOH 176 923  197  HOH HOH B . 
Z 8 HOH 177 924  198  HOH HOH B . 
Z 8 HOH 178 925  199  HOH HOH B . 
Z 8 HOH 179 926  200  HOH HOH B . 
Z 8 HOH 180 927  927  HOH HOH B . 
Z 8 HOH 181 928  928  HOH HOH B . 
Z 8 HOH 182 929  929  HOH HOH B . 
Z 8 HOH 183 930  930  HOH HOH B . 
Z 8 HOH 184 931  931  HOH HOH B . 
Z 8 HOH 185 932  932  HOH HOH B . 
Z 8 HOH 186 933  201  HOH HOH B . 
Z 8 HOH 187 934  203  HOH HOH B . 
Z 8 HOH 188 935  204  HOH HOH B . 
Z 8 HOH 189 936  208  HOH HOH B . 
Z 8 HOH 190 937  210  HOH HOH B . 
Z 8 HOH 191 938  211  HOH HOH B . 
Z 8 HOH 192 939  217  HOH HOH B . 
Z 8 HOH 193 940  218  HOH HOH B . 
Z 8 HOH 194 941  220  HOH HOH B . 
Z 8 HOH 195 942  222  HOH HOH B . 
Z 8 HOH 196 943  229  HOH HOH B . 
Z 8 HOH 197 944  231  HOH HOH B . 
Z 8 HOH 198 945  233  HOH HOH B . 
Z 8 HOH 199 946  236  HOH HOH B . 
Z 8 HOH 200 947  237  HOH HOH B . 
Z 8 HOH 201 948  238  HOH HOH B . 
Z 8 HOH 202 949  239  HOH HOH B . 
Z 8 HOH 203 950  240  HOH HOH B . 
Z 8 HOH 204 951  241  HOH HOH B . 
Z 8 HOH 205 952  243  HOH HOH B . 
Z 8 HOH 206 953  244  HOH HOH B . 
Z 8 HOH 207 954  247  HOH HOH B . 
Z 8 HOH 208 955  250  HOH HOH B . 
Z 8 HOH 209 956  253  HOH HOH B . 
Z 8 HOH 210 957  259  HOH HOH B . 
Z 8 HOH 211 958  260  HOH HOH B . 
Z 8 HOH 212 959  261  HOH HOH B . 
Z 8 HOH 213 960  263  HOH HOH B . 
Z 8 HOH 214 961  264  HOH HOH B . 
Z 8 HOH 215 962  265  HOH HOH B . 
Z 8 HOH 216 963  266  HOH HOH B . 
Z 8 HOH 217 964  269  HOH HOH B . 
Z 8 HOH 218 965  272  HOH HOH B . 
Z 8 HOH 219 966  274  HOH HOH B . 
Z 8 HOH 220 967  278  HOH HOH B . 
Z 8 HOH 221 968  280  HOH HOH B . 
Z 8 HOH 222 969  283  HOH HOH B . 
Z 8 HOH 223 970  286  HOH HOH B . 
Z 8 HOH 224 971  287  HOH HOH B . 
Z 8 HOH 225 972  288  HOH HOH B . 
Z 8 HOH 226 973  291  HOH HOH B . 
Z 8 HOH 227 974  294  HOH HOH B . 
Z 8 HOH 228 975  295  HOH HOH B . 
Z 8 HOH 229 976  297  HOH HOH B . 
Z 8 HOH 230 977  298  HOH HOH B . 
Z 8 HOH 231 978  299  HOH HOH B . 
Z 8 HOH 232 979  301  HOH HOH B . 
Z 8 HOH 233 980  302  HOH HOH B . 
Z 8 HOH 234 981  303  HOH HOH B . 
Z 8 HOH 235 982  304  HOH HOH B . 
Z 8 HOH 236 983  309  HOH HOH B . 
Z 8 HOH 237 984  311  HOH HOH B . 
Z 8 HOH 238 985  312  HOH HOH B . 
Z 8 HOH 239 986  313  HOH HOH B . 
Z 8 HOH 240 987  314  HOH HOH B . 
Z 8 HOH 241 988  316  HOH HOH B . 
Z 8 HOH 242 989  334  HOH HOH B . 
Z 8 HOH 243 990  336  HOH HOH B . 
Z 8 HOH 244 991  337  HOH HOH B . 
Z 8 HOH 245 992  339  HOH HOH B . 
Z 8 HOH 246 993  341  HOH HOH B . 
Z 8 HOH 247 994  342  HOH HOH B . 
Z 8 HOH 248 995  343  HOH HOH B . 
Z 8 HOH 249 996  345  HOH HOH B . 
Z 8 HOH 250 997  346  HOH HOH B . 
Z 8 HOH 251 998  349  HOH HOH B . 
Z 8 HOH 252 999  351  HOH HOH B . 
Z 8 HOH 253 1000 355  HOH HOH B . 
Z 8 HOH 254 1001 356  HOH HOH B . 
Z 8 HOH 255 1002 360  HOH HOH B . 
Z 8 HOH 256 1003 362  HOH HOH B . 
Z 8 HOH 257 1004 364  HOH HOH B . 
Z 8 HOH 258 1005 367  HOH HOH B . 
Z 8 HOH 259 1006 368  HOH HOH B . 
Z 8 HOH 260 1007 370  HOH HOH B . 
Z 8 HOH 261 1008 373  HOH HOH B . 
Z 8 HOH 262 1009 377  HOH HOH B . 
Z 8 HOH 263 1010 379  HOH HOH B . 
Z 8 HOH 264 1011 382  HOH HOH B . 
Z 8 HOH 265 1012 384  HOH HOH B . 
Z 8 HOH 266 1013 386  HOH HOH B . 
Z 8 HOH 267 1014 388  HOH HOH B . 
Z 8 HOH 268 1015 389  HOH HOH B . 
Z 8 HOH 269 1016 390  HOH HOH B . 
Z 8 HOH 270 1017 392  HOH HOH B . 
Z 8 HOH 271 1018 395  HOH HOH B . 
Z 8 HOH 272 1019 397  HOH HOH B . 
Z 8 HOH 273 1020 401  HOH HOH B . 
Z 8 HOH 274 1021 402  HOH HOH B . 
Z 8 HOH 275 1022 404  HOH HOH B . 
Z 8 HOH 276 1023 407  HOH HOH B . 
Z 8 HOH 277 1024 409  HOH HOH B . 
Z 8 HOH 278 1027 414  HOH HOH B . 
Z 8 HOH 279 1028 417  HOH HOH B . 
Z 8 HOH 280 1029 418  HOH HOH B . 
Z 8 HOH 281 1030 419  HOH HOH B . 
Z 8 HOH 282 1031 420  HOH HOH B . 
Z 8 HOH 283 1032 421  HOH HOH B . 
Z 8 HOH 284 1033 422  HOH HOH B . 
Z 8 HOH 285 1034 427  HOH HOH B . 
Z 8 HOH 286 1035 428  HOH HOH B . 
Z 8 HOH 287 1036 429  HOH HOH B . 
Z 8 HOH 288 1037 430  HOH HOH B . 
Z 8 HOH 289 1038 431  HOH HOH B . 
Z 8 HOH 290 1039 432  HOH HOH B . 
Z 8 HOH 291 1040 434  HOH HOH B . 
Z 8 HOH 292 1041 435  HOH HOH B . 
Z 8 HOH 293 1042 437  HOH HOH B . 
Z 8 HOH 294 1043 438  HOH HOH B . 
Z 8 HOH 295 1044 439  HOH HOH B . 
Z 8 HOH 296 1045 440  HOH HOH B . 
Z 8 HOH 297 1046 442  HOH HOH B . 
Z 8 HOH 298 1047 443  HOH HOH B . 
Z 8 HOH 299 1048 444  HOH HOH B . 
Z 8 HOH 300 1049 445  HOH HOH B . 
Z 8 HOH 301 1050 447  HOH HOH B . 
Z 8 HOH 302 1051 449  HOH HOH B . 
Z 8 HOH 303 1052 450  HOH HOH B . 
Z 8 HOH 304 1053 453  HOH HOH B . 
Z 8 HOH 305 1054 454  HOH HOH B . 
Z 8 HOH 306 1055 457  HOH HOH B . 
Z 8 HOH 307 1056 458  HOH HOH B . 
Z 8 HOH 308 1057 461  HOH HOH B . 
Z 8 HOH 309 1058 462  HOH HOH B . 
Z 8 HOH 310 1059 464  HOH HOH B . 
Z 8 HOH 311 1060 466  HOH HOH B . 
Z 8 HOH 312 1061 467  HOH HOH B . 
Z 8 HOH 313 1062 470  HOH HOH B . 
Z 8 HOH 314 1063 475  HOH HOH B . 
Z 8 HOH 315 1064 479  HOH HOH B . 
Z 8 HOH 316 1065 481  HOH HOH B . 
Z 8 HOH 317 1066 483  HOH HOH B . 
Z 8 HOH 318 1067 487  HOH HOH B . 
Z 8 HOH 319 1068 488  HOH HOH B . 
Z 8 HOH 320 1069 490  HOH HOH B . 
Z 8 HOH 321 1070 492  HOH HOH B . 
Z 8 HOH 322 1071 493  HOH HOH B . 
Z 8 HOH 323 1072 494  HOH HOH B . 
Z 8 HOH 324 1073 497  HOH HOH B . 
Z 8 HOH 325 1074 498  HOH HOH B . 
Z 8 HOH 326 1075 499  HOH HOH B . 
Z 8 HOH 327 1076 500  HOH HOH B . 
Z 8 HOH 328 1077 502  HOH HOH B . 
Z 8 HOH 329 1078 508  HOH HOH B . 
Z 8 HOH 330 1079 509  HOH HOH B . 
Z 8 HOH 331 1080 510  HOH HOH B . 
Z 8 HOH 332 1081 511  HOH HOH B . 
Z 8 HOH 333 1082 516  HOH HOH B . 
Z 8 HOH 334 1083 518  HOH HOH B . 
Z 8 HOH 335 1084 521  HOH HOH B . 
Z 8 HOH 336 1085 523  HOH HOH B . 
Z 8 HOH 337 1086 524  HOH HOH B . 
Z 8 HOH 338 1087 525  HOH HOH B . 
Z 8 HOH 339 1088 527  HOH HOH B . 
Z 8 HOH 340 1089 528  HOH HOH B . 
Z 8 HOH 341 1090 529  HOH HOH B . 
Z 8 HOH 342 1091 531  HOH HOH B . 
Z 8 HOH 343 1092 532  HOH HOH B . 
Z 8 HOH 344 1093 535  HOH HOH B . 
Z 8 HOH 345 1094 537  HOH HOH B . 
Z 8 HOH 346 1095 538  HOH HOH B . 
Z 8 HOH 347 1096 539  HOH HOH B . 
Z 8 HOH 348 1097 541  HOH HOH B . 
Z 8 HOH 349 1098 545  HOH HOH B . 
Z 8 HOH 350 1099 548  HOH HOH B . 
Z 8 HOH 351 1100 550  HOH HOH B . 
Z 8 HOH 352 1103 551  HOH HOH B . 
Z 8 HOH 353 1104 552  HOH HOH B . 
Z 8 HOH 354 1105 553  HOH HOH B . 
Z 8 HOH 355 1106 555  HOH HOH B . 
Z 8 HOH 356 1107 557  HOH HOH B . 
Z 8 HOH 357 1108 559  HOH HOH B . 
Z 8 HOH 358 1109 560  HOH HOH B . 
Z 8 HOH 359 1110 564  HOH HOH B . 
Z 8 HOH 360 1111 565  HOH HOH B . 
Z 8 HOH 361 1112 568  HOH HOH B . 
Z 8 HOH 362 1113 569  HOH HOH B . 
Z 8 HOH 363 1114 570  HOH HOH B . 
Z 8 HOH 364 1115 571  HOH HOH B . 
Z 8 HOH 365 1116 572  HOH HOH B . 
Z 8 HOH 366 1117 573  HOH HOH B . 
Z 8 HOH 367 1118 574  HOH HOH B . 
Z 8 HOH 368 1119 577  HOH HOH B . 
Z 8 HOH 369 1120 578  HOH HOH B . 
Z 8 HOH 370 1121 579  HOH HOH B . 
Z 8 HOH 371 1122 581  HOH HOH B . 
Z 8 HOH 372 1123 582  HOH HOH B . 
Z 8 HOH 373 1124 583  HOH HOH B . 
Z 8 HOH 374 1125 584  HOH HOH B . 
Z 8 HOH 375 1126 585  HOH HOH B . 
Z 8 HOH 376 1127 586  HOH HOH B . 
Z 8 HOH 377 1128 589  HOH HOH B . 
Z 8 HOH 378 1129 590  HOH HOH B . 
Z 8 HOH 379 1130 591  HOH HOH B . 
Z 8 HOH 380 1131 593  HOH HOH B . 
Z 8 HOH 381 1132 594  HOH HOH B . 
Z 8 HOH 382 1133 596  HOH HOH B . 
Z 8 HOH 383 1134 597  HOH HOH B . 
Z 8 HOH 384 1135 601  HOH HOH B . 
Z 8 HOH 385 1136 603  HOH HOH B . 
Z 8 HOH 386 1137 607  HOH HOH B . 
Z 8 HOH 387 1138 608  HOH HOH B . 
Z 8 HOH 388 1139 612  HOH HOH B . 
Z 8 HOH 389 1140 613  HOH HOH B . 
Z 8 HOH 390 1141 614  HOH HOH B . 
Z 8 HOH 391 1142 619  HOH HOH B . 
Z 8 HOH 392 1143 620  HOH HOH B . 
Z 8 HOH 393 1144 626  HOH HOH B . 
Z 8 HOH 394 1145 627  HOH HOH B . 
Z 8 HOH 395 1146 632  HOH HOH B . 
Z 8 HOH 396 1147 633  HOH HOH B . 
Z 8 HOH 397 1148 634  HOH HOH B . 
Z 8 HOH 398 1149 635  HOH HOH B . 
Z 8 HOH 399 1150 637  HOH HOH B . 
Z 8 HOH 400 1151 638  HOH HOH B . 
Z 8 HOH 401 1152 641  HOH HOH B . 
Z 8 HOH 402 1153 643  HOH HOH B . 
Z 8 HOH 403 1154 644  HOH HOH B . 
Z 8 HOH 404 1155 652  HOH HOH B . 
Z 8 HOH 405 1156 653  HOH HOH B . 
Z 8 HOH 406 1157 654  HOH HOH B . 
Z 8 HOH 407 1158 655  HOH HOH B . 
Z 8 HOH 408 1159 658  HOH HOH B . 
Z 8 HOH 409 1160 659  HOH HOH B . 
Z 8 HOH 410 1161 663  HOH HOH B . 
Z 8 HOH 411 1162 664  HOH HOH B . 
Z 8 HOH 412 1163 665  HOH HOH B . 
Z 8 HOH 413 1164 666  HOH HOH B . 
Z 8 HOH 414 1165 667  HOH HOH B . 
Z 8 HOH 415 1166 668  HOH HOH B . 
Z 8 HOH 416 1167 670  HOH HOH B . 
Z 8 HOH 417 1168 676  HOH HOH B . 
Z 8 HOH 418 1169 681  HOH HOH B . 
Z 8 HOH 419 1170 684  HOH HOH B . 
Z 8 HOH 420 1171 685  HOH HOH B . 
Z 8 HOH 421 1172 686  HOH HOH B . 
Z 8 HOH 422 1173 687  HOH HOH B . 
Z 8 HOH 423 1174 688  HOH HOH B . 
Z 8 HOH 424 1175 689  HOH HOH B . 
Z 8 HOH 425 1176 690  HOH HOH B . 
Z 8 HOH 426 1177 697  HOH HOH B . 
Z 8 HOH 427 1178 698  HOH HOH B . 
Z 8 HOH 428 1179 700  HOH HOH B . 
Z 8 HOH 429 1180 701  HOH HOH B . 
Z 8 HOH 430 1181 703  HOH HOH B . 
Z 8 HOH 431 1182 706  HOH HOH B . 
Z 8 HOH 432 1183 707  HOH HOH B . 
Z 8 HOH 433 1184 713  HOH HOH B . 
Z 8 HOH 434 1185 715  HOH HOH B . 
Z 8 HOH 435 1186 717  HOH HOH B . 
Z 8 HOH 436 1187 720  HOH HOH B . 
Z 8 HOH 437 1188 724  HOH HOH B . 
Z 8 HOH 438 1189 725  HOH HOH B . 
Z 8 HOH 439 1190 726  HOH HOH B . 
Z 8 HOH 440 1191 727  HOH HOH B . 
Z 8 HOH 441 1192 729  HOH HOH B . 
Z 8 HOH 442 1193 731  HOH HOH B . 
Z 8 HOH 443 1194 733  HOH HOH B . 
Z 8 HOH 444 1195 738  HOH HOH B . 
Z 8 HOH 445 1196 739  HOH HOH B . 
Z 8 HOH 446 1197 742  HOH HOH B . 
Z 8 HOH 447 1198 743  HOH HOH B . 
Z 8 HOH 448 1199 744  HOH HOH B . 
Z 8 HOH 449 1200 745  HOH HOH B . 
Z 8 HOH 450 1201 746  HOH HOH B . 
Z 8 HOH 451 1202 748  HOH HOH B . 
Z 8 HOH 452 1203 749  HOH HOH B . 
Z 8 HOH 453 1204 750  HOH HOH B . 
Z 8 HOH 454 1205 751  HOH HOH B . 
Z 8 HOH 455 1206 802  HOH HOH B . 
Z 8 HOH 456 1207 803  HOH HOH B . 
# 
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 90  A ASN 110 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 518 A ASN 538 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 725 A ASN 745 ? ASN 'GLYCOSYLATION SITE' 
4 B ASN 90  B ASN 110 ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 518 B ASN 538 ? ASN 'GLYCOSYLATION SITE' 
6 B ASN 725 B ASN 745 ? ASN 'GLYCOSYLATION SITE' 
7 A TPQ 441 A TPQ 461 ? TYR ?                    
8 B TPQ 441 B TPQ 461 ? TYR ?                    
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 22780 ? 
1 MORE         -92   ? 
1 'SSA (A^2)'  46890 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O4  ? A TPQ 441 ? A TPQ 461 ? 1_555 CU ? C CU . ? A CU 801 ? 1_555 NE2 ? A HIS 490 ? A HIS 510 ? 1_555 89.8  ? 
2  O4  ? A TPQ 441 ? A TPQ 461 ? 1_555 CU ? C CU . ? A CU 801 ? 1_555 NE2 ? A HIS 492 ? A HIS 512 ? 1_555 113.0 ? 
3  NE2 ? A HIS 490 ? A HIS 510 ? 1_555 CU ? C CU . ? A CU 801 ? 1_555 NE2 ? A HIS 492 ? A HIS 512 ? 1_555 97.9  ? 
4  O4  ? A TPQ 441 ? A TPQ 461 ? 1_555 CU ? C CU . ? A CU 801 ? 1_555 ND1 ? A HIS 655 ? A HIS 675 ? 1_555 103.5 ? 
5  NE2 ? A HIS 490 ? A HIS 510 ? 1_555 CU ? C CU . ? A CU 801 ? 1_555 ND1 ? A HIS 655 ? A HIS 675 ? 1_555 97.4  ? 
6  NE2 ? A HIS 492 ? A HIS 512 ? 1_555 CU ? C CU . ? A CU 801 ? 1_555 ND1 ? A HIS 655 ? A HIS 675 ? 1_555 140.3 ? 
7  OD1 ? A ASP 499 ? A ASP 519 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? A LEU 500 ? A LEU 520 ? 1_555 102.3 ? 
8  OD1 ? A ASP 499 ? A ASP 519 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 501 ? A ASP 521 ? 1_555 87.3  ? 
9  O   ? A LEU 500 ? A LEU 520 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 501 ? A ASP 521 ? 1_555 77.9  ? 
10 OD1 ? A ASP 499 ? A ASP 519 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 644 ? A ASP 664 ? 1_555 97.0  ? 
11 O   ? A LEU 500 ? A LEU 520 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 644 ? A ASP 664 ? 1_555 157.4 ? 
12 OD1 ? A ASP 501 ? A ASP 521 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 OD1 ? A ASP 644 ? A ASP 664 ? 1_555 91.4  ? 
13 OD1 ? A ASP 499 ? A ASP 519 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? A LEU 645 ? A LEU 665 ? 1_555 85.6  ? 
14 O   ? A LEU 500 ? A LEU 520 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? A LEU 645 ? A LEU 665 ? 1_555 91.6  ? 
15 OD1 ? A ASP 501 ? A ASP 521 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? A LEU 645 ? A LEU 665 ? 1_555 165.7 ? 
16 OD1 ? A ASP 644 ? A ASP 664 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? A LEU 645 ? A LEU 665 ? 1_555 101.8 ? 
17 OD1 ? A ASP 499 ? A ASP 519 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? Y HOH .   ? A HOH 20  ? 1_555 174.0 ? 
18 O   ? A LEU 500 ? A LEU 520 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? Y HOH .   ? A HOH 20  ? 1_555 71.8  ? 
19 OD1 ? A ASP 501 ? A ASP 521 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? Y HOH .   ? A HOH 20  ? 1_555 90.9  ? 
20 OD1 ? A ASP 644 ? A ASP 664 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? Y HOH .   ? A HOH 20  ? 1_555 88.8  ? 
21 O   ? A LEU 645 ? A LEU 665 ? 1_555 CA ? D CA . ? A CA 802 ? 1_555 O   ? Y HOH .   ? A HOH 20  ? 1_555 94.9  ? 
22 OE1 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OE2 ? A GLU 542 ? A GLU 562 ? 1_555 51.3  ? 
23 OE1 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? A PHE 633 ? A PHE 653 ? 1_555 90.2  ? 
24 OE2 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? A PHE 633 ? A PHE 653 ? 1_555 98.4  ? 
25 OE1 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OD1 ? A ASN 636 ? A ASN 656 ? 1_555 81.9  ? 
26 OE2 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OD1 ? A ASN 636 ? A ASN 656 ? 1_555 131.5 ? 
27 O   ? A PHE 633 ? A PHE 653 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OD1 ? A ASN 636 ? A ASN 656 ? 1_555 92.9  ? 
28 OE1 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OE1 ? A GLU 638 ? A GLU 658 ? 1_555 99.5  ? 
29 OE2 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OE1 ? A GLU 638 ? A GLU 658 ? 1_555 92.0  ? 
30 O   ? A PHE 633 ? A PHE 653 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OE1 ? A GLU 638 ? A GLU 658 ? 1_555 168.8 ? 
31 OD1 ? A ASN 636 ? A ASN 656 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 OE1 ? A GLU 638 ? A GLU 658 ? 1_555 83.1  ? 
32 OE1 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 758 ? 1_555 126.8 ? 
33 OE2 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 758 ? 1_555 75.5  ? 
34 O   ? A PHE 633 ? A PHE 653 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 758 ? 1_555 98.2  ? 
35 OD1 ? A ASN 636 ? A ASN 656 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 758 ? 1_555 148.8 ? 
36 OE1 ? A GLU 638 ? A GLU 658 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 758 ? 1_555 80.4  ? 
37 OE1 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 817 ? 1_555 155.8 ? 
38 OE2 ? A GLU 542 ? A GLU 562 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 817 ? 1_555 151.8 ? 
39 O   ? A PHE 633 ? A PHE 653 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 817 ? 1_555 80.1  ? 
40 OD1 ? A ASN 636 ? A ASN 656 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 817 ? 1_555 76.6  ? 
41 OE1 ? A GLU 638 ? A GLU 658 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 817 ? 1_555 88.8  ? 
42 O   ? Y HOH .   ? A HOH 758 ? 1_555 CA ? E CA . ? A CA 803 ? 1_555 O   ? Y HOH .   ? A HOH 817 ? 1_555 76.8  ? 
43 O4  ? B TPQ 441 ? B TPQ 461 ? 1_555 CU ? O CU . ? B CU 801 ? 1_555 NE2 ? B HIS 490 ? B HIS 510 ? 1_555 89.5  ? 
44 O4  ? B TPQ 441 ? B TPQ 461 ? 1_555 CU ? O CU . ? B CU 801 ? 1_555 NE2 ? B HIS 492 ? B HIS 512 ? 1_555 111.6 ? 
45 NE2 ? B HIS 490 ? B HIS 510 ? 1_555 CU ? O CU . ? B CU 801 ? 1_555 NE2 ? B HIS 492 ? B HIS 512 ? 1_555 96.9  ? 
46 O4  ? B TPQ 441 ? B TPQ 461 ? 1_555 CU ? O CU . ? B CU 801 ? 1_555 ND1 ? B HIS 655 ? B HIS 675 ? 1_555 103.6 ? 
47 NE2 ? B HIS 490 ? B HIS 510 ? 1_555 CU ? O CU . ? B CU 801 ? 1_555 ND1 ? B HIS 655 ? B HIS 675 ? 1_555 95.7  ? 
48 NE2 ? B HIS 492 ? B HIS 512 ? 1_555 CU ? O CU . ? B CU 801 ? 1_555 ND1 ? B HIS 655 ? B HIS 675 ? 1_555 142.6 ? 
49 OD1 ? B ASP 499 ? B ASP 519 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? B LEU 500 ? B LEU 520 ? 1_555 101.0 ? 
50 OD1 ? B ASP 499 ? B ASP 519 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 OD1 ? B ASP 501 ? B ASP 521 ? 1_555 89.0  ? 
51 O   ? B LEU 500 ? B LEU 520 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 OD1 ? B ASP 501 ? B ASP 521 ? 1_555 76.7  ? 
52 OD1 ? B ASP 499 ? B ASP 519 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 OD1 ? B ASP 644 ? B ASP 664 ? 1_555 100.4 ? 
53 O   ? B LEU 500 ? B LEU 520 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 OD1 ? B ASP 644 ? B ASP 664 ? 1_555 154.0 ? 
54 OD1 ? B ASP 501 ? B ASP 521 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 OD1 ? B ASP 644 ? B ASP 664 ? 1_555 89.1  ? 
55 OD1 ? B ASP 499 ? B ASP 519 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? B LEU 645 ? B LEU 665 ? 1_555 87.7  ? 
56 O   ? B LEU 500 ? B LEU 520 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? B LEU 645 ? B LEU 665 ? 1_555 94.1  ? 
57 OD1 ? B ASP 501 ? B ASP 521 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? B LEU 645 ? B LEU 665 ? 1_555 169.5 ? 
58 OD1 ? B ASP 644 ? B ASP 664 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? B LEU 645 ? B LEU 665 ? 1_555 101.3 ? 
59 OD1 ? B ASP 499 ? B ASP 519 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? Z HOH .   ? B HOH 876 ? 1_555 174.6 ? 
60 O   ? B LEU 500 ? B LEU 520 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? Z HOH .   ? B HOH 876 ? 1_555 74.1  ? 
61 OD1 ? B ASP 501 ? B ASP 521 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? Z HOH .   ? B HOH 876 ? 1_555 87.6  ? 
62 OD1 ? B ASP 644 ? B ASP 664 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? Z HOH .   ? B HOH 876 ? 1_555 83.8  ? 
63 O   ? B LEU 645 ? B LEU 665 ? 1_555 CA ? P CA . ? B CA 802 ? 1_555 O   ? Z HOH .   ? B HOH 876 ? 1_555 94.9  ? 
64 OE1 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OE2 ? B GLU 542 ? B GLU 562 ? 1_555 48.9  ? 
65 OE1 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? B PHE 633 ? B PHE 653 ? 1_555 92.5  ? 
66 OE2 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? B PHE 633 ? B PHE 653 ? 1_555 104.9 ? 
67 OE1 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OD1 ? B ASN 636 ? B ASN 656 ? 1_555 82.0  ? 
68 OE2 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OD1 ? B ASN 636 ? B ASN 656 ? 1_555 129.2 ? 
69 O   ? B PHE 633 ? B PHE 653 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OD1 ? B ASN 636 ? B ASN 656 ? 1_555 86.9  ? 
70 OE1 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OE1 ? B GLU 638 ? B GLU 658 ? 1_555 95.7  ? 
71 OE2 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OE1 ? B GLU 638 ? B GLU 658 ? 1_555 80.0  ? 
72 O   ? B PHE 633 ? B PHE 653 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OE1 ? B GLU 638 ? B GLU 658 ? 1_555 171.7 ? 
73 OD1 ? B ASN 636 ? B ASN 656 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 OE1 ? B GLU 638 ? B GLU 658 ? 1_555 95.2  ? 
74 OE1 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 5   ? 1_555 153.0 ? 
75 OE2 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 5   ? 1_555 157.0 ? 
76 O   ? B PHE 633 ? B PHE 653 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 5   ? 1_555 74.8  ? 
77 OD1 ? B ASN 636 ? B ASN 656 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 5   ? 1_555 73.8  ? 
78 OE1 ? B GLU 638 ? B GLU 658 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 5   ? 1_555 98.1  ? 
79 OE1 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 834 ? 1_555 121.7 ? 
80 OE2 ? B GLU 542 ? B GLU 562 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 834 ? 1_555 73.1  ? 
81 O   ? B PHE 633 ? B PHE 653 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 834 ? 1_555 98.7  ? 
82 OD1 ? B ASN 636 ? B ASN 656 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 834 ? 1_555 155.0 ? 
83 OE1 ? B GLU 638 ? B GLU 658 ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 834 ? 1_555 76.1  ? 
84 O   ? Z HOH .   ? B HOH 5   ? 1_555 CA ? Q CA . ? B CA 803 ? 1_555 O   ? Z HOH .   ? B HOH 834 ? 1_555 84.2  ? 
# 
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 2009-10-20 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-01 
# 
_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' 'Derived calculations'      
2 2 'Structure model' 'Non-polymer description'   
3 2 'Structure model' 'Version format compliance' 
4 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.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 DENZO       .        ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com      'data reduction'  
http://www.hkl-xray.com/                     ?          ? 
2 SCALEPACK   .        ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com      'data scaling'    
http://www.hkl-xray.com/                     ?          ? 
3 REFMAC      .        ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 
4 PDB_EXTRACT 3.005    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 
5 Blu-Ice     .        ?               ?       ?                    ?                     'data collection' ? ?          ? 
6 HKL-2000    .        ?               ?       ?                    ?                     'data reduction'  ? ?          ? 
7 HKL-2000    .        ?               ?       ?                    ?                     'data scaling'    ? ?          ? 
8 REFMAC      5.5.0063 ?               ?       ?                    ?                     phasing           ? ?          ? 
# 
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 HIS A 178 ? ? -133.92 -65.44  
2  1 ARG A 190 ? ? -119.42 73.14   
3  1 TYR A 459 ? ? -161.48 -88.29  
4  1 VAL A 604 ? ? -102.38 -64.32  
5  1 GLN A 610 ? ? 47.85   -110.07 
6  1 ASN A 690 ? ? -112.63 50.10   
7  1 THR B 62  ? ? -91.58  59.12   
8  1 SER B 129 ? ? 37.84   65.10   
9  1 HIS B 178 ? ? 56.30   -99.01  
10 1 TYR B 319 ? ? -160.01 107.91  
11 1 TYR B 459 ? ? -161.77 -85.85  
12 1 VAL B 604 ? ? -102.57 -65.94  
13 1 GLN B 610 ? ? 48.30   -109.92 
14 1 ASN B 657 ? ? 39.63   63.37   
15 1 ASN B 690 ? ? -110.76 54.21   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ARG 28  ? CG  ? A ARG 8   CG  
2   1 Y 1 A ARG 28  ? CD  ? A ARG 8   CD  
3   1 Y 1 A ARG 28  ? NE  ? A ARG 8   NE  
4   1 Y 1 A ARG 28  ? CZ  ? A ARG 8   CZ  
5   1 Y 1 A ARG 28  ? NH1 ? A ARG 8   NH1 
6   1 Y 1 A ARG 28  ? NH2 ? A ARG 8   NH2 
7   1 Y 1 A GLN 39  ? CG  ? A GLN 19  CG  
8   1 Y 1 A GLN 39  ? CD  ? A GLN 19  CD  
9   1 Y 1 A GLN 39  ? OE1 ? A GLN 19  OE1 
10  1 Y 1 A GLN 39  ? NE2 ? A GLN 19  NE2 
11  1 Y 1 A LYS 52  ? CE  ? A LYS 32  CE  
12  1 Y 1 A LYS 52  ? NZ  ? A LYS 32  NZ  
13  1 Y 1 A ARG 55  ? CZ  ? A ARG 35  CZ  
14  1 Y 1 A ARG 55  ? NH1 ? A ARG 35  NH1 
15  1 Y 1 A ARG 55  ? NH2 ? A ARG 35  NH2 
16  1 Y 1 A LYS 78  ? NZ  ? A LYS 58  NZ  
17  1 Y 1 A GLU 90  ? OE1 ? A GLU 70  OE1 
18  1 Y 1 A GLU 90  ? OE2 ? A GLU 70  OE2 
19  1 Y 1 A ARG 91  ? CG  ? A ARG 71  CG  
20  1 Y 1 A ARG 91  ? CD  ? A ARG 71  CD  
21  1 Y 1 A ARG 91  ? NE  ? A ARG 71  NE  
22  1 Y 1 A ARG 91  ? CZ  ? A ARG 71  CZ  
23  1 Y 1 A ARG 91  ? NH1 ? A ARG 71  NH1 
24  1 Y 1 A ARG 91  ? NH2 ? A ARG 71  NH2 
25  1 Y 1 A GLN 135 ? OE1 ? A GLN 115 OE1 
26  1 Y 1 A GLN 135 ? NE2 ? A GLN 115 NE2 
27  1 Y 1 A TYR 152 ? CD1 ? A TYR 132 CD1 
28  1 Y 1 A TYR 152 ? CD2 ? A TYR 132 CD2 
29  1 Y 1 A TYR 152 ? CE1 ? A TYR 132 CE1 
30  1 Y 1 A TYR 152 ? CE2 ? A TYR 132 CE2 
31  1 Y 1 A TYR 152 ? CZ  ? A TYR 132 CZ  
32  1 Y 1 A TYR 152 ? OH  ? A TYR 132 OH  
33  1 Y 1 A LYS 241 ? CE  ? A LYS 221 CE  
34  1 Y 1 A LYS 241 ? NZ  ? A LYS 221 NZ  
35  1 Y 1 A GLU 247 ? CG  ? A GLU 227 CG  
36  1 Y 1 A GLU 247 ? CD  ? A GLU 227 CD  
37  1 Y 1 A GLU 247 ? OE1 ? A GLU 227 OE1 
38  1 Y 1 A GLU 247 ? OE2 ? A GLU 227 OE2 
39  1 Y 1 A ARG 251 ? CG  ? A ARG 231 CG  
40  1 Y 1 A ARG 251 ? CD  ? A ARG 231 CD  
41  1 Y 1 A ARG 251 ? NE  ? A ARG 231 NE  
42  1 Y 1 A ARG 251 ? CZ  ? A ARG 231 CZ  
43  1 Y 1 A ARG 251 ? NH1 ? A ARG 231 NH1 
44  1 Y 1 A ARG 251 ? NH2 ? A ARG 231 NH2 
45  1 Y 1 A LYS 252 ? CE  ? A LYS 232 CE  
46  1 Y 1 A LYS 252 ? NZ  ? A LYS 232 NZ  
47  1 Y 1 A ASP 259 ? CG  ? A ASP 239 CG  
48  1 Y 1 A ASP 259 ? OD1 ? A ASP 239 OD1 
49  1 Y 1 A ASP 259 ? OD2 ? A ASP 239 OD2 
50  1 Y 1 A GLU 264 ? CG  ? A GLU 244 CG  
51  1 Y 1 A GLU 264 ? CD  ? A GLU 244 CD  
52  1 Y 1 A GLU 264 ? OE1 ? A GLU 244 OE1 
53  1 Y 1 A GLU 264 ? OE2 ? A GLU 244 OE2 
54  1 Y 1 A GLU 278 ? CG  ? A GLU 258 CG  
55  1 Y 1 A GLU 278 ? CD  ? A GLU 258 CD  
56  1 Y 1 A GLU 278 ? OE1 ? A GLU 258 OE1 
57  1 Y 1 A GLU 278 ? OE2 ? A GLU 258 OE2 
58  1 Y 1 A SER 293 ? OG  ? A SER 273 OG  
59  1 Y 1 A HIS 296 ? CG  ? A HIS 276 CG  
60  1 Y 1 A HIS 296 ? ND1 ? A HIS 276 ND1 
61  1 Y 1 A HIS 296 ? CD2 ? A HIS 276 CD2 
62  1 Y 1 A HIS 296 ? CE1 ? A HIS 276 CE1 
63  1 Y 1 A HIS 296 ? NE2 ? A HIS 276 NE2 
64  1 Y 1 A ARG 301 ? CG  ? A ARG 281 CG  
65  1 Y 1 A ARG 301 ? CD  ? A ARG 281 CD  
66  1 Y 1 A ARG 301 ? NE  ? A ARG 281 NE  
67  1 Y 1 A ARG 301 ? CZ  ? A ARG 281 CZ  
68  1 Y 1 A ARG 301 ? NH1 ? A ARG 281 NH1 
69  1 Y 1 A ARG 301 ? NH2 ? A ARG 281 NH2 
70  1 Y 1 A LYS 436 ? CG  ? A LYS 416 CG  
71  1 Y 1 A LYS 436 ? CD  ? A LYS 416 CD  
72  1 Y 1 A LYS 436 ? CE  ? A LYS 416 CE  
73  1 Y 1 A LYS 436 ? NZ  ? A LYS 416 NZ  
74  1 Y 1 A VAL 458 ? CG1 ? A VAL 438 CG1 
75  1 Y 1 A VAL 458 ? CG2 ? A VAL 438 CG2 
76  1 Y 1 A GLN 533 ? CG  ? A GLN 513 CG  
77  1 Y 1 A GLN 533 ? CD  ? A GLN 513 CD  
78  1 Y 1 A GLN 533 ? OE1 ? A GLN 513 OE1 
79  1 Y 1 A GLN 533 ? NE2 ? A GLN 513 NE2 
80  1 Y 1 A LYS 535 ? CE  ? A LYS 515 CE  
81  1 Y 1 A LYS 535 ? NZ  ? A LYS 515 NZ  
82  1 Y 1 A ARG 546 ? NE  ? A ARG 526 NE  
83  1 Y 1 A ARG 546 ? CZ  ? A ARG 526 CZ  
84  1 Y 1 A ARG 546 ? NH1 ? A ARG 526 NH1 
85  1 Y 1 A ARG 546 ? NH2 ? A ARG 526 NH2 
86  1 Y 1 A ARG 568 ? NE  ? A ARG 548 NE  
87  1 Y 1 A ARG 568 ? CZ  ? A ARG 548 CZ  
88  1 Y 1 A ARG 568 ? NH1 ? A ARG 548 NH1 
89  1 Y 1 A ARG 568 ? NH2 ? A ARG 548 NH2 
90  1 Y 1 A LYS 570 ? CG  ? A LYS 550 CG  
91  1 Y 1 A LYS 570 ? CD  ? A LYS 550 CD  
92  1 Y 1 A LYS 570 ? CE  ? A LYS 550 CE  
93  1 Y 1 A LYS 570 ? NZ  ? A LYS 550 NZ  
94  1 Y 1 A LYS 572 ? CG  ? A LYS 552 CG  
95  1 Y 1 A LYS 572 ? CD  ? A LYS 552 CD  
96  1 Y 1 A LYS 572 ? CE  ? A LYS 552 CE  
97  1 Y 1 A LYS 572 ? NZ  ? A LYS 552 NZ  
98  1 Y 1 A LYS 575 ? CD  ? A LYS 555 CD  
99  1 Y 1 A LYS 575 ? CE  ? A LYS 555 CE  
100 1 Y 1 A LYS 575 ? NZ  ? A LYS 555 NZ  
101 1 Y 1 A LYS 590 ? CD  ? A LYS 570 CD  
102 1 Y 1 A LYS 590 ? CE  ? A LYS 570 CE  
103 1 Y 1 A LYS 590 ? NZ  ? A LYS 570 NZ  
104 1 Y 1 B ARG 28  ? CG  ? B ARG 8   CG  
105 1 Y 1 B ARG 28  ? CD  ? B ARG 8   CD  
106 1 Y 1 B ARG 28  ? NE  ? B ARG 8   NE  
107 1 Y 1 B ARG 28  ? CZ  ? B ARG 8   CZ  
108 1 Y 1 B ARG 28  ? NH1 ? B ARG 8   NH1 
109 1 Y 1 B ARG 28  ? NH2 ? B ARG 8   NH2 
110 1 Y 1 B GLN 39  ? CG  ? B GLN 19  CG  
111 1 Y 1 B GLN 39  ? CD  ? B GLN 19  CD  
112 1 Y 1 B GLN 39  ? OE1 ? B GLN 19  OE1 
113 1 Y 1 B GLN 39  ? NE2 ? B GLN 19  NE2 
114 1 Y 1 B LYS 52  ? CG  ? B LYS 32  CG  
115 1 Y 1 B LYS 52  ? CD  ? B LYS 32  CD  
116 1 Y 1 B LYS 52  ? CE  ? B LYS 32  CE  
117 1 Y 1 B LYS 52  ? NZ  ? B LYS 32  NZ  
118 1 Y 1 B ARG 55  ? NH1 ? B ARG 35  NH1 
119 1 Y 1 B ARG 55  ? NH2 ? B ARG 35  NH2 
120 1 Y 1 B ARG 84  ? NE  ? B ARG 64  NE  
121 1 Y 1 B ARG 84  ? CZ  ? B ARG 64  CZ  
122 1 Y 1 B ARG 84  ? NH1 ? B ARG 64  NH1 
123 1 Y 1 B ARG 84  ? NH2 ? B ARG 64  NH2 
124 1 Y 1 B LYS 88  ? CE  ? B LYS 68  CE  
125 1 Y 1 B LYS 88  ? NZ  ? B LYS 68  NZ  
126 1 Y 1 B ARG 91  ? CG  ? B ARG 71  CG  
127 1 Y 1 B ARG 91  ? CD  ? B ARG 71  CD  
128 1 Y 1 B ARG 91  ? NE  ? B ARG 71  NE  
129 1 Y 1 B ARG 91  ? CZ  ? B ARG 71  CZ  
130 1 Y 1 B ARG 91  ? NH1 ? B ARG 71  NH1 
131 1 Y 1 B ARG 91  ? NH2 ? B ARG 71  NH2 
132 1 Y 1 B GLU 107 ? CG  ? B GLU 87  CG  
133 1 Y 1 B GLU 107 ? CD  ? B GLU 87  CD  
134 1 Y 1 B GLU 107 ? OE1 ? B GLU 87  OE1 
135 1 Y 1 B GLU 107 ? OE2 ? B GLU 87  OE2 
136 1 Y 1 B ARG 126 ? CG  ? B ARG 106 CG  
137 1 Y 1 B ARG 126 ? CD  ? B ARG 106 CD  
138 1 Y 1 B ARG 126 ? NE  ? B ARG 106 NE  
139 1 Y 1 B ARG 126 ? CZ  ? B ARG 106 CZ  
140 1 Y 1 B ARG 126 ? NH1 ? B ARG 106 NH1 
141 1 Y 1 B ARG 126 ? NH2 ? B ARG 106 NH2 
142 1 Y 1 B SER 129 ? OG  ? B SER 109 OG  
143 1 Y 1 B GLN 156 ? CG  ? B GLN 136 CG  
144 1 Y 1 B GLN 156 ? CD  ? B GLN 136 CD  
145 1 Y 1 B GLN 156 ? OE1 ? B GLN 136 OE1 
146 1 Y 1 B GLN 156 ? NE2 ? B GLN 136 NE2 
147 1 Y 1 B GLN 164 ? CG  ? B GLN 144 CG  
148 1 Y 1 B GLN 164 ? CD  ? B GLN 144 CD  
149 1 Y 1 B GLN 164 ? OE1 ? B GLN 144 OE1 
150 1 Y 1 B GLN 164 ? NE2 ? B GLN 144 NE2 
151 1 Y 1 B GLU 247 ? CG  ? B GLU 227 CG  
152 1 Y 1 B GLU 247 ? CD  ? B GLU 227 CD  
153 1 Y 1 B GLU 247 ? OE1 ? B GLU 227 OE1 
154 1 Y 1 B GLU 247 ? OE2 ? B GLU 227 OE2 
155 1 Y 1 B ARG 251 ? CG  ? B ARG 231 CG  
156 1 Y 1 B ARG 251 ? CD  ? B ARG 231 CD  
157 1 Y 1 B ARG 251 ? NE  ? B ARG 231 NE  
158 1 Y 1 B ARG 251 ? CZ  ? B ARG 231 CZ  
159 1 Y 1 B ARG 251 ? NH1 ? B ARG 231 NH1 
160 1 Y 1 B ARG 251 ? NH2 ? B ARG 231 NH2 
161 1 Y 1 B GLU 278 ? CG  ? B GLU 258 CG  
162 1 Y 1 B GLU 278 ? CD  ? B GLU 258 CD  
163 1 Y 1 B GLU 278 ? OE1 ? B GLU 258 OE1 
164 1 Y 1 B GLU 278 ? OE2 ? B GLU 258 OE2 
165 1 Y 1 B ARG 311 ? CG  ? B ARG 291 CG  
166 1 Y 1 B ARG 311 ? CD  ? B ARG 291 CD  
167 1 Y 1 B ARG 311 ? NE  ? B ARG 291 NE  
168 1 Y 1 B ARG 311 ? CZ  ? B ARG 291 CZ  
169 1 Y 1 B ARG 311 ? NH1 ? B ARG 291 NH1 
170 1 Y 1 B ARG 311 ? NH2 ? B ARG 291 NH2 
171 1 Y 1 B GLU 313 ? CG  ? B GLU 293 CG  
172 1 Y 1 B GLU 313 ? CD  ? B GLU 293 CD  
173 1 Y 1 B GLU 313 ? OE1 ? B GLU 293 OE1 
174 1 Y 1 B GLU 313 ? OE2 ? B GLU 293 OE2 
175 1 Y 1 B VAL 458 ? CG1 ? B VAL 438 CG1 
176 1 Y 1 B VAL 458 ? CG2 ? B VAL 438 CG2 
177 1 Y 1 B GLN 533 ? CG  ? B GLN 513 CG  
178 1 Y 1 B GLN 533 ? CD  ? B GLN 513 CD  
179 1 Y 1 B GLN 533 ? OE1 ? B GLN 513 OE1 
180 1 Y 1 B GLN 533 ? NE2 ? B GLN 513 NE2 
181 1 Y 1 B LYS 535 ? CD  ? B LYS 515 CD  
182 1 Y 1 B LYS 535 ? CE  ? B LYS 515 CE  
183 1 Y 1 B LYS 535 ? NZ  ? B LYS 515 NZ  
184 1 Y 1 B ARG 546 ? NE  ? B ARG 526 NE  
185 1 Y 1 B ARG 546 ? CZ  ? B ARG 526 CZ  
186 1 Y 1 B ARG 546 ? NH1 ? B ARG 526 NH1 
187 1 Y 1 B ARG 546 ? NH2 ? B ARG 526 NH2 
188 1 Y 1 B GLN 556 ? CG  ? B GLN 536 CG  
189 1 Y 1 B GLN 556 ? CD  ? B GLN 536 CD  
190 1 Y 1 B GLN 556 ? OE1 ? B GLN 536 OE1 
191 1 Y 1 B GLN 556 ? NE2 ? B GLN 536 NE2 
192 1 Y 1 B ARG 568 ? CZ  ? B ARG 548 CZ  
193 1 Y 1 B ARG 568 ? NH1 ? B ARG 548 NH1 
194 1 Y 1 B ARG 568 ? NH2 ? B ARG 548 NH2 
195 1 Y 1 B LYS 570 ? CG  ? B LYS 550 CG  
196 1 Y 1 B LYS 570 ? CD  ? B LYS 550 CD  
197 1 Y 1 B LYS 570 ? CE  ? B LYS 550 CE  
198 1 Y 1 B LYS 570 ? NZ  ? B LYS 550 NZ  
199 1 Y 1 B LYS 572 ? CG  ? B LYS 552 CG  
200 1 Y 1 B LYS 572 ? CD  ? B LYS 552 CD  
201 1 Y 1 B LYS 572 ? CE  ? B LYS 552 CE  
202 1 Y 1 B LYS 572 ? NZ  ? B LYS 552 NZ  
203 1 Y 1 B LYS 590 ? CE  ? B LYS 570 CE  
204 1 Y 1 B LYS 590 ? NZ  ? B LYS 570 NZ  
205 1 Y 1 B ASN 721 ? CG  ? B ASN 701 CG  
206 1 Y 1 B ASN 721 ? OD1 ? B ASN 701 OD1 
207 1 Y 1 B ASN 721 ? ND2 ? B ASN 701 ND2 
# 
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 ARG 21  ? A ARG 1   
2  1 Y 1 A SER 22  ? A SER 2   
3  1 Y 1 A PRO 23  ? A PRO 3   
4  1 Y 1 A GLY 24  ? A GLY 4   
5  1 Y 1 A THR 25  ? A THR 5   
6  1 Y 1 A LEU 26  ? A LEU 6   
7  1 Y 1 A PRO 268 ? A PRO 248 
8  1 Y 1 A GLY 269 ? A GLY 249 
9  1 Y 1 A GLY 270 ? A GLY 250 
10 1 Y 1 A LYS 271 ? A LYS 251 
11 1 Y 1 A GLY 272 ? A GLY 252 
12 1 Y 1 A HIS 273 ? A HIS 253 
13 1 Y 1 A ASP 274 ? A ASP 254 
14 1 Y 1 A SER 275 ? A SER 255 
15 1 Y 1 A THR 276 ? A THR 256 
16 1 Y 1 A GLU 277 ? A GLU 257 
17 1 Y 1 B ARG 21  ? B ARG 1   
18 1 Y 1 B SER 22  ? B SER 2   
19 1 Y 1 B PRO 23  ? B PRO 3   
20 1 Y 1 B GLY 24  ? B GLY 4   
21 1 Y 1 B THR 25  ? B THR 5   
22 1 Y 1 B LEU 26  ? B LEU 6   
23 1 Y 1 B PRO 27  ? B PRO 7   
24 1 Y 1 B GLU 264 ? B GLU 244 
25 1 Y 1 B ASP 265 ? B ASP 245 
26 1 Y 1 B PRO 266 ? B PRO 246 
27 1 Y 1 B LEU 267 ? B LEU 247 
28 1 Y 1 B PRO 268 ? B PRO 248 
29 1 Y 1 B GLY 269 ? B GLY 249 
30 1 Y 1 B GLY 270 ? B GLY 250 
31 1 Y 1 B LYS 271 ? B LYS 251 
32 1 Y 1 B GLY 272 ? B GLY 252 
33 1 Y 1 B HIS 273 ? B HIS 253 
34 1 Y 1 B ASP 274 ? B ASP 254 
35 1 Y 1 B SER 275 ? B SER 255 
36 1 Y 1 B THR 276 ? B THR 256 
37 1 Y 1 B GLU 277 ? B GLU 257 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION'                  CU  
3 'CALCIUM ION'                      CA  
4 GLYCEROL                           GOL 
5 '1,5-BIS(4-AMIDINOPHENOXY)PENTANE' PNT 
6 N-ACETYL-D-GLUCOSAMINE             NAG 
7 BETA-D-MANNOSE                     BMA 
8 water                              HOH 
# 
