data_4LXS
# 
_entry.id   4LXS 
# 
_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   4LXS         
RCSB  RCSB081219   
WWPDB D_1000081219 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3e07 'Spaetzle ligand' unspecified 
PDB 4LXR .                 unspecified 
# 
_pdbx_database_status.entry_id                        4LXS 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2013-07-30 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Stelter, M.'    1 
'Parthier, C.'   2 
'Breithaupt, C.' 3 
'Stubbs, M.T.'   4 
# 
_citation.id                        primary 
_citation.title                     
'Structure of the Toll-Spatzle complex, a molecular hub in Drosophila development and innate immunity.' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            111 
_citation.page_first                6281 
_citation.page_last                 6286 
_citation.year                      2014 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24733933 
_citation.pdbx_database_id_DOI      10.1073/pnas.1320678111 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Parthier, C.'   1 
primary 'Stelter, M.'    2 
primary 'Ursel, C.'      3 
primary 'Fandrich, U.'   4 
primary 'Lilie, H.'      5 
primary 'Breithaupt, C.' 6 
primary 'Stubbs, M.T.'   7 
# 
_cell.entry_id           4LXS 
_cell.length_a           171.278 
_cell.length_b           76.824 
_cell.length_c           123.822 
_cell.angle_alpha        90.00 
_cell.angle_beta         126.29 
_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                         4LXS 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_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 'Protein toll'                                        89632.398 1  ? ? 'UNP residues 28-802' ? 
2 polymer     man 'Protein spaetzle C-106'                              13006.618 2  ? ? ?                     ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                                221.208   19 ? ? ?                     ? 
4 non-polymer man BETA-D-MANNOSE                                        180.156   3  ? ? ?                     ? 
5 non-polymer man ALPHA-D-MANNOSE                                       180.156   1  ? ? ?                     ? 
6 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   1  ? ? ?                     ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;SFGRDACSEMSIDGLCQCAPIMSEYEIICPANAENPTFRLTIQPKDYVQIMCNLTDTTDYQQLPKKLRIGEVDRVQMRRC
MLPGHTPIASILDYLGIVSPTTLIFESDNLGMNITRQHLDRLHGLKRFRFTTRRLTHIPANLLTDMRNLSHLELRANIEE
MPSHLFDDLENLESIEFGSNKLRQMPRGIFGKMPKLKQLNLWSNQLHNLTKHDFEGATSVLGIDIHDNGIEQLPHDVFAH
LTNVTDINLSANLFRSLPQGLFDHNKHLNEVRLMNNRVPLATLPSRLFANQPELQILRLRAELQSLPGDLFEHSTQITNI
SLGDNLLKTLPATLLEHQVNLLSLDLSNNRLTHLPDSLFAHTTNLTDLRLEDNLLTGISGDIFSNLGNLVTLVMSRNRLR
TIDSRAFVSTNGLRHLHLDHNDIDLQQPLLDIMLQTQINSPFGYMHGLLTLNLRNNSIIFVYNDWKNTMLQLRELDLSYN
NISSLGYEDLAFLSQNRLHVNMTHNKIRRIALPEDVHLGEGYNNNLVHVDLNDNPLVCDCTILWFIQLVRGVHKPQYSRQ
FKLRTDRLVCSQPNVLEGTPVRQIEPQTLICPLDFSDDPRERKCPRGCNCHVRTYDKALVINCHSGNLTHVPRLPNLHKN
MQLMELHLENNTLLRLPSANTPGYESVTSLHLAGNNLTSIDVDQLPTNLTHLDISWNHLQMLNATVLGFLNRTMKWRSVK
LSGNPWMCDCTAKPLLLFTQDNFERIGDRNEMMCVNAEMPTRMVELSTNDICPAETGHHHHHH
;
;SFGRDACSEMSIDGLCQCAPIMSEYEIICPANAENPTFRLTIQPKDYVQIMCNLTDTTDYQQLPKKLRIGEVDRVQMRRC
MLPGHTPIASILDYLGIVSPTTLIFESDNLGMNITRQHLDRLHGLKRFRFTTRRLTHIPANLLTDMRNLSHLELRANIEE
MPSHLFDDLENLESIEFGSNKLRQMPRGIFGKMPKLKQLNLWSNQLHNLTKHDFEGATSVLGIDIHDNGIEQLPHDVFAH
LTNVTDINLSANLFRSLPQGLFDHNKHLNEVRLMNNRVPLATLPSRLFANQPELQILRLRAELQSLPGDLFEHSTQITNI
SLGDNLLKTLPATLLEHQVNLLSLDLSNNRLTHLPDSLFAHTTNLTDLRLEDNLLTGISGDIFSNLGNLVTLVMSRNRLR
TIDSRAFVSTNGLRHLHLDHNDIDLQQPLLDIMLQTQINSPFGYMHGLLTLNLRNNSIIFVYNDWKNTMLQLRELDLSYN
NISSLGYEDLAFLSQNRLHVNMTHNKIRRIALPEDVHLGEGYNNNLVHVDLNDNPLVCDCTILWFIQLVRGVHKPQYSRQ
FKLRTDRLVCSQPNVLEGTPVRQIEPQTLICPLDFSDDPRERKCPRGCNCHVRTYDKALVINCHSGNLTHVPRLPNLHKN
MQLMELHLENNTLLRLPSANTPGYESVTSLHLAGNNLTSIDVDQLPTNLTHLDISWNHLQMLNATVLGFLNRTMKWRSVK
LSGNPWMCDCTAKPLLLFTQDNFERIGDRNEMMCVNAEMPTRMVELSTNDICPAETGHHHHHH
;
A   ? 
2 'polypeptide(L)' no no 
;VGGSDERFLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASI
KSDGELDVVQNSFKIPSCCKCALKTGLEHHHHHH
;
;VGGSDERFLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASI
KSDGELDVVQNSFKIPSCCKCALKTGLEHHHHHH
;
J,K ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   PHE n 
1 3   GLY n 
1 4   ARG n 
1 5   ASP n 
1 6   ALA n 
1 7   CYS n 
1 8   SER n 
1 9   GLU n 
1 10  MET n 
1 11  SER n 
1 12  ILE n 
1 13  ASP n 
1 14  GLY n 
1 15  LEU n 
1 16  CYS n 
1 17  GLN n 
1 18  CYS n 
1 19  ALA n 
1 20  PRO n 
1 21  ILE n 
1 22  MET n 
1 23  SER n 
1 24  GLU n 
1 25  TYR n 
1 26  GLU n 
1 27  ILE n 
1 28  ILE n 
1 29  CYS n 
1 30  PRO n 
1 31  ALA n 
1 32  ASN n 
1 33  ALA n 
1 34  GLU n 
1 35  ASN n 
1 36  PRO n 
1 37  THR n 
1 38  PHE n 
1 39  ARG n 
1 40  LEU n 
1 41  THR n 
1 42  ILE n 
1 43  GLN n 
1 44  PRO n 
1 45  LYS n 
1 46  ASP n 
1 47  TYR n 
1 48  VAL n 
1 49  GLN n 
1 50  ILE n 
1 51  MET n 
1 52  CYS n 
1 53  ASN n 
1 54  LEU n 
1 55  THR n 
1 56  ASP n 
1 57  THR n 
1 58  THR n 
1 59  ASP n 
1 60  TYR n 
1 61  GLN n 
1 62  GLN n 
1 63  LEU n 
1 64  PRO n 
1 65  LYS n 
1 66  LYS n 
1 67  LEU n 
1 68  ARG n 
1 69  ILE n 
1 70  GLY n 
1 71  GLU n 
1 72  VAL n 
1 73  ASP n 
1 74  ARG n 
1 75  VAL n 
1 76  GLN n 
1 77  MET n 
1 78  ARG n 
1 79  ARG n 
1 80  CYS n 
1 81  MET n 
1 82  LEU n 
1 83  PRO n 
1 84  GLY n 
1 85  HIS n 
1 86  THR n 
1 87  PRO n 
1 88  ILE n 
1 89  ALA n 
1 90  SER n 
1 91  ILE n 
1 92  LEU n 
1 93  ASP n 
1 94  TYR n 
1 95  LEU n 
1 96  GLY n 
1 97  ILE n 
1 98  VAL n 
1 99  SER n 
1 100 PRO n 
1 101 THR n 
1 102 THR n 
1 103 LEU n 
1 104 ILE n 
1 105 PHE n 
1 106 GLU n 
1 107 SER n 
1 108 ASP n 
1 109 ASN n 
1 110 LEU n 
1 111 GLY n 
1 112 MET n 
1 113 ASN n 
1 114 ILE n 
1 115 THR n 
1 116 ARG n 
1 117 GLN n 
1 118 HIS n 
1 119 LEU n 
1 120 ASP n 
1 121 ARG n 
1 122 LEU n 
1 123 HIS n 
1 124 GLY n 
1 125 LEU n 
1 126 LYS n 
1 127 ARG n 
1 128 PHE n 
1 129 ARG n 
1 130 PHE n 
1 131 THR n 
1 132 THR n 
1 133 ARG n 
1 134 ARG n 
1 135 LEU n 
1 136 THR n 
1 137 HIS n 
1 138 ILE n 
1 139 PRO n 
1 140 ALA n 
1 141 ASN n 
1 142 LEU n 
1 143 LEU n 
1 144 THR n 
1 145 ASP n 
1 146 MET n 
1 147 ARG n 
1 148 ASN n 
1 149 LEU n 
1 150 SER n 
1 151 HIS n 
1 152 LEU n 
1 153 GLU n 
1 154 LEU n 
1 155 ARG n 
1 156 ALA n 
1 157 ASN n 
1 158 ILE n 
1 159 GLU n 
1 160 GLU n 
1 161 MET n 
1 162 PRO n 
1 163 SER n 
1 164 HIS n 
1 165 LEU n 
1 166 PHE n 
1 167 ASP n 
1 168 ASP n 
1 169 LEU n 
1 170 GLU n 
1 171 ASN n 
1 172 LEU n 
1 173 GLU n 
1 174 SER n 
1 175 ILE n 
1 176 GLU n 
1 177 PHE n 
1 178 GLY n 
1 179 SER n 
1 180 ASN n 
1 181 LYS n 
1 182 LEU n 
1 183 ARG n 
1 184 GLN n 
1 185 MET n 
1 186 PRO n 
1 187 ARG n 
1 188 GLY n 
1 189 ILE n 
1 190 PHE n 
1 191 GLY n 
1 192 LYS n 
1 193 MET n 
1 194 PRO n 
1 195 LYS n 
1 196 LEU n 
1 197 LYS n 
1 198 GLN n 
1 199 LEU n 
1 200 ASN n 
1 201 LEU n 
1 202 TRP n 
1 203 SER n 
1 204 ASN n 
1 205 GLN n 
1 206 LEU n 
1 207 HIS n 
1 208 ASN n 
1 209 LEU n 
1 210 THR n 
1 211 LYS n 
1 212 HIS n 
1 213 ASP n 
1 214 PHE n 
1 215 GLU n 
1 216 GLY n 
1 217 ALA n 
1 218 THR n 
1 219 SER n 
1 220 VAL n 
1 221 LEU n 
1 222 GLY n 
1 223 ILE n 
1 224 ASP n 
1 225 ILE n 
1 226 HIS n 
1 227 ASP n 
1 228 ASN n 
1 229 GLY n 
1 230 ILE n 
1 231 GLU n 
1 232 GLN n 
1 233 LEU n 
1 234 PRO n 
1 235 HIS n 
1 236 ASP n 
1 237 VAL n 
1 238 PHE n 
1 239 ALA n 
1 240 HIS n 
1 241 LEU n 
1 242 THR n 
1 243 ASN n 
1 244 VAL n 
1 245 THR n 
1 246 ASP n 
1 247 ILE n 
1 248 ASN n 
1 249 LEU n 
1 250 SER n 
1 251 ALA n 
1 252 ASN n 
1 253 LEU n 
1 254 PHE n 
1 255 ARG n 
1 256 SER n 
1 257 LEU n 
1 258 PRO n 
1 259 GLN n 
1 260 GLY n 
1 261 LEU n 
1 262 PHE n 
1 263 ASP n 
1 264 HIS n 
1 265 ASN n 
1 266 LYS n 
1 267 HIS n 
1 268 LEU n 
1 269 ASN n 
1 270 GLU n 
1 271 VAL n 
1 272 ARG n 
1 273 LEU n 
1 274 MET n 
1 275 ASN n 
1 276 ASN n 
1 277 ARG n 
1 278 VAL n 
1 279 PRO n 
1 280 LEU n 
1 281 ALA n 
1 282 THR n 
1 283 LEU n 
1 284 PRO n 
1 285 SER n 
1 286 ARG n 
1 287 LEU n 
1 288 PHE n 
1 289 ALA n 
1 290 ASN n 
1 291 GLN n 
1 292 PRO n 
1 293 GLU n 
1 294 LEU n 
1 295 GLN n 
1 296 ILE n 
1 297 LEU n 
1 298 ARG n 
1 299 LEU n 
1 300 ARG n 
1 301 ALA n 
1 302 GLU n 
1 303 LEU n 
1 304 GLN n 
1 305 SER n 
1 306 LEU n 
1 307 PRO n 
1 308 GLY n 
1 309 ASP n 
1 310 LEU n 
1 311 PHE n 
1 312 GLU n 
1 313 HIS n 
1 314 SER n 
1 315 THR n 
1 316 GLN n 
1 317 ILE n 
1 318 THR n 
1 319 ASN n 
1 320 ILE n 
1 321 SER n 
1 322 LEU n 
1 323 GLY n 
1 324 ASP n 
1 325 ASN n 
1 326 LEU n 
1 327 LEU n 
1 328 LYS n 
1 329 THR n 
1 330 LEU n 
1 331 PRO n 
1 332 ALA n 
1 333 THR n 
1 334 LEU n 
1 335 LEU n 
1 336 GLU n 
1 337 HIS n 
1 338 GLN n 
1 339 VAL n 
1 340 ASN n 
1 341 LEU n 
1 342 LEU n 
1 343 SER n 
1 344 LEU n 
1 345 ASP n 
1 346 LEU n 
1 347 SER n 
1 348 ASN n 
1 349 ASN n 
1 350 ARG n 
1 351 LEU n 
1 352 THR n 
1 353 HIS n 
1 354 LEU n 
1 355 PRO n 
1 356 ASP n 
1 357 SER n 
1 358 LEU n 
1 359 PHE n 
1 360 ALA n 
1 361 HIS n 
1 362 THR n 
1 363 THR n 
1 364 ASN n 
1 365 LEU n 
1 366 THR n 
1 367 ASP n 
1 368 LEU n 
1 369 ARG n 
1 370 LEU n 
1 371 GLU n 
1 372 ASP n 
1 373 ASN n 
1 374 LEU n 
1 375 LEU n 
1 376 THR n 
1 377 GLY n 
1 378 ILE n 
1 379 SER n 
1 380 GLY n 
1 381 ASP n 
1 382 ILE n 
1 383 PHE n 
1 384 SER n 
1 385 ASN n 
1 386 LEU n 
1 387 GLY n 
1 388 ASN n 
1 389 LEU n 
1 390 VAL n 
1 391 THR n 
1 392 LEU n 
1 393 VAL n 
1 394 MET n 
1 395 SER n 
1 396 ARG n 
1 397 ASN n 
1 398 ARG n 
1 399 LEU n 
1 400 ARG n 
1 401 THR n 
1 402 ILE n 
1 403 ASP n 
1 404 SER n 
1 405 ARG n 
1 406 ALA n 
1 407 PHE n 
1 408 VAL n 
1 409 SER n 
1 410 THR n 
1 411 ASN n 
1 412 GLY n 
1 413 LEU n 
1 414 ARG n 
1 415 HIS n 
1 416 LEU n 
1 417 HIS n 
1 418 LEU n 
1 419 ASP n 
1 420 HIS n 
1 421 ASN n 
1 422 ASP n 
1 423 ILE n 
1 424 ASP n 
1 425 LEU n 
1 426 GLN n 
1 427 GLN n 
1 428 PRO n 
1 429 LEU n 
1 430 LEU n 
1 431 ASP n 
1 432 ILE n 
1 433 MET n 
1 434 LEU n 
1 435 GLN n 
1 436 THR n 
1 437 GLN n 
1 438 ILE n 
1 439 ASN n 
1 440 SER n 
1 441 PRO n 
1 442 PHE n 
1 443 GLY n 
1 444 TYR n 
1 445 MET n 
1 446 HIS n 
1 447 GLY n 
1 448 LEU n 
1 449 LEU n 
1 450 THR n 
1 451 LEU n 
1 452 ASN n 
1 453 LEU n 
1 454 ARG n 
1 455 ASN n 
1 456 ASN n 
1 457 SER n 
1 458 ILE n 
1 459 ILE n 
1 460 PHE n 
1 461 VAL n 
1 462 TYR n 
1 463 ASN n 
1 464 ASP n 
1 465 TRP n 
1 466 LYS n 
1 467 ASN n 
1 468 THR n 
1 469 MET n 
1 470 LEU n 
1 471 GLN n 
1 472 LEU n 
1 473 ARG n 
1 474 GLU n 
1 475 LEU n 
1 476 ASP n 
1 477 LEU n 
1 478 SER n 
1 479 TYR n 
1 480 ASN n 
1 481 ASN n 
1 482 ILE n 
1 483 SER n 
1 484 SER n 
1 485 LEU n 
1 486 GLY n 
1 487 TYR n 
1 488 GLU n 
1 489 ASP n 
1 490 LEU n 
1 491 ALA n 
1 492 PHE n 
1 493 LEU n 
1 494 SER n 
1 495 GLN n 
1 496 ASN n 
1 497 ARG n 
1 498 LEU n 
1 499 HIS n 
1 500 VAL n 
1 501 ASN n 
1 502 MET n 
1 503 THR n 
1 504 HIS n 
1 505 ASN n 
1 506 LYS n 
1 507 ILE n 
1 508 ARG n 
1 509 ARG n 
1 510 ILE n 
1 511 ALA n 
1 512 LEU n 
1 513 PRO n 
1 514 GLU n 
1 515 ASP n 
1 516 VAL n 
1 517 HIS n 
1 518 LEU n 
1 519 GLY n 
1 520 GLU n 
1 521 GLY n 
1 522 TYR n 
1 523 ASN n 
1 524 ASN n 
1 525 ASN n 
1 526 LEU n 
1 527 VAL n 
1 528 HIS n 
1 529 VAL n 
1 530 ASP n 
1 531 LEU n 
1 532 ASN n 
1 533 ASP n 
1 534 ASN n 
1 535 PRO n 
1 536 LEU n 
1 537 VAL n 
1 538 CYS n 
1 539 ASP n 
1 540 CYS n 
1 541 THR n 
1 542 ILE n 
1 543 LEU n 
1 544 TRP n 
1 545 PHE n 
1 546 ILE n 
1 547 GLN n 
1 548 LEU n 
1 549 VAL n 
1 550 ARG n 
1 551 GLY n 
1 552 VAL n 
1 553 HIS n 
1 554 LYS n 
1 555 PRO n 
1 556 GLN n 
1 557 TYR n 
1 558 SER n 
1 559 ARG n 
1 560 GLN n 
1 561 PHE n 
1 562 LYS n 
1 563 LEU n 
1 564 ARG n 
1 565 THR n 
1 566 ASP n 
1 567 ARG n 
1 568 LEU n 
1 569 VAL n 
1 570 CYS n 
1 571 SER n 
1 572 GLN n 
1 573 PRO n 
1 574 ASN n 
1 575 VAL n 
1 576 LEU n 
1 577 GLU n 
1 578 GLY n 
1 579 THR n 
1 580 PRO n 
1 581 VAL n 
1 582 ARG n 
1 583 GLN n 
1 584 ILE n 
1 585 GLU n 
1 586 PRO n 
1 587 GLN n 
1 588 THR n 
1 589 LEU n 
1 590 ILE n 
1 591 CYS n 
1 592 PRO n 
1 593 LEU n 
1 594 ASP n 
1 595 PHE n 
1 596 SER n 
1 597 ASP n 
1 598 ASP n 
1 599 PRO n 
1 600 ARG n 
1 601 GLU n 
1 602 ARG n 
1 603 LYS n 
1 604 CYS n 
1 605 PRO n 
1 606 ARG n 
1 607 GLY n 
1 608 CYS n 
1 609 ASN n 
1 610 CYS n 
1 611 HIS n 
1 612 VAL n 
1 613 ARG n 
1 614 THR n 
1 615 TYR n 
1 616 ASP n 
1 617 LYS n 
1 618 ALA n 
1 619 LEU n 
1 620 VAL n 
1 621 ILE n 
1 622 ASN n 
1 623 CYS n 
1 624 HIS n 
1 625 SER n 
1 626 GLY n 
1 627 ASN n 
1 628 LEU n 
1 629 THR n 
1 630 HIS n 
1 631 VAL n 
1 632 PRO n 
1 633 ARG n 
1 634 LEU n 
1 635 PRO n 
1 636 ASN n 
1 637 LEU n 
1 638 HIS n 
1 639 LYS n 
1 640 ASN n 
1 641 MET n 
1 642 GLN n 
1 643 LEU n 
1 644 MET n 
1 645 GLU n 
1 646 LEU n 
1 647 HIS n 
1 648 LEU n 
1 649 GLU n 
1 650 ASN n 
1 651 ASN n 
1 652 THR n 
1 653 LEU n 
1 654 LEU n 
1 655 ARG n 
1 656 LEU n 
1 657 PRO n 
1 658 SER n 
1 659 ALA n 
1 660 ASN n 
1 661 THR n 
1 662 PRO n 
1 663 GLY n 
1 664 TYR n 
1 665 GLU n 
1 666 SER n 
1 667 VAL n 
1 668 THR n 
1 669 SER n 
1 670 LEU n 
1 671 HIS n 
1 672 LEU n 
1 673 ALA n 
1 674 GLY n 
1 675 ASN n 
1 676 ASN n 
1 677 LEU n 
1 678 THR n 
1 679 SER n 
1 680 ILE n 
1 681 ASP n 
1 682 VAL n 
1 683 ASP n 
1 684 GLN n 
1 685 LEU n 
1 686 PRO n 
1 687 THR n 
1 688 ASN n 
1 689 LEU n 
1 690 THR n 
1 691 HIS n 
1 692 LEU n 
1 693 ASP n 
1 694 ILE n 
1 695 SER n 
1 696 TRP n 
1 697 ASN n 
1 698 HIS n 
1 699 LEU n 
1 700 GLN n 
1 701 MET n 
1 702 LEU n 
1 703 ASN n 
1 704 ALA n 
1 705 THR n 
1 706 VAL n 
1 707 LEU n 
1 708 GLY n 
1 709 PHE n 
1 710 LEU n 
1 711 ASN n 
1 712 ARG n 
1 713 THR n 
1 714 MET n 
1 715 LYS n 
1 716 TRP n 
1 717 ARG n 
1 718 SER n 
1 719 VAL n 
1 720 LYS n 
1 721 LEU n 
1 722 SER n 
1 723 GLY n 
1 724 ASN n 
1 725 PRO n 
1 726 TRP n 
1 727 MET n 
1 728 CYS n 
1 729 ASP n 
1 730 CYS n 
1 731 THR n 
1 732 ALA n 
1 733 LYS n 
1 734 PRO n 
1 735 LEU n 
1 736 LEU n 
1 737 LEU n 
1 738 PHE n 
1 739 THR n 
1 740 GLN n 
1 741 ASP n 
1 742 ASN n 
1 743 PHE n 
1 744 GLU n 
1 745 ARG n 
1 746 ILE n 
1 747 GLY n 
1 748 ASP n 
1 749 ARG n 
1 750 ASN n 
1 751 GLU n 
1 752 MET n 
1 753 MET n 
1 754 CYS n 
1 755 VAL n 
1 756 ASN n 
1 757 ALA n 
1 758 GLU n 
1 759 MET n 
1 760 PRO n 
1 761 THR n 
1 762 ARG n 
1 763 MET n 
1 764 VAL n 
1 765 GLU n 
1 766 LEU n 
1 767 SER n 
1 768 THR n 
1 769 ASN n 
1 770 ASP n 
1 771 ILE n 
1 772 CYS n 
1 773 PRO n 
1 774 ALA n 
1 775 GLU n 
1 776 THR n 
1 777 GLY n 
1 778 HIS n 
1 779 HIS n 
1 780 HIS n 
1 781 HIS n 
1 782 HIS n 
1 783 HIS n 
2 1   VAL n 
2 2   GLY n 
2 3   GLY n 
2 4   SER n 
2 5   ASP n 
2 6   GLU n 
2 7   ARG n 
2 8   PHE n 
2 9   LEU n 
2 10  CYS n 
2 11  ARG n 
2 12  SER n 
2 13  ILE n 
2 14  ARG n 
2 15  LYS n 
2 16  LEU n 
2 17  VAL n 
2 18  TYR n 
2 19  PRO n 
2 20  LYS n 
2 21  LYS n 
2 22  GLY n 
2 23  LEU n 
2 24  ARG n 
2 25  ALA n 
2 26  ASP n 
2 27  ASP n 
2 28  THR n 
2 29  TRP n 
2 30  GLN n 
2 31  LEU n 
2 32  ILE n 
2 33  VAL n 
2 34  ASN n 
2 35  ASN n 
2 36  ASP n 
2 37  GLU n 
2 38  TYR n 
2 39  LYS n 
2 40  GLN n 
2 41  ALA n 
2 42  ILE n 
2 43  GLN n 
2 44  ILE n 
2 45  GLU n 
2 46  GLU n 
2 47  CYS n 
2 48  GLU n 
2 49  GLY n 
2 50  ALA n 
2 51  ASP n 
2 52  GLN n 
2 53  PRO n 
2 54  CYS n 
2 55  ASP n 
2 56  PHE n 
2 57  ALA n 
2 58  ALA n 
2 59  ASN n 
2 60  PHE n 
2 61  PRO n 
2 62  GLN n 
2 63  SER n 
2 64  TYR n 
2 65  ASN n 
2 66  PRO n 
2 67  ILE n 
2 68  CYS n 
2 69  LYS n 
2 70  GLN n 
2 71  HIS n 
2 72  TYR n 
2 73  THR n 
2 74  GLN n 
2 75  GLN n 
2 76  THR n 
2 77  LEU n 
2 78  ALA n 
2 79  SER n 
2 80  ILE n 
2 81  LYS n 
2 82  SER n 
2 83  ASP n 
2 84  GLY n 
2 85  GLU n 
2 86  LEU n 
2 87  ASP n 
2 88  VAL n 
2 89  VAL n 
2 90  GLN n 
2 91  ASN n 
2 92  SER n 
2 93  PHE n 
2 94  LYS n 
2 95  ILE n 
2 96  PRO n 
2 97  SER n 
2 98  CYS n 
2 99  CYS n 
2 100 LYS n 
2 101 CYS n 
2 102 ALA n 
2 103 LEU n 
2 104 LYS n 
2 105 THR n 
2 106 GLY n 
2 107 LEU n 
2 108 GLU n 
2 109 HIS n 
2 110 HIS n 
2 111 HIS n 
2 112 HIS n 
2 113 HIS n 
2 114 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_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 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample ? ? ? 'Fruit fly' ? 'Tl, CG5490'  ? ? ? ? ? ? 'Drosophila melanogaster' 7227 ? ? ? ? ? ? ? ? 'Drosophila melanogaster' 
7227 ? ? ? ? ? ? 'Schneider 2'   ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? 'Fruit fly' ? 'spz, CG6134' ? ? ? ? ? ? 'Drosophila melanogaster' 7227 ? ? ? ? ? ? ? ? 'Escherichia coli'        
562  ? ? ? ? ? ? 'Rosetta (DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP TOLL_DROME P08953 1 
;SFGRDACSEMSIDGLCQCAPIMSEYEIICPANAENPTFRLTIQPKDYVQIMCNLTDTTDYQQLPKKLRIGEVDRVQMRRC
MLPGHTPIASILDYLGIVSPTTLIFESDNLGMNITRQHLDRLHGLKRFRFTTRRLTHIPANLLTDMRNLSHLELRANIEE
MPSHLFDDLENLESIEFGSNKLRQMPRGIFGKMPKLKQLNLWSNQLHNLTKHDFEGATSVLGIDIHDNGIEQLPHDVFAH
LTNVTDINLSANLFRSLPQGLFDHNKHLNEVRLMNNRVPLATLPSRLFANQPELQILRLRAELQSLPGDLFEHSTQITNI
SLGDNLLKTLPATLLEHQVNLLSLDLSNNRLTHLPDSLFAHTTNLTDLRLEDNLLTGISGDIFSNLGNLVTLVMSRNRLR
TIDSRAFVSTNGLRHLHLDHNDIDLQQPLLDIMLQTQINSPFGYMHGLLTLNLRNNSIIFVYNDWKNTMLQLRELDLSYN
NISSLGYEDLAFLSQNRLHVNMTHNKIRRIALPEDVHLGEGYNNNLVHVDLNDNPLVCDCTILWFIQLVRGVHKPQYSRQ
FKLRTDRLVCSQPNVLEGTPVRQIEPQTLICPLDFSDDPRERKCPRGCNCHVRTYDKALVINCHSGNLTHVPRLPNLHKN
MQLMELHLENNTLLRLPSANTPGYESVTSLHLAGNNLTSIDVDQLPTNLTHLDISWNHLQMLNATVLGFLNRTMKWRSVK
LSGNPWMCDCTAKPLLLFTQDNFERIGDRNEMMCVNAEMPTRMVELSTNDICPAE
;
28  ? 
2 UNP SPZ_DROME  P48607 2 
;VGGSDERFLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASI
KSDGELDVVQNSFKIPSCCKCALKTG
;
221 ? 
# 
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 4LXS A 1 ? 775 ? P08953 28  ? 802 ? 28 802 
2 2 4LXS J 1 ? 106 ? P48607 221 ? 326 ? 1  106 
3 2 4LXS K 1 ? 106 ? P48607 221 ? 326 ? 1  106 
# 
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 4LXS THR A 776 ? UNP P08953 ? ? 'EXPRESSION TAG' 803 1  
1 4LXS GLY A 777 ? UNP P08953 ? ? 'EXPRESSION TAG' 804 2  
1 4LXS HIS A 778 ? UNP P08953 ? ? 'EXPRESSION TAG' 805 3  
1 4LXS HIS A 779 ? UNP P08953 ? ? 'EXPRESSION TAG' 806 4  
1 4LXS HIS A 780 ? UNP P08953 ? ? 'EXPRESSION TAG' 807 5  
1 4LXS HIS A 781 ? UNP P08953 ? ? 'EXPRESSION TAG' 808 6  
1 4LXS HIS A 782 ? UNP P08953 ? ? 'EXPRESSION TAG' 809 7  
1 4LXS HIS A 783 ? UNP P08953 ? ? 'EXPRESSION TAG' 810 8  
2 4LXS LEU J 107 ? UNP P48607 ? ? 'EXPRESSION TAG' 107 9  
2 4LXS GLU J 108 ? UNP P48607 ? ? 'EXPRESSION TAG' 108 10 
2 4LXS HIS J 109 ? UNP P48607 ? ? 'EXPRESSION TAG' 109 11 
2 4LXS HIS J 110 ? UNP P48607 ? ? 'EXPRESSION TAG' 110 12 
2 4LXS HIS J 111 ? UNP P48607 ? ? 'EXPRESSION TAG' 111 13 
2 4LXS HIS J 112 ? UNP P48607 ? ? 'EXPRESSION TAG' 112 14 
2 4LXS HIS J 113 ? UNP P48607 ? ? 'EXPRESSION TAG' 113 15 
2 4LXS HIS J 114 ? UNP P48607 ? ? 'EXPRESSION TAG' 114 16 
3 4LXS LEU K 107 ? UNP P48607 ? ? 'EXPRESSION TAG' 107 17 
3 4LXS GLU K 108 ? UNP P48607 ? ? 'EXPRESSION TAG' 108 18 
3 4LXS HIS K 109 ? UNP P48607 ? ? 'EXPRESSION TAG' 109 19 
3 4LXS HIS K 110 ? UNP P48607 ? ? 'EXPRESSION TAG' 110 20 
3 4LXS HIS K 111 ? UNP P48607 ? ? 'EXPRESSION TAG' 111 21 
3 4LXS HIS K 112 ? UNP P48607 ? ? 'EXPRESSION TAG' 112 22 
3 4LXS HIS K 113 ? UNP P48607 ? ? 'EXPRESSION TAG' 113 23 
3 4LXS HIS K 114 ? UNP P48607 ? ? 'EXPRESSION TAG' 114 24 
# 
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 
CYS 'L-peptide linking' y CYSTEINE                                              ?     'C3 H7 N O2 S'   121.158 
EPE non-polymer         . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 
GLN 'L-peptide linking' y GLUTAMINE                                             ?     'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                       ?     'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                               ?     'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                             ?     'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE                                            ?     'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                               ?     'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                ?     'C6 H15 N2 O2 1' 147.195 
MAN D-saccharide        . ALPHA-D-MANNOSE                                       ?     'C6 H12 O6'      180.156 
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 
PRO 'L-peptide linking' y PROLINE                                               ?     'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                ?     'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                             ?     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                            ?     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                              ?     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                ?     'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4LXS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.84 
_exptl_crystal.density_percent_sol   56.67 
_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.temp            287 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'100 mM HEPES, 5% (v/v) propan-2-ol, 10% PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 287K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   2012-03-08 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'BESSY BL 14.2' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9184 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'BESSY BEAMLINE 14.2' 
_diffrn_source.pdbx_synchrotron_site       BESSY 
_diffrn_source.pdbx_synchrotron_beamline   14.2 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9184 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4LXS 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   2.0 
_reflns.d_resolution_low             34 
_reflns.d_resolution_high            3.3 
_reflns.number_obs                   18492 
_reflns.number_all                   19867 
_reflns.percent_possible_obs         93.1 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             3.3 
_reflns_shell.d_res_low              3.4 
_reflns_shell.percent_possible_all   80.3 
_reflns_shell.Rmerge_I_obs           0.498 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.8 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4LXS 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     18480 
_refine.ls_number_reflns_all                     18492 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             33.948 
_refine.ls_d_res_high                            3.300 
_refine.ls_percent_reflns_obs                    93.59 
_refine.ls_R_factor_obs                          0.2094 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2066 
_refine.ls_R_factor_R_free                       0.2636 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_number_reflns_R_free                  925 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            1.000 
_refine.occupancy_max                            1.000 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               34.8766 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 4LXR' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.49 
_refine.pdbx_overall_phase_error                 31.30 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6986 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         325 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7311 
_refine_hist.d_res_high                       3.300 
_refine_hist.d_res_low                        33.948 
# 
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 
f_bond_d           0.005  ? ? 7480  'X-RAY DIFFRACTION' ? 
f_angle_d          0.947  ? ? 10140 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 21.299 ? ? 2848  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.060  ? ? 1213  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 1277  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 3.30   3.4739  2205 0.3038 82.00 0.3906 . . 117 . . . . 
'X-RAY DIFFRACTION' . 3.4739 3.6913  2329 0.2474 89.00 0.3282 . . 123 . . . . 
'X-RAY DIFFRACTION' . 3.6913 3.9759  2508 0.2064 94.00 0.2428 . . 131 . . . . 
'X-RAY DIFFRACTION' . 3.9759 4.3752  2588 0.1796 97.00 0.2467 . . 136 . . . . 
'X-RAY DIFFRACTION' . 4.3752 5.0066  2620 0.1659 98.00 0.2339 . . 138 . . . . 
'X-RAY DIFFRACTION' . 5.0066 6.3012  2646 0.2235 98.00 0.2512 . . 139 . . . . 
'X-RAY DIFFRACTION' . 6.3012 33.9494 2659 0.2014 97.00 0.2569 . . 141 . . . . 
# 
_struct.entry_id                  4LXS 
_struct.title                     
'Structure of the Toll - Spatzle complex, a molecular hub in Drosophila development and innate immunity (glycosylated form)' 
_struct.pdbx_descriptor           'Protein toll, Protein spaetzle C-106' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4LXS 
_struct_keywords.text            
;TLR, LEUCINE-RICH REPEAT, IMMUNE SYSTEM, CYTOKINE RECEPTOR, EMBRYONIC DEVELOPMENT, INNATE IMMUNITY, RECEPTOR-LIGAND COMPLEX, IMMUNE SYSTEM-CYTOKINE complex
;
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM/CYTOKINE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 2 ? 
D  N N 3 ? 
E  N N 3 ? 
F  N N 4 ? 
G  N N 4 ? 
H  N N 5 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 6 ? 
# 
_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  GLY A 3   ? GLU A 9   ? GLY A 30  GLU A 36  1 ? 7  
HELX_P HELX_P2  2  ASP A 56  ? LEU A 63  ? ASP A 83  LEU A 90  5 ? 8  
HELX_P HELX_P3  3  PRO A 87  ? LEU A 95  ? PRO A 114 LEU A 122 1 ? 9  
HELX_P HELX_P4  4  THR A 115 ? ASP A 120 ? THR A 142 ASP A 147 5 ? 6  
HELX_P HELX_P5  5  PRO A 162 ? PHE A 166 ? PRO A 189 PHE A 193 5 ? 5  
HELX_P HELX_P6  6  THR A 210 ? GLU A 215 ? THR A 237 GLU A 242 5 ? 6  
HELX_P HELX_P7  7  PRO A 307 ? GLU A 312 ? PRO A 334 GLU A 339 5 ? 6  
HELX_P HELX_P8  8  PRO A 331 ? GLU A 336 ? PRO A 358 GLU A 363 5 ? 6  
HELX_P HELX_P9  9  SER A 404 ? VAL A 408 ? SER A 431 VAL A 435 5 ? 5  
HELX_P HELX_P10 10 PRO A 428 ? LEU A 434 ? PRO A 455 LEU A 461 1 ? 7  
HELX_P HELX_P11 11 ASN A 463 ? THR A 468 ? ASN A 490 THR A 495 1 ? 6  
HELX_P HELX_P12 12 ASP A 539 ? THR A 541 ? ASP A 566 THR A 568 5 ? 3  
HELX_P HELX_P13 13 ILE A 542 ? ARG A 550 ? ILE A 569 ARG A 577 1 ? 9  
HELX_P HELX_P14 14 GLN A 556 ? ARG A 559 ? GLN A 583 ARG A 586 5 ? 4  
HELX_P HELX_P15 15 GLY A 663 ? VAL A 667 ? GLY A 690 VAL A 694 5 ? 5  
HELX_P HELX_P16 16 ASN A 703 ? LEU A 710 ? ASN A 730 LEU A 737 1 ? 8  
HELX_P HELX_P17 17 ALA A 732 ? ASN A 742 ? ALA A 759 ASN A 769 1 ? 11 
HELX_P HELX_P18 18 ASP A 748 ? MET A 752 ? ASP A 775 MET A 779 5 ? 5  
HELX_P HELX_P19 19 ARG A 762 ? LEU A 766 ? ARG A 789 LEU A 793 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 7   SG  ? ? ? 1_555 A CYS 18  SG ? ? A CYS 34   A CYS 45   1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf2  disulf ? ? A CYS 16  SG  ? ? ? 1_555 A CYS 29  SG ? ? A CYS 43   A CYS 56   1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf3  disulf ? ? A CYS 52  SG  ? ? ? 1_555 A CYS 80  SG ? ? A CYS 79   A CYS 107  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf4  disulf ? ? A CYS 538 SG  ? ? ? 1_555 A CYS 570 SG ? ? A CYS 565  A CYS 597  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf5  disulf ? ? A CYS 540 SG  ? ? ? 1_555 A CYS 591 SG ? ? A CYS 567  A CYS 618  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf6  disulf ? ? A CYS 604 SG  ? ? ? 1_555 A CYS 610 SG ? ? A CYS 631  A CYS 637  1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf7  disulf ? ? A CYS 608 SG  ? ? ? 1_555 A CYS 623 SG ? ? A CYS 635  A CYS 650  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf8  disulf ? ? A CYS 728 SG  ? ? ? 1_555 A CYS 754 SG ? ? A CYS 755  A CYS 781  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf9  disulf ? ? A CYS 730 SG  ? ? ? 1_555 A CYS 772 SG ? ? A CYS 757  A CYS 799  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf10 disulf ? ? B CYS 10  SG  ? ? ? 1_555 B CYS 68  SG ? ? J CYS 10   J CYS 68   1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf11 disulf ? ? B CYS 47  SG  ? ? ? 1_555 B CYS 99  SG ? ? J CYS 47   J CYS 99   1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf12 disulf ? ? B CYS 54  SG  ? ? ? 1_555 B CYS 101 SG ? ? J CYS 54   J CYS 101  1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf13 disulf ? ? B CYS 98  SG  ? ? ? 1_555 C CYS 98  SG ? ? J CYS 98   K CYS 98   1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf14 disulf ? ? C CYS 10  SG  ? ? ? 1_555 C CYS 68  SG ? ? K CYS 10   K CYS 68   1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf15 disulf ? ? C CYS 47  SG  ? ? ? 1_555 C CYS 99  SG ? ? K CYS 47   K CYS 99   1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf16 disulf ? ? C CYS 54  SG  ? ? ? 1_555 C CYS 101 SG ? ? K CYS 54   K CYS 101  1_555 ? ? ? ? ? ? ? 2.035 ? 
covale1  covale ? ? E NAG .   O4  ? ? ? 1_555 F BMA .   C1 ? ? A NAG 2002 A BMA 2003 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale2  covale ? ? A ASN 364 ND2 ? ? ? 1_555 V NAG .   C1 ? ? A ASN 391  A NAG 2019 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale3  covale ? ? A ASN 676 ND2 ? ? ? 1_555 T NAG .   C1 ? ? A ASN 703  A NAG 2017 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale4  covale ? ? T NAG .   O4  ? ? ? 1_555 U NAG .   C1 ? ? A NAG 2017 A NAG 2018 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale5  covale ? ? F BMA .   O3  ? ? ? 1_555 G BMA .   C1 ? ? A BMA 2003 A BMA 2004 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale6  covale ? ? G BMA .   O3  ? ? ? 1_555 H MAN .   C1 ? ? A BMA 2004 A MAN 2005 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale7  covale ? ? A ASN 53  ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 80   A NAG 2007 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale8  covale ? ? A ASN 148 ND2 ? ? ? 1_555 Y NAG .   C1 ? ? A ASN 175  A NAG 2022 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale9  covale ? ? A ASN 501 ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 528  A NAG 2010 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale10 covale ? ? K NAG .   O4  ? ? ? 1_555 L NAG .   C1 ? ? A NAG 2008 A NAG 2009 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale11 covale ? ? N NAG .   O4  ? ? ? 1_555 O BMA .   C1 ? ? A NAG 2011 A BMA 2012 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale12 covale ? ? A ASN 243 ND2 ? ? ? 1_555 R NAG .   C1 ? ? A ASN 270  A NAG 2015 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale13 covale ? ? A ASN 208 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 235  A NAG 2006 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale14 covale ? ? A ASN 113 ND2 ? ? ? 1_555 P NAG .   C1 ? ? A ASN 140  A NAG 2013 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale15 covale ? ? A ASN 319 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 346  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale16 covale ? ? A ASN 455 ND2 ? ? ? 1_555 K NAG .   C1 ? ? A ASN 482  A NAG 2008 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale17 covale ? ? M NAG .   O4  ? ? ? 1_555 N NAG .   C1 ? ? A NAG 2010 A NAG 2011 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale18 covale ? ? R NAG .   O4  ? ? ? 1_555 S NAG .   C1 ? ? A NAG 2015 A NAG 2016 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale19 covale ? ? A ASN 627 ND2 ? ? ? 1_555 Z NAG .   C1 ? ? A ASN 654  A NAG 2023 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale20 covale ? ? P NAG .   O4  ? ? ? 1_555 Q NAG .   C1 ? ? A NAG 2013 A NAG 2014 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale21 covale ? ? A ASN 481 ND2 ? ? ? 1_555 X NAG .   C1 ? ? A ASN 508  A NAG 2021 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale22 covale ? ? V NAG .   O4  ? ? ? 1_555 W NAG .   C1 ? ? A NAG 2019 A NAG 2020 1_555 ? ? ? ? ? ? ? 1.453 ? 
covale23 covale ? ? D NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? A NAG 2001 A NAG 2002 1_555 ? ? ? ? ? ? ? 1.459 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 ASP 13  A . ? ASP 40  A GLY 14  A ? GLY 41  A 1 -3.02 
2 CYS 29  A . ? CYS 56  A PRO 30  A ? PRO 57  A 1 -2.12 
3 GLN 572 A . ? GLN 599 A PRO 573 A ? PRO 600 A 1 1.10  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 15 ? 
B ? 2  ? 
C ? 9  ? 
D ? 2  ? 
E ? 5  ? 
F ? 2  ? 
G ? 2  ? 
H ? 3  ? 
I ? 2  ? 
J ? 2  ? 
# 
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  ? parallel      
A 5  6  ? parallel      
A 6  7  ? parallel      
A 7  8  ? parallel      
A 8  9  ? parallel      
A 9  10 ? parallel      
A 10 11 ? parallel      
A 11 12 ? parallel      
A 12 13 ? parallel      
A 13 14 ? parallel      
A 14 15 ? parallel      
B 1  2  ? parallel      
C 1  2  ? parallel      
C 2  3  ? parallel      
C 3  4  ? parallel      
C 4  5  ? parallel      
C 5  6  ? parallel      
C 6  7  ? parallel      
C 7  8  ? parallel      
C 8  9  ? parallel      
D 1  2  ? parallel      
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? parallel      
E 4  5  ? parallel      
F 1  2  ? parallel      
G 1  2  ? anti-parallel 
H 1  2  ? anti-parallel 
H 2  3  ? anti-parallel 
I 1  2  ? anti-parallel 
J 1  2  ? 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  PRO A 20  ? ILE A 21  ? PRO A 47  ILE A 48  
A 2  GLU A 24  ? GLU A 26  ? GLU A 51  GLU A 53  
A 3  PHE A 38  ? GLN A 43  ? PHE A 65  GLN A 70  
A 4  TYR A 47  ? CYS A 52  ? TYR A 74  CYS A 79  
A 5  ARG A 74  ? ARG A 78  ? ARG A 101 ARG A 105 
A 6  THR A 102 ? GLU A 106 ? THR A 129 GLU A 133 
A 7  ARG A 127 ? THR A 131 ? ARG A 154 THR A 158 
A 8  HIS A 151 ? ARG A 155 ? HIS A 178 ARG A 182 
A 9  SER A 174 ? GLU A 176 ? SER A 201 GLU A 203 
A 10 GLN A 198 ? ASN A 200 ? GLN A 225 ASN A 227 
A 11 GLY A 222 ? ASP A 224 ? GLY A 249 ASP A 251 
A 12 ASP A 246 ? ASN A 248 ? ASP A 273 ASN A 275 
A 13 GLU A 270 ? LEU A 273 ? GLU A 297 LEU A 300 
A 14 ILE A 296 ? LEU A 299 ? ILE A 323 LEU A 326 
A 15 ILE A 320 ? SER A 321 ? ILE A 347 SER A 348 
B 1  GLY A 70  ? GLU A 71  ? GLY A 97  GLU A 98  
B 2  ILE A 97  ? VAL A 98  ? ILE A 124 VAL A 125 
C 1  SER A 343 ? ASP A 345 ? SER A 370 ASP A 372 
C 2  ASP A 367 ? ARG A 369 ? ASP A 394 ARG A 396 
C 3  THR A 391 ? VAL A 393 ? THR A 418 VAL A 420 
C 4  HIS A 415 ? HIS A 417 ? HIS A 442 HIS A 444 
C 5  THR A 450 ? ASN A 452 ? THR A 477 ASN A 479 
C 6  GLU A 474 ? ASP A 476 ? GLU A 501 ASP A 503 
C 7  LEU A 498 ? ASN A 501 ? LEU A 525 ASN A 528 
C 8  VAL A 527 ? ASP A 530 ? VAL A 554 ASP A 557 
C 9  PHE A 561 ? ARG A 564 ? PHE A 588 ARG A 591 
D 1  SER A 484 ? GLY A 486 ? SER A 511 GLY A 513 
D 2  ARG A 509 ? ALA A 511 ? ARG A 536 ALA A 538 
E 1  ILE A 590 ? CYS A 591 ? ILE A 617 CYS A 618 
E 2  ASN A 609 ? ARG A 613 ? ASN A 636 ARG A 640 
E 3  ALA A 618 ? ASN A 622 ? ALA A 645 ASN A 649 
E 4  LEU A 643 ? HIS A 647 ? LEU A 670 HIS A 674 
E 5  SER A 669 ? HIS A 671 ? SER A 696 HIS A 698 
F 1  HIS A 691 ? ASP A 693 ? HIS A 718 ASP A 720 
F 2  SER A 718 ? LYS A 720 ? SER A 745 LYS A 747 
G 1  LYS B 15  ? LEU B 16  ? LYS J 15  LEU J 16  
G 2  GLN B 43  ? ILE B 44  ? GLN J 43  ILE J 44  
H 1  ASN B 65  ? THR B 73  ? ASN J 65  THR J 73  
H 2  ILE B 95  ? LYS B 104 ? ILE J 95  LYS J 104 
H 3  GLU C 6   ? PHE C 8   ? GLU K 6   PHE K 8   
I 1  SER C 12  ? LYS C 15  ? SER K 12  LYS K 15  
I 2  ILE C 44  ? CYS C 47  ? ILE K 44  CYS K 47  
J 1  ILE C 67  ? TYR C 72  ? ILE K 67  TYR K 72  
J 2  PRO C 96  ? ALA C 102 ? PRO K 96  ALA K 102 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1  2  N ILE A 21  ? N ILE A 48  O GLU A 24  ? O GLU A 51  
A 2  3  N TYR A 25  ? N TYR A 52  O ILE A 42  ? O ILE A 69  
A 3  4  N THR A 41  ? N THR A 68  O GLN A 49  ? O GLN A 76  
A 4  5  N ILE A 50  ? N ILE A 77  O GLN A 76  ? O GLN A 103 
A 5  6  N VAL A 75  ? N VAL A 102 O THR A 102 ? O THR A 129 
A 6  7  N PHE A 105 ? N PHE A 132 O ARG A 129 ? O ARG A 156 
A 7  8  N PHE A 130 ? N PHE A 157 O ARG A 155 ? O ARG A 182 
A 8  9  N LEU A 152 ? N LEU A 179 O GLU A 176 ? O GLU A 203 
A 9  10 N ILE A 175 ? N ILE A 202 O ASN A 200 ? O ASN A 227 
A 10 11 N LEU A 199 ? N LEU A 226 O GLY A 222 ? O GLY A 249 
A 11 12 N ILE A 223 ? N ILE A 250 O ASP A 246 ? O ASP A 273 
A 12 13 N ILE A 247 ? N ILE A 274 O GLU A 270 ? O GLU A 297 
A 13 14 N LEU A 273 ? N LEU A 300 O ARG A 298 ? O ARG A 325 
A 14 15 N LEU A 299 ? N LEU A 326 O SER A 321 ? O SER A 348 
B 1  2  N GLY A 70  ? N GLY A 97  O VAL A 98  ? O VAL A 125 
C 1  2  N LEU A 344 ? N LEU A 371 O ARG A 369 ? O ARG A 396 
C 2  3  N LEU A 368 ? N LEU A 395 O VAL A 393 ? O VAL A 420 
C 3  4  N LEU A 392 ? N LEU A 419 O HIS A 415 ? O HIS A 442 
C 4  5  N LEU A 416 ? N LEU A 443 O THR A 450 ? O THR A 477 
C 5  6  N LEU A 451 ? N LEU A 478 O GLU A 474 ? O GLU A 501 
C 6  7  N LEU A 475 ? N LEU A 502 O ASN A 501 ? O ASN A 528 
C 7  8  N LEU A 498 ? N LEU A 525 O HIS A 528 ? O HIS A 555 
C 8  9  N VAL A 527 ? N VAL A 554 O LYS A 562 ? O LYS A 589 
D 1  2  N LEU A 485 ? N LEU A 512 O ALA A 511 ? O ALA A 538 
E 1  2  N CYS A 591 ? N CYS A 618 O VAL A 612 ? O VAL A 639 
E 2  3  N ASN A 609 ? N ASN A 636 O ASN A 622 ? O ASN A 649 
E 3  4  N LEU A 619 ? N LEU A 646 O LEU A 643 ? O LEU A 670 
E 4  5  N MET A 644 ? N MET A 671 O SER A 669 ? O SER A 696 
F 1  2  N LEU A 692 ? N LEU A 719 O LYS A 720 ? O LYS A 747 
G 1  2  N LYS B 15  ? N LYS J 15  O ILE B 44  ? O ILE J 44  
H 1  2  N LYS B 69  ? N LYS J 69  O LYS B 100 ? O LYS J 100 
H 2  3  N LEU B 103 ? N LEU J 103 O ARG C 7   ? O ARG K 7   
I 1  2  N ILE C 13  ? N ILE K 13  O GLU C 46  ? O GLU K 46  
J 1  2  N LYS C 69  ? N LYS K 69  O LYS C 100 ? O LYS K 100 
# 
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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE EPE A 2024'                                        
AC2 Software ? ? ? ? 3  'BINDING SITE FOR MONO-SACCHARIDE NAG A2007 BOUND TO ASN A 80'               
AC3 Software ? ? ? ? 3  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 140 RESIDUES 2013 TO 2014' 
AC4 Software ? ? ? ? 5  'BINDING SITE FOR MONO-SACCHARIDE NAG A2022 BOUND TO ASN A 175'              
AC5 Software ? ? ? ? 2  'BINDING SITE FOR MONO-SACCHARIDE NAG A2006 BOUND TO ASN A 235'              
AC6 Software ? ? ? ? 6  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 270 RESIDUES 2015 TO 2016' 
AC7 Software ? ? ? ? 9  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 346 RESIDUES 2001 TO 2005' 
AC8 Software ? ? ? ? 3  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 391 RESIDUES 2019 TO 2020' 
AC9 Software ? ? ? ? 5  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 482 RESIDUES 2008 TO 2009' 
BC1 Software ? ? ? ? 2  'BINDING SITE FOR MONO-SACCHARIDE NAG A2021 BOUND TO ASN A 508'              
BC2 Software ? ? ? ? 6  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 528 RESIDUES 2010 TO 2012' 
BC3 Software ? ? ? ? 4  'BINDING SITE FOR MONO-SACCHARIDE NAG A2023 BOUND TO ASN A 654'              
BC4 Software ? ? ? ? 3  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 703 RESIDUES 2017 TO 2018' 
# 
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 10 ARG A 133 ? ARG A 160  . ? 1_555 ? 
2  AC1 10 ASN A 157 ? ASN A 184  . ? 1_555 ? 
3  AC1 10 ASN A 180 ? ASN A 207  . ? 1_555 ? 
4  AC1 10 SER A 203 ? SER A 230  . ? 1_555 ? 
5  AC1 10 ASN A 204 ? ASN A 231  . ? 1_555 ? 
6  AC1 10 GLN A 205 ? GLN A 232  . ? 1_555 ? 
7  AC1 10 ARG A 749 ? ARG A 776  . ? 2_556 ? 
8  AC1 10 ASN A 750 ? ASN A 777  . ? 2_556 ? 
9  AC1 10 ARG A 762 ? ARG A 789  . ? 2_556 ? 
10 AC1 10 VAL A 764 ? VAL A 791  . ? 2_556 ? 
11 AC2 3  ASN A 35  ? ASN A 62   . ? 1_555 ? 
12 AC2 3  ASN A 53  ? ASN A 80   . ? 1_555 ? 
13 AC2 3  ARG A 79  ? ARG A 106  . ? 1_555 ? 
14 AC3 3  MET A 112 ? MET A 139  . ? 1_555 ? 
15 AC3 3  ASN A 113 ? ASN A 140  . ? 1_555 ? 
16 AC3 3  ARG A 187 ? ARG A 214  . ? 2_455 ? 
17 AC4 5  HIS A 123 ? HIS A 150  . ? 1_555 ? 
18 AC4 5  GLY A 124 ? GLY A 151  . ? 1_555 ? 
19 AC4 5  ASN A 148 ? ASN A 175  . ? 1_555 ? 
20 AC4 5  ASP A 381 ? ASP A 408  . ? 4_455 ? 
21 AC4 5  ARG A 405 ? ARG A 432  . ? 4_455 ? 
22 AC5 2  ASN A 208 ? ASN A 235  . ? 1_555 ? 
23 AC5 2  GLU A 231 ? GLU A 258  . ? 1_555 ? 
24 AC6 6  THR A 242 ? THR A 269  . ? 1_555 ? 
25 AC6 6  ASN A 243 ? ASN A 270  . ? 1_555 ? 
26 AC6 6  THR A 376 ? THR A 403  . ? 4_455 ? 
27 AC6 6  ARG A 398 ? ARG A 425  . ? 4_455 ? 
28 AC6 6  ASP A 422 ? ASP A 449  . ? 4_455 ? 
29 AC6 6  NAG L .   ? NAG A 2009 . ? 4_455 ? 
30 AC7 9  ILE A 296 ? ILE A 323  . ? 1_555 ? 
31 AC7 9  ARG A 298 ? ARG A 325  . ? 1_555 ? 
32 AC7 9  ASN A 319 ? ASN A 346  . ? 1_555 ? 
33 AC7 9  SER A 343 ? SER A 370  . ? 1_555 ? 
34 AC7 9  ASP A 367 ? ASP A 394  . ? 1_555 ? 
35 AC7 9  GLU B 48  ? GLU J 48   . ? 1_555 ? 
36 AC7 9  GLY B 49  ? GLY J 49   . ? 1_555 ? 
37 AC7 9  ALA B 50  ? ALA J 50   . ? 1_555 ? 
38 AC7 9  GLN B 52  ? GLN J 52   . ? 1_555 ? 
39 AC8 3  ASN A 340 ? ASN A 367  . ? 1_555 ? 
40 AC8 3  THR A 363 ? THR A 390  . ? 1_555 ? 
41 AC8 3  ASN A 364 ? ASN A 391  . ? 1_555 ? 
42 AC9 5  ARG A 398 ? ARG A 425  . ? 1_555 ? 
43 AC9 5  HIS A 420 ? HIS A 447  . ? 1_555 ? 
44 AC9 5  ASN A 455 ? ASN A 482  . ? 1_555 ? 
45 AC9 5  TYR A 479 ? TYR A 506  . ? 1_555 ? 
46 AC9 5  NAG S .   ? NAG A 2016 . ? 4_445 ? 
47 BC1 2  SER A 457 ? SER A 484  . ? 1_555 ? 
48 BC1 2  ASN A 481 ? ASN A 508  . ? 1_555 ? 
49 BC2 6  ARG A 454 ? ARG A 481  . ? 1_555 ? 
50 BC2 6  ASN A 501 ? ASN A 528  . ? 1_555 ? 
51 BC2 6  THR A 503 ? THR A 530  . ? 1_555 ? 
52 BC2 6  HIS A 504 ? HIS A 531  . ? 1_555 ? 
53 BC2 6  ASP A 530 ? ASP A 557  . ? 1_555 ? 
54 BC2 6  ARG A 567 ? ARG A 594  . ? 1_555 ? 
55 BC3 4  ASP A 5   ? ASP A 32   . ? 2_546 ? 
56 BC3 4  SER A 625 ? SER A 652  . ? 1_555 ? 
57 BC3 4  ASN A 627 ? ASN A 654  . ? 1_555 ? 
58 BC3 4  LEU A 628 ? LEU A 655  . ? 1_555 ? 
59 BC4 3  GLU A 71  ? GLU A 98   . ? 2_546 ? 
60 BC4 3  ASN A 676 ? ASN A 703  . ? 1_555 ? 
61 BC4 3  HIS A 698 ? HIS A 725  . ? 1_555 ? 
# 
_atom_sites.entry_id                    4LXS 
_atom_sites.fract_transf_matrix[1][1]   0.005838 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004287 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013017 
_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]   0.010020 
_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 
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   . SER A  1 1   ? -68.395 7.349   25.209  1.00 32.75  ? 28   SER A N   1 
ATOM   2    C CA  . SER A  1 1   ? -69.801 6.963   25.212  1.00 40.54  ? 28   SER A CA  1 
ATOM   3    C C   . SER A  1 1   ? -70.158 6.232   26.494  1.00 36.91  ? 28   SER A C   1 
ATOM   4    O O   . SER A  1 1   ? -71.049 6.649   27.232  1.00 40.85  ? 28   SER A O   1 
ATOM   5    C CB  . SER A  1 1   ? -70.123 6.075   24.009  1.00 41.04  ? 28   SER A CB  1 
ATOM   6    O OG  . SER A  1 1   ? -70.057 6.798   22.790  1.00 39.62  ? 28   SER A OG  1 
ATOM   7    N N   . PHE A  1 2   ? -69.469 5.125   26.745  1.00 32.68  ? 29   PHE A N   1 
ATOM   8    C CA  . PHE A  1 2   ? -69.631 4.403   27.995  1.00 34.83  ? 29   PHE A CA  1 
ATOM   9    C C   . PHE A  1 2   ? -68.273 4.175   28.624  1.00 39.84  ? 29   PHE A C   1 
ATOM   10   O O   . PHE A  1 2   ? -67.425 3.492   28.052  1.00 39.31  ? 29   PHE A O   1 
ATOM   11   C CB  . PHE A  1 2   ? -70.326 3.063   27.771  1.00 32.65  ? 29   PHE A CB  1 
ATOM   12   C CG  . PHE A  1 2   ? -70.415 2.217   29.009  1.00 33.61  ? 29   PHE A CG  1 
ATOM   13   C CD1 . PHE A  1 2   ? -71.455 2.388   29.906  1.00 33.80  ? 29   PHE A CD1 1 
ATOM   14   C CD2 . PHE A  1 2   ? -69.460 1.251   29.276  1.00 29.29  ? 29   PHE A CD2 1 
ATOM   15   C CE1 . PHE A  1 2   ? -71.540 1.614   31.044  1.00 30.09  ? 29   PHE A CE1 1 
ATOM   16   C CE2 . PHE A  1 2   ? -69.541 0.477   30.412  1.00 30.44  ? 29   PHE A CE2 1 
ATOM   17   C CZ  . PHE A  1 2   ? -70.582 0.658   31.297  1.00 29.71  ? 29   PHE A CZ  1 
ATOM   18   N N   . GLY A  1 3   ? -68.069 4.745   29.805  1.00 49.03  ? 30   GLY A N   1 
ATOM   19   C CA  . GLY A  1 3   ? -66.799 4.606   30.492  1.00 60.85  ? 30   GLY A CA  1 
ATOM   20   C C   . GLY A  1 3   ? -66.934 4.254   31.960  1.00 58.73  ? 30   GLY A C   1 
ATOM   21   O O   . GLY A  1 3   ? -68.011 3.880   32.431  1.00 57.68  ? 30   GLY A O   1 
ATOM   22   N N   . ARG A  1 4   ? -65.823 4.382   32.679  1.00 56.36  ? 31   ARG A N   1 
ATOM   23   C CA  . ARG A  1 4   ? -65.761 4.106   34.111  1.00 64.01  ? 31   ARG A CA  1 
ATOM   24   C C   . ARG A  1 4   ? -66.814 4.878   34.892  1.00 59.69  ? 31   ARG A C   1 
ATOM   25   O O   . ARG A  1 4   ? -67.300 4.419   35.928  1.00 57.36  ? 31   ARG A O   1 
ATOM   26   C CB  . ARG A  1 4   ? -64.369 4.466   34.633  1.00 74.27  ? 31   ARG A CB  1 
ATOM   27   C CG  . ARG A  1 4   ? -64.185 4.352   36.137  1.00 67.03  ? 31   ARG A CG  1 
ATOM   28   C CD  . ARG A  1 4   ? -62.738 4.635   36.525  1.00 79.51  ? 31   ARG A CD  1 
ATOM   29   N NE  . ARG A  1 4   ? -61.835 3.539   36.169  1.00 90.13  ? 31   ARG A NE  1 
ATOM   30   C CZ  . ARG A  1 4   ? -61.230 3.406   34.990  1.00 87.83  ? 31   ARG A CZ  1 
ATOM   31   N NH1 . ARG A  1 4   ? -61.432 4.299   34.028  1.00 81.92  1 31   ARG A NH1 1 
ATOM   32   N NH2 . ARG A  1 4   ? -60.427 2.373   34.769  1.00 84.25  ? 31   ARG A NH2 1 
ATOM   33   N N   . ASP A  1 5   ? -67.165 6.054   34.384  1.00 55.30  ? 32   ASP A N   1 
ATOM   34   C CA  . ASP A  1 5   ? -68.102 6.917   35.077  1.00 53.97  ? 32   ASP A CA  1 
ATOM   35   C C   . ASP A  1 5   ? -69.499 6.311   35.102  1.00 50.35  ? 32   ASP A C   1 
ATOM   36   O O   . ASP A  1 5   ? -70.154 6.285   36.143  1.00 53.77  ? 32   ASP A O   1 
ATOM   37   C CB  . ASP A  1 5   ? -68.132 8.296   34.434  1.00 54.03  ? 32   ASP A CB  1 
ATOM   38   C CG  . ASP A  1 5   ? -68.871 9.300   35.278  1.00 62.25  ? 32   ASP A CG  1 
ATOM   39   O OD1 . ASP A  1 5   ? -68.487 9.492   36.452  1.00 58.35  ? 32   ASP A OD1 1 
ATOM   40   O OD2 . ASP A  1 5   ? -69.855 9.876   34.775  1.00 65.94  1 32   ASP A OD2 1 
ATOM   41   N N   . ALA A  1 6   ? -69.946 5.821   33.952  1.00 47.46  ? 33   ALA A N   1 
ATOM   42   C CA  . ALA A  1 6   ? -71.244 5.168   33.855  1.00 45.67  ? 33   ALA A CA  1 
ATOM   43   C C   . ALA A  1 6   ? -71.220 3.874   34.653  1.00 45.13  ? 33   ALA A C   1 
ATOM   44   O O   . ALA A  1 6   ? -72.215 3.469   35.259  1.00 43.90  ? 33   ALA A O   1 
ATOM   45   C CB  . ALA A  1 6   ? -71.571 4.884   32.407  1.00 41.71  ? 33   ALA A CB  1 
ATOM   46   N N   . CYS A  1 7   ? -70.054 3.243   34.648  1.00 46.75  ? 34   CYS A N   1 
ATOM   47   C CA  . CYS A  1 7   ? -69.838 1.955   35.285  1.00 45.65  ? 34   CYS A CA  1 
ATOM   48   C C   . CYS A  1 7   ? -70.119 2.003   36.788  1.00 52.06  ? 34   CYS A C   1 
ATOM   49   O O   . CYS A  1 7   ? -70.811 1.140   37.329  1.00 55.02  ? 34   CYS A O   1 
ATOM   50   C CB  . CYS A  1 7   ? -68.397 1.512   35.023  1.00 45.55  ? 34   CYS A CB  1 
ATOM   51   S SG  . CYS A  1 7   ? -68.026 -0.200  35.401  1.00 39.76  ? 34   CYS A SG  1 
ATOM   52   N N   . SER A  1 8   ? -69.585 3.022   37.451  1.00 52.80  ? 35   SER A N   1 
ATOM   53   C CA  . SER A  1 8   ? -69.723 3.170   38.895  1.00 52.49  ? 35   SER A CA  1 
ATOM   54   C C   . SER A  1 8   ? -71.182 3.307   39.327  1.00 56.56  ? 35   SER A C   1 
ATOM   55   O O   . SER A  1 8   ? -71.566 2.864   40.410  1.00 63.39  ? 35   SER A O   1 
ATOM   56   C CB  . SER A  1 8   ? -68.935 4.391   39.362  1.00 62.31  ? 35   SER A CB  1 
ATOM   57   O OG  . SER A  1 8   ? -69.415 5.564   38.729  1.00 60.90  ? 35   SER A OG  1 
ATOM   58   N N   . GLU A  1 9   ? -71.989 3.922   38.472  1.00 52.10  ? 36   GLU A N   1 
ATOM   59   C CA  . GLU A  1 9   ? -73.392 4.154   38.780  1.00 52.80  ? 36   GLU A CA  1 
ATOM   60   C C   . GLU A  1 9   ? -74.208 2.868   38.674  1.00 56.63  ? 36   GLU A C   1 
ATOM   61   O O   . GLU A  1 9   ? -73.926 1.997   37.851  1.00 52.25  ? 36   GLU A O   1 
ATOM   62   C CB  . GLU A  1 9   ? -73.953 5.219   37.844  1.00 55.38  ? 36   GLU A CB  1 
ATOM   63   C CG  . GLU A  1 9   ? -73.077 6.458   37.748  1.00 57.41  ? 36   GLU A CG  1 
ATOM   64   C CD  . GLU A  1 9   ? -73.492 7.381   36.619  1.00 63.99  ? 36   GLU A CD  1 
ATOM   65   O OE1 . GLU A  1 9   ? -72.863 8.448   36.459  1.00 63.75  ? 36   GLU A OE1 1 
ATOM   66   O OE2 . GLU A  1 9   ? -74.447 7.037   35.889  1.00 69.97  1 36   GLU A OE2 1 
ATOM   67   N N   . ASP A  1 13  ? -77.689 1.137   39.392  1.00 62.90  ? 40   ASP A N   1 
ATOM   68   C CA  . ASP A  1 13  ? -77.545 1.677   40.739  1.00 76.05  ? 40   ASP A CA  1 
ATOM   69   C C   . ASP A  1 13  ? -78.890 1.959   41.415  1.00 81.41  ? 40   ASP A C   1 
ATOM   70   O O   . ASP A  1 13  ? -79.326 3.109   41.469  1.00 78.52  ? 40   ASP A O   1 
ATOM   71   C CB  . ASP A  1 13  ? -76.728 2.966   40.688  1.00 74.86  ? 40   ASP A CB  1 
ATOM   72   C CG  . ASP A  1 13  ? -76.432 3.524   42.059  1.00 89.28  ? 40   ASP A CG  1 
ATOM   73   O OD1 . ASP A  1 13  ? -76.284 2.725   43.008  1.00 96.46  1 40   ASP A OD1 1 
ATOM   74   O OD2 . ASP A  1 13  ? -76.348 4.763   42.186  1.00 89.55  ? 40   ASP A OD2 1 
ATOM   75   N N   . GLY A  1 14  ? -79.550 0.924   41.930  1.00 79.09  ? 41   GLY A N   1 
ATOM   76   C CA  . GLY A  1 14  ? -79.084 -0.445  41.821  1.00 74.20  ? 41   GLY A CA  1 
ATOM   77   C C   . GLY A  1 14  ? -79.848 -1.179  40.736  1.00 73.28  ? 41   GLY A C   1 
ATOM   78   O O   . GLY A  1 14  ? -80.939 -1.697  40.967  1.00 74.73  ? 41   GLY A O   1 
ATOM   79   N N   . LEU A  1 15  ? -79.271 -1.204  39.542  1.00 66.09  ? 42   LEU A N   1 
ATOM   80   C CA  . LEU A  1 15  ? -79.851 -1.892  38.400  1.00 56.66  ? 42   LEU A CA  1 
ATOM   81   C C   . LEU A  1 15  ? -79.074 -3.183  38.213  1.00 51.21  ? 42   LEU A C   1 
ATOM   82   O O   . LEU A  1 15  ? -79.452 -4.241  38.719  1.00 42.50  ? 42   LEU A O   1 
ATOM   83   C CB  . LEU A  1 15  ? -79.719 -1.005  37.157  1.00 60.99  ? 42   LEU A CB  1 
ATOM   84   C CG  . LEU A  1 15  ? -80.059 -1.509  35.749  1.00 67.82  ? 42   LEU A CG  1 
ATOM   85   C CD1 . LEU A  1 15  ? -81.561 -1.491  35.466  1.00 53.18  ? 42   LEU A CD1 1 
ATOM   86   C CD2 . LEU A  1 15  ? -79.284 -0.701  34.707  1.00 55.66  ? 42   LEU A CD2 1 
ATOM   87   N N   . CYS A  1 16  ? -77.970 -3.074  37.488  1.00 47.54  ? 43   CYS A N   1 
ATOM   88   C CA  . CYS A  1 16  ? -77.022 -4.155  37.340  1.00 40.15  ? 43   CYS A CA  1 
ATOM   89   C C   . CYS A  1 16  ? -75.713 -3.542  37.764  1.00 38.04  ? 43   CYS A C   1 
ATOM   90   O O   . CYS A  1 16  ? -75.538 -2.328  37.649  1.00 45.52  ? 43   CYS A O   1 
ATOM   91   C CB  . CYS A  1 16  ? -76.941 -4.588  35.880  1.00 41.07  ? 43   CYS A CB  1 
ATOM   92   S SG  . CYS A  1 16  ? -78.490 -5.225  35.206  1.00 49.88  ? 43   CYS A SG  1 
ATOM   93   N N   . GLN A  1 17  ? -74.791 -4.353  38.263  1.00 31.17  ? 44   GLN A N   1 
ATOM   94   C CA  . GLN A  1 17  ? -73.522 -3.805  38.721  1.00 38.65  ? 44   GLN A CA  1 
ATOM   95   C C   . GLN A  1 17  ? -72.435 -3.878  37.657  1.00 33.31  ? 44   GLN A C   1 
ATOM   96   O O   . GLN A  1 17  ? -72.309 -4.868  36.943  1.00 33.09  ? 44   GLN A O   1 
ATOM   97   C CB  . GLN A  1 17  ? -73.057 -4.491  40.003  1.00 40.05  ? 44   GLN A CB  1 
ATOM   98   C CG  . GLN A  1 17  ? -72.651 -5.937  39.821  1.00 40.62  ? 44   GLN A CG  1 
ATOM   99   C CD  . GLN A  1 17  ? -72.261 -6.581  41.126  1.00 36.53  ? 44   GLN A CD  1 
ATOM   100  O OE1 . GLN A  1 17  ? -72.378 -5.970  42.185  1.00 38.94  ? 44   GLN A OE1 1 
ATOM   101  N NE2 . GLN A  1 17  ? -71.800 -7.823  41.061  1.00 37.70  ? 44   GLN A NE2 1 
ATOM   102  N N   . CYS A  1 18  ? -71.654 -2.811  37.557  1.00 29.50  ? 45   CYS A N   1 
ATOM   103  C CA  . CYS A  1 18  ? -70.535 -2.770  36.637  1.00 27.02  ? 45   CYS A CA  1 
ATOM   104  C C   . CYS A  1 18  ? -69.240 -2.643  37.425  1.00 37.70  ? 45   CYS A C   1 
ATOM   105  O O   . CYS A  1 18  ? -69.211 -2.042  38.498  1.00 44.84  ? 45   CYS A O   1 
ATOM   106  C CB  . CYS A  1 18  ? -70.689 -1.593  35.679  1.00 35.29  ? 45   CYS A CB  1 
ATOM   107  S SG  . CYS A  1 18  ? -69.351 -1.420  34.476  1.00 47.98  ? 45   CYS A SG  1 
ATOM   108  N N   . ALA A  1 19  ? -68.168 -3.208  36.889  1.00 34.41  ? 46   ALA A N   1 
ATOM   109  C CA  . ALA A  1 19  ? -66.877 -3.167  37.556  1.00 34.34  ? 46   ALA A CA  1 
ATOM   110  C C   . ALA A  1 19  ? -65.764 -3.227  36.523  1.00 41.98  ? 46   ALA A C   1 
ATOM   111  O O   . ALA A  1 19  ? -65.565 -4.259  35.889  1.00 46.67  ? 46   ALA A O   1 
ATOM   112  C CB  . ALA A  1 19  ? -66.758 -4.320  38.533  1.00 34.05  ? 46   ALA A CB  1 
ATOM   113  N N   . PRO A  1 20  ? -65.030 -2.119  36.352  1.00 45.26  ? 47   PRO A N   1 
ATOM   114  C CA  . PRO A  1 20  ? -64.003 -2.035  35.307  1.00 45.37  ? 47   PRO A CA  1 
ATOM   115  C C   . PRO A  1 20  ? -62.820 -2.953  35.582  1.00 41.29  ? 47   PRO A C   1 
ATOM   116  O O   . PRO A  1 20  ? -62.099 -2.740  36.550  1.00 42.38  ? 47   PRO A O   1 
ATOM   117  C CB  . PRO A  1 20  ? -63.558 -0.573  35.369  1.00 46.67  ? 47   PRO A CB  1 
ATOM   118  C CG  . PRO A  1 20  ? -63.863 -0.143  36.759  1.00 54.53  ? 47   PRO A CG  1 
ATOM   119  C CD  . PRO A  1 20  ? -65.092 -0.897  37.172  1.00 49.51  ? 47   PRO A CD  1 
ATOM   120  N N   . ILE A  1 21  ? -62.630 -3.965  34.742  1.00 44.51  ? 48   ILE A N   1 
ATOM   121  C CA  . ILE A  1 21  ? -61.474 -4.842  34.874  1.00 49.77  ? 48   ILE A CA  1 
ATOM   122  C C   . ILE A  1 21  ? -60.545 -4.689  33.673  1.00 52.34  ? 48   ILE A C   1 
ATOM   123  O O   . ILE A  1 21  ? -60.984 -4.325  32.577  1.00 43.24  ? 48   ILE A O   1 
ATOM   124  C CB  . ILE A  1 21  ? -61.875 -6.326  35.064  1.00 43.28  ? 48   ILE A CB  1 
ATOM   125  C CG1 . ILE A  1 21  ? -61.958 -7.055  33.722  1.00 52.11  ? 48   ILE A CG1 1 
ATOM   126  C CG2 . ILE A  1 21  ? -63.181 -6.429  35.834  1.00 39.73  ? 48   ILE A CG2 1 
ATOM   127  C CD1 . ILE A  1 21  ? -62.325 -8.517  33.848  1.00 54.54  ? 48   ILE A CD1 1 
ATOM   128  N N   . MET A  1 22  ? -59.261 -4.958  33.900  1.00 55.83  ? 49   MET A N   1 
ATOM   129  C CA  . MET A  1 22  ? -58.233 -4.801  32.878  1.00 54.26  ? 49   MET A CA  1 
ATOM   130  C C   . MET A  1 22  ? -58.327 -3.433  32.210  1.00 54.29  ? 49   MET A C   1 
ATOM   131  O O   . MET A  1 22  ? -57.899 -2.423  32.767  1.00 64.78  ? 49   MET A O   1 
ATOM   132  C CB  . MET A  1 22  ? -58.338 -5.918  31.837  1.00 55.75  ? 49   MET A CB  1 
ATOM   133  C CG  . MET A  1 22  ? -58.037 -7.306  32.387  1.00 58.37  ? 49   MET A CG  1 
ATOM   134  S SD  . MET A  1 22  ? -56.309 -7.510  32.869  1.00 54.20  ? 49   MET A SD  1 
ATOM   135  C CE  . MET A  1 22  ? -56.291 -9.243  33.320  1.00 47.08  ? 49   MET A CE  1 
ATOM   136  N N   . SER A  1 23  ? -58.903 -3.408  31.016  1.00 43.12  ? 50   SER A N   1 
ATOM   137  C CA  . SER A  1 23  ? -59.128 -2.164  30.301  1.00 46.99  ? 50   SER A CA  1 
ATOM   138  C C   . SER A  1 23  ? -60.592 -2.100  29.882  1.00 50.85  ? 50   SER A C   1 
ATOM   139  O O   . SER A  1 23  ? -61.054 -1.113  29.306  1.00 41.95  ? 50   SER A O   1 
ATOM   140  C CB  . SER A  1 23  ? -58.216 -2.095  29.080  1.00 43.30  ? 50   SER A CB  1 
ATOM   141  O OG  . SER A  1 23  ? -58.195 -3.341  28.405  1.00 37.26  ? 50   SER A OG  1 
ATOM   142  N N   . GLU A  1 24  ? -61.319 -3.165  30.197  1.00 47.64  ? 51   GLU A N   1 
ATOM   143  C CA  . GLU A  1 24  ? -62.707 -3.298  29.788  1.00 42.41  ? 51   GLU A CA  1 
ATOM   144  C C   . GLU A  1 24  ? -63.665 -3.114  30.960  1.00 40.95  ? 51   GLU A C   1 
ATOM   145  O O   . GLU A  1 24  ? -63.286 -2.601  32.010  1.00 46.33  ? 51   GLU A O   1 
ATOM   146  C CB  . GLU A  1 24  ? -62.926 -4.663  29.131  1.00 44.16  ? 51   GLU A CB  1 
ATOM   147  C CG  . GLU A  1 24  ? -62.530 -5.843  30.003  1.00 38.70  ? 51   GLU A CG  1 
ATOM   148  C CD  . GLU A  1 24  ? -62.515 -7.149  29.236  1.00 38.10  ? 51   GLU A CD  1 
ATOM   149  O OE1 . GLU A  1 24  ? -62.599 -8.218  29.878  1.00 40.36  ? 51   GLU A OE1 1 
ATOM   150  O OE2 . GLU A  1 24  ? -62.413 -7.105  27.990  1.00 37.57  1 51   GLU A OE2 1 
ATOM   151  N N   . TYR A  1 25  ? -64.910 -3.535  30.768  1.00 35.43  ? 52   TYR A N   1 
ATOM   152  C CA  . TYR A  1 25  ? -65.939 -3.398  31.786  1.00 33.54  ? 52   TYR A CA  1 
ATOM   153  C C   . TYR A  1 25  ? -66.845 -4.621  31.775  1.00 34.14  ? 52   TYR A C   1 
ATOM   154  O O   . TYR A  1 25  ? -67.392 -4.977  30.732  1.00 31.83  ? 52   TYR A O   1 
ATOM   155  C CB  . TYR A  1 25  ? -66.779 -2.153  31.518  1.00 35.05  ? 52   TYR A CB  1 
ATOM   156  C CG  . TYR A  1 25  ? -65.999 -0.859  31.493  1.00 42.18  ? 52   TYR A CG  1 
ATOM   157  C CD1 . TYR A  1 25  ? -65.763 -0.147  32.662  1.00 50.78  ? 52   TYR A CD1 1 
ATOM   158  C CD2 . TYR A  1 25  ? -65.515 -0.338  30.299  1.00 42.77  ? 52   TYR A CD2 1 
ATOM   159  C CE1 . TYR A  1 25  ? -65.056 1.044   32.645  1.00 53.53  ? 52   TYR A CE1 1 
ATOM   160  C CE2 . TYR A  1 25  ? -64.808 0.855   30.273  1.00 50.54  ? 52   TYR A CE2 1 
ATOM   161  C CZ  . TYR A  1 25  ? -64.582 1.542   31.450  1.00 51.10  ? 52   TYR A CZ  1 
ATOM   162  O OH  . TYR A  1 25  ? -63.883 2.728   31.434  1.00 43.38  ? 52   TYR A OH  1 
ATOM   163  N N   . GLU A  1 26  ? -67.014 -5.250  32.935  1.00 28.09  ? 53   GLU A N   1 
ATOM   164  C CA  . GLU A  1 26  ? -67.811 -6.467  33.043  1.00 20.60  ? 53   GLU A CA  1 
ATOM   165  C C   . GLU A  1 26  ? -69.151 -6.223  33.720  1.00 19.53  ? 53   GLU A C   1 
ATOM   166  O O   . GLU A  1 26  ? -69.282 -6.433  34.922  1.00 21.20  ? 53   GLU A O   1 
ATOM   167  C CB  . GLU A  1 26  ? -67.047 -7.523  33.832  1.00 23.27  ? 53   GLU A CB  1 
ATOM   168  C CG  . GLU A  1 26  ? -67.741 -8.868  33.900  1.00 29.95  ? 53   GLU A CG  1 
ATOM   169  C CD  . GLU A  1 26  ? -67.122 -9.882  32.957  1.00 46.98  ? 53   GLU A CD  1 
ATOM   170  O OE1 . GLU A  1 26  ? -66.197 -9.507  32.199  1.00 43.65  ? 53   GLU A OE1 1 
ATOM   171  O OE2 . GLU A  1 26  ? -67.556 -11.056 32.980  1.00 43.38  1 53   GLU A OE2 1 
ATOM   172  N N   . ILE A  1 27  ? -70.147 -5.796  32.951  1.00 18.05  ? 54   ILE A N   1 
ATOM   173  C CA  . ILE A  1 27  ? -71.477 -5.542  33.497  1.00 18.41  ? 54   ILE A CA  1 
ATOM   174  C C   . ILE A  1 27  ? -72.243 -6.836  33.740  1.00 18.70  ? 54   ILE A C   1 
ATOM   175  O O   . ILE A  1 27  ? -72.221 -7.742  32.913  1.00 18.92  ? 54   ILE A O   1 
ATOM   176  C CB  . ILE A  1 27  ? -72.300 -4.637  32.583  1.00 18.25  ? 54   ILE A CB  1 
ATOM   177  C CG1 . ILE A  1 27  ? -71.497 -3.386  32.227  1.00 22.31  ? 54   ILE A CG1 1 
ATOM   178  C CG2 . ILE A  1 27  ? -73.619 -4.271  33.246  1.00 19.75  ? 54   ILE A CG2 1 
ATOM   179  C CD1 . ILE A  1 27  ? -72.319 -2.301  31.581  1.00 25.08  ? 54   ILE A CD1 1 
ATOM   180  N N   . ILE A  1 28  ? -72.916 -6.914  34.883  1.00 20.84  ? 55   ILE A N   1 
ATOM   181  C CA  . ILE A  1 28  ? -73.588 -8.135  35.305  1.00 24.90  ? 55   ILE A CA  1 
ATOM   182  C C   . ILE A  1 28  ? -75.007 -7.827  35.721  1.00 34.66  ? 55   ILE A C   1 
ATOM   183  O O   . ILE A  1 28  ? -75.234 -7.105  36.693  1.00 40.27  ? 55   ILE A O   1 
ATOM   184  C CB  . ILE A  1 28  ? -72.885 -8.787  36.515  1.00 29.70  ? 55   ILE A CB  1 
ATOM   185  C CG1 . ILE A  1 28  ? -71.459 -9.223  36.148  1.00 35.57  ? 55   ILE A CG1 1 
ATOM   186  C CG2 . ILE A  1 28  ? -73.704 -9.961  37.027  1.00 27.71  ? 55   ILE A CG2 1 
ATOM   187  C CD1 . ILE A  1 28  ? -70.601 -9.652  37.331  1.00 22.97  ? 55   ILE A CD1 1 
ATOM   188  N N   . CYS A  1 29  ? -75.962 -8.384  34.986  1.00 33.90  ? 56   CYS A N   1 
ATOM   189  C CA  . CYS A  1 29  ? -77.368 -8.195  35.301  1.00 31.05  ? 56   CYS A CA  1 
ATOM   190  C C   . CYS A  1 29  ? -78.039 -9.536  35.570  1.00 33.79  ? 56   CYS A C   1 
ATOM   191  O O   . CYS A  1 29  ? -77.952 -10.449 34.749  1.00 33.33  ? 56   CYS A O   1 
ATOM   192  C CB  . CYS A  1 29  ? -78.069 -7.458  34.166  1.00 28.99  ? 56   CYS A CB  1 
ATOM   193  S SG  . CYS A  1 29  ? -77.268 -5.903  33.739  1.00 36.73  ? 56   CYS A SG  1 
ATOM   194  N N   . PRO A  1 30  ? -78.703 -9.666  36.729  1.00 35.97  ? 57   PRO A N   1 
ATOM   195  C CA  . PRO A  1 30  ? -78.806 -8.650  37.781  1.00 34.83  ? 57   PRO A CA  1 
ATOM   196  C C   . PRO A  1 30  ? -77.495 -8.484  38.537  1.00 46.16  ? 57   PRO A C   1 
ATOM   197  O O   . PRO A  1 30  ? -76.578 -9.291  38.370  1.00 45.27  ? 57   PRO A O   1 
ATOM   198  C CB  . PRO A  1 30  ? -79.868 -9.224  38.726  1.00 34.76  ? 57   PRO A CB  1 
ATOM   199  C CG  . PRO A  1 30  ? -80.571 -10.271 37.950  1.00 31.91  ? 57   PRO A CG  1 
ATOM   200  C CD  . PRO A  1 30  ? -79.561 -10.827 37.008  1.00 35.40  ? 57   PRO A CD  1 
ATOM   201  N N   . ALA A  1 31  ? -77.423 -7.445  39.360  1.00 49.68  ? 58   ALA A N   1 
ATOM   202  C CA  . ALA A  1 31  ? -76.209 -7.120  40.093  1.00 47.87  ? 58   ALA A CA  1 
ATOM   203  C C   . ALA A  1 31  ? -75.819 -8.186  41.121  1.00 54.20  ? 58   ALA A C   1 
ATOM   204  O O   . ALA A  1 31  ? -74.637 -8.363  41.418  1.00 51.29  ? 58   ALA A O   1 
ATOM   205  C CB  . ALA A  1 31  ? -76.356 -5.764  40.761  1.00 50.91  ? 58   ALA A CB  1 
ATOM   206  N N   . ASN A  1 32  ? -76.802 -8.899  41.660  1.00 53.42  ? 59   ASN A N   1 
ATOM   207  C CA  . ASN A  1 32  ? -76.523 -9.867  42.720  1.00 65.97  ? 59   ASN A CA  1 
ATOM   208  C C   . ASN A  1 32  ? -76.769 -11.330 42.351  1.00 64.00  ? 59   ASN A C   1 
ATOM   209  O O   . ASN A  1 32  ? -76.594 -12.223 43.182  1.00 60.29  ? 59   ASN A O   1 
ATOM   210  C CB  . ASN A  1 32  ? -77.299 -9.509  43.991  1.00 78.56  ? 59   ASN A CB  1 
ATOM   211  C CG  . ASN A  1 32  ? -76.438 -8.801  45.023  1.00 78.83  ? 59   ASN A CG  1 
ATOM   212  O OD1 . ASN A  1 32  ? -75.951 -7.694  44.790  1.00 78.79  ? 59   ASN A OD1 1 
ATOM   213  N ND2 . ASN A  1 32  ? -76.255 -9.435  46.176  1.00 81.32  ? 59   ASN A ND2 1 
ATOM   214  N N   . ALA A  1 33  ? -77.167 -11.574 41.107  1.00 62.70  ? 60   ALA A N   1 
ATOM   215  C CA  . ALA A  1 33  ? -77.467 -12.932 40.659  1.00 61.79  ? 60   ALA A CA  1 
ATOM   216  C C   . ALA A  1 33  ? -76.233 -13.822 40.639  1.00 61.94  ? 60   ALA A C   1 
ATOM   217  O O   . ALA A  1 33  ? -75.133 -13.374 40.310  1.00 54.34  ? 60   ALA A O   1 
ATOM   218  C CB  . ALA A  1 33  ? -78.105 -12.908 39.290  1.00 55.40  ? 60   ALA A CB  1 
ATOM   219  N N   . GLU A  1 34  ? -76.429 -15.089 40.989  1.00 64.82  ? 61   GLU A N   1 
ATOM   220  C CA  . GLU A  1 34  ? -75.355 -16.073 40.939  1.00 67.55  ? 61   GLU A CA  1 
ATOM   221  C C   . GLU A  1 34  ? -75.040 -16.384 39.482  1.00 53.30  ? 61   GLU A C   1 
ATOM   222  O O   . GLU A  1 34  ? -73.940 -16.109 39.001  1.00 39.82  ? 61   GLU A O   1 
ATOM   223  C CB  . GLU A  1 34  ? -75.752 -17.353 41.682  1.00 71.08  ? 61   GLU A CB  1 
ATOM   224  C CG  . GLU A  1 34  ? -76.056 -17.166 43.169  1.00 76.31  ? 61   GLU A CG  1 
ATOM   225  C CD  . GLU A  1 34  ? -77.458 -16.632 43.435  1.00 77.55  ? 61   GLU A CD  1 
ATOM   226  O OE1 . GLU A  1 34  ? -78.294 -16.645 42.506  1.00 66.32  ? 61   GLU A OE1 1 
ATOM   227  O OE2 . GLU A  1 34  ? -77.722 -16.199 44.579  1.00 78.72  1 61   GLU A OE2 1 
ATOM   228  N N   . ASN A  1 35  ? -76.018 -16.964 38.791  1.00 50.52  ? 62   ASN A N   1 
ATOM   229  C CA  . ASN A  1 35  ? -75.942 -17.170 37.352  1.00 44.83  ? 62   ASN A CA  1 
ATOM   230  C C   . ASN A  1 35  ? -76.746 -16.079 36.666  1.00 42.87  ? 62   ASN A C   1 
ATOM   231  O O   . ASN A  1 35  ? -77.951 -16.228 36.467  1.00 46.29  ? 62   ASN A O   1 
ATOM   232  C CB  . ASN A  1 35  ? -76.500 -18.542 36.977  1.00 46.70  ? 62   ASN A CB  1 
ATOM   233  C CG  . ASN A  1 35  ? -75.780 -19.677 37.682  1.00 50.36  ? 62   ASN A CG  1 
ATOM   234  O OD1 . ASN A  1 35  ? -76.344 -20.334 38.559  1.00 50.72  ? 62   ASN A OD1 1 
ATOM   235  N ND2 . ASN A  1 35  ? -74.529 -19.918 37.297  1.00 45.87  ? 62   ASN A ND2 1 
ATOM   236  N N   . PRO A  1 36  ? -76.079 -14.978 36.294  1.00 38.50  ? 63   PRO A N   1 
ATOM   237  C CA  . PRO A  1 36  ? -76.796 -13.774 35.877  1.00 37.49  ? 63   PRO A CA  1 
ATOM   238  C C   . PRO A  1 36  ? -77.509 -13.985 34.557  1.00 32.50  ? 63   PRO A C   1 
ATOM   239  O O   . PRO A  1 36  ? -77.104 -14.837 33.765  1.00 30.46  ? 63   PRO A O   1 
ATOM   240  C CB  . PRO A  1 36  ? -75.682 -12.728 35.710  1.00 30.09  ? 63   PRO A CB  1 
ATOM   241  C CG  . PRO A  1 36  ? -74.390 -13.435 35.975  1.00 26.45  ? 63   PRO A CG  1 
ATOM   242  C CD  . PRO A  1 36  ? -74.653 -14.903 35.953  1.00 31.68  ? 63   PRO A CD  1 
ATOM   243  N N   . THR A  1 37  ? -78.571 -13.222 34.339  1.00 28.59  ? 64   THR A N   1 
ATOM   244  C CA  . THR A  1 37  ? -79.271 -13.249 33.069  1.00 30.76  ? 64   THR A CA  1 
ATOM   245  C C   . THR A  1 37  ? -78.307 -12.830 31.961  1.00 29.44  ? 64   THR A C   1 
ATOM   246  O O   . THR A  1 37  ? -78.120 -13.551 30.979  1.00 27.58  ? 64   THR A O   1 
ATOM   247  C CB  . THR A  1 37  ? -80.488 -12.310 33.086  1.00 29.40  ? 64   THR A CB  1 
ATOM   248  O OG1 . THR A  1 37  ? -81.286 -12.582 34.243  1.00 31.18  ? 64   THR A OG1 1 
ATOM   249  C CG2 . THR A  1 37  ? -81.333 -12.516 31.854  1.00 28.28  ? 64   THR A CG2 1 
ATOM   250  N N   . PHE A  1 38  ? -77.678 -11.672 32.143  1.00 26.12  ? 65   PHE A N   1 
ATOM   251  C CA  . PHE A  1 38  ? -76.746 -11.142 31.157  1.00 21.82  ? 65   PHE A CA  1 
ATOM   252  C C   . PHE A  1 38  ? -75.389 -10.853 31.764  1.00 21.99  ? 65   PHE A C   1 
ATOM   253  O O   . PHE A  1 38  ? -75.278 -10.580 32.957  1.00 28.52  ? 65   PHE A O   1 
ATOM   254  C CB  . PHE A  1 38  ? -77.299 -9.860  30.541  1.00 19.24  ? 65   PHE A CB  1 
ATOM   255  C CG  . PHE A  1 38  ? -78.585 -10.055 29.812  1.00 22.00  ? 65   PHE A CG  1 
ATOM   256  C CD1 . PHE A  1 38  ? -78.601 -10.641 28.561  1.00 21.50  ? 65   PHE A CD1 1 
ATOM   257  C CD2 . PHE A  1 38  ? -79.783 -9.658  30.378  1.00 27.82  ? 65   PHE A CD2 1 
ATOM   258  C CE1 . PHE A  1 38  ? -79.787 -10.827 27.885  1.00 25.10  ? 65   PHE A CE1 1 
ATOM   259  C CE2 . PHE A  1 38  ? -80.974 -9.837  29.706  1.00 27.89  ? 65   PHE A CE2 1 
ATOM   260  C CZ  . PHE A  1 38  ? -80.976 -10.424 28.458  1.00 26.89  ? 65   PHE A CZ  1 
ATOM   261  N N   . ARG A  1 39  ? -74.354 -10.904 30.935  1.00 16.32  ? 66   ARG A N   1 
ATOM   262  C CA  . ARG A  1 39  ? -73.030 -10.499 31.372  1.00 16.95  ? 66   ARG A CA  1 
ATOM   263  C C   . ARG A  1 39  ? -72.308 -9.764  30.256  1.00 18.01  ? 66   ARG A C   1 
ATOM   264  O O   . ARG A  1 39  ? -71.443 -10.325 29.588  1.00 21.08  ? 66   ARG A O   1 
ATOM   265  C CB  . ARG A  1 39  ? -72.212 -11.702 31.826  1.00 21.63  ? 66   ARG A CB  1 
ATOM   266  C CG  . ARG A  1 39  ? -71.018 -11.326 32.683  1.00 26.05  ? 66   ARG A CG  1 
ATOM   267  C CD  . ARG A  1 39  ? -70.045 -12.479 32.809  1.00 31.63  ? 66   ARG A CD  1 
ATOM   268  N NE  . ARG A  1 39  ? -70.694 -13.708 33.250  1.00 33.89  ? 66   ARG A NE  1 
ATOM   269  C CZ  . ARG A  1 39  ? -70.967 -13.992 34.519  1.00 32.52  ? 66   ARG A CZ  1 
ATOM   270  N NH1 . ARG A  1 39  ? -70.657 -13.127 35.476  1.00 30.97  1 66   ARG A NH1 1 
ATOM   271  N NH2 . ARG A  1 39  ? -71.553 -15.141 34.828  1.00 29.46  ? 66   ARG A NH2 1 
ATOM   272  N N   . LEU A  1 40  ? -72.674 -8.505  30.060  1.00 18.67  ? 67   LEU A N   1 
ATOM   273  C CA  . LEU A  1 40  ? -72.058 -7.673  29.039  1.00 17.50  ? 67   LEU A CA  1 
ATOM   274  C C   . LEU A  1 40  ? -70.605 -7.437  29.384  1.00 19.30  ? 67   LEU A C   1 
ATOM   275  O O   . LEU A  1 40  ? -70.260 -7.281  30.552  1.00 22.85  ? 67   LEU A O   1 
ATOM   276  C CB  . LEU A  1 40  ? -72.759 -6.321  28.939  1.00 16.39  ? 67   LEU A CB  1 
ATOM   277  C CG  . LEU A  1 40  ? -74.140 -6.216  28.301  1.00 16.07  ? 67   LEU A CG  1 
ATOM   278  C CD1 . LEU A  1 40  ? -75.203 -6.955  29.099  1.00 15.34  ? 67   LEU A CD1 1 
ATOM   279  C CD2 . LEU A  1 40  ? -74.497 -4.751  28.183  1.00 22.16  ? 67   LEU A CD2 1 
ATOM   280  N N   . THR A  1 41  ? -69.760 -7.414  28.362  1.00 18.82  ? 68   THR A N   1 
ATOM   281  C CA  . THR A  1 41  ? -68.354 -7.095  28.535  1.00 20.63  ? 68   THR A CA  1 
ATOM   282  C C   . THR A  1 41  ? -67.970 -6.052  27.496  1.00 22.99  ? 68   THR A C   1 
ATOM   283  O O   . THR A  1 41  ? -67.806 -6.364  26.316  1.00 24.24  ? 68   THR A O   1 
ATOM   284  C CB  . THR A  1 41  ? -67.468 -8.346  28.392  1.00 21.23  ? 68   THR A CB  1 
ATOM   285  O OG1 . THR A  1 41  ? -67.800 -9.288  29.420  1.00 17.89  ? 68   THR A OG1 1 
ATOM   286  C CG2 . THR A  1 41  ? -66.002 -7.979  28.511  1.00 29.94  ? 68   THR A CG2 1 
ATOM   287  N N   . ILE A  1 42  ? -67.846 -4.804  27.931  1.00 25.72  ? 69   ILE A N   1 
ATOM   288  C CA  . ILE A  1 42  ? -67.600 -3.713  26.996  1.00 29.16  ? 69   ILE A CA  1 
ATOM   289  C C   . ILE A  1 42  ? -66.146 -3.248  26.996  1.00 29.74  ? 69   ILE A C   1 
ATOM   290  O O   . ILE A  1 42  ? -65.576 -2.942  28.039  1.00 34.05  ? 69   ILE A O   1 
ATOM   291  C CB  . ILE A  1 42  ? -68.523 -2.494  27.263  1.00 24.27  ? 69   ILE A CB  1 
ATOM   292  C CG1 . ILE A  1 42  ? -69.996 -2.890  27.170  1.00 24.12  ? 69   ILE A CG1 1 
ATOM   293  C CG2 . ILE A  1 42  ? -68.230 -1.377  26.285  1.00 22.11  ? 69   ILE A CG2 1 
ATOM   294  C CD1 . ILE A  1 42  ? -70.631 -3.237  28.500  1.00 25.81  ? 69   ILE A CD1 1 
ATOM   295  N N   . GLN A  1 43  ? -65.554 -3.217  25.810  1.00 29.58  ? 70   GLN A N   1 
ATOM   296  C CA  . GLN A  1 43  ? -64.280 -2.556  25.587  1.00 29.44  ? 70   GLN A CA  1 
ATOM   297  C C   . GLN A  1 43  ? -64.535 -1.465  24.545  1.00 30.55  ? 70   GLN A C   1 
ATOM   298  O O   . GLN A  1 43  ? -64.528 -1.732  23.338  1.00 26.60  ? 70   GLN A O   1 
ATOM   299  C CB  . GLN A  1 43  ? -63.226 -3.564  25.119  1.00 31.96  ? 70   GLN A CB  1 
ATOM   300  C CG  . GLN A  1 43  ? -61.956 -2.964  24.515  1.00 42.88  ? 70   GLN A CG  1 
ATOM   301  C CD  . GLN A  1 43  ? -60.929 -2.548  25.553  1.00 48.23  ? 70   GLN A CD  1 
ATOM   302  O OE1 . GLN A  1 43  ? -61.275 -2.040  26.620  1.00 52.70  ? 70   GLN A OE1 1 
ATOM   303  N NE2 . GLN A  1 43  ? -59.653 -2.765  25.241  1.00 40.10  ? 70   GLN A NE2 1 
ATOM   304  N N   . PRO A  1 44  ? -64.804 -0.237  25.022  1.00 33.30  ? 71   PRO A N   1 
ATOM   305  C CA  . PRO A  1 44  ? -65.218 0.948   24.254  1.00 33.81  ? 71   PRO A CA  1 
ATOM   306  C C   . PRO A  1 44  ? -64.454 1.136   22.950  1.00 32.70  ? 71   PRO A C   1 
ATOM   307  O O   . PRO A  1 44  ? -63.285 0.774   22.881  1.00 41.76  ? 71   PRO A O   1 
ATOM   308  C CB  . PRO A  1 44  ? -64.915 2.095   25.214  1.00 33.62  ? 71   PRO A CB  1 
ATOM   309  C CG  . PRO A  1 44  ? -65.157 1.497   26.560  1.00 35.44  ? 71   PRO A CG  1 
ATOM   310  C CD  . PRO A  1 44  ? -64.725 0.055   26.466  1.00 31.81  ? 71   PRO A CD  1 
ATOM   311  N N   . LYS A  1 45  ? -65.124 1.681   21.936  1.00 31.17  ? 72   LYS A N   1 
ATOM   312  C CA  . LYS A  1 45  ? -64.568 1.844   20.589  1.00 26.97  ? 72   LYS A CA  1 
ATOM   313  C C   . LYS A  1 45  ? -64.278 0.526   19.866  1.00 28.81  ? 72   LYS A C   1 
ATOM   314  O O   . LYS A  1 45  ? -64.366 0.456   18.641  1.00 35.40  ? 72   LYS A O   1 
ATOM   315  C CB  . LYS A  1 45  ? -63.327 2.743   20.589  1.00 26.40  ? 72   LYS A CB  1 
ATOM   316  C CG  . LYS A  1 45  ? -63.618 4.233   20.704  1.00 35.29  ? 72   LYS A CG  1 
ATOM   317  C CD  . LYS A  1 45  ? -62.321 5.050   20.641  1.00 60.03  ? 72   LYS A CD  1 
ATOM   318  C CE  . LYS A  1 45  ? -62.571 6.556   20.757  1.00 54.43  ? 72   LYS A CE  1 
ATOM   319  N NZ  . LYS A  1 45  ? -61.302 7.340   20.871  1.00 27.45  1 72   LYS A NZ  1 
ATOM   320  N N   . ASP A  1 46  ? -63.949 -0.517  20.620  1.00 26.94  ? 73   ASP A N   1 
ATOM   321  C CA  . ASP A  1 46  ? -63.592 -1.799  20.023  1.00 35.73  ? 73   ASP A CA  1 
ATOM   322  C C   . ASP A  1 46  ? -64.806 -2.707  19.836  1.00 34.40  ? 73   ASP A C   1 
ATOM   323  O O   . ASP A  1 46  ? -65.482 -2.650  18.803  1.00 31.83  ? 73   ASP A O   1 
ATOM   324  C CB  . ASP A  1 46  ? -62.519 -2.504  20.859  1.00 41.88  ? 73   ASP A CB  1 
ATOM   325  C CG  . ASP A  1 46  ? -61.850 -3.648  20.113  1.00 51.16  ? 73   ASP A CG  1 
ATOM   326  O OD1 . ASP A  1 46  ? -62.151 -3.843  18.913  1.00 49.50  ? 73   ASP A OD1 1 
ATOM   327  O OD2 . ASP A  1 46  ? -61.007 -4.343  20.725  1.00 53.11  1 73   ASP A OD2 1 
ATOM   328  N N   . TYR A  1 47  ? -65.079 -3.541  20.835  1.00 26.66  ? 74   TYR A N   1 
ATOM   329  C CA  . TYR A  1 47  ? -66.129 -4.540  20.710  1.00 25.38  ? 74   TYR A CA  1 
ATOM   330  C C   . TYR A  1 47  ? -67.083 -4.532  21.907  1.00 19.84  ? 74   TYR A C   1 
ATOM   331  O O   . TYR A  1 47  ? -66.987 -3.673  22.780  1.00 19.20  ? 74   TYR A O   1 
ATOM   332  C CB  . TYR A  1 47  ? -65.509 -5.930  20.522  1.00 28.08  ? 74   TYR A CB  1 
ATOM   333  C CG  . TYR A  1 47  ? -64.913 -6.503  21.785  1.00 30.21  ? 74   TYR A CG  1 
ATOM   334  C CD1 . TYR A  1 47  ? -63.693 -6.053  22.263  1.00 31.93  ? 74   TYR A CD1 1 
ATOM   335  C CD2 . TYR A  1 47  ? -65.578 -7.492  22.505  1.00 28.44  ? 74   TYR A CD2 1 
ATOM   336  C CE1 . TYR A  1 47  ? -63.148 -6.570  23.425  1.00 39.42  ? 74   TYR A CE1 1 
ATOM   337  C CE2 . TYR A  1 47  ? -65.043 -8.015  23.668  1.00 28.30  ? 74   TYR A CE2 1 
ATOM   338  C CZ  . TYR A  1 47  ? -63.827 -7.549  24.124  1.00 39.77  ? 74   TYR A CZ  1 
ATOM   339  O OH  . TYR A  1 47  ? -63.279 -8.061  25.279  1.00 51.24  ? 74   TYR A OH  1 
ATOM   340  N N   . VAL A  1 48  ? -68.012 -5.483  21.922  1.00 16.48  ? 75   VAL A N   1 
ATOM   341  C CA  . VAL A  1 48  ? -68.897 -5.698  23.064  1.00 16.09  ? 75   VAL A CA  1 
ATOM   342  C C   . VAL A  1 48  ? -69.516 -7.087  23.009  1.00 11.46  ? 75   VAL A C   1 
ATOM   343  O O   . VAL A  1 48  ? -70.225 -7.424  22.069  1.00 8.59   ? 75   VAL A O   1 
ATOM   344  C CB  . VAL A  1 48  ? -70.015 -4.634  23.149  1.00 17.55  ? 75   VAL A CB  1 
ATOM   345  C CG1 . VAL A  1 48  ? -70.516 -4.270  21.767  1.00 15.86  ? 75   VAL A CG1 1 
ATOM   346  C CG2 . VAL A  1 48  ? -71.154 -5.118  24.038  1.00 12.50  ? 75   VAL A CG2 1 
ATOM   347  N N   . GLN A  1 49  ? -69.232 -7.898  24.019  1.00 12.43  ? 76   GLN A N   1 
ATOM   348  C CA  . GLN A  1 49  ? -69.769 -9.249  24.073  1.00 12.10  ? 76   GLN A CA  1 
ATOM   349  C C   . GLN A  1 49  ? -70.948 -9.342  25.020  1.00 12.32  ? 76   GLN A C   1 
ATOM   350  O O   . GLN A  1 49  ? -70.854 -8.934  26.176  1.00 14.57  ? 76   GLN A O   1 
ATOM   351  C CB  . GLN A  1 49  ? -68.700 -10.251 24.501  1.00 13.78  ? 76   GLN A CB  1 
ATOM   352  C CG  . GLN A  1 49  ? -69.275 -11.449 25.244  1.00 14.53  ? 76   GLN A CG  1 
ATOM   353  C CD  . GLN A  1 49  ? -68.360 -12.648 25.222  1.00 19.39  ? 76   GLN A CD  1 
ATOM   354  O OE1 . GLN A  1 49  ? -67.349 -12.658 24.517  1.00 17.65  ? 76   GLN A OE1 1 
ATOM   355  N NE2 . GLN A  1 49  ? -68.710 -13.675 25.992  1.00 17.57  ? 76   GLN A NE2 1 
ATOM   356  N N   . ILE A  1 50  ? -72.051 -9.897  24.524  1.00 11.25  ? 77   ILE A N   1 
ATOM   357  C CA  . ILE A  1 50  ? -73.261 -10.063 25.320  1.00 11.13  ? 77   ILE A CA  1 
ATOM   358  C C   . ILE A  1 50  ? -73.551 -11.536 25.602  1.00 10.60  ? 77   ILE A C   1 
ATOM   359  O O   . ILE A  1 50  ? -73.999 -12.270 24.726  1.00 9.30   ? 77   ILE A O   1 
ATOM   360  C CB  . ILE A  1 50  ? -74.464 -9.441  24.618  1.00 9.77   ? 77   ILE A CB  1 
ATOM   361  C CG1 . ILE A  1 50  ? -74.150 -8.001  24.221  1.00 9.38   ? 77   ILE A CG1 1 
ATOM   362  C CG2 . ILE A  1 50  ? -75.690 -9.496  25.512  1.00 13.18  ? 77   ILE A CG2 1 
ATOM   363  C CD1 . ILE A  1 50  ? -75.276 -7.323  23.471  1.00 9.63   ? 77   ILE A CD1 1 
ATOM   364  N N   . MET A  1 51  ? -73.294 -11.955 26.835  1.00 12.69  ? 78   MET A N   1 
ATOM   365  C CA  . MET A  1 51  ? -73.409 -13.356 27.216  1.00 13.50  ? 78   MET A CA  1 
ATOM   366  C C   . MET A  1 51  ? -74.687 -13.571 27.995  1.00 14.61  ? 78   MET A C   1 
ATOM   367  O O   . MET A  1 51  ? -74.825 -13.092 29.120  1.00 19.50  ? 78   MET A O   1 
ATOM   368  C CB  . MET A  1 51  ? -72.203 -13.774 28.060  1.00 18.43  ? 78   MET A CB  1 
ATOM   369  C CG  . MET A  1 51  ? -72.397 -15.059 28.856  1.00 23.25  ? 78   MET A CG  1 
ATOM   370  S SD  . MET A  1 51  ? -71.948 -16.539 27.939  1.00 32.58  ? 78   MET A SD  1 
ATOM   371  C CE  . MET A  1 51  ? -70.267 -16.131 27.490  1.00 29.47  ? 78   MET A CE  1 
ATOM   372  N N   . CYS A  1 52  ? -75.618 -14.303 27.395  1.00 13.14  ? 79   CYS A N   1 
ATOM   373  C CA  . CYS A  1 52  ? -76.943 -14.470 27.965  1.00 12.78  ? 79   CYS A CA  1 
ATOM   374  C C   . CYS A  1 52  ? -77.091 -15.776 28.735  1.00 14.54  ? 79   CYS A C   1 
ATOM   375  O O   . CYS A  1 52  ? -76.260 -16.672 28.637  1.00 17.08  ? 79   CYS A O   1 
ATOM   376  C CB  . CYS A  1 52  ? -77.991 -14.414 26.854  1.00 14.46  ? 79   CYS A CB  1 
ATOM   377  S SG  . CYS A  1 52  ? -77.854 -12.990 25.752  1.00 17.11  ? 79   CYS A SG  1 
ATOM   378  N N   . ASN A  1 53  ? -78.166 -15.869 29.505  1.00 16.05  ? 80   ASN A N   1 
ATOM   379  C CA  . ASN A  1 53  ? -78.543 -17.102 30.170  1.00 18.51  ? 80   ASN A CA  1 
ATOM   380  C C   . ASN A  1 53  ? -80.056 -17.057 30.366  1.00 21.77  ? 80   ASN A C   1 
ATOM   381  O O   . ASN A  1 53  ? -80.546 -16.712 31.441  1.00 25.61  ? 80   ASN A O   1 
ATOM   382  C CB  . ASN A  1 53  ? -77.806 -17.225 31.501  1.00 24.06  ? 80   ASN A CB  1 
ATOM   383  C CG  . ASN A  1 53  ? -77.840 -18.630 32.064  1.00 24.57  ? 80   ASN A CG  1 
ATOM   384  O OD1 . ASN A  1 53  ? -78.334 -19.558 31.424  1.00 23.10  ? 80   ASN A OD1 1 
ATOM   385  N ND2 . ASN A  1 53  ? -77.302 -18.793 33.270  1.00 28.21  ? 80   ASN A ND2 1 
ATOM   386  N N   . LEU A  1 54  ? -80.792 -17.387 29.307  1.00 23.16  ? 81   LEU A N   1 
ATOM   387  C CA  . LEU A  1 54  ? -82.224 -17.085 29.234  1.00 23.30  ? 81   LEU A CA  1 
ATOM   388  C C   . LEU A  1 54  ? -83.121 -18.328 29.172  1.00 22.27  ? 81   LEU A C   1 
ATOM   389  O O   . LEU A  1 54  ? -82.741 -19.356 28.611  1.00 20.64  ? 81   LEU A O   1 
ATOM   390  C CB  . LEU A  1 54  ? -82.503 -16.180 28.025  1.00 20.96  ? 81   LEU A CB  1 
ATOM   391  C CG  . LEU A  1 54  ? -82.268 -14.663 28.076  1.00 21.37  ? 81   LEU A CG  1 
ATOM   392  C CD1 . LEU A  1 54  ? -81.026 -14.287 28.849  1.00 24.39  ? 81   LEU A CD1 1 
ATOM   393  C CD2 . LEU A  1 54  ? -82.174 -14.082 26.674  1.00 17.01  ? 81   LEU A CD2 1 
ATOM   394  N N   . THR A  1 55  ? -84.315 -18.218 29.751  1.00 22.07  ? 82   THR A N   1 
ATOM   395  C CA  . THR A  1 55  ? -85.302 -19.296 29.729  1.00 27.87  ? 82   THR A CA  1 
ATOM   396  C C   . THR A  1 55  ? -86.366 -19.033 28.670  1.00 33.82  ? 82   THR A C   1 
ATOM   397  O O   . THR A  1 55  ? -86.471 -19.759 27.682  1.00 38.47  ? 82   THR A O   1 
ATOM   398  C CB  . THR A  1 55  ? -86.011 -19.426 31.077  1.00 26.88  ? 82   THR A CB  1 
ATOM   399  O OG1 . THR A  1 55  ? -86.774 -18.240 31.325  1.00 29.54  ? 82   THR A OG1 1 
ATOM   400  C CG2 . THR A  1 55  ? -84.998 -19.612 32.189  1.00 31.39  ? 82   THR A CG2 1 
ATOM   401  N N   . ASP A  1 56  ? -87.171 -18.000 28.899  1.00 34.34  ? 83   ASP A N   1 
ATOM   402  C CA  . ASP A  1 56  ? -88.096 -17.509 27.888  1.00 38.04  ? 83   ASP A CA  1 
ATOM   403  C C   . ASP A  1 56  ? -87.540 -16.213 27.309  1.00 34.87  ? 83   ASP A C   1 
ATOM   404  O O   . ASP A  1 56  ? -86.648 -15.606 27.887  1.00 32.63  ? 83   ASP A O   1 
ATOM   405  C CB  . ASP A  1 56  ? -89.493 -17.289 28.479  1.00 40.76  ? 83   ASP A CB  1 
ATOM   406  C CG  . ASP A  1 56  ? -90.207 -18.598 28.802  1.00 47.92  ? 83   ASP A CG  1 
ATOM   407  O OD1 . ASP A  1 56  ? -90.806 -19.193 27.877  1.00 43.75  ? 83   ASP A OD1 1 
ATOM   408  O OD2 . ASP A  1 56  ? -90.175 -19.029 29.979  1.00 42.97  1 83   ASP A OD2 1 
ATOM   409  N N   . THR A  1 57  ? -88.068 -15.789 26.169  1.00 41.56  ? 84   THR A N   1 
ATOM   410  C CA  . THR A  1 57  ? -87.557 -14.606 25.479  1.00 40.27  ? 84   THR A CA  1 
ATOM   411  C C   . THR A  1 57  ? -87.817 -13.308 26.254  1.00 34.67  ? 84   THR A C   1 
ATOM   412  O O   . THR A  1 57  ? -87.276 -12.254 25.918  1.00 25.34  ? 84   THR A O   1 
ATOM   413  C CB  . THR A  1 57  ? -88.173 -14.487 24.061  1.00 46.95  ? 84   THR A CB  1 
ATOM   414  O OG1 . THR A  1 57  ? -87.432 -13.540 23.279  1.00 34.08  ? 84   THR A OG1 1 
ATOM   415  C CG2 . THR A  1 57  ? -89.642 -14.063 24.143  1.00 41.45  ? 84   THR A CG2 1 
ATOM   416  N N   . THR A  1 58  ? -88.640 -13.397 27.294  1.00 42.94  ? 85   THR A N   1 
ATOM   417  C CA  . THR A  1 58  ? -89.099 -12.217 28.028  1.00 46.90  ? 85   THR A CA  1 
ATOM   418  C C   . THR A  1 58  ? -88.076 -11.691 29.033  1.00 42.85  ? 85   THR A C   1 
ATOM   419  O O   . THR A  1 58  ? -88.342 -10.730 29.758  1.00 41.76  ? 85   THR A O   1 
ATOM   420  C CB  . THR A  1 58  ? -90.424 -12.500 28.771  1.00 40.57  ? 85   THR A CB  1 
ATOM   421  O OG1 . THR A  1 58  ? -90.241 -13.595 29.676  1.00 41.43  ? 85   THR A OG1 1 
ATOM   422  C CG2 . THR A  1 58  ? -91.525 -12.846 27.781  1.00 41.33  ? 85   THR A CG2 1 
ATOM   423  N N   . ASP A  1 59  ? -86.907 -12.322 29.068  1.00 39.97  ? 86   ASP A N   1 
ATOM   424  C CA  . ASP A  1 59  ? -85.875 -11.966 30.033  1.00 31.11  ? 86   ASP A CA  1 
ATOM   425  C C   . ASP A  1 59  ? -85.102 -10.728 29.607  1.00 31.32  ? 86   ASP A C   1 
ATOM   426  O O   . ASP A  1 59  ? -84.370 -10.145 30.402  1.00 38.79  ? 86   ASP A O   1 
ATOM   427  C CB  . ASP A  1 59  ? -84.913 -13.134 30.234  1.00 22.64  ? 86   ASP A CB  1 
ATOM   428  C CG  . ASP A  1 59  ? -85.635 -14.433 30.513  1.00 31.30  ? 86   ASP A CG  1 
ATOM   429  O OD1 . ASP A  1 59  ? -86.773 -14.388 31.030  1.00 35.53  ? 86   ASP A OD1 1 
ATOM   430  O OD2 . ASP A  1 59  ? -85.067 -15.502 30.207  1.00 31.32  1 86   ASP A OD2 1 
ATOM   431  N N   . TYR A  1 60  ? -85.276 -10.315 28.358  1.00 30.82  ? 87   TYR A N   1 
ATOM   432  C CA  . TYR A  1 60  ? -84.532 -9.177  27.825  1.00 30.52  ? 87   TYR A CA  1 
ATOM   433  C C   . TYR A  1 60  ? -84.855 -7.857  28.524  1.00 34.59  ? 87   TYR A C   1 
ATOM   434  O O   . TYR A  1 60  ? -84.240 -6.832  28.231  1.00 33.65  ? 87   TYR A O   1 
ATOM   435  C CB  . TYR A  1 60  ? -84.764 -9.038  26.322  1.00 29.54  ? 87   TYR A CB  1 
ATOM   436  C CG  . TYR A  1 60  ? -83.974 -10.011 25.477  1.00 29.76  ? 87   TYR A CG  1 
ATOM   437  C CD1 . TYR A  1 60  ? -82.661 -9.743  25.113  1.00 26.44  ? 87   TYR A CD1 1 
ATOM   438  C CD2 . TYR A  1 60  ? -84.545 -11.191 25.029  1.00 36.34  ? 87   TYR A CD2 1 
ATOM   439  C CE1 . TYR A  1 60  ? -81.938 -10.631 24.330  1.00 21.08  ? 87   TYR A CE1 1 
ATOM   440  C CE2 . TYR A  1 60  ? -83.828 -12.084 24.245  1.00 31.07  ? 87   TYR A CE2 1 
ATOM   441  C CZ  . TYR A  1 60  ? -82.528 -11.799 23.901  1.00 18.99  ? 87   TYR A CZ  1 
ATOM   442  O OH  . TYR A  1 60  ? -81.825 -12.690 23.124  1.00 13.14  ? 87   TYR A OH  1 
ATOM   443  N N   . GLN A  1 61  ? -85.820 -7.885  29.439  1.00 40.81  ? 88   GLN A N   1 
ATOM   444  C CA  . GLN A  1 61  ? -86.182 -6.706  30.221  1.00 44.97  ? 88   GLN A CA  1 
ATOM   445  C C   . GLN A  1 61  ? -85.066 -6.332  31.186  1.00 36.31  ? 88   GLN A C   1 
ATOM   446  O O   . GLN A  1 61  ? -84.814 -5.151  31.442  1.00 28.33  ? 88   GLN A O   1 
ATOM   447  C CB  . GLN A  1 61  ? -87.469 -6.958  31.008  1.00 44.72  ? 88   GLN A CB  1 
ATOM   448  C CG  . GLN A  1 61  ? -88.732 -7.015  30.165  1.00 47.15  ? 88   GLN A CG  1 
ATOM   449  C CD  . GLN A  1 61  ? -89.975 -7.179  31.015  1.00 51.17  ? 88   GLN A CD  1 
ATOM   450  O OE1 . GLN A  1 61  ? -89.992 -7.973  31.956  1.00 55.48  ? 88   GLN A OE1 1 
ATOM   451  N NE2 . GLN A  1 61  ? -91.019 -6.416  30.699  1.00 45.12  ? 88   GLN A NE2 1 
ATOM   452  N N   . GLN A  1 62  ? -84.393 -7.353  31.707  1.00 31.96  ? 89   GLN A N   1 
ATOM   453  C CA  . GLN A  1 62  ? -83.373 -7.168  32.730  1.00 38.14  ? 89   GLN A CA  1 
ATOM   454  C C   . GLN A  1 62  ? -82.064 -6.643  32.154  1.00 36.61  ? 89   GLN A C   1 
ATOM   455  O O   . GLN A  1 62  ? -81.066 -6.510  32.869  1.00 36.55  ? 89   GLN A O   1 
ATOM   456  C CB  . GLN A  1 62  ? -83.154 -8.473  33.493  1.00 36.83  ? 89   GLN A CB  1 
ATOM   457  C CG  . GLN A  1 62  ? -84.421 -8.968  34.172  1.00 37.36  ? 89   GLN A CG  1 
ATOM   458  C CD  . GLN A  1 62  ? -84.591 -10.466 34.066  1.00 36.87  ? 89   GLN A CD  1 
ATOM   459  O OE1 . GLN A  1 62  ? -83.619 -11.220 34.152  1.00 35.21  ? 89   GLN A OE1 1 
ATOM   460  N NE2 . GLN A  1 62  ? -85.832 -10.909 33.871  1.00 29.67  ? 89   GLN A NE2 1 
ATOM   461  N N   . LEU A  1 63  ? -82.085 -6.342  30.859  1.00 29.71  ? 90   LEU A N   1 
ATOM   462  C CA  . LEU A  1 63  ? -80.969 -5.692  30.189  1.00 30.65  ? 90   LEU A CA  1 
ATOM   463  C C   . LEU A  1 63  ? -80.740 -4.326  30.828  1.00 31.85  ? 90   LEU A C   1 
ATOM   464  O O   . LEU A  1 63  ? -81.681 -3.706  31.318  1.00 39.18  ? 90   LEU A O   1 
ATOM   465  C CB  . LEU A  1 63  ? -81.290 -5.533  28.703  1.00 31.59  ? 90   LEU A CB  1 
ATOM   466  C CG  . LEU A  1 63  ? -80.188 -5.785  27.670  1.00 30.37  ? 90   LEU A CG  1 
ATOM   467  C CD1 . LEU A  1 63  ? -79.597 -7.176  27.816  1.00 21.87  ? 90   LEU A CD1 1 
ATOM   468  C CD2 . LEU A  1 63  ? -80.739 -5.594  26.271  1.00 32.76  ? 90   LEU A CD2 1 
ATOM   469  N N   . PRO A  1 64  ? -79.486 -3.853  30.841  1.00 31.18  ? 91   PRO A N   1 
ATOM   470  C CA  . PRO A  1 64  ? -79.242 -2.538  31.440  1.00 41.98  ? 91   PRO A CA  1 
ATOM   471  C C   . PRO A  1 64  ? -79.888 -1.414  30.626  1.00 43.14  ? 91   PRO A C   1 
ATOM   472  O O   . PRO A  1 64  ? -79.747 -1.365  29.399  1.00 38.16  ? 91   PRO A O   1 
ATOM   473  C CB  . PRO A  1 64  ? -77.711 -2.421  31.422  1.00 38.93  ? 91   PRO A CB  1 
ATOM   474  C CG  . PRO A  1 64  ? -77.270 -3.344  30.338  1.00 28.62  ? 91   PRO A CG  1 
ATOM   475  C CD  . PRO A  1 64  ? -78.242 -4.485  30.369  1.00 31.71  ? 91   PRO A CD  1 
ATOM   476  N N   . LYS A  1 65  ? -80.591 -0.522  31.316  1.00 38.11  ? 92   LYS A N   1 
ATOM   477  C CA  . LYS A  1 65  ? -81.305 0.568   30.662  1.00 40.52  ? 92   LYS A CA  1 
ATOM   478  C C   . LYS A  1 65  ? -80.406 1.776   30.410  1.00 43.18  ? 92   LYS A C   1 
ATOM   479  O O   . LYS A  1 65  ? -79.545 2.093   31.229  1.00 47.49  ? 92   LYS A O   1 
ATOM   480  C CB  . LYS A  1 65  ? -82.498 0.987   31.520  1.00 46.41  ? 92   LYS A CB  1 
ATOM   481  C CG  . LYS A  1 65  ? -83.198 -0.177  32.204  1.00 48.96  ? 92   LYS A CG  1 
ATOM   482  C CD  . LYS A  1 65  ? -84.495 0.265   32.864  1.00 45.12  ? 92   LYS A CD  1 
ATOM   483  C CE  . LYS A  1 65  ? -85.238 -0.916  33.468  1.00 37.15  ? 92   LYS A CE  1 
ATOM   484  N NZ  . LYS A  1 65  ? -86.534 -0.510  34.073  1.00 34.51  1 92   LYS A NZ  1 
ATOM   485  N N   . LYS A  1 66  ? -80.618 2.444   29.279  1.00 45.30  ? 93   LYS A N   1 
ATOM   486  C CA  . LYS A  1 66  ? -79.908 3.681   28.943  1.00 48.88  ? 93   LYS A CA  1 
ATOM   487  C C   . LYS A  1 66  ? -78.395 3.547   29.042  1.00 43.03  ? 93   LYS A C   1 
ATOM   488  O O   . LYS A  1 66  ? -77.754 4.324   29.749  1.00 41.59  ? 93   LYS A O   1 
ATOM   489  C CB  . LYS A  1 66  ? -80.353 4.831   29.854  1.00 53.65  ? 93   LYS A CB  1 
ATOM   490  C CG  . LYS A  1 66  ? -81.802 5.269   29.701  1.00 59.34  ? 93   LYS A CG  1 
ATOM   491  C CD  . LYS A  1 66  ? -82.084 6.476   30.594  1.00 66.08  ? 93   LYS A CD  1 
ATOM   492  C CE  . LYS A  1 66  ? -83.522 6.971   30.470  1.00 71.22  ? 93   LYS A CE  1 
ATOM   493  N NZ  . LYS A  1 66  ? -84.513 6.093   31.161  1.00 66.26  1 93   LYS A NZ  1 
ATOM   494  N N   . LEU A  1 67  ? -77.822 2.578   28.334  1.00 41.21  ? 94   LEU A N   1 
ATOM   495  C CA  . LEU A  1 67  ? -76.400 2.281   28.494  1.00 39.46  ? 94   LEU A CA  1 
ATOM   496  C C   . LEU A  1 67  ? -75.459 3.184   27.692  1.00 36.29  ? 94   LEU A C   1 
ATOM   497  O O   . LEU A  1 67  ? -74.439 3.636   28.216  1.00 39.02  ? 94   LEU A O   1 
ATOM   498  C CB  . LEU A  1 67  ? -76.109 0.815   28.182  1.00 35.18  ? 94   LEU A CB  1 
ATOM   499  C CG  . LEU A  1 67  ? -74.882 0.312   28.939  1.00 31.56  ? 94   LEU A CG  1 
ATOM   500  C CD1 . LEU A  1 67  ? -75.202 0.230   30.426  1.00 36.75  ? 94   LEU A CD1 1 
ATOM   501  C CD2 . LEU A  1 67  ? -74.414 -1.027  28.402  1.00 31.30  ? 94   LEU A CD2 1 
ATOM   502  N N   . ARG A  1 68  ? -75.796 3.422   26.426  1.00 29.96  ? 95   ARG A N   1 
ATOM   503  C CA  . ARG A  1 68  ? -75.005 4.289   25.546  1.00 32.31  ? 95   ARG A CA  1 
ATOM   504  C C   . ARG A  1 68  ? -73.549 3.843   25.352  1.00 29.43  ? 95   ARG A C   1 
ATOM   505  O O   . ARG A  1 68  ? -72.622 4.482   25.845  1.00 31.81  ? 95   ARG A O   1 
ATOM   506  C CB  . ARG A  1 68  ? -75.056 5.739   26.032  1.00 34.27  ? 95   ARG A CB  1 
ATOM   507  C CG  . ARG A  1 68  ? -76.400 6.405   25.832  1.00 34.82  ? 95   ARG A CG  1 
ATOM   508  C CD  . ARG A  1 68  ? -76.756 6.456   24.354  1.00 43.77  ? 95   ARG A CD  1 
ATOM   509  N NE  . ARG A  1 68  ? -78.047 7.099   24.112  1.00 55.48  ? 95   ARG A NE  1 
ATOM   510  C CZ  . ARG A  1 68  ? -79.205 6.452   23.999  1.00 40.80  ? 95   ARG A CZ  1 
ATOM   511  N NH1 . ARG A  1 68  ? -79.252 5.130   24.106  1.00 35.36  1 95   ARG A NH1 1 
ATOM   512  N NH2 . ARG A  1 68  ? -80.321 7.133   23.778  1.00 34.63  ? 95   ARG A NH2 1 
ATOM   513  N N   . ILE A  1 69  ? -73.360 2.757   24.614  1.00 26.07  ? 96   ILE A N   1 
ATOM   514  C CA  . ILE A  1 69  ? -72.034 2.196   24.384  1.00 27.85  ? 96   ILE A CA  1 
ATOM   515  C C   . ILE A  1 69  ? -71.325 2.905   23.229  1.00 31.84  ? 96   ILE A C   1 
ATOM   516  O O   . ILE A  1 69  ? -70.113 2.787   23.057  1.00 36.58  ? 96   ILE A O   1 
ATOM   517  C CB  . ILE A  1 69  ? -72.125 0.678   24.114  1.00 24.47  ? 96   ILE A CB  1 
ATOM   518  C CG1 . ILE A  1 69  ? -72.977 0.009   25.193  1.00 23.61  ? 96   ILE A CG1 1 
ATOM   519  C CG2 . ILE A  1 69  ? -70.746 0.037   24.056  1.00 19.68  ? 96   ILE A CG2 1 
ATOM   520  C CD1 . ILE A  1 69  ? -73.059 -1.491  25.060  1.00 21.24  ? 96   ILE A CD1 1 
ATOM   521  N N   . GLY A  1 70  ? -72.084 3.660   22.445  1.00 33.77  ? 97   GLY A N   1 
ATOM   522  C CA  . GLY A  1 70  ? -71.515 4.389   21.326  1.00 35.44  ? 97   GLY A CA  1 
ATOM   523  C C   . GLY A  1 70  ? -70.962 3.485   20.244  1.00 33.03  ? 97   GLY A C   1 
ATOM   524  O O   . GLY A  1 70  ? -71.298 2.302   20.182  1.00 31.88  ? 97   GLY A O   1 
ATOM   525  N N   . GLU A  1 71  ? -70.116 4.045   19.386  1.00 32.77  ? 98   GLU A N   1 
ATOM   526  C CA  . GLU A  1 71  ? -69.568 3.294   18.263  1.00 35.15  ? 98   GLU A CA  1 
ATOM   527  C C   . GLU A  1 71  ? -68.776 2.074   18.725  1.00 37.74  ? 98   GLU A C   1 
ATOM   528  O O   . GLU A  1 71  ? -68.113 2.100   19.766  1.00 29.51  ? 98   GLU A O   1 
ATOM   529  C CB  . GLU A  1 71  ? -68.717 4.193   17.360  1.00 40.71  ? 98   GLU A CB  1 
ATOM   530  C CG  . GLU A  1 71  ? -69.512 4.900   16.260  1.00 54.81  ? 98   GLU A CG  1 
ATOM   531  C CD  . GLU A  1 71  ? -69.661 6.400   16.488  1.00 67.57  ? 98   GLU A CD  1 
ATOM   532  O OE1 . GLU A  1 71  ? -68.898 6.964   17.308  1.00 62.19  ? 98   GLU A OE1 1 
ATOM   533  O OE2 . GLU A  1 71  ? -70.543 7.012   15.841  1.00 55.91  1 98   GLU A OE2 1 
ATOM   534  N N   . VAL A  1 72  ? -68.878 0.999   17.950  1.00 38.53  ? 99   VAL A N   1 
ATOM   535  C CA  . VAL A  1 72  ? -68.206 -0.255  18.260  1.00 32.79  ? 99   VAL A CA  1 
ATOM   536  C C   . VAL A  1 72  ? -68.029 -1.044  16.967  1.00 30.39  ? 99   VAL A C   1 
ATOM   537  O O   . VAL A  1 72  ? -68.876 -0.992  16.074  1.00 29.72  ? 99   VAL A O   1 
ATOM   538  C CB  . VAL A  1 72  ? -68.992 -1.073  19.320  1.00 25.96  ? 99   VAL A CB  1 
ATOM   539  C CG1 . VAL A  1 72  ? -69.689 -2.269  18.695  1.00 23.10  ? 99   VAL A CG1 1 
ATOM   540  C CG2 . VAL A  1 72  ? -68.070 -1.523  20.429  1.00 22.61  ? 99   VAL A CG2 1 
ATOM   541  N N   . ASP A  1 73  ? -66.916 -1.752  16.849  1.00 29.10  ? 100  ASP A N   1 
ATOM   542  C CA  . ASP A  1 73  ? -66.630 -2.450  15.607  1.00 31.26  ? 100  ASP A CA  1 
ATOM   543  C C   . ASP A  1 73  ? -67.215 -3.845  15.589  1.00 22.78  ? 100  ASP A C   1 
ATOM   544  O O   . ASP A  1 73  ? -67.657 -4.321  14.549  1.00 23.06  ? 100  ASP A O   1 
ATOM   545  C CB  . ASP A  1 73  ? -65.125 -2.499  15.349  1.00 38.83  ? 100  ASP A CB  1 
ATOM   546  C CG  . ASP A  1 73  ? -64.579 -1.171  14.863  1.00 54.03  ? 100  ASP A CG  1 
ATOM   547  O OD1 . ASP A  1 73  ? -65.241 -0.132  15.092  1.00 43.35  ? 100  ASP A OD1 1 
ATOM   548  O OD2 . ASP A  1 73  ? -63.490 -1.164  14.250  1.00 73.13  1 100  ASP A OD2 1 
ATOM   549  N N   . ARG A  1 74  ? -67.224 -4.499  16.741  1.00 20.63  ? 101  ARG A N   1 
ATOM   550  C CA  . ARG A  1 74  ? -67.630 -5.893  16.790  1.00 16.42  ? 101  ARG A CA  1 
ATOM   551  C C   . ARG A  1 74  ? -68.636 -6.191  17.894  1.00 13.66  ? 101  ARG A C   1 
ATOM   552  O O   . ARG A  1 74  ? -68.404 -5.882  19.057  1.00 15.98  ? 101  ARG A O   1 
ATOM   553  C CB  . ARG A  1 74  ? -66.405 -6.791  16.938  1.00 15.81  ? 101  ARG A CB  1 
ATOM   554  C CG  . ARG A  1 74  ? -66.742 -8.258  17.066  1.00 17.63  ? 101  ARG A CG  1 
ATOM   555  C CD  . ARG A  1 74  ? -65.491 -9.117  17.051  1.00 28.87  ? 101  ARG A CD  1 
ATOM   556  N NE  . ARG A  1 74  ? -65.439 -10.009 18.206  1.00 31.05  ? 101  ARG A NE  1 
ATOM   557  C CZ  . ARG A  1 74  ? -64.720 -9.772  19.299  1.00 34.95  ? 101  ARG A CZ  1 
ATOM   558  N NH1 . ARG A  1 74  ? -64.737 -10.638 20.300  1.00 43.86  1 101  ARG A NH1 1 
ATOM   559  N NH2 . ARG A  1 74  ? -63.981 -8.673  19.391  1.00 30.62  ? 101  ARG A NH2 1 
ATOM   560  N N   . VAL A  1 75  ? -69.758 -6.793  17.521  1.00 10.70  ? 102  VAL A N   1 
ATOM   561  C CA  . VAL A  1 75  ? -70.741 -7.230  18.499  1.00 8.15   ? 102  VAL A CA  1 
ATOM   562  C C   . VAL A  1 75  ? -70.800 -8.748  18.526  1.00 7.54   ? 102  VAL A C   1 
ATOM   563  O O   . VAL A  1 75  ? -70.872 -9.396  17.486  1.00 7.43   ? 102  VAL A O   1 
ATOM   564  C CB  . VAL A  1 75  ? -72.134 -6.678  18.197  1.00 6.86   ? 102  VAL A CB  1 
ATOM   565  C CG1 . VAL A  1 75  ? -73.116 -7.135  19.254  1.00 6.42   ? 102  VAL A CG1 1 
ATOM   566  C CG2 . VAL A  1 75  ? -72.093 -5.173  18.135  1.00 8.87   ? 102  VAL A CG2 1 
ATOM   567  N N   . GLN A  1 76  ? -70.763 -9.310  19.724  1.00 7.75   ? 103  GLN A N   1 
ATOM   568  C CA  . GLN A  1 76  ? -70.754 -10.752 19.886  1.00 8.48   ? 103  GLN A CA  1 
ATOM   569  C C   . GLN A  1 76  ? -71.819 -11.182 20.884  1.00 11.16  ? 103  GLN A C   1 
ATOM   570  O O   . GLN A  1 76  ? -71.818 -10.751 22.035  1.00 14.52  ? 103  GLN A O   1 
ATOM   571  C CB  . GLN A  1 76  ? -69.374 -11.209 20.352  1.00 11.18  ? 103  GLN A CB  1 
ATOM   572  C CG  . GLN A  1 76  ? -69.312 -12.641 20.845  1.00 14.22  ? 103  GLN A CG  1 
ATOM   573  C CD  . GLN A  1 76  ? -67.942 -12.998 21.398  1.00 22.61  ? 103  GLN A CD  1 
ATOM   574  O OE1 . GLN A  1 76  ? -67.059 -12.142 21.491  1.00 24.55  ? 103  GLN A OE1 1 
ATOM   575  N NE2 . GLN A  1 76  ? -67.758 -14.265 21.771  1.00 21.58  ? 103  GLN A NE2 1 
ATOM   576  N N   . MET A  1 77  ? -72.739 -12.025 20.435  1.00 8.73   ? 104  MET A N   1 
ATOM   577  C CA  . MET A  1 77  ? -73.781 -12.531 21.307  1.00 7.55   ? 104  MET A CA  1 
ATOM   578  C C   . MET A  1 77  ? -73.613 -14.026 21.514  1.00 9.58   ? 104  MET A C   1 
ATOM   579  O O   . MET A  1 77  ? -73.611 -14.792 20.555  1.00 9.10   ? 104  MET A O   1 
ATOM   580  C CB  . MET A  1 77  ? -75.149 -12.260 20.700  1.00 7.72   ? 104  MET A CB  1 
ATOM   581  C CG  . MET A  1 77  ? -75.411 -10.809 20.349  1.00 7.61   ? 104  MET A CG  1 
ATOM   582  S SD  . MET A  1 77  ? -77.167 -10.509 20.046  1.00 2.91   ? 104  MET A SD  1 
ATOM   583  C CE  . MET A  1 77  ? -77.170 -8.726  20.056  1.00 4.82   ? 104  MET A CE  1 
ATOM   584  N N   . ARG A  1 78  ? -73.476 -14.444 22.765  1.00 11.53  ? 105  ARG A N   1 
ATOM   585  C CA  . ARG A  1 78  ? -73.369 -15.862 23.069  1.00 11.76  ? 105  ARG A CA  1 
ATOM   586  C C   . ARG A  1 78  ? -74.536 -16.350 23.920  1.00 12.42  ? 105  ARG A C   1 
ATOM   587  O O   . ARG A  1 78  ? -74.957 -15.670 24.852  1.00 14.70  ? 105  ARG A O   1 
ATOM   588  C CB  . ARG A  1 78  ? -72.045 -16.162 23.764  1.00 16.92  ? 105  ARG A CB  1 
ATOM   589  C CG  . ARG A  1 78  ? -70.819 -15.915 22.899  1.00 22.97  ? 105  ARG A CG  1 
ATOM   590  C CD  . ARG A  1 78  ? -69.532 -16.153 23.688  1.00 29.30  ? 105  ARG A CD  1 
ATOM   591  N NE  . ARG A  1 78  ? -69.484 -17.496 24.258  1.00 36.55  ? 105  ARG A NE  1 
ATOM   592  C CZ  . ARG A  1 78  ? -68.582 -17.898 25.146  1.00 31.64  ? 105  ARG A CZ  1 
ATOM   593  N NH1 . ARG A  1 78  ? -68.616 -19.138 25.611  1.00 35.99  1 105  ARG A NH1 1 
ATOM   594  N NH2 . ARG A  1 78  ? -67.655 -17.055 25.574  1.00 28.97  ? 105  ARG A NH2 1 
ATOM   595  N N   . ARG A  1 79  ? -75.057 -17.524 23.572  1.00 12.58  ? 106  ARG A N   1 
ATOM   596  C CA  . ARG A  1 79  ? -76.127 -18.181 24.320  1.00 12.38  ? 106  ARG A CA  1 
ATOM   597  C C   . ARG A  1 79  ? -77.405 -17.354 24.384  1.00 10.44  ? 106  ARG A C   1 
ATOM   598  O O   . ARG A  1 79  ? -78.096 -17.350 25.399  1.00 11.86  ? 106  ARG A O   1 
ATOM   599  C CB  . ARG A  1 79  ? -75.665 -18.515 25.740  1.00 17.68  ? 106  ARG A CB  1 
ATOM   600  C CG  . ARG A  1 79  ? -74.491 -19.464 25.820  1.00 16.72  ? 106  ARG A CG  1 
ATOM   601  C CD  . ARG A  1 79  ? -73.939 -19.489 27.234  1.00 23.02  ? 106  ARG A CD  1 
ATOM   602  N NE  . ARG A  1 79  ? -75.004 -19.553 28.233  1.00 31.55  ? 106  ARG A NE  1 
ATOM   603  C CZ  . ARG A  1 79  ? -75.360 -20.658 28.882  1.00 37.61  ? 106  ARG A CZ  1 
ATOM   604  N NH1 . ARG A  1 79  ? -76.341 -20.620 29.776  1.00 31.12  1 106  ARG A NH1 1 
ATOM   605  N NH2 . ARG A  1 79  ? -74.729 -21.800 28.641  1.00 39.14  ? 106  ARG A NH2 1 
ATOM   606  N N   . CYS A  1 80  ? -77.728 -16.669 23.296  1.00 10.13  ? 107  CYS A N   1 
ATOM   607  C CA  . CYS A  1 80  ? -78.880 -15.776 23.292  1.00 12.11  ? 107  CYS A CA  1 
ATOM   608  C C   . CYS A  1 80  ? -80.137 -16.323 22.599  1.00 13.51  ? 107  CYS A C   1 
ATOM   609  O O   . CYS A  1 80  ? -80.050 -17.087 21.637  1.00 12.72  ? 107  CYS A O   1 
ATOM   610  C CB  . CYS A  1 80  ? -78.490 -14.428 22.692  1.00 10.51  ? 107  CYS A CB  1 
ATOM   611  S SG  . CYS A  1 80  ? -77.476 -13.436 23.802  1.00 13.83  ? 107  CYS A SG  1 
ATOM   612  N N   . MET A  1 81  ? -81.302 -15.928 23.113  1.00 14.23  ? 108  MET A N   1 
ATOM   613  C CA  . MET A  1 81  ? -82.571 -16.197 22.455  1.00 12.18  ? 108  MET A CA  1 
ATOM   614  C C   . MET A  1 81  ? -82.624 -15.349 21.204  1.00 12.40  ? 108  MET A C   1 
ATOM   615  O O   . MET A  1 81  ? -82.319 -14.160 21.256  1.00 11.81  ? 108  MET A O   1 
ATOM   616  C CB  . MET A  1 81  ? -83.750 -15.759 23.328  1.00 13.60  ? 108  MET A CB  1 
ATOM   617  C CG  . MET A  1 81  ? -83.857 -16.399 24.686  1.00 15.50  ? 108  MET A CG  1 
ATOM   618  S SD  . MET A  1 81  ? -84.047 -18.175 24.607  1.00 26.03  ? 108  MET A SD  1 
ATOM   619  C CE  . MET A  1 81  ? -82.564 -18.672 25.471  1.00 24.60  ? 108  MET A CE  1 
ATOM   620  N N   . LEU A  1 82  ? -83.010 -15.944 20.082  1.00 11.85  ? 109  LEU A N   1 
ATOM   621  C CA  . LEU A  1 82  ? -83.427 -15.146 18.943  1.00 11.24  ? 109  LEU A CA  1 
ATOM   622  C C   . LEU A  1 82  ? -84.630 -14.341 19.424  1.00 13.80  ? 109  LEU A C   1 
ATOM   623  O O   . LEU A  1 82  ? -85.513 -14.879 20.097  1.00 19.09  ? 109  LEU A O   1 
ATOM   624  C CB  . LEU A  1 82  ? -83.796 -16.036 17.756  1.00 11.53  ? 109  LEU A CB  1 
ATOM   625  C CG  . LEU A  1 82  ? -82.635 -16.661 16.977  1.00 9.67   ? 109  LEU A CG  1 
ATOM   626  C CD1 . LEU A  1 82  ? -83.091 -17.890 16.205  1.00 8.58   ? 109  LEU A CD1 1 
ATOM   627  C CD2 . LEU A  1 82  ? -82.025 -15.638 16.033  1.00 7.37   ? 109  LEU A CD2 1 
ATOM   628  N N   . PRO A  1 83  ? -84.657 -13.042 19.103  1.00 10.68  ? 110  PRO A N   1 
ATOM   629  C CA  . PRO A  1 83  ? -85.611 -12.092 19.686  1.00 13.48  ? 110  PRO A CA  1 
ATOM   630  C C   . PRO A  1 83  ? -87.010 -12.111 19.072  1.00 17.76  ? 110  PRO A C   1 
ATOM   631  O O   . PRO A  1 83  ? -87.512 -11.044 18.722  1.00 15.78  ? 110  PRO A O   1 
ATOM   632  C CB  . PRO A  1 83  ? -84.951 -10.744 19.412  1.00 13.55  ? 110  PRO A CB  1 
ATOM   633  C CG  . PRO A  1 83  ? -84.170 -10.967 18.170  1.00 11.22  ? 110  PRO A CG  1 
ATOM   634  C CD  . PRO A  1 83  ? -83.707 -12.388 18.189  1.00 8.93   ? 110  PRO A CD  1 
ATOM   635  N N   . GLY A  1 84  ? -87.620 -13.290 18.954  1.00 20.79  ? 111  GLY A N   1 
ATOM   636  C CA  . GLY A  1 84  ? -88.979 -13.430 18.447  1.00 19.96  ? 111  GLY A CA  1 
ATOM   637  C C   . GLY A  1 84  ? -89.236 -12.856 17.060  1.00 24.95  ? 111  GLY A C   1 
ATOM   638  O O   . GLY A  1 84  ? -88.613 -13.266 16.081  1.00 23.63  ? 111  GLY A O   1 
ATOM   639  N N   . HIS A  1 85  ? -90.177 -11.917 16.980  1.00 27.90  ? 112  HIS A N   1 
ATOM   640  C CA  . HIS A  1 85  ? -90.465 -11.200 15.744  1.00 22.38  ? 112  HIS A CA  1 
ATOM   641  C C   . HIS A  1 85  ? -89.875 -9.800  15.828  1.00 23.04  ? 112  HIS A C   1 
ATOM   642  O O   . HIS A  1 85  ? -90.405 -8.851  15.250  1.00 24.91  ? 112  HIS A O   1 
ATOM   643  C CB  . HIS A  1 85  ? -91.973 -11.087 15.524  1.00 29.63  ? 112  HIS A CB  1 
ATOM   644  C CG  . HIS A  1 85  ? -92.658 -12.395 15.278  1.00 35.02  ? 112  HIS A CG  1 
ATOM   645  N ND1 . HIS A  1 85  ? -93.007 -13.256 16.296  1.00 40.97  ? 112  HIS A ND1 1 
ATOM   646  C CD2 . HIS A  1 85  ? -93.078 -12.980 14.130  1.00 34.79  ? 112  HIS A CD2 1 
ATOM   647  C CE1 . HIS A  1 85  ? -93.603 -14.320 15.785  1.00 44.93  ? 112  HIS A CE1 1 
ATOM   648  N NE2 . HIS A  1 85  ? -93.658 -14.177 14.473  1.00 31.34  ? 112  HIS A NE2 1 
ATOM   649  N N   . THR A  1 86  ? -88.787 -9.669  16.573  1.00 20.68  ? 113  THR A N   1 
ATOM   650  C CA  . THR A  1 86  ? -88.138 -8.380  16.735  1.00 21.47  ? 113  THR A CA  1 
ATOM   651  C C   . THR A  1 86  ? -86.768 -8.445  16.086  1.00 19.26  ? 113  THR A C   1 
ATOM   652  O O   . THR A  1 86  ? -86.061 -9.431  16.251  1.00 18.75  ? 113  THR A O   1 
ATOM   653  C CB  . THR A  1 86  ? -87.982 -8.014  18.227  1.00 21.57  ? 113  THR A CB  1 
ATOM   654  O OG1 . THR A  1 86  ? -89.264 -8.046  18.868  1.00 27.48  ? 113  THR A OG1 1 
ATOM   655  C CG2 . THR A  1 86  ? -87.376 -6.631  18.386  1.00 20.80  ? 113  THR A CG2 1 
ATOM   656  N N   . PRO A  1 87  ? -86.403 -7.409  15.315  1.00 18.73  ? 114  PRO A N   1 
ATOM   657  C CA  . PRO A  1 87  ? -85.049 -7.323  14.768  1.00 14.49  ? 114  PRO A CA  1 
ATOM   658  C C   . PRO A  1 87  ? -84.029 -7.313  15.898  1.00 15.89  ? 114  PRO A C   1 
ATOM   659  O O   . PRO A  1 87  ? -84.252 -6.661  16.919  1.00 13.74  ? 114  PRO A O   1 
ATOM   660  C CB  . PRO A  1 87  ? -85.041 -5.963  14.068  1.00 15.49  ? 114  PRO A CB  1 
ATOM   661  C CG  . PRO A  1 87  ? -86.449 -5.693  13.740  1.00 19.51  ? 114  PRO A CG  1 
ATOM   662  C CD  . PRO A  1 87  ? -87.262 -6.311  14.839  1.00 23.72  ? 114  PRO A CD  1 
ATOM   663  N N   . ILE A  1 88  ? -82.930 -8.037  15.719  1.00 14.81  ? 115  ILE A N   1 
ATOM   664  C CA  . ILE A  1 88  ? -81.862 -8.042  16.704  1.00 11.42  ? 115  ILE A CA  1 
ATOM   665  C C   . ILE A  1 88  ? -81.337 -6.628  16.845  1.00 12.05  ? 115  ILE A C   1 
ATOM   666  O O   . ILE A  1 88  ? -80.981 -6.194  17.938  1.00 13.93  ? 115  ILE A O   1 
ATOM   667  C CB  . ILE A  1 88  ? -80.707 -8.940  16.270  1.00 9.56   ? 115  ILE A CB  1 
ATOM   668  C CG1 . ILE A  1 88  ? -81.192 -10.372 16.046  1.00 8.83   ? 115  ILE A CG1 1 
ATOM   669  C CG2 . ILE A  1 88  ? -79.613 -8.906  17.302  1.00 8.37   ? 115  ILE A CG2 1 
ATOM   670  C CD1 . ILE A  1 88  ? -80.161 -11.264 15.386  1.00 5.88   ? 115  ILE A CD1 1 
ATOM   671  N N   . ALA A  1 89  ? -81.320 -5.903  15.728  1.00 11.72  ? 116  ALA A N   1 
ATOM   672  C CA  . ALA A  1 89  ? -80.848 -4.524  15.697  1.00 11.48  ? 116  ALA A CA  1 
ATOM   673  C C   . ALA A  1 89  ? -81.595 -3.633  16.680  1.00 13.84  ? 116  ALA A C   1 
ATOM   674  O O   . ALA A  1 89  ? -81.152 -2.530  16.979  1.00 15.34  ? 116  ALA A O   1 
ATOM   675  C CB  . ALA A  1 89  ? -80.957 -3.962  14.300  1.00 12.31  ? 116  ALA A CB  1 
ATOM   676  N N   . SER A  1 90  ? -82.733 -4.112  17.173  1.00 14.46  ? 117  SER A N   1 
ATOM   677  C CA  . SER A  1 90  ? -83.475 -3.397  18.199  1.00 15.71  ? 117  SER A CA  1 
ATOM   678  C C   . SER A  1 90  ? -82.701 -3.450  19.502  1.00 14.34  ? 117  SER A C   1 
ATOM   679  O O   . SER A  1 90  ? -82.452 -2.420  20.123  1.00 14.65  ? 117  SER A O   1 
ATOM   680  C CB  . SER A  1 90  ? -84.860 -4.010  18.395  1.00 18.03  ? 117  SER A CB  1 
ATOM   681  O OG  . SER A  1 90  ? -85.581 -4.047  17.177  1.00 20.29  ? 117  SER A OG  1 
ATOM   682  N N   . ILE A  1 91  ? -82.323 -4.659  19.906  1.00 14.13  ? 118  ILE A N   1 
ATOM   683  C CA  . ILE A  1 91  ? -81.530 -4.858  21.115  1.00 16.54  ? 118  ILE A CA  1 
ATOM   684  C C   . ILE A  1 91  ? -80.247 -4.029  21.054  1.00 15.25  ? 118  ILE A C   1 
ATOM   685  O O   . ILE A  1 91  ? -79.846 -3.406  22.037  1.00 17.53  ? 118  ILE A O   1 
ATOM   686  C CB  . ILE A  1 91  ? -81.174 -6.348  21.336  1.00 12.02  ? 118  ILE A CB  1 
ATOM   687  C CG1 . ILE A  1 91  ? -82.393 -7.239  21.089  1.00 14.87  ? 118  ILE A CG1 1 
ATOM   688  C CG2 . ILE A  1 91  ? -80.657 -6.567  22.738  1.00 7.94   ? 118  ILE A CG2 1 
ATOM   689  C CD1 . ILE A  1 91  ? -82.143 -8.711  21.356  1.00 10.77  ? 118  ILE A CD1 1 
ATOM   690  N N   . LEU A  1 92  ? -79.621 -4.007  19.886  1.00 11.14  ? 119  LEU A N   1 
ATOM   691  C CA  . LEU A  1 92  ? -78.425 -3.207  19.690  1.00 12.79  ? 119  LEU A CA  1 
ATOM   692  C C   . LEU A  1 92  ? -78.720 -1.711  19.850  1.00 18.37  ? 119  LEU A C   1 
ATOM   693  O O   . LEU A  1 92  ? -77.876 -0.953  20.327  1.00 19.42  ? 119  LEU A O   1 
ATOM   694  C CB  . LEU A  1 92  ? -77.816 -3.503  18.320  1.00 15.16  ? 119  LEU A CB  1 
ATOM   695  C CG  . LEU A  1 92  ? -77.455 -4.969  18.068  1.00 10.37  ? 119  LEU A CG  1 
ATOM   696  C CD1 . LEU A  1 92  ? -77.022 -5.193  16.637  1.00 9.02   ? 119  LEU A CD1 1 
ATOM   697  C CD2 . LEU A  1 92  ? -76.360 -5.389  19.003  1.00 11.16  ? 119  LEU A CD2 1 
ATOM   698  N N   . ASP A  1 93  ? -79.919 -1.290  19.457  1.00 18.20  ? 120  ASP A N   1 
ATOM   699  C CA  . ASP A  1 93  ? -80.335 0.097   19.640  1.00 17.24  ? 120  ASP A CA  1 
ATOM   700  C C   . ASP A  1 93  ? -80.615 0.399   21.104  1.00 23.16  ? 120  ASP A C   1 
ATOM   701  O O   . ASP A  1 93  ? -80.303 1.487   21.594  1.00 23.52  ? 120  ASP A O   1 
ATOM   702  C CB  . ASP A  1 93  ? -81.584 0.397   18.818  1.00 14.69  ? 120  ASP A CB  1 
ATOM   703  C CG  . ASP A  1 93  ? -81.315 0.374   17.342  1.00 20.86  ? 120  ASP A CG  1 
ATOM   704  O OD1 . ASP A  1 93  ? -80.138 0.552   16.960  1.00 23.55  ? 120  ASP A OD1 1 
ATOM   705  O OD2 . ASP A  1 93  ? -82.272 0.170   16.566  1.00 21.30  1 120  ASP A OD2 1 
ATOM   706  N N   . TYR A  1 94  ? -81.219 -0.569  21.790  1.00 22.29  ? 121  TYR A N   1 
ATOM   707  C CA  . TYR A  1 94  ? -81.585 -0.423  23.191  1.00 18.15  ? 121  TYR A CA  1 
ATOM   708  C C   . TYR A  1 94  ? -80.345 -0.181  24.019  1.00 21.18  ? 121  TYR A C   1 
ATOM   709  O O   . TYR A  1 94  ? -80.351 0.652   24.924  1.00 29.35  ? 121  TYR A O   1 
ATOM   710  C CB  . TYR A  1 94  ? -82.313 -1.674  23.686  1.00 21.31  ? 121  TYR A CB  1 
ATOM   711  C CG  . TYR A  1 94  ? -82.784 -1.607  25.126  1.00 26.93  ? 121  TYR A CG  1 
ATOM   712  C CD1 . TYR A  1 94  ? -83.874 -0.822  25.491  1.00 33.08  ? 121  TYR A CD1 1 
ATOM   713  C CD2 . TYR A  1 94  ? -82.154 -2.349  26.117  1.00 26.55  ? 121  TYR A CD2 1 
ATOM   714  C CE1 . TYR A  1 94  ? -84.314 -0.766  26.810  1.00 32.58  ? 121  TYR A CE1 1 
ATOM   715  C CE2 . TYR A  1 94  ? -82.586 -2.302  27.437  1.00 32.16  ? 121  TYR A CE2 1 
ATOM   716  C CZ  . TYR A  1 94  ? -83.665 -1.509  27.779  1.00 31.72  ? 121  TYR A CZ  1 
ATOM   717  O OH  . TYR A  1 94  ? -84.089 -1.465  29.091  1.00 20.20  ? 121  TYR A OH  1 
ATOM   718  N N   . LEU A  1 95  ? -79.272 -0.898  23.695  1.00 19.76  ? 122  LEU A N   1 
ATOM   719  C CA  . LEU A  1 95  ? -78.020 -0.766  24.438  1.00 23.05  ? 122  LEU A CA  1 
ATOM   720  C C   . LEU A  1 95  ? -77.185 0.428   23.993  1.00 24.13  ? 122  LEU A C   1 
ATOM   721  O O   . LEU A  1 95  ? -76.130 0.695   24.562  1.00 27.38  ? 122  LEU A O   1 
ATOM   722  C CB  . LEU A  1 95  ? -77.196 -2.050  24.356  1.00 18.78  ? 122  LEU A CB  1 
ATOM   723  C CG  . LEU A  1 95  ? -77.788 -3.212  25.150  1.00 21.41  ? 122  LEU A CG  1 
ATOM   724  C CD1 . LEU A  1 95  ? -76.954 -4.462  24.979  1.00 17.13  ? 122  LEU A CD1 1 
ATOM   725  C CD2 . LEU A  1 95  ? -77.911 -2.840  26.619  1.00 27.85  ? 122  LEU A CD2 1 
ATOM   726  N N   . GLY A  1 96  ? -77.658 1.139   22.976  1.00 22.51  ? 123  GLY A N   1 
ATOM   727  C CA  . GLY A  1 96  ? -77.013 2.363   22.543  1.00 23.17  ? 123  GLY A CA  1 
ATOM   728  C C   . GLY A  1 96  ? -75.842 2.146   21.608  1.00 23.71  ? 123  GLY A C   1 
ATOM   729  O O   . GLY A  1 96  ? -75.069 3.074   21.352  1.00 23.14  ? 123  GLY A O   1 
ATOM   730  N N   . ILE A  1 97  ? -75.712 0.922   21.101  1.00 22.13  ? 124  ILE A N   1 
ATOM   731  C CA  . ILE A  1 97  ? -74.656 0.583   20.152  1.00 22.57  ? 124  ILE A CA  1 
ATOM   732  C C   . ILE A  1 97  ? -74.898 1.258   18.806  1.00 23.80  ? 124  ILE A C   1 
ATOM   733  O O   . ILE A  1 97  ? -76.038 1.380   18.360  1.00 26.66  ? 124  ILE A O   1 
ATOM   734  C CB  . ILE A  1 97  ? -74.569 -0.933  19.930  1.00 17.69  ? 124  ILE A CB  1 
ATOM   735  C CG1 . ILE A  1 97  ? -74.708 -1.673  21.258  1.00 17.37  ? 124  ILE A CG1 1 
ATOM   736  C CG2 . ILE A  1 97  ? -73.265 -1.294  19.240  1.00 22.35  ? 124  ILE A CG2 1 
ATOM   737  C CD1 . ILE A  1 97  ? -74.428 -3.158  21.166  1.00 13.95  ? 124  ILE A CD1 1 
ATOM   738  N N   . VAL A  1 98  ? -73.825 1.698   18.159  1.00 22.35  ? 125  VAL A N   1 
ATOM   739  C CA  . VAL A  1 98  ? -73.952 2.403   16.891  1.00 24.44  ? 125  VAL A CA  1 
ATOM   740  C C   . VAL A  1 98  ? -72.995 1.860   15.831  1.00 29.21  ? 125  VAL A C   1 
ATOM   741  O O   . VAL A  1 98  ? -71.807 1.663   16.093  1.00 33.05  ? 125  VAL A O   1 
ATOM   742  C CB  . VAL A  1 98  ? -73.743 3.922   17.074  1.00 27.43  ? 125  VAL A CB  1 
ATOM   743  C CG1 . VAL A  1 98  ? -73.582 4.611   15.731  1.00 35.01  ? 125  VAL A CG1 1 
ATOM   744  C CG2 . VAL A  1 98  ? -74.904 4.525   17.845  1.00 25.40  ? 125  VAL A CG2 1 
ATOM   745  N N   . SER A  1 99  ? -73.539 1.617   14.640  1.00 28.05  ? 126  SER A N   1 
ATOM   746  C CA  . SER A  1 99  ? -72.786 1.137   13.476  1.00 26.12  ? 126  SER A CA  1 
ATOM   747  C C   . SER A  1 99  ? -71.721 0.066   13.751  1.00 19.28  ? 126  SER A C   1 
ATOM   748  O O   . SER A  1 99  ? -70.527 0.357   13.738  1.00 21.50  ? 126  SER A O   1 
ATOM   749  C CB  . SER A  1 99  ? -72.184 2.318   12.702  1.00 26.15  ? 126  SER A CB  1 
ATOM   750  O OG  . SER A  1 99  ? -71.476 3.193   13.562  1.00 32.25  ? 126  SER A OG  1 
ATOM   751  N N   . PRO A  1 100 ? -72.158 -1.174  14.015  1.00 16.06  ? 127  PRO A N   1 
ATOM   752  C CA  . PRO A  1 100 ? -71.232 -2.303  14.111  1.00 21.65  ? 127  PRO A CA  1 
ATOM   753  C C   . PRO A  1 100 ? -70.757 -2.772  12.741  1.00 27.10  ? 127  PRO A C   1 
ATOM   754  O O   . PRO A  1 100 ? -71.492 -2.671  11.756  1.00 23.61  ? 127  PRO A O   1 
ATOM   755  C CB  . PRO A  1 100 ? -72.082 -3.396  14.762  1.00 16.16  ? 127  PRO A CB  1 
ATOM   756  C CG  . PRO A  1 100 ? -73.174 -2.666  15.452  1.00 18.03  ? 127  PRO A CG  1 
ATOM   757  C CD  . PRO A  1 100 ? -73.481 -1.523  14.549  1.00 24.32  ? 127  PRO A CD  1 
ATOM   758  N N   . THR A  1 101 ? -69.528 -3.283  12.706  1.00 26.00  ? 128  THR A N   1 
ATOM   759  C CA  . THR A  1 101 ? -68.899 -3.808  11.504  1.00 17.93  ? 128  THR A CA  1 
ATOM   760  C C   . THR A  1 101 ? -69.063 -5.319  11.511  1.00 12.88  ? 128  THR A C   1 
ATOM   761  O O   . THR A  1 101 ? -69.143 -5.961  10.469  1.00 11.41  ? 128  THR A O   1 
ATOM   762  C CB  . THR A  1 101 ? -67.395 -3.464  11.512  1.00 28.71  ? 128  THR A CB  1 
ATOM   763  O OG1 . THR A  1 101 ? -67.232 -2.041  11.560  1.00 38.06  ? 128  THR A OG1 1 
ATOM   764  C CG2 . THR A  1 101 ? -66.682 -4.022  10.288  1.00 27.61  ? 128  THR A CG2 1 
ATOM   765  N N   . THR A  1 102 ? -69.125 -5.882  12.709  1.00 12.95  ? 129  THR A N   1 
ATOM   766  C CA  . THR A  1 102 ? -69.245 -7.321  12.866  1.00 12.72  ? 129  THR A CA  1 
ATOM   767  C C   . THR A  1 102 ? -70.339 -7.679  13.856  1.00 11.88  ? 129  THR A C   1 
ATOM   768  O O   . THR A  1 102 ? -70.375 -7.152  14.966  1.00 13.50  ? 129  THR A O   1 
ATOM   769  C CB  . THR A  1 102 ? -67.941 -7.917  13.391  1.00 13.14  ? 129  THR A CB  1 
ATOM   770  O OG1 . THR A  1 102 ? -66.870 -7.548  12.518  1.00 20.21  ? 129  THR A OG1 1 
ATOM   771  C CG2 . THR A  1 102 ? -68.038 -9.436  13.482  1.00 10.16  ? 129  THR A CG2 1 
ATOM   772  N N   . LEU A  1 103 ? -71.237 -8.569  13.451  1.00 8.20   ? 130  LEU A N   1 
ATOM   773  C CA  . LEU A  1 103 ? -72.166 -9.170  14.393  1.00 7.39   ? 130  LEU A CA  1 
ATOM   774  C C   . LEU A  1 103 ? -71.889 -10.656 14.453  1.00 7.06   ? 130  LEU A C   1 
ATOM   775  O O   . LEU A  1 103 ? -71.824 -11.322 13.421  1.00 6.59   ? 130  LEU A O   1 
ATOM   776  C CB  . LEU A  1 103 ? -73.623 -8.939  13.992  1.00 6.21   ? 130  LEU A CB  1 
ATOM   777  C CG  . LEU A  1 103 ? -74.627 -9.651  14.910  1.00 3.98   ? 130  LEU A CG  1 
ATOM   778  C CD1 . LEU A  1 103 ? -75.030 -8.790  16.083  1.00 4.05   ? 130  LEU A CD1 1 
ATOM   779  C CD2 . LEU A  1 103 ? -75.846 -10.092 14.150  1.00 4.55   ? 130  LEU A CD2 1 
ATOM   780  N N   . ILE A  1 104 ? -71.718 -11.178 15.661  1.00 7.01   ? 131  ILE A N   1 
ATOM   781  C CA  . ILE A  1 104 ? -71.521 -12.607 15.830  1.00 6.39   ? 131  ILE A CA  1 
ATOM   782  C C   . ILE A  1 104 ? -72.612 -13.206 16.697  1.00 6.08   ? 131  ILE A C   1 
ATOM   783  O O   . ILE A  1 104 ? -72.718 -12.894 17.878  1.00 7.78   ? 131  ILE A O   1 
ATOM   784  C CB  . ILE A  1 104 ? -70.142 -12.934 16.416  1.00 7.91   ? 131  ILE A CB  1 
ATOM   785  C CG1 . ILE A  1 104 ? -69.052 -12.671 15.364  1.00 10.11  ? 131  ILE A CG1 1 
ATOM   786  C CG2 . ILE A  1 104 ? -70.117 -14.371 16.897  1.00 8.20   ? 131  ILE A CG2 1 
ATOM   787  C CD1 . ILE A  1 104 ? -67.702 -13.310 15.657  1.00 13.95  ? 131  ILE A CD1 1 
ATOM   788  N N   . PHE A  1 105 ? -73.434 -14.056 16.093  1.00 5.23   ? 132  PHE A N   1 
ATOM   789  C CA  . PHE A  1 105 ? -74.513 -14.706 16.815  1.00 4.58   ? 132  PHE A CA  1 
ATOM   790  C C   . PHE A  1 105 ? -74.191 -16.182 17.007  1.00 4.95   ? 132  PHE A C   1 
ATOM   791  O O   . PHE A  1 105 ? -74.129 -16.951 16.047  1.00 3.90   ? 132  PHE A O   1 
ATOM   792  C CB  . PHE A  1 105 ? -75.853 -14.521 16.097  1.00 4.59   ? 132  PHE A CB  1 
ATOM   793  C CG  . PHE A  1 105 ? -77.034 -14.610 17.013  1.00 4.60   ? 132  PHE A CG  1 
ATOM   794  C CD1 . PHE A  1 105 ? -77.527 -13.474 17.636  1.00 4.62   ? 132  PHE A CD1 1 
ATOM   795  C CD2 . PHE A  1 105 ? -77.629 -15.830 17.282  1.00 4.77   ? 132  PHE A CD2 1 
ATOM   796  C CE1 . PHE A  1 105 ? -78.597 -13.547 18.500  1.00 4.46   ? 132  PHE A CE1 1 
ATOM   797  C CE2 . PHE A  1 105 ? -78.699 -15.912 18.143  1.00 6.90   ? 132  PHE A CE2 1 
ATOM   798  C CZ  . PHE A  1 105 ? -79.186 -14.766 18.752  1.00 8.02   ? 132  PHE A CZ  1 
ATOM   799  N N   . GLU A  1 106 ? -73.994 -16.568 18.262  1.00 7.25   ? 133  GLU A N   1 
ATOM   800  C CA  . GLU A  1 106 ? -73.459 -17.883 18.589  1.00 10.52  ? 133  GLU A CA  1 
ATOM   801  C C   . GLU A  1 106 ? -74.155 -18.464 19.811  1.00 8.13   ? 133  GLU A C   1 
ATOM   802  O O   . GLU A  1 106 ? -73.723 -18.250 20.934  1.00 11.68  ? 133  GLU A O   1 
ATOM   803  C CB  . GLU A  1 106 ? -71.954 -17.758 18.840  1.00 13.88  ? 133  GLU A CB  1 
ATOM   804  C CG  . GLU A  1 106 ? -71.235 -19.044 19.192  1.00 21.58  ? 133  GLU A CG  1 
ATOM   805  C CD  . GLU A  1 106 ? -69.776 -18.804 19.544  1.00 28.84  ? 133  GLU A CD  1 
ATOM   806  O OE1 . GLU A  1 106 ? -69.318 -19.341 20.575  1.00 32.32  ? 133  GLU A OE1 1 
ATOM   807  O OE2 . GLU A  1 106 ? -69.089 -18.075 18.792  1.00 26.18  1 133  GLU A OE2 1 
ATOM   808  N N   . SER A  1 107 ? -75.235 -19.200 19.588  1.00 6.43   ? 134  SER A N   1 
ATOM   809  C CA  . SER A  1 107 ? -76.035 -19.715 20.686  1.00 7.63   ? 134  SER A CA  1 
ATOM   810  C C   . SER A  1 107 ? -76.487 -21.134 20.440  1.00 8.18   ? 134  SER A C   1 
ATOM   811  O O   . SER A  1 107 ? -76.461 -21.611 19.320  1.00 9.75   ? 134  SER A O   1 
ATOM   812  C CB  . SER A  1 107 ? -77.279 -18.860 20.876  1.00 9.50   ? 134  SER A CB  1 
ATOM   813  O OG  . SER A  1 107 ? -78.358 -19.669 21.314  1.00 8.96   ? 134  SER A OG  1 
ATOM   814  N N   . ASP A  1 108 ? -76.917 -21.806 21.497  1.00 8.85   ? 135  ASP A N   1 
ATOM   815  C CA  . ASP A  1 108 ? -77.551 -23.103 21.353  1.00 9.00   ? 135  ASP A CA  1 
ATOM   816  C C   . ASP A  1 108 ? -78.893 -23.060 22.048  1.00 13.68  ? 135  ASP A C   1 
ATOM   817  O O   . ASP A  1 108 ? -79.557 -24.081 22.224  1.00 17.06  ? 135  ASP A O   1 
ATOM   818  C CB  . ASP A  1 108 ? -76.675 -24.204 21.926  1.00 7.69   ? 135  ASP A CB  1 
ATOM   819  C CG  . ASP A  1 108 ? -75.377 -24.336 21.186  1.00 10.88  ? 135  ASP A CG  1 
ATOM   820  O OD1 . ASP A  1 108 ? -75.382 -24.900 20.078  1.00 10.99  ? 135  ASP A OD1 1 
ATOM   821  O OD2 . ASP A  1 108 ? -74.349 -23.863 21.700  1.00 17.57  1 135  ASP A OD2 1 
ATOM   822  N N   . ASN A  1 109 ? -79.282 -21.858 22.451  1.00 11.88  ? 136  ASN A N   1 
ATOM   823  C CA  . ASN A  1 109 ? -80.601 -21.641 23.002  1.00 11.19  ? 136  ASN A CA  1 
ATOM   824  C C   . ASN A  1 109 ? -81.273 -20.529 22.232  1.00 15.48  ? 136  ASN A C   1 
ATOM   825  O O   . ASN A  1 109 ? -81.361 -19.395 22.708  1.00 12.97  ? 136  ASN A O   1 
ATOM   826  C CB  . ASN A  1 109 ? -80.519 -21.292 24.475  1.00 13.74  ? 136  ASN A CB  1 
ATOM   827  C CG  . ASN A  1 109 ? -81.577 -21.993 25.280  1.00 26.28  ? 136  ASN A CG  1 
ATOM   828  O OD1 . ASN A  1 109 ? -81.272 -22.737 26.218  1.00 36.71  ? 136  ASN A OD1 1 
ATOM   829  N ND2 . ASN A  1 109 ? -82.836 -21.789 24.902  1.00 23.52  ? 136  ASN A ND2 1 
ATOM   830  N N   . LEU A  1 110 ? -81.737 -20.874 21.031  1.00 15.55  ? 137  LEU A N   1 
ATOM   831  C CA  . LEU A  1 110 ? -82.266 -19.909 20.077  1.00 9.19   ? 137  LEU A CA  1 
ATOM   832  C C   . LEU A  1 110 ? -83.732 -19.594 20.349  1.00 10.03  ? 137  LEU A C   1 
ATOM   833  O O   . LEU A  1 110 ? -84.136 -18.434 20.358  1.00 11.04  ? 137  LEU A O   1 
ATOM   834  C CB  . LEU A  1 110 ? -82.088 -20.439 18.652  1.00 8.53   ? 137  LEU A CB  1 
ATOM   835  C CG  . LEU A  1 110 ? -80.665 -20.809 18.219  1.00 9.07   ? 137  LEU A CG  1 
ATOM   836  C CD1 . LEU A  1 110 ? -80.637 -21.389 16.817  1.00 7.59   ? 137  LEU A CD1 1 
ATOM   837  C CD2 . LEU A  1 110 ? -79.745 -19.607 18.300  1.00 9.09   ? 137  LEU A CD2 1 
ATOM   838  N N   . GLY A  1 111 ? -84.528 -20.632 20.576  1.00 11.14  ? 138  GLY A N   1 
ATOM   839  C CA  . GLY A  1 111 ? -85.950 -20.457 20.806  1.00 11.14  ? 138  GLY A CA  1 
ATOM   840  C C   . GLY A  1 111 ? -86.763 -20.563 19.528  1.00 12.93  ? 138  GLY A C   1 
ATOM   841  O O   . GLY A  1 111 ? -87.967 -20.821 19.567  1.00 13.76  ? 138  GLY A O   1 
ATOM   842  N N   . MET A  1 112 ? -86.098 -20.364 18.393  1.00 13.82  ? 139  MET A N   1 
ATOM   843  C CA  . MET A  1 112 ? -86.745 -20.428 17.088  1.00 11.63  ? 139  MET A CA  1 
ATOM   844  C C   . MET A  1 112 ? -85.749 -20.706 15.963  1.00 12.70  ? 139  MET A C   1 
ATOM   845  O O   . MET A  1 112 ? -84.697 -21.313 16.172  1.00 11.19  ? 139  MET A O   1 
ATOM   846  C CB  . MET A  1 112 ? -87.508 -19.128 16.803  1.00 11.58  ? 139  MET A CB  1 
ATOM   847  C CG  . MET A  1 112 ? -86.680 -17.857 16.985  1.00 11.95  ? 139  MET A CG  1 
ATOM   848  S SD  . MET A  1 112 ? -87.615 -16.306 16.858  1.00 10.39  ? 139  MET A SD  1 
ATOM   849  C CE  . MET A  1 112 ? -88.171 -16.389 15.162  1.00 10.51  ? 139  MET A CE  1 
ATOM   850  N N   . ASN A  1 113 ? -86.112 -20.278 14.761  1.00 13.20  ? 140  ASN A N   1 
ATOM   851  C CA  . ASN A  1 113 ? -85.241 -20.368 13.605  1.00 10.77  ? 140  ASN A CA  1 
ATOM   852  C C   . ASN A  1 113 ? -84.924 -18.960 13.148  1.00 10.10  ? 140  ASN A C   1 
ATOM   853  O O   . ASN A  1 113 ? -85.746 -18.053 13.284  1.00 7.53   ? 140  ASN A O   1 
ATOM   854  C CB  . ASN A  1 113 ? -85.918 -21.131 12.468  1.00 15.35  ? 140  ASN A CB  1 
ATOM   855  C CG  . ASN A  1 113 ? -86.070 -22.608 12.759  1.00 21.62  ? 140  ASN A CG  1 
ATOM   856  O OD1 . ASN A  1 113 ? -85.106 -23.279 13.127  1.00 26.39  ? 140  ASN A OD1 1 
ATOM   857  N ND2 . ASN A  1 113 ? -87.294 -23.123 12.607  1.00 29.20  ? 140  ASN A ND2 1 
ATOM   858  N N   . ILE A  1 114 ? -83.726 -18.780 12.610  1.00 11.84  ? 141  ILE A N   1 
ATOM   859  C CA  . ILE A  1 114 ? -83.268 -17.469 12.173  1.00 9.85   ? 141  ILE A CA  1 
ATOM   860  C C   . ILE A  1 114 ? -84.157 -16.975 11.026  1.00 9.84   ? 141  ILE A C   1 
ATOM   861  O O   . ILE A  1 114 ? -84.630 -17.767 10.217  1.00 11.09  ? 141  ILE A O   1 
ATOM   862  C CB  . ILE A  1 114 ? -81.772 -17.539 11.769  1.00 8.61   ? 141  ILE A CB  1 
ATOM   863  C CG1 . ILE A  1 114 ? -81.201 -16.153 11.453  1.00 7.13   ? 141  ILE A CG1 1 
ATOM   864  C CG2 . ILE A  1 114 ? -81.569 -18.529 10.631  1.00 10.17  ? 141  ILE A CG2 1 
ATOM   865  C CD1 . ILE A  1 114 ? -80.452 -15.522 12.597  1.00 3.86   ? 141  ILE A CD1 1 
ATOM   866  N N   . THR A  1 115 ? -84.432 -15.673 10.991  1.00 9.15   ? 142  THR A N   1 
ATOM   867  C CA  . THR A  1 115 ? -85.283 -15.092 9.955   1.00 8.25   ? 142  THR A CA  1 
ATOM   868  C C   . THR A  1 115 ? -84.660 -13.804 9.435   1.00 8.74   ? 142  THR A C   1 
ATOM   869  O O   . THR A  1 115 ? -83.919 -13.147 10.162  1.00 9.04   ? 142  THR A O   1 
ATOM   870  C CB  . THR A  1 115 ? -86.686 -14.744 10.492  1.00 9.70   ? 142  THR A CB  1 
ATOM   871  O OG1 . THR A  1 115 ? -86.732 -13.357 10.852  1.00 11.19  ? 142  THR A OG1 1 
ATOM   872  C CG2 . THR A  1 115 ? -87.045 -15.592 11.707  1.00 8.68   ? 142  THR A CG2 1 
ATOM   873  N N   . ARG A  1 116 ? -84.974 -13.439 8.190   1.00 8.85   ? 143  ARG A N   1 
ATOM   874  C CA  . ARG A  1 116 ? -84.437 -12.221 7.577   1.00 8.00   ? 143  ARG A CA  1 
ATOM   875  C C   . ARG A  1 116 ? -84.752 -10.983 8.414   1.00 10.99  ? 143  ARG A C   1 
ATOM   876  O O   . ARG A  1 116 ? -84.001 -10.005 8.413   1.00 12.82  ? 143  ARG A O   1 
ATOM   877  C CB  . ARG A  1 116 ? -84.956 -12.039 6.146   1.00 6.70   ? 143  ARG A CB  1 
ATOM   878  C CG  . ARG A  1 116 ? -85.463 -10.620 5.858   1.00 16.80  ? 143  ARG A CG  1 
ATOM   879  C CD  . ARG A  1 116 ? -85.451 -10.236 4.378   1.00 23.19  ? 143  ARG A CD  1 
ATOM   880  N NE  . ARG A  1 116 ? -86.544 -10.843 3.616   1.00 45.05  ? 143  ARG A NE  1 
ATOM   881  C CZ  . ARG A  1 116 ? -87.629 -10.195 3.195   1.00 36.39  ? 143  ARG A CZ  1 
ATOM   882  N NH1 . ARG A  1 116 ? -88.562 -10.849 2.508   1.00 27.36  1 143  ARG A NH1 1 
ATOM   883  N NH2 . ARG A  1 116 ? -87.780 -8.898  3.452   1.00 28.77  ? 143  ARG A NH2 1 
ATOM   884  N N   . GLN A  1 117 ? -85.855 -11.044 9.150   1.00 12.17  ? 144  GLN A N   1 
ATOM   885  C CA  . GLN A  1 117 ? -86.329 -9.896  9.911   1.00 12.70  ? 144  GLN A CA  1 
ATOM   886  C C   . GLN A  1 117 ? -85.409 -9.572  11.066  1.00 11.68  ? 144  GLN A C   1 
ATOM   887  O O   . GLN A  1 117 ? -85.340 -8.427  11.507  1.00 13.82  ? 144  GLN A O   1 
ATOM   888  C CB  . GLN A  1 117 ? -87.737 -10.141 10.442  1.00 16.43  ? 144  GLN A CB  1 
ATOM   889  C CG  . GLN A  1 117 ? -88.427 -8.878  10.913  1.00 15.91  ? 144  GLN A CG  1 
ATOM   890  C CD  . GLN A  1 117 ? -89.318 -9.132  12.099  1.00 20.55  ? 144  GLN A CD  1 
ATOM   891  O OE1 . GLN A  1 117 ? -89.699 -10.274 12.371  1.00 21.79  ? 144  GLN A OE1 1 
ATOM   892  N NE2 . GLN A  1 117 ? -89.644 -8.069  12.829  1.00 24.72  ? 144  GLN A NE2 1 
ATOM   893  N N   . HIS A  1 118 ? -84.711 -10.589 11.558  1.00 12.83  ? 145  HIS A N   1 
ATOM   894  C CA  . HIS A  1 118 ? -83.719 -10.411 12.614  1.00 13.52  ? 145  HIS A CA  1 
ATOM   895  C C   . HIS A  1 118 ? -82.606 -9.469  12.146  1.00 15.44  ? 145  HIS A C   1 
ATOM   896  O O   . HIS A  1 118 ? -81.982 -8.754  12.941  1.00 12.09  ? 145  HIS A O   1 
ATOM   897  C CB  . HIS A  1 118 ? -83.117 -11.762 12.993  1.00 9.14   ? 145  HIS A CB  1 
ATOM   898  C CG  . HIS A  1 118 ? -84.076 -12.689 13.673  1.00 8.95   ? 145  HIS A CG  1 
ATOM   899  N ND1 . HIS A  1 118 ? -84.917 -12.281 14.686  1.00 9.67   ? 145  HIS A ND1 1 
ATOM   900  C CD2 . HIS A  1 118 ? -84.306 -14.012 13.505  1.00 8.39   ? 145  HIS A CD2 1 
ATOM   901  C CE1 . HIS A  1 118 ? -85.631 -13.310 15.104  1.00 8.99   ? 145  HIS A CE1 1 
ATOM   902  N NE2 . HIS A  1 118 ? -85.280 -14.373 14.404  1.00 8.82   ? 145  HIS A NE2 1 
ATOM   903  N N   . LEU A  1 119 ? -82.386 -9.465  10.838  1.00 14.17  ? 146  LEU A N   1 
ATOM   904  C CA  . LEU A  1 119 ? -81.283 -8.740  10.242  1.00 12.16  ? 146  LEU A CA  1 
ATOM   905  C C   . LEU A  1 119 ? -81.720 -7.448  9.583   1.00 12.75  ? 146  LEU A C   1 
ATOM   906  O O   . LEU A  1 119 ? -81.099 -6.998  8.627   1.00 18.41  ? 146  LEU A O   1 
ATOM   907  C CB  . LEU A  1 119 ? -80.601 -9.629  9.211   1.00 13.76  ? 146  LEU A CB  1 
ATOM   908  C CG  . LEU A  1 119 ? -79.917 -10.853 9.813   1.00 13.39  ? 146  LEU A CG  1 
ATOM   909  C CD1 . LEU A  1 119 ? -79.671 -11.914 8.751   1.00 11.81  ? 146  LEU A CD1 1 
ATOM   910  C CD2 . LEU A  1 119 ? -78.615 -10.427 10.475  1.00 10.00  ? 146  LEU A CD2 1 
ATOM   911  N N   . ASP A  1 120 ? -82.789 -6.845  10.075  1.00 12.54  ? 147  ASP A N   1 
ATOM   912  C CA  . ASP A  1 120 ? -83.180 -5.553  9.539   1.00 17.46  ? 147  ASP A CA  1 
ATOM   913  C C   . ASP A  1 120 ? -82.300 -4.510  10.203  1.00 15.81  ? 147  ASP A C   1 
ATOM   914  O O   . ASP A  1 120 ? -81.986 -4.641  11.386  1.00 13.93  ? 147  ASP A O   1 
ATOM   915  C CB  . ASP A  1 120 ? -84.664 -5.277  9.787   1.00 16.41  ? 147  ASP A CB  1 
ATOM   916  C CG  . ASP A  1 120 ? -85.571 -6.234  9.027   1.00 23.05  ? 147  ASP A CG  1 
ATOM   917  O OD1 . ASP A  1 120 ? -85.118 -6.807  8.007   1.00 21.33  ? 147  ASP A OD1 1 
ATOM   918  O OD2 . ASP A  1 120 ? -86.739 -6.409  9.445   1.00 27.23  1 147  ASP A OD2 1 
ATOM   919  N N   . ARG A  1 121 ? -81.885 -3.507  9.427   1.00 15.22  ? 148  ARG A N   1 
ATOM   920  C CA  . ARG A  1 121 ? -81.023 -2.411  9.888   1.00 16.80  ? 148  ARG A CA  1 
ATOM   921  C C   . ARG A  1 121 ? -79.569 -2.846  10.119  1.00 20.42  ? 148  ARG A C   1 
ATOM   922  O O   . ARG A  1 121 ? -78.703 -2.043  10.489  1.00 17.35  ? 148  ARG A O   1 
ATOM   923  C CB  . ARG A  1 121 ? -81.584 -1.740  11.148  1.00 14.93  ? 148  ARG A CB  1 
ATOM   924  C CG  . ARG A  1 121 ? -83.025 -1.331  11.051  1.00 10.43  ? 148  ARG A CG  1 
ATOM   925  C CD  . ARG A  1 121 ? -83.394 -0.437  12.209  1.00 13.33  ? 148  ARG A CD  1 
ATOM   926  N NE  . ARG A  1 121 ? -83.417 -1.152  13.477  1.00 13.37  ? 148  ARG A NE  1 
ATOM   927  C CZ  . ARG A  1 121 ? -84.492 -1.769  13.954  1.00 16.73  ? 148  ARG A CZ  1 
ATOM   928  N NH1 . ARG A  1 121 ? -85.622 -1.762  13.260  1.00 18.34  1 148  ARG A NH1 1 
ATOM   929  N NH2 . ARG A  1 121 ? -84.442 -2.396  15.120  1.00 18.22  ? 148  ARG A NH2 1 
ATOM   930  N N   . LEU A  1 122 ? -79.310 -4.128  9.915   1.00 18.23  ? 149  LEU A N   1 
ATOM   931  C CA  . LEU A  1 122 ? -77.955 -4.639  9.987   1.00 18.06  ? 149  LEU A CA  1 
ATOM   932  C C   . LEU A  1 122 ? -77.562 -5.030  8.575   1.00 24.34  ? 149  LEU A C   1 
ATOM   933  O O   . LEU A  1 122 ? -76.873 -6.027  8.349   1.00 21.29  ? 149  LEU A O   1 
ATOM   934  C CB  . LEU A  1 122 ? -77.870 -5.830  10.942  1.00 14.17  ? 149  LEU A CB  1 
ATOM   935  C CG  . LEU A  1 122 ? -78.284 -5.496  12.373  1.00 10.21  ? 149  LEU A CG  1 
ATOM   936  C CD1 . LEU A  1 122 ? -78.277 -6.730  13.247  1.00 7.39   ? 149  LEU A CD1 1 
ATOM   937  C CD2 . LEU A  1 122 ? -77.379 -4.422  12.937  1.00 9.08   ? 149  LEU A CD2 1 
ATOM   938  N N   . HIS A  1 123 ? -78.040 -4.235  7.624   1.00 28.83  ? 150  HIS A N   1 
ATOM   939  C CA  . HIS A  1 123 ? -77.666 -4.392  6.233   1.00 25.12  ? 150  HIS A CA  1 
ATOM   940  C C   . HIS A  1 123 ? -76.282 -3.785  5.993   1.00 22.69  ? 150  HIS A C   1 
ATOM   941  O O   . HIS A  1 123 ? -75.575 -4.189  5.069   1.00 23.25  ? 150  HIS A O   1 
ATOM   942  C CB  . HIS A  1 123 ? -78.712 -3.743  5.326   1.00 24.77  ? 150  HIS A CB  1 
ATOM   943  C CG  . HIS A  1 123 ? -80.011 -4.487  5.267   1.00 28.50  ? 150  HIS A CG  1 
ATOM   944  N ND1 . HIS A  1 123 ? -80.186 -5.730  5.839   1.00 28.63  ? 150  HIS A ND1 1 
ATOM   945  C CD2 . HIS A  1 123 ? -81.196 -4.166  4.695   1.00 35.33  ? 150  HIS A CD2 1 
ATOM   946  C CE1 . HIS A  1 123 ? -81.424 -6.141  5.623   1.00 29.88  ? 150  HIS A CE1 1 
ATOM   947  N NE2 . HIS A  1 123 ? -82.058 -5.210  4.932   1.00 33.96  ? 150  HIS A NE2 1 
ATOM   948  N N   . GLY A  1 124 ? -75.893 -2.833  6.841   1.00 18.68  ? 151  GLY A N   1 
ATOM   949  C CA  . GLY A  1 124 ? -74.601 -2.172  6.731   1.00 26.32  ? 151  GLY A CA  1 
ATOM   950  C C   . GLY A  1 124 ? -73.391 -3.001  7.146   1.00 23.16  ? 151  GLY A C   1 
ATOM   951  O O   . GLY A  1 124 ? -72.242 -2.581  6.964   1.00 14.66  ? 151  GLY A O   1 
ATOM   952  N N   . LEU A  1 125 ? -73.657 -4.184  7.696   1.00 22.91  ? 152  LEU A N   1 
ATOM   953  C CA  . LEU A  1 125 ? -72.621 -5.089  8.195   1.00 16.23  ? 152  LEU A CA  1 
ATOM   954  C C   . LEU A  1 125 ? -71.560 -5.456  7.162   1.00 14.19  ? 152  LEU A C   1 
ATOM   955  O O   . LEU A  1 125 ? -71.823 -5.477  5.965   1.00 18.47  ? 152  LEU A O   1 
ATOM   956  C CB  . LEU A  1 125 ? -73.259 -6.376  8.726   1.00 13.57  ? 152  LEU A CB  1 
ATOM   957  C CG  . LEU A  1 125 ? -73.991 -6.328  10.067  1.00 14.87  ? 152  LEU A CG  1 
ATOM   958  C CD1 . LEU A  1 125 ? -74.336 -7.739  10.510  1.00 13.97  ? 152  LEU A CD1 1 
ATOM   959  C CD2 . LEU A  1 125 ? -73.172 -5.617  11.143  1.00 14.03  ? 152  LEU A CD2 1 
ATOM   960  N N   . LYS A  1 126 ? -70.361 -5.761  7.643   1.00 12.90  ? 153  LYS A N   1 
ATOM   961  C CA  . LYS A  1 126 ? -69.295 -6.251  6.784   1.00 12.89  ? 153  LYS A CA  1 
ATOM   962  C C   . LYS A  1 126 ? -68.993 -7.700  7.123   1.00 12.72  ? 153  LYS A C   1 
ATOM   963  O O   . LYS A  1 126 ? -68.474 -8.454  6.298   1.00 13.53  ? 153  LYS A O   1 
ATOM   964  C CB  . LYS A  1 126 ? -68.040 -5.404  6.956   1.00 12.46  ? 153  LYS A CB  1 
ATOM   965  C CG  . LYS A  1 126 ? -68.156 -4.022  6.370   1.00 12.87  ? 153  LYS A CG  1 
ATOM   966  C CD  . LYS A  1 126 ? -66.910 -3.218  6.640   1.00 16.92  ? 153  LYS A CD  1 
ATOM   967  C CE  . LYS A  1 126 ? -66.648 -2.258  5.501   1.00 34.86  ? 153  LYS A CE  1 
ATOM   968  N NZ  . LYS A  1 126 ? -66.704 -2.971  4.191   1.00 40.68  1 153  LYS A NZ  1 
ATOM   969  N N   . ARG A  1 127 ? -69.330 -8.088  8.345   1.00 9.85   ? 154  ARG A N   1 
ATOM   970  C CA  . ARG A  1 127 ? -69.039 -9.428  8.809   1.00 10.38  ? 154  ARG A CA  1 
ATOM   971  C C   . ARG A  1 127 ? -70.192 -9.951  9.655   1.00 10.84  ? 154  ARG A C   1 
ATOM   972  O O   . ARG A  1 127 ? -70.632 -9.287  10.591  1.00 12.19  ? 154  ARG A O   1 
ATOM   973  C CB  . ARG A  1 127 ? -67.740 -9.412  9.609   1.00 13.26  ? 154  ARG A CB  1 
ATOM   974  C CG  . ARG A  1 127 ? -67.227 -10.768 10.065  1.00 16.58  ? 154  ARG A CG  1 
ATOM   975  C CD  . ARG A  1 127 ? -65.897 -10.582 10.800  1.00 32.72  ? 154  ARG A CD  1 
ATOM   976  N NE  . ARG A  1 127 ? -65.544 -11.710 11.660  1.00 38.83  ? 154  ARG A NE  1 
ATOM   977  C CZ  . ARG A  1 127 ? -64.582 -12.586 11.391  1.00 31.96  ? 154  ARG A CZ  1 
ATOM   978  N NH1 . ARG A  1 127 ? -63.868 -12.466 10.278  1.00 22.69  1 154  ARG A NH1 1 
ATOM   979  N NH2 . ARG A  1 127 ? -64.331 -13.580 12.237  1.00 29.61  ? 154  ARG A NH2 1 
ATOM   980  N N   . PHE A  1 128 ? -70.687 -11.136 9.311   1.00 7.64   ? 155  PHE A N   1 
ATOM   981  C CA  . PHE A  1 128 ? -71.738 -11.791 10.079  1.00 5.40   ? 155  PHE A CA  1 
ATOM   982  C C   . PHE A  1 128 ? -71.390 -13.254 10.309  1.00 6.59   ? 155  PHE A C   1 
ATOM   983  O O   . PHE A  1 128 ? -70.969 -13.942 9.382   1.00 7.90   ? 155  PHE A O   1 
ATOM   984  C CB  . PHE A  1 128 ? -73.071 -11.692 9.339   1.00 5.11   ? 155  PHE A CB  1 
ATOM   985  C CG  . PHE A  1 128 ? -74.174 -12.531 9.944   1.00 5.52   ? 155  PHE A CG  1 
ATOM   986  C CD1 . PHE A  1 128 ? -74.855 -12.099 11.074  1.00 3.96   ? 155  PHE A CD1 1 
ATOM   987  C CD2 . PHE A  1 128 ? -74.542 -13.742 9.371   1.00 4.11   ? 155  PHE A CD2 1 
ATOM   988  C CE1 . PHE A  1 128 ? -75.862 -12.860 11.622  1.00 2.15   ? 155  PHE A CE1 1 
ATOM   989  C CE2 . PHE A  1 128 ? -75.551 -14.504 9.921   1.00 2.91   ? 155  PHE A CE2 1 
ATOM   990  C CZ  . PHE A  1 128 ? -76.210 -14.060 11.048  1.00 2.89   ? 155  PHE A CZ  1 
ATOM   991  N N   . ARG A  1 129 ? -71.557 -13.733 11.537  1.00 2.90   ? 156  ARG A N   1 
ATOM   992  C CA  . ARG A  1 129 ? -71.397 -15.155 11.809  1.00 2.99   ? 156  ARG A CA  1 
ATOM   993  C C   . ARG A  1 129 ? -72.535 -15.662 12.654  1.00 3.37   ? 156  ARG A C   1 
ATOM   994  O O   . ARG A  1 129 ? -72.876 -15.063 13.664  1.00 4.29   ? 156  ARG A O   1 
ATOM   995  C CB  . ARG A  1 129 ? -70.075 -15.455 12.506  1.00 7.98   ? 156  ARG A CB  1 
ATOM   996  C CG  . ARG A  1 129 ? -70.065 -16.798 13.220  1.00 8.33   ? 156  ARG A CG  1 
ATOM   997  C CD  . ARG A  1 129 ? -68.663 -17.289 13.513  1.00 13.25  ? 156  ARG A CD  1 
ATOM   998  N NE  . ARG A  1 129 ? -68.019 -16.659 14.666  1.00 19.03  ? 156  ARG A NE  1 
ATOM   999  C CZ  . ARG A  1 129 ? -68.232 -17.022 15.929  1.00 21.10  ? 156  ARG A CZ  1 
ATOM   1000 N NH1 . ARG A  1 129 ? -69.104 -17.987 16.208  1.00 19.01  1 156  ARG A NH1 1 
ATOM   1001 N NH2 . ARG A  1 129 ? -67.590 -16.407 16.917  1.00 17.67  ? 156  ARG A NH2 1 
ATOM   1002 N N   . PHE A  1 130 ? -73.121 -16.773 12.231  1.00 3.85   ? 157  PHE A N   1 
ATOM   1003 C CA  . PHE A  1 130 ? -74.220 -17.391 12.951  1.00 3.74   ? 157  PHE A CA  1 
ATOM   1004 C C   . PHE A  1 130 ? -73.840 -18.832 13.230  1.00 4.32   ? 157  PHE A C   1 
ATOM   1005 O O   . PHE A  1 130 ? -73.586 -19.600 12.306  1.00 4.30   ? 157  PHE A O   1 
ATOM   1006 C CB  . PHE A  1 130 ? -75.509 -17.319 12.121  1.00 3.73   ? 157  PHE A CB  1 
ATOM   1007 C CG  . PHE A  1 130 ? -76.686 -18.003 12.760  1.00 3.70   ? 157  PHE A CG  1 
ATOM   1008 C CD1 . PHE A  1 130 ? -77.384 -17.396 13.789  1.00 3.89   ? 157  PHE A CD1 1 
ATOM   1009 C CD2 . PHE A  1 130 ? -77.093 -19.251 12.329  1.00 3.53   ? 157  PHE A CD2 1 
ATOM   1010 C CE1 . PHE A  1 130 ? -78.454 -18.025 14.383  1.00 3.88   ? 157  PHE A CE1 1 
ATOM   1011 C CE2 . PHE A  1 130 ? -78.161 -19.876 12.918  1.00 4.45   ? 157  PHE A CE2 1 
ATOM   1012 C CZ  . PHE A  1 130 ? -78.843 -19.263 13.947  1.00 3.94   ? 157  PHE A CZ  1 
ATOM   1013 N N   . THR A  1 131 ? -73.778 -19.201 14.501  1.00 4.00   ? 158  THR A N   1 
ATOM   1014 C CA  . THR A  1 131 ? -73.340 -20.542 14.854  1.00 6.08   ? 158  THR A CA  1 
ATOM   1015 C C   . THR A  1 131 ? -74.283 -21.137 15.873  1.00 4.92   ? 158  THR A C   1 
ATOM   1016 O O   . THR A  1 131 ? -74.615 -20.491 16.855  1.00 5.55   ? 158  THR A O   1 
ATOM   1017 C CB  . THR A  1 131 ? -71.907 -20.538 15.438  1.00 9.37   ? 158  THR A CB  1 
ATOM   1018 O OG1 . THR A  1 131 ? -70.943 -20.344 14.389  1.00 10.20  ? 158  THR A OG1 1 
ATOM   1019 C CG2 . THR A  1 131 ? -71.614 -21.849 16.147  1.00 11.27  ? 158  THR A CG2 1 
ATOM   1020 N N   . THR A  1 132 ? -74.719 -22.366 15.635  1.00 4.73   ? 159  THR A N   1 
ATOM   1021 C CA  . THR A  1 132 ? -75.584 -23.052 16.578  1.00 5.64   ? 159  THR A CA  1 
ATOM   1022 C C   . THR A  1 132 ? -75.511 -24.552 16.379  1.00 8.20   ? 159  THR A C   1 
ATOM   1023 O O   . THR A  1 132 ? -75.460 -25.030 15.249  1.00 10.11  ? 159  THR A O   1 
ATOM   1024 C CB  . THR A  1 132 ? -77.046 -22.594 16.442  1.00 8.88   ? 159  THR A CB  1 
ATOM   1025 O OG1 . THR A  1 132 ? -77.898 -23.471 17.189  1.00 12.20  ? 159  THR A OG1 1 
ATOM   1026 C CG2 . THR A  1 132 ? -77.482 -22.608 14.991  1.00 14.06  ? 159  THR A CG2 1 
ATOM   1027 N N   . ARG A  1 133 ? -75.500 -25.294 17.482  1.00 9.99   ? 160  ARG A N   1 
ATOM   1028 C CA  . ARG A  1 133 ? -75.512 -26.751 17.419  1.00 13.88  ? 160  ARG A CA  1 
ATOM   1029 C C   . ARG A  1 133 ? -76.900 -27.325 17.698  1.00 16.35  ? 160  ARG A C   1 
ATOM   1030 O O   . ARG A  1 133 ? -77.059 -28.527 17.943  1.00 17.21  ? 160  ARG A O   1 
ATOM   1031 C CB  . ARG A  1 133 ? -74.472 -27.343 18.360  1.00 15.98  ? 160  ARG A CB  1 
ATOM   1032 C CG  . ARG A  1 133 ? -73.050 -27.178 17.859  1.00 23.71  ? 160  ARG A CG  1 
ATOM   1033 C CD  . ARG A  1 133 ? -72.073 -27.216 19.013  1.00 31.65  ? 160  ARG A CD  1 
ATOM   1034 N NE  . ARG A  1 133 ? -72.363 -26.148 19.966  1.00 35.78  ? 160  ARG A NE  1 
ATOM   1035 C CZ  . ARG A  1 133 ? -71.728 -25.976 21.119  1.00 33.38  ? 160  ARG A CZ  1 
ATOM   1036 N NH1 . ARG A  1 133 ? -70.757 -26.806 21.477  1.00 38.73  1 160  ARG A NH1 1 
ATOM   1037 N NH2 . ARG A  1 133 ? -72.067 -24.972 21.914  1.00 34.94  ? 160  ARG A NH2 1 
ATOM   1038 N N   . ARG A  1 134 ? -77.899 -26.450 17.658  1.00 14.16  ? 161  ARG A N   1 
ATOM   1039 C CA  . ARG A  1 134 ? -79.286 -26.870 17.647  1.00 14.42  ? 161  ARG A CA  1 
ATOM   1040 C C   . ARG A  1 134 ? -79.597 -27.442 16.276  1.00 21.72  ? 161  ARG A C   1 
ATOM   1041 O O   . ARG A  1 134 ? -78.876 -27.170 15.307  1.00 22.17  ? 161  ARG A O   1 
ATOM   1042 C CB  . ARG A  1 134 ? -80.200 -25.679 17.905  1.00 11.82  ? 161  ARG A CB  1 
ATOM   1043 C CG  . ARG A  1 134 ? -80.255 -25.225 19.347  1.00 14.37  ? 161  ARG A CG  1 
ATOM   1044 C CD  . ARG A  1 134 ? -81.193 -26.086 20.188  1.00 17.26  ? 161  ARG A CD  1 
ATOM   1045 N NE  . ARG A  1 134 ? -80.651 -27.415 20.456  1.00 16.90  ? 161  ARG A NE  1 
ATOM   1046 C CZ  . ARG A  1 134 ? -79.818 -27.697 21.453  1.00 18.97  ? 161  ARG A CZ  1 
ATOM   1047 N NH1 . ARG A  1 134 ? -79.420 -26.742 22.288  1.00 13.40  1 161  ARG A NH1 1 
ATOM   1048 N NH2 . ARG A  1 134 ? -79.381 -28.938 21.614  1.00 22.72  ? 161  ARG A NH2 1 
ATOM   1049 N N   . LEU A  1 135 ? -80.653 -28.247 16.192  1.00 17.50  ? 162  LEU A N   1 
ATOM   1050 C CA  . LEU A  1 135 ? -81.180 -28.627 14.896  1.00 12.62  ? 162  LEU A CA  1 
ATOM   1051 C C   . LEU A  1 135 ? -81.997 -27.444 14.455  1.00 13.10  ? 162  LEU A C   1 
ATOM   1052 O O   . LEU A  1 135 ? -82.991 -27.104 15.089  1.00 20.89  ? 162  LEU A O   1 
ATOM   1053 C CB  . LEU A  1 135 ? -82.075 -29.850 14.999  1.00 16.24  ? 162  LEU A CB  1 
ATOM   1054 C CG  . LEU A  1 135 ? -82.714 -30.264 13.676  1.00 13.64  ? 162  LEU A CG  1 
ATOM   1055 C CD1 . LEU A  1 135 ? -81.633 -30.661 12.692  1.00 19.13  ? 162  LEU A CD1 1 
ATOM   1056 C CD2 . LEU A  1 135 ? -83.698 -31.393 13.876  1.00 11.15  ? 162  LEU A CD2 1 
ATOM   1057 N N   . THR A  1 136 ? -81.570 -26.792 13.386  1.00 12.48  ? 163  THR A N   1 
ATOM   1058 C CA  . THR A  1 136 ? -82.236 -25.575 12.961  1.00 13.29  ? 163  THR A CA  1 
ATOM   1059 C C   . THR A  1 136 ? -82.135 -25.400 11.462  1.00 13.11  ? 163  THR A C   1 
ATOM   1060 O O   . THR A  1 136 ? -81.140 -25.773 10.848  1.00 14.50  ? 163  THR A O   1 
ATOM   1061 C CB  . THR A  1 136 ? -81.693 -24.338 13.719  1.00 14.03  ? 163  THR A CB  1 
ATOM   1062 O OG1 . THR A  1 136 ? -82.640 -23.946 14.725  1.00 15.98  ? 163  THR A OG1 1 
ATOM   1063 C CG2 . THR A  1 136 ? -81.441 -23.166 12.776  1.00 10.73  ? 163  THR A CG2 1 
ATOM   1064 N N   . HIS A  1 137 ? -83.197 -24.863 10.877  1.00 17.12  ? 164  HIS A N   1 
ATOM   1065 C CA  . HIS A  1 137 ? -83.231 -24.582 9.456   1.00 18.32  ? 164  HIS A CA  1 
ATOM   1066 C C   . HIS A  1 137 ? -82.877 -23.121 9.198   1.00 15.17  ? 164  HIS A C   1 
ATOM   1067 O O   . HIS A  1 137 ? -83.320 -22.228 9.918   1.00 15.69  ? 164  HIS A O   1 
ATOM   1068 C CB  . HIS A  1 137 ? -84.620 -24.893 8.903   1.00 24.27  ? 164  HIS A CB  1 
ATOM   1069 C CG  . HIS A  1 137 ? -84.790 -24.523 7.464   1.00 25.90  ? 164  HIS A CG  1 
ATOM   1070 N ND1 . HIS A  1 137 ? -84.269 -25.280 6.436   1.00 23.42  ? 164  HIS A ND1 1 
ATOM   1071 C CD2 . HIS A  1 137 ? -85.414 -23.472 6.881   1.00 21.04  ? 164  HIS A CD2 1 
ATOM   1072 C CE1 . HIS A  1 137 ? -84.570 -24.713 5.282   1.00 22.63  ? 164  HIS A CE1 1 
ATOM   1073 N NE2 . HIS A  1 137 ? -85.265 -23.615 5.524   1.00 21.44  ? 164  HIS A NE2 1 
ATOM   1074 N N   . ILE A  1 138 ? -82.067 -22.885 8.172   1.00 13.24  ? 165  ILE A N   1 
ATOM   1075 C CA  . ILE A  1 138 ? -81.715 -21.526 7.773   1.00 15.74  ? 165  ILE A CA  1 
ATOM   1076 C C   . ILE A  1 138 ? -82.421 -21.136 6.470   1.00 15.35  ? 165  ILE A C   1 
ATOM   1077 O O   . ILE A  1 138 ? -82.232 -21.779 5.437   1.00 18.54  ? 165  ILE A O   1 
ATOM   1078 C CB  . ILE A  1 138 ? -80.176 -21.350 7.649   1.00 12.74  ? 165  ILE A CB  1 
ATOM   1079 C CG1 . ILE A  1 138 ? -79.534 -21.389 9.040   1.00 9.95   ? 165  ILE A CG1 1 
ATOM   1080 C CG2 . ILE A  1 138 ? -79.830 -20.044 6.944   1.00 8.86   ? 165  ILE A CG2 1 
ATOM   1081 C CD1 . ILE A  1 138 ? -78.020 -21.424 9.039   1.00 6.56   ? 165  ILE A CD1 1 
ATOM   1082 N N   . PRO A  1 139 ? -83.253 -20.085 6.522   1.00 10.55  ? 166  PRO A N   1 
ATOM   1083 C CA  . PRO A  1 139 ? -84.006 -19.610 5.359   1.00 12.62  ? 166  PRO A CA  1 
ATOM   1084 C C   . PRO A  1 139 ? -83.091 -19.041 4.287   1.00 10.71  ? 166  PRO A C   1 
ATOM   1085 O O   . PRO A  1 139 ? -82.117 -18.387 4.616   1.00 12.16  ? 166  PRO A O   1 
ATOM   1086 C CB  . PRO A  1 139 ? -84.880 -18.495 5.942   1.00 12.38  ? 166  PRO A CB  1 
ATOM   1087 C CG  . PRO A  1 139 ? -84.157 -18.041 7.141   1.00 11.19  ? 166  PRO A CG  1 
ATOM   1088 C CD  . PRO A  1 139 ? -83.520 -19.270 7.715   1.00 10.37  ? 166  PRO A CD  1 
ATOM   1089 N N   . ALA A  1 140 ? -83.405 -19.283 3.022   1.00 10.83  ? 167  ALA A N   1 
ATOM   1090 C CA  . ALA A  1 140 ? -82.582 -18.780 1.934   1.00 11.32  ? 167  ALA A CA  1 
ATOM   1091 C C   . ALA A  1 140 ? -82.892 -17.321 1.609   1.00 11.93  ? 167  ALA A C   1 
ATOM   1092 O O   . ALA A  1 140 ? -82.243 -16.712 0.755   1.00 11.11  ? 167  ALA A O   1 
ATOM   1093 C CB  . ALA A  1 140 ? -82.758 -19.633 0.718   1.00 12.81  ? 167  ALA A CB  1 
ATOM   1094 N N   . ASN A  1 141 ? -83.888 -16.765 2.287   1.00 11.45  ? 168  ASN A N   1 
ATOM   1095 C CA  . ASN A  1 141 ? -84.201 -15.355 2.129   1.00 11.12  ? 168  ASN A CA  1 
ATOM   1096 C C   . ASN A  1 141 ? -83.546 -14.558 3.247   1.00 11.82  ? 168  ASN A C   1 
ATOM   1097 O O   . ASN A  1 141 ? -83.831 -13.378 3.442   1.00 12.05  ? 168  ASN A O   1 
ATOM   1098 C CB  . ASN A  1 141 ? -85.718 -15.130 2.091   1.00 11.87  ? 168  ASN A CB  1 
ATOM   1099 C CG  . ASN A  1 141 ? -86.336 -14.989 3.471   1.00 14.52  ? 168  ASN A CG  1 
ATOM   1100 O OD1 . ASN A  1 141 ? -85.977 -15.698 4.411   1.00 12.20  ? 168  ASN A OD1 1 
ATOM   1101 N ND2 . ASN A  1 141 ? -87.283 -14.066 3.593   1.00 17.76  ? 168  ASN A ND2 1 
ATOM   1102 N N   . LEU A  1 142 ? -82.649 -15.228 3.966   1.00 10.71  ? 169  LEU A N   1 
ATOM   1103 C CA  . LEU A  1 142 ? -82.048 -14.692 5.179   1.00 8.20   ? 169  LEU A CA  1 
ATOM   1104 C C   . LEU A  1 142 ? -81.134 -13.522 4.899   1.00 8.75   ? 169  LEU A C   1 
ATOM   1105 O O   . LEU A  1 142 ? -81.193 -12.500 5.579   1.00 10.68  ? 169  LEU A O   1 
ATOM   1106 C CB  . LEU A  1 142 ? -81.254 -15.780 5.893   1.00 7.84   ? 169  LEU A CB  1 
ATOM   1107 C CG  . LEU A  1 142 ? -80.622 -15.402 7.224   1.00 8.26   ? 169  LEU A CG  1 
ATOM   1108 C CD1 . LEU A  1 142 ? -81.693 -14.896 8.158   1.00 7.32   ? 169  LEU A CD1 1 
ATOM   1109 C CD2 . LEU A  1 142 ? -79.903 -16.597 7.819   1.00 6.73   ? 169  LEU A CD2 1 
ATOM   1110 N N   . LEU A  1 143 ? -80.278 -13.677 3.901   1.00 8.44   ? 170  LEU A N   1 
ATOM   1111 C CA  . LEU A  1 143 ? -79.299 -12.652 3.596   1.00 9.84   ? 170  LEU A CA  1 
ATOM   1112 C C   . LEU A  1 143 ? -79.792 -11.797 2.456   1.00 11.75  ? 170  LEU A C   1 
ATOM   1113 O O   . LEU A  1 143 ? -79.167 -11.721 1.397   1.00 15.59  ? 170  LEU A O   1 
ATOM   1114 C CB  . LEU A  1 143 ? -77.962 -13.287 3.244   1.00 13.01  ? 170  LEU A CB  1 
ATOM   1115 C CG  . LEU A  1 143 ? -77.325 -14.095 4.369   1.00 8.19   ? 170  LEU A CG  1 
ATOM   1116 C CD1 . LEU A  1 143 ? -75.982 -14.621 3.907   1.00 7.46   ? 170  LEU A CD1 1 
ATOM   1117 C CD2 . LEU A  1 143 ? -77.186 -13.236 5.614   1.00 6.92   ? 170  LEU A CD2 1 
ATOM   1118 N N   . THR A  1 144 ? -80.932 -11.163 2.683   1.00 12.38  ? 171  THR A N   1 
ATOM   1119 C CA  . THR A  1 144 ? -81.535 -10.299 1.690   1.00 15.40  ? 171  THR A CA  1 
ATOM   1120 C C   . THR A  1 144 ? -81.058 -8.882  1.927   1.00 17.40  ? 171  THR A C   1 
ATOM   1121 O O   . THR A  1 144 ? -81.058 -8.402  3.061   1.00 17.46  ? 171  THR A O   1 
ATOM   1122 C CB  . THR A  1 144 ? -83.067 -10.348 1.768   1.00 15.51  ? 171  THR A CB  1 
ATOM   1123 O OG1 . THR A  1 144 ? -83.510 -11.703 1.638   1.00 12.59  ? 171  THR A OG1 1 
ATOM   1124 C CG2 . THR A  1 144 ? -83.685 -9.516  0.663   1.00 24.34  ? 171  THR A CG2 1 
ATOM   1125 N N   . ASP A  1 145 ? -80.637 -8.229  0.849   1.00 19.38  ? 172  ASP A N   1 
ATOM   1126 C CA  . ASP A  1 145 ? -80.177 -6.845  0.892   1.00 24.21  ? 172  ASP A CA  1 
ATOM   1127 C C   . ASP A  1 145 ? -78.901 -6.707  1.713   1.00 24.74  ? 172  ASP A C   1 
ATOM   1128 O O   . ASP A  1 145 ? -78.637 -5.654  2.292   1.00 26.42  ? 172  ASP A O   1 
ATOM   1129 C CB  . ASP A  1 145 ? -81.269 -5.906  1.429   1.00 24.16  ? 172  ASP A CB  1 
ATOM   1130 C CG  . ASP A  1 145 ? -82.612 -6.093  0.725   1.00 26.69  ? 172  ASP A CG  1 
ATOM   1131 O OD1 . ASP A  1 145 ? -82.633 -6.534  -0.447  1.00 25.73  ? 172  ASP A OD1 1 
ATOM   1132 O OD2 . ASP A  1 145 ? -83.653 -5.795  1.346   1.00 24.83  1 172  ASP A OD2 1 
ATOM   1133 N N   . MET A  1 146 ? -78.113 -7.778  1.758   1.00 20.66  ? 173  MET A N   1 
ATOM   1134 C CA  . MET A  1 146 ? -76.825 -7.755  2.440   1.00 19.00  ? 173  MET A CA  1 
ATOM   1135 C C   . MET A  1 146 ? -75.711 -7.408  1.458   1.00 26.89  ? 173  MET A C   1 
ATOM   1136 O O   . MET A  1 146 ? -74.822 -8.221  1.196   1.00 24.79  ? 173  MET A O   1 
ATOM   1137 C CB  . MET A  1 146 ? -76.545 -9.106  3.086   1.00 16.32  ? 173  MET A CB  1 
ATOM   1138 C CG  . MET A  1 146 ? -77.380 -9.405  4.318   1.00 15.62  ? 173  MET A CG  1 
ATOM   1139 S SD  . MET A  1 146 ? -77.100 -8.203  5.629   1.00 14.36  ? 173  MET A SD  1 
ATOM   1140 C CE  . MET A  1 146 ? -77.781 -9.060  7.042   1.00 11.09  ? 173  MET A CE  1 
ATOM   1141 N N   . ARG A  1 147 ? -75.768 -6.192  0.921   1.00 32.24  ? 174  ARG A N   1 
ATOM   1142 C CA  . ARG A  1 147 ? -74.845 -5.751  -0.124  1.00 27.61  ? 174  ARG A CA  1 
ATOM   1143 C C   . ARG A  1 147 ? -73.412 -5.534  0.381   1.00 27.32  ? 174  ARG A C   1 
ATOM   1144 O O   . ARG A  1 147 ? -72.474 -5.450  -0.411  1.00 24.59  ? 174  ARG A O   1 
ATOM   1145 C CB  . ARG A  1 147 ? -75.368 -4.465  -0.780  1.00 30.19  ? 174  ARG A CB  1 
ATOM   1146 C CG  . ARG A  1 147 ? -76.678 -4.623  -1.541  1.00 28.83  ? 174  ARG A CG  1 
ATOM   1147 C CD  . ARG A  1 147 ? -76.508 -5.507  -2.761  1.00 32.17  ? 174  ARG A CD  1 
ATOM   1148 N NE  . ARG A  1 147 ? -77.787 -5.832  -3.387  1.00 39.53  ? 174  ARG A NE  1 
ATOM   1149 C CZ  . ARG A  1 147 ? -77.924 -6.635  -4.440  1.00 36.80  ? 174  ARG A CZ  1 
ATOM   1150 N NH1 . ARG A  1 147 ? -76.856 -7.201  -4.994  1.00 29.08  1 174  ARG A NH1 1 
ATOM   1151 N NH2 . ARG A  1 147 ? -79.131 -6.873  -4.940  1.00 32.91  ? 174  ARG A NH2 1 
ATOM   1152 N N   . ASN A  1 148 ? -73.246 -5.450  1.697   1.00 26.20  ? 175  ASN A N   1 
ATOM   1153 C CA  . ASN A  1 148 ? -71.954 -5.108  2.275   1.00 24.01  ? 175  ASN A CA  1 
ATOM   1154 C C   . ASN A  1 148 ? -71.234 -6.271  2.934   1.00 19.22  ? 175  ASN A C   1 
ATOM   1155 O O   . ASN A  1 148 ? -70.031 -6.196  3.196   1.00 15.72  ? 175  ASN A O   1 
ATOM   1156 C CB  . ASN A  1 148 ? -72.114 -3.975  3.274   1.00 26.61  ? 175  ASN A CB  1 
ATOM   1157 C CG  . ASN A  1 148 ? -72.611 -2.715  2.632   1.00 38.49  ? 175  ASN A CG  1 
ATOM   1158 O OD1 . ASN A  1 148 ? -72.553 -2.559  1.408   1.00 38.32  ? 175  ASN A OD1 1 
ATOM   1159 N ND2 . ASN A  1 148 ? -73.106 -1.796  3.454   1.00 46.01  ? 175  ASN A ND2 1 
ATOM   1160 N N   . LEU A  1 149 ? -71.978 -7.332  3.217   1.00 16.27  ? 176  LEU A N   1 
ATOM   1161 C CA  . LEU A  1 149 ? -71.382 -8.544  3.741   1.00 12.49  ? 176  LEU A CA  1 
ATOM   1162 C C   . LEU A  1 149 ? -70.161 -8.893  2.908   1.00 13.69  ? 176  LEU A C   1 
ATOM   1163 O O   . LEU A  1 149 ? -70.266 -9.083  1.699   1.00 16.26  ? 176  LEU A O   1 
ATOM   1164 C CB  . LEU A  1 149 ? -72.386 -9.684  3.681   1.00 11.06  ? 176  LEU A CB  1 
ATOM   1165 C CG  . LEU A  1 149 ? -72.555 -10.418 5.002   1.00 10.25  ? 176  LEU A CG  1 
ATOM   1166 C CD1 . LEU A  1 149 ? -73.055 -9.451  6.062   1.00 11.36  ? 176  LEU A CD1 1 
ATOM   1167 C CD2 . LEU A  1 149 ? -73.495 -11.599 4.841   1.00 9.78   ? 176  LEU A CD2 1 
ATOM   1168 N N   . SER A  1 150 ? -68.996 -8.927  3.549   1.00 13.34  ? 177  SER A N   1 
ATOM   1169 C CA  . SER A  1 150 ? -67.765 -9.304  2.865   1.00 12.43  ? 177  SER A CA  1 
ATOM   1170 C C   . SER A  1 150 ? -67.263 -10.630 3.395   1.00 9.80   ? 177  SER A C   1 
ATOM   1171 O O   . SER A  1 150 ? -66.549 -11.353 2.700   1.00 9.67   ? 177  SER A O   1 
ATOM   1172 C CB  . SER A  1 150 ? -66.694 -8.241  3.059   1.00 12.90  ? 177  SER A CB  1 
ATOM   1173 O OG  . SER A  1 150 ? -66.400 -8.088  4.431   1.00 14.39  ? 177  SER A OG  1 
ATOM   1174 N N   . HIS A  1 151 ? -67.640 -10.938 4.632   1.00 8.50   ? 178  HIS A N   1 
ATOM   1175 C CA  . HIS A  1 151 ? -67.290 -12.209 5.252   1.00 10.35  ? 178  HIS A CA  1 
ATOM   1176 C C   . HIS A  1 151 ? -68.516 -12.871 5.858   1.00 7.50   ? 178  HIS A C   1 
ATOM   1177 O O   . HIS A  1 151 ? -69.159 -12.313 6.741   1.00 7.88   ? 178  HIS A O   1 
ATOM   1178 C CB  . HIS A  1 151 ? -66.211 -12.020 6.332   1.00 15.93  ? 178  HIS A CB  1 
ATOM   1179 C CG  . HIS A  1 151 ? -65.861 -13.282 7.066   1.00 16.08  ? 178  HIS A CG  1 
ATOM   1180 N ND1 . HIS A  1 151 ? -64.995 -14.227 6.556   1.00 11.02  ? 178  HIS A ND1 1 
ATOM   1181 C CD2 . HIS A  1 151 ? -66.273 -13.761 8.265   1.00 15.95  ? 178  HIS A CD2 1 
ATOM   1182 C CE1 . HIS A  1 151 ? -64.884 -15.229 7.410   1.00 9.41   ? 178  HIS A CE1 1 
ATOM   1183 N NE2 . HIS A  1 151 ? -65.651 -14.972 8.454   1.00 12.67  ? 178  HIS A NE2 1 
ATOM   1184 N N   . LEU A  1 152 ? -68.827 -14.071 5.387   1.00 6.31   ? 179  LEU A N   1 
ATOM   1185 C CA  . LEU A  1 152 ? -69.955 -14.828 5.910   1.00 7.08   ? 179  LEU A CA  1 
ATOM   1186 C C   . LEU A  1 152 ? -69.506 -16.150 6.528   1.00 7.81   ? 179  LEU A C   1 
ATOM   1187 O O   . LEU A  1 152 ? -68.612 -16.813 6.008   1.00 10.43  ? 179  LEU A O   1 
ATOM   1188 C CB  . LEU A  1 152 ? -70.963 -15.102 4.792   1.00 8.26   ? 179  LEU A CB  1 
ATOM   1189 C CG  . LEU A  1 152 ? -72.150 -16.015 5.115   1.00 7.24   ? 179  LEU A CG  1 
ATOM   1190 C CD1 . LEU A  1 152 ? -73.111 -15.340 6.081   1.00 6.01   ? 179  LEU A CD1 1 
ATOM   1191 C CD2 . LEU A  1 152 ? -72.859 -16.433 3.837   1.00 8.47   ? 179  LEU A CD2 1 
ATOM   1192 N N   . GLU A  1 153 ? -70.122 -16.532 7.638   1.00 5.37   ? 180  GLU A N   1 
ATOM   1193 C CA  . GLU A  1 153 ? -69.877 -17.842 8.216   1.00 5.79   ? 180  GLU A CA  1 
ATOM   1194 C C   . GLU A  1 153 ? -71.103 -18.319 8.961   1.00 6.36   ? 180  GLU A C   1 
ATOM   1195 O O   . GLU A  1 153 ? -71.574 -17.665 9.889   1.00 6.73   ? 180  GLU A O   1 
ATOM   1196 C CB  . GLU A  1 153 ? -68.681 -17.819 9.165   1.00 9.17   ? 180  GLU A CB  1 
ATOM   1197 C CG  . GLU A  1 153 ? -68.462 -19.146 9.887   1.00 11.08  ? 180  GLU A CG  1 
ATOM   1198 C CD  . GLU A  1 153 ? -67.472 -19.045 11.042  1.00 14.69  ? 180  GLU A CD  1 
ATOM   1199 O OE1 . GLU A  1 153 ? -66.794 -17.999 11.160  1.00 12.04  ? 180  GLU A OE1 1 
ATOM   1200 O OE2 . GLU A  1 153 ? -67.390 -20.006 11.842  1.00 15.63  1 180  GLU A OE2 1 
ATOM   1201 N N   . LEU A  1 154 ? -71.620 -19.467 8.552   1.00 5.92   ? 181  LEU A N   1 
ATOM   1202 C CA  . LEU A  1 154 ? -72.780 -20.044 9.200   1.00 5.54   ? 181  LEU A CA  1 
ATOM   1203 C C   . LEU A  1 154 ? -72.433 -21.472 9.577   1.00 5.13   ? 181  LEU A C   1 
ATOM   1204 O O   . LEU A  1 154 ? -71.784 -22.177 8.809   1.00 6.32   ? 181  LEU A O   1 
ATOM   1205 C CB  . LEU A  1 154 ? -73.983 -20.026 8.249   1.00 6.39   ? 181  LEU A CB  1 
ATOM   1206 C CG  . LEU A  1 154 ? -74.294 -18.742 7.466   1.00 5.19   ? 181  LEU A CG  1 
ATOM   1207 C CD1 . LEU A  1 154 ? -75.241 -19.049 6.320   1.00 3.75   ? 181  LEU A CD1 1 
ATOM   1208 C CD2 . LEU A  1 154 ? -74.864 -17.644 8.366   1.00 3.01   ? 181  LEU A CD2 1 
ATOM   1209 N N   . ARG A  1 155 ? -72.854 -21.901 10.757  1.00 5.04   ? 182  ARG A N   1 
ATOM   1210 C CA  . ARG A  1 155 ? -72.629 -23.276 11.164  1.00 6.90   ? 182  ARG A CA  1 
ATOM   1211 C C   . ARG A  1 155 ? -73.809 -23.816 11.941  1.00 7.49   ? 182  ARG A C   1 
ATOM   1212 O O   . ARG A  1 155 ? -73.876 -23.658 13.157  1.00 7.91   ? 182  ARG A O   1 
ATOM   1213 C CB  . ARG A  1 155 ? -71.377 -23.372 12.020  1.00 10.39  ? 182  ARG A CB  1 
ATOM   1214 C CG  . ARG A  1 155 ? -70.975 -24.788 12.367  1.00 12.12  ? 182  ARG A CG  1 
ATOM   1215 C CD  . ARG A  1 155 ? -69.967 -24.762 13.496  1.00 19.98  ? 182  ARG A CD  1 
ATOM   1216 N NE  . ARG A  1 155 ? -69.098 -23.593 13.396  1.00 24.32  ? 182  ARG A NE  1 
ATOM   1217 C CZ  . ARG A  1 155 ? -67.771 -23.635 13.427  1.00 26.37  ? 182  ARG A CZ  1 
ATOM   1218 N NH1 . ARG A  1 155 ? -67.140 -24.797 13.560  1.00 17.62  1 182  ARG A NH1 1 
ATOM   1219 N NH2 . ARG A  1 155 ? -67.079 -22.507 13.328  1.00 26.10  ? 182  ARG A NH2 1 
ATOM   1220 N N   . ALA A  1 156 ? -74.735 -24.457 11.239  1.00 8.51   ? 183  ALA A N   1 
ATOM   1221 C CA  . ALA A  1 156 ? -75.940 -24.979 11.874  1.00 12.06  ? 183  ALA A CA  1 
ATOM   1222 C C   . ALA A  1 156 ? -76.268 -26.376 11.377  1.00 14.13  ? 183  ALA A C   1 
ATOM   1223 O O   . ALA A  1 156 ? -77.440 -26.734 11.263  1.00 16.30  ? 183  ALA A O   1 
ATOM   1224 C CB  . ALA A  1 156 ? -77.121 -24.044 11.634  1.00 9.22   ? 183  ALA A CB  1 
ATOM   1225 N N   . ASN A  1 157 ? -75.229 -27.160 11.098  1.00 15.07  ? 184  ASN A N   1 
ATOM   1226 C CA  . ASN A  1 157 ? -75.395 -28.492 10.527  1.00 15.78  ? 184  ASN A CA  1 
ATOM   1227 C C   . ASN A  1 157 ? -76.170 -28.404 9.221   1.00 15.36  ? 184  ASN A C   1 
ATOM   1228 O O   . ASN A  1 157 ? -77.071 -29.204 8.966   1.00 16.27  ? 184  ASN A O   1 
ATOM   1229 C CB  . ASN A  1 157 ? -76.103 -29.439 11.504  1.00 16.86  ? 184  ASN A CB  1 
ATOM   1230 C CG  . ASN A  1 157 ? -75.207 -29.884 12.648  1.00 16.70  ? 184  ASN A CG  1 
ATOM   1231 O OD1 . ASN A  1 157 ? -74.316 -30.707 12.460  1.00 15.07  ? 184  ASN A OD1 1 
ATOM   1232 N ND2 . ASN A  1 157 ? -75.462 -29.361 13.847  1.00 15.62  ? 184  ASN A ND2 1 
ATOM   1233 N N   . ILE A  1 158 ? -75.813 -27.415 8.408   1.00 11.23  ? 185  ILE A N   1 
ATOM   1234 C CA  . ILE A  1 158 ? -76.510 -27.134 7.161   1.00 11.50  ? 185  ILE A CA  1 
ATOM   1235 C C   . ILE A  1 158 ? -76.368 -28.253 6.141   1.00 13.84  ? 185  ILE A C   1 
ATOM   1236 O O   . ILE A  1 158 ? -75.258 -28.578 5.727   1.00 13.80  ? 185  ILE A O   1 
ATOM   1237 C CB  . ILE A  1 158 ? -75.979 -25.854 6.531   1.00 11.43  ? 185  ILE A CB  1 
ATOM   1238 C CG1 . ILE A  1 158 ? -76.152 -24.685 7.504   1.00 12.03  ? 185  ILE A CG1 1 
ATOM   1239 C CG2 . ILE A  1 158 ? -76.673 -25.598 5.206   1.00 14.58  ? 185  ILE A CG2 1 
ATOM   1240 C CD1 . ILE A  1 158 ? -75.728 -23.341 6.940   1.00 9.56   ? 185  ILE A CD1 1 
ATOM   1241 N N   . GLU A  1 159 ? -77.498 -28.819 5.719   1.00 18.17  ? 186  GLU A N   1 
ATOM   1242 C CA  . GLU A  1 159 ? -77.504 -29.982 4.825   1.00 17.26  ? 186  GLU A CA  1 
ATOM   1243 C C   . GLU A  1 159 ? -77.403 -29.626 3.345   1.00 13.88  ? 186  GLU A C   1 
ATOM   1244 O O   . GLU A  1 159 ? -76.883 -30.409 2.548   1.00 12.68  ? 186  GLU A O   1 
ATOM   1245 C CB  . GLU A  1 159 ? -78.737 -30.855 5.079   1.00 14.78  ? 186  GLU A CB  1 
ATOM   1246 C CG  . GLU A  1 159 ? -78.557 -31.839 6.219   1.00 18.32  ? 186  GLU A CG  1 
ATOM   1247 C CD  . GLU A  1 159 ? -79.854 -32.485 6.648   1.00 22.73  ? 186  GLU A CD  1 
ATOM   1248 O OE1 . GLU A  1 159 ? -79.811 -33.567 7.276   1.00 20.48  ? 186  GLU A OE1 1 
ATOM   1249 O OE2 . GLU A  1 159 ? -80.917 -31.901 6.362   1.00 28.12  1 186  GLU A OE2 1 
ATOM   1250 N N   . GLU A  1 160 ? -77.907 -28.450 2.986   1.00 14.12  ? 187  GLU A N   1 
ATOM   1251 C CA  . GLU A  1 160 ? -77.844 -27.970 1.609   1.00 18.06  ? 187  GLU A CA  1 
ATOM   1252 C C   . GLU A  1 160 ? -78.304 -26.528 1.511   1.00 20.06  ? 187  GLU A C   1 
ATOM   1253 O O   . GLU A  1 160 ? -79.248 -26.121 2.187   1.00 20.77  ? 187  GLU A O   1 
ATOM   1254 C CB  . GLU A  1 160 ? -78.694 -28.836 0.683   1.00 20.67  ? 187  GLU A CB  1 
ATOM   1255 C CG  . GLU A  1 160 ? -80.154 -28.947 1.069   1.00 16.71  ? 187  GLU A CG  1 
ATOM   1256 C CD  . GLU A  1 160 ? -80.914 -29.822 0.098   1.00 32.86  ? 187  GLU A CD  1 
ATOM   1257 O OE1 . GLU A  1 160 ? -80.755 -29.610 -1.125  1.00 39.44  ? 187  GLU A OE1 1 
ATOM   1258 O OE2 . GLU A  1 160 ? -81.650 -30.730 0.550   1.00 37.35  1 187  GLU A OE2 1 
ATOM   1259 N N   . MET A  1 161 ? -77.641 -25.757 0.659   1.00 17.05  ? 188  MET A N   1 
ATOM   1260 C CA  . MET A  1 161 ? -77.971 -24.350 0.537   1.00 19.76  ? 188  MET A CA  1 
ATOM   1261 C C   . MET A  1 161 ? -78.305 -23.977 -0.898  1.00 17.95  ? 188  MET A C   1 
ATOM   1262 O O   . MET A  1 161 ? -77.496 -24.180 -1.799  1.00 21.61  ? 188  MET A O   1 
ATOM   1263 C CB  . MET A  1 161 ? -76.832 -23.483 1.074   1.00 25.53  ? 188  MET A CB  1 
ATOM   1264 C CG  . MET A  1 161 ? -77.327 -22.219 1.758   1.00 37.33  ? 188  MET A CG  1 
ATOM   1265 S SD  . MET A  1 161 ? -78.655 -22.582 2.936   1.00 73.71  ? 188  MET A SD  1 
ATOM   1266 C CE  . MET A  1 161 ? -79.133 -20.942 3.471   1.00 23.35  ? 188  MET A CE  1 
ATOM   1267 N N   . PRO A  1 162 ? -79.510 -23.433 -1.109  1.00 16.26  ? 189  PRO A N   1 
ATOM   1268 C CA  . PRO A  1 162 ? -80.014 -23.036 -2.426  1.00 19.72  ? 189  PRO A CA  1 
ATOM   1269 C C   . PRO A  1 162 ? -79.428 -21.714 -2.912  1.00 18.34  ? 189  PRO A C   1 
ATOM   1270 O O   . PRO A  1 162 ? -79.345 -20.747 -2.155  1.00 18.09  ? 189  PRO A O   1 
ATOM   1271 C CB  . PRO A  1 162 ? -81.518 -22.899 -2.191  1.00 18.44  ? 189  PRO A CB  1 
ATOM   1272 C CG  . PRO A  1 162 ? -81.627 -22.533 -0.778  1.00 19.29  ? 189  PRO A CG  1 
ATOM   1273 C CD  . PRO A  1 162 ? -80.512 -23.223 -0.054  1.00 18.52  ? 189  PRO A CD  1 
ATOM   1274 N N   . SER A  1 163 ? -79.043 -21.695 -4.183  1.00 16.11  ? 190  SER A N   1 
ATOM   1275 C CA  . SER A  1 163 ? -78.329 -20.578 -4.795  1.00 18.15  ? 190  SER A CA  1 
ATOM   1276 C C   . SER A  1 163 ? -78.895 -19.191 -4.484  1.00 20.51  ? 190  SER A C   1 
ATOM   1277 O O   . SER A  1 163 ? -78.142 -18.233 -4.303  1.00 17.25  ? 190  SER A O   1 
ATOM   1278 C CB  . SER A  1 163 ? -78.254 -20.789 -6.308  1.00 21.54  ? 190  SER A CB  1 
ATOM   1279 O OG  . SER A  1 163 ? -79.295 -21.649 -6.746  1.00 19.81  ? 190  SER A OG  1 
ATOM   1280 N N   . HIS A  1 164 ? -80.217 -19.084 -4.395  1.00 23.98  ? 191  HIS A N   1 
ATOM   1281 C CA  . HIS A  1 164 ? -80.853 -17.781 -4.214  1.00 19.89  ? 191  HIS A CA  1 
ATOM   1282 C C   . HIS A  1 164 ? -80.654 -17.212 -2.811  1.00 19.53  ? 191  HIS A C   1 
ATOM   1283 O O   . HIS A  1 164 ? -81.382 -16.311 -2.392  1.00 17.60  ? 191  HIS A O   1 
ATOM   1284 C CB  . HIS A  1 164 ? -82.339 -17.833 -4.576  1.00 17.07  ? 191  HIS A CB  1 
ATOM   1285 C CG  . HIS A  1 164 ? -83.179 -18.591 -3.596  1.00 22.78  ? 191  HIS A CG  1 
ATOM   1286 N ND1 . HIS A  1 164 ? -83.514 -19.917 -3.772  1.00 26.29  ? 191  HIS A ND1 1 
ATOM   1287 C CD2 . HIS A  1 164 ? -83.762 -18.205 -2.435  1.00 18.57  ? 191  HIS A CD2 1 
ATOM   1288 C CE1 . HIS A  1 164 ? -84.264 -20.318 -2.760  1.00 23.57  ? 191  HIS A CE1 1 
ATOM   1289 N NE2 . HIS A  1 164 ? -84.432 -19.297 -1.936  1.00 21.17  ? 191  HIS A NE2 1 
ATOM   1290 N N   . LEU A  1 165 ? -79.669 -17.745 -2.092  1.00 20.43  ? 192  LEU A N   1 
ATOM   1291 C CA  . LEU A  1 165 ? -79.272 -17.191 -0.807  1.00 18.45  ? 192  LEU A CA  1 
ATOM   1292 C C   . LEU A  1 165 ? -78.298 -16.064 -1.075  1.00 19.43  ? 192  LEU A C   1 
ATOM   1293 O O   . LEU A  1 165 ? -78.445 -14.951 -0.548  1.00 17.95  ? 192  LEU A O   1 
ATOM   1294 C CB  . LEU A  1 165 ? -78.595 -18.250 0.057   1.00 14.51  ? 192  LEU A CB  1 
ATOM   1295 C CG  . LEU A  1 165 ? -78.068 -17.727 1.392   1.00 11.92  ? 192  LEU A CG  1 
ATOM   1296 C CD1 . LEU A  1 165 ? -79.169 -17.592 2.412   1.00 8.38   ? 192  LEU A CD1 1 
ATOM   1297 C CD2 . LEU A  1 165 ? -76.982 -18.626 1.904   1.00 17.29  ? 192  LEU A CD2 1 
ATOM   1298 N N   . PHE A  1 166 ? -77.316 -16.364 -1.922  1.00 15.49  ? 193  PHE A N   1 
ATOM   1299 C CA  . PHE A  1 166 ? -76.265 -15.413 -2.266  1.00 17.44  ? 193  PHE A CA  1 
ATOM   1300 C C   . PHE A  1 166 ? -76.710 -14.425 -3.340  1.00 19.16  ? 193  PHE A C   1 
ATOM   1301 O O   . PHE A  1 166 ? -75.974 -14.162 -4.284  1.00 17.16  ? 193  PHE A O   1 
ATOM   1302 C CB  . PHE A  1 166 ? -75.013 -16.151 -2.751  1.00 14.70  ? 193  PHE A CB  1 
ATOM   1303 C CG  . PHE A  1 166 ? -74.747 -17.443 -2.029  1.00 16.46  ? 193  PHE A CG  1 
ATOM   1304 C CD1 . PHE A  1 166 ? -74.313 -17.445 -0.716  1.00 18.81  ? 193  PHE A CD1 1 
ATOM   1305 C CD2 . PHE A  1 166 ? -74.920 -18.657 -2.668  1.00 18.22  ? 193  PHE A CD2 1 
ATOM   1306 C CE1 . PHE A  1 166 ? -74.068 -18.634 -0.052  1.00 15.85  ? 193  PHE A CE1 1 
ATOM   1307 C CE2 . PHE A  1 166 ? -74.677 -19.847 -2.011  1.00 16.69  ? 193  PHE A CE2 1 
ATOM   1308 C CZ  . PHE A  1 166 ? -74.251 -19.835 -0.702  1.00 15.42  ? 193  PHE A CZ  1 
ATOM   1309 N N   . ASP A  1 167 ? -77.907 -13.870 -3.198  1.00 22.53  ? 194  ASP A N   1 
ATOM   1310 C CA  . ASP A  1 167 ? -78.451 -13.008 -4.239  1.00 21.09  ? 194  ASP A CA  1 
ATOM   1311 C C   . ASP A  1 167 ? -77.942 -11.580 -4.133  1.00 22.08  ? 194  ASP A C   1 
ATOM   1312 O O   . ASP A  1 167 ? -77.611 -10.965 -5.142  1.00 24.99  ? 194  ASP A O   1 
ATOM   1313 C CB  . ASP A  1 167 ? -79.981 -13.044 -4.236  1.00 24.64  ? 194  ASP A CB  1 
ATOM   1314 C CG  . ASP A  1 167 ? -80.537 -14.245 -4.978  1.00 22.54  ? 194  ASP A CG  1 
ATOM   1315 O OD1 . ASP A  1 167 ? -79.731 -15.102 -5.402  1.00 20.56  ? 194  ASP A OD1 1 
ATOM   1316 O OD2 . ASP A  1 167 ? -81.776 -14.330 -5.137  1.00 22.02  1 194  ASP A OD2 1 
ATOM   1317 N N   . ASP A  1 168 ? -77.874 -11.061 -2.912  1.00 23.17  ? 195  ASP A N   1 
ATOM   1318 C CA  . ASP A  1 168 ? -77.453 -9.679  -2.692  1.00 24.49  ? 195  ASP A CA  1 
ATOM   1319 C C   . ASP A  1 168 ? -76.061 -9.604  -2.066  1.00 23.99  ? 195  ASP A C   1 
ATOM   1320 O O   . ASP A  1 168 ? -75.661 -8.565  -1.537  1.00 23.77  ? 195  ASP A O   1 
ATOM   1321 C CB  . ASP A  1 168 ? -78.468 -8.942  -1.810  1.00 25.91  ? 195  ASP A CB  1 
ATOM   1322 C CG  . ASP A  1 168 ? -79.900 -9.118  -2.291  1.00 24.33  ? 195  ASP A CG  1 
ATOM   1323 O OD1 . ASP A  1 168 ? -80.266 -10.246 -2.674  1.00 23.42  ? 195  ASP A OD1 1 
ATOM   1324 O OD2 . ASP A  1 168 ? -80.661 -8.130  -2.286  1.00 25.59  1 195  ASP A OD2 1 
ATOM   1325 N N   . LEU A  1 169 ? -75.326 -10.711 -2.137  1.00 25.13  ? 196  LEU A N   1 
ATOM   1326 C CA  . LEU A  1 169 ? -73.999 -10.806 -1.529  1.00 22.39  ? 196  LEU A CA  1 
ATOM   1327 C C   . LEU A  1 169 ? -72.909 -10.448 -2.527  1.00 20.59  ? 196  LEU A C   1 
ATOM   1328 O O   . LEU A  1 169 ? -71.929 -11.171 -2.661  1.00 18.59  ? 196  LEU A O   1 
ATOM   1329 C CB  . LEU A  1 169 ? -73.762 -12.222 -1.003  1.00 13.10  ? 196  LEU A CB  1 
ATOM   1330 C CG  . LEU A  1 169 ? -74.877 -12.761 -0.107  1.00 14.17  ? 196  LEU A CG  1 
ATOM   1331 C CD1 . LEU A  1 169 ? -74.455 -14.057 0.545   1.00 12.93  ? 196  LEU A CD1 1 
ATOM   1332 C CD2 . LEU A  1 169 ? -75.278 -11.743 0.946   1.00 14.41  ? 196  LEU A CD2 1 
ATOM   1333 N N   . GLU A  1 170 ? -73.088 -9.326  -3.218  1.00 25.99  ? 197  GLU A N   1 
ATOM   1334 C CA  . GLU A  1 170 ? -72.226 -8.939  -4.334  1.00 24.76  ? 197  GLU A CA  1 
ATOM   1335 C C   . GLU A  1 170 ? -70.808 -8.615  -3.889  1.00 24.20  ? 197  GLU A C   1 
ATOM   1336 O O   . GLU A  1 170 ? -69.861 -8.689  -4.677  1.00 22.53  ? 197  GLU A O   1 
ATOM   1337 C CB  . GLU A  1 170 ? -72.822 -7.728  -5.061  1.00 29.83  ? 197  GLU A CB  1 
ATOM   1338 C CG  . GLU A  1 170 ? -72.801 -6.435  -4.244  1.00 28.71  ? 197  GLU A CG  1 
ATOM   1339 C CD  . GLU A  1 170 ? -73.784 -5.394  -4.752  1.00 35.26  ? 197  GLU A CD  1 
ATOM   1340 O OE1 . GLU A  1 170 ? -74.551 -5.706  -5.691  1.00 44.66  ? 197  GLU A OE1 1 
ATOM   1341 O OE2 . GLU A  1 170 ? -73.798 -4.269  -4.204  1.00 28.09  1 197  GLU A OE2 1 
ATOM   1342 N N   . ASN A  1 171 ? -70.665 -8.252  -2.621  1.00 24.43  ? 198  ASN A N   1 
ATOM   1343 C CA  . ASN A  1 171 ? -69.375 -7.827  -2.105  1.00 23.12  ? 198  ASN A CA  1 
ATOM   1344 C C   . ASN A  1 171 ? -68.731 -8.876  -1.225  1.00 18.54  ? 198  ASN A C   1 
ATOM   1345 O O   . ASN A  1 171 ? -67.695 -8.627  -0.612  1.00 16.98  ? 198  ASN A O   1 
ATOM   1346 C CB  . ASN A  1 171 ? -69.510 -6.503  -1.359  1.00 21.41  ? 198  ASN A CB  1 
ATOM   1347 C CG  . ASN A  1 171 ? -69.714 -5.333  -2.300  1.00 33.03  ? 198  ASN A CG  1 
ATOM   1348 O OD1 . ASN A  1 171 ? -69.687 -5.495  -3.526  1.00 30.11  ? 198  ASN A OD1 1 
ATOM   1349 N ND2 . ASN A  1 171 ? -69.927 -4.147  -1.736  1.00 34.98  ? 198  ASN A ND2 1 
ATOM   1350 N N   . LEU A  1 172 ? -69.346 -10.053 -1.175  1.00 17.59  ? 199  LEU A N   1 
ATOM   1351 C CA  . LEU A  1 172 ? -68.819 -11.143 -0.372  1.00 13.41  ? 199  LEU A CA  1 
ATOM   1352 C C   . LEU A  1 172 ? -67.536 -11.659 -0.987  1.00 16.18  ? 199  LEU A C   1 
ATOM   1353 O O   . LEU A  1 172 ? -67.526 -12.104 -2.138  1.00 15.95  ? 199  LEU A O   1 
ATOM   1354 C CB  . LEU A  1 172 ? -69.819 -12.281 -0.268  1.00 10.86  ? 199  LEU A CB  1 
ATOM   1355 C CG  . LEU A  1 172 ? -69.622 -13.113 0.991   1.00 8.76   ? 199  LEU A CG  1 
ATOM   1356 C CD1 . LEU A  1 172 ? -70.124 -12.329 2.177   1.00 9.03   ? 199  LEU A CD1 1 
ATOM   1357 C CD2 . LEU A  1 172 ? -70.337 -14.442 0.887   1.00 10.58  ? 199  LEU A CD2 1 
ATOM   1358 N N   . GLU A  1 173 ? -66.458 -11.592 -0.208  1.00 15.70  ? 200  GLU A N   1 
ATOM   1359 C CA  . GLU A  1 173 ? -65.144 -12.021 -0.660  1.00 11.54  ? 200  GLU A CA  1 
ATOM   1360 C C   . GLU A  1 173 ? -64.752 -13.381 -0.089  1.00 13.97  ? 200  GLU A C   1 
ATOM   1361 O O   . GLU A  1 173 ? -64.019 -14.131 -0.730  1.00 14.66  ? 200  GLU A O   1 
ATOM   1362 C CB  . GLU A  1 173 ? -64.094 -10.984 -0.283  1.00 12.14  ? 200  GLU A CB  1 
ATOM   1363 C CG  . GLU A  1 173 ? -64.357 -9.607  -0.845  1.00 16.97  ? 200  GLU A CG  1 
ATOM   1364 C CD  . GLU A  1 173 ? -63.209 -8.650  -0.589  1.00 20.57  ? 200  GLU A CD  1 
ATOM   1365 O OE1 . GLU A  1 173 ? -62.065 -8.974  -0.974  1.00 17.13  ? 200  GLU A OE1 1 
ATOM   1366 O OE2 . GLU A  1 173 ? -63.451 -7.576  0.001   1.00 21.85  1 200  GLU A OE2 1 
ATOM   1367 N N   . SER A  1 174 ? -65.236 -13.700 1.111   1.00 12.39  ? 201  SER A N   1 
ATOM   1368 C CA  . SER A  1 174 ? -64.866 -14.954 1.771   1.00 9.51   ? 201  SER A CA  1 
ATOM   1369 C C   . SER A  1 174 ? -66.039 -15.693 2.415   1.00 9.78   ? 201  SER A C   1 
ATOM   1370 O O   . SER A  1 174 ? -66.870 -15.093 3.094   1.00 10.24  ? 201  SER A O   1 
ATOM   1371 C CB  . SER A  1 174 ? -63.790 -14.696 2.816   1.00 9.82   ? 201  SER A CB  1 
ATOM   1372 O OG  . SER A  1 174 ? -64.213 -13.687 3.714   1.00 13.20  ? 201  SER A OG  1 
ATOM   1373 N N   . ILE A  1 175 ? -66.075 -17.007 2.208   1.00 9.78   ? 202  ILE A N   1 
ATOM   1374 C CA  . ILE A  1 175 ? -67.153 -17.868 2.688   1.00 9.37   ? 202  ILE A CA  1 
ATOM   1375 C C   . ILE A  1 175 ? -66.606 -18.934 3.631   1.00 10.98  ? 202  ILE A C   1 
ATOM   1376 O O   . ILE A  1 175 ? -65.643 -19.624 3.295   1.00 11.63  ? 202  ILE A O   1 
ATOM   1377 C CB  . ILE A  1 175 ? -67.828 -18.606 1.510   1.00 10.31  ? 202  ILE A CB  1 
ATOM   1378 C CG1 . ILE A  1 175 ? -68.782 -17.689 0.749   1.00 13.32  ? 202  ILE A CG1 1 
ATOM   1379 C CG2 . ILE A  1 175 ? -68.592 -19.809 1.997   1.00 8.71   ? 202  ILE A CG2 1 
ATOM   1380 C CD1 . ILE A  1 175 ? -69.370 -18.331 -0.501  1.00 9.05   ? 202  ILE A CD1 1 
ATOM   1381 N N   . GLU A  1 176 ? -67.223 -19.080 4.801   1.00 9.19   ? 203  GLU A N   1 
ATOM   1382 C CA  . GLU A  1 176 ? -66.833 -20.129 5.738   1.00 9.75   ? 203  GLU A CA  1 
ATOM   1383 C C   . GLU A  1 176 ? -68.016 -20.991 6.156   1.00 10.58  ? 203  GLU A C   1 
ATOM   1384 O O   . GLU A  1 176 ? -68.810 -20.591 7.011   1.00 10.32  ? 203  GLU A O   1 
ATOM   1385 C CB  . GLU A  1 176 ? -66.164 -19.533 6.979   1.00 10.53  ? 203  GLU A CB  1 
ATOM   1386 C CG  . GLU A  1 176 ? -65.824 -20.555 8.063   1.00 10.68  ? 203  GLU A CG  1 
ATOM   1387 C CD  . GLU A  1 176 ? -64.998 -21.717 7.540   1.00 14.96  ? 203  GLU A CD  1 
ATOM   1388 O OE1 . GLU A  1 176 ? -63.792 -21.798 7.875   1.00 17.16  ? 203  GLU A OE1 1 
ATOM   1389 O OE2 . GLU A  1 176 ? -65.553 -22.552 6.790   1.00 14.12  1 203  GLU A OE2 1 
ATOM   1390 N N   . PHE A  1 177 ? -68.119 -22.179 5.561   1.00 10.92  ? 204  PHE A N   1 
ATOM   1391 C CA  . PHE A  1 177 ? -69.206 -23.109 5.871   1.00 10.72  ? 204  PHE A CA  1 
ATOM   1392 C C   . PHE A  1 177 ? -68.711 -24.470 6.360   1.00 10.16  ? 204  PHE A C   1 
ATOM   1393 O O   . PHE A  1 177 ? -69.310 -25.498 6.050   1.00 11.52  ? 204  PHE A O   1 
ATOM   1394 C CB  . PHE A  1 177 ? -70.106 -23.312 4.651   1.00 8.68   ? 204  PHE A CB  1 
ATOM   1395 C CG  . PHE A  1 177 ? -70.890 -22.102 4.269   1.00 5.96   ? 204  PHE A CG  1 
ATOM   1396 C CD1 . PHE A  1 177 ? -71.399 -21.257 5.238   1.00 7.24   ? 204  PHE A CD1 1 
ATOM   1397 C CD2 . PHE A  1 177 ? -71.123 -21.809 2.943   1.00 5.31   ? 204  PHE A CD2 1 
ATOM   1398 C CE1 . PHE A  1 177 ? -72.131 -20.133 4.886   1.00 6.89   ? 204  PHE A CE1 1 
ATOM   1399 C CE2 . PHE A  1 177 ? -71.848 -20.687 2.583   1.00 7.68   ? 204  PHE A CE2 1 
ATOM   1400 C CZ  . PHE A  1 177 ? -72.352 -19.848 3.556   1.00 6.53   ? 204  PHE A CZ  1 
ATOM   1401 N N   . GLY A  1 178 ? -67.627 -24.477 7.124   1.00 8.98   ? 205  GLY A N   1 
ATOM   1402 C CA  . GLY A  1 178 ? -67.109 -25.713 7.678   1.00 9.08   ? 205  GLY A CA  1 
ATOM   1403 C C   . GLY A  1 178 ? -67.996 -26.300 8.759   1.00 9.24   ? 205  GLY A C   1 
ATOM   1404 O O   . GLY A  1 178 ? -68.720 -25.573 9.438   1.00 10.63  ? 205  GLY A O   1 
ATOM   1405 N N   . SER A  1 179 ? -67.928 -27.618 8.925   1.00 8.37   ? 206  SER A N   1 
ATOM   1406 C CA  . SER A  1 179 ? -68.726 -28.338 9.923   1.00 14.02  ? 206  SER A CA  1 
ATOM   1407 C C   . SER A  1 179 ? -70.242 -28.175 9.728   1.00 18.57  ? 206  SER A C   1 
ATOM   1408 O O   . SER A  1 179 ? -71.021 -28.129 10.688  1.00 19.96  ? 206  SER A O   1 
ATOM   1409 C CB  . SER A  1 179 ? -68.297 -27.983 11.349  1.00 16.46  ? 206  SER A CB  1 
ATOM   1410 O OG  . SER A  1 179 ? -68.390 -26.589 11.578  1.00 17.98  ? 206  SER A OG  1 
ATOM   1411 N N   . ASN A  1 180 ? -70.641 -28.078 8.466   1.00 16.31  ? 207  ASN A N   1 
ATOM   1412 C CA  . ASN A  1 180 ? -72.031 -28.199 8.067   1.00 12.29  ? 207  ASN A CA  1 
ATOM   1413 C C   . ASN A  1 180 ? -72.175 -29.550 7.381   1.00 14.86  ? 207  ASN A C   1 
ATOM   1414 O O   . ASN A  1 180 ? -71.230 -30.335 7.370   1.00 18.36  ? 207  ASN A O   1 
ATOM   1415 C CB  . ASN A  1 180 ? -72.405 -27.063 7.124   1.00 11.93  ? 207  ASN A CB  1 
ATOM   1416 C CG  . ASN A  1 180 ? -72.430 -25.722 7.821   1.00 10.96  ? 207  ASN A CG  1 
ATOM   1417 O OD1 . ASN A  1 180 ? -73.088 -25.562 8.851   1.00 12.64  ? 207  ASN A OD1 1 
ATOM   1418 N ND2 . ASN A  1 180 ? -71.706 -24.751 7.272   1.00 7.23   ? 207  ASN A ND2 1 
ATOM   1419 N N   . LYS A  1 181 ? -73.334 -29.835 6.801   1.00 14.21  ? 208  LYS A N   1 
ATOM   1420 C CA  . LYS A  1 181 ? -73.536 -31.148 6.198   1.00 14.92  ? 208  LYS A CA  1 
ATOM   1421 C C   . LYS A  1 181 ? -73.626 -31.113 4.677   1.00 12.91  ? 208  LYS A C   1 
ATOM   1422 O O   . LYS A  1 181 ? -74.211 -32.015 4.084   1.00 15.52  ? 208  LYS A O   1 
ATOM   1423 C CB  . LYS A  1 181 ? -74.787 -31.824 6.765   1.00 16.36  ? 208  LYS A CB  1 
ATOM   1424 C CG  . LYS A  1 181 ? -74.670 -32.318 8.197   1.00 16.28  ? 208  LYS A CG  1 
ATOM   1425 C CD  . LYS A  1 181 ? -75.847 -33.214 8.529   1.00 17.60  ? 208  LYS A CD  1 
ATOM   1426 C CE  . LYS A  1 181 ? -75.832 -33.660 9.972   1.00 20.44  ? 208  LYS A CE  1 
ATOM   1427 N NZ  . LYS A  1 181 ? -77.005 -34.528 10.280  1.00 25.11  1 208  LYS A NZ  1 
ATOM   1428 N N   . LEU A  1 182 ? -73.046 -30.090 4.052   1.00 10.16  ? 209  LEU A N   1 
ATOM   1429 C CA  . LEU A  1 182 ? -73.131 -29.930 2.597   1.00 11.14  ? 209  LEU A CA  1 
ATOM   1430 C C   . LEU A  1 182 ? -72.725 -31.180 1.826   1.00 11.81  ? 209  LEU A C   1 
ATOM   1431 O O   . LEU A  1 182 ? -71.576 -31.607 1.875   1.00 11.03  ? 209  LEU A O   1 
ATOM   1432 C CB  . LEU A  1 182 ? -72.282 -28.756 2.117   1.00 9.74   ? 209  LEU A CB  1 
ATOM   1433 C CG  . LEU A  1 182 ? -72.570 -27.373 2.688   1.00 8.37   ? 209  LEU A CG  1 
ATOM   1434 C CD1 . LEU A  1 182 ? -72.044 -26.324 1.734   1.00 6.17   ? 209  LEU A CD1 1 
ATOM   1435 C CD2 . LEU A  1 182 ? -74.048 -27.181 2.956   1.00 11.15  ? 209  LEU A CD2 1 
ATOM   1436 N N   . ARG A  1 183 ? -73.676 -31.754 1.100   1.00 15.93  ? 210  ARG A N   1 
ATOM   1437 C CA  . ARG A  1 183 ? -73.425 -32.982 0.360   1.00 17.51  ? 210  ARG A CA  1 
ATOM   1438 C C   . ARG A  1 183 ? -73.114 -32.663 -1.094  1.00 15.54  ? 210  ARG A C   1 
ATOM   1439 O O   . ARG A  1 183 ? -72.593 -33.501 -1.828  1.00 14.08  ? 210  ARG A O   1 
ATOM   1440 C CB  . ARG A  1 183 ? -74.632 -33.918 0.454   1.00 21.08  ? 210  ARG A CB  1 
ATOM   1441 C CG  . ARG A  1 183 ? -75.437 -33.757 1.740   1.00 21.68  ? 210  ARG A CG  1 
ATOM   1442 C CD  . ARG A  1 183 ? -76.449 -34.875 1.934   1.00 22.64  ? 210  ARG A CD  1 
ATOM   1443 N NE  . ARG A  1 183 ? -77.238 -34.682 3.147   1.00 28.20  ? 210  ARG A NE  1 
ATOM   1444 C CZ  . ARG A  1 183 ? -76.857 -35.071 4.362   1.00 36.38  ? 210  ARG A CZ  1 
ATOM   1445 N NH1 . ARG A  1 183 ? -75.691 -35.678 4.535   1.00 36.88  1 210  ARG A NH1 1 
ATOM   1446 N NH2 . ARG A  1 183 ? -77.642 -34.851 5.409   1.00 36.08  ? 210  ARG A NH2 1 
ATOM   1447 N N   . GLN A  1 184 ? -73.432 -31.440 -1.502  1.00 15.65  ? 211  GLN A N   1 
ATOM   1448 C CA  . GLN A  1 184 ? -73.186 -31.019 -2.873  1.00 18.99  ? 211  GLN A CA  1 
ATOM   1449 C C   . GLN A  1 184 ? -72.907 -29.530 -2.972  1.00 17.33  ? 211  GLN A C   1 
ATOM   1450 O O   . GLN A  1 184 ? -73.478 -28.727 -2.241  1.00 16.65  ? 211  GLN A O   1 
ATOM   1451 C CB  . GLN A  1 184 ? -74.383 -31.358 -3.752  1.00 20.70  ? 211  GLN A CB  1 
ATOM   1452 C CG  . GLN A  1 184 ? -74.107 -31.248 -5.230  1.00 20.03  ? 211  GLN A CG  1 
ATOM   1453 C CD  . GLN A  1 184 ? -74.308 -32.569 -5.927  1.00 31.61  ? 211  GLN A CD  1 
ATOM   1454 O OE1 . GLN A  1 184 ? -74.818 -33.519 -5.332  1.00 25.77  ? 211  GLN A OE1 1 
ATOM   1455 N NE2 . GLN A  1 184 ? -73.904 -32.643 -7.192  1.00 52.47  ? 211  GLN A NE2 1 
ATOM   1456 N N   . MET A  1 185 ? -72.026 -29.168 -3.892  1.00 19.80  ? 212  MET A N   1 
ATOM   1457 C CA  . MET A  1 185 ? -71.747 -27.771 -4.169  1.00 21.76  ? 212  MET A CA  1 
ATOM   1458 C C   . MET A  1 185 ? -72.931 -27.100 -4.886  1.00 25.52  ? 212  MET A C   1 
ATOM   1459 O O   . MET A  1 185 ? -73.386 -27.575 -5.936  1.00 25.46  ? 212  MET A O   1 
ATOM   1460 C CB  . MET A  1 185 ? -70.476 -27.660 -5.012  1.00 20.41  ? 212  MET A CB  1 
ATOM   1461 C CG  . MET A  1 185 ? -70.170 -26.257 -5.489  1.00 22.00  ? 212  MET A CG  1 
ATOM   1462 S SD  . MET A  1 185 ? -69.390 -25.265 -4.213  1.00 12.68  ? 212  MET A SD  1 
ATOM   1463 C CE  . MET A  1 185 ? -67.884 -26.207 -4.014  1.00 19.65  ? 212  MET A CE  1 
ATOM   1464 N N   . PRO A  1 186 ? -73.442 -25.999 -4.308  1.00 20.62  ? 213  PRO A N   1 
ATOM   1465 C CA  . PRO A  1 186 ? -74.508 -25.194 -4.914  1.00 20.01  ? 213  PRO A CA  1 
ATOM   1466 C C   . PRO A  1 186 ? -74.126 -24.717 -6.301  1.00 22.67  ? 213  PRO A C   1 
ATOM   1467 O O   . PRO A  1 186 ? -73.060 -24.128 -6.470  1.00 20.06  ? 213  PRO A O   1 
ATOM   1468 C CB  . PRO A  1 186 ? -74.609 -23.994 -3.973  1.00 15.24  ? 213  PRO A CB  1 
ATOM   1469 C CG  . PRO A  1 186 ? -74.200 -24.533 -2.663  1.00 16.68  ? 213  PRO A CG  1 
ATOM   1470 C CD  . PRO A  1 186 ? -73.114 -25.534 -2.950  1.00 15.47  ? 213  PRO A CD  1 
ATOM   1471 N N   . ARG A  1 187 ? -74.988 -24.969 -7.280  1.00 31.92  ? 214  ARG A N   1 
ATOM   1472 C CA  . ARG A  1 187 ? -74.740 -24.526 -8.647  1.00 32.55  ? 214  ARG A CA  1 
ATOM   1473 C C   . ARG A  1 187 ? -75.110 -23.061 -8.827  1.00 22.28  ? 214  ARG A C   1 
ATOM   1474 O O   . ARG A  1 187 ? -75.940 -22.528 -8.093  1.00 17.22  ? 214  ARG A O   1 
ATOM   1475 C CB  . ARG A  1 187 ? -75.509 -25.395 -9.643  1.00 36.71  ? 214  ARG A CB  1 
ATOM   1476 C CG  . ARG A  1 187 ? -75.085 -26.858 -9.634  1.00 50.99  ? 214  ARG A CG  1 
ATOM   1477 C CD  . ARG A  1 187 ? -73.624 -27.023 -10.036 1.00 50.52  ? 214  ARG A CD  1 
ATOM   1478 N NE  . ARG A  1 187 ? -73.234 -28.429 -10.120 1.00 51.61  ? 214  ARG A NE  1 
ATOM   1479 C CZ  . ARG A  1 187 ? -73.500 -29.219 -11.158 1.00 54.06  ? 214  ARG A CZ  1 
ATOM   1480 N NH1 . ARG A  1 187 ? -74.168 -28.746 -12.203 1.00 45.23  1 214  ARG A NH1 1 
ATOM   1481 N NH2 . ARG A  1 187 ? -73.104 -30.485 -11.148 1.00 55.58  ? 214  ARG A NH2 1 
ATOM   1482 N N   . GLY A  1 188 ? -74.474 -22.419 -9.801  1.00 25.67  ? 215  GLY A N   1 
ATOM   1483 C CA  . GLY A  1 188 ? -74.747 -21.031 -10.135 1.00 30.31  ? 215  GLY A CA  1 
ATOM   1484 C C   . GLY A  1 188 ? -74.646 -20.066 -8.970  1.00 28.95  ? 215  GLY A C   1 
ATOM   1485 O O   . GLY A  1 188 ? -75.627 -19.414 -8.610  1.00 31.08  ? 215  GLY A O   1 
ATOM   1486 N N   . ILE A  1 189 ? -73.459 -19.965 -8.379  1.00 29.26  ? 216  ILE A N   1 
ATOM   1487 C CA  . ILE A  1 189 ? -73.273 -19.100 -7.219  1.00 27.07  ? 216  ILE A CA  1 
ATOM   1488 C C   . ILE A  1 189 ? -72.163 -18.072 -7.411  1.00 27.63  ? 216  ILE A C   1 
ATOM   1489 O O   . ILE A  1 189 ? -72.236 -16.972 -6.862  1.00 26.17  ? 216  ILE A O   1 
ATOM   1490 C CB  . ILE A  1 189 ? -72.980 -19.913 -5.942  1.00 22.68  ? 216  ILE A CB  1 
ATOM   1491 C CG1 . ILE A  1 189 ? -71.817 -20.874 -6.188  1.00 21.46  ? 216  ILE A CG1 1 
ATOM   1492 C CG2 . ILE A  1 189 ? -74.216 -20.679 -5.504  1.00 23.05  ? 216  ILE A CG2 1 
ATOM   1493 C CD1 . ILE A  1 189 ? -71.398 -21.643 -4.972  1.00 19.85  ? 216  ILE A CD1 1 
ATOM   1494 N N   . PHE A  1 190 ? -71.141 -18.422 -8.189  1.00 24.94  ? 217  PHE A N   1 
ATOM   1495 C CA  . PHE A  1 190 ? -69.972 -17.555 -8.312  1.00 21.05  ? 217  PHE A CA  1 
ATOM   1496 C C   . PHE A  1 190 ? -70.268 -16.330 -9.159  1.00 20.96  ? 217  PHE A C   1 
ATOM   1497 O O   . PHE A  1 190 ? -69.558 -15.328 -9.084  1.00 20.62  ? 217  PHE A O   1 
ATOM   1498 C CB  . PHE A  1 190 ? -68.761 -18.328 -8.834  1.00 18.17  ? 217  PHE A CB  1 
ATOM   1499 C CG  . PHE A  1 190 ? -68.408 -19.520 -7.991  1.00 20.84  ? 217  PHE A CG  1 
ATOM   1500 C CD1 . PHE A  1 190 ? -68.131 -19.370 -6.646  1.00 15.15  ? 217  PHE A CD1 1 
ATOM   1501 C CD2 . PHE A  1 190 ? -68.373 -20.793 -8.537  1.00 27.01  ? 217  PHE A CD2 1 
ATOM   1502 C CE1 . PHE A  1 190 ? -67.825 -20.462 -5.864  1.00 14.12  ? 217  PHE A CE1 1 
ATOM   1503 C CE2 . PHE A  1 190 ? -68.057 -21.892 -7.755  1.00 20.89  ? 217  PHE A CE2 1 
ATOM   1504 C CZ  . PHE A  1 190 ? -67.789 -21.724 -6.418  1.00 14.36  ? 217  PHE A CZ  1 
ATOM   1505 N N   . GLY A  1 191 ? -71.336 -16.413 -9.946  1.00 20.36  ? 218  GLY A N   1 
ATOM   1506 C CA  . GLY A  1 191 ? -71.793 -15.287 -10.735 1.00 17.99  ? 218  GLY A CA  1 
ATOM   1507 C C   . GLY A  1 191 ? -72.358 -14.170 -9.877  1.00 18.79  ? 218  GLY A C   1 
ATOM   1508 O O   . GLY A  1 191 ? -72.332 -13.002 -10.268 1.00 25.30  ? 218  GLY A O   1 
ATOM   1509 N N   . LYS A  1 192 ? -72.868 -14.518 -8.702  1.00 14.92  ? 219  LYS A N   1 
ATOM   1510 C CA  . LYS A  1 192 ? -73.474 -13.520 -7.833  1.00 16.18  ? 219  LYS A CA  1 
ATOM   1511 C C   . LYS A  1 192 ? -72.444 -12.905 -6.893  1.00 17.72  ? 219  LYS A C   1 
ATOM   1512 O O   . LYS A  1 192 ? -72.691 -11.871 -6.269  1.00 15.58  ? 219  LYS A O   1 
ATOM   1513 C CB  . LYS A  1 192 ? -74.636 -14.125 -7.041  1.00 18.28  ? 219  LYS A CB  1 
ATOM   1514 C CG  . LYS A  1 192 ? -75.697 -14.814 -7.904  1.00 31.77  ? 219  LYS A CG  1 
ATOM   1515 C CD  . LYS A  1 192 ? -77.126 -14.522 -7.421  1.00 30.43  ? 219  LYS A CD  1 
ATOM   1516 C CE  . LYS A  1 192 ? -77.533 -13.065 -7.675  1.00 26.81  ? 219  LYS A CE  1 
ATOM   1517 N NZ  . LYS A  1 192 ? -77.720 -12.740 -9.126  1.00 22.51  1 219  LYS A NZ  1 
ATOM   1518 N N   . MET A  1 193 ? -71.285 -13.551 -6.803  1.00 19.49  ? 220  MET A N   1 
ATOM   1519 C CA  . MET A  1 193 ? -70.203 -13.091 -5.940  1.00 21.02  ? 220  MET A CA  1 
ATOM   1520 C C   . MET A  1 193 ? -68.903 -13.033 -6.729  1.00 19.61  ? 220  MET A C   1 
ATOM   1521 O O   . MET A  1 193 ? -68.113 -13.976 -6.700  1.00 18.60  ? 220  MET A O   1 
ATOM   1522 C CB  . MET A  1 193 ? -70.047 -14.026 -4.740  1.00 16.69  ? 220  MET A CB  1 
ATOM   1523 C CG  . MET A  1 193 ? -71.299 -14.148 -3.886  1.00 14.22  ? 220  MET A CG  1 
ATOM   1524 S SD  . MET A  1 193 ? -71.192 -15.463 -2.661  1.00 13.25  ? 220  MET A SD  1 
ATOM   1525 C CE  . MET A  1 193 ? -70.753 -16.850 -3.708  1.00 13.05  ? 220  MET A CE  1 
ATOM   1526 N N   . PRO A  1 194 ? -68.677 -11.914 -7.433  1.00 19.45  ? 221  PRO A N   1 
ATOM   1527 C CA  . PRO A  1 194 ? -67.548 -11.752 -8.353  1.00 22.74  ? 221  PRO A CA  1 
ATOM   1528 C C   . PRO A  1 194 ? -66.249 -11.361 -7.647  1.00 21.96  ? 221  PRO A C   1 
ATOM   1529 O O   . PRO A  1 194 ? -65.217 -11.219 -8.303  1.00 16.62  ? 221  PRO A O   1 
ATOM   1530 C CB  . PRO A  1 194 ? -68.009 -10.610 -9.272  1.00 22.53  ? 221  PRO A CB  1 
ATOM   1531 C CG  . PRO A  1 194 ? -69.305 -10.074 -8.671  1.00 19.84  ? 221  PRO A CG  1 
ATOM   1532 C CD  . PRO A  1 194 ? -69.453 -10.673 -7.314  1.00 18.38  ? 221  PRO A CD  1 
ATOM   1533 N N   . LYS A  1 195 ? -66.308 -11.191 -6.329  1.00 19.47  ? 222  LYS A N   1 
ATOM   1534 C CA  . LYS A  1 195 ? -65.141 -10.788 -5.555  1.00 16.58  ? 222  LYS A CA  1 
ATOM   1535 C C   . LYS A  1 195 ? -64.771 -11.848 -4.528  1.00 16.75  ? 222  LYS A C   1 
ATOM   1536 O O   . LYS A  1 195 ? -63.968 -11.601 -3.628  1.00 14.50  ? 222  LYS A O   1 
ATOM   1537 C CB  . LYS A  1 195 ? -65.407 -9.460  -4.848  1.00 18.22  ? 222  LYS A CB  1 
ATOM   1538 C CG  . LYS A  1 195 ? -65.376 -8.252  -5.762  1.00 22.90  ? 222  LYS A CG  1 
ATOM   1539 C CD  . LYS A  1 195 ? -65.829 -6.999  -5.032  1.00 25.94  ? 222  LYS A CD  1 
ATOM   1540 C CE  . LYS A  1 195 ? -65.055 -6.798  -3.741  1.00 22.49  ? 222  LYS A CE  1 
ATOM   1541 N NZ  . LYS A  1 195 ? -65.505 -5.570  -3.031  1.00 30.11  1 222  LYS A NZ  1 
ATOM   1542 N N   . LEU A  1 196 ? -65.368 -13.026 -4.662  1.00 17.05  ? 223  LEU A N   1 
ATOM   1543 C CA  . LEU A  1 196 ? -65.154 -14.093 -3.697  1.00 14.71  ? 223  LEU A CA  1 
ATOM   1544 C C   . LEU A  1 196 ? -63.734 -14.627 -3.811  1.00 12.87  ? 223  LEU A C   1 
ATOM   1545 O O   . LEU A  1 196 ? -63.305 -15.010 -4.895  1.00 14.53  ? 223  LEU A O   1 
ATOM   1546 C CB  . LEU A  1 196 ? -66.156 -15.223 -3.928  1.00 12.75  ? 223  LEU A CB  1 
ATOM   1547 C CG  . LEU A  1 196 ? -66.089 -16.368 -2.919  1.00 10.15  ? 223  LEU A CG  1 
ATOM   1548 C CD1 . LEU A  1 196 ? -66.582 -15.915 -1.558  1.00 9.03   ? 223  LEU A CD1 1 
ATOM   1549 C CD2 . LEU A  1 196 ? -66.879 -17.560 -3.415  1.00 9.57   ? 223  LEU A CD2 1 
ATOM   1550 N N   . LYS A  1 197 ? -63.004 -14.654 -2.699  1.00 10.43  ? 224  LYS A N   1 
ATOM   1551 C CA  . LYS A  1 197 ? -61.621 -15.126 -2.722  1.00 10.77  ? 224  LYS A CA  1 
ATOM   1552 C C   . LYS A  1 197 ? -61.397 -16.389 -1.903  1.00 12.29  ? 224  LYS A C   1 
ATOM   1553 O O   . LYS A  1 197 ? -60.756 -17.324 -2.374  1.00 15.06  ? 224  LYS A O   1 
ATOM   1554 C CB  . LYS A  1 197 ? -60.649 -14.022 -2.296  1.00 10.79  ? 224  LYS A CB  1 
ATOM   1555 C CG  . LYS A  1 197 ? -60.349 -13.026 -3.403  1.00 9.04   ? 224  LYS A CG  1 
ATOM   1556 C CD  . LYS A  1 197 ? -60.107 -11.639 -2.856  1.00 10.64  ? 224  LYS A CD  1 
ATOM   1557 C CE  . LYS A  1 197 ? -60.742 -10.590 -3.756  1.00 16.32  ? 224  LYS A CE  1 
ATOM   1558 N NZ  . LYS A  1 197 ? -60.837 -9.264  -3.077  1.00 23.50  1 224  LYS A NZ  1 
ATOM   1559 N N   . GLN A  1 198 ? -61.919 -16.427 -0.683  1.00 10.82  ? 225  GLN A N   1 
ATOM   1560 C CA  . GLN A  1 198 ? -61.762 -17.618 0.145   1.00 11.29  ? 225  GLN A CA  1 
ATOM   1561 C C   . GLN A  1 198 ? -63.033 -18.461 0.151   1.00 12.00  ? 225  GLN A C   1 
ATOM   1562 O O   . GLN A  1 198 ? -64.132 -17.941 0.311   1.00 15.91  ? 225  GLN A O   1 
ATOM   1563 C CB  . GLN A  1 198 ? -61.364 -17.243 1.575   1.00 11.16  ? 225  GLN A CB  1 
ATOM   1564 C CG  . GLN A  1 198 ? -60.881 -18.420 2.416   1.00 11.86  ? 225  GLN A CG  1 
ATOM   1565 C CD  . GLN A  1 198 ? -59.585 -19.030 1.896   1.00 14.81  ? 225  GLN A CD  1 
ATOM   1566 O OE1 . GLN A  1 198 ? -58.595 -18.324 1.677   1.00 14.71  ? 225  GLN A OE1 1 
ATOM   1567 N NE2 . GLN A  1 198 ? -59.588 -20.349 1.693   1.00 11.15  ? 225  GLN A NE2 1 
ATOM   1568 N N   . LEU A  1 199 ? -62.884 -19.767 -0.023  1.00 10.21  ? 226  LEU A N   1 
ATOM   1569 C CA  . LEU A  1 199 ? -64.034 -20.660 -0.006  1.00 10.36  ? 226  LEU A CA  1 
ATOM   1570 C C   . LEU A  1 199 ? -63.793 -21.853 0.923   1.00 13.32  ? 226  LEU A C   1 
ATOM   1571 O O   . LEU A  1 199 ? -63.395 -22.928 0.473   1.00 15.90  ? 226  LEU A O   1 
ATOM   1572 C CB  . LEU A  1 199 ? -64.336 -21.137 -1.430  1.00 11.57  ? 226  LEU A CB  1 
ATOM   1573 C CG  . LEU A  1 199 ? -65.518 -22.080 -1.671  1.00 8.94   ? 226  LEU A CG  1 
ATOM   1574 C CD1 . LEU A  1 199 ? -66.827 -21.396 -1.350  1.00 8.77   ? 226  LEU A CD1 1 
ATOM   1575 C CD2 . LEU A  1 199 ? -65.508 -22.575 -3.097  1.00 8.04   ? 226  LEU A CD2 1 
ATOM   1576 N N   . ASN A  1 200 ? -64.021 -21.671 2.221   1.00 11.89  ? 227  ASN A N   1 
ATOM   1577 C CA  . ASN A  1 200 ? -63.788 -22.759 3.172   1.00 12.69  ? 227  ASN A CA  1 
ATOM   1578 C C   . ASN A  1 200 ? -64.968 -23.715 3.246   1.00 12.89  ? 227  ASN A C   1 
ATOM   1579 O O   . ASN A  1 200 ? -66.051 -23.344 3.704   1.00 12.30  ? 227  ASN A O   1 
ATOM   1580 C CB  . ASN A  1 200 ? -63.460 -22.233 4.574   1.00 12.51  ? 227  ASN A CB  1 
ATOM   1581 C CG  . ASN A  1 200 ? -62.158 -21.466 4.622   1.00 11.92  ? 227  ASN A CG  1 
ATOM   1582 O OD1 . ASN A  1 200 ? -61.393 -21.460 3.656   1.00 13.27  ? 227  ASN A OD1 1 
ATOM   1583 N ND2 . ASN A  1 200 ? -61.895 -20.817 5.751   1.00 9.49   ? 227  ASN A ND2 1 
ATOM   1584 N N   . LEU A  1 201 ? -64.748 -24.949 2.801   1.00 11.68  ? 228  LEU A N   1 
ATOM   1585 C CA  . LEU A  1 201 ? -65.795 -25.964 2.821   1.00 12.02  ? 228  LEU A CA  1 
ATOM   1586 C C   . LEU A  1 201 ? -65.342 -27.247 3.502   1.00 12.60  ? 228  LEU A C   1 
ATOM   1587 O O   . LEU A  1 201 ? -65.812 -28.335 3.167   1.00 14.53  ? 228  LEU A O   1 
ATOM   1588 C CB  . LEU A  1 201 ? -66.268 -26.263 1.405   1.00 10.76  ? 228  LEU A CB  1 
ATOM   1589 C CG  . LEU A  1 201 ? -67.044 -25.100 0.807   1.00 10.45  ? 228  LEU A CG  1 
ATOM   1590 C CD1 . LEU A  1 201 ? -67.085 -25.228 -0.692  1.00 11.00  ? 228  LEU A CD1 1 
ATOM   1591 C CD2 . LEU A  1 201 ? -68.439 -25.090 1.391   1.00 10.07  ? 228  LEU A CD2 1 
ATOM   1592 N N   . TRP A  1 202 ? -64.435 -27.109 4.463   1.00 10.57  ? 229  TRP A N   1 
ATOM   1593 C CA  . TRP A  1 202 ? -63.936 -28.247 5.221   1.00 9.81   ? 229  TRP A CA  1 
ATOM   1594 C C   . TRP A  1 202 ? -65.016 -28.872 6.105   1.00 9.68   ? 229  TRP A C   1 
ATOM   1595 O O   . TRP A  1 202 ? -66.036 -28.247 6.383   1.00 9.25   ? 229  TRP A O   1 
ATOM   1596 C CB  . TRP A  1 202 ? -62.731 -27.826 6.062   1.00 8.26   ? 229  TRP A CB  1 
ATOM   1597 C CG  . TRP A  1 202 ? -62.972 -26.612 6.902   1.00 7.73   ? 229  TRP A CG  1 
ATOM   1598 C CD1 . TRP A  1 202 ? -62.905 -25.311 6.499   1.00 9.07   ? 229  TRP A CD1 1 
ATOM   1599 C CD2 . TRP A  1 202 ? -63.310 -26.584 8.293   1.00 7.20   ? 229  TRP A CD2 1 
ATOM   1600 N NE1 . TRP A  1 202 ? -63.184 -24.475 7.552   1.00 8.98   ? 229  TRP A NE1 1 
ATOM   1601 C CE2 . TRP A  1 202 ? -63.436 -25.233 8.664   1.00 7.13   ? 229  TRP A CE2 1 
ATOM   1602 C CE3 . TRP A  1 202 ? -63.517 -27.571 9.259   1.00 7.43   ? 229  TRP A CE3 1 
ATOM   1603 C CZ2 . TRP A  1 202 ? -63.763 -24.846 9.957   1.00 6.99   ? 229  TRP A CZ2 1 
ATOM   1604 C CZ3 . TRP A  1 202 ? -63.841 -27.185 10.539  1.00 7.28   ? 229  TRP A CZ3 1 
ATOM   1605 C CH2 . TRP A  1 202 ? -63.961 -25.834 10.878  1.00 8.14   ? 229  TRP A CH2 1 
ATOM   1606 N N   . SER A  1 203 ? -64.782 -30.108 6.536   1.00 9.02   ? 230  SER A N   1 
ATOM   1607 C CA  . SER A  1 203 ? -65.702 -30.819 7.424   1.00 10.76  ? 230  SER A CA  1 
ATOM   1608 C C   . SER A  1 203 ? -67.164 -30.794 6.962   1.00 16.17  ? 230  SER A C   1 
ATOM   1609 O O   . SER A  1 203 ? -68.062 -30.447 7.730   1.00 16.64  ? 230  SER A O   1 
ATOM   1610 C CB  . SER A  1 203 ? -65.586 -30.312 8.865   1.00 11.73  ? 230  SER A CB  1 
ATOM   1611 O OG  . SER A  1 203 ? -64.391 -30.763 9.476   1.00 8.02   ? 230  SER A OG  1 
ATOM   1612 N N   . ASN A  1 204 ? -67.391 -31.153 5.701   1.00 16.54  ? 231  ASN A N   1 
ATOM   1613 C CA  . ASN A  1 204 ? -68.741 -31.368 5.195   1.00 13.04  ? 231  ASN A CA  1 
ATOM   1614 C C   . ASN A  1 204 ? -68.907 -32.805 4.716   1.00 16.87  ? 231  ASN A C   1 
ATOM   1615 O O   . ASN A  1 204 ? -68.513 -33.743 5.405   1.00 20.14  ? 231  ASN A O   1 
ATOM   1616 C CB  . ASN A  1 204 ? -69.056 -30.395 4.067   1.00 9.45   ? 231  ASN A CB  1 
ATOM   1617 C CG  . ASN A  1 204 ? -69.354 -29.010 4.569   1.00 8.64   ? 231  ASN A CG  1 
ATOM   1618 O OD1 . ASN A  1 204 ? -70.424 -28.754 5.111   1.00 8.40   ? 231  ASN A OD1 1 
ATOM   1619 N ND2 . ASN A  1 204 ? -68.412 -28.101 4.385   1.00 10.26  ? 231  ASN A ND2 1 
ATOM   1620 N N   . GLN A  1 205 ? -69.487 -32.971 3.531   1.00 18.34  ? 232  GLN A N   1 
ATOM   1621 C CA  . GLN A  1 205 ? -69.626 -34.285 2.906   1.00 15.48  ? 232  GLN A CA  1 
ATOM   1622 C C   . GLN A  1 205 ? -69.402 -34.184 1.397   1.00 16.70  ? 232  GLN A C   1 
ATOM   1623 O O   . GLN A  1 205 ? -69.754 -35.096 0.652   1.00 20.90  ? 232  GLN A O   1 
ATOM   1624 C CB  . GLN A  1 205 ? -71.013 -34.869 3.173   1.00 14.77  ? 232  GLN A CB  1 
ATOM   1625 C CG  . GLN A  1 205 ? -71.399 -34.956 4.633   1.00 17.42  ? 232  GLN A CG  1 
ATOM   1626 C CD  . GLN A  1 205 ? -72.761 -35.575 4.824   1.00 25.29  ? 232  GLN A CD  1 
ATOM   1627 O OE1 . GLN A  1 205 ? -73.401 -35.400 5.861   1.00 25.86  ? 232  GLN A OE1 1 
ATOM   1628 N NE2 . GLN A  1 205 ? -73.216 -36.311 3.816   1.00 25.91  ? 232  GLN A NE2 1 
ATOM   1629 N N   . LEU A  1 206 ? -68.808 -33.078 0.956   1.00 13.78  ? 233  LEU A N   1 
ATOM   1630 C CA  . LEU A  1 206 ? -68.650 -32.776 -0.466  1.00 12.73  ? 233  LEU A CA  1 
ATOM   1631 C C   . LEU A  1 206 ? -67.954 -33.858 -1.291  1.00 12.83  ? 233  LEU A C   1 
ATOM   1632 O O   . LEU A  1 206 ? -66.927 -33.597 -1.913  1.00 12.36  ? 233  LEU A O   1 
ATOM   1633 C CB  . LEU A  1 206 ? -67.893 -31.464 -0.634  1.00 10.80  ? 233  LEU A CB  1 
ATOM   1634 C CG  . LEU A  1 206 ? -68.574 -30.216 -0.085  1.00 12.15  ? 233  LEU A CG  1 
ATOM   1635 C CD1 . LEU A  1 206 ? -67.780 -28.987 -0.489  1.00 14.03  ? 233  LEU A CD1 1 
ATOM   1636 C CD2 . LEU A  1 206 ? -70.000 -30.124 -0.587  1.00 11.78  ? 233  LEU A CD2 1 
ATOM   1637 N N   . HIS A  1 207 ? -68.535 -35.053 -1.322  1.00 12.54  ? 234  HIS A N   1 
ATOM   1638 C CA  . HIS A  1 207 ? -67.924 -36.192 -1.994  1.00 15.88  ? 234  HIS A CA  1 
ATOM   1639 C C   . HIS A  1 207 ? -67.655 -35.961 -3.471  1.00 23.46  ? 234  HIS A C   1 
ATOM   1640 O O   . HIS A  1 207 ? -66.557 -35.549 -3.859  1.00 22.93  ? 234  HIS A O   1 
ATOM   1641 C CB  . HIS A  1 207 ? -68.784 -37.436 -1.823  1.00 16.39  ? 234  HIS A CB  1 
ATOM   1642 C CG  . HIS A  1 207 ? -68.706 -38.033 -0.456  1.00 21.13  ? 234  HIS A CG  1 
ATOM   1643 N ND1 . HIS A  1 207 ? -68.608 -37.265 0.685   1.00 22.84  ? 234  HIS A ND1 1 
ATOM   1644 C CD2 . HIS A  1 207 ? -68.707 -39.322 -0.043  1.00 28.98  ? 234  HIS A CD2 1 
ATOM   1645 C CE1 . HIS A  1 207 ? -68.554 -38.056 1.743   1.00 28.41  ? 234  HIS A CE1 1 
ATOM   1646 N NE2 . HIS A  1 207 ? -68.613 -39.309 1.328   1.00 38.75  ? 234  HIS A NE2 1 
ATOM   1647 N N   . ASN A  1 208 ? -68.660 -36.237 -4.292  1.00 26.02  ? 235  ASN A N   1 
ATOM   1648 C CA  . ASN A  1 208 ? -68.487 -36.189 -5.736  1.00 28.12  ? 235  ASN A CA  1 
ATOM   1649 C C   . ASN A  1 208 ? -68.544 -34.772 -6.293  1.00 19.71  ? 235  ASN A C   1 
ATOM   1650 O O   . ASN A  1 208 ? -69.497 -34.407 -6.971  1.00 33.13  ? 235  ASN A O   1 
ATOM   1651 C CB  . ASN A  1 208 ? -69.538 -37.059 -6.432  1.00 42.44  ? 235  ASN A CB  1 
ATOM   1652 C CG  . ASN A  1 208 ? -69.747 -38.395 -5.742  1.00 41.67  ? 235  ASN A CG  1 
ATOM   1653 O OD1 . ASN A  1 208 ? -70.848 -38.695 -5.273  1.00 41.56  ? 235  ASN A OD1 1 
ATOM   1654 N ND2 . ASN A  1 208 ? -68.697 -39.212 -5.691  1.00 41.66  ? 235  ASN A ND2 1 
ATOM   1655 N N   . LEU A  1 209 ? -67.531 -33.967 -6.006  1.00 15.70  ? 236  LEU A N   1 
ATOM   1656 C CA  . LEU A  1 209 ? -67.428 -32.673 -6.655  1.00 17.89  ? 236  LEU A CA  1 
ATOM   1657 C C   . LEU A  1 209 ? -67.038 -32.931 -8.092  1.00 22.55  ? 236  LEU A C   1 
ATOM   1658 O O   . LEU A  1 209 ? -66.583 -34.027 -8.421  1.00 24.33  ? 236  LEU A O   1 
ATOM   1659 C CB  . LEU A  1 209 ? -66.369 -31.794 -5.991  1.00 19.17  ? 236  LEU A CB  1 
ATOM   1660 C CG  . LEU A  1 209 ? -66.627 -31.298 -4.569  1.00 14.64  ? 236  LEU A CG  1 
ATOM   1661 C CD1 . LEU A  1 209 ? -66.011 -29.935 -4.407  1.00 7.76   ? 236  LEU A CD1 1 
ATOM   1662 C CD2 . LEU A  1 209 ? -68.115 -31.256 -4.259  1.00 19.45  ? 236  LEU A CD2 1 
ATOM   1663 N N   . THR A  1 210 ? -67.209 -31.931 -8.950  1.00 25.59  ? 237  THR A N   1 
ATOM   1664 C CA  . THR A  1 210 ? -66.825 -32.079 -10.346 1.00 22.09  ? 237  THR A CA  1 
ATOM   1665 C C   . THR A  1 210 ? -66.645 -30.739 -11.057 1.00 20.41  ? 237  THR A C   1 
ATOM   1666 O O   . THR A  1 210 ? -67.218 -29.731 -10.641 1.00 18.02  ? 237  THR A O   1 
ATOM   1667 C CB  . THR A  1 210 ? -67.835 -32.936 -11.103 1.00 18.79  ? 237  THR A CB  1 
ATOM   1668 O OG1 . THR A  1 210 ? -67.262 -33.353 -12.349 1.00 30.53  ? 237  THR A OG1 1 
ATOM   1669 C CG2 . THR A  1 210 ? -69.115 -32.151 -11.344 1.00 25.96  ? 237  THR A CG2 1 
ATOM   1670 N N   . LYS A  1 211 ? -65.844 -30.760 -12.127 1.00 18.57  ? 238  LYS A N   1 
ATOM   1671 C CA  . LYS A  1 211 ? -65.483 -29.587 -12.938 1.00 17.89  ? 238  LYS A CA  1 
ATOM   1672 C C   . LYS A  1 211 ? -66.583 -28.545 -13.078 1.00 22.52  ? 238  LYS A C   1 
ATOM   1673 O O   . LYS A  1 211 ? -66.314 -27.345 -13.153 1.00 21.76  ? 238  LYS A O   1 
ATOM   1674 C CB  . LYS A  1 211 ? -65.024 -30.042 -14.330 1.00 20.06  ? 238  LYS A CB  1 
ATOM   1675 C CG  . LYS A  1 211 ? -64.969 -28.950 -15.403 1.00 18.57  ? 238  LYS A CG  1 
ATOM   1676 C CD  . LYS A  1 211 ? -64.332 -29.477 -16.693 1.00 17.82  ? 238  LYS A CD  1 
ATOM   1677 C CE  . LYS A  1 211 ? -64.596 -28.568 -17.896 1.00 21.29  ? 238  LYS A CE  1 
ATOM   1678 N NZ  . LYS A  1 211 ? -63.670 -27.401 -18.023 1.00 14.75  1 238  LYS A NZ  1 
ATOM   1679 N N   . HIS A  1 212 ? -67.825 -29.015 -13.100 1.00 29.06  ? 239  HIS A N   1 
ATOM   1680 C CA  . HIS A  1 212 ? -68.974 -28.136 -13.226 1.00 32.09  ? 239  HIS A CA  1 
ATOM   1681 C C   . HIS A  1 212 ? -69.215 -27.344 -11.945 1.00 31.07  ? 239  HIS A C   1 
ATOM   1682 O O   . HIS A  1 212 ? -69.721 -26.225 -11.991 1.00 35.57  ? 239  HIS A O   1 
ATOM   1683 C CB  . HIS A  1 212 ? -70.223 -28.943 -13.590 1.00 39.83  ? 239  HIS A CB  1 
ATOM   1684 C CG  . HIS A  1 212 ? -71.353 -28.103 -14.102 1.00 54.98  ? 239  HIS A CG  1 
ATOM   1685 N ND1 . HIS A  1 212 ? -72.617 -28.607 -14.319 1.00 57.78  ? 239  HIS A ND1 1 
ATOM   1686 C CD2 . HIS A  1 212 ? -71.406 -26.794 -14.444 1.00 46.32  ? 239  HIS A CD2 1 
ATOM   1687 C CE1 . HIS A  1 212 ? -73.402 -27.643 -14.766 1.00 57.68  ? 239  HIS A CE1 1 
ATOM   1688 N NE2 . HIS A  1 212 ? -72.691 -26.533 -14.851 1.00 45.40  ? 239  HIS A NE2 1 
ATOM   1689 N N   . ASP A  1 213 ? -68.837 -27.916 -10.806 1.00 30.71  ? 240  ASP A N   1 
ATOM   1690 C CA  . ASP A  1 213 ? -69.115 -27.289 -9.513  1.00 25.59  ? 240  ASP A CA  1 
ATOM   1691 C C   . ASP A  1 213 ? -68.370 -25.974 -9.266  1.00 19.65  ? 240  ASP A C   1 
ATOM   1692 O O   . ASP A  1 213 ? -68.678 -25.256 -8.320  1.00 17.49  ? 240  ASP A O   1 
ATOM   1693 C CB  . ASP A  1 213 ? -68.869 -28.271 -8.363  1.00 20.38  ? 240  ASP A CB  1 
ATOM   1694 C CG  . ASP A  1 213 ? -70.020 -29.244 -8.173  1.00 29.43  ? 240  ASP A CG  1 
ATOM   1695 O OD1 . ASP A  1 213 ? -71.108 -28.990 -8.733  1.00 39.47  ? 240  ASP A OD1 1 
ATOM   1696 O OD2 . ASP A  1 213 ? -69.848 -30.255 -7.458  1.00 27.09  1 240  ASP A OD2 1 
ATOM   1697 N N   . PHE A  1 214 ? -67.409 -25.645 -10.120 1.00 19.32  ? 241  PHE A N   1 
ATOM   1698 C CA  . PHE A  1 214 ? -66.610 -24.444 -9.905  1.00 19.47  ? 241  PHE A CA  1 
ATOM   1699 C C   . PHE A  1 214 ? -66.638 -23.472 -11.072 1.00 23.76  ? 241  PHE A C   1 
ATOM   1700 O O   . PHE A  1 214 ? -65.826 -22.551 -11.146 1.00 20.78  ? 241  PHE A O   1 
ATOM   1701 C CB  . PHE A  1 214 ? -65.178 -24.830 -9.549  1.00 17.04  ? 241  PHE A CB  1 
ATOM   1702 C CG  . PHE A  1 214 ? -65.080 -25.567 -8.261  1.00 15.26  ? 241  PHE A CG  1 
ATOM   1703 C CD1 . PHE A  1 214 ? -65.051 -24.878 -7.060  1.00 12.70  ? 241  PHE A CD1 1 
ATOM   1704 C CD2 . PHE A  1 214 ? -65.063 -26.948 -8.239  1.00 15.85  ? 241  PHE A CD2 1 
ATOM   1705 C CE1 . PHE A  1 214 ? -64.985 -25.549 -5.864  1.00 9.79   ? 241  PHE A CE1 1 
ATOM   1706 C CE2 . PHE A  1 214 ? -64.994 -27.628 -7.041  1.00 16.26  ? 241  PHE A CE2 1 
ATOM   1707 C CZ  . PHE A  1 214 ? -64.957 -26.925 -5.852  1.00 11.55  ? 241  PHE A CZ  1 
ATOM   1708 N N   . GLU A  1 215 ? -67.595 -23.677 -11.970 1.00 26.38  ? 242  GLU A N   1 
ATOM   1709 C CA  . GLU A  1 215 ? -67.751 -22.837 -13.148 1.00 26.02  ? 242  GLU A CA  1 
ATOM   1710 C C   . GLU A  1 215 ? -68.047 -21.387 -12.782 1.00 18.11  ? 242  GLU A C   1 
ATOM   1711 O O   . GLU A  1 215 ? -69.079 -21.090 -12.196 1.00 17.88  ? 242  GLU A O   1 
ATOM   1712 C CB  . GLU A  1 215 ? -68.875 -23.391 -14.021 1.00 34.77  ? 242  GLU A CB  1 
ATOM   1713 C CG  . GLU A  1 215 ? -68.768 -23.032 -15.490 1.00 46.19  ? 242  GLU A CG  1 
ATOM   1714 C CD  . GLU A  1 215 ? -69.980 -23.481 -16.279 1.00 52.17  ? 242  GLU A CD  1 
ATOM   1715 O OE1 . GLU A  1 215 ? -69.797 -24.048 -17.379 1.00 58.37  ? 242  GLU A OE1 1 
ATOM   1716 O OE2 . GLU A  1 215 ? -71.115 -23.265 -15.795 1.00 47.64  1 242  GLU A OE2 1 
ATOM   1717 N N   . GLY A  1 216 ? -67.137 -20.488 -13.134 1.00 15.35  ? 243  GLY A N   1 
ATOM   1718 C CA  . GLY A  1 216 ? -67.330 -19.079 -12.855 1.00 16.25  ? 243  GLY A CA  1 
ATOM   1719 C C   . GLY A  1 216 ? -66.525 -18.610 -11.661 1.00 23.03  ? 243  GLY A C   1 
ATOM   1720 O O   . GLY A  1 216 ? -66.528 -17.425 -11.320 1.00 22.85  ? 243  GLY A O   1 
ATOM   1721 N N   . ALA A  1 217 ? -65.827 -19.546 -11.023 1.00 27.79  ? 244  ALA A N   1 
ATOM   1722 C CA  . ALA A  1 217 ? -64.996 -19.230 -9.863  1.00 25.03  ? 244  ALA A CA  1 
ATOM   1723 C C   . ALA A  1 217 ? -63.567 -18.837 -10.256 1.00 23.18  ? 244  ALA A C   1 
ATOM   1724 O O   . ALA A  1 217 ? -62.594 -19.401 -9.748  1.00 21.78  ? 244  ALA A O   1 
ATOM   1725 C CB  . ALA A  1 217 ? -64.980 -20.402 -8.882  1.00 17.54  ? 244  ALA A CB  1 
ATOM   1726 N N   . THR A  1 218 ? -63.443 -17.872 -11.161 1.00 20.58  ? 245  THR A N   1 
ATOM   1727 C CA  . THR A  1 218 ? -62.130 -17.366 -11.534 1.00 21.69  ? 245  THR A CA  1 
ATOM   1728 C C   . THR A  1 218 ? -61.780 -16.191 -10.639 1.00 20.53  ? 245  THR A C   1 
ATOM   1729 O O   . THR A  1 218 ? -60.783 -15.508 -10.848 1.00 26.94  ? 245  THR A O   1 
ATOM   1730 C CB  . THR A  1 218 ? -62.075 -16.915 -12.998 1.00 24.00  ? 245  THR A CB  1 
ATOM   1731 O OG1 . THR A  1 218 ? -62.890 -15.749 -13.169 1.00 28.71  ? 245  THR A OG1 1 
ATOM   1732 C CG2 . THR A  1 218 ? -62.557 -18.032 -13.919 1.00 25.91  ? 245  THR A CG2 1 
ATOM   1733 N N   . SER A  1 219 ? -62.623 -15.955 -9.645  1.00 19.07  ? 246  SER A N   1 
ATOM   1734 C CA  . SER A  1 219 ? -62.366 -14.933 -8.645  1.00 17.42  ? 246  SER A CA  1 
ATOM   1735 C C   . SER A  1 219 ? -61.711 -15.584 -7.436  1.00 14.14  ? 246  SER A C   1 
ATOM   1736 O O   . SER A  1 219 ? -61.010 -14.928 -6.675  1.00 12.98  ? 246  SER A O   1 
ATOM   1737 C CB  . SER A  1 219 ? -63.681 -14.238 -8.256  1.00 21.11  ? 246  SER A CB  1 
ATOM   1738 O OG  . SER A  1 219 ? -63.776 -14.000 -6.858  1.00 14.49  ? 246  SER A OG  1 
ATOM   1739 N N   . VAL A  1 220 ? -61.930 -16.889 -7.292  1.00 15.18  ? 247  VAL A N   1 
ATOM   1740 C CA  . VAL A  1 220 ? -61.511 -17.652 -6.116  1.00 12.65  ? 247  VAL A CA  1 
ATOM   1741 C C   . VAL A  1 220 ? -60.003 -17.924 -6.048  1.00 16.00  ? 247  VAL A C   1 
ATOM   1742 O O   . VAL A  1 220 ? -59.392 -18.403 -7.008  1.00 16.90  ? 247  VAL A O   1 
ATOM   1743 C CB  . VAL A  1 220 ? -62.285 -18.988 -6.027  1.00 11.17  ? 247  VAL A CB  1 
ATOM   1744 C CG1 . VAL A  1 220 ? -61.704 -19.882 -4.954  1.00 10.77  ? 247  VAL A CG1 1 
ATOM   1745 C CG2 . VAL A  1 220 ? -63.752 -18.728 -5.765  1.00 11.38  ? 247  VAL A CG2 1 
ATOM   1746 N N   . LEU A  1 221 ? -59.418 -17.613 -4.894  1.00 14.33  ? 248  LEU A N   1 
ATOM   1747 C CA  . LEU A  1 221 ? -57.997 -17.797 -4.656  1.00 11.08  ? 248  LEU A CA  1 
ATOM   1748 C C   . LEU A  1 221 ? -57.754 -19.025 -3.799  1.00 13.96  ? 248  LEU A C   1 
ATOM   1749 O O   . LEU A  1 221 ? -56.944 -19.874 -4.147  1.00 15.67  ? 248  LEU A O   1 
ATOM   1750 C CB  . LEU A  1 221 ? -57.432 -16.575 -3.946  1.00 9.18   ? 248  LEU A CB  1 
ATOM   1751 C CG  . LEU A  1 221 ? -57.558 -15.284 -4.740  1.00 8.25   ? 248  LEU A CG  1 
ATOM   1752 C CD1 . LEU A  1 221 ? -57.021 -14.124 -3.936  1.00 9.08   ? 248  LEU A CD1 1 
ATOM   1753 C CD2 . LEU A  1 221 ? -56.833 -15.413 -6.072  1.00 6.98   ? 248  LEU A CD2 1 
ATOM   1754 N N   . GLY A  1 222 ? -58.454 -19.110 -2.671  1.00 14.26  ? 249  GLY A N   1 
ATOM   1755 C CA  . GLY A  1 222 ? -58.294 -20.227 -1.756  1.00 12.15  ? 249  GLY A CA  1 
ATOM   1756 C C   . GLY A  1 222 ? -59.537 -21.083 -1.582  1.00 10.26  ? 249  GLY A C   1 
ATOM   1757 O O   . GLY A  1 222 ? -60.616 -20.581 -1.273  1.00 10.13  ? 249  GLY A O   1 
ATOM   1758 N N   . ILE A  1 223 ? -59.381 -22.386 -1.780  1.00 8.36   ? 250  ILE A N   1 
ATOM   1759 C CA  . ILE A  1 223 ? -60.478 -23.323 -1.578  1.00 8.15   ? 250  ILE A CA  1 
ATOM   1760 C C   . ILE A  1 223 ? -60.067 -24.474 -0.663  1.00 10.04  ? 250  ILE A C   1 
ATOM   1761 O O   . ILE A  1 223 ? -59.204 -25.280 -1.007  1.00 11.11  ? 250  ILE A O   1 
ATOM   1762 C CB  . ILE A  1 223 ? -60.970 -23.894 -2.909  1.00 8.55   ? 250  ILE A CB  1 
ATOM   1763 C CG1 . ILE A  1 223 ? -61.822 -25.143 -2.664  1.00 9.58   ? 250  ILE A CG1 1 
ATOM   1764 C CG2 . ILE A  1 223 ? -59.792 -24.201 -3.814  1.00 9.01   ? 250  ILE A CG2 1 
ATOM   1765 C CD1 . ILE A  1 223 ? -61.889 -26.093 -3.846  1.00 11.22  ? 250  ILE A CD1 1 
ATOM   1766 N N   . ASP A  1 224 ? -60.682 -24.547 0.511   1.00 10.20  ? 251  ASP A N   1 
ATOM   1767 C CA  . ASP A  1 224 ? -60.372 -25.611 1.454   1.00 8.63   ? 251  ASP A CA  1 
ATOM   1768 C C   . ASP A  1 224 ? -61.481 -26.650 1.427   1.00 8.81   ? 251  ASP A C   1 
ATOM   1769 O O   . ASP A  1 224 ? -62.648 -26.325 1.636   1.00 9.71   ? 251  ASP A O   1 
ATOM   1770 C CB  . ASP A  1 224 ? -60.209 -25.043 2.866   1.00 8.81   ? 251  ASP A CB  1 
ATOM   1771 C CG  . ASP A  1 224 ? -59.603 -26.044 3.838   1.00 9.09   ? 251  ASP A CG  1 
ATOM   1772 O OD1 . ASP A  1 224 ? -59.698 -27.265 3.589   1.00 8.32   ? 251  ASP A OD1 1 
ATOM   1773 O OD2 . ASP A  1 224 ? -59.030 -25.611 4.863   1.00 10.26  1 251  ASP A OD2 1 
ATOM   1774 N N   . ILE A  1 225 ? -61.116 -27.900 1.166   1.00 7.64   ? 252  ILE A N   1 
ATOM   1775 C CA  . ILE A  1 225 ? -62.086 -28.992 1.200   1.00 9.52   ? 252  ILE A CA  1 
ATOM   1776 C C   . ILE A  1 225 ? -61.594 -30.146 2.076   1.00 9.52   ? 252  ILE A C   1 
ATOM   1777 O O   . ILE A  1 225 ? -61.959 -31.306 1.864   1.00 9.15   ? 252  ILE A O   1 
ATOM   1778 C CB  . ILE A  1 225 ? -62.456 -29.515 -0.228  1.00 9.53   ? 252  ILE A CB  1 
ATOM   1779 C CG1 . ILE A  1 225 ? -61.231 -30.087 -0.946  1.00 8.22   ? 252  ILE A CG1 1 
ATOM   1780 C CG2 . ILE A  1 225 ? -63.120 -28.423 -1.063  1.00 6.59   ? 252  ILE A CG2 1 
ATOM   1781 C CD1 . ILE A  1 225 ? -61.507 -30.532 -2.353  1.00 5.68   ? 252  ILE A CD1 1 
ATOM   1782 N N   . HIS A  1 226 ? -60.765 -29.827 3.065   1.00 10.31  ? 253  HIS A N   1 
ATOM   1783 C CA  . HIS A  1 226 ? -60.212 -30.869 3.924   1.00 10.32  ? 253  HIS A CA  1 
ATOM   1784 C C   . HIS A  1 226 ? -61.297 -31.470 4.803   1.00 11.03  ? 253  HIS A C   1 
ATOM   1785 O O   . HIS A  1 226 ? -62.358 -30.870 4.966   1.00 11.21  ? 253  HIS A O   1 
ATOM   1786 C CB  . HIS A  1 226 ? -59.015 -30.368 4.746   1.00 8.75   ? 253  HIS A CB  1 
ATOM   1787 C CG  . HIS A  1 226 ? -59.383 -29.592 5.973   1.00 7.84   ? 253  HIS A CG  1 
ATOM   1788 N ND1 . HIS A  1 226 ? -59.296 -28.219 6.036   1.00 7.47   ? 253  HIS A ND1 1 
ATOM   1789 C CD2 . HIS A  1 226 ? -59.796 -30.000 7.196   1.00 8.73   ? 253  HIS A CD2 1 
ATOM   1790 C CE1 . HIS A  1 226 ? -59.656 -27.812 7.240   1.00 8.79   ? 253  HIS A CE1 1 
ATOM   1791 N NE2 . HIS A  1 226 ? -59.969 -28.873 7.962   1.00 9.11   ? 253  HIS A NE2 1 
ATOM   1792 N N   . ASP A  1 227 ? -61.033 -32.654 5.351   1.00 10.77  ? 254  ASP A N   1 
ATOM   1793 C CA  . ASP A  1 227 ? -62.042 -33.401 6.099   1.00 10.47  ? 254  ASP A CA  1 
ATOM   1794 C C   . ASP A  1 227 ? -63.315 -33.489 5.279   1.00 13.51  ? 254  ASP A C   1 
ATOM   1795 O O   . ASP A  1 227 ? -64.327 -32.905 5.645   1.00 16.98  ? 254  ASP A O   1 
ATOM   1796 C CB  . ASP A  1 227 ? -62.336 -32.730 7.445   1.00 11.20  ? 254  ASP A CB  1 
ATOM   1797 C CG  . ASP A  1 227 ? -63.361 -33.487 8.264   1.00 10.39  ? 254  ASP A CG  1 
ATOM   1798 O OD1 . ASP A  1 227 ? -63.409 -34.728 8.149   1.00 10.95  ? 254  ASP A OD1 1 
ATOM   1799 O OD2 . ASP A  1 227 ? -64.123 -32.840 9.012   1.00 9.87   1 254  ASP A OD2 1 
ATOM   1800 N N   . ASN A  1 228 ? -63.256 -34.180 4.144   1.00 17.22  ? 255  ASN A N   1 
ATOM   1801 C CA  . ASN A  1 228 ? -64.428 -34.304 3.277   1.00 17.04  ? 255  ASN A CA  1 
ATOM   1802 C C   . ASN A  1 228 ? -64.553 -35.668 2.608   1.00 19.85  ? 255  ASN A C   1 
ATOM   1803 O O   . ASN A  1 228 ? -65.107 -35.787 1.513   1.00 16.74  ? 255  ASN A O   1 
ATOM   1804 C CB  . ASN A  1 228 ? -64.461 -33.189 2.232   1.00 11.13  ? 255  ASN A CB  1 
ATOM   1805 C CG  . ASN A  1 228 ? -65.484 -32.123 2.559   1.00 11.72  ? 255  ASN A CG  1 
ATOM   1806 O OD1 . ASN A  1 228 ? -66.563 -32.421 3.057   1.00 10.88  ? 255  ASN A OD1 1 
ATOM   1807 N ND2 . ASN A  1 228 ? -65.147 -30.875 2.287   1.00 13.82  ? 255  ASN A ND2 1 
ATOM   1808 N N   . GLY A  1 229 ? -64.012 -36.690 3.267   1.00 21.97  ? 256  GLY A N   1 
ATOM   1809 C CA  . GLY A  1 229 ? -64.163 -38.070 2.835   1.00 21.47  ? 256  GLY A CA  1 
ATOM   1810 C C   . GLY A  1 229 ? -63.855 -38.384 1.382   1.00 19.93  ? 256  GLY A C   1 
ATOM   1811 O O   . GLY A  1 229 ? -64.018 -39.522 0.955   1.00 25.91  ? 256  GLY A O   1 
ATOM   1812 N N   . ILE A  1 230 ? -63.415 -37.378 0.633   1.00 14.76  ? 257  ILE A N   1 
ATOM   1813 C CA  . ILE A  1 230 ? -63.095 -37.513 -0.780  1.00 12.90  ? 257  ILE A CA  1 
ATOM   1814 C C   . ILE A  1 230 ? -62.191 -38.712 -1.089  1.00 17.35  ? 257  ILE A C   1 
ATOM   1815 O O   . ILE A  1 230 ? -61.007 -38.730 -0.750  1.00 15.82  ? 257  ILE A O   1 
ATOM   1816 C CB  . ILE A  1 230 ? -62.454 -36.227 -1.301  1.00 12.78  ? 257  ILE A CB  1 
ATOM   1817 C CG1 . ILE A  1 230 ? -63.409 -35.057 -1.086  1.00 10.36  ? 257  ILE A CG1 1 
ATOM   1818 C CG2 . ILE A  1 230 ? -62.072 -36.368 -2.767  1.00 16.09  ? 257  ILE A CG2 1 
ATOM   1819 C CD1 . ILE A  1 230 ? -62.779 -33.717 -1.324  1.00 11.03  ? 257  ILE A CD1 1 
ATOM   1820 N N   . GLU A  1 231 ? -62.781 -39.711 -1.735  1.00 18.89  ? 258  GLU A N   1 
ATOM   1821 C CA  . GLU A  1 231 ? -62.089 -40.932 -2.104  1.00 14.19  ? 258  GLU A CA  1 
ATOM   1822 C C   . GLU A  1 231 ? -61.246 -40.720 -3.355  1.00 19.84  ? 258  GLU A C   1 
ATOM   1823 O O   . GLU A  1 231 ? -60.175 -41.305 -3.485  1.00 29.67  ? 258  GLU A O   1 
ATOM   1824 C CB  . GLU A  1 231 ? -63.101 -42.048 -2.342  1.00 12.33  ? 258  GLU A CB  1 
ATOM   1825 C CG  . GLU A  1 231 ? -62.796 -43.325 -1.604  1.00 14.58  ? 258  GLU A CG  1 
ATOM   1826 C CD  . GLU A  1 231 ? -64.000 -43.857 -0.878  1.00 15.24  ? 258  GLU A CD  1 
ATOM   1827 O OE1 . GLU A  1 231 ? -63.849 -44.792 -0.061  1.00 14.96  ? 258  GLU A OE1 1 
ATOM   1828 O OE2 . GLU A  1 231 ? -65.102 -43.330 -1.122  1.00 19.42  1 258  GLU A OE2 1 
ATOM   1829 N N   . GLN A  1 232 ? -61.734 -39.888 -4.273  1.00 19.92  ? 259  GLN A N   1 
ATOM   1830 C CA  . GLN A  1 232 ? -60.994 -39.555 -5.492  1.00 23.52  ? 259  GLN A CA  1 
ATOM   1831 C C   . GLN A  1 232 ? -61.618 -38.383 -6.258  1.00 22.98  ? 259  GLN A C   1 
ATOM   1832 O O   . GLN A  1 232 ? -62.833 -38.187 -6.231  1.00 23.41  ? 259  GLN A O   1 
ATOM   1833 C CB  . GLN A  1 232 ? -60.860 -40.777 -6.403  1.00 23.18  ? 259  GLN A CB  1 
ATOM   1834 C CG  . GLN A  1 232 ? -62.180 -41.409 -6.797  1.00 32.38  ? 259  GLN A CG  1 
ATOM   1835 C CD  . GLN A  1 232 ? -61.993 -42.685 -7.596  1.00 49.57  ? 259  GLN A CD  1 
ATOM   1836 O OE1 . GLN A  1 232 ? -61.030 -43.425 -7.386  1.00 55.57  ? 259  GLN A OE1 1 
ATOM   1837 N NE2 . GLN A  1 232 ? -62.910 -42.945 -8.523  1.00 52.68  ? 259  GLN A NE2 1 
ATOM   1838 N N   . LEU A  1 233 ? -60.773 -37.610 -6.935  1.00 19.26  ? 260  LEU A N   1 
ATOM   1839 C CA  . LEU A  1 233 ? -61.216 -36.430 -7.664  1.00 16.69  ? 260  LEU A CA  1 
ATOM   1840 C C   . LEU A  1 233 ? -61.028 -36.603 -9.159  1.00 22.09  ? 260  LEU A C   1 
ATOM   1841 O O   . LEU A  1 233 ? -60.024 -37.165 -9.603  1.00 18.90  ? 260  LEU A O   1 
ATOM   1842 C CB  . LEU A  1 233 ? -60.437 -35.186 -7.224  1.00 17.31  ? 260  LEU A CB  1 
ATOM   1843 C CG  . LEU A  1 233 ? -60.646 -34.562 -5.843  1.00 15.05  ? 260  LEU A CG  1 
ATOM   1844 C CD1 . LEU A  1 233 ? -59.726 -33.369 -5.698  1.00 14.88  ? 260  LEU A CD1 1 
ATOM   1845 C CD2 . LEU A  1 233 ? -62.082 -34.135 -5.642  1.00 15.83  ? 260  LEU A CD2 1 
ATOM   1846 N N   . PRO A  1 234 ? -62.012 -36.131 -9.942  1.00 28.24  ? 261  PRO A N   1 
ATOM   1847 C CA  . PRO A  1 234 ? -61.857 -35.955 -11.388 1.00 25.13  ? 261  PRO A CA  1 
ATOM   1848 C C   . PRO A  1 234 ? -60.690 -35.022 -11.706 1.00 24.71  ? 261  PRO A C   1 
ATOM   1849 O O   . PRO A  1 234 ? -60.492 -34.024 -11.018 1.00 26.71  ? 261  PRO A O   1 
ATOM   1850 C CB  . PRO A  1 234 ? -63.180 -35.310 -11.791 1.00 22.33  ? 261  PRO A CB  1 
ATOM   1851 C CG  . PRO A  1 234 ? -64.161 -35.881 -10.825 1.00 19.96  ? 261  PRO A CG  1 
ATOM   1852 C CD  . PRO A  1 234 ? -63.420 -35.999 -9.522  1.00 21.10  ? 261  PRO A CD  1 
ATOM   1853 N N   . HIS A  1 235 ? -59.935 -35.341 -12.751 1.00 23.27  ? 262  HIS A N   1 
ATOM   1854 C CA  . HIS A  1 235 ? -58.726 -34.596 -13.096 1.00 24.09  ? 262  HIS A CA  1 
ATOM   1855 C C   . HIS A  1 235 ? -58.962 -33.160 -13.571 1.00 23.62  ? 262  HIS A C   1 
ATOM   1856 O O   . HIS A  1 235 ? -58.048 -32.513 -14.089 1.00 21.88  ? 262  HIS A O   1 
ATOM   1857 C CB  . HIS A  1 235 ? -57.976 -35.341 -14.191 1.00 26.40  ? 262  HIS A CB  1 
ATOM   1858 C CG  . HIS A  1 235 ? -58.653 -35.281 -15.523 1.00 20.82  ? 262  HIS A CG  1 
ATOM   1859 N ND1 . HIS A  1 235 ? -58.606 -34.167 -16.332 1.00 20.30  ? 262  HIS A ND1 1 
ATOM   1860 C CD2 . HIS A  1 235 ? -59.399 -36.196 -16.184 1.00 18.27  ? 262  HIS A CD2 1 
ATOM   1861 C CE1 . HIS A  1 235 ? -59.289 -34.400 -17.437 1.00 22.00  ? 262  HIS A CE1 1 
ATOM   1862 N NE2 . HIS A  1 235 ? -59.779 -35.624 -17.373 1.00 20.81  ? 262  HIS A NE2 1 
ATOM   1863 N N   . ASP A  1 236 ? -60.182 -32.666 -13.426 1.00 23.41  ? 263  ASP A N   1 
ATOM   1864 C CA  . ASP A  1 236 ? -60.496 -31.327 -13.896 1.00 23.63  ? 263  ASP A CA  1 
ATOM   1865 C C   . ASP A  1 236 ? -61.370 -30.588 -12.900 1.00 23.92  ? 263  ASP A C   1 
ATOM   1866 O O   . ASP A  1 236 ? -61.930 -29.543 -13.223 1.00 21.31  ? 263  ASP A O   1 
ATOM   1867 C CB  . ASP A  1 236 ? -61.186 -31.387 -15.258 1.00 23.03  ? 263  ASP A CB  1 
ATOM   1868 C CG  . ASP A  1 236 ? -62.194 -32.514 -15.348 1.00 24.84  ? 263  ASP A CG  1 
ATOM   1869 O OD1 . ASP A  1 236 ? -62.491 -33.126 -14.300 1.00 23.46  ? 263  ASP A OD1 1 
ATOM   1870 O OD2 . ASP A  1 236 ? -62.693 -32.786 -16.463 1.00 27.07  1 263  ASP A OD2 1 
ATOM   1871 N N   . VAL A  1 237 ? -61.482 -31.137 -11.693 1.00 25.88  ? 264  VAL A N   1 
ATOM   1872 C CA  . VAL A  1 237 ? -62.308 -30.542 -10.646 1.00 22.71  ? 264  VAL A CA  1 
ATOM   1873 C C   . VAL A  1 237 ? -61.987 -29.069 -10.487 1.00 21.15  ? 264  VAL A C   1 
ATOM   1874 O O   . VAL A  1 237 ? -62.882 -28.235 -10.331 1.00 18.95  ? 264  VAL A O   1 
ATOM   1875 C CB  . VAL A  1 237 ? -62.091 -31.233 -9.291  1.00 22.24  ? 264  VAL A CB  1 
ATOM   1876 C CG1 . VAL A  1 237 ? -62.739 -30.431 -8.180  1.00 23.07  ? 264  VAL A CG1 1 
ATOM   1877 C CG2 . VAL A  1 237 ? -62.660 -32.629 -9.317  1.00 23.51  ? 264  VAL A CG2 1 
ATOM   1878 N N   . PHE A  1 238 ? -60.698 -28.758 -10.568 1.00 22.08  ? 265  PHE A N   1 
ATOM   1879 C CA  . PHE A  1 238 ? -60.221 -27.399 -10.367 1.00 21.32  ? 265  PHE A CA  1 
ATOM   1880 C C   . PHE A  1 238 ? -60.053 -26.648 -11.684 1.00 18.18  ? 265  PHE A C   1 
ATOM   1881 O O   . PHE A  1 238 ? -59.580 -25.514 -11.686 1.00 16.23  ? 265  PHE A O   1 
ATOM   1882 C CB  . PHE A  1 238 ? -58.889 -27.420 -9.612  1.00 19.19  ? 265  PHE A CB  1 
ATOM   1883 C CG  . PHE A  1 238 ? -58.894 -28.299 -8.388  1.00 20.80  ? 265  PHE A CG  1 
ATOM   1884 C CD1 . PHE A  1 238 ? -59.977 -28.304 -7.520  1.00 17.60  ? 265  PHE A CD1 1 
ATOM   1885 C CD2 . PHE A  1 238 ? -57.814 -29.129 -8.109  1.00 19.39  ? 265  PHE A CD2 1 
ATOM   1886 C CE1 . PHE A  1 238 ? -59.980 -29.118 -6.397  1.00 18.86  ? 265  PHE A CE1 1 
ATOM   1887 C CE2 . PHE A  1 238 ? -57.811 -29.946 -6.990  1.00 14.27  ? 265  PHE A CE2 1 
ATOM   1888 C CZ  . PHE A  1 238 ? -58.895 -29.941 -6.133  1.00 15.23  ? 265  PHE A CZ  1 
ATOM   1889 N N   . ALA A  1 239 ? -60.454 -27.270 -12.794 1.00 17.06  ? 266  ALA A N   1 
ATOM   1890 C CA  . ALA A  1 239 ? -60.164 -26.732 -14.127 1.00 19.05  ? 266  ALA A CA  1 
ATOM   1891 C C   . ALA A  1 239 ? -60.722 -25.333 -14.361 1.00 16.01  ? 266  ALA A C   1 
ATOM   1892 O O   . ALA A  1 239 ? -60.212 -24.585 -15.197 1.00 14.73  ? 266  ALA A O   1 
ATOM   1893 C CB  . ALA A  1 239 ? -60.641 -27.684 -15.213 1.00 17.66  ? 266  ALA A CB  1 
ATOM   1894 N N   . HIS A  1 240 ? -61.765 -24.988 -13.617 1.00 14.76  ? 267  HIS A N   1 
ATOM   1895 C CA  . HIS A  1 240 ? -62.356 -23.662 -13.700 1.00 18.67  ? 267  HIS A CA  1 
ATOM   1896 C C   . HIS A  1 240 ? -61.716 -22.720 -12.684 1.00 17.47  ? 267  HIS A C   1 
ATOM   1897 O O   . HIS A  1 240 ? -61.877 -21.501 -12.759 1.00 18.69  ? 267  HIS A O   1 
ATOM   1898 C CB  . HIS A  1 240 ? -63.874 -23.733 -13.493 1.00 21.96  ? 267  HIS A CB  1 
ATOM   1899 C CG  . HIS A  1 240 ? -64.625 -24.237 -14.688 1.00 22.24  ? 267  HIS A CG  1 
ATOM   1900 N ND1 . HIS A  1 240 ? -64.152 -24.102 -15.975 1.00 21.84  ? 267  HIS A ND1 1 
ATOM   1901 C CD2 . HIS A  1 240 ? -65.811 -24.882 -14.789 1.00 24.05  ? 267  HIS A CD2 1 
ATOM   1902 C CE1 . HIS A  1 240 ? -65.016 -24.638 -16.818 1.00 23.99  ? 267  HIS A CE1 1 
ATOM   1903 N NE2 . HIS A  1 240 ? -66.034 -25.114 -16.124 1.00 27.29  ? 267  HIS A NE2 1 
ATOM   1904 N N   . LEU A  1 241 ? -60.988 -23.293 -11.734 1.00 17.98  ? 268  LEU A N   1 
ATOM   1905 C CA  . LEU A  1 241 ? -60.307 -22.507 -10.713 1.00 21.06  ? 268  LEU A CA  1 
ATOM   1906 C C   . LEU A  1 241 ? -58.951 -22.038 -11.232 1.00 20.55  ? 268  LEU A C   1 
ATOM   1907 O O   . LEU A  1 241 ? -57.914 -22.478 -10.738 1.00 20.15  ? 268  LEU A O   1 
ATOM   1908 C CB  . LEU A  1 241 ? -60.111 -23.349 -9.448  1.00 18.56  ? 268  LEU A CB  1 
ATOM   1909 C CG  . LEU A  1 241 ? -61.352 -23.774 -8.659  1.00 15.28  ? 268  LEU A CG  1 
ATOM   1910 C CD1 . LEU A  1 241 ? -61.017 -24.869 -7.652  1.00 12.95  ? 268  LEU A CD1 1 
ATOM   1911 C CD2 . LEU A  1 241 ? -61.947 -22.573 -7.953  1.00 15.58  ? 268  LEU A CD2 1 
ATOM   1912 N N   . THR A  1 242 ? -58.952 -21.145 -12.218 1.00 18.16  ? 269  THR A N   1 
ATOM   1913 C CA  . THR A  1 242 ? -57.711 -20.820 -12.923 1.00 23.10  ? 269  THR A CA  1 
ATOM   1914 C C   . THR A  1 242 ? -56.692 -19.988 -12.127 1.00 25.97  ? 269  THR A C   1 
ATOM   1915 O O   . THR A  1 242 ? -55.483 -20.133 -12.327 1.00 26.59  ? 269  THR A O   1 
ATOM   1916 C CB  . THR A  1 242 ? -57.970 -20.193 -14.316 1.00 20.18  ? 269  THR A CB  1 
ATOM   1917 O OG1 . THR A  1 242 ? -58.647 -18.941 -14.172 1.00 22.38  ? 269  THR A OG1 1 
ATOM   1918 C CG2 . THR A  1 242 ? -58.801 -21.132 -15.176 1.00 15.19  ? 269  THR A CG2 1 
ATOM   1919 N N   . ASN A  1 243 ? -57.166 -19.131 -11.228 1.00 20.03  ? 270  ASN A N   1 
ATOM   1920 C CA  . ASN A  1 243 ? -56.253 -18.317 -10.431 1.00 21.70  ? 270  ASN A CA  1 
ATOM   1921 C C   . ASN A  1 243 ? -56.236 -18.729 -8.963  1.00 24.44  ? 270  ASN A C   1 
ATOM   1922 O O   . ASN A  1 243 ? -55.976 -17.911 -8.076  1.00 23.02  ? 270  ASN A O   1 
ATOM   1923 C CB  . ASN A  1 243 ? -56.597 -16.840 -10.578 1.00 20.60  ? 270  ASN A CB  1 
ATOM   1924 C CG  . ASN A  1 243 ? -57.409 -16.577 -11.804 1.00 22.88  ? 270  ASN A CG  1 
ATOM   1925 O OD1 . ASN A  1 243 ? -58.237 -17.398 -12.177 1.00 27.97  ? 270  ASN A OD1 1 
ATOM   1926 N ND2 . ASN A  1 243 ? -57.170 -15.451 -12.458 1.00 27.56  ? 270  ASN A ND2 1 
ATOM   1927 N N   . VAL A  1 244 ? -56.513 -20.006 -8.716  1.00 22.32  ? 271  VAL A N   1 
ATOM   1928 C CA  . VAL A  1 244 ? -56.509 -20.544 -7.362  1.00 17.67  ? 271  VAL A CA  1 
ATOM   1929 C C   . VAL A  1 244 ? -55.060 -20.608 -6.869  1.00 17.97  ? 271  VAL A C   1 
ATOM   1930 O O   . VAL A  1 244 ? -54.140 -20.861 -7.651  1.00 18.64  ? 271  VAL A O   1 
ATOM   1931 C CB  . VAL A  1 244 ? -57.210 -21.936 -7.301  1.00 13.89  ? 271  VAL A CB  1 
ATOM   1932 C CG1 . VAL A  1 244 ? -56.373 -23.003 -7.979  1.00 15.81  ? 271  VAL A CG1 1 
ATOM   1933 C CG2 . VAL A  1 244 ? -57.508 -22.336 -5.875  1.00 11.48  ? 271  VAL A CG2 1 
ATOM   1934 N N   . THR A  1 245 ? -54.853 -20.343 -5.582  1.00 14.46  ? 272  THR A N   1 
ATOM   1935 C CA  . THR A  1 245 ? -53.510 -20.325 -5.023  1.00 10.67  ? 272  THR A CA  1 
ATOM   1936 C C   . THR A  1 245 ? -53.362 -21.189 -3.769  1.00 11.56  ? 272  THR A C   1 
ATOM   1937 O O   . THR A  1 245 ? -52.261 -21.595 -3.425  1.00 14.95  ? 272  THR A O   1 
ATOM   1938 C CB  . THR A  1 245 ? -53.054 -18.894 -4.699  1.00 10.99  ? 272  THR A CB  1 
ATOM   1939 O OG1 . THR A  1 245 ? -53.899 -18.339 -3.688  1.00 11.68  ? 272  THR A OG1 1 
ATOM   1940 C CG2 . THR A  1 245 ? -53.116 -18.022 -5.934  1.00 11.63  ? 272  THR A CG2 1 
ATOM   1941 N N   . ASP A  1 246 ? -54.455 -21.468 -3.072  1.00 11.95  ? 273  ASP A N   1 
ATOM   1942 C CA  . ASP A  1 246 ? -54.369 -22.337 -1.900  1.00 11.23  ? 273  ASP A CA  1 
ATOM   1943 C C   . ASP A  1 246 ? -55.415 -23.446 -1.924  1.00 10.50  ? 273  ASP A C   1 
ATOM   1944 O O   . ASP A  1 246 ? -56.601 -23.202 -1.723  1.00 10.98  ? 273  ASP A O   1 
ATOM   1945 C CB  . ASP A  1 246 ? -54.508 -21.529 -0.611  1.00 12.44  ? 273  ASP A CB  1 
ATOM   1946 C CG  . ASP A  1 246 ? -53.959 -20.128 -0.746  1.00 21.58  ? 273  ASP A CG  1 
ATOM   1947 O OD1 . ASP A  1 246 ? -52.766 -19.991 -1.100  1.00 18.60  ? 273  ASP A OD1 1 
ATOM   1948 O OD2 . ASP A  1 246 ? -54.731 -19.166 -0.516  1.00 28.43  1 273  ASP A OD2 1 
ATOM   1949 N N   . ILE A  1 247 ? -54.968 -24.669 -2.174  1.00 7.91   ? 274  ILE A N   1 
ATOM   1950 C CA  . ILE A  1 247 ? -55.850 -25.816 -2.108  1.00 6.62   ? 274  ILE A CA  1 
ATOM   1951 C C   . ILE A  1 247 ? -55.567 -26.568 -0.816  1.00 7.51   ? 274  ILE A C   1 
ATOM   1952 O O   . ILE A  1 247 ? -54.507 -26.412 -0.220  1.00 8.97   ? 274  ILE A O   1 
ATOM   1953 C CB  . ILE A  1 247 ? -55.642 -26.728 -3.318  1.00 6.34   ? 274  ILE A CB  1 
ATOM   1954 C CG1 . ILE A  1 247 ? -55.365 -25.873 -4.556  1.00 9.14   ? 274  ILE A CG1 1 
ATOM   1955 C CG2 . ILE A  1 247 ? -56.845 -27.625 -3.525  1.00 6.79   ? 274  ILE A CG2 1 
ATOM   1956 C CD1 . ILE A  1 247 ? -56.011 -26.376 -5.836  1.00 11.41  ? 274  ILE A CD1 1 
ATOM   1957 N N   . ASN A  1 248 ? -56.519 -27.372 -0.370  1.00 7.88   ? 275  ASN A N   1 
ATOM   1958 C CA  . ASN A  1 248 ? -56.334 -28.147 0.843   1.00 7.32   ? 275  ASN A CA  1 
ATOM   1959 C C   . ASN A  1 248 ? -57.178 -29.411 0.791   1.00 6.42   ? 275  ASN A C   1 
ATOM   1960 O O   . ASN A  1 248 ? -58.381 -29.378 1.028   1.00 6.74   ? 275  ASN A O   1 
ATOM   1961 C CB  . ASN A  1 248 ? -56.685 -27.302 2.064   1.00 7.50   ? 275  ASN A CB  1 
ATOM   1962 C CG  . ASN A  1 248 ? -56.261 -27.946 3.358   1.00 7.07   ? 275  ASN A CG  1 
ATOM   1963 O OD1 . ASN A  1 248 ? -56.102 -29.163 3.433   1.00 6.72   ? 275  ASN A OD1 1 
ATOM   1964 N ND2 . ASN A  1 248 ? -56.079 -27.133 4.392   1.00 7.61   ? 275  ASN A ND2 1 
ATOM   1965 N N   . LEU A  1 249 ? -56.533 -30.523 0.476   1.00 5.71   ? 276  LEU A N   1 
ATOM   1966 C CA  . LEU A  1 249 ? -57.228 -31.780 0.251   1.00 7.29   ? 276  LEU A CA  1 
ATOM   1967 C C   . LEU A  1 249 ? -56.992 -32.722 1.423   1.00 8.17   ? 276  LEU A C   1 
ATOM   1968 O O   . LEU A  1 249 ? -56.908 -33.939 1.254   1.00 8.85   ? 276  LEU A O   1 
ATOM   1969 C CB  . LEU A  1 249 ? -56.720 -32.415 -1.044  1.00 6.09   ? 276  LEU A CB  1 
ATOM   1970 C CG  . LEU A  1 249 ? -56.513 -31.396 -2.162  1.00 4.69   ? 276  LEU A CG  1 
ATOM   1971 C CD1 . LEU A  1 249 ? -55.738 -31.977 -3.328  1.00 3.68   ? 276  LEU A CD1 1 
ATOM   1972 C CD2 . LEU A  1 249 ? -57.861 -30.888 -2.613  1.00 7.88   ? 276  LEU A CD2 1 
ATOM   1973 N N   . SER A  1 250 ? -56.892 -32.154 2.617   1.00 7.48   ? 277  SER A N   1 
ATOM   1974 C CA  . SER A  1 250 ? -56.445 -32.923 3.771   1.00 7.96   ? 277  SER A CA  1 
ATOM   1975 C C   . SER A  1 250 ? -57.548 -33.725 4.457   1.00 9.75   ? 277  SER A C   1 
ATOM   1976 O O   . SER A  1 250 ? -58.736 -33.520 4.213   1.00 9.52   ? 277  SER A O   1 
ATOM   1977 C CB  . SER A  1 250 ? -55.769 -31.998 4.777   1.00 6.45   ? 277  SER A CB  1 
ATOM   1978 O OG  . SER A  1 250 ? -54.838 -31.165 4.118   1.00 6.68   ? 277  SER A OG  1 
ATOM   1979 N N   . ALA A  1 251 ? -57.129 -34.650 5.311   1.00 10.01  ? 278  ALA A N   1 
ATOM   1980 C CA  . ALA A  1 251 ? -58.039 -35.436 6.141   1.00 9.83   ? 278  ALA A CA  1 
ATOM   1981 C C   . ALA A  1 251 ? -59.029 -36.257 5.327   1.00 9.53   ? 278  ALA A C   1 
ATOM   1982 O O   . ALA A  1 251 ? -60.010 -36.759 5.866   1.00 10.71  ? 278  ALA A O   1 
ATOM   1983 C CB  . ALA A  1 251 ? -58.763 -34.548 7.159   1.00 7.52   ? 278  ALA A CB  1 
ATOM   1984 N N   . ASN A  1 252 ? -58.756 -36.409 4.034   1.00 9.57   ? 279  ASN A N   1 
ATOM   1985 C CA  . ASN A  1 252 ? -59.651 -37.145 3.151   1.00 12.42  ? 279  ASN A CA  1 
ATOM   1986 C C   . ASN A  1 252 ? -59.326 -38.636 3.092   1.00 14.26  ? 279  ASN A C   1 
ATOM   1987 O O   . ASN A  1 252 ? -58.838 -39.209 4.063   1.00 12.21  ? 279  ASN A O   1 
ATOM   1988 C CB  . ASN A  1 252 ? -59.664 -36.533 1.746   1.00 13.22  ? 279  ASN A CB  1 
ATOM   1989 C CG  . ASN A  1 252 ? -60.357 -35.174 1.699   1.00 11.53  ? 279  ASN A CG  1 
ATOM   1990 O OD1 . ASN A  1 252 ? -61.401 -34.971 2.314   1.00 10.58  ? 279  ASN A OD1 1 
ATOM   1991 N ND2 . ASN A  1 252 ? -59.771 -34.240 0.964   1.00 10.41  ? 279  ASN A ND2 1 
ATOM   1992 N N   . LEU A  1 253 ? -59.610 -39.263 1.955   1.00 21.41  ? 280  LEU A N   1 
ATOM   1993 C CA  . LEU A  1 253 ? -59.492 -40.717 1.828   1.00 22.03  ? 280  LEU A CA  1 
ATOM   1994 C C   . LEU A  1 253 ? -58.870 -41.165 0.507   1.00 19.56  ? 280  LEU A C   1 
ATOM   1995 O O   . LEU A  1 253 ? -59.150 -42.267 0.035   1.00 20.60  ? 280  LEU A O   1 
ATOM   1996 C CB  . LEU A  1 253 ? -60.867 -41.388 1.967   1.00 21.79  ? 280  LEU A CB  1 
ATOM   1997 C CG  . LEU A  1 253 ? -61.449 -41.731 3.341   1.00 19.43  ? 280  LEU A CG  1 
ATOM   1998 C CD1 . LEU A  1 253 ? -61.944 -40.499 4.058   1.00 20.25  ? 280  LEU A CD1 1 
ATOM   1999 C CD2 . LEU A  1 253 ? -62.577 -42.730 3.190   1.00 21.65  ? 280  LEU A CD2 1 
ATOM   2000 N N   . PHE A  1 254 ? -58.035 -40.320 -0.086  1.00 16.32  ? 281  PHE A N   1 
ATOM   2001 C CA  . PHE A  1 254 ? -57.419 -40.636 -1.370  1.00 18.05  ? 281  PHE A CA  1 
ATOM   2002 C C   . PHE A  1 254 ? -56.604 -41.922 -1.327  1.00 21.97  ? 281  PHE A C   1 
ATOM   2003 O O   . PHE A  1 254 ? -55.808 -42.130 -0.411  1.00 22.63  ? 281  PHE A O   1 
ATOM   2004 C CB  . PHE A  1 254 ? -56.512 -39.493 -1.820  1.00 19.96  ? 281  PHE A CB  1 
ATOM   2005 C CG  . PHE A  1 254 ? -57.238 -38.212 -2.102  1.00 20.28  ? 281  PHE A CG  1 
ATOM   2006 C CD1 . PHE A  1 254 ? -57.467 -37.296 -1.093  1.00 17.50  ? 281  PHE A CD1 1 
ATOM   2007 C CD2 . PHE A  1 254 ? -57.683 -37.919 -3.380  1.00 21.84  ? 281  PHE A CD2 1 
ATOM   2008 C CE1 . PHE A  1 254 ? -58.128 -36.112 -1.352  1.00 16.30  ? 281  PHE A CE1 1 
ATOM   2009 C CE2 . PHE A  1 254 ? -58.344 -36.739 -3.645  1.00 20.83  ? 281  PHE A CE2 1 
ATOM   2010 C CZ  . PHE A  1 254 ? -58.566 -35.835 -2.630  1.00 19.52  ? 281  PHE A CZ  1 
ATOM   2011 N N   . ARG A  1 255 ? -56.812 -42.785 -2.317  1.00 23.45  ? 282  ARG A N   1 
ATOM   2012 C CA  . ARG A  1 255 ? -55.937 -43.935 -2.531  1.00 26.13  ? 282  ARG A CA  1 
ATOM   2013 C C   . ARG A  1 255 ? -55.036 -43.624 -3.714  1.00 23.77  ? 282  ARG A C   1 
ATOM   2014 O O   . ARG A  1 255 ? -53.947 -44.188 -3.855  1.00 24.35  ? 282  ARG A O   1 
ATOM   2015 C CB  . ARG A  1 255 ? -56.741 -45.206 -2.809  1.00 24.20  ? 282  ARG A CB  1 
ATOM   2016 C CG  . ARG A  1 255 ? -57.326 -45.866 -1.574  1.00 29.84  ? 282  ARG A CG  1 
ATOM   2017 C CD  . ARG A  1 255 ? -56.566 -47.132 -1.201  1.00 32.54  ? 282  ARG A CD  1 
ATOM   2018 N NE  . ARG A  1 255 ? -57.323 -47.944 -0.254  1.00 42.32  ? 282  ARG A NE  1 
ATOM   2019 C CZ  . ARG A  1 255 ? -57.482 -47.635 1.029   1.00 49.86  ? 282  ARG A CZ  1 
ATOM   2020 N NH1 . ARG A  1 255 ? -56.933 -46.531 1.517   1.00 38.56  1 282  ARG A NH1 1 
ATOM   2021 N NH2 . ARG A  1 255 ? -58.189 -48.427 1.825   1.00 59.93  ? 282  ARG A NH2 1 
ATOM   2022 N N   . SER A  1 256 ? -55.507 -42.710 -4.555  1.00 17.11  ? 283  SER A N   1 
ATOM   2023 C CA  . SER A  1 256 ? -54.763 -42.272 -5.723  1.00 16.83  ? 283  SER A CA  1 
ATOM   2024 C C   . SER A  1 256 ? -55.266 -40.916 -6.188  1.00 18.67  ? 283  SER A C   1 
ATOM   2025 O O   . SER A  1 256 ? -56.303 -40.439 -5.736  1.00 21.50  ? 283  SER A O   1 
ATOM   2026 C CB  . SER A  1 256 ? -54.880 -43.297 -6.849  1.00 19.05  ? 283  SER A CB  1 
ATOM   2027 O OG  . SER A  1 256 ? -56.222 -43.704 -7.026  1.00 20.40  ? 283  SER A OG  1 
ATOM   2028 N N   . LEU A  1 257 ? -54.507 -40.287 -7.078  1.00 20.37  ? 284  LEU A N   1 
ATOM   2029 C CA  . LEU A  1 257 ? -54.879 -39.003 -7.650  1.00 18.68  ? 284  LEU A CA  1 
ATOM   2030 C C   . LEU A  1 257 ? -54.630 -39.055 -9.145  1.00 25.08  ? 284  LEU A C   1 
ATOM   2031 O O   . LEU A  1 257 ? -53.684 -39.699 -9.596  1.00 31.57  ? 284  LEU A O   1 
ATOM   2032 C CB  . LEU A  1 257 ? -54.053 -37.869 -7.043  1.00 14.99  ? 284  LEU A CB  1 
ATOM   2033 C CG  . LEU A  1 257 ? -54.548 -37.143 -5.795  1.00 9.88   ? 284  LEU A CG  1 
ATOM   2034 C CD1 . LEU A  1 257 ? -54.525 -38.049 -4.593  1.00 12.33  ? 284  LEU A CD1 1 
ATOM   2035 C CD2 . LEU A  1 257 ? -53.674 -35.940 -5.545  1.00 8.77   ? 284  LEU A CD2 1 
ATOM   2036 N N   . PRO A  1 258 ? -55.479 -38.378 -9.925  1.00 24.58  ? 285  PRO A N   1 
ATOM   2037 C CA  . PRO A  1 258 ? -55.294 -38.362 -11.375 1.00 22.15  ? 285  PRO A CA  1 
ATOM   2038 C C   . PRO A  1 258 ? -54.208 -37.377 -11.768 1.00 21.77  ? 285  PRO A C   1 
ATOM   2039 O O   . PRO A  1 258 ? -54.054 -36.337 -11.124 1.00 18.21  ? 285  PRO A O   1 
ATOM   2040 C CB  . PRO A  1 258 ? -56.647 -37.874 -11.881 1.00 32.99  ? 285  PRO A CB  1 
ATOM   2041 C CG  . PRO A  1 258 ? -57.148 -36.990 -10.785 1.00 28.03  ? 285  PRO A CG  1 
ATOM   2042 C CD  . PRO A  1 258 ? -56.674 -37.623 -9.507  1.00 26.59  ? 285  PRO A CD  1 
ATOM   2043 N N   . GLN A  1 259 ? -53.457 -37.706 -12.812 1.00 24.49  ? 286  GLN A N   1 
ATOM   2044 C CA  . GLN A  1 259 ? -52.431 -36.803 -13.305 1.00 23.75  ? 286  GLN A CA  1 
ATOM   2045 C C   . GLN A  1 259 ? -53.088 -35.578 -13.940 1.00 22.13  ? 286  GLN A C   1 
ATOM   2046 O O   . GLN A  1 259 ? -54.249 -35.626 -14.340 1.00 20.52  ? 286  GLN A O   1 
ATOM   2047 C CB  . GLN A  1 259 ? -51.513 -37.511 -14.302 1.00 21.76  ? 286  GLN A CB  1 
ATOM   2048 C CG  . GLN A  1 259 ? -50.183 -36.802 -14.501 1.00 25.41  ? 286  GLN A CG  1 
ATOM   2049 C CD  . GLN A  1 259 ? -49.351 -37.412 -15.605 1.00 21.89  ? 286  GLN A CD  1 
ATOM   2050 O OE1 . GLN A  1 259 ? -49.617 -38.528 -16.054 1.00 17.60  ? 286  GLN A OE1 1 
ATOM   2051 N NE2 . GLN A  1 259 ? -48.336 -36.677 -16.055 1.00 21.28  ? 286  GLN A NE2 1 
ATOM   2052 N N   . GLY A  1 260 ? -52.346 -34.478 -14.014 1.00 23.37  ? 287  GLY A N   1 
ATOM   2053 C CA  . GLY A  1 260 ? -52.876 -33.239 -14.545 1.00 21.47  ? 287  GLY A CA  1 
ATOM   2054 C C   . GLY A  1 260 ? -53.867 -32.579 -13.604 1.00 22.81  ? 287  GLY A C   1 
ATOM   2055 O O   . GLY A  1 260 ? -54.547 -31.628 -13.990 1.00 27.57  ? 287  GLY A O   1 
ATOM   2056 N N   . LEU A  1 261 ? -53.944 -33.079 -12.372 1.00 18.37  ? 288  LEU A N   1 
ATOM   2057 C CA  . LEU A  1 261 ? -54.894 -32.579 -11.377 1.00 16.42  ? 288  LEU A CA  1 
ATOM   2058 C C   . LEU A  1 261 ? -54.813 -31.066 -11.168 1.00 17.37  ? 288  LEU A C   1 
ATOM   2059 O O   . LEU A  1 261 ? -55.836 -30.412 -10.942 1.00 15.92  ? 288  LEU A O   1 
ATOM   2060 C CB  . LEU A  1 261 ? -54.701 -33.304 -10.043 1.00 16.10  ? 288  LEU A CB  1 
ATOM   2061 C CG  . LEU A  1 261 ? -55.552 -32.821 -8.864  1.00 14.95  ? 288  LEU A CG  1 
ATOM   2062 C CD1 . LEU A  1 261 ? -57.016 -33.167 -9.055  1.00 19.33  ? 288  LEU A CD1 1 
ATOM   2063 C CD2 . LEU A  1 261 ? -55.040 -33.403 -7.565  1.00 13.42  ? 288  LEU A CD2 1 
ATOM   2064 N N   . PHE A  1 262 ? -53.603 -30.514 -11.253 1.00 17.29  ? 289  PHE A N   1 
ATOM   2065 C CA  . PHE A  1 262 ? -53.403 -29.074 -11.103 1.00 14.67  ? 289  PHE A CA  1 
ATOM   2066 C C   . PHE A  1 262 ? -52.912 -28.407 -12.381 1.00 19.16  ? 289  PHE A C   1 
ATOM   2067 O O   . PHE A  1 262 ? -52.499 -27.245 -12.356 1.00 16.16  ? 289  PHE A O   1 
ATOM   2068 C CB  . PHE A  1 262 ? -52.424 -28.777 -9.975  1.00 12.83  ? 289  PHE A CB  1 
ATOM   2069 C CG  . PHE A  1 262 ? -52.860 -29.299 -8.644  1.00 13.83  ? 289  PHE A CG  1 
ATOM   2070 C CD1 . PHE A  1 262 ? -53.834 -28.648 -7.916  1.00 12.76  ? 289  PHE A CD1 1 
ATOM   2071 C CD2 . PHE A  1 262 ? -52.287 -30.441 -8.114  1.00 14.50  ? 289  PHE A CD2 1 
ATOM   2072 C CE1 . PHE A  1 262 ? -54.232 -29.132 -6.690  1.00 14.00  ? 289  PHE A CE1 1 
ATOM   2073 C CE2 . PHE A  1 262 ? -52.681 -30.926 -6.885  1.00 11.36  ? 289  PHE A CE2 1 
ATOM   2074 C CZ  . PHE A  1 262 ? -53.652 -30.274 -6.173  1.00 12.89  ? 289  PHE A CZ  1 
ATOM   2075 N N   . ASP A  1 263 ? -52.970 -29.146 -13.488 1.00 23.75  ? 290  ASP A N   1 
ATOM   2076 C CA  . ASP A  1 263 ? -52.493 -28.679 -14.792 1.00 24.38  ? 290  ASP A CA  1 
ATOM   2077 C C   . ASP A  1 263 ? -53.031 -27.315 -15.226 1.00 27.79  ? 290  ASP A C   1 
ATOM   2078 O O   . ASP A  1 263 ? -52.315 -26.533 -15.850 1.00 25.11  ? 290  ASP A O   1 
ATOM   2079 C CB  . ASP A  1 263 ? -52.817 -29.710 -15.874 1.00 24.76  ? 290  ASP A CB  1 
ATOM   2080 C CG  . ASP A  1 263 ? -51.613 -30.530 -16.273 1.00 32.54  ? 290  ASP A CG  1 
ATOM   2081 O OD1 . ASP A  1 263 ? -50.811 -30.876 -15.382 1.00 40.59  ? 290  ASP A OD1 1 
ATOM   2082 O OD2 . ASP A  1 263 ? -51.460 -30.823 -17.478 1.00 36.27  1 290  ASP A OD2 1 
ATOM   2083 N N   . HIS A  1 264 ? -54.291 -27.038 -14.903 1.00 28.50  ? 291  HIS A N   1 
ATOM   2084 C CA  . HIS A  1 264 ? -54.938 -25.802 -15.337 1.00 26.52  ? 291  HIS A CA  1 
ATOM   2085 C C   . HIS A  1 264 ? -54.777 -24.658 -14.329 1.00 23.84  ? 291  HIS A C   1 
ATOM   2086 O O   . HIS A  1 264 ? -55.174 -23.520 -14.589 1.00 19.17  ? 291  HIS A O   1 
ATOM   2087 C CB  . HIS A  1 264 ? -56.415 -26.067 -15.630 1.00 25.07  ? 291  HIS A CB  1 
ATOM   2088 C CG  . HIS A  1 264 ? -56.642 -27.217 -16.560 1.00 32.49  ? 291  HIS A CG  1 
ATOM   2089 N ND1 . HIS A  1 264 ? -57.077 -28.451 -16.125 1.00 37.45  ? 291  HIS A ND1 1 
ATOM   2090 C CD2 . HIS A  1 264 ? -56.469 -27.330 -17.899 1.00 36.68  ? 291  HIS A CD2 1 
ATOM   2091 C CE1 . HIS A  1 264 ? -57.178 -29.269 -17.158 1.00 38.78  ? 291  HIS A CE1 1 
ATOM   2092 N NE2 . HIS A  1 264 ? -56.814 -28.614 -18.246 1.00 38.84  ? 291  HIS A NE2 1 
ATOM   2093 N N   . ASN A  1 265 ? -54.175 -24.967 -13.186 1.00 22.34  ? 292  ASN A N   1 
ATOM   2094 C CA  . ASN A  1 265 ? -53.979 -23.980 -12.133 1.00 22.12  ? 292  ASN A CA  1 
ATOM   2095 C C   . ASN A  1 265 ? -52.500 -23.684 -11.905 1.00 22.50  ? 292  ASN A C   1 
ATOM   2096 O O   . ASN A  1 265 ? -51.913 -24.091 -10.904 1.00 18.72  ? 292  ASN A O   1 
ATOM   2097 C CB  . ASN A  1 265 ? -54.617 -24.479 -10.847 1.00 18.45  ? 292  ASN A CB  1 
ATOM   2098 C CG  . ASN A  1 265 ? -55.640 -25.556 -11.102 1.00 17.68  ? 292  ASN A CG  1 
ATOM   2099 O OD1 . ASN A  1 265 ? -55.437 -26.713 -10.748 1.00 17.57  ? 292  ASN A OD1 1 
ATOM   2100 N ND2 . ASN A  1 265 ? -56.743 -25.185 -11.732 1.00 19.44  ? 292  ASN A ND2 1 
ATOM   2101 N N   . LYS A  1 266 ? -51.901 -22.968 -12.846 1.00 20.82  ? 293  LYS A N   1 
ATOM   2102 C CA  . LYS A  1 266 ? -50.497 -22.623 -12.755 1.00 17.37  ? 293  LYS A CA  1 
ATOM   2103 C C   . LYS A  1 266 ? -50.295 -21.308 -12.006 1.00 20.36  ? 293  LYS A C   1 
ATOM   2104 O O   . LYS A  1 266 ? -49.386 -20.539 -12.318 1.00 26.05  ? 293  LYS A O   1 
ATOM   2105 C CB  . LYS A  1 266 ? -49.879 -22.557 -14.151 1.00 19.65  ? 293  LYS A CB  1 
ATOM   2106 C CG  . LYS A  1 266 ? -49.922 -23.878 -14.906 1.00 21.11  ? 293  LYS A CG  1 
ATOM   2107 C CD  . LYS A  1 266 ? -49.289 -25.004 -14.097 1.00 19.16  ? 293  LYS A CD  1 
ATOM   2108 C CE  . LYS A  1 266 ? -49.251 -26.306 -14.881 1.00 21.63  ? 293  LYS A CE  1 
ATOM   2109 N NZ  . LYS A  1 266 ? -48.592 -26.125 -16.207 1.00 23.55  1 293  LYS A NZ  1 
ATOM   2110 N N   . HIS A  1 267 ? -51.147 -21.051 -11.020 1.00 16.64  ? 294  HIS A N   1 
ATOM   2111 C CA  . HIS A  1 267 ? -50.967 -19.906 -10.137 1.00 16.29  ? 294  HIS A CA  1 
ATOM   2112 C C   . HIS A  1 267 ? -50.864 -20.366 -8.691  1.00 18.09  ? 294  HIS A C   1 
ATOM   2113 O O   . HIS A  1 267 ? -50.850 -19.544 -7.772  1.00 17.48  ? 294  HIS A O   1 
ATOM   2114 C CB  . HIS A  1 267 ? -52.115 -18.912 -10.287 1.00 19.92  ? 294  HIS A CB  1 
ATOM   2115 C CG  . HIS A  1 267 ? -51.858 -17.841 -11.298 1.00 20.25  ? 294  HIS A CG  1 
ATOM   2116 N ND1 . HIS A  1 267 ? -51.889 -18.076 -12.656 1.00 20.94  ? 294  HIS A ND1 1 
ATOM   2117 C CD2 . HIS A  1 267 ? -51.564 -16.528 -11.149 1.00 20.66  ? 294  HIS A CD2 1 
ATOM   2118 C CE1 . HIS A  1 267 ? -51.624 -16.953 -13.300 1.00 24.70  ? 294  HIS A CE1 1 
ATOM   2119 N NE2 . HIS A  1 267 ? -51.422 -15.999 -12.408 1.00 25.77  ? 294  HIS A NE2 1 
ATOM   2120 N N   . LEU A  1 268 ? -50.793 -21.686 -8.507  1.00 20.13  ? 295  LEU A N   1 
ATOM   2121 C CA  . LEU A  1 268 ? -50.693 -22.310 -7.186  1.00 12.76  ? 295  LEU A CA  1 
ATOM   2122 C C   . LEU A  1 268 ? -49.569 -21.725 -6.351  1.00 12.10  ? 295  LEU A C   1 
ATOM   2123 O O   . LEU A  1 268 ? -48.497 -21.424 -6.858  1.00 15.13  ? 295  LEU A O   1 
ATOM   2124 C CB  . LEU A  1 268 ? -50.484 -23.819 -7.312  1.00 11.43  ? 295  LEU A CB  1 
ATOM   2125 C CG  . LEU A  1 268 ? -51.715 -24.653 -7.653  1.00 12.74  ? 295  LEU A CG  1 
ATOM   2126 C CD1 . LEU A  1 268 ? -51.361 -26.128 -7.713  1.00 9.58   ? 295  LEU A CD1 1 
ATOM   2127 C CD2 . LEU A  1 268 ? -52.814 -24.395 -6.637  1.00 11.85  ? 295  LEU A CD2 1 
ATOM   2128 N N   . ASN A  1 269 ? -49.829 -21.576 -5.062  1.00 12.67  ? 296  ASN A N   1 
ATOM   2129 C CA  . ASN A  1 269 ? -48.886 -20.965 -4.146  1.00 11.18  ? 296  ASN A CA  1 
ATOM   2130 C C   . ASN A  1 269 ? -48.635 -21.888 -2.967  1.00 11.46  ? 296  ASN A C   1 
ATOM   2131 O O   . ASN A  1 269 ? -47.641 -21.745 -2.259  1.00 14.24  ? 296  ASN A O   1 
ATOM   2132 C CB  . ASN A  1 269 ? -49.450 -19.642 -3.638  1.00 12.63  ? 296  ASN A CB  1 
ATOM   2133 C CG  . ASN A  1 269 ? -48.439 -18.525 -3.677  1.00 18.58  ? 296  ASN A CG  1 
ATOM   2134 O OD1 . ASN A  1 269 ? -47.498 -18.495 -2.879  1.00 16.92  ? 296  ASN A OD1 1 
ATOM   2135 N ND2 . ASN A  1 269 ? -48.634 -17.583 -4.601  1.00 20.71  ? 296  ASN A ND2 1 
ATOM   2136 N N   . GLU A  1 270 ? -49.549 -22.831 -2.762  1.00 8.60   ? 297  GLU A N   1 
ATOM   2137 C CA  . GLU A  1 270 ? -49.479 -23.748 -1.638  1.00 7.81   ? 297  GLU A CA  1 
ATOM   2138 C C   . GLU A  1 270 ? -50.586 -24.783 -1.728  1.00 8.01   ? 297  GLU A C   1 
ATOM   2139 O O   . GLU A  1 270 ? -51.762 -24.455 -1.637  1.00 9.53   ? 297  GLU A O   1 
ATOM   2140 C CB  . GLU A  1 270 ? -49.590 -22.987 -0.313  1.00 8.91   ? 297  GLU A CB  1 
ATOM   2141 C CG  . GLU A  1 270 ? -49.523 -23.857 0.934   1.00 9.75   ? 297  GLU A CG  1 
ATOM   2142 C CD  . GLU A  1 270 ? -49.682 -23.043 2.213   1.00 14.98  ? 297  GLU A CD  1 
ATOM   2143 O OE1 . GLU A  1 270 ? -49.734 -23.648 3.313   1.00 10.80  ? 297  GLU A OE1 1 
ATOM   2144 O OE2 . GLU A  1 270 ? -49.756 -21.793 2.112   1.00 12.67  1 297  GLU A OE2 1 
ATOM   2145 N N   . VAL A  1 271 ? -50.200 -26.034 -1.923  1.00 7.63   ? 298  VAL A N   1 
ATOM   2146 C CA  . VAL A  1 271 ? -51.122 -27.151 -1.832  1.00 6.28   ? 298  VAL A CA  1 
ATOM   2147 C C   . VAL A  1 271 ? -50.807 -27.887 -0.540  1.00 7.21   ? 298  VAL A C   1 
ATOM   2148 O O   . VAL A  1 271 ? -49.651 -27.948 -0.124  1.00 6.95   ? 298  VAL A O   1 
ATOM   2149 C CB  . VAL A  1 271 ? -50.932 -28.106 -3.009  1.00 5.48   ? 298  VAL A CB  1 
ATOM   2150 C CG1 . VAL A  1 271 ? -51.974 -29.206 -2.979  1.00 5.42   ? 298  VAL A CG1 1 
ATOM   2151 C CG2 . VAL A  1 271 ? -51.000 -27.342 -4.305  1.00 7.19   ? 298  VAL A CG2 1 
ATOM   2152 N N   . ARG A  1 272 ? -51.830 -28.422 0.116   1.00 7.48   ? 299  ARG A N   1 
ATOM   2153 C CA  . ARG A  1 272 ? -51.621 -29.219 1.321   1.00 7.25   ? 299  ARG A CA  1 
ATOM   2154 C C   . ARG A  1 272 ? -52.476 -30.484 1.276   1.00 7.20   ? 299  ARG A C   1 
ATOM   2155 O O   . ARG A  1 272 ? -53.692 -30.415 1.106   1.00 7.99   ? 299  ARG A O   1 
ATOM   2156 C CB  . ARG A  1 272 ? -51.916 -28.397 2.583   1.00 5.79   ? 299  ARG A CB  1 
ATOM   2157 C CG  . ARG A  1 272 ? -51.314 -26.997 2.551   1.00 6.82   ? 299  ARG A CG  1 
ATOM   2158 C CD  . ARG A  1 272 ? -51.224 -26.370 3.924   1.00 8.48   ? 299  ARG A CD  1 
ATOM   2159 N NE  . ARG A  1 272 ? -52.513 -26.345 4.604   1.00 16.39  ? 299  ARG A NE  1 
ATOM   2160 C CZ  . ARG A  1 272 ? -52.911 -25.370 5.418   1.00 19.76  ? 299  ARG A CZ  1 
ATOM   2161 N NH1 . ARG A  1 272 ? -52.117 -24.327 5.646   1.00 18.28  1 299  ARG A NH1 1 
ATOM   2162 N NH2 . ARG A  1 272 ? -54.107 -25.437 5.997   1.00 14.34  ? 299  ARG A NH2 1 
ATOM   2163 N N   . LEU A  1 273 ? -51.828 -31.637 1.407   1.00 6.58   ? 300  LEU A N   1 
ATOM   2164 C CA  . LEU A  1 273 ? -52.523 -32.917 1.442   1.00 5.93   ? 300  LEU A CA  1 
ATOM   2165 C C   . LEU A  1 273 ? -52.128 -33.642 2.723   1.00 5.18   ? 300  LEU A C   1 
ATOM   2166 O O   . LEU A  1 273 ? -51.597 -34.746 2.698   1.00 6.17   ? 300  LEU A O   1 
ATOM   2167 C CB  . LEU A  1 273 ? -52.160 -33.754 0.213   1.00 5.33   ? 300  LEU A CB  1 
ATOM   2168 C CG  . LEU A  1 273 ? -53.212 -34.675 -0.416  1.00 4.05   ? 300  LEU A CG  1 
ATOM   2169 C CD1 . LEU A  1 273 ? -52.657 -35.335 -1.667  1.00 3.55   ? 300  LEU A CD1 1 
ATOM   2170 C CD2 . LEU A  1 273 ? -53.693 -35.731 0.557   1.00 5.94   ? 300  LEU A CD2 1 
ATOM   2171 N N   . MET A  1 274 ? -52.388 -33.009 3.852   1.00 4.07   ? 301  MET A N   1 
ATOM   2172 C CA  . MET A  1 274 ? -51.953 -33.557 5.117   1.00 5.24   ? 301  MET A CA  1 
ATOM   2173 C C   . MET A  1 274 ? -52.914 -34.592 5.678   1.00 7.69   ? 301  MET A C   1 
ATOM   2174 O O   . MET A  1 274 ? -54.114 -34.534 5.435   1.00 8.75   ? 301  MET A O   1 
ATOM   2175 C CB  . MET A  1 274 ? -51.791 -32.432 6.128   1.00 5.70   ? 301  MET A CB  1 
ATOM   2176 C CG  . MET A  1 274 ? -50.677 -31.471 5.818   1.00 4.57   ? 301  MET A CG  1 
ATOM   2177 S SD  . MET A  1 274 ? -50.869 -30.028 6.864   1.00 2.47   ? 301  MET A SD  1 
ATOM   2178 C CE  . MET A  1 274 ? -52.310 -29.290 6.132   1.00 9.62   ? 301  MET A CE  1 
ATOM   2179 N N   . ASN A  1 275 ? -52.365 -35.545 6.425   1.00 9.07   ? 302  ASN A N   1 
ATOM   2180 C CA  . ASN A  1 275 ? -53.152 -36.437 7.275   1.00 9.62   ? 302  ASN A CA  1 
ATOM   2181 C C   . ASN A  1 275 ? -54.277 -37.238 6.616   1.00 9.67   ? 302  ASN A C   1 
ATOM   2182 O O   . ASN A  1 275 ? -55.350 -37.411 7.191   1.00 7.89   ? 302  ASN A O   1 
ATOM   2183 C CB  . ASN A  1 275 ? -53.683 -35.664 8.477   1.00 8.24   ? 302  ASN A CB  1 
ATOM   2184 C CG  . ASN A  1 275 ? -52.802 -35.817 9.676   1.00 11.26  ? 302  ASN A CG  1 
ATOM   2185 O OD1 . ASN A  1 275 ? -52.496 -36.936 10.090  1.00 10.21  ? 302  ASN A OD1 1 
ATOM   2186 N ND2 . ASN A  1 275 ? -52.357 -34.699 10.231  1.00 16.75  ? 302  ASN A ND2 1 
ATOM   2187 N N   . ASN A  1 276 ? -54.016 -37.740 5.420   1.00 8.81   ? 303  ASN A N   1 
ATOM   2188 C CA  . ASN A  1 276 ? -54.975 -38.580 4.726   1.00 9.60   ? 303  ASN A CA  1 
ATOM   2189 C C   . ASN A  1 276 ? -55.404 -39.783 5.557   1.00 11.01  ? 303  ASN A C   1 
ATOM   2190 O O   . ASN A  1 276 ? -54.594 -40.638 5.886   1.00 16.29  ? 303  ASN A O   1 
ATOM   2191 C CB  . ASN A  1 276 ? -54.383 -39.053 3.411   1.00 10.67  ? 303  ASN A CB  1 
ATOM   2192 C CG  . ASN A  1 276 ? -55.384 -39.033 2.297   1.00 17.33  ? 303  ASN A CG  1 
ATOM   2193 O OD1 . ASN A  1 276 ? -55.589 -40.037 1.615   1.00 21.11  ? 303  ASN A OD1 1 
ATOM   2194 N ND2 . ASN A  1 276 ? -56.037 -37.885 2.109   1.00 15.52  ? 303  ASN A ND2 1 
ATOM   2195 N N   . ARG A  1 277 ? -56.688 -39.852 5.877   1.00 13.56  ? 304  ARG A N   1 
ATOM   2196 C CA  . ARG A  1 277 ? -57.210 -40.889 6.763   1.00 13.06  ? 304  ARG A CA  1 
ATOM   2197 C C   . ARG A  1 277 ? -57.038 -42.323 6.239   1.00 14.01  ? 304  ARG A C   1 
ATOM   2198 O O   . ARG A  1 277 ? -57.325 -43.277 6.956   1.00 15.57  ? 304  ARG A O   1 
ATOM   2199 C CB  . ARG A  1 277 ? -58.673 -40.606 7.135   1.00 11.17  ? 304  ARG A CB  1 
ATOM   2200 C CG  . ARG A  1 277 ? -58.862 -39.695 8.359   1.00 12.96  ? 304  ARG A CG  1 
ATOM   2201 C CD  . ARG A  1 277 ? -58.199 -38.334 8.167   1.00 14.48  ? 304  ARG A CD  1 
ATOM   2202 N NE  . ARG A  1 277 ? -58.383 -37.416 9.293   1.00 17.53  ? 304  ARG A NE  1 
ATOM   2203 C CZ  . ARG A  1 277 ? -57.490 -37.221 10.261  1.00 15.66  ? 304  ARG A CZ  1 
ATOM   2204 N NH1 . ARG A  1 277 ? -56.343 -37.885 10.258  1.00 16.09  1 304  ARG A NH1 1 
ATOM   2205 N NH2 . ARG A  1 277 ? -57.744 -36.362 11.237  1.00 16.03  ? 304  ARG A NH2 1 
ATOM   2206 N N   . VAL A  1 278 ? -56.581 -42.475 4.998   1.00 15.74  ? 305  VAL A N   1 
ATOM   2207 C CA  . VAL A  1 278 ? -56.148 -43.786 4.495   1.00 22.72  ? 305  VAL A CA  1 
ATOM   2208 C C   . VAL A  1 278 ? -54.852 -43.674 3.676   1.00 22.53  ? 305  VAL A C   1 
ATOM   2209 O O   . VAL A  1 278 ? -54.615 -42.650 3.026   1.00 20.00  ? 305  VAL A O   1 
ATOM   2210 C CB  . VAL A  1 278 ? -57.241 -44.523 3.652   1.00 23.03  ? 305  VAL A CB  1 
ATOM   2211 C CG1 . VAL A  1 278 ? -58.428 -44.932 4.510   1.00 19.82  ? 305  VAL A CG1 1 
ATOM   2212 C CG2 . VAL A  1 278 ? -57.669 -43.692 2.464   1.00 24.94  ? 305  VAL A CG2 1 
ATOM   2213 N N   . PRO A  1 279 ? -54.009 -44.726 3.715   1.00 18.82  ? 306  PRO A N   1 
ATOM   2214 C CA  . PRO A  1 279 ? -52.717 -44.827 3.024   1.00 17.52  ? 306  PRO A CA  1 
ATOM   2215 C C   . PRO A  1 279 ? -52.731 -44.526 1.526   1.00 20.47  ? 306  PRO A C   1 
ATOM   2216 O O   . PRO A  1 279 ? -53.296 -45.300 0.749   1.00 23.27  ? 306  PRO A O   1 
ATOM   2217 C CB  . PRO A  1 279 ? -52.332 -46.297 3.233   1.00 20.07  ? 306  PRO A CB  1 
ATOM   2218 C CG  . PRO A  1 279 ? -53.579 -46.973 3.720   1.00 18.00  ? 306  PRO A CG  1 
ATOM   2219 C CD  . PRO A  1 279 ? -54.253 -45.929 4.524   1.00 18.09  ? 306  PRO A CD  1 
ATOM   2220 N N   . LEU A  1 280 ? -52.081 -43.429 1.140   1.00 17.33  ? 307  LEU A N   1 
ATOM   2221 C CA  . LEU A  1 280 ? -51.912 -43.054 -0.263  1.00 18.28  ? 307  LEU A CA  1 
ATOM   2222 C C   . LEU A  1 280 ? -50.481 -43.339 -0.737  1.00 23.43  ? 307  LEU A C   1 
ATOM   2223 O O   . LEU A  1 280 ? -49.546 -42.596 -0.421  1.00 23.54  ? 307  LEU A O   1 
ATOM   2224 C CB  . LEU A  1 280 ? -52.261 -41.578 -0.458  1.00 18.25  ? 307  LEU A CB  1 
ATOM   2225 C CG  . LEU A  1 280 ? -51.779 -40.878 -1.732  1.00 21.09  ? 307  LEU A CG  1 
ATOM   2226 C CD1 . LEU A  1 280 ? -52.352 -41.527 -2.976  1.00 20.73  ? 307  LEU A CD1 1 
ATOM   2227 C CD2 . LEU A  1 280 ? -52.124 -39.399 -1.690  1.00 20.86  ? 307  LEU A CD2 1 
ATOM   2228 N N   . ALA A  1 281 ? -50.334 -44.414 -1.510  1.00 26.23  ? 308  ALA A N   1 
ATOM   2229 C CA  . ALA A  1 281 ? -49.033 -44.968 -1.902  1.00 19.66  ? 308  ALA A CA  1 
ATOM   2230 C C   . ALA A  1 281 ? -48.046 -43.974 -2.503  1.00 20.08  ? 308  ALA A C   1 
ATOM   2231 O O   . ALA A  1 281 ? -46.891 -43.919 -2.091  1.00 21.53  ? 308  ALA A O   1 
ATOM   2232 C CB  . ALA A  1 281 ? -49.234 -46.128 -2.858  1.00 22.68  ? 308  ALA A CB  1 
ATOM   2233 N N   . THR A  1 282 ? -48.499 -43.207 -3.489  1.00 22.77  ? 309  THR A N   1 
ATOM   2234 C CA  . THR A  1 282 ? -47.627 -42.267 -4.189  1.00 26.85  ? 309  THR A CA  1 
ATOM   2235 C C   . THR A  1 282 ? -48.405 -41.187 -4.938  1.00 28.71  ? 309  THR A C   1 
ATOM   2236 O O   . THR A  1 282 ? -49.596 -41.336 -5.207  1.00 35.16  ? 309  THR A O   1 
ATOM   2237 C CB  . THR A  1 282 ? -46.704 -42.999 -5.186  1.00 26.51  ? 309  THR A CB  1 
ATOM   2238 O OG1 . THR A  1 282 ? -46.219 -42.071 -6.166  1.00 24.37  ? 309  THR A OG1 1 
ATOM   2239 C CG2 . THR A  1 282 ? -47.460 -44.114 -5.884  1.00 26.70  ? 309  THR A CG2 1 
ATOM   2240 N N   . LEU A  1 283 ? -47.721 -40.097 -5.268  1.00 28.80  ? 310  LEU A N   1 
ATOM   2241 C CA  . LEU A  1 283 ? -48.314 -39.030 -6.062  1.00 28.36  ? 310  LEU A CA  1 
ATOM   2242 C C   . LEU A  1 283 ? -48.004 -39.270 -7.533  1.00 34.76  ? 310  LEU A C   1 
ATOM   2243 O O   . LEU A  1 283 ? -46.878 -39.628 -7.875  1.00 39.05  ? 310  LEU A O   1 
ATOM   2244 C CB  . LEU A  1 283 ? -47.758 -37.672 -5.635  1.00 26.80  ? 310  LEU A CB  1 
ATOM   2245 C CG  . LEU A  1 283 ? -47.822 -37.349 -4.141  1.00 27.82  ? 310  LEU A CG  1 
ATOM   2246 C CD1 . LEU A  1 283 ? -47.349 -35.923 -3.864  1.00 18.65  ? 310  LEU A CD1 1 
ATOM   2247 C CD2 . LEU A  1 283 ? -49.224 -37.583 -3.592  1.00 24.33  ? 310  LEU A CD2 1 
ATOM   2248 N N   . PRO A  1 284 ? -49.008 -39.092 -8.408  1.00 40.80  ? 311  PRO A N   1 
ATOM   2249 C CA  . PRO A  1 284 ? -48.836 -39.240 -9.861  1.00 36.64  ? 311  PRO A CA  1 
ATOM   2250 C C   . PRO A  1 284 ? -47.751 -38.338 -10.449 1.00 28.51  ? 311  PRO A C   1 
ATOM   2251 O O   . PRO A  1 284 ? -47.430 -37.297 -9.873  1.00 27.05  ? 311  PRO A O   1 
ATOM   2252 C CB  . PRO A  1 284 ? -50.214 -38.850 -10.424 1.00 37.62  ? 311  PRO A CB  1 
ATOM   2253 C CG  . PRO A  1 284 ? -50.961 -38.216 -9.278  1.00 28.94  ? 311  PRO A CG  1 
ATOM   2254 C CD  . PRO A  1 284 ? -50.418 -38.868 -8.050  1.00 33.43  ? 311  PRO A CD  1 
ATOM   2255 N N   . SER A  1 285 ? -47.204 -38.753 -11.589 1.00 25.51  ? 312  SER A N   1 
ATOM   2256 C CA  . SER A  1 285 ? -46.149 -38.018 -12.280 1.00 28.03  ? 312  SER A CA  1 
ATOM   2257 C C   . SER A  1 285 ? -46.428 -36.523 -12.398 1.00 31.08  ? 312  SER A C   1 
ATOM   2258 O O   . SER A  1 285 ? -47.584 -36.106 -12.524 1.00 30.37  ? 312  SER A O   1 
ATOM   2259 C CB  . SER A  1 285 ? -45.930 -38.607 -13.678 1.00 25.94  ? 312  SER A CB  1 
ATOM   2260 O OG  . SER A  1 285 ? -45.255 -37.690 -14.525 1.00 23.13  ? 312  SER A OG  1 
ATOM   2261 N N   . ARG A  1 286 ? -45.359 -35.729 -12.334 1.00 29.87  ? 313  ARG A N   1 
ATOM   2262 C CA  . ARG A  1 286 ? -45.415 -34.285 -12.575 1.00 29.35  ? 313  ARG A CA  1 
ATOM   2263 C C   . ARG A  1 286 ? -46.561 -33.552 -11.876 1.00 33.14  ? 313  ARG A C   1 
ATOM   2264 O O   . ARG A  1 286 ? -47.026 -32.518 -12.368 1.00 33.32  ? 313  ARG A O   1 
ATOM   2265 C CB  . ARG A  1 286 ? -45.504 -34.003 -14.073 1.00 31.45  ? 313  ARG A CB  1 
ATOM   2266 C CG  . ARG A  1 286 ? -44.225 -34.198 -14.840 1.00 31.01  ? 313  ARG A CG  1 
ATOM   2267 C CD  . ARG A  1 286 ? -44.437 -33.769 -16.279 1.00 44.95  ? 313  ARG A CD  1 
ATOM   2268 N NE  . ARG A  1 286 ? -43.716 -34.627 -17.211 1.00 56.36  ? 313  ARG A NE  1 
ATOM   2269 C CZ  . ARG A  1 286 ? -42.610 -34.270 -17.853 1.00 49.35  ? 313  ARG A CZ  1 
ATOM   2270 N NH1 . ARG A  1 286 ? -42.096 -33.057 -17.675 1.00 41.82  1 313  ARG A NH1 1 
ATOM   2271 N NH2 . ARG A  1 286 ? -42.025 -35.127 -18.678 1.00 37.88  ? 313  ARG A NH2 1 
ATOM   2272 N N   . LEU A  1 287 ? -47.015 -34.091 -10.747 1.00 28.86  ? 314  LEU A N   1 
ATOM   2273 C CA  . LEU A  1 287 ? -48.175 -33.551 -10.048 1.00 23.52  ? 314  LEU A CA  1 
ATOM   2274 C C   . LEU A  1 287 ? -47.982 -32.076 -9.714  1.00 21.49  ? 314  LEU A C   1 
ATOM   2275 O O   . LEU A  1 287 ? -48.901 -31.274 -9.878  1.00 21.46  ? 314  LEU A O   1 
ATOM   2276 C CB  . LEU A  1 287 ? -48.471 -34.363 -8.784  1.00 22.86  ? 314  LEU A CB  1 
ATOM   2277 C CG  . LEU A  1 287 ? -49.875 -34.273 -8.173  1.00 19.68  ? 314  LEU A CG  1 
ATOM   2278 C CD1 . LEU A  1 287 ? -50.104 -35.425 -7.231  1.00 22.25  ? 314  LEU A CD1 1 
ATOM   2279 C CD2 . LEU A  1 287 ? -50.072 -32.986 -7.419  1.00 17.12  ? 314  LEU A CD2 1 
ATOM   2280 N N   . PHE A  1 288 ? -46.789 -31.717 -9.253  1.00 18.41  ? 315  PHE A N   1 
ATOM   2281 C CA  . PHE A  1 288 ? -46.504 -30.319 -8.954  1.00 20.34  ? 315  PHE A CA  1 
ATOM   2282 C C   . PHE A  1 288 ? -45.528 -29.704 -9.962  1.00 21.46  ? 315  PHE A C   1 
ATOM   2283 O O   . PHE A  1 288 ? -44.986 -28.618 -9.743  1.00 18.73  ? 315  PHE A O   1 
ATOM   2284 C CB  . PHE A  1 288 ? -45.999 -30.160 -7.518  1.00 15.16  ? 315  PHE A CB  1 
ATOM   2285 C CG  . PHE A  1 288 ? -46.967 -30.652 -6.477  1.00 18.31  ? 315  PHE A CG  1 
ATOM   2286 C CD1 . PHE A  1 288 ? -48.119 -29.939 -6.189  1.00 16.17  ? 315  PHE A CD1 1 
ATOM   2287 C CD2 . PHE A  1 288 ? -46.726 -31.829 -5.783  1.00 21.86  ? 315  PHE A CD2 1 
ATOM   2288 C CE1 . PHE A  1 288 ? -49.015 -30.395 -5.230  1.00 15.24  ? 315  PHE A CE1 1 
ATOM   2289 C CE2 . PHE A  1 288 ? -47.619 -32.289 -4.820  1.00 16.04  ? 315  PHE A CE2 1 
ATOM   2290 C CZ  . PHE A  1 288 ? -48.760 -31.571 -4.543  1.00 11.28  ? 315  PHE A CZ  1 
ATOM   2291 N N   . ALA A  1 289 ? -45.331 -30.391 -11.083 1.00 19.76  ? 316  ALA A N   1 
ATOM   2292 C CA  . ALA A  1 289 ? -44.380 -29.935 -12.087 1.00 19.14  ? 316  ALA A CA  1 
ATOM   2293 C C   . ALA A  1 289 ? -44.915 -28.790 -12.928 1.00 19.86  ? 316  ALA A C   1 
ATOM   2294 O O   . ALA A  1 289 ? -46.118 -28.700 -13.180 1.00 26.18  ? 316  ALA A O   1 
ATOM   2295 C CB  . ALA A  1 289 ? -43.966 -31.080 -12.982 1.00 25.29  ? 316  ALA A CB  1 
ATOM   2296 N N   . ASN A  1 290 ? -43.996 -27.934 -13.367 1.00 17.19  ? 317  ASN A N   1 
ATOM   2297 C CA  . ASN A  1 290 ? -44.293 -26.805 -14.247 1.00 16.93  ? 317  ASN A CA  1 
ATOM   2298 C C   . ASN A  1 290 ? -45.160 -25.749 -13.584 1.00 16.43  ? 317  ASN A C   1 
ATOM   2299 O O   . ASN A  1 290 ? -45.982 -25.117 -14.237 1.00 18.96  ? 317  ASN A O   1 
ATOM   2300 C CB  . ASN A  1 290 ? -44.919 -27.275 -15.561 1.00 14.25  ? 317  ASN A CB  1 
ATOM   2301 C CG  . ASN A  1 290 ? -44.088 -28.334 -16.249 1.00 18.09  ? 317  ASN A CG  1 
ATOM   2302 O OD1 . ASN A  1 290 ? -43.133 -28.020 -16.958 1.00 18.87  ? 317  ASN A OD1 1 
ATOM   2303 N ND2 . ASN A  1 290 ? -44.444 -29.599 -16.043 1.00 19.04  ? 317  ASN A ND2 1 
ATOM   2304 N N   . GLN A  1 291 ? -44.958 -25.563 -12.284 1.00 15.49  ? 318  GLN A N   1 
ATOM   2305 C CA  . GLN A  1 291 ? -45.706 -24.586 -11.503 1.00 14.56  ? 318  GLN A CA  1 
ATOM   2306 C C   . GLN A  1 291 ? -44.863 -23.354 -11.163 1.00 18.23  ? 318  GLN A C   1 
ATOM   2307 O O   . GLN A  1 291 ? -44.079 -23.370 -10.209 1.00 19.33  ? 318  GLN A O   1 
ATOM   2308 C CB  . GLN A  1 291 ? -46.222 -25.239 -10.223 1.00 13.72  ? 318  GLN A CB  1 
ATOM   2309 C CG  . GLN A  1 291 ? -47.503 -26.017 -10.404 1.00 13.97  ? 318  GLN A CG  1 
ATOM   2310 C CD  . GLN A  1 291 ? -48.704 -25.104 -10.519 1.00 18.30  ? 318  GLN A CD  1 
ATOM   2311 O OE1 . GLN A  1 291 ? -48.587 -23.883 -10.380 1.00 16.28  ? 318  GLN A OE1 1 
ATOM   2312 N NE2 . GLN A  1 291 ? -49.870 -25.688 -10.768 1.00 19.88  ? 318  GLN A NE2 1 
ATOM   2313 N N   . PRO A  1 292 ? -45.032 -22.275 -11.939 1.00 15.22  ? 319  PRO A N   1 
ATOM   2314 C CA  . PRO A  1 292 ? -44.230 -21.048 -11.840 1.00 14.15  ? 319  PRO A CA  1 
ATOM   2315 C C   . PRO A  1 292 ? -44.344 -20.249 -10.533 1.00 15.83  ? 319  PRO A C   1 
ATOM   2316 O O   . PRO A  1 292 ? -43.504 -19.382 -10.299 1.00 23.14  ? 319  PRO A O   1 
ATOM   2317 C CB  . PRO A  1 292 ? -44.741 -20.203 -13.012 1.00 18.68  ? 319  PRO A CB  1 
ATOM   2318 C CG  . PRO A  1 292 ? -46.099 -20.752 -13.321 1.00 20.05  ? 319  PRO A CG  1 
ATOM   2319 C CD  . PRO A  1 292 ? -45.994 -22.214 -13.051 1.00 15.20  ? 319  PRO A CD  1 
ATOM   2320 N N   . GLU A  1 293 ? -45.344 -20.512 -9.699  1.00 16.39  ? 320  GLU A N   1 
ATOM   2321 C CA  . GLU A  1 293 ? -45.508 -19.723 -8.479  1.00 15.09  ? 320  GLU A CA  1 
ATOM   2322 C C   . GLU A  1 293 ? -45.573 -20.579 -7.216  1.00 15.26  ? 320  GLU A C   1 
ATOM   2323 O O   . GLU A  1 293 ? -45.661 -20.050 -6.106  1.00 13.91  ? 320  GLU A O   1 
ATOM   2324 C CB  . GLU A  1 293 ? -46.754 -18.836 -8.574  1.00 18.80  ? 320  GLU A CB  1 
ATOM   2325 C CG  . GLU A  1 293 ? -46.609 -17.623 -9.490  1.00 27.61  ? 320  GLU A CG  1 
ATOM   2326 C CD  . GLU A  1 293 ? -47.952 -16.979 -9.839  1.00 34.92  ? 320  GLU A CD  1 
ATOM   2327 O OE1 . GLU A  1 293 ? -48.978 -17.353 -9.223  1.00 27.67  ? 320  GLU A OE1 1 
ATOM   2328 O OE2 . GLU A  1 293 ? -47.978 -16.104 -10.737 1.00 30.84  1 320  GLU A OE2 1 
ATOM   2329 N N   . LEU A  1 294 ? -45.524 -21.898 -7.389  1.00 15.22  ? 321  LEU A N   1 
ATOM   2330 C CA  . LEU A  1 294 ? -45.682 -22.831 -6.275  1.00 13.51  ? 321  LEU A CA  1 
ATOM   2331 C C   . LEU A  1 294 ? -44.565 -22.690 -5.259  1.00 13.50  ? 321  LEU A C   1 
ATOM   2332 O O   . LEU A  1 294 ? -43.391 -22.769 -5.608  1.00 17.64  ? 321  LEU A O   1 
ATOM   2333 C CB  . LEU A  1 294 ? -45.751 -24.272 -6.785  1.00 11.68  ? 321  LEU A CB  1 
ATOM   2334 C CG  . LEU A  1 294 ? -45.856 -25.405 -5.764  1.00 10.25  ? 321  LEU A CG  1 
ATOM   2335 C CD1 . LEU A  1 294 ? -46.832 -25.070 -4.652  1.00 10.07  ? 321  LEU A CD1 1 
ATOM   2336 C CD2 . LEU A  1 294 ? -46.280 -26.680 -6.474  1.00 11.13  ? 321  LEU A CD2 1 
ATOM   2337 N N   . GLN A  1 295 ? -44.938 -22.485 -4.001  1.00 11.41  ? 322  GLN A N   1 
ATOM   2338 C CA  . GLN A  1 295 ? -43.957 -22.310 -2.941  1.00 12.08  ? 322  GLN A CA  1 
ATOM   2339 C C   . GLN A  1 295 ? -44.084 -23.360 -1.843  1.00 13.92  ? 322  GLN A C   1 
ATOM   2340 O O   . GLN A  1 295 ? -43.425 -24.395 -1.883  1.00 17.05  ? 322  GLN A O   1 
ATOM   2341 C CB  . GLN A  1 295 ? -44.053 -20.907 -2.351  1.00 10.64  ? 322  GLN A CB  1 
ATOM   2342 C CG  . GLN A  1 295 ? -43.605 -19.835 -3.308  1.00 14.94  ? 322  GLN A CG  1 
ATOM   2343 C CD  . GLN A  1 295 ? -43.290 -18.532 -2.609  1.00 23.55  ? 322  GLN A CD  1 
ATOM   2344 O OE1 . GLN A  1 295 ? -43.964 -18.149 -1.651  1.00 23.68  ? 322  GLN A OE1 1 
ATOM   2345 N NE2 . GLN A  1 295 ? -42.254 -17.841 -3.083  1.00 26.35  ? 322  GLN A NE2 1 
ATOM   2346 N N   . ILE A  1 296 ? -44.930 -23.086 -0.861  1.00 11.66  ? 323  ILE A N   1 
ATOM   2347 C CA  . ILE A  1 296 ? -45.124 -23.987 0.265   1.00 8.92   ? 323  ILE A CA  1 
ATOM   2348 C C   . ILE A  1 296 ? -45.825 -25.275 -0.169  1.00 8.29   ? 323  ILE A C   1 
ATOM   2349 O O   . ILE A  1 296 ? -46.682 -25.265 -1.042  1.00 9.85   ? 323  ILE A O   1 
ATOM   2350 C CB  . ILE A  1 296 ? -45.926 -23.273 1.362   1.00 8.95   ? 323  ILE A CB  1 
ATOM   2351 C CG1 . ILE A  1 296 ? -45.202 -21.989 1.763   1.00 9.84   ? 323  ILE A CG1 1 
ATOM   2352 C CG2 . ILE A  1 296 ? -46.165 -24.176 2.562   1.00 8.97   ? 323  ILE A CG2 1 
ATOM   2353 C CD1 . ILE A  1 296 ? -46.099 -20.957 2.372   1.00 12.53  ? 323  ILE A CD1 1 
ATOM   2354 N N   . LEU A  1 297 ? -45.429 -26.390 0.424   1.00 8.21   ? 324  LEU A N   1 
ATOM   2355 C CA  . LEU A  1 297 ? -46.090 -27.663 0.179   1.00 8.04   ? 324  LEU A CA  1 
ATOM   2356 C C   . LEU A  1 297 ? -46.138 -28.476 1.468   1.00 7.96   ? 324  LEU A C   1 
ATOM   2357 O O   . LEU A  1 297 ? -45.240 -28.385 2.303   1.00 8.08   ? 324  LEU A O   1 
ATOM   2358 C CB  . LEU A  1 297 ? -45.371 -28.437 -0.921  1.00 7.58   ? 324  LEU A CB  1 
ATOM   2359 C CG  . LEU A  1 297 ? -45.771 -28.088 -2.352  1.00 8.81   ? 324  LEU A CG  1 
ATOM   2360 C CD1 . LEU A  1 297 ? -44.619 -28.301 -3.309  1.00 11.35  ? 324  LEU A CD1 1 
ATOM   2361 C CD2 . LEU A  1 297 ? -46.941 -28.952 -2.761  1.00 10.67  ? 324  LEU A CD2 1 
ATOM   2362 N N   . ARG A  1 298 ? -47.205 -29.249 1.643   1.00 7.08   ? 325  ARG A N   1 
ATOM   2363 C CA  . ARG A  1 298 ? -47.373 -30.061 2.843   1.00 6.61   ? 325  ARG A CA  1 
ATOM   2364 C C   . ARG A  1 298 ? -48.001 -31.387 2.459   1.00 7.38   ? 325  ARG A C   1 
ATOM   2365 O O   . ARG A  1 298 ? -49.156 -31.433 2.048   1.00 7.52   ? 325  ARG A O   1 
ATOM   2366 C CB  . ARG A  1 298 ? -48.271 -29.362 3.861   1.00 5.35   ? 325  ARG A CB  1 
ATOM   2367 C CG  . ARG A  1 298 ? -47.900 -27.920 4.150   1.00 5.66   ? 325  ARG A CG  1 
ATOM   2368 C CD  . ARG A  1 298 ? -47.093 -27.803 5.407   1.00 5.95   ? 325  ARG A CD  1 
ATOM   2369 N NE  . ARG A  1 298 ? -46.752 -26.418 5.707   1.00 7.25   ? 325  ARG A NE  1 
ATOM   2370 C CZ  . ARG A  1 298 ? -45.582 -25.859 5.421   1.00 8.27   ? 325  ARG A CZ  1 
ATOM   2371 N NH1 . ARG A  1 298 ? -44.637 -26.563 4.812   1.00 7.82   1 325  ARG A NH1 1 
ATOM   2372 N NH2 . ARG A  1 298 ? -45.358 -24.593 5.744   1.00 9.53   ? 325  ARG A NH2 1 
ATOM   2373 N N   . LEU A  1 299 ? -47.238 -32.466 2.578   1.00 8.25   ? 326  LEU A N   1 
ATOM   2374 C CA  . LEU A  1 299 ? -47.723 -33.780 2.180   1.00 8.31   ? 326  LEU A CA  1 
ATOM   2375 C C   . LEU A  1 299 ? -47.564 -34.773 3.329   1.00 9.53   ? 326  LEU A C   1 
ATOM   2376 O O   . LEU A  1 299 ? -46.486 -34.911 3.902   1.00 10.90  ? 326  LEU A O   1 
ATOM   2377 C CB  . LEU A  1 299 ? -46.975 -34.259 0.937   1.00 8.84   ? 326  LEU A CB  1 
ATOM   2378 C CG  . LEU A  1 299 ? -46.682 -33.161 -0.093  1.00 8.07   ? 326  LEU A CG  1 
ATOM   2379 C CD1 . LEU A  1 299 ? -45.814 -33.678 -1.219  1.00 10.89  ? 326  LEU A CD1 1 
ATOM   2380 C CD2 . LEU A  1 299 ? -47.958 -32.583 -0.653  1.00 8.59   ? 326  LEU A CD2 1 
ATOM   2381 N N   . ARG A  1 300 ? -48.654 -35.444 3.674   1.00 8.04   ? 327  ARG A N   1 
ATOM   2382 C CA  . ARG A  1 300 ? -48.637 -36.458 4.717   1.00 9.86   ? 327  ARG A CA  1 
ATOM   2383 C C   . ARG A  1 300 ? -49.798 -37.416 4.502   1.00 11.28  ? 327  ARG A C   1 
ATOM   2384 O O   . ARG A  1 300 ? -50.906 -37.195 4.994   1.00 10.76  ? 327  ARG A O   1 
ATOM   2385 C CB  . ARG A  1 300 ? -48.717 -35.833 6.114   1.00 9.37   ? 327  ARG A CB  1 
ATOM   2386 C CG  . ARG A  1 300 ? -48.758 -36.875 7.218   1.00 8.65   ? 327  ARG A CG  1 
ATOM   2387 C CD  . ARG A  1 300 ? -48.896 -36.274 8.595   1.00 8.56   ? 327  ARG A CD  1 
ATOM   2388 N NE  . ARG A  1 300 ? -48.952 -37.340 9.591   1.00 11.37  ? 327  ARG A NE  1 
ATOM   2389 C CZ  . ARG A  1 300 ? -48.889 -37.156 10.906  1.00 11.16  ? 327  ARG A CZ  1 
ATOM   2390 N NH1 . ARG A  1 300 ? -48.761 -35.933 11.406  1.00 11.73  1 327  ARG A NH1 1 
ATOM   2391 N NH2 . ARG A  1 300 ? -48.954 -38.202 11.721  1.00 7.42   ? 327  ARG A NH2 1 
ATOM   2392 N N   . ALA A  1 301 ? -49.540 -38.475 3.750   1.00 10.30  ? 328  ALA A N   1 
ATOM   2393 C CA  . ALA A  1 301 ? -50.569 -39.451 3.449   1.00 10.73  ? 328  ALA A CA  1 
ATOM   2394 C C   . ALA A  1 301 ? -50.003 -40.855 3.555   1.00 16.10  ? 328  ALA A C   1 
ATOM   2395 O O   . ALA A  1 301 ? -50.504 -41.779 2.916   1.00 17.35  ? 328  ALA A O   1 
ATOM   2396 C CB  . ALA A  1 301 ? -51.118 -39.210 2.069   1.00 12.31  ? 328  ALA A CB  1 
ATOM   2397 N N   . GLU A  1 302 ? -48.964 -41.002 4.376   1.00 19.29  ? 329  GLU A N   1 
ATOM   2398 C CA  . GLU A  1 302 ? -48.204 -42.248 4.480   1.00 17.56  ? 329  GLU A CA  1 
ATOM   2399 C C   . GLU A  1 302 ? -47.687 -42.661 3.111   1.00 15.75  ? 329  GLU A C   1 
ATOM   2400 O O   . GLU A  1 302 ? -47.827 -43.810 2.692   1.00 15.33  ? 329  GLU A O   1 
ATOM   2401 C CB  . GLU A  1 302 ? -49.039 -43.357 5.115   1.00 16.59  ? 329  GLU A CB  1 
ATOM   2402 C CG  . GLU A  1 302 ? -49.633 -42.956 6.445   1.00 23.96  ? 329  GLU A CG  1 
ATOM   2403 C CD  . GLU A  1 302 ? -50.179 -44.135 7.214   1.00 40.69  ? 329  GLU A CD  1 
ATOM   2404 O OE1 . GLU A  1 302 ? -51.100 -43.929 8.033   1.00 57.56  ? 329  GLU A OE1 1 
ATOM   2405 O OE2 . GLU A  1 302 ? -49.683 -45.266 7.005   1.00 31.76  1 329  GLU A OE2 1 
ATOM   2406 N N   . LEU A  1 303 ? -47.099 -41.696 2.416   1.00 15.50  ? 330  LEU A N   1 
ATOM   2407 C CA  . LEU A  1 303 ? -46.563 -41.928 1.090   1.00 18.73  ? 330  LEU A CA  1 
ATOM   2408 C C   . LEU A  1 303 ? -45.416 -42.921 1.158   1.00 24.61  ? 330  LEU A C   1 
ATOM   2409 O O   . LEU A  1 303 ? -44.608 -42.881 2.089   1.00 22.37  ? 330  LEU A O   1 
ATOM   2410 C CB  . LEU A  1 303 ? -46.075 -40.620 0.471   1.00 19.14  ? 330  LEU A CB  1 
ATOM   2411 C CG  . LEU A  1 303 ? -47.129 -39.629 -0.015  1.00 19.14  ? 330  LEU A CG  1 
ATOM   2412 C CD1 . LEU A  1 303 ? -47.639 -38.768 1.127   1.00 17.56  ? 330  LEU A CD1 1 
ATOM   2413 C CD2 . LEU A  1 303 ? -46.549 -38.766 -1.116  1.00 19.92  ? 330  LEU A CD2 1 
ATOM   2414 N N   . GLN A  1 304 ? -45.345 -43.799 0.160   1.00 25.79  ? 331  GLN A N   1 
ATOM   2415 C CA  . GLN A  1 304 ? -44.312 -44.826 0.108   1.00 21.14  ? 331  GLN A CA  1 
ATOM   2416 C C   . GLN A  1 304 ? -43.178 -44.472 -0.849  1.00 18.96  ? 331  GLN A C   1 
ATOM   2417 O O   . GLN A  1 304 ? -42.053 -44.931 -0.674  1.00 21.08  ? 331  GLN A O   1 
ATOM   2418 C CB  . GLN A  1 304 ? -44.924 -46.169 -0.278  1.00 17.80  ? 331  GLN A CB  1 
ATOM   2419 C CG  . GLN A  1 304 ? -46.057 -46.588 0.630   1.00 20.15  ? 331  GLN A CG  1 
ATOM   2420 C CD  . GLN A  1 304 ? -46.513 -48.006 0.373   1.00 25.49  ? 331  GLN A CD  1 
ATOM   2421 O OE1 . GLN A  1 304 ? -46.567 -48.458 -0.770  1.00 23.14  ? 331  GLN A OE1 1 
ATOM   2422 N NE2 . GLN A  1 304 ? -46.834 -48.722 1.442   1.00 32.18  ? 331  GLN A NE2 1 
ATOM   2423 N N   . SER A  1 305 ? -43.473 -43.657 -1.855  1.00 17.84  ? 332  SER A N   1 
ATOM   2424 C CA  . SER A  1 305 ? -42.475 -43.300 -2.859  1.00 19.81  ? 332  SER A CA  1 
ATOM   2425 C C   . SER A  1 305 ? -42.858 -42.028 -3.602  1.00 24.26  ? 332  SER A C   1 
ATOM   2426 O O   . SER A  1 305 ? -43.972 -41.526 -3.460  1.00 26.22  ? 332  SER A O   1 
ATOM   2427 C CB  . SER A  1 305 ? -42.281 -44.447 -3.857  1.00 22.38  ? 332  SER A CB  1 
ATOM   2428 O OG  . SER A  1 305 ? -43.520 -44.909 -4.374  1.00 19.45  ? 332  SER A OG  1 
ATOM   2429 N N   . LEU A  1 306 ? -41.928 -41.509 -4.396  1.00 20.97  ? 333  LEU A N   1 
ATOM   2430 C CA  . LEU A  1 306 ? -42.168 -40.284 -5.145  1.00 20.75  ? 333  LEU A CA  1 
ATOM   2431 C C   . LEU A  1 306 ? -41.530 -40.369 -6.527  1.00 25.56  ? 333  LEU A C   1 
ATOM   2432 O O   . LEU A  1 306 ? -40.541 -41.078 -6.716  1.00 29.26  ? 333  LEU A O   1 
ATOM   2433 C CB  . LEU A  1 306 ? -41.608 -39.075 -4.387  1.00 17.66  ? 333  LEU A CB  1 
ATOM   2434 C CG  . LEU A  1 306 ? -42.168 -38.787 -2.991  1.00 17.29  ? 333  LEU A CG  1 
ATOM   2435 C CD1 . LEU A  1 306 ? -41.326 -37.753 -2.277  1.00 16.76  ? 333  LEU A CD1 1 
ATOM   2436 C CD2 . LEU A  1 306 ? -43.609 -38.329 -3.064  1.00 15.95  ? 333  LEU A CD2 1 
ATOM   2437 N N   . PRO A  1 307 ? -42.111 -39.661 -7.505  1.00 25.77  ? 334  PRO A N   1 
ATOM   2438 C CA  . PRO A  1 307 ? -41.518 -39.512 -8.838  1.00 28.24  ? 334  PRO A CA  1 
ATOM   2439 C C   . PRO A  1 307 ? -40.504 -38.379 -8.851  1.00 26.92  ? 334  PRO A C   1 
ATOM   2440 O O   . PRO A  1 307 ? -40.719 -37.375 -8.178  1.00 27.06  ? 334  PRO A O   1 
ATOM   2441 C CB  . PRO A  1 307 ? -42.718 -39.133 -9.702  1.00 34.97  ? 334  PRO A CB  1 
ATOM   2442 C CG  . PRO A  1 307 ? -43.617 -38.403 -8.771  1.00 33.08  ? 334  PRO A CG  1 
ATOM   2443 C CD  . PRO A  1 307 ? -43.466 -39.088 -7.438  1.00 27.19  ? 334  PRO A CD  1 
ATOM   2444 N N   . GLY A  1 308 ? -39.420 -38.534 -9.604  1.00 26.78  ? 335  GLY A N   1 
ATOM   2445 C CA  . GLY A  1 308 ? -38.385 -37.516 -9.650  1.00 30.18  ? 335  GLY A CA  1 
ATOM   2446 C C   . GLY A  1 308 ? -38.891 -36.224 -10.259 1.00 34.45  ? 335  GLY A C   1 
ATOM   2447 O O   . GLY A  1 308 ? -38.431 -35.128 -9.916  1.00 26.59  ? 335  GLY A O   1 
ATOM   2448 N N   . ASP A  1 309 ? -39.859 -36.361 -11.162 1.00 33.99  ? 336  ASP A N   1 
ATOM   2449 C CA  . ASP A  1 309 ? -40.433 -35.220 -11.860 1.00 32.52  ? 336  ASP A CA  1 
ATOM   2450 C C   . ASP A  1 309 ? -41.612 -34.619 -11.098 1.00 32.18  ? 336  ASP A C   1 
ATOM   2451 O O   . ASP A  1 309 ? -42.395 -33.862 -11.667 1.00 33.88  ? 336  ASP A O   1 
ATOM   2452 C CB  . ASP A  1 309 ? -40.866 -35.614 -13.281 1.00 37.80  ? 336  ASP A CB  1 
ATOM   2453 C CG  . ASP A  1 309 ? -41.847 -36.784 -13.299 1.00 40.04  ? 336  ASP A CG  1 
ATOM   2454 O OD1 . ASP A  1 309 ? -42.961 -36.643 -12.750 1.00 43.21  ? 336  ASP A OD1 1 
ATOM   2455 O OD2 . ASP A  1 309 ? -41.514 -37.840 -13.883 1.00 33.75  1 336  ASP A OD2 1 
ATOM   2456 N N   . LEU A  1 310 ? -41.737 -34.964 -9.818  1.00 32.54  ? 337  LEU A N   1 
ATOM   2457 C CA  . LEU A  1 310 ? -42.831 -34.462 -8.987  1.00 24.74  ? 337  LEU A CA  1 
ATOM   2458 C C   . LEU A  1 310 ? -42.806 -32.944 -8.855  1.00 19.65  ? 337  LEU A C   1 
ATOM   2459 O O   . LEU A  1 310 ? -43.857 -32.311 -8.814  1.00 20.15  ? 337  LEU A O   1 
ATOM   2460 C CB  . LEU A  1 310 ? -42.797 -35.092 -7.594  1.00 21.47  ? 337  LEU A CB  1 
ATOM   2461 C CG  . LEU A  1 310 ? -43.962 -34.717 -6.675  1.00 20.00  ? 337  LEU A CG  1 
ATOM   2462 C CD1 . LEU A  1 310 ? -45.230 -35.437 -7.096  1.00 25.22  ? 337  LEU A CD1 1 
ATOM   2463 C CD2 . LEU A  1 310 ? -43.635 -35.019 -5.229  1.00 19.98  ? 337  LEU A CD2 1 
ATOM   2464 N N   . PHE A  1 311 ? -41.610 -32.364 -8.784  1.00 16.02  ? 338  PHE A N   1 
ATOM   2465 C CA  . PHE A  1 311 ? -41.482 -30.918 -8.680  1.00 14.49  ? 338  PHE A CA  1 
ATOM   2466 C C   . PHE A  1 311 ? -40.767 -30.324 -9.883  1.00 17.66  ? 338  PHE A C   1 
ATOM   2467 O O   . PHE A  1 311 ? -40.279 -29.196 -9.815  1.00 16.94  ? 338  PHE A O   1 
ATOM   2468 C CB  . PHE A  1 311 ? -40.723 -30.523 -7.416  1.00 16.31  ? 338  PHE A CB  1 
ATOM   2469 C CG  . PHE A  1 311 ? -41.278 -31.112 -6.156  1.00 17.85  ? 338  PHE A CG  1 
ATOM   2470 C CD1 . PHE A  1 311 ? -42.499 -30.693 -5.658  1.00 17.57  ? 338  PHE A CD1 1 
ATOM   2471 C CD2 . PHE A  1 311 ? -40.565 -32.070 -5.454  1.00 20.02  ? 338  PHE A CD2 1 
ATOM   2472 C CE1 . PHE A  1 311 ? -43.010 -31.232 -4.489  1.00 18.03  ? 338  PHE A CE1 1 
ATOM   2473 C CE2 . PHE A  1 311 ? -41.067 -32.615 -4.283  1.00 19.42  ? 338  PHE A CE2 1 
ATOM   2474 C CZ  . PHE A  1 311 ? -42.290 -32.193 -3.798  1.00 19.94  ? 338  PHE A CZ  1 
ATOM   2475 N N   . GLU A  1 312 ? -40.709 -31.081 -10.978 1.00 21.46  ? 339  GLU A N   1 
ATOM   2476 C CA  . GLU A  1 312 ? -39.961 -30.680 -12.175 1.00 22.23  ? 339  GLU A CA  1 
ATOM   2477 C C   . GLU A  1 312 ? -40.331 -29.288 -12.690 1.00 19.38  ? 339  GLU A C   1 
ATOM   2478 O O   . GLU A  1 312 ? -41.497 -29.004 -12.932 1.00 21.29  ? 339  GLU A O   1 
ATOM   2479 C CB  . GLU A  1 312 ? -40.129 -31.719 -13.287 1.00 21.71  ? 339  GLU A CB  1 
ATOM   2480 C CG  . GLU A  1 312 ? -39.341 -31.404 -14.548 1.00 32.30  ? 339  GLU A CG  1 
ATOM   2481 C CD  . GLU A  1 312 ? -39.398 -32.525 -15.577 1.00 45.99  ? 339  GLU A CD  1 
ATOM   2482 O OE1 . GLU A  1 312 ? -39.182 -32.244 -16.779 1.00 42.45  ? 339  GLU A OE1 1 
ATOM   2483 O OE2 . GLU A  1 312 ? -39.652 -33.686 -15.184 1.00 46.01  1 339  GLU A OE2 1 
ATOM   2484 N N   . HIS A  1 313 ? -39.322 -28.431 -12.835 1.00 19.99  ? 340  HIS A N   1 
ATOM   2485 C CA  . HIS A  1 313 ? -39.479 -27.044 -13.298 1.00 22.07  ? 340  HIS A CA  1 
ATOM   2486 C C   . HIS A  1 313 ? -40.202 -26.103 -12.325 1.00 19.46  ? 340  HIS A C   1 
ATOM   2487 O O   . HIS A  1 313 ? -40.522 -24.969 -12.682 1.00 19.68  ? 340  HIS A O   1 
ATOM   2488 C CB  . HIS A  1 313 ? -40.140 -26.976 -14.682 1.00 24.20  ? 340  HIS A CB  1 
ATOM   2489 C CG  . HIS A  1 313 ? -39.390 -27.711 -15.749 1.00 30.84  ? 340  HIS A CG  1 
ATOM   2490 N ND1 . HIS A  1 313 ? -40.022 -28.395 -16.765 1.00 34.19  ? 340  HIS A ND1 1 
ATOM   2491 C CD2 . HIS A  1 313 ? -38.062 -27.868 -15.959 1.00 32.67  ? 340  HIS A CD2 1 
ATOM   2492 C CE1 . HIS A  1 313 ? -39.116 -28.946 -17.553 1.00 34.24  ? 340  HIS A CE1 1 
ATOM   2493 N NE2 . HIS A  1 313 ? -37.919 -28.641 -17.087 1.00 39.98  ? 340  HIS A NE2 1 
ATOM   2494 N N   . SER A  1 314 ? -40.452 -26.560 -11.103 1.00 19.71  ? 341  SER A N   1 
ATOM   2495 C CA  . SER A  1 314 ? -41.140 -25.725 -10.118 1.00 20.62  ? 341  SER A CA  1 
ATOM   2496 C C   . SER A  1 314 ? -40.130 -24.982 -9.252  1.00 21.42  ? 341  SER A C   1 
ATOM   2497 O O   . SER A  1 314 ? -40.084 -25.144 -8.033  1.00 21.13  ? 341  SER A O   1 
ATOM   2498 C CB  . SER A  1 314 ? -42.093 -26.562 -9.257  1.00 20.64  ? 341  SER A CB  1 
ATOM   2499 O OG  . SER A  1 314 ? -43.185 -27.053 -10.024 1.00 19.86  ? 341  SER A OG  1 
ATOM   2500 N N   . THR A  1 315 ? -39.336 -24.141 -9.901  1.00 20.89  ? 342  THR A N   1 
ATOM   2501 C CA  . THR A  1 315 ? -38.163 -23.536 -9.283  1.00 22.69  ? 342  THR A CA  1 
ATOM   2502 C C   . THR A  1 315 ? -38.466 -22.459 -8.240  1.00 22.66  ? 342  THR A C   1 
ATOM   2503 O O   . THR A  1 315 ? -37.628 -21.592 -7.977  1.00 21.69  ? 342  THR A O   1 
ATOM   2504 C CB  . THR A  1 315 ? -37.270 -22.906 -10.357 1.00 22.81  ? 342  THR A CB  1 
ATOM   2505 O OG1 . THR A  1 315 ? -37.432 -21.482 -10.335 1.00 27.65  ? 342  THR A OG1 1 
ATOM   2506 C CG2 . THR A  1 315 ? -37.644 -23.442 -11.735 1.00 16.75  ? 342  THR A CG2 1 
ATOM   2507 N N   . GLN A  1 316 ? -39.648 -22.507 -7.637  1.00 17.80  ? 343  GLN A N   1 
ATOM   2508 C CA  . GLN A  1 316 ? -40.016 -21.467 -6.690  1.00 19.51  ? 343  GLN A CA  1 
ATOM   2509 C C   . GLN A  1 316 ? -40.308 -21.979 -5.286  1.00 17.70  ? 343  GLN A C   1 
ATOM   2510 O O   . GLN A  1 316 ? -40.357 -21.196 -4.334  1.00 15.03  ? 343  GLN A O   1 
ATOM   2511 C CB  . GLN A  1 316 ? -41.193 -20.650 -7.215  1.00 19.41  ? 343  GLN A CB  1 
ATOM   2512 C CG  . GLN A  1 316 ? -40.975 -19.172 -7.038  1.00 22.84  ? 343  GLN A CG  1 
ATOM   2513 C CD  . GLN A  1 316 ? -39.585 -18.773 -7.473  1.00 30.77  ? 343  GLN A CD  1 
ATOM   2514 O OE1 . GLN A  1 316 ? -39.160 -19.088 -8.587  1.00 27.16  ? 343  GLN A OE1 1 
ATOM   2515 N NE2 . GLN A  1 316 ? -38.857 -18.099 -6.588  1.00 31.01  ? 343  GLN A NE2 1 
ATOM   2516 N N   . ILE A  1 317 ? -40.502 -23.290 -5.172  1.00 12.80  ? 344  ILE A N   1 
ATOM   2517 C CA  . ILE A  1 317 ? -40.792 -23.928 -3.898  1.00 10.23  ? 344  ILE A CA  1 
ATOM   2518 C C   . ILE A  1 317 ? -39.846 -23.443 -2.809  1.00 11.30  ? 344  ILE A C   1 
ATOM   2519 O O   . ILE A  1 317 ? -38.644 -23.363 -3.024  1.00 13.59  ? 344  ILE A O   1 
ATOM   2520 C CB  . ILE A  1 317 ? -40.669 -25.449 -4.023  1.00 11.07  ? 344  ILE A CB  1 
ATOM   2521 C CG1 . ILE A  1 317 ? -41.578 -25.960 -5.138  1.00 12.53  ? 344  ILE A CG1 1 
ATOM   2522 C CG2 . ILE A  1 317 ? -41.001 -26.128 -2.708  1.00 10.27  ? 344  ILE A CG2 1 
ATOM   2523 C CD1 . ILE A  1 317 ? -41.474 -27.448 -5.364  1.00 14.48  ? 344  ILE A CD1 1 
ATOM   2524 N N   . THR A  1 318 ? -40.391 -23.094 -1.648  1.00 11.36  ? 345  THR A N   1 
ATOM   2525 C CA  . THR A  1 318 ? -39.558 -22.653 -0.535  1.00 11.02  ? 345  THR A CA  1 
ATOM   2526 C C   . THR A  1 318 ? -39.620 -23.597 0.670   1.00 13.95  ? 345  THR A C   1 
ATOM   2527 O O   . THR A  1 318 ? -38.603 -23.846 1.309   1.00 15.51  ? 345  THR A O   1 
ATOM   2528 C CB  . THR A  1 318 ? -39.912 -21.236 -0.075  1.00 9.14   ? 345  THR A CB  1 
ATOM   2529 O OG1 . THR A  1 318 ? -41.233 -21.232 0.477   1.00 10.54  ? 345  THR A OG1 1 
ATOM   2530 C CG2 . THR A  1 318 ? -39.836 -20.264 -1.238  1.00 11.25  ? 345  THR A CG2 1 
ATOM   2531 N N   . ASN A  1 319 ? -40.806 -24.095 1.008   1.00 12.08  ? 346  ASN A N   1 
ATOM   2532 C CA  . ASN A  1 319 ? -40.914 -25.094 2.070   1.00 11.01  ? 346  ASN A CA  1 
ATOM   2533 C C   . ASN A  1 319 ? -41.555 -26.381 1.567   1.00 9.19   ? 346  ASN A C   1 
ATOM   2534 O O   . ASN A  1 319 ? -42.420 -26.338 0.703   1.00 9.61   ? 346  ASN A O   1 
ATOM   2535 C CB  . ASN A  1 319 ? -41.699 -24.555 3.268   1.00 10.68  ? 346  ASN A CB  1 
ATOM   2536 C CG  . ASN A  1 319 ? -41.226 -23.190 3.708   1.00 11.31  ? 346  ASN A CG  1 
ATOM   2537 O OD1 . ASN A  1 319 ? -40.885 -22.354 2.883   1.00 12.16  ? 346  ASN A OD1 1 
ATOM   2538 N ND2 . ASN A  1 319 ? -41.207 -22.956 5.014   1.00 15.68  ? 346  ASN A ND2 1 
ATOM   2539 N N   . ILE A  1 320 ? -41.118 -27.522 2.097   1.00 8.42   ? 347  ILE A N   1 
ATOM   2540 C CA  . ILE A  1 320 ? -41.741 -28.812 1.802   1.00 7.37   ? 347  ILE A CA  1 
ATOM   2541 C C   . ILE A  1 320 ? -41.820 -29.628 3.074   1.00 7.04   ? 347  ILE A C   1 
ATOM   2542 O O   . ILE A  1 320 ? -40.819 -29.794 3.760   1.00 8.60   ? 347  ILE A O   1 
ATOM   2543 C CB  . ILE A  1 320 ? -40.939 -29.642 0.780   1.00 7.00   ? 347  ILE A CB  1 
ATOM   2544 C CG1 . ILE A  1 320 ? -41.032 -29.018 -0.608  1.00 9.13   ? 347  ILE A CG1 1 
ATOM   2545 C CG2 . ILE A  1 320 ? -41.452 -31.083 0.733   1.00 5.71   ? 347  ILE A CG2 1 
ATOM   2546 C CD1 . ILE A  1 320 ? -40.438 -29.872 -1.697  1.00 10.44  ? 347  ILE A CD1 1 
ATOM   2547 N N   . SER A  1 321 ? -43.003 -30.134 3.395   1.00 5.91   ? 348  SER A N   1 
ATOM   2548 C CA  . SER A  1 321 ? -43.145 -31.007 4.544   1.00 5.38   ? 348  SER A CA  1 
ATOM   2549 C C   . SER A  1 321 ? -43.502 -32.398 4.074   1.00 6.67   ? 348  SER A C   1 
ATOM   2550 O O   . SER A  1 321 ? -44.669 -32.714 3.879   1.00 7.79   ? 348  SER A O   1 
ATOM   2551 C CB  . SER A  1 321 ? -44.211 -30.484 5.504   1.00 4.90   ? 348  SER A CB  1 
ATOM   2552 O OG  . SER A  1 321 ? -43.857 -29.218 6.027   1.00 3.79   ? 348  SER A OG  1 
ATOM   2553 N N   . LEU A  1 322 ? -42.486 -33.227 3.878   1.00 8.00   ? 349  LEU A N   1 
ATOM   2554 C CA  . LEU A  1 322 ? -42.702 -34.631 3.556   1.00 9.82   ? 349  LEU A CA  1 
ATOM   2555 C C   . LEU A  1 322 ? -42.515 -35.492 4.794   1.00 10.02  ? 349  LEU A C   1 
ATOM   2556 O O   . LEU A  1 322 ? -42.231 -36.689 4.707   1.00 8.78   ? 349  LEU A O   1 
ATOM   2557 C CB  . LEU A  1 322 ? -41.759 -35.076 2.449   1.00 8.39   ? 349  LEU A CB  1 
ATOM   2558 C CG  . LEU A  1 322 ? -42.317 -34.774 1.070   1.00 7.17   ? 349  LEU A CG  1 
ATOM   2559 C CD1 . LEU A  1 322 ? -41.281 -35.091 0.033   1.00 9.47   ? 349  LEU A CD1 1 
ATOM   2560 C CD2 . LEU A  1 322 ? -43.560 -35.607 0.862   1.00 9.18   ? 349  LEU A CD2 1 
ATOM   2561 N N   . GLY A  1 323 ? -42.676 -34.861 5.951   1.00 10.17  ? 350  GLY A N   1 
ATOM   2562 C CA  . GLY A  1 323 ? -42.581 -35.553 7.216   1.00 10.94  ? 350  GLY A CA  1 
ATOM   2563 C C   . GLY A  1 323 ? -43.740 -36.502 7.437   1.00 13.23  ? 350  GLY A C   1 
ATOM   2564 O O   . GLY A  1 323 ? -44.777 -36.396 6.781   1.00 13.04  ? 350  GLY A O   1 
ATOM   2565 N N   . ASP A  1 324 ? -43.545 -37.437 8.360   1.00 14.88  ? 351  ASP A N   1 
ATOM   2566 C CA  . ASP A  1 324 ? -44.574 -38.392 8.769   1.00 13.97  ? 351  ASP A CA  1 
ATOM   2567 C C   . ASP A  1 324 ? -45.131 -39.238 7.633   1.00 13.64  ? 351  ASP A C   1 
ATOM   2568 O O   . ASP A  1 324 ? -46.332 -39.506 7.591   1.00 17.99  ? 351  ASP A O   1 
ATOM   2569 C CB  . ASP A  1 324 ? -45.723 -37.683 9.487   1.00 13.88  ? 351  ASP A CB  1 
ATOM   2570 C CG  . ASP A  1 324 ? -45.270 -36.946 10.729  1.00 16.32  ? 351  ASP A CG  1 
ATOM   2571 O OD1 . ASP A  1 324 ? -44.893 -37.618 11.718  1.00 14.27  ? 351  ASP A OD1 1 
ATOM   2572 O OD2 . ASP A  1 324 ? -45.312 -35.695 10.713  1.00 17.77  1 351  ASP A OD2 1 
ATOM   2573 N N   . ASN A  1 325 ? -44.268 -39.650 6.712   1.00 12.49  ? 352  ASN A N   1 
ATOM   2574 C CA  . ASN A  1 325 ? -44.683 -40.560 5.651   1.00 15.26  ? 352  ASN A CA  1 
ATOM   2575 C C   . ASN A  1 325 ? -44.128 -41.960 5.858   1.00 15.54  ? 352  ASN A C   1 
ATOM   2576 O O   . ASN A  1 325 ? -43.883 -42.376 6.993   1.00 12.77  ? 352  ASN A O   1 
ATOM   2577 C CB  . ASN A  1 325 ? -44.302 -40.027 4.268   1.00 14.77  ? 352  ASN A CB  1 
ATOM   2578 C CG  . ASN A  1 325 ? -45.265 -38.974 3.766   1.00 13.84  ? 352  ASN A CG  1 
ATOM   2579 O OD1 . ASN A  1 325 ? -46.453 -39.010 4.080   1.00 14.92  ? 352  ASN A OD1 1 
ATOM   2580 N ND2 . ASN A  1 325 ? -44.759 -38.027 2.985   1.00 12.36  ? 352  ASN A ND2 1 
ATOM   2581 N N   . LEU A  1 326 ? -43.950 -42.685 4.757   1.00 16.40  ? 353  LEU A N   1 
ATOM   2582 C CA  . LEU A  1 326 ? -43.391 -44.031 4.797   1.00 18.52  ? 353  LEU A CA  1 
ATOM   2583 C C   . LEU A  1 326 ? -42.288 -44.185 3.766   1.00 18.68  ? 353  LEU A C   1 
ATOM   2584 O O   . LEU A  1 326 ? -41.979 -45.301 3.346   1.00 18.36  ? 353  LEU A O   1 
ATOM   2585 C CB  . LEU A  1 326 ? -44.467 -45.084 4.535   1.00 16.00  ? 353  LEU A CB  1 
ATOM   2586 C CG  . LEU A  1 326 ? -45.426 -45.427 5.670   1.00 16.40  ? 353  LEU A CG  1 
ATOM   2587 C CD1 . LEU A  1 326 ? -46.289 -46.617 5.265   1.00 17.38  ? 353  LEU A CD1 1 
ATOM   2588 C CD2 . LEU A  1 326 ? -44.662 -45.709 6.955   1.00 15.99  ? 353  LEU A CD2 1 
ATOM   2589 N N   . LEU A  1 327 ? -41.707 -43.059 3.359   1.00 19.47  ? 354  LEU A N   1 
ATOM   2590 C CA  . LEU A  1 327 ? -40.634 -43.047 2.367   1.00 21.48  ? 354  LEU A CA  1 
ATOM   2591 C C   . LEU A  1 327 ? -39.460 -43.925 2.795   1.00 21.20  ? 354  LEU A C   1 
ATOM   2592 O O   . LEU A  1 327 ? -38.961 -43.811 3.915   1.00 20.56  ? 354  LEU A O   1 
ATOM   2593 C CB  . LEU A  1 327 ? -40.154 -41.615 2.117   1.00 16.19  ? 354  LEU A CB  1 
ATOM   2594 C CG  . LEU A  1 327 ? -41.200 -40.611 1.635   1.00 15.25  ? 354  LEU A CG  1 
ATOM   2595 C CD1 . LEU A  1 327 ? -40.639 -39.198 1.695   1.00 12.75  ? 354  LEU A CD1 1 
ATOM   2596 C CD2 . LEU A  1 327 ? -41.684 -40.952 0.230   1.00 14.05  ? 354  LEU A CD2 1 
ATOM   2597 N N   . LYS A  1 328 ? -39.033 -44.812 1.904   1.00 19.59  ? 355  LYS A N   1 
ATOM   2598 C CA  . LYS A  1 328 ? -37.900 -45.674 2.188   1.00 20.87  ? 355  LYS A CA  1 
ATOM   2599 C C   . LYS A  1 328 ? -36.651 -44.953 1.729   1.00 23.61  ? 355  LYS A C   1 
ATOM   2600 O O   . LYS A  1 328 ? -35.616 -44.986 2.393   1.00 21.47  ? 355  LYS A O   1 
ATOM   2601 C CB  . LYS A  1 328 ? -38.037 -47.001 1.450   1.00 24.49  ? 355  LYS A CB  1 
ATOM   2602 C CG  . LYS A  1 328 ? -37.337 -48.153 2.139   1.00 28.12  ? 355  LYS A CG  1 
ATOM   2603 C CD  . LYS A  1 328 ? -37.898 -48.347 3.537   1.00 34.27  ? 355  LYS A CD  1 
ATOM   2604 C CE  . LYS A  1 328 ? -37.198 -49.477 4.274   1.00 50.35  ? 355  LYS A CE  1 
ATOM   2605 N NZ  . LYS A  1 328 ? -35.737 -49.238 4.415   1.00 36.34  1 355  LYS A NZ  1 
ATOM   2606 N N   . THR A  1 329 ? -36.766 -44.299 0.578   1.00 24.55  ? 356  THR A N   1 
ATOM   2607 C CA  . THR A  1 329 ? -35.701 -43.463 0.040   1.00 22.00  ? 356  THR A CA  1 
ATOM   2608 C C   . THR A  1 329 ? -36.338 -42.364 -0.793  1.00 18.53  ? 356  THR A C   1 
ATOM   2609 O O   . THR A  1 329 ? -37.558 -42.222 -0.806  1.00 20.00  ? 356  THR A O   1 
ATOM   2610 C CB  . THR A  1 329 ? -34.713 -44.276 -0.824  1.00 22.99  ? 356  THR A CB  1 
ATOM   2611 O OG1 . THR A  1 329 ? -33.853 -43.387 -1.547  1.00 20.84  ? 356  THR A OG1 1 
ATOM   2612 C CG2 . THR A  1 329 ? -35.458 -45.156 -1.811  1.00 22.55  ? 356  THR A CG2 1 
ATOM   2613 N N   . LEU A  1 330 ? -35.516 -41.585 -1.480  1.00 16.95  ? 357  LEU A N   1 
ATOM   2614 C CA  . LEU A  1 330 ? -36.019 -40.600 -2.426  1.00 19.30  ? 357  LEU A CA  1 
ATOM   2615 C C   . LEU A  1 330 ? -35.356 -40.781 -3.788  1.00 25.04  ? 357  LEU A C   1 
ATOM   2616 O O   . LEU A  1 330 ? -34.228 -41.260 -3.873  1.00 30.12  ? 357  LEU A O   1 
ATOM   2617 C CB  . LEU A  1 330 ? -35.761 -39.189 -1.910  1.00 18.13  ? 357  LEU A CB  1 
ATOM   2618 C CG  . LEU A  1 330 ? -36.599 -38.760 -0.710  1.00 16.20  ? 357  LEU A CG  1 
ATOM   2619 C CD1 . LEU A  1 330 ? -36.343 -37.302 -0.396  1.00 17.58  ? 357  LEU A CD1 1 
ATOM   2620 C CD2 . LEU A  1 330 ? -38.065 -38.984 -0.997  1.00 17.60  ? 357  LEU A CD2 1 
ATOM   2621 N N   . PRO A  1 331 ? -36.060 -40.417 -4.867  1.00 24.63  ? 358  PRO A N   1 
ATOM   2622 C CA  . PRO A  1 331 ? -35.368 -40.396 -6.158  1.00 25.68  ? 358  PRO A CA  1 
ATOM   2623 C C   . PRO A  1 331 ? -34.360 -39.254 -6.154  1.00 24.07  ? 358  PRO A C   1 
ATOM   2624 O O   . PRO A  1 331 ? -34.557 -38.276 -5.432  1.00 20.66  ? 358  PRO A O   1 
ATOM   2625 C CB  . PRO A  1 331 ? -36.496 -40.137 -7.160  1.00 23.66  ? 358  PRO A CB  1 
ATOM   2626 C CG  . PRO A  1 331 ? -37.561 -39.466 -6.364  1.00 26.04  ? 358  PRO A CG  1 
ATOM   2627 C CD  . PRO A  1 331 ? -37.482 -40.057 -4.988  1.00 23.18  ? 358  PRO A CD  1 
ATOM   2628 N N   . ALA A  1 332 ? -33.293 -39.381 -6.934  1.00 25.52  ? 359  ALA A N   1 
ATOM   2629 C CA  . ALA A  1 332 ? -32.180 -38.440 -6.848  1.00 28.98  ? 359  ALA A CA  1 
ATOM   2630 C C   . ALA A  1 332 ? -32.515 -37.078 -7.436  1.00 25.54  ? 359  ALA A C   1 
ATOM   2631 O O   . ALA A  1 332 ? -32.077 -36.045 -6.928  1.00 22.35  ? 359  ALA A O   1 
ATOM   2632 C CB  . ALA A  1 332 ? -30.938 -39.019 -7.519  1.00 33.08  ? 359  ALA A CB  1 
ATOM   2633 N N   . THR A  1 333 ? -33.301 -37.085 -8.506  1.00 27.30  ? 360  THR A N   1 
ATOM   2634 C CA  . THR A  1 333 ? -33.590 -35.870 -9.257  1.00 26.85  ? 360  THR A CA  1 
ATOM   2635 C C   . THR A  1 333 ? -34.655 -35.012 -8.597  1.00 27.91  ? 360  THR A C   1 
ATOM   2636 O O   . THR A  1 333 ? -34.865 -33.868 -8.999  1.00 29.85  ? 360  THR A O   1 
ATOM   2637 C CB  . THR A  1 333 ? -34.077 -36.215 -10.659 1.00 22.83  ? 360  THR A CB  1 
ATOM   2638 O OG1 . THR A  1 333 ? -34.164 -37.640 -10.783 1.00 18.93  ? 360  THR A OG1 1 
ATOM   2639 C CG2 . THR A  1 333 ? -33.119 -35.656 -11.706 1.00 21.83  ? 360  THR A CG2 1 
ATOM   2640 N N   . LEU A  1 334 ? -35.308 -35.572 -7.581  1.00 27.78  ? 361  LEU A N   1 
ATOM   2641 C CA  . LEU A  1 334 ? -36.492 -34.978 -6.964  1.00 26.50  ? 361  LEU A CA  1 
ATOM   2642 C C   . LEU A  1 334 ? -36.378 -33.488 -6.665  1.00 26.43  ? 361  LEU A C   1 
ATOM   2643 O O   . LEU A  1 334 ? -37.363 -32.755 -6.764  1.00 31.35  ? 361  LEU A O   1 
ATOM   2644 C CB  . LEU A  1 334 ? -36.869 -35.733 -5.689  1.00 23.65  ? 361  LEU A CB  1 
ATOM   2645 C CG  . LEU A  1 334 ? -38.124 -35.217 -4.983  1.00 24.98  ? 361  LEU A CG  1 
ATOM   2646 C CD1 . LEU A  1 334 ? -39.340 -35.350 -5.887  1.00 25.31  ? 361  LEU A CD1 1 
ATOM   2647 C CD2 . LEU A  1 334 ? -38.345 -35.945 -3.670  1.00 27.63  ? 361  LEU A CD2 1 
ATOM   2648 N N   . LEU A  1 335 ? -35.182 -33.031 -6.319  1.00 19.54  ? 362  LEU A N   1 
ATOM   2649 C CA  . LEU A  1 335 ? -35.007 -31.618 -6.015  1.00 23.95  ? 362  LEU A CA  1 
ATOM   2650 C C   . LEU A  1 335 ? -34.016 -30.921 -6.941  1.00 27.31  ? 362  LEU A C   1 
ATOM   2651 O O   . LEU A  1 335 ? -33.349 -29.970 -6.535  1.00 26.97  ? 362  LEU A O   1 
ATOM   2652 C CB  . LEU A  1 335 ? -34.608 -31.433 -4.552  1.00 20.93  ? 362  LEU A CB  1 
ATOM   2653 C CG  . LEU A  1 335 ? -35.672 -31.899 -3.559  1.00 19.23  ? 362  LEU A CG  1 
ATOM   2654 C CD1 . LEU A  1 335 ? -35.181 -31.751 -2.148  1.00 17.16  ? 362  LEU A CD1 1 
ATOM   2655 C CD2 . LEU A  1 335 ? -36.942 -31.101 -3.750  1.00 26.26  ? 362  LEU A CD2 1 
ATOM   2656 N N   . GLU A  1 336 ? -33.940 -31.384 -8.188  1.00 28.89  ? 363  GLU A N   1 
ATOM   2657 C CA  . GLU A  1 336 ? -32.990 -30.833 -9.154  1.00 27.31  ? 363  GLU A CA  1 
ATOM   2658 C C   . GLU A  1 336 ? -33.180 -29.339 -9.413  1.00 31.11  ? 363  GLU A C   1 
ATOM   2659 O O   . GLU A  1 336 ? -32.208 -28.587 -9.449  1.00 31.16  ? 363  GLU A O   1 
ATOM   2660 C CB  . GLU A  1 336 ? -33.036 -31.584 -10.490 1.00 24.74  ? 363  GLU A CB  1 
ATOM   2661 C CG  . GLU A  1 336 ? -32.065 -30.999 -11.515 1.00 29.95  ? 363  GLU A CG  1 
ATOM   2662 C CD  . GLU A  1 336 ? -32.288 -31.505 -12.927 1.00 40.34  ? 363  GLU A CD  1 
ATOM   2663 O OE1 . GLU A  1 336 ? -32.850 -32.613 -13.088 1.00 43.73  ? 363  GLU A OE1 1 
ATOM   2664 O OE2 . GLU A  1 336 ? -31.899 -30.784 -13.876 1.00 33.85  1 363  GLU A OE2 1 
ATOM   2665 N N   . HIS A  1 337 ? -34.428 -28.911 -9.593  1.00 29.77  ? 364  HIS A N   1 
ATOM   2666 C CA  . HIS A  1 337 ? -34.697 -27.530 -9.988  1.00 25.10  ? 364  HIS A CA  1 
ATOM   2667 C C   . HIS A  1 337 ? -35.087 -26.627 -8.820  1.00 25.27  ? 364  HIS A C   1 
ATOM   2668 O O   . HIS A  1 337 ? -35.305 -25.431 -9.003  1.00 25.25  ? 364  HIS A O   1 
ATOM   2669 C CB  . HIS A  1 337 ? -35.798 -27.476 -11.046 1.00 23.60  ? 364  HIS A CB  1 
ATOM   2670 C CG  . HIS A  1 337 ? -35.700 -28.547 -12.086 1.00 29.17  ? 364  HIS A CG  1 
ATOM   2671 N ND1 . HIS A  1 337 ? -36.074 -29.853 -11.847 1.00 32.92  ? 364  HIS A ND1 1 
ATOM   2672 C CD2 . HIS A  1 337 ? -35.290 -28.503 -13.375 1.00 30.80  ? 364  HIS A CD2 1 
ATOM   2673 C CE1 . HIS A  1 337 ? -35.892 -30.568 -12.943 1.00 37.60  ? 364  HIS A CE1 1 
ATOM   2674 N NE2 . HIS A  1 337 ? -35.417 -29.773 -13.885 1.00 37.11  ? 364  HIS A NE2 1 
ATOM   2675 N N   . GLN A  1 338 ? -35.164 -27.195 -7.623  1.00 24.42  ? 365  GLN A N   1 
ATOM   2676 C CA  . GLN A  1 338 ? -35.701 -26.476 -6.473  1.00 20.74  ? 365  GLN A CA  1 
ATOM   2677 C C   . GLN A  1 338 ? -34.650 -25.585 -5.839  1.00 19.59  ? 365  GLN A C   1 
ATOM   2678 O O   . GLN A  1 338 ? -34.395 -25.668 -4.644  1.00 19.61  ? 365  GLN A O   1 
ATOM   2679 C CB  . GLN A  1 338 ? -36.260 -27.457 -5.442  1.00 22.77  ? 365  GLN A CB  1 
ATOM   2680 C CG  . GLN A  1 338 ? -37.603 -28.060 -5.822  1.00 23.49  ? 365  GLN A CG  1 
ATOM   2681 C CD  . GLN A  1 338 ? -37.605 -28.643 -7.224  1.00 29.75  ? 365  GLN A CD  1 
ATOM   2682 O OE1 . GLN A  1 338 ? -36.789 -29.509 -7.553  1.00 25.19  ? 365  GLN A OE1 1 
ATOM   2683 N NE2 . GLN A  1 338 ? -38.504 -28.145 -8.069  1.00 31.46  ? 365  GLN A NE2 1 
ATOM   2684 N N   . VAL A  1 339 ? -34.052 -24.727 -6.657  1.00 23.61  ? 366  VAL A N   1 
ATOM   2685 C CA  . VAL A  1 339 ? -32.970 -23.843 -6.236  1.00 25.36  ? 366  VAL A CA  1 
ATOM   2686 C C   . VAL A  1 339 ? -33.305 -23.043 -4.984  1.00 28.76  ? 366  VAL A C   1 
ATOM   2687 O O   . VAL A  1 339 ? -32.465 -22.892 -4.092  1.00 27.38  ? 366  VAL A O   1 
ATOM   2688 C CB  . VAL A  1 339 ? -32.621 -22.848 -7.355  1.00 27.30  ? 366  VAL A CB  1 
ATOM   2689 C CG1 . VAL A  1 339 ? -31.500 -21.912 -6.918  1.00 27.73  ? 366  VAL A CG1 1 
ATOM   2690 C CG2 . VAL A  1 339 ? -32.254 -23.600 -8.627  1.00 32.69  ? 366  VAL A CG2 1 
ATOM   2691 N N   . ASN A  1 340 ? -34.538 -22.545 -4.917  1.00 25.66  ? 367  ASN A N   1 
ATOM   2692 C CA  . ASN A  1 340 ? -34.933 -21.626 -3.854  1.00 20.30  ? 367  ASN A CA  1 
ATOM   2693 C C   . ASN A  1 340 ? -35.521 -22.288 -2.618  1.00 16.94  ? 367  ASN A C   1 
ATOM   2694 O O   . ASN A  1 340 ? -36.010 -21.601 -1.729  1.00 14.05  ? 367  ASN A O   1 
ATOM   2695 C CB  . ASN A  1 340 ? -35.905 -20.582 -4.390  1.00 21.51  ? 367  ASN A CB  1 
ATOM   2696 C CG  . ASN A  1 340 ? -35.320 -19.781 -5.521  1.00 29.91  ? 367  ASN A CG  1 
ATOM   2697 O OD1 . ASN A  1 340 ? -34.585 -18.818 -5.297  1.00 31.49  ? 367  ASN A OD1 1 
ATOM   2698 N ND2 . ASN A  1 340 ? -35.639 -20.172 -6.750  1.00 33.51  ? 367  ASN A ND2 1 
ATOM   2699 N N   . LEU A  1 341 ? -35.473 -23.616 -2.572  1.00 16.82  ? 368  LEU A N   1 
ATOM   2700 C CA  . LEU A  1 341 ? -35.940 -24.371 -1.414  1.00 14.02  ? 368  LEU A CA  1 
ATOM   2701 C C   . LEU A  1 341 ? -35.212 -23.911 -0.153  1.00 14.02  ? 368  LEU A C   1 
ATOM   2702 O O   . LEU A  1 341 ? -34.037 -23.564 -0.207  1.00 18.72  ? 368  LEU A O   1 
ATOM   2703 C CB  . LEU A  1 341 ? -35.733 -25.864 -1.655  1.00 11.76  ? 368  LEU A CB  1 
ATOM   2704 C CG  . LEU A  1 341 ? -36.269 -26.903 -0.677  1.00 9.84   ? 368  LEU A CG  1 
ATOM   2705 C CD1 . LEU A  1 341 ? -37.587 -26.481 -0.075  1.00 10.63  ? 368  LEU A CD1 1 
ATOM   2706 C CD2 . LEU A  1 341 ? -36.433 -28.212 -1.421  1.00 14.06  ? 368  LEU A CD2 1 
ATOM   2707 N N   . LEU A  1 342 ? -35.915 -23.894 0.973   1.00 12.19  ? 369  LEU A N   1 
ATOM   2708 C CA  . LEU A  1 342 ? -35.393 -23.309 2.203   1.00 10.09  ? 369  LEU A CA  1 
ATOM   2709 C C   . LEU A  1 342 ? -35.499 -24.263 3.391   1.00 12.18  ? 369  LEU A C   1 
ATOM   2710 O O   . LEU A  1 342 ? -34.798 -24.097 4.386   1.00 11.95  ? 369  LEU A O   1 
ATOM   2711 C CB  . LEU A  1 342 ? -36.167 -22.034 2.535   1.00 9.55   ? 369  LEU A CB  1 
ATOM   2712 C CG  . LEU A  1 342 ? -35.540 -20.668 2.278   1.00 7.95   ? 369  LEU A CG  1 
ATOM   2713 C CD1 . LEU A  1 342 ? -34.826 -20.652 0.955   1.00 8.41   ? 369  LEU A CD1 1 
ATOM   2714 C CD2 . LEU A  1 342 ? -36.607 -19.584 2.317   1.00 8.11   ? 369  LEU A CD2 1 
ATOM   2715 N N   . SER A  1 343 ? -36.387 -25.249 3.298   1.00 13.47  ? 370  SER A N   1 
ATOM   2716 C CA  . SER A  1 343 ? -36.671 -26.114 4.437   1.00 11.78  ? 370  SER A CA  1 
ATOM   2717 C C   . SER A  1 343 ? -37.302 -27.442 4.044   1.00 10.96  ? 370  SER A C   1 
ATOM   2718 O O   . SER A  1 343 ? -38.523 -27.573 4.050   1.00 12.39  ? 370  SER A O   1 
ATOM   2719 C CB  . SER A  1 343 ? -37.588 -25.393 5.433   1.00 13.40  ? 370  SER A CB  1 
ATOM   2720 O OG  . SER A  1 343 ? -38.071 -26.283 6.434   1.00 11.78  ? 370  SER A OG  1 
ATOM   2721 N N   . LEU A  1 344 ? -36.469 -28.422 3.705   1.00 9.12   ? 371  LEU A N   1 
ATOM   2722 C CA  . LEU A  1 344 ? -36.949 -29.780 3.512   1.00 8.37   ? 371  LEU A CA  1 
ATOM   2723 C C   . LEU A  1 344 ? -37.149 -30.395 4.882   1.00 7.23   ? 371  LEU A C   1 
ATOM   2724 O O   . LEU A  1 344 ? -36.464 -30.036 5.829   1.00 8.37   ? 371  LEU A O   1 
ATOM   2725 C CB  . LEU A  1 344 ? -35.966 -30.606 2.685   1.00 7.88   ? 371  LEU A CB  1 
ATOM   2726 C CG  . LEU A  1 344 ? -36.344 -32.060 2.377   1.00 9.33   ? 371  LEU A CG  1 
ATOM   2727 C CD1 . LEU A  1 344 ? -37.791 -32.190 1.940   1.00 7.72   ? 371  LEU A CD1 1 
ATOM   2728 C CD2 . LEU A  1 344 ? -35.431 -32.634 1.306   1.00 9.05   ? 371  LEU A CD2 1 
ATOM   2729 N N   . ASP A  1 345 ? -38.107 -31.302 4.991   1.00 7.90   ? 372  ASP A N   1 
ATOM   2730 C CA  . ASP A  1 345 ? -38.426 -31.917 6.266   1.00 8.84   ? 372  ASP A CA  1 
ATOM   2731 C C   . ASP A  1 345 ? -38.911 -33.340 6.043   1.00 9.02   ? 372  ASP A C   1 
ATOM   2732 O O   . ASP A  1 345 ? -40.085 -33.576 5.757   1.00 9.63   ? 372  ASP A O   1 
ATOM   2733 C CB  . ASP A  1 345 ? -39.476 -31.090 7.011   1.00 8.61   ? 372  ASP A CB  1 
ATOM   2734 C CG  . ASP A  1 345 ? -40.052 -31.817 8.209   1.00 10.15  ? 372  ASP A CG  1 
ATOM   2735 O OD1 . ASP A  1 345 ? -39.312 -32.584 8.860   1.00 9.65   ? 372  ASP A OD1 1 
ATOM   2736 O OD2 . ASP A  1 345 ? -41.253 -31.623 8.495   1.00 11.35  1 372  ASP A OD2 1 
ATOM   2737 N N   . LEU A  1 346 ? -37.985 -34.282 6.173   1.00 8.62   ? 373  LEU A N   1 
ATOM   2738 C CA  . LEU A  1 346 ? -38.278 -35.686 5.959   1.00 7.81   ? 373  LEU A CA  1 
ATOM   2739 C C   . LEU A  1 346 ? -38.344 -36.427 7.281   1.00 8.43   ? 373  LEU A C   1 
ATOM   2740 O O   . LEU A  1 346 ? -38.057 -37.618 7.345   1.00 10.23  ? 373  LEU A O   1 
ATOM   2741 C CB  . LEU A  1 346 ? -37.211 -36.307 5.067   1.00 6.26   ? 373  LEU A CB  1 
ATOM   2742 C CG  . LEU A  1 346 ? -37.189 -35.797 3.632   1.00 7.64   ? 373  LEU A CG  1 
ATOM   2743 C CD1 . LEU A  1 346 ? -35.869 -36.126 2.978   1.00 7.09   ? 373  LEU A CD1 1 
ATOM   2744 C CD2 . LEU A  1 346 ? -38.331 -36.416 2.860   1.00 9.91   ? 373  LEU A CD2 1 
ATOM   2745 N N   . SER A  1 347 ? -38.721 -35.719 8.337   1.00 7.35   ? 374  SER A N   1 
ATOM   2746 C CA  . SER A  1 347 ? -38.847 -36.337 9.648   1.00 11.01  ? 374  SER A CA  1 
ATOM   2747 C C   . SER A  1 347 ? -39.864 -37.487 9.667   1.00 16.19  ? 374  SER A C   1 
ATOM   2748 O O   . SER A  1 347 ? -40.903 -37.427 9.008   1.00 13.30  ? 374  SER A O   1 
ATOM   2749 C CB  . SER A  1 347 ? -39.203 -35.285 10.697  1.00 12.90  ? 374  SER A CB  1 
ATOM   2750 O OG  . SER A  1 347 ? -40.100 -34.329 10.163  1.00 12.63  ? 374  SER A OG  1 
ATOM   2751 N N   . ASN A  1 348 ? -39.537 -38.533 10.422  1.00 18.26  ? 375  ASN A N   1 
ATOM   2752 C CA  . ASN A  1 348 ? -40.385 -39.720 10.563  1.00 15.32  ? 375  ASN A CA  1 
ATOM   2753 C C   . ASN A  1 348 ? -40.702 -40.441 9.259   1.00 15.63  ? 375  ASN A C   1 
ATOM   2754 O O   . ASN A  1 348 ? -41.809 -40.349 8.737   1.00 17.81  ? 375  ASN A O   1 
ATOM   2755 C CB  . ASN A  1 348 ? -41.673 -39.391 11.312  1.00 14.14  ? 375  ASN A CB  1 
ATOM   2756 C CG  . ASN A  1 348 ? -41.409 -38.780 12.661  1.00 18.70  ? 375  ASN A CG  1 
ATOM   2757 O OD1 . ASN A  1 348 ? -41.351 -37.556 12.798  1.00 22.33  ? 375  ASN A OD1 1 
ATOM   2758 N ND2 . ASN A  1 348 ? -41.236 -39.627 13.671  1.00 16.32  ? 375  ASN A ND2 1 
ATOM   2759 N N   . ASN A  1 349 ? -39.715 -41.150 8.731   1.00 17.68  ? 376  ASN A N   1 
ATOM   2760 C CA  . ASN A  1 349 ? -39.934 -42.049 7.611   1.00 18.62  ? 376  ASN A CA  1 
ATOM   2761 C C   . ASN A  1 349 ? -39.131 -43.317 7.846   1.00 21.15  ? 376  ASN A C   1 
ATOM   2762 O O   . ASN A  1 349 ? -38.639 -43.558 8.951   1.00 19.23  ? 376  ASN A O   1 
ATOM   2763 C CB  . ASN A  1 349 ? -39.520 -41.398 6.290   1.00 15.80  ? 376  ASN A CB  1 
ATOM   2764 C CG  . ASN A  1 349 ? -40.439 -40.263 5.878   1.00 15.97  ? 376  ASN A CG  1 
ATOM   2765 O OD1 . ASN A  1 349 ? -41.193 -40.385 4.916   1.00 16.55  ? 376  ASN A OD1 1 
ATOM   2766 N ND2 . ASN A  1 349 ? -40.375 -39.150 6.599   1.00 13.91  ? 376  ASN A ND2 1 
ATOM   2767 N N   . ARG A  1 350 ? -39.005 -44.130 6.808   1.00 21.61  ? 377  ARG A N   1 
ATOM   2768 C CA  . ARG A  1 350 ? -38.139 -45.294 6.869   1.00 25.69  ? 377  ARG A CA  1 
ATOM   2769 C C   . ARG A  1 350 ? -36.936 -45.033 5.963   1.00 23.34  ? 377  ARG A C   1 
ATOM   2770 O O   . ARG A  1 350 ? -36.392 -45.949 5.340   1.00 22.39  ? 377  ARG A O   1 
ATOM   2771 C CB  . ARG A  1 350 ? -38.892 -46.553 6.433   1.00 27.00  ? 377  ARG A CB  1 
ATOM   2772 C CG  . ARG A  1 350 ? -40.342 -46.610 6.896   1.00 25.51  ? 377  ARG A CG  1 
ATOM   2773 C CD  . ARG A  1 350 ? -40.463 -46.671 8.411   1.00 32.75  ? 377  ARG A CD  1 
ATOM   2774 N NE  . ARG A  1 350 ? -41.860 -46.651 8.853   1.00 46.47  ? 377  ARG A NE  1 
ATOM   2775 C CZ  . ARG A  1 350 ? -42.574 -47.730 9.172   1.00 45.25  ? 377  ARG A CZ  1 
ATOM   2776 N NH1 . ARG A  1 350 ? -43.835 -47.597 9.563   1.00 39.05  1 377  ARG A NH1 1 
ATOM   2777 N NH2 . ARG A  1 350 ? -42.033 -48.942 9.107   1.00 39.18  ? 377  ARG A NH2 1 
ATOM   2778 N N   . LEU A  1 351 ? -36.539 -43.765 5.892   1.00 18.30  ? 378  LEU A N   1 
ATOM   2779 C CA  . LEU A  1 351 ? -35.420 -43.355 5.059   1.00 16.82  ? 378  LEU A CA  1 
ATOM   2780 C C   . LEU A  1 351 ? -34.155 -44.073 5.474   1.00 16.22  ? 378  LEU A C   1 
ATOM   2781 O O   . LEU A  1 351 ? -33.718 -43.947 6.611   1.00 18.49  ? 378  LEU A O   1 
ATOM   2782 C CB  . LEU A  1 351 ? -35.201 -41.850 5.157   1.00 14.31  ? 378  LEU A CB  1 
ATOM   2783 C CG  . LEU A  1 351 ? -36.106 -40.968 4.306   1.00 12.43  ? 378  LEU A CG  1 
ATOM   2784 C CD1 . LEU A  1 351 ? -35.799 -39.525 4.593   1.00 11.22  ? 378  LEU A CD1 1 
ATOM   2785 C CD2 . LEU A  1 351 ? -35.899 -41.262 2.838   1.00 13.05  ? 378  LEU A CD2 1 
ATOM   2786 N N   . THR A  1 352 ? -33.573 -44.828 4.549   1.00 20.46  ? 379  THR A N   1 
ATOM   2787 C CA  . THR A  1 352 ? -32.343 -45.562 4.824   1.00 19.76  ? 379  THR A CA  1 
ATOM   2788 C C   . THR A  1 352 ? -31.155 -45.006 4.041   1.00 20.56  ? 379  THR A C   1 
ATOM   2789 O O   . THR A  1 352 ? -30.003 -45.238 4.406   1.00 23.94  ? 379  THR A O   1 
ATOM   2790 C CB  . THR A  1 352 ? -32.504 -47.066 4.538   1.00 19.03  ? 379  THR A CB  1 
ATOM   2791 O OG1 . THR A  1 352 ? -32.903 -47.262 3.175   1.00 17.46  ? 379  THR A OG1 1 
ATOM   2792 C CG2 . THR A  1 352 ? -33.550 -47.657 5.461   1.00 17.48  ? 379  THR A CG2 1 
ATOM   2793 N N   . HIS A  1 353 ? -31.438 -44.265 2.974   1.00 18.81  ? 380  HIS A N   1 
ATOM   2794 C CA  . HIS A  1 353 ? -30.387 -43.622 2.195   1.00 19.15  ? 380  HIS A CA  1 
ATOM   2795 C C   . HIS A  1 353 ? -30.925 -42.511 1.300   1.00 21.24  ? 380  HIS A C   1 
ATOM   2796 O O   . HIS A  1 353 ? -32.020 -42.609 0.758   1.00 25.53  ? 380  HIS A O   1 
ATOM   2797 C CB  . HIS A  1 353 ? -29.643 -44.654 1.352   1.00 23.85  ? 380  HIS A CB  1 
ATOM   2798 C CG  . HIS A  1 353 ? -30.530 -45.438 0.436   1.00 31.48  ? 380  HIS A CG  1 
ATOM   2799 N ND1 . HIS A  1 353 ? -30.763 -45.067 -0.872  1.00 39.06  ? 380  HIS A ND1 1 
ATOM   2800 C CD2 . HIS A  1 353 ? -31.238 -46.575 0.636   1.00 27.27  ? 380  HIS A CD2 1 
ATOM   2801 C CE1 . HIS A  1 353 ? -31.574 -45.943 -1.438  1.00 41.32  ? 380  HIS A CE1 1 
ATOM   2802 N NE2 . HIS A  1 353 ? -31.877 -46.869 -0.545  1.00 37.43  ? 380  HIS A NE2 1 
ATOM   2803 N N   . LEU A  1 354 ? -30.140 -41.455 1.144   1.00 20.12  ? 381  LEU A N   1 
ATOM   2804 C CA  . LEU A  1 354 ? -30.512 -40.340 0.289   1.00 18.71  ? 381  LEU A CA  1 
ATOM   2805 C C   . LEU A  1 354 ? -29.431 -40.139 -0.751  1.00 23.14  ? 381  LEU A C   1 
ATOM   2806 O O   . LEU A  1 354 ? -28.385 -39.578 -0.432  1.00 24.53  ? 381  LEU A O   1 
ATOM   2807 C CB  . LEU A  1 354 ? -30.607 -39.060 1.112   1.00 20.47  ? 381  LEU A CB  1 
ATOM   2808 C CG  . LEU A  1 354 ? -31.329 -39.109 2.453   1.00 20.07  ? 381  LEU A CG  1 
ATOM   2809 C CD1 . LEU A  1 354 ? -30.876 -37.948 3.323   1.00 13.31  ? 381  LEU A CD1 1 
ATOM   2810 C CD2 . LEU A  1 354 ? -32.829 -39.067 2.234   1.00 18.71  ? 381  LEU A CD2 1 
ATOM   2811 N N   . PRO A  1 355 ? -29.675 -40.601 -1.989  1.00 25.82  ? 382  PRO A N   1 
ATOM   2812 C CA  . PRO A  1 355 ? -28.806 -40.429 -3.156  1.00 31.38  ? 382  PRO A CA  1 
ATOM   2813 C C   . PRO A  1 355 ? -27.943 -39.176 -3.063  1.00 29.88  ? 382  PRO A C   1 
ATOM   2814 O O   . PRO A  1 355 ? -28.488 -38.076 -2.953  1.00 26.35  ? 382  PRO A O   1 
ATOM   2815 C CB  . PRO A  1 355 ? -29.814 -40.294 -4.296  1.00 30.70  ? 382  PRO A CB  1 
ATOM   2816 C CG  . PRO A  1 355 ? -31.027 -41.101 -3.826  1.00 29.41  ? 382  PRO A CG  1 
ATOM   2817 C CD  . PRO A  1 355 ? -30.863 -41.390 -2.343  1.00 25.75  ? 382  PRO A CD  1 
ATOM   2818 N N   . ASP A  1 356 ? -26.622 -39.355 -3.093  1.00 28.90  ? 383  ASP A N   1 
ATOM   2819 C CA  . ASP A  1 356 ? -25.657 -38.294 -2.779  1.00 28.43  ? 383  ASP A CA  1 
ATOM   2820 C C   . ASP A  1 356 ? -25.843 -36.985 -3.544  1.00 31.72  ? 383  ASP A C   1 
ATOM   2821 O O   . ASP A  1 356 ? -25.291 -35.952 -3.160  1.00 29.72  ? 383  ASP A O   1 
ATOM   2822 C CB  . ASP A  1 356 ? -24.227 -38.799 -2.979  1.00 27.59  ? 383  ASP A CB  1 
ATOM   2823 C CG  . ASP A  1 356 ? -23.777 -39.722 -1.870  1.00 34.59  ? 383  ASP A CG  1 
ATOM   2824 O OD1 . ASP A  1 356 ? -24.083 -39.430 -0.694  1.00 34.25  ? 383  ASP A OD1 1 
ATOM   2825 O OD2 . ASP A  1 356 ? -23.119 -40.740 -2.174  1.00 38.77  1 383  ASP A OD2 1 
ATOM   2826 N N   . SER A  1 357 ? -26.618 -37.038 -4.622  1.00 34.37  ? 384  SER A N   1 
ATOM   2827 C CA  . SER A  1 357 ? -26.862 -35.872 -5.459  1.00 26.62  ? 384  SER A CA  1 
ATOM   2828 C C   . SER A  1 357 ? -28.222 -35.258 -5.182  1.00 26.19  ? 384  SER A C   1 
ATOM   2829 O O   . SER A  1 357 ? -28.700 -34.453 -5.973  1.00 25.99  ? 384  SER A O   1 
ATOM   2830 C CB  . SER A  1 357 ? -26.796 -36.270 -6.930  1.00 26.97  ? 384  SER A CB  1 
ATOM   2831 O OG  . SER A  1 357 ? -27.751 -37.282 -7.216  1.00 31.20  ? 384  SER A OG  1 
ATOM   2832 N N   . LEU A  1 358 ? -28.851 -35.645 -4.073  1.00 28.75  ? 385  LEU A N   1 
ATOM   2833 C CA  . LEU A  1 358 ? -30.211 -35.188 -3.778  1.00 29.77  ? 385  LEU A CA  1 
ATOM   2834 C C   . LEU A  1 358 ? -30.247 -33.686 -3.560  1.00 23.97  ? 385  LEU A C   1 
ATOM   2835 O O   . LEU A  1 358 ? -31.019 -32.970 -4.200  1.00 22.09  ? 385  LEU A O   1 
ATOM   2836 C CB  . LEU A  1 358 ? -30.795 -35.913 -2.563  1.00 25.62  ? 385  LEU A CB  1 
ATOM   2837 C CG  . LEU A  1 358 ? -32.237 -35.546 -2.198  1.00 20.28  ? 385  LEU A CG  1 
ATOM   2838 C CD1 . LEU A  1 358 ? -33.165 -35.721 -3.383  1.00 18.56  ? 385  LEU A CD1 1 
ATOM   2839 C CD2 . LEU A  1 358 ? -32.718 -36.382 -1.031  1.00 20.67  ? 385  LEU A CD2 1 
ATOM   2840 N N   . PHE A  1 359 ? -29.396 -33.211 -2.662  1.00 20.26  ? 386  PHE A N   1 
ATOM   2841 C CA  . PHE A  1 359 ? -29.290 -31.786 -2.418  1.00 25.30  ? 386  PHE A CA  1 
ATOM   2842 C C   . PHE A  1 359 ? -28.189 -31.185 -3.283  1.00 27.24  ? 386  PHE A C   1 
ATOM   2843 O O   . PHE A  1 359 ? -27.481 -30.269 -2.860  1.00 29.17  ? 386  PHE A O   1 
ATOM   2844 C CB  . PHE A  1 359 ? -29.011 -31.521 -0.941  1.00 27.13  ? 386  PHE A CB  1 
ATOM   2845 C CG  . PHE A  1 359 ? -29.817 -32.380 -0.013  1.00 25.43  ? 386  PHE A CG  1 
ATOM   2846 C CD1 . PHE A  1 359 ? -31.176 -32.190 0.121   1.00 22.15  ? 386  PHE A CD1 1 
ATOM   2847 C CD2 . PHE A  1 359 ? -29.211 -33.377 0.729   1.00 26.37  ? 386  PHE A CD2 1 
ATOM   2848 C CE1 . PHE A  1 359 ? -31.914 -32.980 0.977   1.00 21.53  ? 386  PHE A CE1 1 
ATOM   2849 C CE2 . PHE A  1 359 ? -29.948 -34.169 1.584   1.00 22.19  ? 386  PHE A CE2 1 
ATOM   2850 C CZ  . PHE A  1 359 ? -31.298 -33.970 1.708   1.00 17.27  ? 386  PHE A CZ  1 
ATOM   2851 N N   . ALA A  1 360 ? -28.049 -31.712 -4.497  1.00 24.23  ? 387  ALA A N   1 
ATOM   2852 C CA  . ALA A  1 360 ? -27.053 -31.220 -5.439  1.00 22.95  ? 387  ALA A CA  1 
ATOM   2853 C C   . ALA A  1 360 ? -27.282 -29.753 -5.756  1.00 23.41  ? 387  ALA A C   1 
ATOM   2854 O O   . ALA A  1 360 ? -26.385 -28.927 -5.605  1.00 23.34  ? 387  ALA A O   1 
ATOM   2855 C CB  . ALA A  1 360 ? -27.074 -32.041 -6.719  1.00 21.36  ? 387  ALA A CB  1 
ATOM   2856 N N   . HIS A  1 361 ? -28.496 -29.428 -6.183  1.00 26.76  ? 388  HIS A N   1 
ATOM   2857 C CA  . HIS A  1 361 ? -28.782 -28.084 -6.658  1.00 26.90  ? 388  HIS A CA  1 
ATOM   2858 C C   . HIS A  1 361 ? -29.495 -27.219 -5.607  1.00 23.33  ? 388  HIS A C   1 
ATOM   2859 O O   . HIS A  1 361 ? -29.567 -26.001 -5.762  1.00 22.74  ? 388  HIS A O   1 
ATOM   2860 C CB  . HIS A  1 361 ? -29.583 -28.131 -7.970  1.00 24.67  ? 388  HIS A CB  1 
ATOM   2861 C CG  . HIS A  1 361 ? -28.984 -29.014 -9.030  1.00 26.54  ? 388  HIS A CG  1 
ATOM   2862 N ND1 . HIS A  1 361 ? -28.920 -30.387 -8.913  1.00 26.01  ? 388  HIS A ND1 1 
ATOM   2863 C CD2 . HIS A  1 361 ? -28.444 -28.717 -10.237 1.00 29.20  ? 388  HIS A CD2 1 
ATOM   2864 C CE1 . HIS A  1 361 ? -28.358 -30.897 -9.995  1.00 23.80  ? 388  HIS A CE1 1 
ATOM   2865 N NE2 . HIS A  1 361 ? -28.060 -29.904 -10.815 1.00 28.44  ? 388  HIS A NE2 1 
ATOM   2866 N N   . THR A  1 362 ? -29.997 -27.832 -4.534  1.00 18.81  ? 389  THR A N   1 
ATOM   2867 C CA  . THR A  1 362 ? -30.742 -27.090 -3.508  1.00 21.22  ? 389  THR A CA  1 
ATOM   2868 C C   . THR A  1 362 ? -29.857 -26.088 -2.759  1.00 23.45  ? 389  THR A C   1 
ATOM   2869 O O   . THR A  1 362 ? -29.743 -26.129 -1.533  1.00 22.33  ? 389  THR A O   1 
ATOM   2870 C CB  . THR A  1 362 ? -31.442 -28.030 -2.490  1.00 20.30  ? 389  THR A CB  1 
ATOM   2871 O OG1 . THR A  1 362 ? -30.465 -28.753 -1.729  1.00 19.82  ? 389  THR A OG1 1 
ATOM   2872 C CG2 . THR A  1 362 ? -32.352 -29.012 -3.204  1.00 19.00  ? 389  THR A CG2 1 
ATOM   2873 N N   . THR A  1 363 ? -29.270 -25.166 -3.514  1.00 26.08  ? 390  THR A N   1 
ATOM   2874 C CA  . THR A  1 363 ? -28.173 -24.320 -3.048  1.00 25.98  ? 390  THR A CA  1 
ATOM   2875 C C   . THR A  1 363 ? -28.531 -23.404 -1.886  1.00 25.85  ? 390  THR A C   1 
ATOM   2876 O O   . THR A  1 363 ? -27.641 -22.929 -1.181  1.00 22.69  ? 390  THR A O   1 
ATOM   2877 C CB  . THR A  1 363 ? -27.643 -23.431 -4.195  1.00 30.05  ? 390  THR A CB  1 
ATOM   2878 O OG1 . THR A  1 363 ? -27.980 -24.017 -5.462  1.00 28.41  ? 390  THR A OG1 1 
ATOM   2879 C CG2 . THR A  1 363 ? -26.141 -23.268 -4.086  1.00 37.33  ? 390  THR A CG2 1 
ATOM   2880 N N   . ASN A  1 364 ? -29.825 -23.148 -1.698  1.00 26.99  ? 391  ASN A N   1 
ATOM   2881 C CA  . ASN A  1 364 ? -30.282 -22.166 -0.712  1.00 26.00  ? 391  ASN A CA  1 
ATOM   2882 C C   . ASN A  1 364 ? -30.843 -22.785 0.560   1.00 20.11  ? 391  ASN A C   1 
ATOM   2883 O O   . ASN A  1 364 ? -31.175 -22.074 1.519   1.00 12.84  ? 391  ASN A O   1 
ATOM   2884 C CB  . ASN A  1 364 ? -31.309 -21.216 -1.331  1.00 24.82  ? 391  ASN A CB  1 
ATOM   2885 C CG  . ASN A  1 364 ? -30.666 -20.006 -1.974  1.00 33.58  ? 391  ASN A CG  1 
ATOM   2886 O OD1 . ASN A  1 364 ? -30.662 -18.914 -1.402  1.00 34.25  ? 391  ASN A OD1 1 
ATOM   2887 N ND2 . ASN A  1 364 ? -30.101 -20.195 -3.159  1.00 39.19  ? 391  ASN A ND2 1 
ATOM   2888 N N   . LEU A  1 365 ? -30.932 -24.113 0.546   1.00 18.70  ? 392  LEU A N   1 
ATOM   2889 C CA  . LEU A  1 365 ? -31.438 -24.895 1.670   1.00 15.24  ? 392  LEU A CA  1 
ATOM   2890 C C   . LEU A  1 365 ? -30.885 -24.399 3.007   1.00 15.23  ? 392  LEU A C   1 
ATOM   2891 O O   . LEU A  1 365 ? -29.678 -24.234 3.164   1.00 23.40  ? 392  LEU A O   1 
ATOM   2892 C CB  . LEU A  1 365 ? -31.100 -26.373 1.460   1.00 13.52  ? 392  LEU A CB  1 
ATOM   2893 C CG  . LEU A  1 365 ? -31.707 -27.370 2.438   1.00 11.47  ? 392  LEU A CG  1 
ATOM   2894 C CD1 . LEU A  1 365 ? -33.169 -27.074 2.621   1.00 12.17  ? 392  LEU A CD1 1 
ATOM   2895 C CD2 . LEU A  1 365 ? -31.524 -28.776 1.917   1.00 14.64  ? 392  LEU A CD2 1 
ATOM   2896 N N   . THR A  1 366 ? -31.775 -24.140 3.957   1.00 11.86  ? 393  THR A N   1 
ATOM   2897 C CA  . THR A  1 366 ? -31.376 -23.601 5.248   1.00 11.18  ? 393  THR A CA  1 
ATOM   2898 C C   . THR A  1 366 ? -31.609 -24.591 6.376   1.00 12.42  ? 393  THR A C   1 
ATOM   2899 O O   . THR A  1 366 ? -30.672 -25.011 7.043   1.00 16.66  ? 393  THR A O   1 
ATOM   2900 C CB  . THR A  1 366 ? -32.119 -22.305 5.551   1.00 12.56  ? 393  THR A CB  1 
ATOM   2901 O OG1 . THR A  1 366 ? -31.694 -21.301 4.620   1.00 14.06  ? 393  THR A OG1 1 
ATOM   2902 C CG2 . THR A  1 366 ? -31.838 -21.844 6.969   1.00 12.55  ? 393  THR A CG2 1 
ATOM   2903 N N   . ASP A  1 367 ? -32.864 -24.953 6.599   1.00 12.01  ? 394  ASP A N   1 
ATOM   2904 C CA  . ASP A  1 367 ? -33.184 -25.951 7.608   1.00 12.87  ? 394  ASP A CA  1 
ATOM   2905 C C   . ASP A  1 367 ? -33.452 -27.300 6.960   1.00 11.92  ? 394  ASP A C   1 
ATOM   2906 O O   . ASP A  1 367 ? -34.354 -27.423 6.142   1.00 12.62  ? 394  ASP A O   1 
ATOM   2907 C CB  . ASP A  1 367 ? -34.412 -25.534 8.418   1.00 13.70  ? 394  ASP A CB  1 
ATOM   2908 C CG  . ASP A  1 367 ? -34.142 -24.359 9.339   1.00 13.47  ? 394  ASP A CG  1 
ATOM   2909 O OD1 . ASP A  1 367 ? -33.987 -23.223 8.837   1.00 16.77  ? 394  ASP A OD1 1 
ATOM   2910 O OD2 . ASP A  1 367 ? -34.112 -24.572 10.569  1.00 9.93   1 394  ASP A OD2 1 
ATOM   2911 N N   . LEU A  1 368 ? -32.669 -28.309 7.324   1.00 11.76  ? 395  LEU A N   1 
ATOM   2912 C CA  . LEU A  1 368 ? -32.967 -29.676 6.921   1.00 8.61   ? 395  LEU A CA  1 
ATOM   2913 C C   . LEU A  1 368 ? -33.282 -30.517 8.148   1.00 9.04   ? 395  LEU A C   1 
ATOM   2914 O O   . LEU A  1 368 ? -32.620 -30.407 9.173   1.00 11.32  ? 395  LEU A O   1 
ATOM   2915 C CB  . LEU A  1 368 ? -31.815 -30.295 6.131   1.00 9.11   ? 395  LEU A CB  1 
ATOM   2916 C CG  . LEU A  1 368 ? -32.065 -31.722 5.633   1.00 11.10  ? 395  LEU A CG  1 
ATOM   2917 C CD1 . LEU A  1 368 ? -33.407 -31.824 4.933   1.00 11.15  ? 395  LEU A CD1 1 
ATOM   2918 C CD2 . LEU A  1 368 ? -30.967 -32.184 4.697   1.00 13.78  ? 395  LEU A CD2 1 
ATOM   2919 N N   . ARG A  1 369 ? -34.317 -31.340 8.042   1.00 9.97   ? 396  ARG A N   1 
ATOM   2920 C CA  . ARG A  1 369 ? -34.718 -32.223 9.127   1.00 10.71  ? 396  ARG A CA  1 
ATOM   2921 C C   . ARG A  1 369 ? -34.821 -33.651 8.603   1.00 8.94   ? 396  ARG A C   1 
ATOM   2922 O O   . ARG A  1 369 ? -35.414 -33.893 7.557   1.00 9.02   ? 396  ARG A O   1 
ATOM   2923 C CB  . ARG A  1 369 ? -36.044 -31.759 9.733   1.00 10.29  ? 396  ARG A CB  1 
ATOM   2924 C CG  . ARG A  1 369 ? -36.019 -30.317 10.209  1.00 11.10  ? 396  ARG A CG  1 
ATOM   2925 C CD  . ARG A  1 369 ? -37.295 -29.942 10.936  1.00 16.47  ? 396  ARG A CD  1 
ATOM   2926 N NE  . ARG A  1 369 ? -37.520 -30.782 12.112  1.00 30.39  ? 396  ARG A NE  1 
ATOM   2927 C CZ  . ARG A  1 369 ? -36.987 -30.560 13.313  1.00 28.72  ? 396  ARG A CZ  1 
ATOM   2928 N NH1 . ARG A  1 369 ? -37.256 -31.383 14.324  1.00 18.86  1 396  ARG A NH1 1 
ATOM   2929 N NH2 . ARG A  1 369 ? -36.185 -29.518 13.504  1.00 23.91  ? 396  ARG A NH2 1 
ATOM   2930 N N   . LEU A  1 370 ? -34.221 -34.589 9.326   1.00 9.36   ? 397  LEU A N   1 
ATOM   2931 C CA  . LEU A  1 370 ? -34.134 -35.971 8.878   1.00 7.61   ? 397  LEU A CA  1 
ATOM   2932 C C   . LEU A  1 370 ? -34.333 -36.902 10.061  1.00 10.13  ? 397  LEU A C   1 
ATOM   2933 O O   . LEU A  1 370 ? -34.183 -38.118 9.941   1.00 10.72  ? 397  LEU A O   1 
ATOM   2934 C CB  . LEU A  1 370 ? -32.768 -36.230 8.251   1.00 7.28   ? 397  LEU A CB  1 
ATOM   2935 C CG  . LEU A  1 370 ? -32.427 -35.472 6.972   1.00 7.16   ? 397  LEU A CG  1 
ATOM   2936 C CD1 . LEU A  1 370 ? -30.948 -35.175 6.877   1.00 6.35   ? 397  LEU A CD1 1 
ATOM   2937 C CD2 . LEU A  1 370 ? -32.863 -36.291 5.789   1.00 11.10  ? 397  LEU A CD2 1 
ATOM   2938 N N   . GLU A  1 371 ? -34.674 -36.319 11.206  1.00 9.59   ? 398  GLU A N   1 
ATOM   2939 C CA  . GLU A  1 371 ? -34.835 -37.080 12.438  1.00 11.10  ? 398  GLU A CA  1 
ATOM   2940 C C   . GLU A  1 371 ? -35.912 -38.166 12.377  1.00 14.02  ? 398  GLU A C   1 
ATOM   2941 O O   . GLU A  1 371 ? -36.950 -38.016 11.727  1.00 11.80  ? 398  GLU A O   1 
ATOM   2942 C CB  . GLU A  1 371 ? -35.097 -36.149 13.623  1.00 12.22  ? 398  GLU A CB  1 
ATOM   2943 C CG  . GLU A  1 371 ? -36.421 -35.412 13.564  1.00 17.02  ? 398  GLU A CG  1 
ATOM   2944 C CD  . GLU A  1 371 ? -36.357 -34.139 12.740  1.00 14.11  ? 398  GLU A CD  1 
ATOM   2945 O OE1 . GLU A  1 371 ? -35.402 -33.977 11.947  1.00 12.29  ? 398  GLU A OE1 1 
ATOM   2946 O OE2 . GLU A  1 371 ? -37.266 -33.298 12.898  1.00 12.11  1 398  GLU A OE2 1 
ATOM   2947 N N   . ASP A  1 372 ? -35.639 -39.258 13.080  1.00 18.71  ? 399  ASP A N   1 
ATOM   2948 C CA  . ASP A  1 372 ? -36.505 -40.433 13.111  1.00 17.68  ? 399  ASP A CA  1 
ATOM   2949 C C   . ASP A  1 372 ? -36.588 -41.136 11.763  1.00 14.79  ? 399  ASP A C   1 
ATOM   2950 O O   . ASP A  1 372 ? -37.645 -41.245 11.144  1.00 13.93  ? 399  ASP A O   1 
ATOM   2951 C CB  . ASP A  1 372 ? -37.868 -40.104 13.714  1.00 15.32  ? 399  ASP A CB  1 
ATOM   2952 C CG  . ASP A  1 372 ? -37.757 -39.710 15.168  1.00 13.63  ? 399  ASP A CG  1 
ATOM   2953 O OD1 . ASP A  1 372 ? -37.779 -40.617 16.029  1.00 11.61  ? 399  ASP A OD1 1 
ATOM   2954 O OD2 . ASP A  1 372 ? -37.608 -38.500 15.444  1.00 13.03  1 399  ASP A OD2 1 
ATOM   2955 N N   . ASN A  1 373 ? -35.429 -41.607 11.326  1.00 13.97  ? 400  ASN A N   1 
ATOM   2956 C CA  . ASN A  1 373 ? -35.320 -42.440 10.149  1.00 15.42  ? 400  ASN A CA  1 
ATOM   2957 C C   . ASN A  1 373 ? -34.299 -43.530 10.404  1.00 13.28  ? 400  ASN A C   1 
ATOM   2958 O O   . ASN A  1 373 ? -33.821 -43.689 11.524  1.00 15.66  ? 400  ASN A O   1 
ATOM   2959 C CB  . ASN A  1 373 ? -34.924 -41.608 8.937   1.00 15.37  ? 400  ASN A CB  1 
ATOM   2960 C CG  . ASN A  1 373 ? -36.021 -40.670 8.500   1.00 14.35  ? 400  ASN A CG  1 
ATOM   2961 O OD1 . ASN A  1 373 ? -36.860 -41.024 7.678   1.00 13.33  ? 400  ASN A OD1 1 
ATOM   2962 N ND2 . ASN A  1 373 ? -36.027 -39.468 9.055   1.00 12.99  ? 400  ASN A ND2 1 
ATOM   2963 N N   . LEU A  1 374 ? -33.977 -44.287 9.368   1.00 12.34  ? 401  LEU A N   1 
ATOM   2964 C CA  . LEU A  1 374 ? -33.025 -45.371 9.503   1.00 12.36  ? 401  LEU A CA  1 
ATOM   2965 C C   . LEU A  1 374 ? -31.781 -45.049 8.703   1.00 10.99  ? 401  LEU A C   1 
ATOM   2966 O O   . LEU A  1 374 ? -31.182 -45.927 8.082   1.00 10.13  ? 401  LEU A O   1 
ATOM   2967 C CB  . LEU A  1 374 ? -33.645 -46.676 9.022   1.00 13.15  ? 401  LEU A CB  1 
ATOM   2968 C CG  . LEU A  1 374 ? -34.993 -46.974 9.667   1.00 10.63  ? 401  LEU A CG  1 
ATOM   2969 C CD1 . LEU A  1 374 ? -35.492 -48.334 9.229   1.00 22.59  ? 401  LEU A CD1 1 
ATOM   2970 C CD2 . LEU A  1 374 ? -34.877 -46.904 11.174  1.00 10.54  ? 401  LEU A CD2 1 
ATOM   2971 N N   . LEU A  1 375 ? -31.414 -43.774 8.705   1.00 9.56   ? 402  LEU A N   1 
ATOM   2972 C CA  . LEU A  1 375 ? -30.184 -43.347 8.069   1.00 11.99  ? 402  LEU A CA  1 
ATOM   2973 C C   . LEU A  1 375 ? -29.046 -43.972 8.852   1.00 15.67  ? 402  LEU A C   1 
ATOM   2974 O O   . LEU A  1 375 ? -29.195 -44.246 10.043  1.00 17.23  ? 402  LEU A O   1 
ATOM   2975 C CB  . LEU A  1 375 ? -30.065 -41.826 8.083   1.00 11.98  ? 402  LEU A CB  1 
ATOM   2976 C CG  . LEU A  1 375 ? -31.030 -41.018 7.216   1.00 8.13   ? 402  LEU A CG  1 
ATOM   2977 C CD1 . LEU A  1 375 ? -30.640 -39.559 7.255   1.00 5.89   ? 402  LEU A CD1 1 
ATOM   2978 C CD2 . LEU A  1 375 ? -31.045 -41.525 5.787   1.00 10.91  ? 402  LEU A CD2 1 
ATOM   2979 N N   . THR A  1 376 ? -27.914 -44.207 8.199   1.00 14.01  ? 403  THR A N   1 
ATOM   2980 C CA  . THR A  1 376 ? -26.850 -44.966 8.844   1.00 12.98  ? 403  THR A CA  1 
ATOM   2981 C C   . THR A  1 376 ? -25.468 -44.343 8.749   1.00 15.10  ? 403  THR A C   1 
ATOM   2982 O O   . THR A  1 376 ? -24.494 -44.927 9.212   1.00 16.13  ? 403  THR A O   1 
ATOM   2983 C CB  . THR A  1 376 ? -26.772 -46.376 8.283   1.00 10.48  ? 403  THR A CB  1 
ATOM   2984 O OG1 . THR A  1 376 ? -26.894 -46.319 6.855   1.00 9.82   ? 403  THR A OG1 1 
ATOM   2985 C CG2 . THR A  1 376 ? -27.888 -47.218 8.862   1.00 10.49  ? 403  THR A CG2 1 
ATOM   2986 N N   . GLY A  1 377 ? -25.370 -43.166 8.154   1.00 11.21  ? 404  GLY A N   1 
ATOM   2987 C CA  . GLY A  1 377 ? -24.084 -42.512 8.087   1.00 8.97   ? 404  GLY A CA  1 
ATOM   2988 C C   . GLY A  1 377 ? -24.097 -41.368 7.115   1.00 8.76   ? 404  GLY A C   1 
ATOM   2989 O O   . GLY A  1 377 ? -24.811 -41.406 6.119   1.00 9.79   ? 404  GLY A O   1 
ATOM   2990 N N   . ILE A  1 378 ? -23.307 -40.346 7.412   1.00 8.60   ? 405  ILE A N   1 
ATOM   2991 C CA  . ILE A  1 378 ? -23.193 -39.200 6.532   1.00 9.09   ? 405  ILE A CA  1 
ATOM   2992 C C   . ILE A  1 378 ? -22.021 -39.403 5.583   1.00 10.46  ? 405  ILE A C   1 
ATOM   2993 O O   . ILE A  1 378 ? -20.904 -39.655 6.011   1.00 11.21  ? 405  ILE A O   1 
ATOM   2994 C CB  . ILE A  1 378 ? -23.029 -37.885 7.314   1.00 8.44   ? 405  ILE A CB  1 
ATOM   2995 C CG1 . ILE A  1 378 ? -24.242 -37.633 8.208   1.00 7.58   ? 405  ILE A CG1 1 
ATOM   2996 C CG2 . ILE A  1 378 ? -22.880 -36.722 6.361   1.00 11.48  ? 405  ILE A CG2 1 
ATOM   2997 C CD1 . ILE A  1 378 ? -24.138 -38.206 9.596   1.00 7.13   ? 405  ILE A CD1 1 
ATOM   2998 N N   . SER A  1 379 ? -22.294 -39.315 4.287   1.00 14.51  ? 406  SER A N   1 
ATOM   2999 C CA  . SER A  1 379 ? -21.260 -39.422 3.272   1.00 14.74  ? 406  SER A CA  1 
ATOM   3000 C C   . SER A  1 379 ? -20.534 -38.094 3.134   1.00 19.65  ? 406  SER A C   1 
ATOM   3001 O O   . SER A  1 379 ? -20.607 -37.239 4.017   1.00 19.73  ? 406  SER A O   1 
ATOM   3002 C CB  . SER A  1 379 ? -21.863 -39.831 1.928   1.00 20.14  ? 406  SER A CB  1 
ATOM   3003 O OG  . SER A  1 379 ? -22.808 -38.876 1.478   1.00 23.20  ? 406  SER A OG  1 
ATOM   3004 N N   . GLY A  1 380 ? -19.841 -37.918 2.015   1.00 21.85  ? 407  GLY A N   1 
ATOM   3005 C CA  . GLY A  1 380 ? -18.985 -36.762 1.845   1.00 23.75  ? 407  GLY A CA  1 
ATOM   3006 C C   . GLY A  1 380 ? -19.544 -35.742 0.884   1.00 26.33  ? 407  GLY A C   1 
ATOM   3007 O O   . GLY A  1 380 ? -19.213 -34.556 0.971   1.00 26.15  ? 407  GLY A O   1 
ATOM   3008 N N   . ASP A  1 381 ? -20.395 -36.207 -0.027  1.00 27.87  ? 408  ASP A N   1 
ATOM   3009 C CA  . ASP A  1 381 ? -20.973 -35.345 -1.056  1.00 28.70  ? 408  ASP A CA  1 
ATOM   3010 C C   . ASP A  1 381 ? -22.408 -34.932 -0.746  1.00 27.72  ? 408  ASP A C   1 
ATOM   3011 O O   . ASP A  1 381 ? -22.935 -34.005 -1.361  1.00 33.39  ? 408  ASP A O   1 
ATOM   3012 C CB  . ASP A  1 381 ? -20.946 -36.044 -2.414  1.00 27.55  ? 408  ASP A CB  1 
ATOM   3013 C CG  . ASP A  1 381 ? -19.587 -36.592 -2.757  1.00 33.04  ? 408  ASP A CG  1 
ATOM   3014 O OD1 . ASP A  1 381 ? -18.585 -35.863 -2.583  1.00 30.78  ? 408  ASP A OD1 1 
ATOM   3015 O OD2 . ASP A  1 381 ? -19.526 -37.759 -3.195  1.00 42.82  1 408  ASP A OD2 1 
ATOM   3016 N N   . ILE A  1 382 ? -23.038 -35.620 0.199   1.00 22.13  ? 409  ILE A N   1 
ATOM   3017 C CA  . ILE A  1 382 ? -24.445 -35.384 0.496   1.00 22.48  ? 409  ILE A CA  1 
ATOM   3018 C C   . ILE A  1 382 ? -24.743 -33.939 0.910   1.00 23.58  ? 409  ILE A C   1 
ATOM   3019 O O   . ILE A  1 382 ? -25.831 -33.434 0.643   1.00 29.81  ? 409  ILE A O   1 
ATOM   3020 C CB  . ILE A  1 382 ? -24.975 -36.367 1.566   1.00 26.73  ? 409  ILE A CB  1 
ATOM   3021 C CG1 . ILE A  1 382 ? -26.495 -36.231 1.731   1.00 22.17  ? 409  ILE A CG1 1 
ATOM   3022 C CG2 . ILE A  1 382 ? -24.250 -36.164 2.892   1.00 24.42  ? 409  ILE A CG2 1 
ATOM   3023 C CD1 . ILE A  1 382 ? -27.286 -36.543 0.478   1.00 21.23  ? 409  ILE A CD1 1 
ATOM   3024 N N   . PHE A  1 383 ? -23.780 -33.268 1.536   1.00 18.32  ? 410  PHE A N   1 
ATOM   3025 C CA  . PHE A  1 383 ? -23.995 -31.895 1.996   1.00 18.79  ? 410  PHE A CA  1 
ATOM   3026 C C   . PHE A  1 383 ? -22.984 -30.912 1.422   1.00 25.17  ? 410  PHE A C   1 
ATOM   3027 O O   . PHE A  1 383 ? -22.877 -29.774 1.884   1.00 22.42  ? 410  PHE A O   1 
ATOM   3028 C CB  . PHE A  1 383 ? -23.926 -31.835 3.513   1.00 19.91  ? 410  PHE A CB  1 
ATOM   3029 C CG  . PHE A  1 383 ? -24.880 -32.759 4.195   1.00 22.27  ? 410  PHE A CG  1 
ATOM   3030 C CD1 . PHE A  1 383 ? -26.155 -32.948 3.694   1.00 22.70  ? 410  PHE A CD1 1 
ATOM   3031 C CD2 . PHE A  1 383 ? -24.505 -33.439 5.338   1.00 20.92  ? 410  PHE A CD2 1 
ATOM   3032 C CE1 . PHE A  1 383 ? -27.035 -33.795 4.319   1.00 19.20  ? 410  PHE A CE1 1 
ATOM   3033 C CE2 . PHE A  1 383 ? -25.379 -34.284 5.964   1.00 15.99  ? 410  PHE A CE2 1 
ATOM   3034 C CZ  . PHE A  1 383 ? -26.648 -34.462 5.453   1.00 15.98  ? 410  PHE A CZ  1 
ATOM   3035 N N   . SER A  1 384 ? -22.257 -31.357 0.403   1.00 29.77  ? 411  SER A N   1 
ATOM   3036 C CA  . SER A  1 384 ? -21.135 -30.608 -0.154  1.00 27.31  ? 411  SER A CA  1 
ATOM   3037 C C   . SER A  1 384 ? -21.533 -29.377 -0.961  1.00 31.30  ? 411  SER A C   1 
ATOM   3038 O O   . SER A  1 384 ? -20.739 -28.870 -1.754  1.00 28.87  ? 411  SER A O   1 
ATOM   3039 C CB  . SER A  1 384 ? -20.301 -31.533 -1.032  1.00 26.38  ? 411  SER A CB  1 
ATOM   3040 O OG  . SER A  1 384 ? -21.132 -32.217 -1.948  1.00 24.76  ? 411  SER A OG  1 
ATOM   3041 N N   . ASN A  1 385 ? -22.759 -28.903 -0.759  1.00 41.38  ? 412  ASN A N   1 
ATOM   3042 C CA  . ASN A  1 385 ? -23.261 -27.719 -1.450  1.00 38.94  ? 412  ASN A CA  1 
ATOM   3043 C C   . ASN A  1 385 ? -24.069 -26.822 -0.522  1.00 33.34  ? 412  ASN A C   1 
ATOM   3044 O O   . ASN A  1 385 ? -24.397 -25.685 -0.864  1.00 33.61  ? 412  ASN A O   1 
ATOM   3045 C CB  . ASN A  1 385 ? -24.123 -28.123 -2.646  1.00 35.89  ? 412  ASN A CB  1 
ATOM   3046 C CG  . ASN A  1 385 ? -23.336 -28.868 -3.705  1.00 37.84  ? 412  ASN A CG  1 
ATOM   3047 O OD1 . ASN A  1 385 ? -23.393 -30.098 -3.791  1.00 37.20  ? 412  ASN A OD1 1 
ATOM   3048 N ND2 . ASN A  1 385 ? -22.590 -28.124 -4.516  1.00 37.69  ? 412  ASN A ND2 1 
ATOM   3049 N N   . LEU A  1 386 ? -24.381 -27.340 0.660   1.00 27.07  ? 413  LEU A N   1 
ATOM   3050 C CA  . LEU A  1 386 ? -25.239 -26.631 1.593   1.00 27.63  ? 413  LEU A CA  1 
ATOM   3051 C C   . LEU A  1 386 ? -24.457 -25.645 2.452   1.00 26.48  ? 413  LEU A C   1 
ATOM   3052 O O   . LEU A  1 386 ? -24.467 -25.726 3.684   1.00 28.37  ? 413  LEU A O   1 
ATOM   3053 C CB  . LEU A  1 386 ? -26.002 -27.624 2.471   1.00 30.34  ? 413  LEU A CB  1 
ATOM   3054 C CG  . LEU A  1 386 ? -26.754 -28.743 1.739   1.00 33.10  ? 413  LEU A CG  1 
ATOM   3055 C CD1 . LEU A  1 386 ? -27.592 -29.560 2.717   1.00 24.75  ? 413  LEU A CD1 1 
ATOM   3056 C CD2 . LEU A  1 386 ? -27.620 -28.192 0.610   1.00 31.58  ? 413  LEU A CD2 1 
ATOM   3057 N N   . GLY A  1 387 ? -23.791 -24.699 1.800   1.00 22.65  ? 414  GLY A N   1 
ATOM   3058 C CA  . GLY A  1 387 ? -23.048 -23.679 2.513   1.00 29.42  ? 414  GLY A CA  1 
ATOM   3059 C C   . GLY A  1 387 ? -23.959 -22.750 3.288   1.00 27.70  ? 414  GLY A C   1 
ATOM   3060 O O   . GLY A  1 387 ? -23.509 -21.992 4.146   1.00 22.90  ? 414  GLY A O   1 
ATOM   3061 N N   . ASN A  1 388 ? -25.252 -22.823 2.985   1.00 31.15  ? 415  ASN A N   1 
ATOM   3062 C CA  . ASN A  1 388 ? -26.243 -21.937 3.580   1.00 25.86  ? 415  ASN A CA  1 
ATOM   3063 C C   . ASN A  1 388 ? -27.021 -22.588 4.716   1.00 22.89  ? 415  ASN A C   1 
ATOM   3064 O O   . ASN A  1 388 ? -27.576 -21.894 5.571   1.00 19.53  ? 415  ASN A O   1 
ATOM   3065 C CB  . ASN A  1 388 ? -27.199 -21.437 2.503   1.00 22.94  ? 415  ASN A CB  1 
ATOM   3066 C CG  . ASN A  1 388 ? -26.495 -20.622 1.441   1.00 35.47  ? 415  ASN A CG  1 
ATOM   3067 O OD1 . ASN A  1 388 ? -26.542 -19.391 1.457   1.00 39.19  ? 415  ASN A OD1 1 
ATOM   3068 N ND2 . ASN A  1 388 ? -25.821 -21.303 0.517   1.00 37.76  ? 415  ASN A ND2 1 
ATOM   3069 N N   . LEU A  1 389 ? -27.051 -23.920 4.711   1.00 21.12  ? 416  LEU A N   1 
ATOM   3070 C CA  . LEU A  1 389 ? -27.695 -24.722 5.753   1.00 17.96  ? 416  LEU A CA  1 
ATOM   3071 C C   . LEU A  1 389 ? -27.327 -24.265 7.161   1.00 16.50  ? 416  LEU A C   1 
ATOM   3072 O O   . LEU A  1 389 ? -26.199 -24.455 7.598   1.00 20.91  ? 416  LEU A O   1 
ATOM   3073 C CB  . LEU A  1 389 ? -27.289 -26.182 5.582   1.00 19.06  ? 416  LEU A CB  1 
ATOM   3074 C CG  . LEU A  1 389 ? -27.919 -27.205 6.522   1.00 20.61  ? 416  LEU A CG  1 
ATOM   3075 C CD1 . LEU A  1 389 ? -29.271 -27.643 5.990   1.00 21.27  ? 416  LEU A CD1 1 
ATOM   3076 C CD2 . LEU A  1 389 ? -26.995 -28.398 6.699   1.00 20.57  ? 416  LEU A CD2 1 
ATOM   3077 N N   . VAL A  1 390 ? -28.282 -23.672 7.868   1.00 13.13  ? 417  VAL A N   1 
ATOM   3078 C CA  . VAL A  1 390 ? -28.006 -23.058 9.159   1.00 13.60  ? 417  VAL A CA  1 
ATOM   3079 C C   . VAL A  1 390 ? -28.178 -24.019 10.323  1.00 16.55  ? 417  VAL A C   1 
ATOM   3080 O O   . VAL A  1 390 ? -27.364 -24.037 11.241  1.00 24.77  ? 417  VAL A O   1 
ATOM   3081 C CB  . VAL A  1 390 ? -28.880 -21.816 9.395   1.00 15.25  ? 417  VAL A CB  1 
ATOM   3082 C CG1 . VAL A  1 390 ? -28.646 -21.251 10.786  1.00 15.88  ? 417  VAL A CG1 1 
ATOM   3083 C CG2 . VAL A  1 390 ? -28.575 -20.765 8.350   1.00 21.07  ? 417  VAL A CG2 1 
ATOM   3084 N N   . THR A  1 391 ? -29.237 -24.814 10.303  1.00 14.36  ? 418  THR A N   1 
ATOM   3085 C CA  . THR A  1 391 ? -29.442 -25.775 11.382  1.00 16.16  ? 418  THR A CA  1 
ATOM   3086 C C   . THR A  1 391 ? -29.912 -27.134 10.866  1.00 16.38  ? 418  THR A C   1 
ATOM   3087 O O   . THR A  1 391 ? -30.765 -27.215 9.984   1.00 13.98  ? 418  THR A O   1 
ATOM   3088 C CB  . THR A  1 391 ? -30.397 -25.233 12.465  1.00 14.71  ? 418  THR A CB  1 
ATOM   3089 O OG1 . THR A  1 391 ? -31.306 -26.267 12.857  1.00 13.52  ? 418  THR A OG1 1 
ATOM   3090 C CG2 . THR A  1 391 ? -31.179 -24.033 11.947  1.00 13.25  ? 418  THR A CG2 1 
ATOM   3091 N N   . LEU A  1 392 ? -29.345 -28.200 11.424  1.00 17.18  ? 419  LEU A N   1 
ATOM   3092 C CA  . LEU A  1 392 ? -29.563 -29.546 10.902  1.00 14.33  ? 419  LEU A CA  1 
ATOM   3093 C C   . LEU A  1 392 ? -29.900 -30.567 11.986  1.00 14.15  ? 419  LEU A C   1 
ATOM   3094 O O   . LEU A  1 392 ? -29.333 -30.547 13.075  1.00 14.18  ? 419  LEU A O   1 
ATOM   3095 C CB  . LEU A  1 392 ? -28.331 -30.009 10.136  1.00 12.07  ? 419  LEU A CB  1 
ATOM   3096 C CG  . LEU A  1 392 ? -28.392 -31.428 9.591   1.00 10.73  ? 419  LEU A CG  1 
ATOM   3097 C CD1 . LEU A  1 392 ? -28.621 -31.393 8.095   1.00 15.48  ? 419  LEU A CD1 1 
ATOM   3098 C CD2 . LEU A  1 392 ? -27.119 -32.148 9.925   1.00 13.27  ? 419  LEU A CD2 1 
ATOM   3099 N N   . VAL A  1 393 ? -30.828 -31.464 11.671  1.00 13.83  ? 420  VAL A N   1 
ATOM   3100 C CA  . VAL A  1 393 ? -31.311 -32.441 12.632  1.00 14.25  ? 420  VAL A CA  1 
ATOM   3101 C C   . VAL A  1 393 ? -31.285 -33.843 12.031  1.00 11.71  ? 420  VAL A C   1 
ATOM   3102 O O   . VAL A  1 393 ? -31.768 -34.058 10.922  1.00 8.86   ? 420  VAL A O   1 
ATOM   3103 C CB  . VAL A  1 393 ? -32.758 -32.114 13.082  1.00 15.91  ? 420  VAL A CB  1 
ATOM   3104 C CG1 . VAL A  1 393 ? -33.204 -33.064 14.180  1.00 15.24  ? 420  VAL A CG1 1 
ATOM   3105 C CG2 . VAL A  1 393 ? -32.869 -30.668 13.554  1.00 14.19  ? 420  VAL A CG2 1 
ATOM   3106 N N   . MET A  1 394 ? -30.701 -34.788 12.760  1.00 12.98  ? 421  MET A N   1 
ATOM   3107 C CA  . MET A  1 394 ? -30.738 -36.196 12.377  1.00 10.86  ? 421  MET A CA  1 
ATOM   3108 C C   . MET A  1 394 ? -30.922 -37.024 13.627  1.00 10.39  ? 421  MET A C   1 
ATOM   3109 O O   . MET A  1 394 ? -30.486 -38.171 13.695  1.00 11.24  ? 421  MET A O   1 
ATOM   3110 C CB  . MET A  1 394 ? -29.450 -36.629 11.689  1.00 10.64  ? 421  MET A CB  1 
ATOM   3111 C CG  . MET A  1 394 ? -28.985 -35.711 10.594  1.00 10.05  ? 421  MET A CG  1 
ATOM   3112 S SD  . MET A  1 394 ? -28.072 -36.620 9.354   1.00 6.61   ? 421  MET A SD  1 
ATOM   3113 C CE  . MET A  1 394 ? -27.176 -35.283 8.622   1.00 7.01   ? 421  MET A CE  1 
ATOM   3114 N N   . SER A  1 395 ? -31.558 -36.419 14.619  1.00 9.09   ? 422  SER A N   1 
ATOM   3115 C CA  . SER A  1 395 ? -31.826 -37.077 15.885  1.00 12.35  ? 422  SER A CA  1 
ATOM   3116 C C   . SER A  1 395 ? -32.562 -38.397 15.696  1.00 12.82  ? 422  SER A C   1 
ATOM   3117 O O   . SER A  1 395 ? -33.336 -38.559 14.760  1.00 11.39  ? 422  SER A O   1 
ATOM   3118 C CB  . SER A  1 395 ? -32.661 -36.151 16.761  1.00 16.11  ? 422  SER A CB  1 
ATOM   3119 O OG  . SER A  1 395 ? -32.215 -34.815 16.628  1.00 16.85  ? 422  SER A OG  1 
ATOM   3120 N N   . ARG A  1 396 ? -32.316 -39.337 16.597  1.00 14.02  ? 423  ARG A N   1 
ATOM   3121 C CA  . ARG A  1 396 ? -33.012 -40.612 16.571  1.00 13.79  ? 423  ARG A CA  1 
ATOM   3122 C C   . ARG A  1 396 ? -32.988 -41.272 15.202  1.00 12.41  ? 423  ARG A C   1 
ATOM   3123 O O   . ARG A  1 396 ? -34.031 -41.588 14.641  1.00 14.75  ? 423  ARG A O   1 
ATOM   3124 C CB  . ARG A  1 396 ? -34.457 -40.448 17.048  1.00 15.69  ? 423  ARG A CB  1 
ATOM   3125 C CG  . ARG A  1 396 ? -34.590 -40.173 18.540  1.00 16.76  ? 423  ARG A CG  1 
ATOM   3126 C CD  . ARG A  1 396 ? -36.036 -39.923 18.931  1.00 14.86  ? 423  ARG A CD  1 
ATOM   3127 N NE  . ARG A  1 396 ? -36.599 -38.796 18.197  1.00 16.12  ? 423  ARG A NE  1 
ATOM   3128 C CZ  . ARG A  1 396 ? -36.462 -37.529 18.569  1.00 17.29  ? 423  ARG A CZ  1 
ATOM   3129 N NH1 . ARG A  1 396 ? -35.784 -37.237 19.672  1.00 16.51  1 423  ARG A NH1 1 
ATOM   3130 N NH2 . ARG A  1 396 ? -37.002 -36.557 17.841  1.00 15.26  ? 423  ARG A NH2 1 
ATOM   3131 N N   . ASN A  1 397 ? -31.793 -41.449 14.655  1.00 12.69  ? 424  ASN A N   1 
ATOM   3132 C CA  . ASN A  1 397 ? -31.607 -42.362 13.537  1.00 13.01  ? 424  ASN A CA  1 
ATOM   3133 C C   . ASN A  1 397 ? -30.732 -43.525 13.963  1.00 17.83  ? 424  ASN A C   1 
ATOM   3134 O O   . ASN A  1 397 ? -30.702 -43.903 15.141  1.00 21.26  ? 424  ASN A O   1 
ATOM   3135 C CB  . ASN A  1 397 ? -30.991 -41.658 12.333  1.00 12.08  ? 424  ASN A CB  1 
ATOM   3136 C CG  . ASN A  1 397 ? -31.948 -40.688 11.681  1.00 13.87  ? 424  ASN A CG  1 
ATOM   3137 O OD1 . ASN A  1 397 ? -32.597 -39.895 12.359  1.00 14.15  ? 424  ASN A OD1 1 
ATOM   3138 N ND2 . ASN A  1 397 ? -32.057 -40.760 10.362  1.00 11.97  ? 424  ASN A ND2 1 
ATOM   3139 N N   . ARG A  1 398 ? -30.026 -44.098 12.999  1.00 16.82  ? 425  ARG A N   1 
ATOM   3140 C CA  . ARG A  1 398 ? -29.058 -45.141 13.291  1.00 20.29  ? 425  ARG A CA  1 
ATOM   3141 C C   . ARG A  1 398 ? -27.748 -44.803 12.586  1.00 18.48  ? 425  ARG A C   1 
ATOM   3142 O O   . ARG A  1 398 ? -27.132 -45.663 11.957  1.00 20.12  ? 425  ARG A O   1 
ATOM   3143 C CB  . ARG A  1 398 ? -29.587 -46.517 12.864  1.00 20.71  ? 425  ARG A CB  1 
ATOM   3144 C CG  . ARG A  1 398 ? -30.977 -46.850 13.412  1.00 21.02  ? 425  ARG A CG  1 
ATOM   3145 C CD  . ARG A  1 398 ? -30.984 -48.129 14.245  1.00 35.50  ? 425  ARG A CD  1 
ATOM   3146 N NE  . ARG A  1 398 ? -30.214 -47.997 15.482  1.00 46.15  ? 425  ARG A NE  1 
ATOM   3147 C CZ  . ARG A  1 398 ? -30.559 -48.539 16.648  1.00 50.49  ? 425  ARG A CZ  1 
ATOM   3148 N NH1 . ARG A  1 398 ? -31.669 -49.260 16.754  1.00 54.52  1 425  ARG A NH1 1 
ATOM   3149 N NH2 . ARG A  1 398 ? -29.793 -48.358 17.715  1.00 46.39  ? 425  ARG A NH2 1 
ATOM   3150 N N   . LEU A  1 399 ? -27.345 -43.536 12.680  1.00 15.93  ? 426  LEU A N   1 
ATOM   3151 C CA  . LEU A  1 399 ? -26.079 -43.080 12.113  1.00 13.88  ? 426  LEU A CA  1 
ATOM   3152 C C   . LEU A  1 399 ? -24.925 -43.752 12.828  1.00 14.83  ? 426  LEU A C   1 
ATOM   3153 O O   . LEU A  1 399 ? -24.884 -43.794 14.057  1.00 17.98  ? 426  LEU A O   1 
ATOM   3154 C CB  . LEU A  1 399 ? -25.932 -41.561 12.243  1.00 16.35  ? 426  LEU A CB  1 
ATOM   3155 C CG  . LEU A  1 399 ? -26.884 -40.626 11.485  1.00 16.17  ? 426  LEU A CG  1 
ATOM   3156 C CD1 . LEU A  1 399 ? -26.704 -39.181 11.958  1.00 12.13  ? 426  LEU A CD1 1 
ATOM   3157 C CD2 . LEU A  1 399 ? -26.697 -40.725 9.972   1.00 10.94  ? 426  LEU A CD2 1 
ATOM   3158 N N   . ARG A  1 400 ? -23.984 -44.275 12.053  1.00 15.95  ? 427  ARG A N   1 
ATOM   3159 C CA  . ARG A  1 400 ? -22.823 -44.967 12.606  1.00 17.69  ? 427  ARG A CA  1 
ATOM   3160 C C   . ARG A  1 400 ? -21.523 -44.402 12.033  1.00 14.69  ? 427  ARG A C   1 
ATOM   3161 O O   . ARG A  1 400 ? -20.479 -44.439 12.678  1.00 19.49  ? 427  ARG A O   1 
ATOM   3162 C CB  . ARG A  1 400 ? -22.917 -46.470 12.318  1.00 15.76  ? 427  ARG A CB  1 
ATOM   3163 C CG  . ARG A  1 400 ? -21.681 -47.266 12.697  1.00 19.17  ? 427  ARG A CG  1 
ATOM   3164 C CD  . ARG A  1 400 ? -21.766 -48.712 12.218  1.00 31.23  ? 427  ARG A CD  1 
ATOM   3165 N NE  . ARG A  1 400 ? -20.515 -49.434 12.457  1.00 36.59  ? 427  ARG A NE  1 
ATOM   3166 C CZ  . ARG A  1 400 ? -20.280 -50.685 12.071  1.00 32.28  ? 427  ARG A CZ  1 
ATOM   3167 N NH1 . ARG A  1 400 ? -21.212 -51.372 11.422  1.00 27.66  1 427  ARG A NH1 1 
ATOM   3168 N NH2 . ARG A  1 400 ? -19.108 -51.250 12.332  1.00 33.79  ? 427  ARG A NH2 1 
ATOM   3169 N N   . THR A  1 401 ? -21.604 -43.849 10.830  1.00 12.68  ? 428  THR A N   1 
ATOM   3170 C CA  . THR A  1 401 ? -20.414 -43.484 10.087  1.00 10.50  ? 428  THR A CA  1 
ATOM   3171 C C   . THR A  1 401 ? -20.504 -42.091 9.493   1.00 9.07   ? 428  THR A C   1 
ATOM   3172 O O   . THR A  1 401 ? -20.920 -41.926 8.350   1.00 9.52   ? 428  THR A O   1 
ATOM   3173 C CB  . THR A  1 401 ? -20.177 -44.474 8.931   1.00 16.21  ? 428  THR A CB  1 
ATOM   3174 O OG1 . THR A  1 401 ? -20.328 -45.817 9.407   1.00 19.81  ? 428  THR A OG1 1 
ATOM   3175 C CG2 . THR A  1 401 ? -18.784 -44.302 8.346   1.00 22.89  ? 428  THR A CG2 1 
ATOM   3176 N N   . ILE A  1 402 ? -20.109 -41.087 10.264  1.00 8.27   ? 429  ILE A N   1 
ATOM   3177 C CA  . ILE A  1 402 ? -19.917 -39.759 9.705   1.00 8.25   ? 429  ILE A CA  1 
ATOM   3178 C C   . ILE A  1 402 ? -18.562 -39.692 9.009   1.00 12.49  ? 429  ILE A C   1 
ATOM   3179 O O   . ILE A  1 402 ? -17.515 -39.761 9.654   1.00 11.73  ? 429  ILE A O   1 
ATOM   3180 C CB  . ILE A  1 402 ? -19.943 -38.670 10.771  1.00 7.06   ? 429  ILE A CB  1 
ATOM   3181 C CG1 . ILE A  1 402 ? -21.129 -38.861 11.707  1.00 8.28   ? 429  ILE A CG1 1 
ATOM   3182 C CG2 . ILE A  1 402 ? -19.982 -37.311 10.122  1.00 7.29   ? 429  ILE A CG2 1 
ATOM   3183 C CD1 . ILE A  1 402 ? -21.106 -37.927 12.889  1.00 10.46  ? 429  ILE A CD1 1 
ATOM   3184 N N   . ASP A  1 403 ? -18.599 -39.567 7.687   1.00 14.93  ? 430  ASP A N   1 
ATOM   3185 C CA  . ASP A  1 403 ? -17.414 -39.376 6.869   1.00 12.20  ? 430  ASP A CA  1 
ATOM   3186 C C   . ASP A  1 403 ? -16.617 -38.202 7.405   1.00 15.99  ? 430  ASP A C   1 
ATOM   3187 O O   . ASP A  1 403 ? -17.151 -37.343 8.102   1.00 17.52  ? 430  ASP A O   1 
ATOM   3188 C CB  . ASP A  1 403 ? -17.846 -39.089 5.433   1.00 16.15  ? 430  ASP A CB  1 
ATOM   3189 C CG  . ASP A  1 403 ? -16.682 -38.965 4.478   1.00 21.61  ? 430  ASP A CG  1 
ATOM   3190 O OD1 . ASP A  1 403 ? -16.001 -37.920 4.505   1.00 21.88  ? 430  ASP A OD1 1 
ATOM   3191 O OD2 . ASP A  1 403 ? -16.462 -39.906 3.684   1.00 23.39  1 430  ASP A OD2 1 
ATOM   3192 N N   . SER A  1 404 ? -15.331 -38.169 7.085   1.00 19.78  ? 431  SER A N   1 
ATOM   3193 C CA  . SER A  1 404 ? -14.482 -37.058 7.485   1.00 23.72  ? 431  SER A CA  1 
ATOM   3194 C C   . SER A  1 404 ? -14.801 -35.833 6.636   1.00 24.66  ? 431  SER A C   1 
ATOM   3195 O O   . SER A  1 404 ? -15.001 -34.733 7.153   1.00 27.48  ? 431  SER A O   1 
ATOM   3196 C CB  . SER A  1 404 ? -13.012 -37.438 7.329   1.00 23.57  ? 431  SER A CB  1 
ATOM   3197 O OG  . SER A  1 404 ? -12.756 -37.926 6.022   1.00 20.69  ? 431  SER A OG  1 
ATOM   3198 N N   . ARG A  1 405 ? -14.869 -36.041 5.327   1.00 19.96  ? 432  ARG A N   1 
ATOM   3199 C CA  . ARG A  1 405 ? -15.109 -34.955 4.390   1.00 24.29  ? 432  ARG A CA  1 
ATOM   3200 C C   . ARG A  1 405 ? -16.577 -34.505 4.430   1.00 33.46  ? 432  ARG A C   1 
ATOM   3201 O O   . ARG A  1 405 ? -16.976 -33.585 3.710   1.00 40.90  ? 432  ARG A O   1 
ATOM   3202 C CB  . ARG A  1 405 ? -14.710 -35.404 2.979   1.00 23.73  ? 432  ARG A CB  1 
ATOM   3203 C CG  . ARG A  1 405 ? -14.556 -34.278 1.969   1.00 34.87  ? 432  ARG A CG  1 
ATOM   3204 C CD  . ARG A  1 405 ? -13.858 -34.753 0.707   1.00 45.33  ? 432  ARG A CD  1 
ATOM   3205 N NE  . ARG A  1 405 ? -13.923 -33.774 -0.380  1.00 60.37  ? 432  ARG A NE  1 
ATOM   3206 C CZ  . ARG A  1 405 ? -13.143 -32.700 -0.484  1.00 53.08  ? 432  ARG A CZ  1 
ATOM   3207 N NH1 . ARG A  1 405 ? -12.232 -32.441 0.449   1.00 41.42  1 432  ARG A NH1 1 
ATOM   3208 N NH2 . ARG A  1 405 ? -13.279 -31.878 -1.520  1.00 40.97  ? 432  ARG A NH2 1 
ATOM   3209 N N   . ALA A  1 406 ? -17.369 -35.147 5.288   1.00 31.10  ? 433  ALA A N   1 
ATOM   3210 C CA  . ALA A  1 406 ? -18.811 -34.892 5.378   1.00 27.33  ? 433  ALA A CA  1 
ATOM   3211 C C   . ALA A  1 406 ? -19.187 -33.417 5.554   1.00 29.44  ? 433  ALA A C   1 
ATOM   3212 O O   . ALA A  1 406 ? -19.990 -32.893 4.783   1.00 22.52  ? 433  ALA A O   1 
ATOM   3213 C CB  . ALA A  1 406 ? -19.431 -35.732 6.491   1.00 19.50  ? 433  ALA A CB  1 
ATOM   3214 N N   . PHE A  1 407 ? -18.590 -32.757 6.549   1.00 31.57  ? 434  PHE A N   1 
ATOM   3215 C CA  . PHE A  1 407 ? -19.000 -31.408 6.955   1.00 28.70  ? 434  PHE A CA  1 
ATOM   3216 C C   . PHE A  1 407 ? -18.014 -30.287 6.619   1.00 27.59  ? 434  PHE A C   1 
ATOM   3217 O O   . PHE A  1 407 ? -17.843 -29.350 7.402   1.00 25.26  ? 434  PHE A O   1 
ATOM   3218 C CB  . PHE A  1 407 ? -19.275 -31.379 8.458   1.00 23.54  ? 434  PHE A CB  1 
ATOM   3219 C CG  . PHE A  1 407 ? -20.458 -32.191 8.871   1.00 21.68  ? 434  PHE A CG  1 
ATOM   3220 C CD1 . PHE A  1 407 ? -21.735 -31.660 8.797   1.00 26.74  ? 434  PHE A CD1 1 
ATOM   3221 C CD2 . PHE A  1 407 ? -20.299 -33.483 9.336   1.00 21.08  ? 434  PHE A CD2 1 
ATOM   3222 C CE1 . PHE A  1 407 ? -22.838 -32.406 9.180   1.00 27.05  ? 434  PHE A CE1 1 
ATOM   3223 C CE2 . PHE A  1 407 ? -21.394 -34.235 9.719   1.00 23.86  ? 434  PHE A CE2 1 
ATOM   3224 C CZ  . PHE A  1 407 ? -22.666 -33.698 9.641   1.00 24.70  ? 434  PHE A CZ  1 
ATOM   3225 N N   . VAL A  1 408 ? -17.386 -30.362 5.455   1.00 27.27  ? 435  VAL A N   1 
ATOM   3226 C CA  . VAL A  1 408 ? -16.347 -29.397 5.116   1.00 29.38  ? 435  VAL A CA  1 
ATOM   3227 C C   . VAL A  1 408 ? -16.903 -28.106 4.501   1.00 32.19  ? 435  VAL A C   1 
ATOM   3228 O O   . VAL A  1 408 ? -16.356 -27.021 4.712   1.00 31.96  ? 435  VAL A O   1 
ATOM   3229 C CB  . VAL A  1 408 ? -15.275 -30.028 4.201   1.00 24.86  ? 435  VAL A CB  1 
ATOM   3230 C CG1 . VAL A  1 408 ? -15.907 -30.546 2.920   1.00 30.88  ? 435  VAL A CG1 1 
ATOM   3231 C CG2 . VAL A  1 408 ? -14.162 -29.036 3.907   1.00 21.46  ? 435  VAL A CG2 1 
ATOM   3232 N N   . SER A  1 409 ? -18.002 -28.221 3.759   1.00 32.97  ? 436  SER A N   1 
ATOM   3233 C CA  . SER A  1 409 ? -18.567 -27.068 3.060   1.00 31.68  ? 436  SER A CA  1 
ATOM   3234 C C   . SER A  1 409 ? -19.707 -26.413 3.829   1.00 23.58  ? 436  SER A C   1 
ATOM   3235 O O   . SER A  1 409 ? -20.152 -25.323 3.485   1.00 24.44  ? 436  SER A O   1 
ATOM   3236 C CB  . SER A  1 409 ? -19.034 -27.462 1.655   1.00 26.83  ? 436  SER A CB  1 
ATOM   3237 O OG  . SER A  1 409 ? -17.928 -27.818 0.842   1.00 21.52  ? 436  SER A OG  1 
ATOM   3238 N N   . THR A  1 410 ? -20.173 -27.077 4.876   1.00 19.56  ? 437  THR A N   1 
ATOM   3239 C CA  . THR A  1 410 ? -21.283 -26.561 5.659   1.00 21.08  ? 437  THR A CA  1 
ATOM   3240 C C   . THR A  1 410 ? -20.815 -25.496 6.660   1.00 27.67  ? 437  THR A C   1 
ATOM   3241 O O   . THR A  1 410 ? -20.992 -25.630 7.876   1.00 29.19  ? 437  THR A O   1 
ATOM   3242 C CB  . THR A  1 410 ? -22.025 -27.703 6.378   1.00 23.33  ? 437  THR A CB  1 
ATOM   3243 O OG1 . THR A  1 410 ? -21.083 -28.514 7.089   1.00 28.78  ? 437  THR A OG1 1 
ATOM   3244 C CG2 . THR A  1 410 ? -22.756 -28.578 5.374   1.00 17.74  ? 437  THR A CG2 1 
ATOM   3245 N N   . ASN A  1 411 ? -20.217 -24.431 6.138   1.00 24.40  ? 438  ASN A N   1 
ATOM   3246 C CA  . ASN A  1 411 ? -19.755 -23.332 6.977   1.00 25.72  ? 438  ASN A CA  1 
ATOM   3247 C C   . ASN A  1 411 ? -20.898 -22.448 7.466   1.00 23.63  ? 438  ASN A C   1 
ATOM   3248 O O   . ASN A  1 411 ? -20.698 -21.554 8.285   1.00 21.31  ? 438  ASN A O   1 
ATOM   3249 C CB  . ASN A  1 411 ? -18.717 -22.496 6.228   1.00 26.83  ? 438  ASN A CB  1 
ATOM   3250 C CG  . ASN A  1 411 ? -18.903 -22.553 4.723   1.00 31.89  ? 438  ASN A CG  1 
ATOM   3251 O OD1 . ASN A  1 411 ? -18.258 -23.349 4.039   1.00 32.30  ? 438  ASN A OD1 1 
ATOM   3252 N ND2 . ASN A  1 411 ? -19.791 -21.711 4.198   1.00 31.17  ? 438  ASN A ND2 1 
ATOM   3253 N N   . GLY A  1 412 ? -22.098 -22.704 6.957   1.00 28.97  ? 439  GLY A N   1 
ATOM   3254 C CA  . GLY A  1 412 ? -23.266 -21.934 7.343   1.00 26.73  ? 439  GLY A CA  1 
ATOM   3255 C C   . GLY A  1 412 ? -23.989 -22.546 8.525   1.00 24.90  ? 439  GLY A C   1 
ATOM   3256 O O   . GLY A  1 412 ? -24.906 -21.940 9.085   1.00 22.10  ? 439  GLY A O   1 
ATOM   3257 N N   . LEU A  1 413 ? -23.567 -23.749 8.907   1.00 24.27  ? 440  LEU A N   1 
ATOM   3258 C CA  . LEU A  1 413 ? -24.206 -24.484 9.992   1.00 18.95  ? 440  LEU A CA  1 
ATOM   3259 C C   . LEU A  1 413 ? -23.900 -23.848 11.336  1.00 16.55  ? 440  LEU A C   1 
ATOM   3260 O O   . LEU A  1 413 ? -22.817 -23.318 11.542  1.00 21.28  ? 440  LEU A O   1 
ATOM   3261 C CB  . LEU A  1 413 ? -23.766 -25.948 9.975   1.00 17.29  ? 440  LEU A CB  1 
ATOM   3262 C CG  . LEU A  1 413 ? -24.593 -26.953 10.776  1.00 14.47  ? 440  LEU A CG  1 
ATOM   3263 C CD1 . LEU A  1 413 ? -26.063 -26.813 10.466  1.00 12.37  ? 440  LEU A CD1 1 
ATOM   3264 C CD2 . LEU A  1 413 ? -24.127 -28.362 10.460  1.00 15.94  ? 440  LEU A CD2 1 
ATOM   3265 N N   . ARG A  1 414 ? -24.872 -23.897 12.239  1.00 16.50  ? 441  ARG A N   1 
ATOM   3266 C CA  . ARG A  1 414 ? -24.734 -23.328 13.571  1.00 18.78  ? 441  ARG A CA  1 
ATOM   3267 C C   . ARG A  1 414 ? -25.249 -24.305 14.611  1.00 19.60  ? 441  ARG A C   1 
ATOM   3268 O O   . ARG A  1 414 ? -24.751 -24.361 15.731  1.00 19.58  ? 441  ARG A O   1 
ATOM   3269 C CB  . ARG A  1 414 ? -25.533 -22.035 13.676  1.00 18.81  ? 441  ARG A CB  1 
ATOM   3270 C CG  . ARG A  1 414 ? -25.057 -20.951 12.753  1.00 19.79  ? 441  ARG A CG  1 
ATOM   3271 C CD  . ARG A  1 414 ? -23.590 -20.683 12.971  1.00 19.53  ? 441  ARG A CD  1 
ATOM   3272 N NE  . ARG A  1 414 ? -22.856 -20.757 11.714  1.00 19.48  ? 441  ARG A NE  1 
ATOM   3273 C CZ  . ARG A  1 414 ? -22.304 -19.709 11.117  1.00 22.60  ? 441  ARG A CZ  1 
ATOM   3274 N NH1 . ARG A  1 414 ? -22.390 -18.508 11.677  1.00 22.18  1 441  ARG A NH1 1 
ATOM   3275 N NH2 . ARG A  1 414 ? -21.659 -19.864 9.967   1.00 22.78  ? 441  ARG A NH2 1 
ATOM   3276 N N   . HIS A  1 415 ? -26.263 -25.069 14.230  1.00 19.03  ? 442  HIS A N   1 
ATOM   3277 C CA  . HIS A  1 415 ? -26.897 -26.005 15.142  1.00 17.99  ? 442  HIS A CA  1 
ATOM   3278 C C   . HIS A  1 415 ? -26.948 -27.405 14.534  1.00 19.67  ? 442  HIS A C   1 
ATOM   3279 O O   . HIS A  1 415 ? -27.618 -27.634 13.525  1.00 17.71  ? 442  HIS A O   1 
ATOM   3280 C CB  . HIS A  1 415 ? -28.297 -25.514 15.496  1.00 18.23  ? 442  HIS A CB  1 
ATOM   3281 C CG  . HIS A  1 415 ? -28.344 -24.074 15.905  1.00 25.08  ? 442  HIS A CG  1 
ATOM   3282 N ND1 . HIS A  1 415 ? -27.965 -23.641 17.159  1.00 23.35  ? 442  HIS A ND1 1 
ATOM   3283 C CD2 . HIS A  1 415 ? -28.726 -22.965 15.225  1.00 26.83  ? 442  HIS A CD2 1 
ATOM   3284 C CE1 . HIS A  1 415 ? -28.116 -22.331 17.235  1.00 26.07  ? 442  HIS A CE1 1 
ATOM   3285 N NE2 . HIS A  1 415 ? -28.578 -21.896 16.075  1.00 30.06  ? 442  HIS A NE2 1 
ATOM   3286 N N   . LEU A  1 416 ? -26.229 -28.334 15.161  1.00 19.66  ? 443  LEU A N   1 
ATOM   3287 C CA  . LEU A  1 416 ? -26.085 -29.692 14.653  1.00 14.07  ? 443  LEU A CA  1 
ATOM   3288 C C   . LEU A  1 416 ? -26.539 -30.709 15.683  1.00 13.68  ? 443  LEU A C   1 
ATOM   3289 O O   . LEU A  1 416 ? -25.912 -30.865 16.722  1.00 16.26  ? 443  LEU A O   1 
ATOM   3290 C CB  . LEU A  1 416 ? -24.630 -29.956 14.290  1.00 13.89  ? 443  LEU A CB  1 
ATOM   3291 C CG  . LEU A  1 416 ? -24.262 -31.407 14.000  1.00 16.94  ? 443  LEU A CG  1 
ATOM   3292 C CD1 . LEU A  1 416 ? -25.049 -31.939 12.820  1.00 13.88  ? 443  LEU A CD1 1 
ATOM   3293 C CD2 . LEU A  1 416 ? -22.761 -31.526 13.750  1.00 22.41  ? 443  LEU A CD2 1 
ATOM   3294 N N   . HIS A  1 417 ? -27.630 -31.403 15.385  1.00 18.42  ? 444  HIS A N   1 
ATOM   3295 C CA  . HIS A  1 417 ? -28.212 -32.372 16.309  1.00 18.36  ? 444  HIS A CA  1 
ATOM   3296 C C   . HIS A  1 417 ? -28.108 -33.791 15.756  1.00 15.11  ? 444  HIS A C   1 
ATOM   3297 O O   . HIS A  1 417 ? -28.929 -34.188 14.930  1.00 15.82  ? 444  HIS A O   1 
ATOM   3298 C CB  . HIS A  1 417 ? -29.696 -32.062 16.546  1.00 15.34  ? 444  HIS A CB  1 
ATOM   3299 C CG  . HIS A  1 417 ? -29.978 -30.644 16.944  1.00 16.69  ? 444  HIS A CG  1 
ATOM   3300 N ND1 . HIS A  1 417 ? -30.303 -30.284 18.234  1.00 16.04  ? 444  HIS A ND1 1 
ATOM   3301 C CD2 . HIS A  1 417 ? -30.018 -29.503 16.214  1.00 16.87  ? 444  HIS A CD2 1 
ATOM   3302 C CE1 . HIS A  1 417 ? -30.516 -28.981 18.285  1.00 14.97  ? 444  HIS A CE1 1 
ATOM   3303 N NE2 . HIS A  1 417 ? -30.349 -28.483 17.074  1.00 14.51  ? 444  HIS A NE2 1 
ATOM   3304 N N   . LEU A  1 418 ? -27.119 -34.556 16.210  1.00 10.96  ? 445  LEU A N   1 
ATOM   3305 C CA  . LEU A  1 418 ? -27.021 -35.957 15.814  1.00 11.42  ? 445  LEU A CA  1 
ATOM   3306 C C   . LEU A  1 418 ? -27.279 -36.876 16.994  1.00 11.60  ? 445  LEU A C   1 
ATOM   3307 O O   . LEU A  1 418 ? -26.721 -37.964 17.068  1.00 14.52  ? 445  LEU A O   1 
ATOM   3308 C CB  . LEU A  1 418 ? -25.646 -36.275 15.238  1.00 12.56  ? 445  LEU A CB  1 
ATOM   3309 C CG  . LEU A  1 418 ? -25.032 -35.236 14.311  1.00 17.46  ? 445  LEU A CG  1 
ATOM   3310 C CD1 . LEU A  1 418 ? -23.639 -34.952 14.799  1.00 15.07  ? 445  LEU A CD1 1 
ATOM   3311 C CD2 . LEU A  1 418 ? -25.012 -35.712 12.864  1.00 16.11  ? 445  LEU A CD2 1 
ATOM   3312 N N   . ASP A  1 419 ? -28.124 -36.439 17.915  1.00 10.47  ? 446  ASP A N   1 
ATOM   3313 C CA  . ASP A  1 419 ? -28.386 -37.211 19.120  1.00 13.78  ? 446  ASP A CA  1 
ATOM   3314 C C   . ASP A  1 419 ? -29.061 -38.558 18.842  1.00 17.23  ? 446  ASP A C   1 
ATOM   3315 O O   . ASP A  1 419 ? -29.635 -38.772 17.774  1.00 15.47  ? 446  ASP A O   1 
ATOM   3316 C CB  . ASP A  1 419 ? -29.219 -36.386 20.103  1.00 17.01  ? 446  ASP A CB  1 
ATOM   3317 C CG  . ASP A  1 419 ? -30.418 -35.718 19.441  1.00 19.77  ? 446  ASP A CG  1 
ATOM   3318 O OD1 . ASP A  1 419 ? -31.490 -36.356 19.355  1.00 19.15  1 446  ASP A OD1 1 
ATOM   3319 O OD2 . ASP A  1 419 ? -30.289 -34.551 19.009  1.00 17.53  ? 446  ASP A OD2 1 
ATOM   3320 N N   . HIS A  1 420 ? -28.964 -39.464 19.812  1.00 18.43  ? 447  HIS A N   1 
ATOM   3321 C CA  . HIS A  1 420 ? -29.636 -40.761 19.767  1.00 17.00  ? 447  HIS A CA  1 
ATOM   3322 C C   . HIS A  1 420 ? -29.274 -41.603 18.554  1.00 17.57  ? 447  HIS A C   1 
ATOM   3323 O O   . HIS A  1 420 ? -30.146 -42.149 17.877  1.00 20.84  ? 447  HIS A O   1 
ATOM   3324 C CB  . HIS A  1 420 ? -31.145 -40.576 19.858  1.00 18.36  ? 447  HIS A CB  1 
ATOM   3325 C CG  . HIS A  1 420 ? -31.568 -39.704 20.997  1.00 20.54  ? 447  HIS A CG  1 
ATOM   3326 N ND1 . HIS A  1 420 ? -31.795 -40.193 22.264  1.00 21.23  ? 447  HIS A ND1 1 
ATOM   3327 C CD2 . HIS A  1 420 ? -31.792 -38.371 21.062  1.00 19.12  ? 447  HIS A CD2 1 
ATOM   3328 C CE1 . HIS A  1 420 ? -32.146 -39.200 23.060  1.00 22.03  ? 447  HIS A CE1 1 
ATOM   3329 N NE2 . HIS A  1 420 ? -32.152 -38.083 22.356  1.00 17.82  ? 447  HIS A NE2 1 
ATOM   3330 N N   . ASN A  1 421 ? -27.979 -41.709 18.291  1.00 16.32  ? 448  ASN A N   1 
ATOM   3331 C CA  . ASN A  1 421 ? -27.480 -42.579 17.241  1.00 17.62  ? 448  ASN A CA  1 
ATOM   3332 C C   . ASN A  1 421 ? -26.435 -43.541 17.791  1.00 21.23  ? 448  ASN A C   1 
ATOM   3333 O O   . ASN A  1 421 ? -26.324 -43.724 19.004  1.00 20.05  ? 448  ASN A O   1 
ATOM   3334 C CB  . ASN A  1 421 ? -26.894 -41.755 16.099  1.00 16.53  ? 448  ASN A CB  1 
ATOM   3335 C CG  . ASN A  1 421 ? -27.933 -40.906 15.404  1.00 14.47  ? 448  ASN A CG  1 
ATOM   3336 O OD1 . ASN A  1 421 ? -28.411 -41.252 14.327  1.00 14.76  ? 448  ASN A OD1 1 
ATOM   3337 N ND2 . ASN A  1 421 ? -28.292 -39.788 16.019  1.00 13.16  ? 448  ASN A ND2 1 
ATOM   3338 N N   . ASP A  1 422 ? -25.673 -44.156 16.892  1.00 21.70  ? 449  ASP A N   1 
ATOM   3339 C CA  . ASP A  1 422 ? -24.619 -45.080 17.281  1.00 21.06  ? 449  ASP A CA  1 
ATOM   3340 C C   . ASP A  1 422 ? -23.269 -44.563 16.808  1.00 22.83  ? 449  ASP A C   1 
ATOM   3341 O O   . ASP A  1 422 ? -22.435 -45.331 16.326  1.00 26.71  ? 449  ASP A O   1 
ATOM   3342 C CB  . ASP A  1 422 ? -24.877 -46.470 16.695  1.00 29.57  ? 449  ASP A CB  1 
ATOM   3343 C CG  . ASP A  1 422 ? -25.962 -47.230 17.438  1.00 39.57  ? 449  ASP A CG  1 
ATOM   3344 O OD1 . ASP A  1 422 ? -27.145 -47.115 17.050  1.00 40.08  1 449  ASP A OD1 1 
ATOM   3345 O OD2 . ASP A  1 422 ? -25.629 -47.950 18.407  1.00 37.90  ? 449  ASP A OD2 1 
ATOM   3346 N N   . ILE A  1 423 ? -23.053 -43.259 16.946  1.00 21.82  ? 450  ILE A N   1 
ATOM   3347 C CA  . ILE A  1 423 ? -21.800 -42.659 16.505  1.00 20.96  ? 450  ILE A CA  1 
ATOM   3348 C C   . ILE A  1 423 ? -20.740 -42.709 17.599  1.00 21.06  ? 450  ILE A C   1 
ATOM   3349 O O   . ILE A  1 423 ? -20.996 -42.348 18.746  1.00 17.46  ? 450  ILE A O   1 
ATOM   3350 C CB  . ILE A  1 423 ? -21.986 -41.204 16.038  1.00 20.59  ? 450  ILE A CB  1 
ATOM   3351 C CG1 . ILE A  1 423 ? -23.347 -41.032 15.354  1.00 19.28  ? 450  ILE A CG1 1 
ATOM   3352 C CG2 . ILE A  1 423 ? -20.842 -40.800 15.112  1.00 14.37  ? 450  ILE A CG2 1 
ATOM   3353 C CD1 . ILE A  1 423 ? -23.648 -39.610 14.932  1.00 15.11  ? 450  ILE A CD1 1 
ATOM   3354 N N   . ASP A  1 424 ? -19.548 -43.162 17.219  1.00 29.84  ? 451  ASP A N   1 
ATOM   3355 C CA  . ASP A  1 424 ? -18.417 -43.301 18.132  1.00 26.38  ? 451  ASP A CA  1 
ATOM   3356 C C   . ASP A  1 424 ? -17.209 -42.529 17.613  1.00 26.22  ? 451  ASP A C   1 
ATOM   3357 O O   . ASP A  1 424 ? -16.259 -42.267 18.355  1.00 29.74  ? 451  ASP A O   1 
ATOM   3358 C CB  . ASP A  1 424 ? -18.042 -44.776 18.279  1.00 24.26  ? 451  ASP A CB  1 
ATOM   3359 C CG  . ASP A  1 424 ? -17.803 -45.463 16.934  1.00 30.70  ? 451  ASP A CG  1 
ATOM   3360 O OD1 . ASP A  1 424 ? -17.598 -44.771 15.911  1.00 25.22  ? 451  ASP A OD1 1 
ATOM   3361 O OD2 . ASP A  1 424 ? -17.822 -46.709 16.899  1.00 41.20  1 451  ASP A OD2 1 
ATOM   3362 N N   . LEU A  1 425 ? -17.255 -42.196 16.324  1.00 22.73  ? 452  LEU A N   1 
ATOM   3363 C CA  . LEU A  1 425 ? -16.134 -41.595 15.608  1.00 21.53  ? 452  LEU A CA  1 
ATOM   3364 C C   . LEU A  1 425 ? -14.960 -42.567 15.522  1.00 23.30  ? 452  LEU A C   1 
ATOM   3365 O O   . LEU A  1 425 ? -13.826 -42.176 15.246  1.00 18.41  ? 452  LEU A O   1 
ATOM   3366 C CB  . LEU A  1 425 ? -15.746 -40.249 16.215  1.00 17.72  ? 452  LEU A CB  1 
ATOM   3367 C CG  . LEU A  1 425 ? -16.933 -39.285 16.146  1.00 17.80  ? 452  LEU A CG  1 
ATOM   3368 C CD1 . LEU A  1 425 ? -16.678 -37.995 16.899  1.00 16.10  ? 452  LEU A CD1 1 
ATOM   3369 C CD2 . LEU A  1 425 ? -17.264 -38.995 14.690  1.00 19.91  ? 452  LEU A CD2 1 
ATOM   3370 N N   . GLN A  1 426 ? -15.275 -43.840 15.763  1.00 28.77  ? 453  GLN A N   1 
ATOM   3371 C CA  . GLN A  1 426 ? -14.389 -44.978 15.516  1.00 27.95  ? 453  GLN A CA  1 
ATOM   3372 C C   . GLN A  1 426 ? -13.034 -44.908 16.210  1.00 37.11  ? 453  GLN A C   1 
ATOM   3373 O O   . GLN A  1 426 ? -12.120 -45.650 15.850  1.00 42.29  ? 453  GLN A O   1 
ATOM   3374 C CB  . GLN A  1 426 ? -14.195 -45.188 14.008  1.00 25.88  ? 453  GLN A CB  1 
ATOM   3375 C CG  . GLN A  1 426 ? -15.504 -45.225 13.223  1.00 37.68  ? 453  GLN A CG  1 
ATOM   3376 C CD  . GLN A  1 426 ? -15.332 -45.703 11.789  1.00 35.57  ? 453  GLN A CD  1 
ATOM   3377 O OE1 . GLN A  1 426 ? -14.837 -46.805 11.545  1.00 37.02  ? 453  GLN A OE1 1 
ATOM   3378 N NE2 . GLN A  1 426 ? -15.752 -44.877 10.833  1.00 27.98  ? 453  GLN A NE2 1 
ATOM   3379 N N   . GLN A  1 427 ? -12.905 -44.039 17.210  1.00 37.84  ? 454  GLN A N   1 
ATOM   3380 C CA  . GLN A  1 427 ? -11.599 -43.803 17.823  1.00 39.63  ? 454  GLN A CA  1 
ATOM   3381 C C   . GLN A  1 427 ? -11.083 -44.971 18.645  1.00 41.03  ? 454  GLN A C   1 
ATOM   3382 O O   . GLN A  1 427 ? -11.726 -45.395 19.609  1.00 34.16  ? 454  GLN A O   1 
ATOM   3383 C CB  . GLN A  1 427 ? -11.582 -42.525 18.668  1.00 31.84  ? 454  GLN A CB  1 
ATOM   3384 C CG  . GLN A  1 427 ? -10.944 -41.333 17.963  1.00 36.02  ? 454  GLN A CG  1 
ATOM   3385 C CD  . GLN A  1 427 ? -9.547  -41.626 17.434  1.00 45.11  ? 454  GLN A CD  1 
ATOM   3386 O OE1 . GLN A  1 427 ? -8.770  -42.352 18.060  1.00 42.70  ? 454  GLN A OE1 1 
ATOM   3387 N NE2 . GLN A  1 427 ? -9.221  -41.056 16.274  1.00 37.16  ? 454  GLN A NE2 1 
ATOM   3388 N N   . PRO A  1 428 ? -9.914  -45.499 18.248  1.00 39.59  ? 455  PRO A N   1 
ATOM   3389 C CA  . PRO A  1 428 ? -9.161  -46.441 19.072  1.00 41.21  ? 455  PRO A CA  1 
ATOM   3390 C C   . PRO A  1 428 ? -8.806  -45.745 20.369  1.00 36.95  ? 455  PRO A C   1 
ATOM   3391 O O   . PRO A  1 428 ? -8.430  -44.575 20.346  1.00 34.75  ? 455  PRO A O   1 
ATOM   3392 C CB  . PRO A  1 428 ? -7.895  -46.690 18.247  1.00 45.53  ? 455  PRO A CB  1 
ATOM   3393 C CG  . PRO A  1 428 ? -7.805  -45.518 17.315  1.00 39.63  ? 455  PRO A CG  1 
ATOM   3394 C CD  . PRO A  1 428 ? -9.221  -45.206 16.984  1.00 34.37  ? 455  PRO A CD  1 
ATOM   3395 N N   . LEU A  1 429 ? -8.930  -46.453 21.482  1.00 35.38  ? 456  LEU A N   1 
ATOM   3396 C CA  . LEU A  1 429 ? -8.766  -45.838 22.790  1.00 34.62  ? 456  LEU A CA  1 
ATOM   3397 C C   . LEU A  1 429 ? -7.310  -45.513 23.104  1.00 36.12  ? 456  LEU A C   1 
ATOM   3398 O O   . LEU A  1 429 ? -7.026  -44.753 24.023  1.00 36.02  ? 456  LEU A O   1 
ATOM   3399 C CB  . LEU A  1 429 ? -9.365  -46.728 23.883  1.00 37.01  ? 456  LEU A CB  1 
ATOM   3400 C CG  . LEU A  1 429 ? -10.873 -46.999 23.806  1.00 47.40  ? 456  LEU A CG  1 
ATOM   3401 C CD1 . LEU A  1 429 ? -11.207 -48.154 22.859  1.00 54.12  ? 456  LEU A CD1 1 
ATOM   3402 C CD2 . LEU A  1 429 ? -11.459 -47.246 25.190  1.00 50.60  ? 456  LEU A CD2 1 
ATOM   3403 N N   . LEU A  1 430 ? -6.389  -46.078 22.332  1.00 34.54  ? 457  LEU A N   1 
ATOM   3404 C CA  . LEU A  1 430 ? -4.969  -45.887 22.600  1.00 30.49  ? 457  LEU A CA  1 
ATOM   3405 C C   . LEU A  1 430 ? -4.430  -44.543 22.105  1.00 31.73  ? 457  LEU A C   1 
ATOM   3406 O O   . LEU A  1 430 ? -3.482  -44.010 22.675  1.00 29.36  ? 457  LEU A O   1 
ATOM   3407 C CB  . LEU A  1 430 ? -4.155  -47.027 22.003  1.00 27.21  ? 457  LEU A CB  1 
ATOM   3408 C CG  . LEU A  1 430 ? -2.870  -47.325 22.768  1.00 27.54  ? 457  LEU A CG  1 
ATOM   3409 C CD1 . LEU A  1 430 ? -3.135  -48.334 23.880  1.00 31.27  ? 457  LEU A CD1 1 
ATOM   3410 C CD2 . LEU A  1 430 ? -1.795  -47.817 21.823  1.00 29.89  ? 457  LEU A CD2 1 
ATOM   3411 N N   . ASP A  1 431 ? -5.021  -44.009 21.038  1.00 33.06  ? 458  ASP A N   1 
ATOM   3412 C CA  . ASP A  1 431 ? -4.692  -42.664 20.569  1.00 30.54  ? 458  ASP A CA  1 
ATOM   3413 C C   . ASP A  1 431 ? -5.218  -41.630 21.550  1.00 34.55  ? 458  ASP A C   1 
ATOM   3414 O O   . ASP A  1 431 ? -4.711  -40.513 21.628  1.00 33.16  ? 458  ASP A O   1 
ATOM   3415 C CB  . ASP A  1 431 ? -5.315  -42.398 19.201  1.00 38.14  ? 458  ASP A CB  1 
ATOM   3416 C CG  . ASP A  1 431 ? -4.399  -42.767 18.059  1.00 35.73  ? 458  ASP A CG  1 
ATOM   3417 O OD1 . ASP A  1 431 ? -3.355  -42.098 17.894  1.00 30.87  ? 458  ASP A OD1 1 
ATOM   3418 O OD2 . ASP A  1 431 ? -4.737  -43.712 17.314  1.00 33.74  1 458  ASP A OD2 1 
ATOM   3419 N N   . ILE A  1 432 ? -6.256  -42.017 22.284  1.00 40.23  ? 459  ILE A N   1 
ATOM   3420 C CA  . ILE A  1 432 ? -6.864  -41.165 23.297  1.00 41.88  ? 459  ILE A CA  1 
ATOM   3421 C C   . ILE A  1 432 ? -5.934  -40.988 24.485  1.00 39.54  ? 459  ILE A C   1 
ATOM   3422 O O   . ILE A  1 432 ? -5.596  -39.866 24.856  1.00 41.15  ? 459  ILE A O   1 
ATOM   3423 C CB  . ILE A  1 432 ? -8.171  -41.777 23.824  1.00 38.48  ? 459  ILE A CB  1 
ATOM   3424 C CG1 . ILE A  1 432 ? -9.111  -42.124 22.664  1.00 42.19  ? 459  ILE A CG1 1 
ATOM   3425 C CG2 . ILE A  1 432 ? -8.821  -40.848 24.841  1.00 33.55  ? 459  ILE A CG2 1 
ATOM   3426 C CD1 . ILE A  1 432 ? -9.354  -40.984 21.691  1.00 39.42  ? 459  ILE A CD1 1 
ATOM   3427 N N   . MET A  1 433 ? -5.533  -42.111 25.074  1.00 37.29  ? 460  MET A N   1 
ATOM   3428 C CA  . MET A  1 433 ? -4.655  -42.123 26.237  1.00 36.95  ? 460  MET A CA  1 
ATOM   3429 C C   . MET A  1 433 ? -3.349  -41.391 25.951  1.00 41.95  ? 460  MET A C   1 
ATOM   3430 O O   . MET A  1 433 ? -2.747  -40.805 26.852  1.00 42.87  ? 460  MET A O   1 
ATOM   3431 C CB  . MET A  1 433 ? -4.362  -43.565 26.659  1.00 38.93  ? 460  MET A CB  1 
ATOM   3432 C CG  . MET A  1 433 ? -5.602  -44.441 26.783  1.00 50.42  ? 460  MET A CG  1 
ATOM   3433 S SD  . MET A  1 433 ? -5.239  -46.214 26.757  1.00 80.06  ? 460  MET A SD  1 
ATOM   3434 C CE  . MET A  1 433 ? -6.882  -46.918 26.593  1.00 35.90  ? 460  MET A CE  1 
ATOM   3435 N N   . LEU A  1 434 ? -2.920  -41.420 24.692  1.00 42.13  ? 461  LEU A N   1 
ATOM   3436 C CA  . LEU A  1 434 ? -1.683  -40.755 24.291  1.00 44.43  ? 461  LEU A CA  1 
ATOM   3437 C C   . LEU A  1 434 ? -1.943  -39.356 23.735  1.00 46.46  ? 461  LEU A C   1 
ATOM   3438 O O   . LEU A  1 434 ? -1.212  -38.884 22.863  1.00 45.57  ? 461  LEU A O   1 
ATOM   3439 C CB  . LEU A  1 434 ? -0.910  -41.607 23.279  1.00 38.15  ? 461  LEU A CB  1 
ATOM   3440 C CG  . LEU A  1 434 ? -0.512  -43.001 23.775  1.00 39.09  ? 461  LEU A CG  1 
ATOM   3441 C CD1 . LEU A  1 434 ? 0.255   -43.778 22.709  1.00 28.49  ? 461  LEU A CD1 1 
ATOM   3442 C CD2 . LEU A  1 434 ? 0.298   -42.903 25.064  1.00 36.62  ? 461  LEU A CD2 1 
ATOM   3443 N N   . GLN A  1 435 ? -2.989  -38.713 24.257  1.00 45.86  ? 462  GLN A N   1 
ATOM   3444 C CA  . GLN A  1 435 ? -3.342  -37.318 23.966  1.00 44.57  ? 462  GLN A CA  1 
ATOM   3445 C C   . GLN A  1 435 ? -3.169  -36.885 22.513  1.00 53.69  ? 462  GLN A C   1 
ATOM   3446 O O   . GLN A  1 435 ? -2.743  -35.764 22.241  1.00 60.12  ? 462  GLN A O   1 
ATOM   3447 C CB  . GLN A  1 435 ? -2.595  -36.352 24.902  1.00 46.14  ? 462  GLN A CB  1 
ATOM   3448 C CG  . GLN A  1 435 ? -1.071  -36.336 24.751  1.00 56.99  ? 462  GLN A CG  1 
ATOM   3449 C CD  . GLN A  1 435 ? -0.382  -35.453 25.781  1.00 61.67  ? 462  GLN A CD  1 
ATOM   3450 O OE1 . GLN A  1 435 ? -1.024  -34.932 26.694  1.00 68.53  ? 462  GLN A OE1 1 
ATOM   3451 N NE2 . GLN A  1 435 ? 0.931   -35.283 25.638  1.00 46.87  ? 462  GLN A NE2 1 
ATOM   3452 N N   . THR A  1 436 ? -3.509  -37.770 21.582  1.00 55.87  ? 463  THR A N   1 
ATOM   3453 C CA  . THR A  1 436 ? -3.325  -37.473 20.164  1.00 59.17  ? 463  THR A CA  1 
ATOM   3454 C C   . THR A  1 436 ? -4.237  -36.333 19.701  1.00 53.74  ? 463  THR A C   1 
ATOM   3455 O O   . THR A  1 436 ? -5.455  -36.373 19.889  1.00 46.90  ? 463  THR A O   1 
ATOM   3456 C CB  . THR A  1 436 ? -3.523  -38.728 19.278  1.00 60.08  ? 463  THR A CB  1 
ATOM   3457 O OG1 . THR A  1 436 ? -2.674  -39.789 19.742  1.00 44.82  ? 463  THR A OG1 1 
ATOM   3458 C CG2 . THR A  1 436 ? -3.191  -38.418 17.820  1.00 59.57  ? 463  THR A CG2 1 
ATOM   3459 N N   . GLN A  1 437 ? -3.626  -35.311 19.111  1.00 56.26  ? 464  GLN A N   1 
ATOM   3460 C CA  . GLN A  1 437 ? -4.352  -34.152 18.604  1.00 66.01  ? 464  GLN A CA  1 
ATOM   3461 C C   . GLN A  1 437 ? -5.073  -34.488 17.300  1.00 63.92  ? 464  GLN A C   1 
ATOM   3462 O O   . GLN A  1 437 ? -4.534  -34.303 16.206  1.00 71.20  ? 464  GLN A O   1 
ATOM   3463 C CB  . GLN A  1 437 ? -3.389  -32.977 18.398  1.00 73.13  ? 464  GLN A CB  1 
ATOM   3464 C CG  . GLN A  1 437 ? -4.038  -31.702 17.872  1.00 75.25  ? 464  GLN A CG  1 
ATOM   3465 C CD  . GLN A  1 437 ? -3.066  -30.538 17.806  1.00 71.50  ? 464  GLN A CD  1 
ATOM   3466 O OE1 . GLN A  1 437 ? -2.571  -30.070 18.833  1.00 70.17  ? 464  GLN A OE1 1 
ATOM   3467 N NE2 . GLN A  1 437 ? -2.786  -30.065 16.595  1.00 62.94  ? 464  GLN A NE2 1 
ATOM   3468 N N   . ILE A  1 438 ? -6.296  -34.990 17.415  1.00 50.76  ? 465  ILE A N   1 
ATOM   3469 C CA  . ILE A  1 438 ? -7.036  -35.393 16.233  1.00 42.91  ? 465  ILE A CA  1 
ATOM   3470 C C   . ILE A  1 438 ? -8.462  -34.848 16.280  1.00 41.66  ? 465  ILE A C   1 
ATOM   3471 O O   . ILE A  1 438 ? -9.065  -34.744 17.349  1.00 38.98  ? 465  ILE A O   1 
ATOM   3472 C CB  . ILE A  1 438 ? -7.002  -36.931 16.051  1.00 40.95  ? 465  ILE A CB  1 
ATOM   3473 C CG1 . ILE A  1 438 ? -7.501  -37.318 14.659  1.00 43.89  ? 465  ILE A CG1 1 
ATOM   3474 C CG2 . ILE A  1 438 ? -7.764  -37.638 17.166  1.00 32.53  ? 465  ILE A CG2 1 
ATOM   3475 C CD1 . ILE A  1 438 ? -6.712  -36.674 13.540  1.00 43.38  ? 465  ILE A CD1 1 
ATOM   3476 N N   . ASN A  1 439 ? -8.988  -34.479 15.117  1.00 39.29  ? 466  ASN A N   1 
ATOM   3477 C CA  . ASN A  1 439 ? -10.284 -33.815 15.046  1.00 33.45  ? 466  ASN A CA  1 
ATOM   3478 C C   . ASN A  1 439 ? -11.454 -34.691 14.611  1.00 34.18  ? 466  ASN A C   1 
ATOM   3479 O O   . ASN A  1 439 ? -11.317 -35.582 13.761  1.00 28.01  ? 466  ASN A O   1 
ATOM   3480 C CB  . ASN A  1 439 ? -10.203 -32.600 14.122  1.00 33.45  ? 466  ASN A CB  1 
ATOM   3481 C CG  . ASN A  1 439 ? -9.362  -31.490 14.697  1.00 35.26  ? 466  ASN A CG  1 
ATOM   3482 O OD1 . ASN A  1 439 ? -9.352  -31.268 15.908  1.00 33.74  ? 466  ASN A OD1 1 
ATOM   3483 N ND2 . ASN A  1 439 ? -8.648  -30.779 13.831  1.00 39.26  ? 466  ASN A ND2 1 
ATOM   3484 N N   . SER A  1 440 ? -12.611 -34.414 15.205  1.00 31.66  ? 467  SER A N   1 
ATOM   3485 C CA  . SER A  1 440 ? -13.876 -34.962 14.740  1.00 31.16  ? 467  SER A CA  1 
ATOM   3486 C C   . SER A  1 440 ? -14.177 -34.325 13.390  1.00 26.61  ? 467  SER A C   1 
ATOM   3487 O O   . SER A  1 440 ? -13.662 -33.244 13.093  1.00 24.21  ? 467  SER A O   1 
ATOM   3488 C CB  . SER A  1 440 ? -14.990 -34.628 15.735  1.00 27.08  ? 467  SER A CB  1 
ATOM   3489 O OG  . SER A  1 440 ? -15.269 -33.238 15.736  1.00 28.05  ? 467  SER A OG  1 
ATOM   3490 N N   . PRO A  1 441 ? -15.021 -34.978 12.569  1.00 25.29  ? 468  PRO A N   1 
ATOM   3491 C CA  . PRO A  1 441 ? -15.334 -34.464 11.228  1.00 25.07  ? 468  PRO A CA  1 
ATOM   3492 C C   . PRO A  1 441 ? -16.030 -33.106 11.268  1.00 23.35  ? 468  PRO A C   1 
ATOM   3493 O O   . PRO A  1 441 ? -16.319 -32.519 10.217  1.00 19.73  ? 468  PRO A O   1 
ATOM   3494 C CB  . PRO A  1 441 ? -16.286 -35.523 10.657  1.00 20.08  ? 468  PRO A CB  1 
ATOM   3495 C CG  . PRO A  1 441 ? -16.001 -36.758 11.439  1.00 22.15  ? 468  PRO A CG  1 
ATOM   3496 C CD  . PRO A  1 441 ? -15.659 -36.283 12.817  1.00 24.73  ? 468  PRO A CD  1 
ATOM   3497 N N   . PHE A  1 442 ? -16.284 -32.616 12.477  1.00 20.23  ? 469  PHE A N   1 
ATOM   3498 C CA  . PHE A  1 442 ? -16.971 -31.351 12.666  1.00 22.73  ? 469  PHE A CA  1 
ATOM   3499 C C   . PHE A  1 442 ? -15.943 -30.226 12.734  1.00 26.20  ? 469  PHE A C   1 
ATOM   3500 O O   . PHE A  1 442 ? -16.293 -29.062 12.929  1.00 28.91  ? 469  PHE A O   1 
ATOM   3501 C CB  . PHE A  1 442 ? -17.818 -31.383 13.944  1.00 21.21  ? 469  PHE A CB  1 
ATOM   3502 C CG  . PHE A  1 442 ? -18.705 -32.603 14.071  1.00 24.49  ? 469  PHE A CG  1 
ATOM   3503 C CD1 . PHE A  1 442 ? -19.127 -33.308 12.954  1.00 24.33  ? 469  PHE A CD1 1 
ATOM   3504 C CD2 . PHE A  1 442 ? -19.124 -33.038 15.318  1.00 22.53  ? 469  PHE A CD2 1 
ATOM   3505 C CE1 . PHE A  1 442 ? -19.927 -34.422 13.083  1.00 19.90  ? 469  PHE A CE1 1 
ATOM   3506 C CE2 . PHE A  1 442 ? -19.930 -34.151 15.448  1.00 17.25  ? 469  PHE A CE2 1 
ATOM   3507 C CZ  . PHE A  1 442 ? -20.324 -34.843 14.331  1.00 16.95  ? 469  PHE A CZ  1 
ATOM   3508 N N   . GLY A  1 443 ? -14.676 -30.593 12.554  1.00 26.99  ? 470  GLY A N   1 
ATOM   3509 C CA  . GLY A  1 443 ? -13.549 -29.686 12.697  1.00 22.28  ? 470  GLY A CA  1 
ATOM   3510 C C   . GLY A  1 443 ? -13.634 -28.341 11.997  1.00 26.78  ? 470  GLY A C   1 
ATOM   3511 O O   . GLY A  1 443 ? -13.280 -27.318 12.580  1.00 32.31  ? 470  GLY A O   1 
ATOM   3512 N N   . TYR A  1 444 ? -14.106 -28.330 10.754  1.00 27.70  ? 471  TYR A N   1 
ATOM   3513 C CA  . TYR A  1 444 ? -14.108 -27.107 9.948   1.00 29.69  ? 471  TYR A CA  1 
ATOM   3514 C C   . TYR A  1 444 ? -15.129 -26.069 10.403  1.00 28.88  ? 471  TYR A C   1 
ATOM   3515 O O   . TYR A  1 444 ? -15.080 -24.914 9.979   1.00 32.43  ? 471  TYR A O   1 
ATOM   3516 C CB  . TYR A  1 444 ? -14.374 -27.432 8.480   1.00 28.42  ? 471  TYR A CB  1 
ATOM   3517 C CG  . TYR A  1 444 ? -13.635 -28.635 7.966   1.00 26.50  ? 471  TYR A CG  1 
ATOM   3518 C CD1 . TYR A  1 444 ? -12.324 -28.534 7.529   1.00 29.38  ? 471  TYR A CD1 1 
ATOM   3519 C CD2 . TYR A  1 444 ? -14.254 -29.874 7.907   1.00 29.42  ? 471  TYR A CD2 1 
ATOM   3520 C CE1 . TYR A  1 444 ? -11.646 -29.637 7.053   1.00 29.43  ? 471  TYR A CE1 1 
ATOM   3521 C CE2 . TYR A  1 444 ? -13.586 -30.981 7.431   1.00 33.61  ? 471  TYR A CE2 1 
ATOM   3522 C CZ  . TYR A  1 444 ? -12.283 -30.857 7.007   1.00 28.92  ? 471  TYR A CZ  1 
ATOM   3523 O OH  . TYR A  1 444 ? -11.622 -31.961 6.533   1.00 33.36  ? 471  TYR A OH  1 
ATOM   3524 N N   . MET A  1 445 ? -16.065 -26.477 11.247  1.00 22.90  ? 472  MET A N   1 
ATOM   3525 C CA  . MET A  1 445 ? -17.131 -25.576 11.649  1.00 24.78  ? 472  MET A CA  1 
ATOM   3526 C C   . MET A  1 445 ? -16.766 -24.779 12.890  1.00 27.93  ? 472  MET A C   1 
ATOM   3527 O O   . MET A  1 445 ? -17.100 -25.151 14.011  1.00 26.90  ? 472  MET A O   1 
ATOM   3528 C CB  . MET A  1 445 ? -18.444 -26.336 11.813  1.00 33.50  ? 472  MET A CB  1 
ATOM   3529 C CG  . MET A  1 445 ? -19.026 -26.780 10.474  1.00 34.05  ? 472  MET A CG  1 
ATOM   3530 S SD  . MET A  1 445 ? -20.518 -27.762 10.619  1.00 20.99  ? 472  MET A SD  1 
ATOM   3531 C CE  . MET A  1 445 ? -19.919 -29.102 11.647  1.00 19.56  ? 472  MET A CE  1 
ATOM   3532 N N   . HIS A  1 446 ? -16.068 -23.674 12.647  1.00 38.76  ? 473  HIS A N   1 
ATOM   3533 C CA  . HIS A  1 446 ? -15.550 -22.772 13.672  1.00 34.93  ? 473  HIS A CA  1 
ATOM   3534 C C   . HIS A  1 446 ? -16.665 -21.977 14.332  1.00 32.58  ? 473  HIS A C   1 
ATOM   3535 O O   . HIS A  1 446 ? -16.663 -21.763 15.547  1.00 29.49  ? 473  HIS A O   1 
ATOM   3536 C CB  . HIS A  1 446 ? -14.558 -21.806 13.019  1.00 32.48  ? 473  HIS A CB  1 
ATOM   3537 C CG  . HIS A  1 446 ? -14.696 -21.727 11.528  1.00 47.02  ? 473  HIS A CG  1 
ATOM   3538 N ND1 . HIS A  1 446 ? -13.689 -22.103 10.664  1.00 52.01  ? 473  HIS A ND1 1 
ATOM   3539 C CD2 . HIS A  1 446 ? -15.736 -21.343 10.747  1.00 49.71  ? 473  HIS A CD2 1 
ATOM   3540 C CE1 . HIS A  1 446 ? -14.097 -21.942 9.417   1.00 52.78  ? 473  HIS A CE1 1 
ATOM   3541 N NE2 . HIS A  1 446 ? -15.336 -21.483 9.439   1.00 51.30  ? 473  HIS A NE2 1 
ATOM   3542 N N   . GLY A  1 447 ? -17.616 -21.539 13.513  1.00 39.57  ? 474  GLY A N   1 
ATOM   3543 C CA  . GLY A  1 447 ? -18.711 -20.710 13.976  1.00 36.06  ? 474  GLY A CA  1 
ATOM   3544 C C   . GLY A  1 447 ? -19.903 -21.498 14.481  1.00 27.31  ? 474  GLY A C   1 
ATOM   3545 O O   . GLY A  1 447 ? -20.949 -20.918 14.760  1.00 25.64  ? 474  GLY A O   1 
ATOM   3546 N N   . LEU A  1 448 ? -19.743 -22.813 14.602  1.00 22.39  ? 475  LEU A N   1 
ATOM   3547 C CA  . LEU A  1 448 ? -20.809 -23.680 15.093  1.00 20.34  ? 475  LEU A CA  1 
ATOM   3548 C C   . LEU A  1 448 ? -21.219 -23.298 16.513  1.00 23.60  ? 475  LEU A C   1 
ATOM   3549 O O   . LEU A  1 448 ? -20.384 -22.902 17.325  1.00 28.10  ? 475  LEU A O   1 
ATOM   3550 C CB  . LEU A  1 448 ? -20.365 -25.140 15.055  1.00 24.89  ? 475  LEU A CB  1 
ATOM   3551 C CG  . LEU A  1 448 ? -21.459 -26.204 15.165  1.00 25.15  ? 475  LEU A CG  1 
ATOM   3552 C CD1 . LEU A  1 448 ? -22.119 -26.448 13.811  1.00 19.85  ? 475  LEU A CD1 1 
ATOM   3553 C CD2 . LEU A  1 448 ? -20.904 -27.499 15.745  1.00 20.91  ? 475  LEU A CD2 1 
ATOM   3554 N N   . LEU A  1 449 ? -22.509 -23.423 16.805  1.00 23.24  ? 476  LEU A N   1 
ATOM   3555 C CA  . LEU A  1 449 ? -23.062 -22.978 18.081  1.00 25.75  ? 476  LEU A CA  1 
ATOM   3556 C C   . LEU A  1 449 ? -23.595 -24.139 18.913  1.00 27.03  ? 476  LEU A C   1 
ATOM   3557 O O   . LEU A  1 449 ? -23.472 -24.147 20.142  1.00 24.38  ? 476  LEU A O   1 
ATOM   3558 C CB  . LEU A  1 449 ? -24.192 -21.979 17.833  1.00 26.09  ? 476  LEU A CB  1 
ATOM   3559 C CG  . LEU A  1 449 ? -23.793 -20.686 17.130  1.00 25.29  ? 476  LEU A CG  1 
ATOM   3560 C CD1 . LEU A  1 449 ? -25.011 -19.981 16.559  1.00 18.43  ? 476  LEU A CD1 1 
ATOM   3561 C CD2 . LEU A  1 449 ? -23.056 -19.790 18.109  1.00 34.58  ? 476  LEU A CD2 1 
ATOM   3562 N N   . THR A  1 450 ? -24.198 -25.113 18.236  1.00 22.91  ? 477  THR A N   1 
ATOM   3563 C CA  . THR A  1 450 ? -24.825 -26.238 18.916  1.00 20.89  ? 477  THR A CA  1 
ATOM   3564 C C   . THR A  1 450 ? -24.351 -27.589 18.398  1.00 21.96  ? 477  THR A C   1 
ATOM   3565 O O   . THR A  1 450 ? -24.469 -27.889 17.211  1.00 20.98  ? 477  THR A O   1 
ATOM   3566 C CB  . THR A  1 450 ? -26.351 -26.189 18.784  1.00 19.16  ? 477  THR A CB  1 
ATOM   3567 O OG1 . THR A  1 450 ? -26.845 -24.987 19.384  1.00 24.96  ? 477  THR A OG1 1 
ATOM   3568 C CG2 . THR A  1 450 ? -26.977 -27.391 19.469  1.00 16.34  ? 477  THR A CG2 1 
ATOM   3569 N N   . LEU A  1 451 ? -23.815 -28.399 19.304  1.00 24.89  ? 478  LEU A N   1 
ATOM   3570 C CA  . LEU A  1 451 ? -23.480 -29.783 19.008  1.00 18.51  ? 478  LEU A CA  1 
ATOM   3571 C C   . LEU A  1 451 ? -24.264 -30.666 19.969  1.00 17.86  ? 478  LEU A C   1 
ATOM   3572 O O   . LEU A  1 451 ? -24.266 -30.428 21.176  1.00 17.30  ? 478  LEU A O   1 
ATOM   3573 C CB  . LEU A  1 451 ? -21.986 -30.021 19.187  1.00 19.47  ? 478  LEU A CB  1 
ATOM   3574 C CG  . LEU A  1 451 ? -21.299 -30.853 18.106  1.00 20.72  ? 478  LEU A CG  1 
ATOM   3575 C CD1 . LEU A  1 451 ? -19.984 -31.413 18.628  1.00 18.69  ? 478  LEU A CD1 1 
ATOM   3576 C CD2 . LEU A  1 451 ? -22.207 -31.963 17.611  1.00 21.03  ? 478  LEU A CD2 1 
ATOM   3577 N N   . ASN A  1 452 ? -24.940 -31.678 19.439  1.00 17.01  ? 479  ASN A N   1 
ATOM   3578 C CA  . ASN A  1 452 ? -25.785 -32.512 20.277  1.00 14.72  ? 479  ASN A CA  1 
ATOM   3579 C C   . ASN A  1 452 ? -25.604 -33.993 20.033  1.00 16.32  ? 479  ASN A C   1 
ATOM   3580 O O   . ASN A  1 452 ? -26.368 -34.598 19.288  1.00 20.23  ? 479  ASN A O   1 
ATOM   3581 C CB  . ASN A  1 452 ? -27.250 -32.149 20.093  1.00 11.57  ? 479  ASN A CB  1 
ATOM   3582 C CG  . ASN A  1 452 ? -28.109 -32.663 21.224  1.00 18.32  ? 479  ASN A CG  1 
ATOM   3583 O OD1 . ASN A  1 452 ? -27.924 -33.783 21.705  1.00 17.22  ? 479  ASN A OD1 1 
ATOM   3584 N ND2 . ASN A  1 452 ? -29.040 -31.837 21.676  1.00 26.39  ? 479  ASN A ND2 1 
ATOM   3585 N N   . LEU A  1 453 ? -24.619 -34.579 20.701  1.00 16.39  ? 480  LEU A N   1 
ATOM   3586 C CA  . LEU A  1 453 ? -24.285 -35.980 20.510  1.00 14.18  ? 480  LEU A CA  1 
ATOM   3587 C C   . LEU A  1 453 ? -24.805 -36.847 21.655  1.00 15.53  ? 480  LEU A C   1 
ATOM   3588 O O   . LEU A  1 453 ? -24.268 -37.915 21.932  1.00 17.43  ? 480  LEU A O   1 
ATOM   3589 C CB  . LEU A  1 453 ? -22.776 -36.113 20.375  1.00 14.22  ? 480  LEU A CB  1 
ATOM   3590 C CG  . LEU A  1 453 ? -22.220 -35.135 19.343  1.00 12.69  ? 480  LEU A CG  1 
ATOM   3591 C CD1 . LEU A  1 453 ? -20.820 -34.709 19.703  1.00 12.47  ? 480  LEU A CD1 1 
ATOM   3592 C CD2 . LEU A  1 453 ? -22.238 -35.773 17.976  1.00 14.77  ? 480  LEU A CD2 1 
ATOM   3593 N N   . ARG A  1 454 ? -25.855 -36.372 22.312  1.00 15.99  ? 481  ARG A N   1 
ATOM   3594 C CA  . ARG A  1 454 ? -26.510 -37.110 23.383  1.00 16.97  ? 481  ARG A CA  1 
ATOM   3595 C C   . ARG A  1 454 ? -26.872 -38.523 22.930  1.00 19.24  ? 481  ARG A C   1 
ATOM   3596 O O   . ARG A  1 454 ? -27.178 -38.737 21.758  1.00 21.06  ? 481  ARG A O   1 
ATOM   3597 C CB  . ARG A  1 454 ? -27.768 -36.354 23.820  1.00 16.30  ? 481  ARG A CB  1 
ATOM   3598 C CG  . ARG A  1 454 ? -28.585 -37.036 24.897  1.00 15.77  ? 481  ARG A CG  1 
ATOM   3599 C CD  . ARG A  1 454 ? -29.721 -36.146 25.362  1.00 12.98  ? 481  ARG A CD  1 
ATOM   3600 N NE  . ARG A  1 454 ? -29.244 -34.988 26.110  1.00 12.50  ? 481  ARG A NE  1 
ATOM   3601 C CZ  . ARG A  1 454 ? -29.502 -34.771 27.397  1.00 15.18  ? 481  ARG A CZ  1 
ATOM   3602 N NH1 . ARG A  1 454 ? -30.239 -35.634 28.084  1.00 15.82  1 481  ARG A NH1 1 
ATOM   3603 N NH2 . ARG A  1 454 ? -29.022 -33.690 27.997  1.00 15.30  ? 481  ARG A NH2 1 
ATOM   3604 N N   . ASN A  1 455 ? -26.813 -39.482 23.852  1.00 18.24  ? 482  ASN A N   1 
ATOM   3605 C CA  . ASN A  1 455 ? -27.207 -40.865 23.570  1.00 19.89  ? 482  ASN A CA  1 
ATOM   3606 C C   . ASN A  1 455 ? -26.408 -41.506 22.430  1.00 20.28  ? 482  ASN A C   1 
ATOM   3607 O O   . ASN A  1 455 ? -26.911 -42.374 21.725  1.00 21.93  ? 482  ASN A O   1 
ATOM   3608 C CB  . ASN A  1 455 ? -28.711 -40.943 23.272  1.00 24.86  ? 482  ASN A CB  1 
ATOM   3609 C CG  . ASN A  1 455 ? -29.310 -42.317 23.557  1.00 27.42  ? 482  ASN A CG  1 
ATOM   3610 O OD1 . ASN A  1 455 ? -28.591 -43.289 23.785  1.00 27.15  ? 482  ASN A OD1 1 
ATOM   3611 N ND2 . ASN A  1 455 ? -30.646 -42.390 23.545  1.00 28.22  ? 482  ASN A ND2 1 
ATOM   3612 N N   . ASN A  1 456 ? -25.170 -41.064 22.241  1.00 20.02  ? 483  ASN A N   1 
ATOM   3613 C CA  . ASN A  1 456 ? -24.259 -41.751 21.335  1.00 20.12  ? 483  ASN A CA  1 
ATOM   3614 C C   . ASN A  1 456 ? -23.213 -42.564 22.106  1.00 22.01  ? 483  ASN A C   1 
ATOM   3615 O O   . ASN A  1 456 ? -23.428 -42.938 23.268  1.00 18.05  ? 483  ASN A O   1 
ATOM   3616 C CB  . ASN A  1 456 ? -23.566 -40.763 20.396  1.00 21.16  ? 483  ASN A CB  1 
ATOM   3617 C CG  . ASN A  1 456 ? -24.474 -40.273 19.283  1.00 18.20  ? 483  ASN A CG  1 
ATOM   3618 O OD1 . ASN A  1 456 ? -24.689 -40.969 18.292  1.00 16.70  ? 483  ASN A OD1 1 
ATOM   3619 N ND2 . ASN A  1 456 ? -24.990 -39.058 19.429  1.00 15.53  ? 483  ASN A ND2 1 
ATOM   3620 N N   . SER A  1 457 ? -22.087 -42.826 21.440  1.00 21.91  ? 484  SER A N   1 
ATOM   3621 C CA  . SER A  1 457 ? -20.982 -43.607 22.005  1.00 18.70  ? 484  SER A CA  1 
ATOM   3622 C C   . SER A  1 457 ? -19.624 -42.897 21.855  1.00 21.84  ? 484  SER A C   1 
ATOM   3623 O O   . SER A  1 457 ? -18.610 -43.524 21.532  1.00 24.83  ? 484  SER A O   1 
ATOM   3624 C CB  . SER A  1 457 ? -20.932 -45.025 21.412  1.00 17.23  ? 484  SER A CB  1 
ATOM   3625 O OG  . SER A  1 457 ? -21.926 -45.837 22.011  1.00 22.29  ? 484  SER A OG  1 
ATOM   3626 N N   . ILE A  1 458 ? -19.607 -41.587 22.088  1.00 21.23  ? 485  ILE A N   1 
ATOM   3627 C CA  . ILE A  1 458 ? -18.359 -40.839 22.050  1.00 19.88  ? 485  ILE A CA  1 
ATOM   3628 C C   . ILE A  1 458 ? -17.567 -41.364 23.228  1.00 22.03  ? 485  ILE A C   1 
ATOM   3629 O O   . ILE A  1 458 ? -18.166 -41.676 24.259  1.00 20.22  ? 485  ILE A O   1 
ATOM   3630 C CB  . ILE A  1 458 ? -18.595 -39.331 22.229  1.00 17.60  ? 485  ILE A CB  1 
ATOM   3631 C CG1 . ILE A  1 458 ? -19.517 -38.804 21.136  1.00 19.42  ? 485  ILE A CG1 1 
ATOM   3632 C CG2 . ILE A  1 458 ? -17.281 -38.573 22.210  1.00 14.70  ? 485  ILE A CG2 1 
ATOM   3633 C CD1 . ILE A  1 458 ? -18.868 -38.716 19.772  1.00 19.16  ? 485  ILE A CD1 1 
ATOM   3634 N N   . ILE A  1 459 ? -16.247 -41.498 23.071  1.00 23.74  ? 486  ILE A N   1 
ATOM   3635 C CA  . ILE A  1 459 ? -15.366 -41.956 24.152  1.00 20.01  ? 486  ILE A CA  1 
ATOM   3636 C C   . ILE A  1 459 ? -14.203 -41.010 24.446  1.00 20.39  ? 486  ILE A C   1 
ATOM   3637 O O   . ILE A  1 459 ? -13.187 -41.429 25.014  1.00 27.60  ? 486  ILE A O   1 
ATOM   3638 C CB  . ILE A  1 459 ? -14.766 -43.322 23.832  1.00 16.01  ? 486  ILE A CB  1 
ATOM   3639 C CG1 . ILE A  1 459 ? -13.944 -43.248 22.547  1.00 17.29  ? 486  ILE A CG1 1 
ATOM   3640 C CG2 . ILE A  1 459 ? -15.875 -44.336 23.693  1.00 26.29  ? 486  ILE A CG2 1 
ATOM   3641 C CD1 . ILE A  1 459 ? -12.898 -44.327 22.430  1.00 25.12  ? 486  ILE A CD1 1 
ATOM   3642 N N   . PHE A  1 460 ? -14.365 -39.738 24.087  1.00 17.25  ? 487  PHE A N   1 
ATOM   3643 C CA  . PHE A  1 460 ? -13.278 -38.760 24.151  1.00 15.90  ? 487  PHE A CA  1 
ATOM   3644 C C   . PHE A  1 460 ? -13.757 -37.361 23.785  1.00 13.95  ? 487  PHE A C   1 
ATOM   3645 O O   . PHE A  1 460 ? -14.493 -37.194 22.830  1.00 16.26  ? 487  PHE A O   1 
ATOM   3646 C CB  . PHE A  1 460 ? -12.159 -39.179 23.193  1.00 17.64  ? 487  PHE A CB  1 
ATOM   3647 C CG  . PHE A  1 460 ? -11.038 -38.185 23.082  1.00 20.49  ? 487  PHE A CG  1 
ATOM   3648 C CD1 . PHE A  1 460 ? -10.361 -37.749 24.211  1.00 28.27  ? 487  PHE A CD1 1 
ATOM   3649 C CD2 . PHE A  1 460 ? -10.640 -37.711 21.843  1.00 19.83  ? 487  PHE A CD2 1 
ATOM   3650 C CE1 . PHE A  1 460 ? -9.320  -36.843 24.104  1.00 31.67  ? 487  PHE A CE1 1 
ATOM   3651 C CE2 . PHE A  1 460 ? -9.601  -36.805 21.726  1.00 22.56  ? 487  PHE A CE2 1 
ATOM   3652 C CZ  . PHE A  1 460 ? -8.939  -36.371 22.858  1.00 31.66  ? 487  PHE A CZ  1 
ATOM   3653 N N   . VAL A  1 461 ? -13.332 -36.351 24.536  1.00 16.60  ? 488  VAL A N   1 
ATOM   3654 C CA  . VAL A  1 461 ? -13.621 -34.963 24.173  1.00 15.51  ? 488  VAL A CA  1 
ATOM   3655 C C   . VAL A  1 461 ? -12.650 -34.498 23.087  1.00 18.00  ? 488  VAL A C   1 
ATOM   3656 O O   . VAL A  1 461 ? -11.502 -34.171 23.378  1.00 27.91  ? 488  VAL A O   1 
ATOM   3657 C CB  . VAL A  1 461 ? -13.510 -34.032 25.393  1.00 12.07  ? 488  VAL A CB  1 
ATOM   3658 C CG1 . VAL A  1 461 ? -13.796 -32.597 24.997  1.00 12.12  ? 488  VAL A CG1 1 
ATOM   3659 C CG2 . VAL A  1 461 ? -14.452 -34.485 26.489  1.00 13.07  ? 488  VAL A CG2 1 
ATOM   3660 N N   . TYR A  1 462 ? -13.100 -34.476 21.836  1.00 14.78  ? 489  TYR A N   1 
ATOM   3661 C CA  . TYR A  1 462 ? -12.183 -34.251 20.714  1.00 20.79  ? 489  TYR A CA  1 
ATOM   3662 C C   . TYR A  1 462 ? -11.553 -32.863 20.681  1.00 21.63  ? 489  TYR A C   1 
ATOM   3663 O O   . TYR A  1 462 ? -12.089 -31.907 21.238  1.00 18.79  ? 489  TYR A O   1 
ATOM   3664 C CB  . TYR A  1 462 ? -12.835 -34.602 19.363  1.00 22.74  ? 489  TYR A CB  1 
ATOM   3665 C CG  . TYR A  1 462 ? -13.042 -36.089 19.184  1.00 18.17  ? 489  TYR A CG  1 
ATOM   3666 C CD1 . TYR A  1 462 ? -13.986 -36.760 19.940  1.00 14.42  ? 489  TYR A CD1 1 
ATOM   3667 C CD2 . TYR A  1 462 ? -12.284 -36.823 18.277  1.00 16.15  ? 489  TYR A CD2 1 
ATOM   3668 C CE1 . TYR A  1 462 ? -14.179 -38.110 19.810  1.00 15.64  ? 489  TYR A CE1 1 
ATOM   3669 C CE2 . TYR A  1 462 ? -12.473 -38.189 18.138  1.00 14.44  ? 489  TYR A CE2 1 
ATOM   3670 C CZ  . TYR A  1 462 ? -13.426 -38.823 18.912  1.00 15.90  ? 489  TYR A CZ  1 
ATOM   3671 O OH  . TYR A  1 462 ? -13.656 -40.174 18.808  1.00 18.92  ? 489  TYR A OH  1 
ATOM   3672 N N   . ASN A  1 463 ? -10.402 -32.782 20.023  1.00 29.04  ? 490  ASN A N   1 
ATOM   3673 C CA  . ASN A  1 463 ? -9.606  -31.563 19.951  1.00 34.39  ? 490  ASN A CA  1 
ATOM   3674 C C   . ASN A  1 463 ? -10.388 -30.372 19.420  1.00 32.33  ? 490  ASN A C   1 
ATOM   3675 O O   . ASN A  1 463 ? -10.334 -29.280 19.987  1.00 35.06  ? 490  ASN A O   1 
ATOM   3676 C CB  . ASN A  1 463 ? -8.366  -31.800 19.077  1.00 42.45  ? 490  ASN A CB  1 
ATOM   3677 C CG  . ASN A  1 463 ? -7.457  -30.580 18.996  1.00 50.09  ? 490  ASN A CG  1 
ATOM   3678 O OD1 . ASN A  1 463 ? -6.538  -30.421 19.801  1.00 54.55  ? 490  ASN A OD1 1 
ATOM   3679 N ND2 . ASN A  1 463 ? -7.706  -29.720 18.015  1.00 43.93  ? 490  ASN A ND2 1 
ATOM   3680 N N   . ASP A  1 464 ? -11.123 -30.595 18.337  1.00 34.23  ? 491  ASP A N   1 
ATOM   3681 C CA  . ASP A  1 464 ? -11.793 -29.514 17.620  1.00 33.17  ? 491  ASP A CA  1 
ATOM   3682 C C   . ASP A  1 464 ? -12.861 -28.759 18.420  1.00 27.22  ? 491  ASP A C   1 
ATOM   3683 O O   . ASP A  1 464 ? -13.114 -27.586 18.155  1.00 27.39  ? 491  ASP A O   1 
ATOM   3684 C CB  . ASP A  1 464 ? -12.361 -30.013 16.280  1.00 32.79  ? 491  ASP A CB  1 
ATOM   3685 C CG  . ASP A  1 464 ? -12.953 -31.417 16.369  1.00 31.97  ? 491  ASP A CG  1 
ATOM   3686 O OD1 . ASP A  1 464 ? -12.563 -32.183 17.277  1.00 32.58  ? 491  ASP A OD1 1 
ATOM   3687 O OD2 . ASP A  1 464 ? -13.799 -31.762 15.515  1.00 27.37  1 491  ASP A OD2 1 
ATOM   3688 N N   . TRP A  1 465 ? -13.467 -29.417 19.405  1.00 25.91  ? 492  TRP A N   1 
ATOM   3689 C CA  . TRP A  1 465 ? -14.586 -28.819 20.140  1.00 27.31  ? 492  TRP A CA  1 
ATOM   3690 C C   . TRP A  1 465 ? -14.114 -27.878 21.242  1.00 25.80  ? 492  TRP A C   1 
ATOM   3691 O O   . TRP A  1 465 ? -14.914 -27.175 21.855  1.00 25.03  ? 492  TRP A O   1 
ATOM   3692 C CB  . TRP A  1 465 ? -15.501 -29.895 20.747  1.00 23.06  ? 492  TRP A CB  1 
ATOM   3693 C CG  . TRP A  1 465 ? -15.800 -31.058 19.836  1.00 20.86  ? 492  TRP A CG  1 
ATOM   3694 C CD1 . TRP A  1 465 ? -15.716 -31.089 18.468  1.00 17.79  ? 492  TRP A CD1 1 
ATOM   3695 C CD2 . TRP A  1 465 ? -16.213 -32.365 20.239  1.00 14.20  ? 492  TRP A CD2 1 
ATOM   3696 N NE1 . TRP A  1 465 ? -16.051 -32.334 18.003  1.00 14.83  ? 492  TRP A NE1 1 
ATOM   3697 C CE2 . TRP A  1 465 ? -16.361 -33.136 19.069  1.00 15.21  ? 492  TRP A CE2 1 
ATOM   3698 C CE3 . TRP A  1 465 ? -16.470 -32.959 21.477  1.00 11.11  ? 492  TRP A CE3 1 
ATOM   3699 C CZ2 . TRP A  1 465 ? -16.756 -34.469 19.103  1.00 15.42  ? 492  TRP A CZ2 1 
ATOM   3700 C CZ3 . TRP A  1 465 ? -16.859 -34.280 21.509  1.00 11.79  ? 492  TRP A CZ3 1 
ATOM   3701 C CH2 . TRP A  1 465 ? -16.999 -35.023 20.331  1.00 15.06  ? 492  TRP A CH2 1 
ATOM   3702 N N   . LYS A  1 466 ? -12.812 -27.875 21.495  1.00 31.46  ? 493  LYS A N   1 
ATOM   3703 C CA  . LYS A  1 466 ? -12.253 -27.048 22.551  1.00 30.52  ? 493  LYS A CA  1 
ATOM   3704 C C   . LYS A  1 466 ? -11.555 -25.838 21.964  1.00 31.76  ? 493  LYS A C   1 
ATOM   3705 O O   . LYS A  1 466 ? -11.684 -24.730 22.475  1.00 36.82  ? 493  LYS A O   1 
ATOM   3706 C CB  . LYS A  1 466 ? -11.263 -27.853 23.396  1.00 31.41  ? 493  LYS A CB  1 
ATOM   3707 C CG  . LYS A  1 466 ? -11.863 -29.072 24.089  1.00 32.77  ? 493  LYS A CG  1 
ATOM   3708 C CD  . LYS A  1 466 ? -10.836 -29.801 24.952  1.00 36.91  ? 493  LYS A CD  1 
ATOM   3709 C CE  . LYS A  1 466 ? -9.638  -30.261 24.124  1.00 40.46  ? 493  LYS A CE  1 
ATOM   3710 N NZ  . LYS A  1 466 ? -8.622  -30.990 24.934  1.00 36.19  1 493  LYS A NZ  1 
ATOM   3711 N N   . ASN A  1 467 ? -10.826 -26.054 20.875  1.00 33.90  ? 494  ASN A N   1 
ATOM   3712 C CA  . ASN A  1 467 ? -9.928  -25.032 20.348  1.00 38.83  ? 494  ASN A CA  1 
ATOM   3713 C C   . ASN A  1 467 ? -10.325 -24.446 18.995  1.00 38.12  ? 494  ASN A C   1 
ATOM   3714 O O   . ASN A  1 467 ? -9.962  -23.312 18.684  1.00 43.94  ? 494  ASN A O   1 
ATOM   3715 C CB  . ASN A  1 467 ? -8.494  -25.570 20.290  1.00 43.10  ? 494  ASN A CB  1 
ATOM   3716 C CG  . ASN A  1 467 ? -7.966  -25.970 21.657  1.00 40.18  ? 494  ASN A CG  1 
ATOM   3717 O OD1 . ASN A  1 467 ? -8.115  -25.236 22.635  1.00 33.90  ? 494  ASN A OD1 1 
ATOM   3718 N ND2 . ASN A  1 467 ? -7.352  -27.146 21.733  1.00 38.49  ? 494  ASN A ND2 1 
ATOM   3719 N N   . THR A  1 468 ? -11.060 -25.210 18.190  1.00 34.63  ? 495  THR A N   1 
ATOM   3720 C CA  . THR A  1 468 ? -11.487 -24.717 16.879  1.00 39.84  ? 495  THR A CA  1 
ATOM   3721 C C   . THR A  1 468 ? -12.898 -24.109 16.897  1.00 33.80  ? 495  THR A C   1 
ATOM   3722 O O   . THR A  1 468 ? -13.204 -23.211 16.115  1.00 32.19  ? 495  THR A O   1 
ATOM   3723 C CB  . THR A  1 468 ? -11.386 -25.807 15.782  1.00 37.49  ? 495  THR A CB  1 
ATOM   3724 O OG1 . THR A  1 468 ? -12.336 -26.848 16.038  1.00 32.85  ? 495  THR A OG1 1 
ATOM   3725 C CG2 . THR A  1 468 ? -9.988  -26.400 15.745  1.00 33.22  ? 495  THR A CG2 1 
ATOM   3726 N N   . MET A  1 469 ? -13.748 -24.600 17.794  1.00 30.62  ? 496  MET A N   1 
ATOM   3727 C CA  . MET A  1 469 ? -15.098 -24.073 17.944  1.00 26.49  ? 496  MET A CA  1 
ATOM   3728 C C   . MET A  1 469 ? -15.148 -23.121 19.129  1.00 34.73  ? 496  MET A C   1 
ATOM   3729 O O   . MET A  1 469 ? -15.442 -23.524 20.256  1.00 34.18  ? 496  MET A O   1 
ATOM   3730 C CB  . MET A  1 469 ? -16.095 -25.210 18.151  1.00 24.04  ? 496  MET A CB  1 
ATOM   3731 C CG  . MET A  1 469 ? -16.109 -26.229 17.032  1.00 27.18  ? 496  MET A CG  1 
ATOM   3732 S SD  . MET A  1 469 ? -17.053 -27.707 17.447  1.00 20.86  ? 496  MET A SD  1 
ATOM   3733 C CE  . MET A  1 469 ? -16.811 -28.678 15.970  1.00 18.14  ? 496  MET A CE  1 
ATOM   3734 N N   . LEU A  1 470 ? -14.856 -21.853 18.872  1.00 37.39  ? 497  LEU A N   1 
ATOM   3735 C CA  . LEU A  1 470 ? -14.773 -20.866 19.939  1.00 37.35  ? 497  LEU A CA  1 
ATOM   3736 C C   . LEU A  1 470 ? -16.137 -20.249 20.223  1.00 38.88  ? 497  LEU A C   1 
ATOM   3737 O O   . LEU A  1 470 ? -16.370 -19.691 21.297  1.00 39.71  ? 497  LEU A O   1 
ATOM   3738 C CB  . LEU A  1 470 ? -13.758 -19.778 19.580  1.00 36.28  ? 497  LEU A CB  1 
ATOM   3739 C CG  . LEU A  1 470 ? -12.306 -20.222 19.365  1.00 36.49  ? 497  LEU A CG  1 
ATOM   3740 C CD1 . LEU A  1 470 ? -12.066 -20.691 17.932  1.00 31.93  ? 497  LEU A CD1 1 
ATOM   3741 C CD2 . LEU A  1 470 ? -11.340 -19.107 19.739  1.00 38.48  ? 497  LEU A CD2 1 
ATOM   3742 N N   . GLN A  1 471 ? -17.038 -20.360 19.254  1.00 38.21  ? 498  GLN A N   1 
ATOM   3743 C CA  . GLN A  1 471 ? -18.359 -19.759 19.368  1.00 37.90  ? 498  GLN A CA  1 
ATOM   3744 C C   . GLN A  1 471 ? -19.349 -20.675 20.080  1.00 34.66  ? 498  GLN A C   1 
ATOM   3745 O O   . GLN A  1 471 ? -20.433 -20.243 20.469  1.00 35.21  ? 498  GLN A O   1 
ATOM   3746 C CB  . GLN A  1 471 ? -18.886 -19.393 17.981  1.00 43.11  ? 498  GLN A CB  1 
ATOM   3747 C CG  . GLN A  1 471 ? -18.101 -18.293 17.276  1.00 49.39  ? 498  GLN A CG  1 
ATOM   3748 C CD  . GLN A  1 471 ? -18.482 -16.896 17.744  1.00 52.00  ? 498  GLN A CD  1 
ATOM   3749 O OE1 . GLN A  1 471 ? -18.601 -16.635 18.946  1.00 44.58  ? 498  GLN A OE1 1 
ATOM   3750 N NE2 . GLN A  1 471 ? -18.680 -15.988 16.789  1.00 43.81  ? 498  GLN A NE2 1 
ATOM   3751 N N   . LEU A  1 472 ? -18.957 -21.934 20.250  1.00 33.83  ? 499  LEU A N   1 
ATOM   3752 C CA  . LEU A  1 472 ? -19.808 -22.971 20.836  1.00 30.29  ? 499  LEU A CA  1 
ATOM   3753 C C   . LEU A  1 472 ? -20.506 -22.559 22.128  1.00 31.25  ? 499  LEU A C   1 
ATOM   3754 O O   . LEU A  1 472 ? -19.867 -22.182 23.111  1.00 33.90  ? 499  LEU A O   1 
ATOM   3755 C CB  . LEU A  1 472 ? -18.992 -24.238 21.081  1.00 29.74  ? 499  LEU A CB  1 
ATOM   3756 C CG  . LEU A  1 472 ? -19.604 -25.529 20.549  1.00 24.66  ? 499  LEU A CG  1 
ATOM   3757 C CD1 . LEU A  1 472 ? -18.588 -26.644 20.616  1.00 23.75  ? 499  LEU A CD1 1 
ATOM   3758 C CD2 . LEU A  1 472 ? -20.833 -25.881 21.347  1.00 26.43  ? 499  LEU A CD2 1 
ATOM   3759 N N   . ARG A  1 473 ? -21.829 -22.649 22.113  1.00 34.10  ? 500  ARG A N   1 
ATOM   3760 C CA  . ARG A  1 473 ? -22.643 -22.240 23.245  1.00 36.11  ? 500  ARG A CA  1 
ATOM   3761 C C   . ARG A  1 473 ? -23.279 -23.452 23.894  1.00 32.43  ? 500  ARG A C   1 
ATOM   3762 O O   . ARG A  1 473 ? -23.485 -23.494 25.108  1.00 31.00  ? 500  ARG A O   1 
ATOM   3763 C CB  . ARG A  1 473 ? -23.736 -21.286 22.775  1.00 35.75  ? 500  ARG A CB  1 
ATOM   3764 C CG  . ARG A  1 473 ? -24.639 -20.781 23.878  1.00 40.21  ? 500  ARG A CG  1 
ATOM   3765 C CD  . ARG A  1 473 ? -24.769 -19.281 23.774  1.00 52.77  ? 500  ARG A CD  1 
ATOM   3766 N NE  . ARG A  1 473 ? -24.946 -18.869 22.385  1.00 64.61  ? 500  ARG A NE  1 
ATOM   3767 C CZ  . ARG A  1 473 ? -24.766 -17.628 21.944  1.00 71.56  ? 500  ARG A CZ  1 
ATOM   3768 N NH1 . ARG A  1 473 ? -24.398 -16.669 22.785  1.00 74.09  1 500  ARG A NH1 1 
ATOM   3769 N NH2 . ARG A  1 473 ? -24.950 -17.345 20.661  1.00 66.55  ? 500  ARG A NH2 1 
ATOM   3770 N N   . GLU A  1 474 ? -23.586 -24.445 23.071  1.00 29.18  ? 501  GLU A N   1 
ATOM   3771 C CA  . GLU A  1 474 ? -24.332 -25.599 23.534  1.00 29.04  ? 501  GLU A CA  1 
ATOM   3772 C C   . GLU A  1 474 ? -23.657 -26.897 23.133  1.00 24.08  ? 501  GLU A C   1 
ATOM   3773 O O   . GLU A  1 474 ? -23.579 -27.225 21.951  1.00 20.90  ? 501  GLU A O   1 
ATOM   3774 C CB  . GLU A  1 474 ? -25.752 -25.555 22.971  1.00 34.36  ? 501  GLU A CB  1 
ATOM   3775 C CG  . GLU A  1 474 ? -26.624 -26.714 23.408  1.00 34.64  ? 501  GLU A CG  1 
ATOM   3776 C CD  . GLU A  1 474 ? -26.779 -26.781 24.910  1.00 37.67  ? 501  GLU A CD  1 
ATOM   3777 O OE1 . GLU A  1 474 ? -26.775 -25.712 25.559  1.00 38.20  ? 501  GLU A OE1 1 
ATOM   3778 O OE2 . GLU A  1 474 ? -26.898 -27.905 25.442  1.00 44.29  1 501  GLU A OE2 1 
ATOM   3779 N N   . LEU A  1 475 ? -23.175 -27.638 24.126  1.00 26.52  ? 502  LEU A N   1 
ATOM   3780 C CA  . LEU A  1 475 ? -22.534 -28.923 23.867  1.00 25.97  ? 502  LEU A CA  1 
ATOM   3781 C C   . LEU A  1 475 ? -23.139 -30.025 24.724  1.00 18.16  ? 502  LEU A C   1 
ATOM   3782 O O   . LEU A  1 475 ? -23.157 -29.938 25.950  1.00 15.18  ? 502  LEU A O   1 
ATOM   3783 C CB  . LEU A  1 475 ? -21.026 -28.832 24.088  1.00 22.35  ? 502  LEU A CB  1 
ATOM   3784 C CG  . LEU A  1 475 ? -20.195 -29.896 23.379  1.00 17.67  ? 502  LEU A CG  1 
ATOM   3785 C CD1 . LEU A  1 475 ? -18.826 -29.341 23.085  1.00 30.25  ? 502  LEU A CD1 1 
ATOM   3786 C CD2 . LEU A  1 475 ? -20.076 -31.128 24.236  1.00 18.72  ? 502  LEU A CD2 1 
ATOM   3787 N N   . ASP A  1 476 ? -23.629 -31.065 24.062  1.00 16.12  ? 503  ASP A N   1 
ATOM   3788 C CA  . ASP A  1 476 ? -24.354 -32.118 24.746  1.00 18.54  ? 503  ASP A CA  1 
ATOM   3789 C C   . ASP A  1 476 ? -23.707 -33.468 24.510  1.00 19.83  ? 503  ASP A C   1 
ATOM   3790 O O   . ASP A  1 476 ? -23.933 -34.100 23.479  1.00 18.80  ? 503  ASP A O   1 
ATOM   3791 C CB  . ASP A  1 476 ? -25.806 -32.153 24.280  1.00 17.45  ? 503  ASP A CB  1 
ATOM   3792 C CG  . ASP A  1 476 ? -26.701 -32.919 25.229  1.00 19.35  ? 503  ASP A CG  1 
ATOM   3793 O OD1 . ASP A  1 476 ? -26.189 -33.778 25.981  1.00 18.71  ? 503  ASP A OD1 1 
ATOM   3794 O OD2 . ASP A  1 476 ? -27.921 -32.660 25.224  1.00 20.60  1 503  ASP A OD2 1 
ATOM   3795 N N   . LEU A  1 477 ? -22.911 -33.906 25.481  1.00 20.45  ? 504  LEU A N   1 
ATOM   3796 C CA  . LEU A  1 477 ? -22.244 -35.195 25.406  1.00 15.83  ? 504  LEU A CA  1 
ATOM   3797 C C   . LEU A  1 477 ? -22.802 -36.148 26.439  1.00 16.43  ? 504  LEU A C   1 
ATOM   3798 O O   . LEU A  1 477 ? -22.187 -37.166 26.745  1.00 19.01  ? 504  LEU A O   1 
ATOM   3799 C CB  . LEU A  1 477 ? -20.741 -35.036 25.607  1.00 13.07  ? 504  LEU A CB  1 
ATOM   3800 C CG  . LEU A  1 477 ? -19.992 -34.680 24.328  1.00 13.54  ? 504  LEU A CG  1 
ATOM   3801 C CD1 . LEU A  1 477 ? -18.510 -34.468 24.604  1.00 10.57  ? 504  LEU A CD1 1 
ATOM   3802 C CD2 . LEU A  1 477 ? -20.220 -35.760 23.280  1.00 13.31  ? 504  LEU A CD2 1 
ATOM   3803 N N   . SER A  1 478 ? -23.970 -35.818 26.975  1.00 14.40  ? 505  SER A N   1 
ATOM   3804 C CA  . SER A  1 478 ? -24.615 -36.684 27.948  1.00 19.41  ? 505  SER A CA  1 
ATOM   3805 C C   . SER A  1 478 ? -24.944 -38.035 27.326  1.00 24.04  ? 505  SER A C   1 
ATOM   3806 O O   . SER A  1 478 ? -25.196 -38.121 26.123  1.00 25.92  ? 505  SER A O   1 
ATOM   3807 C CB  . SER A  1 478 ? -25.896 -36.039 28.447  1.00 19.01  ? 505  SER A CB  1 
ATOM   3808 O OG  . SER A  1 478 ? -26.785 -35.854 27.368  1.00 18.83  ? 505  SER A OG  1 
ATOM   3809 N N   . TYR A  1 479 ? -24.932 -39.080 28.150  1.00 24.39  ? 506  TYR A N   1 
ATOM   3810 C CA  . TYR A  1 479 ? -25.324 -40.426 27.731  1.00 26.36  ? 506  TYR A CA  1 
ATOM   3811 C C   . TYR A  1 479 ? -24.399 -41.003 26.667  1.00 24.11  ? 506  TYR A C   1 
ATOM   3812 O O   . TYR A  1 479 ? -24.833 -41.733 25.774  1.00 26.17  ? 506  TYR A O   1 
ATOM   3813 C CB  . TYR A  1 479 ? -26.777 -40.461 27.240  1.00 23.08  ? 506  TYR A CB  1 
ATOM   3814 C CG  . TYR A  1 479 ? -27.812 -40.427 28.335  1.00 21.20  ? 506  TYR A CG  1 
ATOM   3815 C CD1 . TYR A  1 479 ? -28.168 -41.582 29.012  1.00 24.99  ? 506  TYR A CD1 1 
ATOM   3816 C CD2 . TYR A  1 479 ? -28.449 -39.243 28.680  1.00 20.89  ? 506  TYR A CD2 1 
ATOM   3817 C CE1 . TYR A  1 479 ? -29.127 -41.559 30.010  1.00 26.26  ? 506  TYR A CE1 1 
ATOM   3818 C CE2 . TYR A  1 479 ? -29.409 -39.213 29.674  1.00 21.34  ? 506  TYR A CE2 1 
ATOM   3819 C CZ  . TYR A  1 479 ? -29.742 -40.374 30.335  1.00 20.41  ? 506  TYR A CZ  1 
ATOM   3820 O OH  . TYR A  1 479 ? -30.690 -40.358 31.328  1.00 17.79  ? 506  TYR A OH  1 
ATOM   3821 N N   . ASN A  1 480 ? -23.121 -40.677 26.761  1.00 18.43  ? 507  ASN A N   1 
ATOM   3822 C CA  . ASN A  1 480 ? -22.152 -41.342 25.919  1.00 25.22  ? 507  ASN A CA  1 
ATOM   3823 C C   . ASN A  1 480 ? -21.345 -42.395 26.671  1.00 29.70  ? 507  ASN A C   1 
ATOM   3824 O O   . ASN A  1 480 ? -21.842 -43.047 27.592  1.00 27.56  ? 507  ASN A O   1 
ATOM   3825 C CB  . ASN A  1 480 ? -21.240 -40.324 25.232  1.00 26.77  ? 507  ASN A CB  1 
ATOM   3826 C CG  . ASN A  1 480 ? -21.919 -39.632 24.064  1.00 23.71  ? 507  ASN A CG  1 
ATOM   3827 O OD1 . ASN A  1 480 ? -21.819 -40.076 22.920  1.00 18.00  ? 507  ASN A OD1 1 
ATOM   3828 N ND2 . ASN A  1 480 ? -22.611 -38.534 24.348  1.00 23.30  ? 507  ASN A ND2 1 
ATOM   3829 N N   . ASN A  1 481 ? -20.095 -42.557 26.261  1.00 26.88  ? 508  ASN A N   1 
ATOM   3830 C CA  . ASN A  1 481 ? -19.227 -43.579 26.825  1.00 26.40  ? 508  ASN A CA  1 
ATOM   3831 C C   . ASN A  1 481 ? -17.815 -43.053 27.058  1.00 30.84  ? 508  ASN A C   1 
ATOM   3832 O O   . ASN A  1 481 ? -16.829 -43.639 26.609  1.00 28.62  ? 508  ASN A O   1 
ATOM   3833 C CB  . ASN A  1 481 ? -19.210 -44.816 25.926  1.00 29.28  ? 508  ASN A CB  1 
ATOM   3834 C CG  . ASN A  1 481 ? -18.722 -46.052 26.651  1.00 45.02  ? 508  ASN A CG  1 
ATOM   3835 O OD1 . ASN A  1 481 ? -18.041 -45.940 27.668  1.00 45.46  ? 508  ASN A OD1 1 
ATOM   3836 N ND2 . ASN A  1 481 ? -19.053 -47.242 26.128  1.00 52.36  ? 508  ASN A ND2 1 
ATOM   3837 N N   . ILE A  1 482 ? -17.749 -41.923 27.753  1.00 32.89  ? 509  ILE A N   1 
ATOM   3838 C CA  . ILE A  1 482 ? -16.503 -41.343 28.209  1.00 25.91  ? 509  ILE A CA  1 
ATOM   3839 C C   . ILE A  1 482 ? -16.262 -41.901 29.600  1.00 31.98  ? 509  ILE A C   1 
ATOM   3840 O O   . ILE A  1 482 ? -17.120 -41.803 30.478  1.00 27.16  ? 509  ILE A O   1 
ATOM   3841 C CB  . ILE A  1 482 ? -16.595 -39.816 28.265  1.00 18.50  ? 509  ILE A CB  1 
ATOM   3842 C CG1 . ILE A  1 482 ? -17.236 -39.287 26.982  1.00 16.57  ? 509  ILE A CG1 1 
ATOM   3843 C CG2 . ILE A  1 482 ? -15.226 -39.212 28.490  1.00 26.69  ? 509  ILE A CG2 1 
ATOM   3844 C CD1 . ILE A  1 482 ? -17.136 -37.796 26.805  1.00 11.70  ? 509  ILE A CD1 1 
ATOM   3845 N N   . SER A  1 483 ? -15.092 -42.501 29.785  1.00 33.78  ? 510  SER A N   1 
ATOM   3846 C CA  . SER A  1 483 ? -14.801 -43.262 30.991  1.00 28.65  ? 510  SER A CA  1 
ATOM   3847 C C   . SER A  1 483 ? -13.950 -42.501 32.002  1.00 31.91  ? 510  SER A C   1 
ATOM   3848 O O   . SER A  1 483 ? -13.981 -42.805 33.195  1.00 33.81  ? 510  SER A O   1 
ATOM   3849 C CB  . SER A  1 483 ? -14.100 -44.564 30.618  1.00 29.16  ? 510  SER A CB  1 
ATOM   3850 O OG  . SER A  1 483 ? -13.014 -44.302 29.744  1.00 31.22  ? 510  SER A OG  1 
ATOM   3851 N N   . SER A  1 484 ? -13.188 -41.521 31.525  1.00 31.73  ? 511  SER A N   1 
ATOM   3852 C CA  . SER A  1 484 ? -12.265 -40.787 32.382  1.00 28.34  ? 511  SER A CA  1 
ATOM   3853 C C   . SER A  1 484 ? -12.005 -39.387 31.851  1.00 32.99  ? 511  SER A C   1 
ATOM   3854 O O   . SER A  1 484 ? -11.908 -39.177 30.638  1.00 35.05  ? 511  SER A O   1 
ATOM   3855 C CB  . SER A  1 484 ? -10.937 -41.533 32.487  1.00 28.74  ? 511  SER A CB  1 
ATOM   3856 O OG  . SER A  1 484 ? -10.255 -41.524 31.243  1.00 22.41  ? 511  SER A OG  1 
ATOM   3857 N N   . LEU A  1 485 ? -11.882 -38.433 32.769  1.00 32.48  ? 512  LEU A N   1 
ATOM   3858 C CA  . LEU A  1 485 ? -11.546 -37.062 32.408  1.00 33.52  ? 512  LEU A CA  1 
ATOM   3859 C C   . LEU A  1 485 ? -10.141 -36.713 32.866  1.00 35.73  ? 512  LEU A C   1 
ATOM   3860 O O   . LEU A  1 485 ? -9.619  -37.319 33.799  1.00 33.76  ? 512  LEU A O   1 
ATOM   3861 C CB  . LEU A  1 485 ? -12.529 -36.081 33.041  1.00 28.73  ? 512  LEU A CB  1 
ATOM   3862 C CG  . LEU A  1 485 ? -14.000 -36.231 32.669  1.00 35.59  ? 512  LEU A CG  1 
ATOM   3863 C CD1 . LEU A  1 485 ? -14.834 -35.149 33.339  1.00 31.86  ? 512  LEU A CD1 1 
ATOM   3864 C CD2 . LEU A  1 485 ? -14.172 -36.189 31.157  1.00 48.28  ? 512  LEU A CD2 1 
ATOM   3865 N N   . GLY A  1 486 ? -9.539  -35.739 32.189  1.00 42.27  ? 513  GLY A N   1 
ATOM   3866 C CA  . GLY A  1 486 ? -8.303  -35.112 32.630  1.00 38.91  ? 513  GLY A CA  1 
ATOM   3867 C C   . GLY A  1 486 ? -8.533  -33.613 32.594  1.00 41.27  ? 513  GLY A C   1 
ATOM   3868 O O   . GLY A  1 486 ? -9.499  -33.160 31.983  1.00 45.93  ? 513  GLY A O   1 
ATOM   3869 N N   . TYR A  1 487 ? -7.663  -32.832 33.229  1.00 42.12  ? 514  TYR A N   1 
ATOM   3870 C CA  . TYR A  1 487 ? -7.858  -31.379 33.276  1.00 47.54  ? 514  TYR A CA  1 
ATOM   3871 C C   . TYR A  1 487 ? -7.819  -30.732 31.886  1.00 44.16  ? 514  TYR A C   1 
ATOM   3872 O O   . TYR A  1 487 ? -8.144  -29.557 31.734  1.00 43.18  ? 514  TYR A O   1 
ATOM   3873 C CB  . TYR A  1 487 ? -6.840  -30.707 34.211  1.00 54.81  ? 514  TYR A CB  1 
ATOM   3874 C CG  . TYR A  1 487 ? -5.437  -30.621 33.642  1.00 57.67  ? 514  TYR A CG  1 
ATOM   3875 C CD1 . TYR A  1 487 ? -4.548  -31.681 33.770  1.00 57.38  ? 514  TYR A CD1 1 
ATOM   3876 C CD2 . TYR A  1 487 ? -5.003  -29.481 32.977  1.00 55.90  ? 514  TYR A CD2 1 
ATOM   3877 C CE1 . TYR A  1 487 ? -3.270  -31.610 33.248  1.00 53.11  ? 514  TYR A CE1 1 
ATOM   3878 C CE2 . TYR A  1 487 ? -3.725  -29.404 32.452  1.00 55.05  ? 514  TYR A CE2 1 
ATOM   3879 C CZ  . TYR A  1 487 ? -2.864  -30.470 32.590  1.00 53.09  ? 514  TYR A CZ  1 
ATOM   3880 O OH  . TYR A  1 487 ? -1.591  -30.398 32.069  1.00 54.36  ? 514  TYR A OH  1 
ATOM   3881 N N   . GLU A  1 488 ? -7.411  -31.504 30.883  1.00 47.55  ? 515  GLU A N   1 
ATOM   3882 C CA  . GLU A  1 488 ? -7.368  -31.034 29.501  1.00 47.60  ? 515  GLU A CA  1 
ATOM   3883 C C   . GLU A  1 488 ? -8.706  -31.305 28.823  1.00 48.48  ? 515  GLU A C   1 
ATOM   3884 O O   . GLU A  1 488 ? -8.997  -30.769 27.750  1.00 49.06  ? 515  GLU A O   1 
ATOM   3885 C CB  . GLU A  1 488 ? -6.250  -31.734 28.724  1.00 49.49  ? 515  GLU A CB  1 
ATOM   3886 C CG  . GLU A  1 488 ? -4.912  -31.806 29.446  1.00 49.45  ? 515  GLU A CG  1 
ATOM   3887 C CD  . GLU A  1 488 ? -4.782  -33.030 30.339  1.00 47.94  ? 515  GLU A CD  1 
ATOM   3888 O OE1 . GLU A  1 488 ? -5.816  -33.610 30.737  1.00 48.34  ? 515  GLU A OE1 1 
ATOM   3889 O OE2 . GLU A  1 488 ? -3.636  -33.415 30.642  1.00 53.39  1 515  GLU A OE2 1 
ATOM   3890 N N   . ASP A  1 489 ? -9.513  -32.150 29.455  1.00 43.84  ? 516  ASP A N   1 
ATOM   3891 C CA  . ASP A  1 489 ? -10.856 -32.437 28.972  1.00 39.23  ? 516  ASP A CA  1 
ATOM   3892 C C   . ASP A  1 489 ? -11.845 -31.372 29.437  1.00 45.70  ? 516  ASP A C   1 
ATOM   3893 O O   . ASP A  1 489 ? -13.053 -31.497 29.224  1.00 41.46  ? 516  ASP A O   1 
ATOM   3894 C CB  . ASP A  1 489 ? -11.305 -33.812 29.451  1.00 32.45  ? 516  ASP A CB  1 
ATOM   3895 C CG  . ASP A  1 489 ? -10.461 -34.916 28.882  1.00 36.74  ? 516  ASP A CG  1 
ATOM   3896 O OD1 . ASP A  1 489 ? -9.876  -34.707 27.797  1.00 37.99  ? 516  ASP A OD1 1 
ATOM   3897 O OD2 . ASP A  1 489 ? -10.384 -35.989 29.516  1.00 43.44  1 516  ASP A OD2 1 
ATOM   3898 N N   . LEU A  1 490 ? -11.323 -30.329 30.076  1.00 42.16  ? 517  LEU A N   1 
ATOM   3899 C CA  . LEU A  1 490 ? -12.144 -29.225 30.552  1.00 35.26  ? 517  LEU A CA  1 
ATOM   3900 C C   . LEU A  1 490 ? -11.579 -27.883 30.092  1.00 41.80  ? 517  LEU A C   1 
ATOM   3901 O O   . LEU A  1 490 ? -11.795 -26.857 30.734  1.00 48.05  ? 517  LEU A O   1 
ATOM   3902 C CB  . LEU A  1 490 ? -12.252 -29.271 32.075  1.00 28.31  ? 517  LEU A CB  1 
ATOM   3903 C CG  . LEU A  1 490 ? -12.970 -30.505 32.619  1.00 28.46  ? 517  LEU A CG  1 
ATOM   3904 C CD1 . LEU A  1 490 ? -12.844 -30.591 34.122  1.00 38.67  ? 517  LEU A CD1 1 
ATOM   3905 C CD2 . LEU A  1 490 ? -14.425 -30.471 32.226  1.00 29.71  ? 517  LEU A CD2 1 
ATOM   3906 N N   . ALA A  1 491 ? -10.868 -27.899 28.967  1.00 44.18  ? 518  ALA A N   1 
ATOM   3907 C CA  . ALA A  1 491 ? -10.191 -26.709 28.457  1.00 41.84  ? 518  ALA A CA  1 
ATOM   3908 C C   . ALA A  1 491 ? -10.882 -26.128 27.231  1.00 43.97  ? 518  ALA A C   1 
ATOM   3909 O O   . ALA A  1 491 ? -10.333 -26.177 26.133  1.00 53.23  ? 518  ALA A O   1 
ATOM   3910 C CB  . ALA A  1 491 ? -8.744  -27.033 28.122  1.00 32.50  ? 518  ALA A CB  1 
ATOM   3911 N N   . PHE A  1 492 ? -12.070 -25.564 27.411  1.00 34.74  ? 519  PHE A N   1 
ATOM   3912 C CA  . PHE A  1 492 ? -12.816 -25.045 26.271  1.00 40.16  ? 519  PHE A CA  1 
ATOM   3913 C C   . PHE A  1 492 ? -12.588 -23.555 26.004  1.00 41.28  ? 519  PHE A C   1 
ATOM   3914 O O   . PHE A  1 492 ? -12.962 -22.696 26.806  1.00 40.74  ? 519  PHE A O   1 
ATOM   3915 C CB  . PHE A  1 492 ? -14.307 -25.345 26.423  1.00 47.09  ? 519  PHE A CB  1 
ATOM   3916 C CG  . PHE A  1 492 ? -14.637 -26.812 26.397  1.00 41.72  ? 519  PHE A CG  1 
ATOM   3917 C CD1 . PHE A  1 492 ? -14.814 -27.476 25.194  1.00 36.76  ? 519  PHE A CD1 1 
ATOM   3918 C CD2 . PHE A  1 492 ? -14.778 -27.525 27.576  1.00 38.56  ? 519  PHE A CD2 1 
ATOM   3919 C CE1 . PHE A  1 492 ? -15.123 -28.823 25.169  1.00 31.53  ? 519  PHE A CE1 1 
ATOM   3920 C CE2 . PHE A  1 492 ? -15.088 -28.873 27.555  1.00 33.14  ? 519  PHE A CE2 1 
ATOM   3921 C CZ  . PHE A  1 492 ? -15.259 -29.522 26.350  1.00 30.72  ? 519  PHE A CZ  1 
ATOM   3922 N N   . LEU A  1 493 ? -11.985 -23.266 24.855  1.00 41.47  ? 520  LEU A N   1 
ATOM   3923 C CA  . LEU A  1 493 ? -11.699 -21.897 24.434  1.00 47.43  ? 520  LEU A CA  1 
ATOM   3924 C C   . LEU A  1 493 ? -12.924 -21.203 23.848  1.00 40.85  ? 520  LEU A C   1 
ATOM   3925 O O   . LEU A  1 493 ? -12.892 -20.741 22.706  1.00 34.14  ? 520  LEU A O   1 
ATOM   3926 C CB  . LEU A  1 493 ? -10.590 -21.890 23.379  1.00 47.21  ? 520  LEU A CB  1 
ATOM   3927 C CG  . LEU A  1 493 ? -9.124  -21.852 23.806  1.00 42.85  ? 520  LEU A CG  1 
ATOM   3928 C CD1 . LEU A  1 493 ? -8.804  -22.945 24.809  1.00 45.22  ? 520  LEU A CD1 1 
ATOM   3929 C CD2 . LEU A  1 493 ? -8.246  -21.980 22.572  1.00 44.64  ? 520  LEU A CD2 1 
ATOM   3930 N N   . SER A  1 494 ? -13.999 -21.126 24.623  1.00 41.10  ? 521  SER A N   1 
ATOM   3931 C CA  . SER A  1 494 ? -15.213 -20.474 24.147  1.00 49.62  ? 521  SER A CA  1 
ATOM   3932 C C   . SER A  1 494 ? -15.595 -19.294 25.026  1.00 53.15  ? 521  SER A C   1 
ATOM   3933 O O   . SER A  1 494 ? -15.979 -19.464 26.184  1.00 54.04  ? 521  SER A O   1 
ATOM   3934 C CB  . SER A  1 494 ? -16.377 -21.467 24.040  1.00 43.69  ? 521  SER A CB  1 
ATOM   3935 O OG  . SER A  1 494 ? -16.242 -22.292 22.892  1.00 34.71  ? 521  SER A OG  1 
ATOM   3936 N N   . GLN A  1 495 ? -15.484 -18.095 24.461  1.00 54.36  ? 522  GLN A N   1 
ATOM   3937 C CA  . GLN A  1 495 ? -15.876 -16.873 25.156  1.00 63.44  ? 522  GLN A CA  1 
ATOM   3938 C C   . GLN A  1 495 ? -17.369 -16.610 24.981  1.00 57.33  ? 522  GLN A C   1 
ATOM   3939 O O   . GLN A  1 495 ? -17.807 -15.461 24.910  1.00 53.52  ? 522  GLN A O   1 
ATOM   3940 C CB  . GLN A  1 495 ? -15.062 -15.680 24.642  1.00 63.27  ? 522  GLN A CB  1 
ATOM   3941 C CG  . GLN A  1 495 ? -13.672 -15.550 25.254  1.00 56.64  ? 522  GLN A CG  1 
ATOM   3942 C CD  . GLN A  1 495 ? -13.704 -15.038 26.688  1.00 57.54  ? 522  GLN A CD  1 
ATOM   3943 O OE1 . GLN A  1 495 ? -14.239 -15.691 27.589  1.00 47.93  ? 522  GLN A OE1 1 
ATOM   3944 N NE2 . GLN A  1 495 ? -13.132 -13.860 26.902  1.00 55.75  ? 522  GLN A NE2 1 
ATOM   3945 N N   . ASN A  1 496 ? -18.146 -17.685 24.928  1.00 56.85  ? 523  ASN A N   1 
ATOM   3946 C CA  . ASN A  1 496 ? -19.553 -17.592 24.575  1.00 54.62  ? 523  ASN A CA  1 
ATOM   3947 C C   . ASN A  1 496 ? -20.420 -18.554 25.379  1.00 47.20  ? 523  ASN A C   1 
ATOM   3948 O O   . ASN A  1 496 ? -20.868 -19.570 24.851  1.00 46.58  ? 523  ASN A O   1 
ATOM   3949 C CB  . ASN A  1 496 ? -19.719 -17.858 23.076  1.00 55.01  ? 523  ASN A CB  1 
ATOM   3950 C CG  . ASN A  1 496 ? -21.114 -17.556 22.580  1.00 48.16  ? 523  ASN A CG  1 
ATOM   3951 O OD1 . ASN A  1 496 ? -21.877 -16.844 23.233  1.00 48.46  ? 523  ASN A OD1 1 
ATOM   3952 N ND2 . ASN A  1 496 ? -21.455 -18.097 21.416  1.00 42.73  ? 523  ASN A ND2 1 
ATOM   3953 N N   . ARG A  1 497 ? -20.635 -18.215 26.652  1.00 48.93  ? 524  ARG A N   1 
ATOM   3954 C CA  . ARG A  1 497 ? -21.497 -18.958 27.584  1.00 49.02  ? 524  ARG A CA  1 
ATOM   3955 C C   . ARG A  1 497 ? -21.718 -20.428 27.253  1.00 43.83  ? 524  ARG A C   1 
ATOM   3956 O O   . ARG A  1 497 ? -22.858 -20.874 27.111  1.00 43.13  ? 524  ARG A O   1 
ATOM   3957 C CB  . ARG A  1 497 ? -22.854 -18.267 27.731  1.00 51.78  ? 524  ARG A CB  1 
ATOM   3958 C CG  . ARG A  1 497 ? -22.834 -17.009 28.588  1.00 57.31  ? 524  ARG A CG  1 
ATOM   3959 C CD  . ARG A  1 497 ? -24.193 -16.319 28.596  1.00 60.99  ? 524  ARG A CD  1 
ATOM   3960 N NE  . ARG A  1 497 ? -24.530 -15.740 27.296  1.00 68.96  ? 524  ARG A NE  1 
ATOM   3961 C CZ  . ARG A  1 497 ? -25.287 -16.336 26.377  1.00 70.42  ? 524  ARG A CZ  1 
ATOM   3962 N NH1 . ARG A  1 497 ? -25.534 -15.725 25.226  1.00 72.58  1 524  ARG A NH1 1 
ATOM   3963 N NH2 . ARG A  1 497 ? -25.798 -17.539 26.605  1.00 65.80  ? 524  ARG A NH2 1 
ATOM   3964 N N   . LEU A  1 498 ? -20.624 -21.170 27.118  1.00 41.49  ? 525  LEU A N   1 
ATOM   3965 C CA  . LEU A  1 498 ? -20.703 -22.586 26.789  1.00 38.40  ? 525  LEU A CA  1 
ATOM   3966 C C   . LEU A  1 498 ? -21.201 -23.419 27.972  1.00 37.18  ? 525  LEU A C   1 
ATOM   3967 O O   . LEU A  1 498 ? -20.702 -23.289 29.093  1.00 37.66  ? 525  LEU A O   1 
ATOM   3968 C CB  . LEU A  1 498 ? -19.344 -23.093 26.306  1.00 34.86  ? 525  LEU A CB  1 
ATOM   3969 C CG  . LEU A  1 498 ? -19.217 -24.598 26.072  1.00 31.89  ? 525  LEU A CG  1 
ATOM   3970 C CD1 . LEU A  1 498 ? -20.286 -25.089 25.115  1.00 31.72  ? 525  LEU A CD1 1 
ATOM   3971 C CD2 . LEU A  1 498 ? -17.835 -24.924 25.537  1.00 35.88  ? 525  LEU A CD2 1 
ATOM   3972 N N   . HIS A  1 499 ? -22.197 -24.263 27.714  1.00 32.87  ? 526  HIS A N   1 
ATOM   3973 C CA  . HIS A  1 499 ? -22.707 -25.193 28.716  1.00 31.41  ? 526  HIS A CA  1 
ATOM   3974 C C   . HIS A  1 499 ? -22.620 -26.635 28.227  1.00 28.95  ? 526  HIS A C   1 
ATOM   3975 O O   . HIS A  1 499 ? -23.483 -27.111 27.486  1.00 29.46  ? 526  HIS A O   1 
ATOM   3976 C CB  . HIS A  1 499 ? -24.152 -24.870 29.081  1.00 32.71  ? 526  HIS A CB  1 
ATOM   3977 C CG  . HIS A  1 499 ? -24.295 -23.765 30.079  1.00 31.59  ? 526  HIS A CG  1 
ATOM   3978 N ND1 . HIS A  1 499 ? -23.824 -22.490 29.852  1.00 35.41  ? 526  HIS A ND1 1 
ATOM   3979 C CD2 . HIS A  1 499 ? -24.875 -23.741 31.302  1.00 32.52  ? 526  HIS A CD2 1 
ATOM   3980 C CE1 . HIS A  1 499 ? -24.103 -21.729 30.896  1.00 38.91  ? 526  HIS A CE1 1 
ATOM   3981 N NE2 . HIS A  1 499 ? -24.741 -22.463 31.789  1.00 37.72  ? 526  HIS A NE2 1 
ATOM   3982 N N   . VAL A  1 500 ? -21.574 -27.325 28.659  1.00 23.33  ? 527  VAL A N   1 
ATOM   3983 C CA  . VAL A  1 500 ? -21.346 -28.708 28.285  1.00 19.76  ? 527  VAL A CA  1 
ATOM   3984 C C   . VAL A  1 500 ? -22.073 -29.669 29.218  1.00 22.83  ? 527  VAL A C   1 
ATOM   3985 O O   . VAL A  1 500 ? -22.004 -29.533 30.437  1.00 28.71  ? 527  VAL A O   1 
ATOM   3986 C CB  . VAL A  1 500 ? -19.849 -29.016 28.308  1.00 22.22  ? 527  VAL A CB  1 
ATOM   3987 C CG1 . VAL A  1 500 ? -19.599 -30.518 28.283  1.00 22.98  ? 527  VAL A CG1 1 
ATOM   3988 C CG2 . VAL A  1 500 ? -19.162 -28.316 27.146  1.00 29.08  ? 527  VAL A CG2 1 
ATOM   3989 N N   . ASN A  1 501 ? -22.775 -30.639 28.640  1.00 20.29  ? 528  ASN A N   1 
ATOM   3990 C CA  . ASN A  1 501 ? -23.480 -31.640 29.429  1.00 19.15  ? 528  ASN A CA  1 
ATOM   3991 C C   . ASN A  1 501 ? -22.778 -32.983 29.329  1.00 21.70  ? 528  ASN A C   1 
ATOM   3992 O O   . ASN A  1 501 ? -22.679 -33.553 28.242  1.00 22.21  ? 528  ASN A O   1 
ATOM   3993 C CB  . ASN A  1 501 ? -24.925 -31.770 28.950  1.00 21.39  ? 528  ASN A CB  1 
ATOM   3994 C CG  . ASN A  1 501 ? -25.876 -32.178 30.060  1.00 24.96  ? 528  ASN A CG  1 
ATOM   3995 O OD1 . ASN A  1 501 ? -25.557 -33.043 30.877  1.00 22.52  ? 528  ASN A OD1 1 
ATOM   3996 N ND2 . ASN A  1 501 ? -27.056 -31.544 30.095  1.00 28.63  ? 528  ASN A ND2 1 
ATOM   3997 N N   . MET A  1 502 ? -22.284 -33.482 30.461  1.00 24.72  ? 529  MET A N   1 
ATOM   3998 C CA  . MET A  1 502 ? -21.600 -34.773 30.504  1.00 19.24  ? 529  MET A CA  1 
ATOM   3999 C C   . MET A  1 502 ? -22.272 -35.735 31.473  1.00 19.24  ? 529  MET A C   1 
ATOM   4000 O O   . MET A  1 502 ? -21.611 -36.585 32.065  1.00 22.03  ? 529  MET A O   1 
ATOM   4001 C CB  . MET A  1 502 ? -20.134 -34.605 30.901  1.00 16.87  ? 529  MET A CB  1 
ATOM   4002 C CG  . MET A  1 502 ? -19.297 -33.778 29.936  1.00 22.65  ? 529  MET A CG  1 
ATOM   4003 S SD  . MET A  1 502 ? -17.545 -33.797 30.391  1.00 38.17  ? 529  MET A SD  1 
ATOM   4004 C CE  . MET A  1 502 ? -16.833 -32.687 29.177  1.00 29.98  ? 529  MET A CE  1 
ATOM   4005 N N   . THR A  1 503 ? -23.585 -35.598 31.627  1.00 18.51  ? 530  THR A N   1 
ATOM   4006 C CA  . THR A  1 503 ? -24.358 -36.458 32.517  1.00 21.62  ? 530  THR A CA  1 
ATOM   4007 C C   . THR A  1 503 ? -24.499 -37.891 32.004  1.00 22.96  ? 530  THR A C   1 
ATOM   4008 O O   . THR A  1 503 ? -24.440 -38.141 30.802  1.00 21.44  ? 530  THR A O   1 
ATOM   4009 C CB  . THR A  1 503 ? -25.770 -35.895 32.742  1.00 26.50  ? 530  THR A CB  1 
ATOM   4010 O OG1 . THR A  1 503 ? -26.111 -35.021 31.659  1.00 25.41  ? 530  THR A OG1 1 
ATOM   4011 C CG2 . THR A  1 503 ? -25.839 -35.121 34.042  1.00 30.03  ? 530  THR A CG2 1 
ATOM   4012 N N   . HIS A  1 504 ? -24.689 -38.819 32.938  1.00 25.56  ? 531  HIS A N   1 
ATOM   4013 C CA  . HIS A  1 504 ? -24.960 -40.230 32.640  1.00 26.35  ? 531  HIS A CA  1 
ATOM   4014 C C   . HIS A  1 504 ? -23.985 -40.913 31.678  1.00 25.67  ? 531  HIS A C   1 
ATOM   4015 O O   . HIS A  1 504 ? -24.400 -41.639 30.775  1.00 30.29  ? 531  HIS A O   1 
ATOM   4016 C CB  . HIS A  1 504 ? -26.391 -40.413 32.136  1.00 21.39  ? 531  HIS A CB  1 
ATOM   4017 C CG  . HIS A  1 504 ? -27.435 -39.933 33.090  1.00 24.55  ? 531  HIS A CG  1 
ATOM   4018 N ND1 . HIS A  1 504 ? -27.594 -38.602 33.413  1.00 29.74  ? 531  HIS A ND1 1 
ATOM   4019 C CD2 . HIS A  1 504 ? -28.381 -40.604 33.788  1.00 31.82  ? 531  HIS A CD2 1 
ATOM   4020 C CE1 . HIS A  1 504 ? -28.593 -38.474 34.266  1.00 34.61  ? 531  HIS A CE1 1 
ATOM   4021 N NE2 . HIS A  1 504 ? -29.088 -39.675 34.512  1.00 37.73  ? 531  HIS A NE2 1 
ATOM   4022 N N   . ASN A  1 505 ? -22.693 -40.696 31.872  1.00 21.05  ? 532  ASN A N   1 
ATOM   4023 C CA  . ASN A  1 505 ? -21.714 -41.416 31.078  1.00 24.05  ? 532  ASN A CA  1 
ATOM   4024 C C   . ASN A  1 505 ? -21.124 -42.602 31.827  1.00 28.06  ? 532  ASN A C   1 
ATOM   4025 O O   . ASN A  1 505 ? -21.807 -43.278 32.599  1.00 23.08  ? 532  ASN A O   1 
ATOM   4026 C CB  . ASN A  1 505 ? -20.609 -40.480 30.598  1.00 23.18  ? 532  ASN A CB  1 
ATOM   4027 C CG  . ASN A  1 505 ? -21.057 -39.597 29.454  1.00 25.47  ? 532  ASN A CG  1 
ATOM   4028 O OD1 . ASN A  1 505 ? -20.652 -39.789 28.307  1.00 24.29  ? 532  ASN A OD1 1 
ATOM   4029 N ND2 . ASN A  1 505 ? -21.909 -38.627 29.758  1.00 25.93  ? 532  ASN A ND2 1 
ATOM   4030 N N   . LYS A  1 506 ? -19.846 -42.849 31.582  1.00 30.67  ? 533  LYS A N   1 
ATOM   4031 C CA  . LYS A  1 506 ? -19.147 -43.944 32.223  1.00 33.42  ? 533  LYS A CA  1 
ATOM   4032 C C   . LYS A  1 506 ? -17.916 -43.400 32.923  1.00 34.24  ? 533  LYS A C   1 
ATOM   4033 O O   . LYS A  1 506 ? -16.931 -44.112 33.086  1.00 36.27  ? 533  LYS A O   1 
ATOM   4034 C CB  . LYS A  1 506 ? -18.731 -44.980 31.180  1.00 37.18  ? 533  LYS A CB  1 
ATOM   4035 C CG  . LYS A  1 506 ? -19.875 -45.474 30.312  1.00 31.62  ? 533  LYS A CG  1 
ATOM   4036 C CD  . LYS A  1 506 ? -20.328 -46.859 30.724  1.00 24.01  ? 533  LYS A CD  1 
ATOM   4037 C CE  . LYS A  1 506 ? -21.816 -46.876 30.972  1.00 24.09  ? 533  LYS A CE  1 
ATOM   4038 N NZ  . LYS A  1 506 ? -22.534 -46.111 29.918  1.00 39.94  1 533  LYS A NZ  1 
ATOM   4039 N N   . ILE A  1 507 ? -17.969 -42.133 33.324  1.00 31.90  ? 534  ILE A N   1 
ATOM   4040 C CA  . ILE A  1 507 ? -16.836 -41.501 33.988  1.00 29.71  ? 534  ILE A CA  1 
ATOM   4041 C C   . ILE A  1 507 ? -16.636 -42.112 35.365  1.00 32.45  ? 534  ILE A C   1 
ATOM   4042 O O   . ILE A  1 507 ? -17.370 -41.800 36.303  1.00 34.70  ? 534  ILE A O   1 
ATOM   4043 C CB  . ILE A  1 507 ? -17.027 -39.984 34.113  1.00 26.17  ? 534  ILE A CB  1 
ATOM   4044 C CG1 . ILE A  1 507 ? -17.184 -39.357 32.731  1.00 26.15  ? 534  ILE A CG1 1 
ATOM   4045 C CG2 . ILE A  1 507 ? -15.851 -39.351 34.824  1.00 33.08  ? 534  ILE A CG2 1 
ATOM   4046 C CD1 . ILE A  1 507 ? -17.220 -37.859 32.761  1.00 23.83  ? 534  ILE A CD1 1 
ATOM   4047 N N   . ARG A  1 508 ? -15.647 -42.993 35.477  1.00 31.77  ? 535  ARG A N   1 
ATOM   4048 C CA  . ARG A  1 508 ? -15.412 -43.715 36.722  1.00 38.99  ? 535  ARG A CA  1 
ATOM   4049 C C   . ARG A  1 508 ? -14.304 -43.073 37.540  1.00 41.82  ? 535  ARG A C   1 
ATOM   4050 O O   . ARG A  1 508 ? -14.098 -43.428 38.698  1.00 45.77  ? 535  ARG A O   1 
ATOM   4051 C CB  . ARG A  1 508 ? -15.087 -45.187 36.451  1.00 42.06  ? 535  ARG A CB  1 
ATOM   4052 C CG  . ARG A  1 508 ? -16.061 -45.855 35.493  1.00 48.75  ? 535  ARG A CG  1 
ATOM   4053 C CD  . ARG A  1 508 ? -16.323 -47.312 35.837  1.00 49.59  ? 535  ARG A CD  1 
ATOM   4054 N NE  . ARG A  1 508 ? -17.205 -47.450 36.992  1.00 55.89  ? 535  ARG A NE  1 
ATOM   4055 C CZ  . ARG A  1 508 ? -16.794 -47.795 38.208  1.00 66.75  ? 535  ARG A CZ  1 
ATOM   4056 N NH1 . ARG A  1 508 ? -15.508 -48.045 38.420  1.00 64.34  1 535  ARG A NH1 1 
ATOM   4057 N NH2 . ARG A  1 508 ? -17.665 -47.898 39.208  1.00 55.94  ? 535  ARG A NH2 1 
ATOM   4058 N N   . ARG A  1 509 ? -13.597 -42.126 36.932  1.00 41.36  ? 536  ARG A N   1 
ATOM   4059 C CA  . ARG A  1 509 ? -12.551 -41.386 37.628  1.00 41.22  ? 536  ARG A CA  1 
ATOM   4060 C C   . ARG A  1 509 ? -12.340 -40.011 37.009  1.00 36.20  ? 536  ARG A C   1 
ATOM   4061 O O   . ARG A  1 509 ? -12.607 -39.807 35.827  1.00 40.51  ? 536  ARG A O   1 
ATOM   4062 C CB  . ARG A  1 509 ? -11.237 -42.173 37.633  1.00 49.78  ? 536  ARG A CB  1 
ATOM   4063 C CG  . ARG A  1 509 ? -10.757 -42.617 36.256  1.00 54.73  ? 536  ARG A CG  1 
ATOM   4064 C CD  . ARG A  1 509 ? -9.344  -43.182 36.326  1.00 63.75  ? 536  ARG A CD  1 
ATOM   4065 N NE  . ARG A  1 509 ? -9.251  -44.301 37.259  1.00 69.47  ? 536  ARG A NE  1 
ATOM   4066 C CZ  . ARG A  1 509 ? -8.158  -44.613 37.950  1.00 65.64  ? 536  ARG A CZ  1 
ATOM   4067 N NH1 . ARG A  1 509 ? -7.056  -43.886 37.818  1.00 59.33  1 536  ARG A NH1 1 
ATOM   4068 N NH2 . ARG A  1 509 ? -8.170  -45.649 38.778  1.00 58.90  ? 536  ARG A NH2 1 
ATOM   4069 N N   . ILE A  1 510 ? -11.867 -39.068 37.818  1.00 38.37  ? 537  ILE A N   1 
ATOM   4070 C CA  . ILE A  1 510 ? -11.521 -37.730 37.339  1.00 37.18  ? 537  ILE A CA  1 
ATOM   4071 C C   . ILE A  1 510 ? -10.135 -37.309 37.834  1.00 43.36  ? 537  ILE A C   1 
ATOM   4072 O O   . ILE A  1 510 ? -9.986  -36.803 38.947  1.00 47.34  ? 537  ILE A O   1 
ATOM   4073 C CB  . ILE A  1 510 ? -12.557 -36.688 37.781  1.00 29.07  ? 537  ILE A CB  1 
ATOM   4074 C CG1 . ILE A  1 510 ? -13.955 -37.103 37.318  1.00 31.12  ? 537  ILE A CG1 1 
ATOM   4075 C CG2 . ILE A  1 510 ? -12.191 -35.319 37.238  1.00 31.61  ? 537  ILE A CG2 1 
ATOM   4076 C CD1 . ILE A  1 510 ? -15.047 -36.129 37.693  1.00 30.67  ? 537  ILE A CD1 1 
ATOM   4077 N N   . ALA A  1 511 ? -9.121  -37.522 37.000  1.00 44.22  ? 538  ALA A N   1 
ATOM   4078 C CA  . ALA A  1 511 ? -7.739  -37.253 37.386  1.00 40.33  ? 538  ALA A CA  1 
ATOM   4079 C C   . ALA A  1 511 ? -7.415  -35.768 37.364  1.00 43.49  ? 538  ALA A C   1 
ATOM   4080 O O   . ALA A  1 511 ? -7.042  -35.218 36.327  1.00 38.12  ? 538  ALA A O   1 
ATOM   4081 C CB  . ALA A  1 511 ? -6.778  -38.011 36.489  1.00 39.17  ? 538  ALA A CB  1 
ATOM   4082 N N   . LEU A  1 512 ? -7.554  -35.129 38.519  1.00 53.00  ? 539  LEU A N   1 
ATOM   4083 C CA  . LEU A  1 512 ? -7.196  -33.725 38.667  1.00 56.63  ? 539  LEU A CA  1 
ATOM   4084 C C   . LEU A  1 512 ? -5.933  -33.585 39.504  1.00 58.60  ? 539  LEU A C   1 
ATOM   4085 O O   . LEU A  1 512 ? -5.805  -34.225 40.549  1.00 62.51  ? 539  LEU A O   1 
ATOM   4086 C CB  . LEU A  1 512 ? -8.344  -32.941 39.298  1.00 51.96  ? 539  LEU A CB  1 
ATOM   4087 C CG  . LEU A  1 512 ? -9.528  -32.715 38.361  1.00 45.19  ? 539  LEU A CG  1 
ATOM   4088 C CD1 . LEU A  1 512 ? -10.627 -31.957 39.075  1.00 36.70  ? 539  LEU A CD1 1 
ATOM   4089 C CD2 . LEU A  1 512 ? -9.073  -31.972 37.110  1.00 44.75  ? 539  LEU A CD2 1 
ATOM   4090 N N   . PRO A  1 513 ? -4.986  -32.764 39.030  1.00 51.97  ? 540  PRO A N   1 
ATOM   4091 C CA  . PRO A  1 513 ? -3.717  -32.523 39.717  1.00 61.77  ? 540  PRO A CA  1 
ATOM   4092 C C   . PRO A  1 513 ? -3.684  -31.200 40.488  1.00 70.57  ? 540  PRO A C   1 
ATOM   4093 O O   . PRO A  1 513 ? -4.498  -30.309 40.241  1.00 68.86  ? 540  PRO A O   1 
ATOM   4094 C CB  . PRO A  1 513 ? -2.731  -32.457 38.557  1.00 57.42  ? 540  PRO A CB  1 
ATOM   4095 C CG  . PRO A  1 513 ? -3.524  -31.805 37.468  1.00 56.04  ? 540  PRO A CG  1 
ATOM   4096 C CD  . PRO A  1 513 ? -4.963  -32.239 37.653  1.00 50.53  ? 540  PRO A CD  1 
ATOM   4097 N N   . GLU A  1 514 ? -2.746  -31.090 41.427  1.00 72.85  ? 541  GLU A N   1 
ATOM   4098 C CA  . GLU A  1 514 ? -2.430  -29.820 42.070  1.00 71.59  ? 541  GLU A CA  1 
ATOM   4099 C C   . GLU A  1 514 ? -1.535  -29.054 41.107  1.00 72.71  ? 541  GLU A C   1 
ATOM   4100 O O   . GLU A  1 514 ? -0.485  -29.556 40.707  1.00 68.73  ? 541  GLU A O   1 
ATOM   4101 C CB  . GLU A  1 514 ? -1.700  -30.067 43.392  1.00 71.21  ? 541  GLU A CB  1 
ATOM   4102 C CG  . GLU A  1 514 ? -1.194  -28.811 44.099  1.00 76.34  ? 541  GLU A CG  1 
ATOM   4103 C CD  . GLU A  1 514 ? -0.321  -29.134 45.307  1.00 77.17  ? 541  GLU A CD  1 
ATOM   4104 O OE1 . GLU A  1 514 ? -0.181  -30.330 45.641  1.00 74.13  ? 541  GLU A OE1 1 
ATOM   4105 O OE2 . GLU A  1 514 ? 0.230   -28.196 45.922  1.00 71.69  1 541  GLU A OE2 1 
ATOM   4106 N N   . ASP A  1 515 ? -1.942  -27.849 40.719  1.00 72.87  ? 542  ASP A N   1 
ATOM   4107 C CA  . ASP A  1 515 ? -1.235  -27.147 39.649  1.00 74.62  ? 542  ASP A CA  1 
ATOM   4108 C C   . ASP A  1 515 ? -0.969  -25.662 39.883  1.00 74.35  ? 542  ASP A C   1 
ATOM   4109 O O   . ASP A  1 515 ? -1.379  -25.086 40.892  1.00 69.48  ? 542  ASP A O   1 
ATOM   4110 C CB  . ASP A  1 515 ? -1.966  -27.333 38.316  1.00 76.25  ? 542  ASP A CB  1 
ATOM   4111 C CG  . ASP A  1 515 ? -1.179  -28.181 37.339  1.00 76.79  ? 542  ASP A CG  1 
ATOM   4112 O OD1 . ASP A  1 515 ? 0.050   -28.303 37.522  1.00 69.23  1 542  ASP A OD1 1 
ATOM   4113 O OD2 . ASP A  1 515 ? -1.786  -28.720 36.388  1.00 76.12  ? 542  ASP A OD2 1 
ATOM   4114 N N   . VAL A  1 516 ? -0.263  -25.063 38.928  1.00 74.03  ? 543  VAL A N   1 
ATOM   4115 C CA  . VAL A  1 516 ? 0.064   -23.645 38.955  1.00 75.24  ? 543  VAL A CA  1 
ATOM   4116 C C   . VAL A  1 516 ? -0.300  -23.016 37.615  1.00 72.35  ? 543  VAL A C   1 
ATOM   4117 O O   . VAL A  1 516 ? 0.018   -23.561 36.556  1.00 67.67  ? 543  VAL A O   1 
ATOM   4118 C CB  . VAL A  1 516 ? 1.569   -23.411 39.215  1.00 80.22  ? 543  VAL A CB  1 
ATOM   4119 C CG1 . VAL A  1 516 ? 1.886   -21.919 39.222  1.00 70.16  ? 543  VAL A CG1 1 
ATOM   4120 C CG2 . VAL A  1 516 ? 1.999   -24.059 40.523  1.00 73.57  ? 543  VAL A CG2 1 
ATOM   4121 N N   . LEU A  1 526 ? -14.749 -19.124 30.741  1.00 49.75  ? 553  LEU A N   1 
ATOM   4122 C CA  . LEU A  1 526 ? -16.015 -19.446 31.397  1.00 52.23  ? 553  LEU A CA  1 
ATOM   4123 C C   . LEU A  1 526 ? -16.812 -20.522 30.655  1.00 54.21  ? 553  LEU A C   1 
ATOM   4124 O O   . LEU A  1 526 ? -17.374 -20.271 29.583  1.00 50.50  ? 553  LEU A O   1 
ATOM   4125 C CB  . LEU A  1 526 ? -16.872 -18.191 31.557  1.00 49.85  ? 553  LEU A CB  1 
ATOM   4126 C CG  . LEU A  1 526 ? -18.293 -18.491 32.037  1.00 54.83  ? 553  LEU A CG  1 
ATOM   4127 C CD1 . LEU A  1 526 ? -18.269 -19.112 33.435  1.00 46.36  ? 553  LEU A CD1 1 
ATOM   4128 C CD2 . LEU A  1 526 ? -19.164 -17.243 31.987  1.00 49.12  ? 553  LEU A CD2 1 
ATOM   4129 N N   . VAL A  1 527 ? -16.859 -21.719 31.235  1.00 44.57  ? 554  VAL A N   1 
ATOM   4130 C CA  . VAL A  1 527 ? -17.584 -22.846 30.653  1.00 39.51  ? 554  VAL A CA  1 
ATOM   4131 C C   . VAL A  1 527 ? -18.238 -23.675 31.755  1.00 42.90  ? 554  VAL A C   1 
ATOM   4132 O O   . VAL A  1 527 ? -17.589 -24.017 32.740  1.00 48.72  ? 554  VAL A O   1 
ATOM   4133 C CB  . VAL A  1 527 ? -16.638 -23.779 29.868  1.00 39.23  ? 554  VAL A CB  1 
ATOM   4134 C CG1 . VAL A  1 527 ? -17.401 -24.983 29.334  1.00 34.72  ? 554  VAL A CG1 1 
ATOM   4135 C CG2 . VAL A  1 527 ? -15.941 -23.033 28.734  1.00 42.50  ? 554  VAL A CG2 1 
ATOM   4136 N N   . HIS A  1 528 ? -19.517 -24.005 31.598  1.00 36.54  ? 555  HIS A N   1 
ATOM   4137 C CA  . HIS A  1 528 ? -20.200 -24.840 32.584  1.00 35.23  ? 555  HIS A CA  1 
ATOM   4138 C C   . HIS A  1 528 ? -20.183 -26.309 32.175  1.00 31.49  ? 555  HIS A C   1 
ATOM   4139 O O   . HIS A  1 528 ? -20.459 -26.635 31.025  1.00 36.28  ? 555  HIS A O   1 
ATOM   4140 C CB  . HIS A  1 528 ? -21.639 -24.371 32.782  1.00 36.36  ? 555  HIS A CB  1 
ATOM   4141 C CG  . HIS A  1 528 ? -21.753 -22.978 33.316  1.00 40.40  ? 555  HIS A CG  1 
ATOM   4142 N ND1 . HIS A  1 528 ? -21.520 -21.861 32.541  1.00 41.32  ? 555  HIS A ND1 1 
ATOM   4143 C CD2 . HIS A  1 528 ? -22.079 -22.520 34.547  1.00 38.91  ? 555  HIS A CD2 1 
ATOM   4144 C CE1 . HIS A  1 528 ? -21.701 -20.776 33.271  1.00 38.41  ? 555  HIS A CE1 1 
ATOM   4145 N NE2 . HIS A  1 528 ? -22.038 -21.148 34.493  1.00 44.65  ? 555  HIS A NE2 1 
ATOM   4146 N N   . VAL A  1 529 ? -19.864 -27.194 33.114  1.00 25.77  ? 556  VAL A N   1 
ATOM   4147 C CA  . VAL A  1 529 ? -19.789 -28.623 32.815  1.00 22.31  ? 556  VAL A CA  1 
ATOM   4148 C C   . VAL A  1 529 ? -20.553 -29.484 33.814  1.00 29.15  ? 556  VAL A C   1 
ATOM   4149 O O   . VAL A  1 529 ? -20.122 -29.661 34.954  1.00 28.46  ? 556  VAL A O   1 
ATOM   4150 C CB  . VAL A  1 529 ? -18.343 -29.112 32.793  1.00 26.11  ? 556  VAL A CB  1 
ATOM   4151 C CG1 . VAL A  1 529 ? -18.303 -30.617 32.584  1.00 25.64  ? 556  VAL A CG1 1 
ATOM   4152 C CG2 . VAL A  1 529 ? -17.557 -28.386 31.713  1.00 32.59  ? 556  VAL A CG2 1 
ATOM   4153 N N   . ASP A  1 530 ? -21.686 -30.026 33.381  1.00 31.43  ? 557  ASP A N   1 
ATOM   4154 C CA  . ASP A  1 530 ? -22.495 -30.872 34.246  1.00 29.22  ? 557  ASP A CA  1 
ATOM   4155 C C   . ASP A  1 530 ? -21.876 -32.262 34.299  1.00 26.60  ? 557  ASP A C   1 
ATOM   4156 O O   . ASP A  1 530 ? -21.579 -32.851 33.263  1.00 27.48  ? 557  ASP A O   1 
ATOM   4157 C CB  . ASP A  1 530 ? -23.937 -30.930 33.739  1.00 25.19  ? 557  ASP A CB  1 
ATOM   4158 C CG  . ASP A  1 530 ? -24.886 -31.559 34.743  1.00 31.15  ? 557  ASP A CG  1 
ATOM   4159 O OD1 . ASP A  1 530 ? -24.500 -32.547 35.401  1.00 28.51  ? 557  ASP A OD1 1 
ATOM   4160 O OD2 . ASP A  1 530 ? -26.024 -31.063 34.876  1.00 37.20  1 557  ASP A OD2 1 
ATOM   4161 N N   . LEU A  1 531 ? -21.683 -32.781 35.508  1.00 25.33  ? 558  LEU A N   1 
ATOM   4162 C CA  . LEU A  1 531 ? -21.037 -34.077 35.697  1.00 22.84  ? 558  LEU A CA  1 
ATOM   4163 C C   . LEU A  1 531 ? -21.882 -35.027 36.537  1.00 25.20  ? 558  LEU A C   1 
ATOM   4164 O O   . LEU A  1 531 ? -21.374 -36.020 37.056  1.00 24.79  ? 558  LEU A O   1 
ATOM   4165 C CB  . LEU A  1 531 ? -19.669 -33.902 36.358  1.00 23.18  ? 558  LEU A CB  1 
ATOM   4166 C CG  . LEU A  1 531 ? -18.606 -33.111 35.594  1.00 27.76  ? 558  LEU A CG  1 
ATOM   4167 C CD1 . LEU A  1 531 ? -17.353 -32.925 36.435  1.00 21.63  ? 558  LEU A CD1 1 
ATOM   4168 C CD2 . LEU A  1 531 ? -18.265 -33.808 34.295  1.00 33.03  ? 558  LEU A CD2 1 
ATOM   4169 N N   . ASN A  1 532 ? -23.169 -34.724 36.670  1.00 25.44  ? 559  ASN A N   1 
ATOM   4170 C CA  . ASN A  1 532 ? -24.055 -35.533 37.500  1.00 30.78  ? 559  ASN A CA  1 
ATOM   4171 C C   . ASN A  1 532 ? -24.265 -36.950 36.963  1.00 32.85  ? 559  ASN A C   1 
ATOM   4172 O O   . ASN A  1 532 ? -24.123 -37.200 35.766  1.00 32.04  ? 559  ASN A O   1 
ATOM   4173 C CB  . ASN A  1 532 ? -25.406 -34.840 37.673  1.00 35.53  ? 559  ASN A CB  1 
ATOM   4174 C CG  . ASN A  1 532 ? -25.277 -33.440 38.230  1.00 36.51  ? 559  ASN A CG  1 
ATOM   4175 O OD1 . ASN A  1 532 ? -24.234 -32.804 38.107  1.00 32.31  ? 559  ASN A OD1 1 
ATOM   4176 N ND2 . ASN A  1 532 ? -26.345 -32.948 38.843  1.00 45.21  ? 559  ASN A ND2 1 
ATOM   4177 N N   . ASP A  1 533 ? -24.604 -37.866 37.865  1.00 36.89  ? 560  ASP A N   1 
ATOM   4178 C CA  . ASP A  1 533 ? -24.892 -39.259 37.517  1.00 36.49  ? 560  ASP A CA  1 
ATOM   4179 C C   . ASP A  1 533 ? -23.723 -39.960 36.830  1.00 37.87  ? 560  ASP A C   1 
ATOM   4180 O O   . ASP A  1 533 ? -23.750 -40.199 35.626  1.00 31.83  ? 560  ASP A O   1 
ATOM   4181 C CB  . ASP A  1 533 ? -26.142 -39.348 36.647  1.00 27.92  ? 560  ASP A CB  1 
ATOM   4182 C CG  . ASP A  1 533 ? -27.279 -38.516 37.185  1.00 34.10  ? 560  ASP A CG  1 
ATOM   4183 O OD1 . ASP A  1 533 ? -28.061 -39.040 38.006  1.00 38.03  ? 560  ASP A OD1 1 
ATOM   4184 O OD2 . ASP A  1 533 ? -27.392 -37.337 36.784  1.00 36.67  1 560  ASP A OD2 1 
ATOM   4185 N N   . ASN A  1 534 ? -22.697 -40.293 37.603  1.00 41.27  ? 561  ASN A N   1 
ATOM   4186 C CA  . ASN A  1 534 ? -21.537 -40.971 37.048  1.00 35.63  ? 561  ASN A CA  1 
ATOM   4187 C C   . ASN A  1 534 ? -20.980 -42.059 37.952  1.00 38.97  ? 561  ASN A C   1 
ATOM   4188 O O   . ASN A  1 534 ? -21.072 -41.963 39.174  1.00 39.39  ? 561  ASN A O   1 
ATOM   4189 C CB  . ASN A  1 534 ? -20.461 -39.961 36.669  1.00 31.35  ? 561  ASN A CB  1 
ATOM   4190 C CG  . ASN A  1 534 ? -20.673 -39.398 35.291  1.00 26.63  ? 561  ASN A CG  1 
ATOM   4191 O OD1 . ASN A  1 534 ? -20.155 -39.927 34.314  1.00 28.55  ? 561  ASN A OD1 1 
ATOM   4192 N ND2 . ASN A  1 534 ? -21.457 -38.333 35.197  1.00 23.47  ? 561  ASN A ND2 1 
ATOM   4193 N N   . PRO A  1 535 ? -20.413 -43.111 37.341  1.00 42.52  ? 562  PRO A N   1 
ATOM   4194 C CA  . PRO A  1 535 ? -19.896 -44.292 38.040  1.00 41.46  ? 562  PRO A CA  1 
ATOM   4195 C C   . PRO A  1 535 ? -18.570 -44.043 38.749  1.00 40.47  ? 562  PRO A C   1 
ATOM   4196 O O   . PRO A  1 535 ? -17.746 -44.950 38.823  1.00 42.94  ? 562  PRO A O   1 
ATOM   4197 C CB  . PRO A  1 535 ? -19.682 -45.305 36.905  1.00 45.22  ? 562  PRO A CB  1 
ATOM   4198 C CG  . PRO A  1 535 ? -20.459 -44.777 35.740  1.00 44.16  ? 562  PRO A CG  1 
ATOM   4199 C CD  . PRO A  1 535 ? -20.391 -43.297 35.880  1.00 43.99  ? 562  PRO A CD  1 
ATOM   4200 N N   . LEU A  1 536 ? -18.377 -42.836 39.267  1.00 46.33  ? 563  LEU A N   1 
ATOM   4201 C CA  . LEU A  1 536 ? -17.119 -42.454 39.899  1.00 44.21  ? 563  LEU A CA  1 
ATOM   4202 C C   . LEU A  1 536 ? -16.738 -43.378 41.048  1.00 43.36  ? 563  LEU A C   1 
ATOM   4203 O O   . LEU A  1 536 ? -17.544 -43.622 41.948  1.00 41.77  ? 563  LEU A O   1 
ATOM   4204 C CB  . LEU A  1 536 ? -17.208 -41.019 40.417  1.00 39.29  ? 563  LEU A CB  1 
ATOM   4205 C CG  . LEU A  1 536 ? -15.916 -40.211 40.353  1.00 35.71  ? 563  LEU A CG  1 
ATOM   4206 C CD1 . LEU A  1 536 ? -15.557 -39.931 38.908  1.00 34.81  ? 563  LEU A CD1 1 
ATOM   4207 C CD2 . LEU A  1 536 ? -16.054 -38.917 41.132  1.00 41.27  ? 563  LEU A CD2 1 
ATOM   4208 N N   . VAL A  1 537 ? -15.514 -43.900 41.000  1.00 44.73  ? 564  VAL A N   1 
ATOM   4209 C CA  . VAL A  1 537 ? -14.939 -44.606 42.141  1.00 45.46  ? 564  VAL A CA  1 
ATOM   4210 C C   . VAL A  1 537 ? -14.249 -43.583 43.029  1.00 46.49  ? 564  VAL A C   1 
ATOM   4211 O O   . VAL A  1 537 ? -13.611 -42.653 42.535  1.00 44.16  ? 564  VAL A O   1 
ATOM   4212 C CB  . VAL A  1 537 ? -13.930 -45.707 41.726  1.00 43.97  ? 564  VAL A CB  1 
ATOM   4213 C CG1 . VAL A  1 537 ? -14.603 -46.736 40.844  1.00 45.93  ? 564  VAL A CG1 1 
ATOM   4214 C CG2 . VAL A  1 537 ? -12.711 -45.114 41.027  1.00 44.98  ? 564  VAL A CG2 1 
ATOM   4215 N N   . CYS A  1 538 ? -14.390 -43.740 44.340  1.00 48.27  ? 565  CYS A N   1 
ATOM   4216 C CA  . CYS A  1 538 ? -13.852 -42.752 45.268  1.00 46.58  ? 565  CYS A CA  1 
ATOM   4217 C C   . CYS A  1 538 ? -12.601 -43.224 46.003  1.00 44.36  ? 565  CYS A C   1 
ATOM   4218 O O   . CYS A  1 538 ? -12.549 -43.229 47.234  1.00 45.00  ? 565  CYS A O   1 
ATOM   4219 C CB  . CYS A  1 538 ? -14.930 -42.296 46.246  1.00 39.19  ? 565  CYS A CB  1 
ATOM   4220 S SG  . CYS A  1 538 ? -16.232 -41.351 45.441  1.00 30.46  ? 565  CYS A SG  1 
ATOM   4221 N N   . ASP A  1 539 ? -11.595 -43.619 45.230  1.00 36.02  ? 566  ASP A N   1 
ATOM   4222 C CA  . ASP A  1 539 ? -10.304 -43.978 45.786  1.00 36.86  ? 566  ASP A CA  1 
ATOM   4223 C C   . ASP A  1 539 ? -9.377  -42.774 45.716  1.00 34.11  ? 566  ASP A C   1 
ATOM   4224 O O   . ASP A  1 539 ? -9.797  -41.689 45.327  1.00 32.98  ? 566  ASP A O   1 
ATOM   4225 C CB  . ASP A  1 539 ? -9.708  -45.186 45.056  1.00 42.25  ? 566  ASP A CB  1 
ATOM   4226 C CG  . ASP A  1 539 ? -9.756  -45.044 43.547  1.00 47.60  ? 566  ASP A CG  1 
ATOM   4227 O OD1 . ASP A  1 539 ? -9.906  -43.907 43.056  1.00 53.26  ? 566  ASP A OD1 1 
ATOM   4228 O OD2 . ASP A  1 539 ? -9.635  -46.072 42.848  1.00 47.25  1 566  ASP A OD2 1 
ATOM   4229 N N   . CYS A  1 540 ? -8.117  -42.972 46.080  1.00 31.25  ? 567  CYS A N   1 
ATOM   4230 C CA  . CYS A  1 540 ? -7.174  -41.872 46.209  1.00 31.52  ? 567  CYS A CA  1 
ATOM   4231 C C   . CYS A  1 540 ? -6.839  -41.200 44.882  1.00 40.66  ? 567  CYS A C   1 
ATOM   4232 O O   . CYS A  1 540 ? -6.142  -40.184 44.859  1.00 41.50  ? 567  CYS A O   1 
ATOM   4233 C CB  . CYS A  1 540 ? -5.883  -42.369 46.842  1.00 34.87  ? 567  CYS A CB  1 
ATOM   4234 S SG  . CYS A  1 540 ? -4.850  -43.296 45.692  1.00 48.67  ? 567  CYS A SG  1 
ATOM   4235 N N   . THR A  1 541 ? -7.320  -41.766 43.778  1.00 41.24  ? 568  THR A N   1 
ATOM   4236 C CA  . THR A  1 541 ? -6.983  -41.237 42.456  1.00 42.69  ? 568  THR A CA  1 
ATOM   4237 C C   . THR A  1 541 ? -7.693  -39.922 42.149  1.00 40.53  ? 568  THR A C   1 
ATOM   4238 O O   . THR A  1 541 ? -7.201  -39.109 41.365  1.00 48.83  ? 568  THR A O   1 
ATOM   4239 C CB  . THR A  1 541 ? -7.260  -42.258 41.326  1.00 41.15  ? 568  THR A CB  1 
ATOM   4240 O OG1 . THR A  1 541 ? -8.370  -43.088 41.684  1.00 41.55  ? 568  THR A OG1 1 
ATOM   4241 C CG2 . THR A  1 541 ? -6.042  -43.137 41.086  1.00 45.60  ? 568  THR A CG2 1 
ATOM   4242 N N   . ILE A  1 542 ? -8.842  -39.708 42.776  1.00 33.44  ? 569  ILE A N   1 
ATOM   4243 C CA  . ILE A  1 542 ? -9.638  -38.522 42.501  1.00 34.08  ? 569  ILE A CA  1 
ATOM   4244 C C   . ILE A  1 542 ? -9.528  -37.501 43.625  1.00 37.66  ? 569  ILE A C   1 
ATOM   4245 O O   . ILE A  1 542 ? -10.430 -36.693 43.837  1.00 38.81  ? 569  ILE A O   1 
ATOM   4246 C CB  . ILE A  1 542 ? -11.110 -38.891 42.277  1.00 39.22  ? 569  ILE A CB  1 
ATOM   4247 C CG1 . ILE A  1 542 ? -11.720 -39.476 43.553  1.00 41.13  ? 569  ILE A CG1 1 
ATOM   4248 C CG2 . ILE A  1 542 ? -11.225 -39.891 41.139  1.00 42.06  ? 569  ILE A CG2 1 
ATOM   4249 C CD1 . ILE A  1 542 ? -13.221 -39.680 43.478  1.00 35.27  ? 569  ILE A CD1 1 
ATOM   4250 N N   . LEU A  1 543 ? -8.403  -37.538 44.331  1.00 41.41  ? 570  LEU A N   1 
ATOM   4251 C CA  . LEU A  1 543 ? -8.170  -36.674 45.485  1.00 46.76  ? 570  LEU A CA  1 
ATOM   4252 C C   . LEU A  1 543 ? -8.424  -35.189 45.222  1.00 51.22  ? 570  LEU A C   1 
ATOM   4253 O O   . LEU A  1 543 ? -9.298  -34.585 45.844  1.00 50.32  ? 570  LEU A O   1 
ATOM   4254 C CB  . LEU A  1 543 ? -6.741  -36.849 45.990  1.00 46.63  ? 570  LEU A CB  1 
ATOM   4255 C CG  . LEU A  1 543 ? -6.315  -35.822 47.036  1.00 40.81  ? 570  LEU A CG  1 
ATOM   4256 C CD1 . LEU A  1 543 ? -6.945  -36.146 48.377  1.00 39.33  ? 570  LEU A CD1 1 
ATOM   4257 C CD2 . LEU A  1 543 ? -4.805  -35.764 47.132  1.00 37.11  ? 570  LEU A CD2 1 
ATOM   4258 N N   . TRP A  1 544 ? -7.658  -34.610 44.302  1.00 47.77  ? 571  TRP A N   1 
ATOM   4259 C CA  . TRP A  1 544 ? -7.716  -33.174 44.055  1.00 46.19  ? 571  TRP A CA  1 
ATOM   4260 C C   . TRP A  1 544 ? -9.061  -32.706 43.524  1.00 49.43  ? 571  TRP A C   1 
ATOM   4261 O O   . TRP A  1 544 ? -9.426  -31.541 43.685  1.00 50.09  ? 571  TRP A O   1 
ATOM   4262 C CB  . TRP A  1 544 ? -6.597  -32.740 43.113  1.00 48.89  ? 571  TRP A CB  1 
ATOM   4263 C CG  . TRP A  1 544 ? -5.250  -32.886 43.726  1.00 61.05  ? 571  TRP A CG  1 
ATOM   4264 C CD1 . TRP A  1 544 ? -4.245  -33.714 43.319  1.00 61.72  ? 571  TRP A CD1 1 
ATOM   4265 C CD2 . TRP A  1 544 ? -4.761  -32.198 44.883  1.00 65.30  ? 571  TRP A CD2 1 
ATOM   4266 N NE1 . TRP A  1 544 ? -3.155  -33.575 44.144  1.00 61.38  ? 571  TRP A NE1 1 
ATOM   4267 C CE2 . TRP A  1 544 ? -3.447  -32.650 45.113  1.00 67.09  ? 571  TRP A CE2 1 
ATOM   4268 C CE3 . TRP A  1 544 ? -5.305  -31.239 45.744  1.00 59.40  ? 571  TRP A CE3 1 
ATOM   4269 C CZ2 . TRP A  1 544 ? -2.670  -32.177 46.167  1.00 74.34  ? 571  TRP A CZ2 1 
ATOM   4270 C CZ3 . TRP A  1 544 ? -4.533  -30.770 46.789  1.00 59.64  ? 571  TRP A CZ3 1 
ATOM   4271 C CH2 . TRP A  1 544 ? -3.230  -31.239 46.993  1.00 69.53  ? 571  TRP A CH2 1 
ATOM   4272 N N   . PHE A  1 545 ? -9.798  -33.611 42.893  1.00 46.05  ? 572  PHE A N   1 
ATOM   4273 C CA  . PHE A  1 545 ? -11.129 -33.278 42.416  1.00 40.31  ? 572  PHE A CA  1 
ATOM   4274 C C   . PHE A  1 545 ? -12.046 -32.905 43.580  1.00 39.97  ? 572  PHE A C   1 
ATOM   4275 O O   . PHE A  1 545 ? -12.733 -31.887 43.533  1.00 42.79  ? 572  PHE A O   1 
ATOM   4276 C CB  . PHE A  1 545 ? -11.725 -34.424 41.593  1.00 39.11  ? 572  PHE A CB  1 
ATOM   4277 C CG  . PHE A  1 545 ? -13.187 -34.249 41.283  1.00 38.28  ? 572  PHE A CG  1 
ATOM   4278 C CD1 . PHE A  1 545 ? -13.622 -33.192 40.501  1.00 33.99  ? 572  PHE A CD1 1 
ATOM   4279 C CD2 . PHE A  1 545 ? -14.127 -35.140 41.777  1.00 35.69  ? 572  PHE A CD2 1 
ATOM   4280 C CE1 . PHE A  1 545 ? -14.962 -33.022 40.222  1.00 25.57  ? 572  PHE A CE1 1 
ATOM   4281 C CE2 . PHE A  1 545 ? -15.470 -34.976 41.498  1.00 33.19  ? 572  PHE A CE2 1 
ATOM   4282 C CZ  . PHE A  1 545 ? -15.886 -33.916 40.720  1.00 28.69  ? 572  PHE A CZ  1 
ATOM   4283 N N   . ILE A  1 546 ? -12.037 -33.716 44.632  1.00 37.63  ? 573  ILE A N   1 
ATOM   4284 C CA  . ILE A  1 546 ? -12.926 -33.495 45.772  1.00 46.46  ? 573  ILE A CA  1 
ATOM   4285 C C   . ILE A  1 546 ? -12.583 -32.204 46.517  1.00 49.08  ? 573  ILE A C   1 
ATOM   4286 O O   . ILE A  1 546 ? -13.468 -31.470 46.968  1.00 46.94  ? 573  ILE A O   1 
ATOM   4287 C CB  . ILE A  1 546 ? -12.925 -34.699 46.743  1.00 46.43  ? 573  ILE A CB  1 
ATOM   4288 C CG1 . ILE A  1 546 ? -13.851 -35.792 46.224  1.00 44.45  ? 573  ILE A CG1 1 
ATOM   4289 C CG2 . ILE A  1 546 ? -13.405 -34.292 48.130  1.00 44.45  ? 573  ILE A CG2 1 
ATOM   4290 C CD1 . ILE A  1 546 ? -13.361 -36.492 44.995  1.00 45.34  ? 573  ILE A CD1 1 
ATOM   4291 N N   . GLN A  1 547 ? -11.293 -31.924 46.634  1.00 47.19  ? 574  GLN A N   1 
ATOM   4292 C CA  . GLN A  1 547 ? -10.860 -30.684 47.249  1.00 48.16  ? 574  GLN A CA  1 
ATOM   4293 C C   . GLN A  1 547 ? -11.359 -29.519 46.403  1.00 48.62  ? 574  GLN A C   1 
ATOM   4294 O O   . GLN A  1 547 ? -11.860 -28.529 46.933  1.00 51.61  ? 574  GLN A O   1 
ATOM   4295 C CB  . GLN A  1 547 ? -9.337  -30.656 47.386  1.00 52.15  ? 574  GLN A CB  1 
ATOM   4296 C CG  . GLN A  1 547 ? -8.758  -31.804 48.210  1.00 52.86  ? 574  GLN A CG  1 
ATOM   4297 C CD  . GLN A  1 547 ? -9.051  -31.682 49.698  1.00 48.53  ? 574  GLN A CD  1 
ATOM   4298 O OE1 . GLN A  1 547 ? -10.198 -31.799 50.132  1.00 45.66  ? 574  GLN A OE1 1 
ATOM   4299 N NE2 . GLN A  1 547 ? -8.008  -31.450 50.486  1.00 51.85  ? 574  GLN A NE2 1 
ATOM   4300 N N   . LEU A  1 548 ? -11.242 -29.662 45.086  1.00 47.84  ? 575  LEU A N   1 
ATOM   4301 C CA  . LEU A  1 548 ? -11.718 -28.647 44.149  1.00 46.52  ? 575  LEU A CA  1 
ATOM   4302 C C   . LEU A  1 548 ? -13.227 -28.452 44.239  1.00 37.65  ? 575  LEU A C   1 
ATOM   4303 O O   . LEU A  1 548 ? -13.719 -27.331 44.143  1.00 33.64  ? 575  LEU A O   1 
ATOM   4304 C CB  . LEU A  1 548 ? -11.321 -29.010 42.717  1.00 42.15  ? 575  LEU A CB  1 
ATOM   4305 C CG  . LEU A  1 548 ? -11.974 -28.197 41.596  1.00 42.68  ? 575  LEU A CG  1 
ATOM   4306 C CD1 . LEU A  1 548 ? -11.719 -26.715 41.769  1.00 46.63  ? 575  LEU A CD1 1 
ATOM   4307 C CD2 . LEU A  1 548 ? -11.475 -28.658 40.240  1.00 47.75  ? 575  LEU A CD2 1 
ATOM   4308 N N   . VAL A  1 549 ? -13.953 -29.549 44.413  1.00 38.37  ? 576  VAL A N   1 
ATOM   4309 C CA  . VAL A  1 549 ? -15.401 -29.497 44.572  1.00 41.88  ? 576  VAL A CA  1 
ATOM   4310 C C   . VAL A  1 549 ? -15.789 -28.581 45.728  1.00 47.92  ? 576  VAL A C   1 
ATOM   4311 O O   . VAL A  1 549 ? -16.709 -27.771 45.610  1.00 55.10  ? 576  VAL A O   1 
ATOM   4312 C CB  . VAL A  1 549 ? -15.994 -30.907 44.777  1.00 44.90  ? 576  VAL A CB  1 
ATOM   4313 C CG1 . VAL A  1 549 ? -17.355 -30.837 45.455  1.00 44.95  ? 576  VAL A CG1 1 
ATOM   4314 C CG2 . VAL A  1 549 ? -16.082 -31.637 43.447  1.00 38.77  ? 576  VAL A CG2 1 
ATOM   4315 N N   . ARG A  1 550 ? -15.077 -28.703 46.843  1.00 51.10  ? 577  ARG A N   1 
ATOM   4316 C CA  . ARG A  1 550 ? -15.257 -27.776 47.948  1.00 50.72  ? 577  ARG A CA  1 
ATOM   4317 C C   . ARG A  1 550 ? -14.370 -26.569 47.702  1.00 50.62  ? 577  ARG A C   1 
ATOM   4318 O O   . ARG A  1 550 ? -13.695 -26.494 46.678  1.00 50.49  ? 577  ARG A O   1 
ATOM   4319 C CB  . ARG A  1 550 ? -14.917 -28.442 49.279  1.00 54.74  ? 577  ARG A CB  1 
ATOM   4320 C CG  . ARG A  1 550 ? -15.805 -29.634 49.606  1.00 63.62  ? 577  ARG A CG  1 
ATOM   4321 C CD  . ARG A  1 550 ? -15.575 -30.114 51.025  1.00 71.44  ? 577  ARG A CD  1 
ATOM   4322 N NE  . ARG A  1 550 ? -14.154 -30.300 51.309  1.00 74.68  ? 577  ARG A NE  1 
ATOM   4323 C CZ  . ARG A  1 550 ? -13.502 -31.444 51.135  1.00 63.13  ? 577  ARG A CZ  1 
ATOM   4324 N NH1 . ARG A  1 550 ? -14.145 -32.513 50.679  1.00 58.55  1 577  ARG A NH1 1 
ATOM   4325 N NH2 . ARG A  1 550 ? -12.208 -31.518 51.420  1.00 52.52  ? 577  ARG A NH2 1 
ATOM   4326 N N   . GLY A  1 551 ? -14.370 -25.620 48.630  1.00 49.97  ? 578  GLY A N   1 
ATOM   4327 C CA  . GLY A  1 551 ? -13.590 -24.408 48.455  1.00 55.87  ? 578  GLY A CA  1 
ATOM   4328 C C   . GLY A  1 551 ? -12.098 -24.674 48.444  1.00 55.37  ? 578  GLY A C   1 
ATOM   4329 O O   . GLY A  1 551 ? -11.318 -23.868 47.933  1.00 51.73  ? 578  GLY A O   1 
ATOM   4330 N N   . VAL A  1 552 ? -11.723 -25.829 48.991  1.00 53.77  ? 579  VAL A N   1 
ATOM   4331 C CA  . VAL A  1 552 ? -10.335 -26.196 49.263  1.00 46.22  ? 579  VAL A CA  1 
ATOM   4332 C C   . VAL A  1 552 ? -9.354  -25.919 48.126  1.00 50.35  ? 579  VAL A C   1 
ATOM   4333 O O   . VAL A  1 552 ? -8.512  -25.031 48.238  1.00 56.00  ? 579  VAL A O   1 
ATOM   4334 C CB  . VAL A  1 552 ? -10.227 -27.683 49.650  1.00 49.58  ? 579  VAL A CB  1 
ATOM   4335 C CG1 . VAL A  1 552 ? -8.872  -27.969 50.277  1.00 47.33  ? 579  VAL A CG1 1 
ATOM   4336 C CG2 . VAL A  1 552 ? -11.356 -28.066 50.597  1.00 50.47  ? 579  VAL A CG2 1 
ATOM   4337 N N   . HIS A  1 553 ? -9.463  -26.677 47.039  1.00 54.39  ? 580  HIS A N   1 
ATOM   4338 C CA  . HIS A  1 553 ? -8.508  -26.578 45.936  1.00 55.29  ? 580  HIS A CA  1 
ATOM   4339 C C   . HIS A  1 553 ? -9.027  -25.676 44.818  1.00 56.40  ? 580  HIS A C   1 
ATOM   4340 O O   . HIS A  1 553 ? -10.176 -25.799 44.401  1.00 56.01  ? 580  HIS A O   1 
ATOM   4341 C CB  . HIS A  1 553 ? -8.193  -27.969 45.384  1.00 49.29  ? 580  HIS A CB  1 
ATOM   4342 C CG  . HIS A  1 553 ? -6.895  -28.050 44.641  1.00 58.38  ? 580  HIS A CG  1 
ATOM   4343 N ND1 . HIS A  1 553 ? -5.716  -27.542 45.143  1.00 64.32  ? 580  HIS A ND1 1 
ATOM   4344 C CD2 . HIS A  1 553 ? -6.587  -28.597 43.441  1.00 63.43  ? 580  HIS A CD2 1 
ATOM   4345 C CE1 . HIS A  1 553 ? -4.740  -27.764 44.280  1.00 67.10  ? 580  HIS A CE1 1 
ATOM   4346 N NE2 . HIS A  1 553 ? -5.242  -28.402 43.238  1.00 62.32  ? 580  HIS A NE2 1 
ATOM   4347 N N   . LYS A  1 554 ? -8.178  -24.764 44.347  1.00 57.74  ? 581  LYS A N   1 
ATOM   4348 C CA  . LYS A  1 554 ? -8.531  -23.848 43.261  1.00 57.00  ? 581  LYS A CA  1 
ATOM   4349 C C   . LYS A  1 554 ? -7.314  -23.538 42.381  1.00 59.09  ? 581  LYS A C   1 
ATOM   4350 O O   . LYS A  1 554 ? -6.875  -22.392 42.321  1.00 67.90  ? 581  LYS A O   1 
ATOM   4351 C CB  . LYS A  1 554 ? -9.100  -22.539 43.828  1.00 53.06  ? 581  LYS A CB  1 
ATOM   4352 C CG  . LYS A  1 554 ? -10.432 -22.665 44.573  1.00 55.71  ? 581  LYS A CG  1 
ATOM   4353 C CD  . LYS A  1 554 ? -11.594 -22.947 43.623  1.00 56.67  ? 581  LYS A CD  1 
ATOM   4354 C CE  . LYS A  1 554 ? -12.927 -23.003 44.364  1.00 54.40  ? 581  LYS A CE  1 
ATOM   4355 N NZ  . LYS A  1 554 ? -14.079 -23.230 43.440  1.00 47.26  1 581  LYS A NZ  1 
ATOM   4356 N N   . PRO A  1 555 ? -6.784  -24.553 41.676  1.00 58.05  ? 582  PRO A N   1 
ATOM   4357 C CA  . PRO A  1 555 ? -5.491  -24.475 40.980  1.00 63.13  ? 582  PRO A CA  1 
ATOM   4358 C C   . PRO A  1 555 ? -5.503  -23.756 39.629  1.00 62.44  ? 582  PRO A C   1 
ATOM   4359 O O   . PRO A  1 555 ? -5.331  -24.411 38.601  1.00 64.75  ? 582  PRO A O   1 
ATOM   4360 C CB  . PRO A  1 555 ? -5.144  -25.946 40.758  1.00 71.65  ? 582  PRO A CB  1 
ATOM   4361 C CG  . PRO A  1 555 ? -6.472  -26.599 40.574  1.00 67.57  ? 582  PRO A CG  1 
ATOM   4362 C CD  . PRO A  1 555 ? -7.426  -25.867 41.485  1.00 61.84  ? 582  PRO A CD  1 
ATOM   4363 N N   . GLN A  1 556 ? -5.677  -22.437 39.643  1.00 64.19  ? 583  GLN A N   1 
ATOM   4364 C CA  . GLN A  1 556 ? -5.660  -21.611 38.429  1.00 72.17  ? 583  GLN A CA  1 
ATOM   4365 C C   . GLN A  1 556 ? -6.818  -21.871 37.463  1.00 69.96  ? 583  GLN A C   1 
ATOM   4366 O O   . GLN A  1 556 ? -7.781  -21.102 37.424  1.00 70.08  ? 583  GLN A O   1 
ATOM   4367 C CB  . GLN A  1 556 ? -4.319  -21.712 37.688  1.00 75.28  ? 583  GLN A CB  1 
ATOM   4368 C CG  . GLN A  1 556 ? -3.642  -20.367 37.483  1.00 76.06  ? 583  GLN A CG  1 
ATOM   4369 C CD  . GLN A  1 556 ? -2.804  -20.305 36.218  1.00 66.54  ? 583  GLN A CD  1 
ATOM   4370 O OE1 . GLN A  1 556 ? -2.584  -21.313 35.544  1.00 61.50  ? 583  GLN A OE1 1 
ATOM   4371 N NE2 . GLN A  1 556 ? -2.337  -19.109 35.888  1.00 58.38  ? 583  GLN A NE2 1 
ATOM   4372 N N   . TYR A  1 557 ? -6.718  -22.946 36.683  1.00 66.92  ? 584  TYR A N   1 
ATOM   4373 C CA  . TYR A  1 557 ? -7.733  -23.268 35.678  1.00 70.42  ? 584  TYR A CA  1 
ATOM   4374 C C   . TYR A  1 557 ? -9.137  -23.398 36.272  1.00 61.19  ? 584  TYR A C   1 
ATOM   4375 O O   . TYR A  1 557 ? -10.132 -23.197 35.578  1.00 55.80  ? 584  TYR A O   1 
ATOM   4376 C CB  . TYR A  1 557 ? -7.359  -24.542 34.902  1.00 65.14  ? 584  TYR A CB  1 
ATOM   4377 C CG  . TYR A  1 557 ? -7.086  -25.746 35.774  1.00 61.75  ? 584  TYR A CG  1 
ATOM   4378 C CD1 . TYR A  1 557 ? -8.127  -26.469 36.341  1.00 62.34  ? 584  TYR A CD1 1 
ATOM   4379 C CD2 . TYR A  1 557 ? -5.785  -26.167 36.024  1.00 67.04  ? 584  TYR A CD2 1 
ATOM   4380 C CE1 . TYR A  1 557 ? -7.884  -27.567 37.142  1.00 67.07  ? 584  TYR A CE1 1 
ATOM   4381 C CE2 . TYR A  1 557 ? -5.531  -27.268 36.824  1.00 67.66  ? 584  TYR A CE2 1 
ATOM   4382 C CZ  . TYR A  1 557 ? -6.587  -27.964 37.379  1.00 67.09  ? 584  TYR A CZ  1 
ATOM   4383 O OH  . TYR A  1 557 ? -6.352  -29.061 38.174  1.00 62.66  ? 584  TYR A OH  1 
ATOM   4384 N N   . SER A  1 558 ? -9.193  -23.724 37.561  1.00 57.54  ? 585  SER A N   1 
ATOM   4385 C CA  . SER A  1 558 ? -10.446 -23.944 38.279  1.00 62.87  ? 585  SER A CA  1 
ATOM   4386 C C   . SER A  1 558 ? -11.503 -22.859 38.075  1.00 70.19  ? 585  SER A C   1 
ATOM   4387 O O   . SER A  1 558 ? -12.693 -23.156 37.964  1.00 65.13  ? 585  SER A O   1 
ATOM   4388 C CB  . SER A  1 558 ? -10.167 -24.090 39.776  1.00 61.62  ? 585  SER A CB  1 
ATOM   4389 O OG  . SER A  1 558 ? -11.346 -23.866 40.531  1.00 59.84  ? 585  SER A OG  1 
ATOM   4390 N N   . ARG A  1 559 ? -11.069 -21.604 38.033  1.00 72.34  ? 586  ARG A N   1 
ATOM   4391 C CA  . ARG A  1 559 ? -12.002 -20.485 37.979  1.00 68.39  ? 586  ARG A CA  1 
ATOM   4392 C C   . ARG A  1 559 ? -12.530 -20.245 36.570  1.00 60.49  ? 586  ARG A C   1 
ATOM   4393 O O   . ARG A  1 559 ? -13.536 -19.557 36.388  1.00 46.93  ? 586  ARG A O   1 
ATOM   4394 C CB  . ARG A  1 559 ? -11.341 -19.218 38.528  1.00 78.79  ? 586  ARG A CB  1 
ATOM   4395 C CG  . ARG A  1 559 ? -10.811 -19.363 39.949  1.00 73.69  ? 586  ARG A CG  1 
ATOM   4396 C CD  . ARG A  1 559 ? -9.978  -18.157 40.356  1.00 74.35  ? 586  ARG A CD  1 
ATOM   4397 N NE  . ARG A  1 559 ? -10.763 -16.925 40.358  1.00 82.08  ? 586  ARG A NE  1 
ATOM   4398 C CZ  . ARG A  1 559 ? -10.274 -15.729 40.668  1.00 78.44  ? 586  ARG A CZ  1 
ATOM   4399 N NH1 . ARG A  1 559 ? -11.064 -14.662 40.645  1.00 69.35  1 586  ARG A NH1 1 
ATOM   4400 N NH2 . ARG A  1 559 ? -8.997  -15.598 41.004  1.00 70.50  ? 586  ARG A NH2 1 
ATOM   4401 N N   . GLN A  1 560 ? -11.850 -20.819 35.579  1.00 65.68  ? 587  GLN A N   1 
ATOM   4402 C CA  . GLN A  1 560 ? -12.239 -20.646 34.179  1.00 69.03  ? 587  GLN A CA  1 
ATOM   4403 C C   . GLN A  1 560 ? -13.311 -21.641 33.709  1.00 63.04  ? 587  GLN A C   1 
ATOM   4404 O O   . GLN A  1 560 ? -13.838 -21.523 32.599  1.00 53.76  ? 587  GLN A O   1 
ATOM   4405 C CB  . GLN A  1 560 ? -11.012 -20.671 33.263  1.00 53.95  ? 587  GLN A CB  1 
ATOM   4406 C CG  . GLN A  1 560 ? -10.190 -19.397 33.337  1.00 47.69  ? 587  GLN A CG  1 
ATOM   4407 C CD  . GLN A  1 560 ? -9.181  -19.288 32.216  1.00 62.30  ? 587  GLN A CD  1 
ATOM   4408 O OE1 . GLN A  1 560 ? -8.381  -20.198 31.995  1.00 66.92  ? 587  GLN A OE1 1 
ATOM   4409 N NE2 . GLN A  1 560 ? -9.217  -18.173 31.495  1.00 62.97  ? 587  GLN A NE2 1 
ATOM   4410 N N   . PHE A  1 561 ? -13.623 -22.620 34.555  1.00 55.62  ? 588  PHE A N   1 
ATOM   4411 C CA  . PHE A  1 561 ? -14.794 -23.463 34.340  1.00 45.75  ? 588  PHE A CA  1 
ATOM   4412 C C   . PHE A  1 561 ? -15.625 -23.583 35.615  1.00 48.00  ? 588  PHE A C   1 
ATOM   4413 O O   . PHE A  1 561 ? -15.102 -23.426 36.717  1.00 45.23  ? 588  PHE A O   1 
ATOM   4414 C CB  . PHE A  1 561 ? -14.431 -24.840 33.755  1.00 42.59  ? 588  PHE A CB  1 
ATOM   4415 C CG  . PHE A  1 561 ? -13.493 -25.662 34.607  1.00 44.30  ? 588  PHE A CG  1 
ATOM   4416 C CD1 . PHE A  1 561 ? -13.868 -26.108 35.864  1.00 44.33  ? 588  PHE A CD1 1 
ATOM   4417 C CD2 . PHE A  1 561 ? -12.251 -26.034 34.121  1.00 41.45  ? 588  PHE A CD2 1 
ATOM   4418 C CE1 . PHE A  1 561 ? -13.015 -26.876 36.633  1.00 43.39  ? 588  PHE A CE1 1 
ATOM   4419 C CE2 . PHE A  1 561 ? -11.395 -26.804 34.886  1.00 42.04  ? 588  PHE A CE2 1 
ATOM   4420 C CZ  . PHE A  1 561 ? -11.779 -27.225 36.143  1.00 40.20  ? 588  PHE A CZ  1 
ATOM   4421 N N   . LYS A  1 562 ? -16.918 -23.853 35.461  1.00 46.92  ? 589  LYS A N   1 
ATOM   4422 C CA  . LYS A  1 562 ? -17.812 -23.972 36.606  1.00 42.72  ? 589  LYS A CA  1 
ATOM   4423 C C   . LYS A  1 562 ? -18.530 -25.318 36.598  1.00 44.18  ? 589  LYS A C   1 
ATOM   4424 O O   . LYS A  1 562 ? -19.511 -25.513 35.874  1.00 45.03  ? 589  LYS A O   1 
ATOM   4425 C CB  . LYS A  1 562 ? -18.818 -22.818 36.633  1.00 44.64  ? 589  LYS A CB  1 
ATOM   4426 C CG  . LYS A  1 562 ? -19.393 -22.535 38.018  1.00 54.59  ? 589  LYS A CG  1 
ATOM   4427 C CD  . LYS A  1 562 ? -20.706 -23.268 38.256  1.00 56.70  ? 589  LYS A CD  1 
ATOM   4428 C CE  . LYS A  1 562 ? -21.016 -23.382 39.742  1.00 53.92  ? 589  LYS A CE  1 
ATOM   4429 N NZ  . LYS A  1 562 ? -20.076 -24.315 40.421  1.00 38.13  1 589  LYS A NZ  1 
ATOM   4430 N N   . LEU A  1 563 ? -18.032 -26.240 37.413  1.00 35.87  ? 590  LEU A N   1 
ATOM   4431 C CA  . LEU A  1 563 ? -18.542 -27.605 37.448  1.00 33.98  ? 590  LEU A CA  1 
ATOM   4432 C C   . LEU A  1 563 ? -19.872 -27.715 38.176  1.00 37.37  ? 590  LEU A C   1 
ATOM   4433 O O   . LEU A  1 563 ? -20.015 -27.217 39.290  1.00 46.00  ? 590  LEU A O   1 
ATOM   4434 C CB  . LEU A  1 563 ? -17.527 -28.520 38.134  1.00 33.14  ? 590  LEU A CB  1 
ATOM   4435 C CG  . LEU A  1 563 ? -16.556 -29.314 37.261  1.00 29.87  ? 590  LEU A CG  1 
ATOM   4436 C CD1 . LEU A  1 563 ? -16.153 -28.523 36.039  1.00 24.78  ? 590  LEU A CD1 1 
ATOM   4437 C CD2 . LEU A  1 563 ? -15.332 -29.704 38.073  1.00 34.34  ? 590  LEU A CD2 1 
ATOM   4438 N N   . ARG A  1 564 ? -20.846 -28.366 37.546  1.00 33.29  ? 591  ARG A N   1 
ATOM   4439 C CA  . ARG A  1 564 ? -22.045 -28.787 38.263  1.00 38.81  ? 591  ARG A CA  1 
ATOM   4440 C C   . ARG A  1 564 ? -21.864 -30.233 38.675  1.00 34.42  ? 591  ARG A C   1 
ATOM   4441 O O   . ARG A  1 564 ? -21.674 -31.100 37.827  1.00 36.19  ? 591  ARG A O   1 
ATOM   4442 C CB  . ARG A  1 564 ? -23.304 -28.652 37.411  1.00 39.03  ? 591  ARG A CB  1 
ATOM   4443 C CG  . ARG A  1 564 ? -24.498 -29.367 38.030  1.00 41.68  ? 591  ARG A CG  1 
ATOM   4444 C CD  . ARG A  1 564 ? -25.801 -28.969 37.371  1.00 51.63  ? 591  ARG A CD  1 
ATOM   4445 N NE  . ARG A  1 564 ? -26.094 -27.550 37.553  1.00 63.20  ? 591  ARG A NE  1 
ATOM   4446 C CZ  . ARG A  1 564 ? -27.204 -26.957 37.124  1.00 67.08  ? 591  ARG A CZ  1 
ATOM   4447 N NH1 . ARG A  1 564 ? -28.130 -27.663 36.487  1.00 77.14  1 591  ARG A NH1 1 
ATOM   4448 N NH2 . ARG A  1 564 ? -27.389 -25.660 37.331  1.00 56.94  ? 591  ARG A NH2 1 
ATOM   4449 N N   . THR A  1 565 ? -21.914 -30.495 39.975  1.00 35.91  ? 592  THR A N   1 
ATOM   4450 C CA  . THR A  1 565 ? -21.573 -31.814 40.494  1.00 38.28  ? 592  THR A CA  1 
ATOM   4451 C C   . THR A  1 565 ? -22.551 -32.285 41.564  1.00 39.25  ? 592  THR A C   1 
ATOM   4452 O O   . THR A  1 565 ? -22.321 -33.306 42.213  1.00 35.15  ? 592  THR A O   1 
ATOM   4453 C CB  . THR A  1 565 ? -20.152 -31.817 41.095  1.00 41.83  ? 592  THR A CB  1 
ATOM   4454 O OG1 . THR A  1 565 ? -20.065 -30.828 42.130  1.00 36.91  ? 592  THR A OG1 1 
ATOM   4455 C CG2 . THR A  1 565 ? -19.111 -31.510 40.026  1.00 35.12  ? 592  THR A CG2 1 
ATOM   4456 N N   . ASP A  1 566 ? -23.644 -31.543 41.730  1.00 41.16  ? 593  ASP A N   1 
ATOM   4457 C CA  . ASP A  1 566 ? -24.592 -31.773 42.820  1.00 41.07  ? 593  ASP A CA  1 
ATOM   4458 C C   . ASP A  1 566 ? -25.136 -33.196 42.881  1.00 45.20  ? 593  ASP A C   1 
ATOM   4459 O O   . ASP A  1 566 ? -25.478 -33.684 43.956  1.00 47.99  ? 593  ASP A O   1 
ATOM   4460 C CB  . ASP A  1 566 ? -25.749 -30.762 42.768  1.00 55.43  ? 593  ASP A CB  1 
ATOM   4461 C CG  . ASP A  1 566 ? -26.672 -30.976 41.574  1.00 54.23  ? 593  ASP A CG  1 
ATOM   4462 O OD1 . ASP A  1 566 ? -26.303 -30.562 40.452  1.00 52.32  ? 593  ASP A OD1 1 
ATOM   4463 O OD2 . ASP A  1 566 ? -27.774 -31.542 41.763  1.00 45.32  1 593  ASP A OD2 1 
ATOM   4464 N N   . ARG A  1 567 ? -25.217 -33.859 41.731  1.00 46.96  ? 594  ARG A N   1 
ATOM   4465 C CA  . ARG A  1 567 ? -25.676 -35.244 41.692  1.00 47.13  ? 594  ARG A CA  1 
ATOM   4466 C C   . ARG A  1 567 ? -24.607 -36.202 41.166  1.00 44.98  ? 594  ARG A C   1 
ATOM   4467 O O   . ARG A  1 567 ? -24.904 -37.131 40.416  1.00 42.68  ? 594  ARG A O   1 
ATOM   4468 C CB  . ARG A  1 567 ? -26.973 -35.377 40.888  1.00 46.87  ? 594  ARG A CB  1 
ATOM   4469 C CG  . ARG A  1 567 ? -28.213 -34.881 41.617  1.00 49.23  ? 594  ARG A CG  1 
ATOM   4470 C CD  . ARG A  1 567 ? -29.469 -35.158 40.805  1.00 56.52  ? 594  ARG A CD  1 
ATOM   4471 N NE  . ARG A  1 567 ? -29.451 -34.460 39.523  1.00 54.41  ? 594  ARG A NE  1 
ATOM   4472 C CZ  . ARG A  1 567 ? -30.013 -33.273 39.314  1.00 61.16  ? 594  ARG A CZ  1 
ATOM   4473 N NH1 . ARG A  1 567 ? -29.947 -32.708 38.116  1.00 60.69  1 594  ARG A NH1 1 
ATOM   4474 N NH2 . ARG A  1 567 ? -30.642 -32.651 40.303  1.00 65.21  ? 594  ARG A NH2 1 
ATOM   4475 N N   . LEU A  1 568 ? -23.361 -35.967 41.565  1.00 47.83  ? 595  LEU A N   1 
ATOM   4476 C CA  . LEU A  1 568 ? -22.283 -36.911 41.300  1.00 50.60  ? 595  LEU A CA  1 
ATOM   4477 C C   . LEU A  1 568 ? -22.091 -37.767 42.553  1.00 51.42  ? 595  LEU A C   1 
ATOM   4478 O O   . LEU A  1 568 ? -21.830 -37.243 43.633  1.00 52.06  ? 595  LEU A O   1 
ATOM   4479 C CB  . LEU A  1 568 ? -20.995 -36.165 40.952  1.00 45.44  ? 595  LEU A CB  1 
ATOM   4480 C CG  . LEU A  1 568 ? -20.030 -36.819 39.958  1.00 45.30  ? 595  LEU A CG  1 
ATOM   4481 C CD1 . LEU A  1 568 ? -18.813 -35.929 39.735  1.00 33.81  ? 595  LEU A CD1 1 
ATOM   4482 C CD2 . LEU A  1 568 ? -19.605 -38.215 40.407  1.00 46.25  ? 595  LEU A CD2 1 
ATOM   4483 N N   . VAL A  1 569 ? -22.227 -39.081 42.410  1.00 47.32  ? 596  VAL A N   1 
ATOM   4484 C CA  . VAL A  1 569 ? -22.230 -39.970 43.567  1.00 42.55  ? 596  VAL A CA  1 
ATOM   4485 C C   . VAL A  1 569 ? -21.253 -41.135 43.402  1.00 51.95  ? 596  VAL A C   1 
ATOM   4486 O O   . VAL A  1 569 ? -21.149 -41.718 42.323  1.00 57.88  ? 596  VAL A O   1 
ATOM   4487 C CB  . VAL A  1 569 ? -23.657 -40.506 43.843  1.00 44.46  ? 596  VAL A CB  1 
ATOM   4488 C CG1 . VAL A  1 569 ? -23.635 -41.638 44.848  1.00 45.12  ? 596  VAL A CG1 1 
ATOM   4489 C CG2 . VAL A  1 569 ? -24.560 -39.385 44.326  1.00 43.61  ? 596  VAL A CG2 1 
ATOM   4490 N N   . CYS A  1 570 ? -20.536 -41.458 44.476  1.00 52.87  ? 597  CYS A N   1 
ATOM   4491 C CA  . CYS A  1 570 ? -19.586 -42.567 44.484  1.00 47.10  ? 597  CYS A CA  1 
ATOM   4492 C C   . CYS A  1 570 ? -20.276 -43.920 44.335  1.00 52.26  ? 597  CYS A C   1 
ATOM   4493 O O   . CYS A  1 570 ? -21.211 -44.243 45.072  1.00 50.20  ? 597  CYS A O   1 
ATOM   4494 C CB  . CYS A  1 570 ? -18.777 -42.563 45.781  1.00 43.08  ? 597  CYS A CB  1 
ATOM   4495 S SG  . CYS A  1 570 ? -18.073 -40.965 46.217  1.00 43.70  ? 597  CYS A SG  1 
ATOM   4496 N N   . SER A  1 571 ? -19.798 -44.712 43.382  1.00 54.88  ? 598  SER A N   1 
ATOM   4497 C CA  . SER A  1 571 ? -20.318 -46.055 43.167  1.00 55.17  ? 598  SER A CA  1 
ATOM   4498 C C   . SER A  1 571 ? -19.567 -47.044 44.045  1.00 49.11  ? 598  SER A C   1 
ATOM   4499 O O   . SER A  1 571 ? -20.153 -47.954 44.625  1.00 47.51  ? 598  SER A O   1 
ATOM   4500 C CB  . SER A  1 571 ? -20.167 -46.444 41.698  1.00 52.96  ? 598  SER A CB  1 
ATOM   4501 O OG  . SER A  1 571 ? -20.765 -45.469 40.865  1.00 55.39  ? 598  SER A OG  1 
ATOM   4502 N N   . GLN A  1 572 ? -18.257 -46.856 44.129  1.00 45.99  ? 599  GLN A N   1 
ATOM   4503 C CA  . GLN A  1 572 ? -17.416 -47.687 44.970  1.00 48.98  ? 599  GLN A CA  1 
ATOM   4504 C C   . GLN A  1 572 ? -16.374 -46.808 45.651  1.00 52.70  ? 599  GLN A C   1 
ATOM   4505 O O   . GLN A  1 572 ? -15.990 -45.771 45.106  1.00 44.79  ? 599  GLN A O   1 
ATOM   4506 C CB  . GLN A  1 572 ? -16.753 -48.785 44.135  1.00 51.78  ? 599  GLN A CB  1 
ATOM   4507 C CG  . GLN A  1 572 ? -17.699 -49.906 43.732  1.00 51.63  ? 599  GLN A CG  1 
ATOM   4508 C CD  . GLN A  1 572 ? -17.010 -50.997 42.932  1.00 60.19  ? 599  GLN A CD  1 
ATOM   4509 O OE1 . GLN A  1 572 ? -16.018 -50.747 42.241  1.00 48.76  ? 599  GLN A OE1 1 
ATOM   4510 N NE2 . GLN A  1 572 ? -17.533 -52.218 43.023  1.00 56.34  ? 599  GLN A NE2 1 
ATOM   4511 N N   . PRO A  1 573 ? -15.919 -47.208 46.852  1.00 53.26  ? 600  PRO A N   1 
ATOM   4512 C CA  . PRO A  1 573 ? -16.305 -48.426 47.578  1.00 49.58  ? 600  PRO A CA  1 
ATOM   4513 C C   . PRO A  1 573 ? -17.616 -48.318 48.363  1.00 49.21  ? 600  PRO A C   1 
ATOM   4514 O O   . PRO A  1 573 ? -18.215 -47.244 48.465  1.00 40.48  ? 600  PRO A O   1 
ATOM   4515 C CB  . PRO A  1 573 ? -15.140 -48.628 48.544  1.00 56.13  ? 600  PRO A CB  1 
ATOM   4516 C CG  . PRO A  1 573 ? -14.665 -47.253 48.823  1.00 53.94  ? 600  PRO A CG  1 
ATOM   4517 C CD  . PRO A  1 573 ? -14.841 -46.479 47.545  1.00 46.74  ? 600  PRO A CD  1 
ATOM   4518 N N   . ASN A  1 574 ? -18.031 -49.451 48.927  1.00 51.52  ? 601  ASN A N   1 
ATOM   4519 C CA  . ASN A  1 574 ? -19.315 -49.592 49.610  1.00 52.64  ? 601  ASN A CA  1 
ATOM   4520 C C   . ASN A  1 574 ? -19.449 -48.721 50.853  1.00 54.78  ? 601  ASN A C   1 
ATOM   4521 O O   . ASN A  1 574 ? -20.545 -48.546 51.387  1.00 56.91  ? 601  ASN A O   1 
ATOM   4522 C CB  . ASN A  1 574 ? -19.539 -51.056 49.994  1.00 58.31  ? 601  ASN A CB  1 
ATOM   4523 C CG  . ASN A  1 574 ? -19.248 -52.011 48.852  1.00 61.14  ? 601  ASN A CG  1 
ATOM   4524 O OD1 . ASN A  1 574 ? -18.090 -52.237 48.495  1.00 58.00  ? 601  ASN A OD1 1 
ATOM   4525 N ND2 . ASN A  1 574 ? -20.299 -52.587 48.281  1.00 60.60  ? 601  ASN A ND2 1 
ATOM   4526 N N   . VAL A  1 575 ? -18.330 -48.188 51.321  1.00 55.97  ? 602  VAL A N   1 
ATOM   4527 C CA  . VAL A  1 575 ? -18.341 -47.316 52.484  1.00 55.58  ? 602  VAL A CA  1 
ATOM   4528 C C   . VAL A  1 575 ? -18.832 -45.925 52.091  1.00 60.64  ? 602  VAL A C   1 
ATOM   4529 O O   . VAL A  1 575 ? -19.789 -45.407 52.672  1.00 55.11  ? 602  VAL A O   1 
ATOM   4530 C CB  . VAL A  1 575 ? -16.941 -47.201 53.094  1.00 54.13  ? 602  VAL A CB  1 
ATOM   4531 C CG1 . VAL A  1 575 ? -17.037 -46.786 54.556  1.00 56.22  ? 602  VAL A CG1 1 
ATOM   4532 C CG2 . VAL A  1 575 ? -16.196 -48.522 52.950  1.00 47.06  ? 602  VAL A CG2 1 
ATOM   4533 N N   . LEU A  1 576 ? -18.175 -45.335 51.094  1.00 59.38  ? 603  LEU A N   1 
ATOM   4534 C CA  . LEU A  1 576 ? -18.508 -43.994 50.620  1.00 49.35  ? 603  LEU A CA  1 
ATOM   4535 C C   . LEU A  1 576 ? -19.696 -44.010 49.674  1.00 51.67  ? 603  LEU A C   1 
ATOM   4536 O O   . LEU A  1 576 ? -20.260 -42.962 49.364  1.00 53.33  ? 603  LEU A O   1 
ATOM   4537 C CB  . LEU A  1 576 ? -17.317 -43.356 49.897  1.00 49.29  ? 603  LEU A CB  1 
ATOM   4538 C CG  . LEU A  1 576 ? -16.022 -43.064 50.660  1.00 55.91  ? 603  LEU A CG  1 
ATOM   4539 C CD1 . LEU A  1 576 ? -15.113 -44.282 50.690  1.00 56.45  ? 603  LEU A CD1 1 
ATOM   4540 C CD2 . LEU A  1 576 ? -15.297 -41.869 50.054  1.00 44.11  ? 603  LEU A CD2 1 
ATOM   4541 N N   . GLU A  1 577 ? -20.061 -45.201 49.209  1.00 56.77  ? 604  GLU A N   1 
ATOM   4542 C CA  . GLU A  1 577 ? -21.113 -45.354 48.210  1.00 55.42  ? 604  GLU A CA  1 
ATOM   4543 C C   . GLU A  1 577 ? -22.403 -44.645 48.599  1.00 48.37  ? 604  GLU A C   1 
ATOM   4544 O O   . GLU A  1 577 ? -22.789 -44.632 49.768  1.00 52.79  ? 604  GLU A O   1 
ATOM   4545 C CB  . GLU A  1 577 ? -21.403 -46.833 47.957  1.00 53.77  ? 604  GLU A CB  1 
ATOM   4546 C CG  . GLU A  1 577 ? -22.307 -47.078 46.763  1.00 55.17  ? 604  GLU A CG  1 
ATOM   4547 C CD  . GLU A  1 577 ? -23.453 -48.011 47.083  1.00 56.97  ? 604  GLU A CD  1 
ATOM   4548 O OE1 . GLU A  1 577 ? -23.975 -48.653 46.146  1.00 55.25  ? 604  GLU A OE1 1 
ATOM   4549 O OE2 . GLU A  1 577 ? -23.835 -48.097 48.270  1.00 54.45  1 604  GLU A OE2 1 
ATOM   4550 N N   . GLY A  1 578 ? -23.056 -44.047 47.611  1.00 48.96  ? 605  GLY A N   1 
ATOM   4551 C CA  . GLY A  1 578 ? -24.345 -43.418 47.822  1.00 62.52  ? 605  GLY A CA  1 
ATOM   4552 C C   . GLY A  1 578 ? -24.234 -41.981 48.289  1.00 55.47  ? 605  GLY A C   1 
ATOM   4553 O O   . GLY A  1 578 ? -25.246 -41.319 48.522  1.00 51.72  ? 605  GLY A O   1 
ATOM   4554 N N   . THR A  1 579 ? -23.003 -41.495 48.412  1.00 45.74  ? 606  THR A N   1 
ATOM   4555 C CA  . THR A  1 579 ? -22.767 -40.176 48.982  1.00 46.06  ? 606  THR A CA  1 
ATOM   4556 C C   . THR A  1 579 ? -22.121 -39.213 47.994  1.00 44.62  ? 606  THR A C   1 
ATOM   4557 O O   . THR A  1 579 ? -21.158 -39.568 47.318  1.00 46.70  ? 606  THR A O   1 
ATOM   4558 C CB  . THR A  1 579 ? -21.867 -40.269 50.214  1.00 55.02  ? 606  THR A CB  1 
ATOM   4559 O OG1 . THR A  1 579 ? -20.535 -40.606 49.804  1.00 55.40  ? 606  THR A OG1 1 
ATOM   4560 C CG2 . THR A  1 579 ? -22.395 -41.331 51.174  1.00 55.01  ? 606  THR A CG2 1 
ATOM   4561 N N   . PRO A  1 580 ? -22.654 -37.984 47.921  1.00 43.78  ? 607  PRO A N   1 
ATOM   4562 C CA  . PRO A  1 580 ? -22.192 -36.890 47.055  1.00 48.90  ? 607  PRO A CA  1 
ATOM   4563 C C   . PRO A  1 580 ? -20.734 -36.485 47.274  1.00 48.41  ? 607  PRO A C   1 
ATOM   4564 O O   . PRO A  1 580 ? -20.099 -36.907 48.240  1.00 49.48  ? 607  PRO A O   1 
ATOM   4565 C CB  . PRO A  1 580 ? -23.120 -35.735 47.432  1.00 51.06  ? 607  PRO A CB  1 
ATOM   4566 C CG  . PRO A  1 580 ? -24.360 -36.401 47.901  1.00 52.44  ? 607  PRO A CG  1 
ATOM   4567 C CD  . PRO A  1 580 ? -23.898 -37.630 48.625  1.00 46.97  ? 607  PRO A CD  1 
ATOM   4568 N N   . VAL A  1 581 ? -20.229 -35.648 46.373  1.00 47.01  ? 608  VAL A N   1 
ATOM   4569 C CA  . VAL A  1 581 ? -18.803 -35.356 46.284  1.00 51.22  ? 608  VAL A CA  1 
ATOM   4570 C C   . VAL A  1 581 ? -18.358 -34.233 47.222  1.00 55.87  ? 608  VAL A C   1 
ATOM   4571 O O   . VAL A  1 581 ? -17.212 -34.206 47.674  1.00 57.95  ? 608  VAL A O   1 
ATOM   4572 C CB  . VAL A  1 581 ? -18.409 -35.005 44.833  1.00 51.62  ? 608  VAL A CB  1 
ATOM   4573 C CG1 . VAL A  1 581 ? -16.907 -34.874 44.704  1.00 54.75  ? 608  VAL A CG1 1 
ATOM   4574 C CG2 . VAL A  1 581 ? -18.917 -36.066 43.879  1.00 42.38  ? 608  VAL A CG2 1 
ATOM   4575 N N   . ARG A  1 582 ? -19.265 -33.308 47.515  1.00 60.79  ? 609  ARG A N   1 
ATOM   4576 C CA  . ARG A  1 582 ? -18.951 -32.204 48.418  1.00 70.29  ? 609  ARG A CA  1 
ATOM   4577 C C   . ARG A  1 582 ? -18.924 -32.676 49.874  1.00 68.22  ? 609  ARG A C   1 
ATOM   4578 O O   . ARG A  1 582 ? -18.267 -32.068 50.723  1.00 66.73  ? 609  ARG A O   1 
ATOM   4579 C CB  . ARG A  1 582 ? -19.954 -31.056 48.233  1.00 79.21  ? 609  ARG A CB  1 
ATOM   4580 C CG  . ARG A  1 582 ? -19.662 -29.813 49.072  1.00 89.12  ? 609  ARG A CG  1 
ATOM   4581 C CD  . ARG A  1 582 ? -20.684 -28.701 48.833  1.00 103.26 ? 609  ARG A CD  1 
ATOM   4582 N NE  . ARG A  1 582 ? -20.434 -27.962 47.597  1.00 104.12 ? 609  ARG A NE  1 
ATOM   4583 C CZ  . ARG A  1 582 ? -21.054 -26.835 47.256  1.00 104.85 ? 609  ARG A CZ  1 
ATOM   4584 N NH1 . ARG A  1 582 ? -21.969 -26.305 48.058  1.00 97.18  1 609  ARG A NH1 1 
ATOM   4585 N NH2 . ARG A  1 582 ? -20.757 -26.234 46.113  1.00 112.40 ? 609  ARG A NH2 1 
ATOM   4586 N N   . GLN A  1 583 ? -19.624 -33.775 50.147  1.00 58.63  ? 610  GLN A N   1 
ATOM   4587 C CA  . GLN A  1 583 ? -19.753 -34.298 51.505  1.00 54.25  ? 610  GLN A CA  1 
ATOM   4588 C C   . GLN A  1 583 ? -18.498 -34.998 52.018  1.00 52.62  ? 610  GLN A C   1 
ATOM   4589 O O   . GLN A  1 583 ? -18.106 -34.816 53.171  1.00 59.22  ? 610  GLN A O   1 
ATOM   4590 C CB  . GLN A  1 583 ? -20.933 -35.265 51.593  1.00 53.19  ? 610  GLN A CB  1 
ATOM   4591 C CG  . GLN A  1 583 ? -22.289 -34.622 51.383  1.00 59.23  ? 610  GLN A CG  1 
ATOM   4592 C CD  . GLN A  1 583 ? -23.422 -35.630 51.441  1.00 64.57  ? 610  GLN A CD  1 
ATOM   4593 O OE1 . GLN A  1 583 ? -23.217 -36.790 51.807  1.00 63.48  ? 610  GLN A OE1 1 
ATOM   4594 N NE2 . GLN A  1 583 ? -24.624 -35.195 51.073  1.00 55.90  ? 610  GLN A NE2 1 
ATOM   4595 N N   . ILE A  1 584 ? -17.875 -35.807 51.170  1.00 43.76  ? 611  ILE A N   1 
ATOM   4596 C CA  . ILE A  1 584 ? -16.774 -36.650 51.617  1.00 43.09  ? 611  ILE A CA  1 
ATOM   4597 C C   . ILE A  1 584 ? -15.538 -35.847 52.013  1.00 44.72  ? 611  ILE A C   1 
ATOM   4598 O O   . ILE A  1 584 ? -15.400 -34.675 51.655  1.00 42.32  ? 611  ILE A O   1 
ATOM   4599 C CB  . ILE A  1 584 ? -16.405 -37.719 50.565  1.00 41.13  ? 611  ILE A CB  1 
ATOM   4600 C CG1 . ILE A  1 584 ? -15.776 -37.080 49.334  1.00 37.48  ? 611  ILE A CG1 1 
ATOM   4601 C CG2 . ILE A  1 584 ? -17.635 -38.514 50.155  1.00 50.23  ? 611  ILE A CG2 1 
ATOM   4602 C CD1 . ILE A  1 584 ? -15.538 -38.069 48.233  1.00 35.05  ? 611  ILE A CD1 1 
ATOM   4603 N N   . GLU A  1 585 ? -14.657 -36.491 52.774  1.00 44.38  ? 612  GLU A N   1 
ATOM   4604 C CA  . GLU A  1 585 ? -13.402 -35.886 53.204  1.00 41.18  ? 612  GLU A CA  1 
ATOM   4605 C C   . GLU A  1 585 ? -12.211 -36.717 52.724  1.00 38.47  ? 612  GLU A C   1 
ATOM   4606 O O   . GLU A  1 585 ? -12.168 -37.930 52.929  1.00 42.00  ? 612  GLU A O   1 
ATOM   4607 C CB  . GLU A  1 585 ? -13.379 -35.718 54.723  1.00 41.99  ? 612  GLU A CB  1 
ATOM   4608 C CG  . GLU A  1 585 ? -14.316 -34.633 55.227  1.00 50.73  ? 612  GLU A CG  1 
ATOM   4609 C CD  . GLU A  1 585 ? -14.201 -34.409 56.720  1.00 64.33  ? 612  GLU A CD  1 
ATOM   4610 O OE1 . GLU A  1 585 ? -13.886 -35.376 57.446  1.00 63.72  ? 612  GLU A OE1 1 
ATOM   4611 O OE2 . GLU A  1 585 ? -14.421 -33.264 57.168  1.00 74.53  1 612  GLU A OE2 1 
ATOM   4612 N N   . PRO A  1 586 ? -11.233 -36.052 52.094  1.00 31.98  ? 613  PRO A N   1 
ATOM   4613 C CA  . PRO A  1 586 ? -10.129 -36.644 51.325  1.00 36.83  ? 613  PRO A CA  1 
ATOM   4614 C C   . PRO A  1 586 ? -9.314  -37.762 52.001  1.00 42.84  ? 613  PRO A C   1 
ATOM   4615 O O   . PRO A  1 586 ? -8.507  -38.410 51.329  1.00 44.06  ? 613  PRO A O   1 
ATOM   4616 C CB  . PRO A  1 586 ? -9.234  -35.434 51.011  1.00 37.60  ? 613  PRO A CB  1 
ATOM   4617 C CG  . PRO A  1 586 ? -9.675  -34.361 51.947  1.00 37.96  ? 613  PRO A CG  1 
ATOM   4618 C CD  . PRO A  1 586 ? -11.125 -34.587 52.153  1.00 33.46  ? 613  PRO A CD  1 
ATOM   4619 N N   . GLN A  1 587 ? -9.511  -37.992 53.294  1.00 44.61  ? 614  GLN A N   1 
ATOM   4620 C CA  . GLN A  1 587 ? -8.773  -39.050 53.978  1.00 44.48  ? 614  GLN A CA  1 
ATOM   4621 C C   . GLN A  1 587 ? -9.457  -40.395 53.804  1.00 41.31  ? 614  GLN A C   1 
ATOM   4622 O O   . GLN A  1 587 ? -8.889  -41.437 54.128  1.00 48.61  ? 614  GLN A O   1 
ATOM   4623 C CB  . GLN A  1 587 ? -8.592  -38.736 55.465  1.00 41.32  ? 614  GLN A CB  1 
ATOM   4624 C CG  . GLN A  1 587 ? -9.810  -38.133 56.135  1.00 36.65  ? 614  GLN A CG  1 
ATOM   4625 C CD  . GLN A  1 587 ? -9.875  -36.627 55.957  1.00 45.56  ? 614  GLN A CD  1 
ATOM   4626 O OE1 . GLN A  1 587 ? -9.146  -36.059 55.142  1.00 44.33  ? 614  GLN A OE1 1 
ATOM   4627 N NE2 . GLN A  1 587 ? -10.743 -35.971 56.723  1.00 45.33  ? 614  GLN A NE2 1 
ATOM   4628 N N   . THR A  1 588 ? -10.681 -40.368 53.294  1.00 30.68  ? 615  THR A N   1 
ATOM   4629 C CA  . THR A  1 588 ? -11.397 -41.600 53.010  1.00 37.42  ? 615  THR A CA  1 
ATOM   4630 C C   . THR A  1 588 ? -10.926 -42.119 51.664  1.00 37.50  ? 615  THR A C   1 
ATOM   4631 O O   . THR A  1 588 ? -10.968 -43.320 51.384  1.00 33.07  ? 615  THR A O   1 
ATOM   4632 C CB  . THR A  1 588 ? -12.913 -41.369 52.952  1.00 40.80  ? 615  THR A CB  1 
ATOM   4633 O OG1 . THR A  1 588 ? -13.256 -40.221 53.738  1.00 41.03  ? 615  THR A OG1 1 
ATOM   4634 C CG2 . THR A  1 588 ? -13.659 -42.593 53.472  1.00 36.28  ? 615  THR A CG2 1 
ATOM   4635 N N   . LEU A  1 589 ? -10.474 -41.192 50.830  1.00 37.20  ? 616  LEU A N   1 
ATOM   4636 C CA  . LEU A  1 589 ? -10.003 -41.533 49.501  1.00 38.66  ? 616  LEU A CA  1 
ATOM   4637 C C   . LEU A  1 589 ? -8.695  -42.306 49.600  1.00 37.81  ? 616  LEU A C   1 
ATOM   4638 O O   . LEU A  1 589 ? -7.606  -41.726 49.567  1.00 34.10  ? 616  LEU A O   1 
ATOM   4639 C CB  . LEU A  1 589 ? -9.838  -40.272 48.653  1.00 35.27  ? 616  LEU A CB  1 
ATOM   4640 C CG  . LEU A  1 589 ? -11.060 -39.352 48.645  1.00 25.97  ? 616  LEU A CG  1 
ATOM   4641 C CD1 . LEU A  1 589 ? -10.840 -38.189 47.695  1.00 31.44  ? 616  LEU A CD1 1 
ATOM   4642 C CD2 . LEU A  1 589 ? -12.310 -40.125 48.279  1.00 23.76  ? 616  LEU A CD2 1 
ATOM   4643 N N   . ILE A  1 590 ? -8.825  -43.621 49.736  1.00 36.69  ? 617  ILE A N   1 
ATOM   4644 C CA  . ILE A  1 590 ? -7.683  -44.512 49.855  1.00 35.17  ? 617  ILE A CA  1 
ATOM   4645 C C   . ILE A  1 590 ? -7.673  -45.517 48.710  1.00 32.77  ? 617  ILE A C   1 
ATOM   4646 O O   . ILE A  1 590 ? -8.723  -45.882 48.182  1.00 30.07  ? 617  ILE A O   1 
ATOM   4647 C CB  . ILE A  1 590 ? -7.715  -45.264 51.192  1.00 37.56  ? 617  ILE A CB  1 
ATOM   4648 C CG1 . ILE A  1 590 ? -8.987  -46.102 51.298  1.00 41.44  ? 617  ILE A CG1 1 
ATOM   4649 C CG2 . ILE A  1 590 ? -7.675  -44.289 52.345  1.00 39.98  ? 617  ILE A CG2 1 
ATOM   4650 C CD1 . ILE A  1 590 ? -9.174  -46.759 52.648  1.00 41.05  ? 617  ILE A CD1 1 
ATOM   4651 N N   . CYS A  1 591 ? -6.481  -45.958 48.326  1.00 34.52  ? 618  CYS A N   1 
ATOM   4652 C CA  . CYS A  1 591 ? -6.335  -46.927 47.244  1.00 40.34  ? 618  CYS A CA  1 
ATOM   4653 C C   . CYS A  1 591 ? -5.635  -48.186 47.748  1.00 45.23  ? 618  CYS A C   1 
ATOM   4654 O O   . CYS A  1 591 ? -4.424  -48.174 47.972  1.00 48.34  ? 618  CYS A O   1 
ATOM   4655 C CB  . CYS A  1 591 ? -5.552  -46.321 46.076  1.00 33.19  ? 618  CYS A CB  1 
ATOM   4656 S SG  . CYS A  1 591 ? -6.230  -44.766 45.455  1.00 38.73  ? 618  CYS A SG  1 
ATOM   4657 N N   . PRO A  1 592 ? -6.401  -49.277 47.924  1.00 44.57  ? 619  PRO A N   1 
ATOM   4658 C CA  . PRO A  1 592 ? -5.922  -50.536 48.506  1.00 40.43  ? 619  PRO A CA  1 
ATOM   4659 C C   . PRO A  1 592 ? -4.609  -51.034 47.914  1.00 41.75  ? 619  PRO A C   1 
ATOM   4660 O O   . PRO A  1 592 ? -4.481  -51.145 46.696  1.00 34.69  ? 619  PRO A O   1 
ATOM   4661 C CB  . PRO A  1 592 ? -7.049  -51.513 48.179  1.00 31.81  ? 619  PRO A CB  1 
ATOM   4662 C CG  . PRO A  1 592 ? -8.265  -50.665 48.174  1.00 31.28  ? 619  PRO A CG  1 
ATOM   4663 C CD  . PRO A  1 592 ? -7.837  -49.341 47.598  1.00 40.87  ? 619  PRO A CD  1 
ATOM   4664 N N   . LEU A  1 593 ? -3.644  -51.309 48.788  1.00 49.23  ? 620  LEU A N   1 
ATOM   4665 C CA  . LEU A  1 593 ? -2.396  -51.947 48.395  1.00 52.34  ? 620  LEU A CA  1 
ATOM   4666 C C   . LEU A  1 593 ? -2.589  -53.457 48.496  1.00 57.02  ? 620  LEU A C   1 
ATOM   4667 O O   . LEU A  1 593 ? -2.932  -53.975 49.560  1.00 55.92  ? 620  LEU A O   1 
ATOM   4668 C CB  . LEU A  1 593 ? -1.243  -51.482 49.295  1.00 44.02  ? 620  LEU A CB  1 
ATOM   4669 C CG  . LEU A  1 593 ? 0.203   -51.649 48.800  1.00 36.05  ? 620  LEU A CG  1 
ATOM   4670 C CD1 . LEU A  1 593 ? 1.149   -50.759 49.591  1.00 29.65  ? 620  LEU A CD1 1 
ATOM   4671 C CD2 . LEU A  1 593 ? 0.674   -53.096 48.865  1.00 40.73  ? 620  LEU A CD2 1 
ATOM   4672 N N   . ASP A  1 594 ? -2.378  -54.155 47.383  1.00 59.09  ? 621  ASP A N   1 
ATOM   4673 C CA  . ASP A  1 594 ? -2.575  -55.601 47.332  1.00 59.61  ? 621  ASP A CA  1 
ATOM   4674 C C   . ASP A  1 594 ? -1.600  -56.341 48.245  1.00 59.89  ? 621  ASP A C   1 
ATOM   4675 O O   . ASP A  1 594 ? -0.463  -56.613 47.863  1.00 56.17  ? 621  ASP A O   1 
ATOM   4676 C CB  . ASP A  1 594 ? -2.438  -56.112 45.894  1.00 74.59  ? 621  ASP A CB  1 
ATOM   4677 C CG  . ASP A  1 594 ? -3.513  -55.561 44.973  1.00 73.58  ? 621  ASP A CG  1 
ATOM   4678 O OD1 . ASP A  1 594 ? -4.508  -55.008 45.486  1.00 69.30  ? 621  ASP A OD1 1 
ATOM   4679 O OD2 . ASP A  1 594 ? -3.368  -55.690 43.737  1.00 70.48  1 621  ASP A OD2 1 
ATOM   4680 N N   . LYS A  1 603 ? 4.573   -55.860 48.665  1.00 42.32  ? 630  LYS A N   1 
ATOM   4681 C CA  . LYS A  1 603 ? 3.126   -55.947 48.827  1.00 55.61  ? 630  LYS A CA  1 
ATOM   4682 C C   . LYS A  1 603 ? 2.759   -56.109 50.302  1.00 62.15  ? 630  LYS A C   1 
ATOM   4683 O O   . LYS A  1 603 ? 3.637   -56.302 51.142  1.00 62.22  ? 630  LYS A O   1 
ATOM   4684 C CB  . LYS A  1 603 ? 2.552   -57.098 47.992  1.00 48.65  ? 630  LYS A CB  1 
ATOM   4685 C CG  . LYS A  1 603 ? 3.159   -58.460 48.289  1.00 52.18  ? 630  LYS A CG  1 
ATOM   4686 C CD  . LYS A  1 603 ? 2.090   -59.535 48.405  1.00 43.22  ? 630  LYS A CD  1 
ATOM   4687 C CE  . LYS A  1 603 ? 1.287   -59.671 47.125  1.00 41.44  ? 630  LYS A CE  1 
ATOM   4688 N NZ  . LYS A  1 603 ? 0.156   -60.631 47.288  1.00 34.86  1 630  LYS A NZ  1 
ATOM   4689 N N   . CYS A  1 604 ? 1.466   -56.030 50.609  1.00 65.56  ? 631  CYS A N   1 
ATOM   4690 C CA  . CYS A  1 604 ? 0.985   -56.085 51.993  1.00 62.98  ? 631  CYS A CA  1 
ATOM   4691 C C   . CYS A  1 604 ? 1.017   -57.488 52.605  1.00 65.25  ? 631  CYS A C   1 
ATOM   4692 O O   . CYS A  1 604 ? 0.764   -58.475 51.913  1.00 65.21  ? 631  CYS A O   1 
ATOM   4693 C CB  . CYS A  1 604 ? -0.429  -55.503 52.094  1.00 60.43  ? 631  CYS A CB  1 
ATOM   4694 S SG  . CYS A  1 604 ? -0.469  -53.749 52.527  1.00 81.52  ? 631  CYS A SG  1 
ATOM   4695 N N   . PRO A  1 605 ? 1.319   -57.572 53.915  1.00 68.22  ? 632  PRO A N   1 
ATOM   4696 C CA  . PRO A  1 605 ? 1.429   -58.834 54.664  1.00 68.48  ? 632  PRO A CA  1 
ATOM   4697 C C   . PRO A  1 605 ? 0.105   -59.580 54.815  1.00 66.40  ? 632  PRO A C   1 
ATOM   4698 O O   . PRO A  1 605 ? -0.961  -58.964 54.761  1.00 64.28  ? 632  PRO A O   1 
ATOM   4699 C CB  . PRO A  1 605 ? 1.925   -58.381 56.042  1.00 60.56  ? 632  PRO A CB  1 
ATOM   4700 C CG  . PRO A  1 605 ? 1.505   -56.961 56.150  1.00 56.46  ? 632  PRO A CG  1 
ATOM   4701 C CD  . PRO A  1 605 ? 1.629   -56.408 54.765  1.00 62.75  ? 632  PRO A CD  1 
ATOM   4702 N N   . ARG A  1 606 ? 0.184   -60.896 55.008  1.00 55.66  ? 633  ARG A N   1 
ATOM   4703 C CA  . ARG A  1 606 ? -1.008  -61.713 55.192  1.00 56.80  ? 633  ARG A CA  1 
ATOM   4704 C C   . ARG A  1 606 ? -1.678  -61.371 56.512  1.00 50.91  ? 633  ARG A C   1 
ATOM   4705 O O   . ARG A  1 606 ? -1.007  -61.104 57.503  1.00 58.85  ? 633  ARG A O   1 
ATOM   4706 C CB  . ARG A  1 606 ? -0.665  -63.205 55.149  1.00 71.95  ? 633  ARG A CB  1 
ATOM   4707 C CG  . ARG A  1 606 ? -0.248  -63.722 53.776  1.00 97.32  ? 633  ARG A CG  1 
ATOM   4708 C CD  . ARG A  1 606 ? -0.260  -65.249 53.731  1.00 107.48 ? 633  ARG A CD  1 
ATOM   4709 N NE  . ARG A  1 606 ? 0.342   -65.781 52.509  1.00 114.09 ? 633  ARG A NE  1 
ATOM   4710 C CZ  . ARG A  1 606 ? -0.326  -66.043 51.389  1.00 115.05 ? 633  ARG A CZ  1 
ATOM   4711 N NH1 . ARG A  1 606 ? -1.633  -65.821 51.320  1.00 113.01 1 633  ARG A NH1 1 
ATOM   4712 N NH2 . ARG A  1 606 ? 0.315   -66.527 50.333  1.00 110.94 ? 633  ARG A NH2 1 
ATOM   4713 N N   . GLY A  1 607 ? -3.006  -61.372 56.520  1.00 55.25  ? 634  GLY A N   1 
ATOM   4714 C CA  . GLY A  1 607 ? -3.759  -61.057 57.720  1.00 56.99  ? 634  GLY A CA  1 
ATOM   4715 C C   . GLY A  1 607 ? -3.926  -59.565 57.935  1.00 50.35  ? 634  GLY A C   1 
ATOM   4716 O O   . GLY A  1 607 ? -4.674  -59.135 58.817  1.00 43.31  ? 634  GLY A O   1 
ATOM   4717 N N   . CYS A  1 608 ? -3.231  -58.778 57.118  1.00 50.41  ? 635  CYS A N   1 
ATOM   4718 C CA  . CYS A  1 608 ? -3.249  -57.324 57.239  1.00 56.28  ? 635  CYS A CA  1 
ATOM   4719 C C   . CYS A  1 608 ? -3.864  -56.656 56.012  1.00 61.30  ? 635  CYS A C   1 
ATOM   4720 O O   . CYS A  1 608 ? -3.316  -56.744 54.911  1.00 63.96  ? 635  CYS A O   1 
ATOM   4721 C CB  . CYS A  1 608 ? -1.826  -56.784 57.425  1.00 58.92  ? 635  CYS A CB  1 
ATOM   4722 S SG  . CYS A  1 608 ? -0.869  -57.499 58.785  1.00 57.79  ? 635  CYS A SG  1 
ATOM   4723 N N   . ASN A  1 609 ? -4.993  -55.979 56.201  1.00 55.69  ? 636  ASN A N   1 
ATOM   4724 C CA  . ASN A  1 609 ? -5.554  -55.156 55.137  1.00 52.40  ? 636  ASN A CA  1 
ATOM   4725 C C   . ASN A  1 609 ? -4.812  -53.830 55.081  1.00 47.39  ? 636  ASN A C   1 
ATOM   4726 O O   . ASN A  1 609 ? -4.457  -53.261 56.111  1.00 51.07  ? 636  ASN A O   1 
ATOM   4727 C CB  . ASN A  1 609 ? -7.049  -54.919 55.346  1.00 56.79  ? 636  ASN A CB  1 
ATOM   4728 C CG  . ASN A  1 609 ? -7.339  -53.606 56.042  1.00 51.20  ? 636  ASN A CG  1 
ATOM   4729 O OD1 . ASN A  1 609 ? -7.506  -52.568 55.395  1.00 54.36  ? 636  ASN A OD1 1 
ATOM   4730 N ND2 . ASN A  1 609 ? -7.396  -53.641 57.368  1.00 43.37  ? 636  ASN A ND2 1 
ATOM   4731 N N   . CYS A  1 610 ? -4.558  -53.340 53.878  1.00 47.29  ? 637  CYS A N   1 
ATOM   4732 C CA  . CYS A  1 610 ? -3.759  -52.135 53.731  1.00 47.95  ? 637  CYS A CA  1 
ATOM   4733 C C   . CYS A  1 610 ? -4.393  -51.187 52.724  1.00 55.96  ? 637  CYS A C   1 
ATOM   4734 O O   . CYS A  1 610 ? -5.273  -51.582 51.957  1.00 56.03  ? 637  CYS A O   1 
ATOM   4735 C CB  . CYS A  1 610 ? -2.344  -52.509 53.303  1.00 46.09  ? 637  CYS A CB  1 
ATOM   4736 S SG  . CYS A  1 610 ? -1.763  -54.044 54.061  1.00 48.82  ? 637  CYS A SG  1 
ATOM   4737 N N   . HIS A  1 611 ? -3.948  -49.934 52.740  1.00 48.67  ? 638  HIS A N   1 
ATOM   4738 C CA  . HIS A  1 611 ? -4.458  -48.923 51.822  1.00 45.68  ? 638  HIS A CA  1 
ATOM   4739 C C   . HIS A  1 611 ? -3.582  -47.682 51.852  1.00 42.91  ? 638  HIS A C   1 
ATOM   4740 O O   . HIS A  1 611 ? -2.796  -47.494 52.775  1.00 41.95  ? 638  HIS A O   1 
ATOM   4741 C CB  . HIS A  1 611 ? -5.894  -48.542 52.178  1.00 44.11  ? 638  HIS A CB  1 
ATOM   4742 C CG  . HIS A  1 611 ? -6.033  -47.889 53.517  1.00 44.80  ? 638  HIS A CG  1 
ATOM   4743 N ND1 . HIS A  1 611 ? -6.576  -48.534 54.606  1.00 47.79  ? 638  HIS A ND1 1 
ATOM   4744 C CD2 . HIS A  1 611 ? -5.707  -46.644 53.940  1.00 41.17  ? 638  HIS A CD2 1 
ATOM   4745 C CE1 . HIS A  1 611 ? -6.577  -47.716 55.644  1.00 48.82  ? 638  HIS A CE1 1 
ATOM   4746 N NE2 . HIS A  1 611 ? -6.055  -46.563 55.267  1.00 45.24  ? 638  HIS A NE2 1 
ATOM   4747 N N   . VAL A  1 612 ? -3.733  -46.830 50.844  1.00 47.13  ? 639  VAL A N   1 
ATOM   4748 C CA  . VAL A  1 612 ? -2.964  -45.594 50.761  1.00 42.07  ? 639  VAL A CA  1 
ATOM   4749 C C   . VAL A  1 612 ? -3.856  -44.397 50.451  1.00 41.29  ? 639  VAL A C   1 
ATOM   4750 O O   . VAL A  1 612 ? -4.509  -44.360 49.410  1.00 39.30  ? 639  VAL A O   1 
ATOM   4751 C CB  . VAL A  1 612 ? -1.889  -45.680 49.670  1.00 28.37  ? 639  VAL A CB  1 
ATOM   4752 C CG1 . VAL A  1 612 ? -1.200  -44.341 49.509  1.00 30.41  ? 639  VAL A CG1 1 
ATOM   4753 C CG2 . VAL A  1 612 ? -0.892  -46.765 50.001  1.00 28.38  ? 639  VAL A CG2 1 
ATOM   4754 N N   . ARG A  1 613 ? -3.886  -43.422 51.354  1.00 39.51  ? 640  ARG A N   1 
ATOM   4755 C CA  . ARG A  1 613 ? -4.598  -42.178 51.093  1.00 39.09  ? 640  ARG A CA  1 
ATOM   4756 C C   . ARG A  1 613 ? -3.621  -41.126 50.606  1.00 35.64  ? 640  ARG A C   1 
ATOM   4757 O O   . ARG A  1 613 ? -2.610  -40.862 51.250  1.00 33.35  ? 640  ARG A O   1 
ATOM   4758 C CB  . ARG A  1 613 ? -5.331  -41.689 52.341  1.00 41.48  ? 640  ARG A CB  1 
ATOM   4759 C CG  . ARG A  1 613 ? -4.528  -41.816 53.611  1.00 41.25  ? 640  ARG A CG  1 
ATOM   4760 C CD  . ARG A  1 613 ? -5.429  -41.888 54.828  1.00 45.58  ? 640  ARG A CD  1 
ATOM   4761 N NE  . ARG A  1 613 ? -4.643  -42.095 56.038  1.00 53.36  ? 640  ARG A NE  1 
ATOM   4762 C CZ  . ARG A  1 613 ? -4.228  -41.115 56.832  1.00 45.72  ? 640  ARG A CZ  1 
ATOM   4763 N NH1 . ARG A  1 613 ? -3.511  -41.392 57.912  1.00 36.23  1 640  ARG A NH1 1 
ATOM   4764 N NH2 . ARG A  1 613 ? -4.541  -39.857 56.549  1.00 46.84  ? 640  ARG A NH2 1 
ATOM   4765 N N   . THR A  1 614 ? -3.923  -40.535 49.457  1.00 38.88  ? 641  THR A N   1 
ATOM   4766 C CA  . THR A  1 614 ? -3.049  -39.530 48.874  1.00 37.22  ? 641  THR A CA  1 
ATOM   4767 C C   . THR A  1 614 ? -3.334  -38.163 49.458  1.00 34.44  ? 641  THR A C   1 
ATOM   4768 O O   . THR A  1 614 ? -2.737  -37.174 49.049  1.00 37.60  ? 641  THR A O   1 
ATOM   4769 C CB  . THR A  1 614 ? -3.191  -39.454 47.345  1.00 40.17  ? 641  THR A CB  1 
ATOM   4770 O OG1 . THR A  1 614 ? -4.574  -39.317 46.998  1.00 45.72  ? 641  THR A OG1 1 
ATOM   4771 C CG2 . THR A  1 614 ? -2.626  -40.706 46.691  1.00 39.42  ? 641  THR A CG2 1 
ATOM   4772 N N   . TYR A  1 615 ? -4.250  -38.107 50.417  1.00 36.26  ? 642  TYR A N   1 
ATOM   4773 C CA  . TYR A  1 615 ? -4.521  -36.854 51.103  1.00 43.54  ? 642  TYR A CA  1 
ATOM   4774 C C   . TYR A  1 615 ? -3.310  -36.389 51.913  1.00 44.66  ? 642  TYR A C   1 
ATOM   4775 O O   . TYR A  1 615 ? -3.085  -35.189 52.078  1.00 41.96  ? 642  TYR A O   1 
ATOM   4776 C CB  . TYR A  1 615 ? -5.742  -36.979 52.011  1.00 43.87  ? 642  TYR A CB  1 
ATOM   4777 C CG  . TYR A  1 615 ? -5.873  -35.821 52.965  1.00 43.45  ? 642  TYR A CG  1 
ATOM   4778 C CD1 . TYR A  1 615 ? -6.160  -34.544 52.498  1.00 42.88  ? 642  TYR A CD1 1 
ATOM   4779 C CD2 . TYR A  1 615 ? -5.689  -35.997 54.328  1.00 46.53  ? 642  TYR A CD2 1 
ATOM   4780 C CE1 . TYR A  1 615 ? -6.275  -33.475 53.364  1.00 56.89  ? 642  TYR A CE1 1 
ATOM   4781 C CE2 . TYR A  1 615 ? -5.800  -34.934 55.206  1.00 64.66  ? 642  TYR A CE2 1 
ATOM   4782 C CZ  . TYR A  1 615 ? -6.094  -33.673 54.721  1.00 71.90  ? 642  TYR A CZ  1 
ATOM   4783 O OH  . TYR A  1 615 ? -6.205  -32.612 55.597  1.00 67.58  ? 642  TYR A OH  1 
ATOM   4784 N N   . ASP A  1 616 ? -2.531  -37.347 52.408  1.00 44.31  ? 643  ASP A N   1 
ATOM   4785 C CA  . ASP A  1 616 ? -1.366  -37.042 53.230  1.00 38.30  ? 643  ASP A CA  1 
ATOM   4786 C C   . ASP A  1 616 ? -0.169  -37.930 52.900  1.00 38.46  ? 643  ASP A C   1 
ATOM   4787 O O   . ASP A  1 616 ? 0.800   -37.972 53.657  1.00 44.19  ? 643  ASP A O   1 
ATOM   4788 C CB  . ASP A  1 616 ? -1.711  -37.179 54.714  1.00 41.20  ? 643  ASP A CB  1 
ATOM   4789 C CG  . ASP A  1 616 ? -2.367  -38.505 55.040  1.00 42.18  ? 643  ASP A CG  1 
ATOM   4790 O OD1 . ASP A  1 616 ? -2.539  -39.329 54.119  1.00 43.93  ? 643  ASP A OD1 1 
ATOM   4791 O OD2 . ASP A  1 616 ? -2.712  -38.729 56.219  1.00 39.74  1 643  ASP A OD2 1 
ATOM   4792 N N   . LYS A  1 617 ? -0.248  -38.633 51.773  1.00 38.80  ? 644  LYS A N   1 
ATOM   4793 C CA  . LYS A  1 617 ? 0.804   -39.552 51.333  1.00 41.17  ? 644  LYS A CA  1 
ATOM   4794 C C   . LYS A  1 617 ? 1.131   -40.585 52.403  1.00 40.61  ? 644  LYS A C   1 
ATOM   4795 O O   . LYS A  1 617 ? 2.292   -40.932 52.607  1.00 42.50  ? 644  LYS A O   1 
ATOM   4796 C CB  . LYS A  1 617 ? 2.068   -38.785 50.945  1.00 39.85  ? 644  LYS A CB  1 
ATOM   4797 C CG  . LYS A  1 617 ? 1.812   -37.578 50.060  1.00 44.27  ? 644  LYS A CG  1 
ATOM   4798 C CD  . LYS A  1 617 ? 3.115   -36.882 49.691  1.00 56.86  ? 644  LYS A CD  1 
ATOM   4799 C CE  . LYS A  1 617 ? 2.868   -35.520 49.055  1.00 53.41  ? 644  LYS A CE  1 
ATOM   4800 N NZ  . LYS A  1 617 ? 4.144   -34.826 48.712  1.00 49.13  1 644  LYS A NZ  1 
ATOM   4801 N N   . ALA A  1 618 ? 0.099   -41.077 53.078  1.00 39.18  ? 645  ALA A N   1 
ATOM   4802 C CA  . ALA A  1 618 ? 0.279   -41.950 54.232  1.00 39.75  ? 645  ALA A CA  1 
ATOM   4803 C C   . ALA A  1 618 ? 0.021   -43.416 53.916  1.00 43.71  ? 645  ALA A C   1 
ATOM   4804 O O   . ALA A  1 618 ? -1.101  -43.797 53.577  1.00 47.31  ? 645  ALA A O   1 
ATOM   4805 C CB  . ALA A  1 618 ? -0.622  -41.499 55.372  1.00 46.15  ? 645  ALA A CB  1 
ATOM   4806 N N   . LEU A  1 619 ? 1.057   -44.239 54.044  1.00 37.86  ? 646  LEU A N   1 
ATOM   4807 C CA  . LEU A  1 619 ? 0.906   -45.677 53.862  1.00 35.52  ? 646  LEU A CA  1 
ATOM   4808 C C   . LEU A  1 619 ? 0.436   -46.321 55.161  1.00 33.08  ? 646  LEU A C   1 
ATOM   4809 O O   . LEU A  1 619 ? 1.182   -46.399 56.136  1.00 37.17  ? 646  LEU A O   1 
ATOM   4810 C CB  . LEU A  1 619 ? 2.212   -46.304 53.372  1.00 31.72  ? 646  LEU A CB  1 
ATOM   4811 C CG  . LEU A  1 619 ? 2.289   -47.829 53.295  1.00 28.50  ? 646  LEU A CG  1 
ATOM   4812 C CD1 . LEU A  1 619 ? 1.070   -48.432 52.616  1.00 26.23  ? 646  LEU A CD1 1 
ATOM   4813 C CD2 . LEU A  1 619 ? 3.559   -48.230 52.568  1.00 32.65  ? 646  LEU A CD2 1 
ATOM   4814 N N   . VAL A  1 620 ? -0.812  -46.775 55.160  1.00 32.61  ? 647  VAL A N   1 
ATOM   4815 C CA  . VAL A  1 620 ? -1.438  -47.349 56.343  1.00 30.84  ? 647  VAL A CA  1 
ATOM   4816 C C   . VAL A  1 620 ? -1.438  -48.874 56.278  1.00 38.21  ? 647  VAL A C   1 
ATOM   4817 O O   . VAL A  1 620 ? -1.707  -49.456 55.227  1.00 51.69  ? 647  VAL A O   1 
ATOM   4818 C CB  . VAL A  1 620 ? -2.881  -46.846 56.488  1.00 27.94  ? 647  VAL A CB  1 
ATOM   4819 C CG1 . VAL A  1 620 ? -3.517  -47.401 57.749  1.00 29.18  ? 647  VAL A CG1 1 
ATOM   4820 C CG2 . VAL A  1 620 ? -2.904  -45.326 56.491  1.00 30.16  ? 647  VAL A CG2 1 
ATOM   4821 N N   . ILE A  1 621 ? -1.123  -49.519 57.398  1.00 33.62  ? 648  ILE A N   1 
ATOM   4822 C CA  . ILE A  1 621 ? -1.076  -50.973 57.454  1.00 28.77  ? 648  ILE A CA  1 
ATOM   4823 C C   . ILE A  1 621 ? -1.822  -51.499 58.670  1.00 29.84  ? 648  ILE A C   1 
ATOM   4824 O O   . ILE A  1 621 ? -1.312  -51.436 59.782  1.00 37.59  ? 648  ILE A O   1 
ATOM   4825 C CB  . ILE A  1 621 ? 0.365   -51.473 57.539  1.00 25.41  ? 648  ILE A CB  1 
ATOM   4826 C CG1 . ILE A  1 621 ? 1.251   -50.727 56.539  1.00 27.17  ? 648  ILE A CG1 1 
ATOM   4827 C CG2 . ILE A  1 621 ? 0.409   -52.970 57.314  1.00 35.59  ? 648  ILE A CG2 1 
ATOM   4828 C CD1 . ILE A  1 621 ? 2.699   -51.157 56.563  1.00 32.76  ? 648  ILE A CD1 1 
ATOM   4829 N N   . ASN A  1 622 ? -3.024  -52.026 58.462  1.00 36.06  ? 649  ASN A N   1 
ATOM   4830 C CA  . ASN A  1 622 ? -3.845  -52.510 59.571  1.00 39.83  ? 649  ASN A CA  1 
ATOM   4831 C C   . ASN A  1 622 ? -3.751  -54.017 59.798  1.00 47.49  ? 649  ASN A C   1 
ATOM   4832 O O   . ASN A  1 622 ? -4.347  -54.804 59.061  1.00 50.73  ? 649  ASN A O   1 
ATOM   4833 C CB  . ASN A  1 622 ? -5.305  -52.109 59.373  1.00 35.63  ? 649  ASN A CB  1 
ATOM   4834 C CG  . ASN A  1 622 ? -5.484  -50.615 59.270  1.00 39.99  ? 649  ASN A CG  1 
ATOM   4835 O OD1 . ASN A  1 622 ? -4.646  -49.849 59.741  1.00 40.51  ? 649  ASN A OD1 1 
ATOM   4836 N ND2 . ASN A  1 622 ? -6.579  -50.189 58.652  1.00 44.52  ? 649  ASN A ND2 1 
ATOM   4837 N N   . CYS A  1 623 ? -3.009  -54.410 60.828  1.00 49.66  ? 650  CYS A N   1 
ATOM   4838 C CA  . CYS A  1 623 ? -2.862  -55.818 61.178  1.00 47.24  ? 650  CYS A CA  1 
ATOM   4839 C C   . CYS A  1 623 ? -3.591  -56.120 62.478  1.00 46.64  ? 650  CYS A C   1 
ATOM   4840 O O   . CYS A  1 623 ? -2.984  -56.559 63.451  1.00 46.01  ? 650  CYS A O   1 
ATOM   4841 C CB  . CYS A  1 623 ? -1.385  -56.184 61.316  1.00 45.42  ? 650  CYS A CB  1 
ATOM   4842 S SG  . CYS A  1 623 ? -0.392  -55.834 59.847  1.00 53.28  ? 650  CYS A SG  1 
ATOM   4843 N N   . HIS A  1 624 ? -4.900  -55.890 62.481  1.00 50.49  ? 651  HIS A N   1 
ATOM   4844 C CA  . HIS A  1 624 ? -5.708  -56.022 63.688  1.00 53.13  ? 651  HIS A CA  1 
ATOM   4845 C C   . HIS A  1 624 ? -6.359  -57.395 63.777  1.00 62.35  ? 651  HIS A C   1 
ATOM   4846 O O   . HIS A  1 624 ? -7.539  -57.522 64.107  1.00 57.97  ? 651  HIS A O   1 
ATOM   4847 C CB  . HIS A  1 624 ? -6.767  -54.927 63.723  1.00 46.65  ? 651  HIS A CB  1 
ATOM   4848 C CG  . HIS A  1 624 ? -6.232  -53.574 63.379  1.00 48.07  ? 651  HIS A CG  1 
ATOM   4849 N ND1 . HIS A  1 624 ? -6.994  -52.607 62.760  1.00 53.35  ? 651  HIS A ND1 1 
ATOM   4850 C CD2 . HIS A  1 624 ? -5.006  -53.030 63.559  1.00 46.64  ? 651  HIS A CD2 1 
ATOM   4851 C CE1 . HIS A  1 624 ? -6.261  -51.523 62.579  1.00 53.38  ? 651  HIS A CE1 1 
ATOM   4852 N NE2 . HIS A  1 624 ? -5.050  -51.754 63.053  1.00 48.26  ? 651  HIS A NE2 1 
ATOM   4853 N N   . SER A  1 625 ? -5.570  -58.421 63.479  1.00 70.54  ? 652  SER A N   1 
ATOM   4854 C CA  . SER A  1 625 ? -6.024  -59.801 63.563  1.00 69.91  ? 652  SER A CA  1 
ATOM   4855 C C   . SER A  1 625 ? -6.011  -60.278 65.013  1.00 68.66  ? 652  SER A C   1 
ATOM   4856 O O   . SER A  1 625 ? -6.937  -60.953 65.463  1.00 65.10  ? 652  SER A O   1 
ATOM   4857 C CB  . SER A  1 625 ? -5.133  -60.690 62.696  1.00 66.74  ? 652  SER A CB  1 
ATOM   4858 O OG  . SER A  1 625 ? -3.779  -60.278 62.780  1.00 56.83  ? 652  SER A OG  1 
ATOM   4859 N N   . GLY A  1 626 ? -4.956  -59.917 65.738  1.00 64.56  ? 653  GLY A N   1 
ATOM   4860 C CA  . GLY A  1 626 ? -4.843  -60.254 67.145  1.00 63.13  ? 653  GLY A CA  1 
ATOM   4861 C C   . GLY A  1 626 ? -4.020  -61.501 67.406  1.00 66.05  ? 653  GLY A C   1 
ATOM   4862 O O   . GLY A  1 626 ? -4.213  -62.177 68.419  1.00 62.91  ? 653  GLY A O   1 
ATOM   4863 N N   . ASN A  1 627 ? -3.092  -61.805 66.503  1.00 63.05  ? 654  ASN A N   1 
ATOM   4864 C CA  . ASN A  1 627 ? -2.344  -63.054 66.607  1.00 62.33  ? 654  ASN A CA  1 
ATOM   4865 C C   . ASN A  1 627 ? -0.870  -62.990 66.167  1.00 64.85  ? 654  ASN A C   1 
ATOM   4866 O O   . ASN A  1 627 ? -0.301  -63.982 65.712  1.00 69.08  ? 654  ASN A O   1 
ATOM   4867 C CB  . ASN A  1 627 ? -3.116  -64.193 65.907  1.00 63.42  ? 654  ASN A CB  1 
ATOM   4868 C CG  . ASN A  1 627 ? -2.847  -64.279 64.398  1.00 66.98  ? 654  ASN A CG  1 
ATOM   4869 O OD1 . ASN A  1 627 ? -2.010  -65.071 63.968  1.00 74.90  ? 654  ASN A OD1 1 
ATOM   4870 N ND2 . ASN A  1 627 ? -3.579  -63.499 63.596  1.00 64.29  ? 654  ASN A ND2 1 
ATOM   4871 N N   . LEU A  1 628 ? -0.240  -61.832 66.340  1.00 58.03  ? 655  LEU A N   1 
ATOM   4872 C CA  . LEU A  1 628 ? 1.146   -61.651 65.907  1.00 54.68  ? 655  LEU A CA  1 
ATOM   4873 C C   . LEU A  1 628 ? 2.096   -61.448 67.083  1.00 54.09  ? 655  LEU A C   1 
ATOM   4874 O O   . LEU A  1 628 ? 1.819   -60.648 67.967  1.00 56.87  ? 655  LEU A O   1 
ATOM   4875 C CB  . LEU A  1 628 ? 1.255   -60.454 64.959  1.00 55.74  ? 655  LEU A CB  1 
ATOM   4876 C CG  . LEU A  1 628 ? 0.784   -60.597 63.510  1.00 51.52  ? 655  LEU A CG  1 
ATOM   4877 C CD1 . LEU A  1 628 ? -0.704  -60.866 63.411  1.00 60.43  ? 655  LEU A CD1 1 
ATOM   4878 C CD2 . LEU A  1 628 ? 1.128   -59.341 62.747  1.00 51.25  ? 655  LEU A CD2 1 
ATOM   4879 N N   . THR A  1 629 ? 3.216   -62.168 67.088  1.00 57.59  ? 656  THR A N   1 
ATOM   4880 C CA  . THR A  1 629 ? 4.233   -61.991 68.124  1.00 57.50  ? 656  THR A CA  1 
ATOM   4881 C C   . THR A  1 629 ? 5.398   -61.180 67.569  1.00 56.44  ? 656  THR A C   1 
ATOM   4882 O O   . THR A  1 629 ? 6.098   -60.477 68.301  1.00 52.43  ? 656  THR A O   1 
ATOM   4883 C CB  . THR A  1 629 ? 4.768   -63.338 68.647  1.00 57.65  ? 656  THR A CB  1 
ATOM   4884 O OG1 . THR A  1 629 ? 5.648   -63.917 67.675  1.00 66.44  ? 656  THR A OG1 1 
ATOM   4885 C CG2 . THR A  1 629 ? 3.617   -64.295 68.938  1.00 48.24  ? 656  THR A CG2 1 
ATOM   4886 N N   . HIS A  1 630 ? 5.600   -61.292 66.263  1.00 54.52  ? 657  HIS A N   1 
ATOM   4887 C CA  . HIS A  1 630 ? 6.603   -60.498 65.578  1.00 58.60  ? 657  HIS A CA  1 
ATOM   4888 C C   . HIS A  1 630 ? 5.931   -59.463 64.692  1.00 63.28  ? 657  HIS A C   1 
ATOM   4889 O O   . HIS A  1 630 ? 4.760   -59.605 64.330  1.00 51.63  ? 657  HIS A O   1 
ATOM   4890 C CB  . HIS A  1 630 ? 7.503   -61.395 64.733  1.00 60.97  ? 657  HIS A CB  1 
ATOM   4891 C CG  . HIS A  1 630 ? 8.466   -62.208 65.539  1.00 77.99  ? 657  HIS A CG  1 
ATOM   4892 N ND1 . HIS A  1 630 ? 9.461   -62.969 64.965  1.00 83.68  ? 657  HIS A ND1 1 
ATOM   4893 C CD2 . HIS A  1 630 ? 8.590   -62.372 66.878  1.00 75.82  ? 657  HIS A CD2 1 
ATOM   4894 C CE1 . HIS A  1 630 ? 10.156  -63.570 65.916  1.00 87.20  ? 657  HIS A CE1 1 
ATOM   4895 N NE2 . HIS A  1 630 ? 9.647   -63.224 67.085  1.00 80.75  ? 657  HIS A NE2 1 
ATOM   4896 N N   . VAL A  1 631 ? 6.672   -58.413 64.357  1.00 63.34  ? 658  VAL A N   1 
ATOM   4897 C CA  . VAL A  1 631 ? 6.199   -57.458 63.369  1.00 58.04  ? 658  VAL A CA  1 
ATOM   4898 C C   . VAL A  1 631 ? 6.434   -58.065 61.995  1.00 60.31  ? 658  VAL A C   1 
ATOM   4899 O O   . VAL A  1 631 ? 7.578   -58.344 61.625  1.00 52.44  ? 658  VAL A O   1 
ATOM   4900 C CB  . VAL A  1 631 ? 6.922   -56.107 63.473  1.00 51.78  ? 658  VAL A CB  1 
ATOM   4901 C CG1 . VAL A  1 631 ? 6.459   -55.178 62.368  1.00 49.86  ? 658  VAL A CG1 1 
ATOM   4902 C CG2 . VAL A  1 631 ? 6.663   -55.478 64.825  1.00 58.38  ? 658  VAL A CG2 1 
ATOM   4903 N N   . PRO A  1 632 ? 5.344   -58.281 61.240  1.00 58.49  ? 659  PRO A N   1 
ATOM   4904 C CA  . PRO A  1 632 ? 5.361   -58.944 59.933  1.00 52.39  ? 659  PRO A CA  1 
ATOM   4905 C C   . PRO A  1 632 ? 6.177   -58.149 58.926  1.00 56.05  ? 659  PRO A C   1 
ATOM   4906 O O   . PRO A  1 632 ? 6.394   -56.955 59.130  1.00 57.22  ? 659  PRO A O   1 
ATOM   4907 C CB  . PRO A  1 632 ? 3.885   -58.950 59.531  1.00 48.61  ? 659  PRO A CB  1 
ATOM   4908 C CG  . PRO A  1 632 ? 3.302   -57.790 60.247  1.00 47.71  ? 659  PRO A CG  1 
ATOM   4909 C CD  . PRO A  1 632 ? 4.009   -57.751 61.566  1.00 51.85  ? 659  PRO A CD  1 
ATOM   4910 N N   . ARG A  1 633 ? 6.629   -58.804 57.860  1.00 59.73  ? 660  ARG A N   1 
ATOM   4911 C CA  . ARG A  1 633 ? 7.461   -58.143 56.858  1.00 70.60  ? 660  ARG A CA  1 
ATOM   4912 C C   . ARG A  1 633 ? 6.716   -56.991 56.187  1.00 65.76  ? 660  ARG A C   1 
ATOM   4913 O O   . ARG A  1 633 ? 5.638   -57.176 55.613  1.00 52.50  ? 660  ARG A O   1 
ATOM   4914 C CB  . ARG A  1 633 ? 7.956   -59.144 55.812  1.00 80.70  ? 660  ARG A CB  1 
ATOM   4915 C CG  . ARG A  1 633 ? 8.845   -60.243 56.371  1.00 85.57  ? 660  ARG A CG  1 
ATOM   4916 C CD  . ARG A  1 633 ? 9.324   -61.181 55.268  1.00 94.25  ? 660  ARG A CD  1 
ATOM   4917 N NE  . ARG A  1 633 ? 10.092  -62.306 55.796  1.00 92.71  ? 660  ARG A NE  1 
ATOM   4918 C CZ  . ARG A  1 633 ? 10.622  -63.268 55.048  1.00 91.33  ? 660  ARG A CZ  1 
ATOM   4919 N NH1 . ARG A  1 633 ? 10.469  -63.247 53.730  1.00 94.96  1 660  ARG A NH1 1 
ATOM   4920 N NH2 . ARG A  1 633 ? 11.305  -64.253 55.616  1.00 96.12  ? 660  ARG A NH2 1 
ATOM   4921 N N   . LEU A  1 634 ? 7.304   -55.802 56.263  1.00 62.84  ? 661  LEU A N   1 
ATOM   4922 C CA  . LEU A  1 634 ? 6.648   -54.598 55.773  1.00 59.31  ? 661  LEU A CA  1 
ATOM   4923 C C   . LEU A  1 634 ? 7.172   -54.142 54.413  1.00 50.25  ? 661  LEU A C   1 
ATOM   4924 O O   . LEU A  1 634 ? 8.384   -54.083 54.196  1.00 46.96  ? 661  LEU A O   1 
ATOM   4925 C CB  . LEU A  1 634 ? 6.775   -53.469 56.800  1.00 54.00  ? 661  LEU A CB  1 
ATOM   4926 C CG  . LEU A  1 634 ? 6.069   -53.694 58.141  1.00 48.45  ? 661  LEU A CG  1 
ATOM   4927 C CD1 . LEU A  1 634 ? 6.181   -52.451 59.003  1.00 49.67  ? 661  LEU A CD1 1 
ATOM   4928 C CD2 . LEU A  1 634 ? 4.608   -54.085 57.949  1.00 41.67  ? 661  LEU A CD2 1 
ATOM   4929 N N   . PRO A  1 635 ? 6.247   -53.819 53.493  1.00 42.82  ? 662  PRO A N   1 
ATOM   4930 C CA  . PRO A  1 635 ? 6.586   -53.293 52.168  1.00 46.07  ? 662  PRO A CA  1 
ATOM   4931 C C   . PRO A  1 635 ? 7.243   -51.926 52.287  1.00 47.84  ? 662  PRO A C   1 
ATOM   4932 O O   . PRO A  1 635 ? 6.805   -51.115 53.100  1.00 53.56  ? 662  PRO A O   1 
ATOM   4933 C CB  . PRO A  1 635 ? 5.220   -53.167 51.485  1.00 50.04  ? 662  PRO A CB  1 
ATOM   4934 C CG  . PRO A  1 635 ? 4.244   -53.050 52.602  1.00 44.48  ? 662  PRO A CG  1 
ATOM   4935 C CD  . PRO A  1 635 ? 4.790   -53.914 53.691  1.00 45.02  ? 662  PRO A CD  1 
ATOM   4936 N N   . ASN A  1 636 ? 8.277   -51.676 51.490  1.00 45.31  ? 663  ASN A N   1 
ATOM   4937 C CA  . ASN A  1 636 ? 9.021   -50.424 51.567  1.00 49.80  ? 663  ASN A CA  1 
ATOM   4938 C C   . ASN A  1 636 ? 8.162   -49.196 51.262  1.00 60.72  ? 663  ASN A C   1 
ATOM   4939 O O   . ASN A  1 636 ? 7.104   -49.301 50.638  1.00 59.86  ? 663  ASN A O   1 
ATOM   4940 C CB  . ASN A  1 636 ? 10.226  -50.465 50.626  1.00 53.67  ? 663  ASN A CB  1 
ATOM   4941 C CG  . ASN A  1 636 ? 11.493  -49.942 51.276  1.00 65.33  ? 663  ASN A CG  1 
ATOM   4942 O OD1 . ASN A  1 636 ? 11.607  -48.752 51.582  1.00 63.54  ? 663  ASN A OD1 1 
ATOM   4943 N ND2 . ASN A  1 636 ? 12.460  -50.832 51.481  1.00 64.02  ? 663  ASN A ND2 1 
ATOM   4944 N N   . LEU A  1 637 ? 8.623   -48.031 51.709  1.00 65.52  ? 664  LEU A N   1 
ATOM   4945 C CA  . LEU A  1 637 ? 7.918   -46.778 51.460  1.00 72.12  ? 664  LEU A CA  1 
ATOM   4946 C C   . LEU A  1 637 ? 8.484   -46.096 50.216  1.00 75.71  ? 664  LEU A C   1 
ATOM   4947 O O   . LEU A  1 637 ? 9.700   -45.940 50.085  1.00 71.03  ? 664  LEU A O   1 
ATOM   4948 C CB  . LEU A  1 637 ? 8.020   -45.852 52.681  1.00 67.01  ? 664  LEU A CB  1 
ATOM   4949 C CG  . LEU A  1 637 ? 7.284   -44.506 52.656  1.00 56.50  ? 664  LEU A CG  1 
ATOM   4950 C CD1 . LEU A  1 637 ? 6.328   -44.370 53.832  1.00 37.56  ? 664  LEU A CD1 1 
ATOM   4951 C CD2 . LEU A  1 637 ? 8.268   -43.346 52.637  1.00 52.15  ? 664  LEU A CD2 1 
ATOM   4952 N N   . HIS A  1 638 ? 7.596   -45.707 49.303  1.00 71.95  ? 665  HIS A N   1 
ATOM   4953 C CA  . HIS A  1 638 ? 7.990   -45.015 48.079  1.00 79.36  ? 665  HIS A CA  1 
ATOM   4954 C C   . HIS A  1 638 ? 8.725   -43.719 48.419  1.00 83.71  ? 665  HIS A C   1 
ATOM   4955 O O   . HIS A  1 638 ? 8.440   -43.091 49.439  1.00 87.97  ? 665  HIS A O   1 
ATOM   4956 C CB  . HIS A  1 638 ? 6.751   -44.708 47.231  1.00 77.66  ? 665  HIS A CB  1 
ATOM   4957 C CG  . HIS A  1 638 ? 7.057   -44.327 45.813  1.00 85.25  ? 665  HIS A CG  1 
ATOM   4958 N ND1 . HIS A  1 638 ? 7.670   -43.140 45.473  1.00 85.40  ? 665  HIS A ND1 1 
ATOM   4959 C CD2 . HIS A  1 638 ? 6.816   -44.970 44.646  1.00 82.11  ? 665  HIS A CD2 1 
ATOM   4960 C CE1 . HIS A  1 638 ? 7.804   -43.072 44.161  1.00 80.58  ? 665  HIS A CE1 1 
ATOM   4961 N NE2 . HIS A  1 638 ? 7.294   -44.172 43.635  1.00 81.19  ? 665  HIS A NE2 1 
ATOM   4962 N N   . LYS A  1 639 ? 9.664   -43.315 47.564  1.00 81.59  ? 666  LYS A N   1 
ATOM   4963 C CA  . LYS A  1 639 ? 10.390  -42.057 47.751  1.00 82.78  ? 666  LYS A CA  1 
ATOM   4964 C C   . LYS A  1 639 ? 9.506   -40.835 47.472  1.00 81.36  ? 666  LYS A C   1 
ATOM   4965 O O   . LYS A  1 639 ? 9.998   -39.711 47.367  1.00 75.35  ? 666  LYS A O   1 
ATOM   4966 C CB  . LYS A  1 639 ? 11.643  -42.015 46.870  1.00 83.61  ? 666  LYS A CB  1 
ATOM   4967 C CG  . LYS A  1 639 ? 12.966  -41.930 47.637  1.00 96.54  ? 666  LYS A CG  1 
ATOM   4968 C CD  . LYS A  1 639 ? 13.267  -43.210 48.411  1.00 90.00  ? 666  LYS A CD  1 
ATOM   4969 C CE  . LYS A  1 639 ? 14.725  -43.268 48.862  1.00 77.60  ? 666  LYS A CE  1 
ATOM   4970 N NZ  . LYS A  1 639 ? 15.102  -42.136 49.758  1.00 71.45  1 666  LYS A NZ  1 
ATOM   4971 N N   . ASN A  1 640 ? 8.203   -41.075 47.345  1.00 76.48  ? 667  ASN A N   1 
ATOM   4972 C CA  . ASN A  1 640 ? 7.204   -40.025 47.202  1.00 70.14  ? 667  ASN A CA  1 
ATOM   4973 C C   . ASN A  1 640 ? 6.375   -39.914 48.474  1.00 74.64  ? 667  ASN A C   1 
ATOM   4974 O O   . ASN A  1 640 ? 5.921   -38.830 48.840  1.00 75.03  ? 667  ASN A O   1 
ATOM   4975 C CB  . ASN A  1 640 ? 6.289   -40.321 46.012  1.00 77.39  ? 667  ASN A CB  1 
ATOM   4976 C CG  . ASN A  1 640 ? 5.028   -39.471 46.012  1.00 84.15  ? 667  ASN A CG  1 
ATOM   4977 O OD1 . ASN A  1 640 ? 4.018   -39.831 46.622  1.00 72.39  ? 667  ASN A OD1 1 
ATOM   4978 N ND2 . ASN A  1 640 ? 5.078   -38.340 45.317  1.00 89.67  ? 667  ASN A ND2 1 
ATOM   4979 N N   . MET A  1 641 ? 6.184   -41.046 49.145  1.00 72.04  ? 668  MET A N   1 
ATOM   4980 C CA  . MET A  1 641 ? 5.375   -41.100 50.358  1.00 58.69  ? 668  MET A CA  1 
ATOM   4981 C C   . MET A  1 641 ? 6.076   -40.406 51.526  1.00 53.00  ? 668  MET A C   1 
ATOM   4982 O O   . MET A  1 641 ? 7.288   -40.190 51.493  1.00 49.30  ? 668  MET A O   1 
ATOM   4983 C CB  . MET A  1 641 ? 5.054   -42.552 50.714  1.00 61.90  ? 668  MET A CB  1 
ATOM   4984 C CG  . MET A  1 641 ? 4.448   -43.363 49.573  1.00 67.93  ? 668  MET A CG  1 
ATOM   4985 S SD  . MET A  1 641 ? 2.686   -43.065 49.307  1.00 66.13  ? 668  MET A SD  1 
ATOM   4986 C CE  . MET A  1 641 ? 2.033   -43.581 50.890  1.00 47.39  ? 668  MET A CE  1 
ATOM   4987 N N   . GLN A  1 642 ? 5.306   -40.060 52.554  1.00 51.98  ? 669  GLN A N   1 
ATOM   4988 C CA  . GLN A  1 642 ? 5.831   -39.307 53.691  1.00 50.21  ? 669  GLN A CA  1 
ATOM   4989 C C   . GLN A  1 642 ? 5.415   -39.882 55.040  1.00 35.11  ? 669  GLN A C   1 
ATOM   4990 O O   . GLN A  1 642 ? 6.052   -39.624 56.056  1.00 39.29  ? 669  GLN A O   1 
ATOM   4991 C CB  . GLN A  1 642 ? 5.377   -37.850 53.615  1.00 47.37  ? 669  GLN A CB  1 
ATOM   4992 C CG  . GLN A  1 642 ? 5.946   -37.071 52.450  1.00 41.87  ? 669  GLN A CG  1 
ATOM   4993 C CD  . GLN A  1 642 ? 5.257   -35.737 52.280  1.00 46.08  ? 669  GLN A CD  1 
ATOM   4994 O OE1 . GLN A  1 642 ? 4.258   -35.452 52.947  1.00 36.86  ? 669  GLN A OE1 1 
ATOM   4995 N NE2 . GLN A  1 642 ? 5.782   -34.908 51.384  1.00 46.43  ? 669  GLN A NE2 1 
ATOM   4996 N N   . LEU A  1 643 ? 4.331   -40.640 55.054  1.00 31.20  ? 670  LEU A N   1 
ATOM   4997 C CA  . LEU A  1 643 ? 3.829   -41.206 56.293  1.00 33.89  ? 670  LEU A CA  1 
ATOM   4998 C C   . LEU A  1 643 ? 3.651   -42.710 56.152  1.00 39.02  ? 670  LEU A C   1 
ATOM   4999 O O   . LEU A  1 643 ? 3.184   -43.194 55.124  1.00 44.42  ? 670  LEU A O   1 
ATOM   5000 C CB  . LEU A  1 643 ? 2.494   -40.563 56.673  1.00 34.22  ? 670  LEU A CB  1 
ATOM   5001 C CG  . LEU A  1 643 ? 2.438   -39.334 57.582  1.00 31.16  ? 670  LEU A CG  1 
ATOM   5002 C CD1 . LEU A  1 643 ? 3.226   -38.177 57.005  1.00 28.10  ? 670  LEU A CD1 1 
ATOM   5003 C CD2 . LEU A  1 643 ? 0.988   -38.939 57.810  1.00 29.09  ? 670  LEU A CD2 1 
ATOM   5004 N N   . MET A  1 644 ? 4.022   -43.446 57.191  1.00 35.71  ? 671  MET A N   1 
ATOM   5005 C CA  . MET A  1 644 ? 3.835   -44.887 57.203  1.00 30.59  ? 671  MET A CA  1 
ATOM   5006 C C   . MET A  1 644 ? 3.254   -45.295 58.542  1.00 29.20  ? 671  MET A C   1 
ATOM   5007 O O   . MET A  1 644 ? 3.937   -45.214 59.556  1.00 42.89  ? 671  MET A O   1 
ATOM   5008 C CB  . MET A  1 644 ? 5.170   -45.589 56.978  1.00 30.82  ? 671  MET A CB  1 
ATOM   5009 C CG  . MET A  1 644 ? 5.062   -47.093 56.860  1.00 30.11  ? 671  MET A CG  1 
ATOM   5010 S SD  . MET A  1 644 ? 6.550   -47.834 56.164  1.00 27.57  ? 671  MET A SD  1 
ATOM   5011 C CE  . MET A  1 644 ? 6.042   -49.547 56.065  1.00 28.70  ? 671  MET A CE  1 
ATOM   5012 N N   . GLU A  1 645 ? 1.999   -45.728 58.555  1.00 21.96  ? 672  GLU A N   1 
ATOM   5013 C CA  . GLU A  1 645 ? 1.323   -45.999 59.821  1.00 25.12  ? 672  GLU A CA  1 
ATOM   5014 C C   . GLU A  1 645 ? 1.184   -47.477 60.155  1.00 26.99  ? 672  GLU A C   1 
ATOM   5015 O O   . GLU A  1 645 ? 0.164   -48.093 59.858  1.00 27.60  ? 672  GLU A O   1 
ATOM   5016 C CB  . GLU A  1 645 ? -0.059  -45.351 59.845  1.00 28.38  ? 672  GLU A CB  1 
ATOM   5017 C CG  . GLU A  1 645 ? -0.048  -43.841 59.764  1.00 28.57  ? 672  GLU A CG  1 
ATOM   5018 C CD  . GLU A  1 645 ? -1.448  -43.269 59.735  1.00 30.58  ? 672  GLU A CD  1 
ATOM   5019 O OE1 . GLU A  1 645 ? -1.598  -42.092 59.343  1.00 38.12  ? 672  GLU A OE1 1 
ATOM   5020 O OE2 . GLU A  1 645 ? -2.397  -43.999 60.100  1.00 21.62  1 672  GLU A OE2 1 
ATOM   5021 N N   . LEU A  1 646 ? 2.200   -48.035 60.803  1.00 30.93  ? 673  LEU A N   1 
ATOM   5022 C CA  . LEU A  1 646 ? 2.156   -49.424 61.242  1.00 31.15  ? 673  LEU A CA  1 
ATOM   5023 C C   . LEU A  1 646 ? 1.162   -49.614 62.390  1.00 31.74  ? 673  LEU A C   1 
ATOM   5024 O O   . LEU A  1 646 ? 1.486   -49.380 63.552  1.00 34.03  ? 673  LEU A O   1 
ATOM   5025 C CB  . LEU A  1 646 ? 3.550   -49.899 61.654  1.00 28.21  ? 673  LEU A CB  1 
ATOM   5026 C CG  . LEU A  1 646 ? 3.647   -51.367 62.065  1.00 32.37  ? 673  LEU A CG  1 
ATOM   5027 C CD1 . LEU A  1 646 ? 3.105   -52.260 60.969  1.00 36.05  ? 673  LEU A CD1 1 
ATOM   5028 C CD2 . LEU A  1 646 ? 5.079   -51.739 62.397  1.00 35.77  ? 673  LEU A CD2 1 
ATOM   5029 N N   . HIS A  1 647 ? -0.053  -50.031 62.054  1.00 31.45  ? 674  HIS A N   1 
ATOM   5030 C CA  . HIS A  1 647 ? -1.097  -50.236 63.049  1.00 31.97  ? 674  HIS A CA  1 
ATOM   5031 C C   . HIS A  1 647 ? -1.146  -51.688 63.498  1.00 36.02  ? 674  HIS A C   1 
ATOM   5032 O O   . HIS A  1 647 ? -1.671  -52.545 62.789  1.00 36.71  ? 674  HIS A O   1 
ATOM   5033 C CB  . HIS A  1 647 ? -2.458  -49.823 62.487  1.00 34.69  ? 674  HIS A CB  1 
ATOM   5034 C CG  . HIS A  1 647 ? -2.696  -48.345 62.496  1.00 35.60  ? 674  HIS A CG  1 
ATOM   5035 N ND1 . HIS A  1 647 ? -3.575  -47.739 63.370  1.00 31.18  ? 674  HIS A ND1 1 
ATOM   5036 C CD2 . HIS A  1 647 ? -2.174  -47.353 61.736  1.00 28.26  ? 674  HIS A CD2 1 
ATOM   5037 C CE1 . HIS A  1 647 ? -3.580  -46.436 63.150  1.00 29.30  ? 674  HIS A CE1 1 
ATOM   5038 N NE2 . HIS A  1 647 ? -2.741  -46.177 62.163  1.00 28.65  ? 674  HIS A NE2 1 
ATOM   5039 N N   . LEU A  1 648 ? -0.606  -51.956 64.685  1.00 41.96  ? 675  LEU A N   1 
ATOM   5040 C CA  . LEU A  1 648 ? -0.555  -53.314 65.227  1.00 42.06  ? 675  LEU A CA  1 
ATOM   5041 C C   . LEU A  1 648 ? -1.376  -53.457 66.509  1.00 35.21  ? 675  LEU A C   1 
ATOM   5042 O O   . LEU A  1 648 ? -1.001  -54.199 67.415  1.00 30.46  ? 675  LEU A O   1 
ATOM   5043 C CB  . LEU A  1 648 ? 0.896   -53.726 65.487  1.00 34.49  ? 675  LEU A CB  1 
ATOM   5044 C CG  . LEU A  1 648 ? 1.834   -53.668 64.279  1.00 32.78  ? 675  LEU A CG  1 
ATOM   5045 C CD1 . LEU A  1 648 ? 3.245   -54.036 64.682  1.00 38.79  ? 675  LEU A CD1 1 
ATOM   5046 C CD2 . LEU A  1 648 ? 1.344   -54.586 63.173  1.00 40.24  ? 675  LEU A CD2 1 
ATOM   5047 N N   . GLU A  1 649 ? -2.503  -52.752 66.568  1.00 39.31  ? 676  GLU A N   1 
ATOM   5048 C CA  . GLU A  1 649 ? -3.318  -52.690 67.780  1.00 38.79  ? 676  GLU A CA  1 
ATOM   5049 C C   . GLU A  1 649 ? -3.893  -54.042 68.200  1.00 37.52  ? 676  GLU A C   1 
ATOM   5050 O O   . GLU A  1 649 ? -4.154  -54.908 67.365  1.00 39.25  ? 676  GLU A O   1 
ATOM   5051 C CB  . GLU A  1 649 ? -4.453  -51.668 67.626  1.00 36.66  ? 676  GLU A CB  1 
ATOM   5052 C CG  . GLU A  1 649 ? -4.003  -50.233 67.368  1.00 33.30  ? 676  GLU A CG  1 
ATOM   5053 C CD  . GLU A  1 649 ? -3.881  -49.914 65.887  1.00 40.83  ? 676  GLU A CD  1 
ATOM   5054 O OE1 . GLU A  1 649 ? -4.326  -48.821 65.465  1.00 38.48  ? 676  GLU A OE1 1 
ATOM   5055 O OE2 . GLU A  1 649 ? -3.341  -50.760 65.143  1.00 41.58  1 676  GLU A OE2 1 
ATOM   5056 N N   . ASN A  1 650 ? -4.079  -54.200 69.508  1.00 36.43  ? 677  ASN A N   1 
ATOM   5057 C CA  . ASN A  1 650 ? -4.702  -55.385 70.095  1.00 37.69  ? 677  ASN A CA  1 
ATOM   5058 C C   . ASN A  1 650 ? -4.174  -56.727 69.585  1.00 38.71  ? 677  ASN A C   1 
ATOM   5059 O O   . ASN A  1 650 ? -4.944  -57.601 69.192  1.00 41.04  ? 677  ASN A O   1 
ATOM   5060 C CB  . ASN A  1 650 ? -6.227  -55.308 69.971  1.00 37.16  ? 677  ASN A CB  1 
ATOM   5061 C CG  . ASN A  1 650 ? -6.826  -54.201 70.826  1.00 36.09  ? 677  ASN A CG  1 
ATOM   5062 O OD1 . ASN A  1 650 ? -6.140  -53.249 71.204  1.00 33.33  ? 677  ASN A OD1 1 
ATOM   5063 N ND2 . ASN A  1 650 ? -8.110  -54.327 71.141  1.00 31.10  ? 677  ASN A ND2 1 
ATOM   5064 N N   . ASN A  1 651 ? -2.853  -56.873 69.586  1.00 43.20  ? 678  ASN A N   1 
ATOM   5065 C CA  . ASN A  1 651 ? -2.216  -58.147 69.273  1.00 46.45  ? 678  ASN A CA  1 
ATOM   5066 C C   . ASN A  1 651 ? -1.528  -58.696 70.506  1.00 42.97  ? 678  ASN A C   1 
ATOM   5067 O O   . ASN A  1 651 ? -1.874  -58.349 71.634  1.00 41.48  ? 678  ASN A O   1 
ATOM   5068 C CB  . ASN A  1 651 ? -1.169  -57.997 68.164  1.00 44.23  ? 678  ASN A CB  1 
ATOM   5069 C CG  . ASN A  1 651 ? -1.762  -57.550 66.850  1.00 48.09  ? 678  ASN A CG  1 
ATOM   5070 O OD1 . ASN A  1 651 ? -2.863  -57.955 66.478  1.00 54.34  ? 678  ASN A OD1 1 
ATOM   5071 N ND2 . ASN A  1 651 ? -1.029  -56.706 66.133  1.00 44.56  ? 678  ASN A ND2 1 
ATOM   5072 N N   . THR A  1 652 ? -0.541  -59.553 70.271  1.00 44.66  ? 679  THR A N   1 
ATOM   5073 C CA  . THR A  1 652 ? 0.298   -60.093 71.328  1.00 41.94  ? 679  THR A CA  1 
ATOM   5074 C C   . THR A  1 652 ? 1.735   -60.145 70.841  1.00 41.80  ? 679  THR A C   1 
ATOM   5075 O O   . THR A  1 652 ? 2.339   -61.216 70.800  1.00 42.33  ? 679  THR A O   1 
ATOM   5076 C CB  . THR A  1 652 ? -0.123  -61.519 71.723  1.00 42.65  ? 679  THR A CB  1 
ATOM   5077 O OG1 . THR A  1 652 ? -0.188  -62.338 70.548  1.00 39.98  ? 679  THR A OG1 1 
ATOM   5078 C CG2 . THR A  1 652 ? -1.479  -61.517 72.421  1.00 42.30  ? 679  THR A CG2 1 
ATOM   5079 N N   . LEU A  1 653 ? 2.276   -58.992 70.452  1.00 42.00  ? 680  LEU A N   1 
ATOM   5080 C CA  . LEU A  1 653 ? 3.673   -58.900 70.032  1.00 43.28  ? 680  LEU A CA  1 
ATOM   5081 C C   . LEU A  1 653 ? 4.582   -59.305 71.179  1.00 47.59  ? 680  LEU A C   1 
ATOM   5082 O O   . LEU A  1 653 ? 4.115   -59.572 72.277  1.00 48.38  ? 680  LEU A O   1 
ATOM   5083 C CB  . LEU A  1 653 ? 4.022   -57.478 69.596  1.00 43.14  ? 680  LEU A CB  1 
ATOM   5084 C CG  . LEU A  1 653 ? 4.035   -57.161 68.103  1.00 43.10  ? 680  LEU A CG  1 
ATOM   5085 C CD1 . LEU A  1 653 ? 2.628   -57.155 67.542  1.00 43.38  ? 680  LEU A CD1 1 
ATOM   5086 C CD2 . LEU A  1 653 ? 4.722   -55.829 67.866  1.00 40.64  ? 680  LEU A CD2 1 
ATOM   5087 N N   . LEU A  1 654 ? 5.882   -59.357 70.930  1.00 45.01  ? 681  LEU A N   1 
ATOM   5088 C CA  . LEU A  1 654 ? 6.816   -59.662 72.004  1.00 41.95  ? 681  LEU A CA  1 
ATOM   5089 C C   . LEU A  1 654 ? 7.959   -58.668 71.999  1.00 41.42  ? 681  LEU A C   1 
ATOM   5090 O O   . LEU A  1 654 ? 8.164   -57.934 72.966  1.00 49.14  ? 681  LEU A O   1 
ATOM   5091 C CB  . LEU A  1 654 ? 7.336   -61.097 71.894  1.00 44.34  ? 681  LEU A CB  1 
ATOM   5092 C CG  . LEU A  1 654 ? 6.332   -62.221 72.180  1.00 40.70  ? 681  LEU A CG  1 
ATOM   5093 C CD1 . LEU A  1 654 ? 7.006   -63.575 72.041  1.00 40.84  ? 681  LEU A CD1 1 
ATOM   5094 C CD2 . LEU A  1 654 ? 5.692   -62.077 73.557  1.00 32.02  ? 681  LEU A CD2 1 
ATOM   5095 N N   . ARG A  1 655 ? 8.698   -58.639 70.900  1.00 32.52  ? 682  ARG A N   1 
ATOM   5096 C CA  . ARG A  1 655 ? 9.790   -57.698 70.760  1.00 34.37  ? 682  ARG A CA  1 
ATOM   5097 C C   . ARG A  1 655 ? 9.622   -56.925 69.463  1.00 39.18  ? 682  ARG A C   1 
ATOM   5098 O O   . ARG A  1 655 ? 8.902   -57.351 68.561  1.00 44.62  ? 682  ARG A O   1 
ATOM   5099 C CB  . ARG A  1 655 ? 11.130  -58.432 70.780  1.00 38.38  ? 682  ARG A CB  1 
ATOM   5100 C CG  . ARG A  1 655 ? 12.286  -57.586 71.286  1.00 51.79  ? 682  ARG A CG  1 
ATOM   5101 C CD  . ARG A  1 655 ? 13.578  -58.390 71.387  1.00 67.11  ? 682  ARG A CD  1 
ATOM   5102 N NE  . ARG A  1 655 ? 13.435  -59.590 72.209  1.00 74.35  ? 682  ARG A NE  1 
ATOM   5103 C CZ  . ARG A  1 655 ? 13.519  -59.605 73.537  1.00 73.94  ? 682  ARG A CZ  1 
ATOM   5104 N NH1 . ARG A  1 655 ? 13.736  -58.479 74.204  1.00 71.16  1 682  ARG A NH1 1 
ATOM   5105 N NH2 . ARG A  1 655 ? 13.378  -60.747 74.200  1.00 65.24  ? 682  ARG A NH2 1 
ATOM   5106 N N   . LEU A  1 656 ? 10.279  -55.778 69.376  1.00 41.64  ? 683  LEU A N   1 
ATOM   5107 C CA  . LEU A  1 656 ? 10.266  -54.999 68.151  1.00 45.29  ? 683  LEU A CA  1 
ATOM   5108 C C   . LEU A  1 656 ? 11.539  -55.246 67.349  1.00 47.53  ? 683  LEU A C   1 
ATOM   5109 O O   . LEU A  1 656 ? 12.607  -55.473 67.920  1.00 47.59  ? 683  LEU A O   1 
ATOM   5110 C CB  . LEU A  1 656 ? 10.112  -53.512 68.469  1.00 44.71  ? 683  LEU A CB  1 
ATOM   5111 C CG  . LEU A  1 656 ? 8.722   -53.114 68.964  1.00 48.14  ? 683  LEU A CG  1 
ATOM   5112 C CD1 . LEU A  1 656 ? 8.722   -51.677 69.452  1.00 48.34  ? 683  LEU A CD1 1 
ATOM   5113 C CD2 . LEU A  1 656 ? 7.686   -53.313 67.859  1.00 44.93  ? 683  LEU A CD2 1 
ATOM   5114 N N   . PRO A  1 657 ? 11.424  -55.220 66.015  1.00 45.24  ? 684  PRO A N   1 
ATOM   5115 C CA  . PRO A  1 657 ? 12.591  -55.350 65.136  1.00 49.01  ? 684  PRO A CA  1 
ATOM   5116 C C   . PRO A  1 657 ? 13.501  -54.129 65.224  1.00 45.18  ? 684  PRO A C   1 
ATOM   5117 O O   . PRO A  1 657 ? 13.142  -53.142 65.860  1.00 46.82  ? 684  PRO A O   1 
ATOM   5118 C CB  . PRO A  1 657 ? 11.969  -55.457 63.740  1.00 54.75  ? 684  PRO A CB  1 
ATOM   5119 C CG  . PRO A  1 657 ? 10.619  -54.839 63.871  1.00 53.47  ? 684  PRO A CG  1 
ATOM   5120 C CD  . PRO A  1 657 ? 10.164  -55.159 65.258  1.00 48.91  ? 684  PRO A CD  1 
ATOM   5121 N N   . SER A  1 658 ? 14.666  -54.197 64.589  1.00 45.12  ? 685  SER A N   1 
ATOM   5122 C CA  . SER A  1 658 ? 15.630  -53.105 64.656  1.00 44.65  ? 685  SER A CA  1 
ATOM   5123 C C   . SER A  1 658 ? 15.150  -51.900 63.863  1.00 48.41  ? 685  SER A C   1 
ATOM   5124 O O   . SER A  1 658 ? 14.124  -51.954 63.187  1.00 53.45  ? 685  SER A O   1 
ATOM   5125 C CB  . SER A  1 658 ? 16.988  -53.554 64.120  1.00 48.08  ? 685  SER A CB  1 
ATOM   5126 O OG  . SER A  1 658 ? 16.945  -53.729 62.715  1.00 48.63  ? 685  SER A OG  1 
ATOM   5127 N N   . ALA A  1 659 ? 15.906  -50.812 63.944  1.00 44.91  ? 686  ALA A N   1 
ATOM   5128 C CA  . ALA A  1 659 ? 15.589  -49.611 63.189  1.00 45.43  ? 686  ALA A CA  1 
ATOM   5129 C C   . ALA A  1 659 ? 15.990  -49.785 61.733  1.00 48.68  ? 686  ALA A C   1 
ATOM   5130 O O   . ALA A  1 659 ? 15.527  -49.051 60.860  1.00 47.31  ? 686  ALA A O   1 
ATOM   5131 C CB  . ALA A  1 659 ? 16.298  -48.413 63.787  1.00 52.74  ? 686  ALA A CB  1 
ATOM   5132 N N   . ASN A  1 660 ? 16.857  -50.763 61.481  1.00 48.92  ? 687  ASN A N   1 
ATOM   5133 C CA  . ASN A  1 660 ? 17.389  -51.000 60.144  1.00 46.59  ? 687  ASN A CA  1 
ATOM   5134 C C   . ASN A  1 660 ? 16.579  -52.009 59.347  1.00 46.29  ? 687  ASN A C   1 
ATOM   5135 O O   . ASN A  1 660 ? 16.926  -52.336 58.214  1.00 47.65  ? 687  ASN A O   1 
ATOM   5136 C CB  . ASN A  1 660 ? 18.852  -51.439 60.215  1.00 52.65  ? 687  ASN A CB  1 
ATOM   5137 C CG  . ASN A  1 660 ? 19.805  -50.353 59.763  1.00 53.70  ? 687  ASN A CG  1 
ATOM   5138 O OD1 . ASN A  1 660 ? 20.706  -49.950 60.502  1.00 47.30  ? 687  ASN A OD1 1 
ATOM   5139 N ND2 . ASN A  1 660 ? 19.609  -49.869 58.542  1.00 48.83  ? 687  ASN A ND2 1 
ATOM   5140 N N   . THR A  1 661 ? 15.502  -52.505 59.947  1.00 47.99  ? 688  THR A N   1 
ATOM   5141 C CA  . THR A  1 661 ? 14.591  -53.399 59.248  1.00 48.98  ? 688  THR A CA  1 
ATOM   5142 C C   . THR A  1 661 ? 13.931  -52.650 58.098  1.00 51.27  ? 688  THR A C   1 
ATOM   5143 O O   . THR A  1 661 ? 13.219  -51.672 58.320  1.00 52.24  ? 688  THR A O   1 
ATOM   5144 C CB  . THR A  1 661 ? 13.501  -53.944 60.185  1.00 48.79  ? 688  THR A CB  1 
ATOM   5145 O OG1 . THR A  1 661 ? 14.109  -54.647 61.277  1.00 48.51  ? 688  THR A OG1 1 
ATOM   5146 C CG2 . THR A  1 661 ? 12.575  -54.886 59.430  1.00 46.81  ? 688  THR A CG2 1 
ATOM   5147 N N   . PRO A  1 662 ? 14.178  -53.103 56.860  1.00 49.56  ? 689  PRO A N   1 
ATOM   5148 C CA  . PRO A  1 662 ? 13.647  -52.454 55.656  1.00 50.09  ? 689  PRO A CA  1 
ATOM   5149 C C   . PRO A  1 662 ? 12.125  -52.471 55.642  1.00 49.69  ? 689  PRO A C   1 
ATOM   5150 O O   . PRO A  1 662 ? 11.510  -53.418 56.135  1.00 48.92  ? 689  PRO A O   1 
ATOM   5151 C CB  . PRO A  1 662 ? 14.194  -53.322 54.522  1.00 56.28  ? 689  PRO A CB  1 
ATOM   5152 C CG  . PRO A  1 662 ? 15.377  -54.021 55.114  1.00 55.82  ? 689  PRO A CG  1 
ATOM   5153 C CD  . PRO A  1 662 ? 15.000  -54.277 56.533  1.00 47.59  ? 689  PRO A CD  1 
ATOM   5154 N N   . GLY A  1 663 ? 11.528  -51.427 55.079  1.00 50.27  ? 690  GLY A N   1 
ATOM   5155 C CA  . GLY A  1 663 ? 10.093  -51.240 55.163  1.00 50.43  ? 690  GLY A CA  1 
ATOM   5156 C C   . GLY A  1 663 ? 9.761   -50.619 56.505  1.00 51.30  ? 690  GLY A C   1 
ATOM   5157 O O   . GLY A  1 663 ? 9.288   -49.485 56.582  1.00 52.85  ? 690  GLY A O   1 
ATOM   5158 N N   . TYR A  1 664 ? 10.034  -51.374 57.564  1.00 50.59  ? 691  TYR A N   1 
ATOM   5159 C CA  . TYR A  1 664 ? 9.874   -50.920 58.942  1.00 48.83  ? 691  TYR A CA  1 
ATOM   5160 C C   . TYR A  1 664 ? 10.666  -49.634 59.215  1.00 45.06  ? 691  TYR A C   1 
ATOM   5161 O O   . TYR A  1 664 ? 10.216  -48.769 59.965  1.00 40.23  ? 691  TYR A O   1 
ATOM   5162 C CB  . TYR A  1 664 ? 10.312  -52.050 59.887  1.00 53.29  ? 691  TYR A CB  1 
ATOM   5163 C CG  . TYR A  1 664 ? 10.194  -51.769 61.372  1.00 51.73  ? 691  TYR A CG  1 
ATOM   5164 C CD1 . TYR A  1 664 ? 9.010   -52.021 62.055  1.00 45.31  ? 691  TYR A CD1 1 
ATOM   5165 C CD2 . TYR A  1 664 ? 11.280  -51.288 62.097  1.00 48.58  ? 691  TYR A CD2 1 
ATOM   5166 C CE1 . TYR A  1 664 ? 8.903   -51.779 63.414  1.00 46.26  ? 691  TYR A CE1 1 
ATOM   5167 C CE2 . TYR A  1 664 ? 11.182  -51.041 63.453  1.00 47.61  ? 691  TYR A CE2 1 
ATOM   5168 C CZ  . TYR A  1 664 ? 9.993   -51.289 64.107  1.00 52.68  ? 691  TYR A CZ  1 
ATOM   5169 O OH  . TYR A  1 664 ? 9.898   -51.045 65.459  1.00 52.21  ? 691  TYR A OH  1 
ATOM   5170 N N   . GLU A  1 665 ? 11.832  -49.507 58.584  1.00 45.85  ? 692  GLU A N   1 
ATOM   5171 C CA  . GLU A  1 665 ? 12.739  -48.382 58.825  1.00 47.93  ? 692  GLU A CA  1 
ATOM   5172 C C   . GLU A  1 665 ? 12.186  -47.023 58.393  1.00 53.47  ? 692  GLU A C   1 
ATOM   5173 O O   . GLU A  1 665 ? 12.743  -45.981 58.751  1.00 48.41  ? 692  GLU A O   1 
ATOM   5174 C CB  . GLU A  1 665 ? 14.078  -48.620 58.122  1.00 45.29  ? 692  GLU A CB  1 
ATOM   5175 C CG  . GLU A  1 665 ? 13.968  -48.741 56.612  1.00 49.50  ? 692  GLU A CG  1 
ATOM   5176 C CD  . GLU A  1 665 ? 15.318  -48.769 55.932  1.00 47.27  ? 692  GLU A CD  1 
ATOM   5177 O OE1 . GLU A  1 665 ? 16.342  -48.692 56.643  1.00 48.04  ? 692  GLU A OE1 1 
ATOM   5178 O OE2 . GLU A  1 665 ? 15.356  -48.866 54.688  1.00 46.59  1 692  GLU A OE2 1 
ATOM   5179 N N   . SER A  1 666 ? 11.103  -47.034 57.620  1.00 54.01  ? 693  SER A N   1 
ATOM   5180 C CA  . SER A  1 666 ? 10.540  -45.801 57.074  1.00 50.57  ? 693  SER A CA  1 
ATOM   5181 C C   . SER A  1 666 ? 9.254   -45.390 57.782  1.00 42.13  ? 693  SER A C   1 
ATOM   5182 O O   . SER A  1 666 ? 8.601   -44.426 57.387  1.00 37.99  ? 693  SER A O   1 
ATOM   5183 C CB  . SER A  1 666 ? 10.289  -45.955 55.575  1.00 48.43  ? 693  SER A CB  1 
ATOM   5184 O OG  . SER A  1 666 ? 11.485  -46.306 54.899  1.00 54.65  ? 693  SER A OG  1 
ATOM   5185 N N   . VAL A  1 667 ? 8.908   -46.128 58.833  1.00 45.06  ? 694  VAL A N   1 
ATOM   5186 C CA  . VAL A  1 667 ? 7.699   -45.877 59.615  1.00 40.32  ? 694  VAL A CA  1 
ATOM   5187 C C   . VAL A  1 667 ? 7.737   -44.520 60.317  1.00 38.84  ? 694  VAL A C   1 
ATOM   5188 O O   . VAL A  1 667 ? 8.762   -44.128 60.875  1.00 39.34  ? 694  VAL A O   1 
ATOM   5189 C CB  . VAL A  1 667 ? 7.471   -46.996 60.670  1.00 33.65  ? 694  VAL A CB  1 
ATOM   5190 C CG1 . VAL A  1 667 ? 6.475   -46.558 61.726  1.00 31.97  ? 694  VAL A CG1 1 
ATOM   5191 C CG2 . VAL A  1 667 ? 7.004   -48.278 60.006  1.00 32.02  ? 694  VAL A CG2 1 
ATOM   5192 N N   . THR A  1 668 ? 6.618   -43.802 60.271  1.00 34.85  ? 695  THR A N   1 
ATOM   5193 C CA  . THR A  1 668 ? 6.473   -42.571 61.031  1.00 33.55  ? 695  THR A CA  1 
ATOM   5194 C C   . THR A  1 668 ? 5.585   -42.794 62.249  1.00 31.68  ? 695  THR A C   1 
ATOM   5195 O O   . THR A  1 668 ? 5.758   -42.150 63.282  1.00 36.03  ? 695  THR A O   1 
ATOM   5196 C CB  . THR A  1 668 ? 5.866   -41.446 60.181  1.00 30.17  ? 695  THR A CB  1 
ATOM   5197 O OG1 . THR A  1 668 ? 4.625   -41.891 59.625  1.00 31.73  ? 695  THR A OG1 1 
ATOM   5198 C CG2 . THR A  1 668 ? 6.807   -41.057 59.063  1.00 27.49  ? 695  THR A CG2 1 
ATOM   5199 N N   . SER A  1 669 ? 4.636   -43.711 62.133  1.00 25.13  ? 696  SER A N   1 
ATOM   5200 C CA  . SER A  1 669 ? 3.676   -43.923 63.207  1.00 28.24  ? 696  SER A CA  1 
ATOM   5201 C C   . SER A  1 669 ? 3.591   -45.389 63.638  1.00 32.44  ? 696  SER A C   1 
ATOM   5202 O O   . SER A  1 669 ? 3.542   -46.293 62.804  1.00 32.72  ? 696  SER A O   1 
ATOM   5203 C CB  . SER A  1 669 ? 2.304   -43.393 62.796  1.00 29.86  ? 696  SER A CB  1 
ATOM   5204 O OG  . SER A  1 669 ? 1.414   -43.401 63.893  1.00 24.13  ? 696  SER A OG  1 
ATOM   5205 N N   . LEU A  1 670 ? 3.559   -45.613 64.949  1.00 32.57  ? 697  LEU A N   1 
ATOM   5206 C CA  . LEU A  1 670 ? 3.695   -46.955 65.510  1.00 29.14  ? 697  LEU A CA  1 
ATOM   5207 C C   . LEU A  1 670 ? 2.620   -47.225 66.560  1.00 26.53  ? 697  LEU A C   1 
ATOM   5208 O O   . LEU A  1 670 ? 2.812   -46.943 67.742  1.00 25.48  ? 697  LEU A O   1 
ATOM   5209 C CB  . LEU A  1 670 ? 5.084   -47.102 66.132  1.00 28.25  ? 697  LEU A CB  1 
ATOM   5210 C CG  . LEU A  1 670 ? 5.714   -48.491 66.185  1.00 30.07  ? 697  LEU A CG  1 
ATOM   5211 C CD1 . LEU A  1 670 ? 5.951   -49.014 64.779  1.00 30.16  ? 697  LEU A CD1 1 
ATOM   5212 C CD2 . LEU A  1 670 ? 7.015   -48.448 66.976  1.00 28.01  ? 697  LEU A CD2 1 
ATOM   5213 N N   . HIS A  1 671 ? 1.496   -47.787 66.125  1.00 28.45  ? 698  HIS A N   1 
ATOM   5214 C CA  . HIS A  1 671 ? 0.320   -47.935 66.980  1.00 29.26  ? 698  HIS A CA  1 
ATOM   5215 C C   . HIS A  1 671 ? 0.196   -49.333 67.555  1.00 35.45  ? 698  HIS A C   1 
ATOM   5216 O O   . HIS A  1 671 ? -0.552  -50.159 67.030  1.00 34.19  ? 698  HIS A O   1 
ATOM   5217 C CB  . HIS A  1 671 ? -0.927  -47.603 66.179  1.00 27.75  ? 698  HIS A CB  1 
ATOM   5218 C CG  . HIS A  1 671 ? -0.809  -46.331 65.408  1.00 32.57  ? 698  HIS A CG  1 
ATOM   5219 N ND1 . HIS A  1 671 ? -1.437  -45.167 65.798  1.00 35.28  ? 698  HIS A ND1 1 
ATOM   5220 C CD2 . HIS A  1 671 ? -0.114  -46.027 64.287  1.00 29.89  ? 698  HIS A CD2 1 
ATOM   5221 C CE1 . HIS A  1 671 ? -1.147  -44.207 64.939  1.00 34.29  ? 698  HIS A CE1 1 
ATOM   5222 N NE2 . HIS A  1 671 ? -0.343  -44.702 64.014  1.00 29.62  ? 698  HIS A NE2 1 
ATOM   5223 N N   . LEU A  1 672 ? 0.911   -49.580 68.649  1.00 36.93  ? 699  LEU A N   1 
ATOM   5224 C CA  . LEU A  1 672 ? 1.081   -50.933 69.168  1.00 31.34  ? 699  LEU A CA  1 
ATOM   5225 C C   . LEU A  1 672 ? 0.234   -51.216 70.404  1.00 27.08  ? 699  LEU A C   1 
ATOM   5226 O O   . LEU A  1 672 ? 0.451   -52.213 71.085  1.00 30.13  ? 699  LEU A O   1 
ATOM   5227 C CB  . LEU A  1 672 ? 2.557   -51.184 69.485  1.00 27.89  ? 699  LEU A CB  1 
ATOM   5228 C CG  . LEU A  1 672 ? 3.579   -50.624 68.491  1.00 29.50  ? 699  LEU A CG  1 
ATOM   5229 C CD1 . LEU A  1 672 ? 4.995   -50.919 68.959  1.00 36.90  ? 699  LEU A CD1 1 
ATOM   5230 C CD2 . LEU A  1 672 ? 3.359   -51.172 67.090  1.00 29.20  ? 699  LEU A CD2 1 
ATOM   5231 N N   . ALA A  1 673 ? -0.728  -50.345 70.684  1.00 24.03  ? 700  ALA A N   1 
ATOM   5232 C CA  . ALA A  1 673 ? -1.580  -50.488 71.861  1.00 27.28  ? 700  ALA A CA  1 
ATOM   5233 C C   . ALA A  1 673 ? -2.187  -51.882 71.992  1.00 31.60  ? 700  ALA A C   1 
ATOM   5234 O O   . ALA A  1 673 ? -2.459  -52.545 70.996  1.00 36.13  ? 700  ALA A O   1 
ATOM   5235 C CB  . ALA A  1 673 ? -2.676  -49.444 71.843  1.00 34.34  ? 700  ALA A CB  1 
ATOM   5236 N N   . GLY A  1 674 ? -2.388  -52.320 73.230  1.00 35.94  ? 701  GLY A N   1 
ATOM   5237 C CA  . GLY A  1 674 ? -2.968  -53.625 73.495  1.00 39.30  ? 701  GLY A CA  1 
ATOM   5238 C C   . GLY A  1 674 ? -2.071  -54.777 73.079  1.00 39.64  ? 701  GLY A C   1 
ATOM   5239 O O   . GLY A  1 674 ? -2.537  -55.760 72.502  1.00 38.98  ? 701  GLY A O   1 
ATOM   5240 N N   . ASN A  1 675 ? -0.781  -54.660 73.376  1.00 34.53  ? 702  ASN A N   1 
ATOM   5241 C CA  . ASN A  1 675 ? 0.171   -55.706 73.027  1.00 37.32  ? 702  ASN A CA  1 
ATOM   5242 C C   . ASN A  1 675 ? 1.001   -56.201 74.205  1.00 45.27  ? 702  ASN A C   1 
ATOM   5243 O O   . ASN A  1 675 ? 0.728   -55.860 75.356  1.00 45.18  ? 702  ASN A O   1 
ATOM   5244 C CB  . ASN A  1 675 ? 1.092   -55.239 71.905  1.00 37.84  ? 702  ASN A CB  1 
ATOM   5245 C CG  . ASN A  1 675 ? 0.666   -55.758 70.557  1.00 37.32  ? 702  ASN A CG  1 
ATOM   5246 O OD1 . ASN A  1 675 ? 0.936   -56.907 70.211  1.00 34.82  ? 702  ASN A OD1 1 
ATOM   5247 N ND2 . ASN A  1 675 ? -0.003  -54.915 69.783  1.00 41.79  ? 702  ASN A ND2 1 
ATOM   5248 N N   . ASN A  1 676 ? 2.004   -57.025 73.902  1.00 47.20  ? 703  ASN A N   1 
ATOM   5249 C CA  . ASN A  1 676 ? 2.930   -57.533 74.905  1.00 43.55  ? 703  ASN A CA  1 
ATOM   5250 C C   . ASN A  1 676 ? 4.358   -57.090 74.615  1.00 51.80  ? 703  ASN A C   1 
ATOM   5251 O O   . ASN A  1 676 ? 5.159   -57.875 74.109  1.00 54.98  ? 703  ASN A O   1 
ATOM   5252 C CB  . ASN A  1 676 ? 2.938   -59.062 74.937  1.00 42.55  ? 703  ASN A CB  1 
ATOM   5253 C CG  . ASN A  1 676 ? 1.579   -59.669 75.178  1.00 47.77  ? 703  ASN A CG  1 
ATOM   5254 O OD1 . ASN A  1 676 ? 0.544   -59.020 75.038  1.00 49.71  ? 703  ASN A OD1 1 
ATOM   5255 N ND2 . ASN A  1 676 ? 1.582   -60.950 75.531  1.00 54.97  ? 703  ASN A ND2 1 
ATOM   5256 N N   . LEU A  1 677 ? 4.688   -55.843 74.926  1.00 49.76  ? 704  LEU A N   1 
ATOM   5257 C CA  . LEU A  1 677 ? 6.081   -55.417 74.865  1.00 48.14  ? 704  LEU A CA  1 
ATOM   5258 C C   . LEU A  1 677 ? 6.584   -55.200 76.289  1.00 44.63  ? 704  LEU A C   1 
ATOM   5259 O O   . LEU A  1 677 ? 5.919   -54.543 77.086  1.00 42.15  ? 704  LEU A O   1 
ATOM   5260 C CB  . LEU A  1 677 ? 6.227   -54.147 74.027  1.00 43.86  ? 704  LEU A CB  1 
ATOM   5261 C CG  . LEU A  1 677 ? 5.680   -54.211 72.598  1.00 40.28  ? 704  LEU A CG  1 
ATOM   5262 C CD1 . LEU A  1 677 ? 6.044   -52.952 71.822  1.00 36.54  ? 704  LEU A CD1 1 
ATOM   5263 C CD2 . LEU A  1 677 ? 6.171   -55.456 71.877  1.00 43.84  ? 704  LEU A CD2 1 
ATOM   5264 N N   . THR A  1 678 ? 7.745   -55.762 76.615  1.00 44.83  ? 705  THR A N   1 
ATOM   5265 C CA  . THR A  1 678 ? 8.244   -55.708 77.989  1.00 45.35  ? 705  THR A CA  1 
ATOM   5266 C C   . THR A  1 678 ? 9.458   -54.797 78.138  1.00 39.83  ? 705  THR A C   1 
ATOM   5267 O O   . THR A  1 678 ? 9.800   -54.376 79.244  1.00 41.72  ? 705  THR A O   1 
ATOM   5268 C CB  . THR A  1 678 ? 8.612   -57.101 78.513  1.00 38.27  ? 705  THR A CB  1 
ATOM   5269 O OG1 . THR A  1 678 ? 9.906   -57.469 78.017  1.00 35.48  ? 705  THR A OG1 1 
ATOM   5270 C CG2 . THR A  1 678 ? 7.574   -58.128 78.073  1.00 40.83  ? 705  THR A CG2 1 
ATOM   5271 N N   . SER A  1 679 ? 10.107  -54.498 77.022  1.00 32.90  ? 706  SER A N   1 
ATOM   5272 C CA  . SER A  1 679 ? 11.245  -53.594 77.027  1.00 35.21  ? 706  SER A CA  1 
ATOM   5273 C C   . SER A  1 679 ? 11.468  -53.040 75.628  1.00 43.11  ? 706  SER A C   1 
ATOM   5274 O O   . SER A  1 679 ? 11.397  -53.770 74.639  1.00 49.81  ? 706  SER A O   1 
ATOM   5275 C CB  . SER A  1 679 ? 12.502  -54.307 77.533  1.00 42.86  ? 706  SER A CB  1 
ATOM   5276 O OG  . SER A  1 679 ? 12.759  -55.493 76.799  1.00 48.54  ? 706  SER A OG  1 
ATOM   5277 N N   . ILE A  1 680 ? 11.731  -51.742 75.548  1.00 38.68  ? 707  ILE A N   1 
ATOM   5278 C CA  . ILE A  1 680 ? 11.902  -51.082 74.264  1.00 33.21  ? 707  ILE A CA  1 
ATOM   5279 C C   . ILE A  1 680 ? 13.290  -50.468 74.153  1.00 37.91  ? 707  ILE A C   1 
ATOM   5280 O O   . ILE A  1 680 ? 13.614  -49.519 74.866  1.00 41.50  ? 707  ILE A O   1 
ATOM   5281 C CB  . ILE A  1 680 ? 10.864  -49.966 74.073  1.00 29.08  ? 707  ILE A CB  1 
ATOM   5282 C CG1 . ILE A  1 680 ? 9.452   -50.510 74.264  1.00 24.64  ? 707  ILE A CG1 1 
ATOM   5283 C CG2 . ILE A  1 680 ? 11.003  -49.345 72.701  1.00 38.11  ? 707  ILE A CG2 1 
ATOM   5284 C CD1 . ILE A  1 680 ? 9.081   -51.572 73.268  1.00 36.48  ? 707  ILE A CD1 1 
ATOM   5285 N N   . ASP A  1 681 ? 14.110  -51.011 73.262  1.00 38.75  ? 708  ASP A N   1 
ATOM   5286 C CA  . ASP A  1 681 ? 15.435  -50.451 73.030  1.00 44.93  ? 708  ASP A CA  1 
ATOM   5287 C C   . ASP A  1 681 ? 15.320  -49.251 72.098  1.00 39.26  ? 708  ASP A C   1 
ATOM   5288 O O   . ASP A  1 681 ? 14.417  -49.192 71.268  1.00 37.67  ? 708  ASP A O   1 
ATOM   5289 C CB  . ASP A  1 681 ? 16.379  -51.504 72.438  1.00 51.82  ? 708  ASP A CB  1 
ATOM   5290 C CG  . ASP A  1 681 ? 17.819  -51.018 72.352  1.00 54.92  ? 708  ASP A CG  1 
ATOM   5291 O OD1 . ASP A  1 681 ? 18.222  -50.207 73.213  1.00 54.99  ? 708  ASP A OD1 1 
ATOM   5292 O OD2 . ASP A  1 681 ? 18.547  -51.442 71.426  1.00 52.69  1 708  ASP A OD2 1 
ATOM   5293 N N   . VAL A  1 682 ? 16.239  -48.299 72.236  1.00 41.26  ? 709  VAL A N   1 
ATOM   5294 C CA  . VAL A  1 682 ? 16.227  -47.088 71.421  1.00 38.56  ? 709  VAL A CA  1 
ATOM   5295 C C   . VAL A  1 682 ? 16.606  -47.388 69.968  1.00 49.39  ? 709  VAL A C   1 
ATOM   5296 O O   . VAL A  1 682 ? 16.526  -46.518 69.096  1.00 48.90  ? 709  VAL A O   1 
ATOM   5297 C CB  . VAL A  1 682 ? 17.175  -46.019 71.996  1.00 35.11  ? 709  VAL A CB  1 
ATOM   5298 C CG1 . VAL A  1 682 ? 18.605  -46.265 71.529  1.00 42.87  ? 709  VAL A CG1 1 
ATOM   5299 C CG2 . VAL A  1 682 ? 16.712  -44.629 71.602  1.00 37.53  ? 709  VAL A CG2 1 
ATOM   5300 N N   . ASP A  1 683 ? 17.013  -48.627 69.711  1.00 50.19  ? 710  ASP A N   1 
ATOM   5301 C CA  . ASP A  1 683 ? 17.369  -49.051 68.365  1.00 45.79  ? 710  ASP A CA  1 
ATOM   5302 C C   . ASP A  1 683 ? 16.219  -49.806 67.727  1.00 48.91  ? 710  ASP A C   1 
ATOM   5303 O O   . ASP A  1 683 ? 16.210  -50.030 66.518  1.00 61.19  ? 710  ASP A O   1 
ATOM   5304 C CB  . ASP A  1 683 ? 18.627  -49.916 68.390  1.00 50.09  ? 710  ASP A CB  1 
ATOM   5305 C CG  . ASP A  1 683 ? 19.857  -49.136 68.807  1.00 58.41  ? 710  ASP A CG  1 
ATOM   5306 O OD1 . ASP A  1 683 ? 20.164  -48.111 68.158  1.00 47.01  ? 710  ASP A OD1 1 
ATOM   5307 O OD2 . ASP A  1 683 ? 20.507  -49.539 69.796  1.00 67.01  1 710  ASP A OD2 1 
ATOM   5308 N N   . GLN A  1 684 ? 15.244  -50.197 68.540  1.00 42.39  ? 711  GLN A N   1 
ATOM   5309 C CA  . GLN A  1 684 ? 14.053  -50.858 68.021  1.00 48.07  ? 711  GLN A CA  1 
ATOM   5310 C C   . GLN A  1 684 ? 13.060  -49.836 67.459  1.00 50.16  ? 711  GLN A C   1 
ATOM   5311 O O   . GLN A  1 684 ? 11.982  -50.198 66.981  1.00 49.47  ? 711  GLN A O   1 
ATOM   5312 C CB  . GLN A  1 684 ? 13.392  -51.711 69.105  1.00 39.77  ? 711  GLN A CB  1 
ATOM   5313 C CG  . GLN A  1 684 ? 14.292  -52.792 69.671  1.00 41.20  ? 711  GLN A CG  1 
ATOM   5314 C CD  . GLN A  1 684 ? 13.613  -53.607 70.753  1.00 45.48  ? 711  GLN A CD  1 
ATOM   5315 O OE1 . GLN A  1 684 ? 12.417  -53.460 70.997  1.00 46.73  ? 711  GLN A OE1 1 
ATOM   5316 N NE2 . GLN A  1 684 ? 14.376  -54.472 71.411  1.00 50.92  ? 711  GLN A NE2 1 
ATOM   5317 N N   . LEU A  1 685 ? 13.437  -48.561 67.513  1.00 41.86  ? 712  LEU A N   1 
ATOM   5318 C CA  . LEU A  1 685 ? 12.562  -47.478 67.079  1.00 40.38  ? 712  LEU A CA  1 
ATOM   5319 C C   . LEU A  1 685 ? 13.061  -46.879 65.767  1.00 43.19  ? 712  LEU A C   1 
ATOM   5320 O O   . LEU A  1 685 ? 14.264  -46.688 65.597  1.00 41.81  ? 712  LEU A O   1 
ATOM   5321 C CB  . LEU A  1 685 ? 12.474  -46.399 68.165  1.00 38.99  ? 712  LEU A CB  1 
ATOM   5322 C CG  . LEU A  1 685 ? 12.067  -46.862 69.571  1.00 33.67  ? 712  LEU A CG  1 
ATOM   5323 C CD1 . LEU A  1 685 ? 12.148  -45.723 70.577  1.00 25.37  ? 712  LEU A CD1 1 
ATOM   5324 C CD2 . LEU A  1 685 ? 10.677  -47.476 69.576  1.00 29.88  ? 712  LEU A CD2 1 
ATOM   5325 N N   . PRO A  1 686 ? 12.131  -46.594 64.834  1.00 45.12  ? 713  PRO A N   1 
ATOM   5326 C CA  . PRO A  1 686 ? 12.402  -46.056 63.492  1.00 43.38  ? 713  PRO A CA  1 
ATOM   5327 C C   . PRO A  1 686 ? 12.909  -44.618 63.495  1.00 41.15  ? 713  PRO A C   1 
ATOM   5328 O O   . PRO A  1 686 ? 12.512  -43.829 64.346  1.00 42.55  ? 713  PRO A O   1 
ATOM   5329 C CB  . PRO A  1 686 ? 11.030  -46.111 62.809  1.00 38.37  ? 713  PRO A CB  1 
ATOM   5330 C CG  . PRO A  1 686 ? 10.259  -47.123 63.576  1.00 39.22  ? 713  PRO A CG  1 
ATOM   5331 C CD  . PRO A  1 686 ? 10.713  -46.957 64.990  1.00 44.02  ? 713  PRO A CD  1 
ATOM   5332 N N   . THR A  1 687 ? 13.768  -44.293 62.533  1.00 49.30  ? 714  THR A N   1 
ATOM   5333 C CA  . THR A  1 687 ? 14.343  -42.956 62.405  1.00 53.41  ? 714  THR A CA  1 
ATOM   5334 C C   . THR A  1 687 ? 13.273  -41.904 62.125  1.00 48.64  ? 714  THR A C   1 
ATOM   5335 O O   . THR A  1 687 ? 13.271  -40.830 62.723  1.00 49.54  ? 714  THR A O   1 
ATOM   5336 C CB  . THR A  1 687 ? 15.381  -42.900 61.260  1.00 63.75  ? 714  THR A CB  1 
ATOM   5337 O OG1 . THR A  1 687 ? 16.345  -43.949 61.420  1.00 67.65  ? 714  THR A OG1 1 
ATOM   5338 C CG2 . THR A  1 687 ? 16.090  -41.549 61.237  1.00 51.58  ? 714  THR A CG2 1 
ATOM   5339 N N   . ASN A  1 688 ? 12.367  -42.223 61.208  1.00 45.21  ? 715  ASN A N   1 
ATOM   5340 C CA  . ASN A  1 688 ? 11.328  -41.287 60.795  1.00 47.14  ? 715  ASN A CA  1 
ATOM   5341 C C   . ASN A  1 688 ? 10.123  -41.247 61.739  1.00 46.31  ? 715  ASN A C   1 
ATOM   5342 O O   . ASN A  1 688 ? 9.081   -40.687 61.397  1.00 42.94  ? 715  ASN A O   1 
ATOM   5343 C CB  . ASN A  1 688 ? 10.864  -41.610 59.369  1.00 51.42  ? 715  ASN A CB  1 
ATOM   5344 C CG  . ASN A  1 688 ? 11.777  -41.021 58.309  1.00 56.95  ? 715  ASN A CG  1 
ATOM   5345 O OD1 . ASN A  1 688 ? 12.736  -40.316 58.625  1.00 54.97  ? 715  ASN A OD1 1 
ATOM   5346 N ND2 . ASN A  1 688 ? 11.484  -41.310 57.042  1.00 54.15  ? 715  ASN A ND2 1 
ATOM   5347 N N   . LEU A  1 689 ? 10.268  -41.830 62.926  1.00 41.62  ? 716  LEU A N   1 
ATOM   5348 C CA  . LEU A  1 689 ? 9.144   -41.959 63.850  1.00 36.59  ? 716  LEU A CA  1 
ATOM   5349 C C   . LEU A  1 689 ? 8.654   -40.603 64.347  1.00 36.42  ? 716  LEU A C   1 
ATOM   5350 O O   . LEU A  1 689 ? 9.449   -39.684 64.541  1.00 35.87  ? 716  LEU A O   1 
ATOM   5351 C CB  . LEU A  1 689 ? 9.510   -42.854 65.034  1.00 35.98  ? 716  LEU A CB  1 
ATOM   5352 C CG  . LEU A  1 689 ? 8.319   -43.453 65.785  1.00 34.08  ? 716  LEU A CG  1 
ATOM   5353 C CD1 . LEU A  1 689 ? 7.514   -44.359 64.867  1.00 33.19  ? 716  LEU A CD1 1 
ATOM   5354 C CD2 . LEU A  1 689 ? 8.769   -44.210 67.023  1.00 32.70  ? 716  LEU A CD2 1 
ATOM   5355 N N   . THR A  1 690 ? 7.339   -40.489 64.537  1.00 32.55  ? 717  THR A N   1 
ATOM   5356 C CA  . THR A  1 690 ? 6.725   -39.255 65.018  1.00 27.92  ? 717  THR A CA  1 
ATOM   5357 C C   . THR A  1 690 ? 5.627   -39.542 66.028  1.00 25.34  ? 717  THR A C   1 
ATOM   5358 O O   . THR A  1 690 ? 5.225   -38.666 66.787  1.00 29.56  ? 717  THR A O   1 
ATOM   5359 C CB  . THR A  1 690 ? 6.127   -38.417 63.870  1.00 32.97  ? 717  THR A CB  1 
ATOM   5360 O OG1 . THR A  1 690 ? 5.793   -37.115 64.361  1.00 41.44  ? 717  THR A OG1 1 
ATOM   5361 C CG2 . THR A  1 690 ? 4.868   -39.073 63.304  1.00 30.49  ? 717  THR A CG2 1 
ATOM   5362 N N   . HIS A  1 691 ? 5.134   -40.772 66.026  1.00 23.62  ? 718  HIS A N   1 
ATOM   5363 C CA  . HIS A  1 691 ? 4.135   -41.187 66.997  1.00 25.49  ? 718  HIS A CA  1 
ATOM   5364 C C   . HIS A  1 691 ? 4.585   -42.509 67.583  1.00 25.43  ? 718  HIS A C   1 
ATOM   5365 O O   . HIS A  1 691 ? 5.368   -43.232 66.969  1.00 26.29  ? 718  HIS A O   1 
ATOM   5366 C CB  . HIS A  1 691 ? 2.761   -41.331 66.337  1.00 31.77  ? 718  HIS A CB  1 
ATOM   5367 C CG  . HIS A  1 691 ? 1.626   -41.481 67.306  1.00 28.59  ? 718  HIS A CG  1 
ATOM   5368 N ND1 . HIS A  1 691 ? 1.489   -40.687 68.426  1.00 29.44  ? 718  HIS A ND1 1 
ATOM   5369 C CD2 . HIS A  1 691 ? 0.562   -42.319 67.309  1.00 27.24  ? 718  HIS A CD2 1 
ATOM   5370 C CE1 . HIS A  1 691 ? 0.398   -41.039 69.082  1.00 25.36  ? 718  HIS A CE1 1 
ATOM   5371 N NE2 . HIS A  1 691 ? -0.184  -42.026 68.426  1.00 24.35  ? 718  HIS A NE2 1 
ATOM   5372 N N   . LEU A  1 692 ? 4.100   -42.825 68.773  1.00 22.39  ? 719  LEU A N   1 
ATOM   5373 C CA  . LEU A  1 692 ? 4.533   -44.034 69.443  1.00 23.83  ? 719  LEU A CA  1 
ATOM   5374 C C   . LEU A  1 692 ? 3.526   -44.408 70.504  1.00 22.46  ? 719  LEU A C   1 
ATOM   5375 O O   . LEU A  1 692 ? 3.706   -44.091 71.675  1.00 24.32  ? 719  LEU A O   1 
ATOM   5376 C CB  . LEU A  1 692 ? 5.902   -43.816 70.083  1.00 24.94  ? 719  LEU A CB  1 
ATOM   5377 C CG  . LEU A  1 692 ? 6.865   -45.006 70.114  1.00 26.84  ? 719  LEU A CG  1 
ATOM   5378 C CD1 . LEU A  1 692 ? 8.209   -44.590 70.694  1.00 24.12  ? 719  LEU A CD1 1 
ATOM   5379 C CD2 . LEU A  1 692 ? 6.286   -46.169 70.896  1.00 21.28  ? 719  LEU A CD2 1 
ATOM   5380 N N   . ASP A  1 693 ? 2.463   -45.084 70.094  1.00 21.58  ? 720  ASP A N   1 
ATOM   5381 C CA  . ASP A  1 693 ? 1.443   -45.497 71.039  1.00 22.66  ? 720  ASP A CA  1 
ATOM   5382 C C   . ASP A  1 693 ? 1.767   -46.868 71.601  1.00 28.47  ? 720  ASP A C   1 
ATOM   5383 O O   . ASP A  1 693 ? 1.362   -47.887 71.040  1.00 32.52  ? 720  ASP A O   1 
ATOM   5384 C CB  . ASP A  1 693 ? 0.073   -45.519 70.375  1.00 25.12  ? 720  ASP A CB  1 
ATOM   5385 C CG  . ASP A  1 693 ? -1.050  -45.653 71.373  1.00 26.06  ? 720  ASP A CG  1 
ATOM   5386 O OD1 . ASP A  1 693 ? -0.960  -46.517 72.271  1.00 20.54  ? 720  ASP A OD1 1 
ATOM   5387 O OD2 . ASP A  1 693 ? -2.024  -44.879 71.263  1.00 36.53  1 720  ASP A OD2 1 
ATOM   5388 N N   . ILE A  1 694 ? 2.494   -46.886 72.713  1.00 27.37  ? 721  ILE A N   1 
ATOM   5389 C CA  . ILE A  1 694 ? 2.788   -48.129 73.411  1.00 25.60  ? 721  ILE A CA  1 
ATOM   5390 C C   . ILE A  1 694 ? 1.921   -48.263 74.645  1.00 24.80  ? 721  ILE A C   1 
ATOM   5391 O O   . ILE A  1 694 ? 2.361   -48.796 75.658  1.00 30.40  ? 721  ILE A O   1 
ATOM   5392 C CB  . ILE A  1 694 ? 4.258   -48.213 73.848  1.00 25.19  ? 721  ILE A CB  1 
ATOM   5393 C CG1 . ILE A  1 694 ? 4.811   -46.813 74.110  1.00 25.04  ? 721  ILE A CG1 1 
ATOM   5394 C CG2 . ILE A  1 694 ? 5.080   -48.936 72.799  1.00 30.90  ? 721  ILE A CG2 1 
ATOM   5395 C CD1 . ILE A  1 694 ? 6.267   -46.791 74.498  1.00 21.34  ? 721  ILE A CD1 1 
ATOM   5396 N N   . SER A  1 695 ? 0.692   -47.770 74.564  1.00 26.37  ? 722  SER A N   1 
ATOM   5397 C CA  . SER A  1 695 ? -0.245  -47.940 75.664  1.00 31.20  ? 722  SER A CA  1 
ATOM   5398 C C   . SER A  1 695 ? -0.585  -49.420 75.824  1.00 31.29  ? 722  SER A C   1 
ATOM   5399 O O   . SER A  1 695 ? -0.483  -50.194 74.873  1.00 32.38  ? 722  SER A O   1 
ATOM   5400 C CB  . SER A  1 695 ? -1.516  -47.107 75.445  1.00 30.19  ? 722  SER A CB  1 
ATOM   5401 O OG  . SER A  1 695 ? -2.310  -47.624 74.391  1.00 27.11  ? 722  SER A OG  1 
ATOM   5402 N N   . TRP A  1 696 ? -0.962  -49.804 77.039  1.00 32.69  ? 723  TRP A N   1 
ATOM   5403 C CA  . TRP A  1 696 ? -1.402  -51.164 77.338  1.00 33.82  ? 723  TRP A CA  1 
ATOM   5404 C C   . TRP A  1 696 ? -0.428  -52.247 76.880  1.00 37.80  ? 723  TRP A C   1 
ATOM   5405 O O   . TRP A  1 696 ? -0.747  -53.066 76.018  1.00 38.73  ? 723  TRP A O   1 
ATOM   5406 C CB  . TRP A  1 696 ? -2.807  -51.399 76.784  1.00 30.95  ? 723  TRP A CB  1 
ATOM   5407 C CG  . TRP A  1 696 ? -3.782  -50.423 77.353  1.00 34.63  ? 723  TRP A CG  1 
ATOM   5408 C CD1 . TRP A  1 696 ? -4.180  -49.242 76.799  1.00 32.77  ? 723  TRP A CD1 1 
ATOM   5409 C CD2 . TRP A  1 696 ? -4.454  -50.523 78.613  1.00 38.37  ? 723  TRP A CD2 1 
ATOM   5410 N NE1 . TRP A  1 696 ? -5.072  -48.608 77.629  1.00 32.36  ? 723  TRP A NE1 1 
ATOM   5411 C CE2 . TRP A  1 696 ? -5.256  -49.374 78.750  1.00 33.77  ? 723  TRP A CE2 1 
ATOM   5412 C CE3 . TRP A  1 696 ? -4.460  -51.477 79.637  1.00 40.43  ? 723  TRP A CE3 1 
ATOM   5413 C CZ2 . TRP A  1 696 ? -6.057  -49.154 79.867  1.00 38.97  ? 723  TRP A CZ2 1 
ATOM   5414 C CZ3 . TRP A  1 696 ? -5.255  -51.257 80.746  1.00 35.65  ? 723  TRP A CZ3 1 
ATOM   5415 C CH2 . TRP A  1 696 ? -6.043  -50.105 80.851  1.00 41.31  ? 723  TRP A CH2 1 
ATOM   5416 N N   . ASN A  1 697 ? 0.764   -52.230 77.468  1.00 38.58  ? 724  ASN A N   1 
ATOM   5417 C CA  . ASN A  1 697 ? 1.766   -53.264 77.239  1.00 43.13  ? 724  ASN A CA  1 
ATOM   5418 C C   . ASN A  1 697 ? 2.331   -53.826 78.545  1.00 49.17  ? 724  ASN A C   1 
ATOM   5419 O O   . ASN A  1 697 ? 1.737   -53.656 79.610  1.00 52.41  ? 724  ASN A O   1 
ATOM   5420 C CB  . ASN A  1 697 ? 2.888   -52.746 76.338  1.00 41.20  ? 724  ASN A CB  1 
ATOM   5421 C CG  . ASN A  1 697 ? 2.544   -52.854 74.864  1.00 44.18  ? 724  ASN A CG  1 
ATOM   5422 O OD1 . ASN A  1 697 ? 3.017   -53.755 74.168  1.00 39.97  ? 724  ASN A OD1 1 
ATOM   5423 N ND2 . ASN A  1 697 ? 1.702   -51.942 74.384  1.00 40.54  ? 724  ASN A ND2 1 
ATOM   5424 N N   . HIS A  1 698 ? 3.474   -54.498 78.456  1.00 50.69  ? 725  HIS A N   1 
ATOM   5425 C CA  . HIS A  1 698 ? 4.073   -55.143 79.619  1.00 50.01  ? 725  HIS A CA  1 
ATOM   5426 C C   . HIS A  1 698 ? 5.255   -54.344 80.153  1.00 49.76  ? 725  HIS A C   1 
ATOM   5427 O O   . HIS A  1 698 ? 5.945   -54.789 81.072  1.00 58.72  ? 725  HIS A O   1 
ATOM   5428 C CB  . HIS A  1 698 ? 4.527   -56.561 79.262  1.00 53.32  ? 725  HIS A CB  1 
ATOM   5429 C CG  . HIS A  1 698 ? 3.401   -57.497 78.948  1.00 54.45  ? 725  HIS A CG  1 
ATOM   5430 N ND1 . HIS A  1 698 ? 2.077   -57.128 79.044  1.00 52.31  ? 725  HIS A ND1 1 
ATOM   5431 C CD2 . HIS A  1 698 ? 3.403   -58.789 78.545  1.00 55.72  ? 725  HIS A CD2 1 
ATOM   5432 C CE1 . HIS A  1 698 ? 1.311   -58.151 78.712  1.00 51.81  ? 725  HIS A CE1 1 
ATOM   5433 N NE2 . HIS A  1 698 ? 2.091   -59.172 78.406  1.00 59.86  ? 725  HIS A NE2 1 
ATOM   5434 N N   . LEU A  1 699 ? 5.488   -53.171 79.570  1.00 44.71  ? 726  LEU A N   1 
ATOM   5435 C CA  . LEU A  1 699 ? 6.626   -52.335 79.941  1.00 41.36  ? 726  LEU A CA  1 
ATOM   5436 C C   . LEU A  1 699 ? 6.563   -51.957 81.411  1.00 45.45  ? 726  LEU A C   1 
ATOM   5437 O O   . LEU A  1 699 ? 5.521   -51.513 81.897  1.00 45.42  ? 726  LEU A O   1 
ATOM   5438 C CB  . LEU A  1 699 ? 6.650   -51.064 79.094  1.00 34.27  ? 726  LEU A CB  1 
ATOM   5439 C CG  . LEU A  1 699 ? 6.562   -51.249 77.582  1.00 31.55  ? 726  LEU A CG  1 
ATOM   5440 C CD1 . LEU A  1 699 ? 6.420   -49.909 76.894  1.00 29.09  ? 726  LEU A CD1 1 
ATOM   5441 C CD2 . LEU A  1 699 ? 7.785   -51.974 77.075  1.00 37.11  ? 726  LEU A CD2 1 
ATOM   5442 N N   . GLN A  1 700 ? 7.672   -52.143 82.121  1.00 36.65  ? 727  GLN A N   1 
ATOM   5443 C CA  . GLN A  1 700 ? 7.741   -51.730 83.515  1.00 33.98  ? 727  GLN A CA  1 
ATOM   5444 C C   . GLN A  1 700 ? 8.660   -50.530 83.653  1.00 31.09  ? 727  GLN A C   1 
ATOM   5445 O O   . GLN A  1 700 ? 8.500   -49.712 84.557  1.00 30.73  ? 727  GLN A O   1 
ATOM   5446 C CB  . GLN A  1 700 ? 8.215   -52.878 84.408  1.00 39.72  ? 727  GLN A CB  1 
ATOM   5447 C CG  . GLN A  1 700 ? 7.263   -54.068 84.445  1.00 45.44  ? 727  GLN A CG  1 
ATOM   5448 C CD  . GLN A  1 700 ? 7.651   -55.110 85.479  1.00 47.05  ? 727  GLN A CD  1 
ATOM   5449 O OE1 . GLN A  1 700 ? 8.711   -55.023 86.103  1.00 48.45  ? 727  GLN A OE1 1 
ATOM   5450 N NE2 . GLN A  1 700 ? 6.789   -56.104 85.666  1.00 39.59  ? 727  GLN A NE2 1 
ATOM   5451 N N   . MET A  1 701 ? 9.612   -50.422 82.732  1.00 32.80  ? 728  MET A N   1 
ATOM   5452 C CA  . MET A  1 701 ? 10.621  -49.372 82.782  1.00 31.39  ? 728  MET A CA  1 
ATOM   5453 C C   . MET A  1 701 ? 11.024  -48.935 81.381  1.00 31.80  ? 728  MET A C   1 
ATOM   5454 O O   . MET A  1 701 ? 11.057  -49.744 80.453  1.00 34.77  ? 728  MET A O   1 
ATOM   5455 C CB  . MET A  1 701 ? 11.848  -49.868 83.554  1.00 36.28  ? 728  MET A CB  1 
ATOM   5456 C CG  . MET A  1 701 ? 13.023  -48.896 83.629  1.00 37.40  ? 728  MET A CG  1 
ATOM   5457 S SD  . MET A  1 701 ? 14.159  -49.019 82.227  1.00 48.41  ? 728  MET A SD  1 
ATOM   5458 C CE  . MET A  1 701 ? 14.141  -50.788 81.924  1.00 37.30  ? 728  MET A CE  1 
ATOM   5459 N N   . LEU A  1 702 ? 11.328  -47.650 81.236  1.00 28.56  ? 729  LEU A N   1 
ATOM   5460 C CA  . LEU A  1 702 ? 11.845  -47.113 79.987  1.00 29.43  ? 729  LEU A CA  1 
ATOM   5461 C C   . LEU A  1 702 ? 13.189  -46.443 80.240  1.00 33.21  ? 729  LEU A C   1 
ATOM   5462 O O   . LEU A  1 702 ? 13.283  -45.536 81.064  1.00 40.46  ? 729  LEU A O   1 
ATOM   5463 C CB  . LEU A  1 702 ? 10.863  -46.103 79.394  1.00 28.07  ? 729  LEU A CB  1 
ATOM   5464 C CG  . LEU A  1 702 ? 9.955   -46.587 78.260  1.00 29.99  ? 729  LEU A CG  1 
ATOM   5465 C CD1 . LEU A  1 702 ? 9.190   -47.836 78.655  1.00 28.36  ? 729  LEU A CD1 1 
ATOM   5466 C CD2 . LEU A  1 702 ? 8.995   -45.490 77.837  1.00 25.80  ? 729  LEU A CD2 1 
ATOM   5467 N N   . ASN A  1 703 ? 14.226  -46.893 79.539  1.00 33.04  ? 730  ASN A N   1 
ATOM   5468 C CA  . ASN A  1 703 ? 15.564  -46.334 79.711  1.00 43.13  ? 730  ASN A CA  1 
ATOM   5469 C C   . ASN A  1 703 ? 15.615  -44.855 79.336  1.00 44.60  ? 730  ASN A C   1 
ATOM   5470 O O   . ASN A  1 703 ? 14.760  -44.364 78.602  1.00 42.65  ? 730  ASN A O   1 
ATOM   5471 C CB  . ASN A  1 703 ? 16.594  -47.122 78.894  1.00 55.85  ? 730  ASN A CB  1 
ATOM   5472 C CG  . ASN A  1 703 ? 18.030  -46.867 79.349  1.00 58.00  ? 730  ASN A CG  1 
ATOM   5473 O OD1 . ASN A  1 703 ? 18.646  -45.865 78.979  1.00 49.40  ? 730  ASN A OD1 1 
ATOM   5474 N ND2 . ASN A  1 703 ? 18.570  -47.784 80.149  1.00 52.38  ? 730  ASN A ND2 1 
ATOM   5475 N N   . ALA A  1 704 ? 16.623  -44.152 79.844  1.00 50.85  ? 731  ALA A N   1 
ATOM   5476 C CA  . ALA A  1 704 ? 16.754  -42.713 79.632  1.00 48.45  ? 731  ALA A CA  1 
ATOM   5477 C C   . ALA A  1 704 ? 17.120  -42.343 78.192  1.00 42.45  ? 731  ALA A C   1 
ATOM   5478 O O   . ALA A  1 704 ? 17.004  -41.184 77.790  1.00 37.18  ? 731  ALA A O   1 
ATOM   5479 C CB  . ALA A  1 704 ? 17.770  -42.128 80.607  1.00 48.89  ? 731  ALA A CB  1 
ATOM   5480 N N   . THR A  1 705 ? 17.565  -43.328 77.421  1.00 40.26  ? 732  THR A N   1 
ATOM   5481 C CA  . THR A  1 705 ? 17.948  -43.082 76.037  1.00 40.65  ? 732  THR A CA  1 
ATOM   5482 C C   . THR A  1 705 ? 16.708  -42.953 75.157  1.00 38.42  ? 732  THR A C   1 
ATOM   5483 O O   . THR A  1 705 ? 16.694  -42.194 74.187  1.00 34.28  ? 732  THR A O   1 
ATOM   5484 C CB  . THR A  1 705 ? 18.880  -44.190 75.506  1.00 41.82  ? 732  THR A CB  1 
ATOM   5485 O OG1 . THR A  1 705 ? 19.184  -43.942 74.127  1.00 42.06  ? 732  THR A OG1 1 
ATOM   5486 C CG2 . THR A  1 705 ? 18.235  -45.566 75.655  1.00 40.16  ? 732  THR A CG2 1 
ATOM   5487 N N   . VAL A  1 706 ? 15.668  -43.697 75.518  1.00 37.65  ? 733  VAL A N   1 
ATOM   5488 C CA  . VAL A  1 706 ? 14.375  -43.616 74.855  1.00 34.87  ? 733  VAL A CA  1 
ATOM   5489 C C   . VAL A  1 706 ? 13.765  -42.221 75.016  1.00 33.73  ? 733  VAL A C   1 
ATOM   5490 O O   . VAL A  1 706 ? 13.211  -41.664 74.068  1.00 36.91  ? 733  VAL A O   1 
ATOM   5491 C CB  . VAL A  1 706 ? 13.411  -44.707 75.397  1.00 31.59  ? 733  VAL A CB  1 
ATOM   5492 C CG1 . VAL A  1 706 ? 11.990  -44.189 75.512  1.00 26.69  ? 733  VAL A CG1 1 
ATOM   5493 C CG2 . VAL A  1 706 ? 13.466  -45.950 74.525  1.00 31.69  ? 733  VAL A CG2 1 
ATOM   5494 N N   . LEU A  1 707 ? 13.893  -41.649 76.208  1.00 31.64  ? 734  LEU A N   1 
ATOM   5495 C CA  . LEU A  1 707 ? 13.285  -40.353 76.500  1.00 31.95  ? 734  LEU A CA  1 
ATOM   5496 C C   . LEU A  1 707 ? 13.936  -39.207 75.723  1.00 33.74  ? 734  LEU A C   1 
ATOM   5497 O O   . LEU A  1 707 ? 13.285  -38.212 75.402  1.00 36.84  ? 734  LEU A O   1 
ATOM   5498 C CB  . LEU A  1 707 ? 13.313  -40.057 78.004  1.00 31.36  ? 734  LEU A CB  1 
ATOM   5499 C CG  . LEU A  1 707 ? 12.420  -40.879 78.943  1.00 28.37  ? 734  LEU A CG  1 
ATOM   5500 C CD1 . LEU A  1 707 ? 11.412  -41.735 78.184  1.00 26.85  ? 734  LEU A CD1 1 
ATOM   5501 C CD2 . LEU A  1 707 ? 13.253  -41.735 79.888  1.00 33.10  ? 734  LEU A CD2 1 
ATOM   5502 N N   . GLY A  1 708 ? 15.221  -39.343 75.428  1.00 32.70  ? 735  GLY A N   1 
ATOM   5503 C CA  . GLY A  1 708 ? 15.905  -38.343 74.632  1.00 37.94  ? 735  GLY A CA  1 
ATOM   5504 C C   . GLY A  1 708 ? 15.440  -38.423 73.193  1.00 41.95  ? 735  GLY A C   1 
ATOM   5505 O O   . GLY A  1 708 ? 15.329  -37.408 72.501  1.00 42.93  ? 735  GLY A O   1 
ATOM   5506 N N   . PHE A  1 709 ? 15.163  -39.644 72.745  1.00 44.52  ? 736  PHE A N   1 
ATOM   5507 C CA  . PHE A  1 709 ? 14.680  -39.876 71.389  1.00 41.41  ? 736  PHE A CA  1 
ATOM   5508 C C   . PHE A  1 709 ? 13.311  -39.245 71.193  1.00 37.02  ? 736  PHE A C   1 
ATOM   5509 O O   . PHE A  1 709 ? 13.011  -38.696 70.135  1.00 41.73  ? 736  PHE A O   1 
ATOM   5510 C CB  . PHE A  1 709 ? 14.617  -41.375 71.081  1.00 36.82  ? 736  PHE A CB  1 
ATOM   5511 C CG  . PHE A  1 709 ? 13.991  -41.693 69.751  1.00 42.24  ? 736  PHE A CG  1 
ATOM   5512 C CD1 . PHE A  1 709 ? 14.518  -41.175 68.577  1.00 41.53  ? 736  PHE A CD1 1 
ATOM   5513 C CD2 . PHE A  1 709 ? 12.879  -42.513 69.673  1.00 41.60  ? 736  PHE A CD2 1 
ATOM   5514 C CE1 . PHE A  1 709 ? 13.944  -41.464 67.355  1.00 32.21  ? 736  PHE A CE1 1 
ATOM   5515 C CE2 . PHE A  1 709 ? 12.302  -42.808 68.451  1.00 38.17  ? 736  PHE A CE2 1 
ATOM   5516 C CZ  . PHE A  1 709 ? 12.836  -42.282 67.293  1.00 35.43  ? 736  PHE A CZ  1 
ATOM   5517 N N   . LEU A  1 710 ? 12.488  -39.308 72.231  1.00 32.50  ? 737  LEU A N   1 
ATOM   5518 C CA  . LEU A  1 710 ? 11.136  -38.779 72.155  1.00 31.04  ? 737  LEU A CA  1 
ATOM   5519 C C   . LEU A  1 710 ? 11.108  -37.253 72.209  1.00 36.14  ? 737  LEU A C   1 
ATOM   5520 O O   . LEU A  1 710 ? 10.049  -36.654 72.394  1.00 40.22  ? 737  LEU A O   1 
ATOM   5521 C CB  . LEU A  1 710 ? 10.268  -39.375 73.262  1.00 26.73  ? 737  LEU A CB  1 
ATOM   5522 C CG  . LEU A  1 710 ? 9.486   -40.649 72.932  1.00 19.49  ? 737  LEU A CG  1 
ATOM   5523 C CD1 . LEU A  1 710 ? 10.330  -41.636 72.163  1.00 26.34  ? 737  LEU A CD1 1 
ATOM   5524 C CD2 . LEU A  1 710 ? 8.980   -41.287 74.205  1.00 18.66  ? 737  LEU A CD2 1 
ATOM   5525 N N   . ASN A  1 711 ? 12.268  -36.626 72.037  1.00 38.17  ? 738  ASN A N   1 
ATOM   5526 C CA  . ASN A  1 711 ? 12.344  -35.173 71.993  1.00 43.23  ? 738  ASN A CA  1 
ATOM   5527 C C   . ASN A  1 711 ? 12.079  -34.640 70.587  1.00 42.72  ? 738  ASN A C   1 
ATOM   5528 O O   . ASN A  1 711 ? 12.994  -34.190 69.899  1.00 43.77  ? 738  ASN A O   1 
ATOM   5529 C CB  . ASN A  1 711 ? 13.699  -34.683 72.507  1.00 42.91  ? 738  ASN A CB  1 
ATOM   5530 C CG  . ASN A  1 711 ? 13.754  -33.176 72.657  1.00 51.95  ? 738  ASN A CG  1 
ATOM   5531 O OD1 . ASN A  1 711 ? 12.722  -32.503 72.639  1.00 56.19  ? 738  ASN A OD1 1 
ATOM   5532 N ND2 . ASN A  1 711 ? 14.962  -32.636 72.809  1.00 46.76  ? 738  ASN A ND2 1 
ATOM   5533 N N   . TRP A  1 716 ? 8.991   -33.070 67.121  1.00 36.45  ? 743  TRP A N   1 
ATOM   5534 C CA  . TRP A  1 716 ? 7.826   -33.458 67.910  1.00 42.04  ? 743  TRP A CA  1 
ATOM   5535 C C   . TRP A  1 716 ? 7.604   -34.964 67.898  1.00 40.27  ? 743  TRP A C   1 
ATOM   5536 O O   . TRP A  1 716 ? 7.819   -35.624 66.884  1.00 41.69  ? 743  TRP A O   1 
ATOM   5537 C CB  . TRP A  1 716 ? 6.567   -32.759 67.390  1.00 49.97  ? 743  TRP A CB  1 
ATOM   5538 C CG  . TRP A  1 716 ? 5.286   -33.341 67.932  1.00 44.29  ? 743  TRP A CG  1 
ATOM   5539 C CD1 . TRP A  1 716 ? 4.598   -34.416 67.439  1.00 37.81  ? 743  TRP A CD1 1 
ATOM   5540 C CD2 . TRP A  1 716 ? 4.542   -32.876 69.066  1.00 43.78  ? 743  TRP A CD2 1 
ATOM   5541 N NE1 . TRP A  1 716 ? 3.480   -34.650 68.199  1.00 47.88  ? 743  TRP A NE1 1 
ATOM   5542 C CE2 . TRP A  1 716 ? 3.419   -33.717 69.202  1.00 50.89  ? 743  TRP A CE2 1 
ATOM   5543 C CE3 . TRP A  1 716 ? 4.715   -31.829 69.976  1.00 37.38  ? 743  TRP A CE3 1 
ATOM   5544 C CZ2 . TRP A  1 716 ? 2.472   -33.542 70.213  1.00 42.60  ? 743  TRP A CZ2 1 
ATOM   5545 C CZ3 . TRP A  1 716 ? 3.778   -31.659 70.978  1.00 32.82  ? 743  TRP A CZ3 1 
ATOM   5546 C CH2 . TRP A  1 716 ? 2.671   -32.511 71.089  1.00 36.77  ? 743  TRP A CH2 1 
ATOM   5547 N N   . ARG A  1 717 ? 7.172   -35.504 69.034  1.00 36.12  ? 744  ARG A N   1 
ATOM   5548 C CA  . ARG A  1 717 ? 6.754   -36.898 69.111  1.00 35.94  ? 744  ARG A CA  1 
ATOM   5549 C C   . ARG A  1 717 ? 5.552   -37.041 70.050  1.00 39.71  ? 744  ARG A C   1 
ATOM   5550 O O   . ARG A  1 717 ? 5.700   -36.897 71.264  1.00 41.27  ? 744  ARG A O   1 
ATOM   5551 C CB  . ARG A  1 717 ? 7.893   -37.786 69.623  1.00 23.53  ? 744  ARG A CB  1 
ATOM   5552 C CG  . ARG A  1 717 ? 9.294   -37.264 69.374  1.00 33.01  ? 744  ARG A CG  1 
ATOM   5553 C CD  . ARG A  1 717 ? 9.847   -37.706 68.031  1.00 41.61  ? 744  ARG A CD  1 
ATOM   5554 N NE  . ARG A  1 717 ? 11.307  -37.619 67.997  1.00 43.61  ? 744  ARG A NE  1 
ATOM   5555 C CZ  . ARG A  1 717 ? 12.064  -38.010 66.974  1.00 42.51  ? 744  ARG A CZ  1 
ATOM   5556 N NH1 . ARG A  1 717 ? 11.506  -38.514 65.879  1.00 44.16  1 744  ARG A NH1 1 
ATOM   5557 N NH2 . ARG A  1 717 ? 13.383  -37.895 67.044  1.00 39.94  ? 744  ARG A NH2 1 
ATOM   5558 N N   . SER A  1 718 ? 4.368   -37.319 69.506  1.00 28.14  ? 745  SER A N   1 
ATOM   5559 C CA  . SER A  1 718 ? 3.231   -37.653 70.358  1.00 21.16  ? 745  SER A CA  1 
ATOM   5560 C C   . SER A  1 718 ? 3.446   -39.064 70.890  1.00 22.29  ? 745  SER A C   1 
ATOM   5561 O O   . SER A  1 718 ? 3.827   -39.960 70.137  1.00 22.52  ? 745  SER A O   1 
ATOM   5562 C CB  . SER A  1 718 ? 1.910   -37.560 69.592  1.00 23.61  ? 745  SER A CB  1 
ATOM   5563 O OG  . SER A  1 718 ? 0.795   -37.525 70.473  1.00 18.85  ? 745  SER A OG  1 
ATOM   5564 N N   . VAL A  1 719 ? 3.234   -39.250 72.192  1.00 22.89  ? 746  VAL A N   1 
ATOM   5565 C CA  . VAL A  1 719 ? 3.484   -40.535 72.847  1.00 18.22  ? 746  VAL A CA  1 
ATOM   5566 C C   . VAL A  1 719 ? 2.311   -40.972 73.721  1.00 15.44  ? 746  VAL A C   1 
ATOM   5567 O O   . VAL A  1 719 ? 1.658   -40.142 74.344  1.00 17.49  ? 746  VAL A O   1 
ATOM   5568 C CB  . VAL A  1 719 ? 4.714   -40.463 73.769  1.00 17.52  ? 746  VAL A CB  1 
ATOM   5569 C CG1 . VAL A  1 719 ? 5.323   -41.841 73.937  1.00 18.79  ? 746  VAL A CG1 1 
ATOM   5570 C CG2 . VAL A  1 719 ? 5.743   -39.483 73.233  1.00 19.43  ? 746  VAL A CG2 1 
ATOM   5571 N N   . LYS A  1 720 ? 2.054   -42.275 73.775  1.00 15.02  ? 747  LYS A N   1 
ATOM   5572 C CA  . LYS A  1 720 ? 1.050   -42.829 74.684  1.00 20.03  ? 747  LYS A CA  1 
ATOM   5573 C C   . LYS A  1 720 ? 1.716   -43.837 75.615  1.00 22.93  ? 747  LYS A C   1 
ATOM   5574 O O   . LYS A  1 720 ? 2.506   -44.666 75.165  1.00 22.96  ? 747  LYS A O   1 
ATOM   5575 C CB  . LYS A  1 720 ? -0.076  -43.510 73.907  1.00 21.82  ? 747  LYS A CB  1 
ATOM   5576 C CG  . LYS A  1 720 ? -0.947  -42.571 73.088  1.00 21.80  ? 747  LYS A CG  1 
ATOM   5577 C CD  . LYS A  1 720 ? -2.007  -41.904 73.948  1.00 23.64  ? 747  LYS A CD  1 
ATOM   5578 C CE  . LYS A  1 720 ? -3.264  -41.596 73.139  1.00 36.17  ? 747  LYS A CE  1 
ATOM   5579 N NZ  . LYS A  1 720 ? -3.923  -42.826 72.581  1.00 24.67  1 747  LYS A NZ  1 
ATOM   5580 N N   . LEU A  1 721 ? 1.397   -43.776 76.906  1.00 23.21  ? 748  LEU A N   1 
ATOM   5581 C CA  . LEU A  1 721 ? 2.134   -44.559 77.898  1.00 20.77  ? 748  LEU A CA  1 
ATOM   5582 C C   . LEU A  1 721 ? 1.292   -45.242 78.979  1.00 23.33  ? 748  LEU A C   1 
ATOM   5583 O O   . LEU A  1 721 ? 1.815   -46.039 79.751  1.00 28.63  ? 748  LEU A O   1 
ATOM   5584 C CB  . LEU A  1 721 ? 3.186   -43.679 78.573  1.00 20.13  ? 748  LEU A CB  1 
ATOM   5585 C CG  . LEU A  1 721 ? 4.297   -43.115 77.690  1.00 20.50  ? 748  LEU A CG  1 
ATOM   5586 C CD1 . LEU A  1 721 ? 5.157   -42.143 78.478  1.00 18.68  ? 748  LEU A CD1 1 
ATOM   5587 C CD2 . LEU A  1 721 ? 5.138   -44.239 77.116  1.00 21.18  ? 748  LEU A CD2 1 
ATOM   5588 N N   . SER A  1 722 ? 0.002   -44.938 79.048  1.00 24.73  ? 749  SER A N   1 
ATOM   5589 C CA  . SER A  1 722 ? -0.817  -45.455 80.142  1.00 28.61  ? 749  SER A CA  1 
ATOM   5590 C C   . SER A  1 722 ? -1.010  -46.962 80.035  1.00 29.80  ? 749  SER A C   1 
ATOM   5591 O O   . SER A  1 722 ? -0.615  -47.576 79.048  1.00 27.80  ? 749  SER A O   1 
ATOM   5592 C CB  . SER A  1 722 ? -2.178  -44.758 80.186  1.00 29.15  ? 749  SER A CB  1 
ATOM   5593 O OG  . SER A  1 722 ? -2.988  -45.158 79.097  1.00 28.18  ? 749  SER A OG  1 
ATOM   5594 N N   . GLY A  1 723 ? -1.608  -47.549 81.066  1.00 35.98  ? 750  GLY A N   1 
ATOM   5595 C CA  . GLY A  1 723 ? -1.968  -48.955 81.049  1.00 32.29  ? 750  GLY A CA  1 
ATOM   5596 C C   . GLY A  1 723 ? -0.792  -49.909 81.098  1.00 36.06  ? 750  GLY A C   1 
ATOM   5597 O O   . GLY A  1 723 ? -0.913  -51.066 80.698  1.00 34.45  ? 750  GLY A O   1 
ATOM   5598 N N   . ASN A  1 724 ? 0.350   -49.430 81.582  1.00 37.80  ? 751  ASN A N   1 
ATOM   5599 C CA  . ASN A  1 724 ? 1.522   -50.284 81.746  1.00 35.24  ? 751  ASN A CA  1 
ATOM   5600 C C   . ASN A  1 724 ? 1.913   -50.455 83.206  1.00 43.51  ? 751  ASN A C   1 
ATOM   5601 O O   . ASN A  1 724 ? 1.723   -49.542 84.014  1.00 42.13  ? 751  ASN A O   1 
ATOM   5602 C CB  . ASN A  1 724 ? 2.705   -49.746 80.946  1.00 34.82  ? 751  ASN A CB  1 
ATOM   5603 C CG  . ASN A  1 724 ? 2.476   -49.825 79.458  1.00 40.55  ? 751  ASN A CG  1 
ATOM   5604 O OD1 . ASN A  1 724 ? 1.353   -49.655 78.984  1.00 41.36  ? 751  ASN A OD1 1 
ATOM   5605 N ND2 . ASN A  1 724 ? 3.538   -50.097 78.707  1.00 40.61  ? 751  ASN A ND2 1 
ATOM   5606 N N   . PRO A  1 725 ? 2.461   -51.634 83.550  1.00 45.41  ? 752  PRO A N   1 
ATOM   5607 C CA  . PRO A  1 725 ? 2.860   -51.934 84.928  1.00 41.48  ? 752  PRO A CA  1 
ATOM   5608 C C   . PRO A  1 725 ? 4.125   -51.176 85.310  1.00 45.00  ? 752  PRO A C   1 
ATOM   5609 O O   . PRO A  1 725 ? 5.193   -51.777 85.417  1.00 52.45  ? 752  PRO A O   1 
ATOM   5610 C CB  . PRO A  1 725 ? 3.145   -53.434 84.878  1.00 40.25  ? 752  PRO A CB  1 
ATOM   5611 C CG  . PRO A  1 725 ? 3.574   -53.677 83.469  1.00 39.79  ? 752  PRO A CG  1 
ATOM   5612 C CD  . PRO A  1 725 ? 2.736   -52.759 82.638  1.00 40.05  ? 752  PRO A CD  1 
ATOM   5613 N N   . TRP A  1 726 ? 4.005   -49.870 85.518  1.00 39.44  ? 753  TRP A N   1 
ATOM   5614 C CA  . TRP A  1 726 ? 5.174   -49.047 85.788  1.00 35.25  ? 753  TRP A CA  1 
ATOM   5615 C C   . TRP A  1 726 ? 5.738   -49.250 87.188  1.00 47.50  ? 753  TRP A C   1 
ATOM   5616 O O   . TRP A  1 726 ? 5.115   -48.886 88.189  1.00 44.17  ? 753  TRP A O   1 
ATOM   5617 C CB  . TRP A  1 726 ? 4.866   -47.574 85.551  1.00 30.93  ? 753  TRP A CB  1 
ATOM   5618 C CG  . TRP A  1 726 ? 4.462   -47.295 84.150  1.00 36.16  ? 753  TRP A CG  1 
ATOM   5619 C CD1 . TRP A  1 726 ? 3.244   -46.863 83.717  1.00 39.02  ? 753  TRP A CD1 1 
ATOM   5620 C CD2 . TRP A  1 726 ? 5.271   -47.452 82.983  1.00 32.19  ? 753  TRP A CD2 1 
ATOM   5621 N NE1 . TRP A  1 726 ? 3.249   -46.729 82.351  1.00 30.68  ? 753  TRP A NE1 1 
ATOM   5622 C CE2 . TRP A  1 726 ? 4.484   -47.085 81.877  1.00 29.46  ? 753  TRP A CE2 1 
ATOM   5623 C CE3 . TRP A  1 726 ? 6.589   -47.859 82.766  1.00 34.88  ? 753  TRP A CE3 1 
ATOM   5624 C CZ2 . TRP A  1 726 ? 4.968   -47.115 80.575  1.00 29.71  ? 753  TRP A CZ2 1 
ATOM   5625 C CZ3 . TRP A  1 726 ? 7.067   -47.888 81.472  1.00 32.88  ? 753  TRP A CZ3 1 
ATOM   5626 C CH2 . TRP A  1 726 ? 6.259   -47.519 80.394  1.00 29.19  ? 753  TRP A CH2 1 
ATOM   5627 N N   . MET A  1 727 ? 6.927   -49.843 87.241  1.00 48.45  ? 754  MET A N   1 
ATOM   5628 C CA  . MET A  1 727 ? 7.677   -49.954 88.479  1.00 44.41  ? 754  MET A CA  1 
ATOM   5629 C C   . MET A  1 727 ? 8.327   -48.607 88.769  1.00 43.09  ? 754  MET A C   1 
ATOM   5630 O O   . MET A  1 727 ? 9.326   -48.242 88.146  1.00 37.36  ? 754  MET A O   1 
ATOM   5631 C CB  . MET A  1 727 ? 8.742   -51.042 88.356  1.00 51.74  ? 754  MET A CB  1 
ATOM   5632 C CG  . MET A  1 727 ? 9.582   -51.242 89.607  1.00 61.95  ? 754  MET A CG  1 
ATOM   5633 S SD  . MET A  1 727 ? 10.962  -52.365 89.327  1.00 74.15  ? 754  MET A SD  1 
ATOM   5634 C CE  . MET A  1 727 ? 11.745  -52.355 90.937  1.00 67.91  ? 754  MET A CE  1 
ATOM   5635 N N   . CYS A  1 728 ? 7.744   -47.870 89.711  1.00 47.29  ? 755  CYS A N   1 
ATOM   5636 C CA  . CYS A  1 728 ? 8.210   -46.529 90.052  1.00 49.79  ? 755  CYS A CA  1 
ATOM   5637 C C   . CYS A  1 728 ? 9.146   -46.520 91.265  1.00 48.79  ? 755  CYS A C   1 
ATOM   5638 O O   . CYS A  1 728 ? 8.701   -46.509 92.414  1.00 45.93  ? 755  CYS A O   1 
ATOM   5639 C CB  . CYS A  1 728 ? 7.020   -45.606 90.321  1.00 50.08  ? 755  CYS A CB  1 
ATOM   5640 S SG  . CYS A  1 728 ? 5.664   -45.767 89.150  1.00 26.48  ? 755  CYS A SG  1 
ATOM   5641 N N   . ASP A  1 729 ? 10.444  -46.523 90.998  1.00 44.59  ? 756  ASP A N   1 
ATOM   5642 C CA  . ASP A  1 729 ? 11.442  -46.422 92.048  1.00 40.86  ? 756  ASP A CA  1 
ATOM   5643 C C   . ASP A  1 729 ? 12.464  -45.386 91.611  1.00 45.02  ? 756  ASP A C   1 
ATOM   5644 O O   . ASP A  1 729 ? 12.121  -44.421 90.930  1.00 48.82  ? 756  ASP A O   1 
ATOM   5645 C CB  . ASP A  1 729 ? 12.116  -47.769 92.266  1.00 37.98  ? 756  ASP A CB  1 
ATOM   5646 C CG  . ASP A  1 729 ? 12.700  -48.327 90.992  1.00 44.28  ? 756  ASP A CG  1 
ATOM   5647 O OD1 . ASP A  1 729 ? 13.800  -47.882 90.603  1.00 42.10  1 756  ASP A OD1 1 
ATOM   5648 O OD2 . ASP A  1 729 ? 12.053  -49.197 90.373  1.00 46.04  ? 756  ASP A OD2 1 
ATOM   5649 N N   . CYS A  1 730 ? 13.722  -45.582 91.983  1.00 44.54  ? 757  CYS A N   1 
ATOM   5650 C CA  . CYS A  1 730 ? 14.751  -44.618 91.615  1.00 46.99  ? 757  CYS A CA  1 
ATOM   5651 C C   . CYS A  1 730 ? 15.217  -44.759 90.167  1.00 41.69  ? 757  CYS A C   1 
ATOM   5652 O O   . CYS A  1 730 ? 15.764  -43.815 89.598  1.00 42.90  ? 757  CYS A O   1 
ATOM   5653 C CB  . CYS A  1 730 ? 15.937  -44.672 92.583  1.00 48.80  ? 757  CYS A CB  1 
ATOM   5654 S SG  . CYS A  1 730 ? 15.878  -43.400 93.873  1.00 50.40  ? 757  CYS A SG  1 
ATOM   5655 N N   . THR A  1 731 ? 14.999  -45.925 89.567  1.00 37.99  ? 758  THR A N   1 
ATOM   5656 C CA  . THR A  1 731 ? 15.404  -46.121 88.179  1.00 43.30  ? 758  THR A CA  1 
ATOM   5657 C C   . THR A  1 731 ? 14.337  -45.606 87.222  1.00 43.36  ? 758  THR A C   1 
ATOM   5658 O O   . THR A  1 731 ? 14.574  -45.476 86.021  1.00 43.60  ? 758  THR A O   1 
ATOM   5659 C CB  . THR A  1 731 ? 15.720  -47.594 87.854  1.00 48.11  ? 758  THR A CB  1 
ATOM   5660 O OG1 . THR A  1 731 ? 16.413  -47.666 86.600  1.00 45.09  ? 758  THR A OG1 1 
ATOM   5661 C CG2 . THR A  1 731 ? 14.441  -48.417 87.774  1.00 47.20  ? 758  THR A CG2 1 
ATOM   5662 N N   . ALA A  1 732 ? 13.160  -45.317 87.769  1.00 44.84  ? 759  ALA A N   1 
ATOM   5663 C CA  . ALA A  1 732 ? 12.063  -44.758 86.991  1.00 41.12  ? 759  ALA A CA  1 
ATOM   5664 C C   . ALA A  1 732 ? 12.119  -43.237 87.042  1.00 34.28  ? 759  ALA A C   1 
ATOM   5665 O O   . ALA A  1 732 ? 11.436  -42.557 86.275  1.00 32.45  ? 759  ALA A O   1 
ATOM   5666 C CB  . ALA A  1 732 ? 10.725  -45.261 87.518  1.00 39.47  ? 759  ALA A CB  1 
ATOM   5667 N N   . LYS A  1 733 ? 12.944  -42.718 87.951  1.00 30.75  ? 760  LYS A N   1 
ATOM   5668 C CA  . LYS A  1 733 ? 13.120  -41.275 88.124  1.00 30.11  ? 760  LYS A CA  1 
ATOM   5669 C C   . LYS A  1 733 ? 13.285  -40.463 86.827  1.00 28.09  ? 760  LYS A C   1 
ATOM   5670 O O   . LYS A  1 733 ? 12.716  -39.375 86.721  1.00 27.52  ? 760  LYS A O   1 
ATOM   5671 C CB  . LYS A  1 733 ? 14.264  -40.971 89.105  1.00 33.07  ? 760  LYS A CB  1 
ATOM   5672 C CG  . LYS A  1 733 ? 14.518  -39.479 89.328  1.00 33.09  ? 760  LYS A CG  1 
ATOM   5673 C CD  . LYS A  1 733 ? 15.555  -39.238 90.418  1.00 43.26  ? 760  LYS A CD  1 
ATOM   5674 C CE  . LYS A  1 733 ? 15.783  -37.747 90.656  1.00 51.92  ? 760  LYS A CE  1 
ATOM   5675 N NZ  . LYS A  1 733 ? 16.730  -37.489 91.786  1.00 57.73  1 760  LYS A NZ  1 
ATOM   5676 N N   . PRO A  1 734 ? 14.058  -40.974 85.843  1.00 25.02  ? 761  PRO A N   1 
ATOM   5677 C CA  . PRO A  1 734 ? 14.122  -40.206 84.596  1.00 26.23  ? 761  PRO A CA  1 
ATOM   5678 C C   . PRO A  1 734 ? 12.749  -40.086 83.945  1.00 27.77  ? 761  PRO A C   1 
ATOM   5679 O O   . PRO A  1 734 ? 12.358  -38.993 83.524  1.00 23.29  ? 761  PRO A O   1 
ATOM   5680 C CB  . PRO A  1 734 ? 15.040  -41.055 83.713  1.00 21.94  ? 761  PRO A CB  1 
ATOM   5681 C CG  . PRO A  1 734 ? 15.874  -41.802 84.651  1.00 19.92  ? 761  PRO A CG  1 
ATOM   5682 C CD  . PRO A  1 734 ? 14.999  -42.108 85.821  1.00 24.79  ? 761  PRO A CD  1 
ATOM   5683 N N   . LEU A  1 735 ? 12.029  -41.203 83.880  1.00 28.26  ? 762  LEU A N   1 
ATOM   5684 C CA  . LEU A  1 735 ? 10.718  -41.238 83.249  1.00 25.33  ? 762  LEU A CA  1 
ATOM   5685 C C   . LEU A  1 735 ? 9.767   -40.306 83.977  1.00 23.68  ? 762  LEU A C   1 
ATOM   5686 O O   . LEU A  1 735 ? 8.951   -39.628 83.355  1.00 26.89  ? 762  LEU A O   1 
ATOM   5687 C CB  . LEU A  1 735 ? 10.158  -42.662 83.243  1.00 27.01  ? 762  LEU A CB  1 
ATOM   5688 C CG  . LEU A  1 735 ? 8.872   -42.861 82.440  1.00 21.58  ? 762  LEU A CG  1 
ATOM   5689 C CD1 . LEU A  1 735 ? 9.144   -42.645 80.963  1.00 15.88  ? 762  LEU A CD1 1 
ATOM   5690 C CD2 . LEU A  1 735 ? 8.261   -44.235 82.698  1.00 17.87  ? 762  LEU A CD2 1 
ATOM   5691 N N   . LEU A  1 736 ? 9.888   -40.266 85.299  1.00 23.19  ? 763  LEU A N   1 
ATOM   5692 C CA  . LEU A  1 736 ? 9.028   -39.420 86.112  1.00 23.41  ? 763  LEU A CA  1 
ATOM   5693 C C   . LEU A  1 736 ? 9.303   -37.941 85.854  1.00 23.78  ? 763  LEU A C   1 
ATOM   5694 O O   . LEU A  1 736 ? 8.419   -37.106 86.003  1.00 28.22  ? 763  LEU A O   1 
ATOM   5695 C CB  . LEU A  1 736 ? 9.191   -39.746 87.596  1.00 20.83  ? 763  LEU A CB  1 
ATOM   5696 C CG  . LEU A  1 736 ? 8.041   -39.299 88.498  1.00 21.33  ? 763  LEU A CG  1 
ATOM   5697 C CD1 . LEU A  1 736 ? 7.428   -40.490 89.208  1.00 27.19  ? 763  LEU A CD1 1 
ATOM   5698 C CD2 . LEU A  1 736 ? 8.517   -38.277 89.503  1.00 27.88  ? 763  LEU A CD2 1 
ATOM   5699 N N   . LEU A  1 737 ? 10.526  -37.611 85.460  1.00 21.54  ? 764  LEU A N   1 
ATOM   5700 C CA  . LEU A  1 737 ? 10.825  -36.236 85.088  1.00 22.80  ? 764  LEU A CA  1 
ATOM   5701 C C   . LEU A  1 737 ? 10.382  -35.953 83.659  1.00 21.32  ? 764  LEU A C   1 
ATOM   5702 O O   . LEU A  1 737 ? 10.039  -34.818 83.322  1.00 20.63  ? 764  LEU A O   1 
ATOM   5703 C CB  . LEU A  1 737 ? 12.313  -35.924 85.252  1.00 27.85  ? 764  LEU A CB  1 
ATOM   5704 C CG  . LEU A  1 737 ? 12.800  -35.552 86.654  1.00 24.18  ? 764  LEU A CG  1 
ATOM   5705 C CD1 . LEU A  1 737 ? 14.249  -35.116 86.588  1.00 33.78  ? 764  LEU A CD1 1 
ATOM   5706 C CD2 . LEU A  1 737 ? 11.941  -34.460 87.270  1.00 17.53  ? 764  LEU A CD2 1 
ATOM   5707 N N   . PHE A  1 738 ? 10.399  -36.990 82.825  1.00 23.05  ? 765  PHE A N   1 
ATOM   5708 C CA  . PHE A  1 738 ? 9.975   -36.862 81.436  1.00 19.86  ? 765  PHE A CA  1 
ATOM   5709 C C   . PHE A  1 738 ? 8.545   -36.387 81.407  1.00 18.97  ? 765  PHE A C   1 
ATOM   5710 O O   . PHE A  1 738 ? 8.242   -35.312 80.887  1.00 19.75  ? 765  PHE A O   1 
ATOM   5711 C CB  . PHE A  1 738 ? 10.080  -38.201 80.708  1.00 17.84  ? 765  PHE A CB  1 
ATOM   5712 C CG  . PHE A  1 738 ? 9.749   -38.123 79.242  1.00 22.12  ? 765  PHE A CG  1 
ATOM   5713 C CD1 . PHE A  1 738 ? 10.336  -37.163 78.434  1.00 24.38  ? 765  PHE A CD1 1 
ATOM   5714 C CD2 . PHE A  1 738 ? 8.866   -39.020 78.665  1.00 23.59  ? 765  PHE A CD2 1 
ATOM   5715 C CE1 . PHE A  1 738 ? 10.037  -37.095 77.086  1.00 20.12  ? 765  PHE A CE1 1 
ATOM   5716 C CE2 . PHE A  1 738 ? 8.565   -38.954 77.316  1.00 15.48  ? 765  PHE A CE2 1 
ATOM   5717 C CZ  . PHE A  1 738 ? 9.152   -37.991 76.531  1.00 17.37  ? 765  PHE A CZ  1 
ATOM   5718 N N   . THR A  1 739 ? 7.675   -37.198 81.995  1.00 20.37  ? 766  THR A N   1 
ATOM   5719 C CA  . THR A  1 739 ? 6.256   -36.901 82.060  1.00 20.04  ? 766  THR A CA  1 
ATOM   5720 C C   . THR A  1 739 ? 6.019   -35.514 82.643  1.00 17.76  ? 766  THR A C   1 
ATOM   5721 O O   . THR A  1 739 ? 5.244   -34.727 82.100  1.00 19.00  ? 766  THR A O   1 
ATOM   5722 C CB  . THR A  1 739 ? 5.515   -37.953 82.905  1.00 17.93  ? 766  THR A CB  1 
ATOM   5723 O OG1 . THR A  1 739 ? 5.904   -37.830 84.277  1.00 15.89  ? 766  THR A OG1 1 
ATOM   5724 C CG2 . THR A  1 739 ? 5.844   -39.353 82.413  1.00 15.10  ? 766  THR A CG2 1 
ATOM   5725 N N   . GLN A  1 740 ? 6.719   -35.206 83.727  1.00 14.54  ? 767  GLN A N   1 
ATOM   5726 C CA  . GLN A  1 740 ? 6.487   -33.961 84.444  1.00 17.88  ? 767  GLN A CA  1 
ATOM   5727 C C   . GLN A  1 740 ? 6.703   -32.714 83.594  1.00 20.44  ? 767  GLN A C   1 
ATOM   5728 O O   . GLN A  1 740 ? 6.166   -31.652 83.903  1.00 23.09  ? 767  GLN A O   1 
ATOM   5729 C CB  . GLN A  1 740 ? 7.337   -33.897 85.712  1.00 20.38  ? 767  GLN A CB  1 
ATOM   5730 C CG  . GLN A  1 740 ? 6.727   -34.623 86.901  1.00 25.23  ? 767  GLN A CG  1 
ATOM   5731 C CD  . GLN A  1 740 ? 7.658   -34.663 88.102  1.00 29.18  ? 767  GLN A CD  1 
ATOM   5732 O OE1 . GLN A  1 740 ? 8.752   -34.090 88.078  1.00 23.89  ? 767  GLN A OE1 1 
ATOM   5733 N NE2 . GLN A  1 740 ? 7.225   -35.337 89.163  1.00 29.39  ? 767  GLN A NE2 1 
ATOM   5734 N N   . ASP A  1 741 ? 7.475   -32.832 82.521  1.00 20.15  ? 768  ASP A N   1 
ATOM   5735 C CA  . ASP A  1 741 ? 7.705   -31.670 81.675  1.00 19.79  ? 768  ASP A CA  1 
ATOM   5736 C C   . ASP A  1 741 ? 7.183   -31.848 80.261  1.00 22.68  ? 768  ASP A C   1 
ATOM   5737 O O   . ASP A  1 741 ? 6.784   -30.882 79.617  1.00 27.05  ? 768  ASP A O   1 
ATOM   5738 C CB  . ASP A  1 741 ? 9.180   -31.292 81.638  1.00 19.11  ? 768  ASP A CB  1 
ATOM   5739 C CG  . ASP A  1 741 ? 9.414   -29.977 80.930  1.00 24.42  ? 768  ASP A CG  1 
ATOM   5740 O OD1 . ASP A  1 741 ? 9.301   -28.915 81.588  1.00 17.90  1 768  ASP A OD1 1 
ATOM   5741 O OD2 . ASP A  1 741 ? 9.693   -30.007 79.710  1.00 28.51  ? 768  ASP A OD2 1 
ATOM   5742 N N   . ASN A  1 742 ? 7.186   -33.081 79.775  1.00 20.64  ? 769  ASN A N   1 
ATOM   5743 C CA  . ASN A  1 742 ? 6.689   -33.344 78.431  1.00 24.46  ? 769  ASN A CA  1 
ATOM   5744 C C   . ASN A  1 742 ? 5.195   -33.624 78.396  1.00 25.04  ? 769  ASN A C   1 
ATOM   5745 O O   . ASN A  1 742 ? 4.762   -34.675 77.929  1.00 24.96  ? 769  ASN A O   1 
ATOM   5746 C CB  . ASN A  1 742 ? 7.475   -34.476 77.781  1.00 22.20  ? 769  ASN A CB  1 
ATOM   5747 C CG  . ASN A  1 742 ? 8.811   -34.011 77.257  1.00 29.16  ? 769  ASN A CG  1 
ATOM   5748 O OD1 . ASN A  1 742 ? 9.096   -34.120 76.063  1.00 32.30  ? 769  ASN A OD1 1 
ATOM   5749 N ND2 . ASN A  1 742 ? 9.631   -33.452 78.142  1.00 30.19  ? 769  ASN A ND2 1 
ATOM   5750 N N   . PHE A  1 743 ? 4.420   -32.658 78.881  1.00 25.34  ? 770  PHE A N   1 
ATOM   5751 C CA  . PHE A  1 743 ? 2.968   -32.778 79.003  1.00 26.52  ? 770  PHE A CA  1 
ATOM   5752 C C   . PHE A  1 743 ? 2.237   -32.937 77.673  1.00 29.39  ? 770  PHE A C   1 
ATOM   5753 O O   . PHE A  1 743 ? 1.367   -33.800 77.539  1.00 29.88  ? 770  PHE A O   1 
ATOM   5754 C CB  . PHE A  1 743 ? 2.418   -31.566 79.749  1.00 29.47  ? 770  PHE A CB  1 
ATOM   5755 C CG  . PHE A  1 743 ? 0.956   -31.312 79.514  1.00 31.40  ? 770  PHE A CG  1 
ATOM   5756 C CD1 . PHE A  1 743 ? -0.006  -32.168 80.034  1.00 38.61  ? 770  PHE A CD1 1 
ATOM   5757 C CD2 . PHE A  1 743 ? 0.541   -30.197 78.800  1.00 26.03  ? 770  PHE A CD2 1 
ATOM   5758 C CE1 . PHE A  1 743 ? -1.356  -31.923 79.831  1.00 43.55  ? 770  PHE A CE1 1 
ATOM   5759 C CE2 . PHE A  1 743 ? -0.804  -29.946 78.596  1.00 30.86  ? 770  PHE A CE2 1 
ATOM   5760 C CZ  . PHE A  1 743 ? -1.755  -30.810 79.111  1.00 38.45  ? 770  PHE A CZ  1 
ATOM   5761 N N   . GLU A  1 744 ? 2.584   -32.092 76.704  1.00 33.39  ? 771  GLU A N   1 
ATOM   5762 C CA  . GLU A  1 744 ? 1.977   -32.111 75.372  1.00 24.10  ? 771  GLU A CA  1 
ATOM   5763 C C   . GLU A  1 744 ? 2.098   -33.473 74.705  1.00 24.42  ? 771  GLU A C   1 
ATOM   5764 O O   . GLU A  1 744 ? 1.108   -34.033 74.235  1.00 25.83  ? 771  GLU A O   1 
ATOM   5765 C CB  . GLU A  1 744 ? 2.635   -31.059 74.479  1.00 17.41  ? 771  GLU A CB  1 
ATOM   5766 C CG  . GLU A  1 744 ? 2.431   -29.621 74.933  1.00 21.14  ? 771  GLU A CG  1 
ATOM   5767 C CD  . GLU A  1 744 ? 3.386   -29.191 76.032  1.00 23.13  ? 771  GLU A CD  1 
ATOM   5768 O OE1 . GLU A  1 744 ? 3.648   -29.992 76.953  1.00 26.78  ? 771  GLU A OE1 1 
ATOM   5769 O OE2 . GLU A  1 744 ? 3.879   -28.044 75.973  1.00 20.18  1 771  GLU A OE2 1 
ATOM   5770 N N   . ARG A  1 745 ? 3.320   -33.995 74.679  1.00 24.38  ? 772  ARG A N   1 
ATOM   5771 C CA  . ARG A  1 745 ? 3.626   -35.255 74.015  1.00 23.49  ? 772  ARG A CA  1 
ATOM   5772 C C   . ARG A  1 745 ? 2.803   -36.425 74.537  1.00 20.01  ? 772  ARG A C   1 
ATOM   5773 O O   . ARG A  1 745 ? 2.397   -37.294 73.770  1.00 20.53  ? 772  ARG A O   1 
ATOM   5774 C CB  . ARG A  1 745 ? 5.112   -35.582 74.158  1.00 22.78  ? 772  ARG A CB  1 
ATOM   5775 C CG  . ARG A  1 745 ? 6.034   -34.683 73.370  1.00 25.54  ? 772  ARG A CG  1 
ATOM   5776 C CD  . ARG A  1 745 ? 7.464   -35.143 73.532  1.00 22.99  ? 772  ARG A CD  1 
ATOM   5777 N NE  . ARG A  1 745 ? 8.345   -34.692 72.459  1.00 30.74  ? 772  ARG A NE  1 
ATOM   5778 C CZ  . ARG A  1 745 ? 8.431   -33.440 72.020  1.00 36.43  ? 772  ARG A CZ  1 
ATOM   5779 N NH1 . ARG A  1 745 ? 7.675   -32.484 72.546  1.00 34.79  1 772  ARG A NH1 1 
ATOM   5780 N NH2 . ARG A  1 745 ? 9.275   -33.143 71.041  1.00 38.93  ? 772  ARG A NH2 1 
ATOM   5781 N N   . ILE A  1 746 ? 2.560   -36.453 75.840  1.00 16.77  ? 773  ILE A N   1 
ATOM   5782 C CA  . ILE A  1 746 ? 1.889   -37.598 76.437  1.00 18.11  ? 773  ILE A CA  1 
ATOM   5783 C C   . ILE A  1 746 ? 0.416   -37.308 76.704  1.00 24.09  ? 773  ILE A C   1 
ATOM   5784 O O   . ILE A  1 746 ? 0.072   -36.518 77.584  1.00 24.77  ? 773  ILE A O   1 
ATOM   5785 C CB  . ILE A  1 746 ? 2.590   -38.051 77.725  1.00 17.20  ? 773  ILE A CB  1 
ATOM   5786 C CG1 . ILE A  1 746 ? 4.079   -38.278 77.460  1.00 16.59  ? 773  ILE A CG1 1 
ATOM   5787 C CG2 . ILE A  1 746 ? 1.955   -39.319 78.255  1.00 18.60  ? 773  ILE A CG2 1 
ATOM   5788 C CD1 . ILE A  1 746 ? 4.913   -38.376 78.707  1.00 16.10  ? 773  ILE A CD1 1 
ATOM   5789 N N   . GLY A  1 747 ? -0.451  -37.955 75.932  1.00 23.89  ? 774  GLY A N   1 
ATOM   5790 C CA  . GLY A  1 747 ? -1.877  -37.720 76.027  1.00 18.63  ? 774  GLY A CA  1 
ATOM   5791 C C   . GLY A  1 747 ? -2.490  -38.293 77.285  1.00 20.96  ? 774  GLY A C   1 
ATOM   5792 O O   . GLY A  1 747 ? -3.510  -37.795 77.758  1.00 25.54  ? 774  GLY A O   1 
ATOM   5793 N N   . ASP A  1 748 ? -1.864  -39.332 77.835  1.00 19.40  ? 775  ASP A N   1 
ATOM   5794 C CA  . ASP A  1 748 ? -2.447  -40.078 78.950  1.00 23.15  ? 775  ASP A CA  1 
ATOM   5795 C C   . ASP A  1 748 ? -1.612  -40.027 80.225  1.00 26.19  ? 775  ASP A C   1 
ATOM   5796 O O   . ASP A  1 748 ? -1.544  -41.002 80.977  1.00 26.70  ? 775  ASP A O   1 
ATOM   5797 C CB  . ASP A  1 748 ? -2.686  -41.531 78.540  1.00 23.50  ? 775  ASP A CB  1 
ATOM   5798 C CG  . ASP A  1 748 ? -1.543  -42.095 77.730  1.00 22.91  ? 775  ASP A CG  1 
ATOM   5799 O OD1 . ASP A  1 748 ? -0.611  -41.320 77.430  1.00 20.18  ? 775  ASP A OD1 1 
ATOM   5800 O OD2 . ASP A  1 748 ? -1.584  -43.297 77.381  1.00 24.67  1 775  ASP A OD2 1 
ATOM   5801 N N   . ARG A  1 749 ? -0.986  -38.879 80.459  1.00 26.99  ? 776  ARG A N   1 
ATOM   5802 C CA  . ARG A  1 749 ? -0.174  -38.662 81.645  1.00 24.23  ? 776  ARG A CA  1 
ATOM   5803 C C   . ARG A  1 749 ? -0.992  -38.964 82.895  1.00 30.85  ? 776  ARG A C   1 
ATOM   5804 O O   . ARG A  1 749 ? -0.613  -39.811 83.702  1.00 40.37  ? 776  ARG A O   1 
ATOM   5805 C CB  . ARG A  1 749 ? 0.328   -37.219 81.674  1.00 24.49  ? 776  ARG A CB  1 
ATOM   5806 C CG  . ARG A  1 749 ? 1.763   -37.062 82.135  1.00 21.54  ? 776  ARG A CG  1 
ATOM   5807 C CD  . ARG A  1 749 ? 2.200   -35.609 82.083  1.00 19.84  ? 776  ARG A CD  1 
ATOM   5808 N NE  . ARG A  1 749 ? 1.233   -34.727 82.727  1.00 26.47  ? 776  ARG A NE  1 
ATOM   5809 C CZ  . ARG A  1 749 ? 1.471   -33.458 83.043  1.00 35.74  ? 776  ARG A CZ  1 
ATOM   5810 N NH1 . ARG A  1 749 ? 2.653   -32.913 82.780  1.00 28.41  1 776  ARG A NH1 1 
ATOM   5811 N NH2 . ARG A  1 749 ? 0.527   -32.732 83.627  1.00 40.49  ? 776  ARG A NH2 1 
ATOM   5812 N N   . ASN A  1 750 ? -2.133  -38.296 83.031  1.00 32.23  ? 777  ASN A N   1 
ATOM   5813 C CA  . ASN A  1 750 ? -3.004  -38.486 84.191  1.00 37.01  ? 777  ASN A CA  1 
ATOM   5814 C C   . ASN A  1 750 ? -3.502  -39.920 84.370  1.00 38.83  ? 777  ASN A C   1 
ATOM   5815 O O   . ASN A  1 750 ? -4.095  -40.249 85.396  1.00 42.94  ? 777  ASN A O   1 
ATOM   5816 C CB  . ASN A  1 750 ? -4.189  -37.515 84.142  1.00 35.16  ? 777  ASN A CB  1 
ATOM   5817 C CG  . ASN A  1 750 ? -3.814  -36.113 84.597  1.00 47.53  ? 777  ASN A CG  1 
ATOM   5818 O OD1 . ASN A  1 750 ? -4.053  -35.737 85.747  1.00 48.56  ? 777  ASN A OD1 1 
ATOM   5819 N ND2 . ASN A  1 750 ? -3.218  -35.335 83.696  1.00 40.10  ? 777  ASN A ND2 1 
ATOM   5820 N N   . GLU A  1 751 ? -3.252  -40.766 83.374  1.00 38.42  ? 778  GLU A N   1 
ATOM   5821 C CA  . GLU A  1 751 ? -3.706  -42.153 83.398  1.00 38.72  ? 778  GLU A CA  1 
ATOM   5822 C C   . GLU A  1 751 ? -2.567  -43.126 83.675  1.00 36.10  ? 778  GLU A C   1 
ATOM   5823 O O   . GLU A  1 751 ? -2.803  -44.316 83.869  1.00 42.03  ? 778  GLU A O   1 
ATOM   5824 C CB  . GLU A  1 751 ? -4.387  -42.521 82.075  1.00 40.94  ? 778  GLU A CB  1 
ATOM   5825 C CG  . GLU A  1 751 ? -5.728  -41.836 81.840  1.00 40.66  ? 778  GLU A CG  1 
ATOM   5826 C CD  . GLU A  1 751 ? -6.829  -42.389 82.726  1.00 52.51  ? 778  GLU A CD  1 
ATOM   5827 O OE1 . GLU A  1 751 ? -6.959  -41.927 83.881  1.00 45.16  ? 778  GLU A OE1 1 
ATOM   5828 O OE2 . GLU A  1 751 ? -7.565  -43.289 82.266  1.00 60.68  1 778  GLU A OE2 1 
ATOM   5829 N N   . MET A  1 752 ? -1.336  -42.624 83.687  1.00 33.10  ? 779  MET A N   1 
ATOM   5830 C CA  . MET A  1 752 ? -0.179  -43.472 83.964  1.00 32.70  ? 779  MET A CA  1 
ATOM   5831 C C   . MET A  1 752 ? -0.149  -43.925 85.423  1.00 35.06  ? 779  MET A C   1 
ATOM   5832 O O   . MET A  1 752 ? -0.268  -43.109 86.341  1.00 32.79  ? 779  MET A O   1 
ATOM   5833 C CB  . MET A  1 752 ? 1.118   -42.754 83.607  1.00 26.99  ? 779  MET A CB  1 
ATOM   5834 C CG  . MET A  1 752 ? 1.233   -42.401 82.143  1.00 24.08  ? 779  MET A CG  1 
ATOM   5835 S SD  . MET A  1 752 ? 2.807   -41.620 81.756  1.00 21.06  ? 779  MET A SD  1 
ATOM   5836 C CE  . MET A  1 752 ? 3.943   -42.963 82.085  1.00 19.40  ? 779  MET A CE  1 
ATOM   5837 N N   . MET A  1 753 ? 0.027   -45.228 85.622  1.00 33.69  ? 780  MET A N   1 
ATOM   5838 C CA  . MET A  1 753 ? -0.116  -45.837 86.938  1.00 33.77  ? 780  MET A CA  1 
ATOM   5839 C C   . MET A  1 753 ? 1.159   -46.487 87.460  1.00 38.88  ? 780  MET A C   1 
ATOM   5840 O O   . MET A  1 753 ? 2.016   -46.902 86.684  1.00 35.81  ? 780  MET A O   1 
ATOM   5841 C CB  . MET A  1 753 ? -1.219  -46.887 86.894  1.00 30.46  ? 780  MET A CB  1 
ATOM   5842 C CG  . MET A  1 753 ? -2.580  -46.318 86.604  1.00 33.32  ? 780  MET A CG  1 
ATOM   5843 S SD  . MET A  1 753 ? -3.080  -45.240 87.943  1.00 37.08  ? 780  MET A SD  1 
ATOM   5844 C CE  . MET A  1 753 ? -2.839  -46.336 89.338  1.00 44.43  ? 780  MET A CE  1 
ATOM   5845 N N   . CYS A  1 754 ? 1.262   -46.579 88.784  1.00 44.21  ? 781  CYS A N   1 
ATOM   5846 C CA  . CYS A  1 754 ? 2.355   -47.288 89.446  1.00 43.14  ? 781  CYS A CA  1 
ATOM   5847 C C   . CYS A  1 754 ? 1.878   -48.633 89.995  1.00 55.86  ? 781  CYS A C   1 
ATOM   5848 O O   . CYS A  1 754 ? 0.678   -48.843 90.186  1.00 58.04  ? 781  CYS A O   1 
ATOM   5849 C CB  . CYS A  1 754 ? 2.939   -46.441 90.575  1.00 38.07  ? 781  CYS A CB  1 
ATOM   5850 S SG  . CYS A  1 754 ? 3.967   -45.065 90.022  1.00 44.98  ? 781  CYS A SG  1 
ATOM   5851 N N   . VAL A  1 755 ? 2.817   -49.540 90.250  1.00 55.09  ? 782  VAL A N   1 
ATOM   5852 C CA  . VAL A  1 755 ? 2.473   -50.885 90.712  1.00 59.23  ? 782  VAL A CA  1 
ATOM   5853 C C   . VAL A  1 755 ? 3.204   -51.272 91.998  1.00 63.34  ? 782  VAL A C   1 
ATOM   5854 O O   . VAL A  1 755 ? 3.671   -52.403 92.147  1.00 63.10  ? 782  VAL A O   1 
ATOM   5855 C CB  . VAL A  1 755 ? 2.746   -51.948 89.621  1.00 56.78  ? 782  VAL A CB  1 
ATOM   5856 C CG1 . VAL A  1 755 ? 1.715   -51.840 88.500  1.00 55.45  ? 782  VAL A CG1 1 
ATOM   5857 C CG2 . VAL A  1 755 ? 4.163   -51.813 89.077  1.00 45.22  ? 782  VAL A CG2 1 
ATOM   5858 N N   . ASN A  1 756 ? 3.286   -50.332 92.933  1.00 64.31  ? 783  ASN A N   1 
ATOM   5859 C CA  . ASN A  1 756 ? 4.022   -50.560 94.169  1.00 60.53  ? 783  ASN A CA  1 
ATOM   5860 C C   . ASN A  1 756 ? 3.149   -50.478 95.421  1.00 65.93  ? 783  ASN A C   1 
ATOM   5861 O O   . ASN A  1 756 ? 3.512   -49.819 96.394  1.00 69.55  ? 783  ASN A O   1 
ATOM   5862 C CB  . ASN A  1 756 ? 5.194   -49.579 94.271  1.00 61.16  ? 783  ASN A CB  1 
ATOM   5863 C CG  . ASN A  1 756 ? 6.189   -49.733 93.128  1.00 54.63  ? 783  ASN A CG  1 
ATOM   5864 O OD1 . ASN A  1 756 ? 6.488   -50.846 92.693  1.00 51.70  ? 783  ASN A OD1 1 
ATOM   5865 N ND2 . ASN A  1 756 ? 6.703   -48.612 92.638  1.00 44.04  ? 783  ASN A ND2 1 
ATOM   5866 N N   . ALA A  1 757 ? 2.001   -51.151 95.388  1.00 72.15  ? 784  ALA A N   1 
ATOM   5867 C CA  . ALA A  1 757 ? 1.096   -51.200 96.536  1.00 64.07  ? 784  ALA A CA  1 
ATOM   5868 C C   . ALA A  1 757 ? 0.244   -52.464 96.512  1.00 62.90  ? 784  ALA A C   1 
ATOM   5869 O O   . ALA A  1 757 ? 0.354   -53.280 95.597  1.00 68.56  ? 784  ALA A O   1 
ATOM   5870 C CB  . ALA A  1 757 ? 0.210   -49.963 96.579  1.00 54.11  ? 784  ALA A CB  1 
ATOM   5871 N N   . PRO A  1 760 ? -1.511  -49.327 93.901  1.00 68.09  ? 787  PRO A N   1 
ATOM   5872 C CA  . PRO A  1 760 ? -1.297  -48.505 92.708  1.00 57.77  ? 787  PRO A CA  1 
ATOM   5873 C C   . PRO A  1 760 ? -1.809  -47.078 92.875  1.00 52.60  ? 787  PRO A C   1 
ATOM   5874 O O   . PRO A  1 760 ? -2.920  -46.862 93.361  1.00 53.40  ? 787  PRO A O   1 
ATOM   5875 C CB  . PRO A  1 760 ? -2.115  -49.235 91.644  1.00 53.78  ? 787  PRO A CB  1 
ATOM   5876 C CG  . PRO A  1 760 ? -2.021  -50.664 92.046  1.00 62.04  ? 787  PRO A CG  1 
ATOM   5877 C CD  . PRO A  1 760 ? -2.007  -50.672 93.558  1.00 67.90  ? 787  PRO A CD  1 
ATOM   5878 N N   . THR A  1 761 ? -0.989  -46.113 92.477  1.00 46.58  ? 788  THR A N   1 
ATOM   5879 C CA  . THR A  1 761 ? -1.391  -44.715 92.471  1.00 46.72  ? 788  THR A CA  1 
ATOM   5880 C C   . THR A  1 761 ? -0.987  -44.087 91.148  1.00 39.66  ? 788  THR A C   1 
ATOM   5881 O O   . THR A  1 761 ? -0.003  -44.508 90.538  1.00 39.35  ? 788  THR A O   1 
ATOM   5882 C CB  . THR A  1 761 ? -0.718  -43.926 93.603  1.00 45.84  ? 788  THR A CB  1 
ATOM   5883 O OG1 . THR A  1 761 ? 0.701   -44.111 93.530  1.00 40.40  ? 788  THR A OG1 1 
ATOM   5884 C CG2 . THR A  1 761 ? -1.223  -44.394 94.961  1.00 46.23  ? 788  THR A CG2 1 
ATOM   5885 N N   . ARG A  1 762 ? -1.751  -43.092 90.706  1.00 36.46  ? 789  ARG A N   1 
ATOM   5886 C CA  . ARG A  1 762 ? -1.402  -42.333 89.512  1.00 36.21  ? 789  ARG A CA  1 
ATOM   5887 C C   . ARG A  1 762 ? 0.026   -41.827 89.630  1.00 37.56  ? 789  ARG A C   1 
ATOM   5888 O O   . ARG A  1 762 ? 0.470   -41.438 90.712  1.00 38.28  ? 789  ARG A O   1 
ATOM   5889 C CB  . ARG A  1 762 ? -2.337  -41.139 89.336  1.00 39.75  ? 789  ARG A CB  1 
ATOM   5890 C CG  . ARG A  1 762 ? -3.798  -41.486 89.116  1.00 46.18  ? 789  ARG A CG  1 
ATOM   5891 C CD  . ARG A  1 762 ? -4.618  -40.210 89.044  1.00 47.22  ? 789  ARG A CD  1 
ATOM   5892 N NE  . ARG A  1 762 ? -4.366  -39.368 90.213  1.00 59.38  ? 789  ARG A NE  1 
ATOM   5893 C CZ  . ARG A  1 762 ? -4.459  -38.041 90.223  1.00 59.60  ? 789  ARG A CZ  1 
ATOM   5894 N NH1 . ARG A  1 762 ? -4.795  -37.384 89.118  1.00 58.37  1 789  ARG A NH1 1 
ATOM   5895 N NH2 . ARG A  1 762 ? -4.211  -37.370 91.341  1.00 47.54  ? 789  ARG A NH2 1 
ATOM   5896 N N   . MET A  1 763 ? 0.750   -41.835 88.520  1.00 33.56  ? 790  MET A N   1 
ATOM   5897 C CA  . MET A  1 763 ? 2.130   -41.388 88.542  1.00 27.58  ? 790  MET A CA  1 
ATOM   5898 C C   . MET A  1 763 ? 2.197   -39.876 88.709  1.00 28.61  ? 790  MET A C   1 
ATOM   5899 O O   . MET A  1 763 ? 3.195   -39.339 89.178  1.00 28.82  ? 790  MET A O   1 
ATOM   5900 C CB  . MET A  1 763 ? 2.846   -41.815 87.270  1.00 22.48  ? 790  MET A CB  1 
ATOM   5901 C CG  . MET A  1 763 ? 4.343   -41.724 87.362  1.00 18.39  ? 790  MET A CG  1 
ATOM   5902 S SD  . MET A  1 763 ? 5.120   -42.424 85.903  1.00 21.98  ? 790  MET A SD  1 
ATOM   5903 C CE  . MET A  1 763 ? 4.292   -44.012 85.824  1.00 25.68  ? 790  MET A CE  1 
ATOM   5904 N N   . VAL A  1 764 ? 1.123   -39.191 88.332  1.00 34.32  ? 791  VAL A N   1 
ATOM   5905 C CA  . VAL A  1 764 ? 1.061   -37.741 88.473  1.00 35.29  ? 791  VAL A CA  1 
ATOM   5906 C C   . VAL A  1 764 ? 0.660   -37.362 89.893  1.00 37.28  ? 791  VAL A C   1 
ATOM   5907 O O   . VAL A  1 764 ? 0.313   -36.212 90.169  1.00 42.42  ? 791  VAL A O   1 
ATOM   5908 C CB  . VAL A  1 764 ? 0.079   -37.106 87.471  1.00 35.33  ? 791  VAL A CB  1 
ATOM   5909 C CG1 . VAL A  1 764 ? 0.477   -37.468 86.050  1.00 35.83  ? 791  VAL A CG1 1 
ATOM   5910 C CG2 . VAL A  1 764 ? -1.347  -37.551 87.762  1.00 38.37  ? 791  VAL A CG2 1 
ATOM   5911 N N   . GLU A  1 765 ? 0.704   -38.346 90.784  1.00 30.53  ? 792  GLU A N   1 
ATOM   5912 C CA  . GLU A  1 765 ? 0.448   -38.132 92.196  1.00 29.40  ? 792  GLU A CA  1 
ATOM   5913 C C   . GLU A  1 765 ? 1.752   -38.387 92.937  1.00 34.27  ? 792  GLU A C   1 
ATOM   5914 O O   . GLU A  1 765 ? 1.802   -38.381 94.167  1.00 33.92  ? 792  GLU A O   1 
ATOM   5915 C CB  . GLU A  1 765 ? -0.623  -39.103 92.678  1.00 31.87  ? 792  GLU A CB  1 
ATOM   5916 C CG  . GLU A  1 765 ? -1.832  -38.449 93.305  1.00 32.97  ? 792  GLU A CG  1 
ATOM   5917 C CD  . GLU A  1 765 ? -2.894  -39.462 93.692  1.00 44.85  ? 792  GLU A CD  1 
ATOM   5918 O OE1 . GLU A  1 765 ? -2.672  -40.229 94.655  1.00 49.41  ? 792  GLU A OE1 1 
ATOM   5919 O OE2 . GLU A  1 765 ? -3.949  -39.496 93.024  1.00 41.59  1 792  GLU A OE2 1 
ATOM   5920 N N   . LEU A  1 766 ? 2.809   -38.615 92.164  1.00 35.05  ? 793  LEU A N   1 
ATOM   5921 C CA  . LEU A  1 766 ? 4.110   -38.996 92.704  1.00 32.55  ? 793  LEU A CA  1 
ATOM   5922 C C   . LEU A  1 766 ? 5.129   -37.874 92.576  1.00 34.54  ? 793  LEU A C   1 
ATOM   5923 O O   . LEU A  1 766 ? 5.046   -37.042 91.673  1.00 35.10  ? 793  LEU A O   1 
ATOM   5924 C CB  . LEU A  1 766 ? 4.641   -40.240 91.987  1.00 30.83  ? 793  LEU A CB  1 
ATOM   5925 C CG  . LEU A  1 766 ? 4.271   -41.628 92.519  1.00 34.95  ? 793  LEU A CG  1 
ATOM   5926 C CD1 . LEU A  1 766 ? 5.184   -42.011 93.671  1.00 38.69  ? 793  LEU A CD1 1 
ATOM   5927 C CD2 . LEU A  1 766 ? 2.804   -41.707 92.943  1.00 29.38  ? 793  LEU A CD2 1 
ATOM   5928 N N   . SER A  1 767 ? 6.093   -37.866 93.492  1.00 38.75  ? 794  SER A N   1 
ATOM   5929 C CA  . SER A  1 767 ? 7.205   -36.928 93.451  1.00 34.05  ? 794  SER A CA  1 
ATOM   5930 C C   . SER A  1 767 ? 8.464   -37.690 93.068  1.00 36.32  ? 794  SER A C   1 
ATOM   5931 O O   . SER A  1 767 ? 8.447   -38.917 92.979  1.00 39.27  ? 794  SER A O   1 
ATOM   5932 C CB  . SER A  1 767 ? 7.391   -36.265 94.816  1.00 31.50  ? 794  SER A CB  1 
ATOM   5933 O OG  . SER A  1 767 ? 8.520   -35.412 94.822  1.00 31.85  ? 794  SER A OG  1 
ATOM   5934 N N   . THR A  1 768 ? 9.558   -36.969 92.846  1.00 34.45  ? 795  THR A N   1 
ATOM   5935 C CA  . THR A  1 768 ? 10.824  -37.608 92.512  1.00 29.70  ? 795  THR A CA  1 
ATOM   5936 C C   . THR A  1 768 ? 11.570  -38.010 93.782  1.00 40.21  ? 795  THR A C   1 
ATOM   5937 O O   . THR A  1 768 ? 12.784  -38.217 93.760  1.00 43.14  ? 795  THR A O   1 
ATOM   5938 C CB  . THR A  1 768 ? 11.711  -36.676 91.683  1.00 22.94  ? 795  THR A CB  1 
ATOM   5939 O OG1 . THR A  1 768 ? 12.440  -35.806 92.554  1.00 28.84  ? 795  THR A OG1 1 
ATOM   5940 C CG2 . THR A  1 768 ? 10.864  -35.842 90.752  1.00 25.24  ? 795  THR A CG2 1 
ATOM   5941 N N   . ASN A  1 769 ? 10.835  -38.118 94.887  1.00 40.96  ? 796  ASN A N   1 
ATOM   5942 C CA  . ASN A  1 769 ? 11.420  -38.431 96.187  1.00 40.02  ? 796  ASN A CA  1 
ATOM   5943 C C   . ASN A  1 769 ? 10.655  -39.520 96.927  1.00 41.46  ? 796  ASN A C   1 
ATOM   5944 O O   . ASN A  1 769 ? 11.198  -40.164 97.823  1.00 44.41  ? 796  ASN A O   1 
ATOM   5945 C CB  . ASN A  1 769 ? 11.512  -37.174 97.050  1.00 40.60  ? 796  ASN A CB  1 
ATOM   5946 C CG  . ASN A  1 769 ? 12.476  -36.152 96.484  1.00 44.42  ? 796  ASN A CG  1 
ATOM   5947 O OD1 . ASN A  1 769 ? 13.609  -36.483 96.125  1.00 49.45  ? 796  ASN A OD1 1 
ATOM   5948 N ND2 . ASN A  1 769 ? 12.026  -34.902 96.389  1.00 34.95  ? 796  ASN A ND2 1 
ATOM   5949 N N   . ASP A  1 770 ? 9.392   -39.714 96.557  1.00 42.02  ? 797  ASP A N   1 
ATOM   5950 C CA  . ASP A  1 770 ? 8.622   -40.854 97.045  1.00 44.81  ? 797  ASP A CA  1 
ATOM   5951 C C   . ASP A  1 770 ? 9.283   -42.112 96.497  1.00 39.65  ? 797  ASP A C   1 
ATOM   5952 O O   . ASP A  1 770 ? 9.232   -43.185 97.102  1.00 33.59  ? 797  ASP A O   1 
ATOM   5953 C CB  . ASP A  1 770 ? 7.170   -40.798 96.548  1.00 42.41  ? 797  ASP A CB  1 
ATOM   5954 C CG  . ASP A  1 770 ? 6.409   -39.587 97.062  1.00 40.53  ? 797  ASP A CG  1 
ATOM   5955 O OD1 . ASP A  1 770 ? 5.986   -39.602 98.238  1.00 49.49  ? 797  ASP A OD1 1 
ATOM   5956 O OD2 . ASP A  1 770 ? 6.211   -38.631 96.283  1.00 36.12  1 797  ASP A OD2 1 
ATOM   5957 N N   . ILE A  1 771 ? 9.903   -41.950 95.334  1.00 35.85  ? 798  ILE A N   1 
ATOM   5958 C CA  . ILE A  1 771 ? 10.530  -43.039 94.611  1.00 37.48  ? 798  ILE A CA  1 
ATOM   5959 C C   . ILE A  1 771 ? 12.034  -43.052 94.846  1.00 46.45  ? 798  ILE A C   1 
ATOM   5960 O O   . ILE A  1 771 ? 12.687  -44.089 94.714  1.00 46.28  ? 798  ILE A O   1 
ATOM   5961 C CB  . ILE A  1 771 ? 10.293  -42.873 93.109  1.00 39.47  ? 798  ILE A CB  1 
ATOM   5962 C CG1 . ILE A  1 771 ? 10.537  -41.415 92.710  1.00 37.29  ? 798  ILE A CG1 1 
ATOM   5963 C CG2 . ILE A  1 771 ? 8.881   -43.281 92.748  1.00 38.81  ? 798  ILE A CG2 1 
ATOM   5964 C CD1 . ILE A  1 771 ? 10.442  -41.158 91.231  1.00 34.18  ? 798  ILE A CD1 1 
ATOM   5965 N N   . CYS A  1 772 ? 12.582  -41.893 95.194  1.00 49.73  ? 799  CYS A N   1 
ATOM   5966 C CA  . CYS A  1 772 ? 14.026  -41.751 95.325  1.00 53.16  ? 799  CYS A CA  1 
ATOM   5967 C C   . CYS A  1 772 ? 14.451  -41.268 96.710  1.00 55.66  ? 799  CYS A C   1 
ATOM   5968 O O   . CYS A  1 772 ? 14.234  -40.106 97.063  1.00 55.87  ? 799  CYS A O   1 
ATOM   5969 C CB  . CYS A  1 772 ? 14.565  -40.802 94.249  1.00 49.84  ? 799  CYS A CB  1 
ATOM   5970 S SG  . CYS A  1 772 ? 15.996  -41.436 93.346  1.00 47.80  ? 799  CYS A SG  1 
ATOM   5971 N N   . PRO A  1 773 ? 15.045  -42.172 97.505  1.00 52.76  ? 800  PRO A N   1 
ATOM   5972 C CA  . PRO A  1 773 ? 15.689  -41.806 98.771  1.00 56.74  ? 800  PRO A CA  1 
ATOM   5973 C C   . PRO A  1 773 ? 16.877  -40.865 98.551  1.00 51.25  ? 800  PRO A C   1 
ATOM   5974 O O   . PRO A  1 773 ? 16.687  -39.680 98.267  1.00 39.46  ? 800  PRO A O   1 
ATOM   5975 C CB  . PRO A  1 773 ? 16.179  -43.154 99.312  1.00 55.75  ? 800  PRO A CB  1 
ATOM   5976 C CG  . PRO A  1 773 ? 15.260  -44.159 98.704  1.00 49.05  ? 800  PRO A CG  1 
ATOM   5977 C CD  . PRO A  1 773 ? 14.956  -43.633 97.333  1.00 50.27  ? 800  PRO A CD  1 
ATOM   5978 N N   . ASP B  2 5   ? -48.615 -36.756 28.827  1.00 41.94  ? 5    ASP J N   1 
ATOM   5979 C CA  . ASP B  2 5   ? -48.879 -37.368 27.530  1.00 58.80  ? 5    ASP J CA  1 
ATOM   5980 C C   . ASP B  2 5   ? -49.736 -36.440 26.667  1.00 57.40  ? 5    ASP J C   1 
ATOM   5981 O O   . ASP B  2 5   ? -50.714 -36.867 26.048  1.00 44.21  ? 5    ASP J O   1 
ATOM   5982 C CB  . ASP B  2 5   ? -49.560 -38.731 27.710  1.00 57.29  ? 5    ASP J CB  1 
ATOM   5983 C CG  . ASP B  2 5   ? -49.615 -39.539 26.421  1.00 55.88  ? 5    ASP J CG  1 
ATOM   5984 O OD1 . ASP B  2 5   ? -49.113 -39.055 25.383  1.00 54.62  1 5    ASP J OD1 1 
ATOM   5985 O OD2 . ASP B  2 5   ? -50.155 -40.666 26.449  1.00 54.67  ? 5    ASP J OD2 1 
ATOM   5986 N N   . GLU B  2 6   ? -49.358 -35.165 26.635  1.00 49.96  ? 6    GLU J N   1 
ATOM   5987 C CA  . GLU B  2 6   ? -50.101 -34.155 25.892  1.00 38.43  ? 6    GLU J CA  1 
ATOM   5988 C C   . GLU B  2 6   ? -49.178 -33.054 25.380  1.00 38.67  ? 6    GLU J C   1 
ATOM   5989 O O   . GLU B  2 6   ? -48.130 -32.791 25.963  1.00 45.22  ? 6    GLU J O   1 
ATOM   5990 C CB  . GLU B  2 6   ? -51.207 -33.558 26.772  1.00 39.27  ? 6    GLU J CB  1 
ATOM   5991 C CG  . GLU B  2 6   ? -52.424 -34.470 26.950  1.00 46.82  ? 6    GLU J CG  1 
ATOM   5992 C CD  . GLU B  2 6   ? -53.378 -33.996 28.032  1.00 50.07  ? 6    GLU J CD  1 
ATOM   5993 O OE1 . GLU B  2 6   ? -53.014 -33.062 28.782  1.00 44.39  ? 6    GLU J OE1 1 
ATOM   5994 O OE2 . GLU B  2 6   ? -54.493 -34.563 28.129  1.00 39.91  1 6    GLU J OE2 1 
ATOM   5995 N N   . ARG B  2 7   ? -49.566 -32.424 24.276  1.00 40.79  ? 7    ARG J N   1 
ATOM   5996 C CA  . ARG B  2 7   ? -48.851 -31.262 23.757  1.00 34.37  ? 7    ARG J CA  1 
ATOM   5997 C C   . ARG B  2 7   ? -49.867 -30.187 23.377  1.00 31.09  ? 7    ARG J C   1 
ATOM   5998 O O   . ARG B  2 7   ? -50.931 -30.494 22.843  1.00 33.57  ? 7    ARG J O   1 
ATOM   5999 C CB  . ARG B  2 7   ? -47.982 -31.646 22.553  1.00 32.83  ? 7    ARG J CB  1 
ATOM   6000 C CG  . ARG B  2 7   ? -47.174 -30.494 21.962  1.00 32.13  ? 7    ARG J CG  1 
ATOM   6001 C CD  . ARG B  2 7   ? -46.178 -30.988 20.924  1.00 34.85  ? 7    ARG J CD  1 
ATOM   6002 N NE  . ARG B  2 7   ? -45.621 -29.900 20.122  1.00 35.38  ? 7    ARG J NE  1 
ATOM   6003 C CZ  . ARG B  2 7   ? -45.293 -30.015 18.836  1.00 35.97  ? 7    ARG J CZ  1 
ATOM   6004 N NH1 . ARG B  2 7   ? -45.467 -31.170 18.206  1.00 30.60  1 7    ARG J NH1 1 
ATOM   6005 N NH2 . ARG B  2 7   ? -44.795 -28.979 18.173  1.00 32.80  ? 7    ARG J NH2 1 
ATOM   6006 N N   . PHE B  2 8   ? -49.544 -28.930 23.667  1.00 28.70  ? 8    PHE J N   1 
ATOM   6007 C CA  . PHE B  2 8   ? -50.456 -27.823 23.389  1.00 28.05  ? 8    PHE J CA  1 
ATOM   6008 C C   . PHE B  2 8   ? -49.956 -26.951 22.240  1.00 30.66  ? 8    PHE J C   1 
ATOM   6009 O O   . PHE B  2 8   ? -48.751 -26.842 22.013  1.00 40.34  ? 8    PHE J O   1 
ATOM   6010 C CB  . PHE B  2 8   ? -50.696 -26.998 24.656  1.00 28.64  ? 8    PHE J CB  1 
ATOM   6011 C CG  . PHE B  2 8   ? -51.509 -27.723 25.693  1.00 33.45  ? 8    PHE J CG  1 
ATOM   6012 C CD1 . PHE B  2 8   ? -50.962 -28.768 26.414  1.00 28.94  ? 8    PHE J CD1 1 
ATOM   6013 C CD2 . PHE B  2 8   ? -52.826 -27.372 25.931  1.00 39.06  ? 8    PHE J CD2 1 
ATOM   6014 C CE1 . PHE B  2 8   ? -51.708 -29.446 27.355  1.00 31.05  ? 8    PHE J CE1 1 
ATOM   6015 C CE2 . PHE B  2 8   ? -53.579 -28.046 26.874  1.00 33.62  ? 8    PHE J CE2 1 
ATOM   6016 C CZ  . PHE B  2 8   ? -53.017 -29.085 27.585  1.00 35.91  ? 8    PHE J CZ  1 
ATOM   6017 N N   . LEU B  2 9   ? -50.889 -26.337 21.519  1.00 25.82  ? 9    LEU J N   1 
ATOM   6018 C CA  . LEU B  2 9   ? -50.574 -25.587 20.299  1.00 22.68  ? 9    LEU J CA  1 
ATOM   6019 C C   . LEU B  2 9   ? -49.600 -24.426 20.525  1.00 22.12  ? 9    LEU J C   1 
ATOM   6020 O O   . LEU B  2 9   ? -48.918 -23.983 19.600  1.00 17.47  ? 9    LEU J O   1 
ATOM   6021 C CB  . LEU B  2 9   ? -51.860 -25.073 19.640  1.00 21.71  ? 9    LEU J CB  1 
ATOM   6022 C CG  . LEU B  2 9   ? -52.770 -26.090 18.943  1.00 21.30  ? 9    LEU J CG  1 
ATOM   6023 C CD1 . LEU B  2 9   ? -51.976 -26.967 17.988  1.00 22.85  ? 9    LEU J CD1 1 
ATOM   6024 C CD2 . LEU B  2 9   ? -53.533 -26.947 19.940  1.00 27.56  ? 9    LEU J CD2 1 
ATOM   6025 N N   . CYS B  2 10  ? -49.551 -23.938 21.760  1.00 25.78  ? 10   CYS J N   1 
ATOM   6026 C CA  . CYS B  2 10  ? -48.636 -22.876 22.141  1.00 21.92  ? 10   CYS J CA  1 
ATOM   6027 C C   . CYS B  2 10  ? -47.770 -23.320 23.308  1.00 33.72  ? 10   CYS J C   1 
ATOM   6028 O O   . CYS B  2 10  ? -48.264 -23.484 24.423  1.00 43.15  ? 10   CYS J O   1 
ATOM   6029 C CB  . CYS B  2 10  ? -49.412 -21.629 22.541  1.00 18.05  ? 10   CYS J CB  1 
ATOM   6030 S SG  . CYS B  2 10  ? -49.338 -20.322 21.330  1.00 14.25  ? 10   CYS J SG  1 
ATOM   6031 N N   . ARG B  2 11  ? -46.482 -23.520 23.051  1.00 37.88  ? 11   ARG J N   1 
ATOM   6032 C CA  . ARG B  2 11  ? -45.541 -23.841 24.116  1.00 38.17  ? 11   ARG J CA  1 
ATOM   6033 C C   . ARG B  2 11  ? -45.460 -22.683 25.101  1.00 30.38  ? 11   ARG J C   1 
ATOM   6034 O O   . ARG B  2 11  ? -45.239 -21.538 24.712  1.00 29.27  ? 11   ARG J O   1 
ATOM   6035 C CB  . ARG B  2 11  ? -44.152 -24.164 23.549  1.00 42.08  ? 11   ARG J CB  1 
ATOM   6036 C CG  . ARG B  2 11  ? -44.079 -25.492 22.802  1.00 43.35  ? 11   ARG J CG  1 
ATOM   6037 C CD  . ARG B  2 11  ? -42.664 -26.062 22.792  1.00 48.37  ? 11   ARG J CD  1 
ATOM   6038 N NE  . ARG B  2 11  ? -42.673 -27.522 22.682  1.00 65.70  ? 11   ARG J NE  1 
ATOM   6039 C CZ  . ARG B  2 11  ? -41.598 -28.298 22.807  1.00 57.35  ? 11   ARG J CZ  1 
ATOM   6040 N NH1 . ARG B  2 11  ? -40.408 -27.762 23.048  1.00 44.97  1 11   ARG J NH1 1 
ATOM   6041 N NH2 . ARG B  2 11  ? -41.714 -29.616 22.692  1.00 50.80  ? 11   ARG J NH2 1 
ATOM   6042 N N   . SER B  2 12  ? -45.660 -22.986 26.377  1.00 35.07  ? 12   SER J N   1 
ATOM   6043 C CA  . SER B  2 12  ? -45.562 -21.977 27.422  1.00 41.38  ? 12   SER J CA  1 
ATOM   6044 C C   . SER B  2 12  ? -44.643 -22.447 28.550  1.00 45.56  ? 12   SER J C   1 
ATOM   6045 O O   . SER B  2 12  ? -44.070 -23.538 28.491  1.00 40.70  ? 12   SER J O   1 
ATOM   6046 C CB  . SER B  2 12  ? -46.948 -21.636 27.973  1.00 36.22  ? 12   SER J CB  1 
ATOM   6047 O OG  . SER B  2 12  ? -47.447 -22.686 28.781  1.00 35.98  ? 12   SER J OG  1 
ATOM   6048 N N   . ILE B  2 13  ? -44.502 -21.617 29.577  1.00 47.83  ? 13   ILE J N   1 
ATOM   6049 C CA  . ILE B  2 13  ? -43.650 -21.947 30.716  1.00 55.19  ? 13   ILE J CA  1 
ATOM   6050 C C   . ILE B  2 13  ? -44.278 -21.502 32.045  1.00 55.85  ? 13   ILE J C   1 
ATOM   6051 O O   . ILE B  2 13  ? -44.161 -20.344 32.457  1.00 56.69  ? 13   ILE J O   1 
ATOM   6052 C CB  . ILE B  2 13  ? -42.207 -21.384 30.538  1.00 60.22  ? 13   ILE J CB  1 
ATOM   6053 C CG1 . ILE B  2 13  ? -41.387 -21.555 31.820  1.00 59.67  ? 13   ILE J CG1 1 
ATOM   6054 C CG2 . ILE B  2 13  ? -42.230 -19.925 30.082  1.00 52.53  ? 13   ILE J CG2 1 
ATOM   6055 C CD1 . ILE B  2 13  ? -41.172 -23.002 32.222  1.00 65.42  ? 13   ILE J CD1 1 
ATOM   6056 N N   . ARG B  2 14  ? -44.958 -22.433 32.707  1.00 57.02  ? 14   ARG J N   1 
ATOM   6057 C CA  . ARG B  2 14  ? -45.637 -22.119 33.956  1.00 57.95  ? 14   ARG J CA  1 
ATOM   6058 C C   . ARG B  2 14  ? -44.617 -21.860 35.058  1.00 66.49  ? 14   ARG J C   1 
ATOM   6059 O O   . ARG B  2 14  ? -43.528 -22.434 35.054  1.00 64.22  ? 14   ARG J O   1 
ATOM   6060 C CB  . ARG B  2 14  ? -46.606 -23.233 34.362  1.00 61.62  ? 14   ARG J CB  1 
ATOM   6061 C CG  . ARG B  2 14  ? -45.929 -24.542 34.731  1.00 77.02  ? 14   ARG J CG  1 
ATOM   6062 C CD  . ARG B  2 14  ? -46.858 -25.443 35.539  1.00 85.02  ? 14   ARG J CD  1 
ATOM   6063 N NE  . ARG B  2 14  ? -46.151 -26.590 36.107  1.00 85.35  ? 14   ARG J NE  1 
ATOM   6064 C CZ  . ARG B  2 14  ? -45.502 -26.569 37.268  1.00 76.98  ? 14   ARG J CZ  1 
ATOM   6065 N NH1 . ARG B  2 14  ? -45.464 -25.456 37.990  1.00 73.97  1 14   ARG J NH1 1 
ATOM   6066 N NH2 . ARG B  2 14  ? -44.885 -27.659 37.706  1.00 70.75  ? 14   ARG J NH2 1 
ATOM   6067 N N   . LYS B  2 15  ? -44.973 -20.986 35.994  1.00 69.83  ? 15   LYS J N   1 
ATOM   6068 C CA  . LYS B  2 15  ? -44.049 -20.568 37.041  1.00 64.95  ? 15   LYS J CA  1 
ATOM   6069 C C   . LYS B  2 15  ? -44.730 -20.571 38.412  1.00 67.52  ? 15   LYS J C   1 
ATOM   6070 O O   . LYS B  2 15  ? -45.839 -21.091 38.566  1.00 58.46  ? 15   LYS J O   1 
ATOM   6071 C CB  . LYS B  2 15  ? -43.488 -19.180 36.714  1.00 58.57  ? 15   LYS J CB  1 
ATOM   6072 C CG  . LYS B  2 15  ? -42.042 -18.964 37.122  1.00 61.01  ? 15   LYS J CG  1 
ATOM   6073 C CD  . LYS B  2 15  ? -41.460 -17.730 36.449  1.00 61.32  ? 15   LYS J CD  1 
ATOM   6074 C CE  . LYS B  2 15  ? -41.509 -17.862 34.932  1.00 67.90  ? 15   LYS J CE  1 
ATOM   6075 N NZ  . LYS B  2 15  ? -40.836 -16.726 34.240  1.00 67.38  1 15   LYS J NZ  1 
ATOM   6076 N N   . LEU B  2 16  ? -44.058 -19.989 39.402  1.00 73.63  ? 16   LEU J N   1 
ATOM   6077 C CA  . LEU B  2 16  ? -44.543 -19.988 40.775  1.00 67.29  ? 16   LEU J CA  1 
ATOM   6078 C C   . LEU B  2 16  ? -43.860 -18.872 41.551  1.00 57.95  ? 16   LEU J C   1 
ATOM   6079 O O   . LEU B  2 16  ? -42.957 -19.133 42.335  1.00 59.01  ? 16   LEU J O   1 
ATOM   6080 C CB  . LEU B  2 16  ? -44.227 -21.332 41.437  1.00 68.73  ? 16   LEU J CB  1 
ATOM   6081 C CG  . LEU B  2 16  ? -45.210 -21.932 42.448  1.00 75.29  ? 16   LEU J CG  1 
ATOM   6082 C CD1 . LEU B  2 16  ? -44.672 -23.257 42.997  1.00 60.93  ? 16   LEU J CD1 1 
ATOM   6083 C CD2 . LEU B  2 16  ? -45.525 -20.960 43.580  1.00 72.70  ? 16   LEU J CD2 1 
ATOM   6084 N N   . VAL B  2 17  ? -44.289 -17.632 41.337  1.00 66.56  ? 17   VAL J N   1 
ATOM   6085 C CA  . VAL B  2 17  ? -43.640 -16.491 41.981  1.00 72.72  ? 17   VAL J CA  1 
ATOM   6086 C C   . VAL B  2 17  ? -44.594 -15.590 42.777  1.00 75.40  ? 17   VAL J C   1 
ATOM   6087 O O   . VAL B  2 17  ? -45.755 -15.406 42.405  1.00 65.78  ? 17   VAL J O   1 
ATOM   6088 C CB  . VAL B  2 17  ? -42.855 -15.636 40.960  1.00 65.62  ? 17   VAL J CB  1 
ATOM   6089 C CG1 . VAL B  2 17  ? -41.654 -16.406 40.438  1.00 56.00  ? 17   VAL J CG1 1 
ATOM   6090 C CG2 . VAL B  2 17  ? -43.759 -15.201 39.817  1.00 57.68  ? 17   VAL J CG2 1 
ATOM   6091 N N   . TYR B  2 18  ? -44.085 -15.040 43.879  1.00 80.03  ? 18   TYR J N   1 
ATOM   6092 C CA  . TYR B  2 18  ? -44.839 -14.106 44.715  1.00 79.63  ? 18   TYR J CA  1 
ATOM   6093 C C   . TYR B  2 18  ? -44.163 -12.736 44.700  1.00 74.86  ? 18   TYR J C   1 
ATOM   6094 O O   . TYR B  2 18  ? -44.611 -11.813 44.020  1.00 73.98  ? 18   TYR J O   1 
ATOM   6095 C CB  . TYR B  2 18  ? -44.930 -14.609 46.162  1.00 73.18  ? 18   TYR J CB  1 
ATOM   6096 C CG  . TYR B  2 18  ? -45.863 -15.784 46.397  1.00 71.69  ? 18   TYR J CG  1 
ATOM   6097 C CD1 . TYR B  2 18  ? -45.869 -16.882 45.544  1.00 69.99  ? 18   TYR J CD1 1 
ATOM   6098 C CD2 . TYR B  2 18  ? -46.713 -15.808 47.497  1.00 65.80  ? 18   TYR J CD2 1 
ATOM   6099 C CE1 . TYR B  2 18  ? -46.708 -17.959 45.764  1.00 61.09  ? 18   TYR J CE1 1 
ATOM   6100 C CE2 . TYR B  2 18  ? -47.554 -16.885 47.727  1.00 62.58  ? 18   TYR J CE2 1 
ATOM   6101 C CZ  . TYR B  2 18  ? -47.545 -17.957 46.855  1.00 62.31  ? 18   TYR J CZ  1 
ATOM   6102 O OH  . TYR B  2 18  ? -48.375 -19.034 47.070  1.00 67.92  ? 18   TYR J OH  1 
ATOM   6103 N N   . ILE B  2 42  ? -48.037 -16.548 43.241  1.00 60.24  ? 42   ILE J N   1 
ATOM   6104 C CA  . ILE B  2 42  ? -49.061 -17.379 42.616  1.00 65.84  ? 42   ILE J CA  1 
ATOM   6105 C C   . ILE B  2 42  ? -48.495 -18.117 41.399  1.00 65.71  ? 42   ILE J C   1 
ATOM   6106 O O   . ILE B  2 42  ? -47.582 -17.624 40.731  1.00 60.50  ? 42   ILE J O   1 
ATOM   6107 C CB  . ILE B  2 42  ? -50.304 -16.540 42.211  1.00 50.03  ? 42   ILE J CB  1 
ATOM   6108 C CG1 . ILE B  2 42  ? -51.493 -17.444 41.875  1.00 44.44  ? 42   ILE J CG1 1 
ATOM   6109 C CG2 . ILE B  2 42  ? -49.979 -15.622 41.049  1.00 41.12  ? 42   ILE J CG2 1 
ATOM   6110 C CD1 . ILE B  2 42  ? -51.837 -18.441 42.967  1.00 53.43  ? 42   ILE J CD1 1 
ATOM   6111 N N   . GLN B  2 43  ? -49.024 -19.309 41.132  1.00 64.62  ? 43   GLN J N   1 
ATOM   6112 C CA  . GLN B  2 43  ? -48.625 -20.076 39.957  1.00 54.79  ? 43   GLN J CA  1 
ATOM   6113 C C   . GLN B  2 43  ? -49.031 -19.354 38.681  1.00 49.60  ? 43   GLN J C   1 
ATOM   6114 O O   . GLN B  2 43  ? -50.200 -19.022 38.490  1.00 58.45  ? 43   GLN J O   1 
ATOM   6115 C CB  . GLN B  2 43  ? -49.254 -21.467 39.978  1.00 49.75  ? 43   GLN J CB  1 
ATOM   6116 C CG  . GLN B  2 43  ? -49.256 -22.133 38.617  1.00 48.23  ? 43   GLN J CG  1 
ATOM   6117 C CD  . GLN B  2 43  ? -49.475 -23.624 38.691  1.00 49.17  ? 43   GLN J CD  1 
ATOM   6118 O OE1 . GLN B  2 43  ? -50.589 -24.095 38.932  1.00 44.71  ? 43   GLN J OE1 1 
ATOM   6119 N NE2 . GLN B  2 43  ? -48.407 -24.382 38.482  1.00 54.09  ? 43   GLN J NE2 1 
ATOM   6120 N N   . ILE B  2 44  ? -48.068 -19.108 37.803  1.00 43.55  ? 44   ILE J N   1 
ATOM   6121 C CA  . ILE B  2 44  ? -48.364 -18.390 36.573  1.00 43.72  ? 44   ILE J CA  1 
ATOM   6122 C C   . ILE B  2 44  ? -47.873 -19.125 35.324  1.00 50.47  ? 44   ILE J C   1 
ATOM   6123 O O   . ILE B  2 44  ? -46.702 -19.482 35.223  1.00 56.18  ? 44   ILE J O   1 
ATOM   6124 C CB  . ILE B  2 44  ? -47.799 -16.953 36.615  1.00 42.19  ? 44   ILE J CB  1 
ATOM   6125 C CG1 . ILE B  2 44  ? -46.281 -16.958 36.786  1.00 46.71  ? 44   ILE J CG1 1 
ATOM   6126 C CG2 . ILE B  2 44  ? -48.408 -16.185 37.757  1.00 46.30  ? 44   ILE J CG2 1 
ATOM   6127 C CD1 . ILE B  2 44  ? -45.539 -16.453 35.572  1.00 47.86  ? 44   ILE J CD1 1 
ATOM   6128 N N   . GLU B  2 45  ? -48.781 -19.368 34.383  1.00 45.51  ? 45   GLU J N   1 
ATOM   6129 C CA  . GLU B  2 45  ? -48.390 -19.886 33.076  1.00 42.47  ? 45   GLU J CA  1 
ATOM   6130 C C   . GLU B  2 45  ? -48.063 -18.708 32.165  1.00 36.32  ? 45   GLU J C   1 
ATOM   6131 O O   . GLU B  2 45  ? -48.675 -17.648 32.261  1.00 32.60  ? 45   GLU J O   1 
ATOM   6132 C CB  . GLU B  2 45  ? -49.494 -20.745 32.461  1.00 37.72  ? 45   GLU J CB  1 
ATOM   6133 C CG  . GLU B  2 45  ? -49.089 -21.420 31.160  1.00 34.28  ? 45   GLU J CG  1 
ATOM   6134 C CD  . GLU B  2 45  ? -50.260 -22.068 30.446  1.00 42.21  ? 45   GLU J CD  1 
ATOM   6135 O OE1 . GLU B  2 45  ? -50.064 -22.604 29.334  1.00 40.07  ? 45   GLU J OE1 1 
ATOM   6136 O OE2 . GLU B  2 45  ? -51.381 -22.039 30.997  1.00 54.26  1 45   GLU J OE2 1 
ATOM   6137 N N   . GLU B  2 46  ? -47.091 -18.888 31.285  1.00 33.52  ? 46   GLU J N   1 
ATOM   6138 C CA  . GLU B  2 46  ? -46.629 -17.778 30.475  1.00 32.79  ? 46   GLU J CA  1 
ATOM   6139 C C   . GLU B  2 46  ? -46.119 -18.236 29.122  1.00 39.92  ? 46   GLU J C   1 
ATOM   6140 O O   . GLU B  2 46  ? -45.339 -19.184 29.029  1.00 39.41  ? 46   GLU J O   1 
ATOM   6141 C CB  . GLU B  2 46  ? -45.532 -17.018 31.214  1.00 37.47  ? 46   GLU J CB  1 
ATOM   6142 C CG  . GLU B  2 46  ? -44.786 -16.018 30.356  1.00 40.91  ? 46   GLU J CG  1 
ATOM   6143 C CD  . GLU B  2 46  ? -43.665 -15.334 31.111  1.00 51.81  ? 46   GLU J CD  1 
ATOM   6144 O OE1 . GLU B  2 46  ? -42.888 -14.586 30.476  1.00 56.60  ? 46   GLU J OE1 1 
ATOM   6145 O OE2 . GLU B  2 46  ? -43.561 -15.546 32.340  1.00 45.28  1 46   GLU J OE2 1 
ATOM   6146 N N   . CYS B  2 47  ? -46.565 -17.548 28.077  1.00 41.34  ? 47   CYS J N   1 
ATOM   6147 C CA  . CYS B  2 47  ? -46.136 -17.830 26.716  1.00 35.75  ? 47   CYS J CA  1 
ATOM   6148 C C   . CYS B  2 47  ? -44.623 -17.882 26.607  1.00 34.79  ? 47   CYS J C   1 
ATOM   6149 O O   . CYS B  2 47  ? -43.912 -17.239 27.374  1.00 41.86  ? 47   CYS J O   1 
ATOM   6150 C CB  . CYS B  2 47  ? -46.669 -16.756 25.768  1.00 30.55  ? 47   CYS J CB  1 
ATOM   6151 S SG  . CYS B  2 47  ? -47.829 -17.360 24.539  1.00 37.46  ? 47   CYS J SG  1 
ATOM   6152 N N   . GLU B  2 48  ? -44.140 -18.672 25.660  1.00 35.59  ? 48   GLU J N   1 
ATOM   6153 C CA  . GLU B  2 48  ? -42.747 -18.604 25.257  1.00 37.17  ? 48   GLU J CA  1 
ATOM   6154 C C   . GLU B  2 48  ? -42.677 -17.681 24.050  1.00 37.82  ? 48   GLU J C   1 
ATOM   6155 O O   . GLU B  2 48  ? -42.232 -16.535 24.144  1.00 34.15  ? 48   GLU J O   1 
ATOM   6156 C CB  . GLU B  2 48  ? -42.223 -19.992 24.886  1.00 36.71  ? 48   GLU J CB  1 
ATOM   6157 C CG  . GLU B  2 48  ? -40.839 -19.990 24.250  1.00 39.52  ? 48   GLU J CG  1 
ATOM   6158 C CD  . GLU B  2 48  ? -40.385 -21.375 23.822  1.00 55.30  ? 48   GLU J CD  1 
ATOM   6159 O OE1 . GLU B  2 48  ? -40.449 -22.310 24.650  1.00 55.96  ? 48   GLU J OE1 1 
ATOM   6160 O OE2 . GLU B  2 48  ? -39.969 -21.525 22.654  1.00 58.54  1 48   GLU J OE2 1 
ATOM   6161 N N   . GLY B  2 49  ? -43.152 -18.187 22.918  1.00 45.36  ? 49   GLY J N   1 
ATOM   6162 C CA  . GLY B  2 49  ? -43.137 -17.435 21.682  1.00 41.23  ? 49   GLY J CA  1 
ATOM   6163 C C   . GLY B  2 49  ? -44.461 -16.765 21.401  1.00 27.24  ? 49   GLY J C   1 
ATOM   6164 O O   . GLY B  2 49  ? -45.190 -17.182 20.504  1.00 22.51  ? 49   GLY J O   1 
ATOM   6165 N N   . ALA B  2 50  ? -44.770 -15.731 22.178  1.00 28.31  ? 50   ALA J N   1 
ATOM   6166 C CA  . ALA B  2 50  ? -45.961 -14.930 21.939  1.00 25.66  ? 50   ALA J CA  1 
ATOM   6167 C C   . ALA B  2 50  ? -45.781 -14.133 20.654  1.00 24.00  ? 50   ALA J C   1 
ATOM   6168 O O   . ALA B  2 50  ? -44.657 -13.781 20.287  1.00 23.13  ? 50   ALA J O   1 
ATOM   6169 C CB  . ALA B  2 50  ? -46.238 -14.005 23.113  1.00 19.27  ? 50   ALA J CB  1 
ATOM   6170 N N   . ASP B  2 51  ? -46.895 -13.885 19.966  1.00 22.93  ? 51   ASP J N   1 
ATOM   6171 C CA  . ASP B  2 51  ? -46.919 -13.148 18.701  1.00 24.18  ? 51   ASP J CA  1 
ATOM   6172 C C   . ASP B  2 51  ? -46.202 -13.908 17.578  1.00 23.72  ? 51   ASP J C   1 
ATOM   6173 O O   . ASP B  2 51  ? -46.027 -13.401 16.467  1.00 20.84  ? 51   ASP J O   1 
ATOM   6174 C CB  . ASP B  2 51  ? -46.356 -11.736 18.886  1.00 22.71  ? 51   ASP J CB  1 
ATOM   6175 C CG  . ASP B  2 51  ? -46.892 -11.061 20.135  1.00 24.03  ? 51   ASP J CG  1 
ATOM   6176 O OD1 . ASP B  2 51  ? -48.126 -11.030 20.311  1.00 24.50  ? 51   ASP J OD1 1 
ATOM   6177 O OD2 . ASP B  2 51  ? -46.082 -10.583 20.955  1.00 30.64  1 51   ASP J OD2 1 
ATOM   6178 N N   . GLN B  2 52  ? -45.812 -15.140 17.883  1.00 20.79  ? 52   GLN J N   1 
ATOM   6179 C CA  . GLN B  2 52  ? -45.169 -16.016 16.923  1.00 18.47  ? 52   GLN J CA  1 
ATOM   6180 C C   . GLN B  2 52  ? -46.118 -17.165 16.604  1.00 18.29  ? 52   GLN J C   1 
ATOM   6181 O O   . GLN B  2 52  ? -46.951 -17.525 17.436  1.00 20.86  ? 52   GLN J O   1 
ATOM   6182 C CB  . GLN B  2 52  ? -43.855 -16.543 17.504  1.00 24.62  ? 52   GLN J CB  1 
ATOM   6183 C CG  . GLN B  2 52  ? -42.843 -15.452 17.798  1.00 31.71  ? 52   GLN J CG  1 
ATOM   6184 C CD  . GLN B  2 52  ? -42.490 -14.640 16.561  1.00 37.48  ? 52   GLN J CD  1 
ATOM   6185 O OE1 . GLN B  2 52  ? -42.251 -15.196 15.486  1.00 37.11  ? 52   GLN J OE1 1 
ATOM   6186 N NE2 . GLN B  2 52  ? -42.461 -13.316 16.707  1.00 31.99  ? 52   GLN J NE2 1 
ATOM   6187 N N   . PRO B  2 53  ? -46.006 -17.730 15.391  1.00 14.99  ? 53   PRO J N   1 
ATOM   6188 C CA  . PRO B  2 53  ? -46.842 -18.839 14.916  1.00 14.38  ? 53   PRO J CA  1 
ATOM   6189 C C   . PRO B  2 53  ? -46.956 -19.980 15.919  1.00 19.24  ? 53   PRO J C   1 
ATOM   6190 O O   . PRO B  2 53  ? -45.995 -20.269 16.629  1.00 23.98  ? 53   PRO J O   1 
ATOM   6191 C CB  . PRO B  2 53  ? -46.088 -19.324 13.681  1.00 14.08  ? 53   PRO J CB  1 
ATOM   6192 C CG  . PRO B  2 53  ? -45.427 -18.106 13.157  1.00 14.79  ? 53   PRO J CG  1 
ATOM   6193 C CD  . PRO B  2 53  ? -45.067 -17.271 14.351  1.00 17.71  ? 53   PRO J CD  1 
ATOM   6194 N N   . CYS B  2 54  ? -48.119 -20.621 15.968  1.00 17.33  ? 54   CYS J N   1 
ATOM   6195 C CA  . CYS B  2 54  ? -48.344 -21.738 16.874  1.00 13.27  ? 54   CYS J CA  1 
ATOM   6196 C C   . CYS B  2 54  ? -47.721 -23.009 16.334  1.00 13.84  ? 54   CYS J C   1 
ATOM   6197 O O   . CYS B  2 54  ? -47.267 -23.061 15.194  1.00 14.55  ? 54   CYS J O   1 
ATOM   6198 C CB  . CYS B  2 54  ? -49.838 -21.972 17.065  1.00 15.22  ? 54   CYS J CB  1 
ATOM   6199 S SG  . CYS B  2 54  ? -50.811 -20.481 17.334  1.00 30.11  ? 54   CYS J SG  1 
ATOM   6200 N N   . ASP B  2 55  ? -47.705 -24.042 17.162  1.00 17.15  ? 55   ASP J N   1 
ATOM   6201 C CA  . ASP B  2 55  ? -47.291 -25.356 16.703  1.00 23.56  ? 55   ASP J CA  1 
ATOM   6202 C C   . ASP B  2 55  ? -48.381 -25.942 15.820  1.00 20.01  ? 55   ASP J C   1 
ATOM   6203 O O   . ASP B  2 55  ? -49.564 -25.690 16.040  1.00 17.37  ? 55   ASP J O   1 
ATOM   6204 C CB  . ASP B  2 55  ? -47.015 -26.282 17.885  1.00 31.17  ? 55   ASP J CB  1 
ATOM   6205 C CG  . ASP B  2 55  ? -45.697 -25.982 18.559  1.00 31.74  ? 55   ASP J CG  1 
ATOM   6206 O OD1 . ASP B  2 55  ? -44.771 -25.530 17.849  1.00 25.30  ? 55   ASP J OD1 1 
ATOM   6207 O OD2 . ASP B  2 55  ? -45.593 -26.201 19.789  1.00 32.61  1 55   ASP J OD2 1 
ATOM   6208 N N   . PHE B  2 56  ? -47.975 -26.729 14.831  1.00 20.56  ? 56   PHE J N   1 
ATOM   6209 C CA  . PHE B  2 56  ? -48.900 -27.251 13.837  1.00 18.35  ? 56   PHE J CA  1 
ATOM   6210 C C   . PHE B  2 56  ? -49.666 -26.091 13.227  1.00 18.75  ? 56   PHE J C   1 
ATOM   6211 O O   . PHE B  2 56  ? -50.878 -26.166 13.046  1.00 20.63  ? 56   PHE J O   1 
ATOM   6212 C CB  . PHE B  2 56  ? -49.881 -28.249 14.453  1.00 15.13  ? 56   PHE J CB  1 
ATOM   6213 C CG  . PHE B  2 56  ? -49.224 -29.338 15.245  1.00 19.62  ? 56   PHE J CG  1 
ATOM   6214 C CD1 . PHE B  2 56  ? -48.841 -30.523 14.633  1.00 19.93  ? 56   PHE J CD1 1 
ATOM   6215 C CD2 . PHE B  2 56  ? -48.998 -29.186 16.605  1.00 19.00  ? 56   PHE J CD2 1 
ATOM   6216 C CE1 . PHE B  2 56  ? -48.241 -31.532 15.361  1.00 20.22  ? 56   PHE J CE1 1 
ATOM   6217 C CE2 . PHE B  2 56  ? -48.399 -30.190 17.339  1.00 19.10  ? 56   PHE J CE2 1 
ATOM   6218 C CZ  . PHE B  2 56  ? -48.021 -31.365 16.717  1.00 23.40  ? 56   PHE J CZ  1 
ATOM   6219 N N   . ALA B  2 57  ? -48.955 -25.013 12.916  1.00 16.30  ? 57   ALA J N   1 
ATOM   6220 C CA  . ALA B  2 57  ? -49.585 -23.841 12.326  1.00 12.71  ? 57   ALA J CA  1 
ATOM   6221 C C   . ALA B  2 57  ? -50.050 -24.118 10.904  1.00 11.70  ? 57   ALA J C   1 
ATOM   6222 O O   . ALA B  2 57  ? -50.616 -23.244 10.254  1.00 12.40  ? 57   ALA J O   1 
ATOM   6223 C CB  . ALA B  2 57  ? -48.635 -22.664 12.350  1.00 16.92  ? 57   ALA J CB  1 
ATOM   6224 N N   . ALA B  2 58  ? -49.802 -25.334 10.427  1.00 12.79  ? 58   ALA J N   1 
ATOM   6225 C CA  . ALA B  2 58  ? -50.256 -25.759 9.110   1.00 14.48  ? 58   ALA J CA  1 
ATOM   6226 C C   . ALA B  2 58  ? -51.467 -26.679 9.195   1.00 16.09  ? 58   ALA J C   1 
ATOM   6227 O O   . ALA B  2 58  ? -52.124 -26.930 8.187   1.00 16.61  ? 58   ALA J O   1 
ATOM   6228 C CB  . ALA B  2 58  ? -49.133 -26.446 8.357   1.00 15.29  ? 58   ALA J CB  1 
ATOM   6229 N N   . ASN B  2 59  ? -51.766 -27.175 10.393  1.00 14.68  ? 59   ASN J N   1 
ATOM   6230 C CA  . ASN B  2 59  ? -52.907 -28.071 10.583  1.00 14.87  ? 59   ASN J CA  1 
ATOM   6231 C C   . ASN B  2 59  ? -54.248 -27.360 10.781  1.00 14.60  ? 59   ASN J C   1 
ATOM   6232 O O   . ASN B  2 59  ? -55.199 -27.938 11.301  1.00 16.30  ? 59   ASN J O   1 
ATOM   6233 C CB  . ASN B  2 59  ? -52.637 -29.035 11.738  1.00 12.86  ? 59   ASN J CB  1 
ATOM   6234 C CG  . ASN B  2 59  ? -51.488 -29.966 11.446  1.00 14.71  ? 59   ASN J CG  1 
ATOM   6235 O OD1 . ASN B  2 59  ? -50.333 -29.543 11.402  1.00 18.33  ? 59   ASN J OD1 1 
ATOM   6236 N ND2 . ASN B  2 59  ? -51.795 -31.243 11.232  1.00 11.90  ? 59   ASN J ND2 1 
ATOM   6237 N N   . PHE B  2 60  ? -54.324 -26.110 10.347  1.00 10.92  ? 60   PHE J N   1 
ATOM   6238 C CA  . PHE B  2 60  ? -55.529 -25.330 10.534  1.00 9.95   ? 60   PHE J CA  1 
ATOM   6239 C C   . PHE B  2 60  ? -56.143 -24.935 9.199   1.00 16.59  ? 60   PHE J C   1 
ATOM   6240 O O   . PHE B  2 60  ? -55.433 -24.855 8.196   1.00 21.03  ? 60   PHE J O   1 
ATOM   6241 C CB  . PHE B  2 60  ? -55.215 -24.101 11.377  1.00 10.32  ? 60   PHE J CB  1 
ATOM   6242 C CG  . PHE B  2 60  ? -54.947 -24.420 12.809  1.00 13.86  ? 60   PHE J CG  1 
ATOM   6243 C CD1 . PHE B  2 60  ? -55.986 -24.726 13.662  1.00 13.65  ? 60   PHE J CD1 1 
ATOM   6244 C CD2 . PHE B  2 60  ? -53.654 -24.432 13.303  1.00 18.95  ? 60   PHE J CD2 1 
ATOM   6245 C CE1 . PHE B  2 60  ? -55.745 -25.029 14.986  1.00 15.50  ? 60   PHE J CE1 1 
ATOM   6246 C CE2 . PHE B  2 60  ? -53.404 -24.733 14.631  1.00 15.81  ? 60   PHE J CE2 1 
ATOM   6247 C CZ  . PHE B  2 60  ? -54.449 -25.034 15.471  1.00 14.49  ? 60   PHE J CZ  1 
ATOM   6248 N N   . PRO B  2 61  ? -57.472 -24.709 9.181   1.00 13.73  ? 61   PRO J N   1 
ATOM   6249 C CA  . PRO B  2 61  ? -58.205 -24.265 7.991   1.00 8.70   ? 61   PRO J CA  1 
ATOM   6250 C C   . PRO B  2 61  ? -57.612 -22.993 7.402   1.00 9.50   ? 61   PRO J C   1 
ATOM   6251 O O   . PRO B  2 61  ? -56.935 -22.253 8.106   1.00 11.50  ? 61   PRO J O   1 
ATOM   6252 C CB  . PRO B  2 61  ? -59.601 -24.003 8.536   1.00 10.90  ? 61   PRO J CB  1 
ATOM   6253 C CG  . PRO B  2 61  ? -59.734 -24.961 9.666   1.00 10.83  ? 61   PRO J CG  1 
ATOM   6254 C CD  . PRO B  2 61  ? -58.384 -25.009 10.300  1.00 13.23  ? 61   PRO J CD  1 
ATOM   6255 N N   . GLN B  2 62  ? -57.890 -22.738 6.130   1.00 9.06   ? 62   GLN J N   1 
ATOM   6256 C CA  . GLN B  2 62  ? -57.095 -21.802 5.331   1.00 11.29  ? 62   GLN J CA  1 
ATOM   6257 C C   . GLN B  2 62  ? -57.111 -20.306 5.687   1.00 13.12  ? 62   GLN J C   1 
ATOM   6258 O O   . GLN B  2 62  ? -56.069 -19.648 5.637   1.00 16.29  ? 62   GLN J O   1 
ATOM   6259 C CB  . GLN B  2 62  ? -57.394 -21.993 3.847   1.00 9.59   ? 62   GLN J CB  1 
ATOM   6260 C CG  . GLN B  2 62  ? -56.845 -23.288 3.288   1.00 10.70  ? 62   GLN J CG  1 
ATOM   6261 C CD  . GLN B  2 62  ? -56.717 -23.239 1.786   1.00 11.97  ? 62   GLN J CD  1 
ATOM   6262 O OE1 . GLN B  2 62  ? -57.186 -22.295 1.152   1.00 13.84  ? 62   GLN J OE1 1 
ATOM   6263 N NE2 . GLN B  2 62  ? -56.076 -24.248 1.204   1.00 10.13  ? 62   GLN J NE2 1 
ATOM   6264 N N   . SER B  2 63  ? -58.269 -19.763 6.033   1.00 9.83   ? 63   SER J N   1 
ATOM   6265 C CA  . SER B  2 63  ? -58.359 -18.332 6.310   1.00 11.88  ? 63   SER J CA  1 
ATOM   6266 C C   . SER B  2 63  ? -57.782 -17.943 7.671   1.00 15.36  ? 63   SER J C   1 
ATOM   6267 O O   . SER B  2 63  ? -57.675 -16.758 7.996   1.00 17.03  ? 63   SER J O   1 
ATOM   6268 C CB  . SER B  2 63  ? -59.810 -17.871 6.219   1.00 17.87  ? 63   SER J CB  1 
ATOM   6269 O OG  . SER B  2 63  ? -60.648 -18.678 7.030   1.00 21.00  ? 63   SER J OG  1 
ATOM   6270 N N   . TYR B  2 64  ? -57.407 -18.945 8.458   1.00 16.31  ? 64   TYR J N   1 
ATOM   6271 C CA  . TYR B  2 64  ? -56.993 -18.730 9.839   1.00 14.76  ? 64   TYR J CA  1 
ATOM   6272 C C   . TYR B  2 64  ? -55.480 -18.666 9.991   1.00 20.33  ? 64   TYR J C   1 
ATOM   6273 O O   . TYR B  2 64  ? -54.739 -19.446 9.386   1.00 20.12  ? 64   TYR J O   1 
ATOM   6274 C CB  . TYR B  2 64  ? -57.589 -19.811 10.738  1.00 12.33  ? 64   TYR J CB  1 
ATOM   6275 C CG  . TYR B  2 64  ? -59.082 -19.922 10.563  1.00 18.85  ? 64   TYR J CG  1 
ATOM   6276 C CD1 . TYR B  2 64  ? -59.630 -20.760 9.597   1.00 17.36  ? 64   TYR J CD1 1 
ATOM   6277 C CD2 . TYR B  2 64  ? -59.950 -19.164 11.338  1.00 23.42  ? 64   TYR J CD2 1 
ATOM   6278 C CE1 . TYR B  2 64  ? -61.007 -20.851 9.419   1.00 14.33  ? 64   TYR J CE1 1 
ATOM   6279 C CE2 . TYR B  2 64  ? -61.329 -19.249 11.167  1.00 20.67  ? 64   TYR J CE2 1 
ATOM   6280 C CZ  . TYR B  2 64  ? -61.847 -20.094 10.206  1.00 15.25  ? 64   TYR J CZ  1 
ATOM   6281 O OH  . TYR B  2 64  ? -63.209 -20.181 10.041  1.00 14.57  ? 64   TYR J OH  1 
ATOM   6282 N N   . ASN B  2 65  ? -55.038 -17.718 10.809  1.00 22.11  ? 65   ASN J N   1 
ATOM   6283 C CA  . ASN B  2 65  ? -53.627 -17.471 11.039  1.00 16.29  ? 65   ASN J CA  1 
ATOM   6284 C C   . ASN B  2 65  ? -53.299 -17.751 12.497  1.00 17.65  ? 65   ASN J C   1 
ATOM   6285 O O   . ASN B  2 65  ? -53.684 -16.983 13.375  1.00 17.10  ? 65   ASN J O   1 
ATOM   6286 C CB  . ASN B  2 65  ? -53.313 -16.017 10.691  1.00 17.48  ? 65   ASN J CB  1 
ATOM   6287 C CG  . ASN B  2 65  ? -51.854 -15.676 10.866  1.00 23.21  ? 65   ASN J CG  1 
ATOM   6288 O OD1 . ASN B  2 65  ? -51.032 -15.930 9.985   1.00 26.95  ? 65   ASN J OD1 1 
ATOM   6289 N ND2 . ASN B  2 65  ? -51.523 -15.078 12.003  1.00 26.97  ? 65   ASN J ND2 1 
ATOM   6290 N N   . PRO B  2 66  ? -52.605 -18.870 12.766  1.00 18.64  ? 66   PRO J N   1 
ATOM   6291 C CA  . PRO B  2 66  ? -52.267 -19.284 14.136  1.00 15.97  ? 66   PRO J CA  1 
ATOM   6292 C C   . PRO B  2 66  ? -51.172 -18.416 14.758  1.00 19.46  ? 66   PRO J C   1 
ATOM   6293 O O   . PRO B  2 66  ? -50.056 -18.342 14.235  1.00 17.54  ? 66   PRO J O   1 
ATOM   6294 C CB  . PRO B  2 66  ? -51.758 -20.721 13.960  1.00 14.30  ? 66   PRO J CB  1 
ATOM   6295 C CG  . PRO B  2 66  ? -52.138 -21.122 12.564  1.00 16.62  ? 66   PRO J CG  1 
ATOM   6296 C CD  . PRO B  2 66  ? -52.167 -19.859 11.770  1.00 16.64  ? 66   PRO J CD  1 
ATOM   6297 N N   . ILE B  2 67  ? -51.499 -17.770 15.873  1.00 18.70  ? 67   ILE J N   1 
ATOM   6298 C CA  . ILE B  2 67  ? -50.551 -16.932 16.595  1.00 15.80  ? 67   ILE J CA  1 
ATOM   6299 C C   . ILE B  2 67  ? -50.847 -17.015 18.083  1.00 17.47  ? 67   ILE J C   1 
ATOM   6300 O O   . ILE B  2 67  ? -51.988 -16.833 18.505  1.00 17.46  ? 67   ILE J O   1 
ATOM   6301 C CB  . ILE B  2 67  ? -50.600 -15.476 16.114  1.00 16.86  ? 67   ILE J CB  1 
ATOM   6302 C CG1 . ILE B  2 67  ? -49.615 -15.281 14.962  1.00 16.54  ? 67   ILE J CG1 1 
ATOM   6303 C CG2 . ILE B  2 67  ? -50.278 -14.516 17.246  1.00 19.27  ? 67   ILE J CG2 1 
ATOM   6304 C CD1 . ILE B  2 67  ? -49.577 -13.869 14.420  1.00 26.66  ? 67   ILE J CD1 1 
ATOM   6305 N N   . CYS B  2 68  ? -49.814 -17.304 18.869  1.00 18.49  ? 68   CYS J N   1 
ATOM   6306 C CA  . CYS B  2 68  ? -49.983 -17.626 20.282  1.00 18.88  ? 68   CYS J CA  1 
ATOM   6307 C C   . CYS B  2 68  ? -50.257 -16.396 21.124  1.00 20.19  ? 68   CYS J C   1 
ATOM   6308 O O   . CYS B  2 68  ? -49.557 -15.391 21.013  1.00 20.79  ? 68   CYS J O   1 
ATOM   6309 C CB  . CYS B  2 68  ? -48.747 -18.351 20.798  1.00 17.68  ? 68   CYS J CB  1 
ATOM   6310 S SG  . CYS B  2 68  ? -48.254 -19.711 19.728  1.00 19.04  ? 68   CYS J SG  1 
ATOM   6311 N N   . LYS B  2 69  ? -51.281 -16.475 21.967  1.00 16.63  ? 69   LYS J N   1 
ATOM   6312 C CA  . LYS B  2 69  ? -51.657 -15.326 22.771  1.00 18.09  ? 69   LYS J CA  1 
ATOM   6313 C C   . LYS B  2 69  ? -51.358 -15.488 24.246  1.00 24.36  ? 69   LYS J C   1 
ATOM   6314 O O   . LYS B  2 69  ? -51.563 -16.550 24.831  1.00 25.91  ? 69   LYS J O   1 
ATOM   6315 C CB  . LYS B  2 69  ? -53.127 -14.966 22.570  1.00 21.63  ? 69   LYS J CB  1 
ATOM   6316 C CG  . LYS B  2 69  ? -53.379 -14.148 21.316  1.00 30.86  ? 69   LYS J CG  1 
ATOM   6317 C CD  . LYS B  2 69  ? -52.230 -13.178 21.056  1.00 32.85  ? 69   LYS J CD  1 
ATOM   6318 C CE  . LYS B  2 69  ? -52.321 -12.573 19.665  1.00 32.83  ? 69   LYS J CE  1 
ATOM   6319 N NZ  . LYS B  2 69  ? -50.983 -12.149 19.154  1.00 31.44  1 69   LYS J NZ  1 
ATOM   6320 N N   . GLN B  2 70  ? -50.868 -14.408 24.838  1.00 23.50  ? 70   GLN J N   1 
ATOM   6321 C CA  . GLN B  2 70  ? -50.634 -14.356 26.265  1.00 23.81  ? 70   GLN J CA  1 
ATOM   6322 C C   . GLN B  2 70  ? -51.901 -13.864 26.958  1.00 23.65  ? 70   GLN J C   1 
ATOM   6323 O O   . GLN B  2 70  ? -52.290 -12.708 26.812  1.00 24.08  ? 70   GLN J O   1 
ATOM   6324 C CB  . GLN B  2 70  ? -49.459 -13.423 26.558  1.00 28.03  ? 70   GLN J CB  1 
ATOM   6325 C CG  . GLN B  2 70  ? -49.068 -13.334 28.021  1.00 29.66  ? 70   GLN J CG  1 
ATOM   6326 C CD  . GLN B  2 70  ? -48.510 -14.627 28.568  1.00 27.38  ? 70   GLN J CD  1 
ATOM   6327 O OE1 . GLN B  2 70  ? -47.371 -14.991 28.281  1.00 26.72  ? 70   GLN J OE1 1 
ATOM   6328 N NE2 . GLN B  2 70  ? -49.308 -15.327 29.367  1.00 23.84  ? 70   GLN J NE2 1 
ATOM   6329 N N   . HIS B  2 71  ? -52.553 -14.751 27.698  1.00 24.49  ? 71   HIS J N   1 
ATOM   6330 C CA  . HIS B  2 71  ? -53.754 -14.382 28.438  1.00 29.62  ? 71   HIS J CA  1 
ATOM   6331 C C   . HIS B  2 71  ? -53.451 -14.067 29.908  1.00 34.32  ? 71   HIS J C   1 
ATOM   6332 O O   . HIS B  2 71  ? -52.553 -14.657 30.513  1.00 33.70  ? 71   HIS J O   1 
ATOM   6333 C CB  . HIS B  2 71  ? -54.807 -15.491 28.331  1.00 34.33  ? 71   HIS J CB  1 
ATOM   6334 C CG  . HIS B  2 71  ? -55.585 -15.467 27.051  1.00 35.43  ? 71   HIS J CG  1 
ATOM   6335 N ND1 . HIS B  2 71  ? -56.942 -15.232 27.010  1.00 38.88  ? 71   HIS J ND1 1 
ATOM   6336 C CD2 . HIS B  2 71  ? -55.195 -15.644 25.766  1.00 33.45  ? 71   HIS J CD2 1 
ATOM   6337 C CE1 . HIS B  2 71  ? -57.356 -15.264 25.755  1.00 37.91  ? 71   HIS J CE1 1 
ATOM   6338 N NE2 . HIS B  2 71  ? -56.316 -15.513 24.980  1.00 34.53  ? 71   HIS J NE2 1 
ATOM   6339 N N   . TYR B  2 72  ? -54.206 -13.133 30.478  1.00 32.44  ? 72   TYR J N   1 
ATOM   6340 C CA  . TYR B  2 72  ? -54.008 -12.733 31.867  1.00 32.51  ? 72   TYR J CA  1 
ATOM   6341 C C   . TYR B  2 72  ? -55.234 -13.000 32.725  1.00 36.76  ? 72   TYR J C   1 
ATOM   6342 O O   . TYR B  2 72  ? -56.227 -13.551 32.257  1.00 42.03  ? 72   TYR J O   1 
ATOM   6343 C CB  . TYR B  2 72  ? -53.687 -11.245 31.955  1.00 36.04  ? 72   TYR J CB  1 
ATOM   6344 C CG  . TYR B  2 72  ? -52.443 -10.822 31.221  1.00 37.41  ? 72   TYR J CG  1 
ATOM   6345 C CD1 . TYR B  2 72  ? -51.422 -11.719 30.967  1.00 33.94  ? 72   TYR J CD1 1 
ATOM   6346 C CD2 . TYR B  2 72  ? -52.287 -9.514  30.790  1.00 47.82  ? 72   TYR J CD2 1 
ATOM   6347 C CE1 . TYR B  2 72  ? -50.288 -11.326 30.303  1.00 35.22  ? 72   TYR J CE1 1 
ATOM   6348 C CE2 . TYR B  2 72  ? -51.153 -9.114  30.120  1.00 41.54  ? 72   TYR J CE2 1 
ATOM   6349 C CZ  . TYR B  2 72  ? -50.159 -10.025 29.877  1.00 38.09  ? 72   TYR J CZ  1 
ATOM   6350 O OH  . TYR B  2 72  ? -49.026 -9.629  29.210  1.00 56.01  ? 72   TYR J OH  1 
ATOM   6351 N N   . THR B  2 73  ? -55.145 -12.589 33.985  1.00 34.80  ? 73   THR J N   1 
ATOM   6352 C CA  . THR B  2 73  ? -56.253 -12.662 34.930  1.00 44.17  ? 73   THR J CA  1 
ATOM   6353 C C   . THR B  2 73  ? -56.105 -11.536 35.941  1.00 49.96  ? 73   THR J C   1 
ATOM   6354 O O   . THR B  2 73  ? -55.038 -10.926 36.038  1.00 48.69  ? 73   THR J O   1 
ATOM   6355 C CB  . THR B  2 73  ? -56.268 -13.991 35.716  1.00 47.81  ? 73   THR J CB  1 
ATOM   6356 O OG1 . THR B  2 73  ? -54.930 -14.342 36.091  1.00 44.32  ? 73   THR J OG1 1 
ATOM   6357 C CG2 . THR B  2 73  ? -56.887 -15.118 34.894  1.00 45.38  ? 73   THR J CG2 1 
ATOM   6358 N N   . GLN B  2 74  ? -57.174 -11.275 36.693  1.00 47.89  ? 74   GLN J N   1 
ATOM   6359 C CA  . GLN B  2 74  ? -57.168 -10.270 37.755  1.00 41.45  ? 74   GLN J CA  1 
ATOM   6360 C C   . GLN B  2 74  ? -56.697 -8.909  37.246  1.00 32.90  ? 74   GLN J C   1 
ATOM   6361 O O   . GLN B  2 74  ? -57.190 -7.868  37.672  1.00 23.75  ? 74   GLN J O   1 
ATOM   6362 C CB  . GLN B  2 74  ? -56.292 -10.739 38.924  1.00 55.59  ? 74   GLN J CB  1 
ATOM   6363 C CG  . GLN B  2 74  ? -56.230 -9.775  40.103  1.00 58.38  ? 74   GLN J CG  1 
ATOM   6364 C CD  . GLN B  2 74  ? -55.381 -10.301 41.249  1.00 51.56  ? 74   GLN J CD  1 
ATOM   6365 O OE1 . GLN B  2 74  ? -55.443 -11.482 41.594  1.00 53.16  ? 74   GLN J OE1 1 
ATOM   6366 N NE2 . GLN B  2 74  ? -54.579 -9.423  41.840  1.00 54.01  ? 74   GLN J NE2 1 
ATOM   6367 N N   . LYS B  2 94  ? -51.836 -7.825  37.018  1.00 34.65  ? 94   LYS J N   1 
ATOM   6368 C CA  . LYS B  2 94  ? -51.561 -8.433  35.720  1.00 39.64  ? 94   LYS J CA  1 
ATOM   6369 C C   . LYS B  2 94  ? -50.788 -9.740  35.867  1.00 40.10  ? 94   LYS J C   1 
ATOM   6370 O O   . LYS B  2 94  ? -49.560 -9.765  35.806  1.00 42.44  ? 94   LYS J O   1 
ATOM   6371 C CB  . LYS B  2 94  ? -50.808 -7.460  34.802  1.00 42.72  ? 94   LYS J CB  1 
ATOM   6372 C CG  . LYS B  2 94  ? -49.637 -6.732  35.461  1.00 52.61  ? 94   LYS J CG  1 
ATOM   6373 C CD  . LYS B  2 94  ? -48.895 -5.848  34.466  1.00 55.92  ? 94   LYS J CD  1 
ATOM   6374 C CE  . LYS B  2 94  ? -47.703 -5.162  35.117  1.00 66.86  ? 94   LYS J CE  1 
ATOM   6375 N NZ  . LYS B  2 94  ? -48.108 -4.319  36.278  1.00 54.25  1 94   LYS J NZ  1 
ATOM   6376 N N   . ILE B  2 95  ? -51.522 -10.829 36.058  1.00 36.84  ? 95   ILE J N   1 
ATOM   6377 C CA  . ILE B  2 95  ? -50.918 -12.141 36.230  1.00 31.11  ? 95   ILE J CA  1 
ATOM   6378 C C   . ILE B  2 95  ? -51.119 -13.006 34.988  1.00 29.79  ? 95   ILE J C   1 
ATOM   6379 O O   . ILE B  2 95  ? -52.237 -13.427 34.694  1.00 37.81  ? 95   ILE J O   1 
ATOM   6380 C CB  . ILE B  2 95  ? -51.480 -12.837 37.491  1.00 37.16  ? 95   ILE J CB  1 
ATOM   6381 C CG1 . ILE B  2 95  ? -50.785 -12.295 38.741  1.00 31.09  ? 95   ILE J CG1 1 
ATOM   6382 C CG2 . ILE B  2 95  ? -51.318 -14.347 37.420  1.00 38.18  ? 95   ILE J CG2 1 
ATOM   6383 C CD1 . ILE B  2 95  ? -51.533 -12.573 40.020  1.00 31.81  ? 95   ILE J CD1 1 
ATOM   6384 N N   . PRO B  2 96  ? -50.036 -13.229 34.227  1.00 26.00  ? 96   PRO J N   1 
ATOM   6385 C CA  . PRO B  2 96  ? -50.022 -14.177 33.112  1.00 30.66  ? 96   PRO J CA  1 
ATOM   6386 C C   . PRO B  2 96  ? -50.522 -15.528 33.575  1.00 34.67  ? 96   PRO J C   1 
ATOM   6387 O O   . PRO B  2 96  ? -49.814 -16.215 34.308  1.00 37.43  ? 96   PRO J O   1 
ATOM   6388 C CB  . PRO B  2 96  ? -48.539 -14.268 32.766  1.00 32.34  ? 96   PRO J CB  1 
ATOM   6389 C CG  . PRO B  2 96  ? -48.025 -12.912 33.072  1.00 34.15  ? 96   PRO J CG  1 
ATOM   6390 C CD  . PRO B  2 96  ? -48.787 -12.453 34.293  1.00 34.00  ? 96   PRO J CD  1 
ATOM   6391 N N   . SER B  2 97  ? -51.728 -15.895 33.155  1.00 32.15  ? 97   SER J N   1 
ATOM   6392 C CA  . SER B  2 97  ? -52.378 -17.101 33.648  1.00 32.12  ? 97   SER J CA  1 
ATOM   6393 C C   . SER B  2 97  ? -52.391 -18.200 32.600  1.00 33.66  ? 97   SER J C   1 
ATOM   6394 O O   . SER B  2 97  ? -52.511 -19.384 32.924  1.00 31.94  ? 97   SER J O   1 
ATOM   6395 C CB  . SER B  2 97  ? -53.812 -16.783 34.058  1.00 34.76  ? 97   SER J CB  1 
ATOM   6396 O OG  . SER B  2 97  ? -54.548 -16.281 32.955  1.00 33.79  ? 97   SER J OG  1 
ATOM   6397 N N   . CYS B  2 98  ? -52.268 -17.808 31.339  1.00 33.47  ? 98   CYS J N   1 
ATOM   6398 C CA  . CYS B  2 98  ? -52.425 -18.767 30.260  1.00 31.79  ? 98   CYS J CA  1 
ATOM   6399 C C   . CYS B  2 98  ? -51.809 -18.327 28.937  1.00 30.50  ? 98   CYS J C   1 
ATOM   6400 O O   . CYS B  2 98  ? -51.640 -17.137 28.671  1.00 30.26  ? 98   CYS J O   1 
ATOM   6401 C CB  . CYS B  2 98  ? -53.905 -19.070 30.059  1.00 31.19  ? 98   CYS J CB  1 
ATOM   6402 S SG  . CYS B  2 98  ? -54.185 -20.300 28.801  1.00 53.98  ? 98   CYS J SG  1 
ATOM   6403 N N   . CYS B  2 99  ? -51.481 -19.306 28.105  1.00 27.15  ? 99   CYS J N   1 
ATOM   6404 C CA  . CYS B  2 99  ? -50.927 -19.032 26.791  1.00 25.50  ? 99   CYS J CA  1 
ATOM   6405 C C   . CYS B  2 99  ? -51.529 -19.977 25.765  1.00 29.70  ? 99   CYS J C   1 
ATOM   6406 O O   . CYS B  2 99  ? -51.153 -21.151 25.685  1.00 28.57  ? 99   CYS J O   1 
ATOM   6407 C CB  . CYS B  2 99  ? -49.413 -19.179 26.812  1.00 27.00  ? 99   CYS J CB  1 
ATOM   6408 S SG  . CYS B  2 99  ? -48.659 -19.098 25.188  1.00 28.46  ? 99   CYS J SG  1 
ATOM   6409 N N   . LYS B  2 100 ? -52.473 -19.460 24.984  1.00 29.76  ? 100  LYS J N   1 
ATOM   6410 C CA  . LYS B  2 100 ? -53.163 -20.266 23.986  1.00 22.43  ? 100  LYS J CA  1 
ATOM   6411 C C   . LYS B  2 100 ? -53.097 -19.681 22.573  1.00 22.87  ? 100  LYS J C   1 
ATOM   6412 O O   . LYS B  2 100 ? -52.742 -18.513 22.367  1.00 18.72  ? 100  LYS J O   1 
ATOM   6413 C CB  . LYS B  2 100 ? -54.612 -20.536 24.404  1.00 18.85  ? 100  LYS J CB  1 
ATOM   6414 C CG  . LYS B  2 100 ? -55.398 -19.314 24.838  1.00 21.00  ? 100  LYS J CG  1 
ATOM   6415 C CD  . LYS B  2 100 ? -56.796 -19.733 25.264  1.00 32.39  ? 100  LYS J CD  1 
ATOM   6416 C CE  . LYS B  2 100 ? -57.763 -18.561 25.327  1.00 35.27  ? 100  LYS J CE  1 
ATOM   6417 N NZ  . LYS B  2 100 ? -59.188 -19.012 25.294  1.00 26.45  1 100  LYS J NZ  1 
ATOM   6418 N N   . CYS B  2 101 ? -53.442 -20.524 21.607  1.00 22.96  ? 101  CYS J N   1 
ATOM   6419 C CA  . CYS B  2 101 ? -53.319 -20.199 20.197  1.00 15.53  ? 101  CYS J CA  1 
ATOM   6420 C C   . CYS B  2 101 ? -54.597 -19.556 19.680  1.00 20.45  ? 101  CYS J C   1 
ATOM   6421 O O   . CYS B  2 101 ? -55.685 -20.134 19.773  1.00 19.40  ? 101  CYS J O   1 
ATOM   6422 C CB  . CYS B  2 101 ? -53.023 -21.472 19.411  1.00 12.15  ? 101  CYS J CB  1 
ATOM   6423 S SG  . CYS B  2 101 ? -52.674 -21.199 17.691  1.00 15.31  ? 101  CYS J SG  1 
ATOM   6424 N N   . ALA B  2 102 ? -54.466 -18.351 19.142  1.00 18.67  ? 102  ALA J N   1 
ATOM   6425 C CA  . ALA B  2 102 ? -55.617 -17.642 18.613  1.00 15.51  ? 102  ALA J CA  1 
ATOM   6426 C C   . ALA B  2 102 ? -55.598 -17.672 17.098  1.00 16.46  ? 102  ALA J C   1 
ATOM   6427 O O   . ALA B  2 102 ? -54.791 -16.999 16.466  1.00 20.07  ? 102  ALA J O   1 
ATOM   6428 C CB  . ALA B  2 102 ? -55.638 -16.212 19.111  1.00 17.49  ? 102  ALA J CB  1 
ATOM   6429 N N   . LEU B  2 103 ? -56.482 -18.467 16.513  1.00 17.72  ? 103  LEU J N   1 
ATOM   6430 C CA  . LEU B  2 103 ? -56.662 -18.436 15.074  1.00 17.51  ? 103  LEU J CA  1 
ATOM   6431 C C   . LEU B  2 103 ? -57.301 -17.108 14.703  1.00 17.62  ? 103  LEU J C   1 
ATOM   6432 O O   . LEU B  2 103 ? -58.499 -16.905 14.902  1.00 16.45  ? 103  LEU J O   1 
ATOM   6433 C CB  . LEU B  2 103 ? -57.528 -19.606 14.616  1.00 16.13  ? 103  LEU J CB  1 
ATOM   6434 C CG  . LEU B  2 103 ? -56.990 -20.983 15.007  1.00 14.83  ? 103  LEU J CG  1 
ATOM   6435 C CD1 . LEU B  2 103 ? -57.935 -22.055 14.541  1.00 14.82  ? 103  LEU J CD1 1 
ATOM   6436 C CD2 . LEU B  2 103 ? -55.605 -21.220 14.425  1.00 14.85  ? 103  LEU J CD2 1 
ATOM   6437 N N   . LYS B  2 104 ? -56.485 -16.196 14.186  1.00 18.56  ? 104  LYS J N   1 
ATOM   6438 C CA  . LYS B  2 104 ? -56.959 -14.862 13.841  1.00 22.35  ? 104  LYS J CA  1 
ATOM   6439 C C   . LYS B  2 104 ? -57.252 -14.700 12.358  1.00 24.27  ? 104  LYS J C   1 
ATOM   6440 O O   . LYS B  2 104 ? -56.416 -14.983 11.497  1.00 20.28  ? 104  LYS J O   1 
ATOM   6441 C CB  . LYS B  2 104 ? -55.982 -13.785 14.320  1.00 27.55  ? 104  LYS J CB  1 
ATOM   6442 C CG  . LYS B  2 104 ? -54.518 -14.190 14.246  1.00 28.06  ? 104  LYS J CG  1 
ATOM   6443 C CD  . LYS B  2 104 ? -53.634 -13.176 14.944  1.00 26.78  ? 104  LYS J CD  1 
ATOM   6444 C CE  . LYS B  2 104 ? -54.122 -12.909 16.359  1.00 31.60  ? 104  LYS J CE  1 
ATOM   6445 N NZ  . LYS B  2 104 ? -53.443 -11.729 16.964  1.00 43.23  1 104  LYS J NZ  1 
ATOM   6446 N N   . THR B  2 105 ? -58.464 -14.236 12.084  1.00 31.32  ? 105  THR J N   1 
ATOM   6447 C CA  . THR B  2 105 ? -58.945 -14.031 10.732  1.00 31.95  ? 105  THR J CA  1 
ATOM   6448 C C   . THR B  2 105 ? -58.931 -12.558 10.394  1.00 34.86  ? 105  THR J C   1 
ATOM   6449 O O   . THR B  2 105 ? -59.783 -11.808 10.866  1.00 34.49  ? 105  THR J O   1 
ATOM   6450 C CB  . THR B  2 105 ? -60.396 -14.485 10.615  1.00 33.58  ? 105  THR J CB  1 
ATOM   6451 O OG1 . THR B  2 105 ? -61.059 -14.245 11.862  1.00 31.98  ? 105  THR J OG1 1 
ATOM   6452 C CG2 . THR B  2 105 ? -60.469 -15.961 10.291  1.00 30.05  ? 105  THR J CG2 1 
ATOM   6453 N N   . GLY B  2 106 ? -57.963 -12.137 9.588   1.00 39.50  ? 106  GLY J N   1 
ATOM   6454 C CA  . GLY B  2 106 ? -57.990 -10.791 9.050   1.00 44.57  ? 106  GLY J CA  1 
ATOM   6455 C C   . GLY B  2 106 ? -59.112 -10.721 8.028   1.00 61.02  ? 106  GLY J C   1 
ATOM   6456 O O   . GLY B  2 106 ? -59.556 -11.757 7.524   1.00 56.31  ? 106  GLY J O   1 
ATOM   6457 N N   . LEU B  2 107 ? -59.585 -9.514  7.729   1.00 58.63  ? 107  LEU J N   1 
ATOM   6458 C CA  . LEU B  2 107 ? -60.581 -9.333  6.673   1.00 54.99  ? 107  LEU J CA  1 
ATOM   6459 C C   . LEU B  2 107 ? -59.890 -9.074  5.330   1.00 49.05  ? 107  LEU J C   1 
ATOM   6460 O O   . LEU B  2 107 ? -60.432 -8.398  4.457   1.00 53.83  ? 107  LEU J O   1 
ATOM   6461 C CB  . LEU B  2 107 ? -61.560 -8.198  7.013   1.00 58.81  ? 107  LEU J CB  1 
ATOM   6462 C CG  . LEU B  2 107 ? -63.033 -8.558  7.257   1.00 43.58  ? 107  LEU J CG  1 
ATOM   6463 C CD1 . LEU B  2 107 ? -63.894 -7.301  7.400   1.00 28.39  ? 107  LEU J CD1 1 
ATOM   6464 C CD2 . LEU B  2 107 ? -63.567 -9.464  6.151   1.00 25.27  ? 107  LEU J CD2 1 
ATOM   6465 N N   . GLU B  2 108 ? -58.683 -9.611  5.185   1.00 45.61  ? 108  GLU J N   1 
ATOM   6466 C CA  . GLU B  2 108 ? -57.922 -9.513  3.946   1.00 49.57  ? 108  GLU J CA  1 
ATOM   6467 C C   . GLU B  2 108 ? -57.317 -10.884 3.629   1.00 56.10  ? 108  GLU J C   1 
ATOM   6468 O O   . GLU B  2 108 ? -57.177 -11.730 4.518   1.00 51.01  ? 108  GLU J O   1 
ATOM   6469 C CB  . GLU B  2 108 ? -56.796 -8.477  4.078   1.00 61.60  ? 108  GLU J CB  1 
ATOM   6470 C CG  . GLU B  2 108 ? -57.083 -7.300  5.018   1.00 60.93  ? 108  GLU J CG  1 
ATOM   6471 C CD  . GLU B  2 108 ? -57.748 -6.120  4.326   1.00 62.28  ? 108  GLU J CD  1 
ATOM   6472 O OE1 . GLU B  2 108 ? -57.534 -5.940  3.105   1.00 70.03  ? 108  GLU J OE1 1 
ATOM   6473 O OE2 . GLU B  2 108 ? -58.482 -5.368  5.007   1.00 49.68  1 108  GLU J OE2 1 
ATOM   6474 N N   . HIS B  2 109 ? -56.951 -11.102 2.369   1.00 57.58  ? 109  HIS J N   1 
ATOM   6475 C CA  . HIS B  2 109 ? -56.302 -12.351 1.973   1.00 51.02  ? 109  HIS J CA  1 
ATOM   6476 C C   . HIS B  2 109 ? -54.775 -12.261 2.082   1.00 47.63  ? 109  HIS J C   1 
ATOM   6477 O O   . HIS B  2 109 ? -54.132 -13.092 2.730   1.00 30.48  ? 109  HIS J O   1 
ATOM   6478 C CB  . HIS B  2 109 ? -56.716 -12.751 0.553   1.00 28.66  ? 109  HIS J CB  1 
ATOM   6479 C CG  . HIS B  2 109 ? -57.299 -14.128 0.463   1.00 37.57  ? 109  HIS J CG  1 
ATOM   6480 N ND1 . HIS B  2 109 ? -57.178 -14.919 -0.660  1.00 34.80  ? 109  HIS J ND1 1 
ATOM   6481 C CD2 . HIS B  2 109 ? -58.007 -14.856 1.361   1.00 35.08  ? 109  HIS J CD2 1 
ATOM   6482 C CE1 . HIS B  2 109 ? -57.785 -16.075 -0.451  1.00 25.81  ? 109  HIS J CE1 1 
ATOM   6483 N NE2 . HIS B  2 109 ? -58.298 -16.062 0.767   1.00 26.06  ? 109  HIS J NE2 1 
ATOM   6484 N N   . VAL C  2 1   ? -58.188 -3.432  13.197  1.00 65.18  ? 1    VAL K N   1 
ATOM   6485 C CA  . VAL C  2 1   ? -58.954 -3.084  12.004  1.00 70.02  ? 1    VAL K CA  1 
ATOM   6486 C C   . VAL C  2 1   ? -60.405 -3.563  12.106  1.00 60.32  ? 1    VAL K C   1 
ATOM   6487 O O   . VAL C  2 1   ? -60.831 -4.070  13.145  1.00 52.29  ? 1    VAL K O   1 
ATOM   6488 C CB  . VAL C  2 1   ? -58.293 -3.649  10.721  1.00 61.66  ? 1    VAL K CB  1 
ATOM   6489 C CG1 . VAL C  2 1   ? -57.034 -2.869  10.380  1.00 44.81  ? 1    VAL K CG1 1 
ATOM   6490 C CG2 . VAL C  2 1   ? -57.973 -5.125  10.889  1.00 62.38  ? 1    VAL K CG2 1 
ATOM   6491 N N   . GLY C  2 2   ? -61.163 -3.392  11.029  1.00 53.90  ? 2    GLY K N   1 
ATOM   6492 C CA  . GLY C  2 2   ? -62.544 -3.837  11.002  1.00 72.15  ? 2    GLY K CA  1 
ATOM   6493 C C   . GLY C  2 2   ? -62.648 -5.349  10.907  1.00 76.79  ? 2    GLY K C   1 
ATOM   6494 O O   . GLY C  2 2   ? -61.890 -5.983  10.167  1.00 68.20  ? 2    GLY K O   1 
ATOM   6495 N N   . GLY C  2 3   ? -63.587 -5.924  11.658  1.00 72.83  ? 3    GLY K N   1 
ATOM   6496 C CA  . GLY C  2 3   ? -63.801 -7.362  11.674  1.00 51.99  ? 3    GLY K CA  1 
ATOM   6497 C C   . GLY C  2 3   ? -62.554 -8.171  11.986  1.00 54.87  ? 3    GLY K C   1 
ATOM   6498 O O   . GLY C  2 3   ? -62.315 -9.203  11.362  1.00 55.98  ? 3    GLY K O   1 
ATOM   6499 N N   . SER C  2 4   ? -61.763 -7.701  12.950  1.00 64.68  ? 4    SER K N   1 
ATOM   6500 C CA  . SER C  2 4   ? -60.497 -8.343  13.316  1.00 57.55  ? 4    SER K CA  1 
ATOM   6501 C C   . SER C  2 4   ? -60.678 -9.399  14.407  1.00 53.67  ? 4    SER K C   1 
ATOM   6502 O O   . SER C  2 4   ? -59.893 -9.477  15.356  1.00 48.32  ? 4    SER K O   1 
ATOM   6503 C CB  . SER C  2 4   ? -59.476 -7.293  13.770  1.00 56.81  ? 4    SER K CB  1 
ATOM   6504 O OG  . SER C  2 4   ? -59.943 -6.573  14.900  1.00 49.11  ? 4    SER K OG  1 
ATOM   6505 N N   . ASP C  2 5   ? -61.718 -10.211 14.258  1.00 47.32  ? 5    ASP K N   1 
ATOM   6506 C CA  . ASP C  2 5   ? -62.056 -11.231 15.240  1.00 39.54  ? 5    ASP K CA  1 
ATOM   6507 C C   . ASP C  2 5   ? -61.052 -12.375 15.219  1.00 27.75  ? 5    ASP K C   1 
ATOM   6508 O O   . ASP C  2 5   ? -60.571 -12.777 14.161  1.00 25.71  ? 5    ASP K O   1 
ATOM   6509 C CB  . ASP C  2 5   ? -63.469 -11.758 14.972  1.00 44.02  ? 5    ASP K CB  1 
ATOM   6510 C CG  . ASP C  2 5   ? -63.872 -12.873 15.920  1.00 40.99  ? 5    ASP K CG  1 
ATOM   6511 O OD1 . ASP C  2 5   ? -63.474 -12.819 17.108  1.00 34.03  ? 5    ASP K OD1 1 
ATOM   6512 O OD2 . ASP C  2 5   ? -64.591 -13.799 15.472  1.00 33.00  1 5    ASP K OD2 1 
ATOM   6513 N N   . GLU C  2 6   ? -60.740 -12.893 16.400  1.00 24.67  ? 6    GLU K N   1 
ATOM   6514 C CA  . GLU C  2 6   ? -59.822 -14.015 16.526  1.00 27.81  ? 6    GLU K CA  1 
ATOM   6515 C C   . GLU C  2 6   ? -60.551 -15.221 17.090  1.00 25.80  ? 6    GLU K C   1 
ATOM   6516 O O   . GLU C  2 6   ? -61.343 -15.094 18.023  1.00 34.40  ? 6    GLU K O   1 
ATOM   6517 C CB  . GLU C  2 6   ? -58.648 -13.643 17.433  1.00 38.27  ? 6    GLU K CB  1 
ATOM   6518 C CG  . GLU C  2 6   ? -59.054 -13.104 18.799  1.00 34.62  ? 6    GLU K CG  1 
ATOM   6519 C CD  . GLU C  2 6   ? -57.861 -12.707 19.640  1.00 36.02  ? 6    GLU K CD  1 
ATOM   6520 O OE1 . GLU C  2 6   ? -57.920 -11.639 20.285  1.00 39.81  ? 6    GLU K OE1 1 
ATOM   6521 O OE2 . GLU C  2 6   ? -56.864 -13.463 19.660  1.00 34.14  1 6    GLU K OE2 1 
ATOM   6522 N N   . ARG C  2 7   ? -60.283 -16.396 16.535  1.00 18.34  ? 7    ARG K N   1 
ATOM   6523 C CA  . ARG C  2 7   ? -61.031 -17.579 16.936  1.00 20.04  ? 7    ARG K CA  1 
ATOM   6524 C C   . ARG C  2 7   ? -60.173 -18.562 17.717  1.00 17.05  ? 7    ARG K C   1 
ATOM   6525 O O   . ARG C  2 7   ? -59.160 -19.042 17.222  1.00 18.35  ? 7    ARG K O   1 
ATOM   6526 C CB  . ARG C  2 7   ? -61.631 -18.268 15.712  1.00 22.93  ? 7    ARG K CB  1 
ATOM   6527 C CG  . ARG C  2 7   ? -62.254 -17.311 14.703  1.00 25.96  ? 7    ARG K CG  1 
ATOM   6528 C CD  . ARG C  2 7   ? -63.577 -16.755 15.189  1.00 26.50  ? 7    ARG K CD  1 
ATOM   6529 N NE  . ARG C  2 7   ? -64.537 -17.820 15.450  1.00 23.58  ? 7    ARG K NE  1 
ATOM   6530 C CZ  . ARG C  2 7   ? -65.244 -18.433 14.508  1.00 20.48  ? 7    ARG K CZ  1 
ATOM   6531 N NH1 . ARG C  2 7   ? -66.094 -19.395 14.840  1.00 20.81  1 7    ARG K NH1 1 
ATOM   6532 N NH2 . ARG C  2 7   ? -65.097 -18.087 13.235  1.00 19.14  ? 7    ARG K NH2 1 
ATOM   6533 N N   . PHE C  2 8   ? -60.595 -18.860 18.939  1.00 16.83  ? 8    PHE K N   1 
ATOM   6534 C CA  . PHE C  2 8   ? -59.903 -19.822 19.785  1.00 15.57  ? 8    PHE K CA  1 
ATOM   6535 C C   . PHE C  2 8   ? -60.450 -21.232 19.583  1.00 15.48  ? 8    PHE K C   1 
ATOM   6536 O O   . PHE C  2 8   ? -61.600 -21.408 19.197  1.00 19.02  ? 8    PHE K O   1 
ATOM   6537 C CB  . PHE C  2 8   ? -60.009 -19.400 21.250  1.00 17.45  ? 8    PHE K CB  1 
ATOM   6538 C CG  . PHE C  2 8   ? -59.385 -18.069 21.530  1.00 21.58  ? 8    PHE K CG  1 
ATOM   6539 C CD1 . PHE C  2 8   ? -58.022 -17.967 21.779  1.00 27.42  ? 8    PHE K CD1 1 
ATOM   6540 C CD2 . PHE C  2 8   ? -60.148 -16.916 21.516  1.00 20.99  ? 8    PHE K CD2 1 
ATOM   6541 C CE1 . PHE C  2 8   ? -57.433 -16.739 22.025  1.00 26.17  ? 8    PHE K CE1 1 
ATOM   6542 C CE2 . PHE C  2 8   ? -59.568 -15.684 21.761  1.00 32.67  ? 8    PHE K CE2 1 
ATOM   6543 C CZ  . PHE C  2 8   ? -58.206 -15.596 22.017  1.00 32.34  ? 8    PHE K CZ  1 
ATOM   6544 N N   . LEU C  2 9   ? -59.621 -22.236 19.837  1.00 16.62  ? 9    LEU K N   1 
ATOM   6545 C CA  . LEU C  2 9   ? -60.015 -23.623 19.604  1.00 17.77  ? 9    LEU K CA  1 
ATOM   6546 C C   . LEU C  2 9   ? -61.044 -24.114 20.620  1.00 18.31  ? 9    LEU K C   1 
ATOM   6547 O O   . LEU C  2 9   ? -61.794 -25.051 20.350  1.00 17.72  ? 9    LEU K O   1 
ATOM   6548 C CB  . LEU C  2 9   ? -58.790 -24.548 19.620  1.00 17.76  ? 9    LEU K CB  1 
ATOM   6549 C CG  . LEU C  2 9   ? -57.867 -24.591 18.401  1.00 8.94   ? 9    LEU K CG  1 
ATOM   6550 C CD1 . LEU C  2 9   ? -56.994 -23.348 18.322  1.00 8.48   ? 9    LEU K CD1 1 
ATOM   6551 C CD2 . LEU C  2 9   ? -57.035 -25.863 18.420  1.00 5.98   ? 9    LEU K CD2 1 
ATOM   6552 N N   . CYS C  2 10  ? -61.064 -23.482 21.789  1.00 20.70  ? 10   CYS K N   1 
ATOM   6553 C CA  . CYS C  2 10  ? -61.955 -23.880 22.875  1.00 25.43  ? 10   CYS K CA  1 
ATOM   6554 C C   . CYS C  2 10  ? -62.716 -22.689 23.430  1.00 27.96  ? 10   CYS K C   1 
ATOM   6555 O O   . CYS C  2 10  ? -62.111 -21.721 23.894  1.00 33.50  ? 10   CYS K O   1 
ATOM   6556 C CB  . CYS C  2 10  ? -61.163 -24.532 24.007  1.00 18.51  ? 10   CYS K CB  1 
ATOM   6557 S SG  . CYS C  2 10  ? -60.847 -26.265 23.757  1.00 15.83  ? 10   CYS K SG  1 
ATOM   6558 N N   . ARG C  2 11  ? -64.041 -22.755 23.398  1.00 26.23  ? 11   ARG K N   1 
ATOM   6559 C CA  . ARG C  2 11  ? -64.816 -21.635 23.908  1.00 43.87  ? 11   ARG K CA  1 
ATOM   6560 C C   . ARG C  2 11  ? -64.894 -21.703 25.423  1.00 37.25  ? 11   ARG K C   1 
ATOM   6561 O O   . ARG C  2 11  ? -64.872 -22.783 26.016  1.00 27.45  ? 11   ARG K O   1 
ATOM   6562 C CB  . ARG C  2 11  ? -66.210 -21.539 23.271  1.00 46.16  ? 11   ARG K CB  1 
ATOM   6563 C CG  . ARG C  2 11  ? -67.154 -22.670 23.619  1.00 51.62  ? 11   ARG K CG  1 
ATOM   6564 C CD  . ARG C  2 11  ? -68.604 -22.221 23.520  1.00 49.91  ? 11   ARG K CD  1 
ATOM   6565 N NE  . ARG C  2 11  ? -68.950 -21.742 22.186  1.00 57.22  ? 11   ARG K NE  1 
ATOM   6566 C CZ  . ARG C  2 11  ? -69.333 -22.532 21.189  1.00 55.49  ? 11   ARG K CZ  1 
ATOM   6567 N NH1 . ARG C  2 11  ? -69.636 -22.014 20.006  1.00 47.62  1 11   ARG K NH1 1 
ATOM   6568 N NH2 . ARG C  2 11  ? -69.410 -23.843 21.375  1.00 52.48  ? 11   ARG K NH2 1 
ATOM   6569 N N   . SER C  2 12  ? -64.984 -20.529 26.034  1.00 40.28  ? 12   SER K N   1 
ATOM   6570 C CA  . SER C  2 12  ? -64.897 -20.404 27.473  1.00 39.96  ? 12   SER K CA  1 
ATOM   6571 C C   . SER C  2 12  ? -65.593 -19.131 27.938  1.00 42.03  ? 12   SER K C   1 
ATOM   6572 O O   . SER C  2 12  ? -65.866 -18.232 27.140  1.00 37.68  ? 12   SER K O   1 
ATOM   6573 C CB  . SER C  2 12  ? -63.430 -20.374 27.878  1.00 41.79  ? 12   SER K CB  1 
ATOM   6574 O OG  . SER C  2 12  ? -62.708 -19.479 27.048  1.00 37.36  ? 12   SER K OG  1 
ATOM   6575 N N   . ILE C  2 13  ? -65.871 -19.054 29.234  1.00 43.23  ? 13   ILE K N   1 
ATOM   6576 C CA  . ILE C  2 13  ? -66.591 -17.915 29.785  1.00 44.68  ? 13   ILE K CA  1 
ATOM   6577 C C   . ILE C  2 13  ? -65.745 -17.152 30.794  1.00 40.95  ? 13   ILE K C   1 
ATOM   6578 O O   . ILE C  2 13  ? -65.507 -17.634 31.901  1.00 34.03  ? 13   ILE K O   1 
ATOM   6579 C CB  . ILE C  2 13  ? -67.893 -18.359 30.477  1.00 42.69  ? 13   ILE K CB  1 
ATOM   6580 C CG1 . ILE C  2 13  ? -68.621 -19.408 29.632  1.00 40.53  ? 13   ILE K CG1 1 
ATOM   6581 C CG2 . ILE C  2 13  ? -68.783 -17.156 30.749  1.00 39.15  ? 13   ILE K CG2 1 
ATOM   6582 C CD1 . ILE C  2 13  ? -69.725 -20.137 30.371  1.00 38.33  ? 13   ILE K CD1 1 
ATOM   6583 N N   . ARG C  2 14  ? -65.298 -15.959 30.411  1.00 45.13  ? 14   ARG K N   1 
ATOM   6584 C CA  . ARG C  2 14  ? -64.555 -15.094 31.324  1.00 49.58  ? 14   ARG K CA  1 
ATOM   6585 C C   . ARG C  2 14  ? -65.493 -14.329 32.258  1.00 50.44  ? 14   ARG K C   1 
ATOM   6586 O O   . ARG C  2 14  ? -66.258 -13.463 31.825  1.00 47.23  ? 14   ARG K O   1 
ATOM   6587 C CB  . ARG C  2 14  ? -63.654 -14.121 30.557  1.00 55.75  ? 14   ARG K CB  1 
ATOM   6588 C CG  . ARG C  2 14  ? -62.597 -14.802 29.699  1.00 57.16  ? 14   ARG K CG  1 
ATOM   6589 C CD  . ARG C  2 14  ? -61.568 -13.810 29.174  1.00 49.40  ? 14   ARG K CD  1 
ATOM   6590 N NE  . ARG C  2 14  ? -60.703 -13.316 30.238  1.00 48.73  ? 14   ARG K NE  1 
ATOM   6591 C CZ  . ARG C  2 14  ? -59.677 -13.997 30.737  1.00 54.03  ? 14   ARG K CZ  1 
ATOM   6592 N NH1 . ARG C  2 14  ? -59.391 -15.205 30.273  1.00 48.97  1 14   ARG K NH1 1 
ATOM   6593 N NH2 . ARG C  2 14  ? -58.937 -13.474 31.704  1.00 60.63  ? 14   ARG K NH2 1 
ATOM   6594 N N   . LYS C  2 15  ? -65.423 -14.659 33.544  1.00 47.84  ? 15   LYS K N   1 
ATOM   6595 C CA  . LYS C  2 15  ? -66.267 -14.041 34.555  1.00 40.87  ? 15   LYS K CA  1 
ATOM   6596 C C   . LYS C  2 15  ? -65.406 -13.494 35.682  1.00 37.75  ? 15   LYS K C   1 
ATOM   6597 O O   . LYS C  2 15  ? -64.184 -13.590 35.632  1.00 43.81  ? 15   LYS K O   1 
ATOM   6598 C CB  . LYS C  2 15  ? -67.241 -15.072 35.111  1.00 37.58  ? 15   LYS K CB  1 
ATOM   6599 C CG  . LYS C  2 15  ? -66.556 -16.235 35.792  1.00 38.66  ? 15   LYS K CG  1 
ATOM   6600 C CD  . LYS C  2 15  ? -67.411 -17.488 35.742  1.00 43.69  ? 15   LYS K CD  1 
ATOM   6601 C CE  . LYS C  2 15  ? -68.714 -17.310 36.498  1.00 44.97  ? 15   LYS K CE  1 
ATOM   6602 N NZ  . LYS C  2 15  ? -69.503 -18.572 36.502  1.00 50.38  1 15   LYS K NZ  1 
ATOM   6603 N N   . LEU C  2 16  ? -66.047 -12.924 36.698  1.00 37.30  ? 16   LEU K N   1 
ATOM   6604 C CA  . LEU C  2 16  ? -65.333 -12.392 37.855  1.00 39.14  ? 16   LEU K CA  1 
ATOM   6605 C C   . LEU C  2 16  ? -65.512 -13.276 39.085  1.00 41.17  ? 16   LEU K C   1 
ATOM   6606 O O   . LEU C  2 16  ? -66.460 -13.111 39.851  1.00 37.54  ? 16   LEU K O   1 
ATOM   6607 C CB  . LEU C  2 16  ? -65.782 -10.963 38.166  1.00 37.72  ? 16   LEU K CB  1 
ATOM   6608 C CG  . LEU C  2 16  ? -64.982 -9.840  37.505  1.00 37.46  ? 16   LEU K CG  1 
ATOM   6609 C CD1 . LEU C  2 16  ? -65.105 -9.912  35.993  1.00 38.46  ? 16   LEU K CD1 1 
ATOM   6610 C CD2 . LEU C  2 16  ? -65.417 -8.476  38.027  1.00 30.36  ? 16   LEU K CD2 1 
ATOM   6611 N N   . LYS C  2 39  ? -64.121 -8.422  49.597  1.00 79.52  ? 39   LYS K N   1 
ATOM   6612 C CA  . LYS C  2 39  ? -62.855 -7.704  49.698  1.00 79.39  ? 39   LYS K CA  1 
ATOM   6613 C C   . LYS C  2 39  ? -62.235 -7.486  48.316  1.00 74.72  ? 39   LYS K C   1 
ATOM   6614 O O   . LYS C  2 39  ? -61.756 -6.395  48.005  1.00 63.09  ? 39   LYS K O   1 
ATOM   6615 C CB  . LYS C  2 39  ? -61.883 -8.443  50.634  1.00 75.66  ? 39   LYS K CB  1 
ATOM   6616 C CG  . LYS C  2 39  ? -61.615 -9.914  50.278  1.00 74.19  ? 39   LYS K CG  1 
ATOM   6617 C CD  . LYS C  2 39  ? -60.206 -10.118 49.700  1.00 76.13  ? 39   LYS K CD  1 
ATOM   6618 C CE  . LYS C  2 39  ? -59.107 -9.841  50.732  1.00 69.81  ? 39   LYS K CE  1 
ATOM   6619 N NZ  . LYS C  2 39  ? -57.932 -9.140  50.123  1.00 55.31  ? 39   LYS K NZ  1 
ATOM   6620 N N   . GLN C  2 40  ? -62.268 -8.528  47.490  1.00 82.57  ? 40   GLN K N   1 
ATOM   6621 C CA  . GLN C  2 40  ? -61.690 -8.495  46.148  1.00 81.29  ? 40   GLN K CA  1 
ATOM   6622 C C   . GLN C  2 40  ? -62.125 -9.729  45.362  1.00 79.51  ? 40   GLN K C   1 
ATOM   6623 O O   . GLN C  2 40  ? -62.041 -10.851 45.867  1.00 74.43  ? 40   GLN K O   1 
ATOM   6624 C CB  . GLN C  2 40  ? -60.160 -8.454  46.219  1.00 73.06  ? 40   GLN K CB  1 
ATOM   6625 C CG  . GLN C  2 40  ? -59.474 -8.578  44.867  1.00 70.37  ? 40   GLN K CG  1 
ATOM   6626 C CD  . GLN C  2 40  ? -58.005 -8.940  44.982  1.00 75.24  ? 40   GLN K CD  1 
ATOM   6627 O OE1 . GLN C  2 40  ? -57.408 -8.834  46.054  1.00 85.99  ? 40   GLN K OE1 1 
ATOM   6628 N NE2 . GLN C  2 40  ? -57.417 -9.378  43.875  1.00 64.78  ? 40   GLN K NE2 1 
ATOM   6629 N N   . ALA C  2 41  ? -62.583 -9.522  44.130  1.00 73.12  ? 41   ALA K N   1 
ATOM   6630 C CA  . ALA C  2 41  ? -63.018 -10.623 43.273  1.00 69.56  ? 41   ALA K CA  1 
ATOM   6631 C C   . ALA C  2 41  ? -61.886 -11.094 42.366  1.00 63.15  ? 41   ALA K C   1 
ATOM   6632 O O   . ALA C  2 41  ? -60.840 -10.451 42.285  1.00 60.50  ? 41   ALA K O   1 
ATOM   6633 C CB  . ALA C  2 41  ? -64.221 -10.205 42.445  1.00 72.93  ? 41   ALA K CB  1 
ATOM   6634 N N   . ILE C  2 42  ? -62.098 -12.211 41.675  1.00 61.33  ? 42   ILE K N   1 
ATOM   6635 C CA  . ILE C  2 42  ? -61.060 -12.763 40.806  1.00 60.78  ? 42   ILE K CA  1 
ATOM   6636 C C   . ILE C  2 42  ? -61.575 -13.200 39.423  1.00 55.16  ? 42   ILE K C   1 
ATOM   6637 O O   . ILE C  2 42  ? -62.486 -14.021 39.309  1.00 47.14  ? 42   ILE K O   1 
ATOM   6638 C CB  . ILE C  2 42  ? -60.292 -13.916 41.504  1.00 49.06  ? 42   ILE K CB  1 
ATOM   6639 C CG1 . ILE C  2 42  ? -59.190 -14.465 40.594  1.00 52.67  ? 42   ILE K CG1 1 
ATOM   6640 C CG2 . ILE C  2 42  ? -61.246 -15.013 41.961  1.00 43.37  ? 42   ILE K CG2 1 
ATOM   6641 C CD1 . ILE C  2 42  ? -58.021 -13.523 40.403  1.00 51.66  ? 42   ILE K CD1 1 
ATOM   6642 N N   . GLN C  2 43  ? -60.983 -12.630 38.378  1.00 50.34  ? 43   GLN K N   1 
ATOM   6643 C CA  . GLN C  2 43  ? -61.338 -12.962 37.005  1.00 41.98  ? 43   GLN K CA  1 
ATOM   6644 C C   . GLN C  2 43  ? -60.818 -14.341 36.606  1.00 44.06  ? 43   GLN K C   1 
ATOM   6645 O O   . GLN C  2 43  ? -59.611 -14.568 36.539  1.00 48.39  ? 43   GLN K O   1 
ATOM   6646 C CB  . GLN C  2 43  ? -60.789 -11.904 36.047  1.00 45.38  ? 43   GLN K CB  1 
ATOM   6647 C CG  . GLN C  2 43  ? -60.853 -12.297 34.580  1.00 52.53  ? 43   GLN K CG  1 
ATOM   6648 C CD  . GLN C  2 43  ? -60.154 -11.298 33.673  1.00 65.00  ? 43   GLN K CD  1 
ATOM   6649 O OE1 . GLN C  2 43  ? -60.423 -11.239 32.471  1.00 73.02  ? 43   GLN K OE1 1 
ATOM   6650 N NE2 . GLN C  2 43  ? -59.248 -10.509 34.245  1.00 54.75  ? 43   GLN K NE2 1 
ATOM   6651 N N   . ILE C  2 44  ? -61.734 -15.262 36.335  1.00 42.47  ? 44   ILE K N   1 
ATOM   6652 C CA  . ILE C  2 44  ? -61.345 -16.599 35.911  1.00 46.58  ? 44   ILE K CA  1 
ATOM   6653 C C   . ILE C  2 44  ? -61.829 -16.896 34.493  1.00 46.28  ? 44   ILE K C   1 
ATOM   6654 O O   . ILE C  2 44  ? -62.669 -16.178 33.952  1.00 46.58  ? 44   ILE K O   1 
ATOM   6655 C CB  . ILE C  2 44  ? -61.912 -17.666 36.854  1.00 37.71  ? 44   ILE K CB  1 
ATOM   6656 C CG1 . ILE C  2 44  ? -63.421 -17.778 36.670  1.00 31.68  ? 44   ILE K CG1 1 
ATOM   6657 C CG2 . ILE C  2 44  ? -61.588 -17.328 38.293  1.00 40.04  ? 44   ILE K CG2 1 
ATOM   6658 C CD1 . ILE C  2 44  ? -64.041 -18.852 37.511  1.00 38.83  ? 44   ILE K CD1 1 
ATOM   6659 N N   . GLU C  2 45  ? -61.274 -17.943 33.888  1.00 42.13  ? 45   GLU K N   1 
ATOM   6660 C CA  . GLU C  2 45  ? -61.803 -18.478 32.639  1.00 36.90  ? 45   GLU K CA  1 
ATOM   6661 C C   . GLU C  2 45  ? -62.106 -19.961 32.813  1.00 32.83  ? 45   GLU K C   1 
ATOM   6662 O O   . GLU C  2 45  ? -61.301 -20.716 33.356  1.00 36.53  ? 45   GLU K O   1 
ATOM   6663 C CB  . GLU C  2 45  ? -60.845 -18.255 31.462  1.00 38.81  ? 45   GLU K CB  1 
ATOM   6664 C CG  . GLU C  2 45  ? -61.230 -19.061 30.217  1.00 36.67  ? 45   GLU K CG  1 
ATOM   6665 C CD  . GLU C  2 45  ? -60.495 -18.637 28.953  1.00 36.85  ? 45   GLU K CD  1 
ATOM   6666 O OE1 . GLU C  2 45  ? -59.628 -19.402 28.476  1.00 30.35  ? 45   GLU K OE1 1 
ATOM   6667 O OE2 . GLU C  2 45  ? -60.805 -17.549 28.421  1.00 38.90  1 45   GLU K OE2 1 
ATOM   6668 N N   . GLU C  2 46  ? -63.278 -20.373 32.355  1.00 37.01  ? 46   GLU K N   1 
ATOM   6669 C CA  . GLU C  2 46  ? -63.727 -21.736 32.558  1.00 35.86  ? 46   GLU K CA  1 
ATOM   6670 C C   . GLU C  2 46  ? -64.270 -22.334 31.263  1.00 38.26  ? 46   GLU K C   1 
ATOM   6671 O O   . GLU C  2 46  ? -65.024 -21.685 30.531  1.00 31.01  ? 46   GLU K O   1 
ATOM   6672 C CB  . GLU C  2 46  ? -64.796 -21.761 33.646  1.00 32.01  ? 46   GLU K CB  1 
ATOM   6673 C CG  . GLU C  2 46  ? -65.044 -23.117 34.256  1.00 35.22  ? 46   GLU K CG  1 
ATOM   6674 C CD  . GLU C  2 46  ? -65.977 -23.036 35.445  1.00 49.39  ? 46   GLU K CD  1 
ATOM   6675 O OE1 . GLU C  2 46  ? -67.089 -22.485 35.288  1.00 50.72  ? 46   GLU K OE1 1 
ATOM   6676 O OE2 . GLU C  2 46  ? -65.592 -23.506 36.540  1.00 53.47  1 46   GLU K OE2 1 
ATOM   6677 N N   . CYS C  2 47  ? -63.856 -23.567 30.987  1.00 35.63  ? 47   CYS K N   1 
ATOM   6678 C CA  . CYS C  2 47  ? -64.341 -24.327 29.846  1.00 29.36  ? 47   CYS K CA  1 
ATOM   6679 C C   . CYS C  2 47  ? -65.857 -24.270 29.767  1.00 42.30  ? 47   CYS K C   1 
ATOM   6680 O O   . CYS C  2 47  ? -66.542 -24.552 30.752  1.00 43.54  ? 47   CYS K O   1 
ATOM   6681 C CB  . CYS C  2 47  ? -63.913 -25.784 29.981  1.00 25.83  ? 47   CYS K CB  1 
ATOM   6682 S SG  . CYS C  2 47  ? -62.610 -26.280 28.870  1.00 16.00  ? 47   CYS K SG  1 
ATOM   6683 N N   . GLU C  2 48  ? -66.379 -23.893 28.602  1.00 43.93  ? 48   GLU K N   1 
ATOM   6684 C CA  . GLU C  2 48  ? -67.820 -23.889 28.391  1.00 40.44  ? 48   GLU K CA  1 
ATOM   6685 C C   . GLU C  2 48  ? -68.353 -25.296 28.594  1.00 39.36  ? 48   GLU K C   1 
ATOM   6686 O O   . GLU C  2 48  ? -69.321 -25.506 29.323  1.00 47.56  ? 48   GLU K O   1 
ATOM   6687 C CB  . GLU C  2 48  ? -68.165 -23.402 26.987  1.00 43.48  ? 48   GLU K CB  1 
ATOM   6688 C CG  . GLU C  2 48  ? -69.662 -23.394 26.681  1.00 50.14  ? 48   GLU K CG  1 
ATOM   6689 C CD  . GLU C  2 48  ? -70.403 -22.268 27.384  1.00 59.93  ? 48   GLU K CD  1 
ATOM   6690 O OE1 . GLU C  2 48  ? -70.638 -21.219 26.743  1.00 55.92  ? 48   GLU K OE1 1 
ATOM   6691 O OE2 . GLU C  2 48  ? -70.752 -22.431 28.574  1.00 59.15  1 48   GLU K OE2 1 
ATOM   6692 N N   . GLY C  2 49  ? -67.705 -26.259 27.953  1.00 33.56  ? 49   GLY K N   1 
ATOM   6693 C CA  . GLY C  2 49  ? -68.077 -27.650 28.106  1.00 40.43  ? 49   GLY K CA  1 
ATOM   6694 C C   . GLY C  2 49  ? -66.935 -28.476 28.658  1.00 56.19  ? 49   GLY K C   1 
ATOM   6695 O O   . GLY C  2 49  ? -65.768 -28.092 28.557  1.00 55.14  ? 49   GLY K O   1 
ATOM   6696 N N   . ALA C  2 50  ? -67.267 -29.614 29.254  1.00 62.03  ? 50   ALA K N   1 
ATOM   6697 C CA  . ALA C  2 50  ? -66.245 -30.523 29.750  1.00 60.61  ? 50   ALA K CA  1 
ATOM   6698 C C   . ALA C  2 50  ? -65.961 -31.609 28.716  1.00 50.42  ? 50   ALA K C   1 
ATOM   6699 O O   . ALA C  2 50  ? -66.844 -32.397 28.377  1.00 49.27  ? 50   ALA K O   1 
ATOM   6700 C CB  . ALA C  2 50  ? -66.670 -31.135 31.078  1.00 60.73  ? 50   ALA K CB  1 
ATOM   6701 N N   . ASP C  2 51  ? -64.731 -31.615 28.206  1.00 45.52  ? 51   ASP K N   1 
ATOM   6702 C CA  . ASP C  2 51  ? -64.251 -32.626 27.261  1.00 48.46  ? 51   ASP K CA  1 
ATOM   6703 C C   . ASP C  2 51  ? -64.892 -32.543 25.879  1.00 48.09  ? 51   ASP K C   1 
ATOM   6704 O O   . ASP C  2 51  ? -64.991 -33.543 25.164  1.00 44.23  ? 51   ASP K O   1 
ATOM   6705 C CB  . ASP C  2 51  ? -64.402 -34.037 27.837  1.00 48.59  ? 51   ASP K CB  1 
ATOM   6706 C CG  . ASP C  2 51  ? -63.810 -34.158 29.219  1.00 67.55  ? 51   ASP K CG  1 
ATOM   6707 O OD1 . ASP C  2 51  ? -62.743 -33.550 29.462  1.00 72.50  ? 51   ASP K OD1 1 
ATOM   6708 O OD2 . ASP C  2 51  ? -64.419 -34.850 30.065  1.00 71.48  1 51   ASP K OD2 1 
ATOM   6709 N N   . GLN C  2 52  ? -65.317 -31.346 25.496  1.00 43.72  ? 52   GLN K N   1 
ATOM   6710 C CA  . GLN C  2 52  ? -65.838 -31.147 24.155  1.00 44.90  ? 52   GLN K CA  1 
ATOM   6711 C C   . GLN C  2 52  ? -64.680 -31.131 23.162  1.00 39.71  ? 52   GLN K C   1 
ATOM   6712 O O   . GLN C  2 52  ? -63.625 -30.574 23.455  1.00 40.20  ? 52   GLN K O   1 
ATOM   6713 C CB  . GLN C  2 52  ? -66.634 -29.840 24.075  1.00 51.90  ? 52   GLN K CB  1 
ATOM   6714 C CG  . GLN C  2 52  ? -67.911 -29.815 24.918  1.00 51.22  ? 52   GLN K CG  1 
ATOM   6715 C CD  . GLN C  2 52  ? -69.036 -30.670 24.339  1.00 51.29  ? 52   GLN K CD  1 
ATOM   6716 O OE1 . GLN C  2 52  ? -68.918 -31.221 23.243  1.00 49.68  ? 52   GLN K OE1 1 
ATOM   6717 N NE2 . GLN C  2 52  ? -70.136 -30.779 25.080  1.00 51.85  ? 52   GLN K NE2 1 
ATOM   6718 N N   . PRO C  2 53  ? -64.868 -31.764 21.993  1.00 34.80  ? 53   PRO K N   1 
ATOM   6719 C CA  . PRO C  2 53  ? -63.894 -31.735 20.898  1.00 29.38  ? 53   PRO K CA  1 
ATOM   6720 C C   . PRO C  2 53  ? -63.480 -30.314 20.554  1.00 29.71  ? 53   PRO K C   1 
ATOM   6721 O O   . PRO C  2 53  ? -64.269 -29.385 20.714  1.00 27.75  ? 53   PRO K O   1 
ATOM   6722 C CB  . PRO C  2 53  ? -64.670 -32.341 19.735  1.00 28.79  ? 53   PRO K CB  1 
ATOM   6723 C CG  . PRO C  2 53  ? -65.595 -33.292 20.383  1.00 45.03  ? 53   PRO K CG  1 
ATOM   6724 C CD  . PRO C  2 53  ? -66.002 -32.651 21.686  1.00 48.62  ? 53   PRO K CD  1 
ATOM   6725 N N   . CYS C  2 54  ? -62.245 -30.154 20.093  1.00 30.43  ? 54   CYS K N   1 
ATOM   6726 C CA  . CYS C  2 54  ? -61.699 -28.839 19.808  1.00 22.02  ? 54   CYS K CA  1 
ATOM   6727 C C   . CYS C  2 54  ? -62.189 -28.379 18.457  1.00 16.83  ? 54   CYS K C   1 
ATOM   6728 O O   . CYS C  2 54  ? -62.559 -29.193 17.622  1.00 19.20  ? 54   CYS K O   1 
ATOM   6729 C CB  . CYS C  2 54  ? -60.175 -28.897 19.801  1.00 21.15  ? 54   CYS K CB  1 
ATOM   6730 S SG  . CYS C  2 54  ? -59.468 -29.743 21.219  1.00 27.74  ? 54   CYS K SG  1 
ATOM   6731 N N   . ASP C  2 55  ? -62.186 -27.071 18.241  1.00 17.28  ? 55   ASP K N   1 
ATOM   6732 C CA  . ASP C  2 55  ? -62.571 -26.518 16.950  1.00 19.48  ? 55   ASP K CA  1 
ATOM   6733 C C   . ASP C  2 55  ? -61.388 -26.568 15.995  1.00 16.48  ? 55   ASP K C   1 
ATOM   6734 O O   . ASP C  2 55  ? -60.249 -26.722 16.427  1.00 18.29  ? 55   ASP K O   1 
ATOM   6735 C CB  . ASP C  2 55  ? -63.048 -25.075 17.111  1.00 23.92  ? 55   ASP K CB  1 
ATOM   6736 C CG  . ASP C  2 55  ? -64.406 -24.829 16.470  1.00 21.88  ? 55   ASP K CG  1 
ATOM   6737 O OD1 . ASP C  2 55  ? -64.494 -24.836 15.219  1.00 17.33  ? 55   ASP K OD1 1 
ATOM   6738 O OD2 . ASP C  2 55  ? -65.380 -24.616 17.227  1.00 16.84  1 55   ASP K OD2 1 
ATOM   6739 N N   . PHE C  2 56  ? -61.665 -26.457 14.699  1.00 16.33  ? 56   PHE K N   1 
ATOM   6740 C CA  . PHE C  2 56  ? -60.625 -26.424 13.668  1.00 16.33  ? 56   PHE K CA  1 
ATOM   6741 C C   . PHE C  2 56  ? -59.638 -27.584 13.811  1.00 15.77  ? 56   PHE K C   1 
ATOM   6742 O O   . PHE C  2 56  ? -58.488 -27.493 13.391  1.00 17.81  ? 56   PHE K O   1 
ATOM   6743 C CB  . PHE C  2 56  ? -59.878 -25.087 13.704  1.00 14.88  ? 56   PHE K CB  1 
ATOM   6744 C CG  . PHE C  2 56  ? -60.782 -23.879 13.803  1.00 15.43  ? 56   PHE K CG  1 
ATOM   6745 C CD1 . PHE C  2 56  ? -61.290 -23.277 12.666  1.00 13.99  ? 56   PHE K CD1 1 
ATOM   6746 C CD2 . PHE C  2 56  ? -61.106 -23.336 15.034  1.00 15.00  ? 56   PHE K CD2 1 
ATOM   6747 C CE1 . PHE C  2 56  ? -62.109 -22.169 12.760  1.00 11.20  ? 56   PHE K CE1 1 
ATOM   6748 C CE2 . PHE C  2 56  ? -61.926 -22.229 15.128  1.00 13.92  ? 56   PHE K CE2 1 
ATOM   6749 C CZ  . PHE C  2 56  ? -62.424 -21.646 13.990  1.00 11.65  ? 56   PHE K CZ  1 
ATOM   6750 N N   . ALA C  2 57  ? -60.106 -28.672 14.409  1.00 12.91  ? 57   ALA K N   1 
ATOM   6751 C CA  . ALA C  2 57  ? -59.258 -29.809 14.718  1.00 13.76  ? 57   ALA K CA  1 
ATOM   6752 C C   . ALA C  2 57  ? -59.470 -30.953 13.726  1.00 17.20  ? 57   ALA K C   1 
ATOM   6753 O O   . ALA C  2 57  ? -59.467 -32.129 14.103  1.00 16.54  ? 57   ALA K O   1 
ATOM   6754 C CB  . ALA C  2 57  ? -59.540 -30.272 16.123  1.00 15.86  ? 57   ALA K CB  1 
ATOM   6755 N N   . ALA C  2 58  ? -59.649 -30.606 12.457  1.00 16.32  ? 58   ALA K N   1 
ATOM   6756 C CA  . ALA C  2 58  ? -59.942 -31.598 11.435  1.00 14.16  ? 58   ALA K CA  1 
ATOM   6757 C C   . ALA C  2 58  ? -58.667 -32.153 10.804  1.00 15.05  ? 58   ALA K C   1 
ATOM   6758 O O   . ALA C  2 58  ? -58.671 -33.247 10.234  1.00 15.12  ? 58   ALA K O   1 
ATOM   6759 C CB  . ALA C  2 58  ? -60.846 -30.997 10.368  1.00 9.46   ? 58   ALA K CB  1 
ATOM   6760 N N   . ASN C  2 59  ? -57.577 -31.399 10.910  1.00 14.03  ? 59   ASN K N   1 
ATOM   6761 C CA  . ASN C  2 59  ? -56.353 -31.740 10.190  1.00 13.25  ? 59   ASN K CA  1 
ATOM   6762 C C   . ASN C  2 59  ? -55.315 -32.484 11.026  1.00 12.78  ? 59   ASN K C   1 
ATOM   6763 O O   . ASN C  2 59  ? -54.413 -33.124 10.484  1.00 12.11  ? 59   ASN K O   1 
ATOM   6764 C CB  . ASN C  2 59  ? -55.739 -30.495 9.555   1.00 10.48  ? 59   ASN K CB  1 
ATOM   6765 C CG  . ASN C  2 59  ? -55.312 -30.728 8.126   1.00 7.22   ? 59   ASN K CG  1 
ATOM   6766 O OD1 . ASN C  2 59  ? -54.825 -31.803 7.778   1.00 6.08   ? 59   ASN K OD1 1 
ATOM   6767 N ND2 . ASN C  2 59  ? -55.496 -29.720 7.287   1.00 6.87   ? 59   ASN K ND2 1 
ATOM   6768 N N   . PHE C  2 60  ? -55.451 -32.394 12.343  1.00 14.27  ? 60   PHE K N   1 
ATOM   6769 C CA  . PHE C  2 60  ? -54.627 -33.174 13.256  1.00 14.56  ? 60   PHE K CA  1 
ATOM   6770 C C   . PHE C  2 60  ? -54.859 -34.660 13.029  1.00 15.18  ? 60   PHE K C   1 
ATOM   6771 O O   . PHE C  2 60  ? -55.972 -35.068 12.699  1.00 16.08  ? 60   PHE K O   1 
ATOM   6772 C CB  . PHE C  2 60  ? -54.933 -32.796 14.705  1.00 14.17  ? 60   PHE K CB  1 
ATOM   6773 C CG  . PHE C  2 60  ? -54.609 -31.373 15.027  1.00 13.56  ? 60   PHE K CG  1 
ATOM   6774 C CD1 . PHE C  2 60  ? -53.293 -30.944 15.063  1.00 14.19  ? 60   PHE K CD1 1 
ATOM   6775 C CD2 . PHE C  2 60  ? -55.614 -30.458 15.272  1.00 15.34  ? 60   PHE K CD2 1 
ATOM   6776 C CE1 . PHE C  2 60  ? -52.986 -29.632 15.346  1.00 14.96  ? 60   PHE K CE1 1 
ATOM   6777 C CE2 . PHE C  2 60  ? -55.313 -29.141 15.554  1.00 17.96  ? 60   PHE K CE2 1 
ATOM   6778 C CZ  . PHE C  2 60  ? -53.996 -28.728 15.593  1.00 17.45  ? 60   PHE K CZ  1 
ATOM   6779 N N   . PRO C  2 61  ? -53.801 -35.469 13.193  1.00 15.58  ? 61   PRO K N   1 
ATOM   6780 C CA  . PRO C  2 61  ? -53.854 -36.907 12.920  1.00 17.09  ? 61   PRO K CA  1 
ATOM   6781 C C   . PRO C  2 61  ? -54.967 -37.607 13.678  1.00 21.58  ? 61   PRO K C   1 
ATOM   6782 O O   . PRO C  2 61  ? -55.412 -37.131 14.725  1.00 20.03  ? 61   PRO K O   1 
ATOM   6783 C CB  . PRO C  2 61  ? -52.494 -37.397 13.410  1.00 17.88  ? 61   PRO K CB  1 
ATOM   6784 C CG  . PRO C  2 61  ? -51.609 -36.226 13.228  1.00 16.44  ? 61   PRO K CG  1 
ATOM   6785 C CD  . PRO C  2 61  ? -52.448 -35.046 13.593  1.00 15.02  ? 61   PRO K CD  1 
ATOM   6786 N N   . GLN C  2 62  ? -55.407 -38.739 13.138  1.00 24.25  ? 62   GLN K N   1 
ATOM   6787 C CA  . GLN C  2 62  ? -56.485 -39.519 13.733  1.00 29.05  ? 62   GLN K CA  1 
ATOM   6788 C C   . GLN C  2 62  ? -56.137 -39.912 15.159  1.00 27.22  ? 62   GLN K C   1 
ATOM   6789 O O   . GLN C  2 62  ? -57.009 -40.215 15.970  1.00 28.19  ? 62   GLN K O   1 
ATOM   6790 C CB  . GLN C  2 62  ? -56.741 -40.778 12.902  1.00 33.68  ? 62   GLN K CB  1 
ATOM   6791 C CG  . GLN C  2 62  ? -57.953 -41.569 13.353  1.00 30.86  ? 62   GLN K CG  1 
ATOM   6792 C CD  . GLN C  2 62  ? -59.196 -40.706 13.415  1.00 36.34  ? 62   GLN K CD  1 
ATOM   6793 O OE1 . GLN C  2 62  ? -59.683 -40.226 12.387  1.00 32.18  ? 62   GLN K OE1 1 
ATOM   6794 N NE2 . GLN C  2 62  ? -59.711 -40.489 14.624  1.00 27.95  ? 62   GLN K NE2 1 
ATOM   6795 N N   . SER C  2 63  ? -54.844 -39.890 15.450  1.00 27.63  ? 63   SER K N   1 
ATOM   6796 C CA  . SER C  2 63  ? -54.318 -40.354 16.718  1.00 26.19  ? 63   SER K CA  1 
ATOM   6797 C C   . SER C  2 63  ? -54.411 -39.279 17.791  1.00 26.76  ? 63   SER K C   1 
ATOM   6798 O O   . SER C  2 63  ? -54.721 -39.581 18.940  1.00 32.03  ? 63   SER K O   1 
ATOM   6799 C CB  . SER C  2 63  ? -52.861 -40.776 16.531  1.00 34.09  ? 63   SER K CB  1 
ATOM   6800 O OG  . SER C  2 63  ? -52.590 -41.048 15.160  1.00 33.16  ? 63   SER K OG  1 
ATOM   6801 N N   . TYR C  2 64  ? -54.157 -38.027 17.408  1.00 27.87  ? 64   TYR K N   1 
ATOM   6802 C CA  . TYR C  2 64  ? -54.036 -36.926 18.372  1.00 26.39  ? 64   TYR K CA  1 
ATOM   6803 C C   . TYR C  2 64  ? -55.272 -36.749 19.242  1.00 24.57  ? 64   TYR K C   1 
ATOM   6804 O O   . TYR C  2 64  ? -55.164 -36.299 20.380  1.00 28.04  ? 64   TYR K O   1 
ATOM   6805 C CB  . TYR C  2 64  ? -53.711 -35.595 17.681  1.00 22.27  ? 64   TYR K CB  1 
ATOM   6806 C CG  . TYR C  2 64  ? -52.294 -35.469 17.176  1.00 23.28  ? 64   TYR K CG  1 
ATOM   6807 C CD1 . TYR C  2 64  ? -51.527 -36.596 16.902  1.00 29.98  ? 64   TYR K CD1 1 
ATOM   6808 C CD2 . TYR C  2 64  ? -51.717 -34.222 16.983  1.00 23.56  ? 64   TYR K CD2 1 
ATOM   6809 C CE1 . TYR C  2 64  ? -50.226 -36.488 16.441  1.00 31.48  ? 64   TYR K CE1 1 
ATOM   6810 C CE2 . TYR C  2 64  ? -50.413 -34.101 16.521  1.00 31.14  ? 64   TYR K CE2 1 
ATOM   6811 C CZ  . TYR C  2 64  ? -49.674 -35.240 16.254  1.00 31.83  ? 64   TYR K CZ  1 
ATOM   6812 O OH  . TYR C  2 64  ? -48.381 -35.138 15.796  1.00 27.78  ? 64   TYR K OH  1 
ATOM   6813 N N   . ASN C  2 65  ? -56.430 -37.111 18.696  1.00 21.73  ? 65   ASN K N   1 
ATOM   6814 C CA  . ASN C  2 65  ? -57.710 -36.964 19.379  1.00 22.00  ? 65   ASN K CA  1 
ATOM   6815 C C   . ASN C  2 65  ? -57.798 -35.702 20.229  1.00 19.75  ? 65   ASN K C   1 
ATOM   6816 O O   . ASN C  2 65  ? -57.719 -35.773 21.454  1.00 24.39  ? 65   ASN K O   1 
ATOM   6817 C CB  . ASN C  2 65  ? -58.001 -38.202 20.230  1.00 27.57  ? 65   ASN K CB  1 
ATOM   6818 C CG  . ASN C  2 65  ? -59.347 -38.122 20.937  1.00 40.07  ? 65   ASN K CG  1 
ATOM   6819 O OD1 . ASN C  2 65  ? -59.408 -37.845 22.135  1.00 46.81  ? 65   ASN K OD1 1 
ATOM   6820 N ND2 . ASN C  2 65  ? -60.431 -38.358 20.197  1.00 23.26  ? 65   ASN K ND2 1 
ATOM   6821 N N   . PRO C  2 66  ? -57.911 -34.538 19.578  1.00 14.72  ? 66   PRO K N   1 
ATOM   6822 C CA  . PRO C  2 66  ? -57.978 -33.266 20.303  1.00 18.03  ? 66   PRO K CA  1 
ATOM   6823 C C   . PRO C  2 66  ? -59.223 -33.100 21.173  1.00 21.43  ? 66   PRO K C   1 
ATOM   6824 O O   . PRO C  2 66  ? -60.346 -33.278 20.712  1.00 24.96  ? 66   PRO K O   1 
ATOM   6825 C CB  . PRO C  2 66  ? -57.926 -32.212 19.193  1.00 15.69  ? 66   PRO K CB  1 
ATOM   6826 C CG  . PRO C  2 66  ? -58.144 -32.949 17.930  1.00 22.42  ? 66   PRO K CG  1 
ATOM   6827 C CD  . PRO C  2 66  ? -57.696 -34.341 18.138  1.00 18.29  ? 66   PRO K CD  1 
ATOM   6828 N N   . ILE C  2 67  ? -58.986 -32.755 22.437  1.00 24.15  ? 67   ILE K N   1 
ATOM   6829 C CA  . ILE C  2 67  ? -60.013 -32.599 23.458  1.00 22.35  ? 67   ILE K CA  1 
ATOM   6830 C C   . ILE C  2 67  ? -59.747 -31.285 24.181  1.00 30.50  ? 67   ILE K C   1 
ATOM   6831 O O   . ILE C  2 67  ? -58.592 -30.888 24.348  1.00 32.91  ? 67   ILE K O   1 
ATOM   6832 C CB  . ILE C  2 67  ? -59.916 -33.731 24.503  1.00 23.93  ? 67   ILE K CB  1 
ATOM   6833 C CG1 . ILE C  2 67  ? -59.950 -35.100 23.827  1.00 25.91  ? 67   ILE K CG1 1 
ATOM   6834 C CG2 . ILE C  2 67  ? -61.023 -33.622 25.537  1.00 30.30  ? 67   ILE K CG2 1 
ATOM   6835 C CD1 . ILE C  2 67  ? -61.226 -35.366 23.060  1.00 31.91  ? 67   ILE K CD1 1 
ATOM   6836 N N   . CYS C  2 68  ? -60.802 -30.603 24.611  1.00 31.27  ? 68   CYS K N   1 
ATOM   6837 C CA  . CYS C  2 68  ? -60.631 -29.378 25.386  1.00 31.64  ? 68   CYS K CA  1 
ATOM   6838 C C   . CYS C  2 68  ? -60.388 -29.697 26.857  1.00 29.07  ? 68   CYS K C   1 
ATOM   6839 O O   . CYS C  2 68  ? -61.075 -30.537 27.438  1.00 35.50  ? 68   CYS K O   1 
ATOM   6840 C CB  . CYS C  2 68  ? -61.849 -28.465 25.227  1.00 30.17  ? 68   CYS K CB  1 
ATOM   6841 S SG  . CYS C  2 68  ? -62.084 -27.858 23.540  1.00 31.02  ? 68   CYS K SG  1 
ATOM   6842 N N   . LYS C  2 69  ? -59.409 -29.028 27.457  1.00 25.47  ? 69   LYS K N   1 
ATOM   6843 C CA  . LYS C  2 69  ? -59.090 -29.256 28.864  1.00 29.52  ? 69   LYS K CA  1 
ATOM   6844 C C   . LYS C  2 69  ? -59.204 -27.987 29.705  1.00 27.09  ? 69   LYS K C   1 
ATOM   6845 O O   . LYS C  2 69  ? -59.070 -26.874 29.195  1.00 24.72  ? 69   LYS K O   1 
ATOM   6846 C CB  . LYS C  2 69  ? -57.684 -29.842 29.017  1.00 30.04  ? 69   LYS K CB  1 
ATOM   6847 C CG  . LYS C  2 69  ? -57.493 -31.213 28.400  1.00 30.74  ? 69   LYS K CG  1 
ATOM   6848 C CD  . LYS C  2 69  ? -58.310 -32.269 29.115  1.00 34.51  ? 69   LYS K CD  1 
ATOM   6849 C CE  . LYS C  2 69  ? -58.023 -33.649 28.546  1.00 47.58  ? 69   LYS K CE  1 
ATOM   6850 N NZ  . LYS C  2 69  ? -59.022 -34.653 29.006  1.00 68.21  1 69   LYS K NZ  1 
ATOM   6851 N N   . GLN C  2 70  ? -59.436 -28.176 31.001  1.00 25.92  ? 70   GLN K N   1 
ATOM   6852 C CA  . GLN C  2 70  ? -59.548 -27.074 31.946  1.00 25.46  ? 70   GLN K CA  1 
ATOM   6853 C C   . GLN C  2 70  ? -58.239 -26.871 32.708  1.00 32.24  ? 70   GLN K C   1 
ATOM   6854 O O   . GLN C  2 70  ? -57.808 -27.752 33.452  1.00 31.38  ? 70   GLN K O   1 
ATOM   6855 C CB  . GLN C  2 70  ? -60.687 -27.352 32.927  1.00 21.92  ? 70   GLN K CB  1 
ATOM   6856 C CG  . GLN C  2 70  ? -60.770 -26.375 34.080  1.00 28.18  ? 70   GLN K CG  1 
ATOM   6857 C CD  . GLN C  2 70  ? -61.138 -24.979 33.634  1.00 29.61  ? 70   GLN K CD  1 
ATOM   6858 O OE1 . GLN C  2 70  ? -62.305 -24.689 33.373  1.00 31.77  ? 70   GLN K OE1 1 
ATOM   6859 N NE2 . GLN C  2 70  ? -60.143 -24.103 33.545  1.00 27.93  ? 70   GLN K NE2 1 
ATOM   6860 N N   . HIS C  2 71  ? -57.607 -25.713 32.521  1.00 34.75  ? 71   HIS K N   1 
ATOM   6861 C CA  . HIS C  2 71  ? -56.355 -25.394 33.217  1.00 38.48  ? 71   HIS K CA  1 
ATOM   6862 C C   . HIS C  2 71  ? -56.561 -24.428 34.381  1.00 44.20  ? 71   HIS K C   1 
ATOM   6863 O O   . HIS C  2 71  ? -57.383 -23.510 34.297  1.00 46.79  ? 71   HIS K O   1 
ATOM   6864 C CB  . HIS C  2 71  ? -55.323 -24.810 32.251  1.00 38.36  ? 71   HIS K CB  1 
ATOM   6865 C CG  . HIS C  2 71  ? -54.738 -25.817 31.314  1.00 49.76  ? 71   HIS K CG  1 
ATOM   6866 N ND1 . HIS C  2 71  ? -53.524 -25.633 30.686  1.00 57.34  ? 71   HIS K ND1 1 
ATOM   6867 C CD2 . HIS C  2 71  ? -55.198 -27.022 30.900  1.00 42.40  ? 71   HIS K CD2 1 
ATOM   6868 C CE1 . HIS C  2 71  ? -53.263 -26.682 29.925  1.00 52.20  ? 71   HIS K CE1 1 
ATOM   6869 N NE2 . HIS C  2 71  ? -54.263 -27.538 30.036  1.00 46.13  ? 71   HIS K NE2 1 
ATOM   6870 N N   . TYR C  2 72  ? -55.798 -24.626 35.455  1.00 33.87  ? 72   TYR K N   1 
ATOM   6871 C CA  . TYR C  2 72  ? -55.954 -23.818 36.659  1.00 30.66  ? 72   TYR K CA  1 
ATOM   6872 C C   . TYR C  2 72  ? -54.744 -22.939 36.969  1.00 35.87  ? 72   TYR K C   1 
ATOM   6873 O O   . TYR C  2 72  ? -53.812 -22.841 36.175  1.00 37.64  ? 72   TYR K O   1 
ATOM   6874 C CB  . TYR C  2 72  ? -56.264 -24.711 37.855  1.00 31.43  ? 72   TYR K CB  1 
ATOM   6875 C CG  . TYR C  2 72  ? -57.486 -25.573 37.666  1.00 33.47  ? 72   TYR K CG  1 
ATOM   6876 C CD1 . TYR C  2 72  ? -58.749 -25.104 37.999  1.00 34.54  ? 72   TYR K CD1 1 
ATOM   6877 C CD2 . TYR C  2 72  ? -57.377 -26.860 37.158  1.00 37.16  ? 72   TYR K CD2 1 
ATOM   6878 C CE1 . TYR C  2 72  ? -59.873 -25.893 37.826  1.00 39.02  ? 72   TYR K CE1 1 
ATOM   6879 C CE2 . TYR C  2 72  ? -58.494 -27.659 36.984  1.00 35.61  ? 72   TYR K CE2 1 
ATOM   6880 C CZ  . TYR C  2 72  ? -59.738 -27.171 37.318  1.00 36.84  ? 72   TYR K CZ  1 
ATOM   6881 O OH  . TYR C  2 72  ? -60.848 -27.964 37.141  1.00 32.47  ? 72   TYR K OH  1 
ATOM   6882 N N   . THR C  2 73  ? -54.783 -22.293 38.132  1.00 43.41  ? 73   THR K N   1 
ATOM   6883 C CA  . THR C  2 73  ? -53.688 -21.449 38.612  1.00 40.04  ? 73   THR K CA  1 
ATOM   6884 C C   . THR C  2 73  ? -53.697 -21.410 40.141  1.00 44.48  ? 73   THR K C   1 
ATOM   6885 O O   . THR C  2 73  ? -54.446 -22.148 40.789  1.00 41.78  ? 73   THR K O   1 
ATOM   6886 C CB  . THR C  2 73  ? -53.768 -20.005 38.046  1.00 31.39  ? 73   THR K CB  1 
ATOM   6887 O OG1 . THR C  2 73  ? -52.795 -19.832 37.009  1.00 25.58  ? 73   THR K OG1 1 
ATOM   6888 C CG2 . THR C  2 73  ? -53.504 -18.982 39.133  1.00 32.72  ? 73   THR K CG2 1 
ATOM   6889 N N   . LYS C  2 94  ? -56.424 -23.718 44.481  1.00 38.27  ? 94   LYS K N   1 
ATOM   6890 C CA  . LYS C  2 94  ? -56.669 -24.073 43.085  1.00 47.65  ? 94   LYS K CA  1 
ATOM   6891 C C   . LYS C  2 94  ? -57.769 -23.197 42.490  1.00 54.87  ? 94   LYS K C   1 
ATOM   6892 O O   . LYS C  2 94  ? -58.771 -22.915 43.151  1.00 54.82  ? 94   LYS K O   1 
ATOM   6893 C CB  . LYS C  2 94  ? -57.052 -25.550 42.965  1.00 47.20  ? 94   LYS K CB  1 
ATOM   6894 C CG  . LYS C  2 94  ? -56.976 -26.092 41.546  1.00 42.58  ? 94   LYS K CG  1 
ATOM   6895 C CD  . LYS C  2 94  ? -57.450 -27.539 41.460  1.00 44.32  ? 94   LYS K CD  1 
ATOM   6896 C CE  . LYS C  2 94  ? -58.963 -27.645 41.622  1.00 51.76  ? 94   LYS K CE  1 
ATOM   6897 N NZ  . LYS C  2 94  ? -59.476 -29.025 41.354  1.00 47.11  1 94   LYS K NZ  1 
ATOM   6898 N N   . ILE C  2 95  ? -57.582 -22.776 41.240  1.00 50.33  ? 95   ILE K N   1 
ATOM   6899 C CA  . ILE C  2 95  ? -58.506 -21.837 40.598  1.00 45.57  ? 95   ILE K CA  1 
ATOM   6900 C C   . ILE C  2 95  ? -58.326 -21.787 39.075  1.00 45.89  ? 95   ILE K C   1 
ATOM   6901 O O   . ILE C  2 95  ? -57.204 -21.641 38.590  1.00 43.71  ? 95   ILE K O   1 
ATOM   6902 C CB  . ILE C  2 95  ? -58.342 -20.413 41.190  1.00 44.19  ? 95   ILE K CB  1 
ATOM   6903 C CG1 . ILE C  2 95  ? -59.126 -19.388 40.376  1.00 37.86  ? 95   ILE K CG1 1 
ATOM   6904 C CG2 . ILE C  2 95  ? -56.866 -20.013 41.260  1.00 43.00  ? 95   ILE K CG2 1 
ATOM   6905 C CD1 . ILE C  2 95  ? -58.931 -17.977 40.855  1.00 34.16  ? 95   ILE K CD1 1 
ATOM   6906 N N   . PRO C  2 96  ? -59.436 -21.914 38.320  1.00 45.58  ? 96   PRO K N   1 
ATOM   6907 C CA  . PRO C  2 96  ? -59.444 -21.855 36.851  1.00 37.07  ? 96   PRO K CA  1 
ATOM   6908 C C   . PRO C  2 96  ? -58.695 -20.643 36.303  1.00 40.90  ? 96   PRO K C   1 
ATOM   6909 O O   . PRO C  2 96  ? -58.744 -19.568 36.901  1.00 45.97  ? 96   PRO K O   1 
ATOM   6910 C CB  . PRO C  2 96  ? -60.930 -21.739 36.523  1.00 32.68  ? 96   PRO K CB  1 
ATOM   6911 C CG  . PRO C  2 96  ? -61.601 -22.460 37.628  1.00 34.82  ? 96   PRO K CG  1 
ATOM   6912 C CD  . PRO C  2 96  ? -60.785 -22.169 38.859  1.00 43.73  ? 96   PRO K CD  1 
ATOM   6913 N N   . SER C  2 97  ? -58.007 -20.819 35.179  1.00 39.80  ? 97   SER K N   1 
ATOM   6914 C CA  . SER C  2 97  ? -57.189 -19.748 34.614  1.00 42.56  ? 97   SER K CA  1 
ATOM   6915 C C   . SER C  2 97  ? -57.498 -19.542 33.141  1.00 31.46  ? 97   SER K C   1 
ATOM   6916 O O   . SER C  2 97  ? -57.547 -18.409 32.655  1.00 26.65  ? 97   SER K O   1 
ATOM   6917 C CB  . SER C  2 97  ? -55.694 -20.043 34.808  1.00 44.21  ? 97   SER K CB  1 
ATOM   6918 O OG  . SER C  2 97  ? -55.278 -21.194 34.085  1.00 42.09  ? 97   SER K OG  1 
ATOM   6919 N N   . CYS C  2 98  ? -57.698 -20.653 32.443  1.00 29.72  ? 98   CYS K N   1 
ATOM   6920 C CA  . CYS C  2 98  ? -58.047 -20.633 31.030  1.00 37.95  ? 98   CYS K CA  1 
ATOM   6921 C C   . CYS C  2 98  ? -58.397 -22.037 30.559  1.00 34.14  ? 98   CYS K C   1 
ATOM   6922 O O   . CYS C  2 98  ? -58.337 -22.997 31.333  1.00 30.93  ? 98   CYS K O   1 
ATOM   6923 C CB  . CYS C  2 98  ? -56.903 -20.076 30.182  1.00 38.33  ? 98   CYS K CB  1 
ATOM   6924 S SG  . CYS C  2 98  ? -55.665 -21.305 29.755  1.00 45.66  ? 98   CYS K SG  1 
ATOM   6925 N N   . CYS C  2 99  ? -58.751 -22.148 29.282  1.00 27.98  ? 99   CYS K N   1 
ATOM   6926 C CA  . CYS C  2 99  ? -59.203 -23.410 28.716  1.00 26.56  ? 99   CYS K CA  1 
ATOM   6927 C C   . CYS C  2 99  ? -58.495 -23.688 27.394  1.00 26.30  ? 99   CYS K C   1 
ATOM   6928 O O   . CYS C  2 99  ? -58.683 -22.959 26.421  1.00 27.65  ? 99   CYS K O   1 
ATOM   6929 C CB  . CYS C  2 99  ? -60.716 -23.369 28.513  1.00 24.79  ? 99   CYS K CB  1 
ATOM   6930 S SG  . CYS C  2 99  ? -61.439 -24.913 27.945  1.00 20.71  ? 99   CYS K SG  1 
ATOM   6931 N N   . LYS C  2 100 ? -57.686 -24.744 27.362  1.00 23.07  ? 100  LYS K N   1 
ATOM   6932 C CA  . LYS C  2 100 ? -56.845 -25.030 26.201  1.00 21.77  ? 100  LYS K CA  1 
ATOM   6933 C C   . LYS C  2 100 ? -57.205 -26.352 25.526  1.00 23.24  ? 100  LYS K C   1 
ATOM   6934 O O   . LYS C  2 100 ? -57.790 -27.242 26.145  1.00 20.93  ? 100  LYS K O   1 
ATOM   6935 C CB  . LYS C  2 100 ? -55.366 -25.031 26.597  1.00 24.12  ? 100  LYS K CB  1 
ATOM   6936 C CG  . LYS C  2 100 ? -54.972 -23.877 27.505  1.00 29.07  ? 100  LYS K CG  1 
ATOM   6937 C CD  . LYS C  2 100 ? -53.602 -23.297 27.159  1.00 35.35  ? 100  LYS K CD  1 
ATOM   6938 C CE  . LYS C  2 100 ? -52.449 -24.105 27.732  1.00 35.29  ? 100  LYS K CE  1 
ATOM   6939 N NZ  . LYS C  2 100 ? -51.140 -23.495 27.360  1.00 28.52  1 100  LYS K NZ  1 
ATOM   6940 N N   . CYS C  2 101 ? -56.861 -26.467 24.247  1.00 22.27  ? 101  CYS K N   1 
ATOM   6941 C CA  . CYS C  2 101 ? -57.093 -27.699 23.508  1.00 22.31  ? 101  CYS K CA  1 
ATOM   6942 C C   . CYS C  2 101 ? -55.870 -28.593 23.645  1.00 27.15  ? 101  CYS K C   1 
ATOM   6943 O O   . CYS C  2 101 ? -54.738 -28.106 23.643  1.00 23.93  ? 101  CYS K O   1 
ATOM   6944 C CB  . CYS C  2 101 ? -57.377 -27.406 22.037  1.00 22.69  ? 101  CYS K CB  1 
ATOM   6945 S SG  . CYS C  2 101 ? -57.627 -28.894 21.038  1.00 37.92  ? 101  CYS K SG  1 
ATOM   6946 N N   . ALA C  2 102 ? -56.095 -29.899 23.759  1.00 26.22  ? 102  ALA K N   1 
ATOM   6947 C CA  . ALA C  2 102 ? -55.026 -30.807 24.162  1.00 27.26  ? 102  ALA K CA  1 
ATOM   6948 C C   . ALA C  2 102 ? -54.870 -32.024 23.264  1.00 21.07  ? 102  ALA K C   1 
ATOM   6949 O O   . ALA C  2 102 ? -55.669 -32.955 23.312  1.00 18.65  ? 102  ALA K O   1 
ATOM   6950 C CB  . ALA C  2 102 ? -55.222 -31.242 25.609  1.00 32.62  ? 102  ALA K CB  1 
ATOM   6951 N N   . LEU C  2 103 ? -53.810 -32.014 22.468  1.00 21.38  ? 103  LEU K N   1 
ATOM   6952 C CA  . LEU C  2 103 ? -53.530 -33.100 21.549  1.00 25.07  ? 103  LEU K CA  1 
ATOM   6953 C C   . LEU C  2 103 ? -52.737 -34.180 22.267  1.00 32.20  ? 103  LEU K C   1 
ATOM   6954 O O   . LEU C  2 103 ? -51.984 -33.888 23.196  1.00 33.35  ? 103  LEU K O   1 
ATOM   6955 C CB  . LEU C  2 103 ? -52.725 -32.578 20.358  1.00 23.16  ? 103  LEU K CB  1 
ATOM   6956 C CG  . LEU C  2 103 ? -52.909 -31.092 20.044  1.00 22.12  ? 103  LEU K CG  1 
ATOM   6957 C CD1 . LEU C  2 103 ? -51.722 -30.559 19.266  1.00 22.24  ? 103  LEU K CD1 1 
ATOM   6958 C CD2 . LEU C  2 103 ? -54.205 -30.850 19.281  1.00 21.89  ? 103  LEU K CD2 1 
ATOM   6959 N N   . LYS C  2 104 ? -52.906 -35.425 21.830  1.00 36.49  ? 104  LYS K N   1 
ATOM   6960 C CA  . LYS C  2 104 ? -52.148 -36.546 22.378  1.00 31.99  ? 104  LYS K CA  1 
ATOM   6961 C C   . LYS C  2 104 ? -50.966 -36.901 21.487  1.00 32.32  ? 104  LYS K C   1 
ATOM   6962 O O   . LYS C  2 104 ? -51.122 -37.602 20.489  1.00 28.26  ? 104  LYS K O   1 
ATOM   6963 C CB  . LYS C  2 104 ? -53.042 -37.774 22.560  1.00 26.25  ? 104  LYS K CB  1 
ATOM   6964 C CG  . LYS C  2 104 ? -53.724 -37.864 23.922  1.00 38.57  ? 104  LYS K CG  1 
ATOM   6965 C CD  . LYS C  2 104 ? -54.681 -36.699 24.171  1.00 42.89  ? 104  LYS K CD  1 
ATOM   6966 C CE  . LYS C  2 104 ? -55.172 -36.686 25.615  1.00 49.73  ? 104  LYS K CE  1 
ATOM   6967 N NZ  . LYS C  2 104 ? -56.095 -35.547 25.893  1.00 56.54  1 104  LYS K NZ  1 
ATOM   6968 N N   . THR C  2 105 ? -49.787 -36.406 21.855  1.00 42.80  ? 105  THR K N   1 
ATOM   6969 C CA  . THR C  2 105 ? -48.554 -36.718 21.137  1.00 50.24  ? 105  THR K CA  1 
ATOM   6970 C C   . THR C  2 105 ? -47.334 -36.469 22.026  1.00 59.76  ? 105  THR K C   1 
ATOM   6971 O O   . THR C  2 105 ? -47.468 -36.245 23.232  1.00 57.43  ? 105  THR K O   1 
ATOM   6972 C CB  . THR C  2 105 ? -48.423 -35.890 19.841  1.00 45.68  ? 105  THR K CB  1 
ATOM   6973 O OG1 . THR C  2 105 ? -47.268 -36.322 19.110  1.00 51.88  ? 105  THR K OG1 1 
ATOM   6974 C CG2 . THR C  2 105 ? -48.300 -34.400 20.158  1.00 39.05  ? 105  THR K CG2 1 
ATOM   6975 N N   . GLY C  2 106 ? -46.146 -36.511 21.429  1.00 61.13  ? 106  GLY K N   1 
ATOM   6976 C CA  . GLY C  2 106 ? -44.917 -36.244 22.156  1.00 62.29  ? 106  GLY K CA  1 
ATOM   6977 C C   . GLY C  2 106 ? -44.538 -34.775 22.130  1.00 57.60  ? 106  GLY K C   1 
ATOM   6978 O O   . GLY C  2 106 ? -44.971 -34.029 21.251  1.00 49.56  ? 106  GLY K O   1 
ATOM   6979 N N   . LEU C  2 107 ? -43.730 -34.357 23.101  1.00 60.38  ? 107  LEU K N   1 
ATOM   6980 C CA  . LEU C  2 107 ? -43.260 -32.975 23.159  1.00 61.18  ? 107  LEU K CA  1 
ATOM   6981 C C   . LEU C  2 107 ? -41.981 -32.787 22.348  1.00 60.22  ? 107  LEU K C   1 
ATOM   6982 O O   . LEU C  2 107 ? -41.886 -33.240 21.206  1.00 56.64  ? 107  LEU K O   1 
ATOM   6983 C CB  . LEU C  2 107 ? -43.042 -32.535 24.609  1.00 57.49  ? 107  LEU K CB  1 
ATOM   6984 C CG  . LEU C  2 107 ? -44.297 -32.138 25.393  1.00 49.20  ? 107  LEU K CG  1 
ATOM   6985 C CD1 . LEU C  2 107 ? -43.980 -31.951 26.868  1.00 44.29  ? 107  LEU K CD1 1 
ATOM   6986 C CD2 . LEU C  2 107 ? -44.904 -30.867 24.817  1.00 48.76  ? 107  LEU K CD2 1 
HETATM 6987 C C1  . NAG D  3 .   ? -40.492 -21.733 5.304   1.00 20.56  ? 2001 NAG A C1  1 
HETATM 6988 C C2  . NAG D  3 .   ? -41.333 -21.146 6.450   1.00 22.97  ? 2001 NAG A C2  1 
HETATM 6989 C C3  . NAG D  3 .   ? -40.640 -19.926 7.061   1.00 25.16  ? 2001 NAG A C3  1 
HETATM 6990 C C4  . NAG D  3 .   ? -39.199 -20.240 7.437   1.00 27.59  ? 2001 NAG A C4  1 
HETATM 6991 C C5  . NAG D  3 .   ? -38.464 -20.824 6.234   1.00 20.99  ? 2001 NAG A C5  1 
HETATM 6992 C C6  . NAG D  3 .   ? -37.051 -21.249 6.551   1.00 18.88  ? 2001 NAG A C6  1 
HETATM 6993 C C7  . NAG D  3 .   ? -43.747 -21.528 6.285   1.00 24.49  ? 2001 NAG A C7  1 
HETATM 6994 C C8  . NAG D  3 .   ? -45.047 -21.021 5.749   1.00 21.43  ? 2001 NAG A C8  1 
HETATM 6995 N N2  . NAG D  3 .   ? -42.668 -20.794 5.996   1.00 23.44  ? 2001 NAG A N2  1 
HETATM 6996 O O3  . NAG D  3 .   ? -41.338 -19.487 8.220   1.00 23.87  ? 2001 NAG A O3  1 
HETATM 6997 O O4  . NAG D  3 .   ? -38.561 -19.029 7.839   1.00 31.34  ? 2001 NAG A O4  1 
HETATM 6998 O O5  . NAG D  3 .   ? -39.148 -21.996 5.771   1.00 20.93  ? 2001 NAG A O5  1 
HETATM 6999 O O6  . NAG D  3 .   ? -37.013 -22.562 7.091   1.00 16.02  ? 2001 NAG A O6  1 
HETATM 7000 O O7  . NAG D  3 .   ? -43.674 -22.560 6.948   1.00 31.07  ? 2001 NAG A O7  1 
HETATM 7001 C C1  . NAG E  3 .   ? -38.184 -18.975 9.247   1.00 28.96  ? 2002 NAG A C1  1 
HETATM 7002 C C2  . NAG E  3 .   ? -37.007 -18.035 9.306   1.00 27.45  ? 2002 NAG A C2  1 
HETATM 7003 C C3  . NAG E  3 .   ? -36.458 -17.986 10.720  1.00 24.87  ? 2002 NAG A C3  1 
HETATM 7004 C C4  . NAG E  3 .   ? -37.556 -17.699 11.738  1.00 26.91  ? 2002 NAG A C4  1 
HETATM 7005 C C5  . NAG E  3 .   ? -38.855 -18.483 11.482  1.00 37.89  ? 2002 NAG A C5  1 
HETATM 7006 C C6  . NAG E  3 .   ? -40.055 -17.878 12.185  1.00 46.81  ? 2002 NAG A C6  1 
HETATM 7007 C C7  . NAG E  3 .   ? -35.282 -17.596 7.608   1.00 30.49  ? 2002 NAG A C7  1 
HETATM 7008 C C8  . NAG E  3 .   ? -35.621 -16.154 7.776   1.00 27.42  ? 2002 NAG A C8  1 
HETATM 7009 N N2  . NAG E  3 .   ? -35.973 -18.449 8.369   1.00 32.09  ? 2002 NAG A N2  1 
HETATM 7010 O O3  . NAG E  3 .   ? -35.480 -16.958 10.799  1.00 30.73  ? 2002 NAG A O3  1 
HETATM 7011 O O4  . NAG E  3 .   ? -37.042 -18.012 13.030  1.00 23.97  ? 2002 NAG A O4  1 
HETATM 7012 O O5  . NAG E  3 .   ? -39.196 -18.500 10.085  1.00 35.19  ? 2002 NAG A O5  1 
HETATM 7013 O O6  . NAG E  3 .   ? -40.293 -18.427 13.476  1.00 49.54  ? 2002 NAG A O6  1 
HETATM 7014 O O7  . NAG E  3 .   ? -34.417 -17.980 6.816   1.00 35.89  ? 2002 NAG A O7  1 
HETATM 7015 C C1  . BMA F  4 .   ? -37.063 -16.853 13.867  1.00 24.25  ? 2003 BMA A C1  1 
HETATM 7016 C C2  . BMA F  4 .   ? -37.564 -17.209 15.274  1.00 29.91  ? 2003 BMA A C2  1 
HETATM 7017 C C3  . BMA F  4 .   ? -37.909 -15.890 15.888  1.00 34.00  ? 2003 BMA A C3  1 
HETATM 7018 C C4  . BMA F  4 .   ? -36.617 -15.042 16.031  1.00 29.02  ? 2003 BMA A C4  1 
HETATM 7019 C C5  . BMA F  4 .   ? -35.981 -14.816 14.613  1.00 24.09  ? 2003 BMA A C5  1 
HETATM 7020 C C6  . BMA F  4 .   ? -34.587 -14.162 14.677  1.00 25.26  ? 2003 BMA A C6  1 
HETATM 7021 O O2  . BMA F  4 .   ? -36.518 -17.738 16.054  1.00 29.07  ? 2003 BMA A O2  1 
HETATM 7022 O O3  . BMA F  4 .   ? -38.784 -15.930 17.085  1.00 36.69  ? 2003 BMA A O3  1 
HETATM 7023 O O4  . BMA F  4 .   ? -36.918 -13.795 16.617  1.00 35.38  ? 2003 BMA A O4  1 
HETATM 7024 O O5  . BMA F  4 .   ? -35.866 -16.093 13.914  1.00 20.44  ? 2003 BMA A O5  1 
HETATM 7025 O O6  . BMA F  4 .   ? -34.284 -13.477 13.450  1.00 15.10  ? 2003 BMA A O6  1 
HETATM 7026 C C1  . BMA G  4 .   ? -38.477 -16.833 18.161  1.00 32.79  ? 2004 BMA A C1  1 
HETATM 7027 C C2  . BMA G  4 .   ? -38.013 -15.921 19.266  1.00 41.16  ? 2004 BMA A C2  1 
HETATM 7028 C C3  . BMA G  4 .   ? -38.809 -16.166 20.586  1.00 38.98  ? 2004 BMA A C3  1 
HETATM 7029 C C4  . BMA G  4 .   ? -39.060 -17.668 20.899  1.00 36.14  ? 2004 BMA A C4  1 
HETATM 7030 C C5  . BMA G  4 .   ? -39.397 -18.482 19.651  1.00 37.82  ? 2004 BMA A C5  1 
HETATM 7031 C C6  . BMA G  4 .   ? -40.644 -19.327 19.873  1.00 38.51  ? 2004 BMA A C6  1 
HETATM 7032 O O2  . BMA G  4 .   ? -38.240 -14.573 18.861  1.00 43.41  ? 2004 BMA A O2  1 
HETATM 7033 O O3  . BMA G  4 .   ? -40.016 -15.381 20.695  1.00 30.59  ? 2004 BMA A O3  1 
HETATM 7034 O O4  . BMA G  4 .   ? -37.921 -18.232 21.535  1.00 40.90  ? 2004 BMA A O4  1 
HETATM 7035 O O5  . BMA G  4 .   ? -39.611 -17.588 18.540  1.00 38.03  ? 2004 BMA A O5  1 
HETATM 7036 O O6  . BMA G  4 .   ? -40.769 -20.259 18.813  1.00 43.97  ? 2004 BMA A O6  1 
HETATM 7037 C C1  . MAN H  5 .   ? -39.691 -14.193 21.438  1.00 31.20  ? 2005 MAN A C1  1 
HETATM 7038 C C2  . MAN H  5 .   ? -40.801 -13.817 22.456  1.00 39.28  ? 2005 MAN A C2  1 
HETATM 7039 C C3  . MAN H  5 .   ? -41.911 -12.939 21.814  1.00 36.22  ? 2005 MAN A C3  1 
HETATM 7040 C C4  . MAN H  5 .   ? -41.343 -11.840 20.875  1.00 38.72  ? 2005 MAN A C4  1 
HETATM 7041 C C5  . MAN H  5 .   ? -40.363 -12.454 19.864  1.00 33.23  ? 2005 MAN A C5  1 
HETATM 7042 C C6  . MAN H  5 .   ? -39.713 -11.403 18.964  1.00 30.23  ? 2005 MAN A C6  1 
HETATM 7043 O O2  . MAN H  5 .   ? -40.280 -13.077 23.579  1.00 46.15  ? 2005 MAN A O2  1 
HETATM 7044 O O3  . MAN H  5 .   ? -42.750 -12.350 22.809  1.00 29.01  ? 2005 MAN A O3  1 
HETATM 7045 O O4  . MAN H  5 .   ? -42.406 -11.181 20.173  1.00 32.21  ? 2005 MAN A O4  1 
HETATM 7046 O O5  . MAN H  5 .   ? -39.303 -13.134 20.581  1.00 30.19  ? 2005 MAN A O5  1 
HETATM 7047 O O6  . MAN H  5 .   ? -39.376 -12.002 17.711  1.00 30.02  ? 2005 MAN A O6  1 
HETATM 7048 C C1  . NAG I  3 .   ? -69.127 -40.498 -5.193  1.00 55.00  ? 2006 NAG A C1  1 
HETATM 7049 C C2  . NAG I  3 .   ? -69.527 -41.558 -6.224  1.00 64.75  ? 2006 NAG A C2  1 
HETATM 7050 C C3  . NAG I  3 .   ? -70.097 -42.793 -5.527  1.00 63.64  ? 2006 NAG A C3  1 
HETATM 7051 C C4  . NAG I  3 .   ? -69.133 -43.292 -4.458  1.00 63.10  ? 2006 NAG A C4  1 
HETATM 7052 C C5  . NAG I  3 .   ? -68.792 -42.157 -3.500  1.00 50.33  ? 2006 NAG A C5  1 
HETATM 7053 C C6  . NAG I  3 .   ? -67.791 -42.556 -2.442  1.00 40.98  ? 2006 NAG A C6  1 
HETATM 7054 C C7  . NAG I  3 .   ? -70.227 -40.892 -8.482  1.00 62.35  ? 2006 NAG A C7  1 
HETATM 7055 C C8  . NAG I  3 .   ? -71.328 -40.305 -9.315  1.00 66.59  ? 2006 NAG A C8  1 
HETATM 7056 N N2  . NAG I  3 .   ? -70.485 -41.018 -7.175  1.00 60.10  ? 2006 NAG A N2  1 
HETATM 7057 O O3  . NAG I  3 .   ? -70.321 -43.817 -6.490  1.00 59.48  ? 2006 NAG A O3  1 
HETATM 7058 O O4  . NAG I  3 .   ? -69.716 -44.361 -3.722  1.00 75.74  ? 2006 NAG A O4  1 
HETATM 7059 O O5  . NAG I  3 .   ? -68.217 -41.069 -4.239  1.00 57.46  ? 2006 NAG A O5  1 
HETATM 7060 O O6  . NAG I  3 .   ? -67.985 -43.904 -2.035  1.00 36.61  ? 2006 NAG A O6  1 
HETATM 7061 O O7  . NAG I  3 .   ? -69.154 -41.241 -8.970  1.00 48.57  ? 2006 NAG A O7  1 
HETATM 7062 C C1  . NAG J  3 .   ? -77.485 -20.148 33.718  1.00 33.78  ? 2007 NAG A C1  1 
HETATM 7063 C C2  . NAG J  3 .   ? -76.154 -20.795 34.088  1.00 33.69  ? 2007 NAG A C2  1 
HETATM 7064 C C3  . NAG J  3 .   ? -76.370 -22.245 34.512  1.00 30.63  ? 2007 NAG A C3  1 
HETATM 7065 C C4  . NAG J  3 .   ? -77.438 -22.333 35.595  1.00 30.78  ? 2007 NAG A C4  1 
HETATM 7066 C C5  . NAG J  3 .   ? -78.702 -21.599 35.157  1.00 29.89  ? 2007 NAG A C5  1 
HETATM 7067 C C6  . NAG J  3 .   ? -79.752 -21.537 36.239  1.00 35.65  ? 2007 NAG A C6  1 
HETATM 7068 C C7  . NAG J  3 .   ? -74.170 -19.889 32.971  1.00 41.75  ? 2007 NAG A C7  1 
HETATM 7069 C C8  . NAG J  3 .   ? -73.306 -19.934 31.746  1.00 39.82  ? 2007 NAG A C8  1 
HETATM 7070 N N2  . NAG J  3 .   ? -75.216 -20.721 32.980  1.00 32.98  ? 2007 NAG A N2  1 
HETATM 7071 O O3  . NAG J  3 .   ? -75.141 -22.776 34.995  1.00 28.82  ? 2007 NAG A O3  1 
HETATM 7072 O O4  . NAG J  3 .   ? -77.763 -23.695 35.845  1.00 34.60  ? 2007 NAG A O4  1 
HETATM 7073 O O5  . NAG J  3 .   ? -78.382 -20.244 34.813  1.00 33.18  ? 2007 NAG A O5  1 
HETATM 7074 O O6  . NAG J  3 .   ? -80.067 -22.836 36.720  1.00 49.94  ? 2007 NAG A O6  1 
HETATM 7075 O O7  . NAG J  3 .   ? -73.931 -19.134 33.911  1.00 43.47  ? 2007 NAG A O7  1 
HETATM 7076 C C1  . NAG K  3 .   ? -31.184 -43.723 23.384  1.00 35.45  ? 2008 NAG A C1  1 
HETATM 7077 C C2  . NAG K  3 .   ? -32.439 -43.772 24.249  1.00 38.23  ? 2008 NAG A C2  1 
HETATM 7078 C C3  . NAG K  3 .   ? -33.116 -45.135 24.127  1.00 43.53  ? 2008 NAG A C3  1 
HETATM 7079 C C4  . NAG K  3 .   ? -33.308 -45.548 22.671  1.00 46.05  ? 2008 NAG A C4  1 
HETATM 7080 C C5  . NAG K  3 .   ? -32.049 -45.308 21.835  1.00 43.48  ? 2008 NAG A C5  1 
HETATM 7081 C C6  . NAG K  3 .   ? -32.300 -45.452 20.350  1.00 53.24  ? 2008 NAG A C6  1 
HETATM 7082 C C7  . NAG K  3 .   ? -31.982 -42.244 26.116  1.00 34.21  ? 2008 NAG A C7  1 
HETATM 7083 C C8  . NAG K  3 .   ? -31.677 -42.135 27.579  1.00 32.31  ? 2008 NAG A C8  1 
HETATM 7084 N N2  . NAG K  3 .   ? -32.134 -43.484 25.641  1.00 35.18  ? 2008 NAG A N2  1 
HETATM 7085 O O3  . NAG K  3 .   ? -34.375 -45.086 24.789  1.00 37.18  ? 2008 NAG A O3  1 
HETATM 7086 O O4  . NAG K  3 .   ? -33.521 -46.954 22.647  1.00 61.54  ? 2008 NAG A O4  1 
HETATM 7087 O O5  . NAG K  3 .   ? -31.530 -43.986 22.041  1.00 37.96  ? 2008 NAG A O5  1 
HETATM 7088 O O6  . NAG K  3 .   ? -31.340 -44.742 19.579  1.00 53.85  ? 2008 NAG A O6  1 
HETATM 7089 O O7  . NAG K  3 .   ? -32.068 -41.255 25.393  1.00 26.52  ? 2008 NAG A O7  1 
HETATM 7090 C C1  . NAG L  3 .   ? -34.783 -47.451 22.155  1.00 61.85  ? 2009 NAG A C1  1 
HETATM 7091 C C2  . NAG L  3 .   ? -36.007 -46.582 22.444  1.00 60.95  ? 2009 NAG A C2  1 
HETATM 7092 C C3  . NAG L  3 .   ? -36.934 -46.558 21.226  1.00 66.17  ? 2009 NAG A C3  1 
HETATM 7093 C C4  . NAG L  3 .   ? -37.099 -47.954 20.633  1.00 68.99  ? 2009 NAG A C4  1 
HETATM 7094 C C5  . NAG L  3 .   ? -35.738 -48.554 20.282  1.00 67.46  ? 2009 NAG A C5  1 
HETATM 7095 C C6  . NAG L  3 .   ? -35.519 -48.718 18.796  1.00 65.42  ? 2009 NAG A C6  1 
HETATM 7096 C C7  . NAG L  3 .   ? -37.390 -46.276 24.467  1.00 60.81  ? 2009 NAG A C7  1 
HETATM 7097 C C8  . NAG L  3 .   ? -37.400 -44.809 24.147  1.00 57.28  ? 2009 NAG A C8  1 
HETATM 7098 N N2  . NAG L  3 .   ? -36.716 -47.064 23.620  1.00 63.16  ? 2009 NAG A N2  1 
HETATM 7099 O O3  . NAG L  3 .   ? -36.394 -45.674 20.251  1.00 78.18  ? 2009 NAG A O3  1 
HETATM 7100 O O4  . NAG L  3 .   ? -37.774 -48.810 21.548  1.00 68.39  ? 2009 NAG A O4  1 
HETATM 7101 O O5  . NAG L  3 .   ? -34.693 -47.697 20.760  1.00 57.44  ? 2009 NAG A O5  1 
HETATM 7102 O O6  . NAG L  3 .   ? -34.178 -49.096 18.514  1.00 56.11  ? 2009 NAG A O6  1 
HETATM 7103 O O7  . NAG L  3 .   ? -37.971 -46.730 25.449  1.00 59.54  ? 2009 NAG A O7  1 
HETATM 7104 C C1  . NAG M  3 .   ? -27.867 -31.936 31.222  1.00 25.65  ? 2010 NAG A C1  1 
HETATM 7105 C C2  . NAG M  3 .   ? -28.593 -30.915 32.097  1.00 27.74  ? 2010 NAG A C2  1 
HETATM 7106 C C3  . NAG M  3 .   ? -29.204 -31.600 33.317  1.00 36.11  ? 2010 NAG A C3  1 
HETATM 7107 C C4  . NAG M  3 .   ? -30.049 -32.800 32.906  1.00 32.56  ? 2010 NAG A C4  1 
HETATM 7108 C C5  . NAG M  3 .   ? -29.244 -33.708 31.978  1.00 25.45  ? 2010 NAG A C5  1 
HETATM 7109 C C6  . NAG M  3 .   ? -30.049 -34.855 31.419  1.00 29.46  ? 2010 NAG A C6  1 
HETATM 7110 C C7  . NAG M  3 .   ? -27.422 -28.777 31.766  1.00 43.81  ? 2010 NAG A C7  1 
HETATM 7111 C C8  . NAG M  3 .   ? -26.475 -27.782 32.370  1.00 46.58  ? 2010 NAG A C8  1 
HETATM 7112 N N2  . NAG M  3 .   ? -27.695 -29.851 32.515  1.00 37.40  ? 2010 NAG A N2  1 
HETATM 7113 O O3  . NAG M  3 .   ? -29.984 -30.653 34.040  1.00 45.63  ? 2010 NAG A O3  1 
HETATM 7114 O O4  . NAG M  3 .   ? -30.406 -33.569 34.051  1.00 39.65  ? 2010 NAG A O4  1 
HETATM 7115 O O5  . NAG M  3 .   ? -28.759 -32.960 30.856  1.00 20.51  ? 2010 NAG A O5  1 
HETATM 7116 O O6  . NAG M  3 .   ? -30.018 -35.973 32.294  1.00 39.99  ? 2010 NAG A O6  1 
HETATM 7117 O O7  . NAG M  3 .   ? -27.913 -28.616 30.650  1.00 36.80  ? 2010 NAG A O7  1 
HETATM 7118 C C1  . NAG N  3 .   ? -31.597 -33.174 34.771  1.00 37.19  ? 2011 NAG A C1  1 
HETATM 7119 C C2  . NAG N  3 .   ? -31.751 -34.141 35.922  1.00 44.96  ? 2011 NAG A C2  1 
HETATM 7120 C C3  . NAG N  3 .   ? -33.089 -33.917 36.617  1.00 57.39  ? 2011 NAG A C3  1 
HETATM 7121 C C4  . NAG N  3 .   ? -33.257 -32.451 37.008  1.00 62.04  ? 2011 NAG A C4  1 
HETATM 7122 C C5  . NAG N  3 .   ? -32.884 -31.496 35.865  1.00 52.04  ? 2011 NAG A C5  1 
HETATM 7123 C C6  . NAG N  3 .   ? -32.737 -30.063 36.323  1.00 53.40  ? 2011 NAG A C6  1 
HETATM 7124 C C7  . NAG N  3 .   ? -32.387 -36.118 34.584  1.00 37.23  ? 2011 NAG A C7  1 
HETATM 7125 C C8  . NAG N  3 .   ? -32.057 -37.548 34.279  1.00 41.80  ? 2011 NAG A C8  1 
HETATM 7126 N N2  . NAG N  3 .   ? -31.604 -35.522 35.490  1.00 36.10  ? 2011 NAG A N2  1 
HETATM 7127 O O3  . NAG N  3 .   ? -33.160 -34.737 37.778  1.00 60.11  ? 2011 NAG A O3  1 
HETATM 7128 O O4  . NAG N  3 .   ? -34.619 -32.225 37.357  1.00 66.75  ? 2011 NAG A O4  1 
HETATM 7129 O O5  . NAG N  3 .   ? -31.628 -31.855 35.264  1.00 43.42  ? 2011 NAG A O5  1 
HETATM 7130 O O6  . NAG N  3 .   ? -33.933 -29.571 36.913  1.00 66.80  ? 2011 NAG A O6  1 
HETATM 7131 O O7  . NAG N  3 .   ? -33.321 -35.538 34.041  1.00 47.63  ? 2011 NAG A O7  1 
HETATM 7132 C C1  . BMA O  4 .   ? -34.810 -31.996 38.769  1.00 62.80  ? 2012 BMA A C1  1 
HETATM 7133 C C2  . BMA O  4 .   ? -36.264 -31.541 38.980  1.00 65.76  ? 2012 BMA A C2  1 
HETATM 7134 C C3  . BMA O  4 .   ? -36.492 -31.220 40.460  1.00 71.81  ? 2012 BMA A C3  1 
HETATM 7135 C C4  . BMA O  4 .   ? -36.031 -32.393 41.353  1.00 70.28  ? 2012 BMA A C4  1 
HETATM 7136 C C5  . BMA O  4 .   ? -34.568 -32.767 41.022  1.00 61.28  ? 2012 BMA A C5  1 
HETATM 7137 C C6  . BMA O  4 .   ? -34.069 -33.959 41.823  1.00 63.91  ? 2012 BMA A C6  1 
HETATM 7138 O O2  . BMA O  4 .   ? -37.164 -32.588 38.628  1.00 51.76  ? 2012 BMA A O2  1 
HETATM 7139 O O3  . BMA O  4 .   ? -37.857 -30.871 40.736  1.00 63.61  ? 2012 BMA A O3  1 
HETATM 7140 O O4  . BMA O  4 .   ? -36.139 -32.046 42.727  1.00 63.42  ? 2012 BMA A O4  1 
HETATM 7141 O O5  . BMA O  4 .   ? -34.469 -33.082 39.611  1.00 57.29  ? 2012 BMA A O5  1 
HETATM 7142 O O6  . BMA O  4 .   ? -34.944 -35.060 41.593  1.00 59.76  ? 2012 BMA A O6  1 
HETATM 7143 C C1  . NAG P  3 .   ? -87.258 -24.524 12.251  1.00 38.21  ? 2013 NAG A C1  1 
HETATM 7144 C C2  . NAG P  3 .   ? -87.890 -25.155 13.492  1.00 39.26  ? 2013 NAG A C2  1 
HETATM 7145 C C3  . NAG P  3 .   ? -88.098 -26.655 13.281  1.00 46.62  ? 2013 NAG A C3  1 
HETATM 7146 C C4  . NAG P  3 .   ? -88.861 -26.925 11.985  1.00 49.68  ? 2013 NAG A C4  1 
HETATM 7147 C C5  . NAG P  3 .   ? -88.195 -26.196 10.819  1.00 41.18  ? 2013 NAG A C5  1 
HETATM 7148 C C6  . NAG P  3 .   ? -88.984 -26.296 9.534   1.00 50.14  ? 2013 NAG A C6  1 
HETATM 7149 C C7  . NAG P  3 .   ? -87.421 -24.107 15.671  1.00 33.34  ? 2013 NAG A C7  1 
HETATM 7150 C C8  . NAG P  3 .   ? -88.759 -23.441 15.542  1.00 25.70  ? 2013 NAG A C8  1 
HETATM 7151 N N2  . NAG P  3 .   ? -87.065 -24.916 14.665  1.00 38.09  ? 2013 NAG A N2  1 
HETATM 7152 O O3  . NAG P  3 .   ? -88.790 -27.173 14.412  1.00 42.24  ? 2013 NAG A O3  1 
HETATM 7153 O O4  . NAG P  3 .   ? -88.860 -28.314 11.662  1.00 66.76  ? 2013 NAG A O4  1 
HETATM 7154 O O5  . NAG P  3 .   ? -88.066 -24.798 11.113  1.00 40.35  ? 2013 NAG A O5  1 
HETATM 7155 O O6  . NAG P  3 .   ? -88.215 -26.881 8.493   1.00 55.00  ? 2013 NAG A O6  1 
HETATM 7156 O O7  . NAG P  3 .   ? -86.692 -23.921 16.642  1.00 36.99  ? 2013 NAG A O7  1 
HETATM 7157 C C1  . NAG Q  3 .   ? -89.811 -29.145 12.376  1.00 74.19  ? 2014 NAG A C1  1 
HETATM 7158 C C2  . NAG Q  3 .   ? -90.866 -29.740 11.432  1.00 66.30  ? 2014 NAG A C2  1 
HETATM 7159 C C3  . NAG Q  3 .   ? -91.822 -30.645 12.209  1.00 68.54  ? 2014 NAG A C3  1 
HETATM 7160 C C4  . NAG Q  3 .   ? -91.039 -31.703 12.976  1.00 73.44  ? 2014 NAG A C4  1 
HETATM 7161 C C5  . NAG Q  3 .   ? -90.012 -31.027 13.880  1.00 75.02  ? 2014 NAG A C5  1 
HETATM 7162 C C6  . NAG Q  3 .   ? -89.136 -32.005 14.629  1.00 60.95  ? 2014 NAG A C6  1 
HETATM 7163 C C7  . NAG Q  3 .   ? -92.063 -28.844 9.484   1.00 78.12  ? 2014 NAG A C7  1 
HETATM 7164 C C8  . NAG Q  3 .   ? -92.796 -27.667 8.912   1.00 65.77  ? 2014 NAG A C8  1 
HETATM 7165 N N2  . NAG Q  3 .   ? -91.601 -28.699 10.732  1.00 69.18  ? 2014 NAG A N2  1 
HETATM 7166 O O3  . NAG Q  3 .   ? -92.736 -31.267 11.314  1.00 81.92  ? 2014 NAG A O3  1 
HETATM 7167 O O4  . NAG Q  3 .   ? -91.922 -32.500 13.759  1.00 73.26  ? 2014 NAG A O4  1 
HETATM 7168 O O5  . NAG Q  3 .   ? -89.139 -30.209 13.085  1.00 79.57  ? 2014 NAG A O5  1 
HETATM 7169 O O6  . NAG Q  3 .   ? -88.799 -31.523 15.924  1.00 47.04  ? 2014 NAG A O6  1 
HETATM 7170 O O7  . NAG Q  3 .   ? -91.898 -29.880 8.846   1.00 83.58  ? 2014 NAG A O7  1 
HETATM 7171 C C1  . NAG R  3 .   ? -57.985 -15.399 -13.649 1.00 35.25  ? 2015 NAG A C1  1 
HETATM 7172 C C2  . NAG R  3 .   ? -57.180 -14.121 -13.839 1.00 42.23  ? 2015 NAG A C2  1 
HETATM 7173 C C3  . NAG R  3 .   ? -57.374 -13.570 -15.256 1.00 49.68  ? 2015 NAG A C3  1 
HETATM 7174 C C4  . NAG R  3 .   ? -57.125 -14.654 -16.304 1.00 51.86  ? 2015 NAG A C4  1 
HETATM 7175 C C5  . NAG R  3 .   ? -57.925 -15.910 -15.963 1.00 41.20  ? 2015 NAG A C5  1 
HETATM 7176 C C6  . NAG R  3 .   ? -57.634 -17.068 -16.889 1.00 42.54  ? 2015 NAG A C6  1 
HETATM 7177 C C7  . NAG R  3 .   ? -56.680 -12.591 -11.987 1.00 42.22  ? 2015 NAG A C7  1 
HETATM 7178 C C8  . NAG R  3 .   ? -57.239 -11.582 -11.031 1.00 38.98  ? 2015 NAG A C8  1 
HETATM 7179 N N2  . NAG R  3 .   ? -57.552 -13.125 -12.847 1.00 36.61  ? 2015 NAG A N2  1 
HETATM 7180 O O3  . NAG R  3 .   ? -56.483 -12.473 -15.428 1.00 41.92  ? 2015 NAG A O3  1 
HETATM 7181 O O4  . NAG R  3 .   ? -57.537 -14.234 -17.603 1.00 48.88  ? 2015 NAG A O4  1 
HETATM 7182 O O5  . NAG R  3 .   ? -57.611 -16.347 -14.634 1.00 34.95  ? 2015 NAG A O5  1 
HETATM 7183 O O6  . NAG R  3 .   ? -58.096 -16.802 -18.206 1.00 44.79  ? 2015 NAG A O6  1 
HETATM 7184 O O7  . NAG R  3 .   ? -55.494 -12.913 -11.977 1.00 49.34  ? 2015 NAG A O7  1 
HETATM 7185 C C1  . NAG S  3 .   ? -56.629 -13.340 -18.293 1.00 53.01  ? 2016 NAG A C1  1 
HETATM 7186 C C2  . NAG S  3 .   ? -55.391 -14.047 -18.861 1.00 59.41  ? 2016 NAG A C2  1 
HETATM 7187 C C3  . NAG S  3 .   ? -55.359 -13.914 -20.383 1.00 66.33  ? 2016 NAG A C3  1 
HETATM 7188 C C4  . NAG S  3 .   ? -56.719 -14.237 -20.976 1.00 57.96  ? 2016 NAG A C4  1 
HETATM 7189 C C5  . NAG S  3 .   ? -57.746 -13.218 -20.491 1.00 63.62  ? 2016 NAG A C5  1 
HETATM 7190 C C6  . NAG S  3 .   ? -59.079 -13.832 -20.122 1.00 59.11  ? 2016 NAG A C6  1 
HETATM 7191 C C7  . NAG S  3 .   ? -53.234 -14.303 -17.718 1.00 60.87  ? 2016 NAG A C7  1 
HETATM 7192 C C8  . NAG S  3 .   ? -53.519 -15.777 -17.717 1.00 54.04  ? 2016 NAG A C8  1 
HETATM 7193 N N2  . NAG S  3 .   ? -54.172 -13.526 -18.276 1.00 60.07  ? 2016 NAG A N2  1 
HETATM 7194 O O3  . NAG S  3 .   ? -54.362 -14.777 -20.926 1.00 75.48  ? 2016 NAG A O3  1 
HETATM 7195 O O4  . NAG S  3 .   ? -56.653 -14.195 -22.398 1.00 48.88  ? 2016 NAG A O4  1 
HETATM 7196 O O5  . NAG S  3 .   ? -57.254 -12.518 -19.332 1.00 62.22  ? 2016 NAG A O5  1 
HETATM 7197 O O6  . NAG S  3 .   ? -60.092 -12.844 -19.994 1.00 49.54  ? 2016 NAG A O6  1 
HETATM 7198 O O7  . NAG S  3 .   ? -52.207 -13.839 -17.237 1.00 70.53  ? 2016 NAG A O7  1 
HETATM 7199 C C1  . NAG T  3 .   ? 0.309   -61.367 76.047  1.00 53.04  ? 2017 NAG A C1  1 
HETATM 7200 C C2  . NAG T  3 .   ? 0.354   -62.860 76.371  1.00 55.08  ? 2017 NAG A C2  1 
HETATM 7201 C C3  . NAG T  3 .   ? -1.000  -63.321 76.905  1.00 49.87  ? 2017 NAG A C3  1 
HETATM 7202 C C4  . NAG T  3 .   ? -1.443  -62.435 78.061  1.00 50.37  ? 2017 NAG A C4  1 
HETATM 7203 C C5  . NAG T  3 .   ? -1.390  -60.968 77.648  1.00 55.40  ? 2017 NAG A C5  1 
HETATM 7204 C C6  . NAG T  3 .   ? -1.718  -60.017 78.774  1.00 66.12  ? 2017 NAG A C6  1 
HETATM 7205 C C7  . NAG T  3 .   ? 2.003   -63.932 74.894  1.00 59.23  ? 2017 NAG A C7  1 
HETATM 7206 C C8  . NAG T  3 .   ? 2.208   -64.732 73.644  1.00 47.80  ? 2017 NAG A C8  1 
HETATM 7207 N N2  . NAG T  3 .   ? 0.734   -63.634 75.199  1.00 62.36  ? 2017 NAG A N2  1 
HETATM 7208 O O3  . NAG T  3 .   ? -0.925  -64.677 77.328  1.00 50.65  ? 2017 NAG A O3  1 
HETATM 7209 O O4  . NAG T  3 .   ? -2.783  -62.744 78.418  1.00 55.62  ? 2017 NAG A O4  1 
HETATM 7210 O O5  . NAG T  3 .   ? -0.068  -60.643 77.200  1.00 51.14  ? 2017 NAG A O5  1 
HETATM 7211 O O6  . NAG T  3 .   ? -2.634  -59.014 78.353  1.00 69.08  ? 2017 NAG A O6  1 
HETATM 7212 O O7  . NAG T  3 .   ? 2.944   -63.571 75.596  1.00 63.46  ? 2017 NAG A O7  1 
HETATM 7213 C C1  . NAG U  3 .   ? -2.843  -63.493 79.642  1.00 57.07  ? 2018 NAG A C1  1 
HETATM 7214 C C2  . NAG U  3 .   ? -4.141  -64.279 79.638  1.00 54.38  ? 2018 NAG A C2  1 
HETATM 7215 C C3  . NAG U  3 .   ? -4.321  -64.981 80.981  1.00 52.81  ? 2018 NAG A C3  1 
HETATM 7216 C C4  . NAG U  3 .   ? -3.098  -65.835 81.294  1.00 62.19  ? 2018 NAG A C4  1 
HETATM 7217 C C5  . NAG U  3 .   ? -1.817  -65.007 81.178  1.00 61.69  ? 2018 NAG A C5  1 
HETATM 7218 C C6  . NAG U  3 .   ? -0.562  -65.836 81.323  1.00 56.92  ? 2018 NAG A C6  1 
HETATM 7219 C C7  . NAG U  3 .   ? -5.824  -63.285 78.136  1.00 54.98  ? 2018 NAG A C7  1 
HETATM 7220 C C8  . NAG U  3 .   ? -5.230  -64.132 77.048  1.00 51.75  ? 2018 NAG A C8  1 
HETATM 7221 N N2  . NAG U  3 .   ? -5.269  -63.406 79.351  1.00 59.19  ? 2018 NAG A N2  1 
HETATM 7222 O O3  . NAG U  3 .   ? -5.485  -65.799 80.957  1.00 48.29  ? 2018 NAG A O3  1 
HETATM 7223 O O4  . NAG U  3 .   ? -3.200  -66.364 82.611  1.00 68.65  ? 2018 NAG A O4  1 
HETATM 7224 O O5  . NAG U  3 .   ? -1.750  -64.377 79.888  1.00 64.79  ? 2018 NAG A O5  1 
HETATM 7225 O O6  . NAG U  3 .   ? -0.624  -67.018 80.535  1.00 50.13  ? 2018 NAG A O6  1 
HETATM 7226 O O7  . NAG U  3 .   ? -6.772  -62.532 77.927  1.00 39.77  ? 2018 NAG A O7  1 
HETATM 7227 C C1  . NAG V  3 .   ? -29.807 -18.906 -3.718  1.00 45.48  ? 2019 NAG A C1  1 
HETATM 7228 C C2  . NAG V  3 .   ? -28.877 -19.416 -4.852  1.00 49.66  ? 2019 NAG A C2  1 
HETATM 7229 C C3  . NAG V  3 .   ? -28.690 -18.349 -5.947  1.00 54.53  ? 2019 NAG A C3  1 
HETATM 7230 C C4  . NAG V  3 .   ? -30.033 -17.774 -6.380  1.00 55.96  ? 2019 NAG A C4  1 
HETATM 7231 C C5  . NAG V  3 .   ? -30.769 -17.265 -5.153  1.00 50.63  ? 2019 NAG A C5  1 
HETATM 7232 C C6  . NAG V  3 .   ? -32.109 -16.646 -5.460  1.00 49.84  ? 2019 NAG A C6  1 
HETATM 7233 C C7  . NAG V  3 .   ? -26.807 -19.208 -3.485  1.00 46.16  ? 2019 NAG A C7  1 
HETATM 7234 C C8  . NAG V  3 .   ? -25.532 -19.884 -3.102  1.00 46.70  ? 2019 NAG A C8  1 
HETATM 7235 N N2  . NAG V  3 .   ? -27.589 -19.882 -4.345  1.00 44.77  ? 2019 NAG A N2  1 
HETATM 7236 O O3  . NAG V  3 .   ? -28.064 -18.931 -7.085  1.00 59.49  ? 2019 NAG A O3  1 
HETATM 7237 O O4  . NAG V  3 .   ? -29.853 -16.709 -7.309  1.00 61.28  ? 2019 NAG A O4  1 
HETATM 7238 O O5  . NAG V  3 .   ? -31.011 -18.372 -4.279  1.00 44.84  ? 2019 NAG A O5  1 
HETATM 7239 O O6  . NAG V  3 .   ? -32.520 -15.817 -4.382  1.00 55.85  ? 2019 NAG A O6  1 
HETATM 7240 O O7  . NAG V  3 .   ? -27.111 -18.101 -3.037  1.00 52.56  ? 2019 NAG A O7  1 
HETATM 7241 C C1  . NAG W  3 .   ? -30.197 -17.123 -8.659  1.00 61.93  ? 2020 NAG A C1  1 
HETATM 7242 C C2  . NAG W  3 .   ? -29.571 -16.181 -9.689  1.00 62.73  ? 2020 NAG A C2  1 
HETATM 7243 C C3  . NAG W  3 .   ? -29.989 -16.581 -11.102 1.00 58.99  ? 2020 NAG A C3  1 
HETATM 7244 C C4  . NAG W  3 .   ? -29.741 -18.063 -11.352 1.00 63.77  ? 2020 NAG A C4  1 
HETATM 7245 C C5  . NAG W  3 .   ? -30.306 -18.925 -10.217 1.00 60.42  ? 2020 NAG A C5  1 
HETATM 7246 C C6  . NAG W  3 .   ? -29.898 -20.379 -10.311 1.00 52.28  ? 2020 NAG A C6  1 
HETATM 7247 C C7  . NAG W  3 .   ? -29.314 -14.029 -8.537  1.00 62.30  ? 2020 NAG A C7  1 
HETATM 7248 C C8  . NAG W  3 .   ? -29.820 -12.623 -8.412  1.00 60.49  ? 2020 NAG A C8  1 
HETATM 7249 N N2  . NAG W  3 .   ? -29.942 -14.800 -9.430  1.00 61.20  ? 2020 NAG A N2  1 
HETATM 7250 O O3  . NAG W  3 .   ? -29.235 -15.810 -12.031 1.00 49.46  ? 2020 NAG A O3  1 
HETATM 7251 O O4  . NAG W  3 .   ? -30.351 -18.418 -12.590 1.00 52.33  ? 2020 NAG A O4  1 
HETATM 7252 O O5  . NAG W  3 .   ? -29.825 -18.456 -8.948  1.00 52.96  ? 2020 NAG A O5  1 
HETATM 7253 O O6  . NAG W  3 .   ? -29.962 -20.862 -11.646 1.00 66.48  ? 2020 NAG A O6  1 
HETATM 7254 O O7  . NAG W  3 .   ? -28.387 -14.451 -7.854  1.00 50.64  ? 2020 NAG A O7  1 
HETATM 7255 C C1  . NAG X  3 .   ? -17.890 -47.953 25.627  1.00 55.52  ? 2021 NAG A C1  1 
HETATM 7256 C C2  . NAG X  3 .   ? -17.438 -48.217 24.176  1.00 57.23  ? 2021 NAG A C2  1 
HETATM 7257 C C3  . NAG X  3 .   ? -16.651 -49.530 24.060  1.00 68.99  ? 2021 NAG A C3  1 
HETATM 7258 C C4  . NAG X  3 .   ? -15.567 -49.626 25.124  1.00 68.75  ? 2021 NAG A C4  1 
HETATM 7259 C C5  . NAG X  3 .   ? -16.199 -49.388 26.491  1.00 70.44  ? 2021 NAG A C5  1 
HETATM 7260 C C6  . NAG X  3 .   ? -15.221 -49.456 27.640  1.00 80.57  ? 2021 NAG A C6  1 
HETATM 7261 C C7  . NAG X  3 .   ? -19.569 -49.150 23.337  1.00 64.66  ? 2021 NAG A C7  1 
HETATM 7262 C C8  . NAG X  3 .   ? -20.653 -48.993 22.310  1.00 65.84  ? 2021 NAG A C8  1 
HETATM 7263 N N2  . NAG X  3 .   ? -18.586 -48.240 23.285  1.00 58.90  ? 2021 NAG A N2  1 
HETATM 7264 O O3  . NAG X  3 .   ? -16.067 -49.597 22.765  1.00 83.29  ? 2021 NAG A O3  1 
HETATM 7265 O O4  . NAG X  3 .   ? -14.951 -50.910 25.074  1.00 75.57  ? 2021 NAG A O4  1 
HETATM 7266 O O5  . NAG X  3 .   ? -16.778 -48.077 26.514  1.00 62.09  ? 2021 NAG A O5  1 
HETATM 7267 O O6  . NAG X  3 .   ? -15.076 -50.785 28.122  1.00 77.62  ? 2021 NAG A O6  1 
HETATM 7268 O O7  . NAG X  3 .   ? -19.594 -50.046 24.179  1.00 57.18  ? 2021 NAG A O7  1 
HETATM 7269 C C1  . NAG Y  3 .   ? -73.256 -0.538  2.771   1.00 47.52  ? 2022 NAG A C1  1 
HETATM 7270 C C2  . NAG Y  3 .   ? -74.695 -0.132  3.187   1.00 44.07  ? 2022 NAG A C2  1 
HETATM 7271 C C3  . NAG Y  3 .   ? -74.747 1.199   3.966   1.00 50.50  ? 2022 NAG A C3  1 
HETATM 7272 C C4  . NAG Y  3 .   ? -73.794 2.271   3.439   1.00 53.62  ? 2022 NAG A C4  1 
HETATM 7273 C C5  . NAG Y  3 .   ? -72.609 1.664   2.705   1.00 48.98  ? 2022 NAG A C5  1 
HETATM 7274 C C6  . NAG Y  3 .   ? -71.343 2.460   2.900   1.00 54.34  ? 2022 NAG A C6  1 
HETATM 7275 C C7  . NAG Y  3 .   ? -76.356 -1.152  1.709   1.00 51.60  ? 2022 NAG A C7  1 
HETATM 7276 C C8  . NAG Y  3 .   ? -76.216 -2.370  2.573   1.00 33.80  ? 2022 NAG A C8  1 
HETATM 7277 N N2  . NAG Y  3 .   ? -75.601 -0.104  2.052   1.00 48.06  ? 2022 NAG A N2  1 
HETATM 7278 O O3  . NAG Y  3 .   ? -74.501 0.950   5.343   1.00 52.12  ? 2022 NAG A O3  1 
HETATM 7279 O O4  . NAG Y  3 .   ? -74.470 3.249   2.655   1.00 53.69  ? 2022 NAG A O4  1 
HETATM 7280 O O5  . NAG Y  3 .   ? -72.365 0.367   3.248   1.00 46.33  ? 2022 NAG A O5  1 
HETATM 7281 O O6  . NAG Y  3 .   ? -70.348 2.111   1.948   1.00 54.04  ? 2022 NAG A O6  1 
HETATM 7282 O O7  . NAG Y  3 .   ? -77.123 -1.117  0.750   1.00 63.44  ? 2022 NAG A O7  1 
HETATM 7283 C C1  . NAG Z  3 .   ? -3.471  -63.952 62.222  1.00 70.17  ? 2023 NAG A C1  1 
HETATM 7284 C C2  . NAG Z  3 .   ? -4.512  -64.152 61.115  1.00 67.50  ? 2023 NAG A C2  1 
HETATM 7285 C C3  . NAG Z  3 .   ? -4.057  -65.248 60.140  1.00 63.97  ? 2023 NAG A C3  1 
HETATM 7286 C C4  . NAG Z  3 .   ? -2.624  -65.009 59.671  1.00 69.67  ? 2023 NAG A C4  1 
HETATM 7287 C C5  . NAG Z  3 .   ? -1.692  -64.731 60.848  1.00 61.84  ? 2023 NAG A C5  1 
HETATM 7288 C C6  . NAG Z  3 .   ? -0.301  -64.324 60.420  1.00 47.88  ? 2023 NAG A C6  1 
HETATM 7289 C C7  . NAG Z  3 .   ? -6.948  -64.541 60.990  1.00 57.41  ? 2023 NAG A C7  1 
HETATM 7290 C C8  . NAG Z  3 .   ? -8.179  -64.877 61.780  1.00 43.80  ? 2023 NAG A C8  1 
HETATM 7291 N N2  . NAG Z  3 .   ? -5.811  -64.473 61.689  1.00 60.61  ? 2023 NAG A N2  1 
HETATM 7292 O O3  . NAG Z  3 .   ? -4.933  -65.269 59.016  1.00 39.62  ? 2023 NAG A O3  1 
HETATM 7293 O O4  . NAG Z  3 .   ? -2.130  -66.159 58.991  1.00 84.41  ? 2023 NAG A O4  1 
HETATM 7294 O O5  . NAG Z  3 .   ? -2.209  -63.654 61.641  1.00 69.86  ? 2023 NAG A O5  1 
HETATM 7295 O O6  . NAG Z  3 .   ? 0.080   -64.953 59.204  1.00 41.59  ? 2023 NAG A O6  1 
HETATM 7296 O O7  . NAG Z  3 .   ? -6.982  -64.355 59.776  1.00 60.36  ? 2023 NAG A O7  1 
HETATM 7297 N N1  . EPE AA 6 .   ? -69.949 -31.405 12.279  1.00 36.46  ? 2024 EPE A N1  1 
HETATM 7298 C C2  . EPE AA 6 .   ? -69.254 -32.693 12.436  1.00 47.69  ? 2024 EPE A C2  1 
HETATM 7299 C C3  . EPE AA 6 .   ? -69.112 -33.318 11.053  1.00 45.19  ? 2024 EPE A C3  1 
HETATM 7300 N N4  . EPE AA 6 .   ? -70.045 -32.720 10.112  1.00 35.89  ? 2024 EPE A N4  1 
HETATM 7301 C C5  . EPE AA 6 .   ? -71.379 -32.358 10.557  1.00 28.51  ? 2024 EPE A C5  1 
HETATM 7302 C C6  . EPE AA 6 .   ? -71.349 -31.660 11.910  1.00 28.46  ? 2024 EPE A C6  1 
HETATM 7303 C C7  . EPE AA 6 .   ? -69.794 -32.856 8.691   1.00 25.69  ? 2024 EPE A C7  1 
HETATM 7304 C C8  . EPE AA 6 .   ? -70.812 -33.765 8.017   1.00 27.70  ? 2024 EPE A C8  1 
HETATM 7305 O O8  . EPE AA 6 .   ? -70.891 -34.976 8.735   1.00 39.39  ? 2024 EPE A O8  1 
HETATM 7306 C C9  . EPE AA 6 .   ? -69.872 -30.617 13.520  1.00 33.94  ? 2024 EPE A C9  1 
HETATM 7307 C C10 . EPE AA 6 .   ? -70.876 -31.115 14.553  1.00 31.45  ? 2024 EPE A C10 1 
HETATM 7308 S S   . EPE AA 6 .   ? -71.775 -29.743 15.321  1.00 40.29  ? 2024 EPE A S   1 
HETATM 7309 O O1S . EPE AA 6 .   ? -73.054 -30.244 15.822  1.00 39.35  ? 2024 EPE A O1S 1 
HETATM 7310 O O2S . EPE AA 6 .   ? -70.998 -29.214 16.436  1.00 34.84  ? 2024 EPE A O2S 1 
HETATM 7311 O O3S . EPE AA 6 .   ? -72.007 -28.673 14.345  1.00 27.15  ? 2024 EPE A O3S 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   SER 1   28  28  SER SER A . n 
A 1 2   PHE 2   29  29  PHE PHE A . n 
A 1 3   GLY 3   30  30  GLY GLY A . n 
A 1 4   ARG 4   31  31  ARG ARG A . n 
A 1 5   ASP 5   32  32  ASP ASP A . n 
A 1 6   ALA 6   33  33  ALA ALA A . n 
A 1 7   CYS 7   34  34  CYS CYS A . n 
A 1 8   SER 8   35  35  SER SER A . n 
A 1 9   GLU 9   36  36  GLU GLU A . n 
A 1 10  MET 10  37  ?   ?   ?   A . n 
A 1 11  SER 11  38  ?   ?   ?   A . n 
A 1 12  ILE 12  39  ?   ?   ?   A . n 
A 1 13  ASP 13  40  40  ASP ASP A . n 
A 1 14  GLY 14  41  41  GLY GLY A . n 
A 1 15  LEU 15  42  42  LEU LEU A . n 
A 1 16  CYS 16  43  43  CYS CYS A . n 
A 1 17  GLN 17  44  44  GLN GLN A . n 
A 1 18  CYS 18  45  45  CYS CYS A . n 
A 1 19  ALA 19  46  46  ALA ALA A . n 
A 1 20  PRO 20  47  47  PRO PRO A . n 
A 1 21  ILE 21  48  48  ILE ILE A . n 
A 1 22  MET 22  49  49  MET MET A . n 
A 1 23  SER 23  50  50  SER SER A . n 
A 1 24  GLU 24  51  51  GLU GLU A . n 
A 1 25  TYR 25  52  52  TYR TYR A . n 
A 1 26  GLU 26  53  53  GLU GLU A . n 
A 1 27  ILE 27  54  54  ILE ILE A . n 
A 1 28  ILE 28  55  55  ILE ILE A . n 
A 1 29  CYS 29  56  56  CYS CYS A . n 
A 1 30  PRO 30  57  57  PRO PRO A . n 
A 1 31  ALA 31  58  58  ALA ALA A . n 
A 1 32  ASN 32  59  59  ASN ASN A . n 
A 1 33  ALA 33  60  60  ALA ALA A . n 
A 1 34  GLU 34  61  61  GLU GLU A . n 
A 1 35  ASN 35  62  62  ASN ASN A . n 
A 1 36  PRO 36  63  63  PRO PRO A . n 
A 1 37  THR 37  64  64  THR THR A . n 
A 1 38  PHE 38  65  65  PHE PHE A . n 
A 1 39  ARG 39  66  66  ARG ARG A . n 
A 1 40  LEU 40  67  67  LEU LEU A . n 
A 1 41  THR 41  68  68  THR THR A . n 
A 1 42  ILE 42  69  69  ILE ILE A . n 
A 1 43  GLN 43  70  70  GLN GLN A . n 
A 1 44  PRO 44  71  71  PRO PRO A . n 
A 1 45  LYS 45  72  72  LYS LYS A . n 
A 1 46  ASP 46  73  73  ASP ASP A . n 
A 1 47  TYR 47  74  74  TYR TYR A . n 
A 1 48  VAL 48  75  75  VAL VAL A . n 
A 1 49  GLN 49  76  76  GLN GLN A . n 
A 1 50  ILE 50  77  77  ILE ILE A . n 
A 1 51  MET 51  78  78  MET MET A . n 
A 1 52  CYS 52  79  79  CYS CYS A . n 
A 1 53  ASN 53  80  80  ASN ASN A . n 
A 1 54  LEU 54  81  81  LEU LEU A . n 
A 1 55  THR 55  82  82  THR THR A . n 
A 1 56  ASP 56  83  83  ASP ASP A . n 
A 1 57  THR 57  84  84  THR THR A . n 
A 1 58  THR 58  85  85  THR THR A . n 
A 1 59  ASP 59  86  86  ASP ASP A . n 
A 1 60  TYR 60  87  87  TYR TYR A . n 
A 1 61  GLN 61  88  88  GLN GLN A . n 
A 1 62  GLN 62  89  89  GLN GLN A . n 
A 1 63  LEU 63  90  90  LEU LEU A . n 
A 1 64  PRO 64  91  91  PRO PRO A . n 
A 1 65  LYS 65  92  92  LYS LYS A . n 
A 1 66  LYS 66  93  93  LYS LYS A . n 
A 1 67  LEU 67  94  94  LEU LEU A . n 
A 1 68  ARG 68  95  95  ARG ARG A . n 
A 1 69  ILE 69  96  96  ILE ILE A . n 
A 1 70  GLY 70  97  97  GLY GLY A . n 
A 1 71  GLU 71  98  98  GLU GLU A . n 
A 1 72  VAL 72  99  99  VAL VAL A . n 
A 1 73  ASP 73  100 100 ASP ASP A . n 
A 1 74  ARG 74  101 101 ARG ARG A . n 
A 1 75  VAL 75  102 102 VAL VAL A . n 
A 1 76  GLN 76  103 103 GLN GLN A . n 
A 1 77  MET 77  104 104 MET MET A . n 
A 1 78  ARG 78  105 105 ARG ARG A . n 
A 1 79  ARG 79  106 106 ARG ARG A . n 
A 1 80  CYS 80  107 107 CYS CYS A . n 
A 1 81  MET 81  108 108 MET MET A . n 
A 1 82  LEU 82  109 109 LEU LEU A . n 
A 1 83  PRO 83  110 110 PRO PRO A . n 
A 1 84  GLY 84  111 111 GLY GLY A . n 
A 1 85  HIS 85  112 112 HIS HIS A . n 
A 1 86  THR 86  113 113 THR THR A . n 
A 1 87  PRO 87  114 114 PRO PRO A . n 
A 1 88  ILE 88  115 115 ILE ILE A . n 
A 1 89  ALA 89  116 116 ALA ALA A . n 
A 1 90  SER 90  117 117 SER SER A . n 
A 1 91  ILE 91  118 118 ILE ILE A . n 
A 1 92  LEU 92  119 119 LEU LEU A . n 
A 1 93  ASP 93  120 120 ASP ASP A . n 
A 1 94  TYR 94  121 121 TYR TYR A . n 
A 1 95  LEU 95  122 122 LEU LEU A . n 
A 1 96  GLY 96  123 123 GLY GLY A . n 
A 1 97  ILE 97  124 124 ILE ILE A . n 
A 1 98  VAL 98  125 125 VAL VAL A . n 
A 1 99  SER 99  126 126 SER SER A . n 
A 1 100 PRO 100 127 127 PRO PRO A . n 
A 1 101 THR 101 128 128 THR THR A . n 
A 1 102 THR 102 129 129 THR THR A . n 
A 1 103 LEU 103 130 130 LEU LEU A . n 
A 1 104 ILE 104 131 131 ILE ILE A . n 
A 1 105 PHE 105 132 132 PHE PHE A . n 
A 1 106 GLU 106 133 133 GLU GLU A . n 
A 1 107 SER 107 134 134 SER SER A . n 
A 1 108 ASP 108 135 135 ASP ASP A . n 
A 1 109 ASN 109 136 136 ASN ASN A . n 
A 1 110 LEU 110 137 137 LEU LEU A . n 
A 1 111 GLY 111 138 138 GLY GLY A . n 
A 1 112 MET 112 139 139 MET MET A . n 
A 1 113 ASN 113 140 140 ASN ASN A . n 
A 1 114 ILE 114 141 141 ILE ILE A . n 
A 1 115 THR 115 142 142 THR THR A . n 
A 1 116 ARG 116 143 143 ARG ARG A . n 
A 1 117 GLN 117 144 144 GLN GLN A . n 
A 1 118 HIS 118 145 145 HIS HIS A . n 
A 1 119 LEU 119 146 146 LEU LEU A . n 
A 1 120 ASP 120 147 147 ASP ASP A . n 
A 1 121 ARG 121 148 148 ARG ARG A . n 
A 1 122 LEU 122 149 149 LEU LEU A . n 
A 1 123 HIS 123 150 150 HIS HIS A . n 
A 1 124 GLY 124 151 151 GLY GLY A . n 
A 1 125 LEU 125 152 152 LEU LEU A . n 
A 1 126 LYS 126 153 153 LYS LYS A . n 
A 1 127 ARG 127 154 154 ARG ARG A . n 
A 1 128 PHE 128 155 155 PHE PHE A . n 
A 1 129 ARG 129 156 156 ARG ARG A . n 
A 1 130 PHE 130 157 157 PHE PHE A . n 
A 1 131 THR 131 158 158 THR THR A . n 
A 1 132 THR 132 159 159 THR THR A . n 
A 1 133 ARG 133 160 160 ARG ARG A . n 
A 1 134 ARG 134 161 161 ARG ARG A . n 
A 1 135 LEU 135 162 162 LEU LEU A . n 
A 1 136 THR 136 163 163 THR THR A . n 
A 1 137 HIS 137 164 164 HIS HIS A . n 
A 1 138 ILE 138 165 165 ILE ILE A . n 
A 1 139 PRO 139 166 166 PRO PRO A . n 
A 1 140 ALA 140 167 167 ALA ALA A . n 
A 1 141 ASN 141 168 168 ASN ASN A . n 
A 1 142 LEU 142 169 169 LEU LEU A . n 
A 1 143 LEU 143 170 170 LEU LEU A . n 
A 1 144 THR 144 171 171 THR THR A . n 
A 1 145 ASP 145 172 172 ASP ASP A . n 
A 1 146 MET 146 173 173 MET MET A . n 
A 1 147 ARG 147 174 174 ARG ARG A . n 
A 1 148 ASN 148 175 175 ASN ASN A . n 
A 1 149 LEU 149 176 176 LEU LEU A . n 
A 1 150 SER 150 177 177 SER SER A . n 
A 1 151 HIS 151 178 178 HIS HIS A . n 
A 1 152 LEU 152 179 179 LEU LEU A . n 
A 1 153 GLU 153 180 180 GLU GLU A . n 
A 1 154 LEU 154 181 181 LEU LEU A . n 
A 1 155 ARG 155 182 182 ARG ARG A . n 
A 1 156 ALA 156 183 183 ALA ALA A . n 
A 1 157 ASN 157 184 184 ASN ASN A . n 
A 1 158 ILE 158 185 185 ILE ILE A . n 
A 1 159 GLU 159 186 186 GLU GLU A . n 
A 1 160 GLU 160 187 187 GLU GLU A . n 
A 1 161 MET 161 188 188 MET MET A . n 
A 1 162 PRO 162 189 189 PRO PRO A . n 
A 1 163 SER 163 190 190 SER SER A . n 
A 1 164 HIS 164 191 191 HIS HIS A . n 
A 1 165 LEU 165 192 192 LEU LEU A . n 
A 1 166 PHE 166 193 193 PHE PHE A . n 
A 1 167 ASP 167 194 194 ASP ASP A . n 
A 1 168 ASP 168 195 195 ASP ASP A . n 
A 1 169 LEU 169 196 196 LEU LEU A . n 
A 1 170 GLU 170 197 197 GLU GLU A . n 
A 1 171 ASN 171 198 198 ASN ASN A . n 
A 1 172 LEU 172 199 199 LEU LEU A . n 
A 1 173 GLU 173 200 200 GLU GLU A . n 
A 1 174 SER 174 201 201 SER SER A . n 
A 1 175 ILE 175 202 202 ILE ILE A . n 
A 1 176 GLU 176 203 203 GLU GLU A . n 
A 1 177 PHE 177 204 204 PHE PHE A . n 
A 1 178 GLY 178 205 205 GLY GLY A . n 
A 1 179 SER 179 206 206 SER SER A . n 
A 1 180 ASN 180 207 207 ASN ASN A . n 
A 1 181 LYS 181 208 208 LYS LYS A . n 
A 1 182 LEU 182 209 209 LEU LEU A . n 
A 1 183 ARG 183 210 210 ARG ARG A . n 
A 1 184 GLN 184 211 211 GLN GLN A . n 
A 1 185 MET 185 212 212 MET MET A . n 
A 1 186 PRO 186 213 213 PRO PRO A . n 
A 1 187 ARG 187 214 214 ARG ARG A . n 
A 1 188 GLY 188 215 215 GLY GLY A . n 
A 1 189 ILE 189 216 216 ILE ILE A . n 
A 1 190 PHE 190 217 217 PHE PHE A . n 
A 1 191 GLY 191 218 218 GLY GLY A . n 
A 1 192 LYS 192 219 219 LYS LYS A . n 
A 1 193 MET 193 220 220 MET MET A . n 
A 1 194 PRO 194 221 221 PRO PRO A . n 
A 1 195 LYS 195 222 222 LYS LYS A . n 
A 1 196 LEU 196 223 223 LEU LEU A . n 
A 1 197 LYS 197 224 224 LYS LYS A . n 
A 1 198 GLN 198 225 225 GLN GLN A . n 
A 1 199 LEU 199 226 226 LEU LEU A . n 
A 1 200 ASN 200 227 227 ASN ASN A . n 
A 1 201 LEU 201 228 228 LEU LEU A . n 
A 1 202 TRP 202 229 229 TRP TRP A . n 
A 1 203 SER 203 230 230 SER SER A . n 
A 1 204 ASN 204 231 231 ASN ASN A . n 
A 1 205 GLN 205 232 232 GLN GLN A . n 
A 1 206 LEU 206 233 233 LEU LEU A . n 
A 1 207 HIS 207 234 234 HIS HIS A . n 
A 1 208 ASN 208 235 235 ASN ASN A . n 
A 1 209 LEU 209 236 236 LEU LEU A . n 
A 1 210 THR 210 237 237 THR THR A . n 
A 1 211 LYS 211 238 238 LYS LYS A . n 
A 1 212 HIS 212 239 239 HIS HIS A . n 
A 1 213 ASP 213 240 240 ASP ASP A . n 
A 1 214 PHE 214 241 241 PHE PHE A . n 
A 1 215 GLU 215 242 242 GLU GLU A . n 
A 1 216 GLY 216 243 243 GLY GLY A . n 
A 1 217 ALA 217 244 244 ALA ALA A . n 
A 1 218 THR 218 245 245 THR THR A . n 
A 1 219 SER 219 246 246 SER SER A . n 
A 1 220 VAL 220 247 247 VAL VAL A . n 
A 1 221 LEU 221 248 248 LEU LEU A . n 
A 1 222 GLY 222 249 249 GLY GLY A . n 
A 1 223 ILE 223 250 250 ILE ILE A . n 
A 1 224 ASP 224 251 251 ASP ASP A . n 
A 1 225 ILE 225 252 252 ILE ILE A . n 
A 1 226 HIS 226 253 253 HIS HIS A . n 
A 1 227 ASP 227 254 254 ASP ASP A . n 
A 1 228 ASN 228 255 255 ASN ASN A . n 
A 1 229 GLY 229 256 256 GLY GLY A . n 
A 1 230 ILE 230 257 257 ILE ILE A . n 
A 1 231 GLU 231 258 258 GLU GLU A . n 
A 1 232 GLN 232 259 259 GLN GLN A . n 
A 1 233 LEU 233 260 260 LEU LEU A . n 
A 1 234 PRO 234 261 261 PRO PRO A . n 
A 1 235 HIS 235 262 262 HIS HIS A . n 
A 1 236 ASP 236 263 263 ASP ASP A . n 
A 1 237 VAL 237 264 264 VAL VAL A . n 
A 1 238 PHE 238 265 265 PHE PHE A . n 
A 1 239 ALA 239 266 266 ALA ALA A . n 
A 1 240 HIS 240 267 267 HIS HIS A . n 
A 1 241 LEU 241 268 268 LEU LEU A . n 
A 1 242 THR 242 269 269 THR THR A . n 
A 1 243 ASN 243 270 270 ASN ASN A . n 
A 1 244 VAL 244 271 271 VAL VAL A . n 
A 1 245 THR 245 272 272 THR THR A . n 
A 1 246 ASP 246 273 273 ASP ASP A . n 
A 1 247 ILE 247 274 274 ILE ILE A . n 
A 1 248 ASN 248 275 275 ASN ASN A . n 
A 1 249 LEU 249 276 276 LEU LEU A . n 
A 1 250 SER 250 277 277 SER SER A . n 
A 1 251 ALA 251 278 278 ALA ALA A . n 
A 1 252 ASN 252 279 279 ASN ASN A . n 
A 1 253 LEU 253 280 280 LEU LEU A . n 
A 1 254 PHE 254 281 281 PHE PHE A . n 
A 1 255 ARG 255 282 282 ARG ARG A . n 
A 1 256 SER 256 283 283 SER SER A . n 
A 1 257 LEU 257 284 284 LEU LEU A . n 
A 1 258 PRO 258 285 285 PRO PRO A . n 
A 1 259 GLN 259 286 286 GLN GLN A . n 
A 1 260 GLY 260 287 287 GLY GLY A . n 
A 1 261 LEU 261 288 288 LEU LEU A . n 
A 1 262 PHE 262 289 289 PHE PHE A . n 
A 1 263 ASP 263 290 290 ASP ASP A . n 
A 1 264 HIS 264 291 291 HIS HIS A . n 
A 1 265 ASN 265 292 292 ASN ASN A . n 
A 1 266 LYS 266 293 293 LYS LYS A . n 
A 1 267 HIS 267 294 294 HIS HIS A . n 
A 1 268 LEU 268 295 295 LEU LEU A . n 
A 1 269 ASN 269 296 296 ASN ASN A . n 
A 1 270 GLU 270 297 297 GLU GLU A . n 
A 1 271 VAL 271 298 298 VAL VAL A . n 
A 1 272 ARG 272 299 299 ARG ARG A . n 
A 1 273 LEU 273 300 300 LEU LEU A . n 
A 1 274 MET 274 301 301 MET MET A . n 
A 1 275 ASN 275 302 302 ASN ASN A . n 
A 1 276 ASN 276 303 303 ASN ASN A . n 
A 1 277 ARG 277 304 304 ARG ARG A . n 
A 1 278 VAL 278 305 305 VAL VAL A . n 
A 1 279 PRO 279 306 306 PRO PRO A . n 
A 1 280 LEU 280 307 307 LEU LEU A . n 
A 1 281 ALA 281 308 308 ALA ALA A . n 
A 1 282 THR 282 309 309 THR THR A . n 
A 1 283 LEU 283 310 310 LEU LEU A . n 
A 1 284 PRO 284 311 311 PRO PRO A . n 
A 1 285 SER 285 312 312 SER SER A . n 
A 1 286 ARG 286 313 313 ARG ARG A . n 
A 1 287 LEU 287 314 314 LEU LEU A . n 
A 1 288 PHE 288 315 315 PHE PHE A . n 
A 1 289 ALA 289 316 316 ALA ALA A . n 
A 1 290 ASN 290 317 317 ASN ASN A . n 
A 1 291 GLN 291 318 318 GLN GLN A . n 
A 1 292 PRO 292 319 319 PRO PRO A . n 
A 1 293 GLU 293 320 320 GLU GLU A . n 
A 1 294 LEU 294 321 321 LEU LEU A . n 
A 1 295 GLN 295 322 322 GLN GLN A . n 
A 1 296 ILE 296 323 323 ILE ILE A . n 
A 1 297 LEU 297 324 324 LEU LEU A . n 
A 1 298 ARG 298 325 325 ARG ARG A . n 
A 1 299 LEU 299 326 326 LEU LEU A . n 
A 1 300 ARG 300 327 327 ARG ARG A . n 
A 1 301 ALA 301 328 328 ALA ALA A . n 
A 1 302 GLU 302 329 329 GLU GLU A . n 
A 1 303 LEU 303 330 330 LEU LEU A . n 
A 1 304 GLN 304 331 331 GLN GLN A . n 
A 1 305 SER 305 332 332 SER SER A . n 
A 1 306 LEU 306 333 333 LEU LEU A . n 
A 1 307 PRO 307 334 334 PRO PRO A . n 
A 1 308 GLY 308 335 335 GLY GLY A . n 
A 1 309 ASP 309 336 336 ASP ASP A . n 
A 1 310 LEU 310 337 337 LEU LEU A . n 
A 1 311 PHE 311 338 338 PHE PHE A . n 
A 1 312 GLU 312 339 339 GLU GLU A . n 
A 1 313 HIS 313 340 340 HIS HIS A . n 
A 1 314 SER 314 341 341 SER SER A . n 
A 1 315 THR 315 342 342 THR THR A . n 
A 1 316 GLN 316 343 343 GLN GLN A . n 
A 1 317 ILE 317 344 344 ILE ILE A . n 
A 1 318 THR 318 345 345 THR THR A . n 
A 1 319 ASN 319 346 346 ASN ASN A . n 
A 1 320 ILE 320 347 347 ILE ILE A . n 
A 1 321 SER 321 348 348 SER SER A . n 
A 1 322 LEU 322 349 349 LEU LEU A . n 
A 1 323 GLY 323 350 350 GLY GLY A . n 
A 1 324 ASP 324 351 351 ASP ASP A . n 
A 1 325 ASN 325 352 352 ASN ASN A . n 
A 1 326 LEU 326 353 353 LEU LEU A . n 
A 1 327 LEU 327 354 354 LEU LEU A . n 
A 1 328 LYS 328 355 355 LYS LYS A . n 
A 1 329 THR 329 356 356 THR THR A . n 
A 1 330 LEU 330 357 357 LEU LEU A . n 
A 1 331 PRO 331 358 358 PRO PRO A . n 
A 1 332 ALA 332 359 359 ALA ALA A . n 
A 1 333 THR 333 360 360 THR THR A . n 
A 1 334 LEU 334 361 361 LEU LEU A . n 
A 1 335 LEU 335 362 362 LEU LEU A . n 
A 1 336 GLU 336 363 363 GLU GLU A . n 
A 1 337 HIS 337 364 364 HIS HIS A . n 
A 1 338 GLN 338 365 365 GLN GLN A . n 
A 1 339 VAL 339 366 366 VAL VAL A . n 
A 1 340 ASN 340 367 367 ASN ASN A . n 
A 1 341 LEU 341 368 368 LEU LEU A . n 
A 1 342 LEU 342 369 369 LEU LEU A . n 
A 1 343 SER 343 370 370 SER SER A . n 
A 1 344 LEU 344 371 371 LEU LEU A . n 
A 1 345 ASP 345 372 372 ASP ASP A . n 
A 1 346 LEU 346 373 373 LEU LEU A . n 
A 1 347 SER 347 374 374 SER SER A . n 
A 1 348 ASN 348 375 375 ASN ASN A . n 
A 1 349 ASN 349 376 376 ASN ASN A . n 
A 1 350 ARG 350 377 377 ARG ARG A . n 
A 1 351 LEU 351 378 378 LEU LEU A . n 
A 1 352 THR 352 379 379 THR THR A . n 
A 1 353 HIS 353 380 380 HIS HIS A . n 
A 1 354 LEU 354 381 381 LEU LEU A . n 
A 1 355 PRO 355 382 382 PRO PRO A . n 
A 1 356 ASP 356 383 383 ASP ASP A . n 
A 1 357 SER 357 384 384 SER SER A . n 
A 1 358 LEU 358 385 385 LEU LEU A . n 
A 1 359 PHE 359 386 386 PHE PHE A . n 
A 1 360 ALA 360 387 387 ALA ALA A . n 
A 1 361 HIS 361 388 388 HIS HIS A . n 
A 1 362 THR 362 389 389 THR THR A . n 
A 1 363 THR 363 390 390 THR THR A . n 
A 1 364 ASN 364 391 391 ASN ASN A . n 
A 1 365 LEU 365 392 392 LEU LEU A . n 
A 1 366 THR 366 393 393 THR THR A . n 
A 1 367 ASP 367 394 394 ASP ASP A . n 
A 1 368 LEU 368 395 395 LEU LEU A . n 
A 1 369 ARG 369 396 396 ARG ARG A . n 
A 1 370 LEU 370 397 397 LEU LEU A . n 
A 1 371 GLU 371 398 398 GLU GLU A . n 
A 1 372 ASP 372 399 399 ASP ASP A . n 
A 1 373 ASN 373 400 400 ASN ASN A . n 
A 1 374 LEU 374 401 401 LEU LEU A . n 
A 1 375 LEU 375 402 402 LEU LEU A . n 
A 1 376 THR 376 403 403 THR THR A . n 
A 1 377 GLY 377 404 404 GLY GLY A . n 
A 1 378 ILE 378 405 405 ILE ILE A . n 
A 1 379 SER 379 406 406 SER SER A . n 
A 1 380 GLY 380 407 407 GLY GLY A . n 
A 1 381 ASP 381 408 408 ASP ASP A . n 
A 1 382 ILE 382 409 409 ILE ILE A . n 
A 1 383 PHE 383 410 410 PHE PHE A . n 
A 1 384 SER 384 411 411 SER SER A . n 
A 1 385 ASN 385 412 412 ASN ASN A . n 
A 1 386 LEU 386 413 413 LEU LEU A . n 
A 1 387 GLY 387 414 414 GLY GLY A . n 
A 1 388 ASN 388 415 415 ASN ASN A . n 
A 1 389 LEU 389 416 416 LEU LEU A . n 
A 1 390 VAL 390 417 417 VAL VAL A . n 
A 1 391 THR 391 418 418 THR THR A . n 
A 1 392 LEU 392 419 419 LEU LEU A . n 
A 1 393 VAL 393 420 420 VAL VAL A . n 
A 1 394 MET 394 421 421 MET MET A . n 
A 1 395 SER 395 422 422 SER SER A . n 
A 1 396 ARG 396 423 423 ARG ARG A . n 
A 1 397 ASN 397 424 424 ASN ASN A . n 
A 1 398 ARG 398 425 425 ARG ARG A . n 
A 1 399 LEU 399 426 426 LEU LEU A . n 
A 1 400 ARG 400 427 427 ARG ARG A . n 
A 1 401 THR 401 428 428 THR THR A . n 
A 1 402 ILE 402 429 429 ILE ILE A . n 
A 1 403 ASP 403 430 430 ASP ASP A . n 
A 1 404 SER 404 431 431 SER SER A . n 
A 1 405 ARG 405 432 432 ARG ARG A . n 
A 1 406 ALA 406 433 433 ALA ALA A . n 
A 1 407 PHE 407 434 434 PHE PHE A . n 
A 1 408 VAL 408 435 435 VAL VAL A . n 
A 1 409 SER 409 436 436 SER SER A . n 
A 1 410 THR 410 437 437 THR THR A . n 
A 1 411 ASN 411 438 438 ASN ASN A . n 
A 1 412 GLY 412 439 439 GLY GLY A . n 
A 1 413 LEU 413 440 440 LEU LEU A . n 
A 1 414 ARG 414 441 441 ARG ARG A . n 
A 1 415 HIS 415 442 442 HIS HIS A . n 
A 1 416 LEU 416 443 443 LEU LEU A . n 
A 1 417 HIS 417 444 444 HIS HIS A . n 
A 1 418 LEU 418 445 445 LEU LEU A . n 
A 1 419 ASP 419 446 446 ASP ASP A . n 
A 1 420 HIS 420 447 447 HIS HIS A . n 
A 1 421 ASN 421 448 448 ASN ASN A . n 
A 1 422 ASP 422 449 449 ASP ASP A . n 
A 1 423 ILE 423 450 450 ILE ILE A . n 
A 1 424 ASP 424 451 451 ASP ASP A . n 
A 1 425 LEU 425 452 452 LEU LEU A . n 
A 1 426 GLN 426 453 453 GLN GLN A . n 
A 1 427 GLN 427 454 454 GLN GLN A . n 
A 1 428 PRO 428 455 455 PRO PRO A . n 
A 1 429 LEU 429 456 456 LEU LEU A . n 
A 1 430 LEU 430 457 457 LEU LEU A . n 
A 1 431 ASP 431 458 458 ASP ASP A . n 
A 1 432 ILE 432 459 459 ILE ILE A . n 
A 1 433 MET 433 460 460 MET MET A . n 
A 1 434 LEU 434 461 461 LEU LEU A . n 
A 1 435 GLN 435 462 462 GLN GLN A . n 
A 1 436 THR 436 463 463 THR THR A . n 
A 1 437 GLN 437 464 464 GLN GLN A . n 
A 1 438 ILE 438 465 465 ILE ILE A . n 
A 1 439 ASN 439 466 466 ASN ASN A . n 
A 1 440 SER 440 467 467 SER SER A . n 
A 1 441 PRO 441 468 468 PRO PRO A . n 
A 1 442 PHE 442 469 469 PHE PHE A . n 
A 1 443 GLY 443 470 470 GLY GLY A . n 
A 1 444 TYR 444 471 471 TYR TYR A . n 
A 1 445 MET 445 472 472 MET MET A . n 
A 1 446 HIS 446 473 473 HIS HIS A . n 
A 1 447 GLY 447 474 474 GLY GLY A . n 
A 1 448 LEU 448 475 475 LEU LEU A . n 
A 1 449 LEU 449 476 476 LEU LEU A . n 
A 1 450 THR 450 477 477 THR THR A . n 
A 1 451 LEU 451 478 478 LEU LEU A . n 
A 1 452 ASN 452 479 479 ASN ASN A . n 
A 1 453 LEU 453 480 480 LEU LEU A . n 
A 1 454 ARG 454 481 481 ARG ARG A . n 
A 1 455 ASN 455 482 482 ASN ASN A . n 
A 1 456 ASN 456 483 483 ASN ASN A . n 
A 1 457 SER 457 484 484 SER SER A . n 
A 1 458 ILE 458 485 485 ILE ILE A . n 
A 1 459 ILE 459 486 486 ILE ILE A . n 
A 1 460 PHE 460 487 487 PHE PHE A . n 
A 1 461 VAL 461 488 488 VAL VAL A . n 
A 1 462 TYR 462 489 489 TYR TYR A . n 
A 1 463 ASN 463 490 490 ASN ASN A . n 
A 1 464 ASP 464 491 491 ASP ASP A . n 
A 1 465 TRP 465 492 492 TRP TRP A . n 
A 1 466 LYS 466 493 493 LYS LYS A . n 
A 1 467 ASN 467 494 494 ASN ASN A . n 
A 1 468 THR 468 495 495 THR THR A . n 
A 1 469 MET 469 496 496 MET MET A . n 
A 1 470 LEU 470 497 497 LEU LEU A . n 
A 1 471 GLN 471 498 498 GLN GLN A . n 
A 1 472 LEU 472 499 499 LEU LEU A . n 
A 1 473 ARG 473 500 500 ARG ARG A . n 
A 1 474 GLU 474 501 501 GLU GLU A . n 
A 1 475 LEU 475 502 502 LEU LEU A . n 
A 1 476 ASP 476 503 503 ASP ASP A . n 
A 1 477 LEU 477 504 504 LEU LEU A . n 
A 1 478 SER 478 505 505 SER SER A . n 
A 1 479 TYR 479 506 506 TYR TYR A . n 
A 1 480 ASN 480 507 507 ASN ASN A . n 
A 1 481 ASN 481 508 508 ASN ASN A . n 
A 1 482 ILE 482 509 509 ILE ILE A . n 
A 1 483 SER 483 510 510 SER SER A . n 
A 1 484 SER 484 511 511 SER SER A . n 
A 1 485 LEU 485 512 512 LEU LEU A . n 
A 1 486 GLY 486 513 513 GLY GLY A . n 
A 1 487 TYR 487 514 514 TYR TYR A . n 
A 1 488 GLU 488 515 515 GLU GLU A . n 
A 1 489 ASP 489 516 516 ASP ASP A . n 
A 1 490 LEU 490 517 517 LEU LEU A . n 
A 1 491 ALA 491 518 518 ALA ALA A . n 
A 1 492 PHE 492 519 519 PHE PHE A . n 
A 1 493 LEU 493 520 520 LEU LEU A . n 
A 1 494 SER 494 521 521 SER SER A . n 
A 1 495 GLN 495 522 522 GLN GLN A . n 
A 1 496 ASN 496 523 523 ASN ASN A . n 
A 1 497 ARG 497 524 524 ARG ARG A . n 
A 1 498 LEU 498 525 525 LEU LEU A . n 
A 1 499 HIS 499 526 526 HIS HIS A . n 
A 1 500 VAL 500 527 527 VAL VAL A . n 
A 1 501 ASN 501 528 528 ASN ASN A . n 
A 1 502 MET 502 529 529 MET MET A . n 
A 1 503 THR 503 530 530 THR THR A . n 
A 1 504 HIS 504 531 531 HIS HIS A . n 
A 1 505 ASN 505 532 532 ASN ASN A . n 
A 1 506 LYS 506 533 533 LYS LYS A . n 
A 1 507 ILE 507 534 534 ILE ILE A . n 
A 1 508 ARG 508 535 535 ARG ARG A . n 
A 1 509 ARG 509 536 536 ARG ARG A . n 
A 1 510 ILE 510 537 537 ILE ILE A . n 
A 1 511 ALA 511 538 538 ALA ALA A . n 
A 1 512 LEU 512 539 539 LEU LEU A . n 
A 1 513 PRO 513 540 540 PRO PRO A . n 
A 1 514 GLU 514 541 541 GLU GLU A . n 
A 1 515 ASP 515 542 542 ASP ASP A . n 
A 1 516 VAL 516 543 543 VAL VAL A . n 
A 1 517 HIS 517 544 ?   ?   ?   A . n 
A 1 518 LEU 518 545 ?   ?   ?   A . n 
A 1 519 GLY 519 546 ?   ?   ?   A . n 
A 1 520 GLU 520 547 ?   ?   ?   A . n 
A 1 521 GLY 521 548 ?   ?   ?   A . n 
A 1 522 TYR 522 549 ?   ?   ?   A . n 
A 1 523 ASN 523 550 ?   ?   ?   A . n 
A 1 524 ASN 524 551 ?   ?   ?   A . n 
A 1 525 ASN 525 552 ?   ?   ?   A . n 
A 1 526 LEU 526 553 553 LEU LEU A . n 
A 1 527 VAL 527 554 554 VAL VAL A . n 
A 1 528 HIS 528 555 555 HIS HIS A . n 
A 1 529 VAL 529 556 556 VAL VAL A . n 
A 1 530 ASP 530 557 557 ASP ASP A . n 
A 1 531 LEU 531 558 558 LEU LEU A . n 
A 1 532 ASN 532 559 559 ASN ASN A . n 
A 1 533 ASP 533 560 560 ASP ASP A . n 
A 1 534 ASN 534 561 561 ASN ASN A . n 
A 1 535 PRO 535 562 562 PRO PRO A . n 
A 1 536 LEU 536 563 563 LEU LEU A . n 
A 1 537 VAL 537 564 564 VAL VAL A . n 
A 1 538 CYS 538 565 565 CYS CYS A . n 
A 1 539 ASP 539 566 566 ASP ASP A . n 
A 1 540 CYS 540 567 567 CYS CYS A . n 
A 1 541 THR 541 568 568 THR THR A . n 
A 1 542 ILE 542 569 569 ILE ILE A . n 
A 1 543 LEU 543 570 570 LEU LEU A . n 
A 1 544 TRP 544 571 571 TRP TRP A . n 
A 1 545 PHE 545 572 572 PHE PHE A . n 
A 1 546 ILE 546 573 573 ILE ILE A . n 
A 1 547 GLN 547 574 574 GLN GLN A . n 
A 1 548 LEU 548 575 575 LEU LEU A . n 
A 1 549 VAL 549 576 576 VAL VAL A . n 
A 1 550 ARG 550 577 577 ARG ARG A . n 
A 1 551 GLY 551 578 578 GLY GLY A . n 
A 1 552 VAL 552 579 579 VAL VAL A . n 
A 1 553 HIS 553 580 580 HIS HIS A . n 
A 1 554 LYS 554 581 581 LYS LYS A . n 
A 1 555 PRO 555 582 582 PRO PRO A . n 
A 1 556 GLN 556 583 583 GLN GLN A . n 
A 1 557 TYR 557 584 584 TYR TYR A . n 
A 1 558 SER 558 585 585 SER SER A . n 
A 1 559 ARG 559 586 586 ARG ARG A . n 
A 1 560 GLN 560 587 587 GLN GLN A . n 
A 1 561 PHE 561 588 588 PHE PHE A . n 
A 1 562 LYS 562 589 589 LYS LYS A . n 
A 1 563 LEU 563 590 590 LEU LEU A . n 
A 1 564 ARG 564 591 591 ARG ARG A . n 
A 1 565 THR 565 592 592 THR THR A . n 
A 1 566 ASP 566 593 593 ASP ASP A . n 
A 1 567 ARG 567 594 594 ARG ARG A . n 
A 1 568 LEU 568 595 595 LEU LEU A . n 
A 1 569 VAL 569 596 596 VAL VAL A . n 
A 1 570 CYS 570 597 597 CYS CYS A . n 
A 1 571 SER 571 598 598 SER SER A . n 
A 1 572 GLN 572 599 599 GLN GLN A . n 
A 1 573 PRO 573 600 600 PRO PRO A . n 
A 1 574 ASN 574 601 601 ASN ASN A . n 
A 1 575 VAL 575 602 602 VAL VAL A . n 
A 1 576 LEU 576 603 603 LEU LEU A . n 
A 1 577 GLU 577 604 604 GLU GLU A . n 
A 1 578 GLY 578 605 605 GLY GLY A . n 
A 1 579 THR 579 606 606 THR THR A . n 
A 1 580 PRO 580 607 607 PRO PRO A . n 
A 1 581 VAL 581 608 608 VAL VAL A . n 
A 1 582 ARG 582 609 609 ARG ARG A . n 
A 1 583 GLN 583 610 610 GLN GLN A . n 
A 1 584 ILE 584 611 611 ILE ILE A . n 
A 1 585 GLU 585 612 612 GLU GLU A . n 
A 1 586 PRO 586 613 613 PRO PRO A . n 
A 1 587 GLN 587 614 614 GLN GLN A . n 
A 1 588 THR 588 615 615 THR THR A . n 
A 1 589 LEU 589 616 616 LEU LEU A . n 
A 1 590 ILE 590 617 617 ILE ILE A . n 
A 1 591 CYS 591 618 618 CYS CYS A . n 
A 1 592 PRO 592 619 619 PRO PRO A . n 
A 1 593 LEU 593 620 620 LEU LEU A . n 
A 1 594 ASP 594 621 621 ASP ASP A . n 
A 1 595 PHE 595 622 ?   ?   ?   A . n 
A 1 596 SER 596 623 ?   ?   ?   A . n 
A 1 597 ASP 597 624 ?   ?   ?   A . n 
A 1 598 ASP 598 625 ?   ?   ?   A . n 
A 1 599 PRO 599 626 ?   ?   ?   A . n 
A 1 600 ARG 600 627 ?   ?   ?   A . n 
A 1 601 GLU 601 628 ?   ?   ?   A . n 
A 1 602 ARG 602 629 ?   ?   ?   A . n 
A 1 603 LYS 603 630 630 LYS LYS A . n 
A 1 604 CYS 604 631 631 CYS CYS A . n 
A 1 605 PRO 605 632 632 PRO PRO A . n 
A 1 606 ARG 606 633 633 ARG ARG A . n 
A 1 607 GLY 607 634 634 GLY GLY A . n 
A 1 608 CYS 608 635 635 CYS CYS A . n 
A 1 609 ASN 609 636 636 ASN ASN A . n 
A 1 610 CYS 610 637 637 CYS CYS A . n 
A 1 611 HIS 611 638 638 HIS HIS A . n 
A 1 612 VAL 612 639 639 VAL VAL A . n 
A 1 613 ARG 613 640 640 ARG ARG A . n 
A 1 614 THR 614 641 641 THR THR A . n 
A 1 615 TYR 615 642 642 TYR TYR A . n 
A 1 616 ASP 616 643 643 ASP ASP A . n 
A 1 617 LYS 617 644 644 LYS LYS A . n 
A 1 618 ALA 618 645 645 ALA ALA A . n 
A 1 619 LEU 619 646 646 LEU LEU A . n 
A 1 620 VAL 620 647 647 VAL VAL A . n 
A 1 621 ILE 621 648 648 ILE ILE A . n 
A 1 622 ASN 622 649 649 ASN ASN A . n 
A 1 623 CYS 623 650 650 CYS CYS A . n 
A 1 624 HIS 624 651 651 HIS HIS A . n 
A 1 625 SER 625 652 652 SER SER A . n 
A 1 626 GLY 626 653 653 GLY GLY A . n 
A 1 627 ASN 627 654 654 ASN ASN A . n 
A 1 628 LEU 628 655 655 LEU LEU A . n 
A 1 629 THR 629 656 656 THR THR A . n 
A 1 630 HIS 630 657 657 HIS HIS A . n 
A 1 631 VAL 631 658 658 VAL VAL A . n 
A 1 632 PRO 632 659 659 PRO PRO A . n 
A 1 633 ARG 633 660 660 ARG ARG A . n 
A 1 634 LEU 634 661 661 LEU LEU A . n 
A 1 635 PRO 635 662 662 PRO PRO A . n 
A 1 636 ASN 636 663 663 ASN ASN A . n 
A 1 637 LEU 637 664 664 LEU LEU A . n 
A 1 638 HIS 638 665 665 HIS HIS A . n 
A 1 639 LYS 639 666 666 LYS LYS A . n 
A 1 640 ASN 640 667 667 ASN ASN A . n 
A 1 641 MET 641 668 668 MET MET A . n 
A 1 642 GLN 642 669 669 GLN GLN A . n 
A 1 643 LEU 643 670 670 LEU LEU A . n 
A 1 644 MET 644 671 671 MET MET A . n 
A 1 645 GLU 645 672 672 GLU GLU A . n 
A 1 646 LEU 646 673 673 LEU LEU A . n 
A 1 647 HIS 647 674 674 HIS HIS A . n 
A 1 648 LEU 648 675 675 LEU LEU A . n 
A 1 649 GLU 649 676 676 GLU GLU A . n 
A 1 650 ASN 650 677 677 ASN ASN A . n 
A 1 651 ASN 651 678 678 ASN ASN A . n 
A 1 652 THR 652 679 679 THR THR A . n 
A 1 653 LEU 653 680 680 LEU LEU A . n 
A 1 654 LEU 654 681 681 LEU LEU A . n 
A 1 655 ARG 655 682 682 ARG ARG A . n 
A 1 656 LEU 656 683 683 LEU LEU A . n 
A 1 657 PRO 657 684 684 PRO PRO A . n 
A 1 658 SER 658 685 685 SER SER A . n 
A 1 659 ALA 659 686 686 ALA ALA A . n 
A 1 660 ASN 660 687 687 ASN ASN A . n 
A 1 661 THR 661 688 688 THR THR A . n 
A 1 662 PRO 662 689 689 PRO PRO A . n 
A 1 663 GLY 663 690 690 GLY GLY A . n 
A 1 664 TYR 664 691 691 TYR TYR A . n 
A 1 665 GLU 665 692 692 GLU GLU A . n 
A 1 666 SER 666 693 693 SER SER A . n 
A 1 667 VAL 667 694 694 VAL VAL A . n 
A 1 668 THR 668 695 695 THR THR A . n 
A 1 669 SER 669 696 696 SER SER A . n 
A 1 670 LEU 670 697 697 LEU LEU A . n 
A 1 671 HIS 671 698 698 HIS HIS A . n 
A 1 672 LEU 672 699 699 LEU LEU A . n 
A 1 673 ALA 673 700 700 ALA ALA A . n 
A 1 674 GLY 674 701 701 GLY GLY A . n 
A 1 675 ASN 675 702 702 ASN ASN A . n 
A 1 676 ASN 676 703 703 ASN ASN A . n 
A 1 677 LEU 677 704 704 LEU LEU A . n 
A 1 678 THR 678 705 705 THR THR A . n 
A 1 679 SER 679 706 706 SER SER A . n 
A 1 680 ILE 680 707 707 ILE ILE A . n 
A 1 681 ASP 681 708 708 ASP ASP A . n 
A 1 682 VAL 682 709 709 VAL VAL A . n 
A 1 683 ASP 683 710 710 ASP ASP A . n 
A 1 684 GLN 684 711 711 GLN GLN A . n 
A 1 685 LEU 685 712 712 LEU LEU A . n 
A 1 686 PRO 686 713 713 PRO PRO A . n 
A 1 687 THR 687 714 714 THR THR A . n 
A 1 688 ASN 688 715 715 ASN ASN A . n 
A 1 689 LEU 689 716 716 LEU LEU A . n 
A 1 690 THR 690 717 717 THR THR A . n 
A 1 691 HIS 691 718 718 HIS HIS A . n 
A 1 692 LEU 692 719 719 LEU LEU A . n 
A 1 693 ASP 693 720 720 ASP ASP A . n 
A 1 694 ILE 694 721 721 ILE ILE A . n 
A 1 695 SER 695 722 722 SER SER A . n 
A 1 696 TRP 696 723 723 TRP TRP A . n 
A 1 697 ASN 697 724 724 ASN ASN A . n 
A 1 698 HIS 698 725 725 HIS HIS A . n 
A 1 699 LEU 699 726 726 LEU LEU A . n 
A 1 700 GLN 700 727 727 GLN GLN A . n 
A 1 701 MET 701 728 728 MET MET A . n 
A 1 702 LEU 702 729 729 LEU LEU A . n 
A 1 703 ASN 703 730 730 ASN ASN A . n 
A 1 704 ALA 704 731 731 ALA ALA A . n 
A 1 705 THR 705 732 732 THR THR A . n 
A 1 706 VAL 706 733 733 VAL VAL A . n 
A 1 707 LEU 707 734 734 LEU LEU A . n 
A 1 708 GLY 708 735 735 GLY GLY A . n 
A 1 709 PHE 709 736 736 PHE PHE A . n 
A 1 710 LEU 710 737 737 LEU LEU A . n 
A 1 711 ASN 711 738 738 ASN ASN A . n 
A 1 712 ARG 712 739 ?   ?   ?   A . n 
A 1 713 THR 713 740 ?   ?   ?   A . n 
A 1 714 MET 714 741 ?   ?   ?   A . n 
A 1 715 LYS 715 742 ?   ?   ?   A . n 
A 1 716 TRP 716 743 743 TRP TRP A . n 
A 1 717 ARG 717 744 744 ARG ARG A . n 
A 1 718 SER 718 745 745 SER SER A . n 
A 1 719 VAL 719 746 746 VAL VAL A . n 
A 1 720 LYS 720 747 747 LYS LYS A . n 
A 1 721 LEU 721 748 748 LEU LEU A . n 
A 1 722 SER 722 749 749 SER SER A . n 
A 1 723 GLY 723 750 750 GLY GLY A . n 
A 1 724 ASN 724 751 751 ASN ASN A . n 
A 1 725 PRO 725 752 752 PRO PRO A . n 
A 1 726 TRP 726 753 753 TRP TRP A . n 
A 1 727 MET 727 754 754 MET MET A . n 
A 1 728 CYS 728 755 755 CYS CYS A . n 
A 1 729 ASP 729 756 756 ASP ASP A . n 
A 1 730 CYS 730 757 757 CYS CYS A . n 
A 1 731 THR 731 758 758 THR THR A . n 
A 1 732 ALA 732 759 759 ALA ALA A . n 
A 1 733 LYS 733 760 760 LYS LYS A . n 
A 1 734 PRO 734 761 761 PRO PRO A . n 
A 1 735 LEU 735 762 762 LEU LEU A . n 
A 1 736 LEU 736 763 763 LEU LEU A . n 
A 1 737 LEU 737 764 764 LEU LEU A . n 
A 1 738 PHE 738 765 765 PHE PHE A . n 
A 1 739 THR 739 766 766 THR THR A . n 
A 1 740 GLN 740 767 767 GLN GLN A . n 
A 1 741 ASP 741 768 768 ASP ASP A . n 
A 1 742 ASN 742 769 769 ASN ASN A . n 
A 1 743 PHE 743 770 770 PHE PHE A . n 
A 1 744 GLU 744 771 771 GLU GLU A . n 
A 1 745 ARG 745 772 772 ARG ARG A . n 
A 1 746 ILE 746 773 773 ILE ILE A . n 
A 1 747 GLY 747 774 774 GLY GLY A . n 
A 1 748 ASP 748 775 775 ASP ASP A . n 
A 1 749 ARG 749 776 776 ARG ARG A . n 
A 1 750 ASN 750 777 777 ASN ASN A . n 
A 1 751 GLU 751 778 778 GLU GLU A . n 
A 1 752 MET 752 779 779 MET MET A . n 
A 1 753 MET 753 780 780 MET MET A . n 
A 1 754 CYS 754 781 781 CYS CYS A . n 
A 1 755 VAL 755 782 782 VAL VAL A . n 
A 1 756 ASN 756 783 783 ASN ASN A . n 
A 1 757 ALA 757 784 784 ALA ALA A . n 
A 1 758 GLU 758 785 ?   ?   ?   A . n 
A 1 759 MET 759 786 ?   ?   ?   A . n 
A 1 760 PRO 760 787 787 PRO PRO A . n 
A 1 761 THR 761 788 788 THR THR A . n 
A 1 762 ARG 762 789 789 ARG ARG A . n 
A 1 763 MET 763 790 790 MET MET A . n 
A 1 764 VAL 764 791 791 VAL VAL A . n 
A 1 765 GLU 765 792 792 GLU GLU A . n 
A 1 766 LEU 766 793 793 LEU LEU A . n 
A 1 767 SER 767 794 794 SER SER A . n 
A 1 768 THR 768 795 795 THR THR A . n 
A 1 769 ASN 769 796 796 ASN ASN A . n 
A 1 770 ASP 770 797 797 ASP ASP A . n 
A 1 771 ILE 771 798 798 ILE ILE A . n 
A 1 772 CYS 772 799 799 CYS CYS A . n 
A 1 773 PRO 773 800 800 PRO PRO A . n 
A 1 774 ALA 774 801 ?   ?   ?   A . n 
A 1 775 GLU 775 802 ?   ?   ?   A . n 
A 1 776 THR 776 803 ?   ?   ?   A . n 
A 1 777 GLY 777 804 ?   ?   ?   A . n 
A 1 778 HIS 778 805 ?   ?   ?   A . n 
A 1 779 HIS 779 806 ?   ?   ?   A . n 
A 1 780 HIS 780 807 ?   ?   ?   A . n 
A 1 781 HIS 781 808 ?   ?   ?   A . n 
A 1 782 HIS 782 809 ?   ?   ?   A . n 
A 1 783 HIS 783 810 ?   ?   ?   A . n 
B 2 1   VAL 1   1   ?   ?   ?   J . n 
B 2 2   GLY 2   2   ?   ?   ?   J . n 
B 2 3   GLY 3   3   ?   ?   ?   J . n 
B 2 4   SER 4   4   ?   ?   ?   J . n 
B 2 5   ASP 5   5   5   ASP ASP J . n 
B 2 6   GLU 6   6   6   GLU GLU J . n 
B 2 7   ARG 7   7   7   ARG ARG J . n 
B 2 8   PHE 8   8   8   PHE PHE J . n 
B 2 9   LEU 9   9   9   LEU LEU J . n 
B 2 10  CYS 10  10  10  CYS CYS J . n 
B 2 11  ARG 11  11  11  ARG ARG J . n 
B 2 12  SER 12  12  12  SER SER J . n 
B 2 13  ILE 13  13  13  ILE ILE J . n 
B 2 14  ARG 14  14  14  ARG ARG J . n 
B 2 15  LYS 15  15  15  LYS LYS J . n 
B 2 16  LEU 16  16  16  LEU LEU J . n 
B 2 17  VAL 17  17  17  VAL VAL J . n 
B 2 18  TYR 18  18  18  TYR TYR J . n 
B 2 19  PRO 19  19  ?   ?   ?   J . n 
B 2 20  LYS 20  20  ?   ?   ?   J . n 
B 2 21  LYS 21  21  ?   ?   ?   J . n 
B 2 22  GLY 22  22  ?   ?   ?   J . n 
B 2 23  LEU 23  23  ?   ?   ?   J . n 
B 2 24  ARG 24  24  ?   ?   ?   J . n 
B 2 25  ALA 25  25  ?   ?   ?   J . n 
B 2 26  ASP 26  26  ?   ?   ?   J . n 
B 2 27  ASP 27  27  ?   ?   ?   J . n 
B 2 28  THR 28  28  ?   ?   ?   J . n 
B 2 29  TRP 29  29  ?   ?   ?   J . n 
B 2 30  GLN 30  30  ?   ?   ?   J . n 
B 2 31  LEU 31  31  ?   ?   ?   J . n 
B 2 32  ILE 32  32  ?   ?   ?   J . n 
B 2 33  VAL 33  33  ?   ?   ?   J . n 
B 2 34  ASN 34  34  ?   ?   ?   J . n 
B 2 35  ASN 35  35  ?   ?   ?   J . n 
B 2 36  ASP 36  36  ?   ?   ?   J . n 
B 2 37  GLU 37  37  ?   ?   ?   J . n 
B 2 38  TYR 38  38  ?   ?   ?   J . n 
B 2 39  LYS 39  39  ?   ?   ?   J . n 
B 2 40  GLN 40  40  ?   ?   ?   J . n 
B 2 41  ALA 41  41  ?   ?   ?   J . n 
B 2 42  ILE 42  42  42  ILE ILE J . n 
B 2 43  GLN 43  43  43  GLN GLN J . n 
B 2 44  ILE 44  44  44  ILE ILE J . n 
B 2 45  GLU 45  45  45  GLU GLU J . n 
B 2 46  GLU 46  46  46  GLU GLU J . n 
B 2 47  CYS 47  47  47  CYS CYS J . n 
B 2 48  GLU 48  48  48  GLU GLU J . n 
B 2 49  GLY 49  49  49  GLY GLY J . n 
B 2 50  ALA 50  50  50  ALA ALA J . n 
B 2 51  ASP 51  51  51  ASP ASP J . n 
B 2 52  GLN 52  52  52  GLN GLN J . n 
B 2 53  PRO 53  53  53  PRO PRO J . n 
B 2 54  CYS 54  54  54  CYS CYS J . n 
B 2 55  ASP 55  55  55  ASP ASP J . n 
B 2 56  PHE 56  56  56  PHE PHE J . n 
B 2 57  ALA 57  57  57  ALA ALA J . n 
B 2 58  ALA 58  58  58  ALA ALA J . n 
B 2 59  ASN 59  59  59  ASN ASN J . n 
B 2 60  PHE 60  60  60  PHE PHE J . n 
B 2 61  PRO 61  61  61  PRO PRO J . n 
B 2 62  GLN 62  62  62  GLN GLN J . n 
B 2 63  SER 63  63  63  SER SER J . n 
B 2 64  TYR 64  64  64  TYR TYR J . n 
B 2 65  ASN 65  65  65  ASN ASN J . n 
B 2 66  PRO 66  66  66  PRO PRO J . n 
B 2 67  ILE 67  67  67  ILE ILE J . n 
B 2 68  CYS 68  68  68  CYS CYS J . n 
B 2 69  LYS 69  69  69  LYS LYS J . n 
B 2 70  GLN 70  70  70  GLN GLN J . n 
B 2 71  HIS 71  71  71  HIS HIS J . n 
B 2 72  TYR 72  72  72  TYR TYR J . n 
B 2 73  THR 73  73  73  THR THR J . n 
B 2 74  GLN 74  74  74  GLN GLN J . n 
B 2 75  GLN 75  75  ?   ?   ?   J . n 
B 2 76  THR 76  76  ?   ?   ?   J . n 
B 2 77  LEU 77  77  ?   ?   ?   J . n 
B 2 78  ALA 78  78  ?   ?   ?   J . n 
B 2 79  SER 79  79  ?   ?   ?   J . n 
B 2 80  ILE 80  80  ?   ?   ?   J . n 
B 2 81  LYS 81  81  ?   ?   ?   J . n 
B 2 82  SER 82  82  ?   ?   ?   J . n 
B 2 83  ASP 83  83  ?   ?   ?   J . n 
B 2 84  GLY 84  84  ?   ?   ?   J . n 
B 2 85  GLU 85  85  ?   ?   ?   J . n 
B 2 86  LEU 86  86  ?   ?   ?   J . n 
B 2 87  ASP 87  87  ?   ?   ?   J . n 
B 2 88  VAL 88  88  ?   ?   ?   J . n 
B 2 89  VAL 89  89  ?   ?   ?   J . n 
B 2 90  GLN 90  90  ?   ?   ?   J . n 
B 2 91  ASN 91  91  ?   ?   ?   J . n 
B 2 92  SER 92  92  ?   ?   ?   J . n 
B 2 93  PHE 93  93  ?   ?   ?   J . n 
B 2 94  LYS 94  94  94  LYS LYS J . n 
B 2 95  ILE 95  95  95  ILE ILE J . n 
B 2 96  PRO 96  96  96  PRO PRO J . n 
B 2 97  SER 97  97  97  SER SER J . n 
B 2 98  CYS 98  98  98  CYS CYS J . n 
B 2 99  CYS 99  99  99  CYS CYS J . n 
B 2 100 LYS 100 100 100 LYS LYS J . n 
B 2 101 CYS 101 101 101 CYS CYS J . n 
B 2 102 ALA 102 102 102 ALA ALA J . n 
B 2 103 LEU 103 103 103 LEU LEU J . n 
B 2 104 LYS 104 104 104 LYS LYS J . n 
B 2 105 THR 105 105 105 THR THR J . n 
B 2 106 GLY 106 106 106 GLY GLY J . n 
B 2 107 LEU 107 107 107 LEU LEU J . n 
B 2 108 GLU 108 108 108 GLU GLU J . n 
B 2 109 HIS 109 109 109 HIS HIS J . n 
B 2 110 HIS 110 110 ?   ?   ?   J . n 
B 2 111 HIS 111 111 ?   ?   ?   J . n 
B 2 112 HIS 112 112 ?   ?   ?   J . n 
B 2 113 HIS 113 113 ?   ?   ?   J . n 
B 2 114 HIS 114 114 ?   ?   ?   J . n 
C 2 1   VAL 1   1   1   VAL VAL K . n 
C 2 2   GLY 2   2   2   GLY GLY K . n 
C 2 3   GLY 3   3   3   GLY GLY K . n 
C 2 4   SER 4   4   4   SER SER K . n 
C 2 5   ASP 5   5   5   ASP ASP K . n 
C 2 6   GLU 6   6   6   GLU GLU K . n 
C 2 7   ARG 7   7   7   ARG ARG K . n 
C 2 8   PHE 8   8   8   PHE PHE K . n 
C 2 9   LEU 9   9   9   LEU LEU K . n 
C 2 10  CYS 10  10  10  CYS CYS K . n 
C 2 11  ARG 11  11  11  ARG ARG K . n 
C 2 12  SER 12  12  12  SER SER K . n 
C 2 13  ILE 13  13  13  ILE ILE K . n 
C 2 14  ARG 14  14  14  ARG ARG K . n 
C 2 15  LYS 15  15  15  LYS LYS K . n 
C 2 16  LEU 16  16  16  LEU LEU K . n 
C 2 17  VAL 17  17  ?   ?   ?   K . n 
C 2 18  TYR 18  18  ?   ?   ?   K . n 
C 2 19  PRO 19  19  ?   ?   ?   K . n 
C 2 20  LYS 20  20  ?   ?   ?   K . n 
C 2 21  LYS 21  21  ?   ?   ?   K . n 
C 2 22  GLY 22  22  ?   ?   ?   K . n 
C 2 23  LEU 23  23  ?   ?   ?   K . n 
C 2 24  ARG 24  24  ?   ?   ?   K . n 
C 2 25  ALA 25  25  ?   ?   ?   K . n 
C 2 26  ASP 26  26  ?   ?   ?   K . n 
C 2 27  ASP 27  27  ?   ?   ?   K . n 
C 2 28  THR 28  28  ?   ?   ?   K . n 
C 2 29  TRP 29  29  ?   ?   ?   K . n 
C 2 30  GLN 30  30  ?   ?   ?   K . n 
C 2 31  LEU 31  31  ?   ?   ?   K . n 
C 2 32  ILE 32  32  ?   ?   ?   K . n 
C 2 33  VAL 33  33  ?   ?   ?   K . n 
C 2 34  ASN 34  34  ?   ?   ?   K . n 
C 2 35  ASN 35  35  ?   ?   ?   K . n 
C 2 36  ASP 36  36  ?   ?   ?   K . n 
C 2 37  GLU 37  37  ?   ?   ?   K . n 
C 2 38  TYR 38  38  ?   ?   ?   K . n 
C 2 39  LYS 39  39  39  LYS LYS K . n 
C 2 40  GLN 40  40  40  GLN GLN K . n 
C 2 41  ALA 41  41  41  ALA ALA K . n 
C 2 42  ILE 42  42  42  ILE ILE K . n 
C 2 43  GLN 43  43  43  GLN GLN K . n 
C 2 44  ILE 44  44  44  ILE ILE K . n 
C 2 45  GLU 45  45  45  GLU GLU K . n 
C 2 46  GLU 46  46  46  GLU GLU K . n 
C 2 47  CYS 47  47  47  CYS CYS K . n 
C 2 48  GLU 48  48  48  GLU GLU K . n 
C 2 49  GLY 49  49  49  GLY GLY K . n 
C 2 50  ALA 50  50  50  ALA ALA K . n 
C 2 51  ASP 51  51  51  ASP ASP K . n 
C 2 52  GLN 52  52  52  GLN GLN K . n 
C 2 53  PRO 53  53  53  PRO PRO K . n 
C 2 54  CYS 54  54  54  CYS CYS K . n 
C 2 55  ASP 55  55  55  ASP ASP K . n 
C 2 56  PHE 56  56  56  PHE PHE K . n 
C 2 57  ALA 57  57  57  ALA ALA K . n 
C 2 58  ALA 58  58  58  ALA ALA K . n 
C 2 59  ASN 59  59  59  ASN ASN K . n 
C 2 60  PHE 60  60  60  PHE PHE K . n 
C 2 61  PRO 61  61  61  PRO PRO K . n 
C 2 62  GLN 62  62  62  GLN GLN K . n 
C 2 63  SER 63  63  63  SER SER K . n 
C 2 64  TYR 64  64  64  TYR TYR K . n 
C 2 65  ASN 65  65  65  ASN ASN K . n 
C 2 66  PRO 66  66  66  PRO PRO K . n 
C 2 67  ILE 67  67  67  ILE ILE K . n 
C 2 68  CYS 68  68  68  CYS CYS K . n 
C 2 69  LYS 69  69  69  LYS LYS K . n 
C 2 70  GLN 70  70  70  GLN GLN K . n 
C 2 71  HIS 71  71  71  HIS HIS K . n 
C 2 72  TYR 72  72  72  TYR TYR K . n 
C 2 73  THR 73  73  73  THR THR K . n 
C 2 74  GLN 74  74  ?   ?   ?   K . n 
C 2 75  GLN 75  75  ?   ?   ?   K . n 
C 2 76  THR 76  76  ?   ?   ?   K . n 
C 2 77  LEU 77  77  ?   ?   ?   K . n 
C 2 78  ALA 78  78  ?   ?   ?   K . n 
C 2 79  SER 79  79  ?   ?   ?   K . n 
C 2 80  ILE 80  80  ?   ?   ?   K . n 
C 2 81  LYS 81  81  ?   ?   ?   K . n 
C 2 82  SER 82  82  ?   ?   ?   K . n 
C 2 83  ASP 83  83  ?   ?   ?   K . n 
C 2 84  GLY 84  84  ?   ?   ?   K . n 
C 2 85  GLU 85  85  ?   ?   ?   K . n 
C 2 86  LEU 86  86  ?   ?   ?   K . n 
C 2 87  ASP 87  87  ?   ?   ?   K . n 
C 2 88  VAL 88  88  ?   ?   ?   K . n 
C 2 89  VAL 89  89  ?   ?   ?   K . n 
C 2 90  GLN 90  90  ?   ?   ?   K . n 
C 2 91  ASN 91  91  ?   ?   ?   K . n 
C 2 92  SER 92  92  ?   ?   ?   K . n 
C 2 93  PHE 93  93  ?   ?   ?   K . n 
C 2 94  LYS 94  94  94  LYS LYS K . n 
C 2 95  ILE 95  95  95  ILE ILE K . n 
C 2 96  PRO 96  96  96  PRO PRO K . n 
C 2 97  SER 97  97  97  SER SER K . n 
C 2 98  CYS 98  98  98  CYS CYS K . n 
C 2 99  CYS 99  99  99  CYS CYS K . n 
C 2 100 LYS 100 100 100 LYS LYS K . n 
C 2 101 CYS 101 101 101 CYS CYS K . n 
C 2 102 ALA 102 102 102 ALA ALA K . n 
C 2 103 LEU 103 103 103 LEU LEU K . n 
C 2 104 LYS 104 104 104 LYS LYS K . n 
C 2 105 THR 105 105 105 THR THR K . n 
C 2 106 GLY 106 106 106 GLY GLY K . n 
C 2 107 LEU 107 107 107 LEU LEU K . n 
C 2 108 GLU 108 108 ?   ?   ?   K . n 
C 2 109 HIS 109 109 ?   ?   ?   K . n 
C 2 110 HIS 110 110 ?   ?   ?   K . n 
C 2 111 HIS 111 111 ?   ?   ?   K . n 
C 2 112 HIS 112 112 ?   ?   ?   K . n 
C 2 113 HIS 113 113 ?   ?   ?   K . n 
C 2 114 HIS 114 114 ?   ?   ?   K . 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 
D  3 NAG 1 2001 2001 NAG NAG A . 
E  3 NAG 2 2002 2002 NAG NAG A . 
F  4 BMA 3 2003 2003 BMA BMA A . 
G  4 BMA 4 2004 2004 BMA BMA A . 
H  5 MAN 5 2005 2005 MAN MAN A . 
I  3 NAG 1 2006 2501 NAG NAG A . 
J  3 NAG 1 2007 3001 NAG NAG A . 
K  3 NAG 1 2008 3501 NAG NAG A . 
L  3 NAG 2 2009 3502 NAG NAG A . 
M  3 NAG 1 2010 4001 NAG NAG A . 
N  3 NAG 2 2011 4002 NAG NAG A . 
O  4 BMA 3 2012 4003 BMA BMA A . 
P  3 NAG 1 2013 4501 NAG NAG A . 
Q  3 NAG 2 2014 4502 NAG NAG A . 
R  3 NAG 1 2015 5001 NAG NAG A . 
S  3 NAG 2 2016 5002 NAG NAG A . 
T  3 NAG 1 2017 6001 NAG NAG A . 
U  3 NAG 2 2018 6002 NAG NAG A . 
V  3 NAG 1 2019 6501 NAG NAG A . 
W  3 NAG 2 2020 6502 NAG NAG A . 
X  3 NAG 1 2021 7001 NAG NAG A . 
Y  3 NAG 1 2022 7501 NAG NAG A . 
Z  3 NAG 1 2023 8001 NAG NAG A . 
AA 6 EPE 1 2024 1    EPE EPE A . 
# 
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 364 A ASN 391 ? ASN 'GLYCOSYLATION SITE' 
2  A ASN 676 A ASN 703 ? ASN 'GLYCOSYLATION SITE' 
3  A ASN 53  A ASN 80  ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 148 A ASN 175 ? ASN 'GLYCOSYLATION SITE' 
5  A ASN 501 A ASN 528 ? ASN 'GLYCOSYLATION SITE' 
6  A ASN 243 A ASN 270 ? ASN 'GLYCOSYLATION SITE' 
7  A ASN 208 A ASN 235 ? ASN 'GLYCOSYLATION SITE' 
8  A ASN 113 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 
9  A ASN 319 A ASN 346 ? ASN 'GLYCOSYLATION SITE' 
10 A ASN 455 A ASN 482 ? ASN 'GLYCOSYLATION SITE' 
11 A ASN 627 A ASN 654 ? ASN 'GLYCOSYLATION SITE' 
12 A ASN 481 A ASN 508 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA 
# 
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)' 12390 ? 
1 MORE         61    ? 
1 'SSA (A^2)'  41520 ? 
# 
_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_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 2014-04-09 
2 'Structure model' 1 1 2014-05-21 
3 'Structure model' 1 2 2017-11-15 
# 
_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' 'Database references'    
2 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 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    3 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_software.name' 
# 
_diffrn_reflns.diffrn_id                   1 
_diffrn_reflns.pdbx_d_res_high             3.910 
_diffrn_reflns.pdbx_d_res_low              ? 
_diffrn_reflns.pdbx_number_obs             22848 
_diffrn_reflns.pdbx_Rmerge_I_obs           0.150 
_diffrn_reflns.pdbx_Rsym_value             ? 
_diffrn_reflns.pdbx_chi_squared            ? 
_diffrn_reflns.av_sigmaI_over_netI         ? 
_diffrn_reflns.pdbx_redundancy             ? 
_diffrn_reflns.pdbx_percent_possible_obs   93.80 
_diffrn_reflns.number                      43793 
_diffrn_reflns.pdbx_observed_criterion     ? 
_diffrn_reflns.limit_h_max                 ? 
_diffrn_reflns.limit_h_min                 ? 
_diffrn_reflns.limit_k_max                 ? 
_diffrn_reflns.limit_k_min                 ? 
_diffrn_reflns.limit_l_max                 ? 
_diffrn_reflns.limit_l_min                 ? 
# 
loop_
_pdbx_phasing_MAD_set.id 
_pdbx_phasing_MAD_set.d_res_low 
_pdbx_phasing_MAD_set.d_res_high 
_pdbx_phasing_MAD_set.reflns_acentric 
_pdbx_phasing_MAD_set.reflns_centric 
_pdbx_phasing_MAD_set.power_acentric 
_pdbx_phasing_MAD_set.power_centric 
ISO_1 46.15 3.04 11103 774 0.000 0.000 
ISO_2 46.15 3.04 11082 750 0.667 0.680 
ISO_3 46.15 3.04 11065 748 1.245 1.236 
ISO_4 46.15 3.04 11047 744 1.582 1.486 
ANO_1 46.15 3.04 10474 0   1.046 0.000 
ANO_2 46.15 3.04 15147 0   0.926 0.000 
ANO_3 46.15 3.04 19988 0   0.687 0.000 
ANO_4 46.15 3.04 23777 0   0.345 0.000 
# 
loop_
_pdbx_phasing_MAD_set_shell.id 
_pdbx_phasing_MAD_set_shell.d_res_low 
_pdbx_phasing_MAD_set_shell.d_res_high 
_pdbx_phasing_MAD_set_shell.reflns_acentric 
_pdbx_phasing_MAD_set_shell.reflns_centric 
_pdbx_phasing_MAD_set_shell.power_acentric 
_pdbx_phasing_MAD_set_shell.power_centric 
ISO_1 46.15 13.07 219  41 0.000 0.000 
ISO_1 13.07 9.43  490  61 0.000 0.000 
ISO_1 9.43  7.75  641  65 0.000 0.000 
ISO_1 7.75  6.74  757  65 0.000 0.000 
ISO_1 6.74  6.04  876  67 0.000 0.000 
ISO_1 6.04  5.52  974  66 0.000 0.000 
ISO_1 5.52  5.12  1063 67 0.000 0.000 
ISO_1 5.12  4.79  1103 73 0.000 0.000 
ISO_1 4.79  4.52  1194 70 0.000 0.000 
ISO_1 4.52  4.29  1246 73 0.000 0.000 
ISO_1 4.29  4.09  1332 69 0.000 0.000 
ISO_1 4.09  3.92  1206 57 0.000 0.000 
ISO_1 3.92  3.77  2    0  0.000 0.000 
ISO_1 3.77  3.63  0    0  0.000 0.000 
ISO_1 3.63  3.51  0    0  0.000 0.000 
ISO_1 3.51  3.40  0    0  0.000 0.000 
ISO_1 3.40  3.30  0    0  0.000 0.000 
ISO_1 3.30  3.20  0    0  0.000 0.000 
ISO_1 3.20  3.12  0    0  0.000 0.000 
ISO_1 3.12  3.04  0    0  0.000 0.000 
ANO_1 46.15 13.07 195  0  3.061 0.000 
ANO_1 13.07 9.43  444  0  3.268 0.000 
ANO_1 9.43  7.75  593  0  2.712 0.000 
ANO_1 7.75  6.74  713  0  1.923 0.000 
ANO_1 6.74  6.04  826  0  1.398 0.000 
ANO_1 6.04  5.52  918  0  1.124 0.000 
ANO_1 5.52  5.12  1008 0  0.903 0.000 
ANO_1 5.12  4.79  1048 0  0.741 0.000 
ANO_1 4.79  4.52  1138 0  0.607 0.000 
ANO_1 4.52  4.29  1192 0  0.485 0.000 
ANO_1 4.29  4.09  1267 0  0.389 0.000 
ANO_1 4.09  3.92  1132 0  0.285 0.000 
ANO_1 3.92  3.77  0    0  0.000 0.000 
ANO_1 3.77  3.63  0    0  0.000 0.000 
ANO_1 3.63  3.51  0    0  0.000 0.000 
ANO_1 3.51  3.40  0    0  0.000 0.000 
ANO_1 3.40  3.30  0    0  0.000 0.000 
ANO_1 3.30  3.20  0    0  0.000 0.000 
ANO_1 3.20  3.12  0    0  0.000 0.000 
ANO_1 3.12  3.04  0    0  0.000 0.000 
ISO_2 46.15 13.07 214  36 1.546 1.329 
ISO_2 13.07 9.43  487  58 1.638 1.171 
ISO_2 9.43  7.75  640  61 1.540 1.120 
ISO_2 7.75  6.74  757  64 1.246 0.883 
ISO_2 6.74  6.04  876  65 0.998 0.761 
ISO_2 6.04  5.52  974  62 0.791 0.573 
ISO_2 5.52  5.12  1061 66 0.673 0.517 
ISO_2 5.12  4.79  1102 73 0.562 0.407 
ISO_2 4.79  4.52  1192 70 0.431 0.373 
ISO_2 4.52  4.29  1244 72 0.342 0.288 
ISO_2 4.29  4.09  1332 68 0.259 0.201 
ISO_2 4.09  3.92  1202 55 0.205 0.191 
ISO_2 3.92  3.77  1    0  0.158 0.000 
ISO_2 3.77  3.63  0    0  0.000 0.000 
ISO_2 3.63  3.51  0    0  0.000 0.000 
ISO_2 3.51  3.40  0    0  0.000 0.000 
ISO_2 3.40  3.30  0    0  0.000 0.000 
ISO_2 3.30  3.20  0    0  0.000 0.000 
ISO_2 3.20  3.12  0    0  0.000 0.000 
ISO_2 3.12  3.04  0    0  0.000 0.000 
ANO_2 46.15 13.07 196  0  4.022 0.000 
ANO_2 13.07 9.43  465  0  4.363 0.000 
ANO_2 9.43  7.75  622  0  3.576 0.000 
ANO_2 7.75  6.74  733  0  2.618 0.000 
ANO_2 6.74  6.04  853  0  1.940 0.000 
ANO_2 6.04  5.52  946  0  1.469 0.000 
ANO_2 5.52  5.12  1028 0  1.123 0.000 
ANO_2 5.12  4.79  1089 0  0.927 0.000 
ANO_2 4.79  4.52  1170 0  0.744 0.000 
ANO_2 4.52  4.29  1230 0  0.545 0.000 
ANO_2 4.29  4.09  1292 0  0.414 0.000 
ANO_2 4.09  3.92  1341 0  0.305 0.000 
ANO_2 3.92  3.77  1441 0  0.222 0.000 
ANO_2 3.77  3.63  1510 0  0.172 0.000 
ANO_2 3.63  3.51  1231 0  0.150 0.000 
ANO_2 3.51  3.40  0    0  0.000 0.000 
ANO_2 3.40  3.30  0    0  0.000 0.000 
ANO_2 3.30  3.20  0    0  0.000 0.000 
ANO_2 3.20  3.12  0    0  0.000 0.000 
ANO_2 3.12  3.04  0    0  0.000 0.000 
ISO_3 46.15 13.07 215  37 2.569 2.158 
ISO_3 13.07 9.43  483  60 2.256 1.806 
ISO_3 9.43  7.75  638  62 2.473 1.891 
ISO_3 7.75  6.74  756  61 2.194 1.581 
ISO_3 6.74  6.04  874  66 1.855 1.388 
ISO_3 6.04  5.52  973  63 1.515 1.040 
ISO_3 5.52  5.12  1063 66 1.179 0.804 
ISO_3 5.12  4.79  1100 70 0.918 0.669 
ISO_3 4.79  4.52  1191 69 0.734 0.591 
ISO_3 4.52  4.29  1243 71 0.613 0.538 
ISO_3 4.29  4.09  1327 67 0.513 0.386 
ISO_3 4.09  3.92  1201 56 0.412 0.324 
ISO_3 3.92  3.77  1    0  0.328 0.000 
ISO_3 3.77  3.63  0    0  0.000 0.000 
ISO_3 3.63  3.51  0    0  0.000 0.000 
ISO_3 3.51  3.40  0    0  0.000 0.000 
ISO_3 3.40  3.30  0    0  0.000 0.000 
ISO_3 3.30  3.20  0    0  0.000 0.000 
ISO_3 3.20  3.12  0    0  0.000 0.000 
ISO_3 3.12  3.04  0    0  0.000 0.000 
ANO_3 46.15 13.07 204  0  2.723 0.000 
ANO_3 13.07 9.43  457  0  2.823 0.000 
ANO_3 9.43  7.75  614  0  2.936 0.000 
ANO_3 7.75  6.74  728  0  2.282 0.000 
ANO_3 6.74  6.04  840  0  1.721 0.000 
ANO_3 6.04  5.52  948  0  1.315 0.000 
ANO_3 5.52  5.12  1042 0  1.109 0.000 
ANO_3 5.12  4.79  1088 0  0.875 0.000 
ANO_3 4.79  4.52  1170 0  0.708 0.000 
ANO_3 4.52  4.29  1222 0  0.531 0.000 
ANO_3 4.29  4.09  1305 0  0.411 0.000 
ANO_3 4.09  3.92  1333 0  0.313 0.000 
ANO_3 3.92  3.77  1434 0  0.231 0.000 
ANO_3 3.77  3.63  1508 0  0.177 0.000 
ANO_3 3.63  3.51  1529 0  0.142 0.000 
ANO_3 3.51  3.40  1562 0  0.103 0.000 
ANO_3 3.40  3.30  1643 0  0.089 0.000 
ANO_3 3.30  3.20  1361 0  0.075 0.000 
ANO_3 3.20  3.12  0    0  0.000 0.000 
ANO_3 3.12  3.04  0    0  0.000 0.000 
ISO_4 46.15 13.07 213  39 3.118 2.606 
ISO_4 13.07 9.43  485  60 2.654 1.860 
ISO_4 9.43  7.75  638  63 2.485 1.973 
ISO_4 7.75  6.74  754  62 2.253 1.612 
ISO_4 6.74  6.04  873  64 1.933 1.517 
ISO_4 6.04  5.52  969  64 1.562 1.112 
ISO_4 5.52  5.12  1057 63 1.249 0.913 
ISO_4 5.12  4.79  1098 71 0.925 0.655 
ISO_4 4.79  4.52  1190 70 0.745 0.651 
ISO_4 4.52  4.29  1242 72 0.654 0.613 
ISO_4 4.29  4.09  1326 63 0.584 0.430 
ISO_4 4.09  3.92  1200 53 0.481 0.364 
ISO_4 3.92  3.77  2    0  0.480 0.000 
ISO_4 3.77  3.63  0    0  0.000 0.000 
ISO_4 3.63  3.51  0    0  0.000 0.000 
ISO_4 3.51  3.40  0    0  0.000 0.000 
ISO_4 3.40  3.30  0    0  0.000 0.000 
ISO_4 3.30  3.20  0    0  0.000 0.000 
ISO_4 3.20  3.12  0    0  0.000 0.000 
ISO_4 3.12  3.04  0    0  0.000 0.000 
ANO_4 46.15 13.07 188  0  1.656 0.000 
ANO_4 13.07 9.43  456  0  2.028 0.000 
ANO_4 9.43  7.75  607  0  2.037 0.000 
ANO_4 7.75  6.74  724  0  1.558 0.000 
ANO_4 6.74  6.04  828  0  1.167 0.000 
ANO_4 6.04  5.52  910  0  0.933 0.000 
ANO_4 5.52  5.12  1015 0  0.726 0.000 
ANO_4 5.12  4.79  1056 0  0.585 0.000 
ANO_4 4.79  4.52  1150 0  0.456 0.000 
ANO_4 4.52  4.29  1196 0  0.339 0.000 
ANO_4 4.29  4.09  1290 0  0.249 0.000 
ANO_4 4.09  3.92  1324 0  0.199 0.000 
ANO_4 3.92  3.77  1442 0  0.131 0.000 
ANO_4 3.77  3.63  1506 0  0.105 0.000 
ANO_4 3.63  3.51  1531 0  0.076 0.000 
ANO_4 3.51  3.40  1587 0  0.060 0.000 
ANO_4 3.40  3.30  1674 0  0.052 0.000 
ANO_4 3.30  3.20  1759 0  0.041 0.000 
ANO_4 3.20  3.12  1747 0  0.035 0.000 
ANO_4 3.12  3.04  1787 0  0.029 0.000 
# 
loop_
_pdbx_phasing_MAD_set_site.id 
_pdbx_phasing_MAD_set_site.atom_type_symbol 
_pdbx_phasing_MAD_set_site.Cartn_x 
_pdbx_phasing_MAD_set_site.Cartn_y 
_pdbx_phasing_MAD_set_site.Cartn_z 
_pdbx_phasing_MAD_set_site.occupancy 
_pdbx_phasing_MAD_set_site.b_iso 
1 SM 150.908 29.240 18.435 1.08 111.54 
2 SM 166.845 64.470 28.396 0.92 130.65 
3 SM 193.379 82.116 9.079  1.08 134.61 
4 SM 167.250 68.105 45.159 1.07 202.41 
# 
loop_
_pdbx_phasing_MAD_shell.d_res_low 
_pdbx_phasing_MAD_shell.d_res_high 
_pdbx_phasing_MAD_shell.reflns_acentric 
_pdbx_phasing_MAD_shell.fom_acentric 
_pdbx_phasing_MAD_shell.reflns_centric 
_pdbx_phasing_MAD_shell.fom_centric 
46.15 13.07 225  0.873 42 0.690 
13.07 9.43  490  0.836 69 0.543 
9.43  7.75  644  0.819 68 0.578 
7.75  6.74  758  0.773 67 0.528 
6.74  6.04  878  0.712 70 0.427 
6.04  5.52  975  0.655 71 0.349 
5.52  5.12  1065 0.579 68 0.266 
5.12  4.79  1109 0.497 73 0.201 
4.79  4.52  1203 0.440 71 0.167 
4.52  4.29  1255 0.368 74 0.151 
4.29  4.09  1334 0.302 70 0.098 
4.09  3.92  1374 0.255 74 0.103 
3.92  3.77  1485 0.176 75 0.067 
3.77  3.63  1556 0.141 73 0.070 
3.63  3.51  1583 0.099 77 0.046 
3.51  3.40  1620 0.064 71 0.032 
3.40  3.30  1708 0.052 72 0.031 
3.30  3.20  1787 0.034 71 0.029 
3.20  3.12  1779 0.015 75 0.006 
3.12  3.04  1819 0.013 75 0.005 
# 
_phasing.method   MAD 
# 
_phasing_MAD.entry_id               4LXS 
_phasing_MAD.pdbx_d_res_low         46.150 
_phasing_MAD.pdbx_d_res_high        3.040 
_phasing_MAD.pdbx_reflns_acentric   24647 
_phasing_MAD.pdbx_fom_acentric      0.277 
_phasing_MAD.pdbx_reflns_centric    1406 
_phasing_MAD.pdbx_fom_centric       0.204 
# 
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 XSCALE      .          ?                package 'Wolfgang Kabsch'     ?                               'data scaling'    
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/html_doc/xscale_program.html ?          ? 
2 SHARP       .          ?                package 'Eric de La Fortelle' sharp-develop@globalphasing.com phasing           
http://www.globalphasing.com/sharp/                                         ?          ? 
3 SOLOMON     .          ?                program 'Jan P. Abrahams'     ccp4@ccp4.ac.uk                 phasing           
http://www.ccp4.ac.uk/dist/html/solomon.html                                Fortran_77 ? 
4 PHENIX      1.8.2_1309 ?                package 'Paul D. Adams'       PDAdams@lbl.gov                 refinement        
http://www.phenix-online.org/                                               C++        ? 
5 PDB_EXTRACT 3.11       'April 22, 2011' package PDB                   deposit@deposit.rcsb.org        'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                   C++        ? 
6 MAR345      .          ?                ?       ?                     ?                               'data collection' ? ? ? 
7 XDS         .          ?                ?       ?                     ?                               'data reduction'  ? ? ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND2 A ASN 270 ? ? C2  A NAG 2015 ? ? 1.92 
2 1 OG  A SER 467 ? ? OD2 A ASP 491  ? ? 2.09 
3 1 SG  J CYS 10  ? ? CB  J CYS 68   ? ? 2.13 
4 1 OG  A SER 230 ? ? OD2 A ASP 254  ? ? 2.15 
5 1 NH2 A ARG 640 ? ? OD2 A ASP 643  ? ? 2.17 
6 1 OG  A SER 696 ? ? NE2 A HIS 698  ? ? 2.19 
# 
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 LEU A 42  ? ? -103.66 -85.59  
2  1 MET A 49  ? ? 49.61   -101.64 
3  1 GLU A 51  ? ? -107.16 -164.00 
4  1 LYS A 72  ? ? 65.48   -30.32  
5  1 ASP A 73  ? ? -90.32  -91.77  
6  1 VAL A 75  ? ? -161.25 118.43  
7  1 ASN A 80  ? ? -153.13 80.76   
8  1 THR A 82  ? ? -100.78 -67.51  
9  1 ARG A 95  ? ? 58.86   71.59   
10 1 SER A 126 ? ? 40.68   73.88   
11 1 MET A 139 ? ? -157.87 -154.72 
12 1 ARG A 148 ? ? 72.77   -1.97   
13 1 GLU A 187 ? ? -171.68 141.99  
14 1 PHE A 193 ? ? -81.52  45.57   
15 1 LEU A 196 ? ? -93.06  48.52   
16 1 ASN A 231 ? ? -119.07 -133.38 
17 1 GLN A 232 ? ? -141.63 16.43   
18 1 LEU A 233 ? ? -54.75  60.06   
19 1 HIS A 234 ? ? -58.46  -86.82  
20 1 LYS A 238 ? ? -34.49  -33.05  
21 1 ASN A 255 ? ? -143.23 27.75   
22 1 ILE A 257 ? ? -49.08  109.38  
23 1 HIS A 262 ? ? -67.35  10.35   
24 1 ALA A 278 ? ? 59.96   15.20   
25 1 ASN A 279 ? ? -89.40  -150.13 
26 1 ASN A 292 ? ? -114.55 72.73   
27 1 LYS A 293 ? ? -89.04  33.96   
28 1 GLU A 297 ? ? -175.20 114.06  
29 1 ARG A 313 ? ? 45.85   27.51   
30 1 GLN A 322 ? ? -120.40 -87.42  
31 1 THR A 342 ? ? -72.28  24.32   
32 1 ASN A 352 ? ? -107.36 -152.69 
33 1 SER A 370 ? ? -159.57 85.66   
34 1 ASN A 375 ? ? 58.50   74.25   
35 1 PRO A 382 ? ? -27.08  120.39  
36 1 PHE A 386 ? ? -93.10  35.61   
37 1 THR A 389 ? ? -65.97  58.70   
38 1 ASP A 399 ? ? 66.04   61.88   
39 1 LEU A 416 ? ? -47.03  109.59  
40 1 MET A 421 ? ? -140.79 27.71   
41 1 ASN A 424 ? ? -114.29 -152.39 
42 1 ARG A 441 ? ? -134.40 -32.94  
43 1 ASN A 448 ? ? -125.61 -164.09 
44 1 GLN A 453 ? ? 56.21   16.53   
45 1 LEU A 461 ? ? -95.41  31.54   
46 1 GLN A 462 ? ? 39.82   39.05   
47 1 ASN A 483 ? ? -104.56 -157.02 
48 1 PHE A 487 ? ? -175.70 136.69  
49 1 ASN A 507 ? ? -103.43 -147.52 
50 1 ALA A 518 ? ? -107.12 69.23   
51 1 GLN A 522 ? ? -85.34  34.42   
52 1 ARG A 524 ? ? 23.73   55.57   
53 1 ASN A 532 ? ? -99.64  -144.65 
54 1 ASP A 560 ? ? 58.92   74.01   
55 1 PRO A 562 ? ? -75.04  34.11   
56 1 CYS A 565 ? ? -106.32 55.77   
57 1 GLN A 583 ? ? 66.38   -78.85  
58 1 PRO A 607 ? ? -58.29  170.03  
59 1 LEU A 616 ? ? -69.58  87.52   
60 1 CYS A 650 ? ? -109.80 60.14   
61 1 HIS A 651 ? ? -95.10  44.17   
62 1 ASN A 654 ? ? -144.52 30.77   
63 1 ASN A 678 ? ? -112.99 -156.71 
64 1 LEU A 681 ? ? -131.92 -60.97  
65 1 ASN A 703 ? ? -118.40 77.69   
66 1 LEU A 719 ? ? -160.59 82.88   
67 1 ASN A 724 ? ? -129.84 -162.78 
68 1 ASP A 756 ? ? -133.35 -146.41 
69 1 ASN A 777 ? ? -59.37  -9.14   
70 1 LEU J 16  ? ? -160.09 76.53   
71 1 GLU J 48  ? ? -94.90  -73.17  
72 1 PRO J 96  ? ? -52.49  107.84  
73 1 SER K 4   ? ? -89.89  43.84   
74 1 ASN K 65  ? ? 36.53   72.55   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 37  ? A MET 10  
2   1 Y 1 A SER 38  ? A SER 11  
3   1 Y 1 A ILE 39  ? A ILE 12  
4   1 Y 1 A HIS 544 ? A HIS 517 
5   1 Y 1 A LEU 545 ? A LEU 518 
6   1 Y 1 A GLY 546 ? A GLY 519 
7   1 Y 1 A GLU 547 ? A GLU 520 
8   1 Y 1 A GLY 548 ? A GLY 521 
9   1 Y 1 A TYR 549 ? A TYR 522 
10  1 Y 1 A ASN 550 ? A ASN 523 
11  1 Y 1 A ASN 551 ? A ASN 524 
12  1 Y 1 A ASN 552 ? A ASN 525 
13  1 Y 1 A PHE 622 ? A PHE 595 
14  1 Y 1 A SER 623 ? A SER 596 
15  1 Y 1 A ASP 624 ? A ASP 597 
16  1 Y 1 A ASP 625 ? A ASP 598 
17  1 Y 1 A PRO 626 ? A PRO 599 
18  1 Y 1 A ARG 627 ? A ARG 600 
19  1 Y 1 A GLU 628 ? A GLU 601 
20  1 Y 1 A ARG 629 ? A ARG 602 
21  1 Y 1 A ARG 739 ? A ARG 712 
22  1 Y 1 A THR 740 ? A THR 713 
23  1 Y 1 A MET 741 ? A MET 714 
24  1 Y 1 A LYS 742 ? A LYS 715 
25  1 Y 1 A GLU 785 ? A GLU 758 
26  1 Y 1 A MET 786 ? A MET 759 
27  1 Y 1 A ALA 801 ? A ALA 774 
28  1 Y 1 A GLU 802 ? A GLU 775 
29  1 Y 1 A THR 803 ? A THR 776 
30  1 Y 1 A GLY 804 ? A GLY 777 
31  1 Y 1 A HIS 805 ? A HIS 778 
32  1 Y 1 A HIS 806 ? A HIS 779 
33  1 Y 1 A HIS 807 ? A HIS 780 
34  1 Y 1 A HIS 808 ? A HIS 781 
35  1 Y 1 A HIS 809 ? A HIS 782 
36  1 Y 1 A HIS 810 ? A HIS 783 
37  1 Y 1 J VAL 1   ? B VAL 1   
38  1 Y 1 J GLY 2   ? B GLY 2   
39  1 Y 1 J GLY 3   ? B GLY 3   
40  1 Y 1 J SER 4   ? B SER 4   
41  1 Y 1 J PRO 19  ? B PRO 19  
42  1 Y 1 J LYS 20  ? B LYS 20  
43  1 Y 1 J LYS 21  ? B LYS 21  
44  1 Y 1 J GLY 22  ? B GLY 22  
45  1 Y 1 J LEU 23  ? B LEU 23  
46  1 Y 1 J ARG 24  ? B ARG 24  
47  1 Y 1 J ALA 25  ? B ALA 25  
48  1 Y 1 J ASP 26  ? B ASP 26  
49  1 Y 1 J ASP 27  ? B ASP 27  
50  1 Y 1 J THR 28  ? B THR 28  
51  1 Y 1 J TRP 29  ? B TRP 29  
52  1 Y 1 J GLN 30  ? B GLN 30  
53  1 Y 1 J LEU 31  ? B LEU 31  
54  1 Y 1 J ILE 32  ? B ILE 32  
55  1 Y 1 J VAL 33  ? B VAL 33  
56  1 Y 1 J ASN 34  ? B ASN 34  
57  1 Y 1 J ASN 35  ? B ASN 35  
58  1 Y 1 J ASP 36  ? B ASP 36  
59  1 Y 1 J GLU 37  ? B GLU 37  
60  1 Y 1 J TYR 38  ? B TYR 38  
61  1 Y 1 J LYS 39  ? B LYS 39  
62  1 Y 1 J GLN 40  ? B GLN 40  
63  1 Y 1 J ALA 41  ? B ALA 41  
64  1 Y 1 J GLN 75  ? B GLN 75  
65  1 Y 1 J THR 76  ? B THR 76  
66  1 Y 1 J LEU 77  ? B LEU 77  
67  1 Y 1 J ALA 78  ? B ALA 78  
68  1 Y 1 J SER 79  ? B SER 79  
69  1 Y 1 J ILE 80  ? B ILE 80  
70  1 Y 1 J LYS 81  ? B LYS 81  
71  1 Y 1 J SER 82  ? B SER 82  
72  1 Y 1 J ASP 83  ? B ASP 83  
73  1 Y 1 J GLY 84  ? B GLY 84  
74  1 Y 1 J GLU 85  ? B GLU 85  
75  1 Y 1 J LEU 86  ? B LEU 86  
76  1 Y 1 J ASP 87  ? B ASP 87  
77  1 Y 1 J VAL 88  ? B VAL 88  
78  1 Y 1 J VAL 89  ? B VAL 89  
79  1 Y 1 J GLN 90  ? B GLN 90  
80  1 Y 1 J ASN 91  ? B ASN 91  
81  1 Y 1 J SER 92  ? B SER 92  
82  1 Y 1 J PHE 93  ? B PHE 93  
83  1 Y 1 J HIS 110 ? B HIS 110 
84  1 Y 1 J HIS 111 ? B HIS 111 
85  1 Y 1 J HIS 112 ? B HIS 112 
86  1 Y 1 J HIS 113 ? B HIS 113 
87  1 Y 1 J HIS 114 ? B HIS 114 
88  1 Y 1 K VAL 17  ? C VAL 17  
89  1 Y 1 K TYR 18  ? C TYR 18  
90  1 Y 1 K PRO 19  ? C PRO 19  
91  1 Y 1 K LYS 20  ? C LYS 20  
92  1 Y 1 K LYS 21  ? C LYS 21  
93  1 Y 1 K GLY 22  ? C GLY 22  
94  1 Y 1 K LEU 23  ? C LEU 23  
95  1 Y 1 K ARG 24  ? C ARG 24  
96  1 Y 1 K ALA 25  ? C ALA 25  
97  1 Y 1 K ASP 26  ? C ASP 26  
98  1 Y 1 K ASP 27  ? C ASP 27  
99  1 Y 1 K THR 28  ? C THR 28  
100 1 Y 1 K TRP 29  ? C TRP 29  
101 1 Y 1 K GLN 30  ? C GLN 30  
102 1 Y 1 K LEU 31  ? C LEU 31  
103 1 Y 1 K ILE 32  ? C ILE 32  
104 1 Y 1 K VAL 33  ? C VAL 33  
105 1 Y 1 K ASN 34  ? C ASN 34  
106 1 Y 1 K ASN 35  ? C ASN 35  
107 1 Y 1 K ASP 36  ? C ASP 36  
108 1 Y 1 K GLU 37  ? C GLU 37  
109 1 Y 1 K TYR 38  ? C TYR 38  
110 1 Y 1 K GLN 74  ? C GLN 74  
111 1 Y 1 K GLN 75  ? C GLN 75  
112 1 Y 1 K THR 76  ? C THR 76  
113 1 Y 1 K LEU 77  ? C LEU 77  
114 1 Y 1 K ALA 78  ? C ALA 78  
115 1 Y 1 K SER 79  ? C SER 79  
116 1 Y 1 K ILE 80  ? C ILE 80  
117 1 Y 1 K LYS 81  ? C LYS 81  
118 1 Y 1 K SER 82  ? C SER 82  
119 1 Y 1 K ASP 83  ? C ASP 83  
120 1 Y 1 K GLY 84  ? C GLY 84  
121 1 Y 1 K GLU 85  ? C GLU 85  
122 1 Y 1 K LEU 86  ? C LEU 86  
123 1 Y 1 K ASP 87  ? C ASP 87  
124 1 Y 1 K VAL 88  ? C VAL 88  
125 1 Y 1 K VAL 89  ? C VAL 89  
126 1 Y 1 K GLN 90  ? C GLN 90  
127 1 Y 1 K ASN 91  ? C ASN 91  
128 1 Y 1 K SER 92  ? C SER 92  
129 1 Y 1 K PHE 93  ? C PHE 93  
130 1 Y 1 K GLU 108 ? C GLU 108 
131 1 Y 1 K HIS 109 ? C HIS 109 
132 1 Y 1 K HIS 110 ? C HIS 110 
133 1 Y 1 K HIS 111 ? C HIS 111 
134 1 Y 1 K HIS 112 ? C HIS 112 
135 1 Y 1 K HIS 113 ? C HIS 113 
136 1 Y 1 K HIS 114 ? C HIS 114 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE                                NAG 
4 BETA-D-MANNOSE                                        BMA 
5 ALPHA-D-MANNOSE                                       MAN 
6 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
# 
